data_2H08
# 
_entry.id   2H08 
# 
_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   2H08         pdb_00002h08 10.2210/pdb2h08/pdb 
RCSB  RCSB037766   ?            ?                   
WWPDB D_1000037766 ?            ?                   
# 
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 2H07 'the same protein(S132A)'     unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2H08 
_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           2H08 
_cell.length_a           169.914 
_cell.length_b           169.914 
_cell.length_c           61.706 
_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                         2H08 
_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' 35918.395 2   2.7.6.1 Y146M ? ? 
2 non-polymer syn 'SULFATE ION'                          96.063    6   ?       ?     ? ? 
3 water       nat water                                  18.015    164 ?       ?     ? ? 
# 
_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
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLMAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLMAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   ASN n 
1 4   ILE n 
1 5   LYS n 
1 6   ILE n 
1 7   PHE n 
1 8   SER n 
1 9   GLY n 
1 10  SER n 
1 11  SER n 
1 12  HIS n 
1 13  GLN n 
1 14  ASP n 
1 15  LEU n 
1 16  SER n 
1 17  GLN n 
1 18  LYS n 
1 19  ILE n 
1 20  ALA n 
1 21  ASP n 
1 22  ARG n 
1 23  LEU n 
1 24  GLY n 
1 25  LEU n 
1 26  GLU n 
1 27  LEU n 
1 28  GLY n 
1 29  LYS n 
1 30  VAL n 
1 31  VAL n 
1 32  THR n 
1 33  LYS n 
1 34  LYS n 
1 35  PHE n 
1 36  SER n 
1 37  ASN n 
1 38  GLN n 
1 39  GLU n 
1 40  THR n 
1 41  CYS n 
1 42  VAL n 
1 43  GLU n 
1 44  ILE n 
1 45  GLY n 
1 46  GLU n 
1 47  SER n 
1 48  VAL n 
1 49  ARG n 
1 50  GLY n 
1 51  GLU n 
1 52  ASP n 
1 53  VAL n 
1 54  TYR n 
1 55  ILE n 
1 56  VAL n 
1 57  GLN n 
1 58  SER n 
1 59  GLY n 
1 60  CYS n 
1 61  GLY n 
1 62  GLU n 
1 63  ILE n 
1 64  ASN n 
1 65  ASP n 
1 66  ASN n 
1 67  LEU n 
1 68  MET n 
1 69  GLU n 
1 70  LEU n 
1 71  LEU n 
1 72  ILE n 
1 73  MET n 
1 74  ILE n 
1 75  ASN n 
1 76  ALA n 
1 77  CYS n 
1 78  LYS n 
1 79  ILE n 
1 80  ALA n 
1 81  SER n 
1 82  ALA n 
1 83  SER n 
1 84  ARG n 
1 85  VAL n 
1 86  THR n 
1 87  ALA n 
1 88  VAL n 
1 89  ILE n 
1 90  PRO n 
1 91  CYS n 
1 92  PHE n 
1 93  PRO n 
1 94  TYR n 
1 95  ALA n 
1 96  ARG n 
1 97  GLN n 
1 98  ASP n 
1 99  LYS n 
1 100 LYS n 
1 101 ASP n 
1 102 LYS n 
1 103 SER n 
1 104 ARG n 
1 105 ALA n 
1 106 PRO n 
1 107 ILE n 
1 108 SER n 
1 109 ALA n 
1 110 LYS n 
1 111 LEU n 
1 112 VAL n 
1 113 ALA n 
1 114 ASN n 
1 115 MET n 
1 116 LEU n 
1 117 SER n 
1 118 VAL n 
1 119 ALA n 
1 120 GLY n 
1 121 ALA n 
1 122 ASP n 
1 123 HIS n 
1 124 ILE n 
1 125 ILE n 
1 126 THR n 
1 127 MET n 
1 128 ASP n 
1 129 LEU n 
1 130 HIS n 
1 131 ALA n 
1 132 SER n 
1 133 GLN n 
1 134 ILE n 
1 135 GLN n 
1 136 GLY n 
1 137 PHE n 
1 138 PHE n 
1 139 ASP n 
1 140 ILE n 
1 141 PRO n 
1 142 VAL n 
1 143 ASP n 
1 144 ASN n 
1 145 LEU n 
1 146 MET 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 2H08 A 1 ? 318 ? P60891 1 ? 318 ? 1 318 
2 1 2H08 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 2H08 MET A 146 ? UNP P60891 TYR 146 'engineered mutation' 146 1  
1 2H08 LEU A 319 ? UNP P60891 ?   ?   'expression tag'      319 2  
1 2H08 GLU A 320 ? UNP P60891 ?   ?   'expression tag'      320 3  
1 2H08 HIS A 321 ? UNP P60891 ?   ?   'expression tag'      321 4  
1 2H08 HIS A 322 ? UNP P60891 ?   ?   'expression tag'      322 5  
1 2H08 HIS A 323 ? UNP P60891 ?   ?   'expression tag'      323 6  
1 2H08 HIS A 324 ? UNP P60891 ?   ?   'expression tag'      324 7  
1 2H08 HIS A 325 ? UNP P60891 ?   ?   'expression tag'      325 8  
1 2H08 HIS A 326 ? UNP P60891 ?   ?   'expression tag'      326 9  
2 2H08 MET B 146 ? UNP P60891 TYR 146 'engineered mutation' 146 10 
2 2H08 LEU B 319 ? UNP P60891 ?   ?   'expression tag'      319 11 
2 2H08 GLU B 320 ? UNP P60891 ?   ?   'expression tag'      320 12 
2 2H08 HIS B 321 ? UNP P60891 ?   ?   'expression tag'      321 13 
2 2H08 HIS B 322 ? UNP P60891 ?   ?   'expression tag'      322 14 
2 2H08 HIS B 323 ? UNP P60891 ?   ?   'expression tag'      323 15 
2 2H08 HIS B 324 ? UNP P60891 ?   ?   'expression tag'      324 16 
2 2H08 HIS B 325 ? UNP P60891 ?   ?   'expression tag'      325 17 
2 2H08 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          2H08 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.39 
_exptl_crystal.density_percent_sol   48.44 
_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              4.4 
_exptl_crystal_grow.pdbx_details    
;0.1M citric acid, 1.3M ammonium sulfate, 0.02M sodium dihydrogen phosphate, 0.4M sodium chloride, pH 4.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K
;
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2006-03-03 
_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   1.0000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PHOTON FACTORY BEAMLINE BL-6A' 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
_diffrn_source.pdbx_synchrotron_beamline   BL-6A 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
# 
_reflns.entry_id                     2H08 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             50.0 
_reflns.d_resolution_high            2.5 
_reflns.number_obs                   22978 
_reflns.number_all                   22978 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.092 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.6 
_reflns.B_iso_Wilson_estimate        36.5 
_reflns.pdbx_redundancy              4.5 
_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             2.50 
_reflns_shell.d_res_low              2.59 
_reflns_shell.percent_possible_all   100.0 
_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                                 2H08 
_refine.ls_number_reflns_obs                     22970 
_refine.ls_number_reflns_all                     22971 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               2434628.42 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             49.05 
_refine.ls_d_res_high                            2.50 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_R_factor_obs                          0.207 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.207 
_refine.ls_R_factor_R_free                       0.257 
_refine.ls_R_factor_R_free_error                 0.008 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  1155 
_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                               41.0 
_refine.aniso_B[1][1]                            3.63 
_refine.aniso_B[2][2]                            3.70 
_refine.aniso_B[3][3]                            -7.34 
_refine.aniso_B[1][2]                            5.07 
_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                 0.375023 
_refine.solvent_model_param_bsol                 44.9631 
_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                        2H08 
_refine_analyze.Luzzati_coordinate_error_obs    0.28 
_refine_analyze.Luzzati_sigma_a_obs             0.29 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.38 
_refine_analyze.Luzzati_sigma_a_free            0.39 
_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        4683 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             164 
_refine_hist.number_atoms_total               4877 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        49.05 
# 
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                0.010 ? ? ? '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             1.4   ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      26.5  ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      1.50  ? ? ? '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                       2.50 
_refine_ls_shell.d_res_low                        2.66 
_refine_ls_shell.number_reflns_R_work             3639 
_refine_ls_shell.R_factor_R_work                  0.257 
_refine_ls_shell.percent_reflns_obs               100.0 
_refine_ls_shell.R_factor_R_free                  0.341 
_refine_ls_shell.R_factor_R_free_error            0.024 
_refine_ls_shell.percent_reflns_R_free            5.1 
_refine_ls_shell.number_reflns_R_free             196 
_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                  2H08 
_struct.title                     'crystal structure of human phosphoribosyl pyrophosphate synthetase 1 mutant Y146M' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2H08 
_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  GLU A 161 ? ASN A 164 ? GLU A 161 ASN A 164 5 ? 4  
HELX_P HELX_P7  7  ASP A 171 ? GLY A 173 ? ASP A 171 GLY A 173 5 ? 3  
HELX_P HELX_P8  8  GLY A 174 ? LEU A 185 ? GLY A 174 LEU A 185 1 ? 12 
HELX_P HELX_P9  9  CYS A 226 ? ALA A 239 ? CYS A 226 ALA A 239 1 ? 14 
HELX_P HELX_P10 10 PRO A 256 ? ALA A 264 ? PRO A 256 ALA A 264 1 ? 9  
HELX_P HELX_P11 11 GLN A 277 ? CYS A 284 ? GLN A 277 CYS A 284 1 ? 8  
HELX_P HELX_P12 12 ILE A 292 ? GLY A 306 ? ILE A 292 GLY A 306 1 ? 15 
HELX_P HELX_P13 13 VAL A 309 ? PHE A 313 ? VAL A 309 PHE A 313 5 ? 5  
HELX_P HELX_P14 14 GLN B 13  ? GLY B 24  ? GLN B 13  GLY B 24  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 GLY B 174 ? ASN B 186 ? GLY B 174 ASN B 186 1 ? 13 
HELX_P HELX_P21 21 CYS B 226 ? ALA B 239 ? CYS B 226 ALA B 239 1 ? 14 
HELX_P HELX_P22 22 PRO B 256 ? ALA B 264 ? PRO B 256 ALA B 264 1 ? 9  
HELX_P HELX_P23 23 GLN B 277 ? HIS B 283 ? GLN B 277 HIS B 283 1 ? 7  
HELX_P HELX_P24 24 ILE B 292 ? GLY B 306 ? ILE B 292 GLY B 306 1 ? 15 
HELX_P HELX_P25 25 VAL B 309 ? SER B 314 ? VAL B 309 SER B 314 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 2 ? 
C ? 7 ? 
D ? 5 ? 
E ? 2 ? 
F ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
C 6 7 ? parallel      
D 1 2 ? parallel      
D 2 3 ? parallel      
D 3 4 ? parallel      
D 4 5 ? parallel      
E 1 2 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? parallel      
F 3 4 ? parallel      
F 4 5 ? parallel      
F 5 6 ? parallel      
F 6 7 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ILE A 4   ? SER A 8   ? ILE A 4   SER A 8   
A 2 ASP A 52  ? VAL A 56  ? ASP A 52  VAL A 56  
A 3 ARG A 84  ? ILE A 89  ? ARG A 84  ILE A 89  
A 4 HIS A 123 ? MET A 127 ? HIS A 123 MET A 127 
A 5 VAL A 142 ? LEU A 145 ? VAL A 142 LEU A 145 
B 1 VAL A 30  ? VAL A 31  ? VAL A 30  VAL A 31  
B 2 GLU A 43  ? ILE A 44  ? GLU A 43  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 ? VAL B 208 ? MET B 205 VAL B 208 
F 2 ASP B 188 ? LYS B 194 ? ASP B 188 LYS B 194 
F 3 THR B 166 ? SER B 169 ? THR B 166 SER B 169 
F 4 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 PHE A 7   ? N PHE A 7   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 ILE A 192 ? O ILE A 192 N SER A 169 ? N SER A 169 
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 ALA A 246 ? N ALA A 246 O VAL A 270 ? O VAL A 270 
C 6 7 N VAL A 271 ? N VAL A 271 O ILE A 290 ? O ILE A 290 
D 1 2 N PHE B 7   ? N PHE B 7   O TYR B 54  ? O TYR B 54  
D 2 3 N VAL B 53  ? N VAL B 53  O ARG B 84  ? O ARG B 84  
D 3 4 N ILE B 89  ? N ILE B 89  O ILE B 125 ? O ILE B 125 
D 4 5 N 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 TYR B 245 ? O TYR B 245 
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 ? 6 'BINDING SITE FOR RESIDUE SO4 B 1001' 
AC2 Software A SO4 1002 ? 7 '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 ? 8 'BINDING SITE FOR RESIDUE SO4 A 1004' 
AC5 Software B SO4 1005 ? 8 'BINDING SITE FOR RESIDUE SO4 B 1005' 
AC6 Software A SO4 1006 ? 8 'BINDING SITE FOR RESIDUE SO4 A 1006' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 6 ASP B 224 ? ASP B 224  . ? 1_555 ? 
2  AC1 6 THR B 225 ? THR B 225  . ? 1_555 ? 
3  AC1 6 CYS B 226 ? CYS B 226  . ? 1_555 ? 
4  AC1 6 GLY B 227 ? GLY B 227  . ? 1_555 ? 
5  AC1 6 THR B 228 ? THR B 228  . ? 1_555 ? 
6  AC1 6 HOH J .   ? HOH B 1061 . ? 1_555 ? 
7  AC2 7 ASP A 224 ? ASP A 224  . ? 1_555 ? 
8  AC2 7 THR A 225 ? THR A 225  . ? 1_555 ? 
9  AC2 7 CYS A 226 ? CYS A 226  . ? 1_555 ? 
10 AC2 7 GLY A 227 ? GLY A 227  . ? 1_555 ? 
11 AC2 7 THR A 228 ? THR A 228  . ? 1_555 ? 
12 AC2 7 HOH I .   ? HOH A 1072 . ? 1_555 ? 
13 AC2 7 HOH I .   ? HOH A 1074 . ? 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 1045 . ? 1_555 ? 
21 AC4 8 SER A 47  ? SER A 47   . ? 2_565 ? 
22 AC4 8 ARG A 49  ? ARG A 49   . ? 2_565 ? 
23 AC4 8 SER A 308 ? SER A 308  . ? 1_555 ? 
24 AC4 8 VAL A 309 ? VAL A 309  . ? 1_555 ? 
25 AC4 8 SER A 310 ? SER A 310  . ? 1_555 ? 
26 AC4 8 HOH I .   ? HOH A 1014 . ? 1_555 ? 
27 AC4 8 HOH I .   ? HOH A 1034 . ? 2_565 ? 
28 AC4 8 ARG B 104 ? ARG B 104  . ? 1_555 ? 
29 AC5 8 LYS A 100 ? LYS A 100  . ? 1_555 ? 
30 AC5 8 ASP A 101 ? ASP A 101  . ? 1_555 ? 
31 AC5 8 LYS A 102 ? LYS A 102  . ? 1_555 ? 
32 AC5 8 SER B 132 ? SER B 132  . ? 1_555 ? 
33 AC5 8 GLN B 135 ? GLN B 135  . ? 1_555 ? 
34 AC5 8 ASN B 144 ? ASN B 144  . ? 1_555 ? 
35 AC5 8 HOH J .   ? HOH B 1007 . ? 1_555 ? 
36 AC5 8 HOH J .   ? HOH B 1082 . ? 1_555 ? 
37 AC6 8 SER A 132 ? SER A 132  . ? 1_555 ? 
38 AC6 8 GLN A 135 ? GLN A 135  . ? 1_555 ? 
39 AC6 8 ASN A 144 ? ASN A 144  . ? 1_555 ? 
40 AC6 8 HOH I .   ? HOH A 1020 . ? 1_555 ? 
41 AC6 8 HOH I .   ? HOH A 1079 . ? 1_555 ? 
42 AC6 8 LYS B 100 ? LYS B 100  . ? 1_555 ? 
43 AC6 8 ASP B 101 ? ASP B 101  . ? 1_555 ? 
44 AC6 8 LYS B 102 ? LYS B 102  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2H08 
_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                    2H08 
_atom_sites.fract_transf_matrix[1][1]   0.005885 
_atom_sites.fract_transf_matrix[1][2]   0.003398 
_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]   0.006796 
_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]   0.016206 
_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   ? -96.872  53.201 -23.531 1.00 46.95 ? 3    ASN A N   1 
ATOM   2    C CA  . ASN A 1 3   ? -95.915  52.900 -24.642 1.00 47.34 ? 3    ASN A CA  1 
ATOM   3    C C   . ASN A 1 3   ? -96.532  52.131 -25.823 1.00 46.42 ? 3    ASN A C   1 
ATOM   4    O O   . ASN A 1 3   ? -96.036  52.205 -26.947 1.00 46.45 ? 3    ASN A O   1 
ATOM   5    C CB  . ASN A 1 3   ? -94.694  52.150 -24.113 1.00 48.18 ? 3    ASN A CB  1 
ATOM   6    C CG  . ASN A 1 3   ? -93.723  51.777 -25.214 1.00 49.99 ? 3    ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 3   ? -92.974  52.624 -25.711 1.00 51.77 ? 3    ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 3   ? -93.740  50.508 -25.615 1.00 51.24 ? 3    ASN A ND2 1 
ATOM   9    N N   . ILE A 1 4   ? -97.593  51.377 -25.557 1.00 45.08 ? 4    ILE A N   1 
ATOM   10   C CA  . ILE A 1 4   ? -98.402  50.802 -26.627 1.00 43.77 ? 4    ILE A CA  1 
ATOM   11   C C   . ILE A 1 4   ? -99.609  51.704 -26.898 1.00 42.58 ? 4    ILE A C   1 
ATOM   12   O O   . ILE A 1 4   ? -100.198 52.261 -25.963 1.00 42.74 ? 4    ILE A O   1 
ATOM   13   C CB  . ILE A 1 4   ? -98.836  49.356 -26.292 1.00 43.95 ? 4    ILE A CB  1 
ATOM   14   C CG1 . ILE A 1 4   ? -100.023 48.931 -27.158 1.00 44.05 ? 4    ILE A CG1 1 
ATOM   15   C CG2 . ILE A 1 4   ? -99.145  49.205 -24.799 1.00 44.50 ? 4    ILE A CG2 1 
ATOM   16   C CD1 . ILE A 1 4   ? -100.401 47.479 -27.003 1.00 45.19 ? 4    ILE A CD1 1 
ATOM   17   N N   . LYS A 1 5   ? -99.952  51.856 -28.176 1.00 40.75 ? 5    LYS A N   1 
ATOM   18   C CA  . LYS A 1 5   ? -101.087 52.666 -28.592 1.00 39.24 ? 5    LYS A CA  1 
ATOM   19   C C   . LYS A 1 5   ? -101.931 51.968 -29.660 1.00 37.93 ? 5    LYS A C   1 
ATOM   20   O O   . LYS A 1 5   ? -101.399 51.437 -30.638 1.00 37.43 ? 5    LYS A O   1 
ATOM   21   C CB  . LYS A 1 5   ? -100.618 54.038 -29.079 1.00 39.45 ? 5    LYS A CB  1 
ATOM   22   C CG  . LYS A 1 5   ? -100.736 55.134 -28.029 1.00 40.74 ? 5    LYS A CG  1 
ATOM   23   C CD  . LYS A 1 5   ? -102.135 55.756 -28.007 1.00 42.39 ? 5    LYS A CD  1 
ATOM   24   C CE  . LYS A 1 5   ? -102.455 56.370 -26.658 1.00 43.71 ? 5    LYS A CE  1 
ATOM   25   N NZ  . LYS A 1 5   ? -103.923 56.312 -26.322 1.00 45.35 ? 5    LYS A NZ  1 
ATOM   26   N N   . ILE A 1 6   ? -103.247 51.971 -29.453 1.00 36.78 ? 6    ILE A N   1 
ATOM   27   C CA  . ILE A 1 6   ? -104.202 51.399 -30.405 1.00 35.92 ? 6    ILE A CA  1 
ATOM   28   C C   . ILE A 1 6   ? -105.045 52.479 -31.052 1.00 35.21 ? 6    ILE A C   1 
ATOM   29   O O   . ILE A 1 6   ? -105.706 53.245 -30.372 1.00 35.03 ? 6    ILE A O   1 
ATOM   30   C CB  . ILE A 1 6   ? -105.137 50.338 -29.755 1.00 35.71 ? 6    ILE A CB  1 
ATOM   31   C CG1 . ILE A 1 6   ? -104.354 49.406 -28.837 1.00 36.57 ? 6    ILE A CG1 1 
ATOM   32   C CG2 . ILE A 1 6   ? -105.850 49.518 -30.836 1.00 34.84 ? 6    ILE A CG2 1 
ATOM   33   C CD1 . ILE A 1 6   ? -105.014 48.041 -28.627 1.00 37.42 ? 6    ILE A CD1 1 
ATOM   34   N N   . PHE A 1 7   ? -105.017 52.519 -32.372 1.00 34.86 ? 7    PHE A N   1 
ATOM   35   C CA  . PHE A 1 7   ? -105.899 53.382 -33.136 1.00 34.91 ? 7    PHE A CA  1 
ATOM   36   C C   . PHE A 1 7   ? -106.851 52.529 -33.979 1.00 36.57 ? 7    PHE A C   1 
ATOM   37   O O   . PHE A 1 7   ? -106.535 51.400 -34.351 1.00 36.07 ? 7    PHE A O   1 
ATOM   38   C CB  . PHE A 1 7   ? -105.096 54.301 -34.049 1.00 33.46 ? 7    PHE A CB  1 
ATOM   39   C CG  . PHE A 1 7   ? -104.280 55.330 -33.330 1.00 30.78 ? 7    PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 7   ? -102.993 55.045 -32.909 1.00 29.06 ? 7    PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 7   ? -104.782 56.604 -33.106 1.00 29.07 ? 7    PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 7   ? -102.239 56.007 -32.255 1.00 28.28 ? 7    PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 7   ? -104.023 57.575 -32.456 1.00 27.29 ? 7    PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 7   ? -102.760 57.276 -32.031 1.00 27.40 ? 7    PHE A CZ  1 
ATOM   45   N N   . SER A 1 8   ? -108.015 53.082 -34.273 1.00 38.98 ? 8    SER A N   1 
ATOM   46   C CA  . SER A 1 8   ? -108.986 52.422 -35.110 1.00 41.71 ? 8    SER A CA  1 
ATOM   47   C C   . SER A 1 8   ? -109.118 53.172 -36.423 1.00 44.28 ? 8    SER A C   1 
ATOM   48   O O   . SER A 1 8   ? -108.995 54.403 -36.459 1.00 44.19 ? 8    SER A O   1 
ATOM   49   C CB  . SER A 1 8   ? -110.331 52.405 -34.406 1.00 41.47 ? 8    SER A CB  1 
ATOM   50   O OG  . SER A 1 8   ? -111.326 51.865 -35.242 1.00 41.57 ? 8    SER A OG  1 
ATOM   51   N N   . GLY A 1 9   ? -109.370 52.417 -37.492 1.00 47.20 ? 9    GLY A N   1 
ATOM   52   C CA  . GLY A 1 9   ? -109.753 52.972 -38.780 1.00 51.02 ? 9    GLY A CA  1 
ATOM   53   C C   . GLY A 1 9   ? -111.257 53.166 -38.934 1.00 53.85 ? 9    GLY A C   1 
ATOM   54   O O   . GLY A 1 9   ? -112.031 52.249 -38.692 1.00 54.43 ? 9    GLY A O   1 
ATOM   55   N N   . SER A 1 10  ? -111.665 54.372 -39.328 1.00 56.42 ? 10   SER A N   1 
ATOM   56   C CA  . SER A 1 10  ? -113.066 54.716 -39.637 1.00 58.68 ? 10   SER A CA  1 
ATOM   57   C C   . SER A 1 10  ? -114.094 54.359 -38.566 1.00 60.08 ? 10   SER A C   1 
ATOM   58   O O   . SER A 1 10  ? -113.739 53.971 -37.448 1.00 60.44 ? 10   SER A O   1 
ATOM   59   C CB  . SER A 1 10  ? -113.495 54.156 -41.007 1.00 58.93 ? 10   SER A CB  1 
ATOM   60   O OG  . SER A 1 10  ? -114.568 54.890 -41.589 1.00 59.33 ? 10   SER A OG  1 
ATOM   61   N N   . SER A 1 11  ? -115.365 54.497 -38.947 1.00 61.60 ? 11   SER A N   1 
ATOM   62   C CA  . SER A 1 11  ? -116.521 54.444 -38.051 1.00 63.00 ? 11   SER A CA  1 
ATOM   63   C C   . SER A 1 11  ? -116.694 53.137 -37.268 1.00 63.48 ? 11   SER A C   1 
ATOM   64   O O   . SER A 1 11  ? -117.331 53.123 -36.206 1.00 63.88 ? 11   SER A O   1 
ATOM   65   C CB  . SER A 1 11  ? -117.803 54.744 -38.855 1.00 63.43 ? 11   SER A CB  1 
ATOM   66   O OG  . SER A 1 11  ? -118.759 55.472 -38.088 1.00 64.35 ? 11   SER A OG  1 
ATOM   67   N N   . HIS A 1 12  ? -116.126 52.046 -37.770 1.00 63.74 ? 12   HIS A N   1 
ATOM   68   C CA  . HIS A 1 12  ? -116.378 50.737 -37.162 1.00 63.91 ? 12   HIS A CA  1 
ATOM   69   C C   . HIS A 1 12  ? -115.441 50.425 -35.988 1.00 62.86 ? 12   HIS A C   1 
ATOM   70   O O   . HIS A 1 12  ? -114.528 49.581 -36.058 1.00 62.79 ? 12   HIS A O   1 
ATOM   71   C CB  . HIS A 1 12  ? -116.470 49.658 -38.238 1.00 64.87 ? 12   HIS A CB  1 
ATOM   72   C CG  . HIS A 1 12  ? -117.593 49.902 -39.203 1.00 67.65 ? 12   HIS A CG  1 
ATOM   73   N ND1 . HIS A 1 12  ? -118.296 48.884 -39.811 1.00 70.02 ? 12   HIS A ND1 1 
ATOM   74   C CD2 . HIS A 1 12  ? -118.159 51.056 -39.634 1.00 69.24 ? 12   HIS A CD2 1 
ATOM   75   C CE1 . HIS A 1 12  ? -119.236 49.399 -40.586 1.00 70.81 ? 12   HIS A CE1 1 
ATOM   76   N NE2 . HIS A 1 12  ? -119.174 50.716 -40.496 1.00 70.39 ? 12   HIS A NE2 1 
ATOM   77   N N   . GLN A 1 13  ? -115.735 51.149 -34.905 1.00 61.39 ? 13   GLN A N   1 
ATOM   78   C CA  . GLN A 1 13  ? -114.934 51.218 -33.694 1.00 59.82 ? 13   GLN A CA  1 
ATOM   79   C C   . GLN A 1 13  ? -115.307 50.123 -32.713 1.00 57.86 ? 13   GLN A C   1 
ATOM   80   O O   . GLN A 1 13  ? -114.949 50.200 -31.544 1.00 58.05 ? 13   GLN A O   1 
ATOM   81   C CB  . GLN A 1 13  ? -115.146 52.579 -33.009 1.00 60.39 ? 13   GLN A CB  1 
ATOM   82   C CG  . GLN A 1 13  ? -114.349 53.746 -33.595 1.00 61.75 ? 13   GLN A CG  1 
ATOM   83   C CD  . GLN A 1 13  ? -113.575 54.532 -32.536 1.00 63.51 ? 13   GLN A CD  1 
ATOM   84   O OE1 . GLN A 1 13  ? -112.429 54.934 -32.772 1.00 64.63 ? 13   GLN A OE1 1 
ATOM   85   N NE2 . GLN A 1 13  ? -114.194 54.756 -31.377 1.00 63.58 ? 13   GLN A NE2 1 
ATOM   86   N N   . ASP A 1 14  ? -116.026 49.110 -33.172 1.00 55.47 ? 14   ASP A N   1 
ATOM   87   C CA  . ASP A 1 14  ? -116.497 48.069 -32.265 1.00 53.29 ? 14   ASP A CA  1 
ATOM   88   C C   . ASP A 1 14  ? -115.411 47.076 -31.896 1.00 51.27 ? 14   ASP A C   1 
ATOM   89   O O   . ASP A 1 14  ? -115.085 46.930 -30.713 1.00 51.52 ? 14   ASP A O   1 
ATOM   90   C CB  . ASP A 1 14  ? -117.711 47.344 -32.828 1.00 53.67 ? 14   ASP A CB  1 
ATOM   91   C CG  . ASP A 1 14  ? -118.742 47.069 -31.774 1.00 54.51 ? 14   ASP A CG  1 
ATOM   92   O OD1 . ASP A 1 14  ? -118.562 46.112 -30.985 1.00 54.44 ? 14   ASP A OD1 1 
ATOM   93   O OD2 . ASP A 1 14  ? -119.760 47.780 -31.648 1.00 56.08 ? 14   ASP A OD2 1 
ATOM   94   N N   . LEU A 1 15  ? -114.862 46.398 -32.903 1.00 48.53 ? 15   LEU A N   1 
ATOM   95   C CA  . LEU A 1 15  ? -113.724 45.503 -32.721 1.00 46.28 ? 15   LEU A CA  1 
ATOM   96   C C   . LEU A 1 15  ? -112.595 46.171 -31.924 1.00 45.11 ? 15   LEU A C   1 
ATOM   97   O O   . LEU A 1 15  ? -112.141 45.640 -30.906 1.00 44.94 ? 15   LEU A O   1 
ATOM   98   C CB  . LEU A 1 15  ? -113.193 45.029 -34.078 1.00 45.74 ? 15   LEU A CB  1 
ATOM   99   C CG  . LEU A 1 15  ? -112.982 43.536 -34.322 1.00 44.54 ? 15   LEU A CG  1 
ATOM   100  C CD1 . LEU A 1 15  ? -111.978 43.339 -35.428 1.00 43.52 ? 15   LEU A CD1 1 
ATOM   101  C CD2 . LEU A 1 15  ? -112.545 42.786 -33.078 1.00 43.55 ? 15   LEU A CD2 1 
ATOM   102  N N   . SER A 1 16  ? -112.172 47.344 -32.388 1.00 43.70 ? 16   SER A N   1 
ATOM   103  C CA  . SER A 1 16  ? -111.097 48.109 -31.767 1.00 42.58 ? 16   SER A CA  1 
ATOM   104  C C   . SER A 1 16  ? -111.376 48.509 -30.324 1.00 41.60 ? 16   SER A C   1 
ATOM   105  O O   . SER A 1 16  ? -110.452 48.559 -29.518 1.00 41.13 ? 16   SER A O   1 
ATOM   106  C CB  . SER A 1 16  ? -110.800 49.359 -32.583 1.00 42.56 ? 16   SER A CB  1 
ATOM   107  O OG  . SER A 1 16  ? -110.986 49.109 -33.952 1.00 43.12 ? 16   SER A OG  1 
ATOM   108  N N   . GLN A 1 17  ? -112.638 48.818 -30.019 1.00 40.68 ? 17   GLN A N   1 
ATOM   109  C CA  . GLN A 1 17  ? -113.063 49.090 -28.646 1.00 39.91 ? 17   GLN A CA  1 
ATOM   110  C C   . GLN A 1 17  ? -112.941 47.826 -27.793 1.00 38.89 ? 17   GLN A C   1 
ATOM   111  O O   . GLN A 1 17  ? -112.370 47.862 -26.703 1.00 38.87 ? 17   GLN A O   1 
ATOM   112  C CB  . GLN A 1 17  ? -114.498 49.635 -28.608 1.00 40.21 ? 17   GLN A CB  1 
ATOM   113  C CG  . GLN A 1 17  ? -114.886 50.376 -27.324 1.00 41.55 ? 17   GLN A CG  1 
ATOM   114  C CD  . GLN A 1 17  ? -113.856 51.420 -26.881 1.00 43.61 ? 17   GLN A CD  1 
ATOM   115  O OE1 . GLN A 1 17  ? -113.676 52.449 -27.540 1.00 45.08 ? 17   GLN A OE1 1 
ATOM   116  N NE2 . GLN A 1 17  ? -113.182 51.152 -25.769 1.00 43.68 ? 17   GLN A NE2 1 
ATOM   117  N N   . LYS A 1 18  ? -113.460 46.708 -28.297 1.00 37.67 ? 18   LYS A N   1 
ATOM   118  C CA  . LYS A 1 18  ? -113.320 45.440 -27.604 1.00 36.53 ? 18   LYS A CA  1 
ATOM   119  C C   . LYS A 1 18  ? -111.859 45.135 -27.340 1.00 35.96 ? 18   LYS A C   1 
ATOM   120  O O   . LYS A 1 18  ? -111.492 44.767 -26.218 1.00 36.15 ? 18   LYS A O   1 
ATOM   121  C CB  . LYS A 1 18  ? -113.959 44.314 -28.390 1.00 36.46 ? 18   LYS A CB  1 
ATOM   122  C CG  . LYS A 1 18  ? -115.430 44.140 -28.142 1.00 36.33 ? 18   LYS A CG  1 
ATOM   123  C CD  . LYS A 1 18  ? -116.062 43.522 -29.366 1.00 36.67 ? 18   LYS A CD  1 
ATOM   124  C CE  . LYS A 1 18  ? -117.479 43.076 -29.099 1.00 37.42 ? 18   LYS A CE  1 
ATOM   125  N NZ  . LYS A 1 18  ? -118.435 44.216 -29.284 1.00 38.29 ? 18   LYS A NZ  1 
ATOM   126  N N   . ILE A 1 19  ? -111.024 45.314 -28.364 1.00 35.28 ? 19   ILE A N   1 
ATOM   127  C CA  . ILE A 1 19  ? -109.583 45.058 -28.264 1.00 34.42 ? 19   ILE A CA  1 
ATOM   128  C C   . ILE A 1 19  ? -108.934 45.949 -27.203 1.00 34.42 ? 19   ILE A C   1 
ATOM   129  O O   . ILE A 1 19  ? -108.213 45.458 -26.325 1.00 34.45 ? 19   ILE A O   1 
ATOM   130  C CB  . ILE A 1 19  ? -108.901 45.217 -29.647 1.00 34.10 ? 19   ILE A CB  1 
ATOM   131  C CG1 . ILE A 1 19  ? -109.348 44.093 -30.591 1.00 33.57 ? 19   ILE A CG1 1 
ATOM   132  C CG2 . ILE A 1 19  ? -107.376 45.224 -29.517 1.00 33.67 ? 19   ILE A CG2 1 
ATOM   133  C CD1 . ILE A 1 19  ? -109.258 44.434 -32.070 1.00 32.49 ? 19   ILE A CD1 1 
ATOM   134  N N   . ALA A 1 20  ? -109.218 47.247 -27.257 1.00 34.46 ? 20   ALA A N   1 
ATOM   135  C CA  . ALA A 1 20  ? -108.647 48.202 -26.306 1.00 35.07 ? 20   ALA A CA  1 
ATOM   136  C C   . ALA A 1 20  ? -109.069 47.930 -24.852 1.00 35.82 ? 20   ALA A C   1 
ATOM   137  O O   . ALA A 1 20  ? -108.305 48.186 -23.915 1.00 35.73 ? 20   ALA A O   1 
ATOM   138  C CB  . ALA A 1 20  ? -108.975 49.632 -26.714 1.00 34.41 ? 20   ALA A CB  1 
ATOM   139  N N   . ASP A 1 21  ? -110.280 47.408 -24.673 1.00 36.87 ? 21   ASP A N   1 
ATOM   140  C CA  . ASP A 1 21  ? -110.771 47.059 -23.344 1.00 38.02 ? 21   ASP A CA  1 
ATOM   141  C C   . ASP A 1 21  ? -109.950 45.919 -22.740 1.00 38.25 ? 21   ASP A C   1 
ATOM   142  O O   . ASP A 1 21  ? -109.459 46.025 -21.607 1.00 38.27 ? 21   ASP A O   1 
ATOM   143  C CB  . ASP A 1 21  ? -112.261 46.689 -23.385 1.00 38.38 ? 21   ASP A CB  1 
ATOM   144  C CG  . ASP A 1 21  ? -113.149 47.867 -23.739 1.00 39.55 ? 21   ASP A CG  1 
ATOM   145  O OD1 . ASP A 1 21  ? -112.665 49.028 -23.714 1.00 40.17 ? 21   ASP A OD1 1 
ATOM   146  O OD2 . ASP A 1 21  ? -114.348 47.721 -24.072 1.00 40.63 ? 21   ASP A OD2 1 
ATOM   147  N N   . ARG A 1 22  ? -109.776 44.849 -23.512 1.00 38.45 ? 22   ARG A N   1 
ATOM   148  C CA  . ARG A 1 22  ? -109.046 43.673 -23.030 1.00 38.66 ? 22   ARG A CA  1 
ATOM   149  C C   . ARG A 1 22  ? -107.612 44.017 -22.624 1.00 38.25 ? 22   ARG A C   1 
ATOM   150  O O   . ARG A 1 22  ? -107.003 43.303 -21.832 1.00 38.89 ? 22   ARG A O   1 
ATOM   151  C CB  . ARG A 1 22  ? -109.046 42.560 -24.081 1.00 38.89 ? 22   ARG A CB  1 
ATOM   152  C CG  . ARG A 1 22  ? -110.441 42.163 -24.554 1.00 40.15 ? 22   ARG A CG  1 
ATOM   153  C CD  . ARG A 1 22  ? -110.478 40.909 -25.392 1.00 42.08 ? 22   ARG A CD  1 
ATOM   154  N NE  . ARG A 1 22  ? -111.848 40.496 -25.690 1.00 44.51 ? 22   ARG A NE  1 
ATOM   155  C CZ  . ARG A 1 22  ? -112.631 39.783 -24.875 1.00 45.75 ? 22   ARG A CZ  1 
ATOM   156  N NH1 . ARG A 1 22  ? -112.198 39.381 -23.676 1.00 45.91 ? 22   ARG A NH1 1 
ATOM   157  N NH2 . ARG A 1 22  ? -113.865 39.479 -25.262 1.00 46.26 ? 22   ARG A NH2 1 
ATOM   158  N N   . LEU A 1 23  ? -107.086 45.117 -23.151 1.00 37.31 ? 23   LEU A N   1 
ATOM   159  C CA  . LEU A 1 23  ? -105.699 45.494 -22.892 1.00 36.45 ? 23   LEU A CA  1 
ATOM   160  C C   . LEU A 1 23  ? -105.634 46.616 -21.881 1.00 35.52 ? 23   LEU A C   1 
ATOM   161  O O   . LEU A 1 23  ? -104.545 47.010 -21.474 1.00 35.58 ? 23   LEU A O   1 
ATOM   162  C CB  . LEU A 1 23  ? -104.964 45.883 -24.191 1.00 36.57 ? 23   LEU A CB  1 
ATOM   163  C CG  . LEU A 1 23  ? -104.869 44.806 -25.287 1.00 36.92 ? 23   LEU A CG  1 
ATOM   164  C CD1 . LEU A 1 23  ? -104.380 45.378 -26.606 1.00 37.36 ? 23   LEU A CD1 1 
ATOM   165  C CD2 . LEU A 1 23  ? -103.981 43.655 -24.862 1.00 36.91 ? 23   LEU A CD2 1 
ATOM   166  N N   . GLY A 1 24  ? -106.804 47.111 -21.476 1.00 34.41 ? 24   GLY A N   1 
ATOM   167  C CA  . GLY A 1 24  ? -106.904 48.145 -20.462 1.00 33.25 ? 24   GLY A CA  1 
ATOM   168  C C   . GLY A 1 24  ? -106.554 49.513 -20.997 1.00 32.61 ? 24   GLY A C   1 
ATOM   169  O O   . GLY A 1 24  ? -106.064 50.364 -20.264 1.00 32.34 ? 24   GLY A O   1 
ATOM   170  N N   . LEU A 1 25  ? -106.808 49.722 -22.287 1.00 32.32 ? 25   LEU A N   1 
ATOM   171  C CA  . LEU A 1 25  ? -106.475 50.988 -22.942 1.00 31.91 ? 25   LEU A CA  1 
ATOM   172  C C   . LEU A 1 25  ? -107.692 51.682 -23.534 1.00 31.64 ? 25   LEU A C   1 
ATOM   173  O O   . LEU A 1 25  ? -108.747 51.068 -23.739 1.00 31.16 ? 25   LEU A O   1 
ATOM   174  C CB  . LEU A 1 25  ? -105.441 50.786 -24.055 1.00 31.72 ? 25   LEU A CB  1 
ATOM   175  C CG  . LEU A 1 25  ? -104.216 49.925 -23.796 1.00 31.92 ? 25   LEU A CG  1 
ATOM   176  C CD1 . LEU A 1 25  ? -103.712 49.415 -25.129 1.00 32.23 ? 25   LEU A CD1 1 
ATOM   177  C CD2 . LEU A 1 25  ? -103.131 50.686 -23.023 1.00 32.12 ? 25   LEU A CD2 1 
ATOM   178  N N   . GLU A 1 26  ? -107.516 52.973 -23.797 1.00 31.60 ? 26   GLU A N   1 
ATOM   179  C CA  . GLU A 1 26  ? -108.441 53.738 -24.611 1.00 31.89 ? 26   GLU A CA  1 
ATOM   180  C C   . GLU A 1 26  ? -107.853 53.887 -25.999 1.00 31.23 ? 26   GLU A C   1 
ATOM   181  O O   . GLU A 1 26  ? -106.633 54.004 -26.156 1.00 30.86 ? 26   GLU A O   1 
ATOM   182  C CB  . GLU A 1 26  ? -108.684 55.110 -23.994 1.00 32.64 ? 26   GLU A CB  1 
ATOM   183  C CG  . GLU A 1 26  ? -109.452 55.019 -22.680 1.00 35.52 ? 26   GLU A CG  1 
ATOM   184  C CD  . GLU A 1 26  ? -109.479 56.319 -21.901 1.00 39.04 ? 26   GLU A CD  1 
ATOM   185  O OE1 . GLU A 1 26  ? -108.924 57.348 -22.381 1.00 41.20 ? 26   GLU A OE1 1 
ATOM   186  O OE2 . GLU A 1 26  ? -110.067 56.301 -20.799 1.00 40.15 ? 26   GLU A OE2 1 
ATOM   187  N N   . LEU A 1 27  ? -108.721 53.857 -27.003 1.00 30.80 ? 27   LEU A N   1 
ATOM   188  C CA  . LEU A 1 27  ? -108.304 54.074 -28.385 1.00 30.75 ? 27   LEU A CA  1 
ATOM   189  C C   . LEU A 1 27  ? -107.660 55.447 -28.520 1.00 31.20 ? 27   LEU A C   1 
ATOM   190  O O   . LEU A 1 27  ? -108.134 56.412 -27.947 1.00 30.55 ? 27   LEU A O   1 
ATOM   191  C CB  . LEU A 1 27  ? -109.486 53.909 -29.357 1.00 30.03 ? 27   LEU A CB  1 
ATOM   192  C CG  . LEU A 1 27  ? -109.918 52.442 -29.571 1.00 29.00 ? 27   LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 27  ? -111.361 52.338 -30.055 1.00 28.08 ? 27   LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 27  ? -108.968 51.623 -30.480 1.00 27.23 ? 27   LEU A CD2 1 
ATOM   195  N N   . GLY A 1 28  ? -106.548 55.514 -29.242 1.00 32.54 ? 28   GLY A N   1 
ATOM   196  C CA  . GLY A 1 28  ? -105.896 56.777 -29.525 1.00 34.56 ? 28   GLY A CA  1 
ATOM   197  C C   . GLY A 1 28  ? -106.837 57.753 -30.222 1.00 36.45 ? 28   GLY A C   1 
ATOM   198  O O   . GLY A 1 28  ? -107.757 57.341 -30.942 1.00 35.80 ? 28   GLY A O   1 
ATOM   199  N N   . LYS A 1 29  ? -106.614 59.043 -29.986 1.00 38.61 ? 29   LYS A N   1 
ATOM   200  C CA  . LYS A 1 29  ? -107.395 60.092 -30.620 1.00 41.60 ? 29   LYS A CA  1 
ATOM   201  C C   . LYS A 1 29  ? -106.995 60.238 -32.092 1.00 43.10 ? 29   LYS A C   1 
ATOM   202  O O   . LYS A 1 29  ? -105.815 60.345 -32.425 1.00 42.80 ? 29   LYS A O   1 
ATOM   203  C CB  . LYS A 1 29  ? -107.217 61.422 -29.875 1.00 42.20 ? 29   LYS A CB  1 
ATOM   204  C CG  . LYS A 1 29  ? -107.377 61.327 -28.358 1.00 44.84 ? 29   LYS A CG  1 
ATOM   205  C CD  . LYS A 1 29  ? -107.442 62.710 -27.684 1.00 48.48 ? 29   LYS A CD  1 
ATOM   206  C CE  . LYS A 1 29  ? -106.359 62.873 -26.589 1.00 50.82 ? 29   LYS A CE  1 
ATOM   207  N NZ  . LYS A 1 29  ? -106.537 61.925 -25.424 1.00 52.52 ? 29   LYS A NZ  1 
ATOM   208  N N   . VAL A 1 30  ? -107.980 60.229 -32.973 1.00 45.52 ? 30   VAL A N   1 
ATOM   209  C CA  . VAL A 1 30  ? -107.710 60.420 -34.394 1.00 48.28 ? 30   VAL A CA  1 
ATOM   210  C C   . VAL A 1 30  ? -108.808 61.245 -35.082 1.00 50.50 ? 30   VAL A C   1 
ATOM   211  O O   . VAL A 1 30  ? -109.975 60.850 -35.078 1.00 50.55 ? 30   VAL A O   1 
ATOM   212  C CB  . VAL A 1 30  ? -107.391 59.067 -35.132 1.00 48.01 ? 30   VAL A CB  1 
ATOM   213  C CG1 . VAL A 1 30  ? -108.496 58.027 -34.949 1.00 48.02 ? 30   VAL A CG1 1 
ATOM   214  C CG2 . VAL A 1 30  ? -107.113 59.306 -36.592 1.00 48.05 ? 30   VAL A CG2 1 
ATOM   215  N N   . VAL A 1 31  ? -108.419 62.392 -35.646 1.00 53.45 ? 31   VAL A N   1 
ATOM   216  C CA  . VAL A 1 31  ? -109.336 63.285 -36.371 1.00 56.49 ? 31   VAL A CA  1 
ATOM   217  C C   . VAL A 1 31  ? -109.462 62.867 -37.838 1.00 58.79 ? 31   VAL A C   1 
ATOM   218  O O   . VAL A 1 31  ? -108.471 62.847 -38.573 1.00 58.81 ? 31   VAL A O   1 
ATOM   219  C CB  . VAL A 1 31  ? -108.890 64.775 -36.299 1.00 56.52 ? 31   VAL A CB  1 
ATOM   220  C CG1 . VAL A 1 31  ? -109.960 65.697 -36.896 1.00 56.47 ? 31   VAL A CG1 1 
ATOM   221  C CG2 . VAL A 1 31  ? -108.555 65.187 -34.860 1.00 56.81 ? 31   VAL A CG2 1 
ATOM   222  N N   . THR A 1 32  ? -110.688 62.557 -38.255 1.00 61.78 ? 32   THR A N   1 
ATOM   223  C CA  . THR A 1 32  ? -110.958 62.010 -39.584 1.00 64.74 ? 32   THR A CA  1 
ATOM   224  C C   . THR A 1 32  ? -111.970 62.855 -40.379 1.00 67.01 ? 32   THR A C   1 
ATOM   225  O O   . THR A 1 32  ? -113.167 62.543 -40.401 1.00 67.51 ? 32   THR A O   1 
ATOM   226  C CB  . THR A 1 32  ? -111.452 60.545 -39.454 1.00 64.69 ? 32   THR A CB  1 
ATOM   227  O OG1 . THR A 1 32  ? -110.737 59.889 -38.403 1.00 65.00 ? 32   THR A OG1 1 
ATOM   228  C CG2 . THR A 1 32  ? -111.070 59.735 -40.663 1.00 64.84 ? 32   THR A CG2 1 
ATOM   229  N N   . LYS A 1 33  ? -111.488 63.914 -41.034 1.00 69.47 ? 33   LYS A N   1 
ATOM   230  C CA  . LYS A 1 33  ? -112.350 64.797 -41.840 1.00 71.85 ? 33   LYS A CA  1 
ATOM   231  C C   . LYS A 1 33  ? -112.511 64.293 -43.290 1.00 73.38 ? 33   LYS A C   1 
ATOM   232  O O   . LYS A 1 33  ? -111.514 64.093 -43.994 1.00 73.49 ? 33   LYS A O   1 
ATOM   233  C CB  . LYS A 1 33  ? -111.822 66.237 -41.810 1.00 72.01 ? 33   LYS A CB  1 
ATOM   234  C CG  . LYS A 1 33  ? -111.897 66.898 -40.428 1.00 72.79 ? 33   LYS A CG  1 
ATOM   235  C CD  . LYS A 1 33  ? -111.587 68.393 -40.486 1.00 73.82 ? 33   LYS A CD  1 
ATOM   236  C CE  . LYS A 1 33  ? -112.367 69.165 -39.419 1.00 74.37 ? 33   LYS A CE  1 
ATOM   237  N NZ  . LYS A 1 33  ? -112.432 70.634 -39.698 1.00 74.34 ? 33   LYS A NZ  1 
ATOM   238  N N   . LYS A 1 34  ? -113.761 64.082 -43.723 1.00 75.10 ? 34   LYS A N   1 
ATOM   239  C CA  . LYS A 1 34  ? -114.049 63.478 -45.042 1.00 76.61 ? 34   LYS A CA  1 
ATOM   240  C C   . LYS A 1 34  ? -114.461 64.489 -46.110 1.00 77.01 ? 34   LYS A C   1 
ATOM   241  O O   . LYS A 1 34  ? -115.519 65.120 -46.021 1.00 77.08 ? 34   LYS A O   1 
ATOM   242  C CB  . LYS A 1 34  ? -115.088 62.350 -44.934 1.00 77.21 ? 34   LYS A CB  1 
ATOM   243  C CG  . LYS A 1 34  ? -114.659 61.173 -44.040 1.00 78.93 ? 34   LYS A CG  1 
ATOM   244  C CD  . LYS A 1 34  ? -113.602 60.294 -44.712 1.00 81.06 ? 34   LYS A CD  1 
ATOM   245  C CE  . LYS A 1 34  ? -112.192 60.722 -44.320 1.00 82.44 ? 34   LYS A CE  1 
ATOM   246  N NZ  . LYS A 1 34  ? -111.473 59.630 -43.609 1.00 83.78 ? 34   LYS A NZ  1 
ATOM   247  N N   . PHE A 1 35  ? -113.617 64.598 -47.133 1.00 77.47 ? 35   PHE A N   1 
ATOM   248  C CA  . PHE A 1 35  ? -113.650 65.707 -48.081 1.00 77.85 ? 35   PHE A CA  1 
ATOM   249  C C   . PHE A 1 35  ? -114.629 65.568 -49.241 1.00 77.51 ? 35   PHE A C   1 
ATOM   250  O O   . PHE A 1 35  ? -115.663 64.899 -49.139 1.00 77.54 ? 35   PHE A O   1 
ATOM   251  C CB  . PHE A 1 35  ? -112.248 65.940 -48.653 1.00 78.40 ? 35   PHE A CB  1 
ATOM   252  C CG  . PHE A 1 35  ? -111.307 66.625 -47.709 1.00 80.19 ? 35   PHE A CG  1 
ATOM   253  C CD1 . PHE A 1 35  ? -111.783 67.340 -46.609 1.00 81.34 ? 35   PHE A CD1 1 
ATOM   254  C CD2 . PHE A 1 35  ? -109.937 66.560 -47.926 1.00 81.63 ? 35   PHE A CD2 1 
ATOM   255  C CE1 . PHE A 1 35  ? -110.912 67.971 -45.741 1.00 82.20 ? 35   PHE A CE1 1 
ATOM   256  C CE2 . PHE A 1 35  ? -109.054 67.187 -47.066 1.00 82.62 ? 35   PHE A CE2 1 
ATOM   257  C CZ  . PHE A 1 35  ? -109.543 67.898 -45.969 1.00 82.84 ? 35   PHE A CZ  1 
ATOM   258  N N   . SER A 1 36  ? -114.255 66.232 -50.337 1.00 76.94 ? 36   SER A N   1 
ATOM   259  C CA  . SER A 1 36  ? -114.988 66.298 -51.599 1.00 76.04 ? 36   SER A CA  1 
ATOM   260  C C   . SER A 1 36  ? -115.467 64.954 -52.113 1.00 75.12 ? 36   SER A C   1 
ATOM   261  O O   . SER A 1 36  ? -116.610 64.552 -51.864 1.00 75.15 ? 36   SER A O   1 
ATOM   262  C CB  . SER A 1 36  ? -114.086 66.920 -52.672 1.00 76.24 ? 36   SER A CB  1 
ATOM   263  O OG  . SER A 1 36  ? -112.787 66.343 -52.668 1.00 76.28 ? 36   SER A OG  1 
ATOM   264  N N   . ASN A 1 37  ? -114.577 64.280 -52.841 1.00 73.79 ? 37   ASN A N   1 
ATOM   265  C CA  . ASN A 1 37  ? -114.909 63.051 -53.548 1.00 72.54 ? 37   ASN A CA  1 
ATOM   266  C C   . ASN A 1 37  ? -114.447 61.819 -52.792 1.00 71.02 ? 37   ASN A C   1 
ATOM   267  O O   . ASN A 1 37  ? -113.893 60.889 -53.372 1.00 71.11 ? 37   ASN A O   1 
ATOM   268  C CB  . ASN A 1 37  ? -114.358 63.068 -54.985 1.00 72.96 ? 37   ASN A CB  1 
ATOM   269  C CG  . ASN A 1 37  ? -112.886 63.479 -55.064 1.00 73.75 ? 37   ASN A CG  1 
ATOM   270  O OD1 . ASN A 1 37  ? -112.451 64.081 -56.052 1.00 74.36 ? 37   ASN A OD1 1 
ATOM   271  N ND2 . ASN A 1 37  ? -112.114 63.148 -54.035 1.00 74.45 ? 37   ASN A ND2 1 
ATOM   272  N N   . GLN A 1 38  ? -114.690 61.828 -51.487 1.00 69.08 ? 38   GLN A N   1 
ATOM   273  C CA  . GLN A 1 38  ? -114.263 60.755 -50.599 1.00 67.01 ? 38   GLN A CA  1 
ATOM   274  C C   . GLN A 1 38  ? -112.762 60.802 -50.317 1.00 65.42 ? 38   GLN A C   1 
ATOM   275  O O   . GLN A 1 38  ? -112.224 59.882 -49.691 1.00 65.62 ? 38   GLN A O   1 
ATOM   276  C CB  . GLN A 1 38  ? -114.683 59.382 -51.148 1.00 67.12 ? 38   GLN A CB  1 
ATOM   277  C CG  . GLN A 1 38  ? -114.898 58.305 -50.096 1.00 66.67 ? 38   GLN A CG  1 
ATOM   278  C CD  . GLN A 1 38  ? -115.914 58.691 -49.055 1.00 66.15 ? 38   GLN A CD  1 
ATOM   279  O OE1 . GLN A 1 38  ? -115.565 58.873 -47.890 1.00 66.00 ? 38   GLN A OE1 1 
ATOM   280  N NE2 . GLN A 1 38  ? -117.173 58.826 -49.466 1.00 65.72 ? 38   GLN A NE2 1 
ATOM   281  N N   . GLU A 1 39  ? -112.096 61.870 -50.761 1.00 63.09 ? 39   GLU A N   1 
ATOM   282  C CA  . GLU A 1 39  ? -110.691 62.079 -50.431 1.00 61.01 ? 39   GLU A CA  1 
ATOM   283  C C   . GLU A 1 39  ? -110.528 62.011 -48.916 1.00 60.03 ? 39   GLU A C   1 
ATOM   284  O O   . GLU A 1 39  ? -111.120 62.790 -48.174 1.00 59.67 ? 39   GLU A O   1 
ATOM   285  C CB  . GLU A 1 39  ? -110.150 63.396 -51.005 1.00 60.58 ? 39   GLU A CB  1 
ATOM   286  C CG  . GLU A 1 39  ? -108.673 63.615 -50.714 1.00 59.39 ? 39   GLU A CG  1 
ATOM   287  C CD  . GLU A 1 39  ? -107.993 64.625 -51.617 1.00 58.35 ? 39   GLU A CD  1 
ATOM   288  O OE1 . GLU A 1 39  ? -107.164 65.401 -51.100 1.00 58.12 ? 39   GLU A OE1 1 
ATOM   289  O OE2 . GLU A 1 39  ? -108.253 64.639 -52.836 1.00 57.85 ? 39   GLU A OE2 1 
ATOM   290  N N   . THR A 1 40  ? -109.733 61.044 -48.478 1.00 59.00 ? 40   THR A N   1 
ATOM   291  C CA  . THR A 1 40  ? -109.610 60.698 -47.071 1.00 58.00 ? 40   THR A CA  1 
ATOM   292  C C   . THR A 1 40  ? -108.665 61.653 -46.352 1.00 57.39 ? 40   THR A C   1 
ATOM   293  O O   . THR A 1 40  ? -107.519 61.840 -46.764 1.00 57.10 ? 40   THR A O   1 
ATOM   294  C CB  . THR A 1 40  ? -109.103 59.235 -46.937 1.00 58.00 ? 40   THR A CB  1 
ATOM   295  O OG1 . THR A 1 40  ? -109.990 58.348 -47.632 1.00 57.68 ? 40   THR A OG1 1 
ATOM   296  C CG2 . THR A 1 40  ? -109.152 58.754 -45.485 1.00 57.55 ? 40   THR A CG2 1 
ATOM   297  N N   . CYS A 1 41  ? -109.152 62.261 -45.276 1.00 56.87 ? 41   CYS A N   1 
ATOM   298  C CA  . CYS A 1 41  ? -108.270 62.994 -44.378 1.00 56.44 ? 41   CYS A CA  1 
ATOM   299  C C   . CYS A 1 41  ? -108.230 62.345 -43.010 1.00 55.30 ? 41   CYS A C   1 
ATOM   300  O O   . CYS A 1 41  ? -109.268 62.029 -42.426 1.00 55.29 ? 41   CYS A O   1 
ATOM   301  C CB  . CYS A 1 41  ? -108.652 64.469 -44.271 1.00 56.94 ? 41   CYS A CB  1 
ATOM   302  S SG  . CYS A 1 41  ? -107.260 65.581 -44.603 1.00 59.31 ? 41   CYS A SG  1 
ATOM   303  N N   . VAL A 1 42  ? -107.010 62.121 -42.535 1.00 54.02 ? 42   VAL A N   1 
ATOM   304  C CA  . VAL A 1 42  ? -106.758 61.572 -41.213 1.00 52.68 ? 42   VAL A CA  1 
ATOM   305  C C   . VAL A 1 42  ? -105.764 62.485 -40.517 1.00 51.76 ? 42   VAL A C   1 
ATOM   306  O O   . VAL A 1 42  ? -104.883 63.052 -41.157 1.00 51.75 ? 42   VAL A O   1 
ATOM   307  C CB  . VAL A 1 42  ? -106.170 60.141 -41.275 1.00 52.70 ? 42   VAL A CB  1 
ATOM   308  C CG1 . VAL A 1 42  ? -106.162 59.522 -39.903 1.00 52.93 ? 42   VAL A CG1 1 
ATOM   309  C CG2 . VAL A 1 42  ? -106.949 59.248 -42.237 1.00 52.25 ? 42   VAL A CG2 1 
ATOM   310  N N   . GLU A 1 43  ? -105.925 62.646 -39.210 1.00 50.71 ? 43   GLU A N   1 
ATOM   311  C CA  . GLU A 1 43  ? -104.910 63.300 -38.400 1.00 49.72 ? 43   GLU A CA  1 
ATOM   312  C C   . GLU A 1 43  ? -104.809 62.653 -37.023 1.00 48.31 ? 43   GLU A C   1 
ATOM   313  O O   . GLU A 1 43  ? -105.806 62.495 -36.318 1.00 48.02 ? 43   GLU A O   1 
ATOM   314  C CB  . GLU A 1 43  ? -105.160 64.806 -38.291 1.00 50.33 ? 43   GLU A CB  1 
ATOM   315  C CG  . GLU A 1 43  ? -103.955 65.656 -38.691 1.00 52.38 ? 43   GLU A CG  1 
ATOM   316  C CD  . GLU A 1 43  ? -104.319 67.096 -39.039 1.00 54.56 ? 43   GLU A CD  1 
ATOM   317  O OE1 . GLU A 1 43  ? -104.858 67.811 -38.163 1.00 56.49 ? 43   GLU A OE1 1 
ATOM   318  O OE2 . GLU A 1 43  ? -104.061 67.526 -40.183 1.00 54.93 ? 43   GLU A OE2 1 
ATOM   319  N N   . ILE A 1 44  ? -103.588 62.263 -36.671 1.00 46.68 ? 44   ILE A N   1 
ATOM   320  C CA  . ILE A 1 44  ? -103.268 61.691 -35.370 1.00 44.75 ? 44   ILE A CA  1 
ATOM   321  C C   . ILE A 1 44  ? -103.353 62.798 -34.321 1.00 43.62 ? 44   ILE A C   1 
ATOM   322  O O   . ILE A 1 44  ? -102.533 63.726 -34.313 1.00 43.34 ? 44   ILE A O   1 
ATOM   323  C CB  . ILE A 1 44  ? -101.850 61.056 -35.408 1.00 44.72 ? 44   ILE A CB  1 
ATOM   324  C CG1 . ILE A 1 44  ? -101.642 60.231 -36.699 1.00 44.53 ? 44   ILE A CG1 1 
ATOM   325  C CG2 . ILE A 1 44  ? -101.574 60.226 -34.155 1.00 44.37 ? 44   ILE A CG2 1 
ATOM   326  C CD1 . ILE A 1 44  ? -102.541 58.985 -36.851 1.00 43.83 ? 44   ILE A CD1 1 
ATOM   327  N N   . GLY A 1 45  ? -104.354 62.693 -33.442 1.00 42.30 ? 45   GLY A N   1 
ATOM   328  C CA  . GLY A 1 45  ? -104.626 63.703 -32.432 1.00 40.62 ? 45   GLY A CA  1 
ATOM   329  C C   . GLY A 1 45  ? -103.776 63.608 -31.179 1.00 39.70 ? 45   GLY A C   1 
ATOM   330  O O   . GLY A 1 45  ? -104.096 64.221 -30.170 1.00 39.91 ? 45   GLY A O   1 
ATOM   331  N N   . GLU A 1 46  ? -102.696 62.836 -31.230 1.00 38.68 ? 46   GLU A N   1 
ATOM   332  C CA  . GLU A 1 46  ? -101.759 62.736 -30.110 1.00 37.51 ? 46   GLU A CA  1 
ATOM   333  C C   . GLU A 1 46  ? -100.401 62.237 -30.595 1.00 36.61 ? 46   GLU A C   1 
ATOM   334  O O   . GLU A 1 46  ? -100.307 61.606 -31.644 1.00 36.33 ? 46   GLU A O   1 
ATOM   335  C CB  . GLU A 1 46  ? -102.296 61.801 -29.022 1.00 37.41 ? 46   GLU A CB  1 
ATOM   336  C CG  . GLU A 1 46  ? -102.657 60.405 -29.510 1.00 37.64 ? 46   GLU A CG  1 
ATOM   337  C CD  . GLU A 1 46  ? -103.284 59.568 -28.417 1.00 38.13 ? 46   GLU A CD  1 
ATOM   338  O OE1 . GLU A 1 46  ? -102.527 59.053 -27.583 1.00 39.18 ? 46   GLU A OE1 1 
ATOM   339  O OE2 . GLU A 1 46  ? -104.524 59.438 -28.372 1.00 38.12 ? 46   GLU A OE2 1 
ATOM   340  N N   . SER A 1 47  ? -99.360  62.524 -29.817 1.00 35.51 ? 47   SER A N   1 
ATOM   341  C CA  . SER A 1 47  ? -98.003  62.125 -30.142 1.00 34.34 ? 47   SER A CA  1 
ATOM   342  C C   . SER A 1 47  ? -97.863  60.609 -30.064 1.00 33.80 ? 47   SER A C   1 
ATOM   343  O O   . SER A 1 47  ? -98.306  59.987 -29.098 1.00 34.08 ? 47   SER A O   1 
ATOM   344  C CB  . SER A 1 47  ? -97.021  62.803 -29.196 1.00 34.20 ? 47   SER A CB  1 
ATOM   345  O OG  . SER A 1 47  ? -95.761  62.158 -29.223 1.00 34.58 ? 47   SER A OG  1 
ATOM   346  N N   . VAL A 1 48  ? -97.257  60.020 -31.087 1.00 32.69 ? 48   VAL A N   1 
ATOM   347  C CA  . VAL A 1 48  ? -97.003  58.584 -31.111 1.00 32.06 ? 48   VAL A CA  1 
ATOM   348  C C   . VAL A 1 48  ? -95.500  58.313 -31.136 1.00 31.95 ? 48   VAL A C   1 
ATOM   349  O O   . VAL A 1 48  ? -95.059  57.178 -31.329 1.00 31.56 ? 48   VAL A O   1 
ATOM   350  C CB  . VAL A 1 48  ? -97.710  57.892 -32.294 1.00 31.92 ? 48   VAL A CB  1 
ATOM   351  C CG1 . VAL A 1 48  ? -99.219  58.008 -32.150 1.00 31.45 ? 48   VAL A CG1 1 
ATOM   352  C CG2 . VAL A 1 48  ? -97.241  58.470 -33.643 1.00 32.03 ? 48   VAL A CG2 1 
ATOM   353  N N   . ARG A 1 49  ? -94.728  59.377 -30.911 1.00 32.11 ? 49   ARG A N   1 
ATOM   354  C CA  . ARG A 1 49  ? -93.268  59.344 -30.944 1.00 32.31 ? 49   ARG A CA  1 
ATOM   355  C C   . ARG A 1 49  ? -92.696  58.289 -30.011 1.00 32.55 ? 49   ARG A C   1 
ATOM   356  O O   . ARG A 1 49  ? -93.004  58.279 -28.826 1.00 32.38 ? 49   ARG A O   1 
ATOM   357  C CB  . ARG A 1 49  ? -92.729  60.716 -30.561 1.00 32.34 ? 49   ARG A CB  1 
ATOM   358  C CG  . ARG A 1 49  ? -91.294  60.947 -30.943 1.00 31.79 ? 49   ARG A CG  1 
ATOM   359  C CD  . ARG A 1 49  ? -90.844  62.342 -30.664 1.00 31.38 ? 49   ARG A CD  1 
ATOM   360  N NE  . ARG A 1 49  ? -91.304  63.282 -31.682 1.00 31.43 ? 49   ARG A NE  1 
ATOM   361  C CZ  . ARG A 1 49  ? -90.622  63.601 -32.777 1.00 32.14 ? 49   ARG A CZ  1 
ATOM   362  N NH1 . ARG A 1 49  ? -89.427  63.055 -33.038 1.00 31.93 ? 49   ARG A NH1 1 
ATOM   363  N NH2 . ARG A 1 49  ? -91.142  64.475 -33.621 1.00 33.01 ? 49   ARG A NH2 1 
ATOM   364  N N   . GLY A 1 50  ? -91.881  57.391 -30.556 1.00 33.09 ? 50   GLY A N   1 
ATOM   365  C CA  . GLY A 1 50  ? -91.324  56.293 -29.778 1.00 33.54 ? 50   GLY A CA  1 
ATOM   366  C C   . GLY A 1 50  ? -92.313  55.243 -29.286 1.00 33.95 ? 50   GLY A C   1 
ATOM   367  O O   . GLY A 1 50  ? -91.990  54.460 -28.400 1.00 34.34 ? 50   GLY A O   1 
ATOM   368  N N   . GLU A 1 51  ? -93.509  55.189 -29.858 1.00 34.18 ? 51   GLU A N   1 
ATOM   369  C CA  . GLU A 1 51  ? -94.491  54.205 -29.395 1.00 34.58 ? 51   GLU A CA  1 
ATOM   370  C C   . GLU A 1 51  ? -94.692  53.004 -30.310 1.00 33.92 ? 51   GLU A C   1 
ATOM   371  O O   . GLU A 1 51  ? -94.428  53.069 -31.513 1.00 34.04 ? 51   GLU A O   1 
ATOM   372  C CB  . GLU A 1 51  ? -95.832  54.877 -29.125 1.00 35.31 ? 51   GLU A CB  1 
ATOM   373  C CG  . GLU A 1 51  ? -95.690  56.160 -28.335 1.00 37.98 ? 51   GLU A CG  1 
ATOM   374  C CD  . GLU A 1 51  ? -96.932  56.487 -27.557 1.00 41.73 ? 51   GLU A CD  1 
ATOM   375  O OE1 . GLU A 1 51  ? -98.033  56.459 -28.158 1.00 43.16 ? 51   GLU A OE1 1 
ATOM   376  O OE2 . GLU A 1 51  ? -96.800  56.766 -26.345 1.00 44.02 ? 51   GLU A OE2 1 
ATOM   377  N N   . ASP A 1 52  ? -95.166  51.914 -29.710 1.00 33.06 ? 52   ASP A N   1 
ATOM   378  C CA  . ASP A 1 52  ? -95.537  50.689 -30.409 1.00 32.46 ? 52   ASP A CA  1 
ATOM   379  C C   . ASP A 1 52  ? -97.007  50.806 -30.874 1.00 31.72 ? 52   ASP A C   1 
ATOM   380  O O   . ASP A 1 52  ? -97.936  50.600 -30.101 1.00 31.04 ? 52   ASP A O   1 
ATOM   381  C CB  . ASP A 1 52  ? -95.341  49.501 -29.455 1.00 32.67 ? 52   ASP A CB  1 
ATOM   382  C CG  . ASP A 1 52  ? -95.326  48.151 -30.161 1.00 33.99 ? 52   ASP A CG  1 
ATOM   383  O OD1 . ASP A 1 52  ? -94.983  48.080 -31.360 1.00 34.94 ? 52   ASP A OD1 1 
ATOM   384  O OD2 . ASP A 1 52  ? -95.630  47.082 -29.576 1.00 35.18 ? 52   ASP A OD2 1 
ATOM   385  N N   . VAL A 1 53  ? -97.212  51.150 -32.140 1.00 31.24 ? 53   VAL A N   1 
ATOM   386  C CA  . VAL A 1 53  ? -98.555  51.481 -32.623 1.00 30.98 ? 53   VAL A CA  1 
ATOM   387  C C   . VAL A 1 53  ? -99.294  50.321 -33.301 1.00 31.03 ? 53   VAL A C   1 
ATOM   388  O O   . VAL A 1 53  ? -98.730  49.608 -34.125 1.00 31.07 ? 53   VAL A O   1 
ATOM   389  C CB  . VAL A 1 53  ? -98.518  52.720 -33.525 1.00 30.74 ? 53   VAL A CB  1 
ATOM   390  C CG1 . VAL A 1 53  ? -99.863  52.971 -34.213 1.00 29.80 ? 53   VAL A CG1 1 
ATOM   391  C CG2 . VAL A 1 53  ? -98.094  53.930 -32.695 1.00 31.22 ? 53   VAL A CG2 1 
ATOM   392  N N   . TYR A 1 54  ? -100.560 50.150 -32.936 1.00 31.12 ? 54   TYR A N   1 
ATOM   393  C CA  . TYR A 1 54  ? -101.431 49.167 -33.566 1.00 31.39 ? 54   TYR A CA  1 
ATOM   394  C C   . TYR A 1 54  ? -102.644 49.878 -34.174 1.00 32.21 ? 54   TYR A C   1 
ATOM   395  O O   . TYR A 1 54  ? -103.394 50.575 -33.476 1.00 31.93 ? 54   TYR A O   1 
ATOM   396  C CB  . TYR A 1 54  ? -101.841 48.083 -32.550 1.00 30.93 ? 54   TYR A CB  1 
ATOM   397  C CG  . TYR A 1 54  ? -100.635 47.361 -32.014 1.00 30.33 ? 54   TYR A CG  1 
ATOM   398  C CD1 . TYR A 1 54  ? -99.821  47.948 -31.032 1.00 29.57 ? 54   TYR A CD1 1 
ATOM   399  C CD2 . TYR A 1 54  ? -100.268 46.112 -32.521 1.00 30.09 ? 54   TYR A CD2 1 
ATOM   400  C CE1 . TYR A 1 54  ? -98.689  47.304 -30.563 1.00 29.71 ? 54   TYR A CE1 1 
ATOM   401  C CE2 . TYR A 1 54  ? -99.133  45.457 -32.060 1.00 30.35 ? 54   TYR A CE2 1 
ATOM   402  C CZ  . TYR A 1 54  ? -98.347  46.061 -31.083 1.00 30.52 ? 54   TYR A CZ  1 
ATOM   403  O OH  . TYR A 1 54  ? -97.225  45.413 -30.625 1.00 30.93 ? 54   TYR A OH  1 
ATOM   404  N N   . ILE A 1 55  ? -102.813 49.724 -35.485 1.00 33.21 ? 55   ILE A N   1 
ATOM   405  C CA  . ILE A 1 55  ? -103.962 50.295 -36.168 1.00 34.29 ? 55   ILE A CA  1 
ATOM   406  C C   . ILE A 1 55  ? -104.895 49.192 -36.606 1.00 35.98 ? 55   ILE A C   1 
ATOM   407  O O   . ILE A 1 55  ? -104.523 48.340 -37.409 1.00 36.14 ? 55   ILE A O   1 
ATOM   408  C CB  . ILE A 1 55  ? -103.535 51.158 -37.371 1.00 33.86 ? 55   ILE A CB  1 
ATOM   409  C CG1 . ILE A 1 55  ? -102.564 52.248 -36.916 1.00 32.43 ? 55   ILE A CG1 1 
ATOM   410  C CG2 . ILE A 1 55  ? -104.780 51.755 -38.072 1.00 32.94 ? 55   ILE A CG2 1 
ATOM   411  C CD1 . ILE A 1 55  ? -101.729 52.785 -37.999 1.00 31.63 ? 55   ILE A CD1 1 
ATOM   412  N N   . VAL A 1 56  ? -106.109 49.215 -36.076 1.00 38.14 ? 56   VAL A N   1 
ATOM   413  C CA  . VAL A 1 56  ? -107.086 48.197 -36.396 1.00 41.03 ? 56   VAL A CA  1 
ATOM   414  C C   . VAL A 1 56  ? -107.953 48.690 -37.541 1.00 43.68 ? 56   VAL A C   1 
ATOM   415  O O   . VAL A 1 56  ? -108.563 49.752 -37.453 1.00 43.52 ? 56   VAL A O   1 
ATOM   416  C CB  . VAL A 1 56  ? -107.928 47.808 -35.168 1.00 40.79 ? 56   VAL A CB  1 
ATOM   417  C CG1 . VAL A 1 56  ? -108.869 46.640 -35.489 1.00 40.23 ? 56   VAL A CG1 1 
ATOM   418  C CG2 . VAL A 1 56  ? -107.019 47.450 -34.012 1.00 40.37 ? 56   VAL A CG2 1 
ATOM   419  N N   . GLN A 1 57  ? -107.967 47.903 -38.617 1.00 47.18 ? 57   GLN A N   1 
ATOM   420  C CA  . GLN A 1 57  ? -108.725 48.158 -39.850 1.00 50.75 ? 57   GLN A CA  1 
ATOM   421  C C   . GLN A 1 57  ? -110.157 48.612 -39.605 1.00 52.72 ? 57   GLN A C   1 
ATOM   422  O O   . GLN A 1 57  ? -110.727 48.319 -38.546 1.00 53.54 ? 57   GLN A O   1 
ATOM   423  C CB  . GLN A 1 57  ? -108.727 46.874 -40.697 1.00 51.31 ? 57   GLN A CB  1 
ATOM   424  C CG  . GLN A 1 57  ? -110.068 46.071 -40.828 1.00 53.53 ? 57   GLN A CG  1 
ATOM   425  C CD  . GLN A 1 57  ? -110.880 45.870 -39.529 1.00 55.82 ? 57   GLN A CD  1 
ATOM   426  O OE1 . GLN A 1 57  ? -112.111 45.755 -39.572 1.00 56.88 ? 57   GLN A OE1 1 
ATOM   427  N NE2 . GLN A 1 57  ? -110.199 45.815 -38.396 1.00 56.83 ? 57   GLN A NE2 1 
ATOM   428  N N   . SER A 1 58  ? -110.752 49.313 -40.571 1.00 54.67 ? 58   SER A N   1 
ATOM   429  C CA  . SER A 1 58  ? -112.199 49.574 -40.503 1.00 56.20 ? 58   SER A CA  1 
ATOM   430  C C   . SER A 1 58  ? -113.034 48.407 -41.034 1.00 56.91 ? 58   SER A C   1 
ATOM   431  O O   . SER A 1 58  ? -112.541 47.560 -41.782 1.00 57.24 ? 58   SER A O   1 
ATOM   432  C CB  . SER A 1 58  ? -112.587 50.864 -41.224 1.00 56.34 ? 58   SER A CB  1 
ATOM   433  O OG  . SER A 1 58  ? -113.645 51.495 -40.514 1.00 56.57 ? 58   SER A OG  1 
ATOM   434  N N   . GLY A 1 59  ? -114.300 48.368 -40.635 1.00 57.59 ? 59   GLY A N   1 
ATOM   435  C CA  . GLY A 1 59  ? -115.219 47.351 -41.117 1.00 58.11 ? 59   GLY A CA  1 
ATOM   436  C C   . GLY A 1 59  ? -116.375 47.955 -41.890 1.00 58.21 ? 59   GLY A C   1 
ATOM   437  O O   . GLY A 1 59  ? -117.443 47.336 -42.007 1.00 58.56 ? 59   GLY A O   1 
ATOM   438  N N   . CYS A 1 60  ? -116.160 49.167 -42.408 1.00 57.84 ? 60   CYS A N   1 
ATOM   439  C CA  . CYS A 1 60  ? -117.209 49.921 -43.099 1.00 57.23 ? 60   CYS A CA  1 
ATOM   440  C C   . CYS A 1 60  ? -117.228 49.672 -44.605 1.00 55.44 ? 60   CYS A C   1 
ATOM   441  O O   . CYS A 1 60  ? -117.038 50.597 -45.411 1.00 55.85 ? 60   CYS A O   1 
ATOM   442  C CB  . CYS A 1 60  ? -117.121 51.422 -42.785 1.00 58.05 ? 60   CYS A CB  1 
ATOM   443  S SG  . CYS A 1 60  ? -115.476 52.128 -43.007 1.00 61.57 ? 60   CYS A SG  1 
ATOM   444  N N   . GLY A 1 61  ? -117.446 48.411 -44.966 1.00 52.93 ? 61   GLY A N   1 
ATOM   445  C CA  . GLY A 1 61  ? -117.819 48.047 -46.316 1.00 49.78 ? 61   GLY A CA  1 
ATOM   446  C C   . GLY A 1 61  ? -116.812 48.484 -47.345 1.00 47.14 ? 61   GLY A C   1 
ATOM   447  O O   . GLY A 1 61  ? -115.962 47.675 -47.729 1.00 47.92 ? 61   GLY A O   1 
ATOM   448  N N   . GLU A 1 62  ? -116.898 49.750 -47.764 1.00 43.78 ? 62   GLU A N   1 
ATOM   449  C CA  . GLU A 1 62  ? -116.079 50.297 -48.855 1.00 40.45 ? 62   GLU A CA  1 
ATOM   450  C C   . GLU A 1 62  ? -114.580 50.006 -48.724 1.00 38.08 ? 62   GLU A C   1 
ATOM   451  O O   . GLU A 1 62  ? -113.840 50.741 -48.078 1.00 37.61 ? 62   GLU A O   1 
ATOM   452  C CB  . GLU A 1 62  ? -116.346 51.791 -49.059 1.00 40.03 ? 62   GLU A CB  1 
ATOM   453  C CG  . GLU A 1 62  ? -116.723 52.136 -50.492 1.00 39.05 ? 62   GLU A CG  1 
ATOM   454  C CD  . GLU A 1 62  ? -115.531 52.196 -51.457 1.00 37.64 ? 62   GLU A CD  1 
ATOM   455  O OE1 . GLU A 1 62  ? -114.433 51.697 -51.137 1.00 36.43 ? 62   GLU A OE1 1 
ATOM   456  O OE2 . GLU A 1 62  ? -115.689 52.759 -52.558 1.00 37.14 ? 62   GLU A OE2 1 
ATOM   457  N N   . ILE A 1 63  ? -114.164 48.925 -49.375 1.00 35.75 ? 63   ILE A N   1 
ATOM   458  C CA  . ILE A 1 63  ? -112.825 48.354 -49.242 1.00 33.77 ? 63   ILE A CA  1 
ATOM   459  C C   . ILE A 1 63  ? -111.685 49.310 -49.625 1.00 32.52 ? 63   ILE A C   1 
ATOM   460  O O   . ILE A 1 63  ? -110.676 49.387 -48.911 1.00 33.05 ? 63   ILE A O   1 
ATOM   461  C CB  . ILE A 1 63  ? -112.749 47.016 -50.022 1.00 33.53 ? 63   ILE A CB  1 
ATOM   462  C CG1 . ILE A 1 63  ? -111.487 46.235 -49.656 1.00 33.78 ? 63   ILE A CG1 1 
ATOM   463  C CG2 . ILE A 1 63  ? -112.840 47.245 -51.526 1.00 33.00 ? 63   ILE A CG2 1 
ATOM   464  C CD1 . ILE A 1 63  ? -111.334 44.871 -50.392 1.00 33.16 ? 63   ILE A CD1 1 
ATOM   465  N N   . ASN A 1 64  ? -111.852 50.043 -50.722 1.00 30.37 ? 64   ASN A N   1 
ATOM   466  C CA  . ASN A 1 64  ? -110.849 51.006 -51.167 1.00 29.05 ? 64   ASN A CA  1 
ATOM   467  C C   . ASN A 1 64  ? -110.669 52.211 -50.226 1.00 28.81 ? 64   ASN A C   1 
ATOM   468  O O   . ASN A 1 64  ? -109.539 52.679 -50.014 1.00 28.96 ? 64   ASN A O   1 
ATOM   469  C CB  . ASN A 1 64  ? -111.123 51.427 -52.614 1.00 28.37 ? 64   ASN A CB  1 
ATOM   470  C CG  . ASN A 1 64  ? -111.196 50.217 -53.563 1.00 27.15 ? 64   ASN A CG  1 
ATOM   471  O OD1 . ASN A 1 64  ? -110.390 49.281 -53.458 1.00 24.62 ? 64   ASN A OD1 1 
ATOM   472  N ND2 . ASN A 1 64  ? -112.176 50.223 -54.473 1.00 25.64 ? 64   ASN A ND2 1 
ATOM   473  N N   . ASP A 1 65  ? -111.772 52.690 -49.651 1.00 28.24 ? 65   ASP A N   1 
ATOM   474  C CA  . ASP A 1 65  ? -111.738 53.747 -48.651 1.00 27.81 ? 65   ASP A CA  1 
ATOM   475  C C   . ASP A 1 65  ? -111.049 53.252 -47.398 1.00 27.28 ? 65   ASP A C   1 
ATOM   476  O O   . ASP A 1 65  ? -110.232 53.966 -46.822 1.00 26.87 ? 65   ASP A O   1 
ATOM   477  C CB  . ASP A 1 65  ? -113.157 54.204 -48.278 1.00 28.14 ? 65   ASP A CB  1 
ATOM   478  C CG  . ASP A 1 65  ? -113.833 55.010 -49.373 1.00 28.30 ? 65   ASP A CG  1 
ATOM   479  O OD1 . ASP A 1 65  ? -113.131 55.642 -50.195 1.00 27.20 ? 65   ASP A OD1 1 
ATOM   480  O OD2 . ASP A 1 65  ? -115.082 55.067 -49.474 1.00 29.20 ? 65   ASP A OD2 1 
ATOM   481  N N   . ASN A 1 66  ? -111.391 52.037 -46.969 1.00 27.13 ? 66   ASN A N   1 
ATOM   482  C CA  . ASN A 1 66  ? -110.786 51.456 -45.768 1.00 27.18 ? 66   ASN A CA  1 
ATOM   483  C C   . ASN A 1 66  ? -109.294 51.250 -45.904 1.00 26.24 ? 66   ASN A C   1 
ATOM   484  O O   . ASN A 1 66  ? -108.546 51.572 -44.990 1.00 26.11 ? 66   ASN A O   1 
ATOM   485  C CB  . ASN A 1 66  ? -111.434 50.136 -45.413 1.00 27.76 ? 66   ASN A CB  1 
ATOM   486  C CG  . ASN A 1 66  ? -112.737 50.322 -44.718 1.00 31.17 ? 66   ASN A CG  1 
ATOM   487  O OD1 . ASN A 1 66  ? -113.205 51.456 -44.544 1.00 33.93 ? 66   ASN A OD1 1 
ATOM   488  N ND2 . ASN A 1 66  ? -113.360 49.211 -44.315 1.00 34.38 ? 66   ASN A ND2 1 
ATOM   489  N N   . LEU A 1 67  ? -108.882 50.714 -47.050 1.00 25.26 ? 67   LEU A N   1 
ATOM   490  C CA  . LEU A 1 67  ? -107.477 50.513 -47.353 1.00 24.72 ? 67   LEU A CA  1 
ATOM   491  C C   . LEU A 1 67  ? -106.712 51.849 -47.392 1.00 24.70 ? 67   LEU A C   1 
ATOM   492  O O   . LEU A 1 67  ? -105.662 51.989 -46.768 1.00 24.57 ? 67   LEU A O   1 
ATOM   493  C CB  . LEU A 1 67  ? -107.335 49.733 -48.664 1.00 24.37 ? 67   LEU A CB  1 
ATOM   494  C CG  . LEU A 1 67  ? -105.930 49.456 -49.189 1.00 23.01 ? 67   LEU A CG  1 
ATOM   495  C CD1 . LEU A 1 67  ? -105.114 48.637 -48.180 1.00 22.00 ? 67   LEU A CD1 1 
ATOM   496  C CD2 . LEU A 1 67  ? -106.027 48.766 -50.532 1.00 21.28 ? 67   LEU A CD2 1 
ATOM   497  N N   . MET A 1 68  ? -107.247 52.845 -48.084 1.00 24.86 ? 68   MET A N   1 
ATOM   498  C CA  . MET A 1 68  ? -106.559 54.134 -48.125 1.00 25.41 ? 68   MET A CA  1 
ATOM   499  C C   . MET A 1 68  ? -106.405 54.758 -46.730 1.00 24.94 ? 68   MET A C   1 
ATOM   500  O O   . MET A 1 68  ? -105.300 55.180 -46.347 1.00 25.00 ? 68   MET A O   1 
ATOM   501  C CB  . MET A 1 68  ? -107.229 55.094 -49.109 1.00 26.06 ? 68   MET A CB  1 
ATOM   502  C CG  . MET A 1 68  ? -106.722 54.937 -50.529 1.00 29.39 ? 68   MET A CG  1 
ATOM   503  S SD  . MET A 1 68  ? -104.893 55.146 -50.752 1.00 35.37 ? 68   MET A SD  1 
ATOM   504  C CE  . MET A 1 68  ? -104.610 56.825 -50.124 1.00 33.44 ? 68   MET A CE  1 
ATOM   505  N N   . GLU A 1 69  ? -107.496 54.789 -45.965 1.00 24.22 ? 69   GLU A N   1 
ATOM   506  C CA  . GLU A 1 69  ? -107.451 55.278 -44.591 1.00 23.84 ? 69   GLU A CA  1 
ATOM   507  C C   . GLU A 1 69  ? -106.393 54.556 -43.744 1.00 22.87 ? 69   GLU A C   1 
ATOM   508  O O   . GLU A 1 69  ? -105.634 55.184 -43.009 1.00 22.31 ? 69   GLU A O   1 
ATOM   509  C CB  . GLU A 1 69  ? -108.821 55.172 -43.926 1.00 24.36 ? 69   GLU A CB  1 
ATOM   510  C CG  . GLU A 1 69  ? -108.837 55.843 -42.561 1.00 26.86 ? 69   GLU A CG  1 
ATOM   511  C CD  . GLU A 1 69  ? -110.176 55.790 -41.859 1.00 29.99 ? 69   GLU A CD  1 
ATOM   512  O OE1 . GLU A 1 69  ? -111.019 54.938 -42.204 1.00 30.10 ? 69   GLU A OE1 1 
ATOM   513  O OE2 . GLU A 1 69  ? -110.372 56.622 -40.951 1.00 32.15 ? 69   GLU A OE2 1 
ATOM   514  N N   . LEU A 1 70  ? -106.340 53.239 -43.875 1.00 22.09 ? 70   LEU A N   1 
ATOM   515  C CA  . LEU A 1 70  ? -105.372 52.443 -43.147 1.00 21.82 ? 70   LEU A CA  1 
ATOM   516  C C   . LEU A 1 70  ? -103.954 52.813 -43.590 1.00 21.49 ? 70   LEU A C   1 
ATOM   517  O O   . LEU A 1 70  ? -103.069 53.033 -42.761 1.00 21.31 ? 70   LEU A O   1 
ATOM   518  C CB  . LEU A 1 70  ? -105.658 50.956 -43.375 1.00 21.68 ? 70   LEU A CB  1 
ATOM   519  C CG  . LEU A 1 70  ? -104.594 49.916 -43.051 1.00 22.13 ? 70   LEU A CG  1 
ATOM   520  C CD1 . LEU A 1 70  ? -104.219 49.919 -41.569 1.00 22.47 ? 70   LEU A CD1 1 
ATOM   521  C CD2 . LEU A 1 70  ? -105.118 48.551 -43.471 1.00 22.05 ? 70   LEU A CD2 1 
ATOM   522  N N   . LEU A 1 71  ? -103.760 52.908 -44.901 1.00 21.02 ? 71   LEU A N   1 
ATOM   523  C CA  . LEU A 1 71  ? -102.474 53.269 -45.459 1.00 20.91 ? 71   LEU A CA  1 
ATOM   524  C C   . LEU A 1 71  ? -102.024 54.648 -44.978 1.00 21.28 ? 71   LEU A C   1 
ATOM   525  O O   . LEU A 1 71  ? -100.877 54.819 -44.535 1.00 20.94 ? 71   LEU A O   1 
ATOM   526  C CB  . LEU A 1 71  ? -102.527 53.202 -46.990 1.00 20.95 ? 71   LEU A CB  1 
ATOM   527  C CG  . LEU A 1 71  ? -102.640 51.803 -47.613 1.00 20.21 ? 71   LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 71  ? -102.800 51.977 -49.083 1.00 21.62 ? 71   LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 71  ? -101.424 50.953 -47.345 1.00 19.46 ? 71   LEU A CD2 1 
ATOM   530  N N   . ILE A 1 72  ? -102.935 55.621 -45.046 1.00 21.77 ? 72   ILE A N   1 
ATOM   531  C CA  . ILE A 1 72  ? -102.648 56.983 -44.610 1.00 22.54 ? 72   ILE A CA  1 
ATOM   532  C C   . ILE A 1 72  ? -102.369 57.022 -43.110 1.00 23.59 ? 72   ILE A C   1 
ATOM   533  O O   . ILE A 1 72  ? -101.481 57.749 -42.643 1.00 24.47 ? 72   ILE A O   1 
ATOM   534  C CB  . ILE A 1 72  ? -103.826 57.937 -44.975 1.00 22.52 ? 72   ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 72  ? -103.897 58.204 -46.480 1.00 21.60 ? 72   ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 72  ? -103.708 59.253 -44.233 1.00 22.39 ? 72   ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 72  ? -105.311 58.549 -46.946 1.00 21.90 ? 72   ILE A CD1 1 
ATOM   538  N N   . MET A 1 73  ? -103.119 56.249 -42.336 1.00 24.25 ? 73   MET A N   1 
ATOM   539  C CA  . MET A 1 73  ? -102.839 56.188 -40.914 1.00 25.38 ? 73   MET A CA  1 
ATOM   540  C C   . MET A 1 73  ? -101.437 55.617 -40.661 1.00 25.61 ? 73   MET A C   1 
ATOM   541  O O   . MET A 1 73  ? -100.660 56.223 -39.947 1.00 26.05 ? 73   MET A O   1 
ATOM   542  C CB  . MET A 1 73  ? -103.907 55.391 -40.180 1.00 25.90 ? 73   MET A CB  1 
ATOM   543  C CG  . MET A 1 73  ? -105.137 56.186 -39.897 1.00 28.46 ? 73   MET A CG  1 
ATOM   544  S SD  . MET A 1 73  ? -106.116 55.472 -38.557 1.00 34.14 ? 73   MET A SD  1 
ATOM   545  C CE  . MET A 1 73  ? -106.934 54.173 -39.538 1.00 32.64 ? 73   MET A CE  1 
ATOM   546  N N   . ILE A 1 74  ? -101.118 54.463 -41.250 1.00 25.76 ? 74   ILE A N   1 
ATOM   547  C CA  . ILE A 1 74  ? -99.790  53.868 -41.118 1.00 25.99 ? 74   ILE A CA  1 
ATOM   548  C C   . ILE A 1 74  ? -98.709  54.890 -41.430 1.00 26.71 ? 74   ILE A C   1 
ATOM   549  O O   . ILE A 1 74  ? -97.778  55.061 -40.658 1.00 26.84 ? 74   ILE A O   1 
ATOM   550  C CB  . ILE A 1 74  ? -99.623  52.650 -42.054 1.00 25.72 ? 74   ILE A CB  1 
ATOM   551  C CG1 . ILE A 1 74  ? -100.493 51.491 -41.590 1.00 24.87 ? 74   ILE A CG1 1 
ATOM   552  C CG2 . ILE A 1 74  ? -98.157  52.201 -42.106 1.00 25.52 ? 74   ILE A CG2 1 
ATOM   553  C CD1 . ILE A 1 74  ? -100.755 50.495 -42.647 1.00 23.55 ? 74   ILE A CD1 1 
ATOM   554  N N   . ASN A 1 75  ? -98.849  55.577 -42.561 1.00 27.70 ? 75   ASN A N   1 
ATOM   555  C CA  . ASN A 1 75  ? -97.864  56.565 -42.976 1.00 28.42 ? 75   ASN A CA  1 
ATOM   556  C C   . ASN A 1 75  ? -97.723  57.687 -41.977 1.00 29.04 ? 75   ASN A C   1 
ATOM   557  O O   . ASN A 1 75  ? -96.592  58.084 -41.644 1.00 29.38 ? 75   ASN A O   1 
ATOM   558  C CB  . ASN A 1 75  ? -98.197  57.145 -44.343 1.00 28.44 ? 75   ASN A CB  1 
ATOM   559  C CG  . ASN A 1 75  ? -97.087  58.016 -44.879 1.00 29.18 ? 75   ASN A CG  1 
ATOM   560  O OD1 . ASN A 1 75  ? -97.296  59.192 -45.182 1.00 31.39 ? 75   ASN A OD1 1 
ATOM   561  N ND2 . ASN A 1 75  ? -95.889  57.457 -44.976 1.00 29.18 ? 75   ASN A ND2 1 
ATOM   562  N N   . ALA A 1 76  ? -98.868  58.192 -41.510 1.00 29.36 ? 76   ALA A N   1 
ATOM   563  C CA  . ALA A 1 76  ? -98.908  59.308 -40.565 1.00 29.57 ? 76   ALA A CA  1 
ATOM   564  C C   . ALA A 1 76  ? -98.178  58.988 -39.269 1.00 29.73 ? 76   ALA A C   1 
ATOM   565  O O   . ALA A 1 76  ? -97.443  59.829 -38.748 1.00 29.96 ? 76   ALA A O   1 
ATOM   566  C CB  . ALA A 1 76  ? -100.350 59.724 -40.282 1.00 29.64 ? 76   ALA A CB  1 
ATOM   567  N N   . CYS A 1 77  ? -98.364  57.773 -38.754 1.00 29.84 ? 77   CYS A N   1 
ATOM   568  C CA  . CYS A 1 77  ? -97.643  57.348 -37.549 1.00 30.17 ? 77   CYS A CA  1 
ATOM   569  C C   . CYS A 1 77  ? -96.135  57.218 -37.777 1.00 30.76 ? 77   CYS A C   1 
ATOM   570  O O   . CYS A 1 77  ? -95.355  57.558 -36.897 1.00 31.21 ? 77   CYS A O   1 
ATOM   571  C CB  . CYS A 1 77  ? -98.202  56.044 -36.999 1.00 29.82 ? 77   CYS A CB  1 
ATOM   572  S SG  . CYS A 1 77  ? -99.890  56.202 -36.381 1.00 29.47 ? 77   CYS A SG  1 
ATOM   573  N N   . LYS A 1 78  ? -95.736  56.746 -38.956 1.00 31.04 ? 78   LYS A N   1 
ATOM   574  C CA  . LYS A 1 78  ? -94.332  56.559 -39.290 1.00 31.41 ? 78   LYS A CA  1 
ATOM   575  C C   . LYS A 1 78  ? -93.561  57.883 -39.384 1.00 31.49 ? 78   LYS A C   1 
ATOM   576  O O   . LYS A 1 78  ? -92.519  58.049 -38.740 1.00 31.98 ? 78   LYS A O   1 
ATOM   577  C CB  . LYS A 1 78  ? -94.205  55.767 -40.588 1.00 31.88 ? 78   LYS A CB  1 
ATOM   578  C CG  . LYS A 1 78  ? -93.072  54.768 -40.599 1.00 33.91 ? 78   LYS A CG  1 
ATOM   579  C CD  . LYS A 1 78  ? -93.322  53.668 -39.575 1.00 36.46 ? 78   LYS A CD  1 
ATOM   580  C CE  . LYS A 1 78  ? -92.113  52.777 -39.421 1.00 38.29 ? 78   LYS A CE  1 
ATOM   581  N NZ  . LYS A 1 78  ? -91.816  52.059 -40.696 1.00 39.30 ? 78   LYS A NZ  1 
ATOM   582  N N   . ILE A 1 79  ? -94.065  58.836 -40.164 1.00 31.24 ? 79   ILE A N   1 
ATOM   583  C CA  . ILE A 1 79  ? -93.402  60.143 -40.261 1.00 30.79 ? 79   ILE A CA  1 
ATOM   584  C C   . ILE A 1 79  ? -93.484  60.962 -38.964 1.00 30.50 ? 79   ILE A C   1 
ATOM   585  O O   . ILE A 1 79  ? -92.750  61.942 -38.801 1.00 30.77 ? 79   ILE A O   1 
ATOM   586  C CB  . ILE A 1 79  ? -93.873  60.955 -41.503 1.00 30.76 ? 79   ILE A CB  1 
ATOM   587  C CG1 . ILE A 1 79  ? -95.344  61.350 -41.386 1.00 31.08 ? 79   ILE A CG1 1 
ATOM   588  C CG2 . ILE A 1 79  ? -93.602  60.170 -42.792 1.00 30.80 ? 79   ILE A CG2 1 
ATOM   589  C CD1 . ILE A 1 79  ? -95.850  62.181 -42.545 1.00 32.15 ? 79   ILE A CD1 1 
ATOM   590  N N   . ALA A 1 80  ? -94.360  60.549 -38.044 1.00 29.99 ? 80   ALA A N   1 
ATOM   591  C CA  . ALA A 1 80  ? -94.411  61.122 -36.694 1.00 29.22 ? 80   ALA A CA  1 
ATOM   592  C C   . ALA A 1 80  ? -93.625  60.280 -35.664 1.00 29.04 ? 80   ALA A C   1 
ATOM   593  O O   . ALA A 1 80  ? -93.879  60.333 -34.448 1.00 28.69 ? 80   ALA A O   1 
ATOM   594  C CB  . ALA A 1 80  ? -95.848  61.326 -36.265 1.00 29.14 ? 80   ALA A CB  1 
ATOM   595  N N   . SER A 1 81  ? -92.670  59.499 -36.169 1.00 29.08 ? 81   SER A N   1 
ATOM   596  C CA  . SER A 1 81  ? -91.645  58.831 -35.344 1.00 29.32 ? 81   SER A CA  1 
ATOM   597  C C   . SER A 1 81  ? -92.151  57.756 -34.386 1.00 29.54 ? 81   SER A C   1 
ATOM   598  O O   . SER A 1 81  ? -91.566  57.537 -33.308 1.00 29.80 ? 81   SER A O   1 
ATOM   599  C CB  . SER A 1 81  ? -90.786  59.849 -34.584 1.00 29.17 ? 81   SER A CB  1 
ATOM   600  O OG  . SER A 1 81  ? -90.116  60.718 -35.470 1.00 29.35 ? 81   SER A OG  1 
ATOM   601  N N   . ALA A 1 82  ? -93.226  57.079 -34.783 1.00 29.65 ? 82   ALA A N   1 
ATOM   602  C CA  . ALA A 1 82  ? -93.659  55.884 -34.076 1.00 29.93 ? 82   ALA A CA  1 
ATOM   603  C C   . ALA A 1 82  ? -92.501  54.891 -34.077 1.00 30.35 ? 82   ALA A C   1 
ATOM   604  O O   . ALA A 1 82  ? -91.747  54.767 -35.057 1.00 29.95 ? 82   ALA A O   1 
ATOM   605  C CB  . ALA A 1 82  ? -94.877  55.275 -34.729 1.00 29.70 ? 82   ALA A CB  1 
ATOM   606  N N   . SER A 1 83  ? -92.348  54.192 -32.967 1.00 30.95 ? 83   SER A N   1 
ATOM   607  C CA  . SER A 1 83  ? -91.263  53.242 -32.862 1.00 31.50 ? 83   SER A CA  1 
ATOM   608  C C   . SER A 1 83  ? -91.518  52.067 -33.787 1.00 31.20 ? 83   SER A C   1 
ATOM   609  O O   . SER A 1 83  ? -90.601  51.594 -34.433 1.00 31.56 ? 83   SER A O   1 
ATOM   610  C CB  . SER A 1 83  ? -91.094  52.763 -31.431 1.00 31.98 ? 83   SER A CB  1 
ATOM   611  O OG  . SER A 1 83  ? -90.230  51.638 -31.428 1.00 34.44 ? 83   SER A OG  1 
ATOM   612  N N   . ARG A 1 84  ? -92.769  51.613 -33.854 1.00 30.74 ? 84   ARG A N   1 
ATOM   613  C CA  . ARG A 1 84  ? -93.151  50.460 -34.669 1.00 30.21 ? 84   ARG A CA  1 
ATOM   614  C C   . ARG A 1 84  ? -94.614  50.613 -35.045 1.00 28.96 ? 84   ARG A C   1 
ATOM   615  O O   . ARG A 1 84  ? -95.406  51.131 -34.254 1.00 28.89 ? 84   ARG A O   1 
ATOM   616  C CB  . ARG A 1 84  ? -92.928  49.163 -33.883 1.00 30.98 ? 84   ARG A CB  1 
ATOM   617  C CG  . ARG A 1 84  ? -93.157  47.860 -34.650 1.00 34.09 ? 84   ARG A CG  1 
ATOM   618  C CD  . ARG A 1 84  ? -92.562  46.600 -33.974 1.00 38.39 ? 84   ARG A CD  1 
ATOM   619  N NE  . ARG A 1 84  ? -93.299  46.251 -32.754 1.00 42.07 ? 84   ARG A NE  1 
ATOM   620  C CZ  . ARG A 1 84  ? -92.963  45.278 -31.902 1.00 43.39 ? 84   ARG A CZ  1 
ATOM   621  N NH1 . ARG A 1 84  ? -91.891  44.525 -32.119 1.00 44.06 ? 84   ARG A NH1 1 
ATOM   622  N NH2 . ARG A 1 84  ? -93.706  45.063 -30.824 1.00 43.72 ? 84   ARG A NH2 1 
ATOM   623  N N   . VAL A 1 85  ? -94.968  50.192 -36.258 1.00 27.39 ? 85   VAL A N   1 
ATOM   624  C CA  . VAL A 1 85  ? -96.360  50.246 -36.718 1.00 25.98 ? 85   VAL A CA  1 
ATOM   625  C C   . VAL A 1 85  ? -96.839  48.878 -37.186 1.00 25.13 ? 85   VAL A C   1 
ATOM   626  O O   . VAL A 1 85  ? -96.311  48.318 -38.139 1.00 24.91 ? 85   VAL A O   1 
ATOM   627  C CB  . VAL A 1 85  ? -96.583  51.257 -37.881 1.00 25.79 ? 85   VAL A CB  1 
ATOM   628  C CG1 . VAL A 1 85  ? -98.069  51.319 -38.256 1.00 25.20 ? 85   VAL A CG1 1 
ATOM   629  C CG2 . VAL A 1 85  ? -96.065  52.633 -37.524 1.00 25.36 ? 85   VAL A CG2 1 
ATOM   630  N N   . THR A 1 86  ? -97.851  48.358 -36.506 1.00 24.33 ? 86   THR A N   1 
ATOM   631  C CA  . THR A 1 86  ? -98.472  47.103 -36.883 1.00 23.46 ? 86   THR A CA  1 
ATOM   632  C C   . THR A 1 86  ? -99.854  47.383 -37.454 1.00 22.84 ? 86   THR A C   1 
ATOM   633  O O   . THR A 1 86  ? -100.648 48.100 -36.835 1.00 22.36 ? 86   THR A O   1 
ATOM   634  C CB  . THR A 1 86  ? -98.589  46.193 -35.641 1.00 23.53 ? 86   THR A CB  1 
ATOM   635  O OG1 . THR A 1 86  ? -97.279  45.919 -35.129 1.00 24.10 ? 86   THR A OG1 1 
ATOM   636  C CG2 . THR A 1 86  ? -99.133  44.800 -36.016 1.00 22.91 ? 86   THR A CG2 1 
ATOM   637  N N   . ALA A 1 87  ? -100.139 46.830 -38.633 1.00 22.25 ? 87   ALA A N   1 
ATOM   638  C CA  . ALA A 1 87  ? -101.521 46.823 -39.138 1.00 22.12 ? 87   ALA A CA  1 
ATOM   639  C C   . ALA A 1 87  ? -102.253 45.573 -38.651 1.00 22.09 ? 87   ALA A C   1 
ATOM   640  O O   . ALA A 1 87  ? -101.788 44.439 -38.849 1.00 21.38 ? 87   ALA A O   1 
ATOM   641  C CB  . ALA A 1 87  ? -101.566 46.929 -40.671 1.00 21.77 ? 87   ALA A CB  1 
ATOM   642  N N   . VAL A 1 88  ? -103.386 45.787 -37.984 1.00 22.50 ? 88   VAL A N   1 
ATOM   643  C CA  . VAL A 1 88  ? -104.231 44.694 -37.533 1.00 22.80 ? 88   VAL A CA  1 
ATOM   644  C C   . VAL A 1 88  ? -105.360 44.607 -38.544 1.00 23.63 ? 88   VAL A C   1 
ATOM   645  O O   . VAL A 1 88  ? -106.234 45.469 -38.570 1.00 24.17 ? 88   VAL A O   1 
ATOM   646  C CB  . VAL A 1 88  ? -104.707 44.927 -36.071 1.00 22.86 ? 88   VAL A CB  1 
ATOM   647  C CG1 . VAL A 1 88  ? -105.736 43.871 -35.604 1.00 22.03 ? 88   VAL A CG1 1 
ATOM   648  C CG2 . VAL A 1 88  ? -103.504 44.915 -35.134 1.00 22.67 ? 88   VAL A CG2 1 
ATOM   649  N N   . ILE A 1 89  ? -105.302 43.599 -39.417 1.00 24.34 ? 89   ILE A N   1 
ATOM   650  C CA  . ILE A 1 89  ? -106.241 43.472 -40.531 1.00 25.42 ? 89   ILE A CA  1 
ATOM   651  C C   . ILE A 1 89  ? -106.976 42.147 -40.487 1.00 25.96 ? 89   ILE A C   1 
ATOM   652  O O   . ILE A 1 89  ? -106.678 41.250 -41.270 1.00 25.46 ? 89   ILE A O   1 
ATOM   653  C CB  . ILE A 1 89  ? -105.545 43.561 -41.909 1.00 25.91 ? 89   ILE A CB  1 
ATOM   654  C CG1 . ILE A 1 89  ? -104.492 44.658 -41.970 1.00 26.37 ? 89   ILE A CG1 1 
ATOM   655  C CG2 . ILE A 1 89  ? -106.602 43.792 -43.027 1.00 26.74 ? 89   ILE A CG2 1 
ATOM   656  C CD1 . ILE A 1 89  ? -103.557 44.510 -43.186 1.00 26.17 ? 89   ILE A CD1 1 
ATOM   657  N N   . PRO A 1 90  ? -107.977 42.041 -39.618 1.00 27.02 ? 90   PRO A N   1 
ATOM   658  C CA  . PRO A 1 90  ? -108.632 40.757 -39.347 1.00 27.63 ? 90   PRO A CA  1 
ATOM   659  C C   . PRO A 1 90  ? -109.024 40.087 -40.660 1.00 28.10 ? 90   PRO A C   1 
ATOM   660  O O   . PRO A 1 90  ? -108.831 38.892 -40.820 1.00 28.46 ? 90   PRO A O   1 
ATOM   661  C CB  . PRO A 1 90  ? -109.880 41.165 -38.565 1.00 27.88 ? 90   PRO A CB  1 
ATOM   662  C CG  . PRO A 1 90  ? -109.555 42.504 -37.968 1.00 27.56 ? 90   PRO A CG  1 
ATOM   663  C CD  . PRO A 1 90  ? -108.603 43.159 -38.884 1.00 27.31 ? 90   PRO A CD  1 
ATOM   664  N N   . CYS A 1 91  ? -109.521 40.877 -41.607 1.00 28.40 ? 91   CYS A N   1 
ATOM   665  C CA  . CYS A 1 91  ? -109.901 40.376 -42.918 1.00 28.67 ? 91   CYS A CA  1 
ATOM   666  C C   . CYS A 1 91  ? -109.070 41.070 -44.021 1.00 28.46 ? 91   CYS A C   1 
ATOM   667  O O   . CYS A 1 91  ? -109.295 42.233 -44.340 1.00 28.78 ? 91   CYS A O   1 
ATOM   668  C CB  . CYS A 1 91  ? -111.402 40.613 -43.108 1.00 28.89 ? 91   CYS A CB  1 
ATOM   669  S SG  . CYS A 1 91  ? -112.045 39.954 -44.643 1.00 30.37 ? 91   CYS A SG  1 
ATOM   670  N N   . PHE A 1 92  ? -108.106 40.349 -44.588 1.00 28.33 ? 92   PHE A N   1 
ATOM   671  C CA  . PHE A 1 92  ? -107.116 40.932 -45.501 1.00 27.93 ? 92   PHE A CA  1 
ATOM   672  C C   . PHE A 1 92  ? -107.770 41.329 -46.837 1.00 27.92 ? 92   PHE A C   1 
ATOM   673  O O   . PHE A 1 92  ? -108.378 40.485 -47.503 1.00 27.83 ? 92   PHE A O   1 
ATOM   674  C CB  . PHE A 1 92  ? -105.943 39.961 -45.712 1.00 27.53 ? 92   PHE A CB  1 
ATOM   675  C CG  . PHE A 1 92  ? -104.750 40.581 -46.407 1.00 27.31 ? 92   PHE A CG  1 
ATOM   676  C CD1 . PHE A 1 92  ? -103.727 41.175 -45.672 1.00 26.94 ? 92   PHE A CD1 1 
ATOM   677  C CD2 . PHE A 1 92  ? -104.653 40.584 -47.802 1.00 27.06 ? 92   PHE A CD2 1 
ATOM   678  C CE1 . PHE A 1 92  ? -102.641 41.761 -46.308 1.00 26.46 ? 92   PHE A CE1 1 
ATOM   679  C CE2 . PHE A 1 92  ? -103.557 41.177 -48.451 1.00 26.45 ? 92   PHE A CE2 1 
ATOM   680  C CZ  . PHE A 1 92  ? -102.551 41.761 -47.698 1.00 26.18 ? 92   PHE A CZ  1 
ATOM   681  N N   . PRO A 1 93  ? -107.679 42.609 -47.212 1.00 27.98 ? 93   PRO A N   1 
ATOM   682  C CA  . PRO A 1 93  ? -108.353 43.097 -48.423 1.00 28.10 ? 93   PRO A CA  1 
ATOM   683  C C   . PRO A 1 93  ? -107.684 42.561 -49.679 1.00 28.03 ? 93   PRO A C   1 
ATOM   684  O O   . PRO A 1 93  ? -106.452 42.428 -49.688 1.00 28.20 ? 93   PRO A O   1 
ATOM   685  C CB  . PRO A 1 93  ? -108.212 44.631 -48.329 1.00 28.12 ? 93   PRO A CB  1 
ATOM   686  C CG  . PRO A 1 93  ? -107.050 44.882 -47.414 1.00 28.20 ? 93   PRO A CG  1 
ATOM   687  C CD  . PRO A 1 93  ? -106.957 43.688 -46.507 1.00 28.12 ? 93   PRO A CD  1 
ATOM   688  N N   . TYR A 1 94  ? -108.487 42.237 -50.697 1.00 27.72 ? 94   TYR A N   1 
ATOM   689  C CA  . TYR A 1 94  ? -108.004 41.711 -51.990 1.00 27.57 ? 94   TYR A CA  1 
ATOM   690  C C   . TYR A 1 94  ? -107.340 40.342 -51.920 1.00 28.10 ? 94   TYR A C   1 
ATOM   691  O O   . TYR A 1 94  ? -106.695 39.913 -52.886 1.00 27.87 ? 94   TYR A O   1 
ATOM   692  C CB  . TYR A 1 94  ? -107.088 42.726 -52.714 1.00 27.18 ? 94   TYR A CB  1 
ATOM   693  C CG  . TYR A 1 94  ? -107.867 43.886 -53.247 1.00 25.25 ? 94   TYR A CG  1 
ATOM   694  C CD1 . TYR A 1 94  ? -108.142 44.987 -52.440 1.00 23.87 ? 94   TYR A CD1 1 
ATOM   695  C CD2 . TYR A 1 94  ? -108.372 43.871 -54.537 1.00 23.44 ? 94   TYR A CD2 1 
ATOM   696  C CE1 . TYR A 1 94  ? -108.882 46.043 -52.906 1.00 21.92 ? 94   TYR A CE1 1 
ATOM   697  C CE2 . TYR A 1 94  ? -109.113 44.930 -55.011 1.00 22.44 ? 94   TYR A CE2 1 
ATOM   698  C CZ  . TYR A 1 94  ? -109.365 46.010 -54.185 1.00 21.28 ? 94   TYR A CZ  1 
ATOM   699  O OH  . TYR A 1 94  ? -110.111 47.057 -54.641 1.00 20.72 ? 94   TYR A OH  1 
ATOM   700  N N   . ALA A 1 95  ? -107.524 39.646 -50.797 1.00 29.06 ? 95   ALA A N   1 
ATOM   701  C CA  . ALA A 1 95  ? -106.908 38.332 -50.580 1.00 30.38 ? 95   ALA A CA  1 
ATOM   702  C C   . ALA A 1 95  ? -107.258 37.273 -51.640 1.00 31.65 ? 95   ALA A C   1 
ATOM   703  O O   . ALA A 1 95  ? -106.452 36.392 -51.917 1.00 32.01 ? 95   ALA A O   1 
ATOM   704  C CB  . ALA A 1 95  ? -107.211 37.819 -49.190 1.00 29.88 ? 95   ALA A CB  1 
ATOM   705  N N   . ARG A 1 96  ? -108.442 37.350 -52.233 1.00 33.21 ? 96   ARG A N   1 
ATOM   706  C CA  . ARG A 1 96  ? -108.790 36.430 -53.325 1.00 34.92 ? 96   ARG A CA  1 
ATOM   707  C C   . ARG A 1 96  ? -107.921 36.657 -54.562 1.00 35.30 ? 96   ARG A C   1 
ATOM   708  O O   . ARG A 1 96  ? -107.552 35.702 -55.255 1.00 35.57 ? 96   ARG A O   1 
ATOM   709  C CB  . ARG A 1 96  ? -110.270 36.539 -53.708 1.00 35.59 ? 96   ARG A CB  1 
ATOM   710  C CG  . ARG A 1 96  ? -111.208 36.011 -52.627 1.00 38.77 ? 96   ARG A CG  1 
ATOM   711  C CD  . ARG A 1 96  ? -112.387 35.214 -53.148 1.00 43.79 ? 96   ARG A CD  1 
ATOM   712  N NE  . ARG A 1 96  ? -112.849 34.265 -52.140 1.00 47.75 ? 96   ARG A NE  1 
ATOM   713  C CZ  . ARG A 1 96  ? -113.224 33.016 -52.395 1.00 49.95 ? 96   ARG A CZ  1 
ATOM   714  N NH1 . ARG A 1 96  ? -113.203 32.553 -53.639 1.00 50.62 ? 96   ARG A NH1 1 
ATOM   715  N NH2 . ARG A 1 96  ? -113.624 32.228 -51.399 1.00 51.21 ? 96   ARG A NH2 1 
ATOM   716  N N   . GLN A 1 97  ? -107.591 37.920 -54.830 1.00 35.45 ? 97   GLN A N   1 
ATOM   717  C CA  . GLN A 1 97  ? -106.759 38.263 -55.977 1.00 35.78 ? 97   GLN A CA  1 
ATOM   718  C C   . GLN A 1 97  ? -105.279 38.007 -55.657 1.00 35.36 ? 97   GLN A C   1 
ATOM   719  O O   . GLN A 1 97  ? -104.462 38.932 -55.615 1.00 34.97 ? 97   GLN A O   1 
ATOM   720  C CB  . GLN A 1 97  ? -107.041 39.706 -56.422 1.00 36.37 ? 97   GLN A CB  1 
ATOM   721  C CG  . GLN A 1 97  ? -108.419 39.874 -57.135 1.00 37.80 ? 97   GLN A CG  1 
ATOM   722  C CD  . GLN A 1 97  ? -108.865 41.336 -57.267 1.00 38.80 ? 97   GLN A CD  1 
ATOM   723  O OE1 . GLN A 1 97  ? -108.223 42.139 -57.972 1.00 38.97 ? 97   GLN A OE1 1 
ATOM   724  N NE2 . GLN A 1 97  ? -109.971 41.682 -56.598 1.00 38.89 ? 97   GLN A NE2 1 
ATOM   725  N N   . ASP A 1 98  ? -104.962 36.732 -55.427 1.00 35.35 ? 98   ASP A N   1 
ATOM   726  C CA  . ASP A 1 98  ? -103.630 36.298 -54.976 1.00 35.82 ? 98   ASP A CA  1 
ATOM   727  C C   . ASP A 1 98  ? -102.804 35.489 -56.011 1.00 36.23 ? 98   ASP A C   1 
ATOM   728  O O   . ASP A 1 98  ? -101.730 34.978 -55.691 1.00 36.20 ? 98   ASP A O   1 
ATOM   729  C CB  . ASP A 1 98  ? -103.740 35.528 -53.647 1.00 35.36 ? 98   ASP A CB  1 
ATOM   730  C CG  . ASP A 1 98  ? -104.468 34.186 -53.788 1.00 34.79 ? 98   ASP A CG  1 
ATOM   731  O OD1 . ASP A 1 98  ? -105.333 34.033 -54.678 1.00 33.77 ? 98   ASP A OD1 1 
ATOM   732  O OD2 . ASP A 1 98  ? -104.246 33.225 -53.031 1.00 34.43 ? 98   ASP A OD2 1 
ATOM   733  N N   . LYS A 1 99  ? -103.317 35.390 -57.237 1.00 36.91 ? 99   LYS A N   1 
ATOM   734  C CA  . LYS A 1 99  ? -102.648 34.708 -58.356 1.00 37.44 ? 99   LYS A CA  1 
ATOM   735  C C   . LYS A 1 99  ? -103.275 35.161 -59.673 1.00 37.68 ? 99   LYS A C   1 
ATOM   736  O O   . LYS A 1 99  ? -104.387 35.684 -59.686 1.00 37.51 ? 99   LYS A O   1 
ATOM   737  C CB  . LYS A 1 99  ? -102.746 33.181 -58.227 1.00 37.43 ? 99   LYS A CB  1 
ATOM   738  C CG  . LYS A 1 99  ? -104.161 32.648 -58.015 1.00 38.53 ? 99   LYS A CG  1 
ATOM   739  C CD  . LYS A 1 99  ? -104.237 31.152 -58.268 1.00 41.01 ? 99   LYS A CD  1 
ATOM   740  C CE  . LYS A 1 99  ? -105.224 30.450 -57.323 1.00 42.92 ? 99   LYS A CE  1 
ATOM   741  N NZ  . LYS A 1 99  ? -105.134 28.939 -57.440 1.00 44.01 ? 99   LYS A NZ  1 
ATOM   742  N N   . LYS A 1 100 ? -102.560 34.962 -60.775 1.00 38.43 ? 100  LYS A N   1 
ATOM   743  C CA  . LYS A 1 100 ? -103.059 35.341 -62.101 1.00 39.10 ? 100  LYS A CA  1 
ATOM   744  C C   . LYS A 1 100 ? -104.231 34.458 -62.543 1.00 39.97 ? 100  LYS A C   1 
ATOM   745  O O   . LYS A 1 100 ? -105.157 34.931 -63.210 1.00 39.79 ? 100  LYS A O   1 
ATOM   746  C CB  . LYS A 1 100 ? -101.938 35.267 -63.137 1.00 38.91 ? 100  LYS A CB  1 
ATOM   747  C CG  . LYS A 1 100 ? -100.921 36.389 -63.085 1.00 37.95 ? 100  LYS A CG  1 
ATOM   748  C CD  . LYS A 1 100 ? -100.003 36.264 -64.276 1.00 37.52 ? 100  LYS A CD  1 
ATOM   749  C CE  . LYS A 1 100 ? -98.815  37.199 -64.174 1.00 38.06 ? 100  LYS A CE  1 
ATOM   750  N NZ  . LYS A 1 100 ? -97.664  36.763 -65.043 1.00 38.44 ? 100  LYS A NZ  1 
ATOM   751  N N   . ASP A 1 101 ? -104.166 33.172 -62.178 1.00 41.05 ? 101  ASP A N   1 
ATOM   752  C CA  . ASP A 1 101 ? -105.259 32.215 -62.401 1.00 42.21 ? 101  ASP A CA  1 
ATOM   753  C C   . ASP A 1 101 ? -105.598 32.027 -63.880 1.00 42.57 ? 101  ASP A C   1 
ATOM   754  O O   . ASP A 1 101 ? -106.777 32.011 -64.256 1.00 42.56 ? 101  ASP A O   1 
ATOM   755  C CB  . ASP A 1 101 ? -106.510 32.620 -61.595 1.00 42.64 ? 101  ASP A CB  1 
ATOM   756  C CG  . ASP A 1 101 ? -107.615 31.579 -61.653 1.00 43.78 ? 101  ASP A CG  1 
ATOM   757  O OD1 . ASP A 1 101 ? -107.357 30.394 -61.355 1.00 44.90 ? 101  ASP A OD1 1 
ATOM   758  O OD2 . ASP A 1 101 ? -108.782 31.858 -61.989 1.00 45.28 ? 101  ASP A OD2 1 
ATOM   759  N N   . LYS A 1 102 ? -104.557 31.885 -64.706 1.00 43.00 ? 102  LYS A N   1 
ATOM   760  C CA  . LYS A 1 102 ? -104.708 31.666 -66.154 1.00 43.65 ? 102  LYS A CA  1 
ATOM   761  C C   . LYS A 1 102 ? -105.296 32.873 -66.926 1.00 43.09 ? 102  LYS A C   1 
ATOM   762  O O   . LYS A 1 102 ? -105.819 32.720 -68.035 1.00 43.20 ? 102  LYS A O   1 
ATOM   763  C CB  . LYS A 1 102 ? -105.524 30.387 -66.440 1.00 44.44 ? 102  LYS A CB  1 
ATOM   764  C CG  . LYS A 1 102 ? -105.006 29.105 -65.758 1.00 47.15 ? 102  LYS A CG  1 
ATOM   765  C CD  . LYS A 1 102 ? -105.390 27.864 -66.584 1.00 51.28 ? 102  LYS A CD  1 
ATOM   766  C CE  . LYS A 1 102 ? -106.401 26.944 -65.862 1.00 53.95 ? 102  LYS A CE  1 
ATOM   767  N NZ  . LYS A 1 102 ? -107.131 26.037 -66.819 1.00 55.42 ? 102  LYS A NZ  1 
ATOM   768  N N   . SER A 1 103 ? -105.194 34.063 -66.338 1.00 42.51 ? 103  SER A N   1 
ATOM   769  C CA  . SER A 1 103 ? -105.639 35.308 -66.966 1.00 41.70 ? 103  SER A CA  1 
ATOM   770  C C   . SER A 1 103 ? -104.498 36.327 -67.005 1.00 41.00 ? 103  SER A C   1 
ATOM   771  O O   . SER A 1 103 ? -103.465 36.133 -66.356 1.00 40.88 ? 103  SER A O   1 
ATOM   772  C CB  . SER A 1 103 ? -106.804 35.903 -66.172 1.00 41.87 ? 103  SER A CB  1 
ATOM   773  O OG  . SER A 1 103 ? -108.041 35.337 -66.555 1.00 42.41 ? 103  SER A OG  1 
ATOM   774  N N   . ARG A 1 104 ? -104.686 37.403 -67.769 1.00 40.15 ? 104  ARG A N   1 
ATOM   775  C CA  . ARG A 1 104 ? -103.823 38.580 -67.671 1.00 39.42 ? 104  ARG A CA  1 
ATOM   776  C C   . ARG A 1 104 ? -104.348 39.472 -66.539 1.00 38.77 ? 104  ARG A C   1 
ATOM   777  O O   . ARG A 1 104 ? -104.718 40.630 -66.742 1.00 38.69 ? 104  ARG A O   1 
ATOM   778  C CB  . ARG A 1 104 ? -103.750 39.337 -68.996 1.00 39.33 ? 104  ARG A CB  1 
ATOM   779  C CG  . ARG A 1 104 ? -102.479 39.045 -69.780 1.00 39.79 ? 104  ARG A CG  1 
ATOM   780  C CD  . ARG A 1 104 ? -102.443 39.613 -71.201 1.00 39.73 ? 104  ARG A CD  1 
ATOM   781  N NE  . ARG A 1 104 ? -103.718 39.446 -71.891 1.00 39.16 ? 104  ARG A NE  1 
ATOM   782  C CZ  . ARG A 1 104 ? -103.922 38.660 -72.934 1.00 38.56 ? 104  ARG A CZ  1 
ATOM   783  N NH1 . ARG A 1 104 ? -102.940 37.937 -73.451 1.00 37.72 ? 104  ARG A NH1 1 
ATOM   784  N NH2 . ARG A 1 104 ? -105.129 38.609 -73.474 1.00 39.54 ? 104  ARG A NH2 1 
ATOM   785  N N   . ALA A 1 105 ? -104.367 38.887 -65.345 1.00 37.92 ? 105  ALA A N   1 
ATOM   786  C CA  . ALA A 1 105 ? -104.949 39.483 -64.156 1.00 37.18 ? 105  ALA A CA  1 
ATOM   787  C C   . ALA A 1 105 ? -103.854 40.039 -63.239 1.00 36.55 ? 105  ALA A C   1 
ATOM   788  O O   . ALA A 1 105 ? -102.695 39.622 -63.320 1.00 36.72 ? 105  ALA A O   1 
ATOM   789  C CB  . ALA A 1 105 ? -105.792 38.437 -63.415 1.00 37.04 ? 105  ALA A CB  1 
ATOM   790  N N   . PRO A 1 106 ? -104.213 40.986 -62.378 1.00 35.76 ? 106  PRO A N   1 
ATOM   791  C CA  . PRO A 1 106 ? -103.291 41.470 -61.347 1.00 35.34 ? 106  PRO A CA  1 
ATOM   792  C C   . PRO A 1 106 ? -103.190 40.468 -60.209 1.00 34.75 ? 106  PRO A C   1 
ATOM   793  O O   . PRO A 1 106 ? -104.144 39.709 -59.970 1.00 35.21 ? 106  PRO A O   1 
ATOM   794  C CB  . PRO A 1 106 ? -103.992 42.729 -60.830 1.00 35.45 ? 106  PRO A CB  1 
ATOM   795  C CG  . PRO A 1 106 ? -105.448 42.449 -61.051 1.00 35.47 ? 106  PRO A CG  1 
ATOM   796  C CD  . PRO A 1 106 ? -105.516 41.677 -62.327 1.00 35.55 ? 106  PRO A CD  1 
ATOM   797  N N   . ILE A 1 107 ? -102.057 40.455 -59.516 1.00 33.68 ? 107  ILE A N   1 
ATOM   798  C CA  . ILE A 1 107 ? -102.007 39.796 -58.216 1.00 32.37 ? 107  ILE A CA  1 
ATOM   799  C C   . ILE A 1 107 ? -102.213 40.886 -57.172 1.00 31.15 ? 107  ILE A C   1 
ATOM   800  O O   . ILE A 1 107 ? -101.274 41.323 -56.503 1.00 31.24 ? 107  ILE A O   1 
ATOM   801  C CB  . ILE A 1 107 ? -100.693 39.009 -58.008 1.00 32.47 ? 107  ILE A CB  1 
ATOM   802  C CG1 . ILE A 1 107 ? -100.495 38.014 -59.151 1.00 32.84 ? 107  ILE A CG1 1 
ATOM   803  C CG2 . ILE A 1 107 ? -100.737 38.249 -56.666 1.00 32.45 ? 107  ILE A CG2 1 
ATOM   804  C CD1 . ILE A 1 107 ? -99.090  37.445 -59.272 1.00 33.67 ? 107  ILE A CD1 1 
ATOM   805  N N   . SER A 1 108 ? -103.462 41.328 -57.065 1.00 29.54 ? 108  SER A N   1 
ATOM   806  C CA  . SER A 1 108 ? -103.841 42.467 -56.235 1.00 28.13 ? 108  SER A CA  1 
ATOM   807  C C   . SER A 1 108 ? -103.454 42.327 -54.758 1.00 27.30 ? 108  SER A C   1 
ATOM   808  O O   . SER A 1 108 ? -103.143 43.328 -54.116 1.00 26.78 ? 108  SER A O   1 
ATOM   809  C CB  . SER A 1 108 ? -105.346 42.736 -56.345 1.00 28.23 ? 108  SER A CB  1 
ATOM   810  O OG  . SER A 1 108 ? -105.726 43.152 -57.647 1.00 27.62 ? 108  SER A OG  1 
ATOM   811  N N   . ALA A 1 109 ? -103.465 41.104 -54.218 1.00 26.39 ? 109  ALA A N   1 
ATOM   812  C CA  . ALA A 1 109 ? -103.035 40.908 -52.825 1.00 25.69 ? 109  ALA A CA  1 
ATOM   813  C C   . ALA A 1 109 ? -101.536 41.199 -52.636 1.00 25.13 ? 109  ALA A C   1 
ATOM   814  O O   . ALA A 1 109 ? -101.118 41.643 -51.574 1.00 24.95 ? 109  ALA A O   1 
ATOM   815  C CB  . ALA A 1 109 ? -103.375 39.520 -52.339 1.00 25.77 ? 109  ALA A CB  1 
ATOM   816  N N   . LYS A 1 110 ? -100.732 40.958 -53.669 1.00 24.53 ? 110  LYS A N   1 
ATOM   817  C CA  . LYS A 1 110 ? -99.333  41.350 -53.625 1.00 24.22 ? 110  LYS A CA  1 
ATOM   818  C C   . LYS A 1 110 ? -99.201  42.880 -53.725 1.00 23.98 ? 110  LYS A C   1 
ATOM   819  O O   . LYS A 1 110 ? -98.365  43.491 -53.051 1.00 24.05 ? 110  LYS A O   1 
ATOM   820  C CB  . LYS A 1 110 ? -98.516  40.623 -54.706 1.00 23.99 ? 110  LYS A CB  1 
ATOM   821  C CG  . LYS A 1 110 ? -97.033  41.015 -54.773 1.00 23.96 ? 110  LYS A CG  1 
ATOM   822  C CD  . LYS A 1 110 ? -96.335  40.968 -53.426 1.00 24.22 ? 110  LYS A CD  1 
ATOM   823  C CE  . LYS A 1 110 ? -94.881  40.578 -53.557 1.00 26.06 ? 110  LYS A CE  1 
ATOM   824  N NZ  . LYS A 1 110 ? -94.040  41.732 -53.900 1.00 28.91 ? 110  LYS A NZ  1 
ATOM   825  N N   . LEU A 1 111 ? -100.035 43.505 -54.548 1.00 23.59 ? 111  LEU A N   1 
ATOM   826  C CA  . LEU A 1 111 ? -100.065 44.962 -54.592 1.00 23.43 ? 111  LEU A CA  1 
ATOM   827  C C   . LEU A 1 111 ? -100.326 45.528 -53.184 1.00 23.33 ? 111  LEU A C   1 
ATOM   828  O O   . LEU A 1 111 ? -99.562  46.358 -52.692 1.00 23.78 ? 111  LEU A O   1 
ATOM   829  C CB  . LEU A 1 111 ? -101.137 45.430 -55.569 1.00 23.52 ? 111  LEU A CB  1 
ATOM   830  C CG  . LEU A 1 111 ? -101.126 46.787 -56.291 1.00 23.47 ? 111  LEU A CG  1 
ATOM   831  C CD1 . LEU A 1 111 ? -102.533 47.385 -56.247 1.00 23.48 ? 111  LEU A CD1 1 
ATOM   832  C CD2 . LEU A 1 111 ? -100.091 47.773 -55.766 1.00 22.38 ? 111  LEU A CD2 1 
ATOM   833  N N   . VAL A 1 112 ? -101.391 45.060 -52.536 1.00 22.78 ? 112  VAL A N   1 
ATOM   834  C CA  . VAL A 1 112 ? -101.740 45.485 -51.188 1.00 22.58 ? 112  VAL A CA  1 
ATOM   835  C C   . VAL A 1 112 ? -100.595 45.262 -50.190 1.00 22.81 ? 112  VAL A C   1 
ATOM   836  O O   . VAL A 1 112 ? -100.253 46.155 -49.422 1.00 23.14 ? 112  VAL A O   1 
ATOM   837  C CB  . VAL A 1 112 ? -103.061 44.820 -50.715 1.00 22.44 ? 112  VAL A CB  1 
ATOM   838  C CG1 . VAL A 1 112 ? -103.412 45.221 -49.262 1.00 21.84 ? 112  VAL A CG1 1 
ATOM   839  C CG2 . VAL A 1 112 ? -104.201 45.185 -51.678 1.00 21.85 ? 112  VAL A CG2 1 
ATOM   840  N N   . ALA A 1 113 ? -100.004 44.073 -50.205 1.00 22.99 ? 113  ALA A N   1 
ATOM   841  C CA  . ALA A 1 113 ? -98.810  43.796 -49.407 1.00 22.95 ? 113  ALA A CA  1 
ATOM   842  C C   . ALA A 1 113 ? -97.738  44.873 -49.623 1.00 23.17 ? 113  ALA A C   1 
ATOM   843  O O   . ALA A 1 113 ? -97.184  45.413 -48.645 1.00 23.07 ? 113  ALA A O   1 
ATOM   844  C CB  . ALA A 1 113 ? -98.260  42.423 -49.743 1.00 22.77 ? 113  ALA A CB  1 
ATOM   845  N N   . ASN A 1 114 ? -97.453  45.184 -50.893 1.00 23.15 ? 114  ASN A N   1 
ATOM   846  C CA  . ASN A 1 114 ? -96.460  46.211 -51.237 1.00 23.58 ? 114  ASN A CA  1 
ATOM   847  C C   . ASN A 1 114 ? -96.836  47.617 -50.742 1.00 23.42 ? 114  ASN A C   1 
ATOM   848  O O   . ASN A 1 114 ? -95.982  48.342 -50.239 1.00 23.52 ? 114  ASN A O   1 
ATOM   849  C CB  . ASN A 1 114 ? -96.200  46.251 -52.749 1.00 24.04 ? 114  ASN A CB  1 
ATOM   850  C CG  . ASN A 1 114 ? -95.357  45.080 -53.253 1.00 24.86 ? 114  ASN A CG  1 
ATOM   851  O OD1 . ASN A 1 114 ? -94.694  44.370 -52.486 1.00 26.33 ? 114  ASN A OD1 1 
ATOM   852  N ND2 . ASN A 1 114 ? -95.355  44.901 -54.557 1.00 24.54 ? 114  ASN A ND2 1 
ATOM   853  N N   . MET A 1 115 ? -98.110  47.990 -50.850 1.00 23.11 ? 115  MET A N   1 
ATOM   854  C CA  . MET A 1 115 ? -98.543  49.319 -50.426 1.00 23.10 ? 115  MET A CA  1 
ATOM   855  C C   . MET A 1 115 ? -98.463  49.459 -48.932 1.00 23.02 ? 115  MET A C   1 
ATOM   856  O O   . MET A 1 115 ? -98.041  50.508 -48.425 1.00 23.35 ? 115  MET A O   1 
ATOM   857  C CB  . MET A 1 115 ? -99.955  49.623 -50.914 1.00 23.46 ? 115  MET A CB  1 
ATOM   858  C CG  . MET A 1 115 ? -100.071 49.590 -52.409 1.00 26.23 ? 115  MET A CG  1 
ATOM   859  S SD  . MET A 1 115 ? -101.670 50.049 -52.989 1.00 32.41 ? 115  MET A SD  1 
ATOM   860  C CE  . MET A 1 115 ? -102.637 48.685 -52.494 1.00 31.66 ? 115  MET A CE  1 
ATOM   861  N N   . LEU A 1 116 ? -98.848  48.397 -48.224 1.00 22.61 ? 116  LEU A N   1 
ATOM   862  C CA  . LEU A 1 116 ? -98.718  48.343 -46.776 1.00 22.77 ? 116  LEU A CA  1 
ATOM   863  C C   . LEU A 1 116 ? -97.269  48.500 -46.310 1.00 23.03 ? 116  LEU A C   1 
ATOM   864  O O   . LEU A 1 116 ? -96.989  49.297 -45.419 1.00 23.44 ? 116  LEU A O   1 
ATOM   865  C CB  . LEU A 1 116 ? -99.313  47.033 -46.249 1.00 22.85 ? 116  LEU A CB  1 
ATOM   866  C CG  . LEU A 1 116 ? -100.839 46.981 -46.184 1.00 22.37 ? 116  LEU A CG  1 
ATOM   867  C CD1 . LEU A 1 116 ? -101.279 45.546 -46.083 1.00 21.35 ? 116  LEU A CD1 1 
ATOM   868  C CD2 . LEU A 1 116 ? -101.363 47.831 -44.996 1.00 21.67 ? 116  LEU A CD2 1 
ATOM   869  N N   . SER A 1 117 ? -96.354  47.749 -46.925 1.00 23.06 ? 117  SER A N   1 
ATOM   870  C CA  . SER A 1 117 ? -94.930  47.857 -46.626 1.00 23.19 ? 117  SER A CA  1 
ATOM   871  C C   . SER A 1 117 ? -94.364  49.259 -46.918 1.00 23.04 ? 117  SER A C   1 
ATOM   872  O O   . SER A 1 117 ? -93.795  49.880 -46.023 1.00 23.32 ? 117  SER A O   1 
ATOM   873  C CB  . SER A 1 117 ? -94.121  46.774 -47.366 1.00 23.59 ? 117  SER A CB  1 
ATOM   874  O OG  . SER A 1 117 ? -94.772  45.510 -47.309 1.00 23.94 ? 117  SER A OG  1 
ATOM   875  N N   . VAL A 1 118 ? -94.527  49.764 -48.143 1.00 22.59 ? 118  VAL A N   1 
ATOM   876  C CA  . VAL A 1 118 ? -94.105  51.133 -48.461 1.00 22.49 ? 118  VAL A CA  1 
ATOM   877  C C   . VAL A 1 118 ? -94.820  52.208 -47.627 1.00 22.96 ? 118  VAL A C   1 
ATOM   878  O O   . VAL A 1 118 ? -94.280  53.278 -47.439 1.00 23.45 ? 118  VAL A O   1 
ATOM   879  C CB  . VAL A 1 118 ? -94.187  51.479 -49.991 1.00 22.45 ? 118  VAL A CB  1 
ATOM   880  C CG1 . VAL A 1 118 ? -95.563  52.028 -50.394 1.00 21.56 ? 118  VAL A CG1 1 
ATOM   881  C CG2 . VAL A 1 118 ? -93.116  52.483 -50.363 1.00 22.70 ? 118  VAL A CG2 1 
ATOM   882  N N   . ALA A 1 119 ? -96.017  51.941 -47.115 1.00 23.39 ? 119  ALA A N   1 
ATOM   883  C CA  . ALA A 1 119 ? -96.629  52.916 -46.219 1.00 23.82 ? 119  ALA A CA  1 
ATOM   884  C C   . ALA A 1 119 ? -95.899  52.930 -44.881 1.00 24.15 ? 119  ALA A C   1 
ATOM   885  O O   . ALA A 1 119 ? -96.030  53.878 -44.118 1.00 24.74 ? 119  ALA A O   1 
ATOM   886  C CB  . ALA A 1 119 ? -98.119  52.659 -46.024 1.00 23.65 ? 119  ALA A CB  1 
ATOM   887  N N   . GLY A 1 120 ? -95.123  51.890 -44.603 1.00 24.33 ? 120  GLY A N   1 
ATOM   888  C CA  . GLY A 1 120 ? -94.318  51.847 -43.392 1.00 24.71 ? 120  GLY A CA  1 
ATOM   889  C C   . GLY A 1 120 ? -94.732  50.831 -42.336 1.00 25.14 ? 120  GLY A C   1 
ATOM   890  O O   . GLY A 1 120 ? -94.280  50.929 -41.191 1.00 25.77 ? 120  GLY A O   1 
ATOM   891  N N   . ALA A 1 121 ? -95.565  49.856 -42.698 1.00 25.04 ? 121  ALA A N   1 
ATOM   892  C CA  . ALA A 1 121 ? -95.996  48.823 -41.757 1.00 25.15 ? 121  ALA A CA  1 
ATOM   893  C C   . ALA A 1 121 ? -94.814  47.923 -41.425 1.00 25.27 ? 121  ALA A C   1 
ATOM   894  O O   . ALA A 1 121 ? -94.114  47.472 -42.320 1.00 25.35 ? 121  ALA A O   1 
ATOM   895  C CB  . ALA A 1 121 ? -97.137  48.011 -42.340 1.00 24.85 ? 121  ALA A CB  1 
ATOM   896  N N   . ASP A 1 122 ? -94.582  47.679 -40.139 1.00 25.53 ? 122  ASP A N   1 
ATOM   897  C CA  . ASP A 1 122 ? -93.460  46.848 -39.700 1.00 25.80 ? 122  ASP A CA  1 
ATOM   898  C C   . ASP A 1 122 ? -93.899  45.424 -39.453 1.00 25.70 ? 122  ASP A C   1 
ATOM   899  O O   . ASP A 1 122 ? -93.073  44.537 -39.268 1.00 25.53 ? 122  ASP A O   1 
ATOM   900  C CB  . ASP A 1 122 ? -92.852  47.393 -38.405 1.00 25.80 ? 122  ASP A CB  1 
ATOM   901  C CG  . ASP A 1 122 ? -92.285  48.775 -38.569 1.00 27.18 ? 122  ASP A CG  1 
ATOM   902  O OD1 . ASP A 1 122 ? -92.651  49.664 -37.761 1.00 28.82 ? 122  ASP A OD1 1 
ATOM   903  O OD2 . ASP A 1 122 ? -91.472  49.077 -39.471 1.00 27.91 ? 122  ASP A OD2 1 
ATOM   904  N N   . HIS A 1 123 ? -95.206  45.215 -39.446 1.00 26.06 ? 123  HIS A N   1 
ATOM   905  C CA  . HIS A 1 123 ? -95.781  43.989 -38.915 1.00 26.88 ? 123  HIS A CA  1 
ATOM   906  C C   . HIS A 1 123 ? -97.248  43.955 -39.294 1.00 26.54 ? 123  HIS A C   1 
ATOM   907  O O   . HIS A 1 123 ? -97.901  44.998 -39.366 1.00 26.72 ? 123  HIS A O   1 
ATOM   908  C CB  . HIS A 1 123 ? -95.612  43.955 -37.388 1.00 27.46 ? 123  HIS A CB  1 
ATOM   909  C CG  . HIS A 1 123 ? -95.743  42.591 -36.782 1.00 30.40 ? 123  HIS A CG  1 
ATOM   910  N ND1 . HIS A 1 123 ? -94.658  41.869 -36.324 1.00 32.72 ? 123  HIS A ND1 1 
ATOM   911  C CD2 . HIS A 1 123 ? -96.836  41.831 -36.526 1.00 31.90 ? 123  HIS A CD2 1 
ATOM   912  C CE1 . HIS A 1 123 ? -95.078  40.717 -35.831 1.00 33.64 ? 123  HIS A CE1 1 
ATOM   913  N NE2 . HIS A 1 123 ? -96.396  40.673 -35.938 1.00 33.45 ? 123  HIS A NE2 1 
ATOM   914  N N   . ILE A 1 124 ? -97.748  42.754 -39.572 1.00 26.16 ? 124  ILE A N   1 
ATOM   915  C CA  . ILE A 1 124 ? -99.144  42.529 -39.895 1.00 25.72 ? 124  ILE A CA  1 
ATOM   916  C C   . ILE A 1 124 ? -99.706  41.489 -38.929 1.00 26.12 ? 124  ILE A C   1 
ATOM   917  O O   . ILE A 1 124 ? -99.039  40.496 -38.597 1.00 25.72 ? 124  ILE A O   1 
ATOM   918  C CB  . ILE A 1 124 ? -99.305  42.019 -41.371 1.00 25.80 ? 124  ILE A CB  1 
ATOM   919  C CG1 . ILE A 1 124 ? -98.492  42.862 -42.375 1.00 24.81 ? 124  ILE A CG1 1 
ATOM   920  C CG2 . ILE A 1 124 ? -100.801 41.901 -41.773 1.00 25.12 ? 124  ILE A CG2 1 
ATOM   921  C CD1 . ILE A 1 124 ? -99.081  44.208 -42.686 1.00 24.55 ? 124  ILE A CD1 1 
ATOM   922  N N   . ILE A 1 125 ? -100.935 41.728 -38.475 1.00 26.45 ? 125  ILE A N   1 
ATOM   923  C CA  . ILE A 1 125 ? -101.704 40.729 -37.746 1.00 26.67 ? 125  ILE A CA  1 
ATOM   924  C C   . ILE A 1 125 ? -103.026 40.598 -38.459 1.00 27.44 ? 125  ILE A C   1 
ATOM   925  O O   . ILE A 1 125 ? -103.750 41.577 -38.631 1.00 27.75 ? 125  ILE A O   1 
ATOM   926  C CB  . ILE A 1 125 ? -101.941 41.144 -36.275 1.00 26.40 ? 125  ILE A CB  1 
ATOM   927  C CG1 . ILE A 1 125 ? -100.616 41.235 -35.505 1.00 25.40 ? 125  ILE A CG1 1 
ATOM   928  C CG2 . ILE A 1 125 ? -102.948 40.194 -35.605 1.00 25.82 ? 125  ILE A CG2 1 
ATOM   929  C CD1 . ILE A 1 125 ? -100.722 41.969 -34.165 1.00 23.73 ? 125  ILE A CD1 1 
ATOM   930  N N   . THR A 1 126 ? -103.343 39.384 -38.869 1.00 28.25 ? 126  THR A N   1 
ATOM   931  C CA  . THR A 1 126 ? -104.552 39.136 -39.621 1.00 29.17 ? 126  THR A CA  1 
ATOM   932  C C   . THR A 1 126 ? -105.123 37.765 -39.229 1.00 30.42 ? 126  THR A C   1 
ATOM   933  O O   . THR A 1 126 ? -104.506 37.032 -38.439 1.00 30.21 ? 126  THR A O   1 
ATOM   934  C CB  . THR A 1 126 ? -104.234 39.234 -41.127 1.00 28.95 ? 126  THR A CB  1 
ATOM   935  O OG1 . THR A 1 126 ? -105.452 39.193 -41.879 1.00 29.09 ? 126  THR A OG1 1 
ATOM   936  C CG2 . THR A 1 126 ? -103.441 38.021 -41.600 1.00 27.99 ? 126  THR A CG2 1 
ATOM   937  N N   . MET A 1 127 ? -106.301 37.436 -39.765 1.00 31.81 ? 127  MET A N   1 
ATOM   938  C CA  . MET A 1 127 ? -106.988 36.189 -39.437 1.00 33.32 ? 127  MET A CA  1 
ATOM   939  C C   . MET A 1 127 ? -107.422 35.417 -40.675 1.00 33.88 ? 127  MET A C   1 
ATOM   940  O O   . MET A 1 127 ? -108.129 35.951 -41.523 1.00 33.87 ? 127  MET A O   1 
ATOM   941  C CB  . MET A 1 127 ? -108.196 36.437 -38.522 1.00 33.50 ? 127  MET A CB  1 
ATOM   942  C CG  . MET A 1 127 ? -108.839 35.140 -38.062 1.00 35.95 ? 127  MET A CG  1 
ATOM   943  S SD  . MET A 1 127 ? -109.956 35.269 -36.661 1.00 40.37 ? 127  MET A SD  1 
ATOM   944  C CE  . MET A 1 127 ? -108.750 35.601 -35.295 1.00 39.76 ? 127  MET A CE  1 
ATOM   945  N N   . ASP A 1 128 ? -107.010 34.150 -40.739 1.00 34.91 ? 128  ASP A N   1 
ATOM   946  C CA  . ASP A 1 128 ? -107.305 33.239 -41.846 1.00 35.98 ? 128  ASP A CA  1 
ATOM   947  C C   . ASP A 1 128 ? -107.137 33.861 -43.221 1.00 35.66 ? 128  ASP A C   1 
ATOM   948  O O   . ASP A 1 128 ? -108.117 34.064 -43.949 1.00 35.51 ? 128  ASP A O   1 
ATOM   949  C CB  . ASP A 1 128 ? -108.702 32.619 -41.713 1.00 37.12 ? 128  ASP A CB  1 
ATOM   950  C CG  . ASP A 1 128 ? -108.764 31.563 -40.628 1.00 39.98 ? 128  ASP A CG  1 
ATOM   951  O OD1 . ASP A 1 128 ? -109.889 31.208 -40.198 1.00 43.28 ? 128  ASP A OD1 1 
ATOM   952  O OD2 . ASP A 1 128 ? -107.743 31.037 -40.131 1.00 41.56 ? 128  ASP A OD2 1 
ATOM   953  N N   . LEU A 1 129 ? -105.889 34.181 -43.558 1.00 35.23 ? 129  LEU A N   1 
ATOM   954  C CA  . LEU A 1 129 ? -105.535 34.550 -44.919 1.00 34.83 ? 129  LEU A CA  1 
ATOM   955  C C   . LEU A 1 129 ? -106.197 33.572 -45.884 1.00 34.83 ? 129  LEU A C   1 
ATOM   956  O O   . LEU A 1 129 ? -106.156 32.349 -45.649 1.00 34.79 ? 129  LEU A O   1 
ATOM   957  C CB  . LEU A 1 129 ? -104.024 34.503 -45.086 1.00 34.68 ? 129  LEU A CB  1 
ATOM   958  C CG  . LEU A 1 129 ? -103.320 35.677 -44.418 1.00 34.30 ? 129  LEU A CG  1 
ATOM   959  C CD1 . LEU A 1 129 ? -101.827 35.471 -44.417 1.00 33.79 ? 129  LEU A CD1 1 
ATOM   960  C CD2 . LEU A 1 129 ? -103.711 36.975 -45.113 1.00 33.60 ? 129  LEU A CD2 1 
ATOM   961  N N   . HIS A 1 130 ? -106.830 34.100 -46.938 1.00 34.39 ? 130  HIS A N   1 
ATOM   962  C CA  . HIS A 1 130 ? -107.472 33.250 -47.942 1.00 34.20 ? 130  HIS A CA  1 
ATOM   963  C C   . HIS A 1 130 ? -106.513 32.172 -48.414 1.00 33.96 ? 130  HIS A C   1 
ATOM   964  O O   . HIS A 1 130 ? -106.887 31.016 -48.565 1.00 34.12 ? 130  HIS A O   1 
ATOM   965  C CB  . HIS A 1 130 ? -107.969 34.053 -49.141 1.00 34.37 ? 130  HIS A CB  1 
ATOM   966  C CG  . HIS A 1 130 ? -108.714 33.229 -50.144 1.00 34.59 ? 130  HIS A CG  1 
ATOM   967  N ND1 . HIS A 1 130 ? -108.209 32.939 -51.394 1.00 35.33 ? 130  HIS A ND1 1 
ATOM   968  C CD2 . HIS A 1 130 ? -109.917 32.613 -50.074 1.00 34.54 ? 130  HIS A CD2 1 
ATOM   969  C CE1 . HIS A 1 130 ? -109.076 32.191 -52.055 1.00 35.40 ? 130  HIS A CE1 1 
ATOM   970  N NE2 . HIS A 1 130 ? -110.122 31.981 -51.275 1.00 35.28 ? 130  HIS A NE2 1 
ATOM   971  N N   . ALA A 1 131 ? -105.266 32.557 -48.638 1.00 33.74 ? 131  ALA A N   1 
ATOM   972  C CA  . ALA A 1 131 ? -104.213 31.583 -48.870 1.00 33.40 ? 131  ALA A CA  1 
ATOM   973  C C   . ALA A 1 131 ? -103.000 31.919 -48.011 1.00 33.30 ? 131  ALA A C   1 
ATOM   974  O O   . ALA A 1 131 ? -102.542 33.066 -47.955 1.00 33.11 ? 131  ALA A O   1 
ATOM   975  C CB  . ALA A 1 131 ? -103.846 31.529 -50.345 1.00 33.18 ? 131  ALA A CB  1 
ATOM   976  N N   . SER A 1 132 ? -102.507 30.893 -47.332 1.00 33.42 ? 132  SER A N   1 
ATOM   977  C CA  . SER A 1 132 ? -101.313 30.955 -46.506 1.00 33.51 ? 132  SER A CA  1 
ATOM   978  C C   . SER A 1 132 ? -100.112 31.634 -47.182 1.00 33.04 ? 132  SER A C   1 
ATOM   979  O O   . SER A 1 132 ? -99.325  32.345 -46.529 1.00 33.07 ? 132  SER A O   1 
ATOM   980  C CB  . SER A 1 132 ? -100.927 29.538 -46.140 1.00 33.85 ? 132  SER A CB  1 
ATOM   981  O OG  . SER A 1 132 ? -101.155 29.339 -44.774 1.00 35.97 ? 132  SER A OG  1 
ATOM   982  N N   . GLN A 1 133 ? -99.977  31.394 -48.484 1.00 32.05 ? 133  GLN A N   1 
ATOM   983  C CA  . GLN A 1 133 ? -98.866  31.919 -49.268 1.00 31.36 ? 133  GLN A CA  1 
ATOM   984  C C   . GLN A 1 133 ? -98.806  33.445 -49.264 1.00 30.92 ? 133  GLN A C   1 
ATOM   985  O O   . GLN A 1 133 ? -97.737  34.026 -49.457 1.00 31.23 ? 133  GLN A O   1 
ATOM   986  C CB  . GLN A 1 133 ? -98.919  31.382 -50.702 1.00 31.11 ? 133  GLN A CB  1 
ATOM   987  C CG  . GLN A 1 133 ? -98.598  29.886 -50.806 1.00 30.91 ? 133  GLN A CG  1 
ATOM   988  C CD  . GLN A 1 133 ? -99.821  28.988 -50.668 1.00 31.73 ? 133  GLN A CD  1 
ATOM   989  O OE1 . GLN A 1 133 ? -100.954 29.464 -50.501 1.00 32.37 ? 133  GLN A OE1 1 
ATOM   990  N NE2 . GLN A 1 133 ? -99.598  27.686 -50.747 1.00 31.72 ? 133  GLN A NE2 1 
ATOM   991  N N   . ILE A 1 134 ? -99.944  34.092 -49.026 1.00 30.22 ? 134  ILE A N   1 
ATOM   992  C CA  . ILE A 1 134 ? -99.990  35.550 -48.917 1.00 29.53 ? 134  ILE A CA  1 
ATOM   993  C C   . ILE A 1 134 ? -98.967  36.060 -47.885 1.00 28.90 ? 134  ILE A C   1 
ATOM   994  O O   . ILE A 1 134 ? -98.425  37.150 -48.035 1.00 28.57 ? 134  ILE A O   1 
ATOM   995  C CB  . ILE A 1 134 ? -101.441 36.041 -48.609 1.00 29.47 ? 134  ILE A CB  1 
ATOM   996  C CG1 . ILE A 1 134 ? -102.246 36.130 -49.903 1.00 29.94 ? 134  ILE A CG1 1 
ATOM   997  C CG2 . ILE A 1 134 ? -101.445 37.382 -47.898 1.00 28.68 ? 134  ILE A CG2 1 
ATOM   998  C CD1 . ILE A 1 134 ? -103.754 36.130 -49.701 1.00 30.56 ? 134  ILE A CD1 1 
ATOM   999  N N   . GLN A 1 135 ? -98.700  35.264 -46.855 1.00 28.30 ? 135  GLN A N   1 
ATOM   1000 C CA  . GLN A 1 135 ? -97.695  35.632 -45.868 1.00 28.11 ? 135  GLN A CA  1 
ATOM   1001 C C   . GLN A 1 135 ? -96.388  35.951 -46.584 1.00 27.33 ? 135  GLN A C   1 
ATOM   1002 O O   . GLN A 1 135 ? -95.684  36.914 -46.243 1.00 27.12 ? 135  GLN A O   1 
ATOM   1003 C CB  . GLN A 1 135 ? -97.484  34.501 -44.872 1.00 28.58 ? 135  GLN A CB  1 
ATOM   1004 C CG  . GLN A 1 135 ? -98.449  34.505 -43.696 1.00 30.80 ? 135  GLN A CG  1 
ATOM   1005 C CD  . GLN A 1 135 ? -98.056  33.476 -42.633 1.00 34.11 ? 135  GLN A CD  1 
ATOM   1006 O OE1 . GLN A 1 135 ? -97.302  33.783 -41.699 1.00 35.29 ? 135  GLN A OE1 1 
ATOM   1007 N NE2 . GLN A 1 135 ? -98.544  32.254 -42.791 1.00 35.52 ? 135  GLN A NE2 1 
ATOM   1008 N N   . GLY A 1 136 ? -96.096  35.143 -47.601 1.00 26.38 ? 136  GLY A N   1 
ATOM   1009 C CA  . GLY A 1 136 ? -94.918  35.314 -48.423 1.00 25.58 ? 136  GLY A CA  1 
ATOM   1010 C C   . GLY A 1 136 ? -94.937  36.509 -49.362 1.00 25.20 ? 136  GLY A C   1 
ATOM   1011 O O   . GLY A 1 136 ? -93.938  36.757 -50.030 1.00 25.58 ? 136  GLY A O   1 
ATOM   1012 N N   . PHE A 1 137 ? -96.049  37.241 -49.425 1.00 24.50 ? 137  PHE A N   1 
ATOM   1013 C CA  . PHE A 1 137 ? -96.122  38.474 -50.204 1.00 24.15 ? 137  PHE A CA  1 
ATOM   1014 C C   . PHE A 1 137 ? -95.418  39.636 -49.496 1.00 24.24 ? 137  PHE A C   1 
ATOM   1015 O O   . PHE A 1 137 ? -95.154  40.676 -50.093 1.00 24.11 ? 137  PHE A O   1 
ATOM   1016 C CB  . PHE A 1 137 ? -97.573  38.854 -50.495 1.00 24.05 ? 137  PHE A CB  1 
ATOM   1017 C CG  . PHE A 1 137 ? -98.262  37.958 -51.500 1.00 24.89 ? 137  PHE A CG  1 
ATOM   1018 C CD1 . PHE A 1 137 ? -99.601  38.166 -51.817 1.00 24.69 ? 137  PHE A CD1 1 
ATOM   1019 C CD2 . PHE A 1 137 ? -97.586  36.903 -52.128 1.00 25.50 ? 137  PHE A CD2 1 
ATOM   1020 C CE1 . PHE A 1 137 ? -100.256 37.347 -52.731 1.00 24.18 ? 137  PHE A CE1 1 
ATOM   1021 C CE2 . PHE A 1 137 ? -98.238  36.078 -53.049 1.00 24.75 ? 137  PHE A CE2 1 
ATOM   1022 C CZ  . PHE A 1 137 ? -99.574  36.309 -53.351 1.00 24.38 ? 137  PHE A CZ  1 
ATOM   1023 N N   . PHE A 1 138 ? -95.118  39.461 -48.214 1.00 24.46 ? 138  PHE A N   1 
ATOM   1024 C CA  . PHE A 1 138 ? -94.443  40.495 -47.447 1.00 24.53 ? 138  PHE A CA  1 
ATOM   1025 C C   . PHE A 1 138 ? -92.995  40.113 -47.255 1.00 25.28 ? 138  PHE A C   1 
ATOM   1026 O O   . PHE A 1 138 ? -92.615  38.972 -47.536 1.00 25.43 ? 138  PHE A O   1 
ATOM   1027 C CB  . PHE A 1 138 ? -95.106  40.644 -46.087 1.00 23.99 ? 138  PHE A CB  1 
ATOM   1028 C CG  . PHE A 1 138 ? -96.520  41.132 -46.148 1.00 22.70 ? 138  PHE A CG  1 
ATOM   1029 C CD1 . PHE A 1 138 ? -97.577  40.237 -46.310 1.00 22.10 ? 138  PHE A CD1 1 
ATOM   1030 C CD2 . PHE A 1 138 ? -96.800  42.480 -46.037 1.00 21.57 ? 138  PHE A CD2 1 
ATOM   1031 C CE1 . PHE A 1 138 ? -98.890  40.679 -46.343 1.00 21.45 ? 138  PHE A CE1 1 
ATOM   1032 C CE2 . PHE A 1 138 ? -98.118  42.940 -46.069 1.00 21.65 ? 138  PHE A CE2 1 
ATOM   1033 C CZ  . PHE A 1 138 ? -99.161  42.040 -46.218 1.00 21.40 ? 138  PHE A CZ  1 
ATOM   1034 N N   . ASP A 1 139 ? -92.181  41.058 -46.785 1.00 26.17 ? 139  ASP A N   1 
ATOM   1035 C CA  . ASP A 1 139 ? -90.860  40.717 -46.238 1.00 27.02 ? 139  ASP A CA  1 
ATOM   1036 C C   . ASP A 1 139 ? -90.798  41.027 -44.746 1.00 26.66 ? 139  ASP A C   1 
ATOM   1037 O O   . ASP A 1 139 ? -89.814  40.744 -44.088 1.00 27.79 ? 139  ASP A O   1 
ATOM   1038 C CB  . ASP A 1 139 ? -89.728  41.421 -46.999 1.00 27.73 ? 139  ASP A CB  1 
ATOM   1039 C CG  . ASP A 1 139 ? -89.542  40.872 -48.417 1.00 29.82 ? 139  ASP A CG  1 
ATOM   1040 O OD1 . ASP A 1 139 ? -89.408  39.628 -48.601 1.00 30.60 ? 139  ASP A OD1 1 
ATOM   1041 O OD2 . ASP A 1 139 ? -89.514  41.625 -49.412 1.00 32.45 ? 139  ASP A OD2 1 
ATOM   1042 N N   . ILE A 1 140 ? -91.868  41.598 -44.221 1.00 25.84 ? 140  ILE A N   1 
ATOM   1043 C CA  . ILE A 1 140 ? -92.006  41.877 -42.804 1.00 24.93 ? 140  ILE A CA  1 
ATOM   1044 C C   . ILE A 1 140 ? -92.768  40.708 -42.179 1.00 24.81 ? 140  ILE A C   1 
ATOM   1045 O O   . ILE A 1 140 ? -93.497  40.002 -42.882 1.00 24.97 ? 140  ILE A O   1 
ATOM   1046 C CB  . ILE A 1 140 ? -92.792  43.209 -42.601 1.00 24.63 ? 140  ILE A CB  1 
ATOM   1047 C CG1 . ILE A 1 140 ? -94.162  43.150 -43.312 1.00 24.25 ? 140  ILE A CG1 1 
ATOM   1048 C CG2 . ILE A 1 140 ? -91.946  44.405 -43.054 1.00 23.74 ? 140  ILE A CG2 1 
ATOM   1049 C CD1 . ILE A 1 140 ? -95.134  44.284 -42.964 1.00 23.86 ? 140  ILE A CD1 1 
ATOM   1050 N N   . PRO A 1 141 ? -92.641  40.511 -40.868 1.00 24.57 ? 141  PRO A N   1 
ATOM   1051 C CA  . PRO A 1 141 ? -93.412  39.459 -40.193 1.00 24.58 ? 141  PRO A CA  1 
ATOM   1052 C C   . PRO A 1 141 ? -94.935  39.631 -40.318 1.00 24.96 ? 141  PRO A C   1 
ATOM   1053 O O   . PRO A 1 141 ? -95.482  40.733 -40.126 1.00 24.67 ? 141  PRO A O   1 
ATOM   1054 C CB  . PRO A 1 141 ? -93.005  39.593 -38.724 1.00 24.31 ? 141  PRO A CB  1 
ATOM   1055 C CG  . PRO A 1 141 ? -91.813  40.456 -38.702 1.00 24.51 ? 141  PRO A CG  1 
ATOM   1056 C CD  . PRO A 1 141 ? -91.782  41.266 -39.941 1.00 24.29 ? 141  PRO A CD  1 
ATOM   1057 N N   . VAL A 1 142 ? -95.596  38.514 -40.620 1.00 25.43 ? 142  VAL A N   1 
ATOM   1058 C CA  . VAL A 1 142 ? -97.043  38.383 -40.576 1.00 25.91 ? 142  VAL A CA  1 
ATOM   1059 C C   . VAL A 1 142 ? -97.412  37.285 -39.568 1.00 27.42 ? 142  VAL A C   1 
ATOM   1060 O O   . VAL A 1 142 ? -96.841  36.186 -39.562 1.00 27.92 ? 142  VAL A O   1 
ATOM   1061 C CB  . VAL A 1 142 ? -97.642  37.988 -41.953 1.00 25.57 ? 142  VAL A CB  1 
ATOM   1062 C CG1 . VAL A 1 142 ? -99.169  37.943 -41.899 1.00 25.06 ? 142  VAL A CG1 1 
ATOM   1063 C CG2 . VAL A 1 142 ? -97.162  38.904 -43.074 1.00 24.36 ? 142  VAL A CG2 1 
ATOM   1064 N N   . ASP A 1 143 ? -98.384  37.590 -38.720 1.00 28.55 ? 143  ASP A N   1 
ATOM   1065 C CA  . ASP A 1 143 ? -98.954  36.616 -37.827 1.00 29.49 ? 143  ASP A CA  1 
ATOM   1066 C C   . ASP A 1 143 ? -100.353 36.334 -38.332 1.00 30.54 ? 143  ASP A C   1 
ATOM   1067 O O   . ASP A 1 143 ? -101.224 37.210 -38.314 1.00 30.47 ? 143  ASP A O   1 
ATOM   1068 C CB  . ASP A 1 143 ? -98.940  37.142 -36.390 1.00 29.47 ? 143  ASP A CB  1 
ATOM   1069 C CG  . ASP A 1 143 ? -97.528  37.184 -35.802 1.00 30.33 ? 143  ASP A CG  1 
ATOM   1070 O OD1 . ASP A 1 143 ? -96.725  36.267 -36.111 1.00 30.44 ? 143  ASP A OD1 1 
ATOM   1071 O OD2 . ASP A 1 143 ? -97.120  38.097 -35.043 1.00 30.96 ? 143  ASP A OD2 1 
ATOM   1072 N N   . ASN A 1 144 ? -100.547 35.112 -38.823 1.00 31.96 ? 144  ASN A N   1 
ATOM   1073 C CA  . ASN A 1 144 ? -101.800 34.722 -39.457 1.00 33.42 ? 144  ASN A CA  1 
ATOM   1074 C C   . ASN A 1 144 ? -102.588 33.829 -38.528 1.00 34.61 ? 144  ASN A C   1 
ATOM   1075 O O   . ASN A 1 144 ? -102.396 32.603 -38.504 1.00 34.91 ? 144  ASN A O   1 
ATOM   1076 C CB  . ASN A 1 144 ? -101.546 34.037 -40.800 1.00 33.25 ? 144  ASN A CB  1 
ATOM   1077 C CG  . ASN A 1 144 ? -102.828 33.576 -41.479 1.00 34.01 ? 144  ASN A CG  1 
ATOM   1078 O OD1 . ASN A 1 144 ? -103.861 34.269 -41.470 1.00 33.43 ? 144  ASN A OD1 1 
ATOM   1079 N ND2 . ASN A 1 144 ? -102.763 32.396 -42.091 1.00 34.94 ? 144  ASN A ND2 1 
ATOM   1080 N N   . LEU A 1 145 ? -103.457 34.474 -37.750 1.00 35.80 ? 145  LEU A N   1 
ATOM   1081 C CA  . LEU A 1 145 ? -104.208 33.835 -36.684 1.00 36.73 ? 145  LEU A CA  1 
ATOM   1082 C C   . LEU A 1 145 ? -105.260 32.927 -37.272 1.00 37.98 ? 145  LEU A C   1 
ATOM   1083 O O   . LEU A 1 145 ? -105.682 33.113 -38.416 1.00 38.27 ? 145  LEU A O   1 
ATOM   1084 C CB  . LEU A 1 145 ? -104.857 34.890 -35.783 1.00 36.58 ? 145  LEU A CB  1 
ATOM   1085 C CG  . LEU A 1 145 ? -103.924 35.909 -35.108 1.00 36.14 ? 145  LEU A CG  1 
ATOM   1086 C CD1 . LEU A 1 145 ? -104.714 37.069 -34.520 1.00 35.55 ? 145  LEU A CD1 1 
ATOM   1087 C CD2 . LEU A 1 145 ? -103.080 35.263 -34.039 1.00 35.58 ? 145  LEU A CD2 1 
ATOM   1088 N N   . MET A 1 146 ? -105.677 31.942 -36.482 1.00 39.34 ? 146  MET A N   1 
ATOM   1089 C CA  . MET A 1 146 ? -106.599 30.912 -36.930 1.00 40.43 ? 146  MET A CA  1 
ATOM   1090 C C   . MET A 1 146 ? -107.928 31.074 -36.229 1.00 40.45 ? 146  MET A C   1 
ATOM   1091 O O   . MET A 1 146 ? -107.970 31.277 -35.020 1.00 40.57 ? 146  MET A O   1 
ATOM   1092 C CB  . MET A 1 146 ? -106.038 29.534 -36.592 1.00 41.17 ? 146  MET A CB  1 
ATOM   1093 C CG  . MET A 1 146 ? -104.769 29.174 -37.322 1.00 44.61 ? 146  MET A CG  1 
ATOM   1094 S SD  . MET A 1 146 ? -105.177 28.600 -38.972 1.00 51.68 ? 146  MET A SD  1 
ATOM   1095 C CE  . MET A 1 146 ? -104.595 30.002 -40.013 1.00 51.24 ? 146  MET A CE  1 
ATOM   1096 N N   . ALA A 1 147 ? -109.016 30.982 -36.983 1.00 40.53 ? 147  ALA A N   1 
ATOM   1097 C CA  . ALA A 1 147 ? -110.330 30.876 -36.366 1.00 40.78 ? 147  ALA A CA  1 
ATOM   1098 C C   . ALA A 1 147 ? -110.641 29.418 -36.000 1.00 41.05 ? 147  ALA A C   1 
ATOM   1099 O O   . ALA A 1 147 ? -111.562 29.159 -35.220 1.00 41.02 ? 147  ALA A O   1 
ATOM   1100 C CB  . ALA A 1 147 ? -111.404 31.441 -37.285 1.00 40.54 ? 147  ALA A CB  1 
ATOM   1101 N N   . GLU A 1 148 ? -109.860 28.485 -36.549 1.00 41.30 ? 148  GLU A N   1 
ATOM   1102 C CA  . GLU A 1 148 ? -110.121 27.055 -36.406 1.00 42.12 ? 148  GLU A CA  1 
ATOM   1103 C C   . GLU A 1 148 ? -110.410 26.597 -34.966 1.00 41.95 ? 148  GLU A C   1 
ATOM   1104 O O   . GLU A 1 148 ? -111.442 25.953 -34.738 1.00 42.30 ? 148  GLU A O   1 
ATOM   1105 C CB  . GLU A 1 148 ? -109.032 26.185 -37.057 1.00 42.66 ? 148  GLU A CB  1 
ATOM   1106 C CG  . GLU A 1 148 ? -109.507 24.766 -37.367 1.00 44.82 ? 148  GLU A CG  1 
ATOM   1107 C CD  . GLU A 1 148 ? -108.479 23.895 -38.096 1.00 48.06 ? 148  GLU A CD  1 
ATOM   1108 O OE1 . GLU A 1 148 ? -107.728 24.407 -38.960 1.00 49.91 ? 148  GLU A OE1 1 
ATOM   1109 O OE2 . GLU A 1 148 ? -108.432 22.674 -37.824 1.00 48.95 ? 148  GLU A OE2 1 
ATOM   1110 N N   . PRO A 1 149 ? -109.551 26.918 -33.996 1.00 41.49 ? 149  PRO A N   1 
ATOM   1111 C CA  . PRO A 1 149 ? -109.806 26.471 -32.624 1.00 41.39 ? 149  PRO A CA  1 
ATOM   1112 C C   . PRO A 1 149 ? -111.212 26.849 -32.159 1.00 41.26 ? 149  PRO A C   1 
ATOM   1113 O O   . PRO A 1 149 ? -111.916 25.988 -31.632 1.00 41.72 ? 149  PRO A O   1 
ATOM   1114 C CB  . PRO A 1 149 ? -108.730 27.191 -31.811 1.00 41.58 ? 149  PRO A CB  1 
ATOM   1115 C CG  . PRO A 1 149 ? -107.624 27.437 -32.788 1.00 41.27 ? 149  PRO A CG  1 
ATOM   1116 C CD  . PRO A 1 149 ? -108.295 27.688 -34.096 1.00 41.38 ? 149  PRO A CD  1 
ATOM   1117 N N   . ALA A 1 150 ? -111.628 28.086 -32.410 1.00 40.78 ? 150  ALA A N   1 
ATOM   1118 C CA  . ALA A 1 150 ? -112.903 28.597 -31.929 1.00 40.35 ? 150  ALA A CA  1 
ATOM   1119 C C   . ALA A 1 150 ? -114.100 28.066 -32.715 1.00 40.26 ? 150  ALA A C   1 
ATOM   1120 O O   . ALA A 1 150 ? -115.220 27.996 -32.190 1.00 40.53 ? 150  ALA A O   1 
ATOM   1121 C CB  . ALA A 1 150 ? -112.886 30.113 -31.944 1.00 40.43 ? 150  ALA A CB  1 
ATOM   1122 N N   . VAL A 1 151 ? -113.865 27.710 -33.976 1.00 39.95 ? 151  VAL A N   1 
ATOM   1123 C CA  . VAL A 1 151 ? -114.888 27.107 -34.833 1.00 39.49 ? 151  VAL A CA  1 
ATOM   1124 C C   . VAL A 1 151 ? -115.139 25.656 -34.400 1.00 39.58 ? 151  VAL A C   1 
ATOM   1125 O O   . VAL A 1 151 ? -116.289 25.227 -34.297 1.00 38.97 ? 151  VAL A O   1 
ATOM   1126 C CB  . VAL A 1 151 ? -114.482 27.189 -36.341 1.00 39.27 ? 151  VAL A CB  1 
ATOM   1127 C CG1 . VAL A 1 151 ? -115.246 26.185 -37.201 1.00 38.43 ? 151  VAL A CG1 1 
ATOM   1128 C CG2 . VAL A 1 151 ? -114.679 28.605 -36.875 1.00 39.16 ? 151  VAL A CG2 1 
ATOM   1129 N N   . LEU A 1 152 ? -114.049 24.917 -34.159 1.00 40.02 ? 152  LEU A N   1 
ATOM   1130 C CA  . LEU A 1 152 ? -114.103 23.560 -33.616 1.00 40.31 ? 152  LEU A CA  1 
ATOM   1131 C C   . LEU A 1 152 ? -114.926 23.586 -32.331 1.00 41.23 ? 152  LEU A C   1 
ATOM   1132 O O   . LEU A 1 152 ? -115.940 22.868 -32.210 1.00 41.15 ? 152  LEU A O   1 
ATOM   1133 C CB  . LEU A 1 152 ? -112.695 23.036 -33.336 1.00 39.84 ? 152  LEU A CB  1 
ATOM   1134 C CG  . LEU A 1 152 ? -112.039 21.967 -34.224 1.00 39.48 ? 152  LEU A CG  1 
ATOM   1135 C CD1 . LEU A 1 152 ? -112.737 21.800 -35.561 1.00 39.67 ? 152  LEU A CD1 1 
ATOM   1136 C CD2 . LEU A 1 152 ? -110.565 22.277 -34.434 1.00 38.88 ? 152  LEU A CD2 1 
ATOM   1137 N N   . LYS A 1 153 ? -114.501 24.450 -31.404 1.00 42.16 ? 153  LYS A N   1 
ATOM   1138 C CA  . LYS A 1 153 ? -115.186 24.691 -30.137 1.00 43.13 ? 153  LYS A CA  1 
ATOM   1139 C C   . LYS A 1 153 ? -116.689 24.878 -30.330 1.00 43.44 ? 153  LYS A C   1 
ATOM   1140 O O   . LYS A 1 153 ? -117.489 24.208 -29.683 1.00 43.68 ? 153  LYS A O   1 
ATOM   1141 C CB  . LYS A 1 153 ? -114.591 25.917 -29.448 1.00 43.53 ? 153  LYS A CB  1 
ATOM   1142 C CG  . LYS A 1 153 ? -114.976 26.073 -27.991 1.00 45.09 ? 153  LYS A CG  1 
ATOM   1143 C CD  . LYS A 1 153 ? -113.740 26.190 -27.115 1.00 47.65 ? 153  LYS A CD  1 
ATOM   1144 C CE  . LYS A 1 153 ? -114.092 26.098 -25.632 1.00 49.37 ? 153  LYS A CE  1 
ATOM   1145 N NZ  . LYS A 1 153 ? -115.010 27.200 -25.231 1.00 50.36 ? 153  LYS A NZ  1 
ATOM   1146 N N   . TRP A 1 154 ? -117.061 25.778 -31.233 1.00 43.89 ? 154  TRP A N   1 
ATOM   1147 C CA  . TRP A 1 154 ? -118.461 26.066 -31.501 1.00 44.50 ? 154  TRP A CA  1 
ATOM   1148 C C   . TRP A 1 154 ? -119.241 24.857 -32.029 1.00 45.25 ? 154  TRP A C   1 
ATOM   1149 O O   . TRP A 1 154 ? -120.361 24.618 -31.590 1.00 45.37 ? 154  TRP A O   1 
ATOM   1150 C CB  . TRP A 1 154 ? -118.591 27.246 -32.464 1.00 44.39 ? 154  TRP A CB  1 
ATOM   1151 C CG  . TRP A 1 154 ? -119.969 27.798 -32.505 1.00 44.17 ? 154  TRP A CG  1 
ATOM   1152 C CD1 . TRP A 1 154 ? -120.441 28.856 -31.797 1.00 44.08 ? 154  TRP A CD1 1 
ATOM   1153 C CD2 . TRP A 1 154 ? -121.071 27.306 -33.277 1.00 44.24 ? 154  TRP A CD2 1 
ATOM   1154 N NE1 . TRP A 1 154 ? -121.769 29.066 -32.084 1.00 44.34 ? 154  TRP A NE1 1 
ATOM   1155 C CE2 . TRP A 1 154 ? -122.181 28.126 -32.992 1.00 44.27 ? 154  TRP A CE2 1 
ATOM   1156 C CE3 . TRP A 1 154 ? -121.231 26.255 -34.192 1.00 44.34 ? 154  TRP A CE3 1 
ATOM   1157 C CZ2 . TRP A 1 154 ? -123.436 27.927 -33.578 1.00 44.31 ? 154  TRP A CZ2 1 
ATOM   1158 C CZ3 . TRP A 1 154 ? -122.471 26.058 -34.776 1.00 44.55 ? 154  TRP A CZ3 1 
ATOM   1159 C CH2 . TRP A 1 154 ? -123.561 26.893 -34.467 1.00 44.50 ? 154  TRP A CH2 1 
ATOM   1160 N N   . ILE A 1 155 ? -118.662 24.112 -32.970 1.00 46.11 ? 155  ILE A N   1 
ATOM   1161 C CA  . ILE A 1 155 ? -119.313 22.923 -33.529 1.00 47.04 ? 155  ILE A CA  1 
ATOM   1162 C C   . ILE A 1 155 ? -119.677 21.902 -32.437 1.00 47.97 ? 155  ILE A C   1 
ATOM   1163 O O   . ILE A 1 155 ? -120.793 21.382 -32.410 1.00 47.69 ? 155  ILE A O   1 
ATOM   1164 C CB  . ILE A 1 155 ? -118.417 22.263 -34.619 1.00 46.89 ? 155  ILE A CB  1 
ATOM   1165 C CG1 . ILE A 1 155 ? -118.406 23.109 -35.897 1.00 46.58 ? 155  ILE A CG1 1 
ATOM   1166 C CG2 . ILE A 1 155 ? -118.859 20.814 -34.914 1.00 46.20 ? 155  ILE A CG2 1 
ATOM   1167 C CD1 . ILE A 1 155 ? -117.407 22.637 -36.943 1.00 45.97 ? 155  ILE A CD1 1 
ATOM   1168 N N   . ARG A 1 156 ? -118.722 21.629 -31.550 1.00 49.35 ? 156  ARG A N   1 
ATOM   1169 C CA  . ARG A 1 156 ? -118.900 20.663 -30.469 1.00 50.98 ? 156  ARG A CA  1 
ATOM   1170 C C   . ARG A 1 156 ? -119.960 21.126 -29.456 1.00 51.64 ? 156  ARG A C   1 
ATOM   1171 O O   . ARG A 1 156 ? -120.762 20.318 -28.960 1.00 51.74 ? 156  ARG A O   1 
ATOM   1172 C CB  . ARG A 1 156 ? -117.567 20.411 -29.751 1.00 51.29 ? 156  ARG A CB  1 
ATOM   1173 C CG  . ARG A 1 156 ? -116.580 19.547 -30.524 1.00 52.76 ? 156  ARG A CG  1 
ATOM   1174 C CD  . ARG A 1 156 ? -115.355 19.144 -29.718 1.00 55.79 ? 156  ARG A CD  1 
ATOM   1175 N NE  . ARG A 1 156 ? -114.153 19.057 -30.552 1.00 58.76 ? 156  ARG A NE  1 
ATOM   1176 C CZ  . ARG A 1 156 ? -113.064 19.816 -30.408 1.00 59.95 ? 156  ARG A CZ  1 
ATOM   1177 N NH1 . ARG A 1 156 ? -113.001 20.741 -29.457 1.00 60.64 ? 156  ARG A NH1 1 
ATOM   1178 N NH2 . ARG A 1 156 ? -112.028 19.648 -31.224 1.00 60.33 ? 156  ARG A NH2 1 
ATOM   1179 N N   . GLU A 1 157 ? -119.959 22.428 -29.175 1.00 52.16 ? 157  GLU A N   1 
ATOM   1180 C CA  . GLU A 1 157 ? -120.834 23.016 -28.174 1.00 52.79 ? 157  GLU A CA  1 
ATOM   1181 C C   . GLU A 1 157 ? -122.214 23.421 -28.715 1.00 52.75 ? 157  GLU A C   1 
ATOM   1182 O O   . GLU A 1 157 ? -123.018 23.975 -27.970 1.00 52.77 ? 157  GLU A O   1 
ATOM   1183 C CB  . GLU A 1 157 ? -120.141 24.222 -27.515 1.00 53.20 ? 157  GLU A CB  1 
ATOM   1184 C CG  . GLU A 1 157 ? -119.214 23.860 -26.358 1.00 54.96 ? 157  GLU A CG  1 
ATOM   1185 C CD  . GLU A 1 157 ? -118.306 25.008 -25.912 1.00 56.94 ? 157  GLU A CD  1 
ATOM   1186 O OE1 . GLU A 1 157 ? -118.624 26.188 -26.199 1.00 58.21 ? 157  GLU A OE1 1 
ATOM   1187 O OE2 . GLU A 1 157 ? -117.263 24.732 -25.270 1.00 57.26 ? 157  GLU A OE2 1 
ATOM   1188 N N   . ASN A 1 158 ? -122.504 23.151 -29.989 1.00 52.72 ? 158  ASN A N   1 
ATOM   1189 C CA  . ASN A 1 158 ? -123.749 23.654 -30.584 1.00 52.78 ? 158  ASN A CA  1 
ATOM   1190 C C   . ASN A 1 158 ? -124.513 22.706 -31.506 1.00 52.91 ? 158  ASN A C   1 
ATOM   1191 O O   . ASN A 1 158 ? -125.717 22.891 -31.726 1.00 52.66 ? 158  ASN A O   1 
ATOM   1192 C CB  . ASN A 1 158 ? -123.500 24.982 -31.312 1.00 52.73 ? 158  ASN A CB  1 
ATOM   1193 C CG  . ASN A 1 158 ? -123.358 26.152 -30.362 1.00 52.62 ? 158  ASN A CG  1 
ATOM   1194 O OD1 . ASN A 1 158 ? -124.279 26.946 -30.204 1.00 53.05 ? 158  ASN A OD1 1 
ATOM   1195 N ND2 . ASN A 1 158 ? -122.198 26.267 -29.728 1.00 52.29 ? 158  ASN A ND2 1 
ATOM   1196 N N   . ILE A 1 159 ? -123.820 21.724 -32.073 1.00 53.16 ? 159  ILE A N   1 
ATOM   1197 C CA  . ILE A 1 159 ? -124.475 20.737 -32.936 1.00 53.63 ? 159  ILE A CA  1 
ATOM   1198 C C   . ILE A 1 159 ? -124.444 19.380 -32.241 1.00 53.76 ? 159  ILE A C   1 
ATOM   1199 O O   . ILE A 1 159 ? -123.360 18.820 -31.999 1.00 53.69 ? 159  ILE A O   1 
ATOM   1200 C CB  . ILE A 1 159 ? -123.811 20.677 -34.343 1.00 53.88 ? 159  ILE A CB  1 
ATOM   1201 C CG1 . ILE A 1 159 ? -123.768 22.071 -34.975 1.00 54.17 ? 159  ILE A CG1 1 
ATOM   1202 C CG2 . ILE A 1 159 ? -124.562 19.703 -35.269 1.00 53.93 ? 159  ILE A CG2 1 
ATOM   1203 C CD1 . ILE A 1 159 ? -122.554 22.313 -35.844 1.00 54.60 ? 159  ILE A CD1 1 
ATOM   1204 N N   . SER A 1 160 ? -125.627 18.862 -31.907 1.00 53.81 ? 160  SER A N   1 
ATOM   1205 C CA  . SER A 1 160 ? -125.702 17.663 -31.071 1.00 54.11 ? 160  SER A CA  1 
ATOM   1206 C C   . SER A 1 160 ? -125.076 16.430 -31.749 1.00 54.20 ? 160  SER A C   1 
ATOM   1207 O O   . SER A 1 160 ? -124.357 15.649 -31.111 1.00 53.96 ? 160  SER A O   1 
ATOM   1208 C CB  . SER A 1 160 ? -127.134 17.407 -30.556 1.00 54.05 ? 160  SER A CB  1 
ATOM   1209 O OG  . SER A 1 160 ? -128.092 17.278 -31.596 1.00 53.99 ? 160  SER A OG  1 
ATOM   1210 N N   . GLU A 1 161 ? -125.305 16.306 -33.053 1.00 54.41 ? 161  GLU A N   1 
ATOM   1211 C CA  . GLU A 1 161 ? -124.869 15.145 -33.833 1.00 54.73 ? 161  GLU A CA  1 
ATOM   1212 C C   . GLU A 1 161 ? -123.446 15.271 -34.421 1.00 54.40 ? 161  GLU A C   1 
ATOM   1213 O O   . GLU A 1 161 ? -123.101 14.557 -35.366 1.00 54.52 ? 161  GLU A O   1 
ATOM   1214 C CB  . GLU A 1 161 ? -125.877 14.882 -34.966 1.00 55.02 ? 161  GLU A CB  1 
ATOM   1215 C CG  . GLU A 1 161 ? -127.347 14.994 -34.572 1.00 56.30 ? 161  GLU A CG  1 
ATOM   1216 C CD  . GLU A 1 161 ? -127.894 16.420 -34.651 1.00 58.01 ? 161  GLU A CD  1 
ATOM   1217 O OE1 . GLU A 1 161 ? -127.134 17.399 -34.410 1.00 58.54 ? 161  GLU A OE1 1 
ATOM   1218 O OE2 . GLU A 1 161 ? -129.104 16.567 -34.951 1.00 58.54 ? 161  GLU A OE2 1 
ATOM   1219 N N   . TRP A 1 162 ? -122.621 16.152 -33.857 1.00 53.93 ? 162  TRP A N   1 
ATOM   1220 C CA  . TRP A 1 162 ? -121.315 16.469 -34.444 1.00 53.45 ? 162  TRP A CA  1 
ATOM   1221 C C   . TRP A 1 162 ? -120.346 15.286 -34.644 1.00 53.74 ? 162  TRP A C   1 
ATOM   1222 O O   . TRP A 1 162 ? -119.458 15.367 -35.496 1.00 53.83 ? 162  TRP A O   1 
ATOM   1223 C CB  . TRP A 1 162 ? -120.631 17.633 -33.702 1.00 52.88 ? 162  TRP A CB  1 
ATOM   1224 C CG  . TRP A 1 162 ? -120.063 17.301 -32.365 1.00 51.37 ? 162  TRP A CG  1 
ATOM   1225 C CD1 . TRP A 1 162 ? -120.687 17.426 -31.159 1.00 50.65 ? 162  TRP A CD1 1 
ATOM   1226 C CD2 . TRP A 1 162 ? -118.743 16.813 -32.082 1.00 50.52 ? 162  TRP A CD2 1 
ATOM   1227 N NE1 . TRP A 1 162 ? -119.845 17.036 -30.143 1.00 49.77 ? 162  TRP A NE1 1 
ATOM   1228 C CE2 . TRP A 1 162 ? -118.647 16.650 -30.680 1.00 49.82 ? 162  TRP A CE2 1 
ATOM   1229 C CE3 . TRP A 1 162 ? -117.629 16.490 -32.873 1.00 50.25 ? 162  TRP A CE3 1 
ATOM   1230 C CZ2 . TRP A 1 162 ? -117.488 16.185 -30.051 1.00 49.88 ? 162  TRP A CZ2 1 
ATOM   1231 C CZ3 . TRP A 1 162 ? -116.471 16.025 -32.246 1.00 50.33 ? 162  TRP A CZ3 1 
ATOM   1232 C CH2 . TRP A 1 162 ? -116.412 15.879 -30.846 1.00 50.27 ? 162  TRP A CH2 1 
ATOM   1233 N N   . ARG A 1 163 ? -120.521 14.200 -33.885 1.00 53.78 ? 163  ARG A N   1 
ATOM   1234 C CA  . ARG A 1 163 ? -119.610 13.050 -33.964 1.00 53.86 ? 163  ARG A CA  1 
ATOM   1235 C C   . ARG A 1 163 ? -119.791 12.245 -35.260 1.00 53.53 ? 163  ARG A C   1 
ATOM   1236 O O   . ARG A 1 163 ? -118.866 11.556 -35.720 1.00 53.27 ? 163  ARG A O   1 
ATOM   1237 C CB  . ARG A 1 163 ? -119.746 12.146 -32.735 1.00 54.17 ? 163  ARG A CB  1 
ATOM   1238 C CG  . ARG A 1 163 ? -119.406 12.833 -31.420 1.00 55.49 ? 163  ARG A CG  1 
ATOM   1239 C CD  . ARG A 1 163 ? -118.315 12.154 -30.591 1.00 57.32 ? 163  ARG A CD  1 
ATOM   1240 N NE  . ARG A 1 163 ? -118.225 12.762 -29.260 1.00 58.46 ? 163  ARG A NE  1 
ATOM   1241 C CZ  . ARG A 1 163 ? -117.101 12.926 -28.571 1.00 58.61 ? 163  ARG A CZ  1 
ATOM   1242 N NH1 . ARG A 1 163 ? -115.938 12.518 -29.061 1.00 59.03 ? 163  ARG A NH1 1 
ATOM   1243 N NH2 . ARG A 1 163 ? -117.145 13.500 -27.380 1.00 58.70 ? 163  ARG A NH2 1 
ATOM   1244 N N   . ASN A 1 164 ? -120.986 12.340 -35.840 1.00 53.06 ? 164  ASN A N   1 
ATOM   1245 C CA  . ASN A 1 164 ? -121.245 11.770 -37.154 1.00 52.67 ? 164  ASN A CA  1 
ATOM   1246 C C   . ASN A 1 164 ? -121.662 12.838 -38.163 1.00 51.98 ? 164  ASN A C   1 
ATOM   1247 O O   . ASN A 1 164 ? -122.520 12.595 -39.016 1.00 52.25 ? 164  ASN A O   1 
ATOM   1248 C CB  . ASN A 1 164 ? -122.296 10.646 -37.086 1.00 53.17 ? 164  ASN A CB  1 
ATOM   1249 C CG  . ASN A 1 164 ? -121.932 9.545  -36.086 1.00 53.99 ? 164  ASN A CG  1 
ATOM   1250 O OD1 . ASN A 1 164 ? -120.800 9.034  -36.064 1.00 54.12 ? 164  ASN A OD1 1 
ATOM   1251 N ND2 . ASN A 1 164 ? -122.906 9.168  -35.256 1.00 54.57 ? 164  ASN A ND2 1 
ATOM   1252 N N   . CYS A 1 165 ? -121.060 14.023 -38.066 1.00 50.74 ? 165  CYS A N   1 
ATOM   1253 C CA  . CYS A 1 165 ? -121.288 15.062 -39.064 1.00 49.51 ? 165  CYS A CA  1 
ATOM   1254 C C   . CYS A 1 165 ? -120.275 14.942 -40.211 1.00 48.56 ? 165  CYS A C   1 
ATOM   1255 O O   . CYS A 1 165 ? -119.307 14.186 -40.125 1.00 48.37 ? 165  CYS A O   1 
ATOM   1256 C CB  . CYS A 1 165 ? -121.254 16.459 -38.423 1.00 49.63 ? 165  CYS A CB  1 
ATOM   1257 S SG  . CYS A 1 165 ? -119.610 17.204 -38.237 1.00 49.44 ? 165  CYS A SG  1 
ATOM   1258 N N   . THR A 1 166 ? -120.520 15.675 -41.289 1.00 47.35 ? 166  THR A N   1 
ATOM   1259 C CA  . THR A 1 166 ? -119.537 15.823 -42.355 1.00 46.27 ? 166  THR A CA  1 
ATOM   1260 C C   . THR A 1 166 ? -119.310 17.308 -42.689 1.00 45.16 ? 166  THR A C   1 
ATOM   1261 O O   . THR A 1 166 ? -120.261 18.098 -42.769 1.00 44.94 ? 166  THR A O   1 
ATOM   1262 C CB  . THR A 1 166 ? -119.925 14.982 -43.612 1.00 46.48 ? 166  THR A CB  1 
ATOM   1263 O OG1 . THR A 1 166 ? -119.371 15.578 -44.797 1.00 46.74 ? 166  THR A OG1 1 
ATOM   1264 C CG2 . THR A 1 166 ? -121.425 15.009 -43.856 1.00 46.35 ? 166  THR A CG2 1 
ATOM   1265 N N   . ILE A 1 167 ? -118.041 17.673 -42.862 1.00 43.70 ? 167  ILE A N   1 
ATOM   1266 C CA  . ILE A 1 167 ? -117.657 19.042 -43.204 1.00 42.25 ? 167  ILE A CA  1 
ATOM   1267 C C   . ILE A 1 167 ? -117.564 19.158 -44.711 1.00 41.25 ? 167  ILE A C   1 
ATOM   1268 O O   . ILE A 1 167 ? -116.860 18.385 -45.359 1.00 40.93 ? 167  ILE A O   1 
ATOM   1269 C CB  . ILE A 1 167 ? -116.319 19.405 -42.537 1.00 42.30 ? 167  ILE A CB  1 
ATOM   1270 C CG1 . ILE A 1 167 ? -116.308 18.945 -41.066 1.00 42.62 ? 167  ILE A CG1 1 
ATOM   1271 C CG2 . ILE A 1 167 ? -116.018 20.899 -42.679 1.00 41.60 ? 167  ILE A CG2 1 
ATOM   1272 C CD1 . ILE A 1 167 ? -117.468 19.500 -40.199 1.00 42.45 ? 167  ILE A CD1 1 
ATOM   1273 N N   . VAL A 1 168 ? -118.295 20.114 -45.270 1.00 40.29 ? 168  VAL A N   1 
ATOM   1274 C CA  . VAL A 1 168 ? -118.413 20.229 -46.719 1.00 39.43 ? 168  VAL A CA  1 
ATOM   1275 C C   . VAL A 1 168 ? -117.806 21.522 -47.205 1.00 39.13 ? 168  VAL A C   1 
ATOM   1276 O O   . VAL A 1 168 ? -118.168 22.593 -46.728 1.00 39.26 ? 168  VAL A O   1 
ATOM   1277 C CB  . VAL A 1 168 ? -119.879 20.173 -47.178 1.00 39.21 ? 168  VAL A CB  1 
ATOM   1278 C CG1 . VAL A 1 168 ? -119.967 20.187 -48.691 1.00 39.00 ? 168  VAL A CG1 1 
ATOM   1279 C CG2 . VAL A 1 168 ? -120.563 18.946 -46.620 1.00 39.37 ? 168  VAL A CG2 1 
ATOM   1280 N N   . SER A 1 169 ? -116.881 21.420 -48.154 1.00 38.76 ? 169  SER A N   1 
ATOM   1281 C CA  . SER A 1 169 ? -116.334 22.598 -48.811 1.00 38.38 ? 169  SER A CA  1 
ATOM   1282 C C   . SER A 1 169 ? -117.243 22.973 -49.967 1.00 38.28 ? 169  SER A C   1 
ATOM   1283 O O   . SER A 1 169 ? -117.601 22.110 -50.766 1.00 38.26 ? 169  SER A O   1 
ATOM   1284 C CB  . SER A 1 169 ? -114.913 22.336 -49.324 1.00 38.31 ? 169  SER A CB  1 
ATOM   1285 O OG  . SER A 1 169 ? -114.466 23.406 -50.136 1.00 37.62 ? 169  SER A OG  1 
ATOM   1286 N N   . PRO A 1 170 ? -117.600 24.257 -50.050 1.00 38.32 ? 170  PRO A N   1 
ATOM   1287 C CA  . PRO A 1 170 ? -118.474 24.787 -51.109 1.00 38.44 ? 170  PRO A CA  1 
ATOM   1288 C C   . PRO A 1 170 ? -117.871 24.681 -52.510 1.00 38.71 ? 170  PRO A C   1 
ATOM   1289 O O   . PRO A 1 170 ? -118.615 24.566 -53.487 1.00 38.68 ? 170  PRO A O   1 
ATOM   1290 C CB  . PRO A 1 170 ? -118.605 26.270 -50.742 1.00 38.48 ? 170  PRO A CB  1 
ATOM   1291 C CG  . PRO A 1 170 ? -118.194 26.366 -49.315 1.00 38.32 ? 170  PRO A CG  1 
ATOM   1292 C CD  . PRO A 1 170 ? -117.184 25.303 -49.099 1.00 38.15 ? 170  PRO A CD  1 
ATOM   1293 N N   . ASP A 1 171 ? -116.545 24.755 -52.601 1.00 39.02 ? 171  ASP A N   1 
ATOM   1294 C CA  . ASP A 1 171 ? -115.830 24.622 -53.873 1.00 39.32 ? 171  ASP A CA  1 
ATOM   1295 C C   . ASP A 1 171 ? -114.720 23.590 -53.724 1.00 39.61 ? 171  ASP A C   1 
ATOM   1296 O O   . ASP A 1 171 ? -114.448 23.108 -52.616 1.00 39.44 ? 171  ASP A O   1 
ATOM   1297 C CB  . ASP A 1 171 ? -115.241 25.965 -54.306 1.00 39.19 ? 171  ASP A CB  1 
ATOM   1298 C CG  . ASP A 1 171 ? -114.654 26.748 -53.144 1.00 39.09 ? 171  ASP A CG  1 
ATOM   1299 O OD1 . ASP A 1 171 ? -114.923 27.956 -53.059 1.00 39.96 ? 171  ASP A OD1 1 
ATOM   1300 O OD2 . ASP A 1 171 ? -113.925 26.248 -52.265 1.00 38.54 ? 171  ASP A OD2 1 
ATOM   1301 N N   . ALA A 1 172 ? -114.088 23.248 -54.843 1.00 40.13 ? 172  ALA A N   1 
ATOM   1302 C CA  . ALA A 1 172 ? -112.961 22.312 -54.842 1.00 40.57 ? 172  ALA A CA  1 
ATOM   1303 C C   . ALA A 1 172 ? -111.689 22.934 -54.244 1.00 40.72 ? 172  ALA A C   1 
ATOM   1304 O O   . ALA A 1 172 ? -110.941 22.276 -53.519 1.00 41.05 ? 172  ALA A O   1 
ATOM   1305 C CB  . ALA A 1 172 ? -112.709 21.787 -56.238 1.00 40.75 ? 172  ALA A CB  1 
ATOM   1306 N N   . GLY A 1 173 ? -111.468 24.212 -54.509 1.00 40.81 ? 173  GLY A N   1 
ATOM   1307 C CA  . GLY A 1 173 ? -110.357 24.913 -53.893 1.00 41.06 ? 173  GLY A CA  1 
ATOM   1308 C C   . GLY A 1 173 ? -110.468 25.099 -52.389 1.00 41.16 ? 173  GLY A C   1 
ATOM   1309 O O   . GLY A 1 173 ? -109.657 25.804 -51.792 1.00 41.69 ? 173  GLY A O   1 
ATOM   1310 N N   . GLY A 1 174 ? -111.464 24.474 -51.764 1.00 40.92 ? 174  GLY A N   1 
ATOM   1311 C CA  . GLY A 1 174 ? -111.646 24.597 -50.326 1.00 40.18 ? 174  GLY A CA  1 
ATOM   1312 C C   . GLY A 1 174 ? -111.282 23.341 -49.562 1.00 39.64 ? 174  GLY A C   1 
ATOM   1313 O O   . GLY A 1 174 ? -111.408 23.305 -48.337 1.00 39.77 ? 174  GLY A O   1 
ATOM   1314 N N   . ALA A 1 175 ? -110.815 22.330 -50.289 1.00 39.17 ? 175  ALA A N   1 
ATOM   1315 C CA  . ALA A 1 175 ? -110.477 21.022 -49.737 1.00 39.06 ? 175  ALA A CA  1 
ATOM   1316 C C   . ALA A 1 175 ? -109.626 21.026 -48.468 1.00 39.09 ? 175  ALA A C   1 
ATOM   1317 O O   . ALA A 1 175 ? -110.021 20.441 -47.458 1.00 38.98 ? 175  ALA A O   1 
ATOM   1318 C CB  . ALA A 1 175 ? -109.814 20.170 -50.798 1.00 39.07 ? 175  ALA A CB  1 
ATOM   1319 N N   . LYS A 1 176 ? -108.464 21.673 -48.522 1.00 39.12 ? 176  LYS A N   1 
ATOM   1320 C CA  . LYS A 1 176 ? -107.508 21.619 -47.415 1.00 39.20 ? 176  LYS A CA  1 
ATOM   1321 C C   . LYS A 1 176 ? -108.102 22.124 -46.099 1.00 38.91 ? 176  LYS A C   1 
ATOM   1322 O O   . LYS A 1 176 ? -107.847 21.560 -45.030 1.00 38.77 ? 176  LYS A O   1 
ATOM   1323 C CB  . LYS A 1 176 ? -106.235 22.389 -47.761 1.00 39.40 ? 176  LYS A CB  1 
ATOM   1324 C CG  . LYS A 1 176 ? -104.966 21.639 -47.382 1.00 40.73 ? 176  LYS A CG  1 
ATOM   1325 C CD  . LYS A 1 176 ? -103.777 22.055 -48.239 1.00 42.68 ? 176  LYS A CD  1 
ATOM   1326 C CE  . LYS A 1 176 ? -102.565 21.178 -47.940 1.00 43.97 ? 176  LYS A CE  1 
ATOM   1327 N NZ  . LYS A 1 176 ? -102.739 19.778 -48.486 1.00 44.57 ? 176  LYS A NZ  1 
ATOM   1328 N N   . ARG A 1 177 ? -108.912 23.176 -46.195 1.00 38.54 ? 177  ARG A N   1 
ATOM   1329 C CA  . ARG A 1 177 ? -109.560 23.769 -45.036 1.00 38.27 ? 177  ARG A CA  1 
ATOM   1330 C C   . ARG A 1 177 ? -110.522 22.798 -44.343 1.00 37.49 ? 177  ARG A C   1 
ATOM   1331 O O   . ARG A 1 177 ? -110.473 22.645 -43.119 1.00 37.09 ? 177  ARG A O   1 
ATOM   1332 C CB  . ARG A 1 177 ? -110.303 25.024 -45.464 1.00 38.81 ? 177  ARG A CB  1 
ATOM   1333 C CG  . ARG A 1 177 ? -110.423 26.103 -44.396 1.00 41.04 ? 177  ARG A CG  1 
ATOM   1334 C CD  . ARG A 1 177 ? -111.261 27.324 -44.837 1.00 44.29 ? 177  ARG A CD  1 
ATOM   1335 N NE  . ARG A 1 177 ? -110.655 28.020 -45.979 1.00 47.03 ? 177  ARG A NE  1 
ATOM   1336 C CZ  . ARG A 1 177 ? -111.059 27.915 -47.252 1.00 49.06 ? 177  ARG A CZ  1 
ATOM   1337 N NH1 . ARG A 1 177 ? -112.094 27.143 -47.586 1.00 50.07 ? 177  ARG A NH1 1 
ATOM   1338 N NH2 . ARG A 1 177 ? -110.423 28.595 -48.202 1.00 49.79 ? 177  ARG A NH2 1 
ATOM   1339 N N   . VAL A 1 178 ? -111.381 22.148 -45.129 1.00 36.79 ? 178  VAL A N   1 
ATOM   1340 C CA  . VAL A 1 178 ? -112.401 21.248 -44.583 1.00 36.27 ? 178  VAL A CA  1 
ATOM   1341 C C   . VAL A 1 178 ? -111.840 19.925 -44.059 1.00 36.05 ? 178  VAL A C   1 
ATOM   1342 O O   . VAL A 1 178 ? -112.282 19.451 -43.001 1.00 36.04 ? 178  VAL A O   1 
ATOM   1343 C CB  . VAL A 1 178 ? -113.625 21.008 -45.550 1.00 36.36 ? 178  VAL A CB  1 
ATOM   1344 C CG1 . VAL A 1 178 ? -114.331 22.318 -45.877 1.00 35.64 ? 178  VAL A CG1 1 
ATOM   1345 C CG2 . VAL A 1 178 ? -113.239 20.235 -46.821 1.00 36.67 ? 178  VAL A CG2 1 
ATOM   1346 N N   . THR A 1 179 ? -110.870 19.344 -44.776 1.00 35.56 ? 179  THR A N   1 
ATOM   1347 C CA  . THR A 1 179 ? -110.217 18.110 -44.325 1.00 35.46 ? 179  THR A CA  1 
ATOM   1348 C C   . THR A 1 179 ? -109.456 18.309 -43.021 1.00 35.73 ? 179  THR A C   1 
ATOM   1349 O O   . THR A 1 179 ? -109.350 17.397 -42.224 1.00 35.97 ? 179  THR A O   1 
ATOM   1350 C CB  . THR A 1 179 ? -109.265 17.512 -45.394 1.00 35.15 ? 179  THR A CB  1 
ATOM   1351 O OG1 . THR A 1 179 ? -108.380 18.529 -45.877 1.00 35.93 ? 179  THR A OG1 1 
ATOM   1352 C CG2 . THR A 1 179 ? -110.022 17.079 -46.618 1.00 33.87 ? 179  THR A CG2 1 
ATOM   1353 N N   . SER A 1 180 ? -108.912 19.498 -42.813 1.00 36.38 ? 180  SER A N   1 
ATOM   1354 C CA  . SER A 1 180 ? -108.227 19.812 -41.567 1.00 36.90 ? 180  SER A CA  1 
ATOM   1355 C C   . SER A 1 180 ? -109.214 19.859 -40.400 1.00 37.35 ? 180  SER A C   1 
ATOM   1356 O O   . SER A 1 180 ? -108.911 19.353 -39.321 1.00 37.22 ? 180  SER A O   1 
ATOM   1357 C CB  . SER A 1 180 ? -107.461 21.125 -41.690 1.00 36.93 ? 180  SER A CB  1 
ATOM   1358 O OG  . SER A 1 180 ? -107.460 21.821 -40.455 1.00 37.85 ? 180  SER A OG  1 
ATOM   1359 N N   . ILE A 1 181 ? -110.387 20.460 -40.622 1.00 37.99 ? 181  ILE A N   1 
ATOM   1360 C CA  . ILE A 1 181 ? -111.445 20.477 -39.610 1.00 38.67 ? 181  ILE A CA  1 
ATOM   1361 C C   . ILE A 1 181 ? -111.998 19.065 -39.371 1.00 39.57 ? 181  ILE A C   1 
ATOM   1362 O O   . ILE A 1 181 ? -112.138 18.628 -38.223 1.00 39.65 ? 181  ILE A O   1 
ATOM   1363 C CB  . ILE A 1 181 ? -112.570 21.477 -39.989 1.00 38.48 ? 181  ILE A CB  1 
ATOM   1364 C CG1 . ILE A 1 181 ? -112.110 22.916 -39.727 1.00 38.41 ? 181  ILE A CG1 1 
ATOM   1365 C CG2 . ILE A 1 181 ? -113.861 21.204 -39.197 1.00 38.23 ? 181  ILE A CG2 1 
ATOM   1366 C CD1 . ILE A 1 181 ? -112.795 23.970 -40.595 1.00 37.17 ? 181  ILE A CD1 1 
ATOM   1367 N N   . ALA A 1 182 ? -112.297 18.356 -40.459 1.00 40.68 ? 182  ALA A N   1 
ATOM   1368 C CA  . ALA A 1 182 ? -112.826 16.990 -40.399 1.00 41.39 ? 182  ALA A CA  1 
ATOM   1369 C C   . ALA A 1 182 ? -111.904 16.037 -39.643 1.00 41.92 ? 182  ALA A C   1 
ATOM   1370 O O   . ALA A 1 182 ? -112.376 15.152 -38.936 1.00 42.06 ? 182  ALA A O   1 
ATOM   1371 C CB  . ALA A 1 182 ? -113.102 16.462 -41.801 1.00 41.32 ? 182  ALA A CB  1 
ATOM   1372 N N   . ASP A 1 183 ? -110.598 16.229 -39.794 1.00 42.79 ? 183  ASP A N   1 
ATOM   1373 C CA  . ASP A 1 183 ? -109.603 15.404 -39.105 1.00 43.94 ? 183  ASP A CA  1 
ATOM   1374 C C   . ASP A 1 183 ? -109.509 15.693 -37.607 1.00 44.68 ? 183  ASP A C   1 
ATOM   1375 O O   . ASP A 1 183 ? -109.210 14.797 -36.808 1.00 44.81 ? 183  ASP A O   1 
ATOM   1376 C CB  . ASP A 1 183 ? -108.225 15.563 -39.757 1.00 43.94 ? 183  ASP A CB  1 
ATOM   1377 C CG  . ASP A 1 183 ? -108.120 14.829 -41.082 1.00 44.10 ? 183  ASP A CG  1 
ATOM   1378 O OD1 . ASP A 1 183 ? -109.124 14.230 -41.512 1.00 44.02 ? 183  ASP A OD1 1 
ATOM   1379 O OD2 . ASP A 1 183 ? -107.075 14.801 -41.769 1.00 44.28 ? 183  ASP A OD2 1 
ATOM   1380 N N   . ARG A 1 184 ? -109.757 16.946 -37.235 1.00 45.58 ? 184  ARG A N   1 
ATOM   1381 C CA  . ARG A 1 184 ? -109.707 17.367 -35.837 1.00 46.30 ? 184  ARG A CA  1 
ATOM   1382 C C   . ARG A 1 184 ? -110.872 16.793 -35.048 1.00 45.79 ? 184  ARG A C   1 
ATOM   1383 O O   . ARG A 1 184 ? -110.690 16.318 -33.937 1.00 45.84 ? 184  ARG A O   1 
ATOM   1384 C CB  . ARG A 1 184 ? -109.672 18.890 -35.729 1.00 47.01 ? 184  ARG A CB  1 
ATOM   1385 C CG  . ARG A 1 184 ? -108.305 19.499 -36.013 1.00 50.66 ? 184  ARG A CG  1 
ATOM   1386 C CD  . ARG A 1 184 ? -107.230 19.092 -35.014 1.00 56.07 ? 184  ARG A CD  1 
ATOM   1387 N NE  . ARG A 1 184 ? -106.421 20.219 -34.535 1.00 60.47 ? 184  ARG A NE  1 
ATOM   1388 C CZ  . ARG A 1 184 ? -105.195 20.510 -34.983 1.00 62.92 ? 184  ARG A CZ  1 
ATOM   1389 N NH1 . ARG A 1 184 ? -104.629 19.771 -35.942 1.00 63.80 ? 184  ARG A NH1 1 
ATOM   1390 N NH2 . ARG A 1 184 ? -104.531 21.546 -34.473 1.00 63.80 ? 184  ARG A NH2 1 
ATOM   1391 N N   . LEU A 1 185 ? -112.056 16.817 -35.653 1.00 45.44 ? 185  LEU A N   1 
ATOM   1392 C CA  . LEU A 1 185 ? -113.270 16.276 -35.058 1.00 45.11 ? 185  LEU A CA  1 
ATOM   1393 C C   . LEU A 1 185 ? -113.370 14.756 -35.217 1.00 45.06 ? 185  LEU A C   1 
ATOM   1394 O O   . LEU A 1 185 ? -114.256 14.124 -34.631 1.00 45.24 ? 185  LEU A O   1 
ATOM   1395 C CB  . LEU A 1 185 ? -114.495 16.914 -35.720 1.00 45.03 ? 185  LEU A CB  1 
ATOM   1396 C CG  . LEU A 1 185 ? -114.681 18.431 -35.673 1.00 44.81 ? 185  LEU A CG  1 
ATOM   1397 C CD1 . LEU A 1 185 ? -116.002 18.816 -36.336 1.00 43.56 ? 185  LEU A CD1 1 
ATOM   1398 C CD2 . LEU A 1 185 ? -114.608 18.945 -34.229 1.00 45.14 ? 185  LEU A CD2 1 
ATOM   1399 N N   . ASN A 1 186 ? -112.455 14.187 -36.003 1.00 44.76 ? 186  ASN A N   1 
ATOM   1400 C CA  . ASN A 1 186 ? -112.538 12.810 -36.494 1.00 44.47 ? 186  ASN A CA  1 
ATOM   1401 C C   . ASN A 1 186 ? -113.867 12.494 -37.169 1.00 43.60 ? 186  ASN A C   1 
ATOM   1402 O O   . ASN A 1 186 ? -114.536 11.522 -36.832 1.00 43.82 ? 186  ASN A O   1 
ATOM   1403 C CB  . ASN A 1 186 ? -112.199 11.784 -35.402 1.00 44.92 ? 186  ASN A CB  1 
ATOM   1404 C CG  . ASN A 1 186 ? -110.854 11.123 -35.640 1.00 46.23 ? 186  ASN A CG  1 
ATOM   1405 O OD1 . ASN A 1 186 ? -110.637 10.470 -36.671 1.00 47.05 ? 186  ASN A OD1 1 
ATOM   1406 N ND2 . ASN A 1 186 ? -109.929 11.315 -34.702 1.00 47.15 ? 186  ASN A ND2 1 
ATOM   1407 N N   . VAL A 1 187 ? -114.257 13.335 -38.116 1.00 42.52 ? 187  VAL A N   1 
ATOM   1408 C CA  . VAL A 1 187 ? -115.480 13.083 -38.875 1.00 41.37 ? 187  VAL A CA  1 
ATOM   1409 C C   . VAL A 1 187 ? -115.199 13.019 -40.377 1.00 40.48 ? 187  VAL A C   1 
ATOM   1410 O O   . VAL A 1 187 ? -114.041 13.030 -40.797 1.00 40.28 ? 187  VAL A O   1 
ATOM   1411 C CB  . VAL A 1 187 ? -116.600 14.100 -38.554 1.00 41.39 ? 187  VAL A CB  1 
ATOM   1412 C CG1 . VAL A 1 187 ? -116.940 14.054 -37.070 1.00 40.93 ? 187  VAL A CG1 1 
ATOM   1413 C CG2 . VAL A 1 187 ? -116.223 15.533 -39.019 1.00 41.24 ? 187  VAL A CG2 1 
ATOM   1414 N N   . ASP A 1 188 ? -116.268 12.944 -41.163 1.00 39.50 ? 188  ASP A N   1 
ATOM   1415 C CA  . ASP A 1 188 ? -116.189 12.848 -42.610 1.00 38.70 ? 188  ASP A CA  1 
ATOM   1416 C C   . ASP A 1 188 ? -115.972 14.211 -43.239 1.00 38.06 ? 188  ASP A C   1 
ATOM   1417 O O   . ASP A 1 188 ? -116.181 15.241 -42.602 1.00 38.33 ? 188  ASP A O   1 
ATOM   1418 C CB  . ASP A 1 188 ? -117.493 12.268 -43.153 1.00 38.80 ? 188  ASP A CB  1 
ATOM   1419 C CG  . ASP A 1 188 ? -117.585 10.756 -42.987 1.00 39.10 ? 188  ASP A CG  1 
ATOM   1420 O OD1 . ASP A 1 188 ? -116.729 10.160 -42.301 1.00 38.24 ? 188  ASP A OD1 1 
ATOM   1421 O OD2 . ASP A 1 188 ? -118.499 10.086 -43.519 1.00 40.28 ? 188  ASP A OD2 1 
ATOM   1422 N N   . PHE A 1 189 ? -115.555 14.214 -44.499 1.00 37.04 ? 189  PHE A N   1 
ATOM   1423 C CA  . PHE A 1 189 ? -115.577 15.432 -45.294 1.00 35.85 ? 189  PHE A CA  1 
ATOM   1424 C C   . PHE A 1 189 ? -116.171 15.154 -46.667 1.00 35.80 ? 189  PHE A C   1 
ATOM   1425 O O   . PHE A 1 189 ? -116.120 14.028 -47.163 1.00 36.08 ? 189  PHE A O   1 
ATOM   1426 C CB  . PHE A 1 189 ? -114.172 16.036 -45.414 1.00 35.04 ? 189  PHE A CB  1 
ATOM   1427 C CG  . PHE A 1 189 ? -113.302 15.349 -46.421 1.00 32.98 ? 189  PHE A CG  1 
ATOM   1428 C CD1 . PHE A 1 189 ? -113.276 15.781 -47.743 1.00 31.87 ? 189  PHE A CD1 1 
ATOM   1429 C CD2 . PHE A 1 189 ? -112.515 14.266 -46.052 1.00 31.23 ? 189  PHE A CD2 1 
ATOM   1430 C CE1 . PHE A 1 189 ? -112.471 15.143 -48.683 1.00 31.01 ? 189  PHE A CE1 1 
ATOM   1431 C CE2 . PHE A 1 189 ? -111.706 13.620 -46.986 1.00 30.56 ? 189  PHE A CE2 1 
ATOM   1432 C CZ  . PHE A 1 189 ? -111.684 14.061 -48.304 1.00 30.33 ? 189  PHE A CZ  1 
ATOM   1433 N N   . ALA A 1 190 ? -116.717 16.194 -47.283 1.00 35.75 ? 190  ALA A N   1 
ATOM   1434 C CA  . ALA A 1 190 ? -117.252 16.108 -48.637 1.00 35.56 ? 190  ALA A CA  1 
ATOM   1435 C C   . ALA A 1 190 ? -116.978 17.417 -49.377 1.00 35.82 ? 190  ALA A C   1 
ATOM   1436 O O   . ALA A 1 190 ? -116.573 18.410 -48.776 1.00 35.06 ? 190  ALA A O   1 
ATOM   1437 C CB  . ALA A 1 190 ? -118.735 15.810 -48.606 1.00 35.06 ? 190  ALA A CB  1 
ATOM   1438 N N   . LEU A 1 191 ? -117.217 17.412 -50.685 1.00 36.79 ? 191  LEU A N   1 
ATOM   1439 C CA  . LEU A 1 191 ? -116.810 18.521 -51.531 1.00 37.71 ? 191  LEU A CA  1 
ATOM   1440 C C   . LEU A 1 191 ? -117.745 18.785 -52.703 1.00 38.10 ? 191  LEU A C   1 
ATOM   1441 O O   . LEU A 1 191 ? -118.128 17.867 -53.424 1.00 37.82 ? 191  LEU A O   1 
ATOM   1442 C CB  . LEU A 1 191 ? -115.395 18.271 -52.040 1.00 37.86 ? 191  LEU A CB  1 
ATOM   1443 C CG  . LEU A 1 191 ? -114.670 19.541 -52.415 1.00 38.88 ? 191  LEU A CG  1 
ATOM   1444 C CD1 . LEU A 1 191 ? -113.339 19.574 -51.677 1.00 39.89 ? 191  LEU A CD1 1 
ATOM   1445 C CD2 . LEU A 1 191 ? -114.513 19.594 -53.933 1.00 39.45 ? 191  LEU A CD2 1 
ATOM   1446 N N   . ILE A 1 192 ? -118.084 20.056 -52.893 1.00 39.01 ? 192  ILE A N   1 
ATOM   1447 C CA  . ILE A 1 192 ? -118.935 20.469 -54.000 1.00 40.14 ? 192  ILE A CA  1 
ATOM   1448 C C   . ILE A 1 192 ? -118.126 21.139 -55.116 1.00 41.09 ? 192  ILE A C   1 
ATOM   1449 O O   . ILE A 1 192 ? -117.176 21.859 -54.856 1.00 40.48 ? 192  ILE A O   1 
ATOM   1450 C CB  . ILE A 1 192 ? -120.105 21.368 -53.494 1.00 40.02 ? 192  ILE A CB  1 
ATOM   1451 C CG1 . ILE A 1 192 ? -121.224 20.496 -52.925 1.00 40.01 ? 192  ILE A CG1 1 
ATOM   1452 C CG2 . ILE A 1 192 ? -120.653 22.266 -54.610 1.00 39.84 ? 192  ILE A CG2 1 
ATOM   1453 C CD1 . ILE A 1 192 ? -122.110 21.203 -51.914 1.00 40.09 ? 192  ILE A CD1 1 
ATOM   1454 N N   . HIS A 1 193 ? -118.508 20.874 -56.358 1.00 43.20 ? 193  HIS A N   1 
ATOM   1455 C CA  . HIS A 1 193 ? -117.870 21.488 -57.508 1.00 45.43 ? 193  HIS A CA  1 
ATOM   1456 C C   . HIS A 1 193 ? -118.903 21.890 -58.550 1.00 47.91 ? 193  HIS A C   1 
ATOM   1457 O O   . HIS A 1 193 ? -119.743 21.078 -58.949 1.00 47.88 ? 193  HIS A O   1 
ATOM   1458 C CB  . HIS A 1 193 ? -116.836 20.539 -58.119 1.00 44.77 ? 193  HIS A CB  1 
ATOM   1459 C CG  . HIS A 1 193 ? -116.172 21.085 -59.342 1.00 43.40 ? 193  HIS A CG  1 
ATOM   1460 N ND1 . HIS A 1 193 ? -115.518 22.296 -59.352 1.00 42.39 ? 193  HIS A ND1 1 
ATOM   1461 C CD2 . HIS A 1 193 ? -116.084 20.599 -60.602 1.00 42.72 ? 193  HIS A CD2 1 
ATOM   1462 C CE1 . HIS A 1 193 ? -115.049 22.532 -60.564 1.00 41.95 ? 193  HIS A CE1 1 
ATOM   1463 N NE2 . HIS A 1 193 ? -115.383 21.520 -61.343 1.00 42.09 ? 193  HIS A NE2 1 
ATOM   1464 N N   . LYS A 1 194 ? -118.841 23.150 -58.974 1.00 51.19 ? 194  LYS A N   1 
ATOM   1465 C CA  . LYS A 1 194 ? -119.659 23.645 -60.080 1.00 54.63 ? 194  LYS A CA  1 
ATOM   1466 C C   . LYS A 1 194 ? -118.963 23.366 -61.418 1.00 56.58 ? 194  LYS A C   1 
ATOM   1467 O O   . LYS A 1 194 ? -117.847 23.837 -61.655 1.00 56.47 ? 194  LYS A O   1 
ATOM   1468 C CB  . LYS A 1 194 ? -119.920 25.150 -59.925 1.00 55.20 ? 194  LYS A CB  1 
ATOM   1469 C CG  . LYS A 1 194 ? -121.403 25.548 -59.864 1.00 57.22 ? 194  LYS A CG  1 
ATOM   1470 C CD  . LYS A 1 194 ? -121.584 27.059 -60.069 1.00 59.59 ? 194  LYS A CD  1 
ATOM   1471 C CE  . LYS A 1 194 ? -122.124 27.750 -58.801 1.00 61.09 ? 194  LYS A CE  1 
ATOM   1472 N NZ  . LYS A 1 194 ? -123.583 28.113 -58.896 1.00 62.15 ? 194  LYS A NZ  1 
ATOM   1473 N N   . GLU A 1 195 ? -119.626 22.595 -62.281 1.00 59.25 ? 195  GLU A N   1 
ATOM   1474 C CA  . GLU A 1 195 ? -119.100 22.258 -63.606 1.00 61.85 ? 195  GLU A CA  1 
ATOM   1475 C C   . GLU A 1 195 ? -118.732 23.513 -64.390 1.00 63.14 ? 195  GLU A C   1 
ATOM   1476 O O   . GLU A 1 195 ? -119.554 24.418 -64.538 1.00 63.51 ? 195  GLU A O   1 
ATOM   1477 C CB  . GLU A 1 195 ? -120.117 21.427 -64.393 1.00 62.46 ? 195  GLU A CB  1 
ATOM   1478 C CG  . GLU A 1 195 ? -119.597 20.068 -64.851 1.00 64.45 ? 195  GLU A CG  1 
ATOM   1479 C CD  . GLU A 1 195 ? -119.704 18.999 -63.776 1.00 66.31 ? 195  GLU A CD  1 
ATOM   1480 O OE1 . GLU A 1 195 ? -119.294 19.272 -62.625 1.00 67.14 ? 195  GLU A OE1 1 
ATOM   1481 O OE2 . GLU A 1 195 ? -120.199 17.886 -64.083 1.00 67.02 ? 195  GLU A OE2 1 
ATOM   1482 N N   . ARG A 1 196 ? -117.487 23.572 -64.864 1.00 64.41 ? 196  ARG A N   1 
ATOM   1483 C CA  . ARG A 1 196 ? -116.987 24.743 -65.584 1.00 65.51 ? 196  ARG A CA  1 
ATOM   1484 C C   . ARG A 1 196 ? -116.468 24.334 -66.963 1.00 65.53 ? 196  ARG A C   1 
ATOM   1485 O O   . ARG A 1 196 ? -117.140 23.604 -67.701 1.00 65.48 ? 196  ARG A O   1 
ATOM   1486 C CB  . ARG A 1 196 ? -115.898 25.469 -64.768 1.00 66.14 ? 196  ARG A CB  1 
ATOM   1487 C CG  . ARG A 1 196 ? -116.416 26.187 -63.501 1.00 68.63 ? 196  ARG A CG  1 
ATOM   1488 C CD  . ARG A 1 196 ? -115.368 26.391 -62.374 1.00 72.11 ? 196  ARG A CD  1 
ATOM   1489 N NE  . ARG A 1 196 ? -115.803 25.882 -61.062 1.00 74.35 ? 196  ARG A NE  1 
ATOM   1490 C CZ  . ARG A 1 196 ? -115.217 26.170 -59.890 1.00 75.59 ? 196  ARG A CZ  1 
ATOM   1491 N NH1 . ARG A 1 196 ? -114.163 26.983 -59.842 1.00 76.26 ? 196  ARG A NH1 1 
ATOM   1492 N NH2 . ARG A 1 196 ? -115.690 25.646 -58.757 1.00 75.43 ? 196  ARG A NH2 1 
ATOM   1493 N N   . ASP A 1 203 ? -124.270 25.879 -64.631 1.00 65.60 ? 203  ASP A N   1 
ATOM   1494 C CA  . ASP A 1 203 ? -124.014 24.445 -64.784 1.00 65.26 ? 203  ASP A CA  1 
ATOM   1495 C C   . ASP A 1 203 ? -124.341 23.706 -63.486 1.00 64.83 ? 203  ASP A C   1 
ATOM   1496 O O   . ASP A 1 203 ? -124.565 24.339 -62.448 1.00 65.04 ? 203  ASP A O   1 
ATOM   1497 C CB  . ASP A 1 203 ? -122.560 24.187 -65.213 1.00 65.48 ? 203  ASP A CB  1 
ATOM   1498 C CG  . ASP A 1 203 ? -121.864 25.441 -65.751 1.00 65.41 ? 203  ASP A CG  1 
ATOM   1499 O OD1 . ASP A 1 203 ? -121.588 25.491 -66.971 1.00 65.05 ? 203  ASP A OD1 1 
ATOM   1500 O OD2 . ASP A 1 203 ? -121.549 26.412 -65.018 1.00 65.10 ? 203  ASP A OD2 1 
ATOM   1501 N N   . ARG A 1 204 ? -124.376 22.375 -63.545 1.00 64.06 ? 204  ARG A N   1 
ATOM   1502 C CA  . ARG A 1 204 ? -124.759 21.571 -62.379 1.00 63.20 ? 204  ARG A CA  1 
ATOM   1503 C C   . ARG A 1 204 ? -123.655 21.456 -61.322 1.00 61.59 ? 204  ARG A C   1 
ATOM   1504 O O   . ARG A 1 204 ? -122.461 21.482 -61.638 1.00 61.44 ? 204  ARG A O   1 
ATOM   1505 C CB  . ARG A 1 204 ? -125.263 20.179 -62.795 1.00 63.94 ? 204  ARG A CB  1 
ATOM   1506 C CG  . ARG A 1 204 ? -124.219 19.266 -63.441 1.00 66.24 ? 204  ARG A CG  1 
ATOM   1507 C CD  . ARG A 1 204 ? -124.800 17.979 -64.028 1.00 69.58 ? 204  ARG A CD  1 
ATOM   1508 N NE  . ARG A 1 204 ? -123.776 16.955 -64.255 1.00 72.17 ? 204  ARG A NE  1 
ATOM   1509 C CZ  . ARG A 1 204 ? -123.861 15.988 -65.171 1.00 73.66 ? 204  ARG A CZ  1 
ATOM   1510 N NH1 . ARG A 1 204 ? -124.929 15.898 -65.965 1.00 74.23 ? 204  ARG A NH1 1 
ATOM   1511 N NH2 . ARG A 1 204 ? -122.873 15.108 -65.295 1.00 74.12 ? 204  ARG A NH2 1 
ATOM   1512 N N   . MET A 1 205 ? -124.078 21.340 -60.066 1.00 59.56 ? 205  MET A N   1 
ATOM   1513 C CA  . MET A 1 205 ? -123.171 21.119 -58.952 1.00 57.61 ? 205  MET A CA  1 
ATOM   1514 C C   . MET A 1 205 ? -122.901 19.632 -58.744 1.00 56.01 ? 205  MET A C   1 
ATOM   1515 O O   . MET A 1 205 ? -123.799 18.804 -58.862 1.00 55.87 ? 205  MET A O   1 
ATOM   1516 C CB  . MET A 1 205 ? -123.752 21.721 -57.678 1.00 57.76 ? 205  MET A CB  1 
ATOM   1517 C CG  . MET A 1 205 ? -123.531 23.211 -57.551 1.00 58.28 ? 205  MET A CG  1 
ATOM   1518 S SD  . MET A 1 205 ? -123.634 23.748 -55.847 1.00 59.32 ? 205  MET A SD  1 
ATOM   1519 C CE  . MET A 1 205 ? -122.752 25.347 -55.931 1.00 59.31 ? 205  MET A CE  1 
ATOM   1520 N N   . VAL A 1 206 ? -121.654 19.307 -58.423 1.00 54.12 ? 206  VAL A N   1 
ATOM   1521 C CA  . VAL A 1 206 ? -121.240 17.932 -58.171 1.00 52.14 ? 206  VAL A CA  1 
ATOM   1522 C C   . VAL A 1 206 ? -120.755 17.795 -56.724 1.00 50.90 ? 206  VAL A C   1 
ATOM   1523 O O   . VAL A 1 206 ? -119.998 18.635 -56.234 1.00 50.50 ? 206  VAL A O   1 
ATOM   1524 C CB  . VAL A 1 206 ? -120.159 17.492 -59.205 1.00 52.00 ? 206  VAL A CB  1 
ATOM   1525 C CG1 . VAL A 1 206 ? -119.260 16.392 -58.673 1.00 51.47 ? 206  VAL A CG1 1 
ATOM   1526 C CG2 . VAL A 1 206 ? -120.829 17.047 -60.495 1.00 52.03 ? 206  VAL A CG2 1 
ATOM   1527 N N   . LEU A 1 207 ? -121.203 16.735 -56.053 1.00 49.58 ? 207  LEU A N   1 
ATOM   1528 C CA  . LEU A 1 207 ? -120.840 16.468 -54.667 1.00 48.32 ? 207  LEU A CA  1 
ATOM   1529 C C   . LEU A 1 207 ? -120.062 15.157 -54.513 1.00 47.81 ? 207  LEU A C   1 
ATOM   1530 O O   . LEU A 1 207 ? -120.548 14.096 -54.907 1.00 47.62 ? 207  LEU A O   1 
ATOM   1531 C CB  . LEU A 1 207 ? -122.106 16.412 -53.817 1.00 48.05 ? 207  LEU A CB  1 
ATOM   1532 C CG  . LEU A 1 207 ? -122.048 16.331 -52.286 1.00 47.66 ? 207  LEU A CG  1 
ATOM   1533 C CD1 . LEU A 1 207 ? -123.373 16.806 -51.718 1.00 47.66 ? 207  LEU A CD1 1 
ATOM   1534 C CD2 . LEU A 1 207 ? -121.774 14.923 -51.808 1.00 47.30 ? 207  LEU A CD2 1 
ATOM   1535 N N   . VAL A 1 208 ? -118.871 15.229 -53.918 1.00 47.16 ? 208  VAL A N   1 
ATOM   1536 C CA  . VAL A 1 208 ? -118.092 14.022 -53.632 1.00 46.78 ? 208  VAL A CA  1 
ATOM   1537 C C   . VAL A 1 208 ? -117.865 13.794 -52.129 1.00 47.19 ? 208  VAL A C   1 
ATOM   1538 O O   . VAL A 1 208 ? -117.284 14.634 -51.436 1.00 46.90 ? 208  VAL A O   1 
ATOM   1539 C CB  . VAL A 1 208 ? -116.756 13.942 -54.442 1.00 46.27 ? 208  VAL A CB  1 
ATOM   1540 C CG1 . VAL A 1 208 ? -117.034 13.863 -55.934 1.00 45.50 ? 208  VAL A CG1 1 
ATOM   1541 C CG2 . VAL A 1 208 ? -115.829 15.109 -54.134 1.00 45.75 ? 208  VAL A CG2 1 
ATOM   1542 N N   . GLY A 1 209 ? -118.331 12.646 -51.642 1.00 47.69 ? 209  GLY A N   1 
ATOM   1543 C CA  . GLY A 1 209 ? -118.272 12.322 -50.225 1.00 48.38 ? 209  GLY A CA  1 
ATOM   1544 C C   . GLY A 1 209 ? -119.642 12.083 -49.620 1.00 48.97 ? 209  GLY A C   1 
ATOM   1545 O O   . GLY A 1 209 ? -120.659 12.460 -50.196 1.00 48.54 ? 209  GLY A O   1 
ATOM   1546 N N   . ASP A 1 210 ? -119.665 11.467 -48.442 1.00 50.03 ? 210  ASP A N   1 
ATOM   1547 C CA  . ASP A 1 210 ? -120.915 10.991 -47.850 1.00 51.19 ? 210  ASP A CA  1 
ATOM   1548 C C   . ASP A 1 210 ? -121.616 12.032 -46.975 1.00 51.27 ? 210  ASP A C   1 
ATOM   1549 O O   . ASP A 1 210 ? -121.049 12.494 -45.987 1.00 51.28 ? 210  ASP A O   1 
ATOM   1550 C CB  . ASP A 1 210 ? -120.671 9.699  -47.059 1.00 51.74 ? 210  ASP A CB  1 
ATOM   1551 C CG  . ASP A 1 210 ? -121.968 9.060  -46.557 1.00 53.91 ? 210  ASP A CG  1 
ATOM   1552 O OD1 . ASP A 1 210 ? -123.020 9.200  -47.239 1.00 55.71 ? 210  ASP A OD1 1 
ATOM   1553 O OD2 . ASP A 1 210 ? -122.033 8.406  -45.486 1.00 55.40 ? 210  ASP A OD2 1 
ATOM   1554 N N   . VAL A 1 211 ? -122.848 12.393 -47.337 1.00 51.58 ? 211  VAL A N   1 
ATOM   1555 C CA  . VAL A 1 211 ? -123.649 13.300 -46.500 1.00 52.03 ? 211  VAL A CA  1 
ATOM   1556 C C   . VAL A 1 211 ? -125.030 12.767 -46.088 1.00 52.60 ? 211  VAL A C   1 
ATOM   1557 O O   . VAL A 1 211 ? -125.726 13.406 -45.294 1.00 52.79 ? 211  VAL A O   1 
ATOM   1558 C CB  . VAL A 1 211 ? -123.813 14.718 -47.125 1.00 51.85 ? 211  VAL A CB  1 
ATOM   1559 C CG1 . VAL A 1 211 ? -122.446 15.335 -47.480 1.00 51.60 ? 211  VAL A CG1 1 
ATOM   1560 C CG2 . VAL A 1 211 ? -124.750 14.691 -48.324 1.00 51.41 ? 211  VAL A CG2 1 
ATOM   1561 N N   . LYS A 1 212 ? -125.414 11.606 -46.628 1.00 53.15 ? 212  LYS A N   1 
ATOM   1562 C CA  . LYS A 1 212 ? -126.731 11.005 -46.389 1.00 53.44 ? 212  LYS A CA  1 
ATOM   1563 C C   . LYS A 1 212 ? -126.975 10.734 -44.899 1.00 53.32 ? 212  LYS A C   1 
ATOM   1564 O O   . LYS A 1 212 ? -126.187 10.024 -44.254 1.00 53.31 ? 212  LYS A O   1 
ATOM   1565 C CB  . LYS A 1 212 ? -126.883 9.707  -47.202 1.00 53.85 ? 212  LYS A CB  1 
ATOM   1566 C CG  . LYS A 1 212 ? -128.323 9.183  -47.347 1.00 54.79 ? 212  LYS A CG  1 
ATOM   1567 C CD  . LYS A 1 212 ? -129.033 9.762  -48.581 1.00 56.32 ? 212  LYS A CD  1 
ATOM   1568 C CE  . LYS A 1 212 ? -130.527 9.390  -48.616 1.00 57.70 ? 212  LYS A CE  1 
ATOM   1569 N NZ  . LYS A 1 212 ? -131.415 10.534 -49.029 1.00 58.04 ? 212  LYS A NZ  1 
ATOM   1570 N N   . ASP A 1 213 ? -128.058 11.315 -44.371 1.00 52.94 ? 213  ASP A N   1 
ATOM   1571 C CA  . ASP A 1 213 ? -128.484 11.140 -42.971 1.00 52.82 ? 213  ASP A CA  1 
ATOM   1572 C C   . ASP A 1 213 ? -127.434 11.543 -41.940 1.00 52.30 ? 213  ASP A C   1 
ATOM   1573 O O   . ASP A 1 213 ? -127.264 10.885 -40.908 1.00 52.54 ? 213  ASP A O   1 
ATOM   1574 C CB  . ASP A 1 213 ? -128.965 9.708  -42.701 1.00 53.08 ? 213  ASP A CB  1 
ATOM   1575 C CG  . ASP A 1 213 ? -130.062 9.288  -43.638 1.00 53.88 ? 213  ASP A CG  1 
ATOM   1576 O OD1 . ASP A 1 213 ? -129.896 8.253  -44.316 1.00 55.28 ? 213  ASP A OD1 1 
ATOM   1577 O OD2 . ASP A 1 213 ? -131.117 9.938  -43.776 1.00 54.33 ? 213  ASP A OD2 1 
ATOM   1578 N N   . ARG A 1 214 ? -126.729 12.627 -42.237 1.00 51.40 ? 214  ARG A N   1 
ATOM   1579 C CA  . ARG A 1 214 ? -125.821 13.239 -41.283 1.00 50.41 ? 214  ARG A CA  1 
ATOM   1580 C C   . ARG A 1 214 ? -125.912 14.758 -41.409 1.00 49.37 ? 214  ARG A C   1 
ATOM   1581 O O   . ARG A 1 214 ? -126.397 15.283 -42.418 1.00 49.39 ? 214  ARG A O   1 
ATOM   1582 C CB  . ARG A 1 214 ? -124.376 12.744 -41.473 1.00 50.69 ? 214  ARG A CB  1 
ATOM   1583 C CG  . ARG A 1 214 ? -124.069 12.019 -42.795 1.00 51.13 ? 214  ARG A CG  1 
ATOM   1584 C CD  . ARG A 1 214 ? -122.985 10.925 -42.714 1.00 50.79 ? 214  ARG A CD  1 
ATOM   1585 N NE  . ARG A 1 214 ? -121.743 11.421 -42.133 1.00 50.86 ? 214  ARG A NE  1 
ATOM   1586 C CZ  . ARG A 1 214 ? -120.971 10.738 -41.291 1.00 51.02 ? 214  ARG A CZ  1 
ATOM   1587 N NH1 . ARG A 1 214 ? -121.294 9.499  -40.928 1.00 51.54 ? 214  ARG A NH1 1 
ATOM   1588 N NH2 . ARG A 1 214 ? -119.866 11.294 -40.807 1.00 50.06 ? 214  ARG A NH2 1 
ATOM   1589 N N   . VAL A 1 215 ? -125.465 15.465 -40.381 1.00 47.97 ? 215  VAL A N   1 
ATOM   1590 C CA  . VAL A 1 215 ? -125.454 16.920 -40.440 1.00 46.83 ? 215  VAL A CA  1 
ATOM   1591 C C   . VAL A 1 215 ? -124.313 17.382 -41.344 1.00 45.67 ? 215  VAL A C   1 
ATOM   1592 O O   . VAL A 1 215 ? -123.171 16.955 -41.176 1.00 45.56 ? 215  VAL A O   1 
ATOM   1593 C CB  . VAL A 1 215 ? -125.334 17.560 -39.034 1.00 46.90 ? 215  VAL A CB  1 
ATOM   1594 C CG1 . VAL A 1 215 ? -125.598 19.057 -39.099 1.00 46.61 ? 215  VAL A CG1 1 
ATOM   1595 C CG2 . VAL A 1 215 ? -126.299 16.895 -38.073 1.00 46.67 ? 215  VAL A CG2 1 
ATOM   1596 N N   . ALA A 1 216 ? -124.640 18.236 -42.309 1.00 44.27 ? 216  ALA A N   1 
ATOM   1597 C CA  . ALA A 1 216 ? -123.637 18.831 -43.183 1.00 43.19 ? 216  ALA A CA  1 
ATOM   1598 C C   . ALA A 1 216 ? -123.223 20.224 -42.702 1.00 42.33 ? 216  ALA A C   1 
ATOM   1599 O O   . ALA A 1 216 ? -124.045 21.147 -42.650 1.00 42.33 ? 216  ALA A O   1 
ATOM   1600 C CB  . ALA A 1 216 ? -124.157 18.901 -44.610 1.00 43.28 ? 216  ALA A CB  1 
ATOM   1601 N N   . ILE A 1 217 ? -121.955 20.378 -42.343 1.00 41.14 ? 217  ILE A N   1 
ATOM   1602 C CA  . ILE A 1 217 ? -121.452 21.705 -41.993 1.00 40.19 ? 217  ILE A CA  1 
ATOM   1603 C C   . ILE A 1 217 ? -120.645 22.284 -43.151 1.00 39.84 ? 217  ILE A C   1 
ATOM   1604 O O   . ILE A 1 217 ? -119.537 21.819 -43.438 1.00 39.52 ? 217  ILE A O   1 
ATOM   1605 C CB  . ILE A 1 217 ? -120.626 21.697 -40.660 1.00 39.86 ? 217  ILE A CB  1 
ATOM   1606 C CG1 . ILE A 1 217 ? -121.358 20.928 -39.552 1.00 39.20 ? 217  ILE A CG1 1 
ATOM   1607 C CG2 . ILE A 1 217 ? -120.334 23.118 -40.195 1.00 39.13 ? 217  ILE A CG2 1 
ATOM   1608 C CD1 . ILE A 1 217 ? -120.509 20.696 -38.292 1.00 38.07 ? 217  ILE A CD1 1 
ATOM   1609 N N   . LEU A 1 218 ? -121.215 23.284 -43.824 1.00 39.52 ? 218  LEU A N   1 
ATOM   1610 C CA  . LEU A 1 218 ? -120.479 24.018 -44.849 1.00 39.62 ? 218  LEU A CA  1 
ATOM   1611 C C   . LEU A 1 218 ? -119.465 24.926 -44.192 1.00 40.07 ? 218  LEU A C   1 
ATOM   1612 O O   . LEU A 1 218 ? -119.830 25.814 -43.418 1.00 39.95 ? 218  LEU A O   1 
ATOM   1613 C CB  . LEU A 1 218 ? -121.396 24.857 -45.731 1.00 39.26 ? 218  LEU A CB  1 
ATOM   1614 C CG  . LEU A 1 218 ? -122.020 24.171 -46.944 1.00 38.94 ? 218  LEU A CG  1 
ATOM   1615 C CD1 . LEU A 1 218 ? -123.114 25.068 -47.527 1.00 39.06 ? 218  LEU A CD1 1 
ATOM   1616 C CD2 . LEU A 1 218 ? -120.985 23.799 -48.006 1.00 38.22 ? 218  LEU A CD2 1 
ATOM   1617 N N   . VAL A 1 219 ? -118.193 24.680 -44.484 1.00 40.60 ? 219  VAL A N   1 
ATOM   1618 C CA  . VAL A 1 219 ? -117.124 25.542 -44.012 1.00 41.36 ? 219  VAL A CA  1 
ATOM   1619 C C   . VAL A 1 219 ? -116.407 26.214 -45.177 1.00 42.31 ? 219  VAL A C   1 
ATOM   1620 O O   . VAL A 1 219 ? -116.004 25.559 -46.140 1.00 42.19 ? 219  VAL A O   1 
ATOM   1621 C CB  . VAL A 1 219 ? -116.111 24.788 -43.136 1.00 41.14 ? 219  VAL A CB  1 
ATOM   1622 C CG1 . VAL A 1 219 ? -114.863 25.634 -42.919 1.00 40.78 ? 219  VAL A CG1 1 
ATOM   1623 C CG2 . VAL A 1 219 ? -116.735 24.409 -41.811 1.00 40.77 ? 219  VAL A CG2 1 
ATOM   1624 N N   . ASP A 1 220 ? -116.268 27.531 -45.065 1.00 43.54 ? 220  ASP A N   1 
ATOM   1625 C CA  . ASP A 1 220 ? -115.518 28.341 -46.007 1.00 44.93 ? 220  ASP A CA  1 
ATOM   1626 C C   . ASP A 1 220 ? -114.857 29.529 -45.294 1.00 45.73 ? 220  ASP A C   1 
ATOM   1627 O O   . ASP A 1 220 ? -115.250 29.892 -44.189 1.00 45.65 ? 220  ASP A O   1 
ATOM   1628 C CB  . ASP A 1 220 ? -116.450 28.815 -47.109 1.00 45.30 ? 220  ASP A CB  1 
ATOM   1629 C CG  . ASP A 1 220 ? -115.722 29.146 -48.380 1.00 46.48 ? 220  ASP A CG  1 
ATOM   1630 O OD1 . ASP A 1 220 ? -114.575 28.672 -48.577 1.00 47.17 ? 220  ASP A OD1 1 
ATOM   1631 O OD2 . ASP A 1 220 ? -116.228 29.884 -49.245 1.00 47.74 ? 220  ASP A OD2 1 
ATOM   1632 N N   . ASP A 1 221 ? -113.839 30.128 -45.907 1.00 46.99 ? 221  ASP A N   1 
ATOM   1633 C CA  . ASP A 1 221 ? -113.132 31.231 -45.247 1.00 48.22 ? 221  ASP A CA  1 
ATOM   1634 C C   . ASP A 1 221 ? -113.892 32.557 -45.322 1.00 49.28 ? 221  ASP A C   1 
ATOM   1635 O O   . ASP A 1 221 ? -113.818 33.369 -44.400 1.00 49.51 ? 221  ASP A O   1 
ATOM   1636 C CB  . ASP A 1 221 ? -111.707 31.380 -45.776 1.00 48.01 ? 221  ASP A CB  1 
ATOM   1637 C CG  . ASP A 1 221 ? -111.664 31.783 -47.232 1.00 48.08 ? 221  ASP A CG  1 
ATOM   1638 O OD1 . ASP A 1 221 ? -110.800 32.610 -47.581 1.00 47.50 ? 221  ASP A OD1 1 
ATOM   1639 O OD2 . ASP A 1 221 ? -112.446 31.329 -48.098 1.00 48.60 ? 221  ASP A OD2 1 
ATOM   1640 N N   . MET A 1 222 ? -114.618 32.768 -46.418 1.00 50.55 ? 222  MET A N   1 
ATOM   1641 C CA  . MET A 1 222 ? -115.430 33.972 -46.588 1.00 51.91 ? 222  MET A CA  1 
ATOM   1642 C C   . MET A 1 222 ? -116.643 33.741 -47.479 1.00 52.25 ? 222  MET A C   1 
ATOM   1643 O O   . MET A 1 222 ? -116.585 32.953 -48.417 1.00 52.36 ? 222  MET A O   1 
ATOM   1644 C CB  . MET A 1 222 ? -114.595 35.157 -47.113 1.00 52.45 ? 222  MET A CB  1 
ATOM   1645 C CG  . MET A 1 222 ? -113.754 34.914 -48.377 1.00 53.94 ? 222  MET A CG  1 
ATOM   1646 S SD  . MET A 1 222 ? -112.825 36.436 -48.794 1.00 56.79 ? 222  MET A SD  1 
ATOM   1647 C CE  . MET A 1 222 ? -111.132 35.847 -48.910 1.00 56.19 ? 222  MET A CE  1 
ATOM   1648 N N   . ALA A 1 223 ? -117.740 34.427 -47.167 1.00 52.73 ? 223  ALA A N   1 
ATOM   1649 C CA  . ALA A 1 223 ? -118.937 34.408 -48.006 1.00 53.05 ? 223  ALA A CA  1 
ATOM   1650 C C   . ALA A 1 223 ? -119.441 35.817 -48.258 1.00 53.32 ? 223  ALA A C   1 
ATOM   1651 O O   . ALA A 1 223 ? -119.790 36.541 -47.326 1.00 53.34 ? 223  ALA A O   1 
ATOM   1652 C CB  . ALA A 1 223 ? -120.019 33.567 -47.386 1.00 53.04 ? 223  ALA A CB  1 
ATOM   1653 N N   . ASP A 1 224 ? -119.471 36.187 -49.533 1.00 53.70 ? 224  ASP A N   1 
ATOM   1654 C CA  . ASP A 1 224 ? -119.914 37.500 -49.972 1.00 54.06 ? 224  ASP A CA  1 
ATOM   1655 C C   . ASP A 1 224 ? -121.426 37.536 -50.264 1.00 54.08 ? 224  ASP A C   1 
ATOM   1656 O O   . ASP A 1 224 ? -122.229 37.775 -49.361 1.00 54.38 ? 224  ASP A O   1 
ATOM   1657 C CB  . ASP A 1 224 ? -119.106 37.938 -51.196 1.00 54.26 ? 224  ASP A CB  1 
ATOM   1658 C CG  . ASP A 1 224 ? -119.342 39.379 -51.556 1.00 54.97 ? 224  ASP A CG  1 
ATOM   1659 O OD1 . ASP A 1 224 ? -120.029 40.078 -50.785 1.00 54.64 ? 224  ASP A OD1 1 
ATOM   1660 O OD2 . ASP A 1 224 ? -118.886 39.899 -52.596 1.00 56.52 ? 224  ASP A OD2 1 
ATOM   1661 N N   . THR A 1 225 ? -121.816 37.305 -51.514 1.00 53.75 ? 225  THR A N   1 
ATOM   1662 C CA  . THR A 1 225 ? -123.232 37.329 -51.875 1.00 53.49 ? 225  THR A CA  1 
ATOM   1663 C C   . THR A 1 225 ? -123.958 36.071 -51.371 1.00 53.17 ? 225  THR A C   1 
ATOM   1664 O O   . THR A 1 225 ? -125.193 36.032 -51.312 1.00 53.22 ? 225  THR A O   1 
ATOM   1665 C CB  . THR A 1 225 ? -123.416 37.509 -53.395 1.00 53.60 ? 225  THR A CB  1 
ATOM   1666 O OG1 . THR A 1 225 ? -122.985 36.327 -54.079 1.00 53.70 ? 225  THR A OG1 1 
ATOM   1667 C CG2 . THR A 1 225 ? -122.486 38.603 -53.938 1.00 53.82 ? 225  THR A CG2 1 
ATOM   1668 N N   . CYS A 1 226 ? -123.173 35.064 -50.982 1.00 52.56 ? 226  CYS A N   1 
ATOM   1669 C CA  . CYS A 1 226 ? -123.674 33.783 -50.487 1.00 51.97 ? 226  CYS A CA  1 
ATOM   1670 C C   . CYS A 1 226 ? -124.347 32.970 -51.584 1.00 51.69 ? 226  CYS A C   1 
ATOM   1671 O O   . CYS A 1 226 ? -125.123 32.067 -51.295 1.00 51.35 ? 226  CYS A O   1 
ATOM   1672 C CB  . CYS A 1 226 ? -124.624 33.970 -49.296 1.00 51.89 ? 226  CYS A CB  1 
ATOM   1673 S SG  . CYS A 1 226 ? -123.844 34.652 -47.821 1.00 51.51 ? 226  CYS A SG  1 
ATOM   1674 N N   . GLY A 1 227 ? -124.035 33.290 -52.839 1.00 51.60 ? 227  GLY A N   1 
ATOM   1675 C CA  . GLY A 1 227 ? -124.594 32.584 -53.978 1.00 51.66 ? 227  GLY A CA  1 
ATOM   1676 C C   . GLY A 1 227 ? -124.162 31.132 -54.022 1.00 51.68 ? 227  GLY A C   1 
ATOM   1677 O O   . GLY A 1 227 ? -124.954 30.237 -54.339 1.00 51.82 ? 227  GLY A O   1 
ATOM   1678 N N   . THR A 1 228 ? -122.899 30.911 -53.678 1.00 51.70 ? 228  THR A N   1 
ATOM   1679 C CA  . THR A 1 228 ? -122.277 29.599 -53.756 1.00 51.71 ? 228  THR A CA  1 
ATOM   1680 C C   . THR A 1 228 ? -122.683 28.716 -52.577 1.00 51.79 ? 228  THR A C   1 
ATOM   1681 O O   . THR A 1 228 ? -123.104 27.579 -52.782 1.00 51.87 ? 228  THR A O   1 
ATOM   1682 C CB  . THR A 1 228 ? -120.742 29.765 -53.880 1.00 51.69 ? 228  THR A CB  1 
ATOM   1683 O OG1 . THR A 1 228 ? -120.421 30.060 -55.246 1.00 52.01 ? 228  THR A OG1 1 
ATOM   1684 C CG2 . THR A 1 228 ? -120.009 28.464 -53.622 1.00 51.32 ? 228  THR A CG2 1 
ATOM   1685 N N   . ILE A 1 229 ? -122.578 29.242 -51.356 1.00 51.87 ? 229  ILE A N   1 
ATOM   1686 C CA  . ILE A 1 229 ? -122.975 28.486 -50.165 1.00 52.11 ? 229  ILE A CA  1 
ATOM   1687 C C   . ILE A 1 229 ? -124.487 28.245 -50.089 1.00 52.46 ? 229  ILE A C   1 
ATOM   1688 O O   . ILE A 1 229 ? -124.928 27.321 -49.406 1.00 52.37 ? 229  ILE A O   1 
ATOM   1689 C CB  . ILE A 1 229 ? -122.448 29.132 -48.847 1.00 52.02 ? 229  ILE A CB  1 
ATOM   1690 C CG1 . ILE A 1 229 ? -123.063 30.517 -48.626 1.00 51.75 ? 229  ILE A CG1 1 
ATOM   1691 C CG2 . ILE A 1 229 ? -120.903 29.146 -48.815 1.00 51.94 ? 229  ILE A CG2 1 
ATOM   1692 C CD1 . ILE A 1 229 ? -123.450 30.783 -47.187 1.00 51.34 ? 229  ILE A CD1 1 
ATOM   1693 N N   . CYS A 1 230 ? -125.266 29.068 -50.795 1.00 52.91 ? 230  CYS A N   1 
ATOM   1694 C CA  . CYS A 1 230 ? -126.713 28.883 -50.872 1.00 53.36 ? 230  CYS A CA  1 
ATOM   1695 C C   . CYS A 1 230 ? -127.064 27.742 -51.816 1.00 53.71 ? 230  CYS A C   1 
ATOM   1696 O O   . CYS A 1 230 ? -127.804 26.825 -51.437 1.00 53.72 ? 230  CYS A O   1 
ATOM   1697 C CB  . CYS A 1 230 ? -127.426 30.175 -51.281 1.00 53.36 ? 230  CYS A CB  1 
ATOM   1698 S SG  . CYS A 1 230 ? -127.853 31.216 -49.864 1.00 53.17 ? 230  CYS A SG  1 
ATOM   1699 N N   . HIS A 1 231 ? -126.520 27.791 -53.031 1.00 54.15 ? 231  HIS A N   1 
ATOM   1700 C CA  . HIS A 1 231 ? -126.667 26.682 -53.971 1.00 54.86 ? 231  HIS A CA  1 
ATOM   1701 C C   . HIS A 1 231 ? -126.050 25.396 -53.423 1.00 54.60 ? 231  HIS A C   1 
ATOM   1702 O O   . HIS A 1 231 ? -126.556 24.304 -53.687 1.00 54.60 ? 231  HIS A O   1 
ATOM   1703 C CB  . HIS A 1 231 ? -126.042 27.019 -55.323 1.00 55.49 ? 231  HIS A CB  1 
ATOM   1704 C CG  . HIS A 1 231 ? -126.881 27.926 -56.167 1.00 57.57 ? 231  HIS A CG  1 
ATOM   1705 N ND1 . HIS A 1 231 ? -126.334 28.856 -57.024 1.00 59.05 ? 231  HIS A ND1 1 
ATOM   1706 C CD2 . HIS A 1 231 ? -128.226 28.048 -56.284 1.00 58.91 ? 231  HIS A CD2 1 
ATOM   1707 C CE1 . HIS A 1 231 ? -127.306 29.513 -57.634 1.00 59.72 ? 231  HIS A CE1 1 
ATOM   1708 N NE2 . HIS A 1 231 ? -128.464 29.042 -57.203 1.00 59.65 ? 231  HIS A NE2 1 
ATOM   1709 N N   . ALA A 1 232 ? -124.960 25.534 -52.667 1.00 54.29 ? 232  ALA A N   1 
ATOM   1710 C CA  . ALA A 1 232 ? -124.300 24.391 -52.050 1.00 53.98 ? 232  ALA A CA  1 
ATOM   1711 C C   . ALA A 1 232 ? -125.244 23.733 -51.071 1.00 53.98 ? 232  ALA A C   1 
ATOM   1712 O O   . ALA A 1 232 ? -125.329 22.505 -51.015 1.00 53.91 ? 232  ALA A O   1 
ATOM   1713 C CB  . ALA A 1 232 ? -123.035 24.812 -51.349 1.00 53.85 ? 232  ALA A CB  1 
ATOM   1714 N N   . ALA A 1 233 ? -125.964 24.559 -50.317 1.00 54.01 ? 233  ALA A N   1 
ATOM   1715 C CA  . ALA A 1 233 ? -126.878 24.080 -49.290 1.00 54.20 ? 233  ALA A CA  1 
ATOM   1716 C C   . ALA A 1 233 ? -128.029 23.263 -49.883 1.00 54.31 ? 233  ALA A C   1 
ATOM   1717 O O   . ALA A 1 233 ? -128.422 22.241 -49.310 1.00 54.17 ? 233  ALA A O   1 
ATOM   1718 C CB  . ALA A 1 233 ? -127.405 25.245 -48.461 1.00 54.16 ? 233  ALA A CB  1 
ATOM   1719 N N   . ASP A 1 234 ? -128.545 23.711 -51.029 1.00 54.49 ? 234  ASP A N   1 
ATOM   1720 C CA  . ASP A 1 234 ? -129.605 23.005 -51.749 1.00 54.84 ? 234  ASP A CA  1 
ATOM   1721 C C   . ASP A 1 234 ? -129.170 21.591 -52.102 1.00 54.62 ? 234  ASP A C   1 
ATOM   1722 O O   . ASP A 1 234 ? -129.902 20.625 -51.863 1.00 54.67 ? 234  ASP A O   1 
ATOM   1723 C CB  . ASP A 1 234 ? -129.975 23.746 -53.038 1.00 55.29 ? 234  ASP A CB  1 
ATOM   1724 C CG  . ASP A 1 234 ? -130.726 25.042 -52.781 1.00 56.38 ? 234  ASP A CG  1 
ATOM   1725 O OD1 . ASP A 1 234 ? -131.642 25.053 -51.924 1.00 57.54 ? 234  ASP A OD1 1 
ATOM   1726 O OD2 . ASP A 1 234 ? -130.474 26.098 -53.396 1.00 56.91 ? 234  ASP A OD2 1 
ATOM   1727 N N   . LYS A 1 235 ? -127.970 21.490 -52.668 1.00 54.22 ? 235  LYS A N   1 
ATOM   1728 C CA  . LYS A 1 235 ? -127.405 20.224 -53.104 1.00 53.86 ? 235  LYS A CA  1 
ATOM   1729 C C   . LYS A 1 235 ? -127.245 19.285 -51.926 1.00 53.38 ? 235  LYS A C   1 
ATOM   1730 O O   . LYS A 1 235 ? -127.521 18.090 -52.029 1.00 53.46 ? 235  LYS A O   1 
ATOM   1731 C CB  . LYS A 1 235 ? -126.053 20.443 -53.789 1.00 54.10 ? 235  LYS A CB  1 
ATOM   1732 C CG  . LYS A 1 235 ? -125.972 19.896 -55.213 1.00 54.43 ? 235  LYS A CG  1 
ATOM   1733 C CD  . LYS A 1 235 ? -125.377 18.486 -55.265 1.00 54.42 ? 235  LYS A CD  1 
ATOM   1734 C CE  . LYS A 1 235 ? -125.713 17.807 -56.592 1.00 54.40 ? 235  LYS A CE  1 
ATOM   1735 N NZ  . LYS A 1 235 ? -125.452 16.348 -56.566 1.00 54.55 ? 235  LYS A NZ  1 
ATOM   1736 N N   . LEU A 1 236 ? -126.816 19.834 -50.797 1.00 52.80 ? 236  LEU A N   1 
ATOM   1737 C CA  . LEU A 1 236 ? -126.650 19.034 -49.596 1.00 52.36 ? 236  LEU A CA  1 
ATOM   1738 C C   . LEU A 1 236 ? -127.996 18.490 -49.103 1.00 52.19 ? 236  LEU A C   1 
ATOM   1739 O O   . LEU A 1 236 ? -128.072 17.379 -48.565 1.00 52.19 ? 236  LEU A O   1 
ATOM   1740 C CB  . LEU A 1 236 ? -125.941 19.840 -48.511 1.00 52.21 ? 236  LEU A CB  1 
ATOM   1741 C CG  . LEU A 1 236 ? -124.430 20.000 -48.675 1.00 51.52 ? 236  LEU A CG  1 
ATOM   1742 C CD1 . LEU A 1 236 ? -123.919 21.033 -47.698 1.00 50.65 ? 236  LEU A CD1 1 
ATOM   1743 C CD2 . LEU A 1 236 ? -123.714 18.667 -48.488 1.00 50.76 ? 236  LEU A CD2 1 
ATOM   1744 N N   . LEU A 1 237 ? -129.050 19.277 -49.310 1.00 51.79 ? 237  LEU A N   1 
ATOM   1745 C CA  . LEU A 1 237 ? -130.405 18.848 -49.010 1.00 51.55 ? 237  LEU A CA  1 
ATOM   1746 C C   . LEU A 1 237 ? -130.858 17.777 -50.003 1.00 51.61 ? 237  LEU A C   1 
ATOM   1747 O O   . LEU A 1 237 ? -131.355 16.725 -49.596 1.00 51.78 ? 237  LEU A O   1 
ATOM   1748 C CB  . LEU A 1 237 ? -131.360 20.042 -49.037 1.00 51.36 ? 237  LEU A CB  1 
ATOM   1749 C CG  . LEU A 1 237 ? -131.675 20.793 -47.738 1.00 50.66 ? 237  LEU A CG  1 
ATOM   1750 C CD1 . LEU A 1 237 ? -133.066 21.413 -47.856 1.00 51.38 ? 237  LEU A CD1 1 
ATOM   1751 C CD2 . LEU A 1 237 ? -131.586 19.945 -46.485 1.00 49.16 ? 237  LEU A CD2 1 
ATOM   1752 N N   . SER A 1 238 ? -130.672 18.048 -51.296 1.00 51.49 ? 238  SER A N   1 
ATOM   1753 C CA  . SER A 1 238 ? -130.949 17.079 -52.361 1.00 51.38 ? 238  SER A CA  1 
ATOM   1754 C C   . SER A 1 238 ? -130.272 15.724 -52.125 1.00 51.06 ? 238  SER A C   1 
ATOM   1755 O O   . SER A 1 238 ? -130.824 14.674 -52.458 1.00 51.02 ? 238  SER A O   1 
ATOM   1756 C CB  . SER A 1 238 ? -130.507 17.640 -53.717 1.00 51.58 ? 238  SER A CB  1 
ATOM   1757 O OG  . SER A 1 238 ? -131.526 18.439 -54.309 1.00 52.13 ? 238  SER A OG  1 
ATOM   1758 N N   . ALA A 1 239 ? -129.076 15.760 -51.550 1.00 50.70 ? 239  ALA A N   1 
ATOM   1759 C CA  . ALA A 1 239 ? -128.306 14.552 -51.286 1.00 50.42 ? 239  ALA A CA  1 
ATOM   1760 C C   . ALA A 1 239 ? -128.601 13.981 -49.898 1.00 50.51 ? 239  ALA A C   1 
ATOM   1761 O O   . ALA A 1 239 ? -127.903 13.079 -49.429 1.00 50.30 ? 239  ALA A O   1 
ATOM   1762 C CB  . ALA A 1 239 ? -126.817 14.832 -51.452 1.00 50.20 ? 239  ALA A CB  1 
ATOM   1763 N N   . GLY A 1 240 ? -129.620 14.527 -49.237 1.00 50.71 ? 240  GLY A N   1 
ATOM   1764 C CA  . GLY A 1 240 ? -130.140 13.948 -48.011 1.00 51.20 ? 240  GLY A CA  1 
ATOM   1765 C C   . GLY A 1 240 ? -129.353 14.177 -46.732 1.00 51.74 ? 240  GLY A C   1 
ATOM   1766 O O   . GLY A 1 240 ? -129.255 13.268 -45.887 1.00 51.74 ? 240  GLY A O   1 
ATOM   1767 N N   . ALA A 1 241 ? -128.789 15.375 -46.579 1.00 52.05 ? 241  ALA A N   1 
ATOM   1768 C CA  . ALA A 1 241 ? -128.268 15.802 -45.284 1.00 52.55 ? 241  ALA A CA  1 
ATOM   1769 C C   . ALA A 1 241 ? -129.444 16.033 -44.341 1.00 52.96 ? 241  ALA A C   1 
ATOM   1770 O O   . ALA A 1 241 ? -130.516 16.447 -44.779 1.00 52.80 ? 241  ALA A O   1 
ATOM   1771 C CB  . ALA A 1 241 ? -127.435 17.072 -45.420 1.00 52.43 ? 241  ALA A CB  1 
ATOM   1772 N N   . THR A 1 242 ? -129.240 15.741 -43.057 1.00 53.78 ? 242  THR A N   1 
ATOM   1773 C CA  . THR A 1 242 ? -130.242 15.986 -42.018 1.00 54.61 ? 242  THR A CA  1 
ATOM   1774 C C   . THR A 1 242 ? -130.584 17.475 -41.995 1.00 54.98 ? 242  THR A C   1 
ATOM   1775 O O   . THR A 1 242 ? -131.712 17.867 -42.287 1.00 55.18 ? 242  THR A O   1 
ATOM   1776 C CB  . THR A 1 242 ? -129.708 15.516 -40.643 1.00 54.79 ? 242  THR A CB  1 
ATOM   1777 O OG1 . THR A 1 242 ? -129.634 14.084 -40.621 1.00 55.51 ? 242  THR A OG1 1 
ATOM   1778 C CG2 . THR A 1 242 ? -130.700 15.829 -39.522 1.00 55.17 ? 242  THR A CG2 1 
ATOM   1779 N N   . ARG A 1 243 ? -129.591 18.292 -41.660 1.00 55.33 ? 243  ARG A N   1 
ATOM   1780 C CA  . ARG A 1 243 ? -129.697 19.743 -41.716 1.00 55.59 ? 243  ARG A CA  1 
ATOM   1781 C C   . ARG A 1 243 ? -128.308 20.319 -42.029 1.00 55.42 ? 243  ARG A C   1 
ATOM   1782 O O   . ARG A 1 243 ? -127.280 19.697 -41.715 1.00 55.57 ? 243  ARG A O   1 
ATOM   1783 C CB  . ARG A 1 243 ? -130.267 20.310 -40.407 1.00 55.90 ? 243  ARG A CB  1 
ATOM   1784 C CG  . ARG A 1 243 ? -129.648 19.760 -39.116 1.00 57.00 ? 243  ARG A CG  1 
ATOM   1785 C CD  . ARG A 1 243 ? -130.651 19.569 -37.957 1.00 59.13 ? 243  ARG A CD  1 
ATOM   1786 N NE  . ARG A 1 243 ? -130.127 19.992 -36.651 1.00 60.57 ? 243  ARG A NE  1 
ATOM   1787 C CZ  . ARG A 1 243 ? -129.115 19.399 -36.013 1.00 61.56 ? 243  ARG A CZ  1 
ATOM   1788 N NH1 . ARG A 1 243 ? -128.509 18.356 -36.556 1.00 62.26 ? 243  ARG A NH1 1 
ATOM   1789 N NH2 . ARG A 1 243 ? -128.701 19.838 -34.831 1.00 61.74 ? 243  ARG A NH2 1 
ATOM   1790 N N   . VAL A 1 244 ? -128.274 21.489 -42.662 1.00 54.85 ? 244  VAL A N   1 
ATOM   1791 C CA  . VAL A 1 244 ? -127.001 22.082 -43.070 1.00 54.37 ? 244  VAL A CA  1 
ATOM   1792 C C   . VAL A 1 244 ? -126.698 23.407 -42.374 1.00 53.65 ? 244  VAL A C   1 
ATOM   1793 O O   . VAL A 1 244 ? -127.523 24.322 -42.373 1.00 53.71 ? 244  VAL A O   1 
ATOM   1794 C CB  . VAL A 1 244 ? -126.872 22.197 -44.622 1.00 54.62 ? 244  VAL A CB  1 
ATOM   1795 C CG1 . VAL A 1 244 ? -128.175 22.631 -45.253 1.00 55.03 ? 244  VAL A CG1 1 
ATOM   1796 C CG2 . VAL A 1 244 ? -125.721 23.119 -45.035 1.00 54.61 ? 244  VAL A CG2 1 
ATOM   1797 N N   . TYR A 1 245 ? -125.509 23.480 -41.776 1.00 52.70 ? 245  TYR A N   1 
ATOM   1798 C CA  . TYR A 1 245 ? -124.997 24.711 -41.173 1.00 51.83 ? 245  TYR A CA  1 
ATOM   1799 C C   . TYR A 1 245 ? -124.040 25.416 -42.142 1.00 50.81 ? 245  TYR A C   1 
ATOM   1800 O O   . TYR A 1 245 ? -123.632 24.837 -43.157 1.00 50.73 ? 245  TYR A O   1 
ATOM   1801 C CB  . TYR A 1 245 ? -124.278 24.419 -39.843 1.00 52.03 ? 245  TYR A CB  1 
ATOM   1802 C CG  . TYR A 1 245 ? -125.176 23.933 -38.718 1.00 52.65 ? 245  TYR A CG  1 
ATOM   1803 C CD1 . TYR A 1 245 ? -125.833 22.700 -38.802 1.00 52.68 ? 245  TYR A CD1 1 
ATOM   1804 C CD2 . TYR A 1 245 ? -125.356 24.698 -37.562 1.00 52.83 ? 245  TYR A CD2 1 
ATOM   1805 C CE1 . TYR A 1 245 ? -126.647 22.245 -37.779 1.00 53.02 ? 245  TYR A CE1 1 
ATOM   1806 C CE2 . TYR A 1 245 ? -126.174 24.251 -36.523 1.00 53.06 ? 245  TYR A CE2 1 
ATOM   1807 C CZ  . TYR A 1 245 ? -126.815 23.018 -36.640 1.00 53.56 ? 245  TYR A CZ  1 
ATOM   1808 O OH  . TYR A 1 245 ? -127.641 22.554 -35.635 1.00 53.96 ? 245  TYR A OH  1 
ATOM   1809 N N   . ALA A 1 246 ? -123.693 26.663 -41.825 1.00 49.38 ? 246  ALA A N   1 
ATOM   1810 C CA  . ALA A 1 246 ? -122.718 27.427 -42.595 1.00 48.15 ? 246  ALA A CA  1 
ATOM   1811 C C   . ALA A 1 246 ? -121.767 28.165 -41.660 1.00 47.25 ? 246  ALA A C   1 
ATOM   1812 O O   . ALA A 1 246 ? -122.187 29.019 -40.881 1.00 46.95 ? 246  ALA A O   1 
ATOM   1813 C CB  . ALA A 1 246 ? -123.414 28.402 -43.540 1.00 48.11 ? 246  ALA A CB  1 
ATOM   1814 N N   . ILE A 1 247 ? -120.488 27.807 -41.731 1.00 46.23 ? 247  ILE A N   1 
ATOM   1815 C CA  . ILE A 1 247 ? -119.453 28.466 -40.950 1.00 45.30 ? 247  ILE A CA  1 
ATOM   1816 C C   . ILE A 1 247 ? -118.466 29.193 -41.861 1.00 45.13 ? 247  ILE A C   1 
ATOM   1817 O O   . ILE A 1 247 ? -117.855 28.601 -42.753 1.00 44.58 ? 247  ILE A O   1 
ATOM   1818 C CB  . ILE A 1 247 ? -118.737 27.464 -40.027 1.00 45.14 ? 247  ILE A CB  1 
ATOM   1819 C CG1 . ILE A 1 247 ? -119.780 26.617 -39.273 1.00 44.87 ? 247  ILE A CG1 1 
ATOM   1820 C CG2 . ILE A 1 247 ? -117.782 28.205 -39.085 1.00 44.40 ? 247  ILE A CG2 1 
ATOM   1821 C CD1 . ILE A 1 247 ? -119.302 26.005 -37.969 1.00 44.46 ? 247  ILE A CD1 1 
ATOM   1822 N N   . LEU A 1 248 ? -118.349 30.495 -41.635 1.00 45.22 ? 248  LEU A N   1 
ATOM   1823 C CA  . LEU A 1 248 ? -117.471 31.369 -42.412 1.00 45.30 ? 248  LEU A CA  1 
ATOM   1824 C C   . LEU A 1 248 ? -116.690 32.214 -41.438 1.00 45.32 ? 248  LEU A C   1 
ATOM   1825 O O   . LEU A 1 248 ? -117.267 32.745 -40.494 1.00 45.49 ? 248  LEU A O   1 
ATOM   1826 C CB  . LEU A 1 248 ? -118.295 32.282 -43.312 1.00 45.22 ? 248  LEU A CB  1 
ATOM   1827 C CG  . LEU A 1 248 ? -119.584 31.667 -43.847 1.00 45.73 ? 248  LEU A CG  1 
ATOM   1828 C CD1 . LEU A 1 248 ? -120.672 32.700 -43.939 1.00 46.11 ? 248  LEU A CD1 1 
ATOM   1829 C CD2 . LEU A 1 248 ? -119.327 31.016 -45.192 1.00 46.50 ? 248  LEU A CD2 1 
ATOM   1830 N N   . THR A 1 249 ? -115.385 32.343 -41.631 1.00 45.30 ? 249  THR A N   1 
ATOM   1831 C CA  . THR A 1 249 ? -114.640 33.189 -40.708 1.00 45.47 ? 249  THR A CA  1 
ATOM   1832 C C   . THR A 1 249 ? -114.882 34.657 -41.051 1.00 45.64 ? 249  THR A C   1 
ATOM   1833 O O   . THR A 1 249 ? -115.149 35.476 -40.162 1.00 45.52 ? 249  THR A O   1 
ATOM   1834 C CB  . THR A 1 249 ? -113.134 32.794 -40.583 1.00 45.35 ? 249  THR A CB  1 
ATOM   1835 O OG1 . THR A 1 249 ? -112.299 33.962 -40.626 1.00 45.23 ? 249  THR A OG1 1 
ATOM   1836 C CG2 . THR A 1 249 ? -112.680 31.966 -41.754 1.00 45.71 ? 249  THR A CG2 1 
ATOM   1837 N N   . HIS A 1 250 ? -114.842 34.978 -42.340 1.00 45.83 ? 250  HIS A N   1 
ATOM   1838 C CA  . HIS A 1 250 ? -115.124 36.337 -42.780 1.00 46.08 ? 250  HIS A CA  1 
ATOM   1839 C C   . HIS A 1 250 ? -116.494 36.373 -43.429 1.00 46.78 ? 250  HIS A C   1 
ATOM   1840 O O   . HIS A 1 250 ? -116.723 35.744 -44.472 1.00 46.50 ? 250  HIS A O   1 
ATOM   1841 C CB  . HIS A 1 250 ? -114.042 36.859 -43.740 1.00 45.64 ? 250  HIS A CB  1 
ATOM   1842 C CG  . HIS A 1 250 ? -112.647 36.629 -43.256 1.00 44.49 ? 250  HIS A CG  1 
ATOM   1843 N ND1 . HIS A 1 250 ? -112.139 37.248 -42.132 1.00 43.82 ? 250  HIS A ND1 1 
ATOM   1844 C CD2 . HIS A 1 250 ? -111.658 35.833 -43.728 1.00 43.41 ? 250  HIS A CD2 1 
ATOM   1845 C CE1 . HIS A 1 250 ? -110.895 36.845 -41.938 1.00 43.03 ? 250  HIS A CE1 1 
ATOM   1846 N NE2 . HIS A 1 250 ? -110.578 35.990 -42.893 1.00 42.91 ? 250  HIS A NE2 1 
ATOM   1847 N N   . GLY A 1 251 ? -117.399 37.109 -42.792 1.00 47.73 ? 251  GLY A N   1 
ATOM   1848 C CA  . GLY A 1 251 ? -118.773 37.211 -43.246 1.00 49.31 ? 251  GLY A CA  1 
ATOM   1849 C C   . GLY A 1 251 ? -119.039 38.553 -43.876 1.00 50.57 ? 251  GLY A C   1 
ATOM   1850 O O   . GLY A 1 251 ? -119.573 39.459 -43.227 1.00 50.46 ? 251  GLY A O   1 
ATOM   1851 N N   . ILE A 1 252 ? -118.662 38.678 -45.145 1.00 52.00 ? 252  ILE A N   1 
ATOM   1852 C CA  . ILE A 1 252 ? -118.797 39.938 -45.878 1.00 53.52 ? 252  ILE A CA  1 
ATOM   1853 C C   . ILE A 1 252 ? -120.269 40.306 -46.126 1.00 54.72 ? 252  ILE A C   1 
ATOM   1854 O O   . ILE A 1 252 ? -120.681 41.436 -45.844 1.00 54.90 ? 252  ILE A O   1 
ATOM   1855 C CB  . ILE A 1 252 ? -117.968 39.908 -47.194 1.00 53.45 ? 252  ILE A CB  1 
ATOM   1856 C CG1 . ILE A 1 252 ? -116.559 39.351 -46.917 1.00 53.47 ? 252  ILE A CG1 1 
ATOM   1857 C CG2 . ILE A 1 252 ? -117.933 41.300 -47.830 1.00 53.37 ? 252  ILE A CG2 1 
ATOM   1858 C CD1 . ILE A 1 252 ? -115.587 39.389 -48.091 1.00 53.87 ? 252  ILE A CD1 1 
ATOM   1859 N N   . PHE A 1 253 ? -121.044 39.349 -46.645 1.00 56.15 ? 253  PHE A N   1 
ATOM   1860 C CA  . PHE A 1 253 ? -122.504 39.461 -46.767 1.00 57.59 ? 253  PHE A CA  1 
ATOM   1861 C C   . PHE A 1 253 ? -122.988 40.715 -47.513 1.00 59.08 ? 253  PHE A C   1 
ATOM   1862 O O   . PHE A 1 253 ? -123.576 41.619 -46.914 1.00 59.35 ? 253  PHE A O   1 
ATOM   1863 C CB  . PHE A 1 253 ? -123.174 39.403 -45.382 1.00 57.29 ? 253  PHE A CB  1 
ATOM   1864 C CG  . PHE A 1 253 ? -122.955 38.117 -44.629 1.00 56.35 ? 253  PHE A CG  1 
ATOM   1865 C CD1 . PHE A 1 253 ? -122.780 38.141 -43.252 1.00 55.87 ? 253  PHE A CD1 1 
ATOM   1866 C CD2 . PHE A 1 253 ? -122.966 36.890 -45.275 1.00 55.67 ? 253  PHE A CD2 1 
ATOM   1867 C CE1 . PHE A 1 253 ? -122.592 36.965 -42.535 1.00 55.54 ? 253  PHE A CE1 1 
ATOM   1868 C CE2 . PHE A 1 253 ? -122.780 35.709 -44.565 1.00 55.23 ? 253  PHE A CE2 1 
ATOM   1869 C CZ  . PHE A 1 253 ? -122.594 35.744 -43.199 1.00 55.16 ? 253  PHE A CZ  1 
ATOM   1870 N N   . SER A 1 254 ? -122.752 40.776 -48.815 1.00 60.77 ? 254  SER A N   1 
ATOM   1871 C CA  . SER A 1 254 ? -123.204 41.930 -49.587 1.00 62.59 ? 254  SER A CA  1 
ATOM   1872 C C   . SER A 1 254 ? -124.457 41.606 -50.405 1.00 63.87 ? 254  SER A C   1 
ATOM   1873 O O   . SER A 1 254 ? -125.100 40.589 -50.168 1.00 64.00 ? 254  SER A O   1 
ATOM   1874 C CB  . SER A 1 254 ? -122.077 42.428 -50.482 1.00 62.54 ? 254  SER A CB  1 
ATOM   1875 O OG  . SER A 1 254 ? -121.885 41.541 -51.571 1.00 62.97 ? 254  SER A OG  1 
ATOM   1876 N N   . GLY A 1 255 ? -124.795 42.477 -51.358 1.00 65.40 ? 255  GLY A N   1 
ATOM   1877 C CA  . GLY A 1 255 ? -125.924 42.280 -52.262 1.00 67.26 ? 255  GLY A CA  1 
ATOM   1878 C C   . GLY A 1 255 ? -127.122 41.523 -51.698 1.00 68.71 ? 255  GLY A C   1 
ATOM   1879 O O   . GLY A 1 255 ? -127.734 41.973 -50.727 1.00 68.62 ? 255  GLY A O   1 
ATOM   1880 N N   . PRO A 1 256 ? -127.448 40.372 -52.294 1.00 69.94 ? 256  PRO A N   1 
ATOM   1881 C CA  . PRO A 1 256 ? -128.630 39.592 -51.904 1.00 71.02 ? 256  PRO A CA  1 
ATOM   1882 C C   . PRO A 1 256 ? -128.450 38.766 -50.629 1.00 72.20 ? 256  PRO A C   1 
ATOM   1883 O O   . PRO A 1 256 ? -129.403 38.095 -50.216 1.00 72.28 ? 256  PRO A O   1 
ATOM   1884 C CB  . PRO A 1 256 ? -128.843 38.651 -53.100 1.00 71.03 ? 256  PRO A CB  1 
ATOM   1885 C CG  . PRO A 1 256 ? -127.806 39.039 -54.133 1.00 70.66 ? 256  PRO A CG  1 
ATOM   1886 C CD  . PRO A 1 256 ? -126.709 39.728 -53.394 1.00 70.20 ? 256  PRO A CD  1 
ATOM   1887 N N   . ALA A 1 257 ? -127.270 38.832 -50.011 1.00 73.52 ? 257  ALA A N   1 
ATOM   1888 C CA  . ALA A 1 257 ? -126.901 37.925 -48.919 1.00 74.74 ? 257  ALA A CA  1 
ATOM   1889 C C   . ALA A 1 257 ? -127.956 37.800 -47.825 1.00 75.67 ? 257  ALA A C   1 
ATOM   1890 O O   . ALA A 1 257 ? -128.455 36.701 -47.582 1.00 75.85 ? 257  ALA A O   1 
ATOM   1891 C CB  . ALA A 1 257 ? -125.549 38.296 -48.328 1.00 74.65 ? 257  ALA A CB  1 
ATOM   1892 N N   . ILE A 1 258 ? -128.297 38.924 -47.190 1.00 76.74 ? 258  ILE A N   1 
ATOM   1893 C CA  . ILE A 1 258 ? -129.276 38.964 -46.093 1.00 77.69 ? 258  ILE A CA  1 
ATOM   1894 C C   . ILE A 1 258 ? -130.440 37.991 -46.280 1.00 77.92 ? 258  ILE A C   1 
ATOM   1895 O O   . ILE A 1 258 ? -130.621 37.073 -45.477 1.00 78.00 ? 258  ILE A O   1 
ATOM   1896 C CB  . ILE A 1 258 ? -129.901 40.363 -45.946 1.00 78.10 ? 258  ILE A CB  1 
ATOM   1897 C CG1 . ILE A 1 258 ? -128.819 41.402 -45.650 1.00 19.99 ? 258  ILE A CG1 1 
ATOM   1898 C CG2 . ILE A 1 258 ? -130.962 40.360 -44.856 1.00 19.99 ? 258  ILE A CG2 1 
ATOM   1899 C CD1 . ILE A 1 258 ? -129.309 42.831 -45.727 1.00 79.58 ? 258  ILE A CD1 1 
ATOM   1900 N N   . SER A 1 259 ? -131.216 38.209 -47.343 1.00 78.18 ? 259  SER A N   1 
ATOM   1901 C CA  . SER A 1 259 ? -132.421 37.427 -47.622 1.00 78.24 ? 259  SER A CA  1 
ATOM   1902 C C   . SER A 1 259 ? -132.088 36.029 -48.126 1.00 77.98 ? 259  SER A C   1 
ATOM   1903 O O   . SER A 1 259 ? -132.697 35.056 -47.691 1.00 77.97 ? 259  SER A O   1 
ATOM   1904 C CB  . SER A 1 259 ? -133.321 38.156 -48.628 1.00 78.41 ? 259  SER A CB  1 
ATOM   1905 O OG  . SER A 1 259 ? -132.834 38.004 -49.953 1.00 78.72 ? 259  SER A OG  1 
ATOM   1906 N N   . ARG A 1 260 ? -131.122 35.949 -49.044 1.00 77.72 ? 260  ARG A N   1 
ATOM   1907 C CA  . ARG A 1 260 ? -130.632 34.679 -49.587 1.00 77.30 ? 260  ARG A CA  1 
ATOM   1908 C C   . ARG A 1 260 ? -130.382 33.661 -48.476 1.00 77.09 ? 260  ARG A C   1 
ATOM   1909 O O   . ARG A 1 260 ? -130.736 32.489 -48.614 1.00 77.04 ? 260  ARG A O   1 
ATOM   1910 C CB  . ARG A 1 260 ? -129.347 34.900 -50.390 1.00 77.14 ? 260  ARG A CB  1 
ATOM   1911 C CG  . ARG A 1 260 ? -129.536 35.003 -51.891 1.00 76.44 ? 260  ARG A CG  1 
ATOM   1912 C CD  . ARG A 1 260 ? -128.302 34.613 -52.678 1.00 75.49 ? 260  ARG A CD  1 
ATOM   1913 N NE  . ARG A 1 260 ? -128.372 35.033 -54.076 1.00 75.04 ? 260  ARG A NE  1 
ATOM   1914 C CZ  . ARG A 1 260 ? -127.333 35.464 -54.793 1.00 74.66 ? 260  ARG A CZ  1 
ATOM   1915 N NH1 . ARG A 1 260 ? -126.124 35.544 -54.251 1.00 74.38 ? 260  ARG A NH1 1 
ATOM   1916 N NH2 . ARG A 1 260 ? -127.501 35.820 -56.062 1.00 74.30 ? 260  ARG A NH2 1 
ATOM   1917 N N   . ILE A 1 261 ? -129.785 34.131 -47.377 1.00 76.84 ? 261  ILE A N   1 
ATOM   1918 C CA  . ILE A 1 261 ? -129.533 33.319 -46.185 1.00 76.63 ? 261  ILE A CA  1 
ATOM   1919 C C   . ILE A 1 261 ? -130.837 32.773 -45.600 1.00 76.50 ? 261  ILE A C   1 
ATOM   1920 O O   . ILE A 1 261 ? -131.012 31.558 -45.475 1.00 76.65 ? 261  ILE A O   1 
ATOM   1921 C CB  . ILE A 1 261 ? -128.778 34.144 -45.111 1.00 76.58 ? 261  ILE A CB  1 
ATOM   1922 C CG1 . ILE A 1 261 ? -127.404 34.605 -45.623 1.00 76.39 ? 261  ILE A CG1 1 
ATOM   1923 C CG2 . ILE A 1 261 ? -128.686 33.369 -43.802 1.00 76.62 ? 261  ILE A CG2 1 
ATOM   1924 C CD1 . ILE A 1 261 ? -126.245 33.701 -45.271 1.00 76.28 ? 261  ILE A CD1 1 
ATOM   1925 N N   . ASN A 1 262 ? -131.744 33.683 -45.251 1.00 76.15 ? 262  ASN A N   1 
ATOM   1926 C CA  . ASN A 1 262 ? -133.032 33.328 -44.669 1.00 75.68 ? 262  ASN A CA  1 
ATOM   1927 C C   . ASN A 1 262 ? -133.834 32.373 -45.560 1.00 75.03 ? 262  ASN A C   1 
ATOM   1928 O O   . ASN A 1 262 ? -134.332 31.354 -45.078 1.00 75.25 ? 262  ASN A O   1 
ATOM   1929 C CB  . ASN A 1 262 ? -133.831 34.593 -44.325 1.00 76.05 ? 262  ASN A CB  1 
ATOM   1930 C CG  . ASN A 1 262 ? -133.243 35.361 -43.132 1.00 76.57 ? 262  ASN A CG  1 
ATOM   1931 O OD1 . ASN A 1 262 ? -133.116 34.825 -42.021 1.00 76.93 ? 262  ASN A OD1 1 
ATOM   1932 N ND2 . ASN A 1 262 ? -132.892 36.624 -43.359 1.00 76.81 ? 262  ASN A ND2 1 
ATOM   1933 N N   . ASN A 1 263 ? -133.924 32.688 -46.855 1.00 73.96 ? 263  ASN A N   1 
ATOM   1934 C CA  . ASN A 1 263 ? -134.584 31.828 -47.847 1.00 72.90 ? 263  ASN A CA  1 
ATOM   1935 C C   . ASN A 1 263 ? -133.943 30.449 -48.041 1.00 71.65 ? 263  ASN A C   1 
ATOM   1936 O O   . ASN A 1 263 ? -134.558 29.555 -48.635 1.00 71.88 ? 263  ASN A O   1 
ATOM   1937 C CB  . ASN A 1 263 ? -134.653 32.520 -49.213 1.00 73.30 ? 263  ASN A CB  1 
ATOM   1938 C CG  . ASN A 1 263 ? -135.481 33.785 -49.189 1.00 74.08 ? 263  ASN A CG  1 
ATOM   1939 O OD1 . ASN A 1 263 ? -136.478 33.880 -48.470 1.00 74.74 ? 263  ASN A OD1 1 
ATOM   1940 N ND2 . ASN A 1 263 ? -135.074 34.770 -49.988 1.00 74.96 ? 263  ASN A ND2 1 
ATOM   1941 N N   . ALA A 1 264 ? -132.706 30.285 -47.574 1.00 69.78 ? 264  ALA A N   1 
ATOM   1942 C CA  . ALA A 1 264 ? -132.032 28.992 -47.649 1.00 67.79 ? 264  ALA A CA  1 
ATOM   1943 C C   . ALA A 1 264 ? -132.285 28.183 -46.383 1.00 66.10 ? 264  ALA A C   1 
ATOM   1944 O O   . ALA A 1 264 ? -132.624 28.737 -45.330 1.00 65.89 ? 264  ALA A O   1 
ATOM   1945 C CB  . ALA A 1 264 ? -130.536 29.167 -47.900 1.00 68.02 ? 264  ALA A CB  1 
ATOM   1946 N N   . CYS A 1 265 ? -132.108 26.872 -46.499 1.00 63.97 ? 265  CYS A N   1 
ATOM   1947 C CA  . CYS A 1 265 ? -132.463 25.935 -45.442 1.00 61.94 ? 265  CYS A CA  1 
ATOM   1948 C C   . CYS A 1 265 ? -131.547 25.963 -44.212 1.00 60.17 ? 265  CYS A C   1 
ATOM   1949 O O   . CYS A 1 265 ? -131.768 25.199 -43.266 1.00 60.19 ? 265  CYS A O   1 
ATOM   1950 C CB  . CYS A 1 265 ? -132.473 24.529 -46.015 1.00 62.14 ? 265  CYS A CB  1 
ATOM   1951 S SG  . CYS A 1 265 ? -130.847 24.042 -46.613 1.00 62.89 ? 265  CYS A SG  1 
ATOM   1952 N N   . PHE A 1 266 ? -130.533 26.831 -44.225 1.00 57.76 ? 266  PHE A N   1 
ATOM   1953 C CA  . PHE A 1 266 ? -129.539 26.905 -43.150 1.00 55.28 ? 266  PHE A CA  1 
ATOM   1954 C C   . PHE A 1 266 ? -130.141 26.826 -41.745 1.00 54.09 ? 266  PHE A C   1 
ATOM   1955 O O   . PHE A 1 266 ? -130.962 27.656 -41.359 1.00 54.20 ? 266  PHE A O   1 
ATOM   1956 C CB  . PHE A 1 266 ? -128.698 28.187 -43.268 1.00 54.79 ? 266  PHE A CB  1 
ATOM   1957 C CG  . PHE A 1 266 ? -127.751 28.199 -44.441 1.00 52.64 ? 266  PHE A CG  1 
ATOM   1958 C CD1 . PHE A 1 266 ? -127.806 29.215 -45.377 1.00 51.10 ? 266  PHE A CD1 1 
ATOM   1959 C CD2 . PHE A 1 266 ? -126.793 27.204 -44.596 1.00 51.25 ? 266  PHE A CD2 1 
ATOM   1960 C CE1 . PHE A 1 266 ? -126.933 29.230 -46.458 1.00 50.34 ? 266  PHE A CE1 1 
ATOM   1961 C CE2 . PHE A 1 266 ? -125.922 27.216 -45.676 1.00 50.21 ? 266  PHE A CE2 1 
ATOM   1962 C CZ  . PHE A 1 266 ? -125.992 28.229 -46.604 1.00 49.67 ? 266  PHE A CZ  1 
ATOM   1963 N N   . GLU A 1 267 ? -129.737 25.812 -40.995 1.00 52.42 ? 267  GLU A N   1 
ATOM   1964 C CA  . GLU A 1 267 ? -130.040 25.734 -39.577 1.00 50.98 ? 267  GLU A CA  1 
ATOM   1965 C C   . GLU A 1 267 ? -129.512 26.991 -38.860 1.00 50.13 ? 267  GLU A C   1 
ATOM   1966 O O   . GLU A 1 267 ? -130.233 27.638 -38.100 1.00 50.30 ? 267  GLU A O   1 
ATOM   1967 C CB  . GLU A 1 267 ? -129.412 24.468 -38.996 1.00 50.92 ? 267  GLU A CB  1 
ATOM   1968 C CG  . GLU A 1 267 ? -129.877 24.106 -37.599 1.00 51.14 ? 267  GLU A CG  1 
ATOM   1969 C CD  . GLU A 1 267 ? -131.385 23.948 -37.499 1.00 51.39 ? 267  GLU A CD  1 
ATOM   1970 O OE1 . GLU A 1 267 ? -131.971 23.139 -38.268 1.00 51.04 ? 267  GLU A OE1 1 
ATOM   1971 O OE2 . GLU A 1 267 ? -131.975 24.635 -36.641 1.00 51.76 ? 267  GLU A OE2 1 
ATOM   1972 N N   . ALA A 1 268 ? -128.252 27.329 -39.128 1.00 48.80 ? 268  ALA A N   1 
ATOM   1973 C CA  . ALA A 1 268 ? -127.606 28.529 -38.615 1.00 47.43 ? 268  ALA A CA  1 
ATOM   1974 C C   . ALA A 1 268 ? -126.493 28.951 -39.583 1.00 46.52 ? 268  ALA A C   1 
ATOM   1975 O O   . ALA A 1 268 ? -126.018 28.141 -40.383 1.00 46.62 ? 268  ALA A O   1 
ATOM   1976 C CB  . ALA A 1 268 ? -127.039 28.270 -37.217 1.00 47.36 ? 268  ALA A CB  1 
ATOM   1977 N N   . VAL A 1 269 ? -126.107 30.224 -39.536 1.00 45.10 ? 269  VAL A N   1 
ATOM   1978 C CA  . VAL A 1 269 ? -124.924 30.699 -40.245 1.00 43.61 ? 269  VAL A CA  1 
ATOM   1979 C C   . VAL A 1 269 ? -123.966 31.329 -39.233 1.00 42.99 ? 269  VAL A C   1 
ATOM   1980 O O   . VAL A 1 269 ? -124.320 32.273 -38.527 1.00 43.05 ? 269  VAL A O   1 
ATOM   1981 C CB  . VAL A 1 269 ? -125.285 31.690 -41.354 1.00 43.46 ? 269  VAL A CB  1 
ATOM   1982 C CG1 . VAL A 1 269 ? -124.046 32.064 -42.179 1.00 43.07 ? 269  VAL A CG1 1 
ATOM   1983 C CG2 . VAL A 1 269 ? -126.355 31.102 -42.249 1.00 43.03 ? 269  VAL A CG2 1 
ATOM   1984 N N   . VAL A 1 270 ? -122.757 30.795 -39.143 1.00 42.12 ? 270  VAL A N   1 
ATOM   1985 C CA  . VAL A 1 270 ? -121.816 31.262 -38.126 1.00 41.56 ? 270  VAL A CA  1 
ATOM   1986 C C   . VAL A 1 270 ? -120.642 32.028 -38.745 1.00 41.22 ? 270  VAL A C   1 
ATOM   1987 O O   . VAL A 1 270 ? -120.014 31.578 -39.704 1.00 40.95 ? 270  VAL A O   1 
ATOM   1988 C CB  . VAL A 1 270 ? -121.319 30.112 -37.205 1.00 41.40 ? 270  VAL A CB  1 
ATOM   1989 C CG1 . VAL A 1 270 ? -120.697 30.667 -35.943 1.00 41.40 ? 270  VAL A CG1 1 
ATOM   1990 C CG2 . VAL A 1 270 ? -122.462 29.186 -36.837 1.00 40.82 ? 270  VAL A CG2 1 
ATOM   1991 N N   . VAL A 1 271 ? -120.389 33.209 -38.196 1.00 40.90 ? 271  VAL A N   1 
ATOM   1992 C CA  . VAL A 1 271 ? -119.290 34.053 -38.629 1.00 40.71 ? 271  VAL A CA  1 
ATOM   1993 C C   . VAL A 1 271 ? -118.552 34.617 -37.423 1.00 41.04 ? 271  VAL A C   1 
ATOM   1994 O O   . VAL A 1 271 ? -119.011 34.480 -36.276 1.00 40.64 ? 271  VAL A O   1 
ATOM   1995 C CB  . VAL A 1 271 ? -119.756 35.189 -39.570 1.00 40.67 ? 271  VAL A CB  1 
ATOM   1996 C CG1 . VAL A 1 271 ? -120.169 34.621 -40.919 1.00 40.85 ? 271  VAL A CG1 1 
ATOM   1997 C CG2 . VAL A 1 271 ? -120.892 35.991 -38.966 1.00 40.13 ? 271  VAL A CG2 1 
ATOM   1998 N N   . THR A 1 272 ? -117.392 35.210 -37.688 1.00 41.61 ? 272  THR A N   1 
ATOM   1999 C CA  . THR A 1 272 ? -116.620 35.905 -36.666 1.00 42.34 ? 272  THR A CA  1 
ATOM   2000 C C   . THR A 1 272 ? -116.833 37.408 -36.717 1.00 43.12 ? 272  THR A C   1 
ATOM   2001 O O   . THR A 1 272 ? -117.373 37.974 -37.665 1.00 43.10 ? 272  THR A O   1 
ATOM   2002 C CB  . THR A 1 272 ? -115.103 35.679 -36.823 1.00 42.34 ? 272  THR A CB  1 
ATOM   2003 O OG1 . THR A 1 272 ? -114.652 36.358 -38.010 1.00 41.75 ? 272  THR A OG1 1 
ATOM   2004 C CG2 . THR A 1 272 ? -114.747 34.190 -37.028 1.00 42.27 ? 272  THR A CG2 1 
ATOM   2005 N N   . ASN A 1 273 ? -116.331 38.029 -35.668 1.00 44.20 ? 273  ASN A N   1 
ATOM   2006 C CA  . ASN A 1 273 ? -116.212 39.458 -35.514 1.00 45.28 ? 273  ASN A CA  1 
ATOM   2007 C C   . ASN A 1 273 ? -115.282 40.222 -36.483 1.00 45.88 ? 273  ASN A C   1 
ATOM   2008 O O   . ASN A 1 273 ? -115.129 41.439 -36.342 1.00 45.72 ? 273  ASN A O   1 
ATOM   2009 C CB  . ASN A 1 273 ? -115.708 39.687 -34.098 1.00 45.43 ? 273  ASN A CB  1 
ATOM   2010 C CG  . ASN A 1 273 ? -116.668 40.446 -33.290 1.00 46.34 ? 273  ASN A CG  1 
ATOM   2011 O OD1 . ASN A 1 273 ? -117.709 40.871 -33.804 1.00 48.03 ? 273  ASN A OD1 1 
ATOM   2012 N ND2 . ASN A 1 273 ? -116.350 40.644 -32.015 1.00 46.17 ? 273  ASN A ND2 1 
ATOM   2013 N N   . THR A 1 274 ? -114.656 39.534 -37.441 1.00 46.88 ? 274  THR A N   1 
ATOM   2014 C CA  . THR A 1 274 ? -113.683 40.194 -38.328 1.00 47.96 ? 274  THR A CA  1 
ATOM   2015 C C   . THR A 1 274 ? -114.302 41.342 -39.131 1.00 48.89 ? 274  THR A C   1 
ATOM   2016 O O   . THR A 1 274 ? -113.635 42.331 -39.428 1.00 48.82 ? 274  THR A O   1 
ATOM   2017 C CB  . THR A 1 274 ? -112.917 39.196 -39.258 1.00 47.71 ? 274  THR A CB  1 
ATOM   2018 O OG1 . THR A 1 274 ? -113.834 38.332 -39.931 1.00 48.16 ? 274  THR A OG1 1 
ATOM   2019 C CG2 . THR A 1 274 ? -112.068 38.239 -38.452 1.00 47.31 ? 274  THR A CG2 1 
ATOM   2020 N N   . ILE A 1 275 ? -115.578 41.196 -39.469 1.00 50.50 ? 275  ILE A N   1 
ATOM   2021 C CA  . ILE A 1 275 ? -116.369 42.253 -40.100 1.00 52.01 ? 275  ILE A CA  1 
ATOM   2022 C C   . ILE A 1 275 ? -117.604 42.439 -39.207 1.00 53.74 ? 275  ILE A C   1 
ATOM   2023 O O   . ILE A 1 275 ? -118.082 41.456 -38.627 1.00 53.49 ? 275  ILE A O   1 
ATOM   2024 C CB  . ILE A 1 275 ? -116.746 41.846 -41.561 1.00 51.70 ? 275  ILE A CB  1 
ATOM   2025 C CG1 . ILE A 1 275 ? -115.491 41.763 -42.440 1.00 51.03 ? 275  ILE A CG1 1 
ATOM   2026 C CG2 . ILE A 1 275 ? -117.771 42.804 -42.184 1.00 51.51 ? 275  ILE A CG2 1 
ATOM   2027 C CD1 . ILE A 1 275 ? -115.641 40.866 -43.650 1.00 50.31 ? 275  ILE A CD1 1 
ATOM   2028 N N   . PRO A 1 276 ? -118.092 43.677 -39.048 1.00 55.60 ? 276  PRO A N   1 
ATOM   2029 C CA  . PRO A 1 276 ? -119.291 43.936 -38.235 1.00 57.29 ? 276  PRO A CA  1 
ATOM   2030 C C   . PRO A 1 276 ? -120.554 43.249 -38.774 1.00 59.22 ? 276  PRO A C   1 
ATOM   2031 O O   . PRO A 1 276 ? -120.841 43.315 -39.973 1.00 59.16 ? 276  PRO A O   1 
ATOM   2032 C CB  . PRO A 1 276 ? -119.433 45.461 -38.302 1.00 56.91 ? 276  PRO A CB  1 
ATOM   2033 C CG  . PRO A 1 276 ? -118.082 45.936 -38.613 1.00 56.17 ? 276  PRO A CG  1 
ATOM   2034 C CD  . PRO A 1 276 ? -117.530 44.933 -39.579 1.00 55.66 ? 276  PRO A CD  1 
ATOM   2035 N N   . GLN A 1 277 ? -121.288 42.593 -37.876 1.00 61.70 ? 277  GLN A N   1 
ATOM   2036 C CA  . GLN A 1 277 ? -122.494 41.842 -38.243 1.00 64.12 ? 277  GLN A CA  1 
ATOM   2037 C C   . GLN A 1 277 ? -123.761 42.394 -37.592 1.00 65.95 ? 277  GLN A C   1 
ATOM   2038 O O   . GLN A 1 277 ? -124.867 42.039 -38.003 1.00 66.10 ? 277  GLN A O   1 
ATOM   2039 C CB  . GLN A 1 277 ? -122.355 40.351 -37.889 1.00 64.12 ? 277  GLN A CB  1 
ATOM   2040 C CG  . GLN A 1 277 ? -121.029 39.687 -38.262 1.00 64.12 ? 277  GLN A CG  1 
ATOM   2041 C CD  . GLN A 1 277 ? -120.775 39.640 -39.759 1.00 64.10 ? 277  GLN A CD  1 
ATOM   2042 O OE1 . GLN A 1 277 ? -119.623 39.612 -40.185 1.00 64.55 ? 277  GLN A OE1 1 
ATOM   2043 N NE2 . GLN A 1 277 ? -121.840 39.629 -40.555 1.00 63.86 ? 277  GLN A NE2 1 
ATOM   2044 N N   . GLU A 1 278 ? -123.581 43.251 -36.581 1.00 68.16 ? 278  GLU A N   1 
ATOM   2045 C CA  . GLU A 1 278 ? -124.668 43.880 -35.813 1.00 70.12 ? 278  GLU A CA  1 
ATOM   2046 C C   . GLU A 1 278 ? -125.825 44.379 -36.697 1.00 71.27 ? 278  GLU A C   1 
ATOM   2047 O O   . GLU A 1 278 ? -126.993 44.152 -36.376 1.00 71.43 ? 278  GLU A O   1 
ATOM   2048 C CB  . GLU A 1 278 ? -124.109 45.018 -34.937 1.00 70.49 ? 278  GLU A CB  1 
ATOM   2049 C CG  . GLU A 1 278 ? -123.048 44.589 -33.913 1.00 71.84 ? 278  GLU A CG  1 
ATOM   2050 C CD  . GLU A 1 278 ? -121.612 44.623 -34.453 1.00 73.22 ? 278  GLU A CD  1 
ATOM   2051 O OE1 . GLU A 1 278 ? -121.055 43.539 -34.755 1.00 73.54 ? 278  GLU A OE1 1 
ATOM   2052 O OE2 . GLU A 1 278 ? -121.029 45.729 -34.567 1.00 73.65 ? 278  GLU A OE2 1 
ATOM   2053 N N   . ASP A 1 279 ? -125.478 45.033 -37.808 1.00 72.67 ? 279  ASP A N   1 
ATOM   2054 C CA  . ASP A 1 279 ? -126.423 45.493 -38.835 1.00 74.02 ? 279  ASP A CA  1 
ATOM   2055 C C   . ASP A 1 279 ? -127.173 44.337 -39.534 1.00 74.72 ? 279  ASP A C   1 
ATOM   2056 O O   . ASP A 1 279 ? -128.378 44.441 -39.799 1.00 74.87 ? 279  ASP A O   1 
ATOM   2057 C CB  . ASP A 1 279 ? -125.666 46.360 -39.867 1.00 74.40 ? 279  ASP A CB  1 
ATOM   2058 C CG  . ASP A 1 279 ? -126.586 47.010 -40.911 1.00 75.16 ? 279  ASP A CG  1 
ATOM   2059 O OD1 . ASP A 1 279 ? -127.047 46.309 -41.841 1.00 75.62 ? 279  ASP A OD1 1 
ATOM   2060 O OD2 . ASP A 1 279 ? -126.874 48.228 -40.904 1.00 75.90 ? 279  ASP A OD2 1 
ATOM   2061 N N   . LYS A 1 280 ? -126.457 43.252 -39.833 1.00 75.43 ? 280  LYS A N   1 
ATOM   2062 C CA  . LYS A 1 280 ? -127.030 42.087 -40.521 1.00 76.11 ? 280  LYS A CA  1 
ATOM   2063 C C   . LYS A 1 280 ? -127.783 41.160 -39.569 1.00 76.61 ? 280  LYS A C   1 
ATOM   2064 O O   . LYS A 1 280 ? -128.700 40.453 -39.986 1.00 76.55 ? 280  LYS A O   1 
ATOM   2065 C CB  . LYS A 1 280 ? -125.945 41.270 -41.244 1.00 76.04 ? 280  LYS A CB  1 
ATOM   2066 C CG  . LYS A 1 280 ? -124.890 42.080 -41.982 1.00 76.30 ? 280  LYS A CG  1 
ATOM   2067 C CD  . LYS A 1 280 ? -125.036 41.958 -43.490 1.00 76.40 ? 280  LYS A CD  1 
ATOM   2068 C CE  . LYS A 1 280 ? -124.723 43.281 -44.180 1.00 76.46 ? 280  LYS A CE  1 
ATOM   2069 N NZ  . LYS A 1 280 ? -123.441 43.254 -44.941 1.00 76.27 ? 280  LYS A NZ  1 
ATOM   2070 N N   . MET A 1 281 ? -127.385 41.170 -38.297 1.00 77.38 ? 281  MET A N   1 
ATOM   2071 C CA  . MET A 1 281 ? -127.885 40.230 -37.290 1.00 78.20 ? 281  MET A CA  1 
ATOM   2072 C C   . MET A 1 281 ? -129.364 40.416 -36.944 1.00 78.54 ? 281  MET A C   1 
ATOM   2073 O O   . MET A 1 281 ? -130.057 39.450 -36.617 1.00 78.60 ? 281  MET A O   1 
ATOM   2074 C CB  . MET A 1 281 ? -127.041 40.314 -36.013 1.00 78.37 ? 281  MET A CB  1 
ATOM   2075 C CG  . MET A 1 281 ? -125.710 39.582 -36.090 1.00 79.06 ? 281  MET A CG  1 
ATOM   2076 S SD  . MET A 1 281 ? -125.021 39.218 -34.461 1.00 80.55 ? 281  MET A SD  1 
ATOM   2077 C CE  . MET A 1 281 ? -124.062 40.699 -34.124 1.00 80.43 ? 281  MET A CE  1 
ATOM   2078 N N   . LYS A 1 282 ? -129.834 41.658 -37.007 1.00 78.95 ? 282  LYS A N   1 
ATOM   2079 C CA  . LYS A 1 282 ? -131.230 41.972 -36.712 1.00 79.27 ? 282  LYS A CA  1 
ATOM   2080 C C   . LYS A 1 282 ? -132.169 41.540 -37.838 1.00 79.15 ? 282  LYS A C   1 
ATOM   2081 O O   . LYS A 1 282 ? -133.269 41.053 -37.572 1.00 79.38 ? 282  LYS A O   1 
ATOM   2082 C CB  . LYS A 1 282 ? -131.417 43.460 -36.388 1.00 79.54 ? 282  LYS A CB  1 
ATOM   2083 C CG  . LYS A 1 282 ? -130.547 44.406 -37.199 1.00 80.37 ? 282  LYS A CG  1 
ATOM   2084 C CD  . LYS A 1 282 ? -130.185 45.649 -36.395 1.00 81.30 ? 282  LYS A CD  1 
ATOM   2085 C CE  . LYS A 1 282 ? -129.850 46.816 -37.316 1.00 81.83 ? 282  LYS A CE  1 
ATOM   2086 N NZ  . LYS A 1 282 ? -130.758 47.975 -37.085 1.00 82.23 ? 282  LYS A NZ  1 
ATOM   2087 N N   . HIS A 1 283 ? -131.732 41.705 -39.085 1.00 78.81 ? 283  HIS A N   1 
ATOM   2088 C CA  . HIS A 1 283 ? -132.546 41.307 -40.237 1.00 78.54 ? 283  HIS A CA  1 
ATOM   2089 C C   . HIS A 1 283 ? -132.377 39.820 -40.604 1.00 77.34 ? 283  HIS A C   1 
ATOM   2090 O O   . HIS A 1 283 ? -133.010 39.326 -41.544 1.00 77.29 ? 283  HIS A O   1 
ATOM   2091 C CB  . HIS A 1 283 ? -132.264 42.215 -41.445 1.00 79.33 ? 283  HIS A CB  1 
ATOM   2092 C CG  . HIS A 1 283 ? -133.036 43.503 -41.434 1.00 81.48 ? 283  HIS A CG  1 
ATOM   2093 N ND1 . HIS A 1 283 ? -134.391 43.562 -41.178 1.00 82.97 ? 283  HIS A ND1 1 
ATOM   2094 C CD2 . HIS A 1 283 ? -132.639 44.781 -41.651 1.00 82.88 ? 283  HIS A CD2 1 
ATOM   2095 C CE1 . HIS A 1 283 ? -134.795 44.820 -41.235 1.00 83.68 ? 283  HIS A CE1 1 
ATOM   2096 N NE2 . HIS A 1 283 ? -133.751 45.579 -41.520 1.00 83.67 ? 283  HIS A NE2 1 
ATOM   2097 N N   . CYS A 1 284 ? -131.521 39.126 -39.849 1.00 75.84 ? 284  CYS A N   1 
ATOM   2098 C CA  . CYS A 1 284 ? -131.234 37.703 -40.045 1.00 74.26 ? 284  CYS A CA  1 
ATOM   2099 C C   . CYS A 1 284 ? -130.921 37.028 -38.704 1.00 72.79 ? 284  CYS A C   1 
ATOM   2100 O O   . CYS A 1 284 ? -129.799 37.105 -38.190 1.00 72.70 ? 284  CYS A O   1 
ATOM   2101 C CB  . CYS A 1 284 ? -130.073 37.513 -41.031 1.00 74.47 ? 284  CYS A CB  1 
ATOM   2102 S SG  . CYS A 1 284 ? -129.696 35.793 -41.465 1.00 74.93 ? 284  CYS A SG  1 
ATOM   2103 N N   . SER A 1 285 ? -131.929 36.366 -38.145 1.00 70.90 ? 285  SER A N   1 
ATOM   2104 C CA  . SER A 1 285 ? -131.831 35.774 -36.816 1.00 68.94 ? 285  SER A CA  1 
ATOM   2105 C C   . SER A 1 285 ? -130.887 34.575 -36.773 1.00 67.29 ? 285  SER A C   1 
ATOM   2106 O O   . SER A 1 285 ? -130.255 34.317 -35.746 1.00 67.30 ? 285  SER A O   1 
ATOM   2107 C CB  . SER A 1 285 ? -133.224 35.392 -36.301 1.00 69.13 ? 285  SER A CB  1 
ATOM   2108 O OG  . SER A 1 285 ? -133.319 33.992 -36.043 1.00 69.27 ? 285  SER A OG  1 
ATOM   2109 N N   . LYS A 1 286 ? -130.786 33.848 -37.883 1.00 65.06 ? 286  LYS A N   1 
ATOM   2110 C CA  . LYS A 1 286 ? -129.992 32.620 -37.899 1.00 62.94 ? 286  LYS A CA  1 
ATOM   2111 C C   . LYS A 1 286 ? -128.465 32.832 -37.894 1.00 61.19 ? 286  LYS A C   1 
ATOM   2112 O O   . LYS A 1 286 ? -127.704 31.866 -37.733 1.00 61.09 ? 286  LYS A O   1 
ATOM   2113 C CB  . LYS A 1 286 ? -130.442 31.670 -39.019 1.00 63.04 ? 286  LYS A CB  1 
ATOM   2114 C CG  . LYS A 1 286 ? -130.206 32.168 -40.434 1.00 63.07 ? 286  LYS A CG  1 
ATOM   2115 C CD  . LYS A 1 286 ? -130.562 31.084 -41.448 1.00 62.71 ? 286  LYS A CD  1 
ATOM   2116 C CE  . LYS A 1 286 ? -132.007 31.189 -41.885 1.00 62.37 ? 286  LYS A CE  1 
ATOM   2117 N NZ  . LYS A 1 286 ? -132.624 29.850 -42.021 1.00 62.36 ? 286  LYS A NZ  1 
ATOM   2118 N N   . ILE A 1 287 ? -128.032 34.085 -38.052 1.00 58.75 ? 287  ILE A N   1 
ATOM   2119 C CA  . ILE A 1 287 ? -126.621 34.446 -37.910 1.00 56.39 ? 287  ILE A CA  1 
ATOM   2120 C C   . ILE A 1 287 ? -126.176 34.458 -36.446 1.00 54.60 ? 287  ILE A C   1 
ATOM   2121 O O   . ILE A 1 287 ? -126.866 34.977 -35.570 1.00 54.26 ? 287  ILE A O   1 
ATOM   2122 C CB  . ILE A 1 287 ? -126.311 35.811 -38.577 1.00 56.41 ? 287  ILE A CB  1 
ATOM   2123 C CG1 . ILE A 1 287 ? -126.460 35.720 -40.098 1.00 56.47 ? 287  ILE A CG1 1 
ATOM   2124 C CG2 . ILE A 1 287 ? -124.901 36.287 -38.207 1.00 56.24 ? 287  ILE A CG2 1 
ATOM   2125 C CD1 . ILE A 1 287 ? -126.303 37.051 -40.825 1.00 56.58 ? 287  ILE A CD1 1 
ATOM   2126 N N   . GLN A 1 288 ? -125.011 33.877 -36.197 1.00 52.60 ? 288  GLN A N   1 
ATOM   2127 C CA  . GLN A 1 288 ? -124.395 33.917 -34.881 1.00 50.85 ? 288  GLN A CA  1 
ATOM   2128 C C   . GLN A 1 288 ? -122.909 34.251 -35.005 1.00 49.03 ? 288  GLN A C   1 
ATOM   2129 O O   . GLN A 1 288 ? -122.227 33.743 -35.899 1.00 48.75 ? 288  GLN A O   1 
ATOM   2130 C CB  . GLN A 1 288 ? -124.595 32.582 -34.173 1.00 51.25 ? 288  GLN A CB  1 
ATOM   2131 C CG  . GLN A 1 288 ? -126.005 32.389 -33.644 1.00 52.47 ? 288  GLN A CG  1 
ATOM   2132 C CD  . GLN A 1 288 ? -126.283 30.956 -33.300 1.00 54.19 ? 288  GLN A CD  1 
ATOM   2133 O OE1 . GLN A 1 288 ? -125.709 30.423 -32.349 1.00 54.89 ? 288  GLN A OE1 1 
ATOM   2134 N NE2 . GLN A 1 288 ? -127.155 30.314 -34.074 1.00 54.94 ? 288  GLN A NE2 1 
ATOM   2135 N N   . VAL A 1 289 ? -122.410 35.114 -34.123 1.00 46.87 ? 289  VAL A N   1 
ATOM   2136 C CA  . VAL A 1 289 ? -121.019 35.549 -34.223 1.00 44.86 ? 289  VAL A CA  1 
ATOM   2137 C C   . VAL A 1 289 ? -120.111 34.956 -33.158 1.00 43.40 ? 289  VAL A C   1 
ATOM   2138 O O   . VAL A 1 289 ? -120.433 34.961 -31.970 1.00 43.13 ? 289  VAL A O   1 
ATOM   2139 C CB  . VAL A 1 289 ? -120.842 37.107 -34.318 1.00 44.70 ? 289  VAL A CB  1 
ATOM   2140 C CG1 . VAL A 1 289 ? -121.943 37.733 -35.149 1.00 44.40 ? 289  VAL A CG1 1 
ATOM   2141 C CG2 . VAL A 1 289 ? -120.765 37.749 -32.946 1.00 44.63 ? 289  VAL A CG2 1 
ATOM   2142 N N   . ILE A 1 290 ? -118.980 34.423 -33.600 1.00 41.70 ? 290  ILE A N   1 
ATOM   2143 C CA  . ILE A 1 290 ? -117.932 34.083 -32.669 1.00 40.47 ? 290  ILE A CA  1 
ATOM   2144 C C   . ILE A 1 290 ? -117.117 35.359 -32.530 1.00 40.33 ? 290  ILE A C   1 
ATOM   2145 O O   . ILE A 1 290 ? -116.656 35.922 -33.524 1.00 40.07 ? 290  ILE A O   1 
ATOM   2146 C CB  . ILE A 1 290 ? -117.076 32.903 -33.186 1.00 40.07 ? 290  ILE A CB  1 
ATOM   2147 C CG1 . ILE A 1 290 ? -117.949 31.663 -33.398 1.00 39.21 ? 290  ILE A CG1 1 
ATOM   2148 C CG2 . ILE A 1 290 ? -115.900 32.610 -32.232 1.00 39.43 ? 290  ILE A CG2 1 
ATOM   2149 C CD1 . ILE A 1 290 ? -117.287 30.566 -34.213 1.00 38.44 ? 290  ILE A CD1 1 
ATOM   2150 N N   . ASP A 1 291 ? -116.972 35.825 -31.297 1.00 40.17 ? 291  ASP A N   1 
ATOM   2151 C CA  . ASP A 1 291 ? -116.181 37.008 -31.009 1.00 40.12 ? 291  ASP A CA  1 
ATOM   2152 C C   . ASP A 1 291 ? -114.699 36.622 -31.041 1.00 39.89 ? 291  ASP A C   1 
ATOM   2153 O O   . ASP A 1 291 ? -114.281 35.677 -30.374 1.00 40.20 ? 291  ASP A O   1 
ATOM   2154 C CB  . ASP A 1 291 ? -116.598 37.591 -29.655 1.00 40.33 ? 291  ASP A CB  1 
ATOM   2155 C CG  . ASP A 1 291 ? -115.737 38.769 -29.214 1.00 41.29 ? 291  ASP A CG  1 
ATOM   2156 O OD1 . ASP A 1 291 ? -115.123 39.455 -30.062 1.00 41.38 ? 291  ASP A OD1 1 
ATOM   2157 O OD2 . ASP A 1 291 ? -115.627 39.089 -28.011 1.00 42.65 ? 291  ASP A OD2 1 
ATOM   2158 N N   . ILE A 1 292 ? -113.915 37.343 -31.837 1.00 39.23 ? 292  ILE A N   1 
ATOM   2159 C CA  . ILE A 1 292 ? -112.505 37.010 -32.002 1.00 38.80 ? 292  ILE A CA  1 
ATOM   2160 C C   . ILE A 1 292 ? -111.565 38.080 -31.445 1.00 38.70 ? 292  ILE A C   1 
ATOM   2161 O O   . ILE A 1 292 ? -110.339 37.994 -31.600 1.00 38.45 ? 292  ILE A O   1 
ATOM   2162 C CB  . ILE A 1 292 ? -112.168 36.638 -33.494 1.00 38.68 ? 292  ILE A CB  1 
ATOM   2163 C CG1 . ILE A 1 292 ? -112.774 37.625 -34.501 1.00 37.97 ? 292  ILE A CG1 1 
ATOM   2164 C CG2 . ILE A 1 292 ? -112.659 35.234 -33.798 1.00 38.69 ? 292  ILE A CG2 1 
ATOM   2165 C CD1 . ILE A 1 292 ? -111.952 38.860 -34.744 1.00 36.69 ? 292  ILE A CD1 1 
ATOM   2166 N N   . SER A 1 293 ? -112.150 39.070 -30.776 1.00 38.73 ? 293  SER A N   1 
ATOM   2167 C CA  . SER A 1 293 ? -111.393 40.162 -30.175 1.00 38.88 ? 293  SER A CA  1 
ATOM   2168 C C   . SER A 1 293 ? -110.374 39.721 -29.117 1.00 39.14 ? 293  SER A C   1 
ATOM   2169 O O   . SER A 1 293 ? -109.309 40.326 -29.005 1.00 39.06 ? 293  SER A O   1 
ATOM   2170 C CB  . SER A 1 293 ? -112.336 41.213 -29.593 1.00 38.68 ? 293  SER A CB  1 
ATOM   2171 O OG  . SER A 1 293 ? -113.070 40.704 -28.496 1.00 38.25 ? 293  SER A OG  1 
ATOM   2172 N N   . MET A 1 294 ? -110.698 38.687 -28.344 1.00 39.67 ? 294  MET A N   1 
ATOM   2173 C CA  . MET A 1 294 ? -109.756 38.146 -27.358 1.00 40.81 ? 294  MET A CA  1 
ATOM   2174 C C   . MET A 1 294 ? -108.511 37.665 -28.083 1.00 39.78 ? 294  MET A C   1 
ATOM   2175 O O   . MET A 1 294 ? -107.390 37.937 -27.654 1.00 39.70 ? 294  MET A O   1 
ATOM   2176 C CB  . MET A 1 294 ? -110.366 36.978 -26.562 1.00 42.11 ? 294  MET A CB  1 
ATOM   2177 C CG  . MET A 1 294 ? -110.113 36.947 -25.026 1.00 46.97 ? 294  MET A CG  1 
ATOM   2178 S SD  . MET A 1 294 ? -108.705 37.856 -24.235 1.00 54.49 ? 294  MET A SD  1 
ATOM   2179 C CE  . MET A 1 294 ? -109.286 37.946 -22.437 1.00 54.87 ? 294  MET A CE  1 
ATOM   2180 N N   . ILE A 1 295 ? -108.726 36.964 -29.192 1.00 38.70 ? 295  ILE A N   1 
ATOM   2181 C CA  . ILE A 1 295 ? -107.638 36.446 -30.004 1.00 37.99 ? 295  ILE A CA  1 
ATOM   2182 C C   . ILE A 1 295 ? -106.759 37.576 -30.572 1.00 37.03 ? 295  ILE A C   1 
ATOM   2183 O O   . ILE A 1 295 ? -105.533 37.466 -30.589 1.00 36.73 ? 295  ILE A O   1 
ATOM   2184 C CB  . ILE A 1 295 ? -108.193 35.508 -31.105 1.00 38.12 ? 295  ILE A CB  1 
ATOM   2185 C CG1 . ILE A 1 295 ? -108.776 34.247 -30.452 1.00 38.68 ? 295  ILE A CG1 1 
ATOM   2186 C CG2 . ILE A 1 295 ? -107.101 35.134 -32.077 1.00 38.22 ? 295  ILE A CG2 1 
ATOM   2187 C CD1 . ILE A 1 295 ? -109.532 33.281 -31.389 1.00 39.84 ? 295  ILE A CD1 1 
ATOM   2188 N N   . LEU A 1 296 ? -107.388 38.668 -30.999 1.00 36.04 ? 296  LEU A N   1 
ATOM   2189 C CA  . LEU A 1 296 ? -106.653 39.790 -31.563 1.00 35.07 ? 296  LEU A CA  1 
ATOM   2190 C C   . LEU A 1 296 ? -105.941 40.592 -30.482 1.00 34.70 ? 296  LEU A C   1 
ATOM   2191 O O   . LEU A 1 296 ? -104.823 41.054 -30.688 1.00 34.42 ? 296  LEU A O   1 
ATOM   2192 C CB  . LEU A 1 296 ? -107.565 40.686 -32.416 1.00 34.85 ? 296  LEU A CB  1 
ATOM   2193 C CG  . LEU A 1 296 ? -108.088 40.150 -33.754 1.00 33.93 ? 296  LEU A CG  1 
ATOM   2194 C CD1 . LEU A 1 296 ? -109.157 41.077 -34.315 1.00 32.56 ? 296  LEU A CD1 1 
ATOM   2195 C CD2 . LEU A 1 296 ? -106.961 39.966 -34.766 1.00 33.48 ? 296  LEU A CD2 1 
ATOM   2196 N N   . ALA A 1 297 ? -106.581 40.751 -29.329 1.00 34.60 ? 297  ALA A N   1 
ATOM   2197 C CA  . ALA A 1 297 ? -105.950 41.430 -28.192 1.00 34.74 ? 297  ALA A CA  1 
ATOM   2198 C C   . ALA A 1 297 ? -104.725 40.662 -27.694 1.00 34.82 ? 297  ALA A C   1 
ATOM   2199 O O   . ALA A 1 297 ? -103.660 41.239 -27.449 1.00 35.09 ? 297  ALA A O   1 
ATOM   2200 C CB  . ALA A 1 297 ? -106.959 41.640 -27.058 1.00 34.38 ? 297  ALA A CB  1 
ATOM   2201 N N   . GLU A 1 298 ? -104.889 39.355 -27.562 1.00 35.06 ? 298  GLU A N   1 
ATOM   2202 C CA  . GLU A 1 298 ? -103.815 38.460 -27.158 1.00 35.74 ? 298  GLU A CA  1 
ATOM   2203 C C   . GLU A 1 298 ? -102.623 38.503 -28.118 1.00 35.15 ? 298  GLU A C   1 
ATOM   2204 O O   . GLU A 1 298 ? -101.468 38.474 -27.666 1.00 35.21 ? 298  GLU A O   1 
ATOM   2205 C CB  . GLU A 1 298 ? -104.353 37.024 -27.018 1.00 36.52 ? 298  GLU A CB  1 
ATOM   2206 C CG  . GLU A 1 298 ? -103.558 36.114 -26.092 1.00 39.15 ? 298  GLU A CG  1 
ATOM   2207 C CD  . GLU A 1 298 ? -103.108 36.814 -24.821 1.00 42.25 ? 298  GLU A CD  1 
ATOM   2208 O OE1 . GLU A 1 298 ? -103.856 37.693 -24.319 1.00 43.06 ? 298  GLU A OE1 1 
ATOM   2209 O OE2 . GLU A 1 298 ? -101.995 36.494 -24.329 1.00 43.62 ? 298  GLU A OE2 1 
ATOM   2210 N N   . ALA A 1 299 ? -102.903 38.579 -29.424 1.00 34.03 ? 299  ALA A N   1 
ATOM   2211 C CA  . ALA A 1 299 ? -101.845 38.678 -30.424 1.00 33.49 ? 299  ALA A CA  1 
ATOM   2212 C C   . ALA A 1 299 ? -101.108 40.016 -30.355 1.00 33.21 ? 299  ALA A C   1 
ATOM   2213 O O   . ALA A 1 299 ? -99.885  40.050 -30.487 1.00 32.96 ? 299  ALA A O   1 
ATOM   2214 C CB  . ALA A 1 299 ? -102.378 38.413 -31.825 1.00 33.22 ? 299  ALA A CB  1 
ATOM   2215 N N   . ILE A 1 300 ? -101.839 41.106 -30.127 1.00 33.01 ? 300  ILE A N   1 
ATOM   2216 C CA  . ILE A 1 300 ? -101.214 42.420 -29.971 1.00 33.60 ? 300  ILE A CA  1 
ATOM   2217 C C   . ILE A 1 300 ? -100.330 42.449 -28.720 1.00 34.87 ? 300  ILE A C   1 
ATOM   2218 O O   . ILE A 1 300 ? -99.142  42.806 -28.787 1.00 34.62 ? 300  ILE A O   1 
ATOM   2219 C CB  . ILE A 1 300 ? -102.270 43.550 -29.926 1.00 33.11 ? 300  ILE A CB  1 
ATOM   2220 C CG1 . ILE A 1 300 ? -102.892 43.751 -31.304 1.00 31.62 ? 300  ILE A CG1 1 
ATOM   2221 C CG2 . ILE A 1 300 ? -101.655 44.868 -29.430 1.00 33.18 ? 300  ILE A CG2 1 
ATOM   2222 C CD1 . ILE A 1 300 ? -104.265 44.290 -31.258 1.00 29.93 ? 300  ILE A CD1 1 
ATOM   2223 N N   . ARG A 1 301 ? -100.923 42.061 -27.592 1.00 36.46 ? 301  ARG A N   1 
ATOM   2224 C CA  . ARG A 1 301 ? -100.234 42.018 -26.307 1.00 38.24 ? 301  ARG A CA  1 
ATOM   2225 C C   . ARG A 1 301 ? -98.987  41.159 -26.377 1.00 38.72 ? 301  ARG A C   1 
ATOM   2226 O O   . ARG A 1 301 ? -97.915  41.587 -25.947 1.00 38.53 ? 301  ARG A O   1 
ATOM   2227 C CB  . ARG A 1 301 ? -101.161 41.483 -25.214 1.00 39.04 ? 301  ARG A CB  1 
ATOM   2228 C CG  . ARG A 1 301 ? -100.725 41.872 -23.805 1.00 41.96 ? 301  ARG A CG  1 
ATOM   2229 C CD  . ARG A 1 301 ? -101.512 41.210 -22.683 1.00 46.15 ? 301  ARG A CD  1 
ATOM   2230 N NE  . ARG A 1 301 ? -100.622 40.335 -21.934 1.00 49.95 ? 301  ARG A NE  1 
ATOM   2231 C CZ  . ARG A 1 301 ? -100.751 39.014 -21.849 1.00 52.34 ? 301  ARG A CZ  1 
ATOM   2232 N NH1 . ARG A 1 301 ? -101.767 38.399 -22.449 1.00 53.47 ? 301  ARG A NH1 1 
ATOM   2233 N NH2 . ARG A 1 301 ? -99.867  38.306 -21.150 1.00 53.07 ? 301  ARG A NH2 1 
ATOM   2234 N N   . ARG A 1 302 ? -99.125  39.955 -26.929 1.00 39.53 ? 302  ARG A N   1 
ATOM   2235 C CA  . ARG A 1 302 ? -97.979  39.068 -27.081 1.00 40.68 ? 302  ARG A CA  1 
ATOM   2236 C C   . ARG A 1 302 ? -96.930  39.623 -28.064 1.00 40.84 ? 302  ARG A C   1 
ATOM   2237 O O   . ARG A 1 302 ? -95.739  39.561 -27.784 1.00 40.83 ? 302  ARG A O   1 
ATOM   2238 C CB  . ARG A 1 302 ? -98.426  37.626 -27.365 1.00 41.29 ? 302  ARG A CB  1 
ATOM   2239 C CG  . ARG A 1 302 ? -98.945  36.938 -26.072 1.00 43.74 ? 302  ARG A CG  1 
ATOM   2240 C CD  . ARG A 1 302 ? -99.824  35.687 -26.240 1.00 47.24 ? 302  ARG A CD  1 
ATOM   2241 N NE  . ARG A 1 302 ? -99.805  34.861 -25.024 1.00 50.44 ? 302  ARG A NE  1 
ATOM   2242 C CZ  . ARG A 1 302 ? -99.264  33.637 -24.926 1.00 52.80 ? 302  ARG A CZ  1 
ATOM   2243 N NH1 . ARG A 1 302 ? -98.695  33.049 -25.977 1.00 53.54 ? 302  ARG A NH1 1 
ATOM   2244 N NH2 . ARG A 1 302 ? -99.297  32.986 -23.766 1.00 53.97 ? 302  ARG A NH2 1 
ATOM   2245 N N   . THR A 1 303 ? -97.380  40.216 -29.172 1.00 41.36 ? 303  THR A N   1 
ATOM   2246 C CA  . THR A 1 303 ? -96.496  40.932 -30.108 1.00 41.98 ? 303  THR A CA  1 
ATOM   2247 C C   . THR A 1 303 ? -95.700  42.068 -29.442 1.00 42.50 ? 303  THR A C   1 
ATOM   2248 O O   . THR A 1 303 ? -94.508  42.231 -29.700 1.00 42.36 ? 303  THR A O   1 
ATOM   2249 C CB  . THR A 1 303 ? -97.321  41.522 -31.274 1.00 41.75 ? 303  THR A CB  1 
ATOM   2250 O OG1 . THR A 1 303 ? -97.672  40.477 -32.176 1.00 41.65 ? 303  THR A OG1 1 
ATOM   2251 C CG2 . THR A 1 303 ? -96.476  42.447 -32.129 1.00 41.49 ? 303  THR A CG2 1 
ATOM   2252 N N   . HIS A 1 304 ? -96.381  42.857 -28.612 1.00 43.21 ? 304  HIS A N   1 
ATOM   2253 C CA  . HIS A 1 304 ? -95.748  43.952 -27.889 1.00 44.02 ? 304  HIS A CA  1 
ATOM   2254 C C   . HIS A 1 304 ? -94.757  43.450 -26.833 1.00 45.46 ? 304  HIS A C   1 
ATOM   2255 O O   . HIS A 1 304 ? -93.693  44.029 -26.661 1.00 45.40 ? 304  HIS A O   1 
ATOM   2256 C CB  . HIS A 1 304 ? -96.802  44.868 -27.256 1.00 43.14 ? 304  HIS A CB  1 
ATOM   2257 C CG  . HIS A 1 304 ? -96.222  45.959 -26.410 1.00 41.27 ? 304  HIS A CG  1 
ATOM   2258 N ND1 . HIS A 1 304 ? -95.652  47.094 -26.947 1.00 39.38 ? 304  HIS A ND1 1 
ATOM   2259 C CD2 . HIS A 1 304 ? -96.106  46.079 -25.068 1.00 39.70 ? 304  HIS A CD2 1 
ATOM   2260 C CE1 . HIS A 1 304 ? -95.222  47.871 -25.972 1.00 38.01 ? 304  HIS A CE1 1 
ATOM   2261 N NE2 . HIS A 1 304 ? -95.487  47.280 -24.823 1.00 38.56 ? 304  HIS A NE2 1 
ATOM   2262 N N   . ASN A 1 305 ? -95.109  42.375 -26.136 1.00 47.52 ? 305  ASN A N   1 
ATOM   2263 C CA  . ASN A 1 305 ? -94.264  41.853 -25.065 1.00 49.58 ? 305  ASN A CA  1 
ATOM   2264 C C   . ASN A 1 305 ? -93.154  40.983 -25.609 1.00 51.26 ? 305  ASN A C   1 
ATOM   2265 O O   . ASN A 1 305 ? -92.147  40.776 -24.940 1.00 51.39 ? 305  ASN A O   1 
ATOM   2266 C CB  . ASN A 1 305 ? -95.084  41.060 -24.045 1.00 49.54 ? 305  ASN A CB  1 
ATOM   2267 C CG  . ASN A 1 305 ? -95.956  41.952 -23.168 1.00 50.20 ? 305  ASN A CG  1 
ATOM   2268 O OD1 . ASN A 1 305 ? -95.689  43.145 -23.013 1.00 50.93 ? 305  ASN A OD1 1 
ATOM   2269 N ND2 . ASN A 1 305 ? -97.007  41.371 -22.587 1.00 50.66 ? 305  ASN A ND2 1 
ATOM   2270 N N   . GLY A 1 306 ? -93.341  40.477 -26.825 1.00 53.24 ? 306  GLY A N   1 
ATOM   2271 C CA  . GLY A 1 306 ? -92.435  39.491 -27.386 1.00 55.54 ? 306  GLY A CA  1 
ATOM   2272 C C   . GLY A 1 306 ? -92.646  38.110 -26.792 1.00 57.36 ? 306  GLY A C   1 
ATOM   2273 O O   . GLY A 1 306 ? -91.702  37.334 -26.688 1.00 57.65 ? 306  GLY A O   1 
ATOM   2274 N N   . GLU A 1 307 ? -93.874  37.802 -26.383 1.00 59.18 ? 307  GLU A N   1 
ATOM   2275 C CA  . GLU A 1 307 ? -94.212  36.454 -25.915 1.00 61.38 ? 307  GLU A CA  1 
ATOM   2276 C C   . GLU A 1 307 ? -94.758  35.634 -27.100 1.00 62.98 ? 307  GLU A C   1 
ATOM   2277 O O   . GLU A 1 307 ? -95.025  36.200 -28.163 1.00 63.12 ? 307  GLU A O   1 
ATOM   2278 C CB  . GLU A 1 307 ? -95.189  36.523 -24.722 1.00 61.24 ? 307  GLU A CB  1 
ATOM   2279 C CG  . GLU A 1 307 ? -96.182  35.377 -24.589 1.00 61.80 ? 307  GLU A CG  1 
ATOM   2280 C CD  . GLU A 1 307 ? -95.748  34.310 -23.595 1.00 62.67 ? 307  GLU A CD  1 
ATOM   2281 O OE1 . GLU A 1 307 ? -95.124  33.304 -24.022 1.00 62.48 ? 307  GLU A OE1 1 
ATOM   2282 O OE2 . GLU A 1 307 ? -96.045  34.473 -22.387 1.00 62.95 ? 307  GLU A OE2 1 
ATOM   2283 N N   . SER A 1 308 ? -94.896  34.316 -26.929 1.00 64.92 ? 308  SER A N   1 
ATOM   2284 C CA  . SER A 1 308 ? -95.439  33.443 -27.976 1.00 66.86 ? 308  SER A CA  1 
ATOM   2285 C C   . SER A 1 308 ? -96.784  33.939 -28.493 1.00 68.26 ? 308  SER A C   1 
ATOM   2286 O O   . SER A 1 308 ? -97.650  34.299 -27.715 1.00 68.36 ? 308  SER A O   1 
ATOM   2287 C CB  . SER A 1 308 ? -95.608  32.003 -27.464 1.00 66.86 ? 308  SER A CB  1 
ATOM   2288 O OG  . SER A 1 308 ? -94.361  31.356 -27.272 1.00 67.23 ? 308  SER A OG  1 
ATOM   2289 N N   . VAL A 1 309 ? -96.943  33.968 -29.810 1.00 70.13 ? 309  VAL A N   1 
ATOM   2290 C CA  . VAL A 1 309 ? -98.251  34.182 -30.428 1.00 72.03 ? 309  VAL A CA  1 
ATOM   2291 C C   . VAL A 1 309 ? -98.727  32.863 -31.034 1.00 73.43 ? 309  VAL A C   1 
ATOM   2292 O O   . VAL A 1 309 ? -99.912  32.697 -31.326 1.00 73.52 ? 309  VAL A O   1 
ATOM   2293 C CB  . VAL A 1 309 ? -98.203  35.291 -31.513 1.00 72.03 ? 309  VAL A CB  1 
ATOM   2294 C CG1 . VAL A 1 309 ? -99.572  35.506 -32.151 1.00 72.02 ? 309  VAL A CG1 1 
ATOM   2295 C CG2 . VAL A 1 309 ? -97.693  36.598 -30.921 1.00 72.23 ? 309  VAL A CG2 1 
ATOM   2296 N N   . SER A 1 310 ? -97.793  31.924 -31.189 1.00 75.23 ? 310  SER A N   1 
ATOM   2297 C CA  . SER A 1 310 ? -98.037  30.659 -31.889 1.00 77.01 ? 310  SER A CA  1 
ATOM   2298 C C   . SER A 1 310 ? -99.056  29.723 -31.221 1.00 78.00 ? 310  SER A C   1 
ATOM   2299 O O   . SER A 1 310 ? -99.721  28.941 -31.905 1.00 78.01 ? 310  SER A O   1 
ATOM   2300 C CB  . SER A 1 310 ? -96.709  29.932 -32.170 1.00 77.21 ? 310  SER A CB  1 
ATOM   2301 O OG  . SER A 1 310 ? -96.523  28.808 -31.322 1.00 77.73 ? 310  SER A OG  1 
ATOM   2302 N N   . TYR A 1 311 ? -99.181  29.801 -29.898 1.00 79.29 ? 311  TYR A N   1 
ATOM   2303 C CA  . TYR A 1 311 ? -100.128 28.951 -29.176 1.00 80.55 ? 311  TYR A CA  1 
ATOM   2304 C C   . TYR A 1 311 ? -101.595 29.370 -29.401 1.00 80.45 ? 311  TYR A C   1 
ATOM   2305 O O   . TYR A 1 311 ? -102.518 28.586 -29.151 1.00 80.51 ? 311  TYR A O   1 
ATOM   2306 C CB  . TYR A 1 311 ? -99.749  28.849 -27.687 1.00 81.41 ? 311  TYR A CB  1 
ATOM   2307 C CG  . TYR A 1 311 ? -100.769 29.400 -26.715 1.00 84.22 ? 311  TYR A CG  1 
ATOM   2308 C CD1 . TYR A 1 311 ? -101.662 28.551 -26.047 1.00 86.19 ? 311  TYR A CD1 1 
ATOM   2309 C CD2 . TYR A 1 311 ? -100.836 30.771 -26.454 1.00 86.41 ? 311  TYR A CD2 1 
ATOM   2310 C CE1 . TYR A 1 311 ? -102.602 29.061 -25.148 1.00 87.73 ? 311  TYR A CE1 1 
ATOM   2311 C CE2 . TYR A 1 311 ? -101.766 31.289 -25.559 1.00 87.89 ? 311  TYR A CE2 1 
ATOM   2312 C CZ  . TYR A 1 311 ? -102.643 30.433 -24.911 1.00 88.61 ? 311  TYR A CZ  1 
ATOM   2313 O OH  . TYR A 1 311 ? -103.558 30.964 -24.030 1.00 89.63 ? 311  TYR A OH  1 
ATOM   2314 N N   . LEU A 1 312 ? -101.792 30.594 -29.896 1.00 80.31 ? 312  LEU A N   1 
ATOM   2315 C CA  . LEU A 1 312 ? -103.116 31.103 -30.261 1.00 80.04 ? 312  LEU A CA  1 
ATOM   2316 C C   . LEU A 1 312 ? -103.715 30.417 -31.494 1.00 79.85 ? 312  LEU A C   1 
ATOM   2317 O O   . LEU A 1 312 ? -104.935 30.461 -31.702 1.00 79.74 ? 312  LEU A O   1 
ATOM   2318 C CB  . LEU A 1 312 ? -103.062 32.612 -30.500 1.00 80.07 ? 312  LEU A CB  1 
ATOM   2319 C CG  . LEU A 1 312 ? -103.120 33.551 -29.293 1.00 80.26 ? 312  LEU A CG  1 
ATOM   2320 C CD1 . LEU A 1 312 ? -103.007 35.002 -29.761 1.00 79.84 ? 312  LEU A CD1 1 
ATOM   2321 C CD2 . LEU A 1 312 ? -104.394 33.331 -28.468 1.00 80.49 ? 312  LEU A CD2 1 
ATOM   2322 N N   . PHE A 1 313 ? -102.855 29.798 -32.306 1.00 79.62 ? 313  PHE A N   1 
ATOM   2323 C CA  . PHE A 1 313 ? -103.276 29.079 -33.517 1.00 79.34 ? 313  PHE A CA  1 
ATOM   2324 C C   . PHE A 1 313 ? -104.057 27.803 -33.174 1.00 79.33 ? 313  PHE A C   1 
ATOM   2325 O O   . PHE A 1 313 ? -104.671 27.184 -34.054 1.00 79.24 ? 313  PHE A O   1 
ATOM   2326 C CB  . PHE A 1 313 ? -102.075 28.723 -34.421 1.00 79.08 ? 313  PHE A CB  1 
ATOM   2327 C CG  . PHE A 1 313 ? -101.167 29.889 -34.756 1.00 78.33 ? 313  PHE A CG  1 
ATOM   2328 C CD1 . PHE A 1 313 ? -99.802  29.675 -34.963 1.00 77.62 ? 313  PHE A CD1 1 
ATOM   2329 C CD2 . PHE A 1 313 ? -101.666 31.189 -34.886 1.00 77.79 ? 313  PHE A CD2 1 
ATOM   2330 C CE1 . PHE A 1 313 ? -98.944  30.732 -35.278 1.00 77.27 ? 313  PHE A CE1 1 
ATOM   2331 C CE2 . PHE A 1 313 ? -100.813 32.259 -35.198 1.00 77.28 ? 313  PHE A CE2 1 
ATOM   2332 C CZ  . PHE A 1 313 ? -99.452  32.028 -35.394 1.00 77.07 ? 313  PHE A CZ  1 
ATOM   2333 N N   . ASN B 1 3   ? -79.405  38.695 -81.196 1.00 43.91 ? 3    ASN B N   1 
ATOM   2334 C CA  . ASN B 1 3   ? -79.138  39.202 -79.827 1.00 43.79 ? 3    ASN B CA  1 
ATOM   2335 C C   . ASN B 1 3   ? -79.894  38.454 -78.707 1.00 43.12 ? 3    ASN B C   1 
ATOM   2336 O O   . ASN B 1 3   ? -79.968  38.922 -77.564 1.00 43.26 ? 3    ASN B O   1 
ATOM   2337 C CB  . ASN B 1 3   ? -79.340  40.727 -79.764 1.00 44.36 ? 3    ASN B CB  1 
ATOM   2338 C CG  . ASN B 1 3   ? -80.801  41.130 -79.674 1.00 46.03 ? 3    ASN B CG  1 
ATOM   2339 O OD1 . ASN B 1 3   ? -81.627  40.685 -80.472 1.00 47.66 ? 3    ASN B OD1 1 
ATOM   2340 N ND2 . ASN B 1 3   ? -81.127  41.989 -78.703 1.00 47.00 ? 3    ASN B ND2 1 
ATOM   2341 N N   . ILE B 1 4   ? -80.440  37.288 -79.049 1.00 42.01 ? 4    ILE B N   1 
ATOM   2342 C CA  . ILE B 1 4   ? -80.869  36.293 -78.062 1.00 40.91 ? 4    ILE B CA  1 
ATOM   2343 C C   . ILE B 1 4   ? -79.710  35.329 -77.749 1.00 39.92 ? 4    ILE B C   1 
ATOM   2344 O O   . ILE B 1 4   ? -78.996  34.878 -78.649 1.00 39.33 ? 4    ILE B O   1 
ATOM   2345 C CB  . ILE B 1 4   ? -82.111  35.518 -78.574 1.00 41.18 ? 4    ILE B CB  1 
ATOM   2346 C CG1 . ILE B 1 4   ? -82.641  34.543 -77.525 1.00 41.14 ? 4    ILE B CG1 1 
ATOM   2347 C CG2 . ILE B 1 4   ? -81.804  34.778 -79.893 1.00 41.86 ? 4    ILE B CG2 1 
ATOM   2348 C CD1 . ILE B 1 4   ? -84.062  34.128 -77.803 1.00 42.32 ? 4    ILE B CD1 1 
ATOM   2349 N N   . LYS B 1 5   ? -79.517  35.038 -76.470 1.00 38.99 ? 5    LYS B N   1 
ATOM   2350 C CA  . LYS B 1 5   ? -78.438  34.162 -76.043 1.00 38.60 ? 5    LYS B CA  1 
ATOM   2351 C C   . LYS B 1 5   ? -78.897  33.220 -74.941 1.00 37.79 ? 5    LYS B C   1 
ATOM   2352 O O   . LYS B 1 5   ? -79.334  33.664 -73.874 1.00 37.62 ? 5    LYS B O   1 
ATOM   2353 C CB  . LYS B 1 5   ? -77.230  34.979 -75.589 1.00 38.88 ? 5    LYS B CB  1 
ATOM   2354 C CG  . LYS B 1 5   ? -75.899  34.446 -76.090 1.00 41.21 ? 5    LYS B CG  1 
ATOM   2355 C CD  . LYS B 1 5   ? -75.799  34.415 -77.630 1.00 44.45 ? 5    LYS B CD  1 
ATOM   2356 C CE  . LYS B 1 5   ? -74.954  35.584 -78.182 1.00 46.37 ? 5    LYS B CE  1 
ATOM   2357 N NZ  . LYS B 1 5   ? -74.742  35.512 -79.670 1.00 47.58 ? 5    LYS B NZ  1 
ATOM   2358 N N   . ILE B 1 6   ? -78.807  31.924 -75.219 1.00 36.95 ? 6    ILE B N   1 
ATOM   2359 C CA  . ILE B 1 6   ? -79.224  30.896 -74.273 1.00 36.38 ? 6    ILE B CA  1 
ATOM   2360 C C   . ILE B 1 6   ? -78.038  30.196 -73.617 1.00 36.03 ? 6    ILE B C   1 
ATOM   2361 O O   . ILE B 1 6   ? -77.117  29.748 -74.291 1.00 35.31 ? 6    ILE B O   1 
ATOM   2362 C CB  . ILE B 1 6   ? -80.217  29.901 -74.925 1.00 36.28 ? 6    ILE B CB  1 
ATOM   2363 C CG1 . ILE B 1 6   ? -81.619  30.483 -74.852 1.00 37.47 ? 6    ILE B CG1 1 
ATOM   2364 C CG2 . ILE B 1 6   ? -80.285  28.592 -74.165 1.00 35.66 ? 6    ILE B CG2 1 
ATOM   2365 C CD1 . ILE B 1 6   ? -82.448  30.276 -76.108 1.00 38.83 ? 6    ILE B CD1 1 
ATOM   2366 N N   . PHE B 1 7   ? -78.082  30.126 -72.291 1.00 36.45 ? 7    PHE B N   1 
ATOM   2367 C CA  . PHE B 1 7   ? -77.049  29.474 -71.502 1.00 37.51 ? 7    PHE B CA  1 
ATOM   2368 C C   . PHE B 1 7   ? -77.606  28.316 -70.671 1.00 39.50 ? 7    PHE B C   1 
ATOM   2369 O O   . PHE B 1 7   ? -78.770  28.319 -70.270 1.00 39.30 ? 7    PHE B O   1 
ATOM   2370 C CB  . PHE B 1 7   ? -76.363  30.484 -70.585 1.00 36.26 ? 7    PHE B CB  1 
ATOM   2371 C CG  . PHE B 1 7   ? -75.400  31.394 -71.285 1.00 33.87 ? 7    PHE B CG  1 
ATOM   2372 C CD1 . PHE B 1 7   ? -75.813  32.627 -71.772 1.00 32.70 ? 7    PHE B CD1 1 
ATOM   2373 C CD2 . PHE B 1 7   ? -74.075  31.042 -71.424 1.00 32.03 ? 7    PHE B CD2 1 
ATOM   2374 C CE1 . PHE B 1 7   ? -74.915  33.479 -72.410 1.00 31.74 ? 7    PHE B CE1 1 
ATOM   2375 C CE2 . PHE B 1 7   ? -73.171  31.883 -72.052 1.00 31.18 ? 7    PHE B CE2 1 
ATOM   2376 C CZ  . PHE B 1 7   ? -73.593  33.106 -72.546 1.00 31.22 ? 7    PHE B CZ  1 
ATOM   2377 N N   . SER B 1 8   ? -76.749  27.342 -70.404 1.00 42.22 ? 8    SER B N   1 
ATOM   2378 C CA  . SER B 1 8   ? -77.101  26.212 -69.577 1.00 45.37 ? 8    SER B CA  1 
ATOM   2379 C C   . SER B 1 8   ? -76.346  26.195 -68.251 1.00 48.17 ? 8    SER B C   1 
ATOM   2380 O O   . SER B 1 8   ? -75.161  26.545 -68.190 1.00 47.78 ? 8    SER B O   1 
ATOM   2381 C CB  . SER B 1 8   ? -76.812  24.925 -70.323 1.00 45.14 ? 8    SER B CB  1 
ATOM   2382 O OG  . SER B 1 8   ? -77.271  23.826 -69.574 1.00 45.33 ? 8    SER B OG  1 
ATOM   2383 N N   . GLY B 1 9   ? -77.057  25.769 -67.202 1.00 51.68 ? 9    GLY B N   1 
ATOM   2384 C CA  . GLY B 1 9   ? -76.494  25.536 -65.877 1.00 55.69 ? 9    GLY B CA  1 
ATOM   2385 C C   . GLY B 1 9   ? -75.201  24.726 -65.870 1.00 58.70 ? 9    GLY B C   1 
ATOM   2386 O O   . GLY B 1 9   ? -74.120  25.278 -66.090 1.00 59.38 ? 9    GLY B O   1 
ATOM   2387 N N   . SER B 1 10  ? -75.297  23.425 -65.608 1.00 61.15 ? 10   SER B N   1 
ATOM   2388 C CA  . SER B 1 10  ? -74.112  22.567 -65.597 1.00 63.51 ? 10   SER B CA  1 
ATOM   2389 C C   . SER B 1 10  ? -74.100  21.648 -66.818 1.00 64.80 ? 10   SER B C   1 
ATOM   2390 O O   . SER B 1 10  ? -74.873  21.854 -67.764 1.00 65.34 ? 10   SER B O   1 
ATOM   2391 C CB  . SER B 1 10  ? -74.038  21.752 -64.293 1.00 63.86 ? 10   SER B CB  1 
ATOM   2392 O OG  . SER B 1 10  ? -74.745  20.522 -64.405 1.00 64.71 ? 10   SER B OG  1 
ATOM   2393 N N   . SER B 1 11  ? -73.237  20.628 -66.782 1.00 65.91 ? 11   SER B N   1 
ATOM   2394 C CA  . SER B 1 11  ? -73.123  19.645 -67.866 1.00 66.70 ? 11   SER B CA  1 
ATOM   2395 C C   . SER B 1 11  ? -74.393  18.807 -68.080 1.00 66.89 ? 11   SER B C   1 
ATOM   2396 O O   . SER B 1 11  ? -74.370  17.808 -68.812 1.00 67.26 ? 11   SER B O   1 
ATOM   2397 C CB  . SER B 1 11  ? -71.913  18.730 -67.651 1.00 66.92 ? 11   SER B CB  1 
ATOM   2398 O OG  . SER B 1 11  ? -71.561  18.096 -68.867 1.00 67.29 ? 11   SER B OG  1 
ATOM   2399 N N   . HIS B 1 12  ? -75.492  19.217 -67.442 1.00 66.69 ? 12   HIS B N   1 
ATOM   2400 C CA  . HIS B 1 12  ? -76.802  18.632 -67.710 1.00 66.24 ? 12   HIS B CA  1 
ATOM   2401 C C   . HIS B 1 12  ? -77.496  19.430 -68.817 1.00 64.97 ? 12   HIS B C   1 
ATOM   2402 O O   . HIS B 1 12  ? -78.631  19.920 -68.657 1.00 64.90 ? 12   HIS B O   1 
ATOM   2403 C CB  . HIS B 1 12  ? -77.628  18.557 -66.431 1.00 67.13 ? 12   HIS B CB  1 
ATOM   2404 C CG  . HIS B 1 12  ? -77.235  17.422 -65.537 1.00 69.44 ? 12   HIS B CG  1 
ATOM   2405 N ND1 . HIS B 1 12  ? -78.062  16.346 -65.291 1.00 71.17 ? 12   HIS B ND1 1 
ATOM   2406 C CD2 . HIS B 1 12  ? -76.092  17.185 -64.847 1.00 70.75 ? 12   HIS B CD2 1 
ATOM   2407 C CE1 . HIS B 1 12  ? -77.449  15.499 -64.482 1.00 71.71 ? 12   HIS B CE1 1 
ATOM   2408 N NE2 . HIS B 1 12  ? -76.253  15.983 -64.199 1.00 71.53 ? 12   HIS B NE2 1 
ATOM   2409 N N   . GLN B 1 13  ? -76.778  19.542 -69.940 1.00 62.99 ? 13   GLN B N   1 
ATOM   2410 C CA  . GLN B 1 13  ? -77.199  20.328 -71.096 1.00 60.87 ? 13   GLN B CA  1 
ATOM   2411 C C   . GLN B 1 13  ? -78.527  19.817 -71.652 1.00 58.44 ? 13   GLN B C   1 
ATOM   2412 O O   . GLN B 1 13  ? -79.448  20.597 -71.855 1.00 58.79 ? 13   GLN B O   1 
ATOM   2413 C CB  . GLN B 1 13  ? -76.113  20.339 -72.182 1.00 61.42 ? 13   GLN B CB  1 
ATOM   2414 C CG  . GLN B 1 13  ? -74.683  20.519 -71.666 1.00 63.15 ? 13   GLN B CG  1 
ATOM   2415 C CD  . GLN B 1 13  ? -74.208  21.965 -71.734 1.00 65.13 ? 13   GLN B CD  1 
ATOM   2416 O OE1 . GLN B 1 13  ? -74.366  22.722 -70.775 1.00 66.10 ? 13   GLN B OE1 1 
ATOM   2417 N NE2 . GLN B 1 13  ? -73.626  22.349 -72.867 1.00 65.71 ? 13   GLN B NE2 1 
ATOM   2418 N N   . ASP B 1 14  ? -78.619  18.510 -71.874 1.00 55.13 ? 14   ASP B N   1 
ATOM   2419 C CA  . ASP B 1 14  ? -79.850  17.846 -72.308 1.00 52.00 ? 14   ASP B CA  1 
ATOM   2420 C C   . ASP B 1 14  ? -81.010  18.764 -72.734 1.00 48.89 ? 14   ASP B C   1 
ATOM   2421 O O   . ASP B 1 14  ? -81.130  19.110 -73.912 1.00 48.53 ? 14   ASP B O   1 
ATOM   2422 C CB  . ASP B 1 14  ? -80.315  16.854 -71.231 1.00 52.79 ? 14   ASP B CB  1 
ATOM   2423 C CG  . ASP B 1 14  ? -81.208  15.741 -71.792 1.00 54.36 ? 14   ASP B CG  1 
ATOM   2424 O OD1 . ASP B 1 14  ? -81.580  15.785 -72.995 1.00 55.36 ? 14   ASP B OD1 1 
ATOM   2425 O OD2 . ASP B 1 14  ? -81.589  14.776 -71.086 1.00 55.71 ? 14   ASP B OD2 1 
ATOM   2426 N N   . LEU B 1 15  ? -81.857  19.139 -71.773 1.00 45.30 ? 15   LEU B N   1 
ATOM   2427 C CA  . LEU B 1 15  ? -83.045  19.964 -72.012 1.00 41.85 ? 15   LEU B CA  1 
ATOM   2428 C C   . LEU B 1 15  ? -82.696  21.316 -72.633 1.00 39.95 ? 15   LEU B C   1 
ATOM   2429 O O   . LEU B 1 15  ? -83.372  21.763 -73.562 1.00 39.34 ? 15   LEU B O   1 
ATOM   2430 C CB  . LEU B 1 15  ? -83.804  20.187 -70.705 1.00 41.23 ? 15   LEU B CB  1 
ATOM   2431 C CG  . LEU B 1 15  ? -85.313  20.459 -70.596 1.00 40.54 ? 15   LEU B CG  1 
ATOM   2432 C CD1 . LEU B 1 15  ? -85.566  21.629 -69.646 1.00 40.02 ? 15   LEU B CD1 1 
ATOM   2433 C CD2 . LEU B 1 15  ? -86.044  20.679 -71.912 1.00 39.27 ? 15   LEU B CD2 1 
ATOM   2434 N N   . SER B 1 16  ? -81.645  21.956 -72.118 1.00 37.68 ? 16   SER B N   1 
ATOM   2435 C CA  . SER B 1 16  ? -81.236  23.263 -72.602 1.00 36.24 ? 16   SER B CA  1 
ATOM   2436 C C   . SER B 1 16  ? -80.715  23.207 -74.046 1.00 35.18 ? 16   SER B C   1 
ATOM   2437 O O   . SER B 1 16  ? -80.915  24.151 -74.817 1.00 34.59 ? 16   SER B O   1 
ATOM   2438 C CB  . SER B 1 16  ? -80.238  23.935 -71.640 1.00 36.21 ? 16   SER B CB  1 
ATOM   2439 O OG  . SER B 1 16  ? -79.086  23.142 -71.417 1.00 35.89 ? 16   SER B OG  1 
ATOM   2440 N N   . GLN B 1 17  ? -80.090  22.085 -74.404 1.00 34.10 ? 17   GLN B N   1 
ATOM   2441 C CA  . GLN B 1 17  ? -79.700  21.806 -75.784 1.00 33.56 ? 17   GLN B CA  1 
ATOM   2442 C C   . GLN B 1 17  ? -80.905  21.632 -76.708 1.00 32.66 ? 17   GLN B C   1 
ATOM   2443 O O   . GLN B 1 17  ? -80.908  22.158 -77.828 1.00 32.52 ? 17   GLN B O   1 
ATOM   2444 C CB  . GLN B 1 17  ? -78.777  20.581 -75.862 1.00 34.05 ? 17   GLN B CB  1 
ATOM   2445 C CG  . GLN B 1 17  ? -78.170  20.307 -77.260 1.00 35.83 ? 17   GLN B CG  1 
ATOM   2446 C CD  . GLN B 1 17  ? -77.536  21.552 -77.915 1.00 38.05 ? 17   GLN B CD  1 
ATOM   2447 O OE1 . GLN B 1 17  ? -76.633  22.183 -77.340 1.00 39.09 ? 17   GLN B OE1 1 
ATOM   2448 N NE2 . GLN B 1 17  ? -78.007  21.898 -79.115 1.00 38.17 ? 17   GLN B NE2 1 
ATOM   2449 N N   . LYS B 1 18  ? -81.922  20.901 -76.249 1.00 31.63 ? 18   LYS B N   1 
ATOM   2450 C CA  . LYS B 1 18  ? -83.144  20.736 -77.037 1.00 31.12 ? 18   LYS B CA  1 
ATOM   2451 C C   . LYS B 1 18  ? -83.825  22.067 -77.293 1.00 30.11 ? 18   LYS B C   1 
ATOM   2452 O O   . LYS B 1 18  ? -84.310  22.316 -78.405 1.00 30.03 ? 18   LYS B O   1 
ATOM   2453 C CB  . LYS B 1 18  ? -84.137  19.777 -76.378 1.00 31.70 ? 18   LYS B CB  1 
ATOM   2454 C CG  . LYS B 1 18  ? -83.663  18.342 -76.282 1.00 33.58 ? 18   LYS B CG  1 
ATOM   2455 C CD  . LYS B 1 18  ? -84.851  17.406 -76.207 1.00 36.46 ? 18   LYS B CD  1 
ATOM   2456 C CE  . LYS B 1 18  ? -84.476  16.069 -75.585 1.00 37.87 ? 18   LYS B CE  1 
ATOM   2457 N NZ  . LYS B 1 18  ? -85.655  15.161 -75.672 1.00 39.06 ? 18   LYS B NZ  1 
ATOM   2458 N N   . ILE B 1 19  ? -83.852  22.921 -76.272 1.00 29.10 ? 19   ILE B N   1 
ATOM   2459 C CA  . ILE B 1 19  ? -84.461  24.244 -76.394 1.00 28.21 ? 19   ILE B CA  1 
ATOM   2460 C C   . ILE B 1 19  ? -83.710  25.056 -77.438 1.00 27.98 ? 19   ILE B C   1 
ATOM   2461 O O   . ILE B 1 19  ? -84.318  25.681 -78.301 1.00 27.68 ? 19   ILE B O   1 
ATOM   2462 C CB  . ILE B 1 19  ? -84.515  24.986 -75.028 1.00 27.62 ? 19   ILE B CB  1 
ATOM   2463 C CG1 . ILE B 1 19  ? -85.438  24.251 -74.049 1.00 26.56 ? 19   ILE B CG1 1 
ATOM   2464 C CG2 . ILE B 1 19  ? -85.016  26.399 -75.224 1.00 27.11 ? 19   ILE B CG2 1 
ATOM   2465 C CD1 . ILE B 1 19  ? -85.130  24.467 -72.580 1.00 24.01 ? 19   ILE B CD1 1 
ATOM   2466 N N   . ALA B 1 20  ? -82.386  25.004 -77.363 1.00 28.29 ? 20   ALA B N   1 
ATOM   2467 C CA  . ALA B 1 20  ? -81.518  25.763 -78.250 1.00 28.82 ? 20   ALA B CA  1 
ATOM   2468 C C   . ALA B 1 20  ? -81.670  25.287 -79.695 1.00 29.53 ? 20   ALA B C   1 
ATOM   2469 O O   . ALA B 1 20  ? -81.831  26.116 -80.594 1.00 29.39 ? 20   ALA B O   1 
ATOM   2470 C CB  . ALA B 1 20  ? -80.091  25.659 -77.793 1.00 28.52 ? 20   ALA B CB  1 
ATOM   2471 N N   . ASP B 1 21  ? -81.650  23.963 -79.908 1.00 30.28 ? 21   ASP B N   1 
ATOM   2472 C CA  . ASP B 1 21  ? -81.937  23.390 -81.223 1.00 31.34 ? 21   ASP B CA  1 
ATOM   2473 C C   . ASP B 1 21  ? -83.248  23.960 -81.772 1.00 31.78 ? 21   ASP B C   1 
ATOM   2474 O O   . ASP B 1 21  ? -83.281  24.444 -82.911 1.00 31.57 ? 21   ASP B O   1 
ATOM   2475 C CB  . ASP B 1 21  ? -82.046  21.858 -81.184 1.00 31.95 ? 21   ASP B CB  1 
ATOM   2476 C CG  . ASP B 1 21  ? -80.728  21.162 -80.827 1.00 33.30 ? 21   ASP B CG  1 
ATOM   2477 O OD1 . ASP B 1 21  ? -79.652  21.794 -80.877 1.00 33.63 ? 21   ASP B OD1 1 
ATOM   2478 O OD2 . ASP B 1 21  ? -80.681  19.964 -80.466 1.00 35.04 ? 21   ASP B OD2 1 
ATOM   2479 N N   . ARG B 1 22  ? -84.313  23.935 -80.963 1.00 32.07 ? 22   ARG B N   1 
ATOM   2480 C CA  . ARG B 1 22  ? -85.624  24.371 -81.457 1.00 32.83 ? 22   ARG B CA  1 
ATOM   2481 C C   . ARG B 1 22  ? -85.639  25.857 -81.841 1.00 32.81 ? 22   ARG B C   1 
ATOM   2482 O O   . ARG B 1 22  ? -86.417  26.274 -82.697 1.00 33.02 ? 22   ARG B O   1 
ATOM   2483 C CB  . ARG B 1 22  ? -86.771  23.971 -80.518 1.00 33.04 ? 22   ARG B CB  1 
ATOM   2484 C CG  . ARG B 1 22  ? -86.890  22.453 -80.358 1.00 34.69 ? 22   ARG B CG  1 
ATOM   2485 C CD  . ARG B 1 22  ? -87.912  21.967 -79.351 1.00 37.57 ? 22   ARG B CD  1 
ATOM   2486 N NE  . ARG B 1 22  ? -89.179  21.655 -80.016 1.00 41.08 ? 22   ARG B NE  1 
ATOM   2487 C CZ  . ARG B 1 22  ? -89.611  20.429 -80.329 1.00 43.04 ? 22   ARG B CZ  1 
ATOM   2488 N NH1 . ARG B 1 22  ? -88.896  19.344 -80.029 1.00 43.56 ? 22   ARG B NH1 1 
ATOM   2489 N NH2 . ARG B 1 22  ? -90.782  20.291 -80.941 1.00 43.95 ? 22   ARG B NH2 1 
ATOM   2490 N N   . LEU B 1 23  ? -84.723  26.628 -81.266 1.00 32.73 ? 23   LEU B N   1 
ATOM   2491 C CA  . LEU B 1 23  ? -84.612  28.053 -81.578 1.00 32.46 ? 23   LEU B CA  1 
ATOM   2492 C C   . LEU B 1 23  ? -83.568  28.372 -82.652 1.00 31.86 ? 23   LEU B C   1 
ATOM   2493 O O   . LEU B 1 23  ? -83.394  29.531 -83.018 1.00 31.61 ? 23   LEU B O   1 
ATOM   2494 C CB  . LEU B 1 23  ? -84.316  28.854 -80.310 1.00 32.64 ? 23   LEU B CB  1 
ATOM   2495 C CG  . LEU B 1 23  ? -85.418  28.942 -79.255 1.00 33.30 ? 23   LEU B CG  1 
ATOM   2496 C CD1 . LEU B 1 23  ? -84.871  29.641 -78.039 1.00 33.50 ? 23   LEU B CD1 1 
ATOM   2497 C CD2 . LEU B 1 23  ? -86.659  29.669 -79.766 1.00 33.44 ? 23   LEU B CD2 1 
ATOM   2498 N N   . GLY B 1 24  ? -82.879  27.343 -83.137 1.00 31.42 ? 24   GLY B N   1 
ATOM   2499 C CA  . GLY B 1 24  ? -81.871  27.481 -84.174 1.00 30.78 ? 24   GLY B CA  1 
ATOM   2500 C C   . GLY B 1 24  ? -80.574  28.051 -83.656 1.00 30.69 ? 24   GLY B C   1 
ATOM   2501 O O   . GLY B 1 24  ? -79.834  28.695 -84.398 1.00 30.90 ? 24   GLY B O   1 
ATOM   2502 N N   . LEU B 1 25  ? -80.293  27.798 -82.378 1.00 30.28 ? 25   LEU B N   1 
ATOM   2503 C CA  . LEU B 1 25  ? -79.158  28.392 -81.694 1.00 29.77 ? 25   LEU B CA  1 
ATOM   2504 C C   . LEU B 1 25  ? -78.207  27.349 -81.125 1.00 29.93 ? 25   LEU B C   1 
ATOM   2505 O O   . LEU B 1 25  ? -78.571  26.177 -80.954 1.00 29.62 ? 25   LEU B O   1 
ATOM   2506 C CB  . LEU B 1 25  ? -79.651  29.300 -80.565 1.00 29.37 ? 25   LEU B CB  1 
ATOM   2507 C CG  . LEU B 1 25  ? -80.535  30.492 -80.961 1.00 29.38 ? 25   LEU B CG  1 
ATOM   2508 C CD1 . LEU B 1 25  ? -81.068  31.152 -79.722 1.00 29.40 ? 25   LEU B CD1 1 
ATOM   2509 C CD2 . LEU B 1 25  ? -79.803  31.520 -81.836 1.00 28.61 ? 25   LEU B CD2 1 
ATOM   2510 N N   . GLU B 1 26  ? -76.987  27.789 -80.836 1.00 30.02 ? 26   GLU B N   1 
ATOM   2511 C CA  . GLU B 1 26  ? -76.092  27.032 -79.964 1.00 30.62 ? 26   GLU B CA  1 
ATOM   2512 C C   . GLU B 1 26  ? -76.110  27.619 -78.552 1.00 30.00 ? 26   GLU B C   1 
ATOM   2513 O O   . GLU B 1 26  ? -76.273  28.831 -78.369 1.00 29.35 ? 26   GLU B O   1 
ATOM   2514 C CB  . GLU B 1 26  ? -74.665  27.018 -80.516 1.00 31.13 ? 26   GLU B CB  1 
ATOM   2515 C CG  . GLU B 1 26  ? -74.625  26.545 -81.961 1.00 34.61 ? 26   GLU B CG  1 
ATOM   2516 C CD  . GLU B 1 26  ? -73.266  26.063 -82.392 1.00 38.79 ? 26   GLU B CD  1 
ATOM   2517 O OE1 . GLU B 1 26  ? -72.247  26.503 -81.797 1.00 41.17 ? 26   GLU B OE1 1 
ATOM   2518 O OE2 . GLU B 1 26  ? -73.221  25.253 -83.343 1.00 40.47 ? 26   GLU B OE2 1 
ATOM   2519 N N   . LEU B 1 27  ? -75.952  26.754 -77.557 1.00 29.59 ? 27   LEU B N   1 
ATOM   2520 C CA  . LEU B 1 27  ? -75.721  27.216 -76.201 1.00 29.28 ? 27   LEU B CA  1 
ATOM   2521 C C   . LEU B 1 27  ? -74.440  28.045 -76.168 1.00 29.58 ? 27   LEU B C   1 
ATOM   2522 O O   . LEU B 1 27  ? -73.447  27.668 -76.778 1.00 28.53 ? 27   LEU B O   1 
ATOM   2523 C CB  . LEU B 1 27  ? -75.643  26.029 -75.245 1.00 28.84 ? 27   LEU B CB  1 
ATOM   2524 C CG  . LEU B 1 27  ? -76.972  25.299 -75.014 1.00 28.26 ? 27   LEU B CG  1 
ATOM   2525 C CD1 . LEU B 1 27  ? -76.732  23.920 -74.426 1.00 27.85 ? 27   LEU B CD1 1 
ATOM   2526 C CD2 . LEU B 1 27  ? -77.911  26.099 -74.122 1.00 27.10 ? 27   LEU B CD2 1 
ATOM   2527 N N   . GLY B 1 28  ? -74.492  29.194 -75.496 1.00 30.79 ? 28   GLY B N   1 
ATOM   2528 C CA  . GLY B 1 28  ? -73.326  30.038 -75.284 1.00 32.59 ? 28   GLY B CA  1 
ATOM   2529 C C   . GLY B 1 28  ? -72.240  29.368 -74.451 1.00 34.56 ? 28   GLY B C   1 
ATOM   2530 O O   . GLY B 1 28  ? -72.525  28.496 -73.613 1.00 34.34 ? 28   GLY B O   1 
ATOM   2531 N N   . LYS B 1 29  ? -70.992  29.761 -74.693 1.00 36.73 ? 29   LYS B N   1 
ATOM   2532 C CA  . LYS B 1 29  ? -69.837  29.203 -73.981 1.00 39.24 ? 29   LYS B CA  1 
ATOM   2533 C C   . LYS B 1 29  ? -69.816  29.623 -72.516 1.00 40.24 ? 29   LYS B C   1 
ATOM   2534 O O   . LYS B 1 29  ? -70.011  30.803 -72.190 1.00 40.03 ? 29   LYS B O   1 
ATOM   2535 C CB  . LYS B 1 29  ? -68.511  29.604 -74.648 1.00 39.85 ? 29   LYS B CB  1 
ATOM   2536 C CG  . LYS B 1 29  ? -68.567  29.685 -76.176 1.00 43.07 ? 29   LYS B CG  1 
ATOM   2537 C CD  . LYS B 1 29  ? -67.167  29.595 -76.829 1.00 46.99 ? 29   LYS B CD  1 
ATOM   2538 C CE  . LYS B 1 29  ? -67.096  30.419 -78.135 1.00 49.63 ? 29   LYS B CE  1 
ATOM   2539 N NZ  . LYS B 1 29  ? -67.696  29.709 -79.327 1.00 50.89 ? 29   LYS B NZ  1 
ATOM   2540 N N   . VAL B 1 30  ? -69.603  28.640 -71.644 1.00 41.80 ? 30   VAL B N   1 
ATOM   2541 C CA  . VAL B 1 30  ? -69.466  28.869 -70.210 1.00 43.64 ? 30   VAL B CA  1 
ATOM   2542 C C   . VAL B 1 30  ? -68.325  28.016 -69.680 1.00 45.45 ? 30   VAL B C   1 
ATOM   2543 O O   . VAL B 1 30  ? -68.342  26.799 -69.830 1.00 45.75 ? 30   VAL B O   1 
ATOM   2544 C CB  . VAL B 1 30  ? -70.750  28.511 -69.406 1.00 43.27 ? 30   VAL B CB  1 
ATOM   2545 C CG1 . VAL B 1 30  ? -70.612  28.953 -67.962 1.00 42.73 ? 30   VAL B CG1 1 
ATOM   2546 C CG2 . VAL B 1 30  ? -71.982  29.132 -70.011 1.00 42.62 ? 30   VAL B CG2 1 
ATOM   2547 N N   . VAL B 1 31  ? -67.351  28.659 -69.046 1.00 47.65 ? 31   VAL B N   1 
ATOM   2548 C CA  . VAL B 1 31  ? -66.243  27.955 -68.412 1.00 50.15 ? 31   VAL B CA  1 
ATOM   2549 C C   . VAL B 1 31  ? -66.541  27.797 -66.927 1.00 51.87 ? 31   VAL B C   1 
ATOM   2550 O O   . VAL B 1 31  ? -66.576  28.778 -66.184 1.00 51.97 ? 31   VAL B O   1 
ATOM   2551 C CB  . VAL B 1 31  ? -64.877  28.686 -68.619 1.00 50.24 ? 31   VAL B CB  1 
ATOM   2552 C CG1 . VAL B 1 31  ? -63.719  27.790 -68.200 1.00 50.54 ? 31   VAL B CG1 1 
ATOM   2553 C CG2 . VAL B 1 31  ? -64.699  29.147 -70.075 1.00 50.21 ? 31   VAL B CG2 1 
ATOM   2554 N N   . THR B 1 32  ? -66.771  26.553 -66.515 1.00 54.17 ? 32   THR B N   1 
ATOM   2555 C CA  . THR B 1 32  ? -67.107  26.217 -65.127 1.00 56.29 ? 32   THR B CA  1 
ATOM   2556 C C   . THR B 1 32  ? -65.973  25.466 -64.436 1.00 57.80 ? 32   THR B C   1 
ATOM   2557 O O   . THR B 1 32  ? -65.701  24.310 -64.765 1.00 58.12 ? 32   THR B O   1 
ATOM   2558 C CB  . THR B 1 32  ? -68.409  25.371 -65.067 1.00 56.28 ? 32   THR B CB  1 
ATOM   2559 O OG1 . THR B 1 32  ? -69.500  26.128 -65.602 1.00 56.36 ? 32   THR B OG1 1 
ATOM   2560 C CG2 . THR B 1 32  ? -68.836  25.120 -63.621 1.00 56.44 ? 32   THR B CG2 1 
ATOM   2561 N N   . LYS B 1 33  ? -65.319  26.122 -63.479 1.00 59.44 ? 33   LYS B N   1 
ATOM   2562 C CA  . LYS B 1 33  ? -64.321  25.461 -62.637 1.00 60.94 ? 33   LYS B CA  1 
ATOM   2563 C C   . LYS B 1 33  ? -64.898  25.252 -61.239 1.00 61.70 ? 33   LYS B C   1 
ATOM   2564 O O   . LYS B 1 33  ? -65.423  26.184 -60.642 1.00 62.02 ? 33   LYS B O   1 
ATOM   2565 C CB  . LYS B 1 33  ? -63.014  26.263 -62.597 1.00 61.25 ? 33   LYS B CB  1 
ATOM   2566 C CG  . LYS B 1 33  ? -62.300  26.417 -63.965 1.00 62.40 ? 33   LYS B CG  1 
ATOM   2567 C CD  . LYS B 1 33  ? -62.381  25.141 -64.826 1.00 63.59 ? 33   LYS B CD  1 
ATOM   2568 C CE  . LYS B 1 33  ? -61.562  25.264 -66.105 1.00 64.31 ? 33   LYS B CE  1 
ATOM   2569 N NZ  . LYS B 1 33  ? -62.075  24.351 -67.170 1.00 64.85 ? 33   LYS B NZ  1 
ATOM   2570 N N   . LYS B 1 34  ? -64.821  24.026 -60.728 1.00 62.56 ? 34   LYS B N   1 
ATOM   2571 C CA  . LYS B 1 34  ? -65.514  23.665 -59.487 1.00 63.27 ? 34   LYS B CA  1 
ATOM   2572 C C   . LYS B 1 34  ? -64.600  23.044 -58.433 1.00 63.43 ? 34   LYS B C   1 
ATOM   2573 O O   . LYS B 1 34  ? -64.114  21.926 -58.607 1.00 63.38 ? 34   LYS B O   1 
ATOM   2574 C CB  . LYS B 1 34  ? -66.664  22.706 -59.804 1.00 63.62 ? 34   LYS B CB  1 
ATOM   2575 C CG  . LYS B 1 34  ? -67.721  22.577 -58.718 1.00 64.58 ? 34   LYS B CG  1 
ATOM   2576 C CD  . LYS B 1 34  ? -69.010  23.298 -59.115 1.00 66.29 ? 34   LYS B CD  1 
ATOM   2577 C CE  . LYS B 1 34  ? -69.691  22.671 -60.338 1.00 67.19 ? 34   LYS B CE  1 
ATOM   2578 N NZ  . LYS B 1 34  ? -71.054  23.237 -60.584 1.00 67.59 ? 34   LYS B NZ  1 
ATOM   2579 N N   . PHE B 1 35  ? -64.378  23.774 -57.340 1.00 63.68 ? 35   PHE B N   1 
ATOM   2580 C CA  . PHE B 1 35  ? -63.620  23.266 -56.196 1.00 63.89 ? 35   PHE B CA  1 
ATOM   2581 C C   . PHE B 1 35  ? -64.313  22.047 -55.563 1.00 63.87 ? 35   PHE B C   1 
ATOM   2582 O O   . PHE B 1 35  ? -65.472  21.750 -55.869 1.00 63.87 ? 35   PHE B O   1 
ATOM   2583 C CB  . PHE B 1 35  ? -63.419  24.369 -55.152 1.00 64.11 ? 35   PHE B CB  1 
ATOM   2584 C CG  . PHE B 1 35  ? -62.647  25.566 -55.658 1.00 65.34 ? 35   PHE B CG  1 
ATOM   2585 C CD1 . PHE B 1 35  ? -63.212  26.842 -55.615 1.00 66.10 ? 35   PHE B CD1 1 
ATOM   2586 C CD2 . PHE B 1 35  ? -61.349  25.426 -56.158 1.00 66.28 ? 35   PHE B CD2 1 
ATOM   2587 C CE1 . PHE B 1 35  ? -62.504  27.965 -56.075 1.00 66.65 ? 35   PHE B CE1 1 
ATOM   2588 C CE2 . PHE B 1 35  ? -60.631  26.540 -56.626 1.00 66.83 ? 35   PHE B CE2 1 
ATOM   2589 C CZ  . PHE B 1 35  ? -61.212  27.813 -56.582 1.00 66.90 ? 35   PHE B CZ  1 
ATOM   2590 N N   . SER B 1 36  ? -63.602  21.339 -54.687 1.00 63.84 ? 36   SER B N   1 
ATOM   2591 C CA  . SER B 1 36  ? -64.138  20.116 -54.070 1.00 63.66 ? 36   SER B CA  1 
ATOM   2592 C C   . SER B 1 36  ? -65.211  20.377 -53.005 1.00 63.06 ? 36   SER B C   1 
ATOM   2593 O O   . SER B 1 36  ? -66.106  19.549 -52.810 1.00 63.10 ? 36   SER B O   1 
ATOM   2594 C CB  . SER B 1 36  ? -63.017  19.262 -53.485 1.00 63.86 ? 36   SER B CB  1 
ATOM   2595 O OG  . SER B 1 36  ? -62.168  20.068 -52.698 1.00 64.81 ? 36   SER B OG  1 
ATOM   2596 N N   . ASN B 1 37  ? -65.126  21.521 -52.325 1.00 62.19 ? 37   ASN B N   1 
ATOM   2597 C CA  . ASN B 1 37  ? -66.178  21.933 -51.395 1.00 61.42 ? 37   ASN B CA  1 
ATOM   2598 C C   . ASN B 1 37  ? -67.427  22.389 -52.154 1.00 60.35 ? 37   ASN B C   1 
ATOM   2599 O O   . ASN B 1 37  ? -68.378  22.901 -51.564 1.00 60.42 ? 37   ASN B O   1 
ATOM   2600 C CB  . ASN B 1 37  ? -65.678  23.028 -50.446 1.00 61.81 ? 37   ASN B CB  1 
ATOM   2601 C CG  . ASN B 1 37  ? -64.777  24.036 -51.139 1.00 63.20 ? 37   ASN B CG  1 
ATOM   2602 O OD1 . ASN B 1 37  ? -63.617  23.739 -51.482 1.00 64.45 ? 37   ASN B OD1 1 
ATOM   2603 N ND2 . ASN B 1 37  ? -65.300  25.236 -51.351 1.00 63.82 ? 37   ASN B ND2 1 
ATOM   2604 N N   . GLN B 1 38  ? -67.399  22.175 -53.468 1.00 58.98 ? 38   GLN B N   1 
ATOM   2605 C CA  . GLN B 1 38  ? -68.473  22.516 -54.404 1.00 57.81 ? 38   GLN B CA  1 
ATOM   2606 C C   . GLN B 1 38  ? -68.599  24.011 -54.692 1.00 56.41 ? 38   GLN B C   1 
ATOM   2607 O O   . GLN B 1 38  ? -69.595  24.444 -55.279 1.00 56.49 ? 38   GLN B O   1 
ATOM   2608 C CB  . GLN B 1 38  ? -69.822  21.915 -53.979 1.00 58.15 ? 38   GLN B CB  1 
ATOM   2609 C CG  . GLN B 1 38  ? -70.057  20.493 -54.467 1.00 59.60 ? 38   GLN B CG  1 
ATOM   2610 C CD  . GLN B 1 38  ? -69.932  20.357 -55.975 1.00 61.48 ? 38   GLN B CD  1 
ATOM   2611 O OE1 . GLN B 1 38  ? -68.937  19.825 -56.479 1.00 62.25 ? 38   GLN B OE1 1 
ATOM   2612 N NE2 . GLN B 1 38  ? -70.936  20.841 -56.699 1.00 62.25 ? 38   GLN B NE2 1 
ATOM   2613 N N   . GLU B 1 39  ? -67.595  24.791 -54.288 1.00 54.54 ? 39   GLU B N   1 
ATOM   2614 C CA  . GLU B 1 39  ? -67.578  26.216 -54.579 1.00 52.76 ? 39   GLU B CA  1 
ATOM   2615 C C   . GLU B 1 39  ? -67.532  26.388 -56.078 1.00 52.06 ? 39   GLU B C   1 
ATOM   2616 O O   . GLU B 1 39  ? -66.595  25.941 -56.734 1.00 51.89 ? 39   GLU B O   1 
ATOM   2617 C CB  . GLU B 1 39  ? -66.388  26.914 -53.932 1.00 52.18 ? 39   GLU B CB  1 
ATOM   2618 C CG  . GLU B 1 39  ? -66.399  28.414 -54.149 1.00 50.80 ? 39   GLU B CG  1 
ATOM   2619 C CD  . GLU B 1 39  ? -65.306  29.145 -53.395 1.00 49.74 ? 39   GLU B CD  1 
ATOM   2620 O OE1 . GLU B 1 39  ? -64.651  30.027 -54.006 1.00 49.38 ? 39   GLU B OE1 1 
ATOM   2621 O OE2 . GLU B 1 39  ? -65.113  28.850 -52.196 1.00 48.73 ? 39   GLU B OE2 1 
ATOM   2622 N N   . THR B 1 40  ? -68.558  27.033 -56.611 1.00 51.33 ? 40   THR B N   1 
ATOM   2623 C CA  . THR B 1 40  ? -68.740  27.110 -58.048 1.00 50.69 ? 40   THR B CA  1 
ATOM   2624 C C   . THR B 1 40  ? -68.110  28.358 -58.634 1.00 50.24 ? 40   THR B C   1 
ATOM   2625 O O   . THR B 1 40  ? -68.354  29.474 -58.174 1.00 49.95 ? 40   THR B O   1 
ATOM   2626 C CB  . THR B 1 40  ? -70.236  27.027 -58.400 1.00 50.71 ? 40   THR B CB  1 
ATOM   2627 O OG1 . THR B 1 40  ? -70.844  25.979 -57.633 1.00 50.37 ? 40   THR B OG1 1 
ATOM   2628 C CG2 . THR B 1 40  ? -70.429  26.578 -59.850 1.00 50.71 ? 40   THR B CG2 1 
ATOM   2629 N N   . CYS B 1 41  ? -67.282  28.145 -59.649 1.00 50.05 ? 41   CYS B N   1 
ATOM   2630 C CA  . CYS B 1 41  ? -66.693  29.229 -60.417 1.00 49.90 ? 41   CYS B CA  1 
ATOM   2631 C C   . CYS B 1 41  ? -67.284  29.184 -61.804 1.00 49.01 ? 41   CYS B C   1 
ATOM   2632 O O   . CYS B 1 41  ? -67.448  28.111 -62.384 1.00 48.98 ? 41   CYS B O   1 
ATOM   2633 C CB  . CYS B 1 41  ? -65.178  29.066 -60.500 1.00 50.39 ? 41   CYS B CB  1 
ATOM   2634 S SG  . CYS B 1 41  ? -64.331  29.521 -58.974 1.00 53.45 ? 41   CYS B SG  1 
ATOM   2635 N N   . VAL B 1 42  ? -67.616  30.355 -62.329 1.00 48.15 ? 42   VAL B N   1 
ATOM   2636 C CA  . VAL B 1 42  ? -68.178  30.460 -63.664 1.00 47.22 ? 42   VAL B CA  1 
ATOM   2637 C C   . VAL B 1 42  ? -67.451  31.539 -64.454 1.00 46.60 ? 42   VAL B C   1 
ATOM   2638 O O   . VAL B 1 42  ? -66.933  32.506 -63.892 1.00 46.48 ? 42   VAL B O   1 
ATOM   2639 C CB  . VAL B 1 42  ? -69.708  30.708 -63.613 1.00 47.19 ? 42   VAL B CB  1 
ATOM   2640 C CG1 . VAL B 1 42  ? -70.240  31.135 -64.958 1.00 47.07 ? 42   VAL B CG1 1 
ATOM   2641 C CG2 . VAL B 1 42  ? -70.439  29.450 -63.148 1.00 47.26 ? 42   VAL B CG2 1 
ATOM   2642 N N   . GLU B 1 43  ? -67.385  31.347 -65.764 1.00 45.93 ? 43   GLU B N   1 
ATOM   2643 C CA  . GLU B 1 43  ? -66.834  32.346 -66.655 1.00 45.40 ? 43   GLU B CA  1 
ATOM   2644 C C   . GLU B 1 43  ? -67.649  32.318 -67.922 1.00 43.79 ? 43   GLU B C   1 
ATOM   2645 O O   . GLU B 1 43  ? -67.676  31.310 -68.625 1.00 43.85 ? 43   GLU B O   1 
ATOM   2646 C CB  . GLU B 1 43  ? -65.370  32.045 -66.974 1.00 46.42 ? 43   GLU B CB  1 
ATOM   2647 C CG  . GLU B 1 43  ? -64.415  33.187 -66.666 1.00 50.02 ? 43   GLU B CG  1 
ATOM   2648 C CD  . GLU B 1 43  ? -62.949  32.786 -66.825 1.00 54.55 ? 43   GLU B CD  1 
ATOM   2649 O OE1 . GLU B 1 43  ? -62.253  33.414 -67.669 1.00 56.33 ? 43   GLU B OE1 1 
ATOM   2650 O OE2 . GLU B 1 43  ? -62.492  31.852 -66.106 1.00 55.81 ? 43   GLU B OE2 1 
ATOM   2651 N N   . ILE B 1 44  ? -68.312  33.429 -68.211 1.00 41.83 ? 44   ILE B N   1 
ATOM   2652 C CA  . ILE B 1 44  ? -69.077  33.560 -69.440 1.00 39.73 ? 44   ILE B CA  1 
ATOM   2653 C C   . ILE B 1 44  ? -68.105  33.738 -70.601 1.00 38.52 ? 44   ILE B C   1 
ATOM   2654 O O   . ILE B 1 44  ? -67.413  34.749 -70.694 1.00 38.52 ? 44   ILE B O   1 
ATOM   2655 C CB  . ILE B 1 44  ? -70.085  34.729 -69.324 1.00 39.50 ? 44   ILE B CB  1 
ATOM   2656 C CG1 . ILE B 1 44  ? -70.915  34.601 -68.033 1.00 38.87 ? 44   ILE B CG1 1 
ATOM   2657 C CG2 . ILE B 1 44  ? -70.977  34.804 -70.558 1.00 39.24 ? 44   ILE B CG2 1 
ATOM   2658 C CD1 . ILE B 1 44  ? -71.769  33.315 -67.917 1.00 37.60 ? 44   ILE B CD1 1 
ATOM   2659 N N   . GLY B 1 45  ? -68.047  32.734 -71.472 1.00 37.01 ? 45   GLY B N   1 
ATOM   2660 C CA  . GLY B 1 45  ? -67.044  32.676 -72.520 1.00 35.51 ? 45   GLY B CA  1 
ATOM   2661 C C   . GLY B 1 45  ? -67.304  33.488 -73.777 1.00 34.60 ? 45   GLY B C   1 
ATOM   2662 O O   . GLY B 1 45  ? -66.635  33.286 -74.786 1.00 34.97 ? 45   GLY B O   1 
ATOM   2663 N N   . GLU B 1 46  ? -68.274  34.394 -73.727 1.00 33.41 ? 46   GLU B N   1 
ATOM   2664 C CA  . GLU B 1 46  ? -68.590  35.286 -74.844 1.00 31.97 ? 46   GLU B CA  1 
ATOM   2665 C C   . GLU B 1 46  ? -69.297  36.508 -74.297 1.00 30.67 ? 46   GLU B C   1 
ATOM   2666 O O   . GLU B 1 46  ? -69.862  36.467 -73.208 1.00 30.25 ? 46   GLU B O   1 
ATOM   2667 C CB  . GLU B 1 46  ? -69.477  34.598 -75.897 1.00 32.13 ? 46   GLU B CB  1 
ATOM   2668 C CG  . GLU B 1 46  ? -70.678  33.859 -75.317 1.00 33.35 ? 46   GLU B CG  1 
ATOM   2669 C CD  . GLU B 1 46  ? -71.378  32.993 -76.344 1.00 34.94 ? 46   GLU B CD  1 
ATOM   2670 O OE1 . GLU B 1 46  ? -72.272  33.515 -77.048 1.00 36.14 ? 46   GLU B OE1 1 
ATOM   2671 O OE2 . GLU B 1 46  ? -71.029  31.794 -76.452 1.00 35.08 ? 46   GLU B OE2 1 
ATOM   2672 N N   . SER B 1 47  ? -69.263  37.592 -75.065 1.00 29.53 ? 47   SER B N   1 
ATOM   2673 C CA  . SER B 1 47  ? -69.909  38.842 -74.687 1.00 28.24 ? 47   SER B CA  1 
ATOM   2674 C C   . SER B 1 47  ? -71.422  38.680 -74.641 1.00 27.59 ? 47   SER B C   1 
ATOM   2675 O O   . SER B 1 47  ? -72.007  38.147 -75.581 1.00 28.07 ? 47   SER B O   1 
ATOM   2676 C CB  . SER B 1 47  ? -69.557  39.930 -75.688 1.00 27.84 ? 47   SER B CB  1 
ATOM   2677 O OG  . SER B 1 47  ? -70.225  41.135 -75.369 1.00 27.08 ? 47   SER B OG  1 
ATOM   2678 N N   . VAL B 1 48  ? -72.044  39.130 -73.552 1.00 26.39 ? 48   VAL B N   1 
ATOM   2679 C CA  . VAL B 1 48  ? -73.504  39.260 -73.492 1.00 25.28 ? 48   VAL B CA  1 
ATOM   2680 C C   . VAL B 1 48  ? -73.951  40.731 -73.490 1.00 25.18 ? 48   VAL B C   1 
ATOM   2681 O O   . VAL B 1 48  ? -75.134  41.031 -73.286 1.00 24.92 ? 48   VAL B O   1 
ATOM   2682 C CB  . VAL B 1 48  ? -74.101  38.535 -72.269 1.00 24.86 ? 48   VAL B CB  1 
ATOM   2683 C CG1 . VAL B 1 48  ? -73.874  37.024 -72.380 1.00 24.29 ? 48   VAL B CG1 1 
ATOM   2684 C CG2 . VAL B 1 48  ? -73.551  39.116 -70.952 1.00 23.61 ? 48   VAL B CG2 1 
ATOM   2685 N N   . ARG B 1 49  ? -73.004  41.639 -73.719 1.00 24.95 ? 49   ARG B N   1 
ATOM   2686 C CA  . ARG B 1 49  ? -73.275  43.073 -73.685 1.00 25.53 ? 49   ARG B CA  1 
ATOM   2687 C C   . ARG B 1 49  ? -74.447  43.454 -74.596 1.00 25.86 ? 49   ARG B C   1 
ATOM   2688 O O   . ARG B 1 49  ? -74.416  43.218 -75.786 1.00 25.70 ? 49   ARG B O   1 
ATOM   2689 C CB  . ARG B 1 49  ? -72.018  43.841 -74.077 1.00 25.40 ? 49   ARG B CB  1 
ATOM   2690 C CG  . ARG B 1 49  ? -72.131  45.332 -73.929 1.00 25.25 ? 49   ARG B CG  1 
ATOM   2691 C CD  . ARG B 1 49  ? -70.800  46.061 -74.089 1.00 24.91 ? 49   ARG B CD  1 
ATOM   2692 N NE  . ARG B 1 49  ? -69.788  45.640 -73.120 1.00 23.53 ? 49   ARG B NE  1 
ATOM   2693 C CZ  . ARG B 1 49  ? -69.629  46.189 -71.918 1.00 23.13 ? 49   ARG B CZ  1 
ATOM   2694 N NH1 . ARG B 1 49  ? -70.412  47.178 -71.520 1.00 24.33 ? 49   ARG B NH1 1 
ATOM   2695 N NH2 . ARG B 1 49  ? -68.680  45.758 -71.112 1.00 22.72 ? 49   ARG B NH2 1 
ATOM   2696 N N   . GLY B 1 50  ? -75.497  44.013 -74.015 1.00 26.62 ? 50   GLY B N   1 
ATOM   2697 C CA  . GLY B 1 50  ? -76.657  44.417 -74.781 1.00 27.34 ? 50   GLY B CA  1 
ATOM   2698 C C   . GLY B 1 50  ? -77.532  43.281 -75.271 1.00 28.12 ? 50   GLY B C   1 
ATOM   2699 O O   . GLY B 1 50  ? -78.425  43.496 -76.083 1.00 28.63 ? 50   GLY B O   1 
ATOM   2700 N N   . GLU B 1 51  ? -77.323  42.069 -74.773 1.00 28.58 ? 51   GLU B N   1 
ATOM   2701 C CA  . GLU B 1 51  ? -78.114  40.955 -75.276 1.00 29.08 ? 51   GLU B CA  1 
ATOM   2702 C C   . GLU B 1 51  ? -79.229  40.449 -74.354 1.00 28.40 ? 51   GLU B C   1 
ATOM   2703 O O   . GLU B 1 51  ? -79.172  40.618 -73.135 1.00 28.11 ? 51   GLU B O   1 
ATOM   2704 C CB  . GLU B 1 51  ? -77.200  39.837 -75.731 1.00 30.05 ? 51   GLU B CB  1 
ATOM   2705 C CG  . GLU B 1 51  ? -76.660  40.118 -77.120 1.00 34.16 ? 51   GLU B CG  1 
ATOM   2706 C CD  . GLU B 1 51  ? -75.380  39.375 -77.406 1.00 40.21 ? 51   GLU B CD  1 
ATOM   2707 O OE1 . GLU B 1 51  ? -74.659  39.788 -78.346 1.00 43.19 ? 51   GLU B OE1 1 
ATOM   2708 O OE2 . GLU B 1 51  ? -75.102  38.371 -76.705 1.00 42.60 ? 51   GLU B OE2 1 
ATOM   2709 N N   . ASP B 1 52  ? -80.255  39.864 -74.980 1.00 27.58 ? 52   ASP B N   1 
ATOM   2710 C CA  . ASP B 1 52  ? -81.362  39.206 -74.307 1.00 26.84 ? 52   ASP B CA  1 
ATOM   2711 C C   . ASP B 1 52  ? -80.948  37.779 -73.914 1.00 26.06 ? 52   ASP B C   1 
ATOM   2712 O O   . ASP B 1 52  ? -80.911  36.876 -74.760 1.00 26.00 ? 52   ASP B O   1 
ATOM   2713 C CB  . ASP B 1 52  ? -82.569  39.169 -75.249 1.00 27.29 ? 52   ASP B CB  1 
ATOM   2714 C CG  . ASP B 1 52  ? -83.882  38.907 -74.526 1.00 28.58 ? 52   ASP B CG  1 
ATOM   2715 O OD1 . ASP B 1 52  ? -84.014  39.319 -73.349 1.00 29.65 ? 52   ASP B OD1 1 
ATOM   2716 O OD2 . ASP B 1 52  ? -84.845  38.309 -75.063 1.00 29.02 ? 52   ASP B OD2 1 
ATOM   2717 N N   . VAL B 1 53  ? -80.649  37.588 -72.628 1.00 24.91 ? 53   VAL B N   1 
ATOM   2718 C CA  . VAL B 1 53  ? -80.055  36.349 -72.110 1.00 23.93 ? 53   VAL B CA  1 
ATOM   2719 C C   . VAL B 1 53  ? -81.055  35.470 -71.344 1.00 23.68 ? 53   VAL B C   1 
ATOM   2720 O O   . VAL B 1 53  ? -81.841  35.971 -70.547 1.00 23.79 ? 53   VAL B O   1 
ATOM   2721 C CB  . VAL B 1 53  ? -78.848  36.679 -71.186 1.00 23.60 ? 53   VAL B CB  1 
ATOM   2722 C CG1 . VAL B 1 53  ? -78.350  35.437 -70.403 1.00 22.38 ? 53   VAL B CG1 1 
ATOM   2723 C CG2 . VAL B 1 53  ? -77.728  37.318 -71.996 1.00 23.56 ? 53   VAL B CG2 1 
ATOM   2724 N N   . TYR B 1 54  ? -80.990  34.163 -71.584 1.00 23.45 ? 54   TYR B N   1 
ATOM   2725 C CA  . TYR B 1 54  ? -81.827  33.164 -70.921 1.00 23.32 ? 54   TYR B CA  1 
ATOM   2726 C C   . TYR B 1 54  ? -80.915  32.099 -70.351 1.00 24.00 ? 54   TYR B C   1 
ATOM   2727 O O   . TYR B 1 54  ? -80.109  31.531 -71.075 1.00 23.58 ? 54   TYR B O   1 
ATOM   2728 C CB  . TYR B 1 54  ? -82.804  32.538 -71.926 1.00 22.91 ? 54   TYR B CB  1 
ATOM   2729 C CG  . TYR B 1 54  ? -83.750  33.556 -72.501 1.00 21.80 ? 54   TYR B CG  1 
ATOM   2730 C CD1 . TYR B 1 54  ? -83.359  34.370 -73.567 1.00 21.42 ? 54   TYR B CD1 1 
ATOM   2731 C CD2 . TYR B 1 54  ? -85.027  33.739 -71.955 1.00 20.94 ? 54   TYR B CD2 1 
ATOM   2732 C CE1 . TYR B 1 54  ? -84.220  35.337 -74.091 1.00 21.43 ? 54   TYR B CE1 1 
ATOM   2733 C CE2 . TYR B 1 54  ? -85.891  34.703 -72.458 1.00 20.78 ? 54   TYR B CE2 1 
ATOM   2734 C CZ  . TYR B 1 54  ? -85.484  35.499 -73.530 1.00 21.03 ? 54   TYR B CZ  1 
ATOM   2735 O OH  . TYR B 1 54  ? -86.335  36.456 -74.041 1.00 20.36 ? 54   TYR B OH  1 
ATOM   2736 N N   . ILE B 1 55  ? -80.995  31.875 -69.041 1.00 25.18 ? 55   ILE B N   1 
ATOM   2737 C CA  . ILE B 1 55  ? -80.241  30.811 -68.398 1.00 26.50 ? 55   ILE B CA  1 
ATOM   2738 C C   . ILE B 1 55  ? -81.187  29.704 -67.942 1.00 28.23 ? 55   ILE B C   1 
ATOM   2739 O O   . ILE B 1 55  ? -82.096  29.935 -67.148 1.00 27.86 ? 55   ILE B O   1 
ATOM   2740 C CB  . ILE B 1 55  ? -79.397  31.336 -67.211 1.00 26.20 ? 55   ILE B CB  1 
ATOM   2741 C CG1 . ILE B 1 55  ? -78.504  32.496 -67.652 1.00 25.22 ? 55   ILE B CG1 1 
ATOM   2742 C CG2 . ILE B 1 55  ? -78.570  30.175 -66.554 1.00 25.12 ? 55   ILE B CG2 1 
ATOM   2743 C CD1 . ILE B 1 55  ? -78.186  33.429 -66.525 1.00 24.72 ? 55   ILE B CD1 1 
ATOM   2744 N N   . VAL B 1 56  ? -80.968  28.513 -68.486 1.00 30.79 ? 56   VAL B N   1 
ATOM   2745 C CA  . VAL B 1 56  ? -81.741  27.321 -68.144 1.00 33.33 ? 56   VAL B CA  1 
ATOM   2746 C C   . VAL B 1 56  ? -81.004  26.583 -67.026 1.00 35.75 ? 56   VAL B C   1 
ATOM   2747 O O   . VAL B 1 56  ? -79.842  26.177 -67.195 1.00 35.81 ? 56   VAL B O   1 
ATOM   2748 C CB  . VAL B 1 56  ? -81.978  26.414 -69.394 1.00 32.91 ? 56   VAL B CB  1 
ATOM   2749 C CG1 . VAL B 1 56  ? -82.889  25.239 -69.058 1.00 32.59 ? 56   VAL B CG1 1 
ATOM   2750 C CG2 . VAL B 1 56  ? -82.592  27.218 -70.533 1.00 32.26 ? 56   VAL B CG2 1 
ATOM   2751 N N   . GLN B 1 57  ? -81.666  26.455 -65.878 1.00 38.81 ? 57   GLN B N   1 
ATOM   2752 C CA  . GLN B 1 57  ? -81.080  25.808 -64.701 1.00 42.09 ? 57   GLN B CA  1 
ATOM   2753 C C   . GLN B 1 57  ? -80.910  24.319 -64.932 1.00 43.95 ? 57   GLN B C   1 
ATOM   2754 O O   . GLN B 1 57  ? -81.783  23.670 -65.531 1.00 44.31 ? 57   GLN B O   1 
ATOM   2755 C CB  . GLN B 1 57  ? -81.940  26.032 -63.449 1.00 42.56 ? 57   GLN B CB  1 
ATOM   2756 C CG  . GLN B 1 57  ? -81.337  25.444 -62.153 1.00 44.55 ? 57   GLN B CG  1 
ATOM   2757 C CD  . GLN B 1 57  ? -82.373  25.235 -61.054 1.00 47.62 ? 57   GLN B CD  1 
ATOM   2758 O OE1 . GLN B 1 57  ? -83.153  24.268 -61.081 1.00 48.59 ? 57   GLN B OE1 1 
ATOM   2759 N NE2 . GLN B 1 57  ? -82.386  26.140 -60.082 1.00 48.97 ? 57   GLN B NE2 1 
ATOM   2760 N N   . SER B 1 58  ? -79.792  23.791 -64.429 1.00 46.14 ? 58   SER B N   1 
ATOM   2761 C CA  . SER B 1 58  ? -79.402  22.389 -64.613 1.00 48.32 ? 58   SER B CA  1 
ATOM   2762 C C   . SER B 1 58  ? -80.382  21.378 -64.021 1.00 49.50 ? 58   SER B C   1 
ATOM   2763 O O   . SER B 1 58  ? -81.162  21.696 -63.114 1.00 50.00 ? 58   SER B O   1 
ATOM   2764 C CB  . SER B 1 58  ? -78.011  22.145 -64.020 1.00 48.54 ? 58   SER B CB  1 
ATOM   2765 O OG  . SER B 1 58  ? -77.142  21.585 -64.985 1.00 49.06 ? 58   SER B OG  1 
ATOM   2766 N N   . GLY B 1 59  ? -80.338  20.160 -64.547 1.00 50.57 ? 59   GLY B N   1 
ATOM   2767 C CA  . GLY B 1 59  ? -81.056  19.050 -63.945 1.00 51.73 ? 59   GLY B CA  1 
ATOM   2768 C C   . GLY B 1 59  ? -80.124  18.115 -63.196 1.00 52.40 ? 59   GLY B C   1 
ATOM   2769 O O   . GLY B 1 59  ? -80.475  16.950 -62.964 1.00 52.56 ? 59   GLY B O   1 
ATOM   2770 N N   . CYS B 1 60  ? -78.949  18.639 -62.811 1.00 52.74 ? 60   CYS B N   1 
ATOM   2771 C CA  . CYS B 1 60  ? -77.877  17.887 -62.118 1.00 52.69 ? 60   CYS B CA  1 
ATOM   2772 C C   . CYS B 1 60  ? -78.333  17.009 -60.957 1.00 51.39 ? 60   CYS B C   1 
ATOM   2773 O O   . CYS B 1 60  ? -77.832  15.887 -60.787 1.00 51.73 ? 60   CYS B O   1 
ATOM   2774 C CB  . CYS B 1 60  ? -76.768  18.822 -61.622 1.00 53.49 ? 60   CYS B CB  1 
ATOM   2775 S SG  . CYS B 1 60  ? -76.164  18.418 -59.951 1.00 57.14 ? 60   CYS B SG  1 
ATOM   2776 N N   . GLY B 1 61  ? -79.257  17.541 -60.157 1.00 49.62 ? 61   GLY B N   1 
ATOM   2777 C CA  . GLY B 1 61  ? -79.816  16.828 -59.028 1.00 47.13 ? 61   GLY B CA  1 
ATOM   2778 C C   . GLY B 1 61  ? -79.627  17.591 -57.740 1.00 45.01 ? 61   GLY B C   1 
ATOM   2779 O O   . GLY B 1 61  ? -80.616  17.899 -57.065 1.00 45.41 ? 61   GLY B O   1 
ATOM   2780 N N   . GLU B 1 62  ? -78.373  17.900 -57.395 1.00 42.43 ? 62   GLU B N   1 
ATOM   2781 C CA  . GLU B 1 62  ? -78.091  18.641 -56.162 1.00 39.66 ? 62   GLU B CA  1 
ATOM   2782 C C   . GLU B 1 62  ? -78.631  20.060 -56.276 1.00 37.52 ? 62   GLU B C   1 
ATOM   2783 O O   . GLU B 1 62  ? -78.058  20.901 -56.962 1.00 36.87 ? 62   GLU B O   1 
ATOM   2784 C CB  . GLU B 1 62  ? -76.598  18.644 -55.824 1.00 39.62 ? 62   GLU B CB  1 
ATOM   2785 C CG  . GLU B 1 62  ? -76.310  18.391 -54.349 1.00 39.77 ? 62   GLU B CG  1 
ATOM   2786 C CD  . GLU B 1 62  ? -76.429  19.626 -53.447 1.00 40.60 ? 62   GLU B CD  1 
ATOM   2787 O OE1 . GLU B 1 62  ? -76.993  20.677 -53.843 1.00 41.17 ? 62   GLU B OE1 1 
ATOM   2788 O OE2 . GLU B 1 62  ? -75.949  19.544 -52.306 1.00 40.44 ? 62   GLU B OE2 1 
ATOM   2789 N N   . ILE B 1 63  ? -79.748  20.296 -55.593 1.00 35.54 ? 63   ILE B N   1 
ATOM   2790 C CA  . ILE B 1 63  ? -80.531  21.529 -55.713 1.00 33.77 ? 63   ILE B CA  1 
ATOM   2791 C C   . ILE B 1 63  ? -79.782  22.805 -55.318 1.00 32.64 ? 63   ILE B C   1 
ATOM   2792 O O   . ILE B 1 63  ? -79.860  23.815 -56.013 1.00 32.75 ? 63   ILE B O   1 
ATOM   2793 C CB  . ILE B 1 63  ? -81.872  21.397 -54.945 1.00 33.70 ? 63   ILE B CB  1 
ATOM   2794 C CG1 . ILE B 1 63  ? -82.831  22.524 -55.341 1.00 33.87 ? 63   ILE B CG1 1 
ATOM   2795 C CG2 . ILE B 1 63  ? -81.651  21.322 -53.437 1.00 33.09 ? 63   ILE B CG2 1 
ATOM   2796 C CD1 . ILE B 1 63  ? -84.187  22.482 -54.614 1.00 33.78 ? 63   ILE B CD1 1 
ATOM   2797 N N   . ASN B 1 64  ? -79.039  22.748 -54.219 1.00 31.05 ? 64   ASN B N   1 
ATOM   2798 C CA  . ASN B 1 64  ? -78.320  23.909 -53.756 1.00 29.37 ? 64   ASN B CA  1 
ATOM   2799 C C   . ASN B 1 64  ? -77.156  24.262 -54.683 1.00 28.66 ? 64   ASN B C   1 
ATOM   2800 O O   . ASN B 1 64  ? -76.923  25.447 -54.945 1.00 28.80 ? 64   ASN B O   1 
ATOM   2801 C CB  . ASN B 1 64  ? -77.912  23.753 -52.286 1.00 28.97 ? 64   ASN B CB  1 
ATOM   2802 C CG  . ASN B 1 64  ? -79.117  23.560 -51.365 1.00 28.25 ? 64   ASN B CG  1 
ATOM   2803 O OD1 . ASN B 1 64  ? -79.038  22.858 -50.371 1.00 29.09 ? 64   ASN B OD1 1 
ATOM   2804 N ND2 . ASN B 1 64  ? -80.234  24.181 -51.702 1.00 26.92 ? 64   ASN B ND2 1 
ATOM   2805 N N   . ASP B 1 65  ? -76.459  23.258 -55.213 1.00 27.60 ? 65   ASP B N   1 
ATOM   2806 C CA  . ASP B 1 65  ? -75.404  23.528 -56.208 1.00 27.09 ? 65   ASP B CA  1 
ATOM   2807 C C   . ASP B 1 65  ? -75.977  24.196 -57.432 1.00 26.86 ? 65   ASP B C   1 
ATOM   2808 O O   . ASP B 1 65  ? -75.429  25.198 -57.904 1.00 27.06 ? 65   ASP B O   1 
ATOM   2809 C CB  . ASP B 1 65  ? -74.656  22.270 -56.655 1.00 26.68 ? 65   ASP B CB  1 
ATOM   2810 C CG  . ASP B 1 65  ? -73.936  21.596 -55.533 1.00 25.95 ? 65   ASP B CG  1 
ATOM   2811 O OD1 . ASP B 1 65  ? -73.591  22.258 -54.528 1.00 22.91 ? 65   ASP B OD1 1 
ATOM   2812 O OD2 . ASP B 1 65  ? -73.679  20.382 -55.585 1.00 27.41 ? 65   ASP B OD2 1 
ATOM   2813 N N   . ASN B 1 66  ? -77.076  23.626 -57.928 1.00 26.59 ? 66   ASN B N   1 
ATOM   2814 C CA  . ASN B 1 66  ? -77.794  24.115 -59.100 1.00 26.35 ? 66   ASN B CA  1 
ATOM   2815 C C   . ASN B 1 66  ? -78.289  25.528 -58.895 1.00 25.58 ? 66   ASN B C   1 
ATOM   2816 O O   . ASN B 1 66  ? -78.123  26.367 -59.779 1.00 25.66 ? 66   ASN B O   1 
ATOM   2817 C CB  . ASN B 1 66  ? -78.980  23.199 -59.430 1.00 26.81 ? 66   ASN B CB  1 
ATOM   2818 C CG  . ASN B 1 66  ? -78.547  21.906 -60.121 1.00 29.13 ? 66   ASN B CG  1 
ATOM   2819 O OD1 . ASN B 1 66  ? -77.442  21.821 -60.692 1.00 29.89 ? 66   ASN B OD1 1 
ATOM   2820 N ND2 . ASN B 1 66  ? -79.419  20.880 -60.066 1.00 30.74 ? 66   ASN B ND2 1 
ATOM   2821 N N   . LEU B 1 67  ? -78.879  25.792 -57.730 1.00 24.63 ? 67   LEU B N   1 
ATOM   2822 C CA  . LEU B 1 67  ? -79.376  27.127 -57.427 1.00 24.40 ? 67   LEU B CA  1 
ATOM   2823 C C   . LEU B 1 67  ? -78.245  28.165 -57.425 1.00 24.65 ? 67   LEU B C   1 
ATOM   2824 O O   . LEU B 1 67  ? -78.376  29.223 -58.054 1.00 24.46 ? 67   LEU B O   1 
ATOM   2825 C CB  . LEU B 1 67  ? -80.144  27.158 -56.102 1.00 23.87 ? 67   LEU B CB  1 
ATOM   2826 C CG  . LEU B 1 67  ? -80.715  28.488 -55.617 1.00 22.99 ? 67   LEU B CG  1 
ATOM   2827 C CD1 . LEU B 1 67  ? -81.707  29.067 -56.606 1.00 22.44 ? 67   LEU B CD1 1 
ATOM   2828 C CD2 . LEU B 1 67  ? -81.393  28.275 -54.300 1.00 22.91 ? 67   LEU B CD2 1 
ATOM   2829 N N   . MET B 1 68  ? -77.139  27.856 -56.745 1.00 24.58 ? 68   MET B N   1 
ATOM   2830 C CA  . MET B 1 68  ? -76.044  28.796 -56.678 1.00 25.13 ? 68   MET B CA  1 
ATOM   2831 C C   . MET B 1 68  ? -75.445  29.002 -58.060 1.00 25.35 ? 68   MET B C   1 
ATOM   2832 O O   . MET B 1 68  ? -75.178  30.142 -58.469 1.00 24.86 ? 68   MET B O   1 
ATOM   2833 C CB  . MET B 1 68  ? -75.000  28.354 -55.663 1.00 25.81 ? 68   MET B CB  1 
ATOM   2834 C CG  . MET B 1 68  ? -75.527  28.348 -54.231 1.00 27.78 ? 68   MET B CG  1 
ATOM   2835 S SD  . MET B 1 68  ? -76.022  30.019 -53.707 1.00 31.86 ? 68   MET B SD  1 
ATOM   2836 C CE  . MET B 1 68  ? -74.459  31.025 -54.284 1.00 29.83 ? 68   MET B CE  1 
ATOM   2837 N N   . GLU B 1 69  ? -75.278  27.907 -58.803 1.00 25.54 ? 69   GLU B N   1 
ATOM   2838 C CA  . GLU B 1 69  ? -74.785  28.031 -60.167 1.00 25.81 ? 69   GLU B CA  1 
ATOM   2839 C C   . GLU B 1 69  ? -75.670  28.994 -60.980 1.00 24.66 ? 69   GLU B C   1 
ATOM   2840 O O   . GLU B 1 69  ? -75.162  29.913 -61.618 1.00 24.90 ? 69   GLU B O   1 
ATOM   2841 C CB  . GLU B 1 69  ? -74.638  26.681 -60.859 1.00 26.67 ? 69   GLU B CB  1 
ATOM   2842 C CG  . GLU B 1 69  ? -73.955  26.841 -62.207 1.00 30.72 ? 69   GLU B CG  1 
ATOM   2843 C CD  . GLU B 1 69  ? -73.668  25.539 -62.936 1.00 35.51 ? 69   GLU B CD  1 
ATOM   2844 O OE1 . GLU B 1 69  ? -74.483  24.587 -62.862 1.00 37.13 ? 69   GLU B OE1 1 
ATOM   2845 O OE2 . GLU B 1 69  ? -72.615  25.488 -63.609 1.00 37.62 ? 69   GLU B OE2 1 
ATOM   2846 N N   . LEU B 1 70  ? -76.984  28.794 -60.917 1.00 23.08 ? 70   LEU B N   1 
ATOM   2847 C CA  . LEU B 1 70  ? -77.941  29.685 -61.563 1.00 21.70 ? 70   LEU B CA  1 
ATOM   2848 C C   . LEU B 1 70  ? -77.750  31.137 -61.108 1.00 21.30 ? 70   LEU B C   1 
ATOM   2849 O O   . LEU B 1 70  ? -77.605  32.045 -61.933 1.00 21.40 ? 70   LEU B O   1 
ATOM   2850 C CB  . LEU B 1 70  ? -79.371  29.207 -61.265 1.00 20.91 ? 70   LEU B CB  1 
ATOM   2851 C CG  . LEU B 1 70  ? -80.588  30.010 -61.723 1.00 20.14 ? 70   LEU B CG  1 
ATOM   2852 C CD1 . LEU B 1 70  ? -80.580  30.333 -63.227 1.00 19.23 ? 70   LEU B CD1 1 
ATOM   2853 C CD2 . LEU B 1 70  ? -81.820  29.216 -61.378 1.00 19.54 ? 70   LEU B CD2 1 
ATOM   2854 N N   . LEU B 1 71  ? -77.731  31.350 -59.794 1.00 20.69 ? 71   LEU B N   1 
ATOM   2855 C CA  . LEU B 1 71  ? -77.610  32.688 -59.245 1.00 20.38 ? 71   LEU B CA  1 
ATOM   2856 C C   . LEU B 1 71  ? -76.312  33.349 -59.673 1.00 20.32 ? 71   LEU B C   1 
ATOM   2857 O O   . LEU B 1 71  ? -76.298  34.542 -60.012 1.00 20.48 ? 71   LEU B O   1 
ATOM   2858 C CB  . LEU B 1 71  ? -77.709  32.655 -57.726 1.00 20.43 ? 71   LEU B CB  1 
ATOM   2859 C CG  . LEU B 1 71  ? -79.069  32.338 -57.107 1.00 20.11 ? 71   LEU B CG  1 
ATOM   2860 C CD1 . LEU B 1 71  ? -78.910  32.291 -55.611 1.00 20.34 ? 71   LEU B CD1 1 
ATOM   2861 C CD2 . LEU B 1 71  ? -80.129  33.350 -57.513 1.00 18.93 ? 71   LEU B CD2 1 
ATOM   2862 N N   . ILE B 1 72  ? -75.232  32.572 -59.678 1.00 20.23 ? 72   ILE B N   1 
ATOM   2863 C CA  . ILE B 1 72  ? -73.915  33.092 -60.030 1.00 20.61 ? 72   ILE B CA  1 
ATOM   2864 C C   . ILE B 1 72  ? -73.895  33.494 -61.495 1.00 22.09 ? 72   ILE B C   1 
ATOM   2865 O O   . ILE B 1 72  ? -73.456  34.613 -61.838 1.00 22.38 ? 72   ILE B O   1 
ATOM   2866 C CB  . ILE B 1 72  ? -72.794  32.076 -59.689 1.00 19.85 ? 72   ILE B CB  1 
ATOM   2867 C CG1 . ILE B 1 72  ? -72.563  32.000 -58.175 1.00 17.97 ? 72   ILE B CG1 1 
ATOM   2868 C CG2 . ILE B 1 72  ? -71.517  32.426 -60.405 1.00 19.16 ? 72   ILE B CG2 1 
ATOM   2869 C CD1 . ILE B 1 72  ? -71.882  30.713 -57.719 1.00 15.83 ? 72   ILE B CD1 1 
ATOM   2870 N N   . MET B 1 73  ? -74.403  32.598 -62.345 1.00 23.27 ? 73   MET B N   1 
ATOM   2871 C CA  . MET B 1 73  ? -74.549  32.878 -63.774 1.00 24.82 ? 73   MET B CA  1 
ATOM   2872 C C   . MET B 1 73  ? -75.421  34.089 -64.088 1.00 24.70 ? 73   MET B C   1 
ATOM   2873 O O   . MET B 1 73  ? -75.108  34.832 -65.021 1.00 25.32 ? 73   MET B O   1 
ATOM   2874 C CB  . MET B 1 73  ? -75.087  31.655 -64.521 1.00 25.70 ? 73   MET B CB  1 
ATOM   2875 C CG  . MET B 1 73  ? -74.009  30.796 -65.114 1.00 29.11 ? 73   MET B CG  1 
ATOM   2876 S SD  . MET B 1 73  ? -74.678  29.506 -66.182 1.00 34.59 ? 73   MET B SD  1 
ATOM   2877 C CE  . MET B 1 73  ? -75.072  28.359 -64.939 1.00 34.84 ? 73   MET B CE  1 
ATOM   2878 N N   . ILE B 1 74  ? -76.520  34.281 -63.353 1.00 24.57 ? 74   ILE B N   1 
ATOM   2879 C CA  . ILE B 1 74  ? -77.362  35.482 -63.535 1.00 24.15 ? 74   ILE B CA  1 
ATOM   2880 C C   . ILE B 1 74  ? -76.545  36.735 -63.204 1.00 24.10 ? 74   ILE B C   1 
ATOM   2881 O O   . ILE B 1 74  ? -76.564  37.708 -63.946 1.00 24.35 ? 74   ILE B O   1 
ATOM   2882 C CB  . ILE B 1 74  ? -78.668  35.424 -62.668 1.00 24.02 ? 74   ILE B CB  1 
ATOM   2883 C CG1 . ILE B 1 74  ? -79.677  34.428 -63.243 1.00 24.35 ? 74   ILE B CG1 1 
ATOM   2884 C CG2 . ILE B 1 74  ? -79.345  36.792 -62.570 1.00 22.86 ? 74   ILE B CG2 1 
ATOM   2885 C CD1 . ILE B 1 74  ? -80.815  34.064 -62.281 1.00 23.32 ? 74   ILE B CD1 1 
ATOM   2886 N N   . ASN B 1 75  ? -75.825  36.692 -62.090 1.00 24.12 ? 75   ASN B N   1 
ATOM   2887 C CA  . ASN B 1 75  ? -74.990  37.805 -61.661 1.00 24.21 ? 75   ASN B CA  1 
ATOM   2888 C C   . ASN B 1 75  ? -73.932  38.178 -62.678 1.00 24.00 ? 75   ASN B C   1 
ATOM   2889 O O   . ASN B 1 75  ? -73.742  39.343 -62.967 1.00 24.03 ? 75   ASN B O   1 
ATOM   2890 C CB  . ASN B 1 75  ? -74.304  37.463 -60.337 1.00 24.67 ? 75   ASN B CB  1 
ATOM   2891 C CG  . ASN B 1 75  ? -73.422  38.591 -59.827 1.00 25.03 ? 75   ASN B CG  1 
ATOM   2892 O OD1 . ASN B 1 75  ? -73.933  39.635 -59.399 1.00 26.43 ? 75   ASN B OD1 1 
ATOM   2893 N ND2 . ASN B 1 75  ? -72.097  38.387 -59.862 1.00 23.76 ? 75   ASN B ND2 1 
ATOM   2894 N N   . ALA B 1 76  ? -73.236  37.174 -63.199 1.00 24.04 ? 76   ALA B N   1 
ATOM   2895 C CA  . ALA B 1 76  ? -72.157  37.376 -64.152 1.00 23.96 ? 76   ALA B CA  1 
ATOM   2896 C C   . ALA B 1 76  ? -72.693  38.081 -65.382 1.00 24.05 ? 76   ALA B C   1 
ATOM   2897 O O   . ALA B 1 76  ? -72.073  39.018 -65.871 1.00 24.25 ? 76   ALA B O   1 
ATOM   2898 C CB  . ALA B 1 76  ? -71.516  36.056 -64.529 1.00 23.41 ? 76   ALA B CB  1 
ATOM   2899 N N   . CYS B 1 77  ? -73.860  37.649 -65.855 1.00 23.93 ? 77   CYS B N   1 
ATOM   2900 C CA  . CYS B 1 77  ? -74.464  38.240 -67.047 1.00 24.00 ? 77   CYS B CA  1 
ATOM   2901 C C   . CYS B 1 77  ? -74.955  39.670 -66.829 1.00 24.27 ? 77   CYS B C   1 
ATOM   2902 O O   . CYS B 1 77  ? -74.808  40.509 -67.709 1.00 24.28 ? 77   CYS B O   1 
ATOM   2903 C CB  . CYS B 1 77  ? -75.583  37.362 -67.585 1.00 23.79 ? 77   CYS B CB  1 
ATOM   2904 S SG  . CYS B 1 77  ? -74.982  35.771 -68.159 1.00 23.20 ? 77   CYS B SG  1 
ATOM   2905 N N   . LYS B 1 78  ? -75.524  39.942 -65.662 1.00 24.62 ? 78   LYS B N   1 
ATOM   2906 C CA  . LYS B 1 78  ? -75.934  41.295 -65.306 1.00 25.06 ? 78   LYS B CA  1 
ATOM   2907 C C   . LYS B 1 78  ? -74.776  42.292 -65.196 1.00 24.67 ? 78   LYS B C   1 
ATOM   2908 O O   . LYS B 1 78  ? -74.858  43.389 -65.737 1.00 24.72 ? 78   LYS B O   1 
ATOM   2909 C CB  . LYS B 1 78  ? -76.761  41.292 -64.026 1.00 25.75 ? 78   LYS B CB  1 
ATOM   2910 C CG  . LYS B 1 78  ? -78.255  41.291 -64.311 1.00 28.55 ? 78   LYS B CG  1 
ATOM   2911 C CD  . LYS B 1 78  ? -78.822  42.703 -64.349 1.00 31.87 ? 78   LYS B CD  1 
ATOM   2912 C CE  . LYS B 1 78  ? -80.264  42.695 -64.833 1.00 34.40 ? 78   LYS B CE  1 
ATOM   2913 N NZ  . LYS B 1 78  ? -80.400  43.255 -66.221 1.00 36.00 ? 78   LYS B NZ  1 
ATOM   2914 N N   . ILE B 1 79  ? -73.694  41.921 -64.519 1.00 24.40 ? 79   ILE B N   1 
ATOM   2915 C CA  . ILE B 1 79  ? -72.566  42.850 -64.390 1.00 24.03 ? 79   ILE B CA  1 
ATOM   2916 C C   . ILE B 1 79  ? -71.710  42.903 -65.659 1.00 23.71 ? 79   ILE B C   1 
ATOM   2917 O O   . ILE B 1 79  ? -70.836  43.773 -65.788 1.00 23.96 ? 79   ILE B O   1 
ATOM   2918 C CB  . ILE B 1 79  ? -71.722  42.599 -63.116 1.00 23.91 ? 79   ILE B CB  1 
ATOM   2919 C CG1 . ILE B 1 79  ? -71.017  41.253 -63.174 1.00 23.99 ? 79   ILE B CG1 1 
ATOM   2920 C CG2 . ILE B 1 79  ? -72.577  42.763 -61.862 1.00 24.15 ? 79   ILE B CG2 1 
ATOM   2921 C CD1 . ILE B 1 79  ? -69.944  41.098 -62.141 1.00 24.62 ? 79   ILE B CD1 1 
ATOM   2922 N N   . ALA B 1 80  ? -71.973  41.985 -66.591 1.00 22.94 ? 80   ALA B N   1 
ATOM   2923 C CA  . ALA B 1 80  ? -71.406  42.056 -67.933 1.00 22.32 ? 80   ALA B CA  1 
ATOM   2924 C C   . ALA B 1 80  ? -72.341  42.788 -68.917 1.00 22.10 ? 80   ALA B C   1 
ATOM   2925 O O   . ALA B 1 80  ? -72.190  42.665 -70.131 1.00 21.50 ? 80   ALA B O   1 
ATOM   2926 C CB  . ALA B 1 80  ? -71.039  40.646 -68.448 1.00 21.95 ? 80   ALA B CB  1 
ATOM   2927 N N   . SER B 1 81  ? -73.293  43.554 -68.386 1.00 22.29 ? 81   SER B N   1 
ATOM   2928 C CA  . SER B 1 81  ? -74.173  44.421 -69.196 1.00 22.86 ? 81   SER B CA  1 
ATOM   2929 C C   . SER B 1 81  ? -75.146  43.696 -70.136 1.00 23.25 ? 81   SER B C   1 
ATOM   2930 O O   . SER B 1 81  ? -75.541  44.254 -71.175 1.00 23.42 ? 81   SER B O   1 
ATOM   2931 C CB  . SER B 1 81  ? -73.375  45.455 -70.006 1.00 22.58 ? 81   SER B CB  1 
ATOM   2932 O OG  . SER B 1 81  ? -72.561  46.230 -69.159 1.00 23.72 ? 81   SER B OG  1 
ATOM   2933 N N   . ALA B 1 82  ? -75.548  42.474 -69.795 1.00 23.33 ? 82   ALA B N   1 
ATOM   2934 C CA  . ALA B 1 82  ? -76.682  41.901 -70.504 1.00 23.96 ? 82   ALA B CA  1 
ATOM   2935 C C   . ALA B 1 82  ? -77.843  42.918 -70.508 1.00 24.44 ? 82   ALA B C   1 
ATOM   2936 O O   . ALA B 1 82  ? -78.057  43.661 -69.553 1.00 24.43 ? 82   ALA B O   1 
ATOM   2937 C CB  . ALA B 1 82  ? -77.109  40.577 -69.905 1.00 23.49 ? 82   ALA B CB  1 
ATOM   2938 N N   . SER B 1 83  ? -78.570  42.969 -71.606 1.00 25.12 ? 83   SER B N   1 
ATOM   2939 C CA  . SER B 1 83  ? -79.721  43.845 -71.681 1.00 25.76 ? 83   SER B CA  1 
ATOM   2940 C C   . SER B 1 83  ? -80.858  43.346 -70.794 1.00 25.62 ? 83   SER B C   1 
ATOM   2941 O O   . SER B 1 83  ? -81.559  44.149 -70.164 1.00 25.58 ? 83   SER B O   1 
ATOM   2942 C CB  . SER B 1 83  ? -80.202  43.957 -73.122 1.00 26.20 ? 83   SER B CB  1 
ATOM   2943 O OG  . SER B 1 83  ? -81.169  44.985 -73.205 1.00 27.79 ? 83   SER B OG  1 
ATOM   2944 N N   . ARG B 1 84  ? -81.034  42.024 -70.763 1.00 25.32 ? 84   ARG B N   1 
ATOM   2945 C CA  . ARG B 1 84  ? -82.056  41.378 -69.944 1.00 25.35 ? 84   ARG B CA  1 
ATOM   2946 C C   . ARG B 1 84  ? -81.591  39.971 -69.598 1.00 24.59 ? 84   ARG B C   1 
ATOM   2947 O O   . ARG B 1 84  ? -80.946  39.307 -70.405 1.00 24.23 ? 84   ARG B O   1 
ATOM   2948 C CB  . ARG B 1 84  ? -83.410  41.350 -70.668 1.00 25.88 ? 84   ARG B CB  1 
ATOM   2949 C CG  . ARG B 1 84  ? -84.594  40.885 -69.811 1.00 28.47 ? 84   ARG B CG  1 
ATOM   2950 C CD  . ARG B 1 84  ? -85.996  41.021 -70.463 1.00 31.96 ? 84   ARG B CD  1 
ATOM   2951 N NE  . ARG B 1 84  ? -86.007  40.595 -71.866 1.00 34.69 ? 84   ARG B NE  1 
ATOM   2952 C CZ  . ARG B 1 84  ? -87.095  40.518 -72.634 1.00 36.52 ? 84   ARG B CZ  1 
ATOM   2953 N NH1 . ARG B 1 84  ? -88.299  40.822 -72.154 1.00 37.93 ? 84   ARG B NH1 1 
ATOM   2954 N NH2 . ARG B 1 84  ? -86.981  40.122 -73.889 1.00 36.56 ? 84   ARG B NH2 1 
ATOM   2955 N N   . VAL B 1 85  ? -81.890  39.536 -68.379 1.00 23.98 ? 85   VAL B N   1 
ATOM   2956 C CA  . VAL B 1 85  ? -81.546  38.186 -67.933 1.00 23.55 ? 85   VAL B CA  1 
ATOM   2957 C C   . VAL B 1 85  ? -82.822  37.497 -67.455 1.00 23.13 ? 85   VAL B C   1 
ATOM   2958 O O   . VAL B 1 85  ? -83.512  38.003 -66.591 1.00 22.88 ? 85   VAL B O   1 
ATOM   2959 C CB  . VAL B 1 85  ? -80.422  38.173 -66.835 1.00 23.17 ? 85   VAL B CB  1 
ATOM   2960 C CG1 . VAL B 1 85  ? -80.140  36.746 -66.344 1.00 22.60 ? 85   VAL B CG1 1 
ATOM   2961 C CG2 . VAL B 1 85  ? -79.154  38.789 -67.373 1.00 22.58 ? 85   VAL B CG2 1 
ATOM   2962 N N   . THR B 1 86  ? -83.142  36.369 -68.078 1.00 22.93 ? 86   THR B N   1 
ATOM   2963 C CA  . THR B 1 86  ? -84.315  35.595 -67.736 1.00 22.91 ? 86   THR B CA  1 
ATOM   2964 C C   . THR B 1 86  ? -83.795  34.272 -67.227 1.00 23.11 ? 86   THR B C   1 
ATOM   2965 O O   . THR B 1 86  ? -82.947  33.645 -67.879 1.00 23.27 ? 86   THR B O   1 
ATOM   2966 C CB  . THR B 1 86  ? -85.193  35.343 -68.987 1.00 22.99 ? 86   THR B CB  1 
ATOM   2967 O OG1 . THR B 1 86  ? -85.731  36.581 -69.478 1.00 23.38 ? 86   THR B OG1 1 
ATOM   2968 C CG2 . THR B 1 86  ? -86.433  34.530 -68.638 1.00 21.86 ? 86   THR B CG2 1 
ATOM   2969 N N   . ALA B 1 87  ? -84.285  33.864 -66.062 1.00 22.91 ? 87   ALA B N   1 
ATOM   2970 C CA  . ALA B 1 87  ? -84.016  32.548 -65.537 1.00 23.24 ? 87   ALA B CA  1 
ATOM   2971 C C   . ALA B 1 87  ? -85.131  31.638 -66.004 1.00 23.65 ? 87   ALA B C   1 
ATOM   2972 O O   . ALA B 1 87  ? -86.301  31.840 -65.666 1.00 23.59 ? 87   ALA B O   1 
ATOM   2973 C CB  . ALA B 1 87  ? -83.959  32.587 -64.036 1.00 23.40 ? 87   ALA B CB  1 
ATOM   2974 N N   . VAL B 1 88  ? -84.766  30.659 -66.827 1.00 24.10 ? 88   VAL B N   1 
ATOM   2975 C CA  . VAL B 1 88  ? -85.695  29.618 -67.266 1.00 24.08 ? 88   VAL B CA  1 
ATOM   2976 C C   . VAL B 1 88  ? -85.532  28.461 -66.287 1.00 24.06 ? 88   VAL B C   1 
ATOM   2977 O O   . VAL B 1 88  ? -84.519  27.756 -66.319 1.00 23.84 ? 88   VAL B O   1 
ATOM   2978 C CB  . VAL B 1 88  ? -85.401  29.192 -68.730 1.00 24.24 ? 88   VAL B CB  1 
ATOM   2979 C CG1 . VAL B 1 88  ? -86.435  28.209 -69.247 1.00 24.03 ? 88   VAL B CG1 1 
ATOM   2980 C CG2 . VAL B 1 88  ? -85.330  30.439 -69.644 1.00 24.25 ? 88   VAL B CG2 1 
ATOM   2981 N N   . ILE B 1 89  ? -86.506  28.321 -65.385 1.00 23.94 ? 89   ILE B N   1 
ATOM   2982 C CA  . ILE B 1 89  ? -86.451  27.333 -64.319 1.00 24.08 ? 89   ILE B CA  1 
ATOM   2983 C C   . ILE B 1 89  ? -87.630  26.383 -64.439 1.00 24.36 ? 89   ILE B C   1 
ATOM   2984 O O   . ILE B 1 89  ? -88.662  26.559 -63.777 1.00 23.97 ? 89   ILE B O   1 
ATOM   2985 C CB  . ILE B 1 89  ? -86.474  27.997 -62.922 1.00 24.28 ? 89   ILE B CB  1 
ATOM   2986 C CG1 . ILE B 1 89  ? -85.406  29.084 -62.793 1.00 24.64 ? 89   ILE B CG1 1 
ATOM   2987 C CG2 . ILE B 1 89  ? -86.330  26.942 -61.823 1.00 23.74 ? 89   ILE B CG2 1 
ATOM   2988 C CD1 . ILE B 1 89  ? -85.610  30.002 -61.580 1.00 24.98 ? 89   ILE B CD1 1 
ATOM   2989 N N   . PRO B 1 90  ? -87.459  25.338 -65.241 1.00 24.99 ? 90   PRO B N   1 
ATOM   2990 C CA  . PRO B 1 90  ? -88.546  24.397 -65.519 1.00 25.02 ? 90   PRO B CA  1 
ATOM   2991 C C   . PRO B 1 90  ? -89.185  23.877 -64.214 1.00 25.18 ? 90   PRO B C   1 
ATOM   2992 O O   . PRO B 1 90  ? -90.404  23.847 -64.092 1.00 25.33 ? 90   PRO B O   1 
ATOM   2993 C CB  . PRO B 1 90  ? -87.832  23.269 -66.264 1.00 25.30 ? 90   PRO B CB  1 
ATOM   2994 C CG  . PRO B 1 90  ? -86.603  23.885 -66.853 1.00 25.01 ? 90   PRO B CG  1 
ATOM   2995 C CD  . PRO B 1 90  ? -86.190  24.938 -65.893 1.00 25.17 ? 90   PRO B CD  1 
ATOM   2996 N N   . CYS B 1 91  ? -88.370  23.505 -63.235 1.00 25.09 ? 91   CYS B N   1 
ATOM   2997 C CA  . CYS B 1 91  ? -88.907  23.038 -61.966 1.00 25.11 ? 91   CYS B CA  1 
ATOM   2998 C C   . CYS B 1 91  ? -88.450  23.944 -60.817 1.00 25.02 ? 91   CYS B C   1 
ATOM   2999 O O   . CYS B 1 91  ? -87.279  23.927 -60.449 1.00 24.83 ? 91   CYS B O   1 
ATOM   3000 C CB  . CYS B 1 91  ? -88.491  21.581 -61.715 1.00 25.04 ? 91   CYS B CB  1 
ATOM   3001 S SG  . CYS B 1 91  ? -89.215  20.889 -60.218 1.00 25.60 ? 91   CYS B SG  1 
ATOM   3002 N N   . PHE B 1 92  ? -89.377  24.720 -60.258 1.00 25.00 ? 92   PHE B N   1 
ATOM   3003 C CA  . PHE B 1 92  ? -89.028  25.727 -59.267 1.00 25.64 ? 92   PHE B CA  1 
ATOM   3004 C C   . PHE B 1 92  ? -88.593  25.068 -57.969 1.00 26.60 ? 92   PHE B C   1 
ATOM   3005 O O   . PHE B 1 92  ? -89.319  24.263 -57.385 1.00 26.67 ? 92   PHE B O   1 
ATOM   3006 C CB  . PHE B 1 92  ? -90.163  26.735 -59.035 1.00 25.35 ? 92   PHE B CB  1 
ATOM   3007 C CG  . PHE B 1 92  ? -89.708  28.038 -58.410 1.00 24.58 ? 92   PHE B CG  1 
ATOM   3008 C CD1 . PHE B 1 92  ? -89.292  29.106 -59.213 1.00 24.25 ? 92   PHE B CD1 1 
ATOM   3009 C CD2 . PHE B 1 92  ? -89.694  28.199 -57.018 1.00 23.16 ? 92   PHE B CD2 1 
ATOM   3010 C CE1 . PHE B 1 92  ? -88.863  30.313 -58.639 1.00 23.54 ? 92   PHE B CE1 1 
ATOM   3011 C CE2 . PHE B 1 92  ? -89.278  29.399 -56.433 1.00 22.51 ? 92   PHE B CE2 1 
ATOM   3012 C CZ  . PHE B 1 92  ? -88.855  30.461 -57.246 1.00 22.99 ? 92   PHE B CZ  1 
ATOM   3013 N N   . PRO B 1 93  ? -87.379  25.388 -57.546 1.00 27.50 ? 93   PRO B N   1 
ATOM   3014 C CA  . PRO B 1 93  ? -86.793  24.775 -56.355 1.00 28.35 ? 93   PRO B CA  1 
ATOM   3015 C C   . PRO B 1 93  ? -87.385  25.343 -55.076 1.00 29.11 ? 93   PRO B C   1 
ATOM   3016 O O   . PRO B 1 93  ? -87.668  26.542 -55.019 1.00 29.18 ? 93   PRO B O   1 
ATOM   3017 C CB  . PRO B 1 93  ? -85.300  25.117 -56.475 1.00 28.51 ? 93   PRO B CB  1 
ATOM   3018 C CG  . PRO B 1 93  ? -85.210  26.299 -57.397 1.00 28.33 ? 93   PRO B CG  1 
ATOM   3019 C CD  . PRO B 1 93  ? -86.478  26.356 -58.197 1.00 27.63 ? 93   PRO B CD  1 
ATOM   3020 N N   . TYR B 1 94  ? -87.581  24.476 -54.082 1.00 29.99 ? 94   TYR B N   1 
ATOM   3021 C CA  . TYR B 1 94  ? -88.109  24.840 -52.767 1.00 30.97 ? 94   TYR B CA  1 
ATOM   3022 C C   . TYR B 1 94  ? -89.564  25.298 -52.820 1.00 32.35 ? 94   TYR B C   1 
ATOM   3023 O O   . TYR B 1 94  ? -90.093  25.817 -51.836 1.00 32.21 ? 94   TYR B O   1 
ATOM   3024 C CB  . TYR B 1 94  ? -87.227  25.898 -52.076 1.00 30.86 ? 94   TYR B CB  1 
ATOM   3025 C CG  . TYR B 1 94  ? -85.886  25.388 -51.596 1.00 29.74 ? 94   TYR B CG  1 
ATOM   3026 C CD1 . TYR B 1 94  ? -84.773  25.381 -52.440 1.00 28.30 ? 94   TYR B CD1 1 
ATOM   3027 C CD2 . TYR B 1 94  ? -85.723  24.921 -50.287 1.00 28.84 ? 94   TYR B CD2 1 
ATOM   3028 C CE1 . TYR B 1 94  ? -83.537  24.924 -51.995 1.00 26.59 ? 94   TYR B CE1 1 
ATOM   3029 C CE2 . TYR B 1 94  ? -84.485  24.461 -49.840 1.00 27.45 ? 94   TYR B CE2 1 
ATOM   3030 C CZ  . TYR B 1 94  ? -83.409  24.468 -50.700 1.00 26.22 ? 94   TYR B CZ  1 
ATOM   3031 O OH  . TYR B 1 94  ? -82.208  24.009 -50.259 1.00 25.59 ? 94   TYR B OH  1 
ATOM   3032 N N   . ALA B 1 95  ? -90.215  25.073 -53.961 1.00 34.23 ? 95   ALA B N   1 
ATOM   3033 C CA  . ALA B 1 95  ? -91.626  25.423 -54.153 1.00 36.25 ? 95   ALA B CA  1 
ATOM   3034 C C   . ALA B 1 95  ? -92.608  24.771 -53.167 1.00 38.09 ? 95   ALA B C   1 
ATOM   3035 O O   . ALA B 1 95  ? -93.691  25.307 -52.934 1.00 38.33 ? 95   ALA B O   1 
ATOM   3036 C CB  . ALA B 1 95  ? -92.036  25.134 -55.552 1.00 35.92 ? 95   ALA B CB  1 
ATOM   3037 N N   . ARG B 1 96  ? -92.243  23.628 -52.591 1.00 40.28 ? 96   ARG B N   1 
ATOM   3038 C CA  . ARG B 1 96  ? -93.060  23.018 -51.539 1.00 42.66 ? 96   ARG B CA  1 
ATOM   3039 C C   . ARG B 1 96  ? -92.927  23.790 -50.230 1.00 43.81 ? 96   ARG B C   1 
ATOM   3040 O O   . ARG B 1 96  ? -93.731  23.624 -49.320 1.00 43.93 ? 96   ARG B O   1 
ATOM   3041 C CB  . ARG B 1 96  ? -92.667  21.560 -51.303 1.00 43.17 ? 96   ARG B CB  1 
ATOM   3042 C CG  . ARG B 1 96  ? -93.640  20.540 -51.859 1.00 45.17 ? 96   ARG B CG  1 
ATOM   3043 C CD  . ARG B 1 96  ? -92.990  19.441 -52.707 1.00 48.98 ? 96   ARG B CD  1 
ATOM   3044 N NE  . ARG B 1 96  ? -91.522  19.417 -52.613 1.00 51.91 ? 96   ARG B NE  1 
ATOM   3045 C CZ  . ARG B 1 96  ? -90.815  18.444 -52.030 1.00 53.19 ? 96   ARG B CZ  1 
ATOM   3046 N NH1 . ARG B 1 96  ? -91.424  17.393 -51.482 1.00 53.15 ? 96   ARG B NH1 1 
ATOM   3047 N NH2 . ARG B 1 96  ? -89.490  18.520 -52.002 1.00 54.00 ? 96   ARG B NH2 1 
ATOM   3048 N N   . GLN B 1 97  ? -91.890  24.617 -50.134 1.00 45.47 ? 97   GLN B N   1 
ATOM   3049 C CA  . GLN B 1 97  ? -91.697  25.480 -48.972 1.00 46.86 ? 97   GLN B CA  1 
ATOM   3050 C C   . GLN B 1 97  ? -92.258  26.870 -49.284 1.00 47.78 ? 97   GLN B C   1 
ATOM   3051 O O   . GLN B 1 97  ? -91.533  27.865 -49.301 1.00 47.88 ? 97   GLN B O   1 
ATOM   3052 C CB  . GLN B 1 97  ? -90.214  25.538 -48.588 1.00 46.93 ? 97   GLN B CB  1 
ATOM   3053 C CG  . GLN B 1 97  ? -89.847  24.709 -47.349 1.00 47.61 ? 97   GLN B CG  1 
ATOM   3054 C CD  . GLN B 1 97  ? -88.608  23.835 -47.558 1.00 47.31 ? 97   GLN B CD  1 
ATOM   3055 O OE1 . GLN B 1 97  ? -87.521  24.160 -47.066 1.00 46.67 ? 97   GLN B OE1 1 
ATOM   3056 N NE2 . GLN B 1 97  ? -88.771  22.731 -48.289 1.00 47.55 ? 97   GLN B NE2 1 
ATOM   3057 N N   . ASP B 1 98  ? -93.562  26.922 -49.533 1.00 49.07 ? 98   ASP B N   1 
ATOM   3058 C CA  . ASP B 1 98  ? -94.215  28.154 -49.948 1.00 50.42 ? 98   ASP B CA  1 
ATOM   3059 C C   . ASP B 1 98  ? -95.117  28.757 -48.870 1.00 51.55 ? 98   ASP B C   1 
ATOM   3060 O O   . ASP B 1 98  ? -95.652  29.852 -49.061 1.00 51.87 ? 98   ASP B O   1 
ATOM   3061 C CB  . ASP B 1 98  ? -94.988  27.938 -51.257 1.00 50.28 ? 98   ASP B CB  1 
ATOM   3062 C CG  . ASP B 1 98  ? -96.210  27.035 -51.092 1.00 50.44 ? 98   ASP B CG  1 
ATOM   3063 O OD1 . ASP B 1 98  ? -96.276  26.229 -50.136 1.00 50.64 ? 98   ASP B OD1 1 
ATOM   3064 O OD2 . ASP B 1 98  ? -97.162  27.063 -51.894 1.00 50.38 ? 98   ASP B OD2 1 
ATOM   3065 N N   . LYS B 1 99  ? -95.270  28.052 -47.747 1.00 52.87 ? 99   LYS B N   1 
ATOM   3066 C CA  . LYS B 1 99  ? -96.077  28.526 -46.605 1.00 54.18 ? 99   LYS B CA  1 
ATOM   3067 C C   . LYS B 1 99  ? -95.457  28.179 -45.243 1.00 55.17 ? 99   LYS B C   1 
ATOM   3068 O O   . LYS B 1 99  ? -94.604  27.296 -45.144 1.00 55.15 ? 99   LYS B O   1 
ATOM   3069 C CB  . LYS B 1 99  ? -97.517  27.996 -46.689 1.00 54.06 ? 99   LYS B CB  1 
ATOM   3070 C CG  . LYS B 1 99  ? -97.633  26.481 -46.821 1.00 54.28 ? 99   LYS B CG  1 
ATOM   3071 C CD  . LYS B 1 99  ? -99.067  26.025 -46.627 1.00 55.36 ? 99   LYS B CD  1 
ATOM   3072 C CE  . LYS B 1 99  ? -99.561  25.179 -47.793 1.00 55.86 ? 99   LYS B CE  1 
ATOM   3073 N NZ  . LYS B 1 99  ? -101.008 25.443 -48.088 1.00 55.67 ? 99   LYS B NZ  1 
ATOM   3074 N N   . LYS B 1 100 ? -95.888  28.883 -44.200 1.00 56.58 ? 100  LYS B N   1 
ATOM   3075 C CA  . LYS B 1 100 ? -95.405  28.640 -42.840 1.00 58.01 ? 100  LYS B CA  1 
ATOM   3076 C C   . LYS B 1 100 ? -96.028  27.363 -42.271 1.00 59.17 ? 100  LYS B C   1 
ATOM   3077 O O   . LYS B 1 100 ? -95.337  26.552 -41.637 1.00 59.30 ? 100  LYS B O   1 
ATOM   3078 C CB  . LYS B 1 100 ? -95.734  29.829 -41.932 1.00 57.97 ? 100  LYS B CB  1 
ATOM   3079 C CG  . LYS B 1 100 ? -94.592  30.810 -41.734 1.00 57.88 ? 100  LYS B CG  1 
ATOM   3080 C CD  . LYS B 1 100 ? -94.815  31.646 -40.480 1.00 57.92 ? 100  LYS B CD  1 
ATOM   3081 C CE  . LYS B 1 100 ? -94.190  33.036 -40.596 1.00 57.75 ? 100  LYS B CE  1 
ATOM   3082 N NZ  . LYS B 1 100 ? -94.741  34.027 -39.602 1.00 57.13 ? 100  LYS B NZ  1 
ATOM   3083 N N   . ASP B 1 101 ? -97.335  27.209 -42.513 1.00 60.42 ? 101  ASP B N   1 
ATOM   3084 C CA  . ASP B 1 101 ? -98.141  26.044 -42.107 1.00 61.48 ? 101  ASP B CA  1 
ATOM   3085 C C   . ASP B 1 101 ? -98.108  25.702 -40.602 1.00 61.47 ? 101  ASP B C   1 
ATOM   3086 O O   . ASP B 1 101 ? -97.720  24.593 -40.204 1.00 61.59 ? 101  ASP B O   1 
ATOM   3087 C CB  . ASP B 1 101 ? -97.833  24.814 -42.982 1.00 62.15 ? 101  ASP B CB  1 
ATOM   3088 C CG  . ASP B 1 101 ? -99.086  24.006 -43.319 1.00 64.23 ? 101  ASP B CG  1 
ATOM   3089 O OD1 . ASP B 1 101 ? -99.845  23.633 -42.384 1.00 65.48 ? 101  ASP B OD1 1 
ATOM   3090 O OD2 . ASP B 1 101 ? -99.395  23.698 -44.494 1.00 65.74 ? 101  ASP B OD2 1 
ATOM   3091 N N   . LYS B 1 102 ? -98.532  26.669 -39.785 1.00 61.39 ? 102  LYS B N   1 
ATOM   3092 C CA  . LYS B 1 102 ? -98.663  26.517 -38.322 1.00 61.25 ? 102  LYS B CA  1 
ATOM   3093 C C   . LYS B 1 102 ? -97.358  26.215 -37.559 1.00 60.18 ? 102  LYS B C   1 
ATOM   3094 O O   . LYS B 1 102 ? -97.412  25.844 -36.382 1.00 60.46 ? 102  LYS B O   1 
ATOM   3095 C CB  . LYS B 1 102 ? -99.709  25.452 -37.958 1.00 61.94 ? 102  LYS B CB  1 
ATOM   3096 C CG  . LYS B 1 102 ? -101.150 25.784 -38.300 1.00 64.16 ? 102  LYS B CG  1 
ATOM   3097 C CD  . LYS B 1 102 ? -102.059 24.643 -37.817 1.00 67.35 ? 102  LYS B CD  1 
ATOM   3098 C CE  . LYS B 1 102 ? -103.523 24.865 -38.189 1.00 69.24 ? 102  LYS B CE  1 
ATOM   3099 N NZ  . LYS B 1 102 ? -104.438 24.356 -37.128 1.00 70.22 ? 102  LYS B NZ  1 
ATOM   3100 N N   . SER B 1 103 ? -96.205  26.362 -38.216 1.00 58.48 ? 103  SER B N   1 
ATOM   3101 C CA  . SER B 1 103 ? -94.911  26.183 -37.549 1.00 56.80 ? 103  SER B CA  1 
ATOM   3102 C C   . SER B 1 103 ? -94.010  27.414 -37.720 1.00 55.28 ? 103  SER B C   1 
ATOM   3103 O O   . SER B 1 103 ? -94.346  28.325 -38.478 1.00 55.25 ? 103  SER B O   1 
ATOM   3104 C CB  . SER B 1 103 ? -94.203  24.909 -38.044 1.00 56.97 ? 103  SER B CB  1 
ATOM   3105 O OG  . SER B 1 103 ? -94.535  24.616 -39.390 1.00 57.04 ? 103  SER B OG  1 
ATOM   3106 N N   . ARG B 1 104 ? -92.883  27.442 -37.003 1.00 53.43 ? 104  ARG B N   1 
ATOM   3107 C CA  . ARG B 1 104 ? -91.881  28.506 -37.153 1.00 51.40 ? 104  ARG B CA  1 
ATOM   3108 C C   . ARG B 1 104 ? -90.921  28.184 -38.308 1.00 50.17 ? 104  ARG B C   1 
ATOM   3109 O O   . ARG B 1 104 ? -89.696  28.024 -38.131 1.00 50.12 ? 104  ARG B O   1 
ATOM   3110 C CB  . ARG B 1 104 ? -91.137  28.762 -35.839 1.00 51.19 ? 104  ARG B CB  1 
ATOM   3111 C CG  . ARG B 1 104 ? -91.724  29.920 -35.046 1.00 50.59 ? 104  ARG B CG  1 
ATOM   3112 C CD  . ARG B 1 104 ? -91.173  30.099 -33.640 1.00 49.35 ? 104  ARG B CD  1 
ATOM   3113 N NE  . ARG B 1 104 ? -91.269  28.884 -32.833 1.00 49.23 ? 104  ARG B NE  1 
ATOM   3114 C CZ  . ARG B 1 104 ? -92.076  28.717 -31.796 1.00 49.05 ? 104  ARG B CZ  1 
ATOM   3115 N NH1 . ARG B 1 104 ? -92.894  29.680 -31.411 1.00 49.37 ? 104  ARG B NH1 1 
ATOM   3116 N NH2 . ARG B 1 104 ? -92.063  27.573 -31.133 1.00 49.64 ? 104  ARG B NH2 1 
ATOM   3117 N N   . ALA B 1 105 ? -91.516  28.092 -39.496 1.00 48.32 ? 105  ALA B N   1 
ATOM   3118 C CA  . ALA B 1 105 ? -90.845  27.653 -40.706 1.00 46.31 ? 105  ALA B CA  1 
ATOM   3119 C C   . ALA B 1 105 ? -90.420  28.852 -41.547 1.00 44.77 ? 105  ALA B C   1 
ATOM   3120 O O   . ALA B 1 105 ? -91.045  29.912 -41.489 1.00 44.99 ? 105  ALA B O   1 
ATOM   3121 C CB  . ALA B 1 105 ? -91.792  26.762 -41.512 1.00 46.36 ? 105  ALA B CB  1 
ATOM   3122 N N   . PRO B 1 106 ? -89.368  28.692 -42.342 1.00 43.00 ? 106  PRO B N   1 
ATOM   3123 C CA  . PRO B 1 106 ? -89.090  29.654 -43.407 1.00 41.54 ? 106  PRO B CA  1 
ATOM   3124 C C   . PRO B 1 106 ? -90.134  29.533 -44.530 1.00 39.69 ? 106  PRO B C   1 
ATOM   3125 O O   . PRO B 1 106 ? -90.716  28.456 -44.742 1.00 39.43 ? 106  PRO B O   1 
ATOM   3126 C CB  . PRO B 1 106 ? -87.718  29.201 -43.920 1.00 41.69 ? 106  PRO B CB  1 
ATOM   3127 C CG  . PRO B 1 106 ? -87.686  27.747 -43.639 1.00 42.07 ? 106  PRO B CG  1 
ATOM   3128 C CD  . PRO B 1 106 ? -88.376  27.599 -42.317 1.00 42.97 ? 106  PRO B CD  1 
ATOM   3129 N N   . ILE B 1 107 ? -90.382  30.628 -45.237 1.00 37.58 ? 107  ILE B N   1 
ATOM   3130 C CA  . ILE B 1 107 ? -91.033  30.507 -46.536 1.00 35.44 ? 107  ILE B CA  1 
ATOM   3131 C C   . ILE B 1 107 ? -89.917  30.480 -47.575 1.00 33.43 ? 107  ILE B C   1 
ATOM   3132 O O   . ILE B 1 107 ? -89.649  31.478 -48.234 1.00 33.21 ? 107  ILE B O   1 
ATOM   3133 C CB  . ILE B 1 107 ? -92.034  31.644 -46.788 1.00 35.68 ? 107  ILE B CB  1 
ATOM   3134 C CG1 . ILE B 1 107 ? -92.920  31.860 -45.549 1.00 36.08 ? 107  ILE B CG1 1 
ATOM   3135 C CG2 . ILE B 1 107 ? -92.874  31.320 -48.036 1.00 35.93 ? 107  ILE B CG2 1 
ATOM   3136 C CD1 . ILE B 1 107 ? -94.186  32.710 -45.760 1.00 36.02 ? 107  ILE B CD1 1 
ATOM   3137 N N   . SER B 1 108 ? -89.261  29.325 -47.690 1.00 31.37 ? 108  SER B N   1 
ATOM   3138 C CA  . SER B 1 108 ? -88.052  29.154 -48.511 1.00 29.50 ? 108  SER B CA  1 
ATOM   3139 C C   . SER B 1 108 ? -88.220  29.499 -49.987 1.00 28.05 ? 108  SER B C   1 
ATOM   3140 O O   . SER B 1 108 ? -87.247  29.893 -50.634 1.00 27.51 ? 108  SER B O   1 
ATOM   3141 C CB  . SER B 1 108 ? -87.512  27.732 -48.398 1.00 29.54 ? 108  SER B CB  1 
ATOM   3142 O OG  . SER B 1 108 ? -87.172  27.416 -47.066 1.00 30.32 ? 108  SER B OG  1 
ATOM   3143 N N   . ALA B 1 109 ? -89.435  29.336 -50.518 1.00 26.63 ? 109  ALA B N   1 
ATOM   3144 C CA  . ALA B 1 109 ? -89.710  29.691 -51.915 1.00 25.66 ? 109  ALA B CA  1 
ATOM   3145 C C   . ALA B 1 109 ? -89.705  31.212 -52.107 1.00 24.90 ? 109  ALA B C   1 
ATOM   3146 O O   . ALA B 1 109 ? -89.240  31.713 -53.124 1.00 24.90 ? 109  ALA B O   1 
ATOM   3147 C CB  . ALA B 1 109 ? -91.014  29.083 -52.384 1.00 25.40 ? 109  ALA B CB  1 
ATOM   3148 N N   . LYS B 1 110 ? -90.205  31.942 -51.112 1.00 24.19 ? 110  LYS B N   1 
ATOM   3149 C CA  . LYS B 1 110 ? -90.057  33.393 -51.093 1.00 23.29 ? 110  LYS B CA  1 
ATOM   3150 C C   . LYS B 1 110 ? -88.575  33.793 -50.996 1.00 23.10 ? 110  LYS B C   1 
ATOM   3151 O O   . LYS B 1 110 ? -88.126  34.751 -51.655 1.00 23.12 ? 110  LYS B O   1 
ATOM   3152 C CB  . LYS B 1 110 ? -90.874  34.002 -49.951 1.00 22.87 ? 110  LYS B CB  1 
ATOM   3153 C CG  . LYS B 1 110 ? -90.789  35.535 -49.838 1.00 22.95 ? 110  LYS B CG  1 
ATOM   3154 C CD  . LYS B 1 110 ? -90.929  36.262 -51.177 1.00 23.01 ? 110  LYS B CD  1 
ATOM   3155 C CE  . LYS B 1 110 ? -90.831  37.779 -51.029 1.00 23.77 ? 110  LYS B CE  1 
ATOM   3156 N NZ  . LYS B 1 110 ? -91.677  38.244 -49.899 1.00 24.43 ? 110  LYS B NZ  1 
ATOM   3157 N N   . LEU B 1 111 ? -87.813  33.066 -50.181 1.00 22.24 ? 111  LEU B N   1 
ATOM   3158 C CA  . LEU B 1 111 ? -86.400  33.361 -50.066 1.00 21.97 ? 111  LEU B CA  1 
ATOM   3159 C C   . LEU B 1 111 ? -85.695  33.145 -51.427 1.00 21.58 ? 111  LEU B C   1 
ATOM   3160 O O   . LEU B 1 111 ? -84.951  34.008 -51.899 1.00 20.99 ? 111  LEU B O   1 
ATOM   3161 C CB  . LEU B 1 111 ? -85.775  32.555 -48.917 1.00 22.16 ? 111  LEU B CB  1 
ATOM   3162 C CG  . LEU B 1 111 ? -84.243  32.399 -48.910 1.00 22.14 ? 111  LEU B CG  1 
ATOM   3163 C CD1 . LEU B 1 111 ? -83.540  33.695 -48.499 1.00 21.07 ? 111  LEU B CD1 1 
ATOM   3164 C CD2 . LEU B 1 111 ? -83.817  31.237 -48.019 1.00 21.43 ? 111  LEU B CD2 1 
ATOM   3165 N N   . VAL B 1 112 ? -85.969  32.009 -52.066 1.00 21.53 ? 112  VAL B N   1 
ATOM   3166 C CA  . VAL B 1 112 ? -85.433  31.716 -53.399 1.00 21.57 ? 112  VAL B CA  1 
ATOM   3167 C C   . VAL B 1 112 ? -85.809  32.801 -54.437 1.00 21.72 ? 112  VAL B C   1 
ATOM   3168 O O   . VAL B 1 112 ? -84.957  33.221 -55.217 1.00 21.76 ? 112  VAL B O   1 
ATOM   3169 C CB  . VAL B 1 112 ? -85.810  30.273 -53.861 1.00 21.56 ? 112  VAL B CB  1 
ATOM   3170 C CG1 . VAL B 1 112 ? -85.603  30.070 -55.383 1.00 21.14 ? 112  VAL B CG1 1 
ATOM   3171 C CG2 . VAL B 1 112 ? -85.010  29.250 -53.061 1.00 20.75 ? 112  VAL B CG2 1 
ATOM   3172 N N   . ALA B 1 113 ? -87.063  33.261 -54.422 1.00 21.66 ? 113  ALA B N   1 
ATOM   3173 C CA  . ALA B 1 113 ? -87.493  34.385 -55.261 1.00 21.72 ? 113  ALA B CA  1 
ATOM   3174 C C   . ALA B 1 113 ? -86.709  35.665 -54.962 1.00 22.36 ? 113  ALA B C   1 
ATOM   3175 O O   . ALA B 1 113 ? -86.316  36.386 -55.890 1.00 23.08 ? 113  ALA B O   1 
ATOM   3176 C CB  . ALA B 1 113 ? -88.979  34.631 -55.107 1.00 21.53 ? 113  ALA B CB  1 
ATOM   3177 N N   . ASN B 1 114 ? -86.468  35.956 -53.682 1.00 22.53 ? 114  ASN B N   1 
ATOM   3178 C CA  . ASN B 1 114 ? -85.664  37.129 -53.327 1.00 22.80 ? 114  ASN B CA  1 
ATOM   3179 C C   . ASN B 1 114 ? -84.236  36.986 -53.800 1.00 22.97 ? 114  ASN B C   1 
ATOM   3180 O O   . ASN B 1 114 ? -83.628  37.952 -54.274 1.00 23.39 ? 114  ASN B O   1 
ATOM   3181 C CB  . ASN B 1 114 ? -85.672  37.390 -51.820 1.00 22.74 ? 114  ASN B CB  1 
ATOM   3182 C CG  . ASN B 1 114 ? -86.965  38.017 -51.337 1.00 22.72 ? 114  ASN B CG  1 
ATOM   3183 O OD1 . ASN B 1 114 ? -87.719  38.619 -52.101 1.00 21.52 ? 114  ASN B OD1 1 
ATOM   3184 N ND2 . ASN B 1 114 ? -87.224  37.875 -50.049 1.00 24.02 ? 114  ASN B ND2 1 
ATOM   3185 N N   . MET B 1 115 ? -83.695  35.784 -53.682 1.00 23.01 ? 115  MET B N   1 
ATOM   3186 C CA  . MET B 1 115 ? -82.319  35.558 -54.089 1.00 23.52 ? 115  MET B CA  1 
ATOM   3187 C C   . MET B 1 115 ? -82.213  35.751 -55.591 1.00 23.27 ? 115  MET B C   1 
ATOM   3188 O O   . MET B 1 115 ? -81.304  36.433 -56.055 1.00 22.94 ? 115  MET B O   1 
ATOM   3189 C CB  . MET B 1 115 ? -81.836  34.179 -53.662 1.00 24.11 ? 115  MET B CB  1 
ATOM   3190 C CG  . MET B 1 115 ? -81.774  33.986 -52.156 1.00 28.10 ? 115  MET B CG  1 
ATOM   3191 S SD  . MET B 1 115 ? -81.109  32.364 -51.715 1.00 35.66 ? 115  MET B SD  1 
ATOM   3192 C CE  . MET B 1 115 ? -82.406  31.341 -51.971 1.00 35.46 ? 115  MET B CE  1 
ATOM   3193 N N   . LEU B 1 116 ? -83.167  35.195 -56.349 1.00 23.17 ? 116  LEU B N   1 
ATOM   3194 C CA  . LEU B 1 116 ? -83.171  35.357 -57.806 1.00 22.99 ? 116  LEU B CA  1 
ATOM   3195 C C   . LEU B 1 116 ? -83.286  36.836 -58.220 1.00 23.13 ? 116  LEU B C   1 
ATOM   3196 O O   . LEU B 1 116 ? -82.598  37.281 -59.149 1.00 22.71 ? 116  LEU B O   1 
ATOM   3197 C CB  . LEU B 1 116 ? -84.271  34.511 -58.455 1.00 22.85 ? 116  LEU B CB  1 
ATOM   3198 C CG  . LEU B 1 116 ? -84.023  32.994 -58.537 1.00 22.33 ? 116  LEU B CG  1 
ATOM   3199 C CD1 . LEU B 1 116 ? -85.337  32.234 -58.593 1.00 20.74 ? 116  LEU B CD1 1 
ATOM   3200 C CD2 . LEU B 1 116 ? -83.153  32.638 -59.738 1.00 22.03 ? 116  LEU B CD2 1 
ATOM   3201 N N   . SER B 1 117 ? -84.144  37.580 -57.515 1.00 23.22 ? 117  SER B N   1 
ATOM   3202 C CA  . SER B 1 117 ? -84.307  39.019 -57.718 1.00 23.71 ? 117  SER B CA  1 
ATOM   3203 C C   . SER B 1 117 ? -83.014  39.834 -57.440 1.00 23.84 ? 117  SER B C   1 
ATOM   3204 O O   . SER B 1 117 ? -82.564  40.572 -58.308 1.00 23.80 ? 117  SER B O   1 
ATOM   3205 C CB  . SER B 1 117 ? -85.490  39.553 -56.890 1.00 24.11 ? 117  SER B CB  1 
ATOM   3206 O OG  . SER B 1 117 ? -86.726  38.889 -57.203 1.00 24.38 ? 117  SER B OG  1 
ATOM   3207 N N   . VAL B 1 118 ? -82.411  39.687 -56.255 1.00 23.88 ? 118  VAL B N   1 
ATOM   3208 C CA  . VAL B 1 118 ? -81.148  40.367 -55.960 1.00 23.63 ? 118  VAL B CA  1 
ATOM   3209 C C   . VAL B 1 118 ? -79.984  39.892 -56.816 1.00 23.52 ? 118  VAL B C   1 
ATOM   3210 O O   . VAL B 1 118 ? -79.015  40.624 -57.000 1.00 24.01 ? 118  VAL B O   1 
ATOM   3211 C CB  . VAL B 1 118 ? -80.723  40.333 -54.451 1.00 23.82 ? 118  VAL B CB  1 
ATOM   3212 C CG1 . VAL B 1 118 ? -81.724  41.060 -53.601 1.00 24.62 ? 118  VAL B CG1 1 
ATOM   3213 C CG2 . VAL B 1 118 ? -80.475  38.893 -53.919 1.00 23.95 ? 118  VAL B CG2 1 
ATOM   3214 N N   . ALA B 1 119 ? -80.062  38.686 -57.359 1.00 23.01 ? 119  ALA B N   1 
ATOM   3215 C CA  . ALA B 1 119 ? -78.999  38.234 -58.241 1.00 22.59 ? 119  ALA B CA  1 
ATOM   3216 C C   . ALA B 1 119 ? -79.094  38.995 -59.557 1.00 22.71 ? 119  ALA B C   1 
ATOM   3217 O O   . ALA B 1 119 ? -78.124  39.056 -60.303 1.00 23.08 ? 119  ALA B O   1 
ATOM   3218 C CB  . ALA B 1 119 ? -79.068  36.747 -58.461 1.00 21.91 ? 119  ALA B CB  1 
ATOM   3219 N N   . GLY B 1 120 ? -80.263  39.572 -59.840 1.00 22.75 ? 120  GLY B N   1 
ATOM   3220 C CA  . GLY B 1 120 ? -80.456  40.388 -61.033 1.00 22.91 ? 120  GLY B CA  1 
ATOM   3221 C C   . GLY B 1 120 ? -81.356  39.825 -62.133 1.00 23.00 ? 120  GLY B C   1 
ATOM   3222 O O   . GLY B 1 120 ? -81.300  40.278 -63.278 1.00 23.57 ? 120  GLY B O   1 
ATOM   3223 N N   . ALA B 1 121 ? -82.190  38.846 -61.801 1.00 22.72 ? 121  ALA B N   1 
ATOM   3224 C CA  . ALA B 1 121 ? -83.161  38.308 -62.748 1.00 22.37 ? 121  ALA B CA  1 
ATOM   3225 C C   . ALA B 1 121 ? -84.244  39.338 -63.058 1.00 21.86 ? 121  ALA B C   1 
ATOM   3226 O O   . ALA B 1 121 ? -84.826  39.901 -62.157 1.00 21.19 ? 121  ALA B O   1 
ATOM   3227 C CB  . ALA B 1 121 ? -83.781  37.025 -62.200 1.00 22.31 ? 121  ALA B CB  1 
ATOM   3228 N N   . ASP B 1 122 ? -84.498  39.564 -64.344 1.00 21.93 ? 122  ASP B N   1 
ATOM   3229 C CA  . ASP B 1 122 ? -85.502  40.509 -64.807 1.00 22.22 ? 122  ASP B CA  1 
ATOM   3230 C C   . ASP B 1 122 ? -86.811  39.796 -65.092 1.00 22.76 ? 122  ASP B C   1 
ATOM   3231 O O   . ASP B 1 122 ? -87.863  40.417 -65.165 1.00 23.05 ? 122  ASP B O   1 
ATOM   3232 C CB  . ASP B 1 122 ? -85.039  41.211 -66.091 1.00 21.91 ? 122  ASP B CB  1 
ATOM   3233 C CG  . ASP B 1 122 ? -83.655  41.827 -65.965 1.00 22.28 ? 122  ASP B CG  1 
ATOM   3234 O OD1 . ASP B 1 122 ? -83.442  42.683 -65.067 1.00 24.05 ? 122  ASP B OD1 1 
ATOM   3235 O OD2 . ASP B 1 122 ? -82.712  41.516 -66.717 1.00 20.75 ? 122  ASP B OD2 1 
ATOM   3236 N N   . HIS B 1 123 ? -86.749  38.484 -65.265 1.00 23.46 ? 123  HIS B N   1 
ATOM   3237 C CA  . HIS B 1 123 ? -87.891  37.742 -65.780 1.00 24.09 ? 123  HIS B CA  1 
ATOM   3238 C C   . HIS B 1 123 ? -87.772  36.273 -65.390 1.00 23.53 ? 123  HIS B C   1 
ATOM   3239 O O   . HIS B 1 123 ? -86.673  35.718 -65.378 1.00 23.62 ? 123  HIS B O   1 
ATOM   3240 C CB  . HIS B 1 123 ? -87.942  37.896 -67.307 1.00 24.65 ? 123  HIS B CB  1 
ATOM   3241 C CG  . HIS B 1 123 ? -89.188  37.363 -67.933 1.00 27.89 ? 123  HIS B CG  1 
ATOM   3242 N ND1 . HIS B 1 123 ? -90.236  38.174 -68.310 1.00 31.43 ? 123  HIS B ND1 1 
ATOM   3243 C CD2 . HIS B 1 123 ? -89.553  36.101 -68.255 1.00 29.96 ? 123  HIS B CD2 1 
ATOM   3244 C CE1 . HIS B 1 123 ? -91.194  37.430 -68.838 1.00 32.46 ? 123  HIS B CE1 1 
ATOM   3245 N NE2 . HIS B 1 123 ? -90.804  36.169 -68.815 1.00 31.72 ? 123  HIS B NE2 1 
ATOM   3246 N N   . ILE B 1 124 ? -88.893  35.642 -65.057 1.00 22.96 ? 124  ILE B N   1 
ATOM   3247 C CA  . ILE B 1 124 ? -88.870  34.201 -64.793 1.00 22.66 ? 124  ILE B CA  1 
ATOM   3248 C C   . ILE B 1 124 ? -89.736  33.412 -65.770 1.00 22.82 ? 124  ILE B C   1 
ATOM   3249 O O   . ILE B 1 124 ? -90.878  33.784 -66.032 1.00 22.94 ? 124  ILE B O   1 
ATOM   3250 C CB  . ILE B 1 124 ? -89.262  33.871 -63.328 1.00 22.20 ? 124  ILE B CB  1 
ATOM   3251 C CG1 . ILE B 1 124 ? -88.439  34.708 -62.325 1.00 21.01 ? 124  ILE B CG1 1 
ATOM   3252 C CG2 . ILE B 1 124 ? -89.111  32.362 -63.068 1.00 21.84 ? 124  ILE B CG2 1 
ATOM   3253 C CD1 . ILE B 1 124 ? -86.933  34.354 -62.240 1.00 19.85 ? 124  ILE B CD1 1 
ATOM   3254 N N   . ILE B 1 125 ? -89.178  32.332 -66.311 1.00 22.79 ? 125  ILE B N   1 
ATOM   3255 C CA  . ILE B 1 125 ? -89.965  31.361 -67.067 1.00 22.95 ? 125  ILE B CA  1 
ATOM   3256 C C   . ILE B 1 125 ? -89.922  30.035 -66.345 1.00 23.50 ? 125  ILE B C   1 
ATOM   3257 O O   . ILE B 1 125 ? -88.851  29.481 -66.096 1.00 24.03 ? 125  ILE B O   1 
ATOM   3258 C CB  . ILE B 1 125 ? -89.463  31.223 -68.525 1.00 22.74 ? 125  ILE B CB  1 
ATOM   3259 C CG1 . ILE B 1 125 ? -89.625  32.561 -69.269 1.00 21.82 ? 125  ILE B CG1 1 
ATOM   3260 C CG2 . ILE B 1 125 ? -90.187  30.103 -69.239 1.00 21.66 ? 125  ILE B CG2 1 
ATOM   3261 C CD1 . ILE B 1 125 ? -88.923  32.615 -70.604 1.00 19.62 ? 125  ILE B CD1 1 
ATOM   3262 N N   . THR B 1 126 ? -91.092  29.521 -65.994 1.00 23.93 ? 126  THR B N   1 
ATOM   3263 C CA  . THR B 1 126 ? -91.154  28.279 -65.236 1.00 23.88 ? 126  THR B CA  1 
ATOM   3264 C C   . THR B 1 126 ? -92.336  27.423 -65.688 1.00 23.98 ? 126  THR B C   1 
ATOM   3265 O O   . THR B 1 126 ? -93.111  27.837 -66.539 1.00 23.37 ? 126  THR B O   1 
ATOM   3266 C CB  . THR B 1 126 ? -91.194  28.622 -63.725 1.00 23.75 ? 126  THR B CB  1 
ATOM   3267 O OG1 . THR B 1 126 ? -90.998  27.439 -62.948 1.00 24.51 ? 126  THR B OG1 1 
ATOM   3268 C CG2 . THR B 1 126 ? -92.567  29.146 -63.295 1.00 23.18 ? 126  THR B CG2 1 
ATOM   3269 N N   . MET B 1 127 ? -92.471  26.230 -65.125 1.00 24.73 ? 127  MET B N   1 
ATOM   3270 C CA  . MET B 1 127 ? -93.589  25.360 -65.476 1.00 25.78 ? 127  MET B CA  1 
ATOM   3271 C C   . MET B 1 127 ? -94.301  24.778 -64.264 1.00 26.45 ? 127  MET B C   1 
ATOM   3272 O O   . MET B 1 127 ? -93.713  24.073 -63.462 1.00 26.40 ? 127  MET B O   1 
ATOM   3273 C CB  . MET B 1 127 ? -93.162  24.241 -66.431 1.00 25.89 ? 127  MET B CB  1 
ATOM   3274 C CG  . MET B 1 127 ? -94.339  23.415 -66.965 1.00 26.66 ? 127  MET B CG  1 
ATOM   3275 S SD  . MET B 1 127 ? -93.971  22.374 -68.409 1.00 28.12 ? 127  MET B SD  1 
ATOM   3276 C CE  . MET B 1 127 ? -94.209  23.514 -69.748 1.00 26.87 ? 127  MET B CE  1 
ATOM   3277 N N   . ASP B 1 128 ? -95.588  25.079 -64.162 1.00 27.54 ? 128  ASP B N   1 
ATOM   3278 C CA  . ASP B 1 128 ? -96.445  24.521 -63.141 1.00 28.82 ? 128  ASP B CA  1 
ATOM   3279 C C   . ASP B 1 128 ? -95.880  24.673 -61.732 1.00 28.73 ? 128  ASP B C   1 
ATOM   3280 O O   . ASP B 1 128 ? -95.524  23.692 -61.068 1.00 28.64 ? 128  ASP B O   1 
ATOM   3281 C CB  . ASP B 1 128 ? -96.805  23.070 -63.482 1.00 29.91 ? 128  ASP B CB  1 
ATOM   3282 C CG  . ASP B 1 128 ? -97.948  22.987 -64.468 1.00 32.51 ? 128  ASP B CG  1 
ATOM   3283 O OD1 . ASP B 1 128 ? -99.006  23.600 -64.191 1.00 35.06 ? 128  ASP B OD1 1 
ATOM   3284 O OD2 . ASP B 1 128 ? -97.887  22.354 -65.544 1.00 34.31 ? 128  ASP B OD2 1 
ATOM   3285 N N   . LEU B 1 129 ? -95.806  25.928 -61.294 1.00 28.73 ? 129  LEU B N   1 
ATOM   3286 C CA  . LEU B 1 129 ? -95.452  26.251 -59.926 1.00 28.93 ? 129  LEU B CA  1 
ATOM   3287 C C   . LEU B 1 129 ? -96.334  25.434 -59.012 1.00 29.06 ? 129  LEU B C   1 
ATOM   3288 O O   . LEU B 1 129 ? -97.537  25.313 -59.258 1.00 28.55 ? 129  LEU B O   1 
ATOM   3289 C CB  . LEU B 1 129 ? -95.671  27.731 -59.644 1.00 29.08 ? 129  LEU B CB  1 
ATOM   3290 C CG  . LEU B 1 129 ? -94.696  28.715 -60.284 1.00 29.82 ? 129  LEU B CG  1 
ATOM   3291 C CD1 . LEU B 1 129 ? -95.252  30.149 -60.202 1.00 30.37 ? 129  LEU B CD1 1 
ATOM   3292 C CD2 . LEU B 1 129 ? -93.300  28.620 -59.664 1.00 29.55 ? 129  LEU B CD2 1 
ATOM   3293 N N   . HIS B 1 130 ? -95.732  24.883 -57.956 1.00 29.30 ? 130  HIS B N   1 
ATOM   3294 C CA  . HIS B 1 130 ? -96.461  24.043 -57.013 1.00 29.51 ? 130  HIS B CA  1 
ATOM   3295 C C   . HIS B 1 130 ? -97.658  24.783 -56.451 1.00 29.09 ? 130  HIS B C   1 
ATOM   3296 O O   . HIS B 1 130 ? -98.689  24.180 -56.172 1.00 29.03 ? 130  HIS B O   1 
ATOM   3297 C CB  . HIS B 1 130 ? -95.547  23.581 -55.880 1.00 30.21 ? 130  HIS B CB  1 
ATOM   3298 C CG  . HIS B 1 130 ? -96.257  22.790 -54.826 1.00 31.43 ? 130  HIS B CG  1 
ATOM   3299 N ND1 . HIS B 1 130 ? -96.500  23.284 -53.562 1.00 31.98 ? 130  HIS B ND1 1 
ATOM   3300 C CD2 . HIS B 1 130 ? -96.786  21.543 -54.853 1.00 31.84 ? 130  HIS B CD2 1 
ATOM   3301 C CE1 . HIS B 1 130 ? -97.147  22.375 -52.855 1.00 32.40 ? 130  HIS B CE1 1 
ATOM   3302 N NE2 . HIS B 1 130 ? -97.329  21.309 -53.614 1.00 32.22 ? 130  HIS B NE2 1 
ATOM   3303 N N   . ALA B 1 131 ? -97.500  26.095 -56.274 1.00 28.78 ? 131  ALA B N   1 
ATOM   3304 C CA  . ALA B 1 131 ? -98.604  26.978 -55.913 1.00 28.17 ? 131  ALA B CA  1 
ATOM   3305 C C   . ALA B 1 131 ? -98.519  28.226 -56.763 1.00 27.89 ? 131  ALA B C   1 
ATOM   3306 O O   . ALA B 1 131 ? -97.526  28.944 -56.715 1.00 27.56 ? 131  ALA B O   1 
ATOM   3307 C CB  . ALA B 1 131 ? -98.558  27.323 -54.434 1.00 27.79 ? 131  ALA B CB  1 
ATOM   3308 N N   . SER B 1 132 ? -99.563  28.470 -57.553 1.00 28.05 ? 132  SER B N   1 
ATOM   3309 C CA  . SER B 1 132 ? -99.681  29.685 -58.374 1.00 28.22 ? 132  SER B CA  1 
ATOM   3310 C C   . SER B 1 132 ? -99.266  30.984 -57.658 1.00 27.73 ? 132  SER B C   1 
ATOM   3311 O O   . SER B 1 132 ? -98.662  31.865 -58.273 1.00 27.46 ? 132  SER B O   1 
ATOM   3312 C CB  . SER B 1 132 ? -101.111 29.835 -58.871 1.00 28.47 ? 132  SER B CB  1 
ATOM   3313 O OG  . SER B 1 132 ? -101.317 28.944 -59.941 1.00 30.80 ? 132  SER B OG  1 
ATOM   3314 N N   . GLN B 1 133 ? -99.604  31.077 -56.372 1.00 27.11 ? 133  GLN B N   1 
ATOM   3315 C CA  . GLN B 1 133 ? -99.293  32.234 -55.535 1.00 26.97 ? 133  GLN B CA  1 
ATOM   3316 C C   . GLN B 1 133 ? -97.813  32.595 -55.525 1.00 26.63 ? 133  GLN B C   1 
ATOM   3317 O O   . GLN B 1 133 ? -97.447  33.712 -55.153 1.00 26.84 ? 133  GLN B O   1 
ATOM   3318 C CB  . GLN B 1 133 ? -99.745  31.989 -54.108 1.00 27.02 ? 133  GLN B CB  1 
ATOM   3319 C CG  . GLN B 1 133 ? -101.247 31.984 -53.922 1.00 28.11 ? 133  GLN B CG  1 
ATOM   3320 C CD  . GLN B 1 133 ? -101.858 30.591 -54.033 1.00 30.13 ? 133  GLN B CD  1 
ATOM   3321 O OE1 . GLN B 1 133 ? -101.222 29.651 -54.525 1.00 30.68 ? 133  GLN B OE1 1 
ATOM   3322 N NE2 . GLN B 1 133 ? -103.099 30.461 -53.585 1.00 31.07 ? 133  GLN B NE2 1 
ATOM   3323 N N   . ILE B 1 134 ? -96.966  31.663 -55.955 1.00 26.05 ? 134  ILE B N   1 
ATOM   3324 C CA  . ILE B 1 134 ? -95.523  31.888 -55.939 1.00 25.10 ? 134  ILE B CA  1 
ATOM   3325 C C   . ILE B 1 134 ? -95.158  32.987 -56.931 1.00 24.69 ? 134  ILE B C   1 
ATOM   3326 O O   . ILE B 1 134 ? -94.146  33.647 -56.766 1.00 25.15 ? 134  ILE B O   1 
ATOM   3327 C CB  . ILE B 1 134 ? -94.742  30.539 -56.168 1.00 25.02 ? 134  ILE B CB  1 
ATOM   3328 C CG1 . ILE B 1 134 ? -94.851  29.658 -54.917 1.00 24.20 ? 134  ILE B CG1 1 
ATOM   3329 C CG2 . ILE B 1 134 ? -93.263  30.766 -56.566 1.00 24.59 ? 134  ILE B CG2 1 
ATOM   3330 C CD1 . ILE B 1 134 ? -94.396  28.236 -55.107 1.00 24.46 ? 134  ILE B CD1 1 
ATOM   3331 N N   . GLN B 1 135 ? -95.998  33.216 -57.936 1.00 24.10 ? 135  GLN B N   1 
ATOM   3332 C CA  . GLN B 1 135 ? -95.792  34.347 -58.835 1.00 23.95 ? 135  GLN B CA  1 
ATOM   3333 C C   . GLN B 1 135 ? -95.722  35.638 -58.039 1.00 23.41 ? 135  GLN B C   1 
ATOM   3334 O O   . GLN B 1 135 ? -94.913  36.501 -58.342 1.00 23.47 ? 135  GLN B O   1 
ATOM   3335 C CB  . GLN B 1 135 ? -96.895  34.445 -59.886 1.00 24.17 ? 135  GLN B CB  1 
ATOM   3336 C CG  . GLN B 1 135 ? -96.776  33.445 -61.023 1.00 25.33 ? 135  GLN B CG  1 
ATOM   3337 C CD  . GLN B 1 135 ? -97.522  33.897 -62.285 1.00 27.99 ? 135  GLN B CD  1 
ATOM   3338 O OE1 . GLN B 1 135 ? -97.560  35.075 -62.604 1.00 29.89 ? 135  GLN B OE1 1 
ATOM   3339 N NE2 . GLN B 1 135 ? -98.102  32.960 -62.996 1.00 29.13 ? 135  GLN B NE2 1 
ATOM   3340 N N   . GLY B 1 136 ? -96.562  35.749 -57.007 1.00 22.86 ? 136  GLY B N   1 
ATOM   3341 C CA  . GLY B 1 136 ? -96.577  36.900 -56.122 1.00 22.04 ? 136  GLY B CA  1 
ATOM   3342 C C   . GLY B 1 136 ? -95.386  37.022 -55.167 1.00 21.66 ? 136  GLY B C   1 
ATOM   3343 O O   . GLY B 1 136 ? -95.261  38.009 -54.446 1.00 21.44 ? 136  GLY B O   1 
ATOM   3344 N N   . PHE B 1 137 ? -94.509  36.027 -55.148 1.00 20.99 ? 137  PHE B N   1 
ATOM   3345 C CA  . PHE B 1 137 ? -93.295  36.134 -54.351 1.00 20.54 ? 137  PHE B CA  1 
ATOM   3346 C C   . PHE B 1 137 ? -92.273  37.029 -55.059 1.00 20.51 ? 137  PHE B C   1 
ATOM   3347 O O   . PHE B 1 137 ? -91.240  37.349 -54.489 1.00 20.58 ? 137  PHE B O   1 
ATOM   3348 C CB  . PHE B 1 137 ? -92.691  34.742 -54.056 1.00 20.27 ? 137  PHE B CB  1 
ATOM   3349 C CG  . PHE B 1 137 ? -93.512  33.883 -53.092 1.00 19.93 ? 137  PHE B CG  1 
ATOM   3350 C CD1 . PHE B 1 137 ? -93.100  32.582 -52.785 1.00 19.55 ? 137  PHE B CD1 1 
ATOM   3351 C CD2 . PHE B 1 137 ? -94.684  34.358 -52.504 1.00 19.38 ? 137  PHE B CD2 1 
ATOM   3352 C CE1 . PHE B 1 137 ? -93.839  31.777 -51.915 1.00 19.53 ? 137  PHE B CE1 1 
ATOM   3353 C CE2 . PHE B 1 137 ? -95.437  33.555 -51.634 1.00 18.97 ? 137  PHE B CE2 1 
ATOM   3354 C CZ  . PHE B 1 137 ? -95.022  32.273 -51.329 1.00 19.18 ? 137  PHE B CZ  1 
ATOM   3355 N N   . PHE B 1 138 ? -92.554  37.402 -56.311 1.00 20.67 ? 138  PHE B N   1 
ATOM   3356 C CA  . PHE B 1 138 ? -91.667  38.254 -57.112 1.00 20.84 ? 138  PHE B CA  1 
ATOM   3357 C C   . PHE B 1 138 ? -92.306  39.602 -57.381 1.00 21.48 ? 138  PHE B C   1 
ATOM   3358 O O   . PHE B 1 138 ? -93.538  39.758 -57.300 1.00 21.85 ? 138  PHE B O   1 
ATOM   3359 C CB  . PHE B 1 138 ? -91.388  37.639 -58.490 1.00 20.23 ? 138  PHE B CB  1 
ATOM   3360 C CG  . PHE B 1 138 ? -90.634  36.341 -58.454 1.00 19.66 ? 138  PHE B CG  1 
ATOM   3361 C CD1 . PHE B 1 138 ? -91.317  35.124 -58.285 1.00 17.93 ? 138  PHE B CD1 1 
ATOM   3362 C CD2 . PHE B 1 138 ? -89.240  36.323 -58.606 1.00 18.81 ? 138  PHE B CD2 1 
ATOM   3363 C CE1 . PHE B 1 138 ? -90.636  33.917 -58.270 1.00 17.46 ? 138  PHE B CE1 1 
ATOM   3364 C CE2 . PHE B 1 138 ? -88.535  35.104 -58.600 1.00 18.17 ? 138  PHE B CE2 1 
ATOM   3365 C CZ  . PHE B 1 138 ? -89.236  33.902 -58.431 1.00 17.79 ? 138  PHE B CZ  1 
ATOM   3366 N N   . ASP B 1 139 ? -91.478  40.570 -57.760 1.00 21.78 ? 139  ASP B N   1 
ATOM   3367 C CA  . ASP B 1 139 ? -92.013  41.764 -58.398 1.00 22.18 ? 139  ASP B CA  1 
ATOM   3368 C C   . ASP B 1 139 ? -91.792  41.791 -59.910 1.00 21.91 ? 139  ASP B C   1 
ATOM   3369 O O   . ASP B 1 139 ? -92.575  42.370 -60.641 1.00 22.53 ? 139  ASP B O   1 
ATOM   3370 C CB  . ASP B 1 139 ? -91.502  43.017 -57.705 1.00 22.72 ? 139  ASP B CB  1 
ATOM   3371 C CG  . ASP B 1 139 ? -92.087  43.172 -56.331 1.00 23.59 ? 139  ASP B CG  1 
ATOM   3372 O OD1 . ASP B 1 139 ? -93.327  43.238 -56.201 1.00 24.52 ? 139  ASP B OD1 1 
ATOM   3373 O OD2 . ASP B 1 139 ? -91.385  43.189 -55.311 1.00 25.26 ? 139  ASP B OD2 1 
ATOM   3374 N N   . ILE B 1 140 ? -90.737  41.138 -60.379 1.00 21.60 ? 140  ILE B N   1 
ATOM   3375 C CA  . ILE B 1 140 ? -90.501  40.946 -61.806 1.00 20.86 ? 140  ILE B CA  1 
ATOM   3376 C C   . ILE B 1 140 ? -91.579  39.995 -62.339 1.00 20.87 ? 140  ILE B C   1 
ATOM   3377 O O   . ILE B 1 140 ? -92.150  39.221 -61.578 1.00 20.89 ? 140  ILE B O   1 
ATOM   3378 C CB  . ILE B 1 140 ? -89.085  40.359 -62.020 1.00 20.87 ? 140  ILE B CB  1 
ATOM   3379 C CG1 . ILE B 1 140 ? -88.925  39.028 -61.257 1.00 19.44 ? 140  ILE B CG1 1 
ATOM   3380 C CG2 . ILE B 1 140 ? -87.996  41.393 -61.615 1.00 20.72 ? 140  ILE B CG2 1 
ATOM   3381 C CD1 . ILE B 1 140 ? -87.700  38.244 -61.606 1.00 17.24 ? 140  ILE B CD1 1 
ATOM   3382 N N   . PRO B 1 141 ? -91.896  40.067 -63.628 1.00 20.87 ? 141  PRO B N   1 
ATOM   3383 C CA  . PRO B 1 141 ? -92.887  39.156 -64.205 1.00 20.50 ? 141  PRO B CA  1 
ATOM   3384 C C   . PRO B 1 141 ? -92.434  37.707 -64.237 1.00 20.51 ? 141  PRO B C   1 
ATOM   3385 O O   . PRO B 1 141 ? -91.259  37.386 -64.411 1.00 20.18 ? 141  PRO B O   1 
ATOM   3386 C CB  . PRO B 1 141 ? -93.076  39.691 -65.616 1.00 20.57 ? 141  PRO B CB  1 
ATOM   3387 C CG  . PRO B 1 141 ? -91.850  40.453 -65.895 1.00 20.93 ? 141  PRO B CG  1 
ATOM   3388 C CD  . PRO B 1 141 ? -91.382  41.030 -64.619 1.00 20.87 ? 141  PRO B CD  1 
ATOM   3389 N N   . VAL B 1 142 ? -93.410  36.833 -64.055 1.00 20.95 ? 142  VAL B N   1 
ATOM   3390 C CA  . VAL B 1 142 ? -93.220  35.397 -64.090 1.00 21.34 ? 142  VAL B CA  1 
ATOM   3391 C C   . VAL B 1 142 ? -94.181  34.838 -65.138 1.00 22.20 ? 142  VAL B C   1 
ATOM   3392 O O   . VAL B 1 142 ? -95.357  35.201 -65.178 1.00 22.83 ? 142  VAL B O   1 
ATOM   3393 C CB  . VAL B 1 142 ? -93.524  34.752 -62.698 1.00 21.28 ? 142  VAL B CB  1 
ATOM   3394 C CG1 . VAL B 1 142 ? -93.413  33.202 -62.750 1.00 20.20 ? 142  VAL B CG1 1 
ATOM   3395 C CG2 . VAL B 1 142 ? -92.634  35.357 -61.582 1.00 19.50 ? 142  VAL B CG2 1 
ATOM   3396 N N   . ASP B 1 143 ? -93.681  33.980 -66.010 1.00 22.84 ? 143  ASP B N   1 
ATOM   3397 C CA  . ASP B 1 143 ? -94.572  33.217 -66.862 1.00 23.85 ? 143  ASP B CA  1 
ATOM   3398 C C   . ASP B 1 143 ? -94.596  31.800 -66.322 1.00 24.31 ? 143  ASP B C   1 
ATOM   3399 O O   . ASP B 1 143 ? -93.586  31.079 -66.348 1.00 24.20 ? 143  ASP B O   1 
ATOM   3400 C CB  . ASP B 1 143 ? -94.131  33.267 -68.332 1.00 24.01 ? 143  ASP B CB  1 
ATOM   3401 C CG  . ASP B 1 143 ? -94.237  34.650 -68.912 1.00 24.97 ? 143  ASP B CG  1 
ATOM   3402 O OD1 . ASP B 1 143 ? -95.338  35.250 -68.811 1.00 25.10 ? 143  ASP B OD1 1 
ATOM   3403 O OD2 . ASP B 1 143 ? -93.265  35.232 -69.455 1.00 26.27 ? 143  ASP B OD2 1 
ATOM   3404 N N   . ASN B 1 144 ? -95.750  31.435 -65.782 1.00 25.22 ? 144  ASN B N   1 
ATOM   3405 C CA  . ASN B 1 144 ? -95.967  30.110 -65.222 1.00 25.98 ? 144  ASN B CA  1 
ATOM   3406 C C   . ASN B 1 144 ? -96.667  29.279 -66.276 1.00 26.57 ? 144  ASN B C   1 
ATOM   3407 O O   . ASN B 1 144 ? -97.890  29.341 -66.437 1.00 26.54 ? 144  ASN B O   1 
ATOM   3408 C CB  . ASN B 1 144 ? -96.781  30.190 -63.920 1.00 25.81 ? 144  ASN B CB  1 
ATOM   3409 C CG  . ASN B 1 144 ? -97.033  28.835 -63.312 1.00 26.14 ? 144  ASN B CG  1 
ATOM   3410 O OD1 . ASN B 1 144 ? -96.242  27.912 -63.486 1.00 26.85 ? 144  ASN B OD1 1 
ATOM   3411 N ND2 . ASN B 1 144 ? -98.146  28.701 -62.599 1.00 25.71 ? 144  ASN B ND2 1 
ATOM   3412 N N   . LEU B 1 145 ? -95.861  28.533 -67.019 1.00 27.46 ? 145  LEU B N   1 
ATOM   3413 C CA  . LEU B 1 145 ? -96.349  27.722 -68.122 1.00 28.27 ? 145  LEU B CA  1 
ATOM   3414 C C   . LEU B 1 145 ? -97.056  26.494 -67.593 1.00 29.19 ? 145  LEU B C   1 
ATOM   3415 O O   . LEU B 1 145 ? -96.697  25.957 -66.545 1.00 29.25 ? 145  LEU B O   1 
ATOM   3416 C CB  . LEU B 1 145 ? -95.192  27.302 -69.018 1.00 27.88 ? 145  LEU B CB  1 
ATOM   3417 C CG  . LEU B 1 145 ? -94.409  28.428 -69.682 1.00 27.81 ? 145  LEU B CG  1 
ATOM   3418 C CD1 . LEU B 1 145 ? -93.092  27.883 -70.245 1.00 28.03 ? 145  LEU B CD1 1 
ATOM   3419 C CD2 . LEU B 1 145 ? -95.232  29.110 -70.761 1.00 26.46 ? 145  LEU B CD2 1 
ATOM   3420 N N   . MET B 1 146 ? -98.067  26.056 -68.326 1.00 30.42 ? 146  MET B N   1 
ATOM   3421 C CA  . MET B 1 146 ? -98.850  24.900 -67.932 1.00 31.67 ? 146  MET B CA  1 
ATOM   3422 C C   . MET B 1 146 ? -98.524  23.691 -68.772 1.00 31.38 ? 146  MET B C   1 
ATOM   3423 O O   . MET B 1 146 ? -98.446  23.772 -69.997 1.00 31.31 ? 146  MET B O   1 
ATOM   3424 C CB  . MET B 1 146 ? -100.323 25.197 -68.095 1.00 32.90 ? 146  MET B CB  1 
ATOM   3425 C CG  . MET B 1 146 ? -100.872 26.132 -67.077 1.00 37.22 ? 146  MET B CG  1 
ATOM   3426 S SD  . MET B 1 146 ? -102.583 26.432 -67.463 1.00 45.74 ? 146  MET B SD  1 
ATOM   3427 C CE  . MET B 1 146 ? -102.614 26.360 -69.193 1.00 45.02 ? 146  MET B CE  1 
ATOM   3428 N N   . ALA B 1 147 ? -98.341  22.564 -68.102 1.00 31.39 ? 147  ALA B N   1 
ATOM   3429 C CA  . ALA B 1 147 ? -98.226  21.295 -68.786 1.00 31.52 ? 147  ALA B CA  1 
ATOM   3430 C C   . ALA B 1 147 ? -99.595  20.691 -69.115 1.00 31.40 ? 147  ALA B C   1 
ATOM   3431 O O   . ALA B 1 147 ? -99.659  19.714 -69.851 1.00 31.03 ? 147  ALA B O   1 
ATOM   3432 C CB  . ALA B 1 147 ? -97.391  20.329 -67.968 1.00 31.84 ? 147  ALA B CB  1 
ATOM   3433 N N   . GLU B 1 148 ? -100.672 21.295 -68.602 1.00 31.82 ? 148  GLU B N   1 
ATOM   3434 C CA  . GLU B 1 148 ? -102.053 20.825 -68.823 1.00 32.58 ? 148  GLU B CA  1 
ATOM   3435 C C   . GLU B 1 148 ? -102.386 20.518 -70.300 1.00 32.72 ? 148  GLU B C   1 
ATOM   3436 O O   . GLU B 1 148 ? -102.835 19.404 -70.608 1.00 32.95 ? 148  GLU B O   1 
ATOM   3437 C CB  . GLU B 1 148 ? -103.081 21.790 -68.208 1.00 32.89 ? 148  GLU B CB  1 
ATOM   3438 C CG  . GLU B 1 148 ? -104.542 21.479 -68.514 1.00 34.25 ? 148  GLU B CG  1 
ATOM   3439 C CD  . GLU B 1 148 ? -105.514 22.021 -67.467 1.00 36.42 ? 148  GLU B CD  1 
ATOM   3440 O OE1 . GLU B 1 148 ? -105.158 22.111 -66.275 1.00 38.24 ? 148  GLU B OE1 1 
ATOM   3441 O OE2 . GLU B 1 148 ? -106.659 22.353 -67.822 1.00 37.63 ? 148  GLU B OE2 1 
ATOM   3442 N N   . PRO B 1 149 ? -102.147 21.460 -71.218 1.00 32.49 ? 149  PRO B N   1 
ATOM   3443 C CA  . PRO B 1 149 ? -102.439 21.183 -72.627 1.00 32.41 ? 149  PRO B CA  1 
ATOM   3444 C C   . PRO B 1 149 ? -101.783 19.879 -73.075 1.00 32.27 ? 149  PRO B C   1 
ATOM   3445 O O   . PRO B 1 149 ? -102.438 19.110 -73.770 1.00 32.46 ? 149  PRO B O   1 
ATOM   3446 C CB  . PRO B 1 149 ? -101.851 22.401 -73.365 1.00 32.25 ? 149  PRO B CB  1 
ATOM   3447 C CG  . PRO B 1 149 ? -101.850 23.487 -72.356 1.00 31.91 ? 149  PRO B CG  1 
ATOM   3448 C CD  . PRO B 1 149 ? -101.604 22.822 -71.033 1.00 32.41 ? 149  PRO B CD  1 
ATOM   3449 N N   . ALA B 1 150 ? -100.537 19.633 -72.660 1.00 32.11 ? 150  ALA B N   1 
ATOM   3450 C CA  . ALA B 1 150 ? -99.787  18.437 -73.067 1.00 31.54 ? 150  ALA B CA  1 
ATOM   3451 C C   . ALA B 1 150 ? -100.240 17.187 -72.292 1.00 31.41 ? 150  ALA B C   1 
ATOM   3452 O O   . ALA B 1 150 ? -100.076 16.053 -72.751 1.00 31.46 ? 150  ALA B O   1 
ATOM   3453 C CB  . ALA B 1 150 ? -98.289  18.660 -72.897 1.00 31.10 ? 150  ALA B CB  1 
ATOM   3454 N N   . VAL B 1 151 ? -100.797 17.394 -71.108 1.00 30.90 ? 151  VAL B N   1 
ATOM   3455 C CA  . VAL B 1 151 ? -101.336 16.282 -70.349 1.00 30.27 ? 151  VAL B CA  1 
ATOM   3456 C C   . VAL B 1 151 ? -102.653 15.819 -71.000 1.00 30.44 ? 151  VAL B C   1 
ATOM   3457 O O   . VAL B 1 151 ? -102.846 14.625 -71.230 1.00 30.05 ? 151  VAL B O   1 
ATOM   3458 C CB  . VAL B 1 151 ? -101.487 16.654 -68.864 1.00 29.86 ? 151  VAL B CB  1 
ATOM   3459 C CG1 . VAL B 1 151 ? -102.354 15.647 -68.121 1.00 29.09 ? 151  VAL B CG1 1 
ATOM   3460 C CG2 . VAL B 1 151 ? -100.102 16.753 -68.224 1.00 29.29 ? 151  VAL B CG2 1 
ATOM   3461 N N   . LEU B 1 152 ? -103.522 16.780 -71.323 1.00 30.55 ? 152  LEU B N   1 
ATOM   3462 C CA  . LEU B 1 152 ? -104.807 16.519 -71.974 1.00 30.66 ? 152  LEU B CA  1 
ATOM   3463 C C   . LEU B 1 152 ? -104.643 15.740 -73.277 1.00 31.23 ? 152  LEU B C   1 
ATOM   3464 O O   . LEU B 1 152 ? -105.411 14.810 -73.565 1.00 31.61 ? 152  LEU B O   1 
ATOM   3465 C CB  . LEU B 1 152 ? -105.543 17.831 -72.245 1.00 30.14 ? 152  LEU B CB  1 
ATOM   3466 C CG  . LEU B 1 152 ? -106.053 18.592 -71.014 1.00 29.96 ? 152  LEU B CG  1 
ATOM   3467 C CD1 . LEU B 1 152 ? -106.599 19.947 -71.383 1.00 28.90 ? 152  LEU B CD1 1 
ATOM   3468 C CD2 . LEU B 1 152 ? -107.111 17.800 -70.301 1.00 29.98 ? 152  LEU B CD2 1 
ATOM   3469 N N   . LYS B 1 153 ? -103.624 16.120 -74.042 1.00 31.57 ? 153  LYS B N   1 
ATOM   3470 C CA  . LYS B 1 153 ? -103.335 15.541 -75.347 1.00 31.87 ? 153  LYS B CA  1 
ATOM   3471 C C   . LYS B 1 153 ? -102.728 14.157 -75.187 1.00 31.41 ? 153  LYS B C   1 
ATOM   3472 O O   . LYS B 1 153 ? -103.019 13.253 -75.973 1.00 31.96 ? 153  LYS B O   1 
ATOM   3473 C CB  . LYS B 1 153 ? -102.385 16.467 -76.122 1.00 32.51 ? 153  LYS B CB  1 
ATOM   3474 C CG  . LYS B 1 153 ? -101.447 15.767 -77.096 1.00 34.45 ? 153  LYS B CG  1 
ATOM   3475 C CD  . LYS B 1 153 ? -100.899 16.756 -78.097 1.00 37.68 ? 153  LYS B CD  1 
ATOM   3476 C CE  . LYS B 1 153 ? -101.069 16.233 -79.509 1.00 39.89 ? 153  LYS B CE  1 
ATOM   3477 N NZ  . LYS B 1 153 ? -99.971  15.270 -79.809 1.00 41.37 ? 153  LYS B NZ  1 
ATOM   3478 N N   . TRP B 1 154 ? -101.884 13.989 -74.174 1.00 30.65 ? 154  TRP B N   1 
ATOM   3479 C CA  . TRP B 1 154 ? -101.342 12.675 -73.870 1.00 30.05 ? 154  TRP B CA  1 
ATOM   3480 C C   . TRP B 1 154 ? -102.490 11.726 -73.506 1.00 30.52 ? 154  TRP B C   1 
ATOM   3481 O O   . TRP B 1 154 ? -102.579 10.624 -74.051 1.00 30.52 ? 154  TRP B O   1 
ATOM   3482 C CB  . TRP B 1 154 ? -100.270 12.720 -72.769 1.00 28.95 ? 154  TRP B CB  1 
ATOM   3483 C CG  . TRP B 1 154 ? -99.510  11.439 -72.695 1.00 27.27 ? 154  TRP B CG  1 
ATOM   3484 C CD1 . TRP B 1 154 ? -98.326  11.154 -73.305 1.00 26.19 ? 154  TRP B CD1 1 
ATOM   3485 C CD2 . TRP B 1 154 ? -99.902  10.237 -72.007 1.00 26.29 ? 154  TRP B CD2 1 
ATOM   3486 N NE1 . TRP B 1 154 ? -97.941  9.863  -73.023 1.00 25.93 ? 154  TRP B NE1 1 
ATOM   3487 C CE2 . TRP B 1 154 ? -98.894  9.275  -72.235 1.00 26.30 ? 154  TRP B CE2 1 
ATOM   3488 C CE3 . TRP B 1 154 ? -100.998 9.880  -71.211 1.00 25.66 ? 154  TRP B CE3 1 
ATOM   3489 C CZ2 . TRP B 1 154 ? -98.955  7.978  -71.705 1.00 26.55 ? 154  TRP B CZ2 1 
ATOM   3490 C CZ3 . TRP B 1 154 ? -101.060 8.597  -70.675 1.00 25.68 ? 154  TRP B CZ3 1 
ATOM   3491 C CH2 . TRP B 1 154 ? -100.047 7.660  -70.928 1.00 26.13 ? 154  TRP B CH2 1 
ATOM   3492 N N   . ILE B 1 155 ? -103.356 12.165 -72.596 1.00 30.99 ? 155  ILE B N   1 
ATOM   3493 C CA  . ILE B 1 155 ? -104.507 11.371 -72.164 1.00 31.75 ? 155  ILE B CA  1 
ATOM   3494 C C   . ILE B 1 155 ? -105.368 10.942 -73.362 1.00 32.53 ? 155  ILE B C   1 
ATOM   3495 O O   . ILE B 1 155 ? -105.650 9.757  -73.538 1.00 32.55 ? 155  ILE B O   1 
ATOM   3496 C CB  . ILE B 1 155 ? -105.371 12.142 -71.125 1.00 31.41 ? 155  ILE B CB  1 
ATOM   3497 C CG1 . ILE B 1 155 ? -104.578 12.421 -69.834 1.00 30.82 ? 155  ILE B CG1 1 
ATOM   3498 C CG2 . ILE B 1 155 ? -106.635 11.358 -70.808 1.00 31.28 ? 155  ILE B CG2 1 
ATOM   3499 C CD1 . ILE B 1 155 ? -105.284 13.347 -68.821 1.00 29.00 ? 155  ILE B CD1 1 
ATOM   3500 N N   . ARG B 1 156 ? -105.752 11.906 -74.194 1.00 33.53 ? 156  ARG B N   1 
ATOM   3501 C CA  . ARG B 1 156 ? -106.652 11.645 -75.321 1.00 34.59 ? 156  ARG B CA  1 
ATOM   3502 C C   . ARG B 1 156 ? -106.062 10.636 -76.304 1.00 35.04 ? 156  ARG B C   1 
ATOM   3503 O O   . ARG B 1 156 ? -106.793 9.830  -76.880 1.00 35.25 ? 156  ARG B O   1 
ATOM   3504 C CB  . ARG B 1 156 ? -107.026 12.948 -76.047 1.00 34.93 ? 156  ARG B CB  1 
ATOM   3505 C CG  . ARG B 1 156 ? -108.186 13.746 -75.422 1.00 35.57 ? 156  ARG B CG  1 
ATOM   3506 C CD  . ARG B 1 156 ? -108.678 14.893 -76.301 1.00 36.56 ? 156  ARG B CD  1 
ATOM   3507 N NE  . ARG B 1 156 ? -109.201 16.009 -75.514 1.00 38.46 ? 156  ARG B NE  1 
ATOM   3508 C CZ  . ARG B 1 156 ? -108.548 17.151 -75.276 1.00 39.22 ? 156  ARG B CZ  1 
ATOM   3509 N NH1 . ARG B 1 156 ? -107.327 17.360 -75.778 1.00 38.70 ? 156  ARG B NH1 1 
ATOM   3510 N NH2 . ARG B 1 156 ? -109.130 18.100 -74.540 1.00 39.42 ? 156  ARG B NH2 1 
ATOM   3511 N N   . GLU B 1 157 ? -104.741 10.670 -76.462 1.00 35.54 ? 157  GLU B N   1 
ATOM   3512 C CA  . GLU B 1 157 ? -104.037 9.823  -77.422 1.00 35.91 ? 157  GLU B CA  1 
ATOM   3513 C C   . GLU B 1 157 ? -103.605 8.465  -76.879 1.00 35.62 ? 157  GLU B C   1 
ATOM   3514 O O   . GLU B 1 157 ? -103.413 7.530  -77.653 1.00 35.80 ? 157  GLU B O   1 
ATOM   3515 C CB  . GLU B 1 157 ? -102.823 10.565 -78.002 1.00 36.45 ? 157  GLU B CB  1 
ATOM   3516 C CG  . GLU B 1 157 ? -103.209 11.571 -79.090 1.00 38.26 ? 157  GLU B CG  1 
ATOM   3517 C CD  . GLU B 1 157 ? -102.074 12.469 -79.566 1.00 39.91 ? 157  GLU B CD  1 
ATOM   3518 O OE1 . GLU B 1 157 ? -100.907 12.285 -79.144 1.00 40.98 ? 157  GLU B OE1 1 
ATOM   3519 O OE2 . GLU B 1 157 ? -102.363 13.374 -80.381 1.00 40.73 ? 157  GLU B OE2 1 
ATOM   3520 N N   . ASN B 1 158 ? -103.462 8.329  -75.566 1.00 35.05 ? 158  ASN B N   1 
ATOM   3521 C CA  . ASN B 1 158 ? -102.902 7.089  -75.036 1.00 34.64 ? 158  ASN B CA  1 
ATOM   3522 C C   . ASN B 1 158 ? -103.842 6.256  -74.165 1.00 34.11 ? 158  ASN B C   1 
ATOM   3523 O O   . ASN B 1 158 ? -103.558 5.088  -73.878 1.00 33.64 ? 158  ASN B O   1 
ATOM   3524 C CB  . ASN B 1 158 ? -101.589 7.362  -74.301 1.00 34.93 ? 158  ASN B CB  1 
ATOM   3525 C CG  . ASN B 1 158 ? -100.506 7.858  -75.222 1.00 35.55 ? 158  ASN B CG  1 
ATOM   3526 O OD1 . ASN B 1 158 ? -99.750  7.073  -75.767 1.00 37.38 ? 158  ASN B OD1 1 
ATOM   3527 N ND2 . ASN B 1 158 ? -100.425 9.166  -75.399 1.00 35.52 ? 158  ASN B ND2 1 
ATOM   3528 N N   . ILE B 1 159 ? -104.948 6.858  -73.735 1.00 33.66 ? 159  ILE B N   1 
ATOM   3529 C CA  . ILE B 1 159 ? -105.931 6.130  -72.947 1.00 33.52 ? 159  ILE B CA  1 
ATOM   3530 C C   . ILE B 1 159 ? -107.236 6.040  -73.724 1.00 33.68 ? 159  ILE B C   1 
ATOM   3531 O O   . ILE B 1 159 ? -107.959 7.025  -73.842 1.00 33.48 ? 159  ILE B O   1 
ATOM   3532 C CB  . ILE B 1 159 ? -106.114 6.763  -71.543 1.00 33.37 ? 159  ILE B CB  1 
ATOM   3533 C CG1 . ILE B 1 159 ? -104.781 6.713  -70.780 1.00 33.15 ? 159  ILE B CG1 1 
ATOM   3534 C CG2 . ILE B 1 159 ? -107.232 6.034  -70.748 1.00 32.60 ? 159  ILE B CG2 1 
ATOM   3535 C CD1 . ILE B 1 159 ? -104.727 7.580  -69.559 1.00 32.73 ? 159  ILE B CD1 1 
ATOM   3536 N N   . SER B 1 160 ? -107.526 4.852  -74.262 1.00 33.93 ? 160  SER B N   1 
ATOM   3537 C CA  . SER B 1 160 ? -108.729 4.647  -75.087 1.00 34.13 ? 160  SER B CA  1 
ATOM   3538 C C   . SER B 1 160 ? -110.020 4.982  -74.338 1.00 33.77 ? 160  SER B C   1 
ATOM   3539 O O   . SER B 1 160 ? -110.978 5.475  -74.934 1.00 33.77 ? 160  SER B O   1 
ATOM   3540 C CB  . SER B 1 160 ? -108.797 3.231  -75.665 1.00 34.22 ? 160  SER B CB  1 
ATOM   3541 O OG  . SER B 1 160 ? -107.842 2.373  -75.075 1.00 35.44 ? 160  SER B OG  1 
ATOM   3542 N N   . GLU B 1 161 ? -110.009 4.754  -73.028 1.00 33.28 ? 161  GLU B N   1 
ATOM   3543 C CA  . GLU B 1 161 ? -111.172 4.980  -72.186 1.00 32.81 ? 161  GLU B CA  1 
ATOM   3544 C C   . GLU B 1 161 ? -111.291 6.403  -71.646 1.00 32.16 ? 161  GLU B C   1 
ATOM   3545 O O   . GLU B 1 161 ? -112.107 6.654  -70.761 1.00 32.11 ? 161  GLU B O   1 
ATOM   3546 C CB  . GLU B 1 161 ? -111.179 3.977  -71.020 1.00 33.41 ? 161  GLU B CB  1 
ATOM   3547 C CG  . GLU B 1 161 ? -111.063 2.506  -71.422 1.00 34.76 ? 161  GLU B CG  1 
ATOM   3548 C CD  . GLU B 1 161 ? -109.638 1.976  -71.372 1.00 37.21 ? 161  GLU B CD  1 
ATOM   3549 O OE1 . GLU B 1 161 ? -108.679 2.757  -71.598 1.00 37.66 ? 161  GLU B OE1 1 
ATOM   3550 O OE2 . GLU B 1 161 ? -109.476 0.760  -71.109 1.00 39.32 ? 161  GLU B OE2 1 
ATOM   3551 N N   . TRP B 1 162 ? -110.507 7.338  -72.178 1.00 31.51 ? 162  TRP B N   1 
ATOM   3552 C CA  . TRP B 1 162 ? -110.471 8.693  -71.621 1.00 31.20 ? 162  TRP B CA  1 
ATOM   3553 C C   . TRP B 1 162 ? -111.829 9.387  -71.477 1.00 31.66 ? 162  TRP B C   1 
ATOM   3554 O O   . TRP B 1 162 ? -112.028 10.165 -70.537 1.00 31.39 ? 162  TRP B O   1 
ATOM   3555 C CB  . TRP B 1 162 ? -109.479 9.596  -72.362 1.00 30.80 ? 162  TRP B CB  1 
ATOM   3556 C CG  . TRP B 1 162 ? -109.863 10.056 -73.749 1.00 29.57 ? 162  TRP B CG  1 
ATOM   3557 C CD1 . TRP B 1 162 ? -109.429 9.525  -74.922 1.00 29.06 ? 162  TRP B CD1 1 
ATOM   3558 C CD2 . TRP B 1 162 ? -110.701 11.173 -74.104 1.00 29.09 ? 162  TRP B CD2 1 
ATOM   3559 N NE1 . TRP B 1 162 ? -109.961 10.212 -75.987 1.00 29.49 ? 162  TRP B NE1 1 
ATOM   3560 C CE2 . TRP B 1 162 ? -110.744 11.234 -75.514 1.00 29.08 ? 162  TRP B CE2 1 
ATOM   3561 C CE3 . TRP B 1 162 ? -111.429 12.130 -73.374 1.00 28.15 ? 162  TRP B CE3 1 
ATOM   3562 C CZ2 . TRP B 1 162 ? -111.474 12.215 -76.206 1.00 27.53 ? 162  TRP B CZ2 1 
ATOM   3563 C CZ3 . TRP B 1 162 ? -112.160 13.093 -74.067 1.00 26.74 ? 162  TRP B CZ3 1 
ATOM   3564 C CH2 . TRP B 1 162 ? -112.169 13.130 -75.465 1.00 26.19 ? 162  TRP B CH2 1 
ATOM   3565 N N   . ARG B 1 163 ? -112.755 9.113  -72.401 1.00 32.05 ? 163  ARG B N   1 
ATOM   3566 C CA  . ARG B 1 163 ? -114.100 9.676  -72.307 1.00 32.32 ? 163  ARG B CA  1 
ATOM   3567 C C   . ARG B 1 163 ? -114.862 9.143  -71.089 1.00 31.97 ? 163  ARG B C   1 
ATOM   3568 O O   . ARG B 1 163 ? -115.878 9.697  -70.706 1.00 31.75 ? 163  ARG B O   1 
ATOM   3569 C CB  . ARG B 1 163 ? -114.883 9.448  -73.595 1.00 32.76 ? 163  ARG B CB  1 
ATOM   3570 C CG  . ARG B 1 163 ? -114.431 10.317 -74.747 1.00 34.74 ? 163  ARG B CG  1 
ATOM   3571 C CD  . ARG B 1 163 ? -115.169 10.070 -76.043 1.00 38.73 ? 163  ARG B CD  1 
ATOM   3572 N NE  . ARG B 1 163 ? -114.467 10.657 -77.185 1.00 42.55 ? 163  ARG B NE  1 
ATOM   3573 C CZ  . ARG B 1 163 ? -113.419 10.107 -77.805 1.00 45.05 ? 163  ARG B CZ  1 
ATOM   3574 N NH1 . ARG B 1 163 ? -112.919 8.944  -77.401 1.00 46.18 ? 163  ARG B NH1 1 
ATOM   3575 N NH2 . ARG B 1 163 ? -112.860 10.728 -78.835 1.00 46.42 ? 163  ARG B NH2 1 
ATOM   3576 N N   . ASN B 1 164 ? -114.346 8.089  -70.464 1.00 31.90 ? 164  ASN B N   1 
ATOM   3577 C CA  . ASN B 1 164 ? -114.991 7.511  -69.288 1.00 31.96 ? 164  ASN B CA  1 
ATOM   3578 C C   . ASN B 1 164 ? -114.085 7.344  -68.045 1.00 31.74 ? 164  ASN B C   1 
ATOM   3579 O O   . ASN B 1 164 ? -114.377 6.538  -67.150 1.00 31.93 ? 164  ASN B O   1 
ATOM   3580 C CB  . ASN B 1 164 ? -115.670 6.186  -69.670 1.00 32.12 ? 164  ASN B CB  1 
ATOM   3581 C CG  . ASN B 1 164 ? -116.958 6.397  -70.453 1.00 32.15 ? 164  ASN B CG  1 
ATOM   3582 O OD1 . ASN B 1 164 ? -118.042 6.419  -69.881 1.00 32.31 ? 164  ASN B OD1 1 
ATOM   3583 N ND2 . ASN B 1 164 ? -116.839 6.567  -71.762 1.00 31.82 ? 164  ASN B ND2 1 
ATOM   3584 N N   . CYS B 1 165 ? -113.005 8.122  -67.978 1.00 31.03 ? 165  CYS B N   1 
ATOM   3585 C CA  . CYS B 1 165 ? -112.050 7.991  -66.886 1.00 30.39 ? 165  CYS B CA  1 
ATOM   3586 C C   . CYS B 1 165 ? -112.401 8.911  -65.716 1.00 30.24 ? 165  CYS B C   1 
ATOM   3587 O O   . CYS B 1 165 ? -113.368 9.679  -65.785 1.00 30.14 ? 165  CYS B O   1 
ATOM   3588 C CB  . CYS B 1 165 ? -110.620 8.240  -67.381 1.00 30.18 ? 165  CYS B CB  1 
ATOM   3589 S SG  . CYS B 1 165 ? -110.230 9.977  -67.677 1.00 29.53 ? 165  CYS B SG  1 
ATOM   3590 N N   . THR B 1 166 ? -111.626 8.799  -64.635 1.00 29.78 ? 166  THR B N   1 
ATOM   3591 C CA  . THR B 1 166 ? -111.731 9.688  -63.493 1.00 29.20 ? 166  THR B CA  1 
ATOM   3592 C C   . THR B 1 166 ? -110.349 10.257 -63.209 1.00 28.79 ? 166  THR B C   1 
ATOM   3593 O O   . THR B 1 166 ? -109.355 9.511  -63.136 1.00 28.73 ? 166  THR B O   1 
ATOM   3594 C CB  . THR B 1 166 ? -112.266 8.945  -62.255 1.00 29.49 ? 166  THR B CB  1 
ATOM   3595 O OG1 . THR B 1 166 ? -113.616 8.530  -62.483 1.00 30.53 ? 166  THR B OG1 1 
ATOM   3596 C CG2 . THR B 1 166 ? -112.425 9.893  -61.073 1.00 29.48 ? 166  THR B CG2 1 
ATOM   3597 N N   . ILE B 1 167 ? -110.294 11.580 -63.070 1.00 27.99 ? 167  ILE B N   1 
ATOM   3598 C CA  . ILE B 1 167 ? -109.073 12.270 -62.678 1.00 27.36 ? 167  ILE B CA  1 
ATOM   3599 C C   . ILE B 1 167 ? -109.032 12.365 -61.153 1.00 27.11 ? 167  ILE B C   1 
ATOM   3600 O O   . ILE B 1 167 ? -109.972 12.838 -60.528 1.00 26.96 ? 167  ILE B O   1 
ATOM   3601 C CB  . ILE B 1 167 ? -108.974 13.675 -63.354 1.00 27.21 ? 167  ILE B CB  1 
ATOM   3602 C CG1 . ILE B 1 167 ? -109.290 13.598 -64.867 1.00 26.14 ? 167  ILE B CG1 1 
ATOM   3603 C CG2 . ILE B 1 167 ? -107.590 14.314 -63.103 1.00 26.55 ? 167  ILE B CG2 1 
ATOM   3604 C CD1 . ILE B 1 167 ? -108.497 12.543 -65.665 1.00 23.89 ? 167  ILE B CD1 1 
ATOM   3605 N N   . VAL B 1 168 ? -107.945 11.885 -60.561 1.00 26.90 ? 168  VAL B N   1 
ATOM   3606 C CA  . VAL B 1 168 ? -107.841 11.798 -59.114 1.00 26.84 ? 168  VAL B CA  1 
ATOM   3607 C C   . VAL B 1 168 ? -106.707 12.665 -58.614 1.00 27.41 ? 168  VAL B C   1 
ATOM   3608 O O   . VAL B 1 168 ? -105.583 12.584 -59.124 1.00 27.87 ? 168  VAL B O   1 
ATOM   3609 C CB  . VAL B 1 168 ? -107.610 10.329 -58.639 1.00 26.52 ? 168  VAL B CB  1 
ATOM   3610 C CG1 . VAL B 1 168 ? -107.820 10.196 -57.130 1.00 25.98 ? 168  VAL B CG1 1 
ATOM   3611 C CG2 . VAL B 1 168 ? -108.511 9.375  -59.374 1.00 26.08 ? 168  VAL B CG2 1 
ATOM   3612 N N   . SER B 1 169 ? -106.992 13.496 -57.621 1.00 27.90 ? 169  SER B N   1 
ATOM   3613 C CA  . SER B 1 169 ? -105.929 14.183 -56.898 1.00 28.72 ? 169  SER B CA  1 
ATOM   3614 C C   . SER B 1 169 ? -105.401 13.280 -55.794 1.00 28.97 ? 169  SER B C   1 
ATOM   3615 O O   . SER B 1 169 ? -106.188 12.711 -55.050 1.00 28.67 ? 169  SER B O   1 
ATOM   3616 C CB  . SER B 1 169 ? -106.428 15.491 -56.277 1.00 29.04 ? 169  SER B CB  1 
ATOM   3617 O OG  . SER B 1 169 ? -105.330 16.214 -55.728 1.00 29.50 ? 169  SER B OG  1 
ATOM   3618 N N   . PRO B 1 170 ? -104.079 13.149 -55.686 1.00 29.62 ? 170  PRO B N   1 
ATOM   3619 C CA  . PRO B 1 170 ? -103.471 12.385 -54.592 1.00 30.35 ? 170  PRO B CA  1 
ATOM   3620 C C   . PRO B 1 170 ? -103.612 13.070 -53.242 1.00 31.24 ? 170  PRO B C   1 
ATOM   3621 O O   . PRO B 1 170 ? -103.434 12.418 -52.228 1.00 31.50 ? 170  PRO B O   1 
ATOM   3622 C CB  . PRO B 1 170 ? -101.997 12.278 -55.001 1.00 30.44 ? 170  PRO B CB  1 
ATOM   3623 C CG  . PRO B 1 170 ? -101.760 13.398 -55.922 1.00 30.38 ? 170  PRO B CG  1 
ATOM   3624 C CD  . PRO B 1 170 ? -103.069 13.686 -56.616 1.00 29.76 ? 170  PRO B CD  1 
ATOM   3625 N N   . ASP B 1 171 ? -103.943 14.356 -53.219 1.00 32.45 ? 171  ASP B N   1 
ATOM   3626 C CA  . ASP B 1 171 ? -104.187 15.037 -51.949 1.00 33.76 ? 171  ASP B CA  1 
ATOM   3627 C C   . ASP B 1 171 ? -105.311 16.057 -52.057 1.00 34.37 ? 171  ASP B C   1 
ATOM   3628 O O   . ASP B 1 171 ? -105.913 16.222 -53.123 1.00 34.28 ? 171  ASP B O   1 
ATOM   3629 C CB  . ASP B 1 171 ? -102.912 15.690 -51.425 1.00 34.26 ? 171  ASP B CB  1 
ATOM   3630 C CG  . ASP B 1 171 ? -102.284 16.633 -52.432 1.00 35.89 ? 171  ASP B CG  1 
ATOM   3631 O OD1 . ASP B 1 171 ? -103.038 17.355 -53.137 1.00 38.07 ? 171  ASP B OD1 1 
ATOM   3632 O OD2 . ASP B 1 171 ? -101.049 16.728 -52.581 1.00 36.85 ? 171  ASP B OD2 1 
ATOM   3633 N N   . ALA B 1 172 ? -105.595 16.721 -50.941 1.00 35.27 ? 172  ALA B N   1 
ATOM   3634 C CA  . ALA B 1 172 ? -106.654 17.726 -50.863 1.00 36.09 ? 172  ALA B CA  1 
ATOM   3635 C C   . ALA B 1 172 ? -106.247 18.998 -51.590 1.00 36.46 ? 172  ALA B C   1 
ATOM   3636 O O   . ALA B 1 172 ? -107.069 19.638 -52.232 1.00 36.44 ? 172  ALA B O   1 
ATOM   3637 C CB  . ALA B 1 172 ? -106.996 18.028 -49.402 1.00 36.42 ? 172  ALA B CB  1 
ATOM   3638 N N   . GLY B 1 173 ? -104.964 19.341 -51.505 1.00 37.19 ? 173  GLY B N   1 
ATOM   3639 C CA  . GLY B 1 173 ? -104.420 20.491 -52.208 1.00 37.78 ? 173  GLY B CA  1 
ATOM   3640 C C   . GLY B 1 173 ? -104.670 20.511 -53.713 1.00 38.23 ? 173  GLY B C   1 
ATOM   3641 O O   . GLY B 1 173 ? -104.824 21.589 -54.295 1.00 38.74 ? 173  GLY B O   1 
ATOM   3642 N N   . GLY B 1 174 ? -104.726 19.336 -54.344 1.00 38.16 ? 174  GLY B N   1 
ATOM   3643 C CA  . GLY B 1 174 ? -104.775 19.244 -55.798 1.00 37.98 ? 174  GLY B CA  1 
ATOM   3644 C C   . GLY B 1 174 ? -106.157 19.246 -56.438 1.00 38.03 ? 174  GLY B C   1 
ATOM   3645 O O   . GLY B 1 174 ? -106.290 18.999 -57.647 1.00 38.20 ? 174  GLY B O   1 
ATOM   3646 N N   . ALA B 1 175 ? -107.179 19.530 -55.640 1.00 37.83 ? 175  ALA B N   1 
ATOM   3647 C CA  . ALA B 1 175 ? -108.555 19.519 -56.103 1.00 38.28 ? 175  ALA B CA  1 
ATOM   3648 C C   . ALA B 1 175 ? -108.780 20.333 -57.372 1.00 38.87 ? 175  ALA B C   1 
ATOM   3649 O O   . ALA B 1 175 ? -109.289 19.811 -58.368 1.00 39.32 ? 175  ALA B O   1 
ATOM   3650 C CB  . ALA B 1 175 ? -109.474 19.998 -55.004 1.00 38.27 ? 175  ALA B CB  1 
ATOM   3651 N N   . LYS B 1 176 ? -108.407 21.608 -57.324 1.00 39.33 ? 176  LYS B N   1 
ATOM   3652 C CA  . LYS B 1 176 ? -108.605 22.546 -58.428 1.00 39.76 ? 176  LYS B CA  1 
ATOM   3653 C C   . LYS B 1 176 ? -107.988 22.026 -59.717 1.00 39.08 ? 176  LYS B C   1 
ATOM   3654 O O   . LYS B 1 176 ? -108.656 21.942 -60.751 1.00 39.16 ? 176  LYS B O   1 
ATOM   3655 C CB  . LYS B 1 176 ? -107.992 23.905 -58.072 1.00 40.57 ? 176  LYS B CB  1 
ATOM   3656 C CG  . LYS B 1 176 ? -108.785 25.091 -58.582 1.00 43.35 ? 176  LYS B CG  1 
ATOM   3657 C CD  . LYS B 1 176 ? -108.971 26.131 -57.482 1.00 46.73 ? 176  LYS B CD  1 
ATOM   3658 C CE  . LYS B 1 176 ? -110.165 27.043 -57.789 1.00 48.87 ? 176  LYS B CE  1 
ATOM   3659 N NZ  . LYS B 1 176 ? -111.070 27.196 -56.595 1.00 49.60 ? 176  LYS B NZ  1 
ATOM   3660 N N   . ARG B 1 177 ? -106.715 21.661 -59.638 1.00 38.37 ? 177  ARG B N   1 
ATOM   3661 C CA  . ARG B 1 177 ? -105.995 21.086 -60.761 1.00 37.97 ? 177  ARG B CA  1 
ATOM   3662 C C   . ARG B 1 177 ? -106.698 19.884 -61.397 1.00 37.12 ? 177  ARG B C   1 
ATOM   3663 O O   . ARG B 1 177 ? -106.754 19.797 -62.624 1.00 37.39 ? 177  ARG B O   1 
ATOM   3664 C CB  . ARG B 1 177 ? -104.596 20.694 -60.324 1.00 38.54 ? 177  ARG B CB  1 
ATOM   3665 C CG  . ARG B 1 177 ? -103.675 20.340 -61.458 1.00 40.76 ? 177  ARG B CG  1 
ATOM   3666 C CD  . ARG B 1 177 ? -102.493 19.487 -61.047 1.00 44.11 ? 177  ARG B CD  1 
ATOM   3667 N NE  . ARG B 1 177 ? -102.033 19.786 -59.693 1.00 46.50 ? 177  ARG B NE  1 
ATOM   3668 C CZ  . ARG B 1 177 ? -101.242 20.801 -59.372 1.00 47.96 ? 177  ARG B CZ  1 
ATOM   3669 N NH1 . ARG B 1 177 ? -100.809 21.637 -60.319 1.00 48.55 ? 177  ARG B NH1 1 
ATOM   3670 N NH2 . ARG B 1 177 ? -100.884 20.977 -58.098 1.00 48.31 ? 177  ARG B NH2 1 
ATOM   3671 N N   . VAL B 1 178 ? -107.232 18.960 -60.592 1.00 35.87 ? 178  VAL B N   1 
ATOM   3672 C CA  . VAL B 1 178 ? -107.950 17.828 -61.189 1.00 34.88 ? 178  VAL B CA  1 
ATOM   3673 C C   . VAL B 1 178 ? -109.329 18.189 -61.741 1.00 34.32 ? 178  VAL B C   1 
ATOM   3674 O O   . VAL B 1 178 ? -109.679 17.711 -62.812 1.00 34.30 ? 178  VAL B O   1 
ATOM   3675 C CB  . VAL B 1 178 ? -107.952 16.504 -60.336 1.00 34.77 ? 178  VAL B CB  1 
ATOM   3676 C CG1 . VAL B 1 178 ? -106.546 16.142 -59.912 1.00 34.13 ? 178  VAL B CG1 1 
ATOM   3677 C CG2 . VAL B 1 178 ? -108.915 16.548 -59.146 1.00 34.70 ? 178  VAL B CG2 1 
ATOM   3678 N N   . THR B 1 179 ? -110.092 19.032 -61.040 1.00 33.65 ? 179  THR B N   1 
ATOM   3679 C CA  . THR B 1 179 ? -111.426 19.416 -61.521 1.00 33.23 ? 179  THR B CA  1 
ATOM   3680 C C   . THR B 1 179 ? -111.343 20.138 -62.862 1.00 32.94 ? 179  THR B C   1 
ATOM   3681 O O   . THR B 1 179 ? -112.175 19.925 -63.740 1.00 32.73 ? 179  THR B O   1 
ATOM   3682 C CB  . THR B 1 179 ? -112.187 20.312 -60.504 1.00 33.27 ? 179  THR B CB  1 
ATOM   3683 O OG1 . THR B 1 179 ? -111.339 21.384 -60.062 1.00 33.38 ? 179  THR B OG1 1 
ATOM   3684 C CG2 . THR B 1 179 ? -112.523 19.542 -59.229 1.00 32.74 ? 179  THR B CG2 1 
ATOM   3685 N N   . SER B 1 180 ? -110.334 20.995 -63.006 1.00 32.68 ? 180  SER B N   1 
ATOM   3686 C CA  . SER B 1 180 ? -110.105 21.722 -64.252 1.00 32.35 ? 180  SER B CA  1 
ATOM   3687 C C   . SER B 1 180 ? -109.815 20.768 -65.414 1.00 32.12 ? 180  SER B C   1 
ATOM   3688 O O   . SER B 1 180 ? -110.303 20.984 -66.519 1.00 32.50 ? 180  SER B O   1 
ATOM   3689 C CB  . SER B 1 180 ? -108.981 22.757 -64.073 1.00 32.40 ? 180  SER B CB  1 
ATOM   3690 O OG  . SER B 1 180 ? -108.215 22.919 -65.260 1.00 32.95 ? 180  SER B OG  1 
ATOM   3691 N N   . ILE B 1 181 ? -109.029 19.719 -65.166 1.00 31.89 ? 181  ILE B N   1 
ATOM   3692 C CA  . ILE B 1 181 ? -108.771 18.686 -66.183 1.00 31.79 ? 181  ILE B CA  1 
ATOM   3693 C C   . ILE B 1 181 ? -110.010 17.812 -66.437 1.00 31.91 ? 181  ILE B C   1 
ATOM   3694 O O   . ILE B 1 181 ? -110.302 17.444 -67.584 1.00 32.22 ? 181  ILE B O   1 
ATOM   3695 C CB  . ILE B 1 181 ? -107.521 17.814 -65.823 1.00 31.62 ? 181  ILE B CB  1 
ATOM   3696 C CG1 . ILE B 1 181 ? -106.235 18.656 -65.865 1.00 31.41 ? 181  ILE B CG1 1 
ATOM   3697 C CG2 . ILE B 1 181 ? -107.398 16.603 -66.758 1.00 31.10 ? 181  ILE B CG2 1 
ATOM   3698 C CD1 . ILE B 1 181 ? -104.991 17.928 -65.387 1.00 30.70 ? 181  ILE B CD1 1 
ATOM   3699 N N   . ALA B 1 182 ? -110.738 17.493 -65.373 1.00 31.89 ? 182  ALA B N   1 
ATOM   3700 C CA  . ALA B 1 182 ? -111.945 16.683 -65.486 1.00 32.23 ? 182  ALA B CA  1 
ATOM   3701 C C   . ALA B 1 182 ? -113.065 17.406 -66.242 1.00 32.64 ? 182  ALA B C   1 
ATOM   3702 O O   . ALA B 1 182 ? -113.795 16.781 -67.015 1.00 32.87 ? 182  ALA B O   1 
ATOM   3703 C CB  . ALA B 1 182 ? -112.418 16.214 -64.107 1.00 31.81 ? 182  ALA B CB  1 
ATOM   3704 N N   . ASP B 1 183 ? -113.190 18.713 -66.030 1.00 33.02 ? 183  ASP B N   1 
ATOM   3705 C CA  . ASP B 1 183 ? -114.198 19.510 -66.724 1.00 33.66 ? 183  ASP B CA  1 
ATOM   3706 C C   . ASP B 1 183 ? -113.853 19.704 -68.204 1.00 33.91 ? 183  ASP B C   1 
ATOM   3707 O O   . ASP B 1 183 ? -114.734 19.610 -69.070 1.00 33.72 ? 183  ASP B O   1 
ATOM   3708 C CB  . ASP B 1 183 ? -114.389 20.864 -66.037 1.00 33.74 ? 183  ASP B CB  1 
ATOM   3709 C CG  . ASP B 1 183 ? -115.006 20.746 -64.652 1.00 34.97 ? 183  ASP B CG  1 
ATOM   3710 O OD1 . ASP B 1 183 ? -115.389 19.627 -64.220 1.00 35.95 ? 183  ASP B OD1 1 
ATOM   3711 O OD2 . ASP B 1 183 ? -115.135 21.742 -63.908 1.00 36.13 ? 183  ASP B OD2 1 
ATOM   3712 N N   . ARG B 1 184 ? -112.578 19.977 -68.492 1.00 34.41 ? 184  ARG B N   1 
ATOM   3713 C CA  . ARG B 1 184 ? -112.104 20.089 -69.885 1.00 34.78 ? 184  ARG B CA  1 
ATOM   3714 C C   . ARG B 1 184 ? -112.361 18.804 -70.674 1.00 33.96 ? 184  ARG B C   1 
ATOM   3715 O O   . ARG B 1 184 ? -112.788 18.853 -71.828 1.00 34.12 ? 184  ARG B O   1 
ATOM   3716 C CB  . ARG B 1 184 ? -110.607 20.436 -69.946 1.00 35.62 ? 184  ARG B CB  1 
ATOM   3717 C CG  . ARG B 1 184 ? -110.277 21.934 -69.801 1.00 38.77 ? 184  ARG B CG  1 
ATOM   3718 C CD  . ARG B 1 184 ? -109.051 22.376 -70.608 1.00 43.67 ? 184  ARG B CD  1 
ATOM   3719 N NE  . ARG B 1 184 ? -108.504 23.673 -70.189 1.00 47.89 ? 184  ARG B NE  1 
ATOM   3720 C CZ  . ARG B 1 184 ? -107.224 24.053 -70.335 1.00 50.59 ? 184  ARG B CZ  1 
ATOM   3721 N NH1 . ARG B 1 184 ? -106.327 23.230 -70.882 1.00 50.91 ? 184  ARG B NH1 1 
ATOM   3722 N NH2 . ARG B 1 184 ? -106.835 25.264 -69.924 1.00 52.21 ? 184  ARG B NH2 1 
ATOM   3723 N N   . LEU B 1 185 ? -112.086 17.658 -70.055 1.00 32.92 ? 185  LEU B N   1 
ATOM   3724 C CA  . LEU B 1 185 ? -112.274 16.371 -70.715 1.00 32.08 ? 185  LEU B CA  1 
ATOM   3725 C C   . LEU B 1 185 ? -113.726 15.894 -70.610 1.00 31.82 ? 185  LEU B C   1 
ATOM   3726 O O   . LEU B 1 185 ? -114.121 14.949 -71.279 1.00 32.15 ? 185  LEU B O   1 
ATOM   3727 C CB  . LEU B 1 185 ? -111.336 15.322 -70.122 1.00 31.71 ? 185  LEU B CB  1 
ATOM   3728 C CG  . LEU B 1 185 ? -109.849 15.340 -70.481 1.00 31.28 ? 185  LEU B CG  1 
ATOM   3729 C CD1 . LEU B 1 185 ? -109.109 14.314 -69.613 1.00 31.24 ? 185  LEU B CD1 1 
ATOM   3730 C CD2 . LEU B 1 185 ? -109.603 15.065 -71.968 1.00 30.49 ? 185  LEU B CD2 1 
ATOM   3731 N N   . ASN B 1 186 ? -114.505 16.567 -69.768 1.00 31.36 ? 186  ASN B N   1 
ATOM   3732 C CA  . ASN B 1 186 ? -115.899 16.232 -69.491 1.00 30.86 ? 186  ASN B CA  1 
ATOM   3733 C C   . ASN B 1 186 ? -116.093 14.834 -68.890 1.00 30.32 ? 186  ASN B C   1 
ATOM   3734 O O   . ASN B 1 186 ? -116.894 14.042 -69.383 1.00 30.21 ? 186  ASN B O   1 
ATOM   3735 C CB  . ASN B 1 186 ? -116.810 16.500 -70.702 1.00 31.15 ? 186  ASN B CB  1 
ATOM   3736 C CG  . ASN B 1 186 ? -118.302 16.413 -70.353 1.00 32.53 ? 186  ASN B CG  1 
ATOM   3737 O OD1 . ASN B 1 186 ? -119.087 15.842 -71.112 1.00 35.04 ? 186  ASN B OD1 1 
ATOM   3738 N ND2 . ASN B 1 186 ? -118.692 16.964 -69.206 1.00 32.08 ? 186  ASN B ND2 1 
ATOM   3739 N N   . VAL B 1 187 ? -115.351 14.574 -67.809 1.00 29.72 ? 187  VAL B N   1 
ATOM   3740 C CA  . VAL B 1 187 ? -115.381 13.318 -67.047 1.00 28.99 ? 187  VAL B CA  1 
ATOM   3741 C C   . VAL B 1 187 ? -115.441 13.634 -65.549 1.00 29.00 ? 187  VAL B C   1 
ATOM   3742 O O   . VAL B 1 187 ? -115.549 14.800 -65.171 1.00 28.90 ? 187  VAL B O   1 
ATOM   3743 C CB  . VAL B 1 187 ? -114.140 12.401 -67.363 1.00 28.71 ? 187  VAL B CB  1 
ATOM   3744 C CG1 . VAL B 1 187 ? -114.068 12.088 -68.829 1.00 28.20 ? 187  VAL B CG1 1 
ATOM   3745 C CG2 . VAL B 1 187 ? -112.806 13.038 -66.905 1.00 27.90 ? 187  VAL B CG2 1 
ATOM   3746 N N   . ASP B 1 188 ? -115.371 12.602 -64.707 1.00 29.23 ? 188  ASP B N   1 
ATOM   3747 C CA  . ASP B 1 188 ? -115.379 12.776 -63.250 1.00 29.72 ? 188  ASP B CA  1 
ATOM   3748 C C   . ASP B 1 188 ? -114.010 13.071 -62.659 1.00 29.52 ? 188  ASP B C   1 
ATOM   3749 O O   . ASP B 1 188 ? -112.971 12.928 -63.317 1.00 29.46 ? 188  ASP B O   1 
ATOM   3750 C CB  . ASP B 1 188 ? -115.921 11.530 -62.534 1.00 30.33 ? 188  ASP B CB  1 
ATOM   3751 C CG  . ASP B 1 188 ? -117.171 10.981 -63.166 1.00 31.80 ? 188  ASP B CG  1 
ATOM   3752 O OD1 . ASP B 1 188 ? -117.900 11.745 -63.848 1.00 33.10 ? 188  ASP B OD1 1 
ATOM   3753 O OD2 . ASP B 1 188 ? -117.496 9.786  -63.024 1.00 33.05 ? 188  ASP B OD2 1 
ATOM   3754 N N   . PHE B 1 189 ? -114.029 13.462 -61.391 1.00 29.39 ? 189  PHE B N   1 
ATOM   3755 C CA  . PHE B 1 189 ? -112.819 13.615 -60.607 1.00 29.69 ? 189  PHE B CA  1 
ATOM   3756 C C   . PHE B 1 189 ? -113.045 12.942 -59.267 1.00 29.97 ? 189  PHE B C   1 
ATOM   3757 O O   . PHE B 1 189 ? -114.184 12.742 -58.831 1.00 30.34 ? 189  PHE B O   1 
ATOM   3758 C CB  . PHE B 1 189 ? -112.480 15.098 -60.404 1.00 29.70 ? 189  PHE B CB  1 
ATOM   3759 C CG  . PHE B 1 189 ? -113.398 15.797 -59.439 1.00 29.61 ? 189  PHE B CG  1 
ATOM   3760 C CD1 . PHE B 1 189 ? -113.077 15.887 -58.089 1.00 29.56 ? 189  PHE B CD1 1 
ATOM   3761 C CD2 . PHE B 1 189 ? -114.599 16.341 -59.879 1.00 29.49 ? 189  PHE B CD2 1 
ATOM   3762 C CE1 . PHE B 1 189 ? -113.933 16.528 -57.190 1.00 29.34 ? 189  PHE B CE1 1 
ATOM   3763 C CE2 . PHE B 1 189 ? -115.456 16.978 -58.991 1.00 29.71 ? 189  PHE B CE2 1 
ATOM   3764 C CZ  . PHE B 1 189 ? -115.127 17.071 -57.647 1.00 29.35 ? 189  PHE B CZ  1 
ATOM   3765 N N   . ALA B 1 190 ? -111.957 12.577 -58.616 1.00 30.23 ? 190  ALA B N   1 
ATOM   3766 C CA  . ALA B 1 190 ? -112.038 12.008 -57.283 1.00 30.63 ? 190  ALA B CA  1 
ATOM   3767 C C   . ALA B 1 190 ? -110.862 12.573 -56.530 1.00 30.87 ? 190  ALA B C   1 
ATOM   3768 O O   . ALA B 1 190 ? -109.972 13.170 -57.126 1.00 30.59 ? 190  ALA B O   1 
ATOM   3769 C CB  . ALA B 1 190 ? -111.991 10.483 -57.322 1.00 30.32 ? 190  ALA B CB  1 
ATOM   3770 N N   . LEU B 1 191 ? -110.855 12.385 -55.224 1.00 31.61 ? 191  LEU B N   1 
ATOM   3771 C CA  . LEU B 1 191 ? -109.850 13.007 -54.408 1.00 32.60 ? 191  LEU B CA  1 
ATOM   3772 C C   . LEU B 1 191 ? -109.482 12.140 -53.238 1.00 33.15 ? 191  LEU B C   1 
ATOM   3773 O O   . LEU B 1 191 ? -110.358 11.684 -52.522 1.00 33.53 ? 191  LEU B O   1 
ATOM   3774 C CB  . LEU B 1 191 ? -110.405 14.321 -53.892 1.00 33.06 ? 191  LEU B CB  1 
ATOM   3775 C CG  . LEU B 1 191 ? -109.367 15.289 -53.370 1.00 34.09 ? 191  LEU B CG  1 
ATOM   3776 C CD1 . LEU B 1 191 ? -109.676 16.650 -53.956 1.00 34.97 ? 191  LEU B CD1 1 
ATOM   3777 C CD2 . LEU B 1 191 ? -109.388 15.281 -51.841 1.00 35.05 ? 191  LEU B CD2 1 
ATOM   3778 N N   . ILE B 1 192 ? -108.182 11.952 -53.032 1.00 33.80 ? 192  ILE B N   1 
ATOM   3779 C CA  . ILE B 1 192 ? -107.659 11.253 -51.869 1.00 34.47 ? 192  ILE B CA  1 
ATOM   3780 C C   . ILE B 1 192 ? -107.141 12.210 -50.786 1.00 35.60 ? 192  ILE B C   1 
ATOM   3781 O O   . ILE B 1 192 ? -106.555 13.241 -51.094 1.00 35.46 ? 192  ILE B O   1 
ATOM   3782 C CB  . ILE B 1 192 ? -106.561 10.260 -52.313 1.00 34.32 ? 192  ILE B CB  1 
ATOM   3783 C CG1 . ILE B 1 192 ? -107.215 9.047  -52.993 1.00 33.93 ? 192  ILE B CG1 1 
ATOM   3784 C CG2 . ILE B 1 192 ? -105.658 9.857  -51.131 1.00 33.80 ? 192  ILE B CG2 1 
ATOM   3785 C CD1 . ILE B 1 192 ? -106.272 8.123  -53.677 1.00 33.27 ? 192  ILE B CD1 1 
ATOM   3786 N N   . HIS B 1 193 ? -107.365 11.847 -49.523 1.00 37.00 ? 193  HIS B N   1 
ATOM   3787 C CA  . HIS B 1 193 ? -106.838 12.564 -48.371 1.00 38.41 ? 193  HIS B CA  1 
ATOM   3788 C C   . HIS B 1 193 ? -106.202 11.620 -47.330 1.00 39.78 ? 193  HIS B C   1 
ATOM   3789 O O   . HIS B 1 193 ? -106.850 10.693 -46.838 1.00 39.59 ? 193  HIS B O   1 
ATOM   3790 C CB  . HIS B 1 193 ? -107.956 13.395 -47.731 1.00 38.45 ? 193  HIS B CB  1 
ATOM   3791 C CG  . HIS B 1 193 ? -107.587 13.998 -46.412 1.00 38.15 ? 193  HIS B CG  1 
ATOM   3792 N ND1 . HIS B 1 193 ? -106.402 14.670 -46.206 1.00 38.26 ? 193  HIS B ND1 1 
ATOM   3793 C CD2 . HIS B 1 193 ? -108.246 14.028 -45.231 1.00 38.15 ? 193  HIS B CD2 1 
ATOM   3794 C CE1 . HIS B 1 193 ? -106.348 15.093 -44.956 1.00 38.54 ? 193  HIS B CE1 1 
ATOM   3795 N NE2 . HIS B 1 193 ? -107.454 14.714 -44.342 1.00 38.57 ? 193  HIS B NE2 1 
ATOM   3796 N N   . LYS B 1 194 ? -104.931 11.864 -47.015 1.00 41.66 ? 194  LYS B N   1 
ATOM   3797 C CA  . LYS B 1 194 ? -104.211 11.176 -45.943 1.00 43.63 ? 194  LYS B CA  1 
ATOM   3798 C C   . LYS B 1 194 ? -104.629 11.792 -44.607 1.00 44.54 ? 194  LYS B C   1 
ATOM   3799 O O   . LYS B 1 194 ? -104.403 12.978 -44.367 1.00 44.59 ? 194  LYS B O   1 
ATOM   3800 C CB  . LYS B 1 194 ? -102.692 11.349 -46.130 1.00 44.20 ? 194  LYS B CB  1 
ATOM   3801 C CG  . LYS B 1 194 ? -101.804 10.093 -45.895 1.00 46.35 ? 194  LYS B CG  1 
ATOM   3802 C CD  . LYS B 1 194 ? -101.809 9.606  -44.434 1.00 49.55 ? 194  LYS B CD  1 
ATOM   3803 C CE  . LYS B 1 194 ? -100.603 10.122 -43.617 1.00 51.94 ? 194  LYS B CE  1 
ATOM   3804 N NZ  . LYS B 1 194 ? -100.581 9.588  -42.190 1.00 52.85 ? 194  LYS B NZ  1 
ATOM   3805 N N   . GLU B 1 195 ? -105.241 10.990 -43.743 1.00 45.65 ? 195  GLU B N   1 
ATOM   3806 C CA  . GLU B 1 195 ? -105.663 11.459 -42.418 1.00 46.69 ? 195  GLU B CA  1 
ATOM   3807 C C   . GLU B 1 195 ? -104.535 11.384 -41.380 1.00 46.91 ? 195  GLU B C   1 
ATOM   3808 O O   . GLU B 1 195 ? -103.360 11.174 -41.721 1.00 46.96 ? 195  GLU B O   1 
ATOM   3809 C CB  . GLU B 1 195 ? -106.882 10.672 -41.935 1.00 47.17 ? 195  GLU B CB  1 
ATOM   3810 C CG  . GLU B 1 195 ? -108.197 11.122 -42.562 1.00 49.18 ? 195  GLU B CG  1 
ATOM   3811 C CD  . GLU B 1 195 ? -109.316 10.109 -42.392 1.00 51.74 ? 195  GLU B CD  1 
ATOM   3812 O OE1 . GLU B 1 195 ? -109.018 8.944  -42.048 1.00 52.49 ? 195  GLU B OE1 1 
ATOM   3813 O OE2 . GLU B 1 195 ? -110.499 10.478 -42.602 1.00 53.09 ? 195  GLU B OE2 1 
ATOM   3814 N N   . ASP B 1 203 ? -102.048 6.336  -40.152 1.00 59.67 ? 203  ASP B N   1 
ATOM   3815 C CA  . ASP B 1 203 ? -101.693 6.556  -41.555 1.00 59.63 ? 203  ASP B CA  1 
ATOM   3816 C C   . ASP B 1 203 ? -102.774 5.988  -42.489 1.00 58.29 ? 203  ASP B C   1 
ATOM   3817 O O   . ASP B 1 203 ? -102.679 4.833  -42.931 1.00 58.78 ? 203  ASP B O   1 
ATOM   3818 C CB  . ASP B 1 203 ? -100.317 5.930  -41.857 1.00 60.59 ? 203  ASP B CB  1 
ATOM   3819 C CG  . ASP B 1 203 ? -99.778  6.316  -43.236 1.00 63.09 ? 203  ASP B CG  1 
ATOM   3820 O OD1 . ASP B 1 203 ? -100.197 5.698  -44.252 1.00 64.84 ? 203  ASP B OD1 1 
ATOM   3821 O OD2 . ASP B 1 203 ? -98.922  7.222  -43.397 1.00 65.04 ? 203  ASP B OD2 1 
ATOM   3822 N N   . ARG B 1 204 ? -103.788 6.799  -42.797 1.00 56.13 ? 204  ARG B N   1 
ATOM   3823 C CA  . ARG B 1 204 ? -104.965 6.320  -43.533 1.00 53.97 ? 204  ARG B CA  1 
ATOM   3824 C C   . ARG B 1 204 ? -105.419 7.212  -44.693 1.00 51.28 ? 204  ARG B C   1 
ATOM   3825 O O   . ARG B 1 204 ? -105.555 8.425  -44.533 1.00 51.23 ? 204  ARG B O   1 
ATOM   3826 C CB  . ARG B 1 204 ? -106.125 6.148  -42.564 1.00 54.80 ? 204  ARG B CB  1 
ATOM   3827 C CG  . ARG B 1 204 ? -106.928 4.913  -42.808 1.00 57.62 ? 204  ARG B CG  1 
ATOM   3828 C CD  . ARG B 1 204 ? -107.858 4.561  -41.665 1.00 62.16 ? 204  ARG B CD  1 
ATOM   3829 N NE  . ARG B 1 204 ? -108.894 5.573  -41.447 1.00 65.60 ? 204  ARG B NE  1 
ATOM   3830 C CZ  . ARG B 1 204 ? -109.805 5.943  -42.350 1.00 67.81 ? 204  ARG B CZ  1 
ATOM   3831 N NH1 . ARG B 1 204 ? -109.822 5.403  -43.572 1.00 68.62 ? 204  ARG B NH1 1 
ATOM   3832 N NH2 . ARG B 1 204 ? -110.704 6.868  -42.028 1.00 68.56 ? 204  ARG B NH2 1 
ATOM   3833 N N   . MET B 1 205 ? -105.674 6.610  -45.852 1.00 47.84 ? 205  MET B N   1 
ATOM   3834 C CA  . MET B 1 205 ? -106.194 7.361  -46.993 1.00 44.56 ? 205  MET B CA  1 
ATOM   3835 C C   . MET B 1 205 ? -107.700 7.264  -47.092 1.00 42.96 ? 205  MET B C   1 
ATOM   3836 O O   . MET B 1 205 ? -108.274 6.211  -46.817 1.00 42.71 ? 205  MET B O   1 
ATOM   3837 C CB  . MET B 1 205 ? -105.573 6.885  -48.302 1.00 43.87 ? 205  MET B CB  1 
ATOM   3838 C CG  . MET B 1 205 ? -104.252 7.518  -48.584 1.00 41.36 ? 205  MET B CG  1 
ATOM   3839 S SD  . MET B 1 205 ? -103.466 6.955  -50.076 1.00 37.35 ? 205  MET B SD  1 
ATOM   3840 C CE  . MET B 1 205 ? -102.137 8.180  -50.139 1.00 36.80 ? 205  MET B CE  1 
ATOM   3841 N N   . VAL B 1 206 ? -108.328 8.366  -47.490 1.00 40.98 ? 206  VAL B N   1 
ATOM   3842 C CA  . VAL B 1 206 ? -109.761 8.385  -47.760 1.00 39.25 ? 206  VAL B CA  1 
ATOM   3843 C C   . VAL B 1 206 ? -110.059 8.918  -49.158 1.00 38.40 ? 206  VAL B C   1 
ATOM   3844 O O   . VAL B 1 206 ? -109.572 9.975  -49.569 1.00 38.01 ? 206  VAL B O   1 
ATOM   3845 C CB  . VAL B 1 206 ? -110.565 9.153  -46.690 1.00 39.08 ? 206  VAL B CB  1 
ATOM   3846 C CG1 . VAL B 1 206 ? -110.594 8.364  -45.397 1.00 38.91 ? 206  VAL B CG1 1 
ATOM   3847 C CG2 . VAL B 1 206 ? -109.980 10.530 -46.439 1.00 38.98 ? 206  VAL B CG2 1 
ATOM   3848 N N   . LEU B 1 207 ? -110.858 8.163  -49.897 1.00 37.42 ? 207  LEU B N   1 
ATOM   3849 C CA  . LEU B 1 207 ? -111.193 8.534  -51.255 1.00 36.47 ? 207  LEU B CA  1 
ATOM   3850 C C   . LEU B 1 207 ? -112.631 9.008  -51.287 1.00 36.22 ? 207  LEU B C   1 
ATOM   3851 O O   . LEU B 1 207 ? -113.522 8.323  -50.784 1.00 36.10 ? 207  LEU B O   1 
ATOM   3852 C CB  . LEU B 1 207 ? -110.995 7.345  -52.193 1.00 36.20 ? 207  LEU B CB  1 
ATOM   3853 C CG  . LEU B 1 207 ? -111.530 7.465  -53.620 1.00 35.88 ? 207  LEU B CG  1 
ATOM   3854 C CD1 . LEU B 1 207 ? -110.581 8.275  -54.519 1.00 35.34 ? 207  LEU B CD1 1 
ATOM   3855 C CD2 . LEU B 1 207 ? -111.753 6.084  -54.183 1.00 35.99 ? 207  LEU B CD2 1 
ATOM   3856 N N   . VAL B 1 208 ? -112.832 10.201 -51.847 1.00 35.90 ? 208  VAL B N   1 
ATOM   3857 C CA  . VAL B 1 208 ? -114.155 10.725 -52.153 1.00 35.66 ? 208  VAL B CA  1 
ATOM   3858 C C   . VAL B 1 208 ? -114.260 10.828 -53.671 1.00 36.29 ? 208  VAL B C   1 
ATOM   3859 O O   . VAL B 1 208 ? -113.312 11.253 -54.329 1.00 36.39 ? 208  VAL B O   1 
ATOM   3860 C CB  . VAL B 1 208 ? -114.440 12.102 -51.458 1.00 35.26 ? 208  VAL B CB  1 
ATOM   3861 C CG1 . VAL B 1 208 ? -114.492 11.945 -49.948 1.00 35.01 ? 208  VAL B CG1 1 
ATOM   3862 C CG2 . VAL B 1 208 ? -113.429 13.175 -51.842 1.00 33.92 ? 208  VAL B CG2 1 
ATOM   3863 N N   . GLY B 1 209 ? -115.392 10.411 -54.231 1.00 37.05 ? 209  GLY B N   1 
ATOM   3864 C CA  . GLY B 1 209 ? -115.578 10.429 -55.673 1.00 37.91 ? 209  GLY B CA  1 
ATOM   3865 C C   . GLY B 1 209 ? -115.613 9.044  -56.301 1.00 38.71 ? 209  GLY B C   1 
ATOM   3866 O O   . GLY B 1 209 ? -115.169 8.065  -55.708 1.00 38.43 ? 209  GLY B O   1 
ATOM   3867 N N   . ASP B 1 210 ? -116.128 8.983  -57.525 1.00 39.76 ? 210  ASP B N   1 
ATOM   3868 C CA  . ASP B 1 210 ? -116.438 7.724  -58.192 1.00 40.93 ? 210  ASP B CA  1 
ATOM   3869 C C   . ASP B 1 210 ? -115.285 7.246  -59.077 1.00 40.39 ? 210  ASP B C   1 
ATOM   3870 O O   . ASP B 1 210 ? -114.912 7.924  -60.041 1.00 40.27 ? 210  ASP B O   1 
ATOM   3871 C CB  . ASP B 1 210 ? -117.739 7.875  -59.008 1.00 41.97 ? 210  ASP B CB  1 
ATOM   3872 C CG  . ASP B 1 210 ? -118.134 6.593  -59.754 1.00 45.04 ? 210  ASP B CG  1 
ATOM   3873 O OD1 . ASP B 1 210 ? -118.403 6.694  -60.977 1.00 47.46 ? 210  ASP B OD1 1 
ATOM   3874 O OD2 . ASP B 1 210 ? -118.220 5.454  -59.205 1.00 47.55 ? 210  ASP B OD2 1 
ATOM   3875 N N   . VAL B 1 211 ? -114.716 6.090  -58.728 1.00 39.88 ? 211  VAL B N   1 
ATOM   3876 C CA  . VAL B 1 211 ? -113.683 5.459  -59.557 1.00 39.46 ? 211  VAL B CA  1 
ATOM   3877 C C   . VAL B 1 211 ? -114.047 4.047  -60.019 1.00 39.41 ? 211  VAL B C   1 
ATOM   3878 O O   . VAL B 1 211 ? -113.305 3.439  -60.781 1.00 38.98 ? 211  VAL B O   1 
ATOM   3879 C CB  . VAL B 1 211 ? -112.273 5.461  -58.893 1.00 39.28 ? 211  VAL B CB  1 
ATOM   3880 C CG1 . VAL B 1 211 ? -111.783 6.887  -58.650 1.00 38.80 ? 211  VAL B CG1 1 
ATOM   3881 C CG2 . VAL B 1 211 ? -112.259 4.632  -57.607 1.00 38.74 ? 211  VAL B CG2 1 
ATOM   3882 N N   . LYS B 1 212 ? -115.196 3.542  -59.576 1.00 39.87 ? 212  LYS B N   1 
ATOM   3883 C CA  . LYS B 1 212 ? -115.604 2.172  -59.895 1.00 40.32 ? 212  LYS B CA  1 
ATOM   3884 C C   . LYS B 1 212 ? -115.743 1.900  -61.392 1.00 39.87 ? 212  LYS B C   1 
ATOM   3885 O O   . LYS B 1 212 ? -116.459 2.614  -62.086 1.00 39.85 ? 212  LYS B O   1 
ATOM   3886 C CB  . LYS B 1 212 ? -116.887 1.775  -59.160 1.00 40.76 ? 212  LYS B CB  1 
ATOM   3887 C CG  . LYS B 1 212 ? -117.021 0.261  -59.024 1.00 42.57 ? 212  LYS B CG  1 
ATOM   3888 C CD  . LYS B 1 212 ? -118.327 -0.147 -58.370 1.00 45.51 ? 212  LYS B CD  1 
ATOM   3889 C CE  . LYS B 1 212 ? -118.456 -1.676 -58.308 1.00 47.65 ? 212  LYS B CE  1 
ATOM   3890 N NZ  . LYS B 1 212 ? -117.173 -2.350 -57.920 1.00 48.81 ? 212  LYS B NZ  1 
ATOM   3891 N N   . ASP B 1 213 ? -115.031 0.868  -61.860 1.00 39.52 ? 213  ASP B N   1 
ATOM   3892 C CA  . ASP B 1 213 ? -115.038 0.406  -63.254 1.00 39.31 ? 213  ASP B CA  1 
ATOM   3893 C C   . ASP B 1 213 ? -114.534 1.410  -64.271 1.00 38.46 ? 213  ASP B C   1 
ATOM   3894 O O   . ASP B 1 213 ? -114.772 1.260  -65.473 1.00 38.63 ? 213  ASP B O   1 
ATOM   3895 C CB  . ASP B 1 213 ? -116.427 -0.050 -63.673 1.00 40.10 ? 213  ASP B CB  1 
ATOM   3896 C CG  . ASP B 1 213 ? -116.670 -1.486 -63.362 1.00 42.11 ? 213  ASP B CG  1 
ATOM   3897 O OD1 . ASP B 1 213 ? -117.184 -1.775 -62.260 1.00 43.72 ? 213  ASP B OD1 1 
ATOM   3898 O OD2 . ASP B 1 213 ? -116.381 -2.395 -64.169 1.00 44.49 ? 213  ASP B OD2 1 
ATOM   3899 N N   . ARG B 1 214 ? -113.836 2.425  -63.785 1.00 37.21 ? 214  ARG B N   1 
ATOM   3900 C CA  . ARG B 1 214 ? -113.258 3.450  -64.632 1.00 35.97 ? 214  ARG B CA  1 
ATOM   3901 C C   . ARG B 1 214 ? -111.735 3.398  -64.558 1.00 34.63 ? 214  ARG B C   1 
ATOM   3902 O O   . ARG B 1 214 ? -111.156 2.928  -63.571 1.00 34.46 ? 214  ARG B O   1 
ATOM   3903 C CB  . ARG B 1 214 ? -113.731 4.828  -64.176 1.00 36.45 ? 214  ARG B CB  1 
ATOM   3904 C CG  . ARG B 1 214 ? -115.220 5.069  -64.356 1.00 37.55 ? 214  ARG B CG  1 
ATOM   3905 C CD  . ARG B 1 214 ? -115.731 6.350  -63.720 1.00 40.27 ? 214  ARG B CD  1 
ATOM   3906 N NE  . ARG B 1 214 ? -116.937 6.777  -64.424 1.00 43.95 ? 214  ARG B NE  1 
ATOM   3907 C CZ  . ARG B 1 214 ? -116.993 7.745  -65.339 1.00 45.88 ? 214  ARG B CZ  1 
ATOM   3908 N NH1 . ARG B 1 214 ? -115.911 8.456  -65.662 1.00 46.42 ? 214  ARG B NH1 1 
ATOM   3909 N NH2 . ARG B 1 214 ? -118.153 8.015  -65.924 1.00 47.33 ? 214  ARG B NH2 1 
ATOM   3910 N N   . VAL B 1 215 ? -111.090 3.881  -65.612 1.00 32.70 ? 215  VAL B N   1 
ATOM   3911 C CA  . VAL B 1 215 ? -109.660 4.126  -65.570 1.00 30.97 ? 215  VAL B CA  1 
ATOM   3912 C C   . VAL B 1 215 ? -109.450 5.334  -64.668 1.00 30.44 ? 215  VAL B C   1 
ATOM   3913 O O   . VAL B 1 215 ? -110.147 6.349  -64.797 1.00 30.63 ? 215  VAL B O   1 
ATOM   3914 C CB  . VAL B 1 215 ? -109.104 4.374  -66.982 1.00 30.77 ? 215  VAL B CB  1 
ATOM   3915 C CG1 . VAL B 1 215 ? -107.623 4.763  -66.935 1.00 30.55 ? 215  VAL B CG1 1 
ATOM   3916 C CG2 . VAL B 1 215 ? -109.328 3.137  -67.864 1.00 29.43 ? 215  VAL B CG2 1 
ATOM   3917 N N   . ALA B 1 216 ? -108.535 5.200  -63.716 1.00 29.44 ? 216  ALA B N   1 
ATOM   3918 C CA  . ALA B 1 216 ? -108.210 6.293  -62.810 1.00 28.81 ? 216  ALA B CA  1 
ATOM   3919 C C   . ALA B 1 216 ? -106.867 6.887  -63.195 1.00 28.38 ? 216  ALA B C   1 
ATOM   3920 O O   . ALA B 1 216 ? -105.884 6.166  -63.370 1.00 28.28 ? 216  ALA B O   1 
ATOM   3921 C CB  . ALA B 1 216 ? -108.205 5.825  -61.336 1.00 28.35 ? 216  ALA B CB  1 
ATOM   3922 N N   . ILE B 1 217 ? -106.842 8.204  -63.352 1.00 28.00 ? 217  ILE B N   1 
ATOM   3923 C CA  . ILE B 1 217 ? -105.607 8.912  -63.654 1.00 27.63 ? 217  ILE B CA  1 
ATOM   3924 C C   . ILE B 1 217 ? -105.263 9.826  -62.489 1.00 27.90 ? 217  ILE B C   1 
ATOM   3925 O O   . ILE B 1 217 ? -105.906 10.867 -62.293 1.00 27.66 ? 217  ILE B O   1 
ATOM   3926 C CB  . ILE B 1 217 ? -105.711 9.740  -64.955 1.00 27.23 ? 217  ILE B CB  1 
ATOM   3927 C CG1 . ILE B 1 217 ? -106.400 8.945  -66.075 1.00 27.00 ? 217  ILE B CG1 1 
ATOM   3928 C CG2 . ILE B 1 217 ? -104.326 10.208 -65.371 1.00 26.77 ? 217  ILE B CG2 1 
ATOM   3929 C CD1 . ILE B 1 217 ? -106.598 9.719  -67.394 1.00 25.57 ? 217  ILE B CD1 1 
ATOM   3930 N N   . LEU B 1 218 ? -104.263 9.426  -61.710 1.00 28.22 ? 218  LEU B N   1 
ATOM   3931 C CA  . LEU B 1 218 ? -103.720 10.297 -60.679 1.00 28.66 ? 218  LEU B CA  1 
ATOM   3932 C C   . LEU B 1 218 ? -102.968 11.416 -61.375 1.00 29.01 ? 218  LEU B C   1 
ATOM   3933 O O   . LEU B 1 218 ? -102.053 11.161 -62.149 1.00 28.95 ? 218  LEU B O   1 
ATOM   3934 C CB  . LEU B 1 218 ? -102.778 9.539  -59.736 1.00 28.46 ? 218  LEU B CB  1 
ATOM   3935 C CG  . LEU B 1 218 ? -103.426 8.749  -58.604 1.00 28.19 ? 218  LEU B CG  1 
ATOM   3936 C CD1 . LEU B 1 218 ? -102.526 7.596  -58.180 1.00 27.70 ? 218  LEU B CD1 1 
ATOM   3937 C CD2 . LEU B 1 218 ? -103.759 9.656  -57.425 1.00 28.30 ? 218  LEU B CD2 1 
ATOM   3938 N N   . VAL B 1 219 ? -103.387 12.649 -61.123 1.00 29.61 ? 219  VAL B N   1 
ATOM   3939 C CA  . VAL B 1 219 ? -102.722 13.808 -61.694 1.00 30.29 ? 219  VAL B CA  1 
ATOM   3940 C C   . VAL B 1 219 ? -102.173 14.658 -60.565 1.00 30.96 ? 219  VAL B C   1 
ATOM   3941 O O   . VAL B 1 219 ? -102.896 14.979 -59.626 1.00 31.19 ? 219  VAL B O   1 
ATOM   3942 C CB  . VAL B 1 219 ? -103.668 14.629 -62.609 1.00 29.96 ? 219  VAL B CB  1 
ATOM   3943 C CG1 . VAL B 1 219 ? -103.029 15.925 -63.003 1.00 30.32 ? 219  VAL B CG1 1 
ATOM   3944 C CG2 . VAL B 1 219 ? -103.999 13.853 -63.857 1.00 29.63 ? 219  VAL B CG2 1 
ATOM   3945 N N   . ASP B 1 220 ? -100.889 14.996 -60.650 1.00 31.79 ? 220  ASP B N   1 
ATOM   3946 C CA  . ASP B 1 220 ? -100.258 15.887 -59.683 1.00 32.81 ? 220  ASP B CA  1 
ATOM   3947 C C   . ASP B 1 220 ? -99.180  16.764 -60.330 1.00 33.22 ? 220  ASP B C   1 
ATOM   3948 O O   . ASP B 1 220 ? -98.760  16.528 -61.463 1.00 33.32 ? 220  ASP B O   1 
ATOM   3949 C CB  . ASP B 1 220 ? -99.673  15.069 -58.539 1.00 33.18 ? 220  ASP B CB  1 
ATOM   3950 C CG  . ASP B 1 220 ? -99.628  15.827 -57.228 1.00 34.64 ? 220  ASP B CG  1 
ATOM   3951 O OD1 . ASP B 1 220 ? -100.143 16.966 -57.143 1.00 35.66 ? 220  ASP B OD1 1 
ATOM   3952 O OD2 . ASP B 1 220 ? -99.088  15.346 -56.215 1.00 36.10 ? 220  ASP B OD2 1 
ATOM   3953 N N   . ASP B 1 221 ? -98.734  17.789 -59.622 1.00 33.68 ? 221  ASP B N   1 
ATOM   3954 C CA  . ASP B 1 221 ? -97.701  18.645 -60.177 1.00 34.29 ? 221  ASP B CA  1 
ATOM   3955 C C   . ASP B 1 221 ? -96.319  18.017 -60.017 1.00 34.54 ? 221  ASP B C   1 
ATOM   3956 O O   . ASP B 1 221 ? -95.449  18.198 -60.868 1.00 35.05 ? 221  ASP B O   1 
ATOM   3957 C CB  . ASP B 1 221 ? -97.779  20.056 -59.596 1.00 34.38 ? 221  ASP B CB  1 
ATOM   3958 C CG  . ASP B 1 221 ? -97.090  20.180 -58.261 1.00 35.41 ? 221  ASP B CG  1 
ATOM   3959 O OD1 . ASP B 1 221 ? -97.621  19.658 -57.263 1.00 35.37 ? 221  ASP B OD1 1 
ATOM   3960 O OD2 . ASP B 1 221 ? -96.008  20.793 -58.120 1.00 37.57 ? 221  ASP B OD2 1 
ATOM   3961 N N   . MET B 1 222 ? -96.121  17.262 -58.945 1.00 34.85 ? 222  MET B N   1 
ATOM   3962 C CA  . MET B 1 222 ? -94.849  16.574 -58.733 1.00 35.13 ? 222  MET B CA  1 
ATOM   3963 C C   . MET B 1 222 ? -94.954  15.266 -57.967 1.00 34.65 ? 222  MET B C   1 
ATOM   3964 O O   . MET B 1 222 ? -95.869  15.066 -57.173 1.00 34.42 ? 222  MET B O   1 
ATOM   3965 C CB  . MET B 1 222 ? -93.828  17.484 -58.044 1.00 35.70 ? 222  MET B CB  1 
ATOM   3966 C CG  . MET B 1 222 ? -94.199  17.933 -56.643 1.00 37.85 ? 222  MET B CG  1 
ATOM   3967 S SD  . MET B 1 222 ? -92.886  18.954 -55.925 1.00 42.34 ? 222  MET B SD  1 
ATOM   3968 C CE  . MET B 1 222 ? -93.041  20.538 -56.837 1.00 41.27 ? 222  MET B CE  1 
ATOM   3969 N N   . ALA B 1 223 ? -93.990  14.388 -58.233 1.00 34.49 ? 223  ALA B N   1 
ATOM   3970 C CA  . ALA B 1 223 ? -93.766  13.179 -57.451 1.00 34.12 ? 223  ALA B CA  1 
ATOM   3971 C C   . ALA B 1 223 ? -92.305  13.123 -57.017 1.00 34.08 ? 223  ALA B C   1 
ATOM   3972 O O   . ALA B 1 223 ? -91.389  13.297 -57.833 1.00 33.77 ? 223  ALA B O   1 
ATOM   3973 C CB  . ALA B 1 223 ? -94.115  11.964 -58.258 1.00 33.89 ? 223  ALA B CB  1 
ATOM   3974 N N   . ASP B 1 224 ? -92.099  12.888 -55.723 1.00 34.23 ? 224  ASP B N   1 
ATOM   3975 C CA  . ASP B 1 224 ? -90.761  12.716 -55.162 1.00 34.24 ? 224  ASP B CA  1 
ATOM   3976 C C   . ASP B 1 224 ? -90.440  11.244 -54.896 1.00 34.39 ? 224  ASP B C   1 
ATOM   3977 O O   . ASP B 1 224 ? -90.084  10.522 -55.825 1.00 34.38 ? 224  ASP B O   1 
ATOM   3978 C CB  . ASP B 1 224 ? -90.600  13.529 -53.890 1.00 34.15 ? 224  ASP B CB  1 
ATOM   3979 C CG  . ASP B 1 224 ? -89.165  13.890 -53.618 1.00 34.39 ? 224  ASP B CG  1 
ATOM   3980 O OD1 . ASP B 1 224 ? -88.255  13.328 -54.283 1.00 33.38 ? 224  ASP B OD1 1 
ATOM   3981 O OD2 . ASP B 1 224 ? -88.863  14.740 -52.753 1.00 34.87 ? 224  ASP B OD2 1 
ATOM   3982 N N   . THR B 1 225 ? -90.566  10.815 -53.639 1.00 34.48 ? 225  THR B N   1 
ATOM   3983 C CA  . THR B 1 225 ? -90.316  9.425  -53.250 1.00 34.95 ? 225  THR B CA  1 
ATOM   3984 C C   . THR B 1 225 ? -91.457  8.507  -53.662 1.00 35.33 ? 225  THR B C   1 
ATOM   3985 O O   . THR B 1 225 ? -91.340  7.279  -53.549 1.00 35.99 ? 225  THR B O   1 
ATOM   3986 C CB  . THR B 1 225 ? -90.112  9.294  -51.727 1.00 35.07 ? 225  THR B CB  1 
ATOM   3987 O OG1 . THR B 1 225 ? -91.351  9.575  -51.060 1.00 35.49 ? 225  THR B OG1 1 
ATOM   3988 C CG2 . THR B 1 225 ? -89.129  10.366 -51.187 1.00 34.55 ? 225  THR B CG2 1 
ATOM   3989 N N   . CYS B 1 226 ? -92.563  9.109  -54.107 1.00 35.05 ? 226  CYS B N   1 
ATOM   3990 C CA  . CYS B 1 226 ? -93.706  8.405  -54.698 1.00 34.80 ? 226  CYS B CA  1 
ATOM   3991 C C   . CYS B 1 226 ? -94.500  7.531  -53.739 1.00 34.68 ? 226  CYS B C   1 
ATOM   3992 O O   . CYS B 1 226 ? -95.370  6.775  -54.173 1.00 34.85 ? 226  CYS B O   1 
ATOM   3993 C CB  . CYS B 1 226 ? -93.286  7.592  -55.925 1.00 34.79 ? 226  CYS B CB  1 
ATOM   3994 S SG  . CYS B 1 226 ? -92.639  8.598  -57.258 1.00 34.54 ? 226  CYS B SG  1 
ATOM   3995 N N   . GLY B 1 227 ? -94.218  7.641  -52.446 1.00 34.47 ? 227  GLY B N   1 
ATOM   3996 C CA  . GLY B 1 227 ? -94.956  6.893  -51.440 1.00 34.31 ? 227  GLY B CA  1 
ATOM   3997 C C   . GLY B 1 227 ? -96.440  7.214  -51.487 1.00 34.31 ? 227  GLY B C   1 
ATOM   3998 O O   . GLY B 1 227 ? -97.281  6.355  -51.203 1.00 34.44 ? 227  GLY B O   1 
ATOM   3999 N N   . THR B 1 228 ? -96.753  8.449  -51.881 1.00 34.02 ? 228  THR B N   1 
ATOM   4000 C CA  . THR B 1 228 ? -98.124  8.950  -51.910 1.00 33.77 ? 228  THR B CA  1 
ATOM   4001 C C   . THR B 1 228 ? -98.881  8.399  -53.117 1.00 33.39 ? 228  THR B C   1 
ATOM   4002 O O   . THR B 1 228 ? -99.917  7.759  -52.943 1.00 33.44 ? 228  THR B O   1 
ATOM   4003 C CB  . THR B 1 228 ? -98.148  10.523 -51.846 1.00 33.94 ? 228  THR B CB  1 
ATOM   4004 O OG1 . THR B 1 228 ? -97.839  10.952 -50.513 1.00 32.85 ? 228  THR B OG1 1 
ATOM   4005 C CG2 . THR B 1 228 ? -99.569  11.091 -52.087 1.00 34.25 ? 228  THR B CG2 1 
ATOM   4006 N N   . ILE B 1 229 ? -98.359  8.611  -54.326 1.00 33.08 ? 229  ILE B N   1 
ATOM   4007 C CA  . ILE B 1 229 ? -99.004  8.052  -55.527 1.00 32.81 ? 229  ILE B CA  1 
ATOM   4008 C C   . ILE B 1 229 ? -99.088  6.522  -55.531 1.00 32.51 ? 229  ILE B C   1 
ATOM   4009 O O   . ILE B 1 229 ? -100.084 5.965  -55.997 1.00 32.44 ? 229  ILE B O   1 
ATOM   4010 C CB  . ILE B 1 229 ? -98.380  8.568  -56.873 1.00 32.95 ? 229  ILE B CB  1 
ATOM   4011 C CG1 . ILE B 1 229 ? -96.845  8.517  -56.860 1.00 33.66 ? 229  ILE B CG1 1 
ATOM   4012 C CG2 . ILE B 1 229 ? -98.923  9.934  -57.248 1.00 32.21 ? 229  ILE B CG2 1 
ATOM   4013 C CD1 . ILE B 1 229 ? -96.250  8.204  -58.233 1.00 33.51 ? 229  ILE B CD1 1 
ATOM   4014 N N   . CYS B 1 230 ? -98.055  5.850  -55.014 1.00 32.25 ? 230  CYS B N   1 
ATOM   4015 C CA  . CYS B 1 230 ? -98.059  4.384  -54.917 1.00 31.83 ? 230  CYS B CA  1 
ATOM   4016 C C   . CYS B 1 230 ? -99.191  3.897  -54.012 1.00 31.61 ? 230  CYS B C   1 
ATOM   4017 O O   . CYS B 1 230 ? -99.908  2.956  -54.367 1.00 31.53 ? 230  CYS B O   1 
ATOM   4018 C CB  . CYS B 1 230 ? -96.703  3.840  -54.450 1.00 31.59 ? 230  CYS B CB  1 
ATOM   4019 S SG  . CYS B 1 230 ? -95.407  3.882  -55.716 1.00 31.07 ? 230  CYS B SG  1 
ATOM   4020 N N   . HIS B 1 231 ? -99.364  4.563  -52.871 1.00 31.47 ? 231  HIS B N   1 
ATOM   4021 C CA  . HIS B 1 231 ? -100.450 4.249  -51.934 1.00 31.68 ? 231  HIS B CA  1 
ATOM   4022 C C   . HIS B 1 231 ? -101.819 4.656  -52.486 1.00 30.82 ? 231  HIS B C   1 
ATOM   4023 O O   . HIS B 1 231 ? -102.800 3.940  -52.303 1.00 31.00 ? 231  HIS B O   1 
ATOM   4024 C CB  . HIS B 1 231 ? -100.220 4.910  -50.565 1.00 32.16 ? 231  HIS B CB  1 
ATOM   4025 C CG  . HIS B 1 231 ? -99.299  4.142  -49.674 1.00 35.04 ? 231  HIS B CG  1 
ATOM   4026 N ND1 . HIS B 1 231 ? -97.928  4.281  -49.723 1.00 37.38 ? 231  HIS B ND1 1 
ATOM   4027 C CD2 . HIS B 1 231 ? -99.550  3.219  -48.714 1.00 37.03 ? 231  HIS B CD2 1 
ATOM   4028 C CE1 . HIS B 1 231 ? -97.374  3.480  -48.828 1.00 38.37 ? 231  HIS B CE1 1 
ATOM   4029 N NE2 . HIS B 1 231 ? -98.337  2.827  -48.201 1.00 37.96 ? 231  HIS B NE2 1 
ATOM   4030 N N   . ALA B 1 232 ? -101.889 5.804  -53.151 1.00 29.77 ? 232  ALA B N   1 
ATOM   4031 C CA  . ALA B 1 232 ? -103.123 6.204  -53.811 1.00 29.03 ? 232  ALA B CA  1 
ATOM   4032 C C   . ALA B 1 232 ? -103.565 5.209  -54.912 1.00 28.66 ? 232  ALA B C   1 
ATOM   4033 O O   . ALA B 1 232 ? -104.766 4.946  -55.063 1.00 27.85 ? 232  ALA B O   1 
ATOM   4034 C CB  . ALA B 1 232 ? -102.995 7.612  -54.361 1.00 28.90 ? 232  ALA B CB  1 
ATOM   4035 N N   . ALA B 1 233 ? -102.600 4.663  -55.662 1.00 28.64 ? 233  ALA B N   1 
ATOM   4036 C CA  . ALA B 1 233 ? -102.872 3.638  -56.688 1.00 29.16 ? 233  ALA B CA  1 
ATOM   4037 C C   . ALA B 1 233 ? -103.554 2.404  -56.117 1.00 29.64 ? 233  ALA B C   1 
ATOM   4038 O O   . ALA B 1 233 ? -104.527 1.906  -56.711 1.00 29.71 ? 233  ALA B O   1 
ATOM   4039 C CB  . ALA B 1 233 ? -101.593 3.230  -57.433 1.00 28.65 ? 233  ALA B CB  1 
ATOM   4040 N N   . ASP B 1 234 ? -103.040 1.918  -54.979 1.00 29.99 ? 234  ASP B N   1 
ATOM   4041 C CA  . ASP B 1 234 ? -103.648 0.795  -54.263 1.00 30.57 ? 234  ASP B CA  1 
ATOM   4042 C C   . ASP B 1 234 ? -105.092 1.080  -53.894 1.00 30.47 ? 234  ASP B C   1 
ATOM   4043 O O   . ASP B 1 234 ? -105.981 0.257  -54.139 1.00 30.51 ? 234  ASP B O   1 
ATOM   4044 C CB  . ASP B 1 234 ? -102.884 0.477  -52.974 1.00 31.19 ? 234  ASP B CB  1 
ATOM   4045 C CG  . ASP B 1 234 ? -101.521 -0.146 -53.230 1.00 32.43 ? 234  ASP B CG  1 
ATOM   4046 O OD1 . ASP B 1 234 ? -101.322 -0.750 -54.308 1.00 33.32 ? 234  ASP B OD1 1 
ATOM   4047 O OD2 . ASP B 1 234 ? -100.586 -0.060 -52.403 1.00 33.42 ? 234  ASP B OD2 1 
ATOM   4048 N N   . LYS B 1 235 ? -105.304 2.239  -53.279 1.00 30.21 ? 235  LYS B N   1 
ATOM   4049 C CA  . LYS B 1 235 ? -106.616 2.650  -52.812 1.00 30.32 ? 235  LYS B CA  1 
ATOM   4050 C C   . LYS B 1 235 ? -107.616 2.652  -53.955 1.00 29.55 ? 235  LYS B C   1 
ATOM   4051 O O   . LYS B 1 235 ? -108.733 2.145  -53.808 1.00 29.93 ? 235  LYS B O   1 
ATOM   4052 C CB  . LYS B 1 235 ? -106.542 4.034  -52.138 1.00 31.01 ? 235  LYS B CB  1 
ATOM   4053 C CG  . LYS B 1 235 ? -107.859 4.502  -51.508 1.00 32.86 ? 235  LYS B CG  1 
ATOM   4054 C CD  . LYS B 1 235 ? -107.971 4.053  -50.068 1.00 36.17 ? 235  LYS B CD  1 
ATOM   4055 C CE  . LYS B 1 235 ? -109.427 4.029  -49.603 1.00 38.49 ? 235  LYS B CE  1 
ATOM   4056 N NZ  . LYS B 1 235 ? -109.522 4.076  -48.110 1.00 40.15 ? 235  LYS B NZ  1 
ATOM   4057 N N   . LEU B 1 236 ? -107.195 3.197  -55.091 1.00 28.64 ? 236  LEU B N   1 
ATOM   4058 C CA  . LEU B 1 236 ? -108.036 3.293  -56.286 1.00 27.91 ? 236  LEU B CA  1 
ATOM   4059 C C   . LEU B 1 236 ? -108.447 1.925  -56.838 1.00 27.79 ? 236  LEU B C   1 
ATOM   4060 O O   . LEU B 1 236 ? -109.630 1.723  -57.129 1.00 27.90 ? 236  LEU B O   1 
ATOM   4061 C CB  . LEU B 1 236 ? -107.362 4.156  -57.361 1.00 27.52 ? 236  LEU B CB  1 
ATOM   4062 C CG  . LEU B 1 236 ? -107.209 5.648  -56.999 1.00 27.13 ? 236  LEU B CG  1 
ATOM   4063 C CD1 . LEU B 1 236 ? -106.173 6.337  -57.875 1.00 26.06 ? 236  LEU B CD1 1 
ATOM   4064 C CD2 . LEU B 1 236 ? -108.550 6.386  -57.059 1.00 26.30 ? 236  LEU B CD2 1 
ATOM   4065 N N   . LEU B 1 237 ? -107.490 0.992  -56.959 1.00 27.34 ? 237  LEU B N   1 
ATOM   4066 C CA  . LEU B 1 237 ? -107.804 -0.403 -57.313 1.00 27.09 ? 237  LEU B CA  1 
ATOM   4067 C C   . LEU B 1 237 ? -108.729 -1.067 -56.270 1.00 27.18 ? 237  LEU B C   1 
ATOM   4068 O O   . LEU B 1 237 ? -109.702 -1.730 -56.628 1.00 27.16 ? 237  LEU B O   1 
ATOM   4069 C CB  . LEU B 1 237 ? -106.536 -1.236 -57.569 1.00 26.62 ? 237  LEU B CB  1 
ATOM   4070 C CG  . LEU B 1 237 ? -105.651 -0.888 -58.799 1.00 26.09 ? 237  LEU B CG  1 
ATOM   4071 C CD1 . LEU B 1 237 ? -104.507 -1.873 -59.007 1.00 25.21 ? 237  LEU B CD1 1 
ATOM   4072 C CD2 . LEU B 1 237 ? -106.427 -0.710 -60.127 1.00 24.37 ? 237  LEU B CD2 1 
ATOM   4073 N N   . SER B 1 238 ? -108.449 -0.842 -54.989 1.00 27.28 ? 238  SER B N   1 
ATOM   4074 C CA  . SER B 1 238 ? -109.321 -1.310 -53.915 1.00 27.58 ? 238  SER B CA  1 
ATOM   4075 C C   . SER B 1 238 ? -110.743 -0.791 -54.052 1.00 27.81 ? 238  SER B C   1 
ATOM   4076 O O   . SER B 1 238 ? -111.664 -1.413 -53.530 1.00 27.60 ? 238  SER B O   1 
ATOM   4077 C CB  . SER B 1 238 ? -108.788 -0.890 -52.552 1.00 27.36 ? 238  SER B CB  1 
ATOM   4078 O OG  . SER B 1 238 ? -107.716 -1.718 -52.182 1.00 28.24 ? 238  SER B OG  1 
ATOM   4079 N N   . ALA B 1 239 ? -110.905 0.355  -54.719 1.00 28.04 ? 239  ALA B N   1 
ATOM   4080 C CA  . ALA B 1 239 ? -112.212 0.992  -54.867 1.00 28.44 ? 239  ALA B CA  1 
ATOM   4081 C C   . ALA B 1 239 ? -112.845 0.672  -56.210 1.00 29.06 ? 239  ALA B C   1 
ATOM   4082 O O   . ALA B 1 239 ? -113.912 1.179  -56.544 1.00 29.47 ? 239  ALA B O   1 
ATOM   4083 C CB  . ALA B 1 239 ? -112.100 2.465  -54.687 1.00 28.40 ? 239  ALA B CB  1 
ATOM   4084 N N   . GLY B 1 240 ? -112.183 -0.173 -56.985 1.00 29.61 ? 240  GLY B N   1 
ATOM   4085 C CA  . GLY B 1 240 ? -112.806 -0.722 -58.167 1.00 30.23 ? 240  GLY B CA  1 
ATOM   4086 C C   . GLY B 1 240 ? -112.373 -0.102 -59.470 1.00 30.73 ? 240  GLY B C   1 
ATOM   4087 O O   . GLY B 1 240 ? -112.995 -0.381 -60.491 1.00 31.04 ? 240  GLY B O   1 
ATOM   4088 N N   . ALA B 1 241 ? -111.327 0.728  -59.445 1.00 30.93 ? 241  ALA B N   1 
ATOM   4089 C CA  . ALA B 1 241 ? -110.748 1.255  -60.681 1.00 31.14 ? 241  ALA B CA  1 
ATOM   4090 C C   . ALA B 1 241 ? -110.121 0.128  -61.497 1.00 31.66 ? 241  ALA B C   1 
ATOM   4091 O O   . ALA B 1 241 ? -109.542 -0.825 -60.947 1.00 31.90 ? 241  ALA B O   1 
ATOM   4092 C CB  . ALA B 1 241 ? -109.728 2.358  -60.399 1.00 30.82 ? 241  ALA B CB  1 
ATOM   4093 N N   . THR B 1 242 ? -110.244 0.258  -62.812 1.00 32.22 ? 242  THR B N   1 
ATOM   4094 C CA  . THR B 1 242 ? -109.887 -0.779 -63.761 1.00 32.68 ? 242  THR B CA  1 
ATOM   4095 C C   . THR B 1 242 ? -108.378 -0.849 -63.858 1.00 32.66 ? 242  THR B C   1 
ATOM   4096 O O   . THR B 1 242 ? -107.783 -1.929 -63.833 1.00 32.74 ? 242  THR B O   1 
ATOM   4097 C CB  . THR B 1 242 ? -110.515 -0.436 -65.130 1.00 33.13 ? 242  THR B CB  1 
ATOM   4098 O OG1 . THR B 1 242 ? -111.948 -0.422 -65.005 1.00 33.80 ? 242  THR B OG1 1 
ATOM   4099 C CG2 . THR B 1 242 ? -110.281 -1.558 -66.137 1.00 34.05 ? 242  THR B CG2 1 
ATOM   4100 N N   . ARG B 1 243 ? -107.772 0.321  -63.990 1.00 32.49 ? 243  ARG B N   1 
ATOM   4101 C CA  . ARG B 1 243 ? -106.330 0.473  -63.934 1.00 32.34 ? 243  ARG B CA  1 
ATOM   4102 C C   . ARG B 1 243 ? -106.036 1.885  -63.483 1.00 31.20 ? 243  ARG B C   1 
ATOM   4103 O O   . ARG B 1 243 ? -106.932 2.735  -63.443 1.00 31.20 ? 243  ARG B O   1 
ATOM   4104 C CB  . ARG B 1 243 ? -105.625 0.135  -65.261 1.00 33.12 ? 243  ARG B CB  1 
ATOM   4105 C CG  . ARG B 1 243 ? -106.282 0.656  -66.514 1.00 36.54 ? 243  ARG B CG  1 
ATOM   4106 C CD  . ARG B 1 243 ? -106.307 -0.342 -67.706 1.00 41.67 ? 243  ARG B CD  1 
ATOM   4107 N NE  . ARG B 1 243 ? -106.725 0.343  -68.936 1.00 46.14 ? 243  ARG B NE  1 
ATOM   4108 C CZ  . ARG B 1 243 ? -105.908 1.099  -69.684 1.00 48.80 ? 243  ARG B CZ  1 
ATOM   4109 N NH1 . ARG B 1 243 ? -104.633 1.226  -69.335 1.00 50.01 ? 243  ARG B NH1 1 
ATOM   4110 N NH2 . ARG B 1 243 ? -106.354 1.713  -70.785 1.00 49.18 ? 243  ARG B NH2 1 
ATOM   4111 N N   . VAL B 1 244 ? -104.789 2.107  -63.096 1.00 29.89 ? 244  VAL B N   1 
ATOM   4112 C CA  . VAL B 1 244 ? -104.363 3.371  -62.529 1.00 28.79 ? 244  VAL B CA  1 
ATOM   4113 C C   . VAL B 1 244 ? -103.157 3.886  -63.277 1.00 28.19 ? 244  VAL B C   1 
ATOM   4114 O O   . VAL B 1 244 ? -102.170 3.166  -63.491 1.00 27.83 ? 244  VAL B O   1 
ATOM   4115 C CB  . VAL B 1 244 ? -104.024 3.249  -61.012 1.00 28.73 ? 244  VAL B CB  1 
ATOM   4116 C CG1 . VAL B 1 244 ? -103.486 4.564  -60.474 1.00 27.99 ? 244  VAL B CG1 1 
ATOM   4117 C CG2 . VAL B 1 244 ? -105.261 2.839  -60.218 1.00 28.36 ? 244  VAL B CG2 1 
ATOM   4118 N N   . TYR B 1 245 ? -103.263 5.147  -63.670 1.00 27.74 ? 245  TYR B N   1 
ATOM   4119 C CA  . TYR B 1 245 ? -102.166 5.898  -64.257 1.00 27.38 ? 245  TYR B CA  1 
ATOM   4120 C C   . TYR B 1 245 ? -101.755 7.009  -63.307 1.00 26.71 ? 245  TYR B C   1 
ATOM   4121 O O   . TYR B 1 245 ? -102.565 7.474  -62.497 1.00 26.03 ? 245  TYR B O   1 
ATOM   4122 C CB  . TYR B 1 245 ? -102.614 6.542  -65.568 1.00 27.58 ? 245  TYR B CB  1 
ATOM   4123 C CG  . TYR B 1 245 ? -102.793 5.582  -66.716 1.00 28.08 ? 245  TYR B CG  1 
ATOM   4124 C CD1 . TYR B 1 245 ? -103.999 4.903  -66.903 1.00 27.66 ? 245  TYR B CD1 1 
ATOM   4125 C CD2 . TYR B 1 245 ? -101.764 5.378  -67.634 1.00 28.30 ? 245  TYR B CD2 1 
ATOM   4126 C CE1 . TYR B 1 245 ? -104.167 4.048  -67.956 1.00 28.21 ? 245  TYR B CE1 1 
ATOM   4127 C CE2 . TYR B 1 245 ? -101.920 4.530  -68.692 1.00 28.51 ? 245  TYR B CE2 1 
ATOM   4128 C CZ  . TYR B 1 245 ? -103.124 3.861  -68.854 1.00 29.03 ? 245  TYR B CZ  1 
ATOM   4129 O OH  . TYR B 1 245 ? -103.278 3.007  -69.921 1.00 29.48 ? 245  TYR B OH  1 
ATOM   4130 N N   . ALA B 1 246 ? -100.501 7.436  -63.427 1.00 26.31 ? 246  ALA B N   1 
ATOM   4131 C CA  . ALA B 1 246 ? -100.014 8.608  -62.723 1.00 26.42 ? 246  ALA B CA  1 
ATOM   4132 C C   . ALA B 1 246 ? -99.367  9.566  -63.725 1.00 26.42 ? 246  ALA B C   1 
ATOM   4133 O O   . ALA B 1 246 ? -98.477  9.175  -64.498 1.00 26.45 ? 246  ALA B O   1 
ATOM   4134 C CB  . ALA B 1 246 ? -99.042  8.216  -61.618 1.00 26.38 ? 246  ALA B CB  1 
ATOM   4135 N N   . ILE B 1 247 ? -99.853  10.804 -63.745 1.00 26.21 ? 247  ILE B N   1 
ATOM   4136 C CA  . ILE B 1 247 ? -99.282  11.839 -64.601 1.00 26.29 ? 247  ILE B CA  1 
ATOM   4137 C C   . ILE B 1 247 ? -98.785  12.988 -63.720 1.00 26.63 ? 247  ILE B C   1 
ATOM   4138 O O   . ILE B 1 247 ? -99.571  13.614 -63.011 1.00 26.42 ? 247  ILE B O   1 
ATOM   4139 C CB  . ILE B 1 247 ? -100.303 12.317 -65.670 1.00 26.13 ? 247  ILE B CB  1 
ATOM   4140 C CG1 . ILE B 1 247 ? -100.916 11.117 -66.406 1.00 25.87 ? 247  ILE B CG1 1 
ATOM   4141 C CG2 . ILE B 1 247 ? -99.624  13.264 -66.664 1.00 26.04 ? 247  ILE B CG2 1 
ATOM   4142 C CD1 . ILE B 1 247 ? -101.810 11.475 -67.600 1.00 25.48 ? 247  ILE B CD1 1 
ATOM   4143 N N   . LEU B 1 248 ? -97.475  13.215 -63.726 1.00 27.12 ? 248  LEU B N   1 
ATOM   4144 C CA  . LEU B 1 248 ? -96.870  14.316 -62.966 1.00 27.98 ? 248  LEU B CA  1 
ATOM   4145 C C   . LEU B 1 248 ? -96.180  15.245 -63.930 1.00 28.50 ? 248  LEU B C   1 
ATOM   4146 O O   . LEU B 1 248 ? -95.626  14.774 -64.928 1.00 28.78 ? 248  LEU B O   1 
ATOM   4147 C CB  . LEU B 1 248 ? -95.835  13.802 -61.968 1.00 27.95 ? 248  LEU B CB  1 
ATOM   4148 C CG  . LEU B 1 248 ? -96.315  12.933 -60.800 1.00 28.81 ? 248  LEU B CG  1 
ATOM   4149 C CD1 . LEU B 1 248 ? -97.578  13.478 -60.213 1.00 29.46 ? 248  LEU B CD1 1 
ATOM   4150 C CD2 . LEU B 1 248 ? -96.515  11.487 -61.210 1.00 29.45 ? 248  LEU B CD2 1 
ATOM   4151 N N   . THR B 1 249 ? -96.180  16.552 -63.671 1.00 28.61 ? 249  THR B N   1 
ATOM   4152 C CA  . THR B 1 249 ? -95.349  17.369 -64.544 1.00 28.92 ? 249  THR B CA  1 
ATOM   4153 C C   . THR B 1 249 ? -93.884  17.226 -64.137 1.00 29.05 ? 249  THR B C   1 
ATOM   4154 O O   . THR B 1 249 ? -93.025  17.017 -64.991 1.00 29.11 ? 249  THR B O   1 
ATOM   4155 C CB  . THR B 1 249 ? -95.858  18.841 -64.760 1.00 29.02 ? 249  THR B CB  1 
ATOM   4156 O OG1 . THR B 1 249 ? -94.775  19.772 -64.620 1.00 29.49 ? 249  THR B OG1 1 
ATOM   4157 C CG2 . THR B 1 249 ? -96.879  19.262 -63.731 1.00 28.96 ? 249  THR B CG2 1 
ATOM   4158 N N   . HIS B 1 250 ? -93.618  17.268 -62.831 1.00 29.28 ? 250  HIS B N   1 
ATOM   4159 C CA  . HIS B 1 250 ? -92.245  17.195 -62.317 1.00 29.39 ? 250  HIS B CA  1 
ATOM   4160 C C   . HIS B 1 250 ? -91.916  15.841 -61.702 1.00 29.84 ? 250  HIS B C   1 
ATOM   4161 O O   . HIS B 1 250 ? -92.472  15.459 -60.657 1.00 30.12 ? 250  HIS B O   1 
ATOM   4162 C CB  . HIS B 1 250 ? -91.973  18.318 -61.303 1.00 28.90 ? 250  HIS B CB  1 
ATOM   4163 C CG  . HIS B 1 250 ? -92.254  19.693 -61.833 1.00 28.31 ? 250  HIS B CG  1 
ATOM   4164 N ND1 . HIS B 1 250 ? -91.677  20.182 -62.989 1.00 27.44 ? 250  HIS B ND1 1 
ATOM   4165 C CD2 . HIS B 1 250 ? -93.077  20.671 -61.382 1.00 27.20 ? 250  HIS B CD2 1 
ATOM   4166 C CE1 . HIS B 1 250 ? -92.122  21.404 -63.217 1.00 26.52 ? 250  HIS B CE1 1 
ATOM   4167 N NE2 . HIS B 1 250 ? -92.976  21.721 -62.258 1.00 26.43 ? 250  HIS B NE2 1 
ATOM   4168 N N   . GLY B 1 251 ? -90.998  15.117 -62.336 1.00 30.05 ? 251  GLY B N   1 
ATOM   4169 C CA  . GLY B 1 251 ? -90.584  13.824 -61.811 1.00 30.31 ? 251  GLY B CA  1 
ATOM   4170 C C   . GLY B 1 251 ? -89.268  13.843 -61.056 1.00 30.60 ? 251  GLY B C   1 
ATOM   4171 O O   . GLY B 1 251 ? -88.217  13.563 -61.635 1.00 30.02 ? 251  GLY B O   1 
ATOM   4172 N N   . ILE B 1 252 ? -89.318  14.178 -59.765 1.00 31.46 ? 252  ILE B N   1 
ATOM   4173 C CA  . ILE B 1 252 ? -88.110  14.189 -58.929 1.00 32.15 ? 252  ILE B CA  1 
ATOM   4174 C C   . ILE B 1 252 ? -87.554  12.760 -58.761 1.00 32.31 ? 252  ILE B C   1 
ATOM   4175 O O   . ILE B 1 252 ? -86.401  12.488 -59.080 1.00 32.46 ? 252  ILE B O   1 
ATOM   4176 C CB  . ILE B 1 252 ? -88.385  14.817 -57.538 1.00 32.53 ? 252  ILE B CB  1 
ATOM   4177 C CG1 . ILE B 1 252 ? -89.345  16.027 -57.618 1.00 33.21 ? 252  ILE B CG1 1 
ATOM   4178 C CG2 . ILE B 1 252 ? -87.068  15.074 -56.785 1.00 32.20 ? 252  ILE B CG2 1 
ATOM   4179 C CD1 . ILE B 1 252 ? -88.711  17.333 -57.946 1.00 33.94 ? 252  ILE B CD1 1 
ATOM   4180 N N   . PHE B 1 253 ? -88.378  11.851 -58.256 1.00 32.68 ? 253  PHE B N   1 
ATOM   4181 C CA  . PHE B 1 253 ? -88.012  10.429 -58.184 1.00 32.98 ? 253  PHE B CA  1 
ATOM   4182 C C   . PHE B 1 253 ? -86.719  10.161 -57.399 1.00 33.56 ? 253  PHE B C   1 
ATOM   4183 O O   . PHE B 1 253 ? -85.853  9.412  -57.860 1.00 33.84 ? 253  PHE B O   1 
ATOM   4184 C CB  . PHE B 1 253 ? -87.926  9.800  -59.596 1.00 32.37 ? 253  PHE B CB  1 
ATOM   4185 C CG  . PHE B 1 253 ? -89.204  9.886  -60.398 1.00 30.35 ? 253  PHE B CG  1 
ATOM   4186 C CD1 . PHE B 1 253 ? -89.158  9.988  -61.772 1.00 28.35 ? 253  PHE B CD1 1 
ATOM   4187 C CD2 . PHE B 1 253 ? -90.446  9.842  -59.783 1.00 29.48 ? 253  PHE B CD2 1 
ATOM   4188 C CE1 . PHE B 1 253 ? -90.326  10.051 -62.525 1.00 26.98 ? 253  PHE B CE1 1 
ATOM   4189 C CE2 . PHE B 1 253 ? -91.616  9.911  -60.530 1.00 27.85 ? 253  PHE B CE2 1 
ATOM   4190 C CZ  . PHE B 1 253 ? -91.549  10.006 -61.904 1.00 26.27 ? 253  PHE B CZ  1 
ATOM   4191 N N   . SER B 1 254 ? -86.602  10.770 -56.218 1.00 34.03 ? 254  SER B N   1 
ATOM   4192 C CA  . SER B 1 254 ? -85.456  10.555 -55.332 1.00 34.58 ? 254  SER B CA  1 
ATOM   4193 C C   . SER B 1 254 ? -85.695  9.361  -54.414 1.00 35.17 ? 254  SER B C   1 
ATOM   4194 O O   . SER B 1 254 ? -86.829  8.871  -54.308 1.00 35.21 ? 254  SER B O   1 
ATOM   4195 C CB  . SER B 1 254 ? -85.212  11.793 -54.473 1.00 34.32 ? 254  SER B CB  1 
ATOM   4196 O OG  . SER B 1 254 ? -86.311  11.995 -53.612 1.00 34.22 ? 254  SER B OG  1 
ATOM   4197 N N   . GLY B 1 255 ? -84.636  8.924  -53.726 1.00 35.68 ? 255  GLY B N   1 
ATOM   4198 C CA  . GLY B 1 255 ? -84.712  7.800  -52.803 1.00 36.27 ? 255  GLY B CA  1 
ATOM   4199 C C   . GLY B 1 255 ? -85.302  6.561  -53.464 1.00 36.76 ? 255  GLY B C   1 
ATOM   4200 O O   . GLY B 1 255 ? -84.937  6.252  -54.594 1.00 37.26 ? 255  GLY B O   1 
ATOM   4201 N N   . PRO B 1 256 ? -86.240  5.887  -52.799 1.00 37.02 ? 256  PRO B N   1 
ATOM   4202 C CA  . PRO B 1 256 ? -86.769  4.598  -53.276 1.00 37.30 ? 256  PRO B CA  1 
ATOM   4203 C C   . PRO B 1 256 ? -87.850  4.719  -54.354 1.00 37.66 ? 256  PRO B C   1 
ATOM   4204 O O   . PRO B 1 256 ? -88.515  3.719  -54.661 1.00 38.04 ? 256  PRO B O   1 
ATOM   4205 C CB  . PRO B 1 256 ? -87.404  4.014  -52.012 1.00 37.32 ? 256  PRO B CB  1 
ATOM   4206 C CG  . PRO B 1 256 ? -87.919  5.227  -51.279 1.00 37.10 ? 256  PRO B CG  1 
ATOM   4207 C CD  . PRO B 1 256 ? -86.882  6.306  -51.536 1.00 36.98 ? 256  PRO B CD  1 
ATOM   4208 N N   . ALA B 1 257 ? -88.037  5.913  -54.905 1.00 37.65 ? 257  ALA B N   1 
ATOM   4209 C CA  . ALA B 1 257 ? -89.115  6.148  -55.857 1.00 37.66 ? 257  ALA B CA  1 
ATOM   4210 C C   . ALA B 1 257 ? -89.128  5.120  -56.991 1.00 37.55 ? 257  ALA B C   1 
ATOM   4211 O O   . ALA B 1 257 ? -90.187  4.586  -57.334 1.00 37.27 ? 257  ALA B O   1 
ATOM   4212 C CB  . ALA B 1 257 ? -89.036  7.557  -56.417 1.00 37.51 ? 257  ALA B CB  1 
ATOM   4213 N N   . ILE B 1 258 ? -87.957  4.856  -57.568 1.00 37.52 ? 258  ILE B N   1 
ATOM   4214 C CA  . ILE B 1 258 ? -87.852  3.919  -58.687 1.00 37.63 ? 258  ILE B CA  1 
ATOM   4215 C C   . ILE B 1 258 ? -88.232  2.499  -58.263 1.00 38.21 ? 258  ILE B C   1 
ATOM   4216 O O   . ILE B 1 258 ? -88.915  1.796  -59.010 1.00 38.09 ? 258  ILE B O   1 
ATOM   4217 C CB  . ILE B 1 258 ? -86.438  3.981  -59.355 1.00 37.29 ? 258  ILE B CB  1 
ATOM   4218 C CG1 . ILE B 1 258 ? -86.190  5.351  -60.030 1.00 36.33 ? 258  ILE B CG1 1 
ATOM   4219 C CG2 . ILE B 1 258 ? -86.232  2.830  -60.339 1.00 37.01 ? 258  ILE B CG2 1 
ATOM   4220 C CD1 . ILE B 1 258 ? -87.361  5.952  -60.839 1.00 33.78 ? 258  ILE B CD1 1 
ATOM   4221 N N   . SER B 1 259 ? -87.809  2.100  -57.060 1.00 38.87 ? 259  SER B N   1 
ATOM   4222 C CA  . SER B 1 259 ? -88.158  0.796  -56.494 1.00 39.58 ? 259  SER B CA  1 
ATOM   4223 C C   . SER B 1 259 ? -89.636  0.756  -56.167 1.00 39.54 ? 259  SER B C   1 
ATOM   4224 O O   . SER B 1 259 ? -90.301  -0.261 -56.372 1.00 39.48 ? 259  SER B O   1 
ATOM   4225 C CB  . SER B 1 259 ? -87.348  0.494  -55.221 1.00 40.05 ? 259  SER B CB  1 
ATOM   4226 O OG  . SER B 1 259 ? -85.959  0.367  -55.500 1.00 41.41 ? 259  SER B OG  1 
ATOM   4227 N N   . ARG B 1 260 ? -90.135  1.871  -55.647 1.00 39.71 ? 260  ARG B N   1 
ATOM   4228 C CA  . ARG B 1 260 ? -91.553  2.028  -55.345 1.00 39.89 ? 260  ARG B CA  1 
ATOM   4229 C C   . ARG B 1 260 ? -92.450  1.907  -56.596 1.00 39.94 ? 260  ARG B C   1 
ATOM   4230 O O   . ARG B 1 260 ? -93.504  1.273  -56.540 1.00 40.00 ? 260  ARG B O   1 
ATOM   4231 C CB  . ARG B 1 260 ? -91.785  3.355  -54.627 1.00 40.03 ? 260  ARG B CB  1 
ATOM   4232 C CG  . ARG B 1 260 ? -92.361  3.218  -53.235 1.00 40.46 ? 260  ARG B CG  1 
ATOM   4233 C CD  . ARG B 1 260 ? -91.382  3.528  -52.129 1.00 40.94 ? 260  ARG B CD  1 
ATOM   4234 N NE  . ARG B 1 260 ? -91.677  4.820  -51.521 1.00 41.18 ? 260  ARG B NE  1 
ATOM   4235 C CZ  . ARG B 1 260 ? -91.376  5.161  -50.275 1.00 42.13 ? 260  ARG B CZ  1 
ATOM   4236 N NH1 . ARG B 1 260 ? -90.756  4.315  -49.466 1.00 42.77 ? 260  ARG B NH1 1 
ATOM   4237 N NH2 . ARG B 1 260 ? -91.695  6.363  -49.832 1.00 43.06 ? 260  ARG B NH2 1 
ATOM   4238 N N   . ILE B 1 261 ? -92.011  2.481  -57.718 1.00 39.93 ? 261  ILE B N   1 
ATOM   4239 C CA  . ILE B 1 261 ? -92.793  2.504  -58.958 1.00 40.17 ? 261  ILE B CA  1 
ATOM   4240 C C   . ILE B 1 261 ? -92.780  1.140  -59.668 1.00 40.84 ? 261  ILE B C   1 
ATOM   4241 O O   . ILE B 1 261 ? -93.803  0.676  -60.199 1.00 40.98 ? 261  ILE B O   1 
ATOM   4242 C CB  . ILE B 1 261 ? -92.285  3.636  -59.895 1.00 39.95 ? 261  ILE B CB  1 
ATOM   4243 C CG1 . ILE B 1 261 ? -92.645  5.016  -59.328 1.00 39.63 ? 261  ILE B CG1 1 
ATOM   4244 C CG2 . ILE B 1 261 ? -92.840  3.472  -61.315 1.00 40.06 ? 261  ILE B CG2 1 
ATOM   4245 C CD1 . ILE B 1 261 ? -92.094  6.197  -60.131 1.00 39.34 ? 261  ILE B CD1 1 
ATOM   4246 N N   . ASN B 1 262 ? -91.612  0.505  -59.677 1.00 41.42 ? 262  ASN B N   1 
ATOM   4247 C CA  . ASN B 1 262 ? -91.470  -0.846 -60.200 1.00 41.61 ? 262  ASN B CA  1 
ATOM   4248 C C   . ASN B 1 262 ? -92.312  -1.875 -59.455 1.00 41.73 ? 262  ASN B C   1 
ATOM   4249 O O   . ASN B 1 262 ? -92.726  -2.859 -60.040 1.00 41.84 ? 262  ASN B O   1 
ATOM   4250 C CB  . ASN B 1 262 ? -89.999  -1.251 -60.215 1.00 41.62 ? 262  ASN B CB  1 
ATOM   4251 C CG  . ASN B 1 262 ? -89.234  -0.624 -61.379 1.00 41.76 ? 262  ASN B CG  1 
ATOM   4252 O OD1 . ASN B 1 262 ? -89.798  -0.353 -62.450 1.00 41.54 ? 262  ASN B OD1 1 
ATOM   4253 N ND2 . ASN B 1 262 ? -87.944  -0.390 -61.172 1.00 41.78 ? 262  ASN B ND2 1 
ATOM   4254 N N   . ASN B 1 263 ? -92.584  -1.641 -58.176 1.00 42.08 ? 263  ASN B N   1 
ATOM   4255 C CA  . ASN B 1 263 ? -93.406  -2.565 -57.402 1.00 42.34 ? 263  ASN B CA  1 
ATOM   4256 C C   . ASN B 1 263 ? -94.873  -2.185 -57.431 1.00 42.64 ? 263  ASN B C   1 
ATOM   4257 O O   . ASN B 1 263 ? -95.728  -2.958 -56.987 1.00 43.05 ? 263  ASN B O   1 
ATOM   4258 C CB  . ASN B 1 263 ? -92.925  -2.657 -55.953 1.00 42.52 ? 263  ASN B CB  1 
ATOM   4259 C CG  . ASN B 1 263 ? -91.552  -3.310 -55.822 1.00 42.97 ? 263  ASN B CG  1 
ATOM   4260 O OD1 . ASN B 1 263 ? -90.776  -2.963 -54.935 1.00 43.84 ? 263  ASN B OD1 1 
ATOM   4261 N ND2 . ASN B 1 263 ? -91.254  -4.261 -56.698 1.00 42.83 ? 263  ASN B ND2 1 
ATOM   4262 N N   . ALA B 1 264 ? -95.164  -0.997 -57.962 1.00 42.60 ? 264  ALA B N   1 
ATOM   4263 C CA  . ALA B 1 264 ? -96.512  -0.430 -57.912 1.00 42.26 ? 264  ALA B CA  1 
ATOM   4264 C C   . ALA B 1 264 ? -97.430  -0.977 -58.995 1.00 42.07 ? 264  ALA B C   1 
ATOM   4265 O O   . ALA B 1 264 ? -96.975  -1.471 -60.034 1.00 42.11 ? 264  ALA B O   1 
ATOM   4266 C CB  . ALA B 1 264 ? -96.450  1.081  -57.991 1.00 42.25 ? 264  ALA B CB  1 
ATOM   4267 N N   . CYS B 1 265 ? -98.726  -0.858 -58.744 1.00 41.70 ? 265  CYS B N   1 
ATOM   4268 C CA  . CYS B 1 265 ? -99.741  -1.326 -59.655 1.00 41.82 ? 265  CYS B CA  1 
ATOM   4269 C C   . CYS B 1 265 ? -100.157 -0.250 -60.673 1.00 41.49 ? 265  CYS B C   1 
ATOM   4270 O O   . CYS B 1 265 ? -101.322 -0.169 -61.048 1.00 41.67 ? 265  CYS B O   1 
ATOM   4271 C CB  . CYS B 1 265 ? -100.941 -1.793 -58.842 1.00 42.37 ? 265  CYS B CB  1 
ATOM   4272 S SG  . CYS B 1 265 ? -101.608 -0.517 -57.722 1.00 45.27 ? 265  CYS B SG  1 
ATOM   4273 N N   . PHE B 1 266 ? -99.202  0.571  -61.115 1.00 40.97 ? 266  PHE B N   1 
ATOM   4274 C CA  . PHE B 1 266 ? -99.434  1.557  -62.171 1.00 40.37 ? 266  PHE B CA  1 
ATOM   4275 C C   . PHE B 1 266 ? -99.407  0.899  -63.538 1.00 40.20 ? 266  PHE B C   1 
ATOM   4276 O O   . PHE B 1 266 ? -98.640  -0.033 -63.767 1.00 40.64 ? 266  PHE B O   1 
ATOM   4277 C CB  . PHE B 1 266 ? -98.348  2.641  -62.164 1.00 40.02 ? 266  PHE B CB  1 
ATOM   4278 C CG  . PHE B 1 266 ? -98.383  3.534  -60.966 1.00 39.33 ? 266  PHE B CG  1 
ATOM   4279 C CD1 . PHE B 1 266 ? -97.285  3.626  -60.132 1.00 38.99 ? 266  PHE B CD1 1 
ATOM   4280 C CD2 . PHE B 1 266 ? -99.504  4.291  -60.675 1.00 38.80 ? 266  PHE B CD2 1 
ATOM   4281 C CE1 . PHE B 1 266 ? -97.303  4.445  -59.020 1.00 38.52 ? 266  PHE B CE1 1 
ATOM   4282 C CE2 . PHE B 1 266 ? -99.527  5.117  -59.566 1.00 38.95 ? 266  PHE B CE2 1 
ATOM   4283 C CZ  . PHE B 1 266 ? -98.423  5.192  -58.738 1.00 38.69 ? 266  PHE B CZ  1 
ATOM   4284 N N   . GLU B 1 267 ? -100.217 1.400  -64.460 1.00 39.49 ? 267  GLU B N   1 
ATOM   4285 C CA  . GLU B 1 267 ? -100.106 0.968  -65.835 1.00 39.03 ? 267  GLU B CA  1 
ATOM   4286 C C   . GLU B 1 267 ? -98.967  1.743  -66.493 1.00 37.83 ? 267  GLU B C   1 
ATOM   4287 O O   . GLU B 1 267 ? -98.317  1.242  -67.410 1.00 38.06 ? 267  GLU B O   1 
ATOM   4288 C CB  . GLU B 1 267 ? -101.422 1.197  -66.571 1.00 39.95 ? 267  GLU B CB  1 
ATOM   4289 C CG  . GLU B 1 267 ? -101.462 0.633  -67.989 1.00 43.03 ? 267  GLU B CG  1 
ATOM   4290 C CD  . GLU B 1 267 ? -102.119 -0.734 -68.067 1.00 46.76 ? 267  GLU B CD  1 
ATOM   4291 O OE1 . GLU B 1 267 ? -102.199 -1.434 -67.031 1.00 47.68 ? 267  GLU B OE1 1 
ATOM   4292 O OE2 . GLU B 1 267 ? -102.559 -1.108 -69.178 1.00 49.15 ? 267  GLU B OE2 1 
ATOM   4293 N N   . ALA B 1 268 ? -98.738  2.966  -66.015 1.00 36.08 ? 268  ALA B N   1 
ATOM   4294 C CA  . ALA B 1 268 ? -97.681  3.856  -66.512 1.00 34.32 ? 268  ALA B CA  1 
ATOM   4295 C C   . ALA B 1 268 ? -97.514  5.058  -65.593 1.00 32.91 ? 268  ALA B C   1 
ATOM   4296 O O   . ALA B 1 268 ? -98.458  5.494  -64.940 1.00 32.68 ? 268  ALA B O   1 
ATOM   4297 C CB  . ALA B 1 268 ? -97.990  4.338  -67.934 1.00 34.31 ? 268  ALA B CB  1 
ATOM   4298 N N   . VAL B 1 269 ? -96.306  5.594  -65.553 1.00 31.46 ? 269  VAL B N   1 
ATOM   4299 C CA  . VAL B 1 269 ? -96.055  6.843  -64.859 1.00 30.32 ? 269  VAL B CA  1 
ATOM   4300 C C   . VAL B 1 269 ? -95.564  7.840  -65.889 1.00 29.47 ? 269  VAL B C   1 
ATOM   4301 O O   . VAL B 1 269 ? -94.491  7.661  -66.461 1.00 29.66 ? 269  VAL B O   1 
ATOM   4302 C CB  . VAL B 1 269 ? -95.025  6.684  -63.726 1.00 30.21 ? 269  VAL B CB  1 
ATOM   4303 C CG1 . VAL B 1 269 ? -94.856  7.996  -62.984 1.00 29.88 ? 269  VAL B CG1 1 
ATOM   4304 C CG2 . VAL B 1 269 ? -95.465  5.587  -62.759 1.00 29.96 ? 269  VAL B CG2 1 
ATOM   4305 N N   . VAL B 1 270 ? -96.361  8.877  -66.132 1.00 28.26 ? 270  VAL B N   1 
ATOM   4306 C CA  . VAL B 1 270 ? -96.025  9.885  -67.128 1.00 27.13 ? 270  VAL B CA  1 
ATOM   4307 C C   . VAL B 1 270 ? -95.537  11.169 -66.458 1.00 26.64 ? 270  VAL B C   1 
ATOM   4308 O O   . VAL B 1 270 ? -96.181  11.690 -65.553 1.00 26.11 ? 270  VAL B O   1 
ATOM   4309 C CB  . VAL B 1 270 ? -97.212  10.161 -68.079 1.00 27.15 ? 270  VAL B CB  1 
ATOM   4310 C CG1 . VAL B 1 270 ? -96.807  11.085 -69.227 1.00 26.74 ? 270  VAL B CG1 1 
ATOM   4311 C CG2 . VAL B 1 270 ? -97.745  8.857  -68.641 1.00 26.66 ? 270  VAL B CG2 1 
ATOM   4312 N N   . VAL B 1 271 ? -94.368  11.640 -66.894 1.00 26.38 ? 271  VAL B N   1 
ATOM   4313 C CA  . VAL B 1 271 ? -93.786  12.905 -66.449 1.00 26.00 ? 271  VAL B CA  1 
ATOM   4314 C C   . VAL B 1 271 ? -93.267  13.727 -67.649 1.00 26.20 ? 271  VAL B C   1 
ATOM   4315 O O   . VAL B 1 271 ? -93.068  13.181 -68.746 1.00 26.36 ? 271  VAL B O   1 
ATOM   4316 C CB  . VAL B 1 271 ? -92.642  12.684 -65.429 1.00 25.65 ? 271  VAL B CB  1 
ATOM   4317 C CG1 . VAL B 1 271 ? -93.177  12.075 -64.166 1.00 25.21 ? 271  VAL B CG1 1 
ATOM   4318 C CG2 . VAL B 1 271 ? -91.533  11.809 -66.018 1.00 25.57 ? 271  VAL B CG2 1 
ATOM   4319 N N   . THR B 1 272 ? -93.058  15.028 -67.452 1.00 25.97 ? 272  THR B N   1 
ATOM   4320 C CA  . THR B 1 272 ? -92.364  15.824 -68.464 1.00 26.28 ? 272  THR B CA  1 
ATOM   4321 C C   . THR B 1 272 ? -90.856  15.737 -68.263 1.00 26.83 ? 272  THR B C   1 
ATOM   4322 O O   . THR B 1 272 ? -90.390  15.207 -67.261 1.00 26.83 ? 272  THR B O   1 
ATOM   4323 C CB  . THR B 1 272 ? -92.801  17.310 -68.458 1.00 25.98 ? 272  THR B CB  1 
ATOM   4324 O OG1 . THR B 1 272 ? -92.180  17.986 -67.354 1.00 25.41 ? 272  THR B OG1 1 
ATOM   4325 C CG2 . THR B 1 272 ? -94.307  17.457 -68.237 1.00 24.72 ? 272  THR B CG2 1 
ATOM   4326 N N   . ASN B 1 273 ? -90.096  16.264 -69.214 1.00 27.72 ? 273  ASN B N   1 
ATOM   4327 C CA  . ASN B 1 273 ? -88.646  16.378 -69.034 1.00 28.74 ? 273  ASN B CA  1 
ATOM   4328 C C   . ASN B 1 273 ? -88.213  17.736 -68.480 1.00 29.15 ? 273  ASN B C   1 
ATOM   4329 O O   . ASN B 1 273 ? -87.251  18.306 -68.967 1.00 29.92 ? 273  ASN B O   1 
ATOM   4330 C CB  . ASN B 1 273 ? -87.888  16.056 -70.331 1.00 28.57 ? 273  ASN B CB  1 
ATOM   4331 C CG  . ASN B 1 273 ? -88.306  16.939 -71.495 1.00 29.72 ? 273  ASN B CG  1 
ATOM   4332 O OD1 . ASN B 1 273 ? -89.289  17.677 -71.421 1.00 30.48 ? 273  ASN B OD1 1 
ATOM   4333 N ND2 . ASN B 1 273 ? -87.558  16.863 -72.588 1.00 31.03 ? 273  ASN B ND2 1 
ATOM   4334 N N   . THR B 1 274 ? -88.919  18.253 -67.474 1.00 29.54 ? 274  THR B N   1 
ATOM   4335 C CA  . THR B 1 274 ? -88.448  19.426 -66.720 1.00 30.08 ? 274  THR B CA  1 
ATOM   4336 C C   . THR B 1 274 ? -87.265  19.023 -65.857 1.00 30.52 ? 274  THR B C   1 
ATOM   4337 O O   . THR B 1 274 ? -86.418  19.836 -65.515 1.00 30.07 ? 274  THR B O   1 
ATOM   4338 C CB  . THR B 1 274 ? -89.554  20.011 -65.809 1.00 30.06 ? 274  THR B CB  1 
ATOM   4339 O OG1 . THR B 1 274 ? -90.234  18.950 -65.120 1.00 29.60 ? 274  THR B OG1 1 
ATOM   4340 C CG2 . THR B 1 274 ? -90.649  20.706 -66.639 1.00 29.88 ? 274  THR B CG2 1 
ATOM   4341 N N   . ILE B 1 275 ? -87.266  17.748 -65.484 1.00 31.61 ? 275  ILE B N   1 
ATOM   4342 C CA  . ILE B 1 275 ? -86.165  17.079 -64.812 1.00 32.46 ? 275  ILE B CA  1 
ATOM   4343 C C   . ILE B 1 275 ? -85.668  15.970 -65.764 1.00 33.69 ? 275  ILE B C   1 
ATOM   4344 O O   . ILE B 1 275 ? -86.478  15.327 -66.441 1.00 33.69 ? 275  ILE B O   1 
ATOM   4345 C CB  . ILE B 1 275 ? -86.676  16.534 -63.449 1.00 32.15 ? 275  ILE B CB  1 
ATOM   4346 C CG1 . ILE B 1 275 ? -87.272  17.696 -62.640 1.00 31.73 ? 275  ILE B CG1 1 
ATOM   4347 C CG2 . ILE B 1 275 ? -85.572  15.824 -62.666 1.00 31.52 ? 275  ILE B CG2 1 
ATOM   4348 C CD1 . ILE B 1 275 ? -87.768  17.350 -61.294 1.00 31.17 ? 275  ILE B CD1 1 
ATOM   4349 N N   . PRO B 1 276 ? -84.352  15.768 -65.867 1.00 34.95 ? 276  PRO B N   1 
ATOM   4350 C CA  . PRO B 1 276 ? -83.818  14.718 -66.750 1.00 35.86 ? 276  PRO B CA  1 
ATOM   4351 C C   . PRO B 1 276 ? -84.235  13.340 -66.261 1.00 36.91 ? 276  PRO B C   1 
ATOM   4352 O O   . PRO B 1 276 ? -84.129  13.026 -65.073 1.00 36.93 ? 276  PRO B O   1 
ATOM   4353 C CB  . PRO B 1 276 ? -82.297  14.907 -66.663 1.00 35.55 ? 276  PRO B CB  1 
ATOM   4354 C CG  . PRO B 1 276 ? -82.075  15.628 -65.424 1.00 35.42 ? 276  PRO B CG  1 
ATOM   4355 C CD  . PRO B 1 276 ? -83.277  16.493 -65.171 1.00 34.99 ? 276  PRO B CD  1 
ATOM   4356 N N   . GLN B 1 277 ? -84.713  12.528 -67.192 1.00 38.51 ? 277  GLN B N   1 
ATOM   4357 C CA  . GLN B 1 277 ? -85.401  11.288 -66.866 1.00 40.11 ? 277  GLN B CA  1 
ATOM   4358 C C   . GLN B 1 277 ? -84.646  10.042 -67.371 1.00 41.72 ? 277  GLN B C   1 
ATOM   4359 O O   . GLN B 1 277 ? -84.941  8.922  -66.956 1.00 41.61 ? 277  GLN B O   1 
ATOM   4360 C CB  . GLN B 1 277 ? -86.809  11.358 -67.475 1.00 39.68 ? 277  GLN B CB  1 
ATOM   4361 C CG  . GLN B 1 277 ? -88.027  11.405 -66.533 1.00 39.32 ? 277  GLN B CG  1 
ATOM   4362 C CD  . GLN B 1 277 ? -87.833  12.120 -65.196 1.00 38.56 ? 277  GLN B CD  1 
ATOM   4363 O OE1 . GLN B 1 277 ? -88.087  13.323 -65.070 1.00 37.44 ? 277  GLN B OE1 1 
ATOM   4364 N NE2 . GLN B 1 277 ? -87.439  11.363 -64.183 1.00 38.66 ? 277  GLN B NE2 1 
ATOM   4365 N N   . GLU B 1 278 ? -83.664  10.256 -68.248 1.00 44.04 ? 278  GLU B N   1 
ATOM   4366 C CA  . GLU B 1 278 ? -82.996  9.185  -69.020 1.00 46.41 ? 278  GLU B CA  1 
ATOM   4367 C C   . GLU B 1 278 ? -82.469  8.027  -68.173 1.00 47.19 ? 278  GLU B C   1 
ATOM   4368 O O   . GLU B 1 278 ? -82.791  6.864  -68.430 1.00 47.27 ? 278  GLU B O   1 
ATOM   4369 C CB  . GLU B 1 278 ? -81.867  9.747  -69.904 1.00 46.98 ? 278  GLU B CB  1 
ATOM   4370 C CG  . GLU B 1 278 ? -82.317  10.744 -70.970 1.00 50.03 ? 278  GLU B CG  1 
ATOM   4371 C CD  . GLU B 1 278 ? -82.882  12.041 -70.384 1.00 53.86 ? 278  GLU B CD  1 
ATOM   4372 O OE1 . GLU B 1 278 ? -82.169  12.694 -69.570 1.00 54.39 ? 278  GLU B OE1 1 
ATOM   4373 O OE2 . GLU B 1 278 ? -84.048  12.396 -70.721 1.00 55.76 ? 278  GLU B OE2 1 
ATOM   4374 N N   . ASP B 1 279 ? -81.670  8.352  -67.165 1.00 48.33 ? 279  ASP B N   1 
ATOM   4375 C CA  . ASP B 1 279 ? -81.121  7.339  -66.268 1.00 49.47 ? 279  ASP B CA  1 
ATOM   4376 C C   . ASP B 1 279 ? -82.182  6.650  -65.388 1.00 49.15 ? 279  ASP B C   1 
ATOM   4377 O O   . ASP B 1 279 ? -82.083  5.449  -65.118 1.00 49.36 ? 279  ASP B O   1 
ATOM   4378 C CB  . ASP B 1 279 ? -79.976  7.911  -65.421 1.00 50.35 ? 279  ASP B CB  1 
ATOM   4379 C CG  . ASP B 1 279 ? -78.907  6.872  -65.126 1.00 53.05 ? 279  ASP B CG  1 
ATOM   4380 O OD1 . ASP B 1 279 ? -78.134  6.530  -66.058 1.00 55.11 ? 279  ASP B OD1 1 
ATOM   4381 O OD2 . ASP B 1 279 ? -78.779  6.325  -64.000 1.00 55.35 ? 279  ASP B OD2 1 
ATOM   4382 N N   . LYS B 1 280 ? -83.191  7.404  -64.954 1.00 48.62 ? 280  LYS B N   1 
ATOM   4383 C CA  . LYS B 1 280 ? -84.340  6.823  -64.254 1.00 48.21 ? 280  LYS B CA  1 
ATOM   4384 C C   . LYS B 1 280 ? -85.107  5.821  -65.129 1.00 48.17 ? 280  LYS B C   1 
ATOM   4385 O O   . LYS B 1 280 ? -85.604  4.820  -64.625 1.00 48.13 ? 280  LYS B O   1 
ATOM   4386 C CB  . LYS B 1 280 ? -85.301  7.907  -63.756 1.00 47.89 ? 280  LYS B CB  1 
ATOM   4387 C CG  . LYS B 1 280 ? -84.653  9.031  -62.952 1.00 47.38 ? 280  LYS B CG  1 
ATOM   4388 C CD  . LYS B 1 280 ? -84.447  8.643  -61.497 1.00 46.53 ? 280  LYS B CD  1 
ATOM   4389 C CE  . LYS B 1 280 ? -83.534  9.628  -60.805 1.00 46.34 ? 280  LYS B CE  1 
ATOM   4390 N NZ  . LYS B 1 280 ? -84.275  10.512 -59.872 1.00 46.06 ? 280  LYS B NZ  1 
ATOM   4391 N N   . MET B 1 281 ? -85.194  6.090  -66.432 1.00 48.16 ? 281  MET B N   1 
ATOM   4392 C CA  . MET B 1 281 ? -85.975  5.252  -67.347 1.00 48.27 ? 281  MET B CA  1 
ATOM   4393 C C   . MET B 1 281 ? -85.355  3.867  -67.572 1.00 48.57 ? 281  MET B C   1 
ATOM   4394 O O   . MET B 1 281 ? -86.055  2.847  -67.498 1.00 48.69 ? 281  MET B O   1 
ATOM   4395 C CB  . MET B 1 281 ? -86.203  5.968  -68.678 1.00 48.01 ? 281  MET B CB  1 
ATOM   4396 C CG  . MET B 1 281 ? -87.271  7.038  -68.611 1.00 47.24 ? 281  MET B CG  1 
ATOM   4397 S SD  . MET B 1 281 ? -87.398  8.041  -70.108 1.00 46.09 ? 281  MET B SD  1 
ATOM   4398 C CE  . MET B 1 281 ? -88.474  7.018  -71.096 1.00 45.89 ? 281  MET B CE  1 
ATOM   4399 N N   . LYS B 1 282 ? -84.047  3.847  -67.836 1.00 48.72 ? 282  LYS B N   1 
ATOM   4400 C CA  . LYS B 1 282 ? -83.244  2.624  -67.883 1.00 49.08 ? 282  LYS B CA  1 
ATOM   4401 C C   . LYS B 1 282 ? -83.675  1.593  -66.838 1.00 48.58 ? 282  LYS B C   1 
ATOM   4402 O O   . LYS B 1 282 ? -83.877  0.431  -67.161 1.00 48.63 ? 282  LYS B O   1 
ATOM   4403 C CB  . LYS B 1 282 ? -81.766  2.956  -67.648 1.00 49.69 ? 282  LYS B CB  1 
ATOM   4404 C CG  . LYS B 1 282 ? -80.974  3.377  -68.880 1.00 51.77 ? 282  LYS B CG  1 
ATOM   4405 C CD  . LYS B 1 282 ? -79.540  3.812  -68.508 1.00 54.94 ? 282  LYS B CD  1 
ATOM   4406 C CE  . LYS B 1 282 ? -78.802  2.773  -67.626 1.00 56.98 ? 282  LYS B CE  1 
ATOM   4407 N NZ  . LYS B 1 282 ? -78.688  3.223  -66.189 1.00 58.17 ? 282  LYS B NZ  1 
ATOM   4408 N N   . HIS B 1 283 ? -83.808  2.038  -65.591 1.00 48.21 ? 283  HIS B N   1 
ATOM   4409 C CA  . HIS B 1 283 ? -84.143  1.178  -64.458 1.00 47.94 ? 283  HIS B CA  1 
ATOM   4410 C C   . HIS B 1 283 ? -85.653  1.088  -64.165 1.00 46.96 ? 283  HIS B C   1 
ATOM   4411 O O   . HIS B 1 283 ? -86.057  0.539  -63.130 1.00 46.89 ? 283  HIS B O   1 
ATOM   4412 C CB  . HIS B 1 283 ? -83.415  1.683  -63.207 1.00 48.64 ? 283  HIS B CB  1 
ATOM   4413 C CG  . HIS B 1 283 ? -81.919  1.615  -63.297 1.00 50.73 ? 283  HIS B CG  1 
ATOM   4414 N ND1 . HIS B 1 283 ? -81.214  0.438  -63.152 1.00 52.11 ? 283  HIS B ND1 1 
ATOM   4415 C CD2 . HIS B 1 283 ? -80.993  2.583  -63.497 1.00 51.97 ? 283  HIS B CD2 1 
ATOM   4416 C CE1 . HIS B 1 283 ? -79.922  0.681  -63.272 1.00 53.05 ? 283  HIS B CE1 1 
ATOM   4417 N NE2 . HIS B 1 283 ? -79.760  1.976  -63.481 1.00 53.08 ? 283  HIS B NE2 1 
ATOM   4418 N N   . CYS B 1 284 ? -86.480  1.628  -65.062 1.00 45.72 ? 284  CYS B N   1 
ATOM   4419 C CA  . CYS B 1 284 ? -87.920  1.738  -64.806 1.00 44.72 ? 284  CYS B CA  1 
ATOM   4420 C C   . CYS B 1 284 ? -88.726  1.852  -66.105 1.00 44.01 ? 284  CYS B C   1 
ATOM   4421 O O   . CYS B 1 284 ? -88.836  2.933  -66.698 1.00 44.11 ? 284  CYS B O   1 
ATOM   4422 C CB  . CYS B 1 284 ? -88.204  2.925  -63.871 1.00 44.67 ? 284  CYS B CB  1 
ATOM   4423 S SG  . CYS B 1 284 ? -89.847  2.966  -63.111 1.00 44.09 ? 284  CYS B SG  1 
ATOM   4424 N N   . SER B 1 285 ? -89.287  0.726  -66.542 1.00 42.95 ? 285  SER B N   1 
ATOM   4425 C CA  . SER B 1 285 ? -89.988  0.650  -67.830 1.00 42.07 ? 285  SER B CA  1 
ATOM   4426 C C   . SER B 1 285 ? -91.376  1.319  -67.813 1.00 40.96 ? 285  SER B C   1 
ATOM   4427 O O   . SER B 1 285 ? -91.947  1.624  -68.865 1.00 40.86 ? 285  SER B O   1 
ATOM   4428 C CB  . SER B 1 285 ? -90.093  -0.808 -68.309 1.00 42.45 ? 285  SER B CB  1 
ATOM   4429 O OG  . SER B 1 285 ? -90.178  -1.728 -67.223 1.00 42.86 ? 285  SER B OG  1 
ATOM   4430 N N   . LYS B 1 286 ? -91.901  1.548  -66.613 1.00 39.54 ? 286  LYS B N   1 
ATOM   4431 C CA  . LYS B 1 286 ? -93.186  2.230  -66.430 1.00 38.05 ? 286  LYS B CA  1 
ATOM   4432 C C   . LYS B 1 286 ? -93.160  3.736  -66.749 1.00 36.48 ? 286  LYS B C   1 
ATOM   4433 O O   . LYS B 1 286 ? -94.202  4.357  -66.888 1.00 36.20 ? 286  LYS B O   1 
ATOM   4434 C CB  . LYS B 1 286 ? -93.700  2.005  -65.008 1.00 38.34 ? 286  LYS B CB  1 
ATOM   4435 C CG  . LYS B 1 286 ? -93.905  0.540  -64.642 1.00 39.36 ? 286  LYS B CG  1 
ATOM   4436 C CD  . LYS B 1 286 ? -95.158  0.370  -63.803 1.00 40.68 ? 286  LYS B CD  1 
ATOM   4437 C CE  . LYS B 1 286 ? -95.357  -1.065 -63.370 1.00 41.79 ? 286  LYS B CE  1 
ATOM   4438 N NZ  . LYS B 1 286 ? -94.963  -1.241 -61.939 1.00 43.19 ? 286  LYS B NZ  1 
ATOM   4439 N N   . ILE B 1 287 ? -91.974  4.313  -66.891 1.00 34.97 ? 287  ILE B N   1 
ATOM   4440 C CA  . ILE B 1 287 ? -91.861  5.749  -67.113 1.00 33.42 ? 287  ILE B CA  1 
ATOM   4441 C C   . ILE B 1 287 ? -91.931  6.159  -68.589 1.00 32.69 ? 287  ILE B C   1 
ATOM   4442 O O   . ILE B 1 287 ? -91.238  5.613  -69.455 1.00 32.43 ? 287  ILE B O   1 
ATOM   4443 C CB  . ILE B 1 287 ? -90.596  6.328  -66.394 1.00 33.35 ? 287  ILE B CB  1 
ATOM   4444 C CG1 . ILE B 1 287 ? -90.710  6.113  -64.875 1.00 33.05 ? 287  ILE B CG1 1 
ATOM   4445 C CG2 . ILE B 1 287 ? -90.389  7.823  -66.731 1.00 32.36 ? 287  ILE B CG2 1 
ATOM   4446 C CD1 . ILE B 1 287 ? -89.458  6.452  -64.110 1.00 33.40 ? 287  ILE B CD1 1 
ATOM   4447 N N   . GLN B 1 288 ? -92.793  7.128  -68.863 1.00 31.75 ? 288  GLN B N   1 
ATOM   4448 C CA  . GLN B 1 288 ? -92.857  7.747  -70.172 1.00 31.29 ? 288  GLN B CA  1 
ATOM   4449 C C   . GLN B 1 288 ? -92.708  9.255  -69.972 1.00 31.07 ? 288  GLN B C   1 
ATOM   4450 O O   . GLN B 1 288 ? -93.192  9.807  -68.971 1.00 31.03 ? 288  GLN B O   1 
ATOM   4451 C CB  . GLN B 1 288 ? -94.161  7.371  -70.898 1.00 31.03 ? 288  GLN B CB  1 
ATOM   4452 C CG  . GLN B 1 288 ? -94.269  5.864  -71.207 1.00 31.66 ? 288  GLN B CG  1 
ATOM   4453 C CD  . GLN B 1 288 ? -95.642  5.437  -71.717 1.00 33.24 ? 288  GLN B CD  1 
ATOM   4454 O OE1 . GLN B 1 288 ? -96.194  4.437  -71.253 1.00 33.60 ? 288  GLN B OE1 1 
ATOM   4455 N NE2 . GLN B 1 288 ? -96.193  6.187  -72.670 1.00 34.17 ? 288  GLN B NE2 1 
ATOM   4456 N N   . VAL B 1 289 ? -92.023  9.904  -70.916 1.00 30.63 ? 289  VAL B N   1 
ATOM   4457 C CA  . VAL B 1 289 ? -91.686  11.313 -70.815 1.00 30.39 ? 289  VAL B CA  1 
ATOM   4458 C C   . VAL B 1 289 ? -92.344  12.094 -71.922 1.00 30.74 ? 289  VAL B C   1 
ATOM   4459 O O   . VAL B 1 289 ? -92.164  11.770 -73.102 1.00 30.91 ? 289  VAL B O   1 
ATOM   4460 C CB  . VAL B 1 289 ? -90.161  11.546 -70.911 1.00 30.15 ? 289  VAL B CB  1 
ATOM   4461 C CG1 . VAL B 1 289 ? -89.840  13.019 -71.019 1.00 29.54 ? 289  VAL B CG1 1 
ATOM   4462 C CG2 . VAL B 1 289 ? -89.482  10.995 -69.711 1.00 30.21 ? 289  VAL B CG2 1 
ATOM   4463 N N   . ILE B 1 290 ? -93.100  13.126 -71.542 1.00 30.76 ? 290  ILE B N   1 
ATOM   4464 C CA  . ILE B 1 290 ? -93.568  14.110 -72.503 1.00 30.81 ? 290  ILE B CA  1 
ATOM   4465 C C   . ILE B 1 290 ? -92.469  15.160 -72.643 1.00 31.07 ? 290  ILE B C   1 
ATOM   4466 O O   . ILE B 1 290 ? -91.967  15.695 -71.655 1.00 31.01 ? 290  ILE B O   1 
ATOM   4467 C CB  . ILE B 1 290 ? -94.890  14.761 -72.046 1.00 30.81 ? 290  ILE B CB  1 
ATOM   4468 C CG1 . ILE B 1 290 ? -95.978  13.709 -71.848 1.00 30.58 ? 290  ILE B CG1 1 
ATOM   4469 C CG2 . ILE B 1 290 ? -95.364  15.830 -73.062 1.00 30.39 ? 290  ILE B CG2 1 
ATOM   4470 C CD1 . ILE B 1 290 ? -97.195  14.240 -71.080 1.00 31.00 ? 290  ILE B CD1 1 
ATOM   4471 N N   . ASP B 1 291 ? -92.072  15.429 -73.875 1.00 31.50 ? 291  ASP B N   1 
ATOM   4472 C CA  . ASP B 1 291 ? -91.056  16.434 -74.124 1.00 31.78 ? 291  ASP B CA  1 
ATOM   4473 C C   . ASP B 1 291 ? -91.719  17.798 -74.084 1.00 31.52 ? 291  ASP B C   1 
ATOM   4474 O O   . ASP B 1 291 ? -92.642  18.047 -74.850 1.00 31.65 ? 291  ASP B O   1 
ATOM   4475 C CB  . ASP B 1 291 ? -90.419  16.208 -75.486 1.00 32.18 ? 291  ASP B CB  1 
ATOM   4476 C CG  . ASP B 1 291 ? -89.436  17.294 -75.852 1.00 33.44 ? 291  ASP B CG  1 
ATOM   4477 O OD1 . ASP B 1 291 ? -88.865  17.916 -74.933 1.00 34.54 ? 291  ASP B OD1 1 
ATOM   4478 O OD2 . ASP B 1 291 ? -89.169  17.596 -77.029 1.00 35.25 ? 291  ASP B OD2 1 
ATOM   4479 N N   . ILE B 1 292 ? -91.266  18.669 -73.190 1.00 30.99 ? 292  ILE B N   1 
ATOM   4480 C CA  . ILE B 1 292 ? -91.828  20.008 -73.105 1.00 30.77 ? 292  ILE B CA  1 
ATOM   4481 C C   . ILE B 1 292 ? -90.848  21.093 -73.563 1.00 30.87 ? 292  ILE B C   1 
ATOM   4482 O O   . ILE B 1 292 ? -91.135  22.295 -73.419 1.00 30.72 ? 292  ILE B O   1 
ATOM   4483 C CB  . ILE B 1 292 ? -92.380  20.315 -71.686 1.00 30.79 ? 292  ILE B CB  1 
ATOM   4484 C CG1 . ILE B 1 292 ? -91.349  19.986 -70.594 1.00 30.79 ? 292  ILE B CG1 1 
ATOM   4485 C CG2 . ILE B 1 292 ? -93.700  19.590 -71.459 1.00 30.24 ? 292  ILE B CG2 1 
ATOM   4486 C CD1 . ILE B 1 292 ? -90.201  20.975 -70.479 1.00 29.71 ? 292  ILE B CD1 1 
ATOM   4487 N N   . SER B 1 293 ? -89.716  20.670 -74.131 1.00 30.73 ? 293  SER B N   1 
ATOM   4488 C CA  . SER B 1 293 ? -88.703  21.596 -74.627 1.00 31.07 ? 293  SER B CA  1 
ATOM   4489 C C   . SER B 1 293 ? -89.267  22.621 -75.626 1.00 31.26 ? 293  SER B C   1 
ATOM   4490 O O   . SER B 1 293 ? -88.858  23.785 -75.636 1.00 30.77 ? 293  SER B O   1 
ATOM   4491 C CB  . SER B 1 293 ? -87.544  20.837 -75.254 1.00 31.15 ? 293  SER B CB  1 
ATOM   4492 O OG  . SER B 1 293 ? -87.993  19.961 -76.270 1.00 31.56 ? 293  SER B OG  1 
ATOM   4493 N N   . MET B 1 294 ? -90.219  22.176 -76.439 1.00 31.73 ? 294  MET B N   1 
ATOM   4494 C CA  . MET B 1 294 ? -90.893  23.033 -77.411 1.00 32.63 ? 294  MET B CA  1 
ATOM   4495 C C   . MET B 1 294 ? -91.764  24.117 -76.764 1.00 31.50 ? 294  MET B C   1 
ATOM   4496 O O   . MET B 1 294 ? -91.912  25.207 -77.316 1.00 31.24 ? 294  MET B O   1 
ATOM   4497 C CB  . MET B 1 294 ? -91.740  22.181 -78.371 1.00 33.84 ? 294  MET B CB  1 
ATOM   4498 C CG  . MET B 1 294 ? -92.171  20.833 -77.770 1.00 38.51 ? 294  MET B CG  1 
ATOM   4499 S SD  . MET B 1 294 ? -93.769  21.021 -76.971 1.00 45.63 ? 294  MET B SD  1 
ATOM   4500 C CE  . MET B 1 294 ? -93.909  19.557 -76.064 1.00 46.27 ? 294  MET B CE  1 
ATOM   4501 N N   . ILE B 1 295 ? -92.359  23.805 -75.617 1.00 30.57 ? 295  ILE B N   1 
ATOM   4502 C CA  . ILE B 1 295 ? -93.110  24.801 -74.846 1.00 29.95 ? 295  ILE B CA  1 
ATOM   4503 C C   . ILE B 1 295 ? -92.153  25.823 -74.199 1.00 29.38 ? 295  ILE B C   1 
ATOM   4504 O O   . ILE B 1 295 ? -92.418  27.023 -74.190 1.00 29.02 ? 295  ILE B O   1 
ATOM   4505 C CB  . ILE B 1 295 ? -94.004  24.110 -73.791 1.00 29.90 ? 295  ILE B CB  1 
ATOM   4506 C CG1 . ILE B 1 295 ? -94.883  23.046 -74.472 1.00 30.48 ? 295  ILE B CG1 1 
ATOM   4507 C CG2 . ILE B 1 295 ? -94.865  25.120 -73.069 1.00 28.97 ? 295  ILE B CG2 1 
ATOM   4508 C CD1 . ILE B 1 295 ? -95.671  22.156 -73.517 1.00 30.57 ? 295  ILE B CD1 1 
ATOM   4509 N N   . LEU B 1 296 ? -91.031  25.338 -73.686 1.00 28.83 ? 296  LEU B N   1 
ATOM   4510 C CA  . LEU B 1 296 ? -90.005  26.223 -73.171 1.00 28.67 ? 296  LEU B CA  1 
ATOM   4511 C C   . LEU B 1 296 ? -89.390  27.094 -74.274 1.00 28.67 ? 296  LEU B C   1 
ATOM   4512 O O   . LEU B 1 296 ? -89.274  28.314 -74.102 1.00 28.24 ? 296  LEU B O   1 
ATOM   4513 C CB  . LEU B 1 296 ? -88.942  25.439 -72.397 1.00 28.45 ? 296  LEU B CB  1 
ATOM   4514 C CG  . LEU B 1 296 ? -89.442  24.886 -71.059 1.00 27.82 ? 296  LEU B CG  1 
ATOM   4515 C CD1 . LEU B 1 296 ? -88.357  24.078 -70.388 1.00 26.71 ? 296  LEU B CD1 1 
ATOM   4516 C CD2 . LEU B 1 296 ? -89.905  26.007 -70.142 1.00 27.71 ? 296  LEU B CD2 1 
ATOM   4517 N N   . ALA B 1 297 ? -89.040  26.485 -75.410 1.00 28.74 ? 297  ALA B N   1 
ATOM   4518 C CA  . ALA B 1 297 ? -88.463  27.237 -76.538 1.00 28.81 ? 297  ALA B CA  1 
ATOM   4519 C C   . ALA B 1 297 ? -89.411  28.315 -77.064 1.00 28.73 ? 297  ALA B C   1 
ATOM   4520 O O   . ALA B 1 297 ? -88.995  29.424 -77.365 1.00 28.34 ? 297  ALA B O   1 
ATOM   4521 C CB  . ALA B 1 297 ? -88.030  26.303 -77.658 1.00 28.57 ? 297  ALA B CB  1 
ATOM   4522 N N   . GLU B 1 298 ? -90.688  27.981 -77.137 1.00 29.16 ? 298  GLU B N   1 
ATOM   4523 C CA  . GLU B 1 298 ? -91.707  28.896 -77.635 1.00 30.15 ? 298  GLU B CA  1 
ATOM   4524 C C   . GLU B 1 298 ? -91.963  30.075 -76.701 1.00 29.73 ? 298  GLU B C   1 
ATOM   4525 O O   . GLU B 1 298 ? -92.172  31.195 -77.157 1.00 29.69 ? 298  GLU B O   1 
ATOM   4526 C CB  . GLU B 1 298 ? -93.005  28.133 -77.889 1.00 31.06 ? 298  GLU B CB  1 
ATOM   4527 C CG  . GLU B 1 298 ? -94.059  28.927 -78.628 1.00 34.65 ? 298  GLU B CG  1 
ATOM   4528 C CD  . GLU B 1 298 ? -93.771  29.053 -80.115 1.00 38.35 ? 298  GLU B CD  1 
ATOM   4529 O OE1 . GLU B 1 298 ? -92.627  28.772 -80.539 1.00 39.29 ? 298  GLU B OE1 1 
ATOM   4530 O OE2 . GLU B 1 298 ? -94.699  29.441 -80.864 1.00 40.29 ? 298  GLU B OE2 1 
ATOM   4531 N N   . ALA B 1 299 ? -91.947  29.823 -75.396 1.00 29.09 ? 299  ALA B N   1 
ATOM   4532 C CA  . ALA B 1 299 ? -92.052  30.908 -74.430 1.00 28.70 ? 299  ALA B CA  1 
ATOM   4533 C C   . ALA B 1 299 ? -90.831  31.831 -74.500 1.00 28.54 ? 299  ALA B C   1 
ATOM   4534 O O   . ALA B 1 299 ? -90.972  33.045 -74.376 1.00 28.84 ? 299  ALA B O   1 
ATOM   4535 C CB  . ALA B 1 299 ? -92.263  30.372 -73.013 1.00 28.45 ? 299  ALA B CB  1 
ATOM   4536 N N   . ILE B 1 300 ? -89.646  31.274 -74.708 1.00 28.27 ? 300  ILE B N   1 
ATOM   4537 C CA  . ILE B 1 300 ? -88.452  32.112 -74.857 1.00 28.67 ? 300  ILE B CA  1 
ATOM   4538 C C   . ILE B 1 300 ? -88.542  32.985 -76.108 1.00 29.83 ? 300  ILE B C   1 
ATOM   4539 O O   . ILE B 1 300 ? -88.292  34.187 -76.038 1.00 29.45 ? 300  ILE B O   1 
ATOM   4540 C CB  . ILE B 1 300 ? -87.150  31.274 -74.847 1.00 27.96 ? 300  ILE B CB  1 
ATOM   4541 C CG1 . ILE B 1 300 ? -86.876  30.740 -73.441 1.00 25.80 ? 300  ILE B CG1 1 
ATOM   4542 C CG2 . ILE B 1 300 ? -85.961  32.101 -75.341 1.00 27.70 ? 300  ILE B CG2 1 
ATOM   4543 C CD1 . ILE B 1 300 ? -86.130  29.441 -73.438 1.00 23.82 ? 300  ILE B CD1 1 
ATOM   4544 N N   . ARG B 1 301 ? -88.935  32.370 -77.226 1.00 31.59 ? 301  ARG B N   1 
ATOM   4545 C CA  . ARG B 1 301 ? -89.086  33.041 -78.518 1.00 33.60 ? 301  ARG B CA  1 
ATOM   4546 C C   . ARG B 1 301 ? -90.090  34.177 -78.455 1.00 34.29 ? 301  ARG B C   1 
ATOM   4547 O O   . ARG B 1 301 ? -89.853  35.250 -79.012 1.00 34.34 ? 301  ARG B O   1 
ATOM   4548 C CB  . ARG B 1 301 ? -89.513  32.053 -79.602 1.00 34.48 ? 301  ARG B CB  1 
ATOM   4549 C CG  . ARG B 1 301 ? -89.190  32.504 -81.034 1.00 37.94 ? 301  ARG B CG  1 
ATOM   4550 C CD  . ARG B 1 301 ? -89.684  31.561 -82.149 1.00 42.20 ? 301  ARG B CD  1 
ATOM   4551 N NE  . ARG B 1 301 ? -90.788  32.183 -82.886 1.00 45.86 ? 301  ARG B NE  1 
ATOM   4552 C CZ  . ARG B 1 301 ? -92.071  31.848 -82.752 1.00 47.52 ? 301  ARG B CZ  1 
ATOM   4553 N NH1 . ARG B 1 301 ? -92.424  30.876 -81.923 1.00 47.96 ? 301  ARG B NH1 1 
ATOM   4554 N NH2 . ARG B 1 301 ? -93.006  32.484 -83.451 1.00 48.58 ? 301  ARG B NH2 1 
ATOM   4555 N N   . ARG B 1 302 ? -91.207  33.927 -77.776 1.00 35.16 ? 302  ARG B N   1 
ATOM   4556 C CA  . ARG B 1 302 ? -92.267  34.911 -77.621 1.00 36.01 ? 302  ARG B CA  1 
ATOM   4557 C C   . ARG B 1 302 ? -91.835  36.064 -76.723 1.00 35.84 ? 302  ARG B C   1 
ATOM   4558 O O   . ARG B 1 302 ? -92.026  37.235 -77.071 1.00 36.10 ? 302  ARG B O   1 
ATOM   4559 C CB  . ARG B 1 302 ? -93.529  34.249 -77.058 1.00 36.78 ? 302  ARG B CB  1 
ATOM   4560 C CG  . ARG B 1 302 ? -93.979  32.996 -77.785 1.00 39.09 ? 302  ARG B CG  1 
ATOM   4561 C CD  . ARG B 1 302 ? -94.770  33.251 -79.057 1.00 42.49 ? 302  ARG B CD  1 
ATOM   4562 N NE  . ARG B 1 302 ? -95.279  32.014 -79.665 1.00 44.45 ? 302  ARG B NE  1 
ATOM   4563 C CZ  . ARG B 1 302 ? -96.567  31.762 -79.907 1.00 45.00 ? 302  ARG B CZ  1 
ATOM   4564 N NH1 . ARG B 1 302 ? -97.510  32.641 -79.583 1.00 44.35 ? 302  ARG B NH1 1 
ATOM   4565 N NH2 . ARG B 1 302 ? -96.913  30.620 -80.480 1.00 45.67 ? 302  ARG B NH2 1 
ATOM   4566 N N   . THR B 1 303 ? -91.261  35.720 -75.570 1.00 35.69 ? 303  THR B N   1 
ATOM   4567 C CA  . THR B 1 303 ? -90.636  36.682 -74.666 1.00 35.65 ? 303  THR B CA  1 
ATOM   4568 C C   . THR B 1 303 ? -89.712  37.588 -75.439 1.00 35.87 ? 303  THR B C   1 
ATOM   4569 O O   . THR B 1 303 ? -89.806  38.813 -75.350 1.00 35.66 ? 303  THR B O   1 
ATOM   4570 C CB  . THR B 1 303 ? -89.821  35.945 -73.588 1.00 35.42 ? 303  THR B CB  1 
ATOM   4571 O OG1 . THR B 1 303 ? -90.716  35.324 -72.674 1.00 35.97 ? 303  THR B OG1 1 
ATOM   4572 C CG2 . THR B 1 303 ? -89.056  36.910 -72.697 1.00 34.99 ? 303  THR B CG2 1 
ATOM   4573 N N   . HIS B 1 304 ? -88.809  36.976 -76.197 1.00 36.44 ? 304  HIS B N   1 
ATOM   4574 C CA  . HIS B 1 304 ? -87.834  37.744 -76.947 1.00 37.24 ? 304  HIS B CA  1 
ATOM   4575 C C   . HIS B 1 304 ? -88.514  38.694 -77.933 1.00 38.23 ? 304  HIS B C   1 
ATOM   4576 O O   . HIS B 1 304 ? -88.177  39.870 -77.979 1.00 38.21 ? 304  HIS B O   1 
ATOM   4577 C CB  . HIS B 1 304 ? -86.845  36.832 -77.650 1.00 36.78 ? 304  HIS B CB  1 
ATOM   4578 C CG  . HIS B 1 304 ? -85.807  37.569 -78.427 1.00 35.89 ? 304  HIS B CG  1 
ATOM   4579 N ND1 . HIS B 1 304 ? -84.867  38.377 -77.829 1.00 35.43 ? 304  HIS B ND1 1 
ATOM   4580 C CD2 . HIS B 1 304 ? -85.569  37.635 -79.756 1.00 35.14 ? 304  HIS B CD2 1 
ATOM   4581 C CE1 . HIS B 1 304 ? -84.088  38.903 -78.755 1.00 35.11 ? 304  HIS B CE1 1 
ATOM   4582 N NE2 . HIS B 1 304 ? -84.490  38.465 -79.933 1.00 34.87 ? 304  HIS B NE2 1 
ATOM   4583 N N   . ASN B 1 305 ? -89.498  38.194 -78.675 1.00 39.80 ? 305  ASN B N   1 
ATOM   4584 C CA  . ASN B 1 305 ? -90.139  38.970 -79.746 1.00 41.56 ? 305  ASN B CA  1 
ATOM   4585 C C   . ASN B 1 305 ? -91.207  39.943 -79.276 1.00 43.17 ? 305  ASN B C   1 
ATOM   4586 O O   . ASN B 1 305 ? -91.659  40.777 -80.052 1.00 43.13 ? 305  ASN B O   1 
ATOM   4587 C CB  . ASN B 1 305 ? -90.730  38.049 -80.816 1.00 41.27 ? 305  ASN B CB  1 
ATOM   4588 C CG  . ASN B 1 305 ? -89.669  37.369 -81.653 1.00 41.19 ? 305  ASN B CG  1 
ATOM   4589 O OD1 . ASN B 1 305 ? -88.591  37.915 -81.876 1.00 41.72 ? 305  ASN B OD1 1 
ATOM   4590 N ND2 . ASN B 1 305 ? -89.965  36.164 -82.113 1.00 41.44 ? 305  ASN B ND2 1 
ATOM   4591 N N   . GLY B 1 306 ? -91.600  39.846 -78.007 1.00 45.27 ? 306  GLY B N   1 
ATOM   4592 C CA  . GLY B 1 306 ? -92.730  40.613 -77.502 1.00 47.44 ? 306  GLY B CA  1 
ATOM   4593 C C   . GLY B 1 306 ? -94.061  40.064 -78.008 1.00 49.22 ? 306  GLY B C   1 
ATOM   4594 O O   . GLY B 1 306 ? -95.013  40.817 -78.201 1.00 49.11 ? 306  GLY B O   1 
ATOM   4595 N N   . GLU B 1 307 ? -94.123  38.747 -78.218 1.00 51.16 ? 307  GLU B N   1 
ATOM   4596 C CA  . GLU B 1 307 ? -95.338  38.088 -78.702 1.00 53.16 ? 307  GLU B CA  1 
ATOM   4597 C C   . GLU B 1 307 ? -96.066  37.326 -77.604 1.00 54.31 ? 307  GLU B C   1 
ATOM   4598 O O   . GLU B 1 307 ? -95.440  36.857 -76.648 1.00 54.19 ? 307  GLU B O   1 
ATOM   4599 C CB  . GLU B 1 307 ? -95.008  37.122 -79.838 1.00 53.38 ? 307  GLU B CB  1 
ATOM   4600 C CG  . GLU B 1 307 ? -95.216  37.705 -81.222 1.00 54.71 ? 307  GLU B CG  1 
ATOM   4601 C CD  . GLU B 1 307 ? -94.237  37.134 -82.229 1.00 56.59 ? 307  GLU B CD  1 
ATOM   4602 O OE1 . GLU B 1 307 ? -93.570  37.935 -82.939 1.00 56.90 ? 307  GLU B OE1 1 
ATOM   4603 O OE2 . GLU B 1 307 ? -94.137  35.881 -82.301 1.00 57.31 ? 307  GLU B OE2 1 
ATOM   4604 N N   . SER B 1 308 ? -97.385  37.194 -77.775 1.00 55.87 ? 308  SER B N   1 
ATOM   4605 C CA  . SER B 1 308 ? -98.270  36.483 -76.847 1.00 57.44 ? 308  SER B CA  1 
ATOM   4606 C C   . SER B 1 308 ? -97.748  35.097 -76.464 1.00 58.52 ? 308  SER B C   1 
ATOM   4607 O O   . SER B 1 308 ? -97.374  34.309 -77.327 1.00 58.67 ? 308  SER B O   1 
ATOM   4608 C CB  . SER B 1 308 ? -99.684  36.376 -77.443 1.00 57.50 ? 308  SER B CB  1 
ATOM   4609 O OG  . SER B 1 308 ? -100.490 35.432 -76.744 1.00 58.06 ? 308  SER B OG  1 
ATOM   4610 N N   . VAL B 1 309 ? -97.705  34.826 -75.162 1.00 60.08 ? 309  VAL B N   1 
ATOM   4611 C CA  . VAL B 1 309 ? -97.331  33.509 -74.645 1.00 61.83 ? 309  VAL B CA  1 
ATOM   4612 C C   . VAL B 1 309 ? -98.555  32.801 -74.045 1.00 63.54 ? 309  VAL B C   1 
ATOM   4613 O O   . VAL B 1 309 ? -98.499  31.611 -73.746 1.00 63.75 ? 309  VAL B O   1 
ATOM   4614 C CB  . VAL B 1 309 ? -96.187  33.589 -73.589 1.00 61.50 ? 309  VAL B CB  1 
ATOM   4615 C CG1 . VAL B 1 309 ? -95.621  32.212 -73.300 1.00 61.42 ? 309  VAL B CG1 1 
ATOM   4616 C CG2 . VAL B 1 309 ? -95.077  34.504 -74.053 1.00 60.81 ? 309  VAL B CG2 1 
ATOM   4617 N N   . SER B 1 310 ? -99.652  33.545 -73.878 1.00 65.65 ? 310  SER B N   1 
ATOM   4618 C CA  . SER B 1 310 ? -100.907 33.025 -73.318 1.00 67.75 ? 310  SER B CA  1 
ATOM   4619 C C   . SER B 1 310 ? -101.465 31.894 -74.175 1.00 69.27 ? 310  SER B C   1 
ATOM   4620 O O   . SER B 1 310 ? -102.184 31.026 -73.687 1.00 69.14 ? 310  SER B O   1 
ATOM   4621 C CB  . SER B 1 310 ? -101.951 34.146 -73.214 1.00 67.76 ? 310  SER B CB  1 
ATOM   4622 O OG  . SER B 1 310 ? -101.908 34.780 -71.948 1.00 68.05 ? 310  SER B OG  1 
ATOM   4623 N N   . TYR B 1 311 ? -101.125 31.948 -75.462 1.00 71.41 ? 311  TYR B N   1 
ATOM   4624 C CA  . TYR B 1 311 ? -101.468 30.949 -76.469 1.00 73.47 ? 311  TYR B CA  1 
ATOM   4625 C C   . TYR B 1 311 ? -100.879 29.569 -76.121 1.00 74.53 ? 311  TYR B C   1 
ATOM   4626 O O   . TYR B 1 311 ? -101.439 28.542 -76.499 1.00 74.45 ? 311  TYR B O   1 
ATOM   4627 C CB  . TYR B 1 311 ? -100.993 31.481 -77.832 1.00 73.99 ? 311  TYR B CB  1 
ATOM   4628 C CG  . TYR B 1 311 ? -100.704 30.483 -78.941 1.00 75.79 ? 311  TYR B CG  1 
ATOM   4629 C CD1 . TYR B 1 311 ? -101.492 30.458 -80.101 1.00 77.25 ? 311  TYR B CD1 1 
ATOM   4630 C CD2 . TYR B 1 311 ? -99.609  29.612 -78.869 1.00 76.83 ? 311  TYR B CD2 1 
ATOM   4631 C CE1 . TYR B 1 311 ? -101.220 29.564 -81.143 1.00 78.20 ? 311  TYR B CE1 1 
ATOM   4632 C CE2 . TYR B 1 311 ? -99.335  28.711 -79.901 1.00 77.91 ? 311  TYR B CE2 1 
ATOM   4633 C CZ  . TYR B 1 311 ? -100.138 28.697 -81.033 1.00 78.50 ? 311  TYR B CZ  1 
ATOM   4634 O OH  . TYR B 1 311 ? -99.863  27.815 -82.051 1.00 79.17 ? 311  TYR B OH  1 
ATOM   4635 N N   . LEU B 1 312 ? -99.764  29.566 -75.382 1.00 75.96 ? 312  LEU B N   1 
ATOM   4636 C CA  . LEU B 1 312 ? -99.103  28.342 -74.913 1.00 77.32 ? 312  LEU B CA  1 
ATOM   4637 C C   . LEU B 1 312 ? -99.848  27.677 -73.751 1.00 78.61 ? 312  LEU B C   1 
ATOM   4638 O O   . LEU B 1 312 ? -99.439  26.611 -73.274 1.00 78.56 ? 312  LEU B O   1 
ATOM   4639 C CB  . LEU B 1 312 ? -97.659  28.643 -74.485 1.00 77.12 ? 312  LEU B CB  1 
ATOM   4640 C CG  . LEU B 1 312 ? -96.529  28.701 -75.519 1.00 76.78 ? 312  LEU B CG  1 
ATOM   4641 C CD1 . LEU B 1 312 ? -96.511  30.037 -76.243 1.00 76.94 ? 312  LEU B CD1 1 
ATOM   4642 C CD2 . LEU B 1 312 ? -95.197  28.474 -74.846 1.00 75.91 ? 312  LEU B CD2 1 
ATOM   4643 N N   . PHE B 1 313 ? -100.936 28.308 -73.305 1.00 80.29 ? 313  PHE B N   1 
ATOM   4644 C CA  . PHE B 1 313 ? -101.724 27.819 -72.169 1.00 82.05 ? 313  PHE B CA  1 
ATOM   4645 C C   . PHE B 1 313 ? -102.840 26.836 -72.553 1.00 83.68 ? 313  PHE B C   1 
ATOM   4646 O O   . PHE B 1 313 ? -103.466 26.235 -71.679 1.00 83.80 ? 313  PHE B O   1 
ATOM   4647 C CB  . PHE B 1 313 ? -102.321 28.987 -71.363 1.00 81.76 ? 313  PHE B CB  1 
ATOM   4648 C CG  . PHE B 1 313 ? -101.307 29.803 -70.591 1.00 81.03 ? 313  PHE B CG  1 
ATOM   4649 C CD1 . PHE B 1 313 ? -99.938  29.540 -70.681 1.00 80.47 ? 313  PHE B CD1 1 
ATOM   4650 C CD2 . PHE B 1 313 ? -101.733 30.850 -69.778 1.00 80.43 ? 313  PHE B CD2 1 
ATOM   4651 C CE1 . PHE B 1 313 ? -99.015  30.310 -69.974 1.00 80.28 ? 313  PHE B CE1 1 
ATOM   4652 C CE2 . PHE B 1 313 ? -100.816 31.623 -69.066 1.00 80.28 ? 313  PHE B CE2 1 
ATOM   4653 C CZ  . PHE B 1 313 ? -99.454  31.353 -69.163 1.00 80.18 ? 313  PHE B CZ  1 
ATOM   4654 N N   . SER B 1 314 ? -103.096 26.682 -73.851 1.00 85.74 ? 314  SER B N   1 
ATOM   4655 C CA  . SER B 1 314 ? -104.068 25.695 -74.342 1.00 87.68 ? 314  SER B CA  1 
ATOM   4656 C C   . SER B 1 314 ? -103.742 25.248 -75.770 1.00 89.16 ? 314  SER B C   1 
ATOM   4657 O O   . SER B 1 314 ? -104.625 24.833 -76.525 1.00 89.33 ? 314  SER B O   1 
ATOM   4658 C CB  . SER B 1 314 ? -105.514 26.214 -74.237 1.00 87.70 ? 314  SER B CB  1 
ATOM   4659 O OG  . SER B 1 314 ? -105.584 27.629 -74.308 1.00 87.82 ? 314  SER B OG  1 
ATOM   4660 N N   . HIS B 1 315 ? -102.462 25.336 -76.121 1.00 90.95 ? 315  HIS B N   1 
ATOM   4661 C CA  . HIS B 1 315 ? -101.970 24.953 -77.439 1.00 92.80 ? 315  HIS B CA  1 
ATOM   4662 C C   . HIS B 1 315 ? -100.656 24.193 -77.267 1.00 93.90 ? 315  HIS B C   1 
ATOM   4663 O O   . HIS B 1 315 ? -99.836  24.535 -76.405 1.00 94.10 ? 315  HIS B O   1 
ATOM   4664 C CB  . HIS B 1 315 ? -101.751 26.202 -78.309 1.00 93.05 ? 315  HIS B CB  1 
ATOM   4665 C CG  . HIS B 1 315 ? -102.368 26.123 -79.676 1.00 93.87 ? 315  HIS B CG  1 
ATOM   4666 N ND1 . HIS B 1 315 ? -101.805 25.403 -80.710 1.00 94.28 ? 315  HIS B ND1 1 
ATOM   4667 C CD2 . HIS B 1 315 ? -103.484 26.700 -80.185 1.00 94.21 ? 315  HIS B CD2 1 
ATOM   4668 C CE1 . HIS B 1 315 ? -102.554 25.527 -81.791 1.00 94.37 ? 315  HIS B CE1 1 
ATOM   4669 N NE2 . HIS B 1 315 ? -103.579 26.309 -81.500 1.00 94.36 ? 315  HIS B NE2 1 
ATOM   4670 N N   . VAL B 1 316 ? -100.473 23.152 -78.077 1.00 95.13 ? 316  VAL B N   1 
ATOM   4671 C CA  . VAL B 1 316 ? -99.230  22.383 -78.100 1.00 96.16 ? 316  VAL B CA  1 
ATOM   4672 C C   . VAL B 1 316 ? -98.476  22.719 -79.393 1.00 96.89 ? 316  VAL B C   1 
ATOM   4673 O O   . VAL B 1 316 ? -98.792  22.170 -80.456 1.00 97.04 ? 316  VAL B O   1 
ATOM   4674 C CB  . VAL B 1 316 ? -99.487  20.853 -77.999 1.00 96.22 ? 316  VAL B CB  1 
ATOM   4675 C CG1 . VAL B 1 316 ? -98.188  20.101 -77.716 1.00 96.45 ? 316  VAL B CG1 1 
ATOM   4676 C CG2 . VAL B 1 316 ? -100.534 20.541 -76.931 1.00 96.23 ? 316  VAL B CG2 1 
ATOM   4677 N N   . PRO B 1 317 ? -97.492  23.622 -79.305 1.00 97.47 ? 317  PRO B N   1 
ATOM   4678 C CA  . PRO B 1 317 ? -96.788  24.121 -80.497 1.00 97.84 ? 317  PRO B CA  1 
ATOM   4679 C C   . PRO B 1 317 ? -96.045  23.015 -81.251 1.00 98.12 ? 317  PRO B C   1 
ATOM   4680 O O   . PRO B 1 317 ? -96.043  23.000 -82.484 1.00 98.40 ? 317  PRO B O   1 
ATOM   4681 C CB  . PRO B 1 317 ? -95.800  25.147 -79.924 1.00 97.86 ? 317  PRO B CB  1 
ATOM   4682 C CG  . PRO B 1 317 ? -95.638  24.765 -78.491 1.00 97.78 ? 317  PRO B CG  1 
ATOM   4683 C CD  . PRO B 1 317 ? -96.966  24.221 -78.064 1.00 97.56 ? 317  PRO B CD  1 
HETATM 4684 S S   . SO4 C 2 .   ? -120.130 34.541 -53.188 1.00 79.02 ? 1002 SO4 A S   1 
HETATM 4685 O O1  . SO4 C 2 .   ? -120.643 33.358 -53.875 1.00 79.04 ? 1002 SO4 A O1  1 
HETATM 4686 O O2  . SO4 C 2 .   ? -120.492 35.747 -53.933 1.00 79.05 ? 1002 SO4 A O2  1 
HETATM 4687 O O3  . SO4 C 2 .   ? -120.698 34.600 -51.845 1.00 79.10 ? 1002 SO4 A O3  1 
HETATM 4688 O O4  . SO4 C 2 .   ? -118.677 34.474 -53.081 1.00 78.79 ? 1002 SO4 A O4  1 
HETATM 4689 S S   . SO4 D 2 .   ? -93.963  32.753 -31.496 1.00 38.25 ? 1004 SO4 A S   1 
HETATM 4690 O O1  . SO4 D 2 .   ? -93.190  33.871 -30.962 1.00 38.33 ? 1004 SO4 A O1  1 
HETATM 4691 O O2  . SO4 D 2 .   ? -93.382  32.183 -32.701 1.00 37.38 ? 1004 SO4 A O2  1 
HETATM 4692 O O3  . SO4 D 2 .   ? -94.005  31.734 -30.456 1.00 39.13 ? 1004 SO4 A O3  1 
HETATM 4693 O O4  . SO4 D 2 .   ? -95.307  33.220 -31.818 1.00 38.50 ? 1004 SO4 A O4  1 
HETATM 4694 S S   . SO4 E 2 .   ? -99.951  29.355 -42.170 0.50 66.94 ? 1006 SO4 A S   1 
HETATM 4695 O O1  . SO4 E 2 .   ? -99.062  29.380 -41.012 0.50 67.34 ? 1006 SO4 A O1  1 
HETATM 4696 O O2  . SO4 E 2 .   ? -100.459 30.695 -42.444 0.50 66.68 ? 1006 SO4 A O2  1 
HETATM 4697 O O3  . SO4 E 2 .   ? -99.220  28.853 -43.328 0.50 66.78 ? 1006 SO4 A O3  1 
HETATM 4698 O O4  . SO4 E 2 .   ? -101.088 28.489 -41.883 0.50 67.16 ? 1006 SO4 A O4  1 
HETATM 4699 S S   . SO4 F 2 .   ? -94.260  11.917 -52.816 1.00 63.09 ? 1001 SO4 B S   1 
HETATM 4700 O O1  . SO4 F 2 .   ? -94.863  10.842 -52.031 1.00 63.27 ? 1001 SO4 B O1  1 
HETATM 4701 O O2  . SO4 F 2 .   ? -93.573  11.377 -53.982 1.00 63.37 ? 1001 SO4 B O2  1 
HETATM 4702 O O3  . SO4 F 2 .   ? -95.277  12.824 -53.335 1.00 64.00 ? 1001 SO4 B O3  1 
HETATM 4703 O O4  . SO4 F 2 .   ? -93.340  12.642 -51.957 1.00 62.43 ? 1001 SO4 B O4  1 
HETATM 4704 S S   . SO4 G 2 .   ? -99.259  37.348 -73.167 1.00 33.76 ? 1003 SO4 B S   1 
HETATM 4705 O O1  . SO4 G 2 .   ? -98.418  36.180 -72.896 1.00 33.95 ? 1003 SO4 B O1  1 
HETATM 4706 O O2  . SO4 G 2 .   ? -98.398  38.372 -73.749 1.00 34.63 ? 1003 SO4 B O2  1 
HETATM 4707 O O3  . SO4 G 2 .   ? -100.320 37.009 -74.111 1.00 32.78 ? 1003 SO4 B O3  1 
HETATM 4708 O O4  . SO4 G 2 .   ? -99.837  37.843 -71.917 1.00 33.25 ? 1003 SO4 B O4  1 
HETATM 4709 S S   . SO4 H 2 .   ? -101.463 30.933 -62.624 1.00 44.67 ? 1005 SO4 B S   1 
HETATM 4710 O O1  . SO4 H 2 .   ? -101.401 29.479 -62.598 1.00 44.90 ? 1005 SO4 B O1  1 
HETATM 4711 O O2  . SO4 H 2 .   ? -100.124 31.471 -62.440 1.00 44.54 ? 1005 SO4 B O2  1 
HETATM 4712 O O3  . SO4 H 2 .   ? -102.036 31.410 -63.884 1.00 44.54 ? 1005 SO4 B O3  1 
HETATM 4713 O O4  . SO4 H 2 .   ? -102.303 31.363 -61.505 1.00 45.15 ? 1005 SO4 B O4  1 
HETATM 4714 O O   . HOH I 3 .   ? -96.409  47.979 -33.777 1.00 22.34 ? 1007 HOH A O   1 
HETATM 4715 O O   . HOH I 3 .   ? -94.698  43.382 -49.730 1.00 27.04 ? 1008 HOH A O   1 
HETATM 4716 O O   . HOH I 3 .   ? -111.549 53.694 -26.070 1.00 29.49 ? 1009 HOH A O   1 
HETATM 4717 O O   . HOH I 3 .   ? -109.641 45.672 -43.511 1.00 36.50 ? 1010 HOH A O   1 
HETATM 4718 O O   . HOH I 3 .   ? -98.405  33.009 -38.598 1.00 30.59 ? 1011 HOH A O   1 
HETATM 4719 O O   . HOH I 3 .   ? -110.703 58.918 -31.397 1.00 28.74 ? 1012 HOH A O   1 
HETATM 4720 O O   . HOH I 3 .   ? -91.524  50.920 -27.087 1.00 42.34 ? 1013 HOH A O   1 
HETATM 4721 O O   . HOH I 3 .   ? -93.739  33.297 -35.337 1.00 29.19 ? 1014 HOH A O   1 
HETATM 4722 O O   . HOH I 3 .   ? -92.665  43.725 -46.729 1.00 33.34 ? 1015 HOH A O   1 
HETATM 4723 O O   . HOH I 3 .   ? -114.718 45.220 -43.163 1.00 45.18 ? 1016 HOH A O   1 
HETATM 4724 O O   . HOH I 3 .   ? -99.393  36.726 -18.983 1.00 47.36 ? 1017 HOH A O   1 
HETATM 4725 O O   . HOH I 3 .   ? -97.629  35.491 -67.215 1.00 39.53 ? 1018 HOH A O   1 
HETATM 4726 O O   . HOH I 3 .   ? -96.729  45.696 -56.462 1.00 31.77 ? 1019 HOH A O   1 
HETATM 4727 O O   . HOH I 3 .   ? -97.482  31.090 -44.561 1.00 41.22 ? 1020 HOH A O   1 
HETATM 4728 O O   . HOH I 3 .   ? -93.175  37.418 -43.917 1.00 45.30 ? 1021 HOH A O   1 
HETATM 4729 O O   . HOH I 3 .   ? -107.026 37.478 -74.170 1.00 44.56 ? 1022 HOH A O   1 
HETATM 4730 O O   . HOH I 3 .   ? -110.837 39.126 -51.260 1.00 34.94 ? 1023 HOH A O   1 
HETATM 4731 O O   . HOH I 3 .   ? -104.150 53.248 -27.040 1.00 41.04 ? 1024 HOH A O   1 
HETATM 4732 O O   . HOH I 3 .   ? -106.547 38.125 -59.363 1.00 39.79 ? 1025 HOH A O   1 
HETATM 4733 O O   . HOH I 3 .   ? -106.211 18.988 -44.783 1.00 41.59 ? 1026 HOH A O   1 
HETATM 4734 O O   . HOH I 3 .   ? -111.806 56.982 -46.397 1.00 29.05 ? 1027 HOH A O   1 
HETATM 4735 O O   . HOH I 3 .   ? -92.155  41.122 -50.516 1.00 44.60 ? 1028 HOH A O   1 
HETATM 4736 O O   . HOH I 3 .   ? -105.076 30.376 -70.325 1.00 47.76 ? 1029 HOH A O   1 
HETATM 4737 O O   . HOH I 3 .   ? -105.774 27.382 -29.349 1.00 49.52 ? 1030 HOH A O   1 
HETATM 4738 O O   . HOH I 3 .   ? -89.187  36.976 -46.999 1.00 44.74 ? 1031 HOH A O   1 
HETATM 4739 O O   . HOH I 3 .   ? -104.908 37.169 -76.216 1.00 45.55 ? 1032 HOH A O   1 
HETATM 4740 O O   . HOH I 3 .   ? -91.937  36.311 -46.176 1.00 30.69 ? 1033 HOH A O   1 
HETATM 4741 O O   . HOH I 3 .   ? -95.919  61.740 -32.767 1.00 39.17 ? 1034 HOH A O   1 
HETATM 4742 O O   . HOH I 3 .   ? -109.204 29.572 -43.877 1.00 49.36 ? 1035 HOH A O   1 
HETATM 4743 O O   . HOH I 3 .   ? -112.372 30.017 -53.840 1.00 39.34 ? 1036 HOH A O   1 
HETATM 4744 O O   . HOH I 3 .   ? -109.614 30.008 -54.752 1.00 48.41 ? 1037 HOH A O   1 
HETATM 4745 O O   . HOH I 3 .   ? -107.256 37.429 -43.711 1.00 37.13 ? 1038 HOH A O   1 
HETATM 4746 O O   . HOH I 3 .   ? -108.558 55.048 -32.459 1.00 30.26 ? 1039 HOH A O   1 
HETATM 4747 O O   . HOH I 3 .   ? -109.107 51.293 -42.219 1.00 33.78 ? 1040 HOH A O   1 
HETATM 4748 O O   . HOH I 3 .   ? -119.267 52.422 -44.985 1.00 46.34 ? 1041 HOH A O   1 
HETATM 4749 O O   . HOH I 3 .   ? -120.327 12.475 -57.164 1.00 39.76 ? 1042 HOH A O   1 
HETATM 4750 O O   . HOH I 3 .   ? -103.017 54.089 -24.500 1.00 43.20 ? 1043 HOH A O   1 
HETATM 4751 O O   . HOH I 3 .   ? -92.418  48.643 -44.226 1.00 37.82 ? 1044 HOH A O   1 
HETATM 4752 O O   . HOH I 3 .   ? -108.339 24.802 -48.605 1.00 34.86 ? 1045 HOH A O   1 
HETATM 4753 O O   . HOH I 3 .   ? -117.953 28.407 -24.360 1.00 47.58 ? 1046 HOH A O   1 
HETATM 4754 O O   . HOH I 3 .   ? -103.667 28.386 -47.433 1.00 40.16 ? 1047 HOH A O   1 
HETATM 4755 O O   . HOH I 3 .   ? -118.842 24.103 -70.458 1.00 37.11 ? 1048 HOH A O   1 
HETATM 4756 O O   . HOH I 3 .   ? -100.044 54.060 -23.057 1.00 39.59 ? 1049 HOH A O   1 
HETATM 4757 O O   . HOH I 3 .   ? -108.127 36.577 -46.048 1.00 44.65 ? 1050 HOH A O   1 
HETATM 4758 O O   . HOH I 3 .   ? -113.805 13.873 -27.576 1.00 49.18 ? 1051 HOH A O   1 
HETATM 4759 O O   . HOH I 3 .   ? -130.191 11.380 -51.321 1.00 47.96 ? 1052 HOH A O   1 
HETATM 4760 O O   . HOH I 3 .   ? -115.359 9.324  -46.551 1.00 52.03 ? 1053 HOH A O   1 
HETATM 4761 O O   . HOH I 3 .   ? -108.906 48.679 -43.219 1.00 56.12 ? 1054 HOH A O   1 
HETATM 4762 O O   . HOH I 3 .   ? -89.933  45.031 -47.843 1.00 36.54 ? 1055 HOH A O   1 
HETATM 4763 O O   . HOH I 3 .   ? -111.646 45.266 -45.450 1.00 45.42 ? 1056 HOH A O   1 
HETATM 4764 O O   . HOH I 3 .   ? -115.257 53.826 -29.083 1.00 43.45 ? 1057 HOH A O   1 
HETATM 4765 O O   . HOH I 3 .   ? -116.897 38.374 -40.352 1.00 41.03 ? 1058 HOH A O   1 
HETATM 4766 O O   . HOH I 3 .   ? -114.038 23.472 -68.950 1.00 47.79 ? 1059 HOH A O   1 
HETATM 4767 O O   . HOH I 3 .   ? -111.234 59.247 -22.752 1.00 45.97 ? 1060 HOH A O   1 
HETATM 4768 O O   . HOH I 3 .   ? -96.331  58.485 -23.250 1.00 43.09 ? 1061 HOH A O   1 
HETATM 4769 O O   . HOH I 3 .   ? -107.648 31.819 -54.934 1.00 50.02 ? 1062 HOH A O   1 
HETATM 4770 O O   . HOH I 3 .   ? -105.127 28.091 -54.766 1.00 49.33 ? 1063 HOH A O   1 
HETATM 4771 O O   . HOH I 3 .   ? -107.885 35.857 -62.724 1.00 46.38 ? 1064 HOH A O   1 
HETATM 4772 O O   . HOH I 3 .   ? -108.133 35.155 -59.000 1.00 45.56 ? 1065 HOH A O   1 
HETATM 4773 O O   . HOH I 3 .   ? -112.813 28.733 -41.308 1.00 50.21 ? 1066 HOH A O   1 
HETATM 4774 O O   . HOH I 3 .   ? -88.177  38.653 -45.287 1.00 46.17 ? 1067 HOH A O   1 
HETATM 4775 O O   . HOH I 3 .   ? -109.488 20.492 -30.496 1.00 49.38 ? 1068 HOH A O   1 
HETATM 4776 O O   . HOH I 3 .   ? -114.029 24.248 -57.650 1.00 47.40 ? 1069 HOH A O   1 
HETATM 4777 O O   . HOH I 3 .   ? -108.847 6.831  -35.178 1.00 45.51 ? 1070 HOH A O   1 
HETATM 4778 O O   . HOH I 3 .   ? -110.182 34.654 -46.040 1.00 41.65 ? 1071 HOH A O   1 
HETATM 4779 O O   . HOH I 3 .   ? -120.674 31.768 -51.096 1.00 45.40 ? 1072 HOH A O   1 
HETATM 4780 O O   . HOH I 3 .   ? -118.249 31.178 -49.325 1.00 42.40 ? 1073 HOH A O   1 
HETATM 4781 O O   . HOH I 3 .   ? -117.668 32.198 -52.559 1.00 43.47 ? 1074 HOH A O   1 
HETATM 4782 O O   . HOH I 3 .   ? -127.311 41.492 -47.922 1.00 45.77 ? 1075 HOH A O   1 
HETATM 4783 O O   . HOH I 3 .   ? -91.876  33.039 -25.080 1.00 43.13 ? 1076 HOH A O   1 
HETATM 4784 O O   . HOH I 3 .   ? -112.656 28.457 -50.784 1.00 46.84 ? 1077 HOH A O   1 
HETATM 4785 O O   . HOH I 3 .   ? -103.999 22.899 -43.666 1.00 41.82 ? 1078 HOH A O   1 
HETATM 4786 O O   . HOH I 3 .   ? -101.509 26.507 -43.535 1.00 47.46 ? 1079 HOH A O   1 
HETATM 4787 O O   . HOH J 3 .   ? -103.884 15.951 -47.826 1.00 27.55 ? 1006 HOH B O   1 
HETATM 4788 O O   . HOH J 3 .   ? -99.959  33.573 -60.481 1.00 25.05 ? 1007 HOH B O   1 
HETATM 4789 O O   . HOH J 3 .   ? -83.932  37.839 -70.813 1.00 17.77 ? 1008 HOH B O   1 
HETATM 4790 O O   . HOH J 3 .   ? -88.802  38.633 -54.651 1.00 24.61 ? 1009 HOH B O   1 
HETATM 4791 O O   . HOH J 3 .   ? -105.746 3.163  -46.120 1.00 42.82 ? 1010 HOH B O   1 
HETATM 4792 O O   . HOH J 3 .   ? -88.938  40.364 -57.866 1.00 33.08 ? 1011 HOH B O   1 
HETATM 4793 O O   . HOH J 3 .   ? -89.870  15.999 -64.672 1.00 20.30 ? 1012 HOH B O   1 
HETATM 4794 O O   . HOH J 3 .   ? -84.455  41.981 -60.264 1.00 30.27 ? 1013 HOH B O   1 
HETATM 4795 O O   . HOH J 3 .   ? -118.120 9.370  -52.679 1.00 34.71 ? 1014 HOH B O   1 
HETATM 4796 O O   . HOH J 3 .   ? -70.854  40.966 -71.952 1.00 25.98 ? 1015 HOH B O   1 
HETATM 4797 O O   . HOH J 3 .   ? -94.637  38.637 -60.425 1.00 27.30 ? 1016 HOH B O   1 
HETATM 4798 O O   . HOH J 3 .   ? -90.217  21.752 -53.389 1.00 38.13 ? 1017 HOH B O   1 
HETATM 4799 O O   . HOH J 3 .   ? -117.234 14.053 -60.637 1.00 34.82 ? 1018 HOH B O   1 
HETATM 4800 O O   . HOH J 3 .   ? -117.933 9.913  -67.834 1.00 34.96 ? 1019 HOH B O   1 
HETATM 4801 O O   . HOH J 3 .   ? -91.459  8.782  -47.944 1.00 35.55 ? 1020 HOH B O   1 
HETATM 4802 O O   . HOH J 3 .   ? -112.986 7.288  -74.546 1.00 33.02 ? 1021 HOH B O   1 
HETATM 4803 O O   . HOH J 3 .   ? -85.804  12.279 -62.046 1.00 26.05 ? 1022 HOH B O   1 
HETATM 4804 O O   . HOH J 3 .   ? -89.374  40.712 -68.925 1.00 47.61 ? 1023 HOH B O   1 
HETATM 4805 O O   . HOH J 3 .   ? -90.842  24.520 -80.592 1.00 29.92 ? 1024 HOH B O   1 
HETATM 4806 O O   . HOH J 3 .   ? -73.303  39.371 -81.406 1.00 48.70 ? 1025 HOH B O   1 
HETATM 4807 O O   . HOH J 3 .   ? -70.421  45.376 -68.130 1.00 29.88 ? 1026 HOH B O   1 
HETATM 4808 O O   . HOH J 3 .   ? -73.963  19.002 -57.901 1.00 31.80 ? 1027 HOH B O   1 
HETATM 4809 O O   . HOH J 3 .   ? -72.619  24.300 -58.310 1.00 42.41 ? 1028 HOH B O   1 
HETATM 4810 O O   . HOH J 3 .   ? -90.733  11.983 -75.296 1.00 36.87 ? 1029 HOH B O   1 
HETATM 4811 O O   . HOH J 3 .   ? -98.360  33.080 -65.998 1.00 24.79 ? 1030 HOH B O   1 
HETATM 4812 O O   . HOH J 3 .   ? -101.963 2.894  -72.463 1.00 43.39 ? 1031 HOH B O   1 
HETATM 4813 O O   . HOH J 3 .   ? -92.009  43.703 -52.994 1.00 44.93 ? 1032 HOH B O   1 
HETATM 4814 O O   . HOH J 3 .   ? -76.166  41.669 -59.503 1.00 45.66 ? 1033 HOH B O   1 
HETATM 4815 O O   . HOH J 3 .   ? -85.983  36.721 -48.138 1.00 31.47 ? 1034 HOH B O   1 
HETATM 4816 O O   . HOH J 3 .   ? -93.008  24.494 -58.540 1.00 44.33 ? 1035 HOH B O   1 
HETATM 4817 O O   . HOH J 3 .   ? -99.234  26.547 -60.947 1.00 35.01 ? 1036 HOH B O   1 
HETATM 4818 O O   . HOH J 3 .   ? -83.101  21.644 -66.625 1.00 42.99 ? 1037 HOH B O   1 
HETATM 4819 O O   . HOH J 3 .   ? -91.128  40.551 -53.873 1.00 34.79 ? 1038 HOH B O   1 
HETATM 4820 O O   . HOH J 3 .   ? -94.749  0.429  -54.118 1.00 38.92 ? 1039 HOH B O   1 
HETATM 4821 O O   . HOH J 3 .   ? -89.613  1.360  -50.126 1.00 42.85 ? 1040 HOH B O   1 
HETATM 4822 O O   . HOH J 3 .   ? -69.518  39.438 -65.606 1.00 33.82 ? 1041 HOH B O   1 
HETATM 4823 O O   . HOH J 3 .   ? -95.913  42.899 -57.577 1.00 35.69 ? 1042 HOH B O   1 
HETATM 4824 O O   . HOH J 3 .   ? -78.296  34.946 -81.645 1.00 44.49 ? 1043 HOH B O   1 
HETATM 4825 O O   . HOH J 3 .   ? -84.729  41.294 -82.061 1.00 48.38 ? 1044 HOH B O   1 
HETATM 4826 O O   . HOH J 3 .   ? -98.814  37.561 -69.468 1.00 43.69 ? 1045 HOH B O   1 
HETATM 4827 O O   . HOH J 3 .   ? -88.295  42.825 -65.444 1.00 42.14 ? 1046 HOH B O   1 
HETATM 4828 O O   . HOH J 3 .   ? -116.517 12.297 -71.555 1.00 41.36 ? 1047 HOH B O   1 
HETATM 4829 O O   . HOH J 3 .   ? -94.792  35.813 -42.217 1.00 46.36 ? 1048 HOH B O   1 
HETATM 4830 O O   . HOH J 3 .   ? -66.690  23.354 -76.420 1.00 42.28 ? 1049 HOH B O   1 
HETATM 4831 O O   . HOH J 3 .   ? -84.587  17.181 -68.806 1.00 28.37 ? 1050 HOH B O   1 
HETATM 4832 O O   . HOH J 3 .   ? -83.538  18.809 -61.587 1.00 40.32 ? 1051 HOH B O   1 
HETATM 4833 O O   . HOH J 3 .   ? -72.485  48.440 -72.363 1.00 36.11 ? 1052 HOH B O   1 
HETATM 4834 O O   . HOH J 3 .   ? -100.918 22.349 -65.950 1.00 32.25 ? 1053 HOH B O   1 
HETATM 4835 O O   . HOH J 3 .   ? -84.082  32.276 -82.524 1.00 41.35 ? 1054 HOH B O   1 
HETATM 4836 O O   . HOH J 3 .   ? -84.505  -1.150 -60.195 1.00 45.79 ? 1055 HOH B O   1 
HETATM 4837 O O   . HOH J 3 .   ? -80.307  21.819 -68.626 1.00 46.92 ? 1056 HOH B O   1 
HETATM 4838 O O   . HOH J 3 .   ? -65.141  30.065 -49.728 1.00 38.47 ? 1057 HOH B O   1 
HETATM 4839 O O   . HOH J 3 .   ? -85.348  22.673 -59.132 1.00 37.53 ? 1058 HOH B O   1 
HETATM 4840 O O   . HOH J 3 .   ? -96.237  40.039 -58.417 1.00 32.45 ? 1059 HOH B O   1 
HETATM 4841 O O   . HOH J 3 .   ? -105.905 5.174  -77.503 1.00 47.40 ? 1060 HOH B O   1 
HETATM 4842 O O   . HOH J 3 .   ? -91.951  13.115 -50.115 1.00 44.50 ? 1061 HOH B O   1 
HETATM 4843 O O   . HOH J 3 .   ? -70.568  27.974 -80.101 1.00 52.73 ? 1062 HOH B O   1 
HETATM 4844 O O   . HOH J 3 .   ? -112.779 4.360  -67.924 1.00 36.44 ? 1063 HOH B O   1 
HETATM 4845 O O   . HOH J 3 .   ? -99.790  -2.884 -64.524 1.00 42.42 ? 1064 HOH B O   1 
HETATM 4846 O O   . HOH J 3 .   ? -87.171  1.023  -69.966 1.00 47.86 ? 1065 HOH B O   1 
HETATM 4847 O O   . HOH J 3 .   ? -97.559  0.005  -53.695 1.00 39.34 ? 1066 HOH B O   1 
HETATM 4848 O O   . HOH J 3 .   ? -74.327  21.408 -76.010 1.00 44.11 ? 1067 HOH B O   1 
HETATM 4849 O O   . HOH J 3 .   ? -82.755  -0.280 -69.837 1.00 45.54 ? 1068 HOH B O   1 
HETATM 4850 O O   . HOH J 3 .   ? -74.365  27.033 -71.979 1.00 39.48 ? 1069 HOH B O   1 
HETATM 4851 O O   . HOH J 3 .   ? -83.482  19.069 -67.139 1.00 38.60 ? 1070 HOH B O   1 
HETATM 4852 O O   . HOH J 3 .   ? -109.537 10.339 -79.160 1.00 41.80 ? 1071 HOH B O   1 
HETATM 4853 O O   . HOH J 3 .   ? -101.418 19.944 -64.844 1.00 40.55 ? 1072 HOH B O   1 
HETATM 4854 O O   . HOH J 3 .   ? -89.940  21.954 -56.006 1.00 42.39 ? 1073 HOH B O   1 
HETATM 4855 O O   . HOH J 3 .   ? -99.295  3.735  -72.014 1.00 52.63 ? 1074 HOH B O   1 
HETATM 4856 O O   . HOH J 3 .   ? -99.662  17.687 -64.127 1.00 43.35 ? 1075 HOH B O   1 
HETATM 4857 O O   . HOH J 3 .   ? -107.276 21.011 -75.198 1.00 41.15 ? 1076 HOH B O   1 
HETATM 4858 O O   . HOH J 3 .   ? -104.614 20.043 -75.567 1.00 36.02 ? 1077 HOH B O   1 
HETATM 4859 O O   . HOH J 3 .   ? -81.554  45.724 -64.634 1.00 50.14 ? 1078 HOH B O   1 
HETATM 4860 O O   . HOH J 3 .   ? -93.634  15.996 -53.793 1.00 46.69 ? 1079 HOH B O   1 
HETATM 4861 O O   . HOH J 3 .   ? -90.914  44.679 -65.083 1.00 43.00 ? 1080 HOH B O   1 
HETATM 4862 O O   . HOH J 3 .   ? -96.106  33.885 -37.285 1.00 42.25 ? 1081 HOH B O   1 
HETATM 4863 O O   . HOH J 3 .   ? -100.301 31.196 -65.865 1.00 34.42 ? 1082 HOH B O   1 
HETATM 4864 O O   . HOH J 3 .   ? -119.438 10.639 -54.318 1.00 39.09 ? 1083 HOH B O   1 
HETATM 4865 O O   . HOH J 3 .   ? -70.967  25.542 -73.396 1.00 40.70 ? 1084 HOH B O   1 
HETATM 4866 O O   . HOH J 3 .   ? -74.803  22.847 -60.872 1.00 44.11 ? 1085 HOH B O   1 
HETATM 4867 O O   . HOH J 3 .   ? -78.824  43.233 -59.310 1.00 47.04 ? 1086 HOH B O   1 
HETATM 4868 O O   . HOH J 3 .   ? -80.910  43.913 -61.246 1.00 47.95 ? 1087 HOH B O   1 
HETATM 4869 O O   . HOH J 3 .   ? -94.863  0.450  -49.129 1.00 40.44 ? 1088 HOH B O   1 
HETATM 4870 O O   . HOH J 3 .   ? -81.018  44.796 -57.758 1.00 44.75 ? 1089 HOH B O   1 
HETATM 4871 O O   . HOH J 3 .   ? -75.203  37.013 -84.065 1.00 49.99 ? 1090 HOH B O   1 
HETATM 4872 O O   . HOH J 3 .   ? -101.285 24.328 -53.096 1.00 39.72 ? 1091 HOH B O   1 
HETATM 4873 O O   . HOH J 3 .   ? -101.654 25.175 -50.441 1.00 36.15 ? 1092 HOH B O   1 
HETATM 4874 O O   . HOH J 3 .   ? -99.338  21.175 -49.850 1.00 36.17 ? 1093 HOH B O   1 
HETATM 4875 O O   . HOH J 3 .   ? -97.373  23.010 -49.699 1.00 42.64 ? 1094 HOH B O   1 
HETATM 4876 O O   . HOH J 3 .   ? -105.661 2.667  -73.707 1.00 46.40 ? 1095 HOH B O   1 
HETATM 4877 O O   . HOH J 3 .   ? -103.887 -3.524 -67.717 1.00 47.37 ? 1096 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  CYS 41  41  41  CYS CYS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  MET 68  68  68  MET MET A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  CYS 91  91  91  CYS CYS A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 MET 115 115 115 MET MET A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 HIS 123 123 123 HIS HIS A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 MET 127 127 127 MET MET A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 MET 146 146 146 MET MET A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 TRP 162 162 162 TRP TRP A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 CYS 165 165 165 CYS CYS A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 LYS 197 197 ?   ?   ?   A . n 
A 1 198 LYS 198 198 ?   ?   ?   A . n 
A 1 199 ALA 199 199 ?   ?   ?   A . n 
A 1 200 ASN 200 200 ?   ?   ?   A . n 
A 1 201 GLU 201 201 ?   ?   ?   A . n 
A 1 202 VAL 202 202 ?   ?   ?   A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 MET 205 205 205 MET MET A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 MET 222 222 222 MET MET A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 CYS 226 226 226 CYS CYS A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 CYS 230 230 230 CYS CYS A . n 
A 1 231 HIS 231 231 231 HIS HIS A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 VAL 271 271 271 VAL VAL A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 PRO 276 276 276 PRO PRO A . n 
A 1 277 GLN 277 277 277 GLN GLN A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 MET 281 281 281 MET MET A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 CYS 284 284 284 CYS CYS A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 LYS 286 286 286 LYS LYS A . n 
A 1 287 ILE 287 287 287 ILE ILE A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 MET 294 294 294 MET MET A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 ILE 300 300 300 ILE ILE A . n 
A 1 301 ARG 301 301 301 ARG ARG A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 ASN 305 305 305 ASN ASN A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 PHE 313 313 313 PHE PHE A . n 
A 1 314 SER 314 314 ?   ?   ?   A . n 
A 1 315 HIS 315 315 ?   ?   ?   A . n 
A 1 316 VAL 316 316 ?   ?   ?   A . n 
A 1 317 PRO 317 317 ?   ?   ?   A . n 
A 1 318 LEU 318 318 ?   ?   ?   A . n 
A 1 319 LEU 319 319 ?   ?   ?   A . n 
A 1 320 GLU 320 320 ?   ?   ?   A . n 
A 1 321 HIS 321 321 ?   ?   ?   A . n 
A 1 322 HIS 322 322 ?   ?   ?   A . n 
A 1 323 HIS 323 323 ?   ?   ?   A . n 
A 1 324 HIS 324 324 ?   ?   ?   A . n 
A 1 325 HIS 325 325 ?   ?   ?   A . n 
A 1 326 HIS 326 326 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   ASN 3   3   3   ASN ASN B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  SER 11  11  11  SER SER B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  GLN 13  13  13  GLN GLN B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  GLN 17  17  17  GLN GLN B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  LYS 33  33  33  LYS LYS B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  PHE 35  35  35  PHE PHE B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  CYS 41  41  41  CYS CYS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  CYS 60  60  60  CYS CYS B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  MET 68  68  68  MET MET B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ILE 72  72  72  ILE ILE B . n 
B 1 73  MET 73  73  73  MET MET B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  CYS 77  77  77  CYS CYS B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  PRO 90  90  90  PRO PRO B . n 
B 1 91  CYS 91  91  91  CYS CYS B . n 
B 1 92  PHE 92  92  92  PHE PHE B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  GLN 97  97  97  GLN GLN B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ASN 114 114 114 ASN ASN B . n 
B 1 115 MET 115 115 115 MET MET B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 HIS 123 123 123 HIS HIS B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 THR 126 126 126 THR THR B . n 
B 1 127 MET 127 127 127 MET MET B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 HIS 130 130 130 HIS HIS B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 SER 132 132 132 SER SER B . n 
B 1 133 GLN 133 133 133 GLN GLN B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 PHE 137 137 137 PHE PHE B . n 
B 1 138 PHE 138 138 138 PHE PHE B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 ILE 140 140 140 ILE ILE B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 MET 146 146 146 MET MET 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 5    HOH TIP A . 
I 3 HOH 2  1008 7    HOH TIP A . 
I 3 HOH 3  1009 9    HOH TIP A . 
I 3 HOH 4  1010 16   HOH TIP A . 
I 3 HOH 5  1011 18   HOH TIP A . 
I 3 HOH 6  1012 19   HOH TIP A . 
I 3 HOH 7  1013 22   HOH TIP A . 
I 3 HOH 8  1014 24   HOH TIP A . 
I 3 HOH 9  1015 26   HOH TIP A . 
I 3 HOH 10 1016 28   HOH TIP A . 
I 3 HOH 11 1017 29   HOH TIP A . 
I 3 HOH 12 1018 30   HOH TIP A . 
I 3 HOH 13 1019 31   HOH TIP A . 
I 3 HOH 14 1020 32   HOH TIP A . 
I 3 HOH 15 1021 34   HOH TIP A . 
I 3 HOH 16 1022 37   HOH TIP A . 
I 3 HOH 17 1023 38   HOH TIP A . 
I 3 HOH 18 1024 39   HOH TIP A . 
I 3 HOH 19 1025 41   HOH TIP A . 
I 3 HOH 20 1026 44   HOH TIP A . 
I 3 HOH 21 1027 47   HOH TIP A . 
I 3 HOH 22 1028 48   HOH TIP A . 
I 3 HOH 23 1029 49   HOH TIP A . 
I 3 HOH 24 1030 50   HOH TIP A . 
I 3 HOH 25 1031 53   HOH TIP A . 
I 3 HOH 26 1032 55   HOH TIP A . 
I 3 HOH 27 1033 57   HOH TIP A . 
I 3 HOH 28 1034 61   HOH TIP A . 
I 3 HOH 29 1035 63   HOH TIP A . 
I 3 HOH 30 1036 66   HOH TIP A . 
I 3 HOH 31 1037 67   HOH TIP A . 
I 3 HOH 32 1038 71   HOH TIP A . 
I 3 HOH 33 1039 78   HOH TIP A . 
I 3 HOH 34 1040 81   HOH TIP A . 
I 3 HOH 35 1041 82   HOH TIP A . 
I 3 HOH 36 1042 84   HOH TIP A . 
I 3 HOH 37 1043 87   HOH TIP A . 
I 3 HOH 38 1044 90   HOH TIP A . 
I 3 HOH 39 1045 92   HOH TIP A . 
I 3 HOH 40 1046 98   HOH TIP A . 
I 3 HOH 41 1047 100  HOH TIP A . 
I 3 HOH 42 1048 102  HOH TIP A . 
I 3 HOH 43 1049 106  HOH TIP A . 
I 3 HOH 44 1050 110  HOH TIP A . 
I 3 HOH 45 1051 112  HOH TIP A . 
I 3 HOH 46 1052 113  HOH TIP A . 
I 3 HOH 47 1053 118  HOH TIP A . 
I 3 HOH 48 1054 119  HOH TIP A . 
I 3 HOH 49 1055 120  HOH TIP A . 
I 3 HOH 50 1056 121  HOH TIP A . 
I 3 HOH 51 1057 122  HOH TIP A . 
I 3 HOH 52 1058 123  HOH TIP A . 
I 3 HOH 53 1059 124  HOH TIP A . 
I 3 HOH 54 1060 126  HOH TIP A . 
I 3 HOH 55 1061 130  HOH TIP A . 
I 3 HOH 56 1062 132  HOH TIP A . 
I 3 HOH 57 1063 133  HOH TIP A . 
I 3 HOH 58 1064 135  HOH TIP A . 
I 3 HOH 59 1065 136  HOH TIP A . 
I 3 HOH 60 1066 137  HOH TIP A . 
I 3 HOH 61 1067 138  HOH TIP A . 
I 3 HOH 62 1068 139  HOH TIP A . 
I 3 HOH 63 1069 140  HOH TIP A . 
I 3 HOH 64 1070 141  HOH TIP A . 
I 3 HOH 65 1071 143  HOH TIP A . 
I 3 HOH 66 1072 144  HOH TIP A . 
I 3 HOH 67 1073 145  HOH TIP A . 
I 3 HOH 68 1074 146  HOH TIP A . 
I 3 HOH 69 1075 147  HOH TIP A . 
I 3 HOH 70 1076 148  HOH TIP A . 
I 3 HOH 71 1077 155  HOH TIP A . 
I 3 HOH 72 1078 161  HOH TIP A . 
I 3 HOH 73 1079 164  HOH TIP A . 
J 3 HOH 1  1006 1    HOH TIP B . 
J 3 HOH 2  1007 2    HOH TIP B . 
J 3 HOH 3  1008 3    HOH TIP B . 
J 3 HOH 4  1009 4    HOH TIP B . 
J 3 HOH 5  1010 6    HOH TIP B . 
J 3 HOH 6  1011 8    HOH TIP B . 
J 3 HOH 7  1012 10   HOH TIP B . 
J 3 HOH 8  1013 11   HOH TIP B . 
J 3 HOH 9  1014 12   HOH TIP B . 
J 3 HOH 10 1015 13   HOH TIP B . 
J 3 HOH 11 1016 14   HOH TIP B . 
J 3 HOH 12 1017 15   HOH TIP B . 
J 3 HOH 13 1018 17   HOH TIP B . 
J 3 HOH 14 1019 20   HOH TIP B . 
J 3 HOH 15 1020 21   HOH TIP B . 
J 3 HOH 16 1021 23   HOH TIP B . 
J 3 HOH 17 1022 25   HOH TIP B . 
J 3 HOH 18 1023 27   HOH TIP B . 
J 3 HOH 19 1024 33   HOH TIP B . 
J 3 HOH 20 1025 35   HOH TIP B . 
J 3 HOH 21 1026 36   HOH TIP B . 
J 3 HOH 22 1027 40   HOH TIP B . 
J 3 HOH 23 1028 42   HOH TIP B . 
J 3 HOH 24 1029 43   HOH TIP B . 
J 3 HOH 25 1030 45   HOH TIP B . 
J 3 HOH 26 1031 46   HOH TIP B . 
J 3 HOH 27 1032 51   HOH TIP B . 
J 3 HOH 28 1033 52   HOH TIP B . 
J 3 HOH 29 1034 54   HOH TIP B . 
J 3 HOH 30 1035 56   HOH TIP B . 
J 3 HOH 31 1036 58   HOH TIP B . 
J 3 HOH 32 1037 59   HOH TIP B . 
J 3 HOH 33 1038 60   HOH TIP B . 
J 3 HOH 34 1039 62   HOH TIP B . 
J 3 HOH 35 1040 64   HOH TIP B . 
J 3 HOH 36 1041 65   HOH TIP B . 
J 3 HOH 37 1042 68   HOH TIP B . 
J 3 HOH 38 1043 69   HOH TIP B . 
J 3 HOH 39 1044 70   HOH TIP B . 
J 3 HOH 40 1045 72   HOH TIP B . 
J 3 HOH 41 1046 73   HOH TIP B . 
J 3 HOH 42 1047 74   HOH TIP B . 
J 3 HOH 43 1048 75   HOH TIP B . 
J 3 HOH 44 1049 76   HOH TIP B . 
J 3 HOH 45 1050 77   HOH TIP B . 
J 3 HOH 46 1051 79   HOH TIP B . 
J 3 HOH 47 1052 80   HOH TIP B . 
J 3 HOH 48 1053 83   HOH TIP B . 
J 3 HOH 49 1054 85   HOH TIP B . 
J 3 HOH 50 1055 86   HOH TIP B . 
J 3 HOH 51 1056 88   HOH TIP B . 
J 3 HOH 52 1057 89   HOH TIP B . 
J 3 HOH 53 1058 91   HOH TIP B . 
J 3 HOH 54 1059 93   HOH TIP B . 
J 3 HOH 55 1060 94   HOH TIP B . 
J 3 HOH 56 1061 95   HOH TIP B . 
J 3 HOH 57 1062 96   HOH TIP B . 
J 3 HOH 58 1063 97   HOH TIP B . 
J 3 HOH 59 1064 99   HOH TIP B . 
J 3 HOH 60 1065 101  HOH TIP B . 
J 3 HOH 61 1066 103  HOH TIP B . 
J 3 HOH 62 1067 104  HOH TIP B . 
J 3 HOH 63 1068 105  HOH TIP B . 
J 3 HOH 64 1069 107  HOH TIP B . 
J 3 HOH 65 1070 108  HOH TIP B . 
J 3 HOH 66 1071 109  HOH TIP B . 
J 3 HOH 67 1072 111  HOH TIP B . 
J 3 HOH 68 1073 114  HOH TIP B . 
J 3 HOH 69 1074 115  HOH TIP B . 
J 3 HOH 70 1075 116  HOH TIP B . 
J 3 HOH 71 1076 117  HOH TIP B . 
J 3 HOH 72 1077 125  HOH TIP B . 
J 3 HOH 73 1078 127  HOH TIP B . 
J 3 HOH 74 1079 128  HOH TIP B . 
J 3 HOH 75 1080 129  HOH TIP B . 
J 3 HOH 76 1081 131  HOH TIP B . 
J 3 HOH 77 1082 134  HOH TIP B . 
J 3 HOH 78 1083 142  HOH TIP B . 
J 3 HOH 79 1084 149  HOH TIP B . 
J 3 HOH 80 1085 150  HOH TIP B . 
J 3 HOH 81 1086 151  HOH TIP B . 
J 3 HOH 82 1087 152  HOH TIP B . 
J 3 HOH 83 1088 153  HOH TIP B . 
J 3 HOH 84 1089 154  HOH TIP B . 
J 3 HOH 85 1090 156  HOH TIP B . 
J 3 HOH 86 1091 157  HOH TIP B . 
J 3 HOH 87 1092 158  HOH TIP B . 
J 3 HOH 88 1093 159  HOH TIP B . 
J 3 HOH 89 1094 160  HOH TIP B . 
J 3 HOH 90 1095 162  HOH TIP B . 
J 3 HOH 91 1096 163  HOH TIP 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)' 28920 ? 
1 MORE         -445  ? 
1 'SSA (A^2)'  59790 ? 
# 
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 -84.9570000000  0.8660254038  
-0.5000000000 0.0000000000 147.1498404586 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 -169.9140000000 -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 
ADSC     'data collection' .   ? 2 
HKL-2000 'data scaling'    .   ? 3 
CNS      phasing           .   ? 4 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 171 ? ? CG A ASP 171 ? ? OD2 A ASP 171 ? ? 123.96 118.30 5.66 0.90 N 
2 1 CB B ASP 210 ? ? CG B ASP 210 ? ? OD2 B ASP 210 ? ? 123.89 118.30 5.59 0.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 10  ? ? 51.76   -170.57 
2  1 PHE A 35  ? ? -84.63  -152.35 
3  1 SER A 36  ? ? -47.77  -85.85  
4  1 ASN A 37  ? ? -100.32 44.13   
5  1 GLN A 57  ? ? -44.79  156.24  
6  1 GLU A 62  ? ? -49.43  94.38   
7  1 ASP A 224 ? ? -90.27  -92.93  
8  1 SER A 254 ? ? -103.29 -166.13 
9  1 ASN A 273 ? ? -64.12  1.68    
10 1 SER B 10  ? ? -108.01 -166.11 
11 1 SER B 11  ? ? -63.78  11.33   
12 1 HIS B 12  ? ? -90.93  54.87   
13 1 ASP B 14  ? ? 9.96    -89.57  
14 1 ASP B 224 ? ? -102.67 -100.05 
15 1 CYS B 265 ? ? -89.71  35.73   
16 1 ASN B 273 ? ? -93.96  43.92   
17 1 SER B 314 ? ? -153.69 26.51   
# 
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 
# 
