data_2H07
# 
_entry.id   2H07 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.351 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   2H07         pdb_00002h07 10.2210/pdb2h07/pdb 
RCSB  RCSB037765   ?            ?                   
WWPDB D_1000037765 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 2H06 'the same protein(wild type)' unspecified 
PDB 2H08 'the same protein(Y146M)'     unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2H07 
_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                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
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 
_citation_author.identifier_ORCID 
primary 'Li, S.'   1 ? 
primary 'Lu, Y.'   2 ? 
primary 'Peng, B.' 3 ? 
primary 'Ding, J.' 4 ? 
# 
_cell.entry_id           2H07 
_cell.length_a           170.339 
_cell.length_b           170.339 
_cell.length_c           61.720 
_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                         2H07 
_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' 35934.375 2   2.7.6.1 S132A ? ? 
2 non-polymer syn 'SULFATE ION'                          96.063    6   ?       ?     ? ? 
3 water       nat water                                  18.015    132 ?       ?     ? ? 
# 
_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
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHAAQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHAAQIQGFFDIPVDNLYAEPAVLKWIRENIS
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 ALA 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           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 2H07 A 1 ? 318 ? P60891 1 ? 318 ? 1 318 
2 1 2H07 B 1 ? 318 ? P60891 1 ? 318 ? 1 318 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2H07 ALA A 132 ? UNP P60891 SER 132 'engineered mutation' 132 1  
1 2H07 LEU A 319 ? UNP P60891 ?   ?   'expression tag'      319 2  
1 2H07 GLU A 320 ? UNP P60891 ?   ?   'expression tag'      320 3  
1 2H07 HIS A 321 ? UNP P60891 ?   ?   'expression tag'      321 4  
1 2H07 HIS A 322 ? UNP P60891 ?   ?   'expression tag'      322 5  
1 2H07 HIS A 323 ? UNP P60891 ?   ?   'expression tag'      323 6  
1 2H07 HIS A 324 ? UNP P60891 ?   ?   'expression tag'      324 7  
1 2H07 HIS A 325 ? UNP P60891 ?   ?   'expression tag'      325 8  
1 2H07 HIS A 326 ? UNP P60891 ?   ?   'expression tag'      326 9  
2 2H07 ALA B 132 ? UNP P60891 SER 132 'engineered mutation' 132 10 
2 2H07 LEU B 319 ? UNP P60891 ?   ?   'expression tag'      319 11 
2 2H07 GLU B 320 ? UNP P60891 ?   ?   'expression tag'      320 12 
2 2H07 HIS B 321 ? UNP P60891 ?   ?   'expression tag'      321 13 
2 2H07 HIS B 322 ? UNP P60891 ?   ?   'expression tag'      322 14 
2 2H07 HIS B 323 ? UNP P60891 ?   ?   'expression tag'      323 15 
2 2H07 HIS B 324 ? UNP P60891 ?   ?   'expression tag'      324 16 
2 2H07 HIS B 325 ? UNP P60891 ?   ?   'expression tag'      325 17 
2 2H07 HIS B 326 ? UNP P60891 ?   ?   'expression tag'      326 18 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          2H07 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.40 
_exptl_crystal.density_percent_sol   48.69 
_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              4.3 
_exptl_crystal_grow.pdbx_details    
;0.1M citric acid, 1.3M ammonium sulfate, 0.02M sodium dihydrogen phosphate, 0.4M sodium chloride, pH 4.3, 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               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS IV' 
_diffrn_detector.pdbx_collection_date   2005-06-28 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        RIGAKU 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
# 
_reflns.entry_id                     2H07 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             25.0 
_reflns.d_resolution_high            2.2 
_reflns.number_obs                   33483 
_reflns.number_all                   33884 
_reflns.percent_possible_obs         98.8 
_reflns.pdbx_Rmerge_I_obs            0.067 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        8.6 
_reflns.B_iso_Wilson_estimate        29.8 
_reflns.pdbx_redundancy              4.2 
_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   97.7 
_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                                 2H07 
_refine.ls_number_reflns_obs                     33483 
_refine.ls_number_reflns_all                     33905 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               2601941.55 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             20.00 
_refine.ls_d_res_high                            2.20 
_refine.ls_percent_reflns_obs                    98.7 
_refine.ls_R_factor_obs                          0.218 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.218 
_refine.ls_R_factor_R_free                       0.254 
_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                  1680 
_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                               39.6 
_refine.aniso_B[1][1]                            1.98 
_refine.aniso_B[2][2]                            1.98 
_refine.aniso_B[3][3]                            -3.96 
_refine.aniso_B[1][2]                            4.00 
_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                 0.420705 
_refine.solvent_model_param_bsol                 72.5285 
_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                      2H06 
_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                        2H07 
_refine_analyze.Luzzati_coordinate_error_obs    0.27 
_refine_analyze.Luzzati_sigma_a_obs             0.24 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.33 
_refine_analyze.Luzzati_sigma_a_free            0.32 
_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        4689 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             132 
_refine_hist.number_atoms_total               4851 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        20.00 
# 
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                0.006 ? ? ? '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      0.76  ? ? ? '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             5281 
_refine_ls_shell.R_factor_R_work                  0.266 
_refine_ls_shell.percent_reflns_obs               98.3 
_refine_ls_shell.R_factor_R_free                  0.314 
_refine_ls_shell.R_factor_R_free_error            0.019 
_refine_ls_shell.percent_reflns_R_free            5.1 
_refine_ls_shell.number_reflns_R_free             282 
_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                  2H07 
_struct.title                     'crystal structure of human phosphoribosyl pyrophosphate synthetase 1 mutant S132A' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2H07 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'PRS1, prpp synthetase 1, phosphoribosyl pyrophosphate synthetase 1, mutant, 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  ? LEU A 23  ? GLN A 13  LEU A 23  1 ? 11 
HELX_P HELX_P2  2  GLU A 62  ? ALA A 80  ? GLU A 62  ALA A 80  1 ? 19 
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 ? ILE A 159 ? ALA A 147 ILE A 159 1 ? 13 
HELX_P HELX_P6  6  SER A 160 ? ASN A 164 ? SER A 160 ASN A 164 5 ? 5  
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 ? ASN A 263 ? PRO A 256 ASN A 263 1 ? 8  
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 ? ASN B 263 ? PRO B 256 ASN B 263 1 ? 8  
HELX_P HELX_P24 24 GLN B 277 ? HIS B 283 ? GLN B 277 HIS B 283 1 ? 7  
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 ? HIS B 315 ? VAL B 309 HIS B 315 5 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
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  ? THR A 32  ? VAL A 30  THR A 32  
B 2 VAL A 42  ? ILE A 44  ? VAL A 42  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 ALA A 216 ? ALA A 223 ? ALA A 216 ALA A 223 
C 5 VAL A 244 ? GLY A 251 ? VAL A 244 GLY A 251 
C 6 VAL A 269 ? THR A 272 ? VAL A 269 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 ? GLY B 209 ? MET B 205 GLY B 209 
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 ALA B 216 ? ALA B 223 ? ALA B 216 ALA B 223 
F 5 VAL B 244 ? GLY B 251 ? VAL B 244 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 LYS A 5   ? N LYS A 5   O TYR A 54  ? O TYR A 54  
A 2 3 N VAL A 53  ? N VAL A 53  O ARG A 84  ? O ARG A 84  
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 THR B 86  ? O THR B 86  
D 3 4 N ILE B 89  ? N ILE B 89  O ILE B 125 ? O ILE B 125 
D 4 5 N ILE B 124 ? N ILE B 124 O ASP B 143 ? O ASP B 143 
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 208 ? O VAL B 208 N LEU B 191 ? N LEU B 191 
F 2 3 O ILE B 192 ? O ILE B 192 N SER B 169 ? N SER B 169 
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 ILE B 247 ? O ILE B 247 
F 5 6 N ALA B 246 ? N ALA B 246 O VAL B 270 ? O VAL B 270 
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 B SO4 1001 ? 7  'BINDING SITE FOR RESIDUE SO4 B 1001' 
AC2 Software A SO4 1002 ? 6  'BINDING SITE FOR RESIDUE SO4 A 1002' 
AC3 Software B SO4 1003 ? 7  'BINDING SITE FOR RESIDUE SO4 B 1003' 
AC4 Software A SO4 1004 ? 7  'BINDING SITE FOR RESIDUE SO4 A 1004' 
AC5 Software B SO4 1005 ? 7  'BINDING SITE FOR RESIDUE SO4 B 1005' 
AC6 Software A SO4 1006 ? 11 '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 1081 . ? 1_555 ? 
7  AC1 7  HOH J .   ? HOH B 1082 . ? 1_555 ? 
8  AC2 6  ASP A 224 ? ASP A 224  . ? 1_555 ? 
9  AC2 6  THR A 225 ? THR A 225  . ? 1_555 ? 
10 AC2 6  CYS A 226 ? CYS A 226  . ? 1_555 ? 
11 AC2 6  GLY A 227 ? GLY A 227  . ? 1_555 ? 
12 AC2 6  THR A 228 ? THR A 228  . ? 1_555 ? 
13 AC2 6  HOH I .   ? HOH A 1054 . ? 1_555 ? 
14 AC3 7  ARG A 104 ? ARG A 104  . ? 1_555 ? 
15 AC3 7  SER B 47  ? SER B 47   . ? 3_455 ? 
16 AC3 7  ARG B 49  ? ARG B 49   . ? 3_455 ? 
17 AC3 7  SER B 308 ? SER B 308  . ? 1_555 ? 
18 AC3 7  VAL B 309 ? VAL B 309  . ? 1_555 ? 
19 AC3 7  SER B 310 ? SER B 310  . ? 1_555 ? 
20 AC3 7  HOH J .   ? HOH B 1010 . ? 3_455 ? 
21 AC4 7  SER A 47  ? SER A 47   . ? 2_565 ? 
22 AC4 7  ARG A 49  ? ARG A 49   . ? 2_565 ? 
23 AC4 7  SER A 308 ? SER A 308  . ? 1_555 ? 
24 AC4 7  VAL A 309 ? VAL A 309  . ? 1_555 ? 
25 AC4 7  SER A 310 ? SER A 310  . ? 1_555 ? 
26 AC4 7  HOH I .   ? HOH A 1010 . ? 2_565 ? 
27 AC4 7  ARG B 104 ? ARG B 104  . ? 1_555 ? 
28 AC5 7  ASP A 101 ? ASP A 101  . ? 1_555 ? 
29 AC5 7  LYS A 102 ? LYS A 102  . ? 1_555 ? 
30 AC5 7  ALA B 132 ? ALA B 132  . ? 1_555 ? 
31 AC5 7  GLN B 135 ? GLN B 135  . ? 1_555 ? 
32 AC5 7  ASN B 144 ? ASN B 144  . ? 1_555 ? 
33 AC5 7  TYR B 146 ? TYR B 146  . ? 1_555 ? 
34 AC5 7  HOH J .   ? HOH B 1007 . ? 1_555 ? 
35 AC6 11 ALA A 132 ? ALA A 132  . ? 1_555 ? 
36 AC6 11 GLN A 135 ? GLN A 135  . ? 1_555 ? 
37 AC6 11 ASN A 144 ? ASN A 144  . ? 1_555 ? 
38 AC6 11 TYR A 146 ? TYR A 146  . ? 1_555 ? 
39 AC6 11 HOH I .   ? HOH A 1008 . ? 1_555 ? 
40 AC6 11 HOH I .   ? HOH A 1037 . ? 1_555 ? 
41 AC6 11 HOH I .   ? HOH A 1040 . ? 1_555 ? 
42 AC6 11 LYS B 99  ? LYS B 99   . ? 1_555 ? 
43 AC6 11 LYS B 100 ? LYS B 100  . ? 1_555 ? 
44 AC6 11 ASP B 101 ? ASP B 101  . ? 1_555 ? 
45 AC6 11 LYS B 102 ? LYS B 102  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2H07 
_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                    2H07 
_atom_sites.fract_transf_matrix[1][1]   0.005871 
_atom_sites.fract_transf_matrix[1][2]   0.003389 
_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]   0.006779 
_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]   0.016202 
_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   ? -96.873  53.545 -23.742 1.00 49.03 ? 3    ASN A N   1 
ATOM   2    C CA  . ASN A 1 3   ? -95.891  53.038 -24.743 1.00 48.77 ? 3    ASN A CA  1 
ATOM   3    C C   . ASN A 1 3   ? -96.616  52.380 -25.913 1.00 46.97 ? 3    ASN A C   1 
ATOM   4    O O   . ASN A 1 3   ? -96.143  52.410 -27.049 1.00 46.64 ? 3    ASN A O   1 
ATOM   5    C CB  . ASN A 1 3   ? -94.939  52.048 -24.075 1.00 51.51 ? 3    ASN A CB  1 
ATOM   6    C CG  . ASN A 1 3   ? -93.969  51.421 -25.049 1.00 53.39 ? 3    ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 3   ? -93.314  52.110 -25.832 1.00 55.58 ? 3    ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 3   ? -93.858  50.102 -24.994 1.00 56.08 ? 3    ASN A ND2 1 
ATOM   9    N N   . ILE A 1 4   ? -97.768  51.784 -25.629 1.00 43.29 ? 4    ILE A N   1 
ATOM   10   C CA  . ILE A 1 4   ? -98.565  51.157 -26.671 1.00 42.46 ? 4    ILE A CA  1 
ATOM   11   C C   . ILE A 1 4   ? -99.756  52.062 -27.005 1.00 41.25 ? 4    ILE A C   1 
ATOM   12   O O   . ILE A 1 4   ? -100.358 52.672 -26.120 1.00 40.59 ? 4    ILE A O   1 
ATOM   13   C CB  . ILE A 1 4   ? -99.090  49.783 -26.231 1.00 43.04 ? 4    ILE A CB  1 
ATOM   14   C CG1 . ILE A 1 4   ? -100.030 49.223 -27.297 1.00 42.00 ? 4    ILE A CG1 1 
ATOM   15   C CG2 . ILE A 1 4   ? -99.812  49.907 -24.898 1.00 45.52 ? 4    ILE A CG2 1 
ATOM   16   C CD1 . ILE A 1 4   ? -100.498 47.820 -27.017 1.00 43.86 ? 4    ILE A CD1 1 
ATOM   17   N N   . LYS A 1 5   ? -100.087 52.150 -28.287 1.00 39.07 ? 5    LYS A N   1 
ATOM   18   C CA  . LYS A 1 5   ? -101.197 52.979 -28.726 1.00 37.01 ? 5    LYS A CA  1 
ATOM   19   C C   . LYS A 1 5   ? -102.033 52.285 -29.790 1.00 35.97 ? 5    LYS A C   1 
ATOM   20   O O   . LYS A 1 5   ? -101.503 51.756 -30.766 1.00 34.82 ? 5    LYS A O   1 
ATOM   21   C CB  . LYS A 1 5   ? -100.674 54.316 -29.248 1.00 39.10 ? 5    LYS A CB  1 
ATOM   22   C CG  . LYS A 1 5   ? -100.710 55.426 -28.211 1.00 44.71 ? 5    LYS A CG  1 
ATOM   23   C CD  . LYS A 1 5   ? -102.163 55.806 -27.922 1.00 49.20 ? 5    LYS A CD  1 
ATOM   24   C CE  . LYS A 1 5   ? -102.304 56.697 -26.703 1.00 50.07 ? 5    LYS A CE  1 
ATOM   25   N NZ  . LYS A 1 5   ? -103.743 57.004 -26.430 1.00 51.14 ? 5    LYS A NZ  1 
ATOM   26   N N   . ILE A 1 6   ? -103.347 52.286 -29.582 1.00 34.39 ? 6    ILE A N   1 
ATOM   27   C CA  . ILE A 1 6   ? -104.280 51.670 -30.510 1.00 35.00 ? 6    ILE A CA  1 
ATOM   28   C C   . ILE A 1 6   ? -105.233 52.711 -31.101 1.00 33.83 ? 6    ILE A C   1 
ATOM   29   O O   . ILE A 1 6   ? -105.919 53.426 -30.369 1.00 33.00 ? 6    ILE A O   1 
ATOM   30   C CB  . ILE A 1 6   ? -105.131 50.576 -29.821 1.00 35.92 ? 6    ILE A CB  1 
ATOM   31   C CG1 . ILE A 1 6   ? -104.220 49.566 -29.120 1.00 40.08 ? 6    ILE A CG1 1 
ATOM   32   C CG2 . ILE A 1 6   ? -105.985 49.851 -30.860 1.00 33.99 ? 6    ILE A CG2 1 
ATOM   33   C CD1 . ILE A 1 6   ? -104.969 48.425 -28.442 1.00 40.95 ? 6    ILE A CD1 1 
ATOM   34   N N   . PHE A 1 7   ? -105.252 52.785 -32.430 1.00 32.25 ? 7    PHE A N   1 
ATOM   35   C CA  . PHE A 1 7   ? -106.116 53.697 -33.169 1.00 31.84 ? 7    PHE A CA  1 
ATOM   36   C C   . PHE A 1 7   ? -107.064 52.870 -34.043 1.00 34.77 ? 7    PHE A C   1 
ATOM   37   O O   . PHE A 1 7   ? -106.775 51.720 -34.385 1.00 34.23 ? 7    PHE A O   1 
ATOM   38   C CB  . PHE A 1 7   ? -105.303 54.622 -34.087 1.00 29.23 ? 7    PHE A CB  1 
ATOM   39   C CG  . PHE A 1 7   ? -104.416 55.604 -33.361 1.00 27.78 ? 7    PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 7   ? -103.166 55.223 -32.890 1.00 29.63 ? 7    PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 7   ? -104.825 56.916 -33.171 1.00 25.67 ? 7    PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 7   ? -102.336 56.147 -32.243 1.00 30.01 ? 7    PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 7   ? -104.007 57.842 -32.530 1.00 25.91 ? 7    PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 7   ? -102.763 57.459 -32.065 1.00 27.65 ? 7    PHE A CZ  1 
ATOM   45   N N   . SER A 1 8   ? -108.190 53.472 -34.404 1.00 38.69 ? 8    SER A N   1 
ATOM   46   C CA  . SER A 1 8   ? -109.191 52.837 -35.246 1.00 44.09 ? 8    SER A CA  1 
ATOM   47   C C   . SER A 1 8   ? -109.500 53.751 -36.426 1.00 49.08 ? 8    SER A C   1 
ATOM   48   O O   . SER A 1 8   ? -109.152 54.931 -36.413 1.00 46.91 ? 8    SER A O   1 
ATOM   49   C CB  . SER A 1 8   ? -110.471 52.602 -34.453 1.00 44.94 ? 8    SER A CB  1 
ATOM   50   O OG  . SER A 1 8   ? -111.510 52.141 -35.295 1.00 45.39 ? 8    SER A OG  1 
ATOM   51   N N   . GLY A 1 9   ? -110.161 53.200 -37.439 1.00 56.38 ? 9    GLY A N   1 
ATOM   52   C CA  . GLY A 1 9   ? -110.517 53.986 -38.607 1.00 64.19 ? 9    GLY A CA  1 
ATOM   53   C C   . GLY A 1 9   ? -112.013 54.078 -38.867 1.00 68.77 ? 9    GLY A C   1 
ATOM   54   O O   . GLY A 1 9   ? -112.787 53.223 -38.441 1.00 71.18 ? 9    GLY A O   1 
ATOM   55   N N   . SER A 1 10  ? -112.412 55.138 -39.566 1.00 73.83 ? 10   SER A N   1 
ATOM   56   C CA  . SER A 1 10  ? -113.802 55.396 -39.942 1.00 77.45 ? 10   SER A CA  1 
ATOM   57   C C   . SER A 1 10  ? -114.872 55.122 -38.885 1.00 79.61 ? 10   SER A C   1 
ATOM   58   O O   . SER A 1 10  ? -114.574 54.809 -37.732 1.00 80.33 ? 10   SER A O   1 
ATOM   59   C CB  . SER A 1 10  ? -114.141 54.622 -41.221 1.00 78.33 ? 10   SER A CB  1 
ATOM   60   O OG  . SER A 1 10  ? -115.420 54.974 -41.718 1.00 77.88 ? 10   SER A OG  1 
ATOM   61   N N   . SER A 1 11  ? -116.127 55.256 -39.308 1.00 82.12 ? 11   SER A N   1 
ATOM   62   C CA  . SER A 1 11  ? -117.290 55.056 -38.451 1.00 84.17 ? 11   SER A CA  1 
ATOM   63   C C   . SER A 1 11  ? -117.158 53.833 -37.547 1.00 84.36 ? 11   SER A C   1 
ATOM   64   O O   . SER A 1 11  ? -117.479 53.897 -36.359 1.00 84.75 ? 11   SER A O   1 
ATOM   65   C CB  . SER A 1 11  ? -118.550 54.935 -39.317 1.00 84.34 ? 11   SER A CB  1 
ATOM   66   O OG  . SER A 1 11  ? -119.727 54.927 -38.527 1.00 84.96 ? 11   SER A OG  1 
ATOM   67   N N   . HIS A 1 12  ? -116.689 52.723 -38.106 1.00 83.60 ? 12   HIS A N   1 
ATOM   68   C CA  . HIS A 1 12  ? -116.521 51.502 -37.326 1.00 83.02 ? 12   HIS A CA  1 
ATOM   69   C C   . HIS A 1 12  ? -115.594 51.714 -36.140 1.00 80.70 ? 12   HIS A C   1 
ATOM   70   O O   . HIS A 1 12  ? -114.554 52.359 -36.256 1.00 81.93 ? 12   HIS A O   1 
ATOM   71   C CB  . HIS A 1 12  ? -115.959 50.373 -38.197 1.00 85.71 ? 12   HIS A CB  1 
ATOM   72   C CG  . HIS A 1 12  ? -115.230 49.316 -37.421 1.00 86.80 ? 12   HIS A CG  1 
ATOM   73   N ND1 . HIS A 1 12  ? -114.098 49.586 -36.679 1.00 86.85 ? 12   HIS A ND1 1 
ATOM   74   C CD2 . HIS A 1 12  ? -115.466 47.991 -37.274 1.00 87.64 ? 12   HIS A CD2 1 
ATOM   75   C CE1 . HIS A 1 12  ? -113.670 48.475 -36.111 1.00 87.34 ? 12   HIS A CE1 1 
ATOM   76   N NE2 . HIS A 1 12  ? -114.482 47.490 -36.455 1.00 88.07 ? 12   HIS A NE2 1 
ATOM   77   N N   . GLN A 1 13  ? -115.976 51.155 -35.000 1.00 76.37 ? 13   GLN A N   1 
ATOM   78   C CA  . GLN A 1 13  ? -115.175 51.255 -33.794 1.00 71.79 ? 13   GLN A CA  1 
ATOM   79   C C   . GLN A 1 13  ? -115.561 50.154 -32.836 1.00 68.19 ? 13   GLN A C   1 
ATOM   80   O O   . GLN A 1 13  ? -114.964 50.014 -31.774 1.00 68.86 ? 13   GLN A O   1 
ATOM   81   C CB  . GLN A 1 13  ? -115.359 52.612 -33.110 1.00 74.19 ? 13   GLN A CB  1 
ATOM   82   C CG  . GLN A 1 13  ? -114.373 53.678 -33.566 1.00 75.17 ? 13   GLN A CG  1 
ATOM   83   C CD  . GLN A 1 13  ? -114.071 54.698 -32.479 1.00 76.87 ? 13   GLN A CD  1 
ATOM   84   O OE1 . GLN A 1 13  ? -113.247 55.596 -32.664 1.00 77.79 ? 13   GLN A OE1 1 
ATOM   85   N NE2 . GLN A 1 13  ? -114.736 54.560 -31.336 1.00 77.77 ? 13   GLN A NE2 1 
ATOM   86   N N   . ASP A 1 14  ? -116.561 49.367 -33.215 1.00 62.52 ? 14   ASP A N   1 
ATOM   87   C CA  . ASP A 1 14  ? -117.015 48.280 -32.364 1.00 57.93 ? 14   ASP A CA  1 
ATOM   88   C C   . ASP A 1 14  ? -115.864 47.331 -32.035 1.00 53.78 ? 14   ASP A C   1 
ATOM   89   O O   . ASP A 1 14  ? -115.529 47.128 -30.868 1.00 54.91 ? 14   ASP A O   1 
ATOM   90   C CB  . ASP A 1 14  ? -118.140 47.500 -33.045 1.00 60.60 ? 14   ASP A CB  1 
ATOM   91   C CG  . ASP A 1 14  ? -118.773 46.473 -32.125 1.00 61.09 ? 14   ASP A CG  1 
ATOM   92   O OD1 . ASP A 1 14  ? -119.082 45.356 -32.595 1.00 64.73 ? 14   ASP A OD1 1 
ATOM   93   O OD2 . ASP A 1 14  ? -118.966 46.786 -30.931 1.00 61.65 ? 14   ASP A OD2 1 
ATOM   94   N N   . LEU A 1 15  ? -115.260 46.754 -33.069 1.00 48.17 ? 15   LEU A N   1 
ATOM   95   C CA  . LEU A 1 15  ? -114.152 45.826 -32.883 1.00 43.26 ? 15   LEU A CA  1 
ATOM   96   C C   . LEU A 1 15  ? -112.986 46.521 -32.191 1.00 40.71 ? 15   LEU A C   1 
ATOM   97   O O   . LEU A 1 15  ? -112.422 45.998 -31.231 1.00 39.70 ? 15   LEU A O   1 
ATOM   98   C CB  . LEU A 1 15  ? -113.678 45.273 -34.232 1.00 40.25 ? 15   LEU A CB  1 
ATOM   99   C CG  . LEU A 1 15  ? -113.280 43.794 -34.261 1.00 39.53 ? 15   LEU A CG  1 
ATOM   100  C CD1 . LEU A 1 15  ? -112.490 43.496 -35.527 1.00 38.73 ? 15   LEU A CD1 1 
ATOM   101  C CD2 . LEU A 1 15  ? -112.453 43.452 -33.044 1.00 38.49 ? 15   LEU A CD2 1 
ATOM   102  N N   . SER A 1 16  ? -112.627 47.701 -32.688 1.00 40.15 ? 16   SER A N   1 
ATOM   103  C CA  . SER A 1 16  ? -111.524 48.472 -32.124 1.00 40.29 ? 16   SER A CA  1 
ATOM   104  C C   . SER A 1 16  ? -111.738 48.824 -30.656 1.00 38.40 ? 16   SER A C   1 
ATOM   105  O O   . SER A 1 16  ? -110.798 48.796 -29.868 1.00 37.72 ? 16   SER A O   1 
ATOM   106  C CB  . SER A 1 16  ? -111.308 49.755 -32.925 1.00 40.30 ? 16   SER A CB  1 
ATOM   107  O OG  . SER A 1 16  ? -110.772 49.459 -34.198 1.00 46.61 ? 16   SER A OG  1 
ATOM   108  N N   . GLN A 1 17  ? -112.972 49.157 -30.296 1.00 37.97 ? 17   GLN A N   1 
ATOM   109  C CA  . GLN A 1 17  ? -113.286 49.509 -28.918 1.00 38.27 ? 17   GLN A CA  1 
ATOM   110  C C   . GLN A 1 17  ? -113.174 48.278 -28.032 1.00 37.45 ? 17   GLN A C   1 
ATOM   111  O O   . GLN A 1 17  ? -112.679 48.360 -26.911 1.00 37.75 ? 17   GLN A O   1 
ATOM   112  C CB  . GLN A 1 17  ? -114.699 50.082 -28.813 1.00 40.51 ? 17   GLN A CB  1 
ATOM   113  C CG  . GLN A 1 17  ? -114.941 50.819 -27.514 1.00 43.38 ? 17   GLN A CG  1 
ATOM   114  C CD  . GLN A 1 17  ? -113.980 51.977 -27.334 1.00 44.63 ? 17   GLN A CD  1 
ATOM   115  O OE1 . GLN A 1 17  ? -114.031 52.959 -28.074 1.00 45.67 ? 17   GLN A OE1 1 
ATOM   116  N NE2 . GLN A 1 17  ? -113.089 51.864 -26.351 1.00 46.37 ? 17   GLN A NE2 1 
ATOM   117  N N   . LYS A 1 18  ? -113.638 47.138 -28.536 1.00 35.00 ? 18   LYS A N   1 
ATOM   118  C CA  . LYS A 1 18  ? -113.560 45.904 -27.769 1.00 34.66 ? 18   LYS A CA  1 
ATOM   119  C C   . LYS A 1 18  ? -112.103 45.567 -27.498 1.00 32.87 ? 18   LYS A C   1 
ATOM   120  O O   . LYS A 1 18  ? -111.724 45.253 -26.372 1.00 33.80 ? 18   LYS A O   1 
ATOM   121  C CB  . LYS A 1 18  ? -114.220 44.749 -28.524 1.00 35.31 ? 18   LYS A CB  1 
ATOM   122  C CG  . LYS A 1 18  ? -115.738 44.818 -28.582 1.00 38.48 ? 18   LYS A CG  1 
ATOM   123  C CD  . LYS A 1 18  ? -116.309 43.537 -29.182 1.00 38.98 ? 18   LYS A CD  1 
ATOM   124  C CE  . LYS A 1 18  ? -117.817 43.451 -29.003 1.00 41.90 ? 18   LYS A CE  1 
ATOM   125  N NZ  . LYS A 1 18  ? -118.547 44.595 -29.622 1.00 44.56 ? 18   LYS A NZ  1 
ATOM   126  N N   . ILE A 1 19  ? -111.285 45.635 -28.542 1.00 31.44 ? 19   ILE A N   1 
ATOM   127  C CA  . ILE A 1 19  ? -109.870 45.342 -28.409 1.00 29.25 ? 19   ILE A CA  1 
ATOM   128  C C   . ILE A 1 19  ? -109.215 46.251 -27.368 1.00 29.96 ? 19   ILE A C   1 
ATOM   129  O O   . ILE A 1 19  ? -108.521 45.766 -26.466 1.00 28.37 ? 19   ILE A O   1 
ATOM   130  C CB  . ILE A 1 19  ? -109.161 45.482 -29.772 1.00 29.54 ? 19   ILE A CB  1 
ATOM   131  C CG1 . ILE A 1 19  ? -109.635 44.353 -30.700 1.00 31.14 ? 19   ILE A CG1 1 
ATOM   132  C CG2 . ILE A 1 19  ? -107.647 45.440 -29.590 1.00 28.83 ? 19   ILE A CG2 1 
ATOM   133  C CD1 . ILE A 1 19  ? -109.244 44.520 -32.147 1.00 31.53 ? 19   ILE A CD1 1 
ATOM   134  N N   . ALA A 1 20  ? -109.455 47.559 -27.478 1.00 29.33 ? 20   ALA A N   1 
ATOM   135  C CA  . ALA A 1 20  ? -108.873 48.530 -26.548 1.00 31.18 ? 20   ALA A CA  1 
ATOM   136  C C   . ALA A 1 20  ? -109.291 48.246 -25.111 1.00 33.23 ? 20   ALA A C   1 
ATOM   137  O O   . ALA A 1 20  ? -108.458 48.290 -24.206 1.00 34.49 ? 20   ALA A O   1 
ATOM   138  C CB  . ALA A 1 20  ? -109.274 49.945 -26.939 1.00 29.94 ? 20   ALA A CB  1 
ATOM   139  N N   . ASP A 1 21  ? -110.575 47.950 -24.905 1.00 34.39 ? 21   ASP A N   1 
ATOM   140  C CA  . ASP A 1 21  ? -111.074 47.639 -23.566 1.00 36.08 ? 21   ASP A CA  1 
ATOM   141  C C   . ASP A 1 21  ? -110.349 46.425 -22.994 1.00 35.87 ? 21   ASP A C   1 
ATOM   142  O O   . ASP A 1 21  ? -109.844 46.467 -21.875 1.00 36.08 ? 21   ASP A O   1 
ATOM   143  C CB  . ASP A 1 21  ? -112.576 47.338 -23.580 1.00 37.24 ? 21   ASP A CB  1 
ATOM   144  C CG  . ASP A 1 21  ? -113.410 48.521 -24.014 1.00 39.59 ? 21   ASP A CG  1 
ATOM   145  O OD1 . ASP A 1 21  ? -112.936 49.668 -23.892 1.00 43.24 ? 21   ASP A OD1 1 
ATOM   146  O OD2 . ASP A 1 21  ? -114.554 48.304 -24.467 1.00 42.39 ? 21   ASP A OD2 1 
ATOM   147  N N   . ARG A 1 22  ? -110.299 45.341 -23.761 1.00 35.23 ? 22   ARG A N   1 
ATOM   148  C CA  . ARG A 1 22  ? -109.632 44.133 -23.290 1.00 36.65 ? 22   ARG A CA  1 
ATOM   149  C C   . ARG A 1 22  ? -108.189 44.414 -22.891 1.00 35.57 ? 22   ARG A C   1 
ATOM   150  O O   . ARG A 1 22  ? -107.602 43.681 -22.098 1.00 35.27 ? 22   ARG A O   1 
ATOM   151  C CB  . ARG A 1 22  ? -109.656 43.036 -24.362 1.00 36.42 ? 22   ARG A CB  1 
ATOM   152  C CG  . ARG A 1 22  ? -111.032 42.455 -24.649 1.00 39.40 ? 22   ARG A CG  1 
ATOM   153  C CD  . ARG A 1 22  ? -110.932 41.269 -25.592 1.00 41.58 ? 22   ARG A CD  1 
ATOM   154  N NE  . ARG A 1 22  ? -112.228 40.645 -25.847 1.00 46.01 ? 22   ARG A NE  1 
ATOM   155  C CZ  . ARG A 1 22  ? -113.002 40.108 -24.906 1.00 50.55 ? 22   ARG A CZ  1 
ATOM   156  N NH1 . ARG A 1 22  ? -112.614 40.115 -23.633 1.00 51.13 ? 22   ARG A NH1 1 
ATOM   157  N NH2 . ARG A 1 22  ? -114.169 39.561 -25.233 1.00 49.86 ? 22   ARG A NH2 1 
ATOM   158  N N   . LEU A 1 23  ? -107.619 45.475 -23.450 1.00 35.47 ? 23   LEU A N   1 
ATOM   159  C CA  . LEU A 1 23  ? -106.237 45.835 -23.152 1.00 34.21 ? 23   LEU A CA  1 
ATOM   160  C C   . LEU A 1 23  ? -106.158 46.936 -22.104 1.00 33.15 ? 23   LEU A C   1 
ATOM   161  O O   . LEU A 1 23  ? -105.065 47.349 -21.721 1.00 34.41 ? 23   LEU A O   1 
ATOM   162  C CB  . LEU A 1 23  ? -105.514 46.274 -24.433 1.00 34.47 ? 23   LEU A CB  1 
ATOM   163  C CG  . LEU A 1 23  ? -105.221 45.161 -25.451 1.00 35.84 ? 23   LEU A CG  1 
ATOM   164  C CD1 . LEU A 1 23  ? -104.679 45.754 -26.735 1.00 35.27 ? 23   LEU A CD1 1 
ATOM   165  C CD2 . LEU A 1 23  ? -104.214 44.185 -24.864 1.00 34.07 ? 23   LEU A CD2 1 
ATOM   166  N N   . GLY A 1 24  ? -107.318 47.403 -21.647 1.00 31.63 ? 24   GLY A N   1 
ATOM   167  C CA  . GLY A 1 24  ? -107.363 48.451 -20.638 1.00 31.62 ? 24   GLY A CA  1 
ATOM   168  C C   . GLY A 1 24  ? -106.884 49.794 -21.154 1.00 32.01 ? 24   GLY A C   1 
ATOM   169  O O   . GLY A 1 24  ? -106.221 50.544 -20.442 1.00 31.69 ? 24   GLY A O   1 
ATOM   170  N N   . LEU A 1 25  ? -107.224 50.104 -22.401 1.00 31.36 ? 25   LEU A N   1 
ATOM   171  C CA  . LEU A 1 25  ? -106.802 51.358 -23.001 1.00 31.12 ? 25   LEU A CA  1 
ATOM   172  C C   . LEU A 1 25  ? -107.951 52.073 -23.694 1.00 30.54 ? 25   LEU A C   1 
ATOM   173  O O   . LEU A 1 25  ? -109.001 51.487 -23.964 1.00 30.47 ? 25   LEU A O   1 
ATOM   174  C CB  . LEU A 1 25  ? -105.724 51.098 -24.054 1.00 33.10 ? 25   LEU A CB  1 
ATOM   175  C CG  . LEU A 1 25  ? -104.458 50.329 -23.703 1.00 32.48 ? 25   LEU A CG  1 
ATOM   176  C CD1 . LEU A 1 25  ? -103.742 49.981 -24.989 1.00 32.42 ? 25   LEU A CD1 1 
ATOM   177  C CD2 . LEU A 1 25  ? -103.564 51.154 -22.790 1.00 32.58 ? 25   LEU A CD2 1 
ATOM   178  N N   . GLU A 1 26  ? -107.738 53.349 -23.978 1.00 29.38 ? 26   GLU A N   1 
ATOM   179  C CA  . GLU A 1 26  ? -108.713 54.123 -24.714 1.00 28.88 ? 26   GLU A CA  1 
ATOM   180  C C   . GLU A 1 26  ? -108.136 54.172 -26.125 1.00 29.29 ? 26   GLU A C   1 
ATOM   181  O O   . GLU A 1 26  ? -106.911 54.074 -26.312 1.00 26.79 ? 26   GLU A O   1 
ATOM   182  C CB  . GLU A 1 26  ? -108.832 55.542 -24.169 1.00 32.81 ? 26   GLU A CB  1 
ATOM   183  C CG  . GLU A 1 26  ? -109.271 55.630 -22.715 1.00 39.48 ? 26   GLU A CG  1 
ATOM   184  C CD  . GLU A 1 26  ? -109.575 57.056 -22.295 1.00 43.01 ? 26   GLU A CD  1 
ATOM   185  O OE1 . GLU A 1 26  ? -108.855 57.980 -22.735 1.00 42.49 ? 26   GLU A OE1 1 
ATOM   186  O OE2 . GLU A 1 26  ? -110.532 57.252 -21.517 1.00 47.43 ? 26   GLU A OE2 1 
ATOM   187  N N   . LEU A 1 27  ? -109.009 54.287 -27.117 1.00 28.88 ? 27   LEU A N   1 
ATOM   188  C CA  . LEU A 1 27  ? -108.558 54.376 -28.496 1.00 27.96 ? 27   LEU A CA  1 
ATOM   189  C C   . LEU A 1 27  ? -107.872 55.727 -28.640 1.00 26.88 ? 27   LEU A C   1 
ATOM   190  O O   . LEU A 1 27  ? -108.334 56.708 -28.089 1.00 25.99 ? 27   LEU A O   1 
ATOM   191  C CB  . LEU A 1 27  ? -109.744 54.274 -29.454 1.00 27.05 ? 27   LEU A CB  1 
ATOM   192  C CG  . LEU A 1 27  ? -110.288 52.856 -29.694 1.00 28.63 ? 27   LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 27  ? -111.573 52.907 -30.508 1.00 27.15 ? 27   LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 27  ? -109.240 52.031 -30.419 1.00 29.45 ? 27   LEU A CD2 1 
ATOM   195  N N   . GLY A 1 28  ? -106.752 55.767 -29.354 1.00 28.12 ? 28   GLY A N   1 
ATOM   196  C CA  . GLY A 1 28  ? -106.053 57.023 -29.548 1.00 29.68 ? 28   GLY A CA  1 
ATOM   197  C C   . GLY A 1 28  ? -106.889 58.048 -30.303 1.00 32.26 ? 28   GLY A C   1 
ATOM   198  O O   . GLY A 1 28  ? -107.752 57.688 -31.107 1.00 31.70 ? 28   GLY A O   1 
ATOM   199  N N   . LYS A 1 29  ? -106.634 59.326 -30.036 1.00 32.38 ? 29   LYS A N   1 
ATOM   200  C CA  . LYS A 1 29  ? -107.349 60.427 -30.678 1.00 37.47 ? 29   LYS A CA  1 
ATOM   201  C C   . LYS A 1 29  ? -106.949 60.638 -32.141 1.00 38.46 ? 29   LYS A C   1 
ATOM   202  O O   . LYS A 1 29  ? -105.794 60.938 -32.437 1.00 38.61 ? 29   LYS A O   1 
ATOM   203  C CB  . LYS A 1 29  ? -107.097 61.733 -29.916 1.00 38.58 ? 29   LYS A CB  1 
ATOM   204  C CG  . LYS A 1 29  ? -107.682 61.775 -28.517 1.00 43.84 ? 29   LYS A CG  1 
ATOM   205  C CD  . LYS A 1 29  ? -107.443 63.128 -27.863 1.00 47.59 ? 29   LYS A CD  1 
ATOM   206  C CE  . LYS A 1 29  ? -106.021 63.270 -27.333 1.00 49.97 ? 29   LYS A CE  1 
ATOM   207  N NZ  . LYS A 1 29  ? -105.799 62.445 -26.105 1.00 52.90 ? 29   LYS A NZ  1 
ATOM   208  N N   . VAL A 1 30  ? -107.906 60.495 -33.049 1.00 40.56 ? 30   VAL A N   1 
ATOM   209  C CA  . VAL A 1 30  ? -107.635 60.699 -34.466 1.00 45.75 ? 30   VAL A CA  1 
ATOM   210  C C   . VAL A 1 30  ? -108.736 61.531 -35.124 1.00 48.36 ? 30   VAL A C   1 
ATOM   211  O O   . VAL A 1 30  ? -109.903 61.148 -35.113 1.00 47.50 ? 30   VAL A O   1 
ATOM   212  C CB  . VAL A 1 30  ? -107.500 59.354 -35.218 1.00 46.67 ? 30   VAL A CB  1 
ATOM   213  C CG1 . VAL A 1 30  ? -108.711 58.474 -34.948 1.00 48.95 ? 30   VAL A CG1 1 
ATOM   214  C CG2 . VAL A 1 30  ? -107.360 59.609 -36.707 1.00 47.58 ? 30   VAL A CG2 1 
ATOM   215  N N   . VAL A 1 31  ? -108.351 62.675 -35.683 1.00 52.32 ? 31   VAL A N   1 
ATOM   216  C CA  . VAL A 1 31  ? -109.291 63.573 -36.352 1.00 57.73 ? 31   VAL A CA  1 
ATOM   217  C C   . VAL A 1 31  ? -109.498 63.108 -37.787 1.00 60.86 ? 31   VAL A C   1 
ATOM   218  O O   . VAL A 1 31  ? -108.538 62.781 -38.485 1.00 62.02 ? 31   VAL A O   1 
ATOM   219  C CB  . VAL A 1 31  ? -108.759 65.024 -36.381 1.00 57.91 ? 31   VAL A CB  1 
ATOM   220  C CG1 . VAL A 1 31  ? -109.807 65.949 -36.972 1.00 58.00 ? 31   VAL A CG1 1 
ATOM   221  C CG2 . VAL A 1 31  ? -108.369 65.470 -34.974 1.00 58.38 ? 31   VAL A CG2 1 
ATOM   222  N N   . THR A 1 32  ? -110.750 63.088 -38.231 1.00 64.81 ? 32   THR A N   1 
ATOM   223  C CA  . THR A 1 32  ? -111.055 62.644 -39.584 1.00 68.38 ? 32   THR A CA  1 
ATOM   224  C C   . THR A 1 32  ? -112.139 63.478 -40.262 1.00 71.05 ? 32   THR A C   1 
ATOM   225  O O   . THR A 1 32  ? -113.270 63.558 -39.780 1.00 72.22 ? 32   THR A O   1 
ATOM   226  C CB  . THR A 1 32  ? -111.498 61.169 -39.581 1.00 67.47 ? 32   THR A CB  1 
ATOM   227  O OG1 . THR A 1 32  ? -110.470 60.367 -38.991 1.00 66.77 ? 32   THR A OG1 1 
ATOM   228  C CG2 . THR A 1 32  ? -111.764 60.684 -41.001 1.00 67.87 ? 32   THR A CG2 1 
ATOM   229  N N   . LYS A 1 33  ? -111.784 64.094 -41.386 1.00 74.07 ? 33   LYS A N   1 
ATOM   230  C CA  . LYS A 1 33  ? -112.722 64.912 -42.154 1.00 76.76 ? 33   LYS A CA  1 
ATOM   231  C C   . LYS A 1 33  ? -112.702 64.475 -43.619 1.00 77.98 ? 33   LYS A C   1 
ATOM   232  O O   . LYS A 1 33  ? -111.656 64.518 -44.270 1.00 77.63 ? 33   LYS A O   1 
ATOM   233  C CB  . LYS A 1 33  ? -112.347 66.395 -42.055 1.00 76.16 ? 33   LYS A CB  1 
ATOM   234  C CG  . LYS A 1 33  ? -112.533 67.004 -40.671 1.00 77.90 ? 33   LYS A CG  1 
ATOM   235  C CD  . LYS A 1 33  ? -112.225 68.496 -40.687 1.00 79.73 ? 33   LYS A CD  1 
ATOM   236  C CE  . LYS A 1 33  ? -112.593 69.162 -39.370 1.00 81.13 ? 33   LYS A CE  1 
ATOM   237  N NZ  . LYS A 1 33  ? -112.458 70.645 -39.449 1.00 83.01 ? 33   LYS A NZ  1 
ATOM   238  N N   . LYS A 1 34  ? -113.854 64.044 -44.131 1.00 79.04 ? 34   LYS A N   1 
ATOM   239  C CA  . LYS A 1 34  ? -113.952 63.602 -45.521 1.00 79.33 ? 34   LYS A CA  1 
ATOM   240  C C   . LYS A 1 34  ? -114.195 64.757 -46.472 1.00 79.33 ? 34   LYS A C   1 
ATOM   241  O O   . LYS A 1 34  ? -115.209 65.449 -46.390 1.00 80.25 ? 34   LYS A O   1 
ATOM   242  C CB  . LYS A 1 34  ? -115.066 62.571 -45.686 1.00 79.95 ? 34   LYS A CB  1 
ATOM   243  C CG  . LYS A 1 34  ? -114.732 61.221 -45.093 1.00 80.87 ? 34   LYS A CG  1 
ATOM   244  C CD  . LYS A 1 34  ? -113.474 60.649 -45.721 1.00 82.01 ? 34   LYS A CD  1 
ATOM   245  C CE  . LYS A 1 34  ? -112.376 60.468 -44.687 1.00 83.01 ? 34   LYS A CE  1 
ATOM   246  N NZ  . LYS A 1 34  ? -111.962 61.755 -44.070 1.00 83.05 ? 34   LYS A NZ  1 
ATOM   247  N N   . PHE A 1 35  ? -113.251 64.950 -47.381 1.00 79.31 ? 35   PHE A N   1 
ATOM   248  C CA  . PHE A 1 35  ? -113.330 66.019 -48.357 1.00 79.80 ? 35   PHE A CA  1 
ATOM   249  C C   . PHE A 1 35  ? -114.372 65.795 -49.441 1.00 79.84 ? 35   PHE A C   1 
ATOM   250  O O   . PHE A 1 35  ? -115.255 64.942 -49.323 1.00 78.47 ? 35   PHE A O   1 
ATOM   251  C CB  . PHE A 1 35  ? -111.959 66.228 -48.998 1.00 81.96 ? 35   PHE A CB  1 
ATOM   252  C CG  . PHE A 1 35  ? -111.113 67.252 -48.299 1.00 84.16 ? 35   PHE A CG  1 
ATOM   253  C CD1 . PHE A 1 35  ? -111.116 67.349 -46.910 1.00 84.58 ? 35   PHE A CD1 1 
ATOM   254  C CD2 . PHE A 1 35  ? -110.310 68.123 -49.031 1.00 84.97 ? 35   PHE A CD2 1 
ATOM   255  C CE1 . PHE A 1 35  ? -110.333 68.300 -46.262 1.00 85.80 ? 35   PHE A CE1 1 
ATOM   256  C CE2 . PHE A 1 35  ? -109.522 69.076 -48.394 1.00 85.47 ? 35   PHE A CE2 1 
ATOM   257  C CZ  . PHE A 1 35  ? -109.534 69.166 -47.006 1.00 86.38 ? 35   PHE A CZ  1 
ATOM   258  N N   . SER A 1 36  ? -114.237 66.588 -50.498 1.00 79.01 ? 36   SER A N   1 
ATOM   259  C CA  . SER A 1 36  ? -115.120 66.575 -51.656 1.00 76.23 ? 36   SER A CA  1 
ATOM   260  C C   . SER A 1 36  ? -115.641 65.216 -52.089 1.00 74.28 ? 36   SER A C   1 
ATOM   261  O O   . SER A 1 36  ? -116.759 64.831 -51.748 1.00 75.38 ? 36   SER A O   1 
ATOM   262  C CB  . SER A 1 36  ? -114.411 67.230 -52.846 1.00 76.77 ? 36   SER A CB  1 
ATOM   263  O OG  . SER A 1 36  ? -113.221 66.538 -53.184 1.00 76.36 ? 36   SER A OG  1 
ATOM   264  N N   . ASN A 1 37  ? -114.815 64.502 -52.845 1.00 71.53 ? 37   ASN A N   1 
ATOM   265  C CA  . ASN A 1 37  ? -115.175 63.199 -53.392 1.00 68.90 ? 37   ASN A CA  1 
ATOM   266  C C   . ASN A 1 37  ? -114.682 62.007 -52.592 1.00 65.95 ? 37   ASN A C   1 
ATOM   267  O O   . ASN A 1 37  ? -114.145 61.054 -53.152 1.00 64.34 ? 37   ASN A O   1 
ATOM   268  C CB  . ASN A 1 37  ? -114.654 63.104 -54.823 1.00 71.04 ? 37   ASN A CB  1 
ATOM   269  C CG  . ASN A 1 37  ? -113.194 63.508 -54.936 1.00 72.37 ? 37   ASN A CG  1 
ATOM   270  O OD1 . ASN A 1 37  ? -112.643 63.597 -56.036 1.00 74.27 ? 37   ASN A OD1 1 
ATOM   271  N ND2 . ASN A 1 37  ? -112.559 63.757 -53.793 1.00 72.95 ? 37   ASN A ND2 1 
ATOM   272  N N   . GLN A 1 38  ? -114.878 62.062 -51.283 1.00 63.19 ? 38   GLN A N   1 
ATOM   273  C CA  . GLN A 1 38  ? -114.468 60.986 -50.392 1.00 60.11 ? 38   GLN A CA  1 
ATOM   274  C C   . GLN A 1 38  ? -112.962 61.005 -50.169 1.00 57.15 ? 38   GLN A C   1 
ATOM   275  O O   . GLN A 1 38  ? -112.400 60.067 -49.598 1.00 58.95 ? 38   GLN A O   1 
ATOM   276  C CB  . GLN A 1 38  ? -114.911 59.630 -50.958 1.00 60.78 ? 38   GLN A CB  1 
ATOM   277  C CG  . GLN A 1 38  ? -114.879 58.474 -49.969 1.00 60.43 ? 38   GLN A CG  1 
ATOM   278  C CD  . GLN A 1 38  ? -115.707 58.738 -48.726 1.00 61.61 ? 38   GLN A CD  1 
ATOM   279  O OE1 . GLN A 1 38  ? -115.302 59.496 -47.842 1.00 61.26 ? 38   GLN A OE1 1 
ATOM   280  N NE2 . GLN A 1 38  ? -116.880 58.119 -48.656 1.00 62.41 ? 38   GLN A NE2 1 
ATOM   281  N N   . GLU A 1 39  ? -112.303 62.069 -50.622 1.00 52.24 ? 39   GLU A N   1 
ATOM   282  C CA  . GLU A 1 39  ? -110.866 62.183 -50.413 1.00 48.73 ? 39   GLU A CA  1 
ATOM   283  C C   . GLU A 1 39  ? -110.663 62.150 -48.899 1.00 47.43 ? 39   GLU A C   1 
ATOM   284  O O   . GLU A 1 39  ? -111.202 62.984 -48.168 1.00 45.29 ? 39   GLU A O   1 
ATOM   285  C CB  . GLU A 1 39  ? -110.330 63.487 -51.005 1.00 46.83 ? 39   GLU A CB  1 
ATOM   286  C CG  . GLU A 1 39  ? -108.869 63.749 -50.696 1.00 45.51 ? 39   GLU A CG  1 
ATOM   287  C CD  . GLU A 1 39  ? -108.292 64.877 -51.519 1.00 45.23 ? 39   GLU A CD  1 
ATOM   288  O OE1 . GLU A 1 39  ? -107.235 65.423 -51.137 1.00 43.49 ? 39   GLU A OE1 1 
ATOM   289  O OE2 . GLU A 1 39  ? -108.894 65.212 -52.558 1.00 46.98 ? 39   GLU A OE2 1 
ATOM   290  N N   . THR A 1 40  ? -109.889 61.171 -48.445 1.00 46.18 ? 40   THR A N   1 
ATOM   291  C CA  . THR A 1 40  ? -109.633 60.955 -47.028 1.00 46.06 ? 40   THR A CA  1 
ATOM   292  C C   . THR A 1 40  ? -108.632 61.887 -46.353 1.00 45.82 ? 40   THR A C   1 
ATOM   293  O O   . THR A 1 40  ? -107.498 62.053 -46.809 1.00 44.22 ? 40   THR A O   1 
ATOM   294  C CB  . THR A 1 40  ? -109.149 59.504 -46.781 1.00 48.79 ? 40   THR A CB  1 
ATOM   295  O OG1 . THR A 1 40  ? -110.028 58.580 -47.440 1.00 49.99 ? 40   THR A OG1 1 
ATOM   296  C CG2 . THR A 1 40  ? -109.115 59.203 -45.284 1.00 48.32 ? 40   THR A CG2 1 
ATOM   297  N N   . CYS A 1 41  ? -109.067 62.487 -45.252 1.00 45.77 ? 41   CYS A N   1 
ATOM   298  C CA  . CYS A 1 41  ? -108.214 63.366 -44.460 1.00 48.25 ? 41   CYS A CA  1 
ATOM   299  C C   . CYS A 1 41  ? -108.110 62.748 -43.073 1.00 46.09 ? 41   CYS A C   1 
ATOM   300  O O   . CYS A 1 41  ? -109.119 62.394 -42.466 1.00 46.87 ? 41   CYS A O   1 
ATOM   301  C CB  . CYS A 1 41  ? -108.802 64.780 -44.365 1.00 52.03 ? 41   CYS A CB  1 
ATOM   302  S SG  . CYS A 1 41  ? -108.377 65.882 -45.757 1.00 61.88 ? 41   CYS A SG  1 
ATOM   303  N N   . VAL A 1 42  ? -106.887 62.596 -42.586 1.00 45.67 ? 42   VAL A N   1 
ATOM   304  C CA  . VAL A 1 42  ? -106.662 62.012 -41.273 1.00 45.17 ? 42   VAL A CA  1 
ATOM   305  C C   . VAL A 1 42  ? -105.637 62.841 -40.529 1.00 45.02 ? 42   VAL A C   1 
ATOM   306  O O   . VAL A 1 42  ? -104.709 63.377 -41.129 1.00 45.78 ? 42   VAL A O   1 
ATOM   307  C CB  . VAL A 1 42  ? -106.143 60.568 -41.384 1.00 44.80 ? 42   VAL A CB  1 
ATOM   308  C CG1 . VAL A 1 42  ? -106.024 59.952 -40.009 1.00 45.30 ? 42   VAL A CG1 1 
ATOM   309  C CG2 . VAL A 1 42  ? -107.076 59.745 -42.246 1.00 45.38 ? 42   VAL A CG2 1 
ATOM   310  N N   . GLU A 1 43  ? -105.810 62.957 -39.220 1.00 45.38 ? 43   GLU A N   1 
ATOM   311  C CA  . GLU A 1 43  ? -104.879 63.727 -38.418 1.00 44.85 ? 43   GLU A CA  1 
ATOM   312  C C   . GLU A 1 43  ? -104.753 63.111 -37.031 1.00 43.58 ? 43   GLU A C   1 
ATOM   313  O O   . GLU A 1 43  ? -105.706 63.097 -36.264 1.00 43.18 ? 43   GLU A O   1 
ATOM   314  C CB  . GLU A 1 43  ? -105.357 65.175 -38.327 1.00 47.36 ? 43   GLU A CB  1 
ATOM   315  C CG  . GLU A 1 43  ? -104.237 66.194 -38.320 1.00 52.06 ? 43   GLU A CG  1 
ATOM   316  C CD  . GLU A 1 43  ? -104.700 67.576 -38.746 1.00 56.81 ? 43   GLU A CD  1 
ATOM   317  O OE1 . GLU A 1 43  ? -105.459 68.217 -37.980 1.00 59.37 ? 43   GLU A OE1 1 
ATOM   318  O OE2 . GLU A 1 43  ? -104.309 68.018 -39.851 1.00 55.79 ? 43   GLU A OE2 1 
ATOM   319  N N   . ILE A 1 44  ? -103.571 62.590 -36.720 1.00 41.74 ? 44   ILE A N   1 
ATOM   320  C CA  . ILE A 1 44  ? -103.318 61.966 -35.423 1.00 40.11 ? 44   ILE A CA  1 
ATOM   321  C C   . ILE A 1 44  ? -103.478 63.017 -34.326 1.00 39.84 ? 44   ILE A C   1 
ATOM   322  O O   . ILE A 1 44  ? -102.699 63.963 -34.238 1.00 39.56 ? 44   ILE A O   1 
ATOM   323  C CB  . ILE A 1 44  ? -101.895 61.371 -35.380 1.00 41.03 ? 44   ILE A CB  1 
ATOM   324  C CG1 . ILE A 1 44  ? -101.662 60.487 -36.612 1.00 40.65 ? 44   ILE A CG1 1 
ATOM   325  C CG2 . ILE A 1 44  ? -101.706 60.552 -34.113 1.00 39.68 ? 44   ILE A CG2 1 
ATOM   326  C CD1 . ILE A 1 44  ? -102.688 59.374 -36.784 1.00 39.43 ? 44   ILE A CD1 1 
ATOM   327  N N   . GLY A 1 45  ? -104.505 62.847 -33.501 1.00 37.59 ? 45   GLY A N   1 
ATOM   328  C CA  . GLY A 1 45  ? -104.772 63.796 -32.442 1.00 36.25 ? 45   GLY A CA  1 
ATOM   329  C C   . GLY A 1 45  ? -103.840 63.779 -31.249 1.00 35.47 ? 45   GLY A C   1 
ATOM   330  O O   . GLY A 1 45  ? -104.065 64.510 -30.291 1.00 36.19 ? 45   GLY A O   1 
ATOM   331  N N   . GLU A 1 46  ? -102.814 62.938 -31.280 1.00 35.14 ? 46   GLU A N   1 
ATOM   332  C CA  . GLU A 1 46  ? -101.856 62.889 -30.183 1.00 34.05 ? 46   GLU A CA  1 
ATOM   333  C C   . GLU A 1 46  ? -100.500 62.414 -30.674 1.00 32.71 ? 46   GLU A C   1 
ATOM   334  O O   . GLU A 1 46  ? -100.374 61.894 -31.783 1.00 31.39 ? 46   GLU A O   1 
ATOM   335  C CB  . GLU A 1 46  ? -102.357 61.972 -29.075 1.00 35.10 ? 46   GLU A CB  1 
ATOM   336  C CG  . GLU A 1 46  ? -102.803 60.609 -29.560 1.00 37.28 ? 46   GLU A CG  1 
ATOM   337  C CD  . GLU A 1 46  ? -103.342 59.760 -28.436 1.00 38.21 ? 46   GLU A CD  1 
ATOM   338  O OE1 . GLU A 1 46  ? -102.529 59.280 -27.626 1.00 40.40 ? 46   GLU A OE1 1 
ATOM   339  O OE2 . GLU A 1 46  ? -104.575 59.588 -28.357 1.00 38.54 ? 46   GLU A OE2 1 
ATOM   340  N N   . SER A 1 47  ? -99.486  62.599 -29.840 1.00 30.72 ? 47   SER A N   1 
ATOM   341  C CA  . SER A 1 47  ? -98.127  62.205 -30.189 1.00 30.70 ? 47   SER A CA  1 
ATOM   342  C C   . SER A 1 47  ? -97.953  60.696 -30.152 1.00 29.54 ? 47   SER A C   1 
ATOM   343  O O   . SER A 1 47  ? -98.464  60.038 -29.258 1.00 28.96 ? 47   SER A O   1 
ATOM   344  C CB  . SER A 1 47  ? -97.125  62.836 -29.226 1.00 29.53 ? 47   SER A CB  1 
ATOM   345  O OG  . SER A 1 47  ? -95.815  62.360 -29.483 1.00 32.86 ? 47   SER A OG  1 
ATOM   346  N N   . VAL A 1 48  ? -97.242  60.151 -31.131 1.00 27.08 ? 48   VAL A N   1 
ATOM   347  C CA  . VAL A 1 48  ? -96.998  58.713 -31.177 1.00 26.67 ? 48   VAL A CA  1 
ATOM   348  C C   . VAL A 1 48  ? -95.491  58.470 -31.275 1.00 26.21 ? 48   VAL A C   1 
ATOM   349  O O   . VAL A 1 48  ? -95.046  57.354 -31.541 1.00 25.83 ? 48   VAL A O   1 
ATOM   350  C CB  . VAL A 1 48  ? -97.698  58.058 -32.399 1.00 27.08 ? 48   VAL A CB  1 
ATOM   351  C CG1 . VAL A 1 48  ? -99.210  58.177 -32.266 1.00 25.16 ? 48   VAL A CG1 1 
ATOM   352  C CG2 . VAL A 1 48  ? -97.215  58.711 -33.693 1.00 25.79 ? 48   VAL A CG2 1 
ATOM   353  N N   . ARG A 1 49  ? -94.718  59.530 -31.045 1.00 27.38 ? 49   ARG A N   1 
ATOM   354  C CA  . ARG A 1 49  ? -93.262  59.480 -31.120 1.00 28.70 ? 49   ARG A CA  1 
ATOM   355  C C   . ARG A 1 49  ? -92.681  58.406 -30.211 1.00 31.03 ? 49   ARG A C   1 
ATOM   356  O O   . ARG A 1 49  ? -92.938  58.388 -29.008 1.00 28.22 ? 49   ARG A O   1 
ATOM   357  C CB  . ARG A 1 49  ? -92.675  60.853 -30.749 1.00 29.05 ? 49   ARG A CB  1 
ATOM   358  C CG  . ARG A 1 49  ? -91.177  60.983 -31.002 1.00 28.93 ? 49   ARG A CG  1 
ATOM   359  C CD  . ARG A 1 49  ? -90.680  62.405 -30.755 1.00 27.83 ? 49   ARG A CD  1 
ATOM   360  N NE  . ARG A 1 49  ? -91.319  63.384 -31.635 1.00 26.63 ? 49   ARG A NE  1 
ATOM   361  C CZ  . ARG A 1 49  ? -90.867  63.728 -32.837 1.00 26.33 ? 49   ARG A CZ  1 
ATOM   362  N NH1 . ARG A 1 49  ? -89.763  63.183 -33.329 1.00 25.78 ? 49   ARG A NH1 1 
ATOM   363  N NH2 . ARG A 1 49  ? -91.523  64.623 -33.554 1.00 26.21 ? 49   ARG A NH2 1 
ATOM   364  N N   . GLY A 1 50  ? -91.894  57.509 -30.792 1.00 32.00 ? 50   GLY A N   1 
ATOM   365  C CA  . GLY A 1 50  ? -91.299  56.442 -30.010 1.00 32.44 ? 50   GLY A CA  1 
ATOM   366  C C   . GLY A 1 50  ? -92.295  55.424 -29.478 1.00 35.31 ? 50   GLY A C   1 
ATOM   367  O O   . GLY A 1 50  ? -91.971  54.687 -28.544 1.00 35.54 ? 50   GLY A O   1 
ATOM   368  N N   . GLU A 1 51  ? -93.495  55.351 -30.045 1.00 34.79 ? 51   GLU A N   1 
ATOM   369  C CA  . GLU A 1 51  ? -94.477  54.392 -29.532 1.00 35.88 ? 51   GLU A CA  1 
ATOM   370  C C   . GLU A 1 51  ? -94.743  53.178 -30.409 1.00 34.45 ? 51   GLU A C   1 
ATOM   371  O O   . GLU A 1 51  ? -94.545  53.224 -31.616 1.00 34.51 ? 51   GLU A O   1 
ATOM   372  C CB  . GLU A 1 51  ? -95.796  55.112 -29.298 1.00 38.55 ? 51   GLU A CB  1 
ATOM   373  C CG  . GLU A 1 51  ? -95.583  56.477 -28.719 1.00 44.30 ? 51   GLU A CG  1 
ATOM   374  C CD  . GLU A 1 51  ? -96.482  56.745 -27.559 1.00 48.69 ? 51   GLU A CD  1 
ATOM   375  O OE1 . GLU A 1 51  ? -97.717  56.775 -27.773 1.00 51.59 ? 51   GLU A OE1 1 
ATOM   376  O OE2 . GLU A 1 51  ? -95.949  56.916 -26.438 1.00 51.18 ? 51   GLU A OE2 1 
ATOM   377  N N   . ASP A 1 52  ? -95.202  52.092 -29.787 1.00 32.33 ? 52   ASP A N   1 
ATOM   378  C CA  . ASP A 1 52  ? -95.549  50.851 -30.497 1.00 31.84 ? 52   ASP A CA  1 
ATOM   379  C C   . ASP A 1 52  ? -97.013  51.056 -30.899 1.00 30.80 ? 52   ASP A C   1 
ATOM   380  O O   . ASP A 1 52  ? -97.915  50.934 -30.082 1.00 29.33 ? 52   ASP A O   1 
ATOM   381  C CB  . ASP A 1 52  ? -95.377  49.641 -29.561 1.00 32.10 ? 52   ASP A CB  1 
ATOM   382  C CG  . ASP A 1 52  ? -95.530  48.292 -30.278 1.00 35.77 ? 52   ASP A CG  1 
ATOM   383  O OD1 . ASP A 1 52  ? -95.291  48.206 -31.507 1.00 35.88 ? 52   ASP A OD1 1 
ATOM   384  O OD2 . ASP A 1 52  ? -95.866  47.298 -29.597 1.00 35.30 ? 52   ASP A OD2 1 
ATOM   385  N N   . VAL A 1 53  ? -97.239  51.393 -32.162 1.00 30.30 ? 53   VAL A N   1 
ATOM   386  C CA  . VAL A 1 53  ? -98.586  51.690 -32.638 1.00 28.73 ? 53   VAL A CA  1 
ATOM   387  C C   . VAL A 1 53  ? -99.319  50.566 -33.360 1.00 28.97 ? 53   VAL A C   1 
ATOM   388  O O   . VAL A 1 53  ? -98.732  49.870 -34.185 1.00 31.60 ? 53   VAL A O   1 
ATOM   389  C CB  . VAL A 1 53  ? -98.536  52.905 -33.587 1.00 28.70 ? 53   VAL A CB  1 
ATOM   390  C CG1 . VAL A 1 53  ? -99.935  53.263 -34.079 1.00 28.51 ? 53   VAL A CG1 1 
ATOM   391  C CG2 . VAL A 1 53  ? -97.898  54.086 -32.869 1.00 28.52 ? 53   VAL A CG2 1 
ATOM   392  N N   . TYR A 1 54  ? -100.611 50.431 -33.069 1.00 27.42 ? 54   TYR A N   1 
ATOM   393  C CA  . TYR A 1 54  ? -101.471 49.428 -33.695 1.00 26.90 ? 54   TYR A CA  1 
ATOM   394  C C   . TYR A 1 54  ? -102.719 50.111 -34.268 1.00 27.16 ? 54   TYR A C   1 
ATOM   395  O O   . TYR A 1 54  ? -103.490 50.725 -33.530 1.00 29.26 ? 54   TYR A O   1 
ATOM   396  C CB  . TYR A 1 54  ? -101.907 48.369 -32.667 1.00 27.53 ? 54   TYR A CB  1 
ATOM   397  C CG  . TYR A 1 54  ? -100.755 47.581 -32.101 1.00 27.73 ? 54   TYR A CG  1 
ATOM   398  C CD1 . TYR A 1 54  ? -99.874  48.169 -31.188 1.00 26.71 ? 54   TYR A CD1 1 
ATOM   399  C CD2 . TYR A 1 54  ? -100.487 46.279 -32.538 1.00 25.72 ? 54   TYR A CD2 1 
ATOM   400  C CE1 . TYR A 1 54  ? -98.762  47.497 -30.731 1.00 27.91 ? 54   TYR A CE1 1 
ATOM   401  C CE2 . TYR A 1 54  ? -99.360  45.592 -32.081 1.00 28.47 ? 54   TYR A CE2 1 
ATOM   402  C CZ  . TYR A 1 54  ? -98.503  46.213 -31.176 1.00 27.87 ? 54   TYR A CZ  1 
ATOM   403  O OH  . TYR A 1 54  ? -97.385  45.563 -30.702 1.00 29.18 ? 54   TYR A OH  1 
ATOM   404  N N   . ILE A 1 55  ? -102.911 50.005 -35.578 1.00 27.68 ? 55   ILE A N   1 
ATOM   405  C CA  . ILE A 1 55  ? -104.072 50.591 -36.250 1.00 27.61 ? 55   ILE A CA  1 
ATOM   406  C C   . ILE A 1 55  ? -105.007 49.456 -36.654 1.00 28.77 ? 55   ILE A C   1 
ATOM   407  O O   . ILE A 1 55  ? -104.605 48.560 -37.385 1.00 29.78 ? 55   ILE A O   1 
ATOM   408  C CB  . ILE A 1 55  ? -103.650 51.367 -37.519 1.00 24.98 ? 55   ILE A CB  1 
ATOM   409  C CG1 . ILE A 1 55  ? -102.638 52.444 -37.149 1.00 25.90 ? 55   ILE A CG1 1 
ATOM   410  C CG2 . ILE A 1 55  ? -104.872 52.033 -38.174 1.00 25.09 ? 55   ILE A CG2 1 
ATOM   411  C CD1 . ILE A 1 55  ? -102.018 53.101 -38.330 1.00 28.49 ? 55   ILE A CD1 1 
ATOM   412  N N   . VAL A 1 56  ? -106.246 49.483 -36.168 1.00 31.45 ? 56   VAL A N   1 
ATOM   413  C CA  . VAL A 1 56  ? -107.208 48.435 -36.499 1.00 33.18 ? 56   VAL A CA  1 
ATOM   414  C C   . VAL A 1 56  ? -108.079 48.901 -37.656 1.00 37.33 ? 56   VAL A C   1 
ATOM   415  O O   . VAL A 1 56  ? -108.689 49.965 -37.582 1.00 36.08 ? 56   VAL A O   1 
ATOM   416  C CB  . VAL A 1 56  ? -108.106 48.101 -35.298 1.00 33.10 ? 56   VAL A CB  1 
ATOM   417  C CG1 . VAL A 1 56  ? -108.963 46.874 -35.609 1.00 30.99 ? 56   VAL A CG1 1 
ATOM   418  C CG2 . VAL A 1 56  ? -107.257 47.856 -34.073 1.00 34.36 ? 56   VAL A CG2 1 
ATOM   419  N N   . GLN A 1 57  ? -108.117 48.102 -38.721 1.00 43.10 ? 57   GLN A N   1 
ATOM   420  C CA  . GLN A 1 57  ? -108.887 48.403 -39.927 1.00 49.57 ? 57   GLN A CA  1 
ATOM   421  C C   . GLN A 1 57  ? -110.356 48.661 -39.644 1.00 52.56 ? 57   GLN A C   1 
ATOM   422  O O   . GLN A 1 57  ? -110.964 47.984 -38.814 1.00 53.07 ? 57   GLN A O   1 
ATOM   423  C CB  . GLN A 1 57  ? -108.741 47.254 -40.944 1.00 51.64 ? 57   GLN A CB  1 
ATOM   424  C CG  . GLN A 1 57  ? -110.044 46.719 -41.568 1.00 57.19 ? 57   GLN A CG  1 
ATOM   425  C CD  . GLN A 1 57  ? -110.901 45.905 -40.592 1.00 59.49 ? 57   GLN A CD  1 
ATOM   426  O OE1 . GLN A 1 57  ? -111.976 45.403 -40.946 1.00 60.51 ? 57   GLN A OE1 1 
ATOM   427  N NE2 . GLN A 1 57  ? -110.428 45.773 -39.360 1.00 61.17 ? 57   GLN A NE2 1 
ATOM   428  N N   . SER A 1 58  ? -110.919 49.647 -40.338 1.00 55.99 ? 58   SER A N   1 
ATOM   429  C CA  . SER A 1 58  ? -112.324 49.997 -40.176 1.00 58.98 ? 58   SER A CA  1 
ATOM   430  C C   . SER A 1 58  ? -113.205 48.939 -40.832 1.00 60.42 ? 58   SER A C   1 
ATOM   431  O O   . SER A 1 58  ? -112.715 48.058 -41.538 1.00 61.06 ? 58   SER A O   1 
ATOM   432  C CB  . SER A 1 58  ? -112.606 51.363 -40.811 1.00 58.92 ? 58   SER A CB  1 
ATOM   433  O OG  . SER A 1 58  ? -113.905 51.814 -40.465 1.00 57.78 ? 58   SER A OG  1 
ATOM   434  N N   . GLY A 1 59  ? -114.508 49.026 -40.598 1.00 62.47 ? 59   GLY A N   1 
ATOM   435  C CA  . GLY A 1 59  ? -115.417 48.059 -41.191 1.00 65.01 ? 59   GLY A CA  1 
ATOM   436  C C   . GLY A 1 59  ? -116.557 48.754 -41.905 1.00 65.58 ? 59   GLY A C   1 
ATOM   437  O O   . GLY A 1 59  ? -117.711 48.334 -41.812 1.00 65.94 ? 59   GLY A O   1 
ATOM   438  N N   . CYS A 1 60  ? -116.227 49.827 -42.618 1.00 65.87 ? 60   CYS A N   1 
ATOM   439  C CA  . CYS A 1 60  ? -117.223 50.599 -43.343 1.00 65.46 ? 60   CYS A CA  1 
ATOM   440  C C   . CYS A 1 60  ? -117.443 50.168 -44.786 1.00 62.81 ? 60   CYS A C   1 
ATOM   441  O O   . CYS A 1 60  ? -117.449 51.000 -45.696 1.00 64.23 ? 60   CYS A O   1 
ATOM   442  C CB  . CYS A 1 60  ? -116.871 52.086 -43.302 1.00 67.27 ? 60   CYS A CB  1 
ATOM   443  S SG  . CYS A 1 60  ? -117.612 52.961 -41.895 1.00 73.51 ? 60   CYS A SG  1 
ATOM   444  N N   . GLY A 1 61  ? -117.623 48.864 -44.976 1.00 58.65 ? 61   GLY A N   1 
ATOM   445  C CA  . GLY A 1 61  ? -117.889 48.302 -46.288 1.00 53.03 ? 61   GLY A CA  1 
ATOM   446  C C   . GLY A 1 61  ? -117.071 48.728 -47.487 1.00 49.11 ? 61   GLY A C   1 
ATOM   447  O O   . GLY A 1 61  ? -116.456 47.877 -48.123 1.00 51.31 ? 61   GLY A O   1 
ATOM   448  N N   . GLU A 1 62  ? -117.080 50.018 -47.816 1.00 43.28 ? 62   GLU A N   1 
ATOM   449  C CA  . GLU A 1 62  ? -116.336 50.536 -48.965 1.00 38.10 ? 62   GLU A CA  1 
ATOM   450  C C   . GLU A 1 62  ? -114.862 50.161 -48.815 1.00 34.08 ? 62   GLU A C   1 
ATOM   451  O O   . GLU A 1 62  ? -114.093 50.851 -48.148 1.00 31.64 ? 62   GLU A O   1 
ATOM   452  C CB  . GLU A 1 62  ? -116.502 52.054 -49.045 1.00 36.65 ? 62   GLU A CB  1 
ATOM   453  C CG  . GLU A 1 62  ? -116.789 52.593 -50.444 1.00 35.69 ? 62   GLU A CG  1 
ATOM   454  C CD  . GLU A 1 62  ? -115.635 52.376 -51.430 1.00 35.19 ? 62   GLU A CD  1 
ATOM   455  O OE1 . GLU A 1 62  ? -114.559 51.904 -51.009 1.00 31.23 ? 62   GLU A OE1 1 
ATOM   456  O OE2 . GLU A 1 62  ? -115.808 52.684 -52.628 1.00 32.62 ? 62   GLU A OE2 1 
ATOM   457  N N   . ILE A 1 63  ? -114.486 49.061 -49.455 1.00 29.76 ? 63   ILE A N   1 
ATOM   458  C CA  . ILE A 1 63  ? -113.135 48.531 -49.370 1.00 31.31 ? 63   ILE A CA  1 
ATOM   459  C C   . ILE A 1 63  ? -111.991 49.477 -49.754 1.00 29.98 ? 63   ILE A C   1 
ATOM   460  O O   . ILE A 1 63  ? -110.935 49.457 -49.111 1.00 29.94 ? 63   ILE A O   1 
ATOM   461  C CB  . ILE A 1 63  ? -113.024 47.221 -50.185 1.00 31.25 ? 63   ILE A CB  1 
ATOM   462  C CG1 . ILE A 1 63  ? -111.736 46.490 -49.812 1.00 32.96 ? 63   ILE A CG1 1 
ATOM   463  C CG2 . ILE A 1 63  ? -113.067 47.517 -51.678 1.00 33.48 ? 63   ILE A CG2 1 
ATOM   464  C CD1 . ILE A 1 63  ? -111.552 45.162 -50.535 1.00 33.61 ? 63   ILE A CD1 1 
ATOM   465  N N   . ASN A 1 64  ? -112.192 50.304 -50.777 1.00 26.75 ? 64   ASN A N   1 
ATOM   466  C CA  . ASN A 1 64  ? -111.147 51.229 -51.200 1.00 27.30 ? 64   ASN A CA  1 
ATOM   467  C C   . ASN A 1 64  ? -110.987 52.448 -50.271 1.00 28.89 ? 64   ASN A C   1 
ATOM   468  O O   . ASN A 1 64  ? -109.891 52.980 -50.125 1.00 28.63 ? 64   ASN A O   1 
ATOM   469  C CB  . ASN A 1 64  ? -111.392 51.670 -52.642 1.00 26.45 ? 64   ASN A CB  1 
ATOM   470  C CG  . ASN A 1 64  ? -111.497 50.487 -53.594 1.00 27.20 ? 64   ASN A CG  1 
ATOM   471  O OD1 . ASN A 1 64  ? -110.711 49.535 -53.513 1.00 23.86 ? 64   ASN A OD1 1 
ATOM   472  N ND2 . ASN A 1 64  ? -112.464 50.540 -54.500 1.00 24.42 ? 64   ASN A ND2 1 
ATOM   473  N N   . ASP A 1 65  ? -112.074 52.896 -49.651 1.00 28.59 ? 65   ASP A N   1 
ATOM   474  C CA  . ASP A 1 65  ? -111.981 54.017 -48.722 1.00 27.43 ? 65   ASP A CA  1 
ATOM   475  C C   . ASP A 1 65  ? -111.290 53.483 -47.461 1.00 26.21 ? 65   ASP A C   1 
ATOM   476  O O   . ASP A 1 65  ? -110.458 54.151 -46.857 1.00 24.90 ? 65   ASP A O   1 
ATOM   477  C CB  . ASP A 1 65  ? -113.374 54.540 -48.360 1.00 28.73 ? 65   ASP A CB  1 
ATOM   478  C CG  . ASP A 1 65  ? -114.090 55.190 -49.537 1.00 30.84 ? 65   ASP A CG  1 
ATOM   479  O OD1 . ASP A 1 65  ? -113.413 55.727 -50.447 1.00 27.67 ? 65   ASP A OD1 1 
ATOM   480  O OD2 . ASP A 1 65  ? -115.338 55.180 -49.533 1.00 31.13 ? 65   ASP A OD2 1 
ATOM   481  N N   . ASN A 1 66  ? -111.638 52.261 -47.078 1.00 25.84 ? 66   ASN A N   1 
ATOM   482  C CA  . ASN A 1 66  ? -111.048 51.640 -45.901 1.00 27.50 ? 66   ASN A CA  1 
ATOM   483  C C   . ASN A 1 66  ? -109.551 51.447 -46.088 1.00 25.44 ? 66   ASN A C   1 
ATOM   484  O O   . ASN A 1 66  ? -108.762 51.847 -45.231 1.00 25.09 ? 66   ASN A O   1 
ATOM   485  C CB  . ASN A 1 66  ? -111.738 50.310 -45.611 1.00 28.56 ? 66   ASN A CB  1 
ATOM   486  C CG  . ASN A 1 66  ? -112.971 50.476 -44.727 1.00 35.10 ? 66   ASN A CG  1 
ATOM   487  O OD1 . ASN A 1 66  ? -113.750 51.423 -44.883 1.00 36.09 ? 66   ASN A OD1 1 
ATOM   488  N ND2 . ASN A 1 66  ? -113.155 49.548 -43.794 1.00 38.44 ? 66   ASN A ND2 1 
ATOM   489  N N   . LEU A 1 67  ? -109.156 50.862 -47.213 1.00 22.57 ? 67   LEU A N   1 
ATOM   490  C CA  . LEU A 1 67  ? -107.738 50.659 -47.479 1.00 23.43 ? 67   LEU A CA  1 
ATOM   491  C C   . LEU A 1 67  ? -106.966 51.979 -47.438 1.00 22.08 ? 67   LEU A C   1 
ATOM   492  O O   . LEU A 1 67  ? -105.976 52.088 -46.730 1.00 22.76 ? 67   LEU A O   1 
ATOM   493  C CB  . LEU A 1 67  ? -107.538 49.976 -48.825 1.00 21.64 ? 67   LEU A CB  1 
ATOM   494  C CG  . LEU A 1 67  ? -106.095 49.684 -49.228 1.00 22.61 ? 67   LEU A CG  1 
ATOM   495  C CD1 . LEU A 1 67  ? -105.397 48.869 -48.142 1.00 22.19 ? 67   LEU A CD1 1 
ATOM   496  C CD2 . LEU A 1 67  ? -106.093 48.935 -50.548 1.00 21.74 ? 67   LEU A CD2 1 
ATOM   497  N N   . MET A 1 68  ? -107.424 52.981 -48.185 1.00 23.21 ? 68   MET A N   1 
ATOM   498  C CA  . MET A 1 68  ? -106.756 54.272 -48.199 1.00 24.05 ? 68   MET A CA  1 
ATOM   499  C C   . MET A 1 68  ? -106.651 54.911 -46.812 1.00 24.50 ? 68   MET A C   1 
ATOM   500  O O   . MET A 1 68  ? -105.590 55.415 -46.447 1.00 26.49 ? 68   MET A O   1 
ATOM   501  C CB  . MET A 1 68  ? -107.460 55.248 -49.156 1.00 25.77 ? 68   MET A CB  1 
ATOM   502  C CG  . MET A 1 68  ? -107.081 55.062 -50.619 1.00 31.94 ? 68   MET A CG  1 
ATOM   503  S SD  . MET A 1 68  ? -105.277 55.012 -50.924 1.00 37.34 ? 68   MET A SD  1 
ATOM   504  C CE  . MET A 1 68  ? -104.740 56.627 -50.313 1.00 24.98 ? 68   MET A CE  1 
ATOM   505  N N   . GLU A 1 69  ? -107.747 54.912 -46.051 1.00 24.27 ? 69   GLU A N   1 
ATOM   506  C CA  . GLU A 1 69  ? -107.723 55.490 -44.714 1.00 25.16 ? 69   GLU A CA  1 
ATOM   507  C C   . GLU A 1 69  ? -106.664 54.778 -43.864 1.00 24.93 ? 69   GLU A C   1 
ATOM   508  O O   . GLU A 1 69  ? -105.945 55.419 -43.094 1.00 23.41 ? 69   GLU A O   1 
ATOM   509  C CB  . GLU A 1 69  ? -109.102 55.388 -44.039 1.00 27.28 ? 69   GLU A CB  1 
ATOM   510  C CG  . GLU A 1 69  ? -109.104 55.961 -42.629 1.00 32.88 ? 69   GLU A CG  1 
ATOM   511  C CD  . GLU A 1 69  ? -110.458 55.919 -41.936 1.00 36.89 ? 69   GLU A CD  1 
ATOM   512  O OE1 . GLU A 1 69  ? -111.169 54.898 -42.041 1.00 39.84 ? 69   GLU A OE1 1 
ATOM   513  O OE2 . GLU A 1 69  ? -110.800 56.910 -41.261 1.00 40.70 ? 69   GLU A OE2 1 
ATOM   514  N N   . LEU A 1 70  ? -106.559 53.459 -44.019 1.00 22.02 ? 70   LEU A N   1 
ATOM   515  C CA  . LEU A 1 70  ? -105.571 52.683 -43.275 1.00 23.52 ? 70   LEU A CA  1 
ATOM   516  C C   . LEU A 1 70  ? -104.150 53.070 -43.707 1.00 26.18 ? 70   LEU A C   1 
ATOM   517  O O   . LEU A 1 70  ? -103.271 53.274 -42.865 1.00 24.75 ? 70   LEU A O   1 
ATOM   518  C CB  . LEU A 1 70  ? -105.790 51.184 -43.511 1.00 22.65 ? 70   LEU A CB  1 
ATOM   519  C CG  . LEU A 1 70  ? -104.770 50.164 -42.984 1.00 24.31 ? 70   LEU A CG  1 
ATOM   520  C CD1 . LEU A 1 70  ? -104.757 50.148 -41.458 1.00 22.86 ? 70   LEU A CD1 1 
ATOM   521  C CD2 . LEU A 1 70  ? -105.135 48.774 -43.518 1.00 20.42 ? 70   LEU A CD2 1 
ATOM   522  N N   . LEU A 1 71  ? -103.925 53.179 -45.016 1.00 23.47 ? 71   LEU A N   1 
ATOM   523  C CA  . LEU A 1 71  ? -102.596 53.528 -45.507 1.00 23.80 ? 71   LEU A CA  1 
ATOM   524  C C   . LEU A 1 71  ? -102.196 54.938 -45.070 1.00 24.24 ? 71   LEU A C   1 
ATOM   525  O O   . LEU A 1 71  ? -101.054 55.172 -44.670 1.00 22.13 ? 71   LEU A O   1 
ATOM   526  C CB  . LEU A 1 71  ? -102.541 53.408 -47.036 1.00 23.09 ? 71   LEU A CB  1 
ATOM   527  C CG  . LEU A 1 71  ? -102.789 52.010 -47.636 1.00 24.08 ? 71   LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 71  ? -102.900 52.106 -49.145 1.00 26.71 ? 71   LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 71  ? -101.658 51.074 -47.265 1.00 23.63 ? 71   LEU A CD2 1 
ATOM   530  N N   . ILE A 1 72  ? -103.145 55.866 -45.143 1.00 23.77 ? 72   ILE A N   1 
ATOM   531  C CA  . ILE A 1 72  ? -102.904 57.246 -44.759 1.00 26.17 ? 72   ILE A CA  1 
ATOM   532  C C   . ILE A 1 72  ? -102.586 57.345 -43.262 1.00 26.21 ? 72   ILE A C   1 
ATOM   533  O O   . ILE A 1 72  ? -101.713 58.112 -42.851 1.00 28.08 ? 72   ILE A O   1 
ATOM   534  C CB  . ILE A 1 72  ? -104.125 58.122 -45.145 1.00 26.83 ? 72   ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 72  ? -104.141 58.315 -46.660 1.00 27.75 ? 72   ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 72  ? -104.071 59.469 -44.452 1.00 28.30 ? 72   ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 72  ? -105.393 58.949 -47.191 1.00 29.36 ? 72   ILE A CD1 1 
ATOM   538  N N   . MET A 1 73  ? -103.277 56.558 -42.449 1.00 25.06 ? 73   MET A N   1 
ATOM   539  C CA  . MET A 1 73  ? -103.016 56.567 -41.018 1.00 26.34 ? 73   MET A CA  1 
ATOM   540  C C   . MET A 1 73  ? -101.625 56.012 -40.752 1.00 25.95 ? 73   MET A C   1 
ATOM   541  O O   . MET A 1 73  ? -100.880 56.551 -39.934 1.00 26.75 ? 73   MET A O   1 
ATOM   542  C CB  . MET A 1 73  ? -104.056 55.738 -40.269 1.00 25.14 ? 73   MET A CB  1 
ATOM   543  C CG  . MET A 1 73  ? -105.395 56.416 -40.157 1.00 28.93 ? 73   MET A CG  1 
ATOM   544  S SD  . MET A 1 73  ? -106.453 55.600 -38.953 1.00 38.85 ? 73   MET A SD  1 
ATOM   545  C CE  . MET A 1 73  ? -105.764 56.215 -37.446 1.00 29.48 ? 73   MET A CE  1 
ATOM   546  N N   . ILE A 1 74  ? -101.274 54.936 -41.446 1.00 24.87 ? 74   ILE A N   1 
ATOM   547  C CA  . ILE A 1 74  ? -99.955  54.336 -41.284 1.00 24.53 ? 74   ILE A CA  1 
ATOM   548  C C   . ILE A 1 74  ? -98.868  55.341 -41.656 1.00 26.33 ? 74   ILE A C   1 
ATOM   549  O O   . ILE A 1 74  ? -97.863  55.457 -40.965 1.00 26.87 ? 74   ILE A O   1 
ATOM   550  C CB  . ILE A 1 74  ? -99.775  53.088 -42.182 1.00 22.69 ? 74   ILE A CB  1 
ATOM   551  C CG1 . ILE A 1 74  ? -100.756 51.991 -41.771 1.00 21.36 ? 74   ILE A CG1 1 
ATOM   552  C CG2 . ILE A 1 74  ? -98.352  52.564 -42.060 1.00 23.29 ? 74   ILE A CG2 1 
ATOM   553  C CD1 . ILE A 1 74  ? -100.813 50.828 -42.728 1.00 20.73 ? 74   ILE A CD1 1 
ATOM   554  N N   . ASN A 1 75  ? -99.069  56.065 -42.753 1.00 27.47 ? 75   ASN A N   1 
ATOM   555  C CA  . ASN A 1 75  ? -98.082  57.036 -43.196 1.00 27.38 ? 75   ASN A CA  1 
ATOM   556  C C   . ASN A 1 75  ? -97.900  58.169 -42.174 1.00 27.59 ? 75   ASN A C   1 
ATOM   557  O O   . ASN A 1 75  ? -96.775  58.562 -41.857 1.00 28.09 ? 75   ASN A O   1 
ATOM   558  C CB  . ASN A 1 75  ? -98.489  57.613 -44.553 1.00 28.84 ? 75   ASN A CB  1 
ATOM   559  C CG  . ASN A 1 75  ? -97.609  58.779 -44.979 1.00 33.10 ? 75   ASN A CG  1 
ATOM   560  O OD1 . ASN A 1 75  ? -98.079  59.913 -45.115 1.00 36.61 ? 75   ASN A OD1 1 
ATOM   561  N ND2 . ASN A 1 75  ? -96.324  58.509 -45.176 1.00 31.95 ? 75   ASN A ND2 1 
ATOM   562  N N   . ALA A 1 76  ? -99.014  58.681 -41.662 1.00 27.58 ? 76   ALA A N   1 
ATOM   563  C CA  . ALA A 1 76  ? -98.991  59.776 -40.701 1.00 26.94 ? 76   ALA A CA  1 
ATOM   564  C C   . ALA A 1 76  ? -98.265  59.387 -39.420 1.00 24.68 ? 76   ALA A C   1 
ATOM   565  O O   . ALA A 1 76  ? -97.509  60.179 -38.872 1.00 26.18 ? 76   ALA A O   1 
ATOM   566  C CB  . ALA A 1 76  ? -100.425 60.233 -40.385 1.00 26.44 ? 76   ALA A CB  1 
ATOM   567  N N   . CYS A 1 77  ? -98.495  58.170 -38.946 1.00 25.28 ? 77   CYS A N   1 
ATOM   568  C CA  . CYS A 1 77  ? -97.841  57.703 -37.728 1.00 27.37 ? 77   CYS A CA  1 
ATOM   569  C C   . CYS A 1 77  ? -96.341  57.559 -37.987 1.00 28.73 ? 77   CYS A C   1 
ATOM   570  O O   . CYS A 1 77  ? -95.522  58.049 -37.216 1.00 28.36 ? 77   CYS A O   1 
ATOM   571  C CB  . CYS A 1 77  ? -98.447  56.368 -37.268 1.00 24.80 ? 77   CYS A CB  1 
ATOM   572  S SG  . CYS A 1 77  ? -100.087 56.503 -36.461 1.00 27.85 ? 77   CYS A SG  1 
ATOM   573  N N   . LYS A 1 78  ? -95.996  56.914 -39.097 1.00 29.76 ? 78   LYS A N   1 
ATOM   574  C CA  . LYS A 1 78  ? -94.602  56.706 -39.470 1.00 31.65 ? 78   LYS A CA  1 
ATOM   575  C C   . LYS A 1 78  ? -93.795  58.008 -39.515 1.00 30.01 ? 78   LYS A C   1 
ATOM   576  O O   . LYS A 1 78  ? -92.753  58.118 -38.878 1.00 31.64 ? 78   LYS A O   1 
ATOM   577  C CB  . LYS A 1 78  ? -94.530  56.000 -40.831 1.00 32.46 ? 78   LYS A CB  1 
ATOM   578  C CG  . LYS A 1 78  ? -93.457  54.934 -40.898 1.00 38.18 ? 78   LYS A CG  1 
ATOM   579  C CD  . LYS A 1 78  ? -93.649  53.928 -39.763 1.00 40.46 ? 78   LYS A CD  1 
ATOM   580  C CE  . LYS A 1 78  ? -92.389  53.120 -39.508 1.00 41.14 ? 78   LYS A CE  1 
ATOM   581  N NZ  . LYS A 1 78  ? -92.045  52.226 -40.644 1.00 42.67 ? 78   LYS A NZ  1 
ATOM   582  N N   . ILE A 1 79  ? -94.270  58.996 -40.265 1.00 30.16 ? 79   ILE A N   1 
ATOM   583  C CA  . ILE A 1 79  ? -93.551  60.269 -40.352 1.00 28.64 ? 79   ILE A CA  1 
ATOM   584  C C   . ILE A 1 79  ? -93.640  61.090 -39.062 1.00 29.82 ? 79   ILE A C   1 
ATOM   585  O O   . ILE A 1 79  ? -92.923  62.075 -38.899 1.00 29.88 ? 79   ILE A O   1 
ATOM   586  C CB  . ILE A 1 79  ? -94.039  61.135 -41.525 1.00 28.51 ? 79   ILE A CB  1 
ATOM   587  C CG1 . ILE A 1 79  ? -95.530  61.395 -41.390 1.00 25.67 ? 79   ILE A CG1 1 
ATOM   588  C CG2 . ILE A 1 79  ? -93.772  60.427 -42.863 1.00 29.41 ? 79   ILE A CG2 1 
ATOM   589  C CD1 . ILE A 1 79  ? -96.026  62.430 -42.361 1.00 28.33 ? 79   ILE A CD1 1 
ATOM   590  N N   . ALA A 1 80  ? -94.530  60.687 -38.156 1.00 30.82 ? 80   ALA A N   1 
ATOM   591  C CA  . ALA A 1 80  ? -94.662  61.352 -36.857 1.00 30.79 ? 80   ALA A CA  1 
ATOM   592  C C   . ALA A 1 80  ? -93.720  60.662 -35.852 1.00 31.42 ? 80   ALA A C   1 
ATOM   593  O O   . ALA A 1 80  ? -93.883  60.771 -34.637 1.00 32.36 ? 80   ALA A O   1 
ATOM   594  C CB  . ALA A 1 80  ? -96.103  61.309 -36.365 1.00 29.48 ? 80   ALA A CB  1 
ATOM   595  N N   . SER A 1 81  ? -92.737  59.945 -36.395 1.00 32.51 ? 81   SER A N   1 
ATOM   596  C CA  . SER A 1 81  ? -91.715  59.246 -35.617 1.00 31.93 ? 81   SER A CA  1 
ATOM   597  C C   . SER A 1 81  ? -92.176  58.121 -34.717 1.00 32.78 ? 81   SER A C   1 
ATOM   598  O O   . SER A 1 81  ? -91.570  57.870 -33.670 1.00 32.23 ? 81   SER A O   1 
ATOM   599  C CB  . SER A 1 81  ? -90.891  60.231 -34.779 1.00 31.20 ? 81   SER A CB  1 
ATOM   600  O OG  . SER A 1 81  ? -90.190  61.139 -35.592 1.00 29.18 ? 81   SER A OG  1 
ATOM   601  N N   . ALA A 1 82  ? -93.232  57.427 -35.116 1.00 32.67 ? 82   ALA A N   1 
ATOM   602  C CA  . ALA A 1 82  ? -93.693  56.297 -34.328 1.00 31.96 ? 82   ALA A CA  1 
ATOM   603  C C   . ALA A 1 82  ? -92.564  55.260 -34.350 1.00 31.65 ? 82   ALA A C   1 
ATOM   604  O O   . ALA A 1 82  ? -91.863  55.109 -35.353 1.00 30.11 ? 82   ALA A O   1 
ATOM   605  C CB  . ALA A 1 82  ? -94.969  55.711 -34.937 1.00 31.05 ? 82   ALA A CB  1 
ATOM   606  N N   . SER A 1 83  ? -92.388  54.557 -33.240 1.00 32.06 ? 83   SER A N   1 
ATOM   607  C CA  . SER A 1 83  ? -91.345  53.545 -33.147 1.00 32.08 ? 83   SER A CA  1 
ATOM   608  C C   . SER A 1 83  ? -91.624  52.335 -34.031 1.00 32.31 ? 83   SER A C   1 
ATOM   609  O O   . SER A 1 83  ? -90.719  51.797 -34.670 1.00 31.62 ? 83   SER A O   1 
ATOM   610  C CB  . SER A 1 83  ? -91.183  53.082 -31.701 1.00 33.15 ? 83   SER A CB  1 
ATOM   611  O OG  . SER A 1 83  ? -90.411  51.894 -31.643 1.00 37.21 ? 83   SER A OG  1 
ATOM   612  N N   . ARG A 1 84  ? -92.879  51.900 -34.058 1.00 31.21 ? 84   ARG A N   1 
ATOM   613  C CA  . ARG A 1 84  ? -93.268  50.752 -34.868 1.00 30.86 ? 84   ARG A CA  1 
ATOM   614  C C   . ARG A 1 84  ? -94.755  50.832 -35.167 1.00 29.58 ? 84   ARG A C   1 
ATOM   615  O O   . ARG A 1 84  ? -95.545  51.211 -34.302 1.00 29.40 ? 84   ARG A O   1 
ATOM   616  C CB  . ARG A 1 84  ? -92.949  49.450 -34.118 1.00 31.30 ? 84   ARG A CB  1 
ATOM   617  C CG  . ARG A 1 84  ? -93.231  48.176 -34.910 1.00 37.11 ? 84   ARG A CG  1 
ATOM   618  C CD  . ARG A 1 84  ? -92.739  46.902 -34.190 1.00 39.36 ? 84   ARG A CD  1 
ATOM   619  N NE  . ARG A 1 84  ? -93.532  46.602 -33.001 1.00 43.86 ? 84   ARG A NE  1 
ATOM   620  C CZ  . ARG A 1 84  ? -93.338  45.555 -32.203 1.00 44.49 ? 84   ARG A CZ  1 
ATOM   621  N NH1 . ARG A 1 84  ? -92.365  44.687 -32.456 1.00 43.53 ? 84   ARG A NH1 1 
ATOM   622  N NH2 . ARG A 1 84  ? -94.129  45.372 -31.155 1.00 43.60 ? 84   ARG A NH2 1 
ATOM   623  N N   . VAL A 1 85  ? -95.138  50.478 -36.389 1.00 28.58 ? 85   VAL A N   1 
ATOM   624  C CA  . VAL A 1 85  ? -96.545  50.509 -36.771 1.00 26.89 ? 85   VAL A CA  1 
ATOM   625  C C   . VAL A 1 85  ? -96.999  49.142 -37.255 1.00 26.21 ? 85   VAL A C   1 
ATOM   626  O O   . VAL A 1 85  ? -96.408  48.567 -38.170 1.00 24.63 ? 85   VAL A O   1 
ATOM   627  C CB  . VAL A 1 85  ? -96.828  51.533 -37.921 1.00 27.98 ? 85   VAL A CB  1 
ATOM   628  C CG1 . VAL A 1 85  ? -98.341  51.588 -38.197 1.00 24.86 ? 85   VAL A CG1 1 
ATOM   629  C CG2 . VAL A 1 85  ? -96.308  52.919 -37.548 1.00 23.74 ? 85   VAL A CG2 1 
ATOM   630  N N   . THR A 1 86  ? -98.065  48.637 -36.648 1.00 25.19 ? 86   THR A N   1 
ATOM   631  C CA  . THR A 1 86  ? -98.609  47.348 -37.016 1.00 25.09 ? 86   THR A CA  1 
ATOM   632  C C   . THR A 1 86  ? -100.025 47.515 -37.538 1.00 26.32 ? 86   THR A C   1 
ATOM   633  O O   . THR A 1 86  ? -100.837 48.216 -36.930 1.00 24.45 ? 86   THR A O   1 
ATOM   634  C CB  . THR A 1 86  ? -98.668  46.398 -35.801 1.00 26.26 ? 86   THR A CB  1 
ATOM   635  O OG1 . THR A 1 86  ? -97.345  46.150 -35.329 1.00 25.97 ? 86   THR A OG1 1 
ATOM   636  C CG2 . THR A 1 86  ? -99.336  45.080 -36.181 1.00 22.05 ? 86   THR A CG2 1 
ATOM   637  N N   . ALA A 1 87  ? -100.312 46.882 -38.671 1.00 25.94 ? 87   ALA A N   1 
ATOM   638  C CA  . ALA A 1 87  ? -101.644 46.931 -39.232 1.00 25.68 ? 87   ALA A CA  1 
ATOM   639  C C   . ALA A 1 87  ? -102.381 45.678 -38.785 1.00 24.80 ? 87   ALA A C   1 
ATOM   640  O O   . ALA A 1 87  ? -101.938 44.563 -39.029 1.00 24.96 ? 87   ALA A O   1 
ATOM   641  C CB  . ALA A 1 87  ? -101.596 47.002 -40.773 1.00 24.60 ? 87   ALA A CB  1 
ATOM   642  N N   . VAL A 1 88  ? -103.485 45.884 -38.078 1.00 26.20 ? 88   VAL A N   1 
ATOM   643  C CA  . VAL A 1 88  ? -104.330 44.801 -37.595 1.00 23.44 ? 88   VAL A CA  1 
ATOM   644  C C   . VAL A 1 88  ? -105.473 44.821 -38.605 1.00 26.76 ? 88   VAL A C   1 
ATOM   645  O O   . VAL A 1 88  ? -106.298 45.744 -38.625 1.00 25.13 ? 88   VAL A O   1 
ATOM   646  C CB  . VAL A 1 88  ? -104.846 45.094 -36.177 1.00 22.54 ? 88   VAL A CB  1 
ATOM   647  C CG1 . VAL A 1 88  ? -105.790 43.990 -35.722 1.00 21.26 ? 88   VAL A CG1 1 
ATOM   648  C CG2 . VAL A 1 88  ? -103.654 45.216 -35.220 1.00 21.02 ? 88   VAL A CG2 1 
ATOM   649  N N   . ILE A 1 89  ? -105.491 43.814 -39.469 1.00 25.61 ? 89   ILE A N   1 
ATOM   650  C CA  . ILE A 1 89  ? -106.473 43.732 -40.519 1.00 26.92 ? 89   ILE A CA  1 
ATOM   651  C C   . ILE A 1 89  ? -107.144 42.371 -40.474 1.00 25.74 ? 89   ILE A C   1 
ATOM   652  O O   . ILE A 1 89  ? -106.677 41.426 -41.099 1.00 23.80 ? 89   ILE A O   1 
ATOM   653  C CB  . ILE A 1 89  ? -105.799 43.886 -41.902 1.00 29.46 ? 89   ILE A CB  1 
ATOM   654  C CG1 . ILE A 1 89  ? -104.888 45.110 -41.915 1.00 29.25 ? 89   ILE A CG1 1 
ATOM   655  C CG2 . ILE A 1 89  ? -106.847 44.029 -42.969 1.00 30.97 ? 89   ILE A CG2 1 
ATOM   656  C CD1 . ILE A 1 89  ? -103.828 45.052 -43.036 1.00 27.73 ? 89   ILE A CD1 1 
ATOM   657  N N   . PRO A 1 90  ? -108.253 42.258 -39.728 1.00 27.28 ? 90   PRO A N   1 
ATOM   658  C CA  . PRO A 1 90  ? -109.028 41.031 -39.552 1.00 28.72 ? 90   PRO A CA  1 
ATOM   659  C C   . PRO A 1 90  ? -109.348 40.361 -40.881 1.00 27.36 ? 90   PRO A C   1 
ATOM   660  O O   . PRO A 1 90  ? -109.145 39.169 -41.038 1.00 30.59 ? 90   PRO A O   1 
ATOM   661  C CB  . PRO A 1 90  ? -110.281 41.518 -38.821 1.00 29.09 ? 90   PRO A CB  1 
ATOM   662  C CG  . PRO A 1 90  ? -109.768 42.693 -38.040 1.00 29.94 ? 90   PRO A CG  1 
ATOM   663  C CD  . PRO A 1 90  ? -108.924 43.393 -39.063 1.00 30.05 ? 90   PRO A CD  1 
ATOM   664  N N   . CYS A 1 91  ? -109.841 41.144 -41.829 1.00 27.68 ? 91   CYS A N   1 
ATOM   665  C CA  . CYS A 1 91  ? -110.199 40.643 -43.158 1.00 27.52 ? 91   CYS A CA  1 
ATOM   666  C C   . CYS A 1 91  ? -109.310 41.321 -44.213 1.00 26.06 ? 91   CYS A C   1 
ATOM   667  O O   . CYS A 1 91  ? -109.584 42.432 -44.637 1.00 24.37 ? 91   CYS A O   1 
ATOM   668  C CB  . CYS A 1 91  ? -111.677 40.943 -43.430 1.00 28.90 ? 91   CYS A CB  1 
ATOM   669  S SG  . CYS A 1 91  ? -112.350 40.083 -44.873 1.00 33.60 ? 91   CYS A SG  1 
ATOM   670  N N   . PHE A 1 92  ? -108.238 40.648 -44.620 1.00 26.95 ? 92   PHE A N   1 
ATOM   671  C CA  . PHE A 1 92  ? -107.305 41.204 -45.591 1.00 25.60 ? 92   PHE A CA  1 
ATOM   672  C C   . PHE A 1 92  ? -107.976 41.544 -46.930 1.00 25.92 ? 92   PHE A C   1 
ATOM   673  O O   . PHE A 1 92  ? -108.466 40.657 -47.643 1.00 24.26 ? 92   PHE A O   1 
ATOM   674  C CB  . PHE A 1 92  ? -106.168 40.221 -45.831 1.00 27.40 ? 92   PHE A CB  1 
ATOM   675  C CG  . PHE A 1 92  ? -104.989 40.822 -46.540 1.00 30.10 ? 92   PHE A CG  1 
ATOM   676  C CD1 . PHE A 1 92  ? -103.982 41.464 -45.822 1.00 28.42 ? 92   PHE A CD1 1 
ATOM   677  C CD2 . PHE A 1 92  ? -104.887 40.752 -47.926 1.00 28.72 ? 92   PHE A CD2 1 
ATOM   678  C CE1 . PHE A 1 92  ? -102.894 42.025 -46.476 1.00 30.24 ? 92   PHE A CE1 1 
ATOM   679  C CE2 . PHE A 1 92  ? -103.798 41.313 -48.591 1.00 30.60 ? 92   PHE A CE2 1 
ATOM   680  C CZ  . PHE A 1 92  ? -102.800 41.948 -47.869 1.00 29.15 ? 92   PHE A CZ  1 
ATOM   681  N N   . PRO A 1 93  ? -107.990 42.837 -47.294 1.00 25.83 ? 93   PRO A N   1 
ATOM   682  C CA  . PRO A 1 93  ? -108.601 43.308 -48.543 1.00 25.80 ? 93   PRO A CA  1 
ATOM   683  C C   . PRO A 1 93  ? -107.943 42.745 -49.788 1.00 26.73 ? 93   PRO A C   1 
ATOM   684  O O   . PRO A 1 93  ? -106.718 42.618 -49.853 1.00 26.48 ? 93   PRO A O   1 
ATOM   685  C CB  . PRO A 1 93  ? -108.471 44.832 -48.443 1.00 28.54 ? 93   PRO A CB  1 
ATOM   686  C CG  . PRO A 1 93  ? -107.252 45.024 -47.613 1.00 27.92 ? 93   PRO A CG  1 
ATOM   687  C CD  . PRO A 1 93  ? -107.382 43.958 -46.551 1.00 27.28 ? 93   PRO A CD  1 
ATOM   688  N N   . TYR A 1 94  ? -108.779 42.404 -50.769 1.00 27.35 ? 94   TYR A N   1 
ATOM   689  C CA  . TYR A 1 94  ? -108.341 41.847 -52.048 1.00 25.43 ? 94   TYR A CA  1 
ATOM   690  C C   . TYR A 1 94  ? -107.620 40.514 -51.927 1.00 24.70 ? 94   TYR A C   1 
ATOM   691  O O   . TYR A 1 94  ? -106.953 40.094 -52.865 1.00 23.96 ? 94   TYR A O   1 
ATOM   692  C CB  . TYR A 1 94  ? -107.435 42.846 -52.792 1.00 25.63 ? 94   TYR A CB  1 
ATOM   693  C CG  . TYR A 1 94  ? -108.176 44.053 -53.316 1.00 22.49 ? 94   TYR A CG  1 
ATOM   694  C CD1 . TYR A 1 94  ? -108.429 45.149 -52.493 1.00 22.91 ? 94   TYR A CD1 1 
ATOM   695  C CD2 . TYR A 1 94  ? -108.669 44.076 -54.615 1.00 21.66 ? 94   TYR A CD2 1 
ATOM   696  C CE1 . TYR A 1 94  ? -109.153 46.233 -52.946 1.00 20.82 ? 94   TYR A CE1 1 
ATOM   697  C CE2 . TYR A 1 94  ? -109.404 45.161 -55.086 1.00 22.87 ? 94   TYR A CE2 1 
ATOM   698  C CZ  . TYR A 1 94  ? -109.642 46.237 -54.247 1.00 21.12 ? 94   TYR A CZ  1 
ATOM   699  O OH  . TYR A 1 94  ? -110.356 47.318 -54.705 1.00 20.26 ? 94   TYR A OH  1 
ATOM   700  N N   . ALA A 1 95  ? -107.765 39.845 -50.786 1.00 23.29 ? 95   ALA A N   1 
ATOM   701  C CA  . ALA A 1 95  ? -107.102 38.551 -50.571 1.00 25.76 ? 95   ALA A CA  1 
ATOM   702  C C   . ALA A 1 95  ? -107.474 37.502 -51.621 1.00 26.09 ? 95   ALA A C   1 
ATOM   703  O O   . ALA A 1 95  ? -106.671 36.635 -51.948 1.00 27.47 ? 95   ALA A O   1 
ATOM   704  C CB  . ALA A 1 95  ? -107.424 38.014 -49.174 1.00 22.29 ? 95   ALA A CB  1 
ATOM   705  N N   . ARG A 1 96  ? -108.690 37.573 -52.143 1.00 26.85 ? 96   ARG A N   1 
ATOM   706  C CA  . ARG A 1 96  ? -109.114 36.615 -53.151 1.00 30.45 ? 96   ARG A CA  1 
ATOM   707  C C   . ARG A 1 96  ? -108.381 36.821 -54.479 1.00 32.51 ? 96   ARG A C   1 
ATOM   708  O O   . ARG A 1 96  ? -108.277 35.890 -55.280 1.00 31.34 ? 96   ARG A O   1 
ATOM   709  C CB  . ARG A 1 96  ? -110.621 36.714 -53.391 1.00 33.33 ? 96   ARG A CB  1 
ATOM   710  C CG  . ARG A 1 96  ? -111.481 36.240 -52.237 1.00 37.33 ? 96   ARG A CG  1 
ATOM   711  C CD  . ARG A 1 96  ? -112.745 35.587 -52.760 1.00 43.39 ? 96   ARG A CD  1 
ATOM   712  N NE  . ARG A 1 96  ? -112.965 34.290 -52.125 1.00 50.32 ? 96   ARG A NE  1 
ATOM   713  C CZ  . ARG A 1 96  ? -113.687 33.304 -52.651 1.00 50.99 ? 96   ARG A CZ  1 
ATOM   714  N NH1 . ARG A 1 96  ? -114.269 33.462 -53.833 1.00 49.46 ? 96   ARG A NH1 1 
ATOM   715  N NH2 . ARG A 1 96  ? -113.815 32.154 -51.996 1.00 51.43 ? 96   ARG A NH2 1 
ATOM   716  N N   . GLN A 1 97  ? -107.887 38.038 -54.716 1.00 30.11 ? 97   GLN A N   1 
ATOM   717  C CA  . GLN A 1 97  ? -107.169 38.337 -55.957 1.00 31.36 ? 97   GLN A CA  1 
ATOM   718  C C   . GLN A 1 97  ? -105.688 38.061 -55.718 1.00 29.50 ? 97   GLN A C   1 
ATOM   719  O O   . GLN A 1 97  ? -104.864 38.980 -55.712 1.00 28.51 ? 97   GLN A O   1 
ATOM   720  C CB  . GLN A 1 97  ? -107.400 39.807 -56.363 1.00 30.26 ? 97   GLN A CB  1 
ATOM   721  C CG  . GLN A 1 97  ? -108.842 40.099 -56.787 1.00 34.79 ? 97   GLN A CG  1 
ATOM   722  C CD  . GLN A 1 97  ? -109.086 41.558 -57.179 1.00 37.38 ? 97   GLN A CD  1 
ATOM   723  O OE1 . GLN A 1 97  ? -108.347 42.140 -57.978 1.00 37.00 ? 97   GLN A OE1 1 
ATOM   724  N NE2 . GLN A 1 97  ? -110.134 42.144 -56.622 1.00 36.76 ? 97   GLN A NE2 1 
ATOM   725  N N   . ASP A 1 98  ? -105.361 36.785 -55.531 1.00 29.64 ? 98   ASP A N   1 
ATOM   726  C CA  . ASP A 1 98  ? -103.989 36.380 -55.229 1.00 32.28 ? 98   ASP A CA  1 
ATOM   727  C C   . ASP A 1 98  ? -103.240 35.531 -56.267 1.00 32.24 ? 98   ASP A C   1 
ATOM   728  O O   . ASP A 1 98  ? -102.229 34.909 -55.952 1.00 33.16 ? 98   ASP A O   1 
ATOM   729  C CB  . ASP A 1 98  ? -103.966 35.679 -53.857 1.00 31.37 ? 98   ASP A CB  1 
ATOM   730  C CG  . ASP A 1 98  ? -104.795 34.399 -53.826 1.00 32.63 ? 98   ASP A CG  1 
ATOM   731  O OD1 . ASP A 1 98  ? -105.750 34.268 -54.615 1.00 31.98 ? 98   ASP A OD1 1 
ATOM   732  O OD2 . ASP A 1 98  ? -104.497 33.526 -52.991 1.00 34.21 ? 98   ASP A OD2 1 
ATOM   733  N N   . LYS A 1 99  ? -103.731 35.520 -57.501 1.00 32.32 ? 99   LYS A N   1 
ATOM   734  C CA  . LYS A 1 99  ? -103.102 34.780 -58.593 1.00 31.32 ? 99   LYS A CA  1 
ATOM   735  C C   . LYS A 1 99  ? -103.734 35.208 -59.914 1.00 30.52 ? 99   LYS A C   1 
ATOM   736  O O   . LYS A 1 99  ? -104.860 35.693 -59.931 1.00 28.73 ? 99   LYS A O   1 
ATOM   737  C CB  . LYS A 1 99  ? -103.253 33.272 -58.390 1.00 30.99 ? 99   LYS A CB  1 
ATOM   738  C CG  . LYS A 1 99  ? -104.674 32.785 -58.230 1.00 37.21 ? 99   LYS A CG  1 
ATOM   739  C CD  . LYS A 1 99  ? -104.681 31.367 -57.664 1.00 42.13 ? 99   LYS A CD  1 
ATOM   740  C CE  . LYS A 1 99  ? -106.062 30.948 -57.172 1.00 45.05 ? 99   LYS A CE  1 
ATOM   741  N NZ  . LYS A 1 99  ? -106.000 29.655 -56.406 1.00 48.70 ? 99   LYS A NZ  1 
ATOM   742  N N   . LYS A 1 100 ? -102.997 35.055 -61.011 1.00 31.28 ? 100  LYS A N   1 
ATOM   743  C CA  . LYS A 1 100 ? -103.495 35.439 -62.335 1.00 33.35 ? 100  LYS A CA  1 
ATOM   744  C C   . LYS A 1 100 ? -104.628 34.530 -62.796 1.00 34.99 ? 100  LYS A C   1 
ATOM   745  O O   . LYS A 1 100 ? -105.533 34.966 -63.509 1.00 34.01 ? 100  LYS A O   1 
ATOM   746  C CB  . LYS A 1 100 ? -102.375 35.394 -63.375 1.00 31.36 ? 100  LYS A CB  1 
ATOM   747  C CG  . LYS A 1 100 ? -101.288 36.437 -63.203 1.00 31.32 ? 100  LYS A CG  1 
ATOM   748  C CD  . LYS A 1 100 ? -100.288 36.326 -64.336 1.00 27.38 ? 100  LYS A CD  1 
ATOM   749  C CE  . LYS A 1 100 ? -99.097  37.211 -64.098 1.00 30.09 ? 100  LYS A CE  1 
ATOM   750  N NZ  . LYS A 1 100 ? -98.022  36.991 -65.118 1.00 28.68 ? 100  LYS A NZ  1 
ATOM   751  N N   . ASP A 1 101 ? -104.554 33.261 -62.409 1.00 37.70 ? 101  ASP A N   1 
ATOM   752  C CA  . ASP A 1 101 ? -105.596 32.301 -62.760 1.00 41.40 ? 101  ASP A CA  1 
ATOM   753  C C   . ASP A 1 101 ? -105.805 32.192 -64.272 1.00 42.93 ? 101  ASP A C   1 
ATOM   754  O O   . ASP A 1 101 ? -106.942 32.282 -64.746 1.00 42.84 ? 101  ASP A O   1 
ATOM   755  C CB  . ASP A 1 101 ? -106.910 32.731 -62.099 1.00 42.65 ? 101  ASP A CB  1 
ATOM   756  C CG  . ASP A 1 101 ? -107.921 31.611 -62.018 1.00 45.34 ? 101  ASP A CG  1 
ATOM   757  O OD1 . ASP A 1 101 ? -107.657 30.627 -61.290 1.00 47.44 ? 101  ASP A OD1 1 
ATOM   758  O OD2 . ASP A 1 101 ? -108.980 31.716 -62.672 1.00 45.52 ? 101  ASP A OD2 1 
ATOM   759  N N   . LYS A 1 102 ? -104.723 31.989 -65.023 1.00 43.00 ? 102  LYS A N   1 
ATOM   760  C CA  . LYS A 1 102 ? -104.814 31.879 -66.483 1.00 43.78 ? 102  LYS A CA  1 
ATOM   761  C C   . LYS A 1 102 ? -105.389 33.105 -67.175 1.00 42.96 ? 102  LYS A C   1 
ATOM   762  O O   . LYS A 1 102 ? -106.098 32.974 -68.173 1.00 45.29 ? 102  LYS A O   1 
ATOM   763  C CB  . LYS A 1 102 ? -105.654 30.666 -66.892 1.00 46.27 ? 102  LYS A CB  1 
ATOM   764  C CG  . LYS A 1 102 ? -104.904 29.344 -66.918 1.00 50.84 ? 102  LYS A CG  1 
ATOM   765  C CD  . LYS A 1 102 ? -104.937 28.712 -68.308 1.00 52.76 ? 102  LYS A CD  1 
ATOM   766  C CE  . LYS A 1 102 ? -106.337 28.236 -68.664 1.00 54.90 ? 102  LYS A CE  1 
ATOM   767  N NZ  . LYS A 1 102 ? -106.403 27.698 -70.054 1.00 54.05 ? 102  LYS A NZ  1 
ATOM   768  N N   . SER A 1 103 ? -105.102 34.288 -66.651 1.00 40.73 ? 103  SER A N   1 
ATOM   769  C CA  . SER A 1 103 ? -105.586 35.516 -67.271 1.00 38.80 ? 103  SER A CA  1 
ATOM   770  C C   . SER A 1 103 ? -104.563 36.625 -67.134 1.00 35.37 ? 103  SER A C   1 
ATOM   771  O O   . SER A 1 103 ? -103.556 36.473 -66.445 1.00 35.12 ? 103  SER A O   1 
ATOM   772  C CB  . SER A 1 103 ? -106.892 35.970 -66.618 1.00 40.78 ? 103  SER A CB  1 
ATOM   773  O OG  . SER A 1 103 ? -107.877 34.959 -66.730 1.00 45.79 ? 103  SER A OG  1 
ATOM   774  N N   . ARG A 1 104 ? -104.831 37.732 -67.820 1.00 33.39 ? 104  ARG A N   1 
ATOM   775  C CA  . ARG A 1 104 ? -103.983 38.918 -67.774 1.00 32.91 ? 104  ARG A CA  1 
ATOM   776  C C   . ARG A 1 104 ? -104.591 39.742 -66.654 1.00 31.78 ? 104  ARG A C   1 
ATOM   777  O O   . ARG A 1 104 ? -105.100 40.846 -66.855 1.00 32.45 ? 104  ARG A O   1 
ATOM   778  C CB  . ARG A 1 104 ? -104.030 39.678 -69.110 1.00 34.47 ? 104  ARG A CB  1 
ATOM   779  C CG  . ARG A 1 104 ? -103.091 39.117 -70.164 1.00 37.15 ? 104  ARG A CG  1 
ATOM   780  C CD  . ARG A 1 104 ? -103.059 39.973 -71.423 1.00 36.12 ? 104  ARG A CD  1 
ATOM   781  N NE  . ARG A 1 104 ? -104.210 39.728 -72.283 1.00 39.12 ? 104  ARG A NE  1 
ATOM   782  C CZ  . ARG A 1 104 ? -104.254 38.787 -73.216 1.00 36.07 ? 104  ARG A CZ  1 
ATOM   783  N NH1 . ARG A 1 104 ? -103.211 38.005 -73.417 1.00 35.96 ? 104  ARG A NH1 1 
ATOM   784  N NH2 . ARG A 1 104 ? -105.348 38.620 -73.944 1.00 43.14 ? 104  ARG A NH2 1 
ATOM   785  N N   . ALA A 1 105 ? -104.548 39.160 -65.466 1.00 30.00 ? 105  ALA A N   1 
ATOM   786  C CA  . ALA A 1 105 ? -105.114 39.770 -64.290 1.00 29.64 ? 105  ALA A CA  1 
ATOM   787  C C   . ALA A 1 105 ? -104.053 40.245 -63.314 1.00 28.05 ? 105  ALA A C   1 
ATOM   788  O O   . ALA A 1 105 ? -102.908 39.824 -63.371 1.00 26.67 ? 105  ALA A O   1 
ATOM   789  C CB  . ALA A 1 105 ? -106.036 38.783 -63.613 1.00 30.19 ? 105  ALA A CB  1 
ATOM   790  N N   . PRO A 1 106 ? -104.427 41.153 -62.407 1.00 26.73 ? 106  PRO A N   1 
ATOM   791  C CA  . PRO A 1 106 ? -103.472 41.660 -61.426 1.00 27.44 ? 106  PRO A CA  1 
ATOM   792  C C   . PRO A 1 106 ? -103.452 40.706 -60.242 1.00 26.00 ? 106  PRO A C   1 
ATOM   793  O O   . PRO A 1 106 ? -104.377 39.912 -60.070 1.00 27.02 ? 106  PRO A O   1 
ATOM   794  C CB  . PRO A 1 106 ? -104.081 42.991 -61.037 1.00 26.74 ? 106  PRO A CB  1 
ATOM   795  C CG  . PRO A 1 106 ? -105.536 42.647 -60.996 1.00 27.86 ? 106  PRO A CG  1 
ATOM   796  C CD  . PRO A 1 106 ? -105.720 41.846 -62.273 1.00 27.50 ? 106  PRO A CD  1 
ATOM   797  N N   . ILE A 1 107 ? -102.386 40.751 -59.454 1.00 25.22 ? 107  ILE A N   1 
ATOM   798  C CA  . ILE A 1 107 ? -102.322 39.938 -58.242 1.00 24.11 ? 107  ILE A CA  1 
ATOM   799  C C   . ILE A 1 107 ? -102.492 41.044 -57.201 1.00 24.99 ? 107  ILE A C   1 
ATOM   800  O O   . ILE A 1 107 ? -101.545 41.463 -56.538 1.00 25.66 ? 107  ILE A O   1 
ATOM   801  C CB  . ILE A 1 107 ? -100.965 39.229 -58.087 1.00 23.46 ? 107  ILE A CB  1 
ATOM   802  C CG1 . ILE A 1 107 ? -100.757 38.251 -59.247 1.00 25.68 ? 107  ILE A CG1 1 
ATOM   803  C CG2 . ILE A 1 107 ? -100.924 38.457 -56.767 1.00 24.58 ? 107  ILE A CG2 1 
ATOM   804  C CD1 . ILE A 1 107 ? -99.428  37.502 -59.215 1.00 21.74 ? 107  ILE A CD1 1 
ATOM   805  N N   . SER A 1 108 ? -103.722 41.539 -57.116 1.00 24.35 ? 108  SER A N   1 
ATOM   806  C CA  . SER A 1 108 ? -104.086 42.631 -56.224 1.00 24.28 ? 108  SER A CA  1 
ATOM   807  C C   . SER A 1 108 ? -103.670 42.472 -54.775 1.00 23.41 ? 108  SER A C   1 
ATOM   808  O O   . SER A 1 108 ? -103.311 43.455 -54.129 1.00 23.90 ? 108  SER A O   1 
ATOM   809  C CB  . SER A 1 108 ? -105.589 42.870 -56.296 1.00 23.55 ? 108  SER A CB  1 
ATOM   810  O OG  . SER A 1 108 ? -105.966 43.246 -57.599 1.00 22.64 ? 108  SER A OG  1 
ATOM   811  N N   . ALA A 1 109 ? -103.724 41.249 -54.258 1.00 21.80 ? 109  ALA A N   1 
ATOM   812  C CA  . ALA A 1 109 ? -103.331 41.019 -52.874 1.00 21.71 ? 109  ALA A CA  1 
ATOM   813  C C   . ALA A 1 109 ? -101.863 41.402 -52.676 1.00 22.81 ? 109  ALA A C   1 
ATOM   814  O O   . ALA A 1 109 ? -101.470 41.878 -51.608 1.00 24.95 ? 109  ALA A O   1 
ATOM   815  C CB  . ALA A 1 109 ? -103.557 39.564 -52.503 1.00 21.61 ? 109  ALA A CB  1 
ATOM   816  N N   . LYS A 1 110 ? -101.046 41.194 -53.704 1.00 23.49 ? 110  LYS A N   1 
ATOM   817  C CA  . LYS A 1 110 ? -99.634  41.548 -53.616 1.00 21.31 ? 110  LYS A CA  1 
ATOM   818  C C   . LYS A 1 110 ? -99.476  43.059 -53.745 1.00 21.00 ? 110  LYS A C   1 
ATOM   819  O O   . LYS A 1 110 ? -98.592  43.647 -53.133 1.00 22.76 ? 110  LYS A O   1 
ATOM   820  C CB  . LYS A 1 110 ? -98.839  40.854 -54.715 1.00 22.62 ? 110  LYS A CB  1 
ATOM   821  C CG  . LYS A 1 110 ? -97.379  41.269 -54.767 1.00 24.83 ? 110  LYS A CG  1 
ATOM   822  C CD  . LYS A 1 110 ? -96.656  40.875 -53.489 1.00 25.91 ? 110  LYS A CD  1 
ATOM   823  C CE  . LYS A 1 110 ? -95.150  40.971 -53.653 1.00 27.52 ? 110  LYS A CE  1 
ATOM   824  N NZ  . LYS A 1 110 ? -94.732  42.381 -53.615 1.00 34.94 ? 110  LYS A NZ  1 
ATOM   825  N N   . LEU A 1 111 ? -100.324 43.689 -54.555 1.00 20.22 ? 111  LEU A N   1 
ATOM   826  C CA  . LEU A 1 111 ? -100.258 45.138 -54.714 1.00 19.61 ? 111  LEU A CA  1 
ATOM   827  C C   . LEU A 1 111 ? -100.515 45.706 -53.313 1.00 20.68 ? 111  LEU A C   1 
ATOM   828  O O   . LEU A 1 111 ? -99.784  46.581 -52.831 1.00 20.93 ? 111  LEU A O   1 
ATOM   829  C CB  . LEU A 1 111 ? -101.357 45.617 -55.664 1.00 22.44 ? 111  LEU A CB  1 
ATOM   830  C CG  . LEU A 1 111 ? -101.310 46.956 -56.416 1.00 27.46 ? 111  LEU A CG  1 
ATOM   831  C CD1 . LEU A 1 111 ? -102.730 47.515 -56.484 1.00 29.26 ? 111  LEU A CD1 1 
ATOM   832  C CD2 . LEU A 1 111 ? -100.389 47.944 -55.764 1.00 24.61 ? 111  LEU A CD2 1 
ATOM   833  N N   . VAL A 1 112 ? -101.563 45.198 -52.670 1.00 17.40 ? 112  VAL A N   1 
ATOM   834  C CA  . VAL A 1 112 ? -101.927 45.633 -51.331 1.00 20.72 ? 112  VAL A CA  1 
ATOM   835  C C   . VAL A 1 112 ? -100.794 45.439 -50.322 1.00 21.41 ? 112  VAL A C   1 
ATOM   836  O O   . VAL A 1 112 ? -100.473 46.354 -49.571 1.00 22.84 ? 112  VAL A O   1 
ATOM   837  C CB  . VAL A 1 112 ? -103.199 44.899 -50.839 1.00 18.94 ? 112  VAL A CB  1 
ATOM   838  C CG1 . VAL A 1 112 ? -103.506 45.278 -49.387 1.00 22.87 ? 112  VAL A CG1 1 
ATOM   839  C CG2 . VAL A 1 112 ? -104.368 45.289 -51.731 1.00 19.61 ? 112  VAL A CG2 1 
ATOM   840  N N   . ALA A 1 113 ? -100.184 44.257 -50.307 1.00 21.05 ? 113  ALA A N   1 
ATOM   841  C CA  . ALA A 1 113 ? -99.081  44.005 -49.383 1.00 21.74 ? 113  ALA A CA  1 
ATOM   842  C C   . ALA A 1 113 ? -97.983  45.038 -49.632 1.00 23.94 ? 113  ALA A C   1 
ATOM   843  O O   . ALA A 1 113 ? -97.373  45.556 -48.688 1.00 22.01 ? 113  ALA A O   1 
ATOM   844  C CB  . ALA A 1 113 ? -98.526  42.593 -49.587 1.00 19.86 ? 113  ALA A CB  1 
ATOM   845  N N   . ASN A 1 114 ? -97.736  45.346 -50.906 1.00 24.03 ? 114  ASN A N   1 
ATOM   846  C CA  . ASN A 1 114 ? -96.709  46.327 -51.242 1.00 24.56 ? 114  ASN A CA  1 
ATOM   847  C C   . ASN A 1 114 ? -97.095  47.730 -50.803 1.00 24.94 ? 114  ASN A C   1 
ATOM   848  O O   . ASN A 1 114 ? -96.257  48.475 -50.288 1.00 26.30 ? 114  ASN A O   1 
ATOM   849  C CB  . ASN A 1 114 ? -96.408  46.322 -52.744 1.00 25.43 ? 114  ASN A CB  1 
ATOM   850  C CG  . ASN A 1 114 ? -95.527  45.162 -53.155 1.00 24.94 ? 114  ASN A CG  1 
ATOM   851  O OD1 . ASN A 1 114 ? -94.809  44.594 -52.334 1.00 25.91 ? 114  ASN A OD1 1 
ATOM   852  N ND2 . ASN A 1 114 ? -95.556  44.823 -54.430 1.00 20.96 ? 114  ASN A ND2 1 
ATOM   853  N N   . MET A 1 115 ? -98.359  48.099 -50.988 1.00 24.45 ? 115  MET A N   1 
ATOM   854  C CA  . MET A 1 115 ? -98.784  49.431 -50.573 1.00 25.56 ? 115  MET A CA  1 
ATOM   855  C C   . MET A 1 115 ? -98.640  49.552 -49.068 1.00 24.48 ? 115  MET A C   1 
ATOM   856  O O   . MET A 1 115 ? -98.143  50.560 -48.565 1.00 23.49 ? 115  MET A O   1 
ATOM   857  C CB  . MET A 1 115 ? -100.229 49.694 -50.984 1.00 25.49 ? 115  MET A CB  1 
ATOM   858  C CG  . MET A 1 115 ? -100.402 49.792 -52.488 1.00 31.15 ? 115  MET A CG  1 
ATOM   859  S SD  . MET A 1 115 ? -102.095 50.067 -52.943 1.00 35.96 ? 115  MET A SD  1 
ATOM   860  C CE  . MET A 1 115 ? -102.720 48.463 -52.810 1.00 32.19 ? 115  MET A CE  1 
ATOM   861  N N   . LEU A 1 116 ? -99.081  48.520 -48.354 1.00 24.43 ? 116  LEU A N   1 
ATOM   862  C CA  . LEU A 1 116 ? -98.989  48.519 -46.899 1.00 25.71 ? 116  LEU A CA  1 
ATOM   863  C C   . LEU A 1 116 ? -97.535  48.675 -46.485 1.00 25.63 ? 116  LEU A C   1 
ATOM   864  O O   . LEU A 1 116 ? -97.199  49.483 -45.616 1.00 27.04 ? 116  LEU A O   1 
ATOM   865  C CB  . LEU A 1 116 ? -99.566  47.219 -46.329 1.00 23.91 ? 116  LEU A CB  1 
ATOM   866  C CG  . LEU A 1 116 ? -101.091 47.187 -46.195 1.00 24.37 ? 116  LEU A CG  1 
ATOM   867  C CD1 . LEU A 1 116 ? -101.595 45.754 -46.140 1.00 20.41 ? 116  LEU A CD1 1 
ATOM   868  C CD2 . LEU A 1 116 ? -101.502 47.988 -44.948 1.00 20.50 ? 116  LEU A CD2 1 
ATOM   869  N N   . SER A 1 117 ? -96.663  47.905 -47.117 1.00 25.33 ? 117  SER A N   1 
ATOM   870  C CA  . SER A 1 117 ? -95.254  47.996 -46.789 1.00 28.01 ? 117  SER A CA  1 
ATOM   871  C C   . SER A 1 117 ? -94.695  49.395 -47.067 1.00 27.51 ? 117  SER A C   1 
ATOM   872  O O   . SER A 1 117 ? -94.093  50.011 -46.185 1.00 28.65 ? 117  SER A O   1 
ATOM   873  C CB  . SER A 1 117 ? -94.476  46.937 -47.565 1.00 29.59 ? 117  SER A CB  1 
ATOM   874  O OG  . SER A 1 117 ? -94.965  45.645 -47.241 1.00 30.73 ? 117  SER A OG  1 
ATOM   875  N N   . VAL A 1 118 ? -94.906  49.913 -48.274 1.00 24.83 ? 118  VAL A N   1 
ATOM   876  C CA  . VAL A 1 118 ? -94.388  51.237 -48.584 1.00 24.15 ? 118  VAL A CA  1 
ATOM   877  C C   . VAL A 1 118 ? -95.060  52.312 -47.736 1.00 24.73 ? 118  VAL A C   1 
ATOM   878  O O   . VAL A 1 118 ? -94.485  53.361 -47.499 1.00 25.12 ? 118  VAL A O   1 
ATOM   879  C CB  . VAL A 1 118 ? -94.533  51.585 -50.097 1.00 25.37 ? 118  VAL A CB  1 
ATOM   880  C CG1 . VAL A 1 118 ? -95.920  52.157 -50.402 1.00 24.14 ? 118  VAL A CG1 1 
ATOM   881  C CG2 . VAL A 1 118 ? -93.455  52.572 -50.495 1.00 24.63 ? 118  VAL A CG2 1 
ATOM   882  N N   . ALA A 1 119 ? -96.281  52.064 -47.273 1.00 24.13 ? 119  ALA A N   1 
ATOM   883  C CA  . ALA A 1 119 ? -96.945  53.051 -46.437 1.00 23.23 ? 119  ALA A CA  1 
ATOM   884  C C   . ALA A 1 119 ? -96.144  53.184 -45.145 1.00 24.70 ? 119  ALA A C   1 
ATOM   885  O O   . ALA A 1 119 ? -96.162  54.223 -44.500 1.00 27.28 ? 119  ALA A O   1 
ATOM   886  C CB  . ALA A 1 119 ? -98.382  52.626 -46.137 1.00 23.53 ? 119  ALA A CB  1 
ATOM   887  N N   . GLY A 1 120 ? -95.446  52.118 -44.768 1.00 25.26 ? 120  GLY A N   1 
ATOM   888  C CA  . GLY A 1 120 ? -94.641  52.159 -43.565 1.00 24.18 ? 120  GLY A CA  1 
ATOM   889  C C   . GLY A 1 120 ? -94.968  51.109 -42.517 1.00 24.45 ? 120  GLY A C   1 
ATOM   890  O O   . GLY A 1 120 ? -94.474  51.191 -41.392 1.00 23.87 ? 120  GLY A O   1 
ATOM   891  N N   . ALA A 1 121 ? -95.782  50.120 -42.873 1.00 22.78 ? 121  ALA A N   1 
ATOM   892  C CA  . ALA A 1 121 ? -96.149  49.076 -41.925 1.00 24.00 ? 121  ALA A CA  1 
ATOM   893  C C   . ALA A 1 121 ? -94.949  48.194 -41.619 1.00 24.37 ? 121  ALA A C   1 
ATOM   894  O O   . ALA A 1 121 ? -94.240  47.778 -42.534 1.00 24.58 ? 121  ALA A O   1 
ATOM   895  C CB  . ALA A 1 121 ? -97.283  48.225 -42.495 1.00 24.91 ? 121  ALA A CB  1 
ATOM   896  N N   . ASP A 1 122 ? -94.734  47.904 -40.338 1.00 23.03 ? 122  ASP A N   1 
ATOM   897  C CA  . ASP A 1 122 ? -93.628  47.049 -39.905 1.00 22.74 ? 122  ASP A CA  1 
ATOM   898  C C   . ASP A 1 122 ? -94.060  45.642 -39.564 1.00 21.75 ? 122  ASP A C   1 
ATOM   899  O O   . ASP A 1 122 ? -93.220  44.756 -39.401 1.00 23.77 ? 122  ASP A O   1 
ATOM   900  C CB  . ASP A 1 122 ? -92.967  47.593 -38.637 1.00 22.62 ? 122  ASP A CB  1 
ATOM   901  C CG  . ASP A 1 122 ? -92.559  49.027 -38.757 1.00 26.44 ? 122  ASP A CG  1 
ATOM   902  O OD1 . ASP A 1 122 ? -93.246  49.876 -38.158 1.00 29.62 ? 122  ASP A OD1 1 
ATOM   903  O OD2 . ASP A 1 122 ? -91.557  49.309 -39.452 1.00 27.95 ? 122  ASP A OD2 1 
ATOM   904  N N   . HIS A 1 123 ? -95.362  45.439 -39.422 1.00 24.05 ? 123  HIS A N   1 
ATOM   905  C CA  . HIS A 1 123 ? -95.877  44.139 -39.013 1.00 27.17 ? 123  HIS A CA  1 
ATOM   906  C C   . HIS A 1 123 ? -97.360  44.068 -39.341 1.00 26.09 ? 123  HIS A C   1 
ATOM   907  O O   . HIS A 1 123 ? -98.052  45.085 -39.307 1.00 25.89 ? 123  HIS A O   1 
ATOM   908  C CB  . HIS A 1 123 ? -95.657  43.959 -37.489 1.00 31.82 ? 123  HIS A CB  1 
ATOM   909  C CG  . HIS A 1 123 ? -96.152  42.652 -36.937 1.00 34.87 ? 123  HIS A CG  1 
ATOM   910  N ND1 . HIS A 1 123 ? -96.149  41.485 -37.666 1.00 38.10 ? 123  HIS A ND1 1 
ATOM   911  C CD2 . HIS A 1 123 ? -96.611  42.323 -35.706 1.00 36.99 ? 123  HIS A CD2 1 
ATOM   912  C CE1 . HIS A 1 123 ? -96.583  40.492 -36.910 1.00 36.21 ? 123  HIS A CE1 1 
ATOM   913  N NE2 . HIS A 1 123 ? -96.869  40.973 -35.717 1.00 36.31 ? 123  HIS A NE2 1 
ATOM   914  N N   . ILE A 1 124 ? -97.827  42.863 -39.658 1.00 24.32 ? 124  ILE A N   1 
ATOM   915  C CA  . ILE A 1 124 ? -99.221  42.618 -39.991 1.00 23.40 ? 124  ILE A CA  1 
ATOM   916  C C   . ILE A 1 124 ? -99.860  41.562 -39.073 1.00 23.99 ? 124  ILE A C   1 
ATOM   917  O O   . ILE A 1 124 ? -99.245  40.541 -38.764 1.00 25.13 ? 124  ILE A O   1 
ATOM   918  C CB  . ILE A 1 124 ? -99.390  42.060 -41.451 1.00 23.59 ? 124  ILE A CB  1 
ATOM   919  C CG1 . ILE A 1 124 ? -98.673  42.938 -42.492 1.00 22.74 ? 124  ILE A CG1 1 
ATOM   920  C CG2 . ILE A 1 124 ? -100.876 41.945 -41.771 1.00 20.16 ? 124  ILE A CG2 1 
ATOM   921  C CD1 . ILE A 1 124 ? -99.257  44.326 -42.697 1.00 22.02 ? 124  ILE A CD1 1 
ATOM   922  N N   . ILE A 1 125 ? -101.098 41.815 -38.651 1.00 25.60 ? 125  ILE A N   1 
ATOM   923  C CA  . ILE A 1 125 ? -101.880 40.882 -37.837 1.00 23.71 ? 125  ILE A CA  1 
ATOM   924  C C   . ILE A 1 125 ? -103.214 40.774 -38.570 1.00 23.95 ? 125  ILE A C   1 
ATOM   925  O O   . ILE A 1 125 ? -103.917 41.765 -38.732 1.00 25.12 ? 125  ILE A O   1 
ATOM   926  C CB  . ILE A 1 125 ? -102.127 41.406 -36.397 1.00 24.80 ? 125  ILE A CB  1 
ATOM   927  C CG1 . ILE A 1 125 ? -100.808 41.438 -35.611 1.00 22.51 ? 125  ILE A CG1 1 
ATOM   928  C CG2 . ILE A 1 125 ? -103.143 40.501 -35.672 1.00 23.69 ? 125  ILE A CG2 1 
ATOM   929  C CD1 . ILE A 1 125 ? -100.929 42.150 -34.278 1.00 23.65 ? 125  ILE A CD1 1 
ATOM   930  N N   . THR A 1 126 ? -103.542 39.581 -39.051 1.00 26.49 ? 126  THR A N   1 
ATOM   931  C CA  . THR A 1 126 ? -104.789 39.361 -39.780 1.00 27.60 ? 126  THR A CA  1 
ATOM   932  C C   . THR A 1 126 ? -105.367 38.026 -39.322 1.00 28.23 ? 126  THR A C   1 
ATOM   933  O O   . THR A 1 126 ? -104.738 37.310 -38.536 1.00 27.49 ? 126  THR A O   1 
ATOM   934  C CB  . THR A 1 126 ? -104.531 39.302 -41.304 1.00 29.54 ? 126  THR A CB  1 
ATOM   935  O OG1 . THR A 1 126 ? -105.776 39.172 -42.010 1.00 32.54 ? 126  THR A OG1 1 
ATOM   936  C CG2 . THR A 1 126 ? -103.619 38.113 -41.632 1.00 26.14 ? 126  THR A CG2 1 
ATOM   937  N N   . MET A 1 127 ? -106.565 37.696 -39.794 1.00 27.51 ? 127  MET A N   1 
ATOM   938  C CA  . MET A 1 127 ? -107.185 36.428 -39.425 1.00 28.34 ? 127  MET A CA  1 
ATOM   939  C C   . MET A 1 127 ? -107.612 35.636 -40.654 1.00 27.58 ? 127  MET A C   1 
ATOM   940  O O   . MET A 1 127 ? -108.214 36.185 -41.580 1.00 28.12 ? 127  MET A O   1 
ATOM   941  C CB  . MET A 1 127 ? -108.397 36.660 -38.513 1.00 27.35 ? 127  MET A CB  1 
ATOM   942  C CG  . MET A 1 127 ? -109.146 35.378 -38.166 1.00 30.95 ? 127  MET A CG  1 
ATOM   943  S SD  . MET A 1 127 ? -110.222 35.532 -36.700 1.00 35.48 ? 127  MET A SD  1 
ATOM   944  C CE  . MET A 1 127 ? -108.979 35.818 -35.405 1.00 29.52 ? 127  MET A CE  1 
ATOM   945  N N   . ASP A 1 128 ? -107.284 34.348 -40.650 1.00 27.99 ? 128  ASP A N   1 
ATOM   946  C CA  . ASP A 1 128 ? -107.627 33.429 -41.731 1.00 28.37 ? 128  ASP A CA  1 
ATOM   947  C C   . ASP A 1 128 ? -107.436 33.992 -43.141 1.00 29.12 ? 128  ASP A C   1 
ATOM   948  O O   . ASP A 1 128 ? -108.406 34.272 -43.852 1.00 28.25 ? 128  ASP A O   1 
ATOM   949  C CB  . ASP A 1 128 ? -109.064 32.925 -41.546 1.00 30.41 ? 128  ASP A CB  1 
ATOM   950  C CG  . ASP A 1 128 ? -109.216 32.031 -40.309 1.00 33.86 ? 128  ASP A CG  1 
ATOM   951  O OD1 . ASP A 1 128 ? -110.179 32.224 -39.527 1.00 37.82 ? 128  ASP A OD1 1 
ATOM   952  O OD2 . ASP A 1 128 ? -108.371 31.130 -40.118 1.00 31.95 ? 128  ASP A OD2 1 
ATOM   953  N N   . LEU A 1 129 ? -106.172 34.161 -43.532 1.00 26.48 ? 129  LEU A N   1 
ATOM   954  C CA  . LEU A 1 129 ? -105.843 34.655 -44.861 1.00 25.04 ? 129  LEU A CA  1 
ATOM   955  C C   . LEU A 1 129 ? -106.481 33.718 -45.872 1.00 24.44 ? 129  LEU A C   1 
ATOM   956  O O   . LEU A 1 129 ? -106.462 32.499 -45.679 1.00 21.74 ? 129  LEU A O   1 
ATOM   957  C CB  . LEU A 1 129 ? -104.332 34.658 -45.057 1.00 24.49 ? 129  LEU A CB  1 
ATOM   958  C CG  . LEU A 1 129 ? -103.594 35.807 -44.384 1.00 25.86 ? 129  LEU A CG  1 
ATOM   959  C CD1 . LEU A 1 129 ? -102.096 35.548 -44.463 1.00 28.98 ? 129  LEU A CD1 1 
ATOM   960  C CD2 . LEU A 1 129 ? -103.967 37.125 -45.072 1.00 23.79 ? 129  LEU A CD2 1 
ATOM   961  N N   . HIS A 1 130 ? -107.045 34.272 -46.944 1.00 24.39 ? 130  HIS A N   1 
ATOM   962  C CA  . HIS A 1 130 ? -107.692 33.438 -47.952 1.00 24.43 ? 130  HIS A CA  1 
ATOM   963  C C   . HIS A 1 130 ? -106.767 32.325 -48.407 1.00 24.76 ? 130  HIS A C   1 
ATOM   964  O O   . HIS A 1 130 ? -107.211 31.214 -48.674 1.00 27.13 ? 130  HIS A O   1 
ATOM   965  C CB  . HIS A 1 130 ? -108.143 34.258 -49.157 1.00 26.08 ? 130  HIS A CB  1 
ATOM   966  C CG  . HIS A 1 130 ? -108.853 33.443 -50.195 1.00 27.56 ? 130  HIS A CG  1 
ATOM   967  N ND1 . HIS A 1 130 ? -108.309 33.169 -51.426 1.00 29.94 ? 130  HIS A ND1 1 
ATOM   968  C CD2 . HIS A 1 130 ? -110.053 32.814 -50.161 1.00 27.04 ? 130  HIS A CD2 1 
ATOM   969  C CE1 . HIS A 1 130 ? -109.143 32.405 -52.116 1.00 28.21 ? 130  HIS A CE1 1 
ATOM   970  N NE2 . HIS A 1 130 ? -110.206 32.178 -51.369 1.00 29.93 ? 130  HIS A NE2 1 
ATOM   971  N N   . ALA A 1 131 ? -105.478 32.633 -48.500 1.00 24.96 ? 131  ALA A N   1 
ATOM   972  C CA  . ALA A 1 131 ? -104.460 31.657 -48.875 1.00 23.83 ? 131  ALA A CA  1 
ATOM   973  C C   . ALA A 1 131 ? -103.239 31.958 -48.019 1.00 25.23 ? 131  ALA A C   1 
ATOM   974  O O   . ALA A 1 131 ? -102.770 33.097 -47.981 1.00 24.25 ? 131  ALA A O   1 
ATOM   975  C CB  . ALA A 1 131 ? -104.102 31.782 -50.350 1.00 23.90 ? 131  ALA A CB  1 
ATOM   976  N N   . ALA A 1 132 ? -102.731 30.935 -47.337 1.00 25.79 ? 132  ALA A N   1 
ATOM   977  C CA  . ALA A 1 132 ? -101.567 31.081 -46.474 1.00 27.74 ? 132  ALA A CA  1 
ATOM   978  C C   . ALA A 1 132 ? -100.363 31.656 -47.232 1.00 28.25 ? 132  ALA A C   1 
ATOM   979  O O   . ALA A 1 132 ? -99.490  32.316 -46.643 1.00 25.70 ? 132  ALA A O   1 
ATOM   980  C CB  . ALA A 1 132 ? -101.201 29.714 -45.859 1.00 27.24 ? 132  ALA A CB  1 
ATOM   981  N N   . GLN A 1 133 ? -100.312 31.410 -48.539 1.00 26.31 ? 133  GLN A N   1 
ATOM   982  C CA  . GLN A 1 133 ? -99.191  31.916 -49.326 1.00 25.60 ? 133  GLN A CA  1 
ATOM   983  C C   . GLN A 1 133 ? -99.082  33.443 -49.315 1.00 24.97 ? 133  GLN A C   1 
ATOM   984  O O   . GLN A 1 133 ? -98.009  33.994 -49.550 1.00 24.97 ? 133  GLN A O   1 
ATOM   985  C CB  . GLN A 1 133 ? -99.273  31.402 -50.766 1.00 23.73 ? 133  GLN A CB  1 
ATOM   986  C CG  . GLN A 1 133 ? -98.967  29.908 -50.908 1.00 23.08 ? 133  GLN A CG  1 
ATOM   987  C CD  . GLN A 1 133 ? -100.189 29.023 -50.741 1.00 24.76 ? 133  GLN A CD  1 
ATOM   988  O OE1 . GLN A 1 133 ? -101.189 29.422 -50.157 1.00 26.42 ? 133  GLN A OE1 1 
ATOM   989  N NE2 . GLN A 1 133 ? -100.105 27.808 -51.252 1.00 27.59 ? 133  GLN A NE2 1 
ATOM   990  N N   . ILE A 1 134 ? -100.188 34.122 -49.030 1.00 25.21 ? 134  ILE A N   1 
ATOM   991  C CA  . ILE A 1 134 ? -100.203 35.585 -49.004 1.00 25.86 ? 134  ILE A CA  1 
ATOM   992  C C   . ILE A 1 134 ? -99.205  36.141 -47.986 1.00 26.11 ? 134  ILE A C   1 
ATOM   993  O O   . ILE A 1 134 ? -98.720  37.265 -48.127 1.00 27.45 ? 134  ILE A O   1 
ATOM   994  C CB  . ILE A 1 134 ? -101.635 36.118 -48.710 1.00 24.23 ? 134  ILE A CB  1 
ATOM   995  C CG1 . ILE A 1 134 ? -102.527 35.836 -49.917 1.00 23.05 ? 134  ILE A CG1 1 
ATOM   996  C CG2 . ILE A 1 134 ? -101.601 37.612 -48.377 1.00 23.45 ? 134  ILE A CG2 1 
ATOM   997  C CD1 . ILE A 1 134 ? -103.978 36.256 -49.741 1.00 25.08 ? 134  ILE A CD1 1 
ATOM   998  N N   . GLN A 1 135 ? -98.891  35.354 -46.967 1.00 25.02 ? 135  GLN A N   1 
ATOM   999  C CA  . GLN A 1 135 ? -97.913  35.799 -45.989 1.00 25.47 ? 135  GLN A CA  1 
ATOM   1000 C C   . GLN A 1 135 ? -96.601  36.067 -46.718 1.00 25.98 ? 135  GLN A C   1 
ATOM   1001 O O   . GLN A 1 135 ? -95.819  36.934 -46.319 1.00 25.61 ? 135  GLN A O   1 
ATOM   1002 C CB  . GLN A 1 135 ? -97.692  34.734 -44.915 1.00 27.41 ? 135  GLN A CB  1 
ATOM   1003 C CG  . GLN A 1 135 ? -98.727  34.748 -43.798 1.00 29.06 ? 135  GLN A CG  1 
ATOM   1004 C CD  . GLN A 1 135 ? -98.200  34.108 -42.520 1.00 31.76 ? 135  GLN A CD  1 
ATOM   1005 O OE1 . GLN A 1 135 ? -97.133  34.469 -42.035 1.00 33.44 ? 135  GLN A OE1 1 
ATOM   1006 N NE2 . GLN A 1 135 ? -98.953  33.166 -41.968 1.00 32.24 ? 135  GLN A NE2 1 
ATOM   1007 N N   . GLY A 1 136 ? -96.371  35.319 -47.795 1.00 24.75 ? 136  GLY A N   1 
ATOM   1008 C CA  . GLY A 1 136 ? -95.151  35.484 -48.569 1.00 23.26 ? 136  GLY A CA  1 
ATOM   1009 C C   . GLY A 1 136 ? -95.154  36.681 -49.503 1.00 23.45 ? 136  GLY A C   1 
ATOM   1010 O O   . GLY A 1 136 ? -94.160  36.938 -50.186 1.00 22.43 ? 136  GLY A O   1 
ATOM   1011 N N   . PHE A 1 137 ? -96.273  37.403 -49.552 1.00 21.54 ? 137  PHE A N   1 
ATOM   1012 C CA  . PHE A 1 137 ? -96.379  38.591 -50.392 1.00 21.63 ? 137  PHE A CA  1 
ATOM   1013 C C   . PHE A 1 137 ? -95.715  39.771 -49.681 1.00 23.65 ? 137  PHE A C   1 
ATOM   1014 O O   . PHE A 1 137 ? -95.577  40.856 -50.251 1.00 22.59 ? 137  PHE A O   1 
ATOM   1015 C CB  . PHE A 1 137 ? -97.847  38.929 -50.680 1.00 21.64 ? 137  PHE A CB  1 
ATOM   1016 C CG  . PHE A 1 137 ? -98.523  37.984 -51.639 1.00 23.73 ? 137  PHE A CG  1 
ATOM   1017 C CD1 . PHE A 1 137 ? -99.859  38.160 -51.967 1.00 21.83 ? 137  PHE A CD1 1 
ATOM   1018 C CD2 . PHE A 1 137 ? -97.823  36.927 -52.221 1.00 23.28 ? 137  PHE A CD2 1 
ATOM   1019 C CE1 . PHE A 1 137 ? -100.496 37.310 -52.858 1.00 23.56 ? 137  PHE A CE1 1 
ATOM   1020 C CE2 . PHE A 1 137 ? -98.449  36.072 -53.111 1.00 26.40 ? 137  PHE A CE2 1 
ATOM   1021 C CZ  . PHE A 1 137 ? -99.795  36.264 -53.432 1.00 26.12 ? 137  PHE A CZ  1 
ATOM   1022 N N   . PHE A 1 138 ? -95.315  39.553 -48.430 1.00 22.39 ? 138  PHE A N   1 
ATOM   1023 C CA  . PHE A 1 138 ? -94.645  40.587 -47.643 1.00 24.40 ? 138  PHE A CA  1 
ATOM   1024 C C   . PHE A 1 138 ? -93.226  40.138 -47.369 1.00 25.84 ? 138  PHE A C   1 
ATOM   1025 O O   . PHE A 1 138 ? -92.891  38.960 -47.538 1.00 27.87 ? 138  PHE A O   1 
ATOM   1026 C CB  . PHE A 1 138 ? -95.291  40.777 -46.256 1.00 21.65 ? 138  PHE A CB  1 
ATOM   1027 C CG  . PHE A 1 138 ? -96.674  41.335 -46.285 1.00 22.56 ? 138  PHE A CG  1 
ATOM   1028 C CD1 . PHE A 1 138 ? -97.772  40.496 -46.409 1.00 23.22 ? 138  PHE A CD1 1 
ATOM   1029 C CD2 . PHE A 1 138 ? -96.885  42.704 -46.151 1.00 23.19 ? 138  PHE A CD2 1 
ATOM   1030 C CE1 . PHE A 1 138 ? -99.061  41.007 -46.402 1.00 24.08 ? 138  PHE A CE1 1 
ATOM   1031 C CE2 . PHE A 1 138 ? -98.173  43.227 -46.142 1.00 24.85 ? 138  PHE A CE2 1 
ATOM   1032 C CZ  . PHE A 1 138 ? -99.265  42.381 -46.263 1.00 23.84 ? 138  PHE A CZ  1 
ATOM   1033 N N   . ASP A 1 139 ? -92.398  41.088 -46.948 1.00 26.41 ? 139  ASP A N   1 
ATOM   1034 C CA  . ASP A 1 139 ? -91.048  40.782 -46.527 1.00 28.99 ? 139  ASP A CA  1 
ATOM   1035 C C   . ASP A 1 139 ? -91.092  41.019 -45.007 1.00 30.79 ? 139  ASP A C   1 
ATOM   1036 O O   . ASP A 1 139 ? -90.291  40.465 -44.254 1.00 34.85 ? 139  ASP A O   1 
ATOM   1037 C CB  . ASP A 1 139 ? -90.009  41.678 -47.215 1.00 31.16 ? 139  ASP A CB  1 
ATOM   1038 C CG  . ASP A 1 139 ? -89.694  41.225 -48.655 1.00 32.72 ? 139  ASP A CG  1 
ATOM   1039 O OD1 . ASP A 1 139 ? -89.741  40.012 -48.948 1.00 29.25 ? 139  ASP A OD1 1 
ATOM   1040 O OD2 . ASP A 1 139 ? -89.376  42.088 -49.496 1.00 37.82 ? 139  ASP A OD2 1 
ATOM   1041 N N   . ILE A 1 140 ? -92.056  41.823 -44.558 1.00 28.82 ? 140  ILE A N   1 
ATOM   1042 C CA  . ILE A 1 140 ? -92.228  42.093 -43.125 1.00 27.39 ? 140  ILE A CA  1 
ATOM   1043 C C   . ILE A 1 140 ? -92.990  40.941 -42.476 1.00 26.15 ? 140  ILE A C   1 
ATOM   1044 O O   . ILE A 1 140 ? -93.724  40.214 -43.145 1.00 25.46 ? 140  ILE A O   1 
ATOM   1045 C CB  . ILE A 1 140 ? -93.035  43.389 -42.856 1.00 25.95 ? 140  ILE A CB  1 
ATOM   1046 C CG1 . ILE A 1 140 ? -94.360  43.353 -43.632 1.00 25.76 ? 140  ILE A CG1 1 
ATOM   1047 C CG2 . ILE A 1 140 ? -92.197  44.603 -43.203 1.00 28.35 ? 140  ILE A CG2 1 
ATOM   1048 C CD1 . ILE A 1 140 ? -95.259  44.571 -43.405 1.00 22.89 ? 140  ILE A CD1 1 
ATOM   1049 N N   . PRO A 1 141 ? -92.823  40.764 -41.159 1.00 25.54 ? 141  PRO A N   1 
ATOM   1050 C CA  . PRO A 1 141 ? -93.500  39.691 -40.423 1.00 24.42 ? 141  PRO A CA  1 
ATOM   1051 C C   . PRO A 1 141 ? -95.030  39.788 -40.442 1.00 23.78 ? 141  PRO A C   1 
ATOM   1052 O O   . PRO A 1 141 ? -95.598  40.847 -40.215 1.00 22.86 ? 141  PRO A O   1 
ATOM   1053 C CB  . PRO A 1 141 ? -92.960  39.846 -38.997 1.00 24.56 ? 141  PRO A CB  1 
ATOM   1054 C CG  . PRO A 1 141 ? -91.648  40.526 -39.181 1.00 27.58 ? 141  PRO A CG  1 
ATOM   1055 C CD  . PRO A 1 141 ? -91.924  41.520 -40.275 1.00 23.57 ? 141  PRO A CD  1 
ATOM   1056 N N   . VAL A 1 142 ? -95.682  38.662 -40.707 1.00 25.84 ? 142  VAL A N   1 
ATOM   1057 C CA  . VAL A 1 142 ? -97.136  38.582 -40.706 1.00 24.24 ? 142  VAL A CA  1 
ATOM   1058 C C   . VAL A 1 142 ? -97.557  37.484 -39.722 1.00 25.59 ? 142  VAL A C   1 
ATOM   1059 O O   . VAL A 1 142 ? -96.945  36.419 -39.666 1.00 25.69 ? 142  VAL A O   1 
ATOM   1060 C CB  . VAL A 1 142 ? -97.698  38.204 -42.096 1.00 25.81 ? 142  VAL A CB  1 
ATOM   1061 C CG1 . VAL A 1 142 ? -99.212  38.164 -42.039 1.00 23.64 ? 142  VAL A CG1 1 
ATOM   1062 C CG2 . VAL A 1 142 ? -97.220  39.190 -43.154 1.00 24.59 ? 142  VAL A CG2 1 
ATOM   1063 N N   . ASP A 1 143 ? -98.576  37.762 -38.919 1.00 26.22 ? 143  ASP A N   1 
ATOM   1064 C CA  . ASP A 1 143 ? -99.105  36.774 -37.992 1.00 25.87 ? 143  ASP A CA  1 
ATOM   1065 C C   . ASP A 1 143 ? -100.541 36.525 -38.420 1.00 25.45 ? 143  ASP A C   1 
ATOM   1066 O O   . ASP A 1 143 ? -101.390 37.413 -38.336 1.00 25.83 ? 143  ASP A O   1 
ATOM   1067 C CB  . ASP A 1 143 ? -99.038  37.273 -36.549 1.00 27.61 ? 143  ASP A CB  1 
ATOM   1068 C CG  . ASP A 1 143 ? -97.621  37.245 -35.996 1.00 30.15 ? 143  ASP A CG  1 
ATOM   1069 O OD1 . ASP A 1 143 ? -96.929  36.227 -36.213 1.00 30.82 ? 143  ASP A OD1 1 
ATOM   1070 O OD2 . ASP A 1 143 ? -97.198  38.225 -35.348 1.00 28.26 ? 143  ASP A OD2 1 
ATOM   1071 N N   . ASN A 1 144 ? -100.788 35.315 -38.909 1.00 27.21 ? 144  ASN A N   1 
ATOM   1072 C CA  . ASN A 1 144 ? -102.096 34.897 -39.404 1.00 28.58 ? 144  ASN A CA  1 
ATOM   1073 C C   . ASN A 1 144 ? -102.811 34.049 -38.344 1.00 30.44 ? 144  ASN A C   1 
ATOM   1074 O O   . ASN A 1 144 ? -102.460 32.887 -38.115 1.00 31.93 ? 144  ASN A O   1 
ATOM   1075 C CB  . ASN A 1 144 ? -101.890 34.116 -40.714 1.00 27.24 ? 144  ASN A CB  1 
ATOM   1076 C CG  . ASN A 1 144 ? -103.194 33.661 -41.363 1.00 28.27 ? 144  ASN A CG  1 
ATOM   1077 O OD1 . ASN A 1 144 ? -104.211 34.360 -41.338 1.00 27.09 ? 144  ASN A OD1 1 
ATOM   1078 N ND2 . ASN A 1 144 ? -103.154 32.488 -41.977 1.00 28.36 ? 144  ASN A ND2 1 
ATOM   1079 N N   . LEU A 1 145 ? -103.801 34.656 -37.692 1.00 31.64 ? 145  LEU A N   1 
ATOM   1080 C CA  . LEU A 1 145 ? -104.582 33.999 -36.645 1.00 31.67 ? 145  LEU A CA  1 
ATOM   1081 C C   . LEU A 1 145 ? -105.663 33.121 -37.255 1.00 32.68 ? 145  LEU A C   1 
ATOM   1082 O O   . LEU A 1 145 ? -106.030 33.299 -38.414 1.00 33.68 ? 145  LEU A O   1 
ATOM   1083 C CB  . LEU A 1 145 ? -105.228 35.047 -35.740 1.00 30.16 ? 145  LEU A CB  1 
ATOM   1084 C CG  . LEU A 1 145 ? -104.273 36.011 -35.031 1.00 31.32 ? 145  LEU A CG  1 
ATOM   1085 C CD1 . LEU A 1 145 ? -105.047 37.215 -34.504 1.00 29.32 ? 145  LEU A CD1 1 
ATOM   1086 C CD2 . LEU A 1 145 ? -103.554 35.289 -33.913 1.00 30.04 ? 145  LEU A CD2 1 
ATOM   1087 N N   . TYR A 1 146 ? -106.178 32.180 -36.464 1.00 33.53 ? 146  TYR A N   1 
ATOM   1088 C CA  . TYR A 1 146 ? -107.208 31.258 -36.937 1.00 33.14 ? 146  TYR A CA  1 
ATOM   1089 C C   . TYR A 1 146 ? -108.462 31.288 -36.089 1.00 32.78 ? 146  TYR A C   1 
ATOM   1090 O O   . TYR A 1 146 ? -108.400 31.411 -34.871 1.00 31.49 ? 146  TYR A O   1 
ATOM   1091 C CB  . TYR A 1 146 ? -106.667 29.831 -36.954 1.00 34.08 ? 146  TYR A CB  1 
ATOM   1092 C CG  . TYR A 1 146 ? -105.331 29.716 -37.627 1.00 36.43 ? 146  TYR A CG  1 
ATOM   1093 C CD1 . TYR A 1 146 ? -104.160 29.663 -36.881 1.00 36.55 ? 146  TYR A CD1 1 
ATOM   1094 C CD2 . TYR A 1 146 ? -105.231 29.718 -39.019 1.00 38.53 ? 146  TYR A CD2 1 
ATOM   1095 C CE1 . TYR A 1 146 ? -102.918 29.620 -37.499 1.00 40.04 ? 146  TYR A CE1 1 
ATOM   1096 C CE2 . TYR A 1 146 ? -103.989 29.675 -39.651 1.00 38.66 ? 146  TYR A CE2 1 
ATOM   1097 C CZ  . TYR A 1 146 ? -102.839 29.628 -38.885 1.00 40.38 ? 146  TYR A CZ  1 
ATOM   1098 O OH  . TYR A 1 146 ? -101.606 29.595 -39.493 1.00 42.25 ? 146  TYR A OH  1 
ATOM   1099 N N   . ALA A 1 147 ? -109.608 31.161 -36.741 1.00 33.91 ? 147  ALA A N   1 
ATOM   1100 C CA  . ALA A 1 147 ? -110.871 31.155 -36.025 1.00 34.61 ? 147  ALA A CA  1 
ATOM   1101 C C   . ALA A 1 147 ? -111.256 29.704 -35.750 1.00 34.58 ? 147  ALA A C   1 
ATOM   1102 O O   . ALA A 1 147 ? -112.182 29.435 -34.988 1.00 33.26 ? 147  ALA A O   1 
ATOM   1103 C CB  . ALA A 1 147 ? -111.949 31.842 -36.860 1.00 34.05 ? 147  ALA A CB  1 
ATOM   1104 N N   . GLU A 1 148 ? -110.518 28.784 -36.368 1.00 36.09 ? 148  GLU A N   1 
ATOM   1105 C CA  . GLU A 1 148 ? -110.765 27.349 -36.245 1.00 38.31 ? 148  GLU A CA  1 
ATOM   1106 C C   . GLU A 1 148 ? -111.068 26.860 -34.825 1.00 37.80 ? 148  GLU A C   1 
ATOM   1107 O O   . GLU A 1 148 ? -112.100 26.238 -34.588 1.00 37.16 ? 148  GLU A O   1 
ATOM   1108 C CB  . GLU A 1 148 ? -109.584 26.557 -36.810 1.00 41.05 ? 148  GLU A CB  1 
ATOM   1109 C CG  . GLU A 1 148 ? -109.894 25.076 -37.008 1.00 47.13 ? 148  GLU A CG  1 
ATOM   1110 C CD  . GLU A 1 148 ? -108.667 24.248 -37.367 1.00 50.51 ? 148  GLU A CD  1 
ATOM   1111 O OE1 . GLU A 1 148 ? -108.020 24.533 -38.394 1.00 54.26 ? 148  GLU A OE1 1 
ATOM   1112 O OE2 . GLU A 1 148 ? -108.352 23.303 -36.619 1.00 54.08 ? 148  GLU A OE2 1 
ATOM   1113 N N   . PRO A 1 149 ? -110.176 27.133 -33.861 1.00 37.72 ? 149  PRO A N   1 
ATOM   1114 C CA  . PRO A 1 149 ? -110.460 26.667 -32.501 1.00 37.94 ? 149  PRO A CA  1 
ATOM   1115 C C   . PRO A 1 149 ? -111.858 27.102 -32.057 1.00 38.33 ? 149  PRO A C   1 
ATOM   1116 O O   . PRO A 1 149 ? -112.652 26.291 -31.574 1.00 38.67 ? 149  PRO A O   1 
ATOM   1117 C CB  . PRO A 1 149 ? -109.348 27.314 -31.680 1.00 38.58 ? 149  PRO A CB  1 
ATOM   1118 C CG  . PRO A 1 149 ? -108.211 27.419 -32.683 1.00 37.50 ? 149  PRO A CG  1 
ATOM   1119 C CD  . PRO A 1 149 ? -108.930 27.919 -33.899 1.00 37.19 ? 149  PRO A CD  1 
ATOM   1120 N N   . ALA A 1 150 ? -112.170 28.378 -32.252 1.00 37.01 ? 150  ALA A N   1 
ATOM   1121 C CA  . ALA A 1 150 ? -113.474 28.896 -31.866 1.00 36.93 ? 150  ALA A CA  1 
ATOM   1122 C C   . ALA A 1 150 ? -114.611 28.208 -32.625 1.00 36.48 ? 150  ALA A C   1 
ATOM   1123 O O   . ALA A 1 150 ? -115.657 27.917 -32.052 1.00 38.01 ? 150  ALA A O   1 
ATOM   1124 C CB  . ALA A 1 150 ? -113.520 30.398 -32.090 1.00 37.08 ? 150  ALA A CB  1 
ATOM   1125 N N   . VAL A 1 151 ? -114.397 27.946 -33.912 1.00 36.23 ? 151  VAL A N   1 
ATOM   1126 C CA  . VAL A 1 151 ? -115.399 27.287 -34.755 1.00 34.64 ? 151  VAL A CA  1 
ATOM   1127 C C   . VAL A 1 151 ? -115.680 25.858 -34.294 1.00 35.44 ? 151  VAL A C   1 
ATOM   1128 O O   . VAL A 1 151 ? -116.837 25.439 -34.211 1.00 34.62 ? 151  VAL A O   1 
ATOM   1129 C CB  . VAL A 1 151 ? -114.942 27.256 -36.238 1.00 33.27 ? 151  VAL A CB  1 
ATOM   1130 C CG1 . VAL A 1 151 ? -115.896 26.408 -37.084 1.00 29.41 ? 151  VAL A CG1 1 
ATOM   1131 C CG2 . VAL A 1 151 ? -114.886 28.670 -36.779 1.00 32.60 ? 151  VAL A CG2 1 
ATOM   1132 N N   . LEU A 1 152 ? -114.612 25.114 -34.016 1.00 34.81 ? 152  LEU A N   1 
ATOM   1133 C CA  . LEU A 1 152 ? -114.723 23.736 -33.554 1.00 36.15 ? 152  LEU A CA  1 
ATOM   1134 C C   . LEU A 1 152 ? -115.529 23.724 -32.269 1.00 38.36 ? 152  LEU A C   1 
ATOM   1135 O O   . LEU A 1 152 ? -116.489 22.964 -32.121 1.00 39.27 ? 152  LEU A O   1 
ATOM   1136 C CB  . LEU A 1 152 ? -113.332 23.159 -33.282 1.00 34.73 ? 152  LEU A CB  1 
ATOM   1137 C CG  . LEU A 1 152 ? -112.640 22.306 -34.352 1.00 36.62 ? 152  LEU A CG  1 
ATOM   1138 C CD1 . LEU A 1 152 ? -113.039 22.754 -35.743 1.00 35.86 ? 152  LEU A CD1 1 
ATOM   1139 C CD2 . LEU A 1 152 ? -111.127 22.394 -34.154 1.00 33.73 ? 152  LEU A CD2 1 
ATOM   1140 N N   . LYS A 1 153 ? -115.120 24.588 -31.348 1.00 40.41 ? 153  LYS A N   1 
ATOM   1141 C CA  . LYS A 1 153 ? -115.757 24.720 -30.052 1.00 40.61 ? 153  LYS A CA  1 
ATOM   1142 C C   . LYS A 1 153 ? -117.240 25.022 -30.230 1.00 40.25 ? 153  LYS A C   1 
ATOM   1143 O O   . LYS A 1 153 ? -118.083 24.405 -29.585 1.00 41.79 ? 153  LYS A O   1 
ATOM   1144 C CB  . LYS A 1 153 ? -115.062 25.834 -29.266 1.00 42.89 ? 153  LYS A CB  1 
ATOM   1145 C CG  . LYS A 1 153 ? -115.353 25.867 -27.778 1.00 47.63 ? 153  LYS A CG  1 
ATOM   1146 C CD  . LYS A 1 153 ? -114.469 26.905 -27.097 1.00 50.82 ? 153  LYS A CD  1 
ATOM   1147 C CE  . LYS A 1 153 ? -114.673 26.938 -25.586 1.00 53.48 ? 153  LYS A CE  1 
ATOM   1148 N NZ  . LYS A 1 153 ? -116.058 27.342 -25.206 1.00 56.71 ? 153  LYS A NZ  1 
ATOM   1149 N N   . TRP A 1 154 ? -117.557 25.956 -31.120 1.00 39.27 ? 154  TRP A N   1 
ATOM   1150 C CA  . TRP A 1 154 ? -118.943 26.324 -31.362 1.00 38.69 ? 154  TRP A CA  1 
ATOM   1151 C C   . TRP A 1 154 ? -119.727 25.137 -31.938 1.00 39.80 ? 154  TRP A C   1 
ATOM   1152 O O   . TRP A 1 154 ? -120.891 24.915 -31.588 1.00 38.17 ? 154  TRP A O   1 
ATOM   1153 C CB  . TRP A 1 154 ? -119.017 27.504 -32.334 1.00 37.17 ? 154  TRP A CB  1 
ATOM   1154 C CG  . TRP A 1 154 ? -120.394 28.063 -32.472 1.00 34.86 ? 154  TRP A CG  1 
ATOM   1155 C CD1 . TRP A 1 154 ? -120.894 29.166 -31.850 1.00 34.66 ? 154  TRP A CD1 1 
ATOM   1156 C CD2 . TRP A 1 154 ? -121.470 27.513 -33.241 1.00 35.44 ? 154  TRP A CD2 1 
ATOM   1157 N NE1 . TRP A 1 154 ? -122.214 29.348 -32.188 1.00 34.68 ? 154  TRP A NE1 1 
ATOM   1158 C CE2 . TRP A 1 154 ? -122.591 28.354 -33.054 1.00 36.11 ? 154  TRP A CE2 1 
ATOM   1159 C CE3 . TRP A 1 154 ? -121.588 26.411 -34.100 1.00 35.44 ? 154  TRP A CE3 1 
ATOM   1160 C CZ2 . TRP A 1 154 ? -123.830 28.103 -33.656 1.00 35.36 ? 154  TRP A CZ2 1 
ATOM   1161 C CZ3 . TRP A 1 154 ? -122.817 26.161 -34.703 1.00 35.97 ? 154  TRP A CZ3 1 
ATOM   1162 C CH2 . TRP A 1 154 ? -123.920 27.017 -34.489 1.00 35.94 ? 154  TRP A CH2 1 
ATOM   1163 N N   . ILE A 1 155 ? -119.087 24.382 -32.827 1.00 41.21 ? 155  ILE A N   1 
ATOM   1164 C CA  . ILE A 1 155 ? -119.726 23.224 -33.451 1.00 42.24 ? 155  ILE A CA  1 
ATOM   1165 C C   . ILE A 1 155 ? -120.100 22.171 -32.413 1.00 43.30 ? 155  ILE A C   1 
ATOM   1166 O O   . ILE A 1 155 ? -121.184 21.594 -32.465 1.00 43.30 ? 155  ILE A O   1 
ATOM   1167 C CB  . ILE A 1 155 ? -118.799 22.559 -34.505 1.00 42.10 ? 155  ILE A CB  1 
ATOM   1168 C CG1 . ILE A 1 155 ? -118.604 23.506 -35.700 1.00 40.99 ? 155  ILE A CG1 1 
ATOM   1169 C CG2 . ILE A 1 155 ? -119.399 21.220 -34.961 1.00 41.44 ? 155  ILE A CG2 1 
ATOM   1170 C CD1 . ILE A 1 155 ? -117.738 22.937 -36.822 1.00 36.64 ? 155  ILE A CD1 1 
ATOM   1171 N N   . ARG A 1 156 ? -119.197 21.927 -31.474 1.00 44.67 ? 156  ARG A N   1 
ATOM   1172 C CA  . ARG A 1 156 ? -119.431 20.939 -30.428 1.00 47.80 ? 156  ARG A CA  1 
ATOM   1173 C C   . ARG A 1 156 ? -120.542 21.337 -29.458 1.00 48.53 ? 156  ARG A C   1 
ATOM   1174 O O   . ARG A 1 156 ? -121.333 20.485 -29.038 1.00 49.52 ? 156  ARG A O   1 
ATOM   1175 C CB  . ARG A 1 156 ? -118.141 20.693 -29.631 1.00 48.01 ? 156  ARG A CB  1 
ATOM   1176 C CG  . ARG A 1 156 ? -117.022 20.025 -30.404 1.00 51.33 ? 156  ARG A CG  1 
ATOM   1177 C CD  . ARG A 1 156 ? -115.702 20.198 -29.660 1.00 54.75 ? 156  ARG A CD  1 
ATOM   1178 N NE  . ARG A 1 156 ? -114.574 19.843 -30.510 1.00 59.19 ? 156  ARG A NE  1 
ATOM   1179 C CZ  . ARG A 1 156 ? -113.316 20.200 -30.280 1.00 60.55 ? 156  ARG A CZ  1 
ATOM   1180 N NH1 . ARG A 1 156 ? -113.014 20.932 -29.216 1.00 62.40 ? 156  ARG A NH1 1 
ATOM   1181 N NH2 . ARG A 1 156 ? -112.361 19.828 -31.122 1.00 61.73 ? 156  ARG A NH2 1 
ATOM   1182 N N   . GLU A 1 157 ? -120.609 22.620 -29.107 1.00 48.46 ? 157  GLU A N   1 
ATOM   1183 C CA  . GLU A 1 157 ? -121.607 23.105 -28.149 1.00 48.69 ? 157  GLU A CA  1 
ATOM   1184 C C   . GLU A 1 157 ? -122.984 23.453 -28.703 1.00 48.29 ? 157  GLU A C   1 
ATOM   1185 O O   . GLU A 1 157 ? -123.954 23.547 -27.939 1.00 48.10 ? 157  GLU A O   1 
ATOM   1186 C CB  . GLU A 1 157 ? -121.052 24.323 -27.404 1.00 49.03 ? 157  GLU A CB  1 
ATOM   1187 C CG  . GLU A 1 157 ? -119.563 24.227 -27.119 1.00 51.21 ? 157  GLU A CG  1 
ATOM   1188 C CD  . GLU A 1 157 ? -119.059 25.319 -26.188 1.00 53.96 ? 157  GLU A CD  1 
ATOM   1189 O OE1 . GLU A 1 157 ? -119.565 26.466 -26.268 1.00 54.28 ? 157  GLU A OE1 1 
ATOM   1190 O OE2 . GLU A 1 157 ? -118.145 25.024 -25.383 1.00 54.15 ? 157  GLU A OE2 1 
ATOM   1191 N N   . ASN A 1 158 ? -123.088 23.636 -30.014 1.00 47.15 ? 158  ASN A N   1 
ATOM   1192 C CA  . ASN A 1 158 ? -124.371 23.998 -30.599 1.00 46.99 ? 158  ASN A CA  1 
ATOM   1193 C C   . ASN A 1 158 ? -124.978 22.973 -31.540 1.00 47.34 ? 158  ASN A C   1 
ATOM   1194 O O   . ASN A 1 158 ? -126.134 23.101 -31.949 1.00 46.48 ? 158  ASN A O   1 
ATOM   1195 C CB  . ASN A 1 158 ? -124.226 25.342 -31.302 1.00 47.40 ? 158  ASN A CB  1 
ATOM   1196 C CG  . ASN A 1 158 ? -123.792 26.439 -30.352 1.00 46.83 ? 158  ASN A CG  1 
ATOM   1197 O OD1 . ASN A 1 158 ? -124.617 27.159 -29.792 1.00 49.05 ? 158  ASN A OD1 1 
ATOM   1198 N ND2 . ASN A 1 158 ? -122.491 26.559 -30.151 1.00 46.26 ? 158  ASN A ND2 1 
ATOM   1199 N N   . ILE A 1 159 ? -124.206 21.955 -31.887 1.00 47.68 ? 159  ILE A N   1 
ATOM   1200 C CA  . ILE A 1 159 ? -124.716 20.921 -32.779 1.00 48.70 ? 159  ILE A CA  1 
ATOM   1201 C C   . ILE A 1 159 ? -124.671 19.564 -32.078 1.00 48.64 ? 159  ILE A C   1 
ATOM   1202 O O   . ILE A 1 159 ? -123.597 19.018 -31.829 1.00 46.39 ? 159  ILE A O   1 
ATOM   1203 C CB  . ILE A 1 159 ? -123.904 20.889 -34.088 1.00 50.39 ? 159  ILE A CB  1 
ATOM   1204 C CG1 . ILE A 1 159 ? -124.118 22.205 -34.851 1.00 52.02 ? 159  ILE A CG1 1 
ATOM   1205 C CG2 . ILE A 1 159 ? -124.333 19.718 -34.947 1.00 50.62 ? 159  ILE A CG2 1 
ATOM   1206 C CD1 . ILE A 1 159 ? -123.347 22.296 -36.151 1.00 50.89 ? 159  ILE A CD1 1 
ATOM   1207 N N   . SER A 1 160 ? -125.845 19.023 -31.767 1.00 49.62 ? 160  SER A N   1 
ATOM   1208 C CA  . SER A 1 160 ? -125.921 17.749 -31.064 1.00 52.69 ? 160  SER A CA  1 
ATOM   1209 C C   . SER A 1 160 ? -125.388 16.541 -31.831 1.00 53.05 ? 160  SER A C   1 
ATOM   1210 O O   . SER A 1 160 ? -124.658 15.717 -31.272 1.00 51.68 ? 160  SER A O   1 
ATOM   1211 C CB  . SER A 1 160 ? -127.358 17.488 -30.603 1.00 53.91 ? 160  SER A CB  1 
ATOM   1212 O OG  . SER A 1 160 ? -128.270 17.589 -31.677 1.00 57.86 ? 160  SER A OG  1 
ATOM   1213 N N   . GLU A 1 161 ? -125.733 16.444 -33.109 1.00 54.39 ? 161  GLU A N   1 
ATOM   1214 C CA  . GLU A 1 161 ? -125.286 15.321 -33.928 1.00 56.05 ? 161  GLU A CA  1 
ATOM   1215 C C   . GLU A 1 161 ? -123.910 15.562 -34.556 1.00 55.32 ? 161  GLU A C   1 
ATOM   1216 O O   . GLU A 1 161 ? -123.605 15.010 -35.609 1.00 54.95 ? 161  GLU A O   1 
ATOM   1217 C CB  . GLU A 1 161 ? -126.303 15.053 -35.045 1.00 56.85 ? 161  GLU A CB  1 
ATOM   1218 C CG  . GLU A 1 161 ? -127.769 15.093 -34.620 1.00 60.12 ? 161  GLU A CG  1 
ATOM   1219 C CD  . GLU A 1 161 ? -128.371 16.493 -34.696 1.00 63.06 ? 161  GLU A CD  1 
ATOM   1220 O OE1 . GLU A 1 161 ? -127.796 17.429 -34.097 1.00 63.15 ? 161  GLU A OE1 1 
ATOM   1221 O OE2 . GLU A 1 161 ? -129.425 16.657 -35.355 1.00 63.35 ? 161  GLU A OE2 1 
ATOM   1222 N N   . TRP A 1 162 ? -123.070 16.363 -33.910 1.00 54.80 ? 162  TRP A N   1 
ATOM   1223 C CA  . TRP A 1 162 ? -121.764 16.659 -34.482 1.00 55.32 ? 162  TRP A CA  1 
ATOM   1224 C C   . TRP A 1 162 ? -120.822 15.466 -34.587 1.00 56.63 ? 162  TRP A C   1 
ATOM   1225 O O   . TRP A 1 162 ? -119.969 15.426 -35.480 1.00 57.44 ? 162  TRP A O   1 
ATOM   1226 C CB  . TRP A 1 162 ? -121.077 17.796 -33.715 1.00 53.28 ? 162  TRP A CB  1 
ATOM   1227 C CG  . TRP A 1 162 ? -120.541 17.441 -32.366 1.00 51.58 ? 162  TRP A CG  1 
ATOM   1228 C CD1 . TRP A 1 162 ? -121.188 17.552 -31.168 1.00 50.59 ? 162  TRP A CD1 1 
ATOM   1229 C CD2 . TRP A 1 162 ? -119.220 16.976 -32.067 1.00 51.17 ? 162  TRP A CD2 1 
ATOM   1230 N NE1 . TRP A 1 162 ? -120.350 17.185 -30.140 1.00 48.62 ? 162  TRP A NE1 1 
ATOM   1231 C CE2 . TRP A 1 162 ? -119.142 16.814 -30.663 1.00 50.70 ? 162  TRP A CE2 1 
ATOM   1232 C CE3 . TRP A 1 162 ? -118.104 16.656 -32.850 1.00 51.51 ? 162  TRP A CE3 1 
ATOM   1233 C CZ2 . TRP A 1 162 ? -117.975 16.381 -30.023 1.00 51.06 ? 162  TRP A CZ2 1 
ATOM   1234 C CZ3 . TRP A 1 162 ? -116.943 16.223 -32.213 1.00 52.80 ? 162  TRP A CZ3 1 
ATOM   1235 C CH2 . TRP A 1 162 ? -116.894 16.077 -30.811 1.00 52.45 ? 162  TRP A CH2 1 
ATOM   1236 N N   . ARG A 1 163 ? -120.976 14.501 -33.684 1.00 55.66 ? 163  ARG A N   1 
ATOM   1237 C CA  . ARG A 1 163 ? -120.139 13.305 -33.685 1.00 54.91 ? 163  ARG A CA  1 
ATOM   1238 C C   . ARG A 1 163 ? -120.225 12.571 -35.017 1.00 53.88 ? 163  ARG A C   1 
ATOM   1239 O O   . ARG A 1 163 ? -119.287 11.881 -35.417 1.00 54.22 ? 163  ARG A O   1 
ATOM   1240 C CB  . ARG A 1 163 ? -120.568 12.356 -32.563 1.00 57.01 ? 163  ARG A CB  1 
ATOM   1241 C CG  . ARG A 1 163 ? -120.335 12.882 -31.153 1.00 57.68 ? 163  ARG A CG  1 
ATOM   1242 C CD  . ARG A 1 163 ? -118.902 12.658 -30.704 1.00 58.57 ? 163  ARG A CD  1 
ATOM   1243 N NE  . ARG A 1 163 ? -118.655 13.201 -29.369 1.00 59.57 ? 163  ARG A NE  1 
ATOM   1244 C CZ  . ARG A 1 163 ? -117.486 13.137 -28.740 1.00 57.94 ? 163  ARG A CZ  1 
ATOM   1245 N NH1 . ARG A 1 163 ? -116.450 12.550 -29.319 1.00 58.16 ? 163  ARG A NH1 1 
ATOM   1246 N NH2 . ARG A 1 163 ? -117.349 13.673 -27.538 1.00 57.94 ? 163  ARG A NH2 1 
ATOM   1247 N N   . ASN A 1 164 ? -121.350 12.721 -35.707 1.00 51.45 ? 164  ASN A N   1 
ATOM   1248 C CA  . ASN A 1 164 ? -121.535 12.045 -36.983 1.00 49.96 ? 164  ASN A CA  1 
ATOM   1249 C C   . ASN A 1 164 ? -121.992 12.993 -38.082 1.00 47.99 ? 164  ASN A C   1 
ATOM   1250 O O   . ASN A 1 164 ? -122.836 12.639 -38.900 1.00 48.03 ? 164  ASN A O   1 
ATOM   1251 C CB  . ASN A 1 164 ? -122.554 10.906 -36.833 1.00 54.36 ? 164  ASN A CB  1 
ATOM   1252 C CG  . ASN A 1 164 ? -122.179 9.923  -35.731 1.00 56.69 ? 164  ASN A CG  1 
ATOM   1253 O OD1 . ASN A 1 164 ? -121.108 9.308  -35.765 1.00 58.17 ? 164  ASN A OD1 1 
ATOM   1254 N ND2 . ASN A 1 164 ? -123.063 9.771  -34.747 1.00 58.13 ? 164  ASN A ND2 1 
ATOM   1255 N N   . CYS A 1 165 ? -121.431 14.197 -38.107 1.00 45.14 ? 165  CYS A N   1 
ATOM   1256 C CA  . CYS A 1 165 ? -121.800 15.171 -39.128 1.00 42.77 ? 165  CYS A CA  1 
ATOM   1257 C C   . CYS A 1 165 ? -120.761 15.170 -40.243 1.00 41.31 ? 165  CYS A C   1 
ATOM   1258 O O   . CYS A 1 165 ? -119.742 14.482 -40.161 1.00 40.36 ? 165  CYS A O   1 
ATOM   1259 C CB  . CYS A 1 165 ? -121.856 16.571 -38.526 1.00 44.07 ? 165  CYS A CB  1 
ATOM   1260 S SG  . CYS A 1 165 ? -120.219 17.212 -38.066 1.00 42.81 ? 165  CYS A SG  1 
ATOM   1261 N N   . THR A 1 166 ? -121.025 15.957 -41.278 1.00 39.40 ? 166  THR A N   1 
ATOM   1262 C CA  . THR A 1 166 ? -120.106 16.073 -42.396 1.00 39.93 ? 166  THR A CA  1 
ATOM   1263 C C   . THR A 1 166 ? -119.739 17.531 -42.640 1.00 38.54 ? 166  THR A C   1 
ATOM   1264 O O   . THR A 1 166 ? -120.615 18.395 -42.712 1.00 38.28 ? 166  THR A O   1 
ATOM   1265 C CB  . THR A 1 166 ? -120.710 15.507 -43.706 1.00 39.37 ? 166  THR A CB  1 
ATOM   1266 O OG1 . THR A 1 166 ? -120.982 14.112 -43.542 1.00 40.14 ? 166  THR A OG1 1 
ATOM   1267 C CG2 . THR A 1 166 ? -119.730 15.687 -44.866 1.00 39.97 ? 166  THR A CG2 1 
ATOM   1268 N N   . ILE A 1 167 ? -118.441 17.800 -42.755 1.00 37.05 ? 167  ILE A N   1 
ATOM   1269 C CA  . ILE A 1 167 ? -117.964 19.151 -43.034 1.00 36.30 ? 167  ILE A CA  1 
ATOM   1270 C C   . ILE A 1 167 ? -117.955 19.277 -44.560 1.00 35.05 ? 167  ILE A C   1 
ATOM   1271 O O   . ILE A 1 167 ? -117.242 18.541 -45.235 1.00 36.05 ? 167  ILE A O   1 
ATOM   1272 C CB  . ILE A 1 167 ? -116.541 19.358 -42.505 1.00 36.04 ? 167  ILE A CB  1 
ATOM   1273 C CG1 . ILE A 1 167 ? -116.451 18.862 -41.058 1.00 38.30 ? 167  ILE A CG1 1 
ATOM   1274 C CG2 . ILE A 1 167 ? -116.166 20.827 -42.593 1.00 33.35 ? 167  ILE A CG2 1 
ATOM   1275 C CD1 . ILE A 1 167 ? -117.444 19.524 -40.108 1.00 37.93 ? 167  ILE A CD1 1 
ATOM   1276 N N   . VAL A 1 168 ? -118.742 20.204 -45.095 1.00 34.09 ? 168  VAL A N   1 
ATOM   1277 C CA  . VAL A 1 168 ? -118.839 20.380 -46.538 1.00 34.88 ? 168  VAL A CA  1 
ATOM   1278 C C   . VAL A 1 168 ? -118.207 21.667 -47.073 1.00 35.14 ? 168  VAL A C   1 
ATOM   1279 O O   . VAL A 1 168 ? -118.394 22.744 -46.508 1.00 34.95 ? 168  VAL A O   1 
ATOM   1280 C CB  . VAL A 1 168 ? -120.325 20.363 -46.994 1.00 35.22 ? 168  VAL A CB  1 
ATOM   1281 C CG1 . VAL A 1 168 ? -120.408 20.410 -48.508 1.00 34.35 ? 168  VAL A CG1 1 
ATOM   1282 C CG2 . VAL A 1 168 ? -121.031 19.121 -46.450 1.00 35.88 ? 168  VAL A CG2 1 
ATOM   1283 N N   . SER A 1 169 ? -117.467 21.547 -48.174 1.00 33.65 ? 169  SER A N   1 
ATOM   1284 C CA  . SER A 1 169 ? -116.843 22.699 -48.812 1.00 33.36 ? 169  SER A CA  1 
ATOM   1285 C C   . SER A 1 169 ? -117.701 23.127 -50.003 1.00 34.35 ? 169  SER A C   1 
ATOM   1286 O O   . SER A 1 169 ? -118.072 22.294 -50.838 1.00 34.51 ? 169  SER A O   1 
ATOM   1287 C CB  . SER A 1 169 ? -115.430 22.343 -49.307 1.00 34.81 ? 169  SER A CB  1 
ATOM   1288 O OG  . SER A 1 169 ? -114.866 23.420 -50.023 1.00 30.36 ? 169  SER A OG  1 
ATOM   1289 N N   . PRO A 1 170 ? -118.032 24.429 -50.091 1.00 33.11 ? 170  PRO A N   1 
ATOM   1290 C CA  . PRO A 1 170 ? -118.856 25.011 -51.159 1.00 33.02 ? 170  PRO A CA  1 
ATOM   1291 C C   . PRO A 1 170 ? -118.255 24.827 -52.555 1.00 34.11 ? 170  PRO A C   1 
ATOM   1292 O O   . PRO A 1 170 ? -118.974 24.794 -53.552 1.00 34.12 ? 170  PRO A O   1 
ATOM   1293 C CB  . PRO A 1 170 ? -118.940 26.486 -50.770 1.00 33.75 ? 170  PRO A CB  1 
ATOM   1294 C CG  . PRO A 1 170 ? -118.768 26.455 -49.285 1.00 34.33 ? 170  PRO A CG  1 
ATOM   1295 C CD  . PRO A 1 170 ? -117.660 25.462 -49.108 1.00 31.49 ? 170  PRO A CD  1 
ATOM   1296 N N   . ASP A 1 171 ? -116.935 24.718 -52.617 1.00 34.85 ? 171  ASP A N   1 
ATOM   1297 C CA  . ASP A 1 171 ? -116.243 24.542 -53.892 1.00 34.74 ? 171  ASP A CA  1 
ATOM   1298 C C   . ASP A 1 171 ? -115.007 23.662 -53.745 1.00 36.23 ? 171  ASP A C   1 
ATOM   1299 O O   . ASP A 1 171 ? -114.670 23.220 -52.632 1.00 34.37 ? 171  ASP A O   1 
ATOM   1300 C CB  . ASP A 1 171 ? -115.855 25.906 -54.445 1.00 34.05 ? 171  ASP A CB  1 
ATOM   1301 C CG  . ASP A 1 171 ? -115.217 26.793 -53.390 1.00 34.18 ? 171  ASP A CG  1 
ATOM   1302 O OD1 . ASP A 1 171 ? -115.584 27.979 -53.320 1.00 36.06 ? 171  ASP A OD1 1 
ATOM   1303 O OD2 . ASP A 1 171 ? -114.354 26.305 -52.636 1.00 31.37 ? 171  ASP A OD2 1 
ATOM   1304 N N   . ALA A 1 172 ? -114.348 23.405 -54.870 1.00 37.19 ? 172  ALA A N   1 
ATOM   1305 C CA  . ALA A 1 172 ? -113.155 22.565 -54.892 1.00 38.21 ? 172  ALA A CA  1 
ATOM   1306 C C   . ALA A 1 172 ? -112.002 23.231 -54.140 1.00 37.60 ? 172  ALA A C   1 
ATOM   1307 O O   . ALA A 1 172 ? -111.192 22.573 -53.490 1.00 38.47 ? 172  ALA A O   1 
ATOM   1308 C CB  . ALA A 1 172 ? -112.745 22.287 -56.357 1.00 38.94 ? 172  ALA A CB  1 
ATOM   1309 N N   . GLY A 1 173 ? -111.954 24.552 -54.217 1.00 38.18 ? 173  GLY A N   1 
ATOM   1310 C CA  . GLY A 1 173 ? -110.905 25.295 -53.550 1.00 38.32 ? 173  GLY A CA  1 
ATOM   1311 C C   . GLY A 1 173 ? -110.881 25.278 -52.033 1.00 38.95 ? 173  GLY A C   1 
ATOM   1312 O O   . GLY A 1 173 ? -109.890 25.702 -51.441 1.00 39.09 ? 173  GLY A O   1 
ATOM   1313 N N   . GLY A 1 174 ? -111.955 24.825 -51.387 1.00 39.20 ? 174  GLY A N   1 
ATOM   1314 C CA  . GLY A 1 174 ? -111.967 24.809 -49.930 1.00 36.31 ? 174  GLY A CA  1 
ATOM   1315 C C   . GLY A 1 174 ? -111.673 23.449 -49.323 1.00 36.09 ? 174  GLY A C   1 
ATOM   1316 O O   . GLY A 1 174 ? -111.875 23.240 -48.126 1.00 36.86 ? 174  GLY A O   1 
ATOM   1317 N N   . ALA A 1 175 ? -111.203 22.521 -50.146 1.00 35.18 ? 175  ALA A N   1 
ATOM   1318 C CA  . ALA A 1 175 ? -110.922 21.172 -49.681 1.00 37.27 ? 175  ALA A CA  1 
ATOM   1319 C C   . ALA A 1 175 ? -110.084 21.115 -48.406 1.00 37.95 ? 175  ALA A C   1 
ATOM   1320 O O   . ALA A 1 175 ? -110.525 20.573 -47.393 1.00 37.25 ? 175  ALA A O   1 
ATOM   1321 C CB  . ALA A 1 175 ? -110.244 20.374 -50.786 1.00 37.93 ? 175  ALA A CB  1 
ATOM   1322 N N   . LYS A 1 176 ? -108.873 21.662 -48.464 1.00 38.97 ? 176  LYS A N   1 
ATOM   1323 C CA  . LYS A 1 176 ? -107.959 21.651 -47.325 1.00 38.14 ? 176  LYS A CA  1 
ATOM   1324 C C   . LYS A 1 176 ? -108.587 22.221 -46.064 1.00 38.42 ? 176  LYS A C   1 
ATOM   1325 O O   . LYS A 1 176 ? -108.377 21.709 -44.968 1.00 36.46 ? 176  LYS A O   1 
ATOM   1326 C CB  . LYS A 1 176 ? -106.697 22.436 -47.675 1.00 39.84 ? 176  LYS A CB  1 
ATOM   1327 C CG  . LYS A 1 176 ? -105.421 21.634 -47.526 1.00 44.15 ? 176  LYS A CG  1 
ATOM   1328 C CD  . LYS A 1 176 ? -104.249 22.287 -48.252 1.00 48.28 ? 176  LYS A CD  1 
ATOM   1329 C CE  . LYS A 1 176 ? -103.021 21.379 -48.242 1.00 49.16 ? 176  LYS A CE  1 
ATOM   1330 N NZ  . LYS A 1 176 ? -103.328 20.040 -48.842 1.00 50.36 ? 176  LYS A NZ  1 
ATOM   1331 N N   . ARG A 1 177 ? -109.353 23.290 -46.222 1.00 37.54 ? 177  ARG A N   1 
ATOM   1332 C CA  . ARG A 1 177 ? -109.996 23.927 -45.089 1.00 38.81 ? 177  ARG A CA  1 
ATOM   1333 C C   . ARG A 1 177 ? -110.979 22.988 -44.382 1.00 37.90 ? 177  ARG A C   1 
ATOM   1334 O O   . ARG A 1 177 ? -110.971 22.881 -43.155 1.00 38.41 ? 177  ARG A O   1 
ATOM   1335 C CB  . ARG A 1 177 ? -110.716 25.199 -45.552 1.00 42.24 ? 177  ARG A CB  1 
ATOM   1336 C CG  . ARG A 1 177 ? -111.090 26.146 -44.425 1.00 45.52 ? 177  ARG A CG  1 
ATOM   1337 C CD  . ARG A 1 177 ? -111.840 27.378 -44.925 1.00 48.20 ? 177  ARG A CD  1 
ATOM   1338 N NE  . ARG A 1 177 ? -111.003 28.272 -45.726 1.00 51.32 ? 177  ARG A NE  1 
ATOM   1339 C CZ  . ARG A 1 177 ? -110.909 28.243 -47.054 1.00 51.41 ? 177  ARG A CZ  1 
ATOM   1340 N NH1 . ARG A 1 177 ? -111.605 27.359 -47.760 1.00 50.42 ? 177  ARG A NH1 1 
ATOM   1341 N NH2 . ARG A 1 177 ? -110.119 29.108 -47.681 1.00 49.95 ? 177  ARG A NH2 1 
ATOM   1342 N N   . VAL A 1 178 ? -111.809 22.288 -45.149 1.00 36.66 ? 178  VAL A N   1 
ATOM   1343 C CA  . VAL A 1 178 ? -112.789 21.395 -44.543 1.00 35.11 ? 178  VAL A CA  1 
ATOM   1344 C C   . VAL A 1 178 ? -112.227 20.059 -44.071 1.00 34.98 ? 178  VAL A C   1 
ATOM   1345 O O   . VAL A 1 178 ? -112.705 19.512 -43.079 1.00 34.27 ? 178  VAL A O   1 
ATOM   1346 C CB  . VAL A 1 178 ? -113.993 21.147 -45.485 1.00 36.56 ? 178  VAL A CB  1 
ATOM   1347 C CG1 . VAL A 1 178 ? -114.630 22.474 -45.851 1.00 33.86 ? 178  VAL A CG1 1 
ATOM   1348 C CG2 . VAL A 1 178 ? -113.559 20.389 -46.730 1.00 37.23 ? 178  VAL A CG2 1 
ATOM   1349 N N   . THR A 1 179 ? -111.217 19.532 -44.759 1.00 32.79 ? 179  THR A N   1 
ATOM   1350 C CA  . THR A 1 179 ? -110.630 18.260 -44.336 1.00 32.96 ? 179  THR A CA  1 
ATOM   1351 C C   . THR A 1 179 ? -109.893 18.437 -43.018 1.00 32.74 ? 179  THR A C   1 
ATOM   1352 O O   . THR A 1 179 ? -109.838 17.524 -42.200 1.00 32.87 ? 179  THR A O   1 
ATOM   1353 C CB  . THR A 1 179 ? -109.644 17.689 -45.378 1.00 32.28 ? 179  THR A CB  1 
ATOM   1354 O OG1 . THR A 1 179 ? -108.668 18.679 -45.715 1.00 35.45 ? 179  THR A OG1 1 
ATOM   1355 C CG2 . THR A 1 179 ? -110.388 17.248 -46.625 1.00 32.73 ? 179  THR A CG2 1 
ATOM   1356 N N   . SER A 1 180 ? -109.315 19.616 -42.828 1.00 33.40 ? 180  SER A N   1 
ATOM   1357 C CA  . SER A 1 180 ? -108.601 19.929 -41.602 1.00 34.55 ? 180  SER A CA  1 
ATOM   1358 C C   . SER A 1 180 ? -109.584 19.960 -40.435 1.00 35.49 ? 180  SER A C   1 
ATOM   1359 O O   . SER A 1 180 ? -109.326 19.387 -39.379 1.00 36.24 ? 180  SER A O   1 
ATOM   1360 C CB  . SER A 1 180 ? -107.909 21.283 -41.732 1.00 34.82 ? 180  SER A CB  1 
ATOM   1361 O OG  . SER A 1 180 ? -107.558 21.784 -40.461 1.00 40.82 ? 180  SER A OG  1 
ATOM   1362 N N   . ILE A 1 181 ? -110.714 20.632 -40.629 1.00 36.32 ? 181  ILE A N   1 
ATOM   1363 C CA  . ILE A 1 181 ? -111.731 20.711 -39.588 1.00 38.04 ? 181  ILE A CA  1 
ATOM   1364 C C   . ILE A 1 181 ? -112.389 19.350 -39.377 1.00 38.95 ? 181  ILE A C   1 
ATOM   1365 O O   . ILE A 1 181 ? -112.723 18.977 -38.251 1.00 39.86 ? 181  ILE A O   1 
ATOM   1366 C CB  . ILE A 1 181 ? -112.814 21.755 -39.950 1.00 38.75 ? 181  ILE A CB  1 
ATOM   1367 C CG1 . ILE A 1 181 ? -112.226 23.163 -39.817 1.00 39.54 ? 181  ILE A CG1 1 
ATOM   1368 C CG2 . ILE A 1 181 ? -114.034 21.595 -39.051 1.00 39.62 ? 181  ILE A CG2 1 
ATOM   1369 C CD1 . ILE A 1 181 ? -113.169 24.261 -40.231 1.00 38.15 ? 181  ILE A CD1 1 
ATOM   1370 N N   . ALA A 1 182 ? -112.568 18.608 -40.464 1.00 38.81 ? 182  ALA A N   1 
ATOM   1371 C CA  . ALA A 1 182 ? -113.185 17.294 -40.390 1.00 38.38 ? 182  ALA A CA  1 
ATOM   1372 C C   . ALA A 1 182 ? -112.268 16.307 -39.673 1.00 39.13 ? 182  ALA A C   1 
ATOM   1373 O O   . ALA A 1 182 ? -112.739 15.398 -38.990 1.00 39.86 ? 182  ALA A O   1 
ATOM   1374 C CB  . ALA A 1 182 ? -113.516 16.788 -41.791 1.00 37.71 ? 182  ALA A CB  1 
ATOM   1375 N N   . ASP A 1 183 ? -110.960 16.484 -39.831 1.00 38.11 ? 183  ASP A N   1 
ATOM   1376 C CA  . ASP A 1 183 ? -110.005 15.601 -39.179 1.00 39.73 ? 183  ASP A CA  1 
ATOM   1377 C C   . ASP A 1 183 ? -109.971 15.853 -37.667 1.00 40.99 ? 183  ASP A C   1 
ATOM   1378 O O   . ASP A 1 183 ? -109.881 14.909 -36.880 1.00 40.38 ? 183  ASP A O   1 
ATOM   1379 C CB  . ASP A 1 183 ? -108.606 15.795 -39.768 1.00 39.67 ? 183  ASP A CB  1 
ATOM   1380 C CG  . ASP A 1 183 ? -108.444 15.130 -41.117 1.00 40.83 ? 183  ASP A CG  1 
ATOM   1381 O OD1 . ASP A 1 183 ? -109.413 14.521 -41.610 1.00 43.16 ? 183  ASP A OD1 1 
ATOM   1382 O OD2 . ASP A 1 183 ? -107.341 15.213 -41.688 1.00 41.52 ? 183  ASP A OD2 1 
ATOM   1383 N N   . ARG A 1 184 ? -110.038 17.121 -37.269 1.00 41.49 ? 184  ARG A N   1 
ATOM   1384 C CA  . ARG A 1 184 ? -110.030 17.488 -35.854 1.00 43.06 ? 184  ARG A CA  1 
ATOM   1385 C C   . ARG A 1 184 ? -111.261 16.935 -35.131 1.00 42.99 ? 184  ARG A C   1 
ATOM   1386 O O   . ARG A 1 184 ? -111.171 16.484 -33.992 1.00 43.32 ? 184  ARG A O   1 
ATOM   1387 C CB  . ARG A 1 184 ? -110.004 19.014 -35.690 1.00 42.94 ? 184  ARG A CB  1 
ATOM   1388 C CG  . ARG A 1 184 ? -108.632 19.638 -35.521 1.00 47.41 ? 184  ARG A CG  1 
ATOM   1389 C CD  . ARG A 1 184 ? -107.774 19.494 -36.759 1.00 52.08 ? 184  ARG A CD  1 
ATOM   1390 N NE  . ARG A 1 184 ? -106.829 20.606 -36.896 1.00 56.42 ? 184  ARG A NE  1 
ATOM   1391 C CZ  . ARG A 1 184 ? -106.027 20.777 -37.944 1.00 56.94 ? 184  ARG A CZ  1 
ATOM   1392 N NH1 . ARG A 1 184 ? -106.055 19.900 -38.943 1.00 58.29 ? 184  ARG A NH1 1 
ATOM   1393 N NH2 . ARG A 1 184 ? -105.213 21.827 -38.002 1.00 53.86 ? 184  ARG A NH2 1 
ATOM   1394 N N   . LEU A 1 185 ? -112.409 16.977 -35.797 1.00 43.81 ? 185  LEU A N   1 
ATOM   1395 C CA  . LEU A 1 185 ? -113.651 16.490 -35.209 1.00 43.85 ? 185  LEU A CA  1 
ATOM   1396 C C   . LEU A 1 185 ? -113.823 14.989 -35.369 1.00 44.75 ? 185  LEU A C   1 
ATOM   1397 O O   . LEU A 1 185 ? -114.642 14.378 -34.683 1.00 45.86 ? 185  LEU A O   1 
ATOM   1398 C CB  . LEU A 1 185 ? -114.848 17.188 -35.851 1.00 41.52 ? 185  LEU A CB  1 
ATOM   1399 C CG  . LEU A 1 185 ? -114.954 18.685 -35.569 1.00 42.47 ? 185  LEU A CG  1 
ATOM   1400 C CD1 . LEU A 1 185 ? -116.184 19.245 -36.263 1.00 40.72 ? 185  LEU A CD1 1 
ATOM   1401 C CD2 . LEU A 1 185 ? -115.038 18.913 -34.055 1.00 42.11 ? 185  LEU A CD2 1 
ATOM   1402 N N   . ASN A 1 186 ? -113.048 14.402 -36.274 1.00 44.53 ? 186  ASN A N   1 
ATOM   1403 C CA  . ASN A 1 186 ? -113.126 12.975 -36.548 1.00 45.30 ? 186  ASN A CA  1 
ATOM   1404 C C   . ASN A 1 186 ? -114.420 12.606 -37.257 1.00 44.53 ? 186  ASN A C   1 
ATOM   1405 O O   . ASN A 1 186 ? -115.026 11.584 -36.943 1.00 44.83 ? 186  ASN A O   1 
ATOM   1406 C CB  . ASN A 1 186 ? -113.006 12.165 -35.254 1.00 47.61 ? 186  ASN A CB  1 
ATOM   1407 C CG  . ASN A 1 186 ? -111.637 11.551 -35.084 1.00 50.39 ? 186  ASN A CG  1 
ATOM   1408 O OD1 . ASN A 1 186 ? -111.196 10.741 -35.910 1.00 53.28 ? 186  ASN A OD1 1 
ATOM   1409 N ND2 . ASN A 1 186 ? -110.950 11.929 -34.012 1.00 51.70 ? 186  ASN A ND2 1 
ATOM   1410 N N   . VAL A 1 187 ? -114.842 13.438 -38.205 1.00 42.56 ? 187  VAL A N   1 
ATOM   1411 C CA  . VAL A 1 187 ? -116.060 13.179 -38.965 1.00 40.93 ? 187  VAL A CA  1 
ATOM   1412 C C   . VAL A 1 187 ? -115.745 13.121 -40.461 1.00 40.56 ? 187  VAL A C   1 
ATOM   1413 O O   . VAL A 1 187 ? -114.575 13.186 -40.846 1.00 38.54 ? 187  VAL A O   1 
ATOM   1414 C CB  . VAL A 1 187 ? -117.117 14.276 -38.703 1.00 42.69 ? 187  VAL A CB  1 
ATOM   1415 C CG1 . VAL A 1 187 ? -117.431 14.338 -37.210 1.00 41.70 ? 187  VAL A CG1 1 
ATOM   1416 C CG2 . VAL A 1 187 ? -116.608 15.630 -39.197 1.00 42.09 ? 187  VAL A CG2 1 
ATOM   1417 N N   . ASP A 1 188 ? -116.782 12.997 -41.290 1.00 39.66 ? 188  ASP A N   1 
ATOM   1418 C CA  . ASP A 1 188 ? -116.610 12.927 -42.739 1.00 41.11 ? 188  ASP A CA  1 
ATOM   1419 C C   . ASP A 1 188 ? -116.556 14.318 -43.349 1.00 40.12 ? 188  ASP A C   1 
ATOM   1420 O O   . ASP A 1 188 ? -116.967 15.298 -42.734 1.00 40.64 ? 188  ASP A O   1 
ATOM   1421 C CB  . ASP A 1 188 ? -117.775 12.170 -43.403 1.00 41.25 ? 188  ASP A CB  1 
ATOM   1422 C CG  . ASP A 1 188 ? -117.986 10.794 -42.832 1.00 41.50 ? 188  ASP A CG  1 
ATOM   1423 O OD1 . ASP A 1 188 ? -116.986 10.135 -42.493 1.00 41.50 ? 188  ASP A OD1 1 
ATOM   1424 O OD2 . ASP A 1 188 ? -119.152 10.370 -42.730 1.00 45.34 ? 188  ASP A OD2 1 
ATOM   1425 N N   . PHE A 1 189 ? -116.054 14.385 -44.573 1.00 39.30 ? 189  PHE A N   1 
ATOM   1426 C CA  . PHE A 1 189 ? -115.969 15.637 -45.293 1.00 36.61 ? 189  PHE A CA  1 
ATOM   1427 C C   . PHE A 1 189 ? -116.543 15.359 -46.664 1.00 35.46 ? 189  PHE A C   1 
ATOM   1428 O O   . PHE A 1 189 ? -116.598 14.216 -47.104 1.00 35.87 ? 189  PHE A O   1 
ATOM   1429 C CB  . PHE A 1 189 ? -114.513 16.116 -45.389 1.00 34.63 ? 189  PHE A CB  1 
ATOM   1430 C CG  . PHE A 1 189 ? -113.673 15.338 -46.353 1.00 33.41 ? 189  PHE A CG  1 
ATOM   1431 C CD1 . PHE A 1 189 ? -113.700 15.645 -47.704 1.00 34.29 ? 189  PHE A CD1 1 
ATOM   1432 C CD2 . PHE A 1 189 ? -112.850 14.308 -45.916 1.00 33.13 ? 189  PHE A CD2 1 
ATOM   1433 C CE1 . PHE A 1 189 ? -112.930 14.939 -48.613 1.00 33.29 ? 189  PHE A CE1 1 
ATOM   1434 C CE2 . PHE A 1 189 ? -112.066 13.586 -46.829 1.00 34.31 ? 189  PHE A CE2 1 
ATOM   1435 C CZ  . PHE A 1 189 ? -112.108 13.908 -48.179 1.00 33.02 ? 189  PHE A CZ  1 
ATOM   1436 N N   . ALA A 1 190 ? -116.978 16.411 -47.335 1.00 35.03 ? 190  ALA A N   1 
ATOM   1437 C CA  . ALA A 1 190 ? -117.547 16.271 -48.652 1.00 35.53 ? 190  ALA A CA  1 
ATOM   1438 C C   . ALA A 1 190 ? -117.233 17.559 -49.371 1.00 35.81 ? 190  ALA A C   1 
ATOM   1439 O O   . ALA A 1 190 ? -116.896 18.554 -48.736 1.00 35.88 ? 190  ALA A O   1 
ATOM   1440 C CB  . ALA A 1 190 ? -119.034 16.061 -48.553 1.00 34.90 ? 190  ALA A CB  1 
ATOM   1441 N N   . LEU A 1 191 ? -117.337 17.552 -50.689 1.00 36.43 ? 191  LEU A N   1 
ATOM   1442 C CA  . LEU A 1 191 ? -117.039 18.751 -51.448 1.00 36.47 ? 191  LEU A CA  1 
ATOM   1443 C C   . LEU A 1 191 ? -117.998 18.895 -52.607 1.00 36.38 ? 191  LEU A C   1 
ATOM   1444 O O   . LEU A 1 191 ? -118.430 17.905 -53.199 1.00 36.40 ? 191  LEU A O   1 
ATOM   1445 C CB  . LEU A 1 191 ? -115.592 18.718 -51.949 1.00 35.79 ? 191  LEU A CB  1 
ATOM   1446 C CG  . LEU A 1 191 ? -115.130 19.891 -52.815 1.00 39.18 ? 191  LEU A CG  1 
ATOM   1447 C CD1 . LEU A 1 191 ? -113.636 20.120 -52.599 1.00 41.21 ? 191  LEU A CD1 1 
ATOM   1448 C CD2 . LEU A 1 191 ? -115.443 19.614 -54.277 1.00 39.14 ? 191  LEU A CD2 1 
ATOM   1449 N N   . ILE A 1 192 ? -118.331 20.141 -52.916 1.00 35.28 ? 192  ILE A N   1 
ATOM   1450 C CA  . ILE A 1 192 ? -119.234 20.441 -54.004 1.00 37.85 ? 192  ILE A CA  1 
ATOM   1451 C C   . ILE A 1 192 ? -118.469 21.188 -55.075 1.00 37.90 ? 192  ILE A C   1 
ATOM   1452 O O   . ILE A 1 192 ? -117.537 21.925 -54.777 1.00 36.90 ? 192  ILE A O   1 
ATOM   1453 C CB  . ILE A 1 192 ? -120.415 21.302 -53.523 1.00 36.88 ? 192  ILE A CB  1 
ATOM   1454 C CG1 . ILE A 1 192 ? -121.288 20.483 -52.568 1.00 39.36 ? 192  ILE A CG1 1 
ATOM   1455 C CG2 . ILE A 1 192 ? -121.224 21.793 -54.714 1.00 38.66 ? 192  ILE A CG2 1 
ATOM   1456 C CD1 . ILE A 1 192 ? -122.520 21.211 -52.079 1.00 38.88 ? 192  ILE A CD1 1 
ATOM   1457 N N   . HIS A 1 193 ? -118.856 20.980 -56.326 1.00 39.65 ? 193  HIS A N   1 
ATOM   1458 C CA  . HIS A 1 193 ? -118.199 21.645 -57.435 1.00 42.28 ? 193  HIS A CA  1 
ATOM   1459 C C   . HIS A 1 193 ? -119.203 22.057 -58.498 1.00 45.12 ? 193  HIS A C   1 
ATOM   1460 O O   . HIS A 1 193 ? -120.080 21.280 -58.869 1.00 43.86 ? 193  HIS A O   1 
ATOM   1461 C CB  . HIS A 1 193 ? -117.157 20.720 -58.060 1.00 41.83 ? 193  HIS A CB  1 
ATOM   1462 C CG  . HIS A 1 193 ? -116.528 21.272 -59.302 1.00 40.32 ? 193  HIS A CG  1 
ATOM   1463 N ND1 . HIS A 1 193 ? -115.848 22.469 -59.324 1.00 39.64 ? 193  HIS A ND1 1 
ATOM   1464 C CD2 . HIS A 1 193 ? -116.477 20.784 -60.564 1.00 40.07 ? 193  HIS A CD2 1 
ATOM   1465 C CE1 . HIS A 1 193 ? -115.403 22.698 -60.548 1.00 38.55 ? 193  HIS A CE1 1 
ATOM   1466 N NE2 . HIS A 1 193 ? -115.771 21.691 -61.318 1.00 40.87 ? 193  HIS A NE2 1 
ATOM   1467 N N   . LYS A 1 194 ? -119.080 23.290 -58.972 1.00 49.17 ? 194  LYS A N   1 
ATOM   1468 C CA  . LYS A 1 194 ? -119.960 23.779 -60.019 1.00 55.55 ? 194  LYS A CA  1 
ATOM   1469 C C   . LYS A 1 194 ? -119.290 23.468 -61.345 1.00 59.08 ? 194  LYS A C   1 
ATOM   1470 O O   . LYS A 1 194 ? -118.206 23.976 -61.628 1.00 57.29 ? 194  LYS A O   1 
ATOM   1471 C CB  . LYS A 1 194 ? -120.172 25.290 -59.904 1.00 59.55 ? 194  LYS A CB  1 
ATOM   1472 C CG  . LYS A 1 194 ? -121.345 25.701 -59.034 1.00 64.91 ? 194  LYS A CG  1 
ATOM   1473 C CD  . LYS A 1 194 ? -122.105 26.861 -59.676 1.00 67.36 ? 194  LYS A CD  1 
ATOM   1474 C CE  . LYS A 1 194 ? -123.354 27.225 -58.876 1.00 69.08 ? 194  LYS A CE  1 
ATOM   1475 N NZ  . LYS A 1 194 ? -124.133 28.334 -59.502 1.00 67.82 ? 194  LYS A NZ  1 
ATOM   1476 N N   . GLU A 1 195 ? -119.927 22.628 -62.154 1.00 63.88 ? 195  GLU A N   1 
ATOM   1477 C CA  . GLU A 1 195 ? -119.367 22.269 -63.452 1.00 68.28 ? 195  GLU A CA  1 
ATOM   1478 C C   . GLU A 1 195 ? -118.941 23.540 -64.185 1.00 68.86 ? 195  GLU A C   1 
ATOM   1479 O O   . GLU A 1 195 ? -119.750 24.187 -64.848 1.00 70.10 ? 195  GLU A O   1 
ATOM   1480 C CB  . GLU A 1 195 ? -120.399 21.500 -64.280 1.00 71.00 ? 195  GLU A CB  1 
ATOM   1481 C CG  . GLU A 1 195 ? -119.963 20.090 -64.666 1.00 75.35 ? 195  GLU A CG  1 
ATOM   1482 C CD  . GLU A 1 195 ? -119.813 19.165 -63.470 1.00 77.02 ? 195  GLU A CD  1 
ATOM   1483 O OE1 . GLU A 1 195 ? -119.033 19.498 -62.549 1.00 77.11 ? 195  GLU A OE1 1 
ATOM   1484 O OE2 . GLU A 1 195 ? -120.473 18.101 -63.456 1.00 76.30 ? 195  GLU A OE2 1 
ATOM   1485 N N   . ARG A 1 196 ? -117.664 23.892 -64.044 1.00 69.19 ? 196  ARG A N   1 
ATOM   1486 C CA  . ARG A 1 196 ? -117.102 25.087 -64.668 1.00 68.31 ? 196  ARG A CA  1 
ATOM   1487 C C   . ARG A 1 196 ? -116.425 24.737 -65.989 1.00 67.48 ? 196  ARG A C   1 
ATOM   1488 O O   . ARG A 1 196 ? -117.070 24.246 -66.917 1.00 67.27 ? 196  ARG A O   1 
ATOM   1489 C CB  . ARG A 1 196 ? -116.090 25.752 -63.714 1.00 67.93 ? 196  ARG A CB  1 
ATOM   1490 C CG  . ARG A 1 196 ? -116.697 26.209 -62.376 1.00 65.87 ? 196  ARG A CG  1 
ATOM   1491 C CD  . ARG A 1 196 ? -115.659 26.317 -61.249 1.00 64.20 ? 196  ARG A CD  1 
ATOM   1492 N NE  . ARG A 1 196 ? -116.179 25.760 -59.994 1.00 63.09 ? 196  ARG A NE  1 
ATOM   1493 C CZ  . ARG A 1 196 ? -115.483 25.631 -58.865 1.00 60.39 ? 196  ARG A CZ  1 
ATOM   1494 N NH1 . ARG A 1 196 ? -114.219 26.023 -58.801 1.00 59.74 ? 196  ARG A NH1 1 
ATOM   1495 N NH2 . ARG A 1 196 ? -116.052 25.090 -57.798 1.00 55.63 ? 196  ARG A NH2 1 
ATOM   1496 N N   . ASP A 1 203 ? -124.670 26.281 -64.626 1.00 72.76 ? 203  ASP A N   1 
ATOM   1497 C CA  . ASP A 1 203 ? -124.168 24.911 -64.614 1.00 72.17 ? 203  ASP A CA  1 
ATOM   1498 C C   . ASP A 1 203 ? -124.778 24.138 -63.452 1.00 71.72 ? 203  ASP A C   1 
ATOM   1499 O O   . ASP A 1 203 ? -125.476 24.710 -62.613 1.00 72.13 ? 203  ASP A O   1 
ATOM   1500 C CB  . ASP A 1 203 ? -122.644 24.907 -64.480 1.00 73.03 ? 203  ASP A CB  1 
ATOM   1501 C CG  . ASP A 1 203 ? -121.965 25.796 -65.503 1.00 73.10 ? 203  ASP A CG  1 
ATOM   1502 O OD1 . ASP A 1 203 ? -122.155 25.566 -66.716 1.00 72.51 ? 203  ASP A OD1 1 
ATOM   1503 O OD2 . ASP A 1 203 ? -121.239 26.724 -65.089 1.00 72.00 ? 203  ASP A OD2 1 
ATOM   1504 N N   . ARG A 1 204 ? -124.509 22.837 -63.405 1.00 70.08 ? 204  ARG A N   1 
ATOM   1505 C CA  . ARG A 1 204 ? -125.034 21.994 -62.336 1.00 68.33 ? 204  ARG A CA  1 
ATOM   1506 C C   . ARG A 1 204 ? -123.952 21.770 -61.288 1.00 65.19 ? 204  ARG A C   1 
ATOM   1507 O O   . ARG A 1 204 ? -122.762 21.895 -61.577 1.00 65.28 ? 204  ARG A O   1 
ATOM   1508 C CB  . ARG A 1 204 ? -125.479 20.640 -62.895 1.00 71.56 ? 204  ARG A CB  1 
ATOM   1509 C CG  . ARG A 1 204 ? -124.329 19.683 -63.165 1.00 75.13 ? 204  ARG A CG  1 
ATOM   1510 C CD  . ARG A 1 204 ? -124.794 18.419 -63.863 1.00 78.86 ? 204  ARG A CD  1 
ATOM   1511 N NE  . ARG A 1 204 ? -123.715 17.440 -63.966 1.00 82.05 ? 204  ARG A NE  1 
ATOM   1512 C CZ  . ARG A 1 204 ? -123.739 16.381 -64.769 1.00 83.36 ? 204  ARG A CZ  1 
ATOM   1513 N NH1 . ARG A 1 204 ? -124.787 16.158 -65.551 1.00 84.41 ? 204  ARG A NH1 1 
ATOM   1514 N NH2 . ARG A 1 204 ? -122.712 15.544 -64.791 1.00 84.49 ? 204  ARG A NH2 1 
ATOM   1515 N N   . MET A 1 205 ? -124.364 21.434 -60.072 1.00 60.72 ? 205  MET A N   1 
ATOM   1516 C CA  . MET A 1 205 ? -123.410 21.183 -59.008 1.00 57.21 ? 205  MET A CA  1 
ATOM   1517 C C   . MET A 1 205 ? -123.255 19.697 -58.738 1.00 54.99 ? 205  MET A C   1 
ATOM   1518 O O   . MET A 1 205 ? -124.227 18.947 -58.745 1.00 54.44 ? 205  MET A O   1 
ATOM   1519 C CB  . MET A 1 205 ? -123.832 21.891 -57.724 1.00 58.60 ? 205  MET A CB  1 
ATOM   1520 C CG  . MET A 1 205 ? -123.694 23.396 -57.780 1.00 60.31 ? 205  MET A CG  1 
ATOM   1521 S SD  . MET A 1 205 ? -123.923 24.114 -56.157 1.00 62.71 ? 205  MET A SD  1 
ATOM   1522 C CE  . MET A 1 205 ? -125.681 23.784 -55.917 1.00 64.53 ? 205  MET A CE  1 
ATOM   1523 N N   . VAL A 1 206 ? -122.017 19.285 -58.497 1.00 51.92 ? 206  VAL A N   1 
ATOM   1524 C CA  . VAL A 1 206 ? -121.692 17.895 -58.216 1.00 48.56 ? 206  VAL A CA  1 
ATOM   1525 C C   . VAL A 1 206 ? -121.249 17.802 -56.758 1.00 46.22 ? 206  VAL A C   1 
ATOM   1526 O O   . VAL A 1 206 ? -120.692 18.754 -56.211 1.00 43.87 ? 206  VAL A O   1 
ATOM   1527 C CB  . VAL A 1 206 ? -120.549 17.410 -59.140 1.00 48.74 ? 206  VAL A CB  1 
ATOM   1528 C CG1 . VAL A 1 206 ? -120.094 16.023 -58.738 1.00 50.17 ? 206  VAL A CG1 1 
ATOM   1529 C CG2 . VAL A 1 206 ? -121.020 17.409 -60.577 1.00 49.17 ? 206  VAL A CG2 1 
ATOM   1530 N N   . LEU A 1 207 ? -121.500 16.661 -56.132 1.00 43.92 ? 207  LEU A N   1 
ATOM   1531 C CA  . LEU A 1 207 ? -121.118 16.475 -54.744 1.00 43.57 ? 207  LEU A CA  1 
ATOM   1532 C C   . LEU A 1 207 ? -120.427 15.135 -54.523 1.00 42.28 ? 207  LEU A C   1 
ATOM   1533 O O   . LEU A 1 207 ? -120.906 14.089 -54.958 1.00 42.76 ? 207  LEU A O   1 
ATOM   1534 C CB  . LEU A 1 207 ? -122.354 16.582 -53.841 1.00 43.62 ? 207  LEU A CB  1 
ATOM   1535 C CG  . LEU A 1 207 ? -122.168 16.628 -52.316 1.00 44.73 ? 207  LEU A CG  1 
ATOM   1536 C CD1 . LEU A 1 207 ? -123.475 17.073 -51.681 1.00 45.36 ? 207  LEU A CD1 1 
ATOM   1537 C CD2 . LEU A 1 207 ? -121.754 15.274 -51.778 1.00 44.43 ? 207  LEU A CD2 1 
ATOM   1538 N N   . VAL A 1 208 ? -119.289 15.188 -53.847 1.00 39.62 ? 208  VAL A N   1 
ATOM   1539 C CA  . VAL A 1 208 ? -118.522 14.000 -53.538 1.00 38.36 ? 208  VAL A CA  1 
ATOM   1540 C C   . VAL A 1 208 ? -118.370 13.953 -52.030 1.00 39.50 ? 208  VAL A C   1 
ATOM   1541 O O   . VAL A 1 208 ? -118.061 14.961 -51.397 1.00 40.60 ? 208  VAL A O   1 
ATOM   1542 C CB  . VAL A 1 208 ? -117.138 14.033 -54.219 1.00 35.87 ? 208  VAL A CB  1 
ATOM   1543 C CG1 . VAL A 1 208 ? -117.313 14.272 -55.699 1.00 34.90 ? 208  VAL A CG1 1 
ATOM   1544 C CG2 . VAL A 1 208 ? -116.264 15.114 -53.610 1.00 31.76 ? 208  VAL A CG2 1 
ATOM   1545 N N   . GLY A 1 209 ? -118.600 12.780 -51.454 1.00 40.28 ? 209  GLY A N   1 
ATOM   1546 C CA  . GLY A 1 209 ? -118.508 12.639 -50.012 1.00 41.80 ? 209  GLY A CA  1 
ATOM   1547 C C   . GLY A 1 209 ? -119.865 12.245 -49.471 1.00 42.92 ? 209  GLY A C   1 
ATOM   1548 O O   . GLY A 1 209 ? -120.881 12.444 -50.129 1.00 41.52 ? 209  GLY A O   1 
ATOM   1549 N N   . ASP A 1 210 ? -119.889 11.688 -48.271 1.00 45.00 ? 210  ASP A N   1 
ATOM   1550 C CA  . ASP A 1 210 ? -121.130 11.209 -47.680 1.00 47.24 ? 210  ASP A CA  1 
ATOM   1551 C C   . ASP A 1 210 ? -121.836 12.195 -46.753 1.00 47.32 ? 210  ASP A C   1 
ATOM   1552 O O   . ASP A 1 210 ? -121.315 12.546 -45.690 1.00 47.20 ? 210  ASP A O   1 
ATOM   1553 C CB  . ASP A 1 210 ? -120.837 9.901  -46.931 1.00 49.02 ? 210  ASP A CB  1 
ATOM   1554 C CG  . ASP A 1 210 ? -122.076 9.275  -46.335 1.00 51.91 ? 210  ASP A CG  1 
ATOM   1555 O OD1 . ASP A 1 210 ? -123.169 9.494  -46.908 1.00 53.67 ? 210  ASP A OD1 1 
ATOM   1556 O OD2 . ASP A 1 210 ? -121.961 8.554  -45.317 1.00 52.21 ? 210  ASP A OD2 1 
ATOM   1557 N N   . VAL A 1 211 ? -123.034 12.619 -47.154 1.00 47.77 ? 211  VAL A N   1 
ATOM   1558 C CA  . VAL A 1 211 ? -123.839 13.563 -46.373 1.00 48.43 ? 211  VAL A CA  1 
ATOM   1559 C C   . VAL A 1 211 ? -125.243 13.027 -46.053 1.00 49.39 ? 211  VAL A C   1 
ATOM   1560 O O   . VAL A 1 211 ? -125.971 13.619 -45.254 1.00 48.71 ? 211  VAL A O   1 
ATOM   1561 C CB  . VAL A 1 211 ? -124.036 14.909 -47.136 1.00 48.27 ? 211  VAL A CB  1 
ATOM   1562 C CG1 . VAL A 1 211 ? -122.682 15.536 -47.476 1.00 47.87 ? 211  VAL A CG1 1 
ATOM   1563 C CG2 . VAL A 1 211 ? -124.859 14.680 -48.386 1.00 46.42 ? 211  VAL A CG2 1 
ATOM   1564 N N   . LYS A 1 212 ? -125.613 11.916 -46.683 1.00 51.15 ? 212  LYS A N   1 
ATOM   1565 C CA  . LYS A 1 212 ? -126.927 11.292 -46.506 1.00 52.63 ? 212  LYS A CA  1 
ATOM   1566 C C   . LYS A 1 212 ? -127.273 10.973 -45.053 1.00 52.97 ? 212  LYS A C   1 
ATOM   1567 O O   . LYS A 1 212 ? -126.513 10.290 -44.364 1.00 52.02 ? 212  LYS A O   1 
ATOM   1568 C CB  . LYS A 1 212 ? -126.995 9.995  -47.317 1.00 55.09 ? 212  LYS A CB  1 
ATOM   1569 C CG  . LYS A 1 212 ? -128.383 9.367  -47.401 1.00 57.26 ? 212  LYS A CG  1 
ATOM   1570 C CD  . LYS A 1 212 ? -129.309 10.203 -48.274 1.00 59.17 ? 212  LYS A CD  1 
ATOM   1571 C CE  . LYS A 1 212 ? -130.687 9.565  -48.402 1.00 60.99 ? 212  LYS A CE  1 
ATOM   1572 N NZ  . LYS A 1 212 ? -131.634 10.363 -49.247 1.00 61.25 ? 212  LYS A NZ  1 
ATOM   1573 N N   . ASP A 1 213 ? -128.434 11.453 -44.605 1.00 53.43 ? 213  ASP A N   1 
ATOM   1574 C CA  . ASP A 1 213 ? -128.917 11.227 -43.238 1.00 54.37 ? 213  ASP A CA  1 
ATOM   1575 C C   . ASP A 1 213 ? -127.982 11.707 -42.144 1.00 53.58 ? 213  ASP A C   1 
ATOM   1576 O O   . ASP A 1 213 ? -127.735 10.998 -41.168 1.00 54.09 ? 213  ASP A O   1 
ATOM   1577 C CB  . ASP A 1 213 ? -129.218 9.745  -43.016 1.00 55.30 ? 213  ASP A CB  1 
ATOM   1578 C CG  . ASP A 1 213 ? -130.440 9.288  -43.769 1.00 57.92 ? 213  ASP A CG  1 
ATOM   1579 O OD1 . ASP A 1 213 ? -130.641 8.062  -43.913 1.00 60.57 ? 213  ASP A OD1 1 
ATOM   1580 O OD2 . ASP A 1 213 ? -131.208 10.164 -44.216 1.00 60.34 ? 213  ASP A OD2 1 
ATOM   1581 N N   . ARG A 1 214 ? -127.455 12.909 -42.311 1.00 52.88 ? 214  ARG A N   1 
ATOM   1582 C CA  . ARG A 1 214 ? -126.562 13.476 -41.315 1.00 51.84 ? 214  ARG A CA  1 
ATOM   1583 C C   . ARG A 1 214 ? -126.435 14.978 -41.495 1.00 50.03 ? 214  ARG A C   1 
ATOM   1584 O O   . ARG A 1 214 ? -126.627 15.500 -42.591 1.00 50.15 ? 214  ARG A O   1 
ATOM   1585 C CB  . ARG A 1 214 ? -125.192 12.788 -41.371 1.00 53.24 ? 214  ARG A CB  1 
ATOM   1586 C CG  . ARG A 1 214 ? -124.690 12.430 -42.761 1.00 53.93 ? 214  ARG A CG  1 
ATOM   1587 C CD  . ARG A 1 214 ? -123.527 11.435 -42.664 1.00 53.23 ? 214  ARG A CD  1 
ATOM   1588 N NE  . ARG A 1 214 ? -122.377 11.994 -41.961 1.00 52.10 ? 214  ARG A NE  1 
ATOM   1589 C CZ  . ARG A 1 214 ? -121.477 11.269 -41.305 1.00 52.18 ? 214  ARG A CZ  1 
ATOM   1590 N NH1 . ARG A 1 214 ? -121.597 9.950  -41.260 1.00 53.26 ? 214  ARG A NH1 1 
ATOM   1591 N NH2 . ARG A 1 214 ? -120.455 11.858 -40.697 1.00 48.65 ? 214  ARG A NH2 1 
ATOM   1592 N N   . VAL A 1 215 ? -126.139 15.676 -40.408 1.00 47.95 ? 215  VAL A N   1 
ATOM   1593 C CA  . VAL A 1 215 ? -126.015 17.125 -40.458 1.00 46.59 ? 215  VAL A CA  1 
ATOM   1594 C C   . VAL A 1 215 ? -124.847 17.558 -41.341 1.00 45.68 ? 215  VAL A C   1 
ATOM   1595 O O   . VAL A 1 215 ? -123.737 17.049 -41.210 1.00 45.72 ? 215  VAL A O   1 
ATOM   1596 C CB  . VAL A 1 215 ? -125.815 17.706 -39.045 1.00 47.43 ? 215  VAL A CB  1 
ATOM   1597 C CG1 . VAL A 1 215 ? -125.850 19.231 -39.095 1.00 46.65 ? 215  VAL A CG1 1 
ATOM   1598 C CG2 . VAL A 1 215 ? -126.891 17.172 -38.112 1.00 46.74 ? 215  VAL A CG2 1 
ATOM   1599 N N   . ALA A 1 216 ? -125.102 18.504 -42.237 1.00 43.63 ? 216  ALA A N   1 
ATOM   1600 C CA  . ALA A 1 216 ? -124.063 18.999 -43.127 1.00 43.10 ? 216  ALA A CA  1 
ATOM   1601 C C   . ALA A 1 216 ? -123.642 20.409 -42.729 1.00 42.11 ? 216  ALA A C   1 
ATOM   1602 O O   . ALA A 1 216 ? -124.462 21.331 -42.697 1.00 41.31 ? 216  ALA A O   1 
ATOM   1603 C CB  . ALA A 1 216 ? -124.560 18.989 -44.567 1.00 41.22 ? 216  ALA A CB  1 
ATOM   1604 N N   . ILE A 1 217 ? -122.361 20.576 -42.424 1.00 41.43 ? 217  ILE A N   1 
ATOM   1605 C CA  . ILE A 1 217 ? -121.855 21.889 -42.044 1.00 40.84 ? 217  ILE A CA  1 
ATOM   1606 C C   . ILE A 1 217 ? -120.991 22.482 -43.152 1.00 39.68 ? 217  ILE A C   1 
ATOM   1607 O O   . ILE A 1 217 ? -119.866 22.041 -43.376 1.00 39.02 ? 217  ILE A O   1 
ATOM   1608 C CB  . ILE A 1 217 ? -121.005 21.828 -40.744 1.00 39.50 ? 217  ILE A CB  1 
ATOM   1609 C CG1 . ILE A 1 217 ? -121.818 21.212 -39.604 1.00 37.69 ? 217  ILE A CG1 1 
ATOM   1610 C CG2 . ILE A 1 217 ? -120.567 23.227 -40.347 1.00 37.12 ? 217  ILE A CG2 1 
ATOM   1611 C CD1 . ILE A 1 217 ? -121.042 21.101 -38.308 1.00 37.30 ? 217  ILE A CD1 1 
ATOM   1612 N N   . LEU A 1 218 ? -121.531 23.474 -43.851 1.00 38.31 ? 218  LEU A N   1 
ATOM   1613 C CA  . LEU A 1 218 ? -120.795 24.145 -44.909 1.00 37.63 ? 218  LEU A CA  1 
ATOM   1614 C C   . LEU A 1 218 ? -119.798 25.092 -44.263 1.00 39.84 ? 218  LEU A C   1 
ATOM   1615 O O   . LEU A 1 218 ? -120.178 25.973 -43.485 1.00 40.19 ? 218  LEU A O   1 
ATOM   1616 C CB  . LEU A 1 218 ? -121.740 24.937 -45.810 1.00 36.25 ? 218  LEU A CB  1 
ATOM   1617 C CG  . LEU A 1 218 ? -122.428 24.140 -46.916 1.00 36.95 ? 218  LEU A CG  1 
ATOM   1618 C CD1 . LEU A 1 218 ? -123.539 24.974 -47.538 1.00 37.39 ? 218  LEU A CD1 1 
ATOM   1619 C CD2 . LEU A 1 218 ? -121.395 23.739 -47.968 1.00 35.50 ? 218  LEU A CD2 1 
ATOM   1620 N N   . VAL A 1 219 ? -118.522 24.896 -44.580 1.00 39.76 ? 219  VAL A N   1 
ATOM   1621 C CA  . VAL A 1 219 ? -117.455 25.719 -44.035 1.00 40.19 ? 219  VAL A CA  1 
ATOM   1622 C C   . VAL A 1 219 ? -116.698 26.411 -45.161 1.00 40.47 ? 219  VAL A C   1 
ATOM   1623 O O   . VAL A 1 219 ? -116.348 25.793 -46.164 1.00 39.50 ? 219  VAL A O   1 
ATOM   1624 C CB  . VAL A 1 219 ? -116.471 24.870 -43.204 1.00 40.91 ? 219  VAL A CB  1 
ATOM   1625 C CG1 . VAL A 1 219 ? -115.360 25.741 -42.668 1.00 41.69 ? 219  VAL A CG1 1 
ATOM   1626 C CG2 . VAL A 1 219 ? -117.207 24.192 -42.065 1.00 41.12 ? 219  VAL A CG2 1 
ATOM   1627 N N   . ASP A 1 220 ? -116.452 27.702 -44.978 1.00 40.96 ? 220  ASP A N   1 
ATOM   1628 C CA  . ASP A 1 220 ? -115.760 28.507 -45.970 1.00 41.22 ? 220  ASP A CA  1 
ATOM   1629 C C   . ASP A 1 220 ? -115.088 29.680 -45.246 1.00 40.98 ? 220  ASP A C   1 
ATOM   1630 O O   . ASP A 1 220 ? -115.509 30.059 -44.153 1.00 38.86 ? 220  ASP A O   1 
ATOM   1631 C CB  . ASP A 1 220 ? -116.781 29.007 -46.992 1.00 40.74 ? 220  ASP A CB  1 
ATOM   1632 C CG  . ASP A 1 220 ? -116.158 29.339 -48.324 1.00 42.66 ? 220  ASP A CG  1 
ATOM   1633 O OD1 . ASP A 1 220 ? -115.050 28.831 -48.590 1.00 42.53 ? 220  ASP A OD1 1 
ATOM   1634 O OD2 . ASP A 1 220 ? -116.784 30.090 -49.107 1.00 43.33 ? 220  ASP A OD2 1 
ATOM   1635 N N   . ASP A 1 221 ? -114.041 30.251 -45.833 1.00 41.16 ? 221  ASP A N   1 
ATOM   1636 C CA  . ASP A 1 221 ? -113.372 31.367 -45.170 1.00 41.38 ? 221  ASP A CA  1 
ATOM   1637 C C   . ASP A 1 221 ? -114.188 32.642 -45.257 1.00 40.81 ? 221  ASP A C   1 
ATOM   1638 O O   . ASP A 1 221 ? -114.114 33.484 -44.367 1.00 41.01 ? 221  ASP A O   1 
ATOM   1639 C CB  . ASP A 1 221 ? -111.974 31.615 -45.742 1.00 41.38 ? 221  ASP A CB  1 
ATOM   1640 C CG  . ASP A 1 221 ? -111.995 32.026 -47.196 1.00 43.14 ? 221  ASP A CG  1 
ATOM   1641 O OD1 . ASP A 1 221 ? -111.031 32.698 -47.616 1.00 44.69 ? 221  ASP A OD1 1 
ATOM   1642 O OD2 . ASP A 1 221 ? -112.954 31.673 -47.921 1.00 45.39 ? 221  ASP A OD2 1 
ATOM   1643 N N   . MET A 1 222 ? -114.961 32.788 -46.327 1.00 41.67 ? 222  MET A N   1 
ATOM   1644 C CA  . MET A 1 222 ? -115.793 33.972 -46.490 1.00 44.93 ? 222  MET A CA  1 
ATOM   1645 C C   . MET A 1 222 ? -116.992 33.733 -47.391 1.00 45.58 ? 222  MET A C   1 
ATOM   1646 O O   . MET A 1 222 ? -117.048 32.756 -48.136 1.00 46.12 ? 222  MET A O   1 
ATOM   1647 C CB  . MET A 1 222 ? -114.977 35.145 -47.042 1.00 46.64 ? 222  MET A CB  1 
ATOM   1648 C CG  . MET A 1 222 ? -114.403 34.931 -48.434 1.00 48.03 ? 222  MET A CG  1 
ATOM   1649 S SD  . MET A 1 222 ? -113.572 36.420 -49.043 1.00 54.41 ? 222  MET A SD  1 
ATOM   1650 C CE  . MET A 1 222 ? -111.933 36.251 -48.324 1.00 49.69 ? 222  MET A CE  1 
ATOM   1651 N N   . ALA A 1 223 ? -117.955 34.643 -47.297 1.00 46.91 ? 223  ALA A N   1 
ATOM   1652 C CA  . ALA A 1 223 ? -119.175 34.596 -48.090 1.00 48.30 ? 223  ALA A CA  1 
ATOM   1653 C C   . ALA A 1 223 ? -119.609 36.032 -48.340 1.00 49.34 ? 223  ALA A C   1 
ATOM   1654 O O   . ALA A 1 223 ? -119.658 36.841 -47.419 1.00 51.11 ? 223  ALA A O   1 
ATOM   1655 C CB  . ALA A 1 223 ? -120.256 33.848 -47.348 1.00 45.03 ? 223  ALA A CB  1 
ATOM   1656 N N   . ASP A 1 224 ? -119.911 36.350 -49.590 1.00 51.41 ? 224  ASP A N   1 
ATOM   1657 C CA  . ASP A 1 224 ? -120.330 37.696 -49.943 1.00 52.90 ? 224  ASP A CA  1 
ATOM   1658 C C   . ASP A 1 224 ? -121.815 37.724 -50.274 1.00 53.30 ? 224  ASP A C   1 
ATOM   1659 O O   . ASP A 1 224 ? -122.644 37.979 -49.404 1.00 54.99 ? 224  ASP A O   1 
ATOM   1660 C CB  . ASP A 1 224 ? -119.524 38.204 -51.136 1.00 52.81 ? 224  ASP A CB  1 
ATOM   1661 C CG  . ASP A 1 224 ? -119.898 39.614 -51.523 1.00 56.08 ? 224  ASP A CG  1 
ATOM   1662 O OD1 . ASP A 1 224 ? -119.800 40.503 -50.657 1.00 57.64 ? 224  ASP A OD1 1 
ATOM   1663 O OD2 . ASP A 1 224 ? -120.291 39.838 -52.687 1.00 58.47 ? 224  ASP A OD2 1 
ATOM   1664 N N   . THR A 1 225 ? -122.147 37.458 -51.533 1.00 53.35 ? 225  THR A N   1 
ATOM   1665 C CA  . THR A 1 225 ? -123.537 37.455 -51.971 1.00 52.87 ? 225  THR A CA  1 
ATOM   1666 C C   . THR A 1 225 ? -124.227 36.172 -51.508 1.00 52.06 ? 225  THR A C   1 
ATOM   1667 O O   . THR A 1 225 ? -125.456 36.074 -51.512 1.00 51.77 ? 225  THR A O   1 
ATOM   1668 C CB  . THR A 1 225 ? -123.629 37.558 -53.506 1.00 53.00 ? 225  THR A CB  1 
ATOM   1669 O OG1 . THR A 1 225 ? -123.242 36.313 -54.097 1.00 53.77 ? 225  THR A OG1 1 
ATOM   1670 C CG2 . THR A 1 225 ? -122.696 38.646 -54.013 1.00 51.70 ? 225  THR A CG2 1 
ATOM   1671 N N   . CYS A 1 226 ? -123.419 35.193 -51.111 1.00 50.71 ? 226  CYS A N   1 
ATOM   1672 C CA  . CYS A 1 226 ? -123.908 33.907 -50.623 1.00 49.28 ? 226  CYS A CA  1 
ATOM   1673 C C   . CYS A 1 226 ? -124.608 33.065 -51.673 1.00 48.69 ? 226  CYS A C   1 
ATOM   1674 O O   . CYS A 1 226 ? -125.318 32.117 -51.340 1.00 47.70 ? 226  CYS A O   1 
ATOM   1675 C CB  . CYS A 1 226 ? -124.840 34.120 -49.429 1.00 48.80 ? 226  CYS A CB  1 
ATOM   1676 S SG  . CYS A 1 226 ? -123.993 34.797 -48.000 1.00 46.69 ? 226  CYS A SG  1 
ATOM   1677 N N   . GLY A 1 227 ? -124.404 33.407 -52.940 1.00 49.11 ? 227  GLY A N   1 
ATOM   1678 C CA  . GLY A 1 227 ? -125.025 32.646 -54.008 1.00 49.58 ? 227  GLY A CA  1 
ATOM   1679 C C   . GLY A 1 227 ? -124.590 31.197 -53.924 1.00 49.50 ? 227  GLY A C   1 
ATOM   1680 O O   . GLY A 1 227 ? -125.412 30.278 -53.870 1.00 49.79 ? 227  GLY A O   1 
ATOM   1681 N N   . THR A 1 228 ? -123.278 31.006 -53.901 1.00 48.95 ? 228  THR A N   1 
ATOM   1682 C CA  . THR A 1 228 ? -122.684 29.684 -53.814 1.00 49.26 ? 228  THR A CA  1 
ATOM   1683 C C   . THR A 1 228 ? -123.154 28.945 -52.568 1.00 49.22 ? 228  THR A C   1 
ATOM   1684 O O   . THR A 1 228 ? -123.714 27.856 -52.658 1.00 49.14 ? 228  THR A O   1 
ATOM   1685 C CB  . THR A 1 228 ? -121.150 29.789 -53.777 1.00 49.64 ? 228  THR A CB  1 
ATOM   1686 O OG1 . THR A 1 228 ? -120.682 30.298 -55.031 1.00 48.65 ? 228  THR A OG1 1 
ATOM   1687 C CG2 . THR A 1 228 ? -120.521 28.435 -53.501 1.00 47.79 ? 228  THR A CG2 1 
ATOM   1688 N N   . ILE A 1 229 ? -122.929 29.555 -51.409 1.00 49.09 ? 229  ILE A N   1 
ATOM   1689 C CA  . ILE A 1 229 ? -123.300 28.962 -50.133 1.00 48.70 ? 229  ILE A CA  1 
ATOM   1690 C C   . ILE A 1 229 ? -124.765 28.522 -50.083 1.00 49.26 ? 229  ILE A C   1 
ATOM   1691 O O   . ILE A 1 229 ? -125.090 27.501 -49.480 1.00 47.16 ? 229  ILE A O   1 
ATOM   1692 C CB  . ILE A 1 229 ? -123.011 29.948 -48.972 1.00 49.89 ? 229  ILE A CB  1 
ATOM   1693 C CG1 . ILE A 1 229 ? -122.525 29.176 -47.749 1.00 50.45 ? 229  ILE A CG1 1 
ATOM   1694 C CG2 . ILE A 1 229 ? -124.248 30.759 -48.629 1.00 49.66 ? 229  ILE A CG2 1 
ATOM   1695 C CD1 . ILE A 1 229 ? -121.156 28.579 -47.932 1.00 50.74 ? 229  ILE A CD1 1 
ATOM   1696 N N   . CYS A 1 230 ? -125.642 29.289 -50.724 1.00 50.00 ? 230  CYS A N   1 
ATOM   1697 C CA  . CYS A 1 230 ? -127.061 28.963 -50.740 1.00 51.28 ? 230  CYS A CA  1 
ATOM   1698 C C   . CYS A 1 230 ? -127.375 27.825 -51.707 1.00 51.84 ? 230  CYS A C   1 
ATOM   1699 O O   . CYS A 1 230 ? -128.241 26.988 -51.437 1.00 49.98 ? 230  CYS A O   1 
ATOM   1700 C CB  . CYS A 1 230 ? -127.888 30.205 -51.083 1.00 50.92 ? 230  CYS A CB  1 
ATOM   1701 S SG  . CYS A 1 230 ? -128.019 31.381 -49.710 1.00 52.10 ? 230  CYS A SG  1 
ATOM   1702 N N   . HIS A 1 231 ? -126.676 27.787 -52.834 1.00 52.73 ? 231  HIS A N   1 
ATOM   1703 C CA  . HIS A 1 231 ? -126.903 26.709 -53.782 1.00 53.94 ? 231  HIS A CA  1 
ATOM   1704 C C   . HIS A 1 231 ? -126.381 25.399 -53.208 1.00 53.02 ? 231  HIS A C   1 
ATOM   1705 O O   . HIS A 1 231 ? -127.016 24.352 -53.342 1.00 54.24 ? 231  HIS A O   1 
ATOM   1706 C CB  . HIS A 1 231 ? -126.222 27.004 -55.115 1.00 56.21 ? 231  HIS A CB  1 
ATOM   1707 C CG  . HIS A 1 231 ? -127.046 27.844 -56.032 1.00 58.80 ? 231  HIS A CG  1 
ATOM   1708 N ND1 . HIS A 1 231 ? -128.377 27.579 -56.284 1.00 60.09 ? 231  HIS A ND1 1 
ATOM   1709 C CD2 . HIS A 1 231 ? -126.736 28.932 -56.775 1.00 60.20 ? 231  HIS A CD2 1 
ATOM   1710 C CE1 . HIS A 1 231 ? -128.847 28.465 -57.140 1.00 60.33 ? 231  HIS A CE1 1 
ATOM   1711 N NE2 . HIS A 1 231 ? -127.870 29.299 -57.455 1.00 60.43 ? 231  HIS A NE2 1 
ATOM   1712 N N   . ALA A 1 232 ? -125.225 25.462 -52.557 1.00 50.74 ? 232  ALA A N   1 
ATOM   1713 C CA  . ALA A 1 232 ? -124.627 24.275 -51.964 1.00 49.07 ? 232  ALA A CA  1 
ATOM   1714 C C   . ALA A 1 232 ? -125.568 23.686 -50.925 1.00 49.03 ? 232  ALA A C   1 
ATOM   1715 O O   . ALA A 1 232 ? -125.598 22.474 -50.713 1.00 47.70 ? 232  ALA A O   1 
ATOM   1716 C CB  . ALA A 1 232 ? -123.293 24.630 -51.325 1.00 48.71 ? 232  ALA A CB  1 
ATOM   1717 N N   . ALA A 1 233 ? -126.339 24.554 -50.279 1.00 48.90 ? 233  ALA A N   1 
ATOM   1718 C CA  . ALA A 1 233 ? -127.280 24.117 -49.258 1.00 49.36 ? 233  ALA A CA  1 
ATOM   1719 C C   . ALA A 1 233 ? -128.430 23.326 -49.874 1.00 49.22 ? 233  ALA A C   1 
ATOM   1720 O O   . ALA A 1 233 ? -128.818 22.279 -49.358 1.00 48.32 ? 233  ALA A O   1 
ATOM   1721 C CB  . ALA A 1 233 ? -127.814 25.319 -48.493 1.00 48.96 ? 233  ALA A CB  1 
ATOM   1722 N N   . ASP A 1 234 ? -128.979 23.831 -50.974 1.00 50.31 ? 234  ASP A N   1 
ATOM   1723 C CA  . ASP A 1 234 ? -130.074 23.141 -51.648 1.00 51.40 ? 234  ASP A CA  1 
ATOM   1724 C C   . ASP A 1 234 ? -129.581 21.771 -52.086 1.00 50.75 ? 234  ASP A C   1 
ATOM   1725 O O   . ASP A 1 234 ? -130.263 20.760 -51.902 1.00 50.78 ? 234  ASP A O   1 
ATOM   1726 C CB  . ASP A 1 234 ? -130.535 23.926 -52.877 1.00 53.95 ? 234  ASP A CB  1 
ATOM   1727 C CG  . ASP A 1 234 ? -131.190 25.237 -52.518 1.00 55.43 ? 234  ASP A CG  1 
ATOM   1728 O OD1 . ASP A 1 234 ? -132.160 25.220 -51.729 1.00 57.37 ? 234  ASP A OD1 1 
ATOM   1729 O OD2 . ASP A 1 234 ? -130.740 26.283 -53.031 1.00 57.50 ? 234  ASP A OD2 1 
ATOM   1730 N N   . LYS A 1 235 ? -128.384 21.758 -52.664 1.00 49.85 ? 235  LYS A N   1 
ATOM   1731 C CA  . LYS A 1 235 ? -127.756 20.533 -53.141 1.00 49.72 ? 235  LYS A CA  1 
ATOM   1732 C C   . LYS A 1 235 ? -127.657 19.533 -51.998 1.00 48.60 ? 235  LYS A C   1 
ATOM   1733 O O   . LYS A 1 235 ? -128.069 18.381 -52.129 1.00 48.26 ? 235  LYS A O   1 
ATOM   1734 C CB  . LYS A 1 235 ? -126.353 20.841 -53.681 1.00 50.68 ? 235  LYS A CB  1 
ATOM   1735 C CG  . LYS A 1 235 ? -126.050 20.249 -55.052 1.00 52.57 ? 235  LYS A CG  1 
ATOM   1736 C CD  . LYS A 1 235 ? -125.982 18.727 -55.039 1.00 51.81 ? 235  LYS A CD  1 
ATOM   1737 C CE  . LYS A 1 235 ? -125.824 18.182 -56.455 1.00 53.02 ? 235  LYS A CE  1 
ATOM   1738 N NZ  . LYS A 1 235 ? -125.635 16.701 -56.502 1.00 52.76 ? 235  LYS A NZ  1 
ATOM   1739 N N   . LEU A 1 236 ? -127.110 19.984 -50.873 1.00 47.52 ? 236  LEU A N   1 
ATOM   1740 C CA  . LEU A 1 236 ? -126.965 19.119 -49.714 1.00 48.09 ? 236  LEU A CA  1 
ATOM   1741 C C   . LEU A 1 236 ? -128.309 18.536 -49.290 1.00 48.69 ? 236  LEU A C   1 
ATOM   1742 O O   . LEU A 1 236 ? -128.380 17.391 -48.837 1.00 49.48 ? 236  LEU A O   1 
ATOM   1743 C CB  . LEU A 1 236 ? -126.335 19.888 -48.550 1.00 46.54 ? 236  LEU A CB  1 
ATOM   1744 C CG  . LEU A 1 236 ? -124.835 20.185 -48.668 1.00 45.81 ? 236  LEU A CG  1 
ATOM   1745 C CD1 . LEU A 1 236 ? -124.399 21.121 -47.556 1.00 42.61 ? 236  LEU A CD1 1 
ATOM   1746 C CD2 . LEU A 1 236 ? -124.059 18.878 -48.609 1.00 42.91 ? 236  LEU A CD2 1 
ATOM   1747 N N   . LEU A 1 237 ? -129.379 19.311 -49.436 1.00 49.04 ? 237  LEU A N   1 
ATOM   1748 C CA  . LEU A 1 237 ? -130.697 18.808 -49.061 1.00 50.31 ? 237  LEU A CA  1 
ATOM   1749 C C   . LEU A 1 237 ? -131.098 17.689 -50.003 1.00 51.10 ? 237  LEU A C   1 
ATOM   1750 O O   . LEU A 1 237 ? -131.469 16.603 -49.568 1.00 51.94 ? 237  LEU A O   1 
ATOM   1751 C CB  . LEU A 1 237 ? -131.745 19.921 -49.103 1.00 48.42 ? 237  LEU A CB  1 
ATOM   1752 C CG  . LEU A 1 237 ? -131.738 20.911 -47.933 1.00 48.09 ? 237  LEU A CG  1 
ATOM   1753 C CD1 . LEU A 1 237 ? -132.936 21.826 -48.066 1.00 48.13 ? 237  LEU A CD1 1 
ATOM   1754 C CD2 . LEU A 1 237 ? -131.807 20.169 -46.603 1.00 45.87 ? 237  LEU A CD2 1 
ATOM   1755 N N   . SER A 1 238 ? -131.011 17.961 -51.299 1.00 51.73 ? 238  SER A N   1 
ATOM   1756 C CA  . SER A 1 238 ? -131.348 16.972 -52.309 1.00 52.11 ? 238  SER A CA  1 
ATOM   1757 C C   . SER A 1 238 ? -130.515 15.714 -52.085 1.00 52.44 ? 238  SER A C   1 
ATOM   1758 O O   . SER A 1 238 ? -130.944 14.603 -52.393 1.00 52.91 ? 238  SER A O   1 
ATOM   1759 C CB  . SER A 1 238 ? -131.068 17.538 -53.699 1.00 52.20 ? 238  SER A CB  1 
ATOM   1760 O OG  . SER A 1 238 ? -131.764 18.759 -53.884 1.00 54.21 ? 238  SER A OG  1 
ATOM   1761 N N   . ALA A 1 239 ? -129.319 15.896 -51.539 1.00 51.74 ? 239  ALA A N   1 
ATOM   1762 C CA  . ALA A 1 239 ? -128.433 14.771 -51.275 1.00 51.82 ? 239  ALA A CA  1 
ATOM   1763 C C   . ALA A 1 239 ? -128.920 13.974 -50.071 1.00 52.14 ? 239  ALA A C   1 
ATOM   1764 O O   . ALA A 1 239 ? -128.381 12.916 -49.757 1.00 51.36 ? 239  ALA A O   1 
ATOM   1765 C CB  . ALA A 1 239 ? -127.015 15.266 -51.035 1.00 51.19 ? 239  ALA A CB  1 
ATOM   1766 N N   . GLY A 1 240 ? -129.933 14.497 -49.391 1.00 52.66 ? 240  GLY A N   1 
ATOM   1767 C CA  . GLY A 1 240 ? -130.472 13.808 -48.235 1.00 52.69 ? 240  GLY A CA  1 
ATOM   1768 C C   . GLY A 1 240 ? -129.846 14.227 -46.921 1.00 53.18 ? 240  GLY A C   1 
ATOM   1769 O O   . GLY A 1 240 ? -129.748 13.421 -45.989 1.00 52.88 ? 240  GLY A O   1 
ATOM   1770 N N   . ALA A 1 241 ? -129.420 15.482 -46.834 1.00 53.72 ? 241  ALA A N   1 
ATOM   1771 C CA  . ALA A 1 241 ? -128.812 15.982 -45.606 1.00 54.24 ? 241  ALA A CA  1 
ATOM   1772 C C   . ALA A 1 241 ? -129.882 16.275 -44.562 1.00 54.31 ? 241  ALA A C   1 
ATOM   1773 O O   . ALA A 1 241 ? -130.973 16.733 -44.889 1.00 53.72 ? 241  ALA A O   1 
ATOM   1774 C CB  . ALA A 1 241 ? -128.009 17.249 -45.892 1.00 54.61 ? 241  ALA A CB  1 
ATOM   1775 N N   . THR A 1 242 ? -129.567 16.008 -43.301 1.00 55.93 ? 242  THR A N   1 
ATOM   1776 C CA  . THR A 1 242 ? -130.516 16.254 -42.222 1.00 58.06 ? 242  THR A CA  1 
ATOM   1777 C C   . THR A 1 242 ? -130.725 17.753 -42.057 1.00 59.29 ? 242  THR A C   1 
ATOM   1778 O O   . THR A 1 242 ? -131.818 18.272 -42.275 1.00 60.06 ? 242  THR A O   1 
ATOM   1779 C CB  . THR A 1 242 ? -130.001 15.673 -40.892 1.00 57.52 ? 242  THR A CB  1 
ATOM   1780 O OG1 . THR A 1 242 ? -129.805 14.262 -41.039 1.00 61.63 ? 242  THR A OG1 1 
ATOM   1781 C CG2 . THR A 1 242 ? -130.993 15.925 -39.771 1.00 58.04 ? 242  THR A CG2 1 
ATOM   1782 N N   . ARG A 1 243 ? -129.654 18.443 -41.684 1.00 60.15 ? 243  ARG A N   1 
ATOM   1783 C CA  . ARG A 1 243 ? -129.685 19.884 -41.471 1.00 58.80 ? 243  ARG A CA  1 
ATOM   1784 C C   . ARG A 1 243 ? -128.380 20.470 -41.991 1.00 57.25 ? 243  ARG A C   1 
ATOM   1785 O O   . ARG A 1 243 ? -127.310 19.899 -41.776 1.00 57.35 ? 243  ARG A O   1 
ATOM   1786 C CB  . ARG A 1 243 ? -129.829 20.182 -39.979 1.00 58.96 ? 243  ARG A CB  1 
ATOM   1787 C CG  . ARG A 1 243 ? -131.012 19.497 -39.338 1.00 61.20 ? 243  ARG A CG  1 
ATOM   1788 C CD  . ARG A 1 243 ? -131.156 19.894 -37.884 1.00 62.10 ? 243  ARG A CD  1 
ATOM   1789 N NE  . ARG A 1 243 ? -129.944 19.619 -37.119 1.00 64.32 ? 243  ARG A NE  1 
ATOM   1790 C CZ  . ARG A 1 243 ? -129.843 19.774 -35.802 1.00 65.15 ? 243  ARG A CZ  1 
ATOM   1791 N NH1 . ARG A 1 243 ? -130.888 20.201 -35.103 1.00 66.71 ? 243  ARG A NH1 1 
ATOM   1792 N NH2 . ARG A 1 243 ? -128.699 19.503 -35.184 1.00 63.64 ? 243  ARG A NH2 1 
ATOM   1793 N N   . VAL A 1 244 ? -128.474 21.605 -42.671 1.00 56.09 ? 244  VAL A N   1 
ATOM   1794 C CA  . VAL A 1 244 ? -127.304 22.253 -43.227 1.00 55.17 ? 244  VAL A CA  1 
ATOM   1795 C C   . VAL A 1 244 ? -126.967 23.583 -42.564 1.00 53.99 ? 244  VAL A C   1 
ATOM   1796 O O   . VAL A 1 244 ? -127.751 24.534 -42.610 1.00 53.37 ? 244  VAL A O   1 
ATOM   1797 C CB  . VAL A 1 244 ? -127.485 22.495 -44.751 1.00 56.14 ? 244  VAL A CB  1 
ATOM   1798 C CG1 . VAL A 1 244 ? -128.790 23.221 -44.997 1.00 57.65 ? 244  VAL A CG1 1 
ATOM   1799 C CG2 . VAL A 1 244 ? -126.317 23.310 -45.296 1.00 56.74 ? 244  VAL A CG2 1 
ATOM   1800 N N   . TYR A 1 245 ? -125.797 23.635 -41.938 1.00 51.80 ? 245  TYR A N   1 
ATOM   1801 C CA  . TYR A 1 245 ? -125.324 24.856 -41.301 1.00 50.05 ? 245  TYR A CA  1 
ATOM   1802 C C   . TYR A 1 245 ? -124.302 25.491 -42.250 1.00 48.76 ? 245  TYR A C   1 
ATOM   1803 O O   . TYR A 1 245 ? -123.863 24.869 -43.220 1.00 47.12 ? 245  TYR A O   1 
ATOM   1804 C CB  . TYR A 1 245 ? -124.650 24.561 -39.950 1.00 49.51 ? 245  TYR A CB  1 
ATOM   1805 C CG  . TYR A 1 245 ? -125.569 23.993 -38.890 1.00 50.40 ? 245  TYR A CG  1 
ATOM   1806 C CD1 . TYR A 1 245 ? -126.199 22.761 -39.078 1.00 50.77 ? 245  TYR A CD1 1 
ATOM   1807 C CD2 . TYR A 1 245 ? -125.802 24.679 -37.698 1.00 50.54 ? 245  TYR A CD2 1 
ATOM   1808 C CE1 . TYR A 1 245 ? -127.039 22.221 -38.110 1.00 50.80 ? 245  TYR A CE1 1 
ATOM   1809 C CE2 . TYR A 1 245 ? -126.645 24.151 -36.716 1.00 50.88 ? 245  TYR A CE2 1 
ATOM   1810 C CZ  . TYR A 1 245 ? -127.263 22.917 -36.932 1.00 51.04 ? 245  TYR A CZ  1 
ATOM   1811 O OH  . TYR A 1 245 ? -128.122 22.390 -35.995 1.00 50.71 ? 245  TYR A OH  1 
ATOM   1812 N N   . ALA A 1 246 ? -123.938 26.734 -41.969 1.00 46.90 ? 246  ALA A N   1 
ATOM   1813 C CA  . ALA A 1 246 ? -122.969 27.448 -42.782 1.00 45.29 ? 246  ALA A CA  1 
ATOM   1814 C C   . ALA A 1 246 ? -122.093 28.268 -41.845 1.00 44.22 ? 246  ALA A C   1 
ATOM   1815 O O   . ALA A 1 246 ? -122.577 29.179 -41.173 1.00 42.41 ? 246  ALA A O   1 
ATOM   1816 C CB  . ALA A 1 246 ? -123.684 28.347 -43.776 1.00 44.84 ? 246  ALA A CB  1 
ATOM   1817 N N   . ILE A 1 247 ? -120.809 27.925 -41.784 1.00 43.18 ? 247  ILE A N   1 
ATOM   1818 C CA  . ILE A 1 247 ? -119.879 28.634 -40.920 1.00 42.99 ? 247  ILE A CA  1 
ATOM   1819 C C   . ILE A 1 247 ? -118.820 29.378 -41.729 1.00 43.48 ? 247  ILE A C   1 
ATOM   1820 O O   . ILE A 1 247 ? -118.086 28.781 -42.515 1.00 43.20 ? 247  ILE A O   1 
ATOM   1821 C CB  . ILE A 1 247 ? -119.183 27.667 -39.946 1.00 41.75 ? 247  ILE A CB  1 
ATOM   1822 C CG1 . ILE A 1 247 ? -120.237 26.954 -39.100 1.00 40.36 ? 247  ILE A CG1 1 
ATOM   1823 C CG2 . ILE A 1 247 ? -118.197 28.431 -39.066 1.00 40.62 ? 247  ILE A CG2 1 
ATOM   1824 C CD1 . ILE A 1 247 ? -119.666 26.058 -38.015 1.00 42.40 ? 247  ILE A CD1 1 
ATOM   1825 N N   . LEU A 1 248 ? -118.751 30.688 -41.522 1.00 44.09 ? 248  LEU A N   1 
ATOM   1826 C CA  . LEU A 1 248 ? -117.800 31.539 -42.228 1.00 44.72 ? 248  LEU A CA  1 
ATOM   1827 C C   . LEU A 1 248 ? -117.042 32.381 -41.215 1.00 45.42 ? 248  LEU A C   1 
ATOM   1828 O O   . LEU A 1 248 ? -117.597 32.774 -40.190 1.00 45.93 ? 248  LEU A O   1 
ATOM   1829 C CB  . LEU A 1 248 ? -118.544 32.482 -43.169 1.00 45.30 ? 248  LEU A CB  1 
ATOM   1830 C CG  . LEU A 1 248 ? -119.672 31.885 -44.010 1.00 46.05 ? 248  LEU A CG  1 
ATOM   1831 C CD1 . LEU A 1 248 ? -120.672 32.980 -44.317 1.00 46.80 ? 248  LEU A CD1 1 
ATOM   1832 C CD2 . LEU A 1 248 ? -119.119 31.257 -45.281 1.00 45.33 ? 248  LEU A CD2 1 
ATOM   1833 N N   . THR A 1 249 ? -115.774 32.657 -41.483 1.00 43.71 ? 249  THR A N   1 
ATOM   1834 C CA  . THR A 1 249 ? -115.030 33.491 -40.562 1.00 43.47 ? 249  THR A CA  1 
ATOM   1835 C C   . THR A 1 249 ? -115.289 34.948 -40.947 1.00 42.29 ? 249  THR A C   1 
ATOM   1836 O O   . THR A 1 249 ? -115.574 35.787 -40.093 1.00 39.43 ? 249  THR A O   1 
ATOM   1837 C CB  . THR A 1 249 ? -113.517 33.169 -40.589 1.00 44.78 ? 249  THR A CB  1 
ATOM   1838 O OG1 . THR A 1 249 ? -112.766 34.360 -40.316 1.00 47.36 ? 249  THR A OG1 1 
ATOM   1839 C CG2 . THR A 1 249 ? -113.113 32.591 -41.920 1.00 48.76 ? 249  THR A CG2 1 
ATOM   1840 N N   . HIS A 1 250 ? -115.233 35.232 -42.242 1.00 41.41 ? 250  HIS A N   1 
ATOM   1841 C CA  . HIS A 1 250 ? -115.469 36.581 -42.738 1.00 41.70 ? 250  HIS A CA  1 
ATOM   1842 C C   . HIS A 1 250 ? -116.834 36.632 -43.411 1.00 43.09 ? 250  HIS A C   1 
ATOM   1843 O O   . HIS A 1 250 ? -117.056 35.965 -44.429 1.00 42.34 ? 250  HIS A O   1 
ATOM   1844 C CB  . HIS A 1 250 ? -114.393 36.972 -43.757 1.00 39.79 ? 250  HIS A CB  1 
ATOM   1845 C CG  . HIS A 1 250 ? -112.994 36.739 -43.281 1.00 36.20 ? 250  HIS A CG  1 
ATOM   1846 N ND1 . HIS A 1 250 ? -112.462 37.388 -42.191 1.00 36.49 ? 250  HIS A ND1 1 
ATOM   1847 C CD2 . HIS A 1 250 ? -112.030 35.905 -43.736 1.00 36.08 ? 250  HIS A CD2 1 
ATOM   1848 C CE1 . HIS A 1 250 ? -111.224 36.961 -41.990 1.00 36.51 ? 250  HIS A CE1 1 
ATOM   1849 N NE2 . HIS A 1 250 ? -110.940 36.062 -42.912 1.00 36.12 ? 250  HIS A NE2 1 
ATOM   1850 N N   . GLY A 1 251 ? -117.737 37.426 -42.843 1.00 44.49 ? 251  GLY A N   1 
ATOM   1851 C CA  . GLY A 1 251 ? -119.074 37.556 -43.397 1.00 47.87 ? 251  GLY A CA  1 
ATOM   1852 C C   . GLY A 1 251 ? -119.274 38.867 -44.133 1.00 50.88 ? 251  GLY A C   1 
ATOM   1853 O O   . GLY A 1 251 ? -119.793 39.832 -43.571 1.00 49.99 ? 251  GLY A O   1 
ATOM   1854 N N   . ILE A 1 252 ? -118.857 38.898 -45.397 1.00 53.75 ? 252  ILE A N   1 
ATOM   1855 C CA  . ILE A 1 252 ? -118.970 40.088 -46.238 1.00 57.53 ? 252  ILE A CA  1 
ATOM   1856 C C   . ILE A 1 252 ? -120.384 40.198 -46.801 1.00 59.79 ? 252  ILE A C   1 
ATOM   1857 O O   . ILE A 1 252 ? -120.593 40.720 -47.896 1.00 62.33 ? 252  ILE A O   1 
ATOM   1858 C CB  . ILE A 1 252 ? -117.977 40.019 -47.423 1.00 57.15 ? 252  ILE A CB  1 
ATOM   1859 C CG1 . ILE A 1 252 ? -116.581 39.657 -46.915 1.00 56.73 ? 252  ILE A CG1 1 
ATOM   1860 C CG2 . ILE A 1 252 ? -117.930 41.357 -48.152 1.00 56.65 ? 252  ILE A CG2 1 
ATOM   1861 C CD1 . ILE A 1 252 ? -115.572 39.433 -48.024 1.00 57.41 ? 252  ILE A CD1 1 
ATOM   1862 N N   . PHE A 1 253 ? -121.352 39.695 -46.048 1.00 61.22 ? 253  PHE A N   1 
ATOM   1863 C CA  . PHE A 1 253 ? -122.748 39.716 -46.466 1.00 62.21 ? 253  PHE A CA  1 
ATOM   1864 C C   . PHE A 1 253 ? -123.118 41.005 -47.198 1.00 62.64 ? 253  PHE A C   1 
ATOM   1865 O O   . PHE A 1 253 ? -123.146 42.086 -46.608 1.00 64.72 ? 253  PHE A O   1 
ATOM   1866 C CB  . PHE A 1 253 ? -123.637 39.535 -45.240 1.00 59.53 ? 253  PHE A CB  1 
ATOM   1867 C CG  . PHE A 1 253 ? -123.370 38.273 -44.480 1.00 58.49 ? 253  PHE A CG  1 
ATOM   1868 C CD1 . PHE A 1 253 ? -123.454 38.255 -43.093 1.00 58.96 ? 253  PHE A CD1 1 
ATOM   1869 C CD2 . PHE A 1 253 ? -123.052 37.098 -45.147 1.00 57.51 ? 253  PHE A CD2 1 
ATOM   1870 C CE1 . PHE A 1 253 ? -123.224 37.082 -42.381 1.00 58.87 ? 253  PHE A CE1 1 
ATOM   1871 C CE2 . PHE A 1 253 ? -122.822 35.921 -44.448 1.00 58.10 ? 253  PHE A CE2 1 
ATOM   1872 C CZ  . PHE A 1 253 ? -122.907 35.911 -43.064 1.00 58.89 ? 253  PHE A CZ  1 
ATOM   1873 N N   . SER A 1 254 ? -123.395 40.884 -48.488 1.00 63.00 ? 254  SER A N   1 
ATOM   1874 C CA  . SER A 1 254 ? -123.754 42.040 -49.297 1.00 64.41 ? 254  SER A CA  1 
ATOM   1875 C C   . SER A 1 254 ? -124.770 41.652 -50.355 1.00 65.19 ? 254  SER A C   1 
ATOM   1876 O O   . SER A 1 254 ? -124.924 40.473 -50.675 1.00 65.04 ? 254  SER A O   1 
ATOM   1877 C CB  . SER A 1 254 ? -122.515 42.602 -49.986 1.00 65.16 ? 254  SER A CB  1 
ATOM   1878 O OG  . SER A 1 254 ? -122.022 41.684 -50.947 1.00 64.94 ? 254  SER A OG  1 
ATOM   1879 N N   . GLY A 1 255 ? -125.451 42.651 -50.905 1.00 65.51 ? 255  GLY A N   1 
ATOM   1880 C CA  . GLY A 1 255 ? -126.444 42.389 -51.928 1.00 66.74 ? 255  GLY A CA  1 
ATOM   1881 C C   . GLY A 1 255 ? -127.592 41.536 -51.422 1.00 68.33 ? 255  GLY A C   1 
ATOM   1882 O O   . GLY A 1 255 ? -128.221 41.873 -50.415 1.00 68.09 ? 255  GLY A O   1 
ATOM   1883 N N   . PRO A 1 256 ? -127.888 40.416 -52.105 1.00 68.74 ? 256  PRO A N   1 
ATOM   1884 C CA  . PRO A 1 256 ? -128.966 39.485 -51.752 1.00 69.63 ? 256  PRO A CA  1 
ATOM   1885 C C   . PRO A 1 256 ? -128.733 38.761 -50.428 1.00 71.10 ? 256  PRO A C   1 
ATOM   1886 O O   . PRO A 1 256 ? -129.682 38.368 -49.750 1.00 70.00 ? 256  PRO A O   1 
ATOM   1887 C CB  . PRO A 1 256 ? -128.981 38.513 -52.930 1.00 69.61 ? 256  PRO A CB  1 
ATOM   1888 C CG  . PRO A 1 256 ? -128.411 39.322 -54.061 1.00 69.80 ? 256  PRO A CG  1 
ATOM   1889 C CD  . PRO A 1 256 ? -127.280 40.038 -53.391 1.00 68.63 ? 256  PRO A CD  1 
ATOM   1890 N N   . ALA A 1 257 ? -127.460 38.592 -50.080 1.00 72.59 ? 257  ALA A N   1 
ATOM   1891 C CA  . ALA A 1 257 ? -127.037 37.906 -48.860 1.00 73.54 ? 257  ALA A CA  1 
ATOM   1892 C C   . ALA A 1 257 ? -128.102 37.777 -47.774 1.00 74.32 ? 257  ALA A C   1 
ATOM   1893 O O   . ALA A 1 257 ? -128.579 36.677 -47.493 1.00 75.92 ? 257  ALA A O   1 
ATOM   1894 C CB  . ALA A 1 257 ? -125.801 38.593 -48.288 1.00 74.45 ? 257  ALA A CB  1 
ATOM   1895 N N   . ILE A 1 258 ? -128.467 38.903 -47.168 1.00 75.27 ? 258  ILE A N   1 
ATOM   1896 C CA  . ILE A 1 258 ? -129.460 38.937 -46.095 1.00 76.28 ? 258  ILE A CA  1 
ATOM   1897 C C   . ILE A 1 258 ? -130.730 38.145 -46.379 1.00 77.26 ? 258  ILE A C   1 
ATOM   1898 O O   . ILE A 1 258 ? -131.150 37.311 -45.581 1.00 77.29 ? 258  ILE A O   1 
ATOM   1899 C CB  . ILE A 1 258 ? -129.915 40.369 -45.799 1.00 78.56 ? 258  ILE A CB  1 
ATOM   1900 C CG1 . ILE A 1 258 ? -128.714 41.252 -45.468 1.00 80.37 ? 258  ILE A CG1 1 
ATOM   1901 C CG2 . ILE A 1 258 ? -130.949 40.344 -44.689 1.00 77.27 ? 258  ILE A CG2 1 
ATOM   1902 C CD1 . ILE A 1 258 ? -129.054 42.710 -45.158 1.00 80.86 ? 258  ILE A CD1 1 
ATOM   1903 N N   . SER A 1 259 ? -131.359 38.444 -47.507 1.00 77.67 ? 259  SER A N   1 
ATOM   1904 C CA  . SER A 1 259 ? -132.591 37.769 -47.877 1.00 78.00 ? 259  SER A CA  1 
ATOM   1905 C C   . SER A 1 259 ? -132.312 36.324 -48.259 1.00 77.31 ? 259  SER A C   1 
ATOM   1906 O O   . SER A 1 259 ? -133.067 35.424 -47.898 1.00 77.92 ? 259  SER A O   1 
ATOM   1907 C CB  . SER A 1 259 ? -133.271 38.500 -49.044 1.00 78.53 ? 259  SER A CB  1 
ATOM   1908 O OG  . SER A 1 259 ? -132.468 38.478 -50.214 1.00 77.91 ? 259  SER A OG  1 
ATOM   1909 N N   . ARG A 1 260 ? -131.214 36.105 -48.973 1.00 77.03 ? 260  ARG A N   1 
ATOM   1910 C CA  . ARG A 1 260 ? -130.852 34.767 -49.416 1.00 75.76 ? 260  ARG A CA  1 
ATOM   1911 C C   . ARG A 1 260 ? -130.727 33.726 -48.312 1.00 75.58 ? 260  ARG A C   1 
ATOM   1912 O O   . ARG A 1 260 ? -131.280 32.633 -48.436 1.00 74.93 ? 260  ARG A O   1 
ATOM   1913 C CB  . ARG A 1 260 ? -129.556 34.806 -50.229 1.00 73.52 ? 260  ARG A CB  1 
ATOM   1914 C CG  . ARG A 1 260 ? -129.732 35.320 -51.643 1.00 70.17 ? 260  ARG A CG  1 
ATOM   1915 C CD  . ARG A 1 260 ? -128.431 35.232 -52.414 1.00 69.41 ? 260  ARG A CD  1 
ATOM   1916 N NE  . ARG A 1 260 ? -128.598 35.580 -53.820 1.00 68.03 ? 260  ARG A NE  1 
ATOM   1917 C CZ  . ARG A 1 260 ? -127.600 35.637 -54.695 1.00 68.19 ? 260  ARG A CZ  1 
ATOM   1918 N NH1 . ARG A 1 260 ? -126.361 35.372 -54.305 1.00 67.33 ? 260  ARG A NH1 1 
ATOM   1919 N NH2 . ARG A 1 260 ? -127.838 35.955 -55.961 1.00 68.67 ? 260  ARG A NH2 1 
ATOM   1920 N N   . ILE A 1 261 ? -130.011 34.045 -47.235 1.00 75.93 ? 261  ILE A N   1 
ATOM   1921 C CA  . ILE A 1 261 ? -129.857 33.063 -46.168 1.00 76.75 ? 261  ILE A CA  1 
ATOM   1922 C C   . ILE A 1 261 ? -131.173 32.827 -45.439 1.00 76.97 ? 261  ILE A C   1 
ATOM   1923 O O   . ILE A 1 261 ? -131.404 31.744 -44.904 1.00 77.52 ? 261  ILE A O   1 
ATOM   1924 C CB  . ILE A 1 261 ? -128.764 33.458 -45.133 1.00 76.71 ? 261  ILE A CB  1 
ATOM   1925 C CG1 . ILE A 1 261 ? -129.311 34.472 -44.130 1.00 77.33 ? 261  ILE A CG1 1 
ATOM   1926 C CG2 . ILE A 1 261 ? -127.539 34.004 -45.857 1.00 76.15 ? 261  ILE A CG2 1 
ATOM   1927 C CD1 . ILE A 1 261 ? -129.256 35.893 -44.596 1.00 79.40 ? 261  ILE A CD1 1 
ATOM   1928 N N   . ASN A 1 262 ? -132.035 33.838 -45.415 1.00 77.29 ? 262  ASN A N   1 
ATOM   1929 C CA  . ASN A 1 262 ? -133.329 33.683 -44.761 1.00 77.33 ? 262  ASN A CA  1 
ATOM   1930 C C   . ASN A 1 262 ? -134.159 32.708 -45.586 1.00 76.84 ? 262  ASN A C   1 
ATOM   1931 O O   . ASN A 1 262 ? -134.716 31.748 -45.056 1.00 77.19 ? 262  ASN A O   1 
ATOM   1932 C CB  . ASN A 1 262 ? -134.061 35.023 -44.661 1.00 77.16 ? 262  ASN A CB  1 
ATOM   1933 C CG  . ASN A 1 262 ? -133.360 36.004 -43.741 1.00 77.81 ? 262  ASN A CG  1 
ATOM   1934 O OD1 . ASN A 1 262 ? -132.900 35.639 -42.658 1.00 77.34 ? 262  ASN A OD1 1 
ATOM   1935 N ND2 . ASN A 1 262 ? -133.292 37.261 -44.162 1.00 77.70 ? 262  ASN A ND2 1 
ATOM   1936 N N   . ASN A 1 263 ? -134.225 32.960 -46.891 1.00 75.85 ? 263  ASN A N   1 
ATOM   1937 C CA  . ASN A 1 263 ? -134.977 32.107 -47.803 1.00 75.00 ? 263  ASN A CA  1 
ATOM   1938 C C   . ASN A 1 263 ? -134.263 30.771 -48.010 1.00 73.56 ? 263  ASN A C   1 
ATOM   1939 O O   . ASN A 1 263 ? -134.736 29.918 -48.755 1.00 74.17 ? 263  ASN A O   1 
ATOM   1940 C CB  . ASN A 1 263 ? -135.153 32.798 -49.158 1.00 76.33 ? 263  ASN A CB  1 
ATOM   1941 C CG  . ASN A 1 263 ? -135.709 34.201 -49.032 1.00 77.16 ? 263  ASN A CG  1 
ATOM   1942 O OD1 . ASN A 1 263 ? -136.769 34.414 -48.445 1.00 78.31 ? 263  ASN A OD1 1 
ATOM   1943 N ND2 . ASN A 1 263 ? -134.994 35.170 -49.593 1.00 78.02 ? 263  ASN A ND2 1 
ATOM   1944 N N   . ALA A 1 264 ? -133.120 30.599 -47.354 1.00 71.03 ? 264  ALA A N   1 
ATOM   1945 C CA  . ALA A 1 264 ? -132.345 29.364 -47.463 1.00 68.21 ? 264  ALA A CA  1 
ATOM   1946 C C   . ALA A 1 264 ? -132.613 28.492 -46.243 1.00 66.23 ? 264  ALA A C   1 
ATOM   1947 O O   . ALA A 1 264 ? -132.776 29.000 -45.137 1.00 66.07 ? 264  ALA A O   1 
ATOM   1948 C CB  . ALA A 1 264 ? -130.871 29.689 -47.564 1.00 69.43 ? 264  ALA A CB  1 
ATOM   1949 N N   . CYS A 1 265 ? -132.638 27.182 -46.445 1.00 63.33 ? 265  CYS A N   1 
ATOM   1950 C CA  . CYS A 1 265 ? -132.899 26.234 -45.369 1.00 60.87 ? 265  CYS A CA  1 
ATOM   1951 C C   . CYS A 1 265 ? -131.816 26.181 -44.292 1.00 58.01 ? 265  CYS A C   1 
ATOM   1952 O O   . CYS A 1 265 ? -131.758 25.210 -43.533 1.00 58.59 ? 265  CYS A O   1 
ATOM   1953 C CB  . CYS A 1 265 ? -133.037 24.840 -45.944 1.00 62.56 ? 265  CYS A CB  1 
ATOM   1954 S SG  . CYS A 1 265 ? -131.457 24.216 -46.504 1.00 67.38 ? 265  CYS A SG  1 
ATOM   1955 N N   . PHE A 1 266 ? -130.972 27.201 -44.204 1.00 54.11 ? 266  PHE A N   1 
ATOM   1956 C CA  . PHE A 1 266 ? -129.915 27.190 -43.202 1.00 51.17 ? 266  PHE A CA  1 
ATOM   1957 C C   . PHE A 1 266 ? -130.452 27.105 -41.782 1.00 50.88 ? 266  PHE A C   1 
ATOM   1958 O O   . PHE A 1 266 ? -131.211 27.964 -41.341 1.00 51.29 ? 266  PHE A O   1 
ATOM   1959 C CB  . PHE A 1 266 ? -129.032 28.445 -43.309 1.00 49.30 ? 266  PHE A CB  1 
ATOM   1960 C CG  . PHE A 1 266 ? -128.154 28.474 -44.517 1.00 45.39 ? 266  PHE A CG  1 
ATOM   1961 C CD1 . PHE A 1 266 ? -128.303 29.466 -45.469 1.00 43.70 ? 266  PHE A CD1 1 
ATOM   1962 C CD2 . PHE A 1 266 ? -127.176 27.503 -44.701 1.00 45.23 ? 266  PHE A CD2 1 
ATOM   1963 C CE1 . PHE A 1 266 ? -127.488 29.493 -46.596 1.00 44.58 ? 266  PHE A CE1 1 
ATOM   1964 C CE2 . PHE A 1 266 ? -126.358 27.523 -45.822 1.00 44.95 ? 266  PHE A CE2 1 
ATOM   1965 C CZ  . PHE A 1 266 ? -126.515 28.519 -46.771 1.00 43.23 ? 266  PHE A CZ  1 
ATOM   1966 N N   . GLU A 1 267 ? -130.048 26.075 -41.055 1.00 49.96 ? 267  GLU A N   1 
ATOM   1967 C CA  . GLU A 1 267 ? -130.475 25.926 -39.675 1.00 49.45 ? 267  GLU A CA  1 
ATOM   1968 C C   . GLU A 1 267 ? -129.963 27.178 -38.955 1.00 49.11 ? 267  GLU A C   1 
ATOM   1969 O O   . GLU A 1 267 ? -130.651 27.781 -38.135 1.00 50.49 ? 267  GLU A O   1 
ATOM   1970 C CB  . GLU A 1 267 ? -129.834 24.668 -39.084 1.00 50.63 ? 267  GLU A CB  1 
ATOM   1971 C CG  . GLU A 1 267 ? -130.020 24.495 -37.584 1.00 53.43 ? 267  GLU A CG  1 
ATOM   1972 C CD  . GLU A 1 267 ? -131.472 24.549 -37.160 1.00 55.43 ? 267  GLU A CD  1 
ATOM   1973 O OE1 . GLU A 1 267 ? -132.323 23.954 -37.860 1.00 55.48 ? 267  GLU A OE1 1 
ATOM   1974 O OE2 . GLU A 1 267 ? -131.758 25.176 -36.115 1.00 57.57 ? 267  GLU A OE2 1 
ATOM   1975 N N   . ALA A 1 268 ? -128.739 27.560 -39.303 1.00 46.11 ? 268  ALA A N   1 
ATOM   1976 C CA  . ALA A 1 268 ? -128.070 28.710 -38.724 1.00 43.80 ? 268  ALA A CA  1 
ATOM   1977 C C   . ALA A 1 268 ? -126.834 29.073 -39.551 1.00 42.78 ? 268  ALA A C   1 
ATOM   1978 O O   . ALA A 1 268 ? -126.280 28.229 -40.258 1.00 39.97 ? 268  ALA A O   1 
ATOM   1979 C CB  . ALA A 1 268 ? -127.656 28.392 -37.303 1.00 43.68 ? 268  ALA A CB  1 
ATOM   1980 N N   . VAL A 1 269 ? -126.418 30.334 -39.469 1.00 41.73 ? 269  VAL A N   1 
ATOM   1981 C CA  . VAL A 1 269 ? -125.241 30.812 -40.181 1.00 40.85 ? 269  VAL A CA  1 
ATOM   1982 C C   . VAL A 1 269 ? -124.327 31.496 -39.172 1.00 40.77 ? 269  VAL A C   1 
ATOM   1983 O O   . VAL A 1 269 ? -124.680 32.527 -38.593 1.00 41.65 ? 269  VAL A O   1 
ATOM   1984 C CB  . VAL A 1 269 ? -125.621 31.800 -41.277 1.00 40.72 ? 269  VAL A CB  1 
ATOM   1985 C CG1 . VAL A 1 269 ? -124.361 32.271 -42.011 1.00 41.27 ? 269  VAL A CG1 1 
ATOM   1986 C CG2 . VAL A 1 269 ? -126.591 31.138 -42.238 1.00 41.75 ? 269  VAL A CG2 1 
ATOM   1987 N N   . VAL A 1 270 ? -123.158 30.912 -38.951 1.00 38.80 ? 270  VAL A N   1 
ATOM   1988 C CA  . VAL A 1 270 ? -122.215 31.457 -37.990 1.00 36.76 ? 270  VAL A CA  1 
ATOM   1989 C C   . VAL A 1 270 ? -121.076 32.212 -38.663 1.00 36.84 ? 270  VAL A C   1 
ATOM   1990 O O   . VAL A 1 270 ? -120.486 31.729 -39.626 1.00 36.97 ? 270  VAL A O   1 
ATOM   1991 C CB  . VAL A 1 270 ? -121.606 30.333 -37.130 1.00 35.55 ? 270  VAL A CB  1 
ATOM   1992 C CG1 . VAL A 1 270 ? -120.880 30.928 -35.943 1.00 35.14 ? 270  VAL A CG1 1 
ATOM   1993 C CG2 . VAL A 1 270 ? -122.686 29.367 -36.689 1.00 33.69 ? 270  VAL A CG2 1 
ATOM   1994 N N   . VAL A 1 271 ? -120.779 33.402 -38.153 1.00 35.33 ? 271  VAL A N   1 
ATOM   1995 C CA  . VAL A 1 271 ? -119.704 34.222 -38.690 1.00 33.75 ? 271  VAL A CA  1 
ATOM   1996 C C   . VAL A 1 271 ? -118.981 34.881 -37.533 1.00 34.59 ? 271  VAL A C   1 
ATOM   1997 O O   . VAL A 1 271 ? -119.489 34.916 -36.404 1.00 32.16 ? 271  VAL A O   1 
ATOM   1998 C CB  . VAL A 1 271 ? -120.224 35.316 -39.646 1.00 34.32 ? 271  VAL A CB  1 
ATOM   1999 C CG1 . VAL A 1 271 ? -120.832 34.672 -40.879 1.00 34.33 ? 271  VAL A CG1 1 
ATOM   2000 C CG2 . VAL A 1 271 ? -121.235 36.192 -38.938 1.00 31.47 ? 271  VAL A CG2 1 
ATOM   2001 N N   . THR A 1 272 ? -117.783 35.384 -37.800 1.00 33.77 ? 272  THR A N   1 
ATOM   2002 C CA  . THR A 1 272 ? -117.019 36.035 -36.753 1.00 35.18 ? 272  THR A CA  1 
ATOM   2003 C C   . THR A 1 272 ? -117.236 37.530 -36.753 1.00 36.21 ? 272  THR A C   1 
ATOM   2004 O O   . THR A 1 272 ? -117.929 38.086 -37.599 1.00 38.25 ? 272  THR A O   1 
ATOM   2005 C CB  . THR A 1 272 ? -115.497 35.804 -36.880 1.00 35.14 ? 272  THR A CB  1 
ATOM   2006 O OG1 . THR A 1 272 ? -114.964 36.673 -37.891 1.00 31.74 ? 272  THR A OG1 1 
ATOM   2007 C CG2 . THR A 1 272 ? -115.196 34.350 -37.227 1.00 37.20 ? 272  THR A CG2 1 
ATOM   2008 N N   . ASN A 1 273 ? -116.597 38.160 -35.787 1.00 36.92 ? 273  ASN A N   1 
ATOM   2009 C CA  . ASN A 1 273 ? -116.652 39.588 -35.572 1.00 39.50 ? 273  ASN A CA  1 
ATOM   2010 C C   . ASN A 1 273 ? -115.702 40.350 -36.501 1.00 38.84 ? 273  ASN A C   1 
ATOM   2011 O O   . ASN A 1 273 ? -115.643 41.570 -36.444 1.00 39.62 ? 273  ASN A O   1 
ATOM   2012 C CB  . ASN A 1 273 ? -116.273 39.852 -34.109 1.00 39.91 ? 273  ASN A CB  1 
ATOM   2013 C CG  . ASN A 1 273 ? -117.239 40.770 -33.420 1.00 45.19 ? 273  ASN A CG  1 
ATOM   2014 O OD1 . ASN A 1 273 ? -118.397 40.882 -33.839 1.00 50.47 ? 273  ASN A OD1 1 
ATOM   2015 N ND2 . ASN A 1 273 ? -116.789 41.426 -32.353 1.00 44.22 ? 273  ASN A ND2 1 
ATOM   2016 N N   . THR A 1 274 ? -114.963 39.645 -37.356 1.00 38.99 ? 274  THR A N   1 
ATOM   2017 C CA  . THR A 1 274 ? -114.008 40.331 -38.232 1.00 41.12 ? 274  THR A CA  1 
ATOM   2018 C C   . THR A 1 274 ? -114.611 41.452 -39.074 1.00 40.64 ? 274  THR A C   1 
ATOM   2019 O O   . THR A 1 274 ? -113.890 42.328 -39.537 1.00 41.93 ? 274  THR A O   1 
ATOM   2020 C CB  . THR A 1 274 ? -113.245 39.354 -39.161 1.00 39.94 ? 274  THR A CB  1 
ATOM   2021 O OG1 . THR A 1 274 ? -114.167 38.677 -40.013 1.00 42.49 ? 274  THR A OG1 1 
ATOM   2022 C CG2 . THR A 1 274 ? -112.469 38.328 -38.339 1.00 40.40 ? 274  THR A CG2 1 
ATOM   2023 N N   . ILE A 1 275 ? -115.926 41.427 -39.262 1.00 42.27 ? 275  ILE A N   1 
ATOM   2024 C CA  . ILE A 1 275 ? -116.627 42.453 -40.028 1.00 43.07 ? 275  ILE A CA  1 
ATOM   2025 C C   . ILE A 1 275 ? -117.909 42.741 -39.257 1.00 44.23 ? 275  ILE A C   1 
ATOM   2026 O O   . ILE A 1 275 ? -118.512 41.826 -38.699 1.00 43.81 ? 275  ILE A O   1 
ATOM   2027 C CB  . ILE A 1 275 ? -116.978 41.953 -41.462 1.00 43.65 ? 275  ILE A CB  1 
ATOM   2028 C CG1 . ILE A 1 275 ? -115.690 41.743 -42.269 1.00 42.74 ? 275  ILE A CG1 1 
ATOM   2029 C CG2 . ILE A 1 275 ? -117.869 42.970 -42.182 1.00 44.08 ? 275  ILE A CG2 1 
ATOM   2030 C CD1 . ILE A 1 275 ? -115.945 41.218 -43.659 1.00 43.94 ? 275  ILE A CD1 1 
ATOM   2031 N N   . PRO A 1 276 ? -118.318 44.020 -39.182 1.00 46.52 ? 276  PRO A N   1 
ATOM   2032 C CA  . PRO A 1 276 ? -119.527 44.454 -38.470 1.00 48.98 ? 276  PRO A CA  1 
ATOM   2033 C C   . PRO A 1 276 ? -120.743 43.636 -38.902 1.00 50.73 ? 276  PRO A C   1 
ATOM   2034 O O   . PRO A 1 276 ? -121.016 43.505 -40.096 1.00 50.17 ? 276  PRO A O   1 
ATOM   2035 C CB  . PRO A 1 276 ? -119.631 45.924 -38.858 1.00 48.19 ? 276  PRO A CB  1 
ATOM   2036 C CG  . PRO A 1 276 ? -118.187 46.319 -38.965 1.00 48.82 ? 276  PRO A CG  1 
ATOM   2037 C CD  . PRO A 1 276 ? -117.623 45.177 -39.773 1.00 47.16 ? 276  PRO A CD  1 
ATOM   2038 N N   . GLN A 1 277 ? -121.464 43.084 -37.930 1.00 54.35 ? 277  GLN A N   1 
ATOM   2039 C CA  . GLN A 1 277 ? -122.636 42.263 -38.229 1.00 58.93 ? 277  GLN A CA  1 
ATOM   2040 C C   . GLN A 1 277 ? -123.915 42.737 -37.534 1.00 62.37 ? 277  GLN A C   1 
ATOM   2041 O O   . GLN A 1 277 ? -124.990 42.182 -37.770 1.00 63.10 ? 277  GLN A O   1 
ATOM   2042 C CB  . GLN A 1 277 ? -122.362 40.813 -37.823 1.00 57.58 ? 277  GLN A CB  1 
ATOM   2043 C CG  . GLN A 1 277 ? -121.089 40.225 -38.404 1.00 57.37 ? 277  GLN A CG  1 
ATOM   2044 C CD  . GLN A 1 277 ? -121.165 39.990 -39.901 1.00 57.72 ? 277  GLN A CD  1 
ATOM   2045 O OE1 . GLN A 1 277 ? -120.148 39.755 -40.553 1.00 57.79 ? 277  GLN A OE1 1 
ATOM   2046 N NE2 . GLN A 1 277 ? -122.369 40.041 -40.450 1.00 56.91 ? 277  GLN A NE2 1 
ATOM   2047 N N   . GLU A 1 278 ? -123.798 43.749 -36.678 1.00 66.08 ? 278  GLU A N   1 
ATOM   2048 C CA  . GLU A 1 278 ? -124.946 44.278 -35.941 1.00 69.05 ? 278  GLU A CA  1 
ATOM   2049 C C   . GLU A 1 278 ? -126.122 44.676 -36.848 1.00 69.86 ? 278  GLU A C   1 
ATOM   2050 O O   . GLU A 1 278 ? -127.278 44.382 -36.537 1.00 70.00 ? 278  GLU A O   1 
ATOM   2051 C CB  . GLU A 1 278 ? -124.520 45.486 -35.089 1.00 70.61 ? 278  GLU A CB  1 
ATOM   2052 C CG  . GLU A 1 278 ? -123.431 45.205 -34.037 1.00 73.56 ? 278  GLU A CG  1 
ATOM   2053 C CD  . GLU A 1 278 ? -122.028 45.046 -34.628 1.00 75.26 ? 278  GLU A CD  1 
ATOM   2054 O OE1 . GLU A 1 278 ? -121.760 44.023 -35.297 1.00 76.09 ? 278  GLU A OE1 1 
ATOM   2055 O OE2 . GLU A 1 278 ? -121.189 45.953 -34.423 1.00 74.66 ? 278  GLU A OE2 1 
ATOM   2056 N N   . ASP A 1 279 ? -125.822 45.343 -37.961 1.00 71.08 ? 279  ASP A N   1 
ATOM   2057 C CA  . ASP A 1 279 ? -126.848 45.784 -38.908 1.00 72.54 ? 279  ASP A CA  1 
ATOM   2058 C C   . ASP A 1 279 ? -127.575 44.628 -39.590 1.00 73.16 ? 279  ASP A C   1 
ATOM   2059 O O   . ASP A 1 279 ? -128.803 44.641 -39.707 1.00 72.47 ? 279  ASP A O   1 
ATOM   2060 C CB  . ASP A 1 279 ? -126.219 46.696 -39.973 1.00 74.23 ? 279  ASP A CB  1 
ATOM   2061 C CG  . ASP A 1 279 ? -127.155 46.973 -41.149 1.00 75.16 ? 279  ASP A CG  1 
ATOM   2062 O OD1 . ASP A 1 279 ? -127.443 46.031 -41.919 1.00 74.84 ? 279  ASP A OD1 1 
ATOM   2063 O OD2 . ASP A 1 279 ? -127.599 48.135 -41.307 1.00 76.59 ? 279  ASP A OD2 1 
ATOM   2064 N N   . LYS A 1 280 ? -126.817 43.633 -40.037 1.00 73.32 ? 280  LYS A N   1 
ATOM   2065 C CA  . LYS A 1 280 ? -127.394 42.484 -40.718 1.00 73.57 ? 280  LYS A CA  1 
ATOM   2066 C C   . LYS A 1 280 ? -128.083 41.495 -39.779 1.00 73.85 ? 280  LYS A C   1 
ATOM   2067 O O   . LYS A 1 280 ? -129.087 40.888 -40.152 1.00 73.82 ? 280  LYS A O   1 
ATOM   2068 C CB  . LYS A 1 280 ? -126.308 41.778 -41.524 1.00 73.68 ? 280  LYS A CB  1 
ATOM   2069 C CG  . LYS A 1 280 ? -125.509 42.741 -42.384 1.00 73.89 ? 280  LYS A CG  1 
ATOM   2070 C CD  . LYS A 1 280 ? -124.823 42.043 -43.532 1.00 73.17 ? 280  LYS A CD  1 
ATOM   2071 C CE  . LYS A 1 280 ? -125.839 41.432 -44.478 1.00 74.25 ? 280  LYS A CE  1 
ATOM   2072 N NZ  . LYS A 1 280 ? -126.571 40.268 -43.884 1.00 72.66 ? 280  LYS A NZ  1 
ATOM   2073 N N   . MET A 1 281 ? -127.553 41.336 -38.568 1.00 73.74 ? 281  MET A N   1 
ATOM   2074 C CA  . MET A 1 281 ? -128.140 40.417 -37.596 1.00 74.53 ? 281  MET A CA  1 
ATOM   2075 C C   . MET A 1 281 ? -129.591 40.764 -37.279 1.00 75.21 ? 281  MET A C   1 
ATOM   2076 O O   . MET A 1 281 ? -130.381 39.892 -36.918 1.00 74.28 ? 281  MET A O   1 
ATOM   2077 C CB  . MET A 1 281 ? -127.336 40.419 -36.293 1.00 74.81 ? 281  MET A CB  1 
ATOM   2078 C CG  . MET A 1 281 ? -126.023 39.654 -36.347 1.00 74.89 ? 281  MET A CG  1 
ATOM   2079 S SD  . MET A 1 281 ? -125.254 39.542 -34.709 1.00 75.40 ? 281  MET A SD  1 
ATOM   2080 C CE  . MET A 1 281 ? -124.355 41.090 -34.656 1.00 74.65 ? 281  MET A CE  1 
ATOM   2081 N N   . LYS A 1 282 ? -129.936 42.040 -37.406 1.00 76.12 ? 282  LYS A N   1 
ATOM   2082 C CA  . LYS A 1 282 ? -131.292 42.489 -37.131 1.00 77.29 ? 282  LYS A CA  1 
ATOM   2083 C C   . LYS A 1 282 ? -132.295 41.928 -38.136 1.00 77.57 ? 282  LYS A C   1 
ATOM   2084 O O   . LYS A 1 282 ? -133.363 41.450 -37.753 1.00 78.20 ? 282  LYS A O   1 
ATOM   2085 C CB  . LYS A 1 282 ? -131.350 44.019 -37.148 1.00 76.93 ? 282  LYS A CB  1 
ATOM   2086 C CG  . LYS A 1 282 ? -130.452 44.682 -36.118 1.00 77.98 ? 282  LYS A CG  1 
ATOM   2087 C CD  . LYS A 1 282 ? -130.630 46.191 -36.128 1.00 78.77 ? 282  LYS A CD  1 
ATOM   2088 C CE  . LYS A 1 282 ? -129.850 46.834 -34.995 1.00 79.56 ? 282  LYS A CE  1 
ATOM   2089 N NZ  . LYS A 1 282 ? -130.069 48.306 -34.928 1.00 80.18 ? 282  LYS A NZ  1 
ATOM   2090 N N   . HIS A 1 283 ? -131.943 41.977 -39.419 1.00 77.75 ? 283  HIS A N   1 
ATOM   2091 C CA  . HIS A 1 283 ? -132.831 41.494 -40.477 1.00 77.80 ? 283  HIS A CA  1 
ATOM   2092 C C   . HIS A 1 283 ? -132.631 40.019 -40.815 1.00 76.30 ? 283  HIS A C   1 
ATOM   2093 O O   . HIS A 1 283 ? -133.228 39.505 -41.763 1.00 75.84 ? 283  HIS A O   1 
ATOM   2094 C CB  . HIS A 1 283 ? -132.647 42.342 -41.738 1.00 80.94 ? 283  HIS A CB  1 
ATOM   2095 C CG  . HIS A 1 283 ? -133.903 42.519 -42.535 1.00 84.00 ? 283  HIS A CG  1 
ATOM   2096 N ND1 . HIS A 1 283 ? -134.585 41.462 -43.097 1.00 85.18 ? 283  HIS A ND1 1 
ATOM   2097 C CD2 . HIS A 1 283 ? -134.603 43.633 -42.856 1.00 85.03 ? 283  HIS A CD2 1 
ATOM   2098 C CE1 . HIS A 1 283 ? -135.653 41.917 -43.730 1.00 85.95 ? 283  HIS A CE1 1 
ATOM   2099 N NE2 . HIS A 1 283 ? -135.687 43.231 -43.599 1.00 85.99 ? 283  HIS A NE2 1 
ATOM   2100 N N   . CYS A 1 284 ? -131.781 39.349 -40.042 1.00 73.62 ? 284  CYS A N   1 
ATOM   2101 C CA  . CYS A 1 284 ? -131.506 37.924 -40.228 1.00 70.91 ? 284  CYS A CA  1 
ATOM   2102 C C   . CYS A 1 284 ? -131.336 37.294 -38.857 1.00 68.85 ? 284  CYS A C   1 
ATOM   2103 O O   . CYS A 1 284 ? -130.371 37.583 -38.144 1.00 69.37 ? 284  CYS A O   1 
ATOM   2104 C CB  . CYS A 1 284 ? -130.234 37.708 -41.044 1.00 72.13 ? 284  CYS A CB  1 
ATOM   2105 S SG  . CYS A 1 284 ? -129.930 35.965 -41.442 1.00 71.65 ? 284  CYS A SG  1 
ATOM   2106 N N   . SER A 1 285 ? -132.275 36.428 -38.495 1.00 66.26 ? 285  SER A N   1 
ATOM   2107 C CA  . SER A 1 285 ? -132.259 35.767 -37.198 1.00 63.84 ? 285  SER A CA  1 
ATOM   2108 C C   . SER A 1 285 ? -131.373 34.534 -37.074 1.00 62.10 ? 285  SER A C   1 
ATOM   2109 O O   . SER A 1 285 ? -130.806 34.290 -36.008 1.00 62.69 ? 285  SER A O   1 
ATOM   2110 C CB  . SER A 1 285 ? -133.685 35.396 -36.798 1.00 64.58 ? 285  SER A CB  1 
ATOM   2111 O OG  . SER A 1 285 ? -133.704 34.676 -35.578 1.00 65.61 ? 285  SER A OG  1 
ATOM   2112 N N   . LYS A 1 286 ? -131.247 33.756 -38.142 1.00 60.04 ? 286  LYS A N   1 
ATOM   2113 C CA  . LYS A 1 286 ? -130.429 32.550 -38.082 1.00 58.53 ? 286  LYS A CA  1 
ATOM   2114 C C   . LYS A 1 286 ? -128.931 32.838 -38.034 1.00 56.57 ? 286  LYS A C   1 
ATOM   2115 O O   . LYS A 1 286 ? -128.115 31.914 -38.112 1.00 56.60 ? 286  LYS A O   1 
ATOM   2116 C CB  . LYS A 1 286 ? -130.750 31.654 -39.274 1.00 57.53 ? 286  LYS A CB  1 
ATOM   2117 C CG  . LYS A 1 286 ? -130.578 32.339 -40.610 1.00 58.68 ? 286  LYS A CG  1 
ATOM   2118 C CD  . LYS A 1 286 ? -131.058 31.459 -41.755 1.00 58.73 ? 286  LYS A CD  1 
ATOM   2119 C CE  . LYS A 1 286 ? -132.533 31.159 -41.621 1.00 58.19 ? 286  LYS A CE  1 
ATOM   2120 N NZ  . LYS A 1 286 ? -133.018 30.310 -42.734 1.00 60.78 ? 286  LYS A NZ  1 
ATOM   2121 N N   . ILE A 1 287 ? -128.577 34.110 -37.883 1.00 54.03 ? 287  ILE A N   1 
ATOM   2122 C CA  . ILE A 1 287 ? -127.182 34.499 -37.820 1.00 51.03 ? 287  ILE A CA  1 
ATOM   2123 C C   . ILE A 1 287 ? -126.639 34.654 -36.410 1.00 49.36 ? 287  ILE A C   1 
ATOM   2124 O O   . ILE A 1 287 ? -127.211 35.342 -35.566 1.00 49.71 ? 287  ILE A O   1 
ATOM   2125 C CB  . ILE A 1 287 ? -126.931 35.816 -38.576 1.00 51.52 ? 287  ILE A CB  1 
ATOM   2126 C CG1 . ILE A 1 287 ? -127.054 35.571 -40.078 1.00 52.31 ? 287  ILE A CG1 1 
ATOM   2127 C CG2 . ILE A 1 287 ? -125.548 36.371 -38.221 1.00 50.02 ? 287  ILE A CG2 1 
ATOM   2128 C CD1 . ILE A 1 287 ? -126.720 36.776 -40.930 1.00 52.50 ? 287  ILE A CD1 1 
ATOM   2129 N N   . GLN A 1 288 ? -125.509 34.009 -36.176 1.00 46.50 ? 288  GLN A N   1 
ATOM   2130 C CA  . GLN A 1 288 ? -124.844 34.067 -34.893 1.00 46.21 ? 288  GLN A CA  1 
ATOM   2131 C C   . GLN A 1 288 ? -123.409 34.514 -35.137 1.00 44.74 ? 288  GLN A C   1 
ATOM   2132 O O   . GLN A 1 288 ? -122.823 34.182 -36.170 1.00 43.64 ? 288  GLN A O   1 
ATOM   2133 C CB  . GLN A 1 288 ? -124.869 32.692 -34.231 1.00 47.48 ? 288  GLN A CB  1 
ATOM   2134 C CG  . GLN A 1 288 ? -126.247 32.273 -33.757 1.00 50.35 ? 288  GLN A CG  1 
ATOM   2135 C CD  . GLN A 1 288 ? -126.230 30.926 -33.077 1.00 52.74 ? 288  GLN A CD  1 
ATOM   2136 O OE1 . GLN A 1 288 ? -125.472 30.704 -32.127 1.00 53.21 ? 288  GLN A OE1 1 
ATOM   2137 N NE2 . GLN A 1 288 ? -127.072 30.016 -33.551 1.00 52.66 ? 288  GLN A NE2 1 
ATOM   2138 N N   . VAL A 1 289 ? -122.846 35.278 -34.206 1.00 43.49 ? 289  VAL A N   1 
ATOM   2139 C CA  . VAL A 1 289 ? -121.475 35.742 -34.372 1.00 41.80 ? 289  VAL A CA  1 
ATOM   2140 C C   . VAL A 1 289 ? -120.532 35.289 -33.264 1.00 39.85 ? 289  VAL A C   1 
ATOM   2141 O O   . VAL A 1 289 ? -120.862 35.347 -32.081 1.00 40.42 ? 289  VAL A O   1 
ATOM   2142 C CB  . VAL A 1 289 ? -121.389 37.294 -34.440 1.00 41.80 ? 289  VAL A CB  1 
ATOM   2143 C CG1 . VAL A 1 289 ? -122.522 37.855 -35.281 1.00 41.42 ? 289  VAL A CG1 1 
ATOM   2144 C CG2 . VAL A 1 289 ? -121.413 37.874 -33.046 1.00 44.39 ? 289  VAL A CG2 1 
ATOM   2145 N N   . ILE A 1 290 ? -119.357 34.824 -33.657 1.00 37.30 ? 290  ILE A N   1 
ATOM   2146 C CA  . ILE A 1 290 ? -118.356 34.424 -32.692 1.00 35.23 ? 290  ILE A CA  1 
ATOM   2147 C C   . ILE A 1 290 ? -117.463 35.656 -32.575 1.00 34.95 ? 290  ILE A C   1 
ATOM   2148 O O   . ILE A 1 290 ? -116.930 36.129 -33.577 1.00 34.16 ? 290  ILE A O   1 
ATOM   2149 C CB  . ILE A 1 290 ? -117.507 33.253 -33.204 1.00 35.93 ? 290  ILE A CB  1 
ATOM   2150 C CG1 . ILE A 1 290 ? -118.386 32.025 -33.438 1.00 34.80 ? 290  ILE A CG1 1 
ATOM   2151 C CG2 . ILE A 1 290 ? -116.397 32.950 -32.210 1.00 34.10 ? 290  ILE A CG2 1 
ATOM   2152 C CD1 . ILE A 1 290 ? -117.628 30.856 -34.035 1.00 34.78 ? 290  ILE A CD1 1 
ATOM   2153 N N   . ASP A 1 291 ? -117.321 36.182 -31.364 1.00 34.73 ? 291  ASP A N   1 
ATOM   2154 C CA  . ASP A 1 291 ? -116.492 37.362 -31.122 1.00 35.52 ? 291  ASP A CA  1 
ATOM   2155 C C   . ASP A 1 291 ? -115.015 36.973 -31.098 1.00 35.28 ? 291  ASP A C   1 
ATOM   2156 O O   . ASP A 1 291 ? -114.604 36.135 -30.298 1.00 35.32 ? 291  ASP A O   1 
ATOM   2157 C CB  . ASP A 1 291 ? -116.904 38.008 -29.793 1.00 37.66 ? 291  ASP A CB  1 
ATOM   2158 C CG  . ASP A 1 291 ? -116.017 39.184 -29.394 1.00 41.72 ? 291  ASP A CG  1 
ATOM   2159 O OD1 . ASP A 1 291 ? -115.408 39.826 -30.276 1.00 41.02 ? 291  ASP A OD1 1 
ATOM   2160 O OD2 . ASP A 1 291 ? -115.949 39.481 -28.178 1.00 42.96 ? 291  ASP A OD2 1 
ATOM   2161 N N   . ILE A 1 292 ? -114.223 37.563 -31.992 1.00 32.56 ? 292  ILE A N   1 
ATOM   2162 C CA  . ILE A 1 292 ? -112.798 37.266 -32.036 1.00 31.86 ? 292  ILE A CA  1 
ATOM   2163 C C   . ILE A 1 292 ? -111.935 38.411 -31.502 1.00 32.09 ? 292  ILE A C   1 
ATOM   2164 O O   . ILE A 1 292 ? -110.707 38.388 -31.639 1.00 28.56 ? 292  ILE A O   1 
ATOM   2165 C CB  . ILE A 1 292 ? -112.326 36.877 -33.487 1.00 31.65 ? 292  ILE A CB  1 
ATOM   2166 C CG1 . ILE A 1 292 ? -112.914 37.820 -34.546 1.00 29.40 ? 292  ILE A CG1 1 
ATOM   2167 C CG2 . ILE A 1 292 ? -112.732 35.447 -33.789 1.00 30.65 ? 292  ILE A CG2 1 
ATOM   2168 C CD1 . ILE A 1 292 ? -112.407 39.236 -34.467 1.00 28.77 ? 292  ILE A CD1 1 
ATOM   2169 N N   . SER A 1 293 ? -112.575 39.402 -30.879 1.00 32.23 ? 293  SER A N   1 
ATOM   2170 C CA  . SER A 1 293 ? -111.854 40.556 -30.338 1.00 32.56 ? 293  SER A CA  1 
ATOM   2171 C C   . SER A 1 293 ? -110.813 40.151 -29.303 1.00 33.85 ? 293  SER A C   1 
ATOM   2172 O O   . SER A 1 293 ? -109.740 40.746 -29.223 1.00 34.41 ? 293  SER A O   1 
ATOM   2173 C CB  . SER A 1 293 ? -112.828 41.562 -29.716 1.00 34.79 ? 293  SER A CB  1 
ATOM   2174 O OG  . SER A 1 293 ? -113.516 41.021 -28.598 1.00 33.76 ? 293  SER A OG  1 
ATOM   2175 N N   . MET A 1 294 ? -111.127 39.139 -28.507 1.00 33.77 ? 294  MET A N   1 
ATOM   2176 C CA  . MET A 1 294 ? -110.188 38.680 -27.494 1.00 35.90 ? 294  MET A CA  1 
ATOM   2177 C C   . MET A 1 294 ? -108.942 38.092 -28.150 1.00 33.57 ? 294  MET A C   1 
ATOM   2178 O O   . MET A 1 294 ? -107.827 38.249 -27.654 1.00 32.94 ? 294  MET A O   1 
ATOM   2179 C CB  . MET A 1 294 ? -110.843 37.631 -26.588 1.00 40.13 ? 294  MET A CB  1 
ATOM   2180 C CG  . MET A 1 294 ? -112.207 37.131 -27.072 1.00 49.13 ? 294  MET A CG  1 
ATOM   2181 S SD  . MET A 1 294 ? -112.186 36.341 -28.703 1.00 56.57 ? 294  MET A SD  1 
ATOM   2182 C CE  . MET A 1 294 ? -111.796 34.629 -28.247 1.00 53.36 ? 294  MET A CE  1 
ATOM   2183 N N   . ILE A 1 295 ? -109.133 37.407 -29.267 1.00 31.51 ? 295  ILE A N   1 
ATOM   2184 C CA  . ILE A 1 295 ? -108.010 36.811 -29.971 1.00 30.90 ? 295  ILE A CA  1 
ATOM   2185 C C   . ILE A 1 295 ? -107.102 37.896 -30.522 1.00 28.27 ? 295  ILE A C   1 
ATOM   2186 O O   . ILE A 1 295 ? -105.876 37.809 -30.429 1.00 28.18 ? 295  ILE A O   1 
ATOM   2187 C CB  . ILE A 1 295 ? -108.496 35.926 -31.131 1.00 33.77 ? 295  ILE A CB  1 
ATOM   2188 C CG1 . ILE A 1 295 ? -109.312 34.761 -30.564 1.00 34.04 ? 295  ILE A CG1 1 
ATOM   2189 C CG2 . ILE A 1 295 ? -107.306 35.444 -31.949 1.00 33.64 ? 295  ILE A CG2 1 
ATOM   2190 C CD1 . ILE A 1 295 ? -109.803 33.774 -31.608 1.00 41.35 ? 295  ILE A CD1 1 
ATOM   2191 N N   . LEU A 1 296 ? -107.714 38.926 -31.091 1.00 26.27 ? 296  LEU A N   1 
ATOM   2192 C CA  . LEU A 1 296 ? -106.957 40.028 -31.661 1.00 25.67 ? 296  LEU A CA  1 
ATOM   2193 C C   . LEU A 1 296 ? -106.239 40.820 -30.576 1.00 25.15 ? 296  LEU A C   1 
ATOM   2194 O O   . LEU A 1 296 ? -105.074 41.178 -30.733 1.00 24.10 ? 296  LEU A O   1 
ATOM   2195 C CB  . LEU A 1 296 ? -107.888 40.943 -32.468 1.00 23.02 ? 296  LEU A CB  1 
ATOM   2196 C CG  . LEU A 1 296 ? -108.521 40.285 -33.707 1.00 25.53 ? 296  LEU A CG  1 
ATOM   2197 C CD1 . LEU A 1 296 ? -109.486 41.255 -34.385 1.00 23.51 ? 296  LEU A CD1 1 
ATOM   2198 C CD2 . LEU A 1 296 ? -107.420 39.866 -34.682 1.00 27.72 ? 296  LEU A CD2 1 
ATOM   2199 N N   . ALA A 1 297 ? -106.937 41.085 -29.475 1.00 24.51 ? 297  ALA A N   1 
ATOM   2200 C CA  . ALA A 1 297 ? -106.353 41.836 -28.370 1.00 27.91 ? 297  ALA A CA  1 
ATOM   2201 C C   . ALA A 1 297 ? -105.141 41.094 -27.828 1.00 29.86 ? 297  ALA A C   1 
ATOM   2202 O O   . ALA A 1 297 ? -104.104 41.697 -27.528 1.00 30.02 ? 297  ALA A O   1 
ATOM   2203 C CB  . ALA A 1 297 ? -107.391 42.028 -27.254 1.00 28.92 ? 297  ALA A CB  1 
ATOM   2204 N N   . GLU A 1 298 ? -105.280 39.778 -27.719 1.00 29.89 ? 298  GLU A N   1 
ATOM   2205 C CA  . GLU A 1 298 ? -104.216 38.932 -27.203 1.00 32.60 ? 298  GLU A CA  1 
ATOM   2206 C C   . GLU A 1 298 ? -102.983 38.884 -28.116 1.00 31.86 ? 298  GLU A C   1 
ATOM   2207 O O   . GLU A 1 298 ? -101.854 38.772 -27.639 1.00 32.15 ? 298  GLU A O   1 
ATOM   2208 C CB  . GLU A 1 298 ? -104.768 37.525 -26.969 1.00 35.14 ? 298  GLU A CB  1 
ATOM   2209 C CG  . GLU A 1 298 ? -103.862 36.613 -26.169 1.00 41.22 ? 298  GLU A CG  1 
ATOM   2210 C CD  . GLU A 1 298 ? -103.473 37.209 -24.828 1.00 43.79 ? 298  GLU A CD  1 
ATOM   2211 O OE1 . GLU A 1 298 ? -104.248 38.026 -24.285 1.00 44.95 ? 298  GLU A OE1 1 
ATOM   2212 O OE2 . GLU A 1 298 ? -102.396 36.846 -24.313 1.00 45.51 ? 298  GLU A OE2 1 
ATOM   2213 N N   . ALA A 1 299 ? -103.191 38.959 -29.428 1.00 30.80 ? 299  ALA A N   1 
ATOM   2214 C CA  . ALA A 1 299 ? -102.062 38.943 -30.354 1.00 27.52 ? 299  ALA A CA  1 
ATOM   2215 C C   . ALA A 1 299 ? -101.323 40.280 -30.276 1.00 27.39 ? 299  ALA A C   1 
ATOM   2216 O O   . ALA A 1 299 ? -100.095 40.328 -30.383 1.00 27.70 ? 299  ALA A O   1 
ATOM   2217 C CB  . ALA A 1 299 ? -102.543 38.678 -31.771 1.00 25.36 ? 299  ALA A CB  1 
ATOM   2218 N N   . ILE A 1 300 ? -102.063 41.368 -30.086 1.00 26.34 ? 300  ILE A N   1 
ATOM   2219 C CA  . ILE A 1 300 ? -101.436 42.684 -29.982 1.00 28.29 ? 300  ILE A CA  1 
ATOM   2220 C C   . ILE A 1 300 ? -100.592 42.746 -28.708 1.00 29.16 ? 300  ILE A C   1 
ATOM   2221 O O   . ILE A 1 300 ? -99.413  43.107 -28.735 1.00 28.16 ? 300  ILE A O   1 
ATOM   2222 C CB  . ILE A 1 300 ? -102.485 43.818 -29.943 1.00 27.03 ? 300  ILE A CB  1 
ATOM   2223 C CG1 . ILE A 1 300 ? -103.138 43.969 -31.319 1.00 25.77 ? 300  ILE A CG1 1 
ATOM   2224 C CG2 . ILE A 1 300 ? -101.818 45.139 -29.532 1.00 28.30 ? 300  ILE A CG2 1 
ATOM   2225 C CD1 . ILE A 1 300 ? -104.357 44.885 -31.325 1.00 23.59 ? 300  ILE A CD1 1 
ATOM   2226 N N   . ARG A 1 301 ? -101.207 42.385 -27.593 1.00 31.00 ? 301  ARG A N   1 
ATOM   2227 C CA  . ARG A 1 301 ? -100.516 42.391 -26.318 1.00 32.83 ? 301  ARG A CA  1 
ATOM   2228 C C   . ARG A 1 301 ? -99.274  41.523 -26.400 1.00 33.23 ? 301  ARG A C   1 
ATOM   2229 O O   . ARG A 1 301 ? -98.201  41.916 -25.955 1.00 34.73 ? 301  ARG A O   1 
ATOM   2230 C CB  . ARG A 1 301 ? -101.437 41.871 -25.216 1.00 35.31 ? 301  ARG A CB  1 
ATOM   2231 C CG  . ARG A 1 301 ? -100.773 41.823 -23.861 1.00 40.70 ? 301  ARG A CG  1 
ATOM   2232 C CD  . ARG A 1 301 ? -101.748 41.436 -22.763 1.00 43.58 ? 301  ARG A CD  1 
ATOM   2233 N NE  . ARG A 1 301 ? -101.099 40.527 -21.827 1.00 49.63 ? 301  ARG A NE  1 
ATOM   2234 C CZ  . ARG A 1 301 ? -100.866 39.247 -22.091 1.00 51.11 ? 301  ARG A CZ  1 
ATOM   2235 N NH1 . ARG A 1 301 ? -101.242 38.744 -23.254 1.00 54.28 ? 301  ARG A NH1 1 
ATOM   2236 N NH2 . ARG A 1 301 ? -100.245 38.474 -21.208 1.00 54.08 ? 301  ARG A NH2 1 
ATOM   2237 N N   . ARG A 1 302 ? -99.418  40.341 -26.982 1.00 34.98 ? 302  ARG A N   1 
ATOM   2238 C CA  . ARG A 1 302 ? -98.298  39.426 -27.112 1.00 36.17 ? 302  ARG A CA  1 
ATOM   2239 C C   . ARG A 1 302 ? -97.236  39.921 -28.090 1.00 36.56 ? 302  ARG A C   1 
ATOM   2240 O O   . ARG A 1 302 ? -96.052  39.662 -27.910 1.00 35.92 ? 302  ARG A O   1 
ATOM   2241 C CB  . ARG A 1 302 ? -98.817  38.044 -27.508 1.00 38.82 ? 302  ARG A CB  1 
ATOM   2242 C CG  . ARG A 1 302 ? -99.432  37.303 -26.323 1.00 42.57 ? 302  ARG A CG  1 
ATOM   2243 C CD  . ARG A 1 302 ? -100.396 36.204 -26.742 1.00 43.87 ? 302  ARG A CD  1 
ATOM   2244 N NE  . ARG A 1 302 ? -100.833 35.441 -25.580 1.00 44.37 ? 302  ARG A NE  1 
ATOM   2245 C CZ  . ARG A 1 302 ? -100.105 34.503 -24.983 1.00 45.98 ? 302  ARG A CZ  1 
ATOM   2246 N NH1 . ARG A 1 302 ? -98.900  34.193 -25.446 1.00 43.00 ? 302  ARG A NH1 1 
ATOM   2247 N NH2 . ARG A 1 302 ? -100.568 33.897 -23.898 1.00 47.04 ? 302  ARG A NH2 1 
ATOM   2248 N N   . THR A 1 303 ? -97.659  40.639 -29.123 1.00 37.55 ? 303  THR A N   1 
ATOM   2249 C CA  . THR A 1 303 ? -96.719  41.181 -30.097 1.00 37.37 ? 303  THR A CA  1 
ATOM   2250 C C   . THR A 1 303 ? -95.918  42.284 -29.419 1.00 38.11 ? 303  THR A C   1 
ATOM   2251 O O   . THR A 1 303 ? -94.722  42.441 -29.661 1.00 38.88 ? 303  THR A O   1 
ATOM   2252 C CB  . THR A 1 303 ? -97.456  41.791 -31.299 1.00 36.12 ? 303  THR A CB  1 
ATOM   2253 O OG1 . THR A 1 303 ? -98.011  40.743 -32.094 1.00 34.54 ? 303  THR A OG1 1 
ATOM   2254 C CG2 . THR A 1 303 ? -96.515  42.633 -32.131 1.00 35.59 ? 303  THR A CG2 1 
ATOM   2255 N N   . HIS A 1 304 ? -96.596  43.045 -28.570 1.00 38.53 ? 304  HIS A N   1 
ATOM   2256 C CA  . HIS A 1 304 ? -95.972  44.144 -27.854 1.00 39.64 ? 304  HIS A CA  1 
ATOM   2257 C C   . HIS A 1 304 ? -95.005  43.662 -26.777 1.00 41.01 ? 304  HIS A C   1 
ATOM   2258 O O   . HIS A 1 304 ? -93.920  44.216 -26.618 1.00 40.33 ? 304  HIS A O   1 
ATOM   2259 C CB  . HIS A 1 304 ? -97.043  45.020 -27.207 1.00 39.18 ? 304  HIS A CB  1 
ATOM   2260 C CG  . HIS A 1 304 ? -96.487  46.185 -26.451 1.00 40.95 ? 304  HIS A CG  1 
ATOM   2261 N ND1 . HIS A 1 304 ? -95.753  47.182 -27.056 1.00 41.31 ? 304  HIS A ND1 1 
ATOM   2262 C CD2 . HIS A 1 304 ? -96.543  46.505 -25.136 1.00 40.81 ? 304  HIS A CD2 1 
ATOM   2263 C CE1 . HIS A 1 304 ? -95.381  48.066 -26.148 1.00 38.85 ? 304  HIS A CE1 1 
ATOM   2264 N NE2 . HIS A 1 304 ? -95.847  47.678 -24.975 1.00 40.23 ? 304  HIS A NE2 1 
ATOM   2265 N N   . ASN A 1 305 ? -95.400  42.631 -26.040 1.00 41.82 ? 305  ASN A N   1 
ATOM   2266 C CA  . ASN A 1 305 ? -94.559  42.113 -24.970 1.00 44.70 ? 305  ASN A CA  1 
ATOM   2267 C C   . ASN A 1 305 ? -93.563  41.074 -25.455 1.00 46.56 ? 305  ASN A C   1 
ATOM   2268 O O   . ASN A 1 305 ? -92.794  40.526 -24.665 1.00 46.40 ? 305  ASN A O   1 
ATOM   2269 C CB  . ASN A 1 305 ? -95.431  41.533 -23.858 1.00 44.47 ? 305  ASN A CB  1 
ATOM   2270 C CG  . ASN A 1 305 ? -96.368  42.570 -23.259 1.00 47.41 ? 305  ASN A CG  1 
ATOM   2271 O OD1 . ASN A 1 305 ? -95.936  43.654 -22.858 1.00 50.03 ? 305  ASN A OD1 1 
ATOM   2272 N ND2 . ASN A 1 305 ? -97.655  42.247 -23.196 1.00 48.21 ? 305  ASN A ND2 1 
ATOM   2273 N N   . GLY A 1 306 ? -93.568  40.810 -26.757 1.00 47.13 ? 306  GLY A N   1 
ATOM   2274 C CA  . GLY A 1 306 ? -92.646  39.830 -27.298 1.00 46.90 ? 306  GLY A CA  1 
ATOM   2275 C C   . GLY A 1 306 ? -92.930  38.402 -26.874 1.00 46.57 ? 306  GLY A C   1 
ATOM   2276 O O   . GLY A 1 306 ? -92.033  37.564 -26.903 1.00 46.67 ? 306  GLY A O   1 
ATOM   2277 N N   . GLU A 1 307 ? -94.165  38.114 -26.472 1.00 47.02 ? 307  GLU A N   1 
ATOM   2278 C CA  . GLU A 1 307 ? -94.528  36.757 -26.069 1.00 49.46 ? 307  GLU A CA  1 
ATOM   2279 C C   . GLU A 1 307 ? -95.081  35.980 -27.268 1.00 49.71 ? 307  GLU A C   1 
ATOM   2280 O O   . GLU A 1 307 ? -95.395  36.561 -28.307 1.00 47.33 ? 307  GLU A O   1 
ATOM   2281 C CB  . GLU A 1 307 ? -95.561  36.783 -24.933 1.00 52.55 ? 307  GLU A CB  1 
ATOM   2282 C CG  . GLU A 1 307 ? -96.291  35.448 -24.683 1.00 57.48 ? 307  GLU A CG  1 
ATOM   2283 C CD  . GLU A 1 307 ? -95.389  34.305 -24.196 1.00 60.37 ? 307  GLU A CD  1 
ATOM   2284 O OE1 . GLU A 1 307 ? -94.329  34.047 -24.807 1.00 61.59 ? 307  GLU A OE1 1 
ATOM   2285 O OE2 . GLU A 1 307 ? -95.756  33.643 -23.201 1.00 61.65 ? 307  GLU A OE2 1 
ATOM   2286 N N   . SER A 1 308 ? -95.190  34.664 -27.108 1.00 48.58 ? 308  SER A N   1 
ATOM   2287 C CA  . SER A 1 308 ? -95.682  33.777 -28.150 1.00 48.37 ? 308  SER A CA  1 
ATOM   2288 C C   . SER A 1 308 ? -97.090  34.098 -28.633 1.00 48.73 ? 308  SER A C   1 
ATOM   2289 O O   . SER A 1 308 ? -98.032  34.168 -27.843 1.00 48.78 ? 308  SER A O   1 
ATOM   2290 C CB  . SER A 1 308 ? -95.640  32.325 -27.661 1.00 49.10 ? 308  SER A CB  1 
ATOM   2291 O OG  . SER A 1 308 ? -96.283  31.456 -28.579 1.00 50.29 ? 308  SER A OG  1 
ATOM   2292 N N   . VAL A 1 309 ? -97.226  34.286 -29.941 1.00 47.40 ? 309  VAL A N   1 
ATOM   2293 C CA  . VAL A 1 309 ? -98.523  34.565 -30.534 1.00 47.16 ? 309  VAL A CA  1 
ATOM   2294 C C   . VAL A 1 309 ? -99.094  33.264 -31.098 1.00 47.32 ? 309  VAL A C   1 
ATOM   2295 O O   . VAL A 1 309 ? -100.310 33.106 -31.198 1.00 45.91 ? 309  VAL A O   1 
ATOM   2296 C CB  . VAL A 1 309 ? -98.407  35.614 -31.661 1.00 47.22 ? 309  VAL A CB  1 
ATOM   2297 C CG1 . VAL A 1 309 ? -99.752  35.826 -32.315 1.00 46.76 ? 309  VAL A CG1 1 
ATOM   2298 C CG2 . VAL A 1 309 ? -97.888  36.926 -31.093 1.00 46.64 ? 309  VAL A CG2 1 
ATOM   2299 N N   . SER A 1 310 ? -98.210  32.328 -31.443 1.00 48.33 ? 310  SER A N   1 
ATOM   2300 C CA  . SER A 1 310 ? -98.621  31.032 -32.001 1.00 51.48 ? 310  SER A CA  1 
ATOM   2301 C C   . SER A 1 310 ? -99.519  30.269 -31.028 1.00 51.48 ? 310  SER A C   1 
ATOM   2302 O O   . SER A 1 310 ? -100.293 29.396 -31.425 1.00 50.69 ? 310  SER A O   1 
ATOM   2303 C CB  . SER A 1 310 ? -97.395  30.172 -32.329 1.00 51.56 ? 310  SER A CB  1 
ATOM   2304 O OG  . SER A 1 310 ? -96.778  29.692 -31.145 1.00 52.29 ? 310  SER A OG  1 
ATOM   2305 N N   . TYR A 1 311 ? -99.387  30.598 -29.748 1.00 51.99 ? 311  TYR A N   1 
ATOM   2306 C CA  . TYR A 1 311 ? -100.180 29.984 -28.690 1.00 52.35 ? 311  TYR A CA  1 
ATOM   2307 C C   . TYR A 1 311 ? -101.679 30.106 -28.988 1.00 50.49 ? 311  TYR A C   1 
ATOM   2308 O O   . TYR A 1 311 ? -102.456 29.191 -28.698 1.00 50.17 ? 311  TYR A O   1 
ATOM   2309 C CB  . TYR A 1 311 ? -99.843  30.672 -27.367 1.00 56.49 ? 311  TYR A CB  1 
ATOM   2310 C CG  . TYR A 1 311 ? -100.780 30.366 -26.228 1.00 60.43 ? 311  TYR A CG  1 
ATOM   2311 C CD1 . TYR A 1 311 ? -100.975 29.058 -25.786 1.00 63.09 ? 311  TYR A CD1 1 
ATOM   2312 C CD2 . TYR A 1 311 ? -101.443 31.392 -25.563 1.00 61.76 ? 311  TYR A CD2 1 
ATOM   2313 C CE1 . TYR A 1 311 ? -101.808 28.783 -24.700 1.00 64.71 ? 311  TYR A CE1 1 
ATOM   2314 C CE2 . TYR A 1 311 ? -102.273 31.131 -24.481 1.00 64.04 ? 311  TYR A CE2 1 
ATOM   2315 C CZ  . TYR A 1 311 ? -102.452 29.827 -24.054 1.00 64.61 ? 311  TYR A CZ  1 
ATOM   2316 O OH  . TYR A 1 311 ? -103.269 29.572 -22.976 1.00 66.57 ? 311  TYR A OH  1 
ATOM   2317 N N   . LEU A 1 312 ? -102.070 31.235 -29.578 1.00 47.07 ? 312  LEU A N   1 
ATOM   2318 C CA  . LEU A 1 312 ? -103.465 31.501 -29.918 1.00 44.81 ? 312  LEU A CA  1 
ATOM   2319 C C   . LEU A 1 312 ? -103.972 30.624 -31.062 1.00 45.09 ? 312  LEU A C   1 
ATOM   2320 O O   . LEU A 1 312 ? -105.177 30.460 -31.236 1.00 44.87 ? 312  LEU A O   1 
ATOM   2321 C CB  . LEU A 1 312 ? -103.644 32.975 -30.294 1.00 43.43 ? 312  LEU A CB  1 
ATOM   2322 C CG  . LEU A 1 312 ? -103.070 34.036 -29.347 1.00 42.68 ? 312  LEU A CG  1 
ATOM   2323 C CD1 . LEU A 1 312 ? -103.426 35.415 -29.861 1.00 41.41 ? 312  LEU A CD1 1 
ATOM   2324 C CD2 . LEU A 1 312 ? -103.620 33.847 -27.946 1.00 44.56 ? 312  LEU A CD2 1 
ATOM   2325 N N   . PHE A 1 313 ? -103.052 30.065 -31.843 1.00 45.31 ? 313  PHE A N   1 
ATOM   2326 C CA  . PHE A 1 313 ? -103.419 29.205 -32.970 1.00 46.68 ? 313  PHE A CA  1 
ATOM   2327 C C   . PHE A 1 313 ? -104.339 28.066 -32.539 1.00 46.38 ? 313  PHE A C   1 
ATOM   2328 O O   . PHE A 1 313 ? -105.203 27.674 -33.355 1.00 46.78 ? 313  PHE A O   1 
ATOM   2329 C CB  . PHE A 1 313 ? -102.165 28.623 -33.643 1.00 47.19 ? 313  PHE A CB  1 
ATOM   2330 C CG  . PHE A 1 313 ? -101.313 29.649 -34.354 1.00 47.19 ? 313  PHE A CG  1 
ATOM   2331 C CD1 . PHE A 1 313 ? -100.063 29.299 -34.851 1.00 47.68 ? 313  PHE A CD1 1 
ATOM   2332 C CD2 . PHE A 1 313 ? -101.760 30.957 -34.533 1.00 47.25 ? 313  PHE A CD2 1 
ATOM   2333 C CE1 . PHE A 1 313 ? -99.269  30.229 -35.516 1.00 48.20 ? 313  PHE A CE1 1 
ATOM   2334 C CE2 . PHE A 1 313 ? -100.975 31.896 -35.197 1.00 47.63 ? 313  PHE A CE2 1 
ATOM   2335 C CZ  . PHE A 1 313 ? -99.726  31.531 -35.689 1.00 48.72 ? 313  PHE A CZ  1 
ATOM   2336 N N   . ASN B 1 3   ? -80.430  38.695 -81.607 1.00 49.09 ? 3    ASN B N   1 
ATOM   2337 C CA  . ASN B 1 3   ? -79.711  39.198 -80.402 1.00 46.91 ? 3    ASN B CA  1 
ATOM   2338 C C   . ASN B 1 3   ? -80.206  38.472 -79.151 1.00 45.86 ? 3    ASN B C   1 
ATOM   2339 O O   . ASN B 1 3   ? -80.307  39.053 -78.069 1.00 46.01 ? 3    ASN B O   1 
ATOM   2340 C CB  . ASN B 1 3   ? -79.924  40.705 -80.258 1.00 49.36 ? 3    ASN B CB  1 
ATOM   2341 C CG  . ASN B 1 3   ? -81.358  41.062 -79.951 1.00 51.64 ? 3    ASN B CG  1 
ATOM   2342 O OD1 . ASN B 1 3   ? -82.281  40.510 -80.547 1.00 53.42 ? 3    ASN B OD1 1 
ATOM   2343 N ND2 . ASN B 1 3   ? -81.556  41.998 -79.023 1.00 51.75 ? 3    ASN B ND2 1 
ATOM   2344 N N   . ILE B 1 4   ? -80.516  37.192 -79.320 1.00 42.19 ? 4    ILE B N   1 
ATOM   2345 C CA  . ILE B 1 4   ? -80.976  36.351 -78.231 1.00 39.38 ? 4    ILE B CA  1 
ATOM   2346 C C   . ILE B 1 4   ? -79.809  35.424 -77.861 1.00 38.13 ? 4    ILE B C   1 
ATOM   2347 O O   . ILE B 1 4   ? -79.057  34.980 -78.730 1.00 36.61 ? 4    ILE B O   1 
ATOM   2348 C CB  . ILE B 1 4   ? -82.212  35.537 -78.680 1.00 40.99 ? 4    ILE B CB  1 
ATOM   2349 C CG1 . ILE B 1 4   ? -82.800  34.741 -77.511 1.00 39.28 ? 4    ILE B CG1 1 
ATOM   2350 C CG2 . ILE B 1 4   ? -81.833  34.642 -79.847 1.00 41.76 ? 4    ILE B CG2 1 
ATOM   2351 C CD1 . ILE B 1 4   ? -82.110  33.434 -77.233 1.00 40.34 ? 4    ILE B CD1 1 
ATOM   2352 N N   . LYS B 1 5   ? -79.646  35.162 -76.570 1.00 34.76 ? 5    LYS B N   1 
ATOM   2353 C CA  . LYS B 1 5   ? -78.574  34.306 -76.081 1.00 34.38 ? 5    LYS B CA  1 
ATOM   2354 C C   . LYS B 1 5   ? -79.124  33.327 -75.053 1.00 33.66 ? 5    LYS B C   1 
ATOM   2355 O O   . LYS B 1 5   ? -79.756  33.730 -74.075 1.00 32.65 ? 5    LYS B O   1 
ATOM   2356 C CB  . LYS B 1 5   ? -77.484  35.152 -75.420 1.00 38.39 ? 5    LYS B CB  1 
ATOM   2357 C CG  . LYS B 1 5   ? -76.118  35.049 -76.066 1.00 43.04 ? 5    LYS B CG  1 
ATOM   2358 C CD  . LYS B 1 5   ? -76.115  35.695 -77.439 1.00 46.78 ? 5    LYS B CD  1 
ATOM   2359 C CE  . LYS B 1 5   ? -74.769  35.547 -78.125 1.00 48.37 ? 5    LYS B CE  1 
ATOM   2360 N NZ  . LYS B 1 5   ? -74.794  36.152 -79.489 1.00 47.56 ? 5    LYS B NZ  1 
ATOM   2361 N N   . ILE B 1 6   ? -78.881  32.041 -75.269 1.00 31.56 ? 6    ILE B N   1 
ATOM   2362 C CA  . ILE B 1 6   ? -79.358  31.038 -74.340 1.00 31.03 ? 6    ILE B CA  1 
ATOM   2363 C C   . ILE B 1 6   ? -78.191  30.266 -73.727 1.00 29.99 ? 6    ILE B C   1 
ATOM   2364 O O   . ILE B 1 6   ? -77.308  29.795 -74.438 1.00 28.23 ? 6    ILE B O   1 
ATOM   2365 C CB  . ILE B 1 6   ? -80.341  30.079 -75.039 1.00 33.05 ? 6    ILE B CB  1 
ATOM   2366 C CG1 . ILE B 1 6   ? -80.694  28.923 -74.110 1.00 33.93 ? 6    ILE B CG1 1 
ATOM   2367 C CG2 . ILE B 1 6   ? -79.755  29.600 -76.357 1.00 32.58 ? 6    ILE B CG2 1 
ATOM   2368 C CD1 . ILE B 1 6   ? -81.854  28.099 -74.602 1.00 37.24 ? 6    ILE B CD1 1 
ATOM   2369 N N   . PHE B 1 7   ? -78.184  30.173 -72.401 1.00 28.02 ? 7    PHE B N   1 
ATOM   2370 C CA  . PHE B 1 7   ? -77.129  29.468 -71.670 1.00 29.93 ? 7    PHE B CA  1 
ATOM   2371 C C   . PHE B 1 7   ? -77.719  28.380 -70.792 1.00 31.30 ? 7    PHE B C   1 
ATOM   2372 O O   . PHE B 1 7   ? -78.852  28.495 -70.320 1.00 32.40 ? 7    PHE B O   1 
ATOM   2373 C CB  . PHE B 1 7   ? -76.332  30.429 -70.767 1.00 27.29 ? 7    PHE B CB  1 
ATOM   2374 C CG  . PHE B 1 7   ? -75.521  31.449 -71.513 1.00 25.82 ? 7    PHE B CG  1 
ATOM   2375 C CD1 . PHE B 1 7   ? -76.105  32.618 -71.984 1.00 27.13 ? 7    PHE B CD1 1 
ATOM   2376 C CD2 . PHE B 1 7   ? -74.167  31.245 -71.732 1.00 24.23 ? 7    PHE B CD2 1 
ATOM   2377 C CE1 . PHE B 1 7   ? -75.344  33.573 -72.653 1.00 28.08 ? 7    PHE B CE1 1 
ATOM   2378 C CE2 . PHE B 1 7   ? -73.397  32.190 -72.399 1.00 26.57 ? 7    PHE B CE2 1 
ATOM   2379 C CZ  . PHE B 1 7   ? -73.984  33.356 -72.861 1.00 27.25 ? 7    PHE B CZ  1 
ATOM   2380 N N   . SER B 1 8   ? -76.938  27.335 -70.553 1.00 34.82 ? 8    SER B N   1 
ATOM   2381 C CA  . SER B 1 8   ? -77.395  26.238 -69.719 1.00 41.50 ? 8    SER B CA  1 
ATOM   2382 C C   . SER B 1 8   ? -76.724  26.229 -68.356 1.00 46.04 ? 8    SER B C   1 
ATOM   2383 O O   . SER B 1 8   ? -75.533  26.528 -68.234 1.00 42.50 ? 8    SER B O   1 
ATOM   2384 C CB  . SER B 1 8   ? -77.136  24.903 -70.407 1.00 43.79 ? 8    SER B CB  1 
ATOM   2385 O OG  . SER B 1 8   ? -77.610  23.837 -69.601 1.00 48.45 ? 8    SER B OG  1 
ATOM   2386 N N   . GLY B 1 9   ? -77.510  25.874 -67.339 1.00 52.29 ? 9    GLY B N   1 
ATOM   2387 C CA  . GLY B 1 9   ? -77.020  25.802 -65.976 1.00 59.85 ? 9    GLY B CA  1 
ATOM   2388 C C   . GLY B 1 9   ? -75.718  25.035 -65.863 1.00 65.40 ? 9    GLY B C   1 
ATOM   2389 O O   . GLY B 1 9   ? -74.670  25.630 -65.607 1.00 68.57 ? 9    GLY B O   1 
ATOM   2390 N N   . SER B 1 10  ? -75.772  23.717 -66.048 1.00 69.74 ? 10   SER B N   1 
ATOM   2391 C CA  . SER B 1 10  ? -74.566  22.898 -65.971 1.00 73.91 ? 10   SER B CA  1 
ATOM   2392 C C   . SER B 1 10  ? -74.512  21.911 -67.129 1.00 76.31 ? 10   SER B C   1 
ATOM   2393 O O   . SER B 1 10  ? -75.251  22.041 -68.104 1.00 76.39 ? 10   SER B O   1 
ATOM   2394 C CB  . SER B 1 10  ? -74.517  22.127 -64.653 1.00 74.43 ? 10   SER B CB  1 
ATOM   2395 O OG  . SER B 1 10  ? -75.181  20.882 -64.776 1.00 75.78 ? 10   SER B OG  1 
ATOM   2396 N N   . SER B 1 11  ? -73.638  20.915 -67.005 1.00 79.10 ? 11   SER B N   1 
ATOM   2397 C CA  . SER B 1 11  ? -73.461  19.898 -68.036 1.00 80.85 ? 11   SER B CA  1 
ATOM   2398 C C   . SER B 1 11  ? -74.760  19.198 -68.438 1.00 81.23 ? 11   SER B C   1 
ATOM   2399 O O   . SER B 1 11  ? -74.798  18.490 -69.447 1.00 82.86 ? 11   SER B O   1 
ATOM   2400 C CB  . SER B 1 11  ? -72.443  18.853 -67.574 1.00 80.37 ? 11   SER B CB  1 
ATOM   2401 O OG  . SER B 1 11  ? -72.210  17.897 -68.591 1.00 79.04 ? 11   SER B OG  1 
ATOM   2402 N N   . HIS B 1 12  ? -75.817  19.387 -67.651 1.00 80.02 ? 12   HIS B N   1 
ATOM   2403 C CA  . HIS B 1 12  ? -77.108  18.778 -67.959 1.00 77.92 ? 12   HIS B CA  1 
ATOM   2404 C C   . HIS B 1 12  ? -77.796  19.531 -69.093 1.00 75.74 ? 12   HIS B C   1 
ATOM   2405 O O   . HIS B 1 12  ? -78.968  19.910 -68.997 1.00 74.74 ? 12   HIS B O   1 
ATOM   2406 C CB  . HIS B 1 12  ? -77.990  18.768 -66.714 1.00 80.15 ? 12   HIS B CB  1 
ATOM   2407 C CG  . HIS B 1 12  ? -77.757  17.586 -65.826 1.00 81.55 ? 12   HIS B CG  1 
ATOM   2408 N ND1 . HIS B 1 12  ? -78.315  16.350 -66.072 1.00 81.85 ? 12   HIS B ND1 1 
ATOM   2409 C CD2 . HIS B 1 12  ? -77.007  17.445 -64.709 1.00 81.67 ? 12   HIS B CD2 1 
ATOM   2410 C CE1 . HIS B 1 12  ? -77.921  15.498 -65.142 1.00 82.54 ? 12   HIS B CE1 1 
ATOM   2411 N NE2 . HIS B 1 12  ? -77.127  16.138 -64.303 1.00 82.71 ? 12   HIS B NE2 1 
ATOM   2412 N N   . GLN B 1 13  ? -77.038  19.732 -70.169 1.00 71.96 ? 13   GLN B N   1 
ATOM   2413 C CA  . GLN B 1 13  ? -77.498  20.436 -71.358 1.00 68.50 ? 13   GLN B CA  1 
ATOM   2414 C C   . GLN B 1 13  ? -78.817  19.871 -71.880 1.00 64.00 ? 13   GLN B C   1 
ATOM   2415 O O   . GLN B 1 13  ? -79.603  20.583 -72.496 1.00 65.07 ? 13   GLN B O   1 
ATOM   2416 C CB  . GLN B 1 13  ? -76.443  20.325 -72.463 1.00 71.30 ? 13   GLN B CB  1 
ATOM   2417 C CG  . GLN B 1 13  ? -75.000  20.480 -71.997 1.00 73.48 ? 13   GLN B CG  1 
ATOM   2418 C CD  . GLN B 1 13  ? -74.625  21.913 -71.682 1.00 74.92 ? 13   GLN B CD  1 
ATOM   2419 O OE1 . GLN B 1 13  ? -75.261  22.568 -70.858 1.00 75.56 ? 13   GLN B OE1 1 
ATOM   2420 N NE2 . GLN B 1 13  ? -73.581  22.409 -72.339 1.00 74.99 ? 13   GLN B NE2 1 
ATOM   2421 N N   . ASP B 1 14  ? -79.041  18.586 -71.634 1.00 57.65 ? 14   ASP B N   1 
ATOM   2422 C CA  . ASP B 1 14  ? -80.238  17.886 -72.084 1.00 51.53 ? 14   ASP B CA  1 
ATOM   2423 C C   . ASP B 1 14  ? -81.377  18.785 -72.571 1.00 47.28 ? 14   ASP B C   1 
ATOM   2424 O O   . ASP B 1 14  ? -81.501  19.045 -73.769 1.00 45.32 ? 14   ASP B O   1 
ATOM   2425 C CB  . ASP B 1 14  ? -80.754  16.981 -70.968 1.00 55.48 ? 14   ASP B CB  1 
ATOM   2426 C CG  . ASP B 1 14  ? -81.421  15.734 -71.503 1.00 56.81 ? 14   ASP B CG  1 
ATOM   2427 O OD1 . ASP B 1 14  ? -81.937  15.788 -72.642 1.00 58.36 ? 14   ASP B OD1 1 
ATOM   2428 O OD2 . ASP B 1 14  ? -81.436  14.708 -70.784 1.00 58.61 ? 14   ASP B OD2 1 
ATOM   2429 N N   . LEU B 1 15  ? -82.207  19.250 -71.638 1.00 41.52 ? 15   LEU B N   1 
ATOM   2430 C CA  . LEU B 1 15  ? -83.346  20.112 -71.952 1.00 36.75 ? 15   LEU B CA  1 
ATOM   2431 C C   . LEU B 1 15  ? -82.909  21.409 -72.623 1.00 34.95 ? 15   LEU B C   1 
ATOM   2432 O O   . LEU B 1 15  ? -83.506  21.840 -73.610 1.00 33.88 ? 15   LEU B O   1 
ATOM   2433 C CB  . LEU B 1 15  ? -84.109  20.475 -70.675 1.00 34.82 ? 15   LEU B CB  1 
ATOM   2434 C CG  . LEU B 1 15  ? -85.641  20.407 -70.602 1.00 36.55 ? 15   LEU B CG  1 
ATOM   2435 C CD1 . LEU B 1 15  ? -86.105  21.241 -69.396 1.00 32.80 ? 15   LEU B CD1 1 
ATOM   2436 C CD2 . LEU B 1 15  ? -86.287  20.936 -71.870 1.00 32.52 ? 15   LEU B CD2 1 
ATOM   2437 N N   . SER B 1 16  ? -81.873  22.039 -72.080 1.00 32.57 ? 16   SER B N   1 
ATOM   2438 C CA  . SER B 1 16  ? -81.420  23.299 -72.638 1.00 34.15 ? 16   SER B CA  1 
ATOM   2439 C C   . SER B 1 16  ? -80.935  23.180 -74.079 1.00 33.67 ? 16   SER B C   1 
ATOM   2440 O O   . SER B 1 16  ? -81.070  24.123 -74.853 1.00 33.31 ? 16   SER B O   1 
ATOM   2441 C CB  . SER B 1 16  ? -80.356  23.947 -71.731 1.00 31.80 ? 16   SER B CB  1 
ATOM   2442 O OG  . SER B 1 16  ? -79.305  23.064 -71.398 1.00 35.45 ? 16   SER B OG  1 
ATOM   2443 N N   . GLN B 1 17  ? -80.404  22.020 -74.449 1.00 33.79 ? 17   GLN B N   1 
ATOM   2444 C CA  . GLN B 1 17  ? -79.929  21.813 -75.815 1.00 35.33 ? 17   GLN B CA  1 
ATOM   2445 C C   . GLN B 1 17  ? -81.098  21.603 -76.779 1.00 34.61 ? 17   GLN B C   1 
ATOM   2446 O O   . GLN B 1 17  ? -81.030  21.992 -77.947 1.00 34.30 ? 17   GLN B O   1 
ATOM   2447 C CB  . GLN B 1 17  ? -78.976  20.614 -75.885 1.00 37.00 ? 17   GLN B CB  1 
ATOM   2448 C CG  . GLN B 1 17  ? -78.456  20.330 -77.287 1.00 39.64 ? 17   GLN B CG  1 
ATOM   2449 C CD  . GLN B 1 17  ? -77.734  21.524 -77.897 1.00 43.25 ? 17   GLN B CD  1 
ATOM   2450 O OE1 . GLN B 1 17  ? -76.663  21.922 -77.429 1.00 43.81 ? 17   GLN B OE1 1 
ATOM   2451 N NE2 . GLN B 1 17  ? -78.322  22.106 -78.942 1.00 43.25 ? 17   GLN B NE2 1 
ATOM   2452 N N   . LYS B 1 18  ? -82.170  20.982 -76.296 1.00 33.62 ? 18   LYS B N   1 
ATOM   2453 C CA  . LYS B 1 18  ? -83.334  20.770 -77.145 1.00 33.32 ? 18   LYS B CA  1 
ATOM   2454 C C   . LYS B 1 18  ? -83.986  22.117 -77.416 1.00 31.68 ? 18   LYS B C   1 
ATOM   2455 O O   . LYS B 1 18  ? -84.382  22.416 -78.546 1.00 31.93 ? 18   LYS B O   1 
ATOM   2456 C CB  . LYS B 1 18  ? -84.348  19.840 -76.473 1.00 35.08 ? 18   LYS B CB  1 
ATOM   2457 C CG  . LYS B 1 18  ? -83.934  18.383 -76.435 1.00 36.53 ? 18   LYS B CG  1 
ATOM   2458 C CD  . LYS B 1 18  ? -85.041  17.520 -75.844 1.00 40.40 ? 18   LYS B CD  1 
ATOM   2459 C CE  . LYS B 1 18  ? -84.693  16.040 -75.917 1.00 41.83 ? 18   LYS B CE  1 
ATOM   2460 N NZ  . LYS B 1 18  ? -85.816  15.193 -75.430 1.00 45.10 ? 18   LYS B NZ  1 
ATOM   2461 N N   . ILE B 1 19  ? -84.098  22.925 -76.367 1.00 29.07 ? 19   ILE B N   1 
ATOM   2462 C CA  . ILE B 1 19  ? -84.694  24.247 -76.488 1.00 27.55 ? 19   ILE B CA  1 
ATOM   2463 C C   . ILE B 1 19  ? -83.890  25.034 -77.515 1.00 27.56 ? 19   ILE B C   1 
ATOM   2464 O O   . ILE B 1 19  ? -84.449  25.571 -78.462 1.00 26.91 ? 19   ILE B O   1 
ATOM   2465 C CB  . ILE B 1 19  ? -84.698  24.992 -75.126 1.00 25.21 ? 19   ILE B CB  1 
ATOM   2466 C CG1 . ILE B 1 19  ? -85.717  24.326 -74.187 1.00 28.20 ? 19   ILE B CG1 1 
ATOM   2467 C CG2 . ILE B 1 19  ? -85.039  26.460 -75.325 1.00 23.21 ? 19   ILE B CG2 1 
ATOM   2468 C CD1 . ILE B 1 19  ? -85.669  24.808 -72.751 1.00 25.28 ? 19   ILE B CD1 1 
ATOM   2469 N N   . ALA B 1 20  ? -82.576  25.085 -77.321 1.00 28.68 ? 20   ALA B N   1 
ATOM   2470 C CA  . ALA B 1 20  ? -81.688  25.797 -78.237 1.00 31.42 ? 20   ALA B CA  1 
ATOM   2471 C C   . ALA B 1 20  ? -81.900  25.308 -79.669 1.00 30.48 ? 20   ALA B C   1 
ATOM   2472 O O   . ALA B 1 20  ? -82.060  26.117 -80.579 1.00 31.43 ? 20   ALA B O   1 
ATOM   2473 C CB  . ALA B 1 20  ? -80.232  25.608 -77.819 1.00 27.72 ? 20   ALA B CB  1 
ATOM   2474 N N   . ASP B 1 21  ? -81.918  23.990 -79.864 1.00 32.35 ? 21   ASP B N   1 
ATOM   2475 C CA  . ASP B 1 21  ? -82.136  23.425 -81.199 1.00 33.58 ? 21   ASP B CA  1 
ATOM   2476 C C   . ASP B 1 21  ? -83.423  23.954 -81.809 1.00 34.54 ? 21   ASP B C   1 
ATOM   2477 O O   . ASP B 1 21  ? -83.442  24.374 -82.968 1.00 34.46 ? 21   ASP B O   1 
ATOM   2478 C CB  . ASP B 1 21  ? -82.231  21.895 -81.160 1.00 36.01 ? 21   ASP B CB  1 
ATOM   2479 C CG  . ASP B 1 21  ? -80.909  21.229 -80.837 1.00 40.99 ? 21   ASP B CG  1 
ATOM   2480 O OD1 . ASP B 1 21  ? -79.854  21.861 -81.051 1.00 43.07 ? 21   ASP B OD1 1 
ATOM   2481 O OD2 . ASP B 1 21  ? -80.921  20.062 -80.384 1.00 43.41 ? 21   ASP B OD2 1 
ATOM   2482 N N   . ARG B 1 22  ? -84.500  23.929 -81.026 1.00 33.99 ? 22   ARG B N   1 
ATOM   2483 C CA  . ARG B 1 22  ? -85.797  24.383 -81.507 1.00 34.37 ? 22   ARG B CA  1 
ATOM   2484 C C   . ARG B 1 22  ? -85.825  25.856 -81.891 1.00 33.66 ? 22   ARG B C   1 
ATOM   2485 O O   . ARG B 1 22  ? -86.668  26.273 -82.679 1.00 34.91 ? 22   ARG B O   1 
ATOM   2486 C CB  . ARG B 1 22  ? -86.884  24.082 -80.468 1.00 36.21 ? 22   ARG B CB  1 
ATOM   2487 C CG  . ARG B 1 22  ? -86.965  22.602 -80.092 1.00 41.81 ? 22   ARG B CG  1 
ATOM   2488 C CD  . ARG B 1 22  ? -88.077  22.312 -79.085 1.00 45.17 ? 22   ARG B CD  1 
ATOM   2489 N NE  . ARG B 1 22  ? -89.350  22.043 -79.738 1.00 50.09 ? 22   ARG B NE  1 
ATOM   2490 C CZ  . ARG B 1 22  ? -89.637  20.915 -80.385 1.00 52.98 ? 22   ARG B CZ  1 
ATOM   2491 N NH1 . ARG B 1 22  ? -88.740  19.939 -80.463 1.00 53.36 ? 22   ARG B NH1 1 
ATOM   2492 N NH2 . ARG B 1 22  ? -90.820  20.766 -80.964 1.00 52.07 ? 22   ARG B NH2 1 
ATOM   2493 N N   . LEU B 1 23  ? -84.910  26.644 -81.338 1.00 33.77 ? 23   LEU B N   1 
ATOM   2494 C CA  . LEU B 1 23  ? -84.846  28.068 -81.656 1.00 32.18 ? 23   LEU B CA  1 
ATOM   2495 C C   . LEU B 1 23  ? -83.830  28.331 -82.773 1.00 32.13 ? 23   LEU B C   1 
ATOM   2496 O O   . LEU B 1 23  ? -83.695  29.455 -83.244 1.00 32.01 ? 23   LEU B O   1 
ATOM   2497 C CB  . LEU B 1 23  ? -84.473  28.867 -80.406 1.00 31.45 ? 23   LEU B CB  1 
ATOM   2498 C CG  . LEU B 1 23  ? -85.490  28.835 -79.255 1.00 32.71 ? 23   LEU B CG  1 
ATOM   2499 C CD1 . LEU B 1 23  ? -84.872  29.436 -78.000 1.00 31.73 ? 23   LEU B CD1 1 
ATOM   2500 C CD2 . LEU B 1 23  ? -86.751  29.605 -79.656 1.00 30.11 ? 23   LEU B CD2 1 
ATOM   2501 N N   . GLY B 1 24  ? -83.127  27.285 -83.194 1.00 30.62 ? 24   GLY B N   1 
ATOM   2502 C CA  . GLY B 1 24  ? -82.135  27.427 -84.252 1.00 31.38 ? 24   GLY B CA  1 
ATOM   2503 C C   . GLY B 1 24  ? -80.862  28.074 -83.748 1.00 31.67 ? 24   GLY B C   1 
ATOM   2504 O O   . GLY B 1 24  ? -80.162  28.766 -84.489 1.00 30.93 ? 24   GLY B O   1 
ATOM   2505 N N   . LEU B 1 25  ? -80.557  27.834 -82.478 1.00 30.27 ? 25   LEU B N   1 
ATOM   2506 C CA  . LEU B 1 25  ? -79.381  28.414 -81.856 1.00 28.77 ? 25   LEU B CA  1 
ATOM   2507 C C   . LEU B 1 25  ? -78.499  27.358 -81.207 1.00 29.73 ? 25   LEU B C   1 
ATOM   2508 O O   . LEU B 1 25  ? -78.904  26.209 -81.023 1.00 28.32 ? 25   LEU B O   1 
ATOM   2509 C CB  . LEU B 1 25  ? -79.807  29.408 -80.764 1.00 28.39 ? 25   LEU B CB  1 
ATOM   2510 C CG  . LEU B 1 25  ? -80.725  30.577 -81.126 1.00 28.84 ? 25   LEU B CG  1 
ATOM   2511 C CD1 . LEU B 1 25  ? -81.157  31.287 -79.848 1.00 29.02 ? 25   LEU B CD1 1 
ATOM   2512 C CD2 . LEU B 1 25  ? -80.010  31.536 -82.078 1.00 25.05 ? 25   LEU B CD2 1 
ATOM   2513 N N   . GLU B 1 26  ? -77.281  27.770 -80.880 1.00 28.26 ? 26   GLU B N   1 
ATOM   2514 C CA  . GLU B 1 26  ? -76.357  26.920 -80.166 1.00 29.11 ? 26   GLU B CA  1 
ATOM   2515 C C   . GLU B 1 26  ? -76.360  27.523 -78.765 1.00 28.72 ? 26   GLU B C   1 
ATOM   2516 O O   . GLU B 1 26  ? -76.706  28.695 -78.583 1.00 25.21 ? 26   GLU B O   1 
ATOM   2517 C CB  . GLU B 1 26  ? -74.948  27.008 -80.743 1.00 29.41 ? 26   GLU B CB  1 
ATOM   2518 C CG  . GLU B 1 26  ? -74.831  26.500 -82.163 1.00 38.14 ? 26   GLU B CG  1 
ATOM   2519 C CD  . GLU B 1 26  ? -73.400  26.198 -82.542 1.00 41.23 ? 26   GLU B CD  1 
ATOM   2520 O OE1 . GLU B 1 26  ? -72.504  26.986 -82.166 1.00 42.10 ? 26   GLU B OE1 1 
ATOM   2521 O OE2 . GLU B 1 26  ? -73.175  25.174 -83.221 1.00 45.15 ? 26   GLU B OE2 1 
ATOM   2522 N N   . LEU B 1 27  ? -75.995  26.728 -77.772 1.00 27.74 ? 27   LEU B N   1 
ATOM   2523 C CA  . LEU B 1 27  ? -75.938  27.237 -76.412 1.00 27.25 ? 27   LEU B CA  1 
ATOM   2524 C C   . LEU B 1 27  ? -74.696  28.110 -76.264 1.00 25.50 ? 27   LEU B C   1 
ATOM   2525 O O   . LEU B 1 27  ? -73.648  27.803 -76.823 1.00 24.93 ? 27   LEU B O   1 
ATOM   2526 C CB  . LEU B 1 27  ? -75.875  26.080 -75.420 1.00 26.83 ? 27   LEU B CB  1 
ATOM   2527 C CG  . LEU B 1 27  ? -77.185  25.337 -75.148 1.00 25.37 ? 27   LEU B CG  1 
ATOM   2528 C CD1 . LEU B 1 27  ? -76.895  24.061 -74.371 1.00 25.99 ? 27   LEU B CD1 1 
ATOM   2529 C CD2 . LEU B 1 27  ? -78.129  26.238 -74.365 1.00 24.33 ? 27   LEU B CD2 1 
ATOM   2530 N N   . GLY B 1 28  ? -74.819  29.198 -75.514 1.00 25.65 ? 28   GLY B N   1 
ATOM   2531 C CA  . GLY B 1 28  ? -73.683  30.080 -75.295 1.00 25.85 ? 28   GLY B CA  1 
ATOM   2532 C C   . GLY B 1 28  ? -72.526  29.398 -74.575 1.00 28.76 ? 28   GLY B C   1 
ATOM   2533 O O   . GLY B 1 28  ? -72.717  28.435 -73.826 1.00 27.04 ? 28   GLY B O   1 
ATOM   2534 N N   . LYS B 1 29  ? -71.315  29.885 -74.820 1.00 31.06 ? 29   LYS B N   1 
ATOM   2535 C CA  . LYS B 1 29  ? -70.133  29.326 -74.186 1.00 35.91 ? 29   LYS B CA  1 
ATOM   2536 C C   . LYS B 1 29  ? -70.044  29.769 -72.724 1.00 36.95 ? 29   LYS B C   1 
ATOM   2537 O O   . LYS B 1 29  ? -70.189  30.955 -72.420 1.00 36.97 ? 29   LYS B O   1 
ATOM   2538 C CB  . LYS B 1 29  ? -68.868  29.767 -74.931 1.00 38.38 ? 29   LYS B CB  1 
ATOM   2539 C CG  . LYS B 1 29  ? -68.719  29.173 -76.326 1.00 47.09 ? 29   LYS B CG  1 
ATOM   2540 C CD  . LYS B 1 29  ? -68.634  27.634 -76.286 1.00 51.70 ? 29   LYS B CD  1 
ATOM   2541 C CE  . LYS B 1 29  ? -68.455  27.034 -77.684 1.00 53.42 ? 29   LYS B CE  1 
ATOM   2542 N NZ  . LYS B 1 29  ? -68.556  25.545 -77.694 1.00 53.72 ? 29   LYS B NZ  1 
ATOM   2543 N N   . VAL B 1 30  ? -69.819  28.806 -71.834 1.00 37.39 ? 30   VAL B N   1 
ATOM   2544 C CA  . VAL B 1 30  ? -69.683  29.067 -70.408 1.00 40.53 ? 30   VAL B CA  1 
ATOM   2545 C C   . VAL B 1 30  ? -68.557  28.209 -69.842 1.00 43.35 ? 30   VAL B C   1 
ATOM   2546 O O   . VAL B 1 30  ? -68.589  26.983 -69.953 1.00 44.34 ? 30   VAL B O   1 
ATOM   2547 C CB  . VAL B 1 30  ? -70.968  28.710 -69.618 1.00 40.29 ? 30   VAL B CB  1 
ATOM   2548 C CG1 . VAL B 1 30  ? -70.761  28.998 -68.140 1.00 39.75 ? 30   VAL B CG1 1 
ATOM   2549 C CG2 . VAL B 1 30  ? -72.143  29.498 -70.134 1.00 40.99 ? 30   VAL B CG2 1 
ATOM   2550 N N   . VAL B 1 31  ? -67.566  28.851 -69.236 1.00 46.18 ? 31   VAL B N   1 
ATOM   2551 C CA  . VAL B 1 31  ? -66.447  28.131 -68.632 1.00 49.33 ? 31   VAL B CA  1 
ATOM   2552 C C   . VAL B 1 31  ? -66.802  27.922 -67.160 1.00 50.51 ? 31   VAL B C   1 
ATOM   2553 O O   . VAL B 1 31  ? -66.909  28.886 -66.400 1.00 50.50 ? 31   VAL B O   1 
ATOM   2554 C CB  . VAL B 1 31  ? -65.135  28.945 -68.717 1.00 49.62 ? 31   VAL B CB  1 
ATOM   2555 C CG1 . VAL B 1 31  ? -63.977  28.092 -68.234 1.00 49.32 ? 31   VAL B CG1 1 
ATOM   2556 C CG2 . VAL B 1 31  ? -64.907  29.436 -70.150 1.00 48.77 ? 31   VAL B CG2 1 
ATOM   2557 N N   . THR B 1 32  ? -66.979  26.668 -66.763 1.00 52.98 ? 32   THR B N   1 
ATOM   2558 C CA  . THR B 1 32  ? -67.354  26.354 -65.391 1.00 55.74 ? 32   THR B CA  1 
ATOM   2559 C C   . THR B 1 32  ? -66.331  25.531 -64.621 1.00 57.60 ? 32   THR B C   1 
ATOM   2560 O O   . THR B 1 32  ? -66.074  24.380 -64.953 1.00 59.35 ? 32   THR B O   1 
ATOM   2561 C CB  . THR B 1 32  ? -68.698  25.590 -65.359 1.00 54.38 ? 32   THR B CB  1 
ATOM   2562 O OG1 . THR B 1 32  ? -69.694  26.353 -66.048 1.00 52.84 ? 32   THR B OG1 1 
ATOM   2563 C CG2 . THR B 1 32  ? -69.154  25.355 -63.925 1.00 54.65 ? 32   THR B CG2 1 
ATOM   2564 N N   . LYS B 1 33  ? -65.751  26.128 -63.587 1.00 60.05 ? 33   LYS B N   1 
ATOM   2565 C CA  . LYS B 1 33  ? -64.781  25.429 -62.748 1.00 61.96 ? 33   LYS B CA  1 
ATOM   2566 C C   . LYS B 1 33  ? -65.426  25.205 -61.378 1.00 62.77 ? 33   LYS B C   1 
ATOM   2567 O O   . LYS B 1 33  ? -66.058  26.107 -60.825 1.00 62.77 ? 33   LYS B O   1 
ATOM   2568 C CB  . LYS B 1 33  ? -63.498  26.251 -62.609 1.00 61.77 ? 33   LYS B CB  1 
ATOM   2569 C CG  . LYS B 1 33  ? -62.828  26.599 -63.940 1.00 63.29 ? 33   LYS B CG  1 
ATOM   2570 C CD  . LYS B 1 33  ? -62.594  25.368 -64.817 1.00 63.02 ? 33   LYS B CD  1 
ATOM   2571 C CE  . LYS B 1 33  ? -61.930  25.759 -66.136 1.00 63.11 ? 33   LYS B CE  1 
ATOM   2572 N NZ  . LYS B 1 33  ? -61.829  24.625 -67.096 1.00 62.79 ? 33   LYS B NZ  1 
ATOM   2573 N N   . LYS B 1 34  ? -65.281  24.003 -60.831 1.00 63.12 ? 34   LYS B N   1 
ATOM   2574 C CA  . LYS B 1 34  ? -65.895  23.697 -59.542 1.00 63.84 ? 34   LYS B CA  1 
ATOM   2575 C C   . LYS B 1 34  ? -64.887  23.150 -58.535 1.00 63.69 ? 34   LYS B C   1 
ATOM   2576 O O   . LYS B 1 34  ? -64.035  22.337 -58.885 1.00 64.33 ? 34   LYS B O   1 
ATOM   2577 C CB  . LYS B 1 34  ? -67.014  22.677 -59.748 1.00 65.11 ? 34   LYS B CB  1 
ATOM   2578 C CG  . LYS B 1 34  ? -68.056  22.647 -58.655 1.00 66.49 ? 34   LYS B CG  1 
ATOM   2579 C CD  . LYS B 1 34  ? -69.417  23.109 -59.181 1.00 68.78 ? 34   LYS B CD  1 
ATOM   2580 C CE  . LYS B 1 34  ? -69.966  22.167 -60.250 1.00 69.63 ? 34   LYS B CE  1 
ATOM   2581 N NZ  . LYS B 1 34  ? -71.309  22.592 -60.747 1.00 69.27 ? 34   LYS B NZ  1 
ATOM   2582 N N   . PHE B 1 35  ? -64.993  23.591 -57.285 1.00 63.05 ? 35   PHE B N   1 
ATOM   2583 C CA  . PHE B 1 35  ? -64.087  23.139 -56.234 1.00 62.26 ? 35   PHE B CA  1 
ATOM   2584 C C   . PHE B 1 35  ? -64.618  21.942 -55.467 1.00 62.16 ? 35   PHE B C   1 
ATOM   2585 O O   . PHE B 1 35  ? -65.766  21.536 -55.649 1.00 60.57 ? 35   PHE B O   1 
ATOM   2586 C CB  . PHE B 1 35  ? -63.802  24.276 -55.254 1.00 63.39 ? 35   PHE B CB  1 
ATOM   2587 C CG  . PHE B 1 35  ? -62.953  25.362 -55.831 1.00 64.66 ? 35   PHE B CG  1 
ATOM   2588 C CD1 . PHE B 1 35  ? -63.486  26.276 -56.730 1.00 65.36 ? 35   PHE B CD1 1 
ATOM   2589 C CD2 . PHE B 1 35  ? -61.600  25.446 -55.508 1.00 65.82 ? 35   PHE B CD2 1 
ATOM   2590 C CE1 . PHE B 1 35  ? -62.684  27.256 -57.303 1.00 66.07 ? 35   PHE B CE1 1 
ATOM   2591 C CE2 . PHE B 1 35  ? -60.791  26.423 -56.078 1.00 66.50 ? 35   PHE B CE2 1 
ATOM   2592 C CZ  . PHE B 1 35  ? -61.335  27.330 -56.977 1.00 66.52 ? 35   PHE B CZ  1 
ATOM   2593 N N   . SER B 1 36  ? -63.776  21.384 -54.600 1.00 62.52 ? 36   SER B N   1 
ATOM   2594 C CA  . SER B 1 36  ? -64.149  20.213 -53.801 1.00 63.43 ? 36   SER B CA  1 
ATOM   2595 C C   . SER B 1 36  ? -65.343  20.489 -52.892 1.00 62.59 ? 36   SER B C   1 
ATOM   2596 O O   . SER B 1 36  ? -66.222  19.641 -52.731 1.00 62.83 ? 36   SER B O   1 
ATOM   2597 C CB  . SER B 1 36  ? -62.964  19.756 -52.959 1.00 63.84 ? 36   SER B CB  1 
ATOM   2598 O OG  . SER B 1 36  ? -62.525  20.814 -52.127 1.00 67.77 ? 36   SER B OG  1 
ATOM   2599 N N   . ASN B 1 37  ? -65.370  21.676 -52.297 1.00 60.85 ? 37   ASN B N   1 
ATOM   2600 C CA  . ASN B 1 37  ? -66.471  22.053 -51.418 1.00 58.92 ? 37   ASN B CA  1 
ATOM   2601 C C   . ASN B 1 37  ? -67.687  22.445 -52.249 1.00 57.21 ? 37   ASN B C   1 
ATOM   2602 O O   . ASN B 1 37  ? -68.665  22.982 -51.730 1.00 57.02 ? 37   ASN B O   1 
ATOM   2603 C CB  . ASN B 1 37  ? -66.044  23.215 -50.521 1.00 61.40 ? 37   ASN B CB  1 
ATOM   2604 C CG  . ASN B 1 37  ? -65.150  24.201 -51.240 1.00 64.24 ? 37   ASN B CG  1 
ATOM   2605 O OD1 . ASN B 1 37  ? -64.061  23.847 -51.709 1.00 65.57 ? 37   ASN B OD1 1 
ATOM   2606 N ND2 . ASN B 1 37  ? -65.600  25.447 -51.335 1.00 64.81 ? 37   ASN B ND2 1 
ATOM   2607 N N   . GLN B 1 38  ? -67.606  22.164 -53.545 1.00 54.67 ? 38   GLN B N   1 
ATOM   2608 C CA  . GLN B 1 38  ? -68.661  22.470 -54.498 1.00 52.52 ? 38   GLN B CA  1 
ATOM   2609 C C   . GLN B 1 38  ? -68.847  23.951 -54.759 1.00 50.38 ? 38   GLN B C   1 
ATOM   2610 O O   . GLN B 1 38  ? -69.874  24.362 -55.290 1.00 49.73 ? 38   GLN B O   1 
ATOM   2611 C CB  . GLN B 1 38  ? -69.990  21.857 -54.062 1.00 54.63 ? 38   GLN B CB  1 
ATOM   2612 C CG  . GLN B 1 38  ? -70.191  20.435 -54.553 1.00 56.54 ? 38   GLN B CG  1 
ATOM   2613 C CD  . GLN B 1 38  ? -70.137  20.333 -56.072 1.00 57.26 ? 38   GLN B CD  1 
ATOM   2614 O OE1 . GLN B 1 38  ? -69.074  20.462 -56.682 1.00 58.90 ? 38   GLN B OE1 1 
ATOM   2615 N NE2 . GLN B 1 38  ? -71.288  20.113 -56.688 1.00 58.01 ? 38   GLN B NE2 1 
ATOM   2616 N N   . GLU B 1 39  ? -67.858  24.758 -54.384 1.00 46.50 ? 39   GLU B N   1 
ATOM   2617 C CA  . GLU B 1 39  ? -67.935  26.195 -54.627 1.00 43.77 ? 39   GLU B CA  1 
ATOM   2618 C C   . GLU B 1 39  ? -67.873  26.406 -56.132 1.00 43.85 ? 39   GLU B C   1 
ATOM   2619 O O   . GLU B 1 39  ? -66.849  26.143 -56.764 1.00 42.77 ? 39   GLU B O   1 
ATOM   2620 C CB  . GLU B 1 39  ? -66.780  26.903 -53.935 1.00 41.62 ? 39   GLU B CB  1 
ATOM   2621 C CG  . GLU B 1 39  ? -66.642  28.357 -54.316 1.00 41.64 ? 39   GLU B CG  1 
ATOM   2622 C CD  . GLU B 1 39  ? -65.646  29.081 -53.431 1.00 44.40 ? 39   GLU B CD  1 
ATOM   2623 O OE1 . GLU B 1 39  ? -65.212  30.204 -53.791 1.00 43.33 ? 39   GLU B OE1 1 
ATOM   2624 O OE2 . GLU B 1 39  ? -65.303  28.521 -52.367 1.00 43.18 ? 39   GLU B OE2 1 
ATOM   2625 N N   . THR B 1 40  ? -68.974  26.897 -56.688 1.00 44.39 ? 40   THR B N   1 
ATOM   2626 C CA  . THR B 1 40  ? -69.107  27.102 -58.120 1.00 45.10 ? 40   THR B CA  1 
ATOM   2627 C C   . THR B 1 40  ? -68.422  28.327 -58.708 1.00 44.14 ? 40   THR B C   1 
ATOM   2628 O O   . THR B 1 40  ? -68.585  29.445 -58.222 1.00 42.73 ? 40   THR B O   1 
ATOM   2629 C CB  . THR B 1 40  ? -70.594  27.173 -58.500 1.00 46.82 ? 40   THR B CB  1 
ATOM   2630 O OG1 . THR B 1 40  ? -71.299  26.125 -57.829 1.00 48.66 ? 40   THR B OG1 1 
ATOM   2631 C CG2 . THR B 1 40  ? -70.783  27.007 -60.011 1.00 47.06 ? 40   THR B CG2 1 
ATOM   2632 N N   . CYS B 1 41  ? -67.661  28.099 -59.770 1.00 44.94 ? 41   CYS B N   1 
ATOM   2633 C CA  . CYS B 1 41  ? -66.965  29.164 -60.480 1.00 46.65 ? 41   CYS B CA  1 
ATOM   2634 C C   . CYS B 1 41  ? -67.586  29.180 -61.870 1.00 46.13 ? 41   CYS B C   1 
ATOM   2635 O O   . CYS B 1 41  ? -67.830  28.129 -62.459 1.00 46.67 ? 41   CYS B O   1 
ATOM   2636 C CB  . CYS B 1 41  ? -65.468  28.861 -60.577 1.00 50.32 ? 41   CYS B CB  1 
ATOM   2637 S SG  . CYS B 1 41  ? -64.606  28.832 -58.988 1.00 55.84 ? 41   CYS B SG  1 
ATOM   2638 N N   . VAL B 1 42  ? -67.865  30.371 -62.380 1.00 45.21 ? 42   VAL B N   1 
ATOM   2639 C CA  . VAL B 1 42  ? -68.470  30.513 -63.688 1.00 43.53 ? 42   VAL B CA  1 
ATOM   2640 C C   . VAL B 1 42  ? -67.840  31.662 -64.443 1.00 43.55 ? 42   VAL B C   1 
ATOM   2641 O O   . VAL B 1 42  ? -67.383  32.637 -63.849 1.00 43.92 ? 42   VAL B O   1 
ATOM   2642 C CB  . VAL B 1 42  ? -69.992  30.761 -63.566 1.00 44.57 ? 42   VAL B CB  1 
ATOM   2643 C CG1 . VAL B 1 42  ? -70.556  31.279 -64.873 1.00 42.88 ? 42   VAL B CG1 1 
ATOM   2644 C CG2 . VAL B 1 42  ? -70.692  29.473 -63.176 1.00 46.73 ? 42   VAL B CG2 1 
ATOM   2645 N N   . GLU B 1 43  ? -67.812  31.538 -65.762 1.00 41.56 ? 43   GLU B N   1 
ATOM   2646 C CA  . GLU B 1 43  ? -67.253  32.572 -66.601 1.00 41.02 ? 43   GLU B CA  1 
ATOM   2647 C C   . GLU B 1 43  ? -67.989  32.533 -67.932 1.00 40.09 ? 43   GLU B C   1 
ATOM   2648 O O   . GLU B 1 43  ? -68.008  31.507 -68.610 1.00 38.98 ? 43   GLU B O   1 
ATOM   2649 C CB  . GLU B 1 43  ? -65.766  32.316 -66.817 1.00 44.47 ? 43   GLU B CB  1 
ATOM   2650 C CG  . GLU B 1 43  ? -65.027  33.459 -67.479 1.00 49.11 ? 43   GLU B CG  1 
ATOM   2651 C CD  . GLU B 1 43  ? -63.659  33.043 -67.986 1.00 53.66 ? 43   GLU B CD  1 
ATOM   2652 O OE1 . GLU B 1 43  ? -62.895  32.429 -67.206 1.00 55.47 ? 43   GLU B OE1 1 
ATOM   2653 O OE2 . GLU B 1 43  ? -63.347  33.334 -69.163 1.00 55.57 ? 43   GLU B OE2 1 
ATOM   2654 N N   . ILE B 1 44  ? -68.612  33.646 -68.297 1.00 37.45 ? 44   ILE B N   1 
ATOM   2655 C CA  . ILE B 1 44  ? -69.337  33.719 -69.559 1.00 35.32 ? 44   ILE B CA  1 
ATOM   2656 C C   . ILE B 1 44  ? -68.300  33.807 -70.680 1.00 35.63 ? 44   ILE B C   1 
ATOM   2657 O O   . ILE B 1 44  ? -67.593  34.807 -70.818 1.00 36.11 ? 44   ILE B O   1 
ATOM   2658 C CB  . ILE B 1 44  ? -70.266  34.947 -69.585 1.00 35.25 ? 44   ILE B CB  1 
ATOM   2659 C CG1 . ILE B 1 44  ? -71.165  34.945 -68.341 1.00 33.01 ? 44   ILE B CG1 1 
ATOM   2660 C CG2 . ILE B 1 44  ? -71.118  34.927 -70.848 1.00 34.12 ? 44   ILE B CG2 1 
ATOM   2661 C CD1 . ILE B 1 44  ? -72.003  33.672 -68.176 1.00 32.58 ? 44   ILE B CD1 1 
ATOM   2662 N N   . GLY B 1 45  ? -68.216  32.740 -71.468 1.00 32.90 ? 45   GLY B N   1 
ATOM   2663 C CA  . GLY B 1 45  ? -67.252  32.674 -72.543 1.00 31.88 ? 45   GLY B CA  1 
ATOM   2664 C C   . GLY B 1 45  ? -67.494  33.562 -73.744 1.00 33.80 ? 45   GLY B C   1 
ATOM   2665 O O   . GLY B 1 45  ? -66.723  33.518 -74.699 1.00 35.11 ? 45   GLY B O   1 
ATOM   2666 N N   . GLU B 1 46  ? -68.561  34.350 -73.718 1.00 33.36 ? 46   GLU B N   1 
ATOM   2667 C CA  . GLU B 1 46  ? -68.844  35.260 -74.819 1.00 32.86 ? 46   GLU B CA  1 
ATOM   2668 C C   . GLU B 1 46  ? -69.551  36.494 -74.304 1.00 31.06 ? 46   GLU B C   1 
ATOM   2669 O O   . GLU B 1 46  ? -70.157  36.484 -73.235 1.00 31.15 ? 46   GLU B O   1 
ATOM   2670 C CB  . GLU B 1 46  ? -69.700  34.582 -75.897 1.00 33.52 ? 46   GLU B CB  1 
ATOM   2671 C CG  . GLU B 1 46  ? -70.915  33.843 -75.368 1.00 36.91 ? 46   GLU B CG  1 
ATOM   2672 C CD  . GLU B 1 46  ? -71.649  33.047 -76.447 1.00 39.07 ? 46   GLU B CD  1 
ATOM   2673 O OE1 . GLU B 1 46  ? -72.491  33.626 -77.166 1.00 38.44 ? 46   GLU B OE1 1 
ATOM   2674 O OE2 . GLU B 1 46  ? -71.377  31.837 -76.574 1.00 38.78 ? 46   GLU B OE2 1 
ATOM   2675 N N   . SER B 1 47  ? -69.478  37.561 -75.083 1.00 30.10 ? 47   SER B N   1 
ATOM   2676 C CA  . SER B 1 47  ? -70.103  38.818 -74.707 1.00 27.25 ? 47   SER B CA  1 
ATOM   2677 C C   . SER B 1 47  ? -71.620  38.715 -74.726 1.00 27.65 ? 47   SER B C   1 
ATOM   2678 O O   . SER B 1 47  ? -72.190  38.111 -75.638 1.00 26.10 ? 47   SER B O   1 
ATOM   2679 C CB  . SER B 1 47  ? -69.658  39.917 -75.667 1.00 27.90 ? 47   SER B CB  1 
ATOM   2680 O OG  . SER B 1 47  ? -70.377  41.117 -75.445 1.00 25.39 ? 47   SER B OG  1 
ATOM   2681 N N   . VAL B 1 48  ? -72.276  39.291 -73.719 1.00 23.24 ? 48   VAL B N   1 
ATOM   2682 C CA  . VAL B 1 48  ? -73.737  39.278 -73.661 1.00 23.17 ? 48   VAL B CA  1 
ATOM   2683 C C   . VAL B 1 48  ? -74.218  40.729 -73.594 1.00 23.68 ? 48   VAL B C   1 
ATOM   2684 O O   . VAL B 1 48  ? -75.385  41.012 -73.308 1.00 24.81 ? 48   VAL B O   1 
ATOM   2685 C CB  . VAL B 1 48  ? -74.244  38.519 -72.401 1.00 21.57 ? 48   VAL B CB  1 
ATOM   2686 C CG1 . VAL B 1 48  ? -73.877  37.040 -72.495 1.00 23.00 ? 48   VAL B CG1 1 
ATOM   2687 C CG2 . VAL B 1 48  ? -73.661  39.141 -71.137 1.00 21.19 ? 48   VAL B CG2 1 
ATOM   2688 N N   . ARG B 1 49  ? -73.304  41.645 -73.881 1.00 24.71 ? 49   ARG B N   1 
ATOM   2689 C CA  . ARG B 1 49  ? -73.582  43.071 -73.806 1.00 27.09 ? 49   ARG B CA  1 
ATOM   2690 C C   . ARG B 1 49  ? -74.746  43.532 -74.677 1.00 27.66 ? 49   ARG B C   1 
ATOM   2691 O O   . ARG B 1 49  ? -74.746  43.357 -75.893 1.00 25.63 ? 49   ARG B O   1 
ATOM   2692 C CB  . ARG B 1 49  ? -72.321  43.868 -74.164 1.00 25.00 ? 49   ARG B CB  1 
ATOM   2693 C CG  . ARG B 1 49  ? -72.430  45.361 -73.877 1.00 25.03 ? 49   ARG B CG  1 
ATOM   2694 C CD  . ARG B 1 49  ? -71.089  46.084 -74.061 1.00 23.13 ? 49   ARG B CD  1 
ATOM   2695 N NE  . ARG B 1 49  ? -70.055  45.610 -73.139 1.00 21.49 ? 49   ARG B NE  1 
ATOM   2696 C CZ  . ARG B 1 49  ? -69.742  46.193 -71.980 1.00 24.31 ? 49   ARG B CZ  1 
ATOM   2697 N NH1 . ARG B 1 49  ? -70.375  47.282 -71.580 1.00 22.93 ? 49   ARG B NH1 1 
ATOM   2698 N NH2 . ARG B 1 49  ? -68.782  45.689 -71.216 1.00 21.70 ? 49   ARG B NH2 1 
ATOM   2699 N N   . GLY B 1 50  ? -75.732  44.152 -74.045 1.00 28.21 ? 50   GLY B N   1 
ATOM   2700 C CA  . GLY B 1 50  ? -76.883  44.621 -74.786 1.00 29.07 ? 50   GLY B CA  1 
ATOM   2701 C C   . GLY B 1 50  ? -77.764  43.510 -75.323 1.00 31.03 ? 50   GLY B C   1 
ATOM   2702 O O   . GLY B 1 50  ? -78.589  43.773 -76.183 1.00 30.69 ? 50   GLY B O   1 
ATOM   2703 N N   . GLU B 1 51  ? -77.597  42.277 -74.854 1.00 31.62 ? 51   GLU B N   1 
ATOM   2704 C CA  . GLU B 1 51  ? -78.413  41.170 -75.359 1.00 30.67 ? 51   GLU B CA  1 
ATOM   2705 C C   . GLU B 1 51  ? -79.492  40.600 -74.439 1.00 29.36 ? 51   GLU B C   1 
ATOM   2706 O O   . GLU B 1 51  ? -79.417  40.724 -73.221 1.00 27.24 ? 51   GLU B O   1 
ATOM   2707 C CB  . GLU B 1 51  ? -77.496  40.052 -75.762 1.00 31.82 ? 51   GLU B CB  1 
ATOM   2708 C CG  . GLU B 1 51  ? -76.653  40.440 -76.929 1.00 40.64 ? 51   GLU B CG  1 
ATOM   2709 C CD  . GLU B 1 51  ? -75.738  39.331 -77.324 1.00 44.79 ? 51   GLU B CD  1 
ATOM   2710 O OE1 . GLU B 1 51  ? -75.139  39.432 -78.418 1.00 49.47 ? 51   GLU B OE1 1 
ATOM   2711 O OE2 . GLU B 1 51  ? -75.617  38.359 -76.532 1.00 48.26 ? 51   GLU B OE2 1 
ATOM   2712 N N   . ASP B 1 52  ? -80.472  39.937 -75.055 1.00 28.22 ? 52   ASP B N   1 
ATOM   2713 C CA  . ASP B 1 52  ? -81.616  39.307 -74.370 1.00 27.55 ? 52   ASP B CA  1 
ATOM   2714 C C   . ASP B 1 52  ? -81.169  37.899 -73.972 1.00 27.29 ? 52   ASP B C   1 
ATOM   2715 O O   . ASP B 1 52  ? -81.163  36.969 -74.785 1.00 24.85 ? 52   ASP B O   1 
ATOM   2716 C CB  . ASP B 1 52  ? -82.825  39.261 -75.328 1.00 27.16 ? 52   ASP B CB  1 
ATOM   2717 C CG  . ASP B 1 52  ? -84.140  38.937 -74.623 1.00 29.26 ? 52   ASP B CG  1 
ATOM   2718 O OD1 . ASP B 1 52  ? -84.272  39.249 -73.418 1.00 29.32 ? 52   ASP B OD1 1 
ATOM   2719 O OD2 . ASP B 1 52  ? -85.058  38.384 -75.274 1.00 30.22 ? 52   ASP B OD2 1 
ATOM   2720 N N   . VAL B 1 53  ? -80.799  37.752 -72.704 1.00 27.01 ? 53   VAL B N   1 
ATOM   2721 C CA  . VAL B 1 53  ? -80.278  36.489 -72.196 1.00 24.35 ? 53   VAL B CA  1 
ATOM   2722 C C   . VAL B 1 53  ? -81.276  35.561 -71.500 1.00 26.22 ? 53   VAL B C   1 
ATOM   2723 O O   . VAL B 1 53  ? -82.121  35.994 -70.714 1.00 28.65 ? 53   VAL B O   1 
ATOM   2724 C CB  . VAL B 1 53  ? -79.089  36.770 -71.231 1.00 23.13 ? 53   VAL B CB  1 
ATOM   2725 C CG1 . VAL B 1 53  ? -78.477  35.454 -70.711 1.00 21.22 ? 53   VAL B CG1 1 
ATOM   2726 C CG2 . VAL B 1 53  ? -78.025  37.593 -71.961 1.00 23.47 ? 53   VAL B CG2 1 
ATOM   2727 N N   . TYR B 1 54  ? -81.151  34.271 -71.786 1.00 24.85 ? 54   TYR B N   1 
ATOM   2728 C CA  . TYR B 1 54  ? -81.992  33.266 -71.168 1.00 23.93 ? 54   TYR B CA  1 
ATOM   2729 C C   . TYR B 1 54  ? -81.055  32.209 -70.582 1.00 24.91 ? 54   TYR B C   1 
ATOM   2730 O O   . TYR B 1 54  ? -80.179  31.688 -71.277 1.00 26.62 ? 54   TYR B O   1 
ATOM   2731 C CB  . TYR B 1 54  ? -82.940  32.653 -72.208 1.00 22.78 ? 54   TYR B CB  1 
ATOM   2732 C CG  . TYR B 1 54  ? -83.924  33.663 -72.773 1.00 20.97 ? 54   TYR B CG  1 
ATOM   2733 C CD1 . TYR B 1 54  ? -83.544  34.554 -73.783 1.00 20.58 ? 54   TYR B CD1 1 
ATOM   2734 C CD2 . TYR B 1 54  ? -85.214  33.776 -72.244 1.00 17.92 ? 54   TYR B CD2 1 
ATOM   2735 C CE1 . TYR B 1 54  ? -84.422  35.534 -74.250 1.00 20.01 ? 54   TYR B CE1 1 
ATOM   2736 C CE2 . TYR B 1 54  ? -86.095  34.747 -72.699 1.00 20.09 ? 54   TYR B CE2 1 
ATOM   2737 C CZ  . TYR B 1 54  ? -85.699  35.620 -73.699 1.00 21.20 ? 54   TYR B CZ  1 
ATOM   2738 O OH  . TYR B 1 54  ? -86.588  36.562 -74.160 1.00 22.21 ? 54   TYR B OH  1 
ATOM   2739 N N   . ILE B 1 55  ? -81.216  31.929 -69.294 1.00 23.94 ? 55   ILE B N   1 
ATOM   2740 C CA  . ILE B 1 55  ? -80.405  30.927 -68.601 1.00 23.49 ? 55   ILE B CA  1 
ATOM   2741 C C   . ILE B 1 55  ? -81.364  29.839 -68.134 1.00 24.47 ? 55   ILE B C   1 
ATOM   2742 O O   . ILE B 1 55  ? -82.290  30.108 -67.369 1.00 25.07 ? 55   ILE B O   1 
ATOM   2743 C CB  . ILE B 1 55  ? -79.693  31.518 -67.361 1.00 21.91 ? 55   ILE B CB  1 
ATOM   2744 C CG1 . ILE B 1 55  ? -78.793  32.677 -67.786 1.00 20.92 ? 55   ILE B CG1 1 
ATOM   2745 C CG2 . ILE B 1 55  ? -78.867  30.415 -66.642 1.00 18.45 ? 55   ILE B CG2 1 
ATOM   2746 C CD1 . ILE B 1 55  ? -78.237  33.455 -66.613 1.00 22.83 ? 55   ILE B CD1 1 
ATOM   2747 N N   . VAL B 1 56  ? -81.141  28.621 -68.615 1.00 26.41 ? 56   VAL B N   1 
ATOM   2748 C CA  . VAL B 1 56  ? -81.979  27.474 -68.286 1.00 29.66 ? 56   VAL B CA  1 
ATOM   2749 C C   . VAL B 1 56  ? -81.322  26.684 -67.159 1.00 32.96 ? 56   VAL B C   1 
ATOM   2750 O O   . VAL B 1 56  ? -80.206  26.190 -67.319 1.00 31.36 ? 56   VAL B O   1 
ATOM   2751 C CB  . VAL B 1 56  ? -82.153  26.563 -69.528 1.00 29.12 ? 56   VAL B CB  1 
ATOM   2752 C CG1 . VAL B 1 56  ? -83.179  25.467 -69.256 1.00 28.78 ? 56   VAL B CG1 1 
ATOM   2753 C CG2 . VAL B 1 56  ? -82.583  27.403 -70.723 1.00 28.92 ? 56   VAL B CG2 1 
ATOM   2754 N N   . GLN B 1 57  ? -82.013  26.577 -66.024 1.00 37.23 ? 57   GLN B N   1 
ATOM   2755 C CA  . GLN B 1 57  ? -81.490  25.866 -64.856 1.00 43.50 ? 57   GLN B CA  1 
ATOM   2756 C C   . GLN B 1 57  ? -81.118  24.423 -65.152 1.00 46.66 ? 57   GLN B C   1 
ATOM   2757 O O   . GLN B 1 57  ? -81.873  23.699 -65.800 1.00 47.99 ? 57   GLN B O   1 
ATOM   2758 C CB  . GLN B 1 57  ? -82.505  25.884 -63.711 1.00 46.97 ? 57   GLN B CB  1 
ATOM   2759 C CG  . GLN B 1 57  ? -81.986  25.223 -62.429 1.00 50.42 ? 57   GLN B CG  1 
ATOM   2760 C CD  . GLN B 1 57  ? -82.969  25.318 -61.269 1.00 53.47 ? 57   GLN B CD  1 
ATOM   2761 O OE1 . GLN B 1 57  ? -84.030  24.683 -61.273 1.00 53.74 ? 57   GLN B OE1 1 
ATOM   2762 N NE2 . GLN B 1 57  ? -82.620  26.122 -60.268 1.00 54.59 ? 57   GLN B NE2 1 
ATOM   2763 N N   . SER B 1 58  ? -79.959  24.011 -64.647 1.00 50.63 ? 58   SER B N   1 
ATOM   2764 C CA  . SER B 1 58  ? -79.446  22.655 -64.851 1.00 54.73 ? 58   SER B CA  1 
ATOM   2765 C C   . SER B 1 58  ? -80.287  21.577 -64.171 1.00 56.05 ? 58   SER B C   1 
ATOM   2766 O O   . SER B 1 58  ? -81.119  21.871 -63.321 1.00 57.41 ? 58   SER B O   1 
ATOM   2767 C CB  . SER B 1 58  ? -78.003  22.568 -64.345 1.00 55.27 ? 58   SER B CB  1 
ATOM   2768 O OG  . SER B 1 58  ? -77.490  21.258 -64.490 1.00 57.61 ? 58   SER B OG  1 
ATOM   2769 N N   . GLY B 1 59  ? -80.064  20.324 -64.553 1.00 58.75 ? 59   GLY B N   1 
ATOM   2770 C CA  . GLY B 1 59  ? -80.811  19.229 -63.958 1.00 61.24 ? 59   GLY B CA  1 
ATOM   2771 C C   . GLY B 1 59  ? -79.966  18.321 -63.075 1.00 62.11 ? 59   GLY B C   1 
ATOM   2772 O O   . GLY B 1 59  ? -80.376  17.201 -62.765 1.00 63.68 ? 59   GLY B O   1 
ATOM   2773 N N   . CYS B 1 60  ? -78.795  18.811 -62.667 1.00 62.21 ? 60   CYS B N   1 
ATOM   2774 C CA  . CYS B 1 60  ? -77.857  18.064 -61.821 1.00 61.10 ? 60   CYS B CA  1 
ATOM   2775 C C   . CYS B 1 60  ? -78.465  17.156 -60.763 1.00 59.89 ? 60   CYS B C   1 
ATOM   2776 O O   . CYS B 1 60  ? -78.041  16.008 -60.603 1.00 60.63 ? 60   CYS B O   1 
ATOM   2777 C CB  . CYS B 1 60  ? -76.899  19.023 -61.119 1.00 62.38 ? 60   CYS B CB  1 
ATOM   2778 S SG  . CYS B 1 60  ? -76.392  18.446 -59.467 1.00 66.28 ? 60   CYS B SG  1 
ATOM   2779 N N   . GLY B 1 61  ? -79.437  17.683 -60.026 1.00 57.04 ? 61   GLY B N   1 
ATOM   2780 C CA  . GLY B 1 61  ? -80.065  16.908 -58.974 1.00 52.33 ? 61   GLY B CA  1 
ATOM   2781 C C   . GLY B 1 61  ? -79.846  17.564 -57.624 1.00 48.79 ? 61   GLY B C   1 
ATOM   2782 O O   . GLY B 1 61  ? -80.765  17.617 -56.808 1.00 49.50 ? 61   GLY B O   1 
ATOM   2783 N N   . GLU B 1 62  ? -78.635  18.068 -57.386 1.00 42.76 ? 62   GLU B N   1 
ATOM   2784 C CA  . GLU B 1 62  ? -78.323  18.731 -56.120 1.00 38.24 ? 62   GLU B CA  1 
ATOM   2785 C C   . GLU B 1 62  ? -78.921  20.128 -56.221 1.00 34.03 ? 62   GLU B C   1 
ATOM   2786 O O   . GLU B 1 62  ? -78.334  21.019 -56.835 1.00 31.23 ? 62   GLU B O   1 
ATOM   2787 C CB  . GLU B 1 62  ? -76.812  18.801 -55.928 1.00 37.53 ? 62   GLU B CB  1 
ATOM   2788 C CG  . GLU B 1 62  ? -76.350  18.567 -54.499 1.00 38.74 ? 62   GLU B CG  1 
ATOM   2789 C CD  . GLU B 1 62  ? -76.675  19.715 -53.556 1.00 39.64 ? 62   GLU B CD  1 
ATOM   2790 O OE1 . GLU B 1 62  ? -77.144  20.777 -54.027 1.00 37.91 ? 62   GLU B OE1 1 
ATOM   2791 O OE2 . GLU B 1 62  ? -76.447  19.551 -52.336 1.00 39.02 ? 62   GLU B OE2 1 
ATOM   2792 N N   . ILE B 1 63  ? -80.089  20.308 -55.606 1.00 29.84 ? 63   ILE B N   1 
ATOM   2793 C CA  . ILE B 1 63  ? -80.815  21.567 -55.682 1.00 29.59 ? 63   ILE B CA  1 
ATOM   2794 C C   . ILE B 1 63  ? -80.095  22.835 -55.224 1.00 28.12 ? 63   ILE B C   1 
ATOM   2795 O O   . ILE B 1 63  ? -80.309  23.900 -55.794 1.00 28.74 ? 63   ILE B O   1 
ATOM   2796 C CB  . ILE B 1 63  ? -82.178  21.458 -54.951 1.00 31.21 ? 63   ILE B CB  1 
ATOM   2797 C CG1 . ILE B 1 63  ? -83.069  22.632 -55.349 1.00 31.19 ? 63   ILE B CG1 1 
ATOM   2798 C CG2 . ILE B 1 63  ? -81.976  21.437 -53.452 1.00 32.97 ? 63   ILE B CG2 1 
ATOM   2799 C CD1 . ILE B 1 63  ? -84.410  22.652 -54.652 1.00 36.29 ? 63   ILE B CD1 1 
ATOM   2800 N N   . ASN B 1 64  ? -79.242  22.745 -54.212 1.00 26.97 ? 64   ASN B N   1 
ATOM   2801 C CA  . ASN B 1 64  ? -78.547  23.944 -53.764 1.00 27.35 ? 64   ASN B CA  1 
ATOM   2802 C C   . ASN B 1 64  ? -77.397  24.303 -54.707 1.00 26.88 ? 64   ASN B C   1 
ATOM   2803 O O   . ASN B 1 64  ? -77.123  25.484 -54.934 1.00 26.55 ? 64   ASN B O   1 
ATOM   2804 C CB  . ASN B 1 64  ? -78.057  23.770 -52.328 1.00 24.10 ? 64   ASN B CB  1 
ATOM   2805 C CG  . ASN B 1 64  ? -79.204  23.561 -51.352 1.00 24.17 ? 64   ASN B CG  1 
ATOM   2806 O OD1 . ASN B 1 64  ? -79.122  22.725 -50.455 1.00 24.71 ? 64   ASN B OD1 1 
ATOM   2807 N ND2 . ASN B 1 64  ? -80.282  24.318 -51.529 1.00 16.12 ? 64   ASN B ND2 1 
ATOM   2808 N N   . ASP B 1 65  ? -76.725  23.299 -55.263 1.00 25.09 ? 65   ASP B N   1 
ATOM   2809 C CA  . ASP B 1 65  ? -75.639  23.584 -56.203 1.00 25.64 ? 65   ASP B CA  1 
ATOM   2810 C C   . ASP B 1 65  ? -76.253  24.240 -57.450 1.00 26.20 ? 65   ASP B C   1 
ATOM   2811 O O   . ASP B 1 65  ? -75.760  25.254 -57.942 1.00 24.76 ? 65   ASP B O   1 
ATOM   2812 C CB  . ASP B 1 65  ? -74.909  22.306 -56.625 1.00 24.14 ? 65   ASP B CB  1 
ATOM   2813 C CG  . ASP B 1 65  ? -74.118  21.676 -55.496 1.00 26.25 ? 65   ASP B CG  1 
ATOM   2814 O OD1 . ASP B 1 65  ? -73.795  22.363 -54.501 1.00 25.66 ? 65   ASP B OD1 1 
ATOM   2815 O OD2 . ASP B 1 65  ? -73.800  20.481 -55.615 1.00 29.19 ? 65   ASP B OD2 1 
ATOM   2816 N N   . ASN B 1 66  ? -77.343  23.655 -57.937 1.00 26.30 ? 66   ASN B N   1 
ATOM   2817 C CA  . ASN B 1 66  ? -78.033  24.154 -59.116 1.00 26.26 ? 66   ASN B CA  1 
ATOM   2818 C C   . ASN B 1 66  ? -78.567  25.563 -58.919 1.00 26.08 ? 66   ASN B C   1 
ATOM   2819 O O   . ASN B 1 66  ? -78.471  26.400 -59.814 1.00 25.21 ? 66   ASN B O   1 
ATOM   2820 C CB  . ASN B 1 66  ? -79.182  23.214 -59.493 1.00 27.81 ? 66   ASN B CB  1 
ATOM   2821 C CG  . ASN B 1 66  ? -78.690  21.852 -59.947 1.00 33.28 ? 66   ASN B CG  1 
ATOM   2822 O OD1 . ASN B 1 66  ? -77.656  21.743 -60.614 1.00 35.10 ? 66   ASN B OD1 1 
ATOM   2823 N ND2 . ASN B 1 66  ? -79.433  20.806 -59.602 1.00 34.93 ? 66   ASN B ND2 1 
ATOM   2824 N N   . LEU B 1 67  ? -79.135  25.825 -57.750 1.00 24.56 ? 67   LEU B N   1 
ATOM   2825 C CA  . LEU B 1 67  ? -79.664  27.150 -57.476 1.00 24.80 ? 67   LEU B CA  1 
ATOM   2826 C C   . LEU B 1 67  ? -78.549  28.189 -57.466 1.00 24.24 ? 67   LEU B C   1 
ATOM   2827 O O   . LEU B 1 67  ? -78.667  29.236 -58.108 1.00 23.50 ? 67   LEU B O   1 
ATOM   2828 C CB  . LEU B 1 67  ? -80.401  27.166 -56.138 1.00 23.14 ? 67   LEU B CB  1 
ATOM   2829 C CG  . LEU B 1 67  ? -80.927  28.520 -55.663 1.00 22.48 ? 67   LEU B CG  1 
ATOM   2830 C CD1 . LEU B 1 67  ? -81.881  29.115 -56.687 1.00 17.24 ? 67   LEU B CD1 1 
ATOM   2831 C CD2 . LEU B 1 67  ? -81.626  28.323 -54.319 1.00 22.46 ? 67   LEU B CD2 1 
ATOM   2832 N N   . MET B 1 68  ? -77.467  27.896 -56.751 1.00 23.61 ? 68   MET B N   1 
ATOM   2833 C CA  . MET B 1 68  ? -76.342  28.821 -56.677 1.00 25.66 ? 68   MET B CA  1 
ATOM   2834 C C   . MET B 1 68  ? -75.711  29.049 -58.043 1.00 25.47 ? 68   MET B C   1 
ATOM   2835 O O   . MET B 1 68  ? -75.331  30.174 -58.375 1.00 24.85 ? 68   MET B O   1 
ATOM   2836 C CB  . MET B 1 68  ? -75.269  28.307 -55.711 1.00 27.11 ? 68   MET B CB  1 
ATOM   2837 C CG  . MET B 1 68  ? -75.586  28.533 -54.239 1.00 31.03 ? 68   MET B CG  1 
ATOM   2838 S SD  . MET B 1 68  ? -76.000  30.257 -53.867 1.00 35.72 ? 68   MET B SD  1 
ATOM   2839 C CE  . MET B 1 68  ? -74.578  31.140 -54.597 1.00 23.65 ? 68   MET B CE  1 
ATOM   2840 N N   . GLU B 1 69  ? -75.587  27.981 -58.827 1.00 24.52 ? 69   GLU B N   1 
ATOM   2841 C CA  . GLU B 1 69  ? -74.993  28.102 -60.154 1.00 25.52 ? 69   GLU B CA  1 
ATOM   2842 C C   . GLU B 1 69  ? -75.865  29.022 -61.007 1.00 23.13 ? 69   GLU B C   1 
ATOM   2843 O O   . GLU B 1 69  ? -75.359  29.836 -61.770 1.00 22.86 ? 69   GLU B O   1 
ATOM   2844 C CB  . GLU B 1 69  ? -74.864  26.729 -60.823 1.00 26.70 ? 69   GLU B CB  1 
ATOM   2845 C CG  . GLU B 1 69  ? -74.193  26.777 -62.193 1.00 34.33 ? 69   GLU B CG  1 
ATOM   2846 C CD  . GLU B 1 69  ? -74.122  25.412 -62.870 1.00 38.22 ? 69   GLU B CD  1 
ATOM   2847 O OE1 . GLU B 1 69  ? -75.186  24.818 -63.155 1.00 40.67 ? 69   GLU B OE1 1 
ATOM   2848 O OE2 . GLU B 1 69  ? -72.998  24.931 -63.119 1.00 41.47 ? 69   GLU B OE2 1 
ATOM   2849 N N   . LEU B 1 70  ? -77.177  28.892 -60.868 1.00 20.51 ? 70   LEU B N   1 
ATOM   2850 C CA  . LEU B 1 70  ? -78.102  29.732 -61.620 1.00 21.35 ? 70   LEU B CA  1 
ATOM   2851 C C   . LEU B 1 70  ? -77.956  31.200 -61.209 1.00 21.53 ? 70   LEU B C   1 
ATOM   2852 O O   . LEU B 1 70  ? -77.875  32.091 -62.057 1.00 24.66 ? 70   LEU B O   1 
ATOM   2853 C CB  . LEU B 1 70  ? -79.535  29.261 -61.380 1.00 17.56 ? 70   LEU B CB  1 
ATOM   2854 C CG  . LEU B 1 70  ? -80.689  30.162 -61.834 1.00 20.91 ? 70   LEU B CG  1 
ATOM   2855 C CD1 . LEU B 1 70  ? -80.671  30.385 -63.350 1.00 16.07 ? 70   LEU B CD1 1 
ATOM   2856 C CD2 . LEU B 1 70  ? -81.984  29.503 -61.408 1.00 19.07 ? 70   LEU B CD2 1 
ATOM   2857 N N   . LEU B 1 71  ? -77.905  31.445 -59.904 1.00 20.87 ? 71   LEU B N   1 
ATOM   2858 C CA  . LEU B 1 71  ? -77.788  32.801 -59.390 1.00 20.73 ? 71   LEU B CA  1 
ATOM   2859 C C   . LEU B 1 71  ? -76.487  33.440 -59.833 1.00 21.32 ? 71   LEU B C   1 
ATOM   2860 O O   . LEU B 1 71  ? -76.458  34.607 -60.233 1.00 21.56 ? 71   LEU B O   1 
ATOM   2861 C CB  . LEU B 1 71  ? -77.872  32.795 -57.865 1.00 18.06 ? 71   LEU B CB  1 
ATOM   2862 C CG  . LEU B 1 71  ? -79.198  32.312 -57.259 1.00 22.61 ? 71   LEU B CG  1 
ATOM   2863 C CD1 . LEU B 1 71  ? -79.041  32.200 -55.752 1.00 23.37 ? 71   LEU B CD1 1 
ATOM   2864 C CD2 . LEU B 1 71  ? -80.333  33.264 -57.615 1.00 17.95 ? 71   LEU B CD2 1 
ATOM   2865 N N   . ILE B 1 72  ? -75.411  32.670 -59.753 1.00 22.18 ? 72   ILE B N   1 
ATOM   2866 C CA  . ILE B 1 72  ? -74.092  33.150 -60.149 1.00 23.73 ? 72   ILE B CA  1 
ATOM   2867 C C   . ILE B 1 72  ? -74.052  33.538 -61.625 1.00 24.36 ? 72   ILE B C   1 
ATOM   2868 O O   . ILE B 1 72  ? -73.517  34.596 -61.975 1.00 24.01 ? 72   ILE B O   1 
ATOM   2869 C CB  . ILE B 1 72  ? -73.021  32.086 -59.852 1.00 23.22 ? 72   ILE B CB  1 
ATOM   2870 C CG1 . ILE B 1 72  ? -72.829  31.973 -58.337 1.00 24.18 ? 72   ILE B CG1 1 
ATOM   2871 C CG2 . ILE B 1 72  ? -71.714  32.441 -60.549 1.00 25.95 ? 72   ILE B CG2 1 
ATOM   2872 C CD1 . ILE B 1 72  ? -71.988  30.798 -57.896 1.00 23.74 ? 72   ILE B CD1 1 
ATOM   2873 N N   . MET B 1 73  ? -74.626  32.693 -62.482 1.00 22.74 ? 73   MET B N   1 
ATOM   2874 C CA  . MET B 1 73  ? -74.665  32.972 -63.917 1.00 24.29 ? 73   MET B CA  1 
ATOM   2875 C C   . MET B 1 73  ? -75.488  34.221 -64.221 1.00 23.78 ? 73   MET B C   1 
ATOM   2876 O O   . MET B 1 73  ? -75.147  34.987 -65.119 1.00 25.76 ? 73   MET B O   1 
ATOM   2877 C CB  . MET B 1 73  ? -75.254  31.787 -64.687 1.00 26.90 ? 73   MET B CB  1 
ATOM   2878 C CG  . MET B 1 73  ? -74.373  30.564 -64.735 1.00 28.34 ? 73   MET B CG  1 
ATOM   2879 S SD  . MET B 1 73  ? -75.024  29.376 -65.927 1.00 37.46 ? 73   MET B SD  1 
ATOM   2880 C CE  . MET B 1 73  ? -76.332  28.670 -64.987 1.00 37.01 ? 73   MET B CE  1 
ATOM   2881 N N   . ILE B 1 74  ? -76.587  34.407 -63.490 1.00 23.90 ? 74   ILE B N   1 
ATOM   2882 C CA  . ILE B 1 74  ? -77.428  35.585 -63.663 1.00 22.97 ? 74   ILE B CA  1 
ATOM   2883 C C   . ILE B 1 74  ? -76.622  36.818 -63.261 1.00 24.14 ? 74   ILE B C   1 
ATOM   2884 O O   . ILE B 1 74  ? -76.682  37.848 -63.923 1.00 23.87 ? 74   ILE B O   1 
ATOM   2885 C CB  . ILE B 1 74  ? -78.707  35.525 -62.771 1.00 23.34 ? 74   ILE B CB  1 
ATOM   2886 C CG1 . ILE B 1 74  ? -79.709  34.526 -63.349 1.00 25.39 ? 74   ILE B CG1 1 
ATOM   2887 C CG2 . ILE B 1 74  ? -79.349  36.910 -62.665 1.00 22.72 ? 74   ILE B CG2 1 
ATOM   2888 C CD1 . ILE B 1 74  ? -80.866  34.199 -62.421 1.00 23.31 ? 74   ILE B CD1 1 
ATOM   2889 N N   . ASN B 1 75  ? -75.878  36.711 -62.164 1.00 24.36 ? 75   ASN B N   1 
ATOM   2890 C CA  . ASN B 1 75  ? -75.070  37.830 -61.683 1.00 25.31 ? 75   ASN B CA  1 
ATOM   2891 C C   . ASN B 1 75  ? -74.024  38.224 -62.729 1.00 24.37 ? 75   ASN B C   1 
ATOM   2892 O O   . ASN B 1 75  ? -73.876  39.393 -63.078 1.00 23.98 ? 75   ASN B O   1 
ATOM   2893 C CB  . ASN B 1 75  ? -74.359  37.444 -60.387 1.00 27.49 ? 75   ASN B CB  1 
ATOM   2894 C CG  . ASN B 1 75  ? -73.414  38.530 -59.890 1.00 31.60 ? 75   ASN B CG  1 
ATOM   2895 O OD1 . ASN B 1 75  ? -73.849  39.599 -59.477 1.00 31.51 ? 75   ASN B OD1 1 
ATOM   2896 N ND2 . ASN B 1 75  ? -72.112  38.256 -59.938 1.00 30.55 ? 75   ASN B ND2 1 
ATOM   2897 N N   . ALA B 1 76  ? -73.306  37.224 -63.221 1.00 23.70 ? 76   ALA B N   1 
ATOM   2898 C CA  . ALA B 1 76  ? -72.255  37.427 -64.205 1.00 22.01 ? 76   ALA B CA  1 
ATOM   2899 C C   . ALA B 1 76  ? -72.785  38.122 -65.453 1.00 22.61 ? 76   ALA B C   1 
ATOM   2900 O O   . ALA B 1 76  ? -72.191  39.088 -65.926 1.00 23.46 ? 76   ALA B O   1 
ATOM   2901 C CB  . ALA B 1 76  ? -71.632  36.096 -64.565 1.00 22.35 ? 76   ALA B CB  1 
ATOM   2902 N N   . CYS B 1 77  ? -73.908  37.648 -65.975 1.00 21.89 ? 77   CYS B N   1 
ATOM   2903 C CA  . CYS B 1 77  ? -74.481  38.259 -67.167 1.00 24.87 ? 77   CYS B CA  1 
ATOM   2904 C C   . CYS B 1 77  ? -74.939  39.693 -66.925 1.00 25.49 ? 77   CYS B C   1 
ATOM   2905 O O   . CYS B 1 77  ? -74.713  40.562 -67.759 1.00 23.96 ? 77   CYS B O   1 
ATOM   2906 C CB  . CYS B 1 77  ? -75.639  37.415 -67.702 1.00 23.81 ? 77   CYS B CB  1 
ATOM   2907 S SG  . CYS B 1 77  ? -75.110  35.814 -68.356 1.00 26.41 ? 77   CYS B SG  1 
ATOM   2908 N N   . LYS B 1 78  ? -75.574  39.938 -65.784 1.00 25.94 ? 78   LYS B N   1 
ATOM   2909 C CA  . LYS B 1 78  ? -76.042  41.272 -65.443 1.00 27.33 ? 78   LYS B CA  1 
ATOM   2910 C C   . LYS B 1 78  ? -74.911  42.292 -65.324 1.00 27.39 ? 78   LYS B C   1 
ATOM   2911 O O   . LYS B 1 78  ? -75.020  43.403 -65.836 1.00 26.41 ? 78   LYS B O   1 
ATOM   2912 C CB  . LYS B 1 78  ? -76.837  41.247 -64.129 1.00 30.64 ? 78   LYS B CB  1 
ATOM   2913 C CG  . LYS B 1 78  ? -78.351  41.122 -64.300 1.00 35.27 ? 78   LYS B CG  1 
ATOM   2914 C CD  . LYS B 1 78  ? -78.888  42.241 -65.190 1.00 37.97 ? 78   LYS B CD  1 
ATOM   2915 C CE  . LYS B 1 78  ? -80.380  42.453 -65.012 1.00 39.42 ? 78   LYS B CE  1 
ATOM   2916 N NZ  . LYS B 1 78  ? -80.896  43.457 -65.979 1.00 42.67 ? 78   LYS B NZ  1 
ATOM   2917 N N   . ILE B 1 79  ? -73.825  41.937 -64.650 1.00 28.00 ? 79   ILE B N   1 
ATOM   2918 C CA  . ILE B 1 79  ? -72.749  42.906 -64.510 1.00 27.54 ? 79   ILE B CA  1 
ATOM   2919 C C   . ILE B 1 79  ? -71.885  42.975 -65.765 1.00 27.04 ? 79   ILE B C   1 
ATOM   2920 O O   . ILE B 1 79  ? -70.993  43.815 -65.863 1.00 26.02 ? 79   ILE B O   1 
ATOM   2921 C CB  . ILE B 1 79  ? -71.884  42.643 -63.254 1.00 28.36 ? 79   ILE B CB  1 
ATOM   2922 C CG1 . ILE B 1 79  ? -71.164  41.304 -63.363 1.00 28.56 ? 79   ILE B CG1 1 
ATOM   2923 C CG2 . ILE B 1 79  ? -72.770  42.684 -61.993 1.00 26.75 ? 79   ILE B CG2 1 
ATOM   2924 C CD1 . ILE B 1 79  ? -70.346  40.994 -62.125 1.00 26.61 ? 79   ILE B CD1 1 
ATOM   2925 N N   . ALA B 1 80  ? -72.176  42.094 -66.720 1.00 25.96 ? 80   ALA B N   1 
ATOM   2926 C CA  . ALA B 1 80  ? -71.492  42.079 -68.012 1.00 26.68 ? 80   ALA B CA  1 
ATOM   2927 C C   . ALA B 1 80  ? -72.371  42.860 -69.006 1.00 27.45 ? 80   ALA B C   1 
ATOM   2928 O O   . ALA B 1 80  ? -72.182  42.784 -70.222 1.00 29.63 ? 80   ALA B O   1 
ATOM   2929 C CB  . ALA B 1 80  ? -71.286  40.655 -68.498 1.00 23.27 ? 80   ALA B CB  1 
ATOM   2930 N N   . SER B 1 81  ? -73.343  43.592 -68.468 1.00 26.15 ? 81   SER B N   1 
ATOM   2931 C CA  . SER B 1 81  ? -74.247  44.440 -69.251 1.00 27.43 ? 81   SER B CA  1 
ATOM   2932 C C   . SER B 1 81  ? -75.291  43.791 -70.155 1.00 27.69 ? 81   SER B C   1 
ATOM   2933 O O   . SER B 1 81  ? -75.693  44.377 -71.167 1.00 28.05 ? 81   SER B O   1 
ATOM   2934 C CB  . SER B 1 81  ? -73.442  45.454 -70.077 1.00 26.91 ? 81   SER B CB  1 
ATOM   2935 O OG  . SER B 1 81  ? -72.871  46.447 -69.242 1.00 24.07 ? 81   SER B OG  1 
ATOM   2936 N N   . ALA B 1 82  ? -75.738  42.589 -69.818 1.00 28.46 ? 82   ALA B N   1 
ATOM   2937 C CA  . ALA B 1 82  ? -76.785  41.978 -70.625 1.00 27.74 ? 82   ALA B CA  1 
ATOM   2938 C C   . ALA B 1 82  ? -77.950  42.983 -70.607 1.00 28.82 ? 82   ALA B C   1 
ATOM   2939 O O   . ALA B 1 82  ? -78.168  43.686 -69.614 1.00 25.65 ? 82   ALA B O   1 
ATOM   2940 C CB  . ALA B 1 82  ? -77.220  40.659 -70.019 1.00 26.22 ? 82   ALA B CB  1 
ATOM   2941 N N   . SER B 1 83  ? -78.683  43.073 -71.708 1.00 28.36 ? 83   SER B N   1 
ATOM   2942 C CA  . SER B 1 83  ? -79.801  43.995 -71.772 1.00 29.59 ? 83   SER B CA  1 
ATOM   2943 C C   . SER B 1 83  ? -80.959  43.519 -70.891 1.00 29.42 ? 83   SER B C   1 
ATOM   2944 O O   . SER B 1 83  ? -81.652  44.332 -70.276 1.00 29.18 ? 83   SER B O   1 
ATOM   2945 C CB  . SER B 1 83  ? -80.267  44.148 -73.221 1.00 32.16 ? 83   SER B CB  1 
ATOM   2946 O OG  . SER B 1 83  ? -81.368  45.027 -73.289 1.00 36.47 ? 83   SER B OG  1 
ATOM   2947 N N   . ARG B 1 84  ? -81.170  42.204 -70.844 1.00 27.83 ? 84   ARG B N   1 
ATOM   2948 C CA  . ARG B 1 84  ? -82.227  41.612 -70.026 1.00 27.41 ? 84   ARG B CA  1 
ATOM   2949 C C   . ARG B 1 84  ? -81.794  40.183 -69.714 1.00 26.19 ? 84   ARG B C   1 
ATOM   2950 O O   . ARG B 1 84  ? -81.092  39.570 -70.509 1.00 25.57 ? 84   ARG B O   1 
ATOM   2951 C CB  . ARG B 1 84  ? -83.569  41.630 -70.781 1.00 29.18 ? 84   ARG B CB  1 
ATOM   2952 C CG  . ARG B 1 84  ? -84.760  41.082 -69.981 1.00 35.59 ? 84   ARG B CG  1 
ATOM   2953 C CD  . ARG B 1 84  ? -86.128  41.286 -70.677 1.00 36.62 ? 84   ARG B CD  1 
ATOM   2954 N NE  . ARG B 1 84  ? -86.160  40.741 -72.036 1.00 41.61 ? 84   ARG B NE  1 
ATOM   2955 C CZ  . ARG B 1 84  ? -87.254  40.638 -72.785 1.00 42.24 ? 84   ARG B CZ  1 
ATOM   2956 N NH1 . ARG B 1 84  ? -88.429  41.037 -72.315 1.00 43.42 ? 84   ARG B NH1 1 
ATOM   2957 N NH2 . ARG B 1 84  ? -87.171  40.147 -74.013 1.00 42.58 ? 84   ARG B NH2 1 
ATOM   2958 N N   . VAL B 1 85  ? -82.157  39.671 -68.541 1.00 24.72 ? 85   VAL B N   1 
ATOM   2959 C CA  . VAL B 1 85  ? -81.802  38.295 -68.168 1.00 25.33 ? 85   VAL B CA  1 
ATOM   2960 C C   . VAL B 1 85  ? -83.057  37.600 -67.665 1.00 23.61 ? 85   VAL B C   1 
ATOM   2961 O O   . VAL B 1 85  ? -83.672  38.056 -66.718 1.00 23.65 ? 85   VAL B O   1 
ATOM   2962 C CB  . VAL B 1 85  ? -80.737  38.222 -67.027 1.00 24.49 ? 85   VAL B CB  1 
ATOM   2963 C CG1 . VAL B 1 85  ? -80.447  36.751 -66.687 1.00 23.58 ? 85   VAL B CG1 1 
ATOM   2964 C CG2 . VAL B 1 85  ? -79.453  38.913 -67.442 1.00 23.83 ? 85   VAL B CG2 1 
ATOM   2965 N N   . THR B 1 86  ? -83.431  36.502 -68.309 1.00 23.49 ? 86   THR B N   1 
ATOM   2966 C CA  . THR B 1 86  ? -84.612  35.754 -67.918 1.00 22.25 ? 86   THR B CA  1 
ATOM   2967 C C   . THR B 1 86  ? -84.182  34.409 -67.367 1.00 24.32 ? 86   THR B C   1 
ATOM   2968 O O   . THR B 1 86  ? -83.312  33.742 -67.938 1.00 23.56 ? 86   THR B O   1 
ATOM   2969 C CB  . THR B 1 86  ? -85.532  35.508 -69.132 1.00 21.74 ? 86   THR B CB  1 
ATOM   2970 O OG1 . THR B 1 86  ? -86.053  36.760 -69.589 1.00 23.23 ? 86   THR B OG1 1 
ATOM   2971 C CG2 . THR B 1 86  ? -86.673  34.571 -68.772 1.00 18.27 ? 86   THR B CG2 1 
ATOM   2972 N N   . ALA B 1 87  ? -84.788  34.011 -66.255 1.00 24.96 ? 87   ALA B N   1 
ATOM   2973 C CA  . ALA B 1 87  ? -84.473  32.728 -65.663 1.00 24.87 ? 87   ALA B CA  1 
ATOM   2974 C C   . ALA B 1 87  ? -85.527  31.719 -66.091 1.00 24.31 ? 87   ALA B C   1 
ATOM   2975 O O   . ALA B 1 87  ? -86.700  31.862 -65.771 1.00 26.46 ? 87   ALA B O   1 
ATOM   2976 C CB  . ALA B 1 87  ? -84.428  32.839 -64.134 1.00 24.98 ? 87   ALA B CB  1 
ATOM   2977 N N   . VAL B 1 88  ? -85.102  30.716 -66.848 1.00 24.61 ? 88   VAL B N   1 
ATOM   2978 C CA  . VAL B 1 88  ? -85.995  29.652 -67.321 1.00 23.68 ? 88   VAL B CA  1 
ATOM   2979 C C   . VAL B 1 88  ? -85.808  28.520 -66.300 1.00 23.99 ? 88   VAL B C   1 
ATOM   2980 O O   . VAL B 1 88  ? -84.786  27.826 -66.289 1.00 20.89 ? 88   VAL B O   1 
ATOM   2981 C CB  . VAL B 1 88  ? -85.585  29.194 -68.745 1.00 23.21 ? 88   VAL B CB  1 
ATOM   2982 C CG1 . VAL B 1 88  ? -86.575  28.180 -69.293 1.00 19.58 ? 88   VAL B CG1 1 
ATOM   2983 C CG2 . VAL B 1 88  ? -85.497  30.428 -69.657 1.00 22.51 ? 88   VAL B CG2 1 
ATOM   2984 N N   . ILE B 1 89  ? -86.797  28.359 -65.427 1.00 22.58 ? 89   ILE B N   1 
ATOM   2985 C CA  . ILE B 1 89  ? -86.732  27.373 -64.374 1.00 22.77 ? 89   ILE B CA  1 
ATOM   2986 C C   . ILE B 1 89  ? -87.922  26.432 -64.468 1.00 25.58 ? 89   ILE B C   1 
ATOM   2987 O O   . ILE B 1 89  ? -88.956  26.643 -63.819 1.00 25.82 ? 89   ILE B O   1 
ATOM   2988 C CB  . ILE B 1 89  ? -86.755  28.049 -62.991 1.00 23.98 ? 89   ILE B CB  1 
ATOM   2989 C CG1 . ILE B 1 89  ? -85.851  29.286 -63.002 1.00 23.51 ? 89   ILE B CG1 1 
ATOM   2990 C CG2 . ILE B 1 89  ? -86.272  27.086 -61.950 1.00 25.01 ? 89   ILE B CG2 1 
ATOM   2991 C CD1 . ILE B 1 89  ? -85.889  30.073 -61.694 1.00 23.67 ? 89   ILE B CD1 1 
ATOM   2992 N N   . PRO B 1 90  ? -87.796  25.377 -65.286 1.00 24.99 ? 90   PRO B N   1 
ATOM   2993 C CA  . PRO B 1 90  ? -88.858  24.393 -65.500 1.00 25.53 ? 90   PRO B CA  1 
ATOM   2994 C C   . PRO B 1 90  ? -89.495  23.975 -64.184 1.00 26.30 ? 90   PRO B C   1 
ATOM   2995 O O   . PRO B 1 90  ? -90.699  24.103 -64.013 1.00 28.66 ? 90   PRO B O   1 
ATOM   2996 C CB  . PRO B 1 90  ? -88.133  23.261 -66.225 1.00 25.75 ? 90   PRO B CB  1 
ATOM   2997 C CG  . PRO B 1 90  ? -87.075  24.010 -66.996 1.00 25.31 ? 90   PRO B CG  1 
ATOM   2998 C CD  . PRO B 1 90  ? -86.550  24.961 -65.962 1.00 24.65 ? 90   PRO B CD  1 
ATOM   2999 N N   . CYS B 1 91  ? -88.677  23.506 -63.256 1.00 24.37 ? 91   CYS B N   1 
ATOM   3000 C CA  . CYS B 1 91  ? -89.157  23.089 -61.936 1.00 25.97 ? 91   CYS B CA  1 
ATOM   3001 C C   . CYS B 1 91  ? -88.636  24.072 -60.880 1.00 24.91 ? 91   CYS B C   1 
ATOM   3002 O O   . CYS B 1 91  ? -87.461  24.053 -60.537 1.00 23.54 ? 91   CYS B O   1 
ATOM   3003 C CB  . CYS B 1 91  ? -88.666  21.672 -61.616 1.00 23.19 ? 91   CYS B CB  1 
ATOM   3004 S SG  . CYS B 1 91  ? -89.494  20.942 -60.180 1.00 28.09 ? 91   CYS B SG  1 
ATOM   3005 N N   . PHE B 1 92  ? -89.518  24.922 -60.366 1.00 25.11 ? 92   PHE B N   1 
ATOM   3006 C CA  . PHE B 1 92  ? -89.127  25.930 -59.393 1.00 26.14 ? 92   PHE B CA  1 
ATOM   3007 C C   . PHE B 1 92  ? -88.667  25.354 -58.048 1.00 26.58 ? 92   PHE B C   1 
ATOM   3008 O O   . PHE B 1 92  ? -89.425  24.668 -57.357 1.00 28.91 ? 92   PHE B O   1 
ATOM   3009 C CB  . PHE B 1 92  ? -90.287  26.893 -59.151 1.00 25.13 ? 92   PHE B CB  1 
ATOM   3010 C CG  . PHE B 1 92  ? -89.865  28.183 -58.516 1.00 25.00 ? 92   PHE B CG  1 
ATOM   3011 C CD1 . PHE B 1 92  ? -89.386  29.229 -59.299 1.00 23.26 ? 92   PHE B CD1 1 
ATOM   3012 C CD2 . PHE B 1 92  ? -89.930  28.347 -57.136 1.00 23.52 ? 92   PHE B CD2 1 
ATOM   3013 C CE1 . PHE B 1 92  ? -88.976  30.417 -58.715 1.00 25.21 ? 92   PHE B CE1 1 
ATOM   3014 C CE2 . PHE B 1 92  ? -89.519  29.537 -56.538 1.00 23.74 ? 92   PHE B CE2 1 
ATOM   3015 C CZ  . PHE B 1 92  ? -89.045  30.573 -57.327 1.00 23.57 ? 92   PHE B CZ  1 
ATOM   3016 N N   . PRO B 1 93  ? -87.424  25.658 -57.645 1.00 28.80 ? 93   PRO B N   1 
ATOM   3017 C CA  . PRO B 1 93  ? -86.832  25.183 -56.384 1.00 27.77 ? 93   PRO B CA  1 
ATOM   3018 C C   . PRO B 1 93  ? -87.616  25.648 -55.162 1.00 26.34 ? 93   PRO B C   1 
ATOM   3019 O O   . PRO B 1 93  ? -88.112  26.772 -55.135 1.00 25.27 ? 93   PRO B O   1 
ATOM   3020 C CB  . PRO B 1 93  ? -85.432  25.800 -56.395 1.00 28.54 ? 93   PRO B CB  1 
ATOM   3021 C CG  . PRO B 1 93  ? -85.164  26.106 -57.821 1.00 31.22 ? 93   PRO B CG  1 
ATOM   3022 C CD  . PRO B 1 93  ? -86.496  26.569 -58.337 1.00 29.43 ? 93   PRO B CD  1 
ATOM   3023 N N   . TYR B 1 94  ? -87.702  24.779 -54.157 1.00 25.89 ? 94   TYR B N   1 
ATOM   3024 C CA  . TYR B 1 94  ? -88.391  25.060 -52.898 1.00 26.13 ? 94   TYR B CA  1 
ATOM   3025 C C   . TYR B 1 94  ? -89.853  25.462 -53.005 1.00 26.82 ? 94   TYR B C   1 
ATOM   3026 O O   . TYR B 1 94  ? -90.440  25.945 -52.029 1.00 26.30 ? 94   TYR B O   1 
ATOM   3027 C CB  . TYR B 1 94  ? -87.623  26.131 -52.110 1.00 24.63 ? 94   TYR B CB  1 
ATOM   3028 C CG  . TYR B 1 94  ? -86.280  25.644 -51.631 1.00 24.18 ? 94   TYR B CG  1 
ATOM   3029 C CD1 . TYR B 1 94  ? -85.147  25.716 -52.454 1.00 23.98 ? 94   TYR B CD1 1 
ATOM   3030 C CD2 . TYR B 1 94  ? -86.144  25.058 -50.370 1.00 23.18 ? 94   TYR B CD2 1 
ATOM   3031 C CE1 . TYR B 1 94  ? -83.918  25.216 -52.029 1.00 19.55 ? 94   TYR B CE1 1 
ATOM   3032 C CE2 . TYR B 1 94  ? -84.921  24.556 -49.940 1.00 21.84 ? 94   TYR B CE2 1 
ATOM   3033 C CZ  . TYR B 1 94  ? -83.813  24.639 -50.771 1.00 21.58 ? 94   TYR B CZ  1 
ATOM   3034 O OH  . TYR B 1 94  ? -82.602  24.162 -50.324 1.00 19.78 ? 94   TYR B OH  1 
ATOM   3035 N N   . ALA B 1 95  ? -90.449  25.226 -54.174 1.00 28.20 ? 95   ALA B N   1 
ATOM   3036 C CA  . ALA B 1 95  ? -91.848  25.576 -54.418 1.00 28.97 ? 95   ALA B CA  1 
ATOM   3037 C C   . ALA B 1 95  ? -92.810  25.014 -53.375 1.00 29.07 ? 95   ALA B C   1 
ATOM   3038 O O   . ALA B 1 95  ? -93.817  25.637 -53.058 1.00 30.51 ? 95   ALA B O   1 
ATOM   3039 C CB  . ALA B 1 95  ? -92.263  25.117 -55.802 1.00 28.94 ? 95   ALA B CB  1 
ATOM   3040 N N   . ARG B 1 96  ? -92.503  23.843 -52.837 1.00 29.27 ? 96   ARG B N   1 
ATOM   3041 C CA  . ARG B 1 96  ? -93.369  23.246 -51.829 1.00 30.57 ? 96   ARG B CA  1 
ATOM   3042 C C   . ARG B 1 96  ? -93.269  23.991 -50.500 1.00 30.06 ? 96   ARG B C   1 
ATOM   3043 O O   . ARG B 1 96  ? -94.107  23.821 -49.625 1.00 30.73 ? 96   ARG B O   1 
ATOM   3044 C CB  . ARG B 1 96  ? -93.008  21.776 -51.624 1.00 33.87 ? 96   ARG B CB  1 
ATOM   3045 C CG  . ARG B 1 96  ? -93.448  20.854 -52.756 1.00 35.55 ? 96   ARG B CG  1 
ATOM   3046 C CD  . ARG B 1 96  ? -92.805  19.493 -52.609 1.00 40.68 ? 96   ARG B CD  1 
ATOM   3047 N NE  . ARG B 1 96  ? -91.365  19.545 -52.877 1.00 43.87 ? 96   ARG B NE  1 
ATOM   3048 C CZ  . ARG B 1 96  ? -90.496  18.624 -52.475 1.00 44.93 ? 96   ARG B CZ  1 
ATOM   3049 N NH1 . ARG B 1 96  ? -90.912  17.574 -51.778 1.00 45.38 ? 96   ARG B NH1 1 
ATOM   3050 N NH2 . ARG B 1 96  ? -89.210  18.748 -52.777 1.00 45.79 ? 96   ARG B NH2 1 
ATOM   3051 N N   . GLN B 1 97  ? -92.243  24.817 -50.348 1.00 28.90 ? 97   GLN B N   1 
ATOM   3052 C CA  . GLN B 1 97  ? -92.074  25.578 -49.114 1.00 29.35 ? 97   GLN B CA  1 
ATOM   3053 C C   . GLN B 1 97  ? -92.583  27.007 -49.331 1.00 28.05 ? 97   GLN B C   1 
ATOM   3054 O O   . GLN B 1 97  ? -91.823  27.973 -49.297 1.00 26.33 ? 97   GLN B O   1 
ATOM   3055 C CB  . GLN B 1 97  ? -90.597  25.545 -48.684 1.00 29.33 ? 97   GLN B CB  1 
ATOM   3056 C CG  . GLN B 1 97  ? -90.172  24.153 -48.187 1.00 33.90 ? 97   GLN B CG  1 
ATOM   3057 C CD  . GLN B 1 97  ? -88.727  24.074 -47.709 1.00 37.94 ? 97   GLN B CD  1 
ATOM   3058 O OE1 . GLN B 1 97  ? -88.208  25.000 -47.074 1.00 41.36 ? 97   GLN B OE1 1 
ATOM   3059 N NE2 . GLN B 1 97  ? -88.077  22.955 -47.996 1.00 37.56 ? 97   GLN B NE2 1 
ATOM   3060 N N   . ASP B 1 98  ? -93.891  27.120 -49.542 1.00 28.74 ? 98   ASP B N   1 
ATOM   3061 C CA  . ASP B 1 98  ? -94.529  28.405 -49.813 1.00 31.94 ? 98   ASP B CA  1 
ATOM   3062 C C   . ASP B 1 98  ? -95.471  28.965 -48.739 1.00 31.04 ? 98   ASP B C   1 
ATOM   3063 O O   . ASP B 1 98  ? -96.202  29.915 -49.003 1.00 31.69 ? 98   ASP B O   1 
ATOM   3064 C CB  . ASP B 1 98  ? -95.268  28.323 -51.153 1.00 31.10 ? 98   ASP B CB  1 
ATOM   3065 C CG  . ASP B 1 98  ? -96.342  27.247 -51.165 1.00 33.79 ? 98   ASP B CG  1 
ATOM   3066 O OD1 . ASP B 1 98  ? -96.281  26.321 -50.326 1.00 31.85 ? 98   ASP B OD1 1 
ATOM   3067 O OD2 . ASP B 1 98  ? -97.241  27.324 -52.030 1.00 34.76 ? 98   ASP B OD2 1 
ATOM   3068 N N   . LYS B 1 99  ? -95.461  28.381 -47.543 1.00 31.77 ? 99   LYS B N   1 
ATOM   3069 C CA  . LYS B 1 99  ? -96.294  28.858 -46.429 1.00 32.82 ? 99   LYS B CA  1 
ATOM   3070 C C   . LYS B 1 99  ? -95.725  28.378 -45.093 1.00 33.78 ? 99   LYS B C   1 
ATOM   3071 O O   . LYS B 1 99  ? -94.957  27.419 -45.052 1.00 32.45 ? 99   LYS B O   1 
ATOM   3072 C CB  . LYS B 1 99  ? -97.748  28.394 -46.583 1.00 33.96 ? 99   LYS B CB  1 
ATOM   3073 C CG  . LYS B 1 99  ? -97.956  26.887 -46.627 1.00 37.44 ? 99   LYS B CG  1 
ATOM   3074 C CD  . LYS B 1 99  ? -99.313  26.570 -47.246 1.00 42.18 ? 99   LYS B CD  1 
ATOM   3075 C CE  . LYS B 1 99  ? -99.473  25.096 -47.596 1.00 46.14 ? 99   LYS B CE  1 
ATOM   3076 N NZ  . LYS B 1 99  ? -100.685 24.859 -48.459 1.00 49.36 ? 99   LYS B NZ  1 
ATOM   3077 N N   . LYS B 1 100 ? -96.085  29.060 -44.008 1.00 35.22 ? 100  LYS B N   1 
ATOM   3078 C CA  . LYS B 1 100 ? -95.589  28.697 -42.684 1.00 37.49 ? 100  LYS B CA  1 
ATOM   3079 C C   . LYS B 1 100 ? -96.303  27.450 -42.195 1.00 38.20 ? 100  LYS B C   1 
ATOM   3080 O O   . LYS B 1 100 ? -95.764  26.683 -41.397 1.00 36.92 ? 100  LYS B O   1 
ATOM   3081 C CB  . LYS B 1 100 ? -95.815  29.832 -41.679 1.00 36.75 ? 100  LYS B CB  1 
ATOM   3082 C CG  . LYS B 1 100 ? -94.969  31.081 -41.899 1.00 37.23 ? 100  LYS B CG  1 
ATOM   3083 C CD  . LYS B 1 100 ? -95.204  32.079 -40.758 1.00 33.97 ? 100  LYS B CD  1 
ATOM   3084 C CE  . LYS B 1 100 ? -94.506  33.405 -41.007 1.00 36.09 ? 100  LYS B CE  1 
ATOM   3085 N NZ  . LYS B 1 100 ? -94.770  34.412 -39.924 1.00 34.50 ? 100  LYS B NZ  1 
ATOM   3086 N N   . ASP B 1 101 ? -97.528  27.264 -42.673 1.00 40.54 ? 101  ASP B N   1 
ATOM   3087 C CA  . ASP B 1 101 ? -98.329  26.103 -42.304 1.00 43.23 ? 101  ASP B CA  1 
ATOM   3088 C C   . ASP B 1 101 ? -98.434  25.947 -40.779 1.00 42.23 ? 101  ASP B C   1 
ATOM   3089 O O   . ASP B 1 101 ? -98.197  24.866 -40.244 1.00 41.54 ? 101  ASP B O   1 
ATOM   3090 C CB  . ASP B 1 101 ? -97.703  24.841 -42.917 1.00 45.18 ? 101  ASP B CB  1 
ATOM   3091 C CG  . ASP B 1 101 ? -98.702  23.714 -43.094 1.00 47.52 ? 101  ASP B CG  1 
ATOM   3092 O OD1 . ASP B 1 101 ? -98.257  22.552 -43.184 1.00 49.58 ? 101  ASP B OD1 1 
ATOM   3093 O OD2 . ASP B 1 101 ? -99.923  23.984 -43.157 1.00 49.19 ? 101  ASP B OD2 1 
ATOM   3094 N N   . LYS B 1 102 ? -98.783  27.034 -40.094 1.00 42.61 ? 102  LYS B N   1 
ATOM   3095 C CA  . LYS B 1 102 ? -98.939  27.044 -38.634 1.00 42.82 ? 102  LYS B CA  1 
ATOM   3096 C C   . LYS B 1 102 ? -97.670  26.746 -37.834 1.00 43.12 ? 102  LYS B C   1 
ATOM   3097 O O   . LYS B 1 102 ? -97.751  26.442 -36.643 1.00 42.49 ? 102  LYS B O   1 
ATOM   3098 C CB  . LYS B 1 102 ? -100.016 26.048 -38.188 1.00 43.03 ? 102  LYS B CB  1 
ATOM   3099 C CG  . LYS B 1 102 ? -101.442 26.366 -38.605 1.00 46.14 ? 102  LYS B CG  1 
ATOM   3100 C CD  . LYS B 1 102 ? -102.420 25.620 -37.688 1.00 48.54 ? 102  LYS B CD  1 
ATOM   3101 C CE  . LYS B 1 102 ? -103.833 25.515 -38.271 1.00 49.64 ? 102  LYS B CE  1 
ATOM   3102 N NZ  . LYS B 1 102 ? -104.472 26.828 -38.541 1.00 48.99 ? 102  LYS B NZ  1 
ATOM   3103 N N   . SER B 1 103 ? -96.507  26.827 -38.473 1.00 42.38 ? 103  SER B N   1 
ATOM   3104 C CA  . SER B 1 103 ? -95.241  26.559 -37.790 1.00 40.70 ? 103  SER B CA  1 
ATOM   3105 C C   . SER B 1 103 ? -94.292  27.741 -37.927 1.00 39.09 ? 103  SER B C   1 
ATOM   3106 O O   . SER B 1 103 ? -94.538  28.637 -38.731 1.00 38.95 ? 103  SER B O   1 
ATOM   3107 C CB  . SER B 1 103 ? -94.572  25.326 -38.396 1.00 41.29 ? 103  SER B CB  1 
ATOM   3108 O OG  . SER B 1 103 ? -95.470  24.238 -38.464 1.00 42.92 ? 103  SER B OG  1 
ATOM   3109 N N   . ARG B 1 104 ? -93.220  27.745 -37.133 1.00 38.65 ? 104  ARG B N   1 
ATOM   3110 C CA  . ARG B 1 104 ? -92.204  28.796 -37.201 1.00 37.54 ? 104  ARG B CA  1 
ATOM   3111 C C   . ARG B 1 104 ? -91.250  28.364 -38.313 1.00 38.51 ? 104  ARG B C   1 
ATOM   3112 O O   . ARG B 1 104 ? -90.058  28.118 -38.094 1.00 39.09 ? 104  ARG B O   1 
ATOM   3113 C CB  . ARG B 1 104 ? -91.457  28.934 -35.864 1.00 37.19 ? 104  ARG B CB  1 
ATOM   3114 C CG  . ARG B 1 104 ? -92.191  29.805 -34.838 1.00 39.96 ? 104  ARG B CG  1 
ATOM   3115 C CD  . ARG B 1 104 ? -91.398  30.017 -33.549 1.00 37.41 ? 104  ARG B CD  1 
ATOM   3116 N NE  . ARG B 1 104 ? -91.429  28.845 -32.677 1.00 40.24 ? 104  ARG B NE  1 
ATOM   3117 C CZ  . ARG B 1 104 ? -92.330  28.627 -31.723 1.00 39.75 ? 104  ARG B CZ  1 
ATOM   3118 N NH1 . ARG B 1 104 ? -93.293  29.500 -31.493 1.00 39.94 ? 104  ARG B NH1 1 
ATOM   3119 N NH2 . ARG B 1 104 ? -92.268  27.523 -30.991 1.00 44.67 ? 104  ARG B NH2 1 
ATOM   3120 N N   . ALA B 1 105 ? -91.807  28.264 -39.516 1.00 36.78 ? 105  ALA B N   1 
ATOM   3121 C CA  . ALA B 1 105 ? -91.063  27.830 -40.684 1.00 34.78 ? 105  ALA B CA  1 
ATOM   3122 C C   . ALA B 1 105 ? -90.702  28.973 -41.617 1.00 33.08 ? 105  ALA B C   1 
ATOM   3123 O O   . ALA B 1 105 ? -91.243  30.073 -41.525 1.00 32.53 ? 105  ALA B O   1 
ATOM   3124 C CB  . ALA B 1 105 ? -91.877  26.786 -41.447 1.00 34.82 ? 105  ALA B CB  1 
ATOM   3125 N N   . PRO B 1 106 ? -89.755  28.728 -42.523 1.00 31.13 ? 106  PRO B N   1 
ATOM   3126 C CA  . PRO B 1 106 ? -89.373  29.781 -43.457 1.00 30.01 ? 106  PRO B CA  1 
ATOM   3127 C C   . PRO B 1 106 ? -90.258  29.631 -44.690 1.00 28.83 ? 106  PRO B C   1 
ATOM   3128 O O   . PRO B 1 106 ? -90.790  28.546 -44.947 1.00 28.35 ? 106  PRO B O   1 
ATOM   3129 C CB  . PRO B 1 106 ? -87.924  29.439 -43.764 1.00 31.70 ? 106  PRO B CB  1 
ATOM   3130 C CG  . PRO B 1 106 ? -87.975  27.939 -43.824 1.00 30.87 ? 106  PRO B CG  1 
ATOM   3131 C CD  . PRO B 1 106 ? -88.843  27.573 -42.629 1.00 30.49 ? 106  PRO B CD  1 
ATOM   3132 N N   . ILE B 1 107 ? -90.462  30.712 -45.429 1.00 26.97 ? 107  ILE B N   1 
ATOM   3133 C CA  . ILE B 1 107 ? -91.232  30.595 -46.665 1.00 26.86 ? 107  ILE B CA  1 
ATOM   3134 C C   . ILE B 1 107 ? -90.130  30.619 -47.732 1.00 25.96 ? 107  ILE B C   1 
ATOM   3135 O O   . ILE B 1 107 ? -89.965  31.591 -48.458 1.00 27.08 ? 107  ILE B O   1 
ATOM   3136 C CB  . ILE B 1 107 ? -92.191  31.773 -46.860 1.00 25.80 ? 107  ILE B CB  1 
ATOM   3137 C CG1 . ILE B 1 107 ? -93.247  31.773 -45.752 1.00 24.39 ? 107  ILE B CG1 1 
ATOM   3138 C CG2 . ILE B 1 107 ? -92.871  31.664 -48.226 1.00 25.53 ? 107  ILE B CG2 1 
ATOM   3139 C CD1 . ILE B 1 107 ? -94.236  32.919 -45.857 1.00 22.83 ? 107  ILE B CD1 1 
ATOM   3140 N N   . SER B 1 108 ? -89.362  29.533 -47.776 1.00 24.83 ? 108  SER B N   1 
ATOM   3141 C CA  . SER B 1 108 ? -88.228  29.380 -48.682 1.00 24.00 ? 108  SER B CA  1 
ATOM   3142 C C   . SER B 1 108 ? -88.476  29.722 -50.142 1.00 23.72 ? 108  SER B C   1 
ATOM   3143 O O   . SER B 1 108 ? -87.556  30.150 -50.831 1.00 25.44 ? 108  SER B O   1 
ATOM   3144 C CB  . SER B 1 108 ? -87.693  27.958 -48.594 1.00 23.95 ? 108  SER B CB  1 
ATOM   3145 O OG  . SER B 1 108 ? -87.395  27.613 -47.266 1.00 24.48 ? 108  SER B OG  1 
ATOM   3146 N N   . ALA B 1 109 ? -89.696  29.513 -50.624 1.00 22.71 ? 109  ALA B N   1 
ATOM   3147 C CA  . ALA B 1 109 ? -90.011  29.835 -52.013 1.00 22.39 ? 109  ALA B CA  1 
ATOM   3148 C C   . ALA B 1 109 ? -89.945  31.349 -52.192 1.00 23.74 ? 109  ALA B C   1 
ATOM   3149 O O   . ALA B 1 109 ? -89.594  31.835 -53.271 1.00 24.50 ? 109  ALA B O   1 
ATOM   3150 C CB  . ALA B 1 109 ? -91.389  29.315 -52.386 1.00 20.51 ? 109  ALA B CB  1 
ATOM   3151 N N   . LYS B 1 110 ? -90.282  32.095 -51.138 1.00 23.02 ? 110  LYS B N   1 
ATOM   3152 C CA  . LYS B 1 110 ? -90.216  33.559 -51.204 1.00 21.45 ? 110  LYS B CA  1 
ATOM   3153 C C   . LYS B 1 110 ? -88.757  34.005 -51.141 1.00 22.80 ? 110  LYS B C   1 
ATOM   3154 O O   . LYS B 1 110 ? -88.362  34.961 -51.820 1.00 23.51 ? 110  LYS B O   1 
ATOM   3155 C CB  . LYS B 1 110 ? -90.996  34.212 -50.057 1.00 20.58 ? 110  LYS B CB  1 
ATOM   3156 C CG  . LYS B 1 110 ? -90.870  35.745 -50.011 1.00 17.48 ? 110  LYS B CG  1 
ATOM   3157 C CD  . LYS B 1 110 ? -91.332  36.403 -51.332 1.00 20.05 ? 110  LYS B CD  1 
ATOM   3158 C CE  . LYS B 1 110 ? -91.111  37.917 -51.336 1.00 17.38 ? 110  LYS B CE  1 
ATOM   3159 N NZ  . LYS B 1 110 ? -91.852  38.549 -50.221 1.00 26.15 ? 110  LYS B NZ  1 
ATOM   3160 N N   . LEU B 1 111 ? -87.960  33.319 -50.319 1.00 19.85 ? 111  LEU B N   1 
ATOM   3161 C CA  . LEU B 1 111 ? -86.546  33.643 -50.211 1.00 19.37 ? 111  LEU B CA  1 
ATOM   3162 C C   . LEU B 1 111 ? -85.883  33.429 -51.585 1.00 19.16 ? 111  LEU B C   1 
ATOM   3163 O O   . LEU B 1 111 ? -85.116  34.260 -52.047 1.00 20.69 ? 111  LEU B O   1 
ATOM   3164 C CB  . LEU B 1 111 ? -85.880  32.753 -49.150 1.00 19.39 ? 111  LEU B CB  1 
ATOM   3165 C CG  . LEU B 1 111 ? -84.342  32.709 -49.143 1.00 22.32 ? 111  LEU B CG  1 
ATOM   3166 C CD1 . LEU B 1 111 ? -83.777  34.085 -48.784 1.00 16.51 ? 111  LEU B CD1 1 
ATOM   3167 C CD2 . LEU B 1 111 ? -83.855  31.622 -48.159 1.00 20.12 ? 111  LEU B CD2 1 
ATOM   3168 N N   . VAL B 1 112 ? -86.186  32.303 -52.221 1.00 18.52 ? 112  VAL B N   1 
ATOM   3169 C CA  . VAL B 1 112 ? -85.649  31.981 -53.532 1.00 18.98 ? 112  VAL B CA  1 
ATOM   3170 C C   . VAL B 1 112 ? -86.036  33.059 -54.554 1.00 19.30 ? 112  VAL B C   1 
ATOM   3171 O O   . VAL B 1 112 ? -85.201  33.501 -55.338 1.00 20.12 ? 112  VAL B O   1 
ATOM   3172 C CB  . VAL B 1 112 ? -86.147  30.572 -53.978 1.00 18.66 ? 112  VAL B CB  1 
ATOM   3173 C CG1 . VAL B 1 112 ? -85.956  30.371 -55.476 1.00 18.38 ? 112  VAL B CG1 1 
ATOM   3174 C CG2 . VAL B 1 112 ? -85.368  29.507 -53.203 1.00 18.43 ? 112  VAL B CG2 1 
ATOM   3175 N N   . ALA B 1 113 ? -87.292  33.493 -54.540 1.00 19.07 ? 113  ALA B N   1 
ATOM   3176 C CA  . ALA B 1 113 ? -87.723  34.545 -55.464 1.00 19.39 ? 113  ALA B CA  1 
ATOM   3177 C C   . ALA B 1 113 ? -86.906  35.814 -55.196 1.00 21.22 ? 113  ALA B C   1 
ATOM   3178 O O   . ALA B 1 113 ? -86.469  36.479 -56.136 1.00 21.74 ? 113  ALA B O   1 
ATOM   3179 C CB  . ALA B 1 113 ? -89.200  34.828 -55.291 1.00 17.02 ? 113  ALA B CB  1 
ATOM   3180 N N   . ASN B 1 114 ? -86.677  36.141 -53.921 1.00 20.25 ? 114  ASN B N   1 
ATOM   3181 C CA  . ASN B 1 114 ? -85.895  37.335 -53.598 1.00 21.91 ? 114  ASN B CA  1 
ATOM   3182 C C   . ASN B 1 114 ? -84.442  37.164 -54.019 1.00 22.12 ? 114  ASN B C   1 
ATOM   3183 O O   . ASN B 1 114 ? -83.805  38.106 -54.478 1.00 24.37 ? 114  ASN B O   1 
ATOM   3184 C CB  . ASN B 1 114 ? -85.944  37.663 -52.101 1.00 19.64 ? 114  ASN B CB  1 
ATOM   3185 C CG  . ASN B 1 114 ? -87.257  38.306 -51.681 1.00 22.83 ? 114  ASN B CG  1 
ATOM   3186 O OD1 . ASN B 1 114 ? -87.960  38.905 -52.492 1.00 21.49 ? 114  ASN B OD1 1 
ATOM   3187 N ND2 . ASN B 1 114 ? -87.573  38.209 -50.399 1.00 21.16 ? 114  ASN B ND2 1 
ATOM   3188 N N   . MET B 1 115 ? -83.911  35.963 -53.863 1.00 20.70 ? 115  MET B N   1 
ATOM   3189 C CA  . MET B 1 115 ? -82.533  35.741 -54.257 1.00 23.92 ? 115  MET B CA  1 
ATOM   3190 C C   . MET B 1 115 ? -82.409  35.938 -55.768 1.00 22.92 ? 115  MET B C   1 
ATOM   3191 O O   . MET B 1 115 ? -81.504  36.609 -56.230 1.00 23.78 ? 115  MET B O   1 
ATOM   3192 C CB  . MET B 1 115 ? -82.090  34.338 -53.853 1.00 20.91 ? 115  MET B CB  1 
ATOM   3193 C CG  . MET B 1 115 ? -82.037  34.140 -52.355 1.00 26.57 ? 115  MET B CG  1 
ATOM   3194 S SD  . MET B 1 115 ? -81.433  32.523 -51.965 1.00 35.40 ? 115  MET B SD  1 
ATOM   3195 C CE  . MET B 1 115 ? -82.905  31.646 -51.712 1.00 35.60 ? 115  MET B CE  1 
ATOM   3196 N N   . LEU B 1 116 ? -83.327  35.358 -56.531 1.00 22.47 ? 116  LEU B N   1 
ATOM   3197 C CA  . LEU B 1 116 ? -83.300  35.495 -57.985 1.00 24.24 ? 116  LEU B CA  1 
ATOM   3198 C C   . LEU B 1 116 ? -83.458  36.956 -58.389 1.00 24.67 ? 116  LEU B C   1 
ATOM   3199 O O   . LEU B 1 116 ? -82.865  37.410 -59.366 1.00 25.82 ? 116  LEU B O   1 
ATOM   3200 C CB  . LEU B 1 116 ? -84.424  34.670 -58.616 1.00 20.66 ? 116  LEU B CB  1 
ATOM   3201 C CG  . LEU B 1 116 ? -84.244  33.156 -58.720 1.00 20.52 ? 116  LEU B CG  1 
ATOM   3202 C CD1 . LEU B 1 116 ? -85.605  32.506 -58.872 1.00 18.03 ? 116  LEU B CD1 1 
ATOM   3203 C CD2 . LEU B 1 116 ? -83.331  32.807 -59.907 1.00 13.94 ? 116  LEU B CD2 1 
ATOM   3204 N N   . SER B 1 117 ? -84.272  37.687 -57.638 1.00 26.30 ? 117  SER B N   1 
ATOM   3205 C CA  . SER B 1 117 ? -84.487  39.093 -57.929 1.00 26.51 ? 117  SER B CA  1 
ATOM   3206 C C   . SER B 1 117 ? -83.211  39.902 -57.694 1.00 26.91 ? 117  SER B C   1 
ATOM   3207 O O   . SER B 1 117 ? -82.731  40.575 -58.604 1.00 27.40 ? 117  SER B O   1 
ATOM   3208 C CB  . SER B 1 117 ? -85.634  39.640 -57.076 1.00 27.42 ? 117  SER B CB  1 
ATOM   3209 O OG  . SER B 1 117 ? -86.859  38.967 -57.364 1.00 29.18 ? 117  SER B OG  1 
ATOM   3210 N N   . VAL B 1 118 ? -82.648  39.825 -56.493 1.00 26.85 ? 118  VAL B N   1 
ATOM   3211 C CA  . VAL B 1 118 ? -81.436  40.579 -56.201 1.00 26.52 ? 118  VAL B CA  1 
ATOM   3212 C C   . VAL B 1 118 ? -80.261  40.108 -57.034 1.00 25.48 ? 118  VAL B C   1 
ATOM   3213 O O   . VAL B 1 118 ? -79.313  40.856 -57.233 1.00 26.23 ? 118  VAL B O   1 
ATOM   3214 C CB  . VAL B 1 118 ? -81.034  40.500 -54.713 1.00 28.71 ? 118  VAL B CB  1 
ATOM   3215 C CG1 . VAL B 1 118 ? -82.152  41.049 -53.858 1.00 33.30 ? 118  VAL B CG1 1 
ATOM   3216 C CG2 . VAL B 1 118 ? -80.702  39.054 -54.320 1.00 30.51 ? 118  VAL B CG2 1 
ATOM   3217 N N   . ALA B 1 119 ? -80.312  38.870 -57.517 1.00 21.67 ? 119  ALA B N   1 
ATOM   3218 C CA  . ALA B 1 119 ? -79.226  38.368 -58.348 1.00 21.24 ? 119  ALA B CA  1 
ATOM   3219 C C   . ALA B 1 119 ? -79.236  39.147 -59.656 1.00 21.37 ? 119  ALA B C   1 
ATOM   3220 O O   . ALA B 1 119 ? -78.223  39.237 -60.338 1.00 21.02 ? 119  ALA B O   1 
ATOM   3221 C CB  . ALA B 1 119 ? -79.397  36.878 -58.620 1.00 22.09 ? 119  ALA B CB  1 
ATOM   3222 N N   . GLY B 1 120 ? -80.394  39.708 -59.993 1.00 22.86 ? 120  GLY B N   1 
ATOM   3223 C CA  . GLY B 1 120 ? -80.529  40.480 -61.217 1.00 24.04 ? 120  GLY B CA  1 
ATOM   3224 C C   . GLY B 1 120 ? -81.473  39.906 -62.273 1.00 24.40 ? 120  GLY B C   1 
ATOM   3225 O O   . GLY B 1 120 ? -81.367  40.269 -63.442 1.00 25.78 ? 120  GLY B O   1 
ATOM   3226 N N   . ALA B 1 121 ? -82.400  39.030 -61.884 1.00 25.27 ? 121  ALA B N   1 
ATOM   3227 C CA  . ALA B 1 121 ? -83.348  38.448 -62.844 1.00 25.04 ? 121  ALA B CA  1 
ATOM   3228 C C   . ALA B 1 121 ? -84.410  39.482 -63.194 1.00 23.30 ? 121  ALA B C   1 
ATOM   3229 O O   . ALA B 1 121 ? -84.943  40.131 -62.310 1.00 25.72 ? 121  ALA B O   1 
ATOM   3230 C CB  . ALA B 1 121 ? -84.016  37.200 -62.252 1.00 24.60 ? 121  ALA B CB  1 
ATOM   3231 N N   . ASP B 1 122 ? -84.713  39.621 -64.480 1.00 20.85 ? 122  ASP B N   1 
ATOM   3232 C CA  . ASP B 1 122 ? -85.704  40.589 -64.947 1.00 22.14 ? 122  ASP B CA  1 
ATOM   3233 C C   . ASP B 1 122 ? -87.016  39.912 -65.316 1.00 21.80 ? 122  ASP B C   1 
ATOM   3234 O O   . ASP B 1 122 ? -88.051  40.566 -65.475 1.00 20.59 ? 122  ASP B O   1 
ATOM   3235 C CB  . ASP B 1 122 ? -85.195  41.327 -66.201 1.00 21.09 ? 122  ASP B CB  1 
ATOM   3236 C CG  . ASP B 1 122 ? -83.886  42.069 -65.970 1.00 23.84 ? 122  ASP B CG  1 
ATOM   3237 O OD1 . ASP B 1 122 ? -83.822  42.924 -65.066 1.00 28.58 ? 122  ASP B OD1 1 
ATOM   3238 O OD2 . ASP B 1 122 ? -82.907  41.804 -66.694 1.00 25.07 ? 122  ASP B OD2 1 
ATOM   3239 N N   . HIS B 1 123 ? -86.972  38.596 -65.459 1.00 23.98 ? 123  HIS B N   1 
ATOM   3240 C CA  . HIS B 1 123 ? -88.152  37.866 -65.886 1.00 23.97 ? 123  HIS B CA  1 
ATOM   3241 C C   . HIS B 1 123 ? -87.984  36.399 -65.533 1.00 24.13 ? 123  HIS B C   1 
ATOM   3242 O O   . HIS B 1 123 ? -86.871  35.879 -65.536 1.00 26.56 ? 123  HIS B O   1 
ATOM   3243 C CB  . HIS B 1 123 ? -88.308  38.046 -67.412 1.00 25.05 ? 123  HIS B CB  1 
ATOM   3244 C CG  . HIS B 1 123 ? -89.482  37.331 -68.003 1.00 29.48 ? 123  HIS B CG  1 
ATOM   3245 N ND1 . HIS B 1 123 ? -90.676  37.172 -67.332 1.00 33.56 ? 123  HIS B ND1 1 
ATOM   3246 C CD2 . HIS B 1 123 ? -89.667  36.781 -69.226 1.00 30.88 ? 123  HIS B CD2 1 
ATOM   3247 C CE1 . HIS B 1 123 ? -91.544  36.560 -68.115 1.00 31.48 ? 123  HIS B CE1 1 
ATOM   3248 N NE2 . HIS B 1 123 ? -90.958  36.313 -69.271 1.00 34.01 ? 123  HIS B NE2 1 
ATOM   3249 N N   . ILE B 1 124 ? -89.094  35.741 -65.225 1.00 24.69 ? 124  ILE B N   1 
ATOM   3250 C CA  . ILE B 1 124 ? -89.081  34.328 -64.889 1.00 24.03 ? 124  ILE B CA  1 
ATOM   3251 C C   . ILE B 1 124 ? -90.015  33.541 -65.821 1.00 24.92 ? 124  ILE B C   1 
ATOM   3252 O O   . ILE B 1 124 ? -91.110  34.003 -66.143 1.00 26.94 ? 124  ILE B O   1 
ATOM   3253 C CB  . ILE B 1 124 ? -89.593  34.065 -63.430 1.00 24.44 ? 124  ILE B CB  1 
ATOM   3254 C CG1 . ILE B 1 124 ? -88.770  34.840 -62.387 1.00 22.88 ? 124  ILE B CG1 1 
ATOM   3255 C CG2 . ILE B 1 124 ? -89.570  32.579 -63.154 1.00 22.07 ? 124  ILE B CG2 1 
ATOM   3256 C CD1 . ILE B 1 124 ? -87.299  34.505 -62.342 1.00 22.70 ? 124  ILE B CD1 1 
ATOM   3257 N N   . ILE B 1 125 ? -89.574  32.359 -66.247 1.00 22.67 ? 125  ILE B N   1 
ATOM   3258 C CA  . ILE B 1 125 ? -90.376  31.467 -67.077 1.00 20.11 ? 125  ILE B CA  1 
ATOM   3259 C C   . ILE B 1 125 ? -90.275  30.105 -66.380 1.00 21.28 ? 125  ILE B C   1 
ATOM   3260 O O   . ILE B 1 125 ? -89.180  29.569 -66.226 1.00 21.69 ? 125  ILE B O   1 
ATOM   3261 C CB  . ILE B 1 125 ? -89.822  31.370 -68.529 1.00 22.02 ? 125  ILE B CB  1 
ATOM   3262 C CG1 . ILE B 1 125 ? -89.993  32.725 -69.240 1.00 21.59 ? 125  ILE B CG1 1 
ATOM   3263 C CG2 . ILE B 1 125 ? -90.577  30.275 -69.308 1.00 17.66 ? 125  ILE B CG2 1 
ATOM   3264 C CD1 . ILE B 1 125 ? -89.333  32.810 -70.613 1.00 21.58 ? 125  ILE B CD1 1 
ATOM   3265 N N   . THR B 1 126 ? -91.406  29.557 -65.936 1.00 22.24 ? 126  THR B N   1 
ATOM   3266 C CA  . THR B 1 126 ? -91.397  28.279 -65.229 1.00 22.80 ? 126  THR B CA  1 
ATOM   3267 C C   . THR B 1 126 ? -92.608  27.446 -65.676 1.00 22.40 ? 126  THR B C   1 
ATOM   3268 O O   . THR B 1 126 ? -93.431  27.918 -66.464 1.00 22.74 ? 126  THR B O   1 
ATOM   3269 C CB  . THR B 1 126 ? -91.421  28.546 -63.680 1.00 22.77 ? 126  THR B CB  1 
ATOM   3270 O OG1 . THR B 1 126 ? -91.278  27.319 -62.950 1.00 27.11 ? 126  THR B OG1 1 
ATOM   3271 C CG2 . THR B 1 126 ? -92.716  29.226 -63.285 1.00 22.76 ? 126  THR B CG2 1 
ATOM   3272 N N   . MET B 1 127 ? -92.708  26.206 -65.212 1.00 20.14 ? 127  MET B N   1 
ATOM   3273 C CA  . MET B 1 127 ? -93.855  25.384 -65.580 1.00 20.89 ? 127  MET B CA  1 
ATOM   3274 C C   . MET B 1 127 ? -94.554  24.817 -64.349 1.00 22.30 ? 127  MET B C   1 
ATOM   3275 O O   . MET B 1 127 ? -93.928  24.198 -63.490 1.00 23.26 ? 127  MET B O   1 
ATOM   3276 C CB  . MET B 1 127 ? -93.451  24.238 -66.518 1.00 19.48 ? 127  MET B CB  1 
ATOM   3277 C CG  . MET B 1 127 ? -94.639  23.437 -67.030 1.00 23.16 ? 127  MET B CG  1 
ATOM   3278 S SD  . MET B 1 127 ? -94.258  22.331 -68.411 1.00 28.13 ? 127  MET B SD  1 
ATOM   3279 C CE  . MET B 1 127 ? -94.159  23.528 -69.757 1.00 22.94 ? 127  MET B CE  1 
ATOM   3280 N N   . ASP B 1 128 ? -95.858  25.060 -64.280 1.00 22.99 ? 128  ASP B N   1 
ATOM   3281 C CA  . ASP B 1 128 ? -96.701  24.588 -63.197 1.00 25.33 ? 128  ASP B CA  1 
ATOM   3282 C C   . ASP B 1 128 ? -96.171  24.825 -61.784 1.00 25.81 ? 128  ASP B C   1 
ATOM   3283 O O   . ASP B 1 128 ? -95.790  23.882 -61.081 1.00 24.78 ? 128  ASP B O   1 
ATOM   3284 C CB  . ASP B 1 128 ? -97.021  23.101 -63.396 1.00 28.15 ? 128  ASP B CB  1 
ATOM   3285 C CG  . ASP B 1 128 ? -97.932  22.858 -64.589 1.00 31.43 ? 128  ASP B CG  1 
ATOM   3286 O OD1 . ASP B 1 128 ? -99.042  23.436 -64.628 1.00 33.77 ? 128  ASP B OD1 1 
ATOM   3287 O OD2 . ASP B 1 128 ? -97.540  22.093 -65.491 1.00 34.36 ? 128  ASP B OD2 1 
ATOM   3288 N N   . LEU B 1 129 ? -96.154  26.089 -61.368 1.00 24.14 ? 129  LEU B N   1 
ATOM   3289 C CA  . LEU B 1 129 ? -95.713  26.417 -60.025 1.00 26.16 ? 129  LEU B CA  1 
ATOM   3290 C C   . LEU B 1 129 ? -96.567  25.591 -59.090 1.00 25.16 ? 129  LEU B C   1 
ATOM   3291 O O   . LEU B 1 129 ? -97.759  25.406 -59.345 1.00 24.08 ? 129  LEU B O   1 
ATOM   3292 C CB  . LEU B 1 129 ? -95.936  27.892 -59.729 1.00 26.12 ? 129  LEU B CB  1 
ATOM   3293 C CG  . LEU B 1 129 ? -94.942  28.810 -60.413 1.00 27.06 ? 129  LEU B CG  1 
ATOM   3294 C CD1 . LEU B 1 129 ? -95.397  30.246 -60.227 1.00 29.72 ? 129  LEU B CD1 1 
ATOM   3295 C CD2 . LEU B 1 129 ? -93.542  28.583 -59.818 1.00 25.25 ? 129  LEU B CD2 1 
ATOM   3296 N N   . HIS B 1 130 ? -95.962  25.097 -58.015 1.00 24.92 ? 130  HIS B N   1 
ATOM   3297 C CA  . HIS B 1 130 ? -96.688  24.278 -57.059 1.00 27.32 ? 130  HIS B CA  1 
ATOM   3298 C C   . HIS B 1 130 ? -97.951  24.978 -56.596 1.00 26.06 ? 130  HIS B C   1 
ATOM   3299 O O   . HIS B 1 130 ? -98.948  24.328 -56.299 1.00 26.57 ? 130  HIS B O   1 
ATOM   3300 C CB  . HIS B 1 130 ? -95.810  23.946 -55.853 1.00 30.10 ? 130  HIS B CB  1 
ATOM   3301 C CG  . HIS B 1 130 ? -96.510  23.126 -54.817 1.00 30.86 ? 130  HIS B CG  1 
ATOM   3302 N ND1 . HIS B 1 130 ? -96.822  23.613 -53.567 1.00 32.40 ? 130  HIS B ND1 1 
ATOM   3303 C CD2 . HIS B 1 130 ? -97.006  21.868 -54.868 1.00 31.23 ? 130  HIS B CD2 1 
ATOM   3304 C CE1 . HIS B 1 130 ? -97.483  22.689 -52.890 1.00 28.53 ? 130  HIS B CE1 1 
ATOM   3305 N NE2 . HIS B 1 130 ? -97.606  21.623 -53.656 1.00 31.64 ? 130  HIS B NE2 1 
ATOM   3306 N N   . ALA B 1 131 ? -97.890  26.306 -56.523 1.00 25.00 ? 131  ALA B N   1 
ATOM   3307 C CA  . ALA B 1 131 ? -99.029  27.125 -56.128 1.00 24.95 ? 131  ALA B CA  1 
ATOM   3308 C C   . ALA B 1 131 ? -98.967  28.401 -56.949 1.00 24.79 ? 131  ALA B C   1 
ATOM   3309 O O   . ALA B 1 131 ? -97.953  29.099 -56.944 1.00 24.89 ? 131  ALA B O   1 
ATOM   3310 C CB  . ALA B 1 131 ? -98.969  27.449 -54.635 1.00 22.45 ? 131  ALA B CB  1 
ATOM   3311 N N   . ALA B 1 132 ? -100.050 28.701 -57.658 1.00 26.07 ? 132  ALA B N   1 
ATOM   3312 C CA  . ALA B 1 132 ? -100.107 29.899 -58.495 1.00 26.12 ? 132  ALA B CA  1 
ATOM   3313 C C   . ALA B 1 132 ? -99.729  31.161 -57.707 1.00 26.81 ? 132  ALA B C   1 
ATOM   3314 O O   . ALA B 1 132 ? -99.184  32.108 -58.275 1.00 27.00 ? 132  ALA B O   1 
ATOM   3315 C CB  . ALA B 1 132 ? -101.495 30.056 -59.089 1.00 21.40 ? 132  ALA B CB  1 
ATOM   3316 N N   . GLN B 1 133 ? -100.013 31.169 -56.408 1.00 24.31 ? 133  GLN B N   1 
ATOM   3317 C CA  . GLN B 1 133 ? -99.692  32.329 -55.583 1.00 25.35 ? 133  GLN B CA  1 
ATOM   3318 C C   . GLN B 1 133 ? -98.204  32.652 -55.604 1.00 24.57 ? 133  GLN B C   1 
ATOM   3319 O O   . GLN B 1 133 ? -97.794  33.737 -55.213 1.00 27.31 ? 133  GLN B O   1 
ATOM   3320 C CB  . GLN B 1 133 ? -100.143 32.119 -54.130 1.00 25.04 ? 133  GLN B CB  1 
ATOM   3321 C CG  . GLN B 1 133 ? -101.654 32.172 -53.909 1.00 25.97 ? 133  GLN B CG  1 
ATOM   3322 C CD  . GLN B 1 133 ? -102.354 30.861 -54.240 1.00 28.56 ? 133  GLN B CD  1 
ATOM   3323 O OE1 . GLN B 1 133 ? -101.738 29.916 -54.731 1.00 26.44 ? 133  GLN B OE1 1 
ATOM   3324 N NE2 . GLN B 1 133 ? -103.650 30.801 -53.966 1.00 28.93 ? 133  GLN B NE2 1 
ATOM   3325 N N   . ILE B 1 134 ? -97.389  31.714 -56.061 1.00 26.19 ? 134  ILE B N   1 
ATOM   3326 C CA  . ILE B 1 134 ? -95.953  31.947 -56.096 1.00 25.19 ? 134  ILE B CA  1 
ATOM   3327 C C   . ILE B 1 134 ? -95.549  33.084 -57.040 1.00 25.28 ? 134  ILE B C   1 
ATOM   3328 O O   . ILE B 1 134 ? -94.512  33.716 -56.837 1.00 26.13 ? 134  ILE B O   1 
ATOM   3329 C CB  . ILE B 1 134 ? -95.194  30.638 -56.440 1.00 25.35 ? 134  ILE B CB  1 
ATOM   3330 C CG1 . ILE B 1 134 ? -95.338  29.666 -55.268 1.00 24.82 ? 134  ILE B CG1 1 
ATOM   3331 C CG2 . ILE B 1 134 ? -93.708  30.926 -56.736 1.00 21.17 ? 134  ILE B CG2 1 
ATOM   3332 C CD1 . ILE B 1 134 ? -94.600  28.353 -55.438 1.00 25.82 ? 134  ILE B CD1 1 
ATOM   3333 N N   . GLN B 1 135 ? -96.356  33.362 -58.061 1.00 24.12 ? 135  GLN B N   1 
ATOM   3334 C CA  . GLN B 1 135 ? -96.025  34.472 -58.955 1.00 22.79 ? 135  GLN B CA  1 
ATOM   3335 C C   . GLN B 1 135 ? -95.992  35.741 -58.120 1.00 22.85 ? 135  GLN B C   1 
ATOM   3336 O O   . GLN B 1 135 ? -95.186  36.629 -58.360 1.00 24.20 ? 135  GLN B O   1 
ATOM   3337 C CB  . GLN B 1 135 ? -97.054  34.631 -60.074 1.00 24.25 ? 135  GLN B CB  1 
ATOM   3338 C CG  . GLN B 1 135 ? -96.961  33.571 -61.159 1.00 24.91 ? 135  GLN B CG  1 
ATOM   3339 C CD  . GLN B 1 135 ? -97.648  34.002 -62.443 1.00 25.70 ? 135  GLN B CD  1 
ATOM   3340 O OE1 . GLN B 1 135 ? -97.441  35.111 -62.933 1.00 29.02 ? 135  GLN B OE1 1 
ATOM   3341 N NE2 . GLN B 1 135 ? -98.451  33.125 -63.001 1.00 24.21 ? 135  GLN B NE2 1 
ATOM   3342 N N   . GLY B 1 136 ? -96.876  35.814 -57.133 1.00 22.48 ? 136  GLY B N   1 
ATOM   3343 C CA  . GLY B 1 136 ? -96.922  36.970 -56.260 1.00 21.99 ? 136  GLY B CA  1 
ATOM   3344 C C   . GLY B 1 136 ? -95.719  37.130 -55.338 1.00 23.44 ? 136  GLY B C   1 
ATOM   3345 O O   . GLY B 1 136 ? -95.625  38.119 -54.626 1.00 22.96 ? 136  GLY B O   1 
ATOM   3346 N N   . PHE B 1 137 ? -94.807  36.159 -55.327 1.00 22.49 ? 137  PHE B N   1 
ATOM   3347 C CA  . PHE B 1 137 ? -93.614  36.256 -54.491 1.00 22.42 ? 137  PHE B CA  1 
ATOM   3348 C C   . PHE B 1 137 ? -92.557  37.128 -55.179 1.00 23.01 ? 137  PHE B C   1 
ATOM   3349 O O   . PHE B 1 137 ? -91.545  37.469 -54.590 1.00 21.59 ? 137  PHE B O   1 
ATOM   3350 C CB  . PHE B 1 137 ? -93.029  34.862 -54.209 1.00 19.71 ? 137  PHE B CB  1 
ATOM   3351 C CG  . PHE B 1 137 ? -93.845  34.029 -53.246 1.00 19.45 ? 137  PHE B CG  1 
ATOM   3352 C CD1 . PHE B 1 137 ? -93.423  32.747 -52.891 1.00 20.03 ? 137  PHE B CD1 1 
ATOM   3353 C CD2 . PHE B 1 137 ? -95.011  34.528 -52.672 1.00 19.49 ? 137  PHE B CD2 1 
ATOM   3354 C CE1 . PHE B 1 137 ? -94.142  31.979 -51.977 1.00 18.00 ? 137  PHE B CE1 1 
ATOM   3355 C CE2 . PHE B 1 137 ? -95.741  33.772 -51.759 1.00 19.98 ? 137  PHE B CE2 1 
ATOM   3356 C CZ  . PHE B 1 137 ? -95.308  32.492 -51.407 1.00 20.21 ? 137  PHE B CZ  1 
ATOM   3357 N N   . PHE B 1 138 ? -92.803  37.473 -56.438 1.00 23.66 ? 138  PHE B N   1 
ATOM   3358 C CA  . PHE B 1 138 ? -91.889  38.305 -57.210 1.00 24.35 ? 138  PHE B CA  1 
ATOM   3359 C C   . PHE B 1 138 ? -92.568  39.628 -57.515 1.00 24.73 ? 138  PHE B C   1 
ATOM   3360 O O   . PHE B 1 138 ? -93.779  39.757 -57.377 1.00 25.56 ? 138  PHE B O   1 
ATOM   3361 C CB  . PHE B 1 138 ? -91.561  37.685 -58.584 1.00 21.75 ? 138  PHE B CB  1 
ATOM   3362 C CG  . PHE B 1 138 ? -90.818  36.391 -58.525 1.00 24.86 ? 138  PHE B CG  1 
ATOM   3363 C CD1 . PHE B 1 138 ? -91.498  35.184 -58.349 1.00 23.85 ? 138  PHE B CD1 1 
ATOM   3364 C CD2 . PHE B 1 138 ? -89.433  36.367 -58.697 1.00 23.11 ? 138  PHE B CD2 1 
ATOM   3365 C CE1 . PHE B 1 138 ? -90.808  33.978 -58.347 1.00 24.25 ? 138  PHE B CE1 1 
ATOM   3366 C CE2 . PHE B 1 138 ? -88.731  35.165 -58.699 1.00 23.92 ? 138  PHE B CE2 1 
ATOM   3367 C CZ  . PHE B 1 138 ? -89.415  33.969 -58.527 1.00 23.58 ? 138  PHE B CZ  1 
ATOM   3368 N N   . ASP B 1 139 ? -91.774  40.602 -57.949 1.00 26.37 ? 139  ASP B N   1 
ATOM   3369 C CA  . ASP B 1 139 ? -92.316  41.877 -58.381 1.00 28.33 ? 139  ASP B CA  1 
ATOM   3370 C C   . ASP B 1 139 ? -92.099  41.940 -59.893 1.00 28.51 ? 139  ASP B C   1 
ATOM   3371 O O   . ASP B 1 139 ? -92.837  42.623 -60.600 1.00 31.95 ? 139  ASP B O   1 
ATOM   3372 C CB  . ASP B 1 139 ? -91.656  43.061 -57.668 1.00 31.15 ? 139  ASP B CB  1 
ATOM   3373 C CG  . ASP B 1 139 ? -92.320  43.366 -56.326 1.00 33.72 ? 139  ASP B CG  1 
ATOM   3374 O OD1 . ASP B 1 139 ? -93.562  43.274 -56.246 1.00 31.47 ? 139  ASP B OD1 1 
ATOM   3375 O OD2 . ASP B 1 139 ? -91.608  43.697 -55.358 1.00 36.42 ? 139  ASP B OD2 1 
ATOM   3376 N N   . ILE B 1 140 ? -91.096  41.205 -60.380 1.00 25.98 ? 140  ILE B N   1 
ATOM   3377 C CA  . ILE B 1 140 ? -90.795  41.118 -61.814 1.00 23.65 ? 140  ILE B CA  1 
ATOM   3378 C C   . ILE B 1 140 ? -91.829  40.173 -62.424 1.00 24.18 ? 140  ILE B C   1 
ATOM   3379 O O   . ILE B 1 140 ? -92.394  39.327 -61.725 1.00 24.02 ? 140  ILE B O   1 
ATOM   3380 C CB  . ILE B 1 140 ? -89.391  40.496 -62.093 1.00 21.31 ? 140  ILE B CB  1 
ATOM   3381 C CG1 . ILE B 1 140 ? -89.245  39.181 -61.307 1.00 21.79 ? 140  ILE B CG1 1 
ATOM   3382 C CG2 . ILE B 1 140 ? -88.293  41.500 -61.774 1.00 22.13 ? 140  ILE B CG2 1 
ATOM   3383 C CD1 . ILE B 1 140 ? -87.897  38.516 -61.421 1.00 18.12 ? 140  ILE B CD1 1 
ATOM   3384 N N   . PRO B 1 141 ? -92.078  40.289 -63.736 1.00 23.58 ? 141  PRO B N   1 
ATOM   3385 C CA  . PRO B 1 141 ? -93.059  39.407 -64.373 1.00 22.17 ? 141  PRO B CA  1 
ATOM   3386 C C   . PRO B 1 141 ? -92.676  37.931 -64.417 1.00 22.95 ? 141  PRO B C   1 
ATOM   3387 O O   . PRO B 1 141 ? -91.528  37.565 -64.670 1.00 22.39 ? 141  PRO B O   1 
ATOM   3388 C CB  . PRO B 1 141 ? -93.211  40.007 -65.769 1.00 21.23 ? 141  PRO B CB  1 
ATOM   3389 C CG  . PRO B 1 141 ? -91.873  40.582 -66.038 1.00 23.42 ? 141  PRO B CG  1 
ATOM   3390 C CD  . PRO B 1 141 ? -91.530  41.248 -64.709 1.00 24.24 ? 141  PRO B CD  1 
ATOM   3391 N N   . VAL B 1 142 ? -93.671  37.088 -64.176 1.00 23.95 ? 142  VAL B N   1 
ATOM   3392 C CA  . VAL B 1 142 ? -93.487  35.650 -64.198 1.00 23.91 ? 142  VAL B CA  1 
ATOM   3393 C C   . VAL B 1 142 ? -94.463  35.007 -65.189 1.00 24.78 ? 142  VAL B C   1 
ATOM   3394 O O   . VAL B 1 142 ? -95.657  35.294 -65.170 1.00 23.40 ? 142  VAL B O   1 
ATOM   3395 C CB  . VAL B 1 142 ? -93.759  35.020 -62.796 1.00 24.90 ? 142  VAL B CB  1 
ATOM   3396 C CG1 . VAL B 1 142 ? -93.635  33.509 -62.880 1.00 22.11 ? 142  VAL B CG1 1 
ATOM   3397 C CG2 . VAL B 1 142 ? -92.803  35.590 -61.744 1.00 20.14 ? 142  VAL B CG2 1 
ATOM   3398 N N   . ASP B 1 143 ? -93.954  34.156 -66.070 1.00 25.20 ? 143  ASP B N   1 
ATOM   3399 C CA  . ASP B 1 143 ? -94.831  33.439 -66.988 1.00 25.06 ? 143  ASP B CA  1 
ATOM   3400 C C   . ASP B 1 143 ? -94.848  31.990 -66.487 1.00 25.43 ? 143  ASP B C   1 
ATOM   3401 O O   . ASP B 1 143 ? -93.842  31.284 -66.538 1.00 26.09 ? 143  ASP B O   1 
ATOM   3402 C CB  . ASP B 1 143 ? -94.315  33.512 -68.430 1.00 26.75 ? 143  ASP B CB  1 
ATOM   3403 C CG  . ASP B 1 143 ? -94.448  34.912 -69.034 1.00 28.41 ? 143  ASP B CG  1 
ATOM   3404 O OD1 . ASP B 1 143 ? -95.537  35.516 -68.910 1.00 27.05 ? 143  ASP B OD1 1 
ATOM   3405 O OD2 . ASP B 1 143 ? -93.468  35.402 -69.637 1.00 26.51 ? 143  ASP B OD2 1 
ATOM   3406 N N   . ASN B 1 144 ? -95.990  31.573 -65.960 1.00 26.78 ? 144  ASN B N   1 
ATOM   3407 C CA  . ASN B 1 144 ? -96.160  30.228 -65.433 1.00 27.43 ? 144  ASN B CA  1 
ATOM   3408 C C   . ASN B 1 144 ? -96.898  29.387 -66.469 1.00 27.00 ? 144  ASN B C   1 
ATOM   3409 O O   . ASN B 1 144 ? -98.122  29.440 -66.576 1.00 25.86 ? 144  ASN B O   1 
ATOM   3410 C CB  . ASN B 1 144 ? -96.944  30.292 -64.110 1.00 27.38 ? 144  ASN B CB  1 
ATOM   3411 C CG  . ASN B 1 144 ? -97.166  28.930 -63.490 1.00 27.37 ? 144  ASN B CG  1 
ATOM   3412 O OD1 . ASN B 1 144 ? -96.272  28.080 -63.475 1.00 25.72 ? 144  ASN B OD1 1 
ATOM   3413 N ND2 . ASN B 1 144 ? -98.360  28.721 -62.951 1.00 29.68 ? 144  ASN B ND2 1 
ATOM   3414 N N   . LEU B 1 145 ? -96.129  28.626 -67.238 1.00 28.90 ? 145  LEU B N   1 
ATOM   3415 C CA  . LEU B 1 145 ? -96.659  27.764 -68.289 1.00 29.75 ? 145  LEU B CA  1 
ATOM   3416 C C   . LEU B 1 145 ? -97.329  26.520 -67.727 1.00 31.76 ? 145  LEU B C   1 
ATOM   3417 O O   . LEU B 1 145 ? -96.964  26.033 -66.652 1.00 31.40 ? 145  LEU B O   1 
ATOM   3418 C CB  . LEU B 1 145 ? -95.529  27.335 -69.226 1.00 29.39 ? 145  LEU B CB  1 
ATOM   3419 C CG  . LEU B 1 145 ? -94.704  28.452 -69.863 1.00 28.45 ? 145  LEU B CG  1 
ATOM   3420 C CD1 . LEU B 1 145 ? -93.521  27.851 -70.597 1.00 27.30 ? 145  LEU B CD1 1 
ATOM   3421 C CD2 . LEU B 1 145 ? -95.579  29.273 -70.789 1.00 28.85 ? 145  LEU B CD2 1 
ATOM   3422 N N   . TYR B 1 146 ? -98.304  26.002 -68.466 1.00 34.08 ? 146  TYR B N   1 
ATOM   3423 C CA  . TYR B 1 146 ? -99.015  24.804 -68.046 1.00 34.64 ? 146  TYR B CA  1 
ATOM   3424 C C   . TYR B 1 146 ? -98.678  23.612 -68.902 1.00 33.75 ? 146  TYR B C   1 
ATOM   3425 O O   . TYR B 1 146 ? -98.497  23.734 -70.112 1.00 33.19 ? 146  TYR B O   1 
ATOM   3426 C CB  . TYR B 1 146 ? -100.520 25.004 -68.125 1.00 38.88 ? 146  TYR B CB  1 
ATOM   3427 C CG  . TYR B 1 146 ? -101.017 26.147 -67.308 1.00 45.13 ? 146  TYR B CG  1 
ATOM   3428 C CD1 . TYR B 1 146 ? -101.282 27.377 -67.896 1.00 49.89 ? 146  TYR B CD1 1 
ATOM   3429 C CD2 . TYR B 1 146 ? -101.222 26.007 -65.939 1.00 48.88 ? 146  TYR B CD2 1 
ATOM   3430 C CE1 . TYR B 1 146 ? -101.742 28.442 -67.142 1.00 52.68 ? 146  TYR B CE1 1 
ATOM   3431 C CE2 . TYR B 1 146 ? -101.683 27.064 -65.174 1.00 52.11 ? 146  TYR B CE2 1 
ATOM   3432 C CZ  . TYR B 1 146 ? -101.945 28.274 -65.784 1.00 52.64 ? 146  TYR B CZ  1 
ATOM   3433 O OH  . TYR B 1 146 ? -102.464 29.305 -65.051 1.00 56.65 ? 146  TYR B OH  1 
ATOM   3434 N N   . ALA B 1 147 ? -98.604  22.449 -68.271 1.00 32.93 ? 147  ALA B N   1 
ATOM   3435 C CA  . ALA B 1 147 ? -98.339  21.232 -69.012 1.00 33.14 ? 147  ALA B CA  1 
ATOM   3436 C C   . ALA B 1 147 ? -99.699  20.632 -69.379 1.00 31.83 ? 147  ALA B C   1 
ATOM   3437 O O   . ALA B 1 147 ? -99.772  19.647 -70.108 1.00 32.64 ? 147  ALA B O   1 
ATOM   3438 C CB  . ALA B 1 147 ? -97.540  20.252 -68.150 1.00 33.20 ? 147  ALA B CB  1 
ATOM   3439 N N   . GLU B 1 148 ? -100.773 21.250 -68.885 1.00 31.87 ? 148  GLU B N   1 
ATOM   3440 C CA  . GLU B 1 148 ? -102.132 20.763 -69.132 1.00 34.60 ? 148  GLU B CA  1 
ATOM   3441 C C   . GLU B 1 148 ? -102.458 20.416 -70.587 1.00 34.72 ? 148  GLU B C   1 
ATOM   3442 O O   . GLU B 1 148 ? -102.888 19.297 -70.878 1.00 33.82 ? 148  GLU B O   1 
ATOM   3443 C CB  . GLU B 1 148 ? -103.180 21.755 -68.609 1.00 34.34 ? 148  GLU B CB  1 
ATOM   3444 C CG  . GLU B 1 148 ? -104.606 21.206 -68.697 1.00 37.45 ? 148  GLU B CG  1 
ATOM   3445 C CD  . GLU B 1 148 ? -105.614 21.989 -67.869 1.00 40.74 ? 148  GLU B CD  1 
ATOM   3446 O OE1 . GLU B 1 148 ? -105.213 22.590 -66.853 1.00 45.15 ? 148  GLU B OE1 1 
ATOM   3447 O OE2 . GLU B 1 148 ? -106.814 21.987 -68.212 1.00 40.57 ? 148  GLU B OE2 1 
ATOM   3448 N N   . PRO B 1 149 ? -102.260 21.365 -71.519 1.00 35.00 ? 149  PRO B N   1 
ATOM   3449 C CA  . PRO B 1 149 ? -102.571 21.041 -72.916 1.00 34.38 ? 149  PRO B CA  1 
ATOM   3450 C C   . PRO B 1 149 ? -101.878 19.750 -73.361 1.00 34.21 ? 149  PRO B C   1 
ATOM   3451 O O   . PRO B 1 149 ? -102.477 18.923 -74.048 1.00 33.74 ? 149  PRO B O   1 
ATOM   3452 C CB  . PRO B 1 149 ? -102.077 22.275 -73.675 1.00 34.39 ? 149  PRO B CB  1 
ATOM   3453 C CG  . PRO B 1 149 ? -102.283 23.388 -72.650 1.00 34.71 ? 149  PRO B CG  1 
ATOM   3454 C CD  . PRO B 1 149 ? -101.768 22.751 -71.390 1.00 34.02 ? 149  PRO B CD  1 
ATOM   3455 N N   . ALA B 1 150 ? -100.623 19.577 -72.953 1.00 32.99 ? 150  ALA B N   1 
ATOM   3456 C CA  . ALA B 1 150 ? -99.859  18.384 -73.315 1.00 33.64 ? 150  ALA B CA  1 
ATOM   3457 C C   . ALA B 1 150 ? -100.390 17.141 -72.602 1.00 31.96 ? 150  ALA B C   1 
ATOM   3458 O O   . ALA B 1 150 ? -100.329 16.036 -73.133 1.00 32.96 ? 150  ALA B O   1 
ATOM   3459 C CB  . ALA B 1 150 ? -98.381  18.581 -72.986 1.00 34.14 ? 150  ALA B CB  1 
ATOM   3460 N N   . VAL B 1 151 ? -100.908 17.326 -71.396 1.00 30.48 ? 151  VAL B N   1 
ATOM   3461 C CA  . VAL B 1 151 ? -101.451 16.218 -70.625 1.00 28.01 ? 151  VAL B CA  1 
ATOM   3462 C C   . VAL B 1 151 ? -102.787 15.775 -71.234 1.00 29.93 ? 151  VAL B C   1 
ATOM   3463 O O   . VAL B 1 151 ? -103.015 14.582 -71.466 1.00 29.03 ? 151  VAL B O   1 
ATOM   3464 C CB  . VAL B 1 151 ? -101.629 16.638 -69.147 1.00 27.67 ? 151  VAL B CB  1 
ATOM   3465 C CG1 . VAL B 1 151 ? -102.429 15.604 -68.385 1.00 24.07 ? 151  VAL B CG1 1 
ATOM   3466 C CG2 . VAL B 1 151 ? -100.248 16.826 -68.510 1.00 24.88 ? 151  VAL B CG2 1 
ATOM   3467 N N   . LEU B 1 152 ? -103.659 16.742 -71.508 1.00 29.93 ? 152  LEU B N   1 
ATOM   3468 C CA  . LEU B 1 152 ? -104.956 16.451 -72.106 1.00 31.38 ? 152  LEU B CA  1 
ATOM   3469 C C   . LEU B 1 152 ? -104.772 15.708 -73.433 1.00 32.53 ? 152  LEU B C   1 
ATOM   3470 O O   . LEU B 1 152 ? -105.567 14.839 -73.786 1.00 33.45 ? 152  LEU B O   1 
ATOM   3471 C CB  . LEU B 1 152 ? -105.738 17.757 -72.330 1.00 31.88 ? 152  LEU B CB  1 
ATOM   3472 C CG  . LEU B 1 152 ? -106.228 18.483 -71.063 1.00 31.43 ? 152  LEU B CG  1 
ATOM   3473 C CD1 . LEU B 1 152 ? -106.975 19.747 -71.416 1.00 30.74 ? 152  LEU B CD1 1 
ATOM   3474 C CD2 . LEU B 1 152 ? -107.131 17.556 -70.284 1.00 34.04 ? 152  LEU B CD2 1 
ATOM   3475 N N   . LYS B 1 153 ? -103.704 16.045 -74.150 1.00 33.56 ? 153  LYS B N   1 
ATOM   3476 C CA  . LYS B 1 153 ? -103.396 15.431 -75.437 1.00 33.12 ? 153  LYS B CA  1 
ATOM   3477 C C   . LYS B 1 153 ? -102.856 14.014 -75.266 1.00 33.18 ? 153  LYS B C   1 
ATOM   3478 O O   . LYS B 1 153 ? -103.206 13.111 -76.027 1.00 32.79 ? 153  LYS B O   1 
ATOM   3479 C CB  . LYS B 1 153 ? -102.378 16.296 -76.180 1.00 36.13 ? 153  LYS B CB  1 
ATOM   3480 C CG  . LYS B 1 153 ? -101.999 15.811 -77.569 1.00 38.67 ? 153  LYS B CG  1 
ATOM   3481 C CD  . LYS B 1 153 ? -101.227 16.905 -78.302 1.00 41.16 ? 153  LYS B CD  1 
ATOM   3482 C CE  . LYS B 1 153 ? -100.953 16.530 -79.744 1.00 42.11 ? 153  LYS B CE  1 
ATOM   3483 N NZ  . LYS B 1 153 ? -99.951  15.443 -79.830 1.00 44.21 ? 153  LYS B NZ  1 
ATOM   3484 N N   . TRP B 1 154 ? -101.999 13.814 -74.272 1.00 31.73 ? 154  TRP B N   1 
ATOM   3485 C CA  . TRP B 1 154 ? -101.453 12.485 -74.029 1.00 30.25 ? 154  TRP B CA  1 
ATOM   3486 C C   . TRP B 1 154 ? -102.633 11.580 -73.659 1.00 30.23 ? 154  TRP B C   1 
ATOM   3487 O O   . TRP B 1 154 ? -102.772 10.462 -74.169 1.00 28.76 ? 154  TRP B O   1 
ATOM   3488 C CB  . TRP B 1 154 ? -100.431 12.511 -72.875 1.00 27.43 ? 154  TRP B CB  1 
ATOM   3489 C CG  . TRP B 1 154 ? -99.685  11.213 -72.723 1.00 26.43 ? 154  TRP B CG  1 
ATOM   3490 C CD1 . TRP B 1 154 ? -98.515  10.858 -73.340 1.00 24.71 ? 154  TRP B CD1 1 
ATOM   3491 C CD2 . TRP B 1 154 ? -100.106 10.056 -71.975 1.00 27.10 ? 154  TRP B CD2 1 
ATOM   3492 N NE1 . TRP B 1 154 ? -98.196  9.551  -73.038 1.00 26.47 ? 154  TRP B NE1 1 
ATOM   3493 C CE2 . TRP B 1 154 ? -99.162  9.034  -72.222 1.00 25.90 ? 154  TRP B CE2 1 
ATOM   3494 C CE3 . TRP B 1 154 ? -101.216 9.780  -71.163 1.00 28.25 ? 154  TRP B CE3 1 
ATOM   3495 C CZ2 . TRP B 1 154 ? -99.267  7.766  -71.640 1.00 27.40 ? 154  TRP B CZ2 1 
ATOM   3496 C CZ3 . TRP B 1 154 ? -101.322 8.516  -70.587 1.00 28.02 ? 154  TRP B CZ3 1 
ATOM   3497 C CH2 . TRP B 1 154 ? -100.363 7.518  -70.846 1.00 28.33 ? 154  TRP B CH2 1 
ATOM   3498 N N   . ILE B 1 155 ? -103.495 12.083 -72.781 1.00 31.46 ? 155  ILE B N   1 
ATOM   3499 C CA  . ILE B 1 155 ? -104.658 11.317 -72.338 1.00 30.70 ? 155  ILE B CA  1 
ATOM   3500 C C   . ILE B 1 155 ? -105.548 10.907 -73.506 1.00 32.22 ? 155  ILE B C   1 
ATOM   3501 O O   . ILE B 1 155 ? -105.783 9.716  -73.722 1.00 32.66 ? 155  ILE B O   1 
ATOM   3502 C CB  . ILE B 1 155 ? -105.499 12.115 -71.324 1.00 28.00 ? 155  ILE B CB  1 
ATOM   3503 C CG1 . ILE B 1 155 ? -104.714 12.287 -70.019 1.00 27.11 ? 155  ILE B CG1 1 
ATOM   3504 C CG2 . ILE B 1 155 ? -106.815 11.409 -71.076 1.00 25.96 ? 155  ILE B CG2 1 
ATOM   3505 C CD1 . ILE B 1 155 ? -105.408 13.170 -68.987 1.00 25.55 ? 155  ILE B CD1 1 
ATOM   3506 N N   . ARG B 1 156 ? -106.034 11.890 -74.261 1.00 33.43 ? 156  ARG B N   1 
ATOM   3507 C CA  . ARG B 1 156 ? -106.904 11.607 -75.401 1.00 35.89 ? 156  ARG B CA  1 
ATOM   3508 C C   . ARG B 1 156 ? -106.267 10.631 -76.390 1.00 36.22 ? 156  ARG B C   1 
ATOM   3509 O O   . ARG B 1 156 ? -106.954 9.804  -76.990 1.00 37.25 ? 156  ARG B O   1 
ATOM   3510 C CB  . ARG B 1 156 ? -107.276 12.898 -76.144 1.00 36.05 ? 156  ARG B CB  1 
ATOM   3511 C CG  . ARG B 1 156 ? -108.169 13.854 -75.376 1.00 36.28 ? 156  ARG B CG  1 
ATOM   3512 C CD  . ARG B 1 156 ? -108.850 14.845 -76.325 1.00 40.18 ? 156  ARG B CD  1 
ATOM   3513 N NE  . ARG B 1 156 ? -109.495 15.928 -75.590 1.00 44.64 ? 156  ARG B NE  1 
ATOM   3514 C CZ  . ARG B 1 156 ? -108.924 17.103 -75.338 1.00 46.77 ? 156  ARG B CZ  1 
ATOM   3515 N NH1 . ARG B 1 156 ? -107.693 17.357 -75.775 1.00 45.19 ? 156  ARG B NH1 1 
ATOM   3516 N NH2 . ARG B 1 156 ? -109.576 18.017 -74.627 1.00 47.26 ? 156  ARG B NH2 1 
ATOM   3517 N N   . GLU B 1 157 ? -104.952 10.724 -76.544 1.00 36.32 ? 157  GLU B N   1 
ATOM   3518 C CA  . GLU B 1 157 ? -104.218 9.869  -77.465 1.00 36.55 ? 157  GLU B CA  1 
ATOM   3519 C C   . GLU B 1 157 ? -103.729 8.534  -76.900 1.00 36.79 ? 157  GLU B C   1 
ATOM   3520 O O   . GLU B 1 157 ? -103.469 7.606  -77.662 1.00 36.66 ? 157  GLU B O   1 
ATOM   3521 C CB  . GLU B 1 157 ? -103.018 10.638 -78.029 1.00 39.47 ? 157  GLU B CB  1 
ATOM   3522 C CG  . GLU B 1 157 ? -103.367 11.575 -79.179 1.00 42.75 ? 157  GLU B CG  1 
ATOM   3523 C CD  . GLU B 1 157 ? -102.322 12.654 -79.416 1.00 45.61 ? 157  GLU B CD  1 
ATOM   3524 O OE1 . GLU B 1 157 ? -101.111 12.385 -79.245 1.00 42.93 ? 157  GLU B OE1 1 
ATOM   3525 O OE2 . GLU B 1 157 ? -102.722 13.779 -79.789 1.00 49.12 ? 157  GLU B OE2 1 
ATOM   3526 N N   . ASN B 1 158 ? -103.619 8.409  -75.582 1.00 34.02 ? 158  ASN B N   1 
ATOM   3527 C CA  . ASN B 1 158 ? -103.111 7.158  -75.027 1.00 33.66 ? 158  ASN B CA  1 
ATOM   3528 C C   . ASN B 1 158 ? -104.066 6.317  -74.189 1.00 32.96 ? 158  ASN B C   1 
ATOM   3529 O O   . ASN B 1 158 ? -103.784 5.151  -73.913 1.00 32.37 ? 158  ASN B O   1 
ATOM   3530 C CB  . ASN B 1 158 ? -101.839 7.444  -74.231 1.00 36.18 ? 158  ASN B CB  1 
ATOM   3531 C CG  . ASN B 1 158 ? -100.744 8.032  -75.096 1.00 38.64 ? 158  ASN B CG  1 
ATOM   3532 O OD1 . ASN B 1 158 ? -100.093 7.318  -75.855 1.00 40.62 ? 158  ASN B OD1 1 
ATOM   3533 N ND2 . ASN B 1 158 ? -100.551 9.344  -75.005 1.00 38.48 ? 158  ASN B ND2 1 
ATOM   3534 N N   . ILE B 1 159 ? -105.189 6.891  -73.780 1.00 32.62 ? 159  ILE B N   1 
ATOM   3535 C CA  . ILE B 1 159 ? -106.147 6.129  -72.987 1.00 32.78 ? 159  ILE B CA  1 
ATOM   3536 C C   . ILE B 1 159 ? -107.466 6.013  -73.734 1.00 32.48 ? 159  ILE B C   1 
ATOM   3537 O O   . ILE B 1 159 ? -108.194 6.991  -73.878 1.00 32.18 ? 159  ILE B O   1 
ATOM   3538 C CB  . ILE B 1 159 ? -106.385 6.782  -71.610 1.00 32.28 ? 159  ILE B CB  1 
ATOM   3539 C CG1 . ILE B 1 159 ? -105.051 6.863  -70.854 1.00 31.84 ? 159  ILE B CG1 1 
ATOM   3540 C CG2 . ILE B 1 159 ? -107.426 5.973  -70.824 1.00 28.52 ? 159  ILE B CG2 1 
ATOM   3541 C CD1 . ILE B 1 159 ? -105.086 7.680  -69.582 1.00 31.39 ? 159  ILE B CD1 1 
ATOM   3542 N N   . SER B 1 160 ? -107.748 4.805  -74.215 1.00 33.55 ? 160  SER B N   1 
ATOM   3543 C CA  . SER B 1 160 ? -108.962 4.501  -74.969 1.00 33.37 ? 160  SER B CA  1 
ATOM   3544 C C   . SER B 1 160 ? -110.232 4.934  -74.256 1.00 32.77 ? 160  SER B C   1 
ATOM   3545 O O   . SER B 1 160 ? -111.154 5.464  -74.873 1.00 31.71 ? 160  SER B O   1 
ATOM   3546 C CB  . SER B 1 160 ? -109.049 2.997  -75.228 1.00 34.23 ? 160  SER B CB  1 
ATOM   3547 O OG  . SER B 1 160 ? -107.846 2.506  -75.781 1.00 38.85 ? 160  SER B OG  1 
ATOM   3548 N N   . GLU B 1 161 ? -110.272 4.709  -72.950 1.00 31.89 ? 161  GLU B N   1 
ATOM   3549 C CA  . GLU B 1 161 ? -111.447 5.045  -72.156 1.00 32.73 ? 161  GLU B CA  1 
ATOM   3550 C C   . GLU B 1 161 ? -111.478 6.464  -71.587 1.00 32.48 ? 161  GLU B C   1 
ATOM   3551 O O   . GLU B 1 161 ? -112.251 6.732  -70.667 1.00 32.30 ? 161  GLU B O   1 
ATOM   3552 C CB  . GLU B 1 161 ? -111.574 4.046  -70.998 1.00 33.30 ? 161  GLU B CB  1 
ATOM   3553 C CG  . GLU B 1 161 ? -111.475 2.580  -71.417 1.00 35.76 ? 161  GLU B CG  1 
ATOM   3554 C CD  . GLU B 1 161 ? -110.043 2.062  -71.454 1.00 38.59 ? 161  GLU B CD  1 
ATOM   3555 O OE1 . GLU B 1 161 ? -109.130 2.830  -71.830 1.00 41.82 ? 161  GLU B OE1 1 
ATOM   3556 O OE2 . GLU B 1 161 ? -109.832 0.876  -71.117 1.00 40.62 ? 161  GLU B OE2 1 
ATOM   3557 N N   . TRP B 1 162 ? -110.673 7.379  -72.123 1.00 31.07 ? 162  TRP B N   1 
ATOM   3558 C CA  . TRP B 1 162 ? -110.651 8.731  -71.558 1.00 32.14 ? 162  TRP B CA  1 
ATOM   3559 C C   . TRP B 1 162 ? -112.005 9.402  -71.402 1.00 34.05 ? 162  TRP B C   1 
ATOM   3560 O O   . TRP B 1 162 ? -112.195 10.210 -70.487 1.00 31.83 ? 162  TRP B O   1 
ATOM   3561 C CB  . TRP B 1 162 ? -109.718 9.674  -72.338 1.00 28.56 ? 162  TRP B CB  1 
ATOM   3562 C CG  . TRP B 1 162 ? -110.133 10.069 -73.730 1.00 27.97 ? 162  TRP B CG  1 
ATOM   3563 C CD1 . TRP B 1 162 ? -109.717 9.493  -74.896 1.00 27.09 ? 162  TRP B CD1 1 
ATOM   3564 C CD2 . TRP B 1 162 ? -110.959 11.187 -74.111 1.00 26.92 ? 162  TRP B CD2 1 
ATOM   3565 N NE1 . TRP B 1 162 ? -110.214 10.187 -75.972 1.00 29.29 ? 162  TRP B NE1 1 
ATOM   3566 C CE2 . TRP B 1 162 ? -110.973 11.233 -75.522 1.00 28.14 ? 162  TRP B CE2 1 
ATOM   3567 C CE3 . TRP B 1 162 ? -111.668 12.163 -73.396 1.00 28.08 ? 162  TRP B CE3 1 
ATOM   3568 C CZ2 . TRP B 1 162 ? -111.685 12.213 -76.239 1.00 27.83 ? 162  TRP B CZ2 1 
ATOM   3569 C CZ3 . TRP B 1 162 ? -112.374 13.139 -74.108 1.00 25.70 ? 162  TRP B CZ3 1 
ATOM   3570 C CH2 . TRP B 1 162 ? -112.369 13.158 -75.516 1.00 24.56 ? 162  TRP B CH2 1 
ATOM   3571 N N   . ARG B 1 163 ? -112.950 9.072  -72.278 1.00 34.06 ? 163  ARG B N   1 
ATOM   3572 C CA  . ARG B 1 163 ? -114.265 9.692  -72.203 1.00 33.40 ? 163  ARG B CA  1 
ATOM   3573 C C   . ARG B 1 163 ? -115.084 9.191  -71.025 1.00 33.16 ? 163  ARG B C   1 
ATOM   3574 O O   . ARG B 1 163 ? -116.137 9.739  -70.730 1.00 33.48 ? 163  ARG B O   1 
ATOM   3575 C CB  . ARG B 1 163 ? -115.035 9.474  -73.505 1.00 34.23 ? 163  ARG B CB  1 
ATOM   3576 C CG  . ARG B 1 163 ? -114.401 10.126 -74.719 1.00 35.33 ? 163  ARG B CG  1 
ATOM   3577 C CD  . ARG B 1 163 ? -115.354 10.099 -75.909 1.00 36.05 ? 163  ARG B CD  1 
ATOM   3578 N NE  . ARG B 1 163 ? -114.716 10.583 -77.129 1.00 38.74 ? 163  ARG B NE  1 
ATOM   3579 C CZ  . ARG B 1 163 ? -113.693 9.979  -77.732 1.00 39.36 ? 163  ARG B CZ  1 
ATOM   3580 N NH1 . ARG B 1 163 ? -113.186 8.857  -77.231 1.00 38.03 ? 163  ARG B NH1 1 
ATOM   3581 N NH2 . ARG B 1 163 ? -113.171 10.498 -78.836 1.00 37.38 ? 163  ARG B NH2 1 
ATOM   3582 N N   . ASN B 1 164 ? -114.595 8.155  -70.352 1.00 33.43 ? 164  ASN B N   1 
ATOM   3583 C CA  . ASN B 1 164 ? -115.284 7.590  -69.193 1.00 35.18 ? 164  ASN B CA  1 
ATOM   3584 C C   . ASN B 1 164 ? -114.321 7.347  -68.027 1.00 34.94 ? 164  ASN B C   1 
ATOM   3585 O O   . ASN B 1 164 ? -114.544 6.466  -67.198 1.00 35.93 ? 164  ASN B O   1 
ATOM   3586 C CB  . ASN B 1 164 ? -115.963 6.269  -69.577 1.00 36.25 ? 164  ASN B CB  1 
ATOM   3587 C CG  . ASN B 1 164 ? -117.176 6.474  -70.463 1.00 36.37 ? 164  ASN B CG  1 
ATOM   3588 O OD1 . ASN B 1 164 ? -118.306 6.564  -69.978 1.00 36.70 ? 164  ASN B OD1 1 
ATOM   3589 N ND2 . ASN B 1 164 ? -116.946 6.567  -71.766 1.00 33.98 ? 164  ASN B ND2 1 
ATOM   3590 N N   . CYS B 1 165 ? -113.251 8.131  -67.967 1.00 33.62 ? 165  CYS B N   1 
ATOM   3591 C CA  . CYS B 1 165 ? -112.267 7.978  -66.908 1.00 31.26 ? 165  CYS B CA  1 
ATOM   3592 C C   . CYS B 1 165 ? -112.551 8.969  -65.791 1.00 30.70 ? 165  CYS B C   1 
ATOM   3593 O O   . CYS B 1 165 ? -113.419 9.829  -65.921 1.00 31.44 ? 165  CYS B O   1 
ATOM   3594 C CB  . CYS B 1 165 ? -110.860 8.234  -67.454 1.00 28.12 ? 165  CYS B CB  1 
ATOM   3595 S SG  . CYS B 1 165 ? -110.467 9.993  -67.725 1.00 26.88 ? 165  CYS B SG  1 
ATOM   3596 N N   . THR B 1 166 ? -111.816 8.836  -64.692 1.00 30.02 ? 166  THR B N   1 
ATOM   3597 C CA  . THR B 1 166 ? -111.951 9.740  -63.557 1.00 28.48 ? 166  THR B CA  1 
ATOM   3598 C C   . THR B 1 166 ? -110.583 10.330 -63.245 1.00 28.37 ? 166  THR B C   1 
ATOM   3599 O O   . THR B 1 166 ? -109.605 9.599  -63.090 1.00 28.29 ? 166  THR B O   1 
ATOM   3600 C CB  . THR B 1 166 ? -112.460 9.018  -62.286 1.00 29.05 ? 166  THR B CB  1 
ATOM   3601 O OG1 . THR B 1 166 ? -113.783 8.519  -62.515 1.00 29.08 ? 166  THR B OG1 1 
ATOM   3602 C CG2 . THR B 1 166 ? -112.495 9.988  -61.094 1.00 27.20 ? 166  THR B CG2 1 
ATOM   3603 N N   . ILE B 1 167 ? -110.514 11.655 -63.172 1.00 29.28 ? 167  ILE B N   1 
ATOM   3604 C CA  . ILE B 1 167 ? -109.268 12.339 -62.848 1.00 26.70 ? 167  ILE B CA  1 
ATOM   3605 C C   . ILE B 1 167 ? -109.249 12.451 -61.319 1.00 28.11 ? 167  ILE B C   1 
ATOM   3606 O O   . ILE B 1 167 ? -110.133 13.077 -60.726 1.00 27.56 ? 167  ILE B O   1 
ATOM   3607 C CB  . ILE B 1 167 ? -109.217 13.753 -63.478 1.00 28.22 ? 167  ILE B CB  1 
ATOM   3608 C CG1 . ILE B 1 167 ? -109.518 13.677 -64.987 1.00 26.17 ? 167  ILE B CG1 1 
ATOM   3609 C CG2 . ILE B 1 167 ? -107.862 14.394 -63.209 1.00 24.02 ? 167  ILE B CG2 1 
ATOM   3610 C CD1 . ILE B 1 167 ? -108.735 12.606 -65.749 1.00 24.62 ? 167  ILE B CD1 1 
ATOM   3611 N N   . VAL B 1 168 ? -108.245 11.835 -60.696 1.00 25.14 ? 168  VAL B N   1 
ATOM   3612 C CA  . VAL B 1 168 ? -108.123 11.812 -59.244 1.00 24.09 ? 168  VAL B CA  1 
ATOM   3613 C C   . VAL B 1 168 ? -106.964 12.644 -58.699 1.00 25.06 ? 168  VAL B C   1 
ATOM   3614 O O   . VAL B 1 168 ? -105.850 12.607 -59.223 1.00 24.55 ? 168  VAL B O   1 
ATOM   3615 C CB  . VAL B 1 168 ? -107.924 10.367 -58.730 1.00 23.06 ? 168  VAL B CB  1 
ATOM   3616 C CG1 . VAL B 1 168 ? -108.144 10.317 -57.232 1.00 23.94 ? 168  VAL B CG1 1 
ATOM   3617 C CG2 . VAL B 1 168 ? -108.867 9.407  -59.447 1.00 23.82 ? 168  VAL B CG2 1 
ATOM   3618 N N   . SER B 1 169 ? -107.238 13.397 -57.641 1.00 26.27 ? 169  SER B N   1 
ATOM   3619 C CA  . SER B 1 169 ? -106.208 14.204 -56.993 1.00 27.10 ? 169  SER B CA  1 
ATOM   3620 C C   . SER B 1 169 ? -105.689 13.369 -55.826 1.00 26.01 ? 169  SER B C   1 
ATOM   3621 O O   . SER B 1 169 ? -106.481 12.799 -55.075 1.00 25.64 ? 169  SER B O   1 
ATOM   3622 C CB  . SER B 1 169 ? -106.800 15.507 -56.454 1.00 27.87 ? 169  SER B CB  1 
ATOM   3623 O OG  . SER B 1 169 ? -105.801 16.284 -55.808 1.00 31.63 ? 169  SER B OG  1 
ATOM   3624 N N   . PRO B 1 170 ? -104.359 13.275 -55.666 1.00 25.56 ? 170  PRO B N   1 
ATOM   3625 C CA  . PRO B 1 170 ? -103.805 12.486 -54.561 1.00 26.58 ? 170  PRO B CA  1 
ATOM   3626 C C   . PRO B 1 170 ? -103.951 13.146 -53.196 1.00 28.49 ? 170  PRO B C   1 
ATOM   3627 O O   . PRO B 1 170 ? -103.686 12.523 -52.174 1.00 28.58 ? 170  PRO B O   1 
ATOM   3628 C CB  . PRO B 1 170 ? -102.347 12.276 -54.975 1.00 26.33 ? 170  PRO B CB  1 
ATOM   3629 C CG  . PRO B 1 170 ? -102.042 13.474 -55.788 1.00 26.30 ? 170  PRO B CG  1 
ATOM   3630 C CD  . PRO B 1 170 ? -103.300 13.683 -56.606 1.00 26.97 ? 170  PRO B CD  1 
ATOM   3631 N N   . ASP B 1 171 ? -104.364 14.409 -53.182 1.00 30.85 ? 171  ASP B N   1 
ATOM   3632 C CA  . ASP B 1 171 ? -104.583 15.126 -51.928 1.00 33.25 ? 171  ASP B CA  1 
ATOM   3633 C C   . ASP B 1 171 ? -105.691 16.151 -52.093 1.00 35.37 ? 171  ASP B C   1 
ATOM   3634 O O   . ASP B 1 171 ? -106.178 16.381 -53.204 1.00 34.48 ? 171  ASP B O   1 
ATOM   3635 C CB  . ASP B 1 171 ? -103.309 15.815 -51.427 1.00 33.90 ? 171  ASP B CB  1 
ATOM   3636 C CG  . ASP B 1 171 ? -102.668 16.709 -52.471 1.00 36.54 ? 171  ASP B CG  1 
ATOM   3637 O OD1 . ASP B 1 171 ? -103.391 17.458 -53.165 1.00 38.14 ? 171  ASP B OD1 1 
ATOM   3638 O OD2 . ASP B 1 171 ? -101.428 16.669 -52.586 1.00 38.17 ? 171  ASP B OD2 1 
ATOM   3639 N N   . ALA B 1 172 ? -106.084 16.760 -50.978 1.00 36.52 ? 172  ALA B N   1 
ATOM   3640 C CA  . ALA B 1 172 ? -107.152 17.751 -50.962 1.00 38.02 ? 172  ALA B CA  1 
ATOM   3641 C C   . ALA B 1 172 ? -106.761 19.007 -51.705 1.00 38.30 ? 172  ALA B C   1 
ATOM   3642 O O   . ALA B 1 172 ? -107.581 19.610 -52.389 1.00 38.18 ? 172  ALA B O   1 
ATOM   3643 C CB  . ALA B 1 172 ? -107.518 18.102 -49.518 1.00 41.58 ? 172  ALA B CB  1 
ATOM   3644 N N   . GLY B 1 173 ? -105.497 19.391 -51.567 1.00 39.73 ? 173  GLY B N   1 
ATOM   3645 C CA  . GLY B 1 173 ? -105.009 20.591 -52.219 1.00 39.33 ? 173  GLY B CA  1 
ATOM   3646 C C   . GLY B 1 173 ? -105.059 20.607 -53.737 1.00 38.97 ? 173  GLY B C   1 
ATOM   3647 O O   . GLY B 1 173 ? -104.972 21.676 -54.348 1.00 38.56 ? 173  GLY B O   1 
ATOM   3648 N N   . GLY B 1 174 ? -105.200 19.441 -54.355 1.00 36.51 ? 174  GLY B N   1 
ATOM   3649 C CA  . GLY B 1 174 ? -105.235 19.398 -55.804 1.00 35.14 ? 174  GLY B CA  1 
ATOM   3650 C C   . GLY B 1 174 ? -106.616 19.344 -56.424 1.00 34.54 ? 174  GLY B C   1 
ATOM   3651 O O   . GLY B 1 174 ? -106.745 19.145 -57.629 1.00 35.61 ? 174  GLY B O   1 
ATOM   3652 N N   . ALA B 1 175 ? -107.651 19.524 -55.613 1.00 34.76 ? 175  ALA B N   1 
ATOM   3653 C CA  . ALA B 1 175 ? -109.017 19.469 -56.116 1.00 36.65 ? 175  ALA B CA  1 
ATOM   3654 C C   . ALA B 1 175 ? -109.232 20.366 -57.326 1.00 37.80 ? 175  ALA B C   1 
ATOM   3655 O O   . ALA B 1 175 ? -109.751 19.930 -58.352 1.00 38.21 ? 175  ALA B O   1 
ATOM   3656 C CB  . ALA B 1 175 ? -109.997 19.850 -55.017 1.00 36.15 ? 175  ALA B CB  1 
ATOM   3657 N N   . LYS B 1 176 ? -108.825 21.622 -57.200 1.00 39.08 ? 176  LYS B N   1 
ATOM   3658 C CA  . LYS B 1 176 ? -108.993 22.589 -58.273 1.00 40.49 ? 176  LYS B CA  1 
ATOM   3659 C C   . LYS B 1 176 ? -108.365 22.118 -59.580 1.00 40.29 ? 176  LYS B C   1 
ATOM   3660 O O   . LYS B 1 176 ? -108.985 22.200 -60.636 1.00 40.39 ? 176  LYS B O   1 
ATOM   3661 C CB  . LYS B 1 176 ? -108.391 23.930 -57.852 1.00 42.40 ? 176  LYS B CB  1 
ATOM   3662 C CG  . LYS B 1 176 ? -109.183 25.135 -58.328 1.00 47.09 ? 176  LYS B CG  1 
ATOM   3663 C CD  . LYS B 1 176 ? -108.633 26.421 -57.727 1.00 50.70 ? 176  LYS B CD  1 
ATOM   3664 C CE  . LYS B 1 176 ? -109.617 27.574 -57.883 1.00 53.57 ? 176  LYS B CE  1 
ATOM   3665 N NZ  . LYS B 1 176 ? -110.908 27.307 -57.170 1.00 54.06 ? 176  LYS B NZ  1 
ATOM   3666 N N   . ARG B 1 177 ? -107.137 21.612 -59.506 1.00 40.61 ? 177  ARG B N   1 
ATOM   3667 C CA  . ARG B 1 177 ? -106.435 21.142 -60.695 1.00 40.85 ? 177  ARG B CA  1 
ATOM   3668 C C   . ARG B 1 177 ? -107.138 19.967 -61.380 1.00 40.44 ? 177  ARG B C   1 
ATOM   3669 O O   . ARG B 1 177 ? -107.203 19.907 -62.608 1.00 41.71 ? 177  ARG B O   1 
ATOM   3670 C CB  . ARG B 1 177 ? -105.014 20.727 -60.330 1.00 44.05 ? 177  ARG B CB  1 
ATOM   3671 C CG  . ARG B 1 177 ? -104.133 20.417 -61.515 1.00 46.04 ? 177  ARG B CG  1 
ATOM   3672 C CD  . ARG B 1 177 ? -103.090 19.375 -61.146 1.00 49.58 ? 177  ARG B CD  1 
ATOM   3673 N NE  . ARG B 1 177 ? -102.453 19.661 -59.866 1.00 50.53 ? 177  ARG B NE  1 
ATOM   3674 C CZ  . ARG B 1 177 ? -101.680 20.714 -59.630 1.00 51.74 ? 177  ARG B CZ  1 
ATOM   3675 N NH1 . ARG B 1 177 ? -101.440 21.594 -60.597 1.00 51.09 ? 177  ARG B NH1 1 
ATOM   3676 N NH2 . ARG B 1 177 ? -101.147 20.886 -58.425 1.00 50.10 ? 177  ARG B NH2 1 
ATOM   3677 N N   . VAL B 1 178 ? -107.658 19.026 -60.601 1.00 38.04 ? 178  VAL B N   1 
ATOM   3678 C CA  . VAL B 1 178 ? -108.331 17.886 -61.210 1.00 35.35 ? 178  VAL B CA  1 
ATOM   3679 C C   . VAL B 1 178 ? -109.729 18.242 -61.709 1.00 35.08 ? 178  VAL B C   1 
ATOM   3680 O O   . VAL B 1 178 ? -110.126 17.809 -62.784 1.00 33.87 ? 178  VAL B O   1 
ATOM   3681 C CB  . VAL B 1 178 ? -108.390 16.674 -60.248 1.00 33.37 ? 178  VAL B CB  1 
ATOM   3682 C CG1 . VAL B 1 178 ? -106.972 16.250 -59.896 1.00 31.51 ? 178  VAL B CG1 1 
ATOM   3683 C CG2 . VAL B 1 178 ? -109.182 17.008 -58.995 1.00 33.31 ? 178  VAL B CG2 1 
ATOM   3684 N N   . THR B 1 179 ? -110.476 19.036 -60.948 1.00 34.55 ? 179  THR B N   1 
ATOM   3685 C CA  . THR B 1 179 ? -111.811 19.418 -61.406 1.00 36.27 ? 179  THR B CA  1 
ATOM   3686 C C   . THR B 1 179 ? -111.675 20.155 -62.738 1.00 37.37 ? 179  THR B C   1 
ATOM   3687 O O   . THR B 1 179 ? -112.532 20.050 -63.615 1.00 37.25 ? 179  THR B O   1 
ATOM   3688 C CB  . THR B 1 179 ? -112.536 20.344 -60.397 1.00 35.45 ? 179  THR B CB  1 
ATOM   3689 O OG1 . THR B 1 179 ? -111.699 21.462 -60.073 1.00 35.92 ? 179  THR B OG1 1 
ATOM   3690 C CG2 . THR B 1 179 ? -112.887 19.583 -59.130 1.00 33.32 ? 179  THR B CG2 1 
ATOM   3691 N N   . SER B 1 180 ? -110.576 20.886 -62.883 1.00 37.95 ? 180  SER B N   1 
ATOM   3692 C CA  . SER B 1 180 ? -110.308 21.656 -64.090 1.00 38.74 ? 180  SER B CA  1 
ATOM   3693 C C   . SER B 1 180 ? -110.056 20.778 -65.310 1.00 38.07 ? 180  SER B C   1 
ATOM   3694 O O   . SER B 1 180 ? -110.494 21.094 -66.416 1.00 37.62 ? 180  SER B O   1 
ATOM   3695 C CB  . SER B 1 180 ? -109.107 22.572 -63.862 1.00 38.80 ? 180  SER B CB  1 
ATOM   3696 O OG  . SER B 1 180 ? -108.658 23.118 -65.087 1.00 43.26 ? 180  SER B OG  1 
ATOM   3697 N N   . ILE B 1 181 ? -109.335 19.684 -65.109 1.00 36.95 ? 181  ILE B N   1 
ATOM   3698 C CA  . ILE B 1 181 ? -109.036 18.768 -66.193 1.00 35.80 ? 181  ILE B CA  1 
ATOM   3699 C C   . ILE B 1 181 ? -110.262 17.912 -66.461 1.00 36.24 ? 181  ILE B C   1 
ATOM   3700 O O   . ILE B 1 181 ? -110.560 17.576 -67.606 1.00 36.85 ? 181  ILE B O   1 
ATOM   3701 C CB  . ILE B 1 181 ? -107.828 17.875 -65.830 1.00 37.17 ? 181  ILE B CB  1 
ATOM   3702 C CG1 . ILE B 1 181 ? -106.559 18.727 -65.790 1.00 37.57 ? 181  ILE B CG1 1 
ATOM   3703 C CG2 . ILE B 1 181 ? -107.676 16.751 -66.834 1.00 34.16 ? 181  ILE B CG2 1 
ATOM   3704 C CD1 . ILE B 1 181 ? -105.359 18.012 -65.200 1.00 39.72 ? 181  ILE B CD1 1 
ATOM   3705 N N   . ALA B 1 182 ? -110.986 17.573 -65.400 1.00 37.12 ? 182  ALA B N   1 
ATOM   3706 C CA  . ALA B 1 182 ? -112.185 16.753 -65.533 1.00 36.55 ? 182  ALA B CA  1 
ATOM   3707 C C   . ALA B 1 182 ? -113.238 17.491 -66.352 1.00 36.81 ? 182  ALA B C   1 
ATOM   3708 O O   . ALA B 1 182 ? -113.911 16.892 -67.193 1.00 37.08 ? 182  ALA B O   1 
ATOM   3709 C CB  . ALA B 1 182 ? -112.738 16.392 -64.154 1.00 32.79 ? 182  ALA B CB  1 
ATOM   3710 N N   . ASP B 1 183 ? -113.375 18.790 -66.113 1.00 37.35 ? 183  ASP B N   1 
ATOM   3711 C CA  . ASP B 1 183 ? -114.348 19.591 -66.848 1.00 39.09 ? 183  ASP B CA  1 
ATOM   3712 C C   . ASP B 1 183 ? -113.987 19.748 -68.320 1.00 38.55 ? 183  ASP B C   1 
ATOM   3713 O O   . ASP B 1 183 ? -114.860 19.641 -69.179 1.00 38.12 ? 183  ASP B O   1 
ATOM   3714 C CB  . ASP B 1 183 ? -114.517 20.964 -66.190 1.00 40.25 ? 183  ASP B CB  1 
ATOM   3715 C CG  . ASP B 1 183 ? -115.188 20.872 -64.836 1.00 42.44 ? 183  ASP B CG  1 
ATOM   3716 O OD1 . ASP B 1 183 ? -115.698 19.783 -64.505 1.00 44.98 ? 183  ASP B OD1 1 
ATOM   3717 O OD2 . ASP B 1 183 ? -115.215 21.881 -64.103 1.00 45.17 ? 183  ASP B OD2 1 
ATOM   3718 N N   . ARG B 1 184 ? -112.714 19.995 -68.624 1.00 39.08 ? 184  ARG B N   1 
ATOM   3719 C CA  . ARG B 1 184 ? -112.305 20.129 -70.024 1.00 39.48 ? 184  ARG B CA  1 
ATOM   3720 C C   . ARG B 1 184 ? -112.568 18.828 -70.782 1.00 38.22 ? 184  ARG B C   1 
ATOM   3721 O O   . ARG B 1 184 ? -112.987 18.849 -71.934 1.00 37.34 ? 184  ARG B O   1 
ATOM   3722 C CB  . ARG B 1 184 ? -110.818 20.486 -70.147 1.00 43.75 ? 184  ARG B CB  1 
ATOM   3723 C CG  . ARG B 1 184 ? -110.485 21.950 -69.867 1.00 51.69 ? 184  ARG B CG  1 
ATOM   3724 C CD  . ARG B 1 184 ? -109.060 22.283 -70.300 1.00 57.97 ? 184  ARG B CD  1 
ATOM   3725 N NE  . ARG B 1 184 ? -108.602 23.574 -69.787 1.00 63.89 ? 184  ARG B NE  1 
ATOM   3726 C CZ  . ARG B 1 184 ? -107.370 24.062 -69.949 1.00 66.68 ? 184  ARG B CZ  1 
ATOM   3727 N NH1 . ARG B 1 184 ? -106.451 23.370 -70.620 1.00 66.02 ? 184  ARG B NH1 1 
ATOM   3728 N NH2 . ARG B 1 184 ? -107.051 25.241 -69.425 1.00 67.95 ? 184  ARG B NH2 1 
ATOM   3729 N N   . LEU B 1 185 ? -112.321 17.697 -70.127 1.00 36.72 ? 185  LEU B N   1 
ATOM   3730 C CA  . LEU B 1 185 ? -112.528 16.391 -70.738 1.00 36.39 ? 185  LEU B CA  1 
ATOM   3731 C C   . LEU B 1 185 ? -113.985 15.945 -70.634 1.00 37.23 ? 185  LEU B C   1 
ATOM   3732 O O   . LEU B 1 185 ? -114.446 15.110 -71.409 1.00 39.04 ? 185  LEU B O   1 
ATOM   3733 C CB  . LEU B 1 185 ? -111.631 15.345 -70.063 1.00 33.72 ? 185  LEU B CB  1 
ATOM   3734 C CG  . LEU B 1 185 ? -110.129 15.474 -70.340 1.00 35.46 ? 185  LEU B CG  1 
ATOM   3735 C CD1 . LEU B 1 185 ? -109.347 14.355 -69.631 1.00 31.51 ? 185  LEU B CD1 1 
ATOM   3736 C CD2 . LEU B 1 185 ? -109.904 15.407 -71.847 1.00 32.15 ? 185  LEU B CD2 1 
ATOM   3737 N N   . ASN B 1 186 ? -114.699 16.509 -69.668 1.00 37.93 ? 186  ASN B N   1 
ATOM   3738 C CA  . ASN B 1 186 ? -116.101 16.180 -69.420 1.00 37.47 ? 186  ASN B CA  1 
ATOM   3739 C C   . ASN B 1 186 ? -116.259 14.787 -68.808 1.00 36.11 ? 186  ASN B C   1 
ATOM   3740 O O   . ASN B 1 186 ? -117.021 13.970 -69.311 1.00 38.80 ? 186  ASN B O   1 
ATOM   3741 C CB  . ASN B 1 186 ? -116.919 16.269 -70.712 1.00 39.08 ? 186  ASN B CB  1 
ATOM   3742 C CG  . ASN B 1 186 ? -118.412 16.402 -70.453 1.00 41.69 ? 186  ASN B CG  1 
ATOM   3743 O OD1 . ASN B 1 186 ? -119.227 16.048 -71.301 1.00 45.41 ? 186  ASN B OD1 1 
ATOM   3744 N ND2 . ASN B 1 186 ? -118.775 16.922 -69.286 1.00 40.53 ? 186  ASN B ND2 1 
ATOM   3745 N N   . VAL B 1 187 ? -115.545 14.529 -67.714 1.00 35.27 ? 187  VAL B N   1 
ATOM   3746 C CA  . VAL B 1 187 ? -115.602 13.240 -67.020 1.00 33.25 ? 187  VAL B CA  1 
ATOM   3747 C C   . VAL B 1 187 ? -115.665 13.460 -65.503 1.00 32.58 ? 187  VAL B C   1 
ATOM   3748 O O   . VAL B 1 187 ? -115.688 14.600 -65.039 1.00 31.90 ? 187  VAL B O   1 
ATOM   3749 C CB  . VAL B 1 187 ? -114.361 12.389 -67.350 1.00 32.06 ? 187  VAL B CB  1 
ATOM   3750 C CG1 . VAL B 1 187 ? -114.261 12.187 -68.845 1.00 32.91 ? 187  VAL B CG1 1 
ATOM   3751 C CG2 . VAL B 1 187 ? -113.097 13.078 -66.829 1.00 32.09 ? 187  VAL B CG2 1 
ATOM   3752 N N   . ASP B 1 188 ? -115.681 12.382 -64.729 1.00 31.08 ? 188  ASP B N   1 
ATOM   3753 C CA  . ASP B 1 188 ? -115.750 12.535 -63.289 1.00 31.93 ? 188  ASP B CA  1 
ATOM   3754 C C   . ASP B 1 188 ? -114.394 12.867 -62.664 1.00 30.47 ? 188  ASP B C   1 
ATOM   3755 O O   . ASP B 1 188 ? -113.351 12.796 -63.311 1.00 30.74 ? 188  ASP B O   1 
ATOM   3756 C CB  . ASP B 1 188 ? -116.339 11.263 -62.646 1.00 33.51 ? 188  ASP B CB  1 
ATOM   3757 C CG  . ASP B 1 188 ? -117.645 10.836 -63.291 1.00 35.53 ? 188  ASP B CG  1 
ATOM   3758 O OD1 . ASP B 1 188 ? -118.379 11.723 -63.775 1.00 35.75 ? 188  ASP B OD1 1 
ATOM   3759 O OD2 . ASP B 1 188 ? -117.940 9.626  -63.313 1.00 39.67 ? 188  ASP B OD2 1 
ATOM   3760 N N   . PHE B 1 189 ? -114.425 13.251 -61.399 1.00 30.52 ? 189  PHE B N   1 
ATOM   3761 C CA  . PHE B 1 189 ? -113.212 13.551 -60.671 1.00 30.94 ? 189  PHE B CA  1 
ATOM   3762 C C   . PHE B 1 189 ? -113.407 12.951 -59.295 1.00 31.02 ? 189  PHE B C   1 
ATOM   3763 O O   . PHE B 1 189 ? -114.530 12.621 -58.892 1.00 30.93 ? 189  PHE B O   1 
ATOM   3764 C CB  . PHE B 1 189 ? -112.972 15.061 -60.574 1.00 31.86 ? 189  PHE B CB  1 
ATOM   3765 C CG  . PHE B 1 189 ? -113.804 15.734 -59.538 1.00 32.85 ? 189  PHE B CG  1 
ATOM   3766 C CD1 . PHE B 1 189 ? -113.445 15.668 -58.200 1.00 32.88 ? 189  PHE B CD1 1 
ATOM   3767 C CD2 . PHE B 1 189 ? -114.973 16.390 -59.892 1.00 33.30 ? 189  PHE B CD2 1 
ATOM   3768 C CE1 . PHE B 1 189 ? -114.245 16.235 -57.222 1.00 35.05 ? 189  PHE B CE1 1 
ATOM   3769 C CE2 . PHE B 1 189 ? -115.787 16.964 -58.919 1.00 33.87 ? 189  PHE B CE2 1 
ATOM   3770 C CZ  . PHE B 1 189 ? -115.420 16.885 -57.579 1.00 33.61 ? 189  PHE B CZ  1 
ATOM   3771 N N   . ALA B 1 190 ? -112.308 12.829 -58.569 1.00 31.08 ? 190  ALA B N   1 
ATOM   3772 C CA  . ALA B 1 190 ? -112.339 12.242 -57.249 1.00 31.53 ? 190  ALA B CA  1 
ATOM   3773 C C   . ALA B 1 190 ? -111.162 12.795 -56.472 1.00 31.08 ? 190  ALA B C   1 
ATOM   3774 O O   . ALA B 1 190 ? -110.217 13.287 -57.076 1.00 31.65 ? 190  ALA B O   1 
ATOM   3775 C CB  . ALA B 1 190 ? -112.242 10.745 -57.370 1.00 30.01 ? 190  ALA B CB  1 
ATOM   3776 N N   . LEU B 1 191 ? -111.212 12.735 -55.145 1.00 30.30 ? 191  LEU B N   1 
ATOM   3777 C CA  . LEU B 1 191 ? -110.108 13.239 -54.336 1.00 31.42 ? 191  LEU B CA  1 
ATOM   3778 C C   . LEU B 1 191 ? -109.715 12.277 -53.235 1.00 32.27 ? 191  LEU B C   1 
ATOM   3779 O O   . LEU B 1 191 ? -110.566 11.645 -52.611 1.00 32.21 ? 191  LEU B O   1 
ATOM   3780 C CB  . LEU B 1 191 ? -110.462 14.571 -53.675 1.00 34.51 ? 191  LEU B CB  1 
ATOM   3781 C CG  . LEU B 1 191 ? -110.945 15.742 -54.527 1.00 37.43 ? 191  LEU B CG  1 
ATOM   3782 C CD1 . LEU B 1 191 ? -111.300 16.890 -53.595 1.00 40.25 ? 191  LEU B CD1 1 
ATOM   3783 C CD2 . LEU B 1 191 ? -109.869 16.171 -55.526 1.00 38.74 ? 191  LEU B CD2 1 
ATOM   3784 N N   . ILE B 1 192 ? -108.417 12.183 -52.988 1.00 33.05 ? 192  ILE B N   1 
ATOM   3785 C CA  . ILE B 1 192 ? -107.917 11.339 -51.922 1.00 34.21 ? 192  ILE B CA  1 
ATOM   3786 C C   . ILE B 1 192 ? -107.365 12.247 -50.838 1.00 35.57 ? 192  ILE B C   1 
ATOM   3787 O O   . ILE B 1 192 ? -106.640 13.194 -51.128 1.00 36.20 ? 192  ILE B O   1 
ATOM   3788 C CB  . ILE B 1 192 ? -106.799 10.392 -52.410 1.00 34.70 ? 192  ILE B CB  1 
ATOM   3789 C CG1 . ILE B 1 192 ? -107.429 9.237  -53.194 1.00 35.63 ? 192  ILE B CG1 1 
ATOM   3790 C CG2 . ILE B 1 192 ? -105.967 9.880  -51.215 1.00 31.83 ? 192  ILE B CG2 1 
ATOM   3791 C CD1 . ILE B 1 192 ? -106.478 8.156  -53.569 1.00 35.22 ? 192  ILE B CD1 1 
ATOM   3792 N N   . HIS B 1 193 ? -107.739 11.970 -49.595 1.00 36.35 ? 193  HIS B N   1 
ATOM   3793 C CA  . HIS B 1 193 ? -107.255 12.737 -48.457 1.00 37.28 ? 193  HIS B CA  1 
ATOM   3794 C C   . HIS B 1 193 ? -106.603 11.792 -47.449 1.00 39.13 ? 193  HIS B C   1 
ATOM   3795 O O   . HIS B 1 193 ? -107.197 10.793 -47.033 1.00 36.95 ? 193  HIS B O   1 
ATOM   3796 C CB  . HIS B 1 193 ? -108.402 13.502 -47.786 1.00 37.75 ? 193  HIS B CB  1 
ATOM   3797 C CG  . HIS B 1 193 ? -108.035 14.091 -46.458 1.00 35.71 ? 193  HIS B CG  1 
ATOM   3798 N ND1 . HIS B 1 193 ? -106.891 14.836 -46.264 1.00 35.78 ? 193  HIS B ND1 1 
ATOM   3799 C CD2 . HIS B 1 193 ? -108.651 14.030 -45.254 1.00 35.09 ? 193  HIS B CD2 1 
ATOM   3800 C CE1 . HIS B 1 193 ? -106.817 15.206 -44.999 1.00 36.14 ? 193  HIS B CE1 1 
ATOM   3801 N NE2 . HIS B 1 193 ? -107.874 14.730 -44.363 1.00 35.05 ? 193  HIS B NE2 1 
ATOM   3802 N N   . LYS B 1 194 ? -105.374 12.114 -47.066 1.00 41.58 ? 194  LYS B N   1 
ATOM   3803 C CA  . LYS B 1 194 ? -104.628 11.310 -46.110 1.00 45.41 ? 194  LYS B CA  1 
ATOM   3804 C C   . LYS B 1 194 ? -104.871 11.893 -44.725 1.00 46.91 ? 194  LYS B C   1 
ATOM   3805 O O   . LYS B 1 194 ? -104.568 13.057 -44.476 1.00 47.12 ? 194  LYS B O   1 
ATOM   3806 C CB  . LYS B 1 194 ? -103.134 11.351 -46.455 1.00 47.28 ? 194  LYS B CB  1 
ATOM   3807 C CG  . LYS B 1 194 ? -102.273 10.291 -45.780 1.00 51.80 ? 194  LYS B CG  1 
ATOM   3808 C CD  . LYS B 1 194 ? -102.045 10.602 -44.311 1.00 56.12 ? 194  LYS B CD  1 
ATOM   3809 C CE  . LYS B 1 194 ? -101.133 9.573  -43.657 1.00 58.49 ? 194  LYS B CE  1 
ATOM   3810 N NZ  . LYS B 1 194 ? -100.877 9.894  -42.218 1.00 58.93 ? 194  LYS B NZ  1 
ATOM   3811 N N   . GLU B 1 195 ? -105.432 11.085 -43.833 1.00 49.63 ? 195  GLU B N   1 
ATOM   3812 C CA  . GLU B 1 195 ? -105.720 11.523 -42.469 1.00 52.73 ? 195  GLU B CA  1 
ATOM   3813 C C   . GLU B 1 195 ? -104.538 11.238 -41.543 1.00 52.54 ? 195  GLU B C   1 
ATOM   3814 O O   . GLU B 1 195 ? -103.443 11.773 -41.741 1.00 51.72 ? 195  GLU B O   1 
ATOM   3815 C CB  . GLU B 1 195 ? -106.980 10.823 -41.942 1.00 54.70 ? 195  GLU B CB  1 
ATOM   3816 C CG  . GLU B 1 195 ? -108.224 11.094 -42.781 1.00 58.44 ? 195  GLU B CG  1 
ATOM   3817 C CD  . GLU B 1 195 ? -109.467 10.389 -42.258 1.00 62.08 ? 195  GLU B CD  1 
ATOM   3818 O OE1 . GLU B 1 195 ? -109.432 9.151  -42.084 1.00 62.34 ? 195  GLU B OE1 1 
ATOM   3819 O OE2 . GLU B 1 195 ? -110.487 11.075 -42.027 1.00 64.37 ? 195  GLU B OE2 1 
ATOM   3820 N N   . ASP B 1 203 ? -103.151 8.107  -40.233 1.00 74.33 ? 203  ASP B N   1 
ATOM   3821 C CA  . ASP B 1 203 ? -102.386 7.538  -41.337 1.00 72.90 ? 203  ASP B CA  1 
ATOM   3822 C C   . ASP B 1 203 ? -103.275 6.614  -42.165 1.00 70.51 ? 203  ASP B C   1 
ATOM   3823 O O   . ASP B 1 203 ? -102.981 5.429  -42.322 1.00 72.12 ? 203  ASP B O   1 
ATOM   3824 C CB  . ASP B 1 203 ? -101.181 6.760  -40.794 1.00 75.44 ? 203  ASP B CB  1 
ATOM   3825 C CG  . ASP B 1 203 ? -100.179 6.402  -41.880 1.00 76.94 ? 203  ASP B CG  1 
ATOM   3826 O OD1 . ASP B 1 203 ? -100.553 5.682  -42.830 1.00 77.10 ? 203  ASP B OD1 1 
ATOM   3827 O OD2 . ASP B 1 203 ? -99.015  6.844  -41.783 1.00 77.37 ? 203  ASP B OD2 1 
ATOM   3828 N N   . ARG B 1 204 ? -104.362 7.164  -42.695 1.00 66.00 ? 204  ARG B N   1 
ATOM   3829 C CA  . ARG B 1 204 ? -105.298 6.383  -43.493 1.00 61.26 ? 204  ARG B CA  1 
ATOM   3830 C C   . ARG B 1 204 ? -105.865 7.233  -44.626 1.00 55.97 ? 204  ARG B C   1 
ATOM   3831 O O   . ARG B 1 204 ? -106.245 8.380  -44.418 1.00 54.24 ? 204  ARG B O   1 
ATOM   3832 C CB  . ARG B 1 204 ? -106.429 5.886  -42.598 1.00 65.59 ? 204  ARG B CB  1 
ATOM   3833 C CG  . ARG B 1 204 ? -107.240 4.751  -43.173 1.00 70.98 ? 204  ARG B CG  1 
ATOM   3834 C CD  . ARG B 1 204 ? -108.277 4.294  -42.168 1.00 75.75 ? 204  ARG B CD  1 
ATOM   3835 N NE  . ARG B 1 204 ? -109.198 5.376  -41.836 1.00 79.67 ? 204  ARG B NE  1 
ATOM   3836 C CZ  . ARG B 1 204 ? -110.012 5.953  -42.715 1.00 81.59 ? 204  ARG B CZ  1 
ATOM   3837 N NH1 . ARG B 1 204 ? -110.021 5.548  -43.981 1.00 81.80 ? 204  ARG B NH1 1 
ATOM   3838 N NH2 . ARG B 1 204 ? -110.818 6.933  -42.328 1.00 81.98 ? 204  ARG B NH2 1 
ATOM   3839 N N   . MET B 1 205 ? -105.920 6.673  -45.827 1.00 49.31 ? 205  MET B N   1 
ATOM   3840 C CA  . MET B 1 205 ? -106.444 7.416  -46.964 1.00 45.06 ? 205  MET B CA  1 
ATOM   3841 C C   . MET B 1 205 ? -107.939 7.260  -47.123 1.00 42.36 ? 205  MET B C   1 
ATOM   3842 O O   . MET B 1 205 ? -108.489 6.175  -46.937 1.00 41.47 ? 205  MET B O   1 
ATOM   3843 C CB  . MET B 1 205 ? -105.770 6.979  -48.266 1.00 41.51 ? 205  MET B CB  1 
ATOM   3844 C CG  . MET B 1 205 ? -104.315 7.357  -48.378 1.00 39.57 ? 205  MET B CG  1 
ATOM   3845 S SD  . MET B 1 205 ? -103.672 7.002  -50.016 1.00 35.57 ? 205  MET B SD  1 
ATOM   3846 C CE  . MET B 1 205 ? -102.429 8.261  -50.169 1.00 37.55 ? 205  MET B CE  1 
ATOM   3847 N N   . VAL B 1 206 ? -108.587 8.360  -47.480 1.00 40.96 ? 206  VAL B N   1 
ATOM   3848 C CA  . VAL B 1 206 ? -110.022 8.367  -47.704 1.00 41.79 ? 206  VAL B CA  1 
ATOM   3849 C C   . VAL B 1 206 ? -110.269 8.861  -49.120 1.00 40.82 ? 206  VAL B C   1 
ATOM   3850 O O   . VAL B 1 206 ? -109.609 9.785  -49.591 1.00 41.05 ? 206  VAL B O   1 
ATOM   3851 C CB  . VAL B 1 206 ? -110.744 9.285  -46.710 1.00 40.60 ? 206  VAL B CB  1 
ATOM   3852 C CG1 . VAL B 1 206 ? -110.529 8.781  -45.298 1.00 42.84 ? 206  VAL B CG1 1 
ATOM   3853 C CG2 . VAL B 1 206 ? -110.227 10.693 -46.842 1.00 44.47 ? 206  VAL B CG2 1 
ATOM   3854 N N   . LEU B 1 207 ? -111.223 8.237  -49.796 1.00 39.85 ? 207  LEU B N   1 
ATOM   3855 C CA  . LEU B 1 207 ? -111.541 8.600  -51.162 1.00 37.55 ? 207  LEU B CA  1 
ATOM   3856 C C   . LEU B 1 207 ? -112.989 9.044  -51.318 1.00 37.54 ? 207  LEU B C   1 
ATOM   3857 O O   . LEU B 1 207 ? -113.903 8.407  -50.796 1.00 38.75 ? 207  LEU B O   1 
ATOM   3858 C CB  . LEU B 1 207 ? -111.269 7.402  -52.072 1.00 36.71 ? 207  LEU B CB  1 
ATOM   3859 C CG  . LEU B 1 207 ? -111.684 7.432  -53.547 1.00 36.77 ? 207  LEU B CG  1 
ATOM   3860 C CD1 . LEU B 1 207 ? -110.825 8.418  -54.328 1.00 35.18 ? 207  LEU B CD1 1 
ATOM   3861 C CD2 . LEU B 1 207 ? -111.526 6.025  -54.123 1.00 34.77 ? 207  LEU B CD2 1 
ATOM   3862 N N   . VAL B 1 208 ? -113.179 10.155 -52.024 1.00 35.22 ? 208  VAL B N   1 
ATOM   3863 C CA  . VAL B 1 208 ? -114.501 10.691 -52.315 1.00 34.08 ? 208  VAL B CA  1 
ATOM   3864 C C   . VAL B 1 208 ? -114.527 10.875 -53.826 1.00 34.17 ? 208  VAL B C   1 
ATOM   3865 O O   . VAL B 1 208 ? -113.605 11.450 -54.404 1.00 34.14 ? 208  VAL B O   1 
ATOM   3866 C CB  . VAL B 1 208 ? -114.761 12.063 -51.619 1.00 34.28 ? 208  VAL B CB  1 
ATOM   3867 C CG1 . VAL B 1 208 ? -114.822 11.876 -50.105 1.00 35.59 ? 208  VAL B CG1 1 
ATOM   3868 C CG2 . VAL B 1 208 ? -113.676 13.058 -51.978 1.00 32.99 ? 208  VAL B CG2 1 
ATOM   3869 N N   . GLY B 1 209 ? -115.567 10.365 -54.469 1.00 34.06 ? 209  GLY B N   1 
ATOM   3870 C CA  . GLY B 1 209 ? -115.663 10.491 -55.912 1.00 35.19 ? 209  GLY B CA  1 
ATOM   3871 C C   . GLY B 1 209 ? -115.853 9.131  -56.550 1.00 35.21 ? 209  GLY B C   1 
ATOM   3872 O O   . GLY B 1 209 ? -115.453 8.118  -55.985 1.00 33.85 ? 209  GLY B O   1 
ATOM   3873 N N   . ASP B 1 210 ? -116.447 9.109  -57.737 1.00 36.66 ? 210  ASP B N   1 
ATOM   3874 C CA  . ASP B 1 210 ? -116.714 7.852  -58.427 1.00 37.85 ? 210  ASP B CA  1 
ATOM   3875 C C   . ASP B 1 210 ? -115.572 7.355  -59.306 1.00 36.33 ? 210  ASP B C   1 
ATOM   3876 O O   . ASP B 1 210 ? -115.172 8.018  -60.267 1.00 35.51 ? 210  ASP B O   1 
ATOM   3877 C CB  . ASP B 1 210 ? -117.997 7.986  -59.259 1.00 41.38 ? 210  ASP B CB  1 
ATOM   3878 C CG  . ASP B 1 210 ? -118.314 6.730  -60.052 1.00 45.12 ? 210  ASP B CG  1 
ATOM   3879 O OD1 . ASP B 1 210 ? -117.605 6.460  -61.041 1.00 49.98 ? 210  ASP B OD1 1 
ATOM   3880 O OD2 . ASP B 1 210 ? -119.266 6.006  -59.685 1.00 48.01 ? 210  ASP B OD2 1 
ATOM   3881 N N   . VAL B 1 211 ? -115.054 6.179  -58.962 1.00 34.32 ? 211  VAL B N   1 
ATOM   3882 C CA  . VAL B 1 211 ? -113.973 5.562  -59.716 1.00 35.19 ? 211  VAL B CA  1 
ATOM   3883 C C   . VAL B 1 211 ? -114.332 4.125  -60.109 1.00 34.22 ? 211  VAL B C   1 
ATOM   3884 O O   . VAL B 1 211 ? -113.595 3.472  -60.843 1.00 31.85 ? 211  VAL B O   1 
ATOM   3885 C CB  . VAL B 1 211 ? -112.666 5.536  -58.901 1.00 35.76 ? 211  VAL B CB  1 
ATOM   3886 C CG1 . VAL B 1 211 ? -112.302 6.949  -58.462 1.00 36.80 ? 211  VAL B CG1 1 
ATOM   3887 C CG2 . VAL B 1 211 ? -112.821 4.620  -57.692 1.00 34.72 ? 211  VAL B CG2 1 
ATOM   3888 N N   . LYS B 1 212 ? -115.476 3.646  -59.631 1.00 35.04 ? 212  LYS B N   1 
ATOM   3889 C CA  . LYS B 1 212 ? -115.899 2.280  -59.919 1.00 36.46 ? 212  LYS B CA  1 
ATOM   3890 C C   . LYS B 1 212 ? -116.037 1.951  -61.399 1.00 34.97 ? 212  LYS B C   1 
ATOM   3891 O O   . LYS B 1 212 ? -116.765 2.611  -62.132 1.00 31.59 ? 212  LYS B O   1 
ATOM   3892 C CB  . LYS B 1 212 ? -117.215 1.956  -59.206 1.00 39.32 ? 212  LYS B CB  1 
ATOM   3893 C CG  . LYS B 1 212 ? -117.588 0.480  -59.334 1.00 44.15 ? 212  LYS B CG  1 
ATOM   3894 C CD  . LYS B 1 212 ? -118.705 0.077  -58.403 1.00 47.85 ? 212  LYS B CD  1 
ATOM   3895 C CE  . LYS B 1 212 ? -118.911 -1.423 -58.470 1.00 51.75 ? 212  LYS B CE  1 
ATOM   3896 N NZ  . LYS B 1 212 ? -117.624 -2.150 -58.227 1.00 51.55 ? 212  LYS B NZ  1 
ATOM   3897 N N   . ASP B 1 213 ? -115.330 0.908  -61.819 1.00 37.14 ? 213  ASP B N   1 
ATOM   3898 C CA  . ASP B 1 213 ? -115.345 0.455  -63.202 1.00 38.85 ? 213  ASP B CA  1 
ATOM   3899 C C   . ASP B 1 213 ? -114.850 1.478  -64.197 1.00 38.28 ? 213  ASP B C   1 
ATOM   3900 O O   . ASP B 1 213 ? -115.159 1.385  -65.386 1.00 38.79 ? 213  ASP B O   1 
ATOM   3901 C CB  . ASP B 1 213 ? -116.743 0.015  -63.617 1.00 41.72 ? 213  ASP B CB  1 
ATOM   3902 C CG  . ASP B 1 213 ? -117.116 -1.323 -63.046 1.00 46.98 ? 213  ASP B CG  1 
ATOM   3903 O OD1 . ASP B 1 213 ? -117.377 -1.401 -61.826 1.00 49.61 ? 213  ASP B OD1 1 
ATOM   3904 O OD2 . ASP B 1 213 ? -117.137 -2.302 -63.823 1.00 52.26 ? 213  ASP B OD2 1 
ATOM   3905 N N   . ARG B 1 214 ? -114.096 2.459  -63.719 1.00 36.56 ? 214  ARG B N   1 
ATOM   3906 C CA  . ARG B 1 214 ? -113.549 3.469  -64.615 1.00 34.43 ? 214  ARG B CA  1 
ATOM   3907 C C   . ARG B 1 214 ? -112.034 3.475  -64.527 1.00 31.85 ? 214  ARG B C   1 
ATOM   3908 O O   . ARG B 1 214 ? -111.454 2.990  -63.556 1.00 30.85 ? 214  ARG B O   1 
ATOM   3909 C CB  . ARG B 1 214 ? -114.058 4.862  -64.252 1.00 36.38 ? 214  ARG B CB  1 
ATOM   3910 C CG  . ARG B 1 214 ? -115.550 5.066  -64.410 1.00 39.02 ? 214  ARG B CG  1 
ATOM   3911 C CD  . ARG B 1 214 ? -115.880 6.546  -64.332 1.00 42.02 ? 214  ARG B CD  1 
ATOM   3912 N NE  . ARG B 1 214 ? -117.079 6.851  -65.106 1.00 46.44 ? 214  ARG B NE  1 
ATOM   3913 C CZ  . ARG B 1 214 ? -117.305 8.010  -65.713 1.00 46.47 ? 214  ARG B CZ  1 
ATOM   3914 N NH1 . ARG B 1 214 ? -116.410 8.993  -65.639 1.00 46.38 ? 214  ARG B NH1 1 
ATOM   3915 N NH2 . ARG B 1 214 ? -118.423 8.180  -66.406 1.00 48.91 ? 214  ARG B NH2 1 
ATOM   3916 N N   . VAL B 1 215 ? -111.397 4.013  -65.558 1.00 28.90 ? 215  VAL B N   1 
ATOM   3917 C CA  . VAL B 1 215 ? -109.950 4.137  -65.571 1.00 25.00 ? 215  VAL B CA  1 
ATOM   3918 C C   . VAL B 1 215 ? -109.687 5.348  -64.678 1.00 25.92 ? 215  VAL B C   1 
ATOM   3919 O O   . VAL B 1 215 ? -110.321 6.392  -64.840 1.00 26.68 ? 215  VAL B O   1 
ATOM   3920 C CB  . VAL B 1 215 ? -109.435 4.423  -67.004 1.00 24.27 ? 215  VAL B CB  1 
ATOM   3921 C CG1 . VAL B 1 215 ? -107.962 4.780  -66.972 1.00 21.62 ? 215  VAL B CG1 1 
ATOM   3922 C CG2 . VAL B 1 215 ? -109.687 3.214  -67.905 1.00 18.60 ? 215  VAL B CG2 1 
ATOM   3923 N N   . ALA B 1 216 ? -108.784 5.218  -63.718 1.00 25.05 ? 216  ALA B N   1 
ATOM   3924 C CA  . ALA B 1 216 ? -108.494 6.345  -62.837 1.00 26.45 ? 216  ALA B CA  1 
ATOM   3925 C C   . ALA B 1 216 ? -107.154 6.971  -63.184 1.00 26.37 ? 216  ALA B C   1 
ATOM   3926 O O   . ALA B 1 216 ? -106.143 6.276  -63.305 1.00 28.86 ? 216  ALA B O   1 
ATOM   3927 C CB  . ALA B 1 216 ? -108.501 5.900  -61.374 1.00 23.66 ? 216  ALA B CB  1 
ATOM   3928 N N   . ILE B 1 217 ? -107.148 8.288  -63.346 1.00 26.11 ? 217  ILE B N   1 
ATOM   3929 C CA  . ILE B 1 217 ? -105.918 8.989  -63.675 1.00 26.49 ? 217  ILE B CA  1 
ATOM   3930 C C   . ILE B 1 217 ? -105.511 9.911  -62.536 1.00 26.62 ? 217  ILE B C   1 
ATOM   3931 O O   . ILE B 1 217 ? -106.156 10.932 -62.293 1.00 23.42 ? 217  ILE B O   1 
ATOM   3932 C CB  . ILE B 1 217 ? -106.063 9.835  -64.962 1.00 25.34 ? 217  ILE B CB  1 
ATOM   3933 C CG1 . ILE B 1 217 ? -106.616 8.967  -66.100 1.00 28.01 ? 217  ILE B CG1 1 
ATOM   3934 C CG2 . ILE B 1 217 ? -104.713 10.401 -65.361 1.00 25.38 ? 217  ILE B CG2 1 
ATOM   3935 C CD1 . ILE B 1 217 ? -106.780 9.693  -67.421 1.00 27.61 ? 217  ILE B CD1 1 
ATOM   3936 N N   . LEU B 1 218 ? -104.456 9.531  -61.820 1.00 26.13 ? 218  LEU B N   1 
ATOM   3937 C CA  . LEU B 1 218 ? -103.952 10.358 -60.726 1.00 26.81 ? 218  LEU B CA  1 
ATOM   3938 C C   . LEU B 1 218 ? -103.170 11.496 -61.374 1.00 28.14 ? 218  LEU B C   1 
ATOM   3939 O O   . LEU B 1 218 ? -102.223 11.260 -62.135 1.00 27.10 ? 218  LEU B O   1 
ATOM   3940 C CB  . LEU B 1 218 ? -103.036 9.546  -59.804 1.00 24.26 ? 218  LEU B CB  1 
ATOM   3941 C CG  . LEU B 1 218 ? -103.735 8.662  -58.765 1.00 24.97 ? 218  LEU B CG  1 
ATOM   3942 C CD1 . LEU B 1 218 ? -102.780 7.594  -58.236 1.00 21.86 ? 218  LEU B CD1 1 
ATOM   3943 C CD2 . LEU B 1 218 ? -104.261 9.545  -57.636 1.00 25.54 ? 218  LEU B CD2 1 
ATOM   3944 N N   . VAL B 1 219 ? -103.580 12.726 -61.084 1.00 29.00 ? 219  VAL B N   1 
ATOM   3945 C CA  . VAL B 1 219 ? -102.920 13.895 -61.647 1.00 29.88 ? 219  VAL B CA  1 
ATOM   3946 C C   . VAL B 1 219 ? -102.428 14.837 -60.558 1.00 33.04 ? 219  VAL B C   1 
ATOM   3947 O O   . VAL B 1 219 ? -103.186 15.218 -59.667 1.00 33.83 ? 219  VAL B O   1 
ATOM   3948 C CB  . VAL B 1 219 ? -103.875 14.682 -62.579 1.00 29.32 ? 219  VAL B CB  1 
ATOM   3949 C CG1 . VAL B 1 219 ? -103.171 15.910 -63.134 1.00 29.03 ? 219  VAL B CG1 1 
ATOM   3950 C CG2 . VAL B 1 219 ? -104.353 13.786 -63.715 1.00 28.29 ? 219  VAL B CG2 1 
ATOM   3951 N N   . ASP B 1 220 ? -101.153 15.203 -60.637 1.00 33.69 ? 220  ASP B N   1 
ATOM   3952 C CA  . ASP B 1 220 ? -100.561 16.122 -59.682 1.00 32.74 ? 220  ASP B CA  1 
ATOM   3953 C C   . ASP B 1 220 ? -99.443  16.908 -60.356 1.00 32.41 ? 220  ASP B C   1 
ATOM   3954 O O   . ASP B 1 220 ? -99.046  16.594 -61.474 1.00 29.38 ? 220  ASP B O   1 
ATOM   3955 C CB  . ASP B 1 220 ? -100.020 15.359 -58.478 1.00 35.91 ? 220  ASP B CB  1 
ATOM   3956 C CG  . ASP B 1 220 ? -99.962  16.217 -57.241 1.00 38.48 ? 220  ASP B CG  1 
ATOM   3957 O OD1 . ASP B 1 220 ? -100.749 17.186 -57.163 1.00 39.96 ? 220  ASP B OD1 1 
ATOM   3958 O OD2 . ASP B 1 220 ? -99.148  15.921 -56.346 1.00 40.95 ? 220  ASP B OD2 1 
ATOM   3959 N N   . ASP B 1 221 ? -98.943  17.935 -59.678 1.00 31.62 ? 221  ASP B N   1 
ATOM   3960 C CA  . ASP B 1 221 ? -97.875  18.758 -60.234 1.00 32.36 ? 221  ASP B CA  1 
ATOM   3961 C C   . ASP B 1 221 ? -96.503  18.094 -60.123 1.00 32.04 ? 221  ASP B C   1 
ATOM   3962 O O   . ASP B 1 221 ? -95.643  18.275 -60.988 1.00 31.37 ? 221  ASP B O   1 
ATOM   3963 C CB  . ASP B 1 221 ? -97.856  20.130 -59.546 1.00 34.17 ? 221  ASP B CB  1 
ATOM   3964 C CG  . ASP B 1 221 ? -97.587  20.035 -58.058 1.00 34.99 ? 221  ASP B CG  1 
ATOM   3965 O OD1 . ASP B 1 221 ? -98.243  19.225 -57.377 1.00 39.65 ? 221  ASP B OD1 1 
ATOM   3966 O OD2 . ASP B 1 221 ? -96.725  20.781 -57.563 1.00 38.25 ? 221  ASP B OD2 1 
ATOM   3967 N N   . MET B 1 222 ? -96.301  17.316 -59.065 1.00 32.05 ? 222  MET B N   1 
ATOM   3968 C CA  . MET B 1 222 ? -95.026  16.649 -58.873 1.00 33.91 ? 222  MET B CA  1 
ATOM   3969 C C   . MET B 1 222 ? -95.125  15.388 -58.037 1.00 34.71 ? 222  MET B C   1 
ATOM   3970 O O   . MET B 1 222 ? -96.059  15.202 -57.257 1.00 36.04 ? 222  MET B O   1 
ATOM   3971 C CB  . MET B 1 222 ? -94.025  17.599 -58.206 1.00 36.60 ? 222  MET B CB  1 
ATOM   3972 C CG  . MET B 1 222 ? -94.388  17.982 -56.777 1.00 38.75 ? 222  MET B CG  1 
ATOM   3973 S SD  . MET B 1 222 ? -93.140  19.033 -55.970 1.00 44.80 ? 222  MET B SD  1 
ATOM   3974 C CE  . MET B 1 222 ? -93.612  20.679 -56.583 1.00 41.52 ? 222  MET B CE  1 
ATOM   3975 N N   . ALA B 1 223 ? -94.136  14.522 -58.212 1.00 36.29 ? 223  ALA B N   1 
ATOM   3976 C CA  . ALA B 1 223 ? -94.050  13.277 -57.470 1.00 36.87 ? 223  ALA B CA  1 
ATOM   3977 C C   . ALA B 1 223 ? -92.600  13.149 -57.036 1.00 36.97 ? 223  ALA B C   1 
ATOM   3978 O O   . ALA B 1 223 ? -91.690  13.235 -57.858 1.00 36.90 ? 223  ALA B O   1 
ATOM   3979 C CB  . ALA B 1 223 ? -94.443  12.105 -58.350 1.00 39.67 ? 223  ALA B CB  1 
ATOM   3980 N N   . ASP B 1 224 ? -92.393  12.955 -55.740 1.00 37.71 ? 224  ASP B N   1 
ATOM   3981 C CA  . ASP B 1 224 ? -91.055  12.828 -55.190 1.00 37.51 ? 224  ASP B CA  1 
ATOM   3982 C C   . ASP B 1 224 ? -90.788  11.380 -54.799 1.00 37.69 ? 224  ASP B C   1 
ATOM   3983 O O   . ASP B 1 224 ? -90.406  10.575 -55.645 1.00 38.56 ? 224  ASP B O   1 
ATOM   3984 C CB  . ASP B 1 224 ? -90.909  13.751 -53.978 1.00 40.13 ? 224  ASP B CB  1 
ATOM   3985 C CG  . ASP B 1 224 ? -89.475  13.914 -53.539 1.00 40.39 ? 224  ASP B CG  1 
ATOM   3986 O OD1 . ASP B 1 224 ? -88.565  13.481 -54.281 1.00 38.98 ? 224  ASP B OD1 1 
ATOM   3987 O OD2 . ASP B 1 224 ? -89.260  14.492 -52.451 1.00 45.33 ? 224  ASP B OD2 1 
ATOM   3988 N N   . THR B 1 225 ? -90.999  11.042 -53.530 1.00 36.41 ? 225  THR B N   1 
ATOM   3989 C CA  . THR B 1 225 ? -90.770  9.673  -53.070 1.00 38.12 ? 225  THR B CA  1 
ATOM   3990 C C   . THR B 1 225 ? -91.858  8.724  -53.572 1.00 37.43 ? 225  THR B C   1 
ATOM   3991 O O   . THR B 1 225 ? -91.732  7.507  -53.454 1.00 38.85 ? 225  THR B O   1 
ATOM   3992 C CB  . THR B 1 225 ? -90.719  9.597  -51.533 1.00 38.72 ? 225  THR B CB  1 
ATOM   3993 O OG1 . THR B 1 225 ? -91.999  9.950  -50.991 1.00 42.57 ? 225  THR B OG1 1 
ATOM   3994 C CG2 . THR B 1 225 ? -89.668  10.555 -50.995 1.00 39.39 ? 225  THR B CG2 1 
ATOM   3995 N N   . CYS B 1 226 ? -92.926  9.293  -54.126 1.00 36.07 ? 226  CYS B N   1 
ATOM   3996 C CA  . CYS B 1 226 ? -94.039  8.521  -54.682 1.00 35.44 ? 226  CYS B CA  1 
ATOM   3997 C C   . CYS B 1 226 ? -94.787  7.645  -53.688 1.00 35.97 ? 226  CYS B C   1 
ATOM   3998 O O   . CYS B 1 226 ? -95.583  6.795  -54.083 1.00 35.99 ? 226  CYS B O   1 
ATOM   3999 C CB  . CYS B 1 226 ? -93.548  7.655  -55.844 1.00 35.07 ? 226  CYS B CB  1 
ATOM   4000 S SG  . CYS B 1 226 ? -92.912  8.606  -57.253 1.00 35.61 ? 226  CYS B SG  1 
ATOM   4001 N N   . GLY B 1 227 ? -94.530  7.845  -52.401 1.00 35.62 ? 227  GLY B N   1 
ATOM   4002 C CA  . GLY B 1 227 ? -95.215  7.055  -51.400 1.00 35.01 ? 227  GLY B CA  1 
ATOM   4003 C C   . GLY B 1 227 ? -96.706  7.313  -51.485 1.00 35.58 ? 227  GLY B C   1 
ATOM   4004 O O   . GLY B 1 227 ? -97.517  6.405  -51.317 1.00 33.98 ? 227  GLY B O   1 
ATOM   4005 N N   . THR B 1 228 ? -97.066  8.558  -51.782 1.00 36.24 ? 228  THR B N   1 
ATOM   4006 C CA  . THR B 1 228 ? -98.466  8.944  -51.868 1.00 35.09 ? 228  THR B CA  1 
ATOM   4007 C C   . THR B 1 228 ? -99.193  8.390  -53.087 1.00 33.53 ? 228  THR B C   1 
ATOM   4008 O O   . THR B 1 228 ? -100.256 7.791  -52.943 1.00 33.34 ? 228  THR B O   1 
ATOM   4009 C CB  . THR B 1 228 ? -98.626  10.483 -51.835 1.00 37.28 ? 228  THR B CB  1 
ATOM   4010 O OG1 . THR B 1 228 ? -98.121  10.988 -50.590 1.00 35.38 ? 228  THR B OG1 1 
ATOM   4011 C CG2 . THR B 1 228 ? -100.098 10.870 -51.970 1.00 34.83 ? 228  THR B CG2 1 
ATOM   4012 N N   . ILE B 1 229 ? -98.638  8.572  -54.280 1.00 32.05 ? 229  ILE B N   1 
ATOM   4013 C CA  . ILE B 1 229 ? -99.316  8.062  -55.471 1.00 32.94 ? 229  ILE B CA  1 
ATOM   4014 C C   . ILE B 1 229 ? -99.366  6.538  -55.484 1.00 31.43 ? 229  ILE B C   1 
ATOM   4015 O O   . ILE B 1 229 ? -100.309 5.948  -56.014 1.00 32.01 ? 229  ILE B O   1 
ATOM   4016 C CB  . ILE B 1 229 ? -98.661  8.560  -56.798 1.00 33.34 ? 229  ILE B CB  1 
ATOM   4017 C CG1 . ILE B 1 229 ? -97.159  8.262  -56.799 1.00 33.21 ? 229  ILE B CG1 1 
ATOM   4018 C CG2 . ILE B 1 229 ? -98.947  10.044 -56.994 1.00 34.78 ? 229  ILE B CG2 1 
ATOM   4019 C CD1 . ILE B 1 229 ? -96.500  8.506  -58.139 1.00 31.92 ? 229  ILE B CD1 1 
ATOM   4020 N N   . CYS B 1 230 ? -98.360  5.895  -54.901 1.00 29.25 ? 230  CYS B N   1 
ATOM   4021 C CA  . CYS B 1 230 ? -98.361  4.442  -54.863 1.00 29.37 ? 230  CYS B CA  1 
ATOM   4022 C C   . CYS B 1 230 ? -99.502  3.963  -53.975 1.00 28.19 ? 230  CYS B C   1 
ATOM   4023 O O   . CYS B 1 230 ? -100.225 3.030  -54.327 1.00 26.91 ? 230  CYS B O   1 
ATOM   4024 C CB  . CYS B 1 230 ? -97.014  3.909  -54.364 1.00 28.71 ? 230  CYS B CB  1 
ATOM   4025 S SG  . CYS B 1 230 ? -95.711  3.998  -55.623 1.00 32.69 ? 230  CYS B SG  1 
ATOM   4026 N N   . HIS B 1 231 ? -99.677  4.615  -52.832 1.00 29.72 ? 231  HIS B N   1 
ATOM   4027 C CA  . HIS B 1 231 ? -100.753 4.244  -51.921 1.00 30.67 ? 231  HIS B CA  1 
ATOM   4028 C C   . HIS B 1 231 ? -102.113 4.612  -52.487 1.00 28.74 ? 231  HIS B C   1 
ATOM   4029 O O   . HIS B 1 231 ? -103.080 3.873  -52.307 1.00 28.96 ? 231  HIS B O   1 
ATOM   4030 C CB  . HIS B 1 231 ? -100.562 4.909  -50.553 1.00 34.20 ? 231  HIS B CB  1 
ATOM   4031 C CG  . HIS B 1 231 ? -99.612  4.174  -49.664 1.00 38.38 ? 231  HIS B CG  1 
ATOM   4032 N ND1 . HIS B 1 231 ? -98.296  3.949  -50.006 1.00 41.24 ? 231  HIS B ND1 1 
ATOM   4033 C CD2 . HIS B 1 231 ? -99.790  3.586  -48.458 1.00 41.07 ? 231  HIS B CD2 1 
ATOM   4034 C CE1 . HIS B 1 231 ? -97.706  3.256  -49.051 1.00 40.69 ? 231  HIS B CE1 1 
ATOM   4035 N NE2 . HIS B 1 231 ? -98.591  3.022  -48.099 1.00 41.58 ? 231  HIS B NE2 1 
ATOM   4036 N N   . ALA B 1 232 ? -102.189 5.748  -53.179 1.00 25.61 ? 232  ALA B N   1 
ATOM   4037 C CA  . ALA B 1 232 ? -103.449 6.175  -53.772 1.00 24.31 ? 232  ALA B CA  1 
ATOM   4038 C C   . ALA B 1 232 ? -103.906 5.159  -54.828 1.00 24.25 ? 232  ALA B C   1 
ATOM   4039 O O   . ALA B 1 232 ? -105.096 4.880  -54.950 1.00 23.99 ? 232  ALA B O   1 
ATOM   4040 C CB  . ALA B 1 232 ? -103.293 7.547  -54.395 1.00 24.38 ? 232  ALA B CB  1 
ATOM   4041 N N   . ALA B 1 233 ? -102.953 4.607  -55.578 1.00 24.81 ? 233  ALA B N   1 
ATOM   4042 C CA  . ALA B 1 233 ? -103.254 3.621  -56.620 1.00 27.03 ? 233  ALA B CA  1 
ATOM   4043 C C   . ALA B 1 233 ? -103.910 2.374  -56.032 1.00 28.66 ? 233  ALA B C   1 
ATOM   4044 O O   . ALA B 1 233 ? -104.874 1.854  -56.593 1.00 28.77 ? 233  ALA B O   1 
ATOM   4045 C CB  . ALA B 1 233 ? -101.977 3.239  -57.375 1.00 26.39 ? 233  ALA B CB  1 
ATOM   4046 N N   . ASP B 1 234 ? -103.378 1.888  -54.912 1.00 29.21 ? 234  ASP B N   1 
ATOM   4047 C CA  . ASP B 1 234 ? -103.960 0.727  -54.256 1.00 29.65 ? 234  ASP B CA  1 
ATOM   4048 C C   . ASP B 1 234 ? -105.379 1.080  -53.869 1.00 28.03 ? 234  ASP B C   1 
ATOM   4049 O O   . ASP B 1 234 ? -106.315 0.329  -54.136 1.00 28.84 ? 234  ASP B O   1 
ATOM   4050 C CB  . ASP B 1 234 ? -103.206 0.354  -52.972 1.00 29.60 ? 234  ASP B CB  1 
ATOM   4051 C CG  . ASP B 1 234 ? -101.846 -0.235 -53.243 1.00 31.35 ? 234  ASP B CG  1 
ATOM   4052 O OD1 . ASP B 1 234 ? -101.726 -1.040 -54.185 1.00 33.30 ? 234  ASP B OD1 1 
ATOM   4053 O OD2 . ASP B 1 234 ? -100.896 0.097  -52.503 1.00 36.67 ? 234  ASP B OD2 1 
ATOM   4054 N N   . LYS B 1 235 ? -105.528 2.230  -53.222 1.00 27.28 ? 235  LYS B N   1 
ATOM   4055 C CA  . LYS B 1 235 ? -106.834 2.678  -52.780 1.00 28.09 ? 235  LYS B CA  1 
ATOM   4056 C C   . LYS B 1 235 ? -107.821 2.697  -53.930 1.00 27.00 ? 235  LYS B C   1 
ATOM   4057 O O   . LYS B 1 235 ? -108.955 2.243  -53.789 1.00 26.84 ? 235  LYS B O   1 
ATOM   4058 C CB  . LYS B 1 235 ? -106.748 4.076  -52.167 1.00 29.87 ? 235  LYS B CB  1 
ATOM   4059 C CG  . LYS B 1 235 ? -108.074 4.576  -51.606 1.00 31.71 ? 235  LYS B CG  1 
ATOM   4060 C CD  . LYS B 1 235 ? -108.436 3.867  -50.310 1.00 33.48 ? 235  LYS B CD  1 
ATOM   4061 C CE  . LYS B 1 235 ? -109.830 4.261  -49.832 1.00 36.36 ? 235  LYS B CE  1 
ATOM   4062 N NZ  . LYS B 1 235 ? -110.085 3.822  -48.424 1.00 35.70 ? 235  LYS B NZ  1 
ATOM   4063 N N   . LEU B 1 236 ? -107.384 3.230  -55.068 1.00 25.63 ? 236  LEU B N   1 
ATOM   4064 C CA  . LEU B 1 236 ? -108.241 3.316  -56.239 1.00 25.17 ? 236  LEU B CA  1 
ATOM   4065 C C   . LEU B 1 236 ? -108.643 1.931  -56.772 1.00 25.43 ? 236  LEU B C   1 
ATOM   4066 O O   . LEU B 1 236 ? -109.810 1.700  -57.078 1.00 24.10 ? 236  LEU B O   1 
ATOM   4067 C CB  . LEU B 1 236 ? -107.551 4.142  -57.330 1.00 24.54 ? 236  LEU B CB  1 
ATOM   4068 C CG  . LEU B 1 236 ? -107.447 5.648  -57.051 1.00 22.81 ? 236  LEU B CG  1 
ATOM   4069 C CD1 . LEU B 1 236 ? -106.522 6.302  -58.071 1.00 22.58 ? 236  LEU B CD1 1 
ATOM   4070 C CD2 . LEU B 1 236 ? -108.838 6.271  -57.087 1.00 18.92 ? 236  LEU B CD2 1 
ATOM   4071 N N   . LEU B 1 237 ? -107.691 1.009  -56.880 1.00 26.83 ? 237  LEU B N   1 
ATOM   4072 C CA  . LEU B 1 237 ? -108.033 -0.330 -57.352 1.00 28.64 ? 237  LEU B CA  1 
ATOM   4073 C C   . LEU B 1 237 ? -109.019 -0.959 -56.365 1.00 28.36 ? 237  LEU B C   1 
ATOM   4074 O O   . LEU B 1 237 ? -110.003 -1.568 -56.765 1.00 29.00 ? 237  LEU B O   1 
ATOM   4075 C CB  . LEU B 1 237 ? -106.782 -1.197 -57.487 1.00 28.10 ? 237  LEU B CB  1 
ATOM   4076 C CG  . LEU B 1 237 ? -105.801 -0.831 -58.614 1.00 31.99 ? 237  LEU B CG  1 
ATOM   4077 C CD1 . LEU B 1 237 ? -104.681 -1.854 -58.632 1.00 30.34 ? 237  LEU B CD1 1 
ATOM   4078 C CD2 . LEU B 1 237 ? -106.512 -0.800 -59.982 1.00 27.14 ? 237  LEU B CD2 1 
ATOM   4079 N N   . SER B 1 238 ? -108.766 -0.782 -55.073 1.00 28.70 ? 238  SER B N   1 
ATOM   4080 C CA  . SER B 1 238 ? -109.649 -1.319 -54.037 1.00 28.95 ? 238  SER B CA  1 
ATOM   4081 C C   . SER B 1 238 ? -111.058 -0.761 -54.146 1.00 29.96 ? 238  SER B C   1 
ATOM   4082 O O   . SER B 1 238 ? -112.018 -1.405 -53.717 1.00 30.42 ? 238  SER B O   1 
ATOM   4083 C CB  . SER B 1 238 ? -109.104 -1.001 -52.641 1.00 26.84 ? 238  SER B CB  1 
ATOM   4084 O OG  . SER B 1 238 ? -107.914 -1.726 -52.394 1.00 31.18 ? 238  SER B OG  1 
ATOM   4085 N N   . ALA B 1 239 ? -111.172 0.445  -54.701 1.00 29.75 ? 239  ALA B N   1 
ATOM   4086 C CA  . ALA B 1 239 ? -112.460 1.105  -54.868 1.00 29.97 ? 239  ALA B CA  1 
ATOM   4087 C C   . ALA B 1 239 ? -113.153 0.717  -56.169 1.00 30.59 ? 239  ALA B C   1 
ATOM   4088 O O   . ALA B 1 239 ? -114.226 1.228  -56.479 1.00 31.95 ? 239  ALA B O   1 
ATOM   4089 C CB  . ALA B 1 239 ? -112.287 2.613  -54.815 1.00 30.33 ? 239  ALA B CB  1 
ATOM   4090 N N   . GLY B 1 240 ? -112.542 -0.169 -56.942 1.00 31.79 ? 240  GLY B N   1 
ATOM   4091 C CA  . GLY B 1 240 ? -113.177 -0.593 -58.179 1.00 32.80 ? 240  GLY B CA  1 
ATOM   4092 C C   . GLY B 1 240 ? -112.659 0.023  -59.462 1.00 32.81 ? 240  GLY B C   1 
ATOM   4093 O O   . GLY B 1 240 ? -113.301 -0.098 -60.503 1.00 34.61 ? 240  GLY B O   1 
ATOM   4094 N N   . ALA B 1 241 ? -111.513 0.692  -59.401 1.00 32.66 ? 241  ALA B N   1 
ATOM   4095 C CA  . ALA B 1 241 ? -110.935 1.293  -60.602 1.00 31.56 ? 241  ALA B CA  1 
ATOM   4096 C C   . ALA B 1 241 ? -110.429 0.173  -61.505 1.00 29.98 ? 241  ALA B C   1 
ATOM   4097 O O   . ALA B 1 241 ? -109.881 -0.823 -61.029 1.00 30.26 ? 241  ALA B O   1 
ATOM   4098 C CB  . ALA B 1 241 ? -109.784 2.227  -60.234 1.00 27.96 ? 241  ALA B CB  1 
ATOM   4099 N N   . THR B 1 242 ? -110.607 0.352  -62.805 1.00 30.85 ? 242  THR B N   1 
ATOM   4100 C CA  . THR B 1 242 ? -110.190 -0.634 -63.798 1.00 34.31 ? 242  THR B CA  1 
ATOM   4101 C C   . THR B 1 242 ? -108.680 -0.736 -63.856 1.00 33.29 ? 242  THR B C   1 
ATOM   4102 O O   . THR B 1 242 ? -108.109 -1.825 -63.853 1.00 33.99 ? 242  THR B O   1 
ATOM   4103 C CB  . THR B 1 242 ? -110.692 -0.238 -65.173 1.00 34.91 ? 242  THR B CB  1 
ATOM   4104 O OG1 . THR B 1 242 ? -112.102 -0.019 -65.104 1.00 41.78 ? 242  THR B OG1 1 
ATOM   4105 C CG2 . THR B 1 242 ? -110.407 -1.335 -66.177 1.00 41.04 ? 242  THR B CG2 1 
ATOM   4106 N N   . ARG B 1 243 ? -108.043 0.419  -63.949 1.00 33.31 ? 243  ARG B N   1 
ATOM   4107 C CA  . ARG B 1 243 ? -106.598 0.505  -63.980 1.00 34.29 ? 243  ARG B CA  1 
ATOM   4108 C C   . ARG B 1 243 ? -106.246 1.920  -63.577 1.00 32.65 ? 243  ARG B C   1 
ATOM   4109 O O   . ARG B 1 243 ? -107.061 2.831  -63.704 1.00 32.42 ? 243  ARG B O   1 
ATOM   4110 C CB  . ARG B 1 243 ? -106.034 0.126  -65.363 1.00 37.32 ? 243  ARG B CB  1 
ATOM   4111 C CG  . ARG B 1 243 ? -106.710 0.736  -66.580 1.00 43.49 ? 243  ARG B CG  1 
ATOM   4112 C CD  . ARG B 1 243 ? -106.378 -0.092 -67.838 1.00 47.04 ? 243  ARG B CD  1 
ATOM   4113 N NE  . ARG B 1 243 ? -107.023 0.420  -69.049 1.00 52.41 ? 243  ARG B NE  1 
ATOM   4114 C CZ  . ARG B 1 243 ? -106.577 1.460  -69.752 1.00 53.32 ? 243  ARG B CZ  1 
ATOM   4115 N NH1 . ARG B 1 243 ? -105.485 2.091  -69.367 1.00 54.17 ? 243  ARG B NH1 1 
ATOM   4116 N NH2 . ARG B 1 243 ? -107.215 1.874  -70.839 1.00 53.35 ? 243  ARG B NH2 1 
ATOM   4117 N N   . VAL B 1 244 ? -105.039 2.096  -63.060 1.00 32.06 ? 244  VAL B N   1 
ATOM   4118 C CA  . VAL B 1 244 ? -104.605 3.396  -62.584 1.00 29.70 ? 244  VAL B CA  1 
ATOM   4119 C C   . VAL B 1 244 ? -103.396 3.946  -63.318 1.00 29.70 ? 244  VAL B C   1 
ATOM   4120 O O   . VAL B 1 244 ? -102.456 3.221  -63.636 1.00 29.23 ? 244  VAL B O   1 
ATOM   4121 C CB  . VAL B 1 244 ? -104.283 3.325  -61.071 1.00 28.97 ? 244  VAL B CB  1 
ATOM   4122 C CG1 . VAL B 1 244 ? -103.816 4.688  -60.552 1.00 26.52 ? 244  VAL B CG1 1 
ATOM   4123 C CG2 . VAL B 1 244 ? -105.528 2.871  -60.310 1.00 27.30 ? 244  VAL B CG2 1 
ATOM   4124 N N   . TYR B 1 245 ? -103.447 5.247  -63.584 1.00 29.05 ? 245  TYR B N   1 
ATOM   4125 C CA  . TYR B 1 245 ? -102.364 5.961  -64.240 1.00 26.96 ? 245  TYR B CA  1 
ATOM   4126 C C   . TYR B 1 245 ? -101.956 7.077  -63.293 1.00 24.84 ? 245  TYR B C   1 
ATOM   4127 O O   . TYR B 1 245 ? -102.711 7.450  -62.405 1.00 22.38 ? 245  TYR B O   1 
ATOM   4128 C CB  . TYR B 1 245 ? -102.831 6.601  -65.559 1.00 29.83 ? 245  TYR B CB  1 
ATOM   4129 C CG  . TYR B 1 245 ? -102.978 5.650  -66.724 1.00 29.69 ? 245  TYR B CG  1 
ATOM   4130 C CD1 . TYR B 1 245 ? -104.136 4.902  -66.903 1.00 30.10 ? 245  TYR B CD1 1 
ATOM   4131 C CD2 . TYR B 1 245 ? -101.949 5.500  -67.644 1.00 30.06 ? 245  TYR B CD2 1 
ATOM   4132 C CE1 . TYR B 1 245 ? -104.263 4.032  -67.974 1.00 30.87 ? 245  TYR B CE1 1 
ATOM   4133 C CE2 . TYR B 1 245 ? -102.063 4.634  -68.713 1.00 31.69 ? 245  TYR B CE2 1 
ATOM   4134 C CZ  . TYR B 1 245 ? -103.217 3.905  -68.878 1.00 32.13 ? 245  TYR B CZ  1 
ATOM   4135 O OH  . TYR B 1 245 ? -103.316 3.063  -69.961 1.00 35.73 ? 245  TYR B OH  1 
ATOM   4136 N N   . ALA B 1 246 ? -100.758 7.607  -63.483 1.00 24.11 ? 246  ALA B N   1 
ATOM   4137 C CA  . ALA B 1 246 ? -100.295 8.721  -62.670 1.00 25.29 ? 246  ALA B CA  1 
ATOM   4138 C C   . ALA B 1 246 ? -99.584  9.650  -63.635 1.00 26.02 ? 246  ALA B C   1 
ATOM   4139 O O   . ALA B 1 246 ? -98.661  9.237  -64.336 1.00 27.30 ? 246  ALA B O   1 
ATOM   4140 C CB  . ALA B 1 246 ? -99.340  8.244  -61.579 1.00 23.17 ? 246  ALA B CB  1 
ATOM   4141 N N   . ILE B 1 247 ? -100.038 10.895 -63.691 1.00 27.25 ? 247  ILE B N   1 
ATOM   4142 C CA  . ILE B 1 247 ? -99.443  11.886 -64.573 1.00 27.35 ? 247  ILE B CA  1 
ATOM   4143 C C   . ILE B 1 247 ? -99.032  13.117 -63.755 1.00 28.37 ? 247  ILE B C   1 
ATOM   4144 O O   . ILE B 1 247 ? -99.882  13.839 -63.246 1.00 28.16 ? 247  ILE B O   1 
ATOM   4145 C CB  . ILE B 1 247 ? -100.443 12.301 -65.675 1.00 26.09 ? 247  ILE B CB  1 
ATOM   4146 C CG1 . ILE B 1 247 ? -100.869 11.066 -66.474 1.00 28.77 ? 247  ILE B CG1 1 
ATOM   4147 C CG2 . ILE B 1 247 ? -99.803  13.334 -66.610 1.00 25.79 ? 247  ILE B CG2 1 
ATOM   4148 C CD1 . ILE B 1 247 ? -101.967 11.332 -67.502 1.00 29.63 ? 247  ILE B CD1 1 
ATOM   4149 N N   . LEU B 1 248 ? -97.727  13.335 -63.615 1.00 29.59 ? 248  LEU B N   1 
ATOM   4150 C CA  . LEU B 1 248 ? -97.220  14.482 -62.869 1.00 31.22 ? 248  LEU B CA  1 
ATOM   4151 C C   . LEU B 1 248 ? -96.396  15.324 -63.824 1.00 32.52 ? 248  LEU B C   1 
ATOM   4152 O O   . LEU B 1 248 ? -95.757  14.778 -64.723 1.00 34.04 ? 248  LEU B O   1 
ATOM   4153 C CB  . LEU B 1 248 ? -96.303  14.045 -61.720 1.00 31.83 ? 248  LEU B CB  1 
ATOM   4154 C CG  . LEU B 1 248 ? -96.648  12.898 -60.768 1.00 34.32 ? 248  LEU B CG  1 
ATOM   4155 C CD1 . LEU B 1 248 ? -98.045  13.079 -60.210 1.00 35.43 ? 248  LEU B CD1 1 
ATOM   4156 C CD2 . LEU B 1 248 ? -96.534  11.580 -61.506 1.00 35.72 ? 248  LEU B CD2 1 
ATOM   4157 N N   . THR B 1 249 ? -96.389  16.643 -63.654 1.00 30.75 ? 249  THR B N   1 
ATOM   4158 C CA  . THR B 1 249 ? -95.566  17.433 -64.554 1.00 32.70 ? 249  THR B CA  1 
ATOM   4159 C C   . THR B 1 249 ? -94.087  17.312 -64.167 1.00 32.06 ? 249  THR B C   1 
ATOM   4160 O O   . THR B 1 249 ? -93.243  17.066 -65.026 1.00 32.11 ? 249  THR B O   1 
ATOM   4161 C CB  . THR B 1 249 ? -96.011  18.924 -64.619 1.00 34.02 ? 249  THR B CB  1 
ATOM   4162 O OG1 . THR B 1 249 ? -94.854  19.767 -64.662 1.00 37.37 ? 249  THR B OG1 1 
ATOM   4163 C CG2 . THR B 1 249 ? -96.884  19.294 -63.448 1.00 38.38 ? 249  THR B CG2 1 
ATOM   4164 N N   . HIS B 1 250 ? -93.776  17.441 -62.878 1.00 31.92 ? 250  HIS B N   1 
ATOM   4165 C CA  . HIS B 1 250 ? -92.389  17.336 -62.411 1.00 30.09 ? 250  HIS B CA  1 
ATOM   4166 C C   . HIS B 1 250 ? -92.059  15.969 -61.793 1.00 30.20 ? 250  HIS B C   1 
ATOM   4167 O O   . HIS B 1 250 ? -92.581  15.611 -60.733 1.00 30.46 ? 250  HIS B O   1 
ATOM   4168 C CB  . HIS B 1 250 ? -92.093  18.437 -61.382 1.00 27.41 ? 250  HIS B CB  1 
ATOM   4169 C CG  . HIS B 1 250 ? -92.454  19.814 -61.849 1.00 25.34 ? 250  HIS B CG  1 
ATOM   4170 N ND1 . HIS B 1 250 ? -91.822  20.432 -62.906 1.00 25.56 ? 250  HIS B ND1 1 
ATOM   4171 C CD2 . HIS B 1 250 ? -93.416  20.672 -61.431 1.00 24.58 ? 250  HIS B CD2 1 
ATOM   4172 C CE1 . HIS B 1 250 ? -92.380  21.610 -63.123 1.00 22.07 ? 250  HIS B CE1 1 
ATOM   4173 N NE2 . HIS B 1 250 ? -93.350  21.778 -62.243 1.00 25.72 ? 250  HIS B NE2 1 
ATOM   4174 N N   . GLY B 1 251 ? -91.180  15.214 -62.450 1.00 31.99 ? 251  GLY B N   1 
ATOM   4175 C CA  . GLY B 1 251 ? -90.788  13.904 -61.934 1.00 31.63 ? 251  GLY B CA  1 
ATOM   4176 C C   . GLY B 1 251 ? -89.506  13.918 -61.111 1.00 32.07 ? 251  GLY B C   1 
ATOM   4177 O O   . GLY B 1 251 ? -88.419  13.709 -61.647 1.00 30.74 ? 251  GLY B O   1 
ATOM   4178 N N   . ILE B 1 252 ? -89.627  14.163 -59.807 1.00 32.53 ? 252  ILE B N   1 
ATOM   4179 C CA  . ILE B 1 252 ? -88.461  14.215 -58.913 1.00 33.56 ? 252  ILE B CA  1 
ATOM   4180 C C   . ILE B 1 252 ? -87.891  12.809 -58.718 1.00 32.00 ? 252  ILE B C   1 
ATOM   4181 O O   . ILE B 1 252 ? -86.703  12.584 -58.910 1.00 30.29 ? 252  ILE B O   1 
ATOM   4182 C CB  . ILE B 1 252 ? -88.840  14.793 -57.529 1.00 36.11 ? 252  ILE B CB  1 
ATOM   4183 C CG1 . ILE B 1 252 ? -89.592  16.120 -57.692 1.00 37.08 ? 252  ILE B CG1 1 
ATOM   4184 C CG2 . ILE B 1 252 ? -87.582  14.999 -56.695 1.00 36.55 ? 252  ILE B CG2 1 
ATOM   4185 C CD1 . ILE B 1 252 ? -88.772  17.211 -58.327 1.00 39.58 ? 252  ILE B CD1 1 
ATOM   4186 N N   . PHE B 1 253 ? -88.752  11.878 -58.320 1.00 33.96 ? 253  PHE B N   1 
ATOM   4187 C CA  . PHE B 1 253 ? -88.367  10.485 -58.148 1.00 35.72 ? 253  PHE B CA  1 
ATOM   4188 C C   . PHE B 1 253 ? -87.102  10.256 -57.324 1.00 37.03 ? 253  PHE B C   1 
ATOM   4189 O O   . PHE B 1 253 ? -86.187  9.556  -57.764 1.00 37.34 ? 253  PHE B O   1 
ATOM   4190 C CB  . PHE B 1 253 ? -88.207  9.839  -59.538 1.00 33.77 ? 253  PHE B CB  1 
ATOM   4191 C CG  . PHE B 1 253 ? -89.463  9.859  -60.367 1.00 31.50 ? 253  PHE B CG  1 
ATOM   4192 C CD1 . PHE B 1 253 ? -89.399  9.947  -61.755 1.00 31.64 ? 253  PHE B CD1 1 
ATOM   4193 C CD2 . PHE B 1 253 ? -90.711  9.761  -59.760 1.00 31.93 ? 253  PHE B CD2 1 
ATOM   4194 C CE1 . PHE B 1 253 ? -90.564  9.946  -62.525 1.00 28.23 ? 253  PHE B CE1 1 
ATOM   4195 C CE2 . PHE B 1 253 ? -91.879  9.757  -60.522 1.00 30.44 ? 253  PHE B CE2 1 
ATOM   4196 C CZ  . PHE B 1 253 ? -91.804  9.846  -61.903 1.00 29.64 ? 253  PHE B CZ  1 
ATOM   4197 N N   . SER B 1 254 ? -87.049  10.837 -56.131 1.00 37.04 ? 254  SER B N   1 
ATOM   4198 C CA  . SER B 1 254 ? -85.884  10.664 -55.266 1.00 38.52 ? 254  SER B CA  1 
ATOM   4199 C C   . SER B 1 254 ? -86.083  9.453  -54.344 1.00 38.39 ? 254  SER B C   1 
ATOM   4200 O O   . SER B 1 254 ? -87.159  8.856  -54.315 1.00 39.82 ? 254  SER B O   1 
ATOM   4201 C CB  . SER B 1 254 ? -85.678  11.923 -54.413 1.00 37.71 ? 254  SER B CB  1 
ATOM   4202 O OG  . SER B 1 254 ? -86.683  12.021 -53.421 1.00 34.26 ? 254  SER B OG  1 
ATOM   4203 N N   . GLY B 1 255 ? -85.046  9.105  -53.589 1.00 38.45 ? 255  GLY B N   1 
ATOM   4204 C CA  . GLY B 1 255 ? -85.142  7.997  -52.653 1.00 37.54 ? 255  GLY B CA  1 
ATOM   4205 C C   . GLY B 1 255 ? -85.604  6.678  -53.239 1.00 38.62 ? 255  GLY B C   1 
ATOM   4206 O O   . GLY B 1 255 ? -85.050  6.234  -54.234 1.00 40.03 ? 255  GLY B O   1 
ATOM   4207 N N   . PRO B 1 256 ? -86.623  6.028  -52.646 1.00 38.31 ? 256  PRO B N   1 
ATOM   4208 C CA  . PRO B 1 256 ? -87.182  4.742  -53.081 1.00 39.48 ? 256  PRO B CA  1 
ATOM   4209 C C   . PRO B 1 256 ? -88.225  4.806  -54.205 1.00 39.88 ? 256  PRO B C   1 
ATOM   4210 O O   . PRO B 1 256 ? -88.748  3.771  -54.617 1.00 39.93 ? 256  PRO B O   1 
ATOM   4211 C CB  . PRO B 1 256 ? -87.788  4.195  -51.795 1.00 38.79 ? 256  PRO B CB  1 
ATOM   4212 C CG  . PRO B 1 256 ? -88.390  5.428  -51.216 1.00 38.94 ? 256  PRO B CG  1 
ATOM   4213 C CD  . PRO B 1 256 ? -87.274  6.463  -51.395 1.00 39.15 ? 256  PRO B CD  1 
ATOM   4214 N N   . ALA B 1 257 ? -88.522  6.013  -54.679 1.00 39.40 ? 257  ALA B N   1 
ATOM   4215 C CA  . ALA B 1 257 ? -89.509  6.228  -55.733 1.00 38.55 ? 257  ALA B CA  1 
ATOM   4216 C C   . ALA B 1 257 ? -89.473  5.172  -56.840 1.00 38.55 ? 257  ALA B C   1 
ATOM   4217 O O   . ALA B 1 257 ? -90.463  4.468  -57.067 1.00 37.53 ? 257  ALA B O   1 
ATOM   4218 C CB  . ALA B 1 257 ? -89.328  7.623  -56.339 1.00 38.74 ? 257  ALA B CB  1 
ATOM   4219 N N   . ILE B 1 258 ? -88.337  5.064  -57.525 1.00 38.51 ? 258  ILE B N   1 
ATOM   4220 C CA  . ILE B 1 258 ? -88.186  4.103  -58.607 1.00 39.83 ? 258  ILE B CA  1 
ATOM   4221 C C   . ILE B 1 258 ? -88.520  2.673  -58.188 1.00 40.86 ? 258  ILE B C   1 
ATOM   4222 O O   . ILE B 1 258 ? -89.212  1.964  -58.912 1.00 41.04 ? 258  ILE B O   1 
ATOM   4223 C CB  . ILE B 1 258 ? -86.758  4.152  -59.197 1.00 40.87 ? 258  ILE B CB  1 
ATOM   4224 C CG1 . ILE B 1 258 ? -86.534  5.503  -59.886 1.00 41.15 ? 258  ILE B CG1 1 
ATOM   4225 C CG2 . ILE B 1 258 ? -86.562  3.016  -60.206 1.00 39.96 ? 258  ILE B CG2 1 
ATOM   4226 C CD1 . ILE B 1 258 ? -87.541  5.802  -60.982 1.00 40.03 ? 258  ILE B CD1 1 
ATOM   4227 N N   . SER B 1 259 ? -88.035  2.245  -57.029 1.00 42.33 ? 259  SER B N   1 
ATOM   4228 C CA  . SER B 1 259 ? -88.324  0.896  -56.572 1.00 43.60 ? 259  SER B CA  1 
ATOM   4229 C C   . SER B 1 259 ? -89.796  0.817  -56.206 1.00 42.77 ? 259  SER B C   1 
ATOM   4230 O O   . SER B 1 259 ? -90.455  -0.197 -56.430 1.00 42.69 ? 259  SER B O   1 
ATOM   4231 C CB  . SER B 1 259 ? -87.462  0.552  -55.358 1.00 44.49 ? 259  SER B CB  1 
ATOM   4232 O OG  . SER B 1 259 ? -86.090  0.489  -55.714 1.00 50.18 ? 259  SER B OG  1 
ATOM   4233 N N   . ARG B 1 260 ? -90.304  1.908  -55.651 1.00 43.06 ? 260  ARG B N   1 
ATOM   4234 C CA  . ARG B 1 260 ? -91.697  1.986  -55.248 1.00 43.19 ? 260  ARG B CA  1 
ATOM   4235 C C   . ARG B 1 260 ? -92.630  1.931  -56.467 1.00 43.36 ? 260  ARG B C   1 
ATOM   4236 O O   . ARG B 1 260 ? -93.711  1.352  -56.403 1.00 43.17 ? 260  ARG B O   1 
ATOM   4237 C CB  . ARG B 1 260 ? -91.922  3.275  -54.461 1.00 44.17 ? 260  ARG B CB  1 
ATOM   4238 C CG  . ARG B 1 260 ? -92.840  3.102  -53.278 1.00 45.44 ? 260  ARG B CG  1 
ATOM   4239 C CD  . ARG B 1 260 ? -92.133  3.383  -51.968 1.00 45.80 ? 260  ARG B CD  1 
ATOM   4240 N NE  . ARG B 1 260 ? -91.939  4.811  -51.756 1.00 47.57 ? 260  ARG B NE  1 
ATOM   4241 C CZ  . ARG B 1 260 ? -91.717  5.365  -50.569 1.00 47.38 ? 260  ARG B CZ  1 
ATOM   4242 N NH1 . ARG B 1 260 ? -91.656  4.610  -49.481 1.00 49.06 ? 260  ARG B NH1 1 
ATOM   4243 N NH2 . ARG B 1 260 ? -91.580  6.678  -50.465 1.00 47.77 ? 260  ARG B NH2 1 
ATOM   4244 N N   . ILE B 1 261 ? -92.201  2.522  -57.578 1.00 43.40 ? 261  ILE B N   1 
ATOM   4245 C CA  . ILE B 1 261 ? -93.008  2.529  -58.794 1.00 43.69 ? 261  ILE B CA  1 
ATOM   4246 C C   . ILE B 1 261 ? -92.969  1.176  -59.501 1.00 44.59 ? 261  ILE B C   1 
ATOM   4247 O O   . ILE B 1 261 ? -93.974  0.725  -60.055 1.00 42.92 ? 261  ILE B O   1 
ATOM   4248 C CB  . ILE B 1 261 ? -92.537  3.633  -59.773 1.00 43.49 ? 261  ILE B CB  1 
ATOM   4249 C CG1 . ILE B 1 261 ? -92.825  5.013  -59.169 1.00 42.47 ? 261  ILE B CG1 1 
ATOM   4250 C CG2 . ILE B 1 261 ? -93.235  3.480  -61.125 1.00 42.73 ? 261  ILE B CG2 1 
ATOM   4251 C CD1 . ILE B 1 261 ? -92.378  6.170  -60.031 1.00 40.54 ? 261  ILE B CD1 1 
ATOM   4252 N N   . ASN B 1 262 ? -91.805  0.532  -59.477 1.00 45.34 ? 262  ASN B N   1 
ATOM   4253 C CA  . ASN B 1 262 ? -91.644  -0.770 -60.113 1.00 45.40 ? 262  ASN B CA  1 
ATOM   4254 C C   . ASN B 1 262 ? -92.517  -1.823 -59.455 1.00 45.06 ? 262  ASN B C   1 
ATOM   4255 O O   . ASN B 1 262 ? -92.879  -2.812 -60.078 1.00 47.05 ? 262  ASN B O   1 
ATOM   4256 C CB  . ASN B 1 262 ? -90.183  -1.223 -60.057 1.00 45.93 ? 262  ASN B CB  1 
ATOM   4257 C CG  . ASN B 1 262 ? -89.312  -0.514 -61.073 1.00 46.17 ? 262  ASN B CG  1 
ATOM   4258 O OD1 . ASN B 1 262 ? -89.668  -0.407 -62.245 1.00 46.91 ? 262  ASN B OD1 1 
ATOM   4259 N ND2 . ASN B 1 262 ? -88.155  -0.042 -60.632 1.00 48.68 ? 262  ASN B ND2 1 
ATOM   4260 N N   . ASN B 1 263 ? -92.866  -1.600 -58.195 1.00 45.96 ? 263  ASN B N   1 
ATOM   4261 C CA  . ASN B 1 263 ? -93.687  -2.545 -57.450 1.00 46.77 ? 263  ASN B CA  1 
ATOM   4262 C C   . ASN B 1 263 ? -95.152  -2.124 -57.341 1.00 47.36 ? 263  ASN B C   1 
ATOM   4263 O O   . ASN B 1 263 ? -95.977  -2.871 -56.815 1.00 49.09 ? 263  ASN B O   1 
ATOM   4264 C CB  . ASN B 1 263 ? -93.101  -2.730 -56.045 1.00 47.96 ? 263  ASN B CB  1 
ATOM   4265 C CG  . ASN B 1 263 ? -91.665  -3.238 -56.072 1.00 49.87 ? 263  ASN B CG  1 
ATOM   4266 O OD1 . ASN B 1 263 ? -90.918  -3.079 -55.105 1.00 51.88 ? 263  ASN B OD1 1 
ATOM   4267 N ND2 . ASN B 1 263 ? -91.277  -3.860 -57.178 1.00 49.31 ? 263  ASN B ND2 1 
ATOM   4268 N N   . ALA B 1 264 ? -95.478  -0.936 -57.847 1.00 45.78 ? 264  ALA B N   1 
ATOM   4269 C CA  . ALA B 1 264 ? -96.845  -0.430 -57.775 1.00 43.21 ? 264  ALA B CA  1 
ATOM   4270 C C   . ALA B 1 264 ? -97.726  -0.944 -58.910 1.00 42.83 ? 264  ALA B C   1 
ATOM   4271 O O   . ALA B 1 264 ? -97.243  -1.325 -59.970 1.00 43.69 ? 264  ALA B O   1 
ATOM   4272 C CB  . ALA B 1 264 ? -96.834  1.092  -57.768 1.00 42.87 ? 264  ALA B CB  1 
ATOM   4273 N N   . CYS B 1 265 ? -99.028  -0.924 -58.678 1.00 41.35 ? 265  CYS B N   1 
ATOM   4274 C CA  . CYS B 1 265 ? -99.992  -1.391 -59.649 1.00 42.69 ? 265  CYS B CA  1 
ATOM   4275 C C   . CYS B 1 265 ? -100.345 -0.309 -60.674 1.00 43.00 ? 265  CYS B C   1 
ATOM   4276 O O   . CYS B 1 265 ? -101.518 -0.127 -61.019 1.00 42.85 ? 265  CYS B O   1 
ATOM   4277 C CB  . CYS B 1 265 ? -101.254 -1.822 -58.920 1.00 45.75 ? 265  CYS B CB  1 
ATOM   4278 S SG  . CYS B 1 265 ? -101.883 -0.505 -57.856 1.00 51.43 ? 265  CYS B SG  1 
ATOM   4279 N N   . PHE B 1 266 ? -99.340  0.403  -61.165 1.00 41.34 ? 266  PHE B N   1 
ATOM   4280 C CA  . PHE B 1 266 ? -99.575  1.442  -62.154 1.00 40.56 ? 266  PHE B CA  1 
ATOM   4281 C C   . PHE B 1 266 ? -99.592  0.880  -63.563 1.00 40.21 ? 266  PHE B C   1 
ATOM   4282 O O   . PHE B 1 266 ? -98.811  0.001  -63.899 1.00 41.11 ? 266  PHE B O   1 
ATOM   4283 C CB  . PHE B 1 266 ? -98.486  2.525  -62.089 1.00 39.29 ? 266  PHE B CB  1 
ATOM   4284 C CG  . PHE B 1 266 ? -98.631  3.477  -60.946 1.00 38.53 ? 266  PHE B CG  1 
ATOM   4285 C CD1 . PHE B 1 266 ? -97.657  3.547  -59.965 1.00 38.09 ? 266  PHE B CD1 1 
ATOM   4286 C CD2 . PHE B 1 266 ? -99.722  4.335  -60.875 1.00 38.56 ? 266  PHE B CD2 1 
ATOM   4287 C CE1 . PHE B 1 266 ? -97.754  4.469  -58.928 1.00 38.16 ? 266  PHE B CE1 1 
ATOM   4288 C CE2 . PHE B 1 266 ? -99.829  5.258  -59.845 1.00 38.36 ? 266  PHE B CE2 1 
ATOM   4289 C CZ  . PHE B 1 266 ? -98.841  5.325  -58.869 1.00 38.75 ? 266  PHE B CZ  1 
ATOM   4290 N N   . GLU B 1 267 ? -100.462 1.408  -64.406 1.00 39.30 ? 267  GLU B N   1 
ATOM   4291 C CA  . GLU B 1 267 ? -100.505 0.949  -65.782 1.00 39.21 ? 267  GLU B CA  1 
ATOM   4292 C C   . GLU B 1 267 ? -99.309  1.644  -66.420 1.00 39.10 ? 267  GLU B C   1 
ATOM   4293 O O   . GLU B 1 267 ? -98.620  1.094  -67.276 1.00 40.71 ? 267  GLU B O   1 
ATOM   4294 C CB  . GLU B 1 267 ? -101.805 1.416  -66.441 1.00 43.36 ? 267  GLU B CB  1 
ATOM   4295 C CG  . GLU B 1 267 ? -101.960 0.977  -67.879 1.00 46.75 ? 267  GLU B CG  1 
ATOM   4296 C CD  . GLU B 1 267 ? -101.961 -0.536 -68.030 1.00 50.70 ? 267  GLU B CD  1 
ATOM   4297 O OE1 . GLU B 1 267 ? -102.965 -1.197 -67.668 1.00 50.17 ? 267  GLU B OE1 1 
ATOM   4298 O OE2 . GLU B 1 267 ? -100.937 -1.064 -68.511 1.00 54.79 ? 267  GLU B OE2 1 
ATOM   4299 N N   . ALA B 1 268 ? -99.081  2.873  -65.965 1.00 36.84 ? 268  ALA B N   1 
ATOM   4300 C CA  . ALA B 1 268 ? -98.007  3.727  -66.449 1.00 34.10 ? 268  ALA B CA  1 
ATOM   4301 C C   . ALA B 1 268 ? -97.898  4.984  -65.587 1.00 33.30 ? 268  ALA B C   1 
ATOM   4302 O O   . ALA B 1 268 ? -98.865  5.381  -64.931 1.00 30.14 ? 268  ALA B O   1 
ATOM   4303 C CB  . ALA B 1 268 ? -98.271  4.125  -67.894 1.00 34.10 ? 268  ALA B CB  1 
ATOM   4304 N N   . VAL B 1 269 ? -96.712  5.590  -65.585 1.00 30.88 ? 269  VAL B N   1 
ATOM   4305 C CA  . VAL B 1 269 ? -96.435  6.809  -64.826 1.00 28.14 ? 269  VAL B CA  1 
ATOM   4306 C C   . VAL B 1 269 ? -95.877  7.798  -65.839 1.00 28.46 ? 269  VAL B C   1 
ATOM   4307 O O   . VAL B 1 269 ? -94.814  7.578  -66.420 1.00 27.89 ? 269  VAL B O   1 
ATOM   4308 C CB  . VAL B 1 269 ? -95.412  6.542  -63.725 1.00 27.55 ? 269  VAL B CB  1 
ATOM   4309 C CG1 . VAL B 1 269 ? -95.101  7.837  -62.969 1.00 26.11 ? 269  VAL B CG1 1 
ATOM   4310 C CG2 . VAL B 1 269 ? -95.964  5.494  -62.764 1.00 28.77 ? 269  VAL B CG2 1 
ATOM   4311 N N   . VAL B 1 270 ? -96.607  8.883  -66.055 1.00 27.68 ? 270  VAL B N   1 
ATOM   4312 C CA  . VAL B 1 270 ? -96.218  9.879  -67.035 1.00 26.35 ? 270  VAL B CA  1 
ATOM   4313 C C   . VAL B 1 270 ? -95.717  11.196 -66.426 1.00 25.67 ? 270  VAL B C   1 
ATOM   4314 O O   . VAL B 1 270 ? -96.334  11.745 -65.512 1.00 25.55 ? 270  VAL B O   1 
ATOM   4315 C CB  . VAL B 1 270 ? -97.432  10.165 -67.975 1.00 25.79 ? 270  VAL B CB  1 
ATOM   4316 C CG1 . VAL B 1 270 ? -97.011  11.025 -69.135 1.00 24.79 ? 270  VAL B CG1 1 
ATOM   4317 C CG2 . VAL B 1 270 ? -98.021  8.829  -68.499 1.00 25.56 ? 270  VAL B CG2 1 
ATOM   4318 N N   . VAL B 1 271 ? -94.599  11.699 -66.940 1.00 23.96 ? 271  VAL B N   1 
ATOM   4319 C CA  . VAL B 1 271 ? -94.044  12.968 -66.468 1.00 26.07 ? 271  VAL B CA  1 
ATOM   4320 C C   . VAL B 1 271 ? -93.478  13.779 -67.638 1.00 26.54 ? 271  VAL B C   1 
ATOM   4321 O O   . VAL B 1 271 ? -93.266  13.235 -68.726 1.00 28.10 ? 271  VAL B O   1 
ATOM   4322 C CB  . VAL B 1 271 ? -92.900  12.738 -65.431 1.00 24.44 ? 271  VAL B CB  1 
ATOM   4323 C CG1 . VAL B 1 271 ? -93.459  12.116 -64.182 1.00 24.67 ? 271  VAL B CG1 1 
ATOM   4324 C CG2 . VAL B 1 271 ? -91.818  11.855 -66.015 1.00 24.17 ? 271  VAL B CG2 1 
ATOM   4325 N N   . THR B 1 272 ? -93.252  15.073 -67.433 1.00 24.41 ? 272  THR B N   1 
ATOM   4326 C CA  . THR B 1 272 ? -92.657  15.883 -68.493 1.00 25.60 ? 272  THR B CA  1 
ATOM   4327 C C   . THR B 1 272 ? -91.150  15.808 -68.300 1.00 25.81 ? 272  THR B C   1 
ATOM   4328 O O   . THR B 1 272 ? -90.664  15.170 -67.359 1.00 25.88 ? 272  THR B O   1 
ATOM   4329 C CB  . THR B 1 272 ? -93.053  17.380 -68.419 1.00 24.97 ? 272  THR B CB  1 
ATOM   4330 O OG1 . THR B 1 272 ? -92.397  18.005 -67.301 1.00 26.71 ? 272  THR B OG1 1 
ATOM   4331 C CG2 . THR B 1 272 ? -94.543  17.534 -68.306 1.00 21.99 ? 272  THR B CG2 1 
ATOM   4332 N N   . ASN B 1 273 ? -90.398  16.445 -69.183 1.00 26.78 ? 273  ASN B N   1 
ATOM   4333 C CA  . ASN B 1 273 ? -88.962  16.411 -69.013 1.00 27.40 ? 273  ASN B CA  1 
ATOM   4334 C C   . ASN B 1 273 ? -88.440  17.693 -68.362 1.00 27.79 ? 273  ASN B C   1 
ATOM   4335 O O   . ASN B 1 273 ? -87.325  18.123 -68.634 1.00 28.59 ? 273  ASN B O   1 
ATOM   4336 C CB  . ASN B 1 273 ? -88.260  16.142 -70.350 1.00 27.20 ? 273  ASN B CB  1 
ATOM   4337 C CG  . ASN B 1 273 ? -88.681  17.091 -71.442 1.00 28.56 ? 273  ASN B CG  1 
ATOM   4338 O OD1 . ASN B 1 273 ? -89.719  17.742 -71.358 1.00 33.04 ? 273  ASN B OD1 1 
ATOM   4339 N ND2 . ASN B 1 273 ? -87.883  17.155 -72.501 1.00 29.55 ? 273  ASN B ND2 1 
ATOM   4340 N N   . THR B 1 274 ? -89.249  18.303 -67.496 1.00 28.39 ? 274  THR B N   1 
ATOM   4341 C CA  . THR B 1 274 ? -88.815  19.510 -66.799 1.00 28.48 ? 274  THR B CA  1 
ATOM   4342 C C   . THR B 1 274 ? -87.610  19.146 -65.948 1.00 28.23 ? 274  THR B C   1 
ATOM   4343 O O   . THR B 1 274 ? -86.847  20.006 -65.517 1.00 28.26 ? 274  THR B O   1 
ATOM   4344 C CB  . THR B 1 274 ? -89.927  20.095 -65.890 1.00 27.44 ? 274  THR B CB  1 
ATOM   4345 O OG1 . THR B 1 274 ? -90.397  19.095 -64.979 1.00 27.20 ? 274  THR B OG1 1 
ATOM   4346 C CG2 . THR B 1 274 ? -91.081  20.607 -66.729 1.00 27.69 ? 274  THR B CG2 1 
ATOM   4347 N N   . ILE B 1 275 ? -87.457  17.846 -65.723 1.00 30.72 ? 275  ILE B N   1 
ATOM   4348 C CA  . ILE B 1 275 ? -86.361  17.274 -64.951 1.00 31.56 ? 275  ILE B CA  1 
ATOM   4349 C C   . ILE B 1 275 ? -85.843  16.096 -65.773 1.00 33.68 ? 275  ILE B C   1 
ATOM   4350 O O   . ILE B 1 275 ? -86.636  15.351 -66.345 1.00 32.65 ? 275  ILE B O   1 
ATOM   4351 C CB  . ILE B 1 275 ? -86.864  16.743 -63.588 1.00 30.88 ? 275  ILE B CB  1 
ATOM   4352 C CG1 . ILE B 1 275 ? -87.393  17.906 -62.750 1.00 32.03 ? 275  ILE B CG1 1 
ATOM   4353 C CG2 . ILE B 1 275 ? -85.750  16.007 -62.863 1.00 30.48 ? 275  ILE B CG2 1 
ATOM   4354 C CD1 . ILE B 1 275 ? -87.919  17.502 -61.410 1.00 30.59 ? 275  ILE B CD1 1 
ATOM   4355 N N   . PRO B 1 276 ? -84.511  15.925 -65.864 1.00 36.35 ? 276  PRO B N   1 
ATOM   4356 C CA  . PRO B 1 276 ? -83.954  14.805 -66.639 1.00 38.62 ? 276  PRO B CA  1 
ATOM   4357 C C   . PRO B 1 276 ? -84.547  13.482 -66.154 1.00 39.56 ? 276  PRO B C   1 
ATOM   4358 O O   . PRO B 1 276 ? -84.621  13.225 -64.949 1.00 39.31 ? 276  PRO B O   1 
ATOM   4359 C CB  . PRO B 1 276 ? -82.446  14.923 -66.396 1.00 37.70 ? 276  PRO B CB  1 
ATOM   4360 C CG  . PRO B 1 276 ? -82.359  15.653 -65.087 1.00 39.67 ? 276  PRO B CG  1 
ATOM   4361 C CD  . PRO B 1 276 ? -83.439  16.690 -65.210 1.00 35.95 ? 276  PRO B CD  1 
ATOM   4362 N N   . GLN B 1 277 ? -84.965  12.645 -67.100 1.00 41.60 ? 277  GLN B N   1 
ATOM   4363 C CA  . GLN B 1 277 ? -85.620  11.381 -66.775 1.00 43.71 ? 277  GLN B CA  1 
ATOM   4364 C C   . GLN B 1 277 ? -84.941  10.116 -67.318 1.00 45.95 ? 277  GLN B C   1 
ATOM   4365 O O   . GLN B 1 277 ? -85.292  9.001  -66.932 1.00 46.25 ? 277  GLN B O   1 
ATOM   4366 C CB  . GLN B 1 277 ? -87.064  11.460 -67.285 1.00 42.01 ? 277  GLN B CB  1 
ATOM   4367 C CG  . GLN B 1 277 ? -88.139  11.107 -66.270 1.00 42.88 ? 277  GLN B CG  1 
ATOM   4368 C CD  . GLN B 1 277 ? -88.078  11.945 -65.008 1.00 41.56 ? 277  GLN B CD  1 
ATOM   4369 O OE1 . GLN B 1 277 ? -88.269  13.165 -65.037 1.00 40.72 ? 277  GLN B OE1 1 
ATOM   4370 N NE2 . GLN B 1 277 ? -87.812  11.288 -63.884 1.00 40.43 ? 277  GLN B NE2 1 
ATOM   4371 N N   . GLU B 1 278 ? -83.962  10.297 -68.198 1.00 49.27 ? 278  GLU B N   1 
ATOM   4372 C CA  . GLU B 1 278 ? -83.248  9.185  -68.826 1.00 51.84 ? 278  GLU B CA  1 
ATOM   4373 C C   . GLU B 1 278 ? -82.686  8.126  -67.873 1.00 52.74 ? 278  GLU B C   1 
ATOM   4374 O O   . GLU B 1 278 ? -82.948  6.935  -68.038 1.00 52.61 ? 278  GLU B O   1 
ATOM   4375 C CB  . GLU B 1 278 ? -82.125  9.732  -69.711 1.00 53.66 ? 278  GLU B CB  1 
ATOM   4376 C CG  . GLU B 1 278 ? -82.592  10.751 -70.759 1.00 57.94 ? 278  GLU B CG  1 
ATOM   4377 C CD  . GLU B 1 278 ? -83.129  12.050 -70.146 1.00 61.36 ? 278  GLU B CD  1 
ATOM   4378 O OE1 . GLU B 1 278 ? -82.363  12.737 -69.428 1.00 60.85 ? 278  GLU B OE1 1 
ATOM   4379 O OE2 . GLU B 1 278 ? -84.316  12.385 -70.383 1.00 61.97 ? 278  GLU B OE2 1 
ATOM   4380 N N   . ASP B 1 279 ? -81.911  8.547  -66.881 1.00 53.94 ? 279  ASP B N   1 
ATOM   4381 C CA  . ASP B 1 279 ? -81.333  7.594  -65.939 1.00 54.86 ? 279  ASP B CA  1 
ATOM   4382 C C   . ASP B 1 279 ? -82.432  6.789  -65.243 1.00 54.25 ? 279  ASP B C   1 
ATOM   4383 O O   . ASP B 1 279 ? -82.319  5.573  -65.092 1.00 54.98 ? 279  ASP B O   1 
ATOM   4384 C CB  . ASP B 1 279 ? -80.481  8.325  -64.894 1.00 57.68 ? 279  ASP B CB  1 
ATOM   4385 C CG  . ASP B 1 279 ? -79.656  9.455  -65.498 1.00 60.06 ? 279  ASP B CG  1 
ATOM   4386 O OD1 . ASP B 1 279 ? -80.182  10.589 -65.601 1.00 61.18 ? 279  ASP B OD1 1 
ATOM   4387 O OD2 . ASP B 1 279 ? -78.490  9.207  -65.882 1.00 59.71 ? 279  ASP B OD2 1 
ATOM   4388 N N   . LYS B 1 280 ? -83.493  7.482  -64.832 1.00 52.83 ? 280  LYS B N   1 
ATOM   4389 C CA  . LYS B 1 280 ? -84.636  6.876  -64.145 1.00 50.70 ? 280  LYS B CA  1 
ATOM   4390 C C   . LYS B 1 280 ? -85.371  5.859  -65.018 1.00 50.82 ? 280  LYS B C   1 
ATOM   4391 O O   . LYS B 1 280 ? -85.798  4.809  -64.536 1.00 50.92 ? 280  LYS B O   1 
ATOM   4392 C CB  . LYS B 1 280 ? -85.634  7.962  -63.731 1.00 49.28 ? 280  LYS B CB  1 
ATOM   4393 C CG  . LYS B 1 280 ? -85.043  9.130  -62.945 1.00 48.02 ? 280  LYS B CG  1 
ATOM   4394 C CD  . LYS B 1 280 ? -84.722  8.756  -61.510 1.00 45.90 ? 280  LYS B CD  1 
ATOM   4395 C CE  . LYS B 1 280 ? -84.325  9.988  -60.706 1.00 46.57 ? 280  LYS B CE  1 
ATOM   4396 N NZ  . LYS B 1 280 ? -84.132  9.667  -59.270 1.00 45.36 ? 280  LYS B NZ  1 
ATOM   4397 N N   . MET B 1 281 ? -85.541  6.185  -66.297 1.00 49.67 ? 281  MET B N   1 
ATOM   4398 C CA  . MET B 1 281 ? -86.240  5.301  -67.225 1.00 49.22 ? 281  MET B CA  1 
ATOM   4399 C C   . MET B 1 281 ? -85.535  3.955  -67.387 1.00 49.33 ? 281  MET B C   1 
ATOM   4400 O O   . MET B 1 281 ? -86.188  2.913  -67.475 1.00 48.56 ? 281  MET B O   1 
ATOM   4401 C CB  . MET B 1 281 ? -86.397  5.988  -68.585 1.00 47.68 ? 281  MET B CB  1 
ATOM   4402 C CG  . MET B 1 281 ? -87.264  7.245  -68.535 1.00 48.45 ? 281  MET B CG  1 
ATOM   4403 S SD  . MET B 1 281 ? -87.540  8.004  -70.157 1.00 50.57 ? 281  MET B SD  1 
ATOM   4404 C CE  . MET B 1 281 ? -88.748  6.875  -70.835 1.00 47.91 ? 281  MET B CE  1 
ATOM   4405 N N   . LYS B 1 282 ? -84.206  3.979  -67.414 1.00 49.02 ? 282  LYS B N   1 
ATOM   4406 C CA  . LYS B 1 282 ? -83.424  2.755  -67.553 1.00 49.55 ? 282  LYS B CA  1 
ATOM   4407 C C   . LYS B 1 282 ? -83.827  1.709  -66.518 1.00 49.22 ? 282  LYS B C   1 
ATOM   4408 O O   . LYS B 1 282 ? -83.980  0.536  -66.849 1.00 48.71 ? 282  LYS B O   1 
ATOM   4409 C CB  . LYS B 1 282 ? -81.924  3.058  -67.416 1.00 50.88 ? 282  LYS B CB  1 
ATOM   4410 C CG  . LYS B 1 282 ? -81.305  3.737  -68.637 1.00 52.62 ? 282  LYS B CG  1 
ATOM   4411 C CD  . LYS B 1 282 ? -79.847  4.152  -68.406 1.00 54.03 ? 282  LYS B CD  1 
ATOM   4412 C CE  . LYS B 1 282 ? -78.929  2.963  -68.113 1.00 55.06 ? 282  LYS B CE  1 
ATOM   4413 N NZ  . LYS B 1 282 ? -79.174  2.309  -66.786 1.00 55.85 ? 282  LYS B NZ  1 
ATOM   4414 N N   . HIS B 1 283 ? -84.002  2.144  -65.271 1.00 47.98 ? 283  HIS B N   1 
ATOM   4415 C CA  . HIS B 1 283 ? -84.375  1.246  -64.181 1.00 47.04 ? 283  HIS B CA  1 
ATOM   4416 C C   . HIS B 1 283 ? -85.884  1.154  -63.950 1.00 45.97 ? 283  HIS B C   1 
ATOM   4417 O O   . HIS B 1 283 ? -86.334  0.445  -63.048 1.00 44.35 ? 283  HIS B O   1 
ATOM   4418 C CB  . HIS B 1 283 ? -83.706  1.707  -62.885 1.00 50.39 ? 283  HIS B CB  1 
ATOM   4419 C CG  . HIS B 1 283 ? -82.213  1.748  -62.957 1.00 53.69 ? 283  HIS B CG  1 
ATOM   4420 N ND1 . HIS B 1 283 ? -81.443  0.612  -63.087 1.00 53.44 ? 283  HIS B ND1 1 
ATOM   4421 C CD2 . HIS B 1 283 ? -81.349  2.791  -62.952 1.00 53.62 ? 283  HIS B CD2 1 
ATOM   4422 C CE1 . HIS B 1 283 ? -80.170  0.955  -63.164 1.00 54.87 ? 283  HIS B CE1 1 
ATOM   4423 N NE2 . HIS B 1 283 ? -80.086  2.271  -63.085 1.00 55.26 ? 283  HIS B NE2 1 
ATOM   4424 N N   . CYS B 1 284 ? -86.664  1.872  -64.754 1.00 43.89 ? 284  CYS B N   1 
ATOM   4425 C CA  . CYS B 1 284 ? -88.116  1.866  -64.598 1.00 43.27 ? 284  CYS B CA  1 
ATOM   4426 C C   . CYS B 1 284 ? -88.769  1.976  -65.971 1.00 43.31 ? 284  CYS B C   1 
ATOM   4427 O O   . CYS B 1 284 ? -88.701  3.016  -66.618 1.00 43.77 ? 284  CYS B O   1 
ATOM   4428 C CB  . CYS B 1 284 ? -88.547  3.039  -63.707 1.00 41.45 ? 284  CYS B CB  1 
ATOM   4429 S SG  . CYS B 1 284 ? -90.275  3.002  -63.149 1.00 40.62 ? 284  CYS B SG  1 
ATOM   4430 N N   . SER B 1 285 ? -89.394  0.893  -66.418 1.00 43.07 ? 285  SER B N   1 
ATOM   4431 C CA  . SER B 1 285 ? -90.045  0.887  -67.721 1.00 42.38 ? 285  SER B CA  1 
ATOM   4432 C C   . SER B 1 285 ? -91.478  1.434  -67.697 1.00 40.86 ? 285  SER B C   1 
ATOM   4433 O O   . SER B 1 285 ? -92.036  1.777  -68.742 1.00 39.82 ? 285  SER B O   1 
ATOM   4434 C CB  . SER B 1 285 ? -90.022  -0.527 -68.302 1.00 43.66 ? 285  SER B CB  1 
ATOM   4435 O OG  . SER B 1 285 ? -90.405  -1.475 -67.324 1.00 47.38 ? 285  SER B OG  1 
ATOM   4436 N N   . LYS B 1 286 ? -92.071  1.520  -66.511 1.00 38.33 ? 286  LYS B N   1 
ATOM   4437 C CA  . LYS B 1 286 ? -93.423  2.057  -66.390 1.00 38.41 ? 286  LYS B CA  1 
ATOM   4438 C C   . LYS B 1 286 ? -93.427  3.565  -66.672 1.00 37.19 ? 286  LYS B C   1 
ATOM   4439 O O   . LYS B 1 286 ? -94.481  4.176  -66.835 1.00 37.39 ? 286  LYS B O   1 
ATOM   4440 C CB  . LYS B 1 286 ? -93.972  1.816  -64.982 1.00 37.82 ? 286  LYS B CB  1 
ATOM   4441 C CG  . LYS B 1 286 ? -94.192  0.366  -64.630 1.00 40.31 ? 286  LYS B CG  1 
ATOM   4442 C CD  . LYS B 1 286 ? -94.778  0.247  -63.224 1.00 44.46 ? 286  LYS B CD  1 
ATOM   4443 C CE  . LYS B 1 286 ? -94.930  -1.206 -62.807 1.00 45.89 ? 286  LYS B CE  1 
ATOM   4444 N NZ  . LYS B 1 286 ? -95.299  -1.327 -61.371 1.00 47.14 ? 286  LYS B NZ  1 
ATOM   4445 N N   . ILE B 1 287 ? -92.246  4.164  -66.733 1.00 35.72 ? 287  ILE B N   1 
ATOM   4446 C CA  . ILE B 1 287 ? -92.158  5.589  -66.981 1.00 34.05 ? 287  ILE B CA  1 
ATOM   4447 C C   . ILE B 1 287 ? -92.139  5.981  -68.452 1.00 33.19 ? 287  ILE B C   1 
ATOM   4448 O O   . ILE B 1 287 ? -91.433  5.388  -69.266 1.00 32.45 ? 287  ILE B O   1 
ATOM   4449 C CB  . ILE B 1 287 ? -90.912  6.198  -66.292 1.00 34.25 ? 287  ILE B CB  1 
ATOM   4450 C CG1 . ILE B 1 287 ? -91.010  5.978  -64.779 1.00 34.58 ? 287  ILE B CG1 1 
ATOM   4451 C CG2 . ILE B 1 287 ? -90.808  7.692  -66.621 1.00 34.28 ? 287  ILE B CG2 1 
ATOM   4452 C CD1 . ILE B 1 287 ? -89.884  6.598  -63.967 1.00 35.25 ? 287  ILE B CD1 1 
ATOM   4453 N N   . GLN B 1 288 ? -92.941  6.991  -68.777 1.00 31.86 ? 288  GLN B N   1 
ATOM   4454 C CA  . GLN B 1 288 ? -93.017  7.532  -70.121 1.00 30.96 ? 288  GLN B CA  1 
ATOM   4455 C C   . GLN B 1 288 ? -92.853  9.030  -69.956 1.00 30.91 ? 288  GLN B C   1 
ATOM   4456 O O   . GLN B 1 288 ? -93.362  9.606  -69.000 1.00 31.04 ? 288  GLN B O   1 
ATOM   4457 C CB  . GLN B 1 288 ? -94.366  7.206  -70.768 1.00 31.95 ? 288  GLN B CB  1 
ATOM   4458 C CG  . GLN B 1 288 ? -94.530  5.725  -71.093 1.00 30.16 ? 288  GLN B CG  1 
ATOM   4459 C CD  . GLN B 1 288 ? -95.871  5.408  -71.694 1.00 30.32 ? 288  GLN B CD  1 
ATOM   4460 O OE1 . GLN B 1 288 ? -96.574  4.526  -71.224 1.00 34.45 ? 288  GLN B OE1 1 
ATOM   4461 N NE2 . GLN B 1 288 ? -96.235  6.126  -72.747 1.00 34.14 ? 288  GLN B NE2 1 
ATOM   4462 N N   . VAL B 1 289 ? -92.139  9.657  -70.884 1.00 30.25 ? 289  VAL B N   1 
ATOM   4463 C CA  . VAL B 1 289 ? -91.892  11.091 -70.816 1.00 30.09 ? 289  VAL B CA  1 
ATOM   4464 C C   . VAL B 1 289 ? -92.555  11.935 -71.901 1.00 29.34 ? 289  VAL B C   1 
ATOM   4465 O O   . VAL B 1 289 ? -92.524  11.588 -73.077 1.00 33.30 ? 289  VAL B O   1 
ATOM   4466 C CB  . VAL B 1 289 ? -90.373  11.370 -70.860 1.00 29.66 ? 289  VAL B CB  1 
ATOM   4467 C CG1 . VAL B 1 289 ? -90.109  12.861 -70.872 1.00 30.26 ? 289  VAL B CG1 1 
ATOM   4468 C CG2 . VAL B 1 289 ? -89.700  10.733 -69.655 1.00 30.63 ? 289  VAL B CG2 1 
ATOM   4469 N N   . ILE B 1 290 ? -93.164  13.041 -71.496 1.00 28.17 ? 290  ILE B N   1 
ATOM   4470 C CA  . ILE B 1 290 ? -93.773  13.969 -72.441 1.00 27.02 ? 290  ILE B CA  1 
ATOM   4471 C C   . ILE B 1 290 ? -92.731  15.075 -72.590 1.00 28.10 ? 290  ILE B C   1 
ATOM   4472 O O   . ILE B 1 290 ? -92.263  15.624 -71.598 1.00 25.35 ? 290  ILE B O   1 
ATOM   4473 C CB  . ILE B 1 290 ? -95.082  14.573 -71.891 1.00 26.46 ? 290  ILE B CB  1 
ATOM   4474 C CG1 . ILE B 1 290 ? -96.180  13.513 -71.877 1.00 23.49 ? 290  ILE B CG1 1 
ATOM   4475 C CG2 . ILE B 1 290 ? -95.524  15.765 -72.756 1.00 27.15 ? 290  ILE B CG2 1 
ATOM   4476 C CD1 . ILE B 1 290 ? -97.434  13.962 -71.169 1.00 26.23 ? 290  ILE B CD1 1 
ATOM   4477 N N   . ASP B 1 291 ? -92.343  15.385 -73.822 1.00 30.02 ? 291  ASP B N   1 
ATOM   4478 C CA  . ASP B 1 291 ? -91.342  16.423 -74.044 1.00 30.93 ? 291  ASP B CA  1 
ATOM   4479 C C   . ASP B 1 291 ? -91.992  17.799 -74.050 1.00 30.67 ? 291  ASP B C   1 
ATOM   4480 O O   . ASP B 1 291 ? -92.932  18.037 -74.797 1.00 30.85 ? 291  ASP B O   1 
ATOM   4481 C CB  . ASP B 1 291 ? -90.608  16.170 -75.365 1.00 33.17 ? 291  ASP B CB  1 
ATOM   4482 C CG  . ASP B 1 291 ? -89.671  17.311 -75.753 1.00 36.29 ? 291  ASP B CG  1 
ATOM   4483 O OD1 . ASP B 1 291 ? -89.216  18.065 -74.867 1.00 36.10 ? 291  ASP B OD1 1 
ATOM   4484 O OD2 . ASP B 1 291 ? -89.372  17.441 -76.959 1.00 38.89 ? 291  ASP B OD2 1 
ATOM   4485 N N   . ILE B 1 292 ? -91.513  18.697 -73.194 1.00 28.78 ? 292  ILE B N   1 
ATOM   4486 C CA  . ILE B 1 292 ? -92.081  20.032 -73.148 1.00 27.90 ? 292  ILE B CA  1 
ATOM   4487 C C   . ILE B 1 292 ? -91.111  21.107 -73.638 1.00 28.19 ? 292  ILE B C   1 
ATOM   4488 O O   . ILE B 1 292 ? -91.380  22.300 -73.507 1.00 26.91 ? 292  ILE B O   1 
ATOM   4489 C CB  . ILE B 1 292 ? -92.612  20.392 -71.720 1.00 29.47 ? 292  ILE B CB  1 
ATOM   4490 C CG1 . ILE B 1 292 ? -91.550  20.125 -70.650 1.00 27.76 ? 292  ILE B CG1 1 
ATOM   4491 C CG2 . ILE B 1 292 ? -93.879  19.600 -71.432 1.00 27.68 ? 292  ILE B CG2 1 
ATOM   4492 C CD1 . ILE B 1 292 ? -90.366  21.061 -70.700 1.00 27.66 ? 292  ILE B CD1 1 
ATOM   4493 N N   . SER B 1 293 ? -89.998  20.678 -74.229 1.00 27.69 ? 293  SER B N   1 
ATOM   4494 C CA  . SER B 1 293 ? -89.009  21.618 -74.736 1.00 29.24 ? 293  SER B CA  1 
ATOM   4495 C C   . SER B 1 293 ? -89.608  22.608 -75.738 1.00 30.04 ? 293  SER B C   1 
ATOM   4496 O O   . SER B 1 293 ? -89.258  23.794 -75.725 1.00 29.30 ? 293  SER B O   1 
ATOM   4497 C CB  . SER B 1 293 ? -87.830  20.872 -75.367 1.00 29.71 ? 293  SER B CB  1 
ATOM   4498 O OG  . SER B 1 293 ? -88.240  20.010 -76.414 1.00 31.36 ? 293  SER B OG  1 
ATOM   4499 N N   . MET B 1 294 ? -90.514  22.138 -76.592 1.00 29.57 ? 294  MET B N   1 
ATOM   4500 C CA  . MET B 1 294 ? -91.133  23.027 -77.572 1.00 32.13 ? 294  MET B CA  1 
ATOM   4501 C C   . MET B 1 294 ? -91.969  24.105 -76.911 1.00 29.95 ? 294  MET B C   1 
ATOM   4502 O O   . MET B 1 294 ? -92.044  25.233 -77.396 1.00 29.57 ? 294  MET B O   1 
ATOM   4503 C CB  . MET B 1 294 ? -91.985  22.241 -78.578 1.00 35.29 ? 294  MET B CB  1 
ATOM   4504 C CG  . MET B 1 294 ? -92.452  20.874 -78.115 1.00 43.68 ? 294  MET B CG  1 
ATOM   4505 S SD  . MET B 1 294 ? -94.039  20.925 -77.290 1.00 52.79 ? 294  MET B SD  1 
ATOM   4506 C CE  . MET B 1 294 ? -93.570  20.515 -75.713 1.00 47.74 ? 294  MET B CE  1 
ATOM   4507 N N   . ILE B 1 295 ? -92.598  23.758 -75.797 1.00 29.45 ? 295  ILE B N   1 
ATOM   4508 C CA  . ILE B 1 295 ? -93.402  24.726 -75.077 1.00 28.71 ? 295  ILE B CA  1 
ATOM   4509 C C   . ILE B 1 295 ? -92.474  25.785 -74.469 1.00 28.01 ? 295  ILE B C   1 
ATOM   4510 O O   . ILE B 1 295 ? -92.757  26.983 -74.538 1.00 30.26 ? 295  ILE B O   1 
ATOM   4511 C CB  . ILE B 1 295 ? -94.231  24.028 -73.983 1.00 30.29 ? 295  ILE B CB  1 
ATOM   4512 C CG1 . ILE B 1 295 ? -95.218  23.052 -74.644 1.00 31.04 ? 295  ILE B CG1 1 
ATOM   4513 C CG2 . ILE B 1 295 ? -94.976  25.057 -73.150 1.00 27.31 ? 295  ILE B CG2 1 
ATOM   4514 C CD1 . ILE B 1 295 ? -95.942  22.147 -73.670 1.00 32.38 ? 295  ILE B CD1 1 
ATOM   4515 N N   . LEU B 1 296 ? -91.360  25.349 -73.890 1.00 25.43 ? 296  LEU B N   1 
ATOM   4516 C CA  . LEU B 1 296 ? -90.406  26.286 -73.300 1.00 25.72 ? 296  LEU B CA  1 
ATOM   4517 C C   . LEU B 1 296 ? -89.739  27.109 -74.402 1.00 25.32 ? 296  LEU B C   1 
ATOM   4518 O O   . LEU B 1 296 ? -89.583  28.324 -74.273 1.00 24.66 ? 296  LEU B O   1 
ATOM   4519 C CB  . LEU B 1 296 ? -89.346  25.537 -72.474 1.00 23.81 ? 296  LEU B CB  1 
ATOM   4520 C CG  . LEU B 1 296 ? -89.873  24.870 -71.186 1.00 26.03 ? 296  LEU B CG  1 
ATOM   4521 C CD1 . LEU B 1 296 ? -88.776  24.062 -70.522 1.00 22.49 ? 296  LEU B CD1 1 
ATOM   4522 C CD2 . LEU B 1 296 ? -90.385  25.938 -70.233 1.00 23.03 ? 296  LEU B CD2 1 
ATOM   4523 N N   . ALA B 1 297 ? -89.359  26.447 -75.492 1.00 25.85 ? 297  ALA B N   1 
ATOM   4524 C CA  . ALA B 1 297 ? -88.720  27.133 -76.613 1.00 26.39 ? 297  ALA B CA  1 
ATOM   4525 C C   . ALA B 1 297 ? -89.635  28.238 -77.165 1.00 26.38 ? 297  ALA B C   1 
ATOM   4526 O O   . ALA B 1 297 ? -89.180  29.332 -77.475 1.00 26.55 ? 297  ALA B O   1 
ATOM   4527 C CB  . ALA B 1 297 ? -88.380  26.133 -77.703 1.00 24.10 ? 297  ALA B CB  1 
ATOM   4528 N N   . GLU B 1 298 ? -90.926  27.945 -77.257 1.00 27.28 ? 298  GLU B N   1 
ATOM   4529 C CA  . GLU B 1 298 ? -91.914  28.898 -77.756 1.00 30.84 ? 298  GLU B CA  1 
ATOM   4530 C C   . GLU B 1 298 ? -92.118  30.098 -76.817 1.00 30.64 ? 298  GLU B C   1 
ATOM   4531 O O   . GLU B 1 298 ? -92.275  31.233 -77.269 1.00 29.15 ? 298  GLU B O   1 
ATOM   4532 C CB  . GLU B 1 298 ? -93.258  28.193 -77.963 1.00 34.56 ? 298  GLU B CB  1 
ATOM   4533 C CG  . GLU B 1 298 ? -94.304  29.078 -78.601 1.00 40.22 ? 298  GLU B CG  1 
ATOM   4534 C CD  . GLU B 1 298 ? -94.182  29.124 -80.111 1.00 44.37 ? 298  GLU B CD  1 
ATOM   4535 O OE1 . GLU B 1 298 ? -93.048  29.015 -80.630 1.00 43.82 ? 298  GLU B OE1 1 
ATOM   4536 O OE2 . GLU B 1 298 ? -95.226  29.275 -80.777 1.00 47.14 ? 298  GLU B OE2 1 
ATOM   4537 N N   . ALA B 1 299 ? -92.145  29.845 -75.512 1.00 28.87 ? 299  ALA B N   1 
ATOM   4538 C CA  . ALA B 1 299 ? -92.315  30.936 -74.553 1.00 27.45 ? 299  ALA B CA  1 
ATOM   4539 C C   . ALA B 1 299 ? -91.112  31.874 -74.657 1.00 26.27 ? 299  ALA B C   1 
ATOM   4540 O O   . ALA B 1 299 ? -91.250  33.096 -74.593 1.00 26.53 ? 299  ALA B O   1 
ATOM   4541 C CB  . ALA B 1 299 ? -92.442  30.384 -73.138 1.00 27.32 ? 299  ALA B CB  1 
ATOM   4542 N N   . ILE B 1 300 ? -89.929  31.304 -74.837 1.00 25.29 ? 300  ILE B N   1 
ATOM   4543 C CA  . ILE B 1 300 ? -88.734  32.123 -74.964 1.00 25.92 ? 300  ILE B CA  1 
ATOM   4544 C C   . ILE B 1 300 ? -88.776  32.943 -76.250 1.00 25.92 ? 300  ILE B C   1 
ATOM   4545 O O   . ILE B 1 300 ? -88.499  34.136 -76.234 1.00 24.00 ? 300  ILE B O   1 
ATOM   4546 C CB  . ILE B 1 300 ? -87.457  31.269 -74.968 1.00 23.82 ? 300  ILE B CB  1 
ATOM   4547 C CG1 . ILE B 1 300 ? -87.241  30.652 -73.579 1.00 24.62 ? 300  ILE B CG1 1 
ATOM   4548 C CG2 . ILE B 1 300 ? -86.278  32.119 -75.385 1.00 23.58 ? 300  ILE B CG2 1 
ATOM   4549 C CD1 . ILE B 1 300 ? -86.122  29.618 -73.519 1.00 22.71 ? 300  ILE B CD1 1 
ATOM   4550 N N   . ARG B 1 301 ? -89.125  32.295 -77.358 1.00 27.77 ? 301  ARG B N   1 
ATOM   4551 C CA  . ARG B 1 301 ? -89.196  32.966 -78.647 1.00 29.33 ? 301  ARG B CA  1 
ATOM   4552 C C   . ARG B 1 301 ? -90.197  34.118 -78.631 1.00 31.20 ? 301  ARG B C   1 
ATOM   4553 O O   . ARG B 1 301 ? -89.930  35.197 -79.151 1.00 30.89 ? 301  ARG B O   1 
ATOM   4554 C CB  . ARG B 1 301 ? -89.586  31.970 -79.739 1.00 34.82 ? 301  ARG B CB  1 
ATOM   4555 C CG  . ARG B 1 301 ? -89.500  32.557 -81.143 1.00 39.38 ? 301  ARG B CG  1 
ATOM   4556 C CD  . ARG B 1 301 ? -89.852  31.545 -82.220 1.00 41.10 ? 301  ARG B CD  1 
ATOM   4557 N NE  . ARG B 1 301 ? -91.024  31.980 -82.976 1.00 46.34 ? 301  ARG B NE  1 
ATOM   4558 C CZ  . ARG B 1 301 ? -92.274  31.866 -82.538 1.00 46.45 ? 301  ARG B CZ  1 
ATOM   4559 N NH1 . ARG B 1 301 ? -92.511  31.324 -81.353 1.00 50.35 ? 301  ARG B NH1 1 
ATOM   4560 N NH2 . ARG B 1 301 ? -93.284  32.307 -83.271 1.00 45.96 ? 301  ARG B NH2 1 
ATOM   4561 N N   . ARG B 1 302 ? -91.349  33.886 -78.019 1.00 32.91 ? 302  ARG B N   1 
ATOM   4562 C CA  . ARG B 1 302 ? -92.384  34.903 -77.945 1.00 34.36 ? 302  ARG B CA  1 
ATOM   4563 C C   . ARG B 1 302 ? -92.022  36.001 -76.954 1.00 34.30 ? 302  ARG B C   1 
ATOM   4564 O O   . ARG B 1 302 ? -92.317  37.176 -77.178 1.00 35.24 ? 302  ARG B O   1 
ATOM   4565 C CB  . ARG B 1 302 ? -93.716  34.243 -77.595 1.00 36.91 ? 302  ARG B CB  1 
ATOM   4566 C CG  . ARG B 1 302 ? -94.111  33.192 -78.626 1.00 39.33 ? 302  ARG B CG  1 
ATOM   4567 C CD  . ARG B 1 302 ? -95.527  32.710 -78.439 1.00 44.23 ? 302  ARG B CD  1 
ATOM   4568 N NE  . ARG B 1 302 ? -95.912  31.760 -79.476 1.00 47.20 ? 302  ARG B NE  1 
ATOM   4569 C CZ  . ARG B 1 302 ? -97.162  31.579 -79.886 1.00 49.79 ? 302  ARG B CZ  1 
ATOM   4570 N NH1 . ARG B 1 302 ? -98.149  32.286 -79.347 1.00 49.65 ? 302  ARG B NH1 1 
ATOM   4571 N NH2 . ARG B 1 302 ? -97.425  30.698 -80.838 1.00 52.01 ? 302  ARG B NH2 1 
ATOM   4572 N N   . THR B 1 303 ? -91.371  35.615 -75.866 1.00 32.06 ? 303  THR B N   1 
ATOM   4573 C CA  . THR B 1 303 ? -90.926  36.571 -74.860 1.00 32.77 ? 303  THR B CA  1 
ATOM   4574 C C   . THR B 1 303 ? -89.991  37.555 -75.539 1.00 32.54 ? 303  THR B C   1 
ATOM   4575 O O   . THR B 1 303 ? -90.119  38.761 -75.369 1.00 31.85 ? 303  THR B O   1 
ATOM   4576 C CB  . THR B 1 303 ? -90.140  35.863 -73.732 1.00 32.86 ? 303  THR B CB  1 
ATOM   4577 O OG1 . THR B 1 303 ? -91.059  35.192 -72.869 1.00 35.13 ? 303  THR B OG1 1 
ATOM   4578 C CG2 . THR B 1 303 ? -89.316  36.853 -72.932 1.00 31.48 ? 303  THR B CG2 1 
ATOM   4579 N N   . HIS B 1 304 ? -89.049  37.018 -76.312 1.00 32.88 ? 304  HIS B N   1 
ATOM   4580 C CA  . HIS B 1 304 ? -88.065  37.820 -77.023 1.00 32.36 ? 304  HIS B CA  1 
ATOM   4581 C C   . HIS B 1 304 ? -88.701  38.730 -78.077 1.00 34.72 ? 304  HIS B C   1 
ATOM   4582 O O   . HIS B 1 304 ? -88.315  39.891 -78.208 1.00 34.57 ? 304  HIS B O   1 
ATOM   4583 C CB  . HIS B 1 304 ? -87.034  36.900 -77.676 1.00 32.25 ? 304  HIS B CB  1 
ATOM   4584 C CG  . HIS B 1 304 ? -85.987  37.621 -78.465 1.00 33.76 ? 304  HIS B CG  1 
ATOM   4585 N ND1 . HIS B 1 304 ? -85.121  38.534 -77.899 1.00 34.04 ? 304  HIS B ND1 1 
ATOM   4586 C CD2 . HIS B 1 304 ? -85.665  37.567 -79.779 1.00 32.44 ? 304  HIS B CD2 1 
ATOM   4587 C CE1 . HIS B 1 304 ? -84.314  39.010 -78.829 1.00 33.87 ? 304  HIS B CE1 1 
ATOM   4588 N NE2 . HIS B 1 304 ? -84.623  38.438 -79.981 1.00 34.47 ? 304  HIS B NE2 1 
ATOM   4589 N N   . ASN B 1 305 ? -89.677  38.211 -78.817 1.00 35.96 ? 305  ASN B N   1 
ATOM   4590 C CA  . ASN B 1 305 ? -90.347  38.995 -79.860 1.00 37.92 ? 305  ASN B CA  1 
ATOM   4591 C C   . ASN B 1 305 ? -91.492  39.852 -79.343 1.00 39.33 ? 305  ASN B C   1 
ATOM   4592 O O   . ASN B 1 305 ? -92.095  40.609 -80.103 1.00 38.83 ? 305  ASN B O   1 
ATOM   4593 C CB  . ASN B 1 305 ? -90.886  38.077 -80.962 1.00 37.59 ? 305  ASN B CB  1 
ATOM   4594 C CG  . ASN B 1 305 ? -89.786  37.350 -81.693 1.00 38.73 ? 305  ASN B CG  1 
ATOM   4595 O OD1 . ASN B 1 305 ? -88.749  37.933 -81.999 1.00 39.42 ? 305  ASN B OD1 1 
ATOM   4596 N ND2 . ASN B 1 305 ? -90.002  36.071 -81.981 1.00 40.15 ? 305  ASN B ND2 1 
ATOM   4597 N N   . GLY B 1 306 ? -91.791  39.736 -78.055 1.00 40.66 ? 306  GLY B N   1 
ATOM   4598 C CA  . GLY B 1 306 ? -92.880  40.511 -77.495 1.00 42.06 ? 306  GLY B CA  1 
ATOM   4599 C C   . GLY B 1 306 ? -94.229  40.013 -77.990 1.00 43.26 ? 306  GLY B C   1 
ATOM   4600 O O   . GLY B 1 306 ? -95.159  40.799 -78.155 1.00 43.33 ? 306  GLY B O   1 
ATOM   4601 N N   . GLU B 1 307 ? -94.338  38.707 -78.228 1.00 44.69 ? 307  GLU B N   1 
ATOM   4602 C CA  . GLU B 1 307 ? -95.590  38.116 -78.699 1.00 46.50 ? 307  GLU B CA  1 
ATOM   4603 C C   . GLU B 1 307 ? -96.313  37.332 -77.605 1.00 46.94 ? 307  GLU B C   1 
ATOM   4604 O O   . GLU B 1 307 ? -95.703  36.906 -76.618 1.00 44.71 ? 307  GLU B O   1 
ATOM   4605 C CB  . GLU B 1 307 ? -95.321  37.215 -79.907 1.00 47.83 ? 307  GLU B CB  1 
ATOM   4606 C CG  . GLU B 1 307 ? -94.633  37.976 -81.025 1.00 51.86 ? 307  GLU B CG  1 
ATOM   4607 C CD  . GLU B 1 307 ? -94.335  37.141 -82.247 1.00 53.20 ? 307  GLU B CD  1 
ATOM   4608 O OE1 . GLU B 1 307 ? -93.659  37.688 -83.148 1.00 54.49 ? 307  GLU B OE1 1 
ATOM   4609 O OE2 . GLU B 1 307 ? -94.770  35.963 -82.313 1.00 54.26 ? 307  GLU B OE2 1 
ATOM   4610 N N   . SER B 1 308 ? -97.618  37.147 -77.798 1.00 48.11 ? 308  SER B N   1 
ATOM   4611 C CA  . SER B 1 308 ? -98.457  36.434 -76.843 1.00 48.73 ? 308  SER B CA  1 
ATOM   4612 C C   . SER B 1 308 ? -97.933  35.050 -76.480 1.00 49.53 ? 308  SER B C   1 
ATOM   4613 O O   . SER B 1 308 ? -97.640  34.232 -77.349 1.00 48.52 ? 308  SER B O   1 
ATOM   4614 C CB  . SER B 1 308 ? -99.885  36.310 -77.381 1.00 47.87 ? 308  SER B CB  1 
ATOM   4615 O OG  . SER B 1 308 ? -100.695 35.551 -76.497 1.00 49.35 ? 308  SER B OG  1 
ATOM   4616 N N   . VAL B 1 309 ? -97.820  34.808 -75.179 1.00 50.27 ? 309  VAL B N   1 
ATOM   4617 C CA  . VAL B 1 309 ? -97.351  33.533 -74.652 1.00 50.90 ? 309  VAL B CA  1 
ATOM   4618 C C   . VAL B 1 309 ? -98.545  32.771 -74.074 1.00 51.75 ? 309  VAL B C   1 
ATOM   4619 O O   . VAL B 1 309 ? -98.465  31.574 -73.818 1.00 53.02 ? 309  VAL B O   1 
ATOM   4620 C CB  . VAL B 1 309 ? -96.294  33.754 -73.536 1.00 48.57 ? 309  VAL B CB  1 
ATOM   4621 C CG1 . VAL B 1 309 ? -95.896  32.431 -72.917 1.00 49.00 ? 309  VAL B CG1 1 
ATOM   4622 C CG2 . VAL B 1 309 ? -95.070  34.446 -74.107 1.00 46.55 ? 309  VAL B CG2 1 
ATOM   4623 N N   . SER B 1 310 ? -99.654  33.479 -73.886 1.00 52.04 ? 310  SER B N   1 
ATOM   4624 C CA  . SER B 1 310 ? -100.870 32.901 -73.321 1.00 52.89 ? 310  SER B CA  1 
ATOM   4625 C C   . SER B 1 310 ? -101.448 31.838 -74.249 1.00 53.03 ? 310  SER B C   1 
ATOM   4626 O O   . SER B 1 310 ? -102.210 30.969 -73.829 1.00 50.89 ? 310  SER B O   1 
ATOM   4627 C CB  . SER B 1 310 ? -101.905 34.008 -73.086 1.00 53.38 ? 310  SER B CB  1 
ATOM   4628 O OG  . SER B 1 310 ? -103.006 33.522 -72.344 1.00 56.33 ? 310  SER B OG  1 
ATOM   4629 N N   . TYR B 1 311 ? -101.071 31.937 -75.517 1.00 53.82 ? 311  TYR B N   1 
ATOM   4630 C CA  . TYR B 1 311 ? -101.495 31.016 -76.558 1.00 54.03 ? 311  TYR B CA  1 
ATOM   4631 C C   . TYR B 1 311 ? -101.105 29.587 -76.177 1.00 53.63 ? 311  TYR B C   1 
ATOM   4632 O O   . TYR B 1 311 ? -101.797 28.626 -76.507 1.00 52.53 ? 311  TYR B O   1 
ATOM   4633 C CB  . TYR B 1 311 ? -100.805 31.421 -77.859 1.00 59.22 ? 311  TYR B CB  1 
ATOM   4634 C CG  . TYR B 1 311 ? -100.940 30.436 -78.986 1.00 64.27 ? 311  TYR B CG  1 
ATOM   4635 C CD1 . TYR B 1 311 ? -102.119 30.347 -79.723 1.00 67.33 ? 311  TYR B CD1 1 
ATOM   4636 C CD2 . TYR B 1 311 ? -99.882  29.594 -79.325 1.00 66.47 ? 311  TYR B CD2 1 
ATOM   4637 C CE1 . TYR B 1 311 ? -102.241 29.445 -80.776 1.00 69.20 ? 311  TYR B CE1 1 
ATOM   4638 C CE2 . TYR B 1 311 ? -99.992  28.687 -80.371 1.00 69.06 ? 311  TYR B CE2 1 
ATOM   4639 C CZ  . TYR B 1 311 ? -101.174 28.619 -81.093 1.00 69.98 ? 311  TYR B CZ  1 
ATOM   4640 O OH  . TYR B 1 311 ? -101.288 27.726 -82.133 1.00 72.32 ? 311  TYR B OH  1 
ATOM   4641 N N   . LEU B 1 312 ? -99.989  29.463 -75.468 1.00 51.81 ? 312  LEU B N   1 
ATOM   4642 C CA  . LEU B 1 312 ? -99.471  28.170 -75.043 1.00 50.57 ? 312  LEU B CA  1 
ATOM   4643 C C   . LEU B 1 312 ? -100.246 27.511 -73.898 1.00 50.86 ? 312  LEU B C   1 
ATOM   4644 O O   . LEU B 1 312 ? -100.077 26.321 -73.644 1.00 48.52 ? 312  LEU B O   1 
ATOM   4645 C CB  . LEU B 1 312 ? -98.004  28.326 -74.638 1.00 48.17 ? 312  LEU B CB  1 
ATOM   4646 C CG  . LEU B 1 312 ? -97.059  28.813 -75.740 1.00 46.95 ? 312  LEU B CG  1 
ATOM   4647 C CD1 . LEU B 1 312 ? -95.690  29.114 -75.168 1.00 44.32 ? 312  LEU B CD1 1 
ATOM   4648 C CD2 . LEU B 1 312 ? -96.969  27.750 -76.819 1.00 46.98 ? 312  LEU B CD2 1 
ATOM   4649 N N   . PHE B 1 313 ? -101.092 28.275 -73.212 1.00 52.11 ? 313  PHE B N   1 
ATOM   4650 C CA  . PHE B 1 313 ? -101.856 27.730 -72.090 1.00 55.23 ? 313  PHE B CA  1 
ATOM   4651 C C   . PHE B 1 313 ? -102.911 26.714 -72.497 1.00 57.65 ? 313  PHE B C   1 
ATOM   4652 O O   . PHE B 1 313 ? -103.391 25.943 -71.667 1.00 58.80 ? 313  PHE B O   1 
ATOM   4653 C CB  . PHE B 1 313 ? -102.525 28.855 -71.293 1.00 52.57 ? 313  PHE B CB  1 
ATOM   4654 C CG  . PHE B 1 313 ? -101.556 29.783 -70.618 1.00 50.91 ? 313  PHE B CG  1 
ATOM   4655 C CD1 . PHE B 1 313 ? -100.183 29.552 -70.682 1.00 50.71 ? 313  PHE B CD1 1 
ATOM   4656 C CD2 . PHE B 1 313 ? -102.015 30.892 -69.922 1.00 50.93 ? 313  PHE B CD2 1 
ATOM   4657 C CE1 . PHE B 1 313 ? -99.283  30.417 -70.068 1.00 51.41 ? 313  PHE B CE1 1 
ATOM   4658 C CE2 . PHE B 1 313 ? -101.124 31.764 -69.303 1.00 51.79 ? 313  PHE B CE2 1 
ATOM   4659 C CZ  . PHE B 1 313 ? -99.751  31.525 -69.376 1.00 51.35 ? 313  PHE B CZ  1 
ATOM   4660 N N   . SER B 1 314 ? -103.271 26.708 -73.773 1.00 60.23 ? 314  SER B N   1 
ATOM   4661 C CA  . SER B 1 314 ? -104.276 25.776 -74.261 1.00 63.99 ? 314  SER B CA  1 
ATOM   4662 C C   . SER B 1 314 ? -103.971 25.381 -75.693 1.00 66.16 ? 314  SER B C   1 
ATOM   4663 O O   . SER B 1 314 ? -104.875 25.139 -76.486 1.00 67.89 ? 314  SER B O   1 
ATOM   4664 C CB  . SER B 1 314 ? -105.661 26.420 -74.191 1.00 64.61 ? 314  SER B CB  1 
ATOM   4665 O OG  . SER B 1 314 ? -105.706 27.597 -74.979 1.00 65.18 ? 314  SER B OG  1 
ATOM   4666 N N   . HIS B 1 315 ? -102.689 25.311 -76.020 1.00 69.29 ? 315  HIS B N   1 
ATOM   4667 C CA  . HIS B 1 315 ? -102.286 24.964 -77.370 1.00 72.86 ? 315  HIS B CA  1 
ATOM   4668 C C   . HIS B 1 315 ? -100.889 24.354 -77.351 1.00 73.85 ? 315  HIS B C   1 
ATOM   4669 O O   . HIS B 1 315 ? -99.947  24.950 -76.832 1.00 74.20 ? 315  HIS B O   1 
ATOM   4670 C CB  . HIS B 1 315 ? -102.301 26.223 -78.241 1.00 76.50 ? 315  HIS B CB  1 
ATOM   4671 C CG  . HIS B 1 315 ? -102.840 26.005 -79.620 1.00 79.84 ? 315  HIS B CG  1 
ATOM   4672 N ND1 . HIS B 1 315 ? -102.235 25.170 -80.535 1.00 81.34 ? 315  HIS B ND1 1 
ATOM   4673 C CD2 . HIS B 1 315 ? -103.928 26.520 -80.241 1.00 81.19 ? 315  HIS B CD2 1 
ATOM   4674 C CE1 . HIS B 1 315 ? -102.926 25.181 -81.662 1.00 81.90 ? 315  HIS B CE1 1 
ATOM   4675 N NE2 . HIS B 1 315 ? -103.957 25.992 -81.510 1.00 82.42 ? 315  HIS B NE2 1 
ATOM   4676 N N   . VAL B 1 316 ? -100.766 23.157 -77.910 1.00 74.99 ? 316  VAL B N   1 
ATOM   4677 C CA  . VAL B 1 316 ? -99.486  22.468 -77.966 1.00 75.47 ? 316  VAL B CA  1 
ATOM   4678 C C   . VAL B 1 316 ? -98.777  22.849 -79.258 1.00 75.43 ? 316  VAL B C   1 
ATOM   4679 O O   . VAL B 1 316 ? -99.162  22.405 -80.338 1.00 75.68 ? 316  VAL B O   1 
ATOM   4680 C CB  . VAL B 1 316 ? -99.675  20.938 -77.933 1.00 75.39 ? 316  VAL B CB  1 
ATOM   4681 C CG1 . VAL B 1 316 ? -98.323  20.243 -78.018 1.00 76.13 ? 316  VAL B CG1 1 
ATOM   4682 C CG2 . VAL B 1 316 ? -100.409 20.534 -76.663 1.00 75.50 ? 316  VAL B CG2 1 
ATOM   4683 N N   . PRO B 1 317 ? -97.724  23.675 -79.164 1.00 76.55 ? 317  PRO B N   1 
ATOM   4684 C CA  . PRO B 1 317 ? -96.990  24.092 -80.362 1.00 76.51 ? 317  PRO B CA  1 
ATOM   4685 C C   . PRO B 1 317 ? -96.388  22.912 -81.124 1.00 76.35 ? 317  PRO B C   1 
ATOM   4686 O O   . PRO B 1 317 ? -96.846  22.656 -82.259 1.00 75.77 ? 317  PRO B O   1 
ATOM   4687 C CB  . PRO B 1 317 ? -95.930  25.037 -79.800 1.00 75.85 ? 317  PRO B CB  1 
ATOM   4688 C CG  . PRO B 1 317 ? -95.653  24.450 -78.450 1.00 76.24 ? 317  PRO B CG  1 
ATOM   4689 C CD  . PRO B 1 317 ? -97.041  24.141 -77.943 1.00 75.92 ? 317  PRO B CD  1 
HETATM 4690 S S   . SO4 C 2 .   ? -120.560 34.271 -53.018 1.00 77.08 ? 1002 SO4 A S   1 
HETATM 4691 O O1  . SO4 C 2 .   ? -121.452 33.278 -53.646 1.00 77.80 ? 1002 SO4 A O1  1 
HETATM 4692 O O2  . SO4 C 2 .   ? -120.675 35.558 -53.727 1.00 77.27 ? 1002 SO4 A O2  1 
HETATM 4693 O O3  . SO4 C 2 .   ? -120.942 34.453 -51.607 1.00 77.53 ? 1002 SO4 A O3  1 
HETATM 4694 O O4  . SO4 C 2 .   ? -119.164 33.797 -53.086 1.00 77.61 ? 1002 SO4 A O4  1 
HETATM 4695 S S   . SO4 D 2 .   ? -94.299  32.892 -31.556 1.00 35.25 ? 1004 SO4 A S   1 
HETATM 4696 O O1  . SO4 D 2 .   ? -93.672  34.029 -30.851 1.00 33.94 ? 1004 SO4 A O1  1 
HETATM 4697 O O2  . SO4 D 2 .   ? -93.409  32.443 -32.640 1.00 33.80 ? 1004 SO4 A O2  1 
HETATM 4698 O O3  . SO4 D 2 .   ? -94.509  31.778 -30.618 1.00 32.06 ? 1004 SO4 A O3  1 
HETATM 4699 O O4  . SO4 D 2 .   ? -95.587  33.319 -32.116 1.00 28.88 ? 1004 SO4 A O4  1 
HETATM 4700 S S   . SO4 E 2 .   ? -100.181 29.548 -42.458 1.00 46.71 ? 1006 SO4 A S   1 
HETATM 4701 O O1  . SO4 E 2 .   ? -99.293  29.451 -41.289 1.00 48.07 ? 1006 SO4 A O1  1 
HETATM 4702 O O2  . SO4 E 2 .   ? -100.170 30.935 -42.969 1.00 46.89 ? 1006 SO4 A O2  1 
HETATM 4703 O O3  . SO4 E 2 .   ? -99.730  28.605 -43.498 1.00 46.23 ? 1006 SO4 A O3  1 
HETATM 4704 O O4  . SO4 E 2 .   ? -101.560 29.193 -42.071 1.00 50.11 ? 1006 SO4 A O4  1 
HETATM 4705 S S   . SO4 F 2 .   ? -94.642  11.981 -52.664 1.00 58.33 ? 1001 SO4 B S   1 
HETATM 4706 O O1  . SO4 F 2 .   ? -94.926  10.755 -51.887 1.00 56.01 ? 1001 SO4 B O1  1 
HETATM 4707 O O2  . SO4 F 2 .   ? -94.413  11.640 -54.083 1.00 54.63 ? 1001 SO4 B O2  1 
HETATM 4708 O O3  . SO4 F 2 .   ? -95.798  12.891 -52.574 1.00 58.67 ? 1001 SO4 B O3  1 
HETATM 4709 O O4  . SO4 F 2 .   ? -93.448  12.650 -52.107 1.00 55.47 ? 1001 SO4 B O4  1 
HETATM 4710 S S   . SO4 G 2 .   ? -99.581  37.431 -73.315 1.00 30.16 ? 1003 SO4 B S   1 
HETATM 4711 O O1  . SO4 G 2 .   ? -98.944  36.183 -72.876 1.00 27.69 ? 1003 SO4 B O1  1 
HETATM 4712 O O2  . SO4 G 2 .   ? -98.586  38.293 -73.969 1.00 29.81 ? 1003 SO4 B O2  1 
HETATM 4713 O O3  . SO4 G 2 .   ? -100.652 37.114 -74.268 1.00 29.69 ? 1003 SO4 B O3  1 
HETATM 4714 O O4  . SO4 G 2 .   ? -100.149 38.129 -72.153 1.00 29.72 ? 1003 SO4 B O4  1 
HETATM 4715 S S   . SO4 H 2 .   ? -101.753 31.061 -62.726 1.00 42.27 ? 1005 SO4 B S   1 
HETATM 4716 O O1  . SO4 H 2 .   ? -101.596 29.604 -62.832 1.00 44.91 ? 1005 SO4 B O1  1 
HETATM 4717 O O2  . SO4 H 2 .   ? -100.458 31.626 -62.338 1.00 42.59 ? 1005 SO4 B O2  1 
HETATM 4718 O O3  . SO4 H 2 .   ? -102.179 31.644 -64.011 1.00 44.49 ? 1005 SO4 B O3  1 
HETATM 4719 O O4  . SO4 H 2 .   ? -102.768 31.367 -61.697 1.00 42.78 ? 1005 SO4 B O4  1 
HETATM 4720 O O   . HOH I 3 .   ? -96.654  48.167 -33.876 1.00 18.24 ? 1007 HOH A O   1 
HETATM 4721 O O   . HOH I 3 .   ? -97.897  31.278 -44.377 1.00 23.83 ? 1008 HOH A O   1 
HETATM 4722 O O   . HOH I 3 .   ? -118.970 10.125 -53.419 1.00 40.33 ? 1009 HOH A O   1 
HETATM 4723 O O   . HOH I 3 .   ? -95.818  61.893 -32.867 1.00 21.93 ? 1010 HOH A O   1 
HETATM 4724 O O   . HOH I 3 .   ? -93.743  37.659 -44.165 1.00 33.63 ? 1011 HOH A O   1 
HETATM 4725 O O   . HOH I 3 .   ? -105.787 26.909 -29.368 1.00 42.04 ? 1012 HOH A O   1 
HETATM 4726 O O   . HOH I 3 .   ? -107.768 37.890 -43.665 1.00 21.80 ? 1013 HOH A O   1 
HETATM 4727 O O   . HOH I 3 .   ? -91.433  63.195 -36.834 1.00 29.88 ? 1014 HOH A O   1 
HETATM 4728 O O   . HOH I 3 .   ? -92.992  43.887 -46.863 1.00 32.76 ? 1015 HOH A O   1 
HETATM 4729 O O   . HOH I 3 .   ? -99.888  38.013 -67.021 1.00 27.18 ? 1016 HOH A O   1 
HETATM 4730 O O   . HOH I 3 .   ? -96.248  34.069 -37.450 1.00 35.36 ? 1017 HOH A O   1 
HETATM 4731 O O   . HOH I 3 .   ? -110.992 59.265 -31.825 1.00 36.33 ? 1018 HOH A O   1 
HETATM 4732 O O   . HOH I 3 .   ? -96.751  46.132 -56.537 1.00 24.28 ? 1019 HOH A O   1 
HETATM 4733 O O   . HOH I 3 .   ? -108.374 36.652 -46.187 1.00 34.67 ? 1020 HOH A O   1 
HETATM 4734 O O   . HOH I 3 .   ? -104.160 53.834 -27.200 1.00 30.61 ? 1021 HOH A O   1 
HETATM 4735 O O   . HOH I 3 .   ? -94.854  32.681 -35.645 1.00 49.45 ? 1022 HOH A O   1 
HETATM 4736 O O   . HOH I 3 .   ? -97.414  62.889 -39.080 1.00 33.13 ? 1023 HOH A O   1 
HETATM 4737 O O   . HOH I 3 .   ? -98.593  33.195 -38.681 1.00 28.16 ? 1024 HOH A O   1 
HETATM 4738 O O   . HOH I 3 .   ? -93.360  58.045 -46.377 1.00 45.52 ? 1025 HOH A O   1 
HETATM 4739 O O   . HOH I 3 .   ? -94.573  43.173 -49.864 1.00 28.04 ? 1026 HOH A O   1 
HETATM 4740 O O   . HOH I 3 .   ? -109.355 51.588 -42.226 1.00 39.81 ? 1027 HOH A O   1 
HETATM 4741 O O   . HOH I 3 .   ? -98.272  35.727 -67.392 1.00 37.08 ? 1028 HOH A O   1 
HETATM 4742 O O   . HOH I 3 .   ? -92.602  48.747 -44.308 1.00 31.59 ? 1029 HOH A O   1 
HETATM 4743 O O   . HOH I 3 .   ? -111.785 57.066 -46.308 1.00 34.87 ? 1030 HOH A O   1 
HETATM 4744 O O   . HOH I 3 .   ? -91.086  56.459 -37.811 1.00 31.03 ? 1031 HOH A O   1 
HETATM 4745 O O   . HOH I 3 .   ? -92.403  36.559 -46.194 1.00 32.85 ? 1032 HOH A O   1 
HETATM 4746 O O   . HOH I 3 .   ? -106.498 38.242 -59.411 1.00 38.57 ? 1033 HOH A O   1 
HETATM 4747 O O   . HOH I 3 .   ? -105.173 31.121 -43.641 1.00 27.61 ? 1034 HOH A O   1 
HETATM 4748 O O   . HOH I 3 .   ? -108.775 55.603 -32.736 1.00 34.52 ? 1035 HOH A O   1 
HETATM 4749 O O   . HOH I 3 .   ? -109.416 28.898 -39.169 1.00 36.03 ? 1036 HOH A O   1 
HETATM 4750 O O   . HOH I 3 .   ? -101.619 26.759 -43.761 1.00 45.03 ? 1037 HOH A O   1 
HETATM 4751 O O   . HOH I 3 .   ? -104.356 50.211 -18.415 1.00 29.15 ? 1038 HOH A O   1 
HETATM 4752 O O   . HOH I 3 .   ? -114.930 12.068 -45.294 1.00 43.64 ? 1039 HOH A O   1 
HETATM 4753 O O   . HOH I 3 .   ? -99.217  30.809 -38.942 1.00 31.42 ? 1040 HOH A O   1 
HETATM 4754 O O   . HOH I 3 .   ? -114.752 33.276 -29.344 1.00 41.62 ? 1041 HOH A O   1 
HETATM 4755 O O   . HOH I 3 .   ? -111.029 57.784 -27.337 1.00 47.02 ? 1042 HOH A O   1 
HETATM 4756 O O   . HOH I 3 .   ? -111.315 40.120 -49.313 1.00 50.68 ? 1043 HOH A O   1 
HETATM 4757 O O   . HOH I 3 .   ? -135.344 25.171 -35.996 1.00 55.72 ? 1044 HOH A O   1 
HETATM 4758 O O   . HOH I 3 .   ? -133.000 13.226 -44.585 1.00 42.00 ? 1045 HOH A O   1 
HETATM 4759 O O   . HOH I 3 .   ? -117.142 11.291 -47.091 1.00 50.26 ? 1046 HOH A O   1 
HETATM 4760 O O   . HOH I 3 .   ? -104.207 28.249 -47.236 1.00 43.31 ? 1047 HOH A O   1 
HETATM 4761 O O   . HOH I 3 .   ? -88.208  61.131 -32.615 1.00 35.24 ? 1048 HOH A O   1 
HETATM 4762 O O   . HOH I 3 .   ? -118.540 59.006 -46.069 1.00 49.28 ? 1049 HOH A O   1 
HETATM 4763 O O   . HOH I 3 .   ? -117.058 38.570 -40.228 1.00 40.24 ? 1050 HOH A O   1 
HETATM 4764 O O   . HOH I 3 .   ? -103.160 25.515 -29.710 1.00 48.38 ? 1051 HOH A O   1 
HETATM 4765 O O   . HOH I 3 .   ? -128.607 24.432 -33.883 1.00 57.42 ? 1052 HOH A O   1 
HETATM 4766 O O   . HOH I 3 .   ? -99.815  64.324 -27.362 1.00 42.81 ? 1053 HOH A O   1 
HETATM 4767 O O   . HOH I 3 .   ? -120.997 31.836 -51.101 1.00 43.60 ? 1054 HOH A O   1 
HETATM 4768 O O   . HOH I 3 .   ? -115.464 42.173 -22.807 1.00 44.28 ? 1055 HOH A O   1 
HETATM 4769 O O   . HOH I 3 .   ? -119.487 39.538 -27.114 1.00 47.97 ? 1056 HOH A O   1 
HETATM 4770 O O   . HOH I 3 .   ? -116.902 68.425 -50.403 1.00 50.67 ? 1057 HOH A O   1 
HETATM 4771 O O   . HOH I 3 .   ? -107.010 29.256 -28.178 1.00 48.67 ? 1058 HOH A O   1 
HETATM 4772 O O   . HOH I 3 .   ? -105.224 28.054 -26.787 1.00 51.24 ? 1059 HOH A O   1 
HETATM 4773 O O   . HOH I 3 .   ? -109.949 30.096 -26.834 1.00 48.42 ? 1060 HOH A O   1 
HETATM 4774 O O   . HOH I 3 .   ? -112.800 28.896 -40.940 1.00 54.94 ? 1061 HOH A O   1 
HETATM 4775 O O   . HOH J 3 .   ? -104.037 15.923 -47.818 1.00 36.12 ? 1006 HOH B O   1 
HETATM 4776 O O   . HOH J 3 .   ? -100.490 33.475 -60.577 1.00 23.59 ? 1007 HOH B O   1 
HETATM 4777 O O   . HOH J 3 .   ? -70.567  45.537 -68.271 1.00 23.67 ? 1008 HOH B O   1 
HETATM 4778 O O   . HOH J 3 .   ? -84.035  37.888 -71.044 1.00 22.66 ? 1009 HOH B O   1 
HETATM 4779 O O   . HOH J 3 .   ? -70.880  41.108 -72.000 1.00 23.06 ? 1010 HOH B O   1 
HETATM 4780 O O   . HOH J 3 .   ? -89.215  38.811 -54.723 1.00 24.67 ? 1011 HOH B O   1 
HETATM 4781 O O   . HOH J 3 .   ? -90.107  16.173 -64.826 1.00 21.47 ? 1012 HOH B O   1 
HETATM 4782 O O   . HOH J 3 .   ? -117.078 11.767 -59.058 1.00 36.09 ? 1013 HOH B O   1 
HETATM 4783 O O   . HOH J 3 .   ? -98.379  33.552 -66.087 1.00 25.72 ? 1014 HOH B O   1 
HETATM 4784 O O   . HOH J 3 .   ? -84.217  41.882 -60.530 1.00 23.88 ? 1015 HOH B O   1 
HETATM 4785 O O   . HOH J 3 .   ? -96.160  37.834 -62.858 1.00 23.70 ? 1016 HOH B O   1 
HETATM 4786 O O   . HOH J 3 .   ? -90.412  22.013 -53.163 1.00 23.67 ? 1017 HOH B O   1 
HETATM 4787 O O   . HOH J 3 .   ? -119.885 4.899  -66.682 1.00 40.72 ? 1018 HOH B O   1 
HETATM 4788 O O   . HOH J 3 .   ? -94.590  36.167 -42.047 1.00 31.63 ? 1019 HOH B O   1 
HETATM 4789 O O   . HOH J 3 .   ? -95.015  22.149 -59.012 1.00 32.32 ? 1020 HOH B O   1 
HETATM 4790 O O   . HOH J 3 .   ? -73.372  39.921 -81.833 1.00 44.20 ? 1021 HOH B O   1 
HETATM 4791 O O   . HOH J 3 .   ? -63.780  31.683 -51.612 1.00 28.37 ? 1022 HOH B O   1 
HETATM 4792 O O   . HOH J 3 .   ? -117.774 10.171 -68.030 1.00 40.43 ? 1023 HOH B O   1 
HETATM 4793 O O   . HOH J 3 .   ? -89.069  40.688 -58.065 1.00 34.09 ? 1024 HOH B O   1 
HETATM 4794 O O   . HOH J 3 .   ? -80.628  30.666 -86.425 1.00 28.42 ? 1025 HOH B O   1 
HETATM 4795 O O   . HOH J 3 .   ? -94.866  38.791 -60.737 1.00 28.68 ? 1026 HOH B O   1 
HETATM 4796 O O   . HOH J 3 .   ? -91.972  26.413 -45.897 1.00 36.42 ? 1027 HOH B O   1 
HETATM 4797 O O   . HOH J 3 .   ? -91.809  8.754  -47.770 1.00 42.72 ? 1028 HOH B O   1 
HETATM 4798 O O   . HOH J 3 .   ? -74.512  27.290 -71.944 1.00 25.27 ? 1029 HOH B O   1 
HETATM 4799 O O   . HOH J 3 .   ? -113.061 7.025  -74.826 1.00 32.74 ? 1030 HOH B O   1 
HETATM 4800 O O   . HOH J 3 .   ? -92.293  44.096 -52.995 1.00 36.66 ? 1031 HOH B O   1 
HETATM 4801 O O   . HOH J 3 .   ? -85.885  37.181 -48.177 1.00 23.09 ? 1032 HOH B O   1 
HETATM 4802 O O   . HOH J 3 .   ? -96.401  42.775 -57.969 1.00 42.82 ? 1033 HOH B O   1 
HETATM 4803 O O   . HOH J 3 .   ? -69.427  39.517 -65.813 1.00 32.24 ? 1034 HOH B O   1 
HETATM 4804 O O   . HOH J 3 .   ? -84.538  17.947 -68.249 1.00 36.92 ? 1035 HOH B O   1 
HETATM 4805 O O   . HOH J 3 .   ? -93.708  32.671 -38.048 1.00 26.75 ? 1036 HOH B O   1 
HETATM 4806 O O   . HOH J 3 .   ? -92.260  25.153 -61.471 1.00 23.78 ? 1037 HOH B O   1 
HETATM 4807 O O   . HOH J 3 .   ? -85.601  22.648 -59.288 1.00 40.09 ? 1038 HOH B O   1 
HETATM 4808 O O   . HOH J 3 .   ? -100.845 22.318 -66.229 1.00 34.37 ? 1039 HOH B O   1 
HETATM 4809 O O   . HOH J 3 .   ? -77.397  31.263 -77.548 1.00 31.81 ? 1040 HOH B O   1 
HETATM 4810 O O   . HOH J 3 .   ? -96.918  29.909 -37.779 1.00 32.24 ? 1041 HOH B O   1 
HETATM 4811 O O   . HOH J 3 .   ? -98.975  21.787 -72.409 1.00 31.12 ? 1042 HOH B O   1 
HETATM 4812 O O   . HOH J 3 .   ? -86.091  12.340 -62.060 1.00 28.68 ? 1043 HOH B O   1 
HETATM 4813 O O   . HOH J 3 .   ? -102.256 26.909 -57.508 1.00 35.07 ? 1044 HOH B O   1 
HETATM 4814 O O   . HOH J 3 .   ? -75.532  23.966 -78.587 1.00 34.25 ? 1045 HOH B O   1 
HETATM 4815 O O   . HOH J 3 .   ? -99.643  26.539 -61.228 1.00 28.97 ? 1046 HOH B O   1 
HETATM 4816 O O   . HOH J 3 .   ? -116.743 12.617 -71.538 1.00 41.17 ? 1047 HOH B O   1 
HETATM 4817 O O   . HOH J 3 .   ? -93.558  14.199 -76.037 1.00 35.69 ? 1048 HOH B O   1 
HETATM 4818 O O   . HOH J 3 .   ? -93.283  24.413 -58.612 1.00 29.34 ? 1049 HOH B O   1 
HETATM 4819 O O   . HOH J 3 .   ? -97.651  41.698 -77.458 1.00 35.10 ? 1050 HOH B O   1 
HETATM 4820 O O   . HOH J 3 .   ? -91.229  41.046 -54.233 1.00 37.23 ? 1051 HOH B O   1 
HETATM 4821 O O   . HOH J 3 .   ? -67.847  23.774 -68.388 1.00 43.20 ? 1052 HOH B O   1 
HETATM 4822 O O   . HOH J 3 .   ? -101.951 3.294  -72.377 1.00 41.41 ? 1053 HOH B O   1 
HETATM 4823 O O   . HOH J 3 .   ? -78.257  25.664 -62.849 1.00 34.58 ? 1054 HOH B O   1 
HETATM 4824 O O   . HOH J 3 .   ? -105.410 22.551 -56.770 1.00 33.65 ? 1055 HOH B O   1 
HETATM 4825 O O   . HOH J 3 .   ? -77.930  34.916 -81.468 1.00 41.41 ? 1056 HOH B O   1 
HETATM 4826 O O   . HOH J 3 .   ? -70.637  26.010 -73.120 1.00 43.23 ? 1057 HOH B O   1 
HETATM 4827 O O   . HOH J 3 .   ? -91.338  22.747 -58.026 1.00 36.01 ? 1058 HOH B O   1 
HETATM 4828 O O   . HOH J 3 .   ? -98.246  18.190 -54.879 1.00 43.64 ? 1059 HOH B O   1 
HETATM 4829 O O   . HOH J 3 .   ? -98.293  26.235 -71.241 1.00 37.19 ? 1060 HOH B O   1 
HETATM 4830 O O   . HOH J 3 .   ? -95.791  29.225 -35.089 1.00 49.36 ? 1061 HOH B O   1 
HETATM 4831 O O   . HOH J 3 .   ? -96.150  39.933 -58.481 1.00 39.02 ? 1062 HOH B O   1 
HETATM 4832 O O   . HOH J 3 .   ? -103.766 17.132 -58.099 1.00 36.32 ? 1063 HOH B O   1 
HETATM 4833 O O   . HOH J 3 .   ? -67.739  37.748 -77.687 1.00 43.97 ? 1064 HOH B O   1 
HETATM 4834 O O   . HOH J 3 .   ? -89.998  22.062 -56.077 1.00 41.35 ? 1065 HOH B O   1 
HETATM 4835 O O   . HOH J 3 .   ? -76.276  40.456 -59.205 1.00 37.67 ? 1066 HOH B O   1 
HETATM 4836 O O   . HOH J 3 .   ? -99.541  36.987 -69.303 1.00 47.47 ? 1067 HOH B O   1 
HETATM 4837 O O   . HOH J 3 .   ? -92.202  41.599 -50.757 1.00 43.44 ? 1068 HOH B O   1 
HETATM 4838 O O   . HOH J 3 .   ? -87.059  0.728  -69.008 1.00 46.04 ? 1069 HOH B O   1 
HETATM 4839 O O   . HOH J 3 .   ? -99.942  17.740 -63.889 1.00 44.24 ? 1070 HOH B O   1 
HETATM 4840 O O   . HOH J 3 .   ? -99.176  11.237 -77.521 1.00 47.80 ? 1071 HOH B O   1 
HETATM 4841 O O   . HOH J 3 .   ? -83.430  19.209 -61.722 1.00 47.29 ? 1072 HOH B O   1 
HETATM 4842 O O   . HOH J 3 .   ? -102.199 15.075 -44.443 1.00 57.52 ? 1073 HOH B O   1 
HETATM 4843 O O   . HOH J 3 .   ? -98.816  15.293 -75.247 1.00 39.28 ? 1074 HOH B O   1 
HETATM 4844 O O   . HOH J 3 .   ? -103.490 -0.318 -63.032 1.00 34.42 ? 1075 HOH B O   1 
HETATM 4845 O O   . HOH J 3 .   ? -82.449  10.036 -54.690 1.00 42.84 ? 1076 HOH B O   1 
HETATM 4846 O O   . HOH J 3 .   ? -107.211 6.873  -77.272 1.00 52.84 ? 1077 HOH B O   1 
HETATM 4847 O O   . HOH J 3 .   ? -72.700  24.551 -73.813 1.00 64.65 ? 1078 HOH B O   1 
HETATM 4848 O O   . HOH J 3 .   ? -94.979  44.342 -59.206 1.00 46.34 ? 1079 HOH B O   1 
HETATM 4849 O O   . HOH J 3 .   ? -91.412  47.880 -57.686 1.00 60.22 ? 1080 HOH B O   1 
HETATM 4850 O O   . HOH J 3 .   ? -92.838  14.079 -49.813 1.00 54.75 ? 1081 HOH B O   1 
HETATM 4851 O O   . HOH J 3 .   ? -96.809  10.555 -54.320 1.00 48.05 ? 1082 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 ALA 132 132 132 ALA ALA 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 ALA 132 132 132 ALA ALA 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 
# 
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 3    HOH HOH A . 
I 3 HOH 2  1008 4    HOH HOH A . 
I 3 HOH 3  1009 11   HOH HOH A . 
I 3 HOH 4  1010 12   HOH HOH A . 
I 3 HOH 5  1011 20   HOH HOH A . 
I 3 HOH 6  1012 22   HOH HOH A . 
I 3 HOH 7  1013 23   HOH HOH A . 
I 3 HOH 8  1014 26   HOH HOH A . 
I 3 HOH 9  1015 28   HOH HOH A . 
I 3 HOH 10 1016 29   HOH HOH A . 
I 3 HOH 11 1017 30   HOH HOH A . 
I 3 HOH 12 1018 36   HOH HOH A . 
I 3 HOH 13 1019 39   HOH HOH A . 
I 3 HOH 14 1020 40   HOH HOH A . 
I 3 HOH 15 1021 48   HOH HOH A . 
I 3 HOH 16 1022 51   HOH HOH A . 
I 3 HOH 17 1023 53   HOH HOH A . 
I 3 HOH 18 1024 54   HOH HOH A . 
I 3 HOH 19 1025 56   HOH HOH A . 
I 3 HOH 20 1026 58   HOH HOH A . 
I 3 HOH 21 1027 59   HOH HOH A . 
I 3 HOH 22 1028 61   HOH HOH A . 
I 3 HOH 23 1029 62   HOH HOH A . 
I 3 HOH 24 1030 65   HOH HOH A . 
I 3 HOH 25 1031 68   HOH HOH A . 
I 3 HOH 26 1032 69   HOH HOH A . 
I 3 HOH 27 1033 70   HOH HOH A . 
I 3 HOH 28 1034 72   HOH HOH A . 
I 3 HOH 29 1035 76   HOH HOH A . 
I 3 HOH 30 1036 77   HOH HOH A . 
I 3 HOH 31 1037 80   HOH HOH A . 
I 3 HOH 32 1038 83   HOH HOH A . 
I 3 HOH 33 1039 85   HOH HOH A . 
I 3 HOH 34 1040 92   HOH HOH A . 
I 3 HOH 35 1041 94   HOH HOH A . 
I 3 HOH 36 1042 97   HOH HOH A . 
I 3 HOH 37 1043 100  HOH HOH A . 
I 3 HOH 38 1044 103  HOH HOH A . 
I 3 HOH 39 1045 104  HOH HOH A . 
I 3 HOH 40 1046 105  HOH HOH A . 
I 3 HOH 41 1047 109  HOH HOH A . 
I 3 HOH 42 1048 110  HOH HOH A . 
I 3 HOH 43 1049 112  HOH HOH A . 
I 3 HOH 44 1050 114  HOH HOH A . 
I 3 HOH 45 1051 115  HOH HOH A . 
I 3 HOH 46 1052 118  HOH HOH A . 
I 3 HOH 47 1053 119  HOH HOH A . 
I 3 HOH 48 1054 120  HOH HOH A . 
I 3 HOH 49 1055 121  HOH HOH A . 
I 3 HOH 50 1056 122  HOH HOH A . 
I 3 HOH 51 1057 123  HOH HOH A . 
I 3 HOH 52 1058 124  HOH HOH A . 
I 3 HOH 53 1059 125  HOH HOH A . 
I 3 HOH 54 1060 126  HOH HOH A . 
I 3 HOH 55 1061 130  HOH HOH A . 
J 3 HOH 1  1006 1    HOH HOH B . 
J 3 HOH 2  1007 2    HOH HOH B . 
J 3 HOH 3  1008 5    HOH HOH B . 
J 3 HOH 4  1009 6    HOH HOH B . 
J 3 HOH 5  1010 7    HOH HOH B . 
J 3 HOH 6  1011 8    HOH HOH B . 
J 3 HOH 7  1012 9    HOH HOH B . 
J 3 HOH 8  1013 10   HOH HOH B . 
J 3 HOH 9  1014 13   HOH HOH B . 
J 3 HOH 10 1015 14   HOH HOH B . 
J 3 HOH 11 1016 15   HOH HOH B . 
J 3 HOH 12 1017 16   HOH HOH B . 
J 3 HOH 13 1018 17   HOH HOH B . 
J 3 HOH 14 1019 18   HOH HOH B . 
J 3 HOH 15 1020 19   HOH HOH B . 
J 3 HOH 16 1021 21   HOH HOH B . 
J 3 HOH 17 1022 24   HOH HOH B . 
J 3 HOH 18 1023 25   HOH HOH B . 
J 3 HOH 19 1024 27   HOH HOH B . 
J 3 HOH 20 1025 31   HOH HOH B . 
J 3 HOH 21 1026 32   HOH HOH B . 
J 3 HOH 22 1027 33   HOH HOH B . 
J 3 HOH 23 1028 34   HOH HOH B . 
J 3 HOH 24 1029 35   HOH HOH B . 
J 3 HOH 25 1030 37   HOH HOH B . 
J 3 HOH 26 1031 38   HOH HOH B . 
J 3 HOH 27 1032 41   HOH HOH B . 
J 3 HOH 28 1033 42   HOH HOH B . 
J 3 HOH 29 1034 43   HOH HOH B . 
J 3 HOH 30 1035 44   HOH HOH B . 
J 3 HOH 31 1036 45   HOH HOH B . 
J 3 HOH 32 1037 46   HOH HOH B . 
J 3 HOH 33 1038 47   HOH HOH B . 
J 3 HOH 34 1039 49   HOH HOH B . 
J 3 HOH 35 1040 50   HOH HOH B . 
J 3 HOH 36 1041 52   HOH HOH B . 
J 3 HOH 37 1042 55   HOH HOH B . 
J 3 HOH 38 1043 57   HOH HOH B . 
J 3 HOH 39 1044 60   HOH HOH B . 
J 3 HOH 40 1045 63   HOH HOH B . 
J 3 HOH 41 1046 64   HOH HOH B . 
J 3 HOH 42 1047 66   HOH HOH B . 
J 3 HOH 43 1048 67   HOH HOH B . 
J 3 HOH 44 1049 71   HOH HOH B . 
J 3 HOH 45 1050 73   HOH HOH B . 
J 3 HOH 46 1051 74   HOH HOH B . 
J 3 HOH 47 1052 75   HOH HOH B . 
J 3 HOH 48 1053 78   HOH HOH B . 
J 3 HOH 49 1054 79   HOH HOH B . 
J 3 HOH 50 1055 81   HOH HOH B . 
J 3 HOH 51 1056 82   HOH HOH B . 
J 3 HOH 52 1057 84   HOH HOH B . 
J 3 HOH 53 1058 86   HOH HOH B . 
J 3 HOH 54 1059 87   HOH HOH B . 
J 3 HOH 55 1060 88   HOH HOH B . 
J 3 HOH 56 1061 89   HOH HOH B . 
J 3 HOH 57 1062 90   HOH HOH B . 
J 3 HOH 58 1063 91   HOH HOH B . 
J 3 HOH 59 1064 93   HOH HOH B . 
J 3 HOH 60 1065 95   HOH HOH B . 
J 3 HOH 61 1066 96   HOH HOH B . 
J 3 HOH 62 1067 98   HOH HOH B . 
J 3 HOH 63 1068 99   HOH HOH B . 
J 3 HOH 64 1069 101  HOH HOH B . 
J 3 HOH 65 1070 102  HOH HOH B . 
J 3 HOH 66 1071 106  HOH HOH B . 
J 3 HOH 67 1072 107  HOH HOH B . 
J 3 HOH 68 1073 108  HOH HOH B . 
J 3 HOH 69 1074 111  HOH HOH B . 
J 3 HOH 70 1075 113  HOH HOH B . 
J 3 HOH 71 1076 116  HOH HOH B . 
J 3 HOH 72 1077 117  HOH HOH B . 
J 3 HOH 73 1078 127  HOH HOH B . 
J 3 HOH 74 1079 128  HOH HOH B . 
J 3 HOH 75 1080 129  HOH HOH B . 
J 3 HOH 76 1081 131  HOH HOH B . 
J 3 HOH 77 1082 132  HOH HOH B . 
# 
_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)' 28690 ? 
1 MORE         -451  ? 
1 'SSA (A^2)'  59960 ? 
# 
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_565 -y,x-y+1,z  -0.5000000000 -0.8660254038 0.0000000000 -85.1695000000  0.8660254038  
-0.5000000000 0.0000000000 147.5179012552 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_455 -x+y-1,-x,z -0.5000000000 0.8660254038  0.0000000000 -170.3390000000 -0.8660254038 
-0.5000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2006-10-24 
2 'Structure model' 1 1 2008-05-01 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2021-11-10 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Derived calculations'      
3 3 'Structure model' 'Version format compliance' 
4 4 'Structure model' 'Database references'       
5 4 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' database_2         
2 4 'Structure model' struct_ref_seq_dif 
3 4 'Structure model' struct_site        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_database_2.pdbx_DOI'                
2 4 'Structure model' '_database_2.pdbx_database_accession' 
3 4 'Structure model' '_struct_ref_seq_dif.details'         
4 4 'Structure model' '_struct_site.pdbx_auth_asym_id'      
5 4 'Structure model' '_struct_site.pdbx_auth_comp_id'      
6 4 'Structure model' '_struct_site.pdbx_auth_seq_id'       
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNS          refinement       1.1            ? 1 
CrystalClear 'data reduction' '(MSC/RIGAKU)' ? 2 
d*TREK       '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  ? ? 41.60   -174.27 
2  1 GLN A 13  ? ? -159.46 -3.12   
3  1 PHE A 35  ? ? -72.12  -164.69 
4  1 SER A 36  ? ? -36.70  -82.18  
5  1 ASN A 37  ? ? -97.17  46.70   
6  1 CYS A 60  ? ? -91.66  48.75   
7  1 GLU A 62  ? ? -56.38  95.99   
8  1 ILE A 107 ? ? -107.79 73.14   
9  1 ASP A 128 ? ? 42.30   70.79   
10 1 ASN A 186 ? ? 70.05   40.60   
11 1 GLU A 195 ? ? -48.55  94.40   
12 1 ASP A 224 ? ? -108.21 -87.27  
13 1 ILE A 252 ? ? -81.00  30.09   
14 1 PHE A 253 ? ? -37.89  111.95  
15 1 ALA A 257 ? ? -18.95  -69.12  
16 1 CYS A 265 ? ? -66.36  18.52   
17 1 ASP B 14  ? ? -13.86  -85.56  
18 1 TYR B 94  ? ? 56.68   14.98   
19 1 ILE B 107 ? ? -102.74 70.23   
20 1 ASN B 186 ? ? 71.85   53.02   
21 1 ASP B 224 ? ? -107.26 -95.54  
22 1 CYS B 265 ? ? -84.15  43.49   
23 1 ASN B 273 ? ? -99.73  31.80   
24 1 SER B 314 ? ? -147.37 33.31   
# 
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 
# 
