data_3EFH
# 
_entry.id   3EFH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3EFH         
RCSB  RCSB049257   
WWPDB D_1000049257 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3EFH 
_pdbx_database_status.recvd_initial_deposition_date   2008-09-08 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, X.'   1 ? 
'Peng, X.' 2 ? 
'Li, Y.'   3 ? 
# 
_citation.id                        primary 
_citation.title                     'Crystal structure of human phosphoribosyl pyrophosphate synthetase 1' 
_citation.journal_abbrev            'To be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Peng, X.' 1 
primary 'Li, X.'   2 
# 
_cell.entry_id           3EFH 
_cell.length_a           169.180 
_cell.length_b           169.180 
_cell.length_c           61.840 
_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                         3EFH 
_symmetry.space_group_name_H-M             'H 3' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Ribose-phosphate pyrophosphokinase 1' 35950.375 2   2.7.6.1 ? ? ? 
2 non-polymer syn 'SULFATE ION'                          96.063    6   ?       ? ? ? 
3 water       nat water                                  18.015    108 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Phosphoribosyl pyrophosphate synthetase I, PRS-I, PPRibP' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   ASN n 
1 4   ILE n 
1 5   LYS n 
1 6   ILE n 
1 7   PHE n 
1 8   SER n 
1 9   GLY n 
1 10  SER n 
1 11  SER n 
1 12  HIS n 
1 13  GLN n 
1 14  ASP n 
1 15  LEU n 
1 16  SER n 
1 17  GLN n 
1 18  LYS n 
1 19  ILE n 
1 20  ALA n 
1 21  ASP n 
1 22  ARG n 
1 23  LEU n 
1 24  GLY n 
1 25  LEU n 
1 26  GLU n 
1 27  LEU n 
1 28  GLY n 
1 29  LYS n 
1 30  VAL n 
1 31  VAL n 
1 32  THR n 
1 33  LYS n 
1 34  LYS n 
1 35  PHE n 
1 36  SER n 
1 37  ASN n 
1 38  GLN n 
1 39  GLU n 
1 40  THR n 
1 41  CYS n 
1 42  VAL n 
1 43  GLU n 
1 44  ILE n 
1 45  GLY n 
1 46  GLU n 
1 47  SER n 
1 48  VAL n 
1 49  ARG n 
1 50  GLY n 
1 51  GLU n 
1 52  ASP n 
1 53  VAL n 
1 54  TYR n 
1 55  ILE n 
1 56  VAL n 
1 57  GLN n 
1 58  SER n 
1 59  GLY n 
1 60  CYS n 
1 61  GLY n 
1 62  GLU n 
1 63  ILE n 
1 64  ASN n 
1 65  ASP n 
1 66  ASN n 
1 67  LEU n 
1 68  MET n 
1 69  GLU n 
1 70  LEU n 
1 71  LEU n 
1 72  ILE n 
1 73  MET n 
1 74  ILE n 
1 75  ASN n 
1 76  ALA n 
1 77  CYS n 
1 78  LYS n 
1 79  ILE n 
1 80  ALA n 
1 81  SER n 
1 82  ALA n 
1 83  SER n 
1 84  ARG n 
1 85  VAL n 
1 86  THR n 
1 87  ALA n 
1 88  VAL n 
1 89  ILE n 
1 90  PRO n 
1 91  CYS n 
1 92  PHE n 
1 93  PRO n 
1 94  TYR n 
1 95  ALA n 
1 96  ARG n 
1 97  GLN n 
1 98  ASP n 
1 99  LYS n 
1 100 LYS n 
1 101 ASP n 
1 102 LYS n 
1 103 SER n 
1 104 ARG n 
1 105 ALA n 
1 106 PRO n 
1 107 ILE n 
1 108 SER n 
1 109 ALA n 
1 110 LYS n 
1 111 LEU n 
1 112 VAL n 
1 113 ALA n 
1 114 ASN n 
1 115 MET n 
1 116 LEU n 
1 117 SER n 
1 118 VAL n 
1 119 ALA n 
1 120 GLY n 
1 121 ALA n 
1 122 ASP n 
1 123 HIS n 
1 124 ILE n 
1 125 ILE n 
1 126 THR n 
1 127 MET n 
1 128 ASP n 
1 129 LEU n 
1 130 HIS n 
1 131 ALA n 
1 132 SER n 
1 133 GLN n 
1 134 ILE n 
1 135 GLN n 
1 136 GLY n 
1 137 PHE n 
1 138 PHE n 
1 139 ASP n 
1 140 ILE n 
1 141 PRO n 
1 142 VAL n 
1 143 ASP n 
1 144 ASN n 
1 145 LEU n 
1 146 TYR n 
1 147 ALA n 
1 148 GLU n 
1 149 PRO n 
1 150 ALA n 
1 151 VAL n 
1 152 LEU n 
1 153 LYS n 
1 154 TRP n 
1 155 ILE n 
1 156 ARG n 
1 157 GLU n 
1 158 ASN n 
1 159 ILE n 
1 160 SER n 
1 161 GLU n 
1 162 TRP n 
1 163 ARG n 
1 164 ASN n 
1 165 CYS n 
1 166 THR n 
1 167 ILE n 
1 168 VAL n 
1 169 SER n 
1 170 PRO n 
1 171 ASP n 
1 172 ALA n 
1 173 GLY n 
1 174 GLY n 
1 175 ALA n 
1 176 LYS n 
1 177 ARG n 
1 178 VAL n 
1 179 THR n 
1 180 SER n 
1 181 ILE n 
1 182 ALA n 
1 183 ASP n 
1 184 ARG n 
1 185 LEU n 
1 186 ASN n 
1 187 VAL n 
1 188 ASP n 
1 189 PHE n 
1 190 ALA n 
1 191 LEU n 
1 192 ILE n 
1 193 HIS n 
1 194 LYS n 
1 195 GLU n 
1 196 ARG n 
1 197 LYS n 
1 198 LYS n 
1 199 ALA n 
1 200 ASN n 
1 201 GLU n 
1 202 VAL n 
1 203 ASP n 
1 204 ARG n 
1 205 MET n 
1 206 VAL n 
1 207 LEU n 
1 208 VAL n 
1 209 GLY n 
1 210 ASP n 
1 211 VAL n 
1 212 LYS n 
1 213 ASP n 
1 214 ARG n 
1 215 VAL n 
1 216 ALA n 
1 217 ILE n 
1 218 LEU n 
1 219 VAL n 
1 220 ASP n 
1 221 ASP n 
1 222 MET n 
1 223 ALA n 
1 224 ASP n 
1 225 THR n 
1 226 CYS n 
1 227 GLY n 
1 228 THR n 
1 229 ILE n 
1 230 CYS n 
1 231 HIS n 
1 232 ALA n 
1 233 ALA n 
1 234 ASP n 
1 235 LYS n 
1 236 LEU n 
1 237 LEU n 
1 238 SER n 
1 239 ALA n 
1 240 GLY n 
1 241 ALA n 
1 242 THR n 
1 243 ARG n 
1 244 VAL n 
1 245 TYR n 
1 246 ALA n 
1 247 ILE n 
1 248 LEU n 
1 249 THR n 
1 250 HIS n 
1 251 GLY n 
1 252 ILE n 
1 253 PHE n 
1 254 SER n 
1 255 GLY n 
1 256 PRO n 
1 257 ALA n 
1 258 ILE n 
1 259 SER n 
1 260 ARG n 
1 261 ILE n 
1 262 ASN n 
1 263 ASN n 
1 264 ALA n 
1 265 CYS n 
1 266 PHE n 
1 267 GLU n 
1 268 ALA n 
1 269 VAL n 
1 270 VAL n 
1 271 VAL n 
1 272 THR n 
1 273 ASN n 
1 274 THR n 
1 275 ILE n 
1 276 PRO n 
1 277 GLN n 
1 278 GLU n 
1 279 ASP n 
1 280 LYS n 
1 281 MET n 
1 282 LYS n 
1 283 HIS n 
1 284 CYS n 
1 285 SER n 
1 286 LYS n 
1 287 ILE n 
1 288 GLN n 
1 289 VAL n 
1 290 ILE n 
1 291 ASP n 
1 292 ILE n 
1 293 SER n 
1 294 MET n 
1 295 ILE n 
1 296 LEU n 
1 297 ALA n 
1 298 GLU n 
1 299 ALA n 
1 300 ILE n 
1 301 ARG n 
1 302 ARG n 
1 303 THR n 
1 304 HIS n 
1 305 ASN n 
1 306 GLY n 
1 307 GLU n 
1 308 SER n 
1 309 VAL n 
1 310 SER n 
1 311 TYR n 
1 312 LEU n 
1 313 PHE n 
1 314 SER n 
1 315 HIS n 
1 316 VAL n 
1 317 PRO n 
1 318 LEU n 
1 319 LEU n 
1 320 GLU n 
1 321 HIS n 
1 322 HIS n 
1 323 HIS n 
1 324 HIS n 
1 325 HIS n 
1 326 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PRPS1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(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 3EFH A 1 ? 318 ? P60891 1 ? 318 ? 1 318 
2 1 3EFH 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 3EFH LEU A 319 ? UNP P60891 ? ? 'EXPRESSION TAG' 319 1  
1 3EFH GLU A 320 ? UNP P60891 ? ? 'EXPRESSION TAG' 320 2  
1 3EFH HIS A 321 ? UNP P60891 ? ? 'EXPRESSION TAG' 321 3  
1 3EFH HIS A 322 ? UNP P60891 ? ? 'EXPRESSION TAG' 322 4  
1 3EFH HIS A 323 ? UNP P60891 ? ? 'EXPRESSION TAG' 323 5  
1 3EFH HIS A 324 ? UNP P60891 ? ? 'EXPRESSION TAG' 324 6  
1 3EFH HIS A 325 ? UNP P60891 ? ? 'EXPRESSION TAG' 325 7  
1 3EFH HIS A 326 ? UNP P60891 ? ? 'EXPRESSION TAG' 326 8  
2 3EFH LEU B 319 ? UNP P60891 ? ? 'EXPRESSION TAG' 319 9  
2 3EFH GLU B 320 ? UNP P60891 ? ? 'EXPRESSION TAG' 320 10 
2 3EFH HIS B 321 ? UNP P60891 ? ? 'EXPRESSION TAG' 321 11 
2 3EFH HIS B 322 ? UNP P60891 ? ? 'EXPRESSION TAG' 322 12 
2 3EFH HIS B 323 ? UNP P60891 ? ? 'EXPRESSION TAG' 323 13 
2 3EFH HIS B 324 ? UNP P60891 ? ? 'EXPRESSION TAG' 324 14 
2 3EFH HIS B 325 ? UNP P60891 ? ? 'EXPRESSION TAG' 325 15 
2 3EFH HIS B 326 ? UNP P60891 ? ? 'EXPRESSION TAG' 326 16 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3EFH 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.44 
_exptl_crystal.density_percent_sol   49.62 
_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            295 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.3 
_exptl_crystal_grow.pdbx_details    
'2.1M ammonium sulfate, 0.1M sodium acetate, 10% (v/v) glycerol, pH 4.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR scanner 345 mm plate' 
_diffrn_detector.pdbx_collection_date   2005-11-18 
_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   1.54179 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU MICROMAX-007' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.54179 
# 
_reflns.entry_id                     3EFH 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             42.295 
_reflns.d_resolution_high            2.6 
_reflns.number_obs                   18518 
_reflns.number_all                   18873 
_reflns.percent_possible_obs         91.2 
_reflns.pdbx_Rmerge_I_obs            0.065 
_reflns.pdbx_Rsym_value              0.065 
_reflns.pdbx_netI_over_sigmaI        8.5 
_reflns.B_iso_Wilson_estimate        50.4 
_reflns.pdbx_redundancy              1.4 
_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_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.60 
_reflns_shell.d_res_low              2.74 
_reflns_shell.percent_possible_all   88.5 
_reflns_shell.Rmerge_I_obs           0.345 
_reflns_shell.pdbx_Rsym_value        0.345 
_reflns_shell.meanI_over_sigI_obs    1.8 
_reflns_shell.pdbx_redundancy        1.4 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      2623 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3EFH 
_refine.ls_number_reflns_obs                     17561 
_refine.ls_number_reflns_all                     18508 
_refine.pdbx_ls_sigma_I                          0 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             30.00 
_refine.ls_d_res_high                            2.60 
_refine.ls_percent_reflns_obs                    91.19 
_refine.ls_R_factor_obs                          0.21649 
_refine.ls_R_factor_all                          0.21649 
_refine.ls_R_factor_R_work                       0.21570 
_refine.ls_R_factor_R_free                       0.23133 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  947 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.916 
_refine.correlation_coeff_Fo_to_Fc_free          0.910 
_refine.B_iso_mean                               33.116 
_refine.aniso_B[1][1]                            0.79 
_refine.aniso_B[2][2]                            0.79 
_refine.aniso_B[3][3]                            -1.18 
_refine.aniso_B[1][2]                            0.39 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      'PDB ENTRY 2HCR' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.328 
_refine.overall_SU_ML                            0.184 
_refine.overall_SU_B                             8.566 
_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_overall_phase_error                 ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4592 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             108 
_refine_hist.number_atoms_total               4730 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        30.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.008  0.022  ? 4680 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.080  1.957  ? 6352 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       5.119  5.000  ? 610  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       38.551 24.632 ? 190  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       18.781 15.000 ? 790  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       12.884 15.000 ? 28   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.071  0.200  ? 764  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.003  0.020  ? 3442 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.219  0.200  ? 2203 'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.304  0.200  ? 3169 'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.164  0.200  ? 247  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.221  0.200  ? 88   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.218  0.200  ? 14   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.490  1.500  ? 3146 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 0.649  2.000  ? 4902 'X-RAY DIFFRACTION' ? 
r_scbond_it                  0.826  3.000  ? 1703 'X-RAY DIFFRACTION' ? 
r_scangle_it                 1.243  4.500  ? 1450 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.600 
_refine_ls_shell.d_res_low                        2.667 
_refine_ls_shell.number_reflns_R_work             1265 
_refine_ls_shell.R_factor_R_work                  0.302 
_refine_ls_shell.percent_reflns_obs               88.04 
_refine_ls_shell.R_factor_R_free                  0.326 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             60 
_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' 
# 
_struct.entry_id                  3EFH 
_struct.title                     'Crystal structure of human phosphoribosyl pyrophosphate synthetase 1' 
_struct.pdbx_descriptor           'Ribose-phosphate pyrophosphokinase 1 (E.C.2.7.6.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3EFH 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            
;TRANSFERASE, Charcot-Marie-Tooth disease, Deafness, Disease mutation, Gout, Kinase, Magnesium, Metal-binding, Nucleotide biosynthesis, Polymorphism
;
# 
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 ? 
# 
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 ? ALA A 119 ? ILE A 107 ALA A 119 1 ? 13 
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  GLY A 174 ? LEU A 185 ? GLY A 174 LEU A 185 1 ? 12 
HELX_P HELX_P8  8  CYS A 226 ? ALA A 239 ? CYS A 226 ALA A 239 1 ? 14 
HELX_P HELX_P9  9  PRO A 256 ? ALA A 264 ? PRO A 256 ALA A 264 1 ? 9  
HELX_P HELX_P10 10 GLN A 277 ? CYS A 284 ? GLN A 277 CYS A 284 1 ? 8  
HELX_P HELX_P11 11 ILE A 292 ? GLY A 306 ? ILE A 292 GLY A 306 1 ? 15 
HELX_P HELX_P12 12 SER A 308 ? SER A 314 ? SER A 308 SER A 314 5 ? 7  
HELX_P HELX_P13 13 GLN B 13  ? LEU B 23  ? GLN B 13  LEU B 23  1 ? 11 
HELX_P HELX_P14 14 GLU B 62  ? ALA B 80  ? GLU B 62  ALA B 80  1 ? 19 
HELX_P HELX_P15 15 ILE B 107 ? GLY B 120 ? ILE B 107 GLY B 120 1 ? 14 
HELX_P HELX_P16 16 ALA B 131 ? PHE B 138 ? ALA B 131 PHE B 138 5 ? 8  
HELX_P HELX_P17 17 ALA B 147 ? ILE B 159 ? ALA B 147 ILE B 159 1 ? 13 
HELX_P HELX_P18 18 GLU B 161 ? ASN B 164 ? GLU B 161 ASN B 164 5 ? 4  
HELX_P HELX_P19 19 ASP B 171 ? GLY B 173 ? ASP B 171 GLY B 173 5 ? 3  
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  ? LYS A 34  ? VAL A 30  LYS A 34  
B 2 THR A 40  ? ILE A 44  ? THR A 40  ILE A 44  
C 1 VAL A 206 ? VAL A 208 ? VAL A 206 VAL A 208 
C 2 ASP A 188 ? HIS A 193 ? ASP A 188 HIS A 193 
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 VAL B 206 ? VAL B 208 ? VAL B 206 VAL B 208 
F 2 ASP B 188 ? HIS B 193 ? ASP B 188 HIS B 193 
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 VAL B 269 ? THR B 272 ? VAL B 269 THR B 272 
F 7 ILE B 287 ? ILE B 290 ? ILE B 287 ILE B 290 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N PHE A 7   ? N PHE A 7   O VAL A 56  ? O VAL A 56  
A 2 3 N ILE A 55  ? N ILE A 55  O VAL A 88  ? O VAL A 88  
A 3 4 N ALA A 87  ? N ALA A 87  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 LYS A 33  ? N LYS A 33  O CYS A 41  ? O CYS A 41  
C 1 2 O VAL A 208 ? O VAL A 208 N LEU A 191 ? N LEU A 191 
C 2 3 O ASP A 188 ? O ASP A 188 N ILE A 167 ? N ILE A 167 
C 3 4 N VAL A 168 ? N VAL A 168 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 THR B 86  ? O THR B 86  
D 3 4 N ALA B 87  ? N ALA B 87  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 LYS B 33  ? N LYS B 33  O CYS B 41  ? O CYS B 41  
F 1 2 O VAL B 206 ? O VAL B 206 N HIS B 193 ? N HIS B 193 
F 2 3 O ALA B 190 ? O ALA B 190 N SER B 169 ? N SER B 169 
F 3 4 N VAL B 168 ? N VAL B 168 O ILE B 217 ? O ILE B 217 
F 4 5 N LEU B 218 ? N LEU B 218 O ILE B 247 ? O ILE B 247 
F 5 6 N ALA B 246 ? N ALA B 246 O VAL B 270 ? O VAL B 270 
F 6 7 N VAL B 271 ? N VAL B 271 O ILE B 290 ? O ILE B 290 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 A 327' 
AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 A 328' 
AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 A 329' 
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 B 327' 
AC5 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 B 328' 
AC6 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 B 329' 
# 
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 A 224 ? ASP A 224 . ? 1_555 ? 
2  AC1 6 THR A 225 ? THR A 225 . ? 1_555 ? 
3  AC1 6 CYS A 226 ? CYS A 226 . ? 1_555 ? 
4  AC1 6 GLY A 227 ? GLY A 227 . ? 1_555 ? 
5  AC1 6 THR A 228 ? THR A 228 . ? 1_555 ? 
6  AC1 6 HOH I .   ? HOH A 382 . ? 1_555 ? 
7  AC2 7 SER A 47  ? SER A 47  . ? 1_555 ? 
8  AC2 7 ARG A 49  ? ARG A 49  . ? 1_555 ? 
9  AC2 7 SER A 308 ? SER A 308 . ? 2_555 ? 
10 AC2 7 VAL A 309 ? VAL A 309 . ? 2_555 ? 
11 AC2 7 SER A 310 ? SER A 310 . ? 2_555 ? 
12 AC2 7 HOH I .   ? HOH A 343 . ? 1_555 ? 
13 AC2 7 ARG B 104 ? ARG B 104 . ? 1_555 ? 
14 AC3 7 SER A 132 ? SER A 132 . ? 1_555 ? 
15 AC3 7 GLN A 135 ? GLN A 135 . ? 1_555 ? 
16 AC3 7 ASN A 144 ? ASN A 144 . ? 1_555 ? 
17 AC3 7 TYR A 146 ? TYR A 146 . ? 1_555 ? 
18 AC3 7 LYS B 100 ? LYS B 100 . ? 3_555 ? 
19 AC3 7 ASP B 101 ? ASP B 101 . ? 3_555 ? 
20 AC3 7 LYS B 102 ? LYS B 102 . ? 3_555 ? 
21 AC4 4 ASP B 224 ? ASP B 224 . ? 1_555 ? 
22 AC4 4 THR B 225 ? THR B 225 . ? 1_555 ? 
23 AC4 4 CYS B 226 ? CYS B 226 . ? 1_555 ? 
24 AC4 4 THR B 228 ? THR B 228 . ? 1_555 ? 
25 AC5 7 ARG A 104 ? ARG A 104 . ? 1_555 ? 
26 AC5 7 SER B 47  ? SER B 47  . ? 1_555 ? 
27 AC5 7 ARG B 49  ? ARG B 49  . ? 1_555 ? 
28 AC5 7 SER B 308 ? SER B 308 . ? 3_555 ? 
29 AC5 7 VAL B 309 ? VAL B 309 . ? 3_555 ? 
30 AC5 7 SER B 310 ? SER B 310 . ? 3_555 ? 
31 AC5 7 HOH J .   ? HOH B 334 . ? 1_555 ? 
32 AC6 8 LYS A 100 ? LYS A 100 . ? 2_555 ? 
33 AC6 8 ASP A 101 ? ASP A 101 . ? 2_555 ? 
34 AC6 8 LYS A 102 ? LYS A 102 . ? 2_555 ? 
35 AC6 8 SER B 132 ? SER B 132 . ? 1_555 ? 
36 AC6 8 GLN B 135 ? GLN B 135 . ? 1_555 ? 
37 AC6 8 ASN B 144 ? ASN B 144 . ? 1_555 ? 
38 AC6 8 TYR B 146 ? TYR B 146 . ? 1_555 ? 
39 AC6 8 HOH J .   ? HOH B 335 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3EFH 
_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                    3EFH 
_atom_sites.fract_transf_matrix[1][1]   0.005911 
_atom_sites.fract_transf_matrix[1][2]   0.003413 
_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]   0.006825 
_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]   0.016171 
_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   ? 9.142   -8.030  -59.625 1.00 35.11 ? 3   ASN A N   1 
ATOM   2    C CA  . ASN A 1 3   ? 8.346   -7.510  -58.474 1.00 35.16 ? 3   ASN A CA  1 
ATOM   3    C C   . ASN A 1 3   ? 8.345   -8.481  -57.290 1.00 34.98 ? 3   ASN A C   1 
ATOM   4    O O   . ASN A 1 3   ? 8.427   -8.062  -56.133 1.00 34.97 ? 3   ASN A O   1 
ATOM   5    C CB  . ASN A 1 3   ? 6.908   -7.205  -58.912 1.00 35.35 ? 3   ASN A CB  1 
ATOM   6    C CG  . ASN A 1 3   ? 6.215   -6.210  -57.998 1.00 35.82 ? 3   ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 3   ? 6.463   -5.007  -58.066 1.00 36.71 ? 3   ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 3   ? 5.333   -6.708  -57.144 1.00 36.45 ? 3   ASN A ND2 1 
ATOM   9    N N   . ILE A 1 4   ? 8.247   -9.777  -57.590 1.00 34.65 ? 4   ILE A N   1 
ATOM   10   C CA  . ILE A 1 4   ? 8.265   -10.814 -56.558 1.00 34.39 ? 4   ILE A CA  1 
ATOM   11   C C   . ILE A 1 4   ? 9.696   -11.211 -56.160 1.00 34.12 ? 4   ILE A C   1 
ATOM   12   O O   . ILE A 1 4   ? 10.609  -11.219 -56.995 1.00 33.97 ? 4   ILE A O   1 
ATOM   13   C CB  . ILE A 1 4   ? 7.447   -12.059 -56.988 1.00 34.48 ? 4   ILE A CB  1 
ATOM   14   C CG1 . ILE A 1 4   ? 7.336   -13.063 -55.829 1.00 34.63 ? 4   ILE A CG1 1 
ATOM   15   C CG2 . ILE A 1 4   ? 8.036   -12.692 -58.267 1.00 34.66 ? 4   ILE A CG2 1 
ATOM   16   C CD1 . ILE A 1 4   ? 6.405   -14.223 -56.092 1.00 35.22 ? 4   ILE A CD1 1 
ATOM   17   N N   . LYS A 1 5   ? 9.870   -11.524 -54.874 1.00 33.71 ? 5   LYS A N   1 
ATOM   18   C CA  . LYS A 1 5   ? 11.162  -11.932 -54.321 1.00 33.30 ? 5   LYS A CA  1 
ATOM   19   C C   . LYS A 1 5   ? 10.992  -13.049 -53.301 1.00 32.90 ? 5   LYS A C   1 
ATOM   20   O O   . LYS A 1 5   ? 10.213  -12.932 -52.348 1.00 32.83 ? 5   LYS A O   1 
ATOM   21   C CB  . LYS A 1 5   ? 11.892  -10.737 -53.683 1.00 33.40 ? 5   LYS A CB  1 
ATOM   22   C CG  . LYS A 1 5   ? 12.715  -9.942  -54.669 1.00 33.96 ? 5   LYS A CG  1 
ATOM   23   C CD  . LYS A 1 5   ? 13.926  -10.728 -55.137 1.00 34.84 ? 5   LYS A CD  1 
ATOM   24   C CE  . LYS A 1 5   ? 14.320  -10.329 -56.548 1.00 35.37 ? 5   LYS A CE  1 
ATOM   25   N NZ  . LYS A 1 5   ? 15.318  -11.316 -57.087 1.00 36.39 ? 5   LYS A NZ  1 
ATOM   26   N N   . ILE A 1 6   ? 11.718  -14.140 -53.518 1.00 32.48 ? 6   ILE A N   1 
ATOM   27   C CA  . ILE A 1 6   ? 11.642  -15.287 -52.631 1.00 32.03 ? 6   ILE A CA  1 
ATOM   28   C C   . ILE A 1 6   ? 12.991  -15.504 -51.980 1.00 31.89 ? 6   ILE A C   1 
ATOM   29   O O   . ILE A 1 6   ? 14.008  -15.650 -52.660 1.00 31.85 ? 6   ILE A O   1 
ATOM   30   C CB  . ILE A 1 6   ? 11.183  -16.578 -53.359 1.00 32.00 ? 6   ILE A CB  1 
ATOM   31   C CG1 . ILE A 1 6   ? 10.171  -16.237 -54.475 1.00 31.79 ? 6   ILE A CG1 1 
ATOM   32   C CG2 . ILE A 1 6   ? 10.664  -17.614 -52.332 1.00 31.79 ? 6   ILE A CG2 1 
ATOM   33   C CD1 . ILE A 1 6   ? 8.932   -17.150 -54.506 1.00 31.22 ? 6   ILE A CD1 1 
ATOM   34   N N   . PHE A 1 7   ? 12.993  -15.505 -50.655 1.00 31.78 ? 7   PHE A N   1 
ATOM   35   C CA  . PHE A 1 7   ? 14.199  -15.783 -49.900 1.00 31.86 ? 7   PHE A CA  1 
ATOM   36   C C   . PHE A 1 7   ? 14.033  -17.059 -49.090 1.00 32.34 ? 7   PHE A C   1 
ATOM   37   O O   . PHE A 1 7   ? 12.921  -17.428 -48.709 1.00 32.38 ? 7   PHE A O   1 
ATOM   38   C CB  . PHE A 1 7   ? 14.545  -14.604 -48.989 1.00 31.49 ? 7   PHE A CB  1 
ATOM   39   C CG  . PHE A 1 7   ? 15.073  -13.404 -49.723 1.00 30.25 ? 7   PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 7   ? 16.434  -13.269 -49.967 1.00 28.64 ? 7   PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 7   ? 14.211  -12.404 -50.166 1.00 29.50 ? 7   PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 7   ? 16.935  -12.155 -50.640 1.00 28.04 ? 7   PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 7   ? 14.702  -11.285 -50.843 1.00 28.57 ? 7   PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 7   ? 16.067  -11.162 -51.080 1.00 28.12 ? 7   PHE A CZ  1 
ATOM   45   N N   . SER A 1 8   ? 15.145  -17.739 -48.850 1.00 33.00 ? 8   SER A N   1 
ATOM   46   C CA  . SER A 1 8   ? 15.144  -18.926 -48.019 1.00 33.68 ? 8   SER A CA  1 
ATOM   47   C C   . SER A 1 8   ? 15.811  -18.608 -46.693 1.00 34.44 ? 8   SER A C   1 
ATOM   48   O O   . SER A 1 8   ? 16.947  -18.134 -46.657 1.00 34.42 ? 8   SER A O   1 
ATOM   49   C CB  . SER A 1 8   ? 15.886  -20.063 -48.721 1.00 33.64 ? 8   SER A CB  1 
ATOM   50   O OG  . SER A 1 8   ? 15.728  -21.292 -48.033 1.00 32.98 ? 8   SER A OG  1 
ATOM   51   N N   . GLY A 1 9   ? 15.083  -18.840 -45.604 1.00 35.44 ? 9   GLY A N   1 
ATOM   52   C CA  . GLY A 1 9   ? 15.705  -18.858 -44.260 1.00 36.78 ? 9   GLY A CA  1 
ATOM   53   C C   . GLY A 1 9   ? 16.299  -20.250 -44.059 1.00 37.70 ? 9   GLY A C   1 
ATOM   54   O O   . GLY A 1 9   ? 16.114  -21.138 -44.930 1.00 38.08 ? 9   GLY A O   1 
ATOM   55   N N   . SER A 1 10  ? 17.036  -20.439 -42.948 1.00 38.56 ? 10  SER A N   1 
ATOM   56   C CA  . SER A 1 10  ? 17.662  -21.745 -42.663 1.00 39.44 ? 10  SER A CA  1 
ATOM   57   C C   . SER A 1 10  ? 18.941  -21.988 -43.454 1.00 39.92 ? 10  SER A C   1 
ATOM   58   O O   . SER A 1 10  ? 19.573  -21.052 -43.971 1.00 40.13 ? 10  SER A O   1 
ATOM   59   C CB  . SER A 1 10  ? 16.676  -22.917 -42.935 1.00 39.42 ? 10  SER A CB  1 
ATOM   60   O OG  . SER A 1 10  ? 15.644  -22.920 -41.888 1.00 40.04 ? 10  SER A OG  1 
ATOM   61   N N   . SER A 1 11  ? 19.314  -23.273 -43.512 1.00 40.37 ? 11  SER A N   1 
ATOM   62   C CA  . SER A 1 11  ? 20.376  -23.757 -44.389 1.00 40.86 ? 11  SER A CA  1 
ATOM   63   C C   . SER A 1 11  ? 19.711  -24.675 -45.404 1.00 41.06 ? 11  SER A C   1 
ATOM   64   O O   . SER A 1 11  ? 20.248  -24.912 -46.491 1.00 41.31 ? 11  SER A O   1 
ATOM   65   C CB  . SER A 1 11  ? 21.434  -24.535 -43.588 1.00 40.90 ? 11  SER A CB  1 
ATOM   66   O OG  . SER A 1 11  ? 22.256  -23.617 -42.856 1.00 41.16 ? 11  SER A OG  1 
ATOM   67   N N   . HIS A 1 12  ? 18.526  -25.167 -45.047 1.00 41.19 ? 12  HIS A N   1 
ATOM   68   C CA  . HIS A 1 12  ? 17.766  -26.068 -45.908 1.00 41.31 ? 12  HIS A CA  1 
ATOM   69   C C   . HIS A 1 12  ? 17.125  -25.334 -47.089 1.00 41.18 ? 12  HIS A C   1 
ATOM   70   O O   . HIS A 1 12  ? 15.921  -25.029 -47.073 1.00 41.26 ? 12  HIS A O   1 
ATOM   71   C CB  . HIS A 1 12  ? 16.708  -26.839 -45.101 1.00 41.35 ? 12  HIS A CB  1 
ATOM   72   C CG  . HIS A 1 12  ? 17.283  -27.735 -44.048 1.00 41.86 ? 12  HIS A CG  1 
ATOM   73   N ND1 . HIS A 1 12  ? 17.000  -27.574 -42.698 1.00 42.23 ? 12  HIS A ND1 1 
ATOM   74   C CD2 . HIS A 1 12  ? 18.139  -28.796 -44.149 1.00 42.47 ? 12  HIS A CD2 1 
ATOM   75   C CE1 . HIS A 1 12  ? 17.652  -28.498 -42.011 1.00 42.41 ? 12  HIS A CE1 1 
ATOM   76   N NE2 . HIS A 1 12  ? 18.353  -29.252 -42.869 1.00 42.45 ? 12  HIS A NE2 1 
ATOM   77   N N   . GLN A 1 13  ? 17.948  -25.059 -48.108 1.00 40.90 ? 13  GLN A N   1 
ATOM   78   C CA  . GLN A 1 13  ? 17.470  -24.521 -49.388 1.00 40.67 ? 13  GLN A CA  1 
ATOM   79   C C   . GLN A 1 13  ? 16.446  -25.469 -50.011 1.00 40.24 ? 13  GLN A C   1 
ATOM   80   O O   . GLN A 1 13  ? 15.756  -25.115 -50.968 1.00 40.11 ? 13  GLN A O   1 
ATOM   81   C CB  . GLN A 1 13  ? 18.642  -24.341 -50.362 1.00 40.86 ? 13  GLN A CB  1 
ATOM   82   C CG  . GLN A 1 13  ? 19.747  -23.392 -49.898 1.00 41.47 ? 13  GLN A CG  1 
ATOM   83   C CD  . GLN A 1 13  ? 19.476  -21.943 -50.260 1.00 42.46 ? 13  GLN A CD  1 
ATOM   84   O OE1 . GLN A 1 13  ? 18.557  -21.319 -49.733 1.00 42.89 ? 13  GLN A OE1 1 
ATOM   85   N NE2 . GLN A 1 13  ? 20.292  -21.394 -51.157 1.00 42.59 ? 13  GLN A NE2 1 
ATOM   86   N N   . ASP A 1 14  ? 16.368  -26.670 -49.440 1.00 39.88 ? 14  ASP A N   1 
ATOM   87   C CA  . ASP A 1 14  ? 15.528  -27.777 -49.906 1.00 39.59 ? 14  ASP A CA  1 
ATOM   88   C C   . ASP A 1 14  ? 14.182  -27.369 -50.544 1.00 39.04 ? 14  ASP A C   1 
ATOM   89   O O   . ASP A 1 14  ? 14.036  -27.420 -51.770 1.00 39.04 ? 14  ASP A O   1 
ATOM   90   C CB  . ASP A 1 14  ? 15.326  -28.790 -48.758 1.00 39.85 ? 14  ASP A CB  1 
ATOM   91   C CG  . ASP A 1 14  ? 16.654  -29.195 -48.077 1.00 40.76 ? 14  ASP A CG  1 
ATOM   92   O OD1 . ASP A 1 14  ? 17.733  -29.070 -48.701 1.00 41.87 ? 14  ASP A OD1 1 
ATOM   93   O OD2 . ASP A 1 14  ? 16.619  -29.644 -46.906 1.00 41.43 ? 14  ASP A OD2 1 
ATOM   94   N N   . LEU A 1 15  ? 13.219  -26.952 -49.717 1.00 38.22 ? 15  LEU A N   1 
ATOM   95   C CA  . LEU A 1 15  ? 11.853  -26.665 -50.175 1.00 37.41 ? 15  LEU A CA  1 
ATOM   96   C C   . LEU A 1 15  ? 11.713  -25.333 -50.923 1.00 37.12 ? 15  LEU A C   1 
ATOM   97   O O   . LEU A 1 15  ? 10.888  -25.208 -51.834 1.00 37.02 ? 15  LEU A O   1 
ATOM   98   C CB  . LEU A 1 15  ? 10.878  -26.722 -48.990 1.00 37.33 ? 15  LEU A CB  1 
ATOM   99   C CG  . LEU A 1 15  ? 9.362   -26.607 -49.206 1.00 36.78 ? 15  LEU A CG  1 
ATOM   100  C CD1 . LEU A 1 15  ? 8.812   -27.804 -49.970 1.00 36.62 ? 15  LEU A CD1 1 
ATOM   101  C CD2 . LEU A 1 15  ? 8.656   -26.467 -47.867 1.00 36.25 ? 15  LEU A CD2 1 
ATOM   102  N N   . SER A 1 16  ? 12.512  -24.341 -50.532 1.00 36.63 ? 16  SER A N   1 
ATOM   103  C CA  . SER A 1 16  ? 12.494  -23.027 -51.182 1.00 36.19 ? 16  SER A CA  1 
ATOM   104  C C   . SER A 1 16  ? 12.810  -23.100 -52.676 1.00 35.74 ? 16  SER A C   1 
ATOM   105  O O   . SER A 1 16  ? 12.114  -22.488 -53.489 1.00 35.71 ? 16  SER A O   1 
ATOM   106  C CB  . SER A 1 16  ? 13.470  -22.072 -50.494 1.00 36.21 ? 16  SER A CB  1 
ATOM   107  O OG  . SER A 1 16  ? 13.155  -21.929 -49.120 1.00 36.75 ? 16  SER A OG  1 
ATOM   108  N N   . GLN A 1 17  ? 13.850  -23.859 -53.025 1.00 35.20 ? 17  GLN A N   1 
ATOM   109  C CA  . GLN A 1 17  ? 14.311  -23.974 -54.409 1.00 34.78 ? 17  GLN A CA  1 
ATOM   110  C C   . GLN A 1 17  ? 13.219  -24.483 -55.344 1.00 34.27 ? 17  GLN A C   1 
ATOM   111  O O   . GLN A 1 17  ? 13.075  -23.985 -56.456 1.00 34.33 ? 17  GLN A O   1 
ATOM   112  C CB  . GLN A 1 17  ? 15.557  -24.868 -54.501 1.00 34.94 ? 17  GLN A CB  1 
ATOM   113  C CG  . GLN A 1 17  ? 16.387  -24.687 -55.782 1.00 35.51 ? 17  GLN A CG  1 
ATOM   114  C CD  . GLN A 1 17  ? 16.881  -23.254 -55.983 1.00 36.35 ? 17  GLN A CD  1 
ATOM   115  O OE1 . GLN A 1 17  ? 16.179  -22.414 -56.550 1.00 36.88 ? 17  GLN A OE1 1 
ATOM   116  N NE2 . GLN A 1 17  ? 18.099  -22.979 -55.528 1.00 36.40 ? 17  GLN A NE2 1 
ATOM   117  N N   . LYS A 1 18  ? 12.456  -25.472 -54.883 1.00 33.67 ? 18  LYS A N   1 
ATOM   118  C CA  . LYS A 1 18  ? 11.351  -26.035 -55.658 1.00 32.96 ? 18  LYS A CA  1 
ATOM   119  C C   . LYS A 1 18  ? 10.257  -24.996 -55.877 1.00 32.70 ? 18  LYS A C   1 
ATOM   120  O O   . LYS A 1 18  ? 9.682   -24.907 -56.968 1.00 32.62 ? 18  LYS A O   1 
ATOM   121  C CB  . LYS A 1 18  ? 10.757  -27.264 -54.959 1.00 32.83 ? 18  LYS A CB  1 
ATOM   122  C CG  . LYS A 1 18  ? 11.731  -28.411 -54.721 1.00 32.10 ? 18  LYS A CG  1 
ATOM   123  C CD  . LYS A 1 18  ? 10.956  -29.662 -54.314 1.00 31.79 ? 18  LYS A CD  1 
ATOM   124  C CE  . LYS A 1 18  ? 11.894  -30.859 -54.138 1.00 31.61 ? 18  LYS A CE  1 
ATOM   125  N NZ  . LYS A 1 18  ? 11.118  -32.134 -54.290 1.00 30.94 ? 18  LYS A NZ  1 
ATOM   126  N N   . ILE A 1 19  ? 9.971   -24.218 -54.834 1.00 32.53 ? 19  ILE A N   1 
ATOM   127  C CA  . ILE A 1 19  ? 8.957   -23.162 -54.910 1.00 32.19 ? 19  ILE A CA  1 
ATOM   128  C C   . ILE A 1 19  ? 9.411   -22.092 -55.898 1.00 32.10 ? 19  ILE A C   1 
ATOM   129  O O   . ILE A 1 19  ? 8.630   -21.645 -56.743 1.00 32.08 ? 19  ILE A O   1 
ATOM   130  C CB  . ILE A 1 19  ? 8.655   -22.551 -53.521 1.00 32.11 ? 19  ILE A CB  1 
ATOM   131  C CG1 . ILE A 1 19  ? 8.048   -23.617 -52.598 1.00 31.65 ? 19  ILE A CG1 1 
ATOM   132  C CG2 . ILE A 1 19  ? 7.720   -21.346 -53.647 1.00 32.13 ? 19  ILE A CG2 1 
ATOM   133  C CD1 . ILE A 1 19  ? 8.082   -23.252 -51.124 1.00 31.27 ? 19  ILE A CD1 1 
ATOM   134  N N   . ALA A 1 20  ? 10.681  -21.707 -55.800 1.00 32.00 ? 20  ALA A N   1 
ATOM   135  C CA  . ALA A 1 20  ? 11.289  -20.801 -56.768 1.00 32.05 ? 20  ALA A CA  1 
ATOM   136  C C   . ALA A 1 20  ? 11.232  -21.377 -58.188 1.00 32.10 ? 20  ALA A C   1 
ATOM   137  O O   . ALA A 1 20  ? 10.972  -20.642 -59.143 1.00 32.12 ? 20  ALA A O   1 
ATOM   138  C CB  . ALA A 1 20  ? 12.720  -20.469 -56.366 1.00 31.90 ? 20  ALA A CB  1 
ATOM   139  N N   . ASP A 1 21  ? 11.454  -22.686 -58.316 1.00 32.21 ? 21  ASP A N   1 
ATOM   140  C CA  . ASP A 1 21  ? 11.355  -23.373 -59.607 1.00 32.39 ? 21  ASP A CA  1 
ATOM   141  C C   . ASP A 1 21  ? 9.953   -23.275 -60.199 1.00 32.31 ? 21  ASP A C   1 
ATOM   142  O O   . ASP A 1 21  ? 9.779   -22.792 -61.326 1.00 32.36 ? 21  ASP A O   1 
ATOM   143  C CB  . ASP A 1 21  ? 11.748  -24.849 -59.491 1.00 32.60 ? 21  ASP A CB  1 
ATOM   144  C CG  . ASP A 1 21  ? 13.214  -25.048 -59.171 1.00 33.31 ? 21  ASP A CG  1 
ATOM   145  O OD1 . ASP A 1 21  ? 13.984  -24.062 -59.210 1.00 34.12 ? 21  ASP A OD1 1 
ATOM   146  O OD2 . ASP A 1 21  ? 13.592  -26.205 -58.876 1.00 33.67 ? 21  ASP A OD2 1 
ATOM   147  N N   . ARG A 1 22  ? 8.955   -23.713 -59.434 1.00 32.08 ? 22  ARG A N   1 
ATOM   148  C CA  . ARG A 1 22  ? 7.571   -23.721 -59.915 1.00 31.98 ? 22  ARG A CA  1 
ATOM   149  C C   . ARG A 1 22  ? 7.108   -22.325 -60.356 1.00 31.62 ? 22  ARG A C   1 
ATOM   150  O O   . ARG A 1 22  ? 6.142   -22.193 -61.105 1.00 31.78 ? 22  ARG A O   1 
ATOM   151  C CB  . ARG A 1 22  ? 6.618   -24.346 -58.877 1.00 32.05 ? 22  ARG A CB  1 
ATOM   152  C CG  . ARG A 1 22  ? 7.125   -25.677 -58.307 1.00 32.87 ? 22  ARG A CG  1 
ATOM   153  C CD  . ARG A 1 22  ? 6.057   -26.763 -58.202 1.00 34.56 ? 22  ARG A CD  1 
ATOM   154  N NE  . ARG A 1 22  ? 6.676   -28.069 -57.937 1.00 36.25 ? 22  ARG A NE  1 
ATOM   155  C CZ  . ARG A 1 22  ? 6.100   -29.257 -58.146 1.00 36.84 ? 22  ARG A CZ  1 
ATOM   156  N NH1 . ARG A 1 22  ? 4.865   -29.341 -58.637 1.00 37.07 ? 22  ARG A NH1 1 
ATOM   157  N NH2 . ARG A 1 22  ? 6.770   -30.374 -57.868 1.00 36.13 ? 22  ARG A NH2 1 
ATOM   158  N N   . LEU A 1 23  ? 7.831   -21.295 -59.919 1.00 31.20 ? 23  LEU A N   1 
ATOM   159  C CA  . LEU A 1 23  ? 7.482   -19.904 -60.229 1.00 30.64 ? 23  LEU A CA  1 
ATOM   160  C C   . LEU A 1 23  ? 8.407   -19.247 -61.258 1.00 30.44 ? 23  LEU A C   1 
ATOM   161  O O   . LEU A 1 23  ? 8.208   -18.084 -61.633 1.00 30.44 ? 23  LEU A O   1 
ATOM   162  C CB  . LEU A 1 23  ? 7.429   -19.072 -58.943 1.00 30.58 ? 23  LEU A CB  1 
ATOM   163  C CG  . LEU A 1 23  ? 6.341   -19.478 -57.946 1.00 29.78 ? 23  LEU A CG  1 
ATOM   164  C CD1 . LEU A 1 23  ? 6.600   -18.867 -56.594 1.00 28.78 ? 23  LEU A CD1 1 
ATOM   165  C CD2 . LEU A 1 23  ? 4.954   -19.091 -58.457 1.00 30.08 ? 23  LEU A CD2 1 
ATOM   166  N N   . GLY A 1 24  ? 9.408   -19.999 -61.716 1.00 30.20 ? 24  GLY A N   1 
ATOM   167  C CA  . GLY A 1 24  ? 10.363  -19.505 -62.706 1.00 29.71 ? 24  GLY A CA  1 
ATOM   168  C C   . GLY A 1 24  ? 11.270  -18.453 -62.108 1.00 29.44 ? 24  GLY A C   1 
ATOM   169  O O   . GLY A 1 24  ? 11.691  -17.516 -62.790 1.00 29.52 ? 24  GLY A O   1 
ATOM   170  N N   . LEU A 1 25  ? 11.564  -18.608 -60.821 1.00 29.25 ? 25  LEU A N   1 
ATOM   171  C CA  . LEU A 1 25  ? 12.386  -17.647 -60.092 1.00 29.02 ? 25  LEU A CA  1 
ATOM   172  C C   . LEU A 1 25  ? 13.622  -18.283 -59.483 1.00 28.89 ? 25  LEU A C   1 
ATOM   173  O O   . LEU A 1 25  ? 13.672  -19.494 -59.249 1.00 28.91 ? 25  LEU A O   1 
ATOM   174  C CB  . LEU A 1 25  ? 11.573  -16.969 -58.987 1.00 28.93 ? 25  LEU A CB  1 
ATOM   175  C CG  . LEU A 1 25  ? 10.349  -16.145 -59.391 1.00 29.07 ? 25  LEU A CG  1 
ATOM   176  C CD1 . LEU A 1 25  ? 9.509   -15.851 -58.162 1.00 28.52 ? 25  LEU A CD1 1 
ATOM   177  C CD2 . LEU A 1 25  ? 10.754  -14.856 -60.098 1.00 28.86 ? 25  LEU A CD2 1 
ATOM   178  N N   . GLU A 1 26  ? 14.622  -17.445 -59.239 1.00 28.74 ? 26  GLU A N   1 
ATOM   179  C CA  . GLU A 1 26  ? 15.778  -17.835 -58.446 1.00 28.56 ? 26  GLU A CA  1 
ATOM   180  C C   . GLU A 1 26  ? 15.612  -17.209 -57.075 1.00 28.04 ? 26  GLU A C   1 
ATOM   181  O O   . GLU A 1 26  ? 14.871  -16.234 -56.919 1.00 27.65 ? 26  GLU A O   1 
ATOM   182  C CB  . GLU A 1 26  ? 17.071  -17.349 -59.103 1.00 28.90 ? 26  GLU A CB  1 
ATOM   183  C CG  . GLU A 1 26  ? 17.491  -18.224 -60.292 1.00 30.19 ? 26  GLU A CG  1 
ATOM   184  C CD  . GLU A 1 26  ? 18.654  -17.633 -61.066 1.00 32.21 ? 26  GLU A CD  1 
ATOM   185  O OE1 . GLU A 1 26  ? 19.386  -16.753 -60.518 1.00 33.18 ? 26  GLU A OE1 1 
ATOM   186  O OE2 . GLU A 1 26  ? 18.839  -18.059 -62.231 1.00 33.10 ? 26  GLU A OE2 1 
ATOM   187  N N   . LEU A 1 27  ? 16.294  -17.776 -56.084 1.00 27.73 ? 27  LEU A N   1 
ATOM   188  C CA  . LEU A 1 27  ? 16.220  -17.250 -54.724 1.00 27.51 ? 27  LEU A CA  1 
ATOM   189  C C   . LEU A 1 27  ? 17.105  -16.025 -54.591 1.00 27.58 ? 27  LEU A C   1 
ATOM   190  O O   . LEU A 1 27  ? 18.192  -15.967 -55.169 1.00 27.31 ? 27  LEU A O   1 
ATOM   191  C CB  . LEU A 1 27  ? 16.635  -18.312 -53.697 1.00 27.32 ? 27  LEU A CB  1 
ATOM   192  C CG  . LEU A 1 27  ? 15.733  -19.539 -53.513 1.00 26.93 ? 27  LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 27  ? 16.440  -20.586 -52.649 1.00 26.29 ? 27  LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 27  ? 14.373  -19.158 -52.922 1.00 26.16 ? 27  LEU A CD2 1 
ATOM   195  N N   . GLY A 1 28  ? 16.630  -15.048 -53.823 1.00 27.94 ? 28  GLY A N   1 
ATOM   196  C CA  . GLY A 1 28  ? 17.416  -13.851 -53.541 1.00 28.67 ? 28  GLY A CA  1 
ATOM   197  C C   . GLY A 1 28  ? 18.739  -14.171 -52.862 1.00 29.29 ? 28  GLY A C   1 
ATOM   198  O O   . GLY A 1 28  ? 18.861  -15.161 -52.124 1.00 29.04 ? 28  GLY A O   1 
ATOM   199  N N   . LYS A 1 29  ? 19.733  -13.326 -53.122 1.00 29.95 ? 29  LYS A N   1 
ATOM   200  C CA  . LYS A 1 29  ? 21.043  -13.457 -52.503 1.00 30.79 ? 29  LYS A CA  1 
ATOM   201  C C   . LYS A 1 29  ? 20.985  -13.084 -51.020 1.00 31.46 ? 29  LYS A C   1 
ATOM   202  O O   . LYS A 1 29  ? 20.607  -11.967 -50.658 1.00 31.37 ? 29  LYS A O   1 
ATOM   203  C CB  . LYS A 1 29  ? 22.069  -12.594 -53.242 1.00 30.80 ? 29  LYS A CB  1 
ATOM   204  N N   . VAL A 1 30  ? 21.336  -14.043 -50.167 1.00 32.35 ? 30  VAL A N   1 
ATOM   205  C CA  . VAL A 1 30  ? 21.449  -13.801 -48.735 1.00 33.29 ? 30  VAL A CA  1 
ATOM   206  C C   . VAL A 1 30  ? 22.808  -14.283 -48.271 1.00 33.99 ? 30  VAL A C   1 
ATOM   207  O O   . VAL A 1 30  ? 23.230  -15.392 -48.612 1.00 34.04 ? 30  VAL A O   1 
ATOM   208  C CB  . VAL A 1 30  ? 20.379  -14.555 -47.899 1.00 33.26 ? 30  VAL A CB  1 
ATOM   209  C CG1 . VAL A 1 30  ? 20.160  -13.862 -46.563 1.00 33.11 ? 30  VAL A CG1 1 
ATOM   210  C CG2 . VAL A 1 30  ? 19.071  -14.680 -48.644 1.00 33.54 ? 30  VAL A CG2 1 
ATOM   211  N N   . VAL A 1 31  ? 23.495  -13.435 -47.497 1.00 35.02 ? 31  VAL A N   1 
ATOM   212  C CA  . VAL A 1 31  ? 24.673  -13.864 -46.748 1.00 36.05 ? 31  VAL A CA  1 
ATOM   213  C C   . VAL A 1 31  ? 24.320  -13.896 -45.262 1.00 36.60 ? 31  VAL A C   1 
ATOM   214  O O   . VAL A 1 31  ? 24.086  -12.856 -44.631 1.00 36.76 ? 31  VAL A O   1 
ATOM   215  C CB  . VAL A 1 31  ? 25.943  -12.989 -47.042 1.00 36.07 ? 31  VAL A CB  1 
ATOM   216  C CG1 . VAL A 1 31  ? 25.619  -11.499 -47.030 1.00 36.44 ? 31  VAL A CG1 1 
ATOM   217  C CG2 . VAL A 1 31  ? 27.085  -13.310 -46.064 1.00 36.44 ? 31  VAL A CG2 1 
ATOM   218  N N   . THR A 1 32  ? 24.248  -15.105 -44.719 1.00 37.29 ? 32  THR A N   1 
ATOM   219  C CA  . THR A 1 32  ? 23.959  -15.285 -43.305 1.00 38.04 ? 32  THR A CA  1 
ATOM   220  C C   . THR A 1 32  ? 25.166  -15.878 -42.578 1.00 38.45 ? 32  THR A C   1 
ATOM   221  O O   . THR A 1 32  ? 25.674  -16.934 -42.958 1.00 38.57 ? 32  THR A O   1 
ATOM   222  C CB  . THR A 1 32  ? 22.672  -16.118 -43.072 1.00 38.02 ? 32  THR A CB  1 
ATOM   223  O OG1 . THR A 1 32  ? 22.759  -16.797 -41.812 1.00 38.31 ? 32  THR A OG1 1 
ATOM   224  C CG2 . THR A 1 32  ? 22.474  -17.140 -44.178 1.00 38.20 ? 32  THR A CG2 1 
ATOM   225  N N   . LYS A 1 33  ? 25.633  -15.174 -41.550 1.00 39.09 ? 33  LYS A N   1 
ATOM   226  C CA  . LYS A 1 33  ? 26.798  -15.594 -40.769 1.00 39.66 ? 33  LYS A CA  1 
ATOM   227  C C   . LYS A 1 33  ? 26.438  -15.915 -39.321 1.00 39.91 ? 33  LYS A C   1 
ATOM   228  O O   . LYS A 1 33  ? 25.695  -15.177 -38.673 1.00 39.94 ? 33  LYS A O   1 
ATOM   229  C CB  . LYS A 1 33  ? 27.903  -14.536 -40.832 1.00 39.75 ? 33  LYS A CB  1 
ATOM   230  C CG  . LYS A 1 33  ? 28.959  -14.841 -41.888 1.00 40.35 ? 33  LYS A CG  1 
ATOM   231  C CD  . LYS A 1 33  ? 29.655  -13.558 -42.373 1.00 41.37 ? 33  LYS A CD  1 
ATOM   232  C CE  . LYS A 1 33  ? 30.638  -13.862 -43.511 1.00 41.96 ? 33  LYS A CE  1 
ATOM   233  N NZ  . LYS A 1 33  ? 29.968  -14.530 -44.705 1.00 42.20 ? 33  LYS A NZ  1 
ATOM   234  N N   . LYS A 1 34  ? 26.970  -17.028 -38.825 1.00 40.22 ? 34  LYS A N   1 
ATOM   235  C CA  . LYS A 1 34  ? 26.619  -17.524 -37.497 1.00 40.44 ? 34  LYS A CA  1 
ATOM   236  C C   . LYS A 1 34  ? 27.865  -17.759 -36.655 1.00 40.69 ? 34  LYS A C   1 
ATOM   237  O O   . LYS A 1 34  ? 28.801  -18.439 -37.088 1.00 40.76 ? 34  LYS A O   1 
ATOM   238  C CB  . LYS A 1 34  ? 25.810  -18.822 -37.606 1.00 40.34 ? 34  LYS A CB  1 
ATOM   239  C CG  . LYS A 1 34  ? 24.486  -18.688 -38.356 1.00 40.40 ? 34  LYS A CG  1 
ATOM   240  C CD  . LYS A 1 34  ? 23.788  -20.065 -38.451 1.00 40.23 ? 34  LYS A CD  1 
ATOM   241  C CE  . LYS A 1 34  ? 22.321  -19.906 -38.812 1.00 40.10 ? 34  LYS A CE  1 
ATOM   242  N NZ  . LYS A 1 34  ? 21.550  -21.199 -38.650 1.00 39.70 ? 34  LYS A NZ  1 
ATOM   243  N N   . PHE A 1 35  ? 27.875  -17.184 -35.456 1.00 40.88 ? 35  PHE A N   1 
ATOM   244  C CA  . PHE A 1 35  ? 28.953  -17.424 -34.503 1.00 41.10 ? 35  PHE A CA  1 
ATOM   245  C C   . PHE A 1 35  ? 28.762  -18.794 -33.845 1.00 41.18 ? 35  PHE A C   1 
ATOM   246  O O   . PHE A 1 35  ? 27.696  -19.404 -33.976 1.00 41.12 ? 35  PHE A O   1 
ATOM   247  C CB  . PHE A 1 35  ? 28.992  -16.317 -33.442 1.00 41.24 ? 35  PHE A CB  1 
ATOM   248  C CG  . PHE A 1 35  ? 29.189  -14.928 -34.007 1.00 41.53 ? 35  PHE A CG  1 
ATOM   249  C CD1 . PHE A 1 35  ? 30.334  -14.606 -34.741 1.00 41.89 ? 35  PHE A CD1 1 
ATOM   250  C CD2 . PHE A 1 35  ? 28.238  -13.934 -33.781 1.00 41.68 ? 35  PHE A CD2 1 
ATOM   251  C CE1 . PHE A 1 35  ? 30.518  -13.321 -35.257 1.00 42.10 ? 35  PHE A CE1 1 
ATOM   252  C CE2 . PHE A 1 35  ? 28.411  -12.644 -34.290 1.00 42.23 ? 35  PHE A CE2 1 
ATOM   253  C CZ  . PHE A 1 35  ? 29.554  -12.337 -35.030 1.00 42.31 ? 35  PHE A CZ  1 
ATOM   254  N N   . SER A 1 36  ? 29.793  -19.280 -33.152 1.00 41.35 ? 36  SER A N   1 
ATOM   255  C CA  . SER A 1 36  ? 29.686  -20.521 -32.366 1.00 41.41 ? 36  SER A CA  1 
ATOM   256  C C   . SER A 1 36  ? 28.534  -20.380 -31.375 1.00 41.49 ? 36  SER A C   1 
ATOM   257  O O   . SER A 1 36  ? 27.882  -21.362 -31.009 1.00 41.56 ? 36  SER A O   1 
ATOM   258  C CB  . SER A 1 36  ? 30.987  -20.800 -31.613 1.00 41.39 ? 36  SER A CB  1 
ATOM   259  N N   . ASN A 1 37  ? 28.304  -19.127 -30.975 1.00 41.46 ? 37  ASN A N   1 
ATOM   260  C CA  . ASN A 1 37  ? 27.194  -18.688 -30.134 1.00 41.31 ? 37  ASN A CA  1 
ATOM   261  C C   . ASN A 1 37  ? 25.814  -19.003 -30.719 1.00 41.07 ? 37  ASN A C   1 
ATOM   262  O O   . ASN A 1 37  ? 24.820  -19.084 -29.989 1.00 41.07 ? 37  ASN A O   1 
ATOM   263  C CB  . ASN A 1 37  ? 27.324  -17.170 -29.933 1.00 41.40 ? 37  ASN A CB  1 
ATOM   264  C CG  . ASN A 1 37  ? 26.432  -16.647 -28.823 1.00 41.87 ? 37  ASN A CG  1 
ATOM   265  O OD1 . ASN A 1 37  ? 26.318  -17.251 -27.745 1.00 42.50 ? 37  ASN A OD1 1 
ATOM   266  N ND2 . ASN A 1 37  ? 25.803  -15.505 -29.078 1.00 42.67 ? 37  ASN A ND2 1 
ATOM   267  N N   . GLN A 1 38  ? 25.783  -19.186 -32.040 1.00 40.64 ? 38  GLN A N   1 
ATOM   268  C CA  . GLN A 1 38  ? 24.560  -19.282 -32.846 1.00 40.21 ? 38  GLN A CA  1 
ATOM   269  C C   . GLN A 1 38  ? 23.861  -17.936 -33.023 1.00 39.77 ? 38  GLN A C   1 
ATOM   270  O O   . GLN A 1 38  ? 22.712  -17.875 -33.488 1.00 39.73 ? 38  GLN A O   1 
ATOM   271  C CB  . GLN A 1 38  ? 23.590  -20.364 -32.345 1.00 40.40 ? 38  GLN A CB  1 
ATOM   272  C CG  . GLN A 1 38  ? 23.983  -21.803 -32.743 1.00 40.87 ? 38  GLN A CG  1 
ATOM   273  C CD  . GLN A 1 38  ? 24.345  -21.919 -34.231 1.00 41.50 ? 38  GLN A CD  1 
ATOM   274  O OE1 . GLN A 1 38  ? 25.332  -22.571 -34.584 1.00 42.05 ? 38  GLN A OE1 1 
ATOM   275  N NE2 . GLN A 1 38  ? 23.552  -21.284 -35.111 1.00 41.35 ? 38  GLN A NE2 1 
ATOM   276  N N   . GLU A 1 39  ? 24.564  -16.860 -32.664 1.00 39.18 ? 39  GLU A N   1 
ATOM   277  C CA  . GLU A 1 39  ? 24.094  -15.516 -32.967 1.00 38.62 ? 39  GLU A CA  1 
ATOM   278  C C   . GLU A 1 39  ? 24.057  -15.362 -34.479 1.00 38.30 ? 39  GLU A C   1 
ATOM   279  O O   . GLU A 1 39  ? 25.063  -15.576 -35.160 1.00 38.18 ? 39  GLU A O   1 
ATOM   280  C CB  . GLU A 1 39  ? 24.988  -14.456 -32.326 1.00 38.58 ? 39  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 39  ? 24.385  -13.056 -32.379 1.00 38.56 ? 39  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 39  ? 25.265  -11.997 -31.747 1.00 38.40 ? 39  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 39  ? 25.416  -10.915 -32.359 1.00 38.24 ? 39  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 39  ? 25.803  -12.236 -30.643 1.00 38.49 ? 39  GLU A OE2 1 
ATOM   285  N N   . THR A 1 40  ? 22.882  -15.014 -34.993 1.00 37.99 ? 40  THR A N   1 
ATOM   286  C CA  . THR A 1 40  ? 22.633  -15.021 -36.429 1.00 37.66 ? 40  THR A CA  1 
ATOM   287  C C   . THR A 1 40  ? 22.825  -13.637 -37.046 1.00 37.52 ? 40  THR A C   1 
ATOM   288  O O   . THR A 1 40  ? 22.170  -12.668 -36.653 1.00 37.17 ? 40  THR A O   1 
ATOM   289  C CB  . THR A 1 40  ? 21.227  -15.603 -36.743 1.00 37.63 ? 40  THR A CB  1 
ATOM   290  O OG1 . THR A 1 40  ? 21.193  -16.984 -36.338 1.00 37.76 ? 40  THR A OG1 1 
ATOM   291  C CG2 . THR A 1 40  ? 20.897  -15.507 -38.233 1.00 37.48 ? 40  THR A CG2 1 
ATOM   292  N N   . CYS A 1 41  ? 23.749  -13.561 -38.001 1.00 37.47 ? 41  CYS A N   1 
ATOM   293  C CA  . CYS A 1 41  ? 23.977  -12.350 -38.778 1.00 37.67 ? 41  CYS A CA  1 
ATOM   294  C C   . CYS A 1 41  ? 23.415  -12.562 -40.175 1.00 37.32 ? 41  CYS A C   1 
ATOM   295  O O   . CYS A 1 41  ? 23.620  -13.613 -40.784 1.00 37.34 ? 41  CYS A O   1 
ATOM   296  C CB  . CYS A 1 41  ? 25.468  -12.011 -38.843 1.00 37.85 ? 41  CYS A CB  1 
ATOM   297  S SG  . CYS A 1 41  ? 26.295  -11.919 -37.226 1.00 39.55 ? 41  CYS A SG  1 
ATOM   298  N N   . VAL A 1 42  ? 22.688  -11.563 -40.667 1.00 36.93 ? 42  VAL A N   1 
ATOM   299  C CA  . VAL A 1 42  ? 22.030  -11.640 -41.961 1.00 36.44 ? 42  VAL A CA  1 
ATOM   300  C C   . VAL A 1 42  ? 22.279  -10.347 -42.724 1.00 36.05 ? 42  VAL A C   1 
ATOM   301  O O   . VAL A 1 42  ? 22.170  -9.254  -42.168 1.00 36.04 ? 42  VAL A O   1 
ATOM   302  C CB  . VAL A 1 42  ? 20.507  -11.902 -41.801 1.00 36.63 ? 42  VAL A CB  1 
ATOM   303  C CG1 . VAL A 1 42  ? 19.751  -11.657 -43.110 1.00 36.69 ? 42  VAL A CG1 1 
ATOM   304  C CG2 . VAL A 1 42  ? 20.257  -13.324 -41.301 1.00 36.59 ? 42  VAL A CG2 1 
ATOM   305  N N   . GLU A 1 43  ? 22.634  -10.487 -43.998 1.00 35.46 ? 43  GLU A N   1 
ATOM   306  C CA  . GLU A 1 43  ? 22.863  -9.350  -44.880 1.00 34.80 ? 43  GLU A CA  1 
ATOM   307  C C   . GLU A 1 43  ? 22.183  -9.650  -46.220 1.00 33.93 ? 43  GLU A C   1 
ATOM   308  O O   . GLU A 1 43  ? 22.516  -10.637 -46.888 1.00 33.74 ? 43  GLU A O   1 
ATOM   309  C CB  . GLU A 1 43  ? 24.372  -9.105  -45.023 1.00 35.01 ? 43  GLU A CB  1 
ATOM   310  C CG  . GLU A 1 43  ? 24.786  -7.880  -45.843 1.00 36.41 ? 43  GLU A CG  1 
ATOM   311  C CD  . GLU A 1 43  ? 26.294  -7.594  -45.741 1.00 38.30 ? 43  GLU A CD  1 
ATOM   312  O OE1 . GLU A 1 43  ? 26.870  -7.763  -44.640 1.00 38.78 ? 43  GLU A OE1 1 
ATOM   313  O OE2 . GLU A 1 43  ? 26.902  -7.189  -46.766 1.00 38.59 ? 43  GLU A OE2 1 
ATOM   314  N N   . ILE A 1 44  ? 21.204  -8.818  -46.588 1.00 32.87 ? 44  ILE A N   1 
ATOM   315  C CA  . ILE A 1 44  ? 20.441  -9.012  -47.827 1.00 31.77 ? 44  ILE A CA  1 
ATOM   316  C C   . ILE A 1 44  ? 21.281  -8.579  -49.026 1.00 31.19 ? 44  ILE A C   1 
ATOM   317  O O   . ILE A 1 44  ? 21.697  -7.419  -49.119 1.00 31.04 ? 44  ILE A O   1 
ATOM   318  C CB  . ILE A 1 44  ? 19.068  -8.268  -47.827 1.00 31.74 ? 44  ILE A CB  1 
ATOM   319  C CG1 . ILE A 1 44  ? 18.362  -8.350  -46.456 1.00 31.69 ? 44  ILE A CG1 1 
ATOM   320  C CG2 . ILE A 1 44  ? 18.173  -8.783  -48.967 1.00 31.28 ? 44  ILE A CG2 1 
ATOM   321  C CD1 . ILE A 1 44  ? 17.959  -9.768  -45.998 1.00 32.10 ? 44  ILE A CD1 1 
ATOM   322  N N   . GLY A 1 45  ? 21.514  -9.524  -49.937 1.00 30.42 ? 45  GLY A N   1 
ATOM   323  C CA  . GLY A 1 45  ? 22.484  -9.357  -51.022 1.00 29.47 ? 45  GLY A CA  1 
ATOM   324  C C   . GLY A 1 45  ? 21.994  -8.630  -52.257 1.00 28.84 ? 45  GLY A C   1 
ATOM   325  O O   . GLY A 1 45  ? 22.693  -8.584  -53.265 1.00 28.69 ? 45  GLY A O   1 
ATOM   326  N N   . GLU A 1 46  ? 20.791  -8.069  -52.180 1.00 28.48 ? 46  GLU A N   1 
ATOM   327  C CA  . GLU A 1 46  ? 20.225  -7.252  -53.262 1.00 28.13 ? 46  GLU A CA  1 
ATOM   328  C C   . GLU A 1 46  ? 19.107  -6.362  -52.726 1.00 27.55 ? 46  GLU A C   1 
ATOM   329  O O   . GLU A 1 46  ? 18.615  -6.578  -51.616 1.00 27.59 ? 46  GLU A O   1 
ATOM   330  C CB  . GLU A 1 46  ? 19.706  -8.131  -54.407 1.00 28.24 ? 46  GLU A CB  1 
ATOM   331  C CG  . GLU A 1 46  ? 18.884  -9.326  -53.949 1.00 29.46 ? 46  GLU A CG  1 
ATOM   332  C CD  . GLU A 1 46  ? 18.386  -10.156 -55.106 1.00 31.67 ? 46  GLU A CD  1 
ATOM   333  O OE1 . GLU A 1 46  ? 17.309  -9.832  -55.658 1.00 31.82 ? 46  GLU A OE1 1 
ATOM   334  O OE2 . GLU A 1 46  ? 19.071  -11.140 -55.459 1.00 33.21 ? 46  GLU A OE2 1 
ATOM   335  N N   . SER A 1 47  ? 18.708  -5.376  -53.526 1.00 26.74 ? 47  SER A N   1 
ATOM   336  C CA  . SER A 1 47  ? 17.669  -4.421  -53.152 1.00 26.00 ? 47  SER A CA  1 
ATOM   337  C C   . SER A 1 47  ? 16.273  -5.045  -53.166 1.00 25.66 ? 47  SER A C   1 
ATOM   338  O O   . SER A 1 47  ? 15.821  -5.550  -54.200 1.00 25.42 ? 47  SER A O   1 
ATOM   339  C CB  . SER A 1 47  ? 17.707  -3.217  -54.102 1.00 25.88 ? 47  SER A CB  1 
ATOM   340  O OG  . SER A 1 47  ? 16.685  -2.276  -53.764 1.00 25.65 ? 47  SER A OG  1 
ATOM   341  N N   . VAL A 1 48  ? 15.600  -5.006  -52.013 1.00 25.19 ? 48  VAL A N   1 
ATOM   342  C CA  . VAL A 1 48  ? 14.198  -5.426  -51.914 1.00 24.87 ? 48  VAL A CA  1 
ATOM   343  C C   . VAL A 1 48  ? 13.255  -4.223  -51.927 1.00 24.77 ? 48  VAL A C   1 
ATOM   344  O O   . VAL A 1 48  ? 12.030  -4.386  -51.858 1.00 24.69 ? 48  VAL A O   1 
ATOM   345  C CB  . VAL A 1 48  ? 13.909  -6.300  -50.656 1.00 24.69 ? 48  VAL A CB  1 
ATOM   346  C CG1 . VAL A 1 48  ? 14.579  -7.655  -50.765 1.00 24.53 ? 48  VAL A CG1 1 
ATOM   347  C CG2 . VAL A 1 48  ? 14.307  -5.579  -49.368 1.00 24.92 ? 48  VAL A CG2 1 
ATOM   348  N N   . ARG A 1 49  ? 13.830  -3.023  -52.022 1.00 24.67 ? 49  ARG A N   1 
ATOM   349  C CA  . ARG A 1 49  ? 13.058  -1.775  -52.016 1.00 24.80 ? 49  ARG A CA  1 
ATOM   350  C C   . ARG A 1 49  ? 11.879  -1.814  -52.995 1.00 25.00 ? 49  ARG A C   1 
ATOM   351  O O   . ARG A 1 49  ? 12.077  -1.890  -54.206 1.00 25.00 ? 49  ARG A O   1 
ATOM   352  C CB  . ARG A 1 49  ? 13.965  -0.577  -52.325 1.00 24.65 ? 49  ARG A CB  1 
ATOM   353  C CG  . ARG A 1 49  ? 13.251  0.774   -52.195 1.00 24.40 ? 49  ARG A CG  1 
ATOM   354  C CD  . ARG A 1 49  ? 14.216  1.954   -52.276 1.00 24.10 ? 49  ARG A CD  1 
ATOM   355  N NE  . ARG A 1 49  ? 15.323  1.875   -51.319 1.00 24.58 ? 49  ARG A NE  1 
ATOM   356  C CZ  . ARG A 1 49  ? 15.345  2.458   -50.121 1.00 24.87 ? 49  ARG A CZ  1 
ATOM   357  N NH1 . ARG A 1 49  ? 14.309  3.177   -49.690 1.00 25.29 ? 49  ARG A NH1 1 
ATOM   358  N NH2 . ARG A 1 49  ? 16.411  2.318   -49.346 1.00 24.22 ? 49  ARG A NH2 1 
ATOM   359  N N   . GLY A 1 50  ? 10.662  -1.787  -52.451 1.00 25.24 ? 50  GLY A N   1 
ATOM   360  C CA  . GLY A 1 50  ? 9.435   -1.721  -53.255 1.00 25.60 ? 50  GLY A CA  1 
ATOM   361  C C   . GLY A 1 50  ? 8.852   -3.049  -53.721 1.00 25.89 ? 50  GLY A C   1 
ATOM   362  O O   . GLY A 1 50  ? 7.849   -3.070  -54.446 1.00 25.84 ? 50  GLY A O   1 
ATOM   363  N N   . GLU A 1 51  ? 9.458   -4.154  -53.287 1.00 26.18 ? 51  GLU A N   1 
ATOM   364  C CA  . GLU A 1 51  ? 9.079   -5.489  -53.760 1.00 26.32 ? 51  GLU A CA  1 
ATOM   365  C C   . GLU A 1 51  ? 8.199   -6.310  -52.810 1.00 26.35 ? 51  GLU A C   1 
ATOM   366  O O   . GLU A 1 51  ? 8.057   -5.985  -51.629 1.00 26.39 ? 51  GLU A O   1 
ATOM   367  C CB  . GLU A 1 51  ? 10.331  -6.275  -54.139 1.00 26.40 ? 51  GLU A CB  1 
ATOM   368  C CG  . GLU A 1 51  ? 10.768  -6.017  -55.566 1.00 27.27 ? 51  GLU A CG  1 
ATOM   369  C CD  . GLU A 1 51  ? 12.262  -5.998  -55.727 1.00 28.59 ? 51  GLU A CD  1 
ATOM   370  O OE1 . GLU A 1 51  ? 12.929  -6.950  -55.268 1.00 29.05 ? 51  GLU A OE1 1 
ATOM   371  O OE2 . GLU A 1 51  ? 12.771  -5.026  -56.324 1.00 29.60 ? 51  GLU A OE2 1 
ATOM   372  N N   . ASP A 1 52  ? 7.613   -7.377  -53.362 1.00 26.35 ? 52  ASP A N   1 
ATOM   373  C CA  . ASP A 1 52  ? 6.769   -8.314  -52.626 1.00 26.30 ? 52  ASP A CA  1 
ATOM   374  C C   . ASP A 1 52  ? 7.621   -9.486  -52.124 1.00 26.25 ? 52  ASP A C   1 
ATOM   375  O O   . ASP A 1 52  ? 7.926   -10.423 -52.876 1.00 26.17 ? 52  ASP A O   1 
ATOM   376  C CB  . ASP A 1 52  ? 5.640   -8.813  -53.536 1.00 26.35 ? 52  ASP A CB  1 
ATOM   377  C CG  . ASP A 1 52  ? 4.462   -9.381  -52.763 1.00 26.96 ? 52  ASP A CG  1 
ATOM   378  O OD1 . ASP A 1 52  ? 3.635   -10.098 -53.377 1.00 26.66 ? 52  ASP A OD1 1 
ATOM   379  O OD2 . ASP A 1 52  ? 4.353   -9.109  -51.544 1.00 27.99 ? 52  ASP A OD2 1 
ATOM   380  N N   . VAL A 1 53  ? 8.008   -9.425  -50.852 1.00 26.12 ? 53  VAL A N   1 
ATOM   381  C CA  . VAL A 1 53  ? 8.971   -10.381 -50.292 1.00 26.04 ? 53  VAL A CA  1 
ATOM   382  C C   . VAL A 1 53  ? 8.301   -11.603 -49.661 1.00 26.05 ? 53  VAL A C   1 
ATOM   383  O O   . VAL A 1 53  ? 7.345   -11.478 -48.893 1.00 26.04 ? 53  VAL A O   1 
ATOM   384  C CB  . VAL A 1 53  ? 9.909   -9.712  -49.262 1.00 26.04 ? 53  VAL A CB  1 
ATOM   385  C CG1 . VAL A 1 53  ? 10.916  -10.717 -48.701 1.00 25.84 ? 53  VAL A CG1 1 
ATOM   386  C CG2 . VAL A 1 53  ? 10.630  -8.518  -49.888 1.00 25.98 ? 53  VAL A CG2 1 
ATOM   387  N N   . TYR A 1 54  ? 8.819   -12.781 -50.001 1.00 25.94 ? 54  TYR A N   1 
ATOM   388  C CA  . TYR A 1 54  ? 8.356   -14.035 -49.431 1.00 25.86 ? 54  TYR A CA  1 
ATOM   389  C C   . TYR A 1 54  ? 9.551   -14.787 -48.852 1.00 26.21 ? 54  TYR A C   1 
ATOM   390  O O   . TYR A 1 54  ? 10.405  -15.291 -49.592 1.00 26.20 ? 54  TYR A O   1 
ATOM   391  C CB  . TYR A 1 54  ? 7.639   -14.882 -50.493 1.00 25.66 ? 54  TYR A CB  1 
ATOM   392  C CG  . TYR A 1 54  ? 6.366   -14.258 -51.024 1.00 24.68 ? 54  TYR A CG  1 
ATOM   393  C CD1 . TYR A 1 54  ? 6.403   -13.278 -52.021 1.00 23.97 ? 54  TYR A CD1 1 
ATOM   394  C CD2 . TYR A 1 54  ? 5.121   -14.651 -50.533 1.00 24.10 ? 54  TYR A CD2 1 
ATOM   395  C CE1 . TYR A 1 54  ? 5.234   -12.700 -52.504 1.00 23.15 ? 54  TYR A CE1 1 
ATOM   396  C CE2 . TYR A 1 54  ? 3.944   -14.076 -51.007 1.00 23.47 ? 54  TYR A CE2 1 
ATOM   397  C CZ  . TYR A 1 54  ? 4.008   -13.103 -51.991 1.00 23.02 ? 54  TYR A CZ  1 
ATOM   398  O OH  . TYR A 1 54  ? 2.847   -12.543 -52.463 1.00 22.37 ? 54  TYR A OH  1 
ATOM   399  N N   . ILE A 1 55  ? 9.625   -14.840 -47.527 1.00 26.53 ? 55  ILE A N   1 
ATOM   400  C CA  . ILE A 1 55  ? 10.674  -15.608 -46.867 1.00 26.93 ? 55  ILE A CA  1 
ATOM   401  C C   . ILE A 1 55  ? 10.127  -16.986 -46.517 1.00 27.34 ? 55  ILE A C   1 
ATOM   402  O O   . ILE A 1 55  ? 9.114   -17.104 -45.818 1.00 27.18 ? 55  ILE A O   1 
ATOM   403  C CB  . ILE A 1 55  ? 11.223  -14.893 -45.609 1.00 26.79 ? 55  ILE A CB  1 
ATOM   404  C CG1 . ILE A 1 55  ? 11.732  -13.492 -45.971 1.00 26.89 ? 55  ILE A CG1 1 
ATOM   405  C CG2 . ILE A 1 55  ? 12.342  -15.711 -44.976 1.00 26.57 ? 55  ILE A CG2 1 
ATOM   406  C CD1 . ILE A 1 55  ? 11.768  -12.508 -44.804 1.00 26.42 ? 55  ILE A CD1 1 
ATOM   407  N N   . VAL A 1 56  ? 10.787  -18.022 -47.026 1.00 28.03 ? 56  VAL A N   1 
ATOM   408  C CA  . VAL A 1 56  ? 10.391  -19.395 -46.733 1.00 28.93 ? 56  VAL A CA  1 
ATOM   409  C C   . VAL A 1 56  ? 11.243  -19.964 -45.604 1.00 29.71 ? 56  VAL A C   1 
ATOM   410  O O   . VAL A 1 56  ? 12.470  -20.069 -45.716 1.00 29.77 ? 56  VAL A O   1 
ATOM   411  C CB  . VAL A 1 56  ? 10.471  -20.322 -47.978 1.00 28.90 ? 56  VAL A CB  1 
ATOM   412  C CG1 . VAL A 1 56  ? 9.981   -21.729 -47.630 1.00 28.74 ? 56  VAL A CG1 1 
ATOM   413  C CG2 . VAL A 1 56  ? 9.656   -19.751 -49.138 1.00 28.52 ? 56  VAL A CG2 1 
ATOM   414  N N   . GLN A 1 57  ? 10.582  -20.318 -44.510 1.00 30.70 ? 57  GLN A N   1 
ATOM   415  C CA  . GLN A 1 57  ? 11.262  -20.968 -43.407 1.00 31.84 ? 57  GLN A CA  1 
ATOM   416  C C   . GLN A 1 57  ? 10.835  -22.426 -43.300 1.00 32.37 ? 57  GLN A C   1 
ATOM   417  O O   . GLN A 1 57  ? 9.723   -22.740 -42.866 1.00 32.56 ? 57  GLN A O   1 
ATOM   418  C CB  . GLN A 1 57  ? 11.036  -20.214 -42.090 1.00 31.97 ? 57  GLN A CB  1 
ATOM   419  C CG  . GLN A 1 57  ? 11.990  -20.608 -40.958 1.00 32.71 ? 57  GLN A CG  1 
ATOM   420  C CD  . GLN A 1 57  ? 13.448  -20.558 -41.384 1.00 33.98 ? 57  GLN A CD  1 
ATOM   421  O OE1 . GLN A 1 57  ? 13.931  -21.460 -42.067 1.00 34.60 ? 57  GLN A OE1 1 
ATOM   422  N NE2 . GLN A 1 57  ? 14.156  -19.504 -40.981 1.00 34.10 ? 57  GLN A NE2 1 
ATOM   423  N N   . SER A 1 58  ? 11.738  -23.299 -43.733 1.00 33.13 ? 58  SER A N   1 
ATOM   424  C CA  . SER A 1 58  ? 11.592  -24.740 -43.612 1.00 33.65 ? 58  SER A CA  1 
ATOM   425  C C   . SER A 1 58  ? 12.715  -25.243 -42.709 1.00 33.91 ? 58  SER A C   1 
ATOM   426  O O   . SER A 1 58  ? 13.854  -24.773 -42.808 1.00 33.97 ? 58  SER A O   1 
ATOM   427  C CB  . SER A 1 58  ? 11.685  -25.390 -44.993 1.00 33.71 ? 58  SER A CB  1 
ATOM   428  O OG  . SER A 1 58  ? 11.408  -26.789 -44.923 1.00 34.44 ? 58  SER A OG  1 
ATOM   429  N N   . GLY A 1 59  ? 12.392  -26.182 -41.820 1.00 34.15 ? 59  GLY A N   1 
ATOM   430  C CA  . GLY A 1 59  ? 13.385  -26.737 -40.901 1.00 34.24 ? 59  GLY A CA  1 
ATOM   431  C C   . GLY A 1 59  ? 12.789  -27.513 -39.743 1.00 34.38 ? 59  GLY A C   1 
ATOM   432  O O   . GLY A 1 59  ? 12.445  -28.688 -39.887 1.00 34.55 ? 59  GLY A O   1 
ATOM   433  N N   . CYS A 1 60  ? 12.670  -26.844 -38.595 1.00 34.29 ? 60  CYS A N   1 
ATOM   434  C CA  . CYS A 1 60  ? 12.190  -27.451 -37.343 1.00 34.12 ? 60  CYS A CA  1 
ATOM   435  C C   . CYS A 1 60  ? 13.190  -28.479 -36.784 1.00 33.48 ? 60  CYS A C   1 
ATOM   436  O O   . CYS A 1 60  ? 12.802  -29.487 -36.188 1.00 33.58 ? 60  CYS A O   1 
ATOM   437  C CB  . CYS A 1 60  ? 10.791  -28.068 -37.522 1.00 34.21 ? 60  CYS A CB  1 
ATOM   438  S SG  . CYS A 1 60  ? 9.666   -27.761 -36.115 1.00 36.00 ? 60  CYS A SG  1 
ATOM   439  N N   . GLY A 1 61  ? 14.478  -28.213 -36.987 1.00 32.76 ? 61  GLY A N   1 
ATOM   440  C CA  . GLY A 1 61  ? 15.546  -29.047 -36.434 1.00 31.73 ? 61  GLY A CA  1 
ATOM   441  C C   . GLY A 1 61  ? 16.115  -28.410 -35.179 1.00 30.98 ? 61  GLY A C   1 
ATOM   442  O O   . GLY A 1 61  ? 16.406  -29.091 -34.191 1.00 31.16 ? 61  GLY A O   1 
ATOM   443  N N   . GLU A 1 62  ? 16.295  -27.094 -35.243 1.00 29.96 ? 62  GLU A N   1 
ATOM   444  C CA  . GLU A 1 62  ? 16.583  -26.283 -34.075 1.00 28.95 ? 62  GLU A CA  1 
ATOM   445  C C   . GLU A 1 62  ? 15.607  -25.104 -34.133 1.00 28.19 ? 62  GLU A C   1 
ATOM   446  O O   . GLU A 1 62  ? 15.870  -24.076 -34.773 1.00 28.10 ? 62  GLU A O   1 
ATOM   447  C CB  . GLU A 1 62  ? 18.044  -25.809 -34.070 1.00 29.05 ? 62  GLU A CB  1 
ATOM   448  C CG  . GLU A 1 62  ? 18.725  -25.858 -32.687 1.00 29.43 ? 62  GLU A CG  1 
ATOM   449  C CD  . GLU A 1 62  ? 18.139  -24.861 -31.663 1.00 30.23 ? 62  GLU A CD  1 
ATOM   450  O OE1 . GLU A 1 62  ? 18.836  -24.578 -30.667 1.00 30.02 ? 62  GLU A OE1 1 
ATOM   451  O OE2 . GLU A 1 62  ? 17.000  -24.359 -31.839 1.00 30.63 ? 62  GLU A OE2 1 
ATOM   452  N N   . ILE A 1 63  ? 14.471  -25.283 -33.464 1.00 27.14 ? 63  ILE A N   1 
ATOM   453  C CA  . ILE A 1 63  ? 13.312  -24.395 -33.591 1.00 26.10 ? 63  ILE A CA  1 
ATOM   454  C C   . ILE A 1 63  ? 13.562  -22.937 -33.168 1.00 25.51 ? 63  ILE A C   1 
ATOM   455  O O   . ILE A 1 63  ? 12.974  -22.026 -33.734 1.00 25.36 ? 63  ILE A O   1 
ATOM   456  C CB  . ILE A 1 63  ? 12.071  -24.991 -32.871 1.00 25.99 ? 63  ILE A CB  1 
ATOM   457  C CG1 . ILE A 1 63  ? 10.780  -24.301 -33.326 1.00 26.01 ? 63  ILE A CG1 1 
ATOM   458  C CG2 . ILE A 1 63  ? 12.234  -24.935 -31.355 1.00 25.80 ? 63  ILE A CG2 1 
ATOM   459  C CD1 . ILE A 1 63  ? 9.546   -25.183 -33.204 1.00 25.97 ? 63  ILE A CD1 1 
ATOM   460  N N   . ASN A 1 64  ? 14.435  -22.717 -32.190 1.00 24.93 ? 64  ASN A N   1 
ATOM   461  C CA  . ASN A 1 64  ? 14.760  -21.355 -31.769 1.00 24.45 ? 64  ASN A CA  1 
ATOM   462  C C   . ASN A 1 64  ? 15.688  -20.656 -32.758 1.00 24.59 ? 64  ASN A C   1 
ATOM   463  O O   . ASN A 1 64  ? 15.496  -19.475 -33.075 1.00 24.63 ? 64  ASN A O   1 
ATOM   464  C CB  . ASN A 1 64  ? 15.349  -21.346 -30.363 1.00 24.02 ? 64  ASN A CB  1 
ATOM   465  C CG  . ASN A 1 64  ? 14.441  -22.005 -29.358 1.00 22.78 ? 64  ASN A CG  1 
ATOM   466  O OD1 . ASN A 1 64  ? 13.229  -21.782 -29.358 1.00 20.91 ? 64  ASN A OD1 1 
ATOM   467  N ND2 . ASN A 1 64  ? 15.017  -22.836 -28.496 1.00 22.37 ? 64  ASN A ND2 1 
ATOM   468  N N   . ASP A 1 65  ? 16.682  -21.399 -33.244 1.00 24.55 ? 65  ASP A N   1 
ATOM   469  C CA  . ASP A 1 65  ? 17.562  -20.933 -34.309 1.00 24.42 ? 65  ASP A CA  1 
ATOM   470  C C   . ASP A 1 65  ? 16.762  -20.503 -35.533 1.00 24.45 ? 65  ASP A C   1 
ATOM   471  O O   . ASP A 1 65  ? 16.842  -19.350 -35.950 1.00 24.54 ? 65  ASP A O   1 
ATOM   472  C CB  . ASP A 1 65  ? 18.567  -22.024 -34.690 1.00 24.39 ? 65  ASP A CB  1 
ATOM   473  C CG  . ASP A 1 65  ? 19.651  -22.206 -33.649 1.00 24.05 ? 65  ASP A CG  1 
ATOM   474  O OD1 . ASP A 1 65  ? 19.836  -21.293 -32.819 1.00 23.38 ? 65  ASP A OD1 1 
ATOM   475  O OD2 . ASP A 1 65  ? 20.328  -23.257 -33.667 1.00 24.48 ? 65  ASP A OD2 1 
ATOM   476  N N   . ASN A 1 66  ? 15.971  -21.422 -36.084 1.00 24.33 ? 66  ASN A N   1 
ATOM   477  C CA  . ASN A 1 66  ? 15.189  -21.151 -37.293 1.00 24.34 ? 66  ASN A CA  1 
ATOM   478  C C   . ASN A 1 66  ? 14.154  -20.041 -37.129 1.00 23.94 ? 66  ASN A C   1 
ATOM   479  O O   . ASN A 1 66  ? 13.867  -19.309 -38.081 1.00 24.13 ? 66  ASN A O   1 
ATOM   480  C CB  . ASN A 1 66  ? 14.526  -22.433 -37.811 1.00 24.68 ? 66  ASN A CB  1 
ATOM   481  C CG  . ASN A 1 66  ? 15.542  -23.483 -38.242 1.00 25.84 ? 66  ASN A CG  1 
ATOM   482  O OD1 . ASN A 1 66  ? 16.754  -23.243 -38.227 1.00 27.41 ? 66  ASN A OD1 1 
ATOM   483  N ND2 . ASN A 1 66  ? 15.051  -24.655 -38.627 1.00 27.26 ? 66  ASN A ND2 1 
ATOM   484  N N   . LEU A 1 67  ? 13.601  -19.914 -35.924 1.00 23.28 ? 67  LEU A N   1 
ATOM   485  C CA  . LEU A 1 67  ? 12.639  -18.853 -35.653 1.00 22.70 ? 67  LEU A CA  1 
ATOM   486  C C   . LEU A 1 67  ? 13.338  -17.500 -35.624 1.00 22.61 ? 67  LEU A C   1 
ATOM   487  O O   . LEU A 1 67  ? 12.833  -16.531 -36.188 1.00 22.51 ? 67  LEU A O   1 
ATOM   488  C CB  . LEU A 1 67  ? 11.877  -19.122 -34.352 1.00 22.48 ? 67  LEU A CB  1 
ATOM   489  C CG  . LEU A 1 67  ? 10.565  -18.401 -33.995 1.00 21.58 ? 67  LEU A CG  1 
ATOM   490  C CD1 . LEU A 1 67  ? 10.748  -17.571 -32.747 1.00 20.81 ? 67  LEU A CD1 1 
ATOM   491  C CD2 . LEU A 1 67  ? 9.958   -17.558 -35.136 1.00 20.97 ? 67  LEU A CD2 1 
ATOM   492  N N   . MET A 1 68  ? 14.507  -17.441 -34.988 1.00 22.56 ? 68  MET A N   1 
ATOM   493  C CA  . MET A 1 68  ? 15.278  -16.202 -34.940 1.00 22.62 ? 68  MET A CA  1 
ATOM   494  C C   . MET A 1 68  ? 15.762  -15.785 -36.320 1.00 22.48 ? 68  MET A C   1 
ATOM   495  O O   . MET A 1 68  ? 15.682  -14.606 -36.682 1.00 22.47 ? 68  MET A O   1 
ATOM   496  C CB  . MET A 1 68  ? 16.450  -16.302 -33.964 1.00 22.63 ? 68  MET A CB  1 
ATOM   497  C CG  . MET A 1 68  ? 16.089  -15.906 -32.543 1.00 23.51 ? 68  MET A CG  1 
ATOM   498  S SD  . MET A 1 68  ? 15.191  -14.342 -32.428 1.00 27.18 ? 68  MET A SD  1 
ATOM   499  C CE  . MET A 1 68  ? 16.446  -13.145 -32.905 1.00 24.66 ? 68  MET A CE  1 
ATOM   500  N N   . GLU A 1 69  ? 16.246  -16.763 -37.084 1.00 22.35 ? 69  GLU A N   1 
ATOM   501  C CA  . GLU A 1 69  ? 16.709  -16.539 -38.449 1.00 22.28 ? 69  GLU A CA  1 
ATOM   502  C C   . GLU A 1 69  ? 15.609  -15.897 -39.313 1.00 21.92 ? 69  GLU A C   1 
ATOM   503  O O   . GLU A 1 69  ? 15.833  -14.868 -39.957 1.00 21.83 ? 69  GLU A O   1 
ATOM   504  C CB  . GLU A 1 69  ? 17.175  -17.858 -39.060 1.00 22.43 ? 69  GLU A CB  1 
ATOM   505  C CG  . GLU A 1 69  ? 17.962  -17.678 -40.346 1.00 23.77 ? 69  GLU A CG  1 
ATOM   506  C CD  . GLU A 1 69  ? 18.576  -18.960 -40.855 1.00 25.54 ? 69  GLU A CD  1 
ATOM   507  O OE1 . GLU A 1 69  ? 18.475  -20.010 -40.171 1.00 26.51 ? 69  GLU A OE1 1 
ATOM   508  O OE2 . GLU A 1 69  ? 19.164  -18.915 -41.964 1.00 26.32 ? 69  GLU A OE2 1 
ATOM   509  N N   . LEU A 1 70  ? 14.428  -16.511 -39.298 1.00 21.46 ? 70  LEU A N   1 
ATOM   510  C CA  . LEU A 1 70  ? 13.252  -15.996 -39.988 1.00 20.94 ? 70  LEU A CA  1 
ATOM   511  C C   . LEU A 1 70  ? 12.859  -14.594 -39.518 1.00 21.01 ? 70  LEU A C   1 
ATOM   512  O O   . LEU A 1 70  ? 12.577  -13.721 -40.346 1.00 21.15 ? 70  LEU A O   1 
ATOM   513  C CB  . LEU A 1 70  ? 12.074  -16.962 -39.811 1.00 20.73 ? 70  LEU A CB  1 
ATOM   514  C CG  . LEU A 1 70  ? 10.696  -16.559 -40.342 1.00 19.91 ? 70  LEU A CG  1 
ATOM   515  C CD1 . LEU A 1 70  ? 10.678  -16.440 -41.861 1.00 19.53 ? 70  LEU A CD1 1 
ATOM   516  C CD2 . LEU A 1 70  ? 9.666   -17.565 -39.889 1.00 19.54 ? 70  LEU A CD2 1 
ATOM   517  N N   . LEU A 1 71  ? 12.843  -14.376 -38.203 1.00 20.82 ? 71  LEU A N   1 
ATOM   518  C CA  . LEU A 1 71  ? 12.476  -13.065 -37.652 1.00 20.72 ? 71  LEU A CA  1 
ATOM   519  C C   . LEU A 1 71  ? 13.437  -11.963 -38.086 1.00 20.74 ? 71  LEU A C   1 
ATOM   520  O O   . LEU A 1 71  ? 13.008  -10.862 -38.423 1.00 20.64 ? 71  LEU A O   1 
ATOM   521  C CB  . LEU A 1 71  ? 12.388  -13.102 -36.122 1.00 20.61 ? 71  LEU A CB  1 
ATOM   522  C CG  . LEU A 1 71  ? 11.274  -13.936 -35.489 1.00 20.20 ? 71  LEU A CG  1 
ATOM   523  C CD1 . LEU A 1 71  ? 11.568  -14.115 -34.023 1.00 20.27 ? 71  LEU A CD1 1 
ATOM   524  C CD2 . LEU A 1 71  ? 9.896   -13.322 -35.693 1.00 20.24 ? 71  LEU A CD2 1 
ATOM   525  N N   . ILE A 1 72  ? 14.732  -12.275 -38.077 1.00 20.92 ? 72  ILE A N   1 
ATOM   526  C CA  . ILE A 1 72  ? 15.776  -11.325 -38.466 1.00 21.02 ? 72  ILE A CA  1 
ATOM   527  C C   . ILE A 1 72  ? 15.678  -10.964 -39.959 1.00 21.29 ? 72  ILE A C   1 
ATOM   528  O O   . ILE A 1 72  ? 15.813  -9.796  -40.336 1.00 21.24 ? 72  ILE A O   1 
ATOM   529  C CB  . ILE A 1 72  ? 17.186  -11.858 -38.076 1.00 20.87 ? 72  ILE A CB  1 
ATOM   530  C CG1 . ILE A 1 72  ? 17.408  -11.731 -36.560 1.00 20.43 ? 72  ILE A CG1 1 
ATOM   531  C CG2 . ILE A 1 72  ? 18.287  -11.117 -38.819 1.00 20.96 ? 72  ILE A CG2 1 
ATOM   532  C CD1 . ILE A 1 72  ? 18.450  -12.744 -36.015 1.00 18.61 ? 72  ILE A CD1 1 
ATOM   533  N N   . MET A 1 73  ? 15.420  -11.967 -40.796 1.00 21.58 ? 73  MET A N   1 
ATOM   534  C CA  . MET A 1 73  ? 15.236  -11.749 -42.229 1.00 21.91 ? 73  MET A CA  1 
ATOM   535  C C   . MET A 1 73  ? 14.049  -10.825 -42.518 1.00 21.94 ? 73  MET A C   1 
ATOM   536  O O   . MET A 1 73  ? 14.150  -9.930  -43.362 1.00 21.76 ? 73  MET A O   1 
ATOM   537  C CB  . MET A 1 73  ? 15.068  -13.077 -42.964 1.00 22.16 ? 73  MET A CB  1 
ATOM   538  C CG  . MET A 1 73  ? 16.332  -13.957 -42.948 1.00 23.44 ? 73  MET A CG  1 
ATOM   539  S SD  . MET A 1 73  ? 16.283  -15.184 -44.274 1.00 26.83 ? 73  MET A SD  1 
ATOM   540  C CE  . MET A 1 73  ? 16.463  -14.108 -45.708 1.00 25.89 ? 73  MET A CE  1 
ATOM   541  N N   . ILE A 1 74  ? 12.937  -11.045 -41.811 1.00 22.12 ? 74  ILE A N   1 
ATOM   542  C CA  . ILE A 1 74  ? 11.762  -10.167 -41.894 1.00 22.30 ? 74  ILE A CA  1 
ATOM   543  C C   . ILE A 1 74  ? 12.148  -8.732  -41.545 1.00 22.79 ? 74  ILE A C   1 
ATOM   544  O O   . ILE A 1 74  ? 11.858  -7.805  -42.308 1.00 22.75 ? 74  ILE A O   1 
ATOM   545  C CB  . ILE A 1 74  ? 10.606  -10.633 -40.967 1.00 22.04 ? 74  ILE A CB  1 
ATOM   546  C CG1 . ILE A 1 74  ? 10.049  -11.983 -41.429 1.00 22.01 ? 74  ILE A CG1 1 
ATOM   547  C CG2 . ILE A 1 74  ? 9.490   -9.610  -40.950 1.00 21.70 ? 74  ILE A CG2 1 
ATOM   548  C CD1 . ILE A 1 74  ? 9.176   -12.678 -40.405 1.00 21.40 ? 74  ILE A CD1 1 
ATOM   549  N N   . ASN A 1 75  ? 12.814  -8.556  -40.401 1.00 23.28 ? 75  ASN A N   1 
ATOM   550  C CA  . ASN A 1 75  ? 13.233  -7.231  -39.970 1.00 23.90 ? 75  ASN A CA  1 
ATOM   551  C C   . ASN A 1 75  ? 14.065  -6.553  -41.046 1.00 24.19 ? 75  ASN A C   1 
ATOM   552  O O   . ASN A 1 75  ? 13.741  -5.443  -41.474 1.00 24.15 ? 75  ASN A O   1 
ATOM   553  C CB  . ASN A 1 75  ? 14.009  -7.277  -38.650 1.00 24.01 ? 75  ASN A CB  1 
ATOM   554  C CG  . ASN A 1 75  ? 14.407  -5.888  -38.160 1.00 24.59 ? 75  ASN A CG  1 
ATOM   555  O OD1 . ASN A 1 75  ? 15.594  -5.577  -38.022 1.00 25.30 ? 75  ASN A OD1 1 
ATOM   556  N ND2 . ASN A 1 75  ? 13.411  -5.040  -37.916 1.00 24.73 ? 75  ASN A ND2 1 
ATOM   557  N N   . ALA A 1 76  ? 15.116  -7.244  -41.490 1.00 24.66 ? 76  ALA A N   1 
ATOM   558  C CA  . ALA A 1 76  ? 16.018  -6.736  -42.521 1.00 24.96 ? 76  ALA A CA  1 
ATOM   559  C C   . ALA A 1 76  ? 15.271  -6.237  -43.755 1.00 25.20 ? 76  ALA A C   1 
ATOM   560  O O   . ALA A 1 76  ? 15.503  -5.115  -44.201 1.00 25.36 ? 76  ALA A O   1 
ATOM   561  C CB  . ALA A 1 76  ? 17.049  -7.786  -42.894 1.00 24.90 ? 76  ALA A CB  1 
ATOM   562  N N   . CYS A 1 77  ? 14.362  -7.054  -44.283 1.00 25.60 ? 77  CYS A N   1 
ATOM   563  C CA  . CYS A 1 77  ? 13.578  -6.682  -45.471 1.00 26.07 ? 77  CYS A CA  1 
ATOM   564  C C   . CYS A 1 77  ? 12.640  -5.492  -45.232 1.00 26.43 ? 77  CYS A C   1 
ATOM   565  O O   . CYS A 1 77  ? 12.571  -4.578  -46.055 1.00 26.53 ? 77  CYS A O   1 
ATOM   566  C CB  . CYS A 1 77  ? 12.794  -7.885  -46.012 1.00 25.88 ? 77  CYS A CB  1 
ATOM   567  S SG  . CYS A 1 77  ? 13.850  -9.197  -46.664 1.00 25.72 ? 77  CYS A SG  1 
ATOM   568  N N   . LYS A 1 78  ? 11.936  -5.502  -44.103 1.00 26.88 ? 78  LYS A N   1 
ATOM   569  C CA  . LYS A 1 78  ? 11.006  -4.426  -43.757 1.00 27.33 ? 78  LYS A CA  1 
ATOM   570  C C   . LYS A 1 78  ? 11.752  -3.111  -43.529 1.00 27.44 ? 78  LYS A C   1 
ATOM   571  O O   . LYS A 1 78  ? 11.229  -2.027  -43.790 1.00 27.67 ? 78  LYS A O   1 
ATOM   572  C CB  . LYS A 1 78  ? 10.199  -4.797  -42.510 1.00 27.32 ? 78  LYS A CB  1 
ATOM   573  C CG  . LYS A 1 78  ? 8.859   -4.081  -42.396 1.00 28.31 ? 78  LYS A CG  1 
ATOM   574  C CD  . LYS A 1 78  ? 7.815   -4.687  -43.350 1.00 29.41 ? 78  LYS A CD  1 
ATOM   575  C CE  . LYS A 1 78  ? 6.445   -4.025  -43.214 1.00 29.64 ? 78  LYS A CE  1 
ATOM   576  N NZ  . LYS A 1 78  ? 5.937   -4.122  -41.780 1.00 30.40 ? 78  LYS A NZ  1 
ATOM   577  N N   . ILE A 1 79  ? 12.984  -3.227  -43.054 1.00 27.48 ? 79  ILE A N   1 
ATOM   578  C CA  . ILE A 1 79  ? 13.835  -2.080  -42.774 1.00 27.55 ? 79  ILE A CA  1 
ATOM   579  C C   . ILE A 1 79  ? 14.556  -1.573  -44.040 1.00 27.38 ? 79  ILE A C   1 
ATOM   580  O O   . ILE A 1 79  ? 15.109  -0.467  -44.056 1.00 27.30 ? 79  ILE A O   1 
ATOM   581  C CB  . ILE A 1 79  ? 14.763  -2.411  -41.567 1.00 27.70 ? 79  ILE A CB  1 
ATOM   582  C CG1 . ILE A 1 79  ? 14.355  -1.574  -40.346 1.00 28.20 ? 79  ILE A CG1 1 
ATOM   583  C CG2 . ILE A 1 79  ? 16.243  -2.289  -41.896 1.00 27.75 ? 79  ILE A CG2 1 
ATOM   584  C CD1 . ILE A 1 79  ? 14.603  -2.283  -39.019 1.00 29.94 ? 79  ILE A CD1 1 
ATOM   585  N N   . ALA A 1 80  ? 14.501  -2.377  -45.102 1.00 27.24 ? 80  ALA A N   1 
ATOM   586  C CA  . ALA A 1 80  ? 15.055  -2.018  -46.409 1.00 27.04 ? 80  ALA A CA  1 
ATOM   587  C C   . ALA A 1 80  ? 13.984  -1.661  -47.460 1.00 26.94 ? 80  ALA A C   1 
ATOM   588  O O   . ALA A 1 80  ? 14.194  -1.839  -48.664 1.00 26.94 ? 80  ALA A O   1 
ATOM   589  C CB  . ALA A 1 80  ? 15.970  -3.121  -46.913 1.00 27.03 ? 80  ALA A CB  1 
ATOM   590  N N   . SER A 1 81  ? 12.843  -1.158  -46.985 1.00 26.74 ? 81  SER A N   1 
ATOM   591  C CA  . SER A 1 81  ? 11.767  -0.604  -47.828 1.00 26.55 ? 81  SER A CA  1 
ATOM   592  C C   . SER A 1 81  ? 11.033  -1.612  -48.727 1.00 26.59 ? 81  SER A C   1 
ATOM   593  O O   . SER A 1 81  ? 10.423  -1.227  -49.732 1.00 26.68 ? 81  SER A O   1 
ATOM   594  C CB  . SER A 1 81  ? 12.257  0.598   -48.647 1.00 26.48 ? 81  SER A CB  1 
ATOM   595  O OG  . SER A 1 81  ? 12.542  1.707   -47.811 1.00 26.20 ? 81  SER A OG  1 
ATOM   596  N N   . ALA A 1 82  ? 11.076  -2.894  -48.362 1.00 26.48 ? 82  ALA A N   1 
ATOM   597  C CA  . ALA A 1 82  ? 10.216  -3.884  -49.005 1.00 26.39 ? 82  ALA A CA  1 
ATOM   598  C C   . ALA A 1 82  ? 8.771   -3.383  -48.970 1.00 26.30 ? 82  ALA A C   1 
ATOM   599  O O   . ALA A 1 82  ? 8.342   -2.787  -47.975 1.00 26.23 ? 82  ALA A O   1 
ATOM   600  C CB  . ALA A 1 82  ? 10.319  -5.220  -48.291 1.00 26.22 ? 82  ALA A CB  1 
ATOM   601  N N   . SER A 1 83  ? 8.041   -3.612  -50.062 1.00 26.23 ? 83  SER A N   1 
ATOM   602  C CA  . SER A 1 83  ? 6.630   -3.230  -50.167 1.00 26.12 ? 83  SER A CA  1 
ATOM   603  C C   . SER A 1 83  ? 5.768   -4.069  -49.236 1.00 26.11 ? 83  SER A C   1 
ATOM   604  O O   . SER A 1 83  ? 4.904   -3.546  -48.531 1.00 26.14 ? 83  SER A O   1 
ATOM   605  C CB  . SER A 1 83  ? 6.142   -3.386  -51.610 1.00 26.16 ? 83  SER A CB  1 
ATOM   606  O OG  . SER A 1 83  ? 4.730   -3.313  -51.693 1.00 26.12 ? 83  SER A OG  1 
ATOM   607  N N   . ARG A 1 84  ? 6.006   -5.376  -49.249 1.00 26.07 ? 84  ARG A N   1 
ATOM   608  C CA  . ARG A 1 84  ? 5.300   -6.306  -48.382 1.00 26.06 ? 84  ARG A CA  1 
ATOM   609  C C   . ARG A 1 84  ? 6.265   -7.408  -47.973 1.00 25.64 ? 84  ARG A C   1 
ATOM   610  O O   . ARG A 1 84  ? 7.125   -7.814  -48.759 1.00 25.67 ? 84  ARG A O   1 
ATOM   611  C CB  . ARG A 1 84  ? 4.097   -6.910  -49.112 1.00 26.35 ? 84  ARG A CB  1 
ATOM   612  C CG  . ARG A 1 84  ? 2.797   -6.875  -48.312 1.00 27.78 ? 84  ARG A CG  1 
ATOM   613  C CD  . ARG A 1 84  ? 1.764   -7.925  -48.763 1.00 30.30 ? 84  ARG A CD  1 
ATOM   614  N NE  . ARG A 1 84  ? 1.748   -8.160  -50.213 1.00 32.08 ? 84  ARG A NE  1 
ATOM   615  C CZ  . ARG A 1 84  ? 0.760   -8.764  -50.873 1.00 32.71 ? 84  ARG A CZ  1 
ATOM   616  N NH1 . ARG A 1 84  ? -0.322  -9.182  -50.226 1.00 33.06 ? 84  ARG A NH1 1 
ATOM   617  N NH2 . ARG A 1 84  ? 0.849   -8.940  -52.188 1.00 32.90 ? 84  ARG A NH2 1 
ATOM   618  N N   . VAL A 1 85  ? 6.134   -7.878  -46.736 1.00 25.15 ? 85  VAL A N   1 
ATOM   619  C CA  . VAL A 1 85  ? 6.920   -9.016  -46.271 1.00 24.74 ? 85  VAL A CA  1 
ATOM   620  C C   . VAL A 1 85  ? 5.966   -10.116 -45.812 1.00 24.47 ? 85  VAL A C   1 
ATOM   621  O O   . VAL A 1 85  ? 5.124   -9.892  -44.941 1.00 24.31 ? 85  VAL A O   1 
ATOM   622  C CB  . VAL A 1 85  ? 7.920   -8.633  -45.146 1.00 24.71 ? 85  VAL A CB  1 
ATOM   623  C CG1 . VAL A 1 85  ? 8.866   -9.791  -44.848 1.00 24.97 ? 85  VAL A CG1 1 
ATOM   624  C CG2 . VAL A 1 85  ? 8.719   -7.387  -45.520 1.00 24.37 ? 85  VAL A CG2 1 
ATOM   625  N N   . THR A 1 86  ? 6.103   -11.295 -46.421 1.00 24.15 ? 86  THR A N   1 
ATOM   626  C CA  . THR A 1 86  ? 5.225   -12.434 -46.160 1.00 23.96 ? 86  THR A CA  1 
ATOM   627  C C   . THR A 1 86  ? 6.043   -13.601 -45.633 1.00 23.76 ? 86  THR A C   1 
ATOM   628  O O   . THR A 1 86  ? 7.046   -13.983 -46.233 1.00 23.93 ? 86  THR A O   1 
ATOM   629  C CB  . THR A 1 86  ? 4.483   -12.879 -47.443 1.00 23.93 ? 86  THR A CB  1 
ATOM   630  O OG1 . THR A 1 86  ? 3.569   -11.854 -47.861 1.00 24.79 ? 86  THR A OG1 1 
ATOM   631  C CG2 . THR A 1 86  ? 3.715   -14.179 -47.224 1.00 23.69 ? 86  THR A CG2 1 
ATOM   632  N N   . ALA A 1 87  ? 5.611   -14.162 -44.508 1.00 23.48 ? 87  ALA A N   1 
ATOM   633  C CA  . ALA A 1 87  ? 6.282   -15.313 -43.929 1.00 23.17 ? 87  ALA A CA  1 
ATOM   634  C C   . ALA A 1 87  ? 5.618   -16.597 -44.395 1.00 23.12 ? 87  ALA A C   1 
ATOM   635  O O   . ALA A 1 87  ? 4.419   -16.813 -44.193 1.00 22.85 ? 87  ALA A O   1 
ATOM   636  C CB  . ALA A 1 87  ? 6.289   -15.233 -42.408 1.00 23.16 ? 87  ALA A CB  1 
ATOM   637  N N   . VAL A 1 88  ? 6.415   -17.438 -45.042 1.00 23.13 ? 88  VAL A N   1 
ATOM   638  C CA  . VAL A 1 88  ? 5.975   -18.754 -45.446 1.00 22.95 ? 88  VAL A CA  1 
ATOM   639  C C   . VAL A 1 88  ? 6.528   -19.735 -44.413 1.00 23.04 ? 88  VAL A C   1 
ATOM   640  O O   . VAL A 1 88  ? 7.716   -20.076 -44.423 1.00 22.71 ? 88  VAL A O   1 
ATOM   641  C CB  . VAL A 1 88  ? 6.444   -19.098 -46.877 1.00 22.74 ? 88  VAL A CB  1 
ATOM   642  C CG1 . VAL A 1 88  ? 5.710   -20.318 -47.394 1.00 22.61 ? 88  VAL A CG1 1 
ATOM   643  C CG2 . VAL A 1 88  ? 6.194   -17.925 -47.811 1.00 22.80 ? 88  VAL A CG2 1 
ATOM   644  N N   . ILE A 1 89  ? 5.664   -20.148 -43.490 1.00 23.27 ? 89  ILE A N   1 
ATOM   645  C CA  . ILE A 1 89  ? 6.046   -21.138 -42.492 1.00 23.66 ? 89  ILE A CA  1 
ATOM   646  C C   . ILE A 1 89  ? 5.167   -22.386 -42.633 1.00 23.89 ? 89  ILE A C   1 
ATOM   647  O O   . ILE A 1 89  ? 4.132   -22.490 -41.972 1.00 23.70 ? 89  ILE A O   1 
ATOM   648  C CB  . ILE A 1 89  ? 5.970   -20.589 -41.044 1.00 23.63 ? 89  ILE A CB  1 
ATOM   649  C CG1 . ILE A 1 89  ? 6.001   -19.057 -41.010 1.00 23.42 ? 89  ILE A CG1 1 
ATOM   650  C CG2 . ILE A 1 89  ? 7.106   -21.160 -40.209 1.00 24.17 ? 89  ILE A CG2 1 
ATOM   651  C CD1 . ILE A 1 89  ? 5.306   -18.466 -39.797 1.00 23.05 ? 89  ILE A CD1 1 
ATOM   652  N N   . PRO A 1 90  ? 5.573   -23.333 -43.508 1.00 24.26 ? 90  PRO A N   1 
ATOM   653  C CA  . PRO A 1 90  ? 4.843   -24.588 -43.699 1.00 24.54 ? 90  PRO A CA  1 
ATOM   654  C C   . PRO A 1 90  ? 4.429   -25.233 -42.372 1.00 24.89 ? 90  PRO A C   1 
ATOM   655  O O   . PRO A 1 90  ? 3.271   -25.632 -42.216 1.00 25.02 ? 90  PRO A O   1 
ATOM   656  C CB  . PRO A 1 90  ? 5.861   -25.464 -44.432 1.00 24.50 ? 90  PRO A CB  1 
ATOM   657  C CG  . PRO A 1 90  ? 6.646   -24.500 -45.232 1.00 24.25 ? 90  PRO A CG  1 
ATOM   658  C CD  . PRO A 1 90  ? 6.763   -23.262 -44.383 1.00 24.28 ? 90  PRO A CD  1 
ATOM   659  N N   . CYS A 1 91  ? 5.369   -25.319 -41.432 1.00 25.04 ? 91  CYS A N   1 
ATOM   660  C CA  . CYS A 1 91  ? 5.081   -25.783 -40.080 1.00 25.22 ? 91  CYS A CA  1 
ATOM   661  C C   . CYS A 1 91  ? 5.266   -24.628 -39.092 1.00 24.99 ? 91  CYS A C   1 
ATOM   662  O O   . CYS A 1 91  ? 6.379   -24.125 -38.909 1.00 24.93 ? 91  CYS A O   1 
ATOM   663  C CB  . CYS A 1 91  ? 5.991   -26.957 -39.710 1.00 25.35 ? 91  CYS A CB  1 
ATOM   664  S SG  . CYS A 1 91  ? 5.581   -27.760 -38.147 1.00 26.76 ? 91  CYS A SG  1 
ATOM   665  N N   . PHE A 1 92  ? 4.169   -24.211 -38.462 1.00 24.85 ? 92  PHE A N   1 
ATOM   666  C CA  . PHE A 1 92  ? 4.192   -23.089 -37.531 1.00 24.70 ? 92  PHE A CA  1 
ATOM   667  C C   . PHE A 1 92  ? 4.826   -23.504 -36.199 1.00 24.46 ? 92  PHE A C   1 
ATOM   668  O O   . PHE A 1 92  ? 4.295   -24.383 -35.521 1.00 24.44 ? 92  PHE A O   1 
ATOM   669  C CB  . PHE A 1 92  ? 2.774   -22.554 -37.313 1.00 24.87 ? 92  PHE A CB  1 
ATOM   670  C CG  . PHE A 1 92  ? 2.727   -21.172 -36.725 1.00 25.42 ? 92  PHE A CG  1 
ATOM   671  C CD1 . PHE A 1 92  ? 2.795   -20.053 -37.545 1.00 25.71 ? 92  PHE A CD1 1 
ATOM   672  C CD2 . PHE A 1 92  ? 2.612   -20.988 -35.346 1.00 26.09 ? 92  PHE A CD2 1 
ATOM   673  C CE1 . PHE A 1 92  ? 2.753   -18.774 -37.003 1.00 26.00 ? 92  PHE A CE1 1 
ATOM   674  C CE2 . PHE A 1 92  ? 2.568   -19.712 -34.795 1.00 25.57 ? 92  PHE A CE2 1 
ATOM   675  C CZ  . PHE A 1 92  ? 2.638   -18.606 -35.623 1.00 25.78 ? 92  PHE A CZ  1 
ATOM   676  N N   . PRO A 1 93  ? 5.971   -22.880 -35.831 1.00 24.32 ? 93  PRO A N   1 
ATOM   677  C CA  . PRO A 1 93  ? 6.690   -23.195 -34.588 1.00 24.13 ? 93  PRO A CA  1 
ATOM   678  C C   . PRO A 1 93  ? 5.878   -22.885 -33.331 1.00 24.08 ? 93  PRO A C   1 
ATOM   679  O O   . PRO A 1 93  ? 5.135   -21.894 -33.304 1.00 23.91 ? 93  PRO A O   1 
ATOM   680  C CB  . PRO A 1 93  ? 7.926   -22.286 -34.650 1.00 23.99 ? 93  PRO A CB  1 
ATOM   681  C CG  . PRO A 1 93  ? 7.566   -21.204 -35.587 1.00 24.17 ? 93  PRO A CG  1 
ATOM   682  C CD  . PRO A 1 93  ? 6.657   -21.823 -36.598 1.00 24.23 ? 93  PRO A CD  1 
ATOM   683  N N   . TYR A 1 94  ? 6.024   -23.739 -32.316 1.00 24.02 ? 94  TYR A N   1 
ATOM   684  C CA  . TYR A 1 94  ? 5.315   -23.620 -31.028 1.00 24.30 ? 94  TYR A CA  1 
ATOM   685  C C   . TYR A 1 94  ? 3.787   -23.709 -31.143 1.00 24.88 ? 94  TYR A C   1 
ATOM   686  O O   . TYR A 1 94  ? 3.061   -23.293 -30.232 1.00 24.77 ? 94  TYR A O   1 
ATOM   687  C CB  . TYR A 1 94  ? 5.745   -22.352 -30.265 1.00 23.90 ? 94  TYR A CB  1 
ATOM   688  C CG  . TYR A 1 94  ? 7.164   -22.422 -29.741 1.00 23.48 ? 94  TYR A CG  1 
ATOM   689  C CD1 . TYR A 1 94  ? 7.431   -22.867 -28.444 1.00 22.50 ? 94  TYR A CD1 1 
ATOM   690  C CD2 . TYR A 1 94  ? 8.244   -22.056 -30.546 1.00 22.40 ? 94  TYR A CD2 1 
ATOM   691  C CE1 . TYR A 1 94  ? 8.734   -22.940 -27.964 1.00 21.58 ? 94  TYR A CE1 1 
ATOM   692  C CE2 . TYR A 1 94  ? 9.549   -22.124 -30.075 1.00 21.80 ? 94  TYR A CE2 1 
ATOM   693  C CZ  . TYR A 1 94  ? 9.789   -22.567 -28.785 1.00 21.50 ? 94  TYR A CZ  1 
ATOM   694  O OH  . TYR A 1 94  ? 11.090  -22.640 -28.325 1.00 20.70 ? 94  TYR A OH  1 
ATOM   695  N N   . ALA A 1 95  ? 3.313   -24.286 -32.247 1.00 25.66 ? 95  ALA A N   1 
ATOM   696  C CA  . ALA A 1 95  ? 1.882   -24.366 -32.535 1.00 26.48 ? 95  ALA A CA  1 
ATOM   697  C C   . ALA A 1 95  ? 1.099   -25.204 -31.525 1.00 27.08 ? 95  ALA A C   1 
ATOM   698  O O   . ALA A 1 95  ? -0.090  -24.962 -31.320 1.00 27.26 ? 95  ALA A O   1 
ATOM   699  C CB  . ALA A 1 95  ? 1.645   -24.879 -33.951 1.00 26.40 ? 95  ALA A CB  1 
ATOM   700  N N   . ARG A 1 96  ? 1.755   -26.186 -30.906 1.00 27.83 ? 96  ARG A N   1 
ATOM   701  C CA  . ARG A 1 96  ? 1.110   -26.997 -29.869 1.00 28.63 ? 96  ARG A CA  1 
ATOM   702  C C   . ARG A 1 96  ? 0.788   -26.196 -28.614 1.00 28.91 ? 96  ARG A C   1 
ATOM   703  O O   . ARG A 1 96  ? -0.169  -26.510 -27.911 1.00 29.00 ? 96  ARG A O   1 
ATOM   704  C CB  . ARG A 1 96  ? 1.959   -28.212 -29.496 1.00 28.78 ? 96  ARG A CB  1 
ATOM   705  C CG  . ARG A 1 96  ? 1.582   -29.506 -30.248 1.00 30.18 ? 96  ARG A CG  1 
ATOM   706  C CD  . ARG A 1 96  ? 2.609   -30.596 -29.957 1.00 32.52 ? 96  ARG A CD  1 
ATOM   707  N NE  . ARG A 1 96  ? 3.970   -30.107 -30.185 1.00 34.64 ? 96  ARG A NE  1 
ATOM   708  C CZ  . ARG A 1 96  ? 5.061   -30.869 -30.195 1.00 35.72 ? 96  ARG A CZ  1 
ATOM   709  N NH1 . ARG A 1 96  ? 4.970   -32.181 -29.998 1.00 36.01 ? 96  ARG A NH1 1 
ATOM   710  N NH2 . ARG A 1 96  ? 6.250   -30.312 -30.409 1.00 35.70 ? 96  ARG A NH2 1 
ATOM   711  N N   . GLN A 1 97  ? 1.592   -25.172 -28.336 1.00 29.37 ? 97  GLN A N   1 
ATOM   712  C CA  . GLN A 1 97  ? 1.377   -24.318 -27.168 1.00 29.68 ? 97  GLN A CA  1 
ATOM   713  C C   . GLN A 1 97  ? 0.428   -23.166 -27.483 1.00 29.77 ? 97  GLN A C   1 
ATOM   714  O O   . GLN A 1 97  ? 0.841   -22.006 -27.614 1.00 29.71 ? 97  GLN A O   1 
ATOM   715  C CB  . GLN A 1 97  ? 2.707   -23.817 -26.610 1.00 29.78 ? 97  GLN A CB  1 
ATOM   716  C CG  . GLN A 1 97  ? 3.441   -24.866 -25.797 1.00 30.22 ? 97  GLN A CG  1 
ATOM   717  C CD  . GLN A 1 97  ? 4.931   -24.635 -25.780 1.00 30.95 ? 97  GLN A CD  1 
ATOM   718  O OE1 . GLN A 1 97  ? 5.413   -23.636 -25.236 1.00 31.29 ? 97  GLN A OE1 1 
ATOM   719  N NE2 . GLN A 1 97  ? 5.678   -25.565 -26.373 1.00 31.01 ? 97  GLN A NE2 1 
ATOM   720  N N   . ASP A 1 98  ? -0.852  -23.513 -27.597 1.00 29.99 ? 98  ASP A N   1 
ATOM   721  C CA  . ASP A 1 98  ? -1.902  -22.568 -27.966 1.00 30.37 ? 98  ASP A CA  1 
ATOM   722  C C   . ASP A 1 98  ? -2.913  -22.326 -26.839 1.00 30.61 ? 98  ASP A C   1 
ATOM   723  O O   . ASP A 1 98  ? -3.867  -21.554 -27.008 1.00 30.72 ? 98  ASP A O   1 
ATOM   724  C CB  . ASP A 1 98  ? -2.606  -23.020 -29.260 1.00 30.31 ? 98  ASP A CB  1 
ATOM   725  C CG  . ASP A 1 98  ? -3.070  -24.477 -29.217 1.00 30.49 ? 98  ASP A CG  1 
ATOM   726  O OD1 . ASP A 1 98  ? -2.528  -25.273 -28.426 1.00 30.60 ? 98  ASP A OD1 1 
ATOM   727  O OD2 . ASP A 1 98  ? -3.982  -24.835 -29.992 1.00 30.56 ? 98  ASP A OD2 1 
ATOM   728  N N   . LYS A 1 99  ? -2.686  -22.975 -25.691 1.00 30.91 ? 99  LYS A N   1 
ATOM   729  C CA  . LYS A 1 99  ? -3.570  -22.866 -24.519 1.00 31.15 ? 99  LYS A CA  1 
ATOM   730  C C   . LYS A 1 99  ? -2.845  -23.169 -23.202 1.00 31.36 ? 99  LYS A C   1 
ATOM   731  O O   . LYS A 1 99  ? -1.906  -23.962 -23.167 1.00 31.25 ? 99  LYS A O   1 
ATOM   732  C CB  . LYS A 1 99  ? -4.787  -23.783 -24.676 1.00 31.03 ? 99  LYS A CB  1 
ATOM   733  C CG  . LYS A 1 99  ? -4.443  -25.255 -24.849 1.00 31.35 ? 99  LYS A CG  1 
ATOM   734  C CD  . LYS A 1 99  ? -5.665  -26.091 -25.203 1.00 32.21 ? 99  LYS A CD  1 
ATOM   735  C CE  . LYS A 1 99  ? -5.275  -27.572 -25.359 1.00 32.68 ? 99  LYS A CE  1 
ATOM   736  N NZ  . LYS A 1 99  ? -4.340  -27.778 -26.535 1.00 32.94 ? 99  LYS A NZ  1 
ATOM   737  N N   . LYS A 1 100 ? -3.298  -22.537 -22.121 1.00 31.83 ? 100 LYS A N   1 
ATOM   738  C CA  . LYS A 1 100 ? -2.705  -22.722 -20.791 1.00 32.19 ? 100 LYS A CA  1 
ATOM   739  C C   . LYS A 1 100 ? -2.881  -24.147 -20.284 1.00 32.72 ? 100 LYS A C   1 
ATOM   740  O O   . LYS A 1 100 ? -1.996  -24.684 -19.610 1.00 32.79 ? 100 LYS A O   1 
ATOM   741  C CB  . LYS A 1 100 ? -3.339  -21.767 -19.780 1.00 32.13 ? 100 LYS A CB  1 
ATOM   742  C CG  . LYS A 1 100 ? -2.969  -20.306 -19.962 1.00 31.42 ? 100 LYS A CG  1 
ATOM   743  C CD  . LYS A 1 100 ? -3.606  -19.507 -18.838 1.00 30.32 ? 100 LYS A CD  1 
ATOM   744  C CE  . LYS A 1 100 ? -3.289  -18.040 -18.973 1.00 29.33 ? 100 LYS A CE  1 
ATOM   745  N NZ  . LYS A 1 100 ? -4.050  -17.187 -18.015 1.00 29.18 ? 100 LYS A NZ  1 
ATOM   746  N N   . ASP A 1 101 ? -4.040  -24.732 -20.597 1.00 33.27 ? 101 ASP A N   1 
ATOM   747  C CA  . ASP A 1 101 ? -4.378  -26.122 -20.262 1.00 33.70 ? 101 ASP A CA  1 
ATOM   748  C C   . ASP A 1 101 ? -4.337  -26.413 -18.752 1.00 33.69 ? 101 ASP A C   1 
ATOM   749  O O   . ASP A 1 101 ? -3.753  -27.425 -18.318 1.00 33.66 ? 101 ASP A O   1 
ATOM   750  C CB  . ASP A 1 101 ? -3.505  -27.111 -21.062 1.00 33.95 ? 101 ASP A CB  1 
ATOM   751  C CG  . ASP A 1 101 ? -4.183  -28.462 -21.269 1.00 34.85 ? 101 ASP A CG  1 
ATOM   752  O OD1 . ASP A 1 101 ? -5.310  -28.494 -21.819 1.00 35.75 ? 101 ASP A OD1 1 
ATOM   753  O OD2 . ASP A 1 101 ? -3.582  -29.498 -20.889 1.00 36.18 ? 101 ASP A OD2 1 
ATOM   754  N N   . LYS A 1 102 ? -4.963  -25.516 -17.967 1.00 33.68 ? 102 LYS A N   1 
ATOM   755  C CA  . LYS A 1 102 ? -5.115  -25.709 -16.512 1.00 33.63 ? 102 LYS A CA  1 
ATOM   756  C C   . LYS A 1 102 ? -3.807  -25.621 -15.715 1.00 33.29 ? 102 LYS A C   1 
ATOM   757  O O   . LYS A 1 102 ? -3.617  -26.354 -14.741 1.00 33.46 ? 102 LYS A O   1 
ATOM   758  C CB  . LYS A 1 102 ? -5.793  -27.052 -16.215 1.00 33.85 ? 102 LYS A CB  1 
ATOM   759  C CG  . LYS A 1 102 ? -7.296  -27.010 -16.108 1.00 34.66 ? 102 LYS A CG  1 
ATOM   760  C CD  . LYS A 1 102 ? -7.839  -28.429 -16.066 1.00 36.23 ? 102 LYS A CD  1 
ATOM   761  C CE  . LYS A 1 102 ? -9.003  -28.547 -15.104 1.00 37.35 ? 102 LYS A CE  1 
ATOM   762  N NZ  . LYS A 1 102 ? -9.649  -29.910 -15.180 1.00 38.22 ? 102 LYS A NZ  1 
ATOM   763  N N   . SER A 1 103 ? -2.912  -24.727 -16.130 1.00 32.73 ? 103 SER A N   1 
ATOM   764  C CA  . SER A 1 103 ? -1.655  -24.490 -15.413 1.00 32.07 ? 103 SER A CA  1 
ATOM   765  C C   . SER A 1 103 ? -1.069  -23.123 -15.755 1.00 31.34 ? 103 SER A C   1 
ATOM   766  O O   . SER A 1 103 ? -1.512  -22.473 -16.701 1.00 31.34 ? 103 SER A O   1 
ATOM   767  C CB  . SER A 1 103 ? -0.635  -25.601 -15.702 1.00 32.23 ? 103 SER A CB  1 
ATOM   768  O OG  . SER A 1 103 ? -0.406  -25.741 -17.092 1.00 32.77 ? 103 SER A OG  1 
ATOM   769  N N   . ARG A 1 104 ? -0.080  -22.689 -14.973 1.00 30.46 ? 104 ARG A N   1 
ATOM   770  C CA  . ARG A 1 104 ? 0.576   -21.402 -15.206 1.00 29.59 ? 104 ARG A CA  1 
ATOM   771  C C   . ARG A 1 104 ? 1.611   -21.517 -16.323 1.00 29.05 ? 104 ARG A C   1 
ATOM   772  O O   . ARG A 1 104 ? 2.820   -21.363 -16.106 1.00 28.91 ? 104 ARG A O   1 
ATOM   773  C CB  . ARG A 1 104 ? 1.197   -20.860 -13.917 1.00 29.64 ? 104 ARG A CB  1 
ATOM   774  C CG  . ARG A 1 104 ? 0.177   -20.568 -12.844 1.00 29.44 ? 104 ARG A CG  1 
ATOM   775  C CD  . ARG A 1 104 ? 0.837   -20.264 -11.523 1.00 29.14 ? 104 ARG A CD  1 
ATOM   776  N NE  . ARG A 1 104 ? -0.059  -20.596 -10.420 1.00 28.90 ? 104 ARG A NE  1 
ATOM   777  C CZ  . ARG A 1 104 ? 0.059   -21.681 -9.661  1.00 28.91 ? 104 ARG A CZ  1 
ATOM   778  N NH1 . ARG A 1 104 ? 1.048   -22.543 -9.866  1.00 28.56 ? 104 ARG A NH1 1 
ATOM   779  N NH2 . ARG A 1 104 ? -0.812  -21.896 -8.686  1.00 30.07 ? 104 ARG A NH2 1 
ATOM   780  N N   . ALA A 1 105 ? 1.102   -21.800 -17.520 1.00 28.32 ? 105 ALA A N   1 
ATOM   781  C CA  . ALA A 1 105 ? 1.906   -21.994 -18.716 1.00 27.64 ? 105 ALA A CA  1 
ATOM   782  C C   . ALA A 1 105 ? 1.770   -20.773 -19.615 1.00 27.03 ? 105 ALA A C   1 
ATOM   783  O O   . ALA A 1 105 ? 0.812   -20.014 -19.481 1.00 26.95 ? 105 ALA A O   1 
ATOM   784  C CB  . ALA A 1 105 ? 1.448   -23.251 -19.450 1.00 27.60 ? 105 ALA A CB  1 
ATOM   785  N N   . PRO A 1 106 ? 2.744   -20.559 -20.519 1.00 26.38 ? 106 PRO A N   1 
ATOM   786  C CA  . PRO A 1 106 ? 2.601   -19.481 -21.484 1.00 25.88 ? 106 PRO A CA  1 
ATOM   787  C C   . PRO A 1 106 ? 1.780   -19.955 -22.671 1.00 25.45 ? 106 PRO A C   1 
ATOM   788  O O   . PRO A 1 106 ? 1.653   -21.164 -22.892 1.00 25.52 ? 106 PRO A O   1 
ATOM   789  C CB  . PRO A 1 106 ? 4.044   -19.229 -21.933 1.00 25.98 ? 106 PRO A CB  1 
ATOM   790  C CG  . PRO A 1 106 ? 4.686   -20.564 -21.831 1.00 26.07 ? 106 PRO A CG  1 
ATOM   791  C CD  . PRO A 1 106 ? 4.024   -21.276 -20.684 1.00 26.36 ? 106 PRO A CD  1 
ATOM   792  N N   . ILE A 1 107 ? 1.210   -19.017 -23.416 1.00 24.83 ? 107 ILE A N   1 
ATOM   793  C CA  . ILE A 1 107 ? 0.657   -19.350 -24.720 1.00 24.19 ? 107 ILE A CA  1 
ATOM   794  C C   . ILE A 1 107 ? 1.718   -18.940 -25.738 1.00 23.83 ? 107 ILE A C   1 
ATOM   795  O O   . ILE A 1 107 ? 1.740   -17.806 -26.221 1.00 23.94 ? 107 ILE A O   1 
ATOM   796  C CB  . ILE A 1 107 ? -0.717  -18.693 -24.960 1.00 24.13 ? 107 ILE A CB  1 
ATOM   797  C CG1 . ILE A 1 107 ? -1.685  -19.113 -23.846 1.00 24.16 ? 107 ILE A CG1 1 
ATOM   798  C CG2 . ILE A 1 107 ? -1.268  -19.094 -26.329 1.00 23.97 ? 107 ILE A CG2 1 
ATOM   799  C CD1 . ILE A 1 107 ? -2.966  -18.311 -23.774 1.00 24.28 ? 107 ILE A CD1 1 
ATOM   800  N N   . SER A 1 108 ? 2.617   -19.875 -26.026 1.00 23.23 ? 108 SER A N   1 
ATOM   801  C CA  . SER A 1 108 ? 3.801   -19.596 -26.826 1.00 22.86 ? 108 SER A CA  1 
ATOM   802  C C   . SER A 1 108 ? 3.520   -19.369 -28.314 1.00 22.50 ? 108 SER A C   1 
ATOM   803  O O   . SER A 1 108 ? 4.267   -18.652 -28.978 1.00 22.60 ? 108 SER A O   1 
ATOM   804  C CB  . SER A 1 108 ? 4.864   -20.681 -26.622 1.00 23.06 ? 108 SER A CB  1 
ATOM   805  O OG  . SER A 1 108 ? 5.243   -20.775 -25.258 1.00 23.04 ? 108 SER A OG  1 
ATOM   806  N N   . ALA A 1 109 ? 2.452   -19.966 -28.839 1.00 21.94 ? 109 ALA A N   1 
ATOM   807  C CA  . ALA A 1 109 ? 2.059   -19.713 -30.230 1.00 21.41 ? 109 ALA A CA  1 
ATOM   808  C C   . ALA A 1 109 ? 1.530   -18.286 -30.449 1.00 21.12 ? 109 ALA A C   1 
ATOM   809  O O   . ALA A 1 109 ? 1.537   -17.784 -31.578 1.00 21.12 ? 109 ALA A O   1 
ATOM   810  C CB  . ALA A 1 109 ? 1.041   -20.746 -30.707 1.00 21.51 ? 109 ALA A CB  1 
ATOM   811  N N   . LYS A 1 110 ? 1.067   -17.649 -29.372 1.00 20.57 ? 110 LYS A N   1 
ATOM   812  C CA  . LYS A 1 110 ? 0.648   -16.250 -29.413 1.00 20.15 ? 110 LYS A CA  1 
ATOM   813  C C   . LYS A 1 110 ? 1.859   -15.324 -29.284 1.00 19.74 ? 110 LYS A C   1 
ATOM   814  O O   . LYS A 1 110 ? 1.888   -14.241 -29.878 1.00 19.70 ? 110 LYS A O   1 
ATOM   815  C CB  . LYS A 1 110 ? -0.400  -15.958 -28.327 1.00 20.30 ? 110 LYS A CB  1 
ATOM   816  C CG  . LYS A 1 110 ? -0.851  -14.492 -28.208 1.00 20.23 ? 110 LYS A CG  1 
ATOM   817  C CD  . LYS A 1 110 ? -1.399  -13.926 -29.517 1.00 20.43 ? 110 LYS A CD  1 
ATOM   818  C CE  . LYS A 1 110 ? -1.713  -12.445 -29.380 1.00 21.27 ? 110 LYS A CE  1 
ATOM   819  N NZ  . LYS A 1 110 ? -3.067  -12.211 -28.773 1.00 22.48 ? 110 LYS A NZ  1 
ATOM   820  N N   . LEU A 1 111 ? 2.854   -15.757 -28.514 1.00 19.23 ? 111 LEU A N   1 
ATOM   821  C CA  . LEU A 1 111 ? 4.134   -15.062 -28.453 1.00 18.76 ? 111 LEU A CA  1 
ATOM   822  C C   . LEU A 1 111 ? 4.764   -15.032 -29.844 1.00 18.52 ? 111 LEU A C   1 
ATOM   823  O O   . LEU A 1 111 ? 5.163   -13.969 -30.325 1.00 18.56 ? 111 LEU A O   1 
ATOM   824  C CB  . LEU A 1 111 ? 5.088   -15.758 -27.480 1.00 18.69 ? 111 LEU A CB  1 
ATOM   825  C CG  . LEU A 1 111 ? 6.191   -14.975 -26.755 1.00 18.10 ? 111 LEU A CG  1 
ATOM   826  C CD1 . LEU A 1 111 ? 7.436   -15.846 -26.654 1.00 17.29 ? 111 LEU A CD1 1 
ATOM   827  C CD2 . LEU A 1 111 ? 6.534   -13.647 -27.406 1.00 17.52 ? 111 LEU A CD2 1 
ATOM   828  N N   . VAL A 1 112 ? 4.849   -16.201 -30.480 1.00 18.11 ? 112 VAL A N   1 
ATOM   829  C CA  . VAL A 1 112 ? 5.413   -16.317 -31.826 1.00 17.80 ? 112 VAL A CA  1 
ATOM   830  C C   . VAL A 1 112 ? 4.689   -15.372 -32.796 1.00 17.85 ? 112 VAL A C   1 
ATOM   831  O O   . VAL A 1 112 ? 5.333   -14.589 -33.505 1.00 17.65 ? 112 VAL A O   1 
ATOM   832  C CB  . VAL A 1 112 ? 5.401   -17.790 -32.343 1.00 17.68 ? 112 VAL A CB  1 
ATOM   833  C CG1 . VAL A 1 112 ? 5.804   -17.863 -33.818 1.00 17.41 ? 112 VAL A CG1 1 
ATOM   834  C CG2 . VAL A 1 112 ? 6.326   -18.666 -31.503 1.00 16.90 ? 112 VAL A CG2 1 
ATOM   835  N N   . ALA A 1 113 ? 3.357   -15.431 -32.796 1.00 17.88 ? 113 ALA A N   1 
ATOM   836  C CA  . ALA A 1 113 ? 2.539   -14.569 -33.650 1.00 18.19 ? 113 ALA A CA  1 
ATOM   837  C C   . ALA A 1 113 ? 2.884   -13.095 -33.449 1.00 18.47 ? 113 ALA A C   1 
ATOM   838  O O   . ALA A 1 113 ? 3.076   -12.353 -34.419 1.00 18.17 ? 113 ALA A O   1 
ATOM   839  C CB  . ALA A 1 113 ? 1.058   -14.810 -33.393 1.00 18.01 ? 113 ALA A CB  1 
ATOM   840  N N   . ASN A 1 114 ? 2.962   -12.684 -32.183 1.00 18.90 ? 114 ASN A N   1 
ATOM   841  C CA  . ASN A 1 114 ? 3.341   -11.321 -31.832 1.00 19.36 ? 114 ASN A CA  1 
ATOM   842  C C   . ASN A 1 114 ? 4.763   -10.992 -32.259 1.00 19.55 ? 114 ASN A C   1 
ATOM   843  O O   . ASN A 1 114 ? 5.033   -9.895  -32.738 1.00 19.88 ? 114 ASN A O   1 
ATOM   844  C CB  . ASN A 1 114 ? 3.164   -11.079 -30.330 1.00 19.40 ? 114 ASN A CB  1 
ATOM   845  C CG  . ASN A 1 114 ? 1.714   -10.845 -29.940 1.00 19.65 ? 114 ASN A CG  1 
ATOM   846  O OD1 . ASN A 1 114 ? 0.834   -10.708 -30.794 1.00 21.16 ? 114 ASN A OD1 1 
ATOM   847  N ND2 . ASN A 1 114 ? 1.458   -10.793 -28.640 1.00 18.86 ? 114 ASN A ND2 1 
ATOM   848  N N   . MET A 1 115 ? 5.671   -11.944 -32.090 1.00 19.79 ? 115 MET A N   1 
ATOM   849  C CA  . MET A 1 115 ? 7.061   -11.732 -32.475 1.00 20.07 ? 115 MET A CA  1 
ATOM   850  C C   . MET A 1 115 ? 7.188   -11.504 -33.979 1.00 19.93 ? 115 MET A C   1 
ATOM   851  O O   . MET A 1 115 ? 7.827   -10.543 -34.400 1.00 19.85 ? 115 MET A O   1 
ATOM   852  C CB  . MET A 1 115 ? 7.937   -12.898 -32.015 1.00 20.29 ? 115 MET A CB  1 
ATOM   853  C CG  . MET A 1 115 ? 8.337   -12.827 -30.546 1.00 21.06 ? 115 MET A CG  1 
ATOM   854  S SD  . MET A 1 115 ? 8.992   -14.396 -29.928 1.00 25.45 ? 115 MET A SD  1 
ATOM   855  C CE  . MET A 1 115 ? 10.454  -14.575 -30.931 1.00 24.62 ? 115 MET A CE  1 
ATOM   856  N N   . LEU A 1 116 ? 6.556   -12.378 -34.770 1.00 19.94 ? 116 LEU A N   1 
ATOM   857  C CA  . LEU A 1 116 ? 6.522   -12.259 -36.233 1.00 19.81 ? 116 LEU A CA  1 
ATOM   858  C C   . LEU A 1 116 ? 5.926   -10.933 -36.679 1.00 19.91 ? 116 LEU A C   1 
ATOM   859  O O   . LEU A 1 116 ? 6.471   -10.273 -37.559 1.00 19.73 ? 116 LEU A O   1 
ATOM   860  C CB  . LEU A 1 116 ? 5.741   -13.420 -36.860 1.00 19.72 ? 116 LEU A CB  1 
ATOM   861  C CG  . LEU A 1 116 ? 6.398   -14.805 -36.939 1.00 19.66 ? 116 LEU A CG  1 
ATOM   862  C CD1 . LEU A 1 116 ? 5.354   -15.910 -36.890 1.00 18.80 ? 116 LEU A CD1 1 
ATOM   863  C CD2 . LEU A 1 116 ? 7.249   -14.940 -38.193 1.00 19.48 ? 116 LEU A CD2 1 
ATOM   864  N N   . SER A 1 117 ? 4.817   -10.548 -36.054 1.00 20.41 ? 117 SER A N   1 
ATOM   865  C CA  . SER A 1 117 ? 4.130   -9.286  -36.352 1.00 20.94 ? 117 SER A CA  1 
ATOM   866  C C   . SER A 1 117 ? 5.009   -8.065  -36.091 1.00 21.06 ? 117 SER A C   1 
ATOM   867  O O   . SER A 1 117 ? 5.205   -7.246  -36.988 1.00 21.27 ? 117 SER A O   1 
ATOM   868  C CB  . SER A 1 117 ? 2.828   -9.187  -35.552 1.00 21.10 ? 117 SER A CB  1 
ATOM   869  O OG  . SER A 1 117 ? 2.053   -10.373 -35.704 1.00 21.55 ? 117 SER A OG  1 
ATOM   870  N N   . VAL A 1 118 ? 5.549   -7.957  -34.877 1.00 21.28 ? 118 VAL A N   1 
ATOM   871  C CA  . VAL A 1 118 ? 6.437   -6.840  -34.517 1.00 21.40 ? 118 VAL A CA  1 
ATOM   872  C C   . VAL A 1 118 ? 7.765   -6.850  -35.294 1.00 21.48 ? 118 VAL A C   1 
ATOM   873  O O   . VAL A 1 118 ? 8.484   -5.848  -35.316 1.00 21.70 ? 118 VAL A O   1 
ATOM   874  C CB  . VAL A 1 118 ? 6.694   -6.768  -32.984 1.00 21.46 ? 118 VAL A CB  1 
ATOM   875  C CG1 . VAL A 1 118 ? 7.926   -7.591  -32.582 1.00 21.18 ? 118 VAL A CG1 1 
ATOM   876  C CG2 . VAL A 1 118 ? 6.858   -5.319  -32.542 1.00 21.79 ? 118 VAL A CG2 1 
ATOM   877  N N   . ALA A 1 119 ? 8.082   -7.974  -35.933 1.00 21.47 ? 119 ALA A N   1 
ATOM   878  C CA  . ALA A 1 119 ? 9.262   -8.047  -36.796 1.00 21.54 ? 119 ALA A CA  1 
ATOM   879  C C   . ALA A 1 119 ? 8.995   -7.405  -38.162 1.00 21.65 ? 119 ALA A C   1 
ATOM   880  O O   . ALA A 1 119 ? 9.933   -7.095  -38.906 1.00 21.62 ? 119 ALA A O   1 
ATOM   881  C CB  . ALA A 1 119 ? 9.730   -9.487  -36.951 1.00 21.45 ? 119 ALA A CB  1 
ATOM   882  N N   . GLY A 1 120 ? 7.715   -7.207  -38.480 1.00 21.69 ? 120 GLY A N   1 
ATOM   883  C CA  . GLY A 1 120 ? 7.316   -6.553  -39.725 1.00 21.94 ? 120 GLY A CA  1 
ATOM   884  C C   . GLY A 1 120 ? 6.568   -7.434  -40.711 1.00 22.12 ? 120 GLY A C   1 
ATOM   885  O O   . GLY A 1 120 ? 6.435   -7.079  -41.882 1.00 22.32 ? 120 GLY A O   1 
ATOM   886  N N   . ALA A 1 121 ? 6.082   -8.583  -40.248 1.00 22.16 ? 121 ALA A N   1 
ATOM   887  C CA  . ALA A 1 121 ? 5.276   -9.472  -41.083 1.00 22.20 ? 121 ALA A CA  1 
ATOM   888  C C   . ALA A 1 121 ? 3.956   -8.806  -41.468 1.00 22.27 ? 121 ALA A C   1 
ATOM   889  O O   . ALA A 1 121 ? 3.279   -8.218  -40.626 1.00 22.50 ? 121 ALA A O   1 
ATOM   890  C CB  . ALA A 1 121 ? 5.022   -10.787 -40.370 1.00 22.09 ? 121 ALA A CB  1 
ATOM   891  N N   . ASP A 1 122 ? 3.607   -8.894  -42.746 1.00 22.25 ? 122 ASP A N   1 
ATOM   892  C CA  . ASP A 1 122 ? 2.389   -8.279  -43.264 1.00 22.04 ? 122 ASP A CA  1 
ATOM   893  C C   . ASP A 1 122 ? 1.313   -9.316  -43.514 1.00 21.92 ? 122 ASP A C   1 
ATOM   894  O O   . ASP A 1 122 ? 0.126   -8.995  -43.516 1.00 22.13 ? 122 ASP A O   1 
ATOM   895  C CB  . ASP A 1 122 ? 2.680   -7.538  -44.573 1.00 21.92 ? 122 ASP A CB  1 
ATOM   896  C CG  . ASP A 1 122 ? 3.586   -6.341  -44.378 1.00 22.57 ? 122 ASP A CG  1 
ATOM   897  O OD1 . ASP A 1 122 ? 3.291   -5.496  -43.503 1.00 21.67 ? 122 ASP A OD1 1 
ATOM   898  O OD2 . ASP A 1 122 ? 4.594   -6.241  -45.114 1.00 24.12 ? 122 ASP A OD2 1 
ATOM   899  N N   . HIS A 1 123 ? 1.738   -10.554 -43.732 1.00 21.77 ? 123 HIS A N   1 
ATOM   900  C CA  . HIS A 1 123 ? 0.860   -11.631 -44.163 1.00 21.85 ? 123 HIS A CA  1 
ATOM   901  C C   . HIS A 1 123 ? 1.560   -12.958 -43.910 1.00 21.68 ? 123 HIS A C   1 
ATOM   902  O O   . HIS A 1 123 ? 2.792   -13.034 -43.932 1.00 21.53 ? 123 HIS A O   1 
ATOM   903  C CB  . HIS A 1 123 ? 0.518   -11.467 -45.652 1.00 22.09 ? 123 HIS A CB  1 
ATOM   904  C CG  . HIS A 1 123 ? -0.260  -12.608 -46.233 1.00 22.87 ? 123 HIS A CG  1 
ATOM   905  N ND1 . HIS A 1 123 ? 0.246   -13.424 -47.224 1.00 23.59 ? 123 HIS A ND1 1 
ATOM   906  C CD2 . HIS A 1 123 ? -1.503  -13.070 -45.963 1.00 23.65 ? 123 HIS A CD2 1 
ATOM   907  C CE1 . HIS A 1 123 ? -0.652  -14.340 -47.539 1.00 23.62 ? 123 HIS A CE1 1 
ATOM   908  N NE2 . HIS A 1 123 ? -1.723  -14.148 -46.787 1.00 23.77 ? 123 HIS A NE2 1 
ATOM   909  N N   . ILE A 1 124 ? 0.780   -14.001 -43.646 1.00 21.54 ? 124 ILE A N   1 
ATOM   910  C CA  . ILE A 1 124 ? 1.357   -15.317 -43.382 1.00 21.52 ? 124 ILE A CA  1 
ATOM   911  C C   . ILE A 1 124 ? 0.720   -16.407 -44.238 1.00 21.47 ? 124 ILE A C   1 
ATOM   912  O O   . ILE A 1 124 ? -0.488  -16.396 -44.480 1.00 21.51 ? 124 ILE A O   1 
ATOM   913  C CB  . ILE A 1 124 ? 1.311   -15.684 -41.874 1.00 21.33 ? 124 ILE A CB  1 
ATOM   914  C CG1 . ILE A 1 124 ? 2.172   -14.696 -41.073 1.00 21.65 ? 124 ILE A CG1 1 
ATOM   915  C CG2 . ILE A 1 124 ? 1.753   -17.132 -41.649 1.00 21.12 ? 124 ILE A CG2 1 
ATOM   916  C CD1 . ILE A 1 124 ? 2.708   -15.213 -39.760 1.00 21.46 ? 124 ILE A CD1 1 
ATOM   917  N N   . ILE A 1 125 ? 1.569   -17.321 -44.705 1.00 21.37 ? 125 ILE A N   1 
ATOM   918  C CA  . ILE A 1 125 ? 1.156   -18.521 -45.413 1.00 21.35 ? 125 ILE A CA  1 
ATOM   919  C C   . ILE A 1 125 ? 1.703   -19.696 -44.615 1.00 21.77 ? 125 ILE A C   1 
ATOM   920  O O   . ILE A 1 125 ? 2.902   -19.759 -44.317 1.00 21.84 ? 125 ILE A O   1 
ATOM   921  C CB  . ILE A 1 125 ? 1.726   -18.566 -46.855 1.00 21.15 ? 125 ILE A CB  1 
ATOM   922  C CG1 . ILE A 1 125 ? 1.204   -17.388 -47.682 1.00 20.28 ? 125 ILE A CG1 1 
ATOM   923  C CG2 . ILE A 1 125 ? 1.392   -19.897 -47.531 1.00 21.09 ? 125 ILE A CG2 1 
ATOM   924  C CD1 . ILE A 1 125 ? 2.061   -17.051 -48.883 1.00 18.33 ? 125 ILE A CD1 1 
ATOM   925  N N   . THR A 1 126 ? 0.819   -20.619 -44.256 1.00 22.19 ? 126 THR A N   1 
ATOM   926  C CA  . THR A 1 126 ? 1.207   -21.799 -43.492 1.00 22.58 ? 126 THR A CA  1 
ATOM   927  C C   . THR A 1 126 ? 0.323   -22.985 -43.880 1.00 22.74 ? 126 THR A C   1 
ATOM   928  O O   . THR A 1 126 ? -0.691  -22.808 -44.555 1.00 22.73 ? 126 THR A O   1 
ATOM   929  C CB  . THR A 1 126 ? 1.161   -21.521 -41.963 1.00 22.60 ? 126 THR A CB  1 
ATOM   930  O OG1 . THR A 1 126 ? 1.777   -22.600 -41.247 1.00 22.68 ? 126 THR A OG1 1 
ATOM   931  C CG2 . THR A 1 126 ? -0.265  -21.316 -41.483 1.00 22.67 ? 126 THR A CG2 1 
ATOM   932  N N   . MET A 1 127 ? 0.723   -24.186 -43.469 1.00 23.09 ? 127 MET A N   1 
ATOM   933  C CA  . MET A 1 127 ? -0.038  -25.394 -43.768 1.00 23.63 ? 127 MET A CA  1 
ATOM   934  C C   . MET A 1 127 ? -0.453  -26.123 -42.494 1.00 23.72 ? 127 MET A C   1 
ATOM   935  O O   . MET A 1 127 ? 0.367   -26.341 -41.601 1.00 23.80 ? 127 MET A O   1 
ATOM   936  C CB  . MET A 1 127 ? 0.760   -26.327 -44.687 1.00 23.79 ? 127 MET A CB  1 
ATOM   937  C CG  . MET A 1 127 ? 0.019   -27.613 -45.054 1.00 24.59 ? 127 MET A CG  1 
ATOM   938  S SD  . MET A 1 127 ? 0.627   -28.407 -46.558 1.00 26.61 ? 127 MET A SD  1 
ATOM   939  C CE  . MET A 1 127 ? 0.251   -27.169 -47.800 1.00 26.39 ? 127 MET A CE  1 
ATOM   940  N N   . ASP A 1 128 ? -1.731  -26.490 -42.434 1.00 23.93 ? 128 ASP A N   1 
ATOM   941  C CA  . ASP A 1 128 ? -2.326  -27.230 -41.306 1.00 24.34 ? 128 ASP A CA  1 
ATOM   942  C C   . ASP A 1 128 ? -1.894  -26.777 -39.914 1.00 24.37 ? 128 ASP A C   1 
ATOM   943  O O   . ASP A 1 128 ? -1.182  -27.499 -39.195 1.00 24.34 ? 128 ASP A O   1 
ATOM   944  C CB  . ASP A 1 128 ? -2.131  -28.742 -41.476 1.00 24.42 ? 128 ASP A CB  1 
ATOM   945  C CG  . ASP A 1 128 ? -2.851  -29.275 -42.698 1.00 25.00 ? 128 ASP A CG  1 
ATOM   946  O OD1 . ASP A 1 128 ? -2.246  -30.078 -43.443 1.00 25.82 ? 128 ASP A OD1 1 
ATOM   947  O OD2 . ASP A 1 128 ? -4.014  -28.876 -42.923 1.00 24.84 ? 128 ASP A OD2 1 
ATOM   948  N N   . LEU A 1 129 ? -2.345  -25.571 -39.550 1.00 24.41 ? 129 LEU A N   1 
ATOM   949  C CA  . LEU A 1 129 ? -2.182  -25.035 -38.206 1.00 24.38 ? 129 LEU A CA  1 
ATOM   950  C C   . LEU A 1 129 ? -2.730  -26.020 -37.184 1.00 24.51 ? 129 LEU A C   1 
ATOM   951  O O   . LEU A 1 129 ? -3.883  -26.444 -37.297 1.00 24.55 ? 129 LEU A O   1 
ATOM   952  C CB  . LEU A 1 129 ? -2.930  -23.703 -38.091 1.00 24.27 ? 129 LEU A CB  1 
ATOM   953  C CG  . LEU A 1 129 ? -2.266  -22.520 -38.798 1.00 24.09 ? 129 LEU A CG  1 
ATOM   954  C CD1 . LEU A 1 129 ? -3.184  -21.302 -38.703 1.00 24.51 ? 129 LEU A CD1 1 
ATOM   955  C CD2 . LEU A 1 129 ? -0.893  -22.219 -38.155 1.00 22.53 ? 129 LEU A CD2 1 
ATOM   956  N N   . HIS A 1 130 ? -1.906  -26.383 -36.200 1.00 24.65 ? 130 HIS A N   1 
ATOM   957  C CA  . HIS A 1 130 ? -2.281  -27.384 -35.192 1.00 24.78 ? 130 HIS A CA  1 
ATOM   958  C C   . HIS A 1 130 ? -3.677  -27.139 -34.630 1.00 24.67 ? 130 HIS A C   1 
ATOM   959  O O   . HIS A 1 130 ? -4.352  -28.072 -34.184 1.00 24.64 ? 130 HIS A O   1 
ATOM   960  C CB  . HIS A 1 130 ? -1.260  -27.442 -34.050 1.00 24.96 ? 130 HIS A CB  1 
ATOM   961  C CG  . HIS A 1 130 ? -1.623  -28.419 -32.974 1.00 25.55 ? 130 HIS A CG  1 
ATOM   962  N ND1 . HIS A 1 130 ? -2.253  -28.041 -31.808 1.00 26.07 ? 130 HIS A ND1 1 
ATOM   963  C CD2 . HIS A 1 130 ? -1.476  -29.764 -32.903 1.00 25.92 ? 130 HIS A CD2 1 
ATOM   964  C CE1 . HIS A 1 130 ? -2.461  -29.108 -31.057 1.00 26.08 ? 130 HIS A CE1 1 
ATOM   965  N NE2 . HIS A 1 130 ? -2.000  -30.166 -31.699 1.00 25.72 ? 130 HIS A NE2 1 
ATOM   966  N N   . ALA A 1 131 ? -4.083  -25.871 -34.642 1.00 24.68 ? 131 ALA A N   1 
ATOM   967  C CA  . ALA A 1 131 ? -5.441  -25.459 -34.322 1.00 24.60 ? 131 ALA A CA  1 
ATOM   968  C C   . ALA A 1 131 ? -5.808  -24.242 -35.174 1.00 24.68 ? 131 ALA A C   1 
ATOM   969  O O   . ALA A 1 131 ? -5.002  -23.318 -35.332 1.00 24.38 ? 131 ALA A O   1 
ATOM   970  C CB  . ALA A 1 131 ? -5.564  -25.142 -32.840 1.00 24.55 ? 131 ALA A CB  1 
ATOM   971  N N   . SER A 1 132 ? -7.022  -24.258 -35.724 1.00 24.84 ? 132 SER A N   1 
ATOM   972  C CA  . SER A 1 132 ? -7.530  -23.182 -36.582 1.00 25.12 ? 132 SER A CA  1 
ATOM   973  C C   . SER A 1 132 ? -7.531  -21.808 -35.913 1.00 25.10 ? 132 SER A C   1 
ATOM   974  O O   . SER A 1 132 ? -7.335  -20.777 -36.573 1.00 25.09 ? 132 SER A O   1 
ATOM   975  C CB  . SER A 1 132 ? -8.949  -23.507 -37.041 1.00 25.17 ? 132 SER A CB  1 
ATOM   976  O OG  . SER A 1 132 ? -8.940  -24.229 -38.251 1.00 26.41 ? 132 SER A OG  1 
ATOM   977  N N   . GLN A 1 133 ? -7.748  -21.812 -34.601 1.00 24.89 ? 133 GLN A N   1 
ATOM   978  C CA  . GLN A 1 133 ? -7.853  -20.599 -33.807 1.00 24.81 ? 133 GLN A CA  1 
ATOM   979  C C   . GLN A 1 133 ? -6.538  -19.804 -33.724 1.00 24.55 ? 133 GLN A C   1 
ATOM   980  O O   . GLN A 1 133 ? -6.547  -18.638 -33.327 1.00 24.61 ? 133 GLN A O   1 
ATOM   981  C CB  . GLN A 1 133 ? -8.374  -20.933 -32.404 1.00 24.96 ? 133 GLN A CB  1 
ATOM   982  C CG  . GLN A 1 133 ? -9.763  -21.601 -32.373 1.00 25.93 ? 133 GLN A CG  1 
ATOM   983  C CD  . GLN A 1 133 ? -9.723  -23.136 -32.310 1.00 27.12 ? 133 GLN A CD  1 
ATOM   984  O OE1 . GLN A 1 133 ? -10.759 -23.786 -32.137 1.00 27.38 ? 133 GLN A OE1 1 
ATOM   985  N NE2 . GLN A 1 133 ? -8.534  -23.713 -32.446 1.00 27.67 ? 133 GLN A NE2 1 
ATOM   986  N N   . ILE A 1 134 ? -5.421  -20.430 -34.099 1.00 24.12 ? 134 ILE A N   1 
ATOM   987  C CA  . ILE A 1 134 ? -4.115  -19.752 -34.138 1.00 23.62 ? 134 ILE A CA  1 
ATOM   988  C C   . ILE A 1 134 ? -4.135  -18.595 -35.143 1.00 23.37 ? 134 ILE A C   1 
ATOM   989  O O   . ILE A 1 134 ? -3.441  -17.591 -34.959 1.00 23.56 ? 134 ILE A O   1 
ATOM   990  C CB  . ILE A 1 134 ? -2.948  -20.738 -34.450 1.00 23.68 ? 134 ILE A CB  1 
ATOM   991  C CG1 . ILE A 1 134 ? -2.752  -21.726 -33.294 1.00 23.30 ? 134 ILE A CG1 1 
ATOM   992  C CG2 . ILE A 1 134 ? -1.643  -19.991 -34.729 1.00 23.34 ? 134 ILE A CG2 1 
ATOM   993  C CD1 . ILE A 1 134 ? -1.727  -22.815 -33.572 1.00 22.85 ? 134 ILE A CD1 1 
ATOM   994  N N   . GLN A 1 135 ? -4.935  -18.734 -36.198 1.00 22.91 ? 135 GLN A N   1 
ATOM   995  C CA  . GLN A 1 135 ? -5.163  -17.629 -37.130 1.00 22.43 ? 135 GLN A CA  1 
ATOM   996  C C   . GLN A 1 135 ? -5.585  -16.397 -36.349 1.00 22.02 ? 135 GLN A C   1 
ATOM   997  O O   . GLN A 1 135 ? -5.220  -15.275 -36.697 1.00 22.11 ? 135 GLN A O   1 
ATOM   998  C CB  . GLN A 1 135 ? -6.246  -17.979 -38.150 1.00 22.35 ? 135 GLN A CB  1 
ATOM   999  C CG  . GLN A 1 135 ? -5.826  -19.018 -39.180 1.00 22.56 ? 135 GLN A CG  1 
ATOM   1000 C CD  . GLN A 1 135 ? -6.452  -18.780 -40.543 1.00 22.83 ? 135 GLN A CD  1 
ATOM   1001 O OE1 . GLN A 1 135 ? -6.807  -19.718 -41.248 1.00 23.47 ? 135 GLN A OE1 1 
ATOM   1002 N NE2 . GLN A 1 135 ? -6.583  -17.518 -40.922 1.00 23.31 ? 135 GLN A NE2 1 
ATOM   1003 N N   . GLY A 1 136 ? -6.334  -16.626 -35.274 1.00 21.64 ? 136 GLY A N   1 
ATOM   1004 C CA  . GLY A 1 136 ? -6.846  -15.550 -34.440 1.00 21.35 ? 136 GLY A CA  1 
ATOM   1005 C C   . GLY A 1 136 ? -5.775  -14.865 -33.621 1.00 21.24 ? 136 GLY A C   1 
ATOM   1006 O O   . GLY A 1 136 ? -5.992  -13.755 -33.129 1.00 21.17 ? 136 GLY A O   1 
ATOM   1007 N N   . PHE A 1 137 ? -4.617  -15.514 -33.483 1.00 20.97 ? 137 PHE A N   1 
ATOM   1008 C CA  . PHE A 1 137 ? -3.505  -14.940 -32.725 1.00 20.92 ? 137 PHE A CA  1 
ATOM   1009 C C   . PHE A 1 137 ? -2.864  -13.772 -33.467 1.00 20.95 ? 137 PHE A C   1 
ATOM   1010 O O   . PHE A 1 137 ? -1.963  -13.128 -32.943 1.00 21.05 ? 137 PHE A O   1 
ATOM   1011 C CB  . PHE A 1 137 ? -2.429  -15.996 -32.404 1.00 20.84 ? 137 PHE A CB  1 
ATOM   1012 C CG  . PHE A 1 137 ? -2.895  -17.108 -31.495 1.00 20.76 ? 137 PHE A CG  1 
ATOM   1013 C CD1 . PHE A 1 137 ? -4.176  -17.114 -30.945 1.00 20.88 ? 137 PHE A CD1 1 
ATOM   1014 C CD2 . PHE A 1 137 ? -2.021  -18.142 -31.164 1.00 20.80 ? 137 PHE A CD2 1 
ATOM   1015 C CE1 . PHE A 1 137 ? -4.589  -18.148 -30.109 1.00 20.89 ? 137 PHE A CE1 1 
ATOM   1016 C CE2 . PHE A 1 137 ? -2.423  -19.174 -30.324 1.00 20.58 ? 137 PHE A CE2 1 
ATOM   1017 C CZ  . PHE A 1 137 ? -3.709  -19.177 -29.797 1.00 20.73 ? 137 PHE A CZ  1 
ATOM   1018 N N   . PHE A 1 138 ? -3.328  -13.499 -34.683 1.00 20.98 ? 138 PHE A N   1 
ATOM   1019 C CA  . PHE A 1 138 ? -2.755  -12.419 -35.504 1.00 21.06 ? 138 PHE A CA  1 
ATOM   1020 C C   . PHE A 1 138 ? -3.755  -11.291 -35.731 1.00 21.25 ? 138 PHE A C   1 
ATOM   1021 O O   . PHE A 1 138 ? -4.960  -11.459 -35.544 1.00 21.31 ? 138 PHE A O   1 
ATOM   1022 C CB  . PHE A 1 138 ? -2.311  -12.953 -36.875 1.00 20.80 ? 138 PHE A CB  1 
ATOM   1023 C CG  . PHE A 1 138 ? -1.164  -13.919 -36.817 1.00 20.26 ? 138 PHE A CG  1 
ATOM   1024 C CD1 . PHE A 1 138 ? -1.383  -15.271 -36.574 1.00 20.40 ? 138 PHE A CD1 1 
ATOM   1025 C CD2 . PHE A 1 138 ? 0.137   -13.483 -37.032 1.00 19.98 ? 138 PHE A CD2 1 
ATOM   1026 C CE1 . PHE A 1 138 ? -0.320  -16.171 -36.534 1.00 19.95 ? 138 PHE A CE1 1 
ATOM   1027 C CE2 . PHE A 1 138 ? 1.205   -14.374 -36.997 1.00 19.63 ? 138 PHE A CE2 1 
ATOM   1028 C CZ  . PHE A 1 138 ? 0.976   -15.720 -36.749 1.00 19.64 ? 138 PHE A CZ  1 
ATOM   1029 N N   . ASP A 1 139 ? -3.234  -10.127 -36.142 1.00 21.61 ? 139 ASP A N   1 
ATOM   1030 C CA  . ASP A 1 139 ? -4.104  -9.098  -36.690 1.00 21.92 ? 139 ASP A CA  1 
ATOM   1031 C C   . ASP A 1 139 ? -3.841  -8.950  -38.187 1.00 21.75 ? 139 ASP A C   1 
ATOM   1032 O O   . ASP A 1 139 ? -4.634  -8.351  -38.910 1.00 22.02 ? 139 ASP A O   1 
ATOM   1033 C CB  . ASP A 1 139 ? -3.955  -7.777  -35.925 1.00 22.18 ? 139 ASP A CB  1 
ATOM   1034 C CG  . ASP A 1 139 ? -4.807  -7.760  -34.647 1.00 23.27 ? 139 ASP A CG  1 
ATOM   1035 O OD1 . ASP A 1 139 ? -6.016  -8.102  -34.726 1.00 24.30 ? 139 ASP A OD1 1 
ATOM   1036 O OD2 . ASP A 1 139 ? -4.276  -7.402  -33.566 1.00 24.30 ? 139 ASP A OD2 1 
ATOM   1037 N N   . ILE A 1 140 ? -2.730  -9.524  -38.638 1.00 21.55 ? 140 ILE A N   1 
ATOM   1038 C CA  . ILE A 1 140 ? -2.409  -9.625  -40.064 1.00 21.36 ? 140 ILE A CA  1 
ATOM   1039 C C   . ILE A 1 140 ? -3.132  -10.822 -40.698 1.00 21.35 ? 140 ILE A C   1 
ATOM   1040 O O   . ILE A 1 140 ? -3.429  -11.797 -40.004 1.00 21.27 ? 140 ILE A O   1 
ATOM   1041 C CB  . ILE A 1 140 ? -0.876  -9.738  -40.299 1.00 21.29 ? 140 ILE A CB  1 
ATOM   1042 C CG1 . ILE A 1 140 ? -0.280  -10.892 -39.471 1.00 21.05 ? 140 ILE A CG1 1 
ATOM   1043 C CG2 . ILE A 1 140 ? -0.195  -8.398  -39.997 1.00 20.83 ? 140 ILE A CG2 1 
ATOM   1044 C CD1 . ILE A 1 140 ? 1.214   -11.142 -39.704 1.00 20.04 ? 140 ILE A CD1 1 
ATOM   1045 N N   . PRO A 1 141 ? -3.440  -10.743 -42.011 1.00 21.34 ? 141 PRO A N   1 
ATOM   1046 C CA  . PRO A 1 141 ? -4.062  -11.862 -42.727 1.00 21.33 ? 141 PRO A CA  1 
ATOM   1047 C C   . PRO A 1 141 ? -3.247  -13.149 -42.632 1.00 21.33 ? 141 PRO A C   1 
ATOM   1048 O O   . PRO A 1 141 ? -2.012  -13.116 -42.713 1.00 21.35 ? 141 PRO A O   1 
ATOM   1049 C CB  . PRO A 1 141 ? -4.081  -11.391 -44.184 1.00 21.29 ? 141 PRO A CB  1 
ATOM   1050 C CG  . PRO A 1 141 ? -4.028  -9.929  -44.123 1.00 21.52 ? 141 PRO A CG  1 
ATOM   1051 C CD  . PRO A 1 141 ? -3.238  -9.574  -42.887 1.00 21.42 ? 141 PRO A CD  1 
ATOM   1052 N N   . VAL A 1 142 ? -3.943  -14.268 -42.455 1.00 21.17 ? 142 VAL A N   1 
ATOM   1053 C CA  . VAL A 1 142 ? -3.314  -15.582 -42.446 1.00 21.08 ? 142 VAL A CA  1 
ATOM   1054 C C   . VAL A 1 142 ? -4.007  -16.469 -43.469 1.00 21.40 ? 142 VAL A C   1 
ATOM   1055 O O   . VAL A 1 142 ? -5.235  -16.516 -43.539 1.00 21.14 ? 142 VAL A O   1 
ATOM   1056 C CB  . VAL A 1 142 ? -3.360  -16.251 -41.037 1.00 20.89 ? 142 VAL A CB  1 
ATOM   1057 C CG1 . VAL A 1 142 ? -2.862  -17.684 -41.097 1.00 20.54 ? 142 VAL A CG1 1 
ATOM   1058 C CG2 . VAL A 1 142 ? -2.528  -15.461 -40.032 1.00 20.57 ? 142 VAL A CG2 1 
ATOM   1059 N N   . ASP A 1 143 ? -3.205  -17.154 -44.277 1.00 22.01 ? 143 ASP A N   1 
ATOM   1060 C CA  . ASP A 1 143 ? -3.703  -18.182 -45.172 1.00 22.60 ? 143 ASP A CA  1 
ATOM   1061 C C   . ASP A 1 143 ? -3.185  -19.513 -44.676 1.00 23.14 ? 143 ASP A C   1 
ATOM   1062 O O   . ASP A 1 143 ? -1.974  -19.745 -44.620 1.00 23.41 ? 143 ASP A O   1 
ATOM   1063 C CB  . ASP A 1 143 ? -3.262  -17.920 -46.611 1.00 22.46 ? 143 ASP A CB  1 
ATOM   1064 C CG  . ASP A 1 143 ? -3.961  -16.722 -47.221 1.00 22.55 ? 143 ASP A CG  1 
ATOM   1065 O OD1 . ASP A 1 143 ? -5.196  -16.589 -47.044 1.00 22.15 ? 143 ASP A OD1 1 
ATOM   1066 O OD2 . ASP A 1 143 ? -3.277  -15.912 -47.880 1.00 22.74 ? 143 ASP A OD2 1 
ATOM   1067 N N   . ASN A 1 144 ? -4.120  -20.372 -44.286 1.00 23.84 ? 144 ASN A N   1 
ATOM   1068 C CA  . ASN A 1 144 ? -3.809  -21.674 -43.721 1.00 24.42 ? 144 ASN A CA  1 
ATOM   1069 C C   . ASN A 1 144 ? -4.251  -22.758 -44.707 1.00 25.35 ? 144 ASN A C   1 
ATOM   1070 O O   . ASN A 1 144 ? -5.445  -23.023 -44.874 1.00 25.49 ? 144 ASN A O   1 
ATOM   1071 C CB  . ASN A 1 144 ? -4.463  -21.788 -42.332 1.00 24.05 ? 144 ASN A CB  1 
ATOM   1072 C CG  . ASN A 1 144 ? -4.479  -23.210 -41.782 1.00 23.09 ? 144 ASN A CG  1 
ATOM   1073 O OD1 . ASN A 1 144 ? -5.494  -23.644 -41.237 1.00 22.24 ? 144 ASN A OD1 1 
ATOM   1074 N ND2 . ASN A 1 144 ? -3.361  -23.926 -41.894 1.00 21.83 ? 144 ASN A ND2 1 
ATOM   1075 N N   . LEU A 1 145 ? -3.269  -23.347 -45.381 1.00 26.41 ? 145 LEU A N   1 
ATOM   1076 C CA  . LEU A 1 145 ? -3.500  -24.331 -46.431 1.00 27.68 ? 145 LEU A CA  1 
ATOM   1077 C C   . LEU A 1 145 ? -3.669  -25.736 -45.865 1.00 28.66 ? 145 LEU A C   1 
ATOM   1078 O O   . LEU A 1 145 ? -3.221  -26.023 -44.752 1.00 28.89 ? 145 LEU A O   1 
ATOM   1079 C CB  . LEU A 1 145 ? -2.338  -24.313 -47.429 1.00 27.60 ? 145 LEU A CB  1 
ATOM   1080 C CG  . LEU A 1 145 ? -1.964  -22.949 -48.016 1.00 27.76 ? 145 LEU A CG  1 
ATOM   1081 C CD1 . LEU A 1 145 ? -0.533  -22.952 -48.523 1.00 27.26 ? 145 LEU A CD1 1 
ATOM   1082 C CD2 . LEU A 1 145 ? -2.947  -22.519 -49.106 1.00 27.64 ? 145 LEU A CD2 1 
ATOM   1083 N N   . TYR A 1 146 ? -4.311  -26.608 -46.643 1.00 29.80 ? 146 TYR A N   1 
ATOM   1084 C CA  . TYR A 1 146 ? -4.563  -27.985 -46.225 1.00 30.79 ? 146 TYR A CA  1 
ATOM   1085 C C   . TYR A 1 146 ? -3.808  -28.993 -47.066 1.00 31.14 ? 146 TYR A C   1 
ATOM   1086 O O   . TYR A 1 146 ? -3.756  -28.878 -48.292 1.00 31.25 ? 146 TYR A O   1 
ATOM   1087 C CB  . TYR A 1 146 ? -6.065  -28.291 -46.268 1.00 30.94 ? 146 TYR A CB  1 
ATOM   1088 C CG  . TYR A 1 146 ? -6.854  -27.339 -45.418 1.00 32.36 ? 146 TYR A CG  1 
ATOM   1089 C CD1 . TYR A 1 146 ? -7.630  -26.339 -45.999 1.00 33.69 ? 146 TYR A CD1 1 
ATOM   1090 C CD2 . TYR A 1 146 ? -6.795  -27.414 -44.023 1.00 33.67 ? 146 TYR A CD2 1 
ATOM   1091 C CE1 . TYR A 1 146 ? -8.340  -25.447 -45.213 1.00 34.74 ? 146 TYR A CE1 1 
ATOM   1092 C CE2 . TYR A 1 146 ? -7.501  -26.529 -43.228 1.00 34.62 ? 146 TYR A CE2 1 
ATOM   1093 C CZ  . TYR A 1 146 ? -8.272  -25.552 -43.828 1.00 35.21 ? 146 TYR A CZ  1 
ATOM   1094 O OH  . TYR A 1 146 ? -8.974  -24.678 -43.043 1.00 36.58 ? 146 TYR A OH  1 
ATOM   1095 N N   . ALA A 1 147 ? -3.220  -29.976 -46.389 1.00 31.71 ? 147 ALA A N   1 
ATOM   1096 C CA  . ALA A 1 147 ? -2.618  -31.126 -47.052 1.00 32.20 ? 147 ALA A CA  1 
ATOM   1097 C C   . ALA A 1 147 ? -3.702  -32.152 -47.353 1.00 32.57 ? 147 ALA A C   1 
ATOM   1098 O O   . ALA A 1 147 ? -3.492  -33.070 -48.145 1.00 32.66 ? 147 ALA A O   1 
ATOM   1099 C CB  . ALA A 1 147 ? -1.532  -31.735 -46.180 1.00 32.17 ? 147 ALA A CB  1 
ATOM   1100 N N   . GLU A 1 148 ? -4.864  -31.970 -46.723 1.00 33.04 ? 148 GLU A N   1 
ATOM   1101 C CA  . GLU A 1 148 ? -6.004  -32.881 -46.846 1.00 33.61 ? 148 GLU A CA  1 
ATOM   1102 C C   . GLU A 1 148 ? -6.274  -33.384 -48.277 1.00 33.86 ? 148 GLU A C   1 
ATOM   1103 O O   . GLU A 1 148 ? -6.289  -34.598 -48.497 1.00 33.97 ? 148 GLU A O   1 
ATOM   1104 C CB  . GLU A 1 148 ? -7.268  -32.269 -46.219 1.00 33.71 ? 148 GLU A CB  1 
ATOM   1105 C CG  . GLU A 1 148 ? -8.568  -33.001 -46.602 1.00 34.42 ? 148 GLU A CG  1 
ATOM   1106 C CD  . GLU A 1 148 ? -9.768  -32.511 -45.813 1.00 35.32 ? 148 GLU A CD  1 
ATOM   1107 O OE1 . GLU A 1 148 ? -9.977  -31.276 -45.729 1.00 36.05 ? 148 GLU A OE1 1 
ATOM   1108 O OE2 . GLU A 1 148 ? -10.511 -33.371 -45.287 1.00 35.14 ? 148 GLU A OE2 1 
ATOM   1109 N N   . PRO A 1 149 ? -6.489  -32.466 -49.248 1.00 34.05 ? 149 PRO A N   1 
ATOM   1110 C CA  . PRO A 1 149 ? -6.723  -32.971 -50.605 1.00 34.12 ? 149 PRO A CA  1 
ATOM   1111 C C   . PRO A 1 149 ? -5.617  -33.928 -51.052 1.00 34.22 ? 149 PRO A C   1 
ATOM   1112 O O   . PRO A 1 149 ? -5.913  -35.058 -51.453 1.00 34.22 ? 149 PRO A O   1 
ATOM   1113 C CB  . PRO A 1 149 ? -6.742  -31.696 -51.454 1.00 34.15 ? 149 PRO A CB  1 
ATOM   1114 C CG  . PRO A 1 149 ? -7.205  -30.639 -50.499 1.00 34.07 ? 149 PRO A CG  1 
ATOM   1115 C CD  . PRO A 1 149 ? -6.545  -30.990 -49.203 1.00 34.01 ? 149 PRO A CD  1 
ATOM   1116 N N   . ALA A 1 150 ? -4.360  -33.493 -50.938 1.00 34.34 ? 150 ALA A N   1 
ATOM   1117 C CA  . ALA A 1 150 ? -3.208  -34.352 -51.236 1.00 34.41 ? 150 ALA A CA  1 
ATOM   1118 C C   . ALA A 1 150 ? -3.177  -35.648 -50.403 1.00 34.41 ? 150 ALA A C   1 
ATOM   1119 O O   . ALA A 1 150 ? -2.586  -36.643 -50.828 1.00 34.42 ? 150 ALA A O   1 
ATOM   1120 C CB  . ALA A 1 150 ? -1.906  -33.571 -51.063 1.00 34.41 ? 150 ALA A CB  1 
ATOM   1121 N N   . VAL A 1 151 ? -3.816  -35.627 -49.229 1.00 34.41 ? 151 VAL A N   1 
ATOM   1122 C CA  . VAL A 1 151 ? -3.864  -36.794 -48.335 1.00 34.39 ? 151 VAL A CA  1 
ATOM   1123 C C   . VAL A 1 151 ? -4.979  -37.764 -48.750 1.00 34.54 ? 151 VAL A C   1 
ATOM   1124 O O   . VAL A 1 151 ? -4.765  -38.982 -48.802 1.00 34.40 ? 151 VAL A O   1 
ATOM   1125 C CB  . VAL A 1 151 ? -4.005  -36.366 -46.844 1.00 34.36 ? 151 VAL A CB  1 
ATOM   1126 C CG1 . VAL A 1 151 ? -4.402  -37.548 -45.950 1.00 33.98 ? 151 VAL A CG1 1 
ATOM   1127 C CG2 . VAL A 1 151 ? -2.706  -35.740 -46.354 1.00 34.48 ? 151 VAL A CG2 1 
ATOM   1128 N N   . LEU A 1 152 ? -6.159  -37.217 -49.043 1.00 34.66 ? 152 LEU A N   1 
ATOM   1129 C CA  . LEU A 1 152 ? -7.267  -37.995 -49.594 1.00 34.87 ? 152 LEU A CA  1 
ATOM   1130 C C   . LEU A 1 152 ? -6.802  -38.695 -50.863 1.00 35.31 ? 152 LEU A C   1 
ATOM   1131 O O   . LEU A 1 152 ? -6.922  -39.922 -50.993 1.00 35.50 ? 152 LEU A O   1 
ATOM   1132 C CB  . LEU A 1 152 ? -8.452  -37.077 -49.912 1.00 34.68 ? 152 LEU A CB  1 
ATOM   1133 C CG  . LEU A 1 152 ? -9.617  -36.903 -48.927 1.00 34.38 ? 152 LEU A CG  1 
ATOM   1134 C CD1 . LEU A 1 152 ? -9.290  -37.322 -47.488 1.00 33.84 ? 152 LEU A CD1 1 
ATOM   1135 C CD2 . LEU A 1 152 ? -10.119 -35.468 -48.984 1.00 34.04 ? 152 LEU A CD2 1 
ATOM   1136 N N   . LYS A 1 153 ? -6.249  -37.894 -51.776 1.00 35.73 ? 153 LYS A N   1 
ATOM   1137 C CA  . LYS A 1 153 ? -5.670  -38.355 -53.036 1.00 35.98 ? 153 LYS A CA  1 
ATOM   1138 C C   . LYS A 1 153 ? -4.748  -39.557 -52.824 1.00 35.92 ? 153 LYS A C   1 
ATOM   1139 O O   . LYS A 1 153 ? -4.853  -40.557 -53.537 1.00 35.88 ? 153 LYS A O   1 
ATOM   1140 C CB  . LYS A 1 153 ? -4.895  -37.204 -53.688 1.00 36.09 ? 153 LYS A CB  1 
ATOM   1141 C CG  . LYS A 1 153 ? -5.176  -36.985 -55.176 1.00 36.70 ? 153 LYS A CG  1 
ATOM   1142 C CD  . LYS A 1 153 ? -4.103  -37.632 -56.062 1.00 37.66 ? 153 LYS A CD  1 
ATOM   1143 C CE  . LYS A 1 153 ? -4.334  -37.198 -57.526 1.00 38.20 ? 153 LYS A CE  1 
ATOM   1144 N NZ  . LYS A 1 153 ? -3.622  -38.129 -58.461 1.00 38.85 ? 153 LYS A NZ  1 
ATOM   1145 N N   . TRP A 1 154 ? -3.864  -39.461 -51.830 1.00 36.05 ? 154 TRP A N   1 
ATOM   1146 C CA  . TRP A 1 154 ? -2.871  -40.506 -51.573 1.00 36.21 ? 154 TRP A CA  1 
ATOM   1147 C C   . TRP A 1 154 ? -3.523  -41.805 -51.099 1.00 36.67 ? 154 TRP A C   1 
ATOM   1148 O O   . TRP A 1 154 ? -3.210  -42.881 -51.618 1.00 36.63 ? 154 TRP A O   1 
ATOM   1149 C CB  . TRP A 1 154 ? -1.804  -40.035 -50.574 1.00 35.88 ? 154 TRP A CB  1 
ATOM   1150 C CG  . TRP A 1 154 ? -0.634  -40.981 -50.474 1.00 34.90 ? 154 TRP A CG  1 
ATOM   1151 C CD1 . TRP A 1 154 ? 0.565   -40.880 -51.126 1.00 34.29 ? 154 TRP A CD1 1 
ATOM   1152 C CD2 . TRP A 1 154 ? -0.563  -42.182 -49.691 1.00 33.97 ? 154 TRP A CD2 1 
ATOM   1153 N NE1 . TRP A 1 154 ? 1.380   -41.936 -50.789 1.00 33.72 ? 154 TRP A NE1 1 
ATOM   1154 C CE2 . TRP A 1 154 ? 0.713   -42.752 -49.913 1.00 33.65 ? 154 TRP A CE2 1 
ATOM   1155 C CE3 . TRP A 1 154 ? -1.453  -42.831 -48.821 1.00 33.25 ? 154 TRP A CE3 1 
ATOM   1156 C CZ2 . TRP A 1 154 ? 1.121   -43.939 -49.299 1.00 33.60 ? 154 TRP A CZ2 1 
ATOM   1157 C CZ3 . TRP A 1 154 ? -1.047  -44.011 -48.210 1.00 33.04 ? 154 TRP A CZ3 1 
ATOM   1158 C CH2 . TRP A 1 154 ? 0.230   -44.553 -48.453 1.00 33.18 ? 154 TRP A CH2 1 
ATOM   1159 N N   . ILE A 1 155 ? -4.418  -41.689 -50.114 1.00 37.21 ? 155 ILE A N   1 
ATOM   1160 C CA  . ILE A 1 155 ? -5.154  -42.827 -49.554 1.00 37.62 ? 155 ILE A CA  1 
ATOM   1161 C C   . ILE A 1 155 ? -5.852  -43.634 -50.648 1.00 38.03 ? 155 ILE A C   1 
ATOM   1162 O O   . ILE A 1 155 ? -5.581  -44.829 -50.800 1.00 37.98 ? 155 ILE A O   1 
ATOM   1163 C CB  . ILE A 1 155 ? -6.186  -42.370 -48.480 1.00 37.66 ? 155 ILE A CB  1 
ATOM   1164 C CG1 . ILE A 1 155 ? -5.465  -41.776 -47.262 1.00 37.39 ? 155 ILE A CG1 1 
ATOM   1165 C CG2 . ILE A 1 155 ? -7.100  -43.534 -48.062 1.00 37.54 ? 155 ILE A CG2 1 
ATOM   1166 C CD1 . ILE A 1 155 ? -6.389  -41.052 -46.287 1.00 37.57 ? 155 ILE A CD1 1 
ATOM   1167 N N   . ARG A 1 156 ? -6.729  -42.965 -51.405 1.00 38.56 ? 156 ARG A N   1 
ATOM   1168 C CA  . ARG A 1 156 ? -7.484  -43.576 -52.501 1.00 39.17 ? 156 ARG A CA  1 
ATOM   1169 C C   . ARG A 1 156 ? -6.611  -44.327 -53.500 1.00 39.51 ? 156 ARG A C   1 
ATOM   1170 O O   . ARG A 1 156 ? -7.026  -45.357 -54.043 1.00 39.61 ? 156 ARG A O   1 
ATOM   1171 C CB  . ARG A 1 156 ? -8.272  -42.514 -53.270 1.00 39.26 ? 156 ARG A CB  1 
ATOM   1172 C CG  . ARG A 1 156 ? -9.415  -41.860 -52.506 1.00 40.02 ? 156 ARG A CG  1 
ATOM   1173 C CD  . ARG A 1 156 ? -10.313 -41.087 -53.487 1.00 40.74 ? 156 ARG A CD  1 
ATOM   1174 N NE  . ARG A 1 156 ? -11.158 -40.122 -52.786 1.00 41.72 ? 156 ARG A NE  1 
ATOM   1175 C CZ  . ARG A 1 156 ? -10.947 -38.807 -52.759 1.00 42.42 ? 156 ARG A CZ  1 
ATOM   1176 N NH1 . ARG A 1 156 ? -9.916  -38.272 -53.405 1.00 42.88 ? 156 ARG A NH1 1 
ATOM   1177 N NH2 . ARG A 1 156 ? -11.778 -38.019 -52.087 1.00 42.66 ? 156 ARG A NH2 1 
ATOM   1178 N N   . GLU A 1 157 ? -5.407  -43.807 -53.743 1.00 39.81 ? 157 GLU A N   1 
ATOM   1179 C CA  . GLU A 1 157 ? -4.534  -44.313 -54.800 1.00 40.10 ? 157 GLU A CA  1 
ATOM   1180 C C   . GLU A 1 157 ? -3.500  -45.331 -54.323 1.00 40.14 ? 157 GLU A C   1 
ATOM   1181 O O   . GLU A 1 157 ? -2.939  -46.072 -55.135 1.00 40.16 ? 157 GLU A O   1 
ATOM   1182 C CB  . GLU A 1 157 ? -3.844  -43.150 -55.524 1.00 40.18 ? 157 GLU A CB  1 
ATOM   1183 C CG  . GLU A 1 157 ? -4.781  -42.359 -56.432 1.00 41.30 ? 157 GLU A CG  1 
ATOM   1184 C CD  . GLU A 1 157 ? -4.171  -41.075 -56.984 1.00 42.59 ? 157 GLU A CD  1 
ATOM   1185 O OE1 . GLU A 1 157 ? -2.992  -40.772 -56.685 1.00 42.96 ? 157 GLU A OE1 1 
ATOM   1186 O OE2 . GLU A 1 157 ? -4.885  -40.367 -57.729 1.00 43.03 ? 157 GLU A OE2 1 
ATOM   1187 N N   . ASN A 1 158 ? -3.251  -45.372 -53.017 1.00 40.17 ? 158 ASN A N   1 
ATOM   1188 C CA  . ASN A 1 158 ? -2.209  -46.250 -52.480 1.00 40.10 ? 158 ASN A CA  1 
ATOM   1189 C C   . ASN A 1 158 ? -2.728  -47.327 -51.526 1.00 40.21 ? 158 ASN A C   1 
ATOM   1190 O O   . ASN A 1 158 ? -2.023  -48.299 -51.248 1.00 40.20 ? 158 ASN A O   1 
ATOM   1191 C CB  . ASN A 1 158 ? -1.081  -45.434 -51.830 1.00 40.09 ? 158 ASN A CB  1 
ATOM   1192 C CG  . ASN A 1 158 ? -0.354  -44.528 -52.825 1.00 39.91 ? 158 ASN A CG  1 
ATOM   1193 O OD1 . ASN A 1 158 ? 0.757   -44.832 -53.254 1.00 39.90 ? 158 ASN A OD1 1 
ATOM   1194 N ND2 . ASN A 1 158 ? -0.982  -43.413 -53.190 1.00 39.34 ? 158 ASN A ND2 1 
ATOM   1195 N N   . ILE A 1 159 ? -3.957  -47.159 -51.038 1.00 40.35 ? 159 ILE A N   1 
ATOM   1196 C CA  . ILE A 1 159 ? -4.580  -48.143 -50.141 1.00 40.46 ? 159 ILE A CA  1 
ATOM   1197 C C   . ILE A 1 159 ? -5.749  -48.862 -50.817 1.00 40.43 ? 159 ILE A C   1 
ATOM   1198 O O   . ILE A 1 159 ? -6.840  -48.295 -50.972 1.00 40.32 ? 159 ILE A O   1 
ATOM   1199 C CB  . ILE A 1 159 ? -5.027  -47.510 -48.791 1.00 40.58 ? 159 ILE A CB  1 
ATOM   1200 C CG1 . ILE A 1 159 ? -3.813  -46.955 -48.040 1.00 40.64 ? 159 ILE A CG1 1 
ATOM   1201 C CG2 . ILE A 1 159 ? -5.792  -48.528 -47.930 1.00 40.64 ? 159 ILE A CG2 1 
ATOM   1202 C CD1 . ILE A 1 159 ? -4.137  -46.360 -46.678 1.00 40.63 ? 159 ILE A CD1 1 
ATOM   1203 N N   . SER A 1 160 ? -5.509  -50.117 -51.209 1.00 40.45 ? 160 SER A N   1 
ATOM   1204 C CA  . SER A 1 160 ? -6.508  -50.920 -51.918 1.00 40.47 ? 160 SER A CA  1 
ATOM   1205 C C   . SER A 1 160 ? -7.814  -51.034 -51.127 1.00 40.52 ? 160 SER A C   1 
ATOM   1206 O O   . SER A 1 160 ? -8.910  -50.928 -51.695 1.00 40.50 ? 160 SER A O   1 
ATOM   1207 C CB  . SER A 1 160 ? -5.952  -52.317 -52.216 1.00 40.40 ? 160 SER A CB  1 
ATOM   1208 N N   . GLU A 1 161 ? -7.688  -51.224 -49.816 1.00 40.58 ? 161 GLU A N   1 
ATOM   1209 C CA  . GLU A 1 161 ? -8.836  -51.475 -48.947 1.00 40.79 ? 161 GLU A CA  1 
ATOM   1210 C C   . GLU A 1 161 ? -9.582  -50.208 -48.500 1.00 40.78 ? 161 GLU A C   1 
ATOM   1211 O O   . GLU A 1 161 ? -10.541 -50.298 -47.728 1.00 40.68 ? 161 GLU A O   1 
ATOM   1212 C CB  . GLU A 1 161 ? -8.387  -52.267 -47.718 1.00 40.90 ? 161 GLU A CB  1 
ATOM   1213 C CG  . GLU A 1 161 ? -7.905  -53.684 -48.000 1.00 41.69 ? 161 GLU A CG  1 
ATOM   1214 C CD  . GLU A 1 161 ? -8.958  -54.750 -47.701 1.00 43.08 ? 161 GLU A CD  1 
ATOM   1215 O OE1 . GLU A 1 161 ? -8.715  -55.923 -48.059 1.00 44.15 ? 161 GLU A OE1 1 
ATOM   1216 O OE2 . GLU A 1 161 ? -10.016 -54.431 -47.105 1.00 43.14 ? 161 GLU A OE2 1 
ATOM   1217 N N   . TRP A 1 162 ? -9.157  -49.045 -49.006 1.00 40.91 ? 162 TRP A N   1 
ATOM   1218 C CA  . TRP A 1 162 ? -9.605  -47.735 -48.495 1.00 40.87 ? 162 TRP A CA  1 
ATOM   1219 C C   . TRP A 1 162 ? -11.118 -47.523 -48.338 1.00 40.92 ? 162 TRP A C   1 
ATOM   1220 O O   . TRP A 1 162 ? -11.547 -46.798 -47.435 1.00 40.96 ? 162 TRP A O   1 
ATOM   1221 C CB  . TRP A 1 162 ? -8.979  -46.578 -49.294 1.00 40.91 ? 162 TRP A CB  1 
ATOM   1222 C CG  . TRP A 1 162 ? -9.583  -46.310 -50.655 1.00 40.71 ? 162 TRP A CG  1 
ATOM   1223 C CD1 . TRP A 1 162 ? -9.104  -46.737 -51.864 1.00 40.72 ? 162 TRP A CD1 1 
ATOM   1224 C CD2 . TRP A 1 162 ? -10.753 -45.529 -50.944 1.00 40.56 ? 162 TRP A CD2 1 
ATOM   1225 N NE1 . TRP A 1 162 ? -9.908  -46.283 -52.883 1.00 40.64 ? 162 TRP A NE1 1 
ATOM   1226 C CE2 . TRP A 1 162 ? -10.928 -45.541 -52.348 1.00 40.50 ? 162 TRP A CE2 1 
ATOM   1227 C CE3 . TRP A 1 162 ? -11.675 -44.828 -50.153 1.00 40.55 ? 162 TRP A CE3 1 
ATOM   1228 C CZ2 . TRP A 1 162 ? -11.988 -44.879 -52.979 1.00 40.44 ? 162 TRP A CZ2 1 
ATOM   1229 C CZ3 . TRP A 1 162 ? -12.735 -44.171 -50.783 1.00 40.60 ? 162 TRP A CZ3 1 
ATOM   1230 C CH2 . TRP A 1 162 ? -12.878 -44.201 -52.182 1.00 40.44 ? 162 TRP A CH2 1 
ATOM   1231 N N   . ARG A 1 163 ? -11.911 -48.148 -49.211 1.00 40.84 ? 163 ARG A N   1 
ATOM   1232 C CA  . ARG A 1 163 ? -13.377 -47.997 -49.199 1.00 40.81 ? 163 ARG A CA  1 
ATOM   1233 C C   . ARG A 1 163 ? -14.058 -48.572 -47.955 1.00 40.69 ? 163 ARG A C   1 
ATOM   1234 O O   . ARG A 1 163 ? -15.233 -48.280 -47.686 1.00 40.65 ? 163 ARG A O   1 
ATOM   1235 C CB  . ARG A 1 163 ? -13.998 -48.587 -50.471 1.00 40.87 ? 163 ARG A CB  1 
ATOM   1236 C CG  . ARG A 1 163 ? -13.855 -47.681 -51.677 1.00 41.26 ? 163 ARG A CG  1 
ATOM   1237 C CD  . ARG A 1 163 ? -14.444 -48.280 -52.954 1.00 41.90 ? 163 ARG A CD  1 
ATOM   1238 N NE  . ARG A 1 163 ? -14.120 -47.436 -54.111 1.00 42.29 ? 163 ARG A NE  1 
ATOM   1239 C CZ  . ARG A 1 163 ? -14.831 -46.375 -54.498 1.00 42.08 ? 163 ARG A CZ  1 
ATOM   1240 N NH1 . ARG A 1 163 ? -15.934 -46.030 -53.840 1.00 41.87 ? 163 ARG A NH1 1 
ATOM   1241 N NH2 . ARG A 1 163 ? -14.447 -45.665 -55.558 1.00 42.15 ? 163 ARG A NH2 1 
ATOM   1242 N N   . ASN A 1 164 ? -13.321 -49.385 -47.203 1.00 40.56 ? 164 ASN A N   1 
ATOM   1243 C CA  . ASN A 1 164 ? -13.826 -49.940 -45.951 1.00 40.63 ? 164 ASN A CA  1 
ATOM   1244 C C   . ASN A 1 164 ? -12.828 -49.788 -44.796 1.00 40.43 ? 164 ASN A C   1 
ATOM   1245 O O   . ASN A 1 164 ? -12.858 -50.547 -43.826 1.00 40.35 ? 164 ASN A O   1 
ATOM   1246 C CB  . ASN A 1 164 ? -14.245 -51.410 -46.144 1.00 40.78 ? 164 ASN A CB  1 
ATOM   1247 C CG  . ASN A 1 164 ? -15.416 -51.557 -47.109 1.00 41.32 ? 164 ASN A CG  1 
ATOM   1248 O OD1 . ASN A 1 164 ? -16.452 -50.894 -46.965 1.00 41.66 ? 164 ASN A OD1 1 
ATOM   1249 N ND2 . ASN A 1 164 ? -15.256 -52.434 -48.098 1.00 41.71 ? 164 ASN A ND2 1 
ATOM   1250 N N   . CYS A 1 165 ? -11.951 -48.792 -44.904 1.00 40.20 ? 165 CYS A N   1 
ATOM   1251 C CA  . CYS A 1 165 ? -10.980 -48.517 -43.847 1.00 40.02 ? 165 CYS A CA  1 
ATOM   1252 C C   . CYS A 1 165 ? -11.617 -47.714 -42.711 1.00 39.73 ? 165 CYS A C   1 
ATOM   1253 O O   . CYS A 1 165 ? -12.759 -47.246 -42.825 1.00 40.00 ? 165 CYS A O   1 
ATOM   1254 C CB  . CYS A 1 165 ? -9.758  -47.775 -44.407 1.00 40.03 ? 165 CYS A CB  1 
ATOM   1255 S SG  . CYS A 1 165 ? -9.969  -45.983 -44.600 1.00 40.99 ? 165 CYS A SG  1 
ATOM   1256 N N   . THR A 1 166 ? -10.873 -47.562 -41.619 1.00 39.08 ? 166 THR A N   1 
ATOM   1257 C CA  . THR A 1 166 ? -11.274 -46.694 -40.521 1.00 38.44 ? 166 THR A CA  1 
ATOM   1258 C C   . THR A 1 166 ? -10.187 -45.650 -40.318 1.00 37.94 ? 166 THR A C   1 
ATOM   1259 O O   . THR A 1 166 ? -9.006  -45.991 -40.217 1.00 37.90 ? 166 THR A O   1 
ATOM   1260 C CB  . THR A 1 166 ? -11.455 -47.478 -39.203 1.00 38.52 ? 166 THR A CB  1 
ATOM   1261 O OG1 . THR A 1 166 ? -11.970 -48.792 -39.481 1.00 38.56 ? 166 THR A OG1 1 
ATOM   1262 C CG2 . THR A 1 166 ? -12.405 -46.735 -38.262 1.00 38.69 ? 166 THR A CG2 1 
ATOM   1263 N N   . ILE A 1 167 ? -10.583 -44.381 -40.265 1.00 37.40 ? 167 ILE A N   1 
ATOM   1264 C CA  . ILE A 1 167 ? -9.642  -43.299 -39.971 1.00 36.83 ? 167 ILE A CA  1 
ATOM   1265 C C   . ILE A 1 167 ? -9.537  -43.125 -38.457 1.00 36.55 ? 167 ILE A C   1 
ATOM   1266 O O   . ILE A 1 167 ? -10.542 -42.890 -37.783 1.00 36.35 ? 167 ILE A O   1 
ATOM   1267 C CB  . ILE A 1 167 ? -10.048 -41.970 -40.647 1.00 36.74 ? 167 ILE A CB  1 
ATOM   1268 C CG1 . ILE A 1 167 ? -10.422 -42.186 -42.126 1.00 36.69 ? 167 ILE A CG1 1 
ATOM   1269 C CG2 . ILE A 1 167 ? -8.940  -40.934 -40.498 1.00 36.30 ? 167 ILE A CG2 1 
ATOM   1270 C CD1 . ILE A 1 167 ? -9.261  -42.605 -43.040 1.00 37.40 ? 167 ILE A CD1 1 
ATOM   1271 N N   . VAL A 1 168 ? -8.320  -43.253 -37.931 1.00 36.24 ? 168 VAL A N   1 
ATOM   1272 C CA  . VAL A 1 168 ? -8.108  -43.275 -36.482 1.00 36.07 ? 168 VAL A CA  1 
ATOM   1273 C C   . VAL A 1 168 ? -7.294  -42.090 -35.966 1.00 36.13 ? 168 VAL A C   1 
ATOM   1274 O O   . VAL A 1 168 ? -6.216  -41.784 -36.482 1.00 36.10 ? 168 VAL A O   1 
ATOM   1275 C CB  . VAL A 1 168 ? -7.453  -44.601 -36.011 1.00 35.93 ? 168 VAL A CB  1 
ATOM   1276 C CG1 . VAL A 1 168 ? -7.376  -44.654 -34.489 1.00 35.64 ? 168 VAL A CG1 1 
ATOM   1277 C CG2 . VAL A 1 168 ? -8.223  -45.803 -36.544 1.00 35.71 ? 168 VAL A CG2 1 
ATOM   1278 N N   . SER A 1 169 ? -7.835  -41.428 -34.945 1.00 36.21 ? 169 SER A N   1 
ATOM   1279 C CA  . SER A 1 169 ? -7.144  -40.358 -34.240 1.00 36.22 ? 169 SER A CA  1 
ATOM   1280 C C   . SER A 1 169 ? -6.383  -40.951 -33.059 1.00 36.31 ? 169 SER A C   1 
ATOM   1281 O O   . SER A 1 169 ? -6.990  -41.611 -32.208 1.00 36.33 ? 169 SER A O   1 
ATOM   1282 C CB  . SER A 1 169 ? -8.148  -39.314 -33.756 1.00 36.13 ? 169 SER A CB  1 
ATOM   1283 O OG  . SER A 1 169 ? -7.500  -38.207 -33.164 1.00 35.99 ? 169 SER A OG  1 
ATOM   1284 N N   . PRO A 1 170 ? -5.051  -40.730 -33.008 1.00 36.46 ? 170 PRO A N   1 
ATOM   1285 C CA  . PRO A 1 170 ? -4.184  -41.295 -31.964 1.00 36.56 ? 170 PRO A CA  1 
ATOM   1286 C C   . PRO A 1 170 ? -4.394  -40.689 -30.573 1.00 36.70 ? 170 PRO A C   1 
ATOM   1287 O O   . PRO A 1 170 ? -4.041  -41.315 -29.563 1.00 36.73 ? 170 PRO A O   1 
ATOM   1288 C CB  . PRO A 1 170 ? -2.772  -40.993 -32.477 1.00 36.52 ? 170 PRO A CB  1 
ATOM   1289 C CG  . PRO A 1 170 ? -2.929  -39.797 -33.341 1.00 36.50 ? 170 PRO A CG  1 
ATOM   1290 C CD  . PRO A 1 170 ? -4.288  -39.924 -33.980 1.00 36.46 ? 170 PRO A CD  1 
ATOM   1291 N N   . ASP A 1 171 ? -4.934  -39.473 -30.530 1.00 36.89 ? 171 ASP A N   1 
ATOM   1292 C CA  . ASP A 1 171 ? -5.366  -38.844 -29.278 1.00 36.93 ? 171 ASP A CA  1 
ATOM   1293 C C   . ASP A 1 171 ? -6.781  -38.299 -29.454 1.00 36.96 ? 171 ASP A C   1 
ATOM   1294 O O   . ASP A 1 171 ? -7.333  -38.357 -30.552 1.00 37.04 ? 171 ASP A O   1 
ATOM   1295 C CB  . ASP A 1 171 ? -4.385  -37.753 -28.808 1.00 36.91 ? 171 ASP A CB  1 
ATOM   1296 C CG  . ASP A 1 171 ? -4.089  -36.704 -29.878 1.00 37.13 ? 171 ASP A CG  1 
ATOM   1297 O OD1 . ASP A 1 171 ? -5.032  -36.115 -30.453 1.00 37.19 ? 171 ASP A OD1 1 
ATOM   1298 O OD2 . ASP A 1 171 ? -2.891  -36.452 -30.126 1.00 37.31 ? 171 ASP A OD2 1 
ATOM   1299 N N   . ALA A 1 172 ? -7.367  -37.783 -28.376 1.00 36.99 ? 172 ALA A N   1 
ATOM   1300 C CA  . ALA A 1 172 ? -8.739  -37.274 -28.417 1.00 36.98 ? 172 ALA A CA  1 
ATOM   1301 C C   . ALA A 1 172 ? -8.822  -35.880 -29.048 1.00 37.04 ? 172 ALA A C   1 
ATOM   1302 O O   . ALA A 1 172 ? -9.903  -35.433 -29.454 1.00 37.08 ? 172 ALA A O   1 
ATOM   1303 C CB  . ALA A 1 172 ? -9.346  -37.276 -27.020 1.00 37.06 ? 172 ALA A CB  1 
ATOM   1304 N N   . GLY A 1 173 ? -7.678  -35.202 -29.128 1.00 37.03 ? 173 GLY A N   1 
ATOM   1305 C CA  . GLY A 1 173 ? -7.591  -33.873 -29.735 1.00 36.97 ? 173 GLY A CA  1 
ATOM   1306 C C   . GLY A 1 173 ? -7.912  -33.857 -31.221 1.00 36.90 ? 173 GLY A C   1 
ATOM   1307 O O   . GLY A 1 173 ? -8.646  -32.987 -31.691 1.00 36.96 ? 173 GLY A O   1 
ATOM   1308 N N   . GLY A 1 174 ? -7.374  -34.831 -31.953 1.00 36.78 ? 174 GLY A N   1 
ATOM   1309 C CA  . GLY A 1 174 ? -7.529  -34.901 -33.406 1.00 36.64 ? 174 GLY A CA  1 
ATOM   1310 C C   . GLY A 1 174 ? -8.841  -35.491 -33.900 1.00 36.61 ? 174 GLY A C   1 
ATOM   1311 O O   . GLY A 1 174 ? -8.930  -35.954 -35.044 1.00 36.57 ? 174 GLY A O   1 
ATOM   1312 N N   . ALA A 1 175 ? -9.862  -35.467 -33.044 1.00 36.68 ? 175 ALA A N   1 
ATOM   1313 C CA  . ALA A 1 175 ? -11.188 -35.975 -33.400 1.00 36.65 ? 175 ALA A CA  1 
ATOM   1314 C C   . ALA A 1 175 ? -11.747 -35.296 -34.649 1.00 36.74 ? 175 ALA A C   1 
ATOM   1315 O O   . ALA A 1 175 ? -12.094 -35.975 -35.620 1.00 36.76 ? 175 ALA A O   1 
ATOM   1316 C CB  . ALA A 1 175 ? -12.152 -35.831 -32.227 1.00 36.66 ? 175 ALA A CB  1 
ATOM   1317 N N   . LYS A 1 176 ? -11.814 -33.963 -34.629 1.00 36.82 ? 176 LYS A N   1 
ATOM   1318 C CA  . LYS A 1 176 ? -12.325 -33.188 -35.768 1.00 36.88 ? 176 LYS A CA  1 
ATOM   1319 C C   . LYS A 1 176 ? -11.592 -33.529 -37.067 1.00 36.87 ? 176 LYS A C   1 
ATOM   1320 O O   . LYS A 1 176 ? -12.217 -33.699 -38.115 1.00 36.80 ? 176 LYS A O   1 
ATOM   1321 C CB  . LYS A 1 176 ? -12.252 -31.680 -35.492 1.00 36.77 ? 176 LYS A CB  1 
ATOM   1322 N N   . ARG A 1 177 ? -10.268 -33.646 -36.974 1.00 36.91 ? 177 ARG A N   1 
ATOM   1323 C CA  . ARG A 1 177 ? -9.421  -33.970 -38.116 1.00 36.99 ? 177 ARG A CA  1 
ATOM   1324 C C   . ARG A 1 177 ? -9.816  -35.289 -38.792 1.00 36.89 ? 177 ARG A C   1 
ATOM   1325 O O   . ARG A 1 177 ? -10.060 -35.310 -40.002 1.00 36.89 ? 177 ARG A O   1 
ATOM   1326 C CB  . ARG A 1 177 ? -7.946  -33.985 -37.699 1.00 37.07 ? 177 ARG A CB  1 
ATOM   1327 C CG  . ARG A 1 177 ? -6.973  -33.706 -38.836 1.00 37.97 ? 177 ARG A CG  1 
ATOM   1328 C CD  . ARG A 1 177 ? -5.524  -33.641 -38.360 1.00 39.12 ? 177 ARG A CD  1 
ATOM   1329 N NE  . ARG A 1 177 ? -5.263  -32.477 -37.510 1.00 40.14 ? 177 ARG A NE  1 
ATOM   1330 C CZ  . ARG A 1 177 ? -5.051  -32.532 -36.195 1.00 40.35 ? 177 ARG A CZ  1 
ATOM   1331 N NH1 . ARG A 1 177 ? -5.055  -33.699 -35.556 1.00 40.43 ? 177 ARG A NH1 1 
ATOM   1332 N NH2 . ARG A 1 177 ? -4.824  -31.415 -35.517 1.00 40.70 ? 177 ARG A NH2 1 
ATOM   1333 N N   . VAL A 1 178 ? -9.895  -36.375 -38.019 1.00 36.77 ? 178 VAL A N   1 
ATOM   1334 C CA  . VAL A 1 178 ? -10.185 -37.703 -38.590 1.00 36.68 ? 178 VAL A CA  1 
ATOM   1335 C C   . VAL A 1 178 ? -11.629 -37.854 -39.081 1.00 36.80 ? 178 VAL A C   1 
ATOM   1336 O O   . VAL A 1 178 ? -11.878 -38.561 -40.058 1.00 36.73 ? 178 VAL A O   1 
ATOM   1337 C CB  . VAL A 1 178 ? -9.790  -38.889 -37.646 1.00 36.60 ? 178 VAL A CB  1 
ATOM   1338 C CG1 . VAL A 1 178 ? -8.296  -38.866 -37.358 1.00 36.27 ? 178 VAL A CG1 1 
ATOM   1339 C CG2 . VAL A 1 178 ? -10.600 -38.886 -36.347 1.00 36.55 ? 178 VAL A CG2 1 
ATOM   1340 N N   . THR A 1 179 ? -12.565 -37.188 -38.408 1.00 37.03 ? 179 THR A N   1 
ATOM   1341 C CA  . THR A 1 179 ? -13.973 -37.191 -38.815 1.00 37.13 ? 179 THR A CA  1 
ATOM   1342 C C   . THR A 1 179 ? -14.173 -36.487 -40.153 1.00 37.29 ? 179 THR A C   1 
ATOM   1343 O O   . THR A 1 179 ? -14.987 -36.920 -40.969 1.00 37.32 ? 179 THR A O   1 
ATOM   1344 C CB  . THR A 1 179 ? -14.888 -36.515 -37.766 1.00 37.14 ? 179 THR A CB  1 
ATOM   1345 O OG1 . THR A 1 179 ? -14.288 -35.285 -37.326 1.00 37.26 ? 179 THR A OG1 1 
ATOM   1346 C CG2 . THR A 1 179 ? -15.125 -37.440 -36.572 1.00 36.92 ? 179 THR A CG2 1 
ATOM   1347 N N   . SER A 1 180 ? -13.433 -35.401 -40.366 1.00 37.57 ? 180 SER A N   1 
ATOM   1348 C CA  . SER A 1 180 ? -13.507 -34.643 -41.614 1.00 37.89 ? 180 SER A CA  1 
ATOM   1349 C C   . SER A 1 180 ? -12.978 -35.462 -42.786 1.00 38.11 ? 180 SER A C   1 
ATOM   1350 O O   . SER A 1 180 ? -13.544 -35.426 -43.881 1.00 38.16 ? 180 SER A O   1 
ATOM   1351 C CB  . SER A 1 180 ? -12.736 -33.330 -41.499 1.00 37.83 ? 180 SER A CB  1 
ATOM   1352 O OG  . SER A 1 180 ? -12.712 -32.676 -42.781 1.00 38.13 ? 180 SER A OG  1 
ATOM   1353 N N   . ILE A 1 181 ? -11.888 -36.191 -42.545 1.00 38.36 ? 181 ILE A N   1 
ATOM   1354 C CA  . ILE A 1 181 ? -11.321 -37.098 -43.536 1.00 38.67 ? 181 ILE A CA  1 
ATOM   1355 C C   . ILE A 1 181 ? -12.234 -38.311 -43.731 1.00 38.95 ? 181 ILE A C   1 
ATOM   1356 O O   . ILE A 1 181 ? -12.526 -38.692 -44.871 1.00 38.93 ? 181 ILE A O   1 
ATOM   1357 C CB  . ILE A 1 181 ? -9.863  -37.506 -43.174 1.00 38.67 ? 181 ILE A CB  1 
ATOM   1358 C CG1 . ILE A 1 181 ? -8.914  -36.331 -43.464 1.00 38.74 ? 181 ILE A CG1 1 
ATOM   1359 C CG2 . ILE A 1 181 ? -9.429  -38.766 -43.935 1.00 38.70 ? 181 ILE A CG2 1 
ATOM   1360 C CD1 . ILE A 1 181 ? -7.468  -36.545 -43.056 1.00 38.67 ? 181 ILE A CD1 1 
ATOM   1361 N N   . ALA A 1 182 ? -12.699 -38.888 -42.620 1.00 39.23 ? 182 ALA A N   1 
ATOM   1362 C CA  . ALA A 1 182 ? -13.591 -40.053 -42.649 1.00 39.49 ? 182 ALA A CA  1 
ATOM   1363 C C   . ALA A 1 182 ? -14.876 -39.797 -43.437 1.00 39.70 ? 182 ALA A C   1 
ATOM   1364 O O   . ALA A 1 182 ? -15.362 -40.689 -44.134 1.00 39.76 ? 182 ALA A O   1 
ATOM   1365 C CB  . ALA A 1 182 ? -13.916 -40.529 -41.230 1.00 39.35 ? 182 ALA A CB  1 
ATOM   1366 N N   . ASP A 1 183 ? -15.412 -38.577 -43.332 1.00 40.04 ? 183 ASP A N   1 
ATOM   1367 C CA  . ASP A 1 183 ? -16.650 -38.200 -44.026 1.00 40.43 ? 183 ASP A CA  1 
ATOM   1368 C C   . ASP A 1 183 ? -16.439 -37.973 -45.516 1.00 40.57 ? 183 ASP A C   1 
ATOM   1369 O O   . ASP A 1 183 ? -17.203 -38.474 -46.347 1.00 40.67 ? 183 ASP A O   1 
ATOM   1370 C CB  . ASP A 1 183 ? -17.265 -36.945 -43.403 1.00 40.47 ? 183 ASP A CB  1 
ATOM   1371 C CG  . ASP A 1 183 ? -17.936 -37.222 -42.080 1.00 40.83 ? 183 ASP A CG  1 
ATOM   1372 O OD1 . ASP A 1 183 ? -18.223 -38.403 -41.784 1.00 40.96 ? 183 ASP A OD1 1 
ATOM   1373 O OD2 . ASP A 1 183 ? -18.180 -36.248 -41.336 1.00 41.50 ? 183 ASP A OD2 1 
ATOM   1374 N N   . ARG A 1 184 ? -15.405 -37.199 -45.841 1.00 40.73 ? 184 ARG A N   1 
ATOM   1375 C CA  . ARG A 1 184 ? -15.044 -36.901 -47.223 1.00 40.82 ? 184 ARG A CA  1 
ATOM   1376 C C   . ARG A 1 184 ? -14.850 -38.190 -48.023 1.00 40.54 ? 184 ARG A C   1 
ATOM   1377 O O   . ARG A 1 184 ? -15.196 -38.267 -49.205 1.00 40.41 ? 184 ARG A O   1 
ATOM   1378 C CB  . ARG A 1 184 ? -13.767 -36.054 -47.246 1.00 40.97 ? 184 ARG A CB  1 
ATOM   1379 C CG  . ARG A 1 184 ? -13.595 -35.194 -48.494 1.00 42.29 ? 184 ARG A CG  1 
ATOM   1380 C CD  . ARG A 1 184 ? -14.545 -33.996 -48.512 1.00 44.57 ? 184 ARG A CD  1 
ATOM   1381 N NE  . ARG A 1 184 ? -14.391 -33.205 -49.735 1.00 46.36 ? 184 ARG A NE  1 
ATOM   1382 C CZ  . ARG A 1 184 ? -14.884 -33.562 -50.928 1.00 47.39 ? 184 ARG A CZ  1 
ATOM   1383 N NH1 . ARG A 1 184 ? -15.569 -34.709 -51.080 1.00 47.35 ? 184 ARG A NH1 1 
ATOM   1384 N NH2 . ARG A 1 184 ? -14.686 -32.771 -51.978 1.00 47.87 ? 184 ARG A NH2 1 
ATOM   1385 N N   . LEU A 1 185 ? -14.324 -39.206 -47.345 1.00 40.50 ? 185 LEU A N   1 
ATOM   1386 C CA  . LEU A 1 185 ? -14.039 -40.511 -47.925 1.00 40.43 ? 185 LEU A CA  1 
ATOM   1387 C C   . LEU A 1 185 ? -15.213 -41.472 -47.710 1.00 40.47 ? 185 LEU A C   1 
ATOM   1388 O O   . LEU A 1 185 ? -15.170 -42.628 -48.149 1.00 40.38 ? 185 LEU A O   1 
ATOM   1389 C CB  . LEU A 1 185 ? -12.781 -41.071 -47.256 1.00 40.39 ? 185 LEU A CB  1 
ATOM   1390 C CG  . LEU A 1 185 ? -11.736 -41.871 -48.034 1.00 40.24 ? 185 LEU A CG  1 
ATOM   1391 C CD1 . LEU A 1 185 ? -11.147 -41.068 -49.194 1.00 40.32 ? 185 LEU A CD1 1 
ATOM   1392 C CD2 . LEU A 1 185 ? -10.637 -42.289 -47.066 1.00 40.08 ? 185 LEU A CD2 1 
ATOM   1393 N N   . ASN A 1 186 ? -16.258 -40.969 -47.046 1.00 40.45 ? 186 ASN A N   1 
ATOM   1394 C CA  . ASN A 1 186 ? -17.415 -41.758 -46.590 1.00 40.43 ? 186 ASN A CA  1 
ATOM   1395 C C   . ASN A 1 186 ? -17.023 -43.093 -45.950 1.00 40.21 ? 186 ASN A C   1 
ATOM   1396 O O   . ASN A 1 186 ? -17.425 -44.167 -46.406 1.00 40.14 ? 186 ASN A O   1 
ATOM   1397 C CB  . ASN A 1 186 ? -18.464 -41.936 -47.701 1.00 40.50 ? 186 ASN A CB  1 
ATOM   1398 C CG  . ASN A 1 186 ? -19.822 -42.364 -47.156 1.00 41.01 ? 186 ASN A CG  1 
ATOM   1399 O OD1 . ASN A 1 186 ? -20.078 -43.551 -46.952 1.00 41.39 ? 186 ASN A OD1 1 
ATOM   1400 N ND2 . ASN A 1 186 ? -20.701 -41.393 -46.916 1.00 41.55 ? 186 ASN A ND2 1 
ATOM   1401 N N   . VAL A 1 187 ? -16.211 -43.006 -44.899 1.00 39.99 ? 187 VAL A N   1 
ATOM   1402 C CA  . VAL A 1 187 ? -15.799 -44.181 -44.131 1.00 39.66 ? 187 VAL A CA  1 
ATOM   1403 C C   . VAL A 1 187 ? -15.917 -43.937 -42.624 1.00 39.41 ? 187 VAL A C   1 
ATOM   1404 O O   . VAL A 1 187 ? -16.377 -42.872 -42.191 1.00 39.27 ? 187 VAL A O   1 
ATOM   1405 C CB  . VAL A 1 187 ? -14.361 -44.668 -44.502 1.00 39.72 ? 187 VAL A CB  1 
ATOM   1406 C CG1 . VAL A 1 187 ? -14.357 -45.328 -45.888 1.00 39.51 ? 187 VAL A CG1 1 
ATOM   1407 C CG2 . VAL A 1 187 ? -13.344 -43.523 -44.414 1.00 39.87 ? 187 VAL A CG2 1 
ATOM   1408 N N   . ASP A 1 188 ? -15.510 -44.931 -41.839 1.00 39.11 ? 188 ASP A N   1 
ATOM   1409 C CA  . ASP A 1 188 ? -15.649 -44.885 -40.393 1.00 38.92 ? 188 ASP A CA  1 
ATOM   1410 C C   . ASP A 1 188 ? -14.495 -44.140 -39.739 1.00 38.75 ? 188 ASP A C   1 
ATOM   1411 O O   . ASP A 1 188 ? -13.393 -44.080 -40.283 1.00 38.79 ? 188 ASP A O   1 
ATOM   1412 C CB  . ASP A 1 188 ? -15.724 -46.307 -39.818 1.00 39.05 ? 188 ASP A CB  1 
ATOM   1413 C CG  . ASP A 1 188 ? -17.031 -47.019 -40.148 1.00 39.16 ? 188 ASP A CG  1 
ATOM   1414 O OD1 . ASP A 1 188 ? -17.026 -48.264 -40.163 1.00 39.42 ? 188 ASP A OD1 1 
ATOM   1415 O OD2 . ASP A 1 188 ? -18.068 -46.352 -40.378 1.00 39.42 ? 188 ASP A OD2 1 
ATOM   1416 N N   . PHE A 1 189 ? -14.756 -43.571 -38.567 1.00 38.60 ? 189 PHE A N   1 
ATOM   1417 C CA  . PHE A 1 189 ? -13.688 -43.030 -37.734 1.00 38.39 ? 189 PHE A CA  1 
ATOM   1418 C C   . PHE A 1 189 ? -13.621 -43.779 -36.402 1.00 38.44 ? 189 PHE A C   1 
ATOM   1419 O O   . PHE A 1 189 ? -14.524 -44.553 -36.065 1.00 38.42 ? 189 PHE A O   1 
ATOM   1420 C CB  . PHE A 1 189 ? -13.867 -41.521 -37.512 1.00 38.27 ? 189 PHE A CB  1 
ATOM   1421 C CG  . PHE A 1 189 ? -14.982 -41.171 -36.562 1.00 37.57 ? 189 PHE A CG  1 
ATOM   1422 C CD1 . PHE A 1 189 ? -14.711 -40.889 -35.226 1.00 36.95 ? 189 PHE A CD1 1 
ATOM   1423 C CD2 . PHE A 1 189 ? -16.301 -41.118 -37.003 1.00 37.00 ? 189 PHE A CD2 1 
ATOM   1424 C CE1 . PHE A 1 189 ? -15.734 -40.565 -34.342 1.00 36.85 ? 189 PHE A CE1 1 
ATOM   1425 C CE2 . PHE A 1 189 ? -17.329 -40.794 -36.126 1.00 36.98 ? 189 PHE A CE2 1 
ATOM   1426 C CZ  . PHE A 1 189 ? -17.048 -40.516 -34.791 1.00 36.86 ? 189 PHE A CZ  1 
ATOM   1427 N N   . ALA A 1 190 ? -12.540 -43.546 -35.661 1.00 38.50 ? 190 ALA A N   1 
ATOM   1428 C CA  . ALA A 1 190 ? -12.355 -44.090 -34.318 1.00 38.53 ? 190 ALA A CA  1 
ATOM   1429 C C   . ALA A 1 190 ? -11.307 -43.254 -33.586 1.00 38.69 ? 190 ALA A C   1 
ATOM   1430 O O   . ALA A 1 190 ? -10.423 -42.661 -34.212 1.00 38.62 ? 190 ALA A O   1 
ATOM   1431 C CB  . ALA A 1 190 ? -11.928 -45.555 -34.381 1.00 38.50 ? 190 ALA A CB  1 
ATOM   1432 N N   . LEU A 1 191 ? -11.414 -43.207 -32.261 1.00 38.95 ? 191 LEU A N   1 
ATOM   1433 C CA  . LEU A 1 191 ? -10.517 -42.410 -31.431 1.00 39.17 ? 191 LEU A CA  1 
ATOM   1434 C C   . LEU A 1 191 ? -9.731  -43.286 -30.468 1.00 39.41 ? 191 LEU A C   1 
ATOM   1435 O O   . LEU A 1 191 ? -10.215 -44.326 -30.023 1.00 39.30 ? 191 LEU A O   1 
ATOM   1436 C CB  . LEU A 1 191 ? -11.313 -41.383 -30.613 1.00 39.15 ? 191 LEU A CB  1 
ATOM   1437 C CG  . LEU A 1 191 ? -11.755 -40.020 -31.158 1.00 39.18 ? 191 LEU A CG  1 
ATOM   1438 C CD1 . LEU A 1 191 ? -10.564 -39.184 -31.600 1.00 39.14 ? 191 LEU A CD1 1 
ATOM   1439 C CD2 . LEU A 1 191 ? -12.786 -40.143 -32.276 1.00 39.56 ? 191 LEU A CD2 1 
ATOM   1440 N N   . ILE A 1 192 ? -8.519  -42.841 -30.136 1.00 39.80 ? 192 ILE A N   1 
ATOM   1441 C CA  . ILE A 1 192 ? -7.721  -43.471 -29.095 1.00 40.21 ? 192 ILE A CA  1 
ATOM   1442 C C   . ILE A 1 192 ? -7.447  -42.458 -27.987 1.00 40.66 ? 192 ILE A C   1 
ATOM   1443 O O   . ILE A 1 192 ? -7.330  -41.258 -28.250 1.00 40.72 ? 192 ILE A O   1 
ATOM   1444 C CB  . ILE A 1 192 ? -6.417  -44.077 -29.665 1.00 40.20 ? 192 ILE A CB  1 
ATOM   1445 C CG1 . ILE A 1 192 ? -6.719  -45.438 -30.303 1.00 40.12 ? 192 ILE A CG1 1 
ATOM   1446 C CG2 . ILE A 1 192 ? -5.340  -44.195 -28.587 1.00 40.07 ? 192 ILE A CG2 1 
ATOM   1447 C CD1 . ILE A 1 192 ? -5.520  -46.125 -30.952 1.00 40.49 ? 192 ILE A CD1 1 
ATOM   1448 N N   . HIS A 1 193 ? -7.367  -42.942 -26.749 1.00 41.17 ? 193 HIS A N   1 
ATOM   1449 C CA  . HIS A 1 193 ? -7.152  -42.072 -25.602 1.00 41.82 ? 193 HIS A CA  1 
ATOM   1450 C C   . HIS A 1 193 ? -6.315  -42.733 -24.510 1.00 42.34 ? 193 HIS A C   1 
ATOM   1451 O O   . HIS A 1 193 ? -6.664  -43.807 -24.006 1.00 42.27 ? 193 HIS A O   1 
ATOM   1452 C CB  . HIS A 1 193 ? -8.498  -41.598 -25.041 1.00 41.68 ? 193 HIS A CB  1 
ATOM   1453 C CG  . HIS A 1 193 ? -8.386  -40.779 -23.792 1.00 41.57 ? 193 HIS A CG  1 
ATOM   1454 N ND1 . HIS A 1 193 ? -8.977  -41.154 -22.605 1.00 41.53 ? 193 HIS A ND1 1 
ATOM   1455 C CD2 . HIS A 1 193 ? -7.753  -39.607 -23.545 1.00 41.23 ? 193 HIS A CD2 1 
ATOM   1456 C CE1 . HIS A 1 193 ? -8.718  -40.245 -21.682 1.00 41.38 ? 193 HIS A CE1 1 
ATOM   1457 N NE2 . HIS A 1 193 ? -7.976  -39.297 -22.225 1.00 41.08 ? 193 HIS A NE2 1 
ATOM   1458 N N   . LYS A 1 194 ? -5.205  -42.086 -24.161 1.00 42.97 ? 194 LYS A N   1 
ATOM   1459 C CA  . LYS A 1 194 ? -4.414  -42.489 -23.007 1.00 43.72 ? 194 LYS A CA  1 
ATOM   1460 C C   . LYS A 1 194 ? -5.153  -42.024 -21.755 1.00 44.37 ? 194 LYS A C   1 
ATOM   1461 O O   . LYS A 1 194 ? -5.316  -40.819 -21.524 1.00 44.34 ? 194 LYS A O   1 
ATOM   1462 C CB  . LYS A 1 194 ? -3.009  -41.881 -23.065 1.00 43.56 ? 194 LYS A CB  1 
ATOM   1463 N N   . GLU A 1 195 ? -5.625  -42.982 -20.963 1.00 45.18 ? 195 GLU A N   1 
ATOM   1464 C CA  . GLU A 1 195 ? -6.376  -42.651 -19.763 1.00 45.98 ? 195 GLU A CA  1 
ATOM   1465 C C   . GLU A 1 195 ? -5.410  -42.230 -18.660 1.00 46.36 ? 195 GLU A C   1 
ATOM   1466 O O   . GLU A 1 195 ? -4.474  -42.967 -18.314 1.00 46.41 ? 195 GLU A O   1 
ATOM   1467 C CB  . GLU A 1 195 ? -7.276  -43.814 -19.319 1.00 46.07 ? 195 GLU A CB  1 
ATOM   1468 C CG  . GLU A 1 195 ? -8.286  -44.260 -20.388 1.00 46.89 ? 195 GLU A CG  1 
ATOM   1469 C CD  . GLU A 1 195 ? -9.688  -44.543 -19.819 1.00 48.15 ? 195 GLU A CD  1 
ATOM   1470 O OE1 . GLU A 1 195 ? -9.813  -44.855 -18.608 1.00 48.95 ? 195 GLU A OE1 1 
ATOM   1471 O OE2 . GLU A 1 195 ? -10.672 -44.456 -20.597 1.00 48.42 ? 195 GLU A OE2 1 
ATOM   1472 N N   . ARG A 1 196 ? -5.619  -41.005 -18.151 1.00 46.86 ? 196 ARG A N   1 
ATOM   1473 C CA  . ARG A 1 196 ? -4.837  -40.489 -17.033 1.00 47.25 ? 196 ARG A CA  1 
ATOM   1474 C C   . ARG A 1 196 ? -5.098  -41.349 -15.793 1.00 47.57 ? 196 ARG A C   1 
ATOM   1475 O O   . ARG A 1 196 ? -6.179  -41.273 -15.184 1.00 47.65 ? 196 ARG A O   1 
ATOM   1476 C CB  . ARG A 1 196 ? -5.178  -39.019 -16.768 1.00 47.22 ? 196 ARG A CB  1 
ATOM   1477 N N   . LYS A 1 197 ? -4.112  -42.182 -15.449 1.00 47.79 ? 197 LYS A N   1 
ATOM   1478 C CA  . LYS A 1 197 ? -4.209  -43.062 -14.291 1.00 47.92 ? 197 LYS A CA  1 
ATOM   1479 C C   . LYS A 1 197 ? -3.693  -42.353 -13.046 1.00 47.98 ? 197 LYS A C   1 
ATOM   1480 O O   . LYS A 1 197 ? -4.198  -41.295 -12.669 1.00 48.06 ? 197 LYS A O   1 
ATOM   1481 C CB  . LYS A 1 197 ? -3.439  -44.354 -14.535 1.00 48.01 ? 197 LYS A CB  1 
ATOM   1482 N N   . MET A 1 205 ? -4.730  -47.227 -22.345 1.00 41.05 ? 205 MET A N   1 
ATOM   1483 C CA  . MET A 1 205 ? -5.014  -46.762 -23.700 1.00 41.19 ? 205 MET A CA  1 
ATOM   1484 C C   . MET A 1 205 ? -6.276  -47.438 -24.231 1.00 41.07 ? 205 MET A C   1 
ATOM   1485 O O   . MET A 1 205 ? -6.293  -48.655 -24.451 1.00 41.04 ? 205 MET A O   1 
ATOM   1486 C CB  . MET A 1 205 ? -3.822  -47.044 -24.622 1.00 41.32 ? 205 MET A CB  1 
ATOM   1487 C CG  . MET A 1 205 ? -3.633  -46.021 -25.743 1.00 41.70 ? 205 MET A CG  1 
ATOM   1488 S SD  . MET A 1 205 ? -1.981  -46.126 -26.473 1.00 42.95 ? 205 MET A SD  1 
ATOM   1489 C CE  . MET A 1 205 ? -1.886  -44.603 -27.427 1.00 41.89 ? 205 MET A CE  1 
ATOM   1490 N N   . VAL A 1 206 ? -7.329  -46.643 -24.427 1.00 40.91 ? 206 VAL A N   1 
ATOM   1491 C CA  . VAL A 1 206 ? -8.616  -47.169 -24.891 1.00 40.81 ? 206 VAL A CA  1 
ATOM   1492 C C   . VAL A 1 206 ? -8.916  -46.782 -26.337 1.00 40.69 ? 206 VAL A C   1 
ATOM   1493 O O   . VAL A 1 206 ? -8.397  -45.790 -26.842 1.00 40.58 ? 206 VAL A O   1 
ATOM   1494 C CB  . VAL A 1 206 ? -9.807  -46.753 -23.966 1.00 40.80 ? 206 VAL A CB  1 
ATOM   1495 C CG1 . VAL A 1 206 ? -9.586  -47.257 -22.545 1.00 41.05 ? 206 VAL A CG1 1 
ATOM   1496 C CG2 . VAL A 1 206 ? -10.018 -45.248 -23.971 1.00 40.74 ? 206 VAL A CG2 1 
ATOM   1497 N N   . LEU A 1 207 ? -9.751  -47.585 -26.991 1.00 40.75 ? 207 LEU A N   1 
ATOM   1498 C CA  . LEU A 1 207 ? -10.214 -47.298 -28.345 1.00 40.82 ? 207 LEU A CA  1 
ATOM   1499 C C   . LEU A 1 207 ? -11.737 -47.234 -28.391 1.00 40.83 ? 207 LEU A C   1 
ATOM   1500 O O   . LEU A 1 207 ? -12.423 -48.138 -27.904 1.00 40.89 ? 207 LEU A O   1 
ATOM   1501 C CB  . LEU A 1 207 ? -9.697  -48.356 -29.333 1.00 40.84 ? 207 LEU A CB  1 
ATOM   1502 C CG  . LEU A 1 207 ? -10.239 -48.365 -30.774 1.00 40.95 ? 207 LEU A CG  1 
ATOM   1503 C CD1 . LEU A 1 207 ? -9.896  -47.090 -31.531 1.00 41.28 ? 207 LEU A CD1 1 
ATOM   1504 C CD2 . LEU A 1 207 ? -9.725  -49.575 -31.535 1.00 41.16 ? 207 LEU A CD2 1 
ATOM   1505 N N   . VAL A 1 208 ? -12.258 -46.156 -28.967 1.00 40.77 ? 208 VAL A N   1 
ATOM   1506 C CA  . VAL A 1 208 ? -13.689 -46.057 -29.244 1.00 40.72 ? 208 VAL A CA  1 
ATOM   1507 C C   . VAL A 1 208 ? -13.917 -46.093 -30.754 1.00 40.69 ? 208 VAL A C   1 
ATOM   1508 O O   . VAL A 1 208 ? -13.198 -45.443 -31.510 1.00 40.66 ? 208 VAL A O   1 
ATOM   1509 C CB  . VAL A 1 208 ? -14.350 -44.818 -28.570 1.00 40.70 ? 208 VAL A CB  1 
ATOM   1510 C CG1 . VAL A 1 208 ? -14.074 -44.830 -27.051 1.00 40.51 ? 208 VAL A CG1 1 
ATOM   1511 C CG2 . VAL A 1 208 ? -13.875 -43.505 -29.211 1.00 40.64 ? 208 VAL A CG2 1 
ATOM   1512 N N   . GLY A 1 209 ? -14.905 -46.869 -31.184 1.00 40.73 ? 209 GLY A N   1 
ATOM   1513 C CA  . GLY A 1 209 ? -15.125 -47.105 -32.609 1.00 40.93 ? 209 GLY A CA  1 
ATOM   1514 C C   . GLY A 1 209 ? -14.578 -48.453 -33.045 1.00 41.10 ? 209 GLY A C   1 
ATOM   1515 O O   . GLY A 1 209 ? -13.630 -48.976 -32.448 1.00 41.08 ? 209 GLY A O   1 
ATOM   1516 N N   . ASP A 1 210 ? -15.182 -49.011 -34.093 1.00 41.35 ? 210 ASP A N   1 
ATOM   1517 C CA  . ASP A 1 210 ? -14.824 -50.342 -34.582 1.00 41.65 ? 210 ASP A CA  1 
ATOM   1518 C C   . ASP A 1 210 ? -13.758 -50.272 -35.669 1.00 41.76 ? 210 ASP A C   1 
ATOM   1519 O O   . ASP A 1 210 ? -13.818 -49.424 -36.562 1.00 41.76 ? 210 ASP A O   1 
ATOM   1520 C CB  . ASP A 1 210 ? -16.064 -51.081 -35.098 1.00 41.63 ? 210 ASP A CB  1 
ATOM   1521 N N   . VAL A 1 211 ? -12.786 -51.176 -35.580 1.00 41.91 ? 211 VAL A N   1 
ATOM   1522 C CA  . VAL A 1 211 ? -11.656 -51.214 -36.505 1.00 42.10 ? 211 VAL A CA  1 
ATOM   1523 C C   . VAL A 1 211 ? -11.433 -52.645 -37.020 1.00 42.26 ? 211 VAL A C   1 
ATOM   1524 O O   . VAL A 1 211 ? -10.698 -52.858 -37.990 1.00 42.26 ? 211 VAL A O   1 
ATOM   1525 C CB  . VAL A 1 211 ? -10.366 -50.669 -35.823 1.00 42.10 ? 211 VAL A CB  1 
ATOM   1526 C CG1 . VAL A 1 211 ? -9.165  -50.793 -36.737 1.00 42.19 ? 211 VAL A CG1 1 
ATOM   1527 C CG2 . VAL A 1 211 ? -10.543 -49.212 -35.402 1.00 41.98 ? 211 VAL A CG2 1 
ATOM   1528 N N   . LYS A 1 212 ? -12.101 -53.605 -36.378 1.00 42.45 ? 212 LYS A N   1 
ATOM   1529 C CA  . LYS A 1 212 ? -11.913 -55.043 -36.617 1.00 42.54 ? 212 LYS A CA  1 
ATOM   1530 C C   . LYS A 1 212 ? -12.027 -55.467 -38.087 1.00 42.45 ? 212 LYS A C   1 
ATOM   1531 O O   . LYS A 1 212 ? -12.970 -55.080 -38.784 1.00 42.40 ? 212 LYS A O   1 
ATOM   1532 C CB  . LYS A 1 212 ? -12.902 -55.848 -35.764 1.00 42.66 ? 212 LYS A CB  1 
ATOM   1533 C CG  . LYS A 1 212 ? -12.469 -57.304 -35.521 1.00 43.45 ? 212 LYS A CG  1 
ATOM   1534 C CD  . LYS A 1 212 ? -13.642 -58.143 -35.029 1.00 44.41 ? 212 LYS A CD  1 
ATOM   1535 C CE  . LYS A 1 212 ? -13.287 -59.632 -35.063 1.00 45.02 ? 212 LYS A CE  1 
ATOM   1536 N NZ  . LYS A 1 212 ? -14.563 -60.486 -35.083 1.00 45.45 ? 212 LYS A NZ  1 
ATOM   1537 N N   . ASP A 1 213 ? -11.052 -56.266 -38.529 1.00 42.39 ? 213 ASP A N   1 
ATOM   1538 C CA  . ASP A 1 213 ? -10.984 -56.845 -39.887 1.00 42.41 ? 213 ASP A CA  1 
ATOM   1539 C C   . ASP A 1 213 ? -11.057 -55.819 -41.029 1.00 42.28 ? 213 ASP A C   1 
ATOM   1540 O O   . ASP A 1 213 ? -11.725 -56.036 -42.047 1.00 42.33 ? 213 ASP A O   1 
ATOM   1541 C CB  . ASP A 1 213 ? -12.026 -57.972 -40.063 1.00 42.47 ? 213 ASP A CB  1 
ATOM   1542 C CG  . ASP A 1 213 ? -11.788 -59.125 -39.092 1.00 42.90 ? 213 ASP A CG  1 
ATOM   1543 O OD1 . ASP A 1 213 ? -10.626 -59.337 -38.661 1.00 43.28 ? 213 ASP A OD1 1 
ATOM   1544 O OD2 . ASP A 1 213 ? -12.767 -59.822 -38.760 1.00 43.45 ? 213 ASP A OD2 1 
ATOM   1545 N N   . ARG A 1 214 ? -10.354 -54.705 -40.837 1.00 42.00 ? 214 ARG A N   1 
ATOM   1546 C CA  . ARG A 1 214 ? -10.251 -53.635 -41.825 1.00 41.73 ? 214 ARG A CA  1 
ATOM   1547 C C   . ARG A 1 214 ? -8.921  -52.905 -41.625 1.00 41.32 ? 214 ARG A C   1 
ATOM   1548 O O   . ARG A 1 214 ? -8.272  -53.058 -40.585 1.00 41.34 ? 214 ARG A O   1 
ATOM   1549 C CB  . ARG A 1 214 ? -11.409 -52.650 -41.662 1.00 41.94 ? 214 ARG A CB  1 
ATOM   1550 C CG  . ARG A 1 214 ? -12.779 -53.185 -42.090 1.00 42.61 ? 214 ARG A CG  1 
ATOM   1551 C CD  . ARG A 1 214 ? -13.834 -52.848 -41.053 1.00 43.98 ? 214 ARG A CD  1 
ATOM   1552 N NE  . ARG A 1 214 ? -13.814 -51.430 -40.706 1.00 45.09 ? 214 ARG A NE  1 
ATOM   1553 C CZ  . ARG A 1 214 ? -14.791 -50.573 -40.987 1.00 45.88 ? 214 ARG A CZ  1 
ATOM   1554 N NH1 . ARG A 1 214 ? -15.897 -50.985 -41.609 1.00 46.15 ? 214 ARG A NH1 1 
ATOM   1555 N NH2 . ARG A 1 214 ? -14.663 -49.303 -40.632 1.00 46.22 ? 214 ARG A NH2 1 
ATOM   1556 N N   . VAL A 1 215 ? -8.501  -52.126 -42.614 1.00 40.64 ? 215 VAL A N   1 
ATOM   1557 C CA  . VAL A 1 215 ? -7.266  -51.352 -42.466 1.00 39.99 ? 215 VAL A CA  1 
ATOM   1558 C C   . VAL A 1 215 ? -7.546  -50.065 -41.701 1.00 39.46 ? 215 VAL A C   1 
ATOM   1559 O O   . VAL A 1 215 ? -8.514  -49.367 -41.994 1.00 39.51 ? 215 VAL A O   1 
ATOM   1560 C CB  . VAL A 1 215 ? -6.573  -51.053 -43.831 1.00 40.14 ? 215 VAL A CB  1 
ATOM   1561 C CG1 . VAL A 1 215 ? -7.610  -50.776 -44.936 1.00 40.09 ? 215 VAL A CG1 1 
ATOM   1562 C CG2 . VAL A 1 215 ? -5.578  -49.892 -43.684 1.00 40.15 ? 215 VAL A CG2 1 
ATOM   1563 N N   . ALA A 1 216 ? -6.704  -49.770 -40.708 1.00 38.70 ? 216 ALA A N   1 
ATOM   1564 C CA  . ALA A 1 216 ? -6.807  -48.516 -39.968 1.00 38.00 ? 216 ALA A CA  1 
ATOM   1565 C C   . ALA A 1 216 ? -5.747  -47.519 -40.427 1.00 37.45 ? 216 ALA A C   1 
ATOM   1566 O O   . ALA A 1 216 ? -4.559  -47.846 -40.474 1.00 37.32 ? 216 ALA A O   1 
ATOM   1567 C CB  . ALA A 1 216 ? -6.683  -48.771 -38.470 1.00 38.03 ? 216 ALA A CB  1 
ATOM   1568 N N   . ILE A 1 217 ? -6.182  -46.310 -40.774 1.00 36.89 ? 217 ILE A N   1 
ATOM   1569 C CA  . ILE A 1 217 ? -5.250  -45.214 -41.055 1.00 36.42 ? 217 ILE A CA  1 
ATOM   1570 C C   . ILE A 1 217 ? -5.190  -44.242 -39.877 1.00 36.07 ? 217 ILE A C   1 
ATOM   1571 O O   . ILE A 1 217 ? -6.181  -43.580 -39.554 1.00 35.73 ? 217 ILE A O   1 
ATOM   1572 C CB  . ILE A 1 217 ? -5.616  -44.416 -42.334 1.00 36.47 ? 217 ILE A CB  1 
ATOM   1573 C CG1 . ILE A 1 217 ? -5.890  -45.352 -43.515 1.00 36.53 ? 217 ILE A CG1 1 
ATOM   1574 C CG2 . ILE A 1 217 ? -4.500  -43.419 -42.681 1.00 36.30 ? 217 ILE A CG2 1 
ATOM   1575 C CD1 . ILE A 1 217 ? -6.591  -44.651 -44.688 1.00 36.30 ? 217 ILE A CD1 1 
ATOM   1576 N N   . LEU A 1 218 ? -4.021  -44.177 -39.241 1.00 35.83 ? 218 LEU A N   1 
ATOM   1577 C CA  . LEU A 1 218 ? -3.730  -43.179 -38.215 1.00 35.70 ? 218 LEU A CA  1 
ATOM   1578 C C   . LEU A 1 218 ? -3.530  -41.823 -38.861 1.00 35.67 ? 218 LEU A C   1 
ATOM   1579 O O   . LEU A 1 218 ? -2.593  -41.641 -39.640 1.00 35.61 ? 218 LEU A O   1 
ATOM   1580 C CB  . LEU A 1 218 ? -2.453  -43.552 -37.454 1.00 35.75 ? 218 LEU A CB  1 
ATOM   1581 C CG  . LEU A 1 218 ? -2.464  -43.982 -35.982 1.00 35.62 ? 218 LEU A CG  1 
ATOM   1582 C CD1 . LEU A 1 218 ? -3.851  -44.091 -35.396 1.00 35.69 ? 218 LEU A CD1 1 
ATOM   1583 C CD2 . LEU A 1 218 ? -1.660  -45.277 -35.782 1.00 35.71 ? 218 LEU A CD2 1 
ATOM   1584 N N   . VAL A 1 219 ? -4.407  -40.875 -38.539 1.00 35.73 ? 219 VAL A N   1 
ATOM   1585 C CA  . VAL A 1 219 ? -4.263  -39.509 -39.039 1.00 35.88 ? 219 VAL A CA  1 
ATOM   1586 C C   . VAL A 1 219 ? -4.016  -38.506 -37.912 1.00 36.08 ? 219 VAL A C   1 
ATOM   1587 O O   . VAL A 1 219 ? -4.793  -38.409 -36.954 1.00 36.01 ? 219 VAL A O   1 
ATOM   1588 C CB  . VAL A 1 219 ? -5.462  -39.066 -39.912 1.00 35.82 ? 219 VAL A CB  1 
ATOM   1589 C CG1 . VAL A 1 219 ? -5.264  -37.625 -40.389 1.00 35.89 ? 219 VAL A CG1 1 
ATOM   1590 C CG2 . VAL A 1 219 ? -5.612  -39.989 -41.115 1.00 35.65 ? 219 VAL A CG2 1 
ATOM   1591 N N   . ASP A 1 220 ? -2.913  -37.771 -38.043 1.00 36.32 ? 220 ASP A N   1 
ATOM   1592 C CA  . ASP A 1 220 ? -2.564  -36.713 -37.107 1.00 36.65 ? 220 ASP A CA  1 
ATOM   1593 C C   . ASP A 1 220 ? -1.915  -35.561 -37.877 1.00 36.86 ? 220 ASP A C   1 
ATOM   1594 O O   . ASP A 1 220 ? -1.467  -35.746 -39.011 1.00 36.80 ? 220 ASP A O   1 
ATOM   1595 C CB  . ASP A 1 220 ? -1.623  -37.255 -36.028 1.00 36.70 ? 220 ASP A CB  1 
ATOM   1596 C CG  . ASP A 1 220 ? -1.744  -36.510 -34.707 1.00 36.75 ? 220 ASP A CG  1 
ATOM   1597 O OD1 . ASP A 1 220 ? -2.699  -35.714 -34.532 1.00 36.61 ? 220 ASP A OD1 1 
ATOM   1598 O OD2 . ASP A 1 220 ? -0.880  -36.737 -33.832 1.00 36.80 ? 220 ASP A OD2 1 
ATOM   1599 N N   . ASP A 1 221 ? -1.882  -34.372 -37.278 1.00 37.19 ? 221 ASP A N   1 
ATOM   1600 C CA  . ASP A 1 221 ? -1.314  -33.212 -37.965 1.00 37.57 ? 221 ASP A CA  1 
ATOM   1601 C C   . ASP A 1 221 ? 0.205   -33.247 -37.931 1.00 37.80 ? 221 ASP A C   1 
ATOM   1602 O O   . ASP A 1 221 ? 0.868   -32.921 -38.921 1.00 37.79 ? 221 ASP A O   1 
ATOM   1603 C CB  . ASP A 1 221 ? -1.837  -31.900 -37.374 1.00 37.55 ? 221 ASP A CB  1 
ATOM   1604 C CG  . ASP A 1 221 ? -1.273  -31.606 -35.998 1.00 37.79 ? 221 ASP A CG  1 
ATOM   1605 O OD1 . ASP A 1 221 ? -1.055  -32.558 -35.215 1.00 38.28 ? 221 ASP A OD1 1 
ATOM   1606 O OD2 . ASP A 1 221 ? -1.045  -30.416 -35.701 1.00 38.21 ? 221 ASP A OD2 1 
ATOM   1607 N N   . MET A 1 222 ? 0.747   -33.653 -36.783 1.00 38.10 ? 222 MET A N   1 
ATOM   1608 C CA  . MET A 1 222 ? 2.186   -33.715 -36.604 1.00 38.45 ? 222 MET A CA  1 
ATOM   1609 C C   . MET A 1 222 ? 2.617   -34.822 -35.643 1.00 38.50 ? 222 MET A C   1 
ATOM   1610 O O   . MET A 1 222 ? 1.870   -35.219 -34.745 1.00 38.50 ? 222 MET A O   1 
ATOM   1611 C CB  . MET A 1 222 ? 2.734   -32.343 -36.185 1.00 38.54 ? 222 MET A CB  1 
ATOM   1612 C CG  . MET A 1 222 ? 2.798   -32.058 -34.688 1.00 39.25 ? 222 MET A CG  1 
ATOM   1613 S SD  . MET A 1 222 ? 3.243   -30.333 -34.325 1.00 41.07 ? 222 MET A SD  1 
ATOM   1614 C CE  . MET A 1 222 ? 4.419   -29.951 -35.626 1.00 39.93 ? 222 MET A CE  1 
ATOM   1615 N N   . ALA A 1 223 ? 3.830   -35.329 -35.873 1.00 38.70 ? 223 ALA A N   1 
ATOM   1616 C CA  . ALA A 1 223 ? 4.443   -36.322 -35.002 1.00 38.96 ? 223 ALA A CA  1 
ATOM   1617 C C   . ALA A 1 223 ? 5.874   -35.905 -34.726 1.00 39.23 ? 223 ALA A C   1 
ATOM   1618 O O   . ALA A 1 223 ? 6.489   -35.192 -35.531 1.00 39.29 ? 223 ALA A O   1 
ATOM   1619 C CB  . ALA A 1 223 ? 4.414   -37.688 -35.644 1.00 38.79 ? 223 ALA A CB  1 
ATOM   1620 N N   . ASP A 1 224 ? 6.396   -36.353 -33.588 1.00 39.58 ? 224 ASP A N   1 
ATOM   1621 C CA  . ASP A 1 224 ? 7.758   -36.040 -33.214 1.00 39.99 ? 224 ASP A CA  1 
ATOM   1622 C C   . ASP A 1 224 ? 8.493   -37.330 -32.864 1.00 40.35 ? 224 ASP A C   1 
ATOM   1623 O O   . ASP A 1 224 ? 9.121   -37.942 -33.727 1.00 40.48 ? 224 ASP A O   1 
ATOM   1624 C CB  . ASP A 1 224 ? 7.768   -35.045 -32.049 1.00 39.88 ? 224 ASP A CB  1 
ATOM   1625 C CG  . ASP A 1 224 ? 9.163   -34.594 -31.681 1.00 40.03 ? 224 ASP A CG  1 
ATOM   1626 O OD1 . ASP A 1 224 ? 10.068  -34.717 -32.539 1.00 39.19 ? 224 ASP A OD1 1 
ATOM   1627 O OD2 . ASP A 1 224 ? 9.349   -34.113 -30.534 1.00 40.24 ? 224 ASP A OD2 1 
ATOM   1628 N N   . THR A 1 225 ? 8.391   -37.747 -31.604 1.00 40.67 ? 225 THR A N   1 
ATOM   1629 C CA  . THR A 1 225 ? 9.081   -38.937 -31.123 1.00 40.97 ? 225 THR A CA  1 
ATOM   1630 C C   . THR A 1 225 ? 8.420   -40.217 -31.652 1.00 41.01 ? 225 THR A C   1 
ATOM   1631 O O   . THR A 1 225 ? 9.059   -41.274 -31.709 1.00 41.02 ? 225 THR A O   1 
ATOM   1632 C CB  . THR A 1 225 ? 9.135   -38.952 -29.585 1.00 41.07 ? 225 THR A CB  1 
ATOM   1633 O OG1 . THR A 1 225 ? 7.801   -38.941 -29.052 1.00 41.19 ? 225 THR A OG1 1 
ATOM   1634 C CG2 . THR A 1 225 ? 9.918   -37.730 -29.060 1.00 41.05 ? 225 THR A CG2 1 
ATOM   1635 N N   . CYS A 1 226 ? 7.143   -40.095 -32.038 1.00 40.99 ? 226 CYS A N   1 
ATOM   1636 C CA  . CYS A 1 226 ? 6.336   -41.181 -32.630 1.00 40.97 ? 226 CYS A CA  1 
ATOM   1637 C C   . CYS A 1 226 ? 5.758   -42.175 -31.619 1.00 40.88 ? 226 CYS A C   1 
ATOM   1638 O O   . CYS A 1 226 ? 5.086   -43.132 -32.006 1.00 40.72 ? 226 CYS A O   1 
ATOM   1639 C CB  . CYS A 1 226 ? 7.089   -41.903 -33.753 1.00 40.98 ? 226 CYS A CB  1 
ATOM   1640 S SG  . CYS A 1 226 ? 7.307   -40.890 -35.223 1.00 41.08 ? 226 CYS A SG  1 
ATOM   1641 N N   . GLY A 1 227 ? 6.001   -41.927 -30.333 1.00 40.90 ? 227 GLY A N   1 
ATOM   1642 C CA  . GLY A 1 227 ? 5.511   -42.787 -29.253 1.00 40.93 ? 227 GLY A CA  1 
ATOM   1643 C C   . GLY A 1 227 ? 4.008   -43.000 -29.267 1.00 40.94 ? 227 GLY A C   1 
ATOM   1644 O O   . GLY A 1 227 ? 3.526   -44.136 -29.145 1.00 40.98 ? 227 GLY A O   1 
ATOM   1645 N N   . THR A 1 228 ? 3.276   -41.901 -29.435 1.00 40.92 ? 228 THR A N   1 
ATOM   1646 C CA  . THR A 1 228 ? 1.818   -41.921 -29.477 1.00 40.92 ? 228 THR A CA  1 
ATOM   1647 C C   . THR A 1 228 ? 1.285   -42.732 -30.665 1.00 40.88 ? 228 THR A C   1 
ATOM   1648 O O   . THR A 1 228 ? 0.487   -43.645 -30.467 1.00 40.95 ? 228 THR A O   1 
ATOM   1649 C CB  . THR A 1 228 ? 1.235   -40.490 -29.471 1.00 40.98 ? 228 THR A CB  1 
ATOM   1650 O OG1 . THR A 1 228 ? 1.809   -39.748 -28.380 1.00 41.34 ? 228 THR A OG1 1 
ATOM   1651 C CG2 . THR A 1 228 ? -0.287  -40.521 -29.322 1.00 40.83 ? 228 THR A CG2 1 
ATOM   1652 N N   . ILE A 1 229 ? 1.728   -42.422 -31.886 1.00 40.79 ? 229 ILE A N   1 
ATOM   1653 C CA  . ILE A 1 229 ? 1.298   -43.212 -33.048 1.00 40.66 ? 229 ILE A CA  1 
ATOM   1654 C C   . ILE A 1 229 ? 1.774   -44.666 -32.964 1.00 40.85 ? 229 ILE A C   1 
ATOM   1655 O O   . ILE A 1 229 ? 1.165   -45.556 -33.564 1.00 40.90 ? 229 ILE A O   1 
ATOM   1656 C CB  . ILE A 1 229 ? 1.680   -42.584 -34.436 1.00 40.53 ? 229 ILE A CB  1 
ATOM   1657 C CG1 . ILE A 1 229 ? 3.196   -42.367 -34.572 1.00 40.19 ? 229 ILE A CG1 1 
ATOM   1658 C CG2 . ILE A 1 229 ? 0.884   -41.298 -34.692 1.00 40.23 ? 229 ILE A CG2 1 
ATOM   1659 C CD1 . ILE A 1 229 ? 3.678   -42.301 -36.029 1.00 39.39 ? 229 ILE A CD1 1 
ATOM   1660 N N   . CYS A 1 230 ? 2.850   -44.900 -32.211 1.00 40.94 ? 230 CYS A N   1 
ATOM   1661 C CA  . CYS A 1 230 ? 3.379   -46.253 -32.035 1.00 41.14 ? 230 CYS A CA  1 
ATOM   1662 C C   . CYS A 1 230 ? 2.544   -47.110 -31.085 1.00 40.97 ? 230 CYS A C   1 
ATOM   1663 O O   . CYS A 1 230 ? 2.199   -48.249 -31.421 1.00 40.96 ? 230 CYS A O   1 
ATOM   1664 C CB  . CYS A 1 230 ? 4.852   -46.233 -31.626 1.00 41.15 ? 230 CYS A CB  1 
ATOM   1665 S SG  . CYS A 1 230 ? 5.966   -46.056 -33.058 1.00 42.58 ? 230 CYS A SG  1 
ATOM   1666 N N   . HIS A 1 231 ? 2.216   -46.569 -29.911 1.00 40.80 ? 231 HIS A N   1 
ATOM   1667 C CA  . HIS A 1 231 ? 1.339   -47.278 -28.973 1.00 40.71 ? 231 HIS A CA  1 
ATOM   1668 C C   . HIS A 1 231 ? -0.094  -47.358 -29.508 1.00 40.47 ? 231 HIS A C   1 
ATOM   1669 O O   . HIS A 1 231 ? -0.840  -48.287 -29.179 1.00 40.39 ? 231 HIS A O   1 
ATOM   1670 C CB  . HIS A 1 231 ? 1.366   -46.633 -27.575 1.00 40.84 ? 231 HIS A CB  1 
ATOM   1671 C CG  . HIS A 1 231 ? 2.739   -46.562 -26.974 1.00 41.62 ? 231 HIS A CG  1 
ATOM   1672 N ND1 . HIS A 1 231 ? 3.689   -47.564 -27.143 1.00 42.30 ? 231 HIS A ND1 1 
ATOM   1673 C CD2 . HIS A 1 231 ? 3.317   -45.618 -26.190 1.00 42.09 ? 231 HIS A CD2 1 
ATOM   1674 C CE1 . HIS A 1 231 ? 4.795   -47.233 -26.500 1.00 42.62 ? 231 HIS A CE1 1 
ATOM   1675 N NE2 . HIS A 1 231 ? 4.595   -46.057 -25.911 1.00 42.60 ? 231 HIS A NE2 1 
ATOM   1676 N N   . ALA A 1 232 ? -0.463  -46.384 -30.338 1.00 40.16 ? 232 ALA A N   1 
ATOM   1677 C CA  . ALA A 1 232 ? -1.753  -46.391 -31.020 1.00 39.94 ? 232 ALA A CA  1 
ATOM   1678 C C   . ALA A 1 232 ? -1.845  -47.520 -32.046 1.00 39.76 ? 232 ALA A C   1 
ATOM   1679 O O   . ALA A 1 232 ? -2.888  -48.170 -32.161 1.00 39.71 ? 232 ALA A O   1 
ATOM   1680 C CB  . ALA A 1 232 ? -2.015  -45.048 -31.685 1.00 39.96 ? 232 ALA A CB  1 
ATOM   1681 N N   . ALA A 1 233 ? -0.752  -47.748 -32.782 1.00 39.51 ? 233 ALA A N   1 
ATOM   1682 C CA  . ALA A 1 233 ? -0.711  -48.794 -33.809 1.00 39.40 ? 233 ALA A CA  1 
ATOM   1683 C C   . ALA A 1 233 ? -0.839  -50.191 -33.198 1.00 39.33 ? 233 ALA A C   1 
ATOM   1684 O O   . ALA A 1 233 ? -1.497  -51.074 -33.761 1.00 39.06 ? 233 ALA A O   1 
ATOM   1685 C CB  . ALA A 1 233 ? 0.564   -48.682 -34.639 1.00 39.26 ? 233 ALA A CB  1 
ATOM   1686 N N   . ASP A 1 234 ? -0.211  -50.371 -32.039 1.00 39.36 ? 234 ASP A N   1 
ATOM   1687 C CA  . ASP A 1 234 ? -0.284  -51.624 -31.300 1.00 39.51 ? 234 ASP A CA  1 
ATOM   1688 C C   . ASP A 1 234 ? -1.691  -51.885 -30.758 1.00 39.38 ? 234 ASP A C   1 
ATOM   1689 O O   . ASP A 1 234 ? -2.206  -53.007 -30.862 1.00 39.49 ? 234 ASP A O   1 
ATOM   1690 C CB  . ASP A 1 234 ? 0.768   -51.646 -30.189 1.00 39.61 ? 234 ASP A CB  1 
ATOM   1691 C CG  . ASP A 1 234 ? 2.190   -51.568 -30.736 1.00 40.40 ? 234 ASP A CG  1 
ATOM   1692 O OD1 . ASP A 1 234 ? 2.441   -52.128 -31.830 1.00 41.12 ? 234 ASP A OD1 1 
ATOM   1693 O OD2 . ASP A 1 234 ? 3.058   -50.946 -30.079 1.00 40.80 ? 234 ASP A OD2 1 
ATOM   1694 N N   . LYS A 1 235 ? -2.319  -50.852 -30.198 1.00 39.22 ? 235 LYS A N   1 
ATOM   1695 C CA  . LYS A 1 235 ? -3.705  -50.964 -29.757 1.00 39.14 ? 235 LYS A CA  1 
ATOM   1696 C C   . LYS A 1 235 ? -4.570  -51.366 -30.948 1.00 39.05 ? 235 LYS A C   1 
ATOM   1697 O O   . LYS A 1 235 ? -5.373  -52.298 -30.853 1.00 39.00 ? 235 LYS A O   1 
ATOM   1698 C CB  . LYS A 1 235 ? -4.208  -49.655 -29.136 1.00 39.22 ? 235 LYS A CB  1 
ATOM   1699 N N   . LEU A 1 236 ? -4.373  -50.678 -32.074 1.00 38.97 ? 236 LEU A N   1 
ATOM   1700 C CA  . LEU A 1 236 ? -5.114  -50.959 -33.301 1.00 38.99 ? 236 LEU A CA  1 
ATOM   1701 C C   . LEU A 1 236 ? -4.914  -52.396 -33.777 1.00 39.05 ? 236 LEU A C   1 
ATOM   1702 O O   . LEU A 1 236 ? -5.876  -53.070 -34.163 1.00 39.07 ? 236 LEU A O   1 
ATOM   1703 C CB  . LEU A 1 236 ? -4.738  -49.965 -34.402 1.00 38.95 ? 236 LEU A CB  1 
ATOM   1704 C CG  . LEU A 1 236 ? -5.349  -48.562 -34.288 1.00 38.84 ? 236 LEU A CG  1 
ATOM   1705 C CD1 . LEU A 1 236 ? -4.623  -47.581 -35.199 1.00 38.76 ? 236 LEU A CD1 1 
ATOM   1706 C CD2 . LEU A 1 236 ? -6.841  -48.574 -34.591 1.00 38.42 ? 236 LEU A CD2 1 
ATOM   1707 N N   . LEU A 1 237 ? -3.671  -52.865 -33.737 1.00 39.25 ? 237 LEU A N   1 
ATOM   1708 C CA  . LEU A 1 237 ? -3.363  -54.246 -34.096 1.00 39.37 ? 237 LEU A CA  1 
ATOM   1709 C C   . LEU A 1 237 ? -4.044  -55.267 -33.189 1.00 39.49 ? 237 LEU A C   1 
ATOM   1710 O O   . LEU A 1 237 ? -4.513  -56.303 -33.672 1.00 39.52 ? 237 LEU A O   1 
ATOM   1711 C CB  . LEU A 1 237 ? -1.857  -54.477 -34.099 1.00 39.34 ? 237 LEU A CB  1 
ATOM   1712 C CG  . LEU A 1 237 ? -1.092  -54.181 -35.395 1.00 39.28 ? 237 LEU A CG  1 
ATOM   1713 C CD1 . LEU A 1 237 ? 0.287   -54.743 -35.211 1.00 39.42 ? 237 LEU A CD1 1 
ATOM   1714 C CD2 . LEU A 1 237 ? -1.749  -54.827 -36.609 1.00 39.37 ? 237 LEU A CD2 1 
ATOM   1715 N N   . SER A 1 238 ? -4.087  -54.971 -31.885 1.00 39.55 ? 238 SER A N   1 
ATOM   1716 C CA  . SER A 1 238 ? -4.795  -55.815 -30.911 1.00 39.65 ? 238 SER A CA  1 
ATOM   1717 C C   . SER A 1 238 ? -6.307  -55.858 -31.166 1.00 39.55 ? 238 SER A C   1 
ATOM   1718 O O   . SER A 1 238 ? -6.959  -56.869 -30.888 1.00 39.45 ? 238 SER A O   1 
ATOM   1719 C CB  . SER A 1 238 ? -4.524  -55.336 -29.478 1.00 39.78 ? 238 SER A CB  1 
ATOM   1720 O OG  . SER A 1 238 ? -3.150  -55.520 -29.112 1.00 40.02 ? 238 SER A OG  1 
ATOM   1721 N N   . ALA A 1 239 ? -6.851  -54.760 -31.694 1.00 39.45 ? 239 ALA A N   1 
ATOM   1722 C CA  . ALA A 1 239 ? -8.282  -54.650 -31.983 1.00 39.46 ? 239 ALA A CA  1 
ATOM   1723 C C   . ALA A 1 239 ? -8.669  -55.317 -33.306 1.00 39.48 ? 239 ALA A C   1 
ATOM   1724 O O   . ALA A 1 239 ? -9.844  -55.325 -33.692 1.00 39.31 ? 239 ALA A O   1 
ATOM   1725 C CB  . ALA A 1 239 ? -8.724  -53.185 -31.961 1.00 39.61 ? 239 ALA A CB  1 
ATOM   1726 N N   . GLY A 1 240 ? -7.677  -55.870 -33.999 1.00 39.59 ? 240 GLY A N   1 
ATOM   1727 C CA  . GLY A 1 240 ? -7.924  -56.674 -35.193 1.00 39.77 ? 240 GLY A CA  1 
ATOM   1728 C C   . GLY A 1 240 ? -7.986  -55.904 -36.501 1.00 39.94 ? 240 GLY A C   1 
ATOM   1729 O O   . GLY A 1 240 ? -8.684  -56.310 -37.441 1.00 39.79 ? 240 GLY A O   1 
ATOM   1730 N N   . ALA A 1 241 ? -7.266  -54.786 -36.565 1.00 40.13 ? 241 ALA A N   1 
ATOM   1731 C CA  . ALA A 1 241 ? -7.037  -54.113 -37.836 1.00 40.38 ? 241 ALA A CA  1 
ATOM   1732 C C   . ALA A 1 241 ? -6.117  -55.000 -38.658 1.00 40.55 ? 241 ALA A C   1 
ATOM   1733 O O   . ALA A 1 241 ? -5.164  -55.578 -38.116 1.00 40.50 ? 241 ALA A O   1 
ATOM   1734 C CB  . ALA A 1 241 ? -6.403  -52.760 -37.616 1.00 40.41 ? 241 ALA A CB  1 
ATOM   1735 N N   . THR A 1 242 ? -6.411  -55.127 -39.952 1.00 40.78 ? 242 THR A N   1 
ATOM   1736 C CA  . THR A 1 242 ? -5.575  -55.930 -40.848 1.00 41.04 ? 242 THR A CA  1 
ATOM   1737 C C   . THR A 1 242 ? -4.162  -55.356 -40.894 1.00 41.11 ? 242 THR A C   1 
ATOM   1738 O O   . THR A 1 242 ? -3.181  -56.063 -40.646 1.00 41.23 ? 242 THR A O   1 
ATOM   1739 C CB  . THR A 1 242 ? -6.153  -56.005 -42.277 1.00 41.12 ? 242 THR A CB  1 
ATOM   1740 O OG1 . THR A 1 242 ? -6.541  -54.695 -42.714 1.00 41.32 ? 242 THR A OG1 1 
ATOM   1741 C CG2 . THR A 1 242 ? -7.353  -56.946 -42.333 1.00 41.22 ? 242 THR A CG2 1 
ATOM   1742 N N   . ARG A 1 243 ? -4.078  -54.060 -41.182 1.00 41.15 ? 243 ARG A N   1 
ATOM   1743 C CA  . ARG A 1 243 ? -2.808  -53.350 -41.268 1.00 41.19 ? 243 ARG A CA  1 
ATOM   1744 C C   . ARG A 1 243 ? -2.984  -51.883 -40.876 1.00 40.92 ? 243 ARG A C   1 
ATOM   1745 O O   . ARG A 1 243 ? -4.087  -51.336 -40.979 1.00 41.03 ? 243 ARG A O   1 
ATOM   1746 C CB  . ARG A 1 243 ? -2.211  -53.479 -42.675 1.00 41.43 ? 243 ARG A CB  1 
ATOM   1747 C CG  . ARG A 1 243 ? -3.205  -53.265 -43.818 1.00 42.23 ? 243 ARG A CG  1 
ATOM   1748 C CD  . ARG A 1 243 ? -2.598  -53.680 -45.154 1.00 43.74 ? 243 ARG A CD  1 
ATOM   1749 N NE  . ARG A 1 243 ? -3.636  -53.955 -46.148 1.00 45.16 ? 243 ARG A NE  1 
ATOM   1750 C CZ  . ARG A 1 243 ? -4.023  -55.174 -46.522 1.00 45.96 ? 243 ARG A CZ  1 
ATOM   1751 N NH1 . ARG A 1 243 ? -3.444  -56.263 -45.996 1.00 45.77 ? 243 ARG A NH1 1 
ATOM   1752 N NH2 . ARG A 1 243 ? -4.986  -55.305 -47.436 1.00 46.35 ? 243 ARG A NH2 1 
ATOM   1753 N N   . VAL A 1 244 ? -1.902  -51.256 -40.419 1.00 40.55 ? 244 VAL A N   1 
ATOM   1754 C CA  . VAL A 1 244 ? -1.955  -49.865 -39.951 1.00 40.18 ? 244 VAL A CA  1 
ATOM   1755 C C   . VAL A 1 244 ? -1.102  -48.927 -40.810 1.00 39.93 ? 244 VAL A C   1 
ATOM   1756 O O   . VAL A 1 244 ? 0.074   -49.193 -41.070 1.00 40.04 ? 244 VAL A O   1 
ATOM   1757 C CB  . VAL A 1 244 ? -1.536  -49.731 -38.454 1.00 40.18 ? 244 VAL A CB  1 
ATOM   1758 C CG1 . VAL A 1 244 ? -1.642  -48.284 -37.984 1.00 40.09 ? 244 VAL A CG1 1 
ATOM   1759 C CG2 . VAL A 1 244 ? -2.375  -50.646 -37.564 1.00 39.98 ? 244 VAL A CG2 1 
ATOM   1760 N N   . TYR A 1 245 ? -1.715  -47.832 -41.252 1.00 39.51 ? 245 TYR A N   1 
ATOM   1761 C CA  . TYR A 1 245 ? -0.991  -46.761 -41.926 1.00 39.06 ? 245 TYR A CA  1 
ATOM   1762 C C   . TYR A 1 245 ? -0.929  -45.575 -40.979 1.00 38.48 ? 245 TYR A C   1 
ATOM   1763 O O   . TYR A 1 245 ? -1.760  -45.461 -40.073 1.00 38.48 ? 245 TYR A O   1 
ATOM   1764 C CB  . TYR A 1 245 ? -1.698  -46.352 -43.223 1.00 39.27 ? 245 TYR A CB  1 
ATOM   1765 C CG  . TYR A 1 245 ? -1.668  -47.392 -44.329 1.00 39.95 ? 245 TYR A CG  1 
ATOM   1766 C CD1 . TYR A 1 245 ? -0.848  -47.226 -45.449 1.00 40.48 ? 245 TYR A CD1 1 
ATOM   1767 C CD2 . TYR A 1 245 ? -2.472  -48.532 -44.265 1.00 40.53 ? 245 TYR A CD2 1 
ATOM   1768 C CE1 . TYR A 1 245 ? -0.828  -48.174 -46.473 1.00 40.92 ? 245 TYR A CE1 1 
ATOM   1769 C CE2 . TYR A 1 245 ? -2.459  -49.481 -45.277 1.00 40.97 ? 245 TYR A CE2 1 
ATOM   1770 C CZ  . TYR A 1 245 ? -1.637  -49.300 -46.377 1.00 41.35 ? 245 TYR A CZ  1 
ATOM   1771 O OH  . TYR A 1 245 ? -1.630  -50.253 -47.375 1.00 41.93 ? 245 TYR A OH  1 
ATOM   1772 N N   . ALA A 1 246 ? 0.058   -44.703 -41.182 1.00 37.78 ? 246 ALA A N   1 
ATOM   1773 C CA  . ALA A 1 246 ? 0.178   -43.472 -40.405 1.00 37.05 ? 246 ALA A CA  1 
ATOM   1774 C C   . ALA A 1 246 ? 0.414   -42.289 -41.341 1.00 36.61 ? 246 ALA A C   1 
ATOM   1775 O O   . ALA A 1 246 ? 1.399   -42.268 -42.086 1.00 36.35 ? 246 ALA A O   1 
ATOM   1776 C CB  . ALA A 1 246 ? 1.310   -43.593 -39.389 1.00 37.04 ? 246 ALA A CB  1 
ATOM   1777 N N   . ILE A 1 247 ? -0.503  -41.321 -41.314 1.00 36.08 ? 247 ILE A N   1 
ATOM   1778 C CA  . ILE A 1 247 ? -0.392  -40.124 -42.152 1.00 35.71 ? 247 ILE A CA  1 
ATOM   1779 C C   . ILE A 1 247 ? -0.306  -38.841 -41.321 1.00 35.56 ? 247 ILE A C   1 
ATOM   1780 O O   . ILE A 1 247 ? -1.235  -38.494 -40.589 1.00 35.60 ? 247 ILE A O   1 
ATOM   1781 C CB  . ILE A 1 247 ? -1.548  -40.009 -43.177 1.00 35.59 ? 247 ILE A CB  1 
ATOM   1782 C CG1 . ILE A 1 247 ? -1.632  -41.280 -44.036 1.00 35.52 ? 247 ILE A CG1 1 
ATOM   1783 C CG2 . ILE A 1 247 ? -1.345  -38.771 -44.065 1.00 35.61 ? 247 ILE A CG2 1 
ATOM   1784 C CD1 . ILE A 1 247 ? -2.704  -41.214 -45.123 1.00 35.49 ? 247 ILE A CD1 1 
ATOM   1785 N N   . LEU A 1 248 ? 0.822   -38.149 -41.450 1.00 35.37 ? 248 LEU A N   1 
ATOM   1786 C CA  . LEU A 1 248 ? 1.058   -36.883 -40.761 1.00 35.29 ? 248 LEU A CA  1 
ATOM   1787 C C   . LEU A 1 248 ? 1.438   -35.835 -41.789 1.00 35.16 ? 248 LEU A C   1 
ATOM   1788 O O   . LEU A 1 248 ? 2.182   -36.133 -42.723 1.00 35.19 ? 248 LEU A O   1 
ATOM   1789 C CB  . LEU A 1 248 ? 2.209   -37.025 -39.761 1.00 35.32 ? 248 LEU A CB  1 
ATOM   1790 C CG  . LEU A 1 248 ? 2.335   -38.357 -39.021 1.00 35.40 ? 248 LEU A CG  1 
ATOM   1791 C CD1 . LEU A 1 248 ? 3.797   -38.750 -38.867 1.00 35.61 ? 248 LEU A CD1 1 
ATOM   1792 C CD2 . LEU A 1 248 ? 1.607   -38.329 -37.683 1.00 35.35 ? 248 LEU A CD2 1 
ATOM   1793 N N   . THR A 1 249 ? 0.934   -34.614 -41.626 1.00 35.03 ? 249 THR A N   1 
ATOM   1794 C CA  . THR A 1 249 ? 1.352   -33.511 -42.499 1.00 34.98 ? 249 THR A CA  1 
ATOM   1795 C C   . THR A 1 249 ? 2.717   -32.938 -42.091 1.00 34.97 ? 249 THR A C   1 
ATOM   1796 O O   . THR A 1 249 ? 3.477   -32.481 -42.946 1.00 34.83 ? 249 THR A O   1 
ATOM   1797 C CB  . THR A 1 249 ? 0.260   -32.399 -42.677 1.00 34.98 ? 249 THR A CB  1 
ATOM   1798 O OG1 . THR A 1 249 ? 0.865   -31.097 -42.631 1.00 34.95 ? 249 THR A OG1 1 
ATOM   1799 C CG2 . THR A 1 249 ? -0.828  -32.495 -41.614 1.00 34.99 ? 249 THR A CG2 1 
ATOM   1800 N N   . HIS A 1 250 ? 3.017   -32.969 -40.791 1.00 35.06 ? 250 HIS A N   1 
ATOM   1801 C CA  . HIS A 1 250 ? 4.316   -32.507 -40.282 1.00 35.08 ? 250 HIS A CA  1 
ATOM   1802 C C   . HIS A 1 250 ? 5.055   -33.661 -39.625 1.00 35.60 ? 250 HIS A C   1 
ATOM   1803 O O   . HIS A 1 250 ? 4.615   -34.180 -38.596 1.00 35.63 ? 250 HIS A O   1 
ATOM   1804 C CB  . HIS A 1 250 ? 4.147   -31.369 -39.263 1.00 34.72 ? 250 HIS A CB  1 
ATOM   1805 C CG  . HIS A 1 250 ? 3.281   -30.248 -39.759 1.00 33.72 ? 250 HIS A CG  1 
ATOM   1806 N ND1 . HIS A 1 250 ? 3.633   -29.444 -40.827 1.00 32.98 ? 250 HIS A ND1 1 
ATOM   1807 C CD2 . HIS A 1 250 ? 2.083   -29.784 -39.320 1.00 32.46 ? 250 HIS A CD2 1 
ATOM   1808 C CE1 . HIS A 1 250 ? 2.684   -28.541 -41.032 1.00 32.72 ? 250 HIS A CE1 1 
ATOM   1809 N NE2 . HIS A 1 250 ? 1.732   -28.725 -40.131 1.00 32.37 ? 250 HIS A NE2 1 
ATOM   1810 N N   . GLY A 1 251 ? 6.176   -34.058 -40.225 1.00 36.09 ? 251 GLY A N   1 
ATOM   1811 C CA  . GLY A 1 251 ? 6.978   -35.166 -39.713 1.00 36.70 ? 251 GLY A CA  1 
ATOM   1812 C C   . GLY A 1 251 ? 8.269   -34.686 -39.091 1.00 37.22 ? 251 GLY A C   1 
ATOM   1813 O O   . GLY A 1 251 ? 9.293   -34.597 -39.771 1.00 37.18 ? 251 GLY A O   1 
ATOM   1814 N N   . ILE A 1 252 ? 8.216   -34.369 -37.796 1.00 37.93 ? 252 ILE A N   1 
ATOM   1815 C CA  . ILE A 1 252 ? 9.395   -33.882 -37.075 1.00 38.66 ? 252 ILE A CA  1 
ATOM   1816 C C   . ILE A 1 252 ? 10.405  -35.018 -36.869 1.00 39.38 ? 252 ILE A C   1 
ATOM   1817 O O   . ILE A 1 252 ? 11.602  -34.844 -37.136 1.00 39.40 ? 252 ILE A O   1 
ATOM   1818 C CB  . ILE A 1 252 ? 9.020   -33.193 -35.724 1.00 38.55 ? 252 ILE A CB  1 
ATOM   1819 C CG1 . ILE A 1 252 ? 7.993   -32.073 -35.962 1.00 38.24 ? 252 ILE A CG1 1 
ATOM   1820 C CG2 . ILE A 1 252 ? 10.271  -32.638 -35.024 1.00 38.45 ? 252 ILE A CG2 1 
ATOM   1821 C CD1 . ILE A 1 252 ? 7.363   -31.512 -34.692 1.00 37.56 ? 252 ILE A CD1 1 
ATOM   1822 N N   . PHE A 1 253 ? 9.905   -36.170 -36.414 1.00 40.16 ? 253 PHE A N   1 
ATOM   1823 C CA  . PHE A 1 253 ? 10.699  -37.391 -36.212 1.00 41.04 ? 253 PHE A CA  1 
ATOM   1824 C C   . PHE A 1 253 ? 12.004  -37.192 -35.422 1.00 41.86 ? 253 PHE A C   1 
ATOM   1825 O O   . PHE A 1 253 ? 13.098  -37.244 -35.990 1.00 41.97 ? 253 PHE A O   1 
ATOM   1826 C CB  . PHE A 1 253 ? 10.987  -38.104 -37.547 1.00 40.94 ? 253 PHE A CB  1 
ATOM   1827 C CG  . PHE A 1 253 ? 9.756   -38.445 -38.351 1.00 40.81 ? 253 PHE A CG  1 
ATOM   1828 C CD1 . PHE A 1 253 ? 9.739   -38.248 -39.730 1.00 40.76 ? 253 PHE A CD1 1 
ATOM   1829 C CD2 . PHE A 1 253 ? 8.620   -38.970 -37.740 1.00 40.39 ? 253 PHE A CD2 1 
ATOM   1830 C CE1 . PHE A 1 253 ? 8.608   -38.566 -40.486 1.00 40.46 ? 253 PHE A CE1 1 
ATOM   1831 C CE2 . PHE A 1 253 ? 7.485   -39.286 -38.486 1.00 40.11 ? 253 PHE A CE2 1 
ATOM   1832 C CZ  . PHE A 1 253 ? 7.482   -39.087 -39.860 1.00 39.98 ? 253 PHE A CZ  1 
ATOM   1833 N N   . SER A 1 254 ? 11.886  -36.966 -34.115 1.00 42.86 ? 254 SER A N   1 
ATOM   1834 C CA  . SER A 1 254 ? 13.063  -36.831 -33.254 1.00 43.84 ? 254 SER A CA  1 
ATOM   1835 C C   . SER A 1 254 ? 13.593  -38.183 -32.796 1.00 44.49 ? 254 SER A C   1 
ATOM   1836 O O   . SER A 1 254 ? 12.859  -39.171 -32.771 1.00 44.66 ? 254 SER A O   1 
ATOM   1837 C CB  . SER A 1 254 ? 12.758  -35.967 -32.029 1.00 43.83 ? 254 SER A CB  1 
ATOM   1838 O OG  . SER A 1 254 ? 12.658  -34.597 -32.379 1.00 44.31 ? 254 SER A OG  1 
ATOM   1839 N N   . GLY A 1 255 ? 14.876  -38.201 -32.438 1.00 45.25 ? 255 GLY A N   1 
ATOM   1840 C CA  . GLY A 1 255 ? 15.562  -39.356 -31.856 1.00 46.03 ? 255 GLY A CA  1 
ATOM   1841 C C   . GLY A 1 255 ? 15.067  -40.746 -32.225 1.00 46.59 ? 255 GLY A C   1 
ATOM   1842 O O   . GLY A 1 255 ? 15.419  -41.273 -33.285 1.00 46.56 ? 255 GLY A O   1 
ATOM   1843 N N   . PRO A 1 256 ? 14.238  -41.348 -31.350 1.00 47.14 ? 256 PRO A N   1 
ATOM   1844 C CA  . PRO A 1 256 ? 13.864  -42.757 -31.481 1.00 47.64 ? 256 PRO A CA  1 
ATOM   1845 C C   . PRO A 1 256 ? 12.868  -43.025 -32.610 1.00 48.14 ? 256 PRO A C   1 
ATOM   1846 O O   . PRO A 1 256 ? 12.680  -44.188 -33.003 1.00 48.22 ? 256 PRO A O   1 
ATOM   1847 C CB  . PRO A 1 256 ? 13.222  -43.084 -30.123 1.00 47.62 ? 256 PRO A CB  1 
ATOM   1848 C CG  . PRO A 1 256 ? 13.385  -41.860 -29.261 1.00 47.41 ? 256 PRO A CG  1 
ATOM   1849 C CD  . PRO A 1 256 ? 13.586  -40.718 -30.187 1.00 47.14 ? 256 PRO A CD  1 
ATOM   1850 N N   . ALA A 1 257 ? 12.258  -41.954 -33.123 1.00 48.65 ? 257 ALA A N   1 
ATOM   1851 C CA  . ALA A 1 257 ? 11.208  -42.038 -34.148 1.00 49.14 ? 257 ALA A CA  1 
ATOM   1852 C C   . ALA A 1 257 ? 11.493  -42.981 -35.320 1.00 49.46 ? 257 ALA A C   1 
ATOM   1853 O O   . ALA A 1 257 ? 10.616  -43.751 -35.710 1.00 49.53 ? 257 ALA A O   1 
ATOM   1854 C CB  . ALA A 1 257 ? 10.854  -40.653 -34.661 1.00 49.12 ? 257 ALA A CB  1 
ATOM   1855 N N   . ILE A 1 258 ? 12.708  -42.920 -35.868 1.00 49.83 ? 258 ILE A N   1 
ATOM   1856 C CA  . ILE A 1 258 ? 13.073  -43.724 -37.044 1.00 50.23 ? 258 ILE A CA  1 
ATOM   1857 C C   . ILE A 1 258 ? 13.068  -45.228 -36.762 1.00 50.44 ? 258 ILE A C   1 
ATOM   1858 O O   . ILE A 1 258 ? 12.400  -45.987 -37.470 1.00 50.47 ? 258 ILE A O   1 
ATOM   1859 C CB  . ILE A 1 258 ? 14.425  -43.265 -37.678 1.00 50.26 ? 258 ILE A CB  1 
ATOM   1860 C CG1 . ILE A 1 258 ? 14.286  -41.864 -38.302 1.00 50.50 ? 258 ILE A CG1 1 
ATOM   1861 C CG2 . ILE A 1 258 ? 14.920  -44.269 -38.725 1.00 50.30 ? 258 ILE A CG2 1 
ATOM   1862 C CD1 . ILE A 1 258 ? 13.064  -41.677 -39.213 1.00 50.52 ? 258 ILE A CD1 1 
ATOM   1863 N N   . SER A 1 259 ? 13.804  -45.652 -35.735 1.00 50.79 ? 259 SER A N   1 
ATOM   1864 C CA  . SER A 1 259 ? 13.801  -47.058 -35.318 1.00 51.09 ? 259 SER A CA  1 
ATOM   1865 C C   . SER A 1 259 ? 12.391  -47.525 -34.965 1.00 51.27 ? 259 SER A C   1 
ATOM   1866 O O   . SER A 1 259 ? 11.940  -48.572 -35.455 1.00 51.32 ? 259 SER A O   1 
ATOM   1867 C CB  . SER A 1 259 ? 14.761  -47.297 -34.142 1.00 51.09 ? 259 SER A CB  1 
ATOM   1868 O OG  . SER A 1 259 ? 16.089  -47.518 -34.596 1.00 51.12 ? 259 SER A OG  1 
ATOM   1869 N N   . ARG A 1 260 ? 11.697  -46.730 -34.138 1.00 51.46 ? 260 ARG A N   1 
ATOM   1870 C CA  . ARG A 1 260 ? 10.329  -47.047 -33.720 1.00 51.70 ? 260 ARG A CA  1 
ATOM   1871 C C   . ARG A 1 260 ? 9.361   -47.175 -34.900 1.00 51.78 ? 260 ARG A C   1 
ATOM   1872 O O   . ARG A 1 260 ? 8.431   -47.987 -34.855 1.00 51.81 ? 260 ARG A O   1 
ATOM   1873 C CB  . ARG A 1 260 ? 9.826   -46.022 -32.697 1.00 51.74 ? 260 ARG A CB  1 
ATOM   1874 C CG  . ARG A 1 260 ? 10.442  -46.206 -31.312 1.00 52.18 ? 260 ARG A CG  1 
ATOM   1875 C CD  . ARG A 1 260 ? 10.538  -44.900 -30.547 1.00 52.61 ? 260 ARG A CD  1 
ATOM   1876 N NE  . ARG A 1 260 ? 9.366   -44.633 -29.711 1.00 53.11 ? 260 ARG A NE  1 
ATOM   1877 C CZ  . ARG A 1 260 ? 9.250   -43.593 -28.875 1.00 53.35 ? 260 ARG A CZ  1 
ATOM   1878 N NH1 . ARG A 1 260 ? 10.228  -42.704 -28.757 1.00 53.46 ? 260 ARG A NH1 1 
ATOM   1879 N NH2 . ARG A 1 260 ? 8.152   -43.441 -28.148 1.00 53.25 ? 260 ARG A NH2 1 
ATOM   1880 N N   . ILE A 1 261 ? 9.588   -46.383 -35.951 1.00 51.86 ? 261 ILE A N   1 
ATOM   1881 C CA  . ILE A 1 261 ? 8.811   -46.499 -37.189 1.00 51.95 ? 261 ILE A CA  1 
ATOM   1882 C C   . ILE A 1 261 ? 9.184   -47.772 -37.955 1.00 52.02 ? 261 ILE A C   1 
ATOM   1883 O O   . ILE A 1 261 ? 8.317   -48.428 -38.553 1.00 52.04 ? 261 ILE A O   1 
ATOM   1884 C CB  . ILE A 1 261 ? 8.952   -45.246 -38.105 1.00 51.94 ? 261 ILE A CB  1 
ATOM   1885 C CG1 . ILE A 1 261 ? 8.229   -44.042 -37.484 1.00 51.87 ? 261 ILE A CG1 1 
ATOM   1886 C CG2 . ILE A 1 261 ? 8.363   -45.511 -39.496 1.00 51.99 ? 261 ILE A CG2 1 
ATOM   1887 C CD1 . ILE A 1 261 ? 8.587   -42.698 -38.195 1.00 51.38 ? 261 ILE A CD1 1 
ATOM   1888 N N   . ASN A 1 262 ? 10.473  -48.124 -37.923 1.00 52.12 ? 262 ASN A N   1 
ATOM   1889 C CA  . ASN A 1 262 ? 10.937  -49.363 -38.571 1.00 52.16 ? 262 ASN A CA  1 
ATOM   1890 C C   . ASN A 1 262 ? 10.508  -50.635 -37.832 1.00 52.04 ? 262 ASN A C   1 
ATOM   1891 O O   . ASN A 1 262 ? 10.111  -51.615 -38.462 1.00 52.17 ? 262 ASN A O   1 
ATOM   1892 C CB  . ASN A 1 262 ? 12.464  -49.329 -38.793 1.00 52.25 ? 262 ASN A CB  1 
ATOM   1893 C CG  . ASN A 1 262 ? 12.862  -48.468 -39.997 1.00 52.52 ? 262 ASN A CG  1 
ATOM   1894 O OD1 . ASN A 1 262 ? 12.102  -48.343 -40.959 1.00 52.80 ? 262 ASN A OD1 1 
ATOM   1895 N ND2 . ASN A 1 262 ? 14.057  -47.881 -39.949 1.00 52.58 ? 262 ASN A ND2 1 
ATOM   1896 N N   . ASN A 1 263 ? 10.572  -50.601 -36.501 1.00 51.79 ? 263 ASN A N   1 
ATOM   1897 C CA  . ASN A 1 263 ? 10.184  -51.740 -35.668 1.00 51.52 ? 263 ASN A CA  1 
ATOM   1898 C C   . ASN A 1 263 ? 8.677   -51.983 -35.588 1.00 51.24 ? 263 ASN A C   1 
ATOM   1899 O O   . ASN A 1 263 ? 8.223   -53.137 -35.689 1.00 51.26 ? 263 ASN A O   1 
ATOM   1900 C CB  . ASN A 1 263 ? 10.769  -51.606 -34.260 1.00 51.62 ? 263 ASN A CB  1 
ATOM   1901 C CG  . ASN A 1 263 ? 11.932  -52.547 -34.020 1.00 51.64 ? 263 ASN A CG  1 
ATOM   1902 O OD1 . ASN A 1 263 ? 12.707  -52.845 -34.929 1.00 51.91 ? 263 ASN A OD1 1 
ATOM   1903 N ND2 . ASN A 1 263 ? 12.057  -53.024 -32.787 1.00 51.60 ? 263 ASN A ND2 1 
ATOM   1904 N N   . ALA A 1 264 ? 7.908   -50.900 -35.397 1.00 50.81 ? 264 ALA A N   1 
ATOM   1905 C CA  . ALA A 1 264 ? 6.449   -50.999 -35.297 1.00 50.37 ? 264 ALA A CA  1 
ATOM   1906 C C   . ALA A 1 264 ? 5.827   -51.529 -36.595 1.00 49.99 ? 264 ALA A C   1 
ATOM   1907 O O   . ALA A 1 264 ? 6.519   -51.744 -37.595 1.00 49.97 ? 264 ALA A O   1 
ATOM   1908 C CB  . ALA A 1 264 ? 5.837   -49.652 -34.900 1.00 50.47 ? 264 ALA A CB  1 
ATOM   1909 N N   . CYS A 1 265 ? 4.512   -51.720 -36.563 1.00 49.43 ? 265 CYS A N   1 
ATOM   1910 C CA  . CYS A 1 265 ? 3.793   -52.467 -37.601 1.00 48.96 ? 265 CYS A CA  1 
ATOM   1911 C C   . CYS A 1 265 ? 3.340   -51.679 -38.837 1.00 48.30 ? 265 CYS A C   1 
ATOM   1912 O O   . CYS A 1 265 ? 2.750   -52.260 -39.756 1.00 48.34 ? 265 CYS A O   1 
ATOM   1913 C CB  . CYS A 1 265 ? 2.587   -53.164 -36.967 1.00 49.10 ? 265 CYS A CB  1 
ATOM   1914 S SG  . CYS A 1 265 ? 1.962   -52.254 -35.507 1.00 50.07 ? 265 CYS A SG  1 
ATOM   1915 N N   . PHE A 1 266 ? 3.615   -50.375 -38.863 1.00 47.39 ? 266 PHE A N   1 
ATOM   1916 C CA  . PHE A 1 266 ? 3.141   -49.499 -39.942 1.00 46.41 ? 266 PHE A CA  1 
ATOM   1917 C C   . PHE A 1 266 ? 3.369   -50.085 -41.336 1.00 45.92 ? 266 PHE A C   1 
ATOM   1918 O O   . PHE A 1 266 ? 4.492   -50.461 -41.673 1.00 45.86 ? 266 PHE A O   1 
ATOM   1919 C CB  . PHE A 1 266 ? 3.807   -48.117 -39.866 1.00 46.31 ? 266 PHE A CB  1 
ATOM   1920 C CG  . PHE A 1 266 ? 3.514   -47.358 -38.603 1.00 45.49 ? 266 PHE A CG  1 
ATOM   1921 C CD1 . PHE A 1 266 ? 4.552   -46.976 -37.757 1.00 44.79 ? 266 PHE A CD1 1 
ATOM   1922 C CD2 . PHE A 1 266 ? 2.199   -47.017 -38.264 1.00 44.99 ? 266 PHE A CD2 1 
ATOM   1923 C CE1 . PHE A 1 266 ? 4.287   -46.271 -36.587 1.00 44.62 ? 266 PHE A CE1 1 
ATOM   1924 C CE2 . PHE A 1 266 ? 1.925   -46.316 -37.092 1.00 44.52 ? 266 PHE A CE2 1 
ATOM   1925 C CZ  . PHE A 1 266 ? 2.970   -45.942 -36.254 1.00 44.27 ? 266 PHE A CZ  1 
ATOM   1926 N N   . GLU A 1 267 ? 2.304   -50.180 -42.136 1.00 45.20 ? 267 GLU A N   1 
ATOM   1927 C CA  . GLU A 1 267 ? 2.450   -50.487 -43.561 1.00 44.60 ? 267 GLU A CA  1 
ATOM   1928 C C   . GLU A 1 267 ? 3.417   -49.493 -44.184 1.00 44.18 ? 267 GLU A C   1 
ATOM   1929 O O   . GLU A 1 267 ? 4.462   -49.868 -44.720 1.00 44.27 ? 267 GLU A O   1 
ATOM   1930 C CB  . GLU A 1 267 ? 1.105   -50.402 -44.287 1.00 44.71 ? 267 GLU A CB  1 
ATOM   1931 C CG  . GLU A 1 267 ? 0.384   -51.743 -44.433 1.00 44.75 ? 267 GLU A CG  1 
ATOM   1932 C CD  . GLU A 1 267 ? 1.342   -52.852 -44.869 1.00 44.85 ? 267 GLU A CD  1 
ATOM   1933 O OE1 . GLU A 1 267 ? 1.442   -53.864 -44.135 1.00 44.31 ? 267 GLU A OE1 1 
ATOM   1934 O OE2 . GLU A 1 267 ? 2.000   -52.701 -45.929 1.00 44.74 ? 267 GLU A OE2 1 
ATOM   1935 N N   . ALA A 1 268 ? 3.048   -48.219 -44.090 1.00 43.47 ? 268 ALA A N   1 
ATOM   1936 C CA  . ALA A 1 268 ? 3.883   -47.114 -44.518 1.00 42.74 ? 268 ALA A CA  1 
ATOM   1937 C C   . ALA A 1 268 ? 3.661   -45.948 -43.562 1.00 42.21 ? 268 ALA A C   1 
ATOM   1938 O O   . ALA A 1 268 ? 2.746   -45.979 -42.733 1.00 42.04 ? 268 ALA A O   1 
ATOM   1939 C CB  . ALA A 1 268 ? 3.541   -46.713 -45.951 1.00 42.77 ? 268 ALA A CB  1 
ATOM   1940 N N   . VAL A 1 269 ? 4.514   -44.932 -43.663 1.00 41.55 ? 269 VAL A N   1 
ATOM   1941 C CA  . VAL A 1 269 ? 4.322   -43.695 -42.917 1.00 40.82 ? 269 VAL A CA  1 
ATOM   1942 C C   . VAL A 1 269 ? 4.378   -42.533 -43.897 1.00 40.41 ? 269 VAL A C   1 
ATOM   1943 O O   . VAL A 1 269 ? 5.398   -42.301 -44.547 1.00 40.41 ? 269 VAL A O   1 
ATOM   1944 C CB  . VAL A 1 269 ? 5.357   -43.526 -41.787 1.00 40.85 ? 269 VAL A CB  1 
ATOM   1945 C CG1 . VAL A 1 269 ? 5.136   -42.217 -41.038 1.00 40.59 ? 269 VAL A CG1 1 
ATOM   1946 C CG2 . VAL A 1 269 ? 5.300   -44.713 -40.824 1.00 40.88 ? 269 VAL A CG2 1 
ATOM   1947 N N   . VAL A 1 270 ? 3.265   -41.816 -44.009 1.00 39.83 ? 270 VAL A N   1 
ATOM   1948 C CA  . VAL A 1 270 ? 3.162   -40.727 -44.970 1.00 39.21 ? 270 VAL A CA  1 
ATOM   1949 C C   . VAL A 1 270 ? 3.391   -39.374 -44.302 1.00 38.77 ? 270 VAL A C   1 
ATOM   1950 O O   . VAL A 1 270 ? 2.831   -39.085 -43.241 1.00 38.82 ? 270 VAL A O   1 
ATOM   1951 C CB  . VAL A 1 270 ? 1.804   -40.729 -45.696 1.00 39.18 ? 270 VAL A CB  1 
ATOM   1952 C CG1 . VAL A 1 270 ? 1.877   -39.875 -46.949 1.00 39.26 ? 270 VAL A CG1 1 
ATOM   1953 C CG2 . VAL A 1 270 ? 1.398   -42.149 -46.060 1.00 39.09 ? 270 VAL A CG2 1 
ATOM   1954 N N   . VAL A 1 271 ? 4.235   -38.562 -44.930 1.00 38.11 ? 271 VAL A N   1 
ATOM   1955 C CA  . VAL A 1 271 ? 4.448   -37.182 -44.514 1.00 37.48 ? 271 VAL A CA  1 
ATOM   1956 C C   . VAL A 1 271 ? 4.419   -36.232 -45.709 1.00 37.15 ? 271 VAL A C   1 
ATOM   1957 O O   . VAL A 1 271 ? 4.329   -36.665 -46.859 1.00 37.07 ? 271 VAL A O   1 
ATOM   1958 C CB  . VAL A 1 271 ? 5.780   -37.004 -43.744 1.00 37.41 ? 271 VAL A CB  1 
ATOM   1959 C CG1 . VAL A 1 271 ? 5.604   -37.387 -42.291 1.00 37.63 ? 271 VAL A CG1 1 
ATOM   1960 C CG2 . VAL A 1 271 ? 6.891   -37.812 -44.387 1.00 37.10 ? 271 VAL A CG2 1 
ATOM   1961 N N   . THR A 1 272 ? 4.474   -34.936 -45.429 1.00 36.73 ? 272 THR A N   1 
ATOM   1962 C CA  . THR A 1 272 ? 4.709   -33.955 -46.471 1.00 36.46 ? 272 THR A CA  1 
ATOM   1963 C C   . THR A 1 272 ? 6.131   -33.449 -46.304 1.00 36.43 ? 272 THR A C   1 
ATOM   1964 O O   . THR A 1 272 ? 6.729   -33.618 -45.238 1.00 36.26 ? 272 THR A O   1 
ATOM   1965 C CB  . THR A 1 272 ? 3.735   -32.751 -46.391 1.00 36.43 ? 272 THR A CB  1 
ATOM   1966 O OG1 . THR A 1 272 ? 4.186   -31.822 -45.391 1.00 35.89 ? 272 THR A OG1 1 
ATOM   1967 C CG2 . THR A 1 272 ? 2.307   -33.204 -46.086 1.00 36.13 ? 272 THR A CG2 1 
ATOM   1968 N N   . ASN A 1 273 ? 6.673   -32.834 -47.355 1.00 36.46 ? 273 ASN A N   1 
ATOM   1969 C CA  . ASN A 1 273 ? 7.963   -32.160 -47.249 1.00 36.52 ? 273 ASN A CA  1 
ATOM   1970 C C   . ASN A 1 273 ? 7.787   -30.741 -46.700 1.00 36.77 ? 273 ASN A C   1 
ATOM   1971 O O   . ASN A 1 273 ? 8.438   -29.794 -47.156 1.00 36.75 ? 273 ASN A O   1 
ATOM   1972 C CB  . ASN A 1 273 ? 8.706   -32.167 -48.590 1.00 36.27 ? 273 ASN A CB  1 
ATOM   1973 C CG  . ASN A 1 273 ? 7.912   -31.517 -49.700 1.00 35.96 ? 273 ASN A CG  1 
ATOM   1974 O OD1 . ASN A 1 273 ? 6.764   -31.125 -49.507 1.00 35.19 ? 273 ASN A OD1 1 
ATOM   1975 N ND2 . ASN A 1 273 ? 8.521   -31.396 -50.875 1.00 35.94 ? 273 ASN A ND2 1 
ATOM   1976 N N   . THR A 1 274 ? 6.876   -30.609 -45.732 1.00 37.12 ? 274 THR A N   1 
ATOM   1977 C CA  . THR A 1 274 ? 6.754   -29.407 -44.899 1.00 37.46 ? 274 THR A CA  1 
ATOM   1978 C C   . THR A 1 274 ? 8.075   -29.206 -44.158 1.00 37.83 ? 274 THR A C   1 
ATOM   1979 O O   . THR A 1 274 ? 8.562   -28.086 -44.019 1.00 37.61 ? 274 THR A O   1 
ATOM   1980 C CB  . THR A 1 274 ? 5.599   -29.573 -43.873 1.00 37.34 ? 274 THR A CB  1 
ATOM   1981 O OG1 . THR A 1 274 ? 4.343   -29.275 -44.497 1.00 37.21 ? 274 THR A OG1 1 
ATOM   1982 C CG2 . THR A 1 274 ? 5.778   -28.655 -42.694 1.00 37.59 ? 274 THR A CG2 1 
ATOM   1983 N N   . ILE A 1 275 ? 8.635   -30.327 -43.704 1.00 38.57 ? 275 ILE A N   1 
ATOM   1984 C CA  . ILE A 1 275 ? 9.892   -30.408 -42.980 1.00 39.42 ? 275 ILE A CA  1 
ATOM   1985 C C   . ILE A 1 275 ? 10.784  -31.305 -43.845 1.00 40.32 ? 275 ILE A C   1 
ATOM   1986 O O   . ILE A 1 275 ? 10.282  -32.275 -44.414 1.00 40.39 ? 275 ILE A O   1 
ATOM   1987 C CB  . ILE A 1 275 ? 9.655   -31.046 -41.580 1.00 39.30 ? 275 ILE A CB  1 
ATOM   1988 C CG1 . ILE A 1 275 ? 8.749   -30.149 -40.724 1.00 39.06 ? 275 ILE A CG1 1 
ATOM   1989 C CG2 . ILE A 1 275 ? 10.966  -31.355 -40.861 1.00 39.22 ? 275 ILE A CG2 1 
ATOM   1990 C CD1 . ILE A 1 275 ? 8.028   -30.886 -39.592 1.00 38.13 ? 275 ILE A CD1 1 
ATOM   1991 N N   . PRO A 1 276 ? 12.093  -30.975 -43.983 1.00 41.24 ? 276 PRO A N   1 
ATOM   1992 C CA  . PRO A 1 276 ? 13.002  -31.826 -44.766 1.00 42.10 ? 276 PRO A CA  1 
ATOM   1993 C C   . PRO A 1 276 ? 12.954  -33.306 -44.361 1.00 43.08 ? 276 PRO A C   1 
ATOM   1994 O O   . PRO A 1 276 ? 12.932  -33.622 -43.168 1.00 43.13 ? 276 PRO A O   1 
ATOM   1995 C CB  . PRO A 1 276 ? 14.380  -31.226 -44.465 1.00 41.95 ? 276 PRO A CB  1 
ATOM   1996 C CG  . PRO A 1 276 ? 14.097  -29.793 -44.209 1.00 41.55 ? 276 PRO A CG  1 
ATOM   1997 C CD  . PRO A 1 276 ? 12.791  -29.786 -43.451 1.00 41.20 ? 276 PRO A CD  1 
ATOM   1998 N N   . GLN A 1 277 ? 12.924  -34.196 -45.358 1.00 44.23 ? 277 GLN A N   1 
ATOM   1999 C CA  . GLN A 1 277 ? 12.780  -35.633 -45.112 1.00 45.32 ? 277 GLN A CA  1 
ATOM   2000 C C   . GLN A 1 277 ? 13.788  -36.499 -45.887 1.00 46.15 ? 277 GLN A C   1 
ATOM   2001 O O   . GLN A 1 277 ? 13.602  -37.714 -45.994 1.00 46.24 ? 277 GLN A O   1 
ATOM   2002 C CB  . GLN A 1 277 ? 11.355  -36.118 -45.452 1.00 45.27 ? 277 GLN A CB  1 
ATOM   2003 C CG  . GLN A 1 277 ? 10.188  -35.219 -44.995 1.00 45.46 ? 277 GLN A CG  1 
ATOM   2004 C CD  . GLN A 1 277 ? 9.882   -35.320 -43.498 1.00 45.65 ? 277 GLN A CD  1 
ATOM   2005 O OE1 . GLN A 1 277 ? 10.141  -36.344 -42.855 1.00 45.56 ? 277 GLN A OE1 1 
ATOM   2006 N NE2 . GLN A 1 277 ? 9.314   -34.250 -42.940 1.00 45.77 ? 277 GLN A NE2 1 
ATOM   2007 N N   . GLU A 1 278 ? 14.849  -35.906 -46.431 1.00 47.20 ? 278 GLU A N   1 
ATOM   2008 C CA  . GLU A 1 278 ? 15.820  -36.713 -47.183 1.00 48.20 ? 278 GLU A CA  1 
ATOM   2009 C C   . GLU A 1 278 ? 16.665  -37.612 -46.268 1.00 48.77 ? 278 GLU A C   1 
ATOM   2010 O O   . GLU A 1 278 ? 16.853  -38.802 -46.566 1.00 48.80 ? 278 GLU A O   1 
ATOM   2011 C CB  . GLU A 1 278 ? 16.687  -35.867 -48.134 1.00 48.22 ? 278 GLU A CB  1 
ATOM   2012 C CG  . GLU A 1 278 ? 17.767  -35.007 -47.475 1.00 48.87 ? 278 GLU A CG  1 
ATOM   2013 C CD  . GLU A 1 278 ? 18.906  -34.666 -48.437 1.00 49.90 ? 278 GLU A CD  1 
ATOM   2014 O OE1 . GLU A 1 278 ? 19.486  -33.557 -48.312 1.00 50.00 ? 278 GLU A OE1 1 
ATOM   2015 O OE2 . GLU A 1 278 ? 19.228  -35.505 -49.314 1.00 50.39 ? 278 GLU A OE2 1 
ATOM   2016 N N   . ASP A 1 279 ? 17.144  -37.047 -45.154 1.00 49.55 ? 279 ASP A N   1 
ATOM   2017 C CA  . ASP A 1 279 ? 17.940  -37.789 -44.174 1.00 50.33 ? 279 ASP A CA  1 
ATOM   2018 C C   . ASP A 1 279 ? 17.160  -38.957 -43.576 1.00 50.69 ? 279 ASP A C   1 
ATOM   2019 O O   . ASP A 1 279 ? 17.681  -40.070 -43.456 1.00 50.75 ? 279 ASP A O   1 
ATOM   2020 C CB  . ASP A 1 279 ? 18.427  -36.860 -43.051 1.00 50.45 ? 279 ASP A CB  1 
ATOM   2021 C CG  . ASP A 1 279 ? 19.757  -36.179 -43.384 1.00 51.13 ? 279 ASP A CG  1 
ATOM   2022 O OD1 . ASP A 1 279 ? 20.395  -36.534 -44.405 1.00 51.82 ? 279 ASP A OD1 1 
ATOM   2023 O OD2 . ASP A 1 279 ? 20.169  -35.286 -42.609 1.00 51.63 ? 279 ASP A OD2 1 
ATOM   2024 N N   . LYS A 1 280 ? 15.907  -38.691 -43.213 1.00 51.12 ? 280 LYS A N   1 
ATOM   2025 C CA  . LYS A 1 280 ? 15.041  -39.690 -42.594 1.00 51.49 ? 280 LYS A CA  1 
ATOM   2026 C C   . LYS A 1 280 ? 14.718  -40.840 -43.543 1.00 51.81 ? 280 LYS A C   1 
ATOM   2027 O O   . LYS A 1 280 ? 14.547  -41.991 -43.095 1.00 51.91 ? 280 LYS A O   1 
ATOM   2028 C CB  . LYS A 1 280 ? 13.757  -39.033 -42.075 1.00 51.44 ? 280 LYS A CB  1 
ATOM   2029 C CG  . LYS A 1 280 ? 13.810  -38.576 -40.610 1.00 51.50 ? 280 LYS A CG  1 
ATOM   2030 C CD  . LYS A 1 280 ? 14.983  -37.647 -40.302 1.00 51.28 ? 280 LYS A CD  1 
ATOM   2031 C CE  . LYS A 1 280 ? 15.161  -37.441 -38.799 1.00 51.29 ? 280 LYS A CE  1 
ATOM   2032 N NZ  . LYS A 1 280 ? 14.150  -36.465 -38.265 1.00 51.20 ? 280 LYS A NZ  1 
ATOM   2033 N N   . MET A 1 281 ? 14.643  -40.524 -44.848 1.00 52.16 ? 281 MET A N   1 
ATOM   2034 C CA  . MET A 1 281 ? 14.384  -41.532 -45.883 1.00 52.49 ? 281 MET A CA  1 
ATOM   2035 C C   . MET A 1 281 ? 15.463  -42.604 -45.940 1.00 52.52 ? 281 MET A C   1 
ATOM   2036 O O   . MET A 1 281 ? 15.159  -43.794 -46.099 1.00 52.50 ? 281 MET A O   1 
ATOM   2037 C CB  . MET A 1 281 ? 14.197  -40.874 -47.253 1.00 52.63 ? 281 MET A CB  1 
ATOM   2038 C CG  . MET A 1 281 ? 12.734  -40.594 -47.617 1.00 53.32 ? 281 MET A CG  1 
ATOM   2039 S SD  . MET A 1 281 ? 11.816  -39.667 -46.337 1.00 54.89 ? 281 MET A SD  1 
ATOM   2040 C CE  . MET A 1 281 ? 11.717  -40.885 -45.002 1.00 54.41 ? 281 MET A CE  1 
ATOM   2041 N N   . LYS A 1 282 ? 16.717  -42.170 -45.798 1.00 52.59 ? 282 LYS A N   1 
ATOM   2042 C CA  . LYS A 1 282 ? 17.854  -43.080 -45.764 1.00 52.59 ? 282 LYS A CA  1 
ATOM   2043 C C   . LYS A 1 282 ? 17.624  -44.197 -44.745 1.00 52.55 ? 282 LYS A C   1 
ATOM   2044 O O   . LYS A 1 282 ? 17.529  -45.381 -45.127 1.00 52.60 ? 282 LYS A O   1 
ATOM   2045 C CB  . LYS A 1 282 ? 19.145  -42.314 -45.448 1.00 52.63 ? 282 LYS A CB  1 
ATOM   2046 N N   . HIS A 1 283 ? 17.496  -43.812 -43.465 1.00 52.42 ? 283 HIS A N   1 
ATOM   2047 C CA  . HIS A 1 283 ? 17.401  -44.773 -42.360 1.00 52.20 ? 283 HIS A CA  1 
ATOM   2048 C C   . HIS A 1 283 ? 16.027  -45.442 -42.219 1.00 51.88 ? 283 HIS A C   1 
ATOM   2049 O O   . HIS A 1 283 ? 15.869  -46.364 -41.414 1.00 51.95 ? 283 HIS A O   1 
ATOM   2050 C CB  . HIS A 1 283 ? 17.795  -44.115 -41.025 1.00 52.35 ? 283 HIS A CB  1 
ATOM   2051 C CG  . HIS A 1 283 ? 19.128  -43.426 -41.050 1.00 53.03 ? 283 HIS A CG  1 
ATOM   2052 N ND1 . HIS A 1 283 ? 20.300  -44.070 -41.412 1.00 53.60 ? 283 HIS A ND1 1 
ATOM   2053 C CD2 . HIS A 1 283 ? 19.473  -42.150 -40.729 1.00 53.41 ? 283 HIS A CD2 1 
ATOM   2054 C CE1 . HIS A 1 283 ? 21.307  -43.217 -41.330 1.00 53.81 ? 283 HIS A CE1 1 
ATOM   2055 N NE2 . HIS A 1 283 ? 20.833  -42.045 -40.915 1.00 53.73 ? 283 HIS A NE2 1 
ATOM   2056 N N   . CYS A 1 284 ? 15.043  -44.987 -42.998 1.00 51.42 ? 284 CYS A N   1 
ATOM   2057 C CA  . CYS A 1 284 ? 13.669  -45.494 -42.884 1.00 50.94 ? 284 CYS A CA  1 
ATOM   2058 C C   . CYS A 1 284 ? 12.971  -45.695 -44.241 1.00 50.38 ? 284 CYS A C   1 
ATOM   2059 O O   . CYS A 1 284 ? 12.660  -44.731 -44.950 1.00 50.37 ? 284 CYS A O   1 
ATOM   2060 C CB  . CYS A 1 284 ? 12.837  -44.572 -41.979 1.00 51.05 ? 284 CYS A CB  1 
ATOM   2061 S SG  . CYS A 1 284 ? 11.157  -45.180 -41.657 1.00 51.44 ? 284 CYS A SG  1 
ATOM   2062 N N   . SER A 1 285 ? 12.712  -46.960 -44.573 1.00 49.63 ? 285 SER A N   1 
ATOM   2063 C CA  . SER A 1 285 ? 12.137  -47.346 -45.865 1.00 48.81 ? 285 SER A CA  1 
ATOM   2064 C C   . SER A 1 285 ? 10.618  -47.159 -45.946 1.00 48.11 ? 285 SER A C   1 
ATOM   2065 O O   . SER A 1 285 ? 10.089  -46.819 -47.007 1.00 48.06 ? 285 SER A O   1 
ATOM   2066 C CB  . SER A 1 285 ? 12.509  -48.796 -46.190 1.00 48.91 ? 285 SER A CB  1 
ATOM   2067 O OG  . SER A 1 285 ? 12.128  -49.143 -47.508 1.00 49.17 ? 285 SER A OG  1 
ATOM   2068 N N   . LYS A 1 286 ? 9.931   -47.384 -44.822 1.00 47.18 ? 286 LYS A N   1 
ATOM   2069 C CA  . LYS A 1 286 ? 8.470   -47.248 -44.719 1.00 46.18 ? 286 LYS A CA  1 
ATOM   2070 C C   . LYS A 1 286 ? 7.901   -45.871 -45.059 1.00 45.48 ? 286 LYS A C   1 
ATOM   2071 O O   . LYS A 1 286 ? 6.694   -45.743 -45.279 1.00 45.49 ? 286 LYS A O   1 
ATOM   2072 C CB  . LYS A 1 286 ? 8.002   -47.625 -43.306 1.00 46.20 ? 286 LYS A CB  1 
ATOM   2073 C CG  . LYS A 1 286 ? 7.666   -49.133 -43.157 1.00 46.30 ? 286 LYS A CG  1 
ATOM   2074 C CD  . LYS A 1 286 ? 7.520   -49.488 -41.687 1.00 46.66 ? 286 LYS A CD  1 
ATOM   2075 C CE  . LYS A 1 286 ? 7.595   -51.001 -41.498 1.00 46.88 ? 286 LYS A CE  1 
ATOM   2076 N NZ  . LYS A 1 286 ? 7.179   -51.417 -40.126 1.00 47.05 ? 286 LYS A NZ  1 
ATOM   2077 N N   . ILE A 1 287 ? 8.750   -44.846 -45.096 1.00 44.51 ? 287 ILE A N   1 
ATOM   2078 C CA  . ILE A 1 287 ? 8.244   -43.481 -45.219 1.00 43.57 ? 287 ILE A CA  1 
ATOM   2079 C C   . ILE A 1 287 ? 7.983   -43.035 -46.658 1.00 42.88 ? 287 ILE A C   1 
ATOM   2080 O O   . ILE A 1 287 ? 8.805   -43.244 -47.551 1.00 42.91 ? 287 ILE A O   1 
ATOM   2081 C CB  . ILE A 1 287 ? 9.112   -42.453 -44.448 1.00 43.59 ? 287 ILE A CB  1 
ATOM   2082 C CG1 . ILE A 1 287 ? 9.086   -42.770 -42.948 1.00 43.64 ? 287 ILE A CG1 1 
ATOM   2083 C CG2 . ILE A 1 287 ? 8.612   -41.025 -44.701 1.00 43.36 ? 287 ILE A CG2 1 
ATOM   2084 C CD1 . ILE A 1 287 ? 9.978   -41.869 -42.073 1.00 43.95 ? 287 ILE A CD1 1 
ATOM   2085 N N   . GLN A 1 288 ? 6.812   -42.426 -46.844 1.00 41.96 ? 288 GLN A N   1 
ATOM   2086 C CA  . GLN A 1 288 ? 6.388   -41.851 -48.108 1.00 41.08 ? 288 GLN A CA  1 
ATOM   2087 C C   . GLN A 1 288 ? 6.229   -40.345 -47.897 1.00 40.44 ? 288 GLN A C   1 
ATOM   2088 O O   . GLN A 1 288 ? 5.744   -39.907 -46.847 1.00 40.22 ? 288 GLN A O   1 
ATOM   2089 C CB  . GLN A 1 288 ? 5.040   -42.443 -48.513 1.00 41.15 ? 288 GLN A CB  1 
ATOM   2090 C CG  . GLN A 1 288 ? 5.013   -43.093 -49.881 1.00 41.05 ? 288 GLN A CG  1 
ATOM   2091 C CD  . GLN A 1 288 ? 5.240   -44.588 -49.805 1.00 40.93 ? 288 GLN A CD  1 
ATOM   2092 O OE1 . GLN A 1 288 ? 6.285   -45.049 -49.338 1.00 40.89 ? 288 GLN A OE1 1 
ATOM   2093 N NE2 . GLN A 1 288 ? 4.257   -45.359 -50.262 1.00 40.30 ? 288 GLN A NE2 1 
ATOM   2094 N N   . VAL A 1 289 ? 6.631   -39.553 -48.887 1.00 39.65 ? 289 VAL A N   1 
ATOM   2095 C CA  . VAL A 1 289 ? 6.556   -38.095 -48.773 1.00 38.96 ? 289 VAL A CA  1 
ATOM   2096 C C   . VAL A 1 289 ? 5.677   -37.492 -49.871 1.00 38.49 ? 289 VAL A C   1 
ATOM   2097 O O   . VAL A 1 289 ? 5.885   -37.747 -51.062 1.00 38.34 ? 289 VAL A O   1 
ATOM   2098 C CB  . VAL A 1 289 ? 7.968   -37.426 -48.774 1.00 38.94 ? 289 VAL A CB  1 
ATOM   2099 C CG1 . VAL A 1 289 ? 7.857   -35.911 -48.691 1.00 38.75 ? 289 VAL A CG1 1 
ATOM   2100 C CG2 . VAL A 1 289 ? 8.820   -37.943 -47.623 1.00 38.80 ? 289 VAL A CG2 1 
ATOM   2101 N N   . ILE A 1 290 ? 4.683   -36.710 -49.453 1.00 37.83 ? 290 ILE A N   1 
ATOM   2102 C CA  . ILE A 1 290 ? 3.874   -35.934 -50.381 1.00 37.19 ? 290 ILE A CA  1 
ATOM   2103 C C   . ILE A 1 290 ? 4.520   -34.565 -50.535 1.00 36.67 ? 290 ILE A C   1 
ATOM   2104 O O   . ILE A 1 290 ? 4.649   -33.816 -49.564 1.00 36.55 ? 290 ILE A O   1 
ATOM   2105 C CB  . ILE A 1 290 ? 2.421   -35.732 -49.889 1.00 37.23 ? 290 ILE A CB  1 
ATOM   2106 C CG1 . ILE A 1 290 ? 1.850   -37.026 -49.265 1.00 37.17 ? 290 ILE A CG1 1 
ATOM   2107 C CG2 . ILE A 1 290 ? 1.549   -35.199 -51.037 1.00 37.30 ? 290 ILE A CG2 1 
ATOM   2108 C CD1 . ILE A 1 290 ? 0.484   -36.764 -48.563 1.00 37.36 ? 290 ILE A CD1 1 
ATOM   2109 N N   . ASP A 1 291 ? 4.935   -34.250 -51.757 1.00 36.00 ? 291 ASP A N   1 
ATOM   2110 C CA  . ASP A 1 291 ? 5.495   -32.945 -52.067 1.00 35.35 ? 291 ASP A CA  1 
ATOM   2111 C C   . ASP A 1 291 ? 4.370   -31.909 -52.089 1.00 34.82 ? 291 ASP A C   1 
ATOM   2112 O O   . ASP A 1 291 ? 3.350   -32.100 -52.752 1.00 34.57 ? 291 ASP A O   1 
ATOM   2113 C CB  . ASP A 1 291 ? 6.240   -33.004 -53.404 1.00 35.46 ? 291 ASP A CB  1 
ATOM   2114 C CG  . ASP A 1 291 ? 6.819   -31.659 -53.813 1.00 35.72 ? 291 ASP A CG  1 
ATOM   2115 O OD1 . ASP A 1 291 ? 6.899   -30.734 -52.969 1.00 35.69 ? 291 ASP A OD1 1 
ATOM   2116 O OD2 . ASP A 1 291 ? 7.201   -31.535 -54.999 1.00 36.61 ? 291 ASP A OD2 1 
ATOM   2117 N N   . ILE A 1 292 ? 4.564   -30.823 -51.345 1.00 34.31 ? 292 ILE A N   1 
ATOM   2118 C CA  . ILE A 1 292 ? 3.549   -29.772 -51.202 1.00 33.86 ? 292 ILE A CA  1 
ATOM   2119 C C   . ILE A 1 292 ? 3.997   -28.442 -51.810 1.00 33.44 ? 292 ILE A C   1 
ATOM   2120 O O   . ILE A 1 292 ? 3.311   -27.423 -51.671 1.00 33.43 ? 292 ILE A O   1 
ATOM   2121 C CB  . ILE A 1 292 ? 3.156   -29.542 -49.716 1.00 33.96 ? 292 ILE A CB  1 
ATOM   2122 C CG1 . ILE A 1 292 ? 4.408   -29.307 -48.860 1.00 34.00 ? 292 ILE A CG1 1 
ATOM   2123 C CG2 . ILE A 1 292 ? 2.325   -30.712 -49.195 1.00 33.83 ? 292 ILE A CG2 1 
ATOM   2124 C CD1 . ILE A 1 292 ? 4.179   -28.471 -47.625 1.00 34.38 ? 292 ILE A CD1 1 
ATOM   2125 N N   . SER A 1 293 ? 5.143   -28.465 -52.487 1.00 32.91 ? 293 SER A N   1 
ATOM   2126 C CA  . SER A 1 293 ? 5.732   -27.271 -53.091 1.00 32.36 ? 293 SER A CA  1 
ATOM   2127 C C   . SER A 1 293 ? 4.815   -26.582 -54.105 1.00 32.12 ? 293 SER A C   1 
ATOM   2128 O O   . SER A 1 293 ? 4.830   -25.354 -54.217 1.00 32.31 ? 293 SER A O   1 
ATOM   2129 C CB  . SER A 1 293 ? 7.083   -27.604 -53.732 1.00 32.27 ? 293 SER A CB  1 
ATOM   2130 O OG  . SER A 1 293 ? 6.947   -28.640 -54.684 1.00 31.58 ? 293 SER A OG  1 
ATOM   2131 N N   . MET A 1 294 ? 4.018   -27.369 -54.831 1.00 31.70 ? 294 MET A N   1 
ATOM   2132 C CA  . MET A 1 294 ? 3.051   -26.818 -55.788 1.00 31.25 ? 294 MET A CA  1 
ATOM   2133 C C   . MET A 1 294 ? 1.966   -25.989 -55.097 1.00 30.96 ? 294 MET A C   1 
ATOM   2134 O O   . MET A 1 294 ? 1.577   -24.938 -55.603 1.00 31.08 ? 294 MET A O   1 
ATOM   2135 C CB  . MET A 1 294 ? 2.411   -27.925 -56.635 1.00 31.15 ? 294 MET A CB  1 
ATOM   2136 N N   . ILE A 1 295 ? 1.490   -26.470 -53.948 1.00 30.57 ? 295 ILE A N   1 
ATOM   2137 C CA  . ILE A 1 295 ? 0.471   -25.770 -53.160 1.00 30.21 ? 295 ILE A CA  1 
ATOM   2138 C C   . ILE A 1 295 ? 1.006   -24.445 -52.613 1.00 29.98 ? 295 ILE A C   1 
ATOM   2139 O O   . ILE A 1 295 ? 0.350   -23.405 -52.726 1.00 29.86 ? 295 ILE A O   1 
ATOM   2140 C CB  . ILE A 1 295 ? -0.055  -26.651 -51.997 1.00 30.23 ? 295 ILE A CB  1 
ATOM   2141 C CG1 . ILE A 1 295 ? -0.845  -27.845 -52.547 1.00 30.12 ? 295 ILE A CG1 1 
ATOM   2142 C CG2 . ILE A 1 295 ? -0.923  -25.828 -51.044 1.00 29.93 ? 295 ILE A CG2 1 
ATOM   2143 C CD1 . ILE A 1 295 ? -1.071  -28.968 -51.543 1.00 30.14 ? 295 ILE A CD1 1 
ATOM   2144 N N   . LEU A 1 296 ? 2.199   -24.496 -52.024 1.00 29.80 ? 296 LEU A N   1 
ATOM   2145 C CA  . LEU A 1 296 ? 2.850   -23.309 -51.479 1.00 29.54 ? 296 LEU A CA  1 
ATOM   2146 C C   . LEU A 1 296 ? 3.189   -22.319 -52.587 1.00 29.48 ? 296 LEU A C   1 
ATOM   2147 O O   . LEU A 1 296 ? 2.885   -21.128 -52.471 1.00 29.30 ? 296 LEU A O   1 
ATOM   2148 C CB  . LEU A 1 296 ? 4.115   -23.688 -50.699 1.00 29.51 ? 296 LEU A CB  1 
ATOM   2149 C CG  . LEU A 1 296 ? 3.973   -24.470 -49.389 1.00 28.99 ? 296 LEU A CG  1 
ATOM   2150 C CD1 . LEU A 1 296 ? 5.350   -24.900 -48.899 1.00 28.31 ? 296 LEU A CD1 1 
ATOM   2151 C CD2 . LEU A 1 296 ? 3.263   -23.646 -48.318 1.00 28.85 ? 296 LEU A CD2 1 
ATOM   2152 N N   . ALA A 1 297 ? 3.804   -22.819 -53.662 1.00 29.49 ? 297 ALA A N   1 
ATOM   2153 C CA  . ALA A 1 297 ? 4.140   -21.991 -54.826 1.00 29.61 ? 297 ALA A CA  1 
ATOM   2154 C C   . ALA A 1 297 ? 2.900   -21.283 -55.353 1.00 29.64 ? 297 ALA A C   1 
ATOM   2155 O O   . ALA A 1 297 ? 2.954   -20.115 -55.743 1.00 29.58 ? 297 ALA A O   1 
ATOM   2156 C CB  . ALA A 1 297 ? 4.767   -22.837 -55.927 1.00 29.59 ? 297 ALA A CB  1 
ATOM   2157 N N   . GLU A 1 298 ? 1.784   -22.004 -55.344 1.00 29.83 ? 298 GLU A N   1 
ATOM   2158 C CA  . GLU A 1 298 ? 0.518   -21.483 -55.823 1.00 30.23 ? 298 GLU A CA  1 
ATOM   2159 C C   . GLU A 1 298 ? -0.094  -20.447 -54.890 1.00 30.15 ? 298 GLU A C   1 
ATOM   2160 O O   . GLU A 1 298 ? -0.736  -19.510 -55.354 1.00 30.16 ? 298 GLU A O   1 
ATOM   2161 C CB  . GLU A 1 298 ? -0.469  -22.620 -56.095 1.00 30.41 ? 298 GLU A CB  1 
ATOM   2162 C CG  . GLU A 1 298 ? -0.507  -23.048 -57.552 1.00 31.58 ? 298 GLU A CG  1 
ATOM   2163 C CD  . GLU A 1 298 ? -0.901  -21.903 -58.475 1.00 33.29 ? 298 GLU A CD  1 
ATOM   2164 O OE1 . GLU A 1 298 ? -1.929  -21.240 -58.197 1.00 33.90 ? 298 GLU A OE1 1 
ATOM   2165 O OE2 . GLU A 1 298 ? -0.182  -21.664 -59.471 1.00 33.79 ? 298 GLU A OE2 1 
ATOM   2166 N N   . ALA A 1 299 ? 0.103   -20.612 -53.584 1.00 30.27 ? 299 ALA A N   1 
ATOM   2167 C CA  . ALA A 1 299 ? -0.379  -19.628 -52.613 1.00 30.37 ? 299 ALA A CA  1 
ATOM   2168 C C   . ALA A 1 299 ? 0.366   -18.306 -52.788 1.00 30.60 ? 299 ALA A C   1 
ATOM   2169 O O   . ALA A 1 299 ? -0.229  -17.229 -52.704 1.00 30.37 ? 299 ALA A O   1 
ATOM   2170 C CB  . ALA A 1 299 ? -0.243  -20.152 -51.190 1.00 30.16 ? 299 ALA A CB  1 
ATOM   2171 N N   . ILE A 1 300 ? 1.665   -18.407 -53.057 1.00 31.06 ? 300 ILE A N   1 
ATOM   2172 C CA  . ILE A 1 300 ? 2.517   -17.244 -53.300 1.00 31.67 ? 300 ILE A CA  1 
ATOM   2173 C C   . ILE A 1 300 ? 2.114   -16.507 -54.588 1.00 32.21 ? 300 ILE A C   1 
ATOM   2174 O O   . ILE A 1 300 ? 1.859   -15.295 -54.569 1.00 31.81 ? 300 ILE A O   1 
ATOM   2175 C CB  . ILE A 1 300 ? 4.011   -17.650 -53.327 1.00 31.59 ? 300 ILE A CB  1 
ATOM   2176 C CG1 . ILE A 1 300 ? 4.426   -18.181 -51.949 1.00 31.31 ? 300 ILE A CG1 1 
ATOM   2177 C CG2 . ILE A 1 300 ? 4.888   -16.472 -53.756 1.00 31.72 ? 300 ILE A CG2 1 
ATOM   2178 C CD1 . ILE A 1 300 ? 5.787   -18.830 -51.905 1.00 30.88 ? 300 ILE A CD1 1 
ATOM   2179 N N   . ARG A 1 301 ? 2.041   -17.250 -55.694 1.00 33.09 ? 301 ARG A N   1 
ATOM   2180 C CA  . ARG A 1 301 ? 1.612   -16.697 -56.977 1.00 33.95 ? 301 ARG A CA  1 
ATOM   2181 C C   . ARG A 1 301 ? 0.292   -15.947 -56.832 1.00 34.33 ? 301 ARG A C   1 
ATOM   2182 O O   . ARG A 1 301 ? 0.128   -14.858 -57.385 1.00 34.19 ? 301 ARG A O   1 
ATOM   2183 C CB  . ARG A 1 301 ? 1.471   -17.806 -58.026 1.00 34.10 ? 301 ARG A CB  1 
ATOM   2184 C CG  . ARG A 1 301 ? 1.570   -17.312 -59.472 1.00 35.21 ? 301 ARG A CG  1 
ATOM   2185 C CD  . ARG A 1 301 ? 1.311   -18.433 -60.486 1.00 36.50 ? 301 ARG A CD  1 
ATOM   2186 N NE  . ARG A 1 301 ? -0.117  -18.720 -60.644 1.00 37.92 ? 301 ARG A NE  1 
ATOM   2187 C CZ  . ARG A 1 301 ? -0.945  -18.036 -61.437 1.00 38.50 ? 301 ARG A CZ  1 
ATOM   2188 N NH1 . ARG A 1 301 ? -0.499  -17.008 -62.157 1.00 38.64 ? 301 ARG A NH1 1 
ATOM   2189 N NH2 . ARG A 1 301 ? -2.227  -18.380 -61.508 1.00 38.48 ? 301 ARG A NH2 1 
ATOM   2190 N N   . ARG A 1 302 ? -0.634  -16.521 -56.062 1.00 34.92 ? 302 ARG A N   1 
ATOM   2191 C CA  . ARG A 1 302 ? -1.979  -15.959 -55.930 1.00 35.71 ? 302 ARG A CA  1 
ATOM   2192 C C   . ARG A 1 302 ? -2.112  -14.854 -54.871 1.00 36.07 ? 302 ARG A C   1 
ATOM   2193 O O   . ARG A 1 302 ? -2.993  -13.992 -54.986 1.00 35.96 ? 302 ARG A O   1 
ATOM   2194 C CB  . ARG A 1 302 ? -3.017  -17.068 -55.736 1.00 35.75 ? 302 ARG A CB  1 
ATOM   2195 C CG  . ARG A 1 302 ? -3.027  -18.084 -56.886 1.00 36.55 ? 302 ARG A CG  1 
ATOM   2196 C CD  . ARG A 1 302 ? -4.404  -18.721 -57.081 1.00 37.81 ? 302 ARG A CD  1 
ATOM   2197 N NE  . ARG A 1 302 ? -4.268  -20.088 -57.609 1.00 39.19 ? 302 ARG A NE  1 
ATOM   2198 C CZ  . ARG A 1 302 ? -5.257  -20.798 -58.156 1.00 40.16 ? 302 ARG A CZ  1 
ATOM   2199 N NH1 . ARG A 1 302 ? -6.474  -20.273 -58.271 1.00 40.27 ? 302 ARG A NH1 1 
ATOM   2200 N NH2 . ARG A 1 302 ? -5.025  -22.040 -58.601 1.00 40.77 ? 302 ARG A NH2 1 
ATOM   2201 N N   . THR A 1 303 ? -1.239  -14.876 -53.858 1.00 36.63 ? 303 THR A N   1 
ATOM   2202 C CA  . THR A 1 303 ? -1.135  -13.769 -52.898 1.00 36.95 ? 303 THR A CA  1 
ATOM   2203 C C   . THR A 1 303 ? -0.616  -12.533 -53.623 1.00 37.36 ? 303 THR A C   1 
ATOM   2204 O O   . THR A 1 303 ? -1.088  -11.419 -53.381 1.00 37.44 ? 303 THR A O   1 
ATOM   2205 C CB  . THR A 1 303 ? -0.166  -14.084 -51.725 1.00 36.90 ? 303 THR A CB  1 
ATOM   2206 O OG1 . THR A 1 303 ? -0.602  -15.258 -51.025 1.00 36.65 ? 303 THR A OG1 1 
ATOM   2207 C CG2 . THR A 1 303 ? -0.109  -12.915 -50.739 1.00 37.02 ? 303 THR A CG2 1 
ATOM   2208 N N   . HIS A 1 304 ? 0.355   -12.745 -54.510 1.00 37.90 ? 304 HIS A N   1 
ATOM   2209 C CA  . HIS A 1 304 ? 0.986   -11.661 -55.261 1.00 38.48 ? 304 HIS A CA  1 
ATOM   2210 C C   . HIS A 1 304 ? 0.077   -11.078 -56.346 1.00 38.88 ? 304 HIS A C   1 
ATOM   2211 O O   . HIS A 1 304 ? 0.056   -9.865  -56.551 1.00 38.72 ? 304 HIS A O   1 
ATOM   2212 C CB  . HIS A 1 304 ? 2.310   -12.139 -55.869 1.00 38.43 ? 304 HIS A CB  1 
ATOM   2213 C CG  . HIS A 1 304 ? 3.013   -11.099 -56.685 1.00 38.68 ? 304 HIS A CG  1 
ATOM   2214 N ND1 . HIS A 1 304 ? 3.411   -11.320 -57.986 1.00 38.32 ? 304 HIS A ND1 1 
ATOM   2215 C CD2 . HIS A 1 304 ? 3.381   -9.829  -56.388 1.00 38.62 ? 304 HIS A CD2 1 
ATOM   2216 C CE1 . HIS A 1 304 ? 4.001   -10.234 -58.453 1.00 38.20 ? 304 HIS A CE1 1 
ATOM   2217 N NE2 . HIS A 1 304 ? 3.995   -9.314  -57.504 1.00 38.27 ? 304 HIS A NE2 1 
ATOM   2218 N N   . ASN A 1 305 ? -0.670  -11.945 -57.031 1.00 39.61 ? 305 ASN A N   1 
ATOM   2219 C CA  . ASN A 1 305 ? -1.538  -11.530 -58.138 1.00 40.31 ? 305 ASN A CA  1 
ATOM   2220 C C   . ASN A 1 305 ? -2.881  -10.955 -57.691 1.00 40.77 ? 305 ASN A C   1 
ATOM   2221 O O   . ASN A 1 305 ? -3.471  -10.131 -58.394 1.00 40.77 ? 305 ASN A O   1 
ATOM   2222 C CB  . ASN A 1 305 ? -1.774  -12.696 -59.109 1.00 40.34 ? 305 ASN A CB  1 
ATOM   2223 C CG  . ASN A 1 305 ? -0.504  -13.125 -59.844 1.00 40.79 ? 305 ASN A CG  1 
ATOM   2224 O OD1 . ASN A 1 305 ? 0.584   -12.581 -59.627 1.00 41.28 ? 305 ASN A OD1 1 
ATOM   2225 N ND2 . ASN A 1 305 ? -0.643  -14.116 -60.719 1.00 41.29 ? 305 ASN A ND2 1 
ATOM   2226 N N   . GLY A 1 306 ? -3.357  -11.397 -56.525 1.00 41.45 ? 306 GLY A N   1 
ATOM   2227 C CA  . GLY A 1 306 ? -4.680  -11.022 -56.025 1.00 42.15 ? 306 GLY A CA  1 
ATOM   2228 C C   . GLY A 1 306 ? -5.730  -12.076 -56.327 1.00 42.74 ? 306 GLY A C   1 
ATOM   2229 O O   . GLY A 1 306 ? -6.922  -11.776 -56.355 1.00 42.72 ? 306 GLY A O   1 
ATOM   2230 N N   . GLU A 1 307 ? -5.282  -13.314 -56.544 1.00 43.47 ? 307 GLU A N   1 
ATOM   2231 C CA  . GLU A 1 307 ? -6.162  -14.430 -56.911 1.00 44.29 ? 307 GLU A CA  1 
ATOM   2232 C C   . GLU A 1 307 ? -6.631  -15.263 -55.718 1.00 44.67 ? 307 GLU A C   1 
ATOM   2233 O O   . GLU A 1 307 ? -6.101  -15.138 -54.614 1.00 44.83 ? 307 GLU A O   1 
ATOM   2234 C CB  . GLU A 1 307 ? -5.452  -15.350 -57.898 1.00 44.33 ? 307 GLU A CB  1 
ATOM   2235 C CG  . GLU A 1 307 ? -5.848  -15.175 -59.347 1.00 45.24 ? 307 GLU A CG  1 
ATOM   2236 C CD  . GLU A 1 307 ? -5.069  -16.120 -60.242 1.00 46.84 ? 307 GLU A CD  1 
ATOM   2237 O OE1 . GLU A 1 307 ? -5.707  -16.982 -60.914 1.00 47.24 ? 307 GLU A OE1 1 
ATOM   2238 O OE2 . GLU A 1 307 ? -3.812  -16.009 -60.265 1.00 47.77 ? 307 GLU A OE2 1 
ATOM   2239 N N   . SER A 1 308 ? -7.610  -16.133 -55.965 1.00 45.14 ? 308 SER A N   1 
ATOM   2240 C CA  . SER A 1 308 ? -8.196  -16.968 -54.923 1.00 45.59 ? 308 SER A CA  1 
ATOM   2241 C C   . SER A 1 308 ? -7.306  -18.140 -54.544 1.00 46.03 ? 308 SER A C   1 
ATOM   2242 O O   . SER A 1 308 ? -7.238  -19.148 -55.271 1.00 45.96 ? 308 SER A O   1 
ATOM   2243 C CB  . SER A 1 308 ? -9.570  -17.490 -55.351 1.00 45.63 ? 308 SER A CB  1 
ATOM   2244 O OG  . SER A 1 308 ? -9.963  -18.584 -54.536 1.00 45.42 ? 308 SER A OG  1 
ATOM   2245 N N   . VAL A 1 309 ? -6.648  -18.012 -53.387 1.00 46.71 ? 309 VAL A N   1 
ATOM   2246 C CA  . VAL A 1 309 ? -5.875  -19.120 -52.827 1.00 47.44 ? 309 VAL A CA  1 
ATOM   2247 C C   . VAL A 1 309 ? -6.806  -20.192 -52.240 1.00 47.90 ? 309 VAL A C   1 
ATOM   2248 O O   . VAL A 1 309 ? -6.372  -21.314 -51.978 1.00 48.01 ? 309 VAL A O   1 
ATOM   2249 C CB  . VAL A 1 309 ? -4.830  -18.646 -51.770 1.00 47.43 ? 309 VAL A CB  1 
ATOM   2250 C CG1 . VAL A 1 309 ? -4.174  -17.316 -52.190 1.00 47.73 ? 309 VAL A CG1 1 
ATOM   2251 C CG2 . VAL A 1 309 ? -5.442  -18.531 -50.376 1.00 47.53 ? 309 VAL A CG2 1 
ATOM   2252 N N   . SER A 1 310 ? -8.083  -19.841 -52.055 1.00 48.54 ? 310 SER A N   1 
ATOM   2253 C CA  . SER A 1 310 ? -9.085  -20.749 -51.481 1.00 49.17 ? 310 SER A CA  1 
ATOM   2254 C C   . SER A 1 310 ? -9.334  -21.985 -52.339 1.00 49.56 ? 310 SER A C   1 
ATOM   2255 O O   . SER A 1 310 ? -9.776  -23.014 -51.827 1.00 49.65 ? 310 SER A O   1 
ATOM   2256 C CB  . SER A 1 310 ? -10.408 -20.023 -51.230 1.00 49.20 ? 310 SER A CB  1 
ATOM   2257 O OG  . SER A 1 310 ? -11.053 -19.697 -52.465 1.00 49.51 ? 310 SER A OG  1 
ATOM   2258 N N   . TYR A 1 311 ? -9.061  -21.874 -53.639 1.00 50.09 ? 311 TYR A N   1 
ATOM   2259 C CA  . TYR A 1 311 ? -9.139  -23.013 -54.555 1.00 50.58 ? 311 TYR A CA  1 
ATOM   2260 C C   . TYR A 1 311 ? -8.162  -24.120 -54.150 1.00 50.87 ? 311 TYR A C   1 
ATOM   2261 O O   . TYR A 1 311 ? -8.374  -25.293 -54.470 1.00 50.90 ? 311 TYR A O   1 
ATOM   2262 C CB  . TYR A 1 311 ? -8.866  -22.567 -55.995 1.00 50.60 ? 311 TYR A CB  1 
ATOM   2263 N N   . LEU A 1 312 ? -7.105  -23.731 -53.434 1.00 51.30 ? 312 LEU A N   1 
ATOM   2264 C CA  . LEU A 1 312 ? -6.096  -24.662 -52.920 1.00 51.75 ? 312 LEU A CA  1 
ATOM   2265 C C   . LEU A 1 312 ? -6.592  -25.468 -51.715 1.00 52.11 ? 312 LEU A C   1 
ATOM   2266 O O   . LEU A 1 312 ? -5.949  -26.440 -51.306 1.00 52.13 ? 312 LEU A O   1 
ATOM   2267 C CB  . LEU A 1 312 ? -4.803  -23.917 -52.559 1.00 51.64 ? 312 LEU A CB  1 
ATOM   2268 C CG  . LEU A 1 312 ? -3.745  -23.553 -53.612 1.00 51.62 ? 312 LEU A CG  1 
ATOM   2269 C CD1 . LEU A 1 312 ? -4.322  -23.118 -54.958 1.00 51.98 ? 312 LEU A CD1 1 
ATOM   2270 C CD2 . LEU A 1 312 ? -2.822  -22.476 -53.064 1.00 51.25 ? 312 LEU A CD2 1 
ATOM   2271 N N   . PHE A 1 313 ? -7.731  -25.066 -51.152 1.00 52.56 ? 313 PHE A N   1 
ATOM   2272 C CA  . PHE A 1 313 ? -8.351  -25.819 -50.058 1.00 53.03 ? 313 PHE A CA  1 
ATOM   2273 C C   . PHE A 1 313 ? -8.933  -27.152 -50.540 1.00 53.33 ? 313 PHE A C   1 
ATOM   2274 O O   . PHE A 1 313 ? -9.240  -28.026 -49.725 1.00 53.41 ? 313 PHE A O   1 
ATOM   2275 C CB  . PHE A 1 313 ? -9.445  -25.003 -49.347 1.00 52.98 ? 313 PHE A CB  1 
ATOM   2276 C CG  . PHE A 1 313 ? -8.953  -23.737 -48.680 1.00 52.99 ? 313 PHE A CG  1 
ATOM   2277 C CD1 . PHE A 1 313 ? -7.601  -23.581 -48.327 1.00 53.02 ? 313 PHE A CD1 1 
ATOM   2278 C CD2 . PHE A 1 313 ? -9.859  -22.710 -48.376 1.00 53.10 ? 313 PHE A CD2 1 
ATOM   2279 C CE1 . PHE A 1 313 ? -7.160  -22.409 -47.706 1.00 53.15 ? 313 PHE A CE1 1 
ATOM   2280 C CE2 . PHE A 1 313 ? -9.428  -21.536 -47.753 1.00 53.29 ? 313 PHE A CE2 1 
ATOM   2281 C CZ  . PHE A 1 313 ? -8.076  -21.386 -47.418 1.00 53.21 ? 313 PHE A CZ  1 
ATOM   2282 N N   . SER A 1 314 ? -9.074  -27.300 -51.861 1.00 53.69 ? 314 SER A N   1 
ATOM   2283 C CA  . SER A 1 314 ? -9.723  -28.472 -52.460 1.00 53.98 ? 314 SER A CA  1 
ATOM   2284 C C   . SER A 1 314 ? -8.996  -29.052 -53.680 1.00 54.21 ? 314 SER A C   1 
ATOM   2285 O O   . SER A 1 314 ? -8.960  -30.272 -53.859 1.00 54.30 ? 314 SER A O   1 
ATOM   2286 C CB  . SER A 1 314 ? -11.178 -28.155 -52.811 1.00 53.98 ? 314 SER A CB  1 
ATOM   2287 N N   . HIS A 1 315 ? -8.431  -28.183 -54.518 1.00 54.40 ? 315 HIS A N   1 
ATOM   2288 C CA  . HIS A 1 315 ? -7.770  -28.623 -55.753 1.00 54.63 ? 315 HIS A CA  1 
ATOM   2289 C C   . HIS A 1 315 ? -6.268  -28.863 -55.558 1.00 54.80 ? 315 HIS A C   1 
ATOM   2290 O O   . HIS A 1 315 ? -5.524  -27.938 -55.203 1.00 54.91 ? 315 HIS A O   1 
ATOM   2291 C CB  . HIS A 1 315 ? -8.017  -27.622 -56.886 1.00 54.57 ? 315 HIS A CB  1 
ATOM   2292 N N   . VAL A 1 316 ? -5.843  -30.110 -55.800 1.00 54.90 ? 316 VAL A N   1 
ATOM   2293 C CA  . VAL A 1 316 ? -4.447  -30.529 -55.617 1.00 55.05 ? 316 VAL A CA  1 
ATOM   2294 C C   . VAL A 1 316 ? -3.442  -29.601 -56.300 1.00 55.16 ? 316 VAL A C   1 
ATOM   2295 O O   . VAL A 1 316 ? -3.510  -29.357 -57.511 1.00 55.27 ? 316 VAL A O   1 
ATOM   2296 C CB  . VAL A 1 316 ? -4.255  -31.967 -56.097 1.00 55.03 ? 316 VAL A CB  1 
ATOM   2297 N N   . ASN B 1 3   ? 6.098   -10.431 -1.900  1.00 35.99 ? 3   ASN B N   1 
ATOM   2298 C CA  . ASN B 1 3   ? 5.717   -9.477  -2.985  1.00 36.04 ? 3   ASN B CA  1 
ATOM   2299 C C   . ASN B 1 3   ? 6.695   -9.495  -4.162  1.00 35.77 ? 3   ASN B C   1 
ATOM   2300 O O   . ASN B 1 3   ? 6.324   -9.191  -5.298  1.00 35.78 ? 3   ASN B O   1 
ATOM   2301 C CB  . ASN B 1 3   ? 5.574   -8.058  -2.427  1.00 36.20 ? 3   ASN B CB  1 
ATOM   2302 C CG  . ASN B 1 3   ? 4.754   -7.161  -3.332  1.00 36.63 ? 3   ASN B CG  1 
ATOM   2303 O OD1 . ASN B 1 3   ? 3.561   -7.384  -3.531  1.00 37.39 ? 3   ASN B OD1 1 
ATOM   2304 N ND2 . ASN B 1 3   ? 5.390   -6.136  -3.883  1.00 37.14 ? 3   ASN B ND2 1 
ATOM   2305 N N   . ILE B 1 4   ? 7.944   -9.851  -3.875  1.00 35.45 ? 4   ILE B N   1 
ATOM   2306 C CA  . ILE B 1 4   ? 8.981   -9.976  -4.896  1.00 35.05 ? 4   ILE B CA  1 
ATOM   2307 C C   . ILE B 1 4   ? 9.312   -11.449 -5.166  1.00 34.82 ? 4   ILE B C   1 
ATOM   2308 O O   . ILE B 1 4   ? 9.495   -12.233 -4.232  1.00 34.68 ? 4   ILE B O   1 
ATOM   2309 C CB  . ILE B 1 4   ? 10.256  -9.172  -4.510  1.00 35.09 ? 4   ILE B CB  1 
ATOM   2310 C CG1 . ILE B 1 4   ? 11.390  -9.425  -5.516  1.00 34.95 ? 4   ILE B CG1 1 
ATOM   2311 C CG2 . ILE B 1 4   ? 10.690  -9.479  -3.060  1.00 35.16 ? 4   ILE B CG2 1 
ATOM   2312 C CD1 . ILE B 1 4   ? 12.575  -8.518  -5.325  1.00 35.43 ? 4   ILE B CD1 1 
ATOM   2313 N N   . LYS B 1 5   ? 9.369   -11.817 -6.445  1.00 34.57 ? 5   LYS B N   1 
ATOM   2314 C CA  . LYS B 1 5   ? 9.728   -13.178 -6.847  1.00 34.42 ? 5   LYS B CA  1 
ATOM   2315 C C   . LYS B 1 5   ? 10.856  -13.182 -7.878  1.00 34.13 ? 5   LYS B C   1 
ATOM   2316 O O   . LYS B 1 5   ? 10.838  -12.405 -8.838  1.00 34.03 ? 5   LYS B O   1 
ATOM   2317 C CB  . LYS B 1 5   ? 8.508   -13.926 -7.399  1.00 34.53 ? 5   LYS B CB  1 
ATOM   2318 C CG  . LYS B 1 5   ? 7.448   -14.279 -6.360  1.00 34.99 ? 5   LYS B CG  1 
ATOM   2319 C CD  . LYS B 1 5   ? 7.835   -15.510 -5.535  1.00 36.14 ? 5   LYS B CD  1 
ATOM   2320 C CE  . LYS B 1 5   ? 6.903   -15.694 -4.347  1.00 37.17 ? 5   LYS B CE  1 
ATOM   2321 N NZ  . LYS B 1 5   ? 7.445   -16.719 -3.388  1.00 37.90 ? 5   LYS B NZ  1 
ATOM   2322 N N   . ILE B 1 6   ? 11.839  -14.054 -7.668  1.00 33.93 ? 6   ILE B N   1 
ATOM   2323 C CA  . ILE B 1 6   ? 12.928  -14.210 -8.624  1.00 33.87 ? 6   ILE B CA  1 
ATOM   2324 C C   . ILE B 1 6   ? 12.835  -15.580 -9.280  1.00 34.04 ? 6   ILE B C   1 
ATOM   2325 O O   . ILE B 1 6   ? 12.769  -16.605 -8.593  1.00 33.85 ? 6   ILE B O   1 
ATOM   2326 C CB  . ILE B 1 6   ? 14.332  -14.085 -7.986  1.00 33.68 ? 6   ILE B CB  1 
ATOM   2327 C CG1 . ILE B 1 6   ? 14.320  -13.206 -6.729  1.00 33.18 ? 6   ILE B CG1 1 
ATOM   2328 C CG2 . ILE B 1 6   ? 15.346  -13.618 -9.047  1.00 33.68 ? 6   ILE B CG2 1 
ATOM   2329 C CD1 . ILE B 1 6   ? 14.960  -11.817 -6.907  1.00 33.42 ? 6   ILE B CD1 1 
ATOM   2330 N N   . PHE B 1 7   ? 12.823  -15.591 -10.609 1.00 34.34 ? 7   PHE B N   1 
ATOM   2331 C CA  . PHE B 1 7   ? 12.911  -16.835 -11.359 1.00 34.92 ? 7   PHE B CA  1 
ATOM   2332 C C   . PHE B 1 7   ? 14.198  -16.867 -12.173 1.00 35.53 ? 7   PHE B C   1 
ATOM   2333 O O   . PHE B 1 7   ? 14.669  -15.834 -12.652 1.00 35.43 ? 7   PHE B O   1 
ATOM   2334 C CB  . PHE B 1 7   ? 11.699  -17.019 -12.286 1.00 34.79 ? 7   PHE B CB  1 
ATOM   2335 C CG  . PHE B 1 7   ? 10.415  -17.329 -11.560 1.00 34.09 ? 7   PHE B CG  1 
ATOM   2336 C CD1 . PHE B 1 7   ? 10.032  -18.646 -11.332 1.00 33.23 ? 7   PHE B CD1 1 
ATOM   2337 C CD2 . PHE B 1 7   ? 9.576   -16.303 -11.124 1.00 33.58 ? 7   PHE B CD2 1 
ATOM   2338 C CE1 . PHE B 1 7   ? 8.838   -18.943 -10.676 1.00 32.82 ? 7   PHE B CE1 1 
ATOM   2339 C CE2 . PHE B 1 7   ? 8.383   -16.587 -10.460 1.00 32.90 ? 7   PHE B CE2 1 
ATOM   2340 C CZ  . PHE B 1 7   ? 8.014   -17.909 -10.236 1.00 32.94 ? 7   PHE B CZ  1 
ATOM   2341 N N   . SER B 1 8   ? 14.760  -18.062 -12.321 1.00 36.49 ? 8   SER B N   1 
ATOM   2342 C CA  . SER B 1 8   ? 15.942  -18.268 -13.140 1.00 37.49 ? 8   SER B CA  1 
ATOM   2343 C C   . SER B 1 8   ? 15.529  -18.921 -14.444 1.00 38.25 ? 8   SER B C   1 
ATOM   2344 O O   . SER B 1 8   ? 14.827  -19.943 -14.444 1.00 38.37 ? 8   SER B O   1 
ATOM   2345 C CB  . SER B 1 8   ? 16.933  -19.179 -12.412 1.00 37.60 ? 8   SER B CB  1 
ATOM   2346 O OG  . SER B 1 8   ? 18.120  -19.359 -13.167 1.00 37.80 ? 8   SER B OG  1 
ATOM   2347 N N   . GLY B 1 9   ? 15.955  -18.317 -15.555 1.00 39.14 ? 9   GLY B N   1 
ATOM   2348 C CA  . GLY B 1 9   ? 15.812  -18.974 -16.879 1.00 40.12 ? 9   GLY B CA  1 
ATOM   2349 C C   . GLY B 1 9   ? 17.023  -19.881 -17.068 1.00 40.89 ? 9   GLY B C   1 
ATOM   2350 O O   . GLY B 1 9   ? 17.792  -20.157 -16.080 1.00 41.25 ? 9   GLY B O   1 
ATOM   2351 N N   . SER B 1 10  ? 17.190  -20.350 -18.326 1.00 41.49 ? 10  SER B N   1 
ATOM   2352 C CA  . SER B 1 10  ? 18.370  -21.159 -18.678 1.00 42.03 ? 10  SER B CA  1 
ATOM   2353 C C   . SER B 1 10  ? 18.477  -22.447 -17.830 1.00 42.24 ? 10  SER B C   1 
ATOM   2354 O O   . SER B 1 10  ? 17.441  -23.036 -17.389 1.00 42.42 ? 10  SER B O   1 
ATOM   2355 C CB  . SER B 1 10  ? 19.655  -20.307 -18.583 1.00 42.06 ? 10  SER B CB  1 
ATOM   2356 O OG  . SER B 1 10  ? 20.740  -20.921 -19.268 1.00 42.70 ? 10  SER B OG  1 
ATOM   2357 N N   . SER B 1 11  ? 19.713  -22.880 -17.604 1.00 42.44 ? 11  SER B N   1 
ATOM   2358 C CA  . SER B 1 11  ? 19.999  -24.020 -16.745 1.00 42.64 ? 11  SER B CA  1 
ATOM   2359 C C   . SER B 1 11  ? 21.015  -23.585 -15.699 1.00 42.60 ? 11  SER B C   1 
ATOM   2360 O O   . SER B 1 11  ? 21.105  -24.163 -14.616 1.00 42.82 ? 11  SER B O   1 
ATOM   2361 C CB  . SER B 1 11  ? 20.546  -25.189 -17.564 1.00 42.71 ? 11  SER B CB  1 
ATOM   2362 O OG  . SER B 1 11  ? 21.812  -24.875 -18.118 1.00 43.07 ? 11  SER B OG  1 
ATOM   2363 N N   . HIS B 1 12  ? 21.776  -22.550 -16.042 1.00 42.40 ? 12  HIS B N   1 
ATOM   2364 C CA  . HIS B 1 12  ? 22.751  -21.957 -15.137 1.00 42.23 ? 12  HIS B CA  1 
ATOM   2365 C C   . HIS B 1 12  ? 22.006  -21.127 -14.093 1.00 41.87 ? 12  HIS B C   1 
ATOM   2366 O O   . HIS B 1 12  ? 21.753  -19.930 -14.290 1.00 41.94 ? 12  HIS B O   1 
ATOM   2367 C CB  . HIS B 1 12  ? 23.748  -21.072 -15.905 1.00 42.39 ? 12  HIS B CB  1 
ATOM   2368 C CG  . HIS B 1 12  ? 24.254  -21.678 -17.183 1.00 43.06 ? 12  HIS B CG  1 
ATOM   2369 N ND1 . HIS B 1 12  ? 23.378  -22.064 -18.216 1.00 43.81 ? 12  HIS B ND1 1 
ATOM   2370 C CD2 . HIS B 1 12  ? 25.555  -21.929 -17.607 1.00 43.41 ? 12  HIS B CD2 1 
ATOM   2371 C CE1 . HIS B 1 12  ? 24.112  -22.547 -19.210 1.00 43.75 ? 12  HIS B CE1 1 
ATOM   2372 N NE2 . HIS B 1 12  ? 25.438  -22.472 -18.868 1.00 43.59 ? 12  HIS B NE2 1 
ATOM   2373 N N   . GLN B 1 13  ? 21.640  -21.774 -12.989 1.00 41.28 ? 13  GLN B N   1 
ATOM   2374 C CA  . GLN B 1 13  ? 20.939  -21.090 -11.906 1.00 40.69 ? 13  GLN B CA  1 
ATOM   2375 C C   . GLN B 1 13  ? 21.933  -20.424 -10.953 1.00 40.01 ? 13  GLN B C   1 
ATOM   2376 O O   . GLN B 1 13  ? 21.542  -19.894 -9.909  1.00 40.02 ? 13  GLN B O   1 
ATOM   2377 C CB  . GLN B 1 13  ? 20.021  -22.054 -11.144 1.00 40.86 ? 13  GLN B CB  1 
ATOM   2378 C CG  . GLN B 1 13  ? 18.967  -22.742 -12.007 1.00 41.42 ? 13  GLN B CG  1 
ATOM   2379 C CD  . GLN B 1 13  ? 17.657  -22.966 -11.243 1.00 42.45 ? 13  GLN B CD  1 
ATOM   2380 O OE1 . GLN B 1 13  ? 16.838  -22.042 -11.098 1.00 42.71 ? 13  GLN B OE1 1 
ATOM   2381 N NE2 . GLN B 1 13  ? 17.448  -24.201 -10.761 1.00 42.57 ? 13  GLN B NE2 1 
ATOM   2382 N N   . ASP B 1 14  ? 23.210  -20.443 -11.336 1.00 39.08 ? 14  ASP B N   1 
ATOM   2383 C CA  . ASP B 1 14  ? 24.303  -19.942 -10.502 1.00 38.28 ? 14  ASP B CA  1 
ATOM   2384 C C   . ASP B 1 14  ? 24.171  -18.462 -10.143 1.00 37.46 ? 14  ASP B C   1 
ATOM   2385 O O   . ASP B 1 14  ? 23.942  -18.129 -8.978  1.00 37.32 ? 14  ASP B O   1 
ATOM   2386 C CB  . ASP B 1 14  ? 25.670  -20.246 -11.140 1.00 38.50 ? 14  ASP B CB  1 
ATOM   2387 C CG  . ASP B 1 14  ? 25.649  -20.161 -12.666 1.00 39.26 ? 14  ASP B CG  1 
ATOM   2388 O OD1 . ASP B 1 14  ? 26.026  -21.165 -13.316 1.00 40.15 ? 14  ASP B OD1 1 
ATOM   2389 O OD2 . ASP B 1 14  ? 25.260  -19.097 -13.215 1.00 39.51 ? 14  ASP B OD2 1 
ATOM   2390 N N   . LEU B 1 15  ? 24.307  -17.583 -11.138 1.00 36.49 ? 15  LEU B N   1 
ATOM   2391 C CA  . LEU B 1 15  ? 24.172  -16.138 -10.925 1.00 35.50 ? 15  LEU B CA  1 
ATOM   2392 C C   . LEU B 1 15  ? 22.811  -15.811 -10.317 1.00 35.09 ? 15  LEU B C   1 
ATOM   2393 O O   . LEU B 1 15  ? 22.705  -14.933 -9.460  1.00 35.04 ? 15  LEU B O   1 
ATOM   2394 C CB  . LEU B 1 15  ? 24.380  -15.358 -12.235 1.00 35.25 ? 15  LEU B CB  1 
ATOM   2395 C CG  . LEU B 1 15  ? 24.322  -13.822 -12.171 1.00 34.67 ? 15  LEU B CG  1 
ATOM   2396 C CD1 . LEU B 1 15  ? 25.604  -13.228 -11.580 1.00 33.96 ? 15  LEU B CD1 1 
ATOM   2397 C CD2 . LEU B 1 15  ? 24.046  -13.225 -13.549 1.00 33.69 ? 15  LEU B CD2 1 
ATOM   2398 N N   . SER B 1 16  ? 21.782  -16.533 -10.761 1.00 34.54 ? 16  SER B N   1 
ATOM   2399 C CA  . SER B 1 16  ? 20.430  -16.388 -10.231 1.00 34.08 ? 16  SER B CA  1 
ATOM   2400 C C   . SER B 1 16  ? 20.388  -16.613 -8.724  1.00 33.76 ? 16  SER B C   1 
ATOM   2401 O O   . SER B 1 16  ? 19.900  -15.753 -7.990  1.00 33.64 ? 16  SER B O   1 
ATOM   2402 C CB  . SER B 1 16  ? 19.474  -17.358 -10.924 1.00 34.15 ? 16  SER B CB  1 
ATOM   2403 O OG  . SER B 1 16  ? 19.498  -17.194 -12.330 1.00 34.26 ? 16  SER B OG  1 
ATOM   2404 N N   . GLN B 1 17  ? 20.909  -17.761 -8.278  1.00 33.43 ? 17  GLN B N   1 
ATOM   2405 C CA  . GLN B 1 17  ? 20.941  -18.124 -6.856  1.00 33.27 ? 17  GLN B CA  1 
ATOM   2406 C C   . GLN B 1 17  ? 21.659  -17.113 -5.981  1.00 33.04 ? 17  GLN B C   1 
ATOM   2407 O O   . GLN B 1 17  ? 21.188  -16.801 -4.888  1.00 33.04 ? 17  GLN B O   1 
ATOM   2408 C CB  . GLN B 1 17  ? 21.546  -19.518 -6.626  1.00 33.37 ? 17  GLN B CB  1 
ATOM   2409 C CG  . GLN B 1 17  ? 20.520  -20.628 -6.335  1.00 34.24 ? 17  GLN B CG  1 
ATOM   2410 C CD  . GLN B 1 17  ? 19.608  -20.317 -5.133  1.00 35.56 ? 17  GLN B CD  1 
ATOM   2411 O OE1 . GLN B 1 17  ? 19.996  -19.610 -4.190  1.00 35.96 ? 17  GLN B OE1 1 
ATOM   2412 N NE2 . GLN B 1 17  ? 18.388  -20.852 -5.171  1.00 35.69 ? 17  GLN B NE2 1 
ATOM   2413 N N   . LYS B 1 18  ? 22.796  -16.605 -6.457  1.00 32.72 ? 18  LYS B N   1 
ATOM   2414 C CA  . LYS B 1 18  ? 23.567  -15.615 -5.703  1.00 32.46 ? 18  LYS B CA  1 
ATOM   2415 C C   . LYS B 1 18  ? 22.722  -14.374 -5.443  1.00 32.02 ? 18  LYS B C   1 
ATOM   2416 O O   . LYS B 1 18  ? 22.669  -13.891 -4.312  1.00 32.01 ? 18  LYS B O   1 
ATOM   2417 C CB  . LYS B 1 18  ? 24.876  -15.258 -6.420  1.00 32.70 ? 18  LYS B CB  1 
ATOM   2418 C CG  . LYS B 1 18  ? 25.855  -16.420 -6.496  1.00 33.42 ? 18  LYS B CG  1 
ATOM   2419 C CD  . LYS B 1 18  ? 27.218  -15.999 -7.047  1.00 35.43 ? 18  LYS B CD  1 
ATOM   2420 C CE  . LYS B 1 18  ? 28.103  -17.222 -7.243  1.00 36.32 ? 18  LYS B CE  1 
ATOM   2421 N NZ  . LYS B 1 18  ? 29.551  -16.896 -7.028  1.00 37.06 ? 18  LYS B NZ  1 
ATOM   2422 N N   . ILE B 1 19  ? 22.046  -13.888 -6.487  1.00 31.50 ? 19  ILE B N   1 
ATOM   2423 C CA  . ILE B 1 19  ? 21.125  -12.756 -6.370  1.00 30.95 ? 19  ILE B CA  1 
ATOM   2424 C C   . ILE B 1 19  ? 20.022  -13.098 -5.372  1.00 30.94 ? 19  ILE B C   1 
ATOM   2425 O O   . ILE B 1 19  ? 19.696  -12.289 -4.501  1.00 30.83 ? 19  ILE B O   1 
ATOM   2426 C CB  . ILE B 1 19  ? 20.501  -12.358 -7.736  1.00 30.86 ? 19  ILE B CB  1 
ATOM   2427 C CG1 . ILE B 1 19  ? 21.593  -12.005 -8.758  1.00 30.33 ? 19  ILE B CG1 1 
ATOM   2428 C CG2 . ILE B 1 19  ? 19.519  -11.190 -7.564  1.00 30.47 ? 19  ILE B CG2 1 
ATOM   2429 C CD1 . ILE B 1 19  ? 21.131  -12.052 -10.216 1.00 28.94 ? 19  ILE B CD1 1 
ATOM   2430 N N   . ALA B 1 20  ? 19.467  -14.304 -5.497  1.00 30.91 ? 20  ALA B N   1 
ATOM   2431 C CA  . ALA B 1 20  ? 18.449  -14.792 -4.568  1.00 30.93 ? 20  ALA B CA  1 
ATOM   2432 C C   . ALA B 1 20  ? 18.951  -14.776 -3.119  1.00 30.98 ? 20  ALA B C   1 
ATOM   2433 O O   . ALA B 1 20  ? 18.274  -14.237 -2.238  1.00 30.86 ? 20  ALA B O   1 
ATOM   2434 C CB  . ALA B 1 20  ? 17.987  -16.182 -4.968  1.00 30.84 ? 20  ALA B CB  1 
ATOM   2435 N N   . ASP B 1 21  ? 20.137  -15.354 -2.890  1.00 31.08 ? 21  ASP B N   1 
ATOM   2436 C CA  . ASP B 1 21  ? 20.778  -15.362 -1.571  1.00 31.30 ? 21  ASP B CA  1 
ATOM   2437 C C   . ASP B 1 21  ? 20.928  -13.952 -1.005  1.00 31.23 ? 21  ASP B C   1 
ATOM   2438 O O   . ASP B 1 21  ? 20.533  -13.688 0.134   1.00 31.23 ? 21  ASP B O   1 
ATOM   2439 C CB  . ASP B 1 21  ? 22.162  -16.023 -1.622  1.00 31.51 ? 21  ASP B CB  1 
ATOM   2440 C CG  . ASP B 1 21  ? 22.111  -17.483 -2.032  1.00 32.42 ? 21  ASP B CG  1 
ATOM   2441 O OD1 . ASP B 1 21  ? 21.006  -18.064 -2.058  1.00 32.96 ? 21  ASP B OD1 1 
ATOM   2442 O OD2 . ASP B 1 21  ? 23.188  -18.049 -2.333  1.00 33.26 ? 21  ASP B OD2 1 
ATOM   2443 N N   . ARG B 1 22  ? 21.488  -13.047 -1.808  1.00 31.19 ? 22  ARG B N   1 
ATOM   2444 C CA  . ARG B 1 22  ? 21.763  -11.687 -1.345  1.00 31.21 ? 22  ARG B CA  1 
ATOM   2445 C C   . ARG B 1 22  ? 20.487  -10.934 -0.964  1.00 30.84 ? 22  ARG B C   1 
ATOM   2446 O O   . ARG B 1 22  ? 20.548  -9.914  -0.277  1.00 31.03 ? 22  ARG B O   1 
ATOM   2447 C CB  . ARG B 1 22  ? 22.607  -10.903 -2.365  1.00 31.34 ? 22  ARG B CB  1 
ATOM   2448 C CG  . ARG B 1 22  ? 23.940  -11.578 -2.680  1.00 32.46 ? 22  ARG B CG  1 
ATOM   2449 C CD  . ARG B 1 22  ? 25.105  -10.603 -2.867  1.00 34.76 ? 22  ARG B CD  1 
ATOM   2450 N NE  . ARG B 1 22  ? 26.379  -11.323 -2.794  1.00 36.37 ? 22  ARG B NE  1 
ATOM   2451 C CZ  . ARG B 1 22  ? 27.569  -10.818 -3.132  1.00 37.04 ? 22  ARG B CZ  1 
ATOM   2452 N NH1 . ARG B 1 22  ? 27.683  -9.567  -3.571  1.00 37.19 ? 22  ARG B NH1 1 
ATOM   2453 N NH2 . ARG B 1 22  ? 28.655  -11.572 -3.030  1.00 37.13 ? 22  ARG B NH2 1 
ATOM   2454 N N   . LEU B 1 23  ? 19.337  -11.464 -1.378  1.00 30.43 ? 23  LEU B N   1 
ATOM   2455 C CA  . LEU B 1 23  ? 18.042  -10.831 -1.119  1.00 30.05 ? 23  LEU B CA  1 
ATOM   2456 C C   . LEU B 1 23  ? 17.205  -11.562 -0.068  1.00 29.81 ? 23  LEU B C   1 
ATOM   2457 O O   . LEU B 1 23  ? 16.062  -11.183 0.195   1.00 29.72 ? 23  LEU B O   1 
ATOM   2458 C CB  . LEU B 1 23  ? 17.246  -10.688 -2.423  1.00 29.99 ? 23  LEU B CB  1 
ATOM   2459 C CG  . LEU B 1 23  ? 17.803  -9.765  -3.511  1.00 29.73 ? 23  LEU B CG  1 
ATOM   2460 C CD1 . LEU B 1 23  ? 16.820  -9.671  -4.664  1.00 29.53 ? 23  LEU B CD1 1 
ATOM   2461 C CD2 . LEU B 1 23  ? 18.100  -8.376  -2.960  1.00 30.11 ? 23  LEU B CD2 1 
ATOM   2462 N N   . GLY B 1 24  ? 17.782  -12.607 0.527   1.00 29.56 ? 24  GLY B N   1 
ATOM   2463 C CA  . GLY B 1 24  ? 17.087  -13.421 1.529   1.00 29.23 ? 24  GLY B CA  1 
ATOM   2464 C C   . GLY B 1 24  ? 15.952  -14.230 0.929   1.00 29.04 ? 24  GLY B C   1 
ATOM   2465 O O   . GLY B 1 24  ? 14.967  -14.530 1.607   1.00 29.12 ? 24  GLY B O   1 
ATOM   2466 N N   . LEU B 1 25  ? 16.096  -14.588 -0.347  1.00 28.78 ? 25  LEU B N   1 
ATOM   2467 C CA  . LEU B 1 25  ? 15.015  -15.234 -1.086  1.00 28.55 ? 25  LEU B CA  1 
ATOM   2468 C C   . LEU B 1 25  ? 15.454  -16.531 -1.735  1.00 28.12 ? 25  LEU B C   1 
ATOM   2469 O O   . LEU B 1 25  ? 16.640  -16.740 -1.990  1.00 28.03 ? 25  LEU B O   1 
ATOM   2470 C CB  . LEU B 1 25  ? 14.469  -14.301 -2.175  1.00 28.62 ? 25  LEU B CB  1 
ATOM   2471 C CG  . LEU B 1 25  ? 13.734  -13.005 -1.824  1.00 29.09 ? 25  LEU B CG  1 
ATOM   2472 C CD1 . LEU B 1 25  ? 13.349  -12.262 -3.105  1.00 29.30 ? 25  LEU B CD1 1 
ATOM   2473 C CD2 . LEU B 1 25  ? 12.501  -13.278 -0.978  1.00 29.57 ? 25  LEU B CD2 1 
ATOM   2474 N N   . GLU B 1 26  ? 14.482  -17.398 -1.998  1.00 27.74 ? 26  GLU B N   1 
ATOM   2475 C CA  . GLU B 1 26  ? 14.712  -18.563 -2.840  1.00 27.58 ? 26  GLU B CA  1 
ATOM   2476 C C   . GLU B 1 26  ? 14.161  -18.293 -4.239  1.00 27.06 ? 26  GLU B C   1 
ATOM   2477 O O   . GLU B 1 26  ? 13.287  -17.434 -4.424  1.00 26.70 ? 26  GLU B O   1 
ATOM   2478 C CB  . GLU B 1 26  ? 14.070  -19.812 -2.228  1.00 27.72 ? 26  GLU B CB  1 
ATOM   2479 C CG  . GLU B 1 26  ? 14.827  -20.342 -1.013  1.00 29.01 ? 26  GLU B CG  1 
ATOM   2480 C CD  . GLU B 1 26  ? 14.111  -21.473 -0.294  1.00 31.04 ? 26  GLU B CD  1 
ATOM   2481 O OE1 . GLU B 1 26  ? 13.084  -21.981 -0.804  1.00 31.63 ? 26  GLU B OE1 1 
ATOM   2482 O OE2 . GLU B 1 26  ? 14.588  -21.859 0.795   1.00 32.09 ? 26  GLU B OE2 1 
ATOM   2483 N N   . LEU B 1 27  ? 14.696  -19.012 -5.223  1.00 26.72 ? 27  LEU B N   1 
ATOM   2484 C CA  . LEU B 1 27  ? 14.219  -18.896 -6.592  1.00 26.42 ? 27  LEU B CA  1 
ATOM   2485 C C   . LEU B 1 27  ? 12.874  -19.594 -6.718  1.00 26.36 ? 27  LEU B C   1 
ATOM   2486 O O   . LEU B 1 27  ? 12.672  -20.667 -6.140  1.00 26.08 ? 27  LEU B O   1 
ATOM   2487 C CB  . LEU B 1 27  ? 15.229  -19.514 -7.567  1.00 26.25 ? 27  LEU B CB  1 
ATOM   2488 C CG  . LEU B 1 27  ? 16.605  -18.862 -7.710  1.00 25.54 ? 27  LEU B CG  1 
ATOM   2489 C CD1 . LEU B 1 27  ? 17.533  -19.795 -8.468  1.00 24.68 ? 27  LEU B CD1 1 
ATOM   2490 C CD2 . LEU B 1 27  ? 16.518  -17.511 -8.407  1.00 25.29 ? 27  LEU B CD2 1 
ATOM   2491 N N   . GLY B 1 28  ? 11.962  -18.978 -7.471  1.00 26.55 ? 28  GLY B N   1 
ATOM   2492 C CA  . GLY B 1 28  ? 10.638  -19.555 -7.716  1.00 27.06 ? 28  GLY B CA  1 
ATOM   2493 C C   . GLY B 1 28  ? 10.697  -20.883 -8.454  1.00 27.63 ? 28  GLY B C   1 
ATOM   2494 O O   . GLY B 1 28  ? 11.651  -21.163 -9.192  1.00 27.39 ? 28  GLY B O   1 
ATOM   2495 N N   . LYS B 1 29  ? 9.675   -21.708 -8.253  1.00 28.27 ? 29  LYS B N   1 
ATOM   2496 C CA  . LYS B 1 29  ? 9.628   -23.023 -8.881  1.00 28.98 ? 29  LYS B CA  1 
ATOM   2497 C C   . LYS B 1 29  ? 9.303   -22.904 -10.370 1.00 29.51 ? 29  LYS B C   1 
ATOM   2498 O O   . LYS B 1 29  ? 8.324   -22.265 -10.756 1.00 29.63 ? 29  LYS B O   1 
ATOM   2499 C CB  . LYS B 1 29  ? 8.616   -23.932 -8.169  1.00 28.95 ? 29  LYS B CB  1 
ATOM   2500 N N   . VAL B 1 30  ? 10.155  -23.494 -11.202 1.00 30.17 ? 30  VAL B N   1 
ATOM   2501 C CA  . VAL B 1 30  ? 9.901   -23.569 -12.635 1.00 30.82 ? 30  VAL B CA  1 
ATOM   2502 C C   . VAL B 1 30  ? 10.232  -24.965 -13.115 1.00 31.36 ? 30  VAL B C   1 
ATOM   2503 O O   . VAL B 1 30  ? 11.366  -25.426 -12.969 1.00 31.39 ? 30  VAL B O   1 
ATOM   2504 C CB  . VAL B 1 30  ? 10.764  -22.582 -13.469 1.00 30.71 ? 30  VAL B CB  1 
ATOM   2505 C CG1 . VAL B 1 30  ? 10.038  -22.209 -14.753 1.00 30.42 ? 30  VAL B CG1 1 
ATOM   2506 C CG2 . VAL B 1 30  ? 11.116  -21.340 -12.681 1.00 30.68 ? 30  VAL B CG2 1 
ATOM   2507 N N   . VAL B 1 31  ? 9.239   -25.640 -13.679 1.00 32.13 ? 31  VAL B N   1 
ATOM   2508 C CA  . VAL B 1 31  ? 9.491   -26.876 -14.404 1.00 33.03 ? 31  VAL B CA  1 
ATOM   2509 C C   . VAL B 1 31  ? 9.630   -26.545 -15.887 1.00 33.48 ? 31  VAL B C   1 
ATOM   2510 O O   . VAL B 1 31  ? 8.783   -25.855 -16.461 1.00 33.46 ? 31  VAL B O   1 
ATOM   2511 C CB  . VAL B 1 31  ? 8.425   -27.988 -14.114 1.00 33.15 ? 31  VAL B CB  1 
ATOM   2512 C CG1 . VAL B 1 31  ? 7.017   -27.401 -13.969 1.00 33.42 ? 31  VAL B CG1 1 
ATOM   2513 C CG2 . VAL B 1 31  ? 8.467   -29.089 -15.175 1.00 33.23 ? 31  VAL B CG2 1 
ATOM   2514 N N   . THR B 1 32  ? 10.728  -27.022 -16.478 1.00 34.29 ? 32  THR B N   1 
ATOM   2515 C CA  . THR B 1 32  ? 11.073  -26.732 -17.866 1.00 35.00 ? 32  THR B CA  1 
ATOM   2516 C C   . THR B 1 32  ? 11.250  -28.031 -18.639 1.00 35.62 ? 32  THR B C   1 
ATOM   2517 O O   . THR B 1 32  ? 12.102  -28.857 -18.301 1.00 35.65 ? 32  THR B O   1 
ATOM   2518 C CB  . THR B 1 32  ? 12.377  -25.895 -17.958 1.00 34.91 ? 32  THR B CB  1 
ATOM   2519 O OG1 . THR B 1 32  ? 12.166  -24.617 -17.336 1.00 34.64 ? 32  THR B OG1 1 
ATOM   2520 C CG2 . THR B 1 32  ? 12.802  -25.682 -19.410 1.00 34.96 ? 32  THR B CG2 1 
ATOM   2521 N N   . LYS B 1 33  ? 10.434  -28.216 -19.670 1.00 36.44 ? 33  LYS B N   1 
ATOM   2522 C CA  . LYS B 1 33  ? 10.616  -29.340 -20.577 1.00 37.20 ? 33  LYS B CA  1 
ATOM   2523 C C   . LYS B 1 33  ? 11.094  -28.891 -21.954 1.00 37.58 ? 33  LYS B C   1 
ATOM   2524 O O   . LYS B 1 33  ? 10.662  -27.858 -22.471 1.00 37.81 ? 33  LYS B O   1 
ATOM   2525 C CB  . LYS B 1 33  ? 9.352   -30.203 -20.661 1.00 37.27 ? 33  LYS B CB  1 
ATOM   2526 C CG  . LYS B 1 33  ? 9.394   -31.399 -19.695 1.00 37.98 ? 33  LYS B CG  1 
ATOM   2527 C CD  . LYS B 1 33  ? 8.708   -31.086 -18.357 1.00 38.76 ? 33  LYS B CD  1 
ATOM   2528 C CE  . LYS B 1 33  ? 7.477   -31.996 -18.146 1.00 39.04 ? 33  LYS B CE  1 
ATOM   2529 N NZ  . LYS B 1 33  ? 6.398   -31.768 -19.161 1.00 39.51 ? 33  LYS B NZ  1 
ATOM   2530 N N   . LYS B 1 34  ? 12.013  -29.665 -22.523 1.00 37.97 ? 34  LYS B N   1 
ATOM   2531 C CA  . LYS B 1 34  ? 12.570  -29.378 -23.839 1.00 38.27 ? 34  LYS B CA  1 
ATOM   2532 C C   . LYS B 1 34  ? 12.607  -30.637 -24.694 1.00 38.42 ? 34  LYS B C   1 
ATOM   2533 O O   . LYS B 1 34  ? 13.073  -31.688 -24.247 1.00 38.47 ? 34  LYS B O   1 
ATOM   2534 C CB  . LYS B 1 34  ? 13.979  -28.794 -23.712 1.00 38.33 ? 34  LYS B CB  1 
ATOM   2535 C CG  . LYS B 1 34  ? 14.025  -27.372 -23.175 1.00 38.68 ? 34  LYS B CG  1 
ATOM   2536 C CD  . LYS B 1 34  ? 15.470  -26.908 -23.021 1.00 39.07 ? 34  LYS B CD  1 
ATOM   2537 C CE  . LYS B 1 34  ? 15.516  -25.475 -22.501 1.00 39.24 ? 34  LYS B CE  1 
ATOM   2538 N NZ  . LYS B 1 34  ? 16.919  -24.962 -22.511 1.00 39.59 ? 34  LYS B NZ  1 
ATOM   2539 N N   . PHE B 1 35  ? 12.108  -30.523 -25.924 1.00 38.55 ? 35  PHE B N   1 
ATOM   2540 C CA  . PHE B 1 35  ? 12.180  -31.617 -26.887 1.00 38.61 ? 35  PHE B CA  1 
ATOM   2541 C C   . PHE B 1 35  ? 13.554  -31.615 -27.558 1.00 38.61 ? 35  PHE B C   1 
ATOM   2542 O O   . PHE B 1 35  ? 14.356  -30.711 -27.321 1.00 38.62 ? 35  PHE B O   1 
ATOM   2543 C CB  . PHE B 1 35  ? 11.078  -31.471 -27.939 1.00 38.65 ? 35  PHE B CB  1 
ATOM   2544 C CG  . PHE B 1 35  ? 9.694   -31.353 -27.357 1.00 38.85 ? 35  PHE B CG  1 
ATOM   2545 C CD1 . PHE B 1 35  ? 9.082   -32.445 -26.743 1.00 39.25 ? 35  PHE B CD1 1 
ATOM   2546 C CD2 . PHE B 1 35  ? 8.992   -30.152 -27.444 1.00 39.31 ? 35  PHE B CD2 1 
ATOM   2547 C CE1 . PHE B 1 35  ? 7.795   -32.339 -26.210 1.00 39.82 ? 35  PHE B CE1 1 
ATOM   2548 C CE2 . PHE B 1 35  ? 7.703   -30.033 -26.918 1.00 39.92 ? 35  PHE B CE2 1 
ATOM   2549 C CZ  . PHE B 1 35  ? 7.103   -31.128 -26.299 1.00 40.12 ? 35  PHE B CZ  1 
ATOM   2550 N N   . SER B 1 36  ? 13.823  -32.626 -28.386 1.00 38.63 ? 36  SER B N   1 
ATOM   2551 C CA  . SER B 1 36  ? 15.071  -32.691 -29.160 1.00 38.80 ? 36  SER B CA  1 
ATOM   2552 C C   . SER B 1 36  ? 15.153  -31.510 -30.131 1.00 38.92 ? 36  SER B C   1 
ATOM   2553 O O   . SER B 1 36  ? 16.238  -31.090 -30.545 1.00 39.03 ? 36  SER B O   1 
ATOM   2554 C CB  . SER B 1 36  ? 15.171  -34.014 -29.921 1.00 38.71 ? 36  SER B CB  1 
ATOM   2555 N N   . ASN B 1 37  ? 13.976  -30.987 -30.467 1.00 38.90 ? 37  ASN B N   1 
ATOM   2556 C CA  . ASN B 1 37  ? 13.793  -29.777 -31.255 1.00 38.75 ? 37  ASN B CA  1 
ATOM   2557 C C   . ASN B 1 37  ? 14.337  -28.531 -30.553 1.00 38.52 ? 37  ASN B C   1 
ATOM   2558 O O   . ASN B 1 37  ? 14.482  -27.470 -31.166 1.00 38.52 ? 37  ASN B O   1 
ATOM   2559 C CB  . ASN B 1 37  ? 12.289  -29.595 -31.500 1.00 38.88 ? 37  ASN B CB  1 
ATOM   2560 C CG  . ASN B 1 37  ? 11.988  -28.800 -32.752 1.00 39.29 ? 37  ASN B CG  1 
ATOM   2561 O OD1 . ASN B 1 37  ? 12.868  -28.555 -33.577 1.00 40.00 ? 37  ASN B OD1 1 
ATOM   2562 N ND2 . ASN B 1 37  ? 10.731  -28.395 -32.904 1.00 39.63 ? 37  ASN B ND2 1 
ATOM   2563 N N   . GLN B 1 38  ? 14.639  -28.689 -29.263 1.00 38.23 ? 38  GLN B N   1 
ATOM   2564 C CA  . GLN B 1 38  ? 14.951  -27.587 -28.338 1.00 37.93 ? 38  GLN B CA  1 
ATOM   2565 C C   . GLN B 1 38  ? 13.769  -26.629 -28.130 1.00 37.56 ? 38  GLN B C   1 
ATOM   2566 O O   . GLN B 1 38  ? 13.930  -25.542 -27.554 1.00 37.43 ? 38  GLN B O   1 
ATOM   2567 C CB  . GLN B 1 38  ? 16.242  -26.851 -28.734 1.00 38.00 ? 38  GLN B CB  1 
ATOM   2568 C CG  . GLN B 1 38  ? 17.226  -26.685 -27.567 1.00 38.56 ? 38  GLN B CG  1 
ATOM   2569 C CD  . GLN B 1 38  ? 17.728  -28.028 -27.009 1.00 39.73 ? 38  GLN B CD  1 
ATOM   2570 O OE1 . GLN B 1 38  ? 18.079  -28.946 -27.764 1.00 40.40 ? 38  GLN B OE1 1 
ATOM   2571 N NE2 . GLN B 1 38  ? 17.765  -28.141 -25.680 1.00 40.27 ? 38  GLN B NE2 1 
ATOM   2572 N N   . GLU B 1 39  ? 12.590  -27.052 -28.599 1.00 37.20 ? 39  GLU B N   1 
ATOM   2573 C CA  . GLU B 1 39  ? 11.326  -26.383 -28.299 1.00 36.95 ? 39  GLU B CA  1 
ATOM   2574 C C   . GLU B 1 39  ? 11.137  -26.374 -26.789 1.00 36.82 ? 39  GLU B C   1 
ATOM   2575 O O   . GLU B 1 39  ? 11.242  -27.419 -26.139 1.00 36.61 ? 39  GLU B O   1 
ATOM   2576 C CB  . GLU B 1 39  ? 10.159  -27.098 -28.993 1.00 36.93 ? 39  GLU B CB  1 
ATOM   2577 C CG  . GLU B 1 39  ? 8.777   -26.494 -28.699 1.00 36.63 ? 39  GLU B CG  1 
ATOM   2578 C CD  . GLU B 1 39  ? 7.642   -27.199 -29.439 1.00 36.27 ? 39  GLU B CD  1 
ATOM   2579 O OE1 . GLU B 1 39  ? 6.470   -26.981 -29.058 1.00 35.91 ? 39  GLU B OE1 1 
ATOM   2580 O OE2 . GLU B 1 39  ? 7.911   -27.963 -30.398 1.00 36.13 ? 39  GLU B OE2 1 
ATOM   2581 N N   . THR B 1 40  ? 10.872  -25.191 -26.239 1.00 36.68 ? 40  THR B N   1 
ATOM   2582 C CA  . THR B 1 40  ? 10.900  -25.005 -24.794 1.00 36.59 ? 40  THR B CA  1 
ATOM   2583 C C   . THR B 1 40  ? 9.505   -24.870 -24.181 1.00 36.55 ? 40  THR B C   1 
ATOM   2584 O O   . THR B 1 40  ? 8.695   -24.042 -24.609 1.00 36.55 ? 40  THR B O   1 
ATOM   2585 C CB  . THR B 1 40  ? 11.804  -23.810 -24.412 1.00 36.60 ? 40  THR B CB  1 
ATOM   2586 O OG1 . THR B 1 40  ? 13.111  -24.020 -24.963 1.00 36.68 ? 40  THR B OG1 1 
ATOM   2587 C CG2 . THR B 1 40  ? 11.921  -23.667 -22.894 1.00 36.43 ? 40  THR B CG2 1 
ATOM   2588 N N   . CYS B 1 41  ? 9.240   -25.710 -23.184 1.00 36.35 ? 41  CYS B N   1 
ATOM   2589 C CA  . CYS B 1 41  ? 8.002   -25.661 -22.426 1.00 36.45 ? 41  CYS B CA  1 
ATOM   2590 C C   . CYS B 1 41  ? 8.284   -25.127 -21.031 1.00 35.90 ? 41  CYS B C   1 
ATOM   2591 O O   . CYS B 1 41  ? 9.260   -25.523 -20.395 1.00 35.96 ? 41  CYS B O   1 
ATOM   2592 C CB  . CYS B 1 41  ? 7.373   -27.053 -22.336 1.00 36.58 ? 41  CYS B CB  1 
ATOM   2593 S SG  . CYS B 1 41  ? 7.005   -27.810 -23.932 1.00 38.81 ? 41  CYS B SG  1 
ATOM   2594 N N   . VAL B 1 42  ? 7.430   -24.226 -20.561 1.00 35.37 ? 42  VAL B N   1 
ATOM   2595 C CA  . VAL B 1 42  ? 7.572   -23.649 -19.230 1.00 34.82 ? 42  VAL B CA  1 
ATOM   2596 C C   . VAL B 1 42  ? 6.259   -23.742 -18.459 1.00 34.48 ? 42  VAL B C   1 
ATOM   2597 O O   . VAL B 1 42  ? 5.179   -23.492 -19.000 1.00 34.69 ? 42  VAL B O   1 
ATOM   2598 C CB  . VAL B 1 42  ? 8.079   -22.178 -19.296 1.00 34.91 ? 42  VAL B CB  1 
ATOM   2599 C CG1 . VAL B 1 42  ? 7.868   -21.450 -17.972 1.00 34.99 ? 42  VAL B CG1 1 
ATOM   2600 C CG2 . VAL B 1 42  ? 9.555   -22.132 -19.692 1.00 34.88 ? 42  VAL B CG2 1 
ATOM   2601 N N   . GLU B 1 43  ? 6.363   -24.130 -17.195 1.00 33.85 ? 43  GLU B N   1 
ATOM   2602 C CA  . GLU B 1 43  ? 5.223   -24.141 -16.298 1.00 33.23 ? 43  GLU B CA  1 
ATOM   2603 C C   . GLU B 1 43  ? 5.668   -23.525 -14.976 1.00 32.45 ? 43  GLU B C   1 
ATOM   2604 O O   . GLU B 1 43  ? 6.447   -24.129 -14.233 1.00 32.41 ? 43  GLU B O   1 
ATOM   2605 C CB  . GLU B 1 43  ? 4.717   -25.571 -16.116 1.00 33.49 ? 43  GLU B CB  1 
ATOM   2606 C CG  . GLU B 1 43  ? 3.389   -25.704 -15.372 1.00 34.84 ? 43  GLU B CG  1 
ATOM   2607 C CD  . GLU B 1 43  ? 2.849   -27.126 -15.433 1.00 36.87 ? 43  GLU B CD  1 
ATOM   2608 O OE1 . GLU B 1 43  ? 2.630   -27.631 -16.564 1.00 37.87 ? 43  GLU B OE1 1 
ATOM   2609 O OE2 . GLU B 1 43  ? 2.637   -27.739 -14.354 1.00 37.31 ? 43  GLU B OE2 1 
ATOM   2610 N N   . ILE B 1 44  ? 5.193   -22.307 -14.713 1.00 31.37 ? 44  ILE B N   1 
ATOM   2611 C CA  . ILE B 1 44  ? 5.485   -21.592 -13.469 1.00 30.15 ? 44  ILE B CA  1 
ATOM   2612 C C   . ILE B 1 44  ? 4.857   -22.341 -12.296 1.00 29.30 ? 44  ILE B C   1 
ATOM   2613 O O   . ILE B 1 44  ? 3.634   -22.456 -12.199 1.00 29.01 ? 44  ILE B O   1 
ATOM   2614 C CB  . ILE B 1 44  ? 4.987   -20.116 -13.523 1.00 30.28 ? 44  ILE B CB  1 
ATOM   2615 C CG1 . ILE B 1 44  ? 5.625   -19.353 -14.699 1.00 30.39 ? 44  ILE B CG1 1 
ATOM   2616 C CG2 . ILE B 1 44  ? 5.245   -19.395 -12.203 1.00 30.13 ? 44  ILE B CG2 1 
ATOM   2617 C CD1 . ILE B 1 44  ? 7.162   -19.208 -14.641 1.00 30.57 ? 44  ILE B CD1 1 
ATOM   2618 N N   . GLY B 1 45  ? 5.713   -22.860 -11.420 1.00 28.44 ? 45  GLY B N   1 
ATOM   2619 C CA  . GLY B 1 45  ? 5.290   -23.759 -10.348 1.00 27.36 ? 45  GLY B CA  1 
ATOM   2620 C C   . GLY B 1 45  ? 4.538   -23.114 -9.200  1.00 26.61 ? 45  GLY B C   1 
ATOM   2621 O O   . GLY B 1 45  ? 4.043   -23.815 -8.319  1.00 26.65 ? 45  GLY B O   1 
ATOM   2622 N N   . GLU B 1 46  ? 4.454   -21.782 -9.207  1.00 25.74 ? 46  GLU B N   1 
ATOM   2623 C CA  . GLU B 1 46  ? 3.786   -21.040 -8.136  1.00 24.83 ? 46  GLU B CA  1 
ATOM   2624 C C   . GLU B 1 46  ? 3.122   -19.763 -8.640  1.00 23.99 ? 46  GLU B C   1 
ATOM   2625 O O   . GLU B 1 46  ? 3.530   -19.196 -9.650  1.00 23.81 ? 46  GLU B O   1 
ATOM   2626 C CB  . GLU B 1 46  ? 4.762   -20.724 -6.989  1.00 24.94 ? 46  GLU B CB  1 
ATOM   2627 C CG  . GLU B 1 46  ? 5.821   -19.640 -7.314  1.00 25.38 ? 46  GLU B CG  1 
ATOM   2628 C CD  . GLU B 1 46  ? 7.015   -19.731 -6.375  1.00 26.25 ? 46  GLU B CD  1 
ATOM   2629 O OE1 . GLU B 1 46  ? 7.238   -18.769 -5.602  1.00 26.41 ? 46  GLU B OE1 1 
ATOM   2630 O OE2 . GLU B 1 46  ? 7.728   -20.764 -6.406  1.00 26.54 ? 46  GLU B OE2 1 
ATOM   2631 N N   . SER B 1 47  ? 2.103   -19.319 -7.913  1.00 23.09 ? 47  SER B N   1 
ATOM   2632 C CA  . SER B 1 47  ? 1.348   -18.123 -8.253  1.00 22.18 ? 47  SER B CA  1 
ATOM   2633 C C   . SER B 1 47  ? 2.205   -16.859 -8.195  1.00 22.21 ? 47  SER B C   1 
ATOM   2634 O O   . SER B 1 47  ? 2.959   -16.648 -7.239  1.00 22.13 ? 47  SER B O   1 
ATOM   2635 C CB  . SER B 1 47  ? 0.143   -17.991 -7.324  1.00 21.82 ? 47  SER B CB  1 
ATOM   2636 O OG  . SER B 1 47  ? -0.505  -16.752 -7.506  1.00 20.15 ? 47  SER B OG  1 
ATOM   2637 N N   . VAL B 1 48  ? 2.085   -16.033 -9.233  1.00 22.03 ? 48  VAL B N   1 
ATOM   2638 C CA  . VAL B 1 48  ? 2.768   -14.741 -9.301  1.00 21.78 ? 48  VAL B CA  1 
ATOM   2639 C C   . VAL B 1 48  ? 1.766   -13.585 -9.403  1.00 21.99 ? 48  VAL B C   1 
ATOM   2640 O O   . VAL B 1 48  ? 2.157   -12.425 -9.589  1.00 22.11 ? 48  VAL B O   1 
ATOM   2641 C CB  . VAL B 1 48  ? 3.780   -14.677 -10.480 1.00 21.75 ? 48  VAL B CB  1 
ATOM   2642 C CG1 . VAL B 1 48  ? 4.870   -15.734 -10.317 1.00 21.31 ? 48  VAL B CG1 1 
ATOM   2643 C CG2 . VAL B 1 48  ? 3.076   -14.823 -11.833 1.00 21.55 ? 48  VAL B CG2 1 
ATOM   2644 N N   . ARG B 1 49  ? 0.475   -13.906 -9.283  1.00 22.16 ? 49  ARG B N   1 
ATOM   2645 C CA  . ARG B 1 49  ? -0.593  -12.901 -9.313  1.00 22.16 ? 49  ARG B CA  1 
ATOM   2646 C C   . ARG B 1 49  ? -0.288  -11.743 -8.362  1.00 22.37 ? 49  ARG B C   1 
ATOM   2647 O O   . ARG B 1 49  ? 0.036   -11.962 -7.195  1.00 22.24 ? 49  ARG B O   1 
ATOM   2648 C CB  . ARG B 1 49  ? -1.936  -13.544 -8.958  1.00 22.00 ? 49  ARG B CB  1 
ATOM   2649 C CG  . ARG B 1 49  ? -3.150  -12.727 -9.387  1.00 21.97 ? 49  ARG B CG  1 
ATOM   2650 C CD  . ARG B 1 49  ? -4.455  -13.504 -9.227  1.00 21.89 ? 49  ARG B CD  1 
ATOM   2651 N NE  . ARG B 1 49  ? -4.505  -14.705 -10.066 1.00 21.56 ? 49  ARG B NE  1 
ATOM   2652 C CZ  . ARG B 1 49  ? -5.121  -14.781 -11.243 1.00 20.60 ? 49  ARG B CZ  1 
ATOM   2653 N NH1 . ARG B 1 49  ? -5.750  -13.727 -11.740 1.00 20.44 ? 49  ARG B NH1 1 
ATOM   2654 N NH2 . ARG B 1 49  ? -5.107  -15.915 -11.923 1.00 19.96 ? 49  ARG B NH2 1 
ATOM   2655 N N   . GLY B 1 50  ? -0.358  -10.519 -8.882  1.00 22.86 ? 50  GLY B N   1 
ATOM   2656 C CA  . GLY B 1 50  ? -0.144  -9.306  -8.090  1.00 23.40 ? 50  GLY B CA  1 
ATOM   2657 C C   . GLY B 1 50  ? 1.285   -9.057  -7.632  1.00 24.04 ? 50  GLY B C   1 
ATOM   2658 O O   . GLY B 1 50  ? 1.552   -8.078  -6.929  1.00 24.13 ? 50  GLY B O   1 
ATOM   2659 N N   . GLU B 1 51  ? 2.212   -9.920  -8.042  1.00 24.53 ? 51  GLU B N   1 
ATOM   2660 C CA  . GLU B 1 51  ? 3.597   -9.828  -7.572  1.00 24.96 ? 51  GLU B CA  1 
ATOM   2661 C C   . GLU B 1 51  ? 4.567   -9.158  -8.537  1.00 24.82 ? 51  GLU B C   1 
ATOM   2662 O O   . GLU B 1 51  ? 4.290   -9.023  -9.730  1.00 24.90 ? 51  GLU B O   1 
ATOM   2663 C CB  . GLU B 1 51  ? 4.120   -11.205 -7.172  1.00 25.26 ? 51  GLU B CB  1 
ATOM   2664 C CG  . GLU B 1 51  ? 3.631   -11.640 -5.814  1.00 26.66 ? 51  GLU B CG  1 
ATOM   2665 C CD  . GLU B 1 51  ? 3.341   -13.113 -5.760  1.00 28.92 ? 51  GLU B CD  1 
ATOM   2666 O OE1 . GLU B 1 51  ? 4.278   -13.912 -5.977  1.00 29.97 ? 51  GLU B OE1 1 
ATOM   2667 O OE2 . GLU B 1 51  ? 2.170   -13.467 -5.500  1.00 29.78 ? 51  GLU B OE2 1 
ATOM   2668 N N   . ASP B 1 52  ? 5.706   -8.746  -7.982  1.00 24.69 ? 52  ASP B N   1 
ATOM   2669 C CA  . ASP B 1 52  ? 6.760   -8.046  -8.698  1.00 24.57 ? 52  ASP B CA  1 
ATOM   2670 C C   . ASP B 1 52  ? 7.817   -9.063  -9.127  1.00 24.35 ? 52  ASP B C   1 
ATOM   2671 O O   . ASP B 1 52  ? 8.727   -9.402  -8.357  1.00 24.42 ? 52  ASP B O   1 
ATOM   2672 C CB  . ASP B 1 52  ? 7.369   -6.986  -7.776  1.00 24.69 ? 52  ASP B CB  1 
ATOM   2673 C CG  . ASP B 1 52  ? 8.220   -5.978  -8.514  1.00 25.35 ? 52  ASP B CG  1 
ATOM   2674 O OD1 . ASP B 1 52  ? 9.054   -5.322  -7.850  1.00 25.72 ? 52  ASP B OD1 1 
ATOM   2675 O OD2 . ASP B 1 52  ? 8.059   -5.828  -9.744  1.00 26.13 ? 52  ASP B OD2 1 
ATOM   2676 N N   . VAL B 1 53  ? 7.687   -9.548  -10.361 1.00 23.92 ? 53  VAL B N   1 
ATOM   2677 C CA  . VAL B 1 53  ? 8.457   -10.697 -10.840 1.00 23.40 ? 53  VAL B CA  1 
ATOM   2678 C C   . VAL B 1 53  ? 9.746   -10.292 -11.553 1.00 23.39 ? 53  VAL B C   1 
ATOM   2679 O O   . VAL B 1 53  ? 9.747   -9.394  -12.403 1.00 23.20 ? 53  VAL B O   1 
ATOM   2680 C CB  . VAL B 1 53  ? 7.580   -11.601 -11.746 1.00 23.23 ? 53  VAL B CB  1 
ATOM   2681 C CG1 . VAL B 1 53  ? 8.401   -12.729 -12.389 1.00 22.82 ? 53  VAL B CG1 1 
ATOM   2682 C CG2 . VAL B 1 53  ? 6.431   -12.174 -10.939 1.00 22.79 ? 53  VAL B CG2 1 
ATOM   2683 N N   . TYR B 1 54  ? 10.837  -10.969 -11.189 1.00 23.38 ? 54  TYR B N   1 
ATOM   2684 C CA  . TYR B 1 54  ? 12.150  -10.752 -11.796 1.00 23.27 ? 54  TYR B CA  1 
ATOM   2685 C C   . TYR B 1 54  ? 12.666  -12.052 -12.401 1.00 23.60 ? 54  TYR B C   1 
ATOM   2686 O O   . TYR B 1 54  ? 12.822  -13.055 -11.708 1.00 23.58 ? 54  TYR B O   1 
ATOM   2687 C CB  . TYR B 1 54  ? 13.136  -10.187 -10.764 1.00 22.93 ? 54  TYR B CB  1 
ATOM   2688 C CG  . TYR B 1 54  ? 12.743  -8.810  -10.275 1.00 22.16 ? 54  TYR B CG  1 
ATOM   2689 C CD1 . TYR B 1 54  ? 11.757  -8.651  -9.302  1.00 21.14 ? 54  TYR B CD1 1 
ATOM   2690 C CD2 . TYR B 1 54  ? 13.338  -7.665  -10.802 1.00 21.37 ? 54  TYR B CD2 1 
ATOM   2691 C CE1 . TYR B 1 54  ? 11.378  -7.396  -8.864  1.00 20.62 ? 54  TYR B CE1 1 
ATOM   2692 C CE2 . TYR B 1 54  ? 12.963  -6.400  -10.366 1.00 20.13 ? 54  TYR B CE2 1 
ATOM   2693 C CZ  . TYR B 1 54  ? 11.985  -6.275  -9.397  1.00 20.05 ? 54  TYR B CZ  1 
ATOM   2694 O OH  . TYR B 1 54  ? 11.602  -5.030  -8.953  1.00 19.55 ? 54  TYR B OH  1 
ATOM   2695 N N   . ILE B 1 55  ? 12.904  -12.032 -13.708 1.00 24.13 ? 55  ILE B N   1 
ATOM   2696 C CA  . ILE B 1 55  ? 13.409  -13.201 -14.414 1.00 24.63 ? 55  ILE B CA  1 
ATOM   2697 C C   . ILE B 1 55  ? 14.847  -12.958 -14.849 1.00 25.23 ? 55  ILE B C   1 
ATOM   2698 O O   . ILE B 1 55  ? 15.122  -12.080 -15.674 1.00 25.24 ? 55  ILE B O   1 
ATOM   2699 C CB  . ILE B 1 55  ? 12.527  -13.560 -15.633 1.00 24.52 ? 55  ILE B CB  1 
ATOM   2700 C CG1 . ILE B 1 55  ? 11.059  -13.688 -15.201 1.00 24.06 ? 55  ILE B CG1 1 
ATOM   2701 C CG2 . ILE B 1 55  ? 13.037  -14.848 -16.297 1.00 24.11 ? 55  ILE B CG2 1 
ATOM   2702 C CD1 . ILE B 1 55  ? 10.070  -13.727 -16.342 1.00 23.67 ? 55  ILE B CD1 1 
ATOM   2703 N N   . VAL B 1 56  ? 15.759  -13.737 -14.278 1.00 26.07 ? 56  VAL B N   1 
ATOM   2704 C CA  . VAL B 1 56  ? 17.182  -13.588 -14.553 1.00 27.02 ? 56  VAL B CA  1 
ATOM   2705 C C   . VAL B 1 56  ? 17.612  -14.538 -15.666 1.00 27.97 ? 56  VAL B C   1 
ATOM   2706 O O   . VAL B 1 56  ? 17.361  -15.748 -15.609 1.00 27.93 ? 56  VAL B O   1 
ATOM   2707 C CB  . VAL B 1 56  ? 18.044  -13.814 -13.287 1.00 26.85 ? 56  VAL B CB  1 
ATOM   2708 C CG1 . VAL B 1 56  ? 19.504  -13.464 -13.557 1.00 26.58 ? 56  VAL B CG1 1 
ATOM   2709 C CG2 . VAL B 1 56  ? 17.509  -12.993 -12.116 1.00 26.79 ? 56  VAL B CG2 1 
ATOM   2710 N N   . GLN B 1 57  ? 18.249  -13.969 -16.684 1.00 29.28 ? 57  GLN B N   1 
ATOM   2711 C CA  . GLN B 1 57  ? 18.774  -14.745 -17.792 1.00 30.64 ? 57  GLN B CA  1 
ATOM   2712 C C   . GLN B 1 57  ? 20.296  -14.671 -17.847 1.00 31.40 ? 57  GLN B C   1 
ATOM   2713 O O   . GLN B 1 57  ? 20.878  -13.614 -18.121 1.00 31.63 ? 57  GLN B O   1 
ATOM   2714 C CB  . GLN B 1 57  ? 18.153  -14.307 -19.122 1.00 30.67 ? 57  GLN B CB  1 
ATOM   2715 C CG  . GLN B 1 57  ? 18.398  -15.272 -20.278 1.00 32.03 ? 57  GLN B CG  1 
ATOM   2716 C CD  . GLN B 1 57  ? 18.143  -16.731 -19.902 1.00 33.82 ? 57  GLN B CD  1 
ATOM   2717 O OE1 . GLN B 1 57  ? 18.953  -17.356 -19.209 1.00 34.63 ? 57  GLN B OE1 1 
ATOM   2718 N NE2 . GLN B 1 57  ? 17.022  -17.281 -20.369 1.00 34.03 ? 57  GLN B NE2 1 
ATOM   2719 N N   . SER B 1 58  ? 20.927  -15.806 -17.563 1.00 32.21 ? 58  SER B N   1 
ATOM   2720 C CA  . SER B 1 58  ? 22.369  -15.956 -17.687 1.00 33.02 ? 58  SER B CA  1 
ATOM   2721 C C   . SER B 1 58  ? 22.643  -17.075 -18.690 1.00 33.49 ? 58  SER B C   1 
ATOM   2722 O O   . SER B 1 58  ? 21.860  -18.024 -18.799 1.00 33.71 ? 58  SER B O   1 
ATOM   2723 C CB  . SER B 1 58  ? 22.984  -16.277 -16.319 1.00 33.07 ? 58  SER B CB  1 
ATOM   2724 O OG  . SER B 1 58  ? 24.411  -16.354 -16.383 1.00 33.65 ? 58  SER B OG  1 
ATOM   2725 N N   . GLY B 1 59  ? 23.738  -16.959 -19.435 1.00 33.93 ? 59  GLY B N   1 
ATOM   2726 C CA  . GLY B 1 59  ? 24.118  -18.017 -20.371 1.00 34.33 ? 59  GLY B CA  1 
ATOM   2727 C C   . GLY B 1 59  ? 25.013  -17.570 -21.506 1.00 34.60 ? 59  GLY B C   1 
ATOM   2728 O O   . GLY B 1 59  ? 26.241  -17.616 -21.390 1.00 34.80 ? 59  GLY B O   1 
ATOM   2729 N N   . CYS B 1 60  ? 24.384  -17.142 -22.603 1.00 34.60 ? 60  CYS B N   1 
ATOM   2730 C CA  . CYS B 1 60  ? 25.077  -16.751 -23.839 1.00 34.66 ? 60  CYS B CA  1 
ATOM   2731 C C   . CYS B 1 60  ? 25.953  -17.865 -24.434 1.00 34.25 ? 60  CYS B C   1 
ATOM   2732 O O   . CYS B 1 60  ? 27.061  -17.612 -24.918 1.00 34.46 ? 60  CYS B O   1 
ATOM   2733 C CB  . CYS B 1 60  ? 25.880  -15.460 -23.645 1.00 34.82 ? 60  CYS B CB  1 
ATOM   2734 S SG  . CYS B 1 60  ? 26.291  -14.631 -25.187 1.00 36.33 ? 60  CYS B SG  1 
ATOM   2735 N N   . GLY B 1 61  ? 25.442  -19.096 -24.386 1.00 33.66 ? 61  GLY B N   1 
ATOM   2736 C CA  . GLY B 1 61  ? 26.096  -20.253 -25.007 1.00 32.71 ? 61  GLY B CA  1 
ATOM   2737 C C   . GLY B 1 61  ? 25.301  -20.690 -26.235 1.00 32.11 ? 61  GLY B C   1 
ATOM   2738 O O   . GLY B 1 61  ? 25.872  -20.995 -27.299 1.00 32.33 ? 61  GLY B O   1 
ATOM   2739 N N   . GLU B 1 62  ? 23.979  -20.745 -26.072 1.00 31.17 ? 62  GLU B N   1 
ATOM   2740 C CA  . GLU B 1 62  ? 23.064  -20.876 -27.196 1.00 30.11 ? 62  GLU B CA  1 
ATOM   2741 C C   . GLU B 1 62  ? 22.064  -19.743 -27.071 1.00 29.33 ? 62  GLU B C   1 
ATOM   2742 O O   . GLU B 1 62  ? 21.052  -19.859 -26.382 1.00 29.33 ? 62  GLU B O   1 
ATOM   2743 C CB  . GLU B 1 62  ? 22.356  -22.232 -27.199 1.00 30.11 ? 62  GLU B CB  1 
ATOM   2744 C CG  . GLU B 1 62  ? 22.270  -22.896 -28.583 1.00 30.30 ? 62  GLU B CG  1 
ATOM   2745 C CD  . GLU B 1 62  ? 21.408  -22.137 -29.604 1.00 30.66 ? 62  GLU B CD  1 
ATOM   2746 O OE1 . GLU B 1 62  ? 21.473  -22.494 -30.799 1.00 29.33 ? 62  GLU B OE1 1 
ATOM   2747 O OE2 . GLU B 1 62  ? 20.662  -21.203 -29.232 1.00 31.72 ? 62  GLU B OE2 1 
ATOM   2748 N N   . ILE B 1 63  ? 22.368  -18.648 -27.757 1.00 28.36 ? 63  ILE B N   1 
ATOM   2749 C CA  . ILE B 1 63  ? 21.683  -17.368 -27.588 1.00 27.35 ? 63  ILE B CA  1 
ATOM   2750 C C   . ILE B 1 63  ? 20.185  -17.394 -27.957 1.00 26.88 ? 63  ILE B C   1 
ATOM   2751 O O   . ILE B 1 63  ? 19.372  -16.740 -27.303 1.00 26.86 ? 63  ILE B O   1 
ATOM   2752 C CB  . ILE B 1 63  ? 22.460  -16.248 -28.337 1.00 27.20 ? 63  ILE B CB  1 
ATOM   2753 C CG1 . ILE B 1 63  ? 21.927  -14.860 -27.982 1.00 27.21 ? 63  ILE B CG1 1 
ATOM   2754 C CG2 . ILE B 1 63  ? 22.469  -16.495 -29.845 1.00 26.90 ? 63  ILE B CG2 1 
ATOM   2755 C CD1 . ILE B 1 63  ? 22.803  -13.724 -28.508 1.00 27.21 ? 63  ILE B CD1 1 
ATOM   2756 N N   . ASN B 1 64  ? 19.827  -18.168 -28.979 1.00 26.25 ? 64  ASN B N   1 
ATOM   2757 C CA  . ASN B 1 64  ? 18.438  -18.249 -29.432 1.00 25.66 ? 64  ASN B CA  1 
ATOM   2758 C C   . ASN B 1 64  ? 17.546  -19.084 -28.512 1.00 25.68 ? 64  ASN B C   1 
ATOM   2759 O O   . ASN B 1 64  ? 16.402  -18.708 -28.248 1.00 25.64 ? 64  ASN B O   1 
ATOM   2760 C CB  . ASN B 1 64  ? 18.371  -18.753 -30.876 1.00 25.43 ? 64  ASN B CB  1 
ATOM   2761 C CG  . ASN B 1 64  ? 19.177  -17.893 -31.822 1.00 24.00 ? 64  ASN B CG  1 
ATOM   2762 O OD1 . ASN B 1 64  ? 19.022  -16.676 -31.852 1.00 22.71 ? 64  ASN B OD1 1 
ATOM   2763 N ND2 . ASN B 1 64  ? 20.059  -18.519 -32.589 1.00 23.11 ? 64  ASN B ND2 1 
ATOM   2764 N N   . ASP B 1 65  ? 18.069  -20.212 -28.032 1.00 25.60 ? 65  ASP B N   1 
ATOM   2765 C CA  . ASP B 1 65  ? 17.389  -20.985 -26.991 1.00 25.57 ? 65  ASP B CA  1 
ATOM   2766 C C   . ASP B 1 65  ? 17.199  -20.134 -25.739 1.00 25.44 ? 65  ASP B C   1 
ATOM   2767 O O   . ASP B 1 65  ? 16.094  -20.059 -25.199 1.00 25.46 ? 65  ASP B O   1 
ATOM   2768 C CB  . ASP B 1 65  ? 18.166  -22.261 -26.648 1.00 25.57 ? 65  ASP B CB  1 
ATOM   2769 C CG  . ASP B 1 65  ? 18.307  -23.192 -27.831 1.00 25.85 ? 65  ASP B CG  1 
ATOM   2770 O OD1 . ASP B 1 65  ? 17.434  -23.177 -28.721 1.00 26.29 ? 65  ASP B OD1 1 
ATOM   2771 O OD2 . ASP B 1 65  ? 19.295  -23.952 -27.868 1.00 26.46 ? 65  ASP B OD2 1 
ATOM   2772 N N   . ASN B 1 66  ? 18.275  -19.482 -25.301 1.00 25.22 ? 66  ASN B N   1 
ATOM   2773 C CA  . ASN B 1 66  ? 18.235  -18.615 -24.120 1.00 25.26 ? 66  ASN B CA  1 
ATOM   2774 C C   . ASN B 1 66  ? 17.285  -17.434 -24.253 1.00 24.89 ? 66  ASN B C   1 
ATOM   2775 O O   . ASN B 1 66  ? 16.574  -17.094 -23.300 1.00 24.85 ? 66  ASN B O   1 
ATOM   2776 C CB  . ASN B 1 66  ? 19.646  -18.139 -23.745 1.00 25.39 ? 66  ASN B CB  1 
ATOM   2777 C CG  . ASN B 1 66  ? 20.503  -19.257 -23.181 1.00 26.20 ? 66  ASN B CG  1 
ATOM   2778 O OD1 . ASN B 1 66  ? 20.042  -20.062 -22.357 1.00 27.92 ? 66  ASN B OD1 1 
ATOM   2779 N ND2 . ASN B 1 66  ? 21.756  -19.319 -23.622 1.00 27.35 ? 66  ASN B ND2 1 
ATOM   2780 N N   . LEU B 1 67  ? 17.269  -16.820 -25.433 1.00 24.51 ? 67  LEU B N   1 
ATOM   2781 C CA  . LEU B 1 67  ? 16.387  -15.685 -25.689 1.00 24.10 ? 67  LEU B CA  1 
ATOM   2782 C C   . LEU B 1 67  ? 14.929  -16.124 -25.675 1.00 23.68 ? 67  LEU B C   1 
ATOM   2783 O O   . LEU B 1 67  ? 14.096  -15.473 -25.050 1.00 23.58 ? 67  LEU B O   1 
ATOM   2784 C CB  . LEU B 1 67  ? 16.746  -14.994 -27.010 1.00 24.18 ? 67  LEU B CB  1 
ATOM   2785 C CG  . LEU B 1 67  ? 16.178  -13.615 -27.392 1.00 24.36 ? 67  LEU B CG  1 
ATOM   2786 C CD1 . LEU B 1 67  ? 15.071  -13.764 -28.400 1.00 24.75 ? 67  LEU B CD1 1 
ATOM   2787 C CD2 . LEU B 1 67  ? 15.714  -12.775 -26.189 1.00 24.67 ? 67  LEU B CD2 1 
ATOM   2788 N N   . MET B 1 68  ? 14.632  -17.240 -26.340 1.00 23.34 ? 68  MET B N   1 
ATOM   2789 C CA  . MET B 1 68  ? 13.267  -17.766 -26.383 1.00 23.25 ? 68  MET B CA  1 
ATOM   2790 C C   . MET B 1 68  ? 12.755  -18.216 -25.018 1.00 22.91 ? 68  MET B C   1 
ATOM   2791 O O   . MET B 1 68  ? 11.593  -17.984 -24.686 1.00 22.89 ? 68  MET B O   1 
ATOM   2792 C CB  . MET B 1 68  ? 13.145  -18.904 -27.403 1.00 23.34 ? 68  MET B CB  1 
ATOM   2793 C CG  . MET B 1 68  ? 12.862  -18.426 -28.824 1.00 24.45 ? 68  MET B CG  1 
ATOM   2794 S SD  . MET B 1 68  ? 11.346  -17.431 -28.956 1.00 27.39 ? 68  MET B SD  1 
ATOM   2795 C CE  . MET B 1 68  ? 10.095  -18.599 -28.380 1.00 26.30 ? 68  MET B CE  1 
ATOM   2796 N N   . GLU B 1 69  ? 13.624  -18.857 -24.240 1.00 22.68 ? 69  GLU B N   1 
ATOM   2797 C CA  . GLU B 1 69  ? 13.295  -19.296 -22.886 1.00 22.69 ? 69  GLU B CA  1 
ATOM   2798 C C   . GLU B 1 69  ? 12.875  -18.100 -22.026 1.00 22.40 ? 69  GLU B C   1 
ATOM   2799 O O   . GLU B 1 69  ? 11.849  -18.144 -21.331 1.00 22.38 ? 69  GLU B O   1 
ATOM   2800 C CB  . GLU B 1 69  ? 14.488  -20.028 -22.264 1.00 22.87 ? 69  GLU B CB  1 
ATOM   2801 C CG  . GLU B 1 69  ? 14.150  -20.870 -21.031 1.00 23.68 ? 69  GLU B CG  1 
ATOM   2802 C CD  . GLU B 1 69  ? 15.366  -21.572 -20.429 1.00 24.99 ? 69  GLU B CD  1 
ATOM   2803 O OE1 . GLU B 1 69  ? 16.432  -21.634 -21.084 1.00 26.00 ? 69  GLU B OE1 1 
ATOM   2804 O OE2 . GLU B 1 69  ? 15.256  -22.064 -19.287 1.00 25.35 ? 69  GLU B OE2 1 
ATOM   2805 N N   . LEU B 1 70  ? 13.666  -17.031 -22.093 1.00 22.10 ? 70  LEU B N   1 
ATOM   2806 C CA  . LEU B 1 70  ? 13.343  -15.785 -21.418 1.00 21.78 ? 70  LEU B CA  1 
ATOM   2807 C C   . LEU B 1 70  ? 11.996  -15.242 -21.885 1.00 21.78 ? 70  LEU B C   1 
ATOM   2808 O O   . LEU B 1 70  ? 11.115  -14.958 -21.063 1.00 21.99 ? 70  LEU B O   1 
ATOM   2809 C CB  . LEU B 1 70  ? 14.443  -14.745 -21.668 1.00 21.77 ? 70  LEU B CB  1 
ATOM   2810 C CG  . LEU B 1 70  ? 14.267  -13.353 -21.051 1.00 21.43 ? 70  LEU B CG  1 
ATOM   2811 C CD1 . LEU B 1 70  ? 13.920  -13.425 -19.570 1.00 20.17 ? 70  LEU B CD1 1 
ATOM   2812 C CD2 . LEU B 1 70  ? 15.531  -12.541 -21.256 1.00 21.98 ? 70  LEU B CD2 1 
ATOM   2813 N N   . LEU B 1 71  ? 11.841  -15.100 -23.200 1.00 21.46 ? 71  LEU B N   1 
ATOM   2814 C CA  . LEU B 1 71  ? 10.613  -14.555 -23.770 1.00 21.25 ? 71  LEU B CA  1 
ATOM   2815 C C   . LEU B 1 71  ? 9.384   -15.365 -23.372 1.00 21.12 ? 71  LEU B C   1 
ATOM   2816 O O   . LEU B 1 71  ? 8.335   -14.791 -23.082 1.00 20.97 ? 71  LEU B O   1 
ATOM   2817 C CB  . LEU B 1 71  ? 10.709  -14.455 -25.293 1.00 21.21 ? 71  LEU B CB  1 
ATOM   2818 C CG  . LEU B 1 71  ? 11.691  -13.455 -25.903 1.00 21.20 ? 71  LEU B CG  1 
ATOM   2819 C CD1 . LEU B 1 71  ? 11.646  -13.583 -27.417 1.00 20.90 ? 71  LEU B CD1 1 
ATOM   2820 C CD2 . LEU B 1 71  ? 11.385  -12.024 -25.472 1.00 21.38 ? 71  LEU B CD2 1 
ATOM   2821 N N   . ILE B 1 72  ? 9.523   -16.691 -23.349 1.00 21.00 ? 72  ILE B N   1 
ATOM   2822 C CA  . ILE B 1 72  ? 8.428   -17.574 -22.944 1.00 21.11 ? 72  ILE B CA  1 
ATOM   2823 C C   . ILE B 1 72  ? 8.073   -17.368 -21.465 1.00 21.41 ? 72  ILE B C   1 
ATOM   2824 O O   . ILE B 1 72  ? 6.894   -17.268 -21.115 1.00 21.48 ? 72  ILE B O   1 
ATOM   2825 C CB  . ILE B 1 72  ? 8.738   -19.068 -23.268 1.00 21.08 ? 72  ILE B CB  1 
ATOM   2826 C CG1 . ILE B 1 72  ? 8.579   -19.334 -24.763 1.00 20.57 ? 72  ILE B CG1 1 
ATOM   2827 C CG2 . ILE B 1 72  ? 7.816   -20.016 -22.512 1.00 21.03 ? 72  ILE B CG2 1 
ATOM   2828 C CD1 . ILE B 1 72  ? 9.174   -20.647 -25.211 1.00 20.84 ? 72  ILE B CD1 1 
ATOM   2829 N N   . MET B 1 73  ? 9.091   -17.282 -20.610 1.00 21.76 ? 73  MET B N   1 
ATOM   2830 C CA  . MET B 1 73  ? 8.875   -17.080 -19.176 1.00 22.22 ? 73  MET B CA  1 
ATOM   2831 C C   . MET B 1 73  ? 8.181   -15.758 -18.878 1.00 22.20 ? 73  MET B C   1 
ATOM   2832 O O   . MET B 1 73  ? 7.228   -15.719 -18.090 1.00 21.99 ? 73  MET B O   1 
ATOM   2833 C CB  . MET B 1 73  ? 10.190  -17.151 -18.405 1.00 22.49 ? 73  MET B CB  1 
ATOM   2834 C CG  . MET B 1 73  ? 10.756  -18.547 -18.308 1.00 24.30 ? 73  MET B CG  1 
ATOM   2835 S SD  . MET B 1 73  ? 12.078  -18.615 -17.094 1.00 29.31 ? 73  MET B SD  1 
ATOM   2836 C CE  . MET B 1 73  ? 11.111  -18.621 -15.584 1.00 28.60 ? 73  MET B CE  1 
ATOM   2837 N N   . ILE B 1 74  ? 8.670   -14.681 -19.502 1.00 22.25 ? 74  ILE B N   1 
ATOM   2838 C CA  . ILE B 1 74  ? 8.055   -13.356 -19.369 1.00 22.27 ? 74  ILE B CA  1 
ATOM   2839 C C   . ILE B 1 74  ? 6.566   -13.469 -19.661 1.00 22.34 ? 74  ILE B C   1 
ATOM   2840 O O   . ILE B 1 74  ? 5.737   -13.021 -18.871 1.00 22.39 ? 74  ILE B O   1 
ATOM   2841 C CB  . ILE B 1 74  ? 8.712   -12.320 -20.329 1.00 22.33 ? 74  ILE B CB  1 
ATOM   2842 C CG1 . ILE B 1 74  ? 10.152  -12.010 -19.896 1.00 22.69 ? 74  ILE B CG1 1 
ATOM   2843 C CG2 . ILE B 1 74  ? 7.891   -11.028 -20.397 1.00 21.99 ? 74  ILE B CG2 1 
ATOM   2844 C CD1 . ILE B 1 74  ? 10.996  -11.375 -21.010 1.00 22.15 ? 74  ILE B CD1 1 
ATOM   2845 N N   . ASN B 1 75  ? 6.250   -14.097 -20.792 1.00 22.45 ? 75  ASN B N   1 
ATOM   2846 C CA  . ASN B 1 75  ? 4.884   -14.282 -21.254 1.00 22.69 ? 75  ASN B CA  1 
ATOM   2847 C C   . ASN B 1 75  ? 4.009   -15.068 -20.274 1.00 22.60 ? 75  ASN B C   1 
ATOM   2848 O O   . ASN B 1 75  ? 2.907   -14.629 -19.938 1.00 22.42 ? 75  ASN B O   1 
ATOM   2849 C CB  . ASN B 1 75  ? 4.888   -14.963 -22.628 1.00 22.89 ? 75  ASN B CB  1 
ATOM   2850 C CG  . ASN B 1 75  ? 3.546   -14.867 -23.327 1.00 23.49 ? 75  ASN B CG  1 
ATOM   2851 O OD1 . ASN B 1 75  ? 2.871   -15.878 -23.549 1.00 23.88 ? 75  ASN B OD1 1 
ATOM   2852 N ND2 . ASN B 1 75  ? 3.142   -13.642 -23.661 1.00 23.58 ? 75  ASN B ND2 1 
ATOM   2853 N N   . ALA B 1 76  ? 4.505   -16.228 -19.833 1.00 22.63 ? 76  ALA B N   1 
ATOM   2854 C CA  . ALA B 1 76  ? 3.845   -17.065 -18.822 1.00 22.66 ? 76  ALA B CA  1 
ATOM   2855 C C   . ALA B 1 76  ? 3.467   -16.278 -17.575 1.00 22.86 ? 76  ALA B C   1 
ATOM   2856 O O   . ALA B 1 76  ? 2.355   -16.426 -17.054 1.00 22.94 ? 76  ALA B O   1 
ATOM   2857 C CB  . ALA B 1 76  ? 4.743   -18.232 -18.440 1.00 22.57 ? 76  ALA B CB  1 
ATOM   2858 N N   . CYS B 1 77  ? 4.402   -15.445 -17.112 1.00 22.95 ? 77  CYS B N   1 
ATOM   2859 C CA  . CYS B 1 77  ? 4.213   -14.613 -15.928 1.00 23.04 ? 77  CYS B CA  1 
ATOM   2860 C C   . CYS B 1 77  ? 3.235   -13.469 -16.173 1.00 23.35 ? 77  CYS B C   1 
ATOM   2861 O O   . CYS B 1 77  ? 2.400   -13.175 -15.317 1.00 23.25 ? 77  CYS B O   1 
ATOM   2862 C CB  . CYS B 1 77  ? 5.556   -14.064 -15.438 1.00 23.03 ? 77  CYS B CB  1 
ATOM   2863 S SG  . CYS B 1 77  ? 6.642   -15.300 -14.693 1.00 22.51 ? 77  CYS B SG  1 
ATOM   2864 N N   . LYS B 1 78  ? 3.340   -12.831 -17.338 1.00 23.71 ? 78  LYS B N   1 
ATOM   2865 C CA  . LYS B 1 78  ? 2.462   -11.715 -17.696 1.00 24.24 ? 78  LYS B CA  1 
ATOM   2866 C C   . LYS B 1 78  ? 1.015   -12.178 -17.836 1.00 24.53 ? 78  LYS B C   1 
ATOM   2867 O O   . LYS B 1 78  ? 0.078   -11.432 -17.547 1.00 24.90 ? 78  LYS B O   1 
ATOM   2868 C CB  . LYS B 1 78  ? 2.926   -11.058 -18.999 1.00 24.23 ? 78  LYS B CB  1 
ATOM   2869 C CG  . LYS B 1 78  ? 2.589   -9.575  -19.115 1.00 25.15 ? 78  LYS B CG  1 
ATOM   2870 C CD  . LYS B 1 78  ? 3.377   -8.759  -18.057 1.00 26.64 ? 78  LYS B CD  1 
ATOM   2871 C CE  . LYS B 1 78  ? 2.825   -7.348  -17.917 1.00 27.49 ? 78  LYS B CE  1 
ATOM   2872 N NZ  . LYS B 1 78  ? 3.436   -6.399  -18.916 1.00 28.54 ? 78  LYS B NZ  1 
ATOM   2873 N N   . ILE B 1 79  ? 0.852   -13.423 -18.269 1.00 24.63 ? 79  ILE B N   1 
ATOM   2874 C CA  . ILE B 1 79  ? -0.455  -14.019 -18.514 1.00 24.75 ? 79  ILE B CA  1 
ATOM   2875 C C   . ILE B 1 79  ? -1.048  -14.609 -17.222 1.00 24.70 ? 79  ILE B C   1 
ATOM   2876 O O   . ILE B 1 79  ? -2.262  -14.791 -17.106 1.00 24.57 ? 79  ILE B O   1 
ATOM   2877 C CB  . ILE B 1 79  ? -0.352  -15.025 -19.709 1.00 24.82 ? 79  ILE B CB  1 
ATOM   2878 C CG1 . ILE B 1 79  ? -0.999  -14.431 -20.965 1.00 25.27 ? 79  ILE B CG1 1 
ATOM   2879 C CG2 . ILE B 1 79  ? -0.986  -16.346 -19.406 1.00 25.13 ? 79  ILE B CG2 1 
ATOM   2880 C CD1 . ILE B 1 79  ? -0.263  -13.207 -21.517 1.00 26.30 ? 79  ILE B CD1 1 
ATOM   2881 N N   . ALA B 1 80  ? -0.180  -14.866 -16.246 1.00 24.75 ? 80  ALA B N   1 
ATOM   2882 C CA  . ALA B 1 80  ? -0.593  -15.324 -14.922 1.00 24.71 ? 80  ALA B CA  1 
ATOM   2883 C C   . ALA B 1 80  ? -0.828  -14.154 -13.952 1.00 24.84 ? 80  ALA B C   1 
ATOM   2884 O O   . ALA B 1 80  ? -0.786  -14.332 -12.730 1.00 24.76 ? 80  ALA B O   1 
ATOM   2885 C CB  . ALA B 1 80  ? 0.429   -16.308 -14.359 1.00 24.61 ? 80  ALA B CB  1 
ATOM   2886 N N   . SER B 1 81  ? -1.066  -12.966 -14.513 1.00 24.94 ? 81  SER B N   1 
ATOM   2887 C CA  . SER B 1 81  ? -1.468  -11.768 -13.758 1.00 25.28 ? 81  SER B CA  1 
ATOM   2888 C C   . SER B 1 81  ? -0.393  -11.177 -12.836 1.00 25.53 ? 81  SER B C   1 
ATOM   2889 O O   . SER B 1 81  ? -0.712  -10.602 -11.787 1.00 25.64 ? 81  SER B O   1 
ATOM   2890 C CB  . SER B 1 81  ? -2.770  -12.007 -12.978 1.00 25.20 ? 81  SER B CB  1 
ATOM   2891 O OG  . SER B 1 81  ? -3.879  -12.092 -13.852 1.00 25.49 ? 81  SER B OG  1 
ATOM   2892 N N   . ALA B 1 82  ? 0.872   -11.307 -13.230 1.00 25.66 ? 82  ALA B N   1 
ATOM   2893 C CA  . ALA B 1 82  ? 1.954   -10.642 -12.510 1.00 25.75 ? 82  ALA B CA  1 
ATOM   2894 C C   . ALA B 1 82  ? 1.708   -9.136  -12.498 1.00 25.88 ? 82  ALA B C   1 
ATOM   2895 O O   . ALA B 1 82  ? 1.206   -8.574  -13.477 1.00 25.98 ? 82  ALA B O   1 
ATOM   2896 C CB  . ALA B 1 82  ? 3.296   -10.959 -13.144 1.00 25.64 ? 82  ALA B CB  1 
ATOM   2897 N N   . SER B 1 83  ? 2.039   -8.496  -11.380 1.00 25.94 ? 83  SER B N   1 
ATOM   2898 C CA  . SER B 1 83  ? 1.896   -7.048  -11.251 1.00 25.96 ? 83  SER B CA  1 
ATOM   2899 C C   . SER B 1 83  ? 2.889   -6.325  -12.155 1.00 25.82 ? 83  SER B C   1 
ATOM   2900 O O   . SER B 1 83  ? 2.542   -5.346  -12.819 1.00 26.00 ? 83  SER B O   1 
ATOM   2901 C CB  . SER B 1 83  ? 2.091   -6.622  -9.794  1.00 25.99 ? 83  SER B CB  1 
ATOM   2902 O OG  . SER B 1 83  ? 2.505   -5.268  -9.717  1.00 26.89 ? 83  SER B OG  1 
ATOM   2903 N N   . ARG B 1 84  ? 4.122   -6.822  -12.173 1.00 25.53 ? 84  ARG B N   1 
ATOM   2904 C CA  . ARG B 1 84  ? 5.183   -6.261  -12.993 1.00 25.41 ? 84  ARG B CA  1 
ATOM   2905 C C   . ARG B 1 84  ? 6.172   -7.370  -13.329 1.00 25.04 ? 84  ARG B C   1 
ATOM   2906 O O   . ARG B 1 84  ? 6.511   -8.186  -12.464 1.00 24.88 ? 84  ARG B O   1 
ATOM   2907 C CB  . ARG B 1 84  ? 5.895   -5.131  -12.243 1.00 25.46 ? 84  ARG B CB  1 
ATOM   2908 C CG  . ARG B 1 84  ? 6.169   -3.901  -13.095 1.00 26.60 ? 84  ARG B CG  1 
ATOM   2909 C CD  . ARG B 1 84  ? 7.479   -3.213  -12.697 1.00 28.65 ? 84  ARG B CD  1 
ATOM   2910 N NE  . ARG B 1 84  ? 7.500   -2.772  -11.301 1.00 29.71 ? 84  ARG B NE  1 
ATOM   2911 C CZ  . ARG B 1 84  ? 8.585   -2.331  -10.670 1.00 30.22 ? 84  ARG B CZ  1 
ATOM   2912 N NH1 . ARG B 1 84  ? 9.750   -2.270  -11.303 1.00 30.80 ? 84  ARG B NH1 1 
ATOM   2913 N NH2 . ARG B 1 84  ? 8.508   -1.952  -9.402  1.00 30.13 ? 84  ARG B NH2 1 
ATOM   2914 N N   . VAL B 1 85  ? 6.615   -7.406  -14.585 1.00 24.58 ? 85  VAL B N   1 
ATOM   2915 C CA  . VAL B 1 85  ? 7.627   -8.367  -15.024 1.00 24.17 ? 85  VAL B CA  1 
ATOM   2916 C C   . VAL B 1 85  ? 8.872   -7.621  -15.487 1.00 24.00 ? 85  VAL B C   1 
ATOM   2917 O O   . VAL B 1 85  ? 8.814   -6.825  -16.425 1.00 23.85 ? 85  VAL B O   1 
ATOM   2918 C CB  . VAL B 1 85  ? 7.107   -9.301  -16.154 1.00 24.21 ? 85  VAL B CB  1 
ATOM   2919 C CG1 . VAL B 1 85  ? 8.241   -10.175 -16.709 1.00 24.15 ? 85  VAL B CG1 1 
ATOM   2920 C CG2 . VAL B 1 85  ? 5.967   -10.176 -15.648 1.00 23.74 ? 85  VAL B CG2 1 
ATOM   2921 N N   . THR B 1 86  ? 9.991   -7.883  -14.814 1.00 23.73 ? 86  THR B N   1 
ATOM   2922 C CA  . THR B 1 86  ? 11.263  -7.247  -15.135 1.00 23.46 ? 86  THR B CA  1 
ATOM   2923 C C   . THR B 1 86  ? 12.222  -8.284  -15.683 1.00 23.49 ? 86  THR B C   1 
ATOM   2924 O O   . THR B 1 86  ? 12.440  -9.331  -15.061 1.00 23.67 ? 86  THR B O   1 
ATOM   2925 C CB  . THR B 1 86  ? 11.902  -6.586  -13.889 1.00 23.36 ? 86  THR B CB  1 
ATOM   2926 O OG1 . THR B 1 86  ? 11.126  -5.449  -13.494 1.00 23.04 ? 86  THR B OG1 1 
ATOM   2927 C CG2 . THR B 1 86  ? 13.334  -6.134  -14.172 1.00 23.43 ? 86  THR B CG2 1 
ATOM   2928 N N   . ALA B 1 87  ? 12.791  -7.991  -16.849 1.00 23.31 ? 87  ALA B N   1 
ATOM   2929 C CA  . ALA B 1 87  ? 13.823  -8.837  -17.416 1.00 23.31 ? 87  ALA B CA  1 
ATOM   2930 C C   . ALA B 1 87  ? 15.181  -8.355  -16.937 1.00 23.36 ? 87  ALA B C   1 
ATOM   2931 O O   . ALA B 1 87  ? 15.560  -7.203  -17.149 1.00 23.44 ? 87  ALA B O   1 
ATOM   2932 C CB  . ALA B 1 87  ? 13.750  -8.847  -18.930 1.00 23.31 ? 87  ALA B CB  1 
ATOM   2933 N N   . VAL B 1 88  ? 15.889  -9.252  -16.259 1.00 23.45 ? 88  VAL B N   1 
ATOM   2934 C CA  . VAL B 1 88  ? 17.239  -8.993  -15.780 1.00 23.41 ? 88  VAL B CA  1 
ATOM   2935 C C   . VAL B 1 88  ? 18.183  -9.729  -16.730 1.00 23.46 ? 88  VAL B C   1 
ATOM   2936 O O   . VAL B 1 88  ? 18.399  -10.940 -16.618 1.00 23.21 ? 88  VAL B O   1 
ATOM   2937 C CB  . VAL B 1 88  ? 17.422  -9.458  -14.311 1.00 23.39 ? 88  VAL B CB  1 
ATOM   2938 C CG1 . VAL B 1 88  ? 18.708  -8.896  -13.721 1.00 23.10 ? 88  VAL B CG1 1 
ATOM   2939 C CG2 . VAL B 1 88  ? 16.224  -9.033  -13.471 1.00 23.00 ? 88  VAL B CG2 1 
ATOM   2940 N N   . ILE B 1 89  ? 18.705  -8.975  -17.693 1.00 23.56 ? 89  ILE B N   1 
ATOM   2941 C CA  . ILE B 1 89  ? 19.549  -9.523  -18.737 1.00 23.73 ? 89  ILE B CA  1 
ATOM   2942 C C   . ILE B 1 89  ? 20.938  -8.910  -18.627 1.00 23.80 ? 89  ILE B C   1 
ATOM   2943 O O   . ILE B 1 89  ? 21.227  -7.918  -19.297 1.00 23.69 ? 89  ILE B O   1 
ATOM   2944 C CB  . ILE B 1 89  ? 18.966  -9.211  -20.138 1.00 23.80 ? 89  ILE B CB  1 
ATOM   2945 C CG1 . ILE B 1 89  ? 17.480  -9.581  -20.194 1.00 23.95 ? 89  ILE B CG1 1 
ATOM   2946 C CG2 . ILE B 1 89  ? 19.728  -9.985  -21.214 1.00 24.09 ? 89  ILE B CG2 1 
ATOM   2947 C CD1 . ILE B 1 89  ? 16.735  -8.954  -21.360 1.00 24.73 ? 89  ILE B CD1 1 
ATOM   2948 N N   . PRO B 1 90  ? 21.807  -9.491  -17.775 1.00 24.00 ? 90  PRO B N   1 
ATOM   2949 C CA  . PRO B 1 90  ? 23.144  -8.924  -17.591 1.00 24.14 ? 90  PRO B CA  1 
ATOM   2950 C C   . PRO B 1 90  ? 23.854  -8.662  -18.920 1.00 24.33 ? 90  PRO B C   1 
ATOM   2951 O O   . PRO B 1 90  ? 24.303  -7.541  -19.152 1.00 24.38 ? 90  PRO B O   1 
ATOM   2952 C CB  . PRO B 1 90  ? 23.866  -9.991  -16.761 1.00 24.02 ? 90  PRO B CB  1 
ATOM   2953 C CG  . PRO B 1 90  ? 22.762  -10.619 -15.971 1.00 23.88 ? 90  PRO B CG  1 
ATOM   2954 C CD  . PRO B 1 90  ? 21.607  -10.686 -16.933 1.00 23.95 ? 90  PRO B CD  1 
ATOM   2955 N N   . CYS B 1 91  ? 23.929  -9.672  -19.785 1.00 24.52 ? 91  CYS B N   1 
ATOM   2956 C CA  . CYS B 1 91  ? 24.475  -9.494  -21.132 1.00 24.77 ? 91  CYS B CA  1 
ATOM   2957 C C   . CYS B 1 91  ? 23.340  -9.448  -22.155 1.00 24.56 ? 91  CYS B C   1 
ATOM   2958 O O   . CYS B 1 91  ? 22.640  -10.437 -22.359 1.00 24.55 ? 91  CYS B O   1 
ATOM   2959 C CB  . CYS B 1 91  ? 25.472  -10.611 -21.470 1.00 24.89 ? 91  CYS B CB  1 
ATOM   2960 S SG  . CYS B 1 91  ? 26.350  -10.389 -23.040 1.00 26.08 ? 91  CYS B SG  1 
ATOM   2961 N N   . PHE B 1 92  ? 23.166  -8.291  -22.791 1.00 24.55 ? 92  PHE B N   1 
ATOM   2962 C CA  . PHE B 1 92  ? 22.052  -8.076  -23.717 1.00 24.50 ? 92  PHE B CA  1 
ATOM   2963 C C   . PHE B 1 92  ? 22.294  -8.747  -25.068 1.00 24.49 ? 92  PHE B C   1 
ATOM   2964 O O   . PHE B 1 92  ? 23.237  -8.392  -25.773 1.00 24.42 ? 92  PHE B O   1 
ATOM   2965 C CB  . PHE B 1 92  ? 21.780  -6.578  -23.904 1.00 24.47 ? 92  PHE B CB  1 
ATOM   2966 C CG  . PHE B 1 92  ? 20.508  -6.282  -24.647 1.00 24.06 ? 92  PHE B CG  1 
ATOM   2967 C CD1 . PHE B 1 92  ? 19.291  -6.230  -23.974 1.00 23.99 ? 92  PHE B CD1 1 
ATOM   2968 C CD2 . PHE B 1 92  ? 20.524  -6.056  -26.019 1.00 23.43 ? 92  PHE B CD2 1 
ATOM   2969 C CE1 . PHE B 1 92  ? 18.113  -5.966  -24.659 1.00 23.92 ? 92  PHE B CE1 1 
ATOM   2970 C CE2 . PHE B 1 92  ? 19.347  -5.789  -26.711 1.00 23.45 ? 92  PHE B CE2 1 
ATOM   2971 C CZ  . PHE B 1 92  ? 18.143  -5.744  -26.033 1.00 23.30 ? 92  PHE B CZ  1 
ATOM   2972 N N   . PRO B 1 93  ? 21.430  -9.710  -25.441 1.00 24.61 ? 93  PRO B N   1 
ATOM   2973 C CA  . PRO B 1 93  ? 21.652  -10.485 -26.665 1.00 24.72 ? 93  PRO B CA  1 
ATOM   2974 C C   . PRO B 1 93  ? 21.554  -9.629  -27.927 1.00 24.88 ? 93  PRO B C   1 
ATOM   2975 O O   . PRO B 1 93  ? 20.794  -8.658  -27.960 1.00 24.80 ? 93  PRO B O   1 
ATOM   2976 C CB  . PRO B 1 93  ? 20.532  -11.530 -26.631 1.00 24.67 ? 93  PRO B CB  1 
ATOM   2977 C CG  . PRO B 1 93  ? 19.478  -10.935 -25.766 1.00 24.69 ? 93  PRO B CG  1 
ATOM   2978 C CD  . PRO B 1 93  ? 20.196  -10.118 -24.743 1.00 24.51 ? 93  PRO B CD  1 
ATOM   2979 N N   . TYR B 1 94  ? 22.339  -9.995  -28.941 1.00 25.15 ? 94  TYR B N   1 
ATOM   2980 C CA  . TYR B 1 94  ? 22.375  -9.301  -30.239 1.00 25.45 ? 94  TYR B CA  1 
ATOM   2981 C C   . TYR B 1 94  ? 22.726  -7.811  -30.141 1.00 26.05 ? 94  TYR B C   1 
ATOM   2982 O O   . TYR B 1 94  ? 22.533  -7.059  -31.104 1.00 26.02 ? 94  TYR B O   1 
ATOM   2983 C CB  . TYR B 1 94  ? 21.059  -9.513  -31.015 1.00 25.09 ? 94  TYR B CB  1 
ATOM   2984 C CG  . TYR B 1 94  ? 20.864  -10.929 -31.521 1.00 24.25 ? 94  TYR B CG  1 
ATOM   2985 C CD1 . TYR B 1 94  ? 21.139  -11.262 -32.851 1.00 23.74 ? 94  TYR B CD1 1 
ATOM   2986 C CD2 . TYR B 1 94  ? 20.406  -11.934 -30.676 1.00 22.78 ? 94  TYR B CD2 1 
ATOM   2987 C CE1 . TYR B 1 94  ? 20.960  -12.559 -33.320 1.00 22.27 ? 94  TYR B CE1 1 
ATOM   2988 C CE2 . TYR B 1 94  ? 20.230  -13.232 -31.133 1.00 22.27 ? 94  TYR B CE2 1 
ATOM   2989 C CZ  . TYR B 1 94  ? 20.508  -13.538 -32.452 1.00 22.21 ? 94  TYR B CZ  1 
ATOM   2990 O OH  . TYR B 1 94  ? 20.329  -14.830 -32.896 1.00 22.53 ? 94  TYR B OH  1 
ATOM   2991 N N   . ALA B 1 95  ? 23.267  -7.400  -28.992 1.00 26.80 ? 95  ALA B N   1 
ATOM   2992 C CA  . ALA B 1 95  ? 23.621  -5.996  -28.741 1.00 27.67 ? 95  ALA B CA  1 
ATOM   2993 C C   . ALA B 1 95  ? 24.604  -5.402  -29.759 1.00 28.24 ? 95  ALA B C   1 
ATOM   2994 O O   . ALA B 1 95  ? 24.560  -4.199  -30.031 1.00 28.38 ? 95  ALA B O   1 
ATOM   2995 C CB  . ALA B 1 95  ? 24.149  -5.819  -27.321 1.00 27.55 ? 95  ALA B CB  1 
ATOM   2996 N N   . ARG B 1 96  ? 25.482  -6.237  -30.315 1.00 28.96 ? 96  ARG B N   1 
ATOM   2997 C CA  . ARG B 1 96  ? 26.416  -5.782  -31.352 1.00 29.76 ? 96  ARG B CA  1 
ATOM   2998 C C   . ARG B 1 96  ? 25.728  -5.472  -32.685 1.00 30.20 ? 96  ARG B C   1 
ATOM   2999 O O   . ARG B 1 96  ? 26.309  -4.807  -33.546 1.00 30.24 ? 96  ARG B O   1 
ATOM   3000 C CB  . ARG B 1 96  ? 27.555  -6.783  -31.558 1.00 29.70 ? 96  ARG B CB  1 
ATOM   3001 C CG  . ARG B 1 96  ? 28.786  -6.540  -30.607 1.00 30.42 ? 96  ARG B CG  1 
ATOM   3002 C CD  . ARG B 1 96  ? 29.764  -7.738  -30.830 1.00 31.12 ? 96  ARG B CD  1 
ATOM   3003 N NE  . ARG B 1 96  ? 29.000  -8.991  -30.752 1.00 32.17 ? 96  ARG B NE  1 
ATOM   3004 C CZ  . ARG B 1 96  ? 29.532  -10.209 -30.808 1.00 32.60 ? 96  ARG B CZ  1 
ATOM   3005 N NH1 . ARG B 1 96  ? 30.856  -10.366 -30.928 1.00 33.09 ? 96  ARG B NH1 1 
ATOM   3006 N NH2 . ARG B 1 96  ? 28.729  -11.275 -30.738 1.00 32.29 ? 96  ARG B NH2 1 
ATOM   3007 N N   . GLN B 1 97  ? 24.501  -5.966  -32.853 1.00 30.76 ? 97  GLN B N   1 
ATOM   3008 C CA  . GLN B 1 97  ? 23.690  -5.632  -34.024 1.00 31.38 ? 97  GLN B CA  1 
ATOM   3009 C C   . GLN B 1 97  ? 22.746  -4.468  -33.713 1.00 31.62 ? 97  GLN B C   1 
ATOM   3010 O O   . GLN B 1 97  ? 21.525  -4.630  -33.661 1.00 31.46 ? 97  GLN B O   1 
ATOM   3011 C CB  . GLN B 1 97  ? 22.935  -6.865  -34.544 1.00 31.47 ? 97  GLN B CB  1 
ATOM   3012 C CG  . GLN B 1 97  ? 23.767  -7.745  -35.483 1.00 31.98 ? 97  GLN B CG  1 
ATOM   3013 C CD  . GLN B 1 97  ? 23.282  -9.186  -35.512 1.00 33.16 ? 97  GLN B CD  1 
ATOM   3014 O OE1 . GLN B 1 97  ? 22.197  -9.485  -36.025 1.00 33.92 ? 97  GLN B OE1 1 
ATOM   3015 N NE2 . GLN B 1 97  ? 24.095  -10.094 -34.972 1.00 33.31 ? 97  GLN B NE2 1 
ATOM   3016 N N   . ASP B 1 98  ? 23.339  -3.293  -33.506 1.00 32.16 ? 98  ASP B N   1 
ATOM   3017 C CA  . ASP B 1 98  ? 22.594  -2.079  -33.162 1.00 32.67 ? 98  ASP B CA  1 
ATOM   3018 C C   . ASP B 1 98  ? 22.582  -1.022  -34.280 1.00 32.94 ? 98  ASP B C   1 
ATOM   3019 O O   . ASP B 1 98  ? 21.978  0.045   -34.122 1.00 33.12 ? 98  ASP B O   1 
ATOM   3020 C CB  . ASP B 1 98  ? 23.109  -1.477  -31.844 1.00 32.63 ? 98  ASP B CB  1 
ATOM   3021 C CG  . ASP B 1 98  ? 24.595  -1.134  -31.886 1.00 33.31 ? 98  ASP B CG  1 
ATOM   3022 O OD1 . ASP B 1 98  ? 25.325  -1.662  -32.756 1.00 34.28 ? 98  ASP B OD1 1 
ATOM   3023 O OD2 . ASP B 1 98  ? 25.040  -0.335  -31.034 1.00 33.49 ? 98  ASP B OD2 1 
ATOM   3024 N N   . LYS B 1 99  ? 23.228  -1.329  -35.406 1.00 33.25 ? 99  LYS B N   1 
ATOM   3025 C CA  . LYS B 1 99  ? 23.287  -0.414  -36.555 1.00 33.65 ? 99  LYS B CA  1 
ATOM   3026 C C   . LYS B 1 99  ? 23.381  -1.119  -37.921 1.00 33.83 ? 99  LYS B C   1 
ATOM   3027 O O   . LYS B 1 99  ? 23.827  -2.265  -38.010 1.00 33.70 ? 99  LYS B O   1 
ATOM   3028 C CB  . LYS B 1 99  ? 24.427  0.602   -36.388 1.00 33.64 ? 99  LYS B CB  1 
ATOM   3029 C CG  . LYS B 1 99  ? 25.793  0.025   -36.006 1.00 34.16 ? 99  LYS B CG  1 
ATOM   3030 C CD  . LYS B 1 99  ? 26.817  1.150   -35.863 1.00 35.09 ? 99  LYS B CD  1 
ATOM   3031 C CE  . LYS B 1 99  ? 27.913  0.815   -34.844 1.00 35.65 ? 99  LYS B CE  1 
ATOM   3032 N NZ  . LYS B 1 99  ? 28.601  2.057   -34.349 1.00 35.25 ? 99  LYS B NZ  1 
ATOM   3033 N N   . LYS B 1 100 ? 22.957  -0.419  -38.977 1.00 34.32 ? 100 LYS B N   1 
ATOM   3034 C CA  . LYS B 1 100 ? 23.002  -0.954  -40.344 1.00 34.83 ? 100 LYS B CA  1 
ATOM   3035 C C   . LYS B 1 100 ? 24.407  -1.088  -40.943 1.00 35.34 ? 100 LYS B C   1 
ATOM   3036 O O   . LYS B 1 100 ? 24.641  -1.964  -41.779 1.00 35.46 ? 100 LYS B O   1 
ATOM   3037 C CB  . LYS B 1 100 ? 22.119  -0.128  -41.278 1.00 34.76 ? 100 LYS B CB  1 
ATOM   3038 C CG  . LYS B 1 100 ? 20.638  -0.521  -41.246 1.00 34.48 ? 100 LYS B CG  1 
ATOM   3039 C CD  . LYS B 1 100 ? 19.876  0.286   -42.295 1.00 33.70 ? 100 LYS B CD  1 
ATOM   3040 C CE  . LYS B 1 100 ? 18.390  0.016   -42.185 1.00 33.29 ? 100 LYS B CE  1 
ATOM   3041 N NZ  . LYS B 1 100 ? 17.553  0.869   -43.081 1.00 32.59 ? 100 LYS B NZ  1 
ATOM   3042 N N   . ASP B 1 101 ? 25.326  -0.219  -40.523 1.00 35.84 ? 101 ASP B N   1 
ATOM   3043 C CA  . ASP B 1 101 ? 26.711  -0.214  -41.011 1.00 36.29 ? 101 ASP B CA  1 
ATOM   3044 C C   . ASP B 1 101 ? 26.819  -0.270  -42.536 1.00 36.30 ? 101 ASP B C   1 
ATOM   3045 O O   . ASP B 1 101 ? 27.441  -1.189  -43.083 1.00 36.51 ? 101 ASP B O   1 
ATOM   3046 C CB  . ASP B 1 101 ? 27.517  -1.376  -40.396 1.00 36.53 ? 101 ASP B CB  1 
ATOM   3047 C CG  . ASP B 1 101 ? 28.020  -1.080  -38.985 1.00 37.30 ? 101 ASP B CG  1 
ATOM   3048 O OD1 . ASP B 1 101 ? 28.183  0.116   -38.624 1.00 37.65 ? 101 ASP B OD1 1 
ATOM   3049 O OD2 . ASP B 1 101 ? 28.269  -2.067  -38.232 1.00 38.29 ? 101 ASP B OD2 1 
ATOM   3050 N N   . LYS B 1 102 ? 26.201  0.700   -43.215 1.00 36.11 ? 102 LYS B N   1 
ATOM   3051 C CA  . LYS B 1 102 ? 26.270  0.815   -44.685 1.00 35.93 ? 102 LYS B CA  1 
ATOM   3052 C C   . LYS B 1 102 ? 25.855  -0.446  -45.467 1.00 35.49 ? 102 LYS B C   1 
ATOM   3053 O O   . LYS B 1 102 ? 26.273  -0.631  -46.617 1.00 35.64 ? 102 LYS B O   1 
ATOM   3054 C CB  . LYS B 1 102 ? 27.674  1.253   -45.146 1.00 36.14 ? 102 LYS B CB  1 
ATOM   3055 C CG  . LYS B 1 102 ? 28.122  2.639   -44.709 1.00 36.79 ? 102 LYS B CG  1 
ATOM   3056 C CD  . LYS B 1 102 ? 28.945  3.305   -45.815 1.00 37.76 ? 102 LYS B CD  1 
ATOM   3057 C CE  . LYS B 1 102 ? 29.752  4.499   -45.301 1.00 38.03 ? 102 LYS B CE  1 
ATOM   3058 N NZ  . LYS B 1 102 ? 31.189  4.153   -45.076 1.00 38.40 ? 102 LYS B NZ  1 
ATOM   3059 N N   . SER B 1 103 ? 25.047  -1.311  -44.856 1.00 34.86 ? 103 SER B N   1 
ATOM   3060 C CA  . SER B 1 103 ? 24.596  -2.541  -45.526 1.00 34.18 ? 103 SER B CA  1 
ATOM   3061 C C   . SER B 1 103 ? 23.161  -2.937  -45.173 1.00 33.53 ? 103 SER B C   1 
ATOM   3062 O O   . SER B 1 103 ? 22.616  -2.496  -44.158 1.00 33.36 ? 103 SER B O   1 
ATOM   3063 C CB  . SER B 1 103 ? 25.562  -3.706  -45.258 1.00 34.32 ? 103 SER B CB  1 
ATOM   3064 O OG  . SER B 1 103 ? 25.882  -3.807  -43.864 1.00 34.51 ? 103 SER B OG  1 
ATOM   3065 N N   . ARG B 1 104 ? 22.562  -3.772  -46.023 1.00 32.83 ? 104 ARG B N   1 
ATOM   3066 C CA  . ARG B 1 104 ? 21.201  -4.267  -45.807 1.00 32.13 ? 104 ARG B CA  1 
ATOM   3067 C C   . ARG B 1 104 ? 21.168  -5.305  -44.694 1.00 31.58 ? 104 ARG B C   1 
ATOM   3068 O O   . ARG B 1 104 ? 20.931  -6.499  -44.924 1.00 31.62 ? 104 ARG B O   1 
ATOM   3069 C CB  . ARG B 1 104 ? 20.607  -4.829  -47.097 1.00 32.19 ? 104 ARG B CB  1 
ATOM   3070 C CG  . ARG B 1 104 ? 20.135  -3.757  -48.061 1.00 32.72 ? 104 ARG B CG  1 
ATOM   3071 C CD  . ARG B 1 104 ? 19.597  -4.380  -49.328 1.00 33.68 ? 104 ARG B CD  1 
ATOM   3072 N NE  . ARG B 1 104 ? 19.908  -3.558  -50.499 1.00 34.15 ? 104 ARG B NE  1 
ATOM   3073 C CZ  . ARG B 1 104 ? 20.957  -3.758  -51.294 1.00 34.49 ? 104 ARG B CZ  1 
ATOM   3074 N NH1 . ARG B 1 104 ? 21.807  -4.760  -51.058 1.00 34.56 ? 104 ARG B NH1 1 
ATOM   3075 N NH2 . ARG B 1 104 ? 21.152  -2.954  -52.333 1.00 34.76 ? 104 ARG B NH2 1 
ATOM   3076 N N   . ALA B 1 105 ? 21.424  -4.829  -43.481 1.00 30.73 ? 105 ALA B N   1 
ATOM   3077 C CA  . ALA B 1 105 ? 21.423  -5.672  -42.305 1.00 29.89 ? 105 ALA B CA  1 
ATOM   3078 C C   . ALA B 1 105 ? 20.207  -5.315  -41.454 1.00 29.30 ? 105 ALA B C   1 
ATOM   3079 O O   . ALA B 1 105 ? 19.596  -4.256  -41.647 1.00 29.06 ? 105 ALA B O   1 
ATOM   3080 C CB  . ALA B 1 105 ? 22.708  -5.462  -41.516 1.00 30.03 ? 105 ALA B CB  1 
ATOM   3081 N N   . PRO B 1 106 ? 19.824  -6.215  -40.525 1.00 28.63 ? 106 PRO B N   1 
ATOM   3082 C CA  . PRO B 1 106 ? 18.821  -5.856  -39.547 1.00 28.06 ? 106 PRO B CA  1 
ATOM   3083 C C   . PRO B 1 106 ? 19.482  -5.179  -38.360 1.00 27.44 ? 106 PRO B C   1 
ATOM   3084 O O   . PRO B 1 106 ? 20.684  -5.361  -38.123 1.00 27.57 ? 106 PRO B O   1 
ATOM   3085 C CB  . PRO B 1 106 ? 18.251  -7.212  -39.132 1.00 28.08 ? 106 PRO B CB  1 
ATOM   3086 C CG  . PRO B 1 106 ? 19.414  -8.119  -39.209 1.00 28.28 ? 106 PRO B CG  1 
ATOM   3087 C CD  . PRO B 1 106 ? 20.260  -7.645  -40.363 1.00 28.72 ? 106 PRO B CD  1 
ATOM   3088 N N   . ILE B 1 107 ? 18.705  -4.390  -37.630 1.00 26.62 ? 107 ILE B N   1 
ATOM   3089 C CA  . ILE B 1 107 ? 19.138  -3.900  -36.335 1.00 25.57 ? 107 ILE B CA  1 
ATOM   3090 C C   . ILE B 1 107 ? 18.528  -4.848  -35.304 1.00 25.17 ? 107 ILE B C   1 
ATOM   3091 O O   . ILE B 1 107 ? 17.584  -4.488  -34.594 1.00 24.93 ? 107 ILE B O   1 
ATOM   3092 C CB  . ILE B 1 107 ? 18.710  -2.442  -36.098 1.00 25.48 ? 107 ILE B CB  1 
ATOM   3093 C CG1 . ILE B 1 107 ? 18.977  -1.585  -37.351 1.00 24.60 ? 107 ILE B CG1 1 
ATOM   3094 C CG2 . ILE B 1 107 ? 19.432  -1.882  -34.874 1.00 25.39 ? 107 ILE B CG2 1 
ATOM   3095 C CD1 . ILE B 1 107 ? 18.484  -0.157  -37.228 1.00 24.04 ? 107 ILE B CD1 1 
ATOM   3096 N N   . SER B 1 108 ? 19.078  -6.073  -35.254 1.00 24.66 ? 108 SER B N   1 
ATOM   3097 C CA  . SER B 1 108 ? 18.534  -7.165  -34.438 1.00 24.31 ? 108 SER B CA  1 
ATOM   3098 C C   . SER B 1 108 ? 18.383  -6.839  -32.951 1.00 23.98 ? 108 SER B C   1 
ATOM   3099 O O   . SER B 1 108 ? 17.534  -7.426  -32.278 1.00 24.19 ? 108 SER B O   1 
ATOM   3100 C CB  . SER B 1 108 ? 19.378  -8.432  -34.595 1.00 24.40 ? 108 SER B CB  1 
ATOM   3101 O OG  . SER B 1 108 ? 19.892  -8.537  -35.937 1.00 24.78 ? 108 SER B OG  1 
ATOM   3102 N N   . ALA B 1 109 ? 19.207  -5.920  -32.444 1.00 23.52 ? 109 ALA B N   1 
ATOM   3103 C CA  . ALA B 1 109 ? 19.079  -5.427  -31.068 1.00 22.98 ? 109 ALA B CA  1 
ATOM   3104 C C   . ALA B 1 109 ? 17.748  -4.704  -30.851 1.00 22.72 ? 109 ALA B C   1 
ATOM   3105 O O   . ALA B 1 109 ? 17.157  -4.780  -29.770 1.00 22.71 ? 109 ALA B O   1 
ATOM   3106 C CB  . ALA B 1 109 ? 20.238  -4.521  -30.714 1.00 23.02 ? 109 ALA B CB  1 
ATOM   3107 N N   . LYS B 1 110 ? 17.287  -4.007  -31.888 1.00 22.26 ? 110 LYS B N   1 
ATOM   3108 C CA  . LYS B 1 110 ? 15.969  -3.383  -31.879 1.00 21.72 ? 110 LYS B CA  1 
ATOM   3109 C C   . LYS B 1 110 ? 14.865  -4.439  -31.998 1.00 21.48 ? 110 LYS B C   1 
ATOM   3110 O O   . LYS B 1 110 ? 13.820  -4.323  -31.355 1.00 21.59 ? 110 LYS B O   1 
ATOM   3111 C CB  . LYS B 1 110 ? 15.858  -2.331  -32.991 1.00 21.62 ? 110 LYS B CB  1 
ATOM   3112 C CG  . LYS B 1 110 ? 14.479  -1.685  -33.129 1.00 21.33 ? 110 LYS B CG  1 
ATOM   3113 C CD  . LYS B 1 110 ? 14.045  -0.988  -31.842 1.00 20.45 ? 110 LYS B CD  1 
ATOM   3114 C CE  . LYS B 1 110 ? 12.594  -0.601  -31.896 1.00 20.09 ? 110 LYS B CE  1 
ATOM   3115 N NZ  . LYS B 1 110 ? 12.332  0.235   -33.087 1.00 20.09 ? 110 LYS B NZ  1 
ATOM   3116 N N   . LEU B 1 111 ? 15.104  -5.462  -32.815 1.00 21.16 ? 111 LEU B N   1 
ATOM   3117 C CA  . LEU B 1 111 ? 14.181  -6.587  -32.930 1.00 20.87 ? 111 LEU B CA  1 
ATOM   3118 C C   . LEU B 1 111 ? 14.011  -7.252  -31.559 1.00 20.68 ? 111 LEU B C   1 
ATOM   3119 O O   . LEU B 1 111 ? 12.888  -7.427  -31.087 1.00 20.58 ? 111 LEU B O   1 
ATOM   3120 C CB  . LEU B 1 111 ? 14.701  -7.610  -33.948 1.00 20.85 ? 111 LEU B CB  1 
ATOM   3121 C CG  . LEU B 1 111 ? 13.770  -8.571  -34.703 1.00 20.51 ? 111 LEU B CG  1 
ATOM   3122 C CD1 . LEU B 1 111 ? 14.473  -9.907  -34.880 1.00 20.48 ? 111 LEU B CD1 1 
ATOM   3123 C CD2 . LEU B 1 111 ? 12.416  -8.780  -34.051 1.00 19.58 ? 111 LEU B CD2 1 
ATOM   3124 N N   . VAL B 1 112 ? 15.137  -7.607  -30.934 1.00 20.45 ? 112 VAL B N   1 
ATOM   3125 C CA  . VAL B 1 112 ? 15.162  -8.217  -29.597 1.00 20.15 ? 112 VAL B CA  1 
ATOM   3126 C C   . VAL B 1 112 ? 14.415  -7.362  -28.569 1.00 19.95 ? 112 VAL B C   1 
ATOM   3127 O O   . VAL B 1 112 ? 13.637  -7.889  -27.767 1.00 19.95 ? 112 VAL B O   1 
ATOM   3128 C CB  . VAL B 1 112 ? 16.614  -8.493  -29.112 1.00 20.12 ? 112 VAL B CB  1 
ATOM   3129 C CG1 . VAL B 1 112 ? 16.630  -8.969  -27.657 1.00 19.98 ? 112 VAL B CG1 1 
ATOM   3130 C CG2 . VAL B 1 112 ? 17.292  -9.520  -30.006 1.00 19.90 ? 112 VAL B CG2 1 
ATOM   3131 N N   . ALA B 1 113 ? 14.647  -6.051  -28.609 1.00 19.64 ? 113 ALA B N   1 
ATOM   3132 C CA  . ALA B 1 113 ? 13.956  -5.114  -27.724 1.00 19.51 ? 113 ALA B CA  1 
ATOM   3133 C C   . ALA B 1 113 ? 12.445  -5.123  -27.977 1.00 19.45 ? 113 ALA B C   1 
ATOM   3134 O O   . ALA B 1 113 ? 11.651  -5.130  -27.028 1.00 19.31 ? 113 ALA B O   1 
ATOM   3135 C CB  . ALA B 1 113 ? 14.521  -3.710  -27.877 1.00 19.34 ? 113 ALA B CB  1 
ATOM   3136 N N   . ASN B 1 114 ? 12.056  -5.134  -29.253 1.00 19.30 ? 114 ASN B N   1 
ATOM   3137 C CA  . ASN B 1 114 ? 10.645  -5.251  -29.623 1.00 19.12 ? 114 ASN B CA  1 
ATOM   3138 C C   . ASN B 1 114 ? 10.045  -6.573  -29.170 1.00 18.99 ? 114 ASN B C   1 
ATOM   3139 O O   . ASN B 1 114 ? 8.902   -6.612  -28.712 1.00 18.72 ? 114 ASN B O   1 
ATOM   3140 C CB  . ASN B 1 114 ? 10.443  -5.055  -31.127 1.00 19.11 ? 114 ASN B CB  1 
ATOM   3141 C CG  . ASN B 1 114 ? 10.393  -3.591  -31.527 1.00 19.42 ? 114 ASN B CG  1 
ATOM   3142 O OD1 . ASN B 1 114 ? 10.288  -2.703  -30.682 1.00 19.87 ? 114 ASN B OD1 1 
ATOM   3143 N ND2 . ASN B 1 114 ? 10.463  -3.334  -32.826 1.00 19.68 ? 114 ASN B ND2 1 
ATOM   3144 N N   . MET B 1 115 ? 10.827  -7.648  -29.285 1.00 19.11 ? 115 MET B N   1 
ATOM   3145 C CA  . MET B 1 115 ? 10.401  -8.975  -28.831 1.00 19.30 ? 115 MET B CA  1 
ATOM   3146 C C   . MET B 1 115 ? 10.160  -9.000  -27.323 1.00 19.40 ? 115 MET B C   1 
ATOM   3147 O O   . MET B 1 115 ? 9.086   -9.414  -26.872 1.00 19.29 ? 115 MET B O   1 
ATOM   3148 C CB  . MET B 1 115 ? 11.392  -10.058 -29.264 1.00 19.23 ? 115 MET B CB  1 
ATOM   3149 C CG  . MET B 1 115 ? 11.171  -10.533 -30.698 1.00 19.70 ? 115 MET B CG  1 
ATOM   3150 S SD  . MET B 1 115 ? 12.650  -11.150 -31.529 1.00 22.68 ? 115 MET B SD  1 
ATOM   3151 C CE  . MET B 1 115 ? 12.896  -12.743 -30.757 1.00 18.94 ? 115 MET B CE  1 
ATOM   3152 N N   . LEU B 1 116 ? 11.136  -8.518  -26.554 1.00 19.44 ? 116 LEU B N   1 
ATOM   3153 C CA  . LEU B 1 116 ? 10.985  -8.413  -25.106 1.00 19.64 ? 116 LEU B CA  1 
ATOM   3154 C C   . LEU B 1 116 ? 9.764   -7.578  -24.712 1.00 19.84 ? 116 LEU B C   1 
ATOM   3155 O O   . LEU B 1 116 ? 9.051   -7.921  -23.762 1.00 19.78 ? 116 LEU B O   1 
ATOM   3156 C CB  . LEU B 1 116 ? 12.260  -7.851  -24.460 1.00 19.70 ? 116 LEU B CB  1 
ATOM   3157 C CG  . LEU B 1 116 ? 13.489  -8.763  -24.388 1.00 19.31 ? 116 LEU B CG  1 
ATOM   3158 C CD1 . LEU B 1 116 ? 14.757  -7.936  -24.352 1.00 19.25 ? 116 LEU B CD1 1 
ATOM   3159 C CD2 . LEU B 1 116 ? 13.413  -9.686  -23.183 1.00 19.59 ? 116 LEU B CD2 1 
ATOM   3160 N N   . SER B 1 117 ? 9.528   -6.493  -25.451 1.00 20.10 ? 117 SER B N   1 
ATOM   3161 C CA  . SER B 1 117 ? 8.387   -5.608  -25.204 1.00 20.42 ? 117 SER B CA  1 
ATOM   3162 C C   . SER B 1 117 ? 7.055   -6.311  -25.480 1.00 20.67 ? 117 SER B C   1 
ATOM   3163 O O   . SER B 1 117 ? 6.196   -6.398  -24.595 1.00 20.67 ? 117 SER B O   1 
ATOM   3164 C CB  . SER B 1 117 ? 8.491   -4.326  -26.051 1.00 20.44 ? 117 SER B CB  1 
ATOM   3165 O OG  . SER B 1 117 ? 9.804   -3.765  -25.967 1.00 20.43 ? 117 SER B OG  1 
ATOM   3166 N N   . VAL B 1 118 ? 6.898   -6.818  -26.704 1.00 20.84 ? 118 VAL B N   1 
ATOM   3167 C CA  . VAL B 1 118 ? 5.668   -7.498  -27.111 1.00 21.14 ? 118 VAL B CA  1 
ATOM   3168 C C   . VAL B 1 118 ? 5.438   -8.804  -26.321 1.00 21.23 ? 118 VAL B C   1 
ATOM   3169 O O   . VAL B 1 118 ? 4.329   -9.339  -26.304 1.00 21.34 ? 118 VAL B O   1 
ATOM   3170 C CB  . VAL B 1 118 ? 5.618   -7.719  -28.665 1.00 21.17 ? 118 VAL B CB  1 
ATOM   3171 C CG1 . VAL B 1 118 ? 6.310   -9.024  -29.083 1.00 21.19 ? 118 VAL B CG1 1 
ATOM   3172 C CG2 . VAL B 1 118 ? 4.181   -7.683  -29.170 1.00 21.41 ? 118 VAL B CG2 1 
ATOM   3173 N N   . ALA B 1 119 ? 6.480   -9.297  -25.657 1.00 21.35 ? 119 ALA B N   1 
ATOM   3174 C CA  . ALA B 1 119 ? 6.358   -10.489 -24.812 1.00 21.58 ? 119 ALA B CA  1 
ATOM   3175 C C   . ALA B 1 119 ? 5.735   -10.185 -23.454 1.00 21.66 ? 119 ALA B C   1 
ATOM   3176 O O   . ALA B 1 119 ? 5.136   -11.065 -22.840 1.00 21.90 ? 119 ALA B O   1 
ATOM   3177 C CB  . ALA B 1 119 ? 7.712   -11.180 -24.637 1.00 21.55 ? 119 ALA B CB  1 
ATOM   3178 N N   . GLY B 1 120 ? 5.887   -8.948  -22.981 1.00 21.75 ? 120 GLY B N   1 
ATOM   3179 C CA  . GLY B 1 120 ? 5.244   -8.533  -21.729 1.00 21.91 ? 120 GLY B CA  1 
ATOM   3180 C C   . GLY B 1 120 ? 6.137   -7.892  -20.676 1.00 22.12 ? 120 GLY B C   1 
ATOM   3181 O O   . GLY B 1 120 ? 5.662   -7.560  -19.587 1.00 22.24 ? 120 GLY B O   1 
ATOM   3182 N N   . ALA B 1 121 ? 7.427   -7.724  -20.984 1.00 22.05 ? 121 ALA B N   1 
ATOM   3183 C CA  . ALA B 1 121 ? 8.362   -7.061  -20.070 1.00 21.83 ? 121 ALA B CA  1 
ATOM   3184 C C   . ALA B 1 121 ? 7.920   -5.630  -19.814 1.00 21.80 ? 121 ALA B C   1 
ATOM   3185 O O   . ALA B 1 121 ? 7.430   -4.958  -20.727 1.00 21.80 ? 121 ALA B O   1 
ATOM   3186 C CB  . ALA B 1 121 ? 9.771   -7.081  -20.634 1.00 21.87 ? 121 ALA B CB  1 
ATOM   3187 N N   . ASP B 1 122 ? 8.087   -5.180  -18.568 1.00 21.76 ? 122 ASP B N   1 
ATOM   3188 C CA  . ASP B 1 122 ? 7.674   -3.837  -18.146 1.00 21.71 ? 122 ASP B CA  1 
ATOM   3189 C C   . ASP B 1 122 ? 8.883   -2.988  -17.822 1.00 21.61 ? 122 ASP B C   1 
ATOM   3190 O O   . ASP B 1 122 ? 8.804   -1.759  -17.771 1.00 21.47 ? 122 ASP B O   1 
ATOM   3191 C CB  . ASP B 1 122 ? 6.784   -3.909  -16.899 1.00 21.61 ? 122 ASP B CB  1 
ATOM   3192 C CG  . ASP B 1 122 ? 5.461   -4.600  -17.161 1.00 21.91 ? 122 ASP B CG  1 
ATOM   3193 O OD1 . ASP B 1 122 ? 4.670   -4.094  -17.988 1.00 22.18 ? 122 ASP B OD1 1 
ATOM   3194 O OD2 . ASP B 1 122 ? 5.205   -5.644  -16.524 1.00 22.06 ? 122 ASP B OD2 1 
ATOM   3195 N N   . HIS B 1 123 ? 10.004  -3.659  -17.594 1.00 21.87 ? 123 HIS B N   1 
ATOM   3196 C CA  . HIS B 1 123 ? 11.212  -3.017  -17.105 1.00 22.24 ? 123 HIS B CA  1 
ATOM   3197 C C   . HIS B 1 123 ? 12.408  -3.900  -17.443 1.00 22.16 ? 123 HIS B C   1 
ATOM   3198 O O   . HIS B 1 123 ? 12.288  -5.124  -17.488 1.00 22.16 ? 123 HIS B O   1 
ATOM   3199 C CB  . HIS B 1 123 ? 11.099  -2.796  -15.589 1.00 22.38 ? 123 HIS B CB  1 
ATOM   3200 C CG  . HIS B 1 123 ? 12.264  -2.066  -14.998 1.00 23.57 ? 123 HIS B CG  1 
ATOM   3201 N ND1 . HIS B 1 123 ? 13.242  -2.702  -14.261 1.00 25.04 ? 123 HIS B ND1 1 
ATOM   3202 C CD2 . HIS B 1 123 ? 12.609  -0.755  -15.033 1.00 24.70 ? 123 HIS B CD2 1 
ATOM   3203 C CE1 . HIS B 1 123 ? 14.141  -1.813  -13.867 1.00 25.42 ? 123 HIS B CE1 1 
ATOM   3204 N NE2 . HIS B 1 123 ? 13.782  -0.624  -14.324 1.00 24.93 ? 123 HIS B NE2 1 
ATOM   3205 N N   . ILE B 1 124 ? 13.552  -3.275  -17.705 1.00 22.20 ? 124 ILE B N   1 
ATOM   3206 C CA  . ILE B 1 124 ? 14.769  -4.008  -18.052 1.00 22.00 ? 124 ILE B CA  1 
ATOM   3207 C C   . ILE B 1 124 ? 15.914  -3.557  -17.153 1.00 22.02 ? 124 ILE B C   1 
ATOM   3208 O O   . ILE B 1 124 ? 16.142  -2.356  -16.981 1.00 22.05 ? 124 ILE B O   1 
ATOM   3209 C CB  . ILE B 1 124 ? 15.175  -3.798  -19.547 1.00 22.02 ? 124 ILE B CB  1 
ATOM   3210 C CG1 . ILE B 1 124 ? 14.010  -4.128  -20.509 1.00 21.95 ? 124 ILE B CG1 1 
ATOM   3211 C CG2 . ILE B 1 124 ? 16.453  -4.588  -19.884 1.00 21.43 ? 124 ILE B CG2 1 
ATOM   3212 C CD1 . ILE B 1 124 ? 13.682  -5.616  -20.668 1.00 22.49 ? 124 ILE B CD1 1 
ATOM   3213 N N   . ILE B 1 125 ? 16.612  -4.527  -16.567 1.00 21.91 ? 125 ILE B N   1 
ATOM   3214 C CA  . ILE B 1 125 ? 17.848  -4.276  -15.837 1.00 21.86 ? 125 ILE B CA  1 
ATOM   3215 C C   . ILE B 1 125 ? 18.968  -5.009  -16.576 1.00 21.98 ? 125 ILE B C   1 
ATOM   3216 O O   . ILE B 1 125 ? 18.904  -6.224  -16.772 1.00 21.99 ? 125 ILE B O   1 
ATOM   3217 C CB  . ILE B 1 125 ? 17.753  -4.750  -14.358 1.00 21.81 ? 125 ILE B CB  1 
ATOM   3218 C CG1 . ILE B 1 125 ? 16.591  -4.048  -13.646 1.00 21.53 ? 125 ILE B CG1 1 
ATOM   3219 C CG2 . ILE B 1 125 ? 19.071  -4.496  -13.618 1.00 21.51 ? 125 ILE B CG2 1 
ATOM   3220 C CD1 . ILE B 1 125 ? 16.322  -4.538  -12.226 1.00 21.24 ? 125 ILE B CD1 1 
ATOM   3221 N N   . THR B 1 126 ? 19.985  -4.263  -16.997 1.00 22.07 ? 126 THR B N   1 
ATOM   3222 C CA  . THR B 1 126 ? 21.070  -4.819  -17.808 1.00 21.92 ? 126 THR B CA  1 
ATOM   3223 C C   . THR B 1 126 ? 22.420  -4.223  -17.382 1.00 21.96 ? 126 THR B C   1 
ATOM   3224 O O   . THR B 1 126 ? 22.458  -3.274  -16.587 1.00 21.63 ? 126 THR B O   1 
ATOM   3225 C CB  . THR B 1 126 ? 20.789  -4.599  -19.330 1.00 21.90 ? 126 THR B CB  1 
ATOM   3226 O OG1 . THR B 1 126 ? 21.546  -5.539  -20.109 1.00 21.88 ? 126 THR B OG1 1 
ATOM   3227 C CG2 . THR B 1 126 ? 21.151  -3.186  -19.758 1.00 21.43 ? 126 THR B CG2 1 
ATOM   3228 N N   . MET B 1 127 ? 23.517  -4.786  -17.895 1.00 22.10 ? 127 MET B N   1 
ATOM   3229 C CA  . MET B 1 127 ? 24.855  -4.276  -17.580 1.00 22.35 ? 127 MET B CA  1 
ATOM   3230 C C   . MET B 1 127 ? 25.697  -3.965  -18.819 1.00 22.64 ? 127 MET B C   1 
ATOM   3231 O O   . MET B 1 127 ? 25.900  -4.814  -19.691 1.00 22.47 ? 127 MET B O   1 
ATOM   3232 C CB  . MET B 1 127 ? 25.605  -5.235  -16.647 1.00 22.27 ? 127 MET B CB  1 
ATOM   3233 C CG  . MET B 1 127 ? 26.967  -4.706  -16.173 1.00 22.17 ? 127 MET B CG  1 
ATOM   3234 S SD  . MET B 1 127 ? 27.568  -5.484  -14.653 1.00 22.12 ? 127 MET B SD  1 
ATOM   3235 C CE  . MET B 1 127 ? 26.305  -4.956  -13.483 1.00 20.75 ? 127 MET B CE  1 
ATOM   3236 N N   . ASP B 1 128 ? 26.186  -2.730  -18.866 1.00 23.17 ? 128 ASP B N   1 
ATOM   3237 C CA  . ASP B 1 128 ? 27.117  -2.271  -19.894 1.00 23.81 ? 128 ASP B CA  1 
ATOM   3238 C C   . ASP B 1 128 ? 26.664  -2.572  -21.313 1.00 23.98 ? 128 ASP B C   1 
ATOM   3239 O O   . ASP B 1 128 ? 27.295  -3.353  -22.033 1.00 24.01 ? 128 ASP B O   1 
ATOM   3240 C CB  . ASP B 1 128 ? 28.530  -2.807  -19.635 1.00 23.93 ? 128 ASP B CB  1 
ATOM   3241 C CG  . ASP B 1 128 ? 29.227  -2.072  -18.508 1.00 24.72 ? 128 ASP B CG  1 
ATOM   3242 O OD1 . ASP B 1 128 ? 29.572  -2.729  -17.505 1.00 25.58 ? 128 ASP B OD1 1 
ATOM   3243 O OD2 . ASP B 1 128 ? 29.417  -0.840  -18.621 1.00 25.08 ? 128 ASP B OD2 1 
ATOM   3244 N N   . LEU B 1 129 ? 25.553  -1.944  -21.700 1.00 24.23 ? 129 LEU B N   1 
ATOM   3245 C CA  . LEU B 1 129 ? 25.066  -2.008  -23.069 1.00 24.47 ? 129 LEU B CA  1 
ATOM   3246 C C   . LEU B 1 129 ? 26.209  -1.706  -24.030 1.00 24.63 ? 129 LEU B C   1 
ATOM   3247 O O   . LEU B 1 129 ? 26.946  -0.733  -23.834 1.00 24.71 ? 129 LEU B O   1 
ATOM   3248 C CB  . LEU B 1 129 ? 23.929  -1.003  -23.268 1.00 24.49 ? 129 LEU B CB  1 
ATOM   3249 C CG  . LEU B 1 129 ? 22.597  -1.413  -22.636 1.00 24.85 ? 129 LEU B CG  1 
ATOM   3250 C CD1 . LEU B 1 129 ? 21.658  -0.227  -22.544 1.00 24.70 ? 129 LEU B CD1 1 
ATOM   3251 C CD2 . LEU B 1 129 ? 21.952  -2.572  -23.404 1.00 25.02 ? 129 LEU B CD2 1 
ATOM   3252 N N   . HIS B 1 130 ? 26.363  -2.553  -25.049 1.00 24.67 ? 130 HIS B N   1 
ATOM   3253 C CA  . HIS B 1 130 ? 27.410  -2.382  -26.048 1.00 24.86 ? 130 HIS B CA  1 
ATOM   3254 C C   . HIS B 1 130 ? 27.398  -0.968  -26.612 1.00 24.80 ? 130 HIS B C   1 
ATOM   3255 O O   . HIS B 1 130 ? 28.454  -0.395  -26.887 1.00 24.77 ? 130 HIS B O   1 
ATOM   3256 C CB  . HIS B 1 130 ? 27.272  -3.400  -27.179 1.00 25.17 ? 130 HIS B CB  1 
ATOM   3257 C CG  . HIS B 1 130 ? 28.297  -3.233  -28.257 1.00 25.64 ? 130 HIS B CG  1 
ATOM   3258 N ND1 . HIS B 1 130 ? 27.982  -2.759  -29.513 1.00 26.05 ? 130 HIS B ND1 1 
ATOM   3259 C CD2 . HIS B 1 130 ? 29.635  -3.445  -28.255 1.00 26.06 ? 130 HIS B CD2 1 
ATOM   3260 C CE1 . HIS B 1 130 ? 29.080  -2.707  -30.246 1.00 26.38 ? 130 HIS B CE1 1 
ATOM   3261 N NE2 . HIS B 1 130 ? 30.098  -3.117  -29.505 1.00 26.58 ? 130 HIS B NE2 1 
ATOM   3262 N N   . ALA B 1 131 ? 26.193  -0.431  -26.791 1.00 24.74 ? 131 ALA B N   1 
ATOM   3263 C CA  . ALA B 1 131 ? 25.992  0.989   -27.048 1.00 24.79 ? 131 ALA B CA  1 
ATOM   3264 C C   . ALA B 1 131 ? 24.819  1.480   -26.213 1.00 24.90 ? 131 ALA B C   1 
ATOM   3265 O O   . ALA B 1 131 ? 23.749  0.859   -26.207 1.00 25.08 ? 131 ALA B O   1 
ATOM   3266 C CB  . ALA B 1 131 ? 25.739  1.235   -28.515 1.00 24.83 ? 131 ALA B CB  1 
ATOM   3267 N N   . SER B 1 132 ? 25.032  2.592   -25.510 1.00 24.92 ? 132 SER B N   1 
ATOM   3268 C CA  . SER B 1 132 ? 24.025  3.191   -24.623 1.00 24.93 ? 132 SER B CA  1 
ATOM   3269 C C   . SER B 1 132 ? 22.705  3.467   -25.342 1.00 24.74 ? 132 SER B C   1 
ATOM   3270 O O   . SER B 1 132 ? 21.633  3.399   -24.738 1.00 25.00 ? 132 SER B O   1 
ATOM   3271 C CB  . SER B 1 132 ? 24.554  4.499   -24.030 1.00 25.02 ? 132 SER B CB  1 
ATOM   3272 O OG  . SER B 1 132 ? 25.892  4.321   -23.540 1.00 25.46 ? 132 SER B OG  1 
ATOM   3273 N N   . GLN B 1 133 ? 22.805  3.775   -26.634 1.00 24.34 ? 133 GLN B N   1 
ATOM   3274 C CA  . GLN B 1 133 ? 21.653  4.041   -27.498 1.00 24.10 ? 133 GLN B CA  1 
ATOM   3275 C C   . GLN B 1 133 ? 20.637  2.895   -27.538 1.00 23.73 ? 133 GLN B C   1 
ATOM   3276 O O   . GLN B 1 133 ? 19.471  3.107   -27.895 1.00 23.69 ? 133 GLN B O   1 
ATOM   3277 C CB  . GLN B 1 133 ? 22.121  4.363   -28.924 1.00 24.22 ? 133 GLN B CB  1 
ATOM   3278 C CG  . GLN B 1 133 ? 22.917  5.662   -29.055 1.00 24.86 ? 133 GLN B CG  1 
ATOM   3279 C CD  . GLN B 1 133 ? 24.395  5.509   -28.712 1.00 25.36 ? 133 GLN B CD  1 
ATOM   3280 O OE1 . GLN B 1 133 ? 24.811  4.553   -28.044 1.00 25.89 ? 133 GLN B OE1 1 
ATOM   3281 N NE2 . GLN B 1 133 ? 25.195  6.462   -29.166 1.00 25.03 ? 133 GLN B NE2 1 
ATOM   3282 N N   . ILE B 1 134 ? 21.071  1.689   -27.171 1.00 23.27 ? 134 ILE B N   1 
ATOM   3283 C CA  . ILE B 1 134 ? 20.156  0.546   -27.116 1.00 22.77 ? 134 ILE B CA  1 
ATOM   3284 C C   . ILE B 1 134 ? 19.007  0.788   -26.124 1.00 22.41 ? 134 ILE B C   1 
ATOM   3285 O O   . ILE B 1 134 ? 17.916  0.244   -26.303 1.00 22.63 ? 134 ILE B O   1 
ATOM   3286 C CB  . ILE B 1 134 ? 20.897  -0.806  -26.874 1.00 22.76 ? 134 ILE B CB  1 
ATOM   3287 C CG1 . ILE B 1 134 ? 21.678  -1.209  -28.137 1.00 22.39 ? 134 ILE B CG1 1 
ATOM   3288 C CG2 . ILE B 1 134 ? 19.915  -1.921  -26.509 1.00 22.46 ? 134 ILE B CG2 1 
ATOM   3289 C CD1 . ILE B 1 134 ? 22.720  -2.294  -27.915 1.00 21.82 ? 134 ILE B CD1 1 
ATOM   3290 N N   . GLN B 1 135 ? 19.240  1.621   -25.105 1.00 21.81 ? 135 GLN B N   1 
ATOM   3291 C CA  . GLN B 1 135 ? 18.166  2.034   -24.191 1.00 21.28 ? 135 GLN B CA  1 
ATOM   3292 C C   . GLN B 1 135 ? 16.999  2.604   -24.983 1.00 20.91 ? 135 GLN B C   1 
ATOM   3293 O O   . GLN B 1 135 ? 15.839  2.302   -24.695 1.00 20.93 ? 135 GLN B O   1 
ATOM   3294 C CB  . GLN B 1 135 ? 18.645  3.082   -23.183 1.00 21.35 ? 135 GLN B CB  1 
ATOM   3295 C CG  . GLN B 1 135 ? 19.455  2.544   -22.006 1.00 21.11 ? 135 GLN B CG  1 
ATOM   3296 C CD  . GLN B 1 135 ? 19.368  3.452   -20.782 1.00 20.93 ? 135 GLN B CD  1 
ATOM   3297 O OE1 . GLN B 1 135 ? 20.368  3.998   -20.323 1.00 21.49 ? 135 GLN B OE1 1 
ATOM   3298 N NE2 . GLN B 1 135 ? 18.161  3.623   -20.262 1.00 20.63 ? 135 GLN B NE2 1 
ATOM   3299 N N   . GLY B 1 136 ? 17.325  3.414   -25.992 1.00 20.41 ? 136 GLY B N   1 
ATOM   3300 C CA  . GLY B 1 136 ? 16.333  4.023   -26.876 1.00 19.70 ? 136 GLY B CA  1 
ATOM   3301 C C   . GLY B 1 136 ? 15.574  3.069   -27.786 1.00 19.23 ? 136 GLY B C   1 
ATOM   3302 O O   . GLY B 1 136 ? 14.638  3.480   -28.464 1.00 19.14 ? 136 GLY B O   1 
ATOM   3303 N N   . PHE B 1 137 ? 15.970  1.796   -27.815 1.00 18.85 ? 137 PHE B N   1 
ATOM   3304 C CA  . PHE B 1 137 ? 15.230  0.782   -28.571 1.00 18.37 ? 137 PHE B CA  1 
ATOM   3305 C C   . PHE B 1 137 ? 13.996  0.327   -27.799 1.00 18.41 ? 137 PHE B C   1 
ATOM   3306 O O   . PHE B 1 137 ? 13.246  -0.538  -28.255 1.00 18.47 ? 137 PHE B O   1 
ATOM   3307 C CB  . PHE B 1 137 ? 16.110  -0.428  -28.901 1.00 18.10 ? 137 PHE B CB  1 
ATOM   3308 C CG  . PHE B 1 137 ? 17.278  -0.118  -29.810 1.00 17.47 ? 137 PHE B CG  1 
ATOM   3309 C CD1 . PHE B 1 137 ? 17.404  1.116   -30.434 1.00 16.66 ? 137 PHE B CD1 1 
ATOM   3310 C CD2 . PHE B 1 137 ? 18.238  -1.091  -30.067 1.00 16.37 ? 137 PHE B CD2 1 
ATOM   3311 C CE1 . PHE B 1 137 ? 18.475  1.380   -31.265 1.00 16.50 ? 137 PHE B CE1 1 
ATOM   3312 C CE2 . PHE B 1 137 ? 19.306  -0.833  -30.899 1.00 15.38 ? 137 PHE B CE2 1 
ATOM   3313 C CZ  . PHE B 1 137 ? 19.426  0.402   -31.501 1.00 15.97 ? 137 PHE B CZ  1 
ATOM   3314 N N   . PHE B 1 138 ? 13.794  0.914   -26.624 1.00 18.39 ? 138 PHE B N   1 
ATOM   3315 C CA  . PHE B 1 138 ? 12.664  0.567   -25.781 1.00 18.51 ? 138 PHE B CA  1 
ATOM   3316 C C   . PHE B 1 138 ? 11.786  1.788   -25.561 1.00 18.95 ? 138 PHE B C   1 
ATOM   3317 O O   . PHE B 1 138 ? 12.227  2.924   -25.733 1.00 19.10 ? 138 PHE B O   1 
ATOM   3318 C CB  . PHE B 1 138 ? 13.151  0.075   -24.414 1.00 18.36 ? 138 PHE B CB  1 
ATOM   3319 C CG  . PHE B 1 138 ? 13.836  -1.257  -24.441 1.00 17.00 ? 138 PHE B CG  1 
ATOM   3320 C CD1 . PHE B 1 138 ? 15.221  -1.338  -24.547 1.00 16.88 ? 138 PHE B CD1 1 
ATOM   3321 C CD2 . PHE B 1 138 ? 13.101  -2.431  -24.335 1.00 16.01 ? 138 PHE B CD2 1 
ATOM   3322 C CE1 . PHE B 1 138 ? 15.863  -2.576  -24.556 1.00 16.39 ? 138 PHE B CE1 1 
ATOM   3323 C CE2 . PHE B 1 138 ? 13.723  -3.668  -24.337 1.00 14.92 ? 138 PHE B CE2 1 
ATOM   3324 C CZ  . PHE B 1 138 ? 15.111  -3.743  -24.449 1.00 15.82 ? 138 PHE B CZ  1 
ATOM   3325 N N   . ASP B 1 139 ? 10.537  1.546   -25.175 1.00 19.37 ? 139 ASP B N   1 
ATOM   3326 C CA  . ASP B 1 139 ? 9.719   2.605   -24.603 1.00 19.83 ? 139 ASP B CA  1 
ATOM   3327 C C   . ASP B 1 139 ? 9.506   2.361   -23.107 1.00 19.98 ? 139 ASP B C   1 
ATOM   3328 O O   . ASP B 1 139 ? 9.214   3.292   -22.351 1.00 20.24 ? 139 ASP B O   1 
ATOM   3329 C CB  . ASP B 1 139 ? 8.413   2.775   -25.377 1.00 19.93 ? 139 ASP B CB  1 
ATOM   3330 C CG  . ASP B 1 139 ? 8.627   3.459   -26.726 1.00 21.09 ? 139 ASP B CG  1 
ATOM   3331 O OD1 . ASP B 1 139 ? 9.187   4.581   -26.748 1.00 21.83 ? 139 ASP B OD1 1 
ATOM   3332 O OD2 . ASP B 1 139 ? 8.242   2.876   -27.766 1.00 22.50 ? 139 ASP B OD2 1 
ATOM   3333 N N   . ILE B 1 140 ? 9.684   1.110   -22.685 1.00 19.93 ? 140 ILE B N   1 
ATOM   3334 C CA  . ILE B 1 140 ? 9.762   0.775   -21.261 1.00 19.94 ? 140 ILE B CA  1 
ATOM   3335 C C   . ILE B 1 140 ? 11.068  1.360   -20.703 1.00 20.10 ? 140 ILE B C   1 
ATOM   3336 O O   . ILE B 1 140 ? 11.982  1.662   -21.484 1.00 20.33 ? 140 ILE B O   1 
ATOM   3337 C CB  . ILE B 1 140 ? 9.683   -0.759  -21.020 1.00 19.89 ? 140 ILE B CB  1 
ATOM   3338 C CG1 . ILE B 1 140 ? 10.849  -1.493  -21.719 1.00 19.61 ? 140 ILE B CG1 1 
ATOM   3339 C CG2 . ILE B 1 140 ? 8.284   -1.284  -21.417 1.00 19.54 ? 140 ILE B CG2 1 
ATOM   3340 C CD1 . ILE B 1 140 ? 10.525  -2.995  -22.017 1.00 18.88 ? 140 ILE B CD1 1 
ATOM   3341 N N   . PRO B 1 141 ? 11.149  1.564   -19.366 1.00 20.04 ? 141 PRO B N   1 
ATOM   3342 C CA  . PRO B 1 141 ? 12.420  1.985   -18.778 1.00 20.03 ? 141 PRO B CA  1 
ATOM   3343 C C   . PRO B 1 141 ? 13.479  0.882   -18.757 1.00 20.17 ? 141 PRO B C   1 
ATOM   3344 O O   . PRO B 1 141 ? 13.169  -0.294  -18.538 1.00 20.24 ? 141 PRO B O   1 
ATOM   3345 C CB  . PRO B 1 141 ? 12.034  2.376   -17.346 1.00 19.90 ? 141 PRO B CB  1 
ATOM   3346 C CG  . PRO B 1 141 ? 10.816  1.589   -17.052 1.00 20.07 ? 141 PRO B CG  1 
ATOM   3347 C CD  . PRO B 1 141 ? 10.073  1.484   -18.356 1.00 20.05 ? 141 PRO B CD  1 
ATOM   3348 N N   . VAL B 1 142 ? 14.726  1.286   -18.978 1.00 20.45 ? 142 VAL B N   1 
ATOM   3349 C CA  . VAL B 1 142 ? 15.880  0.400   -18.922 1.00 20.73 ? 142 VAL B CA  1 
ATOM   3350 C C   . VAL B 1 142 ? 16.882  0.991   -17.941 1.00 21.29 ? 142 VAL B C   1 
ATOM   3351 O O   . VAL B 1 142 ? 17.152  2.191   -17.975 1.00 21.42 ? 142 VAL B O   1 
ATOM   3352 C CB  . VAL B 1 142 ? 16.554  0.258   -20.309 1.00 20.47 ? 142 VAL B CB  1 
ATOM   3353 C CG1 . VAL B 1 142 ? 17.839  -0.551  -20.213 1.00 19.72 ? 142 VAL B CG1 1 
ATOM   3354 C CG2 . VAL B 1 142 ? 15.602  -0.381  -21.297 1.00 20.45 ? 142 VAL B CG2 1 
ATOM   3355 N N   . ASP B 1 143 ? 17.412  0.157   -17.054 1.00 21.96 ? 143 ASP B N   1 
ATOM   3356 C CA  . ASP B 1 143 ? 18.501  0.573   -16.184 1.00 22.71 ? 143 ASP B CA  1 
ATOM   3357 C C   . ASP B 1 143 ? 19.777  -0.089  -16.681 1.00 23.25 ? 143 ASP B C   1 
ATOM   3358 O O   . ASP B 1 143 ? 19.905  -1.324  -16.666 1.00 23.38 ? 143 ASP B O   1 
ATOM   3359 C CB  . ASP B 1 143 ? 18.224  0.210   -14.719 1.00 22.62 ? 143 ASP B CB  1 
ATOM   3360 C CG  . ASP B 1 143 ? 17.070  1.003   -14.127 1.00 22.71 ? 143 ASP B CG  1 
ATOM   3361 O OD1 . ASP B 1 143 ? 17.114  2.250   -14.165 1.00 22.41 ? 143 ASP B OD1 1 
ATOM   3362 O OD2 . ASP B 1 143 ? 16.117  0.375   -13.618 1.00 22.60 ? 143 ASP B OD2 1 
ATOM   3363 N N   . ASN B 1 144 ? 20.703  0.741   -17.154 1.00 23.79 ? 144 ASN B N   1 
ATOM   3364 C CA  . ASN B 1 144 ? 21.990  0.269   -17.627 1.00 24.28 ? 144 ASN B CA  1 
ATOM   3365 C C   . ASN B 1 144 ? 23.066  0.456   -16.567 1.00 24.73 ? 144 ASN B C   1 
ATOM   3366 O O   . ASN B 1 144 ? 23.682  1.521   -16.463 1.00 24.65 ? 144 ASN B O   1 
ATOM   3367 C CB  . ASN B 1 144 ? 22.381  0.969   -18.925 1.00 24.17 ? 144 ASN B CB  1 
ATOM   3368 C CG  . ASN B 1 144 ? 23.542  0.295   -19.616 1.00 24.34 ? 144 ASN B CG  1 
ATOM   3369 O OD1 . ASN B 1 144 ? 24.295  0.932   -20.354 1.00 24.75 ? 144 ASN B OD1 1 
ATOM   3370 N ND2 . ASN B 1 144 ? 23.697  -1.003  -19.383 1.00 24.17 ? 144 ASN B ND2 1 
ATOM   3371 N N   . LEU B 1 145 ? 23.270  -0.590  -15.773 1.00 25.43 ? 145 LEU B N   1 
ATOM   3372 C CA  . LEU B 1 145 ? 24.297  -0.597  -14.739 1.00 26.00 ? 145 LEU B CA  1 
ATOM   3373 C C   . LEU B 1 145 ? 25.690  -0.655  -15.360 1.00 26.71 ? 145 LEU B C   1 
ATOM   3374 O O   . LEU B 1 145 ? 25.881  -1.214  -16.445 1.00 26.92 ? 145 LEU B O   1 
ATOM   3375 C CB  . LEU B 1 145 ? 24.079  -1.771  -13.773 1.00 25.83 ? 145 LEU B CB  1 
ATOM   3376 C CG  . LEU B 1 145 ? 22.671  -1.947  -13.173 1.00 25.35 ? 145 LEU B CG  1 
ATOM   3377 C CD1 . LEU B 1 145 ? 22.554  -3.264  -12.422 1.00 24.80 ? 145 LEU B CD1 1 
ATOM   3378 C CD2 . LEU B 1 145 ? 22.274  -0.788  -12.270 1.00 25.02 ? 145 LEU B CD2 1 
ATOM   3379 N N   . TYR B 1 146 ? 26.652  -0.055  -14.667 1.00 27.54 ? 146 TYR B N   1 
ATOM   3380 C CA  . TYR B 1 146 ? 28.042  -0.012  -15.111 1.00 28.27 ? 146 TYR B CA  1 
ATOM   3381 C C   . TYR B 1 146 ? 28.871  -0.956  -14.249 1.00 28.52 ? 146 TYR B C   1 
ATOM   3382 O O   . TYR B 1 146 ? 28.708  -0.991  -13.029 1.00 28.51 ? 146 TYR B O   1 
ATOM   3383 C CB  . TYR B 1 146 ? 28.586  1.422   -14.992 1.00 28.48 ? 146 TYR B CB  1 
ATOM   3384 C CG  . TYR B 1 146 ? 28.085  2.389   -16.053 1.00 29.74 ? 146 TYR B CG  1 
ATOM   3385 C CD1 . TYR B 1 146 ? 26.716  2.518   -16.324 1.00 30.74 ? 146 TYR B CD1 1 
ATOM   3386 C CD2 . TYR B 1 146 ? 28.980  3.190   -16.773 1.00 31.23 ? 146 TYR B CD2 1 
ATOM   3387 C CE1 . TYR B 1 146 ? 26.250  3.401   -17.292 1.00 31.43 ? 146 TYR B CE1 1 
ATOM   3388 C CE2 . TYR B 1 146 ? 28.522  4.080   -17.745 1.00 32.04 ? 146 TYR B CE2 1 
ATOM   3389 C CZ  . TYR B 1 146 ? 27.153  4.179   -17.996 1.00 32.26 ? 146 TYR B CZ  1 
ATOM   3390 O OH  . TYR B 1 146 ? 26.686  5.055   -18.949 1.00 32.98 ? 146 TYR B OH  1 
ATOM   3391 N N   . ALA B 1 147 ? 29.745  -1.733  -14.884 1.00 28.98 ? 147 ALA B N   1 
ATOM   3392 C CA  . ALA B 1 147 ? 30.703  -2.556  -14.145 1.00 29.38 ? 147 ALA B CA  1 
ATOM   3393 C C   . ALA B 1 147 ? 31.886  -1.694  -13.695 1.00 29.69 ? 147 ALA B C   1 
ATOM   3394 O O   . ALA B 1 147 ? 32.593  -2.041  -12.746 1.00 29.76 ? 147 ALA B O   1 
ATOM   3395 C CB  . ALA B 1 147 ? 31.178  -3.736  -14.992 1.00 29.39 ? 147 ALA B CB  1 
ATOM   3396 N N   . GLU B 1 148 ? 32.069  -0.564  -14.379 1.00 30.02 ? 148 GLU B N   1 
ATOM   3397 C CA  . GLU B 1 148 ? 33.115  0.424   -14.091 1.00 30.36 ? 148 GLU B CA  1 
ATOM   3398 C C   . GLU B 1 148 ? 33.464  0.608   -12.603 1.00 30.58 ? 148 GLU B C   1 
ATOM   3399 O O   . GLU B 1 148 ? 34.621  0.424   -12.234 1.00 30.79 ? 148 GLU B O   1 
ATOM   3400 C CB  . GLU B 1 148 ? 32.761  1.768   -14.741 1.00 30.36 ? 148 GLU B CB  1 
ATOM   3401 C CG  . GLU B 1 148 ? 33.803  2.870   -14.580 1.00 30.49 ? 148 GLU B CG  1 
ATOM   3402 C CD  . GLU B 1 148 ? 33.363  4.167   -15.238 1.00 31.04 ? 148 GLU B CD  1 
ATOM   3403 O OE1 . GLU B 1 148 ? 32.399  4.131   -16.035 1.00 31.51 ? 148 GLU B OE1 1 
ATOM   3404 O OE2 . GLU B 1 148 ? 33.973  5.222   -14.960 1.00 31.29 ? 148 GLU B OE2 1 
ATOM   3405 N N   . PRO B 1 149 ? 32.479  0.966   -11.744 1.00 30.73 ? 149 PRO B N   1 
ATOM   3406 C CA  . PRO B 1 149 ? 32.840  1.139   -10.328 1.00 30.73 ? 149 PRO B CA  1 
ATOM   3407 C C   . PRO B 1 149 ? 33.609  -0.056  -9.753  1.00 30.66 ? 149 PRO B C   1 
ATOM   3408 O O   . PRO B 1 149 ? 34.628  0.133   -9.085  1.00 30.60 ? 149 PRO B O   1 
ATOM   3409 C CB  . PRO B 1 149 ? 31.483  1.295   -9.632  1.00 30.79 ? 149 PRO B CB  1 
ATOM   3410 C CG  . PRO B 1 149 ? 30.586  1.831   -10.680 1.00 30.68 ? 149 PRO B CG  1 
ATOM   3411 C CD  . PRO B 1 149 ? 31.044  1.232   -11.977 1.00 30.70 ? 149 PRO B CD  1 
ATOM   3412 N N   . ALA B 1 150 ? 33.125  -1.267  -10.028 1.00 30.73 ? 150 ALA B N   1 
ATOM   3413 C CA  . ALA B 1 150 ? 33.792  -2.503  -9.599  1.00 30.71 ? 150 ALA B CA  1 
ATOM   3414 C C   . ALA B 1 150 ? 35.099  -2.736  -10.356 1.00 30.61 ? 150 ALA B C   1 
ATOM   3415 O O   . ALA B 1 150 ? 36.019  -3.367  -9.837  1.00 30.67 ? 150 ALA B O   1 
ATOM   3416 C CB  . ALA B 1 150 ? 32.858  -3.700  -9.768  1.00 30.60 ? 150 ALA B CB  1 
ATOM   3417 N N   . VAL B 1 151 ? 35.165  -2.233  -11.587 1.00 30.50 ? 151 VAL B N   1 
ATOM   3418 C CA  . VAL B 1 151 ? 36.361  -2.349  -12.415 1.00 30.36 ? 151 VAL B CA  1 
ATOM   3419 C C   . VAL B 1 151 ? 37.429  -1.385  -11.893 1.00 30.37 ? 151 VAL B C   1 
ATOM   3420 O O   . VAL B 1 151 ? 38.565  -1.787  -11.647 1.00 30.35 ? 151 VAL B O   1 
ATOM   3421 C CB  . VAL B 1 151 ? 36.035  -2.106  -13.914 1.00 30.37 ? 151 VAL B CB  1 
ATOM   3422 C CG1 . VAL B 1 151 ? 37.313  -1.968  -14.753 1.00 30.13 ? 151 VAL B CG1 1 
ATOM   3423 C CG2 . VAL B 1 151 ? 35.140  -3.224  -14.451 1.00 29.84 ? 151 VAL B CG2 1 
ATOM   3424 N N   . LEU B 1 152 ? 37.045  -0.122  -11.722 1.00 30.37 ? 152 LEU B N   1 
ATOM   3425 C CA  . LEU B 1 152 ? 37.855  0.878   -11.021 1.00 30.47 ? 152 LEU B CA  1 
ATOM   3426 C C   . LEU B 1 152 ? 38.427  0.357   -9.701  1.00 30.53 ? 152 LEU B C   1 
ATOM   3427 O O   . LEU B 1 152 ? 39.586  0.607   -9.382  1.00 30.49 ? 152 LEU B O   1 
ATOM   3428 C CB  . LEU B 1 152 ? 37.015  2.139   -10.752 1.00 30.50 ? 152 LEU B CB  1 
ATOM   3429 C CG  . LEU B 1 152 ? 37.088  3.374   -11.661 1.00 30.27 ? 152 LEU B CG  1 
ATOM   3430 C CD1 . LEU B 1 152 ? 37.482  3.053   -13.102 1.00 29.84 ? 152 LEU B CD1 1 
ATOM   3431 C CD2 . LEU B 1 152 ? 35.761  4.134   -11.613 1.00 30.43 ? 152 LEU B CD2 1 
ATOM   3432 N N   . LYS B 1 153 ? 37.600  -0.362  -8.944  1.00 30.72 ? 153 LYS B N   1 
ATOM   3433 C CA  . LYS B 1 153 ? 37.987  -0.905  -7.646  1.00 30.80 ? 153 LYS B CA  1 
ATOM   3434 C C   . LYS B 1 153 ? 38.992  -2.034  -7.825  1.00 30.61 ? 153 LYS B C   1 
ATOM   3435 O O   . LYS B 1 153 ? 40.040  -2.043  -7.174  1.00 30.73 ? 153 LYS B O   1 
ATOM   3436 C CB  . LYS B 1 153 ? 36.748  -1.387  -6.884  1.00 31.04 ? 153 LYS B CB  1 
ATOM   3437 C CG  . LYS B 1 153 ? 37.017  -1.952  -5.489  1.00 31.79 ? 153 LYS B CG  1 
ATOM   3438 C CD  . LYS B 1 153 ? 35.699  -2.318  -4.807  1.00 33.12 ? 153 LYS B CD  1 
ATOM   3439 C CE  . LYS B 1 153 ? 35.915  -3.192  -3.574  1.00 34.20 ? 153 LYS B CE  1 
ATOM   3440 N NZ  . LYS B 1 153 ? 36.459  -2.428  -2.415  1.00 34.87 ? 153 LYS B NZ  1 
ATOM   3441 N N   . TRP B 1 154 ? 38.677  -2.972  -8.723  1.00 30.42 ? 154 TRP B N   1 
ATOM   3442 C CA  . TRP B 1 154 ? 39.576  -4.088  -9.013  1.00 30.22 ? 154 TRP B CA  1 
ATOM   3443 C C   . TRP B 1 154 ? 40.975  -3.597  -9.413  1.00 30.46 ? 154 TRP B C   1 
ATOM   3444 O O   . TRP B 1 154 ? 41.983  -4.169  -8.989  1.00 30.19 ? 154 TRP B O   1 
ATOM   3445 C CB  . TRP B 1 154 ? 38.987  -5.006  -10.096 1.00 29.92 ? 154 TRP B CB  1 
ATOM   3446 C CG  . TRP B 1 154 ? 39.762  -6.275  -10.234 1.00 28.76 ? 154 TRP B CG  1 
ATOM   3447 C CD1 . TRP B 1 154 ? 39.514  -7.459  -9.603  1.00 27.57 ? 154 TRP B CD1 1 
ATOM   3448 C CD2 . TRP B 1 154 ? 40.940  -6.480  -11.026 1.00 27.64 ? 154 TRP B CD2 1 
ATOM   3449 N NE1 . TRP B 1 154 ? 40.454  -8.394  -9.963  1.00 27.35 ? 154 TRP B NE1 1 
ATOM   3450 C CE2 . TRP B 1 154 ? 41.343  -7.819  -10.834 1.00 27.39 ? 154 TRP B CE2 1 
ATOM   3451 C CE3 . TRP B 1 154 ? 41.690  -5.661  -11.885 1.00 27.08 ? 154 TRP B CE3 1 
ATOM   3452 C CZ2 . TRP B 1 154 ? 42.466  -8.362  -11.467 1.00 27.25 ? 154 TRP B CZ2 1 
ATOM   3453 C CZ3 . TRP B 1 154 ? 42.804  -6.200  -12.514 1.00 26.40 ? 154 TRP B CZ3 1 
ATOM   3454 C CH2 . TRP B 1 154 ? 43.183  -7.538  -12.299 1.00 26.99 ? 154 TRP B CH2 1 
ATOM   3455 N N   . ILE B 1 155 ? 41.011  -2.534  -10.217 1.00 30.83 ? 155 ILE B N   1 
ATOM   3456 C CA  . ILE B 1 155 ? 42.249  -1.919  -10.705 1.00 31.31 ? 155 ILE B CA  1 
ATOM   3457 C C   . ILE B 1 155 ? 43.142  -1.389  -9.574  1.00 31.88 ? 155 ILE B C   1 
ATOM   3458 O O   . ILE B 1 155 ? 44.325  -1.735  -9.500  1.00 31.89 ? 155 ILE B O   1 
ATOM   3459 C CB  . ILE B 1 155 ? 41.940  -0.803  -11.745 1.00 31.16 ? 155 ILE B CB  1 
ATOM   3460 C CG1 . ILE B 1 155 ? 41.504  -1.427  -13.071 1.00 30.56 ? 155 ILE B CG1 1 
ATOM   3461 C CG2 . ILE B 1 155 ? 43.149  0.094   -11.980 1.00 31.19 ? 155 ILE B CG2 1 
ATOM   3462 C CD1 . ILE B 1 155 ? 40.749  -0.490  -13.981 1.00 29.72 ? 155 ILE B CD1 1 
ATOM   3463 N N   . ARG B 1 156 ? 42.565  -0.565  -8.699  1.00 32.62 ? 156 ARG B N   1 
ATOM   3464 C CA  . ARG B 1 156 ? 43.291  0.033   -7.575  1.00 33.30 ? 156 ARG B CA  1 
ATOM   3465 C C   . ARG B 1 156 ? 43.826  -0.994  -6.572  1.00 33.68 ? 156 ARG B C   1 
ATOM   3466 O O   . ARG B 1 156 ? 44.808  -0.726  -5.866  1.00 33.75 ? 156 ARG B O   1 
ATOM   3467 C CB  . ARG B 1 156 ? 42.412  1.053   -6.842  1.00 33.38 ? 156 ARG B CB  1 
ATOM   3468 C CG  . ARG B 1 156 ? 41.961  2.239   -7.686  1.00 34.03 ? 156 ARG B CG  1 
ATOM   3469 C CD  . ARG B 1 156 ? 41.366  3.332   -6.805  1.00 35.51 ? 156 ARG B CD  1 
ATOM   3470 N NE  . ARG B 1 156 ? 40.429  4.187   -7.531  1.00 36.42 ? 156 ARG B NE  1 
ATOM   3471 C CZ  . ARG B 1 156 ? 39.102  4.082   -7.460  1.00 37.55 ? 156 ARG B CZ  1 
ATOM   3472 N NH1 . ARG B 1 156 ? 38.535  3.158   -6.687  1.00 37.45 ? 156 ARG B NH1 1 
ATOM   3473 N NH2 . ARG B 1 156 ? 38.336  4.908   -8.164  1.00 37.97 ? 156 ARG B NH2 1 
ATOM   3474 N N   . GLU B 1 157 ? 43.182  -2.162  -6.519  1.00 34.06 ? 157 GLU B N   1 
ATOM   3475 C CA  . GLU B 1 157 ? 43.531  -3.203  -5.544  1.00 34.54 ? 157 GLU B CA  1 
ATOM   3476 C C   . GLU B 1 157 ? 44.456  -4.297  -6.084  1.00 34.70 ? 157 GLU B C   1 
ATOM   3477 O O   . GLU B 1 157 ? 45.144  -4.965  -5.308  1.00 34.83 ? 157 GLU B O   1 
ATOM   3478 C CB  . GLU B 1 157 ? 42.260  -3.852  -4.976  1.00 34.61 ? 157 GLU B CB  1 
ATOM   3479 C CG  . GLU B 1 157 ? 41.365  -2.894  -4.193  1.00 35.46 ? 157 GLU B CG  1 
ATOM   3480 C CD  . GLU B 1 157 ? 40.050  -3.533  -3.769  1.00 36.76 ? 157 GLU B CD  1 
ATOM   3481 O OE1 . GLU B 1 157 ? 39.854  -4.751  -4.013  1.00 36.99 ? 157 GLU B OE1 1 
ATOM   3482 O OE2 . GLU B 1 157 ? 39.206  -2.811  -3.186  1.00 37.55 ? 157 GLU B OE2 1 
ATOM   3483 N N   . ASN B 1 158 ? 44.477  -4.481  -7.401  1.00 34.95 ? 158 ASN B N   1 
ATOM   3484 C CA  . ASN B 1 158 ? 45.216  -5.600  -8.003  1.00 35.10 ? 158 ASN B CA  1 
ATOM   3485 C C   . ASN B 1 158 ? 46.386  -5.193  -8.894  1.00 35.16 ? 158 ASN B C   1 
ATOM   3486 O O   . ASN B 1 158 ? 47.210  -6.032  -9.267  1.00 35.20 ? 158 ASN B O   1 
ATOM   3487 C CB  . ASN B 1 158 ? 44.263  -6.527  -8.778  1.00 35.12 ? 158 ASN B CB  1 
ATOM   3488 C CG  . ASN B 1 158 ? 43.241  -7.178  -7.869  1.00 35.41 ? 158 ASN B CG  1 
ATOM   3489 O OD1 . ASN B 1 158 ? 43.468  -8.268  -7.342  1.00 35.71 ? 158 ASN B OD1 1 
ATOM   3490 N ND2 . ASN B 1 158 ? 42.110  -6.504  -7.667  1.00 35.84 ? 158 ASN B ND2 1 
ATOM   3491 N N   . ILE B 1 159 ? 46.450  -3.912  -9.243  1.00 35.22 ? 159 ILE B N   1 
ATOM   3492 C CA  . ILE B 1 159 ? 47.542  -3.402  -10.069 1.00 35.28 ? 159 ILE B CA  1 
ATOM   3493 C C   . ILE B 1 159 ? 48.272  -2.293  -9.310  1.00 35.21 ? 159 ILE B C   1 
ATOM   3494 O O   . ILE B 1 159 ? 47.804  -1.150  -9.233  1.00 35.09 ? 159 ILE B O   1 
ATOM   3495 C CB  . ILE B 1 159 ? 47.045  -2.941  -11.476 1.00 35.45 ? 159 ILE B CB  1 
ATOM   3496 C CG1 . ILE B 1 159 ? 46.448  -4.130  -12.243 1.00 35.60 ? 159 ILE B CG1 1 
ATOM   3497 C CG2 . ILE B 1 159 ? 48.179  -2.307  -12.290 1.00 35.18 ? 159 ILE B CG2 1 
ATOM   3498 C CD1 . ILE B 1 159 ? 45.570  -3.748  -13.423 1.00 35.99 ? 159 ILE B CD1 1 
ATOM   3499 N N   . SER B 1 160 ? 49.416  -2.661  -8.731  1.00 35.19 ? 160 SER B N   1 
ATOM   3500 C CA  . SER B 1 160 ? 50.243  -1.743  -7.950  1.00 35.02 ? 160 SER B CA  1 
ATOM   3501 C C   . SER B 1 160 ? 50.523  -0.429  -8.686  1.00 34.93 ? 160 SER B C   1 
ATOM   3502 O O   . SER B 1 160 ? 50.605  0.636   -8.067  1.00 34.88 ? 160 SER B O   1 
ATOM   3503 C CB  . SER B 1 160 ? 51.569  -2.423  -7.578  1.00 34.94 ? 160 SER B CB  1 
ATOM   3504 N N   . GLU B 1 161 ? 50.634  -0.516  -10.010 1.00 34.75 ? 161 GLU B N   1 
ATOM   3505 C CA  . GLU B 1 161 ? 51.110  0.581   -10.851 1.00 34.75 ? 161 GLU B CA  1 
ATOM   3506 C C   . GLU B 1 161 ? 49.979  1.433   -11.429 1.00 34.58 ? 161 GLU B C   1 
ATOM   3507 O O   . GLU B 1 161 ? 50.229  2.316   -12.258 1.00 34.67 ? 161 GLU B O   1 
ATOM   3508 C CB  . GLU B 1 161 ? 51.979  0.037   -12.004 1.00 34.78 ? 161 GLU B CB  1 
ATOM   3509 C CG  . GLU B 1 161 ? 52.940  -1.104  -11.627 1.00 35.38 ? 161 GLU B CG  1 
ATOM   3510 C CD  . GLU B 1 161 ? 52.257  -2.481  -11.560 1.00 36.73 ? 161 GLU B CD  1 
ATOM   3511 O OE1 . GLU B 1 161 ? 51.055  -2.552  -11.209 1.00 37.55 ? 161 GLU B OE1 1 
ATOM   3512 O OE2 . GLU B 1 161 ? 52.929  -3.509  -11.849 1.00 37.64 ? 161 GLU B OE2 1 
ATOM   3513 N N   . TRP B 1 162 ? 48.749  1.185   -10.977 1.00 34.28 ? 162 TRP B N   1 
ATOM   3514 C CA  . TRP B 1 162 ? 47.553  1.795   -11.571 1.00 34.04 ? 162 TRP B CA  1 
ATOM   3515 C C   . TRP B 1 162 ? 47.612  3.314   -11.734 1.00 34.14 ? 162 TRP B C   1 
ATOM   3516 O O   . TRP B 1 162 ? 46.948  3.872   -12.611 1.00 34.01 ? 162 TRP B O   1 
ATOM   3517 C CB  . TRP B 1 162 ? 46.282  1.384   -10.812 1.00 33.93 ? 162 TRP B CB  1 
ATOM   3518 C CG  . TRP B 1 162 ? 46.075  2.036   -9.466  1.00 33.19 ? 162 TRP B CG  1 
ATOM   3519 C CD1 . TRP B 1 162 ? 46.389  1.510   -8.248  1.00 32.70 ? 162 TRP B CD1 1 
ATOM   3520 C CD2 . TRP B 1 162 ? 45.479  3.317   -9.207  1.00 33.18 ? 162 TRP B CD2 1 
ATOM   3521 N NE1 . TRP B 1 162 ? 46.039  2.382   -7.246  1.00 32.85 ? 162 TRP B NE1 1 
ATOM   3522 C CE2 . TRP B 1 162 ? 45.479  3.501   -7.806  1.00 33.10 ? 162 TRP B CE2 1 
ATOM   3523 C CE3 . TRP B 1 162 ? 44.951  4.332   -10.025 1.00 33.44 ? 162 TRP B CE3 1 
ATOM   3524 C CZ2 . TRP B 1 162 ? 44.966  4.659   -7.197  1.00 33.05 ? 162 TRP B CZ2 1 
ATOM   3525 C CZ3 . TRP B 1 162 ? 44.449  5.488   -9.421  1.00 33.18 ? 162 TRP B CZ3 1 
ATOM   3526 C CH2 . TRP B 1 162 ? 44.461  5.639   -8.018  1.00 32.93 ? 162 TRP B CH2 1 
ATOM   3527 N N   . ARG B 1 163 ? 48.403  3.972   -10.889 1.00 34.22 ? 163 ARG B N   1 
ATOM   3528 C CA  . ARG B 1 163 ? 48.520  5.429   -10.916 1.00 34.28 ? 163 ARG B CA  1 
ATOM   3529 C C   . ARG B 1 163 ? 49.363  5.922   -12.087 1.00 34.24 ? 163 ARG B C   1 
ATOM   3530 O O   . ARG B 1 163 ? 49.422  7.125   -12.344 1.00 34.27 ? 163 ARG B O   1 
ATOM   3531 C CB  . ARG B 1 163 ? 49.079  5.955   -9.590  1.00 34.30 ? 163 ARG B CB  1 
ATOM   3532 C CG  . ARG B 1 163 ? 48.114  5.780   -8.422  1.00 34.72 ? 163 ARG B CG  1 
ATOM   3533 C CD  . ARG B 1 163 ? 48.710  6.328   -7.119  1.00 35.35 ? 163 ARG B CD  1 
ATOM   3534 N NE  . ARG B 1 163 ? 47.793  6.116   -5.999  1.00 36.37 ? 163 ARG B NE  1 
ATOM   3535 C CZ  . ARG B 1 163 ? 47.730  5.003   -5.268  1.00 37.05 ? 163 ARG B CZ  1 
ATOM   3536 N NH1 . ARG B 1 163 ? 48.536  3.975   -5.521  1.00 36.79 ? 163 ARG B NH1 1 
ATOM   3537 N NH2 . ARG B 1 163 ? 46.851  4.918   -4.276  1.00 37.59 ? 163 ARG B NH2 1 
ATOM   3538 N N   . ASN B 1 164 ? 50.003  4.991   -12.792 1.00 34.21 ? 164 ASN B N   1 
ATOM   3539 C CA  . ASN B 1 164 ? 50.851  5.319   -13.941 1.00 34.26 ? 164 ASN B CA  1 
ATOM   3540 C C   . ASN B 1 164 ? 50.555  4.472   -15.181 1.00 34.16 ? 164 ASN B C   1 
ATOM   3541 O O   . ASN B 1 164 ? 51.399  4.342   -16.075 1.00 34.27 ? 164 ASN B O   1 
ATOM   3542 C CB  . ASN B 1 164 ? 52.328  5.189   -13.564 1.00 34.37 ? 164 ASN B CB  1 
ATOM   3543 C CG  . ASN B 1 164 ? 52.802  6.329   -12.706 1.00 34.91 ? 164 ASN B CG  1 
ATOM   3544 O OD1 . ASN B 1 164 ? 53.402  7.281   -13.201 1.00 35.94 ? 164 ASN B OD1 1 
ATOM   3545 N ND2 . ASN B 1 164 ? 52.512  6.259   -11.414 1.00 35.34 ? 164 ASN B ND2 1 
ATOM   3546 N N   . CYS B 1 165 ? 49.355  3.901   -15.233 1.00 33.78 ? 165 CYS B N   1 
ATOM   3547 C CA  . CYS B 1 165 ? 48.998  3.013   -16.329 1.00 33.40 ? 165 CYS B CA  1 
ATOM   3548 C C   . CYS B 1 165 ? 48.365  3.777   -17.493 1.00 33.14 ? 165 CYS B C   1 
ATOM   3549 O O   . CYS B 1 165 ? 48.232  5.008   -17.451 1.00 33.16 ? 165 CYS B O   1 
ATOM   3550 C CB  . CYS B 1 165 ? 48.074  1.889   -15.834 1.00 33.27 ? 165 CYS B CB  1 
ATOM   3551 S SG  . CYS B 1 165 ? 46.388  2.396   -15.461 1.00 33.33 ? 165 CYS B SG  1 
ATOM   3552 N N   . THR B 1 166 ? 48.002  3.034   -18.536 1.00 32.84 ? 166 THR B N   1 
ATOM   3553 C CA  . THR B 1 166 ? 47.238  3.569   -19.645 1.00 32.46 ? 166 THR B CA  1 
ATOM   3554 C C   . THR B 1 166 ? 46.059  2.646   -19.914 1.00 32.27 ? 166 THR B C   1 
ATOM   3555 O O   . THR B 1 166 ? 46.222  1.431   -20.053 1.00 32.17 ? 166 THR B O   1 
ATOM   3556 C CB  . THR B 1 166 ? 48.082  3.704   -20.920 1.00 32.48 ? 166 THR B CB  1 
ATOM   3557 O OG1 . THR B 1 166 ? 49.209  4.548   -20.662 1.00 32.14 ? 166 THR B OG1 1 
ATOM   3558 C CG2 . THR B 1 166 ? 47.259  4.316   -22.041 1.00 32.56 ? 166 THR B CG2 1 
ATOM   3559 N N   . ILE B 1 167 ? 44.873  3.243   -19.959 1.00 32.12 ? 167 ILE B N   1 
ATOM   3560 C CA  . ILE B 1 167 ? 43.657  2.550   -20.355 1.00 31.93 ? 167 ILE B CA  1 
ATOM   3561 C C   . ILE B 1 167 ? 43.619  2.560   -21.879 1.00 31.93 ? 167 ILE B C   1 
ATOM   3562 O O   . ILE B 1 167 ? 43.702  3.616   -22.511 1.00 31.71 ? 167 ILE B O   1 
ATOM   3563 C CB  . ILE B 1 167 ? 42.394  3.234   -19.766 1.00 31.79 ? 167 ILE B CB  1 
ATOM   3564 C CG1 . ILE B 1 167 ? 42.623  3.666   -18.304 1.00 31.51 ? 167 ILE B CG1 1 
ATOM   3565 C CG2 . ILE B 1 167 ? 41.171  2.333   -19.903 1.00 31.56 ? 167 ILE B CG2 1 
ATOM   3566 C CD1 . ILE B 1 167 ? 42.919  2.526   -17.314 1.00 30.92 ? 167 ILE B CD1 1 
ATOM   3567 N N   . VAL B 1 168 ? 43.528  1.375   -22.472 1.00 32.11 ? 168 VAL B N   1 
ATOM   3568 C CA  . VAL B 1 168 ? 43.579  1.255   -23.926 1.00 32.34 ? 168 VAL B CA  1 
ATOM   3569 C C   . VAL B 1 168 ? 42.248  0.722   -24.463 1.00 32.63 ? 168 VAL B C   1 
ATOM   3570 O O   . VAL B 1 168 ? 41.675  -0.214  -23.900 1.00 32.67 ? 168 VAL B O   1 
ATOM   3571 C CB  . VAL B 1 168 ? 44.753  0.341   -24.382 1.00 32.19 ? 168 VAL B CB  1 
ATOM   3572 C CG1 . VAL B 1 168 ? 44.932  0.394   -25.893 1.00 32.16 ? 168 VAL B CG1 1 
ATOM   3573 C CG2 . VAL B 1 168 ? 46.053  0.740   -23.699 1.00 32.03 ? 168 VAL B CG2 1 
ATOM   3574 N N   . SER B 1 169 ? 41.750  1.329   -25.538 1.00 32.95 ? 169 SER B N   1 
ATOM   3575 C CA  . SER B 1 169 ? 40.593  0.780   -26.243 1.00 33.32 ? 169 SER B CA  1 
ATOM   3576 C C   . SER B 1 169 ? 41.080  -0.080  -27.399 1.00 33.59 ? 169 SER B C   1 
ATOM   3577 O O   . SER B 1 169 ? 41.864  0.389   -28.223 1.00 33.62 ? 169 SER B O   1 
ATOM   3578 C CB  . SER B 1 169 ? 39.677  1.889   -26.767 1.00 33.30 ? 169 SER B CB  1 
ATOM   3579 O OG  . SER B 1 169 ? 38.518  1.349   -27.377 1.00 32.89 ? 169 SER B OG  1 
ATOM   3580 N N   . PRO B 1 170 ? 40.628  -1.346  -27.457 1.00 33.92 ? 170 PRO B N   1 
ATOM   3581 C CA  . PRO B 1 170 ? 41.003  -2.242  -28.548 1.00 34.17 ? 170 PRO B CA  1 
ATOM   3582 C C   . PRO B 1 170 ? 40.402  -1.840  -29.894 1.00 34.45 ? 170 PRO B C   1 
ATOM   3583 O O   . PRO B 1 170 ? 40.892  -2.283  -30.931 1.00 34.56 ? 170 PRO B O   1 
ATOM   3584 C CB  . PRO B 1 170 ? 40.457  -3.599  -28.095 1.00 34.11 ? 170 PRO B CB  1 
ATOM   3585 C CG  . PRO B 1 170 ? 39.356  -3.278  -27.170 1.00 34.04 ? 170 PRO B CG  1 
ATOM   3586 C CD  . PRO B 1 170 ? 39.752  -2.014  -26.476 1.00 34.09 ? 170 PRO B CD  1 
ATOM   3587 N N   . ASP B 1 171 ? 39.357  -1.011  -29.873 1.00 34.85 ? 171 ASP B N   1 
ATOM   3588 C CA  . ASP B 1 171 ? 38.726  -0.520  -31.108 1.00 35.18 ? 171 ASP B CA  1 
ATOM   3589 C C   . ASP B 1 171 ? 38.387  0.971   -31.047 1.00 35.56 ? 171 ASP B C   1 
ATOM   3590 O O   . ASP B 1 171 ? 38.449  1.586   -29.981 1.00 35.71 ? 171 ASP B O   1 
ATOM   3591 C CB  . ASP B 1 171 ? 37.482  -1.354  -31.468 1.00 35.04 ? 171 ASP B CB  1 
ATOM   3592 C CG  . ASP B 1 171 ? 36.469  -1.443  -30.330 1.00 34.69 ? 171 ASP B CG  1 
ATOM   3593 O OD1 . ASP B 1 171 ? 36.207  -0.422  -29.658 1.00 33.53 ? 171 ASP B OD1 1 
ATOM   3594 O OD2 . ASP B 1 171 ? 35.920  -2.547  -30.119 1.00 35.10 ? 171 ASP B OD2 1 
ATOM   3595 N N   . ALA B 1 172 ? 38.026  1.536   -32.198 1.00 36.00 ? 172 ALA B N   1 
ATOM   3596 C CA  . ALA B 1 172 ? 37.714  2.964   -32.322 1.00 36.26 ? 172 ALA B CA  1 
ATOM   3597 C C   . ALA B 1 172 ? 36.384  3.337   -31.670 1.00 36.45 ? 172 ALA B C   1 
ATOM   3598 O O   . ALA B 1 172 ? 36.196  4.479   -31.239 1.00 36.51 ? 172 ALA B O   1 
ATOM   3599 C CB  . ALA B 1 172 ? 37.720  3.380   -33.787 1.00 36.36 ? 172 ALA B CB  1 
ATOM   3600 N N   . GLY B 1 173 ? 35.468  2.373   -31.601 1.00 36.62 ? 173 GLY B N   1 
ATOM   3601 C CA  . GLY B 1 173 ? 34.162  2.588   -30.976 1.00 36.76 ? 173 GLY B CA  1 
ATOM   3602 C C   . GLY B 1 173 ? 34.201  2.695   -29.459 1.00 36.86 ? 173 GLY B C   1 
ATOM   3603 O O   . GLY B 1 173 ? 33.311  3.298   -28.854 1.00 37.00 ? 173 GLY B O   1 
ATOM   3604 N N   . GLY B 1 174 ? 35.232  2.117   -28.843 1.00 36.83 ? 174 GLY B N   1 
ATOM   3605 C CA  . GLY B 1 174 ? 35.333  2.073   -27.386 1.00 36.87 ? 174 GLY B CA  1 
ATOM   3606 C C   . GLY B 1 174 ? 36.067  3.237   -26.738 1.00 36.95 ? 174 GLY B C   1 
ATOM   3607 O O   . GLY B 1 174 ? 36.362  3.199   -25.540 1.00 36.98 ? 174 GLY B O   1 
ATOM   3608 N N   . ALA B 1 175 ? 36.353  4.276   -27.520 1.00 36.96 ? 175 ALA B N   1 
ATOM   3609 C CA  . ALA B 1 175 ? 37.127  5.421   -27.037 1.00 37.14 ? 175 ALA B CA  1 
ATOM   3610 C C   . ALA B 1 175 ? 36.500  6.111   -25.826 1.00 37.32 ? 175 ALA B C   1 
ATOM   3611 O O   . ALA B 1 175 ? 37.190  6.372   -24.839 1.00 37.35 ? 175 ALA B O   1 
ATOM   3612 C CB  . ALA B 1 175 ? 37.367  6.423   -28.164 1.00 37.19 ? 175 ALA B CB  1 
ATOM   3613 N N   . LYS B 1 176 ? 35.195  6.389   -25.904 1.00 37.51 ? 176 LYS B N   1 
ATOM   3614 C CA  . LYS B 1 176 ? 34.477  7.106   -24.839 1.00 37.54 ? 176 LYS B CA  1 
ATOM   3615 C C   . LYS B 1 176 ? 34.557  6.386   -23.493 1.00 37.58 ? 176 LYS B C   1 
ATOM   3616 O O   . LYS B 1 176 ? 34.793  7.016   -22.461 1.00 37.59 ? 176 LYS B O   1 
ATOM   3617 C CB  . LYS B 1 176 ? 33.011  7.337   -25.232 1.00 37.56 ? 176 LYS B CB  1 
ATOM   3618 N N   . ARG B 1 177 ? 34.372  5.068   -23.519 1.00 37.68 ? 177 ARG B N   1 
ATOM   3619 C CA  . ARG B 1 177 ? 34.456  4.237   -22.316 1.00 37.81 ? 177 ARG B CA  1 
ATOM   3620 C C   . ARG B 1 177 ? 35.823  4.357   -21.633 1.00 37.64 ? 177 ARG B C   1 
ATOM   3621 O O   . ARG B 1 177 ? 35.907  4.709   -20.448 1.00 37.68 ? 177 ARG B O   1 
ATOM   3622 C CB  . ARG B 1 177 ? 34.150  2.774   -22.647 1.00 37.80 ? 177 ARG B CB  1 
ATOM   3623 C CG  . ARG B 1 177 ? 33.633  1.971   -21.460 1.00 38.74 ? 177 ARG B CG  1 
ATOM   3624 C CD  . ARG B 1 177 ? 33.545  0.475   -21.758 1.00 39.95 ? 177 ARG B CD  1 
ATOM   3625 N NE  . ARG B 1 177 ? 32.554  0.156   -22.789 1.00 41.06 ? 177 ARG B NE  1 
ATOM   3626 C CZ  . ARG B 1 177 ? 32.846  -0.191  -24.044 1.00 41.76 ? 177 ARG B CZ  1 
ATOM   3627 N NH1 . ARG B 1 177 ? 34.111  -0.269  -24.451 1.00 41.89 ? 177 ARG B NH1 1 
ATOM   3628 N NH2 . ARG B 1 177 ? 31.867  -0.461  -24.900 1.00 41.98 ? 177 ARG B NH2 1 
ATOM   3629 N N   . VAL B 1 178 ? 36.889  4.087   -22.388 1.00 37.43 ? 178 VAL B N   1 
ATOM   3630 C CA  . VAL B 1 178 ? 38.249  4.108   -21.841 1.00 37.21 ? 178 VAL B CA  1 
ATOM   3631 C C   . VAL B 1 178 ? 38.656  5.513   -21.402 1.00 37.11 ? 178 VAL B C   1 
ATOM   3632 O O   . VAL B 1 178 ? 39.366  5.676   -20.411 1.00 37.02 ? 178 VAL B O   1 
ATOM   3633 C CB  . VAL B 1 178 ? 39.299  3.478   -22.812 1.00 37.09 ? 178 VAL B CB  1 
ATOM   3634 C CG1 . VAL B 1 178 ? 38.710  2.225   -23.476 1.00 36.94 ? 178 VAL B CG1 1 
ATOM   3635 C CG2 . VAL B 1 178 ? 39.785  4.492   -23.864 1.00 37.01 ? 178 VAL B CG2 1 
ATOM   3636 N N   . THR B 1 179 ? 38.177  6.516   -22.134 1.00 37.22 ? 179 THR B N   1 
ATOM   3637 C CA  . THR B 1 179 ? 38.454  7.920   -21.820 1.00 37.31 ? 179 THR B CA  1 
ATOM   3638 C C   . THR B 1 179 ? 37.754  8.344   -20.517 1.00 37.36 ? 179 THR B C   1 
ATOM   3639 O O   . THR B 1 179 ? 38.320  9.090   -19.717 1.00 37.25 ? 179 THR B O   1 
ATOM   3640 C CB  . THR B 1 179 ? 38.097  8.840   -23.025 1.00 37.28 ? 179 THR B CB  1 
ATOM   3641 O OG1 . THR B 1 179 ? 39.155  9.781   -23.245 1.00 37.42 ? 179 THR B OG1 1 
ATOM   3642 C CG2 . THR B 1 179 ? 36.773  9.573   -22.827 1.00 37.14 ? 179 THR B CG2 1 
ATOM   3643 N N   . SER B 1 180 ? 36.539  7.838   -20.307 1.00 37.50 ? 180 SER B N   1 
ATOM   3644 C CA  . SER B 1 180 ? 35.785  8.074   -19.073 1.00 37.68 ? 180 SER B CA  1 
ATOM   3645 C C   . SER B 1 180 ? 36.446  7.422   -17.849 1.00 37.68 ? 180 SER B C   1 
ATOM   3646 O O   . SER B 1 180 ? 36.398  7.974   -16.746 1.00 37.69 ? 180 SER B O   1 
ATOM   3647 C CB  . SER B 1 180 ? 34.332  7.597   -19.239 1.00 37.66 ? 180 SER B CB  1 
ATOM   3648 O OG  . SER B 1 180 ? 33.779  7.216   -17.949 1.00 38.31 ? 180 SER B OG  1 
ATOM   3649 N N   . ILE B 1 181 ? 37.055  6.254   -18.059 1.00 37.67 ? 181 ILE B N   1 
ATOM   3650 C CA  . ILE B 1 181 ? 37.783  5.529   -17.011 1.00 37.62 ? 181 ILE B CA  1 
ATOM   3651 C C   . ILE B 1 181 ? 39.159  6.154   -16.737 1.00 37.65 ? 181 ILE B C   1 
ATOM   3652 O O   . ILE B 1 181 ? 39.582  6.249   -15.581 1.00 37.64 ? 181 ILE B O   1 
ATOM   3653 C CB  . ILE B 1 181 ? 37.929  4.016   -17.359 1.00 37.63 ? 181 ILE B CB  1 
ATOM   3654 C CG1 . ILE B 1 181 ? 36.551  3.331   -17.362 1.00 37.47 ? 181 ILE B CG1 1 
ATOM   3655 C CG2 . ILE B 1 181 ? 38.887  3.312   -16.392 1.00 37.53 ? 181 ILE B CG2 1 
ATOM   3656 C CD1 . ILE B 1 181 ? 36.590  1.838   -17.658 1.00 37.02 ? 181 ILE B CD1 1 
ATOM   3657 N N   . ALA B 1 182 ? 39.839  6.582   -17.801 1.00 37.63 ? 182 ALA B N   1 
ATOM   3658 C CA  . ALA B 1 182 ? 41.179  7.167   -17.702 1.00 37.62 ? 182 ALA B CA  1 
ATOM   3659 C C   . ALA B 1 182 ? 41.200  8.490   -16.941 1.00 37.65 ? 182 ALA B C   1 
ATOM   3660 O O   . ALA B 1 182 ? 42.176  8.798   -16.245 1.00 37.67 ? 182 ALA B O   1 
ATOM   3661 C CB  . ALA B 1 182 ? 41.788  7.345   -19.086 1.00 37.66 ? 182 ALA B CB  1 
ATOM   3662 N N   . ASP B 1 183 ? 40.128  9.269   -17.078 1.00 37.77 ? 183 ASP B N   1 
ATOM   3663 C CA  . ASP B 1 183 ? 40.012  10.541  -16.368 1.00 37.82 ? 183 ASP B CA  1 
ATOM   3664 C C   . ASP B 1 183 ? 39.737  10.337  -14.881 1.00 37.90 ? 183 ASP B C   1 
ATOM   3665 O O   . ASP B 1 183 ? 40.334  11.013  -14.036 1.00 37.92 ? 183 ASP B O   1 
ATOM   3666 C CB  . ASP B 1 183 ? 38.941  11.434  -17.003 1.00 37.71 ? 183 ASP B CB  1 
ATOM   3667 C CG  . ASP B 1 183 ? 39.318  11.909  -18.399 1.00 37.45 ? 183 ASP B CG  1 
ATOM   3668 O OD1 . ASP B 1 183 ? 40.518  11.895  -18.761 1.00 36.90 ? 183 ASP B OD1 1 
ATOM   3669 O OD2 . ASP B 1 183 ? 38.397  12.309  -19.140 1.00 37.56 ? 183 ASP B OD2 1 
ATOM   3670 N N   . ARG B 1 184 ? 38.835  9.410   -14.566 1.00 37.96 ? 184 ARG B N   1 
ATOM   3671 C CA  . ARG B 1 184 ? 38.550  9.065   -13.175 1.00 38.13 ? 184 ARG B CA  1 
ATOM   3672 C C   . ARG B 1 184 ? 39.840  8.715   -12.439 1.00 37.81 ? 184 ARG B C   1 
ATOM   3673 O O   . ARG B 1 184 ? 40.204  9.383   -11.469 1.00 37.87 ? 184 ARG B O   1 
ATOM   3674 C CB  . ARG B 1 184 ? 37.546  7.912   -13.092 1.00 38.32 ? 184 ARG B CB  1 
ATOM   3675 C CG  . ARG B 1 184 ? 36.086  8.342   -13.169 1.00 39.77 ? 184 ARG B CG  1 
ATOM   3676 C CD  . ARG B 1 184 ? 35.550  8.758   -11.801 1.00 42.18 ? 184 ARG B CD  1 
ATOM   3677 N NE  . ARG B 1 184 ? 34.088  8.819   -11.784 1.00 43.95 ? 184 ARG B NE  1 
ATOM   3678 C CZ  . ARG B 1 184 ? 33.345  8.924   -10.682 1.00 45.03 ? 184 ARG B CZ  1 
ATOM   3679 N NH1 . ARG B 1 184 ? 33.914  8.980   -9.482  1.00 45.19 ? 184 ARG B NH1 1 
ATOM   3680 N NH2 . ARG B 1 184 ? 32.023  8.970   -10.782 1.00 45.65 ? 184 ARG B NH2 1 
ATOM   3681 N N   . LEU B 1 185 ? 40.534  7.690   -12.936 1.00 37.45 ? 185 LEU B N   1 
ATOM   3682 C CA  . LEU B 1 185 ? 41.813  7.231   -12.390 1.00 37.06 ? 185 LEU B CA  1 
ATOM   3683 C C   . LEU B 1 185 ? 42.922  8.283   -12.466 1.00 36.85 ? 185 LEU B C   1 
ATOM   3684 O O   . LEU B 1 185 ? 43.892  8.222   -11.705 1.00 36.76 ? 185 LEU B O   1 
ATOM   3685 C CB  . LEU B 1 185 ? 42.260  5.959   -13.123 1.00 37.04 ? 185 LEU B CB  1 
ATOM   3686 C CG  . LEU B 1 185 ? 42.106  4.567   -12.456 1.00 36.78 ? 185 LEU B CG  1 
ATOM   3687 C CD1 . LEU B 1 185 ? 40.832  4.430   -11.597 1.00 36.44 ? 185 LEU B CD1 1 
ATOM   3688 C CD2 . LEU B 1 185 ? 42.153  3.494   -13.543 1.00 36.49 ? 185 LEU B CD2 1 
ATOM   3689 N N   . ASN B 1 186 ? 42.765  9.238   -13.386 1.00 36.51 ? 186 ASN B N   1 
ATOM   3690 C CA  . ASN B 1 186 ? 43.752  10.292  -13.630 1.00 36.25 ? 186 ASN B CA  1 
ATOM   3691 C C   . ASN B 1 186 ? 45.018  9.732   -14.296 1.00 35.93 ? 186 ASN B C   1 
ATOM   3692 O O   . ASN B 1 186 ? 46.141  9.909   -13.805 1.00 35.87 ? 186 ASN B O   1 
ATOM   3693 C CB  . ASN B 1 186 ? 44.059  11.077  -12.342 1.00 36.31 ? 186 ASN B CB  1 
ATOM   3694 C CG  . ASN B 1 186 ? 44.845  12.354  -12.598 1.00 36.87 ? 186 ASN B CG  1 
ATOM   3695 O OD1 . ASN B 1 186 ? 45.555  12.836  -11.710 1.00 37.60 ? 186 ASN B OD1 1 
ATOM   3696 N ND2 . ASN B 1 186 ? 44.724  12.906  -13.812 1.00 37.49 ? 186 ASN B ND2 1 
ATOM   3697 N N   . VAL B 1 187 ? 44.810  9.047   -15.423 1.00 35.43 ? 187 VAL B N   1 
ATOM   3698 C CA  . VAL B 1 187 ? 45.900  8.425   -16.179 1.00 34.85 ? 187 VAL B CA  1 
ATOM   3699 C C   . VAL B 1 187 ? 45.743  8.675   -17.679 1.00 34.57 ? 187 VAL B C   1 
ATOM   3700 O O   . VAL B 1 187 ? 44.817  9.372   -18.098 1.00 34.47 ? 187 VAL B O   1 
ATOM   3701 C CB  . VAL B 1 187 ? 46.019  6.891   -15.893 1.00 34.88 ? 187 VAL B CB  1 
ATOM   3702 C CG1 . VAL B 1 187 ? 46.490  6.631   -14.458 1.00 34.30 ? 187 VAL B CG1 1 
ATOM   3703 C CG2 . VAL B 1 187 ? 44.703  6.168   -16.188 1.00 34.36 ? 187 VAL B CG2 1 
ATOM   3704 N N   . ASP B 1 188 ? 46.656  8.109   -18.480 1.00 34.40 ? 188 ASP B N   1 
ATOM   3705 C CA  . ASP B 1 188 ? 46.591  8.254   -19.935 1.00 34.26 ? 188 ASP B CA  1 
ATOM   3706 C C   . ASP B 1 188 ? 45.588  7.279   -20.537 1.00 34.14 ? 188 ASP B C   1 
ATOM   3707 O O   . ASP B 1 188 ? 45.234  6.274   -19.922 1.00 34.08 ? 188 ASP B O   1 
ATOM   3708 C CB  . ASP B 1 188 ? 47.969  8.003   -20.566 1.00 34.29 ? 188 ASP B CB  1 
ATOM   3709 C CG  . ASP B 1 188 ? 48.999  9.048   -20.180 1.00 34.26 ? 188 ASP B CG  1 
ATOM   3710 O OD1 . ASP B 1 188 ? 50.199  8.791   -20.401 1.00 34.61 ? 188 ASP B OD1 1 
ATOM   3711 O OD2 . ASP B 1 188 ? 48.625  10.122  -19.664 1.00 34.25 ? 188 ASP B OD2 1 
ATOM   3712 N N   . PHE B 1 189 ? 45.131  7.593   -21.745 1.00 34.12 ? 189 PHE B N   1 
ATOM   3713 C CA  . PHE B 1 189 ? 44.393  6.640   -22.562 1.00 34.18 ? 189 PHE B CA  1 
ATOM   3714 C C   . PHE B 1 189 ? 45.138  6.382   -23.874 1.00 34.19 ? 189 PHE B C   1 
ATOM   3715 O O   . PHE B 1 189 ? 46.080  7.104   -24.211 1.00 33.89 ? 189 PHE B O   1 
ATOM   3716 C CB  . PHE B 1 189 ? 42.950  7.107   -22.805 1.00 34.20 ? 189 PHE B CB  1 
ATOM   3717 C CG  . PHE B 1 189 ? 42.827  8.273   -23.754 1.00 34.13 ? 189 PHE B CG  1 
ATOM   3718 C CD1 . PHE B 1 189 ? 42.609  8.061   -25.115 1.00 34.20 ? 189 PHE B CD1 1 
ATOM   3719 C CD2 . PHE B 1 189 ? 42.910  9.580   -23.286 1.00 34.12 ? 189 PHE B CD2 1 
ATOM   3720 C CE1 . PHE B 1 189 ? 42.491  9.135   -25.996 1.00 34.12 ? 189 PHE B CE1 1 
ATOM   3721 C CE2 . PHE B 1 189 ? 42.792  10.658  -24.158 1.00 34.15 ? 189 PHE B CE2 1 
ATOM   3722 C CZ  . PHE B 1 189 ? 42.581  10.435  -25.516 1.00 34.13 ? 189 PHE B CZ  1 
ATOM   3723 N N   . ALA B 1 190 ? 44.724  5.340   -24.593 1.00 34.49 ? 190 ALA B N   1 
ATOM   3724 C CA  . ALA B 1 190 ? 45.276  5.011   -25.909 1.00 34.88 ? 190 ALA B CA  1 
ATOM   3725 C C   . ALA B 1 190 ? 44.290  4.180   -26.728 1.00 35.18 ? 190 ALA B C   1 
ATOM   3726 O O   . ALA B 1 190 ? 43.617  3.301   -26.192 1.00 35.28 ? 190 ALA B O   1 
ATOM   3727 C CB  . ALA B 1 190 ? 46.609  4.288   -25.781 1.00 34.73 ? 190 ALA B CB  1 
ATOM   3728 N N   . LEU B 1 191 ? 44.199  4.471   -28.024 1.00 35.60 ? 191 LEU B N   1 
ATOM   3729 C CA  . LEU B 1 191 ? 43.256  3.778   -28.895 1.00 36.06 ? 191 LEU B CA  1 
ATOM   3730 C C   . LEU B 1 191 ? 43.937  2.922   -29.938 1.00 36.35 ? 191 LEU B C   1 
ATOM   3731 O O   . LEU B 1 191 ? 44.914  3.335   -30.562 1.00 36.21 ? 191 LEU B O   1 
ATOM   3732 C CB  . LEU B 1 191 ? 42.309  4.757   -29.604 1.00 36.09 ? 191 LEU B CB  1 
ATOM   3733 C CG  . LEU B 1 191 ? 41.152  5.422   -28.856 1.00 36.20 ? 191 LEU B CG  1 
ATOM   3734 C CD1 . LEU B 1 191 ? 40.749  4.607   -27.643 1.00 36.54 ? 191 LEU B CD1 1 
ATOM   3735 C CD2 . LEU B 1 191 ? 41.527  6.831   -28.447 1.00 36.16 ? 191 LEU B CD2 1 
ATOM   3736 N N   . ILE B 1 192 ? 43.392  1.729   -30.132 1.00 36.99 ? 192 ILE B N   1 
ATOM   3737 C CA  . ILE B 1 192 ? 43.805  0.858   -31.219 1.00 37.78 ? 192 ILE B CA  1 
ATOM   3738 C C   . ILE B 1 192 ? 42.716  0.871   -32.293 1.00 38.31 ? 192 ILE B C   1 
ATOM   3739 O O   . ILE B 1 192 ? 41.534  1.061   -31.992 1.00 38.42 ? 192 ILE B O   1 
ATOM   3740 C CB  . ILE B 1 192 ? 44.116  -0.572  -30.704 1.00 37.80 ? 192 ILE B CB  1 
ATOM   3741 C CG1 . ILE B 1 192 ? 45.335  -0.520  -29.769 1.00 37.78 ? 192 ILE B CG1 1 
ATOM   3742 C CG2 . ILE B 1 192 ? 44.326  -1.543  -31.861 1.00 37.64 ? 192 ILE B CG2 1 
ATOM   3743 C CD1 . ILE B 1 192 ? 46.015  -1.844  -29.508 1.00 37.67 ? 192 ILE B CD1 1 
ATOM   3744 N N   . HIS B 1 193 ? 43.129  0.697   -33.545 1.00 39.06 ? 193 HIS B N   1 
ATOM   3745 C CA  . HIS B 1 193 ? 42.207  0.664   -34.670 1.00 39.84 ? 193 HIS B CA  1 
ATOM   3746 C C   . HIS B 1 193 ? 42.716  -0.307  -35.722 1.00 40.51 ? 193 HIS B C   1 
ATOM   3747 O O   . HIS B 1 193 ? 43.847  -0.178  -36.199 1.00 40.48 ? 193 HIS B O   1 
ATOM   3748 C CB  . HIS B 1 193 ? 42.032  2.074   -35.259 1.00 39.80 ? 193 HIS B CB  1 
ATOM   3749 C CG  . HIS B 1 193 ? 41.377  2.101   -36.608 1.00 39.54 ? 193 HIS B CG  1 
ATOM   3750 N ND1 . HIS B 1 193 ? 40.130  1.562   -36.846 1.00 39.25 ? 193 HIS B ND1 1 
ATOM   3751 C CD2 . HIS B 1 193 ? 41.795  2.616   -37.788 1.00 39.23 ? 193 HIS B CD2 1 
ATOM   3752 C CE1 . HIS B 1 193 ? 39.810  1.741   -38.115 1.00 38.91 ? 193 HIS B CE1 1 
ATOM   3753 N NE2 . HIS B 1 193 ? 40.804  2.376   -38.709 1.00 38.88 ? 193 HIS B NE2 1 
ATOM   3754 N N   . LYS B 1 194 ? 41.883  -1.290  -36.061 1.00 41.43 ? 194 LYS B N   1 
ATOM   3755 C CA  . LYS B 1 194 ? 42.191  -2.228  -37.138 1.00 42.48 ? 194 LYS B CA  1 
ATOM   3756 C C   . LYS B 1 194 ? 41.872  -1.574  -38.477 1.00 43.27 ? 194 LYS B C   1 
ATOM   3757 O O   . LYS B 1 194 ? 40.780  -1.024  -38.665 1.00 43.32 ? 194 LYS B O   1 
ATOM   3758 C CB  . LYS B 1 194 ? 41.410  -3.535  -36.976 1.00 42.40 ? 194 LYS B CB  1 
ATOM   3759 N N   . GLU B 1 195 ? 42.826  -1.632  -39.400 1.00 44.30 ? 195 GLU B N   1 
ATOM   3760 C CA  . GLU B 1 195 ? 42.707  -0.921  -40.672 1.00 45.32 ? 195 GLU B CA  1 
ATOM   3761 C C   . GLU B 1 195 ? 41.925  -1.687  -41.734 1.00 45.82 ? 195 GLU B C   1 
ATOM   3762 O O   . GLU B 1 195 ? 41.966  -2.921  -41.795 1.00 46.00 ? 195 GLU B O   1 
ATOM   3763 C CB  . GLU B 1 195 ? 44.086  -0.529  -41.203 1.00 45.42 ? 195 GLU B CB  1 
ATOM   3764 C CG  . GLU B 1 195 ? 44.693  0.682   -40.483 1.00 46.08 ? 195 GLU B CG  1 
ATOM   3765 C CD  . GLU B 1 195 ? 46.009  1.117   -41.104 1.00 47.30 ? 195 GLU B CD  1 
ATOM   3766 O OE1 . GLU B 1 195 ? 46.859  0.240   -41.386 1.00 48.15 ? 195 GLU B OE1 1 
ATOM   3767 O OE2 . GLU B 1 195 ? 46.200  2.340   -41.302 1.00 47.66 ? 195 GLU B OE2 1 
ATOM   3768 N N   . ARG B 1 196 ? 41.200  -0.926  -42.557 1.00 46.38 ? 196 ARG B N   1 
ATOM   3769 C CA  . ARG B 1 196 ? 40.491  -1.470  -43.716 1.00 46.85 ? 196 ARG B CA  1 
ATOM   3770 C C   . ARG B 1 196 ? 41.321  -1.127  -44.952 1.00 47.18 ? 196 ARG B C   1 
ATOM   3771 O O   . ARG B 1 196 ? 41.092  -0.105  -45.613 1.00 47.31 ? 196 ARG B O   1 
ATOM   3772 C CB  . ARG B 1 196 ? 39.075  -0.864  -43.816 1.00 46.86 ? 196 ARG B CB  1 
ATOM   3773 N N   . LYS B 1 197 ? 42.298  -1.986  -45.241 1.00 47.45 ? 197 LYS B N   1 
ATOM   3774 C CA  . LYS B 1 197 ? 43.231  -1.772  -46.346 1.00 47.67 ? 197 LYS B CA  1 
ATOM   3775 C C   . LYS B 1 197 ? 42.610  -2.159  -47.685 1.00 47.76 ? 197 LYS B C   1 
ATOM   3776 O O   . LYS B 1 197 ? 41.552  -1.647  -48.061 1.00 47.95 ? 197 LYS B O   1 
ATOM   3777 C CB  . LYS B 1 197 ? 44.518  -2.554  -46.109 1.00 47.72 ? 197 LYS B CB  1 
ATOM   3778 N N   . MET B 1 205 ? 46.685  -3.060  -37.687 1.00 35.49 ? 205 MET B N   1 
ATOM   3779 C CA  . MET B 1 205 ? 46.366  -2.504  -36.367 1.00 35.70 ? 205 MET B CA  1 
ATOM   3780 C C   . MET B 1 205 ? 47.261  -1.302  -36.023 1.00 35.84 ? 205 MET B C   1 
ATOM   3781 O O   . MET B 1 205 ? 48.492  -1.419  -36.025 1.00 35.85 ? 205 MET B O   1 
ATOM   3782 C CB  . MET B 1 205 ? 46.485  -3.591  -35.292 1.00 35.62 ? 205 MET B CB  1 
ATOM   3783 C CG  . MET B 1 205 ? 45.267  -3.708  -34.390 1.00 35.22 ? 205 MET B CG  1 
ATOM   3784 S SD  . MET B 1 205 ? 45.383  -5.071  -33.207 1.00 35.03 ? 205 MET B SD  1 
ATOM   3785 C CE  . MET B 1 205 ? 43.646  -5.368  -32.840 1.00 34.80 ? 205 MET B CE  1 
ATOM   3786 N N   . VAL B 1 206 ? 46.638  -0.155  -35.740 1.00 35.89 ? 206 VAL B N   1 
ATOM   3787 C CA  . VAL B 1 206 ? 47.370  1.076   -35.396 1.00 36.13 ? 206 VAL B CA  1 
ATOM   3788 C C   . VAL B 1 206 ? 47.048  1.585   -33.987 1.00 36.34 ? 206 VAL B C   1 
ATOM   3789 O O   . VAL B 1 206 ? 45.889  1.604   -33.570 1.00 36.45 ? 206 VAL B O   1 
ATOM   3790 C CB  . VAL B 1 206 ? 47.158  2.230   -36.435 1.00 36.01 ? 206 VAL B CB  1 
ATOM   3791 C CG1 . VAL B 1 206 ? 47.871  1.923   -37.742 1.00 36.31 ? 206 VAL B CG1 1 
ATOM   3792 C CG2 . VAL B 1 206 ? 45.679  2.498   -36.690 1.00 36.15 ? 206 VAL B CG2 1 
ATOM   3793 N N   . LEU B 1 207 ? 48.085  1.993   -33.261 1.00 36.48 ? 207 LEU B N   1 
ATOM   3794 C CA  . LEU B 1 207 ? 47.920  2.527   -31.916 1.00 36.63 ? 207 LEU B CA  1 
ATOM   3795 C C   . LEU B 1 207 ? 48.160  4.031   -31.907 1.00 36.91 ? 207 LEU B C   1 
ATOM   3796 O O   . LEU B 1 207 ? 49.094  4.525   -32.543 1.00 37.08 ? 207 LEU B O   1 
ATOM   3797 C CB  . LEU B 1 207 ? 48.863  1.817   -30.934 1.00 36.56 ? 207 LEU B CB  1 
ATOM   3798 C CG  . LEU B 1 207 ? 49.027  2.327   -29.492 1.00 36.26 ? 207 LEU B CG  1 
ATOM   3799 C CD1 . LEU B 1 207 ? 47.835  1.977   -28.611 1.00 35.59 ? 207 LEU B CD1 1 
ATOM   3800 C CD2 . LEU B 1 207 ? 50.312  1.796   -28.880 1.00 35.11 ? 207 LEU B CD2 1 
ATOM   3801 N N   . VAL B 1 208 ? 47.295  4.756   -31.204 1.00 37.15 ? 208 VAL B N   1 
ATOM   3802 C CA  . VAL B 1 208 ? 47.503  6.179   -30.957 1.00 37.30 ? 208 VAL B CA  1 
ATOM   3803 C C   . VAL B 1 208 ? 47.592  6.425   -29.454 1.00 37.53 ? 208 VAL B C   1 
ATOM   3804 O O   . VAL B 1 208 ? 46.697  6.043   -28.696 1.00 37.53 ? 208 VAL B O   1 
ATOM   3805 C CB  . VAL B 1 208 ? 46.412  7.080   -31.616 1.00 37.18 ? 208 VAL B CB  1 
ATOM   3806 C CG1 . VAL B 1 208 ? 46.596  7.122   -33.126 1.00 37.23 ? 208 VAL B CG1 1 
ATOM   3807 C CG2 . VAL B 1 208 ? 45.006  6.617   -31.256 1.00 37.01 ? 208 VAL B CG2 1 
ATOM   3808 N N   . GLY B 1 209 ? 48.689  7.042   -29.027 1.00 37.76 ? 209 GLY B N   1 
ATOM   3809 C CA  . GLY B 1 209 ? 48.905  7.322   -27.613 1.00 38.19 ? 209 GLY B CA  1 
ATOM   3810 C C   . GLY B 1 209 ? 50.155  6.661   -27.070 1.00 38.46 ? 209 GLY B C   1 
ATOM   3811 O O   . GLY B 1 209 ? 50.571  5.597   -27.547 1.00 38.40 ? 209 GLY B O   1 
ATOM   3812 N N   . ASP B 1 210 ? 50.753  7.303   -26.067 1.00 38.81 ? 210 ASP B N   1 
ATOM   3813 C CA  . ASP B 1 210 ? 51.985  6.805   -25.462 1.00 39.06 ? 210 ASP B CA  1 
ATOM   3814 C C   . ASP B 1 210 ? 51.664  5.675   -24.495 1.00 39.23 ? 210 ASP B C   1 
ATOM   3815 O O   . ASP B 1 210 ? 50.882  5.848   -23.555 1.00 39.33 ? 210 ASP B O   1 
ATOM   3816 C CB  . ASP B 1 210 ? 52.731  7.936   -24.745 1.00 38.97 ? 210 ASP B CB  1 
ATOM   3817 N N   . VAL B 1 211 ? 52.264  4.515   -24.744 1.00 39.39 ? 211 VAL B N   1 
ATOM   3818 C CA  . VAL B 1 211 ? 52.096  3.351   -23.879 1.00 39.58 ? 211 VAL B CA  1 
ATOM   3819 C C   . VAL B 1 211 ? 53.445  2.911   -23.275 1.00 39.79 ? 211 VAL B C   1 
ATOM   3820 O O   . VAL B 1 211 ? 53.493  2.062   -22.376 1.00 39.87 ? 211 VAL B O   1 
ATOM   3821 C CB  . VAL B 1 211 ? 51.338  2.213   -24.644 1.00 39.55 ? 211 VAL B CB  1 
ATOM   3822 C CG1 . VAL B 1 211 ? 51.891  0.835   -24.343 1.00 39.42 ? 211 VAL B CG1 1 
ATOM   3823 C CG2 . VAL B 1 211 ? 49.842  2.283   -24.345 1.00 39.49 ? 211 VAL B CG2 1 
ATOM   3824 N N   . LYS B 1 212 ? 54.524  3.544   -23.751 1.00 39.90 ? 212 LYS B N   1 
ATOM   3825 C CA  . LYS B 1 212 ? 55.901  3.195   -23.390 1.00 40.02 ? 212 LYS B CA  1 
ATOM   3826 C C   . LYS B 1 212 ? 56.162  3.233   -21.883 1.00 39.91 ? 212 LYS B C   1 
ATOM   3827 O O   . LYS B 1 212 ? 55.814  4.208   -21.212 1.00 40.01 ? 212 LYS B O   1 
ATOM   3828 C CB  . LYS B 1 212 ? 56.876  4.136   -24.107 1.00 40.16 ? 212 LYS B CB  1 
ATOM   3829 C CG  . LYS B 1 212 ? 58.316  3.609   -24.180 1.00 41.06 ? 212 LYS B CG  1 
ATOM   3830 C CD  . LYS B 1 212 ? 59.258  4.812   -24.495 1.00 42.52 ? 212 LYS B CD  1 
ATOM   3831 C CE  . LYS B 1 212 ? 60.616  4.200   -25.009 1.00 43.28 ? 212 LYS B CE  1 
ATOM   3832 N NZ  . LYS B 1 212 ? 61.469  5.256   -25.701 1.00 43.83 ? 212 LYS B NZ  1 
ATOM   3833 N N   . ASP B 1 213 ? 56.777  2.162   -21.376 1.00 39.69 ? 213 ASP B N   1 
ATOM   3834 C CA  . ASP B 1 213 ? 57.129  2.000   -19.954 1.00 39.50 ? 213 ASP B CA  1 
ATOM   3835 C C   . ASP B 1 213 ? 55.964  2.188   -18.987 1.00 39.27 ? 213 ASP B C   1 
ATOM   3836 O O   . ASP B 1 213 ? 56.134  2.670   -17.860 1.00 39.39 ? 213 ASP B O   1 
ATOM   3837 C CB  . ASP B 1 213 ? 58.308  2.891   -19.567 1.00 39.65 ? 213 ASP B CB  1 
ATOM   3838 C CG  . ASP B 1 213 ? 59.627  2.318   -20.013 1.00 40.25 ? 213 ASP B CG  1 
ATOM   3839 O OD1 . ASP B 1 213 ? 59.959  2.451   -21.213 1.00 40.51 ? 213 ASP B OD1 1 
ATOM   3840 O OD2 . ASP B 1 213 ? 60.327  1.729   -19.162 1.00 41.16 ? 213 ASP B OD2 1 
ATOM   3841 N N   . ARG B 1 214 ? 54.781  1.801   -19.447 1.00 38.76 ? 214 ARG B N   1 
ATOM   3842 C CA  . ARG B 1 214 ? 53.576  1.832   -18.645 1.00 38.31 ? 214 ARG B CA  1 
ATOM   3843 C C   . ARG B 1 214 ? 52.914  0.468   -18.765 1.00 37.62 ? 214 ARG B C   1 
ATOM   3844 O O   . ARG B 1 214 ? 53.024  -0.188  -19.800 1.00 37.59 ? 214 ARG B O   1 
ATOM   3845 C CB  . ARG B 1 214 ? 52.625  2.918   -19.163 1.00 38.68 ? 214 ARG B CB  1 
ATOM   3846 C CG  . ARG B 1 214 ? 53.030  4.350   -18.807 1.00 39.84 ? 214 ARG B CG  1 
ATOM   3847 C CD  . ARG B 1 214 ? 51.970  5.349   -19.261 1.00 42.10 ? 214 ARG B CD  1 
ATOM   3848 N NE  . ARG B 1 214 ? 51.889  6.516   -18.383 1.00 44.39 ? 214 ARG B NE  1 
ATOM   3849 C CZ  . ARG B 1 214 ? 52.555  7.656   -18.567 1.00 45.80 ? 214 ARG B CZ  1 
ATOM   3850 N NH1 . ARG B 1 214 ? 53.370  7.807   -19.608 1.00 46.20 ? 214 ARG B NH1 1 
ATOM   3851 N NH2 . ARG B 1 214 ? 52.405  8.654   -17.704 1.00 46.22 ? 214 ARG B NH2 1 
ATOM   3852 N N   . VAL B 1 215 ? 52.240  0.029   -17.710 1.00 36.73 ? 215 VAL B N   1 
ATOM   3853 C CA  . VAL B 1 215 ? 51.403  -1.154  -17.829 1.00 35.78 ? 215 VAL B CA  1 
ATOM   3854 C C   . VAL B 1 215 ? 50.129  -0.719  -18.554 1.00 35.26 ? 215 VAL B C   1 
ATOM   3855 O O   . VAL B 1 215 ? 49.499  0.277   -18.181 1.00 35.11 ? 215 VAL B O   1 
ATOM   3856 C CB  . VAL B 1 215 ? 51.127  -1.852  -16.458 1.00 35.81 ? 215 VAL B CB  1 
ATOM   3857 C CG1 . VAL B 1 215 ? 52.178  -1.445  -15.424 1.00 35.66 ? 215 VAL B CG1 1 
ATOM   3858 C CG2 . VAL B 1 215 ? 49.708  -1.570  -15.936 1.00 35.61 ? 215 VAL B CG2 1 
ATOM   3859 N N   . ALA B 1 216 ? 49.790  -1.437  -19.621 1.00 34.43 ? 216 ALA B N   1 
ATOM   3860 C CA  . ALA B 1 216 ? 48.621  -1.106  -20.422 1.00 33.74 ? 216 ALA B CA  1 
ATOM   3861 C C   . ALA B 1 216 ? 47.436  -1.956  -19.995 1.00 33.27 ? 216 ALA B C   1 
ATOM   3862 O O   . ALA B 1 216 ? 47.580  -3.157  -19.743 1.00 33.16 ? 216 ALA B O   1 
ATOM   3863 C CB  . ALA B 1 216 ? 48.915  -1.295  -21.902 1.00 33.68 ? 216 ALA B CB  1 
ATOM   3864 N N   . ILE B 1 217 ? 46.270  -1.321  -19.893 1.00 32.75 ? 217 ILE B N   1 
ATOM   3865 C CA  . ILE B 1 217 ? 45.046  -2.027  -19.539 1.00 32.33 ? 217 ILE B CA  1 
ATOM   3866 C C   . ILE B 1 217 ? 44.027  -1.905  -20.670 1.00 32.21 ? 217 ILE B C   1 
ATOM   3867 O O   . ILE B 1 217 ? 43.481  -0.827  -20.926 1.00 32.19 ? 217 ILE B O   1 
ATOM   3868 C CB  . ILE B 1 217 ? 44.445  -1.533  -18.201 1.00 32.20 ? 217 ILE B CB  1 
ATOM   3869 C CG1 . ILE B 1 217 ? 45.492  -1.607  -17.077 1.00 32.35 ? 217 ILE B CG1 1 
ATOM   3870 C CG2 . ILE B 1 217 ? 43.205  -2.348  -17.843 1.00 32.12 ? 217 ILE B CG2 1 
ATOM   3871 C CD1 . ILE B 1 217 ? 45.006  -0.995  -15.735 1.00 32.14 ? 217 ILE B CD1 1 
ATOM   3872 N N   . LEU B 1 218 ? 43.803  -3.023  -21.356 1.00 31.93 ? 218 LEU B N   1 
ATOM   3873 C CA  . LEU B 1 218 ? 42.769  -3.131  -22.370 1.00 31.82 ? 218 LEU B CA  1 
ATOM   3874 C C   . LEU B 1 218 ? 41.391  -3.153  -21.714 1.00 31.77 ? 218 LEU B C   1 
ATOM   3875 O O   . LEU B 1 218 ? 41.100  -4.025  -20.897 1.00 31.72 ? 218 LEU B O   1 
ATOM   3876 C CB  . LEU B 1 218 ? 42.986  -4.405  -23.192 1.00 31.77 ? 218 LEU B CB  1 
ATOM   3877 C CG  . LEU B 1 218 ? 43.490  -4.349  -24.641 1.00 31.51 ? 218 LEU B CG  1 
ATOM   3878 C CD1 . LEU B 1 218 ? 43.889  -2.959  -25.091 1.00 31.04 ? 218 LEU B CD1 1 
ATOM   3879 C CD2 . LEU B 1 218 ? 44.610  -5.366  -24.892 1.00 31.13 ? 218 LEU B CD2 1 
ATOM   3880 N N   . VAL B 1 219 ? 40.554  -2.179  -22.058 1.00 31.91 ? 219 VAL B N   1 
ATOM   3881 C CA  . VAL B 1 219 ? 39.188  -2.127  -21.535 1.00 32.00 ? 219 VAL B CA  1 
ATOM   3882 C C   . VAL B 1 219 ? 38.167  -2.093  -22.668 1.00 32.18 ? 219 VAL B C   1 
ATOM   3883 O O   . VAL B 1 219 ? 38.233  -1.242  -23.560 1.00 31.90 ? 219 VAL B O   1 
ATOM   3884 C CB  . VAL B 1 219 ? 38.967  -0.932  -20.560 1.00 31.95 ? 219 VAL B CB  1 
ATOM   3885 C CG1 . VAL B 1 219 ? 37.504  -0.863  -20.118 1.00 31.93 ? 219 VAL B CG1 1 
ATOM   3886 C CG2 . VAL B 1 219 ? 39.867  -1.062  -19.339 1.00 31.52 ? 219 VAL B CG2 1 
ATOM   3887 N N   . ASP B 1 220 ? 37.234  -3.041  -22.619 1.00 32.59 ? 220 ASP B N   1 
ATOM   3888 C CA  . ASP B 1 220 ? 36.138  -3.135  -23.577 1.00 32.99 ? 220 ASP B CA  1 
ATOM   3889 C C   . ASP B 1 220 ? 34.923  -3.673  -22.826 1.00 33.11 ? 220 ASP B C   1 
ATOM   3890 O O   . ASP B 1 220 ? 35.050  -4.102  -21.682 1.00 33.12 ? 220 ASP B O   1 
ATOM   3891 C CB  . ASP B 1 220 ? 36.531  -4.071  -24.726 1.00 33.12 ? 220 ASP B CB  1 
ATOM   3892 C CG  . ASP B 1 220 ? 35.995  -3.612  -26.082 1.00 33.84 ? 220 ASP B CG  1 
ATOM   3893 O OD1 . ASP B 1 220 ? 35.474  -2.475  -26.196 1.00 34.69 ? 220 ASP B OD1 1 
ATOM   3894 O OD2 . ASP B 1 220 ? 36.116  -4.395  -27.050 1.00 34.39 ? 220 ASP B OD2 1 
ATOM   3895 N N   . ASP B 1 221 ? 33.746  -3.642  -23.444 1.00 33.51 ? 221 ASP B N   1 
ATOM   3896 C CA  . ASP B 1 221 ? 32.542  -4.129  -22.761 1.00 33.80 ? 221 ASP B CA  1 
ATOM   3897 C C   . ASP B 1 221 ? 32.376  -5.631  -22.927 1.00 34.09 ? 221 ASP B C   1 
ATOM   3898 O O   . ASP B 1 221 ? 31.694  -6.281  -22.132 1.00 33.95 ? 221 ASP B O   1 
ATOM   3899 C CB  . ASP B 1 221 ? 31.278  -3.387  -23.228 1.00 33.69 ? 221 ASP B CB  1 
ATOM   3900 C CG  . ASP B 1 221 ? 30.631  -4.021  -24.452 1.00 33.68 ? 221 ASP B CG  1 
ATOM   3901 O OD1 . ASP B 1 221 ? 31.266  -4.016  -25.530 1.00 33.17 ? 221 ASP B OD1 1 
ATOM   3902 O OD2 . ASP B 1 221 ? 29.480  -4.511  -24.336 1.00 33.49 ? 221 ASP B OD2 1 
ATOM   3903 N N   . MET B 1 222 ? 33.030  -6.172  -23.954 1.00 34.69 ? 222 MET B N   1 
ATOM   3904 C CA  . MET B 1 222 ? 32.785  -7.532  -24.412 1.00 35.33 ? 222 MET B CA  1 
ATOM   3905 C C   . MET B 1 222 ? 34.000  -8.154  -25.099 1.00 35.40 ? 222 MET B C   1 
ATOM   3906 O O   . MET B 1 222 ? 34.711  -7.491  -25.856 1.00 35.50 ? 222 MET B O   1 
ATOM   3907 C CB  . MET B 1 222 ? 31.589  -7.521  -25.366 1.00 35.65 ? 222 MET B CB  1 
ATOM   3908 C CG  . MET B 1 222 ? 31.490  -8.711  -26.309 1.00 37.16 ? 222 MET B CG  1 
ATOM   3909 S SD  . MET B 1 222 ? 30.057  -8.545  -27.385 1.00 40.73 ? 222 MET B SD  1 
ATOM   3910 C CE  . MET B 1 222 ? 28.715  -8.778  -26.202 1.00 39.71 ? 222 MET B CE  1 
ATOM   3911 N N   . ALA B 1 223 ? 34.222  -9.436  -24.822 1.00 35.53 ? 223 ALA B N   1 
ATOM   3912 C CA  . ALA B 1 223 ? 35.212  -10.238 -25.532 1.00 35.58 ? 223 ALA B CA  1 
ATOM   3913 C C   . ALA B 1 223 ? 34.559  -11.534 -25.981 1.00 35.70 ? 223 ALA B C   1 
ATOM   3914 O O   . ALA B 1 223 ? 33.712  -12.096 -25.271 1.00 35.74 ? 223 ALA B O   1 
ATOM   3915 C CB  . ALA B 1 223 ? 36.400  -10.533 -24.648 1.00 35.51 ? 223 ALA B CB  1 
ATOM   3916 N N   . ASP B 1 224 ? 34.964  -12.007 -27.160 1.00 35.68 ? 224 ASP B N   1 
ATOM   3917 C CA  . ASP B 1 224 ? 34.339  -13.168 -27.766 1.00 35.73 ? 224 ASP B CA  1 
ATOM   3918 C C   . ASP B 1 224 ? 35.420  -14.172 -28.182 1.00 35.81 ? 224 ASP B C   1 
ATOM   3919 O O   . ASP B 1 224 ? 35.879  -14.959 -27.354 1.00 35.81 ? 224 ASP B O   1 
ATOM   3920 C CB  . ASP B 1 224 ? 33.455  -12.724 -28.946 1.00 35.65 ? 224 ASP B CB  1 
ATOM   3921 C CG  . ASP B 1 224 ? 32.519  -13.822 -29.421 1.00 35.64 ? 224 ASP B CG  1 
ATOM   3922 O OD1 . ASP B 1 224 ? 32.590  -14.954 -28.903 1.00 35.24 ? 224 ASP B OD1 1 
ATOM   3923 O OD2 . ASP B 1 224 ? 31.701  -13.542 -30.324 1.00 35.91 ? 224 ASP B OD2 1 
ATOM   3924 N N   . THR B 1 225 ? 35.835  -14.135 -29.446 1.00 35.90 ? 225 THR B N   1 
ATOM   3925 C CA  . THR B 1 225 ? 36.883  -15.032 -29.938 1.00 36.10 ? 225 THR B CA  1 
ATOM   3926 C C   . THR B 1 225 ? 38.257  -14.616 -29.404 1.00 36.18 ? 225 THR B C   1 
ATOM   3927 O O   . THR B 1 225 ? 39.194  -15.419 -29.392 1.00 36.25 ? 225 THR B O   1 
ATOM   3928 C CB  . THR B 1 225 ? 36.927  -15.083 -31.479 1.00 36.15 ? 225 THR B CB  1 
ATOM   3929 O OG1 . THR B 1 225 ? 37.491  -13.868 -31.987 1.00 36.17 ? 225 THR B OG1 1 
ATOM   3930 C CG2 . THR B 1 225 ? 35.525  -15.297 -32.068 1.00 36.15 ? 225 THR B CG2 1 
ATOM   3931 N N   . CYS B 1 226 ? 38.354  -13.356 -28.974 1.00 36.12 ? 226 CYS B N   1 
ATOM   3932 C CA  . CYS B 1 226 ? 39.558  -12.769 -28.365 1.00 36.08 ? 226 CYS B CA  1 
ATOM   3933 C C   . CYS B 1 226 ? 40.673  -12.434 -29.354 1.00 35.87 ? 226 CYS B C   1 
ATOM   3934 O O   . CYS B 1 226 ? 41.737  -11.938 -28.954 1.00 35.71 ? 226 CYS B O   1 
ATOM   3935 C CB  . CYS B 1 226 ? 40.078  -13.625 -27.206 1.00 36.19 ? 226 CYS B CB  1 
ATOM   3936 S SG  . CYS B 1 226 ? 38.882  -13.787 -25.883 1.00 36.66 ? 226 CYS B SG  1 
ATOM   3937 N N   . GLY B 1 227 ? 40.420  -12.677 -30.641 1.00 35.79 ? 227 GLY B N   1 
ATOM   3938 C CA  . GLY B 1 227 ? 41.343  -12.252 -31.695 1.00 35.73 ? 227 GLY B CA  1 
ATOM   3939 C C   . GLY B 1 227 ? 41.784  -10.815 -31.500 1.00 35.64 ? 227 GLY B C   1 
ATOM   3940 O O   . GLY B 1 227 ? 42.981  -10.522 -31.501 1.00 35.60 ? 227 GLY B O   1 
ATOM   3941 N N   . THR B 1 228 ? 40.807  -9.932  -31.294 1.00 35.52 ? 228 THR B N   1 
ATOM   3942 C CA  . THR B 1 228 ? 41.046  -8.497  -31.135 1.00 35.33 ? 228 THR B CA  1 
ATOM   3943 C C   . THR B 1 228 ? 41.947  -8.150  -29.945 1.00 35.18 ? 228 THR B C   1 
ATOM   3944 O O   . THR B 1 228 ? 42.954  -7.460  -30.122 1.00 35.21 ? 228 THR B O   1 
ATOM   3945 C CB  . THR B 1 228 ? 39.710  -7.704  -31.081 1.00 35.36 ? 228 THR B CB  1 
ATOM   3946 O OG1 . THR B 1 228 ? 39.073  -7.761  -32.372 1.00 35.64 ? 228 THR B OG1 1 
ATOM   3947 C CG2 . THR B 1 228 ? 39.936  -6.241  -30.688 1.00 35.07 ? 228 THR B CG2 1 
ATOM   3948 N N   . ILE B 1 229 ? 41.598  -8.625  -28.749 1.00 34.87 ? 229 ILE B N   1 
ATOM   3949 C CA  . ILE B 1 229 ? 42.389  -8.302  -27.550 1.00 34.57 ? 229 ILE B CA  1 
ATOM   3950 C C   . ILE B 1 229 ? 43.773  -8.947  -27.539 1.00 34.47 ? 229 ILE B C   1 
ATOM   3951 O O   . ILE B 1 229 ? 44.732  -8.343  -27.054 1.00 34.54 ? 229 ILE B O   1 
ATOM   3952 C CB  . ILE B 1 229 ? 41.646  -8.582  -26.207 1.00 34.50 ? 229 ILE B CB  1 
ATOM   3953 C CG1 . ILE B 1 229 ? 40.883  -9.913  -26.259 1.00 34.30 ? 229 ILE B CG1 1 
ATOM   3954 C CG2 . ILE B 1 229 ? 40.721  -7.405  -25.859 1.00 34.39 ? 229 ILE B CG2 1 
ATOM   3955 C CD1 . ILE B 1 229 ? 40.603  -10.513 -24.893 1.00 33.98 ? 229 ILE B CD1 1 
ATOM   3956 N N   . CYS B 1 230 ? 43.873  -10.161 -28.077 1.00 34.25 ? 230 CYS B N   1 
ATOM   3957 C CA  . CYS B 1 230 ? 45.157  -10.842 -28.207 1.00 34.13 ? 230 CYS B CA  1 
ATOM   3958 C C   . CYS B 1 230 ? 46.080  -10.072 -29.149 1.00 33.96 ? 230 CYS B C   1 
ATOM   3959 O O   . CYS B 1 230 ? 47.257  -9.863  -28.836 1.00 34.13 ? 230 CYS B O   1 
ATOM   3960 C CB  . CYS B 1 230 ? 44.975  -12.286 -28.693 1.00 34.18 ? 230 CYS B CB  1 
ATOM   3961 S SG  . CYS B 1 230 ? 44.372  -13.464 -27.441 1.00 35.20 ? 230 CYS B SG  1 
ATOM   3962 N N   . HIS B 1 231 ? 45.542  -9.645  -30.292 1.00 33.61 ? 231 HIS B N   1 
ATOM   3963 C CA  . HIS B 1 231 ? 46.316  -8.881  -31.274 1.00 33.36 ? 231 HIS B CA  1 
ATOM   3964 C C   . HIS B 1 231 ? 46.707  -7.508  -30.741 1.00 32.99 ? 231 HIS B C   1 
ATOM   3965 O O   . HIS B 1 231 ? 47.828  -7.045  -30.964 1.00 32.98 ? 231 HIS B O   1 
ATOM   3966 C CB  . HIS B 1 231 ? 45.567  -8.771  -32.604 1.00 33.47 ? 231 HIS B CB  1 
ATOM   3967 C CG  . HIS B 1 231 ? 45.669  -10.004 -33.449 1.00 34.34 ? 231 HIS B CG  1 
ATOM   3968 N ND1 . HIS B 1 231 ? 44.732  -11.019 -33.408 1.00 35.34 ? 231 HIS B ND1 1 
ATOM   3969 C CD2 . HIS B 1 231 ? 46.611  -10.399 -34.339 1.00 35.02 ? 231 HIS B CD2 1 
ATOM   3970 C CE1 . HIS B 1 231 ? 45.085  -11.979 -34.245 1.00 35.21 ? 231 HIS B CE1 1 
ATOM   3971 N NE2 . HIS B 1 231 ? 46.223  -11.629 -34.821 1.00 35.20 ? 231 HIS B NE2 1 
ATOM   3972 N N   . ALA B 1 232 ? 45.783  -6.875  -30.022 1.00 32.64 ? 232 ALA B N   1 
ATOM   3973 C CA  . ALA B 1 232 ? 46.060  -5.624  -29.321 1.00 32.27 ? 232 ALA B CA  1 
ATOM   3974 C C   . ALA B 1 232 ? 47.109  -5.791  -28.209 1.00 32.07 ? 232 ALA B C   1 
ATOM   3975 O O   . ALA B 1 232 ? 47.899  -4.879  -27.964 1.00 31.90 ? 232 ALA B O   1 
ATOM   3976 C CB  . ALA B 1 232 ? 44.769  -5.044  -28.758 1.00 32.26 ? 232 ALA B CB  1 
ATOM   3977 N N   . ALA B 1 233 ? 47.111  -6.949  -27.545 1.00 31.88 ? 233 ALA B N   1 
ATOM   3978 C CA  . ALA B 1 233 ? 48.104  -7.250  -26.503 1.00 31.90 ? 233 ALA B CA  1 
ATOM   3979 C C   . ALA B 1 233 ? 49.525  -7.279  -27.063 1.00 31.85 ? 233 ALA B C   1 
ATOM   3980 O O   . ALA B 1 233 ? 50.419  -6.617  -26.526 1.00 31.80 ? 233 ALA B O   1 
ATOM   3981 C CB  . ALA B 1 233 ? 47.781  -8.564  -25.800 1.00 31.86 ? 233 ALA B CB  1 
ATOM   3982 N N   . ASP B 1 234 ? 49.724  -8.047  -28.136 1.00 31.73 ? 234 ASP B N   1 
ATOM   3983 C CA  . ASP B 1 234 ? 50.997  -8.056  -28.854 1.00 31.68 ? 234 ASP B CA  1 
ATOM   3984 C C   . ASP B 1 234 ? 51.396  -6.634  -29.247 1.00 31.54 ? 234 ASP B C   1 
ATOM   3985 O O   . ASP B 1 234 ? 52.520  -6.202  -28.990 1.00 31.44 ? 234 ASP B O   1 
ATOM   3986 C CB  . ASP B 1 234 ? 50.912  -8.935  -30.110 1.00 31.68 ? 234 ASP B CB  1 
ATOM   3987 C CG  . ASP B 1 234 ? 50.911  -10.424 -29.797 1.00 31.72 ? 234 ASP B CG  1 
ATOM   3988 O OD1 . ASP B 1 234 ? 51.283  -10.816 -28.670 1.00 31.17 ? 234 ASP B OD1 1 
ATOM   3989 O OD2 . ASP B 1 234 ? 50.541  -11.213 -30.694 1.00 32.53 ? 234 ASP B OD2 1 
ATOM   3990 N N   . LYS B 1 235 ? 50.449  -5.911  -29.843 1.00 31.46 ? 235 LYS B N   1 
ATOM   3991 C CA  . LYS B 1 235 ? 50.685  -4.571  -30.374 1.00 31.49 ? 235 LYS B CA  1 
ATOM   3992 C C   . LYS B 1 235 ? 51.167  -3.614  -29.292 1.00 31.37 ? 235 LYS B C   1 
ATOM   3993 O O   . LYS B 1 235 ? 52.064  -2.801  -29.527 1.00 31.45 ? 235 LYS B O   1 
ATOM   3994 C CB  . LYS B 1 235 ? 49.417  -4.032  -31.058 1.00 31.59 ? 235 LYS B CB  1 
ATOM   3995 C CG  . LYS B 1 235 ? 49.590  -2.703  -31.788 1.00 31.91 ? 235 LYS B CG  1 
ATOM   3996 C CD  . LYS B 1 235 ? 50.485  -2.826  -33.021 1.00 32.98 ? 235 LYS B CD  1 
ATOM   3997 C CE  . LYS B 1 235 ? 50.951  -1.446  -33.490 1.00 33.86 ? 235 LYS B CE  1 
ATOM   3998 N NZ  . LYS B 1 235 ? 51.713  -1.505  -34.773 1.00 34.16 ? 235 LYS B NZ  1 
ATOM   3999 N N   . LEU B 1 236 ? 50.571  -3.726  -28.109 1.00 31.24 ? 236 LEU B N   1 
ATOM   4000 C CA  . LEU B 1 236 ? 50.926  -2.875  -26.981 1.00 30.93 ? 236 LEU B CA  1 
ATOM   4001 C C   . LEU B 1 236 ? 52.333  -3.174  -26.472 1.00 30.90 ? 236 LEU B C   1 
ATOM   4002 O O   . LEU B 1 236 ? 53.093  -2.251  -26.176 1.00 30.88 ? 236 LEU B O   1 
ATOM   4003 C CB  . LEU B 1 236 ? 49.894  -3.006  -25.855 1.00 30.91 ? 236 LEU B CB  1 
ATOM   4004 C CG  . LEU B 1 236 ? 48.453  -2.572  -26.171 1.00 30.56 ? 236 LEU B CG  1 
ATOM   4005 C CD1 . LEU B 1 236 ? 47.508  -2.964  -25.044 1.00 29.46 ? 236 LEU B CD1 1 
ATOM   4006 C CD2 . LEU B 1 236 ? 48.351  -1.078  -26.471 1.00 29.64 ? 236 LEU B CD2 1 
ATOM   4007 N N   . LEU B 1 237 ? 52.677  -4.458  -26.384 1.00 30.82 ? 237 LEU B N   1 
ATOM   4008 C CA  . LEU B 1 237 ? 54.011  -4.874  -25.933 1.00 30.64 ? 237 LEU B CA  1 
ATOM   4009 C C   . LEU B 1 237 ? 55.101  -4.430  -26.907 1.00 30.69 ? 237 LEU B C   1 
ATOM   4010 O O   . LEU B 1 237 ? 56.185  -4.005  -26.487 1.00 30.58 ? 237 LEU B O   1 
ATOM   4011 C CB  . LEU B 1 237 ? 54.064  -6.384  -25.676 1.00 30.45 ? 237 LEU B CB  1 
ATOM   4012 C CG  . LEU B 1 237 ? 53.285  -6.890  -24.447 1.00 30.24 ? 237 LEU B CG  1 
ATOM   4013 C CD1 . LEU B 1 237 ? 53.385  -8.398  -24.298 1.00 29.31 ? 237 LEU B CD1 1 
ATOM   4014 C CD2 . LEU B 1 237 ? 53.723  -6.214  -23.153 1.00 29.72 ? 237 LEU B CD2 1 
ATOM   4015 N N   . SER B 1 238 ? 54.795  -4.510  -28.202 1.00 30.93 ? 238 SER B N   1 
ATOM   4016 C CA  . SER B 1 238 ? 55.648  -3.943  -29.243 1.00 31.10 ? 238 SER B CA  1 
ATOM   4017 C C   . SER B 1 238 ? 55.846  -2.443  -29.047 1.00 31.21 ? 238 SER B C   1 
ATOM   4018 O O   . SER B 1 238 ? 56.884  -1.897  -29.425 1.00 31.23 ? 238 SER B O   1 
ATOM   4019 C CB  . SER B 1 238 ? 55.037  -4.184  -30.623 1.00 31.07 ? 238 SER B CB  1 
ATOM   4020 O OG  . SER B 1 238 ? 54.905  -5.580  -30.885 1.00 31.49 ? 238 SER B OG  1 
ATOM   4021 N N   . ALA B 1 239 ? 54.846  -1.782  -28.462 1.00 31.46 ? 239 ALA B N   1 
ATOM   4022 C CA  . ALA B 1 239 ? 54.895  -0.333  -28.273 1.00 31.80 ? 239 ALA B CA  1 
ATOM   4023 C C   . ALA B 1 239 ? 55.624  0.070   -26.988 1.00 32.02 ? 239 ALA B C   1 
ATOM   4024 O O   . ALA B 1 239 ? 55.809  1.258   -26.721 1.00 31.93 ? 239 ALA B O   1 
ATOM   4025 C CB  . ALA B 1 239 ? 53.496  0.257   -28.318 1.00 31.73 ? 239 ALA B CB  1 
ATOM   4026 N N   . GLY B 1 240 ? 56.036  -0.924  -26.206 1.00 32.38 ? 240 GLY B N   1 
ATOM   4027 C CA  . GLY B 1 240 ? 56.868  -0.697  -25.030 1.00 32.96 ? 240 GLY B CA  1 
ATOM   4028 C C   . GLY B 1 240 ? 56.153  -0.787  -23.694 1.00 33.42 ? 240 GLY B C   1 
ATOM   4029 O O   . GLY B 1 240 ? 56.653  -0.279  -22.684 1.00 33.57 ? 240 GLY B O   1 
ATOM   4030 N N   . ALA B 1 241 ? 54.984  -1.428  -23.687 1.00 33.68 ? 241 ALA B N   1 
ATOM   4031 C CA  . ALA B 1 241 ? 54.235  -1.645  -22.449 1.00 33.97 ? 241 ALA B CA  1 
ATOM   4032 C C   . ALA B 1 241 ? 54.905  -2.734  -21.622 1.00 34.14 ? 241 ALA B C   1 
ATOM   4033 O O   . ALA B 1 241 ? 55.315  -3.763  -22.158 1.00 34.19 ? 241 ALA B O   1 
ATOM   4034 C CB  . ALA B 1 241 ? 52.788  -2.018  -22.745 1.00 33.95 ? 241 ALA B CB  1 
ATOM   4035 N N   . THR B 1 242 ? 55.027  -2.500  -20.317 1.00 34.37 ? 242 THR B N   1 
ATOM   4036 C CA  . THR B 1 242 ? 55.693  -3.466  -19.448 1.00 34.62 ? 242 THR B CA  1 
ATOM   4037 C C   . THR B 1 242 ? 54.845  -4.736  -19.335 1.00 34.81 ? 242 THR B C   1 
ATOM   4038 O O   . THR B 1 242 ? 55.361  -5.854  -19.439 1.00 35.03 ? 242 THR B O   1 
ATOM   4039 C CB  . THR B 1 242 ? 56.027  -2.874  -18.051 1.00 34.62 ? 242 THR B CB  1 
ATOM   4040 O OG1 . THR B 1 242 ? 54.817  -2.620  -17.323 1.00 34.78 ? 242 THR B OG1 1 
ATOM   4041 C CG2 . THR B 1 242 ? 56.825  -1.571  -18.190 1.00 34.70 ? 242 THR B CG2 1 
ATOM   4042 N N   . ARG B 1 243 ? 53.542  -4.554  -19.145 1.00 34.87 ? 243 ARG B N   1 
ATOM   4043 C CA  . ARG B 1 243 ? 52.600  -5.671  -19.131 1.00 34.97 ? 243 ARG B CA  1 
ATOM   4044 C C   . ARG B 1 243 ? 51.230  -5.262  -19.667 1.00 34.71 ? 243 ARG B C   1 
ATOM   4045 O O   . ARG B 1 243 ? 50.928  -4.065  -19.797 1.00 34.90 ? 243 ARG B O   1 
ATOM   4046 C CB  . ARG B 1 243 ? 52.483  -6.286  -17.731 1.00 35.17 ? 243 ARG B CB  1 
ATOM   4047 C CG  . ARG B 1 243 ? 52.282  -5.291  -16.599 1.00 36.11 ? 243 ARG B CG  1 
ATOM   4048 C CD  . ARG B 1 243 ? 52.167  -5.989  -15.249 1.00 37.57 ? 243 ARG B CD  1 
ATOM   4049 N NE  . ARG B 1 243 ? 53.353  -6.783  -14.921 1.00 38.47 ? 243 ARG B NE  1 
ATOM   4050 C CZ  . ARG B 1 243 ? 54.396  -6.335  -14.228 1.00 38.99 ? 243 ARG B CZ  1 
ATOM   4051 N NH1 . ARG B 1 243 ? 54.418  -5.088  -13.771 1.00 38.80 ? 243 ARG B NH1 1 
ATOM   4052 N NH2 . ARG B 1 243 ? 55.422  -7.139  -13.986 1.00 39.41 ? 243 ARG B NH2 1 
ATOM   4053 N N   . VAL B 1 244 ? 50.412  -6.256  -20.000 1.00 34.25 ? 244 VAL B N   1 
ATOM   4054 C CA  . VAL B 1 244 ? 49.072  -5.996  -20.512 1.00 33.83 ? 244 VAL B CA  1 
ATOM   4055 C C   . VAL B 1 244 ? 48.020  -6.785  -19.732 1.00 33.70 ? 244 VAL B C   1 
ATOM   4056 O O   . VAL B 1 244 ? 48.125  -8.008  -19.561 1.00 33.48 ? 244 VAL B O   1 
ATOM   4057 C CB  . VAL B 1 244 ? 48.951  -6.292  -22.036 1.00 33.83 ? 244 VAL B CB  1 
ATOM   4058 C CG1 . VAL B 1 244 ? 47.547  -5.961  -22.542 1.00 33.48 ? 244 VAL B CG1 1 
ATOM   4059 C CG2 . VAL B 1 244 ? 49.987  -5.500  -22.832 1.00 33.52 ? 244 VAL B CG2 1 
ATOM   4060 N N   . TYR B 1 245 ? 47.016  -6.053  -19.246 1.00 33.49 ? 245 TYR B N   1 
ATOM   4061 C CA  . TYR B 1 245 ? 45.820  -6.651  -18.668 1.00 33.25 ? 245 TYR B CA  1 
ATOM   4062 C C   . TYR B 1 245 ? 44.668  -6.454  -19.643 1.00 32.91 ? 245 TYR B C   1 
ATOM   4063 O O   . TYR B 1 245 ? 44.739  -5.621  -20.548 1.00 32.90 ? 245 TYR B O   1 
ATOM   4064 C CB  . TYR B 1 245 ? 45.463  -5.984  -17.334 1.00 33.36 ? 245 TYR B CB  1 
ATOM   4065 C CG  . TYR B 1 245 ? 46.493  -6.144  -16.237 1.00 33.87 ? 245 TYR B CG  1 
ATOM   4066 C CD1 . TYR B 1 245 ? 46.374  -7.159  -15.288 1.00 34.20 ? 245 TYR B CD1 1 
ATOM   4067 C CD2 . TYR B 1 245 ? 47.574  -5.264  -16.135 1.00 34.28 ? 245 TYR B CD2 1 
ATOM   4068 C CE1 . TYR B 1 245 ? 47.311  -7.300  -14.270 1.00 34.90 ? 245 TYR B CE1 1 
ATOM   4069 C CE2 . TYR B 1 245 ? 48.518  -5.398  -15.124 1.00 34.44 ? 245 TYR B CE2 1 
ATOM   4070 C CZ  . TYR B 1 245 ? 48.384  -6.416  -14.196 1.00 35.13 ? 245 TYR B CZ  1 
ATOM   4071 O OH  . TYR B 1 245 ? 49.321  -6.548  -13.192 1.00 35.67 ? 245 TYR B OH  1 
ATOM   4072 N N   . ALA B 1 246 ? 43.601  -7.222  -19.454 1.00 32.53 ? 246 ALA B N   1 
ATOM   4073 C CA  . ALA B 1 246 ? 42.384  -7.031  -20.217 1.00 32.12 ? 246 ALA B CA  1 
ATOM   4074 C C   . ALA B 1 246 ? 41.193  -7.146  -19.280 1.00 31.84 ? 246 ALA B C   1 
ATOM   4075 O O   . ALA B 1 246 ? 40.973  -8.191  -18.668 1.00 31.72 ? 246 ALA B O   1 
ATOM   4076 C CB  . ALA B 1 246 ? 42.293  -8.054  -21.343 1.00 32.20 ? 246 ALA B CB  1 
ATOM   4077 N N   . ILE B 1 247 ? 40.447  -6.056  -19.139 1.00 31.60 ? 247 ILE B N   1 
ATOM   4078 C CA  . ILE B 1 247 ? 39.214  -6.079  -18.360 1.00 31.34 ? 247 ILE B CA  1 
ATOM   4079 C C   . ILE B 1 247 ? 38.023  -5.861  -19.288 1.00 31.25 ? 247 ILE B C   1 
ATOM   4080 O O   . ILE B 1 247 ? 37.947  -4.856  -19.998 1.00 31.20 ? 247 ILE B O   1 
ATOM   4081 C CB  . ILE B 1 247 ? 39.217  -5.059  -17.194 1.00 31.39 ? 247 ILE B CB  1 
ATOM   4082 C CG1 . ILE B 1 247 ? 40.581  -5.048  -16.489 1.00 31.23 ? 247 ILE B CG1 1 
ATOM   4083 C CG2 . ILE B 1 247 ? 38.083  -5.379  -16.211 1.00 31.32 ? 247 ILE B CG2 1 
ATOM   4084 C CD1 . ILE B 1 247 ? 40.707  -4.049  -15.364 1.00 30.84 ? 247 ILE B CD1 1 
ATOM   4085 N N   . LEU B 1 248 ? 37.115  -6.833  -19.290 1.00 31.11 ? 248 LEU B N   1 
ATOM   4086 C CA  . LEU B 1 248 ? 35.929  -6.825  -20.145 1.00 31.13 ? 248 LEU B CA  1 
ATOM   4087 C C   . LEU B 1 248 ? 34.767  -7.291  -19.287 1.00 31.03 ? 248 LEU B C   1 
ATOM   4088 O O   . LEU B 1 248 ? 34.914  -8.241  -18.525 1.00 31.00 ? 248 LEU B O   1 
ATOM   4089 C CB  . LEU B 1 248 ? 36.102  -7.817  -21.296 1.00 31.12 ? 248 LEU B CB  1 
ATOM   4090 C CG  . LEU B 1 248 ? 37.542  -8.203  -21.659 1.00 31.50 ? 248 LEU B CG  1 
ATOM   4091 C CD1 . LEU B 1 248 ? 37.711  -9.716  -21.668 1.00 32.01 ? 248 LEU B CD1 1 
ATOM   4092 C CD2 . LEU B 1 248 ? 37.971  -7.567  -22.979 1.00 32.37 ? 248 LEU B CD2 1 
ATOM   4093 N N   . THR B 1 249 ? 33.615  -6.643  -19.392 1.00 31.00 ? 249 THR B N   1 
ATOM   4094 C CA  . THR B 1 249 ? 32.482  -7.074  -18.566 1.00 31.10 ? 249 THR B CA  1 
ATOM   4095 C C   . THR B 1 249 ? 31.807  -8.356  -19.053 1.00 31.20 ? 249 THR B C   1 
ATOM   4096 O O   . THR B 1 249 ? 31.464  -9.214  -18.237 1.00 31.24 ? 249 THR B O   1 
ATOM   4097 C CB  . THR B 1 249 ? 31.437  -5.952  -18.291 1.00 31.18 ? 249 THR B CB  1 
ATOM   4098 O OG1 . THR B 1 249 ? 30.111  -6.449  -18.531 1.00 30.85 ? 249 THR B OG1 1 
ATOM   4099 C CG2 . THR B 1 249 ? 31.694  -4.716  -19.162 1.00 31.04 ? 249 THR B CG2 1 
ATOM   4100 N N   . HIS B 1 250 ? 31.639  -8.498  -20.368 1.00 31.29 ? 250 HIS B N   1 
ATOM   4101 C CA  . HIS B 1 250 ? 30.992  -9.688  -20.930 1.00 31.29 ? 250 HIS B CA  1 
ATOM   4102 C C   . HIS B 1 250 ? 32.004  -10.641 -21.572 1.00 31.85 ? 250 HIS B C   1 
ATOM   4103 O O   . HIS B 1 250 ? 32.497  -10.392 -22.675 1.00 31.88 ? 250 HIS B O   1 
ATOM   4104 C CB  . HIS B 1 250 ? 29.899  -9.296  -21.937 1.00 30.97 ? 250 HIS B CB  1 
ATOM   4105 C CG  . HIS B 1 250 ? 28.928  -8.281  -21.416 1.00 29.39 ? 250 HIS B CG  1 
ATOM   4106 N ND1 . HIS B 1 250 ? 27.999  -8.572  -20.443 1.00 27.79 ? 250 HIS B ND1 1 
ATOM   4107 C CD2 . HIS B 1 250 ? 28.739  -6.977  -21.736 1.00 27.97 ? 250 HIS B CD2 1 
ATOM   4108 C CE1 . HIS B 1 250 ? 27.283  -7.493  -20.180 1.00 27.37 ? 250 HIS B CE1 1 
ATOM   4109 N NE2 . HIS B 1 250 ? 27.712  -6.510  -20.952 1.00 26.52 ? 250 HIS B NE2 1 
ATOM   4110 N N   . GLY B 1 251 ? 32.307  -11.732 -20.872 1.00 32.50 ? 251 GLY B N   1 
ATOM   4111 C CA  . GLY B 1 251 ? 33.274  -12.718 -21.351 1.00 33.29 ? 251 GLY B CA  1 
ATOM   4112 C C   . GLY B 1 251 ? 32.628  -13.923 -22.009 1.00 33.91 ? 251 GLY B C   1 
ATOM   4113 O O   . GLY B 1 251 ? 32.523  -14.987 -21.397 1.00 33.95 ? 251 GLY B O   1 
ATOM   4114 N N   . ILE B 1 252 ? 32.201  -13.751 -23.259 1.00 34.63 ? 252 ILE B N   1 
ATOM   4115 C CA  . ILE B 1 252 ? 31.545  -14.815 -24.027 1.00 35.32 ? 252 ILE B CA  1 
ATOM   4116 C C   . ILE B 1 252 ? 32.478  -16.015 -24.200 1.00 35.98 ? 252 ILE B C   1 
ATOM   4117 O O   . ILE B 1 252 ? 32.107  -17.153 -23.887 1.00 36.01 ? 252 ILE B O   1 
ATOM   4118 C CB  . ILE B 1 252 ? 31.073  -14.306 -25.416 1.00 35.24 ? 252 ILE B CB  1 
ATOM   4119 C CG1 . ILE B 1 252 ? 30.028  -13.194 -25.252 1.00 34.91 ? 252 ILE B CG1 1 
ATOM   4120 C CG2 . ILE B 1 252 ? 30.533  -15.465 -26.266 1.00 35.29 ? 252 ILE B CG2 1 
ATOM   4121 C CD1 . ILE B 1 252 ? 29.744  -12.401 -26.526 1.00 34.35 ? 252 ILE B CD1 1 
ATOM   4122 N N   . PHE B 1 253 ? 33.684  -15.738 -24.699 1.00 36.66 ? 253 PHE B N   1 
ATOM   4123 C CA  . PHE B 1 253 ? 34.744  -16.733 -24.862 1.00 37.30 ? 253 PHE B CA  1 
ATOM   4124 C C   . PHE B 1 253 ? 34.354  -17.937 -25.729 1.00 37.99 ? 253 PHE B C   1 
ATOM   4125 O O   . PHE B 1 253 ? 34.463  -19.088 -25.290 1.00 38.08 ? 253 PHE B O   1 
ATOM   4126 C CB  . PHE B 1 253 ? 35.298  -17.178 -23.497 1.00 37.08 ? 253 PHE B CB  1 
ATOM   4127 C CG  . PHE B 1 253 ? 35.928  -16.063 -22.701 1.00 36.80 ? 253 PHE B CG  1 
ATOM   4128 C CD1 . PHE B 1 253 ? 35.709  -15.961 -21.333 1.00 36.54 ? 253 PHE B CD1 1 
ATOM   4129 C CD2 . PHE B 1 253 ? 36.741  -15.111 -23.320 1.00 36.70 ? 253 PHE B CD2 1 
ATOM   4130 C CE1 . PHE B 1 253 ? 36.292  -14.930 -20.590 1.00 36.37 ? 253 PHE B CE1 1 
ATOM   4131 C CE2 . PHE B 1 253 ? 37.324  -14.076 -22.587 1.00 35.92 ? 253 PHE B CE2 1 
ATOM   4132 C CZ  . PHE B 1 253 ? 37.102  -13.988 -21.222 1.00 36.01 ? 253 PHE B CZ  1 
ATOM   4133 N N   . SER B 1 254 ? 33.909  -17.661 -26.959 1.00 38.81 ? 254 SER B N   1 
ATOM   4134 C CA  . SER B 1 254 ? 33.569  -18.719 -27.919 1.00 39.59 ? 254 SER B CA  1 
ATOM   4135 C C   . SER B 1 254 ? 34.815  -19.500 -28.304 1.00 40.13 ? 254 SER B C   1 
ATOM   4136 O O   . SER B 1 254 ? 35.890  -18.916 -28.464 1.00 40.12 ? 254 SER B O   1 
ATOM   4137 C CB  . SER B 1 254 ? 32.935  -18.148 -29.192 1.00 39.55 ? 254 SER B CB  1 
ATOM   4138 O OG  . SER B 1 254 ? 31.940  -17.115 -28.859 1.00 39.79 ? 254 SER B OG  1 
ATOM   4139 N N   . GLY B 1 255 ? 34.650  -20.816 -28.446 1.00 40.80 ? 255 GLY B N   1 
ATOM   4140 C CA  . GLY B 1 255 ? 35.712  -21.737 -28.874 1.00 41.50 ? 255 GLY B CA  1 
ATOM   4141 C C   . GLY B 1 255 ? 37.150  -21.344 -28.572 1.00 42.01 ? 255 GLY B C   1 
ATOM   4142 O O   . GLY B 1 255 ? 37.598  -21.465 -27.423 1.00 42.04 ? 255 GLY B O   1 
ATOM   4143 N N   . PRO B 1 256 ? 37.870  -20.841 -29.599 1.00 42.36 ? 256 PRO B N   1 
ATOM   4144 C CA  . PRO B 1 256 ? 39.324  -20.611 -29.602 1.00 42.70 ? 256 PRO B CA  1 
ATOM   4145 C C   . PRO B 1 256 ? 39.819  -19.599 -28.571 1.00 43.07 ? 256 PRO B C   1 
ATOM   4146 O O   . PRO B 1 256 ? 41.016  -19.559 -28.278 1.00 43.13 ? 256 PRO B O   1 
ATOM   4147 C CB  . PRO B 1 256 ? 39.587  -20.074 -31.017 1.00 42.66 ? 256 PRO B CB  1 
ATOM   4148 C CG  . PRO B 1 256 ? 38.287  -19.487 -31.444 1.00 42.58 ? 256 PRO B CG  1 
ATOM   4149 C CD  . PRO B 1 256 ? 37.259  -20.418 -30.874 1.00 42.37 ? 256 PRO B CD  1 
ATOM   4150 N N   . ALA B 1 257 ? 38.902  -18.801 -28.030 1.00 43.54 ? 257 ALA B N   1 
ATOM   4151 C CA  . ALA B 1 257 ? 39.233  -17.695 -27.130 1.00 44.10 ? 257 ALA B CA  1 
ATOM   4152 C C   . ALA B 1 257 ? 40.165  -18.041 -25.968 1.00 44.50 ? 257 ALA B C   1 
ATOM   4153 O O   . ALA B 1 257 ? 41.061  -17.259 -25.642 1.00 44.43 ? 257 ALA B O   1 
ATOM   4154 C CB  . ALA B 1 257 ? 37.970  -17.049 -26.611 1.00 44.08 ? 257 ALA B CB  1 
ATOM   4155 N N   . ILE B 1 258 ? 39.953  -19.205 -25.348 1.00 45.00 ? 258 ILE B N   1 
ATOM   4156 C CA  . ILE B 1 258 ? 40.736  -19.578 -24.172 1.00 45.47 ? 258 ILE B CA  1 
ATOM   4157 C C   . ILE B 1 258 ? 42.103  -20.167 -24.541 1.00 45.80 ? 258 ILE B C   1 
ATOM   4158 O O   . ILE B 1 258 ? 43.074  -20.000 -23.794 1.00 45.89 ? 258 ILE B O   1 
ATOM   4159 C CB  . ILE B 1 258 ? 39.951  -20.498 -23.188 1.00 45.51 ? 258 ILE B CB  1 
ATOM   4160 C CG1 . ILE B 1 258 ? 40.279  -21.984 -23.418 1.00 45.61 ? 258 ILE B CG1 1 
ATOM   4161 C CG2 . ILE B 1 258 ? 38.441  -20.200 -23.235 1.00 45.54 ? 258 ILE B CG2 1 
ATOM   4162 C CD1 . ILE B 1 258 ? 40.355  -22.794 -22.123 1.00 45.74 ? 258 ILE B CD1 1 
ATOM   4163 N N   . SER B 1 259 ? 42.176  -20.845 -25.687 1.00 46.15 ? 259 SER B N   1 
ATOM   4164 C CA  . SER B 1 259 ? 43.455  -21.313 -26.226 1.00 46.50 ? 259 SER B CA  1 
ATOM   4165 C C   . SER B 1 259 ? 44.327  -20.112 -26.558 1.00 46.62 ? 259 SER B C   1 
ATOM   4166 O O   . SER B 1 259 ? 45.547  -20.138 -26.364 1.00 46.64 ? 259 SER B O   1 
ATOM   4167 C CB  . SER B 1 259 ? 43.250  -22.174 -27.479 1.00 46.56 ? 259 SER B CB  1 
ATOM   4168 O OG  . SER B 1 259 ? 42.963  -23.522 -27.135 1.00 46.86 ? 259 SER B OG  1 
ATOM   4169 N N   . ARG B 1 260 ? 43.675  -19.060 -27.050 1.00 46.87 ? 260 ARG B N   1 
ATOM   4170 C CA  . ARG B 1 260 ? 44.341  -17.813 -27.406 1.00 47.09 ? 260 ARG B CA  1 
ATOM   4171 C C   . ARG B 1 260 ? 44.777  -17.006 -26.182 1.00 47.25 ? 260 ARG B C   1 
ATOM   4172 O O   . ARG B 1 260 ? 45.845  -16.392 -26.191 1.00 47.33 ? 260 ARG B O   1 
ATOM   4173 C CB  . ARG B 1 260 ? 43.450  -16.988 -28.343 1.00 47.04 ? 260 ARG B CB  1 
ATOM   4174 C CG  . ARG B 1 260 ? 43.694  -17.309 -29.810 1.00 46.98 ? 260 ARG B CG  1 
ATOM   4175 C CD  . ARG B 1 260 ? 42.415  -17.553 -30.586 1.00 46.71 ? 260 ARG B CD  1 
ATOM   4176 N NE  . ARG B 1 260 ? 41.816  -16.328 -31.113 1.00 46.79 ? 260 ARG B NE  1 
ATOM   4177 C CZ  . ARG B 1 260 ? 41.083  -16.273 -32.225 1.00 46.70 ? 260 ARG B CZ  1 
ATOM   4178 N NH1 . ARG B 1 260 ? 40.871  -17.366 -32.950 1.00 46.77 ? 260 ARG B NH1 1 
ATOM   4179 N NH2 . ARG B 1 260 ? 40.568  -15.121 -32.624 1.00 46.60 ? 260 ARG B NH2 1 
ATOM   4180 N N   . ILE B 1 261 ? 43.958  -17.026 -25.131 1.00 47.50 ? 261 ILE B N   1 
ATOM   4181 C CA  . ILE B 1 261 ? 44.274  -16.330 -23.880 1.00 47.72 ? 261 ILE B CA  1 
ATOM   4182 C C   . ILE B 1 261 ? 45.508  -16.933 -23.197 1.00 47.96 ? 261 ILE B C   1 
ATOM   4183 O O   . ILE B 1 261 ? 46.376  -16.200 -22.709 1.00 48.06 ? 261 ILE B O   1 
ATOM   4184 C CB  . ILE B 1 261 ? 43.048  -16.289 -22.924 1.00 47.71 ? 261 ILE B CB  1 
ATOM   4185 C CG1 . ILE B 1 261 ? 42.057  -15.216 -23.398 1.00 47.49 ? 261 ILE B CG1 1 
ATOM   4186 C CG2 . ILE B 1 261 ? 43.482  -15.984 -21.488 1.00 47.77 ? 261 ILE B CG2 1 
ATOM   4187 C CD1 . ILE B 1 261 ? 40.647  -15.386 -22.860 1.00 47.02 ? 261 ILE B CD1 1 
ATOM   4188 N N   . ASN B 1 262 ? 45.579  -18.266 -23.185 1.00 48.16 ? 262 ASN B N   1 
ATOM   4189 C CA  . ASN B 1 262 ? 46.756  -18.979 -22.677 1.00 48.30 ? 262 ASN B CA  1 
ATOM   4190 C C   . ASN B 1 262 ? 48.023  -18.762 -23.521 1.00 48.32 ? 262 ASN B C   1 
ATOM   4191 O O   . ASN B 1 262 ? 49.136  -18.796 -22.992 1.00 48.38 ? 262 ASN B O   1 
ATOM   4192 C CB  . ASN B 1 262 ? 46.459  -20.478 -22.546 1.00 48.35 ? 262 ASN B CB  1 
ATOM   4193 C CG  . ASN B 1 262 ? 45.452  -20.792 -21.439 1.00 48.69 ? 262 ASN B CG  1 
ATOM   4194 O OD1 . ASN B 1 262 ? 44.495  -21.539 -21.654 1.00 49.09 ? 262 ASN B OD1 1 
ATOM   4195 N ND2 . ASN B 1 262 ? 45.673  -20.234 -20.249 1.00 48.81 ? 262 ASN B ND2 1 
ATOM   4196 N N   . ASN B 1 263 ? 47.847  -18.536 -24.824 1.00 48.29 ? 263 ASN B N   1 
ATOM   4197 C CA  . ASN B 1 263 ? 48.970  -18.314 -25.740 1.00 48.32 ? 263 ASN B CA  1 
ATOM   4198 C C   . ASN B 1 263 ? 49.531  -16.889 -25.742 1.00 48.12 ? 263 ASN B C   1 
ATOM   4199 O O   . ASN B 1 263 ? 50.744  -16.700 -25.909 1.00 48.09 ? 263 ASN B O   1 
ATOM   4200 C CB  . ASN B 1 263 ? 48.600  -18.725 -27.171 1.00 48.51 ? 263 ASN B CB  1 
ATOM   4201 C CG  . ASN B 1 263 ? 49.126  -20.109 -27.545 1.00 49.09 ? 263 ASN B CG  1 
ATOM   4202 O OD1 . ASN B 1 263 ? 50.314  -20.403 -27.386 1.00 49.56 ? 263 ASN B OD1 1 
ATOM   4203 N ND2 . ASN B 1 263 ? 48.244  -20.957 -28.063 1.00 49.54 ? 263 ASN B ND2 1 
ATOM   4204 N N   . ALA B 1 264 ? 48.650  -15.895 -25.566 1.00 47.87 ? 264 ALA B N   1 
ATOM   4205 C CA  . ALA B 1 264 ? 49.075  -14.491 -25.591 1.00 47.54 ? 264 ALA B CA  1 
ATOM   4206 C C   . ALA B 1 264 ? 49.606  -14.033 -24.235 1.00 47.26 ? 264 ALA B C   1 
ATOM   4207 O O   . ALA B 1 264 ? 49.193  -14.541 -23.188 1.00 47.17 ? 264 ALA B O   1 
ATOM   4208 C CB  . ALA B 1 264 ? 47.933  -13.580 -26.061 1.00 47.53 ? 264 ALA B CB  1 
ATOM   4209 N N   . CYS B 1 265 ? 50.525  -13.070 -24.269 1.00 46.83 ? 265 CYS B N   1 
ATOM   4210 C CA  . CYS B 1 265 ? 51.105  -12.510 -23.057 1.00 46.44 ? 265 CYS B CA  1 
ATOM   4211 C C   . CYS B 1 265 ? 50.136  -11.559 -22.357 1.00 45.77 ? 265 CYS B C   1 
ATOM   4212 O O   . CYS B 1 265 ? 50.247  -10.333 -22.470 1.00 45.84 ? 265 CYS B O   1 
ATOM   4213 C CB  . CYS B 1 265 ? 52.430  -11.808 -23.362 1.00 46.60 ? 265 CYS B CB  1 
ATOM   4214 S SG  . CYS B 1 265 ? 53.771  -12.921 -23.821 1.00 48.21 ? 265 CYS B SG  1 
ATOM   4215 N N   . PHE B 1 266 ? 49.173  -12.146 -21.654 1.00 44.93 ? 266 PHE B N   1 
ATOM   4216 C CA  . PHE B 1 266 ? 48.311  -11.409 -20.744 1.00 44.08 ? 266 PHE B CA  1 
ATOM   4217 C C   . PHE B 1 266 ? 48.784  -11.671 -19.320 1.00 43.48 ? 266 PHE B C   1 
ATOM   4218 O O   . PHE B 1 266 ? 49.119  -12.807 -18.973 1.00 43.36 ? 266 PHE B O   1 
ATOM   4219 C CB  . PHE B 1 266 ? 46.852  -11.864 -20.873 1.00 44.07 ? 266 PHE B CB  1 
ATOM   4220 C CG  . PHE B 1 266 ? 46.137  -11.328 -22.084 1.00 43.88 ? 266 PHE B CG  1 
ATOM   4221 C CD1 . PHE B 1 266 ? 45.590  -12.202 -23.022 1.00 43.66 ? 266 PHE B CD1 1 
ATOM   4222 C CD2 . PHE B 1 266 ? 45.987  -9.956  -22.278 1.00 44.00 ? 266 PHE B CD2 1 
ATOM   4223 C CE1 . PHE B 1 266 ? 44.916  -11.719 -24.141 1.00 43.61 ? 266 PHE B CE1 1 
ATOM   4224 C CE2 . PHE B 1 266 ? 45.315  -9.462  -23.394 1.00 43.74 ? 266 PHE B CE2 1 
ATOM   4225 C CZ  . PHE B 1 266 ? 44.780  -10.346 -24.327 1.00 43.78 ? 266 PHE B CZ  1 
ATOM   4226 N N   . GLU B 1 267 ? 48.820  -10.621 -18.501 1.00 42.68 ? 267 GLU B N   1 
ATOM   4227 C CA  . GLU B 1 267 ? 49.012  -10.795 -17.065 1.00 41.98 ? 267 GLU B CA  1 
ATOM   4228 C C   . GLU B 1 267 ? 47.795  -11.496 -16.476 1.00 41.34 ? 267 GLU B C   1 
ATOM   4229 O O   . GLU B 1 267 ? 47.920  -12.509 -15.783 1.00 41.46 ? 267 GLU B O   1 
ATOM   4230 C CB  . GLU B 1 267 ? 49.249  -9.453  -16.369 1.00 42.11 ? 267 GLU B CB  1 
ATOM   4231 C CG  . GLU B 1 267 ? 50.703  -9.015  -16.342 1.00 42.49 ? 267 GLU B CG  1 
ATOM   4232 C CD  . GLU B 1 267 ? 51.568  -9.893  -15.433 1.00 43.04 ? 267 GLU B CD  1 
ATOM   4233 O OE1 . GLU B 1 267 ? 52.807  -9.886  -15.609 1.00 43.04 ? 267 GLU B OE1 1 
ATOM   4234 O OE2 . GLU B 1 267 ? 51.010  -10.587 -14.543 1.00 43.68 ? 267 GLU B OE2 1 
ATOM   4235 N N   . ALA B 1 268 ? 46.621  -10.938 -16.768 1.00 40.38 ? 268 ALA B N   1 
ATOM   4236 C CA  . ALA B 1 268 ? 45.340  -11.546 -16.433 1.00 39.37 ? 268 ALA B CA  1 
ATOM   4237 C C   . ALA B 1 268 ? 44.255  -11.015 -17.367 1.00 38.65 ? 268 ALA B C   1 
ATOM   4238 O O   . ALA B 1 268 ? 44.335  -9.886  -17.854 1.00 38.56 ? 268 ALA B O   1 
ATOM   4239 C CB  . ALA B 1 268 ? 44.973  -11.270 -14.977 1.00 39.42 ? 268 ALA B CB  1 
ATOM   4240 N N   . VAL B 1 269 ? 43.257  -11.846 -17.637 1.00 37.73 ? 269 VAL B N   1 
ATOM   4241 C CA  . VAL B 1 269 ? 42.053  -11.392 -18.316 1.00 36.91 ? 269 VAL B CA  1 
ATOM   4242 C C   . VAL B 1 269 ? 40.941  -11.381 -17.273 1.00 36.23 ? 269 VAL B C   1 
ATOM   4243 O O   . VAL B 1 269 ? 40.593  -12.421 -16.712 1.00 36.02 ? 269 VAL B O   1 
ATOM   4244 C CB  . VAL B 1 269 ? 41.671  -12.295 -19.515 1.00 36.88 ? 269 VAL B CB  1 
ATOM   4245 C CG1 . VAL B 1 269 ? 40.562  -11.642 -20.322 1.00 36.89 ? 269 VAL B CG1 1 
ATOM   4246 C CG2 . VAL B 1 269 ? 42.885  -12.524 -20.415 1.00 37.11 ? 269 VAL B CG2 1 
ATOM   4247 N N   . VAL B 1 270 ? 40.410  -10.196 -16.996 1.00 35.41 ? 270 VAL B N   1 
ATOM   4248 C CA  . VAL B 1 270 ? 39.368  -10.049 -15.990 1.00 34.66 ? 270 VAL B CA  1 
ATOM   4249 C C   . VAL B 1 270 ? 38.017  -9.843  -16.650 1.00 34.22 ? 270 VAL B C   1 
ATOM   4250 O O   . VAL B 1 270 ? 37.873  -9.038  -17.570 1.00 34.17 ? 270 VAL B O   1 
ATOM   4251 C CB  . VAL B 1 270 ? 39.645  -8.880  -15.010 1.00 34.69 ? 270 VAL B CB  1 
ATOM   4252 C CG1 . VAL B 1 270 ? 38.856  -9.082  -13.719 1.00 34.67 ? 270 VAL B CG1 1 
ATOM   4253 C CG2 . VAL B 1 270 ? 41.131  -8.776  -14.702 1.00 34.27 ? 270 VAL B CG2 1 
ATOM   4254 N N   . VAL B 1 271 ? 37.034  -10.599 -16.178 1.00 33.70 ? 271 VAL B N   1 
ATOM   4255 C CA  . VAL B 1 271 ? 35.651  -10.428 -16.595 1.00 33.09 ? 271 VAL B CA  1 
ATOM   4256 C C   . VAL B 1 271 ? 34.735  -10.406 -15.375 1.00 32.70 ? 271 VAL B C   1 
ATOM   4257 O O   . VAL B 1 271 ? 35.166  -10.694 -14.258 1.00 32.58 ? 271 VAL B O   1 
ATOM   4258 C CB  . VAL B 1 271 ? 35.191  -11.531 -17.594 1.00 33.12 ? 271 VAL B CB  1 
ATOM   4259 C CG1 . VAL B 1 271 ? 35.761  -11.276 -18.981 1.00 33.06 ? 271 VAL B CG1 1 
ATOM   4260 C CG2 . VAL B 1 271 ? 35.566  -12.932 -17.098 1.00 32.75 ? 271 VAL B CG2 1 
ATOM   4261 N N   . THR B 1 272 ? 33.477  -10.043 -15.600 1.00 32.35 ? 272 THR B N   1 
ATOM   4262 C CA  . THR B 1 272 ? 32.440  -10.165 -14.580 1.00 31.88 ? 272 THR B CA  1 
ATOM   4263 C C   . THR B 1 272 ? 31.724  -11.496 -14.797 1.00 31.87 ? 272 THR B C   1 
ATOM   4264 O O   . THR B 1 272 ? 31.818  -12.082 -15.884 1.00 31.64 ? 272 THR B O   1 
ATOM   4265 C CB  . THR B 1 272 ? 31.414  -9.022  -14.677 1.00 31.79 ? 272 THR B CB  1 
ATOM   4266 O OG1 . THR B 1 272 ? 30.578  -9.223  -15.823 1.00 31.02 ? 272 THR B OG1 1 
ATOM   4267 C CG2 . THR B 1 272 ? 32.115  -7.665  -14.781 1.00 31.22 ? 272 THR B CG2 1 
ATOM   4268 N N   . ASN B 1 273 ? 31.011  -11.974 -13.776 1.00 31.89 ? 273 ASN B N   1 
ATOM   4269 C CA  . ASN B 1 273 ? 30.254  -13.225 -13.911 1.00 31.99 ? 273 ASN B CA  1 
ATOM   4270 C C   . ASN B 1 273 ? 28.872  -13.017 -14.528 1.00 32.12 ? 273 ASN B C   1 
ATOM   4271 O O   . ASN B 1 273 ? 27.969  -13.835 -14.351 1.00 32.28 ? 273 ASN B O   1 
ATOM   4272 C CB  . ASN B 1 273 ? 30.170  -13.987 -12.582 1.00 31.82 ? 273 ASN B CB  1 
ATOM   4273 C CG  . ASN B 1 273 ? 29.413  -13.229 -11.521 1.00 31.72 ? 273 ASN B CG  1 
ATOM   4274 O OD1 . ASN B 1 273 ? 29.352  -12.001 -11.537 1.00 31.57 ? 273 ASN B OD1 1 
ATOM   4275 N ND2 . ASN B 1 273 ? 28.831  -13.962 -10.583 1.00 32.50 ? 273 ASN B ND2 1 
ATOM   4276 N N   . THR B 1 274 ? 28.726  -11.910 -15.252 1.00 32.37 ? 274 THR B N   1 
ATOM   4277 C CA  . THR B 1 274 ? 27.587  -11.658 -16.129 1.00 32.66 ? 274 THR B CA  1 
ATOM   4278 C C   . THR B 1 274 ? 27.285  -12.889 -16.992 1.00 33.13 ? 274 THR B C   1 
ATOM   4279 O O   . THR B 1 274 ? 26.132  -13.163 -17.342 1.00 32.89 ? 274 THR B O   1 
ATOM   4280 C CB  . THR B 1 274 ? 27.881  -10.408 -17.006 1.00 32.54 ? 274 THR B CB  1 
ATOM   4281 O OG1 . THR B 1 274 ? 27.259  -9.257  -16.420 1.00 32.32 ? 274 THR B OG1 1 
ATOM   4282 C CG2 . THR B 1 274 ? 27.380  -10.569 -18.429 1.00 32.49 ? 274 THR B CG2 1 
ATOM   4283 N N   . ILE B 1 275 ? 28.348  -13.624 -17.313 1.00 33.95 ? 275 ILE B N   1 
ATOM   4284 C CA  . ILE B 1 275 ? 28.285  -14.870 -18.061 1.00 34.87 ? 275 ILE B CA  1 
ATOM   4285 C C   . ILE B 1 275 ? 29.018  -15.916 -17.205 1.00 35.82 ? 275 ILE B C   1 
ATOM   4286 O O   . ILE B 1 275 ? 30.013  -15.583 -16.562 1.00 35.94 ? 275 ILE B O   1 
ATOM   4287 C CB  . ILE B 1 275 ? 28.931  -14.689 -19.474 1.00 34.66 ? 275 ILE B CB  1 
ATOM   4288 C CG1 . ILE B 1 275 ? 28.162  -13.616 -20.267 1.00 34.35 ? 275 ILE B CG1 1 
ATOM   4289 C CG2 . ILE B 1 275 ? 28.996  -16.010 -20.244 1.00 34.75 ? 275 ILE B CG2 1 
ATOM   4290 C CD1 . ILE B 1 275 ? 28.562  -13.476 -21.750 1.00 33.87 ? 275 ILE B CD1 1 
ATOM   4291 N N   . PRO B 1 276 ? 28.506  -17.166 -17.153 1.00 36.82 ? 276 PRO B N   1 
ATOM   4292 C CA  . PRO B 1 276 ? 29.146  -18.237 -16.372 1.00 37.62 ? 276 PRO B CA  1 
ATOM   4293 C C   . PRO B 1 276 ? 30.600  -18.489 -16.773 1.00 38.54 ? 276 PRO B C   1 
ATOM   4294 O O   . PRO B 1 276 ? 30.881  -18.746 -17.946 1.00 38.57 ? 276 PRO B O   1 
ATOM   4295 C CB  . PRO B 1 276 ? 28.291  -19.466 -16.703 1.00 37.50 ? 276 PRO B CB  1 
ATOM   4296 C CG  . PRO B 1 276 ? 26.974  -18.912 -17.086 1.00 37.20 ? 276 PRO B CG  1 
ATOM   4297 C CD  . PRO B 1 276 ? 27.271  -17.639 -17.808 1.00 36.89 ? 276 PRO B CD  1 
ATOM   4298 N N   . GLN B 1 277 ? 31.509  -18.422 -15.800 1.00 39.75 ? 277 GLN B N   1 
ATOM   4299 C CA  . GLN B 1 277 ? 32.947  -18.554 -16.068 1.00 41.06 ? 277 GLN B CA  1 
ATOM   4300 C C   . GLN B 1 277 ? 33.601  -19.787 -15.422 1.00 42.02 ? 277 GLN B C   1 
ATOM   4301 O O   . GLN B 1 277 ? 34.788  -20.053 -15.654 1.00 42.15 ? 277 GLN B O   1 
ATOM   4302 C CB  . GLN B 1 277 ? 33.701  -17.287 -15.637 1.00 40.91 ? 277 GLN B CB  1 
ATOM   4303 C CG  . GLN B 1 277 ? 33.195  -15.970 -16.237 1.00 41.34 ? 277 GLN B CG  1 
ATOM   4304 C CD  . GLN B 1 277 ? 33.360  -15.882 -17.752 1.00 41.78 ? 277 GLN B CD  1 
ATOM   4305 O OE1 . GLN B 1 277 ? 34.316  -16.414 -18.322 1.00 42.60 ? 277 GLN B OE1 1 
ATOM   4306 N NE2 . GLN B 1 277 ? 32.426  -15.197 -18.410 1.00 41.51 ? 277 GLN B NE2 1 
ATOM   4307 N N   . GLU B 1 278 ? 32.829  -20.529 -14.623 1.00 43.22 ? 278 GLU B N   1 
ATOM   4308 C CA  . GLU B 1 278 ? 33.345  -21.694 -13.883 1.00 44.36 ? 278 GLU B CA  1 
ATOM   4309 C C   . GLU B 1 278 ? 34.107  -22.689 -14.757 1.00 44.89 ? 278 GLU B C   1 
ATOM   4310 O O   . GLU B 1 278 ? 35.256  -23.037 -14.447 1.00 44.90 ? 278 GLU B O   1 
ATOM   4311 C CB  . GLU B 1 278 ? 32.213  -22.401 -13.120 1.00 44.47 ? 278 GLU B CB  1 
ATOM   4312 C CG  . GLU B 1 278 ? 32.119  -22.051 -11.625 1.00 45.39 ? 278 GLU B CG  1 
ATOM   4313 C CD  . GLU B 1 278 ? 31.618  -20.627 -11.342 1.00 46.89 ? 278 GLU B CD  1 
ATOM   4314 O OE1 . GLU B 1 278 ? 31.490  -19.816 -12.287 1.00 47.50 ? 278 GLU B OE1 1 
ATOM   4315 O OE2 . GLU B 1 278 ? 31.350  -20.320 -10.156 1.00 47.13 ? 278 GLU B OE2 1 
ATOM   4316 N N   . ASP B 1 279 ? 33.471  -23.125 -15.849 1.00 45.74 ? 279 ASP B N   1 
ATOM   4317 C CA  . ASP B 1 279 ? 34.076  -24.098 -16.766 1.00 46.56 ? 279 ASP B CA  1 
ATOM   4318 C C   . ASP B 1 279 ? 35.285  -23.568 -17.532 1.00 46.84 ? 279 ASP B C   1 
ATOM   4319 O O   . ASP B 1 279 ? 36.187  -24.332 -17.870 1.00 46.98 ? 279 ASP B O   1 
ATOM   4320 C CB  . ASP B 1 279 ? 33.035  -24.646 -17.749 1.00 46.74 ? 279 ASP B CB  1 
ATOM   4321 C CG  . ASP B 1 279 ? 32.440  -25.972 -17.296 1.00 47.59 ? 279 ASP B CG  1 
ATOM   4322 O OD1 . ASP B 1 279 ? 33.162  -26.770 -16.650 1.00 48.50 ? 279 ASP B OD1 1 
ATOM   4323 O OD2 . ASP B 1 279 ? 31.250  -26.224 -17.601 1.00 48.40 ? 279 ASP B OD2 1 
ATOM   4324 N N   . LYS B 1 280 ? 35.300  -22.266 -17.809 1.00 47.25 ? 280 LYS B N   1 
ATOM   4325 C CA  . LYS B 1 280 ? 36.401  -21.659 -18.561 1.00 47.56 ? 280 LYS B CA  1 
ATOM   4326 C C   . LYS B 1 280 ? 37.646  -21.417 -17.705 1.00 47.78 ? 280 LYS B C   1 
ATOM   4327 O O   . LYS B 1 280 ? 38.773  -21.557 -18.191 1.00 47.83 ? 280 LYS B O   1 
ATOM   4328 C CB  . LYS B 1 280 ? 35.941  -20.387 -19.277 1.00 47.51 ? 280 LYS B CB  1 
ATOM   4329 C CG  . LYS B 1 280 ? 35.538  -20.661 -20.717 1.00 47.55 ? 280 LYS B CG  1 
ATOM   4330 C CD  . LYS B 1 280 ? 34.231  -19.994 -21.094 1.00 47.52 ? 280 LYS B CD  1 
ATOM   4331 C CE  . LYS B 1 280 ? 33.711  -20.553 -22.414 1.00 47.19 ? 280 LYS B CE  1 
ATOM   4332 N NZ  . LYS B 1 280 ? 32.265  -20.224 -22.614 1.00 47.17 ? 280 LYS B NZ  1 
ATOM   4333 N N   . MET B 1 281 ? 37.436  -21.066 -16.436 1.00 48.00 ? 281 MET B N   1 
ATOM   4334 C CA  . MET B 1 281 ? 38.535  -20.893 -15.479 1.00 48.14 ? 281 MET B CA  1 
ATOM   4335 C C   . MET B 1 281 ? 39.276  -22.209 -15.241 1.00 48.05 ? 281 MET B C   1 
ATOM   4336 O O   . MET B 1 281 ? 40.444  -22.207 -14.836 1.00 48.11 ? 281 MET B O   1 
ATOM   4337 C CB  . MET B 1 281 ? 38.017  -20.330 -14.149 1.00 48.30 ? 281 MET B CB  1 
ATOM   4338 C CG  . MET B 1 281 ? 37.489  -18.901 -14.251 1.00 48.71 ? 281 MET B CG  1 
ATOM   4339 S SD  . MET B 1 281 ? 36.300  -18.516 -12.952 1.00 49.67 ? 281 MET B SD  1 
ATOM   4340 C CE  . MET B 1 281 ? 37.386  -18.248 -11.549 1.00 49.43 ? 281 MET B CE  1 
ATOM   4341 N N   . LYS B 1 282 ? 38.591  -23.326 -15.498 1.00 47.93 ? 282 LYS B N   1 
ATOM   4342 C CA  . LYS B 1 282 ? 39.211  -24.647 -15.418 1.00 47.80 ? 282 LYS B CA  1 
ATOM   4343 C C   . LYS B 1 282 ? 40.451  -24.720 -16.315 1.00 47.68 ? 282 LYS B C   1 
ATOM   4344 O O   . LYS B 1 282 ? 41.569  -24.877 -15.814 1.00 47.83 ? 282 LYS B O   1 
ATOM   4345 C CB  . LYS B 1 282 ? 38.208  -25.746 -15.786 1.00 47.74 ? 282 LYS B CB  1 
ATOM   4346 N N   . HIS B 1 283 ? 40.260  -24.570 -17.626 1.00 47.39 ? 283 HIS B N   1 
ATOM   4347 C CA  . HIS B 1 283 ? 41.371  -24.701 -18.578 1.00 47.10 ? 283 HIS B CA  1 
ATOM   4348 C C   . HIS B 1 283 ? 42.051  -23.359 -18.895 1.00 46.66 ? 283 HIS B C   1 
ATOM   4349 O O   . HIS B 1 283 ? 42.791  -23.251 -19.880 1.00 46.55 ? 283 HIS B O   1 
ATOM   4350 C CB  . HIS B 1 283 ? 40.935  -25.403 -19.883 1.00 47.28 ? 283 HIS B CB  1 
ATOM   4351 C CG  . HIS B 1 283 ? 39.644  -26.167 -19.778 1.00 47.95 ? 283 HIS B CG  1 
ATOM   4352 N ND1 . HIS B 1 283 ? 39.444  -27.172 -18.819 1.00 48.45 ? 283 HIS B ND1 1 
ATOM   4353 C CD2 . HIS B 1 283 ? 38.493  -26.085 -20.538 1.00 48.38 ? 283 HIS B CD2 1 
ATOM   4354 C CE1 . HIS B 1 283 ? 38.221  -27.662 -18.979 1.00 48.62 ? 283 HIS B CE1 1 
ATOM   4355 N NE2 . HIS B 1 283 ? 37.624  -27.022 -20.017 1.00 48.69 ? 283 HIS B NE2 1 
ATOM   4356 N N   . CYS B 1 284 ? 41.801  -22.347 -18.062 1.00 46.04 ? 284 CYS B N   1 
ATOM   4357 C CA  . CYS B 1 284 ? 42.451  -21.041 -18.215 1.00 45.50 ? 284 CYS B CA  1 
ATOM   4358 C C   . CYS B 1 284 ? 42.720  -20.353 -16.873 1.00 44.92 ? 284 CYS B C   1 
ATOM   4359 O O   . CYS B 1 284 ? 41.797  -19.866 -16.214 1.00 44.95 ? 284 CYS B O   1 
ATOM   4360 C CB  . CYS B 1 284 ? 41.641  -20.127 -19.139 1.00 45.54 ? 284 CYS B CB  1 
ATOM   4361 S SG  . CYS B 1 284 ? 42.542  -18.635 -19.659 1.00 46.45 ? 284 CYS B SG  1 
ATOM   4362 N N   . SER B 1 285 ? 43.995  -20.321 -16.484 1.00 44.11 ? 285 SER B N   1 
ATOM   4363 C CA  . SER B 1 285 ? 44.430  -19.726 -15.214 1.00 43.20 ? 285 SER B CA  1 
ATOM   4364 C C   . SER B 1 285 ? 44.459  -18.200 -15.235 1.00 42.42 ? 285 SER B C   1 
ATOM   4365 O O   . SER B 1 285 ? 44.269  -17.558 -14.192 1.00 42.43 ? 285 SER B O   1 
ATOM   4366 C CB  . SER B 1 285 ? 45.798  -20.278 -14.781 1.00 43.34 ? 285 SER B CB  1 
ATOM   4367 O OG  . SER B 1 285 ? 46.608  -20.622 -15.951 1.00 43.48 ? 285 SER B OG  1 
ATOM   4368 N N   . LYS B 1 286 ? 44.690  -17.629 -16.420 1.00 41.37 ? 286 LYS B N   1 
ATOM   4369 C CA  . LYS B 1 286 ? 44.740  -16.168 -16.590 1.00 40.32 ? 286 LYS B CA  1 
ATOM   4370 C C   . LYS B 1 286 ? 43.410  -15.462 -16.284 1.00 39.50 ? 286 LYS B C   1 
ATOM   4371 O O   . LYS B 1 286 ? 43.403  -14.292 -15.897 1.00 39.52 ? 286 LYS B O   1 
ATOM   4372 C CB  . LYS B 1 286 ? 45.216  -15.808 -18.001 1.00 40.29 ? 286 LYS B CB  1 
ATOM   4373 N N   . ILE B 1 287 ? 42.296  -16.174 -16.447 1.00 38.36 ? 287 ILE B N   1 
ATOM   4374 C CA  . ILE B 1 287 ? 40.968  -15.594 -16.229 1.00 37.33 ? 287 ILE B CA  1 
ATOM   4375 C C   . ILE B 1 287 ? 40.662  -15.371 -14.749 1.00 36.66 ? 287 ILE B C   1 
ATOM   4376 O O   . ILE B 1 287 ? 40.773  -16.282 -13.935 1.00 36.71 ? 287 ILE B O   1 
ATOM   4377 C CB  . ILE B 1 287 ? 39.834  -16.438 -16.891 1.00 37.35 ? 287 ILE B CB  1 
ATOM   4378 C CG1 . ILE B 1 287 ? 39.963  -16.405 -18.419 1.00 37.16 ? 287 ILE B CG1 1 
ATOM   4379 C CG2 . ILE B 1 287 ? 38.448  -15.929 -16.465 1.00 37.02 ? 287 ILE B CG2 1 
ATOM   4380 C CD1 . ILE B 1 287 ? 39.102  -17.424 -19.140 1.00 37.08 ? 287 ILE B CD1 1 
ATOM   4381 N N   . GLN B 1 288 ? 40.289  -14.140 -14.418 1.00 35.75 ? 288 GLN B N   1 
ATOM   4382 C CA  . GLN B 1 288 ? 39.745  -13.814 -13.109 1.00 34.89 ? 288 GLN B CA  1 
ATOM   4383 C C   . GLN B 1 288 ? 38.337  -13.261 -13.255 1.00 34.27 ? 288 GLN B C   1 
ATOM   4384 O O   . GLN B 1 288 ? 37.997  -12.674 -14.286 1.00 34.20 ? 288 GLN B O   1 
ATOM   4385 C CB  . GLN B 1 288 ? 40.636  -12.807 -12.389 1.00 34.93 ? 288 GLN B CB  1 
ATOM   4386 C CG  . GLN B 1 288 ? 41.563  -13.447 -11.384 1.00 35.07 ? 288 GLN B CG  1 
ATOM   4387 C CD  . GLN B 1 288 ? 42.809  -12.634 -11.156 1.00 35.09 ? 288 GLN B CD  1 
ATOM   4388 O OE1 . GLN B 1 288 ? 43.635  -12.482 -12.055 1.00 34.95 ? 288 GLN B OE1 1 
ATOM   4389 N NE2 . GLN B 1 288 ? 42.962  -12.114 -9.944  1.00 35.29 ? 288 GLN B NE2 1 
ATOM   4390 N N   . VAL B 1 289 ? 37.522  -13.453 -12.221 1.00 33.46 ? 289 VAL B N   1 
ATOM   4391 C CA  . VAL B 1 289 ? 36.131  -13.016 -12.255 1.00 32.74 ? 289 VAL B CA  1 
ATOM   4392 C C   . VAL B 1 289 ? 35.827  -11.994 -11.162 1.00 32.29 ? 289 VAL B C   1 
ATOM   4393 O O   . VAL B 1 289 ? 36.263  -12.144 -10.017 1.00 32.23 ? 289 VAL B O   1 
ATOM   4394 C CB  . VAL B 1 289 ? 35.155  -14.212 -12.146 1.00 32.68 ? 289 VAL B CB  1 
ATOM   4395 C CG1 . VAL B 1 289 ? 33.724  -13.757 -12.352 1.00 32.37 ? 289 VAL B CG1 1 
ATOM   4396 C CG2 . VAL B 1 289 ? 35.500  -15.266 -13.173 1.00 32.77 ? 289 VAL B CG2 1 
ATOM   4397 N N   . ILE B 1 290 ? 35.097  -10.947 -11.538 1.00 31.75 ? 290 ILE B N   1 
ATOM   4398 C CA  . ILE B 1 290 ? 34.506  -10.023 -10.577 1.00 31.26 ? 290 ILE B CA  1 
ATOM   4399 C C   . ILE B 1 290 ? 33.040  -10.401 -10.416 1.00 31.02 ? 290 ILE B C   1 
ATOM   4400 O O   . ILE B 1 290 ? 32.322  -10.564 -11.404 1.00 31.12 ? 290 ILE B O   1 
ATOM   4401 C CB  . ILE B 1 290 ? 34.593  -8.557  -11.045 1.00 31.21 ? 290 ILE B CB  1 
ATOM   4402 C CG1 . ILE B 1 290 ? 36.042  -8.180  -11.365 1.00 30.84 ? 290 ILE B CG1 1 
ATOM   4403 C CG2 . ILE B 1 290 ? 33.991  -7.623  -9.986  1.00 31.15 ? 290 ILE B CG2 1 
ATOM   4404 C CD1 . ILE B 1 290 ? 36.165  -6.784  -12.032 1.00 31.02 ? 290 ILE B CD1 1 
ATOM   4405 N N   . ASP B 1 291 ? 32.604  -10.546 -9.170  1.00 30.68 ? 291 ASP B N   1 
ATOM   4406 C CA  . ASP B 1 291 ? 31.214  -10.867 -8.872  1.00 30.45 ? 291 ASP B CA  1 
ATOM   4407 C C   . ASP B 1 291 ? 30.362  -9.602  -8.936  1.00 30.02 ? 291 ASP B C   1 
ATOM   4408 O O   . ASP B 1 291 ? 30.602  -8.644  -8.202  1.00 29.97 ? 291 ASP B O   1 
ATOM   4409 C CB  . ASP B 1 291 ? 31.114  -11.522 -7.490  1.00 30.63 ? 291 ASP B CB  1 
ATOM   4410 C CG  . ASP B 1 291 ? 29.735  -12.087 -7.202  1.00 31.14 ? 291 ASP B CG  1 
ATOM   4411 O OD1 . ASP B 1 291 ? 28.894  -12.154 -8.124  1.00 31.63 ? 291 ASP B OD1 1 
ATOM   4412 O OD2 . ASP B 1 291 ? 29.492  -12.474 -6.040  1.00 32.21 ? 291 ASP B OD2 1 
ATOM   4413 N N   . ILE B 1 292 ? 29.374  -9.601  -9.824  1.00 29.67 ? 292 ILE B N   1 
ATOM   4414 C CA  . ILE B 1 292 ? 28.492  -8.440  -9.996  1.00 29.29 ? 292 ILE B CA  1 
ATOM   4415 C C   . ILE B 1 292 ? 27.072  -8.693  -9.467  1.00 29.08 ? 292 ILE B C   1 
ATOM   4416 O O   . ILE B 1 292 ? 26.167  -7.873  -9.661  1.00 29.12 ? 292 ILE B O   1 
ATOM   4417 C CB  . ILE B 1 292 ? 28.469  -7.928  -11.476 1.00 29.25 ? 292 ILE B CB  1 
ATOM   4418 C CG1 . ILE B 1 292 ? 28.260  -9.077  -12.473 1.00 29.09 ? 292 ILE B CG1 1 
ATOM   4419 C CG2 . ILE B 1 292 ? 29.767  -7.196  -11.808 1.00 28.87 ? 292 ILE B CG2 1 
ATOM   4420 C CD1 . ILE B 1 292 ? 26.808  -9.426  -12.754 1.00 28.45 ? 292 ILE B CD1 1 
ATOM   4421 N N   . SER B 1 293 ? 26.898  -9.825  -8.789  1.00 28.81 ? 293 SER B N   1 
ATOM   4422 C CA  . SER B 1 293 ? 25.611  -10.211 -8.208  1.00 28.54 ? 293 SER B CA  1 
ATOM   4423 C C   . SER B 1 293 ? 25.097  -9.224  -7.154  1.00 28.50 ? 293 SER B C   1 
ATOM   4424 O O   . SER B 1 293 ? 23.885  -9.073  -6.990  1.00 28.54 ? 293 SER B O   1 
ATOM   4425 C CB  . SER B 1 293 ? 25.686  -11.624 -7.624  1.00 28.41 ? 293 SER B CB  1 
ATOM   4426 O OG  . SER B 1 293 ? 26.757  -11.732 -6.705  1.00 28.05 ? 293 SER B OG  1 
ATOM   4427 N N   . MET B 1 294 ? 26.016  -8.561  -6.451  1.00 28.36 ? 294 MET B N   1 
ATOM   4428 C CA  . MET B 1 294 ? 25.666  -7.530  -5.470  1.00 28.30 ? 294 MET B CA  1 
ATOM   4429 C C   . MET B 1 294 ? 25.002  -6.333  -6.133  1.00 28.17 ? 294 MET B C   1 
ATOM   4430 O O   . MET B 1 294 ? 24.022  -5.798  -5.618  1.00 28.18 ? 294 MET B O   1 
ATOM   4431 C CB  . MET B 1 294 ? 26.908  -7.054  -4.704  1.00 28.32 ? 294 MET B CB  1 
ATOM   4432 N N   . ILE B 1 295 ? 25.547  -5.922  -7.274  1.00 28.04 ? 295 ILE B N   1 
ATOM   4433 C CA  . ILE B 1 295 ? 25.020  -4.790  -8.025  1.00 28.03 ? 295 ILE B CA  1 
ATOM   4434 C C   . ILE B 1 295 ? 23.632  -5.129  -8.564  1.00 27.96 ? 295 ILE B C   1 
ATOM   4435 O O   . ILE B 1 295 ? 22.698  -4.334  -8.430  1.00 27.77 ? 295 ILE B O   1 
ATOM   4436 C CB  . ILE B 1 295 ? 25.984  -4.364  -9.166  1.00 28.08 ? 295 ILE B CB  1 
ATOM   4437 C CG1 . ILE B 1 295 ? 27.379  -4.068  -8.595  1.00 28.41 ? 295 ILE B CG1 1 
ATOM   4438 C CG2 . ILE B 1 295 ? 25.440  -3.145  -9.915  1.00 27.81 ? 295 ILE B CG2 1 
ATOM   4439 C CD1 . ILE B 1 295 ? 28.509  -4.118  -9.614  1.00 29.06 ? 295 ILE B CD1 1 
ATOM   4440 N N   . LEU B 1 296 ? 23.500  -6.319  -9.149  1.00 28.02 ? 296 LEU B N   1 
ATOM   4441 C CA  . LEU B 1 296 ? 22.215  -6.785  -9.665  1.00 28.06 ? 296 LEU B CA  1 
ATOM   4442 C C   . LEU B 1 296 ? 21.189  -6.943  -8.546  1.00 28.27 ? 296 LEU B C   1 
ATOM   4443 O O   . LEU B 1 296 ? 20.098  -6.369  -8.620  1.00 28.45 ? 296 LEU B O   1 
ATOM   4444 C CB  . LEU B 1 296 ? 22.369  -8.089  -10.452 1.00 27.96 ? 296 LEU B CB  1 
ATOM   4445 C CG  . LEU B 1 296 ? 23.196  -8.054  -11.744 1.00 27.70 ? 296 LEU B CG  1 
ATOM   4446 C CD1 . LEU B 1 296 ? 23.139  -9.409  -12.426 1.00 26.64 ? 296 LEU B CD1 1 
ATOM   4447 C CD2 . LEU B 1 296 ? 22.700  -6.970  -12.690 1.00 28.33 ? 296 LEU B CD2 1 
ATOM   4448 N N   . ALA B 1 297 ? 21.550  -7.697  -7.504  1.00 28.40 ? 297 ALA B N   1 
ATOM   4449 C CA  . ALA B 1 297 ? 20.687  -7.860  -6.330  1.00 28.51 ? 297 ALA B CA  1 
ATOM   4450 C C   . ALA B 1 297 ? 20.231  -6.504  -5.825  1.00 28.55 ? 297 ALA B C   1 
ATOM   4451 O O   . ALA B 1 297 ? 19.073  -6.333  -5.447  1.00 28.32 ? 297 ALA B O   1 
ATOM   4452 C CB  . ALA B 1 297 ? 21.412  -8.617  -5.226  1.00 28.54 ? 297 ALA B CB  1 
ATOM   4453 N N   . GLU B 1 298 ? 21.159  -5.547  -5.847  1.00 29.01 ? 298 GLU B N   1 
ATOM   4454 C CA  . GLU B 1 298 ? 20.913  -4.175  -5.413  1.00 29.39 ? 298 GLU B CA  1 
ATOM   4455 C C   . GLU B 1 298 ? 20.017  -3.401  -6.356  1.00 29.21 ? 298 GLU B C   1 
ATOM   4456 O O   . GLU B 1 298 ? 19.245  -2.560  -5.910  1.00 29.30 ? 298 GLU B O   1 
ATOM   4457 C CB  . GLU B 1 298 ? 22.229  -3.417  -5.222  1.00 29.65 ? 298 GLU B CB  1 
ATOM   4458 C CG  . GLU B 1 298 ? 22.740  -3.432  -3.800  1.00 30.93 ? 298 GLU B CG  1 
ATOM   4459 C CD  . GLU B 1 298 ? 21.813  -2.693  -2.867  1.00 32.92 ? 298 GLU B CD  1 
ATOM   4460 O OE1 . GLU B 1 298 ? 21.826  -1.438  -2.883  1.00 34.06 ? 298 GLU B OE1 1 
ATOM   4461 O OE2 . GLU B 1 298 ? 21.068  -3.370  -2.125  1.00 33.29 ? 298 GLU B OE2 1 
ATOM   4462 N N   . ALA B 1 299 ? 20.125  -3.672  -7.654  1.00 29.19 ? 299 ALA B N   1 
ATOM   4463 C CA  . ALA B 1 299 ? 19.249  -3.017  -8.622  1.00 29.17 ? 299 ALA B CA  1 
ATOM   4464 C C   . ALA B 1 299 ? 17.825  -3.512  -8.426  1.00 29.23 ? 299 ALA B C   1 
ATOM   4465 O O   . ALA B 1 299 ? 16.890  -2.718  -8.361  1.00 29.18 ? 299 ALA B O   1 
ATOM   4466 C CB  . ALA B 1 299 ? 19.719  -3.272  -10.041 1.00 29.15 ? 299 ALA B CB  1 
ATOM   4467 N N   . ILE B 1 300 ? 17.679  -4.830  -8.306  1.00 29.46 ? 300 ILE B N   1 
ATOM   4468 C CA  . ILE B 1 300 ? 16.380  -5.454  -8.066  1.00 29.74 ? 300 ILE B CA  1 
ATOM   4469 C C   . ILE B 1 300 ? 15.741  -4.923  -6.774  1.00 30.27 ? 300 ILE B C   1 
ATOM   4470 O O   . ILE B 1 300 ? 14.652  -4.335  -6.819  1.00 30.06 ? 300 ILE B O   1 
ATOM   4471 C CB  . ILE B 1 300 ? 16.484  -7.005  -8.079  1.00 29.48 ? 300 ILE B CB  1 
ATOM   4472 C CG1 . ILE B 1 300 ? 16.789  -7.495  -9.504  1.00 28.74 ? 300 ILE B CG1 1 
ATOM   4473 C CG2 . ILE B 1 300 ? 15.197  -7.645  -7.551  1.00 29.40 ? 300 ILE B CG2 1 
ATOM   4474 C CD1 . ILE B 1 300 ? 17.213  -8.945  -9.603  1.00 27.09 ? 300 ILE B CD1 1 
ATOM   4475 N N   . ARG B 1 301 ? 16.436  -5.092  -5.645  1.00 31.05 ? 301 ARG B N   1 
ATOM   4476 C CA  . ARG B 1 301 ? 15.939  -4.628  -4.343  1.00 31.94 ? 301 ARG B CA  1 
ATOM   4477 C C   . ARG B 1 301 ? 15.450  -3.185  -4.401  1.00 32.36 ? 301 ARG B C   1 
ATOM   4478 O O   . ARG B 1 301 ? 14.430  -2.844  -3.787  1.00 32.21 ? 301 ARG B O   1 
ATOM   4479 C CB  . ARG B 1 301 ? 17.013  -4.772  -3.255  1.00 32.05 ? 301 ARG B CB  1 
ATOM   4480 C CG  . ARG B 1 301 ? 16.499  -4.507  -1.829  1.00 33.13 ? 301 ARG B CG  1 
ATOM   4481 C CD  . ARG B 1 301 ? 17.600  -4.627  -0.760  1.00 34.71 ? 301 ARG B CD  1 
ATOM   4482 N NE  . ARG B 1 301 ? 18.657  -3.609  -0.894  1.00 36.13 ? 301 ARG B NE  1 
ATOM   4483 C CZ  . ARG B 1 301 ? 18.540  -2.329  -0.514  1.00 37.30 ? 301 ARG B CZ  1 
ATOM   4484 N NH1 . ARG B 1 301 ? 17.401  -1.869  0.027   1.00 37.43 ? 301 ARG B NH1 1 
ATOM   4485 N NH2 . ARG B 1 301 ? 19.568  -1.495  -0.682  1.00 37.49 ? 301 ARG B NH2 1 
ATOM   4486 N N   . ARG B 1 302 ? 16.175  -2.352  -5.154  1.00 32.98 ? 302 ARG B N   1 
ATOM   4487 C CA  . ARG B 1 302 ? 15.885  -0.917  -5.226  1.00 33.53 ? 302 ARG B CA  1 
ATOM   4488 C C   . ARG B 1 302 ? 14.791  -0.563  -6.231  1.00 33.70 ? 302 ARG B C   1 
ATOM   4489 O O   . ARG B 1 302 ? 14.027  0.386   -6.008  1.00 33.58 ? 302 ARG B O   1 
ATOM   4490 C CB  . ARG B 1 302 ? 17.162  -0.110  -5.479  1.00 33.64 ? 302 ARG B CB  1 
ATOM   4491 C CG  . ARG B 1 302 ? 18.215  -0.304  -4.392  1.00 34.52 ? 302 ARG B CG  1 
ATOM   4492 C CD  . ARG B 1 302 ? 19.013  0.990   -4.162  1.00 36.03 ? 302 ARG B CD  1 
ATOM   4493 N NE  . ARG B 1 302 ? 20.210  0.717   -3.355  1.00 36.60 ? 302 ARG B NE  1 
ATOM   4494 C CZ  . ARG B 1 302 ? 21.055  1.652   -2.924  1.00 36.41 ? 302 ARG B CZ  1 
ATOM   4495 N NH1 . ARG B 1 302 ? 20.845  2.938   -3.213  1.00 35.78 ? 302 ARG B NH1 1 
ATOM   4496 N NH2 . ARG B 1 302 ? 22.115  1.292   -2.199  1.00 36.55 ? 302 ARG B NH2 1 
ATOM   4497 N N   . THR B 1 303 ? 14.710  -1.323  -7.325  1.00 34.16 ? 303 THR B N   1 
ATOM   4498 C CA  . THR B 1 303 ? 13.605  -1.154  -8.269  1.00 34.68 ? 303 THR B CA  1 
ATOM   4499 C C   . THR B 1 303 ? 12.282  -1.425  -7.551  1.00 34.96 ? 303 THR B C   1 
ATOM   4500 O O   . THR B 1 303 ? 11.330  -0.658  -7.680  1.00 34.91 ? 303 THR B O   1 
ATOM   4501 C CB  . THR B 1 303 ? 13.707  -2.100  -9.493  1.00 34.67 ? 303 THR B CB  1 
ATOM   4502 O OG1 . THR B 1 303 ? 15.063  -2.180  -9.949  1.00 34.75 ? 303 THR B OG1 1 
ATOM   4503 C CG2 . THR B 1 303 ? 12.830  -1.592  -10.628 1.00 34.79 ? 303 THR B CG2 1 
ATOM   4504 N N   . HIS B 1 304 ? 12.245  -2.510  -6.781  1.00 35.54 ? 304 HIS B N   1 
ATOM   4505 C CA  . HIS B 1 304 ? 11.031  -2.929  -6.088  1.00 36.12 ? 304 HIS B CA  1 
ATOM   4506 C C   . HIS B 1 304 ? 10.643  -2.001  -4.932  1.00 36.55 ? 304 HIS B C   1 
ATOM   4507 O O   . HIS B 1 304 ? 9.455   -1.814  -4.662  1.00 36.62 ? 304 HIS B O   1 
ATOM   4508 C CB  . HIS B 1 304 ? 11.157  -4.380  -5.605  1.00 36.00 ? 304 HIS B CB  1 
ATOM   4509 C CG  . HIS B 1 304 ? 10.032  -4.821  -4.724  1.00 36.16 ? 304 HIS B CG  1 
ATOM   4510 N ND1 . HIS B 1 304 ? 10.239  -5.394  -3.487  1.00 36.30 ? 304 HIS B ND1 1 
ATOM   4511 C CD2 . HIS B 1 304 ? 8.688   -4.749  -4.886  1.00 36.23 ? 304 HIS B CD2 1 
ATOM   4512 C CE1 . HIS B 1 304 ? 9.073   -5.667  -2.930  1.00 36.14 ? 304 HIS B CE1 1 
ATOM   4513 N NE2 . HIS B 1 304 ? 8.116   -5.281  -3.757  1.00 36.32 ? 304 HIS B NE2 1 
ATOM   4514 N N   . ASN B 1 305 ? 11.639  -1.416  -4.267  1.00 37.15 ? 305 ASN B N   1 
ATOM   4515 C CA  . ASN B 1 305 ? 11.390  -0.508  -3.145  1.00 37.85 ? 305 ASN B CA  1 
ATOM   4516 C C   . ASN B 1 305 ? 11.157  0.944   -3.554  1.00 38.34 ? 305 ASN B C   1 
ATOM   4517 O O   . ASN B 1 305 ? 10.539  1.710   -2.815  1.00 38.35 ? 305 ASN B O   1 
ATOM   4518 C CB  . ASN B 1 305 ? 12.526  -0.592  -2.124  1.00 37.89 ? 305 ASN B CB  1 
ATOM   4519 C CG  . ASN B 1 305 ? 12.406  -1.801  -1.218  1.00 38.17 ? 305 ASN B CG  1 
ATOM   4520 O OD1 . ASN B 1 305 ? 11.475  -2.603  -1.340  1.00 38.79 ? 305 ASN B OD1 1 
ATOM   4521 N ND2 . ASN B 1 305 ? 13.350  -1.938  -0.295  1.00 38.45 ? 305 ASN B ND2 1 
ATOM   4522 N N   . GLY B 1 306 ? 11.652  1.317   -4.730  1.00 39.02 ? 306 GLY B N   1 
ATOM   4523 C CA  . GLY B 1 306 ? 11.484  2.675   -5.236  1.00 39.82 ? 306 GLY B CA  1 
ATOM   4524 C C   . GLY B 1 306 ? 12.593  3.599   -4.777  1.00 40.39 ? 306 GLY B C   1 
ATOM   4525 O O   . GLY B 1 306 ? 12.399  4.809   -4.663  1.00 40.42 ? 306 GLY B O   1 
ATOM   4526 N N   . GLU B 1 307 ? 13.757  3.019   -4.506  1.00 40.99 ? 307 GLU B N   1 
ATOM   4527 C CA  . GLU B 1 307 ? 14.940  3.789   -4.152  1.00 41.68 ? 307 GLU B CA  1 
ATOM   4528 C C   . GLU B 1 307 ? 15.762  4.098   -5.392  1.00 42.04 ? 307 GLU B C   1 
ATOM   4529 O O   . GLU B 1 307 ? 15.500  3.565   -6.475  1.00 42.09 ? 307 GLU B O   1 
ATOM   4530 C CB  . GLU B 1 307 ? 15.805  3.015   -3.157  1.00 41.75 ? 307 GLU B CB  1 
ATOM   4531 C CG  . GLU B 1 307 ? 15.284  3.034   -1.731  1.00 42.31 ? 307 GLU B CG  1 
ATOM   4532 C CD  . GLU B 1 307 ? 15.763  1.829   -0.951  1.00 43.44 ? 307 GLU B CD  1 
ATOM   4533 O OE1 . GLU B 1 307 ? 16.996  1.596   -0.900  1.00 43.51 ? 307 GLU B OE1 1 
ATOM   4534 O OE2 . GLU B 1 307 ? 14.900  1.117   -0.380  1.00 44.12 ? 307 GLU B OE2 1 
ATOM   4535 N N   . SER B 1 308 ? 16.759  4.961   -5.221  1.00 42.45 ? 308 SER B N   1 
ATOM   4536 C CA  . SER B 1 308 ? 17.694  5.285   -6.283  1.00 42.85 ? 308 SER B CA  1 
ATOM   4537 C C   . SER B 1 308 ? 18.595  4.094   -6.588  1.00 43.16 ? 308 SER B C   1 
ATOM   4538 O O   . SER B 1 308 ? 19.279  3.590   -5.699  1.00 43.29 ? 308 SER B O   1 
ATOM   4539 C CB  . SER B 1 308 ? 18.551  6.485   -5.873  1.00 42.78 ? 308 SER B CB  1 
ATOM   4540 O OG  . SER B 1 308 ? 19.651  6.638   -6.766  1.00 43.06 ? 308 SER B OG  1 
ATOM   4541 N N   . VAL B 1 309 ? 18.588  3.640   -7.839  1.00 43.58 ? 309 VAL B N   1 
ATOM   4542 C CA  . VAL B 1 309 ? 19.558  2.638   -8.284  1.00 44.05 ? 309 VAL B CA  1 
ATOM   4543 C C   . VAL B 1 309 ? 20.798  3.313   -8.881  1.00 44.43 ? 309 VAL B C   1 
ATOM   4544 O O   . VAL B 1 309 ? 21.759  2.632   -9.262  1.00 44.42 ? 309 VAL B O   1 
ATOM   4545 C CB  . VAL B 1 309 ? 18.956  1.584   -9.280  1.00 43.98 ? 309 VAL B CB  1 
ATOM   4546 C CG1 . VAL B 1 309 ? 17.533  1.198   -8.873  1.00 44.22 ? 309 VAL B CG1 1 
ATOM   4547 C CG2 . VAL B 1 309 ? 18.975  2.092   -10.721 1.00 43.74 ? 309 VAL B CG2 1 
ATOM   4548 N N   . SER B 1 310 ? 20.771  4.653   -8.954  1.00 44.93 ? 310 SER B N   1 
ATOM   4549 C CA  . SER B 1 310 ? 21.887  5.413   -9.527  1.00 45.48 ? 310 SER B CA  1 
ATOM   4550 C C   . SER B 1 310 ? 23.150  5.362   -8.670  1.00 45.70 ? 310 SER B C   1 
ATOM   4551 O O   . SER B 1 310 ? 24.258  5.452   -9.202  1.00 45.76 ? 310 SER B O   1 
ATOM   4552 C CB  . SER B 1 310 ? 21.486  6.868   -9.863  1.00 45.50 ? 310 SER B CB  1 
ATOM   4553 O OG  . SER B 1 310 ? 20.629  7.457   -8.826  1.00 45.79 ? 310 SER B OG  1 
ATOM   4554 N N   . TYR B 1 311 ? 22.983  5.200   -7.356  1.00 46.08 ? 311 TYR B N   1 
ATOM   4555 C CA  . TYR B 1 311 ? 24.122  5.028   -6.448  1.00 46.47 ? 311 TYR B CA  1 
ATOM   4556 C C   . TYR B 1 311 ? 25.088  3.958   -6.980  1.00 46.77 ? 311 TYR B C   1 
ATOM   4557 O O   . TYR B 1 311 ? 26.307  4.073   -6.833  1.00 46.77 ? 311 TYR B O   1 
ATOM   4558 C CB  . TYR B 1 311 ? 23.643  4.655   -5.037  1.00 46.42 ? 311 TYR B CB  1 
ATOM   4559 N N   . LEU B 1 312 ? 24.521  2.941   -7.632  1.00 47.21 ? 312 LEU B N   1 
ATOM   4560 C CA  . LEU B 1 312 ? 25.268  1.819   -8.207  1.00 47.60 ? 312 LEU B CA  1 
ATOM   4561 C C   . LEU B 1 312 ? 26.072  2.188   -9.452  1.00 47.95 ? 312 LEU B C   1 
ATOM   4562 O O   . LEU B 1 312 ? 26.869  1.380   -9.944  1.00 48.04 ? 312 LEU B O   1 
ATOM   4563 C CB  . LEU B 1 312 ? 24.307  0.676   -8.548  1.00 47.53 ? 312 LEU B CB  1 
ATOM   4564 C CG  . LEU B 1 312 ? 24.003  -0.432  -7.510  1.00 47.43 ? 312 LEU B CG  1 
ATOM   4565 C CD1 . LEU B 1 312 ? 24.515  -0.145  -6.030  1.00 46.95 ? 312 LEU B CD1 1 
ATOM   4566 C CD2 . LEU B 1 312 ? 22.464  -0.689  -7.569  1.00 47.37 ? 312 LEU B CD2 1 
ATOM   4567 N N   . PHE B 1 313 ? 25.857  3.393   -9.971  1.00 48.33 ? 313 PHE B N   1 
ATOM   4568 C CA  . PHE B 1 313 ? 26.617  3.854   -11.131 1.00 48.78 ? 313 PHE B CA  1 
ATOM   4569 C C   . PHE B 1 313 ? 28.022  4.306   -10.725 1.00 49.07 ? 313 PHE B C   1 
ATOM   4570 O O   . PHE B 1 313 ? 28.956  4.249   -11.539 1.00 49.14 ? 313 PHE B O   1 
ATOM   4571 C CB  . PHE B 1 313 ? 25.879  4.977   -11.881 1.00 48.80 ? 313 PHE B CB  1 
ATOM   4572 C CG  . PHE B 1 313 ? 24.634  4.520   -12.607 1.00 48.88 ? 313 PHE B CG  1 
ATOM   4573 C CD1 . PHE B 1 313 ? 24.352  3.162   -12.779 1.00 48.90 ? 313 PHE B CD1 1 
ATOM   4574 C CD2 . PHE B 1 313 ? 23.757  5.456   -13.149 1.00 48.97 ? 313 PHE B CD2 1 
ATOM   4575 C CE1 . PHE B 1 313 ? 23.205  2.747   -13.452 1.00 48.82 ? 313 PHE B CE1 1 
ATOM   4576 C CE2 . PHE B 1 313 ? 22.609  5.050   -13.833 1.00 49.08 ? 313 PHE B CE2 1 
ATOM   4577 C CZ  . PHE B 1 313 ? 22.334  3.691   -13.983 1.00 48.93 ? 313 PHE B CZ  1 
ATOM   4578 N N   . SER B 1 314 ? 28.168  4.741   -9.471  1.00 49.40 ? 314 SER B N   1 
ATOM   4579 C CA  . SER B 1 314 ? 29.448  5.255   -8.974  1.00 49.67 ? 314 SER B CA  1 
ATOM   4580 C C   . SER B 1 314 ? 29.846  4.702   -7.598  1.00 49.87 ? 314 SER B C   1 
ATOM   4581 O O   . SER B 1 314 ? 30.707  5.272   -6.914  1.00 49.94 ? 314 SER B O   1 
ATOM   4582 C CB  . SER B 1 314 ? 29.430  6.783   -8.960  1.00 49.74 ? 314 SER B CB  1 
ATOM   4583 N N   . HIS B 1 315 ? 29.221  3.593   -7.200  1.00 50.07 ? 315 HIS B N   1 
ATOM   4584 C CA  . HIS B 1 315 ? 29.549  2.915   -5.942  1.00 50.25 ? 315 HIS B CA  1 
ATOM   4585 C C   . HIS B 1 315 ? 29.317  1.406   -6.030  1.00 50.37 ? 315 HIS B C   1 
ATOM   4586 O O   . HIS B 1 315 ? 28.386  0.949   -6.698  1.00 50.36 ? 315 HIS B O   1 
ATOM   4587 C CB  . HIS B 1 315 ? 28.760  3.516   -4.778  1.00 50.23 ? 315 HIS B CB  1 
ATOM   4588 N N   . VAL B 1 316 ? 30.173  0.643   -5.353  1.00 50.55 ? 316 VAL B N   1 
ATOM   4589 C CA  . VAL B 1 316 ? 30.089  -0.816  -5.357  1.00 50.77 ? 316 VAL B CA  1 
ATOM   4590 C C   . VAL B 1 316 ? 29.240  -1.343  -4.186  1.00 50.90 ? 316 VAL B C   1 
ATOM   4591 O O   . VAL B 1 316 ? 29.747  -1.843  -3.172  1.00 50.99 ? 316 VAL B O   1 
ATOM   4592 C CB  . VAL B 1 316 ? 31.492  -1.436  -5.348  1.00 50.72 ? 316 VAL B CB  1 
HETATM 4593 S S   . SO4 C 2 .   ? 4.999   -37.797 -30.248 0.50 22.38 ? 327 SO4 A S   1 
HETATM 4594 O O1  . SO4 C 2 .   ? 5.058   -38.563 -31.489 0.50 22.90 ? 327 SO4 A O1  1 
HETATM 4595 O O2  . SO4 C 2 .   ? 5.143   -38.705 -29.109 0.50 22.53 ? 327 SO4 A O2  1 
HETATM 4596 O O3  . SO4 C 2 .   ? 3.716   -37.092 -30.190 0.50 21.98 ? 327 SO4 A O3  1 
HETATM 4597 O O4  . SO4 C 2 .   ? 6.090   -36.827 -30.223 0.50 22.66 ? 327 SO4 A O4  1 
HETATM 4598 S S   . SO4 D 2 .   ? 18.559  -0.318  -51.442 0.70 14.76 ? 328 SO4 A S   1 
HETATM 4599 O O1  . SO4 D 2 .   ? 18.891  -1.132  -52.612 0.70 15.42 ? 328 SO4 A O1  1 
HETATM 4600 O O2  . SO4 D 2 .   ? 18.600  -1.161  -50.249 0.70 14.81 ? 328 SO4 A O2  1 
HETATM 4601 O O3  . SO4 D 2 .   ? 17.217  0.247   -51.610 0.70 14.81 ? 328 SO4 A O3  1 
HETATM 4602 O O4  . SO4 D 2 .   ? 19.527  0.772   -51.321 0.70 14.59 ? 328 SO4 A O4  1 
HETATM 4603 S S   . SO4 E 2 .   ? -9.533  -22.498 -41.096 0.50 23.70 ? 329 SO4 A S   1 
HETATM 4604 O O1  . SO4 E 2 .   ? -9.868  -22.167 -42.484 0.50 23.41 ? 329 SO4 A O1  1 
HETATM 4605 O O2  . SO4 E 2 .   ? -9.091  -23.886 -40.960 0.50 23.31 ? 329 SO4 A O2  1 
HETATM 4606 O O3  . SO4 E 2 .   ? -10.700 -22.311 -40.244 0.50 23.83 ? 329 SO4 A O3  1 
HETATM 4607 O O4  . SO4 E 2 .   ? -8.460  -21.631 -40.619 0.50 23.93 ? 329 SO4 A O4  1 
HETATM 4608 S S   . SO4 F 2 .   ? 36.553  -10.672 -30.625 0.50 16.95 ? 327 SO4 B S   1 
HETATM 4609 O O1  . SO4 F 2 .   ? 36.659  -11.549 -31.787 0.50 17.29 ? 327 SO4 B O1  1 
HETATM 4610 O O2  . SO4 F 2 .   ? 36.666  -11.456 -29.404 0.50 17.17 ? 327 SO4 B O2  1 
HETATM 4611 O O3  . SO4 F 2 .   ? 35.262  -9.989  -30.646 0.50 17.00 ? 327 SO4 B O3  1 
HETATM 4612 O O4  . SO4 F 2 .   ? 37.631  -9.696  -30.661 0.50 16.67 ? 327 SO4 B O4  1 
HETATM 4613 S S   . SO4 G 2 .   ? -2.902  -18.430 -9.924  0.75 15.77 ? 328 SO4 B S   1 
HETATM 4614 O O1  . SO4 G 2 .   ? -2.668  -19.129 -11.191 0.75 17.04 ? 328 SO4 B O1  1 
HETATM 4615 O O2  . SO4 G 2 .   ? -2.664  -19.366 -8.828  0.75 16.78 ? 328 SO4 B O2  1 
HETATM 4616 O O3  . SO4 G 2 .   ? -4.267  -17.919 -9.858  0.75 16.89 ? 328 SO4 B O3  1 
HETATM 4617 O O4  . SO4 G 2 .   ? -1.980  -17.299 -9.846  0.75 17.26 ? 328 SO4 B O4  1 
HETATM 4618 S S   . SO4 H 2 .   ? 24.071  5.383   -20.451 0.50 18.11 ? 329 SO4 B S   1 
HETATM 4619 O O1  . SO4 H 2 .   ? 23.062  5.648   -21.466 0.50 18.31 ? 329 SO4 B O1  1 
HETATM 4620 O O2  . SO4 H 2 .   ? 24.652  4.062   -20.665 0.50 18.32 ? 329 SO4 B O2  1 
HETATM 4621 O O3  . SO4 H 2 .   ? 23.459  5.445   -19.124 0.50 18.46 ? 329 SO4 B O3  1 
HETATM 4622 O O4  . SO4 H 2 .   ? 25.123  6.388   -20.558 0.50 18.82 ? 329 SO4 B O4  1 
HETATM 4623 O O   . HOH I 3 .   ? -5.660  -13.140 -38.888 1.00 27.25 ? 330 HOH A O   1 
HETATM 4624 O O   . HOH I 3 .   ? 4.760   -4.271  -56.108 1.00 28.68 ? 331 HOH A O   1 
HETATM 4625 O O   . HOH I 3 .   ? -9.060  -47.067 -55.813 1.00 30.36 ? 332 HOH A O   1 
HETATM 4626 O O   . HOH I 3 .   ? 10.887  -5.140  -34.653 1.00 25.84 ? 333 HOH A O   1 
HETATM 4627 O O   . HOH I 3 .   ? 4.354   -27.252 -31.176 1.00 37.46 ? 334 HOH A O   1 
HETATM 4628 O O   . HOH I 3 .   ? -9.634  -29.578 -47.771 1.00 36.37 ? 335 HOH A O   1 
HETATM 4629 O O   . HOH I 3 .   ? 3.194   -6.717  -38.544 1.00 28.15 ? 336 HOH A O   1 
HETATM 4630 O O   . HOH I 3 .   ? -4.188  -51.997 -47.658 1.00 33.79 ? 337 HOH A O   1 
HETATM 4631 O O   . HOH I 3 .   ? 5.111   -10.176 -49.338 1.00 32.66 ? 338 HOH A O   1 
HETATM 4632 O O   . HOH I 3 .   ? 12.398  -2.841  -36.420 1.00 31.68 ? 339 HOH A O   1 
HETATM 4633 O O   . HOH I 3 .   ? 12.966  -14.499 -56.104 1.00 29.25 ? 340 HOH A O   1 
HETATM 4634 O O   . HOH I 3 .   ? 26.205  -9.447  -29.714 1.00 32.37 ? 341 HOH A O   1 
HETATM 4635 O O   . HOH I 3 .   ? -3.691  -40.030 -60.851 1.00 31.91 ? 342 HOH A O   1 
HETATM 4636 O O   . HOH I 3 .   ? 16.235  -3.068  -50.336 1.00 33.69 ? 343 HOH A O   1 
HETATM 4637 O O   . HOH I 3 .   ? -10.099 -43.944 -16.149 1.00 31.78 ? 344 HOH A O   1 
HETATM 4638 O O   . HOH I 3 .   ? 10.421  -15.629 -64.399 1.00 33.13 ? 345 HOH A O   1 
HETATM 4639 O O   . HOH I 3 .   ? 1.043   -26.420 -37.110 1.00 35.64 ? 346 HOH A O   1 
HETATM 4640 O O   . HOH I 3 .   ? 0.319   -53.109 -40.849 1.00 41.66 ? 347 HOH A O   1 
HETATM 4641 O O   . HOH I 3 .   ? -0.234  -29.233 -37.737 1.00 42.10 ? 348 HOH A O   1 
HETATM 4642 O O   . HOH I 3 .   ? -8.761  -26.807 -35.900 1.00 37.85 ? 349 HOH A O   1 
HETATM 4643 O O   . HOH I 3 .   ? 1.416   -37.703 -33.940 1.00 32.68 ? 350 HOH A O   1 
HETATM 4644 O O   . HOH I 3 .   ? 6.748   -32.794 -42.571 1.00 38.51 ? 351 HOH A O   1 
HETATM 4645 O O   . HOH I 3 .   ? 17.008  -32.310 -46.131 1.00 39.25 ? 352 HOH A O   1 
HETATM 4646 O O   . HOH I 3 .   ? 18.360  -20.357 -46.093 1.00 35.85 ? 353 HOH A O   1 
HETATM 4647 O O   . HOH I 3 .   ? -17.139 -44.498 -37.406 1.00 35.86 ? 354 HOH A O   1 
HETATM 4648 O O   . HOH I 3 .   ? -13.423 -35.947 -52.167 1.00 36.29 ? 355 HOH A O   1 
HETATM 4649 O O   . HOH I 3 .   ? -7.115  -28.133 -27.833 1.00 35.31 ? 356 HOH A O   1 
HETATM 4650 O O   . HOH I 3 .   ? -18.861 -46.427 -37.266 1.00 32.86 ? 357 HOH A O   1 
HETATM 4651 O O   . HOH I 3 .   ? 14.209  -40.820 -35.418 1.00 42.74 ? 358 HOH A O   1 
HETATM 4652 O O   . HOH I 3 .   ? 17.555  -20.127 -56.834 1.00 35.57 ? 359 HOH A O   1 
HETATM 4653 O O   . HOH I 3 .   ? 4.728   -31.447 -61.002 1.00 36.67 ? 360 HOH A O   1 
HETATM 4654 O O   . HOH I 3 .   ? 21.002  -24.688 -36.110 1.00 36.39 ? 361 HOH A O   1 
HETATM 4655 O O   . HOH I 3 .   ? 17.357  -16.723 -50.599 1.00 37.29 ? 362 HOH A O   1 
HETATM 4656 O O   . HOH I 3 .   ? -11.442 -51.366 -50.761 1.00 36.66 ? 363 HOH A O   1 
HETATM 4657 O O   . HOH I 3 .   ? 8.889   -1.362  -45.587 1.00 32.80 ? 364 HOH A O   1 
HETATM 4658 O O   . HOH I 3 .   ? 0.057   -11.433 -33.443 1.00 35.26 ? 365 HOH A O   1 
HETATM 4659 O O   . HOH I 3 .   ? -2.551  -42.051 -10.394 1.00 33.87 ? 366 HOH A O   1 
HETATM 4660 O O   . HOH I 3 .   ? 8.839   -40.896 -27.036 1.00 41.11 ? 367 HOH A O   1 
HETATM 4661 O O   . HOH I 3 .   ? -3.385  -46.394 -20.313 1.00 45.27 ? 368 HOH A O   1 
HETATM 4662 O O   . HOH I 3 .   ? 10.965  -47.969 -42.849 1.00 42.34 ? 369 HOH A O   1 
HETATM 4663 O O   . HOH I 3 .   ? 0.836   -24.949 -39.374 1.00 36.68 ? 370 HOH A O   1 
HETATM 4664 O O   . HOH I 3 .   ? 2.938   -12.022 -26.700 1.00 32.21 ? 371 HOH A O   1 
HETATM 4665 O O   . HOH I 3 .   ? 15.590  -46.420 -46.537 1.00 39.12 ? 372 HOH A O   1 
HETATM 4666 O O   . HOH I 3 .   ? -4.791  -19.918 -61.387 1.00 42.56 ? 373 HOH A O   1 
HETATM 4667 O O   . HOH I 3 .   ? 25.745  -22.278 -29.988 1.00 37.01 ? 374 HOH A O   1 
HETATM 4668 O O   . HOH I 3 .   ? 11.595  -43.957 -47.288 1.00 41.62 ? 375 HOH A O   1 
HETATM 4669 O O   . HOH I 3 .   ? 13.415  -50.552 -49.279 1.00 35.68 ? 376 HOH A O   1 
HETATM 4670 O O   . HOH I 3 .   ? 22.091  -20.298 -43.495 1.00 34.63 ? 377 HOH A O   1 
HETATM 4671 O O   . HOH I 3 .   ? -13.142 -20.091 -54.080 1.00 34.88 ? 378 HOH A O   1 
HETATM 4672 O O   . HOH I 3 .   ? -16.341 -43.668 -54.755 1.00 36.81 ? 379 HOH A O   1 
HETATM 4673 O O   . HOH I 3 .   ? 21.433  -18.733 -41.398 1.00 43.39 ? 380 HOH A O   1 
HETATM 4674 O O   . HOH I 3 .   ? -20.341 -48.541 -40.567 1.00 38.07 ? 381 HOH A O   1 
HETATM 4675 O O   . HOH I 3 .   ? 2.889   -39.776 -32.515 1.00 37.51 ? 382 HOH A O   1 
HETATM 4676 O O   . HOH I 3 .   ? 8.103   -41.431 -50.855 1.00 36.63 ? 383 HOH A O   1 
HETATM 4677 O O   . HOH I 3 .   ? 4.574   -28.068 -26.676 1.00 33.13 ? 384 HOH A O   1 
HETATM 4678 O O   . HOH I 3 .   ? -14.541 -49.461 -27.012 1.00 39.47 ? 385 HOH A O   1 
HETATM 4679 O O   . HOH I 3 .   ? 14.805  -49.596 -42.115 1.00 34.88 ? 386 HOH A O   1 
HETATM 4680 O O   . HOH I 3 .   ? 20.962  -39.297 -40.176 1.00 34.98 ? 387 HOH A O   1 
HETATM 4681 O O   . HOH I 3 .   ? 5.186   -26.656 -35.498 1.00 40.19 ? 388 HOH A O   1 
HETATM 4682 O O   . HOH J 3 .   ? 9.245   -6.530  -11.996 1.00 22.90 ? 330 HOH B O   1 
HETATM 4683 O O   . HOH J 3 .   ? 10.922  -2.126  -27.745 1.00 31.38 ? 331 HOH B O   1 
HETATM 4684 O O   . HOH J 3 .   ? 3.318   -5.750  -5.568  1.00 31.02 ? 332 HOH B O   1 
HETATM 4685 O O   . HOH J 3 .   ? 0.359   -18.366 -17.200 1.00 27.27 ? 333 HOH B O   1 
HETATM 4686 O O   . HOH J 3 .   ? 0.164   -16.677 -10.987 1.00 24.97 ? 334 HOH B O   1 
HETATM 4687 O O   . HOH J 3 .   ? 20.832  5.476   -22.658 1.00 26.27 ? 335 HOH B O   1 
HETATM 4688 O O   . HOH J 3 .   ? 54.956  7.699   -16.450 1.00 31.33 ? 336 HOH B O   1 
HETATM 4689 O O   . HOH J 3 .   ? 13.808  3.197   -22.690 1.00 32.73 ? 337 HOH B O   1 
HETATM 4690 O O   . HOH J 3 .   ? 33.280  -23.649 -28.518 1.00 35.76 ? 338 HOH B O   1 
HETATM 4691 O O   . HOH J 3 .   ? 10.316  6.581   -25.428 1.00 30.41 ? 339 HOH B O   1 
HETATM 4692 O O   . HOH J 3 .   ? 39.089  -14.876 -34.872 1.00 42.92 ? 340 HOH B O   1 
HETATM 4693 O O   . HOH J 3 .   ? 5.659   -4.427  -22.700 1.00 38.56 ? 341 HOH B O   1 
HETATM 4694 O O   . HOH J 3 .   ? 4.263   -1.534  -19.698 1.00 27.52 ? 342 HOH B O   1 
HETATM 4695 O O   . HOH J 3 .   ? -4.004  -14.137 -15.291 1.00 31.72 ? 343 HOH B O   1 
HETATM 4696 O O   . HOH J 3 .   ? 29.746  -18.125 -12.910 1.00 38.71 ? 344 HOH B O   1 
HETATM 4697 O O   . HOH J 3 .   ? 15.252  3.870   -20.458 1.00 36.54 ? 345 HOH B O   1 
HETATM 4698 O O   . HOH J 3 .   ? 27.448  -4.148  -41.806 1.00 38.35 ? 346 HOH B O   1 
HETATM 4699 O O   . HOH J 3 .   ? 48.169  -8.024  -10.832 1.00 25.93 ? 347 HOH B O   1 
HETATM 4700 O O   . HOH J 3 .   ? 59.310  1.218   -16.158 1.00 26.91 ? 348 HOH B O   1 
HETATM 4701 O O   . HOH J 3 .   ? 61.087  7.600   -26.859 1.00 42.91 ? 349 HOH B O   1 
HETATM 4702 O O   . HOH J 3 .   ? 30.482  4.362   -13.484 1.00 37.00 ? 350 HOH B O   1 
HETATM 4703 O O   . HOH J 3 .   ? 18.229  4.371   -15.674 1.00 33.27 ? 351 HOH B O   1 
HETATM 4704 O O   . HOH J 3 .   ? 13.207  5.578   -25.040 1.00 38.49 ? 352 HOH B O   1 
HETATM 4705 O O   . HOH J 3 .   ? 8.419   -0.712  -25.094 1.00 35.36 ? 353 HOH B O   1 
HETATM 4706 O O   . HOH J 3 .   ? 13.712  -20.087 -10.905 1.00 31.74 ? 354 HOH B O   1 
HETATM 4707 O O   . HOH J 3 .   ? 47.727  -22.754 -26.226 1.00 37.64 ? 355 HOH B O   1 
HETATM 4708 O O   . HOH J 3 .   ? 31.029  -12.230 -18.505 1.00 40.39 ? 356 HOH B O   1 
HETATM 4709 O O   . HOH J 3 .   ? 46.040  -4.538  -40.395 1.00 41.06 ? 357 HOH B O   1 
HETATM 4710 O O   . HOH J 3 .   ? 26.803  -16.221 -14.740 1.00 36.35 ? 358 HOH B O   1 
HETATM 4711 O O   . HOH J 3 .   ? 57.104  -3.854  -13.675 1.00 41.30 ? 359 HOH B O   1 
HETATM 4712 O O   . HOH J 3 .   ? 52.167  -5.936  -12.162 1.00 39.88 ? 360 HOH B O   1 
HETATM 4713 O O   . HOH J 3 .   ? 41.084  -26.276 -13.157 1.00 34.35 ? 361 HOH B O   1 
HETATM 4714 O O   . HOH J 3 .   ? 22.863  -12.284 -20.424 1.00 37.12 ? 362 HOH B O   1 
HETATM 4715 O O   . HOH J 3 .   ? 25.728  -5.370  -24.519 1.00 37.43 ? 363 HOH B O   1 
HETATM 4716 O O   . HOH J 3 .   ? 20.195  -18.138 -16.081 1.00 37.18 ? 364 HOH B O   1 
HETATM 4717 O O   . HOH J 3 .   ? 42.466  -21.432 -13.334 1.00 40.80 ? 365 HOH B O   1 
HETATM 4718 O O   . HOH J 3 .   ? 28.837  1.548   -31.659 1.00 42.66 ? 366 HOH B O   1 
HETATM 4719 O O   . HOH J 3 .   ? 46.700  -16.020 -28.715 1.00 33.50 ? 367 HOH B O   1 
HETATM 4720 O O   . HOH J 3 .   ? 41.681  -18.511 -14.141 1.00 40.22 ? 368 HOH B O   1 
HETATM 4721 O O   . HOH J 3 .   ? 24.032  -5.658  -21.447 1.00 31.23 ? 369 HOH B O   1 
HETATM 4722 O O   . HOH J 3 .   ? 17.802  -22.629 -23.203 1.00 32.91 ? 370 HOH B O   1 
HETATM 4723 O O   . HOH J 3 .   ? 26.845  1.109   -21.928 1.00 33.40 ? 371 HOH B O   1 
HETATM 4724 O O   . HOH J 3 .   ? 7.032   -21.487 -8.974  1.00 43.53 ? 372 HOH B O   1 
HETATM 4725 O O   . HOH J 3 .   ? 44.323  -24.929 -15.587 1.00 35.19 ? 373 HOH B O   1 
HETATM 4726 O O   . HOH J 3 .   ? 0.376   -8.777  -16.148 1.00 35.31 ? 374 HOH B O   1 
HETATM 4727 O O   . HOH J 3 .   ? 12.960  -15.086 -4.765  1.00 49.01 ? 375 HOH B O   1 
HETATM 4728 O O   . HOH J 3 .   ? 4.129   -12.057 -2.776  1.00 41.84 ? 376 HOH B O   1 
HETATM 4729 O O   . HOH J 3 .   ? 48.082  -5.788  -5.310  1.00 36.93 ? 377 HOH B O   1 
HETATM 4730 O O   . HOH J 3 .   ? 30.856  -1.107  -21.234 1.00 46.02 ? 378 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  CYS 41  41  41  CYS CYS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  MET 68  68  68  MET MET A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  CYS 91  91  91  CYS CYS A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 MET 115 115 115 MET MET A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 HIS 123 123 123 HIS HIS A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 MET 127 127 127 MET MET A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 TRP 162 162 162 TRP TRP A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 CYS 165 165 165 CYS CYS A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 LYS 197 197 197 LYS LYS 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 ?   ?   ?   A . n 
A 1 204 ARG 204 204 ?   ?   ?   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 314 314 314 SER SER A . n 
A 1 315 HIS 315 315 315 HIS HIS A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 PRO 317 317 ?   ?   ?   A . n 
A 1 318 LEU 318 318 ?   ?   ?   A . n 
A 1 319 LEU 319 319 ?   ?   ?   A . n 
A 1 320 GLU 320 320 ?   ?   ?   A . n 
A 1 321 HIS 321 321 ?   ?   ?   A . n 
A 1 322 HIS 322 322 ?   ?   ?   A . n 
A 1 323 HIS 323 323 ?   ?   ?   A . n 
A 1 324 HIS 324 324 ?   ?   ?   A . n 
A 1 325 HIS 325 325 ?   ?   ?   A . n 
A 1 326 HIS 326 326 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   ASN 3   3   3   ASN ASN B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  SER 11  11  11  SER SER B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  GLN 13  13  13  GLN GLN B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  GLN 17  17  17  GLN GLN B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  LYS 33  33  33  LYS LYS B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  PHE 35  35  35  PHE PHE B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  CYS 41  41  41  CYS CYS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  CYS 60  60  60  CYS CYS B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  MET 68  68  68  MET MET B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ILE 72  72  72  ILE ILE B . n 
B 1 73  MET 73  73  73  MET MET B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  CYS 77  77  77  CYS CYS B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  PRO 90  90  90  PRO PRO B . n 
B 1 91  CYS 91  91  91  CYS CYS B . n 
B 1 92  PHE 92  92  92  PHE PHE B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  GLN 97  97  97  GLN GLN B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ASN 114 114 114 ASN ASN B . n 
B 1 115 MET 115 115 115 MET MET B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 HIS 123 123 123 HIS HIS B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 THR 126 126 126 THR THR B . n 
B 1 127 MET 127 127 127 MET MET B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 HIS 130 130 130 HIS HIS B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 SER 132 132 132 SER SER B . n 
B 1 133 GLN 133 133 133 GLN GLN B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 PHE 137 137 137 PHE PHE B . n 
B 1 138 PHE 138 138 138 PHE PHE B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 ILE 140 140 140 ILE ILE B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 TYR 146 146 146 TYR TYR B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 TRP 154 154 154 TRP TRP B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 GLU 157 157 157 GLU GLU B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 ILE 159 159 159 ILE ILE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 TRP 162 162 162 TRP TRP B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 ASN 164 164 164 ASN ASN B . n 
B 1 165 CYS 165 165 165 CYS CYS B . n 
B 1 166 THR 166 166 166 THR THR B . n 
B 1 167 ILE 167 167 167 ILE ILE B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 ASP 171 171 171 ASP ASP B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 LYS 176 176 176 LYS LYS B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 SER 180 180 180 SER SER B . n 
B 1 181 ILE 181 181 181 ILE ILE B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 ASP 183 183 183 ASP ASP B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 PHE 189 189 189 PHE PHE B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 HIS 193 193 193 HIS HIS B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 ARG 196 196 196 ARG ARG B . n 
B 1 197 LYS 197 197 197 LYS LYS 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 ?   ?   ?   B . n 
B 1 204 ARG 204 204 ?   ?   ?   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 ?   ?   ?   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_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly   ?    hexameric 6 
2 software_defined_assembly PISA trimeric  3 
3 software_defined_assembly PISA trimeric  3 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2,3 A,B,C,D,E,F,G,H,I,J 
2 1,2,3 A,C,D,E,I           
3 1,2,3 B,F,G,H,J           
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
2 'ABSA (A^2)' 3580  ? 
2 MORE         -134  ? 
2 'SSA (A^2)'  40380 ? 
3 'ABSA (A^2)' 3630  ? 
3 MORE         -137  ? 
3 'SSA (A^2)'  40230 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -y,x-y,z  -0.5000000000 -0.8660254038 0.0000000000 0.0000000000 0.8660254038  -0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_555 -x+y,-x,z -0.5000000000 0.8660254038  0.0000000000 0.0000000000 -0.8660254038 -0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2008-09-30 
2 'Structure model' 1 1 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MAR345dtb 'data collection' .        ? 1 
AMoRE     phasing           .        ? 2 
REFMAC    refinement        5.2.0019 ? 3 
MOSFLM    'data reduction'  .        ? 4 
SCALA     'data scaling'    .        ? 5 
# 
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  ? ? 78.92   -161.94 
2  1 ASP A 14  ? ? -33.53  -74.43  
3  1 ASP A 224 ? ? -128.21 -87.14  
4  1 CYS A 226 ? ? 80.12   2.38    
5  1 PHE A 253 ? ? 49.23   72.47   
6  1 ASN A 273 ? ? -84.03  39.08   
7  1 SER A 314 ? ? -136.25 -37.66  
8  1 SER B 10  ? ? 59.09   -149.49 
9  1 TYR B 94  ? ? 57.64   15.93   
10 1 ASN B 186 ? ? 70.46   54.56   
11 1 ASP B 224 ? ? -129.59 -95.95  
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 29  ? CG  ? A LYS 29  CG  
2   1 Y 1 A LYS 29  ? CD  ? A LYS 29  CD  
3   1 Y 1 A LYS 29  ? CE  ? A LYS 29  CE  
4   1 Y 1 A LYS 29  ? NZ  ? A LYS 29  NZ  
5   1 Y 1 A SER 36  ? OG  ? A SER 36  OG  
6   1 Y 1 A SER 160 ? OG  ? A SER 160 OG  
7   1 Y 1 A LYS 176 ? CG  ? A LYS 176 CG  
8   1 Y 1 A LYS 176 ? CD  ? A LYS 176 CD  
9   1 Y 1 A LYS 176 ? CE  ? A LYS 176 CE  
10  1 Y 1 A LYS 176 ? NZ  ? A LYS 176 NZ  
11  1 Y 1 A LYS 194 ? CG  ? A LYS 194 CG  
12  1 Y 1 A LYS 194 ? CD  ? A LYS 194 CD  
13  1 Y 1 A LYS 194 ? CE  ? A LYS 194 CE  
14  1 Y 1 A LYS 194 ? NZ  ? A LYS 194 NZ  
15  1 Y 1 A ARG 196 ? CG  ? A ARG 196 CG  
16  1 Y 1 A ARG 196 ? CD  ? A ARG 196 CD  
17  1 Y 1 A ARG 196 ? NE  ? A ARG 196 NE  
18  1 Y 1 A ARG 196 ? CZ  ? A ARG 196 CZ  
19  1 Y 1 A ARG 196 ? NH1 ? A ARG 196 NH1 
20  1 Y 1 A ARG 196 ? NH2 ? A ARG 196 NH2 
21  1 Y 1 A LYS 197 ? CG  ? A LYS 197 CG  
22  1 Y 1 A LYS 197 ? CD  ? A LYS 197 CD  
23  1 Y 1 A LYS 197 ? CE  ? A LYS 197 CE  
24  1 Y 1 A LYS 197 ? NZ  ? A LYS 197 NZ  
25  1 Y 1 A ASP 210 ? CG  ? A ASP 210 CG  
26  1 Y 1 A ASP 210 ? OD1 ? A ASP 210 OD1 
27  1 Y 1 A ASP 210 ? OD2 ? A ASP 210 OD2 
28  1 Y 1 A LYS 235 ? CG  ? A LYS 235 CG  
29  1 Y 1 A LYS 235 ? CD  ? A LYS 235 CD  
30  1 Y 1 A LYS 235 ? CE  ? A LYS 235 CE  
31  1 Y 1 A LYS 235 ? NZ  ? A LYS 235 NZ  
32  1 Y 1 A LYS 282 ? CG  ? A LYS 282 CG  
33  1 Y 1 A LYS 282 ? CD  ? A LYS 282 CD  
34  1 Y 1 A LYS 282 ? CE  ? A LYS 282 CE  
35  1 Y 1 A LYS 282 ? NZ  ? A LYS 282 NZ  
36  1 Y 1 A MET 294 ? CG  ? A MET 294 CG  
37  1 Y 1 A MET 294 ? SD  ? A MET 294 SD  
38  1 Y 1 A MET 294 ? CE  ? A MET 294 CE  
39  1 Y 1 A TYR 311 ? CG  ? A TYR 311 CG  
40  1 Y 1 A TYR 311 ? CD1 ? A TYR 311 CD1 
41  1 Y 1 A TYR 311 ? CD2 ? A TYR 311 CD2 
42  1 Y 1 A TYR 311 ? CE1 ? A TYR 311 CE1 
43  1 Y 1 A TYR 311 ? CE2 ? A TYR 311 CE2 
44  1 Y 1 A TYR 311 ? CZ  ? A TYR 311 CZ  
45  1 Y 1 A TYR 311 ? OH  ? A TYR 311 OH  
46  1 Y 1 A SER 314 ? OG  ? A SER 314 OG  
47  1 Y 1 A HIS 315 ? CG  ? A HIS 315 CG  
48  1 Y 1 A HIS 315 ? ND1 ? A HIS 315 ND1 
49  1 Y 1 A HIS 315 ? CD2 ? A HIS 315 CD2 
50  1 Y 1 A HIS 315 ? CE1 ? A HIS 315 CE1 
51  1 Y 1 A HIS 315 ? NE2 ? A HIS 315 NE2 
52  1 Y 1 A VAL 316 ? CG1 ? A VAL 316 CG1 
53  1 Y 1 A VAL 316 ? CG2 ? A VAL 316 CG2 
54  1 Y 1 B LYS 29  ? CG  ? B LYS 29  CG  
55  1 Y 1 B LYS 29  ? CD  ? B LYS 29  CD  
56  1 Y 1 B LYS 29  ? CE  ? B LYS 29  CE  
57  1 Y 1 B LYS 29  ? NZ  ? B LYS 29  NZ  
58  1 Y 1 B SER 36  ? OG  ? B SER 36  OG  
59  1 Y 1 B SER 160 ? OG  ? B SER 160 OG  
60  1 Y 1 B LYS 176 ? CG  ? B LYS 176 CG  
61  1 Y 1 B LYS 176 ? CD  ? B LYS 176 CD  
62  1 Y 1 B LYS 176 ? CE  ? B LYS 176 CE  
63  1 Y 1 B LYS 176 ? NZ  ? B LYS 176 NZ  
64  1 Y 1 B LYS 194 ? CG  ? B LYS 194 CG  
65  1 Y 1 B LYS 194 ? CD  ? B LYS 194 CD  
66  1 Y 1 B LYS 194 ? CE  ? B LYS 194 CE  
67  1 Y 1 B LYS 194 ? NZ  ? B LYS 194 NZ  
68  1 Y 1 B ARG 196 ? CG  ? B ARG 196 CG  
69  1 Y 1 B ARG 196 ? CD  ? B ARG 196 CD  
70  1 Y 1 B ARG 196 ? NE  ? B ARG 196 NE  
71  1 Y 1 B ARG 196 ? CZ  ? B ARG 196 CZ  
72  1 Y 1 B ARG 196 ? NH1 ? B ARG 196 NH1 
73  1 Y 1 B ARG 196 ? NH2 ? B ARG 196 NH2 
74  1 Y 1 B LYS 197 ? CG  ? B LYS 197 CG  
75  1 Y 1 B LYS 197 ? CD  ? B LYS 197 CD  
76  1 Y 1 B LYS 197 ? CE  ? B LYS 197 CE  
77  1 Y 1 B LYS 197 ? NZ  ? B LYS 197 NZ  
78  1 Y 1 B ASP 210 ? CG  ? B ASP 210 CG  
79  1 Y 1 B ASP 210 ? OD1 ? B ASP 210 OD1 
80  1 Y 1 B ASP 210 ? OD2 ? B ASP 210 OD2 
81  1 Y 1 B LYS 282 ? CG  ? B LYS 282 CG  
82  1 Y 1 B LYS 282 ? CD  ? B LYS 282 CD  
83  1 Y 1 B LYS 282 ? CE  ? B LYS 282 CE  
84  1 Y 1 B LYS 282 ? NZ  ? B LYS 282 NZ  
85  1 Y 1 B LYS 286 ? CG  ? B LYS 286 CG  
86  1 Y 1 B LYS 286 ? CD  ? B LYS 286 CD  
87  1 Y 1 B LYS 286 ? CE  ? B LYS 286 CE  
88  1 Y 1 B LYS 286 ? NZ  ? B LYS 286 NZ  
89  1 Y 1 B MET 294 ? CG  ? B MET 294 CG  
90  1 Y 1 B MET 294 ? SD  ? B MET 294 SD  
91  1 Y 1 B MET 294 ? CE  ? B MET 294 CE  
92  1 Y 1 B TYR 311 ? CG  ? B TYR 311 CG  
93  1 Y 1 B TYR 311 ? CD1 ? B TYR 311 CD1 
94  1 Y 1 B TYR 311 ? CD2 ? B TYR 311 CD2 
95  1 Y 1 B TYR 311 ? CE1 ? B TYR 311 CE1 
96  1 Y 1 B TYR 311 ? CE2 ? B TYR 311 CE2 
97  1 Y 1 B TYR 311 ? CZ  ? B TYR 311 CZ  
98  1 Y 1 B TYR 311 ? OH  ? B TYR 311 OH  
99  1 Y 1 B SER 314 ? OG  ? B SER 314 OG  
100 1 Y 1 B HIS 315 ? CG  ? B HIS 315 CG  
101 1 Y 1 B HIS 315 ? ND1 ? B HIS 315 ND1 
102 1 Y 1 B HIS 315 ? CD2 ? B HIS 315 CD2 
103 1 Y 1 B HIS 315 ? CE1 ? B HIS 315 CE1 
104 1 Y 1 B HIS 315 ? NE2 ? B HIS 315 NE2 
105 1 Y 1 B VAL 316 ? CG1 ? B VAL 316 CG1 
106 1 Y 1 B VAL 316 ? CG2 ? B VAL 316 CG2 
# 
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 198 ? A LYS 198 
4  1 Y 1 A ALA 199 ? A ALA 199 
5  1 Y 1 A ASN 200 ? A ASN 200 
6  1 Y 1 A GLU 201 ? A GLU 201 
7  1 Y 1 A VAL 202 ? A VAL 202 
8  1 Y 1 A ASP 203 ? A ASP 203 
9  1 Y 1 A ARG 204 ? A ARG 204 
10 1 Y 1 A PRO 317 ? A PRO 317 
11 1 Y 1 A LEU 318 ? A LEU 318 
12 1 Y 1 A LEU 319 ? A LEU 319 
13 1 Y 1 A GLU 320 ? A GLU 320 
14 1 Y 1 A HIS 321 ? A HIS 321 
15 1 Y 1 A HIS 322 ? A HIS 322 
16 1 Y 1 A HIS 323 ? A HIS 323 
17 1 Y 1 A HIS 324 ? A HIS 324 
18 1 Y 1 A HIS 325 ? A HIS 325 
19 1 Y 1 A HIS 326 ? A HIS 326 
20 1 Y 1 B MET 1   ? B MET 1   
21 1 Y 1 B PRO 2   ? B PRO 2   
22 1 Y 1 B LYS 198 ? B LYS 198 
23 1 Y 1 B ALA 199 ? B ALA 199 
24 1 Y 1 B ASN 200 ? B ASN 200 
25 1 Y 1 B GLU 201 ? B GLU 201 
26 1 Y 1 B VAL 202 ? B VAL 202 
27 1 Y 1 B ASP 203 ? B ASP 203 
28 1 Y 1 B ARG 204 ? B ARG 204 
29 1 Y 1 B PRO 317 ? B PRO 317 
30 1 Y 1 B LEU 318 ? B LEU 318 
31 1 Y 1 B LEU 319 ? B LEU 319 
32 1 Y 1 B GLU 320 ? B GLU 320 
33 1 Y 1 B HIS 321 ? B HIS 321 
34 1 Y 1 B HIS 322 ? B HIS 322 
35 1 Y 1 B HIS 323 ? B HIS 323 
36 1 Y 1 B HIS 324 ? B HIS 324 
37 1 Y 1 B HIS 325 ? B HIS 325 
38 1 Y 1 B HIS 326 ? B HIS 326 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SO4 1  327 1   SO4 SO4 A . 
D 2 SO4 1  328 4   SO4 SO4 A . 
E 2 SO4 1  329 6   SO4 SO4 A . 
F 2 SO4 1  327 2   SO4 SO4 B . 
G 2 SO4 1  328 3   SO4 SO4 B . 
H 2 SO4 1  329 5   SO4 SO4 B . 
I 3 HOH 1  330 3   HOH HOH A . 
I 3 HOH 2  331 5   HOH HOH A . 
I 3 HOH 3  332 7   HOH HOH A . 
I 3 HOH 4  333 8   HOH HOH A . 
I 3 HOH 5  334 13  HOH HOH A . 
I 3 HOH 6  335 14  HOH HOH A . 
I 3 HOH 7  336 15  HOH HOH A . 
I 3 HOH 8  337 16  HOH HOH A . 
I 3 HOH 9  338 17  HOH HOH A . 
I 3 HOH 10 339 18  HOH HOH A . 
I 3 HOH 11 340 19  HOH HOH A . 
I 3 HOH 12 341 22  HOH HOH A . 
I 3 HOH 13 342 24  HOH HOH A . 
I 3 HOH 14 343 26  HOH HOH A . 
I 3 HOH 15 344 27  HOH HOH A . 
I 3 HOH 16 345 28  HOH HOH A . 
I 3 HOH 17 346 29  HOH HOH A . 
I 3 HOH 18 347 30  HOH HOH A . 
I 3 HOH 19 348 31  HOH HOH A . 
I 3 HOH 20 349 34  HOH HOH A . 
I 3 HOH 21 350 35  HOH HOH A . 
I 3 HOH 22 351 36  HOH HOH A . 
I 3 HOH 23 352 38  HOH HOH A . 
I 3 HOH 24 353 40  HOH HOH A . 
I 3 HOH 25 354 41  HOH HOH A . 
I 3 HOH 26 355 42  HOH HOH A . 
I 3 HOH 27 356 45  HOH HOH A . 
I 3 HOH 28 357 48  HOH HOH A . 
I 3 HOH 29 358 49  HOH HOH A . 
I 3 HOH 30 359 54  HOH HOH A . 
I 3 HOH 31 360 56  HOH HOH A . 
I 3 HOH 32 361 59  HOH HOH A . 
I 3 HOH 33 362 61  HOH HOH A . 
I 3 HOH 34 363 63  HOH HOH A . 
I 3 HOH 35 364 69  HOH HOH A . 
I 3 HOH 36 365 70  HOH HOH A . 
I 3 HOH 37 366 71  HOH HOH A . 
I 3 HOH 38 367 73  HOH HOH A . 
I 3 HOH 39 368 74  HOH HOH A . 
I 3 HOH 40 369 76  HOH HOH A . 
I 3 HOH 41 370 77  HOH HOH A . 
I 3 HOH 42 371 80  HOH HOH A . 
I 3 HOH 43 372 81  HOH HOH A . 
I 3 HOH 44 373 82  HOH HOH A . 
I 3 HOH 45 374 85  HOH HOH A . 
I 3 HOH 46 375 87  HOH HOH A . 
I 3 HOH 47 376 88  HOH HOH A . 
I 3 HOH 48 377 89  HOH HOH A . 
I 3 HOH 49 378 90  HOH HOH A . 
I 3 HOH 50 379 93  HOH HOH A . 
I 3 HOH 51 380 94  HOH HOH A . 
I 3 HOH 52 381 95  HOH HOH A . 
I 3 HOH 53 382 96  HOH HOH A . 
I 3 HOH 54 383 97  HOH HOH A . 
I 3 HOH 55 384 99  HOH HOH A . 
I 3 HOH 56 385 100 HOH HOH A . 
I 3 HOH 57 386 102 HOH HOH A . 
I 3 HOH 58 387 107 HOH HOH A . 
I 3 HOH 59 388 108 HOH HOH A . 
J 3 HOH 1  330 1   HOH HOH B . 
J 3 HOH 2  331 2   HOH HOH B . 
J 3 HOH 3  332 4   HOH HOH B . 
J 3 HOH 4  333 6   HOH HOH B . 
J 3 HOH 5  334 9   HOH HOH B . 
J 3 HOH 6  335 10  HOH HOH B . 
J 3 HOH 7  336 11  HOH HOH B . 
J 3 HOH 8  337 12  HOH HOH B . 
J 3 HOH 9  338 20  HOH HOH B . 
J 3 HOH 10 339 21  HOH HOH B . 
J 3 HOH 11 340 23  HOH HOH B . 
J 3 HOH 12 341 25  HOH HOH B . 
J 3 HOH 13 342 32  HOH HOH B . 
J 3 HOH 14 343 33  HOH HOH B . 
J 3 HOH 15 344 37  HOH HOH B . 
J 3 HOH 16 345 39  HOH HOH B . 
J 3 HOH 17 346 43  HOH HOH B . 
J 3 HOH 18 347 44  HOH HOH B . 
J 3 HOH 19 348 46  HOH HOH B . 
J 3 HOH 20 349 47  HOH HOH B . 
J 3 HOH 21 350 50  HOH HOH B . 
J 3 HOH 22 351 51  HOH HOH B . 
J 3 HOH 23 352 52  HOH HOH B . 
J 3 HOH 24 353 53  HOH HOH B . 
J 3 HOH 25 354 55  HOH HOH B . 
J 3 HOH 26 355 57  HOH HOH B . 
J 3 HOH 27 356 58  HOH HOH B . 
J 3 HOH 28 357 60  HOH HOH B . 
J 3 HOH 29 358 62  HOH HOH B . 
J 3 HOH 30 359 64  HOH HOH B . 
J 3 HOH 31 360 65  HOH HOH B . 
J 3 HOH 32 361 66  HOH HOH B . 
J 3 HOH 33 362 67  HOH HOH B . 
J 3 HOH 34 363 68  HOH HOH B . 
J 3 HOH 35 364 72  HOH HOH B . 
J 3 HOH 36 365 75  HOH HOH B . 
J 3 HOH 37 366 78  HOH HOH B . 
J 3 HOH 38 367 79  HOH HOH B . 
J 3 HOH 39 368 83  HOH HOH B . 
J 3 HOH 40 369 84  HOH HOH B . 
J 3 HOH 41 370 86  HOH HOH B . 
J 3 HOH 42 371 91  HOH HOH B . 
J 3 HOH 43 372 92  HOH HOH B . 
J 3 HOH 44 373 98  HOH HOH B . 
J 3 HOH 45 374 101 HOH HOH B . 
J 3 HOH 46 375 103 HOH HOH B . 
J 3 HOH 47 376 104 HOH HOH B . 
J 3 HOH 48 377 105 HOH HOH B . 
J 3 HOH 49 378 106 HOH HOH B . 
# 
