data_2H06
# 
_entry.id   2H06 
# 
_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   2H06         
RCSB  RCSB037764   
WWPDB D_1000037764 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 2H07 'the same protein(S132A)' unspecified 
PDB 2H08 'the same protein(Y146M)' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2H06 
_pdbx_database_status.recvd_initial_deposition_date   2006-05-14 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Li, S.'   1 
'Peng, B.' 2 
'Ding, J.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site' 
_citation.journal_abbrev            Biochem.J. 
_citation.journal_volume            401 
_citation.page_first                39 
_citation.page_last                 47 
_citation.year                      2007 
_citation.journal_id_ASTM           BIJOAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0264-6021 
_citation.journal_id_CSD            0043 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   16939420 
_citation.pdbx_database_id_DOI      10.1042/BJ20061066 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Li, S.'   1 
primary 'Lu, Y.'   2 
primary 'Peng, B.' 3 
primary 'Ding, J.' 4 
# 
_cell.entry_id           2H06 
_cell.length_a           169.683 
_cell.length_b           169.683 
_cell.length_c           61.598 
_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                         2H06 
_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 I' 35950.375 2   2.7.6.1 ? ? ? 
2 non-polymer syn 'SULFATE ION'                          96.063    6   ?       ? ? ? 
3 water       nat water                                  18.015    183 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Phosphoribosyl pyrophosphate synthetase I, PRS-I, PPRibP, PRPP synthetase 1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   ASN n 
1 4   ILE n 
1 5   LYS n 
1 6   ILE n 
1 7   PHE n 
1 8   SER n 
1 9   GLY n 
1 10  SER n 
1 11  SER n 
1 12  HIS n 
1 13  GLN n 
1 14  ASP n 
1 15  LEU n 
1 16  SER n 
1 17  GLN n 
1 18  LYS n 
1 19  ILE n 
1 20  ALA n 
1 21  ASP n 
1 22  ARG n 
1 23  LEU n 
1 24  GLY n 
1 25  LEU n 
1 26  GLU n 
1 27  LEU n 
1 28  GLY n 
1 29  LYS n 
1 30  VAL n 
1 31  VAL n 
1 32  THR n 
1 33  LYS n 
1 34  LYS n 
1 35  PHE n 
1 36  SER n 
1 37  ASN n 
1 38  GLN n 
1 39  GLU n 
1 40  THR n 
1 41  CYS n 
1 42  VAL n 
1 43  GLU n 
1 44  ILE n 
1 45  GLY n 
1 46  GLU n 
1 47  SER n 
1 48  VAL n 
1 49  ARG n 
1 50  GLY n 
1 51  GLU n 
1 52  ASP n 
1 53  VAL n 
1 54  TYR n 
1 55  ILE n 
1 56  VAL n 
1 57  GLN n 
1 58  SER n 
1 59  GLY n 
1 60  CYS n 
1 61  GLY n 
1 62  GLU n 
1 63  ILE n 
1 64  ASN n 
1 65  ASP n 
1 66  ASN n 
1 67  LEU n 
1 68  MET n 
1 69  GLU n 
1 70  LEU n 
1 71  LEU n 
1 72  ILE n 
1 73  MET n 
1 74  ILE n 
1 75  ASN n 
1 76  ALA n 
1 77  CYS n 
1 78  LYS n 
1 79  ILE n 
1 80  ALA n 
1 81  SER n 
1 82  ALA n 
1 83  SER n 
1 84  ARG n 
1 85  VAL n 
1 86  THR n 
1 87  ALA n 
1 88  VAL n 
1 89  ILE n 
1 90  PRO n 
1 91  CYS n 
1 92  PHE n 
1 93  PRO n 
1 94  TYR n 
1 95  ALA n 
1 96  ARG n 
1 97  GLN n 
1 98  ASP n 
1 99  LYS n 
1 100 LYS n 
1 101 ASP n 
1 102 LYS n 
1 103 SER n 
1 104 ARG n 
1 105 ALA n 
1 106 PRO n 
1 107 ILE n 
1 108 SER n 
1 109 ALA n 
1 110 LYS n 
1 111 LEU n 
1 112 VAL n 
1 113 ALA n 
1 114 ASN n 
1 115 MET n 
1 116 LEU n 
1 117 SER n 
1 118 VAL n 
1 119 ALA n 
1 120 GLY n 
1 121 ALA n 
1 122 ASP n 
1 123 HIS n 
1 124 ILE n 
1 125 ILE n 
1 126 THR n 
1 127 MET n 
1 128 ASP n 
1 129 LEU n 
1 130 HIS n 
1 131 ALA n 
1 132 SER n 
1 133 GLN n 
1 134 ILE n 
1 135 GLN n 
1 136 GLY n 
1 137 PHE n 
1 138 PHE n 
1 139 ASP n 
1 140 ILE n 
1 141 PRO n 
1 142 VAL n 
1 143 ASP n 
1 144 ASN n 
1 145 LEU n 
1 146 TYR n 
1 147 ALA n 
1 148 GLU n 
1 149 PRO n 
1 150 ALA n 
1 151 VAL n 
1 152 LEU n 
1 153 LYS n 
1 154 TRP n 
1 155 ILE n 
1 156 ARG n 
1 157 GLU n 
1 158 ASN n 
1 159 ILE n 
1 160 SER n 
1 161 GLU n 
1 162 TRP n 
1 163 ARG n 
1 164 ASN n 
1 165 CYS n 
1 166 THR n 
1 167 ILE n 
1 168 VAL n 
1 169 SER n 
1 170 PRO n 
1 171 ASP n 
1 172 ALA n 
1 173 GLY n 
1 174 GLY n 
1 175 ALA n 
1 176 LYS n 
1 177 ARG n 
1 178 VAL n 
1 179 THR n 
1 180 SER n 
1 181 ILE n 
1 182 ALA n 
1 183 ASP n 
1 184 ARG n 
1 185 LEU n 
1 186 ASN n 
1 187 VAL n 
1 188 ASP n 
1 189 PHE n 
1 190 ALA n 
1 191 LEU n 
1 192 ILE n 
1 193 HIS n 
1 194 LYS n 
1 195 GLU n 
1 196 ARG n 
1 197 LYS n 
1 198 LYS n 
1 199 ALA n 
1 200 ASN n 
1 201 GLU n 
1 202 VAL n 
1 203 ASP n 
1 204 ARG n 
1 205 MET n 
1 206 VAL n 
1 207 LEU n 
1 208 VAL n 
1 209 GLY n 
1 210 ASP n 
1 211 VAL n 
1 212 LYS n 
1 213 ASP n 
1 214 ARG n 
1 215 VAL n 
1 216 ALA n 
1 217 ILE n 
1 218 LEU n 
1 219 VAL n 
1 220 ASP n 
1 221 ASP n 
1 222 MET n 
1 223 ALA n 
1 224 ASP n 
1 225 THR n 
1 226 CYS n 
1 227 GLY n 
1 228 THR n 
1 229 ILE n 
1 230 CYS n 
1 231 HIS n 
1 232 ALA n 
1 233 ALA n 
1 234 ASP n 
1 235 LYS n 
1 236 LEU n 
1 237 LEU n 
1 238 SER n 
1 239 ALA n 
1 240 GLY n 
1 241 ALA n 
1 242 THR n 
1 243 ARG n 
1 244 VAL n 
1 245 TYR n 
1 246 ALA n 
1 247 ILE n 
1 248 LEU n 
1 249 THR n 
1 250 HIS n 
1 251 GLY n 
1 252 ILE n 
1 253 PHE n 
1 254 SER n 
1 255 GLY n 
1 256 PRO n 
1 257 ALA n 
1 258 ILE n 
1 259 SER n 
1 260 ARG n 
1 261 ILE n 
1 262 ASN n 
1 263 ASN n 
1 264 ALA n 
1 265 CYS n 
1 266 PHE n 
1 267 GLU n 
1 268 ALA n 
1 269 VAL n 
1 270 VAL n 
1 271 VAL n 
1 272 THR n 
1 273 ASN n 
1 274 THR n 
1 275 ILE n 
1 276 PRO n 
1 277 GLN n 
1 278 GLU n 
1 279 ASP n 
1 280 LYS n 
1 281 MET n 
1 282 LYS n 
1 283 HIS n 
1 284 CYS n 
1 285 SER n 
1 286 LYS n 
1 287 ILE n 
1 288 GLN n 
1 289 VAL n 
1 290 ILE n 
1 291 ASP n 
1 292 ILE n 
1 293 SER n 
1 294 MET n 
1 295 ILE n 
1 296 LEU n 
1 297 ALA n 
1 298 GLU n 
1 299 ALA n 
1 300 ILE n 
1 301 ARG n 
1 302 ARG n 
1 303 THR n 
1 304 HIS n 
1 305 ASN n 
1 306 GLY n 
1 307 GLU n 
1 308 SER n 
1 309 VAL n 
1 310 SER n 
1 311 TYR n 
1 312 LEU n 
1 313 PHE n 
1 314 SER n 
1 315 HIS n 
1 316 VAL n 
1 317 PRO n 
1 318 LEU n 
1 319 LEU n 
1 320 GLU n 
1 321 HIS n 
1 322 HIS n 
1 323 HIS n 
1 324 HIS n 
1 325 HIS n 
1 326 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   'Escherichia coli' 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL-21(DE3)' 
_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                       'pET-22b(+)' 
_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           0 
_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 2H06 A 1 ? 318 ? P60891 0 ? 317 ? 1 318 
2 1 2H06 B 1 ? 318 ? P60891 0 ? 317 ? 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 2H06 LEU A 319 ? UNP P60891 ? ? 'EXPRESSION TAG' 319 1  
1 2H06 GLU A 320 ? UNP P60891 ? ? 'EXPRESSION TAG' 320 2  
1 2H06 HIS A 321 ? UNP P60891 ? ? 'EXPRESSION TAG' 321 3  
1 2H06 HIS A 322 ? UNP P60891 ? ? 'EXPRESSION TAG' 322 4  
1 2H06 HIS A 323 ? UNP P60891 ? ? 'EXPRESSION TAG' 323 5  
1 2H06 HIS A 324 ? UNP P60891 ? ? 'EXPRESSION TAG' 324 6  
1 2H06 HIS A 325 ? UNP P60891 ? ? 'EXPRESSION TAG' 325 7  
1 2H06 HIS A 326 ? UNP P60891 ? ? 'EXPRESSION TAG' 326 8  
2 2H06 LEU B 319 ? UNP P60891 ? ? 'EXPRESSION TAG' 319 9  
2 2H06 GLU B 320 ? UNP P60891 ? ? 'EXPRESSION TAG' 320 10 
2 2H06 HIS B 321 ? UNP P60891 ? ? 'EXPRESSION TAG' 321 11 
2 2H06 HIS B 322 ? UNP P60891 ? ? 'EXPRESSION TAG' 322 12 
2 2H06 HIS B 323 ? UNP P60891 ? ? 'EXPRESSION TAG' 323 13 
2 2H06 HIS B 324 ? UNP P60891 ? ? 'EXPRESSION TAG' 324 14 
2 2H06 HIS B 325 ? UNP P60891 ? ? 'EXPRESSION TAG' 325 15 
2 2H06 HIS B 326 ? UNP P60891 ? ? 'EXPRESSION TAG' 326 16 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          2H06 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.37 
_exptl_crystal.density_percent_sol   48.16 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.15 
_exptl_crystal_grow.pdbx_details    
;0.1M citric acid, 1.3M ammonium sulfate, 0.02M sodium dihydrogen phosphate, 0.4M sodium chloride, pH 4.15, VAPOR DIFFUSION, HANGING DROP, temperature 293K
;
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2004-10-15 
_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   0.9780 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PHOTON FACTORY BEAMLINE BL-6A' 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
_diffrn_source.pdbx_synchrotron_beamline   BL-6A 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9780 
# 
_reflns.entry_id                     2H06 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             50.0 
_reflns.d_resolution_high            2.2 
_reflns.number_obs                   33517 
_reflns.number_all                   33560 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.074 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.8 
_reflns.B_iso_Wilson_estimate        26.2 
_reflns.pdbx_redundancy              3.2 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.20 
_reflns_shell.d_res_low              2.28 
_reflns_shell.percent_possible_all   99.9 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2H06 
_refine.ls_number_reflns_obs                     33517 
_refine.ls_number_reflns_all                     33560 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               2718982.29 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             48.98 
_refine.ls_d_res_high                            2.20 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_R_factor_obs                          0.212 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.212 
_refine.ls_R_factor_R_free                       0.245 
_refine.ls_R_factor_R_free_error                 0.006 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  1676 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               43.8 
_refine.aniso_B[1][1]                            3.86 
_refine.aniso_B[2][2]                            3.86 
_refine.aniso_B[3][3]                            -7.72 
_refine.aniso_B[1][2]                            4.97 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.386452 
_refine.solvent_model_param_bsol                 69.0654 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      1DKR 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        2H06 
_refine_analyze.Luzzati_coordinate_error_obs    0.27 
_refine_analyze.Luzzati_sigma_a_obs             0.29 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.32 
_refine_analyze.Luzzati_sigma_a_free            0.37 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4691 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             183 
_refine_hist.number_atoms_total               4904 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        48.98 
# 
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 
c_bond_d                0.007 ? ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             1.2   ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      23.6  ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      0.78  ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       2.20 
_refine_ls_shell.d_res_low                        2.34 
_refine_ls_shell.number_reflns_R_work             5266 
_refine_ls_shell.R_factor_R_work                  0.287 
_refine_ls_shell.percent_reflns_obs               99.8 
_refine_ls_shell.R_factor_R_free                  0.342 
_refine_ls_shell.R_factor_R_free_error            0.020 
_refine_ls_shell.percent_reflns_R_free            5.4 
_refine_ls_shell.number_reflns_R_free             303 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 protein_rep.param protein.top 'X-RAY DIFFRACTION' 
2 water.param       water.top   'X-RAY DIFFRACTION' 
3 ion.param         ion.top     'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2H06 
_struct.title                     'Crystal structure of human phosphoribosyl pyrophosphate synthetase 1' 
_struct.pdbx_descriptor           'Ribose-phosphate pyrophosphokinase I (E.C.2.7.6.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2H06 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'PRS1, prpp synthetase 1, phosphoribosyl pyrophosphate synthetase 1, 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 
# 
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  ? GLY A 24  ? GLN A 13  GLY A 24  1 ? 12 
HELX_P HELX_P2  2  GLU A 62  ? ILE A 79  ? GLU A 62  ILE A 79  1 ? 18 
HELX_P HELX_P3  3  ILE A 107 ? GLY A 120 ? ILE A 107 GLY A 120 1 ? 14 
HELX_P HELX_P4  4  ALA A 131 ? PHE A 138 ? ALA A 131 PHE A 138 5 ? 8  
HELX_P HELX_P5  5  ALA A 147 ? GLU A 157 ? ALA A 147 GLU A 157 1 ? 11 
HELX_P HELX_P6  6  GLU A 161 ? ASN A 164 ? GLU A 161 ASN A 164 5 ? 4  
HELX_P HELX_P7  7  ASP A 171 ? GLY A 173 ? ASP A 171 GLY A 173 5 ? 3  
HELX_P HELX_P8  8  GLY A 174 ? ASN A 186 ? GLY A 174 ASN A 186 1 ? 13 
HELX_P HELX_P9  9  CYS A 226 ? ALA A 239 ? CYS A 226 ALA A 239 1 ? 14 
HELX_P HELX_P10 10 PRO A 256 ? ALA A 264 ? PRO A 256 ALA A 264 1 ? 9  
HELX_P HELX_P11 11 GLN A 277 ? CYS A 284 ? GLN A 277 CYS A 284 1 ? 8  
HELX_P HELX_P12 12 ILE A 292 ? GLY A 306 ? ILE A 292 GLY A 306 1 ? 15 
HELX_P HELX_P13 13 VAL A 309 ? PHE A 313 ? VAL A 309 PHE A 313 5 ? 5  
HELX_P HELX_P14 14 HIS B 12  ? LEU B 23  ? HIS B 12  LEU B 23  1 ? 12 
HELX_P HELX_P15 15 GLU B 62  ? ALA B 80  ? GLU B 62  ALA B 80  1 ? 19 
HELX_P HELX_P16 16 ILE B 107 ? GLY B 120 ? ILE B 107 GLY B 120 1 ? 14 
HELX_P HELX_P17 17 ALA B 131 ? PHE B 138 ? ALA B 131 PHE B 138 5 ? 8  
HELX_P HELX_P18 18 ALA B 147 ? ILE B 159 ? ALA B 147 ILE B 159 1 ? 13 
HELX_P HELX_P19 19 GLU B 161 ? ASN B 164 ? GLU B 161 ASN B 164 5 ? 4  
HELX_P HELX_P20 20 ASP B 171 ? GLY B 173 ? ASP B 171 GLY B 173 5 ? 3  
HELX_P HELX_P21 21 GLY B 174 ? ASN B 186 ? GLY B 174 ASN B 186 1 ? 13 
HELX_P HELX_P22 22 CYS B 226 ? ALA B 239 ? CYS B 226 ALA B 239 1 ? 14 
HELX_P HELX_P23 23 PRO B 256 ? ALA B 264 ? PRO B 256 ALA B 264 1 ? 9  
HELX_P HELX_P24 24 GLN B 277 ? CYS B 284 ? GLN B 277 CYS B 284 1 ? 8  
HELX_P HELX_P25 25 ILE B 292 ? GLY B 306 ? ILE B 292 GLY B 306 1 ? 15 
HELX_P HELX_P26 26 VAL B 309 ? SER B 314 ? VAL B 309 SER B 314 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 2 ? 
C ? 7 ? 
D ? 5 ? 
E ? 2 ? 
F ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
C 6 7 ? parallel      
D 1 2 ? parallel      
D 2 3 ? parallel      
D 3 4 ? parallel      
D 4 5 ? parallel      
E 1 2 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? parallel      
F 3 4 ? parallel      
F 4 5 ? parallel      
F 5 6 ? parallel      
F 6 7 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ILE A 4   ? SER A 8   ? ILE A 4   SER A 8   
A 2 ASP A 52  ? VAL A 56  ? ASP A 52  VAL A 56  
A 3 ARG A 84  ? ILE A 89  ? ARG A 84  ILE A 89  
A 4 HIS A 123 ? MET A 127 ? HIS A 123 MET A 127 
A 5 VAL A 142 ? LEU A 145 ? VAL A 142 LEU A 145 
B 1 VAL A 30  ? LYS A 34  ? VAL A 30  LYS A 34  
B 2 THR A 40  ? ILE A 44  ? THR A 40  ILE A 44  
C 1 MET A 205 ? VAL A 208 ? MET A 205 VAL A 208 
C 2 ASP A 188 ? LYS A 194 ? ASP A 188 LYS A 194 
C 3 THR A 166 ? SER A 169 ? THR A 166 SER A 169 
C 4 ARG A 214 ? ALA A 223 ? ARG A 214 ALA A 223 
C 5 ALA A 241 ? GLY A 251 ? ALA A 241 GLY A 251 
C 6 PHE A 266 ? THR A 272 ? PHE A 266 THR A 272 
C 7 ILE A 287 ? ILE A 290 ? ILE A 287 ILE A 290 
D 1 ILE B 4   ? SER B 8   ? ILE B 4   SER B 8   
D 2 ASP B 52  ? VAL B 56  ? ASP B 52  VAL B 56  
D 3 ARG B 84  ? ILE B 89  ? ARG B 84  ILE B 89  
D 4 HIS B 123 ? MET B 127 ? HIS B 123 MET B 127 
D 5 VAL B 142 ? LEU B 145 ? VAL B 142 LEU B 145 
E 1 VAL B 30  ? LYS B 34  ? VAL B 30  LYS B 34  
E 2 THR B 40  ? ILE B 44  ? THR B 40  ILE B 44  
F 1 MET B 205 ? VAL B 208 ? MET B 205 VAL B 208 
F 2 ASP B 188 ? LYS B 194 ? ASP B 188 LYS B 194 
F 3 THR B 166 ? SER B 169 ? THR B 166 SER B 169 
F 4 VAL B 215 ? ALA B 223 ? VAL B 215 ALA B 223 
F 5 ARG B 243 ? GLY B 251 ? ARG B 243 GLY B 251 
F 6 PHE B 266 ? THR B 272 ? PHE B 266 THR B 272 
F 7 ILE B 287 ? ILE B 290 ? ILE B 287 ILE B 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 PHE A 7   ? N PHE A 7   O VAL A 56  ? O VAL A 56  
A 2 3 N VAL A 53  ? N VAL A 53  O THR A 86  ? O THR A 86  
A 3 4 N ILE A 89  ? N ILE A 89  O ILE A 125 ? O ILE A 125 
A 4 5 N THR A 126 ? N THR A 126 O LEU A 145 ? O LEU A 145 
B 1 2 N VAL A 31  ? N VAL A 31  O GLU A 43  ? O GLU A 43  
C 1 2 O VAL A 206 ? O VAL A 206 N HIS A 193 ? N HIS A 193 
C 2 3 O ASP A 188 ? O ASP A 188 N ILE A 167 ? N ILE A 167 
C 3 4 N THR A 166 ? N THR A 166 O ILE A 217 ? O ILE A 217 
C 4 5 N LEU A 218 ? N LEU A 218 O ILE A 247 ? O ILE A 247 
C 5 6 N LEU A 248 ? N LEU A 248 O VAL A 270 ? O VAL A 270 
C 6 7 N VAL A 271 ? N VAL A 271 O ILE A 290 ? O ILE A 290 
D 1 2 N PHE B 7   ? N PHE B 7   O TYR B 54  ? O TYR B 54  
D 2 3 N VAL B 53  ? N VAL B 53  O ARG B 84  ? O ARG B 84  
D 3 4 N ILE B 89  ? N ILE B 89  O ILE B 125 ? O ILE B 125 
D 4 5 N THR B 126 ? N THR B 126 O LEU B 145 ? O LEU B 145 
E 1 2 N VAL B 31  ? N VAL B 31  O GLU B 43  ? O GLU B 43  
F 1 2 O VAL B 206 ? O VAL B 206 N HIS B 193 ? N HIS B 193 
F 2 3 O ASP B 188 ? O ASP B 188 N ILE B 167 ? N ILE B 167 
F 3 4 N THR B 166 ? N THR B 166 O ILE B 217 ? O ILE B 217 
F 4 5 N LEU B 218 ? N LEU B 218 O TYR B 245 ? O TYR B 245 
F 5 6 N VAL B 244 ? N VAL B 244 O GLU B 267 ? O GLU B 267 
F 6 7 N VAL B 271 ? N VAL B 271 O ILE B 290 ? O ILE B 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 1001' 
AC2 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE SO4 A 1002' 
AC3 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 B 1003' 
AC4 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 A 1004' 
AC5 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SO4 B 1005' 
AC6 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE SO4 A 1006' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 7  ASP B 224 ? ASP B 224  . ? 1_555 ? 
2  AC1 7  THR B 225 ? THR B 225  . ? 1_555 ? 
3  AC1 7  CYS B 226 ? CYS B 226  . ? 1_555 ? 
4  AC1 7  GLY B 227 ? GLY B 227  . ? 1_555 ? 
5  AC1 7  THR B 228 ? THR B 228  . ? 1_555 ? 
6  AC1 7  HOH J .   ? HOH B 1113 . ? 1_555 ? 
7  AC1 7  HOH J .   ? HOH B 1116 . ? 1_555 ? 
8  AC2 7  ASP A 224 ? ASP A 224  . ? 1_555 ? 
9  AC2 7  THR A 225 ? THR A 225  . ? 1_555 ? 
10 AC2 7  CYS A 226 ? CYS A 226  . ? 1_555 ? 
11 AC2 7  GLY A 227 ? GLY A 227  . ? 1_555 ? 
12 AC2 7  THR A 228 ? THR A 228  . ? 1_555 ? 
13 AC2 7  HOH I .   ? HOH A 1076 . ? 1_555 ? 
14 AC2 7  HOH I .   ? HOH A 1077 . ? 1_555 ? 
15 AC3 8  ARG A 104 ? ARG A 104  . ? 1_555 ? 
16 AC3 8  SER B 47  ? SER B 47   . ? 2_455 ? 
17 AC3 8  ARG B 49  ? ARG B 49   . ? 2_455 ? 
18 AC3 8  SER B 308 ? SER B 308  . ? 1_555 ? 
19 AC3 8  VAL B 309 ? VAL B 309  . ? 1_555 ? 
20 AC3 8  SER B 310 ? SER B 310  . ? 1_555 ? 
21 AC3 8  HOH J .   ? HOH B 1007 . ? 2_455 ? 
22 AC3 8  HOH J .   ? HOH B 1114 . ? 1_555 ? 
23 AC4 8  SER A 47  ? SER A 47   . ? 3_445 ? 
24 AC4 8  ARG A 49  ? ARG A 49   . ? 3_445 ? 
25 AC4 8  SER A 308 ? SER A 308  . ? 1_555 ? 
26 AC4 8  VAL A 309 ? VAL A 309  . ? 1_555 ? 
27 AC4 8  SER A 310 ? SER A 310  . ? 1_555 ? 
28 AC4 8  HOH I .   ? HOH A 1040 . ? 1_555 ? 
29 AC4 8  HOH I .   ? HOH A 1056 . ? 3_445 ? 
30 AC4 8  ARG B 104 ? ARG B 104  . ? 1_555 ? 
31 AC5 10 LYS A 99  ? LYS A 99   . ? 1_555 ? 
32 AC5 10 LYS A 100 ? LYS A 100  . ? 1_555 ? 
33 AC5 10 ASP A 101 ? ASP A 101  . ? 1_555 ? 
34 AC5 10 LYS A 102 ? LYS A 102  . ? 1_555 ? 
35 AC5 10 SER B 132 ? SER B 132  . ? 1_555 ? 
36 AC5 10 GLN B 135 ? GLN B 135  . ? 1_555 ? 
37 AC5 10 ASN B 144 ? ASN B 144  . ? 1_555 ? 
38 AC5 10 TYR B 146 ? TYR B 146  . ? 1_555 ? 
39 AC5 10 HOH J .   ? HOH B 1066 . ? 1_555 ? 
40 AC5 10 HOH J .   ? HOH B 1115 . ? 1_555 ? 
41 AC6 9  SER A 132 ? SER A 132  . ? 1_555 ? 
42 AC6 9  GLN A 135 ? GLN A 135  . ? 1_555 ? 
43 AC6 9  ASN A 144 ? ASN A 144  . ? 1_555 ? 
44 AC6 9  TYR A 146 ? TYR A 146  . ? 1_555 ? 
45 AC6 9  HOH I .   ? HOH A 1008 . ? 1_555 ? 
46 AC6 9  LYS B 99  ? LYS B 99   . ? 1_555 ? 
47 AC6 9  LYS B 100 ? LYS B 100  . ? 1_555 ? 
48 AC6 9  ASP B 101 ? ASP B 101  . ? 1_555 ? 
49 AC6 9  LYS B 102 ? LYS B 102  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2H06 
_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                    2H06 
_atom_sites.fract_transf_matrix[1][1]   0.005893 
_atom_sites.fract_transf_matrix[1][2]   0.003403 
_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]   0.006805 
_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]   0.016234 
_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   ? -96.259  -53.155 23.727 1.00 52.10 ? 3    ASN A N   1 
ATOM   2    C CA  . ASN A 1 3   ? -95.383  -52.680 24.841 1.00 51.63 ? 3    ASN A CA  1 
ATOM   3    C C   . ASN A 1 3   ? -96.243  -52.121 25.967 1.00 50.09 ? 3    ASN A C   1 
ATOM   4    O O   . ASN A 1 3   ? -95.958  -52.343 27.142 1.00 50.17 ? 3    ASN A O   1 
ATOM   5    C CB  . ASN A 1 3   ? -94.417  -51.610 24.325 1.00 54.67 ? 3    ASN A CB  1 
ATOM   6    C CG  . ASN A 1 3   ? -93.371  -51.215 25.349 1.00 55.95 ? 3    ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 3   ? -92.744  -52.066 25.979 1.00 58.99 ? 3    ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 3   ? -93.162  -49.915 25.504 1.00 56.51 ? 3    ASN A ND2 1 
ATOM   9    N N   . ILE A 1 4   ? -97.303  -51.403 25.614 1.00 46.27 ? 4    ILE A N   1 
ATOM   10   C CA  . ILE A 1 4   ? -98.190  -50.857 26.631 1.00 44.93 ? 4    ILE A CA  1 
ATOM   11   C C   . ILE A 1 4   ? -99.395  -51.766 26.894 1.00 43.48 ? 4    ILE A C   1 
ATOM   12   O O   . ILE A 1 4   ? -100.002 -52.303 25.966 1.00 43.54 ? 4    ILE A O   1 
ATOM   13   C CB  . ILE A 1 4   ? -98.702  -49.456 26.250 1.00 45.23 ? 4    ILE A CB  1 
ATOM   14   C CG1 . ILE A 1 4   ? -99.767  -49.011 27.249 1.00 43.61 ? 4    ILE A CG1 1 
ATOM   15   C CG2 . ILE A 1 4   ? -99.257  -49.467 24.837 1.00 47.87 ? 4    ILE A CG2 1 
ATOM   16   C CD1 . ILE A 1 4   ? -100.104 -47.547 27.164 1.00 46.29 ? 4    ILE A CD1 1 
ATOM   17   N N   . LYS A 1 5   ? -99.726  -51.931 28.172 1.00 40.69 ? 5    LYS A N   1 
ATOM   18   C CA  . LYS A 1 5   ? -100.849 -52.754 28.586 1.00 38.26 ? 5    LYS A CA  1 
ATOM   19   C C   . LYS A 1 5   ? -101.677 -52.054 29.650 1.00 37.16 ? 5    LYS A C   1 
ATOM   20   O O   . LYS A 1 5   ? -101.138 -51.490 30.594 1.00 39.15 ? 5    LYS A O   1 
ATOM   21   C CB  . LYS A 1 5   ? -100.348 -54.102 29.109 1.00 39.42 ? 5    LYS A CB  1 
ATOM   22   C CG  . LYS A 1 5   ? -100.430 -55.216 28.078 1.00 43.46 ? 5    LYS A CG  1 
ATOM   23   C CD  . LYS A 1 5   ? -101.891 -55.548 27.781 1.00 45.61 ? 5    LYS A CD  1 
ATOM   24   C CE  . LYS A 1 5   ? -102.028 -56.614 26.713 1.00 48.25 ? 5    LYS A CE  1 
ATOM   25   N NZ  . LYS A 1 5   ? -103.452 -57.039 26.528 1.00 49.04 ? 5    LYS A NZ  1 
ATOM   26   N N   . ILE A 1 6   ? -102.993 -52.084 29.483 1.00 35.90 ? 6    ILE A N   1 
ATOM   27   C CA  . ILE A 1 6   ? -103.898 -51.457 30.428 1.00 35.98 ? 6    ILE A CA  1 
ATOM   28   C C   . ILE A 1 6   ? -104.832 -52.488 31.037 1.00 35.49 ? 6    ILE A C   1 
ATOM   29   O O   . ILE A 1 6   ? -105.505 -53.228 30.316 1.00 33.37 ? 6    ILE A O   1 
ATOM   30   C CB  . ILE A 1 6   ? -104.780 -50.373 29.759 1.00 37.72 ? 6    ILE A CB  1 
ATOM   31   C CG1 . ILE A 1 6   ? -103.910 -49.232 29.234 1.00 39.62 ? 6    ILE A CG1 1 
ATOM   32   C CG2 . ILE A 1 6   ? -105.785 -49.834 30.767 1.00 36.09 ? 6    ILE A CG2 1 
ATOM   33   C CD1 . ILE A 1 6   ? -104.703 -48.074 28.669 1.00 40.05 ? 6    ILE A CD1 1 
ATOM   34   N N   . PHE A 1 7   ? -104.862 -52.525 32.366 1.00 33.81 ? 7    PHE A N   1 
ATOM   35   C CA  . PHE A 1 7   ? -105.728 -53.438 33.104 1.00 33.65 ? 7    PHE A CA  1 
ATOM   36   C C   . PHE A 1 7   ? -106.692 -52.619 33.967 1.00 35.60 ? 7    PHE A C   1 
ATOM   37   O O   . PHE A 1 7   ? -106.398 -51.484 34.351 1.00 34.04 ? 7    PHE A O   1 
ATOM   38   C CB  . PHE A 1 7   ? -104.919 -54.357 34.030 1.00 29.88 ? 7    PHE A CB  1 
ATOM   39   C CG  . PHE A 1 7   ? -104.049 -55.351 33.317 1.00 31.10 ? 7    PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 7   ? -102.750 -55.023 32.947 1.00 30.45 ? 7    PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 7   ? -104.518 -56.633 33.046 1.00 28.36 ? 7    PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 7   ? -101.932 -55.959 32.325 1.00 30.04 ? 7    PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 7   ? -103.711 -57.572 32.426 1.00 26.78 ? 7    PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 7   ? -102.416 -57.239 32.064 1.00 29.57 ? 7    PHE A CZ  1 
ATOM   45   N N   . SER A 1 8   ? -107.837 -53.203 34.285 1.00 38.79 ? 8    SER A N   1 
ATOM   46   C CA  . SER A 1 8   ? -108.817 -52.525 35.114 1.00 44.52 ? 8    SER A CA  1 
ATOM   47   C C   . SER A 1 8   ? -109.068 -53.299 36.391 1.00 49.32 ? 8    SER A C   1 
ATOM   48   O O   . SER A 1 8   ? -108.890 -54.514 36.438 1.00 48.80 ? 8    SER A O   1 
ATOM   49   C CB  . SER A 1 8   ? -110.134 -52.373 34.364 1.00 45.61 ? 8    SER A CB  1 
ATOM   50   O OG  . SER A 1 8   ? -111.137 -51.871 35.223 1.00 46.64 ? 8    SER A OG  1 
ATOM   51   N N   . GLY A 1 9   ? -109.482 -52.583 37.430 1.00 56.61 ? 9    GLY A N   1 
ATOM   52   C CA  . GLY A 1 9   ? -109.791 -53.221 38.695 1.00 62.96 ? 9    GLY A CA  1 
ATOM   53   C C   . GLY A 1 9   ? -111.287 -53.466 38.806 1.00 68.64 ? 9    GLY A C   1 
ATOM   54   O O   . GLY A 1 9   ? -112.084 -52.802 38.143 1.00 69.75 ? 9    GLY A O   1 
ATOM   55   N N   . SER A 1 10  ? -111.666 -54.436 39.630 1.00 74.37 ? 10   SER A N   1 
ATOM   56   C CA  . SER A 1 10  ? -113.067 -54.783 39.863 1.00 79.21 ? 10   SER A CA  1 
ATOM   57   C C   . SER A 1 10  ? -113.916 -54.880 38.605 1.00 81.64 ? 10   SER A C   1 
ATOM   58   O O   . SER A 1 10  ? -113.412 -54.835 37.481 1.00 83.28 ? 10   SER A O   1 
ATOM   59   C CB  . SER A 1 10  ? -113.719 -53.751 40.769 1.00 80.35 ? 10   SER A CB  1 
ATOM   60   O OG  . SER A 1 10  ? -114.109 -52.627 39.995 1.00 81.35 ? 10   SER A OG  1 
ATOM   61   N N   . SER A 1 11  ? -115.223 -55.000 38.823 1.00 84.13 ? 11   SER A N   1 
ATOM   62   C CA  . SER A 1 11  ? -116.185 -55.090 37.736 1.00 86.65 ? 11   SER A CA  1 
ATOM   63   C C   . SER A 1 11  ? -116.216 -53.748 37.025 1.00 86.67 ? 11   SER A C   1 
ATOM   64   O O   . SER A 1 11  ? -116.587 -53.666 35.854 1.00 87.45 ? 11   SER A O   1 
ATOM   65   C CB  . SER A 1 11  ? -117.577 -55.423 38.280 1.00 88.50 ? 11   SER A CB  1 
ATOM   66   O OG  . SER A 1 11  ? -118.523 -55.533 37.228 1.00 90.33 ? 11   SER A OG  1 
ATOM   67   N N   . HIS A 1 12  ? -115.835 -52.693 37.742 1.00 86.17 ? 12   HIS A N   1 
ATOM   68   C CA  . HIS A 1 12  ? -115.798 -51.362 37.149 1.00 85.74 ? 12   HIS A CA  1 
ATOM   69   C C   . HIS A 1 12  ? -114.901 -51.413 35.926 1.00 83.46 ? 12   HIS A C   1 
ATOM   70   O O   . HIS A 1 12  ? -113.735 -51.801 36.018 1.00 84.26 ? 12   HIS A O   1 
ATOM   71   C CB  . HIS A 1 12  ? -115.225 -50.333 38.127 1.00 87.77 ? 12   HIS A CB  1 
ATOM   72   C CG  . HIS A 1 12  ? -114.659 -49.115 37.458 1.00 89.44 ? 12   HIS A CG  1 
ATOM   73   N ND1 . HIS A 1 12  ? -113.646 -49.181 36.524 1.00 89.73 ? 12   HIS A ND1 1 
ATOM   74   C CD2 . HIS A 1 12  ? -114.959 -47.802 37.589 1.00 90.81 ? 12   HIS A CD2 1 
ATOM   75   C CE1 . HIS A 1 12  ? -113.349 -47.964 36.109 1.00 90.11 ? 12   HIS A CE1 1 
ATOM   76   N NE2 . HIS A 1 12  ? -114.131 -47.107 36.740 1.00 90.74 ? 12   HIS A NE2 1 
ATOM   77   N N   . GLN A 1 13  ? -115.441 -51.024 34.782 1.00 79.28 ? 13   GLN A N   1 
ATOM   78   C CA  . GLN A 1 13  ? -114.657 -51.017 33.564 1.00 74.75 ? 13   GLN A CA  1 
ATOM   79   C C   . GLN A 1 13  ? -115.120 -49.899 32.667 1.00 70.21 ? 13   GLN A C   1 
ATOM   80   O O   . GLN A 1 13  ? -114.555 -49.677 31.602 1.00 71.38 ? 13   GLN A O   1 
ATOM   81   C CB  . GLN A 1 13  ? -114.765 -52.359 32.833 1.00 76.33 ? 13   GLN A CB  1 
ATOM   82   C CG  . GLN A 1 13  ? -113.993 -53.483 33.509 1.00 78.28 ? 13   GLN A CG  1 
ATOM   83   C CD  . GLN A 1 13  ? -113.678 -54.633 32.571 1.00 79.56 ? 13   GLN A CD  1 
ATOM   84   O OE1 . GLN A 1 13  ? -112.969 -55.570 32.939 1.00 80.64 ? 13   GLN A OE1 1 
ATOM   85   N NE2 . GLN A 1 13  ? -114.204 -54.567 31.352 1.00 80.68 ? 13   GLN A NE2 1 
ATOM   86   N N   . ASP A 1 14  ? -116.144 -49.181 33.102 1.00 63.94 ? 14   ASP A N   1 
ATOM   87   C CA  . ASP A 1 14  ? -116.658 -48.088 32.300 1.00 59.09 ? 14   ASP A CA  1 
ATOM   88   C C   . ASP A 1 14  ? -115.533 -47.106 31.989 1.00 55.41 ? 14   ASP A C   1 
ATOM   89   O O   . ASP A 1 14  ? -115.225 -46.861 30.824 1.00 56.06 ? 14   ASP A O   1 
ATOM   90   C CB  . ASP A 1 14  ? -117.796 -47.379 33.029 1.00 60.32 ? 14   ASP A CB  1 
ATOM   91   C CG  . ASP A 1 14  ? -118.565 -46.443 32.126 1.00 61.69 ? 14   ASP A CG  1 
ATOM   92   O OD1 . ASP A 1 14  ? -117.948 -45.518 31.556 1.00 61.36 ? 14   ASP A OD1 1 
ATOM   93   O OD2 . ASP A 1 14  ? -119.790 -46.636 31.983 1.00 65.09 ? 14   ASP A OD2 1 
ATOM   94   N N   . LEU A 1 15  ? -114.912 -46.556 33.028 1.00 50.19 ? 15   LEU A N   1 
ATOM   95   C CA  . LEU A 1 15  ? -113.822 -45.610 32.836 1.00 45.11 ? 15   LEU A CA  1 
ATOM   96   C C   . LEU A 1 15  ? -112.659 -46.318 32.148 1.00 43.72 ? 15   LEU A C   1 
ATOM   97   O O   . LEU A 1 15  ? -112.095 -45.803 31.187 1.00 43.78 ? 15   LEU A O   1 
ATOM   98   C CB  . LEU A 1 15  ? -113.352 -45.041 34.178 1.00 42.54 ? 15   LEU A CB  1 
ATOM   99   C CG  . LEU A 1 15  ? -112.761 -43.626 34.173 1.00 40.93 ? 15   LEU A CG  1 
ATOM   100  C CD1 . LEU A 1 15  ? -112.054 -43.373 35.488 1.00 41.56 ? 15   LEU A CD1 1 
ATOM   101  C CD2 . LEU A 1 15  ? -111.791 -43.455 33.024 1.00 41.06 ? 15   LEU A CD2 1 
ATOM   102  N N   . SER A 1 16  ? -112.304 -47.500 32.643 1.00 42.87 ? 16   SER A N   1 
ATOM   103  C CA  . SER A 1 16  ? -111.207 -48.276 32.073 1.00 42.10 ? 16   SER A CA  1 
ATOM   104  C C   . SER A 1 16  ? -111.397 -48.548 30.589 1.00 40.98 ? 16   SER A C   1 
ATOM   105  O O   . SER A 1 16  ? -110.464 -48.410 29.805 1.00 40.80 ? 16   SER A O   1 
ATOM   106  C CB  . SER A 1 16  ? -111.061 -49.611 32.798 1.00 41.73 ? 16   SER A CB  1 
ATOM   107  O OG  . SER A 1 16  ? -110.569 -49.421 34.107 1.00 49.18 ? 16   SER A OG  1 
ATOM   108  N N   . GLN A 1 17  ? -112.606 -48.944 30.213 1.00 40.99 ? 17   GLN A N   1 
ATOM   109  C CA  . GLN A 1 17  ? -112.910 -49.243 28.821 1.00 42.45 ? 17   GLN A CA  1 
ATOM   110  C C   . GLN A 1 17  ? -112.811 -47.984 27.972 1.00 42.06 ? 17   GLN A C   1 
ATOM   111  O O   . GLN A 1 17  ? -112.309 -48.024 26.852 1.00 41.95 ? 17   GLN A O   1 
ATOM   112  C CB  . GLN A 1 17  ? -114.311 -49.844 28.696 1.00 44.88 ? 17   GLN A CB  1 
ATOM   113  C CG  . GLN A 1 17  ? -114.567 -50.472 27.347 1.00 47.04 ? 17   GLN A CG  1 
ATOM   114  C CD  . GLN A 1 17  ? -113.553 -51.548 27.025 1.00 49.51 ? 17   GLN A CD  1 
ATOM   115  O OE1 . GLN A 1 17  ? -113.506 -52.589 27.684 1.00 49.90 ? 17   GLN A OE1 1 
ATOM   116  N NE2 . GLN A 1 17  ? -112.727 -51.300 26.011 1.00 50.06 ? 17   GLN A NE2 1 
ATOM   117  N N   . LYS A 1 18  ? -113.287 -46.863 28.503 1.00 40.54 ? 18   LYS A N   1 
ATOM   118  C CA  . LYS A 1 18  ? -113.208 -45.615 27.764 1.00 39.81 ? 18   LYS A CA  1 
ATOM   119  C C   . LYS A 1 18  ? -111.751 -45.302 27.477 1.00 38.51 ? 18   LYS A C   1 
ATOM   120  O O   . LYS A 1 18  ? -111.395 -44.902 26.371 1.00 39.44 ? 18   LYS A O   1 
ATOM   121  C CB  . LYS A 1 18  ? -113.825 -44.466 28.561 1.00 39.96 ? 18   LYS A CB  1 
ATOM   122  C CG  . LYS A 1 18  ? -115.339 -44.390 28.497 1.00 40.85 ? 18   LYS A CG  1 
ATOM   123  C CD  . LYS A 1 18  ? -115.840 -43.159 29.241 1.00 43.03 ? 18   LYS A CD  1 
ATOM   124  C CE  . LYS A 1 18  ? -117.320 -42.933 29.016 1.00 45.57 ? 18   LYS A CE  1 
ATOM   125  N NZ  . LYS A 1 18  ? -118.121 -44.130 29.404 1.00 49.16 ? 18   LYS A NZ  1 
ATOM   126  N N   . ILE A 1 19  ? -110.903 -45.498 28.478 1.00 37.30 ? 19   ILE A N   1 
ATOM   127  C CA  . ILE A 1 19  ? -109.481 -45.216 28.328 1.00 35.84 ? 19   ILE A CA  1 
ATOM   128  C C   . ILE A 1 19  ? -108.811 -46.118 27.302 1.00 34.94 ? 19   ILE A C   1 
ATOM   129  O O   . ILE A 1 19  ? -108.087 -45.638 26.434 1.00 35.20 ? 19   ILE A O   1 
ATOM   130  C CB  . ILE A 1 19  ? -108.750 -45.333 29.687 1.00 36.10 ? 19   ILE A CB  1 
ATOM   131  C CG1 . ILE A 1 19  ? -109.263 -44.233 30.627 1.00 36.08 ? 19   ILE A CG1 1 
ATOM   132  C CG2 . ILE A 1 19  ? -107.240 -45.203 29.494 1.00 34.82 ? 19   ILE A CG2 1 
ATOM   133  C CD1 . ILE A 1 19  ? -108.697 -44.293 32.027 1.00 36.83 ? 19   ILE A CD1 1 
ATOM   134  N N   . ALA A 1 20  ? -109.053 -47.420 27.392 1.00 34.55 ? 20   ALA A N   1 
ATOM   135  C CA  . ALA A 1 20  ? -108.450 -48.348 26.451 1.00 35.27 ? 20   ALA A CA  1 
ATOM   136  C C   . ALA A 1 20  ? -108.891 -48.008 25.027 1.00 35.72 ? 20   ALA A C   1 
ATOM   137  O O   . ALA A 1 20  ? -108.082 -48.017 24.105 1.00 36.71 ? 20   ALA A O   1 
ATOM   138  C CB  . ALA A 1 20  ? -108.826 -49.782 26.808 1.00 34.43 ? 20   ALA A CB  1 
ATOM   139  N N   . ASP A 1 21  ? -110.171 -47.694 24.848 1.00 38.29 ? 21   ASP A N   1 
ATOM   140  C CA  . ASP A 1 21  ? -110.678 -47.341 23.522 1.00 40.19 ? 21   ASP A CA  1 
ATOM   141  C C   . ASP A 1 21  ? -109.930 -46.149 22.944 1.00 40.16 ? 21   ASP A C   1 
ATOM   142  O O   . ASP A 1 21  ? -109.443 -46.203 21.815 1.00 40.39 ? 21   ASP A O   1 
ATOM   143  C CB  . ASP A 1 21  ? -112.166 -46.996 23.570 1.00 42.01 ? 21   ASP A CB  1 
ATOM   144  C CG  . ASP A 1 21  ? -113.025 -48.175 23.952 1.00 44.89 ? 21   ASP A CG  1 
ATOM   145  O OD1 . ASP A 1 21  ? -112.595 -49.327 23.734 1.00 46.70 ? 21   ASP A OD1 1 
ATOM   146  O OD2 . ASP A 1 21  ? -114.143 -47.946 24.461 1.00 49.24 ? 21   ASP A OD2 1 
ATOM   147  N N   . ARG A 1 22  ? -109.839 -45.072 23.718 1.00 38.33 ? 22   ARG A N   1 
ATOM   148  C CA  . ARG A 1 22  ? -109.149 -43.876 23.248 1.00 40.91 ? 22   ARG A CA  1 
ATOM   149  C C   . ARG A 1 22  ? -107.709 -44.149 22.836 1.00 40.10 ? 22   ARG A C   1 
ATOM   150  O O   . ARG A 1 22  ? -107.136 -43.425 22.026 1.00 41.29 ? 22   ARG A O   1 
ATOM   151  C CB  . ARG A 1 22  ? -109.171 -42.783 24.321 1.00 39.90 ? 22   ARG A CB  1 
ATOM   152  C CG  . ARG A 1 22  ? -110.534 -42.148 24.530 1.00 41.64 ? 22   ARG A CG  1 
ATOM   153  C CD  . ARG A 1 22  ? -110.456 -41.008 25.526 1.00 43.47 ? 22   ARG A CD  1 
ATOM   154  N NE  . ARG A 1 22  ? -111.755 -40.377 25.766 1.00 46.45 ? 22   ARG A NE  1 
ATOM   155  C CZ  . ARG A 1 22  ? -112.482 -39.766 24.832 1.00 48.44 ? 22   ARG A CZ  1 
ATOM   156  N NH1 . ARG A 1 22  ? -112.046 -39.700 23.575 1.00 47.38 ? 22   ARG A NH1 1 
ATOM   157  N NH2 . ARG A 1 22  ? -113.643 -39.208 25.155 1.00 47.55 ? 22   ARG A NH2 1 
ATOM   158  N N   . LEU A 1 23  ? -107.124 -45.197 23.397 1.00 39.97 ? 23   LEU A N   1 
ATOM   159  C CA  . LEU A 1 23  ? -105.749 -45.541 23.087 1.00 39.32 ? 23   LEU A CA  1 
ATOM   160  C C   . LEU A 1 23  ? -105.659 -46.618 22.005 1.00 38.28 ? 23   LEU A C   1 
ATOM   161  O O   . LEU A 1 23  ? -104.564 -46.971 21.574 1.00 38.95 ? 23   LEU A O   1 
ATOM   162  C CB  . LEU A 1 23  ? -105.032 -45.997 24.367 1.00 40.58 ? 23   LEU A CB  1 
ATOM   163  C CG  . LEU A 1 23  ? -104.954 -44.944 25.486 1.00 41.81 ? 23   LEU A CG  1 
ATOM   164  C CD1 . LEU A 1 23  ? -104.307 -45.539 26.717 1.00 41.03 ? 23   LEU A CD1 1 
ATOM   165  C CD2 . LEU A 1 23  ? -104.160 -43.736 25.009 1.00 41.05 ? 23   LEU A CD2 1 
ATOM   166  N N   . GLY A 1 24  ? -106.812 -47.124 21.567 1.00 37.19 ? 24   GLY A N   1 
ATOM   167  C CA  . GLY A 1 24  ? -106.839 -48.154 20.536 1.00 35.49 ? 24   GLY A CA  1 
ATOM   168  C C   . GLY A 1 24  ? -106.386 -49.497 21.078 1.00 35.66 ? 24   GLY A C   1 
ATOM   169  O O   . GLY A 1 24  ? -105.736 -50.281 20.389 1.00 35.06 ? 24   GLY A O   1 
ATOM   170  N N   . LEU A 1 25  ? -106.737 -49.763 22.329 1.00 35.63 ? 25   LEU A N   1 
ATOM   171  C CA  . LEU A 1 25  ? -106.351 -51.004 22.985 1.00 34.20 ? 25   LEU A CA  1 
ATOM   172  C C   . LEU A 1 25  ? -107.535 -51.686 23.662 1.00 33.98 ? 25   LEU A C   1 
ATOM   173  O O   . LEU A 1 25  ? -108.580 -51.072 23.903 1.00 31.45 ? 25   LEU A O   1 
ATOM   174  C CB  . LEU A 1 25  ? -105.303 -50.718 24.062 1.00 35.28 ? 25   LEU A CB  1 
ATOM   175  C CG  . LEU A 1 25  ? -104.024 -49.967 23.700 1.00 37.62 ? 25   LEU A CG  1 
ATOM   176  C CD1 . LEU A 1 25  ? -103.280 -49.629 24.986 1.00 38.39 ? 25   LEU A CD1 1 
ATOM   177  C CD2 . LEU A 1 25  ? -103.155 -50.809 22.766 1.00 34.85 ? 25   LEU A CD2 1 
ATOM   178  N N   . GLU A 1 26  ? -107.356 -52.966 23.964 1.00 32.59 ? 26   GLU A N   1 
ATOM   179  C CA  . GLU A 1 26  ? -108.355 -53.724 24.689 1.00 33.40 ? 26   GLU A CA  1 
ATOM   180  C C   . GLU A 1 26  ? -107.761 -53.858 26.091 1.00 33.23 ? 26   GLU A C   1 
ATOM   181  O O   . GLU A 1 26  ? -106.534 -53.845 26.261 1.00 29.22 ? 26   GLU A O   1 
ATOM   182  C CB  . GLU A 1 26  ? -108.537 -55.119 24.100 1.00 37.23 ? 26   GLU A CB  1 
ATOM   183  C CG  . GLU A 1 26  ? -108.814 -55.151 22.616 1.00 43.28 ? 26   GLU A CG  1 
ATOM   184  C CD  . GLU A 1 26  ? -109.092 -56.557 22.127 1.00 47.20 ? 26   GLU A CD  1 
ATOM   185  O OE1 . GLU A 1 26  ? -108.547 -57.515 22.725 1.00 47.86 ? 26   GLU A OE1 1 
ATOM   186  O OE2 . GLU A 1 26  ? -109.846 -56.701 21.142 1.00 49.37 ? 26   GLU A OE2 1 
ATOM   187  N N   . LEU A 1 27  ? -108.624 -53.982 27.091 1.00 31.18 ? 27   LEU A N   1 
ATOM   188  C CA  . LEU A 1 27  ? -108.158 -54.131 28.457 1.00 29.08 ? 27   LEU A CA  1 
ATOM   189  C C   . LEU A 1 27  ? -107.488 -55.492 28.631 1.00 29.34 ? 27   LEU A C   1 
ATOM   190  O O   . LEU A 1 27  ? -107.949 -56.495 28.092 1.00 25.95 ? 27   LEU A O   1 
ATOM   191  C CB  . LEU A 1 27  ? -109.332 -53.985 29.432 1.00 28.67 ? 27   LEU A CB  1 
ATOM   192  C CG  . LEU A 1 27  ? -109.879 -52.563 29.650 1.00 32.14 ? 27   LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 27  ? -111.188 -52.617 30.447 1.00 30.20 ? 27   LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 27  ? -108.841 -51.713 30.379 1.00 30.41 ? 27   LEU A CD2 1 
ATOM   195  N N   . GLY A 1 28  ? -106.387 -55.518 29.374 1.00 32.03 ? 28   GLY A N   1 
ATOM   196  C CA  . GLY A 1 28  ? -105.692 -56.768 29.615 1.00 34.56 ? 28   GLY A CA  1 
ATOM   197  C C   . GLY A 1 28  ? -106.598 -57.782 30.293 1.00 36.26 ? 28   GLY A C   1 
ATOM   198  O O   . GLY A 1 28  ? -107.536 -57.411 30.998 1.00 35.61 ? 28   GLY A O   1 
ATOM   199  N N   . LYS A 1 29  ? -106.324 -59.064 30.077 1.00 38.59 ? 29   LYS A N   1 
ATOM   200  C CA  . LYS A 1 29  ? -107.120 -60.130 30.674 1.00 43.62 ? 29   LYS A CA  1 
ATOM   201  C C   . LYS A 1 29  ? -106.685 -60.374 32.124 1.00 44.97 ? 29   LYS A C   1 
ATOM   202  O O   . LYS A 1 29  ? -105.501 -60.523 32.406 1.00 43.57 ? 29   LYS A O   1 
ATOM   203  C CB  . LYS A 1 29  ? -106.942 -61.433 29.882 1.00 46.42 ? 29   LYS A CB  1 
ATOM   204  C CG  . LYS A 1 29  ? -106.815 -61.250 28.373 1.00 52.96 ? 29   LYS A CG  1 
ATOM   205  C CD  . LYS A 1 29  ? -106.529 -62.580 27.676 1.00 56.95 ? 29   LYS A CD  1 
ATOM   206  C CE  . LYS A 1 29  ? -106.107 -62.385 26.220 1.00 59.39 ? 29   LYS A CE  1 
ATOM   207  N NZ  . LYS A 1 29  ? -107.163 -61.737 25.379 1.00 60.96 ? 29   LYS A NZ  1 
ATOM   208  N N   . VAL A 1 30  ? -107.640 -60.413 33.040 1.00 48.44 ? 30   VAL A N   1 
ATOM   209  C CA  . VAL A 1 30  ? -107.321 -60.673 34.439 1.00 53.60 ? 30   VAL A CA  1 
ATOM   210  C C   . VAL A 1 30  ? -108.454 -61.415 35.144 1.00 55.69 ? 30   VAL A C   1 
ATOM   211  O O   . VAL A 1 30  ? -109.584 -60.934 35.186 1.00 55.86 ? 30   VAL A O   1 
ATOM   212  C CB  . VAL A 1 30  ? -107.004 -59.360 35.209 1.00 54.71 ? 30   VAL A CB  1 
ATOM   213  C CG1 . VAL A 1 30  ? -108.116 -58.348 35.015 1.00 56.69 ? 30   VAL A CG1 1 
ATOM   214  C CG2 . VAL A 1 30  ? -106.817 -59.661 36.687 1.00 55.47 ? 30   VAL A CG2 1 
ATOM   215  N N   . VAL A 1 31  ? -108.141 -62.597 35.677 1.00 58.88 ? 31   VAL A N   1 
ATOM   216  C CA  . VAL A 1 31  ? -109.116 -63.415 36.399 1.00 62.56 ? 31   VAL A CA  1 
ATOM   217  C C   . VAL A 1 31  ? -109.186 -62.925 37.837 1.00 65.19 ? 31   VAL A C   1 
ATOM   218  O O   . VAL A 1 31  ? -108.163 -62.836 38.518 1.00 65.00 ? 31   VAL A O   1 
ATOM   219  C CB  . VAL A 1 31  ? -108.715 -64.908 36.425 1.00 64.09 ? 31   VAL A CB  1 
ATOM   220  C CG1 . VAL A 1 31  ? -109.768 -65.715 37.177 1.00 64.52 ? 31   VAL A CG1 1 
ATOM   221  C CG2 . VAL A 1 31  ? -108.552 -65.435 35.011 1.00 64.94 ? 31   VAL A CG2 1 
ATOM   222  N N   . THR A 1 32  ? -110.395 -62.624 38.298 1.00 68.79 ? 32   THR A N   1 
ATOM   223  C CA  . THR A 1 32  ? -110.595 -62.115 39.649 1.00 72.85 ? 32   THR A CA  1 
ATOM   224  C C   . THR A 1 32  ? -111.639 -62.894 40.449 1.00 75.18 ? 32   THR A C   1 
ATOM   225  O O   . THR A 1 32  ? -112.842 -62.733 40.237 1.00 76.47 ? 32   THR A O   1 
ATOM   226  C CB  . THR A 1 32  ? -111.010 -60.630 39.593 1.00 71.89 ? 32   THR A CB  1 
ATOM   227  O OG1 . THR A 1 32  ? -109.943 -59.862 39.024 1.00 71.05 ? 32   THR A OG1 1 
ATOM   228  C CG2 . THR A 1 32  ? -111.324 -60.103 40.978 1.00 72.85 ? 32   THR A CG2 1 
ATOM   229  N N   . LYS A 1 33  ? -111.172 -63.727 41.377 1.00 77.93 ? 33   LYS A N   1 
ATOM   230  C CA  . LYS A 1 33  ? -112.060 -64.531 42.221 1.00 80.50 ? 33   LYS A CA  1 
ATOM   231  C C   . LYS A 1 33  ? -112.094 -63.979 43.649 1.00 81.77 ? 33   LYS A C   1 
ATOM   232  O O   . LYS A 1 33  ? -111.063 -63.940 44.322 1.00 81.27 ? 33   LYS A O   1 
ATOM   233  C CB  . LYS A 1 33  ? -111.576 -65.983 42.262 1.00 80.40 ? 33   LYS A CB  1 
ATOM   234  C CG  . LYS A 1 33  ? -111.463 -66.663 40.908 1.00 81.70 ? 33   LYS A CG  1 
ATOM   235  C CD  . LYS A 1 33  ? -110.949 -68.082 41.079 1.00 83.24 ? 33   LYS A CD  1 
ATOM   236  C CE  . LYS A 1 33  ? -110.842 -68.814 39.758 1.00 84.52 ? 33   LYS A CE  1 
ATOM   237  N NZ  . LYS A 1 33  ? -110.421 -70.224 39.981 1.00 86.19 ? 33   LYS A NZ  1 
ATOM   238  N N   . LYS A 1 34  ? -113.269 -63.554 44.113 1.00 83.29 ? 34   LYS A N   1 
ATOM   239  C CA  . LYS A 1 34  ? -113.393 -63.014 45.470 1.00 84.09 ? 34   LYS A CA  1 
ATOM   240  C C   . LYS A 1 34  ? -113.801 -64.103 46.450 1.00 84.65 ? 34   LYS A C   1 
ATOM   241  O O   . LYS A 1 34  ? -114.953 -64.535 46.477 1.00 84.27 ? 34   LYS A O   1 
ATOM   242  C CB  . LYS A 1 34  ? -114.412 -61.871 45.516 1.00 84.42 ? 34   LYS A CB  1 
ATOM   243  C CG  . LYS A 1 34  ? -114.149 -60.721 44.539 1.00 85.39 ? 34   LYS A CG  1 
ATOM   244  C CD  . LYS A 1 34  ? -112.756 -60.104 44.677 1.00 85.52 ? 34   LYS A CD  1 
ATOM   245  C CE  . LYS A 1 34  ? -111.696 -60.971 44.014 1.00 86.08 ? 34   LYS A CE  1 
ATOM   246  N NZ  . LYS A 1 34  ? -110.357 -60.336 43.917 1.00 86.60 ? 34   LYS A NZ  1 
ATOM   247  N N   . PHE A 1 35  ? -112.833 -64.539 47.251 1.00 85.65 ? 35   PHE A N   1 
ATOM   248  C CA  . PHE A 1 35  ? -113.026 -65.588 48.245 1.00 86.55 ? 35   PHE A CA  1 
ATOM   249  C C   . PHE A 1 35  ? -114.168 -65.356 49.224 1.00 86.41 ? 35   PHE A C   1 
ATOM   250  O O   . PHE A 1 35  ? -115.160 -64.694 48.921 1.00 86.39 ? 35   PHE A O   1 
ATOM   251  C CB  . PHE A 1 35  ? -111.739 -65.787 49.050 1.00 88.72 ? 35   PHE A CB  1 
ATOM   252  C CG  . PHE A 1 35  ? -110.684 -66.576 48.334 1.00 91.16 ? 35   PHE A CG  1 
ATOM   253  C CD1 . PHE A 1 35  ? -110.333 -66.272 47.024 1.00 91.82 ? 35   PHE A CD1 1 
ATOM   254  C CD2 . PHE A 1 35  ? -110.017 -67.611 48.985 1.00 92.19 ? 35   PHE A CD2 1 
ATOM   255  C CE1 . PHE A 1 35  ? -109.334 -66.987 46.374 1.00 92.44 ? 35   PHE A CE1 1 
ATOM   256  C CE2 . PHE A 1 35  ? -109.015 -68.331 48.344 1.00 92.27 ? 35   PHE A CE2 1 
ATOM   257  C CZ  . PHE A 1 35  ? -108.673 -68.018 47.035 1.00 93.15 ? 35   PHE A CZ  1 
ATOM   258  N N   . SER A 1 36  ? -113.990 -65.921 50.413 1.00 86.04 ? 36   SER A N   1 
ATOM   259  C CA  . SER A 1 36  ? -114.954 -65.847 51.501 1.00 84.41 ? 36   SER A CA  1 
ATOM   260  C C   . SER A 1 36  ? -115.142 -64.441 52.046 1.00 83.05 ? 36   SER A C   1 
ATOM   261  O O   . SER A 1 36  ? -115.974 -63.675 51.560 1.00 85.17 ? 36   SER A O   1 
ATOM   262  C CB  . SER A 1 36  ? -114.500 -66.761 52.637 1.00 84.13 ? 36   SER A CB  1 
ATOM   263  O OG  . SER A 1 36  ? -113.217 -66.389 53.110 1.00 82.16 ? 36   SER A OG  1 
ATOM   264  N N   . ASN A 1 37  ? -114.364 -64.123 53.074 1.00 80.26 ? 37   ASN A N   1 
ATOM   265  C CA  . ASN A 1 37  ? -114.411 -62.827 53.735 1.00 77.48 ? 37   ASN A CA  1 
ATOM   266  C C   . ASN A 1 37  ? -114.020 -61.698 52.795 1.00 74.65 ? 37   ASN A C   1 
ATOM   267  O O   . ASN A 1 37  ? -113.473 -60.683 53.220 1.00 74.18 ? 37   ASN A O   1 
ATOM   268  C CB  . ASN A 1 37  ? -113.483 -62.845 54.954 1.00 79.57 ? 37   ASN A CB  1 
ATOM   269  C CG  . ASN A 1 37  ? -112.131 -63.475 54.654 1.00 80.07 ? 37   ASN A CG  1 
ATOM   270  O OD1 . ASN A 1 37  ? -111.302 -63.651 55.550 1.00 81.14 ? 37   ASN A OD1 1 
ATOM   271  N ND2 . ASN A 1 37  ? -111.904 -63.818 53.389 1.00 81.13 ? 37   ASN A ND2 1 
ATOM   272  N N   . GLN A 1 38  ? -114.316 -61.883 51.516 1.00 70.68 ? 38   GLN A N   1 
ATOM   273  C CA  . GLN A 1 38  ? -113.994 -60.902 50.494 1.00 66.92 ? 38   GLN A CA  1 
ATOM   274  C C   . GLN A 1 38  ? -112.491 -60.888 50.266 1.00 63.82 ? 38   GLN A C   1 
ATOM   275  O O   . GLN A 1 38  ? -111.935 -59.899 49.792 1.00 63.98 ? 38   GLN A O   1 
ATOM   276  C CB  . GLN A 1 38  ? -114.489 -59.509 50.904 1.00 67.90 ? 38   GLN A CB  1 
ATOM   277  C CG  . GLN A 1 38  ? -114.337 -58.424 49.837 1.00 66.85 ? 38   GLN A CG  1 
ATOM   278  C CD  . GLN A 1 38  ? -115.132 -58.708 48.576 1.00 67.00 ? 38   GLN A CD  1 
ATOM   279  O OE1 . GLN A 1 38  ? -114.810 -59.616 47.808 1.00 66.52 ? 38   GLN A OE1 1 
ATOM   280  N NE2 . GLN A 1 38  ? -116.181 -57.928 48.357 1.00 67.22 ? 38   GLN A NE2 1 
ATOM   281  N N   . GLU A 1 39  ? -111.828 -61.988 50.611 1.00 59.33 ? 39   GLU A N   1 
ATOM   282  C CA  . GLU A 1 39  ? -110.393 -62.067 50.393 1.00 55.92 ? 39   GLU A CA  1 
ATOM   283  C C   . GLU A 1 39  ? -110.228 -61.920 48.886 1.00 54.82 ? 39   GLU A C   1 
ATOM   284  O O   . GLU A 1 39  ? -110.760 -62.714 48.107 1.00 52.64 ? 39   GLU A O   1 
ATOM   285  C CB  . GLU A 1 39  ? -109.834 -63.411 50.862 1.00 54.87 ? 39   GLU A CB  1 
ATOM   286  C CG  . GLU A 1 39  ? -108.386 -63.324 51.297 1.00 55.20 ? 39   GLU A CG  1 
ATOM   287  C CD  . GLU A 1 39  ? -107.832 -64.642 51.793 1.00 55.28 ? 39   GLU A CD  1 
ATOM   288  O OE1 . GLU A 1 39  ? -107.367 -65.445 50.961 1.00 55.92 ? 39   GLU A OE1 1 
ATOM   289  O OE2 . GLU A 1 39  ? -107.865 -64.876 53.019 1.00 57.45 ? 39   GLU A OE2 1 
ATOM   290  N N   . THR A 1 40  ? -109.498 -60.890 48.486 1.00 53.73 ? 40   THR A N   1 
ATOM   291  C CA  . THR A 1 40  ? -109.286 -60.591 47.085 1.00 53.51 ? 40   THR A CA  1 
ATOM   292  C C   . THR A 1 40  ? -108.294 -61.508 46.387 1.00 53.97 ? 40   THR A C   1 
ATOM   293  O O   . THR A 1 40  ? -107.137 -61.616 46.791 1.00 54.32 ? 40   THR A O   1 
ATOM   294  C CB  . THR A 1 40  ? -108.804 -59.145 46.932 1.00 53.58 ? 40   THR A CB  1 
ATOM   295  O OG1 . THR A 1 40  ? -109.718 -58.271 47.602 1.00 54.16 ? 40   THR A OG1 1 
ATOM   296  C CG2 . THR A 1 40  ? -108.707 -58.755 45.465 1.00 53.64 ? 40   THR A CG2 1 
ATOM   297  N N   . CYS A 1 41  ? -108.747 -62.175 45.335 1.00 55.23 ? 41   CYS A N   1 
ATOM   298  C CA  . CYS A 1 41  ? -107.857 -63.041 44.580 1.00 57.06 ? 41   CYS A CA  1 
ATOM   299  C C   . CYS A 1 41  ? -107.808 -62.529 43.144 1.00 55.68 ? 41   CYS A C   1 
ATOM   300  O O   . CYS A 1 41  ? -108.836 -62.388 42.481 1.00 56.75 ? 41   CYS A O   1 
ATOM   301  C CB  . CYS A 1 41  ? -108.344 -64.490 44.627 1.00 58.26 ? 41   CYS A CB  1 
ATOM   302  S SG  . CYS A 1 41  ? -107.000 -65.707 44.594 1.00 66.71 ? 41   CYS A SG  1 
ATOM   303  N N   . VAL A 1 42  ? -106.602 -62.228 42.682 1.00 54.67 ? 42   VAL A N   1 
ATOM   304  C CA  . VAL A 1 42  ? -106.393 -61.712 41.342 1.00 53.93 ? 42   VAL A CA  1 
ATOM   305  C C   . VAL A 1 42  ? -105.398 -62.570 40.608 1.00 53.56 ? 42   VAL A C   1 
ATOM   306  O O   . VAL A 1 42  ? -104.559 -63.224 41.218 1.00 55.37 ? 42   VAL A O   1 
ATOM   307  C CB  . VAL A 1 42  ? -105.862 -60.270 41.385 1.00 54.28 ? 42   VAL A CB  1 
ATOM   308  C CG1 . VAL A 1 42  ? -105.251 -59.894 40.048 1.00 53.18 ? 42   VAL A CG1 1 
ATOM   309  C CG2 . VAL A 1 42  ? -106.991 -59.318 41.730 1.00 54.50 ? 42   VAL A CG2 1 
ATOM   310  N N   . GLU A 1 43  ? -105.493 -62.573 39.289 1.00 53.45 ? 43   GLU A N   1 
ATOM   311  C CA  . GLU A 1 43  ? -104.575 -63.359 38.497 1.00 52.55 ? 43   GLU A CA  1 
ATOM   312  C C   . GLU A 1 43  ? -104.462 -62.762 37.103 1.00 50.97 ? 43   GLU A C   1 
ATOM   313  O O   . GLU A 1 43  ? -105.414 -62.774 36.327 1.00 50.42 ? 43   GLU A O   1 
ATOM   314  C CB  . GLU A 1 43  ? -105.058 -64.806 38.440 1.00 54.33 ? 43   GLU A CB  1 
ATOM   315  C CG  . GLU A 1 43  ? -104.029 -65.796 37.936 1.00 57.91 ? 43   GLU A CG  1 
ATOM   316  C CD  . GLU A 1 43  ? -104.146 -67.151 38.619 1.00 61.05 ? 43   GLU A CD  1 
ATOM   317  O OE1 . GLU A 1 43  ? -104.392 -68.163 37.917 1.00 62.79 ? 43   GLU A OE1 1 
ATOM   318  O OE2 . GLU A 1 43  ? -103.992 -67.203 39.862 1.00 58.78 ? 43   GLU A OE2 1 
ATOM   319  N N   . ILE A 1 44  ? -103.290 -62.216 36.803 1.00 48.95 ? 44   ILE A N   1 
ATOM   320  C CA  . ILE A 1 44  ? -103.026 -61.612 35.506 1.00 46.08 ? 44   ILE A CA  1 
ATOM   321  C C   . ILE A 1 44  ? -103.181 -62.688 34.434 1.00 45.35 ? 44   ILE A C   1 
ATOM   322  O O   . ILE A 1 44  ? -102.444 -63.675 34.414 1.00 45.42 ? 44   ILE A O   1 
ATOM   323  C CB  . ILE A 1 44  ? -101.602 -61.023 35.477 1.00 46.68 ? 44   ILE A CB  1 
ATOM   324  C CG1 . ILE A 1 44  ? -101.427 -60.034 36.642 1.00 46.14 ? 44   ILE A CG1 1 
ATOM   325  C CG2 . ILE A 1 44  ? -101.351 -60.321 34.156 1.00 46.49 ? 44   ILE A CG2 1 
ATOM   326  C CD1 . ILE A 1 44  ? -102.419 -58.875 36.632 1.00 46.19 ? 44   ILE A CD1 1 
ATOM   327  N N   . GLY A 1 45  ? -104.152 -62.493 33.548 1.00 43.17 ? 45   GLY A N   1 
ATOM   328  C CA  . GLY A 1 45  ? -104.418 -63.464 32.507 1.00 41.04 ? 45   GLY A CA  1 
ATOM   329  C C   . GLY A 1 45  ? -103.478 -63.515 31.325 1.00 40.07 ? 45   GLY A C   1 
ATOM   330  O O   . GLY A 1 45  ? -103.706 -64.300 30.410 1.00 41.12 ? 45   GLY A O   1 
ATOM   331  N N   . GLU A 1 46  ? -102.440 -62.688 31.308 1.00 39.16 ? 46   GLU A N   1 
ATOM   332  C CA  . GLU A 1 46  ? -101.490 -62.720 30.195 1.00 38.47 ? 46   GLU A CA  1 
ATOM   333  C C   . GLU A 1 46  ? -100.131 -62.209 30.646 1.00 37.83 ? 46   GLU A C   1 
ATOM   334  O O   . GLU A 1 46  ? -99.998  -61.656 31.735 1.00 36.00 ? 46   GLU A O   1 
ATOM   335  C CB  . GLU A 1 46  ? -102.002 -61.874 29.027 1.00 38.65 ? 46   GLU A CB  1 
ATOM   336  C CG  . GLU A 1 46  ? -102.451 -60.490 29.441 1.00 41.20 ? 46   GLU A CG  1 
ATOM   337  C CD  . GLU A 1 46  ? -102.977 -59.663 28.286 1.00 42.04 ? 46   GLU A CD  1 
ATOM   338  O OE1 . GLU A 1 46  ? -102.166 -59.291 27.418 1.00 45.26 ? 46   GLU A OE1 1 
ATOM   339  O OE2 . GLU A 1 46  ? -104.195 -59.386 28.250 1.00 40.06 ? 46   GLU A OE2 1 
ATOM   340  N N   . SER A 1 47  ? -99.122  -62.391 29.803 1.00 35.57 ? 47   SER A N   1 
ATOM   341  C CA  . SER A 1 47  ? -97.780  -61.952 30.146 1.00 35.28 ? 47   SER A CA  1 
ATOM   342  C C   . SER A 1 47  ? -97.644  -60.436 30.114 1.00 35.12 ? 47   SER A C   1 
ATOM   343  O O   . SER A 1 47  ? -98.179  -59.786 29.222 1.00 33.38 ? 47   SER A O   1 
ATOM   344  C CB  . SER A 1 47  ? -96.760  -62.573 29.194 1.00 33.63 ? 47   SER A CB  1 
ATOM   345  O OG  . SER A 1 47  ? -95.460  -62.052 29.435 1.00 35.32 ? 47   SER A OG  1 
ATOM   346  N N   . VAL A 1 48  ? -96.940  -59.875 31.092 1.00 31.63 ? 48   VAL A N   1 
ATOM   347  C CA  . VAL A 1 48  ? -96.720  -58.433 31.139 1.00 31.23 ? 48   VAL A CA  1 
ATOM   348  C C   . VAL A 1 48  ? -95.220  -58.219 31.228 1.00 32.04 ? 48   VAL A C   1 
ATOM   349  O O   . VAL A 1 48  ? -94.739  -57.112 31.473 1.00 30.97 ? 48   VAL A O   1 
ATOM   350  C CB  . VAL A 1 48  ? -97.377  -57.805 32.373 1.00 31.31 ? 48   VAL A CB  1 
ATOM   351  C CG1 . VAL A 1 48  ? -98.891  -57.910 32.262 1.00 30.68 ? 48   VAL A CG1 1 
ATOM   352  C CG2 . VAL A 1 48  ? -96.864  -58.493 33.639 1.00 31.44 ? 48   VAL A CG2 1 
ATOM   353  N N   . ARG A 1 49  ? -94.489  -59.306 31.009 1.00 33.69 ? 49   ARG A N   1 
ATOM   354  C CA  . ARG A 1 49  ? -93.041  -59.294 31.091 1.00 36.16 ? 49   ARG A CA  1 
ATOM   355  C C   . ARG A 1 49  ? -92.444  -58.230 30.199 1.00 36.89 ? 49   ARG A C   1 
ATOM   356  O O   . ARG A 1 49  ? -92.587  -58.276 28.982 1.00 34.63 ? 49   ARG A O   1 
ATOM   357  C CB  . ARG A 1 49  ? -92.480  -60.669 30.719 1.00 36.83 ? 49   ARG A CB  1 
ATOM   358  C CG  . ARG A 1 49  ? -90.985  -60.774 30.939 1.00 36.73 ? 49   ARG A CG  1 
ATOM   359  C CD  . ARG A 1 49  ? -90.480  -62.180 30.702 1.00 35.78 ? 49   ARG A CD  1 
ATOM   360  N NE  . ARG A 1 49  ? -91.087  -63.157 31.600 1.00 33.85 ? 49   ARG A NE  1 
ATOM   361  C CZ  . ARG A 1 49  ? -90.620  -63.484 32.801 1.00 33.45 ? 49   ARG A CZ  1 
ATOM   362  N NH1 . ARG A 1 49  ? -89.521  -62.914 33.279 1.00 33.17 ? 49   ARG A NH1 1 
ATOM   363  N NH2 . ARG A 1 49  ? -91.262  -64.388 33.528 1.00 29.10 ? 49   ARG A NH2 1 
ATOM   364  N N   . GLY A 1 50  ? -91.781  -57.260 30.813 1.00 37.14 ? 50   GLY A N   1 
ATOM   365  C CA  . GLY A 1 50  ? -91.162  -56.206 30.042 1.00 36.92 ? 50   GLY A CA  1 
ATOM   366  C C   . GLY A 1 50  ? -92.111  -55.163 29.476 1.00 38.15 ? 50   GLY A C   1 
ATOM   367  O O   . GLY A 1 50  ? -91.698  -54.370 28.630 1.00 37.97 ? 50   GLY A O   1 
ATOM   368  N N   . GLU A 1 51  ? -93.365  -55.142 29.920 1.00 37.16 ? 51   GLU A N   1 
ATOM   369  C CA  . GLU A 1 51  ? -94.319  -54.154 29.407 1.00 36.88 ? 51   GLU A CA  1 
ATOM   370  C C   . GLU A 1 51  ? -94.532  -52.939 30.307 1.00 35.07 ? 51   GLU A C   1 
ATOM   371  O O   . GLU A 1 51  ? -94.234  -52.975 31.501 1.00 34.48 ? 51   GLU A O   1 
ATOM   372  C CB  . GLU A 1 51  ? -95.679  -54.800 29.181 1.00 39.97 ? 51   GLU A CB  1 
ATOM   373  C CG  . GLU A 1 51  ? -95.714  -55.895 28.142 1.00 44.54 ? 51   GLU A CG  1 
ATOM   374  C CD  . GLU A 1 51  ? -97.141  -56.247 27.780 1.00 49.23 ? 51   GLU A CD  1 
ATOM   375  O OE1 . GLU A 1 51  ? -97.926  -56.549 28.711 1.00 49.38 ? 51   GLU A OE1 1 
ATOM   376  O OE2 . GLU A 1 51  ? -97.480  -56.205 26.574 1.00 51.89 ? 51   GLU A OE2 1 
ATOM   377  N N   . ASP A 1 52  ? -95.078  -51.878 29.718 1.00 33.35 ? 52   ASP A N   1 
ATOM   378  C CA  . ASP A 1 52  ? -95.387  -50.637 30.428 1.00 33.01 ? 52   ASP A CA  1 
ATOM   379  C C   . ASP A 1 52  ? -96.847  -50.789 30.876 1.00 32.67 ? 52   ASP A C   1 
ATOM   380  O O   . ASP A 1 52  ? -97.779  -50.442 30.149 1.00 31.61 ? 52   ASP A O   1 
ATOM   381  C CB  . ASP A 1 52  ? -95.222  -49.437 29.477 1.00 31.71 ? 52   ASP A CB  1 
ATOM   382  C CG  . ASP A 1 52  ? -95.231  -48.091 30.202 1.00 33.77 ? 52   ASP A CG  1 
ATOM   383  O OD1 . ASP A 1 52  ? -94.972  -48.053 31.427 1.00 32.58 ? 52   ASP A OD1 1 
ATOM   384  O OD2 . ASP A 1 52  ? -95.483  -47.059 29.538 1.00 34.80 ? 52   ASP A OD2 1 
ATOM   385  N N   . VAL A 1 53  ? -97.029  -51.325 32.079 1.00 33.08 ? 53   VAL A N   1 
ATOM   386  C CA  . VAL A 1 53  ? -98.359  -51.590 32.629 1.00 32.10 ? 53   VAL A CA  1 
ATOM   387  C C   . VAL A 1 53  ? -99.046  -50.447 33.361 1.00 32.82 ? 53   VAL A C   1 
ATOM   388  O O   . VAL A 1 53  ? -98.438  -49.781 34.205 1.00 33.81 ? 53   VAL A O   1 
ATOM   389  C CB  . VAL A 1 53  ? -98.294  -52.782 33.586 1.00 30.97 ? 53   VAL A CB  1 
ATOM   390  C CG1 . VAL A 1 53  ? -99.681  -53.105 34.127 1.00 32.38 ? 53   VAL A CG1 1 
ATOM   391  C CG2 . VAL A 1 53  ? -97.705  -53.981 32.865 1.00 33.91 ? 53   VAL A CG2 1 
ATOM   392  N N   . TYR A 1 54  ? -100.324 -50.244 33.042 1.00 30.78 ? 54   TYR A N   1 
ATOM   393  C CA  . TYR A 1 54  ? -101.148 -49.217 33.673 1.00 29.68 ? 54   TYR A CA  1 
ATOM   394  C C   . TYR A 1 54  ? -102.389 -49.887 34.259 1.00 31.30 ? 54   TYR A C   1 
ATOM   395  O O   . TYR A 1 54  ? -103.140 -50.559 33.548 1.00 32.85 ? 54   TYR A O   1 
ATOM   396  C CB  . TYR A 1 54  ? -101.580 -48.145 32.656 1.00 29.36 ? 54   TYR A CB  1 
ATOM   397  C CG  . TYR A 1 54  ? -100.429 -47.342 32.107 1.00 30.83 ? 54   TYR A CG  1 
ATOM   398  C CD1 . TYR A 1 54  ? -99.586  -47.880 31.136 1.00 30.34 ? 54   TYR A CD1 1 
ATOM   399  C CD2 . TYR A 1 54  ? -100.135 -46.066 32.609 1.00 29.20 ? 54   TYR A CD2 1 
ATOM   400  C CE1 . TYR A 1 54  ? -98.483  -47.183 30.678 1.00 30.14 ? 54   TYR A CE1 1 
ATOM   401  C CE2 . TYR A 1 54  ? -99.027  -45.356 32.157 1.00 30.18 ? 54   TYR A CE2 1 
ATOM   402  C CZ  . TYR A 1 54  ? -98.203  -45.927 31.188 1.00 32.41 ? 54   TYR A CZ  1 
ATOM   403  O OH  . TYR A 1 54  ? -97.100  -45.252 30.720 1.00 33.29 ? 54   TYR A OH  1 
ATOM   404  N N   . ILE A 1 55  ? -102.600 -49.702 35.559 1.00 29.64 ? 55   ILE A N   1 
ATOM   405  C CA  . ILE A 1 55  ? -103.741 -50.295 36.240 1.00 27.68 ? 55   ILE A CA  1 
ATOM   406  C C   . ILE A 1 55  ? -104.712 -49.213 36.659 1.00 28.71 ? 55   ILE A C   1 
ATOM   407  O O   . ILE A 1 55  ? -104.399 -48.398 37.516 1.00 31.55 ? 55   ILE A O   1 
ATOM   408  C CB  . ILE A 1 55  ? -103.284 -51.078 37.483 1.00 26.02 ? 55   ILE A CB  1 
ATOM   409  C CG1 . ILE A 1 55  ? -102.337 -52.196 37.042 1.00 24.22 ? 55   ILE A CG1 1 
ATOM   410  C CG2 . ILE A 1 55  ? -104.492 -51.665 38.217 1.00 24.56 ? 55   ILE A CG2 1 
ATOM   411  C CD1 . ILE A 1 55  ? -101.778 -53.002 38.144 1.00 20.38 ? 55   ILE A CD1 1 
ATOM   412  N N   . VAL A 1 56  ? -105.887 -49.195 36.043 1.00 29.58 ? 56   VAL A N   1 
ATOM   413  C CA  . VAL A 1 56  ? -106.878 -48.194 36.375 1.00 33.10 ? 56   VAL A CA  1 
ATOM   414  C C   . VAL A 1 56  ? -107.734 -48.702 37.517 1.00 37.52 ? 56   VAL A C   1 
ATOM   415  O O   . VAL A 1 56  ? -108.397 -49.730 37.401 1.00 37.01 ? 56   VAL A O   1 
ATOM   416  C CB  . VAL A 1 56  ? -107.772 -47.860 35.169 1.00 32.38 ? 56   VAL A CB  1 
ATOM   417  C CG1 . VAL A 1 56  ? -108.728 -46.738 35.535 1.00 27.94 ? 56   VAL A CG1 1 
ATOM   418  C CG2 . VAL A 1 56  ? -106.912 -47.455 33.979 1.00 33.77 ? 56   VAL A CG2 1 
ATOM   419  N N   . GLN A 1 57  ? -107.698 -47.968 38.623 1.00 44.87 ? 57   GLN A N   1 
ATOM   420  C CA  . GLN A 1 57  ? -108.438 -48.296 39.839 1.00 52.46 ? 57   GLN A CA  1 
ATOM   421  C C   . GLN A 1 57  ? -109.920 -48.509 39.622 1.00 55.85 ? 57   GLN A C   1 
ATOM   422  O O   . GLN A 1 57  ? -110.526 -47.878 38.762 1.00 56.30 ? 57   GLN A O   1 
ATOM   423  C CB  . GLN A 1 57  ? -108.256 -47.183 40.878 1.00 56.03 ? 57   GLN A CB  1 
ATOM   424  C CG  . GLN A 1 57  ? -109.562 -46.558 41.398 1.00 61.48 ? 57   GLN A CG  1 
ATOM   425  C CD  . GLN A 1 57  ? -110.360 -45.805 40.327 1.00 65.25 ? 57   GLN A CD  1 
ATOM   426  O OE1 . GLN A 1 57  ? -111.499 -45.368 40.565 1.00 64.86 ? 57   GLN A OE1 1 
ATOM   427  N NE2 . GLN A 1 57  ? -109.767 -45.652 39.144 1.00 65.46 ? 57   GLN A NE2 1 
ATOM   428  N N   . SER A 1 58  ? -110.497 -49.391 40.429 1.00 60.57 ? 58   SER A N   1 
ATOM   429  C CA  . SER A 1 58  ? -111.922 -49.678 40.374 1.00 65.85 ? 58   SER A CA  1 
ATOM   430  C C   . SER A 1 58  ? -112.715 -48.470 40.857 1.00 67.33 ? 58   SER A C   1 
ATOM   431  O O   . SER A 1 58  ? -112.205 -47.630 41.599 1.00 68.53 ? 58   SER A O   1 
ATOM   432  C CB  . SER A 1 58  ? -112.253 -50.876 41.265 1.00 66.71 ? 58   SER A CB  1 
ATOM   433  O OG  . SER A 1 58  ? -113.649 -50.976 41.492 1.00 68.87 ? 58   SER A OG  1 
ATOM   434  N N   . GLY A 1 59  ? -113.964 -48.380 40.430 1.00 69.34 ? 59   GLY A N   1 
ATOM   435  C CA  . GLY A 1 59  ? -114.800 -47.282 40.873 1.00 71.65 ? 59   GLY A CA  1 
ATOM   436  C C   . GLY A 1 59  ? -115.974 -47.878 41.629 1.00 71.86 ? 59   GLY A C   1 
ATOM   437  O O   . GLY A 1 59  ? -117.061 -47.304 41.652 1.00 72.77 ? 59   GLY A O   1 
ATOM   438  N N   . CYS A 1 60  ? -115.746 -49.029 42.260 1.00 71.51 ? 60   CYS A N   1 
ATOM   439  C CA  . CYS A 1 60  ? -116.784 -49.734 43.000 1.00 70.61 ? 60   CYS A CA  1 
ATOM   440  C C   . CYS A 1 60  ? -116.875 -49.533 44.514 1.00 67.62 ? 60   CYS A C   1 
ATOM   441  O O   . CYS A 1 60  ? -116.436 -50.379 45.295 1.00 68.50 ? 60   CYS A O   1 
ATOM   442  C CB  . CYS A 1 60  ? -116.701 -51.232 42.670 1.00 72.50 ? 60   CYS A CB  1 
ATOM   443  S SG  . CYS A 1 60  ? -117.478 -51.609 41.067 1.00 78.09 ? 60   CYS A SG  1 
ATOM   444  N N   . GLY A 1 61  ? -117.478 -48.417 44.906 1.00 64.06 ? 61   GLY A N   1 
ATOM   445  C CA  . GLY A 1 61  ? -117.700 -48.068 46.296 1.00 58.69 ? 61   GLY A CA  1 
ATOM   446  C C   . GLY A 1 61  ? -116.860 -48.508 47.466 1.00 54.17 ? 61   GLY A C   1 
ATOM   447  O O   . GLY A 1 61  ? -116.354 -47.651 48.181 1.00 55.33 ? 61   GLY A O   1 
ATOM   448  N N   . GLU A 1 62  ? -116.733 -49.809 47.703 1.00 48.19 ? 62   GLU A N   1 
ATOM   449  C CA  . GLU A 1 62  ? -115.948 -50.294 48.844 1.00 41.36 ? 62   GLU A CA  1 
ATOM   450  C C   . GLU A 1 62  ? -114.459 -49.945 48.718 1.00 37.81 ? 62   GLU A C   1 
ATOM   451  O O   . GLU A 1 62  ? -113.696 -50.676 48.099 1.00 35.87 ? 62   GLU A O   1 
ATOM   452  C CB  . GLU A 1 62  ? -116.138 -51.806 48.978 1.00 39.91 ? 62   GLU A CB  1 
ATOM   453  C CG  . GLU A 1 62  ? -116.440 -52.306 50.398 1.00 38.81 ? 62   GLU A CG  1 
ATOM   454  C CD  . GLU A 1 62  ? -115.284 -52.108 51.388 1.00 39.07 ? 62   GLU A CD  1 
ATOM   455  O OE1 . GLU A 1 62  ? -114.118 -51.959 50.950 1.00 36.64 ? 62   GLU A OE1 1 
ATOM   456  O OE2 . GLU A 1 62  ? -115.547 -52.125 52.611 1.00 37.41 ? 62   GLU A OE2 1 
ATOM   457  N N   . ILE A 1 63  ? -114.069 -48.826 49.331 1.00 34.82 ? 63   ILE A N   1 
ATOM   458  C CA  . ILE A 1 63  ? -112.699 -48.320 49.281 1.00 32.51 ? 63   ILE A CA  1 
ATOM   459  C C   . ILE A 1 63  ? -111.590 -49.296 49.691 1.00 32.68 ? 63   ILE A C   1 
ATOM   460  O O   . ILE A 1 63  ? -110.541 -49.354 49.038 1.00 33.06 ? 63   ILE A O   1 
ATOM   461  C CB  . ILE A 1 63  ? -112.563 -47.016 50.116 1.00 32.62 ? 63   ILE A CB  1 
ATOM   462  C CG1 . ILE A 1 63  ? -111.275 -46.289 49.751 1.00 34.35 ? 63   ILE A CG1 1 
ATOM   463  C CG2 . ILE A 1 63  ? -112.581 -47.323 51.591 1.00 33.30 ? 63   ILE A CG2 1 
ATOM   464  C CD1 . ILE A 1 63  ? -111.113 -44.934 50.466 1.00 36.39 ? 63   ILE A CD1 1 
ATOM   465  N N   . ASN A 1 64  ? -111.801 -50.058 50.756 1.00 28.10 ? 64   ASN A N   1 
ATOM   466  C CA  . ASN A 1 64  ? -110.775 -50.999 51.178 1.00 28.81 ? 64   ASN A CA  1 
ATOM   467  C C   . ASN A 1 64  ? -110.612 -52.192 50.220 1.00 30.02 ? 64   ASN A C   1 
ATOM   468  O O   . ASN A 1 64  ? -109.484 -52.634 49.981 1.00 28.49 ? 64   ASN A O   1 
ATOM   469  C CB  . ASN A 1 64  ? -111.046 -51.462 52.609 1.00 29.07 ? 64   ASN A CB  1 
ATOM   470  C CG  . ASN A 1 64  ? -111.086 -50.295 53.583 1.00 29.72 ? 64   ASN A CG  1 
ATOM   471  O OD1 . ASN A 1 64  ? -110.242 -49.395 53.516 1.00 27.77 ? 64   ASN A OD1 1 
ATOM   472  N ND2 . ASN A 1 64  ? -112.064 -50.298 54.489 1.00 27.94 ? 64   ASN A ND2 1 
ATOM   473  N N   . ASP A 1 65  ? -111.711 -52.706 49.663 1.00 28.71 ? 65   ASP A N   1 
ATOM   474  C CA  . ASP A 1 65  ? -111.615 -53.816 48.710 1.00 29.26 ? 65   ASP A CA  1 
ATOM   475  C C   . ASP A 1 65  ? -110.922 -53.298 47.448 1.00 30.07 ? 65   ASP A C   1 
ATOM   476  O O   . ASP A 1 65  ? -110.083 -53.976 46.865 1.00 29.67 ? 65   ASP A O   1 
ATOM   477  C CB  . ASP A 1 65  ? -113.003 -54.346 48.318 1.00 30.45 ? 65   ASP A CB  1 
ATOM   478  C CG  . ASP A 1 65  ? -113.734 -55.005 49.472 1.00 32.23 ? 65   ASP A CG  1 
ATOM   479  O OD1 . ASP A 1 65  ? -113.091 -55.746 50.250 1.00 29.21 ? 65   ASP A OD1 1 
ATOM   480  O OD2 . ASP A 1 65  ? -114.960 -54.797 49.584 1.00 34.90 ? 65   ASP A OD2 1 
ATOM   481  N N   . ASN A 1 66  ? -111.291 -52.090 47.032 1.00 30.55 ? 66   ASN A N   1 
ATOM   482  C CA  . ASN A 1 66  ? -110.709 -51.478 45.846 1.00 32.89 ? 66   ASN A CA  1 
ATOM   483  C C   . ASN A 1 66  ? -109.208 -51.267 45.981 1.00 31.51 ? 66   ASN A C   1 
ATOM   484  O O   . ASN A 1 66  ? -108.441 -51.597 45.075 1.00 30.56 ? 66   ASN A O   1 
ATOM   485  C CB  . ASN A 1 66  ? -111.391 -50.148 45.569 1.00 35.49 ? 66   ASN A CB  1 
ATOM   486  C CG  . ASN A 1 66  ? -112.496 -50.270 44.548 1.00 43.35 ? 66   ASN A CG  1 
ATOM   487  O OD1 . ASN A 1 66  ? -113.292 -51.218 44.566 1.00 45.13 ? 66   ASN A OD1 1 
ATOM   488  N ND2 . ASN A 1 66  ? -112.561 -49.300 43.647 1.00 48.82 ? 66   ASN A ND2 1 
ATOM   489  N N   . LEU A 1 67  ? -108.794 -50.715 47.118 1.00 29.76 ? 67   LEU A N   1 
ATOM   490  C CA  . LEU A 1 67  ? -107.386 -50.465 47.376 1.00 28.01 ? 67   LEU A CA  1 
ATOM   491  C C   . LEU A 1 67  ? -106.604 -51.778 47.422 1.00 28.73 ? 67   LEU A C   1 
ATOM   492  O O   . LEU A 1 67  ? -105.519 -51.882 46.854 1.00 29.84 ? 67   LEU A O   1 
ATOM   493  C CB  . LEU A 1 67  ? -107.226 -49.705 48.693 1.00 26.34 ? 67   LEU A CB  1 
ATOM   494  C CG  . LEU A 1 67  ? -105.791 -49.494 49.158 1.00 22.78 ? 67   LEU A CG  1 
ATOM   495  C CD1 . LEU A 1 67  ? -104.980 -48.782 48.079 1.00 23.97 ? 67   LEU A CD1 1 
ATOM   496  C CD2 . LEU A 1 67  ? -105.812 -48.707 50.433 1.00 22.92 ? 67   LEU A CD2 1 
ATOM   497  N N   . MET A 1 68  ? -107.147 -52.787 48.092 1.00 28.89 ? 68   MET A N   1 
ATOM   498  C CA  . MET A 1 68  ? -106.448 -54.065 48.148 1.00 30.80 ? 68   MET A CA  1 
ATOM   499  C C   . MET A 1 68  ? -106.317 -54.698 46.760 1.00 30.47 ? 68   MET A C   1 
ATOM   500  O O   . MET A 1 68  ? -105.260 -55.225 46.416 1.00 28.14 ? 68   MET A O   1 
ATOM   501  C CB  . MET A 1 68  ? -107.152 -55.041 49.094 1.00 30.78 ? 68   MET A CB  1 
ATOM   502  C CG  . MET A 1 68  ? -106.775 -54.844 50.548 1.00 35.57 ? 68   MET A CG  1 
ATOM   503  S SD  . MET A 1 68  ? -104.964 -54.756 50.786 1.00 42.18 ? 68   MET A SD  1 
ATOM   504  C CE  . MET A 1 68  ? -104.465 -56.374 50.203 1.00 31.05 ? 68   MET A CE  1 
ATOM   505  N N   . GLU A 1 69  ? -107.381 -54.642 45.960 1.00 30.14 ? 69   GLU A N   1 
ATOM   506  C CA  . GLU A 1 69  ? -107.316 -55.225 44.626 1.00 30.89 ? 69   GLU A CA  1 
ATOM   507  C C   . GLU A 1 69  ? -106.267 -54.497 43.781 1.00 29.79 ? 69   GLU A C   1 
ATOM   508  O O   . GLU A 1 69  ? -105.529 -55.121 43.020 1.00 28.14 ? 69   GLU A O   1 
ATOM   509  C CB  . GLU A 1 69  ? -108.681 -55.175 43.938 1.00 32.72 ? 69   GLU A CB  1 
ATOM   510  C CG  . GLU A 1 69  ? -108.664 -55.750 42.526 1.00 38.43 ? 69   GLU A CG  1 
ATOM   511  C CD  . GLU A 1 69  ? -110.049 -55.845 41.903 1.00 43.28 ? 69   GLU A CD  1 
ATOM   512  O OE1 . GLU A 1 69  ? -110.792 -54.841 41.930 1.00 43.74 ? 69   GLU A OE1 1 
ATOM   513  O OE2 . GLU A 1 69  ? -110.390 -56.927 41.378 1.00 48.26 ? 69   GLU A OE2 1 
ATOM   514  N N   . LEU A 1 70  ? -106.195 -53.179 43.934 1.00 27.74 ? 70   LEU A N   1 
ATOM   515  C CA  . LEU A 1 70  ? -105.228 -52.382 43.192 1.00 27.80 ? 70   LEU A CA  1 
ATOM   516  C C   . LEU A 1 70  ? -103.804 -52.769 43.601 1.00 28.37 ? 70   LEU A C   1 
ATOM   517  O O   . LEU A 1 70  ? -102.918 -52.919 42.754 1.00 28.15 ? 70   LEU A O   1 
ATOM   518  C CB  . LEU A 1 70  ? -105.452 -50.891 43.469 1.00 26.66 ? 70   LEU A CB  1 
ATOM   519  C CG  . LEU A 1 70  ? -104.333 -49.977 42.967 1.00 29.17 ? 70   LEU A CG  1 
ATOM   520  C CD1 . LEU A 1 70  ? -104.221 -50.079 41.448 1.00 26.80 ? 70   LEU A CD1 1 
ATOM   521  C CD2 . LEU A 1 70  ? -104.614 -48.545 43.395 1.00 29.58 ? 70   LEU A CD2 1 
ATOM   522  N N   . LEU A 1 71  ? -103.594 -52.919 44.907 1.00 26.76 ? 71   LEU A N   1 
ATOM   523  C CA  . LEU A 1 71  ? -102.289 -53.286 45.441 1.00 25.22 ? 71   LEU A CA  1 
ATOM   524  C C   . LEU A 1 71  ? -101.873 -54.683 45.004 1.00 25.98 ? 71   LEU A C   1 
ATOM   525  O O   . LEU A 1 71  ? -100.723 -54.918 44.620 1.00 26.53 ? 71   LEU A O   1 
ATOM   526  C CB  . LEU A 1 71  ? -102.313 -53.204 46.967 1.00 25.95 ? 71   LEU A CB  1 
ATOM   527  C CG  . LEU A 1 71  ? -102.459 -51.764 47.489 1.00 25.13 ? 71   LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 71  ? -102.783 -51.767 48.958 1.00 25.42 ? 71   LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 71  ? -101.172 -50.995 47.227 1.00 21.02 ? 71   LEU A CD2 1 
ATOM   530  N N   . ILE A 1 72  ? -102.814 -55.612 45.062 1.00 25.54 ? 72   ILE A N   1 
ATOM   531  C CA  . ILE A 1 72  ? -102.548 -56.982 44.672 1.00 26.25 ? 72   ILE A CA  1 
ATOM   532  C C   . ILE A 1 72  ? -102.214 -57.063 43.185 1.00 26.15 ? 72   ILE A C   1 
ATOM   533  O O   . ILE A 1 72  ? -101.350 -57.843 42.774 1.00 27.21 ? 72   ILE A O   1 
ATOM   534  C CB  . ILE A 1 72  ? -103.770 -57.868 44.987 1.00 28.87 ? 72   ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 72  ? -103.945 -57.970 46.505 1.00 27.33 ? 72   ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 72  ? -103.606 -59.243 44.357 1.00 27.28 ? 72   ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 72  ? -105.223 -58.656 46.925 1.00 30.86 ? 72   ILE A CD1 1 
ATOM   538  N N   . MET A 1 73  ? -102.886 -56.245 42.380 1.00 25.19 ? 73   MET A N   1 
ATOM   539  C CA  . MET A 1 73  ? -102.648 -56.252 40.946 1.00 26.02 ? 73   MET A CA  1 
ATOM   540  C C   . MET A 1 73  ? -101.274 -55.696 40.619 1.00 27.59 ? 73   MET A C   1 
ATOM   541  O O   . MET A 1 73  ? -100.576 -56.222 39.756 1.00 29.80 ? 73   MET A O   1 
ATOM   542  C CB  . MET A 1 73  ? -103.732 -55.454 40.218 1.00 28.85 ? 73   MET A CB  1 
ATOM   543  C CG  . MET A 1 73  ? -105.022 -56.235 40.015 1.00 34.55 ? 73   MET A CG  1 
ATOM   544  S SD  . MET A 1 73  ? -106.204 -55.342 38.979 1.00 42.39 ? 73   MET A SD  1 
ATOM   545  C CE  . MET A 1 73  ? -105.321 -55.391 37.427 1.00 34.90 ? 73   MET A CE  1 
ATOM   546  N N   . ILE A 1 74  ? -100.890 -54.629 41.313 1.00 27.06 ? 74   ILE A N   1 
ATOM   547  C CA  . ILE A 1 74  ? -99.594  -54.010 41.119 1.00 25.29 ? 74   ILE A CA  1 
ATOM   548  C C   . ILE A 1 74  ? -98.526  -55.041 41.461 1.00 27.24 ? 74   ILE A C   1 
ATOM   549  O O   . ILE A 1 74  ? -97.564  -55.231 40.721 1.00 28.75 ? 74   ILE A O   1 
ATOM   550  C CB  . ILE A 1 74  ? -99.412  -52.786 42.069 1.00 24.77 ? 74   ILE A CB  1 
ATOM   551  C CG1 . ILE A 1 74  ? -100.377 -51.662 41.675 1.00 22.96 ? 74   ILE A CG1 1 
ATOM   552  C CG2 . ILE A 1 74  ? -97.965  -52.318 42.039 1.00 19.95 ? 74   ILE A CG2 1 
ATOM   553  C CD1 . ILE A 1 74  ? -100.517 -50.571 42.722 1.00 23.97 ? 74   ILE A CD1 1 
ATOM   554  N N   . ASN A 1 75  ? -98.698  -55.705 42.597 1.00 27.93 ? 75   ASN A N   1 
ATOM   555  C CA  . ASN A 1 75  ? -97.734  -56.696 43.037 1.00 29.40 ? 75   ASN A CA  1 
ATOM   556  C C   . ASN A 1 75  ? -97.610  -57.857 42.056 1.00 30.52 ? 75   ASN A C   1 
ATOM   557  O O   . ASN A 1 75  ? -96.499  -58.302 41.748 1.00 32.11 ? 75   ASN A O   1 
ATOM   558  C CB  . ASN A 1 75  ? -98.117  -57.219 44.420 1.00 30.82 ? 75   ASN A CB  1 
ATOM   559  C CG  . ASN A 1 75  ? -97.107  -58.220 44.961 1.00 34.53 ? 75   ASN A CG  1 
ATOM   560  O OD1 . ASN A 1 75  ? -97.325  -59.436 44.917 1.00 34.33 ? 75   ASN A OD1 1 
ATOM   561  N ND2 . ASN A 1 75  ? -95.991  -57.710 45.462 1.00 35.64 ? 75   ASN A ND2 1 
ATOM   562  N N   . ALA A 1 76  ? -98.744  -58.347 41.559 1.00 30.49 ? 76   ALA A N   1 
ATOM   563  C CA  . ALA A 1 76  ? -98.712  -59.468 40.623 1.00 30.93 ? 76   ALA A CA  1 
ATOM   564  C C   . ALA A 1 76  ? -97.937  -59.104 39.365 1.00 31.77 ? 76   ALA A C   1 
ATOM   565  O O   . ALA A 1 76  ? -97.132  -59.898 38.873 1.00 30.76 ? 76   ALA A O   1 
ATOM   566  C CB  . ALA A 1 76  ? -100.130 -59.901 40.255 1.00 29.38 ? 76   ALA A CB  1 
ATOM   567  N N   . CYS A 1 77  ? -98.180  -57.904 38.847 1.00 30.73 ? 77   CYS A N   1 
ATOM   568  C CA  . CYS A 1 77  ? -97.501  -57.462 37.636 1.00 32.61 ? 77   CYS A CA  1 
ATOM   569  C C   . CYS A 1 77  ? -96.006  -57.298 37.866 1.00 33.19 ? 77   CYS A C   1 
ATOM   570  O O   . CYS A 1 77  ? -95.201  -57.671 37.018 1.00 34.14 ? 77   CYS A O   1 
ATOM   571  C CB  . CYS A 1 77  ? -98.083  -56.134 37.142 1.00 30.78 ? 77   CYS A CB  1 
ATOM   572  S SG  . CYS A 1 77  ? -99.739  -56.230 36.460 1.00 32.98 ? 77   CYS A SG  1 
ATOM   573  N N   . LYS A 1 78  ? -95.642  -56.735 39.014 1.00 33.83 ? 78   LYS A N   1 
ATOM   574  C CA  . LYS A 1 78  ? -94.242  -56.509 39.348 1.00 33.26 ? 78   LYS A CA  1 
ATOM   575  C C   . LYS A 1 78  ? -93.459  -57.820 39.462 1.00 33.52 ? 78   LYS A C   1 
ATOM   576  O O   . LYS A 1 78  ? -92.374  -57.946 38.899 1.00 34.77 ? 78   LYS A O   1 
ATOM   577  C CB  . LYS A 1 78  ? -94.143  -55.712 40.651 1.00 36.05 ? 78   LYS A CB  1 
ATOM   578  C CG  . LYS A 1 78  ? -93.015  -54.700 40.664 1.00 39.29 ? 78   LYS A CG  1 
ATOM   579  C CD  . LYS A 1 78  ? -93.176  -53.690 39.536 1.00 40.37 ? 78   LYS A CD  1 
ATOM   580  C CE  . LYS A 1 78  ? -92.002  -52.723 39.483 1.00 41.73 ? 78   LYS A CE  1 
ATOM   581  N NZ  . LYS A 1 78  ? -91.778  -52.027 40.783 1.00 39.93 ? 78   LYS A NZ  1 
ATOM   582  N N   . ILE A 1 79  ? -93.994  -58.802 40.176 1.00 32.88 ? 79   ILE A N   1 
ATOM   583  C CA  . ILE A 1 79  ? -93.290  -60.077 40.298 1.00 33.07 ? 79   ILE A CA  1 
ATOM   584  C C   . ILE A 1 79  ? -93.425  -60.890 39.006 1.00 33.49 ? 79   ILE A C   1 
ATOM   585  O O   . ILE A 1 79  ? -92.864  -61.986 38.889 1.00 32.64 ? 79   ILE A O   1 
ATOM   586  C CB  . ILE A 1 79  ? -93.805  -60.919 41.489 1.00 33.80 ? 79   ILE A CB  1 
ATOM   587  C CG1 . ILE A 1 79  ? -95.291  -61.231 41.310 1.00 35.24 ? 79   ILE A CG1 1 
ATOM   588  C CG2 . ILE A 1 79  ? -93.585  -60.162 42.793 1.00 33.23 ? 79   ILE A CG2 1 
ATOM   589  C CD1 . ILE A 1 79  ? -95.850  -62.137 42.375 1.00 37.91 ? 79   ILE A CD1 1 
ATOM   590  N N   . ALA A 1 80  ? -94.169  -60.346 38.041 1.00 31.93 ? 80   ALA A N   1 
ATOM   591  C CA  . ALA A 1 80  ? -94.346  -60.996 36.739 1.00 31.36 ? 80   ALA A CA  1 
ATOM   592  C C   . ALA A 1 80  ? -93.387  -60.338 35.745 1.00 31.37 ? 80   ALA A C   1 
ATOM   593  O O   . ALA A 1 80  ? -93.499  -60.507 34.529 1.00 32.56 ? 80   ALA A O   1 
ATOM   594  C CB  . ALA A 1 80  ? -95.773  -60.851 36.262 1.00 29.96 ? 80   ALA A CB  1 
ATOM   595  N N   . SER A 1 81  ? -92.454  -59.565 36.290 1.00 30.85 ? 81   SER A N   1 
ATOM   596  C CA  . SER A 1 81  ? -91.428  -58.880 35.513 1.00 31.13 ? 81   SER A CA  1 
ATOM   597  C C   . SER A 1 81  ? -91.885  -57.766 34.593 1.00 31.90 ? 81   SER A C   1 
ATOM   598  O O   . SER A 1 81  ? -91.238  -57.488 33.581 1.00 30.59 ? 81   SER A O   1 
ATOM   599  C CB  . SER A 1 81  ? -90.606  -59.890 34.714 1.00 31.20 ? 81   SER A CB  1 
ATOM   600  O OG  . SER A 1 81  ? -89.880  -60.745 35.579 1.00 29.93 ? 81   SER A OG  1 
ATOM   601  N N   . ALA A 1 82  ? -92.994  -57.122 34.938 1.00 32.87 ? 82   ALA A N   1 
ATOM   602  C CA  . ALA A 1 82  ? -93.464  -56.004 34.137 1.00 34.14 ? 82   ALA A CA  1 
ATOM   603  C C   . ALA A 1 82  ? -92.324  -54.990 34.139 1.00 36.00 ? 82   ALA A C   1 
ATOM   604  O O   . ALA A 1 82  ? -91.578  -54.880 35.113 1.00 35.91 ? 82   ALA A O   1 
ATOM   605  C CB  . ALA A 1 82  ? -94.706  -55.389 34.755 1.00 31.77 ? 82   ALA A CB  1 
ATOM   606  N N   . SER A 1 83  ? -92.176  -54.263 33.043 1.00 37.75 ? 83   SER A N   1 
ATOM   607  C CA  . SER A 1 83  ? -91.119  -53.272 32.951 1.00 38.80 ? 83   SER A CA  1 
ATOM   608  C C   . SER A 1 83  ? -91.370  -52.094 33.885 1.00 38.70 ? 83   SER A C   1 
ATOM   609  O O   . SER A 1 83  ? -90.450  -51.621 34.555 1.00 37.42 ? 83   SER A O   1 
ATOM   610  C CB  . SER A 1 83  ? -90.996  -52.765 31.518 1.00 40.08 ? 83   SER A CB  1 
ATOM   611  O OG  . SER A 1 83  ? -90.133  -51.644 31.477 1.00 46.43 ? 83   SER A OG  1 
ATOM   612  N N   . ARG A 1 84  ? -92.617  -51.623 33.923 1.00 37.82 ? 84   ARG A N   1 
ATOM   613  C CA  . ARG A 1 84  ? -92.990  -50.488 34.764 1.00 35.76 ? 84   ARG A CA  1 
ATOM   614  C C   . ARG A 1 84  ? -94.472  -50.583 35.122 1.00 34.05 ? 84   ARG A C   1 
ATOM   615  O O   . ARG A 1 84  ? -95.283  -51.005 34.302 1.00 34.21 ? 84   ARG A O   1 
ATOM   616  C CB  . ARG A 1 84  ? -92.705  -49.177 34.012 1.00 36.69 ? 84   ARG A CB  1 
ATOM   617  C CG  . ARG A 1 84  ? -92.919  -47.911 34.830 1.00 41.93 ? 84   ARG A CG  1 
ATOM   618  C CD  . ARG A 1 84  ? -92.460  -46.653 34.088 1.00 43.67 ? 84   ARG A CD  1 
ATOM   619  N NE  . ARG A 1 84  ? -93.257  -46.400 32.890 1.00 50.60 ? 84   ARG A NE  1 
ATOM   620  C CZ  . ARG A 1 84  ? -93.188  -45.292 32.154 1.00 50.75 ? 84   ARG A CZ  1 
ATOM   621  N NH1 . ARG A 1 84  ? -92.352  -44.314 32.484 1.00 53.33 ? 84   ARG A NH1 1 
ATOM   622  N NH2 . ARG A 1 84  ? -93.961  -45.161 31.088 1.00 50.57 ? 84   ARG A NH2 1 
ATOM   623  N N   . VAL A 1 85  ? -94.824  -50.212 36.352 1.00 32.44 ? 85   VAL A N   1 
ATOM   624  C CA  . VAL A 1 85  ? -96.220  -50.256 36.783 1.00 29.67 ? 85   VAL A CA  1 
ATOM   625  C C   . VAL A 1 85  ? -96.689  -48.885 37.258 1.00 28.71 ? 85   VAL A C   1 
ATOM   626  O O   . VAL A 1 85  ? -96.160  -48.339 38.221 1.00 27.78 ? 85   VAL A O   1 
ATOM   627  C CB  . VAL A 1 85  ? -96.459  -51.247 37.945 1.00 29.95 ? 85   VAL A CB  1 
ATOM   628  C CG1 . VAL A 1 85  ? -97.965  -51.345 38.216 1.00 27.46 ? 85   VAL A CG1 1 
ATOM   629  C CG2 . VAL A 1 85  ? -95.871  -52.620 37.619 1.00 26.52 ? 85   VAL A CG2 1 
ATOM   630  N N   . THR A 1 86  ? -97.681  -48.340 36.566 1.00 24.80 ? 86   THR A N   1 
ATOM   631  C CA  . THR A 1 86  ? -98.244  -47.050 36.912 1.00 24.84 ? 86   THR A CA  1 
ATOM   632  C C   . THR A 1 86  ? -99.642  -47.271 37.474 1.00 25.92 ? 86   THR A C   1 
ATOM   633  O O   . THR A 1 86  ? -100.433 -48.033 36.900 1.00 22.82 ? 86   THR A O   1 
ATOM   634  C CB  . THR A 1 86  ? -98.354  -46.137 35.664 1.00 25.59 ? 86   THR A CB  1 
ATOM   635  O OG1 . THR A 1 86  ? -97.042  -45.759 35.234 1.00 28.33 ? 86   THR A OG1 1 
ATOM   636  C CG2 . THR A 1 86  ? -99.171  -44.872 35.976 1.00 23.48 ? 86   THR A CG2 1 
ATOM   637  N N   . ALA A 1 87  ? -99.932  -46.653 38.618 1.00 23.52 ? 87   ALA A N   1 
ATOM   638  C CA  . ALA A 1 87  ? -101.269 -46.759 39.186 1.00 24.88 ? 87   ALA A CA  1 
ATOM   639  C C   . ALA A 1 87  ? -102.020 -45.508 38.713 1.00 23.34 ? 87   ALA A C   1 
ATOM   640  O O   . ALA A 1 87  ? -101.553 -44.390 38.908 1.00 22.52 ? 87   ALA A O   1 
ATOM   641  C CB  . ALA A 1 87  ? -101.216 -46.800 40.716 1.00 23.77 ? 87   ALA A CB  1 
ATOM   642  N N   . VAL A 1 88  ? -103.146 -45.703 38.034 1.00 22.24 ? 88   VAL A N   1 
ATOM   643  C CA  . VAL A 1 88  ? -103.958 -44.584 37.567 1.00 22.34 ? 88   VAL A CA  1 
ATOM   644  C C   . VAL A 1 88  ? -105.100 -44.583 38.571 1.00 23.17 ? 88   VAL A C   1 
ATOM   645  O O   . VAL A 1 88  ? -105.909 -45.516 38.589 1.00 21.68 ? 88   VAL A O   1 
ATOM   646  C CB  . VAL A 1 88  ? -104.486 -44.823 36.127 1.00 21.98 ? 88   VAL A CB  1 
ATOM   647  C CG1 . VAL A 1 88  ? -105.393 -43.661 35.693 1.00 22.84 ? 88   VAL A CG1 1 
ATOM   648  C CG2 . VAL A 1 88  ? -103.320 -44.936 35.158 1.00 23.26 ? 88   VAL A CG2 1 
ATOM   649  N N   . ILE A 1 89  ? -105.126 -43.553 39.420 1.00 23.15 ? 89   ILE A N   1 
ATOM   650  C CA  . ILE A 1 89  ? -106.113 -43.421 40.496 1.00 26.79 ? 89   ILE A CA  1 
ATOM   651  C C   . ILE A 1 89  ? -106.849 -42.085 40.443 1.00 27.21 ? 89   ILE A C   1 
ATOM   652  O O   . ILE A 1 89  ? -106.485 -41.141 41.141 1.00 25.35 ? 89   ILE A O   1 
ATOM   653  C CB  . ILE A 1 89  ? -105.439 -43.495 41.892 1.00 29.05 ? 89   ILE A CB  1 
ATOM   654  C CG1 . ILE A 1 89  ? -104.431 -44.645 41.957 1.00 27.04 ? 89   ILE A CG1 1 
ATOM   655  C CG2 . ILE A 1 89  ? -106.511 -43.699 42.967 1.00 28.51 ? 89   ILE A CG2 1 
ATOM   656  C CD1 . ILE A 1 89  ? -103.460 -44.521 43.147 1.00 26.71 ? 89   ILE A CD1 1 
ATOM   657  N N   . PRO A 1 90  ? -107.914 -42.002 39.637 1.00 29.89 ? 90   PRO A N   1 
ATOM   658  C CA  . PRO A 1 90  ? -108.701 -40.777 39.493 1.00 32.08 ? 90   PRO A CA  1 
ATOM   659  C C   . PRO A 1 90  ? -108.975 -40.138 40.845 1.00 31.61 ? 90   PRO A C   1 
ATOM   660  O O   . PRO A 1 90  ? -108.710 -38.956 41.047 1.00 33.43 ? 90   PRO A O   1 
ATOM   661  C CB  . PRO A 1 90  ? -109.973 -41.281 38.809 1.00 30.70 ? 90   PRO A CB  1 
ATOM   662  C CG  . PRO A 1 90  ? -109.448 -42.396 37.960 1.00 30.61 ? 90   PRO A CG  1 
ATOM   663  C CD  . PRO A 1 90  ? -108.601 -43.124 38.975 1.00 31.35 ? 90   PRO A CD  1 
ATOM   664  N N   . CYS A 1 91  ? -109.478 -40.945 41.772 1.00 29.79 ? 91   CYS A N   1 
ATOM   665  C CA  . CYS A 1 91  ? -109.799 -40.478 43.110 1.00 31.16 ? 91   CYS A CA  1 
ATOM   666  C C   . CYS A 1 91  ? -108.866 -41.176 44.113 1.00 31.07 ? 91   CYS A C   1 
ATOM   667  O O   . CYS A 1 91  ? -109.005 -42.364 44.379 1.00 29.47 ? 91   CYS A O   1 
ATOM   668  C CB  . CYS A 1 91  ? -111.274 -40.792 43.393 1.00 33.29 ? 91   CYS A CB  1 
ATOM   669  S SG  . CYS A 1 91  ? -111.922 -40.031 44.884 1.00 37.85 ? 91   CYS A SG  1 
ATOM   670  N N   . PHE A 1 92  ? -107.906 -40.433 44.655 1.00 30.62 ? 92   PHE A N   1 
ATOM   671  C CA  . PHE A 1 92  ? -106.944 -40.997 45.594 1.00 29.82 ? 92   PHE A CA  1 
ATOM   672  C C   . PHE A 1 92  ? -107.625 -41.381 46.907 1.00 31.08 ? 92   PHE A C   1 
ATOM   673  O O   . PHE A 1 92  ? -108.142 -40.522 47.622 1.00 29.03 ? 92   PHE A O   1 
ATOM   674  C CB  . PHE A 1 92  ? -105.816 -39.991 45.870 1.00 29.36 ? 92   PHE A CB  1 
ATOM   675  C CG  . PHE A 1 92  ? -104.575 -40.616 46.462 1.00 29.53 ? 92   PHE A CG  1 
ATOM   676  C CD1 . PHE A 1 92  ? -103.564 -41.103 45.638 1.00 29.16 ? 92   PHE A CD1 1 
ATOM   677  C CD2 . PHE A 1 92  ? -104.433 -40.744 47.843 1.00 29.69 ? 92   PHE A CD2 1 
ATOM   678  C CE1 . PHE A 1 92  ? -102.430 -41.711 46.185 1.00 32.38 ? 92   PHE A CE1 1 
ATOM   679  C CE2 . PHE A 1 92  ? -103.301 -41.351 48.399 1.00 30.25 ? 92   PHE A CE2 1 
ATOM   680  C CZ  . PHE A 1 92  ? -102.300 -41.834 47.570 1.00 30.00 ? 92   PHE A CZ  1 
ATOM   681  N N   . PRO A 1 93  ? -107.623 -42.685 47.246 1.00 32.21 ? 93   PRO A N   1 
ATOM   682  C CA  . PRO A 1 93  ? -108.259 -43.129 48.487 1.00 32.09 ? 93   PRO A CA  1 
ATOM   683  C C   . PRO A 1 93  ? -107.558 -42.572 49.720 1.00 32.86 ? 93   PRO A C   1 
ATOM   684  O O   . PRO A 1 93  ? -106.334 -42.435 49.740 1.00 32.47 ? 93   PRO A O   1 
ATOM   685  C CB  . PRO A 1 93  ? -108.191 -44.658 48.387 1.00 31.56 ? 93   PRO A CB  1 
ATOM   686  C CG  . PRO A 1 93  ? -106.971 -44.899 47.579 1.00 32.88 ? 93   PRO A CG  1 
ATOM   687  C CD  . PRO A 1 93  ? -107.048 -43.831 46.510 1.00 33.72 ? 93   PRO A CD  1 
ATOM   688  N N   . TYR A 1 94  ? -108.359 -42.242 50.732 1.00 30.36 ? 94   TYR A N   1 
ATOM   689  C CA  . TYR A 1 94  ? -107.891 -41.684 51.999 1.00 30.11 ? 94   TYR A CA  1 
ATOM   690  C C   . TYR A 1 94  ? -107.192 -40.335 51.882 1.00 29.22 ? 94   TYR A C   1 
ATOM   691  O O   . TYR A 1 94  ? -106.523 -39.910 52.817 1.00 28.97 ? 94   TYR A O   1 
ATOM   692  C CB  . TYR A 1 94  ? -106.969 -42.678 52.730 1.00 29.37 ? 94   TYR A CB  1 
ATOM   693  C CG  . TYR A 1 94  ? -107.707 -43.882 53.266 1.00 27.44 ? 94   TYR A CG  1 
ATOM   694  C CD1 . TYR A 1 94  ? -107.966 -44.983 52.452 1.00 28.08 ? 94   TYR A CD1 1 
ATOM   695  C CD2 . TYR A 1 94  ? -108.206 -43.892 54.565 1.00 26.65 ? 94   TYR A CD2 1 
ATOM   696  C CE1 . TYR A 1 94  ? -108.706 -46.060 52.918 1.00 25.77 ? 94   TYR A CE1 1 
ATOM   697  C CE2 . TYR A 1 94  ? -108.948 -44.961 55.041 1.00 25.29 ? 94   TYR A CE2 1 
ATOM   698  C CZ  . TYR A 1 94  ? -109.193 -46.041 54.213 1.00 25.19 ? 94   TYR A CZ  1 
ATOM   699  O OH  . TYR A 1 94  ? -109.910 -47.107 54.686 1.00 23.82 ? 94   TYR A OH  1 
ATOM   700  N N   . ALA A 1 95  ? -107.374 -39.651 50.756 1.00 27.89 ? 95   ALA A N   1 
ATOM   701  C CA  . ALA A 1 95  ? -106.732 -38.353 50.533 1.00 29.54 ? 95   ALA A CA  1 
ATOM   702  C C   . ALA A 1 95  ? -107.066 -37.331 51.612 1.00 31.29 ? 95   ALA A C   1 
ATOM   703  O O   . ALA A 1 95  ? -106.239 -36.486 51.948 1.00 33.36 ? 95   ALA A O   1 
ATOM   704  C CB  . ALA A 1 95  ? -107.111 -37.799 49.147 1.00 25.62 ? 95   ALA A CB  1 
ATOM   705  N N   . ARG A 1 96  ? -108.278 -37.406 52.151 1.00 33.00 ? 96   ARG A N   1 
ATOM   706  C CA  . ARG A 1 96  ? -108.716 -36.488 53.197 1.00 36.15 ? 96   ARG A CA  1 
ATOM   707  C C   . ARG A 1 96  ? -107.929 -36.667 54.499 1.00 37.19 ? 96   ARG A C   1 
ATOM   708  O O   . ARG A 1 96  ? -107.711 -35.710 55.242 1.00 37.42 ? 96   ARG A O   1 
ATOM   709  C CB  . ARG A 1 96  ? -110.211 -36.682 53.468 1.00 40.66 ? 96   ARG A CB  1 
ATOM   710  C CG  . ARG A 1 96  ? -111.124 -35.979 52.474 1.00 45.31 ? 96   ARG A CG  1 
ATOM   711  C CD  . ARG A 1 96  ? -111.852 -34.819 53.143 1.00 51.13 ? 96   ARG A CD  1 
ATOM   712  N NE  . ARG A 1 96  ? -112.494 -33.937 52.172 1.00 58.26 ? 96   ARG A NE  1 
ATOM   713  C CZ  . ARG A 1 96  ? -113.138 -32.818 52.491 1.00 59.61 ? 96   ARG A CZ  1 
ATOM   714  N NH1 . ARG A 1 96  ? -113.232 -32.446 53.761 1.00 60.08 ? 96   ARG A NH1 1 
ATOM   715  N NH2 . ARG A 1 96  ? -113.672 -32.061 51.540 1.00 60.69 ? 96   ARG A NH2 1 
ATOM   716  N N   . GLN A 1 97  ? -107.514 -37.898 54.781 1.00 36.60 ? 97   GLN A N   1 
ATOM   717  C CA  . GLN A 1 97  ? -106.744 -38.182 55.988 1.00 35.29 ? 97   GLN A CA  1 
ATOM   718  C C   . GLN A 1 97  ? -105.273 -37.930 55.658 1.00 33.36 ? 97   GLN A C   1 
ATOM   719  O O   . GLN A 1 97  ? -104.470 -38.862 55.574 1.00 33.01 ? 97   GLN A O   1 
ATOM   720  C CB  . GLN A 1 97  ? -106.979 -39.638 56.425 1.00 35.73 ? 97   GLN A CB  1 
ATOM   721  C CG  . GLN A 1 97  ? -108.384 -39.879 56.995 1.00 40.93 ? 97   GLN A CG  1 
ATOM   722  C CD  . GLN A 1 97  ? -108.719 -41.357 57.218 1.00 44.70 ? 97   GLN A CD  1 
ATOM   723  O OE1 . GLN A 1 97  ? -108.000 -42.090 57.917 1.00 43.05 ? 97   GLN A OE1 1 
ATOM   724  N NE2 . GLN A 1 97  ? -109.827 -41.797 56.628 1.00 44.99 ? 97   GLN A NE2 1 
ATOM   725  N N   . ASP A 1 98  ? -104.932 -36.656 55.467 1.00 32.65 ? 98   ASP A N   1 
ATOM   726  C CA  . ASP A 1 98  ? -103.572 -36.264 55.102 1.00 33.75 ? 98   ASP A CA  1 
ATOM   727  C C   . ASP A 1 98  ? -102.838 -35.392 56.125 1.00 33.82 ? 98   ASP A C   1 
ATOM   728  O O   . ASP A 1 98  ? -101.825 -34.769 55.804 1.00 33.86 ? 98   ASP A O   1 
ATOM   729  C CB  . ASP A 1 98  ? -103.587 -35.565 53.733 1.00 31.80 ? 98   ASP A CB  1 
ATOM   730  C CG  . ASP A 1 98  ? -104.347 -34.247 53.755 1.00 35.94 ? 98   ASP A CG  1 
ATOM   731  O OD1 . ASP A 1 98  ? -105.283 -34.108 54.568 1.00 34.26 ? 98   ASP A OD1 1 
ATOM   732  O OD2 . ASP A 1 98  ? -104.017 -33.351 52.950 1.00 35.26 ? 98   ASP A OD2 1 
ATOM   733  N N   . LYS A 1 99  ? -103.336 -35.363 57.358 1.00 33.37 ? 99   LYS A N   1 
ATOM   734  C CA  . LYS A 1 99  ? -102.706 -34.588 58.419 1.00 33.99 ? 99   LYS A CA  1 
ATOM   735  C C   . LYS A 1 99  ? -103.290 -35.022 59.765 1.00 34.92 ? 99   LYS A C   1 
ATOM   736  O O   . LYS A 1 99  ? -104.374 -35.602 59.814 1.00 34.43 ? 99   LYS A O   1 
ATOM   737  C CB  . LYS A 1 99  ? -102.936 -33.089 58.194 1.00 34.17 ? 99   LYS A CB  1 
ATOM   738  C CG  . LYS A 1 99  ? -104.392 -32.650 58.324 1.00 37.54 ? 99   LYS A CG  1 
ATOM   739  C CD  . LYS A 1 99  ? -104.576 -31.158 58.078 1.00 39.95 ? 99   LYS A CD  1 
ATOM   740  C CE  . LYS A 1 99  ? -104.236 -30.772 56.645 1.00 43.70 ? 99   LYS A CE  1 
ATOM   741  N NZ  . LYS A 1 99  ? -104.459 -29.308 56.386 1.00 48.27 ? 99   LYS A NZ  1 
ATOM   742  N N   . LYS A 1 100 ? -102.576 -34.757 60.854 1.00 35.87 ? 100  LYS A N   1 
ATOM   743  C CA  . LYS A 1 100 ? -103.063 -35.148 62.175 1.00 37.67 ? 100  LYS A CA  1 
ATOM   744  C C   . LYS A 1 100 ? -104.198 -34.260 62.672 1.00 39.70 ? 100  LYS A C   1 
ATOM   745  O O   . LYS A 1 100 ? -105.088 -34.725 63.381 1.00 37.76 ? 100  LYS A O   1 
ATOM   746  C CB  . LYS A 1 100 ? -101.923 -35.125 63.202 1.00 36.80 ? 100  LYS A CB  1 
ATOM   747  C CG  . LYS A 1 100 ? -100.883 -36.227 63.032 1.00 35.01 ? 100  LYS A CG  1 
ATOM   748  C CD  . LYS A 1 100 ? -99.867  -36.187 64.157 1.00 32.12 ? 100  LYS A CD  1 
ATOM   749  C CE  . LYS A 1 100 ? -98.771  -37.193 63.919 1.00 35.04 ? 100  LYS A CE  1 
ATOM   750  N NZ  . LYS A 1 100 ? -97.694  -37.080 64.945 1.00 35.24 ? 100  LYS A NZ  1 
ATOM   751  N N   . ASP A 1 101 ? -104.152 -32.982 62.304 1.00 44.28 ? 101  ASP A N   1 
ATOM   752  C CA  . ASP A 1 101 ? -105.172 -32.015 62.707 1.00 47.65 ? 101  ASP A CA  1 
ATOM   753  C C   . ASP A 1 101 ? -105.306 -31.912 64.227 1.00 49.06 ? 101  ASP A C   1 
ATOM   754  O O   . ASP A 1 101 ? -106.424 -31.883 64.745 1.00 48.19 ? 101  ASP A O   1 
ATOM   755  C CB  . ASP A 1 101 ? -106.529 -32.404 62.114 1.00 49.75 ? 101  ASP A CB  1 
ATOM   756  C CG  . ASP A 1 101 ? -107.419 -31.200 61.852 1.00 52.11 ? 101  ASP A CG  1 
ATOM   757  O OD1 . ASP A 1 101 ? -107.038 -30.359 61.012 1.00 52.12 ? 101  ASP A OD1 1 
ATOM   758  O OD2 . ASP A 1 101 ? -108.497 -31.090 62.477 1.00 55.71 ? 101  ASP A OD2 1 
ATOM   759  N N   . LYS A 1 102 ? -104.175 -31.849 64.931 1.00 49.55 ? 102  LYS A N   1 
ATOM   760  C CA  . LYS A 1 102 ? -104.158 -31.757 66.396 1.00 51.31 ? 102  LYS A CA  1 
ATOM   761  C C   . LYS A 1 102 ? -104.793 -32.947 67.106 1.00 50.09 ? 102  LYS A C   1 
ATOM   762  O O   . LYS A 1 102 ? -105.525 -32.775 68.081 1.00 52.23 ? 102  LYS A O   1 
ATOM   763  C CB  . LYS A 1 102 ? -104.850 -30.477 66.884 1.00 53.94 ? 102  LYS A CB  1 
ATOM   764  C CG  . LYS A 1 102 ? -104.203 -29.191 66.402 1.00 59.72 ? 102  LYS A CG  1 
ATOM   765  C CD  . LYS A 1 102 ? -104.270 -28.085 67.449 1.00 63.52 ? 102  LYS A CD  1 
ATOM   766  C CE  . LYS A 1 102 ? -105.700 -27.657 67.729 1.00 66.48 ? 102  LYS A CE  1 
ATOM   767  N NZ  . LYS A 1 102 ? -105.749 -26.527 68.705 1.00 68.80 ? 102  LYS A NZ  1 
ATOM   768  N N   . SER A 1 103 ? -104.513 -34.150 66.622 1.00 48.03 ? 103  SER A N   1 
ATOM   769  C CA  . SER A 1 103 ? -105.050 -35.359 67.237 1.00 44.22 ? 103  SER A CA  1 
ATOM   770  C C   . SER A 1 103 ? -104.103 -36.521 67.013 1.00 41.74 ? 103  SER A C   1 
ATOM   771  O O   . SER A 1 103 ? -103.186 -36.428 66.200 1.00 42.15 ? 103  SER A O   1 
ATOM   772  C CB  . SER A 1 103 ? -106.405 -35.688 66.635 1.00 45.95 ? 103  SER A CB  1 
ATOM   773  O OG  . SER A 1 103 ? -107.281 -34.586 66.780 1.00 48.72 ? 103  SER A OG  1 
ATOM   774  N N   . ARG A 1 104 ? -104.312 -37.603 67.754 1.00 39.64 ? 104  ARG A N   1 
ATOM   775  C CA  . ARG A 1 104 ? -103.493 -38.799 67.609 1.00 39.19 ? 104  ARG A CA  1 
ATOM   776  C C   . ARG A 1 104 ? -104.155 -39.619 66.521 1.00 36.86 ? 104  ARG A C   1 
ATOM   777  O O   . ARG A 1 104 ? -104.681 -40.710 66.755 1.00 36.93 ? 104  ARG A O   1 
ATOM   778  C CB  . ARG A 1 104 ? -103.446 -39.601 68.909 1.00 39.47 ? 104  ARG A CB  1 
ATOM   779  C CG  . ARG A 1 104 ? -102.460 -39.049 69.906 1.00 42.98 ? 104  ARG A CG  1 
ATOM   780  C CD  . ARG A 1 104 ? -102.487 -39.848 71.177 1.00 42.75 ? 104  ARG A CD  1 
ATOM   781  N NE  . ARG A 1 104 ? -103.662 -39.519 71.971 1.00 42.67 ? 104  ARG A NE  1 
ATOM   782  C CZ  . ARG A 1 104 ? -103.665 -38.626 72.947 1.00 40.66 ? 104  ARG A CZ  1 
ATOM   783  N NH1 . ARG A 1 104 ? -102.558 -37.976 73.251 1.00 41.36 ? 104  ARG A NH1 1 
ATOM   784  N NH2 . ARG A 1 104 ? -104.777 -38.383 73.618 1.00 46.94 ? 104  ARG A NH2 1 
ATOM   785  N N   . ALA A 1 105 ? -104.125 -39.054 65.323 1.00 33.94 ? 105  ALA A N   1 
ATOM   786  C CA  . ALA A 1 105 ? -104.737 -39.655 64.166 1.00 33.51 ? 105  ALA A CA  1 
ATOM   787  C C   . ALA A 1 105 ? -103.716 -40.143 63.170 1.00 33.39 ? 105  ALA A C   1 
ATOM   788  O O   . ALA A 1 105 ? -102.555 -39.698 63.165 1.00 32.13 ? 105  ALA A O   1 
ATOM   789  C CB  . ALA A 1 105 ? -105.674 -38.647 63.509 1.00 34.47 ? 105  ALA A CB  1 
ATOM   790  N N   . PRO A 1 106 ? -104.134 -41.072 62.296 1.00 31.38 ? 106  PRO A N   1 
ATOM   791  C CA  . PRO A 1 106 ? -103.248 -41.621 61.274 1.00 31.95 ? 106  PRO A CA  1 
ATOM   792  C C   . PRO A 1 106 ? -103.144 -40.616 60.125 1.00 31.28 ? 106  PRO A C   1 
ATOM   793  O O   . PRO A 1 106 ? -104.013 -39.759 59.948 1.00 33.58 ? 106  PRO A O   1 
ATOM   794  C CB  . PRO A 1 106 ? -103.972 -42.896 60.840 1.00 32.87 ? 106  PRO A CB  1 
ATOM   795  C CG  . PRO A 1 106 ? -105.414 -42.511 60.936 1.00 31.12 ? 106  PRO A CG  1 
ATOM   796  C CD  . PRO A 1 106 ? -105.449 -41.739 62.252 1.00 31.94 ? 106  PRO A CD  1 
ATOM   797  N N   . ILE A 1 107 ? -102.051 -40.659 59.376 1.00 31.54 ? 107  ILE A N   1 
ATOM   798  C CA  . ILE A 1 107 ? -101.932 -39.810 58.191 1.00 29.61 ? 107  ILE A CA  1 
ATOM   799  C C   . ILE A 1 107 ? -102.097 -40.881 57.113 1.00 28.21 ? 107  ILE A C   1 
ATOM   800  O O   . ILE A 1 107 ? -101.153 -41.233 56.399 1.00 29.68 ? 107  ILE A O   1 
ATOM   801  C CB  . ILE A 1 107 ? -100.564 -39.109 58.093 1.00 28.29 ? 107  ILE A CB  1 
ATOM   802  C CG1 . ILE A 1 107 ? -100.387 -38.124 59.264 1.00 28.58 ? 107  ILE A CG1 1 
ATOM   803  C CG2 . ILE A 1 107 ? -100.515 -38.295 56.803 1.00 30.22 ? 107  ILE A CG2 1 
ATOM   804  C CD1 . ILE A 1 107 ? -99.135  -37.257 59.163 1.00 22.84 ? 107  ILE A CD1 1 
ATOM   805  N N   . SER A 1 108 ? -103.312 -41.431 57.091 1.00 25.38 ? 108  SER A N   1 
ATOM   806  C CA  . SER A 1 108 ? -103.725 -42.495 56.191 1.00 24.46 ? 108  SER A CA  1 
ATOM   807  C C   . SER A 1 108 ? -103.331 -42.325 54.740 1.00 24.09 ? 108  SER A C   1 
ATOM   808  O O   . SER A 1 108 ? -103.078 -43.313 54.048 1.00 22.24 ? 108  SER A O   1 
ATOM   809  C CB  . SER A 1 108 ? -105.243 -42.704 56.246 1.00 21.45 ? 108  SER A CB  1 
ATOM   810  O OG  . SER A 1 108 ? -105.664 -43.103 57.530 1.00 24.56 ? 108  SER A OG  1 
ATOM   811  N N   . ALA A 1 109 ? -103.295 -41.087 54.263 1.00 23.87 ? 109  ALA A N   1 
ATOM   812  C CA  . ALA A 1 109 ? -102.946 -40.871 52.867 1.00 23.51 ? 109  ALA A CA  1 
ATOM   813  C C   . ALA A 1 109 ? -101.467 -41.199 52.641 1.00 22.87 ? 109  ALA A C   1 
ATOM   814  O O   . ALA A 1 109 ? -101.081 -41.630 51.555 1.00 24.06 ? 109  ALA A O   1 
ATOM   815  C CB  . ALA A 1 109 ? -103.264 -39.431 52.452 1.00 20.44 ? 109  ALA A CB  1 
ATOM   816  N N   . LYS A 1 110 ? -100.644 -41.003 53.668 1.00 23.26 ? 110  LYS A N   1 
ATOM   817  C CA  . LYS A 1 110 ? -99.228  -41.321 53.563 1.00 24.40 ? 110  LYS A CA  1 
ATOM   818  C C   . LYS A 1 110 ? -99.075  -42.834 53.700 1.00 24.77 ? 110  LYS A C   1 
ATOM   819  O O   . LYS A 1 110 ? -98.165  -43.427 53.130 1.00 26.48 ? 110  LYS A O   1 
ATOM   820  C CB  . LYS A 1 110 ? -98.420  -40.619 54.659 1.00 25.07 ? 110  LYS A CB  1 
ATOM   821  C CG  . LYS A 1 110 ? -96.954  -41.064 54.727 1.00 23.52 ? 110  LYS A CG  1 
ATOM   822  C CD  . LYS A 1 110 ? -96.258  -40.829 53.398 1.00 26.90 ? 110  LYS A CD  1 
ATOM   823  C CE  . LYS A 1 110 ? -94.739  -40.843 53.533 1.00 30.00 ? 110  LYS A CE  1 
ATOM   824  N NZ  . LYS A 1 110 ? -94.226  -42.200 53.781 1.00 39.13 ? 110  LYS A NZ  1 
ATOM   825  N N   . LEU A 1 111 ? -99.961  -43.460 54.467 1.00 25.32 ? 111  LEU A N   1 
ATOM   826  C CA  . LEU A 1 111 ? -99.893  -44.912 54.627 1.00 26.05 ? 111  LEU A CA  1 
ATOM   827  C C   . LEU A 1 111 ? -100.163 -45.489 53.236 1.00 25.86 ? 111  LEU A C   1 
ATOM   828  O O   . LEU A 1 111 ? -99.412  -46.332 52.739 1.00 25.39 ? 111  LEU A O   1 
ATOM   829  C CB  . LEU A 1 111 ? -100.976 -45.401 55.585 1.00 26.28 ? 111  LEU A CB  1 
ATOM   830  C CG  . LEU A 1 111 ? -100.869 -46.749 56.311 1.00 30.77 ? 111  LEU A CG  1 
ATOM   831  C CD1 . LEU A 1 111 ? -102.288 -47.311 56.458 1.00 29.37 ? 111  LEU A CD1 1 
ATOM   832  C CD2 . LEU A 1 111 ? -99.983  -47.732 55.580 1.00 28.74 ? 111  LEU A CD2 1 
ATOM   833  N N   . VAL A 1 112 ? -101.237 -45.009 52.609 1.00 23.42 ? 112  VAL A N   1 
ATOM   834  C CA  . VAL A 1 112 ? -101.627 -45.477 51.286 1.00 23.46 ? 112  VAL A CA  1 
ATOM   835  C C   . VAL A 1 112 ? -100.491 -45.269 50.278 1.00 23.02 ? 112  VAL A C   1 
ATOM   836  O O   . VAL A 1 112 ? -100.184 -46.149 49.481 1.00 25.25 ? 112  VAL A O   1 
ATOM   837  C CB  . VAL A 1 112 ? -102.902 -44.746 50.803 1.00 21.10 ? 112  VAL A CB  1 
ATOM   838  C CG1 . VAL A 1 112 ? -103.256 -45.181 49.362 1.00 23.22 ? 112  VAL A CG1 1 
ATOM   839  C CG2 . VAL A 1 112 ? -104.056 -45.068 51.746 1.00 22.09 ? 112  VAL A CG2 1 
ATOM   840  N N   . ALA A 1 113 ? -99.865  -44.103 50.320 1.00 22.74 ? 113  ALA A N   1 
ATOM   841  C CA  . ALA A 1 113 ? -98.763  -43.818 49.410 1.00 23.95 ? 113  ALA A CA  1 
ATOM   842  C C   . ALA A 1 113 ? -97.668  -44.868 49.620 1.00 24.40 ? 113  ALA A C   1 
ATOM   843  O O   . ALA A 1 113 ? -97.122  -45.409 48.650 1.00 24.52 ? 113  ALA A O   1 
ATOM   844  C CB  . ALA A 1 113 ? -98.219  -42.418 49.675 1.00 19.11 ? 113  ALA A CB  1 
ATOM   845  N N   . ASN A 1 114 ? -97.358  -45.160 50.884 1.00 23.25 ? 114  ASN A N   1 
ATOM   846  C CA  . ASN A 1 114 ? -96.327  -46.144 51.203 1.00 22.85 ? 114  ASN A CA  1 
ATOM   847  C C   . ASN A 1 114 ? -96.730  -47.548 50.754 1.00 23.27 ? 114  ASN A C   1 
ATOM   848  O O   . ASN A 1 114 ? -95.890  -48.311 50.296 1.00 25.84 ? 114  ASN A O   1 
ATOM   849  C CB  . ASN A 1 114 ? -96.019  -46.168 52.707 1.00 22.55 ? 114  ASN A CB  1 
ATOM   850  C CG  . ASN A 1 114 ? -95.130  -45.003 53.165 1.00 27.04 ? 114  ASN A CG  1 
ATOM   851  O OD1 . ASN A 1 114 ? -94.389  -44.402 52.381 1.00 27.48 ? 114  ASN A OD1 1 
ATOM   852  N ND2 . ASN A 1 114 ? -95.178  -44.715 54.453 1.00 23.40 ? 114  ASN A ND2 1 
ATOM   853  N N   . MET A 1 115 ? -98.007  -47.894 50.875 1.00 21.82 ? 115  MET A N   1 
ATOM   854  C CA  . MET A 1 115 ? -98.448  -49.230 50.471 1.00 24.39 ? 115  MET A CA  1 
ATOM   855  C C   . MET A 1 115 ? -98.334  -49.413 48.970 1.00 22.56 ? 115  MET A C   1 
ATOM   856  O O   . MET A 1 115 ? -97.925  -50.469 48.493 1.00 23.97 ? 115  MET A O   1 
ATOM   857  C CB  . MET A 1 115 ? -99.885  -49.480 50.926 1.00 25.09 ? 115  MET A CB  1 
ATOM   858  C CG  . MET A 1 115 ? -100.034 -49.428 52.432 1.00 30.23 ? 115  MET A CG  1 
ATOM   859  S SD  . MET A 1 115 ? -101.652 -49.919 52.986 1.00 39.36 ? 115  MET A SD  1 
ATOM   860  C CE  . MET A 1 115 ? -102.551 -48.471 52.684 1.00 33.39 ? 115  MET A CE  1 
ATOM   861  N N   . LEU A 1 116 ? -98.695  -48.375 48.228 1.00 23.14 ? 116  LEU A N   1 
ATOM   862  C CA  . LEU A 1 116 ? -98.606  -48.400 46.772 1.00 23.67 ? 116  LEU A CA  1 
ATOM   863  C C   . LEU A 1 116 ? -97.145  -48.536 46.356 1.00 25.18 ? 116  LEU A C   1 
ATOM   864  O O   . LEU A 1 116 ? -96.811  -49.285 45.440 1.00 25.50 ? 116  LEU A O   1 
ATOM   865  C CB  . LEU A 1 116 ? -99.169  -47.095 46.200 1.00 24.55 ? 116  LEU A CB  1 
ATOM   866  C CG  . LEU A 1 116 ? -100.688 -46.941 46.175 1.00 24.33 ? 116  LEU A CG  1 
ATOM   867  C CD1 . LEU A 1 116 ? -101.072 -45.473 46.023 1.00 24.00 ? 116  LEU A CD1 1 
ATOM   868  C CD2 . LEU A 1 116 ? -101.239 -47.773 45.019 1.00 23.54 ? 116  LEU A CD2 1 
ATOM   869  N N   . SER A 1 117 ? -96.274  -47.794 47.032 1.00 23.58 ? 117  SER A N   1 
ATOM   870  C CA  . SER A 1 117 ? -94.862  -47.842 46.718 1.00 28.02 ? 117  SER A CA  1 
ATOM   871  C C   . SER A 1 117 ? -94.290  -49.243 46.960 1.00 28.88 ? 117  SER A C   1 
ATOM   872  O O   . SER A 1 117 ? -93.710  -49.848 46.049 1.00 28.24 ? 117  SER A O   1 
ATOM   873  C CB  . SER A 1 117 ? -94.107  -46.799 47.549 1.00 30.92 ? 117  SER A CB  1 
ATOM   874  O OG  . SER A 1 117 ? -94.668  -45.504 47.344 1.00 33.65 ? 117  SER A OG  1 
ATOM   875  N N   . VAL A 1 118 ? -94.476  -49.775 48.166 1.00 26.14 ? 118  VAL A N   1 
ATOM   876  C CA  . VAL A 1 118 ? -93.956  -51.105 48.477 1.00 26.00 ? 118  VAL A CA  1 
ATOM   877  C C   . VAL A 1 118 ? -94.666  -52.186 47.660 1.00 26.79 ? 118  VAL A C   1 
ATOM   878  O O   . VAL A 1 118 ? -94.176  -53.299 47.544 1.00 29.58 ? 118  VAL A O   1 
ATOM   879  C CB  . VAL A 1 118 ? -94.082  -51.438 49.998 1.00 27.10 ? 118  VAL A CB  1 
ATOM   880  C CG1 . VAL A 1 118 ? -95.495  -51.961 50.338 1.00 27.18 ? 118  VAL A CG1 1 
ATOM   881  C CG2 . VAL A 1 118 ? -93.040  -52.469 50.378 1.00 28.60 ? 118  VAL A CG2 1 
ATOM   882  N N   . ALA A 1 119 ? -95.826  -51.876 47.096 1.00 26.52 ? 119  ALA A N   1 
ATOM   883  C CA  . ALA A 1 119 ? -96.519  -52.878 46.289 1.00 26.55 ? 119  ALA A CA  1 
ATOM   884  C C   . ALA A 1 119 ? -95.774  -52.952 44.962 1.00 26.79 ? 119  ALA A C   1 
ATOM   885  O O   . ALA A 1 119 ? -95.925  -53.912 44.213 1.00 27.75 ? 119  ALA A O   1 
ATOM   886  C CB  . ALA A 1 119 ? -97.978  -52.478 46.052 1.00 25.78 ? 119  ALA A CB  1 
ATOM   887  N N   . GLY A 1 120 ? -94.975  -51.924 44.678 1.00 25.96 ? 120  GLY A N   1 
ATOM   888  C CA  . GLY A 1 120 ? -94.210  -51.900 43.444 1.00 24.96 ? 120  GLY A CA  1 
ATOM   889  C C   . GLY A 1 120 ? -94.594  -50.847 42.407 1.00 25.14 ? 120  GLY A C   1 
ATOM   890  O O   . GLY A 1 120 ? -94.114  -50.903 41.281 1.00 25.77 ? 120  GLY A O   1 
ATOM   891  N N   . ALA A 1 121 ? -95.447  -49.890 42.761 1.00 24.24 ? 121  ALA A N   1 
ATOM   892  C CA  . ALA A 1 121 ? -95.845  -48.844 41.812 1.00 23.57 ? 121  ALA A CA  1 
ATOM   893  C C   . ALA A 1 121 ? -94.665  -47.944 41.495 1.00 24.19 ? 121  ALA A C   1 
ATOM   894  O O   . ALA A 1 121 ? -94.012  -47.438 42.408 1.00 25.34 ? 121  ALA A O   1 
ATOM   895  C CB  . ALA A 1 121 ? -96.966  -48.010 42.393 1.00 22.88 ? 121  ALA A CB  1 
ATOM   896  N N   . ASP A 1 122 ? -94.403  -47.731 40.207 1.00 21.90 ? 122  ASP A N   1 
ATOM   897  C CA  . ASP A 1 122 ? -93.301  -46.874 39.774 1.00 22.85 ? 122  ASP A CA  1 
ATOM   898  C C   . ASP A 1 122 ? -93.748  -45.454 39.480 1.00 23.23 ? 122  ASP A C   1 
ATOM   899  O O   . ASP A 1 122 ? -92.926  -44.537 39.407 1.00 24.39 ? 122  ASP A O   1 
ATOM   900  C CB  . ASP A 1 122 ? -92.677  -47.403 38.487 1.00 22.85 ? 122  ASP A CB  1 
ATOM   901  C CG  . ASP A 1 122 ? -92.098  -48.776 38.645 1.00 26.47 ? 122  ASP A CG  1 
ATOM   902  O OD1 . ASP A 1 122 ? -92.444  -49.659 37.827 1.00 30.87 ? 122  ASP A OD1 1 
ATOM   903  O OD2 . ASP A 1 122 ? -91.300  -48.973 39.584 1.00 27.23 ? 122  ASP A OD2 1 
ATOM   904  N N   . HIS A 1 123 ? -95.047  -45.272 39.298 1.00 21.26 ? 123  HIS A N   1 
ATOM   905  C CA  . HIS A 1 123 ? -95.567  -43.963 38.922 1.00 25.20 ? 123  HIS A CA  1 
ATOM   906  C C   . HIS A 1 123 ? -97.035  -43.885 39.289 1.00 24.35 ? 123  HIS A C   1 
ATOM   907  O O   . HIS A 1 123 ? -97.738  -44.895 39.270 1.00 25.69 ? 123  HIS A O   1 
ATOM   908  C CB  . HIS A 1 123 ? -95.414  -43.801 37.402 1.00 27.46 ? 123  HIS A CB  1 
ATOM   909  C CG  . HIS A 1 123 ? -95.831  -42.465 36.874 1.00 30.49 ? 123  HIS A CG  1 
ATOM   910  N ND1 . HIS A 1 123 ? -96.333  -42.296 35.600 1.00 34.05 ? 123  HIS A ND1 1 
ATOM   911  C CD2 . HIS A 1 123 ? -95.754  -41.222 37.409 1.00 31.29 ? 123  HIS A CD2 1 
ATOM   912  C CE1 . HIS A 1 123 ? -96.540  -41.014 35.372 1.00 32.59 ? 123  HIS A CE1 1 
ATOM   913  N NE2 . HIS A 1 123 ? -96.195  -40.340 36.457 1.00 31.41 ? 123  HIS A NE2 1 
ATOM   914  N N   . ILE A 1 124 ? -97.498  -42.690 39.626 1.00 24.40 ? 124  ILE A N   1 
ATOM   915  C CA  . ILE A 1 124 ? -98.901  -42.512 39.962 1.00 24.88 ? 124  ILE A CA  1 
ATOM   916  C C   . ILE A 1 124 ? -99.504  -41.448 39.059 1.00 26.59 ? 124  ILE A C   1 
ATOM   917  O O   . ILE A 1 124 ? -98.867  -40.438 38.761 1.00 26.65 ? 124  ILE A O   1 
ATOM   918  C CB  . ILE A 1 124 ? -99.113  -42.042 41.433 1.00 25.18 ? 124  ILE A CB  1 
ATOM   919  C CG1 . ILE A 1 124 ? -98.459  -43.011 42.437 1.00 23.13 ? 124  ILE A CG1 1 
ATOM   920  C CG2 . ILE A 1 124 ? -100.608 -41.926 41.706 1.00 22.58 ? 124  ILE A CG2 1 
ATOM   921  C CD1 . ILE A 1 124 ? -99.121  -44.388 42.528 1.00 22.19 ? 124  ILE A CD1 1 
ATOM   922  N N   . ILE A 1 125 ? -100.730 -41.688 38.611 1.00 28.10 ? 125  ILE A N   1 
ATOM   923  C CA  . ILE A 1 125 ? -101.451 -40.721 37.798 1.00 28.95 ? 125  ILE A CA  1 
ATOM   924  C C   . ILE A 1 125 ? -102.777 -40.573 38.517 1.00 29.18 ? 125  ILE A C   1 
ATOM   925  O O   . ILE A 1 125 ? -103.521 -41.540 38.665 1.00 29.82 ? 125  ILE A O   1 
ATOM   926  C CB  . ILE A 1 125 ? -101.698 -41.220 36.344 1.00 29.58 ? 125  ILE A CB  1 
ATOM   927  C CG1 . ILE A 1 125 ? -100.368 -41.281 35.582 1.00 27.46 ? 125  ILE A CG1 1 
ATOM   928  C CG2 . ILE A 1 125 ? -102.672 -40.282 35.629 1.00 26.25 ? 125  ILE A CG2 1 
ATOM   929  C CD1 . ILE A 1 125 ? -100.479 -41.873 34.197 1.00 25.26 ? 125  ILE A CD1 1 
ATOM   930  N N   . THR A 1 126 ? -103.066 -39.369 38.985 1.00 30.42 ? 126  THR A N   1 
ATOM   931  C CA  . THR A 1 126 ? -104.310 -39.139 39.695 1.00 31.32 ? 126  THR A CA  1 
ATOM   932  C C   . THR A 1 126 ? -104.904 -37.809 39.257 1.00 32.32 ? 126  THR A C   1 
ATOM   933  O O   . THR A 1 126 ? -104.307 -37.100 38.438 1.00 32.33 ? 126  THR A O   1 
ATOM   934  C CB  . THR A 1 126 ? -104.064 -39.121 41.216 1.00 31.84 ? 126  THR A CB  1 
ATOM   935  O OG1 . THR A 1 126 ? -105.319 -39.031 41.902 1.00 31.59 ? 126  THR A OG1 1 
ATOM   936  C CG2 . THR A 1 126 ? -103.173 -37.935 41.599 1.00 29.17 ? 126  THR A CG2 1 
ATOM   937  N N   . MET A 1 127 ? -106.079 -37.479 39.791 1.00 31.00 ? 127  MET A N   1 
ATOM   938  C CA  . MET A 1 127 ? -106.738 -36.216 39.462 1.00 33.10 ? 127  MET A CA  1 
ATOM   939  C C   . MET A 1 127 ? -107.233 -35.457 40.699 1.00 32.87 ? 127  MET A C   1 
ATOM   940  O O   . MET A 1 127 ? -107.888 -36.036 41.571 1.00 30.82 ? 127  MET A O   1 
ATOM   941  C CB  . MET A 1 127 ? -107.905 -36.454 38.501 1.00 32.70 ? 127  MET A CB  1 
ATOM   942  C CG  . MET A 1 127 ? -108.651 -35.173 38.160 1.00 37.06 ? 127  MET A CG  1 
ATOM   943  S SD  . MET A 1 127 ? -109.755 -35.312 36.728 1.00 44.25 ? 127  MET A SD  1 
ATOM   944  C CE  . MET A 1 127 ? -108.558 -35.565 35.438 1.00 38.70 ? 127  MET A CE  1 
ATOM   945  N N   . ASP A 1 128 ? -106.915 -34.162 40.743 1.00 33.80 ? 128  ASP A N   1 
ATOM   946  C CA  . ASP A 1 128 ? -107.292 -33.269 41.831 1.00 35.98 ? 128  ASP A CA  1 
ATOM   947  C C   . ASP A 1 128 ? -107.091 -33.844 43.227 1.00 36.31 ? 128  ASP A C   1 
ATOM   948  O O   . ASP A 1 128 ? -108.062 -34.107 43.949 1.00 35.34 ? 128  ASP A O   1 
ATOM   949  C CB  . ASP A 1 128 ? -108.749 -32.806 41.670 1.00 38.87 ? 128  ASP A CB  1 
ATOM   950  C CG  . ASP A 1 128 ? -108.930 -31.842 40.500 1.00 42.88 ? 128  ASP A CG  1 
ATOM   951  O OD1 . ASP A 1 128 ? -110.028 -31.827 39.890 1.00 47.25 ? 128  ASP A OD1 1 
ATOM   952  O OD2 . ASP A 1 128 ? -107.977 -31.096 40.193 1.00 40.83 ? 128  ASP A OD2 1 
ATOM   953  N N   . LEU A 1 129 ? -105.830 -34.060 43.601 1.00 34.53 ? 129  LEU A N   1 
ATOM   954  C CA  . LEU A 1 129 ? -105.516 -34.563 44.938 1.00 35.01 ? 129  LEU A CA  1 
ATOM   955  C C   . LEU A 1 129 ? -106.139 -33.587 45.924 1.00 35.07 ? 129  LEU A C   1 
ATOM   956  O O   . LEU A 1 129 ? -106.053 -32.370 45.715 1.00 35.44 ? 129  LEU A O   1 
ATOM   957  C CB  . LEU A 1 129 ? -104.003 -34.588 45.158 1.00 33.61 ? 129  LEU A CB  1 
ATOM   958  C CG  . LEU A 1 129 ? -103.246 -35.618 44.329 1.00 32.72 ? 129  LEU A CG  1 
ATOM   959  C CD1 . LEU A 1 129 ? -101.767 -35.382 44.438 1.00 31.10 ? 129  LEU A CD1 1 
ATOM   960  C CD2 . LEU A 1 129 ? -103.625 -37.017 44.817 1.00 32.85 ? 129  LEU A CD2 1 
ATOM   961  N N   . HIS A 1 130 ? -106.747 -34.098 46.995 1.00 33.78 ? 130  HIS A N   1 
ATOM   962  C CA  . HIS A 1 130 ? -107.382 -33.223 47.981 1.00 33.34 ? 130  HIS A CA  1 
ATOM   963  C C   . HIS A 1 130 ? -106.439 -32.107 48.411 1.00 32.68 ? 130  HIS A C   1 
ATOM   964  O O   . HIS A 1 130 ? -106.875 -31.011 48.750 1.00 33.30 ? 130  HIS A O   1 
ATOM   965  C CB  . HIS A 1 130 ? -107.835 -34.015 49.207 1.00 35.97 ? 130  HIS A CB  1 
ATOM   966  C CG  . HIS A 1 130 ? -108.535 -33.183 50.237 1.00 38.01 ? 130  HIS A CG  1 
ATOM   967  N ND1 . HIS A 1 130 ? -108.008 -32.950 51.489 1.00 40.16 ? 130  HIS A ND1 1 
ATOM   968  C CD2 . HIS A 1 130 ? -109.732 -32.551 50.215 1.00 37.64 ? 130  HIS A CD2 1 
ATOM   969  C CE1 . HIS A 1 130 ? -108.849 -32.217 52.192 1.00 38.89 ? 130  HIS A CE1 1 
ATOM   970  N NE2 . HIS A 1 130 ? -109.906 -31.962 51.441 1.00 39.62 ? 130  HIS A NE2 1 
ATOM   971  N N   . ALA A 1 131 ? -105.144 -32.395 48.394 1.00 31.03 ? 131  ALA A N   1 
ATOM   972  C CA  . ALA A 1 131 ? -104.129 -31.414 48.746 1.00 30.93 ? 131  ALA A CA  1 
ATOM   973  C C   . ALA A 1 131 ? -102.872 -31.708 47.927 1.00 31.91 ? 131  ALA A C   1 
ATOM   974  O O   . ALA A 1 131 ? -102.391 -32.839 47.902 1.00 28.48 ? 131  ALA A O   1 
ATOM   975  C CB  . ALA A 1 131 ? -103.818 -31.490 50.230 1.00 31.35 ? 131  ALA A CB  1 
ATOM   976  N N   . SER A 1 132 ? -102.357 -30.685 47.253 1.00 32.37 ? 132  SER A N   1 
ATOM   977  C CA  . SER A 1 132 ? -101.158 -30.825 46.436 1.00 34.36 ? 132  SER A CA  1 
ATOM   978  C C   . SER A 1 132 ? -100.014 -31.522 47.189 1.00 33.44 ? 132  SER A C   1 
ATOM   979  O O   . SER A 1 132 ? -99.246  -32.287 46.599 1.00 31.57 ? 132  SER A O   1 
ATOM   980  C CB  . SER A 1 132 ? -100.681 -29.449 45.977 1.00 35.05 ? 132  SER A CB  1 
ATOM   981  O OG  . SER A 1 132 ? -101.639 -28.818 45.153 1.00 43.99 ? 132  SER A OG  1 
ATOM   982  N N   . GLN A 1 133 ? -99.900  -31.250 48.486 1.00 30.94 ? 133  GLN A N   1 
ATOM   983  C CA  . GLN A 1 133 ? -98.829  -31.837 49.276 1.00 29.34 ? 133  GLN A CA  1 
ATOM   984  C C   . GLN A 1 133 ? -98.796  -33.360 49.232 1.00 30.94 ? 133  GLN A C   1 
ATOM   985  O O   . GLN A 1 133 ? -97.737  -33.967 49.391 1.00 30.44 ? 133  GLN A O   1 
ATOM   986  C CB  . GLN A 1 133 ? -98.903  -31.350 50.724 1.00 30.48 ? 133  GLN A CB  1 
ATOM   987  C CG  . GLN A 1 133 ? -98.560  -29.869 50.901 1.00 28.91 ? 133  GLN A CG  1 
ATOM   988  C CD  . GLN A 1 133 ? -99.757  -28.967 50.684 1.00 31.46 ? 133  GLN A CD  1 
ATOM   989  O OE1 . GLN A 1 133 ? -100.789 -29.405 50.186 1.00 32.59 ? 133  GLN A OE1 1 
ATOM   990  N NE2 . GLN A 1 133 ? -99.624  -27.700 51.056 1.00 30.23 ? 133  GLN A NE2 1 
ATOM   991  N N   . ILE A 1 134 ? -99.943  -33.989 49.004 1.00 30.71 ? 134  ILE A N   1 
ATOM   992  C CA  . ILE A 1 134 ? -99.968  -35.438 48.931 1.00 30.34 ? 134  ILE A CA  1 
ATOM   993  C C   . ILE A 1 134 ? -98.912  -35.964 47.933 1.00 30.44 ? 134  ILE A C   1 
ATOM   994  O O   . ILE A 1 134 ? -98.387  -37.066 48.108 1.00 29.99 ? 134  ILE A O   1 
ATOM   995  C CB  . ILE A 1 134 ? -101.392 -35.942 48.585 1.00 29.47 ? 134  ILE A CB  1 
ATOM   996  C CG1 . ILE A 1 134 ? -102.315 -35.651 49.773 1.00 29.70 ? 134  ILE A CG1 1 
ATOM   997  C CG2 . ILE A 1 134 ? -101.385 -37.432 48.299 1.00 25.01 ? 134  ILE A CG2 1 
ATOM   998  C CD1 . ILE A 1 134 ? -103.726 -36.110 49.599 1.00 30.25 ? 134  ILE A CD1 1 
ATOM   999  N N   . GLN A 1 135 ? -98.570  -35.178 46.914 1.00 27.37 ? 135  GLN A N   1 
ATOM   1000 C CA  . GLN A 1 135 ? -97.546  -35.628 45.961 1.00 27.50 ? 135  GLN A CA  1 
ATOM   1001 C C   . GLN A 1 135 ? -96.246  -35.940 46.696 1.00 27.74 ? 135  GLN A C   1 
ATOM   1002 O O   . GLN A 1 135 ? -95.534  -36.884 46.353 1.00 28.40 ? 135  GLN A O   1 
ATOM   1003 C CB  . GLN A 1 135 ? -97.257  -34.560 44.903 1.00 28.87 ? 135  GLN A CB  1 
ATOM   1004 C CG  . GLN A 1 135 ? -98.274  -34.450 43.779 1.00 31.47 ? 135  GLN A CG  1 
ATOM   1005 C CD  . GLN A 1 135 ? -97.647  -33.884 42.508 1.00 34.88 ? 135  GLN A CD  1 
ATOM   1006 O OE1 . GLN A 1 135 ? -96.598  -34.358 42.058 1.00 36.03 ? 135  GLN A OE1 1 
ATOM   1007 N NE2 . GLN A 1 135 ? -98.282  -32.878 41.925 1.00 33.63 ? 135  GLN A NE2 1 
ATOM   1008 N N   . GLY A 1 136 ? -95.933  -35.119 47.697 1.00 27.48 ? 136  GLY A N   1 
ATOM   1009 C CA  . GLY A 1 136 ? -94.725  -35.317 48.476 1.00 25.72 ? 136  GLY A CA  1 
ATOM   1010 C C   . GLY A 1 136 ? -94.744  -36.548 49.371 1.00 27.03 ? 136  GLY A C   1 
ATOM   1011 O O   . GLY A 1 136 ? -93.745  -36.871 50.006 1.00 26.97 ? 136  GLY A O   1 
ATOM   1012 N N   . PHE A 1 137 ? -95.880  -37.233 49.444 1.00 27.56 ? 137  PHE A N   1 
ATOM   1013 C CA  . PHE A 1 137 ? -95.972  -38.435 50.260 1.00 26.09 ? 137  PHE A CA  1 
ATOM   1014 C C   . PHE A 1 137 ? -95.314  -39.614 49.540 1.00 26.65 ? 137  PHE A C   1 
ATOM   1015 O O   . PHE A 1 137 ? -95.131  -40.687 50.116 1.00 27.51 ? 137  PHE A O   1 
ATOM   1016 C CB  . PHE A 1 137 ? -97.434  -38.758 50.571 1.00 23.33 ? 137  PHE A CB  1 
ATOM   1017 C CG  . PHE A 1 137 ? -98.076  -37.811 51.554 1.00 24.59 ? 137  PHE A CG  1 
ATOM   1018 C CD1 . PHE A 1 137 ? -99.394  -37.991 51.937 1.00 23.76 ? 137  PHE A CD1 1 
ATOM   1019 C CD2 . PHE A 1 137 ? -97.360  -36.744 52.099 1.00 26.95 ? 137  PHE A CD2 1 
ATOM   1020 C CE1 . PHE A 1 137 ? -99.998  -37.138 52.841 1.00 24.51 ? 137  PHE A CE1 1 
ATOM   1021 C CE2 . PHE A 1 137 ? -97.957  -35.882 53.006 1.00 24.97 ? 137  PHE A CE2 1 
ATOM   1022 C CZ  . PHE A 1 137 ? -99.284  -36.083 53.379 1.00 26.89 ? 137  PHE A CZ  1 
ATOM   1023 N N   . PHE A 1 138 ? -94.957  -39.407 48.277 1.00 26.46 ? 138  PHE A N   1 
ATOM   1024 C CA  . PHE A 1 138 ? -94.309  -40.447 47.487 1.00 26.21 ? 138  PHE A CA  1 
ATOM   1025 C C   . PHE A 1 138 ? -92.874  -40.031 47.205 1.00 26.38 ? 138  PHE A C   1 
ATOM   1026 O O   . PHE A 1 138 ? -92.511  -38.875 47.389 1.00 27.57 ? 138  PHE A O   1 
ATOM   1027 C CB  . PHE A 1 138 ? -94.998  -40.625 46.125 1.00 25.88 ? 138  PHE A CB  1 
ATOM   1028 C CG  . PHE A 1 138 ? -96.384  -41.179 46.195 1.00 26.73 ? 138  PHE A CG  1 
ATOM   1029 C CD1 . PHE A 1 138 ? -97.481  -40.335 46.335 1.00 26.54 ? 138  PHE A CD1 1 
ATOM   1030 C CD2 . PHE A 1 138 ? -96.599  -42.548 46.077 1.00 25.76 ? 138  PHE A CD2 1 
ATOM   1031 C CE1 . PHE A 1 138 ? -98.774  -40.846 46.352 1.00 27.59 ? 138  PHE A CE1 1 
ATOM   1032 C CE2 . PHE A 1 138 ? -97.885  -43.072 46.092 1.00 28.72 ? 138  PHE A CE2 1 
ATOM   1033 C CZ  . PHE A 1 138 ? -98.978  -42.218 46.229 1.00 28.75 ? 138  PHE A CZ  1 
ATOM   1034 N N   . ASP A 1 139 ? -92.054  -40.982 46.775 1.00 28.51 ? 139  ASP A N   1 
ATOM   1035 C CA  . ASP A 1 139 ? -90.689  -40.662 46.368 1.00 30.23 ? 139  ASP A CA  1 
ATOM   1036 C C   . ASP A 1 139 ? -90.691  -40.911 44.856 1.00 31.31 ? 139  ASP A C   1 
ATOM   1037 O O   . ASP A 1 139 ? -89.841  -40.400 44.124 1.00 34.78 ? 139  ASP A O   1 
ATOM   1038 C CB  . ASP A 1 139 ? -89.648  -41.543 47.074 1.00 31.68 ? 139  ASP A CB  1 
ATOM   1039 C CG  . ASP A 1 139 ? -89.413  -41.126 48.532 1.00 32.49 ? 139  ASP A CG  1 
ATOM   1040 O OD1 . ASP A 1 139 ? -89.351  -39.911 48.828 1.00 30.52 ? 139  ASP A OD1 1 
ATOM   1041 O OD2 . ASP A 1 139 ? -89.275  -42.020 49.385 1.00 37.49 ? 139  ASP A OD2 1 
ATOM   1042 N N   . ILE A 1 140 ? -91.669  -41.690 44.398 1.00 27.87 ? 140  ILE A N   1 
ATOM   1043 C CA  . ILE A 1 140 ? -91.832  -41.971 42.976 1.00 26.05 ? 140  ILE A CA  1 
ATOM   1044 C C   . ILE A 1 140 ? -92.619  -40.797 42.400 1.00 25.42 ? 140  ILE A C   1 
ATOM   1045 O O   . ILE A 1 140 ? -93.305  -40.088 43.135 1.00 27.75 ? 140  ILE A O   1 
ATOM   1046 C CB  . ILE A 1 140 ? -92.648  -43.275 42.721 1.00 23.02 ? 140  ILE A CB  1 
ATOM   1047 C CG1 . ILE A 1 140 ? -93.986  -43.212 43.474 1.00 25.27 ? 140  ILE A CG1 1 
ATOM   1048 C CG2 . ILE A 1 140 ? -91.849  -44.484 43.151 1.00 22.61 ? 140  ILE A CG2 1 
ATOM   1049 C CD1 . ILE A 1 140 ? -94.899  -44.414 43.243 1.00 22.36 ? 140  ILE A CD1 1 
ATOM   1050 N N   . PRO A 1 141 ? -92.527  -40.573 41.079 1.00 26.59 ? 141  PRO A N   1 
ATOM   1051 C CA  . PRO A 1 141 ? -93.230  -39.483 40.387 1.00 24.13 ? 141  PRO A CA  1 
ATOM   1052 C C   . PRO A 1 141 ? -94.769  -39.552 40.437 1.00 25.34 ? 141  PRO A C   1 
ATOM   1053 O O   . PRO A 1 141 ? -95.371  -40.618 40.260 1.00 22.57 ? 141  PRO A O   1 
ATOM   1054 C CB  . PRO A 1 141 ? -92.738  -39.613 38.945 1.00 24.47 ? 141  PRO A CB  1 
ATOM   1055 C CG  . PRO A 1 141 ? -91.398  -40.224 39.075 1.00 26.53 ? 141  PRO A CG  1 
ATOM   1056 C CD  . PRO A 1 141 ? -91.603  -41.260 40.161 1.00 26.97 ? 141  PRO A CD  1 
ATOM   1057 N N   . VAL A 1 142 ? -95.403  -38.406 40.649 1.00 24.95 ? 142  VAL A N   1 
ATOM   1058 C CA  . VAL A 1 142 ? -96.855  -38.349 40.651 1.00 26.09 ? 142  VAL A CA  1 
ATOM   1059 C C   . VAL A 1 142 ? -97.308  -37.229 39.706 1.00 28.64 ? 142  VAL A C   1 
ATOM   1060 O O   . VAL A 1 142 ? -96.801  -36.107 39.754 1.00 28.03 ? 142  VAL A O   1 
ATOM   1061 C CB  . VAL A 1 142 ? -97.426  -38.072 42.071 1.00 27.06 ? 142  VAL A CB  1 
ATOM   1062 C CG1 . VAL A 1 142 ? -98.940  -38.142 42.043 1.00 24.21 ? 142  VAL A CG1 1 
ATOM   1063 C CG2 . VAL A 1 142 ? -96.870  -39.065 43.074 1.00 23.40 ? 142  VAL A CG2 1 
ATOM   1064 N N   . ASP A 1 143 ? -98.236  -37.549 38.812 1.00 29.87 ? 143  ASP A N   1 
ATOM   1065 C CA  . ASP A 1 143 ? -98.778  -36.555 37.902 1.00 28.83 ? 143  ASP A CA  1 
ATOM   1066 C C   . ASP A 1 143 ? -100.204 -36.303 38.363 1.00 28.89 ? 143  ASP A C   1 
ATOM   1067 O O   . ASP A 1 143 ? -101.057 -37.181 38.256 1.00 29.47 ? 143  ASP A O   1 
ATOM   1068 C CB  . ASP A 1 143 ? -98.749  -37.065 36.461 1.00 29.66 ? 143  ASP A CB  1 
ATOM   1069 C CG  . ASP A 1 143 ? -97.341  -37.100 35.896 1.00 31.56 ? 143  ASP A CG  1 
ATOM   1070 O OD1 . ASP A 1 143 ? -96.628  -36.086 36.071 1.00 29.28 ? 143  ASP A OD1 1 
ATOM   1071 O OD2 . ASP A 1 143 ? -96.949  -38.124 35.290 1.00 30.66 ? 143  ASP A OD2 1 
ATOM   1072 N N   . ASN A 1 144 ? -100.443 -35.109 38.899 1.00 28.80 ? 144  ASN A N   1 
ATOM   1073 C CA  . ASN A 1 144 ? -101.753 -34.712 39.416 1.00 30.03 ? 144  ASN A CA  1 
ATOM   1074 C C   . ASN A 1 144 ? -102.466 -33.850 38.364 1.00 32.21 ? 144  ASN A C   1 
ATOM   1075 O O   . ASN A 1 144 ? -102.193 -32.650 38.220 1.00 31.47 ? 144  ASN A O   1 
ATOM   1076 C CB  . ASN A 1 144 ? -101.550 -33.951 40.743 1.00 28.84 ? 144  ASN A CB  1 
ATOM   1077 C CG  . ASN A 1 144 ? -102.857 -33.570 41.437 1.00 30.47 ? 144  ASN A CG  1 
ATOM   1078 O OD1 . ASN A 1 144 ? -103.822 -34.341 41.481 1.00 27.92 ? 144  ASN A OD1 1 
ATOM   1079 N ND2 . ASN A 1 144 ? -102.873 -32.374 42.017 1.00 30.03 ? 144  ASN A ND2 1 
ATOM   1080 N N   . LEU A 1 145 ? -103.359 -34.496 37.615 1.00 33.15 ? 145  LEU A N   1 
ATOM   1081 C CA  . LEU A 1 145 ? -104.142 -33.851 36.564 1.00 33.29 ? 145  LEU A CA  1 
ATOM   1082 C C   . LEU A 1 145 ? -105.212 -32.974 37.196 1.00 33.63 ? 145  LEU A C   1 
ATOM   1083 O O   . LEU A 1 145 ? -105.592 -33.185 38.346 1.00 33.83 ? 145  LEU A O   1 
ATOM   1084 C CB  . LEU A 1 145 ? -104.807 -34.911 35.683 1.00 33.84 ? 145  LEU A CB  1 
ATOM   1085 C CG  . LEU A 1 145 ? -103.874 -35.938 35.037 1.00 33.63 ? 145  LEU A CG  1 
ATOM   1086 C CD1 . LEU A 1 145 ? -104.691 -36.980 34.301 1.00 35.35 ? 145  LEU A CD1 1 
ATOM   1087 C CD2 . LEU A 1 145 ? -102.932 -35.248 34.093 1.00 34.30 ? 145  LEU A CD2 1 
ATOM   1088 N N   . TYR A 1 146 ? -105.703 -31.995 36.442 1.00 35.51 ? 146  TYR A N   1 
ATOM   1089 C CA  . TYR A 1 146 ? -106.725 -31.092 36.956 1.00 37.78 ? 146  TYR A CA  1 
ATOM   1090 C C   . TYR A 1 146 ? -107.984 -31.100 36.104 1.00 37.89 ? 146  TYR A C   1 
ATOM   1091 O O   . TYR A 1 146 ? -107.921 -31.184 34.882 1.00 38.69 ? 146  TYR A O   1 
ATOM   1092 C CB  . TYR A 1 146 ? -106.186 -29.659 37.033 1.00 39.69 ? 146  TYR A CB  1 
ATOM   1093 C CG  . TYR A 1 146 ? -104.832 -29.554 37.689 1.00 45.02 ? 146  TYR A CG  1 
ATOM   1094 C CD1 . TYR A 1 146 ? -103.665 -29.694 36.938 1.00 46.14 ? 146  TYR A CD1 1 
ATOM   1095 C CD2 . TYR A 1 146 ? -104.714 -29.366 39.072 1.00 46.86 ? 146  TYR A CD2 1 
ATOM   1096 C CE1 . TYR A 1 146 ? -102.413 -29.657 37.541 1.00 49.60 ? 146  TYR A CE1 1 
ATOM   1097 C CE2 . TYR A 1 146 ? -103.460 -29.327 39.691 1.00 48.86 ? 146  TYR A CE2 1 
ATOM   1098 C CZ  . TYR A 1 146 ? -102.316 -29.476 38.915 1.00 50.56 ? 146  TYR A CZ  1 
ATOM   1099 O OH  . TYR A 1 146 ? -101.073 -29.469 39.501 1.00 52.43 ? 146  TYR A OH  1 
ATOM   1100 N N   . ALA A 1 147 ? -109.130 -31.002 36.760 1.00 37.51 ? 147  ALA A N   1 
ATOM   1101 C CA  . ALA A 1 147 ? -110.395 -30.970 36.054 1.00 38.03 ? 147  ALA A CA  1 
ATOM   1102 C C   . ALA A 1 147 ? -110.811 -29.515 35.852 1.00 39.03 ? 147  ALA A C   1 
ATOM   1103 O O   . ALA A 1 147 ? -111.822 -29.245 35.205 1.00 38.94 ? 147  ALA A O   1 
ATOM   1104 C CB  . ALA A 1 147 ? -111.456 -31.705 36.858 1.00 37.97 ? 147  ALA A CB  1 
ATOM   1105 N N   . GLU A 1 148 ? -110.018 -28.594 36.402 1.00 37.40 ? 148  GLU A N   1 
ATOM   1106 C CA  . GLU A 1 148 ? -110.300 -27.166 36.323 1.00 40.02 ? 148  GLU A CA  1 
ATOM   1107 C C   . GLU A 1 148 ? -110.578 -26.679 34.900 1.00 40.40 ? 148  GLU A C   1 
ATOM   1108 O O   . GLU A 1 148 ? -111.591 -26.029 34.649 1.00 40.69 ? 148  GLU A O   1 
ATOM   1109 C CB  . GLU A 1 148 ? -109.147 -26.354 36.926 1.00 42.95 ? 148  GLU A CB  1 
ATOM   1110 C CG  . GLU A 1 148 ? -109.536 -24.923 37.278 1.00 45.75 ? 148  GLU A CG  1 
ATOM   1111 C CD  . GLU A 1 148 ? -108.381 -24.101 37.848 1.00 49.21 ? 148  GLU A CD  1 
ATOM   1112 O OE1 . GLU A 1 148 ? -107.686 -24.589 38.768 1.00 51.70 ? 148  GLU A OE1 1 
ATOM   1113 O OE2 . GLU A 1 148 ? -108.181 -22.957 37.384 1.00 48.63 ? 148  GLU A OE2 1 
ATOM   1114 N N   . PRO A 1 149 ? -109.682 -26.977 33.948 1.00 39.94 ? 149  PRO A N   1 
ATOM   1115 C CA  . PRO A 1 149 ? -109.976 -26.501 32.594 1.00 39.25 ? 149  PRO A CA  1 
ATOM   1116 C C   . PRO A 1 149 ? -111.379 -26.928 32.144 1.00 39.03 ? 149  PRO A C   1 
ATOM   1117 O O   . PRO A 1 149 ? -112.164 -26.107 31.669 1.00 40.06 ? 149  PRO A O   1 
ATOM   1118 C CB  . PRO A 1 149 ? -108.868 -27.137 31.763 1.00 39.77 ? 149  PRO A CB  1 
ATOM   1119 C CG  . PRO A 1 149 ? -107.704 -27.181 32.746 1.00 38.88 ? 149  PRO A CG  1 
ATOM   1120 C CD  . PRO A 1 149 ? -108.379 -27.669 34.003 1.00 38.80 ? 149  PRO A CD  1 
ATOM   1121 N N   . ALA A 1 150 ? -111.702 -28.205 32.323 1.00 38.27 ? 150  ALA A N   1 
ATOM   1122 C CA  . ALA A 1 150 ? -113.006 -28.721 31.924 1.00 39.00 ? 150  ALA A CA  1 
ATOM   1123 C C   . ALA A 1 150 ? -114.151 -28.074 32.703 1.00 40.17 ? 150  ALA A C   1 
ATOM   1124 O O   . ALA A 1 150 ? -115.207 -27.789 32.138 1.00 41.54 ? 150  ALA A O   1 
ATOM   1125 C CB  . ALA A 1 150 ? -113.045 -30.239 32.093 1.00 38.84 ? 150  ALA A CB  1 
ATOM   1126 N N   . VAL A 1 151 ? -113.946 -27.850 33.999 1.00 39.41 ? 151  VAL A N   1 
ATOM   1127 C CA  . VAL A 1 151 ? -114.970 -27.222 34.830 1.00 39.15 ? 151  VAL A CA  1 
ATOM   1128 C C   . VAL A 1 151 ? -115.211 -25.797 34.322 1.00 40.91 ? 151  VAL A C   1 
ATOM   1129 O O   . VAL A 1 151 ? -116.353 -25.372 34.136 1.00 39.81 ? 151  VAL A O   1 
ATOM   1130 C CB  . VAL A 1 151 ? -114.533 -27.153 36.311 1.00 37.85 ? 151  VAL A CB  1 
ATOM   1131 C CG1 . VAL A 1 151 ? -115.571 -26.404 37.132 1.00 36.59 ? 151  VAL A CG1 1 
ATOM   1132 C CG2 . VAL A 1 151 ? -114.344 -28.553 36.858 1.00 36.78 ? 151  VAL A CG2 1 
ATOM   1133 N N   . LEU A 1 152 ? -114.120 -25.069 34.109 1.00 41.79 ? 152  LEU A N   1 
ATOM   1134 C CA  . LEU A 1 152 ? -114.182 -23.702 33.617 1.00 43.72 ? 152  LEU A CA  1 
ATOM   1135 C C   . LEU A 1 152 ? -115.047 -23.705 32.363 1.00 45.73 ? 152  LEU A C   1 
ATOM   1136 O O   . LEU A 1 152 ? -116.068 -23.012 32.293 1.00 47.06 ? 152  LEU A O   1 
ATOM   1137 C CB  . LEU A 1 152 ? -112.769 -23.214 33.287 1.00 42.70 ? 152  LEU A CB  1 
ATOM   1138 C CG  . LEU A 1 152 ? -112.191 -22.054 34.102 1.00 44.74 ? 152  LEU A CG  1 
ATOM   1139 C CD1 . LEU A 1 152 ? -112.620 -22.139 35.551 1.00 45.35 ? 152  LEU A CD1 1 
ATOM   1140 C CD2 . LEU A 1 152 ? -110.683 -22.084 33.985 1.00 44.22 ? 152  LEU A CD2 1 
ATOM   1141 N N   . LYS A 1 153 ? -114.637 -24.519 31.394 1.00 46.05 ? 153  LYS A N   1 
ATOM   1142 C CA  . LYS A 1 153 ? -115.332 -24.656 30.123 1.00 46.56 ? 153  LYS A CA  1 
ATOM   1143 C C   . LYS A 1 153 ? -116.807 -24.999 30.279 1.00 46.17 ? 153  LYS A C   1 
ATOM   1144 O O   . LYS A 1 153 ? -117.630 -24.552 29.486 1.00 48.29 ? 153  LYS A O   1 
ATOM   1145 C CB  . LYS A 1 153 ? -114.636 -25.720 29.271 1.00 48.10 ? 153  LYS A CB  1 
ATOM   1146 C CG  . LYS A 1 153 ? -115.223 -25.927 27.887 1.00 51.02 ? 153  LYS A CG  1 
ATOM   1147 C CD  . LYS A 1 153 ? -114.233 -26.685 27.009 1.00 54.77 ? 153  LYS A CD  1 
ATOM   1148 C CE  . LYS A 1 153 ? -114.758 -26.908 25.596 1.00 56.65 ? 153  LYS A CE  1 
ATOM   1149 N NZ  . LYS A 1 153 ? -115.903 -27.867 25.570 1.00 61.02 ? 153  LYS A NZ  1 
ATOM   1150 N N   . TRP A 1 154 ? -117.151 -25.784 31.292 1.00 45.54 ? 154  TRP A N   1 
ATOM   1151 C CA  . TRP A 1 154 ? -118.548 -26.159 31.497 1.00 45.15 ? 154  TRP A CA  1 
ATOM   1152 C C   . TRP A 1 154 ? -119.346 -24.982 32.064 1.00 46.02 ? 154  TRP A C   1 
ATOM   1153 O O   . TRP A 1 154 ? -120.520 -24.789 31.728 1.00 45.26 ? 154  TRP A O   1 
ATOM   1154 C CB  . TRP A 1 154 ? -118.651 -27.348 32.454 1.00 43.18 ? 154  TRP A CB  1 
ATOM   1155 C CG  . TRP A 1 154 ? -120.039 -27.904 32.564 1.00 41.16 ? 154  TRP A CG  1 
ATOM   1156 C CD1 . TRP A 1 154 ? -120.543 -28.979 31.895 1.00 40.28 ? 154  TRP A CD1 1 
ATOM   1157 C CD2 . TRP A 1 154 ? -121.117 -27.384 33.356 1.00 41.69 ? 154  TRP A CD2 1 
ATOM   1158 N NE1 . TRP A 1 154 ? -121.863 -29.171 32.225 1.00 41.19 ? 154  TRP A NE1 1 
ATOM   1159 C CE2 . TRP A 1 154 ? -122.240 -28.212 33.131 1.00 41.67 ? 154  TRP A CE2 1 
ATOM   1160 C CE3 . TRP A 1 154 ? -121.236 -26.316 34.260 1.00 41.74 ? 154  TRP A CE3 1 
ATOM   1161 C CZ2 . TRP A 1 154 ? -123.478 -27.986 33.740 1.00 41.53 ? 154  TRP A CZ2 1 
ATOM   1162 C CZ3 . TRP A 1 154 ? -122.466 -26.090 34.871 1.00 41.05 ? 154  TRP A CZ3 1 
ATOM   1163 C CH2 . TRP A 1 154 ? -123.567 -26.934 34.619 1.00 42.49 ? 154  TRP A CH2 1 
ATOM   1164 N N   . ILE A 1 155 ? -118.705 -24.207 32.935 1.00 46.39 ? 155  ILE A N   1 
ATOM   1165 C CA  . ILE A 1 155 ? -119.342 -23.049 33.551 1.00 46.15 ? 155  ILE A CA  1 
ATOM   1166 C C   . ILE A 1 155 ? -119.732 -22.016 32.493 1.00 47.58 ? 155  ILE A C   1 
ATOM   1167 O O   . ILE A 1 155 ? -120.860 -21.523 32.478 1.00 48.38 ? 155  ILE A O   1 
ATOM   1168 C CB  . ILE A 1 155 ? -118.401 -22.383 34.595 1.00 44.93 ? 155  ILE A CB  1 
ATOM   1169 C CG1 . ILE A 1 155 ? -118.300 -23.270 35.844 1.00 42.25 ? 155  ILE A CG1 1 
ATOM   1170 C CG2 . ILE A 1 155 ? -118.901 -20.977 34.943 1.00 40.18 ? 155  ILE A CG2 1 
ATOM   1171 C CD1 . ILE A 1 155 ? -117.415 -22.702 36.945 1.00 41.34 ? 155  ILE A CD1 1 
ATOM   1172 N N   . ARG A 1 156 ? -118.790 -21.703 31.610 1.00 49.59 ? 156  ARG A N   1 
ATOM   1173 C CA  . ARG A 1 156 ? -119.000 -20.730 30.546 1.00 53.03 ? 156  ARG A CA  1 
ATOM   1174 C C   . ARG A 1 156 ? -120.056 -21.169 29.542 1.00 54.61 ? 156  ARG A C   1 
ATOM   1175 O O   . ARG A 1 156 ? -120.789 -20.337 29.001 1.00 55.47 ? 156  ARG A O   1 
ATOM   1176 C CB  . ARG A 1 156 ? -117.687 -20.468 29.808 1.00 54.82 ? 156  ARG A CB  1 
ATOM   1177 C CG  . ARG A 1 156 ? -116.592 -19.864 30.655 1.00 59.17 ? 156  ARG A CG  1 
ATOM   1178 C CD  . ARG A 1 156 ? -115.264 -19.956 29.932 1.00 63.35 ? 156  ARG A CD  1 
ATOM   1179 N NE  . ARG A 1 156 ? -114.183 -19.408 30.740 1.00 68.71 ? 156  ARG A NE  1 
ATOM   1180 C CZ  . ARG A 1 156 ? -112.893 -19.552 30.459 1.00 70.26 ? 156  ARG A CZ  1 
ATOM   1181 N NH1 . ARG A 1 156 ? -112.517 -20.235 29.386 1.00 71.99 ? 156  ARG A NH1 1 
ATOM   1182 N NH2 . ARG A 1 156 ? -111.982 -19.007 31.251 1.00 70.95 ? 156  ARG A NH2 1 
ATOM   1183 N N   . GLU A 1 157 ? -120.132 -22.471 29.287 1.00 54.61 ? 157  GLU A N   1 
ATOM   1184 C CA  . GLU A 1 157 ? -121.094 -23.000 28.331 1.00 54.98 ? 157  GLU A CA  1 
ATOM   1185 C C   . GLU A 1 157 ? -122.405 -23.499 28.932 1.00 54.71 ? 157  GLU A C   1 
ATOM   1186 O O   . GLU A 1 157 ? -123.193 -24.127 28.233 1.00 55.61 ? 157  GLU A O   1 
ATOM   1187 C CB  . GLU A 1 157 ? -120.451 -24.125 27.531 1.00 56.22 ? 157  GLU A CB  1 
ATOM   1188 C CG  . GLU A 1 157 ? -119.063 -23.781 27.032 1.00 59.56 ? 157  GLU A CG  1 
ATOM   1189 C CD  . GLU A 1 157 ? -118.409 -24.921 26.277 1.00 62.45 ? 157  GLU A CD  1 
ATOM   1190 O OE1 . GLU A 1 157 ? -118.479 -26.076 26.760 1.00 65.54 ? 157  GLU A OE1 1 
ATOM   1191 O OE2 . GLU A 1 157 ? -117.818 -24.656 25.207 1.00 62.02 ? 157  GLU A OE2 1 
ATOM   1192 N N   . ASN A 1 158 ? -122.663 -23.244 30.210 1.00 52.65 ? 158  ASN A N   1 
ATOM   1193 C CA  . ASN A 1 158 ? -123.918 -23.729 30.776 1.00 51.60 ? 158  ASN A CA  1 
ATOM   1194 C C   . ASN A 1 158 ? -124.637 -22.751 31.680 1.00 51.86 ? 158  ASN A C   1 
ATOM   1195 O O   . ASN A 1 158 ? -125.830 -22.900 31.943 1.00 50.77 ? 158  ASN A O   1 
ATOM   1196 C CB  . ASN A 1 158 ? -123.690 -25.041 31.522 1.00 51.89 ? 158  ASN A CB  1 
ATOM   1197 C CG  . ASN A 1 158 ? -123.449 -26.204 30.582 1.00 50.98 ? 158  ASN A CG  1 
ATOM   1198 O OD1 . ASN A 1 158 ? -124.362 -26.966 30.263 1.00 51.22 ? 158  ASN A OD1 1 
ATOM   1199 N ND2 . ASN A 1 158 ? -122.215 -26.339 30.121 1.00 51.44 ? 158  ASN A ND2 1 
ATOM   1200 N N   . ILE A 1 159 ? -123.907 -21.759 32.168 1.00 52.38 ? 159  ILE A N   1 
ATOM   1201 C CA  . ILE A 1 159 ? -124.490 -20.748 33.033 1.00 53.12 ? 159  ILE A CA  1 
ATOM   1202 C C   . ILE A 1 159 ? -124.404 -19.428 32.276 1.00 53.24 ? 159  ILE A C   1 
ATOM   1203 O O   . ILE A 1 159 ? -123.317 -18.885 32.082 1.00 52.54 ? 159  ILE A O   1 
ATOM   1204 C CB  . ILE A 1 159 ? -123.724 -20.670 34.371 1.00 54.84 ? 159  ILE A CB  1 
ATOM   1205 C CG1 . ILE A 1 159 ? -123.793 -22.031 35.077 1.00 54.41 ? 159  ILE A CG1 1 
ATOM   1206 C CG2 . ILE A 1 159 ? -124.330 -19.599 35.264 1.00 54.51 ? 159  ILE A CG2 1 
ATOM   1207 C CD1 . ILE A 1 159 ? -122.982 -22.098 36.354 1.00 54.62 ? 159  ILE A CD1 1 
ATOM   1208 N N   . SER A 1 160 ? -125.553 -18.929 31.831 1.00 54.04 ? 160  SER A N   1 
ATOM   1209 C CA  . SER A 1 160 ? -125.600 -17.691 31.066 1.00 56.20 ? 160  SER A CA  1 
ATOM   1210 C C   . SER A 1 160 ? -125.105 -16.472 31.841 1.00 57.19 ? 160  SER A C   1 
ATOM   1211 O O   . SER A 1 160 ? -124.579 -15.525 31.252 1.00 57.11 ? 160  SER A O   1 
ATOM   1212 C CB  . SER A 1 160 ? -127.023 -17.446 30.548 1.00 56.40 ? 160  SER A CB  1 
ATOM   1213 O OG  . SER A 1 160 ? -127.955 -17.401 31.614 1.00 56.69 ? 160  SER A OG  1 
ATOM   1214 N N   . GLU A 1 161 ? -125.246 -16.505 33.160 1.00 58.86 ? 161  GLU A N   1 
ATOM   1215 C CA  . GLU A 1 161 ? -124.821 -15.385 33.997 1.00 60.38 ? 161  GLU A CA  1 
ATOM   1216 C C   . GLU A 1 161 ? -123.403 -15.540 34.565 1.00 59.15 ? 161  GLU A C   1 
ATOM   1217 O O   . GLU A 1 161 ? -122.965 -14.732 35.384 1.00 58.91 ? 161  GLU A O   1 
ATOM   1218 C CB  . GLU A 1 161 ? -125.814 -15.202 35.153 1.00 60.87 ? 161  GLU A CB  1 
ATOM   1219 C CG  . GLU A 1 161 ? -127.282 -15.296 34.748 1.00 65.26 ? 161  GLU A CG  1 
ATOM   1220 C CD  . GLU A 1 161 ? -127.809 -16.726 34.765 1.00 68.26 ? 161  GLU A CD  1 
ATOM   1221 O OE1 . GLU A 1 161 ? -127.195 -17.606 34.122 1.00 68.80 ? 161  GLU A OE1 1 
ATOM   1222 O OE2 . GLU A 1 161 ? -128.844 -16.972 35.422 1.00 69.25 ? 161  GLU A OE2 1 
ATOM   1223 N N   . TRP A 1 162 ? -122.680 -16.562 34.120 1.00 58.53 ? 162  TRP A N   1 
ATOM   1224 C CA  . TRP A 1 162 ? -121.338 -16.811 34.634 1.00 58.34 ? 162  TRP A CA  1 
ATOM   1225 C C   . TRP A 1 162 ? -120.442 -15.579 34.639 1.00 58.78 ? 162  TRP A C   1 
ATOM   1226 O O   . TRP A 1 162 ? -119.580 -15.438 35.513 1.00 58.32 ? 162  TRP A O   1 
ATOM   1227 C CB  . TRP A 1 162 ? -120.656 -17.927 33.844 1.00 56.10 ? 162  TRP A CB  1 
ATOM   1228 C CG  . TRP A 1 162 ? -120.187 -17.519 32.500 1.00 54.54 ? 162  TRP A CG  1 
ATOM   1229 C CD1 . TRP A 1 162 ? -120.872 -17.617 31.325 1.00 53.68 ? 162  TRP A CD1 1 
ATOM   1230 C CD2 . TRP A 1 162 ? -118.909 -16.969 32.176 1.00 54.59 ? 162  TRP A CD2 1 
ATOM   1231 N NE1 . TRP A 1 162 ? -120.098 -17.160 30.286 1.00 53.17 ? 162  TRP A NE1 1 
ATOM   1232 C CE2 . TRP A 1 162 ? -118.889 -16.744 30.783 1.00 53.87 ? 162  TRP A CE2 1 
ATOM   1233 C CE3 . TRP A 1 162 ? -117.781 -16.619 32.933 1.00 54.46 ? 162  TRP A CE3 1 
ATOM   1234 C CZ2 . TRP A 1 162 ? -117.778 -16.216 30.122 1.00 54.43 ? 162  TRP A CZ2 1 
ATOM   1235 C CZ3 . TRP A 1 162 ? -116.677 -16.092 32.279 1.00 54.95 ? 162  TRP A CZ3 1 
ATOM   1236 C CH2 . TRP A 1 162 ? -116.689 -15.884 30.885 1.00 55.14 ? 162  TRP A CH2 1 
ATOM   1237 N N   . ARG A 1 163 ? -120.641 -14.682 33.679 1.00 58.28 ? 163  ARG A N   1 
ATOM   1238 C CA  . ARG A 1 163 ? -119.813 -13.478 33.605 1.00 57.81 ? 163  ARG A CA  1 
ATOM   1239 C C   . ARG A 1 163 ? -119.800 -12.681 34.920 1.00 57.51 ? 163  ARG A C   1 
ATOM   1240 O O   . ARG A 1 163 ? -118.856 -11.942 35.197 1.00 57.83 ? 163  ARG A O   1 
ATOM   1241 C CB  . ARG A 1 163 ? -120.293 -12.567 32.461 1.00 59.08 ? 163  ARG A CB  1 
ATOM   1242 C CG  . ARG A 1 163 ? -119.988 -13.065 31.029 1.00 59.07 ? 163  ARG A CG  1 
ATOM   1243 C CD  . ARG A 1 163 ? -118.656 -12.519 30.509 1.00 57.54 ? 163  ARG A CD  1 
ATOM   1244 N NE  . ARG A 1 163 ? -118.293 -13.065 29.199 1.00 57.88 ? 163  ARG A NE  1 
ATOM   1245 C CZ  . ARG A 1 163 ? -117.105 -12.903 28.624 1.00 55.14 ? 163  ARG A CZ  1 
ATOM   1246 N NH1 . ARG A 1 163 ? -116.159 -12.204 29.233 1.00 55.57 ? 163  ARG A NH1 1 
ATOM   1247 N NH2 . ARG A 1 163 ? -116.854 -13.465 27.450 1.00 56.12 ? 163  ARG A NH2 1 
ATOM   1248 N N   . ASN A 1 164 ? -120.845 -12.836 35.728 1.00 55.95 ? 164  ASN A N   1 
ATOM   1249 C CA  . ASN A 1 164 ? -120.950 -12.136 37.004 1.00 54.84 ? 164  ASN A CA  1 
ATOM   1250 C C   . ASN A 1 164 ? -121.536 -13.103 38.007 1.00 54.39 ? 164  ASN A C   1 
ATOM   1251 O O   . ASN A 1 164 ? -122.589 -12.856 38.589 1.00 54.94 ? 164  ASN A O   1 
ATOM   1252 C CB  . ASN A 1 164 ? -121.874 -10.912 36.897 1.00 58.12 ? 164  ASN A CB  1 
ATOM   1253 C CG  . ASN A 1 164 ? -121.393 -9.895  35.887 1.00 59.07 ? 164  ASN A CG  1 
ATOM   1254 O OD1 . ASN A 1 164 ? -120.292 -9.350  35.998 1.00 59.85 ? 164  ASN A OD1 1 
ATOM   1255 N ND2 . ASN A 1 164 ? -122.230 -9.625  34.890 1.00 59.53 ? 164  ASN A ND2 1 
ATOM   1256 N N   . CYS A 1 165 ? -120.861 -14.222 38.205 1.00 52.57 ? 165  CYS A N   1 
ATOM   1257 C CA  . CYS A 1 165 ? -121.350 -15.216 39.141 1.00 51.17 ? 165  CYS A CA  1 
ATOM   1258 C C   . CYS A 1 165 ? -120.374 -15.202 40.308 1.00 49.98 ? 165  CYS A C   1 
ATOM   1259 O O   . CYS A 1 165 ? -119.358 -14.507 40.266 1.00 48.61 ? 165  CYS A O   1 
ATOM   1260 C CB  . CYS A 1 165 ? -121.347 -16.593 38.475 1.00 52.08 ? 165  CYS A CB  1 
ATOM   1261 S SG  . CYS A 1 165 ? -119.670 -17.213 38.202 1.00 52.22 ? 165  CYS A SG  1 
ATOM   1262 N N   . THR A 1 166 ? -120.674 -15.967 41.345 1.00 48.27 ? 166  THR A N   1 
ATOM   1263 C CA  . THR A 1 166 ? -119.785 -16.041 42.488 1.00 47.15 ? 166  THR A CA  1 
ATOM   1264 C C   . THR A 1 166 ? -119.435 -17.496 42.756 1.00 45.55 ? 166  THR A C   1 
ATOM   1265 O O   . THR A 1 166 ? -120.324 -18.343 42.884 1.00 45.48 ? 166  THR A O   1 
ATOM   1266 C CB  . THR A 1 166 ? -120.427 -15.448 43.757 1.00 46.67 ? 166  THR A CB  1 
ATOM   1267 O OG1 . THR A 1 166 ? -120.733 -14.066 43.538 1.00 48.57 ? 166  THR A OG1 1 
ATOM   1268 C CG2 . THR A 1 166 ? -119.469 -15.571 44.936 1.00 46.03 ? 166  THR A CG2 1 
ATOM   1269 N N   . ILE A 1 167 ? -118.136 -17.781 42.812 1.00 43.11 ? 167  ILE A N   1 
ATOM   1270 C CA  . ILE A 1 167 ? -117.652 -19.126 43.101 1.00 40.77 ? 167  ILE A CA  1 
ATOM   1271 C C   . ILE A 1 167 ? -117.609 -19.221 44.622 1.00 39.58 ? 167  ILE A C   1 
ATOM   1272 O O   . ILE A 1 167 ? -116.957 -18.416 45.278 1.00 42.27 ? 167  ILE A O   1 
ATOM   1273 C CB  . ILE A 1 167 ? -116.245 -19.334 42.527 1.00 39.31 ? 167  ILE A CB  1 
ATOM   1274 C CG1 . ILE A 1 167 ? -116.227 -18.904 41.057 1.00 40.40 ? 167  ILE A CG1 1 
ATOM   1275 C CG2 . ILE A 1 167 ? -115.829 -20.790 42.675 1.00 35.38 ? 167  ILE A CG2 1 
ATOM   1276 C CD1 . ILE A 1 167 ? -117.308 -19.576 40.191 1.00 38.00 ? 167  ILE A CD1 1 
ATOM   1277 N N   . VAL A 1 168 ? -118.308 -20.192 45.189 1.00 38.25 ? 168  VAL A N   1 
ATOM   1278 C CA  . VAL A 1 168 ? -118.345 -20.313 46.636 1.00 38.05 ? 168  VAL A CA  1 
ATOM   1279 C C   . VAL A 1 168 ? -117.728 -21.610 47.158 1.00 38.93 ? 168  VAL A C   1 
ATOM   1280 O O   . VAL A 1 168 ? -117.927 -22.678 46.590 1.00 38.97 ? 168  VAL A O   1 
ATOM   1281 C CB  . VAL A 1 168 ? -119.803 -20.200 47.142 1.00 37.24 ? 168  VAL A CB  1 
ATOM   1282 C CG1 . VAL A 1 168 ? -119.833 -20.179 48.645 1.00 36.27 ? 168  VAL A CG1 1 
ATOM   1283 C CG2 . VAL A 1 168 ? -120.453 -18.942 46.572 1.00 37.07 ? 168  VAL A CG2 1 
ATOM   1284 N N   . SER A 1 169 ? -116.966 -21.502 48.240 1.00 39.14 ? 169  SER A N   1 
ATOM   1285 C CA  . SER A 1 169 ? -116.339 -22.662 48.857 1.00 40.75 ? 169  SER A CA  1 
ATOM   1286 C C   . SER A 1 169 ? -117.188 -23.076 50.058 1.00 41.69 ? 169  SER A C   1 
ATOM   1287 O O   . SER A 1 169 ? -117.493 -22.249 50.920 1.00 41.85 ? 169  SER A O   1 
ATOM   1288 C CB  . SER A 1 169 ? -114.913 -22.315 49.320 1.00 40.64 ? 169  SER A CB  1 
ATOM   1289 O OG  . SER A 1 169 ? -114.308 -23.423 49.952 1.00 42.15 ? 169  SER A OG  1 
ATOM   1290 N N   . PRO A 1 170 ? -117.583 -24.361 50.123 1.00 42.28 ? 170  PRO A N   1 
ATOM   1291 C CA  . PRO A 1 170 ? -118.403 -24.950 51.188 1.00 42.68 ? 170  PRO A CA  1 
ATOM   1292 C C   . PRO A 1 170 ? -117.788 -24.805 52.574 1.00 42.85 ? 170  PRO A C   1 
ATOM   1293 O O   . PRO A 1 170 ? -118.484 -24.860 53.584 1.00 42.50 ? 170  PRO A O   1 
ATOM   1294 C CB  . PRO A 1 170 ? -118.511 -26.420 50.770 1.00 41.93 ? 170  PRO A CB  1 
ATOM   1295 C CG  . PRO A 1 170 ? -118.348 -26.362 49.278 1.00 43.45 ? 170  PRO A CG  1 
ATOM   1296 C CD  . PRO A 1 170 ? -117.217 -25.390 49.134 1.00 42.02 ? 170  PRO A CD  1 
ATOM   1297 N N   . ASP A 1 171 ? -116.475 -24.631 52.620 1.00 43.89 ? 171  ASP A N   1 
ATOM   1298 C CA  . ASP A 1 171 ? -115.792 -24.503 53.898 1.00 45.43 ? 171  ASP A CA  1 
ATOM   1299 C C   . ASP A 1 171 ? -114.526 -23.678 53.793 1.00 46.35 ? 171  ASP A C   1 
ATOM   1300 O O   . ASP A 1 171 ? -114.153 -23.209 52.708 1.00 46.72 ? 171  ASP A O   1 
ATOM   1301 C CB  . ASP A 1 171 ? -115.466 -25.891 54.433 1.00 45.15 ? 171  ASP A CB  1 
ATOM   1302 C CG  . ASP A 1 171 ? -114.797 -26.764 53.392 1.00 44.98 ? 171  ASP A CG  1 
ATOM   1303 O OD1 . ASP A 1 171 ? -115.185 -27.942 53.273 1.00 47.60 ? 171  ASP A OD1 1 
ATOM   1304 O OD2 . ASP A 1 171 ? -113.885 -26.274 52.693 1.00 44.15 ? 171  ASP A OD2 1 
ATOM   1305 N N   . ALA A 1 172 ? -113.867 -23.519 54.934 1.00 46.47 ? 172  ALA A N   1 
ATOM   1306 C CA  . ALA A 1 172 ? -112.644 -22.737 55.038 1.00 46.10 ? 172  ALA A CA  1 
ATOM   1307 C C   . ALA A 1 172 ? -111.495 -23.304 54.198 1.00 45.13 ? 172  ALA A C   1 
ATOM   1308 O O   . ALA A 1 172 ? -110.778 -22.561 53.533 1.00 44.18 ? 172  ALA A O   1 
ATOM   1309 C CB  . ALA A 1 172 ? -112.234 -22.641 56.512 1.00 45.98 ? 172  ALA A CB  1 
ATOM   1310 N N   . GLY A 1 173 ? -111.338 -24.624 54.218 1.00 45.52 ? 173  GLY A N   1 
ATOM   1311 C CA  . GLY A 1 173 ? -110.266 -25.262 53.473 1.00 44.38 ? 173  GLY A CA  1 
ATOM   1312 C C   . GLY A 1 173 ? -110.275 -25.136 51.958 1.00 44.45 ? 173  GLY A C   1 
ATOM   1313 O O   . GLY A 1 173 ? -109.235 -25.318 51.320 1.00 45.51 ? 173  GLY A O   1 
ATOM   1314 N N   . GLY A 1 174 ? -111.432 -24.852 51.367 1.00 42.61 ? 174  GLY A N   1 
ATOM   1315 C CA  . GLY A 1 174 ? -111.501 -24.744 49.919 1.00 39.22 ? 174  GLY A CA  1 
ATOM   1316 C C   . GLY A 1 174 ? -111.236 -23.372 49.329 1.00 37.37 ? 174  GLY A C   1 
ATOM   1317 O O   . GLY A 1 174 ? -111.406 -23.179 48.126 1.00 36.96 ? 174  GLY A O   1 
ATOM   1318 N N   . ALA A 1 175 ? -110.824 -22.423 50.163 1.00 35.84 ? 175  ALA A N   1 
ATOM   1319 C CA  . ALA A 1 175 ? -110.560 -21.063 49.706 1.00 37.45 ? 175  ALA A CA  1 
ATOM   1320 C C   . ALA A 1 175 ? -109.678 -20.978 48.460 1.00 39.44 ? 175  ALA A C   1 
ATOM   1321 O O   . ALA A 1 175 ? -110.051 -20.354 47.463 1.00 39.36 ? 175  ALA A O   1 
ATOM   1322 C CB  . ALA A 1 175 ? -109.931 -20.257 50.832 1.00 37.98 ? 175  ALA A CB  1 
ATOM   1323 N N   . LYS A 1 176 ? -108.506 -21.600 48.532 1.00 40.55 ? 176  LYS A N   1 
ATOM   1324 C CA  . LYS A 1 176 ? -107.537 -21.588 47.441 1.00 41.29 ? 176  LYS A CA  1 
ATOM   1325 C C   . LYS A 1 176 ? -108.141 -22.128 46.149 1.00 42.00 ? 176  LYS A C   1 
ATOM   1326 O O   . LYS A 1 176 ? -107.872 -21.621 45.060 1.00 40.81 ? 176  LYS A O   1 
ATOM   1327 C CB  . LYS A 1 176 ? -106.328 -22.427 47.842 1.00 43.68 ? 176  LYS A CB  1 
ATOM   1328 C CG  . LYS A 1 176 ? -104.985 -21.893 47.379 1.00 47.23 ? 176  LYS A CG  1 
ATOM   1329 C CD  . LYS A 1 176 ? -103.858 -22.795 47.896 1.00 51.98 ? 176  LYS A CD  1 
ATOM   1330 C CE  . LYS A 1 176 ? -102.470 -22.297 47.493 1.00 52.89 ? 176  LYS A CE  1 
ATOM   1331 N NZ  . LYS A 1 176 ? -102.088 -21.042 48.201 1.00 54.60 ? 176  LYS A NZ  1 
ATOM   1332 N N   . ARG A 1 177 ? -108.961 -23.165 46.274 1.00 41.77 ? 177  ARG A N   1 
ATOM   1333 C CA  . ARG A 1 177 ? -109.587 -23.768 45.108 1.00 40.77 ? 177  ARG A CA  1 
ATOM   1334 C C   . ARG A 1 177 ? -110.568 -22.807 44.425 1.00 39.94 ? 177  ARG A C   1 
ATOM   1335 O O   . ARG A 1 177 ? -110.497 -22.606 43.214 1.00 40.39 ? 177  ARG A O   1 
ATOM   1336 C CB  . ARG A 1 177 ? -110.307 -25.057 45.514 1.00 42.80 ? 177  ARG A CB  1 
ATOM   1337 C CG  . ARG A 1 177 ? -110.701 -25.950 44.355 1.00 43.88 ? 177  ARG A CG  1 
ATOM   1338 C CD  . ARG A 1 177 ? -111.377 -27.237 44.829 1.00 47.33 ? 177  ARG A CD  1 
ATOM   1339 N NE  . ARG A 1 177 ? -110.464 -28.102 45.574 1.00 48.73 ? 177  ARG A NE  1 
ATOM   1340 C CZ  . ARG A 1 177 ? -110.463 -28.244 46.899 1.00 50.49 ? 177  ARG A CZ  1 
ATOM   1341 N NH1 . ARG A 1 177 ? -111.339 -27.581 47.649 1.00 49.44 ? 177  ARG A NH1 1 
ATOM   1342 N NH2 . ARG A 1 177 ? -109.573 -29.045 47.477 1.00 49.84 ? 177  ARG A NH2 1 
ATOM   1343 N N   . VAL A 1 178 ? -111.469 -22.202 45.193 1.00 37.18 ? 178  VAL A N   1 
ATOM   1344 C CA  . VAL A 1 178 ? -112.440 -21.292 44.597 1.00 38.23 ? 178  VAL A CA  1 
ATOM   1345 C C   . VAL A 1 178 ? -111.829 -20.006 44.054 1.00 37.74 ? 178  VAL A C   1 
ATOM   1346 O O   . VAL A 1 178 ? -112.204 -19.566 42.972 1.00 37.68 ? 178  VAL A O   1 
ATOM   1347 C CB  . VAL A 1 178 ? -113.601 -20.932 45.583 1.00 38.98 ? 178  VAL A CB  1 
ATOM   1348 C CG1 . VAL A 1 178 ? -114.347 -22.193 45.985 1.00 35.05 ? 178  VAL A CG1 1 
ATOM   1349 C CG2 . VAL A 1 178 ? -113.062 -20.203 46.806 1.00 39.97 ? 178  VAL A CG2 1 
ATOM   1350 N N   . THR A 1 179 ? -110.892 -19.402 44.785 1.00 37.86 ? 179  THR A N   1 
ATOM   1351 C CA  . THR A 1 179 ? -110.267 -18.168 44.305 1.00 39.13 ? 179  THR A CA  1 
ATOM   1352 C C   . THR A 1 179 ? -109.495 -18.404 43.010 1.00 39.53 ? 179  THR A C   1 
ATOM   1353 O O   . THR A 1 179 ? -109.335 -17.497 42.199 1.00 40.10 ? 179  THR A O   1 
ATOM   1354 C CB  . THR A 1 179 ? -109.302 -17.555 45.346 1.00 37.63 ? 179  THR A CB  1 
ATOM   1355 O OG1 . THR A 1 179 ? -108.255 -18.486 45.650 1.00 41.75 ? 179  THR A OG1 1 
ATOM   1356 C CG2 . THR A 1 179 ? -110.046 -17.208 46.607 1.00 37.26 ? 179  THR A CG2 1 
ATOM   1357 N N   . SER A 1 180 ? -109.007 -19.622 42.818 1.00 41.10 ? 180  SER A N   1 
ATOM   1358 C CA  . SER A 1 180 ? -108.274 -19.947 41.601 1.00 42.27 ? 180  SER A CA  1 
ATOM   1359 C C   . SER A 1 180 ? -109.234 -19.922 40.417 1.00 42.74 ? 180  SER A C   1 
ATOM   1360 O O   . SER A 1 180 ? -108.894 -19.440 39.341 1.00 42.52 ? 180  SER A O   1 
ATOM   1361 C CB  . SER A 1 180 ? -107.641 -21.332 41.712 1.00 41.88 ? 180  SER A CB  1 
ATOM   1362 O OG  . SER A 1 180 ? -107.173 -21.764 40.449 1.00 45.95 ? 180  SER A OG  1 
ATOM   1363 N N   . ILE A 1 181 ? -110.437 -20.446 40.626 1.00 43.33 ? 181  ILE A N   1 
ATOM   1364 C CA  . ILE A 1 181 ? -111.446 -20.479 39.580 1.00 44.27 ? 181  ILE A CA  1 
ATOM   1365 C C   . ILE A 1 181 ? -112.028 -19.083 39.370 1.00 45.11 ? 181  ILE A C   1 
ATOM   1366 O O   . ILE A 1 181 ? -112.075 -18.580 38.244 1.00 45.79 ? 181  ILE A O   1 
ATOM   1367 C CB  . ILE A 1 181 ? -112.572 -21.471 39.941 1.00 44.29 ? 181  ILE A CB  1 
ATOM   1368 C CG1 . ILE A 1 181 ? -112.008 -22.896 39.940 1.00 44.78 ? 181  ILE A CG1 1 
ATOM   1369 C CG2 . ILE A 1 181 ? -113.728 -21.343 38.954 1.00 43.80 ? 181  ILE A CG2 1 
ATOM   1370 C CD1 . ILE A 1 181 ? -112.956 -23.938 40.469 1.00 43.59 ? 181  ILE A CD1 1 
ATOM   1371 N N   . ALA A 1 182 ? -112.463 -18.457 40.458 1.00 44.93 ? 182  ALA A N   1 
ATOM   1372 C CA  . ALA A 1 182 ? -113.025 -17.113 40.386 1.00 45.44 ? 182  ALA A CA  1 
ATOM   1373 C C   . ALA A 1 182 ? -112.068 -16.201 39.623 1.00 45.41 ? 182  ALA A C   1 
ATOM   1374 O O   . ALA A 1 182 ? -112.496 -15.387 38.805 1.00 45.71 ? 182  ALA A O   1 
ATOM   1375 C CB  . ALA A 1 182 ? -113.269 -16.568 41.787 1.00 44.97 ? 182  ALA A CB  1 
ATOM   1376 N N   . ASP A 1 183 ? -110.773 -16.352 39.888 1.00 44.50 ? 183  ASP A N   1 
ATOM   1377 C CA  . ASP A 1 183 ? -109.751 -15.553 39.223 1.00 46.13 ? 183  ASP A CA  1 
ATOM   1378 C C   . ASP A 1 183 ? -109.689 -15.824 37.719 1.00 47.71 ? 183  ASP A C   1 
ATOM   1379 O O   . ASP A 1 183 ? -109.578 -14.891 36.924 1.00 47.80 ? 183  ASP A O   1 
ATOM   1380 C CB  . ASP A 1 183 ? -108.377 -15.819 39.851 1.00 44.20 ? 183  ASP A CB  1 
ATOM   1381 C CG  . ASP A 1 183 ? -108.118 -14.971 41.086 1.00 44.62 ? 183  ASP A CG  1 
ATOM   1382 O OD1 . ASP A 1 183 ? -109.089 -14.515 41.726 1.00 42.54 ? 183  ASP A OD1 1 
ATOM   1383 O OD2 . ASP A 1 183 ? -106.934 -14.767 41.426 1.00 45.51 ? 183  ASP A OD2 1 
ATOM   1384 N N   . ARG A 1 184 ? -109.754 -17.095 37.328 1.00 49.17 ? 184  ARG A N   1 
ATOM   1385 C CA  . ARG A 1 184 ? -109.700 -17.454 35.911 1.00 50.32 ? 184  ARG A CA  1 
ATOM   1386 C C   . ARG A 1 184 ? -110.898 -16.918 35.134 1.00 50.75 ? 184  ARG A C   1 
ATOM   1387 O O   . ARG A 1 184 ? -110.766 -16.508 33.983 1.00 50.08 ? 184  ARG A O   1 
ATOM   1388 C CB  . ARG A 1 184 ? -109.637 -18.973 35.735 1.00 54.02 ? 184  ARG A CB  1 
ATOM   1389 C CG  . ARG A 1 184 ? -108.260 -19.527 35.386 1.00 61.49 ? 184  ARG A CG  1 
ATOM   1390 C CD  . ARG A 1 184 ? -107.463 -19.944 36.620 1.00 67.38 ? 184  ARG A CD  1 
ATOM   1391 N NE  . ARG A 1 184 ? -106.161 -20.503 36.254 1.00 72.91 ? 184  ARG A NE  1 
ATOM   1392 C CZ  . ARG A 1 184 ? -105.341 -21.139 37.091 1.00 74.83 ? 184  ARG A CZ  1 
ATOM   1393 N NH1 . ARG A 1 184 ? -105.671 -21.314 38.364 1.00 75.53 ? 184  ARG A NH1 1 
ATOM   1394 N NH2 . ARG A 1 184 ? -104.182 -21.604 36.649 1.00 77.44 ? 184  ARG A NH2 1 
ATOM   1395 N N   . LEU A 1 185 ? -112.064 -16.928 35.771 1.00 50.39 ? 185  LEU A N   1 
ATOM   1396 C CA  . LEU A 1 185 ? -113.295 -16.461 35.149 1.00 49.62 ? 185  LEU A CA  1 
ATOM   1397 C C   . LEU A 1 185 ? -113.501 -14.962 35.321 1.00 50.93 ? 185  LEU A C   1 
ATOM   1398 O O   . LEU A 1 185 ? -114.382 -14.373 34.689 1.00 51.02 ? 185  LEU A O   1 
ATOM   1399 C CB  . LEU A 1 185 ? -114.486 -17.192 35.761 1.00 49.87 ? 185  LEU A CB  1 
ATOM   1400 C CG  . LEU A 1 185 ? -114.491 -18.713 35.623 1.00 48.81 ? 185  LEU A CG  1 
ATOM   1401 C CD1 . LEU A 1 185 ? -115.649 -19.281 36.409 1.00 47.58 ? 185  LEU A CD1 1 
ATOM   1402 C CD2 . LEU A 1 185 ? -114.596 -19.093 34.150 1.00 50.71 ? 185  LEU A CD2 1 
ATOM   1403 N N   . ASN A 1 186 ? -112.684 -14.355 36.179 1.00 50.32 ? 186  ASN A N   1 
ATOM   1404 C CA  . ASN A 1 186 ? -112.778 -12.930 36.479 1.00 49.98 ? 186  ASN A CA  1 
ATOM   1405 C C   . ASN A 1 186 ? -114.083 -12.598 37.186 1.00 48.59 ? 186  ASN A C   1 
ATOM   1406 O O   . ASN A 1 186 ? -114.835 -11.735 36.739 1.00 48.97 ? 186  ASN A O   1 
ATOM   1407 C CB  . ASN A 1 186 ? -112.660 -12.096 35.201 1.00 52.40 ? 186  ASN A CB  1 
ATOM   1408 C CG  . ASN A 1 186 ? -111.234 -11.686 34.908 1.00 55.28 ? 186  ASN A CG  1 
ATOM   1409 O OD1 . ASN A 1 186 ? -110.607 -10.976 35.701 1.00 57.41 ? 186  ASN A OD1 1 
ATOM   1410 N ND2 . ASN A 1 186 ? -110.709 -12.128 33.770 1.00 57.27 ? 186  ASN A ND2 1 
ATOM   1411 N N   . VAL A 1 187 ? -114.359 -13.287 38.288 1.00 46.61 ? 187  VAL A N   1 
ATOM   1412 C CA  . VAL A 1 187 ? -115.584 -13.034 39.031 1.00 44.40 ? 187  VAL A CA  1 
ATOM   1413 C C   . VAL A 1 187 ? -115.340 -13.082 40.541 1.00 43.11 ? 187  VAL A C   1 
ATOM   1414 O O   . VAL A 1 187 ? -114.197 -13.232 40.975 1.00 41.75 ? 187  VAL A O   1 
ATOM   1415 C CB  . VAL A 1 187 ? -116.671 -14.046 38.632 1.00 45.98 ? 187  VAL A CB  1 
ATOM   1416 C CG1 . VAL A 1 187 ? -116.771 -14.115 37.104 1.00 45.09 ? 187  VAL A CG1 1 
ATOM   1417 C CG2 . VAL A 1 187 ? -116.348 -15.417 39.207 1.00 46.67 ? 187  VAL A CG2 1 
ATOM   1418 N N   . ASP A 1 188 ? -116.412 -12.953 41.327 1.00 41.83 ? 188  ASP A N   1 
ATOM   1419 C CA  . ASP A 1 188 ? -116.329 -12.955 42.791 1.00 42.43 ? 188  ASP A CA  1 
ATOM   1420 C C   . ASP A 1 188 ? -116.253 -14.340 43.400 1.00 42.60 ? 188  ASP A C   1 
ATOM   1421 O O   . ASP A 1 188 ? -116.710 -15.321 42.814 1.00 44.30 ? 188  ASP A O   1 
ATOM   1422 C CB  . ASP A 1 188 ? -117.549 -12.268 43.421 1.00 42.09 ? 188  ASP A CB  1 
ATOM   1423 C CG  . ASP A 1 188 ? -117.689 -10.816 43.020 1.00 41.29 ? 188  ASP A CG  1 
ATOM   1424 O OD1 . ASP A 1 188 ? -116.696 -10.209 42.562 1.00 40.27 ? 188  ASP A OD1 1 
ATOM   1425 O OD2 . ASP A 1 188 ? -118.807 -10.285 43.181 1.00 41.68 ? 188  ASP A OD2 1 
ATOM   1426 N N   . PHE A 1 189 ? -115.702 -14.398 44.606 1.00 40.67 ? 189  PHE A N   1 
ATOM   1427 C CA  . PHE A 1 189 ? -115.593 -15.643 45.339 1.00 39.01 ? 189  PHE A CA  1 
ATOM   1428 C C   . PHE A 1 189 ? -116.136 -15.357 46.723 1.00 38.40 ? 189  PHE A C   1 
ATOM   1429 O O   . PHE A 1 189 ? -116.143 -14.212 47.184 1.00 38.22 ? 189  PHE A O   1 
ATOM   1430 C CB  . PHE A 1 189 ? -114.133 -16.122 45.402 1.00 37.74 ? 189  PHE A CB  1 
ATOM   1431 C CG  . PHE A 1 189 ? -113.283 -15.371 46.377 1.00 36.66 ? 189  PHE A CG  1 
ATOM   1432 C CD1 . PHE A 1 189 ? -113.296 -15.711 47.720 1.00 36.23 ? 189  PHE A CD1 1 
ATOM   1433 C CD2 . PHE A 1 189 ? -112.478 -14.319 45.963 1.00 35.99 ? 189  PHE A CD2 1 
ATOM   1434 C CE1 . PHE A 1 189 ? -112.518 -15.025 48.641 1.00 35.48 ? 189  PHE A CE1 1 
ATOM   1435 C CE2 . PHE A 1 189 ? -111.688 -13.618 46.887 1.00 36.89 ? 189  PHE A CE2 1 
ATOM   1436 C CZ  . PHE A 1 189 ? -111.713 -13.975 48.227 1.00 34.27 ? 189  PHE A CZ  1 
ATOM   1437 N N   . ALA A 1 190 ? -116.586 -16.403 47.388 1.00 38.73 ? 190  ALA A N   1 
ATOM   1438 C CA  . ALA A 1 190 ? -117.142 -16.271 48.712 1.00 39.28 ? 190  ALA A CA  1 
ATOM   1439 C C   . ALA A 1 190 ? -116.852 -17.589 49.391 1.00 39.74 ? 190  ALA A C   1 
ATOM   1440 O O   . ALA A 1 190 ? -116.653 -18.597 48.719 1.00 39.79 ? 190  ALA A O   1 
ATOM   1441 C CB  . ALA A 1 190 ? -118.632 -16.035 48.611 1.00 36.62 ? 190  ALA A CB  1 
ATOM   1442 N N   . LEU A 1 191 ? -116.811 -17.588 50.714 1.00 39.81 ? 191  LEU A N   1 
ATOM   1443 C CA  . LEU A 1 191 ? -116.534 -18.812 51.440 1.00 41.55 ? 191  LEU A CA  1 
ATOM   1444 C C   . LEU A 1 191 ? -117.482 -18.934 52.616 1.00 41.46 ? 191  LEU A C   1 
ATOM   1445 O O   . LEU A 1 191 ? -117.885 -17.933 53.206 1.00 41.90 ? 191  LEU A O   1 
ATOM   1446 C CB  . LEU A 1 191 ? -115.071 -18.829 51.904 1.00 41.11 ? 191  LEU A CB  1 
ATOM   1447 C CG  . LEU A 1 191 ? -114.628 -19.894 52.910 1.00 43.97 ? 191  LEU A CG  1 
ATOM   1448 C CD1 . LEU A 1 191 ? -113.122 -20.121 52.789 1.00 45.09 ? 191  LEU A CD1 1 
ATOM   1449 C CD2 . LEU A 1 191 ? -115.005 -19.453 54.322 1.00 43.35 ? 191  LEU A CD2 1 
ATOM   1450 N N   . ILE A 1 192 ? -117.841 -20.170 52.939 1.00 42.71 ? 192  ILE A N   1 
ATOM   1451 C CA  . ILE A 1 192 ? -118.736 -20.452 54.049 1.00 45.84 ? 192  ILE A CA  1 
ATOM   1452 C C   . ILE A 1 192 ? -117.965 -21.210 55.119 1.00 46.59 ? 192  ILE A C   1 
ATOM   1453 O O   . ILE A 1 192 ? -117.038 -21.951 54.815 1.00 47.27 ? 192  ILE A O   1 
ATOM   1454 C CB  . ILE A 1 192 ? -119.955 -21.290 53.593 1.00 45.60 ? 192  ILE A CB  1 
ATOM   1455 C CG1 . ILE A 1 192 ? -120.842 -20.448 52.672 1.00 45.23 ? 192  ILE A CG1 1 
ATOM   1456 C CG2 . ILE A 1 192 ? -120.755 -21.758 54.799 1.00 45.36 ? 192  ILE A CG2 1 
ATOM   1457 C CD1 . ILE A 1 192 ? -122.019 -21.201 52.100 1.00 46.31 ? 192  ILE A CD1 1 
ATOM   1458 N N   . HIS A 1 193 ? -118.353 -21.008 56.372 1.00 48.97 ? 193  HIS A N   1 
ATOM   1459 C CA  . HIS A 1 193 ? -117.697 -21.656 57.495 1.00 50.75 ? 193  HIS A CA  1 
ATOM   1460 C C   . HIS A 1 193 ? -118.720 -22.002 58.566 1.00 54.42 ? 193  HIS A C   1 
ATOM   1461 O O   . HIS A 1 193 ? -119.561 -21.176 58.908 1.00 52.42 ? 193  HIS A O   1 
ATOM   1462 C CB  . HIS A 1 193 ? -116.634 -20.719 58.079 1.00 48.85 ? 193  HIS A CB  1 
ATOM   1463 C CG  . HIS A 1 193 ? -116.019 -21.214 59.351 1.00 46.72 ? 193  HIS A CG  1 
ATOM   1464 N ND1 . HIS A 1 193 ? -115.376 -22.431 59.446 1.00 45.69 ? 193  HIS A ND1 1 
ATOM   1465 C CD2 . HIS A 1 193 ? -115.945 -20.654 60.582 1.00 45.78 ? 193  HIS A CD2 1 
ATOM   1466 C CE1 . HIS A 1 193 ? -114.935 -22.600 60.679 1.00 43.67 ? 193  HIS A CE1 1 
ATOM   1467 N NE2 . HIS A 1 193 ? -115.268 -21.536 61.388 1.00 47.33 ? 193  HIS A NE2 1 
ATOM   1468 N N   . LYS A 1 194 ? -118.660 -23.228 59.080 1.00 59.31 ? 194  LYS A N   1 
ATOM   1469 C CA  . LYS A 1 194 ? -119.573 -23.641 60.139 1.00 66.18 ? 194  LYS A CA  1 
ATOM   1470 C C   . LYS A 1 194 ? -118.949 -23.312 61.489 1.00 69.96 ? 194  LYS A C   1 
ATOM   1471 O O   . LYS A 1 194 ? -117.876 -23.819 61.825 1.00 69.50 ? 194  LYS A O   1 
ATOM   1472 C CB  . LYS A 1 194 ? -119.870 -25.143 60.070 1.00 69.02 ? 194  LYS A CB  1 
ATOM   1473 C CG  . LYS A 1 194 ? -121.078 -25.508 59.225 1.00 72.63 ? 194  LYS A CG  1 
ATOM   1474 C CD  . LYS A 1 194 ? -121.606 -26.902 59.568 1.00 74.37 ? 194  LYS A CD  1 
ATOM   1475 C CE  . LYS A 1 194 ? -122.923 -27.187 58.842 1.00 75.38 ? 194  LYS A CE  1 
ATOM   1476 N NZ  . LYS A 1 194 ? -123.545 -28.493 59.220 1.00 74.97 ? 194  LYS A NZ  1 
ATOM   1477 N N   . GLU A 1 195 ? -119.627 -22.459 62.254 1.00 74.68 ? 195  GLU A N   1 
ATOM   1478 C CA  . GLU A 1 195 ? -119.153 -22.045 63.572 1.00 78.45 ? 195  GLU A CA  1 
ATOM   1479 C C   . GLU A 1 195 ? -118.863 -23.270 64.428 1.00 79.83 ? 195  GLU A C   1 
ATOM   1480 O O   . GLU A 1 195 ? -119.710 -24.150 64.561 1.00 80.30 ? 195  GLU A O   1 
ATOM   1481 C CB  . GLU A 1 195 ? -120.210 -21.180 64.263 1.00 80.51 ? 195  GLU A CB  1 
ATOM   1482 C CG  . GLU A 1 195 ? -119.663 -19.911 64.896 1.00 84.17 ? 195  GLU A CG  1 
ATOM   1483 C CD  . GLU A 1 195 ? -119.206 -18.900 63.862 1.00 85.87 ? 195  GLU A CD  1 
ATOM   1484 O OE1 . GLU A 1 195 ? -118.331 -19.244 63.036 1.00 85.97 ? 195  GLU A OE1 1 
ATOM   1485 O OE2 . GLU A 1 195 ? -119.724 -17.762 63.873 1.00 86.11 ? 195  GLU A OE2 1 
ATOM   1486 N N   . ARG A 1 196 ? -117.667 -23.323 65.008 1.00 81.52 ? 196  ARG A N   1 
ATOM   1487 C CA  . ARG A 1 196 ? -117.275 -24.452 65.846 1.00 82.80 ? 196  ARG A CA  1 
ATOM   1488 C C   . ARG A 1 196 ? -116.933 -24.008 67.263 1.00 82.55 ? 196  ARG A C   1 
ATOM   1489 O O   . ARG A 1 196 ? -116.849 -22.813 67.545 1.00 81.62 ? 196  ARG A O   1 
ATOM   1490 C CB  . ARG A 1 196 ? -116.073 -25.166 65.225 1.00 84.52 ? 196  ARG A CB  1 
ATOM   1491 C CG  . ARG A 1 196 ? -116.306 -25.612 63.791 1.00 87.90 ? 196  ARG A CG  1 
ATOM   1492 C CD  . ARG A 1 196 ? -115.033 -26.144 63.160 1.00 90.77 ? 196  ARG A CD  1 
ATOM   1493 N NE  . ARG A 1 196 ? -115.184 -26.370 61.724 1.00 93.75 ? 196  ARG A NE  1 
ATOM   1494 C CZ  . ARG A 1 196 ? -114.181 -26.687 60.912 1.00 95.25 ? 196  ARG A CZ  1 
ATOM   1495 N NH1 . ARG A 1 196 ? -112.952 -26.816 61.397 1.00 96.05 ? 196  ARG A NH1 1 
ATOM   1496 N NH2 . ARG A 1 196 ? -114.400 -26.869 59.614 1.00 95.30 ? 196  ARG A NH2 1 
ATOM   1497 N N   . ASP A 1 203 ? -124.052 -25.839 65.440 1.00 81.56 ? 203  ASP A N   1 
ATOM   1498 C CA  . ASP A 1 203 ? -123.197 -24.926 64.691 1.00 81.27 ? 203  ASP A CA  1 
ATOM   1499 C C   . ASP A 1 203 ? -123.988 -24.158 63.635 1.00 80.63 ? 203  ASP A C   1 
ATOM   1500 O O   . ASP A 1 203 ? -124.918 -24.692 63.030 1.00 80.59 ? 203  ASP A O   1 
ATOM   1501 C CB  . ASP A 1 203 ? -122.067 -25.701 64.010 1.00 82.02 ? 203  ASP A CB  1 
ATOM   1502 C CG  . ASP A 1 203 ? -121.227 -26.492 64.993 1.00 82.77 ? 203  ASP A CG  1 
ATOM   1503 O OD1 . ASP A 1 203 ? -120.765 -25.904 65.995 1.00 82.65 ? 203  ASP A OD1 1 
ATOM   1504 O OD2 . ASP A 1 203 ? -121.025 -27.702 64.758 1.00 83.73 ? 203  ASP A OD2 1 
ATOM   1505 N N   . ARG A 1 204 ? -123.610 -22.902 63.421 1.00 79.82 ? 204  ARG A N   1 
ATOM   1506 C CA  . ARG A 1 204 ? -124.269 -22.051 62.431 1.00 78.27 ? 204  ARG A CA  1 
ATOM   1507 C C   . ARG A 1 204 ? -123.263 -21.712 61.337 1.00 75.17 ? 204  ARG A C   1 
ATOM   1508 O O   . ARG A 1 204 ? -122.085 -21.497 61.621 1.00 75.44 ? 204  ARG A O   1 
ATOM   1509 C CB  . ARG A 1 204 ? -124.751 -20.752 63.081 1.00 80.62 ? 204  ARG A CB  1 
ATOM   1510 C CG  . ARG A 1 204 ? -123.619 -19.792 63.429 1.00 84.23 ? 204  ARG A CG  1 
ATOM   1511 C CD  . ARG A 1 204 ? -124.139 -18.492 64.011 1.00 87.42 ? 204  ARG A CD  1 
ATOM   1512 N NE  . ARG A 1 204 ? -123.078 -17.499 64.148 1.00 90.64 ? 204  ARG A NE  1 
ATOM   1513 C CZ  . ARG A 1 204 ? -123.228 -16.325 64.752 1.00 92.38 ? 204  ARG A CZ  1 
ATOM   1514 N NH1 . ARG A 1 204 ? -124.398 -15.993 65.282 1.00 93.90 ? 204  ARG A NH1 1 
ATOM   1515 N NH2 . ARG A 1 204 ? -122.210 -15.479 64.826 1.00 93.91 ? 204  ARG A NH2 1 
ATOM   1516 N N   . MET A 1 205 ? -123.716 -21.654 60.091 1.00 70.87 ? 205  MET A N   1 
ATOM   1517 C CA  . MET A 1 205 ? -122.808 -21.328 59.002 1.00 66.51 ? 205  MET A CA  1 
ATOM   1518 C C   . MET A 1 205 ? -122.695 -19.824 58.797 1.00 63.67 ? 205  MET A C   1 
ATOM   1519 O O   . MET A 1 205 ? -123.675 -19.094 58.922 1.00 62.80 ? 205  MET A O   1 
ATOM   1520 C CB  . MET A 1 205 ? -123.261 -21.988 57.698 1.00 67.26 ? 205  MET A CB  1 
ATOM   1521 C CG  . MET A 1 205 ? -123.293 -23.508 57.748 1.00 68.09 ? 205  MET A CG  1 
ATOM   1522 S SD  . MET A 1 205 ? -123.259 -24.258 56.107 1.00 68.65 ? 205  MET A SD  1 
ATOM   1523 C CE  . MET A 1 205 ? -124.644 -23.456 55.357 1.00 70.92 ? 205  MET A CE  1 
ATOM   1524 N N   . VAL A 1 206 ? -121.484 -19.373 58.487 1.00 59.90 ? 206  VAL A N   1 
ATOM   1525 C CA  . VAL A 1 206 ? -121.213 -17.964 58.242 1.00 56.72 ? 206  VAL A CA  1 
ATOM   1526 C C   . VAL A 1 206 ? -120.780 -17.829 56.788 1.00 54.95 ? 206  VAL A C   1 
ATOM   1527 O O   . VAL A 1 206 ? -120.167 -18.741 56.232 1.00 54.43 ? 206  VAL A O   1 
ATOM   1528 C CB  . VAL A 1 206 ? -120.077 -17.442 59.152 1.00 57.28 ? 206  VAL A CB  1 
ATOM   1529 C CG1 . VAL A 1 206 ? -119.788 -15.987 58.843 1.00 58.43 ? 206  VAL A CG1 1 
ATOM   1530 C CG2 . VAL A 1 206 ? -120.463 -17.598 60.608 1.00 57.87 ? 206  VAL A CG2 1 
ATOM   1531 N N   . LEU A 1 207 ? -121.100 -16.695 56.175 1.00 52.81 ? 207  LEU A N   1 
ATOM   1532 C CA  . LEU A 1 207 ? -120.740 -16.463 54.786 1.00 51.04 ? 207  LEU A CA  1 
ATOM   1533 C C   . LEU A 1 207 ? -120.039 -15.127 54.611 1.00 50.42 ? 207  LEU A C   1 
ATOM   1534 O O   . LEU A 1 207 ? -120.524 -14.091 55.067 1.00 50.38 ? 207  LEU A O   1 
ATOM   1535 C CB  . LEU A 1 207 ? -121.990 -16.502 53.901 1.00 51.04 ? 207  LEU A CB  1 
ATOM   1536 C CG  . LEU A 1 207 ? -121.822 -16.562 52.374 1.00 51.22 ? 207  LEU A CG  1 
ATOM   1537 C CD1 . LEU A 1 207 ? -123.163 -16.886 51.747 1.00 51.67 ? 207  LEU A CD1 1 
ATOM   1538 C CD2 . LEU A 1 207 ? -121.291 -15.255 51.828 1.00 50.45 ? 207  LEU A CD2 1 
ATOM   1539 N N   . VAL A 1 208 ? -118.886 -15.166 53.955 1.00 48.46 ? 208  VAL A N   1 
ATOM   1540 C CA  . VAL A 1 208 ? -118.121 -13.965 53.685 1.00 47.15 ? 208  VAL A CA  1 
ATOM   1541 C C   . VAL A 1 208 ? -117.953 -13.869 52.182 1.00 47.08 ? 208  VAL A C   1 
ATOM   1542 O O   . VAL A 1 208 ? -117.462 -14.793 51.543 1.00 47.54 ? 208  VAL A O   1 
ATOM   1543 C CB  . VAL A 1 208 ? -116.740 -14.000 54.362 1.00 45.71 ? 208  VAL A CB  1 
ATOM   1544 C CG1 . VAL A 1 208 ? -116.914 -14.123 55.863 1.00 44.32 ? 208  VAL A CG1 1 
ATOM   1545 C CG2 . VAL A 1 208 ? -115.918 -15.151 53.823 1.00 44.53 ? 208  VAL A CG2 1 
ATOM   1546 N N   . GLY A 1 209 ? -118.374 -12.744 51.621 1.00 47.39 ? 209  GLY A N   1 
ATOM   1547 C CA  . GLY A 1 209 ? -118.282 -12.556 50.185 1.00 48.20 ? 209  GLY A CA  1 
ATOM   1548 C C   . GLY A 1 209 ? -119.631 -12.156 49.624 1.00 48.28 ? 209  GLY A C   1 
ATOM   1549 O O   . GLY A 1 209 ? -120.658 -12.346 50.265 1.00 46.65 ? 209  GLY A O   1 
ATOM   1550 N N   . ASP A 1 210 ? -119.627 -11.604 48.420 1.00 50.64 ? 210  ASP A N   1 
ATOM   1551 C CA  . ASP A 1 210 ? -120.838 -11.105 47.785 1.00 53.06 ? 210  ASP A CA  1 
ATOM   1552 C C   . ASP A 1 210 ? -121.521 -12.084 46.827 1.00 53.99 ? 210  ASP A C   1 
ATOM   1553 O O   . ASP A 1 210 ? -120.973 -12.416 45.768 1.00 54.43 ? 210  ASP A O   1 
ATOM   1554 C CB  . ASP A 1 210 ? -120.478 -9.801  47.053 1.00 54.93 ? 210  ASP A CB  1 
ATOM   1555 C CG  . ASP A 1 210 ? -121.662 -9.167  46.351 1.00 57.33 ? 210  ASP A CG  1 
ATOM   1556 O OD1 . ASP A 1 210 ? -122.808 -9.509  46.711 1.00 59.78 ? 210  ASP A OD1 1 
ATOM   1557 O OD2 . ASP A 1 210 ? -121.447 -8.316  45.453 1.00 57.10 ? 210  ASP A OD2 1 
ATOM   1558 N N   . VAL A 1 211 ? -122.725 -12.528 47.198 1.00 54.93 ? 211  VAL A N   1 
ATOM   1559 C CA  . VAL A 1 211 ? -123.519 -13.458 46.383 1.00 55.43 ? 211  VAL A CA  1 
ATOM   1560 C C   . VAL A 1 211 ? -124.926 -12.934 46.083 1.00 56.37 ? 211  VAL A C   1 
ATOM   1561 O O   . VAL A 1 211 ? -125.663 -13.540 45.305 1.00 57.06 ? 211  VAL A O   1 
ATOM   1562 C CB  . VAL A 1 211 ? -123.707 -14.839 47.078 1.00 54.68 ? 211  VAL A CB  1 
ATOM   1563 C CG1 . VAL A 1 211 ? -122.355 -15.490 47.345 1.00 54.37 ? 211  VAL A CG1 1 
ATOM   1564 C CG2 . VAL A 1 211 ? -124.496 -14.676 48.360 1.00 53.05 ? 211  VAL A CG2 1 
ATOM   1565 N N   . LYS A 1 212 ? -125.292 -11.820 46.711 1.00 57.76 ? 212  LYS A N   1 
ATOM   1566 C CA  . LYS A 1 212 ? -126.612 -11.207 46.545 1.00 58.36 ? 212  LYS A CA  1 
ATOM   1567 C C   . LYS A 1 212 ? -126.965 -10.923 45.084 1.00 58.36 ? 212  LYS A C   1 
ATOM   1568 O O   . LYS A 1 212 ? -126.210 -10.256 44.371 1.00 57.44 ? 212  LYS A O   1 
ATOM   1569 C CB  . LYS A 1 212 ? -126.673 -9.894  47.338 1.00 60.84 ? 212  LYS A CB  1 
ATOM   1570 C CG  . LYS A 1 212 ? -128.067 -9.290  47.499 1.00 63.11 ? 212  LYS A CG  1 
ATOM   1571 C CD  . LYS A 1 212 ? -128.919 -10.098 48.471 1.00 64.97 ? 212  LYS A CD  1 
ATOM   1572 C CE  . LYS A 1 212 ? -130.323 -9.518  48.591 1.00 66.71 ? 212  LYS A CE  1 
ATOM   1573 N NZ  . LYS A 1 212 ? -131.368 -10.571 48.796 1.00 67.48 ? 212  LYS A NZ  1 
ATOM   1574 N N   . ASP A 1 213 ? -128.123 -11.425 44.657 1.00 58.02 ? 213  ASP A N   1 
ATOM   1575 C CA  . ASP A 1 213 ? -128.622 -11.229 43.296 1.00 58.08 ? 213  ASP A CA  1 
ATOM   1576 C C   . ASP A 1 213 ? -127.652 -11.663 42.208 1.00 57.34 ? 213  ASP A C   1 
ATOM   1577 O O   . ASP A 1 213 ? -127.387 -10.920 41.261 1.00 57.27 ? 213  ASP A O   1 
ATOM   1578 C CB  . ASP A 1 213 ? -129.001 -9.764  43.078 1.00 59.36 ? 213  ASP A CB  1 
ATOM   1579 C CG  . ASP A 1 213 ? -130.093 -9.302  44.020 1.00 61.87 ? 213  ASP A CG  1 
ATOM   1580 O OD1 . ASP A 1 213 ? -130.344 -8.078  44.086 1.00 64.48 ? 213  ASP A OD1 1 
ATOM   1581 O OD2 . ASP A 1 213 ? -130.705 -10.162 44.693 1.00 62.69 ? 213  ASP A OD2 1 
ATOM   1582 N N   . ARG A 1 214 ? -127.121 -12.868 42.355 1.00 56.53 ? 214  ARG A N   1 
ATOM   1583 C CA  . ARG A 1 214 ? -126.198 -13.422 41.372 1.00 55.95 ? 214  ARG A CA  1 
ATOM   1584 C C   . ARG A 1 214 ? -126.052 -14.927 41.560 1.00 53.53 ? 214  ARG A C   1 
ATOM   1585 O O   . ARG A 1 214 ? -126.258 -15.445 42.655 1.00 54.27 ? 214  ARG A O   1 
ATOM   1586 C CB  . ARG A 1 214 ? -124.837 -12.713 41.445 1.00 56.30 ? 214  ARG A CB  1 
ATOM   1587 C CG  . ARG A 1 214 ? -124.262 -12.509 42.835 1.00 57.22 ? 214  ARG A CG  1 
ATOM   1588 C CD  . ARG A 1 214 ? -123.131 -11.478 42.782 1.00 57.32 ? 214  ARG A CD  1 
ATOM   1589 N NE  . ARG A 1 214 ? -122.039 -11.899 41.907 1.00 57.31 ? 214  ARG A NE  1 
ATOM   1590 C CZ  . ARG A 1 214 ? -121.167 -11.070 41.340 1.00 57.28 ? 214  ARG A CZ  1 
ATOM   1591 N NH1 . ARG A 1 214 ? -121.253 -9.765  41.550 1.00 58.47 ? 214  ARG A NH1 1 
ATOM   1592 N NH2 . ARG A 1 214 ? -120.205 -11.547 40.561 1.00 56.18 ? 214  ARG A NH2 1 
ATOM   1593 N N   . VAL A 1 215 ? -125.726 -15.634 40.485 1.00 51.17 ? 215  VAL A N   1 
ATOM   1594 C CA  . VAL A 1 215 ? -125.593 -17.083 40.556 1.00 50.22 ? 215  VAL A CA  1 
ATOM   1595 C C   . VAL A 1 215 ? -124.426 -17.523 41.429 1.00 48.14 ? 215  VAL A C   1 
ATOM   1596 O O   . VAL A 1 215 ? -123.309 -17.036 41.281 1.00 48.19 ? 215  VAL A O   1 
ATOM   1597 C CB  . VAL A 1 215 ? -125.416 -17.695 39.151 1.00 50.87 ? 215  VAL A CB  1 
ATOM   1598 C CG1 . VAL A 1 215 ? -125.351 -19.215 39.252 1.00 50.02 ? 215  VAL A CG1 1 
ATOM   1599 C CG2 . VAL A 1 215 ? -126.565 -17.268 38.255 1.00 50.27 ? 215  VAL A CG2 1 
ATOM   1600 N N   . ALA A 1 216 ? -124.697 -18.453 42.335 1.00 46.37 ? 216  ALA A N   1 
ATOM   1601 C CA  . ALA A 1 216 ? -123.673 -18.973 43.229 1.00 46.29 ? 216  ALA A CA  1 
ATOM   1602 C C   . ALA A 1 216 ? -123.244 -20.363 42.771 1.00 45.23 ? 216  ALA A C   1 
ATOM   1603 O O   . ALA A 1 216 ? -124.075 -21.262 42.642 1.00 44.59 ? 216  ALA A O   1 
ATOM   1604 C CB  . ALA A 1 216 ? -124.209 -19.037 44.662 1.00 43.16 ? 216  ALA A CB  1 
ATOM   1605 N N   . ILE A 1 217 ? -121.951 -20.532 42.514 1.00 44.80 ? 217  ILE A N   1 
ATOM   1606 C CA  . ILE A 1 217 ? -121.434 -21.831 42.095 1.00 44.05 ? 217  ILE A CA  1 
ATOM   1607 C C   . ILE A 1 217 ? -120.543 -22.426 43.183 1.00 43.63 ? 217  ILE A C   1 
ATOM   1608 O O   . ILE A 1 217 ? -119.415 -21.982 43.389 1.00 42.35 ? 217  ILE A O   1 
ATOM   1609 C CB  . ILE A 1 217 ? -120.600 -21.738 40.799 1.00 43.89 ? 217  ILE A CB  1 
ATOM   1610 C CG1 . ILE A 1 217 ? -121.426 -21.132 39.665 1.00 41.74 ? 217  ILE A CG1 1 
ATOM   1611 C CG2 . ILE A 1 217 ? -120.132 -23.121 40.392 1.00 42.58 ? 217  ILE A CG2 1 
ATOM   1612 C CD1 . ILE A 1 217 ? -120.634 -20.968 38.377 1.00 40.08 ? 217  ILE A CD1 1 
ATOM   1613 N N   . LEU A 1 218 ? -121.067 -23.423 43.884 1.00 42.66 ? 218  LEU A N   1 
ATOM   1614 C CA  . LEU A 1 218 ? -120.322 -24.094 44.929 1.00 41.81 ? 218  LEU A CA  1 
ATOM   1615 C C   . LEU A 1 218 ? -119.311 -25.031 44.289 1.00 43.74 ? 218  LEU A C   1 
ATOM   1616 O O   . LEU A 1 218 ? -119.670 -25.899 43.486 1.00 43.41 ? 218  LEU A O   1 
ATOM   1617 C CB  . LEU A 1 218 ? -121.267 -24.883 45.831 1.00 40.43 ? 218  LEU A CB  1 
ATOM   1618 C CG  . LEU A 1 218 ? -122.005 -24.029 46.861 1.00 40.99 ? 218  LEU A CG  1 
ATOM   1619 C CD1 . LEU A 1 218 ? -123.178 -24.806 47.449 1.00 40.79 ? 218  LEU A CD1 1 
ATOM   1620 C CD2 . LEU A 1 218 ? -121.021 -23.597 47.955 1.00 40.64 ? 218  LEU A CD2 1 
ATOM   1621 N N   . VAL A 1 219 ? -118.045 -24.840 44.640 1.00 43.48 ? 219  VAL A N   1 
ATOM   1622 C CA  . VAL A 1 219 ? -116.972 -25.662 44.108 1.00 44.85 ? 219  VAL A CA  1 
ATOM   1623 C C   . VAL A 1 219 ? -116.236 -26.363 45.241 1.00 46.64 ? 219  VAL A C   1 
ATOM   1624 O O   . VAL A 1 219 ? -115.885 -25.747 46.252 1.00 45.51 ? 219  VAL A O   1 
ATOM   1625 C CB  . VAL A 1 219 ? -115.961 -24.822 43.305 1.00 44.97 ? 219  VAL A CB  1 
ATOM   1626 C CG1 . VAL A 1 219 ? -114.872 -25.717 42.746 1.00 45.46 ? 219  VAL A CG1 1 
ATOM   1627 C CG2 . VAL A 1 219 ? -116.674 -24.088 42.182 1.00 45.35 ? 219  VAL A CG2 1 
ATOM   1628 N N   . ASP A 1 220 ? -116.013 -27.658 45.059 1.00 47.75 ? 220  ASP A N   1 
ATOM   1629 C CA  . ASP A 1 220 ? -115.327 -28.472 46.047 1.00 49.67 ? 220  ASP A CA  1 
ATOM   1630 C C   . ASP A 1 220 ? -114.668 -29.641 45.316 1.00 50.57 ? 220  ASP A C   1 
ATOM   1631 O O   . ASP A 1 220 ? -115.164 -30.090 44.280 1.00 50.56 ? 220  ASP A O   1 
ATOM   1632 C CB  . ASP A 1 220 ? -116.337 -28.979 47.080 1.00 50.07 ? 220  ASP A CB  1 
ATOM   1633 C CG  . ASP A 1 220 ? -115.672 -29.532 48.324 1.00 52.59 ? 220  ASP A CG  1 
ATOM   1634 O OD1 . ASP A 1 220 ? -114.443 -29.353 48.471 1.00 52.44 ? 220  ASP A OD1 1 
ATOM   1635 O OD2 . ASP A 1 220 ? -116.381 -30.138 49.158 1.00 54.07 ? 220  ASP A OD2 1 
ATOM   1636 N N   . ASP A 1 221 ? -113.547 -30.128 45.838 1.00 51.13 ? 221  ASP A N   1 
ATOM   1637 C CA  . ASP A 1 221 ? -112.859 -31.238 45.187 1.00 51.77 ? 221  ASP A CA  1 
ATOM   1638 C C   . ASP A 1 221 ? -113.679 -32.522 45.229 1.00 52.51 ? 221  ASP A C   1 
ATOM   1639 O O   . ASP A 1 221 ? -113.602 -33.344 44.312 1.00 53.22 ? 221  ASP A O   1 
ATOM   1640 C CB  . ASP A 1 221 ? -111.490 -31.480 45.823 1.00 50.89 ? 221  ASP A CB  1 
ATOM   1641 C CG  . ASP A 1 221 ? -111.584 -31.980 47.247 1.00 51.57 ? 221  ASP A CG  1 
ATOM   1642 O OD1 . ASP A 1 221 ? -110.688 -32.750 47.646 1.00 51.81 ? 221  ASP A OD1 1 
ATOM   1643 O OD2 . ASP A 1 221 ? -112.536 -31.606 47.968 1.00 52.47 ? 221  ASP A OD2 1 
ATOM   1644 N N   . MET A 1 222 ? -114.464 -32.692 46.288 1.00 53.29 ? 222  MET A N   1 
ATOM   1645 C CA  . MET A 1 222 ? -115.294 -33.881 46.435 1.00 55.80 ? 222  MET A CA  1 
ATOM   1646 C C   . MET A 1 222 ? -116.464 -33.651 47.380 1.00 55.09 ? 222  MET A C   1 
ATOM   1647 O O   . MET A 1 222 ? -116.468 -32.711 48.173 1.00 54.95 ? 222  MET A O   1 
ATOM   1648 C CB  . MET A 1 222 ? -114.469 -35.050 46.963 1.00 58.00 ? 222  MET A CB  1 
ATOM   1649 C CG  . MET A 1 222 ? -114.018 -34.877 48.409 1.00 59.23 ? 222  MET A CG  1 
ATOM   1650 S SD  . MET A 1 222 ? -113.282 -36.391 49.057 1.00 64.27 ? 222  MET A SD  1 
ATOM   1651 C CE  . MET A 1 222 ? -111.607 -36.243 48.434 1.00 60.05 ? 222  MET A CE  1 
ATOM   1652 N N   . ALA A 1 223 ? -117.446 -34.540 47.291 1.00 55.35 ? 223  ALA A N   1 
ATOM   1653 C CA  . ALA A 1 223 ? -118.634 -34.484 48.130 1.00 55.78 ? 223  ALA A CA  1 
ATOM   1654 C C   . ALA A 1 223 ? -119.177 -35.894 48.314 1.00 56.65 ? 223  ALA A C   1 
ATOM   1655 O O   . ALA A 1 223 ? -119.487 -36.578 47.341 1.00 57.47 ? 223  ALA A O   1 
ATOM   1656 C CB  . ALA A 1 223 ? -119.679 -33.605 47.492 1.00 53.30 ? 223  ALA A CB  1 
ATOM   1657 N N   . ASP A 1 224 ? -119.286 -36.323 49.566 1.00 57.36 ? 224  ASP A N   1 
ATOM   1658 C CA  . ASP A 1 224 ? -119.780 -37.654 49.878 1.00 58.08 ? 224  ASP A CA  1 
ATOM   1659 C C   . ASP A 1 224 ? -121.272 -37.649 50.205 1.00 58.46 ? 224  ASP A C   1 
ATOM   1660 O O   . ASP A 1 224 ? -122.101 -37.908 49.333 1.00 60.20 ? 224  ASP A O   1 
ATOM   1661 C CB  . ASP A 1 224 ? -118.991 -38.238 51.049 1.00 58.17 ? 224  ASP A CB  1 
ATOM   1662 C CG  . ASP A 1 224 ? -119.350 -39.675 51.325 1.00 59.66 ? 224  ASP A CG  1 
ATOM   1663 O OD1 . ASP A 1 224 ? -119.433 -40.445 50.350 1.00 63.14 ? 224  ASP A OD1 1 
ATOM   1664 O OD2 . ASP A 1 224 ? -119.539 -40.042 52.505 1.00 61.44 ? 224  ASP A OD2 1 
ATOM   1665 N N   . THR A 1 225 ? -121.609 -37.356 51.458 1.00 58.00 ? 225  THR A N   1 
ATOM   1666 C CA  . THR A 1 225 ? -123.002 -37.331 51.896 1.00 57.31 ? 225  THR A CA  1 
ATOM   1667 C C   . THR A 1 225 ? -123.727 -36.055 51.464 1.00 57.17 ? 225  THR A C   1 
ATOM   1668 O O   . THR A 1 225 ? -124.952 -35.959 51.559 1.00 57.12 ? 225  THR A O   1 
ATOM   1669 C CB  . THR A 1 225 ? -123.096 -37.478 53.424 1.00 57.44 ? 225  THR A CB  1 
ATOM   1670 O OG1 . THR A 1 225 ? -122.528 -36.325 54.056 1.00 56.97 ? 225  THR A OG1 1 
ATOM   1671 C CG2 . THR A 1 225 ? -122.336 -38.714 53.875 1.00 56.71 ? 225  THR A CG2 1 
ATOM   1672 N N   . CYS A 1 226 ? -122.959 -35.078 50.994 1.00 56.51 ? 226  CYS A N   1 
ATOM   1673 C CA  . CYS A 1 226 ? -123.503 -33.812 50.517 1.00 56.27 ? 226  CYS A CA  1 
ATOM   1674 C C   . CYS A 1 226 ? -124.227 -32.984 51.568 1.00 55.75 ? 226  CYS A C   1 
ATOM   1675 O O   . CYS A 1 226 ? -124.970 -32.065 51.231 1.00 55.14 ? 226  CYS A O   1 
ATOM   1676 C CB  . CYS A 1 226 ? -124.433 -34.066 49.327 1.00 55.79 ? 226  CYS A CB  1 
ATOM   1677 S SG  . CYS A 1 226 ? -123.582 -34.769 47.901 1.00 54.04 ? 226  CYS A SG  1 
ATOM   1678 N N   . GLY A 1 227 ? -124.005 -33.302 52.838 1.00 56.28 ? 227  GLY A N   1 
ATOM   1679 C CA  . GLY A 1 227 ? -124.651 -32.550 53.898 1.00 56.03 ? 227  GLY A CA  1 
ATOM   1680 C C   . GLY A 1 227 ? -124.085 -31.146 53.986 1.00 55.74 ? 227  GLY A C   1 
ATOM   1681 O O   . GLY A 1 227 ? -124.804 -30.176 54.239 1.00 56.62 ? 227  GLY A O   1 
ATOM   1682 N N   . THR A 1 228 ? -122.782 -31.043 53.764 1.00 55.44 ? 228  THR A N   1 
ATOM   1683 C CA  . THR A 1 228 ? -122.085 -29.768 53.814 1.00 54.76 ? 228  THR A CA  1 
ATOM   1684 C C   . THR A 1 228 ? -122.448 -28.876 52.636 1.00 54.67 ? 228  THR A C   1 
ATOM   1685 O O   . THR A 1 228 ? -122.775 -27.704 52.813 1.00 54.09 ? 228  THR A O   1 
ATOM   1686 C CB  . THR A 1 228 ? -120.558 -29.990 53.823 1.00 55.21 ? 228  THR A CB  1 
ATOM   1687 O OG1 . THR A 1 228 ? -120.165 -30.507 55.101 1.00 55.21 ? 228  THR A OG1 1 
ATOM   1688 C CG2 . THR A 1 228 ? -119.814 -28.690 53.540 1.00 54.75 ? 228  THR A CG2 1 
ATOM   1689 N N   . ILE A 1 229 ? -122.395 -29.439 51.434 1.00 54.26 ? 229  ILE A N   1 
ATOM   1690 C CA  . ILE A 1 229 ? -122.695 -28.684 50.228 1.00 54.01 ? 229  ILE A CA  1 
ATOM   1691 C C   . ILE A 1 229 ? -124.172 -28.311 50.124 1.00 54.91 ? 229  ILE A C   1 
ATOM   1692 O O   . ILE A 1 229 ? -124.513 -27.273 49.558 1.00 53.60 ? 229  ILE A O   1 
ATOM   1693 C CB  . ILE A 1 229 ? -122.265 -29.469 48.973 1.00 54.29 ? 229  ILE A CB  1 
ATOM   1694 C CG1 . ILE A 1 229 ? -122.037 -28.500 47.818 1.00 54.78 ? 229  ILE A CG1 1 
ATOM   1695 C CG2 . ILE A 1 229 ? -123.324 -30.499 48.602 1.00 53.21 ? 229  ILE A CG2 1 
ATOM   1696 C CD1 . ILE A 1 229 ? -121.370 -29.137 46.620 1.00 57.23 ? 229  ILE A CD1 1 
ATOM   1697 N N   . CYS A 1 230 ? -125.043 -29.155 50.671 1.00 55.52 ? 230  CYS A N   1 
ATOM   1698 C CA  . CYS A 1 230 ? -126.471 -28.881 50.639 1.00 56.29 ? 230  CYS A CA  1 
ATOM   1699 C C   . CYS A 1 230 ? -126.816 -27.747 51.592 1.00 57.07 ? 230  CYS A C   1 
ATOM   1700 O O   . CYS A 1 230 ? -127.537 -26.816 51.224 1.00 56.27 ? 230  CYS A O   1 
ATOM   1701 C CB  . CYS A 1 230 ? -127.269 -30.135 50.993 1.00 57.20 ? 230  CYS A CB  1 
ATOM   1702 S SG  . CYS A 1 230 ? -127.515 -31.250 49.587 1.00 59.03 ? 230  CYS A SG  1 
ATOM   1703 N N   . HIS A 1 231 ? -126.304 -27.818 52.816 1.00 57.53 ? 231  HIS A N   1 
ATOM   1704 C CA  . HIS A 1 231 ? -126.565 -26.753 53.773 1.00 59.33 ? 231  HIS A CA  1 
ATOM   1705 C C   . HIS A 1 231 ? -126.004 -25.432 53.251 1.00 59.26 ? 231  HIS A C   1 
ATOM   1706 O O   . HIS A 1 231 ? -126.604 -24.373 53.449 1.00 58.88 ? 231  HIS A O   1 
ATOM   1707 C CB  . HIS A 1 231 ? -125.940 -27.072 55.129 1.00 61.96 ? 231  HIS A CB  1 
ATOM   1708 C CG  . HIS A 1 231 ? -126.823 -27.889 56.017 1.00 65.27 ? 231  HIS A CG  1 
ATOM   1709 N ND1 . HIS A 1 231 ? -128.152 -27.594 56.213 1.00 67.24 ? 231  HIS A ND1 1 
ATOM   1710 C CD2 . HIS A 1 231 ? -126.554 -28.969 56.789 1.00 66.56 ? 231  HIS A CD2 1 
ATOM   1711 C CE1 . HIS A 1 231 ? -128.670 -28.457 57.073 1.00 67.80 ? 231  HIS A CE1 1 
ATOM   1712 N NE2 . HIS A 1 231 ? -127.721 -29.299 57.436 1.00 67.52 ? 231  HIS A NE2 1 
ATOM   1713 N N   . ALA A 1 232 ? -124.856 -25.500 52.582 1.00 57.37 ? 232  ALA A N   1 
ATOM   1714 C CA  . ALA A 1 232 ? -124.226 -24.307 52.030 1.00 56.33 ? 232  ALA A CA  1 
ATOM   1715 C C   . ALA A 1 232 ? -125.149 -23.661 51.010 1.00 56.10 ? 232  ALA A C   1 
ATOM   1716 O O   . ALA A 1 232 ? -125.223 -22.435 50.909 1.00 56.41 ? 232  ALA A O   1 
ATOM   1717 C CB  . ALA A 1 232 ? -122.897 -24.669 51.376 1.00 55.73 ? 232  ALA A CB  1 
ATOM   1718 N N   . ALA A 1 233 ? -125.855 -24.494 50.253 1.00 55.37 ? 233  ALA A N   1 
ATOM   1719 C CA  . ALA A 1 233 ? -126.773 -24.000 49.236 1.00 55.21 ? 233  ALA A CA  1 
ATOM   1720 C C   . ALA A 1 233 ? -127.909 -23.193 49.864 1.00 55.44 ? 233  ALA A C   1 
ATOM   1721 O O   . ALA A 1 233 ? -128.271 -22.126 49.363 1.00 54.58 ? 233  ALA A O   1 
ATOM   1722 C CB  . ALA A 1 233 ? -127.334 -25.163 48.430 1.00 55.57 ? 233  ALA A CB  1 
ATOM   1723 N N   . ASP A 1 234 ? -128.471 -23.702 50.957 1.00 55.76 ? 234  ASP A N   1 
ATOM   1724 C CA  . ASP A 1 234 ? -129.555 -23.000 51.637 1.00 56.24 ? 234  ASP A CA  1 
ATOM   1725 C C   . ASP A 1 234 ? -129.050 -21.621 52.024 1.00 55.79 ? 234  ASP A C   1 
ATOM   1726 O O   . ASP A 1 234 ? -129.665 -20.602 51.701 1.00 56.00 ? 234  ASP A O   1 
ATOM   1727 C CB  . ASP A 1 234 ? -129.991 -23.749 52.900 1.00 57.23 ? 234  ASP A CB  1 
ATOM   1728 C CG  . ASP A 1 234 ? -130.552 -25.125 52.602 1.00 58.57 ? 234  ASP A CG  1 
ATOM   1729 O OD1 . ASP A 1 234 ? -131.373 -25.246 51.669 1.00 58.51 ? 234  ASP A OD1 1 
ATOM   1730 O OD2 . ASP A 1 234 ? -130.183 -26.085 53.313 1.00 60.39 ? 234  ASP A OD2 1 
ATOM   1731 N N   . LYS A 1 235 ? -127.917 -21.606 52.716 1.00 55.04 ? 235  LYS A N   1 
ATOM   1732 C CA  . LYS A 1 235 ? -127.297 -20.364 53.157 1.00 55.56 ? 235  LYS A CA  1 
ATOM   1733 C C   . LYS A 1 235 ? -127.212 -19.421 51.968 1.00 55.01 ? 235  LYS A C   1 
ATOM   1734 O O   . LYS A 1 235 ? -127.650 -18.275 52.041 1.00 55.28 ? 235  LYS A O   1 
ATOM   1735 C CB  . LYS A 1 235 ? -125.895 -20.647 53.706 1.00 57.07 ? 235  LYS A CB  1 
ATOM   1736 C CG  . LYS A 1 235 ? -125.651 -20.152 55.129 1.00 58.61 ? 235  LYS A CG  1 
ATOM   1737 C CD  . LYS A 1 235 ? -125.438 -18.646 55.191 1.00 58.37 ? 235  LYS A CD  1 
ATOM   1738 C CE  . LYS A 1 235 ? -125.199 -18.185 56.624 1.00 59.17 ? 235  LYS A CE  1 
ATOM   1739 N NZ  . LYS A 1 235 ? -124.828 -16.744 56.697 1.00 60.00 ? 235  LYS A NZ  1 
ATOM   1740 N N   . LEU A 1 236 ? -126.660 -19.921 50.868 1.00 54.96 ? 236  LEU A N   1 
ATOM   1741 C CA  . LEU A 1 236 ? -126.519 -19.124 49.660 1.00 55.23 ? 236  LEU A CA  1 
ATOM   1742 C C   . LEU A 1 236 ? -127.854 -18.534 49.210 1.00 55.46 ? 236  LEU A C   1 
ATOM   1743 O O   . LEU A 1 236 ? -127.913 -17.386 48.771 1.00 55.45 ? 236  LEU A O   1 
ATOM   1744 C CB  . LEU A 1 236 ? -125.897 -19.969 48.546 1.00 54.24 ? 236  LEU A CB  1 
ATOM   1745 C CG  . LEU A 1 236 ? -124.421 -20.306 48.781 1.00 53.93 ? 236  LEU A CG  1 
ATOM   1746 C CD1 . LEU A 1 236 ? -123.895 -21.222 47.687 1.00 51.77 ? 236  LEU A CD1 1 
ATOM   1747 C CD2 . LEU A 1 236 ? -123.627 -19.008 48.826 1.00 52.88 ? 236  LEU A CD2 1 
ATOM   1748 N N   . LEU A 1 237 ? -128.926 -19.310 49.319 1.00 55.95 ? 237  LEU A N   1 
ATOM   1749 C CA  . LEU A 1 237 ? -130.236 -18.805 48.935 1.00 55.87 ? 237  LEU A CA  1 
ATOM   1750 C C   . LEU A 1 237 ? -130.658 -17.711 49.905 1.00 56.17 ? 237  LEU A C   1 
ATOM   1751 O O   . LEU A 1 237 ? -131.039 -16.615 49.496 1.00 56.53 ? 237  LEU A O   1 
ATOM   1752 C CB  . LEU A 1 237 ? -131.274 -19.923 48.937 1.00 53.70 ? 237  LEU A CB  1 
ATOM   1753 C CG  . LEU A 1 237 ? -131.322 -20.771 47.669 1.00 54.56 ? 237  LEU A CG  1 
ATOM   1754 C CD1 . LEU A 1 237 ? -132.556 -21.650 47.724 1.00 56.11 ? 237  LEU A CD1 1 
ATOM   1755 C CD2 . LEU A 1 237 ? -131.383 -19.877 46.434 1.00 52.58 ? 237  LEU A CD2 1 
ATOM   1756 N N   . SER A 1 238 ? -130.578 -18.012 51.195 1.00 56.25 ? 238  SER A N   1 
ATOM   1757 C CA  . SER A 1 238 ? -130.938 -17.044 52.216 1.00 56.83 ? 238  SER A CA  1 
ATOM   1758 C C   . SER A 1 238 ? -130.133 -15.757 52.036 1.00 57.57 ? 238  SER A C   1 
ATOM   1759 O O   . SER A 1 238 ? -130.612 -14.666 52.344 1.00 57.85 ? 238  SER A O   1 
ATOM   1760 C CB  . SER A 1 238 ? -130.678 -17.633 53.601 1.00 57.19 ? 238  SER A CB  1 
ATOM   1761 O OG  . SER A 1 238 ? -131.393 -18.846 53.772 1.00 59.37 ? 238  SER A OG  1 
ATOM   1762 N N   . ALA A 1 239 ? -128.912 -15.888 51.528 1.00 57.83 ? 239  ALA A N   1 
ATOM   1763 C CA  . ALA A 1 239 ? -128.050 -14.733 51.310 1.00 58.70 ? 239  ALA A CA  1 
ATOM   1764 C C   . ALA A 1 239 ? -128.452 -13.977 50.054 1.00 59.68 ? 239  ALA A C   1 
ATOM   1765 O O   . ALA A 1 239 ? -127.826 -12.984 49.689 1.00 60.11 ? 239  ALA A O   1 
ATOM   1766 C CB  . ALA A 1 239 ? -126.595 -15.174 51.207 1.00 58.02 ? 239  ALA A CB  1 
ATOM   1767 N N   . GLY A 1 240 ? -129.492 -14.457 49.383 1.00 61.12 ? 240  GLY A N   1 
ATOM   1768 C CA  . GLY A 1 240 ? -129.951 -13.790 48.179 1.00 61.98 ? 240  GLY A CA  1 
ATOM   1769 C C   . GLY A 1 240 ? -129.292 -14.250 46.894 1.00 62.95 ? 240  GLY A C   1 
ATOM   1770 O O   . GLY A 1 240 ? -129.142 -13.466 45.956 1.00 63.48 ? 240  GLY A O   1 
ATOM   1771 N N   . ALA A 1 241 ? -128.888 -15.513 46.842 1.00 63.58 ? 241  ALA A N   1 
ATOM   1772 C CA  . ALA A 1 241 ? -128.264 -16.040 45.634 1.00 63.73 ? 241  ALA A CA  1 
ATOM   1773 C C   . ALA A 1 241 ? -129.362 -16.290 44.614 1.00 63.50 ? 241  ALA A C   1 
ATOM   1774 O O   . ALA A 1 241 ? -130.428 -16.793 44.962 1.00 63.08 ? 241  ALA A O   1 
ATOM   1775 C CB  . ALA A 1 241 ? -127.528 -17.339 45.939 1.00 63.74 ? 241  ALA A CB  1 
ATOM   1776 N N   . THR A 1 242 ? -129.110 -15.926 43.362 1.00 64.23 ? 242  THR A N   1 
ATOM   1777 C CA  . THR A 1 242 ? -130.090 -16.130 42.299 1.00 64.95 ? 242  THR A CA  1 
ATOM   1778 C C   . THR A 1 242 ? -130.427 -17.613 42.231 1.00 65.24 ? 242  THR A C   1 
ATOM   1779 O O   . THR A 1 242 ? -131.548 -18.031 42.520 1.00 65.35 ? 242  THR A O   1 
ATOM   1780 C CB  . THR A 1 242 ? -129.524 -15.694 40.938 1.00 65.73 ? 242  THR A CB  1 
ATOM   1781 O OG1 . THR A 1 242 ? -129.300 -14.279 40.947 1.00 68.45 ? 242  THR A OG1 1 
ATOM   1782 C CG2 . THR A 1 242 ? -130.485 -16.047 39.819 1.00 66.12 ? 242  THR A CG2 1 
ATOM   1783 N N   . ARG A 1 243 ? -129.429 -18.395 41.840 1.00 65.26 ? 243  ARG A N   1 
ATOM   1784 C CA  . ARG A 1 243 ? -129.546 -19.839 41.728 1.00 64.18 ? 243  ARG A CA  1 
ATOM   1785 C C   . ARG A 1 243 ? -128.222 -20.392 42.249 1.00 62.77 ? 243  ARG A C   1 
ATOM   1786 O O   . ARG A 1 243 ? -127.194 -19.717 42.188 1.00 61.68 ? 243  ARG A O   1 
ATOM   1787 C CB  . ARG A 1 243 ? -129.727 -20.248 40.266 1.00 64.95 ? 243  ARG A CB  1 
ATOM   1788 C CG  . ARG A 1 243 ? -130.866 -19.555 39.552 1.00 68.32 ? 243  ARG A CG  1 
ATOM   1789 C CD  . ARG A 1 243 ? -130.925 -19.975 38.091 1.00 69.57 ? 243  ARG A CD  1 
ATOM   1790 N NE  . ARG A 1 243 ? -129.673 -19.697 37.393 1.00 71.00 ? 243  ARG A NE  1 
ATOM   1791 C CZ  . ARG A 1 243 ? -129.475 -19.916 36.097 1.00 71.76 ? 243  ARG A CZ  1 
ATOM   1792 N NH1 . ARG A 1 243 ? -130.452 -20.419 35.353 1.00 73.36 ? 243  ARG A NH1 1 
ATOM   1793 N NH2 . ARG A 1 243 ? -128.305 -19.627 35.542 1.00 70.91 ? 243  ARG A NH2 1 
ATOM   1794 N N   . VAL A 1 244 ? -128.241 -21.613 42.760 1.00 60.88 ? 244  VAL A N   1 
ATOM   1795 C CA  . VAL A 1 244 ? -127.019 -22.203 43.271 1.00 60.16 ? 244  VAL A CA  1 
ATOM   1796 C C   . VAL A 1 244 ? -126.678 -23.508 42.564 1.00 59.28 ? 244  VAL A C   1 
ATOM   1797 O O   . VAL A 1 244 ? -127.499 -24.426 42.492 1.00 59.13 ? 244  VAL A O   1 
ATOM   1798 C CB  . VAL A 1 244 ? -127.112 -22.454 44.800 1.00 59.89 ? 244  VAL A CB  1 
ATOM   1799 C CG1 . VAL A 1 244 ? -128.339 -23.282 45.122 1.00 60.15 ? 244  VAL A CG1 1 
ATOM   1800 C CG2 . VAL A 1 244 ? -125.858 -23.161 45.289 1.00 59.16 ? 244  VAL A CG2 1 
ATOM   1801 N N   . TYR A 1 245 ? -125.467 -23.569 42.022 1.00 56.13 ? 245  TYR A N   1 
ATOM   1802 C CA  . TYR A 1 245 ? -124.988 -24.767 41.351 1.00 55.20 ? 245  TYR A CA  1 
ATOM   1803 C C   . TYR A 1 245 ? -123.940 -25.389 42.266 1.00 53.62 ? 245  TYR A C   1 
ATOM   1804 O O   . TYR A 1 245 ? -123.482 -24.754 43.219 1.00 52.47 ? 245  TYR A O   1 
ATOM   1805 C CB  . TYR A 1 245 ? -124.335 -24.427 40.005 1.00 56.15 ? 245  TYR A CB  1 
ATOM   1806 C CG  . TYR A 1 245 ? -125.276 -23.896 38.945 1.00 57.95 ? 245  TYR A CG  1 
ATOM   1807 C CD1 . TYR A 1 245 ? -125.986 -22.711 39.142 1.00 58.55 ? 245  TYR A CD1 1 
ATOM   1808 C CD2 . TYR A 1 245 ? -125.431 -24.563 37.727 1.00 57.94 ? 245  TYR A CD2 1 
ATOM   1809 C CE1 . TYR A 1 245 ? -126.825 -22.199 38.155 1.00 59.22 ? 245  TYR A CE1 1 
ATOM   1810 C CE2 . TYR A 1 245 ? -126.267 -24.060 36.732 1.00 58.04 ? 245  TYR A CE2 1 
ATOM   1811 C CZ  . TYR A 1 245 ? -126.960 -22.877 36.954 1.00 58.83 ? 245  TYR A CZ  1 
ATOM   1812 O OH  . TYR A 1 245 ? -127.788 -22.366 35.983 1.00 58.73 ? 245  TYR A OH  1 
ATOM   1813 N N   . ALA A 1 246 ? -123.564 -26.629 41.978 1.00 51.16 ? 246  ALA A N   1 
ATOM   1814 C CA  . ALA A 1 246 ? -122.554 -27.326 42.764 1.00 49.16 ? 246  ALA A CA  1 
ATOM   1815 C C   . ALA A 1 246 ? -121.661 -28.134 41.829 1.00 48.13 ? 246  ALA A C   1 
ATOM   1816 O O   . ALA A 1 246 ? -122.146 -28.988 41.082 1.00 47.29 ? 246  ALA A O   1 
ATOM   1817 C CB  . ALA A 1 246 ? -123.219 -28.241 43.781 1.00 48.74 ? 246  ALA A CB  1 
ATOM   1818 N N   . ILE A 1 247 ? -120.360 -27.852 41.864 1.00 46.14 ? 247  ILE A N   1 
ATOM   1819 C CA  . ILE A 1 247 ? -119.399 -28.557 41.023 1.00 46.32 ? 247  ILE A CA  1 
ATOM   1820 C C   . ILE A 1 247 ? -118.366 -29.318 41.855 1.00 46.48 ? 247  ILE A C   1 
ATOM   1821 O O   . ILE A 1 247 ? -117.586 -28.723 42.601 1.00 45.08 ? 247  ILE A O   1 
ATOM   1822 C CB  . ILE A 1 247 ? -118.670 -27.587 40.072 1.00 45.02 ? 247  ILE A CB  1 
ATOM   1823 C CG1 . ILE A 1 247 ? -119.695 -26.900 39.164 1.00 44.83 ? 247  ILE A CG1 1 
ATOM   1824 C CG2 . ILE A 1 247 ? -117.641 -28.347 39.244 1.00 44.48 ? 247  ILE A CG2 1 
ATOM   1825 C CD1 . ILE A 1 247 ? -119.102 -26.024 38.091 1.00 43.91 ? 247  ILE A CD1 1 
ATOM   1826 N N   . LEU A 1 248 ? -118.375 -30.639 41.713 1.00 47.43 ? 248  LEU A N   1 
ATOM   1827 C CA  . LEU A 1 248 ? -117.465 -31.514 42.443 1.00 48.41 ? 248  LEU A CA  1 
ATOM   1828 C C   . LEU A 1 248 ? -116.671 -32.329 41.439 1.00 49.87 ? 248  LEU A C   1 
ATOM   1829 O O   . LEU A 1 248 ? -117.239 -32.852 40.482 1.00 50.79 ? 248  LEU A O   1 
ATOM   1830 C CB  . LEU A 1 248 ? -118.262 -32.471 43.320 1.00 47.85 ? 248  LEU A CB  1 
ATOM   1831 C CG  . LEU A 1 248 ? -119.484 -31.877 44.019 1.00 49.62 ? 248  LEU A CG  1 
ATOM   1832 C CD1 . LEU A 1 248 ? -120.408 -33.005 44.425 1.00 49.90 ? 248  LEU A CD1 1 
ATOM   1833 C CD2 . LEU A 1 248 ? -119.064 -31.044 45.217 1.00 49.26 ? 248  LEU A CD2 1 
ATOM   1834 N N   . THR A 1 249 ? -115.364 -32.456 41.637 1.00 49.41 ? 249  THR A N   1 
ATOM   1835 C CA  . THR A 1 249 ? -114.602 -33.250 40.690 1.00 48.81 ? 249  THR A CA  1 
ATOM   1836 C C   . THR A 1 249 ? -114.798 -34.727 41.039 1.00 48.66 ? 249  THR A C   1 
ATOM   1837 O O   . THR A 1 249 ? -114.937 -35.573 40.154 1.00 48.36 ? 249  THR A O   1 
ATOM   1838 C CB  . THR A 1 249 ? -113.108 -32.868 40.684 1.00 49.54 ? 249  THR A CB  1 
ATOM   1839 O OG1 . THR A 1 249 ? -112.325 -33.986 41.106 1.00 52.63 ? 249  THR A OG1 1 
ATOM   1840 C CG2 . THR A 1 249 ? -112.857 -31.674 41.585 1.00 51.39 ? 249  THR A CG2 1 
ATOM   1841 N N   . HIS A 1 250 ? -114.845 -35.035 42.329 1.00 47.00 ? 250  HIS A N   1 
ATOM   1842 C CA  . HIS A 1 250 ? -115.057 -36.411 42.763 1.00 46.56 ? 250  HIS A CA  1 
ATOM   1843 C C   . HIS A 1 250 ? -116.420 -36.507 43.428 1.00 48.27 ? 250  HIS A C   1 
ATOM   1844 O O   . HIS A 1 250 ? -116.640 -35.931 44.497 1.00 47.87 ? 250  HIS A O   1 
ATOM   1845 C CB  . HIS A 1 250 ? -113.977 -36.834 43.761 1.00 43.24 ? 250  HIS A CB  1 
ATOM   1846 C CG  . HIS A 1 250 ? -112.583 -36.598 43.276 1.00 38.64 ? 250  HIS A CG  1 
ATOM   1847 N ND1 . HIS A 1 250 ? -112.056 -37.248 42.184 1.00 39.53 ? 250  HIS A ND1 1 
ATOM   1848 C CD2 . HIS A 1 250 ? -111.615 -35.769 43.731 1.00 36.03 ? 250  HIS A CD2 1 
ATOM   1849 C CE1 . HIS A 1 250 ? -110.814 -36.831 41.984 1.00 35.40 ? 250  HIS A CE1 1 
ATOM   1850 N NE2 . HIS A 1 250 ? -110.524 -35.936 42.908 1.00 37.17 ? 250  HIS A NE2 1 
ATOM   1851 N N   . GLY A 1 251 ? -117.335 -37.229 42.794 1.00 50.70 ? 251  GLY A N   1 
ATOM   1852 C CA  . GLY A 1 251 ? -118.671 -37.372 43.345 1.00 54.00 ? 251  GLY A CA  1 
ATOM   1853 C C   . GLY A 1 251 ? -118.901 -38.705 44.023 1.00 56.90 ? 251  GLY A C   1 
ATOM   1854 O O   . GLY A 1 251 ? -119.396 -39.649 43.407 1.00 56.15 ? 251  GLY A O   1 
ATOM   1855 N N   . ILE A 1 252 ? -118.536 -38.780 45.298 1.00 59.76 ? 252  ILE A N   1 
ATOM   1856 C CA  . ILE A 1 252 ? -118.679 -40.004 46.091 1.00 63.64 ? 252  ILE A CA  1 
ATOM   1857 C C   . ILE A 1 252 ? -120.055 -40.019 46.750 1.00 65.23 ? 252  ILE A C   1 
ATOM   1858 O O   . ILE A 1 252 ? -120.183 -40.307 47.940 1.00 67.37 ? 252  ILE A O   1 
ATOM   1859 C CB  . ILE A 1 252 ? -117.616 -40.053 47.205 1.00 63.27 ? 252  ILE A CB  1 
ATOM   1860 C CG1 . ILE A 1 252 ? -116.266 -39.603 46.640 1.00 63.70 ? 252  ILE A CG1 1 
ATOM   1861 C CG2 . ILE A 1 252 ? -117.516 -41.455 47.776 1.00 63.45 ? 252  ILE A CG2 1 
ATOM   1862 C CD1 . ILE A 1 252 ? -115.358 -39.017 47.684 1.00 64.03 ? 252  ILE A CD1 1 
ATOM   1863 N N   . PHE A 1 253 ? -121.074 -39.696 45.968 1.00 66.63 ? 253  PHE A N   1 
ATOM   1864 C CA  . PHE A 1 253 ? -122.447 -39.625 46.436 1.00 67.57 ? 253  PHE A CA  1 
ATOM   1865 C C   . PHE A 1 253 ? -122.965 -40.850 47.175 1.00 68.20 ? 253  PHE A C   1 
ATOM   1866 O O   . PHE A 1 253 ? -123.639 -41.688 46.587 1.00 68.64 ? 253  PHE A O   1 
ATOM   1867 C CB  . PHE A 1 253 ? -123.339 -39.335 45.239 1.00 65.76 ? 253  PHE A CB  1 
ATOM   1868 C CG  . PHE A 1 253 ? -123.004 -38.069 44.539 1.00 64.25 ? 253  PHE A CG  1 
ATOM   1869 C CD1 . PHE A 1 253 ? -123.077 -37.973 43.153 1.00 64.37 ? 253  PHE A CD1 1 
ATOM   1870 C CD2 . PHE A 1 253 ? -122.647 -36.950 45.273 1.00 63.93 ? 253  PHE A CD2 1 
ATOM   1871 C CE1 . PHE A 1 253 ? -122.801 -36.776 42.523 1.00 64.34 ? 253  PHE A CE1 1 
ATOM   1872 C CE2 . PHE A 1 253 ? -122.371 -35.752 44.651 1.00 64.33 ? 253  PHE A CE2 1 
ATOM   1873 C CZ  . PHE A 1 253 ? -122.448 -35.663 43.275 1.00 64.12 ? 253  PHE A CZ  1 
ATOM   1874 N N   . SER A 1 254 ? -122.688 -40.929 48.470 1.00 69.54 ? 254  SER A N   1 
ATOM   1875 C CA  . SER A 1 254 ? -123.116 -42.066 49.282 1.00 71.72 ? 254  SER A CA  1 
ATOM   1876 C C   . SER A 1 254 ? -124.204 -41.669 50.276 1.00 72.84 ? 254  SER A C   1 
ATOM   1877 O O   . SER A 1 254 ? -124.446 -40.486 50.490 1.00 72.92 ? 254  SER A O   1 
ATOM   1878 C CB  . SER A 1 254 ? -121.915 -42.608 50.040 1.00 72.36 ? 254  SER A CB  1 
ATOM   1879 O OG  . SER A 1 254 ? -121.435 -41.639 50.958 1.00 72.63 ? 254  SER A OG  1 
ATOM   1880 N N   . GLY A 1 255 ? -124.852 -42.663 50.881 1.00 74.22 ? 255  GLY A N   1 
ATOM   1881 C CA  . GLY A 1 255 ? -125.886 -42.410 51.871 1.00 75.75 ? 255  GLY A CA  1 
ATOM   1882 C C   . GLY A 1 255 ? -127.028 -41.516 51.431 1.00 77.21 ? 255  GLY A C   1 
ATOM   1883 O O   . GLY A 1 255 ? -127.730 -41.839 50.473 1.00 77.25 ? 255  GLY A O   1 
ATOM   1884 N N   . PRO A 1 256 ? -127.249 -40.392 52.139 1.00 78.84 ? 256  PRO A N   1 
ATOM   1885 C CA  . PRO A 1 256 ? -128.305 -39.410 51.869 1.00 79.81 ? 256  PRO A CA  1 
ATOM   1886 C C   . PRO A 1 256 ? -128.051 -38.521 50.656 1.00 81.44 ? 256  PRO A C   1 
ATOM   1887 O O   . PRO A 1 256 ? -128.946 -37.806 50.211 1.00 81.53 ? 256  PRO A O   1 
ATOM   1888 C CB  . PRO A 1 256 ? -128.352 -38.597 53.165 1.00 78.71 ? 256  PRO A CB  1 
ATOM   1889 C CG  . PRO A 1 256 ? -127.826 -39.563 54.196 1.00 78.29 ? 256  PRO A CG  1 
ATOM   1890 C CD  . PRO A 1 256 ? -126.662 -40.140 53.465 1.00 77.79 ? 256  PRO A CD  1 
ATOM   1891 N N   . ALA A 1 257 ? -126.833 -38.567 50.126 1.00 83.14 ? 257  ALA A N   1 
ATOM   1892 C CA  . ALA A 1 257 ? -126.468 -37.751 48.975 1.00 83.91 ? 257  ALA A CA  1 
ATOM   1893 C C   . ALA A 1 257 ? -127.510 -37.794 47.865 1.00 84.48 ? 257  ALA A C   1 
ATOM   1894 O O   . ALA A 1 257 ? -128.098 -36.769 47.516 1.00 86.89 ? 257  ALA A O   1 
ATOM   1895 C CB  . ALA A 1 257 ? -125.115 -38.196 48.434 1.00 83.47 ? 257  ALA A CB  1 
ATOM   1896 N N   . ILE A 1 258 ? -127.734 -38.985 47.320 1.00 84.52 ? 258  ILE A N   1 
ATOM   1897 C CA  . ILE A 1 258 ? -128.683 -39.192 46.229 1.00 85.72 ? 258  ILE A CA  1 
ATOM   1898 C C   . ILE A 1 258 ? -129.992 -38.417 46.335 1.00 86.11 ? 258  ILE A C   1 
ATOM   1899 O O   . ILE A 1 258 ? -130.541 -37.982 45.323 1.00 87.45 ? 258  ILE A O   1 
ATOM   1900 C CB  . ILE A 1 258 ? -129.070 -40.673 46.099 1.00 87.00 ? 258  ILE A CB  1 
ATOM   1901 C CG1 . ILE A 1 258 ? -127.808 -41.554 46.056 1.00 89.17 ? 258  ILE A CG1 1 
ATOM   1902 C CG2 . ILE A 1 258 ? -129.984 -40.840 44.873 1.00 87.18 ? 258  ILE A CG2 1 
ATOM   1903 C CD1 . ILE A 1 258 ? -128.084 -43.042 45.816 1.00 87.87 ? 258  ILE A CD1 1 
ATOM   1904 N N   . SER A 1 259 ? -130.505 -38.271 47.552 1.00 85.52 ? 259  SER A N   1 
ATOM   1905 C CA  . SER A 1 259 ? -131.765 -37.569 47.754 1.00 84.10 ? 259  SER A CA  1 
ATOM   1906 C C   . SER A 1 259 ? -131.557 -36.127 48.177 1.00 83.20 ? 259  SER A C   1 
ATOM   1907 O O   . SER A 1 259 ? -132.278 -35.234 47.734 1.00 83.12 ? 259  SER A O   1 
ATOM   1908 C CB  . SER A 1 259 ? -132.615 -38.294 48.804 1.00 84.09 ? 259  SER A CB  1 
ATOM   1909 O OG  . SER A 1 259 ? -131.996 -38.273 50.080 1.00 82.33 ? 259  SER A OG  1 
ATOM   1910 N N   . ARG A 1 260 ? -130.569 -35.903 49.034 1.00 81.71 ? 260  ARG A N   1 
ATOM   1911 C CA  . ARG A 1 260 ? -130.284 -34.563 49.521 1.00 79.87 ? 260  ARG A CA  1 
ATOM   1912 C C   . ARG A 1 260 ? -130.146 -33.535 48.408 1.00 79.04 ? 260  ARG A C   1 
ATOM   1913 O O   . ARG A 1 260 ? -130.591 -32.398 48.560 1.00 78.32 ? 260  ARG A O   1 
ATOM   1914 C CB  . ARG A 1 260 ? -129.014 -34.567 50.375 1.00 79.26 ? 260  ARG A CB  1 
ATOM   1915 C CG  . ARG A 1 260 ? -129.194 -35.152 51.764 1.00 76.76 ? 260  ARG A CG  1 
ATOM   1916 C CD  . ARG A 1 260 ? -127.896 -35.088 52.547 1.00 75.81 ? 260  ARG A CD  1 
ATOM   1917 N NE  . ARG A 1 260 ? -128.064 -35.487 53.940 1.00 74.92 ? 260  ARG A NE  1 
ATOM   1918 C CZ  . ARG A 1 260 ? -127.064 -35.598 54.809 1.00 74.98 ? 260  ARG A CZ  1 
ATOM   1919 N NH1 . ARG A 1 260 ? -125.819 -35.342 54.427 1.00 74.00 ? 260  ARG A NH1 1 
ATOM   1920 N NH2 . ARG A 1 260 ? -127.306 -35.960 56.062 1.00 74.75 ? 260  ARG A NH2 1 
ATOM   1921 N N   . ILE A 1 261 ? -129.539 -33.922 47.289 1.00 78.74 ? 261  ILE A N   1 
ATOM   1922 C CA  . ILE A 1 261 ? -129.367 -32.973 46.195 1.00 78.71 ? 261  ILE A CA  1 
ATOM   1923 C C   . ILE A 1 261 ? -130.694 -32.688 45.507 1.00 78.97 ? 261  ILE A C   1 
ATOM   1924 O O   . ILE A 1 261 ? -130.960 -31.554 45.116 1.00 78.94 ? 261  ILE A O   1 
ATOM   1925 C CB  . ILE A 1 261 ? -128.330 -33.464 45.142 1.00 78.83 ? 261  ILE A CB  1 
ATOM   1926 C CG1 . ILE A 1 261 ? -128.990 -34.387 44.119 1.00 78.93 ? 261  ILE A CG1 1 
ATOM   1927 C CG2 . ILE A 1 261 ? -127.181 -34.177 45.840 1.00 78.56 ? 261  ILE A CG2 1 
ATOM   1928 C CD1 . ILE A 1 261 ? -129.509 -35.670 44.691 1.00 79.96 ? 261  ILE A CD1 1 
ATOM   1929 N N   . ASN A 1 262 ? -131.531 -33.711 45.369 1.00 79.62 ? 262  ASN A N   1 
ATOM   1930 C CA  . ASN A 1 262 ? -132.830 -33.529 44.734 1.00 79.69 ? 262  ASN A CA  1 
ATOM   1931 C C   . ASN A 1 262 ? -133.623 -32.532 45.557 1.00 79.33 ? 262  ASN A C   1 
ATOM   1932 O O   . ASN A 1 262 ? -134.057 -31.500 45.049 1.00 79.91 ? 262  ASN A O   1 
ATOM   1933 C CB  . ASN A 1 262 ? -133.594 -34.853 44.662 1.00 80.01 ? 262  ASN A CB  1 
ATOM   1934 C CG  . ASN A 1 262 ? -132.924 -35.865 43.756 1.00 81.08 ? 262  ASN A CG  1 
ATOM   1935 O OD1 . ASN A 1 262 ? -132.568 -35.560 42.616 1.00 81.40 ? 262  ASN A OD1 1 
ATOM   1936 N ND2 . ASN A 1 262 ? -132.763 -37.084 44.254 1.00 81.62 ? 262  ASN A ND2 1 
ATOM   1937 N N   . ASN A 1 263 ? -133.791 -32.845 46.838 1.00 78.97 ? 263  ASN A N   1 
ATOM   1938 C CA  . ASN A 1 263 ? -134.528 -31.985 47.756 1.00 78.72 ? 263  ASN A CA  1 
ATOM   1939 C C   . ASN A 1 263 ? -133.849 -30.621 47.897 1.00 77.87 ? 263  ASN A C   1 
ATOM   1940 O O   . ASN A 1 263 ? -134.446 -29.672 48.402 1.00 78.37 ? 263  ASN A O   1 
ATOM   1941 C CB  . ASN A 1 263 ? -134.633 -32.650 49.129 1.00 79.53 ? 263  ASN A CB  1 
ATOM   1942 C CG  . ASN A 1 263 ? -135.079 -34.093 49.044 1.00 80.41 ? 263  ASN A CG  1 
ATOM   1943 O OD1 . ASN A 1 263 ? -136.096 -34.409 48.425 1.00 80.86 ? 263  ASN A OD1 1 
ATOM   1944 N ND2 . ASN A 1 263 ? -134.319 -34.980 49.675 1.00 80.77 ? 263  ASN A ND2 1 
ATOM   1945 N N   . ALA A 1 264 ? -132.598 -30.533 47.458 1.00 75.83 ? 264  ALA A N   1 
ATOM   1946 C CA  . ALA A 1 264 ? -131.850 -29.282 47.518 1.00 73.42 ? 264  ALA A CA  1 
ATOM   1947 C C   . ALA A 1 264 ? -132.309 -28.386 46.370 1.00 71.73 ? 264  ALA A C   1 
ATOM   1948 O O   . ALA A 1 264 ? -132.999 -28.841 45.461 1.00 70.78 ? 264  ALA A O   1 
ATOM   1949 C CB  . ALA A 1 264 ? -130.362 -29.561 47.404 1.00 74.21 ? 264  ALA A CB  1 
ATOM   1950 N N   . CYS A 1 265 ? -131.920 -27.119 46.402 1.00 69.26 ? 265  CYS A N   1 
ATOM   1951 C CA  . CYS A 1 265 ? -132.317 -26.187 45.358 1.00 67.05 ? 265  CYS A CA  1 
ATOM   1952 C C   . CYS A 1 265 ? -131.296 -26.059 44.228 1.00 64.40 ? 265  CYS A C   1 
ATOM   1953 O O   . CYS A 1 265 ? -131.373 -25.121 43.430 1.00 64.01 ? 265  CYS A O   1 
ATOM   1954 C CB  . CYS A 1 265 ? -132.546 -24.813 45.965 1.00 68.72 ? 265  CYS A CB  1 
ATOM   1955 S SG  . CYS A 1 265 ? -131.076 -24.203 46.784 1.00 75.57 ? 265  CYS A SG  1 
ATOM   1956 N N   . PHE A 1 266 ? -130.350 -26.990 44.147 1.00 60.49 ? 266  PHE A N   1 
ATOM   1957 C CA  . PHE A 1 266 ? -129.331 -26.939 43.101 1.00 57.31 ? 266  PHE A CA  1 
ATOM   1958 C C   . PHE A 1 266 ? -129.932 -26.827 41.708 1.00 56.75 ? 266  PHE A C   1 
ATOM   1959 O O   . PHE A 1 266 ? -130.799 -27.609 41.324 1.00 57.29 ? 266  PHE A O   1 
ATOM   1960 C CB  . PHE A 1 266 ? -128.440 -28.189 43.139 1.00 55.25 ? 266  PHE A CB  1 
ATOM   1961 C CG  . PHE A 1 266 ? -127.644 -28.332 44.392 1.00 51.68 ? 266  PHE A CG  1 
ATOM   1962 C CD1 . PHE A 1 266 ? -127.738 -29.488 45.147 1.00 50.20 ? 266  PHE A CD1 1 
ATOM   1963 C CD2 . PHE A 1 266 ? -126.804 -27.311 44.821 1.00 50.93 ? 266  PHE A CD2 1 
ATOM   1964 C CE1 . PHE A 1 266 ? -127.005 -29.629 46.317 1.00 51.27 ? 266  PHE A CE1 1 
ATOM   1965 C CE2 . PHE A 1 266 ? -126.067 -27.442 45.990 1.00 50.77 ? 266  PHE A CE2 1 
ATOM   1966 C CZ  . PHE A 1 266 ? -126.169 -28.603 46.739 1.00 49.64 ? 266  PHE A CZ  1 
ATOM   1967 N N   . GLU A 1 267 ? -129.458 -25.858 40.941 1.00 55.63 ? 267  GLU A N   1 
ATOM   1968 C CA  . GLU A 1 267 ? -129.948 -25.701 39.588 1.00 54.71 ? 267  GLU A CA  1 
ATOM   1969 C C   . GLU A 1 267 ? -129.394 -26.890 38.804 1.00 54.15 ? 267  GLU A C   1 
ATOM   1970 O O   . GLU A 1 267 ? -129.871 -27.227 37.722 1.00 54.72 ? 267  GLU A O   1 
ATOM   1971 C CB  . GLU A 1 267 ? -129.440 -24.393 38.997 1.00 55.41 ? 267  GLU A CB  1 
ATOM   1972 C CG  . GLU A 1 267 ? -129.973 -24.132 37.611 1.00 58.43 ? 267  GLU A CG  1 
ATOM   1973 C CD  . GLU A 1 267 ? -131.482 -23.960 37.601 1.00 58.97 ? 267  GLU A CD  1 
ATOM   1974 O OE1 . GLU A 1 267 ? -131.985 -23.039 38.286 1.00 57.48 ? 267  GLU A OE1 1 
ATOM   1975 O OE2 . GLU A 1 267 ? -132.162 -24.743 36.904 1.00 61.17 ? 267  GLU A OE2 1 
ATOM   1976 N N   . ALA A 1 268 ? -128.368 -27.509 39.380 1.00 52.03 ? 268  ALA A N   1 
ATOM   1977 C CA  . ALA A 1 268 ? -127.682 -28.659 38.806 1.00 49.03 ? 268  ALA A CA  1 
ATOM   1978 C C   . ALA A 1 268 ? -126.449 -29.018 39.642 1.00 47.90 ? 268  ALA A C   1 
ATOM   1979 O O   . ALA A 1 268 ? -125.920 -28.185 40.387 1.00 46.01 ? 268  ALA A O   1 
ATOM   1980 C CB  . ALA A 1 268 ? -127.254 -28.355 37.388 1.00 49.47 ? 268  ALA A CB  1 
ATOM   1981 N N   . VAL A 1 269 ? -126.008 -30.265 39.515 1.00 46.04 ? 269  VAL A N   1 
ATOM   1982 C CA  . VAL A 1 269 ? -124.826 -30.751 40.223 1.00 44.70 ? 269  VAL A CA  1 
ATOM   1983 C C   . VAL A 1 269 ? -123.898 -31.418 39.211 1.00 44.76 ? 269  VAL A C   1 
ATOM   1984 O O   . VAL A 1 269 ? -124.226 -32.468 38.649 1.00 45.13 ? 269  VAL A O   1 
ATOM   1985 C CB  . VAL A 1 269 ? -125.197 -31.769 41.306 1.00 44.35 ? 269  VAL A CB  1 
ATOM   1986 C CG1 . VAL A 1 269 ? -123.938 -32.213 42.046 1.00 44.21 ? 269  VAL A CG1 1 
ATOM   1987 C CG2 . VAL A 1 269 ? -126.198 -31.151 42.279 1.00 44.35 ? 269  VAL A CG2 1 
ATOM   1988 N N   . VAL A 1 270 ? -122.738 -30.809 38.984 1.00 42.70 ? 270  VAL A N   1 
ATOM   1989 C CA  . VAL A 1 270 ? -121.774 -31.332 38.018 1.00 41.70 ? 270  VAL A CA  1 
ATOM   1990 C C   . VAL A 1 270 ? -120.592 -32.076 38.653 1.00 41.93 ? 270  VAL A C   1 
ATOM   1991 O O   . VAL A 1 270 ? -119.932 -31.564 39.559 1.00 42.96 ? 270  VAL A O   1 
ATOM   1992 C CB  . VAL A 1 270 ? -121.212 -30.192 37.146 1.00 40.21 ? 270  VAL A CB  1 
ATOM   1993 C CG1 . VAL A 1 270 ? -120.446 -30.762 35.972 1.00 40.10 ? 270  VAL A CG1 1 
ATOM   1994 C CG2 . VAL A 1 270 ? -122.344 -29.292 36.674 1.00 39.52 ? 270  VAL A CG2 1 
ATOM   1995 N N   . VAL A 1 271 ? -120.324 -33.281 38.161 1.00 41.17 ? 271  VAL A N   1 
ATOM   1996 C CA  . VAL A 1 271 ? -119.224 -34.095 38.658 1.00 40.02 ? 271  VAL A CA  1 
ATOM   1997 C C   . VAL A 1 271 ? -118.494 -34.744 37.498 1.00 41.69 ? 271  VAL A C   1 
ATOM   1998 O O   . VAL A 1 271 ? -119.020 -34.827 36.386 1.00 41.47 ? 271  VAL A O   1 
ATOM   1999 C CB  . VAL A 1 271 ? -119.715 -35.203 39.606 1.00 40.73 ? 271  VAL A CB  1 
ATOM   2000 C CG1 . VAL A 1 271 ? -120.309 -34.584 40.863 1.00 41.26 ? 271  VAL A CG1 1 
ATOM   2001 C CG2 . VAL A 1 271 ? -120.742 -36.077 38.904 1.00 39.01 ? 271  VAL A CG2 1 
ATOM   2002 N N   . THR A 1 272 ? -117.275 -35.199 37.755 1.00 41.22 ? 272  THR A N   1 
ATOM   2003 C CA  . THR A 1 272 ? -116.491 -35.841 36.718 1.00 42.30 ? 272  THR A CA  1 
ATOM   2004 C C   . THR A 1 272 ? -116.732 -37.338 36.716 1.00 44.27 ? 272  THR A C   1 
ATOM   2005 O O   . THR A 1 272 ? -117.418 -37.883 37.576 1.00 44.53 ? 272  THR A O   1 
ATOM   2006 C CB  . THR A 1 272 ? -114.996 -35.629 36.913 1.00 42.39 ? 272  THR A CB  1 
ATOM   2007 O OG1 . THR A 1 272 ? -114.548 -36.468 37.986 1.00 40.18 ? 272  THR A OG1 1 
ATOM   2008 C CG2 . THR A 1 272 ? -114.694 -34.160 37.232 1.00 42.42 ? 272  THR A CG2 1 
ATOM   2009 N N   . ASN A 1 273 ? -116.122 -37.986 35.739 1.00 45.00 ? 273  ASN A N   1 
ATOM   2010 C CA  . ASN A 1 273 ? -116.220 -39.415 35.526 1.00 47.37 ? 273  ASN A CA  1 
ATOM   2011 C C   . ASN A 1 273 ? -115.267 -40.216 36.425 1.00 47.68 ? 273  ASN A C   1 
ATOM   2012 O O   . ASN A 1 273 ? -115.141 -41.428 36.266 1.00 48.11 ? 273  ASN A O   1 
ATOM   2013 C CB  . ASN A 1 273 ? -115.893 -39.685 34.052 1.00 48.79 ? 273  ASN A CB  1 
ATOM   2014 C CG  . ASN A 1 273 ? -116.843 -40.659 33.424 1.00 52.20 ? 273  ASN A CG  1 
ATOM   2015 O OD1 . ASN A 1 273 ? -117.967 -40.835 33.905 1.00 57.01 ? 273  ASN A OD1 1 
ATOM   2016 N ND2 . ASN A 1 273 ? -116.416 -41.294 32.335 1.00 50.31 ? 273  ASN A ND2 1 
ATOM   2017 N N   . THR A 1 274 ? -114.596 -39.552 37.360 1.00 47.15 ? 274  THR A N   1 
ATOM   2018 C CA  . THR A 1 274 ? -113.640 -40.251 38.217 1.00 48.80 ? 274  THR A CA  1 
ATOM   2019 C C   . THR A 1 274 ? -114.258 -41.398 39.017 1.00 49.44 ? 274  THR A C   1 
ATOM   2020 O O   . THR A 1 274 ? -113.555 -42.314 39.440 1.00 49.05 ? 274  THR A O   1 
ATOM   2021 C CB  . THR A 1 274 ? -112.918 -39.280 39.189 1.00 47.59 ? 274  THR A CB  1 
ATOM   2022 O OG1 . THR A 1 274 ? -113.877 -38.626 40.024 1.00 49.44 ? 274  THR A OG1 1 
ATOM   2023 C CG2 . THR A 1 274 ? -112.143 -38.223 38.411 1.00 46.01 ? 274  THR A CG2 1 
ATOM   2024 N N   . ILE A 1 275 ? -115.568 -41.351 39.214 1.00 52.14 ? 275  ILE A N   1 
ATOM   2025 C CA  . ILE A 1 275 ? -116.275 -42.387 39.949 1.00 53.61 ? 275  ILE A CA  1 
ATOM   2026 C C   . ILE A 1 275 ? -117.574 -42.626 39.184 1.00 55.26 ? 275  ILE A C   1 
ATOM   2027 O O   . ILE A 1 275 ? -118.163 -41.676 38.661 1.00 55.85 ? 275  ILE A O   1 
ATOM   2028 C CB  . ILE A 1 275 ? -116.565 -41.920 41.405 1.00 53.55 ? 275  ILE A CB  1 
ATOM   2029 C CG1 . ILE A 1 275 ? -115.237 -41.848 42.174 1.00 52.09 ? 275  ILE A CG1 1 
ATOM   2030 C CG2 . ILE A 1 275 ? -117.519 -42.883 42.096 1.00 54.03 ? 275  ILE A CG2 1 
ATOM   2031 C CD1 . ILE A 1 275 ? -115.395 -41.326 43.591 1.00 52.21 ? 275  ILE A CD1 1 
ATOM   2032 N N   . PRO A 1 276 ? -118.005 -43.899 39.067 1.00 58.50 ? 276  PRO A N   1 
ATOM   2033 C CA  . PRO A 1 276 ? -119.225 -44.330 38.367 1.00 59.94 ? 276  PRO A CA  1 
ATOM   2034 C C   . PRO A 1 276 ? -120.457 -43.541 38.804 1.00 61.07 ? 276  PRO A C   1 
ATOM   2035 O O   . PRO A 1 276 ? -120.825 -43.562 39.979 1.00 60.94 ? 276  PRO A O   1 
ATOM   2036 C CB  . PRO A 1 276 ? -119.309 -45.805 38.724 1.00 58.57 ? 276  PRO A CB  1 
ATOM   2037 C CG  . PRO A 1 276 ? -117.858 -46.187 38.820 1.00 58.88 ? 276  PRO A CG  1 
ATOM   2038 C CD  . PRO A 1 276 ? -117.314 -45.060 39.653 1.00 58.12 ? 276  PRO A CD  1 
ATOM   2039 N N   . GLN A 1 277 ? -121.099 -42.863 37.851 1.00 63.93 ? 277  GLN A N   1 
ATOM   2040 C CA  . GLN A 1 277 ? -122.278 -42.045 38.144 1.00 66.71 ? 277  GLN A CA  1 
ATOM   2041 C C   . GLN A 1 277 ? -123.587 -42.520 37.503 1.00 69.65 ? 277  GLN A C   1 
ATOM   2042 O O   . GLN A 1 277 ? -124.661 -42.027 37.858 1.00 70.40 ? 277  GLN A O   1 
ATOM   2043 C CB  . GLN A 1 277 ? -122.020 -40.602 37.720 1.00 64.36 ? 277  GLN A CB  1 
ATOM   2044 C CG  . GLN A 1 277 ? -120.741 -40.010 38.278 1.00 63.01 ? 277  GLN A CG  1 
ATOM   2045 C CD  . GLN A 1 277 ? -120.794 -39.798 39.774 1.00 62.76 ? 277  GLN A CD  1 
ATOM   2046 O OE1 . GLN A 1 277 ? -119.784 -39.487 40.399 1.00 61.59 ? 277  GLN A OE1 1 
ATOM   2047 N NE2 . GLN A 1 277 ? -121.976 -39.955 40.355 1.00 62.56 ? 277  GLN A NE2 1 
ATOM   2048 N N   . GLU A 1 278 ? -123.503 -43.460 36.561 1.00 72.66 ? 278  GLU A N   1 
ATOM   2049 C CA  . GLU A 1 278 ? -124.690 -43.976 35.870 1.00 75.17 ? 278  GLU A CA  1 
ATOM   2050 C C   . GLU A 1 278 ? -125.812 -44.362 36.846 1.00 76.48 ? 278  GLU A C   1 
ATOM   2051 O O   . GLU A 1 278 ? -126.955 -43.928 36.693 1.00 76.23 ? 278  GLU A O   1 
ATOM   2052 C CB  . GLU A 1 278 ? -124.320 -45.195 35.013 1.00 76.57 ? 278  GLU A CB  1 
ATOM   2053 C CG  . GLU A 1 278 ? -123.334 -44.931 33.870 1.00 79.05 ? 278  GLU A CG  1 
ATOM   2054 C CD  . GLU A 1 278 ? -121.970 -44.440 34.347 1.00 81.50 ? 278  GLU A CD  1 
ATOM   2055 O OE1 . GLU A 1 278 ? -121.857 -43.258 34.744 1.00 83.24 ? 278  GLU A OE1 1 
ATOM   2056 O OE2 . GLU A 1 278 ? -121.007 -45.238 34.333 1.00 81.99 ? 278  GLU A OE2 1 
ATOM   2057 N N   . ASP A 1 279 ? -125.478 -45.185 37.837 1.00 77.87 ? 279  ASP A N   1 
ATOM   2058 C CA  . ASP A 1 279 ? -126.439 -45.636 38.841 1.00 79.36 ? 279  ASP A CA  1 
ATOM   2059 C C   . ASP A 1 279 ? -127.191 -44.469 39.475 1.00 80.20 ? 279  ASP A C   1 
ATOM   2060 O O   . ASP A 1 279 ? -128.423 -44.439 39.484 1.00 79.75 ? 279  ASP A O   1 
ATOM   2061 C CB  . ASP A 1 279 ? -125.713 -46.431 39.932 1.00 80.60 ? 279  ASP A CB  1 
ATOM   2062 C CG  . ASP A 1 279 ? -126.632 -46.850 41.068 1.00 81.01 ? 279  ASP A CG  1 
ATOM   2063 O OD1 . ASP A 1 279 ? -127.164 -45.965 41.771 1.00 81.44 ? 279  ASP A OD1 1 
ATOM   2064 O OD2 . ASP A 1 279 ? -126.819 -48.070 41.261 1.00 82.24 ? 279  ASP A OD2 1 
ATOM   2065 N N   . LYS A 1 280 ? -126.438 -43.512 40.005 1.00 80.29 ? 280  LYS A N   1 
ATOM   2066 C CA  . LYS A 1 280 ? -127.013 -42.346 40.660 1.00 80.22 ? 280  LYS A CA  1 
ATOM   2067 C C   . LYS A 1 280 ? -127.850 -41.444 39.763 1.00 80.51 ? 280  LYS A C   1 
ATOM   2068 O O   . LYS A 1 280 ? -129.004 -41.155 40.077 1.00 80.47 ? 280  LYS A O   1 
ATOM   2069 C CB  . LYS A 1 280 ? -125.906 -41.521 41.304 1.00 80.03 ? 280  LYS A CB  1 
ATOM   2070 C CG  . LYS A 1 280 ? -125.280 -42.192 42.501 1.00 79.37 ? 280  LYS A CG  1 
ATOM   2071 C CD  . LYS A 1 280 ? -124.978 -41.165 43.561 1.00 79.05 ? 280  LYS A CD  1 
ATOM   2072 C CE  . LYS A 1 280 ? -126.170 -40.221 43.761 1.00 78.35 ? 280  LYS A CE  1 
ATOM   2073 N NZ  . LYS A 1 280 ? -126.044 -39.303 44.926 1.00 76.94 ? 280  LYS A NZ  1 
ATOM   2074 N N   . MET A 1 281 ? -127.263 -40.989 38.660 1.00 80.80 ? 281  MET A N   1 
ATOM   2075 C CA  . MET A 1 281 ? -127.967 -40.115 37.727 1.00 81.68 ? 281  MET A CA  1 
ATOM   2076 C C   . MET A 1 281 ? -129.402 -40.584 37.507 1.00 82.61 ? 281  MET A C   1 
ATOM   2077 O O   . MET A 1 281 ? -130.308 -39.774 37.320 1.00 82.04 ? 281  MET A O   1 
ATOM   2078 C CB  . MET A 1 281 ? -127.235 -40.069 36.386 1.00 81.03 ? 281  MET A CB  1 
ATOM   2079 C CG  . MET A 1 281 ? -125.834 -39.499 36.453 1.00 80.25 ? 281  MET A CG  1 
ATOM   2080 S SD  . MET A 1 281 ? -125.130 -39.310 34.808 1.00 80.38 ? 281  MET A SD  1 
ATOM   2081 C CE  . MET A 1 281 ? -124.415 -40.933 34.546 1.00 79.99 ? 281  MET A CE  1 
ATOM   2082 N N   . LYS A 1 282 ? -129.604 -41.896 37.529 1.00 84.07 ? 282  LYS A N   1 
ATOM   2083 C CA  . LYS A 1 282 ? -130.934 -42.458 37.338 1.00 85.16 ? 282  LYS A CA  1 
ATOM   2084 C C   . LYS A 1 282 ? -131.923 -41.893 38.356 1.00 85.34 ? 282  LYS A C   1 
ATOM   2085 O O   . LYS A 1 282 ? -133.019 -41.468 37.994 1.00 85.90 ? 282  LYS A O   1 
ATOM   2086 C CB  . LYS A 1 282 ? -130.886 -43.984 37.456 1.00 85.35 ? 282  LYS A CB  1 
ATOM   2087 C CG  . LYS A 1 282 ? -130.061 -44.660 36.375 1.00 86.57 ? 282  LYS A CG  1 
ATOM   2088 C CD  . LYS A 1 282 ? -130.152 -46.173 36.478 1.00 87.47 ? 282  LYS A CD  1 
ATOM   2089 C CE  . LYS A 1 282 ? -129.404 -46.845 35.338 1.00 88.55 ? 282  LYS A CE  1 
ATOM   2090 N NZ  . LYS A 1 282 ? -129.529 -48.328 35.386 1.00 90.00 ? 282  LYS A NZ  1 
ATOM   2091 N N   . HIS A 1 283 ? -131.527 -41.883 39.626 1.00 85.31 ? 283  HIS A N   1 
ATOM   2092 C CA  . HIS A 1 283 ? -132.385 -41.378 40.695 1.00 85.00 ? 283  HIS A CA  1 
ATOM   2093 C C   . HIS A 1 283 ? -132.178 -39.877 40.925 1.00 83.76 ? 283  HIS A C   1 
ATOM   2094 O O   . HIS A 1 283 ? -132.712 -39.305 41.878 1.00 82.80 ? 283  HIS A O   1 
ATOM   2095 C CB  . HIS A 1 283 ? -132.116 -42.154 41.991 1.00 87.45 ? 283  HIS A CB  1 
ATOM   2096 C CG  . HIS A 1 283 ? -133.308 -42.265 42.894 1.00 89.24 ? 283  HIS A CG  1 
ATOM   2097 N ND1 . HIS A 1 283 ? -133.926 -41.168 43.456 1.00 90.05 ? 283  HIS A ND1 1 
ATOM   2098 C CD2 . HIS A 1 283 ? -134.003 -43.347 43.322 1.00 89.95 ? 283  HIS A CD2 1 
ATOM   2099 C CE1 . HIS A 1 283 ? -134.950 -41.569 44.189 1.00 90.35 ? 283  HIS A CE1 1 
ATOM   2100 N NE2 . HIS A 1 283 ? -135.019 -42.886 44.124 1.00 90.48 ? 283  HIS A NE2 1 
ATOM   2101 N N   . CYS A 1 284 ? -131.402 -39.248 40.047 1.00 81.86 ? 284  CYS A N   1 
ATOM   2102 C CA  . CYS A 1 284 ? -131.133 -37.815 40.145 1.00 80.12 ? 284  CYS A CA  1 
ATOM   2103 C C   . CYS A 1 284 ? -131.000 -37.191 38.761 1.00 78.25 ? 284  CYS A C   1 
ATOM   2104 O O   . CYS A 1 284 ? -130.052 -37.476 38.025 1.00 78.76 ? 284  CYS A O   1 
ATOM   2105 C CB  . CYS A 1 284 ? -129.850 -37.563 40.940 1.00 81.18 ? 284  CYS A CB  1 
ATOM   2106 S SG  . CYS A 1 284 ? -129.553 -35.816 41.307 1.00 83.17 ? 284  CYS A SG  1 
ATOM   2107 N N   . SER A 1 285 ? -131.954 -36.330 38.419 1.00 75.55 ? 285  SER A N   1 
ATOM   2108 C CA  . SER A 1 285 ? -131.975 -35.664 37.120 1.00 72.28 ? 285  SER A CA  1 
ATOM   2109 C C   . SER A 1 285 ? -130.991 -34.510 36.953 1.00 69.96 ? 285  SER A C   1 
ATOM   2110 O O   . SER A 1 285 ? -130.368 -34.366 35.902 1.00 69.64 ? 285  SER A O   1 
ATOM   2111 C CB  . SER A 1 285 ? -133.385 -35.163 36.817 1.00 72.60 ? 285  SER A CB  1 
ATOM   2112 O OG  . SER A 1 285 ? -133.380 -34.299 35.693 1.00 72.41 ? 285  SER A OG  1 
ATOM   2113 N N   . LYS A 1 286 ? -130.855 -33.688 37.985 1.00 67.16 ? 286  LYS A N   1 
ATOM   2114 C CA  . LYS A 1 286 ? -129.961 -32.542 37.927 1.00 64.68 ? 286  LYS A CA  1 
ATOM   2115 C C   . LYS A 1 286 ? -128.457 -32.822 37.954 1.00 62.46 ? 286  LYS A C   1 
ATOM   2116 O O   . LYS A 1 286 ? -127.662 -31.887 38.057 1.00 62.35 ? 286  LYS A O   1 
ATOM   2117 C CB  . LYS A 1 286 ? -130.316 -31.572 39.040 1.00 63.53 ? 286  LYS A CB  1 
ATOM   2118 C CG  . LYS A 1 286 ? -130.661 -32.276 40.320 1.00 63.16 ? 286  LYS A CG  1 
ATOM   2119 C CD  . LYS A 1 286 ? -130.130 -31.506 41.503 1.00 63.24 ? 286  LYS A CD  1 
ATOM   2120 C CE  . LYS A 1 286 ? -131.248 -31.105 42.438 1.00 61.55 ? 286  LYS A CE  1 
ATOM   2121 N NZ  . LYS A 1 286 ? -132.278 -30.294 41.752 1.00 60.54 ? 286  LYS A NZ  1 
ATOM   2122 N N   . ILE A 1 287 ? -128.061 -34.090 37.860 1.00 59.62 ? 287  ILE A N   1 
ATOM   2123 C CA  . ILE A 1 287 ? -126.639 -34.419 37.838 1.00 56.29 ? 287  ILE A CA  1 
ATOM   2124 C C   . ILE A 1 287 ? -126.150 -34.467 36.401 1.00 54.24 ? 287  ILE A C   1 
ATOM   2125 O O   . ILE A 1 287 ? -126.791 -35.046 35.525 1.00 54.17 ? 287  ILE A O   1 
ATOM   2126 C CB  . ILE A 1 287 ? -126.323 -35.785 38.492 1.00 57.09 ? 287  ILE A CB  1 
ATOM   2127 C CG1 . ILE A 1 287 ? -126.496 -35.692 40.011 1.00 57.84 ? 287  ILE A CG1 1 
ATOM   2128 C CG2 . ILE A 1 287 ? -124.885 -36.212 38.139 1.00 55.97 ? 287  ILE A CG2 1 
ATOM   2129 C CD1 . ILE A 1 287 ? -125.894 -36.869 40.772 1.00 58.14 ? 287  ILE A CD1 1 
ATOM   2130 N N   . GLN A 1 288 ? -124.993 -33.869 36.173 1.00 51.70 ? 288  GLN A N   1 
ATOM   2131 C CA  . GLN A 1 288 ? -124.389 -33.831 34.860 1.00 50.65 ? 288  GLN A CA  1 
ATOM   2132 C C   . GLN A 1 288 ? -122.936 -34.240 35.057 1.00 50.39 ? 288  GLN A C   1 
ATOM   2133 O O   . GLN A 1 288 ? -122.271 -33.727 35.956 1.00 49.71 ? 288  GLN A O   1 
ATOM   2134 C CB  . GLN A 1 288 ? -124.493 -32.412 34.294 1.00 51.29 ? 288  GLN A CB  1 
ATOM   2135 C CG  . GLN A 1 288 ? -125.928 -31.960 34.050 1.00 55.21 ? 288  GLN A CG  1 
ATOM   2136 C CD  . GLN A 1 288 ? -126.000 -30.675 33.257 1.00 57.30 ? 288  GLN A CD  1 
ATOM   2137 O OE1 . GLN A 1 288 ? -125.429 -30.576 32.168 1.00 57.83 ? 288  GLN A OE1 1 
ATOM   2138 N NE2 . GLN A 1 288 ? -126.711 -29.684 33.791 1.00 58.16 ? 288  GLN A NE2 1 
ATOM   2139 N N   . VAL A 1 289 ? -122.432 -35.172 34.253 1.00 48.60 ? 289  VAL A N   1 
ATOM   2140 C CA  . VAL A 1 289 ? -121.050 -35.597 34.442 1.00 48.06 ? 289  VAL A CA  1 
ATOM   2141 C C   . VAL A 1 289 ? -120.100 -35.136 33.344 1.00 46.25 ? 289  VAL A C   1 
ATOM   2142 O O   . VAL A 1 289 ? -120.419 -35.215 32.161 1.00 47.90 ? 289  VAL A O   1 
ATOM   2143 C CB  . VAL A 1 289 ? -120.944 -37.141 34.564 1.00 46.29 ? 289  VAL A CB  1 
ATOM   2144 C CG1 . VAL A 1 289 ? -122.115 -37.686 35.358 1.00 44.76 ? 289  VAL A CG1 1 
ATOM   2145 C CG2 . VAL A 1 289 ? -120.888 -37.770 33.198 1.00 46.88 ? 289  VAL A CG2 1 
ATOM   2146 N N   . ILE A 1 290 ? -118.940 -34.630 33.742 1.00 44.48 ? 290  ILE A N   1 
ATOM   2147 C CA  . ILE A 1 290 ? -117.932 -34.213 32.779 1.00 41.93 ? 290  ILE A CA  1 
ATOM   2148 C C   . ILE A 1 290 ? -117.046 -35.439 32.612 1.00 42.66 ? 290  ILE A C   1 
ATOM   2149 O O   . ILE A 1 290 ? -116.514 -35.959 33.594 1.00 41.07 ? 290  ILE A O   1 
ATOM   2150 C CB  . ILE A 1 290 ? -117.052 -33.073 33.311 1.00 41.95 ? 290  ILE A CB  1 
ATOM   2151 C CG1 . ILE A 1 290 ? -117.901 -31.841 33.610 1.00 41.85 ? 290  ILE A CG1 1 
ATOM   2152 C CG2 . ILE A 1 290 ? -115.970 -32.741 32.293 1.00 40.04 ? 290  ILE A CG2 1 
ATOM   2153 C CD1 . ILE A 1 290 ? -117.096 -30.675 34.136 1.00 39.81 ? 290  ILE A CD1 1 
ATOM   2154 N N   . ASP A 1 291 ? -116.898 -35.906 31.380 1.00 42.32 ? 291  ASP A N   1 
ATOM   2155 C CA  . ASP A 1 291 ? -116.075 -37.078 31.106 1.00 43.64 ? 291  ASP A CA  1 
ATOM   2156 C C   . ASP A 1 291 ? -114.598 -36.689 31.123 1.00 43.11 ? 291  ASP A C   1 
ATOM   2157 O O   . ASP A 1 291 ? -114.200 -35.746 30.447 1.00 43.17 ? 291  ASP A O   1 
ATOM   2158 C CB  . ASP A 1 291 ? -116.458 -37.670 29.744 1.00 45.34 ? 291  ASP A CB  1 
ATOM   2159 C CG  . ASP A 1 291 ? -115.691 -38.935 29.417 1.00 48.00 ? 291  ASP A CG  1 
ATOM   2160 O OD1 . ASP A 1 291 ? -115.521 -39.788 30.313 1.00 50.53 ? 291  ASP A OD1 1 
ATOM   2161 O OD2 . ASP A 1 291 ? -115.266 -39.083 28.254 1.00 51.33 ? 291  ASP A OD2 1 
ATOM   2162 N N   . ILE A 1 292 ? -113.797 -37.407 31.909 1.00 41.77 ? 292  ILE A N   1 
ATOM   2163 C CA  . ILE A 1 292 ? -112.372 -37.116 32.007 1.00 41.79 ? 292  ILE A CA  1 
ATOM   2164 C C   . ILE A 1 292 ? -111.492 -38.241 31.484 1.00 41.76 ? 292  ILE A C   1 
ATOM   2165 O O   . ILE A 1 292 ? -110.266 -38.179 31.589 1.00 41.14 ? 292  ILE A O   1 
ATOM   2166 C CB  . ILE A 1 292 ? -111.961 -36.757 33.478 1.00 42.46 ? 292  ILE A CB  1 
ATOM   2167 C CG1 . ILE A 1 292 ? -112.498 -37.789 34.477 1.00 40.95 ? 292  ILE A CG1 1 
ATOM   2168 C CG2 . ILE A 1 292 ? -112.507 -35.384 33.841 1.00 40.51 ? 292  ILE A CG2 1 
ATOM   2169 C CD1 . ILE A 1 292 ? -111.828 -39.126 34.413 1.00 40.39 ? 292  ILE A CD1 1 
ATOM   2170 N N   . SER A 1 293 ? -112.122 -39.261 30.905 1.00 40.85 ? 293  SER A N   1 
ATOM   2171 C CA  . SER A 1 293 ? -111.398 -40.403 30.355 1.00 40.71 ? 293  SER A CA  1 
ATOM   2172 C C   . SER A 1 293 ? -110.359 -39.966 29.326 1.00 41.08 ? 293  SER A C   1 
ATOM   2173 O O   . SER A 1 293 ? -109.258 -40.518 29.258 1.00 41.75 ? 293  SER A O   1 
ATOM   2174 C CB  . SER A 1 293 ? -112.376 -41.387 29.700 1.00 42.03 ? 293  SER A CB  1 
ATOM   2175 O OG  . SER A 1 293 ? -112.979 -40.828 28.543 1.00 41.05 ? 293  SER A OG  1 
ATOM   2176 N N   . MET A 1 294 ? -110.713 -38.973 28.523 1.00 39.72 ? 294  MET A N   1 
ATOM   2177 C CA  . MET A 1 294 ? -109.806 -38.468 27.504 1.00 41.23 ? 294  MET A CA  1 
ATOM   2178 C C   . MET A 1 294 ? -108.573 -37.864 28.169 1.00 39.18 ? 294  MET A C   1 
ATOM   2179 O O   . MET A 1 294 ? -107.453 -38.010 27.679 1.00 38.38 ? 294  MET A O   1 
ATOM   2180 C CB  . MET A 1 294 ? -110.502 -37.403 26.650 1.00 46.88 ? 294  MET A CB  1 
ATOM   2181 C CG  . MET A 1 294 ? -112.003 -37.239 26.925 1.00 55.31 ? 294  MET A CG  1 
ATOM   2182 S SD  . MET A 1 294 ? -112.394 -36.761 28.644 1.00 63.74 ? 294  MET A SD  1 
ATOM   2183 C CE  . MET A 1 294 ? -111.664 -35.095 28.732 1.00 57.85 ? 294  MET A CE  1 
ATOM   2184 N N   . ILE A 1 295 ? -108.786 -37.177 29.284 1.00 36.89 ? 295  ILE A N   1 
ATOM   2185 C CA  . ILE A 1 295 ? -107.684 -36.559 30.011 1.00 36.56 ? 295  ILE A CA  1 
ATOM   2186 C C   . ILE A 1 295 ? -106.755 -37.636 30.564 1.00 34.81 ? 295  ILE A C   1 
ATOM   2187 O O   . ILE A 1 295 ? -105.534 -37.503 30.518 1.00 34.97 ? 295  ILE A O   1 
ATOM   2188 C CB  . ILE A 1 295 ? -108.206 -35.689 31.168 1.00 35.99 ? 295  ILE A CB  1 
ATOM   2189 C CG1 . ILE A 1 295 ? -108.988 -34.501 30.594 1.00 36.87 ? 295  ILE A CG1 1 
ATOM   2190 C CG2 . ILE A 1 295 ? -107.054 -35.230 32.034 1.00 35.43 ? 295  ILE A CG2 1 
ATOM   2191 C CD1 . ILE A 1 295 ? -109.657 -33.608 31.639 1.00 39.43 ? 295  ILE A CD1 1 
ATOM   2192 N N   . LEU A 1 296 ? -107.338 -38.712 31.072 1.00 33.43 ? 296  LEU A N   1 
ATOM   2193 C CA  . LEU A 1 296 ? -106.535 -39.797 31.623 1.00 34.34 ? 296  LEU A CA  1 
ATOM   2194 C C   . LEU A 1 296 ? -105.842 -40.565 30.514 1.00 33.24 ? 296  LEU A C   1 
ATOM   2195 O O   . LEU A 1 296 ? -104.685 -40.949 30.652 1.00 33.55 ? 296  LEU A O   1 
ATOM   2196 C CB  . LEU A 1 296 ? -107.409 -40.743 32.450 1.00 30.92 ? 296  LEU A CB  1 
ATOM   2197 C CG  . LEU A 1 296 ? -108.004 -40.131 33.719 1.00 32.02 ? 296  LEU A CG  1 
ATOM   2198 C CD1 . LEU A 1 296 ? -109.048 -41.065 34.303 1.00 28.72 ? 296  LEU A CD1 1 
ATOM   2199 C CD2 . LEU A 1 296 ? -106.886 -39.861 34.726 1.00 31.07 ? 296  LEU A CD2 1 
ATOM   2200 N N   . ALA A 1 297 ? -106.552 -40.777 29.409 1.00 33.58 ? 297  ALA A N   1 
ATOM   2201 C CA  . ALA A 1 297 ? -105.995 -41.507 28.276 1.00 34.16 ? 297  ALA A CA  1 
ATOM   2202 C C   . ALA A 1 297 ? -104.780 -40.768 27.735 1.00 34.83 ? 297  ALA A C   1 
ATOM   2203 O O   . ALA A 1 297 ? -103.752 -41.369 27.417 1.00 35.71 ? 297  ALA A O   1 
ATOM   2204 C CB  . ALA A 1 297 ? -107.053 -41.663 27.181 1.00 34.16 ? 297  ALA A CB  1 
ATOM   2205 N N   . GLU A 1 298 ? -104.900 -39.452 27.645 1.00 35.77 ? 298  GLU A N   1 
ATOM   2206 C CA  . GLU A 1 298 ? -103.814 -38.623 27.143 1.00 37.92 ? 298  GLU A CA  1 
ATOM   2207 C C   . GLU A 1 298 ? -102.607 -38.648 28.087 1.00 36.57 ? 298  GLU A C   1 
ATOM   2208 O O   . GLU A 1 298 ? -101.456 -38.638 27.639 1.00 35.07 ? 298  GLU A O   1 
ATOM   2209 C CB  . GLU A 1 298 ? -104.306 -37.189 26.960 1.00 38.83 ? 298  GLU A CB  1 
ATOM   2210 C CG  . GLU A 1 298 ? -103.402 -36.344 26.107 1.00 45.31 ? 298  GLU A CG  1 
ATOM   2211 C CD  . GLU A 1 298 ? -103.135 -36.993 24.763 1.00 48.39 ? 298  GLU A CD  1 
ATOM   2212 O OE1 . GLU A 1 298 ? -104.061 -37.637 24.219 1.00 50.38 ? 298  GLU A OE1 1 
ATOM   2213 O OE2 . GLU A 1 298 ? -102.005 -36.854 24.250 1.00 48.99 ? 298  GLU A OE2 1 
ATOM   2214 N N   . ALA A 1 299 ? -102.876 -38.670 29.391 1.00 34.81 ? 299  ALA A N   1 
ATOM   2215 C CA  . ALA A 1 299 ? -101.811 -38.704 30.388 1.00 33.35 ? 299  ALA A CA  1 
ATOM   2216 C C   . ALA A 1 299 ? -101.044 -40.015 30.266 1.00 32.32 ? 299  ALA A C   1 
ATOM   2217 O O   . ALA A 1 299 ? -99.820  -40.036 30.328 1.00 32.27 ? 299  ALA A O   1 
ATOM   2218 C CB  . ALA A 1 299 ? -102.397 -38.564 31.789 1.00 33.69 ? 299  ALA A CB  1 
ATOM   2219 N N   . ILE A 1 300 ? -101.766 -41.113 30.085 1.00 32.01 ? 300  ILE A N   1 
ATOM   2220 C CA  . ILE A 1 300 ? -101.127 -42.420 29.944 1.00 33.43 ? 300  ILE A CA  1 
ATOM   2221 C C   . ILE A 1 300 ? -100.289 -42.493 28.670 1.00 35.80 ? 300  ILE A C   1 
ATOM   2222 O O   . ILE A 1 300 ? -99.146  -42.964 28.685 1.00 35.70 ? 300  ILE A O   1 
ATOM   2223 C CB  . ILE A 1 300 ? -102.176 -43.547 29.909 1.00 33.41 ? 300  ILE A CB  1 
ATOM   2224 C CG1 . ILE A 1 300 ? -102.900 -43.607 31.256 1.00 33.00 ? 300  ILE A CG1 1 
ATOM   2225 C CG2 . ILE A 1 300 ? -101.508 -44.882 29.594 1.00 34.09 ? 300  ILE A CG2 1 
ATOM   2226 C CD1 . ILE A 1 300 ? -103.996 -44.623 31.306 1.00 32.07 ? 300  ILE A CD1 1 
ATOM   2227 N N   . ARG A 1 301 ? -100.866 -42.023 27.569 1.00 37.74 ? 301  ARG A N   1 
ATOM   2228 C CA  . ARG A 1 301 ? -100.189 -42.044 26.283 1.00 39.80 ? 301  ARG A CA  1 
ATOM   2229 C C   . ARG A 1 301 ? -98.916  -41.227 26.356 1.00 40.27 ? 301  ARG A C   1 
ATOM   2230 O O   . ARG A 1 301 ? -97.872  -41.653 25.874 1.00 41.84 ? 301  ARG A O   1 
ATOM   2231 C CB  . ARG A 1 301 ? -101.108 -41.485 25.197 1.00 43.47 ? 301  ARG A CB  1 
ATOM   2232 C CG  . ARG A 1 301 ? -100.611 -41.727 23.775 1.00 50.19 ? 301  ARG A CG  1 
ATOM   2233 C CD  . ARG A 1 301 ? -101.601 -41.188 22.747 1.00 53.39 ? 301  ARG A CD  1 
ATOM   2234 N NE  . ARG A 1 301 ? -101.017 -40.119 21.945 1.00 58.63 ? 301  ARG A NE  1 
ATOM   2235 C CZ  . ARG A 1 301 ? -100.509 -39.000 22.451 1.00 61.27 ? 301  ARG A CZ  1 
ATOM   2236 N NH1 . ARG A 1 301 ? -100.515 -38.806 23.762 1.00 65.23 ? 301  ARG A NH1 1 
ATOM   2237 N NH2 . ARG A 1 301 ? -99.991  -38.075 21.652 1.00 61.96 ? 301  ARG A NH2 1 
ATOM   2238 N N   . ARG A 1 302 ? -98.999  -40.050 26.966 1.00 41.79 ? 302  ARG A N   1 
ATOM   2239 C CA  . ARG A 1 302 ? -97.830  -39.191 27.096 1.00 42.42 ? 302  ARG A CA  1 
ATOM   2240 C C   . ARG A 1 302 ? -96.815  -39.762 28.081 1.00 42.26 ? 302  ARG A C   1 
ATOM   2241 O O   . ARG A 1 302 ? -95.609  -39.673 27.860 1.00 42.71 ? 302  ARG A O   1 
ATOM   2242 C CB  . ARG A 1 302 ? -98.270  -37.780 27.490 1.00 44.23 ? 302  ARG A CB  1 
ATOM   2243 C CG  . ARG A 1 302 ? -98.898  -37.032 26.315 1.00 49.35 ? 302  ARG A CG  1 
ATOM   2244 C CD  . ARG A 1 302 ? -99.815  -35.903 26.755 1.00 53.99 ? 302  ARG A CD  1 
ATOM   2245 N NE  . ARG A 1 302 ? -100.337 -35.163 25.608 1.00 55.81 ? 302  ARG A NE  1 
ATOM   2246 C CZ  . ARG A 1 302 ? -99.670  -34.208 24.966 1.00 57.82 ? 302  ARG A CZ  1 
ATOM   2247 N NH1 . ARG A 1 302 ? -98.453  -33.863 25.359 1.00 56.70 ? 302  ARG A NH1 1 
ATOM   2248 N NH2 . ARG A 1 302 ? -100.216 -33.604 23.917 1.00 59.55 ? 302  ARG A NH2 1 
ATOM   2249 N N   . THR A 1 303 ? -97.300  -40.357 29.166 1.00 41.99 ? 303  THR A N   1 
ATOM   2250 C CA  . THR A 1 303 ? -96.408  -40.965 30.146 1.00 43.03 ? 303  THR A CA  1 
ATOM   2251 C C   . THR A 1 303 ? -95.591  -42.056 29.461 1.00 43.79 ? 303  THR A C   1 
ATOM   2252 O O   . THR A 1 303 ? -94.396  -42.194 29.707 1.00 44.81 ? 303  THR A O   1 
ATOM   2253 C CB  . THR A 1 303 ? -97.191  -41.616 31.300 1.00 40.61 ? 303  THR A CB  1 
ATOM   2254 O OG1 . THR A 1 303 ? -97.754  -40.599 32.130 1.00 42.07 ? 303  THR A OG1 1 
ATOM   2255 C CG2 . THR A 1 303 ? -96.277  -42.500 32.130 1.00 40.79 ? 303  THR A CG2 1 
ATOM   2256 N N   . HIS A 1 304 ? -96.251  -42.829 28.602 1.00 43.64 ? 304  HIS A N   1 
ATOM   2257 C CA  . HIS A 1 304 ? -95.601  -43.916 27.878 1.00 44.87 ? 304  HIS A CA  1 
ATOM   2258 C C   . HIS A 1 304 ? -94.639  -43.421 26.796 1.00 46.05 ? 304  HIS A C   1 
ATOM   2259 O O   . HIS A 1 304 ? -93.528  -43.932 26.665 1.00 45.78 ? 304  HIS A O   1 
ATOM   2260 C CB  . HIS A 1 304 ? -96.658  -44.817 27.235 1.00 43.12 ? 304  HIS A CB  1 
ATOM   2261 C CG  . HIS A 1 304 ? -96.089  -45.945 26.432 1.00 43.66 ? 304  HIS A CG  1 
ATOM   2262 N ND1 . HIS A 1 304 ? -95.410  -47.001 27.005 1.00 43.26 ? 304  HIS A ND1 1 
ATOM   2263 C CD2 . HIS A 1 304 ? -96.122  -46.202 25.102 1.00 42.20 ? 304  HIS A CD2 1 
ATOM   2264 C CE1 . HIS A 1 304 ? -95.054  -47.857 26.066 1.00 39.46 ? 304  HIS A CE1 1 
ATOM   2265 N NE2 . HIS A 1 304 ? -95.475  -47.396 24.900 1.00 40.86 ? 304  HIS A NE2 1 
ATOM   2266 N N   . ASN A 1 305 ? -95.070  -42.430 26.024 1.00 47.03 ? 305  ASN A N   1 
ATOM   2267 C CA  . ASN A 1 305 ? -94.249  -41.901 24.942 1.00 50.15 ? 305  ASN A CA  1 
ATOM   2268 C C   . ASN A 1 305 ? -93.273  -40.817 25.388 1.00 52.22 ? 305  ASN A C   1 
ATOM   2269 O O   . ASN A 1 305 ? -92.609  -40.198 24.559 1.00 52.21 ? 305  ASN A O   1 
ATOM   2270 C CB  . ASN A 1 305 ? -95.142  -41.359 23.816 1.00 50.55 ? 305  ASN A CB  1 
ATOM   2271 C CG  . ASN A 1 305 ? -96.046  -42.432 23.213 1.00 53.72 ? 305  ASN A CG  1 
ATOM   2272 O OD1 . ASN A 1 305 ? -95.583  -43.506 22.822 1.00 55.69 ? 305  ASN A OD1 1 
ATOM   2273 N ND2 . ASN A 1 305 ? -97.341  -42.141 23.133 1.00 55.73 ? 305  ASN A ND2 1 
ATOM   2274 N N   . GLY A 1 306 ? -93.177  -40.591 26.694 1.00 53.47 ? 306  GLY A N   1 
ATOM   2275 C CA  . GLY A 1 306 ? -92.267  -39.572 27.189 1.00 54.23 ? 306  GLY A CA  1 
ATOM   2276 C C   . GLY A 1 306 ? -92.644  -38.161 26.774 1.00 55.07 ? 306  GLY A C   1 
ATOM   2277 O O   . GLY A 1 306 ? -91.825  -37.248 26.851 1.00 55.20 ? 306  GLY A O   1 
ATOM   2278 N N   . GLU A 1 307 ? -93.885  -37.976 26.337 1.00 57.10 ? 307  GLU A N   1 
ATOM   2279 C CA  . GLU A 1 307 ? -94.362  -36.659 25.911 1.00 59.00 ? 307  GLU A CA  1 
ATOM   2280 C C   . GLU A 1 307 ? -94.794  -35.830 27.122 1.00 59.92 ? 307  GLU A C   1 
ATOM   2281 O O   . GLU A 1 307 ? -95.052  -36.376 28.196 1.00 58.72 ? 307  GLU A O   1 
ATOM   2282 C CB  . GLU A 1 307 ? -95.532  -36.825 24.936 1.00 61.07 ? 307  GLU A CB  1 
ATOM   2283 C CG  . GLU A 1 307 ? -96.280  -35.541 24.564 1.00 64.96 ? 307  GLU A CG  1 
ATOM   2284 C CD  . GLU A 1 307 ? -95.490  -34.601 23.662 1.00 66.75 ? 307  GLU A CD  1 
ATOM   2285 O OE1 . GLU A 1 307 ? -94.692  -33.784 24.180 1.00 66.69 ? 307  GLU A OE1 1 
ATOM   2286 O OE2 . GLU A 1 307 ? -95.670  -34.686 22.426 1.00 67.15 ? 307  GLU A OE2 1 
ATOM   2287 N N   . SER A 1 308 ? -94.872  -34.514 26.940 1.00 60.19 ? 308  SER A N   1 
ATOM   2288 C CA  . SER A 1 308 ? -95.256  -33.600 28.009 1.00 60.50 ? 308  SER A CA  1 
ATOM   2289 C C   . SER A 1 308 ? -96.691  -33.802 28.488 1.00 61.18 ? 308  SER A C   1 
ATOM   2290 O O   . SER A 1 308 ? -97.631  -33.747 27.698 1.00 61.59 ? 308  SER A O   1 
ATOM   2291 C CB  . SER A 1 308 ? -95.072  -32.149 27.547 1.00 60.99 ? 308  SER A CB  1 
ATOM   2292 O OG  . SER A 1 308 ? -95.588  -31.230 28.499 1.00 60.63 ? 308  SER A OG  1 
ATOM   2293 N N   . VAL A 1 309 ? -96.850  -34.028 29.789 1.00 61.05 ? 309  VAL A N   1 
ATOM   2294 C CA  . VAL A 1 309 ? -98.167  -34.226 30.386 1.00 61.68 ? 309  VAL A CA  1 
ATOM   2295 C C   . VAL A 1 309 ? -98.696  -32.931 31.008 1.00 62.69 ? 309  VAL A C   1 
ATOM   2296 O O   . VAL A 1 309 ? -99.908  -32.755 31.155 1.00 60.79 ? 309  VAL A O   1 
ATOM   2297 C CB  . VAL A 1 309 ? -98.119  -35.313 31.481 1.00 61.80 ? 309  VAL A CB  1 
ATOM   2298 C CG1 . VAL A 1 309 ? -99.487  -35.478 32.112 1.00 61.12 ? 309  VAL A CG1 1 
ATOM   2299 C CG2 . VAL A 1 309 ? -97.653  -36.629 30.886 1.00 61.49 ? 309  VAL A CG2 1 
ATOM   2300 N N   . SER A 1 310 ? -97.782  -32.029 31.362 1.00 63.86 ? 310  SER A N   1 
ATOM   2301 C CA  . SER A 1 310 ? -98.136  -30.749 31.980 1.00 66.01 ? 310  SER A CA  1 
ATOM   2302 C C   . SER A 1 310 ? -99.089  -29.920 31.120 1.00 66.86 ? 310  SER A C   1 
ATOM   2303 O O   . SER A 1 310 ? -99.878  -29.128 31.637 1.00 66.14 ? 310  SER A O   1 
ATOM   2304 C CB  . SER A 1 310 ? -96.872  -29.929 32.253 1.00 66.04 ? 310  SER A CB  1 
ATOM   2305 O OG  . SER A 1 310 ? -96.253  -29.539 31.039 1.00 67.97 ? 310  SER A OG  1 
ATOM   2306 N N   . TYR A 1 311 ? -99.000  -30.096 29.806 1.00 68.00 ? 311  TYR A N   1 
ATOM   2307 C CA  . TYR A 1 311 ? -99.854  -29.374 28.871 1.00 68.75 ? 311  TYR A CA  1 
ATOM   2308 C C   . TYR A 1 311 ? -101.344 -29.612 29.174 1.00 66.46 ? 311  TYR A C   1 
ATOM   2309 O O   . TYR A 1 311 ? -102.182 -28.747 28.914 1.00 64.82 ? 311  TYR A O   1 
ATOM   2310 C CB  . TYR A 1 311 ? -99.504  -29.802 27.439 1.00 74.41 ? 311  TYR A CB  1 
ATOM   2311 C CG  . TYR A 1 311 ? -100.681 -30.234 26.602 1.00 80.32 ? 311  TYR A CG  1 
ATOM   2312 C CD1 . TYR A 1 311 ? -101.556 -29.296 26.050 1.00 83.52 ? 311  TYR A CD1 1 
ATOM   2313 C CD2 . TYR A 1 311 ? -100.945 -31.585 26.393 1.00 83.06 ? 311  TYR A CD2 1 
ATOM   2314 C CE1 . TYR A 1 311 ? -102.670 -29.698 25.315 1.00 86.11 ? 311  TYR A CE1 1 
ATOM   2315 C CE2 . TYR A 1 311 ? -102.053 -31.998 25.662 1.00 85.90 ? 311  TYR A CE2 1 
ATOM   2316 C CZ  . TYR A 1 311 ? -102.912 -31.052 25.127 1.00 86.89 ? 311  TYR A CZ  1 
ATOM   2317 O OH  . TYR A 1 311 ? -104.017 -31.466 24.415 1.00 88.32 ? 311  TYR A OH  1 
ATOM   2318 N N   . LEU A 1 312 ? -101.661 -30.779 29.731 1.00 63.65 ? 312  LEU A N   1 
ATOM   2319 C CA  . LEU A 1 312 ? -103.040 -31.129 30.075 1.00 60.98 ? 312  LEU A CA  1 
ATOM   2320 C C   . LEU A 1 312 ? -103.566 -30.324 31.259 1.00 60.57 ? 312  LEU A C   1 
ATOM   2321 O O   . LEU A 1 312 ? -104.779 -30.197 31.444 1.00 61.05 ? 312  LEU A O   1 
ATOM   2322 C CB  . LEU A 1 312 ? -103.142 -32.616 30.408 1.00 59.58 ? 312  LEU A CB  1 
ATOM   2323 C CG  . LEU A 1 312 ? -102.898 -33.604 29.271 1.00 58.75 ? 312  LEU A CG  1 
ATOM   2324 C CD1 . LEU A 1 312 ? -102.826 -35.020 29.818 1.00 56.96 ? 312  LEU A CD1 1 
ATOM   2325 C CD2 . LEU A 1 312 ? -104.016 -33.469 28.252 1.00 59.34 ? 312  LEU A CD2 1 
ATOM   2326 N N   . PHE A 1 313 ? -102.653 -29.795 32.067 1.00 59.86 ? 313  PHE A N   1 
ATOM   2327 C CA  . PHE A 1 313 ? -103.026 -29.005 33.237 1.00 59.28 ? 313  PHE A CA  1 
ATOM   2328 C C   . PHE A 1 313 ? -103.961 -27.854 32.858 1.00 58.89 ? 313  PHE A C   1 
ATOM   2329 O O   . PHE A 1 313 ? -104.741 -27.418 33.734 1.00 58.53 ? 313  PHE A O   1 
ATOM   2330 C CB  . PHE A 1 313 ? -101.768 -28.462 33.935 1.00 58.26 ? 313  PHE A CB  1 
ATOM   2331 C CG  . PHE A 1 313 ? -100.871 -29.535 34.507 1.00 57.70 ? 313  PHE A CG  1 
ATOM   2332 C CD1 . PHE A 1 313 ? -99.600  -29.214 34.980 1.00 57.84 ? 313  PHE A CD1 1 
ATOM   2333 C CD2 . PHE A 1 313 ? -101.290 -30.864 34.569 1.00 57.55 ? 313  PHE A CD2 1 
ATOM   2334 C CE1 . PHE A 1 313 ? -98.759  -30.198 35.504 1.00 56.45 ? 313  PHE A CE1 1 
ATOM   2335 C CE2 . PHE A 1 313 ? -100.457 -31.856 35.091 1.00 56.38 ? 313  PHE A CE2 1 
ATOM   2336 C CZ  . PHE A 1 313 ? -99.190  -31.522 35.559 1.00 57.27 ? 313  PHE A CZ  1 
ATOM   2337 N N   . ASN B 1 3   ? -80.375  -38.845 81.272 1.00 49.86 ? 3    ASN B N   1 
ATOM   2338 C CA  . ASN B 1 3   ? -79.506  -39.106 80.089 1.00 46.68 ? 3    ASN B CA  1 
ATOM   2339 C C   . ASN B 1 3   ? -79.923  -38.262 78.883 1.00 45.15 ? 3    ASN B C   1 
ATOM   2340 O O   . ASN B 1 3   ? -79.785  -38.680 77.732 1.00 45.32 ? 3    ASN B O   1 
ATOM   2341 C CB  . ASN B 1 3   ? -79.538  -40.598 79.735 1.00 49.25 ? 3    ASN B CB  1 
ATOM   2342 C CG  . ASN B 1 3   ? -80.948  -41.127 79.535 1.00 51.99 ? 3    ASN B CG  1 
ATOM   2343 O OD1 . ASN B 1 3   ? -81.926  -40.399 79.712 1.00 52.58 ? 3    ASN B OD1 1 
ATOM   2344 N ND2 . ASN B 1 3   ? -81.060  -42.404 79.167 1.00 50.78 ? 3    ASN B ND2 1 
ATOM   2345 N N   . ILE B 1 4   ? -80.433  -37.068 79.160 1.00 40.28 ? 4    ILE B N   1 
ATOM   2346 C CA  . ILE B 1 4   ? -80.858  -36.142 78.120 1.00 37.71 ? 4    ILE B CA  1 
ATOM   2347 C C   . ILE B 1 4   ? -79.659  -35.255 77.769 1.00 35.80 ? 4    ILE B C   1 
ATOM   2348 O O   . ILE B 1 4   ? -78.945  -34.798 78.655 1.00 36.37 ? 4    ILE B O   1 
ATOM   2349 C CB  . ILE B 1 4   ? -82.042  -35.272 78.635 1.00 39.19 ? 4    ILE B CB  1 
ATOM   2350 C CG1 . ILE B 1 4   ? -82.623  -34.396 77.519 1.00 37.86 ? 4    ILE B CG1 1 
ATOM   2351 C CG2 . ILE B 1 4   ? -81.573  -34.425 79.808 1.00 42.63 ? 4    ILE B CG2 1 
ATOM   2352 C CD1 . ILE B 1 4   ? -81.800  -33.162 77.188 1.00 39.50 ? 4    ILE B CD1 1 
ATOM   2353 N N   . LYS B 1 5   ? -79.425  -35.035 76.478 1.00 32.96 ? 5    LYS B N   1 
ATOM   2354 C CA  . LYS B 1 5   ? -78.316  -34.196 76.031 1.00 31.51 ? 5    LYS B CA  1 
ATOM   2355 C C   . LYS B 1 5   ? -78.810  -33.213 74.968 1.00 30.47 ? 5    LYS B C   1 
ATOM   2356 O O   . LYS B 1 5   ? -79.347  -33.617 73.937 1.00 28.02 ? 5    LYS B O   1 
ATOM   2357 C CB  . LYS B 1 5   ? -77.198  -35.062 75.450 1.00 34.93 ? 5    LYS B CB  1 
ATOM   2358 C CG  . LYS B 1 5   ? -75.825  -34.827 76.070 1.00 39.91 ? 5    LYS B CG  1 
ATOM   2359 C CD  . LYS B 1 5   ? -75.803  -35.229 77.544 1.00 45.10 ? 5    LYS B CD  1 
ATOM   2360 C CE  . LYS B 1 5   ? -74.428  -35.043 78.173 1.00 47.60 ? 5    LYS B CE  1 
ATOM   2361 N NZ  . LYS B 1 5   ? -74.378  -35.472 79.613 1.00 48.72 ? 5    LYS B NZ  1 
ATOM   2362 N N   . ILE B 1 6   ? -78.633  -31.920 75.211 1.00 28.24 ? 6    ILE B N   1 
ATOM   2363 C CA  . ILE B 1 6   ? -79.083  -30.937 74.240 1.00 28.12 ? 6    ILE B CA  1 
ATOM   2364 C C   . ILE B 1 6   ? -77.924  -30.141 73.648 1.00 28.47 ? 6    ILE B C   1 
ATOM   2365 O O   . ILE B 1 6   ? -77.074  -29.642 74.380 1.00 29.33 ? 6    ILE B O   1 
ATOM   2366 C CB  . ILE B 1 6   ? -80.118  -29.976 74.861 1.00 27.83 ? 6    ILE B CB  1 
ATOM   2367 C CG1 . ILE B 1 6   ? -80.482  -28.890 73.848 1.00 28.30 ? 6    ILE B CG1 1 
ATOM   2368 C CG2 . ILE B 1 6   ? -79.576  -29.382 76.154 1.00 26.69 ? 6    ILE B CG2 1 
ATOM   2369 C CD1 . ILE B 1 6   ? -81.662  -28.041 74.261 1.00 33.14 ? 6    ILE B CD1 1 
ATOM   2370 N N   . PHE B 1 7   ? -77.889  -30.047 72.319 1.00 26.92 ? 7    PHE B N   1 
ATOM   2371 C CA  . PHE B 1 7   ? -76.837  -29.309 71.612 1.00 32.30 ? 7    PHE B CA  1 
ATOM   2372 C C   . PHE B 1 7   ? -77.432  -28.187 70.762 1.00 34.28 ? 7    PHE B C   1 
ATOM   2373 O O   . PHE B 1 7   ? -78.584  -28.259 70.333 1.00 33.57 ? 7    PHE B O   1 
ATOM   2374 C CB  . PHE B 1 7   ? -76.026  -30.228 70.684 1.00 31.10 ? 7    PHE B CB  1 
ATOM   2375 C CG  . PHE B 1 7   ? -75.213  -31.283 71.399 1.00 32.03 ? 7    PHE B CG  1 
ATOM   2376 C CD1 . PHE B 1 7   ? -75.800  -32.460 71.838 1.00 32.45 ? 7    PHE B CD1 1 
ATOM   2377 C CD2 . PHE B 1 7   ? -73.851  -31.109 71.593 1.00 29.61 ? 7    PHE B CD2 1 
ATOM   2378 C CE1 . PHE B 1 7   ? -75.033  -33.452 72.453 1.00 36.32 ? 7    PHE B CE1 1 
ATOM   2379 C CE2 . PHE B 1 7   ? -73.080  -32.086 72.203 1.00 30.24 ? 7    PHE B CE2 1 
ATOM   2380 C CZ  . PHE B 1 7   ? -73.669  -33.264 72.636 1.00 33.54 ? 7    PHE B CZ  1 
ATOM   2381 N N   . SER B 1 8   ? -76.639  -27.154 70.517 1.00 40.08 ? 8    SER B N   1 
ATOM   2382 C CA  . SER B 1 8   ? -77.089  -26.033 69.710 1.00 47.75 ? 8    SER B CA  1 
ATOM   2383 C C   . SER B 1 8   ? -76.430  -26.055 68.342 1.00 53.34 ? 8    SER B C   1 
ATOM   2384 O O   . SER B 1 8   ? -75.262  -26.427 68.207 1.00 52.89 ? 8    SER B O   1 
ATOM   2385 C CB  . SER B 1 8   ? -76.760  -24.713 70.393 1.00 49.81 ? 8    SER B CB  1 
ATOM   2386 O OG  . SER B 1 8   ? -77.159  -23.626 69.577 1.00 53.39 ? 8    SER B OG  1 
ATOM   2387 N N   . GLY B 1 9   ? -77.193  -25.639 67.335 1.00 59.67 ? 9    GLY B N   1 
ATOM   2388 C CA  . GLY B 1 9   ? -76.701  -25.603 65.972 1.00 66.11 ? 9    GLY B CA  1 
ATOM   2389 C C   . GLY B 1 9   ? -75.388  -24.864 65.773 1.00 71.71 ? 9    GLY B C   1 
ATOM   2390 O O   . GLY B 1 9   ? -74.361  -25.492 65.512 1.00 73.79 ? 9    GLY B O   1 
ATOM   2391 N N   . SER B 1 10  ? -75.409  -23.537 65.898 1.00 75.81 ? 10   SER B N   1 
ATOM   2392 C CA  . SER B 1 10  ? -74.208  -22.729 65.700 1.00 79.92 ? 10   SER B CA  1 
ATOM   2393 C C   . SER B 1 10  ? -73.910  -21.809 66.878 1.00 81.75 ? 10   SER B C   1 
ATOM   2394 O O   . SER B 1 10  ? -74.103  -22.181 68.034 1.00 82.61 ? 10   SER B O   1 
ATOM   2395 C CB  . SER B 1 10  ? -74.345  -21.882 64.431 1.00 81.37 ? 10   SER B CB  1 
ATOM   2396 O OG  . SER B 1 10  ? -75.307  -20.854 64.611 1.00 82.70 ? 10   SER B OG  1 
ATOM   2397 N N   . SER B 1 11  ? -73.435  -20.603 66.571 1.00 83.56 ? 11   SER B N   1 
ATOM   2398 C CA  . SER B 1 11  ? -73.099  -19.623 67.598 1.00 84.94 ? 11   SER B CA  1 
ATOM   2399 C C   . SER B 1 11  ? -74.347  -18.977 68.184 1.00 84.50 ? 11   SER B C   1 
ATOM   2400 O O   . SER B 1 11  ? -74.278  -18.262 69.188 1.00 85.29 ? 11   SER B O   1 
ATOM   2401 C CB  . SER B 1 11  ? -72.189  -18.539 67.020 1.00 85.70 ? 11   SER B CB  1 
ATOM   2402 O OG  . SER B 1 11  ? -71.814  -17.620 68.029 1.00 86.23 ? 11   SER B OG  1 
ATOM   2403 N N   . HIS B 1 12  ? -75.487  -19.229 67.549 1.00 82.91 ? 12   HIS B N   1 
ATOM   2404 C CA  . HIS B 1 12  ? -76.753  -18.680 68.012 1.00 80.80 ? 12   HIS B CA  1 
ATOM   2405 C C   . HIS B 1 12  ? -77.303  -19.487 69.177 1.00 78.60 ? 12   HIS B C   1 
ATOM   2406 O O   . HIS B 1 12  ? -78.424  -19.990 69.122 1.00 78.01 ? 12   HIS B O   1 
ATOM   2407 C CB  . HIS B 1 12  ? -77.760  -18.657 66.867 1.00 82.18 ? 12   HIS B CB  1 
ATOM   2408 C CG  . HIS B 1 12  ? -77.538  -17.542 65.897 1.00 83.71 ? 12   HIS B CG  1 
ATOM   2409 N ND1 . HIS B 1 12  ? -78.005  -16.262 66.113 1.00 83.90 ? 12   HIS B ND1 1 
ATOM   2410 C CD2 . HIS B 1 12  ? -76.881  -17.507 64.715 1.00 83.92 ? 12   HIS B CD2 1 
ATOM   2411 C CE1 . HIS B 1 12  ? -77.648  -15.490 65.104 1.00 84.11 ? 12   HIS B CE1 1 
ATOM   2412 N NE2 . HIS B 1 12  ? -76.964  -16.220 64.240 1.00 84.13 ? 12   HIS B NE2 1 
ATOM   2413 N N   . GLN B 1 13  ? -76.501  -19.611 70.231 1.00 74.73 ? 13   GLN B N   1 
ATOM   2414 C CA  . GLN B 1 13  ? -76.906  -20.348 71.422 1.00 70.55 ? 13   GLN B CA  1 
ATOM   2415 C C   . GLN B 1 13  ? -78.245  -19.793 71.918 1.00 65.95 ? 13   GLN B C   1 
ATOM   2416 O O   . GLN B 1 13  ? -79.016  -20.488 72.573 1.00 66.47 ? 13   GLN B O   1 
ATOM   2417 C CB  . GLN B 1 13  ? -75.851  -20.187 72.521 1.00 72.66 ? 13   GLN B CB  1 
ATOM   2418 C CG  . GLN B 1 13  ? -74.420  -20.522 72.106 1.00 74.79 ? 13   GLN B CG  1 
ATOM   2419 C CD  . GLN B 1 13  ? -74.198  -22.004 71.877 1.00 75.91 ? 13   GLN B CD  1 
ATOM   2420 O OE1 . GLN B 1 13  ? -74.797  -22.601 70.985 1.00 77.25 ? 13   GLN B OE1 1 
ATOM   2421 N NE2 . GLN B 1 13  ? -73.333  -22.608 72.687 1.00 76.18 ? 13   GLN B NE2 1 
ATOM   2422 N N   . ASP B 1 14  ? -78.502  -18.534 71.581 1.00 58.81 ? 14   ASP B N   1 
ATOM   2423 C CA  . ASP B 1 14  ? -79.707  -17.811 71.969 1.00 53.53 ? 14   ASP B CA  1 
ATOM   2424 C C   . ASP B 1 14  ? -80.897  -18.654 72.437 1.00 49.78 ? 14   ASP B C   1 
ATOM   2425 O O   . ASP B 1 14  ? -81.063  -18.898 73.630 1.00 47.02 ? 14   ASP B O   1 
ATOM   2426 C CB  . ASP B 1 14  ? -80.146  -16.911 70.815 1.00 57.08 ? 14   ASP B CB  1 
ATOM   2427 C CG  . ASP B 1 14  ? -80.848  -15.663 71.294 1.00 57.96 ? 14   ASP B CG  1 
ATOM   2428 O OD1 . ASP B 1 14  ? -81.070  -15.557 72.521 1.00 59.30 ? 14   ASP B OD1 1 
ATOM   2429 O OD2 . ASP B 1 14  ? -81.173  -14.793 70.450 1.00 59.46 ? 14   ASP B OD2 1 
ATOM   2430 N N   . LEU B 1 15  ? -81.729  -19.082 71.492 1.00 45.53 ? 15   LEU B N   1 
ATOM   2431 C CA  . LEU B 1 15  ? -82.907  -19.888 71.797 1.00 41.08 ? 15   LEU B CA  1 
ATOM   2432 C C   . LEU B 1 15  ? -82.525  -21.202 72.489 1.00 39.30 ? 15   LEU B C   1 
ATOM   2433 O O   . LEU B 1 15  ? -83.140  -21.592 73.485 1.00 37.45 ? 15   LEU B O   1 
ATOM   2434 C CB  . LEU B 1 15  ? -83.665  -20.214 70.509 1.00 39.64 ? 15   LEU B CB  1 
ATOM   2435 C CG  . LEU B 1 15  ? -85.185  -20.384 70.540 1.00 41.18 ? 15   LEU B CG  1 
ATOM   2436 C CD1 . LEU B 1 15  ? -85.598  -21.269 69.359 1.00 39.80 ? 15   LEU B CD1 1 
ATOM   2437 C CD2 . LEU B 1 15  ? -85.641  -21.008 71.839 1.00 40.85 ? 15   LEU B CD2 1 
ATOM   2438 N N   . SER B 1 16  ? -81.511  -21.883 71.963 1.00 37.31 ? 16   SER B N   1 
ATOM   2439 C CA  . SER B 1 16  ? -81.101  -23.159 72.535 1.00 37.56 ? 16   SER B CA  1 
ATOM   2440 C C   . SER B 1 16  ? -80.653  -23.054 73.987 1.00 36.42 ? 16   SER B C   1 
ATOM   2441 O O   . SER B 1 16  ? -80.837  -23.991 74.758 1.00 35.47 ? 16   SER B O   1 
ATOM   2442 C CB  . SER B 1 16  ? -80.012  -23.819 71.669 1.00 38.13 ? 16   SER B CB  1 
ATOM   2443 O OG  . SER B 1 16  ? -78.944  -22.935 71.383 1.00 39.75 ? 16   SER B OG  1 
ATOM   2444 N N   . GLN B 1 17  ? -80.088  -21.909 74.366 1.00 35.67 ? 17   GLN B N   1 
ATOM   2445 C CA  . GLN B 1 17  ? -79.635  -21.701 75.739 1.00 34.33 ? 17   GLN B CA  1 
ATOM   2446 C C   . GLN B 1 17  ? -80.820  -21.503 76.681 1.00 33.43 ? 17   GLN B C   1 
ATOM   2447 O O   . GLN B 1 17  ? -80.797  -21.953 77.827 1.00 32.46 ? 17   GLN B O   1 
ATOM   2448 C CB  . GLN B 1 17  ? -78.702  -20.490 75.822 1.00 36.33 ? 17   GLN B CB  1 
ATOM   2449 C CG  . GLN B 1 17  ? -78.121  -20.269 77.208 1.00 37.60 ? 17   GLN B CG  1 
ATOM   2450 C CD  . GLN B 1 17  ? -77.360  -21.485 77.723 1.00 41.04 ? 17   GLN B CD  1 
ATOM   2451 O OE1 . GLN B 1 17  ? -76.361  -21.904 77.133 1.00 42.53 ? 17   GLN B OE1 1 
ATOM   2452 N NE2 . GLN B 1 17  ? -77.830  -22.055 78.828 1.00 41.30 ? 17   GLN B NE2 1 
ATOM   2453 N N   . LYS B 1 18  ? -81.857  -20.826 76.205 1.00 32.87 ? 18   LYS B N   1 
ATOM   2454 C CA  . LYS B 1 18  ? -83.042  -20.616 77.031 1.00 33.53 ? 18   LYS B CA  1 
ATOM   2455 C C   . LYS B 1 18  ? -83.701  -21.957 77.326 1.00 31.15 ? 18   LYS B C   1 
ATOM   2456 O O   . LYS B 1 18  ? -84.166  -22.203 78.438 1.00 33.03 ? 18   LYS B O   1 
ATOM   2457 C CB  . LYS B 1 18  ? -84.052  -19.715 76.320 1.00 34.40 ? 18   LYS B CB  1 
ATOM   2458 C CG  . LYS B 1 18  ? -83.636  -18.273 76.223 1.00 37.69 ? 18   LYS B CG  1 
ATOM   2459 C CD  . LYS B 1 18  ? -84.760  -17.437 75.629 1.00 42.11 ? 18   LYS B CD  1 
ATOM   2460 C CE  . LYS B 1 18  ? -84.486  -15.952 75.784 1.00 44.13 ? 18   LYS B CE  1 
ATOM   2461 N NZ  . LYS B 1 18  ? -85.677  -15.147 75.393 1.00 49.42 ? 18   LYS B NZ  1 
ATOM   2462 N N   . ILE B 1 19  ? -83.751  -22.812 76.311 1.00 28.45 ? 19   ILE B N   1 
ATOM   2463 C CA  . ILE B 1 19  ? -84.348  -24.132 76.444 1.00 27.07 ? 19   ILE B CA  1 
ATOM   2464 C C   . ILE B 1 19  ? -83.559  -24.957 77.453 1.00 27.02 ? 19   ILE B C   1 
ATOM   2465 O O   . ILE B 1 19  ? -84.135  -25.552 78.358 1.00 26.64 ? 19   ILE B O   1 
ATOM   2466 C CB  . ILE B 1 19  ? -84.370  -24.867 75.081 1.00 25.51 ? 19   ILE B CB  1 
ATOM   2467 C CG1 . ILE B 1 19  ? -85.363  -24.171 74.142 1.00 27.64 ? 19   ILE B CG1 1 
ATOM   2468 C CG2 . ILE B 1 19  ? -84.771  -26.327 75.269 1.00 25.20 ? 19   ILE B CG2 1 
ATOM   2469 C CD1 . ILE B 1 19  ? -85.298  -24.638 72.700 1.00 21.72 ? 19   ILE B CD1 1 
ATOM   2470 N N   . ALA B 1 20  ? -82.237  -24.978 77.292 1.00 28.79 ? 20   ALA B N   1 
ATOM   2471 C CA  . ALA B 1 20  ? -81.361  -25.734 78.184 1.00 30.65 ? 20   ALA B CA  1 
ATOM   2472 C C   . ALA B 1 20  ? -81.518  -25.231 79.615 1.00 31.71 ? 20   ALA B C   1 
ATOM   2473 O O   . ALA B 1 20  ? -81.557  -26.028 80.545 1.00 30.36 ? 20   ALA B O   1 
ATOM   2474 C CB  . ALA B 1 20  ? -79.910  -25.606 77.734 1.00 29.10 ? 20   ALA B CB  1 
ATOM   2475 N N   . ASP B 1 21  ? -81.615  -23.912 79.782 1.00 35.06 ? 21   ASP B N   1 
ATOM   2476 C CA  . ASP B 1 21  ? -81.792  -23.327 81.111 1.00 38.23 ? 21   ASP B CA  1 
ATOM   2477 C C   . ASP B 1 21  ? -83.083  -23.848 81.725 1.00 40.06 ? 21   ASP B C   1 
ATOM   2478 O O   . ASP B 1 21  ? -83.103  -24.271 82.883 1.00 40.51 ? 21   ASP B O   1 
ATOM   2479 C CB  . ASP B 1 21  ? -81.861  -21.793 81.053 1.00 39.00 ? 21   ASP B CB  1 
ATOM   2480 C CG  . ASP B 1 21  ? -80.535  -21.156 80.688 1.00 41.65 ? 21   ASP B CG  1 
ATOM   2481 O OD1 . ASP B 1 21  ? -79.486  -21.794 80.898 1.00 43.17 ? 21   ASP B OD1 1 
ATOM   2482 O OD2 . ASP B 1 21  ? -80.533  -20.003 80.204 1.00 45.32 ? 21   ASP B OD2 1 
ATOM   2483 N N   . ARG B 1 22  ? -84.161  -23.827 80.945 1.00 40.02 ? 22   ARG B N   1 
ATOM   2484 C CA  . ARG B 1 22  ? -85.453  -24.292 81.436 1.00 39.82 ? 22   ARG B CA  1 
ATOM   2485 C C   . ARG B 1 22  ? -85.456  -25.770 81.787 1.00 39.48 ? 22   ARG B C   1 
ATOM   2486 O O   . ARG B 1 22  ? -86.319  -26.229 82.533 1.00 41.02 ? 22   ARG B O   1 
ATOM   2487 C CB  . ARG B 1 22  ? -86.551  -23.998 80.416 1.00 39.78 ? 22   ARG B CB  1 
ATOM   2488 C CG  . ARG B 1 22  ? -86.932  -22.527 80.351 1.00 44.48 ? 22   ARG B CG  1 
ATOM   2489 C CD  . ARG B 1 22  ? -87.999  -22.259 79.306 1.00 48.11 ? 22   ARG B CD  1 
ATOM   2490 N NE  . ARG B 1 22  ? -88.757  -21.044 79.593 1.00 55.37 ? 22   ARG B NE  1 
ATOM   2491 C CZ  . ARG B 1 22  ? -88.214  -19.845 79.790 1.00 59.05 ? 22   ARG B CZ  1 
ATOM   2492 N NH1 . ARG B 1 22  ? -86.895  -19.693 79.734 1.00 61.81 ? 22   ARG B NH1 1 
ATOM   2493 N NH2 . ARG B 1 22  ? -88.989  -18.793 80.033 1.00 59.87 ? 22   ARG B NH2 1 
ATOM   2494 N N   . LEU B 1 23  ? -84.496  -26.517 81.254 1.00 36.85 ? 23   LEU B N   1 
ATOM   2495 C CA  . LEU B 1 23  ? -84.417  -27.946 81.540 1.00 34.26 ? 23   LEU B CA  1 
ATOM   2496 C C   . LEU B 1 23  ? -83.410  -28.222 82.652 1.00 32.23 ? 23   LEU B C   1 
ATOM   2497 O O   . LEU B 1 23  ? -83.246  -29.360 83.078 1.00 32.18 ? 23   LEU B O   1 
ATOM   2498 C CB  . LEU B 1 23  ? -84.029  -28.721 80.272 1.00 32.24 ? 23   LEU B CB  1 
ATOM   2499 C CG  . LEU B 1 23  ? -85.029  -28.678 79.107 1.00 31.22 ? 23   LEU B CG  1 
ATOM   2500 C CD1 . LEU B 1 23  ? -84.460  -29.372 77.889 1.00 28.96 ? 23   LEU B CD1 1 
ATOM   2501 C CD2 . LEU B 1 23  ? -86.325  -29.346 79.533 1.00 29.52 ? 23   LEU B CD2 1 
ATOM   2502 N N   . GLY B 1 24  ? -82.743  -27.168 83.111 1.00 33.59 ? 24   GLY B N   1 
ATOM   2503 C CA  . GLY B 1 24  ? -81.748  -27.297 84.166 1.00 32.19 ? 24   GLY B CA  1 
ATOM   2504 C C   . GLY B 1 24  ? -80.486  -27.934 83.629 1.00 32.93 ? 24   GLY B C   1 
ATOM   2505 O O   . GLY B 1 24  ? -79.767  -28.623 84.351 1.00 32.15 ? 24   GLY B O   1 
ATOM   2506 N N   . LEU B 1 25  ? -80.207  -27.689 82.351 1.00 32.53 ? 25   LEU B N   1 
ATOM   2507 C CA  . LEU B 1 25  ? -79.044  -28.271 81.698 1.00 31.33 ? 25   LEU B CA  1 
ATOM   2508 C C   . LEU B 1 25  ? -78.158  -27.247 81.016 1.00 32.36 ? 25   LEU B C   1 
ATOM   2509 O O   . LEU B 1 25  ? -78.575  -26.124 80.743 1.00 30.52 ? 25   LEU B O   1 
ATOM   2510 C CB  . LEU B 1 25  ? -79.504  -29.272 80.630 1.00 30.23 ? 25   LEU B CB  1 
ATOM   2511 C CG  . LEU B 1 25  ? -80.449  -30.399 81.043 1.00 30.77 ? 25   LEU B CG  1 
ATOM   2512 C CD1 . LEU B 1 25  ? -80.921  -31.144 79.798 1.00 31.20 ? 25   LEU B CD1 1 
ATOM   2513 C CD2 . LEU B 1 25  ? -79.739  -31.350 82.016 1.00 29.46 ? 25   LEU B CD2 1 
ATOM   2514 N N   . GLU B 1 26  ? -76.925  -27.650 80.738 1.00 32.92 ? 26   GLU B N   1 
ATOM   2515 C CA  . GLU B 1 26  ? -76.002  -26.803 80.004 1.00 33.65 ? 26   GLU B CA  1 
ATOM   2516 C C   . GLU B 1 26  ? -75.980  -27.393 78.601 1.00 33.71 ? 26   GLU B C   1 
ATOM   2517 O O   . GLU B 1 26  ? -76.230  -28.587 78.414 1.00 31.82 ? 26   GLU B O   1 
ATOM   2518 C CB  . GLU B 1 26  ? -74.595  -26.871 80.582 1.00 35.35 ? 26   GLU B CB  1 
ATOM   2519 C CG  . GLU B 1 26  ? -74.478  -26.372 82.010 1.00 43.54 ? 26   GLU B CG  1 
ATOM   2520 C CD  . GLU B 1 26  ? -73.036  -26.184 82.417 1.00 46.97 ? 26   GLU B CD  1 
ATOM   2521 O OE1 . GLU B 1 26  ? -72.195  -27.019 82.011 1.00 48.97 ? 26   GLU B OE1 1 
ATOM   2522 O OE2 . GLU B 1 26  ? -72.746  -25.209 83.143 1.00 49.57 ? 26   GLU B OE2 1 
ATOM   2523 N N   . LEU B 1 27  ? -75.710  -26.558 77.610 1.00 32.27 ? 27   LEU B N   1 
ATOM   2524 C CA  . LEU B 1 27  ? -75.633  -27.048 76.245 1.00 30.86 ? 27   LEU B CA  1 
ATOM   2525 C C   . LEU B 1 27  ? -74.375  -27.901 76.153 1.00 29.02 ? 27   LEU B C   1 
ATOM   2526 O O   . LEU B 1 27  ? -73.349  -27.546 76.719 1.00 27.64 ? 27   LEU B O   1 
ATOM   2527 C CB  . LEU B 1 27  ? -75.544  -25.876 75.268 1.00 29.93 ? 27   LEU B CB  1 
ATOM   2528 C CG  . LEU B 1 27  ? -76.858  -25.138 74.995 1.00 30.85 ? 27   LEU B CG  1 
ATOM   2529 C CD1 . LEU B 1 27  ? -76.586  -23.880 74.177 1.00 28.57 ? 27   LEU B CD1 1 
ATOM   2530 C CD2 . LEU B 1 27  ? -77.821  -26.064 74.252 1.00 30.15 ? 27   LEU B CD2 1 
ATOM   2531 N N   . GLY B 1 28  ? -74.464  -29.029 75.453 1.00 29.72 ? 28   GLY B N   1 
ATOM   2532 C CA  . GLY B 1 28  ? -73.318  -29.908 75.294 1.00 29.46 ? 28   GLY B CA  1 
ATOM   2533 C C   . GLY B 1 28  ? -72.201  -29.255 74.504 1.00 31.30 ? 28   GLY B C   1 
ATOM   2534 O O   . GLY B 1 28  ? -72.435  -28.328 73.725 1.00 29.28 ? 28   GLY B O   1 
ATOM   2535 N N   . LYS B 1 29  ? -70.980  -29.735 74.706 1.00 34.17 ? 29   LYS B N   1 
ATOM   2536 C CA  . LYS B 1 29  ? -69.821  -29.182 74.021 1.00 38.81 ? 29   LYS B CA  1 
ATOM   2537 C C   . LYS B 1 29  ? -69.736  -29.624 72.564 1.00 41.60 ? 29   LYS B C   1 
ATOM   2538 O O   . LYS B 1 29  ? -69.953  -30.797 72.243 1.00 41.04 ? 29   LYS B O   1 
ATOM   2539 C CB  . LYS B 1 29  ? -68.541  -29.583 74.755 1.00 41.23 ? 29   LYS B CB  1 
ATOM   2540 C CG  . LYS B 1 29  ? -68.474  -29.076 76.190 1.00 48.82 ? 29   LYS B CG  1 
ATOM   2541 C CD  . LYS B 1 29  ? -68.543  -27.544 76.243 1.00 53.02 ? 29   LYS B CD  1 
ATOM   2542 C CE  . LYS B 1 29  ? -68.546  -27.017 77.677 1.00 53.74 ? 29   LYS B CE  1 
ATOM   2543 N NZ  . LYS B 1 29  ? -68.553  -25.528 77.710 1.00 53.83 ? 29   LYS B NZ  1 
ATOM   2544 N N   . VAL B 1 30  ? -69.423  -28.671 71.690 1.00 42.97 ? 30   VAL B N   1 
ATOM   2545 C CA  . VAL B 1 30  ? -69.293  -28.938 70.263 1.00 45.99 ? 30   VAL B CA  1 
ATOM   2546 C C   . VAL B 1 30  ? -68.166  -28.119 69.643 1.00 47.73 ? 30   VAL B C   1 
ATOM   2547 O O   . VAL B 1 30  ? -68.251  -26.895 69.574 1.00 48.57 ? 30   VAL B O   1 
ATOM   2548 C CB  . VAL B 1 30  ? -70.587  -28.593 69.497 1.00 45.56 ? 30   VAL B CB  1 
ATOM   2549 C CG1 . VAL B 1 30  ? -70.409  -28.900 68.019 1.00 46.77 ? 30   VAL B CG1 1 
ATOM   2550 C CG2 . VAL B 1 30  ? -71.744  -29.382 70.049 1.00 46.05 ? 30   VAL B CG2 1 
ATOM   2551 N N   . VAL B 1 31  ? -67.117  -28.798 69.190 1.00 49.85 ? 31   VAL B N   1 
ATOM   2552 C CA  . VAL B 1 31  ? -65.988  -28.130 68.551 1.00 52.02 ? 31   VAL B CA  1 
ATOM   2553 C C   . VAL B 1 31  ? -66.357  -27.882 67.090 1.00 53.37 ? 31   VAL B C   1 
ATOM   2554 O O   . VAL B 1 31  ? -66.563  -28.825 66.324 1.00 52.40 ? 31   VAL B O   1 
ATOM   2555 C CB  . VAL B 1 31  ? -64.713  -29.002 68.594 1.00 53.66 ? 31   VAL B CB  1 
ATOM   2556 C CG1 . VAL B 1 31  ? -63.526  -28.207 68.066 1.00 54.28 ? 31   VAL B CG1 1 
ATOM   2557 C CG2 . VAL B 1 31  ? -64.456  -29.493 70.018 1.00 53.69 ? 31   VAL B CG2 1 
ATOM   2558 N N   . THR B 1 32  ? -66.445  -26.613 66.707 1.00 55.47 ? 32   THR B N   1 
ATOM   2559 C CA  . THR B 1 32  ? -66.811  -26.263 65.338 1.00 58.33 ? 32   THR B CA  1 
ATOM   2560 C C   . THR B 1 32  ? -65.708  -25.542 64.580 1.00 59.76 ? 32   THR B C   1 
ATOM   2561 O O   . THR B 1 32  ? -65.009  -24.697 65.131 1.00 60.75 ? 32   THR B O   1 
ATOM   2562 C CB  . THR B 1 32  ? -68.071  -25.373 65.312 1.00 57.25 ? 32   THR B CB  1 
ATOM   2563 O OG1 . THR B 1 32  ? -69.167  -26.087 65.893 1.00 56.65 ? 32   THR B OG1 1 
ATOM   2564 C CG2 . THR B 1 32  ? -68.426  -24.984 63.883 1.00 58.45 ? 32   THR B CG2 1 
ATOM   2565 N N   . LYS B 1 33  ? -65.557  -25.892 63.309 1.00 62.64 ? 33   LYS B N   1 
ATOM   2566 C CA  . LYS B 1 33  ? -64.561  -25.270 62.448 1.00 64.25 ? 33   LYS B CA  1 
ATOM   2567 C C   . LYS B 1 33  ? -65.220  -25.018 61.096 1.00 64.76 ? 33   LYS B C   1 
ATOM   2568 O O   . LYS B 1 33  ? -65.797  -25.928 60.496 1.00 64.37 ? 33   LYS B O   1 
ATOM   2569 C CB  . LYS B 1 33  ? -63.345  -26.187 62.292 1.00 64.56 ? 33   LYS B CB  1 
ATOM   2570 C CG  . LYS B 1 33  ? -62.708  -26.597 63.615 1.00 66.40 ? 33   LYS B CG  1 
ATOM   2571 C CD  . LYS B 1 33  ? -62.306  -25.379 64.443 1.00 67.53 ? 33   LYS B CD  1 
ATOM   2572 C CE  . LYS B 1 33  ? -61.702  -25.788 65.778 1.00 67.21 ? 33   LYS B CE  1 
ATOM   2573 N NZ  . LYS B 1 33  ? -61.396  -24.610 66.636 1.00 67.03 ? 33   LYS B NZ  1 
ATOM   2574 N N   . LYS B 1 34  ? -65.163  -23.776 60.630 1.00 66.15 ? 34   LYS B N   1 
ATOM   2575 C CA  . LYS B 1 34  ? -65.779  -23.434 59.354 1.00 67.77 ? 34   LYS B CA  1 
ATOM   2576 C C   . LYS B 1 34  ? -64.755  -22.920 58.347 1.00 68.52 ? 34   LYS B C   1 
ATOM   2577 O O   . LYS B 1 34  ? -63.991  -21.997 58.641 1.00 69.53 ? 34   LYS B O   1 
ATOM   2578 C CB  . LYS B 1 34  ? -66.849  -22.367 59.564 1.00 68.58 ? 34   LYS B CB  1 
ATOM   2579 C CG  . LYS B 1 34  ? -67.968  -22.417 58.555 1.00 69.49 ? 34   LYS B CG  1 
ATOM   2580 C CD  . LYS B 1 34  ? -69.038  -23.403 58.991 1.00 71.51 ? 34   LYS B CD  1 
ATOM   2581 C CE  . LYS B 1 34  ? -69.645  -22.978 60.321 1.00 72.28 ? 34   LYS B CE  1 
ATOM   2582 N NZ  . LYS B 1 34  ? -70.805  -23.821 60.717 1.00 72.86 ? 34   LYS B NZ  1 
ATOM   2583 N N   . PHE B 1 35  ? -64.748  -23.511 57.156 1.00 68.74 ? 35   PHE B N   1 
ATOM   2584 C CA  . PHE B 1 35  ? -63.817  -23.099 56.113 1.00 67.84 ? 35   PHE B CA  1 
ATOM   2585 C C   . PHE B 1 35  ? -64.345  -22.008 55.220 1.00 68.21 ? 35   PHE B C   1 
ATOM   2586 O O   . PHE B 1 35  ? -65.533  -21.691 55.218 1.00 67.41 ? 35   PHE B O   1 
ATOM   2587 C CB  . PHE B 1 35  ? -63.442  -24.261 55.211 1.00 68.27 ? 35   PHE B CB  1 
ATOM   2588 C CG  . PHE B 1 35  ? -62.788  -25.370 55.907 1.00 68.90 ? 35   PHE B CG  1 
ATOM   2589 C CD1 . PHE B 1 35  ? -63.477  -26.094 56.857 1.00 69.72 ? 35   PHE B CD1 1 
ATOM   2590 C CD2 . PHE B 1 35  ? -61.499  -25.747 55.560 1.00 69.60 ? 35   PHE B CD2 1 
ATOM   2591 C CE1 . PHE B 1 35  ? -62.905  -27.184 57.449 1.00 70.63 ? 35   PHE B CE1 1 
ATOM   2592 C CE2 . PHE B 1 35  ? -60.914  -26.846 56.153 1.00 69.92 ? 35   PHE B CE2 1 
ATOM   2593 C CZ  . PHE B 1 35  ? -61.620  -27.567 57.099 1.00 69.73 ? 35   PHE B CZ  1 
ATOM   2594 N N   . SER B 1 36  ? -63.413  -21.460 54.451 1.00 68.48 ? 36   SER B N   1 
ATOM   2595 C CA  . SER B 1 36  ? -63.635  -20.429 53.457 1.00 68.17 ? 36   SER B CA  1 
ATOM   2596 C C   . SER B 1 36  ? -64.962  -20.639 52.781 1.00 67.99 ? 36   SER B C   1 
ATOM   2597 O O   . SER B 1 36  ? -65.842  -19.787 52.812 1.00 68.38 ? 36   SER B O   1 
ATOM   2598 C CB  . SER B 1 36  ? -62.556  -20.544 52.399 1.00 69.20 ? 36   SER B CB  1 
ATOM   2599 O OG  . SER B 1 36  ? -62.367  -21.916 52.063 1.00 71.75 ? 36   SER B OG  1 
ATOM   2600 N N   . ASN B 1 37  ? -65.045  -21.796 52.138 1.00 66.09 ? 37   ASN B N   1 
ATOM   2601 C CA  . ASN B 1 37  ? -66.200  -22.249 51.385 1.00 64.51 ? 37   ASN B CA  1 
ATOM   2602 C C   . ASN B 1 37  ? -67.423  -22.530 52.262 1.00 63.36 ? 37   ASN B C   1 
ATOM   2603 O O   . ASN B 1 37  ? -68.450  -23.024 51.780 1.00 62.93 ? 37   ASN B O   1 
ATOM   2604 C CB  . ASN B 1 37  ? -65.812  -23.514 50.606 1.00 66.43 ? 37   ASN B CB  1 
ATOM   2605 C CG  . ASN B 1 37  ? -65.007  -24.510 51.458 1.00 67.86 ? 37   ASN B CG  1 
ATOM   2606 O OD1 . ASN B 1 37  ? -64.730  -24.254 52.636 1.00 69.04 ? 37   ASN B OD1 1 
ATOM   2607 N ND2 . ASN B 1 37  ? -64.629  -25.641 50.864 1.00 68.66 ? 37   ASN B ND2 1 
ATOM   2608 N N   . GLN B 1 38  ? -67.318  -22.194 53.542 1.00 60.98 ? 38   GLN B N   1 
ATOM   2609 C CA  . GLN B 1 38  ? -68.383  -22.442 54.499 1.00 59.31 ? 38   GLN B CA  1 
ATOM   2610 C C   . GLN B 1 38  ? -68.597  -23.926 54.696 1.00 57.08 ? 38   GLN B C   1 
ATOM   2611 O O   . GLN B 1 38  ? -69.670  -24.367 55.115 1.00 56.66 ? 38   GLN B O   1 
ATOM   2612 C CB  . GLN B 1 38  ? -69.698  -21.784 54.076 1.00 61.30 ? 38   GLN B CB  1 
ATOM   2613 C CG  . GLN B 1 38  ? -69.895  -20.375 54.580 1.00 64.17 ? 38   GLN B CG  1 
ATOM   2614 C CD  . GLN B 1 38  ? -69.574  -20.248 56.054 1.00 66.05 ? 38   GLN B CD  1 
ATOM   2615 O OE1 . GLN B 1 38  ? -68.407  -20.271 56.446 1.00 67.52 ? 38   GLN B OE1 1 
ATOM   2616 N NE2 . GLN B 1 38  ? -70.606  -20.134 56.882 1.00 65.21 ? 38   GLN B NE2 1 
ATOM   2617 N N   . GLU B 1 39  ? -67.573  -24.699 54.356 1.00 53.75 ? 39   GLU B N   1 
ATOM   2618 C CA  . GLU B 1 39  ? -67.616  -26.138 54.552 1.00 50.99 ? 39   GLU B CA  1 
ATOM   2619 C C   . GLU B 1 39  ? -67.552  -26.287 56.055 1.00 49.58 ? 39   GLU B C   1 
ATOM   2620 O O   . GLU B 1 39  ? -66.589  -25.859 56.692 1.00 46.45 ? 39   GLU B O   1 
ATOM   2621 C CB  . GLU B 1 39  ? -66.410  -26.806 53.901 1.00 50.26 ? 39   GLU B CB  1 
ATOM   2622 C CG  . GLU B 1 39  ? -66.195  -28.226 54.375 1.00 50.94 ? 39   GLU B CG  1 
ATOM   2623 C CD  . GLU B 1 39  ? -65.198  -28.989 53.521 1.00 52.56 ? 39   GLU B CD  1 
ATOM   2624 O OE1 . GLU B 1 39  ? -64.783  -30.096 53.937 1.00 53.31 ? 39   GLU B OE1 1 
ATOM   2625 O OE2 . GLU B 1 39  ? -64.835  -28.489 52.435 1.00 51.75 ? 39   GLU B OE2 1 
ATOM   2626 N N   . THR B 1 40  ? -68.581  -26.898 56.617 1.00 49.43 ? 40   THR B N   1 
ATOM   2627 C CA  . THR B 1 40  ? -68.658  -27.048 58.051 1.00 49.69 ? 40   THR B CA  1 
ATOM   2628 C C   . THR B 1 40  ? -68.121  -28.356 58.609 1.00 50.08 ? 40   THR B C   1 
ATOM   2629 O O   . THR B 1 40  ? -68.532  -29.444 58.196 1.00 48.34 ? 40   THR B O   1 
ATOM   2630 C CB  . THR B 1 40  ? -70.108  -26.891 58.508 1.00 50.33 ? 40   THR B CB  1 
ATOM   2631 O OG1 . THR B 1 40  ? -70.681  -25.740 57.880 1.00 52.03 ? 40   THR B OG1 1 
ATOM   2632 C CG2 . THR B 1 40  ? -70.183  -26.735 60.010 1.00 51.28 ? 40   THR B CG2 1 
ATOM   2633 N N   . CYS B 1 41  ? -67.180  -28.253 59.539 1.00 51.50 ? 41   CYS B N   1 
ATOM   2634 C CA  . CYS B 1 41  ? -66.664  -29.449 60.183 1.00 54.31 ? 41   CYS B CA  1 
ATOM   2635 C C   . CYS B 1 41  ? -66.999  -29.310 61.659 1.00 53.46 ? 41   CYS B C   1 
ATOM   2636 O O   . CYS B 1 41  ? -66.652  -28.322 62.310 1.00 54.21 ? 41   CYS B O   1 
ATOM   2637 C CB  . CYS B 1 41  ? -65.155  -29.613 59.952 1.00 57.72 ? 41   CYS B CB  1 
ATOM   2638 S SG  . CYS B 1 41  ? -64.230  -28.096 59.929 1.00 69.63 ? 41   CYS B SG  1 
ATOM   2639 N N   . VAL B 1 42  ? -67.713  -30.302 62.167 1.00 52.85 ? 42   VAL B N   1 
ATOM   2640 C CA  . VAL B 1 42  ? -68.148  -30.323 63.549 1.00 51.40 ? 42   VAL B CA  1 
ATOM   2641 C C   . VAL B 1 42  ? -67.506  -31.463 64.319 1.00 50.99 ? 42   VAL B C   1 
ATOM   2642 O O   . VAL B 1 42  ? -67.052  -32.444 63.737 1.00 52.41 ? 42   VAL B O   1 
ATOM   2643 C CB  . VAL B 1 42  ? -69.684  -30.456 63.606 1.00 52.18 ? 42   VAL B CB  1 
ATOM   2644 C CG1 . VAL B 1 42  ? -70.129  -30.960 64.948 1.00 52.28 ? 42   VAL B CG1 1 
ATOM   2645 C CG2 . VAL B 1 42  ? -70.320  -29.111 63.321 1.00 54.43 ? 42   VAL B CG2 1 
ATOM   2646 N N   . GLU B 1 43  ? -67.461  -31.322 65.636 1.00 50.02 ? 43   GLU B N   1 
ATOM   2647 C CA  . GLU B 1 43  ? -66.898  -32.353 66.486 1.00 49.31 ? 43   GLU B CA  1 
ATOM   2648 C C   . GLU B 1 43  ? -67.600  -32.362 67.833 1.00 47.52 ? 43   GLU B C   1 
ATOM   2649 O O   . GLU B 1 43  ? -67.467  -31.422 68.607 1.00 47.47 ? 43   GLU B O   1 
ATOM   2650 C CB  . GLU B 1 43  ? -65.415  -32.110 66.705 1.00 52.30 ? 43   GLU B CB  1 
ATOM   2651 C CG  . GLU B 1 43  ? -64.773  -33.144 67.605 1.00 56.48 ? 43   GLU B CG  1 
ATOM   2652 C CD  . GLU B 1 43  ? -63.321  -32.829 67.907 1.00 60.82 ? 43   GLU B CD  1 
ATOM   2653 O OE1 . GLU B 1 43  ? -62.570  -32.524 66.955 1.00 61.72 ? 43   GLU B OE1 1 
ATOM   2654 O OE2 . GLU B 1 43  ? -62.927  -32.896 69.092 1.00 62.40 ? 43   GLU B OE2 1 
ATOM   2655 N N   . ILE B 1 44  ? -68.342  -33.425 68.121 1.00 44.83 ? 44   ILE B N   1 
ATOM   2656 C CA  . ILE B 1 44  ? -69.054  -33.523 69.393 1.00 40.77 ? 44   ILE B CA  1 
ATOM   2657 C C   . ILE B 1 44  ? -68.034  -33.631 70.538 1.00 40.43 ? 44   ILE B C   1 
ATOM   2658 O O   . ILE B 1 44  ? -67.311  -34.622 70.660 1.00 40.14 ? 44   ILE B O   1 
ATOM   2659 C CB  . ILE B 1 44  ? -70.011  -34.745 69.390 1.00 39.14 ? 44   ILE B CB  1 
ATOM   2660 C CG1 . ILE B 1 44  ? -70.934  -34.684 68.165 1.00 36.85 ? 44   ILE B CG1 1 
ATOM   2661 C CG2 . ILE B 1 44  ? -70.862  -34.752 70.652 1.00 36.82 ? 44   ILE B CG2 1 
ATOM   2662 C CD1 . ILE B 1 44  ? -71.739  -33.388 68.048 1.00 35.46 ? 44   ILE B CD1 1 
ATOM   2663 N N   . GLY B 1 45  ? -67.987  -32.603 71.380 1.00 38.10 ? 45   GLY B N   1 
ATOM   2664 C CA  . GLY B 1 45  ? -67.031  -32.573 72.470 1.00 37.12 ? 45   GLY B CA  1 
ATOM   2665 C C   . GLY B 1 45  ? -67.273  -33.426 73.701 1.00 37.23 ? 45   GLY B C   1 
ATOM   2666 O O   . GLY B 1 45  ? -66.602  -33.240 74.710 1.00 38.58 ? 45   GLY B O   1 
ATOM   2667 N N   . GLU B 1 46  ? -68.223  -34.350 73.638 1.00 36.33 ? 46   GLU B N   1 
ATOM   2668 C CA  . GLU B 1 46  ? -68.494  -35.233 74.764 1.00 34.31 ? 46   GLU B CA  1 
ATOM   2669 C C   . GLU B 1 46  ? -69.232  -36.449 74.251 1.00 31.98 ? 46   GLU B C   1 
ATOM   2670 O O   . GLU B 1 46  ? -69.875  -36.394 73.209 1.00 31.01 ? 46   GLU B O   1 
ATOM   2671 C CB  . GLU B 1 46  ? -69.338  -34.524 75.834 1.00 34.42 ? 46   GLU B CB  1 
ATOM   2672 C CG  . GLU B 1 46  ? -70.440  -33.643 75.274 1.00 37.33 ? 46   GLU B CG  1 
ATOM   2673 C CD  . GLU B 1 46  ? -71.251  -32.930 76.351 1.00 39.49 ? 46   GLU B CD  1 
ATOM   2674 O OE1 . GLU B 1 46  ? -72.192  -33.544 76.901 1.00 38.73 ? 46   GLU B OE1 1 
ATOM   2675 O OE2 . GLU B 1 46  ? -70.942  -31.751 76.641 1.00 38.03 ? 46   GLU B OE2 1 
ATOM   2676 N N   . SER B 1 47  ? -69.131  -37.547 74.983 1.00 30.36 ? 47   SER B N   1 
ATOM   2677 C CA  . SER B 1 47  ? -69.807  -38.773 74.602 1.00 28.83 ? 47   SER B CA  1 
ATOM   2678 C C   . SER B 1 47  ? -71.323  -38.607 74.619 1.00 30.08 ? 47   SER B C   1 
ATOM   2679 O O   . SER B 1 47  ? -71.867  -37.943 75.499 1.00 27.70 ? 47   SER B O   1 
ATOM   2680 C CB  . SER B 1 47  ? -69.430  -39.894 75.566 1.00 26.51 ? 47   SER B CB  1 
ATOM   2681 O OG  . SER B 1 47  ? -70.197  -41.057 75.306 1.00 27.79 ? 47   SER B OG  1 
ATOM   2682 N N   . VAL B 1 48  ? -72.001  -39.198 73.639 1.00 28.28 ? 48   VAL B N   1 
ATOM   2683 C CA  . VAL B 1 48  ? -73.456  -39.155 73.598 1.00 26.46 ? 48   VAL B CA  1 
ATOM   2684 C C   . VAL B 1 48  ? -73.935  -40.600 73.519 1.00 27.56 ? 48   VAL B C   1 
ATOM   2685 O O   . VAL B 1 48  ? -75.115  -40.876 73.290 1.00 26.89 ? 48   VAL B O   1 
ATOM   2686 C CB  . VAL B 1 48  ? -73.987  -38.356 72.377 1.00 27.18 ? 48   VAL B CB  1 
ATOM   2687 C CG1 . VAL B 1 48  ? -73.630  -36.887 72.527 1.00 26.20 ? 48   VAL B CG1 1 
ATOM   2688 C CG2 . VAL B 1 48  ? -73.418  -38.922 71.078 1.00 24.21 ? 48   VAL B CG2 1 
ATOM   2689 N N   . ARG B 1 49  ? -73.001  -41.525 73.729 1.00 28.06 ? 49   ARG B N   1 
ATOM   2690 C CA  . ARG B 1 49  ? -73.301  -42.952 73.675 1.00 28.06 ? 49   ARG B CA  1 
ATOM   2691 C C   . ARG B 1 49  ? -74.448  -43.328 74.620 1.00 29.58 ? 49   ARG B C   1 
ATOM   2692 O O   . ARG B 1 49  ? -74.400  -43.047 75.816 1.00 27.26 ? 49   ARG B O   1 
ATOM   2693 C CB  . ARG B 1 49  ? -72.043  -43.761 74.016 1.00 26.73 ? 49   ARG B CB  1 
ATOM   2694 C CG  . ARG B 1 49  ? -72.164  -45.261 73.745 1.00 26.08 ? 49   ARG B CG  1 
ATOM   2695 C CD  . ARG B 1 49  ? -70.839  -45.986 73.984 1.00 24.40 ? 49   ARG B CD  1 
ATOM   2696 N NE  . ARG B 1 49  ? -69.757  -45.547 73.096 1.00 22.72 ? 49   ARG B NE  1 
ATOM   2697 C CZ  . ARG B 1 49  ? -69.497  -46.064 71.894 1.00 24.95 ? 49   ARG B CZ  1 
ATOM   2698 N NH1 . ARG B 1 49  ? -70.238  -47.047 71.398 1.00 26.74 ? 49   ARG B NH1 1 
ATOM   2699 N NH2 . ARG B 1 49  ? -68.462  -45.628 71.197 1.00 25.34 ? 49   ARG B NH2 1 
ATOM   2700 N N   . GLY B 1 50  ? -75.478  -43.959 74.063 1.00 29.25 ? 50   GLY B N   1 
ATOM   2701 C CA  . GLY B 1 50  ? -76.627  -44.371 74.849 1.00 30.37 ? 50   GLY B CA  1 
ATOM   2702 C C   . GLY B 1 50  ? -77.483  -43.243 75.399 1.00 32.68 ? 50   GLY B C   1 
ATOM   2703 O O   . GLY B 1 50  ? -78.340  -43.472 76.249 1.00 34.44 ? 50   GLY B O   1 
ATOM   2704 N N   . GLU B 1 51  ? -77.284  -42.026 74.907 1.00 33.62 ? 51   GLU B N   1 
ATOM   2705 C CA  . GLU B 1 51  ? -78.045  -40.891 75.409 1.00 32.31 ? 51   GLU B CA  1 
ATOM   2706 C C   . GLU B 1 51  ? -79.122  -40.334 74.468 1.00 31.96 ? 51   GLU B C   1 
ATOM   2707 O O   . GLU B 1 51  ? -79.040  -40.479 73.247 1.00 29.42 ? 51   GLU B O   1 
ATOM   2708 C CB  . GLU B 1 51  ? -77.068  -39.790 75.805 1.00 35.10 ? 51   GLU B CB  1 
ATOM   2709 C CG  . GLU B 1 51  ? -76.142  -40.231 76.918 1.00 43.33 ? 51   GLU B CG  1 
ATOM   2710 C CD  . GLU B 1 51  ? -75.335  -39.099 77.507 1.00 49.22 ? 51   GLU B CD  1 
ATOM   2711 O OE1 . GLU B 1 51  ? -74.665  -39.327 78.539 1.00 54.36 ? 51   GLU B OE1 1 
ATOM   2712 O OE2 . GLU B 1 51  ? -75.364  -37.984 76.944 1.00 53.35 ? 51   GLU B OE2 1 
ATOM   2713 N N   . ASP B 1 52  ? -80.133  -39.699 75.063 1.00 30.61 ? 52   ASP B N   1 
ATOM   2714 C CA  . ASP B 1 52  ? -81.247  -39.094 74.334 1.00 29.09 ? 52   ASP B CA  1 
ATOM   2715 C C   . ASP B 1 52  ? -80.793  -37.698 73.899 1.00 27.41 ? 52   ASP B C   1 
ATOM   2716 O O   . ASP B 1 52  ? -80.719  -36.766 74.701 1.00 24.75 ? 52   ASP B O   1 
ATOM   2717 C CB  . ASP B 1 52  ? -82.474  -39.015 75.252 1.00 30.29 ? 52   ASP B CB  1 
ATOM   2718 C CG  . ASP B 1 52  ? -83.758  -38.745 74.494 1.00 32.66 ? 52   ASP B CG  1 
ATOM   2719 O OD1 . ASP B 1 52  ? -83.788  -38.981 73.263 1.00 34.26 ? 52   ASP B OD1 1 
ATOM   2720 O OD2 . ASP B 1 52  ? -84.746  -38.310 75.129 1.00 31.78 ? 52   ASP B OD2 1 
ATOM   2721 N N   . VAL B 1 53  ? -80.490  -37.562 72.614 1.00 25.56 ? 53   VAL B N   1 
ATOM   2722 C CA  . VAL B 1 53  ? -79.974  -36.310 72.080 1.00 23.74 ? 53   VAL B CA  1 
ATOM   2723 C C   . VAL B 1 53  ? -80.973  -35.382 71.385 1.00 25.45 ? 53   VAL B C   1 
ATOM   2724 O O   . VAL B 1 53  ? -81.822  -35.819 70.605 1.00 26.32 ? 53   VAL B O   1 
ATOM   2725 C CB  . VAL B 1 53  ? -78.814  -36.611 71.106 1.00 23.55 ? 53   VAL B CB  1 
ATOM   2726 C CG1 . VAL B 1 53  ? -78.253  -35.313 70.502 1.00 21.33 ? 53   VAL B CG1 1 
ATOM   2727 C CG2 . VAL B 1 53  ? -77.740  -37.390 71.838 1.00 21.54 ? 53   VAL B CG2 1 
ATOM   2728 N N   . TYR B 1 54  ? -80.857  -34.091 71.673 1.00 23.57 ? 54   TYR B N   1 
ATOM   2729 C CA  . TYR B 1 54  ? -81.715  -33.101 71.044 1.00 25.00 ? 54   TYR B CA  1 
ATOM   2730 C C   . TYR B 1 54  ? -80.811  -32.033 70.456 1.00 26.33 ? 54   TYR B C   1 
ATOM   2731 O O   . TYR B 1 54  ? -80.001  -31.437 71.174 1.00 27.99 ? 54   TYR B O   1 
ATOM   2732 C CB  . TYR B 1 54  ? -82.677  -32.484 72.070 1.00 25.62 ? 54   TYR B CB  1 
ATOM   2733 C CG  . TYR B 1 54  ? -83.635  -33.494 72.657 1.00 26.09 ? 54   TYR B CG  1 
ATOM   2734 C CD1 . TYR B 1 54  ? -83.196  -34.443 73.589 1.00 28.91 ? 54   TYR B CD1 1 
ATOM   2735 C CD2 . TYR B 1 54  ? -84.963  -33.553 72.230 1.00 23.86 ? 54   TYR B CD2 1 
ATOM   2736 C CE1 . TYR B 1 54  ? -84.055  -35.430 74.072 1.00 26.58 ? 54   TYR B CE1 1 
ATOM   2737 C CE2 . TYR B 1 54  ? -85.828  -34.526 72.706 1.00 24.92 ? 54   TYR B CE2 1 
ATOM   2738 C CZ  . TYR B 1 54  ? -85.370  -35.466 73.625 1.00 27.47 ? 54   TYR B CZ  1 
ATOM   2739 O OH  . TYR B 1 54  ? -86.217  -36.454 74.075 1.00 24.51 ? 54   TYR B OH  1 
ATOM   2740 N N   . ILE B 1 55  ? -80.923  -31.812 69.149 1.00 27.18 ? 55   ILE B N   1 
ATOM   2741 C CA  . ILE B 1 55  ? -80.122  -30.791 68.482 1.00 27.85 ? 55   ILE B CA  1 
ATOM   2742 C C   . ILE B 1 55  ? -81.036  -29.662 68.017 1.00 29.13 ? 55   ILE B C   1 
ATOM   2743 O O   . ILE B 1 55  ? -81.944  -29.878 67.223 1.00 29.38 ? 55   ILE B O   1 
ATOM   2744 C CB  . ILE B 1 55  ? -79.363  -31.364 67.257 1.00 29.46 ? 55   ILE B CB  1 
ATOM   2745 C CG1 . ILE B 1 55  ? -78.443  -32.500 67.700 1.00 28.78 ? 55   ILE B CG1 1 
ATOM   2746 C CG2 . ILE B 1 55  ? -78.525  -30.264 66.597 1.00 27.35 ? 55   ILE B CG2 1 
ATOM   2747 C CD1 . ILE B 1 55  ? -77.918  -33.327 66.547 1.00 33.38 ? 55   ILE B CD1 1 
ATOM   2748 N N   . VAL B 1 56  ? -80.794  -28.461 68.529 1.00 31.67 ? 56   VAL B N   1 
ATOM   2749 C CA  . VAL B 1 56  ? -81.590  -27.295 68.174 1.00 35.99 ? 56   VAL B CA  1 
ATOM   2750 C C   . VAL B 1 56  ? -80.901  -26.530 67.051 1.00 39.24 ? 56   VAL B C   1 
ATOM   2751 O O   . VAL B 1 56  ? -79.742  -26.138 67.188 1.00 38.49 ? 56   VAL B O   1 
ATOM   2752 C CB  . VAL B 1 56  ? -81.765  -26.332 69.380 1.00 34.70 ? 56   VAL B CB  1 
ATOM   2753 C CG1 . VAL B 1 56  ? -82.737  -25.224 69.019 1.00 34.39 ? 56   VAL B CG1 1 
ATOM   2754 C CG2 . VAL B 1 56  ? -82.259  -27.091 70.599 1.00 35.47 ? 56   VAL B CG2 1 
ATOM   2755 N N   . GLN B 1 57  ? -81.619  -26.314 65.952 1.00 43.13 ? 57   GLN B N   1 
ATOM   2756 C CA  . GLN B 1 57  ? -81.081  -25.598 64.795 1.00 48.49 ? 57   GLN B CA  1 
ATOM   2757 C C   . GLN B 1 57  ? -80.847  -24.118 65.076 1.00 52.14 ? 57   GLN B C   1 
ATOM   2758 O O   . GLN B 1 57  ? -81.628  -23.472 65.777 1.00 53.05 ? 57   GLN B O   1 
ATOM   2759 C CB  . GLN B 1 57  ? -82.024  -25.737 63.597 1.00 50.02 ? 57   GLN B CB  1 
ATOM   2760 C CG  . GLN B 1 57  ? -81.479  -25.113 62.315 1.00 51.95 ? 57   GLN B CG  1 
ATOM   2761 C CD  . GLN B 1 57  ? -82.423  -25.267 61.137 1.00 54.33 ? 57   GLN B CD  1 
ATOM   2762 O OE1 . GLN B 1 57  ? -83.508  -24.674 61.102 1.00 53.83 ? 57   GLN B OE1 1 
ATOM   2763 N NE2 . GLN B 1 57  ? -82.017  -26.073 60.163 1.00 55.90 ? 57   GLN B NE2 1 
ATOM   2764 N N   . SER B 1 58  ? -79.775  -23.584 64.502 1.00 56.77 ? 58   SER B N   1 
ATOM   2765 C CA  . SER B 1 58  ? -79.402  -22.182 64.687 1.00 61.33 ? 58   SER B CA  1 
ATOM   2766 C C   . SER B 1 58  ? -80.402  -21.181 64.156 1.00 62.97 ? 58   SER B C   1 
ATOM   2767 O O   . SER B 1 58  ? -81.553  -21.500 63.873 1.00 65.50 ? 58   SER B O   1 
ATOM   2768 C CB  . SER B 1 58  ? -78.064  -21.886 64.008 1.00 61.72 ? 58   SER B CB  1 
ATOM   2769 O OG  . SER B 1 58  ? -77.030  -22.736 64.462 1.00 62.37 ? 58   SER B OG  1 
ATOM   2770 N N   . GLY B 1 59  ? -79.913  -19.954 64.017 1.00 65.86 ? 59   GLY B N   1 
ATOM   2771 C CA  . GLY B 1 59  ? -80.699  -18.846 63.507 1.00 68.20 ? 59   GLY B CA  1 
ATOM   2772 C C   . GLY B 1 59  ? -79.766  -17.946 62.723 1.00 70.03 ? 59   GLY B C   1 
ATOM   2773 O O   . GLY B 1 59  ? -80.098  -16.802 62.396 1.00 71.59 ? 59   GLY B O   1 
ATOM   2774 N N   . CYS B 1 60  ? -78.578  -18.489 62.453 1.00 70.46 ? 60   CYS B N   1 
ATOM   2775 C CA  . CYS B 1 60  ? -77.505  -17.837 61.706 1.00 69.57 ? 60   CYS B CA  1 
ATOM   2776 C C   . CYS B 1 60  ? -77.971  -16.996 60.526 1.00 67.55 ? 60   CYS B C   1 
ATOM   2777 O O   . CYS B 1 60  ? -77.308  -16.027 60.145 1.00 68.23 ? 60   CYS B O   1 
ATOM   2778 C CB  . CYS B 1 60  ? -76.518  -18.893 61.209 1.00 70.71 ? 60   CYS B CB  1 
ATOM   2779 S SG  . CYS B 1 60  ? -76.001  -18.688 59.504 1.00 76.33 ? 60   CYS B SG  1 
ATOM   2780 N N   . GLY B 1 61  ? -79.114  -17.359 59.950 1.00 64.03 ? 61   GLY B N   1 
ATOM   2781 C CA  . GLY B 1 61  ? -79.635  -16.618 58.812 1.00 58.51 ? 61   GLY B CA  1 
ATOM   2782 C C   . GLY B 1 61  ? -79.366  -17.275 57.469 1.00 54.55 ? 61   GLY B C   1 
ATOM   2783 O O   . GLY B 1 61  ? -80.220  -17.235 56.579 1.00 54.83 ? 61   GLY B O   1 
ATOM   2784 N N   . GLU B 1 62  ? -78.179  -17.859 57.302 1.00 47.90 ? 62   GLU B N   1 
ATOM   2785 C CA  . GLU B 1 62  ? -77.861  -18.548 56.054 1.00 41.80 ? 62   GLU B CA  1 
ATOM   2786 C C   . GLU B 1 62  ? -78.486  -19.935 56.175 1.00 38.07 ? 62   GLU B C   1 
ATOM   2787 O O   . GLU B 1 62  ? -77.926  -20.835 56.793 1.00 35.18 ? 62   GLU B O   1 
ATOM   2788 C CB  . GLU B 1 62  ? -76.352  -18.657 55.867 1.00 40.50 ? 62   GLU B CB  1 
ATOM   2789 C CG  . GLU B 1 62  ? -75.871  -18.458 54.431 1.00 40.91 ? 62   GLU B CG  1 
ATOM   2790 C CD  . GLU B 1 62  ? -76.281  -19.579 53.471 1.00 43.44 ? 62   GLU B CD  1 
ATOM   2791 O OE1 . GLU B 1 62  ? -76.766  -20.641 53.925 1.00 41.50 ? 62   GLU B OE1 1 
ATOM   2792 O OE2 . GLU B 1 62  ? -76.103  -19.396 52.247 1.00 41.83 ? 62   GLU B OE2 1 
ATOM   2793 N N   . ILE B 1 63  ? -79.658  -20.097 55.579 1.00 35.35 ? 63   ILE B N   1 
ATOM   2794 C CA  . ILE B 1 63  ? -80.390  -21.344 55.683 1.00 34.27 ? 63   ILE B CA  1 
ATOM   2795 C C   . ILE B 1 63  ? -79.669  -22.608 55.240 1.00 33.39 ? 63   ILE B C   1 
ATOM   2796 O O   . ILE B 1 63  ? -79.792  -23.645 55.888 1.00 32.20 ? 63   ILE B O   1 
ATOM   2797 C CB  . ILE B 1 63  ? -81.731  -21.256 54.951 1.00 35.69 ? 63   ILE B CB  1 
ATOM   2798 C CG1 . ILE B 1 63  ? -82.677  -22.309 55.522 1.00 37.64 ? 63   ILE B CG1 1 
ATOM   2799 C CG2 . ILE B 1 63  ? -81.522  -21.395 53.466 1.00 37.39 ? 63   ILE B CG2 1 
ATOM   2800 C CD1 . ILE B 1 63  ? -83.708  -22.794 54.543 1.00 38.00 ? 63   ILE B CD1 1 
ATOM   2801 N N   . ASN B 1 64  ? -78.919  -22.551 54.148 1.00 30.63 ? 64   ASN B N   1 
ATOM   2802 C CA  . ASN B 1 64  ? -78.236  -23.754 53.716 1.00 29.07 ? 64   ASN B CA  1 
ATOM   2803 C C   . ASN B 1 64  ? -77.099  -24.129 54.662 1.00 28.21 ? 64   ASN B C   1 
ATOM   2804 O O   . ASN B 1 64  ? -76.874  -25.312 54.912 1.00 26.61 ? 64   ASN B O   1 
ATOM   2805 C CB  . ASN B 1 64  ? -77.749  -23.590 52.276 1.00 29.51 ? 64   ASN B CB  1 
ATOM   2806 C CG  . ASN B 1 64  ? -78.902  -23.422 51.301 1.00 27.59 ? 64   ASN B CG  1 
ATOM   2807 O OD1 . ASN B 1 64  ? -78.787  -22.712 50.308 1.00 31.36 ? 64   ASN B OD1 1 
ATOM   2808 N ND2 . ASN B 1 64  ? -80.026  -24.085 51.587 1.00 23.92 ? 64   ASN B ND2 1 
ATOM   2809 N N   . ASP B 1 65  ? -76.393  -23.137 55.204 1.00 26.88 ? 65   ASP B N   1 
ATOM   2810 C CA  . ASP B 1 65  ? -75.308  -23.434 56.141 1.00 28.14 ? 65   ASP B CA  1 
ATOM   2811 C C   . ASP B 1 65  ? -75.894  -24.076 57.400 1.00 27.06 ? 65   ASP B C   1 
ATOM   2812 O O   . ASP B 1 65  ? -75.365  -25.069 57.913 1.00 27.55 ? 65   ASP B O   1 
ATOM   2813 C CB  . ASP B 1 65  ? -74.548  -22.162 56.536 1.00 28.52 ? 65   ASP B CB  1 
ATOM   2814 C CG  . ASP B 1 65  ? -73.796  -21.553 55.381 1.00 30.60 ? 65   ASP B CG  1 
ATOM   2815 O OD1 . ASP B 1 65  ? -73.554  -22.263 54.383 1.00 30.58 ? 65   ASP B OD1 1 
ATOM   2816 O OD2 . ASP B 1 65  ? -73.430  -20.364 55.482 1.00 32.56 ? 65   ASP B OD2 1 
ATOM   2817 N N   . ASN B 1 66  ? -76.983  -23.497 57.897 1.00 27.85 ? 66   ASN B N   1 
ATOM   2818 C CA  . ASN B 1 66  ? -77.647  -24.016 59.094 1.00 29.87 ? 66   ASN B CA  1 
ATOM   2819 C C   . ASN B 1 66  ? -78.160  -25.433 58.873 1.00 29.18 ? 66   ASN B C   1 
ATOM   2820 O O   . ASN B 1 66  ? -77.972  -26.305 59.721 1.00 31.98 ? 66   ASN B O   1 
ATOM   2821 C CB  . ASN B 1 66  ? -78.818  -23.115 59.500 1.00 29.85 ? 66   ASN B CB  1 
ATOM   2822 C CG  . ASN B 1 66  ? -78.361  -21.740 59.979 1.00 35.76 ? 66   ASN B CG  1 
ATOM   2823 O OD1 . ASN B 1 66  ? -77.321  -21.608 60.637 1.00 33.61 ? 66   ASN B OD1 1 
ATOM   2824 N ND2 . ASN B 1 66  ? -79.149  -20.710 59.665 1.00 35.14 ? 66   ASN B ND2 1 
ATOM   2825 N N   . LEU B 1 67  ? -78.795  -25.671 57.731 1.00 26.42 ? 67   LEU B N   1 
ATOM   2826 C CA  . LEU B 1 67  ? -79.326  -26.998 57.454 1.00 26.00 ? 67   LEU B CA  1 
ATOM   2827 C C   . LEU B 1 67  ? -78.229  -28.055 57.414 1.00 26.83 ? 67   LEU B C   1 
ATOM   2828 O O   . LEU B 1 67  ? -78.384  -29.133 57.998 1.00 26.24 ? 67   LEU B O   1 
ATOM   2829 C CB  . LEU B 1 67  ? -80.104  -27.010 56.139 1.00 23.90 ? 67   LEU B CB  1 
ATOM   2830 C CG  . LEU B 1 67  ? -80.640  -28.382 55.700 1.00 23.88 ? 67   LEU B CG  1 
ATOM   2831 C CD1 . LEU B 1 67  ? -81.613  -28.933 56.733 1.00 20.08 ? 67   LEU B CD1 1 
ATOM   2832 C CD2 . LEU B 1 67  ? -81.316  -28.244 54.352 1.00 23.76 ? 67   LEU B CD2 1 
ATOM   2833 N N   . MET B 1 68  ? -77.121  -27.749 56.736 1.00 25.49 ? 68   MET B N   1 
ATOM   2834 C CA  . MET B 1 68  ? -76.021  -28.696 56.641 1.00 25.56 ? 68   MET B CA  1 
ATOM   2835 C C   . MET B 1 68  ? -75.426  -28.945 58.011 1.00 25.31 ? 68   MET B C   1 
ATOM   2836 O O   . MET B 1 68  ? -75.196  -30.096 58.401 1.00 25.67 ? 68   MET B O   1 
ATOM   2837 C CB  . MET B 1 68  ? -74.936  -28.182 55.689 1.00 28.23 ? 68   MET B CB  1 
ATOM   2838 C CG  . MET B 1 68  ? -75.302  -28.295 54.233 1.00 30.90 ? 68   MET B CG  1 
ATOM   2839 S SD  . MET B 1 68  ? -75.830  -29.977 53.794 1.00 38.55 ? 68   MET B SD  1 
ATOM   2840 C CE  . MET B 1 68  ? -74.372  -30.972 54.371 1.00 28.40 ? 68   MET B CE  1 
ATOM   2841 N N   . GLU B 1 69  ? -75.185  -27.865 58.750 1.00 24.79 ? 69   GLU B N   1 
ATOM   2842 C CA  . GLU B 1 69  ? -74.627  -27.992 60.085 1.00 25.72 ? 69   GLU B CA  1 
ATOM   2843 C C   . GLU B 1 69  ? -75.515  -28.930 60.902 1.00 24.50 ? 69   GLU B C   1 
ATOM   2844 O O   . GLU B 1 69  ? -75.022  -29.824 61.578 1.00 26.33 ? 69   GLU B O   1 
ATOM   2845 C CB  . GLU B 1 69  ? -74.536  -26.620 60.765 1.00 27.56 ? 69   GLU B CB  1 
ATOM   2846 C CG  . GLU B 1 69  ? -73.896  -26.668 62.136 1.00 36.70 ? 69   GLU B CG  1 
ATOM   2847 C CD  . GLU B 1 69  ? -73.739  -25.292 62.761 1.00 42.77 ? 69   GLU B CD  1 
ATOM   2848 O OE1 . GLU B 1 69  ? -74.764  -24.601 62.979 1.00 46.90 ? 69   GLU B OE1 1 
ATOM   2849 O OE2 . GLU B 1 69  ? -72.586  -24.898 63.031 1.00 46.27 ? 69   GLU B OE2 1 
ATOM   2850 N N   . LEU B 1 70  ? -76.825  -28.728 60.827 1.00 20.94 ? 70   LEU B N   1 
ATOM   2851 C CA  . LEU B 1 70  ? -77.773  -29.582 61.545 1.00 20.63 ? 70   LEU B CA  1 
ATOM   2852 C C   . LEU B 1 70  ? -77.617  -31.046 61.134 1.00 22.26 ? 70   LEU B C   1 
ATOM   2853 O O   . LEU B 1 70  ? -77.465  -31.928 61.983 1.00 22.07 ? 70   LEU B O   1 
ATOM   2854 C CB  . LEU B 1 70  ? -79.205  -29.121 61.258 1.00 17.93 ? 70   LEU B CB  1 
ATOM   2855 C CG  . LEU B 1 70  ? -80.377  -29.951 61.785 1.00 19.38 ? 70   LEU B CG  1 
ATOM   2856 C CD1 . LEU B 1 70  ? -80.311  -30.091 63.299 1.00 17.72 ? 70   LEU B CD1 1 
ATOM   2857 C CD2 . LEU B 1 70  ? -81.672  -29.263 61.379 1.00 18.55 ? 70   LEU B CD2 1 
ATOM   2858 N N   . LEU B 1 71  ? -77.633  -31.305 59.827 1.00 22.33 ? 71   LEU B N   1 
ATOM   2859 C CA  . LEU B 1 71  ? -77.514  -32.669 59.330 1.00 23.25 ? 71   LEU B CA  1 
ATOM   2860 C C   . LEU B 1 71  ? -76.209  -33.304 59.750 1.00 24.99 ? 71   LEU B C   1 
ATOM   2861 O O   . LEU B 1 71  ? -76.172  -34.478 60.116 1.00 25.44 ? 71   LEU B O   1 
ATOM   2862 C CB  . LEU B 1 71  ? -77.624  -32.689 57.810 1.00 23.78 ? 71   LEU B CB  1 
ATOM   2863 C CG  . LEU B 1 71  ? -78.970  -32.199 57.283 1.00 27.07 ? 71   LEU B CG  1 
ATOM   2864 C CD1 . LEU B 1 71  ? -78.852  -31.852 55.816 1.00 26.20 ? 71   LEU B CD1 1 
ATOM   2865 C CD2 . LEU B 1 71  ? -80.023  -33.272 57.523 1.00 27.08 ? 71   LEU B CD2 1 
ATOM   2866 N N   . ILE B 1 72  ? -75.135  -32.519 59.698 1.00 26.74 ? 72   ILE B N   1 
ATOM   2867 C CA  . ILE B 1 72  ? -73.814  -33.010 60.064 1.00 26.66 ? 72   ILE B CA  1 
ATOM   2868 C C   . ILE B 1 72  ? -73.760  -33.412 61.536 1.00 27.96 ? 72   ILE B C   1 
ATOM   2869 O O   . ILE B 1 72  ? -73.192  -34.462 61.884 1.00 26.11 ? 72   ILE B O   1 
ATOM   2870 C CB  . ILE B 1 72  ? -72.737  -31.946 59.750 1.00 26.91 ? 72   ILE B CB  1 
ATOM   2871 C CG1 . ILE B 1 72  ? -72.562  -31.844 58.232 1.00 24.96 ? 72   ILE B CG1 1 
ATOM   2872 C CG2 . ILE B 1 72  ? -71.432  -32.296 60.433 1.00 25.09 ? 72   ILE B CG2 1 
ATOM   2873 C CD1 . ILE B 1 72  ? -71.719  -30.685 57.784 1.00 29.15 ? 72   ILE B CD1 1 
ATOM   2874 N N   . MET B 1 73  ? -74.359  -32.585 62.392 1.00 26.29 ? 73   MET B N   1 
ATOM   2875 C CA  . MET B 1 73  ? -74.402  -32.877 63.824 1.00 27.72 ? 73   MET B CA  1 
ATOM   2876 C C   . MET B 1 73  ? -75.259  -34.110 64.088 1.00 25.01 ? 73   MET B C   1 
ATOM   2877 O O   . MET B 1 73  ? -74.928  -34.935 64.944 1.00 25.84 ? 73   MET B O   1 
ATOM   2878 C CB  . MET B 1 73  ? -74.956  -31.689 64.610 1.00 27.75 ? 73   MET B CB  1 
ATOM   2879 C CG  . MET B 1 73  ? -74.001  -30.527 64.700 1.00 32.23 ? 73   MET B CG  1 
ATOM   2880 S SD  . MET B 1 73  ? -74.641  -29.261 65.807 1.00 39.33 ? 73   MET B SD  1 
ATOM   2881 C CE  . MET B 1 73  ? -75.463  -28.226 64.642 1.00 37.50 ? 73   MET B CE  1 
ATOM   2882 N N   . ILE B 1 74  ? -76.366  -34.238 63.368 1.00 25.87 ? 74   ILE B N   1 
ATOM   2883 C CA  . ILE B 1 74  ? -77.215  -35.420 63.534 1.00 25.83 ? 74   ILE B CA  1 
ATOM   2884 C C   . ILE B 1 74  ? -76.374  -36.650 63.167 1.00 25.74 ? 74   ILE B C   1 
ATOM   2885 O O   . ILE B 1 74  ? -76.351  -37.636 63.896 1.00 24.54 ? 74   ILE B O   1 
ATOM   2886 C CB  . ILE B 1 74  ? -78.483  -35.339 62.637 1.00 24.88 ? 74   ILE B CB  1 
ATOM   2887 C CG1 . ILE B 1 74  ? -79.419  -34.251 63.181 1.00 28.05 ? 74   ILE B CG1 1 
ATOM   2888 C CG2 . ILE B 1 74  ? -79.224  -36.685 62.623 1.00 23.56 ? 74   ILE B CG2 1 
ATOM   2889 C CD1 . ILE B 1 74  ? -80.600  -33.896 62.277 1.00 27.69 ? 74   ILE B CD1 1 
ATOM   2890 N N   . ASN B 1 75  ? -75.655  -36.564 62.050 1.00 26.46 ? 75   ASN B N   1 
ATOM   2891 C CA  . ASN B 1 75  ? -74.802  -37.655 61.574 1.00 26.35 ? 75   ASN B CA  1 
ATOM   2892 C C   . ASN B 1 75  ? -73.777  -38.085 62.618 1.00 25.96 ? 75   ASN B C   1 
ATOM   2893 O O   . ASN B 1 75  ? -73.626  -39.265 62.918 1.00 26.23 ? 75   ASN B O   1 
ATOM   2894 C CB  . ASN B 1 75  ? -74.057  -37.222 60.311 1.00 29.49 ? 75   ASN B CB  1 
ATOM   2895 C CG  . ASN B 1 75  ? -73.092  -38.287 59.803 1.00 29.72 ? 75   ASN B CG  1 
ATOM   2896 O OD1 . ASN B 1 75  ? -73.511  -39.335 59.317 1.00 31.61 ? 75   ASN B OD1 1 
ATOM   2897 N ND2 . ASN B 1 75  ? -71.794  -38.021 59.922 1.00 28.46 ? 75   ASN B ND2 1 
ATOM   2898 N N   . ALA B 1 76  ? -73.075  -37.098 63.158 1.00 28.58 ? 76   ALA B N   1 
ATOM   2899 C CA  . ALA B 1 76  ? -72.042  -37.304 64.154 1.00 25.51 ? 76   ALA B CA  1 
ATOM   2900 C C   . ALA B 1 76  ? -72.558  -38.007 65.395 1.00 25.45 ? 76   ALA B C   1 
ATOM   2901 O O   . ALA B 1 76  ? -71.922  -38.938 65.893 1.00 24.76 ? 76   ALA B O   1 
ATOM   2902 C CB  . ALA B 1 76  ? -71.431  -35.967 64.532 1.00 27.29 ? 76   ALA B CB  1 
ATOM   2903 N N   . CYS B 1 77  ? -73.700  -37.557 65.903 1.00 25.13 ? 77   CYS B N   1 
ATOM   2904 C CA  . CYS B 1 77  ? -74.288  -38.164 67.095 1.00 25.39 ? 77   CYS B CA  1 
ATOM   2905 C C   . CYS B 1 77  ? -74.742  -39.593 66.820 1.00 25.60 ? 77   CYS B C   1 
ATOM   2906 O O   . CYS B 1 77  ? -74.540  -40.485 67.643 1.00 27.01 ? 77   CYS B O   1 
ATOM   2907 C CB  . CYS B 1 77  ? -75.461  -37.317 67.608 1.00 25.26 ? 77   CYS B CB  1 
ATOM   2908 S SG  . CYS B 1 77  ? -74.943  -35.713 68.313 1.00 23.20 ? 77   CYS B SG  1 
ATOM   2909 N N   . LYS B 1 78  ? -75.345  -39.815 65.661 1.00 26.03 ? 78   LYS B N   1 
ATOM   2910 C CA  . LYS B 1 78  ? -75.798  -41.150 65.296 1.00 27.70 ? 78   LYS B CA  1 
ATOM   2911 C C   . LYS B 1 78  ? -74.657  -42.151 65.203 1.00 28.94 ? 78   LYS B C   1 
ATOM   2912 O O   . LYS B 1 78  ? -74.761  -43.251 65.735 1.00 28.93 ? 78   LYS B O   1 
ATOM   2913 C CB  . LYS B 1 78  ? -76.544  -41.114 63.962 1.00 30.89 ? 78   LYS B CB  1 
ATOM   2914 C CG  . LYS B 1 78  ? -78.045  -40.936 64.101 1.00 36.53 ? 78   LYS B CG  1 
ATOM   2915 C CD  . LYS B 1 78  ? -78.690  -42.198 64.660 1.00 39.93 ? 78   LYS B CD  1 
ATOM   2916 C CE  . LYS B 1 78  ? -80.199  -42.071 64.726 1.00 41.18 ? 78   LYS B CE  1 
ATOM   2917 N NZ  . LYS B 1 78  ? -80.868  -43.390 64.781 1.00 43.58 ? 78   LYS B NZ  1 
ATOM   2918 N N   . ILE B 1 79  ? -73.561  -41.779 64.539 1.00 30.87 ? 79   ILE B N   1 
ATOM   2919 C CA  . ILE B 1 79  ? -72.450  -42.720 64.405 1.00 31.46 ? 79   ILE B CA  1 
ATOM   2920 C C   . ILE B 1 79  ? -71.637  -42.809 65.693 1.00 31.79 ? 79   ILE B C   1 
ATOM   2921 O O   . ILE B 1 79  ? -70.812  -43.704 65.863 1.00 32.60 ? 79   ILE B O   1 
ATOM   2922 C CB  . ILE B 1 79  ? -71.530  -42.386 63.202 1.00 31.50 ? 79   ILE B CB  1 
ATOM   2923 C CG1 . ILE B 1 79  ? -70.865  -41.028 63.373 1.00 33.86 ? 79   ILE B CG1 1 
ATOM   2924 C CG2 . ILE B 1 79  ? -72.332  -42.389 61.921 1.00 31.98 ? 79   ILE B CG2 1 
ATOM   2925 C CD1 . ILE B 1 79  ? -69.824  -40.759 62.298 1.00 31.40 ? 79   ILE B CD1 1 
ATOM   2926 N N   . ALA B 1 80  ? -71.903  -41.872 66.599 1.00 30.18 ? 80   ALA B N   1 
ATOM   2927 C CA  . ALA B 1 80  ? -71.270  -41.834 67.918 1.00 29.21 ? 80   ALA B CA  1 
ATOM   2928 C C   . ALA B 1 80  ? -72.141  -42.645 68.895 1.00 29.94 ? 80   ALA B C   1 
ATOM   2929 O O   . ALA B 1 80  ? -72.038  -42.509 70.122 1.00 29.20 ? 80   ALA B O   1 
ATOM   2930 C CB  . ALA B 1 80  ? -71.133  -40.392 68.405 1.00 24.81 ? 80   ALA B CB  1 
ATOM   2931 N N   . SER B 1 81  ? -73.004  -43.484 68.326 1.00 27.66 ? 81   SER B N   1 
ATOM   2932 C CA  . SER B 1 81  ? -73.902  -44.350 69.082 1.00 28.34 ? 81   SER B CA  1 
ATOM   2933 C C   . SER B 1 81  ? -74.958  -43.702 69.978 1.00 29.58 ? 81   SER B C   1 
ATOM   2934 O O   . SER B 1 81  ? -75.315  -44.275 71.009 1.00 29.95 ? 81   SER B O   1 
ATOM   2935 C CB  . SER B 1 81  ? -73.108  -45.355 69.935 1.00 27.47 ? 81   SER B CB  1 
ATOM   2936 O OG  . SER B 1 81  ? -72.555  -46.387 69.150 1.00 23.95 ? 81   SER B OG  1 
ATOM   2937 N N   . ALA B 1 82  ? -75.480  -42.533 69.633 1.00 28.51 ? 82   ALA B N   1 
ATOM   2938 C CA  . ALA B 1 82  ? -76.509  -41.977 70.511 1.00 28.55 ? 82   ALA B CA  1 
ATOM   2939 C C   . ALA B 1 82  ? -77.725  -42.917 70.528 1.00 28.31 ? 82   ALA B C   1 
ATOM   2940 O O   . ALA B 1 82  ? -78.045  -43.569 69.533 1.00 26.85 ? 82   ALA B O   1 
ATOM   2941 C CB  . ALA B 1 82  ? -76.943  -40.575 70.043 1.00 25.47 ? 82   ALA B CB  1 
ATOM   2942 N N   . SER B 1 83  ? -78.400  -42.976 71.666 1.00 29.33 ? 83   SER B N   1 
ATOM   2943 C CA  . SER B 1 83  ? -79.583  -43.807 71.792 1.00 31.28 ? 83   SER B CA  1 
ATOM   2944 C C   . SER B 1 83  ? -80.691  -43.300 70.864 1.00 31.38 ? 83   SER B C   1 
ATOM   2945 O O   . SER B 1 83  ? -81.385  -44.089 70.210 1.00 30.78 ? 83   SER B O   1 
ATOM   2946 C CB  . SER B 1 83  ? -80.079  -43.803 73.238 1.00 32.80 ? 83   SER B CB  1 
ATOM   2947 O OG  . SER B 1 83  ? -81.223  -44.620 73.361 1.00 37.59 ? 83   SER B OG  1 
ATOM   2948 N N   . ARG B 1 84  ? -80.860  -41.982 70.810 1.00 28.97 ? 84   ARG B N   1 
ATOM   2949 C CA  . ARG B 1 84  ? -81.874  -41.382 69.947 1.00 29.12 ? 84   ARG B CA  1 
ATOM   2950 C C   . ARG B 1 84  ? -81.480  -39.953 69.630 1.00 27.90 ? 84   ARG B C   1 
ATOM   2951 O O   . ARG B 1 84  ? -80.885  -39.269 70.456 1.00 29.30 ? 84   ARG B O   1 
ATOM   2952 C CB  . ARG B 1 84  ? -83.256  -41.410 70.626 1.00 28.48 ? 84   ARG B CB  1 
ATOM   2953 C CG  . ARG B 1 84  ? -84.380  -40.766 69.802 1.00 31.15 ? 84   ARG B CG  1 
ATOM   2954 C CD  . ARG B 1 84  ? -85.782  -41.002 70.410 1.00 32.46 ? 84   ARG B CD  1 
ATOM   2955 N NE  . ARG B 1 84  ? -85.925  -40.377 71.722 1.00 34.99 ? 84   ARG B NE  1 
ATOM   2956 C CZ  . ARG B 1 84  ? -86.978  -40.516 72.523 1.00 37.10 ? 84   ARG B CZ  1 
ATOM   2957 N NH1 . ARG B 1 84  ? -88.011  -41.268 72.161 1.00 37.80 ? 84   ARG B NH1 1 
ATOM   2958 N NH2 . ARG B 1 84  ? -86.994  -39.898 73.694 1.00 36.29 ? 84   ARG B NH2 1 
ATOM   2959 N N   . VAL B 1 85  ? -81.787  -39.505 68.420 1.00 28.14 ? 85   VAL B N   1 
ATOM   2960 C CA  . VAL B 1 85  ? -81.466  -38.139 68.035 1.00 27.13 ? 85   VAL B CA  1 
ATOM   2961 C C   . VAL B 1 85  ? -82.723  -37.445 67.541 1.00 25.90 ? 85   VAL B C   1 
ATOM   2962 O O   . VAL B 1 85  ? -83.383  -37.930 66.628 1.00 25.04 ? 85   VAL B O   1 
ATOM   2963 C CB  . VAL B 1 85  ? -80.398  -38.096 66.920 1.00 28.09 ? 85   VAL B CB  1 
ATOM   2964 C CG1 . VAL B 1 85  ? -80.096  -36.650 66.564 1.00 22.79 ? 85   VAL B CG1 1 
ATOM   2965 C CG2 . VAL B 1 85  ? -79.132  -38.818 67.377 1.00 21.97 ? 85   VAL B CG2 1 
ATOM   2966 N N   . THR B 1 86  ? -83.040  -36.307 68.151 1.00 24.17 ? 86   THR B N   1 
ATOM   2967 C CA  . THR B 1 86  ? -84.223  -35.537 67.800 1.00 23.58 ? 86   THR B CA  1 
ATOM   2968 C C   . THR B 1 86  ? -83.835  -34.189 67.242 1.00 24.84 ? 86   THR B C   1 
ATOM   2969 O O   . THR B 1 86  ? -83.062  -33.455 67.859 1.00 24.96 ? 86   THR B O   1 
ATOM   2970 C CB  . THR B 1 86  ? -85.110  -35.270 69.047 1.00 24.55 ? 86   THR B CB  1 
ATOM   2971 O OG1 . THR B 1 86  ? -85.603  -36.508 69.562 1.00 24.10 ? 86   THR B OG1 1 
ATOM   2972 C CG2 . THR B 1 86  ? -86.276  -34.348 68.700 1.00 21.49 ? 86   THR B CG2 1 
ATOM   2973 N N   . ALA B 1 87  ? -84.368  -33.847 66.075 1.00 25.35 ? 87   ALA B N   1 
ATOM   2974 C CA  . ALA B 1 87  ? -84.069  -32.549 65.511 1.00 22.92 ? 87   ALA B CA  1 
ATOM   2975 C C   . ALA B 1 87  ? -85.128  -31.590 65.999 1.00 24.72 ? 87   ALA B C   1 
ATOM   2976 O O   . ALA B 1 87  ? -86.313  -31.792 65.766 1.00 21.20 ? 87   ALA B O   1 
ATOM   2977 C CB  . ALA B 1 87  ? -84.068  -32.602 63.992 1.00 25.92 ? 87   ALA B CB  1 
ATOM   2978 N N   . VAL B 1 88  ? -84.700  -30.564 66.729 1.00 26.87 ? 88   VAL B N   1 
ATOM   2979 C CA  . VAL B 1 88  ? -85.625  -29.549 67.217 1.00 25.34 ? 88   VAL B CA  1 
ATOM   2980 C C   . VAL B 1 88  ? -85.459  -28.412 66.213 1.00 25.38 ? 88   VAL B C   1 
ATOM   2981 O O   . VAL B 1 88  ? -84.440  -27.725 66.203 1.00 25.77 ? 88   VAL B O   1 
ATOM   2982 C CB  . VAL B 1 88  ? -85.251  -29.092 68.641 1.00 25.34 ? 88   VAL B CB  1 
ATOM   2983 C CG1 . VAL B 1 88  ? -86.245  -28.030 69.134 1.00 20.21 ? 88   VAL B CG1 1 
ATOM   2984 C CG2 . VAL B 1 88  ? -85.261  -30.310 69.583 1.00 22.61 ? 88   VAL B CG2 1 
ATOM   2985 N N   . ILE B 1 89  ? -86.454  -28.242 65.351 1.00 25.23 ? 89   ILE B N   1 
ATOM   2986 C CA  . ILE B 1 89  ? -86.393  -27.230 64.303 1.00 25.74 ? 89   ILE B CA  1 
ATOM   2987 C C   . ILE B 1 89  ? -87.561  -26.265 64.419 1.00 26.83 ? 89   ILE B C   1 
ATOM   2988 O O   . ILE B 1 89  ? -88.600  -26.463 63.791 1.00 26.76 ? 89   ILE B O   1 
ATOM   2989 C CB  . ILE B 1 89  ? -86.462  -27.886 62.900 1.00 27.82 ? 89   ILE B CB  1 
ATOM   2990 C CG1 . ILE B 1 89  ? -85.486  -29.061 62.817 1.00 24.78 ? 89   ILE B CG1 1 
ATOM   2991 C CG2 . ILE B 1 89  ? -86.185  -26.834 61.822 1.00 27.10 ? 89   ILE B CG2 1 
ATOM   2992 C CD1 . ILE B 1 89  ? -85.573  -29.840 61.497 1.00 26.77 ? 89   ILE B CD1 1 
ATOM   2993 N N   . PRO B 1 90  ? -87.393  -25.195 65.206 1.00 28.17 ? 90   PRO B N   1 
ATOM   2994 C CA  . PRO B 1 90  ? -88.426  -24.182 65.424 1.00 30.51 ? 90   PRO B CA  1 
ATOM   2995 C C   . PRO B 1 90  ? -89.123  -23.783 64.140 1.00 29.45 ? 90   PRO B C   1 
ATOM   2996 O O   . PRO B 1 90  ? -90.344  -23.852 64.045 1.00 30.75 ? 90   PRO B O   1 
ATOM   2997 C CB  . PRO B 1 90  ? -87.643  -23.031 66.058 1.00 30.25 ? 90   PRO B CB  1 
ATOM   2998 C CG  . PRO B 1 90  ? -86.620  -23.765 66.861 1.00 30.13 ? 90   PRO B CG  1 
ATOM   2999 C CD  . PRO B 1 90  ? -86.134  -24.789 65.854 1.00 29.98 ? 90   PRO B CD  1 
ATOM   3000 N N   . CYS B 1 91  ? -88.333  -23.383 63.155 1.00 27.32 ? 91   CYS B N   1 
ATOM   3001 C CA  . CYS B 1 91  ? -88.862  -22.964 61.867 1.00 27.58 ? 91   CYS B CA  1 
ATOM   3002 C C   . CYS B 1 91  ? -88.326  -23.896 60.792 1.00 26.20 ? 91   CYS B C   1 
ATOM   3003 O O   . CYS B 1 91  ? -87.151  -23.831 60.432 1.00 24.09 ? 91   CYS B O   1 
ATOM   3004 C CB  . CYS B 1 91  ? -88.442  -21.520 61.576 1.00 28.06 ? 91   CYS B CB  1 
ATOM   3005 S SG  . CYS B 1 91  ? -89.196  -20.837 60.087 1.00 31.08 ? 91   CYS B SG  1 
ATOM   3006 N N   . PHE B 1 92  ? -89.199  -24.751 60.270 1.00 25.27 ? 92   PHE B N   1 
ATOM   3007 C CA  . PHE B 1 92  ? -88.798  -25.735 59.276 1.00 23.94 ? 92   PHE B CA  1 
ATOM   3008 C C   . PHE B 1 92  ? -88.325  -25.142 57.948 1.00 25.19 ? 92   PHE B C   1 
ATOM   3009 O O   . PHE B 1 92  ? -89.050  -24.401 57.289 1.00 25.82 ? 92   PHE B O   1 
ATOM   3010 C CB  . PHE B 1 92  ? -89.950  -26.709 59.034 1.00 24.34 ? 92   PHE B CB  1 
ATOM   3011 C CG  . PHE B 1 92  ? -89.530  -28.003 58.420 1.00 22.47 ? 92   PHE B CG  1 
ATOM   3012 C CD1 . PHE B 1 92  ? -89.044  -29.045 59.213 1.00 22.83 ? 92   PHE B CD1 1 
ATOM   3013 C CD2 . PHE B 1 92  ? -89.613  -28.185 57.041 1.00 21.96 ? 92   PHE B CD2 1 
ATOM   3014 C CE1 . PHE B 1 92  ? -88.648  -30.253 58.630 1.00 24.57 ? 92   PHE B CE1 1 
ATOM   3015 C CE2 . PHE B 1 92  ? -89.221  -29.388 56.447 1.00 22.53 ? 92   PHE B CE2 1 
ATOM   3016 C CZ  . PHE B 1 92  ? -88.738  -30.423 57.243 1.00 23.71 ? 92   PHE B CZ  1 
ATOM   3017 N N   . PRO B 1 93  ? -87.094  -25.486 57.534 1.00 26.56 ? 93   PRO B N   1 
ATOM   3018 C CA  . PRO B 1 93  ? -86.457  -25.024 56.290 1.00 26.55 ? 93   PRO B CA  1 
ATOM   3019 C C   . PRO B 1 93  ? -87.217  -25.453 55.042 1.00 27.62 ? 93   PRO B C   1 
ATOM   3020 O O   . PRO B 1 93  ? -87.675  -26.600 54.949 1.00 28.25 ? 93   PRO B O   1 
ATOM   3021 C CB  . PRO B 1 93  ? -85.076  -25.690 56.326 1.00 28.61 ? 93   PRO B CB  1 
ATOM   3022 C CG  . PRO B 1 93  ? -84.869  -26.072 57.756 1.00 29.72 ? 93   PRO B CG  1 
ATOM   3023 C CD  . PRO B 1 93  ? -86.236  -26.461 58.229 1.00 26.50 ? 93   PRO B CD  1 
ATOM   3024 N N   . TYR B 1 94  ? -87.328  -24.541 54.081 1.00 27.24 ? 94   TYR B N   1 
ATOM   3025 C CA  . TYR B 1 94  ? -88.006  -24.808 52.814 1.00 25.55 ? 94   TYR B CA  1 
ATOM   3026 C C   . TYR B 1 94  ? -89.444  -25.287 52.965 1.00 27.32 ? 94   TYR B C   1 
ATOM   3027 O O   . TYR B 1 94  ? -90.009  -25.864 52.031 1.00 25.63 ? 94   TYR B O   1 
ATOM   3028 C CB  . TYR B 1 94  ? -87.222  -25.842 51.995 1.00 27.60 ? 94   TYR B CB  1 
ATOM   3029 C CG  . TYR B 1 94  ? -85.878  -25.352 51.489 1.00 27.90 ? 94   TYR B CG  1 
ATOM   3030 C CD1 . TYR B 1 94  ? -84.753  -25.354 52.313 1.00 26.97 ? 94   TYR B CD1 1 
ATOM   3031 C CD2 . TYR B 1 94  ? -85.740  -24.862 50.192 1.00 27.72 ? 94   TYR B CD2 1 
ATOM   3032 C CE1 . TYR B 1 94  ? -83.522  -24.879 51.856 1.00 25.68 ? 94   TYR B CE1 1 
ATOM   3033 C CE2 . TYR B 1 94  ? -84.514  -24.377 49.728 1.00 27.75 ? 94   TYR B CE2 1 
ATOM   3034 C CZ  . TYR B 1 94  ? -83.416  -24.389 50.565 1.00 26.31 ? 94   TYR B CZ  1 
ATOM   3035 O OH  . TYR B 1 94  ? -82.223  -23.876 50.123 1.00 27.27 ? 94   TYR B OH  1 
ATOM   3036 N N   . ALA B 1 95  ? -90.036  -25.046 54.134 1.00 27.99 ? 95   ALA B N   1 
ATOM   3037 C CA  . ALA B 1 95  ? -91.420  -25.450 54.392 1.00 30.50 ? 95   ALA B CA  1 
ATOM   3038 C C   . ALA B 1 95  ? -92.389  -24.957 53.317 1.00 32.60 ? 95   ALA B C   1 
ATOM   3039 O O   . ALA B 1 95  ? -93.312  -25.676 52.932 1.00 34.96 ? 95   ALA B O   1 
ATOM   3040 C CB  . ALA B 1 95  ? -91.866  -24.948 55.756 1.00 29.43 ? 95   ALA B CB  1 
ATOM   3041 N N   . ARG B 1 96  ? -92.188  -23.736 52.828 1.00 34.27 ? 96   ARG B N   1 
ATOM   3042 C CA  . ARG B 1 96  ? -93.067  -23.194 51.794 1.00 36.15 ? 96   ARG B CA  1 
ATOM   3043 C C   . ARG B 1 96  ? -92.972  -23.976 50.488 1.00 35.99 ? 96   ARG B C   1 
ATOM   3044 O O   . ARG B 1 96  ? -93.921  -24.017 49.717 1.00 37.69 ? 96   ARG B O   1 
ATOM   3045 C CB  . ARG B 1 96  ? -92.744  -21.726 51.529 1.00 36.28 ? 96   ARG B CB  1 
ATOM   3046 C CG  . ARG B 1 96  ? -93.278  -20.777 52.583 1.00 41.25 ? 96   ARG B CG  1 
ATOM   3047 C CD  . ARG B 1 96  ? -92.639  -19.409 52.455 1.00 43.83 ? 96   ARG B CD  1 
ATOM   3048 N NE  . ARG B 1 96  ? -91.191  -19.483 52.621 1.00 47.50 ? 96   ARG B NE  1 
ATOM   3049 C CZ  . ARG B 1 96  ? -90.365  -18.456 52.456 1.00 49.49 ? 96   ARG B CZ  1 
ATOM   3050 N NH1 . ARG B 1 96  ? -90.840  -17.263 52.117 1.00 48.72 ? 96   ARG B NH1 1 
ATOM   3051 N NH2 . ARG B 1 96  ? -89.062  -18.624 52.630 1.00 51.55 ? 96   ARG B NH2 1 
ATOM   3052 N N   . GLN B 1 97  ? -91.824  -24.586 50.226 1.00 35.73 ? 97   GLN B N   1 
ATOM   3053 C CA  . GLN B 1 97  ? -91.673  -25.369 49.002 1.00 36.54 ? 97   GLN B CA  1 
ATOM   3054 C C   . GLN B 1 97  ? -92.169  -26.792 49.286 1.00 35.87 ? 97   GLN B C   1 
ATOM   3055 O O   . GLN B 1 97  ? -91.395  -27.746 49.342 1.00 33.55 ? 97   GLN B O   1 
ATOM   3056 C CB  . GLN B 1 97  ? -90.210  -25.338 48.545 1.00 35.13 ? 97   GLN B CB  1 
ATOM   3057 C CG  . GLN B 1 97  ? -89.771  -23.936 48.102 1.00 37.18 ? 97   GLN B CG  1 
ATOM   3058 C CD  . GLN B 1 97  ? -88.329  -23.867 47.620 1.00 39.32 ? 97   GLN B CD  1 
ATOM   3059 O OE1 . GLN B 1 97  ? -87.881  -24.699 46.825 1.00 41.45 ? 97   GLN B OE1 1 
ATOM   3060 N NE2 . GLN B 1 97  ? -87.598  -22.865 48.092 1.00 39.84 ? 97   GLN B NE2 1 
ATOM   3061 N N   . ASP B 1 98  ? -93.485  -26.910 49.463 1.00 37.75 ? 98   ASP B N   1 
ATOM   3062 C CA  . ASP B 1 98  ? -94.110  -28.186 49.793 1.00 39.17 ? 98   ASP B CA  1 
ATOM   3063 C C   . ASP B 1 98  ? -95.075  -28.773 48.759 1.00 40.31 ? 98   ASP B C   1 
ATOM   3064 O O   . ASP B 1 98  ? -95.728  -29.779 49.033 1.00 41.78 ? 98   ASP B O   1 
ATOM   3065 C CB  . ASP B 1 98  ? -94.812  -28.060 51.151 1.00 37.81 ? 98   ASP B CB  1 
ATOM   3066 C CG  . ASP B 1 98  ? -96.046  -27.167 51.101 1.00 38.56 ? 98   ASP B CG  1 
ATOM   3067 O OD1 . ASP B 1 98  ? -96.086  -26.219 50.291 1.00 38.33 ? 98   ASP B OD1 1 
ATOM   3068 O OD2 . ASP B 1 98  ? -96.978  -27.406 51.890 1.00 38.35 ? 98   ASP B OD2 1 
ATOM   3069 N N   . LYS B 1 99  ? -95.157  -28.153 47.581 1.00 41.95 ? 99   LYS B N   1 
ATOM   3070 C CA  . LYS B 1 99  ? -96.030  -28.619 46.492 1.00 42.86 ? 99   LYS B CA  1 
ATOM   3071 C C   . LYS B 1 99  ? -95.414  -28.204 45.146 1.00 43.61 ? 99   LYS B C   1 
ATOM   3072 O O   . LYS B 1 99  ? -94.526  -27.356 45.106 1.00 42.15 ? 99   LYS B O   1 
ATOM   3073 C CB  . LYS B 1 99  ? -97.428  -27.999 46.620 1.00 43.74 ? 99   LYS B CB  1 
ATOM   3074 C CG  . LYS B 1 99  ? -97.438  -26.479 46.472 1.00 47.16 ? 99   LYS B CG  1 
ATOM   3075 C CD  . LYS B 1 99  ? -98.849  -25.885 46.458 1.00 49.42 ? 99   LYS B CD  1 
ATOM   3076 C CE  . LYS B 1 99  ? -99.517  -25.960 47.822 1.00 52.46 ? 99   LYS B CE  1 
ATOM   3077 N NZ  . LYS B 1 99  ? -100.877 -25.329 47.827 1.00 54.34 ? 99   LYS B NZ  1 
ATOM   3078 N N   . LYS B 1 100 ? -95.878  -28.800 44.050 1.00 44.21 ? 100  LYS B N   1 
ATOM   3079 C CA  . LYS B 1 100 ? -95.366  -28.447 42.726 1.00 46.69 ? 100  LYS B CA  1 
ATOM   3080 C C   . LYS B 1 100 ? -96.116  -27.225 42.202 1.00 49.73 ? 100  LYS B C   1 
ATOM   3081 O O   . LYS B 1 100 ? -95.552  -26.391 41.488 1.00 50.73 ? 100  LYS B O   1 
ATOM   3082 C CB  . LYS B 1 100 ? -95.563  -29.591 41.730 1.00 45.27 ? 100  LYS B CB  1 
ATOM   3083 C CG  . LYS B 1 100 ? -94.680  -30.799 41.931 1.00 44.63 ? 100  LYS B CG  1 
ATOM   3084 C CD  . LYS B 1 100 ? -94.925  -31.804 40.817 1.00 39.80 ? 100  LYS B CD  1 
ATOM   3085 C CE  . LYS B 1 100 ? -94.108  -33.061 41.015 1.00 42.11 ? 100  LYS B CE  1 
ATOM   3086 N NZ  . LYS B 1 100 ? -94.470  -34.133 40.029 1.00 41.29 ? 100  LYS B NZ  1 
ATOM   3087 N N   . ASP B 1 101 ? -97.399  -27.144 42.551 1.00 52.63 ? 101  ASP B N   1 
ATOM   3088 C CA  . ASP B 1 101 ? -98.283  -26.049 42.145 1.00 56.19 ? 101  ASP B CA  1 
ATOM   3089 C C   . ASP B 1 101 ? -98.219  -25.780 40.643 1.00 56.53 ? 101  ASP B C   1 
ATOM   3090 O O   . ASP B 1 101 ? -97.851  -24.680 40.218 1.00 56.46 ? 101  ASP B O   1 
ATOM   3091 C CB  . ASP B 1 101 ? -97.944  -24.763 42.918 1.00 59.00 ? 101  ASP B CB  1 
ATOM   3092 C CG  . ASP B 1 101 ? -99.142  -23.829 43.047 1.00 62.37 ? 101  ASP B CG  1 
ATOM   3093 O OD1 . ASP B 1 101 ? -99.116  -22.729 42.455 1.00 63.95 ? 101  ASP B OD1 1 
ATOM   3094 O OD2 . ASP B 1 101 ? -100.111 -24.206 43.746 1.00 65.12 ? 101  ASP B OD2 1 
ATOM   3095 N N   . LYS B 1 102 ? -98.581  -26.794 39.855 1.00 56.46 ? 102  LYS B N   1 
ATOM   3096 C CA  . LYS B 1 102 ? -98.589  -26.731 38.389 1.00 56.55 ? 102  LYS B CA  1 
ATOM   3097 C C   . LYS B 1 102 ? -97.263  -26.351 37.721 1.00 55.88 ? 102  LYS B C   1 
ATOM   3098 O O   . LYS B 1 102 ? -97.257  -25.654 36.703 1.00 56.49 ? 102  LYS B O   1 
ATOM   3099 C CB  . LYS B 1 102 ? -99.681  -25.777 37.909 1.00 57.50 ? 102  LYS B CB  1 
ATOM   3100 C CG  . LYS B 1 102 ? -101.097 -26.229 38.220 1.00 60.52 ? 102  LYS B CG  1 
ATOM   3101 C CD  . LYS B 1 102 ? -102.102 -25.164 37.800 1.00 62.91 ? 102  LYS B CD  1 
ATOM   3102 C CE  . LYS B 1 102 ? -103.518 -25.718 37.720 1.00 64.41 ? 102  LYS B CE  1 
ATOM   3103 N NZ  . LYS B 1 102 ? -104.023 -26.306 38.990 1.00 65.12 ? 102  LYS B NZ  1 
ATOM   3104 N N   . SER B 1 103 ? -96.144  -26.800 38.281 1.00 53.31 ? 103  SER B N   1 
ATOM   3105 C CA  . SER B 1 103 ? -94.847  -26.492 37.686 1.00 50.75 ? 103  SER B CA  1 
ATOM   3106 C C   . SER B 1 103 ? -93.859  -27.639 37.886 1.00 49.37 ? 103  SER B C   1 
ATOM   3107 O O   . SER B 1 103 ? -94.065  -28.498 38.743 1.00 47.35 ? 103  SER B O   1 
ATOM   3108 C CB  . SER B 1 103 ? -94.273  -25.222 38.308 1.00 52.57 ? 103  SER B CB  1 
ATOM   3109 O OG  . SER B 1 103 ? -95.238  -24.186 38.318 1.00 55.46 ? 103  SER B OG  1 
ATOM   3110 N N   . ARG B 1 104 ? -92.797  -27.657 37.083 1.00 47.94 ? 104  ARG B N   1 
ATOM   3111 C CA  . ARG B 1 104 ? -91.773  -28.687 37.199 1.00 46.49 ? 104  ARG B CA  1 
ATOM   3112 C C   . ARG B 1 104 ? -90.773  -28.232 38.254 1.00 46.84 ? 104  ARG B C   1 
ATOM   3113 O O   . ARG B 1 104 ? -89.580  -28.030 37.983 1.00 47.74 ? 104  ARG B O   1 
ATOM   3114 C CB  . ARG B 1 104 ? -91.061  -28.916 35.863 1.00 46.41 ? 104  ARG B CB  1 
ATOM   3115 C CG  . ARG B 1 104 ? -91.832  -29.819 34.910 1.00 49.02 ? 104  ARG B CG  1 
ATOM   3116 C CD  . ARG B 1 104 ? -91.003  -30.168 33.683 1.00 48.03 ? 104  ARG B CD  1 
ATOM   3117 N NE  . ARG B 1 104 ? -90.851  -29.023 32.791 1.00 50.35 ? 104  ARG B NE  1 
ATOM   3118 C CZ  . ARG B 1 104 ? -91.803  -28.561 31.988 1.00 46.51 ? 104  ARG B CZ  1 
ATOM   3119 N NH1 . ARG B 1 104 ? -92.989  -29.144 31.952 1.00 46.84 ? 104  ARG B NH1 1 
ATOM   3120 N NH2 . ARG B 1 104 ? -91.567  -27.506 31.223 1.00 50.17 ? 104  ARG B NH2 1 
ATOM   3121 N N   . ALA B 1 105 ? -91.284  -28.055 39.467 1.00 44.10 ? 105  ALA B N   1 
ATOM   3122 C CA  . ALA B 1 105 ? -90.471  -27.612 40.582 1.00 42.89 ? 105  ALA B CA  1 
ATOM   3123 C C   . ALA B 1 105 ? -90.202  -28.748 41.559 1.00 41.08 ? 105  ALA B C   1 
ATOM   3124 O O   . ALA B 1 105 ? -90.817  -29.817 41.497 1.00 40.91 ? 105  ALA B O   1 
ATOM   3125 C CB  . ALA B 1 105 ? -91.157  -26.456 41.297 1.00 43.75 ? 105  ALA B CB  1 
ATOM   3126 N N   . PRO B 1 106 ? -89.252  -28.534 42.474 1.00 38.44 ? 106  PRO B N   1 
ATOM   3127 C CA  . PRO B 1 106 ? -88.942  -29.570 43.454 1.00 38.23 ? 106  PRO B CA  1 
ATOM   3128 C C   . PRO B 1 106 ? -89.867  -29.398 44.659 1.00 35.29 ? 106  PRO B C   1 
ATOM   3129 O O   . PRO B 1 106 ? -90.410  -28.317 44.885 1.00 35.43 ? 106  PRO B O   1 
ATOM   3130 C CB  . PRO B 1 106 ? -87.493  -29.272 43.814 1.00 37.81 ? 106  PRO B CB  1 
ATOM   3131 C CG  . PRO B 1 106 ? -87.475  -27.783 43.796 1.00 38.30 ? 106  PRO B CG  1 
ATOM   3132 C CD  . PRO B 1 106 ? -88.244  -27.460 42.525 1.00 39.03 ? 106  PRO B CD  1 
ATOM   3133 N N   . ILE B 1 107 ? -90.102  -30.466 45.406 1.00 34.09 ? 107  ILE B N   1 
ATOM   3134 C CA  . ILE B 1 107 ? -90.895  -30.339 46.630 1.00 33.15 ? 107  ILE B CA  1 
ATOM   3135 C C   . ILE B 1 107 ? -89.767  -30.410 47.658 1.00 31.54 ? 107  ILE B C   1 
ATOM   3136 O O   . ILE B 1 107 ? -89.564  -31.436 48.312 1.00 32.09 ? 107  ILE B O   1 
ATOM   3137 C CB  . ILE B 1 107 ? -91.872  -31.503 46.817 1.00 34.26 ? 107  ILE B CB  1 
ATOM   3138 C CG1 . ILE B 1 107 ? -92.866  -31.553 45.652 1.00 33.67 ? 107  ILE B CG1 1 
ATOM   3139 C CG2 . ILE B 1 107 ? -92.645  -31.313 48.116 1.00 33.29 ? 107  ILE B CG2 1 
ATOM   3140 C CD1 . ILE B 1 107 ? -93.795  -32.763 45.703 1.00 30.99 ? 107  ILE B CD1 1 
ATOM   3141 N N   . SER B 1 108 ? -89.003  -29.317 47.726 1.00 29.76 ? 108  SER B N   1 
ATOM   3142 C CA  . SER B 1 108 ? -87.857  -29.193 48.616 1.00 27.49 ? 108  SER B CA  1 
ATOM   3143 C C   . SER B 1 108 ? -88.125  -29.559 50.065 1.00 26.78 ? 108  SER B C   1 
ATOM   3144 O O   . SER B 1 108 ? -87.227  -30.043 50.765 1.00 26.62 ? 108  SER B O   1 
ATOM   3145 C CB  . SER B 1 108 ? -87.296  -27.776 48.583 1.00 28.63 ? 108  SER B CB  1 
ATOM   3146 O OG  . SER B 1 108 ? -87.153  -27.313 47.266 1.00 27.40 ? 108  SER B OG  1 
ATOM   3147 N N   . ALA B 1 109 ? -89.347  -29.330 50.531 1.00 23.72 ? 109  ALA B N   1 
ATOM   3148 C CA  . ALA B 1 109 ? -89.676  -29.651 51.919 1.00 22.68 ? 109  ALA B CA  1 
ATOM   3149 C C   . ALA B 1 109 ? -89.583  -31.152 52.115 1.00 23.31 ? 109  ALA B C   1 
ATOM   3150 O O   . ALA B 1 109 ? -89.196  -31.625 53.187 1.00 22.61 ? 109  ALA B O   1 
ATOM   3151 C CB  . ALA B 1 109 ? -91.080  -29.158 52.263 1.00 22.85 ? 109  ALA B CB  1 
ATOM   3152 N N   . LYS B 1 110 ? -89.948  -31.899 51.072 1.00 22.97 ? 110  LYS B N   1 
ATOM   3153 C CA  . LYS B 1 110 ? -89.888  -33.349 51.122 1.00 22.75 ? 110  LYS B CA  1 
ATOM   3154 C C   . LYS B 1 110 ? -88.417  -33.769 51.052 1.00 26.08 ? 110  LYS B C   1 
ATOM   3155 O O   . LYS B 1 110 ? -87.974  -34.683 51.771 1.00 26.77 ? 110  LYS B O   1 
ATOM   3156 C CB  . LYS B 1 110 ? -90.681  -33.962 49.961 1.00 22.51 ? 110  LYS B CB  1 
ATOM   3157 C CG  . LYS B 1 110 ? -90.576  -35.480 49.870 1.00 24.35 ? 110  LYS B CG  1 
ATOM   3158 C CD  . LYS B 1 110 ? -90.857  -36.144 51.215 1.00 28.43 ? 110  LYS B CD  1 
ATOM   3159 C CE  . LYS B 1 110 ? -90.590  -37.649 51.196 1.00 30.49 ? 110  LYS B CE  1 
ATOM   3160 N NZ  . LYS B 1 110 ? -91.531  -38.374 50.313 1.00 30.81 ? 110  LYS B NZ  1 
ATOM   3161 N N   . LEU B 1 111 ? -87.655  -33.106 50.186 1.00 24.29 ? 111  LEU B N   1 
ATOM   3162 C CA  . LEU B 1 111 ? -86.234  -33.407 50.080 1.00 22.99 ? 111  LEU B CA  1 
ATOM   3163 C C   . LEU B 1 111 ? -85.595  -33.179 51.460 1.00 23.65 ? 111  LEU B C   1 
ATOM   3164 O O   . LEU B 1 111 ? -84.844  -34.017 51.961 1.00 21.02 ? 111  LEU B O   1 
ATOM   3165 C CB  . LEU B 1 111 ? -85.579  -32.496 49.040 1.00 23.43 ? 111  LEU B CB  1 
ATOM   3166 C CG  . LEU B 1 111 ? -84.045  -32.460 49.000 1.00 25.70 ? 111  LEU B CG  1 
ATOM   3167 C CD1 . LEU B 1 111 ? -83.484  -33.835 48.653 1.00 22.27 ? 111  LEU B CD1 1 
ATOM   3168 C CD2 . LEU B 1 111 ? -83.602  -31.408 47.987 1.00 22.52 ? 111  LEU B CD2 1 
ATOM   3169 N N   . VAL B 1 112 ? -85.904  -32.046 52.085 1.00 22.77 ? 112  VAL B N   1 
ATOM   3170 C CA  . VAL B 1 112 ? -85.340  -31.767 53.401 1.00 24.29 ? 112  VAL B CA  1 
ATOM   3171 C C   . VAL B 1 112 ? -85.695  -32.862 54.415 1.00 25.30 ? 112  VAL B C   1 
ATOM   3172 O O   . VAL B 1 112 ? -84.830  -33.313 55.168 1.00 27.83 ? 112  VAL B O   1 
ATOM   3173 C CB  . VAL B 1 112 ? -85.787  -30.381 53.918 1.00 22.88 ? 112  VAL B CB  1 
ATOM   3174 C CG1 . VAL B 1 112 ? -85.426  -30.214 55.403 1.00 23.07 ? 112  VAL B CG1 1 
ATOM   3175 C CG2 . VAL B 1 112 ? -85.083  -29.302 53.107 1.00 23.74 ? 112  VAL B CG2 1 
ATOM   3176 N N   . ALA B 1 113 ? -86.954  -33.299 54.425 1.00 24.51 ? 113  ALA B N   1 
ATOM   3177 C CA  . ALA B 1 113 ? -87.395  -34.354 55.338 1.00 21.92 ? 113  ALA B CA  1 
ATOM   3178 C C   . ALA B 1 113 ? -86.589  -35.628 55.076 1.00 23.57 ? 113  ALA B C   1 
ATOM   3179 O O   . ALA B 1 113 ? -86.180  -36.322 56.015 1.00 21.52 ? 113  ALA B O   1 
ATOM   3180 C CB  . ALA B 1 113 ? -88.878  -34.628 55.146 1.00 19.14 ? 113  ALA B CB  1 
ATOM   3181 N N   . ASN B 1 114 ? -86.362  -35.938 53.800 1.00 23.07 ? 114  ASN B N   1 
ATOM   3182 C CA  . ASN B 1 114 ? -85.579  -37.115 53.449 1.00 23.69 ? 114  ASN B CA  1 
ATOM   3183 C C   . ASN B 1 114 ? -84.135  -36.964 53.886 1.00 21.98 ? 114  ASN B C   1 
ATOM   3184 O O   . ASN B 1 114 ? -83.507  -37.921 54.329 1.00 26.12 ? 114  ASN B O   1 
ATOM   3185 C CB  . ASN B 1 114 ? -85.620  -37.383 51.945 1.00 23.65 ? 114  ASN B CB  1 
ATOM   3186 C CG  . ASN B 1 114 ? -86.896  -38.076 51.516 1.00 24.20 ? 114  ASN B CG  1 
ATOM   3187 O OD1 . ASN B 1 114 ? -87.610  -38.642 52.338 1.00 24.98 ? 114  ASN B OD1 1 
ATOM   3188 N ND2 . ASN B 1 114 ? -87.177  -38.050 50.223 1.00 25.22 ? 114  ASN B ND2 1 
ATOM   3189 N N   . MET B 1 115 ? -83.599  -35.762 53.765 1.00 21.81 ? 115  MET B N   1 
ATOM   3190 C CA  . MET B 1 115 ? -82.220  -35.548 54.174 1.00 24.10 ? 115  MET B CA  1 
ATOM   3191 C C   . MET B 1 115 ? -82.107  -35.760 55.687 1.00 25.26 ? 115  MET B C   1 
ATOM   3192 O O   . MET B 1 115 ? -81.198  -36.450 56.155 1.00 23.92 ? 115  MET B O   1 
ATOM   3193 C CB  . MET B 1 115 ? -81.766  -34.138 53.792 1.00 25.14 ? 115  MET B CB  1 
ATOM   3194 C CG  . MET B 1 115 ? -81.664  -33.912 52.279 1.00 29.85 ? 115  MET B CG  1 
ATOM   3195 S SD  . MET B 1 115 ? -81.174  -32.222 51.887 1.00 37.38 ? 115  MET B SD  1 
ATOM   3196 C CE  . MET B 1 115 ? -82.705  -31.478 51.650 1.00 36.60 ? 115  MET B CE  1 
ATOM   3197 N N   . LEU B 1 116 ? -83.038  -35.176 56.444 1.00 23.90 ? 116  LEU B N   1 
ATOM   3198 C CA  . LEU B 1 116 ? -83.037  -35.319 57.898 1.00 23.61 ? 116  LEU B CA  1 
ATOM   3199 C C   . LEU B 1 116 ? -83.156  -36.788 58.284 1.00 24.62 ? 116  LEU B C   1 
ATOM   3200 O O   . LEU B 1 116 ? -82.566  -37.231 59.270 1.00 24.46 ? 116  LEU B O   1 
ATOM   3201 C CB  . LEU B 1 116 ? -84.188  -34.517 58.514 1.00 23.34 ? 116  LEU B CB  1 
ATOM   3202 C CG  . LEU B 1 116 ? -84.043  -32.985 58.523 1.00 22.80 ? 116  LEU B CG  1 
ATOM   3203 C CD1 . LEU B 1 116 ? -85.413  -32.340 58.630 1.00 20.44 ? 116  LEU B CD1 1 
ATOM   3204 C CD2 . LEU B 1 116 ? -83.153  -32.543 59.687 1.00 22.26 ? 116  LEU B CD2 1 
ATOM   3205 N N   . SER B 1 117 ? -83.919  -37.544 57.497 1.00 25.86 ? 117  SER B N   1 
ATOM   3206 C CA  . SER B 1 117 ? -84.095  -38.964 57.757 1.00 25.63 ? 117  SER B CA  1 
ATOM   3207 C C   . SER B 1 117 ? -82.823  -39.763 57.496 1.00 25.15 ? 117  SER B C   1 
ATOM   3208 O O   . SER B 1 117 ? -82.396  -40.541 58.346 1.00 26.42 ? 117  SER B O   1 
ATOM   3209 C CB  . SER B 1 117 ? -85.238  -39.524 56.910 1.00 26.91 ? 117  SER B CB  1 
ATOM   3210 O OG  . SER B 1 117 ? -86.483  -38.938 57.280 1.00 30.72 ? 117  SER B OG  1 
ATOM   3211 N N   . VAL B 1 118 ? -82.207  -39.584 56.334 1.00 23.67 ? 118  VAL B N   1 
ATOM   3212 C CA  . VAL B 1 118 ? -80.993  -40.335 56.054 1.00 25.42 ? 118  VAL B CA  1 
ATOM   3213 C C   . VAL B 1 118 ? -79.842  -39.874 56.933 1.00 24.00 ? 118  VAL B C   1 
ATOM   3214 O O   . VAL B 1 118 ? -78.941  -40.650 57.226 1.00 26.92 ? 118  VAL B O   1 
ATOM   3215 C CB  . VAL B 1 118 ? -80.577  -40.251 54.556 1.00 26.44 ? 118  VAL B CB  1 
ATOM   3216 C CG1 . VAL B 1 118 ? -81.706  -40.762 53.697 1.00 29.10 ? 118  VAL B CG1 1 
ATOM   3217 C CG2 . VAL B 1 118 ? -80.203  -38.827 54.164 1.00 29.03 ? 118  VAL B CG2 1 
ATOM   3218 N N   . ALA B 1 119 ? -79.868  -38.622 57.367 1.00 22.35 ? 119  ALA B N   1 
ATOM   3219 C CA  . ALA B 1 119 ? -78.802  -38.131 58.233 1.00 23.09 ? 119  ALA B CA  1 
ATOM   3220 C C   . ALA B 1 119 ? -78.840  -38.929 59.522 1.00 24.15 ? 119  ALA B C   1 
ATOM   3221 O O   . ALA B 1 119 ? -77.810  -39.163 60.138 1.00 25.38 ? 119  ALA B O   1 
ATOM   3222 C CB  . ALA B 1 119 ? -78.986  -36.643 58.534 1.00 21.10 ? 119  ALA B CB  1 
ATOM   3223 N N   . GLY B 1 120 ? -80.039  -39.341 59.924 1.00 25.36 ? 120  GLY B N   1 
ATOM   3224 C CA  . GLY B 1 120 ? -80.191  -40.115 61.148 1.00 27.31 ? 120  GLY B CA  1 
ATOM   3225 C C   . GLY B 1 120 ? -81.212  -39.600 62.163 1.00 27.84 ? 120  GLY B C   1 
ATOM   3226 O O   . GLY B 1 120 ? -81.210  -40.031 63.309 1.00 27.57 ? 120  GLY B O   1 
ATOM   3227 N N   . ALA B 1 121 ? -82.093  -38.689 61.771 1.00 25.20 ? 121  ALA B N   1 
ATOM   3228 C CA  . ALA B 1 121 ? -83.090  -38.188 62.716 1.00 25.78 ? 121  ALA B CA  1 
ATOM   3229 C C   . ALA B 1 121 ? -84.109  -39.280 63.062 1.00 25.78 ? 121  ALA B C   1 
ATOM   3230 O O   . ALA B 1 121 ? -84.615  -39.959 62.172 1.00 22.90 ? 121  ALA B O   1 
ATOM   3231 C CB  . ALA B 1 121 ? -83.816  -36.963 62.118 1.00 25.39 ? 121  ALA B CB  1 
ATOM   3232 N N   . ASP B 1 122 ? -84.399  -39.443 64.353 1.00 25.19 ? 122  ASP B N   1 
ATOM   3233 C CA  . ASP B 1 122 ? -85.363  -40.435 64.819 1.00 23.41 ? 122  ASP B CA  1 
ATOM   3234 C C   . ASP B 1 122 ? -86.663  -39.764 65.202 1.00 24.36 ? 122  ASP B C   1 
ATOM   3235 O O   . ASP B 1 122 ? -87.689  -40.420 65.400 1.00 24.64 ? 122  ASP B O   1 
ATOM   3236 C CB  . ASP B 1 122 ? -84.856  -41.154 66.071 1.00 25.04 ? 122  ASP B CB  1 
ATOM   3237 C CG  . ASP B 1 122 ? -83.560  -41.878 65.850 1.00 27.41 ? 122  ASP B CG  1 
ATOM   3238 O OD1 . ASP B 1 122 ? -83.537  -42.806 65.023 1.00 27.41 ? 122  ASP B OD1 1 
ATOM   3239 O OD2 . ASP B 1 122 ? -82.563  -41.513 66.505 1.00 27.79 ? 122  ASP B OD2 1 
ATOM   3240 N N   . HIS B 1 123 ? -86.620  -38.449 65.330 1.00 25.38 ? 123  HIS B N   1 
ATOM   3241 C CA  . HIS B 1 123 ? -87.792  -37.722 65.763 1.00 25.99 ? 123  HIS B CA  1 
ATOM   3242 C C   . HIS B 1 123 ? -87.594  -36.253 65.441 1.00 25.28 ? 123  HIS B C   1 
ATOM   3243 O O   . HIS B 1 123 ? -86.477  -35.735 65.513 1.00 26.98 ? 123  HIS B O   1 
ATOM   3244 C CB  . HIS B 1 123 ? -87.957  -37.948 67.273 1.00 27.49 ? 123  HIS B CB  1 
ATOM   3245 C CG  . HIS B 1 123 ? -89.047  -37.147 67.918 1.00 32.87 ? 123  HIS B CG  1 
ATOM   3246 N ND1 . HIS B 1 123 ? -90.330  -37.086 67.423 1.00 37.15 ? 123  HIS B ND1 1 
ATOM   3247 C CD2 . HIS B 1 123 ? -89.053  -36.430 69.065 1.00 36.38 ? 123  HIS B CD2 1 
ATOM   3248 C CE1 . HIS B 1 123 ? -91.081  -36.365 68.237 1.00 35.70 ? 123  HIS B CE1 1 
ATOM   3249 N NE2 . HIS B 1 123 ? -90.330  -35.956 69.242 1.00 37.08 ? 123  HIS B NE2 1 
ATOM   3250 N N   . ILE B 1 124 ? -88.684  -35.587 65.082 1.00 25.14 ? 124  ILE B N   1 
ATOM   3251 C CA  . ILE B 1 124 ? -88.645  -34.166 64.765 1.00 24.41 ? 124  ILE B CA  1 
ATOM   3252 C C   . ILE B 1 124 ? -89.569  -33.393 65.707 1.00 25.50 ? 124  ILE B C   1 
ATOM   3253 O O   . ILE B 1 124 ? -90.680  -33.837 65.989 1.00 28.16 ? 124  ILE B O   1 
ATOM   3254 C CB  . ILE B 1 124 ? -89.152  -33.857 63.314 1.00 23.21 ? 124  ILE B CB  1 
ATOM   3255 C CG1 . ILE B 1 124 ? -88.289  -34.567 62.250 1.00 21.18 ? 124  ILE B CG1 1 
ATOM   3256 C CG2 . ILE B 1 124 ? -89.160  -32.337 63.104 1.00 21.61 ? 124  ILE B CG2 1 
ATOM   3257 C CD1 . ILE B 1 124 ? -86.802  -34.210 62.292 1.00 19.81 ? 124  ILE B CD1 1 
ATOM   3258 N N   . ILE B 1 125 ? -89.104  -32.250 66.200 1.00 23.85 ? 125  ILE B N   1 
ATOM   3259 C CA  . ILE B 1 125 ? -89.929  -31.376 67.028 1.00 24.79 ? 125  ILE B CA  1 
ATOM   3260 C C   . ILE B 1 125 ? -89.870  -30.030 66.305 1.00 25.02 ? 125  ILE B C   1 
ATOM   3261 O O   . ILE B 1 125 ? -88.787  -29.494 66.068 1.00 25.36 ? 125  ILE B O   1 
ATOM   3262 C CB  . ILE B 1 125 ? -89.382  -31.203 68.468 1.00 26.11 ? 125  ILE B CB  1 
ATOM   3263 C CG1 . ILE B 1 125 ? -89.551  -32.509 69.248 1.00 26.76 ? 125  ILE B CG1 1 
ATOM   3264 C CG2 . ILE B 1 125 ? -90.152  -30.078 69.192 1.00 24.89 ? 125  ILE B CG2 1 
ATOM   3265 C CD1 . ILE B 1 125 ? -88.850  -32.535 70.596 1.00 24.41 ? 125  ILE B CD1 1 
ATOM   3266 N N   . THR B 1 126 ? -91.021  -29.490 65.927 1.00 25.67 ? 126  THR B N   1 
ATOM   3267 C CA  . THR B 1 126 ? -91.031  -28.214 65.215 1.00 25.64 ? 126  THR B CA  1 
ATOM   3268 C C   . THR B 1 126 ? -92.256  -27.415 65.659 1.00 27.33 ? 126  THR B C   1 
ATOM   3269 O O   . THR B 1 126 ? -93.071  -27.909 66.444 1.00 26.39 ? 126  THR B O   1 
ATOM   3270 C CB  . THR B 1 126 ? -91.042  -28.476 63.669 1.00 27.30 ? 126  THR B CB  1 
ATOM   3271 O OG1 . THR B 1 126 ? -90.987  -27.238 62.955 1.00 29.20 ? 126  THR B OG1 1 
ATOM   3272 C CG2 . THR B 1 126 ? -92.298  -29.261 63.258 1.00 24.54 ? 126  THR B CG2 1 
ATOM   3273 N N   . MET B 1 127 ? -92.374  -26.178 65.183 1.00 28.40 ? 127  MET B N   1 
ATOM   3274 C CA  . MET B 1 127 ? -93.516  -25.332 65.534 1.00 28.70 ? 127  MET B CA  1 
ATOM   3275 C C   . MET B 1 127 ? -94.159  -24.720 64.290 1.00 28.79 ? 127  MET B C   1 
ATOM   3276 O O   . MET B 1 127 ? -93.467  -24.210 63.415 1.00 27.80 ? 127  MET B O   1 
ATOM   3277 C CB  . MET B 1 127 ? -93.100  -24.226 66.509 1.00 29.20 ? 127  MET B CB  1 
ATOM   3278 C CG  . MET B 1 127 ? -94.287  -23.367 66.938 1.00 30.09 ? 127  MET B CG  1 
ATOM   3279 S SD  . MET B 1 127 ? -93.895  -22.119 68.178 1.00 31.60 ? 127  MET B SD  1 
ATOM   3280 C CE  . MET B 1 127 ? -93.586  -23.157 69.560 1.00 29.66 ? 127  MET B CE  1 
ATOM   3281 N N   . ASP B 1 128 ? -95.485  -24.790 64.239 1.00 29.38 ? 128  ASP B N   1 
ATOM   3282 C CA  . ASP B 1 128 ? -96.300  -24.294 63.142 1.00 31.68 ? 128  ASP B CA  1 
ATOM   3283 C C   . ASP B 1 128 ? -95.793  -24.545 61.730 1.00 32.34 ? 128  ASP B C   1 
ATOM   3284 O O   . ASP B 1 128 ? -95.433  -23.608 61.002 1.00 31.35 ? 128  ASP B O   1 
ATOM   3285 C CB  . ASP B 1 128 ? -96.620  -22.802 63.322 1.00 33.41 ? 128  ASP B CB  1 
ATOM   3286 C CG  . ASP B 1 128 ? -97.613  -22.555 64.453 1.00 36.28 ? 128  ASP B CG  1 
ATOM   3287 O OD1 . ASP B 1 128 ? -98.728  -23.114 64.402 1.00 39.04 ? 128  ASP B OD1 1 
ATOM   3288 O OD2 . ASP B 1 128 ? -97.278  -21.815 65.400 1.00 39.39 ? 128  ASP B OD2 1 
ATOM   3289 N N   . LEU B 1 129 ? -95.768  -25.818 61.340 1.00 28.34 ? 129  LEU B N   1 
ATOM   3290 C CA  . LEU B 1 129 ? -95.354  -26.174 59.991 1.00 26.55 ? 129  LEU B CA  1 
ATOM   3291 C C   . LEU B 1 129 ? -96.232  -25.395 59.047 1.00 26.77 ? 129  LEU B C   1 
ATOM   3292 O O   . LEU B 1 129 ? -97.446  -25.325 59.252 1.00 25.27 ? 129  LEU B O   1 
ATOM   3293 C CB  . LEU B 1 129 ? -95.571  -27.655 59.721 1.00 26.10 ? 129  LEU B CB  1 
ATOM   3294 C CG  . LEU B 1 129 ? -94.535  -28.564 60.363 1.00 26.11 ? 129  LEU B CG  1 
ATOM   3295 C CD1 . LEU B 1 129 ? -95.031  -29.987 60.253 1.00 26.28 ? 129  LEU B CD1 1 
ATOM   3296 C CD2 . LEU B 1 129 ? -93.160  -28.386 59.680 1.00 24.25 ? 129  LEU B CD2 1 
ATOM   3297 N N   . HIS B 1 130 ? -95.626  -24.838 58.003 1.00 26.18 ? 130  HIS B N   1 
ATOM   3298 C CA  . HIS B 1 130 ? -96.364  -24.050 57.026 1.00 27.91 ? 130  HIS B CA  1 
ATOM   3299 C C   . HIS B 1 130 ? -97.599  -24.793 56.535 1.00 29.38 ? 130  HIS B C   1 
ATOM   3300 O O   . HIS B 1 130 ? -98.619  -24.178 56.225 1.00 29.94 ? 130  HIS B O   1 
ATOM   3301 C CB  . HIS B 1 130 ? -95.457  -23.691 55.835 1.00 30.06 ? 130  HIS B CB  1 
ATOM   3302 C CG  . HIS B 1 130 ? -96.160  -22.938 54.746 1.00 30.27 ? 130  HIS B CG  1 
ATOM   3303 N ND1 . HIS B 1 130 ? -96.584  -23.536 53.580 1.00 33.16 ? 130  HIS B ND1 1 
ATOM   3304 C CD2 . HIS B 1 130 ? -96.530  -21.637 54.656 1.00 29.31 ? 130  HIS B CD2 1 
ATOM   3305 C CE1 . HIS B 1 130 ? -97.184  -22.638 52.815 1.00 31.49 ? 130  HIS B CE1 1 
ATOM   3306 N NE2 . HIS B 1 130 ? -97.163  -21.479 53.448 1.00 34.13 ? 130  HIS B NE2 1 
ATOM   3307 N N   . ALA B 1 131 ? -97.495  -26.118 56.462 1.00 28.92 ? 131  ALA B N   1 
ATOM   3308 C CA  . ALA B 1 131 ? -98.596  -26.973 56.024 1.00 27.92 ? 131  ALA B CA  1 
ATOM   3309 C C   . ALA B 1 131 ? -98.502  -28.262 56.811 1.00 28.34 ? 131  ALA B C   1 
ATOM   3310 O O   . ALA B 1 131 ? -97.486  -28.946 56.767 1.00 28.35 ? 131  ALA B O   1 
ATOM   3311 C CB  . ALA B 1 131 ? -98.486  -27.266 54.533 1.00 27.00 ? 131  ALA B CB  1 
ATOM   3312 N N   . SER B 1 132 ? -99.561  -28.568 57.549 1.00 30.46 ? 132  SER B N   1 
ATOM   3313 C CA  . SER B 1 132 ? -99.633  -29.771 58.366 1.00 32.24 ? 132  SER B CA  1 
ATOM   3314 C C   . SER B 1 132 ? -99.252  -31.034 57.590 1.00 30.25 ? 132  SER B C   1 
ATOM   3315 O O   . SER B 1 132 ? -98.690  -31.977 58.159 1.00 29.43 ? 132  SER B O   1 
ATOM   3316 C CB  . SER B 1 132 ? -101.049 -29.923 58.928 1.00 31.67 ? 132  SER B CB  1 
ATOM   3317 O OG  . SER B 1 132 ? -101.318 -28.869 59.825 1.00 38.46 ? 132  SER B OG  1 
ATOM   3318 N N   . GLN B 1 133 ? -99.562  -31.053 56.298 1.00 27.46 ? 133  GLN B N   1 
ATOM   3319 C CA  . GLN B 1 133 ? -99.236  -32.207 55.472 1.00 28.67 ? 133  GLN B CA  1 
ATOM   3320 C C   . GLN B 1 133 ? -97.742  -32.518 55.497 1.00 28.52 ? 133  GLN B C   1 
ATOM   3321 O O   . GLN B 1 133 ? -97.330  -33.628 55.146 1.00 27.87 ? 133  GLN B O   1 
ATOM   3322 C CB  . GLN B 1 133 ? -99.681  -31.982 54.026 1.00 28.34 ? 133  GLN B CB  1 
ATOM   3323 C CG  . GLN B 1 133 ? -101.195 -31.972 53.822 1.00 30.25 ? 133  GLN B CG  1 
ATOM   3324 C CD  . GLN B 1 133 ? -101.826 -30.631 54.146 1.00 34.06 ? 133  GLN B CD  1 
ATOM   3325 O OE1 . GLN B 1 133 ? -101.146 -29.689 54.563 1.00 31.76 ? 133  GLN B OE1 1 
ATOM   3326 N NE2 . GLN B 1 133 ? -103.136 -30.537 53.951 1.00 33.24 ? 133  GLN B NE2 1 
ATOM   3327 N N   . ILE B 1 134 ? -96.930  -31.552 55.920 1.00 24.50 ? 134  ILE B N   1 
ATOM   3328 C CA  . ILE B 1 134 ? -95.488  -31.765 55.957 1.00 25.64 ? 134  ILE B CA  1 
ATOM   3329 C C   . ILE B 1 134 ? -95.099  -32.905 56.897 1.00 25.96 ? 134  ILE B C   1 
ATOM   3330 O O   . ILE B 1 134 ? -94.044  -33.516 56.726 1.00 26.20 ? 134  ILE B O   1 
ATOM   3331 C CB  . ILE B 1 134 ? -94.729  -30.457 56.350 1.00 25.90 ? 134  ILE B CB  1 
ATOM   3332 C CG1 . ILE B 1 134 ? -94.853  -29.441 55.205 1.00 23.78 ? 134  ILE B CG1 1 
ATOM   3333 C CG2 . ILE B 1 134 ? -93.242  -30.753 56.640 1.00 22.20 ? 134  ILE B CG2 1 
ATOM   3334 C CD1 . ILE B 1 134 ? -94.185  -28.123 55.474 1.00 25.74 ? 134  ILE B CD1 1 
ATOM   3335 N N   . GLN B 1 135 ? -95.946  -33.193 57.881 1.00 25.23 ? 135  GLN B N   1 
ATOM   3336 C CA  . GLN B 1 135 ? -95.678  -34.292 58.804 1.00 26.61 ? 135  GLN B CA  1 
ATOM   3337 C C   . GLN B 1 135 ? -95.657  -35.593 58.005 1.00 25.83 ? 135  GLN B C   1 
ATOM   3338 O O   . GLN B 1 135 ? -94.957  -36.533 58.359 1.00 24.80 ? 135  GLN B O   1 
ATOM   3339 C CB  . GLN B 1 135 ? -96.770  -34.395 59.879 1.00 28.44 ? 135  GLN B CB  1 
ATOM   3340 C CG  . GLN B 1 135 ? -96.635  -33.407 61.021 1.00 30.27 ? 135  GLN B CG  1 
ATOM   3341 C CD  . GLN B 1 135 ? -97.325  -33.905 62.282 1.00 33.10 ? 135  GLN B CD  1 
ATOM   3342 O OE1 . GLN B 1 135 ? -97.131  -35.044 62.698 1.00 37.39 ? 135  GLN B OE1 1 
ATOM   3343 N NE2 . GLN B 1 135 ? -98.123  -33.055 62.897 1.00 33.96 ? 135  GLN B NE2 1 
ATOM   3344 N N   . GLY B 1 136 ? -96.443  -35.635 56.932 1.00 24.12 ? 136  GLY B N   1 
ATOM   3345 C CA  . GLY B 1 136 ? -96.500  -36.818 56.091 1.00 25.19 ? 136  GLY B CA  1 
ATOM   3346 C C   . GLY B 1 136 ? -95.297  -36.964 55.171 1.00 26.16 ? 136  GLY B C   1 
ATOM   3347 O O   . GLY B 1 136 ? -95.214  -37.929 54.416 1.00 25.06 ? 136  GLY B O   1 
ATOM   3348 N N   . PHE B 1 137 ? -94.371  -36.008 55.214 1.00 23.30 ? 137  PHE B N   1 
ATOM   3349 C CA  . PHE B 1 137 ? -93.175  -36.081 54.376 1.00 24.31 ? 137  PHE B CA  1 
ATOM   3350 C C   . PHE B 1 137 ? -92.133  -36.950 55.062 1.00 24.05 ? 137  PHE B C   1 
ATOM   3351 O O   . PHE B 1 137 ? -91.100  -37.262 54.479 1.00 24.58 ? 137  PHE B O   1 
ATOM   3352 C CB  . PHE B 1 137 ? -92.582  -34.685 54.134 1.00 23.38 ? 137  PHE B CB  1 
ATOM   3353 C CG  . PHE B 1 137 ? -93.377  -33.833 53.173 1.00 23.66 ? 137  PHE B CG  1 
ATOM   3354 C CD1 . PHE B 1 137 ? -92.941  -32.557 52.842 1.00 23.20 ? 137  PHE B CD1 1 
ATOM   3355 C CD2 . PHE B 1 137 ? -94.555  -34.300 52.606 1.00 22.07 ? 137  PHE B CD2 1 
ATOM   3356 C CE1 . PHE B 1 137 ? -93.665  -31.756 51.963 1.00 24.35 ? 137  PHE B CE1 1 
ATOM   3357 C CE2 . PHE B 1 137 ? -95.288  -33.505 51.725 1.00 25.54 ? 137  PHE B CE2 1 
ATOM   3358 C CZ  . PHE B 1 137 ? -94.842  -32.230 51.402 1.00 22.87 ? 137  PHE B CZ  1 
ATOM   3359 N N   . PHE B 1 138 ? -92.402  -37.313 56.315 1.00 24.80 ? 138  PHE B N   1 
ATOM   3360 C CA  . PHE B 1 138 ? -91.490  -38.155 57.092 1.00 24.83 ? 138  PHE B CA  1 
ATOM   3361 C C   . PHE B 1 138 ? -92.195  -39.460 57.382 1.00 24.08 ? 138  PHE B C   1 
ATOM   3362 O O   . PHE B 1 138 ? -93.381  -39.596 57.127 1.00 24.48 ? 138  PHE B O   1 
ATOM   3363 C CB  . PHE B 1 138 ? -91.167  -37.553 58.467 1.00 22.98 ? 138  PHE B CB  1 
ATOM   3364 C CG  . PHE B 1 138 ? -90.497  -36.213 58.429 1.00 25.32 ? 138  PHE B CG  1 
ATOM   3365 C CD1 . PHE B 1 138 ? -91.245  -35.045 58.276 1.00 23.08 ? 138  PHE B CD1 1 
ATOM   3366 C CD2 . PHE B 1 138 ? -89.111  -36.114 58.581 1.00 24.89 ? 138  PHE B CD2 1 
ATOM   3367 C CE1 . PHE B 1 138 ? -90.624  -33.798 58.278 1.00 26.24 ? 138  PHE B CE1 1 
ATOM   3368 C CE2 . PHE B 1 138 ? -88.478  -34.876 58.586 1.00 25.61 ? 138  PHE B CE2 1 
ATOM   3369 C CZ  . PHE B 1 138 ? -89.235  -33.711 58.435 1.00 25.57 ? 138  PHE B CZ  1 
ATOM   3370 N N   . ASP B 1 139 ? -91.451  -40.415 57.922 1.00 27.41 ? 139  ASP B N   1 
ATOM   3371 C CA  . ASP B 1 139 ? -92.034  -41.670 58.351 1.00 29.78 ? 139  ASP B CA  1 
ATOM   3372 C C   . ASP B 1 139 ? -91.788  -41.715 59.860 1.00 30.42 ? 139  ASP B C   1 
ATOM   3373 O O   . ASP B 1 139 ? -92.556  -42.314 60.608 1.00 33.61 ? 139  ASP B O   1 
ATOM   3374 C CB  . ASP B 1 139 ? -91.416  -42.860 57.620 1.00 31.56 ? 139  ASP B CB  1 
ATOM   3375 C CG  . ASP B 1 139 ? -92.019  -43.056 56.239 1.00 32.84 ? 139  ASP B CG  1 
ATOM   3376 O OD1 . ASP B 1 139 ? -93.266  -43.081 56.136 1.00 31.84 ? 139  ASP B OD1 1 
ATOM   3377 O OD2 . ASP B 1 139 ? -91.258  -43.174 55.260 1.00 31.73 ? 139  ASP B OD2 1 
ATOM   3378 N N   . ILE B 1 140 ? -90.731  -41.035 60.300 1.00 30.06 ? 140  ILE B N   1 
ATOM   3379 C CA  . ILE B 1 140 ? -90.402  -40.938 61.725 1.00 26.31 ? 140  ILE B CA  1 
ATOM   3380 C C   . ILE B 1 140 ? -91.451  -40.014 62.321 1.00 26.17 ? 140  ILE B C   1 
ATOM   3381 O O   . ILE B 1 140 ? -92.044  -39.195 61.610 1.00 25.89 ? 140  ILE B O   1 
ATOM   3382 C CB  . ILE B 1 140 ? -89.016  -40.288 61.963 1.00 24.60 ? 140  ILE B CB  1 
ATOM   3383 C CG1 . ILE B 1 140 ? -88.966  -38.916 61.279 1.00 25.40 ? 140  ILE B CG1 1 
ATOM   3384 C CG2 . ILE B 1 140 ? -87.907  -41.214 61.480 1.00 25.09 ? 140  ILE B CG2 1 
ATOM   3385 C CD1 . ILE B 1 140 ? -87.676  -38.168 61.486 1.00 19.22 ? 140  ILE B CD1 1 
ATOM   3386 N N   . PRO B 1 141 ? -91.700  -40.123 63.633 1.00 25.79 ? 141  PRO B N   1 
ATOM   3387 C CA  . PRO B 1 141 ? -92.707  -39.248 64.241 1.00 24.50 ? 141  PRO B CA  1 
ATOM   3388 C C   . PRO B 1 141 ? -92.320  -37.764 64.286 1.00 26.17 ? 141  PRO B C   1 
ATOM   3389 O O   . PRO B 1 141 ? -91.154  -37.405 64.473 1.00 23.85 ? 141  PRO B O   1 
ATOM   3390 C CB  . PRO B 1 141 ? -92.903  -39.853 65.633 1.00 24.68 ? 141  PRO B CB  1 
ATOM   3391 C CG  . PRO B 1 141 ? -91.580  -40.510 65.923 1.00 27.57 ? 141  PRO B CG  1 
ATOM   3392 C CD  . PRO B 1 141 ? -91.201  -41.124 64.593 1.00 25.25 ? 141  PRO B CD  1 
ATOM   3393 N N   . VAL B 1 142 ? -93.313  -36.905 64.095 1.00 26.02 ? 142  VAL B N   1 
ATOM   3394 C CA  . VAL B 1 142 ? -93.095  -35.465 64.129 1.00 25.34 ? 142  VAL B CA  1 
ATOM   3395 C C   . VAL B 1 142 ? -94.089  -34.852 65.120 1.00 27.11 ? 142  VAL B C   1 
ATOM   3396 O O   . VAL B 1 142 ? -95.265  -35.220 65.138 1.00 25.36 ? 142  VAL B O   1 
ATOM   3397 C CB  . VAL B 1 142 ? -93.343  -34.808 62.725 1.00 26.14 ? 142  VAL B CB  1 
ATOM   3398 C CG1 . VAL B 1 142 ? -93.175  -33.282 62.817 1.00 24.99 ? 142  VAL B CG1 1 
ATOM   3399 C CG2 . VAL B 1 142 ? -92.382  -35.380 61.688 1.00 23.49 ? 142  VAL B CG2 1 
ATOM   3400 N N   . ASP B 1 143 ? -93.601  -33.962 65.975 1.00 26.37 ? 143  ASP B N   1 
ATOM   3401 C CA  . ASP B 1 143 ? -94.476  -33.248 66.889 1.00 29.13 ? 143  ASP B CA  1 
ATOM   3402 C C   . ASP B 1 143 ? -94.478  -31.818 66.350 1.00 27.83 ? 143  ASP B C   1 
ATOM   3403 O O   . ASP B 1 143 ? -93.440  -31.148 66.328 1.00 28.95 ? 143  ASP B O   1 
ATOM   3404 C CB  . ASP B 1 143 ? -93.945  -33.276 68.330 1.00 31.28 ? 143  ASP B CB  1 
ATOM   3405 C CG  . ASP B 1 143 ? -94.050  -34.650 68.961 1.00 34.19 ? 143  ASP B CG  1 
ATOM   3406 O OD1 . ASP B 1 143 ? -95.140  -35.256 68.883 1.00 34.05 ? 143  ASP B OD1 1 
ATOM   3407 O OD2 . ASP B 1 143 ? -93.047  -35.118 69.538 1.00 35.45 ? 143  ASP B OD2 1 
ATOM   3408 N N   . ASN B 1 144 ? -95.639  -31.379 65.874 1.00 27.72 ? 144  ASN B N   1 
ATOM   3409 C CA  . ASN B 1 144 ? -95.812  -30.039 65.319 1.00 27.01 ? 144  ASN B CA  1 
ATOM   3410 C C   . ASN B 1 144 ? -96.501  -29.182 66.375 1.00 26.59 ? 144  ASN B C   1 
ATOM   3411 O O   . ASN B 1 144 ? -97.721  -29.237 66.543 1.00 25.72 ? 144  ASN B O   1 
ATOM   3412 C CB  . ASN B 1 144 ? -96.656  -30.113 64.033 1.00 26.46 ? 144  ASN B CB  1 
ATOM   3413 C CG  . ASN B 1 144 ? -96.853  -28.757 63.381 1.00 29.09 ? 144  ASN B CG  1 
ATOM   3414 O OD1 . ASN B 1 144 ? -95.949  -27.916 63.373 1.00 26.27 ? 144  ASN B OD1 1 
ATOM   3415 N ND2 . ASN B 1 144 ? -98.034  -28.545 62.812 1.00 31.13 ? 144  ASN B ND2 1 
ATOM   3416 N N   . LEU B 1 145 ? -95.704  -28.409 67.104 1.00 27.04 ? 145  LEU B N   1 
ATOM   3417 C CA  . LEU B 1 145 ? -96.226  -27.546 68.158 1.00 29.24 ? 145  LEU B CA  1 
ATOM   3418 C C   . LEU B 1 145 ? -96.929  -26.319 67.590 1.00 30.35 ? 145  LEU B C   1 
ATOM   3419 O O   . LEU B 1 145 ? -96.554  -25.812 66.539 1.00 29.92 ? 145  LEU B O   1 
ATOM   3420 C CB  . LEU B 1 145 ? -95.090  -27.103 69.073 1.00 27.18 ? 145  LEU B CB  1 
ATOM   3421 C CG  . LEU B 1 145 ? -94.294  -28.219 69.752 1.00 30.89 ? 145  LEU B CG  1 
ATOM   3422 C CD1 . LEU B 1 145 ? -93.093  -27.620 70.466 1.00 28.13 ? 145  LEU B CD1 1 
ATOM   3423 C CD2 . LEU B 1 145 ? -95.177  -28.966 70.718 1.00 31.66 ? 145  LEU B CD2 1 
ATOM   3424 N N   . TYR B 1 146 ? -97.957  -25.838 68.279 1.00 33.01 ? 146  TYR B N   1 
ATOM   3425 C CA  . TYR B 1 146 ? -98.656  -24.658 67.794 1.00 33.59 ? 146  TYR B CA  1 
ATOM   3426 C C   . TYR B 1 146 ? -98.371  -23.463 68.673 1.00 33.87 ? 146  TYR B C   1 
ATOM   3427 O O   . TYR B 1 146 ? -98.205  -23.594 69.883 1.00 33.26 ? 146  TYR B O   1 
ATOM   3428 C CB  . TYR B 1 146 ? -100.160 -24.893 67.757 1.00 38.94 ? 146  TYR B CB  1 
ATOM   3429 C CG  . TYR B 1 146 ? -100.542 -26.134 67.015 1.00 45.65 ? 146  TYR B CG  1 
ATOM   3430 C CD1 . TYR B 1 146 ? -100.449 -27.376 67.629 1.00 50.16 ? 146  TYR B CD1 1 
ATOM   3431 C CD2 . TYR B 1 146 ? -100.969 -26.078 65.685 1.00 49.93 ? 146  TYR B CD2 1 
ATOM   3432 C CE1 . TYR B 1 146 ? -100.769 -28.535 66.950 1.00 52.78 ? 146  TYR B CE1 1 
ATOM   3433 C CE2 . TYR B 1 146 ? -101.294 -27.239 64.990 1.00 51.54 ? 146  TYR B CE2 1 
ATOM   3434 C CZ  . TYR B 1 146 ? -101.192 -28.458 65.639 1.00 52.54 ? 146  TYR B CZ  1 
ATOM   3435 O OH  . TYR B 1 146 ? -101.534 -29.617 65.006 1.00 57.49 ? 146  TYR B OH  1 
ATOM   3436 N N   . ALA B 1 147 ? -98.299  -22.290 68.065 1.00 33.01 ? 147  ALA B N   1 
ATOM   3437 C CA  . ALA B 1 147 ? -98.072  -21.099 68.855 1.00 32.68 ? 147  ALA B CA  1 
ATOM   3438 C C   . ALA B 1 147 ? -99.439  -20.528 69.210 1.00 29.97 ? 147  ALA B C   1 
ATOM   3439 O O   . ALA B 1 147 ? -99.529  -19.583 69.978 1.00 29.55 ? 147  ALA B O   1 
ATOM   3440 C CB  . ALA B 1 147 ? -97.248  -20.077 68.068 1.00 31.82 ? 147  ALA B CB  1 
ATOM   3441 N N   . GLU B 1 148 ? -100.500 -21.130 68.674 1.00 31.29 ? 148  GLU B N   1 
ATOM   3442 C CA  . GLU B 1 148 ? -101.865 -20.651 68.926 1.00 35.52 ? 148  GLU B CA  1 
ATOM   3443 C C   . GLU B 1 148 ? -102.150 -20.323 70.397 1.00 35.71 ? 148  GLU B C   1 
ATOM   3444 O O   . GLU B 1 148 ? -102.544 -19.197 70.719 1.00 36.42 ? 148  GLU B O   1 
ATOM   3445 C CB  . GLU B 1 148 ? -102.908 -21.653 68.410 1.00 36.53 ? 148  GLU B CB  1 
ATOM   3446 C CG  . GLU B 1 148 ? -104.331 -21.108 68.443 1.00 39.78 ? 148  GLU B CG  1 
ATOM   3447 C CD  . GLU B 1 148 ? -105.335 -21.972 67.690 1.00 40.45 ? 148  GLU B CD  1 
ATOM   3448 O OE1 . GLU B 1 148 ? -104.976 -22.522 66.632 1.00 43.78 ? 148  GLU B OE1 1 
ATOM   3449 O OE2 . GLU B 1 148 ? -106.495 -22.084 68.139 1.00 42.29 ? 148  GLU B OE2 1 
ATOM   3450 N N   . PRO B 1 149 ? -101.946 -21.288 71.311 1.00 35.09 ? 149  PRO B N   1 
ATOM   3451 C CA  . PRO B 1 149 ? -102.217 -20.983 72.722 1.00 34.87 ? 149  PRO B CA  1 
ATOM   3452 C C   . PRO B 1 149 ? -101.532 -19.685 73.163 1.00 34.64 ? 149  PRO B C   1 
ATOM   3453 O O   . PRO B 1 149 ? -102.140 -18.841 73.815 1.00 35.58 ? 149  PRO B O   1 
ATOM   3454 C CB  . PRO B 1 149 ? -101.673 -22.216 73.448 1.00 35.52 ? 149  PRO B CB  1 
ATOM   3455 C CG  . PRO B 1 149 ? -101.934 -23.319 72.442 1.00 34.43 ? 149  PRO B CG  1 
ATOM   3456 C CD  . PRO B 1 149 ? -101.485 -22.679 71.150 1.00 34.70 ? 149  PRO B CD  1 
ATOM   3457 N N   . ALA B 1 150 ? -100.270 -19.524 72.781 1.00 34.37 ? 150  ALA B N   1 
ATOM   3458 C CA  . ALA B 1 150 ? -99.505  -18.335 73.140 1.00 33.17 ? 150  ALA B CA  1 
ATOM   3459 C C   . ALA B 1 150 ? -100.021 -17.081 72.427 1.00 33.14 ? 150  ALA B C   1 
ATOM   3460 O O   . ALA B 1 150 ? -99.909  -15.973 72.950 1.00 32.75 ? 150  ALA B O   1 
ATOM   3461 C CB  . ALA B 1 150 ? -98.032  -18.551 72.816 1.00 30.67 ? 150  ALA B CB  1 
ATOM   3462 N N   . VAL B 1 151 ? -100.574 -17.254 71.233 1.00 32.00 ? 151  VAL B N   1 
ATOM   3463 C CA  . VAL B 1 151 ? -101.102 -16.123 70.476 1.00 31.54 ? 151  VAL B CA  1 
ATOM   3464 C C   . VAL B 1 151 ? -102.445 -15.672 71.064 1.00 33.62 ? 151  VAL B C   1 
ATOM   3465 O O   . VAL B 1 151 ? -102.677 -14.479 71.274 1.00 36.43 ? 151  VAL B O   1 
ATOM   3466 C CB  . VAL B 1 151 ? -101.248 -16.502 68.993 1.00 28.93 ? 151  VAL B CB  1 
ATOM   3467 C CG1 . VAL B 1 151 ? -102.013 -15.420 68.227 1.00 26.24 ? 151  VAL B CG1 1 
ATOM   3468 C CG2 . VAL B 1 151 ? -99.856  -16.715 68.397 1.00 27.09 ? 151  VAL B CG2 1 
ATOM   3469 N N   . LEU B 1 152 ? -103.321 -16.630 71.344 1.00 34.18 ? 152  LEU B N   1 
ATOM   3470 C CA  . LEU B 1 152 ? -104.624 -16.329 71.935 1.00 34.70 ? 152  LEU B CA  1 
ATOM   3471 C C   . LEU B 1 152 ? -104.428 -15.591 73.257 1.00 36.03 ? 152  LEU B C   1 
ATOM   3472 O O   . LEU B 1 152 ? -105.164 -14.658 73.580 1.00 37.20 ? 152  LEU B O   1 
ATOM   3473 C CB  . LEU B 1 152 ? -105.399 -17.622 72.191 1.00 31.84 ? 152  LEU B CB  1 
ATOM   3474 C CG  . LEU B 1 152 ? -105.882 -18.389 70.959 1.00 33.98 ? 152  LEU B CG  1 
ATOM   3475 C CD1 . LEU B 1 152 ? -106.314 -19.781 71.343 1.00 34.03 ? 152  LEU B CD1 1 
ATOM   3476 C CD2 . LEU B 1 152 ? -107.019 -17.643 70.318 1.00 33.87 ? 152  LEU B CD2 1 
ATOM   3477 N N   . LYS B 1 153 ? -103.423 -16.019 74.013 1.00 36.26 ? 153  LYS B N   1 
ATOM   3478 C CA  . LYS B 1 153 ? -103.116 -15.420 75.304 1.00 36.37 ? 153  LYS B CA  1 
ATOM   3479 C C   . LYS B 1 153 ? -102.558 -14.015 75.160 1.00 34.91 ? 153  LYS B C   1 
ATOM   3480 O O   . LYS B 1 153 ? -102.898 -13.129 75.933 1.00 36.73 ? 153  LYS B O   1 
ATOM   3481 C CB  . LYS B 1 153 ? -102.119 -16.299 76.058 1.00 36.97 ? 153  LYS B CB  1 
ATOM   3482 C CG  . LYS B 1 153 ? -101.674 -15.762 77.404 1.00 38.66 ? 153  LYS B CG  1 
ATOM   3483 C CD  . LYS B 1 153 ? -100.884 -16.842 78.151 1.00 41.75 ? 153  LYS B CD  1 
ATOM   3484 C CE  . LYS B 1 153 ? -100.440 -16.381 79.525 1.00 42.28 ? 153  LYS B CE  1 
ATOM   3485 N NZ  . LYS B 1 153 ? -99.431  -15.296 79.417 1.00 45.64 ? 153  LYS B NZ  1 
ATOM   3486 N N   . TRP B 1 154 ? -101.691 -13.815 74.177 1.00 34.30 ? 154  TRP B N   1 
ATOM   3487 C CA  . TRP B 1 154 ? -101.108 -12.505 73.954 1.00 33.42 ? 154  TRP B CA  1 
ATOM   3488 C C   . TRP B 1 154 ? -102.238 -11.562 73.527 1.00 33.66 ? 154  TRP B C   1 
ATOM   3489 O O   . TRP B 1 154 ? -102.297 -10.409 73.957 1.00 31.60 ? 154  TRP B O   1 
ATOM   3490 C CB  . TRP B 1 154 ? -100.030 -12.567 72.859 1.00 31.37 ? 154  TRP B CB  1 
ATOM   3491 C CG  . TRP B 1 154 ? -99.308  -11.266 72.683 1.00 31.02 ? 154  TRP B CG  1 
ATOM   3492 C CD1 . TRP B 1 154 ? -98.137  -10.891 73.279 1.00 29.32 ? 154  TRP B CD1 1 
ATOM   3493 C CD2 . TRP B 1 154 ? -99.757  -10.125 71.940 1.00 32.44 ? 154  TRP B CD2 1 
ATOM   3494 N NE1 . TRP B 1 154 ? -97.835  -9.587  72.962 1.00 30.78 ? 154  TRP B NE1 1 
ATOM   3495 C CE2 . TRP B 1 154 ? -98.820  -9.089  72.139 1.00 31.55 ? 154  TRP B CE2 1 
ATOM   3496 C CE3 . TRP B 1 154 ? -100.872 -9.869  71.125 1.00 33.26 ? 154  TRP B CE3 1 
ATOM   3497 C CZ2 . TRP B 1 154 ? -98.951  -7.824  71.561 1.00 33.49 ? 154  TRP B CZ2 1 
ATOM   3498 C CZ3 . TRP B 1 154 ? -101.008 -8.609  70.546 1.00 33.78 ? 154  TRP B CZ3 1 
ATOM   3499 C CH2 . TRP B 1 154 ? -100.054 -7.603  70.770 1.00 33.66 ? 154  TRP B CH2 1 
ATOM   3500 N N   . ILE B 1 155 ? -103.139 -12.065 72.689 1.00 32.96 ? 155  ILE B N   1 
ATOM   3501 C CA  . ILE B 1 155 ? -104.258 -11.257 72.211 1.00 33.89 ? 155  ILE B CA  1 
ATOM   3502 C C   . ILE B 1 155 ? -105.135 -10.773 73.366 1.00 33.76 ? 155  ILE B C   1 
ATOM   3503 O O   . ILE B 1 155 ? -105.355 -9.571  73.529 1.00 32.16 ? 155  ILE B O   1 
ATOM   3504 C CB  . ILE B 1 155 ? -105.132 -12.047 71.205 1.00 32.95 ? 155  ILE B CB  1 
ATOM   3505 C CG1 . ILE B 1 155 ? -104.368 -12.242 69.887 1.00 33.33 ? 155  ILE B CG1 1 
ATOM   3506 C CG2 . ILE B 1 155 ? -106.445 -11.322 70.966 1.00 31.79 ? 155  ILE B CG2 1 
ATOM   3507 C CD1 . ILE B 1 155 ? -105.126 -13.075 68.838 1.00 30.47 ? 155  ILE B CD1 1 
ATOM   3508 N N   . ARG B 1 156 ? -105.624 -11.709 74.170 1.00 34.47 ? 156  ARG B N   1 
ATOM   3509 C CA  . ARG B 1 156 ? -106.490 -11.364 75.297 1.00 37.11 ? 156  ARG B CA  1 
ATOM   3510 C C   . ARG B 1 156 ? -105.824 -10.416 76.290 1.00 37.83 ? 156  ARG B C   1 
ATOM   3511 O O   . ARG B 1 156 ? -106.503 -9.627  76.941 1.00 37.94 ? 156  ARG B O   1 
ATOM   3512 C CB  . ARG B 1 156 ? -106.936 -12.620 76.053 1.00 37.38 ? 156  ARG B CB  1 
ATOM   3513 C CG  . ARG B 1 156 ? -107.765 -13.617 75.263 1.00 37.25 ? 156  ARG B CG  1 
ATOM   3514 C CD  . ARG B 1 156 ? -108.270 -14.711 76.198 1.00 41.88 ? 156  ARG B CD  1 
ATOM   3515 N NE  . ARG B 1 156 ? -109.076 -15.713 75.512 1.00 46.83 ? 156  ARG B NE  1 
ATOM   3516 C CZ  . ARG B 1 156 ? -108.654 -16.939 75.219 1.00 49.97 ? 156  ARG B CZ  1 
ATOM   3517 N NH1 . ARG B 1 156 ? -107.424 -17.319 75.557 1.00 48.84 ? 156  ARG B NH1 1 
ATOM   3518 N NH2 . ARG B 1 156 ? -109.462 -17.785 74.588 1.00 49.45 ? 156  ARG B NH2 1 
ATOM   3519 N N   . GLU B 1 157 ? -104.502 -10.484 76.406 1.00 37.13 ? 157  GLU B N   1 
ATOM   3520 C CA  . GLU B 1 157 ? -103.800 -9.630  77.354 1.00 37.43 ? 157  GLU B CA  1 
ATOM   3521 C C   . GLU B 1 157 ? -103.310 -8.288  76.812 1.00 37.22 ? 157  GLU B C   1 
ATOM   3522 O O   . GLU B 1 157 ? -103.069 -7.366  77.588 1.00 35.64 ? 157  GLU B O   1 
ATOM   3523 C CB  . GLU B 1 157 ? -102.612 -10.389 77.962 1.00 39.23 ? 157  GLU B CB  1 
ATOM   3524 C CG  . GLU B 1 157 ? -102.999 -11.730 78.565 1.00 43.56 ? 157  GLU B CG  1 
ATOM   3525 C CD  . GLU B 1 157 ? -101.874 -12.402 79.336 1.00 45.58 ? 157  GLU B CD  1 
ATOM   3526 O OE1 . GLU B 1 157 ? -100.715 -12.394 78.857 1.00 47.33 ? 157  GLU B OE1 1 
ATOM   3527 O OE2 . GLU B 1 157 ? -102.163 -12.958 80.419 1.00 46.98 ? 157  GLU B OE2 1 
ATOM   3528 N N   . ASN B 1 158 ? -103.183 -8.156  75.496 1.00 35.31 ? 158  ASN B N   1 
ATOM   3529 C CA  . ASN B 1 158 ? -102.671 -6.911  74.932 1.00 35.59 ? 158  ASN B CA  1 
ATOM   3530 C C   . ASN B 1 158 ? -103.646 -6.110  74.074 1.00 35.09 ? 158  ASN B C   1 
ATOM   3531 O O   . ASN B 1 158 ? -103.387 -4.959  73.732 1.00 32.79 ? 158  ASN B O   1 
ATOM   3532 C CB  . ASN B 1 158 ? -101.401 -7.215  74.140 1.00 35.74 ? 158  ASN B CB  1 
ATOM   3533 C CG  . ASN B 1 158 ? -100.353 -7.896  74.993 1.00 39.49 ? 158  ASN B CG  1 
ATOM   3534 O OD1 . ASN B 1 158 ? -99.654  -7.247  75.769 1.00 41.25 ? 158  ASN B OD1 1 
ATOM   3535 N ND2 . ASN B 1 158 ? -100.254 -9.214  74.872 1.00 38.78 ? 158  ASN B ND2 1 
ATOM   3536 N N   . ILE B 1 159 ? -104.766 -6.718  73.721 1.00 35.40 ? 159  ILE B N   1 
ATOM   3537 C CA  . ILE B 1 159 ? -105.753 -6.026  72.917 1.00 34.42 ? 159  ILE B CA  1 
ATOM   3538 C C   . ILE B 1 159 ? -107.058 -5.971  73.698 1.00 34.45 ? 159  ILE B C   1 
ATOM   3539 O O   . ILE B 1 159 ? -107.730 -6.983  73.859 1.00 34.34 ? 159  ILE B O   1 
ATOM   3540 C CB  . ILE B 1 159 ? -105.961 -6.748  71.565 1.00 35.70 ? 159  ILE B CB  1 
ATOM   3541 C CG1 . ILE B 1 159 ? -104.638 -6.757  70.783 1.00 33.55 ? 159  ILE B CG1 1 
ATOM   3542 C CG2 . ILE B 1 159 ? -107.058 -6.054  70.758 1.00 33.05 ? 159  ILE B CG2 1 
ATOM   3543 C CD1 . ILE B 1 159 ? -104.700 -7.539  69.494 1.00 35.31 ? 159  ILE B CD1 1 
ATOM   3544 N N   . SER B 1 160 ? -107.383 -4.775  74.192 1.00 35.88 ? 160  SER B N   1 
ATOM   3545 C CA  . SER B 1 160 ? -108.593 -4.503  74.972 1.00 36.27 ? 160  SER B CA  1 
ATOM   3546 C C   . SER B 1 160 ? -109.862 -4.892  74.230 1.00 35.22 ? 160  SER B C   1 
ATOM   3547 O O   . SER B 1 160 ? -110.800 -5.436  74.817 1.00 35.78 ? 160  SER B O   1 
ATOM   3548 C CB  . SER B 1 160 ? -108.676 -3.008  75.316 1.00 35.74 ? 160  SER B CB  1 
ATOM   3549 O OG  . SER B 1 160 ? -107.447 -2.515  75.818 1.00 39.62 ? 160  SER B OG  1 
ATOM   3550 N N   . GLU B 1 161 ? -109.891 -4.602  72.935 1.00 33.39 ? 161  GLU B N   1 
ATOM   3551 C CA  . GLU B 1 161 ? -111.062 -4.897  72.115 1.00 35.30 ? 161  GLU B CA  1 
ATOM   3552 C C   . GLU B 1 161 ? -111.066 -6.307  71.526 1.00 34.35 ? 161  GLU B C   1 
ATOM   3553 O O   . GLU B 1 161 ? -111.818 -6.579  70.590 1.00 34.50 ? 161  GLU B O   1 
ATOM   3554 C CB  . GLU B 1 161 ? -111.167 -3.874  70.976 1.00 34.95 ? 161  GLU B CB  1 
ATOM   3555 C CG  . GLU B 1 161 ? -110.982 -2.424  71.406 1.00 38.19 ? 161  GLU B CG  1 
ATOM   3556 C CD  . GLU B 1 161 ? -109.543 -1.955  71.318 1.00 42.68 ? 161  GLU B CD  1 
ATOM   3557 O OE1 . GLU B 1 161 ? -108.629 -2.725  71.701 1.00 43.97 ? 161  GLU B OE1 1 
ATOM   3558 O OE2 . GLU B 1 161 ? -109.329 -0.804  70.872 1.00 46.41 ? 161  GLU B OE2 1 
ATOM   3559 N N   . TRP B 1 162 ? -110.261 -7.214  72.074 1.00 32.78 ? 162  TRP B N   1 
ATOM   3560 C CA  . TRP B 1 162 ? -110.204 -8.552  71.514 1.00 32.50 ? 162  TRP B CA  1 
ATOM   3561 C C   . TRP B 1 162 ? -111.552 -9.274  71.388 1.00 34.65 ? 162  TRP B C   1 
ATOM   3562 O O   . TRP B 1 162 ? -111.747 -10.052 70.447 1.00 33.78 ? 162  TRP B O   1 
ATOM   3563 C CB  . TRP B 1 162 ? -109.184 -9.423  72.276 1.00 32.49 ? 162  TRP B CB  1 
ATOM   3564 C CG  . TRP B 1 162 ? -109.583 -9.837  73.658 1.00 29.61 ? 162  TRP B CG  1 
ATOM   3565 C CD1 . TRP B 1 162 ? -109.219 -9.247  74.844 1.00 30.83 ? 162  TRP B CD1 1 
ATOM   3566 C CD2 . TRP B 1 162 ? -110.405 -10.949 74.004 1.00 30.93 ? 162  TRP B CD2 1 
ATOM   3567 N NE1 . TRP B 1 162 ? -109.768 -9.931  75.902 1.00 28.39 ? 162  TRP B NE1 1 
ATOM   3568 C CE2 . TRP B 1 162 ? -110.508 -10.981 75.415 1.00 31.87 ? 162  TRP B CE2 1 
ATOM   3569 C CE3 . TRP B 1 162 ? -111.082 -11.927 73.257 1.00 30.87 ? 162  TRP B CE3 1 
ATOM   3570 C CZ2 . TRP B 1 162 ? -111.249 -11.962 76.098 1.00 30.50 ? 162  TRP B CZ2 1 
ATOM   3571 C CZ3 . TRP B 1 162 ? -111.816 -12.901 73.932 1.00 30.95 ? 162  TRP B CZ3 1 
ATOM   3572 C CH2 . TRP B 1 162 ? -111.897 -12.908 75.340 1.00 29.12 ? 162  TRP B CH2 1 
ATOM   3573 N N   . ARG B 1 163 ? -112.499 -9.019  72.293 1.00 37.04 ? 163  ARG B N   1 
ATOM   3574 C CA  . ARG B 1 163 ? -113.795 -9.701  72.183 1.00 35.94 ? 163  ARG B CA  1 
ATOM   3575 C C   . ARG B 1 163 ? -114.624 -9.195  71.004 1.00 37.12 ? 163  ARG B C   1 
ATOM   3576 O O   . ARG B 1 163 ? -115.672 -9.757  70.690 1.00 38.55 ? 163  ARG B O   1 
ATOM   3577 C CB  . ARG B 1 163 ? -114.609 -9.568  73.472 1.00 36.63 ? 163  ARG B CB  1 
ATOM   3578 C CG  . ARG B 1 163 ? -113.971 -10.219 74.691 1.00 38.70 ? 163  ARG B CG  1 
ATOM   3579 C CD  . ARG B 1 163 ? -114.883 -10.143 75.924 1.00 40.91 ? 163  ARG B CD  1 
ATOM   3580 N NE  . ARG B 1 163 ? -114.148 -10.402 77.165 1.00 46.26 ? 163  ARG B NE  1 
ATOM   3581 C CZ  . ARG B 1 163 ? -114.094 -11.577 77.796 1.00 51.46 ? 163  ARG B CZ  1 
ATOM   3582 N NH1 . ARG B 1 163 ? -114.737 -12.638 77.317 1.00 52.23 ? 163  ARG B NH1 1 
ATOM   3583 N NH2 . ARG B 1 163 ? -113.397 -11.691 78.921 1.00 52.88 ? 163  ARG B NH2 1 
ATOM   3584 N N   . ASN B 1 164 ? -114.145 -8.142  70.347 1.00 35.56 ? 164  ASN B N   1 
ATOM   3585 C CA  . ASN B 1 164 ? -114.835 -7.586  69.189 1.00 37.36 ? 164  ASN B CA  1 
ATOM   3586 C C   . ASN B 1 164 ? -113.896 -7.347  68.000 1.00 37.00 ? 164  ASN B C   1 
ATOM   3587 O O   . ASN B 1 164 ? -114.170 -6.499  67.147 1.00 36.83 ? 164  ASN B O   1 
ATOM   3588 C CB  . ASN B 1 164 ? -115.527 -6.276  69.585 1.00 38.04 ? 164  ASN B CB  1 
ATOM   3589 C CG  . ASN B 1 164 ? -116.749 -6.509  70.461 1.00 39.08 ? 164  ASN B CG  1 
ATOM   3590 O OD1 . ASN B 1 164 ? -117.836 -6.801  69.959 1.00 39.40 ? 164  ASN B OD1 1 
ATOM   3591 N ND2 . ASN B 1 164 ? -116.570 -6.401  71.775 1.00 35.23 ? 164  ASN B ND2 1 
ATOM   3592 N N   . CYS B 1 165 ? -112.793 -8.089  67.938 1.00 33.25 ? 165  CYS B N   1 
ATOM   3593 C CA  . CYS B 1 165 ? -111.841 -7.913  66.847 1.00 31.71 ? 165  CYS B CA  1 
ATOM   3594 C C   . CYS B 1 165 ? -112.151 -8.886  65.709 1.00 32.21 ? 165  CYS B C   1 
ATOM   3595 O O   . CYS B 1 165 ? -113.111 -9.655  65.775 1.00 30.50 ? 165  CYS B O   1 
ATOM   3596 C CB  . CYS B 1 165 ? -110.415 -8.153  67.355 1.00 31.59 ? 165  CYS B CB  1 
ATOM   3597 S SG  . CYS B 1 165 ? -110.052 -9.898  67.769 1.00 31.81 ? 165  CYS B SG  1 
ATOM   3598 N N   . THR B 1 166 ? -111.338 -8.833  64.660 1.00 32.05 ? 166  THR B N   1 
ATOM   3599 C CA  . THR B 1 166 ? -111.491 -9.728  63.529 1.00 31.55 ? 166  THR B CA  1 
ATOM   3600 C C   . THR B 1 166 ? -110.128 -10.316 63.223 1.00 32.30 ? 166  THR B C   1 
ATOM   3601 O O   . THR B 1 166 ? -109.142 -9.586  63.109 1.00 31.04 ? 166  THR B O   1 
ATOM   3602 C CB  . THR B 1 166 ? -112.011 -8.990  62.276 1.00 33.13 ? 166  THR B CB  1 
ATOM   3603 O OG1 . THR B 1 166 ? -113.310 -8.452  62.550 1.00 36.24 ? 166  THR B OG1 1 
ATOM   3604 C CG2 . THR B 1 166 ? -112.119 -9.950  61.078 1.00 31.28 ? 166  THR B CG2 1 
ATOM   3605 N N   . ILE B 1 167 ? -110.065 -11.640 63.136 1.00 31.26 ? 167  ILE B N   1 
ATOM   3606 C CA  . ILE B 1 167 ? -108.823 -12.314 62.798 1.00 29.71 ? 167  ILE B CA  1 
ATOM   3607 C C   . ILE B 1 167 ? -108.856 -12.367 61.278 1.00 30.44 ? 167  ILE B C   1 
ATOM   3608 O O   . ILE B 1 167 ? -109.859 -12.777 60.693 1.00 31.35 ? 167  ILE B O   1 
ATOM   3609 C CB  . ILE B 1 167 ? -108.778 -13.745 63.386 1.00 29.45 ? 167  ILE B CB  1 
ATOM   3610 C CG1 . ILE B 1 167 ? -109.178 -13.704 64.873 1.00 25.59 ? 167  ILE B CG1 1 
ATOM   3611 C CG2 . ILE B 1 167 ? -107.386 -14.334 63.194 1.00 26.01 ? 167  ILE B CG2 1 
ATOM   3612 C CD1 . ILE B 1 167 ? -108.356 -12.706 65.718 1.00 26.62 ? 167  ILE B CD1 1 
ATOM   3613 N N   . VAL B 1 168 ? -107.767 -11.941 60.645 1.00 30.30 ? 168  VAL B N   1 
ATOM   3614 C CA  . VAL B 1 168 ? -107.700 -11.909 59.196 1.00 30.83 ? 168  VAL B CA  1 
ATOM   3615 C C   . VAL B 1 168 ? -106.539 -12.699 58.621 1.00 31.37 ? 168  VAL B C   1 
ATOM   3616 O O   . VAL B 1 168 ? -105.403 -12.595 59.079 1.00 33.26 ? 168  VAL B O   1 
ATOM   3617 C CB  . VAL B 1 168 ? -107.568 -10.458 58.671 1.00 30.46 ? 168  VAL B CB  1 
ATOM   3618 C CG1 . VAL B 1 168 ? -107.850 -10.420 57.179 1.00 28.50 ? 168  VAL B CG1 1 
ATOM   3619 C CG2 . VAL B 1 168 ? -108.507 -9.536  59.418 1.00 29.46 ? 168  VAL B CG2 1 
ATOM   3620 N N   . SER B 1 169 ? -106.835 -13.490 57.605 1.00 31.20 ? 169  SER B N   1 
ATOM   3621 C CA  . SER B 1 169 ? -105.808 -14.269 56.941 1.00 30.91 ? 169  SER B CA  1 
ATOM   3622 C C   . SER B 1 169 ? -105.291 -13.388 55.813 1.00 31.04 ? 169  SER B C   1 
ATOM   3623 O O   . SER B 1 169 ? -106.080 -12.816 55.060 1.00 29.75 ? 169  SER B O   1 
ATOM   3624 C CB  . SER B 1 169 ? -106.404 -15.553 56.361 1.00 30.48 ? 169  SER B CB  1 
ATOM   3625 O OG  . SER B 1 169 ? -105.413 -16.306 55.695 1.00 32.93 ? 169  SER B OG  1 
ATOM   3626 N N   . PRO B 1 170 ? -103.962 -13.243 55.695 1.00 32.06 ? 170  PRO B N   1 
ATOM   3627 C CA  . PRO B 1 170 ? -103.407 -12.408 54.624 1.00 32.41 ? 170  PRO B CA  1 
ATOM   3628 C C   . PRO B 1 170 ? -103.589 -13.044 53.246 1.00 33.90 ? 170  PRO B C   1 
ATOM   3629 O O   . PRO B 1 170 ? -103.518 -12.364 52.229 1.00 34.54 ? 170  PRO B O   1 
ATOM   3630 C CB  . PRO B 1 170 ? -101.940 -12.255 55.025 1.00 33.49 ? 170  PRO B CB  1 
ATOM   3631 C CG  . PRO B 1 170 ? -101.651 -13.529 55.746 1.00 36.10 ? 170  PRO B CG  1 
ATOM   3632 C CD  . PRO B 1 170 ? -102.900 -13.736 56.590 1.00 33.22 ? 170  PRO B CD  1 
ATOM   3633 N N   . ASP B 1 171 ? -103.836 -14.351 53.217 1.00 35.58 ? 171  ASP B N   1 
ATOM   3634 C CA  . ASP B 1 171 ? -104.048 -15.049 51.954 1.00 35.69 ? 171  ASP B CA  1 
ATOM   3635 C C   . ASP B 1 171 ? -105.164 -16.077 52.051 1.00 36.74 ? 171  ASP B C   1 
ATOM   3636 O O   . ASP B 1 171 ? -105.748 -16.282 53.116 1.00 36.34 ? 171  ASP B O   1 
ATOM   3637 C CB  . ASP B 1 171 ? -102.767 -15.737 51.479 1.00 38.19 ? 171  ASP B CB  1 
ATOM   3638 C CG  . ASP B 1 171 ? -102.201 -16.694 52.503 1.00 41.49 ? 171  ASP B CG  1 
ATOM   3639 O OD1 . ASP B 1 171 ? -102.988 -17.372 53.204 1.00 44.96 ? 171  ASP B OD1 1 
ATOM   3640 O OD2 . ASP B 1 171 ? -100.961 -16.778 52.596 1.00 43.57 ? 171  ASP B OD2 1 
ATOM   3641 N N   . ALA B 1 172 ? -105.445 -16.721 50.922 1.00 37.35 ? 172  ALA B N   1 
ATOM   3642 C CA  . ALA B 1 172 ? -106.497 -17.725 50.816 1.00 38.20 ? 172  ALA B CA  1 
ATOM   3643 C C   . ALA B 1 172 ? -106.202 -18.978 51.624 1.00 38.81 ? 172  ALA B C   1 
ATOM   3644 O O   . ALA B 1 172 ? -107.083 -19.530 52.278 1.00 37.79 ? 172  ALA B O   1 
ATOM   3645 C CB  . ALA B 1 172 ? -106.697 -18.098 49.349 1.00 41.71 ? 172  ALA B CB  1 
ATOM   3646 N N   . GLY B 1 173 ? -104.951 -19.418 51.579 1.00 40.16 ? 173  GLY B N   1 
ATOM   3647 C CA  . GLY B 1 173 ? -104.565 -20.618 52.297 1.00 42.08 ? 173  GLY B CA  1 
ATOM   3648 C C   . GLY B 1 173 ? -104.695 -20.602 53.811 1.00 41.61 ? 173  GLY B C   1 
ATOM   3649 O O   . GLY B 1 173 ? -104.818 -21.667 54.421 1.00 42.86 ? 173  GLY B O   1 
ATOM   3650 N N   . GLY B 1 174 ? -104.673 -19.416 54.418 1.00 39.24 ? 174  GLY B N   1 
ATOM   3651 C CA  . GLY B 1 174 ? -104.761 -19.327 55.867 1.00 36.53 ? 174  GLY B CA  1 
ATOM   3652 C C   . GLY B 1 174 ? -106.164 -19.263 56.440 1.00 35.80 ? 174  GLY B C   1 
ATOM   3653 O O   . GLY B 1 174 ? -106.349 -18.941 57.616 1.00 35.61 ? 174  GLY B O   1 
ATOM   3654 N N   . ALA B 1 175 ? -107.155 -19.570 55.616 1.00 36.18 ? 175  ALA B N   1 
ATOM   3655 C CA  . ALA B 1 175 ? -108.541 -19.530 56.057 1.00 39.22 ? 175  ALA B CA  1 
ATOM   3656 C C   . ALA B 1 175 ? -108.761 -20.373 57.303 1.00 41.38 ? 175  ALA B C   1 
ATOM   3657 O O   . ALA B 1 175 ? -109.336 -19.904 58.282 1.00 42.42 ? 175  ALA B O   1 
ATOM   3658 C CB  . ALA B 1 175 ? -109.454 -20.001 54.946 1.00 38.13 ? 175  ALA B CB  1 
ATOM   3659 N N   . LYS B 1 176 ? -108.294 -21.617 57.270 1.00 44.14 ? 176  LYS B N   1 
ATOM   3660 C CA  . LYS B 1 176 ? -108.467 -22.521 58.402 1.00 45.16 ? 176  LYS B CA  1 
ATOM   3661 C C   . LYS B 1 176 ? -107.842 -21.974 59.677 1.00 44.12 ? 176  LYS B C   1 
ATOM   3662 O O   . LYS B 1 176 ? -108.481 -21.938 60.728 1.00 44.12 ? 176  LYS B O   1 
ATOM   3663 C CB  . LYS B 1 176 ? -107.870 -23.888 58.077 1.00 47.00 ? 176  LYS B CB  1 
ATOM   3664 C CG  . LYS B 1 176 ? -108.891 -25.011 58.090 1.00 52.87 ? 176  LYS B CG  1 
ATOM   3665 C CD  . LYS B 1 176 ? -108.260 -26.346 57.725 1.00 55.69 ? 176  LYS B CD  1 
ATOM   3666 C CE  . LYS B 1 176 ? -109.305 -27.455 57.679 1.00 58.06 ? 176  LYS B CE  1 
ATOM   3667 N NZ  . LYS B 1 176 ? -110.366 -27.197 56.657 1.00 58.99 ? 176  LYS B NZ  1 
ATOM   3668 N N   . ARG B 1 177 ? -106.589 -21.549 59.581 1.00 43.69 ? 177  ARG B N   1 
ATOM   3669 C CA  . ARG B 1 177 ? -105.877 -21.003 60.727 1.00 43.92 ? 177  ARG B CA  1 
ATOM   3670 C C   . ARG B 1 177 ? -106.690 -19.914 61.421 1.00 43.69 ? 177  ARG B C   1 
ATOM   3671 O O   . ARG B 1 177 ? -106.954 -20.003 62.618 1.00 45.55 ? 177  ARG B O   1 
ATOM   3672 C CB  . ARG B 1 177 ? -104.539 -20.419 60.279 1.00 47.34 ? 177  ARG B CB  1 
ATOM   3673 C CG  . ARG B 1 177 ? -103.633 -19.983 61.407 1.00 50.34 ? 177  ARG B CG  1 
ATOM   3674 C CD  . ARG B 1 177 ? -102.583 -19.012 60.892 1.00 54.92 ? 177  ARG B CD  1 
ATOM   3675 N NE  . ARG B 1 177 ? -101.978 -19.483 59.652 1.00 56.27 ? 177  ARG B NE  1 
ATOM   3676 C CZ  . ARG B 1 177 ? -101.221 -20.568 59.555 1.00 57.00 ? 177  ARG B CZ  1 
ATOM   3677 N NH1 . ARG B 1 177 ? -100.968 -21.299 60.635 1.00 57.43 ? 177  ARG B NH1 1 
ATOM   3678 N NH2 . ARG B 1 177 ? -100.729 -20.927 58.375 1.00 55.96 ? 177  ARG B NH2 1 
ATOM   3679 N N   . VAL B 1 178 ? -107.102 -18.897 60.666 1.00 41.36 ? 178  VAL B N   1 
ATOM   3680 C CA  . VAL B 1 178 ? -107.856 -17.797 61.251 1.00 40.65 ? 178  VAL B CA  1 
ATOM   3681 C C   . VAL B 1 178 ? -109.239 -18.171 61.784 1.00 39.64 ? 178  VAL B C   1 
ATOM   3682 O O   . VAL B 1 178 ? -109.616 -17.714 62.862 1.00 37.91 ? 178  VAL B O   1 
ATOM   3683 C CB  . VAL B 1 178 ? -107.982 -16.596 60.267 1.00 39.47 ? 178  VAL B CB  1 
ATOM   3684 C CG1 . VAL B 1 178 ? -106.594 -16.128 59.859 1.00 38.79 ? 178  VAL B CG1 1 
ATOM   3685 C CG2 . VAL B 1 178 ? -108.791 -16.982 59.042 1.00 40.55 ? 178  VAL B CG2 1 
ATOM   3686 N N   . THR B 1 179 ? -109.994 -18.996 61.057 1.00 38.82 ? 179  THR B N   1 
ATOM   3687 C CA  . THR B 1 179 ? -111.322 -19.376 61.539 1.00 38.21 ? 179  THR B CA  1 
ATOM   3688 C C   . THR B 1 179 ? -111.194 -20.119 62.869 1.00 38.83 ? 179  THR B C   1 
ATOM   3689 O O   . THR B 1 179 ? -112.055 -20.009 63.743 1.00 38.54 ? 179  THR B O   1 
ATOM   3690 C CB  . THR B 1 179 ? -112.088 -20.279 60.530 1.00 38.17 ? 179  THR B CB  1 
ATOM   3691 O OG1 . THR B 1 179 ? -111.300 -21.430 60.207 1.00 38.30 ? 179  THR B OG1 1 
ATOM   3692 C CG2 . THR B 1 179 ? -112.415 -19.510 59.262 1.00 36.28 ? 179  THR B CG2 1 
ATOM   3693 N N   . SER B 1 180 ? -110.106 -20.868 63.015 1.00 38.36 ? 180  SER B N   1 
ATOM   3694 C CA  . SER B 1 180 ? -109.841 -21.624 64.234 1.00 37.46 ? 180  SER B CA  1 
ATOM   3695 C C   . SER B 1 180 ? -109.622 -20.667 65.403 1.00 37.29 ? 180  SER B C   1 
ATOM   3696 O O   . SER B 1 180 ? -110.137 -20.879 66.501 1.00 37.24 ? 180  SER B O   1 
ATOM   3697 C CB  . SER B 1 180 ? -108.600 -22.506 64.035 1.00 38.58 ? 180  SER B CB  1 
ATOM   3698 O OG  . SER B 1 180 ? -108.225 -23.159 65.231 1.00 41.79 ? 180  SER B OG  1 
ATOM   3699 N N   . ILE B 1 181 ? -108.853 -19.609 65.165 1.00 36.51 ? 181  ILE B N   1 
ATOM   3700 C CA  . ILE B 1 181 ? -108.583 -18.625 66.203 1.00 34.40 ? 181  ILE B CA  1 
ATOM   3701 C C   . ILE B 1 181 ? -109.821 -17.772 66.471 1.00 35.86 ? 181  ILE B C   1 
ATOM   3702 O O   . ILE B 1 181 ? -110.088 -17.399 67.615 1.00 35.45 ? 181  ILE B O   1 
ATOM   3703 C CB  . ILE B 1 181 ? -107.401 -17.719 65.802 1.00 34.29 ? 181  ILE B CB  1 
ATOM   3704 C CG1 . ILE B 1 181 ? -106.115 -18.549 65.776 1.00 34.80 ? 181  ILE B CG1 1 
ATOM   3705 C CG2 . ILE B 1 181 ? -107.269 -16.553 66.770 1.00 31.76 ? 181  ILE B CG2 1 
ATOM   3706 C CD1 . ILE B 1 181 ? -104.891 -17.791 65.322 1.00 35.44 ? 181  ILE B CD1 1 
ATOM   3707 N N   . ALA B 1 182 ? -110.582 -17.475 65.420 1.00 35.22 ? 182  ALA B N   1 
ATOM   3708 C CA  . ALA B 1 182 ? -111.794 -16.669 65.557 1.00 36.34 ? 182  ALA B CA  1 
ATOM   3709 C C   . ALA B 1 182 ? -112.866 -17.409 66.357 1.00 37.82 ? 182  ALA B C   1 
ATOM   3710 O O   . ALA B 1 182 ? -113.541 -16.817 67.200 1.00 38.64 ? 182  ALA B O   1 
ATOM   3711 C CB  . ALA B 1 182 ? -112.332 -16.291 64.186 1.00 32.23 ? 182  ALA B CB  1 
ATOM   3712 N N   . ASP B 1 183 ? -113.021 -18.702 66.090 1.00 38.39 ? 183  ASP B N   1 
ATOM   3713 C CA  . ASP B 1 183 ? -114.004 -19.506 66.808 1.00 40.54 ? 183  ASP B CA  1 
ATOM   3714 C C   . ASP B 1 183 ? -113.629 -19.661 68.287 1.00 40.77 ? 183  ASP B C   1 
ATOM   3715 O O   . ASP B 1 183 ? -114.505 -19.659 69.154 1.00 40.08 ? 183  ASP B O   1 
ATOM   3716 C CB  . ASP B 1 183 ? -114.151 -20.882 66.152 1.00 40.05 ? 183  ASP B CB  1 
ATOM   3717 C CG  . ASP B 1 183 ? -114.848 -20.813 64.809 1.00 41.91 ? 183  ASP B CG  1 
ATOM   3718 O OD1 . ASP B 1 183 ? -115.249 -19.706 64.402 1.00 43.32 ? 183  ASP B OD1 1 
ATOM   3719 O OD2 . ASP B 1 183 ? -115.001 -21.863 64.156 1.00 43.83 ? 183  ASP B OD2 1 
ATOM   3720 N N   . ARG B 1 184 ? -112.337 -19.799 68.578 1.00 41.39 ? 184  ARG B N   1 
ATOM   3721 C CA  . ARG B 1 184 ? -111.898 -19.929 69.970 1.00 43.01 ? 184  ARG B CA  1 
ATOM   3722 C C   . ARG B 1 184 ? -112.168 -18.640 70.748 1.00 41.80 ? 184  ARG B C   1 
ATOM   3723 O O   . ARG B 1 184 ? -112.561 -18.681 71.913 1.00 42.21 ? 184  ARG B O   1 
ATOM   3724 C CB  . ARG B 1 184 ? -110.403 -20.261 70.051 1.00 46.74 ? 184  ARG B CB  1 
ATOM   3725 C CG  . ARG B 1 184 ? -110.083 -21.751 70.079 1.00 52.91 ? 184  ARG B CG  1 
ATOM   3726 C CD  . ARG B 1 184 ? -108.593 -21.975 70.305 1.00 59.67 ? 184  ARG B CD  1 
ATOM   3727 N NE  . ARG B 1 184 ? -108.246 -23.389 70.439 1.00 65.04 ? 184  ARG B NE  1 
ATOM   3728 C CZ  . ARG B 1 184 ? -107.002 -23.854 70.559 1.00 67.33 ? 184  ARG B CZ  1 
ATOM   3729 N NH1 . ARG B 1 184 ? -105.966 -23.020 70.564 1.00 66.54 ? 184  ARG B NH1 1 
ATOM   3730 N NH2 . ARG B 1 184 ? -106.793 -25.163 70.672 1.00 69.73 ? 184  ARG B NH2 1 
ATOM   3731 N N   . LEU B 1 185 ? -111.953 -17.499 70.101 1.00 39.98 ? 185  LEU B N   1 
ATOM   3732 C CA  . LEU B 1 185 ? -112.183 -16.204 70.737 1.00 39.65 ? 185  LEU B CA  1 
ATOM   3733 C C   . LEU B 1 185 ? -113.647 -15.773 70.607 1.00 38.99 ? 185  LEU B C   1 
ATOM   3734 O O   . LEU B 1 185 ? -114.099 -14.873 71.308 1.00 39.82 ? 185  LEU B O   1 
ATOM   3735 C CB  . LEU B 1 185 ? -111.283 -15.134 70.106 1.00 36.74 ? 185  LEU B CB  1 
ATOM   3736 C CG  . LEU B 1 185 ? -109.768 -15.274 70.299 1.00 38.12 ? 185  LEU B CG  1 
ATOM   3737 C CD1 . LEU B 1 185 ? -109.038 -14.158 69.547 1.00 35.76 ? 185  LEU B CD1 1 
ATOM   3738 C CD2 . LEU B 1 185 ? -109.439 -15.215 71.786 1.00 36.92 ? 185  LEU B CD2 1 
ATOM   3739 N N   . ASN B 1 186 ? -114.375 -16.427 69.709 1.00 38.29 ? 186  ASN B N   1 
ATOM   3740 C CA  . ASN B 1 186 ? -115.778 -16.113 69.445 1.00 38.87 ? 186  ASN B CA  1 
ATOM   3741 C C   . ASN B 1 186 ? -115.921 -14.745 68.776 1.00 38.04 ? 186  ASN B C   1 
ATOM   3742 O O   . ASN B 1 186 ? -116.792 -13.955 69.135 1.00 37.44 ? 186  ASN B O   1 
ATOM   3743 C CB  . ASN B 1 186 ? -116.610 -16.138 70.732 1.00 39.96 ? 186  ASN B CB  1 
ATOM   3744 C CG  . ASN B 1 186 ? -118.102 -16.271 70.458 1.00 43.17 ? 186  ASN B CG  1 
ATOM   3745 O OD1 . ASN B 1 186 ? -118.932 -15.812 71.242 1.00 46.53 ? 186  ASN B OD1 1 
ATOM   3746 N ND2 . ASN B 1 186 ? -118.450 -16.918 69.348 1.00 43.71 ? 186  ASN B ND2 1 
ATOM   3747 N N   . VAL B 1 187 ? -115.057 -14.477 67.800 1.00 36.79 ? 187  VAL B N   1 
ATOM   3748 C CA  . VAL B 1 187 ? -115.080 -13.223 67.058 1.00 33.46 ? 187  VAL B CA  1 
ATOM   3749 C C   . VAL B 1 187 ? -115.154 -13.531 65.564 1.00 33.77 ? 187  VAL B C   1 
ATOM   3750 O O   . VAL B 1 187 ? -115.228 -14.698 65.176 1.00 34.54 ? 187  VAL B O   1 
ATOM   3751 C CB  . VAL B 1 187 ? -113.832 -12.375 67.382 1.00 32.79 ? 187  VAL B CB  1 
ATOM   3752 C CG1 . VAL B 1 187 ? -113.832 -12.040 68.859 1.00 34.48 ? 187  VAL B CG1 1 
ATOM   3753 C CG2 . VAL B 1 187 ? -112.540 -13.143 67.026 1.00 28.56 ? 187  VAL B CG2 1 
ATOM   3754 N N   . ASP B 1 188 ? -115.144 -12.494 64.733 1.00 33.24 ? 188  ASP B N   1 
ATOM   3755 C CA  . ASP B 1 188 ? -115.235 -12.667 63.291 1.00 33.18 ? 188  ASP B CA  1 
ATOM   3756 C C   . ASP B 1 188 ? -113.899 -12.981 62.643 1.00 31.89 ? 188  ASP B C   1 
ATOM   3757 O O   . ASP B 1 188 ? -112.847 -12.888 63.266 1.00 33.45 ? 188  ASP B O   1 
ATOM   3758 C CB  . ASP B 1 188 ? -115.813 -11.403 62.633 1.00 35.73 ? 188  ASP B CB  1 
ATOM   3759 C CG  . ASP B 1 188 ? -117.119 -10.959 63.259 1.00 37.60 ? 188  ASP B CG  1 
ATOM   3760 O OD1 . ASP B 1 188 ? -117.818 -11.803 63.851 1.00 40.28 ? 188  ASP B OD1 1 
ATOM   3761 O OD2 . ASP B 1 188 ? -117.453 -9.761  63.152 1.00 43.09 ? 188  ASP B OD2 1 
ATOM   3762 N N   . PHE B 1 189 ? -113.953 -13.341 61.369 1.00 32.30 ? 189  PHE B N   1 
ATOM   3763 C CA  . PHE B 1 189 ? -112.752 -13.639 60.618 1.00 31.14 ? 189  PHE B CA  1 
ATOM   3764 C C   . PHE B 1 189 ? -112.953 -12.993 59.270 1.00 30.22 ? 189  PHE B C   1 
ATOM   3765 O O   . PHE B 1 189 ? -114.073 -12.686 58.875 1.00 30.15 ? 189  PHE B O   1 
ATOM   3766 C CB  . PHE B 1 189 ? -112.561 -15.155 60.469 1.00 31.90 ? 189  PHE B CB  1 
ATOM   3767 C CG  . PHE B 1 189 ? -113.466 -15.787 59.451 1.00 32.52 ? 189  PHE B CG  1 
ATOM   3768 C CD1 . PHE B 1 189 ? -113.089 -15.845 58.115 1.00 29.58 ? 189  PHE B CD1 1 
ATOM   3769 C CD2 . PHE B 1 189 ? -114.708 -16.305 59.824 1.00 33.15 ? 189  PHE B CD2 1 
ATOM   3770 C CE1 . PHE B 1 189 ? -113.925 -16.411 57.163 1.00 32.85 ? 189  PHE B CE1 1 
ATOM   3771 C CE2 . PHE B 1 189 ? -115.560 -16.876 58.871 1.00 31.77 ? 189  PHE B CE2 1 
ATOM   3772 C CZ  . PHE B 1 189 ? -115.167 -16.927 57.541 1.00 32.92 ? 189  PHE B CZ  1 
ATOM   3773 N N   . ALA B 1 190 ? -111.859 -12.773 58.567 1.00 29.89 ? 190  ALA B N   1 
ATOM   3774 C CA  . ALA B 1 190 ? -111.923 -12.164 57.259 1.00 31.52 ? 190  ALA B CA  1 
ATOM   3775 C C   . ALA B 1 190 ? -110.747 -12.745 56.501 1.00 31.17 ? 190  ALA B C   1 
ATOM   3776 O O   . ALA B 1 190 ? -109.826 -13.280 57.116 1.00 32.47 ? 190  ALA B O   1 
ATOM   3777 C CB  . ALA B 1 190 ? -111.804 -10.628 57.382 1.00 29.91 ? 190  ALA B CB  1 
ATOM   3778 N N   . LEU B 1 191 ? -110.774 -12.650 55.178 1.00 32.25 ? 191  LEU B N   1 
ATOM   3779 C CA  . LEU B 1 191 ? -109.692 -13.193 54.363 1.00 33.48 ? 191  LEU B CA  1 
ATOM   3780 C C   . LEU B 1 191 ? -109.300 -12.244 53.254 1.00 33.95 ? 191  LEU B C   1 
ATOM   3781 O O   . LEU B 1 191 ? -110.148 -11.602 52.644 1.00 35.76 ? 191  LEU B O   1 
ATOM   3782 C CB  . LEU B 1 191 ? -110.116 -14.511 53.709 1.00 37.55 ? 191  LEU B CB  1 
ATOM   3783 C CG  . LEU B 1 191 ? -110.592 -15.680 54.563 1.00 40.16 ? 191  LEU B CG  1 
ATOM   3784 C CD1 . LEU B 1 191 ? -111.140 -16.774 53.654 1.00 42.24 ? 191  LEU B CD1 1 
ATOM   3785 C CD2 . LEU B 1 191 ? -109.440 -16.200 55.403 1.00 42.47 ? 191  LEU B CD2 1 
ATOM   3786 N N   . ILE B 1 192 ? -108.008 -12.171 52.982 1.00 35.06 ? 192  ILE B N   1 
ATOM   3787 C CA  . ILE B 1 192 ? -107.519 -11.336 51.908 1.00 34.95 ? 192  ILE B CA  1 
ATOM   3788 C C   . ILE B 1 192 ? -107.005 -12.251 50.812 1.00 36.52 ? 192  ILE B C   1 
ATOM   3789 O O   . ILE B 1 192 ? -106.372 -13.269 51.085 1.00 37.19 ? 192  ILE B O   1 
ATOM   3790 C CB  . ILE B 1 192 ? -106.388 -10.398 52.391 1.00 35.09 ? 192  ILE B CB  1 
ATOM   3791 C CG1 . ILE B 1 192 ? -107.004 -9.195  53.113 1.00 33.55 ? 192  ILE B CG1 1 
ATOM   3792 C CG2 . ILE B 1 192 ? -105.517 -9.953  51.214 1.00 32.91 ? 192  ILE B CG2 1 
ATOM   3793 C CD1 . ILE B 1 192 ? -106.008 -8.186  53.603 1.00 35.36 ? 192  ILE B CD1 1 
ATOM   3794 N N   . HIS B 1 193 ? -107.302 -11.892 49.572 1.00 37.60 ? 193  HIS B N   1 
ATOM   3795 C CA  . HIS B 1 193 ? -106.854 -12.656 48.427 1.00 40.03 ? 193  HIS B CA  1 
ATOM   3796 C C   . HIS B 1 193 ? -106.233 -11.703 47.414 1.00 41.86 ? 193  HIS B C   1 
ATOM   3797 O O   . HIS B 1 193 ? -106.864 -10.732 46.993 1.00 40.91 ? 193  HIS B O   1 
ATOM   3798 C CB  . HIS B 1 193 ? -108.027 -13.412 47.788 1.00 40.71 ? 193  HIS B CB  1 
ATOM   3799 C CG  . HIS B 1 193 ? -107.683 -14.048 46.477 1.00 40.74 ? 193  HIS B CG  1 
ATOM   3800 N ND1 . HIS B 1 193 ? -106.559 -14.827 46.303 1.00 40.49 ? 193  HIS B ND1 1 
ATOM   3801 C CD2 . HIS B 1 193 ? -108.294 -13.994 45.271 1.00 41.68 ? 193  HIS B CD2 1 
ATOM   3802 C CE1 . HIS B 1 193 ? -106.491 -15.222 45.045 1.00 42.63 ? 193  HIS B CE1 1 
ATOM   3803 N NE2 . HIS B 1 193 ? -107.531 -14.731 44.396 1.00 42.92 ? 193  HIS B NE2 1 
ATOM   3804 N N   . LYS B 1 194 ? -104.990 -11.984 47.039 1.00 43.90 ? 194  LYS B N   1 
ATOM   3805 C CA  . LYS B 1 194 ? -104.263 -11.166 46.076 1.00 48.29 ? 194  LYS B CA  1 
ATOM   3806 C C   . LYS B 1 194 ? -104.524 -11.744 44.687 1.00 50.72 ? 194  LYS B C   1 
ATOM   3807 O O   . LYS B 1 194 ? -104.433 -12.956 44.482 1.00 50.23 ? 194  LYS B O   1 
ATOM   3808 C CB  . LYS B 1 194 ? -102.763 -11.207 46.394 1.00 50.44 ? 194  LYS B CB  1 
ATOM   3809 C CG  . LYS B 1 194 ? -101.935 -10.039 45.857 1.00 55.11 ? 194  LYS B CG  1 
ATOM   3810 C CD  . LYS B 1 194 ? -101.614 -10.182 44.377 1.00 58.33 ? 194  LYS B CD  1 
ATOM   3811 C CE  . LYS B 1 194 ? -100.647 -9.093  43.915 1.00 60.18 ? 194  LYS B CE  1 
ATOM   3812 N NZ  . LYS B 1 194 ? -100.170 -9.306  42.511 1.00 60.31 ? 194  LYS B NZ  1 
ATOM   3813 N N   . GLU B 1 195 ? -104.866 -10.879 43.739 1.00 52.61 ? 195  GLU B N   1 
ATOM   3814 C CA  . GLU B 1 195 ? -105.136 -11.318 42.376 1.00 54.80 ? 195  GLU B CA  1 
ATOM   3815 C C   . GLU B 1 195 ? -104.015 -10.866 41.445 1.00 54.80 ? 195  GLU B C   1 
ATOM   3816 O O   . GLU B 1 195 ? -102.834 -11.065 41.743 1.00 54.90 ? 195  GLU B O   1 
ATOM   3817 C CB  . GLU B 1 195 ? -106.476 -10.754 41.901 1.00 55.17 ? 195  GLU B CB  1 
ATOM   3818 C CG  . GLU B 1 195 ? -107.618 -11.055 42.848 1.00 58.70 ? 195  GLU B CG  1 
ATOM   3819 C CD  . GLU B 1 195 ? -108.953 -10.547 42.343 1.00 62.18 ? 195  GLU B CD  1 
ATOM   3820 O OE1 . GLU B 1 195 ? -109.022 -9.374  41.921 1.00 62.27 ? 195  GLU B OE1 1 
ATOM   3821 O OE2 . GLU B 1 195 ? -109.936 -11.320 42.378 1.00 65.20 ? 195  GLU B OE2 1 
ATOM   3822 N N   . ASP B 1 203 ? -102.203 -7.535  40.223 1.00 75.80 ? 203  ASP B N   1 
ATOM   3823 C CA  . ASP B 1 203 ? -101.703 -7.062  41.509 1.00 75.20 ? 203  ASP B CA  1 
ATOM   3824 C C   . ASP B 1 203 ? -102.790 -6.256  42.209 1.00 73.33 ? 203  ASP B C   1 
ATOM   3825 O O   . ASP B 1 203 ? -102.805 -5.027  42.135 1.00 74.24 ? 203  ASP B O   1 
ATOM   3826 C CB  . ASP B 1 203 ? -100.465 -6.185  41.298 1.00 77.57 ? 203  ASP B CB  1 
ATOM   3827 C CG  . ASP B 1 203 ? -99.698  -5.936  42.584 1.00 79.16 ? 203  ASP B CG  1 
ATOM   3828 O OD1 . ASP B 1 203 ? -100.321 -5.521  43.587 1.00 79.86 ? 203  ASP B OD1 1 
ATOM   3829 O OD2 . ASP B 1 203 ? -98.468  -6.152  42.587 1.00 79.36 ? 203  ASP B OD2 1 
ATOM   3830 N N   . ARG B 1 204 ? -103.699 -6.950  42.888 1.00 69.91 ? 204  ARG B N   1 
ATOM   3831 C CA  . ARG B 1 204 ? -104.797 -6.286  43.584 1.00 66.09 ? 204  ARG B CA  1 
ATOM   3832 C C   . ARG B 1 204 ? -105.400 -7.192  44.650 1.00 61.14 ? 204  ARG B C   1 
ATOM   3833 O O   . ARG B 1 204 ? -105.699 -8.351  44.386 1.00 60.60 ? 204  ARG B O   1 
ATOM   3834 C CB  . ARG B 1 204 ? -105.874 -5.898  42.576 1.00 69.84 ? 204  ARG B CB  1 
ATOM   3835 C CG  . ARG B 1 204 ? -106.908 -4.943  43.107 1.00 74.26 ? 204  ARG B CG  1 
ATOM   3836 C CD  . ARG B 1 204 ? -107.881 -4.569  42.011 1.00 78.56 ? 204  ARG B CD  1 
ATOM   3837 N NE  . ARG B 1 204 ? -108.732 -5.694  41.643 1.00 81.84 ? 204  ARG B NE  1 
ATOM   3838 C CZ  . ARG B 1 204 ? -109.621 -6.249  42.461 1.00 84.20 ? 204  ARG B CZ  1 
ATOM   3839 N NH1 . ARG B 1 204 ? -109.773 -5.779  43.696 1.00 85.15 ? 204  ARG B NH1 1 
ATOM   3840 N NH2 . ARG B 1 204 ? -110.362 -7.267  42.045 1.00 84.42 ? 204  ARG B NH2 1 
ATOM   3841 N N   . MET B 1 205 ? -105.585 -6.663  45.851 1.00 54.84 ? 205  MET B N   1 
ATOM   3842 C CA  . MET B 1 205 ? -106.146 -7.452  46.939 1.00 49.33 ? 205  MET B CA  1 
ATOM   3843 C C   . MET B 1 205 ? -107.648 -7.291  47.069 1.00 47.24 ? 205  MET B C   1 
ATOM   3844 O O   . MET B 1 205 ? -108.187 -6.199  46.876 1.00 48.07 ? 205  MET B O   1 
ATOM   3845 C CB  . MET B 1 205 ? -105.495 -7.069  48.273 1.00 46.98 ? 205  MET B CB  1 
ATOM   3846 C CG  . MET B 1 205 ? -104.011 -7.352  48.352 1.00 45.35 ? 205  MET B CG  1 
ATOM   3847 S SD  . MET B 1 205 ? -103.338 -6.999  49.979 1.00 39.11 ? 205  MET B SD  1 
ATOM   3848 C CE  . MET B 1 205 ? -102.128 -8.299  50.148 1.00 41.82 ? 205  MET B CE  1 
ATOM   3849 N N   . VAL B 1 206 ? -108.316 -8.393  47.396 1.00 44.61 ? 206  VAL B N   1 
ATOM   3850 C CA  . VAL B 1 206 ? -109.757 -8.403  47.601 1.00 42.40 ? 206  VAL B CA  1 
ATOM   3851 C C   . VAL B 1 206 ? -109.989 -8.903  49.020 1.00 41.97 ? 206  VAL B C   1 
ATOM   3852 O O   . VAL B 1 206 ? -109.406 -9.902  49.450 1.00 41.82 ? 206  VAL B O   1 
ATOM   3853 C CB  . VAL B 1 206 ? -110.477 -9.340  46.615 1.00 42.60 ? 206  VAL B CB  1 
ATOM   3854 C CG1 . VAL B 1 206 ? -110.275 -8.854  45.196 1.00 45.23 ? 206  VAL B CG1 1 
ATOM   3855 C CG2 . VAL B 1 206 ? -109.952 -10.746 46.756 1.00 45.74 ? 206  VAL B CG2 1 
ATOM   3856 N N   . LEU B 1 207 ? -110.834 -8.200  49.755 1.00 40.72 ? 207  LEU B N   1 
ATOM   3857 C CA  . LEU B 1 207 ? -111.113 -8.575  51.124 1.00 39.17 ? 207  LEU B CA  1 
ATOM   3858 C C   . LEU B 1 207 ? -112.563 -9.015  51.277 1.00 38.84 ? 207  LEU B C   1 
ATOM   3859 O O   . LEU B 1 207 ? -113.464 -8.408  50.708 1.00 38.48 ? 207  LEU B O   1 
ATOM   3860 C CB  . LEU B 1 207 ? -110.822 -7.387  52.048 1.00 39.21 ? 207  LEU B CB  1 
ATOM   3861 C CG  . LEU B 1 207 ? -111.251 -7.442  53.522 1.00 39.31 ? 207  LEU B CG  1 
ATOM   3862 C CD1 . LEU B 1 207 ? -110.392 -8.442  54.296 1.00 38.23 ? 207  LEU B CD1 1 
ATOM   3863 C CD2 . LEU B 1 207 ? -111.103 -6.053  54.125 1.00 39.11 ? 207  LEU B CD2 1 
ATOM   3864 N N   . VAL B 1 208 ? -112.769 -10.095 52.022 1.00 37.50 ? 208  VAL B N   1 
ATOM   3865 C CA  . VAL B 1 208 ? -114.104 -10.595 52.301 1.00 37.52 ? 208  VAL B CA  1 
ATOM   3866 C C   . VAL B 1 208 ? -114.166 -10.793 53.807 1.00 37.64 ? 208  VAL B C   1 
ATOM   3867 O O   . VAL B 1 208 ? -113.240 -11.347 54.409 1.00 36.95 ? 208  VAL B O   1 
ATOM   3868 C CB  . VAL B 1 208 ? -114.411 -11.932 51.564 1.00 35.35 ? 208  VAL B CB  1 
ATOM   3869 C CG1 . VAL B 1 208 ? -114.218 -11.750 50.073 1.00 36.67 ? 208  VAL B CG1 1 
ATOM   3870 C CG2 . VAL B 1 208 ? -113.537 -13.051 52.084 1.00 32.44 ? 208  VAL B CG2 1 
ATOM   3871 N N   . GLY B 1 209 ? -115.247 -10.316 54.416 1.00 37.89 ? 209  GLY B N   1 
ATOM   3872 C CA  . GLY B 1 209 ? -115.403 -10.436 55.857 1.00 38.41 ? 209  GLY B CA  1 
ATOM   3873 C C   . GLY B 1 209 ? -115.555 -9.068  56.489 1.00 39.58 ? 209  GLY B C   1 
ATOM   3874 O O   . GLY B 1 209 ? -115.172 -8.059  55.907 1.00 38.99 ? 209  GLY B O   1 
ATOM   3875 N N   . ASP B 1 210 ? -116.114 -9.038  57.690 1.00 41.57 ? 210  ASP B N   1 
ATOM   3876 C CA  . ASP B 1 210 ? -116.377 -7.788  58.392 1.00 43.05 ? 210  ASP B CA  1 
ATOM   3877 C C   . ASP B 1 210 ? -115.234 -7.305  59.274 1.00 41.27 ? 210  ASP B C   1 
ATOM   3878 O O   . ASP B 1 210 ? -114.867 -7.974  60.248 1.00 40.64 ? 210  ASP B O   1 
ATOM   3879 C CB  . ASP B 1 210 ? -117.650 -7.957  59.249 1.00 46.11 ? 210  ASP B CB  1 
ATOM   3880 C CG  . ASP B 1 210 ? -118.070 -6.677  59.956 1.00 50.20 ? 210  ASP B CG  1 
ATOM   3881 O OD1 . ASP B 1 210 ? -117.267 -6.173  60.762 1.00 54.77 ? 210  ASP B OD1 1 
ATOM   3882 O OD2 . ASP B 1 210 ? -119.197 -6.174  59.715 1.00 54.67 ? 210  ASP B OD2 1 
ATOM   3883 N N   . VAL B 1 211 ? -114.686 -6.136  58.943 1.00 40.47 ? 211  VAL B N   1 
ATOM   3884 C CA  . VAL B 1 211 ? -113.607 -5.533  59.730 1.00 41.48 ? 211  VAL B CA  1 
ATOM   3885 C C   . VAL B 1 211 ? -113.918 -4.079  60.117 1.00 41.57 ? 211  VAL B C   1 
ATOM   3886 O O   . VAL B 1 211 ? -113.205 -3.477  60.919 1.00 39.47 ? 211  VAL B O   1 
ATOM   3887 C CB  . VAL B 1 211 ? -112.233 -5.533  58.975 1.00 42.38 ? 211  VAL B CB  1 
ATOM   3888 C CG1 . VAL B 1 211 ? -111.899 -6.940  58.478 1.00 40.91 ? 211  VAL B CG1 1 
ATOM   3889 C CG2 . VAL B 1 211 ? -112.251 -4.531  57.832 1.00 40.76 ? 211  VAL B CG2 1 
ATOM   3890 N N   . LYS B 1 212 ? -114.984 -3.522  59.555 1.00 42.84 ? 212  LYS B N   1 
ATOM   3891 C CA  . LYS B 1 212 ? -115.350 -2.136  59.840 1.00 43.51 ? 212  LYS B CA  1 
ATOM   3892 C C   . LYS B 1 212 ? -115.524 -1.831  61.328 1.00 42.40 ? 212  LYS B C   1 
ATOM   3893 O O   . LYS B 1 212 ? -116.253 -2.531  62.032 1.00 40.17 ? 212  LYS B O   1 
ATOM   3894 C CB  . LYS B 1 212 ? -116.633 -1.764  59.104 1.00 45.68 ? 212  LYS B CB  1 
ATOM   3895 C CG  . LYS B 1 212 ? -116.926 -0.273  59.150 1.00 50.02 ? 212  LYS B CG  1 
ATOM   3896 C CD  . LYS B 1 212 ? -118.221 0.047   58.444 1.00 53.81 ? 212  LYS B CD  1 
ATOM   3897 C CE  . LYS B 1 212 ? -118.458 1.540   58.435 1.00 56.94 ? 212  LYS B CE  1 
ATOM   3898 N NZ  . LYS B 1 212 ? -117.309 2.252   57.797 1.00 58.13 ? 212  LYS B NZ  1 
ATOM   3899 N N   . ASP B 1 213 ? -114.861 -0.766  61.783 1.00 40.44 ? 213  ASP B N   1 
ATOM   3900 C CA  . ASP B 1 213 ? -114.903 -0.329  63.175 1.00 40.12 ? 213  ASP B CA  1 
ATOM   3901 C C   . ASP B 1 213 ? -114.457 -1.378  64.168 1.00 39.91 ? 213  ASP B C   1 
ATOM   3902 O O   . ASP B 1 213 ? -114.851 -1.341  65.335 1.00 39.19 ? 213  ASP B O   1 
ATOM   3903 C CB  . ASP B 1 213 ? -116.305 0.137   63.559 1.00 43.47 ? 213  ASP B CB  1 
ATOM   3904 C CG  . ASP B 1 213 ? -116.636 1.499   62.992 1.00 48.35 ? 213  ASP B CG  1 
ATOM   3905 O OD1 . ASP B 1 213 ? -116.656 1.634   61.753 1.00 50.43 ? 213  ASP B OD1 1 
ATOM   3906 O OD2 . ASP B 1 213 ? -116.869 2.437   63.787 1.00 53.77 ? 213  ASP B OD2 1 
ATOM   3907 N N   . ARG B 1 214 ? -113.642 -2.316  63.701 1.00 37.68 ? 214  ARG B N   1 
ATOM   3908 C CA  . ARG B 1 214 ? -113.129 -3.379  64.551 1.00 35.97 ? 214  ARG B CA  1 
ATOM   3909 C C   . ARG B 1 214 ? -111.607 -3.393  64.513 1.00 35.15 ? 214  ARG B C   1 
ATOM   3910 O O   . ARG B 1 214 ? -110.992 -2.849  63.595 1.00 33.81 ? 214  ARG B O   1 
ATOM   3911 C CB  . ARG B 1 214 ? -113.632 -4.741  64.062 1.00 37.84 ? 214  ARG B CB  1 
ATOM   3912 C CG  . ARG B 1 214 ? -115.059 -5.086  64.446 1.00 39.88 ? 214  ARG B CG  1 
ATOM   3913 C CD  . ARG B 1 214 ? -115.512 -6.388  63.781 1.00 41.07 ? 214  ARG B CD  1 
ATOM   3914 N NE  . ARG B 1 214 ? -116.743 -6.877  64.392 1.00 46.92 ? 214  ARG B NE  1 
ATOM   3915 C CZ  . ARG B 1 214 ? -116.804 -7.847  65.300 1.00 46.04 ? 214  ARG B CZ  1 
ATOM   3916 N NH1 . ARG B 1 214 ? -115.701 -8.462  65.711 1.00 46.75 ? 214  ARG B NH1 1 
ATOM   3917 N NH2 . ARG B 1 214 ? -117.975 -8.179  65.824 1.00 47.97 ? 214  ARG B NH2 1 
ATOM   3918 N N   . VAL B 1 215 ? -110.998 -4.012  65.516 1.00 32.78 ? 215  VAL B N   1 
ATOM   3919 C CA  . VAL B 1 215 ? -109.553 -4.132  65.541 1.00 30.61 ? 215  VAL B CA  1 
ATOM   3920 C C   . VAL B 1 215 ? -109.297 -5.317  64.618 1.00 31.22 ? 215  VAL B C   1 
ATOM   3921 O O   . VAL B 1 215 ? -109.939 -6.355  64.752 1.00 30.74 ? 215  VAL B O   1 
ATOM   3922 C CB  . VAL B 1 215 ? -109.040 -4.455  66.968 1.00 30.31 ? 215  VAL B CB  1 
ATOM   3923 C CG1 . VAL B 1 215 ? -107.544 -4.724  66.947 1.00 30.43 ? 215  VAL B CG1 1 
ATOM   3924 C CG2 . VAL B 1 215 ? -109.349 -3.300  67.899 1.00 29.22 ? 215  VAL B CG2 1 
ATOM   3925 N N   . ALA B 1 216 ? -108.397 -5.165  63.654 1.00 30.65 ? 216  ALA B N   1 
ATOM   3926 C CA  . ALA B 1 216 ? -108.114 -6.276  62.759 1.00 29.23 ? 216  ALA B CA  1 
ATOM   3927 C C   . ALA B 1 216 ? -106.788 -6.912  63.142 1.00 29.40 ? 216  ALA B C   1 
ATOM   3928 O O   . ALA B 1 216 ? -105.793 -6.219  63.349 1.00 29.67 ? 216  ALA B O   1 
ATOM   3929 C CB  . ALA B 1 216 ? -108.077 -5.802  61.295 1.00 27.06 ? 216  ALA B CB  1 
ATOM   3930 N N   . ILE B 1 217 ? -106.778 -8.234  63.257 1.00 28.62 ? 217  ILE B N   1 
ATOM   3931 C CA  . ILE B 1 217 ? -105.543 -8.924  63.597 1.00 27.82 ? 217  ILE B CA  1 
ATOM   3932 C C   . ILE B 1 217 ? -105.166 -9.869  62.476 1.00 28.35 ? 217  ILE B C   1 
ATOM   3933 O O   . ILE B 1 217 ? -105.829 -10.894 62.264 1.00 25.80 ? 217  ILE B O   1 
ATOM   3934 C CB  . ILE B 1 217 ? -105.657 -9.754  64.894 1.00 26.42 ? 217  ILE B CB  1 
ATOM   3935 C CG1 . ILE B 1 217 ? -106.291 -8.918  66.007 1.00 27.59 ? 217  ILE B CG1 1 
ATOM   3936 C CG2 . ILE B 1 217 ? -104.269 -10.214 65.329 1.00 25.56 ? 217  ILE B CG2 1 
ATOM   3937 C CD1 . ILE B 1 217 ? -106.393 -9.638  67.347 1.00 25.46 ? 217  ILE B CD1 1 
ATOM   3938 N N   . LEU B 1 218 ? -104.114 -9.501  61.750 1.00 27.70 ? 218  LEU B N   1 
ATOM   3939 C CA  . LEU B 1 218 ? -103.591 -10.323 60.667 1.00 29.98 ? 218  LEU B CA  1 
ATOM   3940 C C   . LEU B 1 218 ? -102.808 -11.453 61.321 1.00 30.76 ? 218  LEU B C   1 
ATOM   3941 O O   . LEU B 1 218 ? -101.870 -11.204 62.078 1.00 30.28 ? 218  LEU B O   1 
ATOM   3942 C CB  . LEU B 1 218 ? -102.652 -9.509  59.777 1.00 28.44 ? 218  LEU B CB  1 
ATOM   3943 C CG  . LEU B 1 218 ? -103.291 -8.609  58.722 1.00 29.78 ? 218  LEU B CG  1 
ATOM   3944 C CD1 . LEU B 1 218 ? -102.280 -7.561  58.268 1.00 29.12 ? 218  LEU B CD1 1 
ATOM   3945 C CD2 . LEU B 1 218 ? -103.763 -9.461  57.546 1.00 28.91 ? 218  LEU B CD2 1 
ATOM   3946 N N   . VAL B 1 219 ? -103.208 -12.689 61.046 1.00 31.23 ? 219  VAL B N   1 
ATOM   3947 C CA  . VAL B 1 219 ? -102.527 -13.841 61.618 1.00 32.23 ? 219  VAL B CA  1 
ATOM   3948 C C   . VAL B 1 219 ? -102.048 -14.765 60.521 1.00 34.56 ? 219  VAL B C   1 
ATOM   3949 O O   . VAL B 1 219 ? -102.809 -15.121 59.619 1.00 35.19 ? 219  VAL B O   1 
ATOM   3950 C CB  . VAL B 1 219 ? -103.442 -14.653 62.558 1.00 30.25 ? 219  VAL B CB  1 
ATOM   3951 C CG1 . VAL B 1 219 ? -102.655 -15.812 63.163 1.00 30.32 ? 219  VAL B CG1 1 
ATOM   3952 C CG2 . VAL B 1 219 ? -103.985 -13.758 63.666 1.00 28.34 ? 219  VAL B CG2 1 
ATOM   3953 N N   . ASP B 1 220 ? -100.774 -15.130 60.596 1.00 34.48 ? 220  ASP B N   1 
ATOM   3954 C CA  . ASP B 1 220 ? -100.178 -16.031 59.632 1.00 34.67 ? 220  ASP B CA  1 
ATOM   3955 C C   . ASP B 1 220 ? -99.043  -16.826 60.294 1.00 33.34 ? 220  ASP B C   1 
ATOM   3956 O O   . ASP B 1 220 ? -98.642  -16.528 61.411 1.00 29.43 ? 220  ASP B O   1 
ATOM   3957 C CB  . ASP B 1 220 ? -99.672  -15.239 58.438 1.00 37.53 ? 220  ASP B CB  1 
ATOM   3958 C CG  . ASP B 1 220 ? -99.567  -16.088 57.195 1.00 43.42 ? 220  ASP B CG  1 
ATOM   3959 O OD1 . ASP B 1 220 ? -100.488 -16.904 56.967 1.00 44.10 ? 220  ASP B OD1 1 
ATOM   3960 O OD2 . ASP B 1 220 ? -98.575  -15.939 56.450 1.00 48.16 ? 220  ASP B OD2 1 
ATOM   3961 N N   . ASP B 1 221 ? -98.538  -17.845 59.610 1.00 33.48 ? 221  ASP B N   1 
ATOM   3962 C CA  . ASP B 1 221 ? -97.467  -18.670 60.158 1.00 33.59 ? 221  ASP B CA  1 
ATOM   3963 C C   . ASP B 1 221 ? -96.100  -17.994 60.047 1.00 33.95 ? 221  ASP B C   1 
ATOM   3964 O O   . ASP B 1 221 ? -95.233  -18.178 60.905 1.00 33.52 ? 221  ASP B O   1 
ATOM   3965 C CB  . ASP B 1 221 ? -97.440  -20.027 59.451 1.00 34.31 ? 221  ASP B CB  1 
ATOM   3966 C CG  . ASP B 1 221 ? -96.997  -19.926 58.013 1.00 37.00 ? 221  ASP B CG  1 
ATOM   3967 O OD1 . ASP B 1 221 ? -97.544  -19.081 57.276 1.00 40.80 ? 221  ASP B OD1 1 
ATOM   3968 O OD2 . ASP B 1 221 ? -96.099  -20.695 57.614 1.00 40.12 ? 221  ASP B OD2 1 
ATOM   3969 N N   . MET B 1 222 ? -95.904  -17.211 58.994 1.00 35.43 ? 222  MET B N   1 
ATOM   3970 C CA  . MET B 1 222 ? -94.639  -16.516 58.815 1.00 38.05 ? 222  MET B CA  1 
ATOM   3971 C C   . MET B 1 222 ? -94.750  -15.243 57.994 1.00 38.23 ? 222  MET B C   1 
ATOM   3972 O O   . MET B 1 222 ? -95.715  -15.031 57.263 1.00 38.93 ? 222  MET B O   1 
ATOM   3973 C CB  . MET B 1 222 ? -93.609  -17.434 58.155 1.00 40.98 ? 222  MET B CB  1 
ATOM   3974 C CG  . MET B 1 222 ? -93.953  -17.840 56.728 1.00 45.92 ? 222  MET B CG  1 
ATOM   3975 S SD  . MET B 1 222 ? -92.657  -18.857 55.973 1.00 53.55 ? 222  MET B SD  1 
ATOM   3976 C CE  . MET B 1 222 ? -92.987  -20.464 56.719 1.00 48.73 ? 222  MET B CE  1 
ATOM   3977 N N   . ALA B 1 223 ? -93.739  -14.397 58.138 1.00 38.52 ? 223  ALA B N   1 
ATOM   3978 C CA  . ALA B 1 223 ? -93.648  -13.147 57.406 1.00 38.93 ? 223  ALA B CA  1 
ATOM   3979 C C   . ALA B 1 223 ? -92.192  -13.031 56.979 1.00 38.23 ? 223  ALA B C   1 
ATOM   3980 O O   . ALA B 1 223 ? -91.285  -13.169 57.805 1.00 39.65 ? 223  ALA B O   1 
ATOM   3981 C CB  . ALA B 1 223 ? -94.030  -11.979 58.303 1.00 39.18 ? 223  ALA B CB  1 
ATOM   3982 N N   . ASP B 1 224 ? -91.965  -12.792 55.693 1.00 37.44 ? 224  ASP B N   1 
ATOM   3983 C CA  . ASP B 1 224 ? -90.605  -12.666 55.174 1.00 36.58 ? 224  ASP B CA  1 
ATOM   3984 C C   . ASP B 1 224 ? -90.312  -11.229 54.751 1.00 36.60 ? 224  ASP B C   1 
ATOM   3985 O O   . ASP B 1 224 ? -89.869  -10.425 55.569 1.00 36.58 ? 224  ASP B O   1 
ATOM   3986 C CB  . ASP B 1 224 ? -90.410  -13.615 53.999 1.00 39.30 ? 224  ASP B CB  1 
ATOM   3987 C CG  . ASP B 1 224 ? -88.967  -13.700 53.555 1.00 40.44 ? 224  ASP B CG  1 
ATOM   3988 O OD1 . ASP B 1 224 ? -88.081  -13.194 54.280 1.00 38.76 ? 224  ASP B OD1 1 
ATOM   3989 O OD2 . ASP B 1 224 ? -88.727  -14.288 52.480 1.00 42.52 ? 224  ASP B OD2 1 
ATOM   3990 N N   . THR B 1 225 ? -90.556  -10.891 53.488 1.00 35.50 ? 225  THR B N   1 
ATOM   3991 C CA  . THR B 1 225 ? -90.306  -9.522  53.043 1.00 37.78 ? 225  THR B CA  1 
ATOM   3992 C C   . THR B 1 225 ? -91.381  -8.591  53.601 1.00 38.71 ? 225  THR B C   1 
ATOM   3993 O O   . THR B 1 225 ? -91.194  -7.374  53.658 1.00 40.23 ? 225  THR B O   1 
ATOM   3994 C CB  . THR B 1 225 ? -90.296  -9.414  51.512 1.00 39.18 ? 225  THR B CB  1 
ATOM   3995 O OG1 . THR B 1 225 ? -91.591  -9.745  50.998 1.00 42.85 ? 225  THR B OG1 1 
ATOM   3996 C CG2 . THR B 1 225 ? -89.264  -10.367 50.925 1.00 38.91 ? 225  THR B CG2 1 
ATOM   3997 N N   . CYS B 1 226 ? -92.502  -9.178  54.020 1.00 37.03 ? 226  CYS B N   1 
ATOM   3998 C CA  . CYS B 1 226 ? -93.618  -8.435  54.604 1.00 36.95 ? 226  CYS B CA  1 
ATOM   3999 C C   . CYS B 1 226 ? -94.380  -7.564  53.614 1.00 37.12 ? 226  CYS B C   1 
ATOM   4000 O O   . CYS B 1 226 ? -95.213  -6.750  54.005 1.00 36.88 ? 226  CYS B O   1 
ATOM   4001 C CB  . CYS B 1 226 ? -93.130  -7.568  55.771 1.00 37.80 ? 226  CYS B CB  1 
ATOM   4002 S SG  . CYS B 1 226 ? -92.549  -8.499  57.213 1.00 38.02 ? 226  CYS B SG  1 
ATOM   4003 N N   . GLY B 1 227 ? -94.098  -7.728  52.331 1.00 38.00 ? 227  GLY B N   1 
ATOM   4004 C CA  . GLY B 1 227 ? -94.809  -6.940  51.348 1.00 37.30 ? 227  GLY B CA  1 
ATOM   4005 C C   . GLY B 1 227 ? -96.294  -7.221  51.468 1.00 38.26 ? 227  GLY B C   1 
ATOM   4006 O O   . GLY B 1 227 ? -97.117  -6.307  51.384 1.00 37.87 ? 227  GLY B O   1 
ATOM   4007 N N   . THR B 1 228 ? -96.627  -8.492  51.696 1.00 37.10 ? 228  THR B N   1 
ATOM   4008 C CA  . THR B 1 228 ? -98.013  -8.937  51.810 1.00 37.19 ? 228  THR B CA  1 
ATOM   4009 C C   . THR B 1 228 ? -98.741  -8.393  53.033 1.00 35.18 ? 228  THR B C   1 
ATOM   4010 O O   . THR B 1 228 ? -99.793  -7.772  52.897 1.00 35.44 ? 228  THR B O   1 
ATOM   4011 C CB  . THR B 1 228 ? -98.113  -10.497 51.819 1.00 38.01 ? 228  THR B CB  1 
ATOM   4012 O OG1 . THR B 1 228 ? -97.571  -11.020 50.602 1.00 35.47 ? 228  THR B OG1 1 
ATOM   4013 C CG2 . THR B 1 228 ? -99.563  -10.944 51.928 1.00 35.56 ? 228  THR B CG2 1 
ATOM   4014 N N   . ILE B 1 229 ? -98.200  -8.624  54.223 1.00 33.52 ? 229  ILE B N   1 
ATOM   4015 C CA  . ILE B 1 229 ? -98.860  -8.125  55.428 1.00 35.19 ? 229  ILE B CA  1 
ATOM   4016 C C   . ILE B 1 229 ? -98.936  -6.596  55.442 1.00 35.09 ? 229  ILE B C   1 
ATOM   4017 O O   . ILE B 1 229 ? -99.894  -6.034  55.973 1.00 34.38 ? 229  ILE B O   1 
ATOM   4018 C CB  . ILE B 1 229 ? -98.156  -8.591  56.727 1.00 35.09 ? 229  ILE B CB  1 
ATOM   4019 C CG1 . ILE B 1 229 ? -96.697  -8.133  56.727 1.00 35.30 ? 229  ILE B CG1 1 
ATOM   4020 C CG2 . ILE B 1 229 ? -98.271  -10.101 56.867 1.00 36.37 ? 229  ILE B CG2 1 
ATOM   4021 C CD1 . ILE B 1 229 ? -95.985  -8.384  58.049 1.00 34.62 ? 229  ILE B CD1 1 
ATOM   4022 N N   . CYS B 1 230 ? -97.936  -5.927  54.869 1.00 31.41 ? 230  CYS B N   1 
ATOM   4023 C CA  . CYS B 1 230 ? -97.953  -4.467  54.836 1.00 33.97 ? 230  CYS B CA  1 
ATOM   4024 C C   . CYS B 1 230 ? -99.101  -3.963  53.973 1.00 32.30 ? 230  CYS B C   1 
ATOM   4025 O O   . CYS B 1 230 ? -99.800  -3.027  54.359 1.00 31.75 ? 230  CYS B O   1 
ATOM   4026 C CB  . CYS B 1 230 ? -96.626  -3.905  54.308 1.00 33.31 ? 230  CYS B CB  1 
ATOM   4027 S SG  . CYS B 1 230 ? -95.290  -3.916  55.518 1.00 34.90 ? 230  CYS B SG  1 
ATOM   4028 N N   . HIS B 1 231 ? -99.293  -4.592  52.815 1.00 32.44 ? 231  HIS B N   1 
ATOM   4029 C CA  . HIS B 1 231 ? -100.364 -4.212  51.899 1.00 32.90 ? 231  HIS B CA  1 
ATOM   4030 C C   . HIS B 1 231 ? -101.725 -4.629  52.443 1.00 30.90 ? 231  HIS B C   1 
ATOM   4031 O O   . HIS B 1 231 ? -102.737 -3.995  52.166 1.00 31.02 ? 231  HIS B O   1 
ATOM   4032 C CB  . HIS B 1 231 ? -100.144 -4.836  50.512 1.00 34.79 ? 231  HIS B CB  1 
ATOM   4033 C CG  . HIS B 1 231 ? -99.109  -4.128  49.692 1.00 40.67 ? 231  HIS B CG  1 
ATOM   4034 N ND1 . HIS B 1 231 ? -97.761  -4.213  49.958 1.00 42.98 ? 231  HIS B ND1 1 
ATOM   4035 C CD2 . HIS B 1 231 ? -99.231  -3.284  48.639 1.00 42.98 ? 231  HIS B CD2 1 
ATOM   4036 C CE1 . HIS B 1 231 ? -97.095  -3.454  49.106 1.00 43.29 ? 231  HIS B CE1 1 
ATOM   4037 N NE2 . HIS B 1 231 ? -97.964  -2.879  48.296 1.00 43.63 ? 231  HIS B NE2 1 
ATOM   4038 N N   . ALA B 1 232 ? -101.748 -5.705  53.215 1.00 27.43 ? 232  ALA B N   1 
ATOM   4039 C CA  . ALA B 1 232 ? -102.995 -6.159  53.801 1.00 27.31 ? 232  ALA B CA  1 
ATOM   4040 C C   . ALA B 1 232 ? -103.445 -5.138  54.847 1.00 25.92 ? 232  ALA B C   1 
ATOM   4041 O O   . ALA B 1 232 ? -104.633 -4.856  54.966 1.00 26.17 ? 232  ALA B O   1 
ATOM   4042 C CB  . ALA B 1 232 ? -102.808 -7.526  54.439 1.00 25.25 ? 232  ALA B CB  1 
ATOM   4043 N N   . ALA B 1 233 ? -102.491 -4.585  55.599 1.00 26.18 ? 233  ALA B N   1 
ATOM   4044 C CA  . ALA B 1 233 ? -102.801 -3.589  56.631 1.00 27.04 ? 233  ALA B CA  1 
ATOM   4045 C C   . ALA B 1 233 ? -103.476 -2.349  56.019 1.00 28.53 ? 233  ALA B C   1 
ATOM   4046 O O   . ALA B 1 233 ? -104.468 -1.851  56.558 1.00 26.50 ? 233  ALA B O   1 
ATOM   4047 C CB  . ALA B 1 233 ? -101.530 -3.189  57.381 1.00 24.17 ? 233  ALA B CB  1 
ATOM   4048 N N   . ASP B 1 234 ? -102.941 -1.848  54.906 1.00 29.00 ? 234  ASP B N   1 
ATOM   4049 C CA  . ASP B 1 234 ? -103.557 -0.696  54.242 1.00 31.69 ? 234  ASP B CA  1 
ATOM   4050 C C   . ASP B 1 234 ? -104.976 -1.068  53.868 1.00 31.09 ? 234  ASP B C   1 
ATOM   4051 O O   . ASP B 1 234 ? -105.920 -0.349  54.174 1.00 32.66 ? 234  ASP B O   1 
ATOM   4052 C CB  . ASP B 1 234 ? -102.833 -0.319  52.946 1.00 33.21 ? 234  ASP B CB  1 
ATOM   4053 C CG  . ASP B 1 234 ? -101.457 0.237   53.186 1.00 36.01 ? 234  ASP B CG  1 
ATOM   4054 O OD1 . ASP B 1 234 ? -101.251 0.888   54.230 1.00 38.36 ? 234  ASP B OD1 1 
ATOM   4055 O OD2 . ASP B 1 234 ? -100.586 0.034   52.317 1.00 40.72 ? 234  ASP B OD2 1 
ATOM   4056 N N   . LYS B 1 235 ? -105.111 -2.199  53.185 1.00 30.77 ? 235  LYS B N   1 
ATOM   4057 C CA  . LYS B 1 235 ? -106.410 -2.680  52.758 1.00 29.80 ? 235  LYS B CA  1 
ATOM   4058 C C   . LYS B 1 235 ? -107.387 -2.719  53.928 1.00 29.38 ? 235  LYS B C   1 
ATOM   4059 O O   . LYS B 1 235 ? -108.525 -2.263  53.816 1.00 29.40 ? 235  LYS B O   1 
ATOM   4060 C CB  . LYS B 1 235 ? -106.280 -4.079  52.152 1.00 32.04 ? 235  LYS B CB  1 
ATOM   4061 C CG  . LYS B 1 235 ? -107.578 -4.614  51.564 1.00 35.03 ? 235  LYS B CG  1 
ATOM   4062 C CD  . LYS B 1 235 ? -107.939 -3.868  50.291 1.00 38.52 ? 235  LYS B CD  1 
ATOM   4063 C CE  . LYS B 1 235 ? -109.256 -4.349  49.711 1.00 40.90 ? 235  LYS B CE  1 
ATOM   4064 N NZ  . LYS B 1 235 ? -109.483 -3.795  48.342 1.00 42.59 ? 235  LYS B NZ  1 
ATOM   4065 N N   . LEU B 1 236 ? -106.940 -3.263  55.054 1.00 27.52 ? 236  LEU B N   1 
ATOM   4066 C CA  . LEU B 1 236 ? -107.793 -3.363  56.232 1.00 28.40 ? 236  LEU B CA  1 
ATOM   4067 C C   . LEU B 1 236 ? -108.245 -1.983  56.728 1.00 28.77 ? 236  LEU B C   1 
ATOM   4068 O O   . LEU B 1 236 ? -109.426 -1.780  57.009 1.00 28.95 ? 236  LEU B O   1 
ATOM   4069 C CB  . LEU B 1 236 ? -107.063 -4.134  57.343 1.00 27.71 ? 236  LEU B CB  1 
ATOM   4070 C CG  . LEU B 1 236 ? -106.856 -5.632  57.042 1.00 30.52 ? 236  LEU B CG  1 
ATOM   4071 C CD1 . LEU B 1 236 ? -105.889 -6.260  58.055 1.00 30.10 ? 236  LEU B CD1 1 
ATOM   4072 C CD2 . LEU B 1 236 ? -108.200 -6.349  57.080 1.00 25.40 ? 236  LEU B CD2 1 
ATOM   4073 N N   . LEU B 1 237 ? -107.312 -1.038  56.834 1.00 27.72 ? 237  LEU B N   1 
ATOM   4074 C CA  . LEU B 1 237 ? -107.660 0.303   57.273 1.00 29.00 ? 237  LEU B CA  1 
ATOM   4075 C C   . LEU B 1 237 ? -108.630 0.945   56.276 1.00 29.96 ? 237  LEU B C   1 
ATOM   4076 O O   . LEU B 1 237 ? -109.642 1.524   56.670 1.00 28.30 ? 237  LEU B O   1 
ATOM   4077 C CB  . LEU B 1 237 ? -106.396 1.154   57.436 1.00 29.58 ? 237  LEU B CB  1 
ATOM   4078 C CG  . LEU B 1 237 ? -105.559 0.788   58.674 1.00 32.55 ? 237  LEU B CG  1 
ATOM   4079 C CD1 . LEU B 1 237 ? -104.401 1.755   58.813 1.00 33.18 ? 237  LEU B CD1 1 
ATOM   4080 C CD2 . LEU B 1 237 ? -106.432 0.829   59.935 1.00 29.20 ? 237  LEU B CD2 1 
ATOM   4081 N N   . SER B 1 238 ? -108.342 0.809   54.985 1.00 29.40 ? 238  SER B N   1 
ATOM   4082 C CA  . SER B 1 238 ? -109.222 1.369   53.961 1.00 32.30 ? 238  SER B CA  1 
ATOM   4083 C C   . SER B 1 238 ? -110.630 0.793   54.055 1.00 32.66 ? 238  SER B C   1 
ATOM   4084 O O   . SER B 1 238 ? -111.579 1.391   53.542 1.00 34.11 ? 238  SER B O   1 
ATOM   4085 C CB  . SER B 1 238 ? -108.677 1.086   52.565 1.00 29.85 ? 238  SER B CB  1 
ATOM   4086 O OG  . SER B 1 238 ? -107.450 1.751   52.381 1.00 38.04 ? 238  SER B OG  1 
ATOM   4087 N N   . ALA B 1 239 ? -110.765 -0.367  54.692 1.00 30.47 ? 239  ALA B N   1 
ATOM   4088 C CA  . ALA B 1 239 ? -112.075 -1.001  54.825 1.00 33.30 ? 239  ALA B CA  1 
ATOM   4089 C C   . ALA B 1 239 ? -112.765 -0.610  56.129 1.00 33.54 ? 239  ALA B C   1 
ATOM   4090 O O   . ALA B 1 239 ? -113.852 -1.098  56.435 1.00 35.85 ? 239  ALA B O   1 
ATOM   4091 C CB  . ALA B 1 239 ? -111.944 -2.517  54.740 1.00 31.83 ? 239  ALA B CB  1 
ATOM   4092 N N   . GLY B 1 240 ? -112.128 0.258   56.903 1.00 33.92 ? 240  GLY B N   1 
ATOM   4093 C CA  . GLY B 1 240 ? -112.741 0.689   58.145 1.00 33.35 ? 240  GLY B CA  1 
ATOM   4094 C C   . GLY B 1 240 ? -112.251 0.032   59.420 1.00 34.41 ? 240  GLY B C   1 
ATOM   4095 O O   . GLY B 1 240 ? -112.936 0.101   60.435 1.00 36.59 ? 240  GLY B O   1 
ATOM   4096 N N   . ALA B 1 241 ? -111.090 -0.613  59.391 1.00 33.74 ? 241  ALA B N   1 
ATOM   4097 C CA  . ALA B 1 241 ? -110.565 -1.231  60.608 1.00 32.82 ? 241  ALA B CA  1 
ATOM   4098 C C   . ALA B 1 241 ? -110.013 -0.109  61.481 1.00 33.65 ? 241  ALA B C   1 
ATOM   4099 O O   . ALA B 1 241 ? -109.367 0.819   60.984 1.00 32.51 ? 241  ALA B O   1 
ATOM   4100 C CB  . ALA B 1 241 ? -109.456 -2.231  60.280 1.00 30.22 ? 241  ALA B CB  1 
ATOM   4101 N N   . THR B 1 242 ? -110.273 -0.205  62.779 1.00 34.77 ? 242  THR B N   1 
ATOM   4102 C CA  . THR B 1 242 ? -109.827 0.785   63.752 1.00 36.16 ? 242  THR B CA  1 
ATOM   4103 C C   . THR B 1 242 ? -108.311 0.881   63.781 1.00 36.29 ? 242  THR B C   1 
ATOM   4104 O O   . THR B 1 242 ? -107.739 1.964   63.796 1.00 36.16 ? 242  THR B O   1 
ATOM   4105 C CB  . THR B 1 242 ? -110.308 0.399   65.140 1.00 37.63 ? 242  THR B CB  1 
ATOM   4106 O OG1 . THR B 1 242 ? -111.730 0.249   65.112 1.00 41.54 ? 242  THR B OG1 1 
ATOM   4107 C CG2 . THR B 1 242 ? -109.927 1.467   66.155 1.00 40.37 ? 242  THR B CG2 1 
ATOM   4108 N N   . ARG B 1 243 ? -107.670 -0.277  63.827 1.00 35.85 ? 243  ARG B N   1 
ATOM   4109 C CA  . ARG B 1 243 ? -106.222 -0.360  63.830 1.00 35.88 ? 243  ARG B CA  1 
ATOM   4110 C C   . ARG B 1 243 ? -105.873 -1.781  63.441 1.00 33.87 ? 243  ARG B C   1 
ATOM   4111 O O   . ARG B 1 243 ? -106.728 -2.666  63.465 1.00 33.33 ? 243  ARG B O   1 
ATOM   4112 C CB  . ARG B 1 243 ? -105.638 0.021   65.195 1.00 38.80 ? 243  ARG B CB  1 
ATOM   4113 C CG  . ARG B 1 243 ? -106.292 -0.627  66.390 1.00 45.03 ? 243  ARG B CG  1 
ATOM   4114 C CD  . ARG B 1 243 ? -106.352 0.356   67.570 1.00 49.80 ? 243  ARG B CD  1 
ATOM   4115 N NE  . ARG B 1 243 ? -106.846 -0.289  68.785 1.00 54.57 ? 243  ARG B NE  1 
ATOM   4116 C CZ  . ARG B 1 243 ? -106.150 -1.198  69.462 1.00 56.58 ? 243  ARG B CZ  1 
ATOM   4117 N NH1 . ARG B 1 243 ? -104.948 -1.539  69.031 1.00 56.69 ? 243  ARG B NH1 1 
ATOM   4118 N NH2 . ARG B 1 243 ? -106.645 -1.769  70.554 1.00 55.19 ? 243  ARG B NH2 1 
ATOM   4119 N N   . VAL B 1 244 ? -104.620 -1.998  63.076 1.00 31.60 ? 244  VAL B N   1 
ATOM   4120 C CA  . VAL B 1 244 ? -104.201 -3.305  62.620 1.00 30.74 ? 244  VAL B CA  1 
ATOM   4121 C C   . VAL B 1 244 ? -102.966 -3.855  63.311 1.00 30.49 ? 244  VAL B C   1 
ATOM   4122 O O   . VAL B 1 244 ? -101.995 -3.140  63.555 1.00 31.51 ? 244  VAL B O   1 
ATOM   4123 C CB  . VAL B 1 244 ? -103.949 -3.254  61.098 1.00 30.85 ? 244  VAL B CB  1 
ATOM   4124 C CG1 . VAL B 1 244 ? -103.450 -4.596  60.590 1.00 28.57 ? 244  VAL B CG1 1 
ATOM   4125 C CG2 . VAL B 1 244 ? -105.238 -2.837  60.387 1.00 27.40 ? 244  VAL B CG2 1 
ATOM   4126 N N   . TYR B 1 245 ? -103.030 -5.143  63.617 1.00 30.01 ? 245  TYR B N   1 
ATOM   4127 C CA  . TYR B 1 245 ? -101.939 -5.874  64.245 1.00 30.07 ? 245  TYR B CA  1 
ATOM   4128 C C   . TYR B 1 245 ? -101.616 -7.018  63.302 1.00 30.64 ? 245  TYR B C   1 
ATOM   4129 O O   . TYR B 1 245 ? -102.462 -7.436  62.514 1.00 30.56 ? 245  TYR B O   1 
ATOM   4130 C CB  . TYR B 1 245 ? -102.361 -6.500  65.583 1.00 29.80 ? 245  TYR B CB  1 
ATOM   4131 C CG  . TYR B 1 245 ? -102.608 -5.530  66.712 1.00 30.94 ? 245  TYR B CG  1 
ATOM   4132 C CD1 . TYR B 1 245 ? -103.827 -4.869  66.837 1.00 31.86 ? 245  TYR B CD1 1 
ATOM   4133 C CD2 . TYR B 1 245 ? -101.625 -5.286  67.662 1.00 29.89 ? 245  TYR B CD2 1 
ATOM   4134 C CE1 . TYR B 1 245 ? -104.057 -3.992  67.884 1.00 32.28 ? 245  TYR B CE1 1 
ATOM   4135 C CE2 . TYR B 1 245 ? -101.843 -4.414  68.706 1.00 31.87 ? 245  TYR B CE2 1 
ATOM   4136 C CZ  . TYR B 1 245 ? -103.061 -3.771  68.815 1.00 32.50 ? 245  TYR B CZ  1 
ATOM   4137 O OH  . TYR B 1 245 ? -103.282 -2.922  69.871 1.00 35.94 ? 245  TYR B OH  1 
ATOM   4138 N N   . ALA B 1 246 ? -100.392 -7.520  63.391 1.00 29.94 ? 246  ALA B N   1 
ATOM   4139 C CA  . ALA B 1 246 ? -99.977  -8.650  62.592 1.00 29.50 ? 246  ALA B CA  1 
ATOM   4140 C C   . ALA B 1 246 ? -99.242  -9.560  63.567 1.00 29.73 ? 246  ALA B C   1 
ATOM   4141 O O   . ALA B 1 246 ? -98.329  -9.124  64.274 1.00 29.00 ? 246  ALA B O   1 
ATOM   4142 C CB  . ALA B 1 246 ? -99.056  -8.203  61.463 1.00 28.83 ? 246  ALA B CB  1 
ATOM   4143 N N   . ILE B 1 247 ? -99.666  -10.815 63.626 1.00 28.76 ? 247  ILE B N   1 
ATOM   4144 C CA  . ILE B 1 247 ? -99.048  -11.790 64.512 1.00 27.64 ? 247  ILE B CA  1 
ATOM   4145 C C   . ILE B 1 247 ? -98.617  -12.975 63.659 1.00 29.59 ? 247  ILE B C   1 
ATOM   4146 O O   . ILE B 1 247 ? -99.454  -13.679 63.093 1.00 28.35 ? 247  ILE B O   1 
ATOM   4147 C CB  . ILE B 1 247 ? -100.044 -12.282 65.608 1.00 27.97 ? 247  ILE B CB  1 
ATOM   4148 C CG1 . ILE B 1 247 ? -100.625 -11.082 66.365 1.00 26.23 ? 247  ILE B CG1 1 
ATOM   4149 C CG2 . ILE B 1 247 ? -99.315  -13.196 66.616 1.00 25.48 ? 247  ILE B CG2 1 
ATOM   4150 C CD1 . ILE B 1 247 ? -101.665 -11.455 67.433 1.00 31.66 ? 247  ILE B CD1 1 
ATOM   4151 N N   . LEU B 1 248 ? -97.308  -13.162 63.534 1.00 29.89 ? 248  LEU B N   1 
ATOM   4152 C CA  . LEU B 1 248 ? -96.765  -14.268 62.759 1.00 31.08 ? 248  LEU B CA  1 
ATOM   4153 C C   . LEU B 1 248 ? -95.972  -15.119 63.723 1.00 30.64 ? 248  LEU B C   1 
ATOM   4154 O O   . LEU B 1 248 ? -95.328  -14.582 64.614 1.00 33.06 ? 248  LEU B O   1 
ATOM   4155 C CB  . LEU B 1 248 ? -95.820  -13.767 61.663 1.00 30.92 ? 248  LEU B CB  1 
ATOM   4156 C CG  . LEU B 1 248 ? -96.287  -12.715 60.653 1.00 33.72 ? 248  LEU B CG  1 
ATOM   4157 C CD1 . LEU B 1 248 ? -97.644  -13.107 60.121 1.00 34.30 ? 248  LEU B CD1 1 
ATOM   4158 C CD2 . LEU B 1 248 ? -96.349  -11.335 61.304 1.00 34.47 ? 248  LEU B CD2 1 
ATOM   4159 N N   . THR B 1 249 ? -96.000  -16.438 63.582 1.00 28.41 ? 249  THR B N   1 
ATOM   4160 C CA  . THR B 1 249 ? -95.193  -17.209 64.512 1.00 30.61 ? 249  THR B CA  1 
ATOM   4161 C C   . THR B 1 249 ? -93.707  -17.115 64.126 1.00 30.86 ? 249  THR B C   1 
ATOM   4162 O O   . THR B 1 249 ? -92.852  -16.901 64.986 1.00 30.95 ? 249  THR B O   1 
ATOM   4163 C CB  . THR B 1 249 ? -95.668  -18.683 64.623 1.00 31.12 ? 249  THR B CB  1 
ATOM   4164 O OG1 . THR B 1 249 ? -94.537  -19.562 64.619 1.00 37.50 ? 249  THR B OG1 1 
ATOM   4165 C CG2 . THR B 1 249 ? -96.622  -19.032 63.518 1.00 36.17 ? 249  THR B CG2 1 
ATOM   4166 N N   . HIS B 1 250 ? -93.415  -17.214 62.831 1.00 31.61 ? 250  HIS B N   1 
ATOM   4167 C CA  . HIS B 1 250 ? -92.038  -17.155 62.327 1.00 31.36 ? 250  HIS B CA  1 
ATOM   4168 C C   . HIS B 1 250 ? -91.697  -15.814 61.675 1.00 32.34 ? 250  HIS B C   1 
ATOM   4169 O O   . HIS B 1 250 ? -92.220  -15.480 60.608 1.00 31.32 ? 250  HIS B O   1 
ATOM   4170 C CB  . HIS B 1 250 ? -91.813  -18.266 61.299 1.00 29.57 ? 250  HIS B CB  1 
ATOM   4171 C CG  . HIS B 1 250 ? -92.180  -19.634 61.789 1.00 28.56 ? 250  HIS B CG  1 
ATOM   4172 N ND1 . HIS B 1 250 ? -91.603  -20.206 62.901 1.00 28.74 ? 250  HIS B ND1 1 
ATOM   4173 C CD2 . HIS B 1 250 ? -93.054  -20.549 61.304 1.00 28.85 ? 250  HIS B CD2 1 
ATOM   4174 C CE1 . HIS B 1 250 ? -92.104  -21.417 63.081 1.00 26.64 ? 250  HIS B CE1 1 
ATOM   4175 N NE2 . HIS B 1 250 ? -92.986  -21.648 62.128 1.00 28.59 ? 250  HIS B NE2 1 
ATOM   4176 N N   . GLY B 1 251 ? -90.806  -15.053 62.307 1.00 32.87 ? 251  GLY B N   1 
ATOM   4177 C CA  . GLY B 1 251 ? -90.426  -13.767 61.750 1.00 33.94 ? 251  GLY B CA  1 
ATOM   4178 C C   . GLY B 1 251 ? -89.115  -13.794 60.979 1.00 34.15 ? 251  GLY B C   1 
ATOM   4179 O O   . GLY B 1 251 ? -88.057  -13.524 61.545 1.00 33.45 ? 251  GLY B O   1 
ATOM   4180 N N   . ILE B 1 252 ? -89.180  -14.125 59.691 1.00 35.10 ? 252  ILE B N   1 
ATOM   4181 C CA  . ILE B 1 252 ? -87.984  -14.170 58.845 1.00 34.69 ? 252  ILE B CA  1 
ATOM   4182 C C   . ILE B 1 252 ? -87.460  -12.737 58.678 1.00 33.92 ? 252  ILE B C   1 
ATOM   4183 O O   . ILE B 1 252 ? -86.288  -12.463 58.901 1.00 33.78 ? 252  ILE B O   1 
ATOM   4184 C CB  . ILE B 1 252 ? -88.306  -14.742 57.446 1.00 36.85 ? 252  ILE B CB  1 
ATOM   4185 C CG1 . ILE B 1 252 ? -89.046  -16.076 57.572 1.00 36.18 ? 252  ILE B CG1 1 
ATOM   4186 C CG2 . ILE B 1 252 ? -87.017  -14.933 56.659 1.00 35.79 ? 252  ILE B CG2 1 
ATOM   4187 C CD1 . ILE B 1 252 ? -88.207  -17.182 58.142 1.00 40.47 ? 252  ILE B CD1 1 
ATOM   4188 N N   . PHE B 1 253 ? -88.344  -11.833 58.268 1.00 35.19 ? 253  PHE B N   1 
ATOM   4189 C CA  . PHE B 1 253 ? -87.998  -10.420 58.106 1.00 37.06 ? 253  PHE B CA  1 
ATOM   4190 C C   . PHE B 1 253 ? -86.707  -10.171 57.324 1.00 38.19 ? 253  PHE B C   1 
ATOM   4191 O O   . PHE B 1 253 ? -85.774  -9.561  57.845 1.00 38.05 ? 253  PHE B O   1 
ATOM   4192 C CB  . PHE B 1 253 ? -87.880  -9.755  59.488 1.00 33.89 ? 253  PHE B CB  1 
ATOM   4193 C CG  . PHE B 1 253 ? -89.153  -9.778  60.292 1.00 31.73 ? 253  PHE B CG  1 
ATOM   4194 C CD1 . PHE B 1 253 ? -89.113  -9.893  61.676 1.00 33.66 ? 253  PHE B CD1 1 
ATOM   4195 C CD2 . PHE B 1 253 ? -90.390  -9.669  59.671 1.00 33.36 ? 253  PHE B CD2 1 
ATOM   4196 C CE1 . PHE B 1 253 ? -90.296  -9.899  62.430 1.00 31.02 ? 253  PHE B CE1 1 
ATOM   4197 C CE2 . PHE B 1 253 ? -91.572  -9.674  60.417 1.00 31.56 ? 253  PHE B CE2 1 
ATOM   4198 C CZ  . PHE B 1 253 ? -91.521  -9.789  61.794 1.00 28.76 ? 253  PHE B CZ  1 
ATOM   4199 N N   . SER B 1 254 ? -86.644  -10.636 56.081 1.00 38.91 ? 254  SER B N   1 
ATOM   4200 C CA  . SER B 1 254 ? -85.443  -10.425 55.276 1.00 40.51 ? 254  SER B CA  1 
ATOM   4201 C C   . SER B 1 254 ? -85.672  -9.301  54.274 1.00 40.41 ? 254  SER B C   1 
ATOM   4202 O O   . SER B 1 254 ? -86.776  -8.768  54.172 1.00 40.10 ? 254  SER B O   1 
ATOM   4203 C CB  . SER B 1 254 ? -85.080  -11.706 54.528 1.00 40.12 ? 254  SER B CB  1 
ATOM   4204 O OG  . SER B 1 254 ? -86.068  -12.009 53.564 1.00 41.88 ? 254  SER B OG  1 
ATOM   4205 N N   . GLY B 1 255 ? -84.630  -8.942  53.530 1.00 41.21 ? 255  GLY B N   1 
ATOM   4206 C CA  . GLY B 1 255 ? -84.770  -7.886  52.538 1.00 42.01 ? 255  GLY B CA  1 
ATOM   4207 C C   . GLY B 1 255 ? -85.257  -6.575  53.128 1.00 42.28 ? 255  GLY B C   1 
ATOM   4208 O O   . GLY B 1 255 ? -84.748  -6.145  54.156 1.00 43.79 ? 255  GLY B O   1 
ATOM   4209 N N   . PRO B 1 256 ? -86.251  -5.919  52.505 1.00 43.73 ? 256  PRO B N   1 
ATOM   4210 C CA  . PRO B 1 256 ? -86.793  -4.642  52.989 1.00 45.10 ? 256  PRO B CA  1 
ATOM   4211 C C   . PRO B 1 256 ? -87.892  -4.768  54.050 1.00 45.89 ? 256  PRO B C   1 
ATOM   4212 O O   . PRO B 1 256 ? -88.665  -3.833  54.259 1.00 48.54 ? 256  PRO B O   1 
ATOM   4213 C CB  . PRO B 1 256 ? -87.320  -4.002  51.711 1.00 43.62 ? 256  PRO B CB  1 
ATOM   4214 C CG  . PRO B 1 256 ? -87.919  -5.189  51.019 1.00 43.46 ? 256  PRO B CG  1 
ATOM   4215 C CD  . PRO B 1 256 ? -86.849  -6.270  51.200 1.00 43.32 ? 256  PRO B CD  1 
ATOM   4216 N N   . ALA B 1 257 ? -87.964  -5.916  54.715 1.00 46.37 ? 257  ALA B N   1 
ATOM   4217 C CA  . ALA B 1 257 ? -88.991  -6.138  55.732 1.00 46.25 ? 257  ALA B CA  1 
ATOM   4218 C C   . ALA B 1 257 ? -88.999  -5.070  56.826 1.00 45.63 ? 257  ALA B C   1 
ATOM   4219 O O   . ALA B 1 257 ? -90.016  -4.405  57.042 1.00 44.51 ? 257  ALA B O   1 
ATOM   4220 C CB  . ALA B 1 257 ? -88.826  -7.525  56.361 1.00 45.22 ? 257  ALA B CB  1 
ATOM   4221 N N   . ILE B 1 258 ? -87.872  -4.906  57.514 1.00 44.11 ? 258  ILE B N   1 
ATOM   4222 C CA  . ILE B 1 258 ? -87.783  -3.931  58.594 1.00 44.37 ? 258  ILE B CA  1 
ATOM   4223 C C   . ILE B 1 258 ? -88.122  -2.516  58.130 1.00 44.76 ? 258  ILE B C   1 
ATOM   4224 O O   . ILE B 1 258 ? -88.688  -1.730  58.887 1.00 43.86 ? 258  ILE B O   1 
ATOM   4225 C CB  . ILE B 1 258 ? -86.384  -3.949  59.248 1.00 45.15 ? 258  ILE B CB  1 
ATOM   4226 C CG1 . ILE B 1 258 ? -86.109  -5.343  59.839 1.00 43.91 ? 258  ILE B CG1 1 
ATOM   4227 C CG2 . ILE B 1 258 ? -86.296  -2.877  60.343 1.00 43.47 ? 258  ILE B CG2 1 
ATOM   4228 C CD1 . ILE B 1 258 ? -87.132  -5.806  60.865 1.00 41.28 ? 258  ILE B CD1 1 
ATOM   4229 N N   . SER B 1 259 ? -87.779  -2.199  56.886 1.00 45.06 ? 259  SER B N   1 
ATOM   4230 C CA  . SER B 1 259 ? -88.066  -0.889  56.326 1.00 46.13 ? 259  SER B CA  1 
ATOM   4231 C C   . SER B 1 259 ? -89.563  -0.766  56.082 1.00 45.64 ? 259  SER B C   1 
ATOM   4232 O O   . SER B 1 259 ? -90.173  0.252   56.399 1.00 45.03 ? 259  SER B O   1 
ATOM   4233 C CB  . SER B 1 259 ? -87.310  -0.694  55.010 1.00 47.99 ? 259  SER B CB  1 
ATOM   4234 O OG  . SER B 1 259 ? -85.919  -0.550  55.244 1.00 53.32 ? 259  SER B OG  1 
ATOM   4235 N N   . ARG B 1 260 ? -90.152  -1.811  55.515 1.00 45.65 ? 260  ARG B N   1 
ATOM   4236 C CA  . ARG B 1 260 ? -91.581  -1.814  55.248 1.00 45.59 ? 260  ARG B CA  1 
ATOM   4237 C C   . ARG B 1 260 ? -92.437  -1.828  56.512 1.00 45.07 ? 260  ARG B C   1 
ATOM   4238 O O   . ARG B 1 260 ? -93.560  -1.325  56.506 1.00 44.49 ? 260  ARG B O   1 
ATOM   4239 C CB  . ARG B 1 260 ? -91.945  -2.992  54.348 1.00 45.61 ? 260  ARG B CB  1 
ATOM   4240 C CG  . ARG B 1 260 ? -91.949  -2.597  52.894 1.00 47.91 ? 260  ARG B CG  1 
ATOM   4241 C CD  . ARG B 1 260 ? -91.023  -3.437  52.058 1.00 47.74 ? 260  ARG B CD  1 
ATOM   4242 N NE  . ARG B 1 260 ? -91.599  -4.740  51.769 1.00 49.88 ? 260  ARG B NE  1 
ATOM   4243 C CZ  . ARG B 1 260 ? -91.380  -5.406  50.643 1.00 49.12 ? 260  ARG B CZ  1 
ATOM   4244 N NH1 . ARG B 1 260 ? -90.600  -4.880  49.712 1.00 50.64 ? 260  ARG B NH1 1 
ATOM   4245 N NH2 . ARG B 1 260 ? -91.941  -6.590  50.448 1.00 48.36 ? 260  ARG B NH2 1 
ATOM   4246 N N   . ILE B 1 261 ? -91.908  -2.395  57.592 1.00 44.42 ? 261  ILE B N   1 
ATOM   4247 C CA  . ILE B 1 261 ? -92.644  -2.444  58.849 1.00 45.67 ? 261  ILE B CA  1 
ATOM   4248 C C   . ILE B 1 261 ? -92.634  -1.072  59.526 1.00 46.32 ? 261  ILE B C   1 
ATOM   4249 O O   . ILE B 1 261 ? -93.666  -0.607  60.014 1.00 46.14 ? 261  ILE B O   1 
ATOM   4250 C CB  . ILE B 1 261 ? -92.051  -3.497  59.812 1.00 44.22 ? 261  ILE B CB  1 
ATOM   4251 C CG1 . ILE B 1 261 ? -92.317  -4.904  59.266 1.00 45.02 ? 261  ILE B CG1 1 
ATOM   4252 C CG2 . ILE B 1 261 ? -92.655  -3.331  61.206 1.00 45.64 ? 261  ILE B CG2 1 
ATOM   4253 C CD1 . ILE B 1 261 ? -91.818  -6.025  60.155 1.00 43.11 ? 261  ILE B CD1 1 
ATOM   4254 N N   . ASN B 1 262 ? -91.468  -0.429  59.545 1.00 46.48 ? 262  ASN B N   1 
ATOM   4255 C CA  . ASN B 1 262 ? -91.324  0.895   60.152 1.00 46.41 ? 262  ASN B CA  1 
ATOM   4256 C C   . ASN B 1 262 ? -92.206  1.935   59.475 1.00 46.39 ? 262  ASN B C   1 
ATOM   4257 O O   . ASN B 1 262 ? -92.618  2.911   60.100 1.00 48.63 ? 262  ASN B O   1 
ATOM   4258 C CB  . ASN B 1 262 ? -89.869  1.368   60.087 1.00 45.11 ? 262  ASN B CB  1 
ATOM   4259 C CG  . ASN B 1 262 ? -88.963  0.611   61.036 1.00 44.83 ? 262  ASN B CG  1 
ATOM   4260 O OD1 . ASN B 1 262 ? -89.343  0.304   62.165 1.00 47.34 ? 262  ASN B OD1 1 
ATOM   4261 N ND2 . ASN B 1 262 ? -87.748  0.328   60.590 1.00 45.87 ? 262  ASN B ND2 1 
ATOM   4262 N N   . ASN B 1 263 ? -92.493  1.731   58.195 1.00 46.66 ? 263  ASN B N   1 
ATOM   4263 C CA  . ASN B 1 263 ? -93.323  2.666   57.440 1.00 48.49 ? 263  ASN B CA  1 
ATOM   4264 C C   . ASN B 1 263 ? -94.810  2.276   57.443 1.00 49.32 ? 263  ASN B C   1 
ATOM   4265 O O   . ASN B 1 263 ? -95.678  3.138   57.328 1.00 50.52 ? 263  ASN B O   1 
ATOM   4266 C CB  . ASN B 1 263 ? -92.825  2.756   55.991 1.00 49.32 ? 263  ASN B CB  1 
ATOM   4267 C CG  . ASN B 1 263 ? -91.396  3.287   55.887 1.00 52.22 ? 263  ASN B CG  1 
ATOM   4268 O OD1 . ASN B 1 263 ? -90.714  3.075   54.881 1.00 55.06 ? 263  ASN B OD1 1 
ATOM   4269 N ND2 . ASN B 1 263 ? -90.943  3.988   56.924 1.00 51.48 ? 263  ASN B ND2 1 
ATOM   4270 N N   . ALA B 1 264 ? -95.096  0.982   57.578 1.00 48.18 ? 264  ALA B N   1 
ATOM   4271 C CA  . ALA B 1 264 ? -96.470  0.483   57.557 1.00 46.46 ? 264  ALA B CA  1 
ATOM   4272 C C   . ALA B 1 264 ? -97.350  1.062   58.659 1.00 45.90 ? 264  ALA B C   1 
ATOM   4273 O O   . ALA B 1 264 ? -96.867  1.721   59.568 1.00 47.12 ? 264  ALA B O   1 
ATOM   4274 C CB  . ALA B 1 264 ? -96.469  -1.024  57.641 1.00 46.75 ? 264  ALA B CB  1 
ATOM   4275 N N   . CYS B 1 265 ? -98.647  0.801   58.571 1.00 44.91 ? 265  CYS B N   1 
ATOM   4276 C CA  . CYS B 1 265 ? -99.601  1.298   59.541 1.00 45.78 ? 265  CYS B CA  1 
ATOM   4277 C C   . CYS B 1 265 ? -99.956  0.285   60.632 1.00 45.90 ? 265  CYS B C   1 
ATOM   4278 O O   . CYS B 1 265 ? -101.093 0.266   61.113 1.00 45.91 ? 265  CYS B O   1 
ATOM   4279 C CB  . CYS B 1 265 ? -100.870 1.738   58.816 1.00 48.76 ? 265  CYS B CB  1 
ATOM   4280 S SG  . CYS B 1 265 ? -101.477 0.500   57.625 1.00 57.84 ? 265  CYS B SG  1 
ATOM   4281 N N   . PHE B 1 266 ? -98.996  -0.543  61.043 1.00 43.29 ? 266  PHE B N   1 
ATOM   4282 C CA  . PHE B 1 266 ? -99.255  -1.523  62.099 1.00 41.47 ? 266  PHE B CA  1 
ATOM   4283 C C   . PHE B 1 266 ? -99.197  -0.905  63.487 1.00 41.80 ? 266  PHE B C   1 
ATOM   4284 O O   . PHE B 1 266 ? -98.349  -0.061  63.763 1.00 43.69 ? 266  PHE B O   1 
ATOM   4285 C CB  . PHE B 1 266 ? -98.235  -2.672  62.071 1.00 37.91 ? 266  PHE B CB  1 
ATOM   4286 C CG  . PHE B 1 266 ? -98.265  -3.482  60.825 1.00 37.57 ? 266  PHE B CG  1 
ATOM   4287 C CD1 . PHE B 1 266 ? -97.173  -3.483  59.968 1.00 36.96 ? 266  PHE B CD1 1 
ATOM   4288 C CD2 . PHE B 1 266 ? -99.377  -4.246  60.504 1.00 35.25 ? 266  PHE B CD2 1 
ATOM   4289 C CE1 . PHE B 1 266 ? -97.187  -4.234  58.807 1.00 35.54 ? 266  PHE B CE1 1 
ATOM   4290 C CE2 . PHE B 1 266 ? -99.403  -5.001  59.347 1.00 36.79 ? 266  PHE B CE2 1 
ATOM   4291 C CZ  . PHE B 1 266 ? -98.305  -4.995  58.494 1.00 36.79 ? 266  PHE B CZ  1 
ATOM   4292 N N   . GLU B 1 267 ? -100.079 -1.340  64.378 1.00 40.80 ? 267  GLU B N   1 
ATOM   4293 C CA  . GLU B 1 267 ? -100.036 -0.851  65.748 1.00 41.34 ? 267  GLU B CA  1 
ATOM   4294 C C   . GLU B 1 267 ? -98.809  -1.568  66.323 1.00 40.53 ? 267  GLU B C   1 
ATOM   4295 O O   . GLU B 1 267 ? -98.045  -1.024  67.119 1.00 40.29 ? 267  GLU B O   1 
ATOM   4296 C CB  . GLU B 1 267 ? -101.293 -1.282  66.511 1.00 44.88 ? 267  GLU B CB  1 
ATOM   4297 C CG  . GLU B 1 267 ? -101.327 -0.806  67.949 1.00 50.59 ? 267  GLU B CG  1 
ATOM   4298 C CD  . GLU B 1 267 ? -102.105 0.491   68.126 1.00 55.00 ? 267  GLU B CD  1 
ATOM   4299 O OE1 . GLU B 1 267 ? -103.340 0.429   68.316 1.00 58.45 ? 267  GLU B OE1 1 
ATOM   4300 O OE2 . GLU B 1 267 ? -101.487 1.573   68.063 1.00 56.32 ? 267  GLU B OE2 1 
ATOM   4301 N N   . ALA B 1 268 ? -98.644  -2.812  65.890 1.00 38.49 ? 268  ALA B N   1 
ATOM   4302 C CA  . ALA B 1 268 ? -97.542  -3.661  66.320 1.00 37.72 ? 268  ALA B CA  1 
ATOM   4303 C C   . ALA B 1 268 ? -97.476  -4.930  65.477 1.00 36.71 ? 268  ALA B C   1 
ATOM   4304 O O   . ALA B 1 268 ? -98.470  -5.344  64.880 1.00 35.77 ? 268  ALA B O   1 
ATOM   4305 C CB  . ALA B 1 268 ? -97.701  -4.028  67.790 1.00 37.40 ? 268  ALA B CB  1 
ATOM   4306 N N   . VAL B 1 269 ? -96.291  -5.532  65.431 1.00 35.96 ? 269  VAL B N   1 
ATOM   4307 C CA  . VAL B 1 269 ? -96.057  -6.761  64.690 1.00 33.46 ? 269  VAL B CA  1 
ATOM   4308 C C   . VAL B 1 269 ? -95.460  -7.742  65.683 1.00 33.93 ? 269  VAL B C   1 
ATOM   4309 O O   . VAL B 1 269 ? -94.337  -7.555  66.156 1.00 34.42 ? 269  VAL B O   1 
ATOM   4310 C CB  . VAL B 1 269 ? -95.073  -6.527  63.540 1.00 32.64 ? 269  VAL B CB  1 
ATOM   4311 C CG1 . VAL B 1 269 ? -94.758  -7.843  62.862 1.00 31.77 ? 269  VAL B CG1 1 
ATOM   4312 C CG2 . VAL B 1 269 ? -95.680  -5.535  62.542 1.00 32.43 ? 269  VAL B CG2 1 
ATOM   4313 N N   . VAL B 1 270 ? -96.218  -8.786  65.999 1.00 31.86 ? 270  VAL B N   1 
ATOM   4314 C CA  . VAL B 1 270 ? -95.787  -9.774  66.974 1.00 30.12 ? 270  VAL B CA  1 
ATOM   4315 C C   . VAL B 1 270 ? -95.333  -11.094 66.358 1.00 29.27 ? 270  VAL B C   1 
ATOM   4316 O O   . VAL B 1 270 ? -95.977  -11.624 65.453 1.00 29.45 ? 270  VAL B O   1 
ATOM   4317 C CB  . VAL B 1 270 ? -96.935  -10.076 67.976 1.00 30.65 ? 270  VAL B CB  1 
ATOM   4318 C CG1 . VAL B 1 270 ? -96.404  -10.863 69.151 1.00 30.72 ? 270  VAL B CG1 1 
ATOM   4319 C CG2 . VAL B 1 270 ? -97.586  -8.772  68.448 1.00 29.91 ? 270  VAL B CG2 1 
ATOM   4320 N N   . VAL B 1 271 ? -94.221  -11.624 66.858 1.00 27.48 ? 271  VAL B N   1 
ATOM   4321 C CA  . VAL B 1 271 ? -93.703  -12.893 66.376 1.00 28.04 ? 271  VAL B CA  1 
ATOM   4322 C C   . VAL B 1 271 ? -93.108  -13.659 67.557 1.00 27.92 ? 271  VAL B C   1 
ATOM   4323 O O   . VAL B 1 271 ? -92.865  -13.073 68.607 1.00 29.88 ? 271  VAL B O   1 
ATOM   4324 C CB  . VAL B 1 271 ? -92.616  -12.675 65.297 1.00 29.41 ? 271  VAL B CB  1 
ATOM   4325 C CG1 . VAL B 1 271 ? -93.175  -11.823 64.164 1.00 28.99 ? 271  VAL B CG1 1 
ATOM   4326 C CG2 . VAL B 1 271 ? -91.397  -12.015 65.901 1.00 29.76 ? 271  VAL B CG2 1 
ATOM   4327 N N   . THR B 1 272 ? -92.914  -14.965 67.401 1.00 25.57 ? 272  THR B N   1 
ATOM   4328 C CA  . THR B 1 272 ? -92.304  -15.769 68.448 1.00 27.57 ? 272  THR B CA  1 
ATOM   4329 C C   . THR B 1 272 ? -90.804  -15.686 68.218 1.00 27.67 ? 272  THR B C   1 
ATOM   4330 O O   . THR B 1 272 ? -90.345  -15.064 67.261 1.00 27.24 ? 272  THR B O   1 
ATOM   4331 C CB  . THR B 1 272 ? -92.692  -17.256 68.357 1.00 27.02 ? 272  THR B CB  1 
ATOM   4332 O OG1 . THR B 1 272 ? -92.022  -17.854 67.239 1.00 28.14 ? 272  THR B OG1 1 
ATOM   4333 C CG2 . THR B 1 272 ? -94.189  -17.413 68.204 1.00 26.02 ? 272  THR B CG2 1 
ATOM   4334 N N   . ASN B 1 273 ? -90.027  -16.310 69.089 1.00 29.79 ? 273  ASN B N   1 
ATOM   4335 C CA  . ASN B 1 273 ? -88.591  -16.271 68.899 1.00 32.37 ? 273  ASN B CA  1 
ATOM   4336 C C   . ASN B 1 273 ? -88.076  -17.553 68.260 1.00 33.17 ? 273  ASN B C   1 
ATOM   4337 O O   . ASN B 1 273 ? -86.978  -18.002 68.567 1.00 35.41 ? 273  ASN B O   1 
ATOM   4338 C CB  . ASN B 1 273 ? -87.865  -15.998 70.228 1.00 32.19 ? 273  ASN B CB  1 
ATOM   4339 C CG  . ASN B 1 273 ? -88.280  -16.946 71.333 1.00 33.45 ? 273  ASN B CG  1 
ATOM   4340 O OD1 . ASN B 1 273 ? -89.224  -17.724 71.189 1.00 35.76 ? 273  ASN B OD1 1 
ATOM   4341 N ND2 . ASN B 1 273 ? -87.582  -16.875 72.455 1.00 33.43 ? 273  ASN B ND2 1 
ATOM   4342 N N   . THR B 1 274 ? -88.864  -18.152 67.369 1.00 33.49 ? 274  THR B N   1 
ATOM   4343 C CA  . THR B 1 274 ? -88.413  -19.364 66.693 1.00 33.04 ? 274  THR B CA  1 
ATOM   4344 C C   . THR B 1 274 ? -87.179  -18.988 65.877 1.00 33.95 ? 274  THR B C   1 
ATOM   4345 O O   . THR B 1 274 ? -86.367  -19.838 65.528 1.00 31.15 ? 274  THR B O   1 
ATOM   4346 C CB  . THR B 1 274 ? -89.501  -19.955 65.767 1.00 32.69 ? 274  THR B CB  1 
ATOM   4347 O OG1 . THR B 1 274 ? -90.048  -18.935 64.916 1.00 32.38 ? 274  THR B OG1 1 
ATOM   4348 C CG2 . THR B 1 274 ? -90.592  -20.586 66.596 1.00 31.27 ? 274  THR B CG2 1 
ATOM   4349 N N   . ILE B 1 275 ? -87.066  -17.690 65.591 1.00 34.57 ? 275  ILE B N   1 
ATOM   4350 C CA  . ILE B 1 275 ? -85.956  -17.099 64.853 1.00 34.77 ? 275  ILE B CA  1 
ATOM   4351 C C   . ILE B 1 275 ? -85.453  -15.917 65.699 1.00 34.89 ? 275  ILE B C   1 
ATOM   4352 O O   . ILE B 1 275 ? -86.249  -15.174 66.262 1.00 33.47 ? 275  ILE B O   1 
ATOM   4353 C CB  . ILE B 1 275 ? -86.429  -16.615 63.447 1.00 33.21 ? 275  ILE B CB  1 
ATOM   4354 C CG1 . ILE B 1 275 ? -86.776  -17.827 62.577 1.00 34.60 ? 275  ILE B CG1 1 
ATOM   4355 C CG2 . ILE B 1 275 ? -85.330  -15.835 62.748 1.00 35.74 ? 275  ILE B CG2 1 
ATOM   4356 C CD1 . ILE B 1 275 ? -87.342  -17.467 61.221 1.00 31.13 ? 275  ILE B CD1 1 
ATOM   4357 N N   . PRO B 1 276 ? -84.125  -15.765 65.844 1.00 36.61 ? 276  PRO B N   1 
ATOM   4358 C CA  . PRO B 1 276 ? -83.560  -14.662 66.636 1.00 37.89 ? 276  PRO B CA  1 
ATOM   4359 C C   . PRO B 1 276 ? -84.149  -13.339 66.165 1.00 38.91 ? 276  PRO B C   1 
ATOM   4360 O O   . PRO B 1 276 ? -84.189  -13.065 64.964 1.00 38.07 ? 276  PRO B O   1 
ATOM   4361 C CB  . PRO B 1 276 ? -82.060  -14.782 66.372 1.00 36.61 ? 276  PRO B CB  1 
ATOM   4362 C CG  . PRO B 1 276 ? -82.012  -15.412 65.006 1.00 39.26 ? 276  PRO B CG  1 
ATOM   4363 C CD  . PRO B 1 276 ? -83.070  -16.467 65.100 1.00 36.70 ? 276  PRO B CD  1 
ATOM   4364 N N   . GLN B 1 277 ? -84.610  -12.525 67.109 1.00 41.24 ? 277  GLN B N   1 
ATOM   4365 C CA  . GLN B 1 277 ? -85.247  -11.257 66.767 1.00 44.18 ? 277  GLN B CA  1 
ATOM   4366 C C   . GLN B 1 277 ? -84.553  -10.007 67.327 1.00 46.87 ? 277  GLN B C   1 
ATOM   4367 O O   . GLN B 1 277 ? -84.887  -8.880  66.955 1.00 46.81 ? 277  GLN B O   1 
ATOM   4368 C CB  . GLN B 1 277 ? -86.702  -11.307 67.244 1.00 42.64 ? 277  GLN B CB  1 
ATOM   4369 C CG  . GLN B 1 277 ? -87.742  -10.977 66.196 1.00 45.10 ? 277  GLN B CG  1 
ATOM   4370 C CD  . GLN B 1 277 ? -87.677  -11.871 64.966 1.00 44.61 ? 277  GLN B CD  1 
ATOM   4371 O OE1 . GLN B 1 277 ? -87.796  -13.098 65.050 1.00 42.97 ? 277  GLN B OE1 1 
ATOM   4372 N NE2 . GLN B 1 277 ? -87.498  -11.251 63.810 1.00 45.02 ? 277  GLN B NE2 1 
ATOM   4373 N N   . GLU B 1 278 ? -83.584  -10.210 68.213 1.00 51.31 ? 278  GLU B N   1 
ATOM   4374 C CA  . GLU B 1 278 ? -82.863  -9.103  68.847 1.00 54.93 ? 278  GLU B CA  1 
ATOM   4375 C C   . GLU B 1 278 ? -82.344  -7.998  67.917 1.00 56.05 ? 278  GLU B C   1 
ATOM   4376 O O   . GLU B 1 278 ? -82.656  -6.820  68.116 1.00 55.54 ? 278  GLU B O   1 
ATOM   4377 C CB  . GLU B 1 278 ? -81.708  -9.656  69.691 1.00 57.62 ? 278  GLU B CB  1 
ATOM   4378 C CG  . GLU B 1 278 ? -82.129  -10.228 71.050 1.00 62.72 ? 278  GLU B CG  1 
ATOM   4379 C CD  . GLU B 1 278 ? -83.109  -11.403 70.963 1.00 66.54 ? 278  GLU B CD  1 
ATOM   4380 O OE1 . GLU B 1 278 ? -82.725  -12.485 70.462 1.00 66.80 ? 278  GLU B OE1 1 
ATOM   4381 O OE2 . GLU B 1 278 ? -84.270  -11.244 71.408 1.00 67.90 ? 278  GLU B OE2 1 
ATOM   4382 N N   . ASP B 1 279 ? -81.557  -8.366  66.909 1.00 56.86 ? 279  ASP B N   1 
ATOM   4383 C CA  . ASP B 1 279 ? -81.003  -7.378  65.983 1.00 57.46 ? 279  ASP B CA  1 
ATOM   4384 C C   . ASP B 1 279 ? -82.092  -6.624  65.221 1.00 56.75 ? 279  ASP B C   1 
ATOM   4385 O O   . ASP B 1 279 ? -81.985  -5.418  65.004 1.00 56.66 ? 279  ASP B O   1 
ATOM   4386 C CB  . ASP B 1 279 ? -80.053  -8.050  64.985 1.00 60.13 ? 279  ASP B CB  1 
ATOM   4387 C CG  . ASP B 1 279 ? -79.067  -8.991  65.657 1.00 63.28 ? 279  ASP B CG  1 
ATOM   4388 O OD1 . ASP B 1 279 ? -79.469  -10.127 66.003 1.00 65.68 ? 279  ASP B OD1 1 
ATOM   4389 O OD2 . ASP B 1 279 ? -77.895  -8.594  65.845 1.00 64.34 ? 279  ASP B OD2 1 
ATOM   4390 N N   . LYS B 1 280 ? -83.133  -7.344  64.811 1.00 55.57 ? 280  LYS B N   1 
ATOM   4391 C CA  . LYS B 1 280 ? -84.254  -6.754  64.081 1.00 53.80 ? 280  LYS B CA  1 
ATOM   4392 C C   . LYS B 1 280 ? -84.999  -5.743  64.952 1.00 53.01 ? 280  LYS B C   1 
ATOM   4393 O O   . LYS B 1 280 ? -85.459  -4.713  64.466 1.00 51.48 ? 280  LYS B O   1 
ATOM   4394 C CB  . LYS B 1 280 ? -85.231  -7.849  63.637 1.00 52.20 ? 280  LYS B CB  1 
ATOM   4395 C CG  . LYS B 1 280 ? -84.625  -8.904  62.720 1.00 52.25 ? 280  LYS B CG  1 
ATOM   4396 C CD  . LYS B 1 280 ? -84.243  -8.324  61.367 1.00 51.60 ? 280  LYS B CD  1 
ATOM   4397 C CE  . LYS B 1 280 ? -83.499  -9.338  60.506 1.00 50.98 ? 280  LYS B CE  1 
ATOM   4398 N NZ  . LYS B 1 280 ? -84.302  -10.552 60.188 1.00 51.96 ? 280  LYS B NZ  1 
ATOM   4399 N N   . MET B 1 281 ? -85.125  -6.045  66.241 1.00 52.96 ? 281  MET B N   1 
ATOM   4400 C CA  . MET B 1 281 ? -85.822  -5.153  67.160 1.00 53.57 ? 281  MET B CA  1 
ATOM   4401 C C   . MET B 1 281 ? -85.096  -3.815  67.315 1.00 54.11 ? 281  MET B C   1 
ATOM   4402 O O   . MET B 1 281 ? -85.732  -2.772  67.461 1.00 53.45 ? 281  MET B O   1 
ATOM   4403 C CB  . MET B 1 281 ? -86.001  -5.839  68.521 1.00 52.53 ? 281  MET B CB  1 
ATOM   4404 C CG  . MET B 1 281 ? -86.918  -7.056  68.453 1.00 52.99 ? 281  MET B CG  1 
ATOM   4405 S SD  . MET B 1 281 ? -87.182  -7.941  70.006 1.00 53.40 ? 281  MET B SD  1 
ATOM   4406 C CE  . MET B 1 281 ? -88.507  -6.988  70.706 1.00 51.43 ? 281  MET B CE  1 
ATOM   4407 N N   . LYS B 1 282 ? -83.767  -3.846  67.263 1.00 54.53 ? 282  LYS B N   1 
ATOM   4408 C CA  . LYS B 1 282 ? -82.971  -2.627  67.387 1.00 54.98 ? 282  LYS B CA  1 
ATOM   4409 C C   . LYS B 1 282 ? -83.321  -1.620  66.292 1.00 54.90 ? 282  LYS B C   1 
ATOM   4410 O O   . LYS B 1 282 ? -83.209  -0.416  66.496 1.00 54.91 ? 282  LYS B O   1 
ATOM   4411 C CB  . LYS B 1 282 ? -81.472  -2.952  67.316 1.00 56.37 ? 282  LYS B CB  1 
ATOM   4412 C CG  . LYS B 1 282 ? -80.924  -3.720  68.516 1.00 58.49 ? 282  LYS B CG  1 
ATOM   4413 C CD  . LYS B 1 282 ? -79.473  -4.165  68.305 1.00 59.91 ? 282  LYS B CD  1 
ATOM   4414 C CE  . LYS B 1 282 ? -78.501  -2.989  68.232 1.00 61.78 ? 282  LYS B CE  1 
ATOM   4415 N NZ  . LYS B 1 282 ? -78.703  -2.096  67.050 1.00 62.22 ? 282  LYS B NZ  1 
ATOM   4416 N N   . HIS B 1 283 ? -83.746  -2.111  65.132 1.00 54.38 ? 283  HIS B N   1 
ATOM   4417 C CA  . HIS B 1 283 ? -84.095  -1.231  64.020 1.00 53.41 ? 283  HIS B CA  1 
ATOM   4418 C C   . HIS B 1 283 ? -85.598  -1.168  63.768 1.00 52.54 ? 283  HIS B C   1 
ATOM   4419 O O   . HIS B 1 283 ? -86.054  -0.494  62.843 1.00 52.24 ? 283  HIS B O   1 
ATOM   4420 C CB  . HIS B 1 283 ? -83.384  -1.699  62.751 1.00 56.43 ? 283  HIS B CB  1 
ATOM   4421 C CG  . HIS B 1 283 ? -81.894  -1.751  62.884 1.00 57.57 ? 283  HIS B CG  1 
ATOM   4422 N ND1 . HIS B 1 283 ? -81.131  -0.632  63.131 1.00 56.97 ? 283  HIS B ND1 1 
ATOM   4423 C CD2 . HIS B 1 283 ? -81.028  -2.793  62.831 1.00 58.18 ? 283  HIS B CD2 1 
ATOM   4424 C CE1 . HIS B 1 283 ? -79.859  -0.979  63.227 1.00 58.43 ? 283  HIS B CE1 1 
ATOM   4425 N NE2 . HIS B 1 283 ? -79.771  -2.285  63.050 1.00 59.08 ? 283  HIS B NE2 1 
ATOM   4426 N N   . CYS B 1 284 ? -86.369  -1.870  64.591 1.00 51.02 ? 284  CYS B N   1 
ATOM   4427 C CA  . CYS B 1 284 ? -87.815  -1.890  64.434 1.00 49.91 ? 284  CYS B CA  1 
ATOM   4428 C C   . CYS B 1 284 ? -88.470  -1.975  65.805 1.00 49.39 ? 284  CYS B C   1 
ATOM   4429 O O   . CYS B 1 284 ? -88.389  -2.998  66.480 1.00 49.79 ? 284  CYS B O   1 
ATOM   4430 C CB  . CYS B 1 284 ? -88.230  -3.091  63.578 1.00 48.95 ? 284  CYS B CB  1 
ATOM   4431 S SG  . CYS B 1 284 ? -89.926  -3.001  62.986 1.00 46.33 ? 284  CYS B SG  1 
ATOM   4432 N N   . SER B 1 285 ? -89.119  -0.892  66.210 1.00 48.42 ? 285  SER B N   1 
ATOM   4433 C CA  . SER B 1 285 ? -89.775  -0.829  67.512 1.00 47.78 ? 285  SER B CA  1 
ATOM   4434 C C   . SER B 1 285 ? -91.218  -1.334  67.543 1.00 45.48 ? 285  SER B C   1 
ATOM   4435 O O   . SER B 1 285 ? -91.786  -1.527  68.619 1.00 44.06 ? 285  SER B O   1 
ATOM   4436 C CB  . SER B 1 285 ? -89.715  0.603   68.044 1.00 48.88 ? 285  SER B CB  1 
ATOM   4437 O OG  . SER B 1 285 ? -90.045  1.525   67.021 1.00 51.90 ? 285  SER B OG  1 
ATOM   4438 N N   . LYS B 1 286 ? -91.810  -1.552  66.373 1.00 43.91 ? 286  LYS B N   1 
ATOM   4439 C CA  . LYS B 1 286 ? -93.181  -2.063  66.297 1.00 42.85 ? 286  LYS B CA  1 
ATOM   4440 C C   . LYS B 1 286 ? -93.201  -3.554  66.635 1.00 40.84 ? 286  LYS B C   1 
ATOM   4441 O O   . LYS B 1 286 ? -94.252  -4.136  66.921 1.00 41.96 ? 286  LYS B O   1 
ATOM   4442 C CB  . LYS B 1 286 ? -93.736  -1.880  64.892 1.00 42.98 ? 286  LYS B CB  1 
ATOM   4443 C CG  . LYS B 1 286 ? -94.032  -0.455  64.520 1.00 44.84 ? 286  LYS B CG  1 
ATOM   4444 C CD  . LYS B 1 286 ? -94.579  -0.423  63.112 1.00 46.33 ? 286  LYS B CD  1 
ATOM   4445 C CE  . LYS B 1 286 ? -95.199  0.914   62.780 1.00 48.88 ? 286  LYS B CE  1 
ATOM   4446 N NZ  . LYS B 1 286 ? -95.647  0.895   61.362 1.00 50.57 ? 286  LYS B NZ  1 
ATOM   4447 N N   . ILE B 1 287 ? -92.021  -4.156  66.593 1.00 39.73 ? 287  ILE B N   1 
ATOM   4448 C CA  . ILE B 1 287 ? -91.851  -5.568  66.850 1.00 37.73 ? 287  ILE B CA  1 
ATOM   4449 C C   . ILE B 1 287 ? -91.803  -5.943  68.321 1.00 37.46 ? 287  ILE B C   1 
ATOM   4450 O O   . ILE B 1 287 ? -91.094  -5.339  69.127 1.00 37.87 ? 287  ILE B O   1 
ATOM   4451 C CB  . ILE B 1 287 ? -90.567  -6.092  66.154 1.00 37.58 ? 287  ILE B CB  1 
ATOM   4452 C CG1 . ILE B 1 287 ? -90.711  -5.964  64.638 1.00 36.11 ? 287  ILE B CG1 1 
ATOM   4453 C CG2 . ILE B 1 287 ? -90.302  -7.538  66.544 1.00 34.74 ? 287  ILE B CG2 1 
ATOM   4454 C CD1 . ILE B 1 287 ? -89.469  -6.344  63.860 1.00 37.81 ? 287  ILE B CD1 1 
ATOM   4455 N N   . GLN B 1 288 ? -92.592  -6.954  68.650 1.00 36.07 ? 288  GLN B N   1 
ATOM   4456 C CA  . GLN B 1 288 ? -92.670  -7.499  69.988 1.00 33.62 ? 288  GLN B CA  1 
ATOM   4457 C C   . GLN B 1 288 ? -92.536  -8.997  69.804 1.00 33.15 ? 288  GLN B C   1 
ATOM   4458 O O   . GLN B 1 288 ? -93.023  -9.549  68.815 1.00 30.95 ? 288  GLN B O   1 
ATOM   4459 C CB  . GLN B 1 288 ? -94.011  -7.153  70.635 1.00 33.17 ? 288  GLN B CB  1 
ATOM   4460 C CG  . GLN B 1 288 ? -94.156  -5.669  70.911 1.00 31.77 ? 288  GLN B CG  1 
ATOM   4461 C CD  . GLN B 1 288 ? -95.440  -5.348  71.607 1.00 30.75 ? 288  GLN B CD  1 
ATOM   4462 O OE1 . GLN B 1 288 ? -96.114  -4.385  71.265 1.00 32.85 ? 288  GLN B OE1 1 
ATOM   4463 N NE2 . GLN B 1 288 ? -95.788  -6.148  72.606 1.00 32.68 ? 288  GLN B NE2 1 
ATOM   4464 N N   . VAL B 1 289 ? -91.868  -9.647  70.750 1.00 32.67 ? 289  VAL B N   1 
ATOM   4465 C CA  . VAL B 1 289 ? -91.625  -11.078 70.681 1.00 32.43 ? 289  VAL B CA  1 
ATOM   4466 C C   . VAL B 1 289 ? -92.277  -11.904 71.773 1.00 32.46 ? 289  VAL B C   1 
ATOM   4467 O O   . VAL B 1 289 ? -92.271  -11.518 72.938 1.00 33.46 ? 289  VAL B O   1 
ATOM   4468 C CB  . VAL B 1 289 ? -90.109  -11.368 70.739 1.00 33.71 ? 289  VAL B CB  1 
ATOM   4469 C CG1 . VAL B 1 289 ? -89.864  -12.868 70.735 1.00 32.66 ? 289  VAL B CG1 1 
ATOM   4470 C CG2 . VAL B 1 289 ? -89.408  -10.702 69.563 1.00 34.39 ? 289  VAL B CG2 1 
ATOM   4471 N N   . ILE B 1 290 ? -92.839  -13.045 71.387 1.00 31.24 ? 290  ILE B N   1 
ATOM   4472 C CA  . ILE B 1 290 ? -93.433  -13.964 72.345 1.00 30.89 ? 290  ILE B CA  1 
ATOM   4473 C C   . ILE B 1 290 ? -92.374  -15.047 72.512 1.00 30.92 ? 290  ILE B C   1 
ATOM   4474 O O   . ILE B 1 290 ? -91.962  -15.661 71.533 1.00 30.11 ? 290  ILE B O   1 
ATOM   4475 C CB  . ILE B 1 290 ? -94.709  -14.642 71.804 1.00 31.49 ? 290  ILE B CB  1 
ATOM   4476 C CG1 . ILE B 1 290 ? -95.844  -13.628 71.677 1.00 29.61 ? 290  ILE B CG1 1 
ATOM   4477 C CG2 . ILE B 1 290 ? -95.129  -15.783 72.744 1.00 30.13 ? 290  ILE B CG2 1 
ATOM   4478 C CD1 . ILE B 1 290 ? -97.098  -14.235 71.118 1.00 27.49 ? 290  ILE B CD1 1 
ATOM   4479 N N   . ASP B 1 291 ? -91.918  -15.271 73.738 1.00 32.67 ? 291  ASP B N   1 
ATOM   4480 C CA  . ASP B 1 291 ? -90.902  -16.294 73.986 1.00 32.60 ? 291  ASP B CA  1 
ATOM   4481 C C   . ASP B 1 291 ? -91.542  -17.675 73.987 1.00 32.50 ? 291  ASP B C   1 
ATOM   4482 O O   . ASP B 1 291 ? -92.435  -17.941 74.782 1.00 32.83 ? 291  ASP B O   1 
ATOM   4483 C CB  . ASP B 1 291 ? -90.213  -16.033 75.326 1.00 34.62 ? 291  ASP B CB  1 
ATOM   4484 C CG  . ASP B 1 291 ? -89.267  -17.158 75.731 1.00 37.79 ? 291  ASP B CG  1 
ATOM   4485 O OD1 . ASP B 1 291 ? -88.657  -17.783 74.840 1.00 37.16 ? 291  ASP B OD1 1 
ATOM   4486 O OD2 . ASP B 1 291 ? -89.125  -17.405 76.948 1.00 40.17 ? 291  ASP B OD2 1 
ATOM   4487 N N   . ILE B 1 292 ? -91.104  -18.549 73.086 1.00 30.84 ? 292  ILE B N   1 
ATOM   4488 C CA  . ILE B 1 292 ? -91.670  -19.891 73.029 1.00 30.87 ? 292  ILE B CA  1 
ATOM   4489 C C   . ILE B 1 292 ? -90.701  -20.976 73.531 1.00 31.25 ? 292  ILE B C   1 
ATOM   4490 O O   . ILE B 1 292 ? -90.937  -22.172 73.347 1.00 29.54 ? 292  ILE B O   1 
ATOM   4491 C CB  . ILE B 1 292 ? -92.174  -20.240 71.594 1.00 30.96 ? 292  ILE B CB  1 
ATOM   4492 C CG1 . ILE B 1 292 ? -91.103  -19.940 70.538 1.00 29.49 ? 292  ILE B CG1 1 
ATOM   4493 C CG2 . ILE B 1 292 ? -93.431  -19.442 71.293 1.00 33.44 ? 292  ILE B CG2 1 
ATOM   4494 C CD1 . ILE B 1 292 ? -89.911  -20.856 70.584 1.00 27.13 ? 292  ILE B CD1 1 
ATOM   4495 N N   . SER B 1 293 ? -89.629  -20.552 74.191 1.00 29.73 ? 293  SER B N   1 
ATOM   4496 C CA  . SER B 1 293 ? -88.651  -21.492 74.716 1.00 31.27 ? 293  SER B CA  1 
ATOM   4497 C C   . SER B 1 293 ? -89.258  -22.492 75.704 1.00 33.44 ? 293  SER B C   1 
ATOM   4498 O O   . SER B 1 293 ? -88.885  -23.674 75.707 1.00 30.90 ? 293  SER B O   1 
ATOM   4499 C CB  . SER B 1 293 ? -87.494  -20.736 75.374 1.00 31.63 ? 293  SER B CB  1 
ATOM   4500 O OG  . SER B 1 293 ? -87.950  -19.773 76.309 1.00 29.11 ? 293  SER B OG  1 
ATOM   4501 N N   . MET B 1 294 ? -90.197  -22.036 76.532 1.00 33.20 ? 294  MET B N   1 
ATOM   4502 C CA  . MET B 1 294 ? -90.813  -22.935 77.504 1.00 35.74 ? 294  MET B CA  1 
ATOM   4503 C C   . MET B 1 294 ? -91.607  -24.036 76.826 1.00 32.55 ? 294  MET B C   1 
ATOM   4504 O O   . MET B 1 294 ? -91.671  -25.154 77.325 1.00 33.66 ? 294  MET B O   1 
ATOM   4505 C CB  . MET B 1 294 ? -91.713  -22.169 78.493 1.00 39.59 ? 294  MET B CB  1 
ATOM   4506 C CG  . MET B 1 294 ? -91.960  -20.705 78.151 1.00 50.16 ? 294  MET B CG  1 
ATOM   4507 S SD  . MET B 1 294 ? -93.496  -20.421 77.248 1.00 57.80 ? 294  MET B SD  1 
ATOM   4508 C CE  . MET B 1 294 ? -92.988  -20.792 75.644 1.00 53.09 ? 294  MET B CE  1 
ATOM   4509 N N   . ILE B 1 295 ? -92.216  -23.716 75.691 1.00 32.01 ? 295  ILE B N   1 
ATOM   4510 C CA  . ILE B 1 295 ? -92.986  -24.698 74.942 1.00 29.93 ? 295  ILE B CA  1 
ATOM   4511 C C   . ILE B 1 295 ? -92.038  -25.721 74.324 1.00 29.04 ? 295  ILE B C   1 
ATOM   4512 O O   . ILE B 1 295 ? -92.302  -26.922 74.365 1.00 31.85 ? 295  ILE B O   1 
ATOM   4513 C CB  . ILE B 1 295 ? -93.813  -24.027 73.826 1.00 31.21 ? 295  ILE B CB  1 
ATOM   4514 C CG1 . ILE B 1 295 ? -94.826  -23.057 74.448 1.00 32.36 ? 295  ILE B CG1 1 
ATOM   4515 C CG2 . ILE B 1 295 ? -94.536  -25.089 73.004 1.00 28.59 ? 295  ILE B CG2 1 
ATOM   4516 C CD1 . ILE B 1 295 ? -95.551  -22.183 73.436 1.00 35.24 ? 295  ILE B CD1 1 
ATOM   4517 N N   . LEU B 1 296 ? -90.935  -25.254 73.742 1.00 26.85 ? 296  LEU B N   1 
ATOM   4518 C CA  . LEU B 1 296 ? -89.972  -26.181 73.158 1.00 27.29 ? 296  LEU B CA  1 
ATOM   4519 C C   . LEU B 1 296 ? -89.325  -27.006 74.280 1.00 27.05 ? 296  LEU B C   1 
ATOM   4520 O O   . LEU B 1 296 ? -89.206  -28.232 74.174 1.00 26.56 ? 296  LEU B O   1 
ATOM   4521 C CB  . LEU B 1 296 ? -88.910  -25.423 72.350 1.00 23.95 ? 296  LEU B CB  1 
ATOM   4522 C CG  . LEU B 1 296 ? -89.414  -24.799 71.039 1.00 25.58 ? 296  LEU B CG  1 
ATOM   4523 C CD1 . LEU B 1 296 ? -88.295  -24.022 70.380 1.00 23.17 ? 296  LEU B CD1 1 
ATOM   4524 C CD2 . LEU B 1 296 ? -89.917  -25.896 70.095 1.00 23.38 ? 296  LEU B CD2 1 
ATOM   4525 N N   . ALA B 1 297 ? -88.941  -26.331 75.363 1.00 26.52 ? 297  ALA B N   1 
ATOM   4526 C CA  . ALA B 1 297 ? -88.334  -26.998 76.519 1.00 29.25 ? 297  ALA B CA  1 
ATOM   4527 C C   . ALA B 1 297 ? -89.256  -28.097 77.048 1.00 29.26 ? 297  ALA B C   1 
ATOM   4528 O O   . ALA B 1 297 ? -88.829  -29.221 77.281 1.00 28.88 ? 297  ALA B O   1 
ATOM   4529 C CB  . ALA B 1 297 ? -88.049  -25.980 77.623 1.00 27.19 ? 297  ALA B CB  1 
ATOM   4530 N N   . GLU B 1 298 ? -90.526  -27.761 77.232 1.00 29.78 ? 298  GLU B N   1 
ATOM   4531 C CA  . GLU B 1 298 ? -91.513  -28.711 77.727 1.00 32.10 ? 298  GLU B CA  1 
ATOM   4532 C C   . GLU B 1 298 ? -91.715  -29.898 76.771 1.00 32.86 ? 298  GLU B C   1 
ATOM   4533 O O   . GLU B 1 298 ? -91.773  -31.048 77.206 1.00 32.38 ? 298  GLU B O   1 
ATOM   4534 C CB  . GLU B 1 298 ? -92.849  -27.994 77.950 1.00 36.69 ? 298  GLU B CB  1 
ATOM   4535 C CG  . GLU B 1 298 ? -93.932  -28.877 78.525 1.00 41.45 ? 298  GLU B CG  1 
ATOM   4536 C CD  . GLU B 1 298 ? -93.862  -28.977 80.039 1.00 45.73 ? 298  GLU B CD  1 
ATOM   4537 O OE1 . GLU B 1 298 ? -92.752  -29.138 80.589 1.00 44.95 ? 298  GLU B OE1 1 
ATOM   4538 O OE2 . GLU B 1 298 ? -94.931  -28.902 80.681 1.00 50.00 ? 298  GLU B OE2 1 
ATOM   4539 N N   . ALA B 1 299 ? -91.837  -29.624 75.472 1.00 30.51 ? 299  ALA B N   1 
ATOM   4540 C CA  . ALA B 1 299 ? -92.015  -30.706 74.503 1.00 28.42 ? 299  ALA B CA  1 
ATOM   4541 C C   . ALA B 1 299 ? -90.833  -31.676 74.575 1.00 26.91 ? 299  ALA B C   1 
ATOM   4542 O O   . ALA B 1 299 ? -91.005  -32.892 74.471 1.00 27.24 ? 299  ALA B O   1 
ATOM   4543 C CB  . ALA B 1 299 ? -92.147  -30.142 73.087 1.00 25.54 ? 299  ALA B CB  1 
ATOM   4544 N N   . ILE B 1 300 ? -89.636  -31.131 74.754 1.00 26.06 ? 300  ILE B N   1 
ATOM   4545 C CA  . ILE B 1 300 ? -88.428  -31.946 74.848 1.00 28.32 ? 300  ILE B CA  1 
ATOM   4546 C C   . ILE B 1 300 ? -88.452  -32.807 76.104 1.00 29.47 ? 300  ILE B C   1 
ATOM   4547 O O   . ILE B 1 300 ? -88.153  -33.998 76.050 1.00 29.93 ? 300  ILE B O   1 
ATOM   4548 C CB  . ILE B 1 300 ? -87.151  -31.065 74.854 1.00 24.51 ? 300  ILE B CB  1 
ATOM   4549 C CG1 . ILE B 1 300 ? -86.902  -30.498 73.450 1.00 23.55 ? 300  ILE B CG1 1 
ATOM   4550 C CG2 . ILE B 1 300 ? -85.957  -31.884 75.327 1.00 24.36 ? 300  ILE B CG2 1 
ATOM   4551 C CD1 . ILE B 1 300 ? -85.893  -29.329 73.412 1.00 23.47 ? 300  ILE B CD1 1 
ATOM   4552 N N   . ARG B 1 301 ? -88.814  -32.205 77.233 1.00 33.55 ? 301  ARG B N   1 
ATOM   4553 C CA  . ARG B 1 301 ? -88.885  -32.940 78.491 1.00 35.95 ? 301  ARG B CA  1 
ATOM   4554 C C   . ARG B 1 301 ? -89.963  -34.021 78.433 1.00 37.06 ? 301  ARG B C   1 
ATOM   4555 O O   . ARG B 1 301 ? -89.779  -35.115 78.967 1.00 36.26 ? 301  ARG B O   1 
ATOM   4556 C CB  . ARG B 1 301 ? -89.170  -31.988 79.654 1.00 40.71 ? 301  ARG B CB  1 
ATOM   4557 C CG  . ARG B 1 301 ? -89.438  -32.701 80.979 1.00 45.64 ? 301  ARG B CG  1 
ATOM   4558 C CD  . ARG B 1 301 ? -89.737  -31.728 82.114 1.00 49.04 ? 301  ARG B CD  1 
ATOM   4559 N NE  . ARG B 1 301 ? -90.768  -32.273 82.999 1.00 53.66 ? 301  ARG B NE  1 
ATOM   4560 C CZ  . ARG B 1 301 ? -92.077  -32.159 82.785 1.00 54.75 ? 301  ARG B CZ  1 
ATOM   4561 N NH1 . ARG B 1 301 ? -92.524  -31.508 81.720 1.00 57.31 ? 301  ARG B NH1 1 
ATOM   4562 N NH2 . ARG B 1 301 ? -92.943  -32.714 83.622 1.00 57.71 ? 301  ARG B NH2 1 
ATOM   4563 N N   . ARG B 1 302 ? -91.083  -33.722 77.782 1.00 38.37 ? 302  ARG B N   1 
ATOM   4564 C CA  . ARG B 1 302 ? -92.165  -34.699 77.665 1.00 40.21 ? 302  ARG B CA  1 
ATOM   4565 C C   . ARG B 1 302 ? -91.717  -35.857 76.778 1.00 40.12 ? 302  ARG B C   1 
ATOM   4566 O O   . ARG B 1 302 ? -91.917  -37.024 77.117 1.00 42.26 ? 302  ARG B O   1 
ATOM   4567 C CB  . ARG B 1 302 ? -93.421  -34.070 77.051 1.00 42.19 ? 302  ARG B CB  1 
ATOM   4568 C CG  . ARG B 1 302 ? -93.902  -32.775 77.689 1.00 46.91 ? 302  ARG B CG  1 
ATOM   4569 C CD  . ARG B 1 302 ? -94.174  -32.891 79.177 1.00 48.26 ? 302  ARG B CD  1 
ATOM   4570 N NE  . ARG B 1 302 ? -94.862  -31.698 79.677 1.00 50.71 ? 302  ARG B NE  1 
ATOM   4571 C CZ  . ARG B 1 302 ? -96.185  -31.546 79.710 1.00 51.71 ? 302  ARG B CZ  1 
ATOM   4572 N NH1 . ARG B 1 302 ? -96.990  -32.510 79.280 1.00 48.90 ? 302  ARG B NH1 1 
ATOM   4573 N NH2 . ARG B 1 302 ? -96.709  -30.418 80.169 1.00 52.24 ? 302  ARG B NH2 1 
ATOM   4574 N N   . THR B 1 303 ? -91.113  -35.525 75.641 1.00 37.57 ? 303  THR B N   1 
ATOM   4575 C CA  . THR B 1 303 ? -90.628  -36.528 74.698 1.00 37.14 ? 303  THR B CA  1 
ATOM   4576 C C   . THR B 1 303 ? -89.686  -37.481 75.407 1.00 36.09 ? 303  THR B C   1 
ATOM   4577 O O   . THR B 1 303 ? -89.759  -38.697 75.231 1.00 34.69 ? 303  THR B O   1 
ATOM   4578 C CB  . THR B 1 303 ? -89.830  -35.893 73.550 1.00 36.54 ? 303  THR B CB  1 
ATOM   4579 O OG1 . THR B 1 303 ? -90.634  -34.920 72.884 1.00 40.45 ? 303  THR B OG1 1 
ATOM   4580 C CG2 . THR B 1 303 ? -89.410  -36.947 72.564 1.00 39.41 ? 303  THR B CG2 1 
ATOM   4581 N N   . HIS B 1 304 ? -88.785  -36.908 76.196 1.00 35.52 ? 304  HIS B N   1 
ATOM   4582 C CA  . HIS B 1 304 ? -87.807  -37.688 76.933 1.00 36.44 ? 304  HIS B CA  1 
ATOM   4583 C C   . HIS B 1 304 ? -88.463  -38.611 77.949 1.00 38.29 ? 304  HIS B C   1 
ATOM   4584 O O   . HIS B 1 304 ? -88.107  -39.784 78.042 1.00 37.91 ? 304  HIS B O   1 
ATOM   4585 C CB  . HIS B 1 304 ? -86.833  -36.762 77.649 1.00 34.75 ? 304  HIS B CB  1 
ATOM   4586 C CG  . HIS B 1 304 ? -85.760  -37.488 78.398 1.00 37.55 ? 304  HIS B CG  1 
ATOM   4587 N ND1 . HIS B 1 304 ? -84.740  -38.162 77.767 1.00 36.95 ? 304  HIS B ND1 1 
ATOM   4588 C CD2 . HIS B 1 304 ? -85.568  -37.667 79.726 1.00 34.53 ? 304  HIS B CD2 1 
ATOM   4589 C CE1 . HIS B 1 304 ? -83.961  -38.727 78.674 1.00 37.37 ? 304  HIS B CE1 1 
ATOM   4590 N NE2 . HIS B 1 304 ? -84.442  -38.442 79.869 1.00 35.58 ? 304  HIS B NE2 1 
ATOM   4591 N N   . ASN B 1 305 ? -89.426  -38.083 78.702 1.00 41.22 ? 305  ASN B N   1 
ATOM   4592 C CA  . ASN B 1 305 ? -90.111  -38.872 79.728 1.00 42.85 ? 305  ASN B CA  1 
ATOM   4593 C C   . ASN B 1 305 ? -91.289  -39.680 79.221 1.00 45.74 ? 305  ASN B C   1 
ATOM   4594 O O   . ASN B 1 305 ? -91.971  -40.338 80.007 1.00 46.21 ? 305  ASN B O   1 
ATOM   4595 C CB  . ASN B 1 305 ? -90.592  -37.974 80.871 1.00 41.58 ? 305  ASN B CB  1 
ATOM   4596 C CG  . ASN B 1 305 ? -89.453  -37.289 81.589 1.00 41.55 ? 305  ASN B CG  1 
ATOM   4597 O OD1 . ASN B 1 305 ? -88.355  -37.829 81.678 1.00 43.45 ? 305  ASN B OD1 1 
ATOM   4598 N ND2 . ASN B 1 305 ? -89.710  -36.101 82.117 1.00 43.89 ? 305  ASN B ND2 1 
ATOM   4599 N N   . GLY B 1 306 ? -91.535  -39.644 77.916 1.00 47.42 ? 306  GLY B N   1 
ATOM   4600 C CA  . GLY B 1 306 ? -92.657  -40.392 77.376 1.00 48.32 ? 306  GLY B CA  1 
ATOM   4601 C C   . GLY B 1 306 ? -93.999  -39.849 77.851 1.00 49.52 ? 306  GLY B C   1 
ATOM   4602 O O   . GLY B 1 306 ? -94.984  -40.578 77.914 1.00 47.73 ? 306  GLY B O   1 
ATOM   4603 N N   . GLU B 1 307 ? -94.049  -38.563 78.182 1.00 51.67 ? 307  GLU B N   1 
ATOM   4604 C CA  . GLU B 1 307 ? -95.292  -37.955 78.642 1.00 53.44 ? 307  GLU B CA  1 
ATOM   4605 C C   . GLU B 1 307 ? -95.998  -37.187 77.534 1.00 54.63 ? 307  GLU B C   1 
ATOM   4606 O O   . GLU B 1 307 ? -95.394  -36.863 76.507 1.00 53.39 ? 307  GLU B O   1 
ATOM   4607 C CB  . GLU B 1 307 ? -95.019  -37.032 79.822 1.00 54.90 ? 307  GLU B CB  1 
ATOM   4608 C CG  . GLU B 1 307 ? -94.417  -37.770 80.988 1.00 58.20 ? 307  GLU B CG  1 
ATOM   4609 C CD  . GLU B 1 307 ? -93.951  -36.859 82.097 1.00 60.46 ? 307  GLU B CD  1 
ATOM   4610 O OE1 . GLU B 1 307 ? -93.296  -37.384 83.024 1.00 61.86 ? 307  GLU B OE1 1 
ATOM   4611 O OE2 . GLU B 1 307 ? -94.239  -35.639 82.046 1.00 60.49 ? 307  GLU B OE2 1 
ATOM   4612 N N   . SER B 1 308 ? -97.278  -36.894 77.763 1.00 54.92 ? 308  SER B N   1 
ATOM   4613 C CA  . SER B 1 308 ? -98.131  -36.202 76.800 1.00 55.26 ? 308  SER B CA  1 
ATOM   4614 C C   . SER B 1 308 ? -97.665  -34.816 76.383 1.00 56.33 ? 308  SER B C   1 
ATOM   4615 O O   . SER B 1 308 ? -97.521  -33.924 77.215 1.00 56.31 ? 308  SER B O   1 
ATOM   4616 C CB  . SER B 1 308 ? -99.556  -36.094 77.346 1.00 55.19 ? 308  SER B CB  1 
ATOM   4617 O OG  . SER B 1 308 ? -100.387 -35.369 76.451 1.00 57.82 ? 308  SER B OG  1 
ATOM   4618 N N   . VAL B 1 309 ? -97.448  -34.647 75.080 1.00 57.05 ? 309  VAL B N   1 
ATOM   4619 C CA  . VAL B 1 309 ? -97.020  -33.374 74.504 1.00 58.18 ? 309  VAL B CA  1 
ATOM   4620 C C   . VAL B 1 309 ? -98.233  -32.630 73.921 1.00 59.25 ? 309  VAL B C   1 
ATOM   4621 O O   . VAL B 1 309 ? -98.161  -31.431 73.651 1.00 58.68 ? 309  VAL B O   1 
ATOM   4622 C CB  . VAL B 1 309 ? -95.977  -33.586 73.367 1.00 58.05 ? 309  VAL B CB  1 
ATOM   4623 C CG1 . VAL B 1 309 ? -95.484  -32.244 72.852 1.00 58.04 ? 309  VAL B CG1 1 
ATOM   4624 C CG2 . VAL B 1 309 ? -94.808  -34.421 73.867 1.00 57.00 ? 309  VAL B CG2 1 
ATOM   4625 N N   . SER B 1 310 ? -99.340  -33.351 73.730 1.00 59.97 ? 310  SER B N   1 
ATOM   4626 C CA  . SER B 1 310 ? -100.571 -32.772 73.183 1.00 60.93 ? 310  SER B CA  1 
ATOM   4627 C C   . SER B 1 310 ? -101.071 -31.690 74.125 1.00 60.52 ? 310  SER B C   1 
ATOM   4628 O O   . SER B 1 310 ? -101.786 -30.773 73.726 1.00 58.15 ? 310  SER B O   1 
ATOM   4629 C CB  . SER B 1 310 ? -101.656 -33.843 73.030 1.00 60.89 ? 310  SER B CB  1 
ATOM   4630 O OG  . SER B 1 310 ? -101.253 -34.862 72.134 1.00 65.80 ? 310  SER B OG  1 
ATOM   4631 N N   . TYR B 1 311 ? -100.687 -31.828 75.385 1.00 61.34 ? 311  TYR B N   1 
ATOM   4632 C CA  . TYR B 1 311 ? -101.051 -30.891 76.430 1.00 62.29 ? 311  TYR B CA  1 
ATOM   4633 C C   . TYR B 1 311 ? -100.660 -29.462 76.054 1.00 61.89 ? 311  TYR B C   1 
ATOM   4634 O O   . TYR B 1 311 ? -101.276 -28.502 76.508 1.00 61.22 ? 311  TYR B O   1 
ATOM   4635 C CB  . TYR B 1 311 ? -100.337 -31.289 77.713 1.00 66.23 ? 311  TYR B CB  1 
ATOM   4636 C CG  . TYR B 1 311 ? -100.504 -30.308 78.835 1.00 70.66 ? 311  TYR B CG  1 
ATOM   4637 C CD1 . TYR B 1 311 ? -101.689 -30.254 79.566 1.00 73.02 ? 311  TYR B CD1 1 
ATOM   4638 C CD2 . TYR B 1 311 ? -99.468  -29.444 79.186 1.00 72.02 ? 311  TYR B CD2 1 
ATOM   4639 C CE1 . TYR B 1 311 ? -101.838 -29.368 80.626 1.00 75.38 ? 311  TYR B CE1 1 
ATOM   4640 C CE2 . TYR B 1 311 ? -99.605  -28.554 80.242 1.00 74.87 ? 311  TYR B CE2 1 
ATOM   4641 C CZ  . TYR B 1 311 ? -100.791 -28.523 80.962 1.00 75.68 ? 311  TYR B CZ  1 
ATOM   4642 O OH  . TYR B 1 311 ? -100.928 -27.669 82.032 1.00 77.13 ? 311  TYR B OH  1 
ATOM   4643 N N   . LEU B 1 312 ? -99.632  -29.330 75.222 1.00 60.98 ? 312  LEU B N   1 
ATOM   4644 C CA  . LEU B 1 312 ? -99.145  -28.024 74.796 1.00 60.15 ? 312  LEU B CA  1 
ATOM   4645 C C   . LEU B 1 312 ? -99.885  -27.419 73.602 1.00 61.44 ? 312  LEU B C   1 
ATOM   4646 O O   . LEU B 1 312 ? -99.642  -26.268 73.247 1.00 60.37 ? 312  LEU B O   1 
ATOM   4647 C CB  . LEU B 1 312 ? -97.653  -28.116 74.472 1.00 57.34 ? 312  LEU B CB  1 
ATOM   4648 C CG  . LEU B 1 312 ? -96.743  -28.480 75.647 1.00 56.46 ? 312  LEU B CG  1 
ATOM   4649 C CD1 . LEU B 1 312 ? -95.356  -28.844 75.136 1.00 55.69 ? 312  LEU B CD1 1 
ATOM   4650 C CD2 . LEU B 1 312 ? -96.682  -27.307 76.620 1.00 54.89 ? 312  LEU B CD2 1 
ATOM   4651 N N   . PHE B 1 313 ? -100.781 -28.182 72.979 1.00 63.56 ? 313  PHE B N   1 
ATOM   4652 C CA  . PHE B 1 313 ? -101.520 -27.675 71.823 1.00 66.52 ? 313  PHE B CA  1 
ATOM   4653 C C   . PHE B 1 313 ? -102.639 -26.713 72.197 1.00 68.50 ? 313  PHE B C   1 
ATOM   4654 O O   . PHE B 1 313 ? -103.132 -25.965 71.354 1.00 68.64 ? 313  PHE B O   1 
ATOM   4655 C CB  . PHE B 1 313 ? -102.107 -28.826 70.999 1.00 64.99 ? 313  PHE B CB  1 
ATOM   4656 C CG  . PHE B 1 313 ? -101.074 -29.733 70.394 1.00 64.43 ? 313  PHE B CG  1 
ATOM   4657 C CD1 . PHE B 1 313 ? -99.757  -29.314 70.240 1.00 64.01 ? 313  PHE B CD1 1 
ATOM   4658 C CD2 . PHE B 1 313 ? -101.428 -31.005 69.964 1.00 65.37 ? 313  PHE B CD2 1 
ATOM   4659 C CE1 . PHE B 1 313 ? -98.808  -30.150 69.668 1.00 64.46 ? 313  PHE B CE1 1 
ATOM   4660 C CE2 . PHE B 1 313 ? -100.483 -31.851 69.388 1.00 66.12 ? 313  PHE B CE2 1 
ATOM   4661 C CZ  . PHE B 1 313 ? -99.169  -31.421 69.241 1.00 64.79 ? 313  PHE B CZ  1 
ATOM   4662 N N   . SER B 1 314 ? -103.035 -26.732 73.463 1.00 71.86 ? 314  SER B N   1 
ATOM   4663 C CA  . SER B 1 314 ? -104.105 -25.861 73.938 1.00 75.65 ? 314  SER B CA  1 
ATOM   4664 C C   . SER B 1 314 ? -103.755 -25.339 75.320 1.00 78.13 ? 314  SER B C   1 
ATOM   4665 O O   . SER B 1 314 ? -104.627 -24.895 76.060 1.00 79.22 ? 314  SER B O   1 
ATOM   4666 C CB  . SER B 1 314 ? -105.416 -26.643 74.018 1.00 75.65 ? 314  SER B CB  1 
ATOM   4667 O OG  . SER B 1 314 ? -105.307 -27.703 74.954 1.00 76.49 ? 314  SER B OG  1 
ATOM   4668 N N   . HIS B 1 315 ? -102.478 -25.391 75.673 1.00 80.86 ? 315  HIS B N   1 
ATOM   4669 C CA  . HIS B 1 315 ? -102.083 -24.953 76.997 1.00 83.84 ? 315  HIS B CA  1 
ATOM   4670 C C   . HIS B 1 315 ? -100.705 -24.295 77.009 1.00 83.94 ? 315  HIS B C   1 
ATOM   4671 O O   . HIS B 1 315 ? -99.748  -24.825 76.451 1.00 85.15 ? 315  HIS B O   1 
ATOM   4672 C CB  . HIS B 1 315 ? -102.097 -26.167 77.927 1.00 88.26 ? 315  HIS B CB  1 
ATOM   4673 C CG  . HIS B 1 315 ? -102.123 -25.827 79.383 1.00 92.16 ? 315  HIS B CG  1 
ATOM   4674 N ND1 . HIS B 1 315 ? -101.170 -25.031 79.984 1.00 94.03 ? 315  HIS B ND1 1 
ATOM   4675 C CD2 . HIS B 1 315 ? -102.972 -26.205 80.369 1.00 93.57 ? 315  HIS B CD2 1 
ATOM   4676 C CE1 . HIS B 1 315 ? -101.432 -24.935 81.276 1.00 94.95 ? 315  HIS B CE1 1 
ATOM   4677 N NE2 . HIS B 1 315 ? -102.521 -25.639 81.535 1.00 94.76 ? 315  HIS B NE2 1 
ATOM   4678 N N   . VAL B 1 316 ? -100.609 -23.139 77.654 1.00 83.44 ? 316  VAL B N   1 
ATOM   4679 C CA  . VAL B 1 316 ? -99.343  -22.428 77.746 1.00 82.44 ? 316  VAL B CA  1 
ATOM   4680 C C   . VAL B 1 316 ? -98.634  -22.835 79.035 1.00 81.99 ? 316  VAL B C   1 
ATOM   4681 O O   . VAL B 1 316 ? -99.019  -22.400 80.124 1.00 82.80 ? 316  VAL B O   1 
ATOM   4682 C CB  . VAL B 1 316 ? -99.559  -20.897 77.753 1.00 82.11 ? 316  VAL B CB  1 
ATOM   4683 C CG1 . VAL B 1 316 ? -98.234  -20.184 77.976 1.00 82.72 ? 316  VAL B CG1 1 
ATOM   4684 C CG2 . VAL B 1 316 ? -100.178 -20.457 76.431 1.00 81.56 ? 316  VAL B CG2 1 
ATOM   4685 N N   . PRO B 1 317 ? -97.578  -23.663 78.928 1.00 81.95 ? 317  PRO B N   1 
ATOM   4686 C CA  . PRO B 1 317 ? -96.815  -24.131 80.092 1.00 81.26 ? 317  PRO B CA  1 
ATOM   4687 C C   . PRO B 1 317 ? -96.293  -22.991 80.970 1.00 81.45 ? 317  PRO B C   1 
ATOM   4688 O O   . PRO B 1 317 ? -97.099  -22.462 81.770 1.00 80.54 ? 317  PRO B O   1 
ATOM   4689 C CB  . PRO B 1 317 ? -95.676  -24.918 79.452 1.00 79.81 ? 317  PRO B CB  1 
ATOM   4690 C CG  . PRO B 1 317 ? -95.418  -24.136 78.213 1.00 79.61 ? 317  PRO B CG  1 
ATOM   4691 C CD  . PRO B 1 317 ? -96.833  -23.957 77.693 1.00 80.14 ? 317  PRO B CD  1 
HETATM 4692 S S   . SO4 C 2 .   ? -119.991 -34.202 53.033 1.00 79.56 ? 1002 SO4 A S   1 
HETATM 4693 O O1  . SO4 C 2 .   ? -120.842 -33.265 53.793 1.00 79.47 ? 1002 SO4 A O1  1 
HETATM 4694 O O2  . SO4 C 2 .   ? -120.021 -35.528 53.677 1.00 79.04 ? 1002 SO4 A O2  1 
HETATM 4695 O O3  . SO4 C 2 .   ? -120.491 -34.313 51.652 1.00 79.65 ? 1002 SO4 A O3  1 
HETATM 4696 O O4  . SO4 C 2 .   ? -118.604 -33.701 53.005 1.00 79.54 ? 1002 SO4 A O4  1 
HETATM 4697 S S   . SO4 D 2 .   ? -93.880  -32.728 31.564 1.00 38.69 ? 1004 SO4 A S   1 
HETATM 4698 O O1  . SO4 D 2 .   ? -93.327  -33.901 30.872 1.00 33.78 ? 1004 SO4 A O1  1 
HETATM 4699 O O2  . SO4 D 2 .   ? -92.986  -32.336 32.666 1.00 34.55 ? 1004 SO4 A O2  1 
HETATM 4700 O O3  . SO4 D 2 .   ? -93.999  -31.601 30.616 1.00 38.08 ? 1004 SO4 A O3  1 
HETATM 4701 O O4  . SO4 D 2 .   ? -95.218  -33.045 32.099 1.00 34.24 ? 1004 SO4 A O4  1 
HETATM 4702 S S   . SO4 E 2 .   ? -99.883  -29.548 42.406 1.00 66.36 ? 1006 SO4 A S   1 
HETATM 4703 O O1  . SO4 E 2 .   ? -99.024  -29.344 41.224 1.00 66.88 ? 1006 SO4 A O1  1 
HETATM 4704 O O2  . SO4 E 2 .   ? -100.003 -30.990 42.691 1.00 65.12 ? 1006 SO4 A O2  1 
HETATM 4705 O O3  . SO4 E 2 .   ? -99.279  -28.843 43.553 1.00 65.85 ? 1006 SO4 A O3  1 
HETATM 4706 O O4  . SO4 E 2 .   ? -101.231 -28.998 42.157 1.00 68.32 ? 1006 SO4 A O4  1 
HETATM 4707 S S   . SO4 F 2 .   ? -94.113  -11.964 52.531 1.00 63.06 ? 1001 SO4 B S   1 
HETATM 4708 O O1  . SO4 F 2 .   ? -94.833  -10.872 51.842 1.00 62.35 ? 1001 SO4 B O1  1 
HETATM 4709 O O2  . SO4 F 2 .   ? -93.831  -11.576 53.927 1.00 59.93 ? 1001 SO4 B O2  1 
HETATM 4710 O O3  . SO4 F 2 .   ? -94.939  -13.185 52.529 1.00 63.50 ? 1001 SO4 B O3  1 
HETATM 4711 O O4  . SO4 F 2 .   ? -92.849  -12.234 51.818 1.00 63.26 ? 1001 SO4 B O4  1 
HETATM 4712 S S   . SO4 G 2 .   ? -99.204  -37.316 73.170 1.00 30.38 ? 1003 SO4 B S   1 
HETATM 4713 O O1  . SO4 G 2 .   ? -98.547  -36.071 72.758 1.00 34.53 ? 1003 SO4 B O1  1 
HETATM 4714 O O2  . SO4 G 2 .   ? -98.231  -38.182 73.853 1.00 33.24 ? 1003 SO4 B O2  1 
HETATM 4715 O O3  . SO4 G 2 .   ? -100.306 -36.997 74.085 1.00 32.73 ? 1003 SO4 B O3  1 
HETATM 4716 O O4  . SO4 G 2 .   ? -99.720  -38.015 71.981 1.00 31.45 ? 1003 SO4 B O4  1 
HETATM 4717 S S   . SO4 H 2 .   ? -101.178 -30.965 62.505 1.00 41.24 ? 1005 SO4 B S   1 
HETATM 4718 O O1  . SO4 H 2 .   ? -101.460 -29.517 62.507 1.00 41.01 ? 1005 SO4 B O1  1 
HETATM 4719 O O2  . SO4 H 2 .   ? -99.738  -31.168 62.257 1.00 38.35 ? 1005 SO4 B O2  1 
HETATM 4720 O O3  . SO4 H 2 .   ? -101.557 -31.575 63.786 1.00 41.42 ? 1005 SO4 B O3  1 
HETATM 4721 O O4  . SO4 H 2 .   ? -101.967 -31.609 61.434 1.00 39.39 ? 1005 SO4 B O4  1 
HETATM 4722 O O   . HOH I 3 .   ? -96.359  -48.098 33.821 1.00 27.21 ? 1007 HOH A O   1 
HETATM 4723 O O   . HOH I 3 .   ? -97.508  -31.323 44.420 1.00 32.64 ? 1008 HOH A O   1 
HETATM 4724 O O   . HOH I 3 .   ? -110.474 -39.153 51.539 1.00 35.40 ? 1009 HOH A O   1 
HETATM 4725 O O   . HOH I 3 .   ? -92.303  -48.750 44.074 1.00 30.71 ? 1010 HOH A O   1 
HETATM 4726 O O   . HOH I 3 .   ? -93.501  -37.461 44.126 1.00 28.54 ? 1011 HOH A O   1 
HETATM 4727 O O   . HOH I 3 .   ? -103.744 -50.196 18.501 1.00 31.33 ? 1012 HOH A O   1 
HETATM 4728 O O   . HOH I 3 .   ? -99.612  -37.926 66.896 1.00 25.29 ? 1013 HOH A O   1 
HETATM 4729 O O   . HOH I 3 .   ? -114.867 -11.612 45.689 1.00 45.86 ? 1014 HOH A O   1 
HETATM 4730 O O   . HOH I 3 .   ? -98.394  -32.935 38.685 1.00 37.00 ? 1015 HOH A O   1 
HETATM 4731 O O   . HOH I 3 .   ? -94.253  -43.128 49.884 1.00 30.06 ? 1016 HOH A O   1 
HETATM 4732 O O   . HOH I 3 .   ? -111.365 -53.730 26.362 1.00 32.35 ? 1017 HOH A O   1 
HETATM 4733 O O   . HOH I 3 .   ? -93.288  -58.742 46.577 1.00 44.91 ? 1018 HOH A O   1 
HETATM 4734 O O   . HOH I 3 .   ? -111.428 -56.755 46.465 1.00 31.10 ? 1019 HOH A O   1 
HETATM 4735 O O   . HOH I 3 .   ? -107.939 -36.553 46.340 1.00 34.04 ? 1020 HOH A O   1 
HETATM 4736 O O   . HOH I 3 .   ? -103.889 -53.320 27.118 1.00 32.72 ? 1021 HOH A O   1 
HETATM 4737 O O   . HOH I 3 .   ? -100.949 -40.157 65.687 1.00 31.95 ? 1022 HOH A O   1 
HETATM 4738 O O   . HOH I 3 .   ? -96.654  -45.792 56.466 1.00 27.95 ? 1023 HOH A O   1 
HETATM 4739 O O   . HOH I 3 .   ? -97.860  -35.533 67.432 1.00 39.14 ? 1024 HOH A O   1 
HETATM 4740 O O   . HOH I 3 .   ? -124.833 -14.007 38.710 1.00 59.18 ? 1025 HOH A O   1 
HETATM 4741 O O   . HOH I 3 .   ? -92.017  -36.280 46.005 1.00 37.09 ? 1026 HOH A O   1 
HETATM 4742 O O   . HOH I 3 .   ? -107.215 -37.462 43.756 1.00 30.78 ? 1027 HOH A O   1 
HETATM 4743 O O   . HOH I 3 .   ? -91.032  -62.869 36.548 1.00 42.23 ? 1028 HOH A O   1 
HETATM 4744 O O   . HOH I 3 .   ? -95.015  -55.669 48.038 1.00 26.33 ? 1029 HOH A O   1 
HETATM 4745 O O   . HOH I 3 .   ? -90.709  -56.340 38.041 1.00 38.24 ? 1030 HOH A O   1 
HETATM 4746 O O   . HOH I 3 .   ? -103.626 -28.342 47.366 1.00 51.84 ? 1031 HOH A O   1 
HETATM 4747 O O   . HOH I 3 .   ? -109.064 -28.519 39.413 1.00 42.69 ? 1032 HOH A O   1 
HETATM 4748 O O   . HOH I 3 .   ? -107.687 -35.457 62.604 1.00 45.85 ? 1033 HOH A O   1 
HETATM 4749 O O   . HOH I 3 .   ? -99.448  -64.220 27.407 1.00 46.28 ? 1034 HOH A O   1 
HETATM 4750 O O   . HOH I 3 .   ? -90.489  -44.372 39.258 1.00 39.64 ? 1035 HOH A O   1 
HETATM 4751 O O   . HOH I 3 .   ? -92.742  -43.856 46.701 1.00 33.67 ? 1036 HOH A O   1 
HETATM 4752 O O   . HOH I 3 .   ? -108.471 -55.236 32.642 1.00 40.46 ? 1037 HOH A O   1 
HETATM 4753 O O   . HOH I 3 .   ? -100.385 -53.696 23.470 1.00 35.06 ? 1038 HOH A O   1 
HETATM 4754 O O   . HOH I 3 .   ? -104.774 -30.954 43.581 1.00 44.72 ? 1039 HOH A O   1 
HETATM 4755 O O   . HOH I 3 .   ? -90.519  -33.357 33.003 1.00 22.76 ? 1040 HOH A O   1 
HETATM 4756 O O   . HOH I 3 .   ? -106.102 -38.175 59.196 1.00 45.53 ? 1041 HOH A O   1 
HETATM 4757 O O   . HOH I 3 .   ? -108.390 -34.896 59.602 1.00 52.68 ? 1042 HOH A O   1 
HETATM 4758 O O   . HOH I 3 .   ? -114.197 -13.814 28.170 1.00 51.67 ? 1043 HOH A O   1 
HETATM 4759 O O   . HOH I 3 .   ? -117.247 -11.691 47.183 1.00 44.58 ? 1044 HOH A O   1 
HETATM 4760 O O   . HOH I 3 .   ? -116.114 -9.268  46.617 1.00 55.08 ? 1045 HOH A O   1 
HETATM 4761 O O   . HOH I 3 .   ? -115.355 -25.053 57.945 1.00 38.72 ? 1046 HOH A O   1 
HETATM 4762 O O   . HOH I 3 .   ? -119.997 -11.918 56.556 1.00 59.05 ? 1047 HOH A O   1 
HETATM 4763 O O   . HOH I 3 .   ? -119.085 -10.706 53.976 1.00 45.04 ? 1048 HOH A O   1 
HETATM 4764 O O   . HOH I 3 .   ? -112.632 -28.886 41.019 1.00 55.03 ? 1049 HOH A O   1 
HETATM 4765 O O   . HOH I 3 .   ? -107.034 -43.529 18.669 1.00 77.84 ? 1050 HOH A O   1 
HETATM 4766 O O   . HOH I 3 .   ? -110.556 -58.915 31.620 1.00 41.41 ? 1051 HOH A O   1 
HETATM 4767 O O   . HOH I 3 .   ? -116.822 -48.571 35.462 1.00 74.21 ? 1052 HOH A O   1 
HETATM 4768 O O   . HOH I 3 .   ? -119.219 -48.779 36.389 1.00 46.94 ? 1053 HOH A O   1 
HETATM 4769 O O   . HOH I 3 .   ? -116.309 -46.034 35.838 1.00 51.53 ? 1054 HOH A O   1 
HETATM 4770 O O   . HOH I 3 .   ? -104.662 -44.324 19.242 1.00 60.82 ? 1055 HOH A O   1 
HETATM 4771 O O   . HOH I 3 .   ? -94.128  -64.667 35.498 1.00 50.01 ? 1056 HOH A O   1 
HETATM 4772 O O   . HOH I 3 .   ? -113.825 -37.209 52.681 1.00 54.63 ? 1057 HOH A O   1 
HETATM 4773 O O   . HOH I 3 .   ? -105.849 -28.391 54.502 1.00 69.79 ? 1058 HOH A O   1 
HETATM 4774 O O   . HOH I 3 .   ? -108.120 -30.988 54.665 1.00 58.99 ? 1059 HOH A O   1 
HETATM 4775 O O   . HOH I 3 .   ? -106.273 -36.473 74.740 1.00 57.00 ? 1060 HOH A O   1 
HETATM 4776 O O   . HOH I 3 .   ? -104.288 -37.135 76.385 1.00 61.07 ? 1061 HOH A O   1 
HETATM 4777 O O   . HOH I 3 .   ? -91.311  -38.357 43.492 1.00 78.58 ? 1062 HOH A O   1 
HETATM 4778 O O   . HOH I 3 .   ? -108.460 -25.019 48.635 1.00 54.29 ? 1063 HOH A O   1 
HETATM 4779 O O   . HOH I 3 .   ? -124.995 -27.729 63.871 1.00 65.72 ? 1064 HOH A O   1 
HETATM 4780 O O   . HOH I 3 .   ? -127.836 -21.152 60.025 1.00 56.91 ? 1065 HOH A O   1 
HETATM 4781 O O   . HOH I 3 .   ? -88.023  -34.181 23.400 1.00 45.28 ? 1066 HOH A O   1 
HETATM 4782 O O   . HOH I 3 .   ? -100.672 -49.920 20.012 1.00 56.38 ? 1067 HOH A O   1 
HETATM 4783 O O   . HOH I 3 .   ? -105.990 -26.242 47.850 1.00 61.20 ? 1068 HOH A O   1 
HETATM 4784 O O   . HOH I 3 .   ? -106.403 -26.977 41.761 1.00 55.30 ? 1069 HOH A O   1 
HETATM 4785 O O   . HOH I 3 .   ? -106.859 -29.464 42.505 1.00 64.38 ? 1070 HOH A O   1 
HETATM 4786 O O   . HOH I 3 .   ? -109.426 -29.334 43.575 1.00 58.26 ? 1071 HOH A O   1 
HETATM 4787 O O   . HOH I 3 .   ? -104.124 -23.172 40.736 1.00 57.89 ? 1072 HOH A O   1 
HETATM 4788 O O   . HOH I 3 .   ? -110.369 -39.460 49.051 1.00 63.56 ? 1073 HOH A O   1 
HETATM 4789 O O   . HOH I 3 .   ? -110.316 -38.203 46.758 1.00 43.93 ? 1074 HOH A O   1 
HETATM 4790 O O   . HOH I 3 .   ? -108.933 -45.376 43.785 1.00 44.50 ? 1075 HOH A O   1 
HETATM 4791 O O   . HOH I 3 .   ? -120.760 -31.656 51.103 1.00 58.99 ? 1076 HOH A O   1 
HETATM 4792 O O   . HOH I 3 .   ? -116.518 -32.825 51.651 1.00 64.05 ? 1077 HOH A O   1 
HETATM 4793 O O   . HOH I 3 .   ? -116.718 -38.530 40.343 1.00 44.45 ? 1078 HOH A O   1 
HETATM 4794 O O   . HOH J 3 .   ? -83.838  -37.735 70.821 1.00 21.60 ? 1006 HOH B O   1 
HETATM 4795 O O   . HOH J 3 .   ? -70.570  -40.858 72.045 1.00 27.35 ? 1007 HOH B O   1 
HETATM 4796 O O   . HOH J 3 .   ? -89.881  -21.746 53.215 1.00 33.57 ? 1008 HOH B O   1 
HETATM 4797 O O   . HOH J 3 .   ? -94.599  -22.082 58.901 1.00 30.16 ? 1009 HOH B O   1 
HETATM 4798 O O   . HOH J 3 .   ? -89.628  -16.045 64.771 1.00 22.61 ? 1010 HOH B O   1 
HETATM 4799 O O   . HOH J 3 .   ? -70.336  -45.319 68.137 1.00 26.10 ? 1011 HOH B O   1 
HETATM 4800 O O   . HOH J 3 .   ? -92.059  -41.361 50.491 1.00 30.58 ? 1012 HOH B O   1 
HETATM 4801 O O   . HOH J 3 .   ? -94.582  -38.543 60.529 1.00 31.62 ? 1013 HOH B O   1 
HETATM 4802 O O   . HOH J 3 .   ? -100.587 -22.089 66.107 1.00 36.62 ? 1014 HOH B O   1 
HETATM 4803 O O   . HOH J 3 .   ? -88.858  -38.666 54.619 1.00 25.23 ? 1015 HOH B O   1 
HETATM 4804 O O   . HOH J 3 .   ? -91.120  -22.268 58.080 1.00 39.60 ? 1016 HOH B O   1 
HETATM 4805 O O   . HOH J 3 .   ? -94.278  -36.134 42.087 1.00 32.16 ? 1017 HOH B O   1 
HETATM 4806 O O   . HOH J 3 .   ? -65.097  -29.858 50.151 1.00 37.74 ? 1018 HOH B O   1 
HETATM 4807 O O   . HOH J 3 .   ? -89.035  -3.795  68.554 1.00 35.51 ? 1019 HOH B O   1 
HETATM 4808 O O   . HOH J 3 .   ? -95.553  -39.833 58.429 1.00 34.33 ? 1020 HOH B O   1 
HETATM 4809 O O   . HOH J 3 .   ? -88.739  -40.431 57.854 1.00 35.79 ? 1021 HOH B O   1 
HETATM 4810 O O   . HOH J 3 .   ? -99.123  -26.113 61.138 1.00 35.97 ? 1022 HOH B O   1 
HETATM 4811 O O   . HOH J 3 .   ? -92.885  -24.189 58.500 1.00 34.48 ? 1023 HOH B O   1 
HETATM 4812 O O   . HOH J 3 .   ? -92.843  -32.465 38.236 1.00 43.88 ? 1024 HOH B O   1 
HETATM 4813 O O   . HOH J 3 .   ? -107.103 3.772   54.173 1.00 34.11 ? 1025 HOH B O   1 
HETATM 4814 O O   . HOH J 3 .   ? -85.657  -12.007 61.992 1.00 35.81 ? 1026 HOH B O   1 
HETATM 4815 O O   . HOH J 3 .   ? -92.468  -25.536 29.350 1.00 53.31 ? 1027 HOH B O   1 
HETATM 4816 O O   . HOH J 3 .   ? -75.440  -23.906 78.268 1.00 34.11 ? 1028 HOH B O   1 
HETATM 4817 O O   . HOH J 3 .   ? -92.053  -25.208 61.437 1.00 32.29 ? 1029 HOH B O   1 
HETATM 4818 O O   . HOH J 3 .   ? -117.779 -10.162 67.922 1.00 37.91 ? 1030 HOH B O   1 
HETATM 4819 O O   . HOH J 3 .   ? -91.005  -41.047 73.730 1.00 42.47 ? 1031 HOH B O   1 
HETATM 4820 O O   . HOH J 3 .   ? -101.836 -26.704 57.347 1.00 41.41 ? 1032 HOH B O   1 
HETATM 4821 O O   . HOH J 3 .   ? -90.957  -40.290 53.977 1.00 40.18 ? 1033 HOH B O   1 
HETATM 4822 O O   . HOH J 3 .   ? -77.154  -31.051 77.587 1.00 33.87 ? 1034 HOH B O   1 
HETATM 4823 O O   . HOH J 3 .   ? -72.378  -48.094 72.473 1.00 39.19 ? 1035 HOH B O   1 
HETATM 4824 O O   . HOH J 3 .   ? -103.063 0.257   63.035 1.00 31.85 ? 1036 HOH B O   1 
HETATM 4825 O O   . HOH J 3 .   ? -107.545 -26.081 65.308 1.00 51.29 ? 1037 HOH B O   1 
HETATM 4826 O O   . HOH J 3 .   ? -83.810  -31.900 82.495 1.00 48.47 ? 1038 HOH B O   1 
HETATM 4827 O O   . HOH J 3 .   ? -67.462  -37.638 77.504 1.00 46.74 ? 1039 HOH B O   1 
HETATM 4828 O O   . HOH J 3 .   ? -91.842  -43.706 52.895 1.00 38.85 ? 1040 HOH B O   1 
HETATM 4829 O O   . HOH J 3 .   ? -94.735  -44.446 59.246 1.00 48.77 ? 1041 HOH B O   1 
HETATM 4830 O O   . HOH J 3 .   ? -98.997  -0.897  55.983 1.00 40.13 ? 1042 HOH B O   1 
HETATM 4831 O O   . HOH J 3 .   ? -83.896  -41.841 60.394 1.00 43.68 ? 1043 HOH B O   1 
HETATM 4832 O O   . HOH J 3 .   ? -74.257  -26.985 72.077 1.00 31.33 ? 1044 HOH B O   1 
HETATM 4833 O O   . HOH J 3 .   ? -98.126  -33.148 66.030 1.00 31.43 ? 1045 HOH B O   1 
HETATM 4834 O O   . HOH J 3 .   ? -112.648 -4.345  67.848 1.00 39.02 ? 1046 HOH B O   1 
HETATM 4835 O O   . HOH J 3 .   ? -94.192  -0.341  54.242 1.00 51.72 ? 1047 HOH B O   1 
HETATM 4836 O O   . HOH J 3 .   ? -96.100  -33.493 37.636 1.00 41.23 ? 1048 HOH B O   1 
HETATM 4837 O O   . HOH J 3 .   ? -97.519  -42.011 77.357 1.00 35.52 ? 1049 HOH B O   1 
HETATM 4838 O O   . HOH J 3 .   ? -78.179  -25.544 62.790 1.00 37.13 ? 1050 HOH B O   1 
HETATM 4839 O O   . HOH J 3 .   ? -87.891  1.644   63.947 1.00 48.96 ? 1051 HOH B O   1 
HETATM 4840 O O   . HOH J 3 .   ? -90.549  -31.354 39.064 1.00 30.98 ? 1052 HOH B O   1 
HETATM 4841 O O   . HOH J 3 .   ? -88.043  -42.804 65.059 1.00 31.51 ? 1053 HOH B O   1 
HETATM 4842 O O   . HOH J 3 .   ? -103.226 -17.358 58.378 1.00 36.07 ? 1054 HOH B O   1 
HETATM 4843 O O   . HOH J 3 .   ? -80.270  -30.806 86.230 1.00 44.93 ? 1055 HOH B O   1 
HETATM 4844 O O   . HOH J 3 .   ? -81.389  -12.585 68.629 1.00 61.84 ? 1056 HOH B O   1 
HETATM 4845 O O   . HOH J 3 .   ? -103.231 -2.839  49.752 1.00 47.79 ? 1057 HOH B O   1 
HETATM 4846 O O   . HOH J 3 .   ? -85.774  -43.719 63.945 1.00 34.12 ? 1058 HOH B O   1 
HETATM 4847 O O   . HOH J 3 .   ? -78.420  -43.021 59.095 1.00 45.83 ? 1059 HOH B O   1 
HETATM 4848 O O   . HOH J 3 .   ? -87.459  -24.366 44.285 1.00 45.45 ? 1060 HOH B O   1 
HETATM 4849 O O   . HOH J 3 .   ? -82.476  2.004   63.110 1.00 49.60 ? 1061 HOH B O   1 
HETATM 4850 O O   . HOH J 3 .   ? -98.558  -15.219 75.233 1.00 43.14 ? 1062 HOH B O   1 
HETATM 4851 O O   . HOH J 3 .   ? -76.953  -44.259 67.017 1.00 39.79 ? 1063 HOH B O   1 
HETATM 4852 O O   . HOH J 3 .   ? -101.415 -19.752 65.053 1.00 42.51 ? 1064 HOH B O   1 
HETATM 4853 O O   . HOH J 3 .   ? -116.913 -13.857 60.684 1.00 36.17 ? 1065 HOH B O   1 
HETATM 4854 O O   . HOH J 3 .   ? -99.997  -33.439 60.459 1.00 28.56 ? 1066 HOH B O   1 
HETATM 4855 O O   . HOH J 3 .   ? -84.446  -17.452 68.412 1.00 37.41 ? 1067 HOH B O   1 
HETATM 4856 O O   . HOH J 3 .   ? -95.812  -37.677 62.696 1.00 32.74 ? 1068 HOH B O   1 
HETATM 4857 O O   . HOH J 3 .   ? -97.251  -13.014 56.201 1.00 33.35 ? 1069 HOH B O   1 
HETATM 4858 O O   . HOH J 3 .   ? -91.629  -26.246 45.764 1.00 57.41 ? 1070 HOH B O   1 
HETATM 4859 O O   . HOH J 3 .   ? -116.336 -12.461 71.187 1.00 42.19 ? 1071 HOH B O   1 
HETATM 4860 O O   . HOH J 3 .   ? -66.043  -24.089 68.295 1.00 47.16 ? 1072 HOH B O   1 
HETATM 4861 O O   . HOH J 3 .   ? -97.832  -25.904 71.322 1.00 32.26 ? 1073 HOH B O   1 
HETATM 4862 O O   . HOH J 3 .   ? -117.750 -9.127  52.460 1.00 42.86 ? 1074 HOH B O   1 
HETATM 4863 O O   . HOH J 3 .   ? -80.576  -20.050 68.528 1.00 48.61 ? 1075 HOH B O   1 
HETATM 4864 O O   . HOH J 3 .   ? -85.314  -13.061 70.002 1.00 44.37 ? 1076 HOH B O   1 
HETATM 4865 O O   . HOH J 3 .   ? -89.656  -22.046 56.254 1.00 41.60 ? 1077 HOH B O   1 
HETATM 4866 O O   . HOH J 3 .   ? -87.047  -20.284 56.927 1.00 49.53 ? 1078 HOH B O   1 
HETATM 4867 O O   . HOH J 3 .   ? -101.480 -25.135 50.325 1.00 53.21 ? 1079 HOH B O   1 
HETATM 4868 O O   . HOH J 3 .   ? -75.752  -40.191 59.385 1.00 39.10 ? 1080 HOH B O   1 
HETATM 4869 O O   . HOH J 3 .   ? -80.963  -43.892 58.912 1.00 58.33 ? 1081 HOH B O   1 
HETATM 4870 O O   . HOH J 3 .   ? -90.478  -39.252 69.043 1.00 49.36 ? 1082 HOH B O   1 
HETATM 4871 O O   . HOH J 3 .   ? -89.026  -41.403 68.799 1.00 50.59 ? 1083 HOH B O   1 
HETATM 4872 O O   . HOH J 3 .   ? -87.206  -43.469 68.610 1.00 46.65 ? 1084 HOH B O   1 
HETATM 4873 O O   . HOH J 3 .   ? -88.903  -46.219 68.072 1.00 52.17 ? 1085 HOH B O   1 
HETATM 4874 O O   . HOH J 3 .   ? -103.639 -15.816 47.879 1.00 30.02 ? 1086 HOH B O   1 
HETATM 4875 O O   . HOH J 3 .   ? -105.700 -3.234  46.026 1.00 37.49 ? 1087 HOH B O   1 
HETATM 4876 O O   . HOH J 3 .   ? -96.867  -0.360  49.208 1.00 82.42 ? 1088 HOH B O   1 
HETATM 4877 O O   . HOH J 3 .   ? -94.324  -0.935  48.845 1.00 55.59 ? 1089 HOH B O   1 
HETATM 4878 O O   . HOH J 3 .   ? -80.199  -39.950 83.647 1.00 70.64 ? 1090 HOH B O   1 
HETATM 4879 O O   . HOH J 3 .   ? -82.982  -38.983 83.051 1.00 65.22 ? 1091 HOH B O   1 
HETATM 4880 O O   . HOH J 3 .   ? -78.081  -42.357 83.127 1.00 64.97 ? 1092 HOH B O   1 
HETATM 4881 O O   . HOH J 3 .   ? -84.300  -41.388 82.238 1.00 60.31 ? 1093 HOH B O   1 
HETATM 4882 O O   . HOH J 3 .   ? -73.285  -39.366 81.579 1.00 49.45 ? 1094 HOH B O   1 
HETATM 4883 O O   . HOH J 3 .   ? -71.426  -39.457 79.768 1.00 63.28 ? 1095 HOH B O   1 
HETATM 4884 O O   . HOH J 3 .   ? -69.004  -37.689 79.471 1.00 55.53 ? 1096 HOH B O   1 
HETATM 4885 O O   . HOH J 3 .   ? -72.185  -25.070 73.759 1.00 64.55 ? 1097 HOH B O   1 
HETATM 4886 O O   . HOH J 3 .   ? -69.792  -25.618 73.085 1.00 45.56 ? 1098 HOH B O   1 
HETATM 4887 O O   . HOH J 3 .   ? -95.895  -43.084 57.830 1.00 36.31 ? 1099 HOH B O   1 
HETATM 4888 O O   . HOH J 3 .   ? -97.437  -41.245 58.045 1.00 42.39 ? 1100 HOH B O   1 
HETATM 4889 O O   . HOH J 3 .   ? -117.605 -12.139 59.098 1.00 46.23 ? 1101 HOH B O   1 
HETATM 4890 O O   . HOH J 3 .   ? -75.189  -20.171 75.845 1.00 64.75 ? 1102 HOH B O   1 
HETATM 4891 O O   . HOH J 3 .   ? -81.869  -15.059 74.932 1.00 72.68 ? 1103 HOH B O   1 
HETATM 4892 O O   . HOH J 3 .   ? -103.040 -24.289 58.224 1.00 50.72 ? 1104 HOH B O   1 
HETATM 4893 O O   . HOH J 3 .   ? -100.855 -23.830 53.638 1.00 53.69 ? 1105 HOH B O   1 
HETATM 4894 O O   . HOH J 3 .   ? -98.594  -24.815 50.815 1.00 61.06 ? 1106 HOH B O   1 
HETATM 4895 O O   . HOH J 3 .   ? -101.358 -21.213 53.281 1.00 58.13 ? 1107 HOH B O   1 
HETATM 4896 O O   . HOH J 3 .   ? -97.628  -18.364 54.760 1.00 50.90 ? 1108 HOH B O   1 
HETATM 4897 O O   . HOH J 3 .   ? -102.178 -19.219 41.276 1.00 60.54 ? 1109 HOH B O   1 
HETATM 4898 O O   . HOH J 3 .   ? -104.895 -23.125 43.564 1.00 56.11 ? 1110 HOH B O   1 
HETATM 4899 O O   . HOH J 3 .   ? -102.217 -22.964 43.880 1.00 51.93 ? 1111 HOH B O   1 
HETATM 4900 O O   . HOH J 3 .   ? -85.183  -22.514 59.187 1.00 44.53 ? 1112 HOH B O   1 
HETATM 4901 O O   . HOH J 3 .   ? -96.289  -10.737 54.252 1.00 53.72 ? 1113 HOH B O   1 
HETATM 4902 O O   . HOH J 3 .   ? -99.384  -37.127 69.251 1.00 55.08 ? 1114 HOH B O   1 
HETATM 4903 O O   . HOH J 3 .   ? -100.063 -31.331 65.988 1.00 37.98 ? 1115 HOH B O   1 
HETATM 4904 O O   . HOH J 3 .   ? -93.832  -15.799 53.654 1.00 55.36 ? 1116 HOH B 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   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  CYS 41  41  41  CYS CYS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  MET 68  68  68  MET MET A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  CYS 91  91  91  CYS CYS A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 MET 115 115 115 MET MET A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 HIS 123 123 123 HIS HIS A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 MET 127 127 127 MET MET A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 TRP 162 162 162 TRP TRP A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 CYS 165 165 165 CYS CYS A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 LYS 197 197 ?   ?   ?   A . n 
A 1 198 LYS 198 198 ?   ?   ?   A . n 
A 1 199 ALA 199 199 ?   ?   ?   A . n 
A 1 200 ASN 200 200 ?   ?   ?   A . n 
A 1 201 GLU 201 201 ?   ?   ?   A . n 
A 1 202 VAL 202 202 ?   ?   ?   A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 MET 205 205 205 MET MET A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 MET 222 222 222 MET MET A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 CYS 226 226 226 CYS CYS A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 CYS 230 230 230 CYS CYS A . n 
A 1 231 HIS 231 231 231 HIS HIS A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 VAL 271 271 271 VAL VAL A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 PRO 276 276 276 PRO PRO A . n 
A 1 277 GLN 277 277 277 GLN GLN A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 MET 281 281 281 MET MET A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 CYS 284 284 284 CYS CYS A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 LYS 286 286 286 LYS LYS A . n 
A 1 287 ILE 287 287 287 ILE ILE A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 MET 294 294 294 MET MET A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 ILE 300 300 300 ILE ILE A . n 
A 1 301 ARG 301 301 301 ARG ARG A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 ASN 305 305 305 ASN ASN A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 PHE 313 313 313 PHE PHE A . n 
A 1 314 SER 314 314 ?   ?   ?   A . n 
A 1 315 HIS 315 315 ?   ?   ?   A . n 
A 1 316 VAL 316 316 ?   ?   ?   A . n 
A 1 317 PRO 317 317 ?   ?   ?   A . n 
A 1 318 LEU 318 318 ?   ?   ?   A . n 
A 1 319 LEU 319 319 ?   ?   ?   A . n 
A 1 320 GLU 320 320 ?   ?   ?   A . n 
A 1 321 HIS 321 321 ?   ?   ?   A . n 
A 1 322 HIS 322 322 ?   ?   ?   A . n 
A 1 323 HIS 323 323 ?   ?   ?   A . n 
A 1 324 HIS 324 324 ?   ?   ?   A . n 
A 1 325 HIS 325 325 ?   ?   ?   A . n 
A 1 326 HIS 326 326 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   ASN 3   3   3   ASN ASN B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  SER 11  11  11  SER SER B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  GLN 13  13  13  GLN GLN B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  GLN 17  17  17  GLN GLN B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  LYS 33  33  33  LYS LYS B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  PHE 35  35  35  PHE PHE B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  CYS 41  41  41  CYS CYS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  CYS 60  60  60  CYS CYS B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  MET 68  68  68  MET MET B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ILE 72  72  72  ILE ILE B . n 
B 1 73  MET 73  73  73  MET MET B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  CYS 77  77  77  CYS CYS B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  PRO 90  90  90  PRO PRO B . n 
B 1 91  CYS 91  91  91  CYS CYS B . n 
B 1 92  PHE 92  92  92  PHE PHE B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  GLN 97  97  97  GLN GLN B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ASN 114 114 114 ASN ASN B . n 
B 1 115 MET 115 115 115 MET MET B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 HIS 123 123 123 HIS HIS B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 THR 126 126 126 THR THR B . n 
B 1 127 MET 127 127 127 MET MET B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 HIS 130 130 130 HIS HIS B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 SER 132 132 132 SER SER B . n 
B 1 133 GLN 133 133 133 GLN GLN B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 PHE 137 137 137 PHE PHE B . n 
B 1 138 PHE 138 138 138 PHE PHE B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 ILE 140 140 140 ILE ILE B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 TYR 146 146 146 TYR TYR B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 TRP 154 154 154 TRP TRP B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 GLU 157 157 157 GLU GLU B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 ILE 159 159 159 ILE ILE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 TRP 162 162 162 TRP TRP B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 ASN 164 164 164 ASN ASN B . n 
B 1 165 CYS 165 165 165 CYS CYS B . n 
B 1 166 THR 166 166 166 THR THR B . n 
B 1 167 ILE 167 167 167 ILE ILE B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 ASP 171 171 171 ASP ASP B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 LYS 176 176 176 LYS LYS B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 SER 180 180 180 SER SER B . n 
B 1 181 ILE 181 181 181 ILE ILE B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 ASP 183 183 183 ASP ASP B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 PHE 189 189 189 PHE PHE B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 HIS 193 193 193 HIS HIS B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 ARG 196 196 ?   ?   ?   B . n 
B 1 197 LYS 197 197 ?   ?   ?   B . n 
B 1 198 LYS 198 198 ?   ?   ?   B . n 
B 1 199 ALA 199 199 ?   ?   ?   B . n 
B 1 200 ASN 200 200 ?   ?   ?   B . n 
B 1 201 GLU 201 201 ?   ?   ?   B . n 
B 1 202 VAL 202 202 ?   ?   ?   B . n 
B 1 203 ASP 203 203 203 ASP ASP B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 MET 205 205 205 MET MET B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 VAL 208 208 208 VAL VAL B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 ASP 210 210 210 ASP ASP B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 ASP 213 213 213 ASP ASP B . n 
B 1 214 ARG 214 214 214 ARG ARG B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 ALA 216 216 216 ALA ALA B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 VAL 219 219 219 VAL VAL B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 MET 222 222 222 MET MET B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 ASP 224 224 224 ASP ASP B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 CYS 226 226 226 CYS CYS B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 THR 228 228 228 THR THR B . n 
B 1 229 ILE 229 229 229 ILE ILE B . n 
B 1 230 CYS 230 230 230 CYS CYS B . n 
B 1 231 HIS 231 231 231 HIS HIS B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 ASP 234 234 234 ASP ASP B . n 
B 1 235 LYS 235 235 235 LYS LYS B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 ALA 239 239 239 ALA ALA B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 ARG 243 243 243 ARG ARG B . n 
B 1 244 VAL 244 244 244 VAL VAL B . n 
B 1 245 TYR 245 245 245 TYR TYR B . n 
B 1 246 ALA 246 246 246 ALA ALA B . n 
B 1 247 ILE 247 247 247 ILE ILE B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 THR 249 249 249 THR THR B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 ILE 252 252 252 ILE ILE B . n 
B 1 253 PHE 253 253 253 PHE PHE B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 PRO 256 256 256 PRO PRO B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 SER 259 259 259 SER SER B . n 
B 1 260 ARG 260 260 260 ARG ARG B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 ASN 262 262 262 ASN ASN B . n 
B 1 263 ASN 263 263 263 ASN ASN B . n 
B 1 264 ALA 264 264 264 ALA ALA B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 PHE 266 266 266 PHE PHE B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 ALA 268 268 268 ALA ALA B . n 
B 1 269 VAL 269 269 269 VAL VAL B . n 
B 1 270 VAL 270 270 270 VAL VAL B . n 
B 1 271 VAL 271 271 271 VAL VAL B . n 
B 1 272 THR 272 272 272 THR THR B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 THR 274 274 274 THR THR B . n 
B 1 275 ILE 275 275 275 ILE ILE B . n 
B 1 276 PRO 276 276 276 PRO PRO B . n 
B 1 277 GLN 277 277 277 GLN GLN B . n 
B 1 278 GLU 278 278 278 GLU GLU B . n 
B 1 279 ASP 279 279 279 ASP ASP B . n 
B 1 280 LYS 280 280 280 LYS LYS B . n 
B 1 281 MET 281 281 281 MET MET B . n 
B 1 282 LYS 282 282 282 LYS LYS B . n 
B 1 283 HIS 283 283 283 HIS HIS B . n 
B 1 284 CYS 284 284 284 CYS CYS B . n 
B 1 285 SER 285 285 285 SER SER B . n 
B 1 286 LYS 286 286 286 LYS LYS B . n 
B 1 287 ILE 287 287 287 ILE ILE B . n 
B 1 288 GLN 288 288 288 GLN GLN B . n 
B 1 289 VAL 289 289 289 VAL VAL B . n 
B 1 290 ILE 290 290 290 ILE ILE B . n 
B 1 291 ASP 291 291 291 ASP ASP B . n 
B 1 292 ILE 292 292 292 ILE ILE B . n 
B 1 293 SER 293 293 293 SER SER B . n 
B 1 294 MET 294 294 294 MET MET B . n 
B 1 295 ILE 295 295 295 ILE ILE B . n 
B 1 296 LEU 296 296 296 LEU LEU B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 GLU 298 298 298 GLU GLU B . n 
B 1 299 ALA 299 299 299 ALA ALA B . n 
B 1 300 ILE 300 300 300 ILE ILE B . n 
B 1 301 ARG 301 301 301 ARG ARG B . n 
B 1 302 ARG 302 302 302 ARG ARG B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 HIS 304 304 304 HIS HIS B . n 
B 1 305 ASN 305 305 305 ASN ASN B . n 
B 1 306 GLY 306 306 306 GLY GLY B . n 
B 1 307 GLU 307 307 307 GLU GLU B . n 
B 1 308 SER 308 308 308 SER SER B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 SER 310 310 310 SER SER B . n 
B 1 311 TYR 311 311 311 TYR TYR B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 PHE 313 313 313 PHE PHE B . n 
B 1 314 SER 314 314 314 SER SER B . n 
B 1 315 HIS 315 315 315 HIS HIS B . n 
B 1 316 VAL 316 316 316 VAL VAL B . n 
B 1 317 PRO 317 317 317 PRO PRO B . n 
B 1 318 LEU 318 318 ?   ?   ?   B . n 
B 1 319 LEU 319 319 ?   ?   ?   B . n 
B 1 320 GLU 320 320 ?   ?   ?   B . n 
B 1 321 HIS 321 321 ?   ?   ?   B . n 
B 1 322 HIS 322 322 ?   ?   ?   B . n 
B 1 323 HIS 323 323 ?   ?   ?   B . n 
B 1 324 HIS 324 324 ?   ?   ?   B . n 
B 1 325 HIS 325 325 ?   ?   ?   B . n 
B 1 326 HIS 326 326 ?   ?   ?   B . n 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA,PQS 
_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)' 28920 ? 
1 MORE         -443  ? 
1 'SSA (A^2)'  59120 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z         1.0000000000  0.0000000000  0.0000000000 0.0000000000    0.0000000000  
1.0000000000  0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_455 -y-1,x-y,z    -0.5000000000 -0.8660254038 0.0000000000 -169.6830000000 0.8660254038  
-0.5000000000 0.0000000000 0.0000000000    0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_445 -x+y-1,-x-1,z -0.5000000000 0.8660254038  0.0000000000 -84.8415000000  -0.8660254038 
-0.5000000000 0.0000000000 -146.9497885904 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 2006-10-24 
2 'Structure model' 1 1 2008-05-01 
3 'Structure model' 1 2 2011-07-13 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Derived calculations'      
3 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNS      refinement        1.1 ? 1 
ADSC     'data collection' .   ? 2 
HKL-2000 'data scaling'    .   ? 3 
CNS      phasing           .   ? 4 
# 
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 A 10  ? ? 45.27   -170.58 
2  1 GLN A 13  ? ? -147.87 -2.25   
3  1 PHE A 35  ? ? -53.93  -151.29 
4  1 SER A 36  ? ? -65.89  -92.30  
5  1 ASN A 37  ? ? -62.98  30.87   
6  1 GLU A 62  ? ? -64.65  94.86   
7  1 ILE A 107 ? ? -107.30 66.42   
8  1 ASN A 164 ? ? -140.39 58.60   
9  1 ASP A 224 ? ? -96.10  -84.31  
10 1 ILE A 252 ? ? -89.22  45.80   
11 1 PHE A 253 ? ? -52.01  84.01   
12 1 ALA A 268 ? ? 173.27  158.09  
13 1 SER B 10  ? ? -126.45 -142.22 
14 1 ASP B 14  ? ? -17.95  -87.66  
15 1 ASN B 37  ? ? -66.94  6.91    
16 1 SER B 58  ? ? -63.43  -163.64 
17 1 CYS B 60  ? ? -38.46  -27.77  
18 1 TYR B 94  ? ? 55.98   18.77   
19 1 ILE B 107 ? ? -103.99 72.96   
20 1 ASP B 224 ? ? -110.91 -91.46  
21 1 CYS B 265 ? ? -97.07  34.51   
22 1 SER B 314 ? ? -140.56 19.62   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A PRO 2   ? A PRO 2   
3  1 Y 1 A LYS 197 ? A LYS 197 
4  1 Y 1 A LYS 198 ? A LYS 198 
5  1 Y 1 A ALA 199 ? A ALA 199 
6  1 Y 1 A ASN 200 ? A ASN 200 
7  1 Y 1 A GLU 201 ? A GLU 201 
8  1 Y 1 A VAL 202 ? A VAL 202 
9  1 Y 1 A SER 314 ? A SER 314 
10 1 Y 1 A HIS 315 ? A HIS 315 
11 1 Y 1 A VAL 316 ? A VAL 316 
12 1 Y 1 A PRO 317 ? A PRO 317 
13 1 Y 1 A LEU 318 ? A LEU 318 
14 1 Y 1 A LEU 319 ? A LEU 319 
15 1 Y 1 A GLU 320 ? A GLU 320 
16 1 Y 1 A HIS 321 ? A HIS 321 
17 1 Y 1 A HIS 322 ? A HIS 322 
18 1 Y 1 A HIS 323 ? A HIS 323 
19 1 Y 1 A HIS 324 ? A HIS 324 
20 1 Y 1 A HIS 325 ? A HIS 325 
21 1 Y 1 A HIS 326 ? A HIS 326 
22 1 Y 1 B MET 1   ? B MET 1   
23 1 Y 1 B PRO 2   ? B PRO 2   
24 1 Y 1 B ARG 196 ? B ARG 196 
25 1 Y 1 B LYS 197 ? B LYS 197 
26 1 Y 1 B LYS 198 ? B LYS 198 
27 1 Y 1 B ALA 199 ? B ALA 199 
28 1 Y 1 B ASN 200 ? B ASN 200 
29 1 Y 1 B GLU 201 ? B GLU 201 
30 1 Y 1 B VAL 202 ? B VAL 202 
31 1 Y 1 B LEU 318 ? B LEU 318 
32 1 Y 1 B LEU 319 ? B LEU 319 
33 1 Y 1 B GLU 320 ? B GLU 320 
34 1 Y 1 B HIS 321 ? B HIS 321 
35 1 Y 1 B HIS 322 ? B HIS 322 
36 1 Y 1 B HIS 323 ? B HIS 323 
37 1 Y 1 B HIS 324 ? B HIS 324 
38 1 Y 1 B HIS 325 ? B HIS 325 
39 1 Y 1 B HIS 326 ? B HIS 326 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SO4 1   1002 1002 SO4 SO4 A . 
D 2 SO4 1   1004 1004 SO4 SO4 A . 
E 2 SO4 1   1006 1006 SO4 SO4 A . 
F 2 SO4 1   1001 1001 SO4 SO4 B . 
G 2 SO4 1   1003 1003 SO4 SO4 B . 
H 2 SO4 1   1005 1005 SO4 SO4 B . 
I 3 HOH 1   1007 7    HOH TIP A . 
I 3 HOH 2   1008 8    HOH TIP A . 
I 3 HOH 3   1009 10   HOH TIP A . 
I 3 HOH 4   1010 13   HOH TIP A . 
I 3 HOH 5   1011 15   HOH TIP A . 
I 3 HOH 6   1012 16   HOH TIP A . 
I 3 HOH 7   1013 19   HOH TIP A . 
I 3 HOH 8   1014 21   HOH TIP A . 
I 3 HOH 9   1015 22   HOH TIP A . 
I 3 HOH 10  1016 23   HOH TIP A . 
I 3 HOH 11  1017 26   HOH TIP A . 
I 3 HOH 12  1018 28   HOH TIP A . 
I 3 HOH 13  1019 32   HOH TIP A . 
I 3 HOH 14  1020 33   HOH TIP A . 
I 3 HOH 15  1021 35   HOH TIP A . 
I 3 HOH 16  1022 46   HOH TIP A . 
I 3 HOH 17  1023 48   HOH TIP A . 
I 3 HOH 18  1024 50   HOH TIP A . 
I 3 HOH 19  1025 52   HOH TIP A . 
I 3 HOH 20  1026 53   HOH TIP A . 
I 3 HOH 21  1027 55   HOH TIP A . 
I 3 HOH 22  1028 69   HOH TIP A . 
I 3 HOH 23  1029 72   HOH TIP A . 
I 3 HOH 24  1030 73   HOH TIP A . 
I 3 HOH 25  1031 75   HOH TIP A . 
I 3 HOH 26  1032 77   HOH TIP A . 
I 3 HOH 27  1033 81   HOH TIP A . 
I 3 HOH 28  1034 82   HOH TIP A . 
I 3 HOH 29  1035 95   HOH TIP A . 
I 3 HOH 30  1036 96   HOH TIP A . 
I 3 HOH 31  1037 98   HOH TIP A . 
I 3 HOH 32  1038 99   HOH TIP A . 
I 3 HOH 33  1039 100  HOH TIP A . 
I 3 HOH 34  1040 101  HOH TIP A . 
I 3 HOH 35  1041 103  HOH TIP A . 
I 3 HOH 36  1042 104  HOH TIP A . 
I 3 HOH 37  1043 105  HOH TIP A . 
I 3 HOH 38  1044 106  HOH TIP A . 
I 3 HOH 39  1045 107  HOH TIP A . 
I 3 HOH 40  1046 108  HOH TIP A . 
I 3 HOH 41  1047 109  HOH TIP A . 
I 3 HOH 42  1048 110  HOH TIP A . 
I 3 HOH 43  1049 112  HOH TIP A . 
I 3 HOH 44  1050 135  HOH TIP A . 
I 3 HOH 45  1051 138  HOH TIP A . 
I 3 HOH 46  1052 139  HOH TIP A . 
I 3 HOH 47  1053 140  HOH TIP A . 
I 3 HOH 48  1054 141  HOH TIP A . 
I 3 HOH 49  1055 142  HOH TIP A . 
I 3 HOH 50  1056 143  HOH TIP A . 
I 3 HOH 51  1057 144  HOH TIP A . 
I 3 HOH 52  1058 145  HOH TIP A . 
I 3 HOH 53  1059 146  HOH TIP A . 
I 3 HOH 54  1060 147  HOH TIP A . 
I 3 HOH 55  1061 148  HOH TIP A . 
I 3 HOH 56  1062 151  HOH TIP A . 
I 3 HOH 57  1063 152  HOH TIP A . 
I 3 HOH 58  1064 153  HOH TIP A . 
I 3 HOH 59  1065 154  HOH TIP A . 
I 3 HOH 60  1066 156  HOH TIP A . 
I 3 HOH 61  1067 159  HOH TIP A . 
I 3 HOH 62  1068 165  HOH TIP A . 
I 3 HOH 63  1069 166  HOH TIP A . 
I 3 HOH 64  1070 167  HOH TIP A . 
I 3 HOH 65  1071 168  HOH TIP A . 
I 3 HOH 66  1072 169  HOH TIP A . 
I 3 HOH 67  1073 173  HOH TIP A . 
I 3 HOH 68  1074 174  HOH TIP A . 
I 3 HOH 69  1075 175  HOH TIP A . 
I 3 HOH 70  1076 177  HOH TIP A . 
I 3 HOH 71  1077 178  HOH TIP A . 
I 3 HOH 72  1078 182  HOH TIP A . 
J 3 HOH 1   1006 1    HOH TIP B . 
J 3 HOH 2   1007 2    HOH TIP B . 
J 3 HOH 3   1008 3    HOH TIP B . 
J 3 HOH 4   1009 4    HOH TIP B . 
J 3 HOH 5   1010 5    HOH TIP B . 
J 3 HOH 6   1011 6    HOH TIP B . 
J 3 HOH 7   1012 9    HOH TIP B . 
J 3 HOH 8   1013 11   HOH TIP B . 
J 3 HOH 9   1014 12   HOH TIP B . 
J 3 HOH 10  1015 14   HOH TIP B . 
J 3 HOH 11  1016 17   HOH TIP B . 
J 3 HOH 12  1017 18   HOH TIP B . 
J 3 HOH 13  1018 20   HOH TIP B . 
J 3 HOH 14  1019 24   HOH TIP B . 
J 3 HOH 15  1020 25   HOH TIP B . 
J 3 HOH 16  1021 27   HOH TIP B . 
J 3 HOH 17  1022 29   HOH TIP B . 
J 3 HOH 18  1023 30   HOH TIP B . 
J 3 HOH 19  1024 31   HOH TIP B . 
J 3 HOH 20  1025 34   HOH TIP B . 
J 3 HOH 21  1026 36   HOH TIP B . 
J 3 HOH 22  1027 37   HOH TIP B . 
J 3 HOH 23  1028 38   HOH TIP B . 
J 3 HOH 24  1029 39   HOH TIP B . 
J 3 HOH 25  1030 40   HOH TIP B . 
J 3 HOH 26  1031 41   HOH TIP B . 
J 3 HOH 27  1032 42   HOH TIP B . 
J 3 HOH 28  1033 43   HOH TIP B . 
J 3 HOH 29  1034 44   HOH TIP B . 
J 3 HOH 30  1035 45   HOH TIP B . 
J 3 HOH 31  1036 47   HOH TIP B . 
J 3 HOH 32  1037 49   HOH TIP B . 
J 3 HOH 33  1038 51   HOH TIP B . 
J 3 HOH 34  1039 54   HOH TIP B . 
J 3 HOH 35  1040 56   HOH TIP B . 
J 3 HOH 36  1041 57   HOH TIP B . 
J 3 HOH 37  1042 58   HOH TIP B . 
J 3 HOH 38  1043 59   HOH TIP B . 
J 3 HOH 39  1044 60   HOH TIP B . 
J 3 HOH 40  1045 61   HOH TIP B . 
J 3 HOH 41  1046 62   HOH TIP B . 
J 3 HOH 42  1047 63   HOH TIP B . 
J 3 HOH 43  1048 64   HOH TIP B . 
J 3 HOH 44  1049 65   HOH TIP B . 
J 3 HOH 45  1050 66   HOH TIP B . 
J 3 HOH 46  1051 67   HOH TIP B . 
J 3 HOH 47  1052 68   HOH TIP B . 
J 3 HOH 48  1053 70   HOH TIP B . 
J 3 HOH 49  1054 71   HOH TIP B . 
J 3 HOH 50  1055 74   HOH TIP B . 
J 3 HOH 51  1056 76   HOH TIP B . 
J 3 HOH 52  1057 78   HOH TIP B . 
J 3 HOH 53  1058 79   HOH TIP B . 
J 3 HOH 54  1059 80   HOH TIP B . 
J 3 HOH 55  1060 83   HOH TIP B . 
J 3 HOH 56  1061 84   HOH TIP B . 
J 3 HOH 57  1062 85   HOH TIP B . 
J 3 HOH 58  1063 86   HOH TIP B . 
J 3 HOH 59  1064 87   HOH TIP B . 
J 3 HOH 60  1065 88   HOH TIP B . 
J 3 HOH 61  1066 89   HOH TIP B . 
J 3 HOH 62  1067 90   HOH TIP B . 
J 3 HOH 63  1068 91   HOH TIP B . 
J 3 HOH 64  1069 92   HOH TIP B . 
J 3 HOH 65  1070 93   HOH TIP B . 
J 3 HOH 66  1071 94   HOH TIP B . 
J 3 HOH 67  1072 97   HOH TIP B . 
J 3 HOH 68  1073 102  HOH TIP B . 
J 3 HOH 69  1074 111  HOH TIP B . 
J 3 HOH 70  1075 113  HOH TIP B . 
J 3 HOH 71  1076 114  HOH TIP B . 
J 3 HOH 72  1077 115  HOH TIP B . 
J 3 HOH 73  1078 116  HOH TIP B . 
J 3 HOH 74  1079 117  HOH TIP B . 
J 3 HOH 75  1080 118  HOH TIP B . 
J 3 HOH 76  1081 119  HOH TIP B . 
J 3 HOH 77  1082 120  HOH TIP B . 
J 3 HOH 78  1083 121  HOH TIP B . 
J 3 HOH 79  1084 122  HOH TIP B . 
J 3 HOH 80  1085 123  HOH TIP B . 
J 3 HOH 81  1086 124  HOH TIP B . 
J 3 HOH 82  1087 125  HOH TIP B . 
J 3 HOH 83  1088 126  HOH TIP B . 
J 3 HOH 84  1089 127  HOH TIP B . 
J 3 HOH 85  1090 128  HOH TIP B . 
J 3 HOH 86  1091 129  HOH TIP B . 
J 3 HOH 87  1092 130  HOH TIP B . 
J 3 HOH 88  1093 131  HOH TIP B . 
J 3 HOH 89  1094 132  HOH TIP B . 
J 3 HOH 90  1095 133  HOH TIP B . 
J 3 HOH 91  1096 134  HOH TIP B . 
J 3 HOH 92  1097 136  HOH TIP B . 
J 3 HOH 93  1098 137  HOH TIP B . 
J 3 HOH 94  1099 149  HOH TIP B . 
J 3 HOH 95  1100 150  HOH TIP B . 
J 3 HOH 96  1101 155  HOH TIP B . 
J 3 HOH 97  1102 157  HOH TIP B . 
J 3 HOH 98  1103 158  HOH TIP B . 
J 3 HOH 99  1104 160  HOH TIP B . 
J 3 HOH 100 1105 161  HOH TIP B . 
J 3 HOH 101 1106 162  HOH TIP B . 
J 3 HOH 102 1107 163  HOH TIP B . 
J 3 HOH 103 1108 164  HOH TIP B . 
J 3 HOH 104 1109 170  HOH TIP B . 
J 3 HOH 105 1110 171  HOH TIP B . 
J 3 HOH 106 1111 172  HOH TIP B . 
J 3 HOH 107 1112 176  HOH TIP B . 
J 3 HOH 108 1113 179  HOH TIP B . 
J 3 HOH 109 1114 180  HOH TIP B . 
J 3 HOH 110 1115 181  HOH TIP B . 
J 3 HOH 111 1116 183  HOH TIP B . 
# 
