data_4LZO
# 
_entry.id   4LZO 
# 
_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   4LZO         
RCSB  RCSB081282   
WWPDB D_1000081282 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4LYG . unspecified 
PDB 4LZP . unspecified 
PDB 4M0P . unspecified 
PDB 4M0U . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4LZO 
_pdbx_database_status.recvd_initial_deposition_date   2013-07-31 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Chen, P.' 1 
'Teng, M.' 2 
'Li, X.'   3 
# 
_citation.id                        primary 
_citation.title                     
;Crystal and EM Structures of Human Phosphoribosyl Pyrophosphate Synthase I (PRS1) Provide Novel Insights into the Disease-Associated Mutations
;
_citation.journal_abbrev            'Plos One' 
_citation.journal_volume            10 
_citation.page_first                e0120304 
_citation.page_last                 e0120304 
_citation.year                      2015 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25781187 
_citation.pdbx_database_id_DOI      10.1371/journal.pone.0120304 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Chen, P.'  1  
primary 'Liu, Z.'   2  
primary 'Wang, X.'  3  
primary 'Peng, J.'  4  
primary 'Sun, Q.'   5  
primary 'Li, J.'    6  
primary 'Wang, M.'  7  
primary 'Niu, L.'   8  
primary 'Zhang, Z.' 9  
primary 'Cai, G.'   10 
primary 'Teng, M.'  11 
primary 'Li, X.'    12 
# 
_cell.entry_id           4LZO 
_cell.length_a           170.402 
_cell.length_b           170.402 
_cell.length_c           62.144 
_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                         4LZO 
_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' 35980.402 2 2.7.6.1 A87T ? ? 
2 non-polymer syn 'SULFATE ION'                          96.063    6 ?       ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'PPRibP, Phosphoribosyl pyrophosphate synthase I, PRS-I' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTTVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTTVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
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  THR n 
1 88  VAL n 
1 89  ILE n 
1 90  PRO n 
1 91  CYS n 
1 92  PHE n 
1 93  PRO n 
1 94  TYR n 
1 95  ALA n 
1 96  ARG n 
1 97  GLN n 
1 98  ASP n 
1 99  LYS n 
1 100 LYS n 
1 101 ASP n 
1 102 LYS n 
1 103 SER n 
1 104 ARG n 
1 105 ALA n 
1 106 PRO n 
1 107 ILE n 
1 108 SER n 
1 109 ALA n 
1 110 LYS n 
1 111 LEU n 
1 112 VAL n 
1 113 ALA n 
1 114 ASN n 
1 115 MET n 
1 116 LEU n 
1 117 SER n 
1 118 VAL n 
1 119 ALA n 
1 120 GLY n 
1 121 ALA n 
1 122 ASP n 
1 123 HIS n 
1 124 ILE n 
1 125 ILE n 
1 126 THR n 
1 127 MET n 
1 128 ASP n 
1 129 LEU n 
1 130 HIS n 
1 131 ALA n 
1 132 SER n 
1 133 GLN n 
1 134 ILE n 
1 135 GLN n 
1 136 GLY n 
1 137 PHE n 
1 138 PHE n 
1 139 ASP n 
1 140 ILE n 
1 141 PRO n 
1 142 VAL n 
1 143 ASP n 
1 144 ASN n 
1 145 LEU n 
1 146 TYR n 
1 147 ALA n 
1 148 GLU n 
1 149 PRO n 
1 150 ALA n 
1 151 VAL n 
1 152 LEU n 
1 153 LYS n 
1 154 TRP n 
1 155 ILE n 
1 156 ARG n 
1 157 GLU n 
1 158 ASN n 
1 159 ILE n 
1 160 SER n 
1 161 GLU n 
1 162 TRP n 
1 163 ARG n 
1 164 ASN n 
1 165 CYS n 
1 166 THR n 
1 167 ILE n 
1 168 VAL n 
1 169 SER n 
1 170 PRO n 
1 171 ASP n 
1 172 ALA n 
1 173 GLY n 
1 174 GLY n 
1 175 ALA n 
1 176 LYS n 
1 177 ARG n 
1 178 VAL n 
1 179 THR n 
1 180 SER n 
1 181 ILE n 
1 182 ALA n 
1 183 ASP n 
1 184 ARG n 
1 185 LEU n 
1 186 ASN n 
1 187 VAL n 
1 188 ASP n 
1 189 PHE n 
1 190 ALA n 
1 191 LEU n 
1 192 ILE n 
1 193 HIS n 
1 194 LYS n 
1 195 GLU n 
1 196 ARG n 
1 197 LYS n 
1 198 LYS n 
1 199 ALA n 
1 200 ASN n 
1 201 GLU n 
1 202 VAL n 
1 203 ASP n 
1 204 ARG n 
1 205 MET n 
1 206 VAL n 
1 207 LEU n 
1 208 VAL n 
1 209 GLY n 
1 210 ASP n 
1 211 VAL n 
1 212 LYS n 
1 213 ASP n 
1 214 ARG n 
1 215 VAL n 
1 216 ALA n 
1 217 ILE n 
1 218 LEU n 
1 219 VAL n 
1 220 ASP n 
1 221 ASP n 
1 222 MET n 
1 223 ALA n 
1 224 ASP n 
1 225 THR n 
1 226 CYS n 
1 227 GLY n 
1 228 THR n 
1 229 ILE n 
1 230 CYS n 
1 231 HIS n 
1 232 ALA n 
1 233 ALA n 
1 234 ASP n 
1 235 LYS n 
1 236 LEU n 
1 237 LEU n 
1 238 SER n 
1 239 ALA n 
1 240 GLY n 
1 241 ALA n 
1 242 THR n 
1 243 ARG n 
1 244 VAL n 
1 245 TYR n 
1 246 ALA n 
1 247 ILE n 
1 248 LEU n 
1 249 THR n 
1 250 HIS n 
1 251 GLY n 
1 252 ILE n 
1 253 PHE n 
1 254 SER n 
1 255 GLY n 
1 256 PRO n 
1 257 ALA n 
1 258 ILE n 
1 259 SER n 
1 260 ARG n 
1 261 ILE n 
1 262 ASN n 
1 263 ASN n 
1 264 ALA n 
1 265 CYS n 
1 266 PHE n 
1 267 GLU n 
1 268 ALA n 
1 269 VAL n 
1 270 VAL n 
1 271 VAL n 
1 272 THR n 
1 273 ASN n 
1 274 THR n 
1 275 ILE n 
1 276 PRO n 
1 277 GLN n 
1 278 GLU n 
1 279 ASP n 
1 280 LYS n 
1 281 MET n 
1 282 LYS n 
1 283 HIS n 
1 284 CYS n 
1 285 SER n 
1 286 LYS n 
1 287 ILE n 
1 288 GLN n 
1 289 VAL n 
1 290 ILE n 
1 291 ASP n 
1 292 ILE n 
1 293 SER n 
1 294 MET n 
1 295 ILE n 
1 296 LEU n 
1 297 ALA n 
1 298 GLU n 
1 299 ALA n 
1 300 ILE n 
1 301 ARG n 
1 302 ARG n 
1 303 THR n 
1 304 HIS n 
1 305 ASN n 
1 306 GLY n 
1 307 GLU n 
1 308 SER n 
1 309 VAL n 
1 310 SER n 
1 311 TYR n 
1 312 LEU n 
1 313 PHE n 
1 314 SER n 
1 315 HIS n 
1 316 VAL n 
1 317 PRO n 
1 318 LEU n 
1 319 LEU n 
1 320 GLU n 
1 321 HIS n 
1 322 HIS n 
1 323 HIS n 
1 324 HIS n 
1 325 HIS n 
1 326 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PRPS1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PRPS1_HUMAN 
_struct_ref.pdbx_db_accession          P60891 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 4LZO A 1 ? 318 ? P60891 1 ? 318 ? 1 318 
2 1 4LZO 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 4LZO THR A 87  ? UNP P60891 ALA 87 'ENGINEERED MUTATION' 87  1  
1 4LZO LEU A 319 ? UNP P60891 ?   ?  'EXPRESSION TAG'      319 2  
1 4LZO GLU A 320 ? UNP P60891 ?   ?  'EXPRESSION TAG'      320 3  
1 4LZO HIS A 321 ? UNP P60891 ?   ?  'EXPRESSION TAG'      321 4  
1 4LZO HIS A 322 ? UNP P60891 ?   ?  'EXPRESSION TAG'      322 5  
1 4LZO HIS A 323 ? UNP P60891 ?   ?  'EXPRESSION TAG'      323 6  
1 4LZO HIS A 324 ? UNP P60891 ?   ?  'EXPRESSION TAG'      324 7  
1 4LZO HIS A 325 ? UNP P60891 ?   ?  'EXPRESSION TAG'      325 8  
1 4LZO HIS A 326 ? UNP P60891 ?   ?  'EXPRESSION TAG'      326 9  
2 4LZO THR B 87  ? UNP P60891 ALA 87 'ENGINEERED MUTATION' 87  10 
2 4LZO LEU B 319 ? UNP P60891 ?   ?  'EXPRESSION TAG'      319 11 
2 4LZO GLU B 320 ? UNP P60891 ?   ?  'EXPRESSION TAG'      320 12 
2 4LZO HIS B 321 ? UNP P60891 ?   ?  'EXPRESSION TAG'      321 13 
2 4LZO HIS B 322 ? UNP P60891 ?   ?  'EXPRESSION TAG'      322 14 
2 4LZO HIS B 323 ? UNP P60891 ?   ?  'EXPRESSION TAG'      323 15 
2 4LZO HIS B 324 ? UNP P60891 ?   ?  'EXPRESSION TAG'      324 16 
2 4LZO HIS B 325 ? UNP P60891 ?   ?  'EXPRESSION TAG'      325 17 
2 4LZO HIS B 326 ? UNP P60891 ?   ?  'EXPRESSION TAG'      326 18 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
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          4LZO 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.41 
_exptl_crystal.density_percent_sol   49.02 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.temp            295 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.1 
_exptl_crystal_grow.pdbx_details    'pH 4.1, VAPOR DIFFUSION, 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               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315r' 
_diffrn_detector.pdbx_collection_date   ? 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   . 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRF BEAMLINE BL17U' 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_synchrotron_beamline   BL17U 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     4LZO 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             34.2 
_reflns.d_resolution_high            3.31 
_reflns.number_obs                   10020 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         ? 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high                  3.31 
_reflns_shell.d_res_low                   ? 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.pdbx_redundancy             ? 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.number_possible             ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
# 
_refine.entry_id                                 4LZO 
_refine.ls_number_reflns_obs                     9535 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             34.18 
_refine.ls_d_res_high                            3.31 
_refine.ls_percent_reflns_obs                    99.77 
_refine.ls_R_factor_obs                          0.26552 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.26325 
_refine.ls_R_factor_R_free                       0.31183 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_number_reflns_R_free                  482 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.795 
_refine.correlation_coeff_Fo_to_Fc_free          0.740 
_refine.B_iso_mean                               36.513 
_refine.aniso_B[1][1]                            1.83 
_refine.aniso_B[2][2]                            1.83 
_refine.aniso_B[3][3]                            -2.75 
_refine.aniso_B[1][2]                            0.92 
_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                      ? 
_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                  0.738 
_refine.overall_SU_ML                            0.603 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             34.074 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_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        4684 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               4714 
_refine_hist.d_res_high                       3.31 
_refine_hist.d_res_low                        34.18 
# 
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_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d             0.008  0.022  ? 4774 ? 'X-RAY DIFFRACTION' 
r_bond_other_d               ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg          1.141  1.960  ? 6459 ? 'X-RAY DIFFRACTION' 
r_angle_other_deg            ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg       5.350  5.000  ? 608  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg       38.148 24.523 ? 199  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg       17.552 15.000 ? 857  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg       14.483 15.000 ? 30   ? 'X-RAY DIFFRACTION' 
r_chiral_restr               0.075  0.200  ? 765  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined         0.004  0.021  ? 3478 ? 'X-RAY DIFFRACTION' 
r_gen_planes_other           ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_nbd_refined                ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_nbd_other                  ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_nbtor_refined              ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_nbtor_other                ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined        ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_other          ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined          ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_metal_ion_other            ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined       ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_other         ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined     ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_other       ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_metal_ion_refined ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_metal_ion_other   ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_mcbond_it                  0.370  1.500  ? 3039 ? 'X-RAY DIFFRACTION' 
r_mcbond_other               ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_mcangle_it                 0.685  2.000  ? 4920 ? 'X-RAY DIFFRACTION' 
r_mcangle_other              ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_scbond_it                  0.664  3.000  ? 1735 ? 'X-RAY DIFFRACTION' 
r_scbond_other               ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_scangle_it                 1.209  4.500  ? 1539 ? 'X-RAY DIFFRACTION' 
r_scangle_other              ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_long_range_B_refined       ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_long_range_B_other         ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr           ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_sphericity_free            ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded          ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       3.309 
_refine_ls_shell.d_res_low                        3.395 
_refine_ls_shell.number_reflns_R_work             687 
_refine_ls_shell.R_factor_R_work                  0.247 
_refine_ls_shell.percent_reflns_obs               97.84 
_refine_ls_shell.R_factor_R_free                  0.298 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             37 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  4LZO 
_struct.title                     'Crystal structure of human PRS1 A87T mutant' 
_struct.pdbx_descriptor           'Ribose-phosphate pyrophosphokinase 1 (E.C.2.7.6.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4LZO 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'PRS1, PRPP synthesis enzyme, ATP R5P, TRANSFERASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  HIS A 12  ? LEU A 23  ? HIS A 12  LEU A 23  1 ? 12 
HELX_P HELX_P2  2  GLU A 62  ? ALA A 80  ? GLU A 62  ALA A 80  1 ? 19 
HELX_P HELX_P3  3  ILE A 107 ? GLY A 120 ? ILE A 107 GLY A 120 1 ? 14 
HELX_P HELX_P4  4  ALA A 147 ? ILE A 159 ? ALA A 147 ILE A 159 1 ? 13 
HELX_P HELX_P5  5  GLU A 161 ? ASN A 164 ? GLU A 161 ASN A 164 5 ? 4  
HELX_P HELX_P6  6  ASP A 171 ? GLY A 173 ? ASP A 171 GLY A 173 5 ? 3  
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 ? ASN A 263 ? PRO A 256 ASN A 263 1 ? 8  
HELX_P HELX_P10 10 GLN A 277 ? HIS A 283 ? GLN A 277 HIS A 283 1 ? 7  
HELX_P HELX_P11 11 ILE A 292 ? GLY A 306 ? ILE A 292 GLY A 306 1 ? 15 
HELX_P HELX_P12 12 VAL A 309 ? PHE A 313 ? VAL A 309 PHE A 313 5 ? 5  
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 SER B 160 ? ARG B 163 ? SER B 160 ARG B 163 5 ? 4  
HELX_P HELX_P19 19 GLY B 174 ? ASN B 186 ? GLY B 174 ASN B 186 1 ? 13 
HELX_P HELX_P20 20 CYS B 226 ? ALA B 239 ? CYS B 226 ALA B 239 1 ? 14 
HELX_P HELX_P21 21 PRO B 256 ? ALA B 264 ? PRO B 256 ALA B 264 1 ? 9  
HELX_P HELX_P22 22 GLN B 277 ? CYS B 284 ? GLN B 277 CYS B 284 1 ? 8  
HELX_P HELX_P23 23 ILE B 292 ? GLY B 306 ? ILE B 292 GLY B 306 1 ? 15 
HELX_P HELX_P24 24 SER B 308 ? PHE B 313 ? SER B 308 PHE B 313 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   ? PHE A 7   ? ILE A 4   PHE A 7   
A 2 ASP A 52  ? VAL A 56  ? ASP A 52  VAL A 56  
A 3 ARG A 84  ? VAL A 88  ? ARG A 84  VAL A 88  
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 LYS A 33  ? LYS A 34  ? LYS A 33  LYS A 34  
B 2 THR A 40  ? CYS A 41  ? THR A 40  CYS A 41  
C 1 MET A 205 ? VAL A 208 ? MET A 205 VAL A 208 
C 2 ASP A 188 ? LYS A 194 ? ASP A 188 LYS A 194 
C 3 THR A 166 ? SER A 169 ? THR A 166 SER A 169 
C 4 ALA A 216 ? ALA A 223 ? ALA A 216 ALA A 223 
C 5 VAL A 244 ? GLY A 251 ? VAL A 244 GLY A 251 
C 6 VAL A 269 ? THR A 272 ? VAL A 269 THR A 272 
C 7 ILE A 287 ? ILE A 290 ? ILE A 287 ILE A 290 
D 1 ILE B 4   ? SER B 8   ? ILE B 4   SER B 8   
D 2 ASP B 52  ? VAL B 56  ? ASP B 52  VAL B 56  
D 3 ARG B 84  ? ILE B 89  ? ARG B 84  ILE B 89  
D 4 HIS B 123 ? MET B 127 ? HIS B 123 MET B 127 
D 5 VAL B 142 ? LEU B 145 ? VAL B 142 LEU B 145 
E 1 LYS B 33  ? LYS B 34  ? LYS B 33  LYS B 34  
E 2 THR B 40  ? CYS B 41  ? THR B 40  CYS B 41  
F 1 MET B 205 ? VAL B 208 ? MET B 205 VAL B 208 
F 2 ASP B 188 ? LYS B 194 ? ASP B 188 LYS B 194 
F 3 CYS B 165 ? SER B 169 ? CYS B 165 SER B 169 
F 4 VAL B 215 ? ALA B 223 ? VAL B 215 ALA B 223 
F 5 VAL B 244 ? GLY B 251 ? VAL B 244 GLY B 251 
F 6 PHE B 266 ? THR B 272 ? PHE B 266 THR B 272 
F 7 ILE B 287 ? ILE B 290 ? ILE B 287 ILE B 290 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N PHE A 7   ? N PHE A 7   O TYR A 54  ? O TYR A 54  
A 2 3 N ILE A 55  ? N ILE A 55  O VAL A 88  ? O VAL A 88  
A 3 4 N THR A 87  ? N THR 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 ALA A 190 ? O ALA A 190 N SER A 169 ? N SER A 169 
C 3 4 N THR A 166 ? N THR A 166 O ILE A 217 ? O ILE A 217 
C 4 5 N LEU A 218 ? N LEU A 218 O ILE A 247 ? O ILE A 247 
C 5 6 N LEU A 248 ? N LEU A 248 O VAL A 270 ? O VAL A 270 
C 6 7 N VAL A 269 ? N VAL A 269 O GLN A 288 ? O GLN A 288 
D 1 2 N PHE B 7   ? N PHE B 7   O TYR B 54  ? O TYR B 54  
D 2 3 N ILE B 55  ? N ILE B 55  O VAL B 88  ? O VAL B 88  
D 3 4 N ILE B 89  ? N ILE B 89  O ILE B 125 ? O ILE B 125 
D 4 5 N THR B 126 ? N THR B 126 O LEU B 145 ? O LEU B 145 
E 1 2 N 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 ILE B 192 ? O ILE B 192 N SER B 169 ? N SER B 169 
F 3 4 N THR B 166 ? N THR B 166 O ILE B 217 ? O ILE B 217 
F 4 5 N LEU B 218 ? N LEU B 218 O TYR B 245 ? O TYR B 245 
F 5 6 N VAL B 244 ? N VAL B 244 O GLU B 267 ? O GLU B 267 
F 6 7 N VAL B 269 ? N VAL B 269 O GLN B 288 ? O GLN B 288 
# 
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 1001' 
AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 1002' 
AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 A 1003' 
AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 B 401'  
AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 B 402'  
AC6 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 B 403'  
# 
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 SER A 47  ? SER A 47  . ? 3_555 ? 
2  AC1 6 ARG A 49  ? ARG A 49  . ? 3_555 ? 
3  AC1 6 SER A 308 ? SER A 308 . ? 1_555 ? 
4  AC1 6 VAL A 309 ? VAL A 309 . ? 1_555 ? 
5  AC1 6 SER A 310 ? SER A 310 . ? 1_555 ? 
6  AC1 6 ARG B 104 ? ARG B 104 . ? 3_555 ? 
7  AC2 5 ALA A 223 ? ALA A 223 . ? 1_555 ? 
8  AC2 5 ASP A 224 ? ASP A 224 . ? 1_555 ? 
9  AC2 5 THR A 225 ? THR A 225 . ? 1_555 ? 
10 AC2 5 CYS A 226 ? CYS A 226 . ? 1_555 ? 
11 AC2 5 THR A 228 ? THR A 228 . ? 1_555 ? 
12 AC3 7 SER A 132 ? SER A 132 . ? 1_555 ? 
13 AC3 7 GLN A 135 ? GLN A 135 . ? 1_555 ? 
14 AC3 7 ASN A 144 ? ASN A 144 . ? 1_555 ? 
15 AC3 7 TYR A 146 ? TYR A 146 . ? 1_555 ? 
16 AC3 7 LYS B 100 ? LYS B 100 . ? 3_555 ? 
17 AC3 7 ASP B 101 ? ASP B 101 . ? 3_555 ? 
18 AC3 7 LYS B 102 ? LYS B 102 . ? 3_555 ? 
19 AC4 6 ARG A 104 ? ARG A 104 . ? 2_555 ? 
20 AC4 6 SER B 47  ? SER B 47  . ? 2_555 ? 
21 AC4 6 ARG B 49  ? ARG B 49  . ? 2_555 ? 
22 AC4 6 SER B 308 ? SER B 308 . ? 1_555 ? 
23 AC4 6 VAL B 309 ? VAL B 309 . ? 1_555 ? 
24 AC4 6 SER B 310 ? SER B 310 . ? 1_555 ? 
25 AC5 6 ALA B 223 ? ALA B 223 . ? 1_555 ? 
26 AC5 6 ASP B 224 ? ASP B 224 . ? 1_555 ? 
27 AC5 6 THR B 225 ? THR B 225 . ? 1_555 ? 
28 AC5 6 CYS B 226 ? CYS B 226 . ? 1_555 ? 
29 AC5 6 GLY B 227 ? GLY B 227 . ? 1_555 ? 
30 AC5 6 THR B 228 ? THR B 228 . ? 1_555 ? 
31 AC6 8 LYS A 99  ? LYS A 99  . ? 2_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 ? 
# 
_database_PDB_matrix.entry_id          4LZO 
_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                    4LZO 
_atom_sites.fract_transf_matrix[1][1]   0.005868 
_atom_sites.fract_transf_matrix[1][2]   0.003388 
_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]   0.006776 
_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]   0.016092 
_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   ? 2.375   12.124 -8.328  1.00  41.44 ? 3    ASN A N   1 
ATOM   2    C CA  . ASN A 1 3   ? 2.301   11.102 -7.239  1.00  41.44 ? 3    ASN A CA  1 
ATOM   3    C C   . ASN A 1 3   ? 3.155   11.475 -6.026  1.00  40.87 ? 3    ASN A C   1 
ATOM   4    O O   . ASN A 1 3   ? 2.804   11.145 -4.892  1.00  40.67 ? 3    ASN A O   1 
ATOM   5    C CB  . ASN A 1 3   ? 2.706   9.715  -7.760  1.00  41.85 ? 3    ASN A CB  1 
ATOM   6    C CG  . ASN A 1 3   ? 2.212   8.579  -6.859  1.00  43.12 ? 3    ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 3   ? 1.004   8.344  -6.740  1.00  44.40 ? 3    ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 3   ? 3.151   7.858  -6.240  1.00  44.60 ? 3    ASN A ND2 1 
ATOM   9    N N   . ILE A 1 4   ? 4.272   12.157 -6.286  1.00  40.32 ? 4    ILE A N   1 
ATOM   10   C CA  . ILE A 1 4   ? 5.168   12.691 -5.251  1.00  39.54 ? 4    ILE A CA  1 
ATOM   11   C C   . ILE A 1 4   ? 4.828   14.152 -4.969  1.00  39.07 ? 4    ILE A C   1 
ATOM   12   O O   . ILE A 1 4   ? 4.425   14.882 -5.878  1.00  38.95 ? 4    ILE A O   1 
ATOM   13   C CB  . ILE A 1 4   ? 6.665   12.570 -5.669  1.00  39.49 ? 4    ILE A CB  1 
ATOM   14   C CG1 . ILE A 1 4   ? 7.594   13.024 -4.538  1.00  39.50 ? 4    ILE A CG1 1 
ATOM   15   C CG2 . ILE A 1 4   ? 6.943   13.348 -6.963  1.00  39.23 ? 4    ILE A CG2 1 
ATOM   16   C CD1 . ILE A 1 4   ? 9.039   12.582 -4.702  1.00  40.11 ? 4    ILE A CD1 1 
ATOM   17   N N   . LYS A 1 5   ? 4.981   14.567 -3.713  1.00  38.54 ? 5    LYS A N   1 
ATOM   18   C CA  . LYS A 1 5   ? 4.831   15.968 -3.340  1.00  38.07 ? 5    LYS A CA  1 
ATOM   19   C C   . LYS A 1 5   ? 5.860   16.359 -2.289  1.00  37.73 ? 5    LYS A C   1 
ATOM   20   O O   . LYS A 1 5   ? 6.035   15.657 -1.291  1.00  37.66 ? 5    LYS A O   1 
ATOM   21   C CB  . LYS A 1 5   ? 3.403   16.263 -2.866  1.00  38.02 ? 5    LYS A CB  1 
ATOM   22   C CG  . LYS A 1 5   ? 2.488   16.781 -3.970  1.00  38.64 ? 5    LYS A CG  1 
ATOM   23   C CD  . LYS A 1 5   ? 2.914   18.171 -4.441  1.00  40.05 ? 5    LYS A CD  1 
ATOM   24   C CE  . LYS A 1 5   ? 2.441   18.463 -5.857  1.00  40.76 ? 5    LYS A CE  1 
ATOM   25   N NZ  . LYS A 1 5   ? 2.870   19.823 -6.311  1.00  41.82 ? 5    LYS A NZ  1 
ATOM   26   N N   . ILE A 1 6   ? 6.557   17.468 -2.529  1.00  37.41 ? 6    ILE A N   1 
ATOM   27   C CA  . ILE A 1 6   ? 7.589   17.926 -1.606  1.00  37.20 ? 6    ILE A CA  1 
ATOM   28   C C   . ILE A 1 6   ? 7.172   19.219 -0.926  1.00  37.23 ? 6    ILE A C   1 
ATOM   29   O O   . ILE A 1 6   ? 6.832   20.193 -1.591  1.00  37.15 ? 6    ILE A O   1 
ATOM   30   C CB  . ILE A 1 6   ? 8.966   18.078 -2.293  1.00  37.10 ? 6    ILE A CB  1 
ATOM   31   C CG1 . ILE A 1 6   ? 9.412   16.741 -2.885  1.00  36.83 ? 6    ILE A CG1 1 
ATOM   32   C CG2 . ILE A 1 6   ? 10.017  18.563 -1.299  1.00  37.31 ? 6    ILE A CG2 1 
ATOM   33   C CD1 . ILE A 1 6   ? 10.774  16.777 -3.545  1.00  37.10 ? 6    ILE A CD1 1 
ATOM   34   N N   . PHE A 1 7   ? 7.199   19.202 0.405   1.00  37.43 ? 7    PHE A N   1 
ATOM   35   C CA  . PHE A 1 7   ? 6.833   20.352 1.224   1.00  37.78 ? 7    PHE A CA  1 
ATOM   36   C C   . PHE A 1 7   ? 8.040   20.829 2.022   1.00  38.33 ? 7    PHE A C   1 
ATOM   37   O O   . PHE A 1 7   ? 8.915   20.030 2.345   1.00  38.42 ? 7    PHE A O   1 
ATOM   38   C CB  . PHE A 1 7   ? 5.702   19.960 2.175   1.00  37.65 ? 7    PHE A CB  1 
ATOM   39   C CG  . PHE A 1 7   ? 4.356   19.836 1.510   1.00  36.79 ? 7    PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 7   ? 4.088   18.798 0.632   1.00  35.75 ? 7    PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 7   ? 3.350   20.754 1.786   1.00  36.18 ? 7    PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 7   ? 2.849   18.686 0.028   1.00  35.90 ? 7    PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 7   ? 2.104   20.647 1.189   1.00  35.98 ? 7    PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 7   ? 1.853   19.612 0.306   1.00  35.94 ? 7    PHE A CZ  1 
ATOM   45   N N   . SER A 1 8   ? 8.081   22.123 2.335   1.00  39.24 ? 8    SER A N   1 
ATOM   46   C CA  . SER A 1 8   ? 9.193   22.729 3.083   1.00  40.34 ? 8    SER A CA  1 
ATOM   47   C C   . SER A 1 8   ? 8.820   23.029 4.544   1.00  41.49 ? 8    SER A C   1 
ATOM   48   O O   . SER A 1 8   ? 7.786   22.568 5.031   1.00  41.64 ? 8    SER A O   1 
ATOM   49   C CB  . SER A 1 8   ? 9.656   24.006 2.372   1.00  40.11 ? 8    SER A CB  1 
ATOM   50   O OG  . SER A 1 8   ? 10.726  24.638 3.047   1.00  39.41 ? 8    SER A OG  1 
ATOM   51   N N   . GLY A 1 9   ? 9.670   23.799 5.232   1.00  42.81 ? 9    GLY A N   1 
ATOM   52   C CA  . GLY A 1 9   ? 9.424   24.229 6.619   1.00  44.29 ? 9    GLY A CA  1 
ATOM   53   C C   . GLY A 1 9   ? 9.001   25.685 6.801   1.00  45.22 ? 9    GLY A C   1 
ATOM   54   O O   . GLY A 1 9   ? 8.236   26.220 5.993   1.00  45.18 ? 9    GLY A O   1 
ATOM   55   N N   . SER A 1 10  ? 9.498   26.322 7.865   1.00  46.21 ? 10   SER A N   1 
ATOM   56   C CA  . SER A 1 10  ? 8.987   27.629 8.309   1.00  47.31 ? 10   SER A CA  1 
ATOM   57   C C   . SER A 1 10  ? 9.280   28.725 7.305   1.00  47.97 ? 10   SER A C   1 
ATOM   58   O O   . SER A 1 10  ? 8.387   29.289 6.671   1.00  48.17 ? 10   SER A O   1 
ATOM   59   C CB  . SER A 1 10  ? 9.570   28.014 9.676   1.00  47.26 ? 10   SER A CB  1 
ATOM   60   O OG  . SER A 1 10  ? 9.020   27.242 10.728  1.00  47.23 ? 10   SER A OG  1 
ATOM   61   N N   . SER A 1 11  ? 10.564  29.009 7.192   1.00  48.72 ? 11   SER A N   1 
ATOM   62   C CA  . SER A 1 11  ? 11.073  29.936 6.226   1.00  49.26 ? 11   SER A CA  1 
ATOM   63   C C   . SER A 1 11  ? 12.169  28.864 6.117   1.00  49.39 ? 11   SER A C   1 
ATOM   64   O O   . SER A 1 11  ? 11.923  27.694 6.531   1.00  49.54 ? 11   SER A O   1 
ATOM   65   C CB  . SER A 1 11  ? 11.649  31.180 6.985   1.00  49.37 ? 11   SER A CB  1 
ATOM   66   O OG  . SER A 1 11  ? 11.072  32.373 6.453   1.00  49.96 ? 11   SER A OG  1 
ATOM   67   N N   . HIS A 1 12  ? 13.363  29.239 5.618   0.58  49.36 ? 12   HIS A N   1 
ATOM   68   C CA  . HIS A 1 12  ? 14.479  28.253 5.368   0.58  49.34 ? 12   HIS A CA  1 
ATOM   69   C C   . HIS A 1 12  ? 14.282  27.412 4.076   0.58  49.01 ? 12   HIS A C   1 
ATOM   70   O O   . HIS A 1 12  ? 14.853  26.307 3.886   0.58  48.96 ? 12   HIS A O   1 
ATOM   71   C CB  . HIS A 1 12  ? 14.973  27.306 6.538   0.58  49.54 ? 12   HIS A CB  1 
ATOM   72   C CG  . HIS A 1 12  ? 15.842  26.185 6.026   0.58  50.18 ? 12   HIS A CG  1 
ATOM   73   N ND1 . HIS A 1 12  ? 15.525  24.859 6.218   0.58  50.84 ? 12   HIS A ND1 1 
ATOM   74   C CD2 . HIS A 1 12  ? 16.957  26.193 5.251   0.58  50.86 ? 12   HIS A CD2 1 
ATOM   75   C CE1 . HIS A 1 12  ? 16.428  24.098 5.622   0.58  51.32 ? 12   HIS A CE1 1 
ATOM   76   N NE2 . HIS A 1 12  ? 17.307  24.883 5.027   0.58  51.35 ? 12   HIS A NE2 1 
ATOM   77   N N   . GLN A 1 13  ? 13.507  27.981 3.164   1.00  48.62 ? 13   GLN A N   1 
ATOM   78   C CA  . GLN A 1 13  ? 13.202  27.317 1.897   1.00  48.27 ? 13   GLN A CA  1 
ATOM   79   C C   . GLN A 1 13  ? 14.361  26.849 0.998   1.00  47.75 ? 13   GLN A C   1 
ATOM   80   O O   . GLN A 1 13  ? 14.149  25.982 0.152   1.00  48.01 ? 13   GLN A O   1 
ATOM   81   C CB  . GLN A 1 13  ? 12.250  28.187 1.079   1.00  48.37 ? 13   GLN A CB  1 
ATOM   82   C CG  . GLN A 1 13  ? 10.790  28.051 1.509   1.00  49.05 ? 13   GLN A CG  1 
ATOM   83   C CD  . GLN A 1 13  ? 9.834   28.169 0.340   1.00  49.81 ? 13   GLN A CD  1 
ATOM   84   O OE1 . GLN A 1 13  ? 8.637   27.912 0.481   1.00  49.98 ? 13   GLN A OE1 1 
ATOM   85   N NE2 . GLN A 1 13  ? 10.355  28.561 -0.823  1.00  50.16 ? 13   GLN A NE2 1 
ATOM   86   N N   . ASP A 1 14  ? 15.561  27.409 1.162   1.00  46.95 ? 14   ASP A N   1 
ATOM   87   C CA  . ASP A 1 14  ? 16.637  27.199 0.180   1.00  46.10 ? 14   ASP A CA  1 
ATOM   88   C C   . ASP A 1 14  ? 16.929  25.729 -0.112  1.00  45.29 ? 14   ASP A C   1 
ATOM   89   O O   . ASP A 1 14  ? 16.829  25.291 -1.265  1.00  45.05 ? 14   ASP A O   1 
ATOM   90   C CB  . ASP A 1 14  ? 17.923  27.941 0.574   1.00  46.39 ? 14   ASP A CB  1 
ATOM   91   C CG  . ASP A 1 14  ? 18.846  28.202 -0.624  1.00  46.49 ? 14   ASP A CG  1 
ATOM   92   O OD1 . ASP A 1 14  ? 20.080  28.317 -0.419  1.00  46.61 ? 14   ASP A OD1 1 
ATOM   93   O OD2 . ASP A 1 14  ? 18.336  28.299 -1.766  1.00  46.03 ? 14   ASP A OD2 1 
ATOM   94   N N   . LEU A 1 15  ? 17.275  24.973 0.928   1.00  44.41 ? 15   LEU A N   1 
ATOM   95   C CA  . LEU A 1 15  ? 17.563  23.545 0.776   1.00  43.65 ? 15   LEU A CA  1 
ATOM   96   C C   . LEU A 1 15  ? 16.413  22.807 0.072   1.00  43.12 ? 15   LEU A C   1 
ATOM   97   O O   . LEU A 1 15  ? 16.647  22.044 -0.867  1.00  43.13 ? 15   LEU A O   1 
ATOM   98   C CB  . LEU A 1 15  ? 17.868  22.892 2.134   1.00  43.60 ? 15   LEU A CB  1 
ATOM   99   C CG  . LEU A 1 15  ? 19.039  21.896 2.255   1.00  43.29 ? 15   LEU A CG  1 
ATOM   100  C CD1 . LEU A 1 15  ? 18.720  20.809 3.286   1.00  43.71 ? 15   LEU A CD1 1 
ATOM   101  C CD2 . LEU A 1 15  ? 19.452  21.255 0.923   1.00  42.53 ? 15   LEU A CD2 1 
ATOM   102  N N   . SER A 1 16  ? 15.179  23.051 0.520   1.00  42.34 ? 16   SER A N   1 
ATOM   103  C CA  . SER A 1 16  ? 13.988  22.455 -0.094  1.00  41.64 ? 16   SER A CA  1 
ATOM   104  C C   . SER A 1 16  ? 13.865  22.826 -1.564  1.00  41.06 ? 16   SER A C   1 
ATOM   105  O O   . SER A 1 16  ? 13.866  21.953 -2.431  1.00  41.14 ? 16   SER A O   1 
ATOM   106  C CB  . SER A 1 16  ? 12.725  22.875 0.651   1.00  41.55 ? 16   SER A CB  1 
ATOM   107  O OG  . SER A 1 16  ? 12.739  22.365 1.966   1.00  42.13 ? 16   SER A OG  1 
ATOM   108  N N   . GLN A 1 17  ? 13.773  24.126 -1.829  1.00  40.31 ? 17   GLN A N   1 
ATOM   109  C CA  . GLN A 1 17  ? 13.738  24.659 -3.183  1.00  39.72 ? 17   GLN A CA  1 
ATOM   110  C C   . GLN A 1 17  ? 14.789  24.001 -4.078  1.00  39.16 ? 17   GLN A C   1 
ATOM   111  O O   . GLN A 1 17  ? 14.506  23.686 -5.233  1.00  39.00 ? 17   GLN A O   1 
ATOM   112  C CB  . GLN A 1 17  ? 13.926  26.181 -3.159  1.00  39.87 ? 17   GLN A CB  1 
ATOM   113  C CG  . GLN A 1 17  ? 13.443  26.888 -4.416  1.00  40.64 ? 17   GLN A CG  1 
ATOM   114  C CD  . GLN A 1 17  ? 11.998  26.551 -4.754  1.00  42.09 ? 17   GLN A CD  1 
ATOM   115  O OE1 . GLN A 1 17  ? 11.084  26.816 -3.964  1.00  42.38 ? 17   GLN A OE1 1 
ATOM   116  N NE2 . GLN A 1 17  ? 11.786  25.958 -5.931  1.00  42.63 ? 17   GLN A NE2 1 
ATOM   117  N N   . LYS A 1 18  ? 15.991  23.793 -3.538  1.00  38.50 ? 18   LYS A N   1 
ATOM   118  C CA  . LYS A 1 18  ? 17.043  23.091 -4.263  1.00  37.96 ? 18   LYS A CA  1 
ATOM   119  C C   . LYS A 1 18  ? 16.658  21.636 -4.509  1.00  37.60 ? 18   LYS A C   1 
ATOM   120  O O   . LYS A 1 18  ? 16.808  21.131 -5.621  1.00  37.75 ? 18   LYS A O   1 
ATOM   121  C CB  . LYS A 1 18  ? 18.381  23.182 -3.523  1.00  37.93 ? 18   LYS A CB  1 
ATOM   122  C CG  . LYS A 1 18  ? 19.026  24.567 -3.595  1.00  38.18 ? 18   LYS A CG  1 
ATOM   123  C CD  . LYS A 1 18  ? 20.548  24.500 -3.375  1.00  37.76 ? 18   LYS A CD  1 
ATOM   124  C CE  . LYS A 1 18  ? 21.246  25.719 -3.981  1.00  37.13 ? 18   LYS A CE  1 
ATOM   125  N NZ  . LYS A 1 18  ? 20.814  27.007 -3.367  1.00  36.81 ? 18   LYS A NZ  1 
ATOM   126  N N   . ILE A 1 19  ? 16.146  20.972 -3.477  1.00  37.06 ? 19   ILE A N   1 
ATOM   127  C CA  . ILE A 1 19  ? 15.775  19.565 -3.573  1.00  36.57 ? 19   ILE A CA  1 
ATOM   128  C C   . ILE A 1 19  ? 14.672  19.365 -4.609  1.00  36.42 ? 19   ILE A C   1 
ATOM   129  O O   . ILE A 1 19  ? 14.730  18.436 -5.418  1.00  36.56 ? 19   ILE A O   1 
ATOM   130  C CB  . ILE A 1 19  ? 15.362  18.996 -2.197  1.00  36.49 ? 19   ILE A CB  1 
ATOM   131  C CG1 . ILE A 1 19  ? 16.604  18.779 -1.330  1.00  36.05 ? 19   ILE A CG1 1 
ATOM   132  C CG2 . ILE A 1 19  ? 14.587  17.687 -2.348  1.00  36.56 ? 19   ILE A CG2 1 
ATOM   133  C CD1 . ILE A 1 19  ? 16.343  18.852 0.159   1.00  35.42 ? 19   ILE A CD1 1 
ATOM   134  N N   . ALA A 1 20  ? 13.680  20.250 -4.593  1.00  36.09 ? 20   ALA A N   1 
ATOM   135  C CA  . ALA A 1 20  ? 12.567  20.178 -5.542  1.00  35.78 ? 20   ALA A CA  1 
ATOM   136  C C   . ALA A 1 20  ? 13.006  20.463 -6.972  1.00  35.69 ? 20   ALA A C   1 
ATOM   137  O O   . ALA A 1 20  ? 12.387  19.975 -7.916  1.00  35.70 ? 20   ALA A O   1 
ATOM   138  C CB  . ALA A 1 20  ? 11.445  21.117 -5.133  1.00  35.74 ? 20   ALA A CB  1 
ATOM   139  N N   . ASP A 1 21  ? 14.073  21.250 -7.123  1.00  35.64 ? 21   ASP A N   1 
ATOM   140  C CA  . ASP A 1 21  ? 14.630  21.569 -8.438  1.00  35.33 ? 21   ASP A CA  1 
ATOM   141  C C   . ASP A 1 21  ? 15.228  20.327 -9.072  1.00  34.87 ? 21   ASP A C   1 
ATOM   142  O O   . ASP A 1 21  ? 14.864  19.962 -10.188 1.00  35.01 ? 21   ASP A O   1 
ATOM   143  C CB  . ASP A 1 21  ? 15.685  22.686 -8.351  1.00  35.53 ? 21   ASP A CB  1 
ATOM   144  C CG  . ASP A 1 21  ? 15.068  24.068 -8.160  1.00  36.13 ? 21   ASP A CG  1 
ATOM   145  O OD1 . ASP A 1 21  ? 13.893  24.269 -8.538  1.00  36.73 ? 21   ASP A OD1 1 
ATOM   146  O OD2 . ASP A 1 21  ? 15.754  24.958 -7.620  1.00  37.26 ? 21   ASP A OD2 1 
ATOM   147  N N   . ARG A 1 22  ? 16.119  19.662 -8.345  0.80  34.21 ? 22   ARG A N   1 
ATOM   148  C CA  . ARG A 1 22  ? 16.838  18.510 -8.875  0.80  33.76 ? 22   ARG A CA  1 
ATOM   149  C C   . ARG A 1 22  ? 15.925  17.351 -9.251  0.80  33.16 ? 22   ARG A C   1 
ATOM   150  O O   . ARG A 1 22  ? 16.360  16.396 -9.893  0.80  33.13 ? 22   ARG A O   1 
ATOM   151  C CB  . ARG A 1 22  ? 17.887  18.044 -7.875  0.80  33.95 ? 22   ARG A CB  1 
ATOM   152  C CG  . ARG A 1 22  ? 18.990  19.047 -7.646  0.80  35.03 ? 22   ARG A CG  1 
ATOM   153  C CD  . ARG A 1 22  ? 20.005  18.506 -6.670  0.80  37.10 ? 22   ARG A CD  1 
ATOM   154  N NE  . ARG A 1 22  ? 21.076  19.464 -6.407  0.80  39.36 ? 22   ARG A NE  1 
ATOM   155  C CZ  . ARG A 1 22  ? 22.185  19.583 -7.136  0.80  40.45 ? 22   ARG A CZ  1 
ATOM   156  N NH1 . ARG A 1 22  ? 22.388  18.794 -8.191  0.80  40.81 ? 22   ARG A NH1 1 
ATOM   157  N NH2 . ARG A 1 22  ? 23.099  20.494 -6.802  0.80  40.14 ? 22   ARG A NH2 1 
ATOM   158  N N   . LEU A 1 23  ? 14.662  17.449 -8.849  1.00  32.53 ? 23   LEU A N   1 
ATOM   159  C CA  . LEU A 1 23  ? 13.668  16.415 -9.120  1.00  31.88 ? 23   LEU A CA  1 
ATOM   160  C C   . LEU A 1 23  ? 12.654  16.878 -10.160 1.00  31.45 ? 23   LEU A C   1 
ATOM   161  O O   . LEU A 1 23  ? 11.839  16.092 -10.651 1.00  31.34 ? 23   LEU A O   1 
ATOM   162  C CB  . LEU A 1 23  ? 12.957  16.014 -7.827  1.00  31.80 ? 23   LEU A CB  1 
ATOM   163  C CG  . LEU A 1 23  ? 13.763  15.186 -6.828  1.00  31.38 ? 23   LEU A CG  1 
ATOM   164  C CD1 . LEU A 1 23  ? 13.032  15.147 -5.506  1.00  31.05 ? 23   LEU A CD1 1 
ATOM   165  C CD2 . LEU A 1 23  ? 14.031  13.774 -7.352  1.00  30.59 ? 23   LEU A CD2 1 
ATOM   166  N N   . GLY A 1 24  ? 12.715  18.165 -10.483 1.00  31.01 ? 24   GLY A N   1 
ATOM   167  C CA  . GLY A 1 24  ? 11.855  18.763 -11.497 1.00  30.27 ? 24   GLY A CA  1 
ATOM   168  C C   . GLY A 1 24  ? 10.427  18.973 -11.045 1.00  29.69 ? 24   GLY A C   1 
ATOM   169  O O   . GLY A 1 24  ? 9.508   18.894 -11.858 1.00  29.76 ? 24   GLY A O   1 
ATOM   170  N N   . LEU A 1 25  ? 10.248  19.233 -9.750  1.00  29.18 ? 25   LEU A N   1 
ATOM   171  C CA  . LEU A 1 25  ? 8.937   19.543 -9.167  1.00  28.57 ? 25   LEU A CA  1 
ATOM   172  C C   . LEU A 1 25  ? 8.931   20.938 -8.559  1.00  28.20 ? 25   LEU A C   1 
ATOM   173  O O   . LEU A 1 25  ? 9.989   21.537 -8.363  1.00  28.30 ? 25   LEU A O   1 
ATOM   174  C CB  . LEU A 1 25  ? 8.594   18.560 -8.048  1.00  28.57 ? 25   LEU A CB  1 
ATOM   175  C CG  . LEU A 1 25  ? 8.779   17.055 -8.157  1.00  27.85 ? 25   LEU A CG  1 
ATOM   176  C CD1 . LEU A 1 25  ? 8.733   16.502 -6.748  1.00  27.20 ? 25   LEU A CD1 1 
ATOM   177  C CD2 . LEU A 1 25  ? 7.701   16.445 -9.041  1.00  27.12 ? 25   LEU A CD2 1 
ATOM   178  N N   . GLU A 1 26  ? 7.740   21.442 -8.250  0.40  27.74 ? 26   GLU A N   1 
ATOM   179  C CA  . GLU A 1 26  ? 7.604   22.660 -7.464  0.40  27.39 ? 26   GLU A CA  1 
ATOM   180  C C   . GLU A 1 26  ? 7.166   22.286 -6.059  0.40  27.24 ? 26   GLU A C   1 
ATOM   181  O O   . GLU A 1 26  ? 6.321   21.403 -5.884  0.40  27.08 ? 26   GLU A O   1 
ATOM   182  C CB  . GLU A 1 26  ? 6.587   23.609 -8.096  0.40  27.34 ? 26   GLU A CB  1 
ATOM   183  C CG  . GLU A 1 26  ? 7.090   24.326 -9.335  0.40  27.37 ? 26   GLU A CG  1 
ATOM   184  C CD  . GLU A 1 26  ? 6.087   25.332 -9.873  0.40  27.62 ? 26   GLU A CD  1 
ATOM   185  O OE1 . GLU A 1 26  ? 5.151   25.705 -9.132  0.40  27.75 ? 26   GLU A OE1 1 
ATOM   186  O OE2 . GLU A 1 26  ? 6.233   25.751 -11.040 0.40  27.55 ? 26   GLU A OE2 1 
ATOM   187  N N   . LEU A 1 27  ? 7.746   22.954 -5.063  1.00  27.22 ? 27   LEU A N   1 
ATOM   188  C CA  . LEU A 1 27  ? 7.379   22.743 -3.668  1.00  27.14 ? 27   LEU A CA  1 
ATOM   189  C C   . LEU A 1 27  ? 5.888   22.942 -3.502  1.00  27.36 ? 27   LEU A C   1 
ATOM   190  O O   . LEU A 1 27  ? 5.293   23.779 -4.166  1.00  26.83 ? 27   LEU A O   1 
ATOM   191  C CB  . LEU A 1 27  ? 8.133   23.703 -2.737  1.00  27.11 ? 27   LEU A CB  1 
ATOM   192  C CG  . LEU A 1 27  ? 9.619   23.484 -2.429  1.00  26.56 ? 27   LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 27  ? 10.137  24.621 -1.556  1.00  25.35 ? 27   LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 27  ? 9.859   22.134 -1.766  1.00  26.02 ? 27   LEU A CD2 1 
ATOM   195  N N   . GLY A 1 28  ? 5.296   22.164 -2.605  1.00  28.28 ? 28   GLY A N   1 
ATOM   196  C CA  . GLY A 1 28  ? 3.854   22.168 -2.396  1.00  29.34 ? 28   GLY A CA  1 
ATOM   197  C C   . GLY A 1 28  ? 3.376   23.419 -1.693  1.00  30.10 ? 28   GLY A C   1 
ATOM   198  O O   . GLY A 1 28  ? 4.134   24.058 -0.956  1.00  30.07 ? 28   GLY A O   1 
ATOM   199  N N   . LYS A 1 29  ? 2.112   23.759 -1.926  0.40  30.89 ? 29   LYS A N   1 
ATOM   200  C CA  . LYS A 1 29  ? 1.496   24.929 -1.322  0.40  31.84 ? 29   LYS A CA  1 
ATOM   201  C C   . LYS A 1 29  ? 1.155   24.674 0.144   0.40  32.70 ? 29   LYS A C   1 
ATOM   202  O O   . LYS A 1 29  ? 0.525   23.674 0.483   0.40  32.69 ? 29   LYS A O   1 
ATOM   203  C CB  . LYS A 1 29  ? 0.254   25.343 -2.113  0.40  31.73 ? 29   LYS A CB  1 
ATOM   204  C CG  . LYS A 1 29  ? 0.521   25.533 -3.604  0.40  31.71 ? 29   LYS A CG  1 
ATOM   205  C CD  . LYS A 1 29  ? -0.536  26.409 -4.273  0.40  31.73 ? 29   LYS A CD  1 
ATOM   206  C CE  . LYS A 1 29  ? -1.834  25.654 -4.534  0.40  31.89 ? 29   LYS A CE  1 
ATOM   207  N NZ  . LYS A 1 29  ? -1.723  24.665 -5.647  0.40  31.87 ? 29   LYS A NZ  1 
ATOM   208  N N   . VAL A 1 30  ? 1.603   25.589 0.999   1.00  33.96 ? 30   VAL A N   1 
ATOM   209  C CA  . VAL A 1 30  ? 1.404   25.527 2.447   1.00  35.47 ? 30   VAL A CA  1 
ATOM   210  C C   . VAL A 1 30  ? 1.165   26.956 2.968   1.00  36.72 ? 30   VAL A C   1 
ATOM   211  O O   . VAL A 1 30  ? 1.451   27.929 2.263   1.00  36.80 ? 30   VAL A O   1 
ATOM   212  C CB  . VAL A 1 30  ? 2.634   24.881 3.160   1.00  35.32 ? 30   VAL A CB  1 
ATOM   213  C CG1 . VAL A 1 30  ? 3.796   25.877 3.288   1.00  35.40 ? 30   VAL A CG1 1 
ATOM   214  C CG2 . VAL A 1 30  ? 2.246   24.334 4.523   1.00  35.28 ? 30   VAL A CG2 1 
ATOM   215  N N   . VAL A 1 31  ? 0.641   27.087 4.189   1.00  38.33 ? 31   VAL A N   1 
ATOM   216  C CA  . VAL A 1 31  ? 0.418   28.411 4.788   1.00  39.77 ? 31   VAL A CA  1 
ATOM   217  C C   . VAL A 1 31  ? 0.959   28.469 6.227   1.00  40.86 ? 31   VAL A C   1 
ATOM   218  O O   . VAL A 1 31  ? 0.221   28.739 7.178   1.00  41.14 ? 31   VAL A O   1 
ATOM   219  C CB  . VAL A 1 31  ? -1.084  28.825 4.735   1.00  39.64 ? 31   VAL A CB  1 
ATOM   220  C CG1 . VAL A 1 31  ? -1.266  30.281 5.172   1.00  39.81 ? 31   VAL A CG1 1 
ATOM   221  C CG2 . VAL A 1 31  ? -1.653  28.631 3.331   1.00  39.90 ? 31   VAL A CG2 1 
ATOM   222  N N   . THR A 1 32  ? 2.256   28.222 6.378   1.00  42.25 ? 32   THR A N   1 
ATOM   223  C CA  . THR A 1 32  ? 2.874   28.170 7.706   1.00  43.61 ? 32   THR A CA  1 
ATOM   224  C C   . THR A 1 32  ? 3.119   29.549 8.302   1.00  44.19 ? 32   THR A C   1 
ATOM   225  O O   . THR A 1 32  ? 3.726   30.410 7.664   1.00  44.31 ? 32   THR A O   1 
ATOM   226  C CB  . THR A 1 32  ? 4.200   27.369 7.698   1.00  43.78 ? 32   THR A CB  1 
ATOM   227  O OG1 . THR A 1 32  ? 5.044   27.828 6.625   1.00  43.79 ? 32   THR A OG1 1 
ATOM   228  C CG2 . THR A 1 32  ? 3.918   25.861 7.540   1.00  43.92 ? 32   THR A CG2 1 
ATOM   229  N N   . LYS A 1 33  ? 2.641   29.748 9.527   0.010 45.05 ? 33   LYS A N   1 
ATOM   230  C CA  . LYS A 1 33  ? 2.846   31.002 10.241  0.010 45.84 ? 33   LYS A CA  1 
ATOM   231  C C   . LYS A 1 33  ? 2.774   30.812 11.751  0.010 46.40 ? 33   LYS A C   1 
ATOM   232  O O   . LYS A 1 33  ? 2.452   29.727 12.243  0.010 46.46 ? 33   LYS A O   1 
ATOM   233  C CB  . LYS A 1 33  ? 1.835   32.062 9.786   0.010 45.81 ? 33   LYS A CB  1 
ATOM   234  C CG  . LYS A 1 33  ? 0.384   31.641 9.919   0.010 45.86 ? 33   LYS A CG  1 
ATOM   235  C CD  . LYS A 1 33  ? -0.550  32.778 9.538   0.010 45.89 ? 33   LYS A CD  1 
ATOM   236  C CE  . LYS A 1 33  ? -1.998  32.321 9.522   0.010 45.90 ? 33   LYS A CE  1 
ATOM   237  N NZ  . LYS A 1 33  ? -2.235  31.274 8.490   0.010 45.90 ? 33   LYS A NZ  1 
ATOM   238  N N   . LYS A 1 34  ? 3.083   31.887 12.468  1.00  47.11 ? 34   LYS A N   1 
ATOM   239  C CA  . LYS A 1 34  ? 3.061   31.922 13.919  1.00  47.81 ? 34   LYS A CA  1 
ATOM   240  C C   . LYS A 1 34  ? 1.937   32.850 14.383  1.00  48.11 ? 34   LYS A C   1 
ATOM   241  O O   . LYS A 1 34  ? 1.855   33.998 13.939  1.00  48.25 ? 34   LYS A O   1 
ATOM   242  C CB  . LYS A 1 34  ? 4.396   32.469 14.441  1.00  47.95 ? 34   LYS A CB  1 
ATOM   243  C CG  . LYS A 1 34  ? 5.615   31.554 14.292  1.00  48.47 ? 34   LYS A CG  1 
ATOM   244  C CD  . LYS A 1 34  ? 6.860   32.200 14.927  1.00  49.32 ? 34   LYS A CD  1 
ATOM   245  C CE  . LYS A 1 34  ? 6.574   32.668 16.369  1.00  49.61 ? 34   LYS A CE  1 
ATOM   246  N NZ  . LYS A 1 34  ? 7.700   33.461 16.963  1.00  49.63 ? 34   LYS A NZ  1 
ATOM   247  N N   . PHE A 1 35  ? 1.066   32.369 15.267  1.00  48.47 ? 35   PHE A N   1 
ATOM   248  C CA  . PHE A 1 35  ? 0.093   33.261 15.898  1.00  48.74 ? 35   PHE A CA  1 
ATOM   249  C C   . PHE A 1 35  ? 0.838   34.162 16.866  1.00  48.82 ? 35   PHE A C   1 
ATOM   250  O O   . PHE A 1 35  ? 1.952   33.837 17.297  1.00  48.86 ? 35   PHE A O   1 
ATOM   251  C CB  . PHE A 1 35  ? -1.008  32.498 16.648  1.00  48.87 ? 35   PHE A CB  1 
ATOM   252  C CG  . PHE A 1 35  ? -1.989  31.785 15.758  1.00  49.50 ? 35   PHE A CG  1 
ATOM   253  C CD1 . PHE A 1 35  ? -2.698  30.694 16.242  1.00  50.42 ? 35   PHE A CD1 1 
ATOM   254  C CD2 . PHE A 1 35  ? -2.204  32.192 14.444  1.00  50.50 ? 35   PHE A CD2 1 
ATOM   255  C CE1 . PHE A 1 35  ? -3.609  30.014 15.432  1.00  51.28 ? 35   PHE A CE1 1 
ATOM   256  C CE2 . PHE A 1 35  ? -3.110  31.520 13.623  1.00  51.13 ? 35   PHE A CE2 1 
ATOM   257  C CZ  . PHE A 1 35  ? -3.816  30.428 14.120  1.00  51.29 ? 35   PHE A CZ  1 
ATOM   258  N N   . SER A 1 36  ? 0.214   35.287 17.210  0.010 48.88 ? 36   SER A N   1 
ATOM   259  C CA  . SER A 1 36  ? 0.798   36.281 18.109  0.010 48.94 ? 36   SER A CA  1 
ATOM   260  C C   . SER A 1 36  ? 1.149   35.703 19.480  0.010 49.01 ? 36   SER A C   1 
ATOM   261  O O   . SER A 1 36  ? 1.989   36.250 20.193  0.010 49.00 ? 36   SER A O   1 
ATOM   262  C CB  . SER A 1 36  ? -0.148  37.474 18.267  0.010 48.93 ? 36   SER A CB  1 
ATOM   263  O OG  . SER A 1 36  ? 0.394   38.442 19.148  0.010 48.94 ? 36   SER A OG  1 
ATOM   264  N N   . ASN A 1 37  ? 0.510   34.591 19.838  0.50  49.11 ? 37   ASN A N   1 
ATOM   265  C CA  . ASN A 1 37  ? 0.780   33.936 21.116  0.50  49.26 ? 37   ASN A CA  1 
ATOM   266  C C   . ASN A 1 37  ? 1.625   32.665 20.999  0.50  49.38 ? 37   ASN A C   1 
ATOM   267  O O   . ASN A 1 37  ? 1.385   31.682 21.704  0.50  49.30 ? 37   ASN A O   1 
ATOM   268  C CB  . ASN A 1 37  ? -0.522  33.636 21.858  0.50  49.25 ? 37   ASN A CB  1 
ATOM   269  C CG  . ASN A 1 37  ? -1.385  32.633 21.133  0.50  49.25 ? 37   ASN A CG  1 
ATOM   270  O OD1 . ASN A 1 37  ? -1.168  32.348 19.957  0.50  49.45 ? 37   ASN A OD1 1 
ATOM   271  N ND2 . ASN A 1 37  ? -2.378  32.093 21.831  0.50  49.02 ? 37   ASN A ND2 1 
ATOM   272  N N   . GLN A 1 38  ? 2.605   32.702 20.095  1.00  49.61 ? 38   GLN A N   1 
ATOM   273  C CA  . GLN A 1 38  ? 3.652   31.671 19.950  1.00  49.84 ? 38   GLN A CA  1 
ATOM   274  C C   . GLN A 1 38  ? 3.221   30.303 19.377  1.00  49.87 ? 38   GLN A C   1 
ATOM   275  O O   . GLN A 1 38  ? 4.077   29.399 19.189  1.00  50.20 ? 38   GLN A O   1 
ATOM   276  C CB  . GLN A 1 38  ? 4.443   31.470 21.259  1.00  49.86 ? 38   GLN A CB  1 
ATOM   277  C CG  . GLN A 1 38  ? 4.713   32.734 22.087  1.00  51.21 ? 38   GLN A CG  1 
ATOM   278  C CD  . GLN A 1 38  ? 5.684   33.725 21.444  1.00  53.04 ? 38   GLN A CD  1 
ATOM   279  O OE1 . GLN A 1 38  ? 6.146   33.538 20.312  1.00  54.05 ? 38   GLN A OE1 1 
ATOM   280  N NE2 . GLN A 1 38  ? 5.998   34.793 22.179  1.00  53.06 ? 38   GLN A NE2 1 
ATOM   281  N N   . GLU A 1 39  ? 1.922   30.153 19.072  1.00  49.73 ? 39   GLU A N   1 
ATOM   282  C CA  . GLU A 1 39  ? 1.411   28.897 18.493  1.00  49.47 ? 39   GLU A CA  1 
ATOM   283  C C   . GLU A 1 39  ? 1.849   28.726 17.044  1.00  49.11 ? 39   GLU A C   1 
ATOM   284  O O   . GLU A 1 39  ? 2.152   29.709 16.369  1.00  49.15 ? 39   GLU A O   1 
ATOM   285  C CB  . GLU A 1 39  ? -0.113  28.857 18.561  1.00  49.55 ? 39   GLU A CB  1 
ATOM   286  C CG  . GLU A 1 39  ? -0.674  28.701 19.961  1.00  50.39 ? 39   GLU A CG  1 
ATOM   287  C CD  . GLU A 1 39  ? -2.094  28.165 19.959  1.00  51.67 ? 39   GLU A CD  1 
ATOM   288  O OE1 . GLU A 1 39  ? -2.455  27.428 19.010  1.00  51.46 ? 39   GLU A OE1 1 
ATOM   289  O OE2 . GLU A 1 39  ? -2.844  28.475 20.913  1.00  52.52 ? 39   GLU A OE2 1 
ATOM   290  N N   . THR A 1 40  ? 1.869   27.486 16.558  1.00  48.73 ? 40   THR A N   1 
ATOM   291  C CA  . THR A 1 40  ? 2.222   27.233 15.155  1.00  48.35 ? 40   THR A CA  1 
ATOM   292  C C   . THR A 1 40  ? 1.019   26.840 14.300  1.00  47.84 ? 40   THR A C   1 
ATOM   293  O O   . THR A 1 40  ? 0.337   25.854 14.577  1.00  47.76 ? 40   THR A O   1 
ATOM   294  C CB  . THR A 1 40  ? 3.384   26.224 15.004  1.00  48.56 ? 40   THR A CB  1 
ATOM   295  O OG1 . THR A 1 40  ? 4.547   26.730 15.681  1.00  49.04 ? 40   THR A OG1 1 
ATOM   296  C CG2 . THR A 1 40  ? 3.723   26.013 13.531  1.00  48.43 ? 40   THR A CG2 1 
ATOM   297  N N   . CYS A 1 41  ? 0.789   27.628 13.254  0.89  47.28 ? 41   CYS A N   1 
ATOM   298  C CA  . CYS A 1 41  ? -0.375  27.503 12.375  0.89  46.66 ? 41   CYS A CA  1 
ATOM   299  C C   . CYS A 1 41  ? 0.002   26.934 11.005  0.89  45.70 ? 41   CYS A C   1 
ATOM   300  O O   . CYS A 1 41  ? 0.978   27.381 10.386  0.89  45.72 ? 41   CYS A O   1 
ATOM   301  C CB  . CYS A 1 41  ? -1.069  28.873 12.253  0.89  46.89 ? 41   CYS A CB  1 
ATOM   302  S SG  . CYS A 1 41  ? -1.359  29.529 10.566  0.89  48.31 ? 41   CYS A SG  1 
ATOM   303  N N   . VAL A 1 42  ? -0.769  25.945 10.546  1.00  44.39 ? 42   VAL A N   1 
ATOM   304  C CA  . VAL A 1 42  ? -0.483  25.249 9.283   1.00  43.17 ? 42   VAL A CA  1 
ATOM   305  C C   . VAL A 1 42  ? -1.737  24.986 8.450   1.00  42.35 ? 42   VAL A C   1 
ATOM   306  O O   . VAL A 1 42  ? -2.763  24.533 8.964   1.00  42.29 ? 42   VAL A O   1 
ATOM   307  C CB  . VAL A 1 42  ? 0.272   23.910 9.515   1.00  43.22 ? 42   VAL A CB  1 
ATOM   308  C CG1 . VAL A 1 42  ? 0.325   23.081 8.235   1.00  42.71 ? 42   VAL A CG1 1 
ATOM   309  C CG2 . VAL A 1 42  ? 1.687   24.163 10.032  1.00  43.16 ? 42   VAL A CG2 1 
ATOM   310  N N   . GLU A 1 43  ? -1.631  25.264 7.155   0.40  41.28 ? 43   GLU A N   1 
ATOM   311  C CA  . GLU A 1 43  ? -2.691  24.975 6.203   0.40  40.18 ? 43   GLU A CA  1 
ATOM   312  C C   . GLU A 1 43  ? -2.068  24.389 4.947   0.40  39.45 ? 43   GLU A C   1 
ATOM   313  O O   . GLU A 1 43  ? -1.299  25.062 4.258   0.40  39.35 ? 43   GLU A O   1 
ATOM   314  C CB  . GLU A 1 43  ? -3.439  26.257 5.848   0.40  40.29 ? 43   GLU A CB  1 
ATOM   315  C CG  . GLU A 1 43  ? -4.893  26.062 5.470   0.40  39.98 ? 43   GLU A CG  1 
ATOM   316  C CD  . GLU A 1 43  ? -5.801  26.074 6.679   0.40  39.58 ? 43   GLU A CD  1 
ATOM   317  O OE1 . GLU A 1 43  ? -6.892  26.677 6.598   0.40  39.01 ? 43   GLU A OE1 1 
ATOM   318  O OE2 . GLU A 1 43  ? -5.418  25.489 7.713   0.40  39.66 ? 43   GLU A OE2 1 
ATOM   319  N N   . ILE A 1 44  ? -2.394  23.129 4.663   1.00  38.52 ? 44   ILE A N   1 
ATOM   320  C CA  . ILE A 1 44  ? -1.927  22.447 3.448   1.00  37.53 ? 44   ILE A CA  1 
ATOM   321  C C   . ILE A 1 44  ? -2.696  22.960 2.234   1.00  36.75 ? 44   ILE A C   1 
ATOM   322  O O   . ILE A 1 44  ? -3.886  22.680 2.066   1.00  36.62 ? 44   ILE A O   1 
ATOM   323  C CB  . ILE A 1 44  ? -2.073  20.898 3.543   1.00  37.57 ? 44   ILE A CB  1 
ATOM   324  C CG1 . ILE A 1 44  ? -1.223  20.321 4.689   1.00  37.60 ? 44   ILE A CG1 1 
ATOM   325  C CG2 . ILE A 1 44  ? -1.715  20.236 2.207   1.00  37.42 ? 44   ILE A CG2 1 
ATOM   326  C CD1 . ILE A 1 44  ? 0.291   20.232 4.410   1.00  37.02 ? 44   ILE A CD1 1 
ATOM   327  N N   . GLY A 1 45  ? -2.005  23.703 1.381   1.00  35.90 ? 45   GLY A N   1 
ATOM   328  C CA  . GLY A 1 45  ? -2.657  24.413 0.291   1.00  34.97 ? 45   GLY A CA  1 
ATOM   329  C C   . GLY A 1 45  ? -3.052  23.588 -0.918  1.00  34.32 ? 45   GLY A C   1 
ATOM   330  O O   . GLY A 1 45  ? -3.392  24.153 -1.950  1.00  34.23 ? 45   GLY A O   1 
ATOM   331  N N   . GLU A 1 46  ? -3.005  22.264 -0.804  0.88  33.82 ? 46   GLU A N   1 
ATOM   332  C CA  . GLU A 1 46  ? -3.451  21.378 -1.887  0.88  33.35 ? 46   GLU A CA  1 
ATOM   333  C C   . GLU A 1 46  ? -3.834  19.988 -1.374  0.88  32.73 ? 46   GLU A C   1 
ATOM   334  O O   . GLU A 1 46  ? -3.583  19.660 -0.213  0.88  32.75 ? 46   GLU A O   1 
ATOM   335  C CB  . GLU A 1 46  ? -2.407  21.295 -3.019  0.88  33.59 ? 46   GLU A CB  1 
ATOM   336  C CG  . GLU A 1 46  ? -0.943  21.102 -2.582  0.88  34.90 ? 46   GLU A CG  1 
ATOM   337  C CD  . GLU A 1 46  ? -0.008  20.785 -3.763  0.88  36.45 ? 46   GLU A CD  1 
ATOM   338  O OE1 . GLU A 1 46  ? -0.255  19.777 -4.474  0.88  36.91 ? 46   GLU A OE1 1 
ATOM   339  O OE2 . GLU A 1 46  ? 0.978   21.540 -3.967  0.88  36.79 ? 46   GLU A OE2 1 
ATOM   340  N N   . SER A 1 47  ? -4.448  19.179 -2.238  1.00  31.92 ? 47   SER A N   1 
ATOM   341  C CA  . SER A 1 47  ? -4.880  17.830 -1.862  1.00  31.05 ? 47   SER A CA  1 
ATOM   342  C C   . SER A 1 47  ? -3.746  16.804 -1.972  1.00  30.38 ? 47   SER A C   1 
ATOM   343  O O   . SER A 1 47  ? -3.211  16.568 -3.054  1.00  30.36 ? 47   SER A O   1 
ATOM   344  C CB  . SER A 1 47  ? -6.090  17.407 -2.702  1.00  31.00 ? 47   SER A CB  1 
ATOM   345  O OG  . SER A 1 47  ? -6.507  16.071 -2.372  1.00  31.00 ? 47   SER A OG  1 
ATOM   346  N N   . VAL A 1 48  ? -3.382  16.200 -0.846  1.00  29.60 ? 48   VAL A N   1 
ATOM   347  C CA  . VAL A 1 48  ? -2.317  15.197 -0.817  1.00  28.87 ? 48   VAL A CA  1 
ATOM   348  C C   . VAL A 1 48  ? -2.868  13.770 -0.766  1.00  28.78 ? 48   VAL A C   1 
ATOM   349  O O   . VAL A 1 48  ? -2.133  12.816 -0.498  1.00  28.66 ? 48   VAL A O   1 
ATOM   350  C CB  . VAL A 1 48  ? -1.329  15.425 0.355   1.00  28.70 ? 48   VAL A CB  1 
ATOM   351  C CG1 . VAL A 1 48  ? -0.540  16.712 0.144   1.00  28.42 ? 48   VAL A CG1 1 
ATOM   352  C CG2 . VAL A 1 48  ? -2.052  15.416 1.702   1.00  28.25 ? 48   VAL A CG2 1 
ATOM   353  N N   . ARG A 1 49  ? -4.161  13.637 -1.053  1.00  28.62 ? 49   ARG A N   1 
ATOM   354  C CA  . ARG A 1 49  ? -4.880  12.372 -0.929  1.00  28.38 ? 49   ARG A CA  1 
ATOM   355  C C   . ARG A 1 49  ? -4.318  11.280 -1.833  1.00  28.50 ? 49   ARG A C   1 
ATOM   356  O O   . ARG A 1 49  ? -4.382  11.384 -3.057  1.00  28.69 ? 49   ARG A O   1 
ATOM   357  C CB  . ARG A 1 49  ? -6.364  12.593 -1.215  1.00  28.12 ? 49   ARG A CB  1 
ATOM   358  C CG  . ARG A 1 49  ? -7.209  11.368 -0.996  1.00  28.01 ? 49   ARG A CG  1 
ATOM   359  C CD  . ARG A 1 49  ? -8.663  11.657 -1.271  1.00  28.20 ? 49   ARG A CD  1 
ATOM   360  N NE  . ARG A 1 49  ? -9.227  12.599 -0.306  1.00  28.70 ? 49   ARG A NE  1 
ATOM   361  C CZ  . ARG A 1 49  ? -9.672  12.263 0.903   1.00  28.57 ? 49   ARG A CZ  1 
ATOM   362  N NH1 . ARG A 1 49  ? -9.622  11.004 1.315   1.00  28.62 ? 49   ARG A NH1 1 
ATOM   363  N NH2 . ARG A 1 49  ? -10.176 13.188 1.705   1.00  28.54 ? 49   ARG A NH2 1 
ATOM   364  N N   . GLY A 1 50  ? -3.774  10.235 -1.217  1.00  28.64 ? 50   GLY A N   1 
ATOM   365  C CA  . GLY A 1 50  ? -3.188  9.118  -1.950  1.00  29.08 ? 50   GLY A CA  1 
ATOM   366  C C   . GLY A 1 50  ? -1.784  9.395  -2.469  1.00  29.35 ? 50   GLY A C   1 
ATOM   367  O O   . GLY A 1 50  ? -1.289  8.701  -3.365  1.00  29.38 ? 50   GLY A O   1 
ATOM   368  N N   . GLU A 1 51  ? -1.130  10.401 -1.898  1.00  29.60 ? 51   GLU A N   1 
ATOM   369  C CA  . GLU A 1 51  ? 0.175   10.829 -2.395  1.00  29.92 ? 51   GLU A CA  1 
ATOM   370  C C   . GLU A 1 51  ? 1.344   10.398 -1.513  1.00  29.84 ? 51   GLU A C   1 
ATOM   371  O O   . GLU A 1 51  ? 1.211   10.290 -0.288  1.00  30.09 ? 51   GLU A O   1 
ATOM   372  C CB  . GLU A 1 51  ? 0.203   12.343 -2.601  1.00  29.90 ? 51   GLU A CB  1 
ATOM   373  C CG  . GLU A 1 51  ? -0.829  12.832 -3.589  1.00  30.78 ? 51   GLU A CG  1 
ATOM   374  C CD  . GLU A 1 51  ? -0.441  14.137 -4.236  1.00  32.01 ? 51   GLU A CD  1 
ATOM   375  O OE1 . GLU A 1 51  ? -0.088  15.097 -3.526  1.00  33.45 ? 51   GLU A OE1 1 
ATOM   376  O OE2 . GLU A 1 51  ? -0.490  14.211 -5.473  1.00  32.85 ? 51   GLU A OE2 1 
ATOM   377  N N   . ASP A 1 52  ? 2.480   10.150 -2.161  1.00  29.50 ? 52   ASP A N   1 
ATOM   378  C CA  . ASP A 1 52  ? 3.741   9.907  -1.486  1.00  29.17 ? 52   ASP A CA  1 
ATOM   379  C C   . ASP A 1 52  ? 4.363   11.264 -1.170  1.00  28.67 ? 52   ASP A C   1 
ATOM   380  O O   . ASP A 1 52  ? 4.964   11.895 -2.031  1.00  28.46 ? 52   ASP A O   1 
ATOM   381  C CB  . ASP A 1 52  ? 4.661   9.078  -2.385  1.00  29.37 ? 52   ASP A CB  1 
ATOM   382  C CG  . ASP A 1 52  ? 5.836   8.478  -1.636  1.00  30.42 ? 52   ASP A CG  1 
ATOM   383  O OD1 . ASP A 1 52  ? 5.754   8.315  -0.395  1.00  31.52 ? 52   ASP A OD1 1 
ATOM   384  O OD2 . ASP A 1 52  ? 6.847   8.161  -2.301  1.00  31.72 ? 52   ASP A OD2 1 
ATOM   385  N N   . VAL A 1 53  ? 4.201   11.708 0.071   1.00  28.33 ? 53   VAL A N   1 
ATOM   386  C CA  . VAL A 1 53  ? 4.613   13.046 0.489   1.00  28.10 ? 53   VAL A CA  1 
ATOM   387  C C   . VAL A 1 53  ? 5.999   13.066 1.136   1.00  27.89 ? 53   VAL A C   1 
ATOM   388  O O   . VAL A 1 53  ? 6.429   12.079 1.749   1.00  27.95 ? 53   VAL A O   1 
ATOM   389  C CB  . VAL A 1 53  ? 3.571   13.656 1.446   1.00  28.11 ? 53   VAL A CB  1 
ATOM   390  C CG1 . VAL A 1 53  ? 4.105   14.916 2.120   1.00  28.39 ? 53   VAL A CG1 1 
ATOM   391  C CG2 . VAL A 1 53  ? 2.299   13.972 0.688   1.00  28.39 ? 53   VAL A CG2 1 
ATOM   392  N N   . TYR A 1 54  ? 6.698   14.190 0.979   1.00  27.52 ? 54   TYR A N   1 
ATOM   393  C CA  . TYR A 1 54  ? 8.020   14.370 1.565   1.00  27.27 ? 54   TYR A CA  1 
ATOM   394  C C   . TYR A 1 54  ? 8.125   15.770 2.173   1.00  27.24 ? 54   TYR A C   1 
ATOM   395  O O   . TYR A 1 54  ? 8.015   16.782 1.468   1.00  27.15 ? 54   TYR A O   1 
ATOM   396  C CB  . TYR A 1 54  ? 9.131   14.132 0.524   1.00  27.18 ? 54   TYR A CB  1 
ATOM   397  C CG  . TYR A 1 54  ? 9.179   12.723 -0.053  1.00  27.00 ? 54   TYR A CG  1 
ATOM   398  C CD1 . TYR A 1 54  ? 8.225   12.288 -0.977  1.00  26.82 ? 54   TYR A CD1 1 
ATOM   399  C CD2 . TYR A 1 54  ? 10.193  11.839 0.301   1.00  26.77 ? 54   TYR A CD2 1 
ATOM   400  C CE1 . TYR A 1 54  ? 8.263   11.007 -1.506  1.00  26.36 ? 54   TYR A CE1 1 
ATOM   401  C CE2 . TYR A 1 54  ? 10.245  10.550 -0.232  1.00  26.58 ? 54   TYR A CE2 1 
ATOM   402  C CZ  . TYR A 1 54  ? 9.274   10.141 -1.134  1.00  26.47 ? 54   TYR A CZ  1 
ATOM   403  O OH  . TYR A 1 54  ? 9.316   8.867  -1.662  1.00  25.85 ? 54   TYR A OH  1 
ATOM   404  N N   . ILE A 1 55  ? 8.312   15.824 3.489   1.00  27.14 ? 55   ILE A N   1 
ATOM   405  C CA  . ILE A 1 55  ? 8.524   17.096 4.157   1.00  27.08 ? 55   ILE A CA  1 
ATOM   406  C C   . ILE A 1 55  ? 10.008  17.254 4.486   1.00  27.26 ? 55   ILE A C   1 
ATOM   407  O O   . ILE A 1 55  ? 10.630  16.380 5.086   1.00  26.97 ? 55   ILE A O   1 
ATOM   408  C CB  . ILE A 1 55  ? 7.612   17.271 5.400   1.00  27.15 ? 55   ILE A CB  1 
ATOM   409  C CG1 . ILE A 1 55  ? 6.149   17.009 5.019   1.00  27.06 ? 55   ILE A CG1 1 
ATOM   410  C CG2 . ILE A 1 55  ? 7.728   18.702 5.963   1.00  26.71 ? 55   ILE A CG2 1 
ATOM   411  C CD1 . ILE A 1 55  ? 5.280   16.471 6.152   1.00  28.15 ? 55   ILE A CD1 1 
ATOM   412  N N   . VAL A 1 56  ? 10.570  18.372 4.046   1.00  27.81 ? 56   VAL A N   1 
ATOM   413  C CA  . VAL A 1 56  ? 11.966  18.695 4.301   1.00  28.48 ? 56   VAL A CA  1 
ATOM   414  C C   . VAL A 1 56  ? 12.055  19.707 5.438   1.00  28.88 ? 56   VAL A C   1 
ATOM   415  O O   . VAL A 1 56  ? 11.493  20.811 5.356   1.00  28.68 ? 56   VAL A O   1 
ATOM   416  C CB  . VAL A 1 56  ? 12.673  19.236 3.030   1.00  28.57 ? 56   VAL A CB  1 
ATOM   417  C CG1 . VAL A 1 56  ? 14.103  19.673 3.350   1.00  28.82 ? 56   VAL A CG1 1 
ATOM   418  C CG2 . VAL A 1 56  ? 12.678  18.183 1.920   1.00  28.58 ? 56   VAL A CG2 1 
ATOM   419  N N   . GLN A 1 57  ? 12.775  19.308 6.487   1.00  29.58 ? 57   GLN A N   1 
ATOM   420  C CA  . GLN A 1 57  ? 12.864  20.053 7.752   1.00  30.28 ? 57   GLN A CA  1 
ATOM   421  C C   . GLN A 1 57  ? 13.523  21.424 7.611   1.00  30.48 ? 57   GLN A C   1 
ATOM   422  O O   . GLN A 1 57  ? 14.572  21.568 6.969   1.00  30.69 ? 57   GLN A O   1 
ATOM   423  C CB  . GLN A 1 57  ? 13.563  19.201 8.824   1.00  30.47 ? 57   GLN A CB  1 
ATOM   424  C CG  . GLN A 1 57  ? 14.383  19.964 9.884   1.00  31.18 ? 57   GLN A CG  1 
ATOM   425  C CD  . GLN A 1 57  ? 15.878  20.028 9.551   1.00  31.82 ? 57   GLN A CD  1 
ATOM   426  O OE1 . GLN A 1 57  ? 16.729  19.899 10.437  1.00  31.57 ? 57   GLN A OE1 1 
ATOM   427  N NE2 . GLN A 1 57  ? 16.201  20.215 8.272   1.00  31.71 ? 57   GLN A NE2 1 
ATOM   428  N N   . SER A 1 58  ? 12.894  22.411 8.248   0.10  30.52 ? 58   SER A N   1 
ATOM   429  C CA  . SER A 1 58  ? 13.262  23.824 8.156   0.10  30.55 ? 58   SER A CA  1 
ATOM   430  C C   . SER A 1 58  ? 14.492  24.197 8.966   0.10  30.59 ? 58   SER A C   1 
ATOM   431  O O   . SER A 1 58  ? 15.089  23.357 9.643   0.10  30.62 ? 58   SER A O   1 
ATOM   432  C CB  . SER A 1 58  ? 12.096  24.683 8.656   0.10  30.53 ? 58   SER A CB  1 
ATOM   433  O OG  . SER A 1 58  ? 12.323  26.054 8.369   0.10  30.43 ? 58   SER A OG  1 
ATOM   434  N N   . GLY A 1 59  ? 14.848  25.480 8.915   0.010 30.63 ? 59   GLY A N   1 
ATOM   435  C CA  . GLY A 1 59  ? 15.998  25.983 9.658   0.010 30.68 ? 59   GLY A CA  1 
ATOM   436  C C   . GLY A 1 59  ? 15.811  27.365 10.260  0.010 30.70 ? 59   GLY A C   1 
ATOM   437  O O   . GLY A 1 59  ? 16.707  28.206 10.182  0.010 30.70 ? 59   GLY A O   1 
ATOM   438  N N   . CYS A 1 60  ? 14.651  27.606 10.866  0.010 30.72 ? 60   CYS A N   1 
ATOM   439  C CA  . CYS A 1 60  ? 14.388  28.884 11.526  0.010 30.73 ? 60   CYS A CA  1 
ATOM   440  C C   . CYS A 1 60  ? 15.274  29.205 12.724  0.010 30.72 ? 60   CYS A C   1 
ATOM   441  O O   . CYS A 1 60  ? 15.173  30.283 13.311  0.010 30.72 ? 60   CYS A O   1 
ATOM   442  C CB  . CYS A 1 60  ? 12.887  29.106 11.726  0.010 30.73 ? 60   CYS A CB  1 
ATOM   443  S SG  . CYS A 1 60  ? 12.160  30.282 10.564  0.010 30.74 ? 60   CYS A SG  1 
ATOM   444  N N   . GLY A 1 61  ? 16.145  28.268 13.080  0.010 30.70 ? 61   GLY A N   1 
ATOM   445  C CA  . GLY A 1 61  ? 17.092  28.495 14.162  0.010 30.66 ? 61   GLY A CA  1 
ATOM   446  C C   . GLY A 1 61  ? 16.248  28.612 15.415  0.010 30.62 ? 61   GLY A C   1 
ATOM   447  O O   . GLY A 1 61  ? 16.556  29.396 16.317  0.010 30.63 ? 61   GLY A O   1 
ATOM   448  N N   . GLU A 1 62  ? 15.163  27.843 15.453  0.10  30.57 ? 62   GLU A N   1 
ATOM   449  C CA  . GLU A 1 62  ? 14.378  27.681 16.681  0.10  30.50 ? 62   GLU A CA  1 
ATOM   450  C C   . GLU A 1 62  ? 13.876  26.252 16.603  0.10  30.50 ? 62   GLU A C   1 
ATOM   451  O O   . GLU A 1 62  ? 12.940  25.945 15.863  0.10  30.47 ? 62   GLU A O   1 
ATOM   452  C CB  . GLU A 1 62  ? 13.212  28.673 16.773  0.10  30.48 ? 62   GLU A CB  1 
ATOM   453  C CG  . GLU A 1 62  ? 12.992  29.236 18.185  0.10  30.30 ? 62   GLU A CG  1 
ATOM   454  C CD  . GLU A 1 62  ? 12.691  28.168 19.226  0.10  30.07 ? 62   GLU A CD  1 
ATOM   455  O OE1 . GLU A 1 62  ? 12.402  27.016 18.839  0.10  30.01 ? 62   GLU A OE1 1 
ATOM   456  O OE2 . GLU A 1 62  ? 12.744  28.488 20.432  0.10  30.00 ? 62   GLU A OE2 1 
ATOM   457  N N   . ILE A 1 63  ? 14.529  25.386 17.368  1.00  30.51 ? 63   ILE A N   1 
ATOM   458  C CA  . ILE A 1 63  ? 14.386  23.938 17.240  1.00  30.45 ? 63   ILE A CA  1 
ATOM   459  C C   . ILE A 1 63  ? 13.067  23.372 17.774  1.00  30.43 ? 63   ILE A C   1 
ATOM   460  O O   . ILE A 1 63  ? 12.581  22.347 17.288  1.00  30.78 ? 63   ILE A O   1 
ATOM   461  C CB  . ILE A 1 63  ? 15.565  23.200 17.904  1.00  30.24 ? 63   ILE A CB  1 
ATOM   462  C CG1 . ILE A 1 63  ? 15.634  21.759 17.394  1.00  30.85 ? 63   ILE A CG1 1 
ATOM   463  C CG2 . ILE A 1 63  ? 15.426  23.236 19.405  1.00  29.97 ? 63   ILE A CG2 1 
ATOM   464  C CD1 . ILE A 1 63  ? 16.929  21.036 17.707  1.00  32.40 ? 63   ILE A CD1 1 
ATOM   465  N N   . ASN A 1 64  ? 12.498  24.013 18.785  1.00  30.02 ? 64   ASN A N   1 
ATOM   466  C CA  . ASN A 1 64  ? 11.228  23.553 19.300  1.00  29.66 ? 64   ASN A CA  1 
ATOM   467  C C   . ASN A 1 64  ? 10.096  23.972 18.378  1.00  29.45 ? 64   ASN A C   1 
ATOM   468  O O   . ASN A 1 64  ? 9.258   23.146 18.012  1.00  29.53 ? 64   ASN A O   1 
ATOM   469  C CB  . ASN A 1 64  ? 11.032  24.030 20.729  1.00  29.60 ? 64   ASN A CB  1 
ATOM   470  C CG  . ASN A 1 64  ? 12.051  23.432 21.673  1.00  29.81 ? 64   ASN A CG  1 
ATOM   471  O OD1 . ASN A 1 64  ? 12.583  22.349 21.427  1.00  30.44 ? 64   ASN A OD1 1 
ATOM   472  N ND2 . ASN A 1 64  ? 12.332  24.134 22.758  1.00  30.37 ? 64   ASN A ND2 1 
ATOM   473  N N   . ASP A 1 65  ? 10.104  25.242 17.972  1.00  29.13 ? 65   ASP A N   1 
ATOM   474  C CA  . ASP A 1 65  ? 9.186   25.748 16.949  1.00  28.79 ? 65   ASP A CA  1 
ATOM   475  C C   . ASP A 1 65  ? 9.248   24.869 15.696  1.00  28.63 ? 65   ASP A C   1 
ATOM   476  O O   . ASP A 1 65  ? 8.208   24.399 15.201  1.00  28.82 ? 65   ASP A O   1 
ATOM   477  C CB  . ASP A 1 65  ? 9.517   27.200 16.571  1.00  28.69 ? 65   ASP A CB  1 
ATOM   478  C CG  . ASP A 1 65  ? 9.258   28.187 17.705  1.00  28.57 ? 65   ASP A CG  1 
ATOM   479  O OD1 . ASP A 1 65  ? 8.536   27.851 18.664  1.00  28.35 ? 65   ASP A OD1 1 
ATOM   480  O OD2 . ASP A 1 65  ? 9.774   29.321 17.626  1.00  28.77 ? 65   ASP A OD2 1 
ATOM   481  N N   . ASN A 1 66  ? 10.471  24.640 15.206  1.00  27.96 ? 66   ASN A N   1 
ATOM   482  C CA  . ASN A 1 66  ? 10.693  23.863 13.983  1.00  27.15 ? 66   ASN A CA  1 
ATOM   483  C C   . ASN A 1 66  ? 10.223  22.426 14.074  1.00  26.21 ? 66   ASN A C   1 
ATOM   484  O O   . ASN A 1 66  ? 9.595   21.929 13.139  1.00  26.17 ? 66   ASN A O   1 
ATOM   485  C CB  . ASN A 1 66  ? 12.157  23.929 13.533  1.00  27.45 ? 66   ASN A CB  1 
ATOM   486  C CG  . ASN A 1 66  ? 12.401  25.016 12.487  1.00  28.45 ? 66   ASN A CG  1 
ATOM   487  O OD1 . ASN A 1 66  ? 11.534  25.858 12.225  1.00  30.07 ? 66   ASN A OD1 1 
ATOM   488  N ND2 . ASN A 1 66  ? 13.582  24.995 11.880  1.00  28.52 ? 66   ASN A ND2 1 
ATOM   489  N N   . LEU A 1 67  ? 10.526  21.766 15.193  1.00  25.03 ? 67   LEU A N   1 
ATOM   490  C CA  . LEU A 1 67  ? 10.063  20.402 15.434  1.00  23.77 ? 67   LEU A CA  1 
ATOM   491  C C   . LEU A 1 67  ? 8.538   20.349 15.497  1.00  23.13 ? 67   LEU A C   1 
ATOM   492  O O   . LEU A 1 67  ? 7.923   19.454 14.907  1.00  22.89 ? 67   LEU A O   1 
ATOM   493  C CB  . LEU A 1 67  ? 10.689  19.811 16.708  1.00  23.66 ? 67   LEU A CB  1 
ATOM   494  C CG  . LEU A 1 67  ? 10.204  18.435 17.200  1.00  22.89 ? 67   LEU A CG  1 
ATOM   495  C CD1 . LEU A 1 67  ? 10.413  17.342 16.158  1.00  22.29 ? 67   LEU A CD1 1 
ATOM   496  C CD2 . LEU A 1 67  ? 10.876  18.055 18.499  1.00  21.31 ? 67   LEU A CD2 1 
ATOM   497  N N   . MET A 1 68  ? 7.932   21.300 16.204  0.70  22.33 ? 68   MET A N   1 
ATOM   498  C CA  . MET A 1 68  ? 6.475   21.337 16.284  0.70  21.71 ? 68   MET A CA  1 
ATOM   499  C C   . MET A 1 68  ? 5.838   21.520 14.910  0.70  21.32 ? 68   MET A C   1 
ATOM   500  O O   . MET A 1 68  ? 4.946   20.751 14.541  0.70  21.13 ? 68   MET A O   1 
ATOM   501  C CB  . MET A 1 68  ? 5.975   22.385 17.284  0.70  21.70 ? 68   MET A CB  1 
ATOM   502  C CG  . MET A 1 68  ? 5.795   21.834 18.699  0.70  21.23 ? 68   MET A CG  1 
ATOM   503  S SD  . MET A 1 68  ? 4.912   20.248 18.769  0.70  20.45 ? 68   MET A SD  1 
ATOM   504  C CE  . MET A 1 68  ? 3.252   20.704 18.261  0.70  19.77 ? 68   MET A CE  1 
ATOM   505  N N   . GLU A 1 69  ? 6.322   22.507 14.151  1.00  20.87 ? 69   GLU A N   1 
ATOM   506  C CA  . GLU A 1 69  ? 5.834   22.757 12.788  1.00  20.35 ? 69   GLU A CA  1 
ATOM   507  C C   . GLU A 1 69  ? 5.959   21.506 11.927  1.00  19.70 ? 69   GLU A C   1 
ATOM   508  O O   . GLU A 1 69  ? 5.064   21.185 11.159  1.00  19.47 ? 69   GLU A O   1 
ATOM   509  C CB  . GLU A 1 69  ? 6.575   23.928 12.131  1.00  20.58 ? 69   GLU A CB  1 
ATOM   510  C CG  . GLU A 1 69  ? 5.845   24.501 10.912  1.00  21.29 ? 69   GLU A CG  1 
ATOM   511  C CD  . GLU A 1 69  ? 6.732   25.363 10.025  1.00  22.38 ? 69   GLU A CD  1 
ATOM   512  O OE1 . GLU A 1 69  ? 7.758   24.847 9.516   1.00  22.78 ? 69   GLU A OE1 1 
ATOM   513  O OE2 . GLU A 1 69  ? 6.390   26.556 9.831   1.00  22.61 ? 69   GLU A OE2 1 
ATOM   514  N N   . LEU A 1 70  ? 7.073   20.802 12.076  1.00  19.15 ? 70   LEU A N   1 
ATOM   515  C CA  . LEU A 1 70  ? 7.288   19.543 11.393  1.00  18.77 ? 70   LEU A CA  1 
ATOM   516  C C   . LEU A 1 70  ? 6.237   18.491 11.768  1.00  18.91 ? 70   LEU A C   1 
ATOM   517  O O   . LEU A 1 70  ? 5.700   17.823 10.891  1.00  19.04 ? 70   LEU A O   1 
ATOM   518  C CB  . LEU A 1 70  ? 8.705   19.042 11.665  1.00  18.38 ? 70   LEU A CB  1 
ATOM   519  C CG  . LEU A 1 70  ? 9.181   17.738 11.025  1.00  18.05 ? 70   LEU A CG  1 
ATOM   520  C CD1 . LEU A 1 70  ? 9.030   17.708 9.504   1.00  16.99 ? 70   LEU A CD1 1 
ATOM   521  C CD2 . LEU A 1 70  ? 10.623  17.522 11.422  1.00  18.18 ? 70   LEU A CD2 1 
ATOM   522  N N   . LEU A 1 71  ? 5.928   18.355 13.056  1.00  18.97 ? 71   LEU A N   1 
ATOM   523  C CA  . LEU A 1 71  ? 4.934   17.371 13.498  1.00  18.87 ? 71   LEU A CA  1 
ATOM   524  C C   . LEU A 1 71  ? 3.516   17.741 13.062  1.00  18.81 ? 71   LEU A C   1 
ATOM   525  O O   . LEU A 1 71  ? 2.738   16.872 12.678  1.00  18.79 ? 71   LEU A O   1 
ATOM   526  C CB  . LEU A 1 71  ? 5.008   17.156 15.017  1.00  18.92 ? 71   LEU A CB  1 
ATOM   527  C CG  . LEU A 1 71  ? 6.338   16.601 15.550  1.00  18.64 ? 71   LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 71  ? 6.472   16.824 17.047  1.00  18.33 ? 71   LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 71  ? 6.516   15.127 15.216  1.00  18.16 ? 71   LEU A CD2 1 
ATOM   530  N N   . ILE A 1 72  ? 3.199   19.030 13.107  1.00  18.82 ? 72   ILE A N   1 
ATOM   531  C CA  . ILE A 1 72  ? 1.893   19.523 12.678  1.00  18.85 ? 72   ILE A CA  1 
ATOM   532  C C   . ILE A 1 72  ? 1.673   19.270 11.174  1.00  19.15 ? 72   ILE A C   1 
ATOM   533  O O   . ILE A 1 72  ? 0.546   19.032 10.739  1.00  19.25 ? 72   ILE A O   1 
ATOM   534  C CB  . ILE A 1 72  ? 1.706   21.015 13.066  1.00  18.68 ? 72   ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 72  ? 1.715   21.161 14.589  1.00  17.98 ? 72   ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 72  ? 0.417   21.573 12.498  1.00  18.15 ? 72   ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 72  ? 2.206   22.501 15.090  1.00  18.20 ? 72   ILE A CD1 1 
ATOM   538  N N   . MET A 1 73  ? 2.757   19.291 10.402  0.80  19.42 ? 73   MET A N   1 
ATOM   539  C CA  . MET A 1 73  ? 2.694   19.047 8.965   0.80  19.76 ? 73   MET A CA  1 
ATOM   540  C C   . MET A 1 73  ? 2.424   17.582 8.660   0.80  19.97 ? 73   MET A C   1 
ATOM   541  O O   . MET A 1 73  ? 1.459   17.260 7.967   0.80  19.90 ? 73   MET A O   1 
ATOM   542  C CB  . MET A 1 73  ? 3.985   19.494 8.294   0.80  19.88 ? 73   MET A CB  1 
ATOM   543  C CG  . MET A 1 73  ? 4.130   20.989 8.223   0.80  20.49 ? 73   MET A CG  1 
ATOM   544  S SD  . MET A 1 73  ? 5.028   21.490 6.764   0.80  22.01 ? 73   MET A SD  1 
ATOM   545  C CE  . MET A 1 73  ? 3.900   20.947 5.484   0.80  22.19 ? 73   MET A CE  1 
ATOM   546  N N   . ILE A 1 74  ? 3.282   16.707 9.181   1.00  20.32 ? 74   ILE A N   1 
ATOM   547  C CA  . ILE A 1 74  ? 3.087   15.268 9.100   1.00  20.64 ? 74   ILE A CA  1 
ATOM   548  C C   . ILE A 1 74  ? 1.642   14.925 9.461   1.00  20.86 ? 74   ILE A C   1 
ATOM   549  O O   . ILE A 1 74  ? 0.990   14.150 8.756   1.00  20.86 ? 74   ILE A O   1 
ATOM   550  C CB  . ILE A 1 74  ? 4.041   14.529 10.058  1.00  20.76 ? 74   ILE A CB  1 
ATOM   551  C CG1 . ILE A 1 74  ? 5.494   14.834 9.693   1.00  21.05 ? 74   ILE A CG1 1 
ATOM   552  C CG2 . ILE A 1 74  ? 3.788   13.012 10.025  1.00  21.06 ? 74   ILE A CG2 1 
ATOM   553  C CD1 . ILE A 1 74  ? 6.464   14.688 10.866  1.00  21.71 ? 74   ILE A CD1 1 
ATOM   554  N N   . ASN A 1 75  ? 1.145   15.515 10.548  1.00  21.02 ? 75   ASN A N   1 
ATOM   555  C CA  . ASN A 1 75  ? -0.220  15.272 10.994  1.00  21.29 ? 75   ASN A CA  1 
ATOM   556  C C   . ASN A 1 75  ? -1.275  15.660 9.950   1.00  21.67 ? 75   ASN A C   1 
ATOM   557  O O   . ASN A 1 75  ? -2.088  14.813 9.545   1.00  21.80 ? 75   ASN A O   1 
ATOM   558  C CB  . ASN A 1 75  ? -0.491  15.971 12.330  1.00  21.20 ? 75   ASN A CB  1 
ATOM   559  C CG  . ASN A 1 75  ? -1.782  15.513 12.976  1.00  20.72 ? 75   ASN A CG  1 
ATOM   560  O OD1 . ASN A 1 75  ? -2.692  16.312 13.197  1.00  19.49 ? 75   ASN A OD1 1 
ATOM   561  N ND2 . ASN A 1 75  ? -1.876  14.216 13.266  1.00  20.88 ? 75   ASN A ND2 1 
ATOM   562  N N   . ALA A 1 76  ? -1.260  16.924 9.518   1.00  22.02 ? 76   ALA A N   1 
ATOM   563  C CA  . ALA A 1 76  ? -2.214  17.415 8.521   1.00  22.48 ? 76   ALA A CA  1 
ATOM   564  C C   . ALA A 1 76  ? -2.190  16.516 7.301   1.00  23.14 ? 76   ALA A C   1 
ATOM   565  O O   . ALA A 1 76  ? -3.240  16.152 6.768   1.00  23.26 ? 76   ALA A O   1 
ATOM   566  C CB  . ALA A 1 76  ? -1.910  18.844 8.133   1.00  22.14 ? 76   ALA A CB  1 
ATOM   567  N N   . CYS A 1 77  ? -0.987  16.137 6.879   1.00  23.86 ? 77   CYS A N   1 
ATOM   568  C CA  . CYS A 1 77  ? -0.828  15.188 5.782   1.00  24.54 ? 77   CYS A CA  1 
ATOM   569  C C   . CYS A 1 77  ? -1.462  13.817 6.040   1.00  24.78 ? 77   CYS A C   1 
ATOM   570  O O   . CYS A 1 77  ? -2.112  13.268 5.153   1.00  24.94 ? 77   CYS A O   1 
ATOM   571  C CB  . CYS A 1 77  ? 0.643   15.062 5.386   1.00  24.50 ? 77   CYS A CB  1 
ATOM   572  S SG  . CYS A 1 77  ? 1.233   16.550 4.554   1.00  25.35 ? 77   CYS A SG  1 
ATOM   573  N N   . LYS A 1 78  ? -1.301  13.280 7.249   1.00  25.16 ? 78   LYS A N   1 
ATOM   574  C CA  . LYS A 1 78  ? -1.766  11.922 7.536   1.00  25.44 ? 78   LYS A CA  1 
ATOM   575  C C   . LYS A 1 78  ? -3.283  11.825 7.644   1.00  25.59 ? 78   LYS A C   1 
ATOM   576  O O   . LYS A 1 78  ? -3.870  10.785 7.315   1.00  25.72 ? 78   LYS A O   1 
ATOM   577  C CB  . LYS A 1 78  ? -1.095  11.350 8.791   1.00  25.44 ? 78   LYS A CB  1 
ATOM   578  C CG  . LYS A 1 78  ? -0.897  9.820  8.764   1.00  25.58 ? 78   LYS A CG  1 
ATOM   579  C CD  . LYS A 1 78  ? 0.069   9.408  7.651   1.00  25.62 ? 78   LYS A CD  1 
ATOM   580  C CE  . LYS A 1 78  ? 0.017   7.919  7.333   1.00  25.59 ? 78   LYS A CE  1 
ATOM   581  N NZ  . LYS A 1 78  ? 0.773   7.084  8.302   1.00  24.98 ? 78   LYS A NZ  1 
ATOM   582  N N   . ILE A 1 79  ? -3.917  12.904 8.090   1.00  25.64 ? 79   ILE A N   1 
ATOM   583  C CA  . ILE A 1 79  ? -5.377  12.914 8.196   1.00  25.79 ? 79   ILE A CA  1 
ATOM   584  C C   . ILE A 1 79  ? -6.052  13.465 6.936   1.00  25.86 ? 79   ILE A C   1 
ATOM   585  O O   . ILE A 1 79  ? -7.279  13.491 6.846   1.00  25.96 ? 79   ILE A O   1 
ATOM   586  C CB  . ILE A 1 79  ? -5.885  13.617 9.485   1.00  25.63 ? 79   ILE A CB  1 
ATOM   587  C CG1 . ILE A 1 79  ? -5.501  15.089 9.506   1.00  25.63 ? 79   ILE A CG1 1 
ATOM   588  C CG2 . ILE A 1 79  ? -5.324  12.929 10.715  1.00  25.83 ? 79   ILE A CG2 1 
ATOM   589  C CD1 . ILE A 1 79  ? -6.309  15.893 10.506  1.00  26.64 ? 79   ILE A CD1 1 
ATOM   590  N N   . ALA A 1 80  ? -5.239  13.897 5.971   1.00  25.84 ? 80   ALA A N   1 
ATOM   591  C CA  . ALA A 1 80  ? -5.744  14.294 4.658   1.00  25.82 ? 80   ALA A CA  1 
ATOM   592  C C   . ALA A 1 80  ? -5.503  13.164 3.655   1.00  25.76 ? 80   ALA A C   1 
ATOM   593  O O   . ALA A 1 80  ? -5.418  13.392 2.450   1.00  25.85 ? 80   ALA A O   1 
ATOM   594  C CB  . ALA A 1 80  ? -5.095  15.595 4.196   1.00  25.76 ? 80   ALA A CB  1 
ATOM   595  N N   . SER A 1 81  ? -5.381  11.948 4.188   1.00  25.64 ? 81   SER A N   1 
ATOM   596  C CA  . SER A 1 81  ? -5.284  10.701 3.413   1.00  25.67 ? 81   SER A CA  1 
ATOM   597  C C   . SER A 1 81  ? -4.098  10.549 2.465   1.00  25.78 ? 81   SER A C   1 
ATOM   598  O O   . SER A 1 81  ? -4.200  9.840  1.470   1.00  25.86 ? 81   SER A O   1 
ATOM   599  C CB  . SER A 1 81  ? -6.592  10.389 2.676   1.00  25.56 ? 81   SER A CB  1 
ATOM   600  O OG  . SER A 1 81  ? -7.428  9.556  3.460   1.00  25.63 ? 81   SER A OG  1 
ATOM   601  N N   . ALA A 1 82  ? -2.980  11.196 2.785   1.00  26.08 ? 82   ALA A N   1 
ATOM   602  C CA  . ALA A 1 82  ? -1.725  10.959 2.080   1.00  26.47 ? 82   ALA A CA  1 
ATOM   603  C C   . ALA A 1 82  ? -1.306  9.516  2.258   1.00  26.85 ? 82   ALA A C   1 
ATOM   604  O O   . ALA A 1 82  ? -1.390  8.981  3.358   1.00  26.95 ? 82   ALA A O   1 
ATOM   605  C CB  . ALA A 1 82  ? -0.649  11.873 2.604   1.00  26.46 ? 82   ALA A CB  1 
ATOM   606  N N   . SER A 1 83  ? -0.850  8.904  1.172   1.00  27.48 ? 83   SER A N   1 
ATOM   607  C CA  . SER A 1 83  ? -0.490  7.484  1.138   1.00  28.18 ? 83   SER A CA  1 
ATOM   608  C C   . SER A 1 83  ? 0.714   7.106  2.020   1.00  28.43 ? 83   SER A C   1 
ATOM   609  O O   . SER A 1 83  ? 0.852   5.951  2.437   1.00  28.43 ? 83   SER A O   1 
ATOM   610  C CB  . SER A 1 83  ? -0.223  7.071  -0.313  1.00  28.22 ? 83   SER A CB  1 
ATOM   611  O OG  . SER A 1 83  ? 0.403   5.803  -0.388  1.00  29.29 ? 83   SER A OG  1 
ATOM   612  N N   . ARG A 1 84  ? 1.575   8.085  2.290   1.00  28.77 ? 84   ARG A N   1 
ATOM   613  C CA  . ARG A 1 84  ? 2.837   7.865  2.985   1.00  29.20 ? 84   ARG A CA  1 
ATOM   614  C C   . ARG A 1 84  ? 3.479   9.223  3.254   1.00  29.09 ? 84   ARG A C   1 
ATOM   615  O O   . ARG A 1 84  ? 3.353   10.145 2.443   1.00  28.97 ? 84   ARG A O   1 
ATOM   616  C CB  . ARG A 1 84  ? 3.765   6.999  2.128   1.00  29.50 ? 84   ARG A CB  1 
ATOM   617  C CG  . ARG A 1 84  ? 4.686   6.065  2.916   1.00  31.36 ? 84   ARG A CG  1 
ATOM   618  C CD  . ARG A 1 84  ? 5.395   5.041  2.010   1.00  34.49 ? 84   ARG A CD  1 
ATOM   619  N NE  . ARG A 1 84  ? 6.220   5.695  0.988   1.00  37.31 ? 84   ARG A NE  1 
ATOM   620  C CZ  . ARG A 1 84  ? 7.102   5.080  0.198   1.00  37.67 ? 84   ARG A CZ  1 
ATOM   621  N NH1 . ARG A 1 84  ? 7.295   3.770  0.295   1.00  37.90 ? 84   ARG A NH1 1 
ATOM   622  N NH2 . ARG A 1 84  ? 7.797   5.782  -0.690  1.00  37.59 ? 84   ARG A NH2 1 
ATOM   623  N N   . VAL A 1 85  ? 4.151   9.349  4.399   1.00  29.08 ? 85   VAL A N   1 
ATOM   624  C CA  . VAL A 1 85  ? 4.798   10.609 4.787   1.00  29.04 ? 85   VAL A CA  1 
ATOM   625  C C   . VAL A 1 85  ? 6.246   10.402 5.218   1.00  29.00 ? 85   VAL A C   1 
ATOM   626  O O   . VAL A 1 85  ? 6.508   10.059 6.367   1.00  28.93 ? 85   VAL A O   1 
ATOM   627  C CB  . VAL A 1 85  ? 4.076   11.310 5.960   1.00  28.97 ? 85   VAL A CB  1 
ATOM   628  C CG1 . VAL A 1 85  ? 4.231   12.812 5.835   1.00  29.49 ? 85   VAL A CG1 1 
ATOM   629  C CG2 . VAL A 1 85  ? 2.612   10.943 6.012   1.00  28.82 ? 85   VAL A CG2 1 
ATOM   630  N N   . THR A 1 86  ? 7.184   10.612 4.303   1.00  29.05 ? 86   THR A N   1 
ATOM   631  C CA  . THR A 1 86  ? 8.589   10.571 4.665   1.00  29.26 ? 86   THR A CA  1 
ATOM   632  C C   . THR A 1 86  ? 9.040   11.954 5.103   1.00  29.43 ? 86   THR A C   1 
ATOM   633  O O   . THR A 1 86  ? 8.669   12.957 4.500   1.00  29.63 ? 86   THR A O   1 
ATOM   634  C CB  . THR A 1 86  ? 9.452   10.081 3.501   1.00  29.33 ? 86   THR A CB  1 
ATOM   635  O OG1 . THR A 1 86  ? 9.093   8.729  3.191   1.00  30.18 ? 86   THR A OG1 1 
ATOM   636  C CG2 . THR A 1 86  ? 10.943  10.141 3.849   1.00  29.07 ? 86   THR A CG2 1 
ATOM   637  N N   . THR A 1 87  ? 9.832   12.005 6.165   1.00  29.66 ? 87   THR A N   1 
ATOM   638  C CA  . THR A 1 87  ? 10.391  13.262 6.627   1.00  29.84 ? 87   THR A CA  1 
ATOM   639  C C   . THR A 1 87  ? 11.882  13.293 6.348   1.00  29.98 ? 87   THR A C   1 
ATOM   640  O O   . THR A 1 87  ? 12.638  12.416 6.780   1.00  29.73 ? 87   THR A O   1 
ATOM   641  C CB  . THR A 1 87  ? 10.168  13.471 8.126   1.00  29.95 ? 87   THR A CB  1 
ATOM   642  O OG1 . THR A 1 87  ? 10.824  12.422 8.847   1.00  29.85 ? 87   THR A OG1 1 
ATOM   643  C CG2 . THR A 1 87  ? 8.680   13.464 8.455   1.00  30.28 ? 87   THR A CG2 1 
ATOM   644  N N   . VAL A 1 88  ? 12.295  14.320 5.618   1.00  30.33 ? 88   VAL A N   1 
ATOM   645  C CA  . VAL A 1 88  ? 13.689  14.524 5.279   1.00  30.59 ? 88   VAL A CA  1 
ATOM   646  C C   . VAL A 1 88  ? 14.263  15.460 6.334   1.00  30.70 ? 88   VAL A C   1 
ATOM   647  O O   . VAL A 1 88  ? 14.072  16.676 6.256   1.00  30.90 ? 88   VAL A O   1 
ATOM   648  C CB  . VAL A 1 88  ? 13.827  15.106 3.836   1.00  30.57 ? 88   VAL A CB  1 
ATOM   649  C CG1 . VAL A 1 88  ? 15.271  15.431 3.492   1.00  30.63 ? 88   VAL A CG1 1 
ATOM   650  C CG2 . VAL A 1 88  ? 13.252  14.136 2.809   1.00  30.52 ? 88   VAL A CG2 1 
ATOM   651  N N   . ILE A 1 89  ? 14.921  14.886 7.341   1.00  30.80 ? 89   ILE A N   1 
ATOM   652  C CA  . ILE A 1 89  ? 15.508  15.677 8.421   1.00  30.95 ? 89   ILE A CA  1 
ATOM   653  C C   . ILE A 1 89  ? 17.018  15.494 8.429   1.00  31.05 ? 89   ILE A C   1 
ATOM   654  O O   . ILE A 1 89  ? 17.548  14.692 9.204   1.00  30.74 ? 89   ILE A O   1 
ATOM   655  C CB  . ILE A 1 89  ? 14.973  15.292 9.816   1.00  30.95 ? 89   ILE A CB  1 
ATOM   656  C CG1 . ILE A 1 89  ? 13.531  14.793 9.755   1.00  31.00 ? 89   ILE A CG1 1 
ATOM   657  C CG2 . ILE A 1 89  ? 15.084  16.474 10.766  1.00  31.40 ? 89   ILE A CG2 1 
ATOM   658  C CD1 . ILE A 1 89  ? 13.182  13.837 10.897  1.00  31.34 ? 89   ILE A CD1 1 
ATOM   659  N N   . PRO A 1 90  ? 17.724  16.262 7.588   1.00  31.32 ? 90   PRO A N   1 
ATOM   660  C CA  . PRO A 1 90  ? 19.155  16.069 7.427   1.00  31.80 ? 90   PRO A CA  1 
ATOM   661  C C   . PRO A 1 90  ? 19.869  16.108 8.776   1.00  32.33 ? 90   PRO A C   1 
ATOM   662  O O   . PRO A 1 90  ? 20.782  15.311 9.033   1.00  32.40 ? 90   PRO A O   1 
ATOM   663  C CB  . PRO A 1 90  ? 19.576  17.270 6.575   1.00  31.68 ? 90   PRO A CB  1 
ATOM   664  C CG  . PRO A 1 90  ? 18.340  17.754 5.941   1.00  31.52 ? 90   PRO A CG  1 
ATOM   665  C CD  . PRO A 1 90  ? 17.265  17.494 6.928   1.00  31.39 ? 90   PRO A CD  1 
ATOM   666  N N   . CYS A 1 91  ? 19.446  17.041 9.622   1.00  32.89 ? 91   CYS A N   1 
ATOM   667  C CA  . CYS A 1 91  ? 20.011  17.191 10.949  1.00  33.43 ? 91   CYS A CA  1 
ATOM   668  C C   . CYS A 1 91  ? 18.942  16.886 11.990  1.00  33.13 ? 91   CYS A C   1 
ATOM   669  O O   . CYS A 1 91  ? 18.060  17.707 12.258  1.00  33.08 ? 91   CYS A O   1 
ATOM   670  C CB  . CYS A 1 91  ? 20.566  18.597 11.138  1.00  33.56 ? 91   CYS A CB  1 
ATOM   671  S SG  . CYS A 1 91  ? 21.307  18.820 12.761  1.00  36.01 ? 91   CYS A SG  1 
ATOM   672  N N   . PHE A 1 92  ? 19.033  15.691 12.563  1.00  32.98 ? 92   PHE A N   1 
ATOM   673  C CA  . PHE A 1 92  ? 18.039  15.194 13.499  1.00  32.65 ? 92   PHE A CA  1 
ATOM   674  C C   . PHE A 1 92  ? 18.054  16.006 14.797  1.00  32.52 ? 92   PHE A C   1 
ATOM   675  O O   . PHE A 1 92  ? 19.104  16.152 15.426  1.00  32.53 ? 92   PHE A O   1 
ATOM   676  C CB  . PHE A 1 92  ? 18.270  13.706 13.776  1.00  32.46 ? 92   PHE A CB  1 
ATOM   677  C CG  . PHE A 1 92  ? 17.073  13.007 14.335  1.00  32.39 ? 92   PHE A CG  1 
ATOM   678  C CD1 . PHE A 1 92  ? 16.131  12.441 13.493  1.00  32.51 ? 92   PHE A CD1 1 
ATOM   679  C CD2 . PHE A 1 92  ? 16.882  12.917 15.708  1.00  32.81 ? 92   PHE A CD2 1 
ATOM   680  C CE1 . PHE A 1 92  ? 15.022  11.790 14.011  1.00  32.57 ? 92   PHE A CE1 1 
ATOM   681  C CE2 . PHE A 1 92  ? 15.775  12.268 16.236  1.00  32.64 ? 92   PHE A CE2 1 
ATOM   682  C CZ  . PHE A 1 92  ? 14.845  11.704 15.385  1.00  32.71 ? 92   PHE A CZ  1 
ATOM   683  N N   . PRO A 1 93  ? 16.885  16.555 15.188  1.00  32.39 ? 93   PRO A N   1 
ATOM   684  C CA  . PRO A 1 93  ? 16.721  17.358 16.413  1.00  32.20 ? 93   PRO A CA  1 
ATOM   685  C C   . PRO A 1 93  ? 16.955  16.562 17.698  1.00  32.11 ? 93   PRO A C   1 
ATOM   686  O O   . PRO A 1 93  ? 16.607  15.373 17.761  1.00  32.13 ? 93   PRO A O   1 
ATOM   687  C CB  . PRO A 1 93  ? 15.257  17.809 16.347  1.00  32.17 ? 93   PRO A CB  1 
ATOM   688  C CG  . PRO A 1 93  ? 14.593  16.842 15.422  1.00  32.28 ? 93   PRO A CG  1 
ATOM   689  C CD  . PRO A 1 93  ? 15.633  16.483 14.411  1.00  32.31 ? 93   PRO A CD  1 
ATOM   690  N N   . TYR A 1 94  ? 17.537  17.228 18.704  1.00  31.86 ? 94   TYR A N   1 
ATOM   691  C CA  . TYR A 1 94  ? 17.828  16.646 20.031  1.00  31.50 ? 94   TYR A CA  1 
ATOM   692  C C   . TYR A 1 94  ? 18.706  15.397 19.969  1.00  31.46 ? 94   TYR A C   1 
ATOM   693  O O   . TYR A 1 94  ? 18.592  14.509 20.816  1.00  31.71 ? 94   TYR A O   1 
ATOM   694  C CB  . TYR A 1 94  ? 16.530  16.337 20.790  1.00  31.36 ? 94   TYR A CB  1 
ATOM   695  C CG  . TYR A 1 94  ? 15.863  17.557 21.366  1.00  31.07 ? 94   TYR A CG  1 
ATOM   696  C CD1 . TYR A 1 94  ? 15.090  18.401 20.562  1.00  30.37 ? 94   TYR A CD1 1 
ATOM   697  C CD2 . TYR A 1 94  ? 16.007  17.878 22.716  1.00  30.77 ? 94   TYR A CD2 1 
ATOM   698  C CE1 . TYR A 1 94  ? 14.476  19.532 21.087  1.00  29.86 ? 94   TYR A CE1 1 
ATOM   699  C CE2 . TYR A 1 94  ? 15.396  19.009 23.252  1.00  30.39 ? 94   TYR A CE2 1 
ATOM   700  C CZ  . TYR A 1 94  ? 14.630  19.829 22.431  1.00  29.88 ? 94   TYR A CZ  1 
ATOM   701  O OH  . TYR A 1 94  ? 14.030  20.949 22.953  1.00  29.19 ? 94   TYR A OH  1 
ATOM   702  N N   . ALA A 1 95  ? 19.594  15.347 18.979  1.00  31.22 ? 95   ALA A N   1 
ATOM   703  C CA  . ALA A 1 95  ? 20.298  14.110 18.626  1.00  30.97 ? 95   ALA A CA  1 
ATOM   704  C C   . ALA A 1 95  ? 21.439  13.705 19.568  1.00  30.90 ? 95   ALA A C   1 
ATOM   705  O O   . ALA A 1 95  ? 21.839  12.536 19.581  1.00  30.81 ? 95   ALA A O   1 
ATOM   706  C CB  . ALA A 1 95  ? 20.789  14.174 17.181  1.00  30.81 ? 95   ALA A CB  1 
ATOM   707  N N   . ARG A 1 96  ? 21.958  14.651 20.351  0.20  30.88 ? 96   ARG A N   1 
ATOM   708  C CA  . ARG A 1 96  ? 22.993  14.331 21.341  0.20  30.87 ? 96   ARG A CA  1 
ATOM   709  C C   . ARG A 1 96  ? 22.391  13.792 22.635  0.20  31.01 ? 96   ARG A C   1 
ATOM   710  O O   . ARG A 1 96  ? 23.114  13.301 23.504  0.20  30.98 ? 96   ARG A O   1 
ATOM   711  C CB  . ARG A 1 96  ? 23.883  15.539 21.641  0.20  30.77 ? 96   ARG A CB  1 
ATOM   712  C CG  . ARG A 1 96  ? 24.479  16.191 20.411  0.20  30.53 ? 96   ARG A CG  1 
ATOM   713  C CD  . ARG A 1 96  ? 23.922  17.587 20.206  0.20  30.04 ? 96   ARG A CD  1 
ATOM   714  N NE  . ARG A 1 96  ? 24.765  18.596 20.842  0.20  29.64 ? 96   ARG A NE  1 
ATOM   715  C CZ  . ARG A 1 96  ? 24.533  19.903 20.796  0.20  29.44 ? 96   ARG A CZ  1 
ATOM   716  N NH1 . ARG A 1 96  ? 23.474  20.370 20.149  0.20  29.40 ? 96   ARG A NH1 1 
ATOM   717  N NH2 . ARG A 1 96  ? 25.359  20.745 21.401  0.20  29.26 ? 96   ARG A NH2 1 
ATOM   718  N N   . GLN A 1 97  ? 21.067  13.886 22.751  0.81  31.19 ? 97   GLN A N   1 
ATOM   719  C CA  . GLN A 1 97  ? 20.354  13.412 23.936  0.81  31.42 ? 97   GLN A CA  1 
ATOM   720  C C   . GLN A 1 97  ? 19.839  11.998 23.724  0.81  31.58 ? 97   GLN A C   1 
ATOM   721  O O   . GLN A 1 97  ? 18.626  11.741 23.744  0.81  31.33 ? 97   GLN A O   1 
ATOM   722  C CB  . GLN A 1 97  ? 19.244  14.386 24.332  0.81  31.35 ? 97   GLN A CB  1 
ATOM   723  C CG  . GLN A 1 97  ? 19.784  15.635 25.020  0.81  31.94 ? 97   GLN A CG  1 
ATOM   724  C CD  . GLN A 1 97  ? 18.809  16.797 25.013  0.81  32.85 ? 97   GLN A CD  1 
ATOM   725  O OE1 . GLN A 1 97  ? 17.763  16.747 25.665  0.81  33.06 ? 97   GLN A OE1 1 
ATOM   726  N NE2 . GLN A 1 97  ? 19.157  17.863 24.284  0.81  32.97 ? 97   GLN A NE2 1 
ATOM   727  N N   . ASP A 1 98  ? 20.802  11.090 23.542  1.00  31.94 ? 98   ASP A N   1 
ATOM   728  C CA  . ASP A 1 98  ? 20.551  9.693  23.187  1.00  32.21 ? 98   ASP A CA  1 
ATOM   729  C C   . ASP A 1 98  ? 20.998  8.704  24.262  1.00  32.21 ? 98   ASP A C   1 
ATOM   730  O O   . ASP A 1 98  ? 21.049  7.500  24.004  1.00  32.29 ? 98   ASP A O   1 
ATOM   731  C CB  . ASP A 1 98  ? 21.232  9.353  21.853  1.00  32.28 ? 98   ASP A CB  1 
ATOM   732  C CG  . ASP A 1 98  ? 22.744  9.523  21.900  1.00  32.73 ? 98   ASP A CG  1 
ATOM   733  O OD1 . ASP A 1 98  ? 23.289  9.833  22.984  1.00  33.64 ? 98   ASP A OD1 1 
ATOM   734  O OD2 . ASP A 1 98  ? 23.389  9.349  20.845  1.00  32.51 ? 98   ASP A OD2 1 
ATOM   735  N N   . LYS A 1 99  ? 21.326  9.216  25.451  1.00  32.29 ? 99   LYS A N   1 
ATOM   736  C CA  . LYS A 1 99  ? 21.663  8.381  26.615  1.00  32.41 ? 99   LYS A CA  1 
ATOM   737  C C   . LYS A 1 99  ? 21.632  9.179  27.924  1.00  32.25 ? 99   LYS A C   1 
ATOM   738  O O   . LYS A 1 99  ? 21.993  10.363 27.939  1.00  32.41 ? 99   LYS A O   1 
ATOM   739  C CB  . LYS A 1 99  ? 23.028  7.700  26.426  1.00  32.43 ? 99   LYS A CB  1 
ATOM   740  C CG  . LYS A 1 99  ? 24.217  8.646  26.308  1.00  33.15 ? 99   LYS A CG  1 
ATOM   741  C CD  . LYS A 1 99  ? 25.393  7.969  25.626  1.00  34.91 ? 99   LYS A CD  1 
ATOM   742  C CE  . LYS A 1 99  ? 26.721  8.325  26.296  1.00  36.31 ? 99   LYS A CE  1 
ATOM   743  N NZ  . LYS A 1 99  ? 27.100  9.764  26.112  1.00  37.39 ? 99   LYS A NZ  1 
ATOM   744  N N   . LYS A 1 100 ? 21.203  8.530  29.010  0.87  31.97 ? 100  LYS A N   1 
ATOM   745  C CA  . LYS A 1 100 ? 21.186  9.140  30.350  0.87  31.69 ? 100  LYS A CA  1 
ATOM   746  C C   . LYS A 1 100 ? 22.565  9.634  30.780  0.87  31.54 ? 100  LYS A C   1 
ATOM   747  O O   . LYS A 1 100 ? 22.695  10.714 31.349  0.87  31.57 ? 100  LYS A O   1 
ATOM   748  C CB  . LYS A 1 100 ? 20.665  8.148  31.394  0.87  31.76 ? 100  LYS A CB  1 
ATOM   749  C CG  . LYS A 1 100 ? 19.154  7.985  31.449  0.87  31.37 ? 100  LYS A CG  1 
ATOM   750  C CD  . LYS A 1 100 ? 18.798  6.776  32.293  0.87  30.97 ? 100  LYS A CD  1 
ATOM   751  C CE  . LYS A 1 100 ? 17.310  6.499  32.293  0.87  31.35 ? 100  LYS A CE  1 
ATOM   752  N NZ  . LYS A 1 100 ? 17.009  5.125  32.814  0.87  30.73 ? 100  LYS A NZ  1 
ATOM   753  N N   . ASP A 1 101 ? 23.592  8.838  30.500  0.10  31.35 ? 101  ASP A N   1 
ATOM   754  C CA  . ASP A 1 101 ? 24.956  9.217  30.838  0.10  31.13 ? 101  ASP A CA  1 
ATOM   755  C C   . ASP A 1 101 ? 25.131  9.319  32.349  0.10  30.98 ? 101  ASP A C   1 
ATOM   756  O O   . ASP A 1 101 ? 25.728  10.272 32.849  0.10  30.96 ? 101  ASP A O   1 
ATOM   757  C CB  . ASP A 1 101 ? 25.318  10.552 30.184  0.10  31.11 ? 101  ASP A CB  1 
ATOM   758  C CG  . ASP A 1 101 ? 26.773  10.926 30.388  0.10  31.02 ? 101  ASP A CG  1 
ATOM   759  O OD1 . ASP A 1 101 ? 27.649  10.069 30.147  0.10  30.82 ? 101  ASP A OD1 1 
ATOM   760  O OD2 . ASP A 1 101 ? 27.042  12.080 30.781  0.10  31.04 ? 101  ASP A OD2 1 
ATOM   761  N N   . LYS A 1 102 ? 24.596  8.341  33.073  0.10  30.77 ? 102  LYS A N   1 
ATOM   762  C CA  . LYS A 1 102 ? 24.729  8.296  34.532  0.10  30.58 ? 102  LYS A CA  1 
ATOM   763  C C   . LYS A 1 102 ? 23.914  9.340  35.291  0.10  30.41 ? 102  LYS A C   1 
ATOM   764  O O   . LYS A 1 102 ? 23.973  9.399  36.521  0.10  30.38 ? 102  LYS A O   1 
ATOM   765  C CB  . LYS A 1 102 ? 26.194  8.427  34.952  0.10  30.59 ? 102  LYS A CB  1 
ATOM   766  C CG  . LYS A 1 102 ? 27.044  7.200  34.697  0.10  30.55 ? 102  LYS A CG  1 
ATOM   767  C CD  . LYS A 1 102 ? 28.084  7.030  35.797  0.10  30.58 ? 102  LYS A CD  1 
ATOM   768  C CE  . LYS A 1 102 ? 28.867  8.313  36.039  0.10  30.65 ? 102  LYS A CE  1 
ATOM   769  N NZ  . LYS A 1 102 ? 29.780  8.189  37.211  0.10  30.60 ? 102  LYS A NZ  1 
ATOM   770  N N   . SER A 1 103 ? 23.182  10.173 34.560  1.00  30.23 ? 103  SER A N   1 
ATOM   771  C CA  . SER A 1 103 ? 22.287  11.163 35.160  1.00  29.95 ? 103  SER A CA  1 
ATOM   772  C C   . SER A 1 103 ? 20.853  10.642 35.151  1.00  29.65 ? 103  SER A C   1 
ATOM   773  O O   . SER A 1 103 ? 20.572  9.574  34.592  1.00  29.54 ? 103  SER A O   1 
ATOM   774  C CB  . SER A 1 103 ? 22.362  12.497 34.404  1.00  29.91 ? 103  SER A CB  1 
ATOM   775  O OG  . SER A 1 103 ? 23.680  13.015 34.406  1.00  30.28 ? 103  SER A OG  1 
ATOM   776  N N   . ARG A 1 104 ? 19.957  11.392 35.795  1.00  29.31 ? 104  ARG A N   1 
ATOM   777  C CA  . ARG A 1 104 ? 18.513  11.191 35.662  1.00  28.82 ? 104  ARG A CA  1 
ATOM   778  C C   . ARG A 1 104 ? 18.030  12.157 34.592  1.00  28.65 ? 104  ARG A C   1 
ATOM   779  O O   . ARG A 1 104 ? 17.265  13.080 34.855  1.00  28.77 ? 104  ARG A O   1 
ATOM   780  C CB  . ARG A 1 104 ? 17.792  11.437 36.988  1.00  28.63 ? 104  ARG A CB  1 
ATOM   781  C CG  . ARG A 1 104 ? 17.991  10.329 38.016  1.00  28.95 ? 104  ARG A CG  1 
ATOM   782  C CD  . ARG A 1 104 ? 17.324  10.656 39.352  1.00  29.07 ? 104  ARG A CD  1 
ATOM   783  N NE  . ARG A 1 104 ? 18.113  11.604 40.142  1.00  28.70 ? 104  ARG A NE  1 
ATOM   784  C CZ  . ARG A 1 104 ? 18.780  11.295 41.252  1.00  28.10 ? 104  ARG A CZ  1 
ATOM   785  N NH1 . ARG A 1 104 ? 18.751  10.054 41.733  1.00  27.88 ? 104  ARG A NH1 1 
ATOM   786  N NH2 . ARG A 1 104 ? 19.469  12.237 41.892  1.00  26.75 ? 104  ARG A NH2 1 
ATOM   787  N N   . ALA A 1 105 ? 18.511  11.936 33.375  1.00  28.56 ? 105  ALA A N   1 
ATOM   788  C CA  . ALA A 1 105 ? 18.254  12.823 32.254  1.00  28.30 ? 105  ALA A CA  1 
ATOM   789  C C   . ALA A 1 105 ? 17.351  12.150 31.216  1.00  28.16 ? 105  ALA A C   1 
ATOM   790  O O   . ALA A 1 105 ? 17.195  10.924 31.212  1.00  28.06 ? 105  ALA A O   1 
ATOM   791  C CB  . ALA A 1 105 ? 19.573  13.254 31.626  1.00  28.42 ? 105  ALA A CB  1 
ATOM   792  N N   . PRO A 1 106 ? 16.737  12.953 30.334  1.00  28.03 ? 106  PRO A N   1 
ATOM   793  C CA  . PRO A 1 106 ? 15.886  12.363 29.317  1.00  27.97 ? 106  PRO A CA  1 
ATOM   794  C C   . PRO A 1 106 ? 16.718  11.745 28.197  1.00  27.96 ? 106  PRO A C   1 
ATOM   795  O O   . PRO A 1 106 ? 17.857  12.154 27.978  1.00  28.05 ? 106  PRO A O   1 
ATOM   796  C CB  . PRO A 1 106 ? 15.105  13.567 28.789  1.00  27.82 ? 106  PRO A CB  1 
ATOM   797  C CG  . PRO A 1 106 ? 16.021  14.705 28.981  1.00  27.83 ? 106  PRO A CG  1 
ATOM   798  C CD  . PRO A 1 106 ? 16.739  14.426 30.259  1.00  27.97 ? 106  PRO A CD  1 
ATOM   799  N N   . ILE A 1 107 ? 16.166  10.744 27.523  1.00  27.93 ? 107  ILE A N   1 
ATOM   800  C CA  . ILE A 1 107 ? 16.693  10.334 26.231  1.00  27.86 ? 107  ILE A CA  1 
ATOM   801  C C   . ILE A 1 107 ? 15.756  11.004 25.233  1.00  27.65 ? 107  ILE A C   1 
ATOM   802  O O   . ILE A 1 107 ? 14.752  10.425 24.797  1.00  28.01 ? 107  ILE A O   1 
ATOM   803  C CB  . ILE A 1 107 ? 16.743  8.792  26.064  1.00  27.99 ? 107  ILE A CB  1 
ATOM   804  C CG1 . ILE A 1 107 ? 17.613  8.165  27.159  1.00  28.53 ? 107  ILE A CG1 1 
ATOM   805  C CG2 . ILE A 1 107 ? 17.302  8.415  24.701  1.00  27.88 ? 107  ILE A CG2 1 
ATOM   806  C CD1 . ILE A 1 107 ? 17.495  6.650  27.263  1.00  29.19 ? 107  ILE A CD1 1 
ATOM   807  N N   . SER A 1 108 ? 16.074  12.253 24.914  1.00  27.09 ? 108  SER A N   1 
ATOM   808  C CA  . SER A 1 108 ? 15.162  13.112 24.170  1.00  26.55 ? 108  SER A CA  1 
ATOM   809  C C   . SER A 1 108 ? 15.036  12.715 22.702  1.00  26.35 ? 108  SER A C   1 
ATOM   810  O O   . SER A 1 108 ? 13.959  12.831 22.124  1.00  26.46 ? 108  SER A O   1 
ATOM   811  C CB  . SER A 1 108 ? 15.570  14.585 24.301  1.00  26.67 ? 108  SER A CB  1 
ATOM   812  O OG  . SER A 1 108 ? 15.519  15.027 25.650  1.00  26.00 ? 108  SER A OG  1 
ATOM   813  N N   . ALA A 1 109 ? 16.127  12.247 22.100  1.00  25.93 ? 109  ALA A N   1 
ATOM   814  C CA  . ALA A 1 109 ? 16.085  11.771 20.720  1.00  25.65 ? 109  ALA A CA  1 
ATOM   815  C C   . ALA A 1 109 ? 15.203  10.530 20.567  1.00  25.44 ? 109  ALA A C   1 
ATOM   816  O O   . ALA A 1 109 ? 14.793  10.192 19.450  1.00  25.50 ? 109  ALA A O   1 
ATOM   817  C CB  . ALA A 1 109 ? 17.488  11.498 20.205  1.00  25.87 ? 109  ALA A CB  1 
ATOM   818  N N   . LYS A 1 110 ? 14.930  9.853  21.682  1.00  24.98 ? 110  LYS A N   1 
ATOM   819  C CA  . LYS A 1 110 ? 13.952  8.775  21.703  1.00  24.75 ? 110  LYS A CA  1 
ATOM   820  C C   . LYS A 1 110 ? 12.542  9.334  21.828  1.00  24.69 ? 110  LYS A C   1 
ATOM   821  O O   . LYS A 1 110 ? 11.612  8.864  21.170  1.00  24.50 ? 110  LYS A O   1 
ATOM   822  C CB  . LYS A 1 110 ? 14.234  7.798  22.839  1.00  24.61 ? 110  LYS A CB  1 
ATOM   823  C CG  . LYS A 1 110 ? 13.188  6.686  22.975  1.00  24.73 ? 110  LYS A CG  1 
ATOM   824  C CD  . LYS A 1 110 ? 12.980  5.908  21.664  1.00  23.43 ? 110  LYS A CD  1 
ATOM   825  C CE  . LYS A 1 110 ? 11.931  4.831  21.820  1.00  23.08 ? 110  LYS A CE  1 
ATOM   826  N NZ  . LYS A 1 110 ? 12.334  3.803  22.820  1.00  23.29 ? 110  LYS A NZ  1 
ATOM   827  N N   . LEU A 1 111 ? 12.398  10.332 22.690  1.00  24.84 ? 111  LEU A N   1 
ATOM   828  C CA  . LEU A 1 111 ? 11.160  11.070 22.815  1.00  25.02 ? 111  LEU A CA  1 
ATOM   829  C C   . LEU A 1 111 ? 10.795  11.662 21.450  1.00  24.99 ? 111  LEU A C   1 
ATOM   830  O O   . LEU A 1 111 ? 9.633   11.620 21.041  1.00  24.98 ? 111  LEU A O   1 
ATOM   831  C CB  . LEU A 1 111 ? 11.337  12.182 23.848  1.00  25.09 ? 111  LEU A CB  1 
ATOM   832  C CG  . LEU A 1 111 ? 10.151  12.812 24.570  1.00  25.46 ? 111  LEU A CG  1 
ATOM   833  C CD1 . LEU A 1 111 ? 10.565  14.208 24.999  1.00  25.94 ? 111  LEU A CD1 1 
ATOM   834  C CD2 . LEU A 1 111 ? 8.882   12.877 23.726  1.00  25.92 ? 111  LEU A CD2 1 
ATOM   835  N N   . VAL A 1 112 ? 11.796  12.195 20.747  1.00  24.88 ? 112  VAL A N   1 
ATOM   836  C CA  . VAL A 1 112 ? 11.578  12.830 19.448  1.00  24.74 ? 112  VAL A CA  1 
ATOM   837  C C   . VAL A 1 112 ? 11.215  11.789 18.399  1.00  24.60 ? 112  VAL A C   1 
ATOM   838  O O   . VAL A 1 112 ? 10.292  11.991 17.609  1.00  24.53 ? 112  VAL A O   1 
ATOM   839  C CB  . VAL A 1 112 ? 12.801  13.663 18.993  1.00  24.80 ? 112  VAL A CB  1 
ATOM   840  C CG1 . VAL A 1 112 ? 12.653  14.111 17.532  1.00  24.69 ? 112  VAL A CG1 1 
ATOM   841  C CG2 . VAL A 1 112 ? 12.987  14.870 19.905  1.00  24.64 ? 112  VAL A CG2 1 
ATOM   842  N N   . ALA A 1 113 ? 11.943  10.677 18.400  1.00  24.45 ? 113  ALA A N   1 
ATOM   843  C CA  . ALA A 1 113 ? 11.639  9.560  17.511  1.00  24.23 ? 113  ALA A CA  1 
ATOM   844  C C   . ALA A 1 113 ? 10.196  9.115  17.716  1.00  24.05 ? 113  ALA A C   1 
ATOM   845  O O   . ALA A 1 113 ? 9.450   8.937  16.751  1.00  24.26 ? 113  ALA A O   1 
ATOM   846  C CB  . ALA A 1 113 ? 12.594  8.395  17.760  1.00  24.14 ? 113  ALA A CB  1 
ATOM   847  N N   . ASN A 1 114 ? 9.811   8.960  18.981  1.00  23.64 ? 114  ASN A N   1 
ATOM   848  C CA  . ASN A 1 114 ? 8.461   8.564  19.349  1.00  23.20 ? 114  ASN A CA  1 
ATOM   849  C C   . ASN A 1 114 ? 7.389   9.544  18.898  1.00  23.26 ? 114  ASN A C   1 
ATOM   850  O O   . ASN A 1 114 ? 6.267   9.140  18.604  1.00  23.35 ? 114  ASN A O   1 
ATOM   851  C CB  . ASN A 1 114 ? 8.356   8.353  20.862  1.00  23.17 ? 114  ASN A CB  1 
ATOM   852  C CG  . ASN A 1 114 ? 8.936   7.025  21.310  1.00  21.92 ? 114  ASN A CG  1 
ATOM   853  O OD1 . ASN A 1 114 ? 9.213   6.162  20.495  1.00  21.00 ? 114  ASN A OD1 1 
ATOM   854  N ND2 . ASN A 1 114 ? 9.115   6.857  22.612  1.00  21.07 ? 114  ASN A ND2 1 
ATOM   855  N N   . MET A 1 115 ? 7.726   10.826 18.846  1.00  23.29 ? 115  MET A N   1 
ATOM   856  C CA  . MET A 1 115 ? 6.750   11.828 18.431  1.00  23.49 ? 115  MET A CA  1 
ATOM   857  C C   . MET A 1 115 ? 6.554   11.861 16.924  1.00  23.21 ? 115  MET A C   1 
ATOM   858  O O   . MET A 1 115 ? 5.419   11.856 16.452  1.00  23.32 ? 115  MET A O   1 
ATOM   859  C CB  . MET A 1 115 ? 7.122   13.201 18.955  1.00  23.72 ? 115  MET A CB  1 
ATOM   860  C CG  . MET A 1 115 ? 6.958   13.322 20.456  1.00  25.06 ? 115  MET A CG  1 
ATOM   861  S SD  . MET A 1 115 ? 7.448   14.946 21.029  1.00  27.49 ? 115  MET A SD  1 
ATOM   862  C CE  . MET A 1 115 ? 8.865   15.278 19.977  1.00  27.17 ? 115  MET A CE  1 
ATOM   863  N N   . LEU A 1 116 ? 7.654   11.897 16.174  1.00  22.86 ? 116  LEU A N   1 
ATOM   864  C CA  . LEU A 1 116 ? 7.614   11.706 14.725  1.00  22.32 ? 116  LEU A CA  1 
ATOM   865  C C   . LEU A 1 116 ? 6.816   10.446 14.364  1.00  21.98 ? 116  LEU A C   1 
ATOM   866  O O   . LEU A 1 116 ? 5.991   10.461 13.453  1.00  21.93 ? 116  LEU A O   1 
ATOM   867  C CB  . LEU A 1 116 ? 9.032   11.613 14.167  1.00  22.35 ? 116  LEU A CB  1 
ATOM   868  C CG  . LEU A 1 116 ? 9.891   12.871 14.268  1.00  22.42 ? 116  LEU A CG  1 
ATOM   869  C CD1 . LEU A 1 116 ? 11.358  12.511 14.441  1.00  22.91 ? 116  LEU A CD1 1 
ATOM   870  C CD2 . LEU A 1 116 ? 9.679   13.738 13.037  1.00  22.30 ? 116  LEU A CD2 1 
ATOM   871  N N   . SER A 1 117 ? 7.051   9.369  15.105  1.00  21.55 ? 117  SER A N   1 
ATOM   872  C CA  . SER A 1 117 ? 6.337   8.121  14.899  1.00  21.43 ? 117  SER A CA  1 
ATOM   873  C C   . SER A 1 117 ? 4.827   8.278  15.082  1.00  21.37 ? 117  SER A C   1 
ATOM   874  O O   . SER A 1 117 ? 4.059   7.972  14.169  1.00  21.50 ? 117  SER A O   1 
ATOM   875  C CB  . SER A 1 117 ? 6.880   7.039  15.833  1.00  21.50 ? 117  SER A CB  1 
ATOM   876  O OG  . SER A 1 117 ? 8.211   6.677  15.485  1.00  21.37 ? 117  SER A OG  1 
ATOM   877  N N   . VAL A 1 118 ? 4.413   8.767  16.250  1.00  21.22 ? 118  VAL A N   1 
ATOM   878  C CA  . VAL A 1 118 ? 2.991   8.912  16.586  1.00  21.08 ? 118  VAL A CA  1 
ATOM   879  C C   . VAL A 1 118 ? 2.320   10.038 15.795  1.00  21.06 ? 118  VAL A C   1 
ATOM   880  O O   . VAL A 1 118 ? 1.088   10.123 15.734  1.00  20.94 ? 118  VAL A O   1 
ATOM   881  C CB  . VAL A 1 118 ? 2.768   9.094  18.131  1.00  21.13 ? 118  VAL A CB  1 
ATOM   882  C CG1 . VAL A 1 118 ? 3.026   10.536 18.593  1.00  20.78 ? 118  VAL A CG1 1 
ATOM   883  C CG2 . VAL A 1 118 ? 1.370   8.646  18.537  1.00  21.25 ? 118  VAL A CG2 1 
ATOM   884  N N   . ALA A 1 119 ? 3.135   10.897 15.188  1.00  21.21 ? 119  ALA A N   1 
ATOM   885  C CA  . ALA A 1 119 ? 2.611   11.996 14.390  1.00  21.49 ? 119  ALA A CA  1 
ATOM   886  C C   . ALA A 1 119 ? 2.071   11.444 13.082  1.00  21.74 ? 119  ALA A C   1 
ATOM   887  O O   . ALA A 1 119 ? 1.201   12.046 12.452  1.00  21.71 ? 119  ALA A O   1 
ATOM   888  C CB  . ALA A 1 119 ? 3.686   13.027 14.126  1.00  21.37 ? 119  ALA A CB  1 
ATOM   889  N N   . GLY A 1 120 ? 2.595   10.286 12.691  1.00  22.10 ? 120  GLY A N   1 
ATOM   890  C CA  . GLY A 1 120 ? 2.171   9.605  11.476  1.00  22.39 ? 120  GLY A CA  1 
ATOM   891  C C   . GLY A 1 120 ? 3.256   9.486  10.420  1.00  22.54 ? 120  GLY A C   1 
ATOM   892  O O   . GLY A 1 120 ? 2.958   9.147  9.276   1.00  22.69 ? 120  GLY A O   1 
ATOM   893  N N   . ALA A 1 121 ? 4.507   9.762  10.789  1.00  22.53 ? 121  ALA A N   1 
ATOM   894  C CA  . ALA A 1 121 ? 5.622   9.632  9.852   1.00  22.49 ? 121  ALA A CA  1 
ATOM   895  C C   . ALA A 1 121 ? 5.889   8.155  9.575   1.00  22.51 ? 121  ALA A C   1 
ATOM   896  O O   . ALA A 1 121 ? 6.022   7.365  10.505  1.00  22.78 ? 121  ALA A O   1 
ATOM   897  C CB  . ALA A 1 121 ? 6.864   10.317 10.394  1.00  22.44 ? 121  ALA A CB  1 
ATOM   898  N N   . ASP A 1 122 ? 5.955   7.786  8.300   0.50  22.48 ? 122  ASP A N   1 
ATOM   899  C CA  . ASP A 1 122 ? 6.080   6.385  7.912   0.50  22.53 ? 122  ASP A CA  1 
ATOM   900  C C   . ASP A 1 122 ? 7.518   5.951  7.653   0.50  22.85 ? 122  ASP A C   1 
ATOM   901  O O   . ASP A 1 122 ? 7.827   4.756  7.682   0.50  22.90 ? 122  ASP A O   1 
ATOM   902  C CB  . ASP A 1 122 ? 5.231   6.108  6.675   0.50  22.35 ? 122  ASP A CB  1 
ATOM   903  C CG  . ASP A 1 122 ? 3.767   6.376  6.909   0.50  22.23 ? 122  ASP A CG  1 
ATOM   904  O OD1 . ASP A 1 122 ? 3.180   7.179  6.157   0.50  22.52 ? 122  ASP A OD1 1 
ATOM   905  O OD2 . ASP A 1 122 ? 3.203   5.789  7.854   0.50  21.94 ? 122  ASP A OD2 1 
ATOM   906  N N   . HIS A 1 123 ? 8.393   6.925  7.415   1.00  23.30 ? 123  HIS A N   1 
ATOM   907  C CA  . HIS A 1 123 ? 9.758   6.676  6.949   1.00  23.85 ? 123  HIS A CA  1 
ATOM   908  C C   . HIS A 1 123 ? 10.622  7.922  7.150   1.00  23.89 ? 123  HIS A C   1 
ATOM   909  O O   . HIS A 1 123 ? 10.160  9.043  6.929   1.00  23.75 ? 123  HIS A O   1 
ATOM   910  C CB  . HIS A 1 123 ? 9.720   6.278  5.468   1.00  24.17 ? 123  HIS A CB  1 
ATOM   911  C CG  . HIS A 1 123 ? 11.068  6.095  4.841   1.00  25.39 ? 123  HIS A CG  1 
ATOM   912  N ND1 . HIS A 1 123 ? 11.517  6.887  3.807   1.00  26.50 ? 123  HIS A ND1 1 
ATOM   913  C CD2 . HIS A 1 123 ? 12.059  5.206  5.092   1.00  26.02 ? 123  HIS A CD2 1 
ATOM   914  C CE1 . HIS A 1 123 ? 12.729  6.499  3.452   1.00  26.54 ? 123  HIS A CE1 1 
ATOM   915  N NE2 . HIS A 1 123 ? 13.080  5.479  4.216   1.00  26.24 ? 123  HIS A NE2 1 
ATOM   916  N N   . ILE A 1 124 ? 11.868  7.726  7.574   1.00  24.10 ? 124  ILE A N   1 
ATOM   917  C CA  . ILE A 1 124 ? 12.758  8.855  7.858   1.00  24.35 ? 124  ILE A CA  1 
ATOM   918  C C   . ILE A 1 124 ? 13.949  8.821  6.903   1.00  24.69 ? 124  ILE A C   1 
ATOM   919  O O   . ILE A 1 124 ? 14.394  7.743  6.505   1.00  24.72 ? 124  ILE A O   1 
ATOM   920  C CB  . ILE A 1 124 ? 13.255  8.881  9.362   1.00  24.17 ? 124  ILE A CB  1 
ATOM   921  C CG1 . ILE A 1 124 ? 12.114  8.614  10.354  1.00  23.73 ? 124  ILE A CG1 1 
ATOM   922  C CG2 . ILE A 1 124 ? 13.974  10.196 9.705   1.00  23.85 ? 124  ILE A CG2 1 
ATOM   923  C CD1 . ILE A 1 124 ? 11.144  9.762  10.569  1.00  23.15 ? 124  ILE A CD1 1 
ATOM   924  N N   . ILE A 1 125 ? 14.426  10.006 6.520   1.00  25.13 ? 125  ILE A N   1 
ATOM   925  C CA  . ILE A 1 125 ? 15.678  10.171 5.788   1.00  25.51 ? 125  ILE A CA  1 
ATOM   926  C C   . ILE A 1 125 ? 16.462  11.249 6.491   1.00  26.13 ? 125  ILE A C   1 
ATOM   927  O O   . ILE A 1 125 ? 15.995  12.386 6.634   1.00  26.03 ? 125  ILE A O   1 
ATOM   928  C CB  . ILE A 1 125 ? 15.472  10.606 4.321   1.00  25.41 ? 125  ILE A CB  1 
ATOM   929  C CG1 . ILE A 1 125 ? 14.938  9.438  3.486   1.00  25.63 ? 125  ILE A CG1 1 
ATOM   930  C CG2 . ILE A 1 125 ? 16.781  11.146 3.727   1.00  24.65 ? 125  ILE A CG2 1 
ATOM   931  C CD1 . ILE A 1 125 ? 14.579  9.819  2.047   1.00  26.38 ? 125  ILE A CD1 1 
ATOM   932  N N   . THR A 1 126 ? 17.656  10.884 6.937   1.00  27.08 ? 126  THR A N   1 
ATOM   933  C CA  . THR A 1 126 ? 18.530  11.813 7.632   1.00  27.95 ? 126  THR A CA  1 
ATOM   934  C C   . THR A 1 126 ? 19.976  11.625 7.203   1.00  28.66 ? 126  THR A C   1 
ATOM   935  O O   . THR A 1 126 ? 20.296  10.719 6.444   1.00  28.58 ? 126  THR A O   1 
ATOM   936  C CB  . THR A 1 126 ? 18.397  11.664 9.163   1.00  28.03 ? 126  THR A CB  1 
ATOM   937  O OG1 . THR A 1 126 ? 19.194  12.664 9.818   1.00  27.69 ? 126  THR A OG1 1 
ATOM   938  C CG2 . THR A 1 126 ? 18.816  10.256 9.612   1.00  27.90 ? 126  THR A CG2 1 
ATOM   939  N N   . MET A 1 127 ? 20.845  12.490 7.704   1.00  29.97 ? 127  MET A N   1 
ATOM   940  C CA  . MET A 1 127 ? 22.260  12.466 7.350   1.00  31.21 ? 127  MET A CA  1 
ATOM   941  C C   . MET A 1 127 ? 23.173  12.509 8.593   1.00  31.81 ? 127  MET A C   1 
ATOM   942  O O   . MET A 1 127 ? 22.924  13.264 9.537   1.00  31.86 ? 127  MET A O   1 
ATOM   943  C CB  . MET A 1 127 ? 22.564  13.612 6.384   1.00  31.26 ? 127  MET A CB  1 
ATOM   944  C CG  . MET A 1 127 ? 23.983  13.622 5.837   1.00  32.31 ? 127  MET A CG  1 
ATOM   945  S SD  . MET A 1 127 ? 24.219  14.813 4.487   1.00  33.77 ? 127  MET A SD  1 
ATOM   946  C CE  . MET A 1 127 ? 23.677  13.811 3.093   1.00  34.30 ? 127  MET A CE  1 
ATOM   947  N N   . ASP A 1 128 ? 24.221  11.686 8.569   0.95  32.66 ? 128  ASP A N   1 
ATOM   948  C CA  . ASP A 1 128 ? 25.197  11.531 9.669   0.95  33.78 ? 128  ASP A CA  1 
ATOM   949  C C   . ASP A 1 128 ? 24.640  11.654 11.090  0.95  34.29 ? 128  ASP A C   1 
ATOM   950  O O   . ASP A 1 128 ? 25.025  12.562 11.835  0.95  34.44 ? 128  ASP A O   1 
ATOM   951  C CB  . ASP A 1 128 ? 26.379  12.498 9.509   0.95  33.85 ? 128  ASP A CB  1 
ATOM   952  C CG  . ASP A 1 128 ? 27.119  12.308 8.204   0.95  34.87 ? 128  ASP A CG  1 
ATOM   953  O OD1 . ASP A 1 128 ? 26.885  13.125 7.296   0.95  36.14 ? 128  ASP A OD1 1 
ATOM   954  O OD2 . ASP A 1 128 ? 27.924  11.355 8.074   0.95  35.56 ? 128  ASP A OD2 1 
ATOM   955  N N   . LEU A 1 129 ? 23.741  10.745 11.461  1.00  34.90 ? 129  LEU A N   1 
ATOM   956  C CA  . LEU A 1 129 ? 23.181  10.718 12.812  1.00  35.43 ? 129  LEU A CA  1 
ATOM   957  C C   . LEU A 1 129 ? 24.283  10.763 13.854  1.00  35.69 ? 129  LEU A C   1 
ATOM   958  O O   . LEU A 1 129 ? 25.242  9.993  13.758  1.00  36.09 ? 129  LEU A O   1 
ATOM   959  C CB  . LEU A 1 129 ? 22.374  9.444  13.018  1.00  35.42 ? 129  LEU A CB  1 
ATOM   960  C CG  . LEU A 1 129 ? 21.051  9.377  12.278  1.00  35.83 ? 129  LEU A CG  1 
ATOM   961  C CD1 . LEU A 1 129 ? 20.472  7.990  12.463  1.00  36.37 ? 129  LEU A CD1 1 
ATOM   962  C CD2 . LEU A 1 129 ? 20.107  10.456 12.831  1.00  36.70 ? 129  LEU A CD2 1 
ATOM   963  N N   . HIS A 1 130 ? 24.156  11.652 14.839  0.60  35.73 ? 130  HIS A N   1 
ATOM   964  C CA  . HIS A 1 130 ? 25.158  11.754 15.900  0.60  35.80 ? 130  HIS A CA  1 
ATOM   965  C C   . HIS A 1 130 ? 25.512  10.373 16.451  0.60  35.71 ? 130  HIS A C   1 
ATOM   966  O O   . HIS A 1 130 ? 26.685  10.057 16.648  0.60  35.66 ? 130  HIS A O   1 
ATOM   967  C CB  . HIS A 1 130 ? 24.695  12.686 17.021  0.60  35.99 ? 130  HIS A CB  1 
ATOM   968  C CG  . HIS A 1 130 ? 25.642  12.750 18.179  0.60  36.21 ? 130  HIS A CG  1 
ATOM   969  N ND1 . HIS A 1 130 ? 26.670  13.665 18.250  0.60  36.25 ? 130  HIS A ND1 1 
ATOM   970  C CD2 . HIS A 1 130 ? 25.725  12.002 19.304  0.60  36.57 ? 130  HIS A CD2 1 
ATOM   971  C CE1 . HIS A 1 130 ? 27.342  13.480 19.371  0.60  36.86 ? 130  HIS A CE1 1 
ATOM   972  N NE2 . HIS A 1 130 ? 26.789  12.477 20.030  0.60  36.92 ? 130  HIS A NE2 1 
ATOM   973  N N   . ALA A 1 131 ? 24.489  9.555  16.687  1.00  35.63 ? 131  ALA A N   1 
ATOM   974  C CA  . ALA A 1 131 ? 24.684  8.146  17.014  1.00  35.60 ? 131  ALA A CA  1 
ATOM   975  C C   . ALA A 1 131 ? 23.993  7.253  15.990  1.00  35.57 ? 131  ALA A C   1 
ATOM   976  O O   . ALA A 1 131 ? 22.845  7.499  15.603  1.00  35.56 ? 131  ALA A O   1 
ATOM   977  C CB  . ALA A 1 131 ? 24.178  7.836  18.415  1.00  35.54 ? 131  ALA A CB  1 
ATOM   978  N N   . SER A 1 132 ? 24.703  6.214  15.562  1.00  35.45 ? 132  SER A N   1 
ATOM   979  C CA  . SER A 1 132 ? 24.158  5.224  14.648  1.00  35.32 ? 132  SER A CA  1 
ATOM   980  C C   . SER A 1 132 ? 22.939  4.501  15.241  1.00  35.11 ? 132  SER A C   1 
ATOM   981  O O   . SER A 1 132 ? 21.984  4.179  14.524  1.00  35.02 ? 132  SER A O   1 
ATOM   982  C CB  . SER A 1 132 ? 25.246  4.221  14.288  1.00  35.33 ? 132  SER A CB  1 
ATOM   983  O OG  . SER A 1 132 ? 24.807  3.376  13.248  1.00  36.16 ? 132  SER A OG  1 
ATOM   984  N N   . GLN A 1 133 ? 22.991  4.266  16.553  0.95  34.85 ? 133  GLN A N   1 
ATOM   985  C CA  . GLN A 1 133 ? 21.918  3.616  17.306  0.95  34.70 ? 133  GLN A CA  1 
ATOM   986  C C   . GLN A 1 133 ? 20.569  4.330  17.193  0.95  34.54 ? 133  GLN A C   1 
ATOM   987  O O   . GLN A 1 133 ? 19.535  3.662  17.078  0.95  34.77 ? 133  GLN A O   1 
ATOM   988  C CB  . GLN A 1 133 ? 22.300  3.480  18.779  0.95  34.76 ? 133  GLN A CB  1 
ATOM   989  C CG  . GLN A 1 133 ? 23.410  2.466  19.073  0.95  35.40 ? 133  GLN A CG  1 
ATOM   990  C CD  . GLN A 1 133 ? 24.837  2.995  18.819  0.95  35.78 ? 133  GLN A CD  1 
ATOM   991  O OE1 . GLN A 1 133 ? 25.051  4.183  18.542  0.95  35.84 ? 133  GLN A OE1 1 
ATOM   992  N NE2 . GLN A 1 133 ? 25.817  2.097  18.915  0.95  35.43 ? 133  GLN A NE2 1 
ATOM   993  N N   . ILE A 1 134 ? 20.574  5.672  17.239  1.00  34.09 ? 134  ILE A N   1 
ATOM   994  C CA  . ILE A 1 134 ? 19.379  6.476  16.935  1.00  33.58 ? 134  ILE A CA  1 
ATOM   995  C C   . ILE A 1 134 ? 19.127  6.169  15.442  1.00  33.12 ? 134  ILE A C   1 
ATOM   996  O O   . ILE A 1 134 ? 19.277  7.044  14.537  1.00  33.29 ? 134  ILE A O   1 
ATOM   997  C CB  . ILE A 1 134 ? 19.629  8.007  16.936  1.00  33.76 ? 134  ILE A CB  1 
ATOM   998  C CG1 . ILE A 1 134 ? 20.399  8.454  18.179  1.00  33.99 ? 134  ILE A CG1 1 
ATOM   999  C CG2 . ILE A 1 134 ? 18.288  8.823  16.839  1.00  33.76 ? 134  ILE A CG2 1 
ATOM   1000 C CD1 . ILE A 1 134 ? 20.956  9.863  17.996  1.00  35.38 ? 134  ILE A CD1 1 
ATOM   1001 N N   . GLN A 1 135 ? 18.838  4.852  15.234  1.00  32.34 ? 135  GLN A N   1 
ATOM   1002 C CA  . GLN A 1 135 ? 18.133  4.317  14.059  1.00  31.82 ? 135  GLN A CA  1 
ATOM   1003 C C   . GLN A 1 135 ? 17.227  3.251  14.684  1.00  30.96 ? 135  GLN A C   1 
ATOM   1004 O O   . GLN A 1 135 ? 16.194  2.887  14.122  1.00  30.75 ? 135  GLN A O   1 
ATOM   1005 C CB  . GLN A 1 135 ? 19.071  3.636  13.068  1.00  32.07 ? 135  GLN A CB  1 
ATOM   1006 C CG  . GLN A 1 135 ? 19.467  4.494  11.880  1.00  33.88 ? 135  GLN A CG  1 
ATOM   1007 C CD  . GLN A 1 135 ? 19.836  3.659  10.660  1.00  36.48 ? 135  GLN A CD  1 
ATOM   1008 O OE1 . GLN A 1 135 ? 19.068  2.789  10.227  1.00  37.20 ? 135  GLN A OE1 1 
ATOM   1009 N NE2 . GLN A 1 135 ? 21.014  3.920  10.099  1.00  37.61 ? 135  GLN A NE2 1 
ATOM   1010 N N   . GLY A 1 136 ? 17.633  2.750  15.847  1.00  30.20 ? 136  GLY A N   1 
ATOM   1011 C CA  . GLY A 1 136 ? 16.871  1.740  16.577  1.00  29.15 ? 136  GLY A CA  1 
ATOM   1012 C C   . GLY A 1 136 ? 15.857  2.359  17.518  1.00  28.45 ? 136  GLY A C   1 
ATOM   1013 O O   . GLY A 1 136 ? 15.141  1.652  18.231  1.00  28.43 ? 136  GLY A O   1 
ATOM   1014 N N   . PHE A 1 137 ? 15.803  3.688  17.514  1.00  27.67 ? 137  PHE A N   1 
ATOM   1015 C CA  . PHE A 1 137 ? 14.800  4.432  18.257  1.00  26.89 ? 137  PHE A CA  1 
ATOM   1016 C C   . PHE A 1 137 ? 13.441  4.295  17.557  1.00  26.48 ? 137  PHE A C   1 
ATOM   1017 O O   . PHE A 1 137 ? 12.388  4.329  18.208  1.00  26.31 ? 137  PHE A O   1 
ATOM   1018 C CB  . PHE A 1 137 ? 15.234  5.898  18.392  1.00  26.84 ? 137  PHE A CB  1 
ATOM   1019 C CG  . PHE A 1 137 ? 16.365  6.118  19.382  1.00  26.85 ? 137  PHE A CG  1 
ATOM   1020 C CD1 . PHE A 1 137 ? 16.759  7.411  19.730  1.00  26.98 ? 137  PHE A CD1 1 
ATOM   1021 C CD2 . PHE A 1 137 ? 17.017  5.041  19.984  1.00  26.39 ? 137  PHE A CD2 1 
ATOM   1022 C CE1 . PHE A 1 137 ? 17.797  7.622  20.639  1.00  26.28 ? 137  PHE A CE1 1 
ATOM   1023 C CE2 . PHE A 1 137 ? 18.047  5.244  20.892  1.00  25.75 ? 137  PHE A CE2 1 
ATOM   1024 C CZ  . PHE A 1 137 ? 18.439  6.533  21.218  1.00  26.10 ? 137  PHE A CZ  1 
ATOM   1025 N N   . PHE A 1 138 ? 13.476  4.098  16.238  1.00  25.88 ? 138  PHE A N   1 
ATOM   1026 C CA  . PHE A 1 138 ? 12.261  3.946  15.435  1.00  25.47 ? 138  PHE A CA  1 
ATOM   1027 C C   . PHE A 1 138 ? 11.897  2.494  15.196  1.00  25.72 ? 138  PHE A C   1 
ATOM   1028 O O   . PHE A 1 138 ? 12.757  1.612  15.235  1.00  25.86 ? 138  PHE A O   1 
ATOM   1029 C CB  . PHE A 1 138 ? 12.433  4.615  14.076  1.00  25.10 ? 138  PHE A CB  1 
ATOM   1030 C CG  . PHE A 1 138 ? 12.651  6.091  14.151  1.00  23.87 ? 138  PHE A CG  1 
ATOM   1031 C CD1 . PHE A 1 138 ? 13.928  6.606  14.362  1.00  22.65 ? 138  PHE A CD1 1 
ATOM   1032 C CD2 . PHE A 1 138 ? 11.581  6.973  14.008  1.00  22.33 ? 138  PHE A CD2 1 
ATOM   1033 C CE1 . PHE A 1 138 ? 14.135  7.977  14.427  1.00  22.11 ? 138  PHE A CE1 1 
ATOM   1034 C CE2 . PHE A 1 138 ? 11.778  8.344  14.073  1.00  21.50 ? 138  PHE A CE2 1 
ATOM   1035 C CZ  . PHE A 1 138 ? 13.056  8.848  14.277  1.00  21.49 ? 138  PHE A CZ  1 
ATOM   1036 N N   . ASP A 1 139 ? 10.612  2.260  14.943  1.00  25.92 ? 139  ASP A N   1 
ATOM   1037 C CA  . ASP A 1 139 ? 10.132  0.969  14.462  1.00  26.14 ? 139  ASP A CA  1 
ATOM   1038 C C   . ASP A 1 139 ? 9.739   1.105  12.987  1.00  26.26 ? 139  ASP A C   1 
ATOM   1039 O O   . ASP A 1 139 ? 9.549   0.108  12.288  1.00  26.40 ? 139  ASP A O   1 
ATOM   1040 C CB  . ASP A 1 139 ? 8.956   0.470  15.300  1.00  26.22 ? 139  ASP A CB  1 
ATOM   1041 C CG  . ASP A 1 139 ? 9.315   0.284  16.764  1.00  26.87 ? 139  ASP A CG  1 
ATOM   1042 O OD1 . ASP A 1 139 ? 10.089  -0.658 17.070  1.00  27.59 ? 139  ASP A OD1 1 
ATOM   1043 O OD2 . ASP A 1 139 ? 8.808   1.069  17.611  1.00  27.75 ? 139  ASP A OD2 1 
ATOM   1044 N N   . ILE A 1 140 ? 9.617   2.349  12.523  1.00  26.25 ? 140  ILE A N   1 
ATOM   1045 C CA  . ILE A 1 140 ? 9.502   2.649  11.090  1.00  26.28 ? 140  ILE A CA  1 
ATOM   1046 C C   . ILE A 1 140 ? 10.919  2.708  10.486  1.00  26.40 ? 140  ILE A C   1 
ATOM   1047 O O   . ILE A 1 140 ? 11.873  3.023  11.205  1.00  26.29 ? 140  ILE A O   1 
ATOM   1048 C CB  . ILE A 1 140 ? 8.761   3.998  10.847  1.00  26.36 ? 140  ILE A CB  1 
ATOM   1049 C CG1 . ILE A 1 140 ? 9.563   5.182  11.417  1.00  26.79 ? 140  ILE A CG1 1 
ATOM   1050 C CG2 . ILE A 1 140 ? 7.346   3.954  11.426  1.00  25.86 ? 140  ILE A CG2 1 
ATOM   1051 C CD1 . ILE A 1 140 ? 9.159   6.541  10.866  1.00  26.72 ? 140  ILE A CD1 1 
ATOM   1052 N N   . PRO A 1 141 ? 11.069  2.417  9.172   1.00  26.59 ? 141  PRO A N   1 
ATOM   1053 C CA  . PRO A 1 141 ? 12.434  2.306  8.642   1.00  26.74 ? 141  PRO A CA  1 
ATOM   1054 C C   . PRO A 1 141 ? 13.093  3.664  8.467   1.00  26.95 ? 141  PRO A C   1 
ATOM   1055 O O   . PRO A 1 141 ? 12.414  4.641  8.138   1.00  27.02 ? 141  PRO A O   1 
ATOM   1056 C CB  . PRO A 1 141 ? 12.241  1.635  7.271   1.00  26.77 ? 141  PRO A CB  1 
ATOM   1057 C CG  . PRO A 1 141 ? 10.766  1.305  7.171   1.00  26.80 ? 141  PRO A CG  1 
ATOM   1058 C CD  . PRO A 1 141 ? 10.066  2.228  8.109   1.00  26.56 ? 141  PRO A CD  1 
ATOM   1059 N N   . VAL A 1 142 ? 14.403  3.717  8.697   1.00  27.21 ? 142  VAL A N   1 
ATOM   1060 C CA  . VAL A 1 142 ? 15.173  4.956  8.561   1.00  27.27 ? 142  VAL A CA  1 
ATOM   1061 C C   . VAL A 1 142 ? 16.305  4.743  7.561   1.00  27.62 ? 142  VAL A C   1 
ATOM   1062 O O   . VAL A 1 142 ? 16.924  3.679  7.522   1.00  27.56 ? 142  VAL A O   1 
ATOM   1063 C CB  . VAL A 1 142 ? 15.736  5.448  9.942   1.00  27.13 ? 142  VAL A CB  1 
ATOM   1064 C CG1 . VAL A 1 142 ? 16.662  6.636  9.782   1.00  26.80 ? 142  VAL A CG1 1 
ATOM   1065 C CG2 . VAL A 1 142 ? 14.619  5.817  10.886  1.00  26.45 ? 142  VAL A CG2 1 
ATOM   1066 N N   . ASP A 1 143 ? 16.555  5.757  6.745   0.93  28.24 ? 143  ASP A N   1 
ATOM   1067 C CA  . ASP A 1 143 ? 17.692  5.751  5.838   0.93  29.05 ? 143  ASP A CA  1 
ATOM   1068 C C   . ASP A 1 143 ? 18.664  6.860  6.203   0.93  29.78 ? 143  ASP A C   1 
ATOM   1069 O O   . ASP A 1 143 ? 18.365  8.042  6.043   0.93  29.85 ? 143  ASP A O   1 
ATOM   1070 C CB  . ASP A 1 143 ? 17.225  5.886  4.388   0.93  28.87 ? 143  ASP A CB  1 
ATOM   1071 C CG  . ASP A 1 143 ? 16.572  4.620  3.865   0.93  28.66 ? 143  ASP A CG  1 
ATOM   1072 O OD1 . ASP A 1 143 ? 16.696  3.562  4.517   0.93  28.71 ? 143  ASP A OD1 1 
ATOM   1073 O OD2 . ASP A 1 143 ? 15.935  4.674  2.795   0.93  28.31 ? 143  ASP A OD2 1 
ATOM   1074 N N   . ASN A 1 144 ? 19.828  6.471  6.707   1.00  30.89 ? 144  ASN A N   1 
ATOM   1075 C CA  . ASN A 1 144 ? 20.804  7.438  7.183   1.00  32.13 ? 144  ASN A CA  1 
ATOM   1076 C C   . ASN A 1 144 ? 21.926  7.652  6.193   1.00  32.78 ? 144  ASN A C   1 
ATOM   1077 O O   . ASN A 1 144 ? 22.746  6.760  5.970   1.00  32.86 ? 144  ASN A O   1 
ATOM   1078 C CB  . ASN A 1 144 ? 21.371  7.008  8.539   1.00  32.37 ? 144  ASN A CB  1 
ATOM   1079 C CG  . ASN A 1 144 ? 22.365  8.008  9.105   1.00  32.72 ? 144  ASN A CG  1 
ATOM   1080 O OD1 . ASN A 1 144 ? 22.415  9.171  8.687   1.00  32.62 ? 144  ASN A OD1 1 
ATOM   1081 N ND2 . ASN A 1 144 ? 23.161  7.557  10.073  1.00  33.40 ? 144  ASN A ND2 1 
ATOM   1082 N N   . LEU A 1 145 ? 21.955  8.847  5.614   1.00  33.80 ? 145  LEU A N   1 
ATOM   1083 C CA  . LEU A 1 145 ? 22.973  9.214  4.635   1.00  34.87 ? 145  LEU A CA  1 
ATOM   1084 C C   . LEU A 1 145 ? 24.266  9.665  5.316   1.00  35.71 ? 145  LEU A C   1 
ATOM   1085 O O   . LEU A 1 145 ? 24.261  10.087 6.479   1.00  35.82 ? 145  LEU A O   1 
ATOM   1086 C CB  . LEU A 1 145 ? 22.446  10.291 3.678   1.00  34.77 ? 145  LEU A CB  1 
ATOM   1087 C CG  . LEU A 1 145 ? 21.166  9.922  2.924   1.00  34.59 ? 145  LEU A CG  1 
ATOM   1088 C CD1 . LEU A 1 145 ? 20.736  11.046 1.980   1.00  34.72 ? 145  LEU A CD1 1 
ATOM   1089 C CD2 . LEU A 1 145 ? 21.373  8.625  2.163   1.00  33.88 ? 145  LEU A CD2 1 
ATOM   1090 N N   . TYR A 1 146 ? 25.371  9.559  4.584   1.00  36.52 ? 146  TYR A N   1 
ATOM   1091 C CA  . TYR A 1 146 ? 26.685  9.875  5.120   1.00  37.21 ? 146  TYR A CA  1 
ATOM   1092 C C   . TYR A 1 146 ? 27.275  11.037 4.337   1.00  37.52 ? 146  TYR A C   1 
ATOM   1093 O O   . TYR A 1 146 ? 27.149  11.080 3.112   1.00  37.82 ? 146  TYR A O   1 
ATOM   1094 C CB  . TYR A 1 146 ? 27.595  8.644  5.020   1.00  37.38 ? 146  TYR A CB  1 
ATOM   1095 C CG  . TYR A 1 146 ? 27.004  7.388  5.636   1.00  38.29 ? 146  TYR A CG  1 
ATOM   1096 C CD1 . TYR A 1 146 ? 26.131  6.575  4.907   1.00  38.98 ? 146  TYR A CD1 1 
ATOM   1097 C CD2 . TYR A 1 146 ? 27.315  7.010  6.946   1.00  39.04 ? 146  TYR A CD2 1 
ATOM   1098 C CE1 . TYR A 1 146 ? 25.576  5.421  5.466   1.00  39.27 ? 146  TYR A CE1 1 
ATOM   1099 C CE2 . TYR A 1 146 ? 26.764  5.853  7.515   1.00  39.43 ? 146  TYR A CE2 1 
ATOM   1100 C CZ  . TYR A 1 146 ? 25.891  5.066  6.766   1.00  39.55 ? 146  TYR A CZ  1 
ATOM   1101 O OH  . TYR A 1 146 ? 25.336  3.923  7.303   1.00  39.35 ? 146  TYR A OH  1 
ATOM   1102 N N   . ALA A 1 147 ? 27.901  11.983 5.034   1.00  37.75 ? 147  ALA A N   1 
ATOM   1103 C CA  . ALA A 1 147 ? 28.668  13.026 4.355   1.00  38.07 ? 147  ALA A CA  1 
ATOM   1104 C C   . ALA A 1 147 ? 30.066  12.508 4.033   1.00  38.38 ? 147  ALA A C   1 
ATOM   1105 O O   . ALA A 1 147 ? 30.775  13.084 3.205   1.00  38.36 ? 147  ALA A O   1 
ATOM   1106 C CB  . ALA A 1 147 ? 28.745  14.278 5.193   1.00  38.09 ? 147  ALA A CB  1 
ATOM   1107 N N   . GLU A 1 148 ? 30.434  11.404 4.683   1.00  38.80 ? 148  GLU A N   1 
ATOM   1108 C CA  . GLU A 1 148 ? 31.721  10.718 4.490   1.00  39.31 ? 148  GLU A CA  1 
ATOM   1109 C C   . GLU A 1 148 ? 32.350  10.753 3.076   1.00  39.19 ? 148  GLU A C   1 
ATOM   1110 O O   . GLU A 1 148 ? 33.556  11.046 2.951   1.00  39.27 ? 148  GLU A O   1 
ATOM   1111 C CB  . GLU A 1 148 ? 31.651  9.272  5.028   1.00  39.53 ? 148  GLU A CB  1 
ATOM   1112 C CG  . GLU A 1 148 ? 32.979  8.491  4.941   1.00  41.20 ? 148  GLU A CG  1 
ATOM   1113 C CD  . GLU A 1 148 ? 33.224  7.579  6.139   1.00  43.19 ? 148  GLU A CD  1 
ATOM   1114 O OE1 . GLU A 1 148 ? 32.235  7.175  6.797   1.00  44.30 ? 148  GLU A OE1 1 
ATOM   1115 O OE2 . GLU A 1 148 ? 34.411  7.271  6.422   1.00  43.16 ? 148  GLU A OE2 1 
ATOM   1116 N N   . PRO A 1 149 ? 31.549  10.443 2.011   1.00  39.17 ? 149  PRO A N   1 
ATOM   1117 C CA  . PRO A 1 149 ? 32.164  10.466 0.666   1.00  39.29 ? 149  PRO A CA  1 
ATOM   1118 C C   . PRO A 1 149 ? 32.417  11.873 0.115   1.00  39.49 ? 149  PRO A C   1 
ATOM   1119 O O   . PRO A 1 149 ? 33.394  12.099 -0.601  1.00  39.45 ? 149  PRO A O   1 
ATOM   1120 C CB  . PRO A 1 149 ? 31.106  9.766  -0.205  1.00  39.14 ? 149  PRO A CB  1 
ATOM   1121 C CG  . PRO A 1 149 ? 30.309  8.980  0.722   1.00  38.98 ? 149  PRO A CG  1 
ATOM   1122 C CD  . PRO A 1 149 ? 30.222  9.792  1.972   1.00  39.01 ? 149  PRO A CD  1 
ATOM   1123 N N   . ALA A 1 150 ? 31.522  12.800 0.444   1.00  39.74 ? 150  ALA A N   1 
ATOM   1124 C CA  . ALA A 1 150 ? 31.667  14.196 0.049   1.00  39.93 ? 150  ALA A CA  1 
ATOM   1125 C C   . ALA A 1 150 ? 32.796  14.867 0.824   1.00  40.20 ? 150  ALA A C   1 
ATOM   1126 O O   . ALA A 1 150 ? 33.490  15.737 0.289   1.00  40.31 ? 150  ALA A O   1 
ATOM   1127 C CB  . ALA A 1 150 ? 30.368  14.934 0.265   1.00  39.95 ? 150  ALA A CB  1 
ATOM   1128 N N   . VAL A 1 151 ? 32.970  14.464 2.085   1.00  40.43 ? 151  VAL A N   1 
ATOM   1129 C CA  . VAL A 1 151 ? 34.067  14.969 2.925   1.00  40.59 ? 151  VAL A CA  1 
ATOM   1130 C C   . VAL A 1 151 ? 35.417  14.561 2.339   1.00  40.78 ? 151  VAL A C   1 
ATOM   1131 O O   . VAL A 1 151 ? 36.298  15.401 2.145   1.00  40.64 ? 151  VAL A O   1 
ATOM   1132 C CB  . VAL A 1 151 ? 33.969  14.465 4.393   1.00  40.48 ? 151  VAL A CB  1 
ATOM   1133 C CG1 . VAL A 1 151 ? 35.179  14.927 5.199   1.00  40.29 ? 151  VAL A CG1 1 
ATOM   1134 C CG2 . VAL A 1 151 ? 32.681  14.956 5.053   1.00  40.48 ? 151  VAL A CG2 1 
ATOM   1135 N N   . LEU A 1 152 ? 35.554  13.267 2.053   1.00  41.15 ? 152  LEU A N   1 
ATOM   1136 C CA  . LEU A 1 152 ? 36.769  12.709 1.468   1.00  41.55 ? 152  LEU A CA  1 
ATOM   1137 C C   . LEU A 1 152 ? 37.159  13.406 0.178   1.00  41.85 ? 152  LEU A C   1 
ATOM   1138 O O   . LEU A 1 152 ? 38.278  13.920 0.064   1.00  41.80 ? 152  LEU A O   1 
ATOM   1139 C CB  . LEU A 1 152 ? 36.592  11.214 1.210   1.00  41.51 ? 152  LEU A CB  1 
ATOM   1140 C CG  . LEU A 1 152 ? 37.419  10.219 2.028   1.00  41.51 ? 152  LEU A CG  1 
ATOM   1141 C CD1 . LEU A 1 152 ? 37.500  10.569 3.522   1.00  41.32 ? 152  LEU A CD1 1 
ATOM   1142 C CD2 . LEU A 1 152 ? 36.841  8.830  1.819   1.00  41.45 ? 152  LEU A CD2 1 
ATOM   1143 N N   . LYS A 1 153 ? 36.227  13.410 -0.781  0.60  42.28 ? 153  LYS A N   1 
ATOM   1144 C CA  . LYS A 1 153 ? 36.415  14.064 -2.074  0.60  42.71 ? 153  LYS A CA  1 
ATOM   1145 C C   . LYS A 1 153 ? 36.963  15.472 -1.903  0.60  43.08 ? 153  LYS A C   1 
ATOM   1146 O O   . LYS A 1 153 ? 37.974  15.823 -2.516  0.60  43.02 ? 153  LYS A O   1 
ATOM   1147 C CB  . LYS A 1 153 ? 35.095  14.097 -2.852  0.60  42.68 ? 153  LYS A CB  1 
ATOM   1148 C CG  . LYS A 1 153 ? 35.223  14.577 -4.286  0.60  42.50 ? 153  LYS A CG  1 
ATOM   1149 C CD  . LYS A 1 153 ? 33.925  14.366 -5.049  0.60  42.59 ? 153  LYS A CD  1 
ATOM   1150 C CE  . LYS A 1 153 ? 34.123  14.585 -6.546  0.60  43.17 ? 153  LYS A CE  1 
ATOM   1151 N NZ  . LYS A 1 153 ? 34.433  16.034 -6.911  0.60  43.72 ? 153  LYS A NZ  1 
ATOM   1152 N N   . TRP A 1 154 ? 36.299  16.266 -1.062  1.00  43.68 ? 154  TRP A N   1 
ATOM   1153 C CA  . TRP A 1 154 ? 36.749  17.625 -0.767  1.00  44.49 ? 154  TRP A CA  1 
ATOM   1154 C C   . TRP A 1 154 ? 38.195  17.641 -0.255  1.00  44.96 ? 154  TRP A C   1 
ATOM   1155 O O   . TRP A 1 154 ? 39.047  18.342 -0.813  1.00  44.94 ? 154  TRP A O   1 
ATOM   1156 C CB  . TRP A 1 154 ? 35.820  18.315 0.240   1.00  44.49 ? 154  TRP A CB  1 
ATOM   1157 C CG  . TRP A 1 154 ? 36.097  19.786 0.377   1.00  44.88 ? 154  TRP A CG  1 
ATOM   1158 C CD1 . TRP A 1 154 ? 35.438  20.805 -0.250  1.00  45.13 ? 154  TRP A CD1 1 
ATOM   1159 C CD2 . TRP A 1 154 ? 37.113  20.401 1.181   1.00  45.64 ? 154  TRP A CD2 1 
ATOM   1160 N NE1 . TRP A 1 154 ? 35.974  22.016 0.118   1.00  45.70 ? 154  TRP A NE1 1 
ATOM   1161 C CE2 . TRP A 1 154 ? 37.006  21.798 0.992   1.00  46.20 ? 154  TRP A CE2 1 
ATOM   1162 C CE3 . TRP A 1 154 ? 38.101  19.908 2.047   1.00  45.90 ? 154  TRP A CE3 1 
ATOM   1163 C CZ2 . TRP A 1 154 ? 37.851  22.711 1.638   1.00  46.72 ? 154  TRP A CZ2 1 
ATOM   1164 C CZ3 . TRP A 1 154 ? 38.944  20.813 2.687   1.00  46.25 ? 154  TRP A CZ3 1 
ATOM   1165 C CH2 . TRP A 1 154 ? 38.812  22.200 2.479   1.00  46.70 ? 154  TRP A CH2 1 
ATOM   1166 N N   . ILE A 1 155 ? 38.462  16.871 0.803   1.00  45.50 ? 155  ILE A N   1 
ATOM   1167 C CA  . ILE A 1 155 ? 39.801  16.791 1.397   1.00  45.86 ? 155  ILE A CA  1 
ATOM   1168 C C   . ILE A 1 155 ? 40.867  16.572 0.326   1.00  46.16 ? 155  ILE A C   1 
ATOM   1169 O O   . ILE A 1 155 ? 41.763  17.399 0.167   1.00  46.09 ? 155  ILE A O   1 
ATOM   1170 C CB  . ILE A 1 155 ? 39.906  15.684 2.478   1.00  45.89 ? 155  ILE A CB  1 
ATOM   1171 C CG1 . ILE A 1 155 ? 39.043  16.035 3.691   1.00  45.85 ? 155  ILE A CG1 1 
ATOM   1172 C CG2 . ILE A 1 155 ? 41.367  15.491 2.913   1.00  45.91 ? 155  ILE A CG2 1 
ATOM   1173 C CD1 . ILE A 1 155 ? 39.004  14.947 4.772   1.00  46.20 ? 155  ILE A CD1 1 
ATOM   1174 N N   . ARG A 1 156 ? 40.747  15.471 -0.417  1.00  46.69 ? 156  ARG A N   1 
ATOM   1175 C CA  . ARG A 1 156 ? 41.700  15.145 -1.478  1.00  47.14 ? 156  ARG A CA  1 
ATOM   1176 C C   . ARG A 1 156 ? 41.857  16.320 -2.428  1.00  47.23 ? 156  ARG A C   1 
ATOM   1177 O O   . ARG A 1 156 ? 42.974  16.707 -2.760  1.00  47.34 ? 156  ARG A O   1 
ATOM   1178 C CB  . ARG A 1 156 ? 41.266  13.902 -2.264  1.00  47.20 ? 156  ARG A CB  1 
ATOM   1179 C CG  . ARG A 1 156 ? 41.415  12.583 -1.525  1.00  47.83 ? 156  ARG A CG  1 
ATOM   1180 C CD  . ARG A 1 156 ? 41.072  11.417 -2.445  1.00  49.45 ? 156  ARG A CD  1 
ATOM   1181 N NE  . ARG A 1 156 ? 40.716  10.199 -1.712  1.00  51.01 ? 156  ARG A NE  1 
ATOM   1182 C CZ  . ARG A 1 156 ? 39.489  9.893  -1.284  1.00  51.72 ? 156  ARG A CZ  1 
ATOM   1183 N NH1 . ARG A 1 156 ? 38.464  10.714 -1.502  1.00  51.74 ? 156  ARG A NH1 1 
ATOM   1184 N NH2 . ARG A 1 156 ? 39.285  8.757  -0.630  1.00  51.93 ? 156  ARG A NH2 1 
ATOM   1185 N N   . GLU A 1 157 ? 40.730  16.897 -2.833  1.00  47.34 ? 157  GLU A N   1 
ATOM   1186 C CA  . GLU A 1 157 ? 40.719  17.959 -3.830  1.00  47.43 ? 157  GLU A CA  1 
ATOM   1187 C C   . GLU A 1 157 ? 40.995  19.350 -3.255  1.00  47.37 ? 157  GLU A C   1 
ATOM   1188 O O   . GLU A 1 157 ? 40.941  20.339 -3.992  1.00  47.48 ? 157  GLU A O   1 
ATOM   1189 C CB  . GLU A 1 157 ? 39.386  17.963 -4.592  1.00  47.48 ? 157  GLU A CB  1 
ATOM   1190 C CG  . GLU A 1 157 ? 39.148  16.741 -5.464  1.00  47.63 ? 157  GLU A CG  1 
ATOM   1191 C CD  . GLU A 1 157 ? 37.964  16.906 -6.410  1.00  48.12 ? 157  GLU A CD  1 
ATOM   1192 O OE1 . GLU A 1 157 ? 37.666  15.950 -7.158  1.00  48.15 ? 157  GLU A OE1 1 
ATOM   1193 O OE2 . GLU A 1 157 ? 37.332  17.985 -6.417  1.00  48.27 ? 157  GLU A OE2 1 
ATOM   1194 N N   . ASN A 1 158 ? 41.285  19.442 -1.957  1.00  47.17 ? 158  ASN A N   1 
ATOM   1195 C CA  . ASN A 1 158 ? 41.513  20.757 -1.350  1.00  47.03 ? 158  ASN A CA  1 
ATOM   1196 C C   . ASN A 1 158 ? 42.703  20.885 -0.393  1.00  46.91 ? 158  ASN A C   1 
ATOM   1197 O O   . ASN A 1 158 ? 43.159  21.994 -0.110  1.00  47.09 ? 158  ASN A O   1 
ATOM   1198 C CB  . ASN A 1 158 ? 40.230  21.298 -0.709  1.00  46.87 ? 158  ASN A CB  1 
ATOM   1199 C CG  . ASN A 1 158 ? 39.192  21.700 -1.738  1.00  46.69 ? 158  ASN A CG  1 
ATOM   1200 O OD1 . ASN A 1 158 ? 38.452  20.862 -2.247  1.00  46.69 ? 158  ASN A OD1 1 
ATOM   1201 N ND2 . ASN A 1 158 ? 39.131  22.989 -2.046  1.00  46.77 ? 158  ASN A ND2 1 
ATOM   1202 N N   . ILE A 1 159 ? 43.206  19.756 0.091   1.00  46.61 ? 159  ILE A N   1 
ATOM   1203 C CA  . ILE A 1 159 ? 44.369  19.762 0.971   1.00  46.34 ? 159  ILE A CA  1 
ATOM   1204 C C   . ILE A 1 159 ? 45.571  19.156 0.253   1.00  46.25 ? 159  ILE A C   1 
ATOM   1205 O O   . ILE A 1 159 ? 45.649  17.944 0.031   1.00  46.28 ? 159  ILE A O   1 
ATOM   1206 C CB  . ILE A 1 159 ? 44.067  19.068 2.326   1.00  46.39 ? 159  ILE A CB  1 
ATOM   1207 C CG1 . ILE A 1 159 ? 42.994  19.879 3.069   1.00  46.48 ? 159  ILE A CG1 1 
ATOM   1208 C CG2 . ILE A 1 159 ? 45.353  18.910 3.161   1.00  46.01 ? 159  ILE A CG2 1 
ATOM   1209 C CD1 . ILE A 1 159 ? 42.482  19.262 4.358   1.00  46.78 ? 159  ILE A CD1 1 
ATOM   1210 N N   . SER A 1 160 ? 46.500  20.026 -0.120  1.00  46.13 ? 160  SER A N   1 
ATOM   1211 C CA  . SER A 1 160 ? 47.672  19.645 -0.910  1.00  46.08 ? 160  SER A CA  1 
ATOM   1212 C C   . SER A 1 160 ? 48.491  18.493 -0.317  1.00  46.04 ? 160  SER A C   1 
ATOM   1213 O O   . SER A 1 160 ? 48.982  17.636 -1.050  1.00  46.11 ? 160  SER A O   1 
ATOM   1214 C CB  . SER A 1 160 ? 48.559  20.872 -1.137  1.00  46.12 ? 160  SER A CB  1 
ATOM   1215 O OG  . SER A 1 160 ? 48.388  21.823 -0.093  1.00  46.18 ? 160  SER A OG  1 
ATOM   1216 N N   . GLU A 1 161 ? 48.606  18.473 1.009   0.95  45.99 ? 161  GLU A N   1 
ATOM   1217 C CA  . GLU A 1 161 ? 49.484  17.544 1.722   0.95  45.86 ? 161  GLU A CA  1 
ATOM   1218 C C   . GLU A 1 161 ? 48.739  16.315 2.248   0.95  45.94 ? 161  GLU A C   1 
ATOM   1219 O O   . GLU A 1 161 ? 49.316  15.495 2.971   0.95  45.95 ? 161  GLU A O   1 
ATOM   1220 C CB  . GLU A 1 161 ? 50.166  18.265 2.894   0.95  45.72 ? 161  GLU A CB  1 
ATOM   1221 C CG  . GLU A 1 161 ? 50.813  19.615 2.546   0.95  45.58 ? 161  GLU A CG  1 
ATOM   1222 C CD  . GLU A 1 161 ? 49.872  20.803 2.733   0.95  45.16 ? 161  GLU A CD  1 
ATOM   1223 O OE1 . GLU A 1 161 ? 48.728  20.764 2.225   0.95  45.06 ? 161  GLU A OE1 1 
ATOM   1224 O OE2 . GLU A 1 161 ? 50.278  21.786 3.403   0.95  44.72 ? 161  GLU A OE2 1 
ATOM   1225 N N   . TRP A 1 162 ? 47.466  16.188 1.871   1.00  45.95 ? 162  TRP A N   1 
ATOM   1226 C CA  . TRP A 1 162 ? 46.556  15.206 2.471   1.00  45.87 ? 162  TRP A CA  1 
ATOM   1227 C C   . TRP A 1 162 ? 47.133  13.797 2.639   1.00  45.81 ? 162  TRP A C   1 
ATOM   1228 O O   . TRP A 1 162 ? 46.825  13.112 3.613   1.00  45.94 ? 162  TRP A O   1 
ATOM   1229 C CB  . TRP A 1 162 ? 45.203  15.180 1.738   1.00  45.87 ? 162  TRP A CB  1 
ATOM   1230 C CG  . TRP A 1 162 ? 45.217  14.558 0.371   1.00  46.03 ? 162  TRP A CG  1 
ATOM   1231 C CD1 . TRP A 1 162 ? 45.415  15.198 -0.824  1.00  46.32 ? 162  TRP A CD1 1 
ATOM   1232 C CD2 . TRP A 1 162 ? 44.997  13.177 0.054   1.00  46.04 ? 162  TRP A CD2 1 
ATOM   1233 N NE1 . TRP A 1 162 ? 45.342  14.298 -1.863  1.00  46.49 ? 162  TRP A NE1 1 
ATOM   1234 C CE2 . TRP A 1 162 ? 45.089  13.051 -1.353  1.00  46.33 ? 162  TRP A CE2 1 
ATOM   1235 C CE3 . TRP A 1 162 ? 44.738  12.035 0.820   1.00  45.96 ? 162  TRP A CE3 1 
ATOM   1236 C CZ2 . TRP A 1 162 ? 44.931  11.823 -2.010  1.00  46.14 ? 162  TRP A CZ2 1 
ATOM   1237 C CZ3 . TRP A 1 162 ? 44.580  10.816 0.165   1.00  46.62 ? 162  TRP A CZ3 1 
ATOM   1238 C CH2 . TRP A 1 162 ? 44.676  10.722 -1.239  1.00  46.15 ? 162  TRP A CH2 1 
ATOM   1239 N N   . ARG A 1 163 ? 47.987  13.385 1.704   1.00  45.63 ? 163  ARG A N   1 
ATOM   1240 C CA  . ARG A 1 163 ? 48.602  12.057 1.721   1.00  45.42 ? 163  ARG A CA  1 
ATOM   1241 C C   . ARG A 1 163 ? 49.572  11.898 2.905   1.00  45.16 ? 163  ARG A C   1 
ATOM   1242 O O   . ARG A 1 163 ? 50.120  10.818 3.139   1.00  45.19 ? 163  ARG A O   1 
ATOM   1243 C CB  . ARG A 1 163 ? 49.286  11.773 0.374   1.00  45.59 ? 163  ARG A CB  1 
ATOM   1244 C CG  . ARG A 1 163 ? 48.639  12.498 -0.824  1.00  45.81 ? 163  ARG A CG  1 
ATOM   1245 C CD  . ARG A 1 163 ? 49.169  12.026 -2.173  1.00  46.49 ? 163  ARG A CD  1 
ATOM   1246 N NE  . ARG A 1 163 ? 48.137  11.390 -2.995  1.00  47.52 ? 163  ARG A NE  1 
ATOM   1247 C CZ  . ARG A 1 163 ? 47.944  10.075 -3.111  1.00  47.91 ? 163  ARG A CZ  1 
ATOM   1248 N NH1 . ARG A 1 163 ? 48.708  9.217  -2.447  1.00  47.44 ? 163  ARG A NH1 1 
ATOM   1249 N NH2 . ARG A 1 163 ? 46.974  9.617  -3.895  1.00  48.87 ? 163  ARG A NH2 1 
ATOM   1250 N N   . ASN A 1 164 ? 49.759  12.986 3.651   0.94  44.85 ? 164  ASN A N   1 
ATOM   1251 C CA  . ASN A 1 164 ? 50.514  12.975 4.904   0.94  44.69 ? 164  ASN A CA  1 
ATOM   1252 C C   . ASN A 1 164 ? 49.818  13.766 6.027   0.94  44.38 ? 164  ASN A C   1 
ATOM   1253 O O   . ASN A 1 164 ? 50.484  14.353 6.883   0.94  44.23 ? 164  ASN A O   1 
ATOM   1254 C CB  . ASN A 1 164 ? 51.939  13.513 4.683   0.94  44.84 ? 164  ASN A CB  1 
ATOM   1255 C CG  . ASN A 1 164 ? 52.925  12.429 4.265   0.94  45.13 ? 164  ASN A CG  1 
ATOM   1256 O OD1 . ASN A 1 164 ? 53.539  12.520 3.201   0.94  45.55 ? 164  ASN A OD1 1 
ATOM   1257 N ND2 . ASN A 1 164 ? 53.080  11.398 5.100   0.94  45.17 ? 164  ASN A ND2 1 
ATOM   1258 N N   . CYS A 1 165 ? 48.486  13.776 6.022   1.00  44.02 ? 165  CYS A N   1 
ATOM   1259 C CA  . CYS A 1 165 ? 47.711  14.551 6.999   1.00  43.57 ? 165  CYS A CA  1 
ATOM   1260 C C   . CYS A 1 165 ? 47.207  13.678 8.149   1.00  43.35 ? 165  CYS A C   1 
ATOM   1261 O O   . CYS A 1 165 ? 47.211  12.447 8.046   1.00  43.41 ? 165  CYS A O   1 
ATOM   1262 C CB  . CYS A 1 165 ? 46.521  15.223 6.310   1.00  43.62 ? 165  CYS A CB  1 
ATOM   1263 S SG  . CYS A 1 165 ? 45.158  14.084 5.959   1.00  43.04 ? 165  CYS A SG  1 
ATOM   1264 N N   . THR A 1 166 ? 46.767  14.314 9.235   1.00  42.84 ? 166  THR A N   1 
ATOM   1265 C CA  . THR A 1 166 ? 46.172  13.586 10.358  1.00  42.45 ? 166  THR A CA  1 
ATOM   1266 C C   . THR A 1 166 ? 44.738  14.038 10.638  1.00  42.15 ? 166  THR A C   1 
ATOM   1267 O O   . THR A 1 166 ? 44.474  15.230 10.822  1.00  42.13 ? 166  THR A O   1 
ATOM   1268 C CB  . THR A 1 166 ? 47.030  13.701 11.636  1.00  42.44 ? 166  THR A CB  1 
ATOM   1269 O OG1 . THR A 1 166 ? 48.389  13.396 11.318  1.00  42.55 ? 166  THR A OG1 1 
ATOM   1270 C CG2 . THR A 1 166 ? 46.558  12.724 12.703  1.00  42.40 ? 166  THR A CG2 1 
ATOM   1271 N N   . ILE A 1 167 ? 43.821  13.073 10.665  1.00  41.65 ? 167  ILE A N   1 
ATOM   1272 C CA  . ILE A 1 167 ? 42.420  13.346 10.970  1.00  41.12 ? 167  ILE A CA  1 
ATOM   1273 C C   . ILE A 1 167 ? 42.212  13.267 12.482  1.00  40.76 ? 167  ILE A C   1 
ATOM   1274 O O   . ILE A 1 167 ? 42.431  12.218 13.100  1.00  40.42 ? 167  ILE A O   1 
ATOM   1275 C CB  . ILE A 1 167 ? 41.468  12.380 10.228  1.00  41.19 ? 167  ILE A CB  1 
ATOM   1276 C CG1 . ILE A 1 167 ? 41.911  12.182 8.768   1.00  41.18 ? 167  ILE A CG1 1 
ATOM   1277 C CG2 . ILE A 1 167 ? 40.019  12.874 10.325  1.00  41.09 ? 167  ILE A CG2 1 
ATOM   1278 C CD1 . ILE A 1 167 ? 41.747  13.406 7.886   1.00  41.18 ? 167  ILE A CD1 1 
ATOM   1279 N N   . VAL A 1 168 ? 41.792  14.394 13.061  1.00  40.55 ? 168  VAL A N   1 
ATOM   1280 C CA  . VAL A 1 168 ? 41.759  14.581 14.517  1.00  40.32 ? 168  VAL A CA  1 
ATOM   1281 C C   . VAL A 1 168 ? 40.355  14.703 15.121  1.00  40.36 ? 168  VAL A C   1 
ATOM   1282 O O   . VAL A 1 168 ? 39.578  15.581 14.747  1.00  40.38 ? 168  VAL A O   1 
ATOM   1283 C CB  . VAL A 1 168 ? 42.559  15.833 14.927  1.00  40.18 ? 168  VAL A CB  1 
ATOM   1284 C CG1 . VAL A 1 168 ? 42.445  16.080 16.430  1.00  40.00 ? 168  VAL A CG1 1 
ATOM   1285 C CG2 . VAL A 1 168 ? 44.014  15.694 14.499  1.00  40.19 ? 168  VAL A CG2 1 
ATOM   1286 N N   . SER A 1 169 ? 40.049  13.840 16.084  1.00  40.36 ? 169  SER A N   1 
ATOM   1287 C CA  . SER A 1 169 ? 38.790  13.932 16.818  1.00  40.40 ? 169  SER A CA  1 
ATOM   1288 C C   . SER A 1 169 ? 38.866  14.938 17.966  1.00  40.26 ? 169  SER A C   1 
ATOM   1289 O O   . SER A 1 169 ? 39.812  14.912 18.753  1.00  40.19 ? 169  SER A O   1 
ATOM   1290 C CB  . SER A 1 169 ? 38.387  12.566 17.371  1.00  40.54 ? 169  SER A CB  1 
ATOM   1291 O OG  . SER A 1 169 ? 37.264  12.694 18.225  1.00  40.99 ? 169  SER A OG  1 
ATOM   1292 N N   . PRO A 1 170 ? 37.846  15.806 18.082  1.00  40.19 ? 170  PRO A N   1 
ATOM   1293 C CA  . PRO A 1 170 ? 37.780  16.854 19.107  1.00  40.10 ? 170  PRO A CA  1 
ATOM   1294 C C   . PRO A 1 170 ? 37.408  16.332 20.487  1.00  40.00 ? 170  PRO A C   1 
ATOM   1295 O O   . PRO A 1 170 ? 37.558  17.051 21.473  1.00  40.10 ? 170  PRO A O   1 
ATOM   1296 C CB  . PRO A 1 170 ? 36.668  17.784 18.606  1.00  40.17 ? 170  PRO A CB  1 
ATOM   1297 C CG  . PRO A 1 170 ? 36.255  17.260 17.255  1.00  40.58 ? 170  PRO A CG  1 
ATOM   1298 C CD  . PRO A 1 170 ? 36.674  15.836 17.194  1.00  40.27 ? 170  PRO A CD  1 
ATOM   1299 N N   . ASP A 1 171 ? 36.897  15.105 20.543  1.00  39.95 ? 171  ASP A N   1 
ATOM   1300 C CA  . ASP A 1 171 ? 36.561  14.433 21.804  1.00  39.82 ? 171  ASP A CA  1 
ATOM   1301 C C   . ASP A 1 171 ? 36.988  12.966 21.737  1.00  39.58 ? 171  ASP A C   1 
ATOM   1302 O O   . ASP A 1 171 ? 37.487  12.511 20.705  1.00  39.64 ? 171  ASP A O   1 
ATOM   1303 C CB  . ASP A 1 171 ? 35.062  14.565 22.129  1.00  39.80 ? 171  ASP A CB  1 
ATOM   1304 C CG  . ASP A 1 171 ? 34.161  14.280 20.927  1.00  40.37 ? 171  ASP A CG  1 
ATOM   1305 O OD1 . ASP A 1 171 ? 33.396  15.182 20.524  1.00  40.76 ? 171  ASP A OD1 1 
ATOM   1306 O OD2 . ASP A 1 171 ? 34.206  13.159 20.381  1.00  40.98 ? 171  ASP A OD2 1 
ATOM   1307 N N   . ALA A 1 172 ? 36.825  12.238 22.839  1.00  39.32 ? 172  ALA A N   1 
ATOM   1308 C CA  . ALA A 1 172 ? 37.078  10.798 22.835  1.00  39.12 ? 172  ALA A CA  1 
ATOM   1309 C C   . ALA A 1 172 ? 35.927  10.081 22.137  1.00  38.79 ? 172  ALA A C   1 
ATOM   1310 O O   . ALA A 1 172 ? 36.126  9.095  21.414  1.00  38.75 ? 172  ALA A O   1 
ATOM   1311 C CB  . ALA A 1 172 ? 37.254  10.279 24.255  1.00  39.20 ? 172  ALA A CB  1 
ATOM   1312 N N   . GLY A 1 173 ? 34.723  10.606 22.345  1.00  38.36 ? 173  GLY A N   1 
ATOM   1313 C CA  . GLY A 1 173 ? 33.511  10.065 21.731  1.00  37.86 ? 173  GLY A CA  1 
ATOM   1314 C C   . GLY A 1 173 ? 33.455  10.184 20.214  1.00  37.43 ? 173  GLY A C   1 
ATOM   1315 O O   . GLY A 1 173 ? 32.423  9.902  19.598  1.00  37.29 ? 173  GLY A O   1 
ATOM   1316 N N   . GLY A 1 174 ? 34.560  10.606 19.606  1.00  37.05 ? 174  GLY A N   1 
ATOM   1317 C CA  . GLY A 1 174 ? 34.634  10.733 18.155  1.00  36.55 ? 174  GLY A CA  1 
ATOM   1318 C C   . GLY A 1 174 ? 35.705  9.858  17.535  1.00  36.17 ? 174  GLY A C   1 
ATOM   1319 O O   . GLY A 1 174 ? 36.135  10.104 16.407  1.00  36.03 ? 174  GLY A O   1 
ATOM   1320 N N   . ALA A 1 175 ? 36.119  8.828  18.272  1.00  35.82 ? 175  ALA A N   1 
ATOM   1321 C CA  . ALA A 1 175 ? 37.154  7.900  17.823  1.00  35.59 ? 175  ALA A CA  1 
ATOM   1322 C C   . ALA A 1 175 ? 36.773  7.165  16.547  1.00  35.38 ? 175  ALA A C   1 
ATOM   1323 O O   . ALA A 1 175 ? 37.546  7.129  15.596  1.00  35.49 ? 175  ALA A O   1 
ATOM   1324 C CB  . ALA A 1 175 ? 37.475  6.906  18.917  1.00  35.64 ? 175  ALA A CB  1 
ATOM   1325 N N   . LYS A 1 176 ? 35.575  6.588  16.532  0.80  35.18 ? 176  LYS A N   1 
ATOM   1326 C CA  . LYS A 1 176 ? 35.136  5.739  15.426  0.80  34.94 ? 176  LYS A CA  1 
ATOM   1327 C C   . LYS A 1 176 ? 35.008  6.503  14.111  0.80  34.81 ? 176  LYS A C   1 
ATOM   1328 O O   . LYS A 1 176 ? 35.475  6.039  13.068  0.80  34.68 ? 176  LYS A O   1 
ATOM   1329 C CB  . LYS A 1 176 ? 33.814  5.050  15.769  0.80  34.90 ? 176  LYS A CB  1 
ATOM   1330 C CG  . LYS A 1 176 ? 33.766  3.590  15.346  0.80  35.02 ? 176  LYS A CG  1 
ATOM   1331 C CD  . LYS A 1 176 ? 32.380  2.996  15.551  0.80  35.77 ? 176  LYS A CD  1 
ATOM   1332 C CE  . LYS A 1 176 ? 32.434  1.487  15.776  0.80  35.85 ? 176  LYS A CE  1 
ATOM   1333 N NZ  . LYS A 1 176 ? 32.705  1.131  17.199  0.80  36.29 ? 176  LYS A NZ  1 
ATOM   1334 N N   . ARG A 1 177 ? 34.389  7.678  14.172  0.70  34.86 ? 177  ARG A N   1 
ATOM   1335 C CA  . ARG A 1 177 ? 34.141  8.489  12.985  0.70  35.02 ? 177  ARG A CA  1 
ATOM   1336 C C   . ARG A 1 177 ? 35.433  8.922  12.284  0.70  35.19 ? 177  ARG A C   1 
ATOM   1337 O O   . ARG A 1 177 ? 35.523  8.858  11.052  0.70  35.22 ? 177  ARG A O   1 
ATOM   1338 C CB  . ARG A 1 177 ? 33.295  9.710  13.346  0.70  34.99 ? 177  ARG A CB  1 
ATOM   1339 C CG  . ARG A 1 177 ? 32.620  10.375 12.153  0.70  35.02 ? 177  ARG A CG  1 
ATOM   1340 C CD  . ARG A 1 177 ? 31.994  11.714 12.520  0.70  34.94 ? 177  ARG A CD  1 
ATOM   1341 N NE  . ARG A 1 177 ? 30.892  11.563 13.470  0.70  35.14 ? 177  ARG A NE  1 
ATOM   1342 C CZ  . ARG A 1 177 ? 30.941  11.913 14.755  0.70  35.06 ? 177  ARG A CZ  1 
ATOM   1343 N NH1 . ARG A 1 177 ? 32.037  12.458 15.271  0.70  34.71 ? 177  ARG A NH1 1 
ATOM   1344 N NH2 . ARG A 1 177 ? 29.879  11.726 15.526  0.70  35.28 ? 177  ARG A NH2 1 
ATOM   1345 N N   . VAL A 1 178 ? 36.424  9.359  13.065  1.00  35.34 ? 178  VAL A N   1 
ATOM   1346 C CA  . VAL A 1 178 ? 37.711  9.783  12.494  1.00  35.44 ? 178  VAL A CA  1 
ATOM   1347 C C   . VAL A 1 178 ? 38.563  8.612  11.977  1.00  35.60 ? 178  VAL A C   1 
ATOM   1348 O O   . VAL A 1 178 ? 39.044  8.665  10.833  1.00  35.65 ? 178  VAL A O   1 
ATOM   1349 C CB  . VAL A 1 178 ? 38.538  10.735 13.423  1.00  35.41 ? 178  VAL A CB  1 
ATOM   1350 C CG1 . VAL A 1 178 ? 37.795  12.054 13.640  1.00  35.80 ? 178  VAL A CG1 1 
ATOM   1351 C CG2 . VAL A 1 178 ? 38.914  10.068 14.750  1.00  35.16 ? 178  VAL A CG2 1 
ATOM   1352 N N   . THR A 1 179 ? 38.730  7.563  12.792  1.00  35.68 ? 179  THR A N   1 
ATOM   1353 C CA  . THR A 1 179 ? 39.462  6.358  12.362  1.00  35.98 ? 179  THR A CA  1 
ATOM   1354 C C   . THR A 1 179 ? 38.965  5.843  11.017  1.00  36.20 ? 179  THR A C   1 
ATOM   1355 O O   . THR A 1 179 ? 39.763  5.396  10.185  1.00  36.26 ? 179  THR A O   1 
ATOM   1356 C CB  . THR A 1 179 ? 39.367  5.180  13.363  1.00  35.84 ? 179  THR A CB  1 
ATOM   1357 O OG1 . THR A 1 179 ? 37.995  4.945  13.708  1.00  36.21 ? 179  THR A OG1 1 
ATOM   1358 C CG2 . THR A 1 179 ? 40.183  5.439  14.617  1.00  36.12 ? 179  THR A CG2 1 
ATOM   1359 N N   . SER A 1 180 ? 37.649  5.898  10.811  1.00  36.52 ? 180  SER A N   1 
ATOM   1360 C CA  . SER A 1 180 ? 37.067  5.518  9.529   1.00  37.02 ? 180  SER A CA  1 
ATOM   1361 C C   . SER A 1 180 ? 37.601  6.403  8.414   1.00  37.15 ? 180  SER A C   1 
ATOM   1362 O O   . SER A 1 180 ? 38.135  5.897  7.429   1.00  37.17 ? 180  SER A O   1 
ATOM   1363 C CB  . SER A 1 180 ? 35.542  5.593  9.561   1.00  37.23 ? 180  SER A CB  1 
ATOM   1364 O OG  . SER A 1 180 ? 35.018  5.469  8.243   1.00  37.60 ? 180  SER A OG  1 
ATOM   1365 N N   . ILE A 1 181 ? 37.461  7.717  8.585   1.00  37.36 ? 181  ILE A N   1 
ATOM   1366 C CA  . ILE A 1 181 ? 37.944  8.685  7.605   1.00  37.66 ? 181  ILE A CA  1 
ATOM   1367 C C   . ILE A 1 181 ? 39.445  8.545  7.355   1.00  37.56 ? 181  ILE A C   1 
ATOM   1368 O O   . ILE A 1 181 ? 39.886  8.580  6.203   1.00  37.52 ? 181  ILE A O   1 
ATOM   1369 C CB  . ILE A 1 181 ? 37.540  10.134 7.984   1.00  37.78 ? 181  ILE A CB  1 
ATOM   1370 C CG1 . ILE A 1 181 ? 36.080  10.388 7.580   1.00  38.24 ? 181  ILE A CG1 1 
ATOM   1371 C CG2 . ILE A 1 181 ? 38.443  11.164 7.300   1.00  38.20 ? 181  ILE A CG2 1 
ATOM   1372 C CD1 . ILE A 1 181 ? 35.561  11.774 7.944   1.00  38.87 ? 181  ILE A CD1 1 
ATOM   1373 N N   . ALA A 1 182 ? 40.210  8.368  8.430   1.00  37.53 ? 182  ALA A N   1 
ATOM   1374 C CA  . ALA A 1 182 ? 41.652  8.158  8.331   1.00  37.68 ? 182  ALA A CA  1 
ATOM   1375 C C   . ALA A 1 182 ? 42.001  6.870  7.575   1.00  37.71 ? 182  ALA A C   1 
ATOM   1376 O O   . ALA A 1 182 ? 42.990  6.832  6.836   1.00  37.54 ? 182  ALA A O   1 
ATOM   1377 C CB  . ALA A 1 182 ? 42.285  8.166  9.715   1.00  37.71 ? 182  ALA A CB  1 
ATOM   1378 N N   . ASP A 1 183 ? 41.174  5.838  7.748   1.00  37.81 ? 183  ASP A N   1 
ATOM   1379 C CA  . ASP A 1 183 ? 41.393  4.549  7.096   1.00  38.14 ? 183  ASP A CA  1 
ATOM   1380 C C   . ASP A 1 183 ? 41.145  4.562  5.586   1.00  38.36 ? 183  ASP A C   1 
ATOM   1381 O O   . ASP A 1 183 ? 41.941  4.000  4.827   1.00  38.47 ? 183  ASP A O   1 
ATOM   1382 C CB  . ASP A 1 183 ? 40.584  3.447  7.774   1.00  38.17 ? 183  ASP A CB  1 
ATOM   1383 C CG  . ASP A 1 183 ? 41.295  2.862  8.981   1.00  38.31 ? 183  ASP A CG  1 
ATOM   1384 O OD1 . ASP A 1 183 ? 42.520  2.626  8.914   1.00  38.22 ? 183  ASP A OD1 1 
ATOM   1385 O OD2 . ASP A 1 183 ? 40.622  2.625  9.999   1.00  39.17 ? 183  ASP A OD2 1 
ATOM   1386 N N   . ARG A 1 184 ? 40.050  5.195  5.160   0.40  38.50 ? 184  ARG A N   1 
ATOM   1387 C CA  . ARG A 1 184 ? 39.768  5.389  3.736   0.40  38.59 ? 184  ARG A CA  1 
ATOM   1388 C C   . ARG A 1 184 ? 40.899  6.158  3.051   0.40  38.70 ? 184  ARG A C   1 
ATOM   1389 O O   . ARG A 1 184 ? 41.338  5.790  1.963   0.40  38.66 ? 184  ARG A O   1 
ATOM   1390 C CB  . ARG A 1 184 ? 38.440  6.122  3.545   0.40  38.56 ? 184  ARG A CB  1 
ATOM   1391 C CG  . ARG A 1 184 ? 37.210  5.232  3.621   0.40  38.61 ? 184  ARG A CG  1 
ATOM   1392 C CD  . ARG A 1 184 ? 37.258  4.319  4.835   0.40  39.07 ? 184  ARG A CD  1 
ATOM   1393 N NE  . ARG A 1 184 ? 35.933  3.821  5.200   0.40  39.23 ? 184  ARG A NE  1 
ATOM   1394 C CZ  . ARG A 1 184 ? 35.686  3.041  6.249   0.40  38.89 ? 184  ARG A CZ  1 
ATOM   1395 N NH1 . ARG A 1 184 ? 36.674  2.663  7.051   0.40  38.66 ? 184  ARG A NH1 1 
ATOM   1396 N NH2 . ARG A 1 184 ? 34.446  2.645  6.500   0.40  38.66 ? 184  ARG A NH2 1 
ATOM   1397 N N   . LEU A 1 185 ? 41.375  7.210  3.712   1.00  39.00 ? 185  LEU A N   1 
ATOM   1398 C CA  . LEU A 1 185 ? 42.463  8.058  3.195   1.00  39.33 ? 185  LEU A CA  1 
ATOM   1399 C C   . LEU A 1 185 ? 43.851  7.440  3.356   1.00  39.54 ? 185  LEU A C   1 
ATOM   1400 O O   . LEU A 1 185 ? 44.835  7.958  2.803   1.00  39.33 ? 185  LEU A O   1 
ATOM   1401 C CB  . LEU A 1 185 ? 42.455  9.427  3.890   1.00  39.28 ? 185  LEU A CB  1 
ATOM   1402 C CG  . LEU A 1 185 ? 41.351  10.444 3.599   1.00  39.16 ? 185  LEU A CG  1 
ATOM   1403 C CD1 . LEU A 1 185 ? 41.514  11.617 4.555   1.00  38.58 ? 185  LEU A CD1 1 
ATOM   1404 C CD2 . LEU A 1 185 ? 41.370  10.910 2.138   1.00  39.08 ? 185  LEU A CD2 1 
ATOM   1405 N N   . ASN A 1 186 ? 43.906  6.342  4.116   1.00  39.87 ? 186  ASN A N   1 
ATOM   1406 C CA  . ASN A 1 186 ? 45.143  5.644  4.499   1.00  40.04 ? 186  ASN A CA  1 
ATOM   1407 C C   . ASN A 1 186 ? 46.193  6.553  5.147   1.00  39.96 ? 186  ASN A C   1 
ATOM   1408 O O   . ASN A 1 186 ? 47.374  6.518  4.796   1.00  39.95 ? 186  ASN A O   1 
ATOM   1409 C CB  . ASN A 1 186 ? 45.721  4.840  3.328   1.00  40.10 ? 186  ASN A CB  1 
ATOM   1410 C CG  . ASN A 1 186 ? 46.191  3.466  3.752   1.00  40.86 ? 186  ASN A CG  1 
ATOM   1411 O OD1 . ASN A 1 186 ? 47.297  3.308  4.272   1.00  41.57 ? 186  ASN A OD1 1 
ATOM   1412 N ND2 . ASN A 1 186 ? 45.347  2.460  3.540   1.00  41.91 ? 186  ASN A ND2 1 
ATOM   1413 N N   . VAL A 1 187 ? 45.739  7.366  6.097   1.00  39.95 ? 187  VAL A N   1 
ATOM   1414 C CA  . VAL A 1 187 ? 46.622  8.256  6.853   1.00  40.12 ? 187  VAL A CA  1 
ATOM   1415 C C   . VAL A 1 187 ? 46.420  8.151  8.378   1.00  40.14 ? 187  VAL A C   1 
ATOM   1416 O O   . VAL A 1 187 ? 45.536  7.443  8.860   1.00  40.04 ? 187  VAL A O   1 
ATOM   1417 C CB  . VAL A 1 187 ? 46.497  9.742  6.394   1.00  40.07 ? 187  VAL A CB  1 
ATOM   1418 C CG1 . VAL A 1 187 ? 46.936  9.902  4.949   1.00  40.22 ? 187  VAL A CG1 1 
ATOM   1419 C CG2 . VAL A 1 187 ? 45.076  10.270 6.600   1.00  40.44 ? 187  VAL A CG2 1 
ATOM   1420 N N   . ASP A 1 188 ? 47.250  8.878  9.118   0.90  40.25 ? 188  ASP A N   1 
ATOM   1421 C CA  . ASP A 1 188 ? 47.266  8.855  10.578  0.90  40.42 ? 188  ASP A CA  1 
ATOM   1422 C C   . ASP A 1 188 ? 45.999  9.432  11.227  0.90  40.50 ? 188  ASP A C   1 
ATOM   1423 O O   . ASP A 1 188 ? 45.322  10.285 10.639  0.90  40.47 ? 188  ASP A O   1 
ATOM   1424 C CB  . ASP A 1 188 ? 48.495  9.629  11.076  0.90  40.55 ? 188  ASP A CB  1 
ATOM   1425 C CG  . ASP A 1 188 ? 49.812  8.968  10.683  0.90  40.45 ? 188  ASP A CG  1 
ATOM   1426 O OD1 . ASP A 1 188 ? 49.842  8.221  9.676   0.90  40.16 ? 188  ASP A OD1 1 
ATOM   1427 O OD2 . ASP A 1 188 ? 50.820  9.194  11.392  0.90  40.24 ? 188  ASP A OD2 1 
ATOM   1428 N N   . PHE A 1 189 ? 45.691  8.964  12.440  1.00  40.45 ? 189  PHE A N   1 
ATOM   1429 C CA  . PHE A 1 189 ? 44.587  9.519  13.229  1.00  40.45 ? 189  PHE A CA  1 
ATOM   1430 C C   . PHE A 1 189 ? 45.072  9.979  14.603  1.00  40.55 ? 189  PHE A C   1 
ATOM   1431 O O   . PHE A 1 189 ? 46.030  9.425  15.138  1.00  40.67 ? 189  PHE A O   1 
ATOM   1432 C CB  . PHE A 1 189 ? 43.428  8.514  13.354  1.00  40.36 ? 189  PHE A CB  1 
ATOM   1433 C CG  . PHE A 1 189 ? 43.616  7.472  14.434  1.00  40.25 ? 189  PHE A CG  1 
ATOM   1434 C CD1 . PHE A 1 189 ? 43.216  7.724  15.750  1.00  39.53 ? 189  PHE A CD1 1 
ATOM   1435 C CD2 . PHE A 1 189 ? 44.161  6.226  14.128  1.00  39.98 ? 189  PHE A CD2 1 
ATOM   1436 C CE1 . PHE A 1 189 ? 43.379  6.762  16.738  1.00  39.06 ? 189  PHE A CE1 1 
ATOM   1437 C CE2 . PHE A 1 189 ? 44.325  5.257  15.114  1.00  39.20 ? 189  PHE A CE2 1 
ATOM   1438 C CZ  . PHE A 1 189 ? 43.936  5.525  16.418  1.00  39.13 ? 189  PHE A CZ  1 
ATOM   1439 N N   . ALA A 1 190 ? 44.412  10.989 15.166  1.00  40.61 ? 190  ALA A N   1 
ATOM   1440 C CA  . ALA A 1 190 ? 44.771  11.500 16.489  1.00  40.71 ? 190  ALA A CA  1 
ATOM   1441 C C   . ALA A 1 190 ? 43.559  12.014 17.251  1.00  40.95 ? 190  ALA A C   1 
ATOM   1442 O O   . ALA A 1 190 ? 42.638  12.576 16.661  1.00  41.11 ? 190  ALA A O   1 
ATOM   1443 C CB  . ALA A 1 190 ? 45.819  12.582 16.376  1.00  40.71 ? 190  ALA A CB  1 
ATOM   1444 N N   . LEU A 1 191 ? 43.574  11.824 18.566  1.00  41.22 ? 191  LEU A N   1 
ATOM   1445 C CA  . LEU A 1 191 ? 42.420  12.133 19.401  1.00  41.47 ? 191  LEU A CA  1 
ATOM   1446 C C   . LEU A 1 191 ? 42.769  13.128 20.503  1.00  41.70 ? 191  LEU A C   1 
ATOM   1447 O O   . LEU A 1 191 ? 43.900  13.168 20.988  1.00  41.72 ? 191  LEU A O   1 
ATOM   1448 C CB  . LEU A 1 191 ? 41.835  10.845 19.986  1.00  41.44 ? 191  LEU A CB  1 
ATOM   1449 C CG  . LEU A 1 191 ? 40.444  10.907 20.624  1.00  41.67 ? 191  LEU A CG  1 
ATOM   1450 C CD1 . LEU A 1 191 ? 39.620  9.690  20.238  1.00  41.49 ? 191  LEU A CD1 1 
ATOM   1451 C CD2 . LEU A 1 191 ? 40.539  11.053 22.146  1.00  41.90 ? 191  LEU A CD2 1 
ATOM   1452 N N   . ILE A 1 192 ? 41.781  13.938 20.875  1.00  42.03 ? 192  ILE A N   1 
ATOM   1453 C CA  . ILE A 1 192 ? 41.921  14.939 21.920  1.00  42.13 ? 192  ILE A CA  1 
ATOM   1454 C C   . ILE A 1 192 ? 40.852  14.703 22.967  1.00  42.33 ? 192  ILE A C   1 
ATOM   1455 O O   . ILE A 1 192 ? 39.741  14.292 22.643  1.00  42.43 ? 192  ILE A O   1 
ATOM   1456 C CB  . ILE A 1 192 ? 41.831  16.364 21.345  1.00  42.11 ? 192  ILE A CB  1 
ATOM   1457 C CG1 . ILE A 1 192 ? 43.147  16.720 20.639  1.00  42.33 ? 192  ILE A CG1 1 
ATOM   1458 C CG2 . ILE A 1 192 ? 41.506  17.385 22.436  1.00  42.05 ? 192  ILE A CG2 1 
ATOM   1459 C CD1 . ILE A 1 192 ? 43.024  17.829 19.609  1.00  42.68 ? 192  ILE A CD1 1 
ATOM   1460 N N   . HIS A 1 193 ? 41.205  14.954 24.222  1.00  42.66 ? 193  HIS A N   1 
ATOM   1461 C CA  . HIS A 1 193 ? 40.316  14.728 25.354  1.00  42.91 ? 193  HIS A CA  1 
ATOM   1462 C C   . HIS A 1 193 ? 40.482  15.849 26.369  1.00  42.84 ? 193  HIS A C   1 
ATOM   1463 O O   . HIS A 1 193 ? 41.609  16.216 26.718  1.00  42.86 ? 193  HIS A O   1 
ATOM   1464 C CB  . HIS A 1 193 ? 40.631  13.379 26.003  1.00  43.02 ? 193  HIS A CB  1 
ATOM   1465 C CG  . HIS A 1 193 ? 39.941  13.162 27.311  1.00  43.80 ? 193  HIS A CG  1 
ATOM   1466 N ND1 . HIS A 1 193 ? 38.579  12.973 27.411  1.00  44.91 ? 193  HIS A ND1 1 
ATOM   1467 C CD2 . HIS A 1 193 ? 40.424  13.102 28.574  1.00  44.63 ? 193  HIS A CD2 1 
ATOM   1468 C CE1 . HIS A 1 193 ? 38.252  12.802 28.679  1.00  45.25 ? 193  HIS A CE1 1 
ATOM   1469 N NE2 . HIS A 1 193 ? 39.353  12.877 29.406  1.00  45.31 ? 193  HIS A NE2 1 
ATOM   1470 N N   . LYS A 1 194 ? 39.366  16.395 26.841  0.30  42.93 ? 194  LYS A N   1 
ATOM   1471 C CA  . LYS A 1 194 ? 39.424  17.421 27.872  0.30  43.04 ? 194  LYS A CA  1 
ATOM   1472 C C   . LYS A 1 194 ? 39.418  16.798 29.257  0.30  43.20 ? 194  LYS A C   1 
ATOM   1473 O O   . LYS A 1 194 ? 38.474  16.098 29.632  0.30  43.16 ? 194  LYS A O   1 
ATOM   1474 C CB  . LYS A 1 194 ? 38.287  18.431 27.735  0.30  42.99 ? 194  LYS A CB  1 
ATOM   1475 C CG  . LYS A 1 194 ? 38.290  19.460 28.853  0.30  43.08 ? 194  LYS A CG  1 
ATOM   1476 C CD  . LYS A 1 194 ? 37.436  20.671 28.532  0.30  43.22 ? 194  LYS A CD  1 
ATOM   1477 C CE  . LYS A 1 194 ? 37.455  21.658 29.689  0.30  43.16 ? 194  LYS A CE  1 
ATOM   1478 N NZ  . LYS A 1 194 ? 36.789  22.941 29.336  0.30  43.21 ? 194  LYS A NZ  1 
ATOM   1479 N N   . GLU A 1 195 ? 40.486  17.068 30.004  0.80  43.48 ? 195  GLU A N   1 
ATOM   1480 C CA  . GLU A 1 195 ? 40.717  16.483 31.324  0.80  43.69 ? 195  GLU A CA  1 
ATOM   1481 C C   . GLU A 1 195 ? 39.582  16.770 32.309  0.80  43.66 ? 195  GLU A C   1 
ATOM   1482 O O   . GLU A 1 195 ? 39.226  17.940 32.542  0.80  43.74 ? 195  GLU A O   1 
ATOM   1483 C CB  . GLU A 1 195 ? 42.053  16.987 31.884  0.80  43.74 ? 195  GLU A CB  1 
ATOM   1484 C CG  . GLU A 1 195 ? 42.911  15.907 32.538  0.80  44.14 ? 195  GLU A CG  1 
ATOM   1485 C CD  . GLU A 1 195 ? 43.650  15.030 31.528  0.80  44.60 ? 195  GLU A CD  1 
ATOM   1486 O OE1 . GLU A 1 195 ? 42.998  14.482 30.610  0.80  44.76 ? 195  GLU A OE1 1 
ATOM   1487 O OE2 . GLU A 1 195 ? 44.886  14.872 31.667  0.80  44.44 ? 195  GLU A OE2 1 
ATOM   1488 N N   . ASP A 1 203 ? 39.723  23.006 32.691  0.010 37.91 ? 203  ASP A N   1 
ATOM   1489 C CA  . ASP A 1 203 ? 40.250  21.713 32.271  0.010 37.93 ? 203  ASP A CA  1 
ATOM   1490 C C   . ASP A 1 203 ? 41.497  21.877 31.410  0.010 37.98 ? 203  ASP A C   1 
ATOM   1491 O O   . ASP A 1 203 ? 41.817  22.980 30.965  0.010 37.98 ? 203  ASP A O   1 
ATOM   1492 C CB  . ASP A 1 203 ? 39.187  20.924 31.505  0.010 37.90 ? 203  ASP A CB  1 
ATOM   1493 C CG  . ASP A 1 203 ? 37.969  20.614 32.351  0.010 37.87 ? 203  ASP A CG  1 
ATOM   1494 O OD1 . ASP A 1 203 ? 38.030  20.819 33.581  0.010 37.84 ? 203  ASP A OD1 1 
ATOM   1495 O OD2 . ASP A 1 203 ? 36.950  20.163 31.786  0.010 37.84 ? 203  ASP A OD2 1 
ATOM   1496 N N   . ARG A 1 204 ? 42.198  20.772 31.178  0.010 38.08 ? 204  ARG A N   1 
ATOM   1497 C CA  . ARG A 1 204 ? 43.390  20.786 30.342  0.010 38.21 ? 204  ARG A CA  1 
ATOM   1498 C C   . ARG A 1 204 ? 43.247  19.756 29.228  0.010 38.37 ? 204  ARG A C   1 
ATOM   1499 O O   . ARG A 1 204 ? 42.832  18.621 29.465  0.010 38.36 ? 204  ARG A O   1 
ATOM   1500 C CB  . ARG A 1 204 ? 44.639  20.498 31.179  0.010 38.17 ? 204  ARG A CB  1 
ATOM   1501 C CG  . ARG A 1 204 ? 45.231  19.115 30.968  0.010 38.09 ? 204  ARG A CG  1 
ATOM   1502 C CD  . ARG A 1 204 ? 46.425  19.167 30.024  0.010 37.95 ? 204  ARG A CD  1 
ATOM   1503 N NE  . ARG A 1 204 ? 47.672  19.442 30.737  0.010 37.85 ? 204  ARG A NE  1 
ATOM   1504 C CZ  . ARG A 1 204 ? 48.119  20.659 31.031  0.010 37.79 ? 204  ARG A CZ  1 
ATOM   1505 N NH1 . ARG A 1 204 ? 47.423  21.730 30.673  0.010 37.78 ? 204  ARG A NH1 1 
ATOM   1506 N NH2 . ARG A 1 204 ? 49.265  20.806 31.683  0.010 37.77 ? 204  ARG A NH2 1 
ATOM   1507 N N   . MET A 1 205 ? 43.590  20.162 28.012  0.60  38.60 ? 205  MET A N   1 
ATOM   1508 C CA  . MET A 1 205 ? 43.425  19.315 26.842  0.60  38.99 ? 205  MET A CA  1 
ATOM   1509 C C   . MET A 1 205 ? 44.618  18.392 26.613  0.60  39.30 ? 205  MET A C   1 
ATOM   1510 O O   . MET A 1 205 ? 45.773  18.809 26.734  0.60  39.31 ? 205  MET A O   1 
ATOM   1511 C CB  . MET A 1 205 ? 43.176  20.168 25.602  0.60  38.97 ? 205  MET A CB  1 
ATOM   1512 C CG  . MET A 1 205 ? 41.730  20.581 25.423  0.60  39.63 ? 205  MET A CG  1 
ATOM   1513 S SD  . MET A 1 205 ? 41.409  21.280 23.791  0.60  41.25 ? 205  MET A SD  1 
ATOM   1514 C CE  . MET A 1 205 ? 39.741  20.684 23.477  0.60  40.65 ? 205  MET A CE  1 
ATOM   1515 N N   . VAL A 1 206 ? 44.317  17.143 26.268  1.00  39.69 ? 206  VAL A N   1 
ATOM   1516 C CA  . VAL A 1 206 ? 45.322  16.103 26.092  1.00  40.04 ? 206  VAL A CA  1 
ATOM   1517 C C   . VAL A 1 206 ? 45.229  15.560 24.666  1.00  40.40 ? 206  VAL A C   1 
ATOM   1518 O O   . VAL A 1 206 ? 44.127  15.346 24.161  1.00  40.51 ? 206  VAL A O   1 
ATOM   1519 C CB  . VAL A 1 206 ? 45.136  15.001 27.179  1.00  39.94 ? 206  VAL A CB  1 
ATOM   1520 C CG1 . VAL A 1 206 ? 45.624  13.633 26.715  1.00  40.19 ? 206  VAL A CG1 1 
ATOM   1521 C CG2 . VAL A 1 206 ? 45.834  15.413 28.464  1.00  39.94 ? 206  VAL A CG2 1 
ATOM   1522 N N   . LEU A 1 207 ? 46.376  15.364 24.015  1.00  40.91 ? 207  LEU A N   1 
ATOM   1523 C CA  . LEU A 1 207 ? 46.396  14.898 22.627  1.00  41.66 ? 207  LEU A CA  1 
ATOM   1524 C C   . LEU A 1 207 ? 47.166  13.591 22.446  1.00  42.29 ? 207  LEU A C   1 
ATOM   1525 O O   . LEU A 1 207 ? 48.375  13.524 22.719  1.00  42.59 ? 207  LEU A O   1 
ATOM   1526 C CB  . LEU A 1 207 ? 46.969  15.980 21.701  1.00  41.57 ? 207  LEU A CB  1 
ATOM   1527 C CG  . LEU A 1 207 ? 46.802  15.808 20.187  1.00  41.70 ? 207  LEU A CG  1 
ATOM   1528 C CD1 . LEU A 1 207 ? 46.868  17.160 19.503  1.00  41.82 ? 207  LEU A CD1 1 
ATOM   1529 C CD2 . LEU A 1 207 ? 47.841  14.850 19.592  1.00  41.61 ? 207  LEU A CD2 1 
ATOM   1530 N N   . VAL A 1 208 ? 46.461  12.566 21.963  1.00  42.89 ? 208  VAL A N   1 
ATOM   1531 C CA  . VAL A 1 208 ? 47.069  11.272 21.656  1.00  43.48 ? 208  VAL A CA  1 
ATOM   1532 C C   . VAL A 1 208 ? 47.081  11.022 20.149  1.00  43.95 ? 208  VAL A C   1 
ATOM   1533 O O   . VAL A 1 208 ? 46.035  11.030 19.500  1.00  43.87 ? 208  VAL A O   1 
ATOM   1534 C CB  . VAL A 1 208 ? 46.371  10.112 22.402  1.00  43.46 ? 208  VAL A CB  1 
ATOM   1535 C CG1 . VAL A 1 208 ? 45.997  10.543 23.819  1.00  43.55 ? 208  VAL A CG1 1 
ATOM   1536 C CG2 . VAL A 1 208 ? 45.138  9.626  21.644  1.00  43.81 ? 208  VAL A CG2 1 
ATOM   1537 N N   . GLY A 1 209 ? 48.277  10.806 19.608  1.00  44.72 ? 209  GLY A N   1 
ATOM   1538 C CA  . GLY A 1 209 ? 48.474  10.634 18.164  1.00  45.63 ? 209  GLY A CA  1 
ATOM   1539 C C   . GLY A 1 209 ? 49.571  11.560 17.673  1.00  46.27 ? 209  GLY A C   1 
ATOM   1540 O O   . GLY A 1 209 ? 49.927  12.520 18.364  1.00  46.40 ? 209  GLY A O   1 
ATOM   1541 N N   . ASP A 1 210 ? 50.112  11.284 16.487  1.00  46.86 ? 210  ASP A N   1 
ATOM   1542 C CA  . ASP A 1 210 ? 51.225  12.081 15.965  1.00  47.42 ? 210  ASP A CA  1 
ATOM   1543 C C   . ASP A 1 210 ? 50.778  13.124 14.948  1.00  47.70 ? 210  ASP A C   1 
ATOM   1544 O O   . ASP A 1 210 ? 50.374  12.792 13.832  1.00  47.93 ? 210  ASP A O   1 
ATOM   1545 C CB  . ASP A 1 210 ? 52.321  11.194 15.368  1.00  47.51 ? 210  ASP A CB  1 
ATOM   1546 C CG  . ASP A 1 210 ? 53.552  11.989 14.957  1.00  48.01 ? 210  ASP A CG  1 
ATOM   1547 O OD1 . ASP A 1 210 ? 54.125  12.686 15.824  1.00  48.63 ? 210  ASP A OD1 1 
ATOM   1548 O OD2 . ASP A 1 210 ? 53.944  11.918 13.771  1.00  48.31 ? 210  ASP A OD2 1 
ATOM   1549 N N   . VAL A 1 211 ? 50.872  14.390 15.342  1.00  47.98 ? 211  VAL A N   1 
ATOM   1550 C CA  . VAL A 1 211 ? 50.407  15.498 14.507  1.00  48.20 ? 211  VAL A CA  1 
ATOM   1551 C C   . VAL A 1 211 ? 51.532  16.469 14.140  1.00  48.25 ? 211  VAL A C   1 
ATOM   1552 O O   . VAL A 1 211 ? 51.292  17.477 13.467  1.00  48.49 ? 211  VAL A O   1 
ATOM   1553 C CB  . VAL A 1 211 ? 49.244  16.278 15.186  1.00  48.28 ? 211  VAL A CB  1 
ATOM   1554 C CG1 . VAL A 1 211 ? 48.069  15.347 15.507  1.00  48.20 ? 211  VAL A CG1 1 
ATOM   1555 C CG2 . VAL A 1 211 ? 49.730  16.989 16.445  1.00  48.20 ? 211  VAL A CG2 1 
ATOM   1556 N N   . LYS A 1 212 ? 52.750  16.163 14.583  0.40  48.14 ? 212  LYS A N   1 
ATOM   1557 C CA  . LYS A 1 212 ? 53.903  17.037 14.369  0.40  47.97 ? 212  LYS A CA  1 
ATOM   1558 C C   . LYS A 1 212 ? 54.306  17.099 12.900  0.40  47.91 ? 212  LYS A C   1 
ATOM   1559 O O   . LYS A 1 212 ? 54.520  16.062 12.262  0.40  47.88 ? 212  LYS A O   1 
ATOM   1560 C CB  . LYS A 1 212 ? 55.090  16.578 15.217  0.40  47.97 ? 212  LYS A CB  1 
ATOM   1561 C CG  . LYS A 1 212 ? 56.262  17.547 15.237  0.40  47.81 ? 212  LYS A CG  1 
ATOM   1562 C CD  . LYS A 1 212 ? 55.892  18.840 15.940  0.40  47.74 ? 212  LYS A CD  1 
ATOM   1563 C CE  . LYS A 1 212 ? 57.129  19.620 16.364  0.40  47.71 ? 212  LYS A CE  1 
ATOM   1564 N NZ  . LYS A 1 212 ? 56.778  20.853 17.132  0.40  47.43 ? 212  LYS A NZ  1 
ATOM   1565 N N   . ASP A 1 213 ? 54.406  18.327 12.387  1.00  47.83 ? 213  ASP A N   1 
ATOM   1566 C CA  . ASP A 1 213 ? 54.803  18.619 10.996  1.00  47.78 ? 213  ASP A CA  1 
ATOM   1567 C C   . ASP A 1 213 ? 53.910  17.957 9.947   1.00  47.45 ? 213  ASP A C   1 
ATOM   1568 O O   . ASP A 1 213 ? 54.400  17.364 8.981   1.00  47.37 ? 213  ASP A O   1 
ATOM   1569 C CB  . ASP A 1 213 ? 56.284  18.279 10.727  1.00  47.99 ? 213  ASP A CB  1 
ATOM   1570 C CG  . ASP A 1 213 ? 57.235  18.896 11.744  1.00  48.53 ? 213  ASP A CG  1 
ATOM   1571 O OD1 . ASP A 1 213 ? 58.248  18.240 12.072  1.00  49.28 ? 213  ASP A OD1 1 
ATOM   1572 O OD2 . ASP A 1 213 ? 56.983  20.028 12.215  1.00  49.12 ? 213  ASP A OD2 1 
ATOM   1573 N N   . ARG A 1 214 ? 52.601  18.059 10.145  0.40  47.15 ? 214  ARG A N   1 
ATOM   1574 C CA  . ARG A 1 214 ? 51.640  17.577 9.162   0.40  46.86 ? 214  ARG A CA  1 
ATOM   1575 C C   . ARG A 1 214 ? 50.342  18.366 9.265   0.40  46.79 ? 214  ARG A C   1 
ATOM   1576 O O   . ARG A 1 214 ? 50.086  19.027 10.275  0.40  46.70 ? 214  ARG A O   1 
ATOM   1577 C CB  . ARG A 1 214 ? 51.401  16.067 9.314   0.40  46.78 ? 214  ARG A CB  1 
ATOM   1578 C CG  . ARG A 1 214 ? 51.108  15.603 10.728  0.40  46.29 ? 214  ARG A CG  1 
ATOM   1579 C CD  . ARG A 1 214 ? 51.581  14.170 10.964  0.40  45.34 ? 214  ARG A CD  1 
ATOM   1580 N NE  . ARG A 1 214 ? 50.860  13.187 10.154  0.40  44.72 ? 214  ARG A NE  1 
ATOM   1581 C CZ  . ARG A 1 214 ? 51.399  12.491 9.156   0.40  44.12 ? 214  ARG A CZ  1 
ATOM   1582 N NH1 . ARG A 1 214 ? 52.674  12.662 8.834   0.40  43.59 ? 214  ARG A NH1 1 
ATOM   1583 N NH2 . ARG A 1 214 ? 50.663  11.619 8.478   0.40  43.78 ? 214  ARG A NH2 1 
ATOM   1584 N N   . VAL A 1 215 ? 49.541  18.308 8.206   1.00  46.70 ? 215  VAL A N   1 
ATOM   1585 C CA  . VAL A 1 215 ? 48.259  18.993 8.177   1.00  46.72 ? 215  VAL A CA  1 
ATOM   1586 C C   . VAL A 1 215 ? 47.267  18.260 9.070   1.00  46.68 ? 215  VAL A C   1 
ATOM   1587 O O   . VAL A 1 215 ? 47.065  17.054 8.918   1.00  46.88 ? 215  VAL A O   1 
ATOM   1588 C CB  . VAL A 1 215 ? 47.715  19.103 6.739   1.00  46.67 ? 215  VAL A CB  1 
ATOM   1589 C CG1 . VAL A 1 215 ? 46.280  19.628 6.736   1.00  46.56 ? 215  VAL A CG1 1 
ATOM   1590 C CG2 . VAL A 1 215 ? 48.616  20.015 5.921   1.00  46.87 ? 215  VAL A CG2 1 
ATOM   1591 N N   . ALA A 1 216 ? 46.670  18.984 10.013  1.00  46.42 ? 216  ALA A N   1 
ATOM   1592 C CA  . ALA A 1 216 ? 45.668  18.400 10.899  1.00  46.21 ? 216  ALA A CA  1 
ATOM   1593 C C   . ALA A 1 216 ? 44.263  18.702 10.402  1.00  46.11 ? 216  ALA A C   1 
ATOM   1594 O O   . ALA A 1 216 ? 43.980  19.815 9.958   1.00  46.11 ? 216  ALA A O   1 
ATOM   1595 C CB  . ALA A 1 216 ? 45.851  18.907 12.319  1.00  46.18 ? 216  ALA A CB  1 
ATOM   1596 N N   . ILE A 1 217 ? 43.386  17.705 10.472  1.00  46.04 ? 217  ILE A N   1 
ATOM   1597 C CA  . ILE A 1 217 ? 41.988  17.895 10.088  1.00  46.07 ? 217  ILE A CA  1 
ATOM   1598 C C   . ILE A 1 217 ? 41.040  17.472 11.207  1.00  46.04 ? 217  ILE A C   1 
ATOM   1599 O O   . ILE A 1 217 ? 40.773  16.281 11.398  1.00  45.79 ? 217  ILE A O   1 
ATOM   1600 C CB  . ILE A 1 217 ? 41.620  17.152 8.769   1.00  46.16 ? 217  ILE A CB  1 
ATOM   1601 C CG1 . ILE A 1 217 ? 42.675  17.410 7.683   1.00  46.05 ? 217  ILE A CG1 1 
ATOM   1602 C CG2 . ILE A 1 217 ? 40.213  17.563 8.295   1.00  45.86 ? 217  ILE A CG2 1 
ATOM   1603 C CD1 . ILE A 1 217 ? 42.565  16.507 6.477   1.00  46.08 ? 217  ILE A CD1 1 
ATOM   1604 N N   . LEU A 1 218 ? 40.542  18.462 11.942  1.00  46.17 ? 218  LEU A N   1 
ATOM   1605 C CA  . LEU A 1 218 ? 39.512  18.239 12.943  1.00  46.47 ? 218  LEU A CA  1 
ATOM   1606 C C   . LEU A 1 218 ? 38.228  17.833 12.250  1.00  46.80 ? 218  LEU A C   1 
ATOM   1607 O O   . LEU A 1 218 ? 37.740  18.542 11.374  1.00  46.71 ? 218  LEU A O   1 
ATOM   1608 C CB  . LEU A 1 218 ? 39.273  19.501 13.780  1.00  46.34 ? 218  LEU A CB  1 
ATOM   1609 C CG  . LEU A 1 218 ? 40.064  19.641 15.081  1.00  46.43 ? 218  LEU A CG  1 
ATOM   1610 C CD1 . LEU A 1 218 ? 40.242  21.109 15.436  1.00  46.07 ? 218  LEU A CD1 1 
ATOM   1611 C CD2 . LEU A 1 218 ? 39.389  18.880 16.218  1.00  46.49 ? 218  LEU A CD2 1 
ATOM   1612 N N   . VAL A 1 219 ? 37.690  16.681 12.631  1.00  47.45 ? 219  VAL A N   1 
ATOM   1613 C CA  . VAL A 1 219 ? 36.432  16.212 12.062  1.00  47.95 ? 219  VAL A CA  1 
ATOM   1614 C C   . VAL A 1 219 ? 35.418  15.895 13.157  1.00  48.40 ? 219  VAL A C   1 
ATOM   1615 O O   . VAL A 1 219 ? 35.632  15.008 13.984  1.00  48.33 ? 219  VAL A O   1 
ATOM   1616 C CB  . VAL A 1 219 ? 36.636  15.005 11.110  1.00  47.86 ? 219  VAL A CB  1 
ATOM   1617 C CG1 . VAL A 1 219 ? 35.295  14.438 10.654  1.00  47.88 ? 219  VAL A CG1 1 
ATOM   1618 C CG2 . VAL A 1 219 ? 37.449  15.424 9.904   1.00  47.96 ? 219  VAL A CG2 1 
ATOM   1619 N N   . ASP A 1 220 ? 34.323  16.645 13.155  1.00  49.09 ? 220  ASP A N   1 
ATOM   1620 C CA  . ASP A 1 220 ? 33.211  16.379 14.047  1.00  49.93 ? 220  ASP A CA  1 
ATOM   1621 C C   . ASP A 1 220 ? 31.906  16.291 13.255  1.00  50.60 ? 220  ASP A C   1 
ATOM   1622 O O   . ASP A 1 220 ? 31.836  16.758 12.110  1.00  50.59 ? 220  ASP A O   1 
ATOM   1623 C CB  . ASP A 1 220 ? 33.124  17.458 15.124  1.00  49.91 ? 220  ASP A CB  1 
ATOM   1624 C CG  . ASP A 1 220 ? 32.617  16.917 16.445  1.00  50.11 ? 220  ASP A CG  1 
ATOM   1625 O OD1 . ASP A 1 220 ? 33.075  15.828 16.855  1.00  50.23 ? 220  ASP A OD1 1 
ATOM   1626 O OD2 . ASP A 1 220 ? 31.768  17.581 17.078  1.00  50.41 ? 220  ASP A OD2 1 
ATOM   1627 N N   . ASP A 1 221 ? 30.883  15.679 13.853  1.00  51.43 ? 221  ASP A N   1 
ATOM   1628 C CA  . ASP A 1 221 ? 29.584  15.594 13.201  1.00  52.18 ? 221  ASP A CA  1 
ATOM   1629 C C   . ASP A 1 221 ? 28.887  16.938 13.286  1.00  52.73 ? 221  ASP A C   1 
ATOM   1630 O O   . ASP A 1 221 ? 28.226  17.348 12.335  1.00  52.99 ? 221  ASP A O   1 
ATOM   1631 C CB  . ASP A 1 221 ? 28.715  14.485 13.792  1.00  52.15 ? 221  ASP A CB  1 
ATOM   1632 C CG  . ASP A 1 221 ? 28.272  14.780 15.207  1.00  52.92 ? 221  ASP A CG  1 
ATOM   1633 O OD1 . ASP A 1 221 ? 27.067  14.590 15.506  1.00  53.87 ? 221  ASP A OD1 1 
ATOM   1634 O OD2 . ASP A 1 221 ? 29.124  15.217 16.020  1.00  53.74 ? 221  ASP A OD2 1 
ATOM   1635 N N   . MET A 1 222 ? 29.058  17.629 14.414  0.81  53.36 ? 222  MET A N   1 
ATOM   1636 C CA  . MET A 1 222 ? 28.497  18.966 14.588  0.81  54.01 ? 222  MET A CA  1 
ATOM   1637 C C   . MET A 1 222 ? 29.291  19.836 15.548  0.81  54.39 ? 222  MET A C   1 
ATOM   1638 O O   . MET A 1 222 ? 29.904  19.341 16.493  0.81  54.55 ? 222  MET A O   1 
ATOM   1639 C CB  . MET A 1 222 ? 27.024  18.913 15.022  0.81  54.08 ? 222  MET A CB  1 
ATOM   1640 C CG  . MET A 1 222 ? 26.748  18.282 16.380  0.81  54.61 ? 222  MET A CG  1 
ATOM   1641 S SD  . MET A 1 222 ? 25.132  18.783 17.018  0.81  56.45 ? 222  MET A SD  1 
ATOM   1642 C CE  . MET A 1 222 ? 23.994  18.010 15.844  0.81  56.38 ? 222  MET A CE  1 
ATOM   1643 N N   . ALA A 1 223 ? 29.269  21.138 15.288  1.00  54.84 ? 223  ALA A N   1 
ATOM   1644 C CA  . ALA A 1 223 ? 29.819  22.119 16.207  1.00  55.28 ? 223  ALA A CA  1 
ATOM   1645 C C   . ALA A 1 223 ? 28.731  23.132 16.547  1.00  55.61 ? 223  ALA A C   1 
ATOM   1646 O O   . ALA A 1 223 ? 28.001  23.591 15.661  1.00  55.65 ? 223  ALA A O   1 
ATOM   1647 C CB  . ALA A 1 223 ? 31.022  22.798 15.596  1.00  55.25 ? 223  ALA A CB  1 
ATOM   1648 N N   . ASP A 1 224 ? 28.616  23.465 17.830  1.00  56.00 ? 224  ASP A N   1 
ATOM   1649 C CA  . ASP A 1 224 ? 27.569  24.369 18.285  1.00  56.38 ? 224  ASP A CA  1 
ATOM   1650 C C   . ASP A 1 224 ? 28.126  25.710 18.736  1.00  56.54 ? 224  ASP A C   1 
ATOM   1651 O O   . ASP A 1 224 ? 27.831  26.740 18.137  1.00  56.60 ? 224  ASP A O   1 
ATOM   1652 C CB  . ASP A 1 224 ? 26.749  23.733 19.403  1.00  56.46 ? 224  ASP A CB  1 
ATOM   1653 C CG  . ASP A 1 224 ? 25.681  24.662 19.934  1.00  56.80 ? 224  ASP A CG  1 
ATOM   1654 O OD1 . ASP A 1 224 ? 24.824  25.106 19.144  1.00  56.84 ? 224  ASP A OD1 1 
ATOM   1655 O OD2 . ASP A 1 224 ? 25.702  24.951 21.146  1.00  57.52 ? 224  ASP A OD2 1 
ATOM   1656 N N   . THR A 1 225 ? 28.913  25.688 19.806  1.00  56.85 ? 225  THR A N   1 
ATOM   1657 C CA  . THR A 1 225 ? 29.578  26.893 20.303  1.00  57.11 ? 225  THR A CA  1 
ATOM   1658 C C   . THR A 1 225 ? 30.944  27.038 19.633  1.00  57.23 ? 225  THR A C   1 
ATOM   1659 O O   . THR A 1 225 ? 31.506  28.138 19.568  1.00  57.20 ? 225  THR A O   1 
ATOM   1660 C CB  . THR A 1 225 ? 29.757  26.882 21.856  1.00  57.09 ? 225  THR A CB  1 
ATOM   1661 O OG1 . THR A 1 225 ? 30.799  25.971 22.236  1.00  57.27 ? 225  THR A OG1 1 
ATOM   1662 C CG2 . THR A 1 225 ? 28.458  26.511 22.569  1.00  57.01 ? 225  THR A CG2 1 
ATOM   1663 N N   . CYS A 1 226 ? 31.459  25.912 19.137  0.40  57.32 ? 226  CYS A N   1 
ATOM   1664 C CA  . CYS A 1 226 ? 32.805  25.811 18.569  0.40  57.42 ? 226  CYS A CA  1 
ATOM   1665 C C   . CYS A 1 226 ? 33.889  25.977 19.628  0.40  57.36 ? 226  CYS A C   1 
ATOM   1666 O O   . CYS A 1 226 ? 35.079  25.934 19.312  0.40  57.40 ? 226  CYS A O   1 
ATOM   1667 C CB  . CYS A 1 226 ? 33.008  26.812 17.429  0.40  57.49 ? 226  CYS A CB  1 
ATOM   1668 S SG  . CYS A 1 226 ? 31.763  26.671 16.133  0.40  57.55 ? 226  CYS A SG  1 
ATOM   1669 N N   . GLY A 1 227 ? 33.468  26.164 20.877  1.00  57.24 ? 227  GLY A N   1 
ATOM   1670 C CA  . GLY A 1 227 ? 34.386  26.295 22.004  1.00  57.19 ? 227  GLY A CA  1 
ATOM   1671 C C   . GLY A 1 227 ? 35.386  25.163 22.038  1.00  57.09 ? 227  GLY A C   1 
ATOM   1672 O O   . GLY A 1 227 ? 36.600  25.395 22.010  1.00  57.19 ? 227  GLY A O   1 
ATOM   1673 N N   . THR A 1 228 ? 34.860  23.939 22.073  1.00  56.95 ? 228  THR A N   1 
ATOM   1674 C CA  . THR A 1 228 ? 35.671  22.726 22.103  1.00  56.66 ? 228  THR A CA  1 
ATOM   1675 C C   . THR A 1 228 ? 36.586  22.603 20.885  1.00  56.48 ? 228  THR A C   1 
ATOM   1676 O O   . THR A 1 228 ? 37.759  22.262 21.030  1.00  56.43 ? 228  THR A O   1 
ATOM   1677 C CB  . THR A 1 228 ? 34.785  21.475 22.280  1.00  56.61 ? 228  THR A CB  1 
ATOM   1678 O OG1 . THR A 1 228 ? 34.381  21.385 23.653  1.00  56.42 ? 228  THR A OG1 1 
ATOM   1679 C CG2 . THR A 1 228 ? 35.533  20.205 21.897  1.00  56.71 ? 228  THR A CG2 1 
ATOM   1680 N N   . ILE A 1 229 ? 36.062  22.910 19.702  0.20  56.35 ? 229  ILE A N   1 
ATOM   1681 C CA  . ILE A 1 229 ? 36.841  22.754 18.476  0.20  56.25 ? 229  ILE A CA  1 
ATOM   1682 C C   . ILE A 1 229 ? 37.903  23.845 18.283  0.20  56.23 ? 229  ILE A C   1 
ATOM   1683 O O   . ILE A 1 229 ? 38.924  23.610 17.630  0.20  56.20 ? 229  ILE A O   1 
ATOM   1684 C CB  . ILE A 1 229 ? 35.938  22.597 17.226  0.20  56.21 ? 229  ILE A CB  1 
ATOM   1685 C CG1 . ILE A 1 229 ? 36.642  21.731 16.180  0.20  56.18 ? 229  ILE A CG1 1 
ATOM   1686 C CG2 . ILE A 1 229 ? 35.539  23.951 16.658  0.20  56.15 ? 229  ILE A CG2 1 
ATOM   1687 C CD1 . ILE A 1 229 ? 35.735  20.701 15.519  0.20  56.22 ? 229  ILE A CD1 1 
ATOM   1688 N N   . CYS A 1 230 ? 37.669  25.021 18.866  1.00  56.26 ? 230  CYS A N   1 
ATOM   1689 C CA  . CYS A 1 230 ? 38.615  26.141 18.763  1.00  56.30 ? 230  CYS A CA  1 
ATOM   1690 C C   . CYS A 1 230 ? 39.780  25.970 19.727  1.00  56.22 ? 230  CYS A C   1 
ATOM   1691 O O   . CYS A 1 230 ? 40.922  26.322 19.398  1.00  56.29 ? 230  CYS A O   1 
ATOM   1692 C CB  . CYS A 1 230 ? 37.922  27.492 18.979  1.00  56.31 ? 230  CYS A CB  1 
ATOM   1693 S SG  . CYS A 1 230 ? 37.290  28.250 17.454  1.00  56.67 ? 230  CYS A SG  1 
ATOM   1694 N N   . HIS A 1 231 ? 39.482  25.444 20.918  1.00  56.01 ? 231  HIS A N   1 
ATOM   1695 C CA  . HIS A 1 231 ? 40.520  24.938 21.805  1.00  55.69 ? 231  HIS A CA  1 
ATOM   1696 C C   . HIS A 1 231 ? 41.291  23.857 21.069  1.00  55.16 ? 231  HIS A C   1 
ATOM   1697 O O   . HIS A 1 231 ? 42.496  23.991 20.861  1.00  55.26 ? 231  HIS A O   1 
ATOM   1698 C CB  . HIS A 1 231 ? 39.921  24.362 23.088  1.00  55.88 ? 231  HIS A CB  1 
ATOM   1699 C CG  . HIS A 1 231 ? 39.423  25.397 24.048  1.00  56.89 ? 231  HIS A CG  1 
ATOM   1700 N ND1 . HIS A 1 231 ? 39.651  26.747 23.879  1.00  57.74 ? 231  HIS A ND1 1 
ATOM   1701 C CD2 . HIS A 1 231 ? 38.736  25.272 25.207  1.00  57.53 ? 231  HIS A CD2 1 
ATOM   1702 C CE1 . HIS A 1 231 ? 39.111  27.411 24.886  1.00  58.07 ? 231  HIS A CE1 1 
ATOM   1703 N NE2 . HIS A 1 231 ? 38.552  26.539 25.707  1.00  58.29 ? 231  HIS A NE2 1 
ATOM   1704 N N   . ALA A 1 232 ? 40.582  22.805 20.653  1.00  54.60 ? 232  ALA A N   1 
ATOM   1705 C CA  . ALA A 1 232 ? 41.177  21.688 19.912  1.00  53.99 ? 232  ALA A CA  1 
ATOM   1706 C C   . ALA A 1 232 ? 42.205  22.167 18.890  1.00  53.59 ? 232  ALA A C   1 
ATOM   1707 O O   . ALA A 1 232 ? 43.246  21.533 18.702  1.00  53.44 ? 232  ALA A O   1 
ATOM   1708 C CB  . ALA A 1 232 ? 40.092  20.860 19.233  1.00  53.95 ? 232  ALA A CB  1 
ATOM   1709 N N   . ALA A 1 233 ? 41.909  23.306 18.261  1.00  53.11 ? 233  ALA A N   1 
ATOM   1710 C CA  . ALA A 1 233 ? 42.788  23.931 17.271  1.00  52.62 ? 233  ALA A CA  1 
ATOM   1711 C C   . ALA A 1 233 ? 44.100  24.471 17.858  1.00  52.14 ? 233  ALA A C   1 
ATOM   1712 O O   . ALA A 1 233 ? 45.171  24.269 17.283  1.00  52.09 ? 233  ALA A O   1 
ATOM   1713 C CB  . ALA A 1 233 ? 42.038  25.035 16.520  1.00  52.70 ? 233  ALA A CB  1 
ATOM   1714 N N   . ASP A 1 234 ? 44.010  25.164 18.991  0.40  51.58 ? 234  ASP A N   1 
ATOM   1715 C CA  . ASP A 1 234 ? 45.189  25.682 19.684  0.40  51.03 ? 234  ASP A CA  1 
ATOM   1716 C C   . ASP A 1 234 ? 46.088  24.531 20.110  0.40  50.60 ? 234  ASP A C   1 
ATOM   1717 O O   . ASP A 1 234 ? 47.265  24.480 19.759  0.40  50.61 ? 234  ASP A O   1 
ATOM   1718 C CB  . ASP A 1 234 ? 44.776  26.469 20.927  0.40  51.10 ? 234  ASP A CB  1 
ATOM   1719 C CG  . ASP A 1 234 ? 43.654  27.447 20.652  0.40  51.10 ? 234  ASP A CG  1 
ATOM   1720 O OD1 . ASP A 1 234 ? 43.470  27.825 19.475  0.40  51.10 ? 234  ASP A OD1 1 
ATOM   1721 O OD2 . ASP A 1 234 ? 42.954  27.836 21.611  0.40  50.88 ? 234  ASP A OD2 1 
ATOM   1722 N N   . LYS A 1 235 ? 45.514  23.606 20.871  0.20  50.02 ? 235  LYS A N   1 
ATOM   1723 C CA  . LYS A 1 235 ? 46.230  22.422 21.324  0.20  49.43 ? 235  LYS A CA  1 
ATOM   1724 C C   . LYS A 1 235 ? 46.977  21.784 20.160  0.20  48.97 ? 235  LYS A C   1 
ATOM   1725 O O   . LYS A 1 235 ? 48.097  21.303 20.324  0.20  48.87 ? 235  LYS A O   1 
ATOM   1726 C CB  . LYS A 1 235 ? 45.251  21.414 21.936  0.20  49.47 ? 235  LYS A CB  1 
ATOM   1727 C CG  . LYS A 1 235 ? 45.760  20.711 23.189  0.20  49.51 ? 235  LYS A CG  1 
ATOM   1728 C CD  . LYS A 1 235 ? 47.036  19.915 22.927  0.20  49.57 ? 235  LYS A CD  1 
ATOM   1729 C CE  . LYS A 1 235 ? 47.649  19.462 24.254  0.20  49.68 ? 235  LYS A CE  1 
ATOM   1730 N NZ  . LYS A 1 235 ? 49.046  18.973 24.085  0.20  49.76 ? 235  LYS A NZ  1 
ATOM   1731 N N   . LEU A 1 236 ? 46.348  21.789 18.989  1.00  48.41 ? 236  LEU A N   1 
ATOM   1732 C CA  . LEU A 1 236 ? 46.931  21.189 17.800  1.00  48.00 ? 236  LEU A CA  1 
ATOM   1733 C C   . LEU A 1 236 ? 48.078  22.009 17.230  1.00  47.92 ? 236  LEU A C   1 
ATOM   1734 O O   . LEU A 1 236 ? 49.059  21.441 16.753  1.00  47.97 ? 236  LEU A O   1 
ATOM   1735 C CB  . LEU A 1 236 ? 45.863  20.941 16.735  1.00  47.94 ? 236  LEU A CB  1 
ATOM   1736 C CG  . LEU A 1 236 ? 45.121  19.605 16.798  1.00  47.46 ? 236  LEU A CG  1 
ATOM   1737 C CD1 . LEU A 1 236 ? 43.816  19.697 16.037  1.00  47.49 ? 236  LEU A CD1 1 
ATOM   1738 C CD2 . LEU A 1 236 ? 45.974  18.480 16.241  1.00  47.35 ? 236  LEU A CD2 1 
ATOM   1739 N N   . LEU A 1 237 ? 47.957  23.336 17.273  1.00  47.84 ? 237  LEU A N   1 
ATOM   1740 C CA  . LEU A 1 237 ? 49.058  24.221 16.868  1.00  47.57 ? 237  LEU A CA  1 
ATOM   1741 C C   . LEU A 1 237 ? 50.258  24.065 17.794  1.00  47.23 ? 237  LEU A C   1 
ATOM   1742 O O   . LEU A 1 237 ? 51.383  23.856 17.320  1.00  47.06 ? 237  LEU A O   1 
ATOM   1743 C CB  . LEU A 1 237 ? 48.619  25.688 16.827  1.00  47.73 ? 237  LEU A CB  1 
ATOM   1744 C CG  . LEU A 1 237 ? 47.918  26.222 15.574  1.00  48.04 ? 237  LEU A CG  1 
ATOM   1745 C CD1 . LEU A 1 237 ? 48.232  27.703 15.430  1.00  48.41 ? 237  LEU A CD1 1 
ATOM   1746 C CD2 . LEU A 1 237 ? 48.337  25.482 14.309  1.00  48.96 ? 237  LEU A CD2 1 
ATOM   1747 N N   . SER A 1 238 ? 50.000  24.169 19.103  1.00  46.83 ? 238  SER A N   1 
ATOM   1748 C CA  . SER A 1 238 ? 50.997  23.909 20.151  1.00  46.64 ? 238  SER A CA  1 
ATOM   1749 C C   . SER A 1 238 ? 51.691  22.560 19.982  1.00  46.26 ? 238  SER A C   1 
ATOM   1750 O O   . SER A 1 238 ? 52.835  22.380 20.405  1.00  46.08 ? 238  SER A O   1 
ATOM   1751 C CB  . SER A 1 238 ? 50.338  23.947 21.532  1.00  46.76 ? 238  SER A CB  1 
ATOM   1752 O OG  . SER A 1 238 ? 49.469  25.059 21.665  1.00  47.33 ? 238  SER A OG  1 
ATOM   1753 N N   . ALA A 1 239 ? 50.977  21.613 19.381  1.00  45.99 ? 239  ALA A N   1 
ATOM   1754 C CA  . ALA A 1 239 ? 51.514  20.289 19.115  1.00  45.95 ? 239  ALA A CA  1 
ATOM   1755 C C   . ALA A 1 239 ? 52.386  20.277 17.858  1.00  45.96 ? 239  ALA A C   1 
ATOM   1756 O O   . ALA A 1 239 ? 53.044  19.280 17.556  1.00  45.98 ? 239  ALA A O   1 
ATOM   1757 C CB  . ALA A 1 239 ? 50.383  19.282 18.995  1.00  45.99 ? 239  ALA A CB  1 
ATOM   1758 N N   . GLY A 1 240 ? 52.388  21.389 17.131  1.00  46.06 ? 240  GLY A N   1 
ATOM   1759 C CA  . GLY A 1 240 ? 53.217  21.529 15.939  1.00  46.35 ? 240  GLY A CA  1 
ATOM   1760 C C   . GLY A 1 240 ? 52.552  21.023 14.677  1.00  46.55 ? 240  GLY A C   1 
ATOM   1761 O O   . GLY A 1 240 ? 53.189  20.361 13.851  1.00  46.39 ? 240  GLY A O   1 
ATOM   1762 N N   . ALA A 1 241 ? 51.266  21.325 14.533  1.00  46.94 ? 241  ALA A N   1 
ATOM   1763 C CA  . ALA A 1 241 ? 50.554  21.017 13.305  1.00  47.41 ? 241  ALA A CA  1 
ATOM   1764 C C   . ALA A 1 241 ? 50.942  22.074 12.279  1.00  47.78 ? 241  ALA A C   1 
ATOM   1765 O O   . ALA A 1 241 ? 51.093  23.256 12.624  1.00  48.04 ? 241  ALA A O   1 
ATOM   1766 C CB  . ALA A 1 241 ? 49.058  21.015 13.544  1.00  47.42 ? 241  ALA A CB  1 
ATOM   1767 N N   . THR A 1 242 ? 51.130  21.651 11.031  1.00  48.00 ? 242  THR A N   1 
ATOM   1768 C CA  . THR A 1 242 ? 51.524  22.584 9.982   1.00  48.25 ? 242  THR A CA  1 
ATOM   1769 C C   . THR A 1 242 ? 50.348  23.509 9.665   1.00  48.35 ? 242  THR A C   1 
ATOM   1770 O O   . THR A 1 242 ? 50.466  24.733 9.803   1.00  48.38 ? 242  THR A O   1 
ATOM   1771 C CB  . THR A 1 242 ? 52.062  21.859 8.734   1.00  48.33 ? 242  THR A CB  1 
ATOM   1772 O OG1 . THR A 1 242 ? 53.071  20.922 9.133   1.00  48.30 ? 242  THR A OG1 1 
ATOM   1773 C CG2 . THR A 1 242 ? 52.681  22.857 7.767   1.00  48.65 ? 242  THR A CG2 1 
ATOM   1774 N N   . ARG A 1 243 ? 49.221  22.919 9.266   1.00  48.43 ? 243  ARG A N   1 
ATOM   1775 C CA  . ARG A 1 243 ? 47.975  23.661 9.090   1.00  48.47 ? 243  ARG A CA  1 
ATOM   1776 C C   . ARG A 1 243 ? 46.793  22.837 9.610   1.00  48.11 ? 243  ARG A C   1 
ATOM   1777 O O   . ARG A 1 243 ? 46.628  21.666 9.251   1.00  48.04 ? 243  ARG A O   1 
ATOM   1778 C CB  . ARG A 1 243 ? 47.778  24.068 7.619   1.00  48.65 ? 243  ARG A CB  1 
ATOM   1779 C CG  . ARG A 1 243 ? 48.858  25.025 7.105   1.00  49.86 ? 243  ARG A CG  1 
ATOM   1780 C CD  . ARG A 1 243 ? 48.841  25.254 5.597   1.00  51.81 ? 243  ARG A CD  1 
ATOM   1781 N NE  . ARG A 1 243 ? 48.700  24.019 4.832   1.00  53.55 ? 243  ARG A NE  1 
ATOM   1782 C CZ  . ARG A 1 243 ? 47.686  23.771 4.008   1.00  54.42 ? 243  ARG A CZ  1 
ATOM   1783 N NH1 . ARG A 1 243 ? 46.734  24.679 3.837   1.00  55.12 ? 243  ARG A NH1 1 
ATOM   1784 N NH2 . ARG A 1 243 ? 47.622  22.623 3.350   1.00  54.12 ? 243  ARG A NH2 1 
ATOM   1785 N N   . VAL A 1 244 ? 45.990  23.450 10.474  1.00  47.60 ? 244  VAL A N   1 
ATOM   1786 C CA  . VAL A 1 244 ? 44.786  22.808 10.993  1.00  46.94 ? 244  VAL A CA  1 
ATOM   1787 C C   . VAL A 1 244 ? 43.554  23.144 10.124  1.00  46.53 ? 244  VAL A C   1 
ATOM   1788 O O   . VAL A 1 244 ? 43.398  24.278 9.650   1.00  46.42 ? 244  VAL A O   1 
ATOM   1789 C CB  . VAL A 1 244 ? 44.582  23.147 12.500  1.00  46.86 ? 244  VAL A CB  1 
ATOM   1790 C CG1 . VAL A 1 244 ? 44.234  24.619 12.707  1.00  47.05 ? 244  VAL A CG1 1 
ATOM   1791 C CG2 . VAL A 1 244 ? 43.555  22.234 13.137  1.00  46.87 ? 244  VAL A CG2 1 
ATOM   1792 N N   . TYR A 1 245 ? 42.712  22.136 9.897   0.50  45.98 ? 245  TYR A N   1 
ATOM   1793 C CA  . TYR A 1 245 ? 41.443  22.289 9.186   0.50  45.49 ? 245  TYR A CA  1 
ATOM   1794 C C   . TYR A 1 245 ? 40.340  21.738 10.074  0.50  45.36 ? 245  TYR A C   1 
ATOM   1795 O O   . TYR A 1 245 ? 40.597  20.876 10.917  0.50  45.26 ? 245  TYR A O   1 
ATOM   1796 C CB  . TYR A 1 245 ? 41.447  21.481 7.889   0.50  45.37 ? 245  TYR A CB  1 
ATOM   1797 C CG  . TYR A 1 245 ? 42.133  22.115 6.702   0.50  44.68 ? 245  TYR A CG  1 
ATOM   1798 C CD1 . TYR A 1 245 ? 43.512  22.058 6.557   0.50  44.28 ? 245  TYR A CD1 1 
ATOM   1799 C CD2 . TYR A 1 245 ? 41.397  22.732 5.703   0.50  44.06 ? 245  TYR A CD2 1 
ATOM   1800 C CE1 . TYR A 1 245 ? 44.139  22.616 5.460   0.50  43.74 ? 245  TYR A CE1 1 
ATOM   1801 C CE2 . TYR A 1 245 ? 42.013  23.294 4.606   0.50  43.66 ? 245  TYR A CE2 1 
ATOM   1802 C CZ  . TYR A 1 245 ? 43.383  23.232 4.488   0.50  43.48 ? 245  TYR A CZ  1 
ATOM   1803 O OH  . TYR A 1 245 ? 43.995  23.794 3.395   0.50  43.17 ? 245  TYR A OH  1 
ATOM   1804 N N   . ALA A 1 246 ? 39.117  22.225 9.881   1.00  45.22 ? 246  ALA A N   1 
ATOM   1805 C CA  . ALA A 1 246 ? 37.967  21.700 10.608  1.00  45.24 ? 246  ALA A CA  1 
ATOM   1806 C C   . ALA A 1 246 ? 36.820  21.364 9.672   1.00  45.29 ? 246  ALA A C   1 
ATOM   1807 O O   . ALA A 1 246 ? 36.252  22.246 9.025   1.00  45.27 ? 246  ALA A O   1 
ATOM   1808 C CB  . ALA A 1 246 ? 37.510  22.680 11.676  1.00  45.20 ? 246  ALA A CB  1 
ATOM   1809 N N   . ILE A 1 247 ? 36.488  20.078 9.606   1.00  45.56 ? 247  ILE A N   1 
ATOM   1810 C CA  . ILE A 1 247 ? 35.327  19.619 8.846   1.00  45.87 ? 247  ILE A CA  1 
ATOM   1811 C C   . ILE A 1 247 ? 34.204  19.169 9.771   1.00  46.18 ? 247  ILE A C   1 
ATOM   1812 O O   . ILE A 1 247 ? 34.417  18.414 10.724  1.00  46.22 ? 247  ILE A O   1 
ATOM   1813 C CB  . ILE A 1 247 ? 35.691  18.509 7.852   1.00  45.75 ? 247  ILE A CB  1 
ATOM   1814 C CG1 . ILE A 1 247 ? 36.689  19.052 6.829   1.00  45.68 ? 247  ILE A CG1 1 
ATOM   1815 C CG2 . ILE A 1 247 ? 34.433  17.960 7.167   1.00  45.81 ? 247  ILE A CG2 1 
ATOM   1816 C CD1 . ILE A 1 247 ? 37.421  17.986 6.085   1.00  45.79 ? 247  ILE A CD1 1 
ATOM   1817 N N   . LEU A 1 248 ? 33.009  19.659 9.473   1.00  46.57 ? 248  LEU A N   1 
ATOM   1818 C CA  . LEU A 1 248 ? 31.837  19.383 10.266  1.00  47.28 ? 248  LEU A CA  1 
ATOM   1819 C C   . LEU A 1 248 ? 30.731  19.055 9.290   1.00  47.94 ? 248  LEU A C   1 
ATOM   1820 O O   . LEU A 1 248 ? 30.584  19.751 8.280   1.00  48.19 ? 248  LEU A O   1 
ATOM   1821 C CB  . LEU A 1 248 ? 31.453  20.623 11.070  1.00  47.18 ? 248  LEU A CB  1 
ATOM   1822 C CG  . LEU A 1 248 ? 32.591  21.422 11.706  1.00  47.13 ? 248  LEU A CG  1 
ATOM   1823 C CD1 . LEU A 1 248 ? 32.166  22.850 11.936  1.00  47.23 ? 248  LEU A CD1 1 
ATOM   1824 C CD2 . LEU A 1 248 ? 33.047  20.784 13.002  1.00  47.16 ? 248  LEU A CD2 1 
ATOM   1825 N N   . THR A 1 249 ? 29.962  18.001 9.564   1.00  48.47 ? 249  THR A N   1 
ATOM   1826 C CA  . THR A 1 249 ? 28.803  17.718 8.714   1.00  48.91 ? 249  THR A CA  1 
ATOM   1827 C C   . THR A 1 249 ? 27.621  18.636 9.063   1.00  49.46 ? 249  THR A C   1 
ATOM   1828 O O   . THR A 1 249 ? 26.898  19.088 8.167   1.00  49.46 ? 249  THR A O   1 
ATOM   1829 C CB  . THR A 1 249 ? 28.432  16.202 8.620   1.00  48.79 ? 249  THR A CB  1 
ATOM   1830 O OG1 . THR A 1 249 ? 27.024  16.052 8.375   1.00  48.39 ? 249  THR A OG1 1 
ATOM   1831 C CG2 . THR A 1 249 ? 28.815  15.452 9.879   1.00  48.73 ? 249  THR A CG2 1 
ATOM   1832 N N   . HIS A 1 250 ? 27.452  18.939 10.349  1.00  50.08 ? 250  HIS A N   1 
ATOM   1833 C CA  . HIS A 1 250 ? 26.393  19.853 10.780  1.00  50.76 ? 250  HIS A CA  1 
ATOM   1834 C C   . HIS A 1 250 ? 26.979  21.113 11.391  1.00  51.23 ? 250  HIS A C   1 
ATOM   1835 O O   . HIS A 1 250 ? 27.654  21.063 12.419  1.00  51.32 ? 250  HIS A O   1 
ATOM   1836 C CB  . HIS A 1 250 ? 25.423  19.175 11.752  1.00  50.68 ? 250  HIS A CB  1 
ATOM   1837 C CG  . HIS A 1 250 ? 24.830  17.911 11.219  1.00  51.26 ? 250  HIS A CG  1 
ATOM   1838 N ND1 . HIS A 1 250 ? 23.862  17.899 10.236  1.00  51.69 ? 250  HIS A ND1 1 
ATOM   1839 C CD2 . HIS A 1 250 ? 25.079  16.615 11.519  1.00  52.02 ? 250  HIS A CD2 1 
ATOM   1840 C CE1 . HIS A 1 250 ? 23.535  16.649 9.960   1.00  52.45 ? 250  HIS A CE1 1 
ATOM   1841 N NE2 . HIS A 1 250 ? 24.259  15.850 10.724  1.00  52.94 ? 250  HIS A NE2 1 
ATOM   1842 N N   . GLY A 1 251 ? 26.723  22.241 10.737  1.00  51.91 ? 251  GLY A N   1 
ATOM   1843 C CA  . GLY A 1 251 ? 27.231  23.531 11.192  1.00  52.81 ? 251  GLY A CA  1 
ATOM   1844 C C   . GLY A 1 251 ? 26.149  24.333 11.882  1.00  53.46 ? 251  GLY A C   1 
ATOM   1845 O O   . GLY A 1 251 ? 25.393  25.065 11.229  1.00  53.60 ? 251  GLY A O   1 
ATOM   1846 N N   . ILE A 1 252 ? 26.078  24.193 13.209  1.00  53.99 ? 252  ILE A N   1 
ATOM   1847 C CA  . ILE A 1 252 ? 25.030  24.869 13.977  1.00  54.56 ? 252  ILE A CA  1 
ATOM   1848 C C   . ILE A 1 252 ? 25.459  26.283 14.361  1.00  54.97 ? 252  ILE A C   1 
ATOM   1849 O O   . ILE A 1 252 ? 24.648  27.211 14.301  1.00  55.19 ? 252  ILE A O   1 
ATOM   1850 C CB  . ILE A 1 252 ? 24.561  24.037 15.203  1.00  54.56 ? 252  ILE A CB  1 
ATOM   1851 C CG1 . ILE A 1 252 ? 24.040  22.664 14.739  1.00  54.70 ? 252  ILE A CG1 1 
ATOM   1852 C CG2 . ILE A 1 252 ? 23.492  24.802 15.994  1.00  54.32 ? 252  ILE A CG2 1 
ATOM   1853 C CD1 . ILE A 1 252 ? 23.484  21.761 15.843  1.00  54.45 ? 252  ILE A CD1 1 
ATOM   1854 N N   . PHE A 1 253 ? 26.729  26.436 14.742  1.00  55.35 ? 253  PHE A N   1 
ATOM   1855 C CA  . PHE A 1 253 ? 27.363  27.752 14.928  1.00  55.72 ? 253  PHE A CA  1 
ATOM   1856 C C   . PHE A 1 253 ? 26.523  28.818 15.658  1.00  55.93 ? 253  PHE A C   1 
ATOM   1857 O O   . PHE A 1 253 ? 26.277  29.904 15.115  1.00  55.83 ? 253  PHE A O   1 
ATOM   1858 C CB  . PHE A 1 253 ? 27.801  28.332 13.576  1.00  55.77 ? 253  PHE A CB  1 
ATOM   1859 C CG  . PHE A 1 253 ? 28.777  27.481 12.815  1.00  55.95 ? 253  PHE A CG  1 
ATOM   1860 C CD1 . PHE A 1 253 ? 28.551  27.188 11.478  1.00  55.95 ? 253  PHE A CD1 1 
ATOM   1861 C CD2 . PHE A 1 253 ? 29.932  26.996 13.419  1.00  56.12 ? 253  PHE A CD2 1 
ATOM   1862 C CE1 . PHE A 1 253 ? 29.451  26.415 10.757  1.00  56.06 ? 253  PHE A CE1 1 
ATOM   1863 C CE2 . PHE A 1 253 ? 30.838  26.219 12.703  1.00  56.00 ? 253  PHE A CE2 1 
ATOM   1864 C CZ  . PHE A 1 253 ? 30.596  25.931 11.372  1.00  55.98 ? 253  PHE A CZ  1 
ATOM   1865 N N   . SER A 1 254 ? 26.096  28.520 16.880  1.00  56.30 ? 254  SER A N   1 
ATOM   1866 C CA  . SER A 1 254 ? 25.328  29.486 17.670  1.00  56.66 ? 254  SER A CA  1 
ATOM   1867 C C   . SER A 1 254 ? 26.192  30.177 18.726  1.00  56.73 ? 254  SER A C   1 
ATOM   1868 O O   . SER A 1 254 ? 27.256  29.676 19.092  1.00  56.83 ? 254  SER A O   1 
ATOM   1869 C CB  . SER A 1 254 ? 24.121  28.809 18.330  1.00  56.74 ? 254  SER A CB  1 
ATOM   1870 O OG  . SER A 1 254 ? 24.521  27.707 19.131  1.00  57.46 ? 254  SER A OG  1 
ATOM   1871 N N   . GLY A 1 255 ? 25.730  31.333 19.200  0.05  57.00 ? 255  GLY A N   1 
ATOM   1872 C CA  . GLY A 1 255 ? 26.365  32.042 20.316  0.05  57.31 ? 255  GLY A CA  1 
ATOM   1873 C C   . GLY A 1 255 ? 27.593  32.869 19.961  0.05  57.56 ? 255  GLY A C   1 
ATOM   1874 O O   . GLY A 1 255 ? 27.471  33.920 19.318  0.05  57.54 ? 255  GLY A O   1 
ATOM   1875 N N   . PRO A 1 256 ? 28.784  32.412 20.403  1.00  57.84 ? 256  PRO A N   1 
ATOM   1876 C CA  . PRO A 1 256 ? 30.074  33.030 20.082  1.00  57.96 ? 256  PRO A CA  1 
ATOM   1877 C C   . PRO A 1 256 ? 30.740  32.379 18.874  1.00  58.17 ? 256  PRO A C   1 
ATOM   1878 O O   . PRO A 1 256 ? 31.766  32.867 18.394  1.00  58.27 ? 256  PRO A O   1 
ATOM   1879 C CB  . PRO A 1 256 ? 30.904  32.748 21.336  1.00  57.88 ? 256  PRO A CB  1 
ATOM   1880 C CG  . PRO A 1 256 ? 30.385  31.435 21.836  1.00  57.79 ? 256  PRO A CG  1 
ATOM   1881 C CD  . PRO A 1 256 ? 28.934  31.334 21.405  1.00  57.89 ? 256  PRO A CD  1 
ATOM   1882 N N   . ALA A 1 257 ? 30.139  31.290 18.402  1.00  58.42 ? 257  ALA A N   1 
ATOM   1883 C CA  . ALA A 1 257 ? 30.724  30.401 17.403  1.00  58.74 ? 257  ALA A CA  1 
ATOM   1884 C C   . ALA A 1 257 ? 31.488  31.112 16.290  1.00  59.01 ? 257  ALA A C   1 
ATOM   1885 O O   . ALA A 1 257 ? 32.692  30.870 16.101  1.00  59.01 ? 257  ALA A O   1 
ATOM   1886 C CB  . ALA A 1 257 ? 29.651  29.514 16.814  1.00  58.75 ? 257  ALA A CB  1 
ATOM   1887 N N   . ILE A 1 258 ? 30.785  31.987 15.570  1.00  59.14 ? 258  ILE A N   1 
ATOM   1888 C CA  . ILE A 1 258 ? 31.329  32.641 14.380  1.00  59.34 ? 258  ILE A CA  1 
ATOM   1889 C C   . ILE A 1 258 ? 32.594  33.434 14.695  1.00  59.45 ? 258  ILE A C   1 
ATOM   1890 O O   . ILE A 1 258 ? 33.627  33.253 14.041  1.00  59.43 ? 258  ILE A O   1 
ATOM   1891 C CB  . ILE A 1 258 ? 30.262  33.524 13.687  1.00  59.41 ? 258  ILE A CB  1 
ATOM   1892 C CG1 . ILE A 1 258 ? 29.099  32.651 13.177  1.00  59.42 ? 258  ILE A CG1 1 
ATOM   1893 C CG2 . ILE A 1 258 ? 30.886  34.377 12.568  1.00  59.48 ? 258  ILE A CG2 1 
ATOM   1894 C CD1 . ILE A 1 258 ? 29.523  31.366 12.449  1.00  59.08 ? 258  ILE A CD1 1 
ATOM   1895 N N   . SER A 1 259 ? 32.502  34.294 15.709  1.00  59.59 ? 259  SER A N   1 
ATOM   1896 C CA  . SER A 1 259 ? 33.633  35.095 16.176  1.00  59.69 ? 259  SER A CA  1 
ATOM   1897 C C   . SER A 1 259 ? 34.791  34.230 16.662  1.00  59.62 ? 259  SER A C   1 
ATOM   1898 O O   . SER A 1 259 ? 35.951  34.538 16.377  1.00  59.61 ? 259  SER A O   1 
ATOM   1899 C CB  . SER A 1 259 ? 33.196  36.075 17.276  1.00  59.82 ? 259  SER A CB  1 
ATOM   1900 O OG  . SER A 1 259 ? 32.311  35.462 18.207  1.00  60.11 ? 259  SER A OG  1 
ATOM   1901 N N   . ARG A 1 260 ? 34.466  33.157 17.386  0.10  59.61 ? 260  ARG A N   1 
ATOM   1902 C CA  . ARG A 1 260 ? 35.457  32.205 17.897  0.10  59.63 ? 260  ARG A CA  1 
ATOM   1903 C C   . ARG A 1 260 ? 36.292  31.572 16.778  0.10  59.60 ? 260  ARG A C   1 
ATOM   1904 O O   . ARG A 1 260 ? 37.485  31.322 16.957  0.10  59.55 ? 260  ARG A O   1 
ATOM   1905 C CB  . ARG A 1 260 ? 34.782  31.116 18.746  0.10  59.66 ? 260  ARG A CB  1 
ATOM   1906 C CG  . ARG A 1 260 ? 34.590  31.466 20.225  0.10  59.86 ? 260  ARG A CG  1 
ATOM   1907 C CD  . ARG A 1 260 ? 33.821  30.361 20.960  0.10  60.28 ? 260  ARG A CD  1 
ATOM   1908 N NE  . ARG A 1 260 ? 33.936  30.453 22.418  0.10  60.64 ? 260  ARG A NE  1 
ATOM   1909 C CZ  . ARG A 1 260 ? 33.200  29.748 23.276  0.10  60.81 ? 260  ARG A CZ  1 
ATOM   1910 N NH1 . ARG A 1 260 ? 32.283  28.900 22.831  0.10  60.84 ? 260  ARG A NH1 1 
ATOM   1911 N NH2 . ARG A 1 260 ? 33.379  29.898 24.582  0.10  60.85 ? 260  ARG A NH2 1 
ATOM   1912 N N   . ILE A 1 261 ? 35.658  31.330 15.630  1.00  59.60 ? 261  ILE A N   1 
ATOM   1913 C CA  . ILE A 1 261 ? 36.331  30.781 14.441  1.00  59.70 ? 261  ILE A CA  1 
ATOM   1914 C C   . ILE A 1 261 ? 37.349  31.752 13.820  1.00  59.83 ? 261  ILE A C   1 
ATOM   1915 O O   . ILE A 1 261 ? 38.509  31.383 13.598  1.00  59.95 ? 261  ILE A O   1 
ATOM   1916 C CB  . ILE A 1 261 ? 35.305  30.297 13.379  1.00  59.65 ? 261  ILE A CB  1 
ATOM   1917 C CG1 . ILE A 1 261 ? 34.711  28.951 13.795  1.00  59.57 ? 261  ILE A CG1 1 
ATOM   1918 C CG2 . ILE A 1 261 ? 35.935  30.186 11.992  1.00  59.49 ? 261  ILE A CG2 1 
ATOM   1919 C CD1 . ILE A 1 261 ? 33.264  28.776 13.364  1.00  59.68 ? 261  ILE A CD1 1 
ATOM   1920 N N   . ASN A 1 262 ? 36.912  32.979 13.532  1.00  59.90 ? 262  ASN A N   1 
ATOM   1921 C CA  . ASN A 1 262 ? 37.805  34.036 13.041  1.00  59.94 ? 262  ASN A CA  1 
ATOM   1922 C C   . ASN A 1 262 ? 38.971  34.308 14.004  1.00  59.77 ? 262  ASN A C   1 
ATOM   1923 O O   . ASN A 1 262 ? 40.097  34.568 13.570  1.00  59.68 ? 262  ASN A O   1 
ATOM   1924 C CB  . ASN A 1 262 ? 37.016  35.322 12.775  1.00  60.10 ? 262  ASN A CB  1 
ATOM   1925 C CG  . ASN A 1 262 ? 35.902  35.123 11.761  1.00  60.78 ? 262  ASN A CG  1 
ATOM   1926 O OD1 . ASN A 1 262 ? 36.147  35.065 10.551  1.00  61.23 ? 262  ASN A OD1 1 
ATOM   1927 N ND2 . ASN A 1 262 ? 34.669  35.015 12.249  1.00  61.59 ? 262  ASN A ND2 1 
ATOM   1928 N N   . ASN A 1 263 ? 38.687  34.236 15.307  1.00  59.56 ? 263  ASN A N   1 
ATOM   1929 C CA  . ASN A 1 263 ? 39.711  34.326 16.354  1.00  59.29 ? 263  ASN A CA  1 
ATOM   1930 C C   . ASN A 1 263 ? 40.629  33.099 16.457  1.00  58.94 ? 263  ASN A C   1 
ATOM   1931 O O   . ASN A 1 263 ? 41.660  33.143 17.143  1.00  58.91 ? 263  ASN A O   1 
ATOM   1932 C CB  . ASN A 1 263 ? 39.064  34.613 17.715  1.00  59.44 ? 263  ASN A CB  1 
ATOM   1933 C CG  . ASN A 1 263 ? 38.755  36.088 17.920  1.00  59.67 ? 263  ASN A CG  1 
ATOM   1934 O OD1 . ASN A 1 263 ? 39.469  36.963 17.426  1.00  59.52 ? 263  ASN A OD1 1 
ATOM   1935 N ND2 . ASN A 1 263 ? 37.690  36.370 18.666  1.00  60.08 ? 263  ASN A ND2 1 
ATOM   1936 N N   . ALA A 1 264 ? 40.248  32.014 15.782  1.00  58.40 ? 264  ALA A N   1 
ATOM   1937 C CA  . ALA A 1 264 ? 41.065  30.803 15.726  1.00  57.75 ? 264  ALA A CA  1 
ATOM   1938 C C   . ALA A 1 264 ? 41.975  30.798 14.498  1.00  57.18 ? 264  ALA A C   1 
ATOM   1939 O O   . ALA A 1 264 ? 41.919  31.698 13.655  1.00  57.09 ? 264  ALA A O   1 
ATOM   1940 C CB  . ALA A 1 264 ? 40.182  29.555 15.753  1.00  57.78 ? 264  ALA A CB  1 
ATOM   1941 N N   . CYS A 1 265 ? 42.808  29.768 14.413  1.00  56.45 ? 265  CYS A N   1 
ATOM   1942 C CA  . CYS A 1 265 ? 43.807  29.636 13.365  1.00  55.73 ? 265  CYS A CA  1 
ATOM   1943 C C   . CYS A 1 265 ? 43.318  28.793 12.186  1.00  55.08 ? 265  CYS A C   1 
ATOM   1944 O O   . CYS A 1 265 ? 44.113  28.428 11.312  1.00  54.99 ? 265  CYS A O   1 
ATOM   1945 C CB  . CYS A 1 265 ? 45.064  29.005 13.961  1.00  55.81 ? 265  CYS A CB  1 
ATOM   1946 S SG  . CYS A 1 265 ? 44.709  27.525 14.957  1.00  56.12 ? 265  CYS A SG  1 
ATOM   1947 N N   . PHE A 1 266 ? 42.017  28.490 12.160  1.00  54.21 ? 266  PHE A N   1 
ATOM   1948 C CA  . PHE A 1 266 ? 41.443  27.616 11.127  1.00  53.42 ? 266  PHE A CA  1 
ATOM   1949 C C   . PHE A 1 266 ? 41.766  28.103 9.717   1.00  52.80 ? 266  PHE A C   1 
ATOM   1950 O O   . PHE A 1 266 ? 41.331  29.180 9.314   1.00  52.80 ? 266  PHE A O   1 
ATOM   1951 C CB  . PHE A 1 266 ? 39.920  27.448 11.297  1.00  53.40 ? 266  PHE A CB  1 
ATOM   1952 C CG  . PHE A 1 266 ? 39.523  26.582 12.468  1.00  53.51 ? 266  PHE A CG  1 
ATOM   1953 C CD1 . PHE A 1 266 ? 38.705  27.089 13.478  1.00  53.05 ? 266  PHE A CD1 1 
ATOM   1954 C CD2 . PHE A 1 266 ? 39.969  25.262 12.564  1.00  53.26 ? 266  PHE A CD2 1 
ATOM   1955 C CE1 . PHE A 1 266 ? 38.340  26.302 14.565  1.00  52.75 ? 266  PHE A CE1 1 
ATOM   1956 C CE2 . PHE A 1 266 ? 39.611  24.467 13.653  1.00  53.13 ? 266  PHE A CE2 1 
ATOM   1957 C CZ  . PHE A 1 266 ? 38.792  24.988 14.653  1.00  52.96 ? 266  PHE A CZ  1 
ATOM   1958 N N   . GLU A 1 267 ? 42.554  27.316 8.987   1.00  51.95 ? 267  GLU A N   1 
ATOM   1959 C CA  . GLU A 1 267 ? 42.844  27.579 7.577   1.00  51.11 ? 267  GLU A CA  1 
ATOM   1960 C C   . GLU A 1 267 ? 41.547  27.679 6.766   1.00  50.51 ? 267  GLU A C   1 
ATOM   1961 O O   . GLU A 1 267 ? 41.428  28.508 5.866   1.00  50.48 ? 267  GLU A O   1 
ATOM   1962 C CB  . GLU A 1 267 ? 43.733  26.466 7.020   1.00  51.23 ? 267  GLU A CB  1 
ATOM   1963 C CG  . GLU A 1 267 ? 43.977  26.522 5.515   1.00  51.60 ? 267  GLU A CG  1 
ATOM   1964 C CD  . GLU A 1 267 ? 44.920  27.634 5.097   1.00  52.24 ? 267  GLU A CD  1 
ATOM   1965 O OE1 . GLU A 1 267 ? 45.754  28.066 5.924   1.00  52.93 ? 267  GLU A OE1 1 
ATOM   1966 O OE2 . GLU A 1 267 ? 44.831  28.073 3.931   1.00  52.32 ? 267  GLU A OE2 1 
ATOM   1967 N N   . ALA A 1 268 ? 40.592  26.811 7.097   1.00  49.79 ? 268  ALA A N   1 
ATOM   1968 C CA  . ALA A 1 268 ? 39.238  26.836 6.549   1.00  49.07 ? 268  ALA A CA  1 
ATOM   1969 C C   . ALA A 1 268 ? 38.318  26.031 7.470   1.00  48.56 ? 268  ALA A C   1 
ATOM   1970 O O   . ALA A 1 268 ? 38.796  25.211 8.261   1.00  48.66 ? 268  ALA A O   1 
ATOM   1971 C CB  . ALA A 1 268 ? 39.224  26.251 5.143   1.00  49.18 ? 268  ALA A CB  1 
ATOM   1972 N N   . VAL A 1 269 ? 37.010  26.274 7.382   1.00  47.71 ? 269  VAL A N   1 
ATOM   1973 C CA  . VAL A 1 269 ? 36.034  25.444 8.084   1.00  46.97 ? 269  VAL A CA  1 
ATOM   1974 C C   . VAL A 1 269 ? 34.962  24.977 7.102   1.00  46.61 ? 269  VAL A C   1 
ATOM   1975 O O   . VAL A 1 269 ? 34.266  25.793 6.505   1.00  46.66 ? 269  VAL A O   1 
ATOM   1976 C CB  . VAL A 1 269 ? 35.407  26.172 9.295   1.00  46.96 ? 269  VAL A CB  1 
ATOM   1977 C CG1 . VAL A 1 269 ? 34.310  25.317 9.925   1.00  46.92 ? 269  VAL A CG1 1 
ATOM   1978 C CG2 . VAL A 1 269 ? 36.480  26.511 10.330  1.00  46.78 ? 269  VAL A CG2 1 
ATOM   1979 N N   . VAL A 1 270 ? 34.841  23.663 6.932   1.00  46.05 ? 270  VAL A N   1 
ATOM   1980 C CA  . VAL A 1 270 ? 33.923  23.103 5.942   1.00  45.62 ? 270  VAL A CA  1 
ATOM   1981 C C   . VAL A 1 270 ? 32.669  22.520 6.596   1.00  45.48 ? 270  VAL A C   1 
ATOM   1982 O O   . VAL A 1 270 ? 32.763  21.742 7.553   1.00  45.48 ? 270  VAL A O   1 
ATOM   1983 C CB  . VAL A 1 270 ? 34.612  22.026 5.076   1.00  45.62 ? 270  VAL A CB  1 
ATOM   1984 C CG1 . VAL A 1 270 ? 33.746  21.674 3.868   1.00  45.66 ? 270  VAL A CG1 1 
ATOM   1985 C CG2 . VAL A 1 270 ? 35.978  22.510 4.622   1.00  45.59 ? 270  VAL A CG2 1 
ATOM   1986 N N   . VAL A 1 271 ? 31.501  22.909 6.081   1.00  45.23 ? 271  VAL A N   1 
ATOM   1987 C CA  . VAL A 1 271 ? 30.222  22.348 6.531   1.00  44.92 ? 271  VAL A CA  1 
ATOM   1988 C C   . VAL A 1 271 ? 29.319  21.964 5.361   1.00  44.98 ? 271  VAL A C   1 
ATOM   1989 O O   . VAL A 1 271 ? 29.522  22.417 4.235   1.00  44.99 ? 271  VAL A O   1 
ATOM   1990 C CB  . VAL A 1 271 ? 29.462  23.294 7.487   1.00  44.73 ? 271  VAL A CB  1 
ATOM   1991 C CG1 . VAL A 1 271 ? 30.126  23.313 8.845   1.00  44.81 ? 271  VAL A CG1 1 
ATOM   1992 C CG2 . VAL A 1 271 ? 29.374  24.694 6.906   1.00  44.60 ? 271  VAL A CG2 1 
ATOM   1993 N N   . THR A 1 272 ? 28.347  21.098 5.630   1.00  45.01 ? 272  THR A N   1 
ATOM   1994 C CA  . THR A 1 272 ? 27.339  20.754 4.637   1.00  45.09 ? 272  THR A CA  1 
ATOM   1995 C C   . THR A 1 272 ? 26.103  21.573 4.937   1.00  45.14 ? 272  THR A C   1 
ATOM   1996 O O   . THR A 1 272 ? 25.788  21.820 6.100   1.00  45.24 ? 272  THR A O   1 
ATOM   1997 C CB  . THR A 1 272 ? 26.960  19.259 4.656   1.00  45.08 ? 272  THR A CB  1 
ATOM   1998 O OG1 . THR A 1 272 ? 25.933  19.031 5.636   1.00  45.57 ? 272  THR A OG1 1 
ATOM   1999 C CG2 . THR A 1 272 ? 28.173  18.382 4.956   1.00  45.12 ? 272  THR A CG2 1 
ATOM   2000 N N   . ASN A 1 273 ? 25.403  21.997 3.892   1.00  45.33 ? 273  ASN A N   1 
ATOM   2001 C CA  . ASN A 1 273 ? 24.198  22.793 4.077   1.00  45.44 ? 273  ASN A CA  1 
ATOM   2002 C C   . ASN A 1 273 ? 23.020  21.919 4.514   1.00  45.61 ? 273  ASN A C   1 
ATOM   2003 O O   . ASN A 1 273 ? 21.999  21.821 3.829   1.00  45.58 ? 273  ASN A O   1 
ATOM   2004 C CB  . ASN A 1 273 ? 23.893  23.653 2.835   1.00  45.38 ? 273  ASN A CB  1 
ATOM   2005 C CG  . ASN A 1 273 ? 23.349  22.847 1.659   1.00  45.15 ? 273  ASN A CG  1 
ATOM   2006 O OD1 . ASN A 1 273 ? 22.449  23.310 0.961   1.00  45.86 ? 273  ASN A OD1 1 
ATOM   2007 N ND2 . ASN A 1 273 ? 23.896  21.655 1.425   1.00  44.23 ? 273  ASN A ND2 1 
ATOM   2008 N N   . THR A 1 274 ? 23.200  21.264 5.664   1.00  45.94 ? 274  THR A N   1 
ATOM   2009 C CA  . THR A 1 274 ? 22.102  20.600 6.357   1.00  46.29 ? 274  THR A CA  1 
ATOM   2010 C C   . THR A 1 274 ? 21.428  21.672 7.208   1.00  46.53 ? 274  THR A C   1 
ATOM   2011 O O   . THR A 1 274 ? 20.288  21.515 7.644   1.00  46.46 ? 274  THR A O   1 
ATOM   2012 C CB  . THR A 1 274 ? 22.588  19.413 7.227   1.00  46.29 ? 274  THR A CB  1 
ATOM   2013 O OG1 . THR A 1 274 ? 23.649  19.838 8.091   1.00  46.52 ? 274  THR A OG1 1 
ATOM   2014 C CG2 . THR A 1 274 ? 23.086  18.260 6.354   1.00  46.27 ? 274  THR A CG2 1 
ATOM   2015 N N   . ILE A 1 275 ? 22.159  22.763 7.432   1.00  47.05 ? 275  ILE A N   1 
ATOM   2016 C CA  . ILE A 1 275 ? 21.639  23.967 8.076   1.00  47.68 ? 275  ILE A CA  1 
ATOM   2017 C C   . ILE A 1 275 ? 22.036  25.190 7.240   1.00  48.24 ? 275  ILE A C   1 
ATOM   2018 O O   . ILE A 1 275 ? 23.139  25.219 6.698   1.00  48.25 ? 275  ILE A O   1 
ATOM   2019 C CB  . ILE A 1 275 ? 22.164  24.104 9.528   1.00  47.66 ? 275  ILE A CB  1 
ATOM   2020 C CG1 . ILE A 1 275 ? 21.570  22.996 10.414  1.00  47.33 ? 275  ILE A CG1 1 
ATOM   2021 C CG2 . ILE A 1 275 ? 21.842  25.494 10.108  1.00  47.77 ? 275  ILE A CG2 1 
ATOM   2022 C CD1 . ILE A 1 275 ? 22.268  22.792 11.743  1.00  45.79 ? 275  ILE A CD1 1 
ATOM   2023 N N   . PRO A 1 276 ? 21.127  26.181 7.102   1.00  48.90 ? 276  PRO A N   1 
ATOM   2024 C CA  . PRO A 1 276 ? 21.454  27.425 6.391   1.00  49.49 ? 276  PRO A CA  1 
ATOM   2025 C C   . PRO A 1 276 ? 22.663  28.164 6.978   1.00  50.04 ? 276  PRO A C   1 
ATOM   2026 O O   . PRO A 1 276 ? 22.703  28.475 8.182   1.00  50.03 ? 276  PRO A O   1 
ATOM   2027 C CB  . PRO A 1 276 ? 20.191  28.270 6.562   1.00  49.51 ? 276  PRO A CB  1 
ATOM   2028 C CG  . PRO A 1 276 ? 19.123  27.295 6.717   1.00  49.31 ? 276  PRO A CG  1 
ATOM   2029 C CD  . PRO A 1 276 ? 19.698  26.125 7.453   1.00  48.97 ? 276  PRO A CD  1 
ATOM   2030 N N   . GLN A 1 277 ? 23.633  28.439 6.109   0.10  50.47 ? 277  GLN A N   1 
ATOM   2031 C CA  . GLN A 1 277 ? 24.901  29.038 6.508   0.10  50.94 ? 277  GLN A CA  1 
ATOM   2032 C C   . GLN A 1 277 ? 25.094  30.400 5.849   0.10  51.24 ? 277  GLN A C   1 
ATOM   2033 O O   . GLN A 1 277 ? 26.019  31.136 6.188   0.10  51.28 ? 277  GLN A O   1 
ATOM   2034 C CB  . GLN A 1 277 ? 26.062  28.117 6.123   0.10  50.92 ? 277  GLN A CB  1 
ATOM   2035 C CG  . GLN A 1 277 ? 25.857  26.655 6.485   0.10  50.94 ? 277  GLN A CG  1 
ATOM   2036 C CD  . GLN A 1 277 ? 25.891  26.413 7.980   0.10  50.92 ? 277  GLN A CD  1 
ATOM   2037 O OE1 . GLN A 1 277 ? 24.865  26.136 8.601   0.10  50.94 ? 277  GLN A OE1 1 
ATOM   2038 N NE2 . GLN A 1 277 ? 27.074  26.531 8.568   0.10  50.91 ? 277  GLN A NE2 1 
ATOM   2039 N N   . GLU A 1 278 ? 24.212  30.729 4.907   0.10  51.62 ? 278  GLU A N   1 
ATOM   2040 C CA  . GLU A 1 278 ? 24.329  31.954 4.106   0.10  51.96 ? 278  GLU A CA  1 
ATOM   2041 C C   . GLU A 1 278 ? 24.450  33.228 4.941   0.10  52.23 ? 278  GLU A C   1 
ATOM   2042 O O   . GLU A 1 278 ? 25.052  34.213 4.507   0.10  52.22 ? 278  GLU A O   1 
ATOM   2043 C CB  . GLU A 1 278 ? 23.157  32.062 3.126   0.10  51.94 ? 278  GLU A CB  1 
ATOM   2044 C CG  . GLU A 1 278 ? 23.022  30.867 2.188   0.10  51.93 ? 278  GLU A CG  1 
ATOM   2045 C CD  . GLU A 1 278 ? 22.446  29.641 2.873   0.10  51.91 ? 278  GLU A CD  1 
ATOM   2046 O OE1 . GLU A 1 278 ? 23.041  28.549 2.744   0.10  51.90 ? 278  GLU A OE1 1 
ATOM   2047 O OE2 . GLU A 1 278 ? 21.398  29.771 3.542   0.10  51.93 ? 278  GLU A OE2 1 
ATOM   2048 N N   . ASP A 1 279 ? 23.866  33.192 6.135   1.00  52.56 ? 279  ASP A N   1 
ATOM   2049 C CA  . ASP A 1 279 ? 23.964  34.273 7.115   1.00  53.12 ? 279  ASP A CA  1 
ATOM   2050 C C   . ASP A 1 279 ? 25.355  34.310 7.767   1.00  53.10 ? 279  ASP A C   1 
ATOM   2051 O O   . ASP A 1 279 ? 26.003  35.360 7.822   1.00  53.06 ? 279  ASP A O   1 
ATOM   2052 C CB  . ASP A 1 279 ? 22.870  34.095 8.187   1.00  53.31 ? 279  ASP A CB  1 
ATOM   2053 C CG  . ASP A 1 279 ? 22.634  35.355 9.019   1.00  54.25 ? 279  ASP A CG  1 
ATOM   2054 O OD1 . ASP A 1 279 ? 23.516  35.743 9.829   1.00  55.11 ? 279  ASP A OD1 1 
ATOM   2055 O OD2 . ASP A 1 279 ? 21.541  35.947 8.874   1.00  54.75 ? 279  ASP A OD2 1 
ATOM   2056 N N   . LYS A 1 280 ? 25.802  33.150 8.246   0.10  53.23 ? 280  LYS A N   1 
ATOM   2057 C CA  . LYS A 1 280 ? 27.046  33.022 9.009   0.10  53.37 ? 280  LYS A CA  1 
ATOM   2058 C C   . LYS A 1 280 ? 28.305  33.079 8.143   0.10  53.56 ? 280  LYS A C   1 
ATOM   2059 O O   . LYS A 1 280 ? 29.369  33.488 8.614   0.10  53.55 ? 280  LYS A O   1 
ATOM   2060 C CB  . LYS A 1 280 ? 27.019  31.727 9.818   0.10  53.31 ? 280  LYS A CB  1 
ATOM   2061 C CG  . LYS A 1 280 ? 25.812  31.617 10.732  0.10  53.20 ? 280  LYS A CG  1 
ATOM   2062 C CD  . LYS A 1 280 ? 25.696  30.233 11.337  0.10  53.03 ? 280  LYS A CD  1 
ATOM   2063 C CE  . LYS A 1 280 ? 24.487  30.134 12.252  0.10  52.94 ? 280  LYS A CE  1 
ATOM   2064 N NZ  . LYS A 1 280 ? 24.543  31.130 13.357  0.10  52.88 ? 280  LYS A NZ  1 
ATOM   2065 N N   . MET A 1 281 ? 28.174  32.647 6.890   1.00  53.85 ? 281  MET A N   1 
ATOM   2066 C CA  . MET A 1 281 ? 29.220  32.800 5.876   1.00  54.14 ? 281  MET A CA  1 
ATOM   2067 C C   . MET A 1 281 ? 29.677  34.252 5.726   1.00  53.99 ? 281  MET A C   1 
ATOM   2068 O O   . MET A 1 281 ? 30.873  34.533 5.690   1.00  54.05 ? 281  MET A O   1 
ATOM   2069 C CB  . MET A 1 281 ? 28.722  32.301 4.518   1.00  54.34 ? 281  MET A CB  1 
ATOM   2070 C CG  . MET A 1 281 ? 28.841  30.813 4.310   1.00  55.55 ? 281  MET A CG  1 
ATOM   2071 S SD  . MET A 1 281 ? 28.506  30.352 2.596   1.00  58.69 ? 281  MET A SD  1 
ATOM   2072 C CE  . MET A 1 281 ? 26.748  29.994 2.628   1.00  57.65 ? 281  MET A CE  1 
ATOM   2073 N N   . LYS A 1 282 ? 28.721  35.170 5.626   0.10  53.88 ? 282  LYS A N   1 
ATOM   2074 C CA  . LYS A 1 282 ? 29.037  36.583 5.445   0.10  53.76 ? 282  LYS A CA  1 
ATOM   2075 C C   . LYS A 1 282 ? 29.882  37.114 6.605   0.10  53.63 ? 282  LYS A C   1 
ATOM   2076 O O   . LYS A 1 282 ? 30.765  37.951 6.411   0.10  53.62 ? 282  LYS A O   1 
ATOM   2077 C CB  . LYS A 1 282 ? 27.757  37.405 5.269   0.10  53.80 ? 282  LYS A CB  1 
ATOM   2078 C CG  . LYS A 1 282 ? 26.999  37.088 3.983   0.10  53.84 ? 282  LYS A CG  1 
ATOM   2079 C CD  . LYS A 1 282 ? 25.848  38.058 3.750   0.10  53.90 ? 282  LYS A CD  1 
ATOM   2080 C CE  . LYS A 1 282 ? 25.215  37.844 2.381   0.10  53.89 ? 282  LYS A CE  1 
ATOM   2081 N NZ  . LYS A 1 282 ? 24.186  38.883 2.071   0.10  53.86 ? 282  LYS A NZ  1 
ATOM   2082 N N   . HIS A 1 283 ? 29.620  36.597 7.802   0.10  53.48 ? 283  HIS A N   1 
ATOM   2083 C CA  . HIS A 1 283 ? 30.351  37.004 8.995   0.10  53.33 ? 283  HIS A CA  1 
ATOM   2084 C C   . HIS A 1 283 ? 31.601  36.141 9.200   0.10  53.27 ? 283  HIS A C   1 
ATOM   2085 O O   . HIS A 1 283 ? 32.385  36.386 10.117  0.10  53.26 ? 283  HIS A O   1 
ATOM   2086 C CB  . HIS A 1 283 ? 29.440  36.928 10.224  0.10  53.31 ? 283  HIS A CB  1 
ATOM   2087 C CG  . HIS A 1 283 ? 29.419  38.182 11.043  0.10  53.23 ? 283  HIS A CG  1 
ATOM   2088 N ND1 . HIS A 1 283 ? 30.434  38.527 11.909  0.10  53.18 ? 283  HIS A ND1 1 
ATOM   2089 C CD2 . HIS A 1 283 ? 28.497  39.170 11.133  0.10  53.15 ? 283  HIS A CD2 1 
ATOM   2090 C CE1 . HIS A 1 283 ? 30.142  39.675 12.493  0.10  53.12 ? 283  HIS A CE1 1 
ATOM   2091 N NE2 . HIS A 1 283 ? 28.971  40.087 12.040  0.10  53.12 ? 283  HIS A NE2 1 
ATOM   2092 N N   . CYS A 1 284 ? 31.782  35.134 8.347   0.78  53.22 ? 284  CYS A N   1 
ATOM   2093 C CA  . CYS A 1 284 ? 32.994  34.305 8.386   0.78  53.15 ? 284  CYS A CA  1 
ATOM   2094 C C   . CYS A 1 284 ? 33.539  33.930 7.001   0.78  52.83 ? 284  CYS A C   1 
ATOM   2095 O O   . CYS A 1 284 ? 32.899  33.195 6.246   0.78  52.74 ? 284  CYS A O   1 
ATOM   2096 C CB  . CYS A 1 284 ? 32.771  33.040 9.217   0.78  53.28 ? 284  CYS A CB  1 
ATOM   2097 S SG  . CYS A 1 284 ? 34.183  31.900 9.148   0.78  54.42 ? 284  CYS A SG  1 
ATOM   2098 N N   . SER A 1 285 ? 34.746  34.414 6.707   1.00  52.59 ? 285  SER A N   1 
ATOM   2099 C CA  . SER A 1 285 ? 35.403  34.245 5.399   1.00  52.26 ? 285  SER A CA  1 
ATOM   2100 C C   . SER A 1 285 ? 35.839  32.815 5.068   1.00  51.80 ? 285  SER A C   1 
ATOM   2101 O O   . SER A 1 285 ? 35.626  32.339 3.948   1.00  51.66 ? 285  SER A O   1 
ATOM   2102 C CB  . SER A 1 285 ? 36.614  35.184 5.300   1.00  52.38 ? 285  SER A CB  1 
ATOM   2103 O OG  . SER A 1 285 ? 37.528  34.748 4.308   1.00  52.63 ? 285  SER A OG  1 
ATOM   2104 N N   . LYS A 1 286 ? 36.461  32.154 6.042   1.00  51.30 ? 286  LYS A N   1 
ATOM   2105 C CA  . LYS A 1 286 ? 37.047  30.821 5.855   1.00  50.88 ? 286  LYS A CA  1 
ATOM   2106 C C   . LYS A 1 286 ? 36.027  29.677 5.695   1.00  50.41 ? 286  LYS A C   1 
ATOM   2107 O O   . LYS A 1 286 ? 36.382  28.602 5.195   1.00  50.32 ? 286  LYS A O   1 
ATOM   2108 C CB  . LYS A 1 286 ? 38.049  30.506 6.981   1.00  50.94 ? 286  LYS A CB  1 
ATOM   2109 C CG  . LYS A 1 286 ? 37.544  30.844 8.387   1.00  51.29 ? 286  LYS A CG  1 
ATOM   2110 C CD  . LYS A 1 286 ? 38.573  30.552 9.472   1.00  52.02 ? 286  LYS A CD  1 
ATOM   2111 C CE  . LYS A 1 286 ? 39.571  31.697 9.662   1.00  52.39 ? 286  LYS A CE  1 
ATOM   2112 N NZ  . LYS A 1 286 ? 40.581  31.750 8.564   1.00  52.37 ? 286  LYS A NZ  1 
ATOM   2113 N N   . ILE A 1 287 ? 34.778  29.904 6.115   1.00  49.77 ? 287  ILE A N   1 
ATOM   2114 C CA  . ILE A 1 287 ? 33.722  28.889 5.984   1.00  49.33 ? 287  ILE A CA  1 
ATOM   2115 C C   . ILE A 1 287 ? 33.485  28.487 4.522   1.00  48.90 ? 287  ILE A C   1 
ATOM   2116 O O   . ILE A 1 287 ? 33.448  29.338 3.625   1.00  48.89 ? 287  ILE A O   1 
ATOM   2117 C CB  . ILE A 1 287 ? 32.381  29.316 6.670   1.00  49.43 ? 287  ILE A CB  1 
ATOM   2118 C CG1 . ILE A 1 287 ? 32.508  29.231 8.199   1.00  49.67 ? 287  ILE A CG1 1 
ATOM   2119 C CG2 . ILE A 1 287 ? 31.196  28.439 6.193   1.00  49.37 ? 287  ILE A CG2 1 
ATOM   2120 C CD1 . ILE A 1 287 ? 31.229  29.671 8.955   1.00  50.09 ? 287  ILE A CD1 1 
ATOM   2121 N N   . GLN A 1 288 ? 33.340  27.181 4.301   1.00  48.39 ? 288  GLN A N   1 
ATOM   2122 C CA  . GLN A 1 288 ? 33.117  26.626 2.975   1.00  47.99 ? 288  GLN A CA  1 
ATOM   2123 C C   . GLN A 1 288 ? 32.081  25.522 3.051   1.00  47.70 ? 288  GLN A C   1 
ATOM   2124 O O   . GLN A 1 288 ? 32.068  24.741 4.004   1.00  47.69 ? 288  GLN A O   1 
ATOM   2125 C CB  . GLN A 1 288 ? 34.412  26.054 2.416   1.00  48.03 ? 288  GLN A CB  1 
ATOM   2126 C CG  . GLN A 1 288 ? 35.398  27.092 1.930   1.00  48.51 ? 288  GLN A CG  1 
ATOM   2127 C CD  . GLN A 1 288 ? 36.372  26.522 0.918   1.00  49.34 ? 288  GLN A CD  1 
ATOM   2128 O OE1 . GLN A 1 288 ? 36.234  25.374 0.479   1.00  49.89 ? 288  GLN A OE1 1 
ATOM   2129 N NE2 . GLN A 1 288 ? 37.366  27.319 0.538   1.00  49.33 ? 288  GLN A NE2 1 
ATOM   2130 N N   . VAL A 1 289 ? 31.219  25.444 2.042   1.00  47.31 ? 289  VAL A N   1 
ATOM   2131 C CA  . VAL A 1 289 ? 30.096  24.517 2.106   1.00  46.93 ? 289  VAL A CA  1 
ATOM   2132 C C   . VAL A 1 289 ? 30.114  23.431 1.030   1.00  46.63 ? 289  VAL A C   1 
ATOM   2133 O O   . VAL A 1 289 ? 30.337  23.713 -0.152  1.00  46.60 ? 289  VAL A O   1 
ATOM   2134 C CB  . VAL A 1 289 ? 28.723  25.259 2.121   1.00  46.95 ? 289  VAL A CB  1 
ATOM   2135 C CG1 . VAL A 1 289 ? 28.711  26.361 3.186   1.00  46.77 ? 289  VAL A CG1 1 
ATOM   2136 C CG2 . VAL A 1 289 ? 28.397  25.845 0.753   1.00  47.27 ? 289  VAL A CG2 1 
ATOM   2137 N N   . ILE A 1 290 ? 29.900  22.189 1.464   1.00  46.26 ? 290  ILE A N   1 
ATOM   2138 C CA  . ILE A 1 290 ? 29.572  21.104 0.547   1.00  45.92 ? 290  ILE A CA  1 
ATOM   2139 C C   . ILE A 1 290 ? 28.050  21.067 0.390   1.00  45.61 ? 290  ILE A C   1 
ATOM   2140 O O   . ILE A 1 290 ? 27.313  21.055 1.376   1.00  45.75 ? 290  ILE A O   1 
ATOM   2141 C CB  . ILE A 1 290 ? 30.091  19.733 1.044   1.00  45.99 ? 290  ILE A CB  1 
ATOM   2142 C CG1 . ILE A 1 290 ? 31.623  19.733 1.140   1.00  46.17 ? 290  ILE A CG1 1 
ATOM   2143 C CG2 . ILE A 1 290 ? 29.608  18.613 0.119   1.00  45.94 ? 290  ILE A CG2 1 
ATOM   2144 C CD1 . ILE A 1 290 ? 32.222  18.458 1.759   1.00  46.37 ? 290  ILE A CD1 1 
ATOM   2145 N N   . ASP A 1 291 ? 27.589  21.064 -0.856  1.00  45.15 ? 291  ASP A N   1 
ATOM   2146 C CA  . ASP A 1 291 ? 26.162  21.048 -1.167  1.00  44.74 ? 291  ASP A CA  1 
ATOM   2147 C C   . ASP A 1 291 ? 25.642  19.613 -1.241  1.00  44.38 ? 291  ASP A C   1 
ATOM   2148 O O   . ASP A 1 291 ? 26.012  18.846 -2.133  1.00  44.42 ? 291  ASP A O   1 
ATOM   2149 C CB  . ASP A 1 291 ? 25.904  21.788 -2.487  1.00  44.85 ? 291  ASP A CB  1 
ATOM   2150 C CG  . ASP A 1 291 ? 24.453  21.698 -2.943  1.00  45.10 ? 291  ASP A CG  1 
ATOM   2151 O OD1 . ASP A 1 291 ? 23.556  22.043 -2.143  1.00  45.38 ? 291  ASP A OD1 1 
ATOM   2152 O OD2 . ASP A 1 291 ? 24.206  21.287 -4.104  1.00  45.29 ? 291  ASP A OD2 1 
ATOM   2153 N N   . ILE A 1 292 ? 24.775  19.257 -0.304  1.00  43.91 ? 292  ILE A N   1 
ATOM   2154 C CA  . ILE A 1 292 ? 24.325  17.874 -0.172  1.00  43.36 ? 292  ILE A CA  1 
ATOM   2155 C C   . ILE A 1 292 ? 22.915  17.625 -0.718  1.00  43.06 ? 292  ILE A C   1 
ATOM   2156 O O   . ILE A 1 292 ? 22.348  16.545 -0.525  1.00  43.17 ? 292  ILE A O   1 
ATOM   2157 C CB  . ILE A 1 292 ? 24.452  17.387 1.293   1.00  43.35 ? 292  ILE A CB  1 
ATOM   2158 C CG1 . ILE A 1 292 ? 23.792  18.365 2.276   1.00  43.13 ? 292  ILE A CG1 1 
ATOM   2159 C CG2 . ILE A 1 292 ? 25.914  17.231 1.655   1.00  43.42 ? 292  ILE A CG2 1 
ATOM   2160 C CD1 . ILE A 1 292 ? 22.301  18.188 2.455   1.00  42.41 ? 292  ILE A CD1 1 
ATOM   2161 N N   . SER A 1 293 ? 22.362  18.624 -1.402  1.00  42.56 ? 293  SER A N   1 
ATOM   2162 C CA  . SER A 1 293 ? 21.005  18.537 -1.923  1.00  42.10 ? 293  SER A CA  1 
ATOM   2163 C C   . SER A 1 293 ? 20.808  17.370 -2.899  1.00  41.72 ? 293  SER A C   1 
ATOM   2164 O O   . SER A 1 293 ? 19.851  16.611 -2.753  1.00  41.82 ? 293  SER A O   1 
ATOM   2165 C CB  . SER A 1 293 ? 20.580  19.864 -2.551  1.00  42.13 ? 293  SER A CB  1 
ATOM   2166 O OG  . SER A 1 293 ? 21.474  20.242 -3.579  1.00  42.22 ? 293  SER A OG  1 
ATOM   2167 N N   . MET A 1 294 ? 21.715  17.213 -3.866  0.73  41.14 ? 294  MET A N   1 
ATOM   2168 C CA  . MET A 1 294 ? 21.628  16.107 -4.840  0.73  40.57 ? 294  MET A CA  1 
ATOM   2169 C C   . MET A 1 294 ? 21.549  14.748 -4.147  0.73  39.59 ? 294  MET A C   1 
ATOM   2170 O O   . MET A 1 294 ? 20.857  13.849 -4.615  0.73  39.38 ? 294  MET A O   1 
ATOM   2171 C CB  . MET A 1 294 ? 22.782  16.165 -5.865  0.73  40.97 ? 294  MET A CB  1 
ATOM   2172 C CG  . MET A 1 294 ? 23.016  14.892 -6.735  0.73  42.45 ? 294  MET A CG  1 
ATOM   2173 S SD  . MET A 1 294 ? 21.681  14.292 -7.833  0.73  45.20 ? 294  MET A SD  1 
ATOM   2174 C CE  . MET A 1 294 ? 21.605  15.580 -9.087  0.73  44.35 ? 294  MET A CE  1 
ATOM   2175 N N   . ILE A 1 295 ? 22.246  14.628 -3.020  1.00  38.53 ? 295  ILE A N   1 
ATOM   2176 C CA  . ILE A 1 295 ? 22.267  13.405 -2.222  1.00  37.49 ? 295  ILE A CA  1 
ATOM   2177 C C   . ILE A 1 295 ? 20.931  13.198 -1.522  1.00  36.79 ? 295  ILE A C   1 
ATOM   2178 O O   . ILE A 1 295 ? 20.484  12.064 -1.350  1.00  36.71 ? 295  ILE A O   1 
ATOM   2179 C CB  . ILE A 1 295 ? 23.415  13.423 -1.190  1.00  37.45 ? 295  ILE A CB  1 
ATOM   2180 C CG1 . ILE A 1 295 ? 24.761  13.619 -1.895  1.00  37.54 ? 295  ILE A CG1 1 
ATOM   2181 C CG2 . ILE A 1 295 ? 23.448  12.134 -0.398  1.00  37.60 ? 295  ILE A CG2 1 
ATOM   2182 C CD1 . ILE A 1 295 ? 25.855  14.196 -0.999  1.00  37.57 ? 295  ILE A CD1 1 
ATOM   2183 N N   . LEU A 1 296 ? 20.292  14.293 -1.124  1.00  35.96 ? 296  LEU A N   1 
ATOM   2184 C CA  . LEU A 1 296 ? 18.973  14.205 -0.507  1.00  35.07 ? 296  LEU A CA  1 
ATOM   2185 C C   . LEU A 1 296 ? 17.902  13.977 -1.567  1.00  34.54 ? 296  LEU A C   1 
ATOM   2186 O O   . LEU A 1 296 ? 16.946  13.241 -1.332  1.00  34.39 ? 296  LEU A O   1 
ATOM   2187 C CB  . LEU A 1 296 ? 18.658  15.451 0.330   1.00  34.98 ? 296  LEU A CB  1 
ATOM   2188 C CG  . LEU A 1 296 ? 19.522  15.769 1.560   1.00  34.54 ? 296  LEU A CG  1 
ATOM   2189 C CD1 . LEU A 1 296 ? 18.924  16.961 2.296   1.00  34.23 ? 296  LEU A CD1 1 
ATOM   2190 C CD2 . LEU A 1 296 ? 19.615  14.575 2.505   1.00  33.82 ? 296  LEU A CD2 1 
ATOM   2191 N N   . ALA A 1 297 ? 18.085  14.597 -2.735  1.00  33.91 ? 297  ALA A N   1 
ATOM   2192 C CA  . ALA A 1 297 ? 17.139  14.486 -3.846  1.00  33.35 ? 297  ALA A CA  1 
ATOM   2193 C C   . ALA A 1 297 ? 17.120  13.070 -4.419  1.00  33.14 ? 297  ALA A C   1 
ATOM   2194 O O   . ALA A 1 297 ? 16.050  12.510 -4.705  1.00  32.96 ? 297  ALA A O   1 
ATOM   2195 C CB  . ALA A 1 297 ? 17.467  15.502 -4.927  1.00  33.05 ? 297  ALA A CB  1 
ATOM   2196 N N   . GLU A 1 298 ? 18.316  12.504 -4.566  0.99  32.94 ? 298  GLU A N   1 
ATOM   2197 C CA  . GLU A 1 298 ? 18.516  11.144 -5.059  0.99  32.75 ? 298  GLU A CA  1 
ATOM   2198 C C   . GLU A 1 298 ? 17.865  10.145 -4.113  0.99  32.16 ? 298  GLU A C   1 
ATOM   2199 O O   . GLU A 1 298 ? 17.123  9.259  -4.536  0.99  32.08 ? 298  GLU A O   1 
ATOM   2200 C CB  . GLU A 1 298 ? 20.019  10.860 -5.207  0.99  32.99 ? 298  GLU A CB  1 
ATOM   2201 C CG  . GLU A 1 298 ? 20.393  9.715  -6.155  0.99  34.41 ? 298  GLU A CG  1 
ATOM   2202 C CD  . GLU A 1 298 ? 20.098  9.998  -7.635  0.99  35.85 ? 298  GLU A CD  1 
ATOM   2203 O OE1 . GLU A 1 298 ? 19.908  11.171 -8.023  0.99  36.43 ? 298  GLU A OE1 1 
ATOM   2204 O OE2 . GLU A 1 298 ? 20.054  9.032  -8.423  0.99  36.50 ? 298  GLU A OE2 1 
ATOM   2205 N N   . ALA A 1 299 ? 18.118  10.324 -2.821  1.00  31.67 ? 299  ALA A N   1 
ATOM   2206 C CA  . ALA A 1 299 ? 17.539  9.467  -1.790  1.00  31.25 ? 299  ALA A CA  1 
ATOM   2207 C C   . ALA A 1 299 ? 16.021  9.581  -1.706  1.00  30.93 ? 299  ALA A C   1 
ATOM   2208 O O   . ALA A 1 299 ? 15.354  8.661  -1.239  1.00  30.84 ? 299  ALA A O   1 
ATOM   2209 C CB  . ALA A 1 299 ? 18.165  9.772  -0.440  1.00  31.28 ? 299  ALA A CB  1 
ATOM   2210 N N   . ILE A 1 300 ? 15.484  10.714 -2.151  1.00  30.77 ? 300  ILE A N   1 
ATOM   2211 C CA  . ILE A 1 300 ? 14.035  10.910 -2.214  1.00  30.48 ? 300  ILE A CA  1 
ATOM   2212 C C   . ILE A 1 300 ? 13.457  10.147 -3.405  1.00  30.25 ? 300  ILE A C   1 
ATOM   2213 O O   . ILE A 1 300 ? 12.471  9.419  -3.260  1.00  30.19 ? 300  ILE A O   1 
ATOM   2214 C CB  . ILE A 1 300 ? 13.651  12.417 -2.277  1.00  30.49 ? 300  ILE A CB  1 
ATOM   2215 C CG1 . ILE A 1 300 ? 13.839  13.065 -0.909  1.00  30.26 ? 300  ILE A CG1 1 
ATOM   2216 C CG2 . ILE A 1 300 ? 12.197  12.608 -2.722  1.00  30.65 ? 300  ILE A CG2 1 
ATOM   2217 C CD1 . ILE A 1 300 ? 14.007  14.588 -0.977  1.00  29.92 ? 300  ILE A CD1 1 
ATOM   2218 N N   . ARG A 1 301 ? 14.075  10.309 -4.573  0.98  30.00 ? 301  ARG A N   1 
ATOM   2219 C CA  . ARG A 1 301 ? 13.629  9.596  -5.765  0.98  29.96 ? 301  ARG A CA  1 
ATOM   2220 C C   . ARG A 1 301 ? 13.741  8.081  -5.595  0.98  29.69 ? 301  ARG A C   1 
ATOM   2221 O O   . ARG A 1 301 ? 12.804  7.345  -5.906  0.98  29.43 ? 301  ARG A O   1 
ATOM   2222 C CB  . ARG A 1 301 ? 14.427  10.032 -6.994  0.98  30.24 ? 301  ARG A CB  1 
ATOM   2223 C CG  . ARG A 1 301 ? 13.760  9.664  -8.313  0.98  30.92 ? 301  ARG A CG  1 
ATOM   2224 C CD  . ARG A 1 301 ? 14.559  10.146 -9.509  0.98  32.50 ? 301  ARG A CD  1 
ATOM   2225 N NE  . ARG A 1 301 ? 15.431  9.110  -10.067 0.98  33.63 ? 301  ARG A NE  1 
ATOM   2226 C CZ  . ARG A 1 301 ? 16.754  9.057  -9.914  0.98  34.76 ? 301  ARG A CZ  1 
ATOM   2227 N NH1 . ARG A 1 301 ? 17.402  9.984  -9.206  0.98  34.61 ? 301  ARG A NH1 1 
ATOM   2228 N NH2 . ARG A 1 301 ? 17.436  8.066  -10.482 0.98  35.37 ? 301  ARG A NH2 1 
ATOM   2229 N N   . ARG A 1 302 ? 14.889  7.628  -5.094  0.50  29.49 ? 302  ARG A N   1 
ATOM   2230 C CA  . ARG A 1 302 ? 15.176  6.200  -4.970  0.50  29.34 ? 302  ARG A CA  1 
ATOM   2231 C C   . ARG A 1 302 ? 14.280  5.500  -3.951  0.50  29.41 ? 302  ARG A C   1 
ATOM   2232 O O   . ARG A 1 302 ? 13.908  4.341  -4.133  0.50  29.37 ? 302  ARG A O   1 
ATOM   2233 C CB  . ARG A 1 302 ? 16.659  5.985  -4.680  0.50  29.17 ? 302  ARG A CB  1 
ATOM   2234 C CG  . ARG A 1 302 ? 17.519  6.465  -5.835  0.50  29.16 ? 302  ARG A CG  1 
ATOM   2235 C CD  . ARG A 1 302 ? 19.008  6.344  -5.581  0.50  29.25 ? 302  ARG A CD  1 
ATOM   2236 N NE  . ARG A 1 302 ? 19.743  6.454  -6.837  0.50  28.95 ? 302  ARG A NE  1 
ATOM   2237 C CZ  . ARG A 1 302 ? 20.328  5.431  -7.454  0.50  29.16 ? 302  ARG A CZ  1 
ATOM   2238 N NH1 . ARG A 1 302 ? 20.291  4.218  -6.920  0.50  29.19 ? 302  ARG A NH1 1 
ATOM   2239 N NH2 . ARG A 1 302 ? 20.969  5.623  -8.599  0.50  29.11 ? 302  ARG A NH2 1 
ATOM   2240 N N   . THR A 1 303 ? 13.923  6.224  -2.895  1.00  29.63 ? 303  THR A N   1 
ATOM   2241 C CA  . THR A 1 303 ? 12.920  5.771  -1.943  1.00  29.98 ? 303  THR A CA  1 
ATOM   2242 C C   . THR A 1 303 ? 11.587  5.589  -2.652  1.00  30.38 ? 303  THR A C   1 
ATOM   2243 O O   . THR A 1 303 ? 10.927  4.549  -2.505  1.00  30.39 ? 303  THR A O   1 
ATOM   2244 C CB  . THR A 1 303 ? 12.746  6.791  -0.810  1.00  29.95 ? 303  THR A CB  1 
ATOM   2245 O OG1 . THR A 1 303 ? 13.889  6.732  0.051   1.00  30.26 ? 303  THR A OG1 1 
ATOM   2246 C CG2 . THR A 1 303 ? 11.479  6.504  0.007   1.00  29.92 ? 303  THR A CG2 1 
ATOM   2247 N N   . HIS A 1 304 ? 11.208  6.606  -3.426  1.00  30.80 ? 304  HIS A N   1 
ATOM   2248 C CA  . HIS A 1 304 ? 9.926   6.627  -4.114  1.00  31.19 ? 304  HIS A CA  1 
ATOM   2249 C C   . HIS A 1 304 ? 9.852   5.531  -5.152  1.00  31.56 ? 304  HIS A C   1 
ATOM   2250 O O   . HIS A 1 304 ? 8.849   4.832  -5.237  1.00  31.65 ? 304  HIS A O   1 
ATOM   2251 C CB  . HIS A 1 304 ? 9.690   7.978  -4.781  1.00  31.21 ? 304  HIS A CB  1 
ATOM   2252 C CG  . HIS A 1 304 ? 8.433   8.039  -5.586  1.00  31.95 ? 304  HIS A CG  1 
ATOM   2253 N ND1 . HIS A 1 304 ? 7.196   7.764  -5.041  1.00  32.84 ? 304  HIS A ND1 1 
ATOM   2254 C CD2 . HIS A 1 304 ? 8.216   8.357  -6.888  1.00  32.79 ? 304  HIS A CD2 1 
ATOM   2255 C CE1 . HIS A 1 304 ? 6.270   7.902  -5.973  1.00  33.84 ? 304  HIS A CE1 1 
ATOM   2256 N NE2 . HIS A 1 304 ? 6.862   8.264  -7.103  1.00  33.99 ? 304  HIS A NE2 1 
ATOM   2257 N N   . ASN A 1 305 ? 10.924  5.381  -5.927  1.00  32.21 ? 305  ASN A N   1 
ATOM   2258 C CA  . ASN A 1 305 ? 10.933  4.471  -7.074  1.00  32.78 ? 305  ASN A CA  1 
ATOM   2259 C C   . ASN A 1 305 ? 11.144  3.004  -6.709  1.00  33.22 ? 305  ASN A C   1 
ATOM   2260 O O   . ASN A 1 305 ? 10.894  2.117  -7.532  1.00  33.31 ? 305  ASN A O   1 
ATOM   2261 C CB  . ASN A 1 305 ? 11.978  4.915  -8.105  1.00  32.71 ? 305  ASN A CB  1 
ATOM   2262 C CG  . ASN A 1 305 ? 11.710  6.308  -8.659  1.00  32.80 ? 305  ASN A CG  1 
ATOM   2263 O OD1 . ASN A 1 305 ? 10.653  6.902  -8.432  1.00  32.75 ? 305  ASN A OD1 1 
ATOM   2264 N ND2 . ASN A 1 305 ? 12.677  6.834  -9.395  1.00  33.12 ? 305  ASN A ND2 1 
ATOM   2265 N N   . GLY A 1 306 ? 11.588  2.754  -5.478  1.00  33.80 ? 306  GLY A N   1 
ATOM   2266 C CA  . GLY A 1 306 ? 11.990  1.412  -5.056  1.00  34.60 ? 306  GLY A CA  1 
ATOM   2267 C C   . GLY A 1 306 ? 13.415  1.142  -5.497  1.00  35.20 ? 306  GLY A C   1 
ATOM   2268 O O   . GLY A 1 306 ? 13.858  -0.006 -5.538  1.00  35.26 ? 306  GLY A O   1 
ATOM   2269 N N   . GLU A 1 307 ? 14.124  2.219  -5.829  1.00  35.86 ? 307  GLU A N   1 
ATOM   2270 C CA  . GLU A 1 307 ? 15.497  2.151  -6.308  1.00  36.71 ? 307  GLU A CA  1 
ATOM   2271 C C   . GLU A 1 307 ? 16.460  2.089  -5.114  1.00  36.96 ? 307  GLU A C   1 
ATOM   2272 O O   . GLU A 1 307 ? 16.138  2.571  -4.025  1.00  37.24 ? 307  GLU A O   1 
ATOM   2273 C CB  . GLU A 1 307 ? 15.782  3.351  -7.224  1.00  36.73 ? 307  GLU A CB  1 
ATOM   2274 C CG  . GLU A 1 307 ? 17.228  3.511  -7.695  1.00  38.05 ? 307  GLU A CG  1 
ATOM   2275 C CD  . GLU A 1 307 ? 17.586  2.656  -8.900  1.00  40.01 ? 307  GLU A CD  1 
ATOM   2276 O OE1 . GLU A 1 307 ? 17.326  1.431  -8.888  1.00  40.89 ? 307  GLU A OE1 1 
ATOM   2277 O OE2 . GLU A 1 307 ? 18.158  3.212  -9.864  1.00  40.87 ? 307  GLU A OE2 1 
ATOM   2278 N N   . SER A 1 308 ? 17.630  1.484  -5.317  1.00  37.09 ? 308  SER A N   1 
ATOM   2279 C CA  . SER A 1 308 ? 18.604  1.289  -4.243  1.00  37.08 ? 308  SER A CA  1 
ATOM   2280 C C   . SER A 1 308 ? 19.171  2.604  -3.688  1.00  36.99 ? 308  SER A C   1 
ATOM   2281 O O   . SER A 1 308 ? 19.942  3.306  -4.357  1.00  37.05 ? 308  SER A O   1 
ATOM   2282 C CB  . SER A 1 308 ? 19.727  0.349  -4.704  1.00  37.20 ? 308  SER A CB  1 
ATOM   2283 O OG  . SER A 1 308 ? 20.626  0.048  -3.648  1.00  37.20 ? 308  SER A OG  1 
ATOM   2284 N N   . VAL A 1 309 ? 18.787  2.923  -2.456  1.00  36.81 ? 309  VAL A N   1 
ATOM   2285 C CA  . VAL A 1 309 ? 19.275  4.124  -1.778  1.00  36.91 ? 309  VAL A CA  1 
ATOM   2286 C C   . VAL A 1 309 ? 20.704  3.957  -1.246  1.00  36.89 ? 309  VAL A C   1 
ATOM   2287 O O   . VAL A 1 309 ? 21.516  4.880  -1.348  1.00  37.01 ? 309  VAL A O   1 
ATOM   2288 C CB  . VAL A 1 309 ? 18.335  4.563  -0.621  1.00  36.88 ? 309  VAL A CB  1 
ATOM   2289 C CG1 . VAL A 1 309 ? 18.797  5.893  -0.019  1.00  36.77 ? 309  VAL A CG1 1 
ATOM   2290 C CG2 . VAL A 1 309 ? 16.904  4.692  -1.112  1.00  37.08 ? 309  VAL A CG2 1 
ATOM   2291 N N   . SER A 1 310 ? 21.002  2.781  -0.690  0.010 36.72 ? 310  SER A N   1 
ATOM   2292 C CA  . SER A 1 310 ? 22.273  2.518  0.004   0.010 36.55 ? 310  SER A CA  1 
ATOM   2293 C C   . SER A 1 310 ? 23.520  2.778  -0.842  0.010 36.41 ? 310  SER A C   1 
ATOM   2294 O O   . SER A 1 310 ? 24.598  3.036  -0.306  0.010 36.40 ? 310  SER A O   1 
ATOM   2295 C CB  . SER A 1 310 ? 22.310  1.087  0.546   0.010 36.56 ? 310  SER A CB  1 
ATOM   2296 O OG  . SER A 1 310 ? 22.440  0.147  -0.507  0.010 36.55 ? 310  SER A OG  1 
ATOM   2297 N N   . TYR A 1 311 ? 23.368  2.708  -2.160  0.20  36.24 ? 311  TYR A N   1 
ATOM   2298 C CA  . TYR A 1 311 ? 24.459  3.021  -3.083  0.20  36.07 ? 311  TYR A CA  1 
ATOM   2299 C C   . TYR A 1 311 ? 25.094  4.378  -2.786  0.20  35.92 ? 311  TYR A C   1 
ATOM   2300 O O   . TYR A 1 311 ? 26.311  4.540  -2.900  0.20  35.91 ? 311  TYR A O   1 
ATOM   2301 C CB  . TYR A 1 311 ? 23.958  2.986  -4.528  0.20  36.10 ? 311  TYR A CB  1 
ATOM   2302 C CG  . TYR A 1 311 ? 24.821  3.772  -5.490  0.20  36.11 ? 311  TYR A CG  1 
ATOM   2303 C CD1 . TYR A 1 311 ? 26.178  3.503  -5.611  0.20  36.14 ? 311  TYR A CD1 1 
ATOM   2304 C CD2 . TYR A 1 311 ? 24.278  4.777  -6.281  0.20  36.06 ? 311  TYR A CD2 1 
ATOM   2305 C CE1 . TYR A 1 311 ? 26.972  4.215  -6.488  0.20  36.11 ? 311  TYR A CE1 1 
ATOM   2306 C CE2 . TYR A 1 311 ? 25.065  5.495  -7.162  0.20  36.03 ? 311  TYR A CE2 1 
ATOM   2307 C CZ  . TYR A 1 311 ? 26.412  5.209  -7.261  0.20  36.10 ? 311  TYR A CZ  1 
ATOM   2308 O OH  . TYR A 1 311 ? 27.206  5.916  -8.134  0.20  36.10 ? 311  TYR A OH  1 
ATOM   2309 N N   . LEU A 1 312 ? 24.252  5.343  -2.420  1.00  35.70 ? 312  LEU A N   1 
ATOM   2310 C CA  . LEU A 1 312 ? 24.672  6.695  -2.051  1.00  35.66 ? 312  LEU A CA  1 
ATOM   2311 C C   . LEU A 1 312 ? 25.521  6.746  -0.786  1.00  35.55 ? 312  LEU A C   1 
ATOM   2312 O O   . LEU A 1 312 ? 26.193  7.750  -0.537  1.00  35.61 ? 312  LEU A O   1 
ATOM   2313 C CB  . LEU A 1 312 ? 23.456  7.603  -1.855  1.00  35.71 ? 312  LEU A CB  1 
ATOM   2314 C CG  . LEU A 1 312 ? 22.525  7.869  -3.041  1.00  36.15 ? 312  LEU A CG  1 
ATOM   2315 C CD1 . LEU A 1 312 ? 21.303  8.645  -2.560  1.00  36.07 ? 312  LEU A CD1 1 
ATOM   2316 C CD2 . LEU A 1 312 ? 23.256  8.626  -4.157  1.00  35.79 ? 312  LEU A CD2 1 
ATOM   2317 N N   . PHE A 1 313 ? 25.472  5.678  0.012   0.40  35.37 ? 313  PHE A N   1 
ATOM   2318 C CA  . PHE A 1 313 ? 26.300  5.567  1.213   0.40  35.22 ? 313  PHE A CA  1 
ATOM   2319 C C   . PHE A 1 313 ? 27.783  5.584  0.852   0.40  35.17 ? 313  PHE A C   1 
ATOM   2320 O O   . PHE A 1 313 ? 28.541  6.422  1.341   0.40  35.12 ? 313  PHE A O   1 
ATOM   2321 C CB  . PHE A 1 313 ? 25.987  4.285  1.989   0.40  35.21 ? 313  PHE A CB  1 
ATOM   2322 C CG  . PHE A 1 313 ? 24.557  4.168  2.440   0.40  34.88 ? 313  PHE A CG  1 
ATOM   2323 C CD1 . PHE A 1 313 ? 24.027  2.929  2.770   0.40  34.61 ? 313  PHE A CD1 1 
ATOM   2324 C CD2 . PHE A 1 313 ? 23.743  5.283  2.527   0.40  34.52 ? 313  PHE A CD2 1 
ATOM   2325 C CE1 . PHE A 1 313 ? 22.717  2.807  3.187   0.40  34.35 ? 313  PHE A CE1 1 
ATOM   2326 C CE2 . PHE A 1 313 ? 22.429  5.165  2.944   0.40  34.39 ? 313  PHE A CE2 1 
ATOM   2327 C CZ  . PHE A 1 313 ? 21.916  3.927  3.273   0.40  34.24 ? 313  PHE A CZ  1 
ATOM   2328 N N   . ASN B 1 3   ? 5.435   10.274 49.063  0.40  27.60 ? 3    ASN B N   1 
ATOM   2329 C CA  . ASN B 1 3   ? 5.037   9.614  47.787  0.40  27.75 ? 3    ASN B CA  1 
ATOM   2330 C C   . ASN B 1 3   ? 4.762   10.634 46.684  0.40  27.89 ? 3    ASN B C   1 
ATOM   2331 O O   . ASN B 1 3   ? 4.982   10.357 45.508  0.40  27.84 ? 3    ASN B O   1 
ATOM   2332 C CB  . ASN B 1 3   ? 3.809   8.725  48.008  0.40  27.70 ? 3    ASN B CB  1 
ATOM   2333 C CG  . ASN B 1 3   ? 3.876   7.426  47.222  0.40  27.67 ? 3    ASN B CG  1 
ATOM   2334 O OD1 . ASN B 1 3   ? 3.136   6.481  47.497  0.40  28.12 ? 3    ASN B OD1 1 
ATOM   2335 N ND2 . ASN B 1 3   ? 4.770   7.371  46.243  0.40  27.40 ? 3    ASN B ND2 1 
ATOM   2336 N N   . ILE B 1 4   ? 4.300   11.818 47.082  1.00  28.24 ? 4    ILE B N   1 
ATOM   2337 C CA  . ILE B 1 4   ? 3.924   12.890 46.152  1.00  28.36 ? 4    ILE B CA  1 
ATOM   2338 C C   . ILE B 1 4   ? 5.095   13.845 45.884  1.00  28.26 ? 4    ILE B C   1 
ATOM   2339 O O   . ILE B 1 4   ? 5.739   14.329 46.813  1.00  28.21 ? 4    ILE B O   1 
ATOM   2340 C CB  . ILE B 1 4   ? 2.686   13.662 46.701  1.00  28.39 ? 4    ILE B CB  1 
ATOM   2341 C CG1 . ILE B 1 4   ? 1.922   14.406 45.585  1.00  28.64 ? 4    ILE B CG1 1 
ATOM   2342 C CG2 . ILE B 1 4   ? 3.060   14.527 47.908  1.00  28.94 ? 4    ILE B CG2 1 
ATOM   2343 C CD1 . ILE B 1 4   ? 2.425   15.810 45.241  1.00  27.89 ? 4    ILE B CD1 1 
ATOM   2344 N N   . LYS B 1 5   ? 5.378   14.097 44.612  0.20  28.39 ? 5    LYS B N   1 
ATOM   2345 C CA  . LYS B 1 5   ? 6.441   15.024 44.257  0.20  28.55 ? 5    LYS B CA  1 
ATOM   2346 C C   . LYS B 1 5   ? 5.966   15.963 43.167  0.20  28.77 ? 5    LYS B C   1 
ATOM   2347 O O   . LYS B 1 5   ? 5.470   15.519 42.134  0.20  28.73 ? 5    LYS B O   1 
ATOM   2348 C CB  . LYS B 1 5   ? 7.694   14.273 43.805  0.20  28.53 ? 5    LYS B CB  1 
ATOM   2349 C CG  . LYS B 1 5   ? 8.982   14.901 44.312  0.20  28.51 ? 5    LYS B CG  1 
ATOM   2350 C CD  . LYS B 1 5   ? 9.116   14.688 45.814  0.20  28.27 ? 5    LYS B CD  1 
ATOM   2351 C CE  . LYS B 1 5   ? 9.496   15.978 46.537  0.20  28.26 ? 5    LYS B CE  1 
ATOM   2352 N NZ  . LYS B 1 5   ? 10.911  16.407 46.276  0.20  27.99 ? 5    LYS B NZ  1 
ATOM   2353 N N   . ILE B 1 6   ? 6.111   17.262 43.409  1.00  29.14 ? 6    ILE B N   1 
ATOM   2354 C CA  . ILE B 1 6   ? 5.707   18.278 42.440  1.00  29.68 ? 6    ILE B CA  1 
ATOM   2355 C C   . ILE B 1 6   ? 6.931   18.911 41.812  1.00  30.22 ? 6    ILE B C   1 
ATOM   2356 O O   . ILE B 1 6   ? 7.934   19.126 42.484  1.00  30.14 ? 6    ILE B O   1 
ATOM   2357 C CB  . ILE B 1 6   ? 4.858   19.400 43.075  1.00  29.55 ? 6    ILE B CB  1 
ATOM   2358 C CG1 . ILE B 1 6   ? 3.729   18.804 43.914  1.00  29.69 ? 6    ILE B CG1 1 
ATOM   2359 C CG2 . ILE B 1 6   ? 4.291   20.330 41.993  1.00  29.24 ? 6    ILE B CG2 1 
ATOM   2360 C CD1 . ILE B 1 6   ? 2.716   19.805 44.384  1.00  30.05 ? 6    ILE B CD1 1 
ATOM   2361 N N   . PHE B 1 7   ? 6.840   19.198 40.518  1.00  31.12 ? 7    PHE B N   1 
ATOM   2362 C CA  . PHE B 1 7   ? 7.891   19.907 39.797  1.00  32.02 ? 7    PHE B CA  1 
ATOM   2363 C C   . PHE B 1 7   ? 7.281   21.042 38.981  1.00  32.80 ? 7    PHE B C   1 
ATOM   2364 O O   . PHE B 1 7   ? 6.120   20.966 38.567  1.00  32.69 ? 7    PHE B O   1 
ATOM   2365 C CB  . PHE B 1 7   ? 8.613   18.966 38.834  1.00  31.87 ? 7    PHE B CB  1 
ATOM   2366 C CG  . PHE B 1 7   ? 9.489   17.931 39.496  1.00  31.15 ? 7    PHE B CG  1 
ATOM   2367 C CD1 . PHE B 1 7   ? 8.945   16.761 40.021  1.00  31.01 ? 7    PHE B CD1 1 
ATOM   2368 C CD2 . PHE B 1 7   ? 10.864  18.095 39.531  1.00  29.91 ? 7    PHE B CD2 1 
ATOM   2369 C CE1 . PHE B 1 7   ? 9.760   15.794 40.606  1.00  30.34 ? 7    PHE B CE1 1 
ATOM   2370 C CE2 . PHE B 1 7   ? 11.685  17.135 40.107  1.00  29.77 ? 7    PHE B CE2 1 
ATOM   2371 C CZ  . PHE B 1 7   ? 11.133  15.985 40.647  1.00  30.22 ? 7    PHE B CZ  1 
ATOM   2372 N N   . SER B 1 8   ? 8.077   22.079 38.729  1.00  33.91 ? 8    SER B N   1 
ATOM   2373 C CA  . SER B 1 8   ? 7.652   23.173 37.862  1.00  35.08 ? 8    SER B CA  1 
ATOM   2374 C C   . SER B 1 8   ? 8.326   23.096 36.500  1.00  35.78 ? 8    SER B C   1 
ATOM   2375 O O   . SER B 1 8   ? 9.331   22.406 36.347  1.00  36.11 ? 8    SER B O   1 
ATOM   2376 C CB  . SER B 1 8   ? 7.978   24.519 38.500  1.00  35.15 ? 8    SER B CB  1 
ATOM   2377 O OG  . SER B 1 8   ? 7.527   25.587 37.659  1.00  35.27 ? 8    SER B OG  1 
ATOM   2378 N N   . GLY B 1 9   ? 7.773   23.817 35.521  1.00  36.57 ? 9    GLY B N   1 
ATOM   2379 C CA  . GLY B 1 9   ? 8.377   23.965 34.181  1.00  37.49 ? 9    GLY B CA  1 
ATOM   2380 C C   . GLY B 1 9   ? 9.023   25.333 33.949  1.00  38.08 ? 9    GLY B C   1 
ATOM   2381 O O   . GLY B 1 9   ? 8.399   26.376 34.189  1.00  38.27 ? 9    GLY B O   1 
ATOM   2382 N N   . SER B 1 10  ? 10.273  25.327 33.483  0.10  38.30 ? 10   SER B N   1 
ATOM   2383 C CA  . SER B 1 10  ? 11.072  26.550 33.295  0.10  38.55 ? 10   SER B CA  1 
ATOM   2384 C C   . SER B 1 10  ? 11.266  27.310 34.602  0.10  38.73 ? 10   SER B C   1 
ATOM   2385 O O   . SER B 1 10  ? 11.462  26.707 35.660  0.10  38.75 ? 10   SER B O   1 
ATOM   2386 C CB  . SER B 1 10  ? 10.453  27.484 32.246  0.10  38.54 ? 10   SER B CB  1 
ATOM   2387 O OG  . SER B 1 10  ? 9.531   28.378 32.848  0.10  38.52 ? 10   SER B OG  1 
ATOM   2388 N N   . SER B 1 11  ? 11.203  28.639 34.518  0.20  38.93 ? 11   SER B N   1 
ATOM   2389 C CA  . SER B 1 11  ? 11.445  29.472 35.698  0.20  39.13 ? 11   SER B CA  1 
ATOM   2390 C C   . SER B 1 11  ? 10.207  30.270 36.079  0.20  39.23 ? 11   SER B C   1 
ATOM   2391 O O   . SER B 1 11  ? 10.167  30.895 37.138  0.20  39.25 ? 11   SER B O   1 
ATOM   2392 C CB  . SER B 1 11  ? 12.644  30.402 35.480  0.20  39.14 ? 11   SER B CB  1 
ATOM   2393 O OG  . SER B 1 11  ? 13.039  31.011 36.700  0.20  39.17 ? 11   SER B OG  1 
ATOM   2394 N N   . HIS B 1 12  ? 9.196   30.251 35.216  0.76  39.37 ? 12   HIS B N   1 
ATOM   2395 C CA  . HIS B 1 12  ? 7.897   30.792 35.589  0.76  39.45 ? 12   HIS B CA  1 
ATOM   2396 C C   . HIS B 1 12  ? 7.303   29.856 36.636  0.76  39.10 ? 12   HIS B C   1 
ATOM   2397 O O   . HIS B 1 12  ? 6.471   28.995 36.333  0.76  39.21 ? 12   HIS B O   1 
ATOM   2398 C CB  . HIS B 1 12  ? 6.996   30.959 34.359  0.76  39.66 ? 12   HIS B CB  1 
ATOM   2399 C CG  . HIS B 1 12  ? 7.417   32.084 33.462  0.76  40.75 ? 12   HIS B CG  1 
ATOM   2400 N ND1 . HIS B 1 12  ? 6.888   33.354 33.561  0.76  41.67 ? 12   HIS B ND1 1 
ATOM   2401 C CD2 . HIS B 1 12  ? 8.338   32.137 32.470  0.76  41.40 ? 12   HIS B CD2 1 
ATOM   2402 C CE1 . HIS B 1 12  ? 7.456   34.137 32.660  0.76  41.95 ? 12   HIS B CE1 1 
ATOM   2403 N NE2 . HIS B 1 12  ? 8.339   33.423 31.985  0.76  41.88 ? 12   HIS B NE2 1 
ATOM   2404 N N   . GLN B 1 13  ? 7.767   30.028 37.874  1.00  38.71 ? 13   GLN B N   1 
ATOM   2405 C CA  . GLN B 1 13  ? 7.468   29.094 38.956  1.00  38.40 ? 13   GLN B CA  1 
ATOM   2406 C C   . GLN B 1 13  ? 6.500   29.646 40.010  1.00  37.91 ? 13   GLN B C   1 
ATOM   2407 O O   . GLN B 1 13  ? 6.342   29.041 41.066  1.00  38.07 ? 13   GLN B O   1 
ATOM   2408 C CB  . GLN B 1 13  ? 8.763   28.613 39.641  1.00  38.46 ? 13   GLN B CB  1 
ATOM   2409 C CG  . GLN B 1 13  ? 9.757   27.865 38.737  1.00  39.13 ? 13   GLN B CG  1 
ATOM   2410 C CD  . GLN B 1 13  ? 10.772  27.003 39.520  1.00  40.04 ? 13   GLN B CD  1 
ATOM   2411 O OE1 . GLN B 1 13  ? 10.400  26.155 40.338  1.00  40.21 ? 13   GLN B OE1 1 
ATOM   2412 N NE2 . GLN B 1 13  ? 12.057  27.212 39.247  1.00  40.09 ? 13   GLN B NE2 1 
ATOM   2413 N N   . ASP B 1 14  ? 5.840   30.770 39.733  0.40  37.16 ? 14   ASP B N   1 
ATOM   2414 C CA  . ASP B 1 14  ? 4.935   31.356 40.725  0.40  36.43 ? 14   ASP B CA  1 
ATOM   2415 C C   . ASP B 1 14  ? 3.767   30.433 41.077  0.40  35.94 ? 14   ASP B C   1 
ATOM   2416 O O   . ASP B 1 14  ? 3.604   30.058 42.238  0.40  35.80 ? 14   ASP B O   1 
ATOM   2417 C CB  . ASP B 1 14  ? 4.423   32.728 40.288  0.40  36.44 ? 14   ASP B CB  1 
ATOM   2418 C CG  . ASP B 1 14  ? 3.978   33.576 41.463  0.40  36.49 ? 14   ASP B CG  1 
ATOM   2419 O OD1 . ASP B 1 14  ? 4.862   34.122 42.167  0.40  36.61 ? 14   ASP B OD1 1 
ATOM   2420 O OD2 . ASP B 1 14  ? 2.746   33.696 41.684  0.40  36.42 ? 14   ASP B OD2 1 
ATOM   2421 N N   . LEU B 1 15  ? 2.975   30.062 40.072  1.00  35.53 ? 15   LEU B N   1 
ATOM   2422 C CA  . LEU B 1 15  ? 1.822   29.170 40.243  1.00  34.98 ? 15   LEU B CA  1 
ATOM   2423 C C   . LEU B 1 15  ? 2.233   27.817 40.835  1.00  34.83 ? 15   LEU B C   1 
ATOM   2424 O O   . LEU B 1 15  ? 1.569   27.304 41.741  1.00  35.00 ? 15   LEU B O   1 
ATOM   2425 C CB  . LEU B 1 15  ? 1.104   28.947 38.906  1.00  34.73 ? 15   LEU B CB  1 
ATOM   2426 C CG  . LEU B 1 15  ? -0.407  28.682 38.835  1.00  34.43 ? 15   LEU B CG  1 
ATOM   2427 C CD1 . LEU B 1 15  ? -0.677  27.544 37.864  1.00  34.20 ? 15   LEU B CD1 1 
ATOM   2428 C CD2 . LEU B 1 15  ? -1.064  28.381 40.178  1.00  34.48 ? 15   LEU B CD2 1 
ATOM   2429 N N   . SER B 1 16  ? 3.323   27.248 40.330  1.00  34.25 ? 16   SER B N   1 
ATOM   2430 C CA  . SER B 1 16  ? 3.794   25.962 40.814  1.00  33.87 ? 16   SER B CA  1 
ATOM   2431 C C   . SER B 1 16  ? 4.172   26.008 42.290  1.00  33.67 ? 16   SER B C   1 
ATOM   2432 O O   . SER B 1 16  ? 3.866   25.077 43.046  1.00  33.75 ? 16   SER B O   1 
ATOM   2433 C CB  . SER B 1 16  ? 4.978   25.489 39.984  1.00  33.98 ? 16   SER B CB  1 
ATOM   2434 O OG  . SER B 1 16  ? 4.545   24.991 38.732  1.00  34.26 ? 16   SER B OG  1 
ATOM   2435 N N   . GLN B 1 17  ? 4.827   27.094 42.697  1.00  33.34 ? 17   GLN B N   1 
ATOM   2436 C CA  . GLN B 1 17  ? 5.265   27.248 44.085  1.00  33.03 ? 17   GLN B CA  1 
ATOM   2437 C C   . GLN B 1 17  ? 4.081   27.583 44.970  1.00  32.55 ? 17   GLN B C   1 
ATOM   2438 O O   . GLN B 1 17  ? 4.033   27.155 46.125  1.00  32.55 ? 17   GLN B O   1 
ATOM   2439 C CB  . GLN B 1 17  ? 6.377   28.299 44.212  1.00  33.19 ? 17   GLN B CB  1 
ATOM   2440 C CG  . GLN B 1 17  ? 6.923   28.521 45.629  1.00  34.75 ? 17   GLN B CG  1 
ATOM   2441 C CD  . GLN B 1 17  ? 7.813   27.381 46.147  1.00  37.50 ? 17   GLN B CD  1 
ATOM   2442 O OE1 . GLN B 1 17  ? 8.912   27.131 45.625  1.00  38.09 ? 17   GLN B OE1 1 
ATOM   2443 N NE2 . GLN B 1 17  ? 7.350   26.707 47.203  1.00  38.37 ? 17   GLN B NE2 1 
ATOM   2444 N N   . LYS B 1 18  ? 3.123   28.332 44.420  1.00  32.05 ? 18   LYS B N   1 
ATOM   2445 C CA  . LYS B 1 18  ? 1.855   28.584 45.100  1.00  31.61 ? 18   LYS B CA  1 
ATOM   2446 C C   . LYS B 1 18  ? 1.148   27.278 45.416  1.00  31.25 ? 18   LYS B C   1 
ATOM   2447 O O   . LYS B 1 18  ? 0.709   27.064 46.548  1.00  31.42 ? 18   LYS B O   1 
ATOM   2448 C CB  . LYS B 1 18  ? 0.940   29.478 44.269  1.00  31.69 ? 18   LYS B CB  1 
ATOM   2449 C CG  . LYS B 1 18  ? 0.981   30.937 44.660  1.00  32.39 ? 18   LYS B CG  1 
ATOM   2450 C CD  . LYS B 1 18  ? -0.096  31.713 43.934  1.00  33.97 ? 18   LYS B CD  1 
ATOM   2451 C CE  . LYS B 1 18  ? -0.153  33.157 44.406  1.00  35.22 ? 18   LYS B CE  1 
ATOM   2452 N NZ  . LYS B 1 18  ? -1.436  33.822 44.004  1.00  36.09 ? 18   LYS B NZ  1 
ATOM   2453 N N   . ILE B 1 19  ? 1.047   26.405 44.416  1.00  30.78 ? 19   ILE B N   1 
ATOM   2454 C CA  . ILE B 1 19  ? 0.429   25.088 44.598  1.00  30.25 ? 19   ILE B CA  1 
ATOM   2455 C C   . ILE B 1 19  ? 1.230   24.235 45.593  1.00  30.03 ? 19   ILE B C   1 
ATOM   2456 O O   . ILE B 1 19  ? 0.650   23.554 46.442  1.00  30.01 ? 19   ILE B O   1 
ATOM   2457 C CB  . ILE B 1 19  ? 0.254   24.336 43.251  1.00  30.29 ? 19   ILE B CB  1 
ATOM   2458 C CG1 . ILE B 1 19  ? -0.503  25.205 42.236  1.00  29.81 ? 19   ILE B CG1 1 
ATOM   2459 C CG2 . ILE B 1 19  ? -0.459  22.992 43.464  1.00  29.93 ? 19   ILE B CG2 1 
ATOM   2460 C CD1 . ILE B 1 19  ? -0.333  24.783 40.781  1.00  29.15 ? 19   ILE B CD1 1 
ATOM   2461 N N   . ALA B 1 20  ? 2.558   24.291 45.488  1.00  29.56 ? 20   ALA B N   1 
ATOM   2462 C CA  . ALA B 1 20  ? 3.436   23.560 46.387  1.00  29.44 ? 20   ALA B CA  1 
ATOM   2463 C C   . ALA B 1 20  ? 3.230   23.979 47.848  1.00  29.39 ? 20   ALA B C   1 
ATOM   2464 O O   . ALA B 1 20  ? 2.921   23.144 48.709  1.00  29.37 ? 20   ALA B O   1 
ATOM   2465 C CB  . ALA B 1 20  ? 4.878   23.755 45.968  1.00  29.50 ? 20   ALA B CB  1 
ATOM   2466 N N   . ASP B 1 21  ? 3.396   25.276 48.107  0.40  29.27 ? 21   ASP B N   1 
ATOM   2467 C CA  . ASP B 1 21  ? 3.157   25.863 49.425  0.40  29.26 ? 21   ASP B CA  1 
ATOM   2468 C C   . ASP B 1 21  ? 1.907   25.285 50.069  0.40  29.38 ? 21   ASP B C   1 
ATOM   2469 O O   . ASP B 1 21  ? 1.942   24.812 51.206  0.40  29.33 ? 21   ASP B O   1 
ATOM   2470 C CB  . ASP B 1 21  ? 3.012   27.384 49.313  0.40  29.21 ? 21   ASP B CB  1 
ATOM   2471 C CG  . ASP B 1 21  ? 4.345   28.096 49.263  0.40  28.89 ? 21   ASP B CG  1 
ATOM   2472 O OD1 . ASP B 1 21  ? 5.334   27.530 49.771  0.40  28.93 ? 21   ASP B OD1 1 
ATOM   2473 O OD2 . ASP B 1 21  ? 4.406   29.222 48.727  0.40  28.22 ? 21   ASP B OD2 1 
ATOM   2474 N N   . ARG B 1 22  ? 0.812   25.310 49.315  1.00  29.59 ? 22   ARG B N   1 
ATOM   2475 C CA  . ARG B 1 22  ? -0.502  24.926 49.821  1.00  30.05 ? 22   ARG B CA  1 
ATOM   2476 C C   . ARG B 1 22  ? -0.630  23.438 50.144  1.00  29.86 ? 22   ARG B C   1 
ATOM   2477 O O   . ARG B 1 22  ? -1.494  23.053 50.928  1.00  29.95 ? 22   ARG B O   1 
ATOM   2478 C CB  . ARG B 1 22  ? -1.601  25.384 48.860  1.00  30.30 ? 22   ARG B CB  1 
ATOM   2479 C CG  . ARG B 1 22  ? -1.674  26.904 48.717  1.00  32.01 ? 22   ARG B CG  1 
ATOM   2480 C CD  . ARG B 1 22  ? -2.622  27.325 47.605  1.00  35.11 ? 22   ARG B CD  1 
ATOM   2481 N NE  . ARG B 1 22  ? -3.982  27.549 48.093  1.00  38.12 ? 22   ARG B NE  1 
ATOM   2482 C CZ  . ARG B 1 22  ? -4.506  28.747 48.355  1.00  40.08 ? 22   ARG B CZ  1 
ATOM   2483 N NH1 . ARG B 1 22  ? -3.788  29.855 48.180  1.00  40.21 ? 22   ARG B NH1 1 
ATOM   2484 N NH2 . ARG B 1 22  ? -5.756  28.835 48.797  1.00  41.48 ? 22   ARG B NH2 1 
ATOM   2485 N N   . LEU B 1 23  ? 0.237   22.618 49.555  1.00  29.74 ? 23   LEU B N   1 
ATOM   2486 C CA  . LEU B 1 23  ? 0.255   21.185 49.833  1.00  29.41 ? 23   LEU B CA  1 
ATOM   2487 C C   . LEU B 1 23  ? 1.266   20.875 50.924  1.00  29.43 ? 23   LEU B C   1 
ATOM   2488 O O   . LEU B 1 23  ? 1.399   19.724 51.350  1.00  29.49 ? 23   LEU B O   1 
ATOM   2489 C CB  . LEU B 1 23  ? 0.591   20.401 48.567  1.00  29.27 ? 23   LEU B CB  1 
ATOM   2490 C CG  . LEU B 1 23  ? -0.485  20.336 47.487  1.00  28.73 ? 23   LEU B CG  1 
ATOM   2491 C CD1 . LEU B 1 23  ? 0.140   19.835 46.218  1.00  28.53 ? 23   LEU B CD1 1 
ATOM   2492 C CD2 . LEU B 1 23  ? -1.667  19.462 47.906  1.00  27.90 ? 23   LEU B CD2 1 
ATOM   2493 N N   . GLY B 1 24  ? 1.969   21.915 51.373  1.00  29.33 ? 24   GLY B N   1 
ATOM   2494 C CA  . GLY B 1 24  ? 3.022   21.783 52.378  1.00  29.27 ? 24   GLY B CA  1 
ATOM   2495 C C   . GLY B 1 24  ? 4.212   21.003 51.858  1.00  29.34 ? 24   GLY B C   1 
ATOM   2496 O O   . GLY B 1 24  ? 4.746   20.138 52.556  1.00  29.35 ? 24   GLY B O   1 
ATOM   2497 N N   . LEU B 1 25  ? 4.613   21.308 50.623  1.00  29.43 ? 25   LEU B N   1 
ATOM   2498 C CA  . LEU B 1 25  ? 5.737   20.654 49.962  1.00  29.35 ? 25   LEU B CA  1 
ATOM   2499 C C   . LEU B 1 25  ? 6.677   21.672 49.340  1.00  29.77 ? 25   LEU B C   1 
ATOM   2500 O O   . LEU B 1 25  ? 6.251   22.761 48.957  1.00  29.63 ? 25   LEU B O   1 
ATOM   2501 C CB  . LEU B 1 25  ? 5.239   19.749 48.834  1.00  29.09 ? 25   LEU B CB  1 
ATOM   2502 C CG  . LEU B 1 25  ? 4.355   18.521 49.016  1.00  27.89 ? 25   LEU B CG  1 
ATOM   2503 C CD1 . LEU B 1 25  ? 4.189   17.889 47.659  1.00  27.69 ? 25   LEU B CD1 1 
ATOM   2504 C CD2 . LEU B 1 25  ? 4.977   17.525 49.951  1.00  27.51 ? 25   LEU B CD2 1 
ATOM   2505 N N   . GLU B 1 26  ? 7.951   21.308 49.228  0.94  30.45 ? 26   GLU B N   1 
ATOM   2506 C CA  . GLU B 1 26  ? 8.874   22.026 48.352  0.94  31.21 ? 26   GLU B CA  1 
ATOM   2507 C C   . GLU B 1 26  ? 8.779   21.510 46.916  0.94  31.31 ? 26   GLU B C   1 
ATOM   2508 O O   . GLU B 1 26  ? 8.402   20.357 46.674  0.94  31.16 ? 26   GLU B O   1 
ATOM   2509 C CB  . GLU B 1 26  ? 10.309  21.914 48.852  0.94  31.29 ? 26   GLU B CB  1 
ATOM   2510 C CG  . GLU B 1 26  ? 10.740  23.085 49.699  0.94  33.15 ? 26   GLU B CG  1 
ATOM   2511 C CD  . GLU B 1 26  ? 12.168  22.943 50.184  0.94  35.84 ? 26   GLU B CD  1 
ATOM   2512 O OE1 . GLU B 1 26  ? 13.099  23.141 49.366  0.94  36.67 ? 26   GLU B OE1 1 
ATOM   2513 O OE2 . GLU B 1 26  ? 12.359  22.634 51.386  0.94  36.90 ? 26   GLU B OE2 1 
ATOM   2514 N N   . LEU B 1 27  ? 9.108   22.383 45.967  1.00  31.63 ? 27   LEU B N   1 
ATOM   2515 C CA  . LEU B 1 27  ? 9.188   21.995 44.569  1.00  31.79 ? 27   LEU B CA  1 
ATOM   2516 C C   . LEU B 1 27  ? 10.435  21.158 44.329  1.00  32.15 ? 27   LEU B C   1 
ATOM   2517 O O   . LEU B 1 27  ? 11.535  21.547 44.714  1.00  31.91 ? 27   LEU B O   1 
ATOM   2518 C CB  . LEU B 1 27  ? 9.183   23.226 43.667  1.00  31.59 ? 27   LEU B CB  1 
ATOM   2519 C CG  . LEU B 1 27  ? 7.802   23.780 43.304  1.00  31.52 ? 27   LEU B CG  1 
ATOM   2520 C CD1 . LEU B 1 27  ? 7.940   25.148 42.670  1.00  32.09 ? 27   LEU B CD1 1 
ATOM   2521 C CD2 . LEU B 1 27  ? 7.042   22.846 42.360  1.00  31.08 ? 27   LEU B CD2 1 
ATOM   2522 N N   . GLY B 1 28  ? 10.245  20.000 43.704  1.00  32.90 ? 28   GLY B N   1 
ATOM   2523 C CA  . GLY B 1 28  ? 11.343  19.094 43.377  1.00  33.95 ? 28   GLY B CA  1 
ATOM   2524 C C   . GLY B 1 28  ? 12.434  19.753 42.558  1.00  34.58 ? 28   GLY B C   1 
ATOM   2525 O O   . GLY B 1 28  ? 12.170  20.657 41.766  1.00  34.51 ? 28   GLY B O   1 
ATOM   2526 N N   . LYS B 1 29  ? 13.661  19.280 42.746  1.00  35.39 ? 29   LYS B N   1 
ATOM   2527 C CA  . LYS B 1 29  ? 14.842  19.919 42.176  1.00  36.51 ? 29   LYS B CA  1 
ATOM   2528 C C   . LYS B 1 29  ? 15.047  19.541 40.703  1.00  36.90 ? 29   LYS B C   1 
ATOM   2529 O O   . LYS B 1 29  ? 15.089  18.359 40.357  1.00  36.99 ? 29   LYS B O   1 
ATOM   2530 C CB  . LYS B 1 29  ? 16.087  19.567 43.007  1.00  36.66 ? 29   LYS B CB  1 
ATOM   2531 C CG  . LYS B 1 29  ? 15.838  19.510 44.531  1.00  38.30 ? 29   LYS B CG  1 
ATOM   2532 C CD  . LYS B 1 29  ? 16.941  18.706 45.260  1.00  40.94 ? 29   LYS B CD  1 
ATOM   2533 C CE  . LYS B 1 29  ? 16.546  18.286 46.695  1.00  41.37 ? 29   LYS B CE  1 
ATOM   2534 N NZ  . LYS B 1 29  ? 16.654  19.394 47.705  1.00  42.14 ? 29   LYS B NZ  1 
ATOM   2535 N N   . VAL B 1 30  ? 15.164  20.556 39.845  1.00  37.47 ? 30   VAL B N   1 
ATOM   2536 C CA  . VAL B 1 30  ? 15.378  20.365 38.403  1.00  37.96 ? 30   VAL B CA  1 
ATOM   2537 C C   . VAL B 1 30  ? 16.474  21.286 37.875  1.00  38.25 ? 30   VAL B C   1 
ATOM   2538 O O   . VAL B 1 30  ? 16.595  22.426 38.309  1.00  38.17 ? 30   VAL B O   1 
ATOM   2539 C CB  . VAL B 1 30  ? 14.085  20.630 37.594  1.00  37.99 ? 30   VAL B CB  1 
ATOM   2540 C CG1 . VAL B 1 30  ? 14.370  20.724 36.100  1.00  38.11 ? 30   VAL B CG1 1 
ATOM   2541 C CG2 . VAL B 1 30  ? 13.090  19.541 37.839  1.00  38.26 ? 30   VAL B CG2 1 
ATOM   2542 N N   . VAL B 1 31  ? 17.251  20.783 36.922  1.00  38.70 ? 31   VAL B N   1 
ATOM   2543 C CA  . VAL B 1 31  ? 18.308  21.547 36.276  1.00  39.26 ? 31   VAL B CA  1 
ATOM   2544 C C   . VAL B 1 31  ? 17.932  21.769 34.807  1.00  39.60 ? 31   VAL B C   1 
ATOM   2545 O O   . VAL B 1 31  ? 18.308  20.988 33.938  1.00  40.02 ? 31   VAL B O   1 
ATOM   2546 C CB  . VAL B 1 31  ? 19.656  20.793 36.405  1.00  39.32 ? 31   VAL B CB  1 
ATOM   2547 C CG1 . VAL B 1 31  ? 20.746  21.432 35.521  1.00  39.59 ? 31   VAL B CG1 1 
ATOM   2548 C CG2 . VAL B 1 31  ? 20.094  20.715 37.878  1.00  39.56 ? 31   VAL B CG2 1 
ATOM   2549 N N   . THR B 1 32  ? 17.183  22.833 34.534  0.71  39.96 ? 32   THR B N   1 
ATOM   2550 C CA  . THR B 1 32  ? 16.582  23.033 33.211  0.71  40.27 ? 32   THR B CA  1 
ATOM   2551 C C   . THR B 1 32  ? 17.095  24.255 32.465  0.71  40.43 ? 32   THR B C   1 
ATOM   2552 O O   . THR B 1 32  ? 16.847  25.390 32.871  0.71  40.51 ? 32   THR B O   1 
ATOM   2553 C CB  . THR B 1 32  ? 15.034  23.100 33.283  0.71  40.36 ? 32   THR B CB  1 
ATOM   2554 O OG1 . THR B 1 32  ? 14.520  23.511 32.010  0.71  40.65 ? 32   THR B OG1 1 
ATOM   2555 C CG2 . THR B 1 32  ? 14.555  24.087 34.366  0.71  40.51 ? 32   THR B CG2 1 
ATOM   2556 N N   . LYS B 1 33  ? 17.786  24.028 31.357  0.010 40.76 ? 33   LYS B N   1 
ATOM   2557 C CA  . LYS B 1 33  ? 18.316  25.137 30.583  0.010 41.06 ? 33   LYS B CA  1 
ATOM   2558 C C   . LYS B 1 33  ? 18.228  24.873 29.089  0.010 41.28 ? 33   LYS B C   1 
ATOM   2559 O O   . LYS B 1 33  ? 18.367  23.733 28.640  0.010 41.30 ? 33   LYS B O   1 
ATOM   2560 C CB  . LYS B 1 33  ? 19.768  25.407 30.975  0.010 41.04 ? 33   LYS B CB  1 
ATOM   2561 C CG  . LYS B 1 33  ? 20.702  24.252 30.668  0.010 41.05 ? 33   LYS B CG  1 
ATOM   2562 C CD  . LYS B 1 33  ? 22.074  24.466 31.278  0.010 41.05 ? 33   LYS B CD  1 
ATOM   2563 C CE  . LYS B 1 33  ? 22.965  23.258 31.048  0.010 41.05 ? 33   LYS B CE  1 
ATOM   2564 N NZ  . LYS B 1 33  ? 24.300  23.424 31.684  0.010 41.05 ? 33   LYS B NZ  1 
ATOM   2565 N N   . LYS B 1 34  ? 17.991  25.938 28.330  1.00  41.59 ? 34   LYS B N   1 
ATOM   2566 C CA  . LYS B 1 34  ? 18.040  25.882 26.880  1.00  41.78 ? 34   LYS B CA  1 
ATOM   2567 C C   . LYS B 1 34  ? 19.498  25.785 26.472  1.00  41.43 ? 34   LYS B C   1 
ATOM   2568 O O   . LYS B 1 34  ? 20.355  26.445 27.060  1.00  41.57 ? 34   LYS B O   1 
ATOM   2569 C CB  . LYS B 1 34  ? 17.419  27.139 26.261  1.00  42.10 ? 34   LYS B CB  1 
ATOM   2570 C CG  . LYS B 1 34  ? 15.891  27.236 26.386  1.00  43.63 ? 34   LYS B CG  1 
ATOM   2571 C CD  . LYS B 1 34  ? 15.234  27.646 25.043  1.00  46.34 ? 34   LYS B CD  1 
ATOM   2572 C CE  . LYS B 1 34  ? 15.713  29.030 24.520  1.00  47.30 ? 34   LYS B CE  1 
ATOM   2573 N NZ  . LYS B 1 34  ? 15.422  29.226 23.056  1.00  47.49 ? 34   LYS B NZ  1 
ATOM   2574 N N   . PHE B 1 35  ? 19.784  24.954 25.476  0.010 40.93 ? 35   PHE B N   1 
ATOM   2575 C CA  . PHE B 1 35  ? 21.137  24.863 24.945  0.010 40.39 ? 35   PHE B CA  1 
ATOM   2576 C C   . PHE B 1 35  ? 21.397  26.029 24.003  0.010 40.02 ? 35   PHE B C   1 
ATOM   2577 O O   . PHE B 1 35  ? 20.479  26.769 23.649  0.010 39.97 ? 35   PHE B O   1 
ATOM   2578 C CB  . PHE B 1 35  ? 21.361  23.533 24.229  0.010 40.42 ? 35   PHE B CB  1 
ATOM   2579 C CG  . PHE B 1 35  ? 21.637  22.384 25.155  0.010 40.37 ? 35   PHE B CG  1 
ATOM   2580 C CD1 . PHE B 1 35  ? 20.871  21.233 25.098  0.010 40.35 ? 35   PHE B CD1 1 
ATOM   2581 C CD2 . PHE B 1 35  ? 22.663  22.456 26.083  0.010 40.36 ? 35   PHE B CD2 1 
ATOM   2582 C CE1 . PHE B 1 35  ? 21.126  20.173 25.942  0.010 40.34 ? 35   PHE B CE1 1 
ATOM   2583 C CE2 . PHE B 1 35  ? 22.921  21.399 26.934  0.010 40.34 ? 35   PHE B CE2 1 
ATOM   2584 C CZ  . PHE B 1 35  ? 22.153  20.256 26.863  0.010 40.34 ? 35   PHE B CZ  1 
ATOM   2585 N N   . SER B 1 36  ? 22.650  26.195 23.599  0.010 39.52 ? 36   SER B N   1 
ATOM   2586 C CA  . SER B 1 36  ? 23.000  27.296 22.717  0.010 39.04 ? 36   SER B CA  1 
ATOM   2587 C C   . SER B 1 36  ? 22.240  27.205 21.395  0.010 38.70 ? 36   SER B C   1 
ATOM   2588 O O   . SER B 1 36  ? 21.964  28.224 20.763  0.010 38.66 ? 36   SER B O   1 
ATOM   2589 C CB  . SER B 1 36  ? 24.510  27.345 22.481  0.010 39.06 ? 36   SER B CB  1 
ATOM   2590 O OG  . SER B 1 36  ? 24.866  28.457 21.678  0.010 39.04 ? 36   SER B OG  1 
ATOM   2591 N N   . ASN B 1 37  ? 21.890  25.988 20.986  0.010 38.26 ? 37   ASN B N   1 
ATOM   2592 C CA  . ASN B 1 37  ? 21.145  25.798 19.741  0.010 37.84 ? 37   ASN B CA  1 
ATOM   2593 C C   . ASN B 1 37  ? 19.629  25.794 19.926  0.010 37.56 ? 37   ASN B C   1 
ATOM   2594 O O   . ASN B 1 37  ? 18.883  25.516 18.987  0.010 37.52 ? 37   ASN B O   1 
ATOM   2595 C CB  . ASN B 1 37  ? 21.602  24.538 18.998  0.010 37.85 ? 37   ASN B CB  1 
ATOM   2596 C CG  . ASN B 1 37  ? 21.107  23.262 19.643  0.010 37.82 ? 37   ASN B CG  1 
ATOM   2597 O OD1 . ASN B 1 37  ? 21.292  23.043 20.840  0.010 37.82 ? 37   ASN B OD1 1 
ATOM   2598 N ND2 . ASN B 1 37  ? 20.481  22.403 18.847  0.010 37.81 ? 37   ASN B ND2 1 
ATOM   2599 N N   . GLN B 1 38  ? 19.177  26.096 21.138  0.10  37.20 ? 38   GLN B N   1 
ATOM   2600 C CA  . GLN B 1 38  ? 17.751  26.266 21.395  0.10  36.86 ? 38   GLN B CA  1 
ATOM   2601 C C   . GLN B 1 38  ? 17.050  24.958 21.714  0.10  36.68 ? 38   GLN B C   1 
ATOM   2602 O O   . GLN B 1 38  ? 15.766  24.895 21.667  0.10  36.63 ? 38   GLN B O   1 
ATOM   2603 C CB  . GLN B 1 38  ? 17.036  26.760 20.136  0.10  36.84 ? 38   GLN B CB  1 
ATOM   2604 C CG  . GLN B 1 38  ? 17.855  27.713 19.306  0.10  36.72 ? 38   GLN B CG  1 
ATOM   2605 C CD  . GLN B 1 38  ? 18.461  28.813 20.142  0.10  36.60 ? 38   GLN B CD  1 
ATOM   2606 O OE1 . GLN B 1 38  ? 19.680  28.973 20.186  0.10  36.43 ? 38   GLN B OE1 1 
ATOM   2607 N NE2 . GLN B 1 38  ? 17.613  29.576 20.823  0.10  36.62 ? 38   GLN B NE2 1 
ATOM   2608 N N   . GLU B 1 39  ? 17.854  23.908 22.017  0.40  36.47 ? 39   GLU B N   1 
ATOM   2609 C CA  . GLU B 1 39  ? 17.136  22.690 22.403  0.40  36.31 ? 39   GLU B CA  1 
ATOM   2610 C C   . GLU B 1 39  ? 17.161  22.812 23.902  0.40  36.36 ? 39   GLU B C   1 
ATOM   2611 O O   . GLU B 1 39  ? 17.965  23.569 24.453  0.40  36.27 ? 39   GLU B O   1 
ATOM   2612 C CB  . GLU B 1 39  ? 17.820  21.419 21.933  0.40  36.28 ? 39   GLU B CB  1 
ATOM   2613 C CG  . GLU B 1 39  ? 19.309  21.426 22.142  0.40  36.19 ? 39   GLU B CG  1 
ATOM   2614 C CD  . GLU B 1 39  ? 19.946  20.220 21.512  0.40  36.06 ? 39   GLU B CD  1 
ATOM   2615 O OE1 . GLU B 1 39  ? 20.484  19.373 22.257  0.40  35.77 ? 39   GLU B OE1 1 
ATOM   2616 O OE2 . GLU B 1 39  ? 19.893  20.108 20.271  0.40  36.39 ? 39   GLU B OE2 1 
ATOM   2617 N N   . THR B 1 40  ? 16.269  22.076 24.556  1.00  36.52 ? 40   THR B N   1 
ATOM   2618 C CA  . THR B 1 40  ? 16.115  22.149 26.003  1.00  36.56 ? 40   THR B CA  1 
ATOM   2619 C C   . THR B 1 40  ? 16.768  20.953 26.689  1.00  36.57 ? 40   THR B C   1 
ATOM   2620 O O   . THR B 1 40  ? 16.497  19.802 26.346  1.00  36.41 ? 40   THR B O   1 
ATOM   2621 C CB  . THR B 1 40  ? 14.619  22.257 26.419  1.00  36.61 ? 40   THR B CB  1 
ATOM   2622 O OG1 . THR B 1 40  ? 13.996  23.341 25.715  1.00  36.28 ? 40   THR B OG1 1 
ATOM   2623 C CG2 . THR B 1 40  ? 14.496  22.524 27.925  1.00  37.01 ? 40   THR B CG2 1 
ATOM   2624 N N   . CYS B 1 41  ? 17.651  21.252 27.640  1.00  36.70 ? 41   CYS B N   1 
ATOM   2625 C CA  . CYS B 1 41  ? 18.176  20.268 28.582  1.00  36.74 ? 41   CYS B CA  1 
ATOM   2626 C C   . CYS B 1 41  ? 17.287  20.238 29.809  1.00  36.37 ? 41   CYS B C   1 
ATOM   2627 O O   . CYS B 1 41  ? 16.776  21.284 30.241  1.00  36.67 ? 41   CYS B O   1 
ATOM   2628 C CB  . CYS B 1 41  ? 19.588  20.644 29.026  1.00  36.89 ? 41   CYS B CB  1 
ATOM   2629 S SG  . CYS B 1 41  ? 19.835  20.611 30.840  1.00  38.17 ? 41   CYS B SG  1 
ATOM   2630 N N   . VAL B 1 42  ? 17.128  19.044 30.376  1.00  35.56 ? 42   VAL B N   1 
ATOM   2631 C CA  . VAL B 1 42  ? 16.385  18.860 31.612  1.00  34.79 ? 42   VAL B CA  1 
ATOM   2632 C C   . VAL B 1 42  ? 17.070  17.782 32.432  1.00  34.21 ? 42   VAL B C   1 
ATOM   2633 O O   . VAL B 1 42  ? 17.434  16.734 31.902  1.00  34.34 ? 42   VAL B O   1 
ATOM   2634 C CB  . VAL B 1 42  ? 14.914  18.477 31.325  1.00  34.92 ? 42   VAL B CB  1 
ATOM   2635 C CG1 . VAL B 1 42  ? 14.249  17.814 32.545  1.00  34.98 ? 42   VAL B CG1 1 
ATOM   2636 C CG2 . VAL B 1 42  ? 14.118  19.703 30.859  1.00  35.04 ? 42   VAL B CG2 1 
ATOM   2637 N N   . GLU B 1 43  ? 17.268  18.048 33.718  0.40  33.44 ? 43   GLU B N   1 
ATOM   2638 C CA  . GLU B 1 43  ? 17.819  17.039 34.609  0.40  32.67 ? 43   GLU B CA  1 
ATOM   2639 C C   . GLU B 1 43  ? 17.052  17.001 35.922  0.40  32.13 ? 43   GLU B C   1 
ATOM   2640 O O   . GLU B 1 43  ? 16.872  18.033 36.573  0.40  32.06 ? 43   GLU B O   1 
ATOM   2641 C CB  . GLU B 1 43  ? 19.307  17.284 34.857  0.40  32.70 ? 43   GLU B CB  1 
ATOM   2642 C CG  . GLU B 1 43  ? 20.030  16.078 35.428  0.40  32.59 ? 43   GLU B CG  1 
ATOM   2643 C CD  . GLU B 1 43  ? 21.395  16.427 35.979  0.40  32.54 ? 43   GLU B CD  1 
ATOM   2644 O OE1 . GLU B 1 43  ? 21.777  15.860 37.025  0.40  32.55 ? 43   GLU B OE1 1 
ATOM   2645 O OE2 . GLU B 1 43  ? 22.084  17.272 35.371  0.40  32.47 ? 43   GLU B OE2 1 
ATOM   2646 N N   . ILE B 1 44  ? 16.600  15.807 36.298  1.00  31.39 ? 44   ILE B N   1 
ATOM   2647 C CA  . ILE B 1 44  ? 15.839  15.614 37.528  1.00  30.85 ? 44   ILE B CA  1 
ATOM   2648 C C   . ILE B 1 44  ? 16.801  15.387 38.675  1.00  30.65 ? 44   ILE B C   1 
ATOM   2649 O O   . ILE B 1 44  ? 17.399  14.320 38.796  1.00  30.72 ? 44   ILE B O   1 
ATOM   2650 C CB  . ILE B 1 44  ? 14.833  14.442 37.426  1.00  30.70 ? 44   ILE B CB  1 
ATOM   2651 C CG1 . ILE B 1 44  ? 13.807  14.687 36.310  1.00  30.59 ? 44   ILE B CG1 1 
ATOM   2652 C CG2 . ILE B 1 44  ? 14.127  14.218 38.758  1.00  30.68 ? 44   ILE B CG2 1 
ATOM   2653 C CD1 . ILE B 1 44  ? 13.062  16.018 36.404  1.00  30.39 ? 44   ILE B CD1 1 
ATOM   2654 N N   . GLY B 1 45  ? 16.933  16.405 39.519  1.00  30.47 ? 45   GLY B N   1 
ATOM   2655 C CA  . GLY B 1 45  ? 17.953  16.434 40.562  1.00  30.20 ? 45   GLY B CA  1 
ATOM   2656 C C   . GLY B 1 45  ? 17.626  15.697 41.843  1.00  30.00 ? 45   GLY B C   1 
ATOM   2657 O O   . GLY B 1 45  ? 18.139  16.052 42.908  1.00  29.94 ? 45   GLY B O   1 
ATOM   2658 N N   . GLU B 1 46  ? 16.771  14.680 41.744  1.00  29.84 ? 46   GLU B N   1 
ATOM   2659 C CA  . GLU B 1 46  ? 16.414  13.825 42.885  1.00  29.72 ? 46   GLU B CA  1 
ATOM   2660 C C   . GLU B 1 46  ? 15.517  12.657 42.486  1.00  29.02 ? 46   GLU B C   1 
ATOM   2661 O O   . GLU B 1 46  ? 14.480  12.847 41.852  1.00  28.76 ? 46   GLU B O   1 
ATOM   2662 C CB  . GLU B 1 46  ? 15.766  14.627 44.032  1.00  30.05 ? 46   GLU B CB  1 
ATOM   2663 C CG  . GLU B 1 46  ? 14.682  15.618 43.610  1.00  31.46 ? 46   GLU B CG  1 
ATOM   2664 C CD  . GLU B 1 46  ? 13.700  15.892 44.717  1.00  33.70 ? 46   GLU B CD  1 
ATOM   2665 O OE1 . GLU B 1 46  ? 12.793  15.050 44.917  1.00  35.12 ? 46   GLU B OE1 1 
ATOM   2666 O OE2 . GLU B 1 46  ? 13.830  16.948 45.379  1.00  34.58 ? 46   GLU B OE2 1 
ATOM   2667 N N   . SER B 1 47  ? 15.947  11.457 42.878  1.00  28.43 ? 47   SER B N   1 
ATOM   2668 C CA  . SER B 1 47  ? 15.225  10.203 42.666  1.00  27.94 ? 47   SER B CA  1 
ATOM   2669 C C   . SER B 1 47  ? 13.710  10.342 42.822  1.00  27.50 ? 47   SER B C   1 
ATOM   2670 O O   . SER B 1 47  ? 13.212  10.719 43.887  1.00  27.49 ? 47   SER B O   1 
ATOM   2671 C CB  . SER B 1 47  ? 15.737  9.140  43.640  1.00  27.95 ? 47   SER B CB  1 
ATOM   2672 O OG  . SER B 1 47  ? 14.916  7.976  43.594  1.00  28.37 ? 47   SER B OG  1 
ATOM   2673 N N   . VAL B 1 48  ? 12.991  10.037 41.746  1.00  26.80 ? 48   VAL B N   1 
ATOM   2674 C CA  . VAL B 1 48  ? 11.533  10.075 41.738  1.00  26.12 ? 48   VAL B CA  1 
ATOM   2675 C C   . VAL B 1 48  ? 11.019  8.637  41.675  1.00  25.74 ? 48   VAL B C   1 
ATOM   2676 O O   . VAL B 1 48  ? 9.835   8.381  41.436  1.00  25.80 ? 48   VAL B O   1 
ATOM   2677 C CB  . VAL B 1 48  ? 10.984  10.926 40.553  1.00  26.16 ? 48   VAL B CB  1 
ATOM   2678 C CG1 . VAL B 1 48  ? 11.291  12.401 40.760  1.00  26.26 ? 48   VAL B CG1 1 
ATOM   2679 C CG2 . VAL B 1 48  ? 11.569  10.457 39.222  1.00  26.05 ? 48   VAL B CG2 1 
ATOM   2680 N N   . ARG B 1 49  ? 11.940  7.704  41.908  1.00  25.18 ? 49   ARG B N   1 
ATOM   2681 C CA  . ARG B 1 49  ? 11.692  6.266  41.784  1.00  24.40 ? 49   ARG B CA  1 
ATOM   2682 C C   . ARG B 1 49  ? 10.516  5.789  42.625  1.00  23.82 ? 49   ARG B C   1 
ATOM   2683 O O   . ARG B 1 49  ? 10.628  5.692  43.844  1.00  24.00 ? 49   ARG B O   1 
ATOM   2684 C CB  . ARG B 1 49  ? 12.964  5.496  42.176  1.00  24.21 ? 49   ARG B CB  1 
ATOM   2685 C CG  . ARG B 1 49  ? 12.848  3.992  42.027  1.00  23.70 ? 49   ARG B CG  1 
ATOM   2686 C CD  . ARG B 1 49  ? 14.182  3.316  42.213  1.00  23.22 ? 49   ARG B CD  1 
ATOM   2687 N NE  . ARG B 1 49  ? 15.204  3.716  41.232  1.00  22.92 ? 49   ARG B NE  1 
ATOM   2688 C CZ  . ARG B 1 49  ? 15.342  3.185  40.014  1.00  22.37 ? 49   ARG B CZ  1 
ATOM   2689 N NH1 . ARG B 1 49  ? 14.507  2.245  39.586  1.00  22.83 ? 49   ARG B NH1 1 
ATOM   2690 N NH2 . ARG B 1 49  ? 16.312  3.600  39.212  1.00  21.12 ? 49   ARG B NH2 1 
ATOM   2691 N N   . GLY B 1 50  ? 9.397   5.486  41.974  1.00  23.12 ? 50   GLY B N   1 
ATOM   2692 C CA  . GLY B 1 50  ? 8.228   4.970  42.685  1.00  22.83 ? 50   GLY B CA  1 
ATOM   2693 C C   . GLY B 1 50  ? 7.490   6.072  43.428  1.00  22.51 ? 50   GLY B C   1 
ATOM   2694 O O   . GLY B 1 50  ? 6.910   5.853  44.494  1.00  22.75 ? 50   GLY B O   1 
ATOM   2695 N N   . GLU B 1 51  ? 7.526   7.266  42.852  0.40  22.01 ? 51   GLU B N   1 
ATOM   2696 C CA  . GLU B 1 51  ? 6.823   8.404  43.398  0.40  21.59 ? 51   GLU B CA  1 
ATOM   2697 C C   . GLU B 1 51  ? 5.641   8.750  42.508  0.40  21.51 ? 51   GLU B C   1 
ATOM   2698 O O   . GLU B 1 51  ? 5.578   8.353  41.347  0.40  21.40 ? 51   GLU B O   1 
ATOM   2699 C CB  . GLU B 1 51  ? 7.761   9.608  43.505  0.40  21.59 ? 51   GLU B CB  1 
ATOM   2700 C CG  . GLU B 1 51  ? 9.029   9.363  44.313  0.40  21.24 ? 51   GLU B CG  1 
ATOM   2701 C CD  . GLU B 1 51  ? 8.916   9.828  45.746  0.40  20.79 ? 51   GLU B CD  1 
ATOM   2702 O OE1 . GLU B 1 51  ? 8.206   9.168  46.530  0.40  21.04 ? 51   GLU B OE1 1 
ATOM   2703 O OE2 . GLU B 1 51  ? 9.545   10.851 46.094  0.40  20.42 ? 51   GLU B OE2 1 
ATOM   2704 N N   . ASP B 1 52  ? 4.710   9.494  43.086  1.00  21.68 ? 52   ASP B N   1 
ATOM   2705 C CA  . ASP B 1 52  ? 3.553   10.044 42.411  1.00  21.66 ? 52   ASP B CA  1 
ATOM   2706 C C   . ASP B 1 52  ? 3.933   11.461 41.968  1.00  21.64 ? 52   ASP B C   1 
ATOM   2707 O O   . ASP B 1 52  ? 3.766   12.426 42.717  1.00  21.89 ? 52   ASP B O   1 
ATOM   2708 C CB  . ASP B 1 52  ? 2.390   10.081 43.407  1.00  21.73 ? 52   ASP B CB  1 
ATOM   2709 C CG  . ASP B 1 52  ? 1.044   10.089 42.732  1.00  22.69 ? 52   ASP B CG  1 
ATOM   2710 O OD1 . ASP B 1 52  ? 0.851   9.289  41.791  1.00  23.99 ? 52   ASP B OD1 1 
ATOM   2711 O OD2 . ASP B 1 52  ? 0.171   10.881 43.151  1.00  23.47 ? 52   ASP B OD2 1 
ATOM   2712 N N   . VAL B 1 53  ? 4.469   11.571 40.755  1.00  21.53 ? 53   VAL B N   1 
ATOM   2713 C CA  . VAL B 1 53  ? 5.038   12.822 40.237  1.00  21.44 ? 53   VAL B CA  1 
ATOM   2714 C C   . VAL B 1 53  ? 3.979   13.721 39.604  1.00  21.73 ? 53   VAL B C   1 
ATOM   2715 O O   . VAL B 1 53  ? 3.025   13.234 38.992  1.00  21.77 ? 53   VAL B O   1 
ATOM   2716 C CB  . VAL B 1 53  ? 6.169   12.535 39.218  1.00  21.34 ? 53   VAL B CB  1 
ATOM   2717 C CG1 . VAL B 1 53  ? 6.645   13.813 38.533  1.00  20.82 ? 53   VAL B CG1 1 
ATOM   2718 C CG2 . VAL B 1 53  ? 7.336   11.814 39.916  1.00  21.50 ? 53   VAL B CG2 1 
ATOM   2719 N N   . TYR B 1 54  ? 4.156   15.033 39.774  1.00  22.09 ? 54   TYR B N   1 
ATOM   2720 C CA  . TYR B 1 54  ? 3.261   16.047 39.216  1.00  22.32 ? 54   TYR B CA  1 
ATOM   2721 C C   . TYR B 1 54  ? 4.090   17.132 38.541  1.00  22.69 ? 54   TYR B C   1 
ATOM   2722 O O   . TYR B 1 54  ? 5.001   17.699 39.155  1.00  22.91 ? 54   TYR B O   1 
ATOM   2723 C CB  . TYR B 1 54  ? 2.378   16.640 40.319  1.00  22.11 ? 54   TYR B CB  1 
ATOM   2724 C CG  . TYR B 1 54  ? 1.376   15.644 40.838  1.00  22.57 ? 54   TYR B CG  1 
ATOM   2725 C CD1 . TYR B 1 54  ? 1.758   14.653 41.740  1.00  22.85 ? 54   TYR B CD1 1 
ATOM   2726 C CD2 . TYR B 1 54  ? 0.050   15.669 40.407  1.00  23.12 ? 54   TYR B CD2 1 
ATOM   2727 C CE1 . TYR B 1 54  ? 0.850   13.712 42.202  1.00  23.19 ? 54   TYR B CE1 1 
ATOM   2728 C CE2 . TYR B 1 54  ? -0.874  14.727 40.872  1.00  23.39 ? 54   TYR B CE2 1 
ATOM   2729 C CZ  . TYR B 1 54  ? -0.459  13.755 41.770  1.00  23.58 ? 54   TYR B CZ  1 
ATOM   2730 O OH  . TYR B 1 54  ? -1.347  12.826 42.246  1.00  24.95 ? 54   TYR B OH  1 
ATOM   2731 N N   . ILE B 1 55  ? 3.812   17.396 37.267  1.00  23.02 ? 55   ILE B N   1 
ATOM   2732 C CA  . ILE B 1 55  ? 4.497   18.482 36.571  1.00  23.08 ? 55   ILE B CA  1 
ATOM   2733 C C   . ILE B 1 55  ? 3.480   19.542 36.178  1.00  23.76 ? 55   ILE B C   1 
ATOM   2734 O O   . ILE B 1 55  ? 2.514   19.264 35.461  1.00  23.38 ? 55   ILE B O   1 
ATOM   2735 C CB  . ILE B 1 55  ? 5.330   17.999 35.351  1.00  22.79 ? 55   ILE B CB  1 
ATOM   2736 C CG1 . ILE B 1 55  ? 6.267   16.853 35.759  1.00  21.68 ? 55   ILE B CG1 1 
ATOM   2737 C CG2 . ILE B 1 55  ? 6.127   19.174 34.752  1.00  22.23 ? 55   ILE B CG2 1 
ATOM   2738 C CD1 . ILE B 1 55  ? 6.664   15.922 34.629  1.00  20.02 ? 55   ILE B CD1 1 
ATOM   2739 N N   . VAL B 1 56  ? 3.706   20.748 36.689  1.00  24.94 ? 56   VAL B N   1 
ATOM   2740 C CA  . VAL B 1 56  ? 2.839   21.894 36.422  1.00  26.09 ? 56   VAL B CA  1 
ATOM   2741 C C   . VAL B 1 56  ? 3.435   22.705 35.275  1.00  27.03 ? 56   VAL B C   1 
ATOM   2742 O O   . VAL B 1 56  ? 4.616   23.060 35.302  1.00  27.12 ? 56   VAL B O   1 
ATOM   2743 C CB  . VAL B 1 56  ? 2.656   22.775 37.672  1.00  25.84 ? 56   VAL B CB  1 
ATOM   2744 C CG1 . VAL B 1 56  ? 1.453   23.680 37.512  1.00  25.36 ? 56   VAL B CG1 1 
ATOM   2745 C CG2 . VAL B 1 56  ? 2.500   21.904 38.910  1.00  26.26 ? 56   VAL B CG2 1 
ATOM   2746 N N   . GLN B 1 57  ? 2.611   22.981 34.269  0.20  28.33 ? 57   GLN B N   1 
ATOM   2747 C CA  . GLN B 1 57  ? 3.080   23.587 33.029  0.20  29.64 ? 57   GLN B CA  1 
ATOM   2748 C C   . GLN B 1 57  ? 3.387   25.072 33.200  0.20  30.61 ? 57   GLN B C   1 
ATOM   2749 O O   . GLN B 1 57  ? 2.619   25.816 33.818  0.20  30.60 ? 57   GLN B O   1 
ATOM   2750 C CB  . GLN B 1 57  ? 2.070   23.355 31.902  0.20  29.56 ? 57   GLN B CB  1 
ATOM   2751 C CG  . GLN B 1 57  ? 1.335   24.596 31.431  0.20  29.66 ? 57   GLN B CG  1 
ATOM   2752 C CD  . GLN B 1 57  ? 1.854   25.107 30.098  0.20  29.65 ? 57   GLN B CD  1 
ATOM   2753 O OE1 . GLN B 1 57  ? 1.448   26.168 29.624  0.20  29.70 ? 57   GLN B OE1 1 
ATOM   2754 N NE2 . GLN B 1 57  ? 2.752   24.346 29.483  0.20  29.60 ? 57   GLN B NE2 1 
ATOM   2755 N N   . SER B 1 58  ? 4.526   25.474 32.638  1.00  31.99 ? 58   SER B N   1 
ATOM   2756 C CA  . SER B 1 58  ? 5.087   26.832 32.744  1.00  32.99 ? 58   SER B CA  1 
ATOM   2757 C C   . SER B 1 58  ? 4.247   27.945 32.093  1.00  33.30 ? 58   SER B C   1 
ATOM   2758 O O   . SER B 1 58  ? 3.439   27.689 31.193  1.00  33.50 ? 58   SER B O   1 
ATOM   2759 C CB  . SER B 1 58  ? 6.487   26.834 32.126  1.00  33.13 ? 58   SER B CB  1 
ATOM   2760 O OG  . SER B 1 58  ? 7.005   28.149 32.018  1.00  34.04 ? 58   SER B OG  1 
ATOM   2761 N N   . GLY B 1 59  ? 4.463   29.178 32.544  0.010 33.47 ? 59   GLY B N   1 
ATOM   2762 C CA  . GLY B 1 59  ? 3.774   30.332 31.979  0.010 33.61 ? 59   GLY B CA  1 
ATOM   2763 C C   . GLY B 1 59  ? 4.684   31.211 31.144  0.010 33.67 ? 59   GLY B C   1 
ATOM   2764 O O   . GLY B 1 59  ? 4.325   32.331 30.783  0.010 33.69 ? 59   GLY B O   1 
ATOM   2765 N N   . CYS B 1 60  ? 5.865   30.693 30.825  0.10  33.68 ? 60   CYS B N   1 
ATOM   2766 C CA  . CYS B 1 60  ? 6.853   31.438 30.048  0.10  33.66 ? 60   CYS B CA  1 
ATOM   2767 C C   . CYS B 1 60  ? 6.250   32.302 28.936  0.10  33.56 ? 60   CYS B C   1 
ATOM   2768 O O   . CYS B 1 60  ? 6.691   33.434 28.720  0.10  33.56 ? 60   CYS B O   1 
ATOM   2769 C CB  . CYS B 1 60  ? 7.905   30.486 29.469  0.10  33.68 ? 60   CYS B CB  1 
ATOM   2770 S SG  . CYS B 1 60  ? 8.907   31.193 28.138  0.10  33.79 ? 60   CYS B SG  1 
ATOM   2771 N N   . GLY B 1 61  ? 5.246   31.770 28.240  1.00  33.42 ? 61   GLY B N   1 
ATOM   2772 C CA  . GLY B 1 61  ? 4.670   32.442 27.076  1.00  33.14 ? 61   GLY B CA  1 
ATOM   2773 C C   . GLY B 1 61  ? 4.970   31.701 25.783  1.00  32.94 ? 61   GLY B C   1 
ATOM   2774 O O   . GLY B 1 61  ? 4.054   31.411 25.012  1.00  33.17 ? 61   GLY B O   1 
ATOM   2775 N N   . GLU B 1 62  ? 6.252   31.399 25.552  0.50  32.40 ? 62   GLU B N   1 
ATOM   2776 C CA  . GLU B 1 62  ? 6.702   30.645 24.379  0.50  31.76 ? 62   GLU B CA  1 
ATOM   2777 C C   . GLU B 1 62  ? 6.201   29.212 24.480  0.50  31.68 ? 62   GLU B C   1 
ATOM   2778 O O   . GLU B 1 62  ? 6.668   28.442 25.317  0.50  31.66 ? 62   GLU B O   1 
ATOM   2779 C CB  . GLU B 1 62  ? 8.227   30.668 24.279  0.50  31.58 ? 62   GLU B CB  1 
ATOM   2780 C CG  . GLU B 1 62  ? 8.770   30.624 22.857  0.50  30.89 ? 62   GLU B CG  1 
ATOM   2781 C CD  . GLU B 1 62  ? 8.455   29.328 22.142  0.50  29.95 ? 62   GLU B CD  1 
ATOM   2782 O OE1 . GLU B 1 62  ? 7.753   28.484 22.725  0.50  30.09 ? 62   GLU B OE1 1 
ATOM   2783 O OE2 . GLU B 1 62  ? 8.913   29.152 20.997  0.50  29.31 ? 62   GLU B OE2 1 
ATOM   2784 N N   . ILE B 1 63  ? 5.252   28.869 23.613  1.00  31.49 ? 63   ILE B N   1 
ATOM   2785 C CA  . ILE B 1 63  ? 4.479   27.637 23.734  1.00  31.45 ? 63   ILE B CA  1 
ATOM   2786 C C   . ILE B 1 63  ? 5.221   26.361 23.312  1.00  31.48 ? 63   ILE B C   1 
ATOM   2787 O O   . ILE B 1 63  ? 5.045   25.299 23.927  1.00  31.69 ? 63   ILE B O   1 
ATOM   2788 C CB  . ILE B 1 63  ? 3.164   27.739 22.947  1.00  31.41 ? 63   ILE B CB  1 
ATOM   2789 C CG1 . ILE B 1 63  ? 2.111   26.797 23.541  1.00  31.81 ? 63   ILE B CG1 1 
ATOM   2790 C CG2 . ILE B 1 63  ? 3.402   27.446 21.469  1.00  31.43 ? 63   ILE B CG2 1 
ATOM   2791 C CD1 . ILE B 1 63  ? 0.734   26.920 22.901  1.00  32.59 ? 63   ILE B CD1 1 
ATOM   2792 N N   . ASN B 1 64  ? 6.029   26.452 22.263  1.00  31.21 ? 64   ASN B N   1 
ATOM   2793 C CA  . ASN B 1 64  ? 6.753   25.278 21.799  1.00  31.08 ? 64   ASN B CA  1 
ATOM   2794 C C   . ASN B 1 64  ? 7.913   24.923 22.728  1.00  30.94 ? 64   ASN B C   1 
ATOM   2795 O O   . ASN B 1 64  ? 8.111   23.749 23.054  1.00  30.94 ? 64   ASN B O   1 
ATOM   2796 C CB  . ASN B 1 64  ? 7.158   25.441 20.337  1.00  30.95 ? 64   ASN B CB  1 
ATOM   2797 C CG  . ASN B 1 64  ? 5.959   25.741 19.449  1.00  31.65 ? 64   ASN B CG  1 
ATOM   2798 O OD1 . ASN B 1 64  ? 5.942   26.724 18.702  1.00  32.85 ? 64   ASN B OD1 1 
ATOM   2799 N ND2 . ASN B 1 64  ? 4.923   24.911 19.563  1.00  31.26 ? 64   ASN B ND2 1 
ATOM   2800 N N   . ASP B 1 65  ? 8.638   25.942 23.190  1.00  30.79 ? 65   ASP B N   1 
ATOM   2801 C CA  . ASP B 1 65  ? 9.684   25.762 24.192  1.00  30.57 ? 65   ASP B CA  1 
ATOM   2802 C C   . ASP B 1 65  ? 9.104   25.258 25.505  1.00  30.42 ? 65   ASP B C   1 
ATOM   2803 O O   . ASP B 1 65  ? 9.756   24.489 26.217  1.00  30.63 ? 65   ASP B O   1 
ATOM   2804 C CB  . ASP B 1 65  ? 10.447  27.064 24.430  1.00  30.70 ? 65   ASP B CB  1 
ATOM   2805 C CG  . ASP B 1 65  ? 11.214  27.534 23.202  1.00  30.90 ? 65   ASP B CG  1 
ATOM   2806 O OD1 . ASP B 1 65  ? 10.997  26.988 22.102  1.00  30.38 ? 65   ASP B OD1 1 
ATOM   2807 O OD2 . ASP B 1 65  ? 12.042  28.460 23.338  1.00  31.93 ? 65   ASP B OD2 1 
ATOM   2808 N N   . ASN B 1 66  ? 7.884   25.692 25.826  1.00  29.97 ? 66   ASN B N   1 
ATOM   2809 C CA  . ASN B 1 66  ? 7.176   25.171 26.995  1.00  29.49 ? 66   ASN B CA  1 
ATOM   2810 C C   . ASN B 1 66  ? 6.703   23.736 26.821  1.00  28.94 ? 66   ASN B C   1 
ATOM   2811 O O   . ASN B 1 66  ? 6.755   22.961 27.772  1.00  28.72 ? 66   ASN B O   1 
ATOM   2812 C CB  . ASN B 1 66  ? 6.003   26.068 27.388  1.00  29.66 ? 66   ASN B CB  1 
ATOM   2813 C CG  . ASN B 1 66  ? 6.423   27.221 28.290  1.00  30.67 ? 66   ASN B CG  1 
ATOM   2814 O OD1 . ASN B 1 66  ? 7.451   27.160 28.973  1.00  31.49 ? 66   ASN B OD1 1 
ATOM   2815 N ND2 . ASN B 1 66  ? 5.615   28.279 28.305  1.00  31.54 ? 66   ASN B ND2 1 
ATOM   2816 N N   . LEU B 1 67  ? 6.263   23.376 25.613  1.00  28.42 ? 67   LEU B N   1 
ATOM   2817 C CA  . LEU B 1 67  ? 5.741   22.029 25.370  1.00  27.82 ? 67   LEU B CA  1 
ATOM   2818 C C   . LEU B 1 67  ? 6.829   20.954 25.309  1.00  27.64 ? 67   LEU B C   1 
ATOM   2819 O O   . LEU B 1 67  ? 6.638   19.858 25.839  1.00  27.81 ? 67   LEU B O   1 
ATOM   2820 C CB  . LEU B 1 67  ? 4.861   21.968 24.112  1.00  27.66 ? 67   LEU B CB  1 
ATOM   2821 C CG  . LEU B 1 67  ? 4.125   20.634 23.900  1.00  26.99 ? 67   LEU B CG  1 
ATOM   2822 C CD1 . LEU B 1 67  ? 2.786   20.617 24.616  1.00  26.42 ? 67   LEU B CD1 1 
ATOM   2823 C CD2 . LEU B 1 67  ? 3.929   20.356 22.427  1.00  26.47 ? 67   LEU B CD2 1 
ATOM   2824 N N   . MET B 1 68  ? 7.952   21.252 24.658  0.10  27.28 ? 68   MET B N   1 
ATOM   2825 C CA  . MET B 1 68  ? 9.051   20.293 24.589  0.10  26.98 ? 68   MET B CA  1 
ATOM   2826 C C   . MET B 1 68  ? 9.598   20.019 25.984  0.10  26.96 ? 68   MET B C   1 
ATOM   2827 O O   . MET B 1 68  ? 9.801   18.867 26.369  0.10  26.89 ? 68   MET B O   1 
ATOM   2828 C CB  . MET B 1 68  ? 10.150  20.792 23.654  0.10  26.92 ? 68   MET B CB  1 
ATOM   2829 C CG  . MET B 1 68  ? 9.768   20.710 22.191  0.10  26.57 ? 68   MET B CG  1 
ATOM   2830 S SD  . MET B 1 68  ? 9.149   19.074 21.759  0.10  26.08 ? 68   MET B SD  1 
ATOM   2831 C CE  . MET B 1 68  ? 10.495  18.042 22.333  0.10  26.07 ? 68   MET B CE  1 
ATOM   2832 N N   . GLU B 1 69  ? 9.804   21.100 26.733  1.00  26.97 ? 69   GLU B N   1 
ATOM   2833 C CA  . GLU B 1 69  ? 10.243  21.042 28.135  1.00  27.28 ? 69   GLU B CA  1 
ATOM   2834 C C   . GLU B 1 69  ? 9.309   20.195 29.006  1.00  26.74 ? 69   GLU B C   1 
ATOM   2835 O O   . GLU B 1 69  ? 9.772   19.314 29.737  1.00  26.72 ? 69   GLU B O   1 
ATOM   2836 C CB  . GLU B 1 69  ? 10.379  22.460 28.717  1.00  27.58 ? 69   GLU B CB  1 
ATOM   2837 C CG  . GLU B 1 69  ? 11.072  22.524 30.077  1.00  29.62 ? 69   GLU B CG  1 
ATOM   2838 C CD  . GLU B 1 69  ? 11.209  23.947 30.605  1.00  33.05 ? 69   GLU B CD  1 
ATOM   2839 O OE1 . GLU B 1 69  ? 10.203  24.694 30.606  1.00  34.97 ? 69   GLU B OE1 1 
ATOM   2840 O OE2 . GLU B 1 69  ? 12.325  24.317 31.032  1.00  34.14 ? 69   GLU B OE2 1 
ATOM   2841 N N   . LEU B 1 70  ? 8.004   20.458 28.920  1.00  26.13 ? 70   LEU B N   1 
ATOM   2842 C CA  . LEU B 1 70  ? 7.023   19.632 29.610  1.00  25.57 ? 70   LEU B CA  1 
ATOM   2843 C C   . LEU B 1 70  ? 7.174   18.165 29.227  1.00  25.63 ? 70   LEU B C   1 
ATOM   2844 O O   . LEU B 1 70  ? 7.216   17.316 30.110  1.00  25.90 ? 70   LEU B O   1 
ATOM   2845 C CB  . LEU B 1 70  ? 5.592   20.116 29.352  1.00  25.40 ? 70   LEU B CB  1 
ATOM   2846 C CG  . LEU B 1 70  ? 4.413   19.271 29.878  1.00  24.99 ? 70   LEU B CG  1 
ATOM   2847 C CD1 . LEU B 1 70  ? 4.569   18.819 31.335  1.00  24.15 ? 70   LEU B CD1 1 
ATOM   2848 C CD2 . LEU B 1 70  ? 3.105   20.027 29.711  1.00  24.11 ? 70   LEU B CD2 1 
ATOM   2849 N N   . LEU B 1 71  ? 7.274   17.867 27.931  1.00  25.51 ? 71   LEU B N   1 
ATOM   2850 C CA  . LEU B 1 71  ? 7.410   16.477 27.468  1.00  25.45 ? 71   LEU B CA  1 
ATOM   2851 C C   . LEU B 1 71  ? 8.686   15.826 27.983  1.00  25.68 ? 71   LEU B C   1 
ATOM   2852 O O   . LEU B 1 71  ? 8.648   14.765 28.607  1.00  25.54 ? 71   LEU B O   1 
ATOM   2853 C CB  . LEU B 1 71  ? 7.379   16.391 25.943  1.00  25.13 ? 71   LEU B CB  1 
ATOM   2854 C CG  . LEU B 1 71  ? 6.089   16.787 25.223  1.00  25.06 ? 71   LEU B CG  1 
ATOM   2855 C CD1 . LEU B 1 71  ? 6.274   16.697 23.725  1.00  24.70 ? 71   LEU B CD1 1 
ATOM   2856 C CD2 . LEU B 1 71  ? 4.911   15.937 25.669  1.00  25.29 ? 71   LEU B CD2 1 
ATOM   2857 N N   . ILE B 1 72  ? 9.812   16.478 27.715  1.00  26.16 ? 72   ILE B N   1 
ATOM   2858 C CA  . ILE B 1 72  ? 11.129  16.009 28.151  1.00  26.46 ? 72   ILE B CA  1 
ATOM   2859 C C   . ILE B 1 72  ? 11.129  15.668 29.644  1.00  26.76 ? 72   ILE B C   1 
ATOM   2860 O O   . ILE B 1 72  ? 11.626  14.607 30.041  1.00  27.07 ? 72   ILE B O   1 
ATOM   2861 C CB  . ILE B 1 72  ? 12.231  17.038 27.795  1.00  26.38 ? 72   ILE B CB  1 
ATOM   2862 C CG1 . ILE B 1 72  ? 12.581  16.950 26.311  1.00  26.25 ? 72   ILE B CG1 1 
ATOM   2863 C CG2 . ILE B 1 72  ? 13.472  16.803 28.597  1.00  26.34 ? 72   ILE B CG2 1 
ATOM   2864 C CD1 . ILE B 1 72  ? 12.964  18.283 25.711  1.00  26.80 ? 72   ILE B CD1 1 
ATOM   2865 N N   . MET B 1 73  ? 10.549  16.550 30.457  0.97  26.81 ? 73   MET B N   1 
ATOM   2866 C CA  . MET B 1 73  ? 10.345  16.257 31.872  0.97  26.99 ? 73   MET B CA  1 
ATOM   2867 C C   . MET B 1 73  ? 9.525   14.977 32.098  0.97  26.82 ? 73   MET B C   1 
ATOM   2868 O O   . MET B 1 73  ? 9.981   14.063 32.795  0.97  26.67 ? 73   MET B O   1 
ATOM   2869 C CB  . MET B 1 73  ? 9.691   17.440 32.566  0.97  27.20 ? 73   MET B CB  1 
ATOM   2870 C CG  . MET B 1 73  ? 10.644  18.576 32.832  0.97  28.03 ? 73   MET B CG  1 
ATOM   2871 S SD  . MET B 1 73  ? 10.150  19.484 34.300  0.97  30.13 ? 73   MET B SD  1 
ATOM   2872 C CE  . MET B 1 73  ? 10.459  18.253 35.588  0.97  30.11 ? 73   MET B CE  1 
ATOM   2873 N N   . ILE B 1 74  ? 8.337   14.907 31.493  1.00  26.58 ? 74   ILE B N   1 
ATOM   2874 C CA  . ILE B 1 74  ? 7.532   13.688 31.509  1.00  26.42 ? 74   ILE B CA  1 
ATOM   2875 C C   . ILE B 1 74  ? 8.411   12.497 31.150  1.00  26.37 ? 74   ILE B C   1 
ATOM   2876 O O   . ILE B 1 74  ? 8.322   11.444 31.790  1.00  26.29 ? 74   ILE B O   1 
ATOM   2877 C CB  . ILE B 1 74  ? 6.348   13.765 30.517  1.00  26.37 ? 74   ILE B CB  1 
ATOM   2878 C CG1 . ILE B 1 74  ? 5.383   14.882 30.916  1.00  26.86 ? 74   ILE B CG1 1 
ATOM   2879 C CG2 . ILE B 1 74  ? 5.609   12.436 30.442  1.00  26.12 ? 74   ILE B CG2 1 
ATOM   2880 C CD1 . ILE B 1 74  ? 4.555   15.440 29.745  1.00  27.72 ? 74   ILE B CD1 1 
ATOM   2881 N N   . ASN B 1 75  ? 9.262   12.669 30.137  1.00  26.29 ? 75   ASN B N   1 
ATOM   2882 C CA  . ASN B 1 75  ? 10.107  11.578 29.685  1.00  26.11 ? 75   ASN B CA  1 
ATOM   2883 C C   . ASN B 1 75  ? 11.097  11.187 30.753  1.00  25.97 ? 75   ASN B C   1 
ATOM   2884 O O   . ASN B 1 75  ? 11.153  10.018 31.135  1.00  25.95 ? 75   ASN B O   1 
ATOM   2885 C CB  . ASN B 1 75  ? 10.847  11.894 28.385  1.00  26.13 ? 75   ASN B CB  1 
ATOM   2886 C CG  . ASN B 1 75  ? 11.608  10.682 27.856  1.00  26.24 ? 75   ASN B CG  1 
ATOM   2887 O OD1 . ASN B 1 75  ? 11.156  9.542  28.012  1.00  25.75 ? 75   ASN B OD1 1 
ATOM   2888 N ND2 . ASN B 1 75  ? 12.770  10.918 27.249  1.00  26.11 ? 75   ASN B ND2 1 
ATOM   2889 N N   . ALA B 1 76  ? 11.860  12.169 31.233  1.00  25.80 ? 76   ALA B N   1 
ATOM   2890 C CA  . ALA B 1 76  ? 12.879  11.945 32.261  1.00  25.97 ? 76   ALA B CA  1 
ATOM   2891 C C   . ALA B 1 76  ? 12.296  11.201 33.453  1.00  26.03 ? 76   ALA B C   1 
ATOM   2892 O O   . ALA B 1 76  ? 12.837  10.191 33.905  1.00  25.95 ? 76   ALA B O   1 
ATOM   2893 C CB  . ALA B 1 76  ? 13.466  13.263 32.714  1.00  26.07 ? 76   ALA B CB  1 
ATOM   2894 N N   . CYS B 1 77  ? 11.168  11.706 33.939  1.00  26.09 ? 77   CYS B N   1 
ATOM   2895 C CA  . CYS B 1 77  ? 10.457  11.108 35.059  1.00  25.95 ? 77   CYS B CA  1 
ATOM   2896 C C   . CYS B 1 77  ? 9.982   9.669  34.850  1.00  26.07 ? 77   CYS B C   1 
ATOM   2897 O O   . CYS B 1 77  ? 9.953   8.908  35.809  1.00  26.25 ? 77   CYS B O   1 
ATOM   2898 C CB  . CYS B 1 77  ? 9.281   11.994 35.466  1.00  25.81 ? 77   CYS B CB  1 
ATOM   2899 S SG  . CYS B 1 77  ? 9.790   13.487 36.315  1.00  25.68 ? 77   CYS B SG  1 
ATOM   2900 N N   . LYS B 1 78  ? 9.610   9.285  33.628  1.00  26.19 ? 78   LYS B N   1 
ATOM   2901 C CA  . LYS B 1 78  ? 9.102   7.926  33.391  1.00  26.27 ? 78   LYS B CA  1 
ATOM   2902 C C   . LYS B 1 78  ? 10.208  6.885  33.359  1.00  25.99 ? 78   LYS B C   1 
ATOM   2903 O O   . LYS B 1 78  ? 10.088  5.809  33.965  1.00  25.90 ? 78   LYS B O   1 
ATOM   2904 C CB  . LYS B 1 78  ? 8.284   7.845  32.103  1.00  26.51 ? 78   LYS B CB  1 
ATOM   2905 C CG  . LYS B 1 78  ? 6.774   7.979  32.295  1.00  27.85 ? 78   LYS B CG  1 
ATOM   2906 C CD  . LYS B 1 78  ? 6.123   6.703  32.850  1.00  29.37 ? 78   LYS B CD  1 
ATOM   2907 C CE  . LYS B 1 78  ? 4.624   6.679  32.558  1.00  29.24 ? 78   LYS B CE  1 
ATOM   2908 N NZ  . LYS B 1 78  ? 3.857   5.757  33.435  1.00  29.19 ? 78   LYS B NZ  1 
ATOM   2909 N N   . ILE B 1 79  ? 11.283  7.209  32.651  1.00  25.69 ? 79   ILE B N   1 
ATOM   2910 C CA  . ILE B 1 79  ? 12.428  6.308  32.565  1.00  25.42 ? 79   ILE B CA  1 
ATOM   2911 C C   . ILE B 1 79  ? 13.196  6.259  33.891  1.00  25.02 ? 79   ILE B C   1 
ATOM   2912 O O   . ILE B 1 79  ? 13.920  5.300  34.165  1.00  24.99 ? 79   ILE B O   1 
ATOM   2913 C CB  . ILE B 1 79  ? 13.343  6.638  31.356  1.00  25.43 ? 79   ILE B CB  1 
ATOM   2914 C CG1 . ILE B 1 79  ? 13.561  8.163  31.251  1.00  25.63 ? 79   ILE B CG1 1 
ATOM   2915 C CG2 . ILE B 1 79  ? 12.743  6.021  30.089  1.00  25.23 ? 79   ILE B CG2 1 
ATOM   2916 C CD1 . ILE B 1 79  ? 13.990  8.696  29.872  1.00  26.00 ? 79   ILE B CD1 1 
ATOM   2917 N N   . ALA B 1 80  ? 13.003  7.279  34.722  1.00  24.47 ? 80   ALA B N   1 
ATOM   2918 C CA  . ALA B 1 80  ? 13.554  7.267  36.066  1.00  24.06 ? 80   ALA B CA  1 
ATOM   2919 C C   . ALA B 1 80  ? 12.660  6.496  37.043  1.00  23.79 ? 80   ALA B C   1 
ATOM   2920 O O   . ALA B 1 80  ? 12.833  6.593  38.256  1.00  23.46 ? 80   ALA B O   1 
ATOM   2921 C CB  . ALA B 1 80  ? 13.784  8.682  36.553  1.00  24.24 ? 80   ALA B CB  1 
ATOM   2922 N N   . SER B 1 81  ? 11.707  5.735  36.503  1.00  23.62 ? 81   SER B N   1 
ATOM   2923 C CA  . SER B 1 81  ? 10.848  4.815  37.278  1.00  23.32 ? 81   SER B CA  1 
ATOM   2924 C C   . SER B 1 81  ? 9.873   5.509  38.231  1.00  23.05 ? 81   SER B C   1 
ATOM   2925 O O   . SER B 1 81  ? 9.548   4.969  39.294  1.00  23.27 ? 81   SER B O   1 
ATOM   2926 C CB  . SER B 1 81  ? 11.679  3.780  38.062  1.00  23.21 ? 81   SER B CB  1 
ATOM   2927 O OG  . SER B 1 81  ? 12.826  3.352  37.347  1.00  23.64 ? 81   SER B OG  1 
ATOM   2928 N N   . ALA B 1 82  ? 9.411   6.703  37.869  1.00  22.60 ? 82   ALA B N   1 
ATOM   2929 C CA  . ALA B 1 82  ? 8.309   7.312  38.600  1.00  22.31 ? 82   ALA B CA  1 
ATOM   2930 C C   . ALA B 1 82  ? 7.113   6.358  38.558  1.00  22.27 ? 82   ALA B C   1 
ATOM   2931 O O   . ALA B 1 82  ? 6.862   5.696  37.545  1.00  22.48 ? 82   ALA B O   1 
ATOM   2932 C CB  . ALA B 1 82  ? 7.946   8.655  38.011  1.00  22.05 ? 82   ALA B CB  1 
ATOM   2933 N N   . SER B 1 83  ? 6.400   6.262  39.671  0.50  22.18 ? 83   SER B N   1 
ATOM   2934 C CA  . SER B 1 83  ? 5.262   5.365  39.767  0.50  22.22 ? 83   SER B CA  1 
ATOM   2935 C C   . SER B 1 83  ? 4.099   5.811  38.875  0.50  22.36 ? 83   SER B C   1 
ATOM   2936 O O   . SER B 1 83  ? 3.348   4.978  38.365  0.50  22.34 ? 83   SER B O   1 
ATOM   2937 C CB  . SER B 1 83  ? 4.813   5.250  41.223  0.50  22.19 ? 83   SER B CB  1 
ATOM   2938 O OG  . SER B 1 83  ? 3.497   4.709  41.309  0.50  22.19 ? 83   SER B OG  1 
ATOM   2939 N N   . ARG B 1 84  ? 3.973   7.125  38.681  1.00  22.60 ? 84   ARG B N   1 
ATOM   2940 C CA  . ARG B 1 84  ? 2.868   7.737  37.931  1.00  22.73 ? 84   ARG B CA  1 
ATOM   2941 C C   . ARG B 1 84  ? 3.229   9.199  37.662  1.00  22.86 ? 84   ARG B C   1 
ATOM   2942 O O   . ARG B 1 84  ? 3.737   9.881  38.554  1.00  23.06 ? 84   ARG B O   1 
ATOM   2943 C CB  . ARG B 1 84  ? 1.560   7.650  38.739  1.00  22.70 ? 84   ARG B CB  1 
ATOM   2944 C CG  . ARG B 1 84  ? 0.266   7.864  37.939  1.00  22.96 ? 84   ARG B CG  1 
ATOM   2945 C CD  . ARG B 1 84  ? -1.001  7.656  38.798  1.00  23.10 ? 84   ARG B CD  1 
ATOM   2946 N NE  . ARG B 1 84  ? -1.114  8.651  39.865  1.00  22.61 ? 84   ARG B NE  1 
ATOM   2947 C CZ  . ARG B 1 84  ? -2.093  8.710  40.762  1.00  22.62 ? 84   ARG B CZ  1 
ATOM   2948 N NH1 . ARG B 1 84  ? -3.087  7.827  40.751  1.00  23.16 ? 84   ARG B NH1 1 
ATOM   2949 N NH2 . ARG B 1 84  ? -2.070  9.666  41.683  1.00  22.26 ? 84   ARG B NH2 1 
ATOM   2950 N N   . VAL B 1 85  ? 2.985   9.670  36.437  1.00  22.98 ? 85   VAL B N   1 
ATOM   2951 C CA  . VAL B 1 85  ? 3.285   11.061 36.054  1.00  23.04 ? 85   VAL B CA  1 
ATOM   2952 C C   . VAL B 1 85  ? 2.021   11.819 35.657  1.00  23.08 ? 85   VAL B C   1 
ATOM   2953 O O   . VAL B 1 85  ? 1.418   11.547 34.615  1.00  23.20 ? 85   VAL B O   1 
ATOM   2954 C CB  . VAL B 1 85  ? 4.330   11.154 34.911  1.00  22.90 ? 85   VAL B CB  1 
ATOM   2955 C CG1 . VAL B 1 85  ? 4.441   12.581 34.393  1.00  22.61 ? 85   VAL B CG1 1 
ATOM   2956 C CG2 . VAL B 1 85  ? 5.679   10.688 35.397  1.00  23.47 ? 85   VAL B CG2 1 
ATOM   2957 N N   . THR B 1 86  ? 1.618   12.764 36.495  1.00  23.04 ? 86   THR B N   1 
ATOM   2958 C CA  . THR B 1 86  ? 0.511   13.631 36.151  1.00  23.03 ? 86   THR B CA  1 
ATOM   2959 C C   . THR B 1 86  ? 1.047   14.975 35.697  1.00  23.27 ? 86   THR B C   1 
ATOM   2960 O O   . THR B 1 86  ? 2.015   15.496 36.253  1.00  23.14 ? 86   THR B O   1 
ATOM   2961 C CB  . THR B 1 86  ? -0.450  13.818 37.329  1.00  22.94 ? 86   THR B CB  1 
ATOM   2962 O OG1 . THR B 1 86  ? -0.889  12.535 37.785  1.00  22.85 ? 86   THR B OG1 1 
ATOM   2963 C CG2 . THR B 1 86  ? -1.662  14.644 36.925  1.00  22.30 ? 86   THR B CG2 1 
ATOM   2964 N N   . THR B 1 87  ? 0.413   15.516 34.666  1.00  23.55 ? 87   THR B N   1 
ATOM   2965 C CA  . THR B 1 87  ? 0.685   16.861 34.220  1.00  23.75 ? 87   THR B CA  1 
ATOM   2966 C C   . THR B 1 87  ? -0.487  17.739 34.612  1.00  24.07 ? 87   THR B C   1 
ATOM   2967 O O   . THR B 1 87  ? -1.649  17.442 34.295  1.00  23.93 ? 87   THR B O   1 
ATOM   2968 C CB  . THR B 1 87  ? 0.849   16.912 32.714  1.00  23.74 ? 87   THR B CB  1 
ATOM   2969 O OG1 . THR B 1 87  ? -0.299  16.312 32.109  1.00  23.74 ? 87   THR B OG1 1 
ATOM   2970 C CG2 . THR B 1 87  ? 2.085   16.144 32.289  1.00  23.67 ? 87   THR B CG2 1 
ATOM   2971 N N   . VAL B 1 88  ? -0.169  18.810 35.326  1.00  24.47 ? 88   VAL B N   1 
ATOM   2972 C CA  . VAL B 1 88  ? -1.148  19.812 35.694  1.00  24.83 ? 88   VAL B CA  1 
ATOM   2973 C C   . VAL B 1 88  ? -0.956  20.901 34.658  1.00  25.07 ? 88   VAL B C   1 
ATOM   2974 O O   . VAL B 1 88  ? -0.048  21.710 34.764  1.00  25.04 ? 88   VAL B O   1 
ATOM   2975 C CB  . VAL B 1 88  ? -0.921  20.332 37.139  1.00  24.80 ? 88   VAL B CB  1 
ATOM   2976 C CG1 . VAL B 1 88  ? -2.000  21.317 37.539  1.00  24.90 ? 88   VAL B CG1 1 
ATOM   2977 C CG2 . VAL B 1 88  ? -0.891  19.169 38.132  1.00  24.81 ? 88   VAL B CG2 1 
ATOM   2978 N N   . ILE B 1 89  ? -1.784  20.874 33.621  1.00  25.66 ? 89   ILE B N   1 
ATOM   2979 C CA  . ILE B 1 89  ? -1.653  21.792 32.496  1.00  26.12 ? 89   ILE B CA  1 
ATOM   2980 C C   . ILE B 1 89  ? -2.828  22.750 32.498  1.00  26.46 ? 89   ILE B C   1 
ATOM   2981 O O   . ILE B 1 89  ? -3.812  22.523 31.787  1.00  26.32 ? 89   ILE B O   1 
ATOM   2982 C CB  . ILE B 1 89  ? -1.620  21.048 31.146  1.00  26.10 ? 89   ILE B CB  1 
ATOM   2983 C CG1 . ILE B 1 89  ? -0.622  19.888 31.195  1.00  25.79 ? 89   ILE B CG1 1 
ATOM   2984 C CG2 . ILE B 1 89  ? -1.269  22.017 30.018  1.00  26.64 ? 89   ILE B CG2 1 
ATOM   2985 C CD1 . ILE B 1 89  ? -0.740  18.939 30.037  1.00  26.16 ? 89   ILE B CD1 1 
ATOM   2986 N N   . PRO B 1 90  ? -2.725  23.830 33.296  1.00  26.87 ? 90   PRO B N   1 
ATOM   2987 C CA  . PRO B 1 90  ? -3.817  24.774 33.521  1.00  27.11 ? 90   PRO B CA  1 
ATOM   2988 C C   . PRO B 1 90  ? -4.427  25.289 32.214  1.00  27.35 ? 90   PRO B C   1 
ATOM   2989 O O   . PRO B 1 90  ? -5.650  25.280 32.072  1.00  26.96 ? 90   PRO B O   1 
ATOM   2990 C CB  . PRO B 1 90  ? -3.136  25.901 34.311  1.00  27.16 ? 90   PRO B CB  1 
ATOM   2991 C CG  . PRO B 1 90  ? -1.995  25.241 34.989  1.00  26.62 ? 90   PRO B CG  1 
ATOM   2992 C CD  . PRO B 1 90  ? -1.490  24.283 33.963  1.00  26.90 ? 90   PRO B CD  1 
ATOM   2993 N N   . CYS B 1 91  ? -3.573  25.707 31.275  1.00  27.84 ? 91   CYS B N   1 
ATOM   2994 C CA  . CYS B 1 91  ? -4.014  26.131 29.950  1.00  28.18 ? 91   CYS B CA  1 
ATOM   2995 C C   . CYS B 1 91  ? -3.427  25.222 28.873  1.00  28.00 ? 91   CYS B C   1 
ATOM   2996 O O   . CYS B 1 91  ? -2.245  25.309 28.536  1.00  28.05 ? 91   CYS B O   1 
ATOM   2997 C CB  . CYS B 1 91  ? -3.651  27.592 29.694  1.00  28.26 ? 91   CYS B CB  1 
ATOM   2998 S SG  . CYS B 1 91  ? -4.233  28.175 28.097  1.00  29.63 ? 91   CYS B SG  1 
ATOM   2999 N N   . PHE B 1 92  ? -4.278  24.344 28.355  1.00  27.96 ? 92   PHE B N   1 
ATOM   3000 C CA  . PHE B 1 92  ? -3.881  23.293 27.427  1.00  27.75 ? 92   PHE B CA  1 
ATOM   3001 C C   . PHE B 1 92  ? -3.436  23.897 26.104  1.00  27.82 ? 92   PHE B C   1 
ATOM   3002 O O   . PHE B 1 92  ? -4.156  24.712 25.519  1.00  27.71 ? 92   PHE B O   1 
ATOM   3003 C CB  . PHE B 1 92  ? -5.051  22.334 27.214  1.00  27.66 ? 92   PHE B CB  1 
ATOM   3004 C CG  . PHE B 1 92  ? -4.658  21.018 26.642  1.00  26.77 ? 92   PHE B CG  1 
ATOM   3005 C CD1 . PHE B 1 92  ? -4.208  20.003 27.470  1.00  26.50 ? 92   PHE B CD1 1 
ATOM   3006 C CD2 . PHE B 1 92  ? -4.753  20.783 25.278  1.00  26.07 ? 92   PHE B CD2 1 
ATOM   3007 C CE1 . PHE B 1 92  ? -3.849  18.773 26.945  1.00  26.15 ? 92   PHE B CE1 1 
ATOM   3008 C CE2 . PHE B 1 92  ? -4.396  19.558 24.742  1.00  25.73 ? 92   PHE B CE2 1 
ATOM   3009 C CZ  . PHE B 1 92  ? -3.941  18.551 25.576  1.00  25.74 ? 92   PHE B CZ  1 
ATOM   3010 N N   . PRO B 1 93  ? -2.234  23.519 25.644  1.00  28.05 ? 93   PRO B N   1 
ATOM   3011 C CA  . PRO B 1 93  ? -1.697  24.103 24.414  1.00  28.41 ? 93   PRO B CA  1 
ATOM   3012 C C   . PRO B 1 93  ? -2.435  23.637 23.163  1.00  28.82 ? 93   PRO B C   1 
ATOM   3013 O O   . PRO B 1 93  ? -2.865  22.484 23.092  1.00  29.05 ? 93   PRO B O   1 
ATOM   3014 C CB  . PRO B 1 93  ? -0.232  23.638 24.385  1.00  28.39 ? 93   PRO B CB  1 
ATOM   3015 C CG  . PRO B 1 93  ? -0.045  22.699 25.518  1.00  28.03 ? 93   PRO B CG  1 
ATOM   3016 C CD  . PRO B 1 93  ? -1.299  22.583 26.303  1.00  28.02 ? 93   PRO B CD  1 
ATOM   3017 N N   . TYR B 1 94  ? -2.589  24.543 22.198  1.00  29.29 ? 94   TYR B N   1 
ATOM   3018 C CA  . TYR B 1 94  ? -3.172  24.232 20.886  1.00  29.76 ? 94   TYR B CA  1 
ATOM   3019 C C   . TYR B 1 94  ? -4.645  23.826 20.980  1.00  30.28 ? 94   TYR B C   1 
ATOM   3020 O O   . TYR B 1 94  ? -5.224  23.301 20.026  1.00  30.35 ? 94   TYR B O   1 
ATOM   3021 C CB  . TYR B 1 94  ? -2.331  23.174 20.144  1.00  29.61 ? 94   TYR B CB  1 
ATOM   3022 C CG  . TYR B 1 94  ? -0.994  23.684 19.633  1.00  28.98 ? 94   TYR B CG  1 
ATOM   3023 C CD1 . TYR B 1 94  ? 0.107   23.799 20.483  1.00  28.45 ? 94   TYR B CD1 1 
ATOM   3024 C CD2 . TYR B 1 94  ? -0.834  24.044 18.294  1.00  28.33 ? 94   TYR B CD2 1 
ATOM   3025 C CE1 . TYR B 1 94  ? 1.327   24.264 20.010  1.00  28.73 ? 94   TYR B CE1 1 
ATOM   3026 C CE2 . TYR B 1 94  ? 0.378   24.506 17.808  1.00  27.98 ? 94   TYR B CE2 1 
ATOM   3027 C CZ  . TYR B 1 94  ? 1.455   24.614 18.666  1.00  28.80 ? 94   TYR B CZ  1 
ATOM   3028 O OH  . TYR B 1 94  ? 2.661   25.076 18.182  1.00  29.25 ? 94   TYR B OH  1 
ATOM   3029 N N   . ALA B 1 95  ? -5.239  24.104 22.137  1.00  31.04 ? 95   ALA B N   1 
ATOM   3030 C CA  . ALA B 1 95  ? -6.637  23.778 22.430  1.00  32.01 ? 95   ALA B CA  1 
ATOM   3031 C C   . ALA B 1 95  ? -7.647  24.396 21.456  1.00  32.65 ? 95   ALA B C   1 
ATOM   3032 O O   . ALA B 1 95  ? -8.761  23.893 21.316  1.00  32.81 ? 95   ALA B O   1 
ATOM   3033 C CB  . ALA B 1 95  ? -6.977  24.176 23.875  1.00  31.94 ? 95   ALA B CB  1 
ATOM   3034 N N   . ARG B 1 96  ? -7.258  25.485 20.796  0.95  33.58 ? 96   ARG B N   1 
ATOM   3035 C CA  . ARG B 1 96  ? -8.101  26.126 19.790  0.95  34.49 ? 96   ARG B CA  1 
ATOM   3036 C C   . ARG B 1 96  ? -7.991  25.420 18.451  0.95  34.59 ? 96   ARG B C   1 
ATOM   3037 O O   . ARG B 1 96  ? -8.681  25.787 17.500  0.95  34.71 ? 96   ARG B O   1 
ATOM   3038 C CB  . ARG B 1 96  ? -7.710  27.591 19.604  0.95  34.89 ? 96   ARG B CB  1 
ATOM   3039 C CG  . ARG B 1 96  ? -8.280  28.552 20.643  0.95  36.48 ? 96   ARG B CG  1 
ATOM   3040 C CD  . ARG B 1 96  ? -7.767  29.966 20.397  0.95  39.24 ? 96   ARG B CD  1 
ATOM   3041 N NE  . ARG B 1 96  ? -6.315  29.979 20.180  0.95  41.54 ? 96   ARG B NE  1 
ATOM   3042 C CZ  . ARG B 1 96  ? -5.597  31.058 19.859  0.95  43.64 ? 96   ARG B CZ  1 
ATOM   3043 N NH1 . ARG B 1 96  ? -6.182  32.245 19.717  0.95  45.02 ? 96   ARG B NH1 1 
ATOM   3044 N NH2 . ARG B 1 96  ? -4.282  30.951 19.678  0.95  44.02 ? 96   ARG B NH2 1 
ATOM   3045 N N   . GLN B 1 97  ? -7.109  24.427 18.369  0.10  34.91 ? 97   GLN B N   1 
ATOM   3046 C CA  . GLN B 1 97  ? -6.948  23.637 17.152  0.10  35.21 ? 97   GLN B CA  1 
ATOM   3047 C C   . GLN B 1 97  ? -7.481  22.228 17.377  0.10  35.48 ? 97   GLN B C   1 
ATOM   3048 O O   . GLN B 1 97  ? -6.749  21.244 17.278  0.10  35.48 ? 97   GLN B O   1 
ATOM   3049 C CB  . GLN B 1 97  ? -5.486  23.631 16.692  0.10  35.18 ? 97   GLN B CB  1 
ATOM   3050 C CG  . GLN B 1 97  ? -5.072  24.929 15.997  0.10  35.07 ? 97   GLN B CG  1 
ATOM   3051 C CD  . GLN B 1 97  ? -3.565  25.115 15.899  0.10  34.91 ? 97   GLN B CD  1 
ATOM   3052 O OE1 . GLN B 1 97  ? -2.847  24.245 15.408  0.10  34.76 ? 97   GLN B OE1 1 
ATOM   3053 N NE2 . GLN B 1 97  ? -3.086  26.268 16.350  0.10  34.95 ? 97   GLN B NE2 1 
ATOM   3054 N N   . ASP B 1 98  ? -8.776  22.154 17.674  0.10  35.85 ? 98   ASP B N   1 
ATOM   3055 C CA  . ASP B 1 98  ? -9.433  20.909 18.044  0.10  36.25 ? 98   ASP B CA  1 
ATOM   3056 C C   . ASP B 1 98  ? -10.265 20.338 16.901  0.10  36.61 ? 98   ASP B C   1 
ATOM   3057 O O   . ASP B 1 98  ? -10.908 19.300 17.054  0.10  36.62 ? 98   ASP B O   1 
ATOM   3058 C CB  . ASP B 1 98  ? -10.338 21.150 19.249  0.10  36.18 ? 98   ASP B CB  1 
ATOM   3059 C CG  . ASP B 1 98  ? -11.242 22.351 19.058  0.10  36.10 ? 98   ASP B CG  1 
ATOM   3060 O OD1 . ASP B 1 98  ? -10.896 23.227 18.239  0.10  36.06 ? 98   ASP B OD1 1 
ATOM   3061 O OD2 . ASP B 1 98  ? -12.295 22.424 19.720  0.10  35.95 ? 98   ASP B OD2 1 
ATOM   3062 N N   . LYS B 1 99  ? -10.255 21.016 15.759  0.10  37.12 ? 99   LYS B N   1 
ATOM   3063 C CA  . LYS B 1 99  ? -11.051 20.578 14.617  0.10  37.61 ? 99   LYS B CA  1 
ATOM   3064 C C   . LYS B 1 99  ? -10.512 21.094 13.283  0.10  38.04 ? 99   LYS B C   1 
ATOM   3065 O O   . LYS B 1 99  ? -9.771  22.080 13.240  0.10  38.10 ? 99   LYS B O   1 
ATOM   3066 C CB  . LYS B 1 99  ? -12.515 20.989 14.796  0.10  37.54 ? 99   LYS B CB  1 
ATOM   3067 C CG  . LYS B 1 99  ? -12.732 22.488 14.900  0.10  37.47 ? 99   LYS B CG  1 
ATOM   3068 C CD  . LYS B 1 99  ? -14.201 22.815 15.102  0.10  37.30 ? 99   LYS B CD  1 
ATOM   3069 C CE  . LYS B 1 99  ? -14.435 24.315 15.130  0.10  37.29 ? 99   LYS B CE  1 
ATOM   3070 N NZ  . LYS B 1 99  ? -15.882 24.643 15.253  0.10  37.33 ? 99   LYS B NZ  1 
ATOM   3071 N N   . LYS B 1 100 ? -10.901 20.415 12.202  1.00  38.63 ? 100  LYS B N   1 
ATOM   3072 C CA  . LYS B 1 100 ? -10.474 20.750 10.836  1.00  39.07 ? 100  LYS B CA  1 
ATOM   3073 C C   . LYS B 1 100 ? -11.092 22.035 10.306  1.00  39.10 ? 100  LYS B C   1 
ATOM   3074 O O   . LYS B 1 100 ? -10.503 22.689 9.448   1.00  39.43 ? 100  LYS B O   1 
ATOM   3075 C CB  . LYS B 1 100 ? -10.831 19.628 9.864   1.00  39.20 ? 100  LYS B CB  1 
ATOM   3076 C CG  . LYS B 1 100 ? -9.871  18.454 9.803   1.00  40.23 ? 100  LYS B CG  1 
ATOM   3077 C CD  . LYS B 1 100 ? -10.303 17.535 8.667   1.00  42.22 ? 100  LYS B CD  1 
ATOM   3078 C CE  . LYS B 1 100 ? -9.485  16.255 8.590   1.00  43.71 ? 100  LYS B CE  1 
ATOM   3079 N NZ  . LYS B 1 100 ? -9.961  15.409 7.401   1.00  44.72 ? 100  LYS B NZ  1 
ATOM   3080 N N   . ASP B 1 101 ? -12.281 22.378 10.805  0.010 39.06 ? 101  ASP B N   1 
ATOM   3081 C CA  . ASP B 1 101 ? -13.037 23.560 10.362  0.010 38.91 ? 101  ASP B CA  1 
ATOM   3082 C C   . ASP B 1 101 ? -13.171 23.658 8.841   0.010 38.77 ? 101  ASP B C   1 
ATOM   3083 O O   . ASP B 1 101 ? -12.749 24.649 8.240   0.010 38.77 ? 101  ASP B O   1 
ATOM   3084 C CB  . ASP B 1 101 ? -12.423 24.849 10.921  0.010 38.95 ? 101  ASP B CB  1 
ATOM   3085 C CG  . ASP B 1 101 ? -12.521 24.933 12.431  0.010 38.97 ? 101  ASP B CG  1 
ATOM   3086 O OD1 . ASP B 1 101 ? -13.434 24.303 13.004  0.010 38.99 ? 101  ASP B OD1 1 
ATOM   3087 O OD2 . ASP B 1 101 ? -11.686 25.632 13.043  0.010 38.98 ? 101  ASP B OD2 1 
ATOM   3088 N N   . LYS B 1 102 ? -13.764 22.625 8.240   1.00  38.57 ? 102  LYS B N   1 
ATOM   3089 C CA  . LYS B 1 102 ? -13.936 22.517 6.779   1.00  38.19 ? 102  LYS B CA  1 
ATOM   3090 C C   . LYS B 1 102 ? -12.638 22.710 5.975   1.00  37.69 ? 102  LYS B C   1 
ATOM   3091 O O   . LYS B 1 102 ? -12.674 22.906 4.760   1.00  37.80 ? 102  LYS B O   1 
ATOM   3092 C CB  . LYS B 1 102 ? -15.022 23.479 6.264   1.00  38.35 ? 102  LYS B CB  1 
ATOM   3093 C CG  . LYS B 1 102 ? -16.412 23.284 6.851   1.00  38.64 ? 102  LYS B CG  1 
ATOM   3094 C CD  . LYS B 1 102 ? -17.488 23.276 5.757   1.00  39.46 ? 102  LYS B CD  1 
ATOM   3095 C CE  . LYS B 1 102 ? -17.555 24.579 4.969   1.00  39.65 ? 102  LYS B CE  1 
ATOM   3096 N NZ  . LYS B 1 102 ? -18.451 24.438 3.775   1.00  39.60 ? 102  LYS B NZ  1 
ATOM   3097 N N   . SER B 1 103 ? -11.500 22.656 6.657   0.68  36.94 ? 103  SER B N   1 
ATOM   3098 C CA  . SER B 1 103 ? -10.212 22.893 6.017   0.68  36.28 ? 103  SER B CA  1 
ATOM   3099 C C   . SER B 1 103 ? -9.279  21.683 6.087   0.68  35.67 ? 103  SER B C   1 
ATOM   3100 O O   . SER B 1 103 ? -9.528  20.734 6.837   0.68  35.68 ? 103  SER B O   1 
ATOM   3101 C CB  . SER B 1 103 ? -9.537  24.118 6.635   0.68  36.42 ? 103  SER B CB  1 
ATOM   3102 O OG  . SER B 1 103 ? -8.290  24.378 6.011   0.68  36.63 ? 103  SER B OG  1 
ATOM   3103 N N   . ARG B 1 104 ? -8.206  21.738 5.295   1.00  34.84 ? 104  ARG B N   1 
ATOM   3104 C CA  . ARG B 1 104 ? -7.193  20.674 5.215   1.00  33.88 ? 104  ARG B CA  1 
ATOM   3105 C C   . ARG B 1 104 ? -6.117  20.924 6.265   1.00  33.05 ? 104  ARG B C   1 
ATOM   3106 O O   . ARG B 1 104 ? -4.936  21.106 5.946   1.00  32.85 ? 104  ARG B O   1 
ATOM   3107 C CB  . ARG B 1 104 ? -6.582  20.651 3.815   1.00  34.03 ? 104  ARG B CB  1 
ATOM   3108 C CG  . ARG B 1 104 ? -6.133  19.292 3.317   1.00  33.79 ? 104  ARG B CG  1 
ATOM   3109 C CD  . ARG B 1 104 ? -6.580  19.094 1.871   1.00  33.80 ? 104  ARG B CD  1 
ATOM   3110 N NE  . ARG B 1 104 ? -6.484  20.328 1.089   1.00  33.98 ? 104  ARG B NE  1 
ATOM   3111 C CZ  . ARG B 1 104 ? -7.138  20.566 -0.043  1.00  33.92 ? 104  ARG B CZ  1 
ATOM   3112 N NH1 . ARG B 1 104 ? -7.955  19.657 -0.559  1.00  34.41 ? 104  ARG B NH1 1 
ATOM   3113 N NH2 . ARG B 1 104 ? -6.973  21.724 -0.661  1.00  33.79 ? 104  ARG B NH2 1 
ATOM   3114 N N   . ALA B 1 105 ? -6.555  20.913 7.522   1.00  31.99 ? 105  ALA B N   1 
ATOM   3115 C CA  . ALA B 1 105 ? -5.778  21.403 8.650   1.00  30.92 ? 105  ALA B CA  1 
ATOM   3116 C C   . ALA B 1 105 ? -5.513  20.323 9.715   1.00  30.02 ? 105  ALA B C   1 
ATOM   3117 O O   . ALA B 1 105 ? -6.151  19.267 9.715   1.00  29.80 ? 105  ALA B O   1 
ATOM   3118 C CB  . ALA B 1 105 ? -6.501  22.593 9.265   1.00  31.05 ? 105  ALA B CB  1 
ATOM   3119 N N   . PRO B 1 106 ? -4.564  20.584 10.629  0.86  29.14 ? 106  PRO B N   1 
ATOM   3120 C CA  . PRO B 1 106 ? -4.313  19.601 11.674  0.86  28.42 ? 106  PRO B CA  1 
ATOM   3121 C C   . PRO B 1 106 ? -5.259  19.768 12.858  0.86  27.71 ? 106  PRO B C   1 
ATOM   3122 O O   . PRO B 1 106 ? -5.775  20.861 13.095  0.86  27.65 ? 106  PRO B O   1 
ATOM   3123 C CB  . PRO B 1 106 ? -2.880  19.920 12.097  0.86  28.51 ? 106  PRO B CB  1 
ATOM   3124 C CG  . PRO B 1 106 ? -2.752  21.396 11.865  0.86  28.77 ? 106  PRO B CG  1 
ATOM   3125 C CD  . PRO B 1 106 ? -3.652  21.745 10.720  0.86  29.02 ? 106  PRO B CD  1 
ATOM   3126 N N   . ILE B 1 107 ? -5.494  18.687 13.588  1.00  26.99 ? 107  ILE B N   1 
ATOM   3127 C CA  . ILE B 1 107 ? -6.186  18.776 14.869  1.00  26.40 ? 107  ILE B CA  1 
ATOM   3128 C C   . ILE B 1 107 ? -5.112  18.791 15.958  1.00  26.03 ? 107  ILE B C   1 
ATOM   3129 O O   . ILE B 1 107 ? -5.000  17.859 16.764  1.00  25.98 ? 107  ILE B O   1 
ATOM   3130 C CB  . ILE B 1 107 ? -7.184  17.612 15.079  1.00  26.42 ? 107  ILE B CB  1 
ATOM   3131 C CG1 . ILE B 1 107 ? -8.158  17.516 13.900  1.00  26.50 ? 107  ILE B CG1 1 
ATOM   3132 C CG2 . ILE B 1 107 ? -7.969  17.800 16.376  1.00  26.50 ? 107  ILE B CG2 1 
ATOM   3133 C CD1 . ILE B 1 107 ? -9.106  16.312 13.960  1.00  26.89 ? 107  ILE B CD1 1 
ATOM   3134 N N   . SER B 1 108 ? -4.315  19.860 15.954  1.00  25.54 ? 108  SER B N   1 
ATOM   3135 C CA  . SER B 1 108 ? -3.124  19.983 16.802  1.00  25.09 ? 108  SER B CA  1 
ATOM   3136 C C   . SER B 1 108 ? -3.384  19.745 18.282  1.00  24.95 ? 108  SER B C   1 
ATOM   3137 O O   . SER B 1 108 ? -2.464  19.357 19.014  1.00  24.97 ? 108  SER B O   1 
ATOM   3138 C CB  . SER B 1 108 ? -2.473  21.351 16.623  1.00  25.07 ? 108  SER B CB  1 
ATOM   3139 O OG  . SER B 1 108 ? -2.177  21.612 15.263  1.00  24.67 ? 108  SER B OG  1 
ATOM   3140 N N   . ALA B 1 109 ? -4.620  19.983 18.720  1.00  24.54 ? 109  ALA B N   1 
ATOM   3141 C CA  . ALA B 1 109 ? -5.033  19.601 20.073  1.00  24.38 ? 109  ALA B CA  1 
ATOM   3142 C C   . ALA B 1 109 ? -4.863  18.095 20.312  1.00  24.18 ? 109  ALA B C   1 
ATOM   3143 O O   . ALA B 1 109 ? -4.366  17.678 21.359  1.00  24.00 ? 109  ALA B O   1 
ATOM   3144 C CB  . ALA B 1 109 ? -6.468  20.020 20.330  1.00  24.55 ? 109  ALA B CB  1 
ATOM   3145 N N   . LYS B 1 110 ? -5.282  17.295 19.332  1.00  24.03 ? 110  LYS B N   1 
ATOM   3146 C CA  . LYS B 1 110 ? -5.106  15.848 19.363  1.00  23.85 ? 110  LYS B CA  1 
ATOM   3147 C C   . LYS B 1 110 ? -3.631  15.474 19.256  1.00  23.84 ? 110  LYS B C   1 
ATOM   3148 O O   . LYS B 1 110 ? -3.149  14.644 20.033  1.00  23.81 ? 110  LYS B O   1 
ATOM   3149 C CB  . LYS B 1 110 ? -5.934  15.178 18.253  1.00  23.80 ? 110  LYS B CB  1 
ATOM   3150 C CG  . LYS B 1 110 ? -5.705  13.677 18.056  1.00  23.57 ? 110  LYS B CG  1 
ATOM   3151 C CD  . LYS B 1 110 ? -6.000  12.870 19.308  1.00  23.02 ? 110  LYS B CD  1 
ATOM   3152 C CE  . LYS B 1 110 ? -5.674  11.406 19.102  1.00  22.65 ? 110  LYS B CE  1 
ATOM   3153 N NZ  . LYS B 1 110 ? -6.591  10.778 18.127  1.00  22.54 ? 110  LYS B NZ  1 
ATOM   3154 N N   . LEU B 1 111 ? -2.916  16.076 18.303  1.00  23.76 ? 111  LEU B N   1 
ATOM   3155 C CA  . LEU B 1 111 ? -1.492  15.798 18.171  1.00  23.91 ? 111  LEU B CA  1 
ATOM   3156 C C   . LEU B 1 111 ? -0.825  15.950 19.534  1.00  23.98 ? 111  LEU B C   1 
ATOM   3157 O O   . LEU B 1 111 ? -0.199  15.007 20.022  1.00  24.00 ? 111  LEU B O   1 
ATOM   3158 C CB  . LEU B 1 111 ? -0.825  16.696 17.118  1.00  23.99 ? 111  LEU B CB  1 
ATOM   3159 C CG  . LEU B 1 111 ? 0.720   16.768 17.083  1.00  24.36 ? 111  LEU B CG  1 
ATOM   3160 C CD1 . LEU B 1 111 ? 1.402   15.417 16.842  1.00  24.90 ? 111  LEU B CD1 1 
ATOM   3161 C CD2 . LEU B 1 111 ? 1.196   17.759 16.043  1.00  24.20 ? 111  LEU B CD2 1 
ATOM   3162 N N   . VAL B 1 112 ? -0.985  17.125 20.146  1.00  24.06 ? 112  VAL B N   1 
ATOM   3163 C CA  . VAL B 1 112 ? -0.447  17.393 21.488  1.00  24.34 ? 112  VAL B CA  1 
ATOM   3164 C C   . VAL B 1 112 ? -0.894  16.319 22.480  1.00  24.34 ? 112  VAL B C   1 
ATOM   3165 O O   . VAL B 1 112 ? -0.073  15.788 23.229  1.00  24.50 ? 112  VAL B O   1 
ATOM   3166 C CB  . VAL B 1 112 ? -0.845  18.803 22.013  1.00  24.43 ? 112  VAL B CB  1 
ATOM   3167 C CG1 . VAL B 1 112 ? -0.514  18.952 23.492  1.00  24.59 ? 112  VAL B CG1 1 
ATOM   3168 C CG2 . VAL B 1 112 ? -0.150  19.899 21.214  1.00  25.13 ? 112  VAL B CG2 1 
ATOM   3169 N N   . ALA B 1 113 ? -2.186  15.991 22.457  1.00  24.31 ? 113  ALA B N   1 
ATOM   3170 C CA  . ALA B 1 113 ? -2.739  14.928 23.288  1.00  24.26 ? 113  ALA B CA  1 
ATOM   3171 C C   . ALA B 1 113 ? -1.990  13.609 23.094  1.00  24.34 ? 113  ALA B C   1 
ATOM   3172 O O   . ALA B 1 113 ? -1.712  12.902 24.063  1.00  24.49 ? 113  ALA B O   1 
ATOM   3173 C CB  . ALA B 1 113 ? -4.227  14.755 23.012  1.00  24.20 ? 113  ALA B CB  1 
ATOM   3174 N N   . ASN B 1 114 ? -1.650  13.288 21.849  1.00  24.29 ? 114  ASN B N   1 
ATOM   3175 C CA  . ASN B 1 114 ? -0.828  12.116 21.580  1.00  24.30 ? 114  ASN B CA  1 
ATOM   3176 C C   . ASN B 1 114 ? 0.598   12.255 22.117  1.00  24.13 ? 114  ASN B C   1 
ATOM   3177 O O   . ASN B 1 114 ? 1.149   11.294 22.664  1.00  24.16 ? 114  ASN B O   1 
ATOM   3178 C CB  . ASN B 1 114 ? -0.810  11.789 20.082  1.00  24.50 ? 114  ASN B CB  1 
ATOM   3179 C CG  . ASN B 1 114 ? -2.069  11.089 19.621  1.00  24.93 ? 114  ASN B CG  1 
ATOM   3180 O OD1 . ASN B 1 114 ? -2.686  10.332 20.373  1.00  26.69 ? 114  ASN B OD1 1 
ATOM   3181 N ND2 . ASN B 1 114 ? -2.450  11.327 18.374  1.00  24.75 ? 114  ASN B ND2 1 
ATOM   3182 N N   . MET B 1 115 ? 1.187   13.443 21.984  0.90  23.76 ? 115  MET B N   1 
ATOM   3183 C CA  . MET B 1 115 ? 2.591   13.613 22.339  0.90  23.42 ? 115  MET B CA  1 
ATOM   3184 C C   . MET B 1 115 ? 2.795   13.565 23.838  0.90  23.26 ? 115  MET B C   1 
ATOM   3185 O O   . MET B 1 115 ? 3.786   13.016 24.314  0.90  23.26 ? 115  MET B O   1 
ATOM   3186 C CB  . MET B 1 115 ? 3.171   14.887 21.737  0.90  23.50 ? 115  MET B CB  1 
ATOM   3187 C CG  . MET B 1 115 ? 3.292   14.845 20.226  0.90  23.18 ? 115  MET B CG  1 
ATOM   3188 S SD  . MET B 1 115 ? 4.089   16.325 19.599  0.90  23.17 ? 115  MET B SD  1 
ATOM   3189 C CE  . MET B 1 115 ? 3.002   17.594 20.238  0.90  23.45 ? 115  MET B CE  1 
ATOM   3190 N N   . LEU B 1 116 ? 1.848   14.124 24.579  1.00  23.10 ? 116  LEU B N   1 
ATOM   3191 C CA  . LEU B 1 116 ? 1.830   13.969 26.029  1.00  22.95 ? 116  LEU B CA  1 
ATOM   3192 C C   . LEU B 1 116 ? 1.749   12.480 26.377  1.00  22.83 ? 116  LEU B C   1 
ATOM   3193 O O   . LEU B 1 116 ? 2.495   11.998 27.230  1.00  22.99 ? 116  LEU B O   1 
ATOM   3194 C CB  . LEU B 1 116 ? 0.661   14.745 26.654  1.00  23.03 ? 116  LEU B CB  1 
ATOM   3195 C CG  . LEU B 1 116 ? 0.556   16.260 26.390  1.00  23.07 ? 116  LEU B CG  1 
ATOM   3196 C CD1 . LEU B 1 116 ? -0.848  16.794 26.625  1.00  22.86 ? 116  LEU B CD1 1 
ATOM   3197 C CD2 . LEU B 1 116 ? 1.555   17.054 27.205  1.00  23.02 ? 116  LEU B CD2 1 
ATOM   3198 N N   . SER B 1 117 ? 0.876   11.756 25.677  1.00  22.50 ? 117  SER B N   1 
ATOM   3199 C CA  . SER B 1 117 ? 0.638   10.336 25.933  1.00  22.17 ? 117  SER B CA  1 
ATOM   3200 C C   . SER B 1 117 ? 1.828   9.412  25.635  1.00  22.04 ? 117  SER B C   1 
ATOM   3201 O O   . SER B 1 117 ? 2.134   8.531  26.442  1.00  21.82 ? 117  SER B O   1 
ATOM   3202 C CB  . SER B 1 117 ? -0.609  9.874  25.185  1.00  22.27 ? 117  SER B CB  1 
ATOM   3203 O OG  . SER B 1 117 ? -1.697  10.741 25.466  1.00  22.34 ? 117  SER B OG  1 
ATOM   3204 N N   . VAL B 1 118 ? 2.496   9.600  24.494  1.00  21.94 ? 118  VAL B N   1 
ATOM   3205 C CA  . VAL B 1 118 ? 3.715   8.820  24.219  1.00  21.90 ? 118  VAL B CA  1 
ATOM   3206 C C   . VAL B 1 118 ? 4.859   9.198  25.163  1.00  21.89 ? 118  VAL B C   1 
ATOM   3207 O O   . VAL B 1 118 ? 5.685   8.348  25.510  1.00  21.81 ? 118  VAL B O   1 
ATOM   3208 C CB  . VAL B 1 118 ? 4.219   8.877  22.741  1.00  21.70 ? 118  VAL B CB  1 
ATOM   3209 C CG1 . VAL B 1 118 ? 3.351   8.024  21.845  1.00  21.62 ? 118  VAL B CG1 1 
ATOM   3210 C CG2 . VAL B 1 118 ? 4.324   10.304 22.232  1.00  21.84 ? 118  VAL B CG2 1 
ATOM   3211 N N   . ALA B 1 119 ? 4.900   10.462 25.586  1.00  21.80 ? 119  ALA B N   1 
ATOM   3212 C CA  . ALA B 1 119 ? 5.994   10.929 26.431  1.00  21.77 ? 119  ALA B CA  1 
ATOM   3213 C C   . ALA B 1 119 ? 6.008   10.132 27.735  1.00  21.78 ? 119  ALA B C   1 
ATOM   3214 O O   . ALA B 1 119 ? 7.077   9.843  28.294  1.00  21.99 ? 119  ALA B O   1 
ATOM   3215 C CB  . ALA B 1 119 ? 5.882   12.430 26.696  1.00  21.47 ? 119  ALA B CB  1 
ATOM   3216 N N   . GLY B 1 120 ? 4.818   9.758  28.195  1.00  21.56 ? 120  GLY B N   1 
ATOM   3217 C CA  . GLY B 1 120 ? 4.689   8.958  29.406  1.00  21.49 ? 120  GLY B CA  1 
ATOM   3218 C C   . GLY B 1 120 ? 3.703   9.485  30.433  1.00  21.45 ? 120  GLY B C   1 
ATOM   3219 O O   . GLY B 1 120 ? 3.700   9.027  31.570  1.00  21.49 ? 120  GLY B O   1 
ATOM   3220 N N   . ALA B 1 121 ? 2.868   10.446 30.043  1.00  21.38 ? 121  ALA B N   1 
ATOM   3221 C CA  . ALA B 1 121 ? 1.821   10.956 30.926  1.00  21.34 ? 121  ALA B CA  1 
ATOM   3222 C C   . ALA B 1 121 ? 0.819   9.850  31.271  1.00  21.38 ? 121  ALA B C   1 
ATOM   3223 O O   . ALA B 1 121 ? 0.437   9.063  30.402  1.00  21.42 ? 121  ALA B O   1 
ATOM   3224 C CB  . ALA B 1 121 ? 1.119   12.139 30.288  1.00  21.29 ? 121  ALA B CB  1 
ATOM   3225 N N   . ASP B 1 122 ? 0.419   9.790  32.539  1.00  21.40 ? 122  ASP B N   1 
ATOM   3226 C CA  . ASP B 1 122 ? -0.525  8.785  33.012  1.00  21.75 ? 122  ASP B CA  1 
ATOM   3227 C C   . ASP B 1 122 ? -1.895  9.365  33.301  1.00  21.89 ? 122  ASP B C   1 
ATOM   3228 O O   . ASP B 1 122 ? -2.891  8.641  33.315  1.00  22.02 ? 122  ASP B O   1 
ATOM   3229 C CB  . ASP B 1 122 ? -0.004  8.142  34.284  1.00  21.90 ? 122  ASP B CB  1 
ATOM   3230 C CG  . ASP B 1 122 ? 1.139   7.206  34.028  1.00  23.25 ? 122  ASP B CG  1 
ATOM   3231 O OD1 . ASP B 1 122 ? 0.914   6.191  33.336  1.00  24.55 ? 122  ASP B OD1 1 
ATOM   3232 O OD2 . ASP B 1 122 ? 2.261   7.470  34.523  1.00  25.40 ? 122  ASP B OD2 1 
ATOM   3233 N N   . HIS B 1 123 ? -1.932  10.670 33.542  1.00  22.09 ? 123  HIS B N   1 
ATOM   3234 C CA  . HIS B 1 123 ? -3.125  11.359 34.005  1.00  22.31 ? 123  HIS B CA  1 
ATOM   3235 C C   . HIS B 1 123 ? -2.954  12.828 33.653  1.00  22.55 ? 123  HIS B C   1 
ATOM   3236 O O   . HIS B 1 123 ? -1.828  13.323 33.593  1.00  22.42 ? 123  HIS B O   1 
ATOM   3237 C CB  . HIS B 1 123 ? -3.263  11.173 35.519  1.00  22.28 ? 123  HIS B CB  1 
ATOM   3238 C CG  . HIS B 1 123 ? -4.427  11.896 36.122  1.00  22.57 ? 123  HIS B CG  1 
ATOM   3239 N ND1 . HIS B 1 123 ? -5.714  11.762 35.648  1.00  22.73 ? 123  HIS B ND1 1 
ATOM   3240 C CD2 . HIS B 1 123 ? -4.502  12.748 37.171  1.00  22.81 ? 123  HIS B CD2 1 
ATOM   3241 C CE1 . HIS B 1 123 ? -6.529  12.508 36.371  1.00  22.12 ? 123  HIS B CE1 1 
ATOM   3242 N NE2 . HIS B 1 123 ? -5.818  13.119 37.301  1.00  22.29 ? 123  HIS B NE2 1 
ATOM   3243 N N   . ILE B 1 124 ? -4.059  13.520 33.399  1.00  22.89 ? 124  ILE B N   1 
ATOM   3244 C CA  . ILE B 1 124 ? -4.001  14.926 33.031  1.00  23.39 ? 124  ILE B CA  1 
ATOM   3245 C C   . ILE B 1 124 ? -4.917  15.702 33.952  1.00  23.82 ? 124  ILE B C   1 
ATOM   3246 O O   . ILE B 1 124 ? -6.032  15.269 34.239  1.00  23.85 ? 124  ILE B O   1 
ATOM   3247 C CB  . ILE B 1 124 ? -4.422  15.168 31.536  1.00  23.45 ? 124  ILE B CB  1 
ATOM   3248 C CG1 . ILE B 1 124 ? -3.717  14.194 30.561  1.00  23.50 ? 124  ILE B CG1 1 
ATOM   3249 C CG2 . ILE B 1 124 ? -4.219  16.625 31.112  1.00  23.82 ? 124  ILE B CG2 1 
ATOM   3250 C CD1 . ILE B 1 124 ? -2.195  14.315 30.424  1.00  22.76 ? 124  ILE B CD1 1 
ATOM   3251 N N   . ILE B 1 125 ? -4.420  16.835 34.435  1.00  24.57 ? 125  ILE B N   1 
ATOM   3252 C CA  . ILE B 1 125 ? -5.218  17.777 35.205  1.00  25.29 ? 125  ILE B CA  1 
ATOM   3253 C C   . ILE B 1 125 ? -5.108  19.114 34.501  1.00  26.12 ? 125  ILE B C   1 
ATOM   3254 O O   . ILE B 1 125 ? -4.016  19.650 34.330  1.00  26.18 ? 125  ILE B O   1 
ATOM   3255 C CB  . ILE B 1 125 ? -4.745  17.883 36.674  1.00  25.10 ? 125  ILE B CB  1 
ATOM   3256 C CG1 . ILE B 1 125 ? -5.243  16.679 37.480  1.00  24.92 ? 125  ILE B CG1 1 
ATOM   3257 C CG2 . ILE B 1 125 ? -5.232  19.176 37.320  1.00  25.02 ? 125  ILE B CG2 1 
ATOM   3258 C CD1 . ILE B 1 125 ? -4.802  16.684 38.943  1.00  24.91 ? 125  ILE B CD1 1 
ATOM   3259 N N   . THR B 1 126 ? -6.253  19.630 34.071  1.00  27.32 ? 126  THR B N   1 
ATOM   3260 C CA  . THR B 1 126 ? -6.333  20.887 33.336  1.00  28.40 ? 126  THR B CA  1 
ATOM   3261 C C   . THR B 1 126 ? -7.525  21.701 33.834  1.00  29.20 ? 126  THR B C   1 
ATOM   3262 O O   . THR B 1 126 ? -8.342  21.210 34.617  1.00  29.30 ? 126  THR B O   1 
ATOM   3263 C CB  . THR B 1 126 ? -6.484  20.640 31.811  1.00  28.35 ? 126  THR B CB  1 
ATOM   3264 O OG1 . THR B 1 126 ? -6.443  21.886 31.106  1.00  28.67 ? 126  THR B OG1 1 
ATOM   3265 C CG2 . THR B 1 126 ? -7.795  19.929 31.496  1.00  27.96 ? 126  THR B CG2 1 
ATOM   3266 N N   . MET B 1 127 ? -7.633  22.938 33.365  1.00  30.20 ? 127  MET B N   1 
ATOM   3267 C CA  . MET B 1 127 ? -8.770  23.771 33.707  1.00  31.15 ? 127  MET B CA  1 
ATOM   3268 C C   . MET B 1 127 ? -9.425  24.353 32.461  1.00  31.66 ? 127  MET B C   1 
ATOM   3269 O O   . MET B 1 127 ? -8.761  24.914 31.585  1.00  31.61 ? 127  MET B O   1 
ATOM   3270 C CB  . MET B 1 127 ? -8.366  24.880 34.686  1.00  31.34 ? 127  MET B CB  1 
ATOM   3271 C CG  . MET B 1 127 ? -9.529  25.779 35.134  1.00  32.08 ? 127  MET B CG  1 
ATOM   3272 S SD  . MET B 1 127 ? -9.156  26.875 36.519  1.00  33.33 ? 127  MET B SD  1 
ATOM   3273 C CE  . MET B 1 127 ? -8.813  25.689 37.820  1.00  33.71 ? 127  MET B CE  1 
ATOM   3274 N N   . ASP B 1 128 ? -10.744 24.212 32.407  1.00  32.56 ? 128  ASP B N   1 
ATOM   3275 C CA  . ASP B 1 128 ? -11.535 24.762 31.315  1.00  33.67 ? 128  ASP B CA  1 
ATOM   3276 C C   . ASP B 1 128 ? -10.971 24.554 29.921  1.00  34.09 ? 128  ASP B C   1 
ATOM   3277 O O   . ASP B 1 128 ? -10.476 25.518 29.283  1.00  34.37 ? 128  ASP B O   1 
ATOM   3278 C CB  . ASP B 1 128 ? -11.787 26.249 31.533  1.00  33.86 ? 128  ASP B CB  1 
ATOM   3279 C CG  . ASP B 1 128 ? -12.982 26.495 32.399  1.00  34.78 ? 128  ASP B CG  1 
ATOM   3280 O OD1 . ASP B 1 128 ? -14.021 26.924 31.858  1.00  35.69 ? 128  ASP B OD1 1 
ATOM   3281 O OD2 . ASP B 1 128 ? -12.898 26.247 33.620  1.00  35.42 ? 128  ASP B OD2 1 
ATOM   3282 N N   . LEU B 1 129 ? -11.061 23.300 29.448  1.00  34.53 ? 129  LEU B N   1 
ATOM   3283 C CA  . LEU B 1 129 ? -10.704 23.002 28.060  1.00  35.10 ? 129  LEU B CA  1 
ATOM   3284 C C   . LEU B 1 129 ? -11.554 23.838 27.116  1.00  35.49 ? 129  LEU B C   1 
ATOM   3285 O O   . LEU B 1 129 ? -12.734 24.059 27.385  1.00  35.56 ? 129  LEU B O   1 
ATOM   3286 C CB  . LEU B 1 129 ? -10.909 21.519 27.759  1.00  34.99 ? 129  LEU B CB  1 
ATOM   3287 C CG  . LEU B 1 129 ? -9.905  20.529 28.345  1.00  35.47 ? 129  LEU B CG  1 
ATOM   3288 C CD1 . LEU B 1 129 ? -10.501 19.131 28.290  1.00  36.10 ? 129  LEU B CD1 1 
ATOM   3289 C CD2 . LEU B 1 129 ? -8.569  20.584 27.607  1.00  36.06 ? 129  LEU B CD2 1 
ATOM   3290 N N   . HIS B 1 130 ? -10.959 24.313 26.021  1.00  36.06 ? 130  HIS B N   1 
ATOM   3291 C CA  . HIS B 1 130 ? -11.684 25.138 25.058  1.00  36.57 ? 130  HIS B CA  1 
ATOM   3292 C C   . HIS B 1 130 ? -12.891 24.384 24.522  1.00  36.82 ? 130  HIS B C   1 
ATOM   3293 O O   . HIS B 1 130 ? -13.982 24.946 24.394  1.00  37.01 ? 130  HIS B O   1 
ATOM   3294 C CB  . HIS B 1 130 ? -10.790 25.571 23.899  1.00  36.75 ? 130  HIS B CB  1 
ATOM   3295 C CG  . HIS B 1 130 ? -11.523 26.327 22.836  1.00  37.79 ? 130  HIS B CG  1 
ATOM   3296 N ND1 . HIS B 1 130 ? -11.946 27.629 23.006  1.00  38.51 ? 130  HIS B ND1 1 
ATOM   3297 C CD2 . HIS B 1 130 ? -11.932 25.957 21.597  1.00  38.61 ? 130  HIS B CD2 1 
ATOM   3298 C CE1 . HIS B 1 130 ? -12.572 28.033 21.915  1.00  38.97 ? 130  HIS B CE1 1 
ATOM   3299 N NE2 . HIS B 1 130 ? -12.578 27.037 21.045  1.00  39.12 ? 130  HIS B NE2 1 
ATOM   3300 N N   . ALA B 1 131 ? -12.675 23.111 24.202  1.00  37.01 ? 131  ALA B N   1 
ATOM   3301 C CA  . ALA B 1 131 ? -13.747 22.199 23.851  1.00  37.14 ? 131  ALA B CA  1 
ATOM   3302 C C   . ALA B 1 131 ? -13.736 21.058 24.847  1.00  37.37 ? 131  ALA B C   1 
ATOM   3303 O O   . ALA B 1 131 ? -12.678 20.459 25.097  1.00  37.49 ? 131  ALA B O   1 
ATOM   3304 C CB  . ALA B 1 131 ? -13.543 21.665 22.459  1.00  37.09 ? 131  ALA B CB  1 
ATOM   3305 N N   . SER B 1 132 ? -14.910 20.756 25.404  1.00  37.38 ? 132  SER B N   1 
ATOM   3306 C CA  . SER B 1 132 ? -15.075 19.615 26.303  1.00  37.31 ? 132  SER B CA  1 
ATOM   3307 C C   . SER B 1 132 ? -14.516 18.328 25.709  1.00  36.93 ? 132  SER B C   1 
ATOM   3308 O O   . SER B 1 132 ? -13.834 17.563 26.395  1.00  37.10 ? 132  SER B O   1 
ATOM   3309 C CB  . SER B 1 132 ? -16.543 19.427 26.666  1.00  37.52 ? 132  SER B CB  1 
ATOM   3310 O OG  . SER B 1 132 ? -16.828 20.028 27.924  1.00  38.40 ? 132  SER B OG  1 
ATOM   3311 N N   . GLN B 1 133 ? -14.785 18.125 24.424  1.00  36.41 ? 133  GLN B N   1 
ATOM   3312 C CA  . GLN B 1 133 ? -14.370 16.927 23.695  1.00  35.97 ? 133  GLN B CA  1 
ATOM   3313 C C   . GLN B 1 133 ? -12.856 16.660 23.694  1.00  35.57 ? 133  GLN B C   1 
ATOM   3314 O O   . GLN B 1 133 ? -12.422 15.582 23.287  1.00  35.62 ? 133  GLN B O   1 
ATOM   3315 C CB  . GLN B 1 133 ? -14.875 16.986 22.248  1.00  36.08 ? 133  GLN B CB  1 
ATOM   3316 C CG  . GLN B 1 133 ? -16.399 17.068 22.074  1.00  36.06 ? 133  GLN B CG  1 
ATOM   3317 C CD  . GLN B 1 133 ? -16.968 18.477 22.259  1.00  35.97 ? 133  GLN B CD  1 
ATOM   3318 O OE1 . GLN B 1 133 ? -16.229 19.458 22.389  1.00  35.57 ? 133  GLN B OE1 1 
ATOM   3319 N NE2 . GLN B 1 133 ? -18.297 18.576 22.281  1.00  35.81 ? 133  GLN B NE2 1 
ATOM   3320 N N   . ILE B 1 134 ? -12.053 17.623 24.141  1.00  34.94 ? 134  ILE B N   1 
ATOM   3321 C CA  . ILE B 1 134 ? -10.599 17.412 24.191  1.00  34.31 ? 134  ILE B CA  1 
ATOM   3322 C C   . ILE B 1 134 ? -10.204 16.272 25.150  1.00  33.66 ? 134  ILE B C   1 
ATOM   3323 O O   . ILE B 1 134 ? -9.149  15.656 24.987  1.00  33.66 ? 134  ILE B O   1 
ATOM   3324 C CB  . ILE B 1 134 ? -9.805  18.729 24.456  1.00  34.46 ? 134  ILE B CB  1 
ATOM   3325 C CG1 . ILE B 1 134 ? -10.012 19.708 23.291  1.00  34.71 ? 134  ILE B CG1 1 
ATOM   3326 C CG2 . ILE B 1 134 ? -8.308  18.444 24.644  1.00  34.24 ? 134  ILE B CG2 1 
ATOM   3327 C CD1 . ILE B 1 134 ? -9.227  21.010 23.389  1.00  34.69 ? 134  ILE B CD1 1 
ATOM   3328 N N   . GLN B 1 135 ? -11.066 15.982 26.126  1.00  32.75 ? 135  GLN B N   1 
ATOM   3329 C CA  . GLN B 1 135 ? -10.937 14.781 26.953  1.00  31.81 ? 135  GLN B CA  1 
ATOM   3330 C C   . GLN B 1 135 ? -10.914 13.527 26.086  1.00  30.76 ? 135  GLN B C   1 
ATOM   3331 O O   . GLN B 1 135 ? -10.268 12.531 26.422  1.00  30.54 ? 135  GLN B O   1 
ATOM   3332 C CB  . GLN B 1 135 ? -12.107 14.677 27.927  1.00  32.06 ? 135  GLN B CB  1 
ATOM   3333 C CG  . GLN B 1 135 ? -12.040 15.598 29.134  1.00  33.61 ? 135  GLN B CG  1 
ATOM   3334 C CD  . GLN B 1 135 ? -12.714 14.995 30.366  1.00  35.41 ? 135  GLN B CD  1 
ATOM   3335 O OE1 . GLN B 1 135 ? -12.448 13.843 30.728  1.00  36.11 ? 135  GLN B OE1 1 
ATOM   3336 N NE2 . GLN B 1 135 ? -13.580 15.775 31.019  1.00  35.90 ? 135  GLN B NE2 1 
ATOM   3337 N N   . GLY B 1 136 ? -11.628 13.595 24.964  1.00  29.78 ? 136  GLY B N   1 
ATOM   3338 C CA  . GLY B 1 136 ? -11.778 12.466 24.060  1.00  28.32 ? 136  GLY B CA  1 
ATOM   3339 C C   . GLY B 1 136 ? -10.590 12.282 23.147  1.00  27.29 ? 136  GLY B C   1 
ATOM   3340 O O   . GLY B 1 136 ? -10.513 11.293 22.423  1.00  27.57 ? 136  GLY B O   1 
ATOM   3341 N N   . PHE B 1 137 ? -9.657  13.229 23.173  1.00  26.04 ? 137  PHE B N   1 
ATOM   3342 C CA  . PHE B 1 137 ? -8.418  13.071 22.422  1.00  24.63 ? 137  PHE B CA  1 
ATOM   3343 C C   . PHE B 1 137 ? -7.402  12.234 23.196  1.00  23.83 ? 137  PHE B C   1 
ATOM   3344 O O   . PHE B 1 137 ? -6.348  11.894 22.670  1.00  23.63 ? 137  PHE B O   1 
ATOM   3345 C CB  . PHE B 1 137 ? -7.829  14.427 22.036  1.00  24.65 ? 137  PHE B CB  1 
ATOM   3346 C CG  . PHE B 1 137 ? -8.731  15.262 21.170  1.00  24.48 ? 137  PHE B CG  1 
ATOM   3347 C CD1 . PHE B 1 137 ? -8.614  16.646 21.159  1.00  24.57 ? 137  PHE B CD1 1 
ATOM   3348 C CD2 . PHE B 1 137 ? -9.702  14.671 20.370  1.00  24.11 ? 137  PHE B CD2 1 
ATOM   3349 C CE1 . PHE B 1 137 ? -9.447  17.421 20.364  1.00  24.38 ? 137  PHE B CE1 1 
ATOM   3350 C CE2 . PHE B 1 137 ? -10.541 15.444 19.573  1.00  23.78 ? 137  PHE B CE2 1 
ATOM   3351 C CZ  . PHE B 1 137 ? -10.414 16.815 19.570  1.00  23.98 ? 137  PHE B CZ  1 
ATOM   3352 N N   . PHE B 1 138 ? -7.730  11.902 24.445  1.00  23.03 ? 138  PHE B N   1 
ATOM   3353 C CA  . PHE B 1 138 ? -6.875  11.063 25.297  1.00  22.29 ? 138  PHE B CA  1 
ATOM   3354 C C   . PHE B 1 138 ? -7.518  9.717  25.572  1.00  21.86 ? 138  PHE B C   1 
ATOM   3355 O O   . PHE B 1 138 ? -8.744  9.586  25.499  1.00  21.90 ? 138  PHE B O   1 
ATOM   3356 C CB  . PHE B 1 138 ? -6.631  11.724 26.653  1.00  22.14 ? 138  PHE B CB  1 
ATOM   3357 C CG  . PHE B 1 138 ? -5.807  12.971 26.593  1.00  21.08 ? 138  PHE B CG  1 
ATOM   3358 C CD1 . PHE B 1 138 ? -6.423  14.214 26.476  1.00  20.09 ? 138  PHE B CD1 1 
ATOM   3359 C CD2 . PHE B 1 138 ? -4.419  12.908 26.680  1.00  20.06 ? 138  PHE B CD2 1 
ATOM   3360 C CE1 . PHE B 1 138 ? -5.675  15.369 26.431  1.00  19.69 ? 138  PHE B CE1 1 
ATOM   3361 C CE2 . PHE B 1 138 ? -3.659  14.061 26.638  1.00  19.60 ? 138  PHE B CE2 1 
ATOM   3362 C CZ  . PHE B 1 138 ? -4.290  15.294 26.516  1.00  19.70 ? 138  PHE B CZ  1 
ATOM   3363 N N   . ASP B 1 139 ? -6.684  8.732  25.915  0.50  21.25 ? 139  ASP B N   1 
ATOM   3364 C CA  . ASP B 1 139 ? -7.164  7.423  26.344  0.50  20.84 ? 139  ASP B CA  1 
ATOM   3365 C C   . ASP B 1 139 ? -6.908  7.225  27.827  0.50  20.62 ? 139  ASP B C   1 
ATOM   3366 O O   . ASP B 1 139 ? -7.474  6.328  28.456  0.50  20.64 ? 139  ASP B O   1 
ATOM   3367 C CB  . ASP B 1 139 ? -6.490  6.309  25.552  0.50  20.76 ? 139  ASP B CB  1 
ATOM   3368 C CG  . ASP B 1 139 ? -7.128  6.091  24.201  0.50  20.73 ? 139  ASP B CG  1 
ATOM   3369 O OD1 . ASP B 1 139 ? -6.519  5.403  23.354  0.50  20.97 ? 139  ASP B OD1 1 
ATOM   3370 O OD2 . ASP B 1 139 ? -8.244  6.600  23.983  0.50  20.54 ? 139  ASP B OD2 1 
ATOM   3371 N N   . ILE B 1 140 ? -6.027  8.059  28.372  1.00  20.38 ? 140  ILE B N   1 
ATOM   3372 C CA  . ILE B 1 140 ? -5.770  8.104  29.805  1.00  19.92 ? 140  ILE B CA  1 
ATOM   3373 C C   . ILE B 1 140 ? -6.812  9.039  30.407  1.00  20.10 ? 140  ILE B C   1 
ATOM   3374 O O   . ILE B 1 140 ? -7.507  9.721  29.659  1.00  20.13 ? 140  ILE B O   1 
ATOM   3375 C CB  . ILE B 1 140 ? -4.317  8.582  30.128  1.00  19.78 ? 140  ILE B CB  1 
ATOM   3376 C CG1 . ILE B 1 140 ? -3.966  9.869  29.371  1.00  19.45 ? 140  ILE B CG1 1 
ATOM   3377 C CG2 . ILE B 1 140 ? -3.304  7.476  29.825  1.00  19.15 ? 140  ILE B CG2 1 
ATOM   3378 C CD1 . ILE B 1 140 ? -2.780  10.620 29.939  1.00  19.01 ? 140  ILE B CD1 1 
ATOM   3379 N N   . PRO B 1 141 ? -6.948  9.053  31.749  1.00  20.33 ? 141  PRO B N   1 
ATOM   3380 C CA  . PRO B 1 141 ? -7.950  9.899  32.406  1.00  20.55 ? 141  PRO B CA  1 
ATOM   3381 C C   . PRO B 1 141 ? -7.581  11.378 32.452  1.00  20.80 ? 141  PRO B C   1 
ATOM   3382 O O   . PRO B 1 141 ? -6.407  11.724 32.600  1.00  20.60 ? 141  PRO B O   1 
ATOM   3383 C CB  . PRO B 1 141 ? -8.027  9.321  33.820  1.00  20.42 ? 141  PRO B CB  1 
ATOM   3384 C CG  . PRO B 1 141 ? -6.724  8.681  34.035  1.00  20.40 ? 141  PRO B CG  1 
ATOM   3385 C CD  . PRO B 1 141 ? -6.296  8.145  32.711  1.00  20.40 ? 141  PRO B CD  1 
ATOM   3386 N N   . VAL B 1 142 ? -8.599  12.225 32.315  1.00  21.34 ? 142  VAL B N   1 
ATOM   3387 C CA  . VAL B 1 142 ? -8.439  13.673 32.313  1.00  21.93 ? 142  VAL B CA  1 
ATOM   3388 C C   . VAL B 1 142 ? -9.457  14.316 33.245  1.00  22.34 ? 142  VAL B C   1 
ATOM   3389 O O   . VAL B 1 142 ? -10.666 14.149 33.061  1.00  22.73 ? 142  VAL B O   1 
ATOM   3390 C CB  . VAL B 1 142 ? -8.618  14.251 30.887  1.00  21.93 ? 142  VAL B CB  1 
ATOM   3391 C CG1 . VAL B 1 142 ? -8.813  15.777 30.931  1.00  22.03 ? 142  VAL B CG1 1 
ATOM   3392 C CG2 . VAL B 1 142 ? -7.429  13.859 29.997  1.00  21.55 ? 142  VAL B CG2 1 
ATOM   3393 N N   . ASP B 1 143 ? -8.968  15.039 34.245  1.00  22.69 ? 143  ASP B N   1 
ATOM   3394 C CA  . ASP B 1 143 ? -9.846  15.828 35.084  1.00  23.22 ? 143  ASP B CA  1 
ATOM   3395 C C   . ASP B 1 143 ? -9.807  17.265 34.596  1.00  23.69 ? 143  ASP B C   1 
ATOM   3396 O O   . ASP B 1 143 ? -8.814  17.983 34.764  1.00  23.67 ? 143  ASP B O   1 
ATOM   3397 C CB  . ASP B 1 143 ? -9.460  15.726 36.556  1.00  23.16 ? 143  ASP B CB  1 
ATOM   3398 C CG  . ASP B 1 143 ? -9.463  14.304 37.059  1.00  23.44 ? 143  ASP B CG  1 
ATOM   3399 O OD1 . ASP B 1 143 ? -10.418 13.554 36.763  1.00  22.96 ? 143  ASP B OD1 1 
ATOM   3400 O OD2 . ASP B 1 143 ? -8.502  13.941 37.764  1.00  24.83 ? 143  ASP B OD2 1 
ATOM   3401 N N   . ASN B 1 144 ? -10.901 17.664 33.961  1.00  24.33 ? 144  ASN B N   1 
ATOM   3402 C CA  . ASN B 1 144 ? -11.065 19.026 33.490  1.00  24.85 ? 144  ASN B CA  1 
ATOM   3403 C C   . ASN B 1 144 ? -11.835 19.852 34.523  1.00  25.35 ? 144  ASN B C   1 
ATOM   3404 O O   . ASN B 1 144 ? -13.046 19.671 34.722  1.00  25.12 ? 144  ASN B O   1 
ATOM   3405 C CB  . ASN B 1 144 ? -11.743 19.037 32.110  1.00  24.59 ? 144  ASN B CB  1 
ATOM   3406 C CG  . ASN B 1 144 ? -12.011 20.432 31.608  1.00  24.39 ? 144  ASN B CG  1 
ATOM   3407 O OD1 . ASN B 1 144 ? -11.088 21.219 31.366  1.00  25.24 ? 144  ASN B OD1 1 
ATOM   3408 N ND2 . ASN B 1 144 ? -13.285 20.753 31.445  1.00  23.47 ? 144  ASN B ND2 1 
ATOM   3409 N N   . LEU B 1 145 ? -11.106 20.741 35.189  1.00  26.15 ? 145  LEU B N   1 
ATOM   3410 C CA  . LEU B 1 145 ? -11.669 21.575 36.249  1.00  27.03 ? 145  LEU B CA  1 
ATOM   3411 C C   . LEU B 1 145 ? -12.282 22.858 35.702  1.00  27.61 ? 145  LEU B C   1 
ATOM   3412 O O   . LEU B 1 145 ? -11.962 23.298 34.594  1.00  27.66 ? 145  LEU B O   1 
ATOM   3413 C CB  . LEU B 1 145 ? -10.604 21.912 37.296  1.00  27.01 ? 145  LEU B CB  1 
ATOM   3414 C CG  . LEU B 1 145 ? -9.752  20.768 37.852  1.00  26.84 ? 145  LEU B CG  1 
ATOM   3415 C CD1 . LEU B 1 145 ? -8.546  21.337 38.544  1.00  27.04 ? 145  LEU B CD1 1 
ATOM   3416 C CD2 . LEU B 1 145 ? -10.544 19.942 38.818  1.00  27.03 ? 145  LEU B CD2 1 
ATOM   3417 N N   . TYR B 1 146 ? -13.159 23.457 36.498  0.60  28.32 ? 146  TYR B N   1 
ATOM   3418 C CA  . TYR B 1 146 ? -13.871 24.649 36.075  0.60  29.09 ? 146  TYR B CA  1 
ATOM   3419 C C   . TYR B 1 146 ? -13.553 25.849 36.934  0.60  29.47 ? 146  TYR B C   1 
ATOM   3420 O O   . TYR B 1 146 ? -13.389 25.740 38.154  0.60  29.43 ? 146  TYR B O   1 
ATOM   3421 C CB  . TYR B 1 146 ? -15.374 24.403 36.074  0.60  29.17 ? 146  TYR B CB  1 
ATOM   3422 C CG  . TYR B 1 146 ? -15.782 23.281 35.160  0.60  29.98 ? 146  TYR B CG  1 
ATOM   3423 C CD1 . TYR B 1 146 ? -15.856 21.973 35.631  0.60  30.78 ? 146  TYR B CD1 1 
ATOM   3424 C CD2 . TYR B 1 146 ? -16.083 23.523 33.817  0.60  30.82 ? 146  TYR B CD2 1 
ATOM   3425 C CE1 . TYR B 1 146 ? -16.222 20.930 34.793  0.60  31.39 ? 146  TYR B CE1 1 
ATOM   3426 C CE2 . TYR B 1 146 ? -16.455 22.488 32.968  0.60  31.07 ? 146  TYR B CE2 1 
ATOM   3427 C CZ  . TYR B 1 146 ? -16.521 21.195 33.466  0.60  31.43 ? 146  TYR B CZ  1 
ATOM   3428 O OH  . TYR B 1 146 ? -16.890 20.160 32.648  0.60  31.46 ? 146  TYR B OH  1 
ATOM   3429 N N   . ALA B 1 147 ? -13.467 26.998 36.276  1.00  30.14 ? 147  ALA B N   1 
ATOM   3430 C CA  . ALA B 1 147 ? -13.337 28.271 36.965  1.00  30.72 ? 147  ALA B CA  1 
ATOM   3431 C C   . ALA B 1 147 ? -14.726 28.721 37.391  1.00  30.89 ? 147  ALA B C   1 
ATOM   3432 O O   . ALA B 1 147 ? -14.883 29.446 38.373  1.00  30.91 ? 147  ALA B O   1 
ATOM   3433 C CB  . ALA B 1 147 ? -12.690 29.309 36.048  1.00  30.93 ? 147  ALA B CB  1 
ATOM   3434 N N   . GLU B 1 148 ? -15.725 28.255 36.639  1.00  31.24 ? 148  GLU B N   1 
ATOM   3435 C CA  . GLU B 1 148 ? -17.153 28.597 36.818  1.00  31.56 ? 148  GLU B CA  1 
ATOM   3436 C C   . GLU B 1 148 ? -17.721 28.823 38.253  1.00  31.65 ? 148  GLU B C   1 
ATOM   3437 O O   . GLU B 1 148 ? -18.444 29.793 38.472  1.00  31.94 ? 148  GLU B O   1 
ATOM   3438 C CB  . GLU B 1 148 ? -18.050 27.595 36.077  1.00  31.47 ? 148  GLU B CB  1 
ATOM   3439 C CG  . GLU B 1 148 ? -19.492 27.635 36.600  1.00  32.14 ? 148  GLU B CG  1 
ATOM   3440 C CD  . GLU B 1 148 ? -20.482 26.943 35.698  1.00  33.69 ? 148  GLU B CD  1 
ATOM   3441 O OE1 . GLU B 1 148 ? -20.054 26.289 34.714  1.00  34.91 ? 148  GLU B OE1 1 
ATOM   3442 O OE2 . GLU B 1 148 ? -21.697 27.056 35.978  1.00  33.37 ? 148  GLU B OE2 1 
ATOM   3443 N N   . PRO B 1 149 ? -17.422 27.916 39.210  1.00  31.78 ? 149  PRO B N   1 
ATOM   3444 C CA  . PRO B 1 149 ? -17.809 28.209 40.627  1.00  31.85 ? 149  PRO B CA  1 
ATOM   3445 C C   . PRO B 1 149 ? -17.093 29.417 41.244  1.00  31.93 ? 149  PRO B C   1 
ATOM   3446 O O   . PRO B 1 149 ? -17.710 30.148 42.026  1.00  32.01 ? 149  PRO B O   1 
ATOM   3447 C CB  . PRO B 1 149 ? -17.402 26.926 41.371  1.00  31.99 ? 149  PRO B CB  1 
ATOM   3448 C CG  . PRO B 1 149 ? -17.322 25.884 40.349  1.00  31.64 ? 149  PRO B CG  1 
ATOM   3449 C CD  . PRO B 1 149 ? -16.831 26.549 39.122  1.00  31.79 ? 149  PRO B CD  1 
ATOM   3450 N N   . ALA B 1 150 ? -15.810 29.613 40.926  1.00  32.01 ? 150  ALA B N   1 
ATOM   3451 C CA  . ALA B 1 150 ? -15.063 30.760 41.469  1.00  32.05 ? 150  ALA B CA  1 
ATOM   3452 C C   . ALA B 1 150 ? -15.465 32.028 40.711  1.00  31.94 ? 150  ALA B C   1 
ATOM   3453 O O   . ALA B 1 150 ? -15.457 33.136 41.252  1.00  31.64 ? 150  ALA B O   1 
ATOM   3454 C CB  . ALA B 1 150 ? -13.557 30.508 41.375  1.00  32.01 ? 150  ALA B CB  1 
ATOM   3455 N N   . VAL B 1 151 ? -15.823 31.835 39.447  1.00  31.95 ? 151  VAL B N   1 
ATOM   3456 C CA  . VAL B 1 151 ? -16.346 32.908 38.637  1.00  31.98 ? 151  VAL B CA  1 
ATOM   3457 C C   . VAL B 1 151 ? -17.624 33.389 39.308  1.00  31.87 ? 151  VAL B C   1 
ATOM   3458 O O   . VAL B 1 151 ? -17.747 34.569 39.624  1.00  31.79 ? 151  VAL B O   1 
ATOM   3459 C CB  . VAL B 1 151 ? -16.578 32.447 37.183  1.00  32.05 ? 151  VAL B CB  1 
ATOM   3460 C CG1 . VAL B 1 151 ? -17.382 33.472 36.408  1.00  32.15 ? 151  VAL B CG1 1 
ATOM   3461 C CG2 . VAL B 1 151 ? -15.242 32.221 36.497  1.00  32.21 ? 151  VAL B CG2 1 
ATOM   3462 N N   . LEU B 1 152 ? -18.546 32.460 39.565  1.00  31.93 ? 152  LEU B N   1 
ATOM   3463 C CA  . LEU B 1 152 ? -19.791 32.762 40.291  1.00  31.87 ? 152  LEU B CA  1 
ATOM   3464 C C   . LEU B 1 152 ? -19.526 33.444 41.629  1.00  32.05 ? 152  LEU B C   1 
ATOM   3465 O O   . LEU B 1 152 ? -20.230 34.385 42.004  1.00  31.94 ? 152  LEU B O   1 
ATOM   3466 C CB  . LEU B 1 152 ? -20.634 31.503 40.511  1.00  31.53 ? 152  LEU B CB  1 
ATOM   3467 C CG  . LEU B 1 152 ? -21.035 30.700 39.271  1.00  31.26 ? 152  LEU B CG  1 
ATOM   3468 C CD1 . LEU B 1 152 ? -22.161 29.736 39.596  1.00  31.60 ? 152  LEU B CD1 1 
ATOM   3469 C CD2 . LEU B 1 152 ? -21.429 31.604 38.110  1.00  30.02 ? 152  LEU B CD2 1 
ATOM   3470 N N   . LYS B 1 153 ? -18.503 32.970 42.336  1.00  32.29 ? 153  LYS B N   1 
ATOM   3471 C CA  . LYS B 1 153 ? -18.073 33.608 43.568  1.00  32.44 ? 153  LYS B CA  1 
ATOM   3472 C C   . LYS B 1 153 ? -17.660 35.050 43.299  1.00  32.29 ? 153  LYS B C   1 
ATOM   3473 O O   . LYS B 1 153 ? -18.114 35.963 43.990  1.00  32.16 ? 153  LYS B O   1 
ATOM   3474 C CB  . LYS B 1 153 ? -16.928 32.828 44.225  1.00  32.55 ? 153  LYS B CB  1 
ATOM   3475 C CG  . LYS B 1 153 ? -16.590 33.328 45.630  1.00  33.10 ? 153  LYS B CG  1 
ATOM   3476 C CD  . LYS B 1 153 ? -15.628 32.404 46.362  1.00  34.02 ? 153  LYS B CD  1 
ATOM   3477 C CE  . LYS B 1 153 ? -15.677 32.644 47.872  1.00  34.11 ? 153  LYS B CE  1 
ATOM   3478 N NZ  . LYS B 1 153 ? -15.484 34.083 48.228  1.00  35.01 ? 153  LYS B NZ  1 
ATOM   3479 N N   . TRP B 1 154 ? -16.821 35.251 42.285  1.00  32.37 ? 154  TRP B N   1 
ATOM   3480 C CA  . TRP B 1 154 ? -16.339 36.592 41.966  1.00  32.52 ? 154  TRP B CA  1 
ATOM   3481 C C   . TRP B 1 154 ? -17.500 37.509 41.608  1.00  32.90 ? 154  TRP B C   1 
ATOM   3482 O O   . TRP B 1 154 ? -17.583 38.636 42.109  1.00  32.89 ? 154  TRP B O   1 
ATOM   3483 C CB  . TRP B 1 154 ? -15.294 36.588 40.840  1.00  32.37 ? 154  TRP B CB  1 
ATOM   3484 C CG  . TRP B 1 154 ? -14.601 37.906 40.729  1.00  31.61 ? 154  TRP B CG  1 
ATOM   3485 C CD1 . TRP B 1 154 ? -13.414 38.260 41.302  1.00  31.29 ? 154  TRP B CD1 1 
ATOM   3486 C CD2 . TRP B 1 154 ? -15.075 39.064 40.040  1.00  31.32 ? 154  TRP B CD2 1 
ATOM   3487 N NE1 . TRP B 1 154 ? -13.109 39.566 40.998  1.00  30.74 ? 154  TRP B NE1 1 
ATOM   3488 C CE2 . TRP B 1 154 ? -14.114 40.085 40.226  1.00  30.92 ? 154  TRP B CE2 1 
ATOM   3489 C CE3 . TRP B 1 154 ? -16.218 39.339 39.275  1.00  31.53 ? 154  TRP B CE3 1 
ATOM   3490 C CZ2 . TRP B 1 154 ? -14.259 41.359 39.680  1.00  31.25 ? 154  TRP B CZ2 1 
ATOM   3491 C CZ3 . TRP B 1 154 ? -16.365 40.607 38.729  1.00  31.83 ? 154  TRP B CZ3 1 
ATOM   3492 C CH2 . TRP B 1 154 ? -15.388 41.602 38.934  1.00  32.03 ? 154  TRP B CH2 1 
ATOM   3493 N N   . ILE B 1 155 ? -18.392 37.021 40.744  1.00  33.35 ? 155  ILE B N   1 
ATOM   3494 C CA  . ILE B 1 155 ? -19.536 37.803 40.270  1.00  33.73 ? 155  ILE B CA  1 
ATOM   3495 C C   . ILE B 1 155 ? -20.393 38.300 41.440  1.00  34.04 ? 155  ILE B C   1 
ATOM   3496 O O   . ILE B 1 155 ? -20.712 39.491 41.534  1.00  33.93 ? 155  ILE B O   1 
ATOM   3497 C CB  . ILE B 1 155 ? -20.406 37.005 39.265  1.00  33.67 ? 155  ILE B CB  1 
ATOM   3498 C CG1 . ILE B 1 155 ? -19.586 36.616 38.027  1.00  33.62 ? 155  ILE B CG1 1 
ATOM   3499 C CG2 . ILE B 1 155 ? -21.620 37.826 38.837  1.00  33.87 ? 155  ILE B CG2 1 
ATOM   3500 C CD1 . ILE B 1 155 ? -20.334 35.749 37.012  1.00  33.27 ? 155  ILE B CD1 1 
ATOM   3501 N N   . ARG B 1 156 ? -20.729 37.381 42.341  1.00  34.52 ? 156  ARG B N   1 
ATOM   3502 C CA  . ARG B 1 156 ? -21.587 37.678 43.486  1.00  34.87 ? 156  ARG B CA  1 
ATOM   3503 C C   . ARG B 1 156 ? -20.995 38.666 44.482  1.00  35.14 ? 156  ARG B C   1 
ATOM   3504 O O   . ARG B 1 156 ? -21.723 39.478 45.056  1.00  35.39 ? 156  ARG B O   1 
ATOM   3505 C CB  . ARG B 1 156 ? -21.964 36.398 44.225  1.00  34.85 ? 156  ARG B CB  1 
ATOM   3506 C CG  . ARG B 1 156 ? -23.059 35.605 43.563  1.00  34.78 ? 156  ARG B CG  1 
ATOM   3507 C CD  . ARG B 1 156 ? -23.606 34.588 44.538  1.00  34.63 ? 156  ARG B CD  1 
ATOM   3508 N NE  . ARG B 1 156 ? -24.557 33.694 43.889  1.00  35.57 ? 156  ARG B NE  1 
ATOM   3509 C CZ  . ARG B 1 156 ? -24.227 32.593 43.217  1.00  35.75 ? 156  ARG B CZ  1 
ATOM   3510 N NH1 . ARG B 1 156 ? -22.956 32.232 43.094  1.00  36.52 ? 156  ARG B NH1 1 
ATOM   3511 N NH2 . ARG B 1 156 ? -25.174 31.849 42.664  1.00  35.40 ? 156  ARG B NH2 1 
ATOM   3512 N N   . GLU B 1 157 ? -19.685 38.592 44.698  0.40  35.35 ? 157  GLU B N   1 
ATOM   3513 C CA  . GLU B 1 157 ? -19.034 39.445 45.688  0.40  35.60 ? 157  GLU B CA  1 
ATOM   3514 C C   . GLU B 1 157 ? -18.515 40.763 45.113  0.40  35.73 ? 157  GLU B C   1 
ATOM   3515 O O   . GLU B 1 157 ? -18.095 41.643 45.868  0.40  35.67 ? 157  GLU B O   1 
ATOM   3516 C CB  . GLU B 1 157 ? -17.897 38.689 46.376  0.40  35.61 ? 157  GLU B CB  1 
ATOM   3517 C CG  . GLU B 1 157 ? -16.649 38.544 45.531  0.40  35.99 ? 157  GLU B CG  1 
ATOM   3518 C CD  . GLU B 1 157 ? -15.673 37.535 46.101  0.40  36.54 ? 157  GLU B CD  1 
ATOM   3519 O OE1 . GLU B 1 157 ? -14.455 37.693 45.867  0.40  36.81 ? 157  GLU B OE1 1 
ATOM   3520 O OE2 . GLU B 1 157 ? -16.122 36.586 46.782  0.40  36.50 ? 157  GLU B OE2 1 
ATOM   3521 N N   . ASN B 1 158 ? -18.554 40.911 43.791  1.00  35.94 ? 158  ASN B N   1 
ATOM   3522 C CA  . ASN B 1 158 ? -17.968 42.091 43.166  1.00  36.15 ? 158  ASN B CA  1 
ATOM   3523 C C   . ASN B 1 158 ? -18.898 42.932 42.293  1.00  36.18 ? 158  ASN B C   1 
ATOM   3524 O O   . ASN B 1 158 ? -18.670 44.134 42.121  1.00  36.08 ? 158  ASN B O   1 
ATOM   3525 C CB  . ASN B 1 158 ? -16.674 41.718 42.436  1.00  36.35 ? 158  ASN B CB  1 
ATOM   3526 C CG  . ASN B 1 158 ? -15.533 41.425 43.402  1.00  36.72 ? 158  ASN B CG  1 
ATOM   3527 O OD1 . ASN B 1 158 ? -15.196 42.257 44.248  1.00  37.32 ? 158  ASN B OD1 1 
ATOM   3528 N ND2 . ASN B 1 158 ? -14.947 40.237 43.294  1.00  36.59 ? 158  ASN B ND2 1 
ATOM   3529 N N   . ILE B 1 159 ? -19.947 42.313 41.760  1.00  36.21 ? 159  ILE B N   1 
ATOM   3530 C CA  . ILE B 1 159 ? -20.905 43.056 40.949  1.00  36.30 ? 159  ILE B CA  1 
ATOM   3531 C C   . ILE B 1 159 ? -22.219 43.207 41.700  1.00  36.35 ? 159  ILE B C   1 
ATOM   3532 O O   . ILE B 1 159 ? -23.009 42.264 41.802  1.00  36.41 ? 159  ILE B O   1 
ATOM   3533 C CB  . ILE B 1 159 ? -21.096 42.438 39.540  1.00  36.25 ? 159  ILE B CB  1 
ATOM   3534 C CG1 . ILE B 1 159 ? -19.767 42.476 38.783  1.00  36.47 ? 159  ILE B CG1 1 
ATOM   3535 C CG2 . ILE B 1 159 ? -22.182 43.184 38.758  1.00  36.12 ? 159  ILE B CG2 1 
ATOM   3536 C CD1 . ILE B 1 159 ? -19.794 41.786 37.444  1.00  37.49 ? 159  ILE B CD1 1 
ATOM   3537 N N   . SER B 1 160 ? -22.433 44.408 42.230  1.00  36.31 ? 160  SER B N   1 
ATOM   3538 C CA  . SER B 1 160 ? -23.606 44.708 43.039  1.00  36.18 ? 160  SER B CA  1 
ATOM   3539 C C   . SER B 1 160 ? -24.879 44.246 42.336  1.00  35.85 ? 160  SER B C   1 
ATOM   3540 O O   . SER B 1 160 ? -25.693 43.538 42.928  1.00  35.90 ? 160  SER B O   1 
ATOM   3541 C CB  . SER B 1 160 ? -23.662 46.206 43.358  1.00  36.43 ? 160  SER B CB  1 
ATOM   3542 O OG  . SER B 1 160 ? -22.373 46.716 43.688  1.00  37.21 ? 160  SER B OG  1 
ATOM   3543 N N   . GLU B 1 161 ? -25.009 44.599 41.059  1.00  35.56 ? 161  GLU B N   1 
ATOM   3544 C CA  . GLU B 1 161 ? -26.207 44.285 40.269  1.00  35.45 ? 161  GLU B CA  1 
ATOM   3545 C C   . GLU B 1 161 ? -26.253 42.864 39.658  1.00  35.12 ? 161  GLU B C   1 
ATOM   3546 O O   . GLU B 1 161 ? -27.031 42.634 38.725  1.00  34.88 ? 161  GLU B O   1 
ATOM   3547 C CB  . GLU B 1 161 ? -26.404 45.327 39.152  1.00  35.56 ? 161  GLU B CB  1 
ATOM   3548 C CG  . GLU B 1 161 ? -26.131 46.785 39.541  1.00  36.07 ? 161  GLU B CG  1 
ATOM   3549 C CD  . GLU B 1 161 ? -24.697 47.234 39.241  1.00  37.07 ? 161  GLU B CD  1 
ATOM   3550 O OE1 . GLU B 1 161 ? -23.735 46.519 39.621  1.00  36.96 ? 161  GLU B OE1 1 
ATOM   3551 O OE2 . GLU B 1 161 ? -24.527 48.320 38.637  1.00  37.32 ? 161  GLU B OE2 1 
ATOM   3552 N N   . TRP B 1 162 ? -25.456 41.919 40.180  1.00  34.76 ? 162  TRP B N   1 
ATOM   3553 C CA  . TRP B 1 162 ? -25.382 40.568 39.588  1.00  34.48 ? 162  TRP B CA  1 
ATOM   3554 C C   . TRP B 1 162 ? -26.736 39.872 39.499  1.00  34.94 ? 162  TRP B C   1 
ATOM   3555 O O   . TRP B 1 162 ? -26.906 38.947 38.701  1.00  35.14 ? 162  TRP B O   1 
ATOM   3556 C CB  . TRP B 1 162 ? -24.353 39.657 40.286  1.00  34.16 ? 162  TRP B CB  1 
ATOM   3557 C CG  . TRP B 1 162 ? -24.730 39.165 41.670  1.00  32.72 ? 162  TRP B CG  1 
ATOM   3558 C CD1 . TRP B 1 162 ? -24.265 39.648 42.854  1.00  31.63 ? 162  TRP B CD1 1 
ATOM   3559 C CD2 . TRP B 1 162 ? -25.638 38.095 42.005  1.00  31.27 ? 162  TRP B CD2 1 
ATOM   3560 N NE1 . TRP B 1 162 ? -24.822 38.961 43.904  1.00  30.75 ? 162  TRP B NE1 1 
ATOM   3561 C CE2 . TRP B 1 162 ? -25.672 38.007 43.414  1.00  30.49 ? 162  TRP B CE2 1 
ATOM   3562 C CE3 . TRP B 1 162 ? -26.428 37.211 41.255  1.00  30.70 ? 162  TRP B CE3 1 
ATOM   3563 C CZ2 . TRP B 1 162 ? -26.461 37.071 44.090  1.00  29.56 ? 162  TRP B CZ2 1 
ATOM   3564 C CZ3 . TRP B 1 162 ? -27.214 36.279 41.930  1.00  29.97 ? 162  TRP B CZ3 1 
ATOM   3565 C CH2 . TRP B 1 162 ? -27.223 36.221 43.335  1.00  29.47 ? 162  TRP B CH2 1 
ATOM   3566 N N   . ARG B 1 163 ? -27.687 40.318 40.322  1.00  35.15 ? 163  ARG B N   1 
ATOM   3567 C CA  . ARG B 1 163 ? -29.050 39.790 40.320  1.00  35.23 ? 163  ARG B CA  1 
ATOM   3568 C C   . ARG B 1 163 ? -29.888 40.358 39.169  1.00  35.04 ? 163  ARG B C   1 
ATOM   3569 O O   . ARG B 1 163 ? -31.065 40.029 39.033  1.00  35.01 ? 163  ARG B O   1 
ATOM   3570 C CB  . ARG B 1 163 ? -29.723 40.084 41.664  1.00  35.35 ? 163  ARG B CB  1 
ATOM   3571 C CG  . ARG B 1 163 ? -29.037 39.426 42.858  1.00  36.48 ? 163  ARG B CG  1 
ATOM   3572 C CD  . ARG B 1 163 ? -29.838 39.612 44.156  1.00  38.98 ? 163  ARG B CD  1 
ATOM   3573 N NE  . ARG B 1 163 ? -29.213 38.938 45.302  1.00  41.05 ? 163  ARG B NE  1 
ATOM   3574 C CZ  . ARG B 1 163 ? -28.236 39.451 46.057  1.00  42.20 ? 163  ARG B CZ  1 
ATOM   3575 N NH1 . ARG B 1 163 ? -27.747 40.664 45.814  1.00  42.98 ? 163  ARG B NH1 1 
ATOM   3576 N NH2 . ARG B 1 163 ? -27.747 38.750 47.073  1.00  42.49 ? 163  ARG B NH2 1 
ATOM   3577 N N   . ASN B 1 164 ? -29.279 41.218 38.355  1.00  34.90 ? 164  ASN B N   1 
ATOM   3578 C CA  . ASN B 1 164 ? -29.964 41.876 37.242  1.00  34.68 ? 164  ASN B CA  1 
ATOM   3579 C C   . ASN B 1 164 ? -29.036 42.131 36.060  1.00  34.42 ? 164  ASN B C   1 
ATOM   3580 O O   . ASN B 1 164 ? -29.224 43.092 35.298  1.00  34.40 ? 164  ASN B O   1 
ATOM   3581 C CB  . ASN B 1 164 ? -30.585 43.197 37.699  1.00  34.92 ? 164  ASN B CB  1 
ATOM   3582 C CG  . ASN B 1 164 ? -31.917 43.010 38.392  1.00  35.30 ? 164  ASN B CG  1 
ATOM   3583 O OD1 . ASN B 1 164 ? -32.969 43.239 37.796  1.00  35.25 ? 164  ASN B OD1 1 
ATOM   3584 N ND2 . ASN B 1 164 ? -31.884 42.593 39.657  1.00  36.08 ? 164  ASN B ND2 1 
ATOM   3585 N N   . CYS B 1 165 ? -28.040 41.262 35.908  1.00  33.89 ? 165  CYS B N   1 
ATOM   3586 C CA  . CYS B 1 165 ? -27.071 41.390 34.832  1.00  33.38 ? 165  CYS B CA  1 
ATOM   3587 C C   . CYS B 1 165 ? -27.452 40.533 33.627  1.00  32.98 ? 165  CYS B C   1 
ATOM   3588 O O   . CYS B 1 165 ? -28.481 39.859 33.631  1.00  32.95 ? 165  CYS B O   1 
ATOM   3589 C CB  . CYS B 1 165 ? -25.684 41.005 35.335  1.00  33.30 ? 165  CYS B CB  1 
ATOM   3590 S SG  . CYS B 1 165 ? -25.609 39.343 35.958  1.00  33.76 ? 165  CYS B SG  1 
ATOM   3591 N N   . THR B 1 166 ? -26.620 40.588 32.592  1.00  32.61 ? 166  THR B N   1 
ATOM   3592 C CA  . THR B 1 166 ? -26.730 39.706 31.438  1.00  32.09 ? 166  THR B CA  1 
ATOM   3593 C C   . THR B 1 166 ? -25.373 39.065 31.169  1.00  31.84 ? 166  THR B C   1 
ATOM   3594 O O   . THR B 1 166 ? -24.332 39.740 31.155  1.00  31.81 ? 166  THR B O   1 
ATOM   3595 C CB  . THR B 1 166 ? -27.210 40.463 30.193  1.00  32.03 ? 166  THR B CB  1 
ATOM   3596 O OG1 . THR B 1 166 ? -28.513 40.994 30.442  1.00  32.41 ? 166  THR B OG1 1 
ATOM   3597 C CG2 . THR B 1 166 ? -27.279 39.543 28.984  1.00  32.05 ? 166  THR B CG2 1 
ATOM   3598 N N   . ILE B 1 167 ? -25.397 37.752 30.973  1.00  31.43 ? 167  ILE B N   1 
ATOM   3599 C CA  . ILE B 1 167 ? -24.192 36.986 30.715  1.00  30.99 ? 167  ILE B CA  1 
ATOM   3600 C C   . ILE B 1 167 ? -24.111 36.794 29.217  1.00  30.83 ? 167  ILE B C   1 
ATOM   3601 O O   . ILE B 1 167 ? -24.895 36.057 28.631  1.00  30.82 ? 167  ILE B O   1 
ATOM   3602 C CB  . ILE B 1 167 ? -24.207 35.613 31.450  1.00  30.93 ? 167  ILE B CB  1 
ATOM   3603 C CG1 . ILE B 1 167 ? -24.593 35.770 32.936  1.00  30.64 ? 167  ILE B CG1 1 
ATOM   3604 C CG2 . ILE B 1 167 ? -22.883 34.883 31.275  1.00  30.99 ? 167  ILE B CG2 1 
ATOM   3605 C CD1 . ILE B 1 167 ? -23.796 36.823 33.724  1.00  30.16 ? 167  ILE B CD1 1 
ATOM   3606 N N   . VAL B 1 168 ? -23.157 37.479 28.602  1.00  30.85 ? 168  VAL B N   1 
ATOM   3607 C CA  . VAL B 1 168 ? -23.034 37.506 27.147  1.00  30.80 ? 168  VAL B CA  1 
ATOM   3608 C C   . VAL B 1 168 ? -21.895 36.621 26.638  1.00  30.61 ? 168  VAL B C   1 
ATOM   3609 O O   . VAL B 1 168 ? -20.847 36.509 27.269  1.00  30.43 ? 168  VAL B O   1 
ATOM   3610 C CB  . VAL B 1 168 ? -22.835 38.957 26.631  1.00  30.86 ? 168  VAL B CB  1 
ATOM   3611 C CG1 . VAL B 1 168 ? -23.066 39.043 25.125  1.00  30.96 ? 168  VAL B CG1 1 
ATOM   3612 C CG2 . VAL B 1 168 ? -23.770 39.918 27.356  1.00  30.77 ? 168  VAL B CG2 1 
ATOM   3613 N N   . SER B 1 169 ? -22.121 35.989 25.493  1.00  30.70 ? 169  SER B N   1 
ATOM   3614 C CA  . SER B 1 169 ? -21.069 35.267 24.790  1.00  30.92 ? 169  SER B CA  1 
ATOM   3615 C C   . SER B 1 169 ? -20.494 36.128 23.663  1.00  30.95 ? 169  SER B C   1 
ATOM   3616 O O   . SER B 1 169 ? -21.246 36.716 22.880  1.00  30.94 ? 169  SER B O   1 
ATOM   3617 C CB  . SER B 1 169 ? -21.598 33.948 24.225  1.00  31.01 ? 169  SER B CB  1 
ATOM   3618 O OG  . SER B 1 169 ? -20.526 33.106 23.812  1.00  31.18 ? 169  SER B OG  1 
ATOM   3619 N N   . PRO B 1 170 ? -19.156 36.211 23.584  1.00  31.05 ? 170  PRO B N   1 
ATOM   3620 C CA  . PRO B 1 170 ? -18.538 36.988 22.509  1.00  31.21 ? 170  PRO B CA  1 
ATOM   3621 C C   . PRO B 1 170 ? -18.616 36.277 21.163  1.00  31.42 ? 170  PRO B C   1 
ATOM   3622 O O   . PRO B 1 170 ? -18.449 36.907 20.116  1.00  31.63 ? 170  PRO B O   1 
ATOM   3623 C CB  . PRO B 1 170 ? -17.080 37.140 22.962  1.00  31.27 ? 170  PRO B CB  1 
ATOM   3624 C CG  . PRO B 1 170 ? -16.860 36.063 23.969  1.00  31.19 ? 170  PRO B CG  1 
ATOM   3625 C CD  . PRO B 1 170 ? -18.178 35.756 24.594  1.00  30.97 ? 170  PRO B CD  1 
ATOM   3626 N N   . ASP B 1 171 ? -18.867 34.974 21.190  1.00  31.67 ? 171  ASP B N   1 
ATOM   3627 C CA  . ASP B 1 171 ? -19.003 34.202 19.960  1.00  32.01 ? 171  ASP B CA  1 
ATOM   3628 C C   . ASP B 1 171 ? -20.132 33.182 20.070  1.00  32.22 ? 171  ASP B C   1 
ATOM   3629 O O   . ASP B 1 171 ? -20.721 33.015 21.133  1.00  32.38 ? 171  ASP B O   1 
ATOM   3630 C CB  . ASP B 1 171 ? -17.666 33.555 19.561  1.00  31.99 ? 171  ASP B CB  1 
ATOM   3631 C CG  . ASP B 1 171 ? -17.165 32.531 20.573  1.00  32.16 ? 171  ASP B CG  1 
ATOM   3632 O OD1 . ASP B 1 171 ? -17.498 32.624 21.778  1.00  31.80 ? 171  ASP B OD1 1 
ATOM   3633 O OD2 . ASP B 1 171 ? -16.418 31.619 20.150  1.00  33.01 ? 171  ASP B OD2 1 
ATOM   3634 N N   . ALA B 1 172 ? -20.450 32.517 18.967  1.00  32.62 ? 172  ALA B N   1 
ATOM   3635 C CA  . ALA B 1 172 ? -21.518 31.517 18.956  1.00  32.88 ? 172  ALA B CA  1 
ATOM   3636 C C   . ALA B 1 172 ? -21.097 30.252 19.693  1.00  32.97 ? 172  ALA B C   1 
ATOM   3637 O O   . ALA B 1 172 ? -21.890 29.649 20.404  1.00  33.03 ? 172  ALA B O   1 
ATOM   3638 C CB  . ALA B 1 172 ? -21.929 31.189 17.520  1.00  32.99 ? 172  ALA B CB  1 
ATOM   3639 N N   . GLY B 1 173 ? -19.836 29.870 19.524  1.00  33.27 ? 173  GLY B N   1 
ATOM   3640 C CA  . GLY B 1 173 ? -19.283 28.671 20.143  1.00  33.69 ? 173  GLY B CA  1 
ATOM   3641 C C   . GLY B 1 173 ? -19.536 28.585 21.635  1.00  33.98 ? 173  GLY B C   1 
ATOM   3642 O O   . GLY B 1 173 ? -19.871 27.517 22.154  1.00  34.09 ? 173  GLY B O   1 
ATOM   3643 N N   . GLY B 1 174 ? -19.392 29.714 22.323  1.00  34.16 ? 174  GLY B N   1 
ATOM   3644 C CA  . GLY B 1 174 ? -19.552 29.757 23.772  1.00  34.19 ? 174  GLY B CA  1 
ATOM   3645 C C   . GLY B 1 174 ? -20.982 29.957 24.238  1.00  34.16 ? 174  GLY B C   1 
ATOM   3646 O O   . GLY B 1 174 ? -21.224 30.715 25.181  1.00  34.37 ? 174  GLY B O   1 
ATOM   3647 N N   . ALA B 1 175 ? -21.929 29.284 23.588  1.00  33.90 ? 175  ALA B N   1 
ATOM   3648 C CA  . ALA B 1 175 ? -23.331 29.384 23.979  1.00  33.66 ? 175  ALA B CA  1 
ATOM   3649 C C   . ALA B 1 175 ? -23.577 28.668 25.308  1.00  33.61 ? 175  ALA B C   1 
ATOM   3650 O O   . ALA B 1 175 ? -23.942 29.301 26.303  1.00  33.58 ? 175  ALA B O   1 
ATOM   3651 C CB  . ALA B 1 175 ? -24.234 28.836 22.890  1.00  33.64 ? 175  ALA B CB  1 
ATOM   3652 N N   . LYS B 1 176 ? -23.349 27.355 25.324  0.10  33.35 ? 176  LYS B N   1 
ATOM   3653 C CA  . LYS B 1 176 ? -23.567 26.529 26.513  0.10  33.13 ? 176  LYS B CA  1 
ATOM   3654 C C   . LYS B 1 176 ? -22.922 27.105 27.768  0.10  33.00 ? 176  LYS B C   1 
ATOM   3655 O O   . LYS B 1 176 ? -23.536 27.134 28.833  0.10  32.95 ? 176  LYS B O   1 
ATOM   3656 C CB  . LYS B 1 176 ? -23.067 25.104 26.276  0.10  33.10 ? 176  LYS B CB  1 
ATOM   3657 C CG  . LYS B 1 176 ? -24.098 24.184 25.646  0.10  33.12 ? 176  LYS B CG  1 
ATOM   3658 C CD  . LYS B 1 176 ? -23.510 22.814 25.354  0.10  33.07 ? 176  LYS B CD  1 
ATOM   3659 C CE  . LYS B 1 176 ? -24.588 21.742 25.343  0.10  33.03 ? 176  LYS B CE  1 
ATOM   3660 N NZ  . LYS B 1 176 ? -25.749 22.123 24.496  0.10  33.02 ? 176  LYS B NZ  1 
ATOM   3661 N N   . ARG B 1 177 ? -21.687 27.574 27.633  0.60  32.86 ? 177  ARG B N   1 
ATOM   3662 C CA  . ARG B 1 177 ? -20.975 28.145 28.766  0.60  32.81 ? 177  ARG B CA  1 
ATOM   3663 C C   . ARG B 1 177 ? -21.737 29.318 29.386  0.60  32.77 ? 177  ARG B C   1 
ATOM   3664 O O   . ARG B 1 177 ? -21.932 29.351 30.607  0.60  32.78 ? 177  ARG B O   1 
ATOM   3665 C CB  . ARG B 1 177 ? -19.554 28.567 28.377  0.60  32.80 ? 177  ARG B CB  1 
ATOM   3666 C CG  . ARG B 1 177 ? -18.597 28.640 29.564  0.60  32.82 ? 177  ARG B CG  1 
ATOM   3667 C CD  . ARG B 1 177 ? -17.242 29.224 29.185  0.60  33.28 ? 177  ARG B CD  1 
ATOM   3668 N NE  . ARG B 1 177 ? -16.502 28.374 28.252  0.60  33.64 ? 177  ARG B NE  1 
ATOM   3669 C CZ  . ARG B 1 177 ? -15.765 27.320 28.600  0.60  33.81 ? 177  ARG B CZ  1 
ATOM   3670 N NH1 . ARG B 1 177 ? -15.655 26.953 29.870  0.60  33.81 ? 177  ARG B NH1 1 
ATOM   3671 N NH2 . ARG B 1 177 ? -15.137 26.622 27.666  0.60  33.96 ? 177  ARG B NH2 1 
ATOM   3672 N N   . VAL B 1 178 ? -22.170 30.273 28.562  1.00  32.60 ? 178  VAL B N   1 
ATOM   3673 C CA  . VAL B 1 178 ? -22.850 31.460 29.106  1.00  32.69 ? 178  VAL B CA  1 
ATOM   3674 C C   . VAL B 1 178 ? -24.256 31.190 29.651  1.00  32.51 ? 178  VAL B C   1 
ATOM   3675 O O   . VAL B 1 178 ? -24.651 31.793 30.645  1.00  32.53 ? 178  VAL B O   1 
ATOM   3676 C CB  . VAL B 1 178 ? -22.852 32.703 28.152  1.00  32.73 ? 178  VAL B CB  1 
ATOM   3677 C CG1 . VAL B 1 178 ? -21.435 33.179 27.889  1.00  33.23 ? 178  VAL B CG1 1 
ATOM   3678 C CG2 . VAL B 1 178 ? -23.590 32.437 26.855  1.00  33.04 ? 178  VAL B CG2 1 
ATOM   3679 N N   . THR B 1 179 ? -24.993 30.285 29.004  1.00  32.34 ? 179  THR B N   1 
ATOM   3680 C CA  . THR B 1 179 ? -26.327 29.882 29.462  1.00  32.05 ? 179  THR B CA  1 
ATOM   3681 C C   . THR B 1 179 ? -26.244 29.268 30.852  1.00  31.97 ? 179  THR B C   1 
ATOM   3682 O O   . THR B 1 179 ? -26.916 29.716 31.774  1.00  31.67 ? 179  THR B O   1 
ATOM   3683 C CB  . THR B 1 179 ? -26.994 28.863 28.501  1.00  32.02 ? 179  THR B CB  1 
ATOM   3684 O OG1 . THR B 1 179 ? -26.157 27.706 28.367  1.00  32.13 ? 179  THR B OG1 1 
ATOM   3685 C CG2 . THR B 1 179 ? -27.217 29.479 27.127  1.00  31.62 ? 179  THR B CG2 1 
ATOM   3686 N N   . SER B 1 180 ? -25.401 28.247 30.982  1.00  32.24 ? 180  SER B N   1 
ATOM   3687 C CA  . SER B 1 180 ? -25.162 27.553 32.244  1.00  32.51 ? 180  SER B CA  1 
ATOM   3688 C C   . SER B 1 180 ? -24.900 28.494 33.428  1.00  32.55 ? 180  SER B C   1 
ATOM   3689 O O   . SER B 1 180 ? -25.436 28.283 34.522  1.00  32.54 ? 180  SER B O   1 
ATOM   3690 C CB  . SER B 1 180 ? -24.003 26.565 32.075  1.00  32.56 ? 180  SER B CB  1 
ATOM   3691 O OG  . SER B 1 180 ? -23.283 26.376 33.284  1.00  33.19 ? 180  SER B OG  1 
ATOM   3692 N N   . ILE B 1 181 ? -24.073 29.517 33.212  1.00  32.45 ? 181  ILE B N   1 
ATOM   3693 C CA  . ILE B 1 181 ? -23.772 30.484 34.267  1.00  32.43 ? 181  ILE B CA  1 
ATOM   3694 C C   . ILE B 1 181 ? -25.017 31.315 34.589  1.00  32.18 ? 181  ILE B C   1 
ATOM   3695 O O   . ILE B 1 181 ? -25.327 31.553 35.750  1.00  32.18 ? 181  ILE B O   1 
ATOM   3696 C CB  . ILE B 1 181 ? -22.562 31.402 33.901  1.00  32.62 ? 181  ILE B CB  1 
ATOM   3697 C CG1 . ILE B 1 181 ? -21.278 30.568 33.763  1.00  32.88 ? 181  ILE B CG1 1 
ATOM   3698 C CG2 . ILE B 1 181 ? -22.372 32.513 34.949  1.00  32.58 ? 181  ILE B CG2 1 
ATOM   3699 C CD1 . ILE B 1 181 ? -20.010 31.381 33.507  1.00  33.59 ? 181  ILE B CD1 1 
ATOM   3700 N N   . ALA B 1 182 ? -25.730 31.733 33.548  1.00  32.08 ? 182  ALA B N   1 
ATOM   3701 C CA  . ALA B 1 182 ? -26.920 32.569 33.691  1.00  31.89 ? 182  ALA B CA  1 
ATOM   3702 C C   . ALA B 1 182 ? -28.021 31.849 34.447  1.00  31.82 ? 182  ALA B C   1 
ATOM   3703 O O   . ALA B 1 182 ? -28.674 32.442 35.302  1.00  31.88 ? 182  ALA B O   1 
ATOM   3704 C CB  . ALA B 1 182 ? -27.427 33.017 32.323  1.00  31.84 ? 182  ALA B CB  1 
ATOM   3705 N N   . ASP B 1 183 ? -28.207 30.569 34.126  0.60  31.78 ? 183  ASP B N   1 
ATOM   3706 C CA  . ASP B 1 183 ? -29.233 29.742 34.749  0.60  31.75 ? 183  ASP B CA  1 
ATOM   3707 C C   . ASP B 1 183 ? -28.955 29.519 36.232  0.60  32.01 ? 183  ASP B C   1 
ATOM   3708 O O   . ASP B 1 183 ? -29.869 29.594 37.050  0.60  32.03 ? 183  ASP B O   1 
ATOM   3709 C CB  . ASP B 1 183 ? -29.373 28.411 34.004  0.60  31.60 ? 183  ASP B CB  1 
ATOM   3710 C CG  . ASP B 1 183 ? -29.945 28.580 32.600  0.60  31.51 ? 183  ASP B CG  1 
ATOM   3711 O OD1 . ASP B 1 183 ? -29.946 29.713 32.072  0.60  31.53 ? 183  ASP B OD1 1 
ATOM   3712 O OD2 . ASP B 1 183 ? -30.396 27.568 32.020  0.60  31.37 ? 183  ASP B OD2 1 
ATOM   3713 N N   . ARG B 1 184 ? -27.692 29.271 36.576  0.70  32.49 ? 184  ARG B N   1 
ATOM   3714 C CA  . ARG B 1 184 ? -27.282 29.160 37.975  0.70  33.00 ? 184  ARG B CA  1 
ATOM   3715 C C   . ARG B 1 184 ? -27.438 30.484 38.712  0.70  33.13 ? 184  ARG B C   1 
ATOM   3716 O O   . ARG B 1 184 ? -27.823 30.500 39.874  0.70  33.23 ? 184  ARG B O   1 
ATOM   3717 C CB  . ARG B 1 184 ? -25.842 28.662 38.091  0.70  33.11 ? 184  ARG B CB  1 
ATOM   3718 C CG  . ARG B 1 184 ? -25.677 27.152 37.984  0.70  34.23 ? 184  ARG B CG  1 
ATOM   3719 C CD  . ARG B 1 184 ? -24.259 26.757 38.395  0.70  36.45 ? 184  ARG B CD  1 
ATOM   3720 N NE  . ARG B 1 184 ? -23.867 25.404 37.987  0.70  38.35 ? 184  ARG B NE  1 
ATOM   3721 C CZ  . ARG B 1 184 ? -23.668 25.016 36.726  0.70  39.31 ? 184  ARG B CZ  1 
ATOM   3722 N NH1 . ARG B 1 184 ? -23.854 25.866 35.723  0.70  39.33 ? 184  ARG B NH1 1 
ATOM   3723 N NH2 . ARG B 1 184 ? -23.295 23.768 36.461  0.70  39.82 ? 184  ARG B NH2 1 
ATOM   3724 N N   . LEU B 1 185 ? -27.140 31.587 38.029  1.00  33.54 ? 185  LEU B N   1 
ATOM   3725 C CA  . LEU B 1 185 ? -27.313 32.929 38.588  1.00  33.97 ? 185  LEU B CA  1 
ATOM   3726 C C   . LEU B 1 185 ? -28.745 33.448 38.443  1.00  34.21 ? 185  LEU B C   1 
ATOM   3727 O O   . LEU B 1 185 ? -29.080 34.520 38.970  1.00  34.43 ? 185  LEU B O   1 
ATOM   3728 C CB  . LEU B 1 185 ? -26.332 33.923 37.948  1.00  34.01 ? 185  LEU B CB  1 
ATOM   3729 C CG  . LEU B 1 185 ? -24.840 33.866 38.313  1.00  34.13 ? 185  LEU B CG  1 
ATOM   3730 C CD1 . LEU B 1 185 ? -24.104 35.045 37.678  1.00  33.73 ? 185  LEU B CD1 1 
ATOM   3731 C CD2 . LEU B 1 185 ? -24.598 33.831 39.829  1.00  33.99 ? 185  LEU B CD2 1 
ATOM   3732 N N   . ASN B 1 186 ? -29.580 32.679 37.741  1.00  34.30 ? 186  ASN B N   1 
ATOM   3733 C CA  . ASN B 1 186 ? -30.972 33.048 37.452  1.00  34.29 ? 186  ASN B CA  1 
ATOM   3734 C C   . ASN B 1 186 ? -31.090 34.437 36.813  1.00  34.13 ? 186  ASN B C   1 
ATOM   3735 O O   . ASN B 1 186 ? -31.895 35.270 37.243  1.00  33.89 ? 186  ASN B O   1 
ATOM   3736 C CB  . ASN B 1 186 ? -31.846 32.930 38.710  1.00  34.42 ? 186  ASN B CB  1 
ATOM   3737 C CG  . ASN B 1 186 ? -33.302 32.615 38.390  1.00  35.11 ? 186  ASN B CG  1 
ATOM   3738 O OD1 . ASN B 1 186 ? -34.195 32.872 39.204  1.00  35.26 ? 186  ASN B OD1 1 
ATOM   3739 N ND2 . ASN B 1 186 ? -33.548 32.045 37.207  1.00  36.00 ? 186  ASN B ND2 1 
ATOM   3740 N N   . VAL B 1 187 ? -30.263 34.671 35.791  1.00  34.09 ? 187  VAL B N   1 
ATOM   3741 C CA  . VAL B 1 187 ? -30.224 35.942 35.049  1.00  34.08 ? 187  VAL B CA  1 
ATOM   3742 C C   . VAL B 1 187 ? -30.283 35.722 33.525  1.00  34.08 ? 187  VAL B C   1 
ATOM   3743 O O   . VAL B 1 187 ? -30.124 34.594 33.058  1.00  34.16 ? 187  VAL B O   1 
ATOM   3744 C CB  . VAL B 1 187 ? -28.982 36.805 35.430  1.00  34.03 ? 187  VAL B CB  1 
ATOM   3745 C CG1 . VAL B 1 187 ? -29.073 37.278 36.881  1.00  34.08 ? 187  VAL B CG1 1 
ATOM   3746 C CG2 . VAL B 1 187 ? -27.688 36.039 35.203  1.00  34.17 ? 187  VAL B CG2 1 
ATOM   3747 N N   . ASP B 1 188 ? -30.521 36.791 32.761  1.00  34.10 ? 188  ASP B N   1 
ATOM   3748 C CA  . ASP B 1 188 ? -30.605 36.703 31.295  1.00  34.09 ? 188  ASP B CA  1 
ATOM   3749 C C   . ASP B 1 188 ? -29.232 36.425 30.656  1.00  34.06 ? 188  ASP B C   1 
ATOM   3750 O O   . ASP B 1 188 ? -28.192 36.652 31.278  1.00  33.90 ? 188  ASP B O   1 
ATOM   3751 C CB  . ASP B 1 188 ? -31.193 37.994 30.693  1.00  34.19 ? 188  ASP B CB  1 
ATOM   3752 C CG  . ASP B 1 188 ? -32.594 38.318 31.205  1.00  34.36 ? 188  ASP B CG  1 
ATOM   3753 O OD1 . ASP B 1 188 ? -33.495 37.453 31.158  1.00  34.78 ? 188  ASP B OD1 1 
ATOM   3754 O OD2 . ASP B 1 188 ? -32.802 39.467 31.633  1.00  35.25 ? 188  ASP B OD2 1 
ATOM   3755 N N   . PHE B 1 189 ? -29.246 35.935 29.414  1.00  34.21 ? 189  PHE B N   1 
ATOM   3756 C CA  . PHE B 1 189 ? -28.031 35.732 28.608  1.00  34.28 ? 189  PHE B CA  1 
ATOM   3757 C C   . PHE B 1 189 ? -28.182 36.348 27.218  1.00  34.51 ? 189  PHE B C   1 
ATOM   3758 O O   . PHE B 1 189 ? -29.293 36.499 26.724  1.00  34.57 ? 189  PHE B O   1 
ATOM   3759 C CB  . PHE B 1 189 ? -27.687 34.238 28.485  1.00  34.10 ? 189  PHE B CB  1 
ATOM   3760 C CG  . PHE B 1 189 ? -28.504 33.499 27.452  1.00  33.63 ? 189  PHE B CG  1 
ATOM   3761 C CD1 . PHE B 1 189 ? -28.133 33.508 26.106  1.00  33.30 ? 189  PHE B CD1 1 
ATOM   3762 C CD2 . PHE B 1 189 ? -29.638 32.783 27.824  1.00  33.02 ? 189  PHE B CD2 1 
ATOM   3763 C CE1 . PHE B 1 189 ? -28.890 32.826 25.146  1.00  32.41 ? 189  PHE B CE1 1 
ATOM   3764 C CE2 . PHE B 1 189 ? -30.397 32.095 26.870  1.00  32.48 ? 189  PHE B CE2 1 
ATOM   3765 C CZ  . PHE B 1 189 ? -30.021 32.119 25.531  1.00  32.06 ? 189  PHE B CZ  1 
ATOM   3766 N N   . ALA B 1 190 ? -27.062 36.687 26.588  1.00  35.03 ? 190  ALA B N   1 
ATOM   3767 C CA  . ALA B 1 190 ? -27.069 37.264 25.241  1.00  35.62 ? 190  ALA B CA  1 
ATOM   3768 C C   . ALA B 1 190 ? -25.887 36.746 24.426  1.00  35.99 ? 190  ALA B C   1 
ATOM   3769 O O   . ALA B 1 190 ? -24.924 36.237 24.993  1.00  36.11 ? 190  ALA B O   1 
ATOM   3770 C CB  . ALA B 1 190 ? -27.056 38.787 25.310  1.00  35.73 ? 190  ALA B CB  1 
ATOM   3771 N N   . LEU B 1 191 ? -25.949 36.880 23.104  1.00  36.51 ? 191  LEU B N   1 
ATOM   3772 C CA  . LEU B 1 191 ? -25.011 36.163 22.239  1.00  37.04 ? 191  LEU B CA  1 
ATOM   3773 C C   . LEU B 1 191 ? -24.538 36.949 21.005  1.00  37.36 ? 191  LEU B C   1 
ATOM   3774 O O   . LEU B 1 191 ? -25.286 37.146 20.038  1.00  37.32 ? 191  LEU B O   1 
ATOM   3775 C CB  . LEU B 1 191 ? -25.639 34.828 21.826  1.00  37.14 ? 191  LEU B CB  1 
ATOM   3776 C CG  . LEU B 1 191 ? -24.786 33.672 21.305  1.00  37.58 ? 191  LEU B CG  1 
ATOM   3777 C CD1 . LEU B 1 191 ? -25.504 32.365 21.583  1.00  38.40 ? 191  LEU B CD1 1 
ATOM   3778 C CD2 . LEU B 1 191 ? -24.474 33.806 19.813  1.00  37.93 ? 191  LEU B CD2 1 
ATOM   3779 N N   . ILE B 1 192 ? -23.277 37.369 21.047  1.00  37.72 ? 192  ILE B N   1 
ATOM   3780 C CA  . ILE B 1 192 ? -22.652 38.092 19.947  1.00  38.07 ? 192  ILE B CA  1 
ATOM   3781 C C   . ILE B 1 192 ? -22.074 37.117 18.916  1.00  38.55 ? 192  ILE B C   1 
ATOM   3782 O O   . ILE B 1 192 ? -21.375 36.169 19.275  1.00  38.62 ? 192  ILE B O   1 
ATOM   3783 C CB  . ILE B 1 192 ? -21.570 39.067 20.474  1.00  37.93 ? 192  ILE B CB  1 
ATOM   3784 C CG1 . ILE B 1 192 ? -22.246 40.256 21.157  1.00  37.91 ? 192  ILE B CG1 1 
ATOM   3785 C CG2 . ILE B 1 192 ? -20.662 39.557 19.344  1.00  37.91 ? 192  ILE B CG2 1 
ATOM   3786 C CD1 . ILE B 1 192 ? -21.301 41.211 21.853  1.00  38.66 ? 192  ILE B CD1 1 
ATOM   3787 N N   . HIS B 1 193 ? -22.384 37.356 17.642  1.00  39.12 ? 193  HIS B N   1 
ATOM   3788 C CA  . HIS B 1 193 ? -21.856 36.576 16.526  1.00  39.69 ? 193  HIS B CA  1 
ATOM   3789 C C   . HIS B 1 193 ? -21.202 37.525 15.528  1.00  39.85 ? 193  HIS B C   1 
ATOM   3790 O O   . HIS B 1 193 ? -21.692 38.628 15.323  1.00  39.76 ? 193  HIS B O   1 
ATOM   3791 C CB  . HIS B 1 193 ? -22.999 35.786 15.879  1.00  40.00 ? 193  HIS B CB  1 
ATOM   3792 C CG  . HIS B 1 193 ? -22.669 35.190 14.542  1.00  41.22 ? 193  HIS B CG  1 
ATOM   3793 N ND1 . HIS B 1 193 ? -21.589 34.356 14.337  1.00  42.59 ? 193  HIS B ND1 1 
ATOM   3794 C CD2 . HIS B 1 193 ? -23.304 35.280 13.349  1.00  41.76 ? 193  HIS B CD2 1 
ATOM   3795 C CE1 . HIS B 1 193 ? -21.562 33.974 13.072  1.00  42.23 ? 193  HIS B CE1 1 
ATOM   3796 N NE2 . HIS B 1 193 ? -22.591 34.521 12.451  1.00  42.19 ? 193  HIS B NE2 1 
ATOM   3797 N N   . LYS B 1 194 ? -20.089 37.110 14.928  0.20  40.39 ? 194  LYS B N   1 
ATOM   3798 C CA  . LYS B 1 194 ? -19.405 37.939 13.931  0.20  40.91 ? 194  LYS B CA  1 
ATOM   3799 C C   . LYS B 1 194 ? -19.603 37.396 12.520  0.20  41.32 ? 194  LYS B C   1 
ATOM   3800 O O   . LYS B 1 194 ? -19.487 36.192 12.289  0.20  41.35 ? 194  LYS B O   1 
ATOM   3801 C CB  . LYS B 1 194 ? -17.914 38.080 14.252  0.20  40.87 ? 194  LYS B CB  1 
ATOM   3802 C CG  . LYS B 1 194 ? -17.207 39.145 13.422  0.20  40.89 ? 194  LYS B CG  1 
ATOM   3803 C CD  . LYS B 1 194 ? -15.865 39.537 14.020  0.20  40.97 ? 194  LYS B CD  1 
ATOM   3804 C CE  . LYS B 1 194 ? -15.246 40.705 13.259  0.20  41.10 ? 194  LYS B CE  1 
ATOM   3805 N NZ  . LYS B 1 194 ? -13.938 41.138 13.835  0.20  41.09 ? 194  LYS B NZ  1 
ATOM   3806 N N   . GLU B 1 195 ? -19.899 38.296 11.584  1.00  41.90 ? 195  GLU B N   1 
ATOM   3807 C CA  . GLU B 1 195 ? -20.198 37.939 10.189  1.00  42.37 ? 195  GLU B CA  1 
ATOM   3808 C C   . GLU B 1 195 ? -19.095 38.413 9.239   1.00  42.30 ? 195  GLU B C   1 
ATOM   3809 O O   . GLU B 1 195 ? -18.143 37.653 8.932   1.00  42.10 ? 195  GLU B O   1 
ATOM   3810 C CB  . GLU B 1 195 ? -21.549 38.529 9.759   1.00  42.47 ? 195  GLU B CB  1 
ATOM   3811 C CG  . GLU B 1 195 ? -22.712 38.217 10.706  1.00  43.59 ? 195  GLU B CG  1 
ATOM   3812 C CD  . GLU B 1 195 ? -24.013 38.903 10.315  1.00  45.12 ? 195  GLU B CD  1 
ATOM   3813 O OE1 . GLU B 1 195 ? -24.016 39.705 9.352   1.00  46.73 ? 195  GLU B OE1 1 
ATOM   3814 O OE2 . GLU B 1 195 ? -25.040 38.642 10.978  1.00  45.26 ? 195  GLU B OE2 1 
ATOM   3815 N N   . ASP B 1 203 ? -17.933 41.796 8.196   0.010 33.86 ? 203  ASP B N   1 
ATOM   3816 C CA  . ASP B 1 203 ? -17.056 42.383 9.201   0.010 33.87 ? 203  ASP B CA  1 
ATOM   3817 C C   . ASP B 1 203 ? -17.882 43.133 10.243  0.010 33.89 ? 203  ASP B C   1 
ATOM   3818 O O   . ASP B 1 203 ? -17.540 44.248 10.638  0.010 33.88 ? 203  ASP B O   1 
ATOM   3819 C CB  . ASP B 1 203 ? -16.044 43.323 8.540   0.010 33.86 ? 203  ASP B CB  1 
ATOM   3820 C CG  . ASP B 1 203 ? -14.742 43.417 9.312   0.010 33.84 ? 203  ASP B CG  1 
ATOM   3821 O OD1 . ASP B 1 203 ? -14.737 43.085 10.516  0.010 33.83 ? 203  ASP B OD1 1 
ATOM   3822 O OD2 . ASP B 1 203 ? -13.722 43.822 8.714   0.010 33.84 ? 203  ASP B OD2 1 
ATOM   3823 N N   . ARG B 1 204 ? -18.970 42.507 10.684  0.40  33.92 ? 204  ARG B N   1 
ATOM   3824 C CA  . ARG B 1 204 ? -19.890 43.129 11.631  0.40  34.06 ? 204  ARG B CA  1 
ATOM   3825 C C   . ARG B 1 204 ? -20.432 42.138 12.663  0.40  34.25 ? 204  ARG B C   1 
ATOM   3826 O O   . ARG B 1 204 ? -20.658 40.965 12.352  0.40  34.25 ? 204  ARG B O   1 
ATOM   3827 C CB  . ARG B 1 204 ? -21.052 43.791 10.884  0.40  33.96 ? 204  ARG B CB  1 
ATOM   3828 C CG  . ARG B 1 204 ? -20.672 45.072 10.163  0.40  33.93 ? 204  ARG B CG  1 
ATOM   3829 C CD  . ARG B 1 204 ? -20.384 46.185 11.152  0.40  34.01 ? 204  ARG B CD  1 
ATOM   3830 N NE  . ARG B 1 204 ? -21.567 46.480 11.951  0.40  34.23 ? 204  ARG B NE  1 
ATOM   3831 C CZ  . ARG B 1 204 ? -22.709 45.804 11.858  0.40  34.04 ? 204  ARG B CZ  1 
ATOM   3832 N NH1 . ARG B 1 204 ? -22.809 44.791 11.005  0.40  33.25 ? 204  ARG B NH1 1 
ATOM   3833 N NH2 . ARG B 1 204 ? -23.746 46.132 12.617  0.40  34.16 ? 204  ARG B NH2 1 
ATOM   3834 N N   . MET B 1 205 ? -20.643 42.626 13.884  1.00  34.48 ? 205  MET B N   1 
ATOM   3835 C CA  . MET B 1 205 ? -21.202 41.821 14.970  1.00  34.84 ? 205  MET B CA  1 
ATOM   3836 C C   . MET B 1 205 ? -22.716 41.994 15.096  1.00  34.99 ? 205  MET B C   1 
ATOM   3837 O O   . MET B 1 205 ? -23.249 43.087 14.886  1.00  34.92 ? 205  MET B O   1 
ATOM   3838 C CB  . MET B 1 205 ? -20.532 42.166 16.308  1.00  34.97 ? 205  MET B CB  1 
ATOM   3839 C CG  . MET B 1 205 ? -19.105 41.630 16.483  1.00  35.17 ? 205  MET B CG  1 
ATOM   3840 S SD  . MET B 1 205 ? -18.263 42.402 17.888  1.00  35.00 ? 205  MET B SD  1 
ATOM   3841 C CE  . MET B 1 205 ? -17.130 41.108 18.385  1.00  35.44 ? 205  MET B CE  1 
ATOM   3842 N N   . VAL B 1 206 ? -23.388 40.897 15.437  1.00  35.25 ? 206  VAL B N   1 
ATOM   3843 C CA  . VAL B 1 206 ? -24.825 40.879 15.694  1.00  35.53 ? 206  VAL B CA  1 
ATOM   3844 C C   . VAL B 1 206 ? -25.094 40.408 17.116  1.00  35.71 ? 206  VAL B C   1 
ATOM   3845 O O   . VAL B 1 206 ? -24.538 39.400 17.552  1.00  35.77 ? 206  VAL B O   1 
ATOM   3846 C CB  . VAL B 1 206 ? -25.579 39.947 14.718  1.00  35.43 ? 206  VAL B CB  1 
ATOM   3847 C CG1 . VAL B 1 206 ? -25.919 40.677 13.438  1.00  35.42 ? 206  VAL B CG1 1 
ATOM   3848 C CG2 . VAL B 1 206 ? -24.769 38.694 14.426  1.00  35.80 ? 206  VAL B CG2 1 
ATOM   3849 N N   . LEU B 1 207 ? -25.949 41.132 17.832  1.00  35.99 ? 207  LEU B N   1 
ATOM   3850 C CA  . LEU B 1 207 ? -26.299 40.756 19.196  1.00  36.32 ? 207  LEU B CA  1 
ATOM   3851 C C   . LEU B 1 207 ? -27.735 40.268 19.290  1.00  36.72 ? 207  LEU B C   1 
ATOM   3852 O O   . LEU B 1 207 ? -28.658 40.934 18.817  1.00  36.91 ? 207  LEU B O   1 
ATOM   3853 C CB  . LEU B 1 207 ? -26.074 41.926 20.157  1.00  36.25 ? 207  LEU B CB  1 
ATOM   3854 C CG  . LEU B 1 207 ? -26.613 41.783 21.583  1.00  35.89 ? 207  LEU B CG  1 
ATOM   3855 C CD1 . LEU B 1 207 ? -25.715 40.878 22.413  1.00  35.64 ? 207  LEU B CD1 1 
ATOM   3856 C CD2 . LEU B 1 207 ? -26.725 43.154 22.217  1.00  35.20 ? 207  LEU B CD2 1 
ATOM   3857 N N   . VAL B 1 208 ? -27.906 39.099 19.900  1.00  37.05 ? 208  VAL B N   1 
ATOM   3858 C CA  . VAL B 1 208 ? -29.224 38.571 20.203  1.00  37.46 ? 208  VAL B CA  1 
ATOM   3859 C C   . VAL B 1 208 ? -29.387 38.437 21.711  1.00  38.06 ? 208  VAL B C   1 
ATOM   3860 O O   . VAL B 1 208 ? -28.567 37.797 22.384  1.00  38.09 ? 208  VAL B O   1 
ATOM   3861 C CB  . VAL B 1 208 ? -29.497 37.214 19.513  1.00  37.35 ? 208  VAL B CB  1 
ATOM   3862 C CG1 . VAL B 1 208 ? -29.690 37.409 18.023  1.00  37.18 ? 208  VAL B CG1 1 
ATOM   3863 C CG2 . VAL B 1 208 ? -28.385 36.214 19.789  1.00  37.07 ? 208  VAL B CG2 1 
ATOM   3864 N N   . GLY B 1 209 ? -30.454 39.040 22.232  1.00  38.61 ? 209  GLY B N   1 
ATOM   3865 C CA  . GLY B 1 209 ? -30.727 39.031 23.664  1.00  39.14 ? 209  GLY B CA  1 
ATOM   3866 C C   . GLY B 1 209 ? -30.705 40.443 24.202  1.00  39.53 ? 209  GLY B C   1 
ATOM   3867 O O   . GLY B 1 209 ? -29.903 41.268 23.763  1.00  39.66 ? 209  GLY B O   1 
ATOM   3868 N N   . ASP B 1 210 ? -31.600 40.717 25.146  0.50  39.85 ? 210  ASP B N   1 
ATOM   3869 C CA  . ASP B 1 210 ? -31.749 42.043 25.727  0.50  40.16 ? 210  ASP B CA  1 
ATOM   3870 C C   . ASP B 1 210 ? -30.624 42.320 26.714  0.50  40.23 ? 210  ASP B C   1 
ATOM   3871 O O   . ASP B 1 210 ? -30.318 41.490 27.574  0.50  40.22 ? 210  ASP B O   1 
ATOM   3872 C CB  . ASP B 1 210 ? -33.105 42.151 26.427  0.50  40.24 ? 210  ASP B CB  1 
ATOM   3873 C CG  . ASP B 1 210 ? -33.524 43.590 26.685  0.50  40.96 ? 210  ASP B CG  1 
ATOM   3874 O OD1 . ASP B 1 210 ? -33.837 43.914 27.868  0.50  41.68 ? 210  ASP B OD1 1 
ATOM   3875 O OD2 . ASP B 1 210 ? -33.556 44.388 25.709  0.50  40.95 ? 210  ASP B OD2 1 
ATOM   3876 N N   . VAL B 1 211 ? -30.010 43.490 26.579  1.00  40.37 ? 211  VAL B N   1 
ATOM   3877 C CA  . VAL B 1 211 ? -28.976 43.938 27.511  1.00  40.68 ? 211  VAL B CA  1 
ATOM   3878 C C   . VAL B 1 211 ? -29.302 45.321 28.096  1.00  40.77 ? 211  VAL B C   1 
ATOM   3879 O O   . VAL B 1 211 ? -28.638 45.784 29.028  1.00  40.73 ? 211  VAL B O   1 
ATOM   3880 C CB  . VAL B 1 211 ? -27.571 43.954 26.844  1.00  40.78 ? 211  VAL B CB  1 
ATOM   3881 C CG1 . VAL B 1 211 ? -27.044 42.531 26.657  1.00  40.93 ? 211  VAL B CG1 1 
ATOM   3882 C CG2 . VAL B 1 211 ? -27.607 44.701 25.514  1.00  40.55 ? 211  VAL B CG2 1 
ATOM   3883 N N   . LYS B 1 212 ? -30.340 45.954 27.549  0.40  40.78 ? 212  LYS B N   1 
ATOM   3884 C CA  . LYS B 1 212 ? -30.688 47.337 27.862  0.40  40.82 ? 212  LYS B CA  1 
ATOM   3885 C C   . LYS B 1 212 ? -30.860 47.574 29.356  0.40  40.85 ? 212  LYS B C   1 
ATOM   3886 O O   . LYS B 1 212 ? -31.616 46.869 30.024  0.40  40.71 ? 212  LYS B O   1 
ATOM   3887 C CB  . LYS B 1 212 ? -31.954 47.755 27.108  0.40  40.87 ? 212  LYS B CB  1 
ATOM   3888 C CG  . LYS B 1 212 ? -32.103 49.263 26.904  0.40  41.00 ? 212  LYS B CG  1 
ATOM   3889 C CD  . LYS B 1 212 ? -33.473 49.608 26.321  0.40  41.11 ? 212  LYS B CD  1 
ATOM   3890 C CE  . LYS B 1 212 ? -33.694 51.114 26.218  0.40  41.18 ? 212  LYS B CE  1 
ATOM   3891 N NZ  . LYS B 1 212 ? -33.116 51.706 24.976  0.40  41.06 ? 212  LYS B NZ  1 
ATOM   3892 N N   . ASP B 1 213 ? -30.128 48.568 29.856  0.94  41.07 ? 213  ASP B N   1 
ATOM   3893 C CA  . ASP B 1 213 ? -30.170 49.014 31.256  0.94  41.33 ? 213  ASP B CA  1 
ATOM   3894 C C   . ASP B 1 213 ? -29.890 47.886 32.246  0.94  41.26 ? 213  ASP B C   1 
ATOM   3895 O O   . ASP B 1 213 ? -30.651 47.647 33.185  0.94  41.35 ? 213  ASP B O   1 
ATOM   3896 C CB  . ASP B 1 213 ? -31.485 49.746 31.570  0.94  41.44 ? 213  ASP B CB  1 
ATOM   3897 C CG  . ASP B 1 213 ? -31.673 51.003 30.728  0.94  42.02 ? 213  ASP B CG  1 
ATOM   3898 O OD1 . ASP B 1 213 ? -32.752 51.143 30.109  0.94  42.97 ? 213  ASP B OD1 1 
ATOM   3899 O OD2 . ASP B 1 213 ? -30.744 51.850 30.680  0.94  42.43 ? 213  ASP B OD2 1 
ATOM   3900 N N   . ARG B 1 214 ? -28.784 47.192 31.998  0.94  41.21 ? 214  ARG B N   1 
ATOM   3901 C CA  . ARG B 1 214 ? -28.324 46.074 32.808  0.94  41.08 ? 214  ARG B CA  1 
ATOM   3902 C C   . ARG B 1 214 ? -26.809 46.064 32.764  0.94  40.92 ? 214  ARG B C   1 
ATOM   3903 O O   . ARG B 1 214 ? -26.205 46.680 31.889  0.94  40.96 ? 214  ARG B O   1 
ATOM   3904 C CB  . ARG B 1 214 ? -28.824 44.758 32.221  0.94  41.25 ? 214  ARG B CB  1 
ATOM   3905 C CG  . ARG B 1 214 ? -30.320 44.562 32.279  0.94  41.39 ? 214  ARG B CG  1 
ATOM   3906 C CD  . ARG B 1 214 ? -30.719 43.286 31.576  0.94  41.81 ? 214  ARG B CD  1 
ATOM   3907 N NE  . ARG B 1 214 ? -31.811 42.643 32.289  0.94  41.94 ? 214  ARG B NE  1 
ATOM   3908 C CZ  . ARG B 1 214 ? -31.649 41.734 33.244  0.94  42.63 ? 214  ARG B CZ  1 
ATOM   3909 N NH1 . ARG B 1 214 ? -30.436 41.331 33.587  0.94  42.69 ? 214  ARG B NH1 1 
ATOM   3910 N NH2 . ARG B 1 214 ? -32.711 41.210 33.842  0.94  43.15 ? 214  ARG B NH2 1 
ATOM   3911 N N   . VAL B 1 215 ? -26.186 45.351 33.692  1.00  40.75 ? 215  VAL B N   1 
ATOM   3912 C CA  . VAL B 1 215 ? -24.741 45.169 33.630  1.00  40.50 ? 215  VAL B CA  1 
ATOM   3913 C C   . VAL B 1 215 ? -24.404 43.941 32.783  1.00  40.17 ? 215  VAL B C   1 
ATOM   3914 O O   . VAL B 1 215 ? -24.819 42.828 33.089  1.00  39.94 ? 215  VAL B O   1 
ATOM   3915 C CB  . VAL B 1 215 ? -24.109 45.116 35.044  1.00  40.57 ? 215  VAL B CB  1 
ATOM   3916 C CG1 . VAL B 1 215 ? -22.737 44.454 35.025  1.00  40.72 ? 215  VAL B CG1 1 
ATOM   3917 C CG2 . VAL B 1 215 ? -24.010 46.526 35.619  1.00  40.66 ? 215  VAL B CG2 1 
ATOM   3918 N N   . ALA B 1 216 ? -23.667 44.159 31.701  1.00  39.97 ? 216  ALA B N   1 
ATOM   3919 C CA  . ALA B 1 216 ? -23.275 43.068 30.824  1.00  39.82 ? 216  ALA B CA  1 
ATOM   3920 C C   . ALA B 1 216 ? -21.937 42.492 31.259  1.00  39.89 ? 216  ALA B C   1 
ATOM   3921 O O   . ALA B 1 216 ? -20.967 43.230 31.486  1.00  39.90 ? 216  ALA B O   1 
ATOM   3922 C CB  . ALA B 1 216 ? -23.219 43.530 29.379  1.00  39.72 ? 216  ALA B CB  1 
ATOM   3923 N N   . ILE B 1 217 ? -21.903 41.169 31.397  1.00  39.78 ? 217  ILE B N   1 
ATOM   3924 C CA  . ILE B 1 217 ? -20.670 40.464 31.711  1.00  39.53 ? 217  ILE B CA  1 
ATOM   3925 C C   . ILE B 1 217 ? -20.296 39.607 30.518  1.00  39.45 ? 217  ILE B C   1 
ATOM   3926 O O   . ILE B 1 217 ? -21.068 38.752 30.092  1.00  39.40 ? 217  ILE B O   1 
ATOM   3927 C CB  . ILE B 1 217 ? -20.811 39.581 32.954  1.00  39.51 ? 217  ILE B CB  1 
ATOM   3928 C CG1 . ILE B 1 217 ? -21.150 40.435 34.177  1.00  39.40 ? 217  ILE B CG1 1 
ATOM   3929 C CG2 . ILE B 1 217 ? -19.537 38.785 33.177  1.00  39.31 ? 217  ILE B CG2 1 
ATOM   3930 C CD1 . ILE B 1 217 ? -21.911 39.678 35.260  1.00  39.46 ? 217  ILE B CD1 1 
ATOM   3931 N N   . LEU B 1 218 ? -19.116 39.864 29.969  1.00  39.42 ? 218  LEU B N   1 
ATOM   3932 C CA  . LEU B 1 218 ? -18.593 39.056 28.886  1.00  39.38 ? 218  LEU B CA  1 
ATOM   3933 C C   . LEU B 1 218 ? -17.834 37.878 29.454  1.00  39.53 ? 218  LEU B C   1 
ATOM   3934 O O   . LEU B 1 218 ? -16.856 38.035 30.174  1.00  39.44 ? 218  LEU B O   1 
ATOM   3935 C CB  . LEU B 1 218 ? -17.696 39.875 27.954  1.00  39.29 ? 218  LEU B CB  1 
ATOM   3936 C CG  . LEU B 1 218 ? -18.357 40.502 26.722  1.00  38.64 ? 218  LEU B CG  1 
ATOM   3937 C CD1 . LEU B 1 218 ? -17.521 41.643 26.173  1.00  38.43 ? 218  LEU B CD1 1 
ATOM   3938 C CD2 . LEU B 1 218 ? -18.601 39.456 25.649  1.00  38.09 ? 218  LEU B CD2 1 
ATOM   3939 N N   . VAL B 1 219 ? -18.307 36.687 29.121  1.00  39.94 ? 219  VAL B N   1 
ATOM   3940 C CA  . VAL B 1 219 ? -17.672 35.454 29.553  1.00  40.41 ? 219  VAL B CA  1 
ATOM   3941 C C   . VAL B 1 219 ? -17.094 34.692 28.358  1.00  40.75 ? 219  VAL B C   1 
ATOM   3942 O O   . VAL B 1 219 ? -17.802 34.385 27.396  1.00  40.82 ? 219  VAL B O   1 
ATOM   3943 C CB  . VAL B 1 219 ? -18.670 34.552 30.306  1.00  40.32 ? 219  VAL B CB  1 
ATOM   3944 C CG1 . VAL B 1 219 ? -18.042 33.213 30.641  1.00  40.34 ? 219  VAL B CG1 1 
ATOM   3945 C CG2 . VAL B 1 219 ? -19.168 35.241 31.567  1.00  40.98 ? 219  VAL B CG2 1 
ATOM   3946 N N   . ASP B 1 220 ? -15.800 34.401 28.429  1.00  41.21 ? 220  ASP B N   1 
ATOM   3947 C CA  . ASP B 1 220 ? -15.134 33.550 27.458  1.00  41.69 ? 220  ASP B CA  1 
ATOM   3948 C C   . ASP B 1 220 ? -14.193 32.656 28.243  1.00  42.07 ? 220  ASP B C   1 
ATOM   3949 O O   . ASP B 1 220 ? -13.960 32.882 29.435  1.00  41.92 ? 220  ASP B O   1 
ATOM   3950 C CB  . ASP B 1 220 ? -14.340 34.396 26.455  1.00  41.76 ? 220  ASP B CB  1 
ATOM   3951 C CG  . ASP B 1 220 ? -14.378 33.832 25.026  1.00  42.06 ? 220  ASP B CG  1 
ATOM   3952 O OD1 . ASP B 1 220 ? -15.198 32.936 24.732  1.00  42.84 ? 220  ASP B OD1 1 
ATOM   3953 O OD2 . ASP B 1 220 ? -13.582 34.300 24.180  1.00  41.85 ? 220  ASP B OD2 1 
ATOM   3954 N N   . ASP B 1 221 ? -13.650 31.638 27.591  0.94  42.73 ? 221  ASP B N   1 
ATOM   3955 C CA  . ASP B 1 221 ? -12.665 30.800 28.254  0.94  43.42 ? 221  ASP B CA  1 
ATOM   3956 C C   . ASP B 1 221 ? -11.263 31.392 28.093  0.94  43.82 ? 221  ASP B C   1 
ATOM   3957 O O   . ASP B 1 221 ? -10.469 31.393 29.036  0.94  43.76 ? 221  ASP B O   1 
ATOM   3958 C CB  . ASP B 1 221 ? -12.720 29.374 27.723  0.94  43.42 ? 221  ASP B CB  1 
ATOM   3959 C CG  . ASP B 1 221 ? -12.192 29.265 26.320  0.94  43.85 ? 221  ASP B CG  1 
ATOM   3960 O OD1 . ASP B 1 221 ? -12.634 30.055 25.455  0.94  44.04 ? 221  ASP B OD1 1 
ATOM   3961 O OD2 . ASP B 1 221 ? -11.319 28.400 26.089  0.94  44.54 ? 221  ASP B OD2 1 
ATOM   3962 N N   . MET B 1 222 ? -10.969 31.899 26.898  1.00  44.44 ? 222  MET B N   1 
ATOM   3963 C CA  . MET B 1 222 ? -9.690  32.553 26.642  1.00  45.14 ? 222  MET B CA  1 
ATOM   3964 C C   . MET B 1 222 ? -9.824  33.837 25.830  1.00  45.29 ? 222  MET B C   1 
ATOM   3965 O O   . MET B 1 222 ? -10.724 33.977 24.994  1.00  45.46 ? 222  MET B O   1 
ATOM   3966 C CB  . MET B 1 222 ? -8.698  31.597 25.968  1.00  45.41 ? 222  MET B CB  1 
ATOM   3967 C CG  . MET B 1 222 ? -9.099  31.108 24.575  1.00  46.90 ? 222  MET B CG  1 
ATOM   3968 S SD  . MET B 1 222 ? -7.802  30.112 23.797  1.00  50.38 ? 222  MET B SD  1 
ATOM   3969 C CE  . MET B 1 222 ? -7.938  28.561 24.700  1.00  48.96 ? 222  MET B CE  1 
ATOM   3970 N N   . ALA B 1 223 ? -8.925  34.775 26.114  1.00  45.46 ? 223  ALA B N   1 
ATOM   3971 C CA  . ALA B 1 223 ? -8.746  35.976 25.311  1.00  45.51 ? 223  ALA B CA  1 
ATOM   3972 C C   . ALA B 1 223 ? -7.272  36.082 24.990  1.00  45.61 ? 223  ALA B C   1 
ATOM   3973 O O   . ALA B 1 223 ? -6.425  35.947 25.873  1.00  45.68 ? 223  ALA B O   1 
ATOM   3974 C CB  . ALA B 1 223 ? -9.214  37.206 26.062  1.00  45.51 ? 223  ALA B CB  1 
ATOM   3975 N N   . ASP B 1 224 ? -6.972  36.311 23.719  1.00  45.85 ? 224  ASP B N   1 
ATOM   3976 C CA  . ASP B 1 224 ? -5.598  36.355 23.249  1.00  46.17 ? 224  ASP B CA  1 
ATOM   3977 C C   . ASP B 1 224 ? -5.176  37.775 22.886  1.00  46.24 ? 224  ASP B C   1 
ATOM   3978 O O   . ASP B 1 224 ? -4.478  38.426 23.656  1.00  46.38 ? 224  ASP B O   1 
ATOM   3979 C CB  . ASP B 1 224 ? -5.416  35.409 22.062  1.00  46.29 ? 224  ASP B CB  1 
ATOM   3980 C CG  . ASP B 1 224 ? -3.960  35.207 21.697  1.00  46.83 ? 224  ASP B CG  1 
ATOM   3981 O OD1 . ASP B 1 224 ? -3.101  35.965 22.204  1.00  46.83 ? 224  ASP B OD1 1 
ATOM   3982 O OD2 . ASP B 1 224 ? -3.677  34.286 20.900  1.00  47.13 ? 224  ASP B OD2 1 
ATOM   3983 N N   . THR B 1 225 ? -5.591  38.245 21.712  1.00  46.34 ? 225  THR B N   1 
ATOM   3984 C CA  . THR B 1 225 ? -5.272  39.604 21.268  1.00  46.58 ? 225  THR B CA  1 
ATOM   3985 C C   . THR B 1 225 ? -6.291  40.628 21.769  1.00  46.54 ? 225  THR B C   1 
ATOM   3986 O O   . THR B 1 225 ? -6.044  41.842 21.721  1.00  46.55 ? 225  THR B O   1 
ATOM   3987 C CB  . THR B 1 225 ? -5.180  39.696 19.735  1.00  46.67 ? 225  THR B CB  1 
ATOM   3988 O OG1 . THR B 1 225 ? -6.453  39.371 19.158  1.00  47.00 ? 225  THR B OG1 1 
ATOM   3989 C CG2 . THR B 1 225 ? -4.123  38.724 19.213  1.00  47.06 ? 225  THR B CG2 1 
ATOM   3990 N N   . CYS B 1 226 ? -7.435  40.122 22.235  1.00  46.37 ? 226  CYS B N   1 
ATOM   3991 C CA  . CYS B 1 226 ? -8.511  40.933 22.834  1.00  46.14 ? 226  CYS B CA  1 
ATOM   3992 C C   . CYS B 1 226 ? -9.294  41.805 21.849  1.00  45.80 ? 226  CYS B C   1 
ATOM   3993 O O   . CYS B 1 226 ? -10.143 42.602 22.265  1.00  45.94 ? 226  CYS B O   1 
ATOM   3994 C CB  . CYS B 1 226 ? -7.987  41.764 24.010  1.00  46.15 ? 226  CYS B CB  1 
ATOM   3995 S SG  . CYS B 1 226 ? -7.398  40.725 25.354  1.00  46.68 ? 226  CYS B SG  1 
ATOM   3996 N N   . GLY B 1 227 ? -9.016  41.636 20.555  1.00  45.15 ? 227  GLY B N   1 
ATOM   3997 C CA  . GLY B 1 227 ? -9.757  42.318 19.499  1.00  44.32 ? 227  GLY B CA  1 
ATOM   3998 C C   . GLY B 1 227 ? -11.254 42.093 19.599  1.00  43.75 ? 227  GLY B C   1 
ATOM   3999 O O   . GLY B 1 227 ? -12.033 43.042 19.485  1.00  43.86 ? 227  GLY B O   1 
ATOM   4000 N N   . THR B 1 228 ? -11.649 40.841 19.837  1.00  43.09 ? 228  THR B N   1 
ATOM   4001 C CA  . THR B 1 228 ? -13.058 40.454 19.884  1.00  42.48 ? 228  THR B CA  1 
ATOM   4002 C C   . THR B 1 228 ? -13.792 41.128 21.038  1.00  42.15 ? 228  THR B C   1 
ATOM   4003 O O   . THR B 1 228 ? -14.709 41.931 20.816  1.00  42.17 ? 228  THR B O   1 
ATOM   4004 C CB  . THR B 1 228 ? -13.226 38.914 19.955  1.00  42.37 ? 228  THR B CB  1 
ATOM   4005 O OG1 . THR B 1 228 ? -12.667 38.323 18.779  1.00  42.38 ? 228  THR B OG1 1 
ATOM   4006 C CG2 . THR B 1 228 ? -14.689 38.516 20.040  1.00  42.30 ? 228  THR B CG2 1 
ATOM   4007 N N   . ILE B 1 229 ? -13.382 40.810 22.264  1.00  41.59 ? 229  ILE B N   1 
ATOM   4008 C CA  . ILE B 1 229 ? -14.075 41.301 23.462  1.00  41.07 ? 229  ILE B CA  1 
ATOM   4009 C C   . ILE B 1 229 ? -14.244 42.814 23.484  1.00  40.61 ? 229  ILE B C   1 
ATOM   4010 O O   . ILE B 1 229 ? -15.277 43.313 23.922  1.00  40.68 ? 229  ILE B O   1 
ATOM   4011 C CB  . ILE B 1 229 ? -13.396 40.850 24.777  1.00  41.17 ? 229  ILE B CB  1 
ATOM   4012 C CG1 . ILE B 1 229 ? -11.864 40.870 24.624  1.00  41.34 ? 229  ILE B CG1 1 
ATOM   4013 C CG2 . ILE B 1 229 ? -13.906 39.456 25.180  1.00  41.12 ? 229  ILE B CG2 1 
ATOM   4014 C CD1 . ILE B 1 229 ? -11.126 40.987 25.936  1.00  41.47 ? 229  ILE B CD1 1 
ATOM   4015 N N   . CYS B 1 230 ? -13.225 43.533 23.017  1.00  39.98 ? 230  CYS B N   1 
ATOM   4016 C CA  . CYS B 1 230 ? -13.286 44.982 22.882  1.00  39.27 ? 230  CYS B CA  1 
ATOM   4017 C C   . CYS B 1 230 ? -14.427 45.406 21.965  1.00  38.88 ? 230  CYS B C   1 
ATOM   4018 O O   . CYS B 1 230 ? -15.274 46.219 22.349  1.00  38.89 ? 230  CYS B O   1 
ATOM   4019 C CB  . CYS B 1 230 ? -11.958 45.508 22.357  1.00  39.25 ? 230  CYS B CB  1 
ATOM   4020 S SG  . CYS B 1 230 ? -10.644 45.366 23.586  1.00  39.23 ? 230  CYS B SG  1 
ATOM   4021 N N   . HIS B 1 231 ? -14.453 44.833 20.763  0.60  38.31 ? 231  HIS B N   1 
ATOM   4022 C CA  . HIS B 1 231 ? -15.516 45.082 19.795  0.60  37.71 ? 231  HIS B CA  1 
ATOM   4023 C C   . HIS B 1 231 ? -16.863 44.621 20.334  0.60  37.28 ? 231  HIS B C   1 
ATOM   4024 O O   . HIS B 1 231 ? -17.911 45.095 19.900  0.60  37.24 ? 231  HIS B O   1 
ATOM   4025 C CB  . HIS B 1 231 ? -15.200 44.377 18.476  0.60  37.70 ? 231  HIS B CB  1 
ATOM   4026 C CG  . HIS B 1 231 ? -14.160 45.075 17.657  0.60  37.60 ? 231  HIS B CG  1 
ATOM   4027 N ND1 . HIS B 1 231 ? -12.808 44.899 17.859  0.60  37.45 ? 231  HIS B ND1 1 
ATOM   4028 C CD2 . HIS B 1 231 ? -14.276 45.958 16.638  0.60  37.75 ? 231  HIS B CD2 1 
ATOM   4029 C CE1 . HIS B 1 231 ? -12.136 45.638 16.995  0.60  37.57 ? 231  HIS B CE1 1 
ATOM   4030 N NE2 . HIS B 1 231 ? -13.004 46.292 16.244  0.60  37.82 ? 231  HIS B NE2 1 
ATOM   4031 N N   . ALA B 1 232 ? -16.814 43.703 21.292  1.00  36.81 ? 232  ALA B N   1 
ATOM   4032 C CA  . ALA B 1 232 ? -18.010 43.148 21.915  1.00  36.45 ? 232  ALA B CA  1 
ATOM   4033 C C   . ALA B 1 232 ? -18.524 44.006 23.072  1.00  36.08 ? 232  ALA B C   1 
ATOM   4034 O O   . ALA B 1 232 ? -19.720 44.013 23.348  1.00  36.00 ? 232  ALA B O   1 
ATOM   4035 C CB  . ALA B 1 232 ? -17.748 41.718 22.378  1.00  36.54 ? 232  ALA B CB  1 
ATOM   4036 N N   . ALA B 1 233 ? -17.613 44.711 23.742  1.00  35.69 ? 233  ALA B N   1 
ATOM   4037 C CA  . ALA B 1 233 ? -17.971 45.655 24.798  1.00  35.39 ? 233  ALA B CA  1 
ATOM   4038 C C   . ALA B 1 233 ? -18.528 46.940 24.202  1.00  35.31 ? 233  ALA B C   1 
ATOM   4039 O O   . ALA B 1 233 ? -19.408 47.569 24.795  1.00  35.39 ? 233  ALA B O   1 
ATOM   4040 C CB  . ALA B 1 233 ? -16.776 45.952 25.670  1.00  35.32 ? 233  ALA B CB  1 
ATOM   4041 N N   . ASP B 1 234 ? -18.008 47.322 23.032  1.00  35.11 ? 234  ASP B N   1 
ATOM   4042 C CA  . ASP B 1 234 ? -18.555 48.438 22.255  1.00  34.75 ? 234  ASP B CA  1 
ATOM   4043 C C   . ASP B 1 234 ? -20.008 48.152 21.884  1.00  34.28 ? 234  ASP B C   1 
ATOM   4044 O O   . ASP B 1 234 ? -20.896 48.952 22.153  1.00  34.04 ? 234  ASP B O   1 
ATOM   4045 C CB  . ASP B 1 234 ? -17.727 48.681 20.985  1.00  34.91 ? 234  ASP B CB  1 
ATOM   4046 C CG  . ASP B 1 234 ? -16.430 49.447 21.248  1.00  35.28 ? 234  ASP B CG  1 
ATOM   4047 O OD1 . ASP B 1 234 ? -16.134 49.772 22.422  1.00  35.41 ? 234  ASP B OD1 1 
ATOM   4048 O OD2 . ASP B 1 234 ? -15.704 49.725 20.264  1.00  35.62 ? 234  ASP B OD2 1 
ATOM   4049 N N   . LYS B 1 235 ? -20.237 46.994 21.277  1.00  33.99 ? 235  LYS B N   1 
ATOM   4050 C CA  . LYS B 1 235 ? -21.570 46.570 20.890  1.00  33.96 ? 235  LYS B CA  1 
ATOM   4051 C C   . LYS B 1 235 ? -22.517 46.619 22.080  1.00  33.70 ? 235  LYS B C   1 
ATOM   4052 O O   . LYS B 1 235 ? -23.627 47.148 21.977  1.00  33.89 ? 235  LYS B O   1 
ATOM   4053 C CB  . LYS B 1 235 ? -21.536 45.144 20.321  1.00  34.12 ? 235  LYS B CB  1 
ATOM   4054 C CG  . LYS B 1 235 ? -22.827 44.703 19.622  1.00  34.83 ? 235  LYS B CG  1 
ATOM   4055 C CD  . LYS B 1 235 ? -22.694 44.849 18.110  1.00  36.39 ? 235  LYS B CD  1 
ATOM   4056 C CE  . LYS B 1 235 ? -24.087 45.073 17.443  1.00  36.96 ? 235  LYS B CE  1 
ATOM   4057 N NZ  . LYS B 1 235 ? -23.902 45.446 15.993  1.00  37.82 ? 235  LYS B NZ  1 
ATOM   4058 N N   . LEU B 1 236 ? -22.073 46.068 23.206  1.00  33.33 ? 236  LEU B N   1 
ATOM   4059 C CA  . LEU B 1 236 ? -22.926 45.964 24.381  1.00  32.84 ? 236  LEU B CA  1 
ATOM   4060 C C   . LEU B 1 236 ? -23.302 47.344 24.910  1.00  32.62 ? 236  LEU B C   1 
ATOM   4061 O O   . LEU B 1 236 ? -24.457 47.573 25.274  1.00  32.77 ? 236  LEU B O   1 
ATOM   4062 C CB  . LEU B 1 236 ? -22.284 45.089 25.462  1.00  32.90 ? 236  LEU B CB  1 
ATOM   4063 C CG  . LEU B 1 236 ? -22.206 43.584 25.164  1.00  32.41 ? 236  LEU B CG  1 
ATOM   4064 C CD1 . LEU B 1 236 ? -21.317 42.862 26.173  1.00  33.19 ? 236  LEU B CD1 1 
ATOM   4065 C CD2 . LEU B 1 236 ? -23.587 42.977 25.139  1.00  32.26 ? 236  LEU B CD2 1 
ATOM   4066 N N   . LEU B 1 237 ? -22.347 48.271 24.913  1.00  32.12 ? 237  LEU B N   1 
ATOM   4067 C CA  . LEU B 1 237 ? -22.629 49.650 25.308  1.00  31.83 ? 237  LEU B CA  1 
ATOM   4068 C C   . LEU B 1 237 ? -23.422 50.426 24.262  1.00  31.69 ? 237  LEU B C   1 
ATOM   4069 O O   . LEU B 1 237 ? -24.045 51.432 24.583  1.00  31.75 ? 237  LEU B O   1 
ATOM   4070 C CB  . LEU B 1 237 ? -21.343 50.397 25.663  1.00  31.85 ? 237  LEU B CB  1 
ATOM   4071 C CG  . LEU B 1 237 ? -20.847 50.231 27.104  1.00  31.93 ? 237  LEU B CG  1 
ATOM   4072 C CD1 . LEU B 1 237 ? -19.478 50.859 27.263  1.00  31.82 ? 237  LEU B CD1 1 
ATOM   4073 C CD2 . LEU B 1 237 ? -21.822 50.836 28.116  1.00  31.50 ? 237  LEU B CD2 1 
ATOM   4074 N N   . SER B 1 238 ? -23.386 49.961 23.015  1.00  31.58 ? 238  SER B N   1 
ATOM   4075 C CA  . SER B 1 238 ? -24.217 50.524 21.956  1.00  31.30 ? 238  SER B CA  1 
ATOM   4076 C C   . SER B 1 238 ? -25.659 50.065 22.096  1.00  31.07 ? 238  SER B C   1 
ATOM   4077 O O   . SER B 1 238 ? -26.578 50.793 21.724  1.00  31.19 ? 238  SER B O   1 
ATOM   4078 C CB  . SER B 1 238 ? -23.682 50.148 20.572  1.00  31.35 ? 238  SER B CB  1 
ATOM   4079 O OG  . SER B 1 238 ? -22.674 51.053 20.154  1.00  31.82 ? 238  SER B OG  1 
ATOM   4080 N N   . ALA B 1 239 ? -25.856 48.858 22.626  1.00  30.79 ? 239  ALA B N   1 
ATOM   4081 C CA  . ALA B 1 239 ? -27.204 48.334 22.850  1.00  30.57 ? 239  ALA B CA  1 
ATOM   4082 C C   . ALA B 1 239 ? -27.731 48.571 24.285  1.00  30.57 ? 239  ALA B C   1 
ATOM   4083 O O   . ALA B 1 239 ? -28.692 47.923 24.723  1.00  30.60 ? 239  ALA B O   1 
ATOM   4084 C CB  . ALA B 1 239 ? -27.283 46.869 22.454  1.00  30.41 ? 239  ALA B CB  1 
ATOM   4085 N N   . GLY B 1 240 ? -27.102 49.501 25.005  1.00  30.37 ? 240  GLY B N   1 
ATOM   4086 C CA  . GLY B 1 240 ? -27.693 50.070 26.220  1.00  30.30 ? 240  GLY B CA  1 
ATOM   4087 C C   . GLY B 1 240 ? -27.360 49.420 27.555  1.00  30.27 ? 240  GLY B C   1 
ATOM   4088 O O   . GLY B 1 240 ? -28.053 49.644 28.558  1.00  30.11 ? 240  GLY B O   1 
ATOM   4089 N N   . ALA B 1 241 ? -26.300 48.618 27.581  1.00  30.17 ? 241  ALA B N   1 
ATOM   4090 C CA  . ALA B 1 241 ? -25.802 48.053 28.833  1.00  29.92 ? 241  ALA B CA  1 
ATOM   4091 C C   . ALA B 1 241 ? -25.174 49.139 29.691  1.00  29.82 ? 241  ALA B C   1 
ATOM   4092 O O   . ALA B 1 241 ? -24.459 50.004 29.186  1.00  29.73 ? 241  ALA B O   1 
ATOM   4093 C CB  . ALA B 1 241 ? -24.802 46.949 28.564  1.00  29.90 ? 241  ALA B CB  1 
ATOM   4094 N N   . THR B 1 242 ? -25.468 49.083 30.987  1.00  29.94 ? 242  THR B N   1 
ATOM   4095 C CA  . THR B 1 242 ? -24.992 50.049 31.978  1.00  29.97 ? 242  THR B CA  1 
ATOM   4096 C C   . THR B 1 242 ? -23.471 50.137 31.926  1.00  30.05 ? 242  THR B C   1 
ATOM   4097 O O   . THR B 1 242 ? -22.908 51.176 31.582  1.00  29.95 ? 242  THR B O   1 
ATOM   4098 C CB  . THR B 1 242 ? -25.458 49.645 33.404  1.00  30.00 ? 242  THR B CB  1 
ATOM   4099 O OG1 . THR B 1 242 ? -26.862 49.354 33.384  1.00  30.12 ? 242  THR B OG1 1 
ATOM   4100 C CG2 . THR B 1 242 ? -25.189 50.755 34.417  1.00  29.94 ? 242  THR B CG2 1 
ATOM   4101 N N   . ARG B 1 243 ? -22.817 49.029 32.258  1.00  30.29 ? 243  ARG B N   1 
ATOM   4102 C CA  . ARG B 1 243 ? -21.365 48.912 32.165  1.00  30.60 ? 243  ARG B CA  1 
ATOM   4103 C C   . ARG B 1 243 ? -21.008 47.471 31.806  1.00  30.40 ? 243  ARG B C   1 
ATOM   4104 O O   . ARG B 1 243 ? -21.819 46.557 31.994  1.00  30.37 ? 243  ARG B O   1 
ATOM   4105 C CB  . ARG B 1 243 ? -20.686 49.365 33.467  1.00  30.79 ? 243  ARG B CB  1 
ATOM   4106 C CG  . ARG B 1 243 ? -21.098 48.575 34.699  1.00  32.00 ? 243  ARG B CG  1 
ATOM   4107 C CD  . ARG B 1 243 ? -21.054 49.423 35.959  1.00  34.36 ? 243  ARG B CD  1 
ATOM   4108 N NE  . ARG B 1 243 ? -21.311 48.593 37.134  1.00  36.80 ? 243  ARG B NE  1 
ATOM   4109 C CZ  . ARG B 1 243 ? -20.988 48.908 38.389  1.00  37.60 ? 243  ARG B CZ  1 
ATOM   4110 N NH1 . ARG B 1 243 ? -20.377 50.060 38.668  1.00  37.32 ? 243  ARG B NH1 1 
ATOM   4111 N NH2 . ARG B 1 243 ? -21.278 48.053 39.369  1.00  37.69 ? 243  ARG B NH2 1 
ATOM   4112 N N   . VAL B 1 244 ? -19.803 47.276 31.280  1.00  30.21 ? 244  VAL B N   1 
ATOM   4113 C CA  . VAL B 1 244 ? -19.396 45.973 30.772  1.00  30.16 ? 244  VAL B CA  1 
ATOM   4114 C C   . VAL B 1 244 ? -18.246 45.369 31.573  1.00  30.17 ? 244  VAL B C   1 
ATOM   4115 O O   . VAL B 1 244 ? -17.252 46.032 31.859  1.00  30.12 ? 244  VAL B O   1 
ATOM   4116 C CB  . VAL B 1 244 ? -19.019 46.042 29.262  1.00  30.07 ? 244  VAL B CB  1 
ATOM   4117 C CG1 . VAL B 1 244 ? -18.485 44.709 28.773  1.00  30.17 ? 244  VAL B CG1 1 
ATOM   4118 C CG2 . VAL B 1 244 ? -20.213 46.454 28.420  1.00  29.77 ? 244  VAL B CG2 1 
ATOM   4119 N N   . TYR B 1 245 ? -18.399 44.099 31.927  1.00  30.30 ? 245  TYR B N   1 
ATOM   4120 C CA  . TYR B 1 245 ? -17.311 43.329 32.503  1.00  30.68 ? 245  TYR B CA  1 
ATOM   4121 C C   . TYR B 1 245 ? -16.923 42.216 31.530  1.00  30.64 ? 245  TYR B C   1 
ATOM   4122 O O   . TYR B 1 245 ? -17.742 41.775 30.725  1.00  30.47 ? 245  TYR B O   1 
ATOM   4123 C CB  . TYR B 1 245 ? -17.713 42.748 33.870  1.00  30.86 ? 245  TYR B CB  1 
ATOM   4124 C CG  . TYR B 1 245 ? -17.907 43.791 34.952  1.00  31.02 ? 245  TYR B CG  1 
ATOM   4125 C CD1 . TYR B 1 245 ? -19.136 44.432 35.120  1.00  31.71 ? 245  TYR B CD1 1 
ATOM   4126 C CD2 . TYR B 1 245 ? -16.865 44.138 35.801  1.00  30.97 ? 245  TYR B CD2 1 
ATOM   4127 C CE1 . TYR B 1 245 ? -19.320 45.397 36.111  1.00  31.95 ? 245  TYR B CE1 1 
ATOM   4128 C CE2 . TYR B 1 245 ? -17.036 45.101 36.793  1.00  31.74 ? 245  TYR B CE2 1 
ATOM   4129 C CZ  . TYR B 1 245 ? -18.263 45.726 36.944  1.00  32.03 ? 245  TYR B CZ  1 
ATOM   4130 O OH  . TYR B 1 245 ? -18.426 46.679 37.926  1.00  32.13 ? 245  TYR B OH  1 
ATOM   4131 N N   . ALA B 1 246 ? -15.670 41.784 31.592  1.00  30.60 ? 246  ALA B N   1 
ATOM   4132 C CA  . ALA B 1 246 ? -15.232 40.653 30.809  1.00  30.60 ? 246  ALA B CA  1 
ATOM   4133 C C   . ALA B 1 246 ? -14.452 39.738 31.718  1.00  30.64 ? 246  ALA B C   1 
ATOM   4134 O O   . ALA B 1 246 ? -13.484 40.159 32.342  1.00  30.59 ? 246  ALA B O   1 
ATOM   4135 C CB  . ALA B 1 246 ? -14.379 41.107 29.649  1.00  30.87 ? 246  ALA B CB  1 
ATOM   4136 N N   . ILE B 1 247 ? -14.901 38.490 31.806  1.00  30.87 ? 247  ILE B N   1 
ATOM   4137 C CA  . ILE B 1 247 ? -14.244 37.473 32.612  1.00  31.01 ? 247  ILE B CA  1 
ATOM   4138 C C   . ILE B 1 247 ? -13.758 36.369 31.697  1.00  31.28 ? 247  ILE B C   1 
ATOM   4139 O O   . ILE B 1 247 ? -14.555 35.768 30.986  1.00  31.46 ? 247  ILE B O   1 
ATOM   4140 C CB  . ILE B 1 247 ? -15.203 36.856 33.631  1.00  30.88 ? 247  ILE B CB  1 
ATOM   4141 C CG1 . ILE B 1 247 ? -15.881 37.945 34.465  1.00  31.10 ? 247  ILE B CG1 1 
ATOM   4142 C CG2 . ILE B 1 247 ? -14.454 35.885 34.529  1.00  31.23 ? 247  ILE B CG2 1 
ATOM   4143 C CD1 . ILE B 1 247 ? -17.071 37.449 35.262  1.00  31.56 ? 247  ILE B CD1 1 
ATOM   4144 N N   . LEU B 1 248 ? -12.452 36.119 31.708  1.00  31.69 ? 248  LEU B N   1 
ATOM   4145 C CA  . LEU B 1 248 ? -11.862 35.031 30.940  1.00  32.33 ? 248  LEU B CA  1 
ATOM   4146 C C   . LEU B 1 248 ? -11.095 34.146 31.891  1.00  32.93 ? 248  LEU B C   1 
ATOM   4147 O O   . LEU B 1 248 ? -10.331 34.649 32.718  1.00  32.88 ? 248  LEU B O   1 
ATOM   4148 C CB  . LEU B 1 248 ? -10.872 35.547 29.894  1.00  32.19 ? 248  LEU B CB  1 
ATOM   4149 C CG  . LEU B 1 248 ? -11.095 36.776 29.017  1.00  32.53 ? 248  LEU B CG  1 
ATOM   4150 C CD1 . LEU B 1 248 ? -12.517 36.834 28.440  1.00  33.00 ? 248  LEU B CD1 1 
ATOM   4151 C CD2 . LEU B 1 248 ? -10.741 38.041 29.781  1.00  32.88 ? 248  LEU B CD2 1 
ATOM   4152 N N   . THR B 1 249 ? -11.271 32.832 31.777  1.00  33.64 ? 249  THR B N   1 
ATOM   4153 C CA  . THR B 1 249 ? -10.467 31.922 32.590  1.00  34.24 ? 249  THR B CA  1 
ATOM   4154 C C   . THR B 1 249 ? -8.970  31.992 32.239  1.00  34.46 ? 249  THR B C   1 
ATOM   4155 O O   . THR B 1 249 ? -8.142  32.108 33.133  1.00  34.39 ? 249  THR B O   1 
ATOM   4156 C CB  . THR B 1 249 ? -11.030 30.463 32.653  1.00  34.26 ? 249  THR B CB  1 
ATOM   4157 O OG1 . THR B 1 249 ? -10.024 29.531 32.237  1.00  35.27 ? 249  THR B OG1 1 
ATOM   4158 C CG2 . THR B 1 249 ? -12.266 30.288 31.782  1.00  34.37 ? 249  THR B CG2 1 
ATOM   4159 N N   . HIS B 1 250 ? -8.634  31.973 30.951  1.00  35.11 ? 250  HIS B N   1 
ATOM   4160 C CA  . HIS B 1 250 ? -7.233  32.082 30.515  1.00  35.80 ? 250  HIS B CA  1 
ATOM   4161 C C   . HIS B 1 250 ? -6.905  33.469 29.966  1.00  36.26 ? 250  HIS B C   1 
ATOM   4162 O O   . HIS B 1 250 ? -7.512  33.918 28.990  1.00  36.39 ? 250  HIS B O   1 
ATOM   4163 C CB  . HIS B 1 250 ? -6.902  31.016 29.467  1.00  35.78 ? 250  HIS B CB  1 
ATOM   4164 C CG  . HIS B 1 250 ? -7.276  29.628 29.879  1.00  35.77 ? 250  HIS B CG  1 
ATOM   4165 N ND1 . HIS B 1 250 ? -6.569  28.918 30.825  1.00  35.92 ? 250  HIS B ND1 1 
ATOM   4166 C CD2 . HIS B 1 250 ? -8.286  28.820 29.480  1.00  35.71 ? 250  HIS B CD2 1 
ATOM   4167 C CE1 . HIS B 1 250 ? -7.127  27.733 30.991  1.00  35.91 ? 250  HIS B CE1 1 
ATOM   4168 N NE2 . HIS B 1 250 ? -8.171  27.648 30.187  1.00  35.64 ? 250  HIS B NE2 1 
ATOM   4169 N N   . GLY B 1 251 ? -5.946  34.143 30.596  1.00  36.79 ? 251  GLY B N   1 
ATOM   4170 C CA  . GLY B 1 251 ? -5.546  35.486 30.176  1.00  37.41 ? 251  GLY B CA  1 
ATOM   4171 C C   . GLY B 1 251 ? -4.274  35.281 29.375  1.00  37.86 ? 251  GLY B C   1 
ATOM   4172 O O   . GLY B 1 251 ? -3.190  35.123 29.948  1.00  37.87 ? 251  GLY B O   1 
ATOM   4173 N N   . ILE B 1 252 ? -4.411  35.283 28.049  1.00  38.26 ? 252  ILE B N   1 
ATOM   4174 C CA  . ILE B 1 252 ? -3.292  35.014 27.135  1.00  38.73 ? 252  ILE B CA  1 
ATOM   4175 C C   . ILE B 1 252 ? -2.643  36.378 26.845  1.00  39.14 ? 252  ILE B C   1 
ATOM   4176 O O   . ILE B 1 252 ? -1.440  36.564 27.065  1.00  39.24 ? 252  ILE B O   1 
ATOM   4177 C CB  . ILE B 1 252 ? -3.698  34.277 25.819  1.00  38.59 ? 252  ILE B CB  1 
ATOM   4178 C CG1 . ILE B 1 252 ? -4.237  32.870 26.128  1.00  38.64 ? 252  ILE B CG1 1 
ATOM   4179 C CG2 . ILE B 1 252 ? -2.529  34.211 24.850  1.00  38.69 ? 252  ILE B CG2 1 
ATOM   4180 C CD1 . ILE B 1 252 ? -4.835  32.119 24.932  1.00  38.19 ? 252  ILE B CD1 1 
ATOM   4181 N N   . PHE B 1 253 ? -3.453  37.315 26.357  1.00  39.57 ? 253  PHE B N   1 
ATOM   4182 C CA  . PHE B 1 253 ? -3.055  38.715 26.181  1.00  40.00 ? 253  PHE B CA  1 
ATOM   4183 C C   . PHE B 1 253 ? -1.732  38.933 25.416  1.00  40.30 ? 253  PHE B C   1 
ATOM   4184 O O   . PHE B 1 253 ? -0.811  39.586 25.911  1.00  40.36 ? 253  PHE B O   1 
ATOM   4185 C CB  . PHE B 1 253 ? -3.024  39.457 27.531  1.00  40.00 ? 253  PHE B CB  1 
ATOM   4186 C CG  . PHE B 1 253 ? -4.303  39.372 28.327  1.00  39.73 ? 253  PHE B CG  1 
ATOM   4187 C CD1 . PHE B 1 253 ? -4.254  39.301 29.716  1.00  39.49 ? 253  PHE B CD1 1 
ATOM   4188 C CD2 . PHE B 1 253 ? -5.545  39.388 27.703  1.00  39.73 ? 253  PHE B CD2 1 
ATOM   4189 C CE1 . PHE B 1 253 ? -5.415  39.243 30.472  1.00  39.30 ? 253  PHE B CE1 1 
ATOM   4190 C CE2 . PHE B 1 253 ? -6.719  39.327 28.454  1.00  40.08 ? 253  PHE B CE2 1 
ATOM   4191 C CZ  . PHE B 1 253 ? -6.651  39.255 29.839  1.00  39.85 ? 253  PHE B CZ  1 
ATOM   4192 N N   . SER B 1 254 ? -1.647  38.390 24.206  1.00  40.78 ? 254  SER B N   1 
ATOM   4193 C CA  . SER B 1 254 ? -0.491  38.635 23.334  1.00  41.26 ? 254  SER B CA  1 
ATOM   4194 C C   . SER B 1 254 ? -0.707  39.868 22.451  1.00  41.68 ? 254  SER B C   1 
ATOM   4195 O O   . SER B 1 254 ? -1.850  40.277 22.212  1.00  41.98 ? 254  SER B O   1 
ATOM   4196 C CB  . SER B 1 254 ? -0.214  37.416 22.452  1.00  41.20 ? 254  SER B CB  1 
ATOM   4197 O OG  . SER B 1 254 ? -1.224  37.267 21.464  1.00  40.46 ? 254  SER B OG  1 
ATOM   4198 N N   . GLY B 1 255 ? 0.386   40.452 21.963  1.00  41.94 ? 255  GLY B N   1 
ATOM   4199 C CA  . GLY B 1 255 ? 0.298   41.602 21.067  1.00  42.18 ? 255  GLY B CA  1 
ATOM   4200 C C   . GLY B 1 255 ? -0.465  42.778 21.661  1.00  42.47 ? 255  GLY B C   1 
ATOM   4201 O O   . GLY B 1 255 ? -0.244  43.152 22.818  1.00  42.47 ? 255  GLY B O   1 
ATOM   4202 N N   . PRO B 1 256 ? -1.407  43.346 20.886  1.00  42.79 ? 256  PRO B N   1 
ATOM   4203 C CA  . PRO B 1 256 ? -1.997  44.649 21.219  1.00  43.08 ? 256  PRO B CA  1 
ATOM   4204 C C   . PRO B 1 256 ? -3.056  44.605 22.325  1.00  43.31 ? 256  PRO B C   1 
ATOM   4205 O O   . PRO B 1 256 ? -3.703  45.620 22.596  1.00  43.16 ? 256  PRO B O   1 
ATOM   4206 C CB  . PRO B 1 256 ? -2.629  45.091 19.893  1.00  43.06 ? 256  PRO B CB  1 
ATOM   4207 C CG  . PRO B 1 256 ? -2.944  43.809 19.165  1.00  42.94 ? 256  PRO B CG  1 
ATOM   4208 C CD  . PRO B 1 256 ? -2.127  42.687 19.779  1.00  42.83 ? 256  PRO B CD  1 
ATOM   4209 N N   . ALA B 1 257 ? -3.213  43.437 22.947  1.00  43.73 ? 257  ALA B N   1 
ATOM   4210 C CA  . ALA B 1 257 ? -4.194  43.211 24.012  1.00  43.94 ? 257  ALA B CA  1 
ATOM   4211 C C   . ALA B 1 257 ? -4.164  44.270 25.117  1.00  44.04 ? 257  ALA B C   1 
ATOM   4212 O O   . ALA B 1 257 ? -5.193  44.873 25.414  1.00  43.98 ? 257  ALA B O   1 
ATOM   4213 C CB  . ALA B 1 257 ? -4.024  41.812 24.600  1.00  44.03 ? 257  ALA B CB  1 
ATOM   4214 N N   . ILE B 1 258 ? -2.993  44.501 25.711  1.00  44.20 ? 258  ILE B N   1 
ATOM   4215 C CA  . ILE B 1 258 ? -2.862  45.492 26.784  1.00  44.47 ? 258  ILE B CA  1 
ATOM   4216 C C   . ILE B 1 258 ? -3.322  46.868 26.303  1.00  44.55 ? 258  ILE B C   1 
ATOM   4217 O O   . ILE B 1 258 ? -4.076  47.549 27.006  1.00  44.49 ? 258  ILE B O   1 
ATOM   4218 C CB  . ILE B 1 258 ? -1.418  45.545 27.381  1.00  44.53 ? 258  ILE B CB  1 
ATOM   4219 C CG1 . ILE B 1 258 ? -1.027  44.191 27.992  1.00  44.99 ? 258  ILE B CG1 1 
ATOM   4220 C CG2 . ILE B 1 258 ? -1.286  46.650 28.433  1.00  44.33 ? 258  ILE B CG2 1 
ATOM   4221 C CD1 . ILE B 1 258 ? -1.769  43.823 29.301  1.00  45.59 ? 258  ILE B CD1 1 
ATOM   4222 N N   . SER B 1 259 ? -2.886  47.249 25.100  1.00  44.71 ? 259  SER B N   1 
ATOM   4223 C CA  . SER B 1 259 ? -3.316  48.499 24.463  1.00  44.95 ? 259  SER B CA  1 
ATOM   4224 C C   . SER B 1 259 ? -4.819  48.524 24.188  1.00  45.04 ? 259  SER B C   1 
ATOM   4225 O O   . SER B 1 259 ? -5.504  49.487 24.544  1.00  44.95 ? 259  SER B O   1 
ATOM   4226 C CB  . SER B 1 259 ? -2.534  48.758 23.171  1.00  44.93 ? 259  SER B CB  1 
ATOM   4227 O OG  . SER B 1 259 ? -1.329  49.461 23.434  1.00  45.21 ? 259  SER B OG  1 
ATOM   4228 N N   . ARG B 1 260 ? -5.326  47.462 23.566  1.00  45.24 ? 260  ARG B N   1 
ATOM   4229 C CA  . ARG B 1 260 ? -6.757  47.333 23.286  1.00  45.50 ? 260  ARG B CA  1 
ATOM   4230 C C   . ARG B 1 260 ? -7.603  47.438 24.570  1.00  45.58 ? 260  ARG B C   1 
ATOM   4231 O O   . ARG B 1 260 ? -8.640  48.105 24.573  1.00  45.41 ? 260  ARG B O   1 
ATOM   4232 C CB  . ARG B 1 260 ? -7.048  46.015 22.551  1.00  45.67 ? 260  ARG B CB  1 
ATOM   4233 C CG  . ARG B 1 260 ? -7.911  46.150 21.292  1.00  45.72 ? 260  ARG B CG  1 
ATOM   4234 C CD  . ARG B 1 260 ? -7.062  46.130 20.031  1.00  46.35 ? 260  ARG B CD  1 
ATOM   4235 N NE  . ARG B 1 260 ? -6.497  44.803 19.788  1.00  47.28 ? 260  ARG B NE  1 
ATOM   4236 C CZ  . ARG B 1 260 ? -6.652  44.101 18.668  1.00  47.97 ? 260  ARG B CZ  1 
ATOM   4237 N NH1 . ARG B 1 260 ? -7.343  44.596 17.647  1.00  47.41 ? 260  ARG B NH1 1 
ATOM   4238 N NH2 . ARG B 1 260 ? -6.097  42.898 18.563  1.00  49.26 ? 260  ARG B NH2 1 
ATOM   4239 N N   . ILE B 1 261 ? -7.139  46.796 25.649  1.00  45.76 ? 261  ILE B N   1 
ATOM   4240 C CA  . ILE B 1 261 ? -7.821  46.815 26.955  1.00  45.96 ? 261  ILE B CA  1 
ATOM   4241 C C   . ILE B 1 261 ? -7.775  48.187 27.648  1.00  46.03 ? 261  ILE B C   1 
ATOM   4242 O O   . ILE B 1 261 ? -8.824  48.747 27.995  1.00  45.94 ? 261  ILE B O   1 
ATOM   4243 C CB  . ILE B 1 261 ? -7.284  45.709 27.918  1.00  46.02 ? 261  ILE B CB  1 
ATOM   4244 C CG1 . ILE B 1 261 ? -7.627  44.312 27.381  1.00  46.05 ? 261  ILE B CG1 1 
ATOM   4245 C CG2 . ILE B 1 261 ? -7.860  45.884 29.337  1.00  46.10 ? 261  ILE B CG2 1 
ATOM   4246 C CD1 . ILE B 1 261 ? -6.850  43.169 28.040  1.00  46.24 ? 261  ILE B CD1 1 
ATOM   4247 N N   . ASN B 1 262 ? -6.563  48.715 27.851  1.00  46.08 ? 262  ASN B N   1 
ATOM   4248 C CA  . ASN B 1 262 ? -6.369  50.014 28.513  1.00  46.05 ? 262  ASN B CA  1 
ATOM   4249 C C   . ASN B 1 262 ? -7.255  51.122 27.933  1.00  45.83 ? 262  ASN B C   1 
ATOM   4250 O O   . ASN B 1 262 ? -7.748  51.976 28.671  1.00  45.73 ? 262  ASN B O   1 
ATOM   4251 C CB  . ASN B 1 262 ? -4.890  50.440 28.481  1.00  46.15 ? 262  ASN B CB  1 
ATOM   4252 C CG  . ASN B 1 262 ? -4.053  49.799 29.598  1.00  46.44 ? 262  ASN B CG  1 
ATOM   4253 O OD1 . ASN B 1 262 ? -4.529  49.584 30.720  1.00  46.36 ? 262  ASN B OD1 1 
ATOM   4254 N ND2 . ASN B 1 262 ? -2.792  49.512 29.290  1.00  46.86 ? 262  ASN B ND2 1 
ATOM   4255 N N   . ASN B 1 263 ? -7.448  51.095 26.614  1.00  45.64 ? 263  ASN B N   1 
ATOM   4256 C CA  . ASN B 1 263 ? -8.348  52.024 25.925  1.00  45.45 ? 263  ASN B CA  1 
ATOM   4257 C C   . ASN B 1 263 ? -9.808  51.606 26.068  1.00  45.23 ? 263  ASN B C   1 
ATOM   4258 O O   . ASN B 1 263 ? -10.690 52.457 26.216  1.00  45.32 ? 263  ASN B O   1 
ATOM   4259 C CB  . ASN B 1 263 ? -8.028  52.112 24.422  1.00  45.58 ? 263  ASN B CB  1 
ATOM   4260 C CG  . ASN B 1 263 ? -6.588  52.516 24.130  1.00  45.77 ? 263  ASN B CG  1 
ATOM   4261 O OD1 . ASN B 1 263 ? -6.007  52.067 23.136  1.00  45.54 ? 263  ASN B OD1 1 
ATOM   4262 N ND2 . ASN B 1 263 ? -6.015  53.379 24.972  1.00  46.00 ? 263  ASN B ND2 1 
ATOM   4263 N N   . ALA B 1 264 ? -10.046 50.292 26.014  1.00  44.87 ? 264  ALA B N   1 
ATOM   4264 C CA  . ALA B 1 264 ? -11.396 49.722 25.892  1.00  44.49 ? 264  ALA B CA  1 
ATOM   4265 C C   . ALA B 1 264 ? -12.338 50.028 27.049  1.00  44.14 ? 264  ALA B C   1 
ATOM   4266 O O   . ALA B 1 264 ? -11.920 50.191 28.199  1.00  44.10 ? 264  ALA B O   1 
ATOM   4267 C CB  . ALA B 1 264 ? -11.325 48.226 25.658  1.00  44.58 ? 264  ALA B CB  1 
ATOM   4268 N N   . CYS B 1 265 ? -13.623 50.064 26.718  1.00  43.70 ? 265  CYS B N   1 
ATOM   4269 C CA  . CYS B 1 265 ? -14.655 50.571 27.611  1.00  43.49 ? 265  CYS B CA  1 
ATOM   4270 C C   . CYS B 1 265 ? -15.130 49.587 28.685  1.00  42.98 ? 265  CYS B C   1 
ATOM   4271 O O   . CYS B 1 265 ? -16.264 49.693 29.163  1.00  42.77 ? 265  CYS B O   1 
ATOM   4272 C CB  . CYS B 1 265 ? -15.844 51.037 26.778  1.00  43.61 ? 265  CYS B CB  1 
ATOM   4273 S SG  . CYS B 1 265 ? -16.555 49.705 25.769  1.00  44.46 ? 265  CYS B SG  1 
ATOM   4274 N N   . PHE B 1 266 ? -14.274 48.640 29.064  1.00  42.49 ? 266  PHE B N   1 
ATOM   4275 C CA  . PHE B 1 266 ? -14.585 47.723 30.162  1.00  42.18 ? 266  PHE B CA  1 
ATOM   4276 C C   . PHE B 1 266 ? -14.573 48.455 31.506  1.00  41.72 ? 266  PHE B C   1 
ATOM   4277 O O   . PHE B 1 266 ? -13.839 49.428 31.680  1.00  41.81 ? 266  PHE B O   1 
ATOM   4278 C CB  . PHE B 1 266 ? -13.581 46.560 30.212  1.00  42.36 ? 266  PHE B CB  1 
ATOM   4279 C CG  . PHE B 1 266 ? -13.533 45.729 28.956  1.00  42.80 ? 266  PHE B CG  1 
ATOM   4280 C CD1 . PHE B 1 266 ? -12.433 45.804 28.102  1.00  43.21 ? 266  PHE B CD1 1 
ATOM   4281 C CD2 . PHE B 1 266 ? -14.581 44.863 28.633  1.00  43.07 ? 266  PHE B CD2 1 
ATOM   4282 C CE1 . PHE B 1 266 ? -12.376 45.035 26.938  1.00  43.43 ? 266  PHE B CE1 1 
ATOM   4283 C CE2 . PHE B 1 266 ? -14.538 44.091 27.475  1.00  43.29 ? 266  PHE B CE2 1 
ATOM   4284 C CZ  . PHE B 1 266 ? -13.431 44.178 26.623  1.00  43.85 ? 266  PHE B CZ  1 
ATOM   4285 N N   . GLU B 1 267 ? -15.392 47.998 32.450  1.00  41.07 ? 267  GLU B N   1 
ATOM   4286 C CA  . GLU B 1 267 ? -15.219 48.415 33.833  1.00  40.53 ? 267  GLU B CA  1 
ATOM   4287 C C   . GLU B 1 267 ? -14.009 47.643 34.342  1.00  39.97 ? 267  GLU B C   1 
ATOM   4288 O O   . GLU B 1 267 ? -13.023 48.241 34.774  1.00  40.17 ? 267  GLU B O   1 
ATOM   4289 C CB  . GLU B 1 267 ? -16.454 48.104 34.684  1.00  40.72 ? 267  GLU B CB  1 
ATOM   4290 C CG  . GLU B 1 267 ? -16.534 48.877 36.013  1.00  41.32 ? 267  GLU B CG  1 
ATOM   4291 C CD  . GLU B 1 267 ? -17.496 50.063 35.967  1.00  42.27 ? 267  GLU B CD  1 
ATOM   4292 O OE1 . GLU B 1 267 ? -17.718 50.617 34.866  1.00  42.91 ? 267  GLU B OE1 1 
ATOM   4293 O OE2 . GLU B 1 267 ? -18.032 50.443 37.035  1.00  42.24 ? 267  GLU B OE2 1 
ATOM   4294 N N   . ALA B 1 268 ? -14.079 46.314 34.252  1.00  39.12 ? 268  ALA B N   1 
ATOM   4295 C CA  . ALA B 1 268 ? -12.993 45.435 34.699  1.00  38.23 ? 268  ALA B CA  1 
ATOM   4296 C C   . ALA B 1 268 ? -12.775 44.241 33.768  1.00  37.52 ? 268  ALA B C   1 
ATOM   4297 O O   . ALA B 1 268 ? -13.692 43.810 33.063  1.00  37.38 ? 268  ALA B O   1 
ATOM   4298 C CB  . ALA B 1 268 ? -13.248 44.954 36.135  1.00  38.28 ? 268  ALA B CB  1 
ATOM   4299 N N   . VAL B 1 269 ? -11.549 43.724 33.762  1.00  36.60 ? 269  VAL B N   1 
ATOM   4300 C CA  . VAL B 1 269 ? -11.238 42.488 33.058  1.00  35.80 ? 269  VAL B CA  1 
ATOM   4301 C C   . VAL B 1 269 ? -10.720 41.498 34.077  1.00  35.22 ? 269  VAL B C   1 
ATOM   4302 O O   . VAL B 1 269 ? -9.702  41.743 34.717  1.00  35.11 ? 269  VAL B O   1 
ATOM   4303 C CB  . VAL B 1 269 ? -10.184 42.679 31.937  1.00  35.81 ? 269  VAL B CB  1 
ATOM   4304 C CG1 . VAL B 1 269 ? -9.938  41.354 31.205  1.00  35.54 ? 269  VAL B CG1 1 
ATOM   4305 C CG2 . VAL B 1 269 ? -10.619 43.763 30.951  1.00  35.67 ? 269  VAL B CG2 1 
ATOM   4306 N N   . VAL B 1 270 ? -11.428 40.383 34.221  1.00  34.58 ? 270  VAL B N   1 
ATOM   4307 C CA  . VAL B 1 270 ? -11.083 39.374 35.212  1.00  33.98 ? 270  VAL B CA  1 
ATOM   4308 C C   . VAL B 1 270 ? -10.492 38.137 34.559  1.00  33.72 ? 270  VAL B C   1 
ATOM   4309 O O   . VAL B 1 270 ? -11.110 37.543 33.680  1.00  33.73 ? 270  VAL B O   1 
ATOM   4310 C CB  . VAL B 1 270 ? -12.308 38.981 36.059  1.00  33.87 ? 270  VAL B CB  1 
ATOM   4311 C CG1 . VAL B 1 270 ? -11.916 37.956 37.110  1.00  33.75 ? 270  VAL B CG1 1 
ATOM   4312 C CG2 . VAL B 1 270 ? -12.903 40.218 36.728  1.00  33.58 ? 270  VAL B CG2 1 
ATOM   4313 N N   . VAL B 1 271 ? -9.287  37.764 34.990  1.00  33.58 ? 271  VAL B N   1 
ATOM   4314 C CA  . VAL B 1 271 ? -8.662  36.498 34.582  1.00  33.48 ? 271  VAL B CA  1 
ATOM   4315 C C   . VAL B 1 271 ? -8.178  35.668 35.778  1.00  33.67 ? 271  VAL B C   1 
ATOM   4316 O O   . VAL B 1 271 ? -7.927  36.204 36.859  1.00  33.41 ? 271  VAL B O   1 
ATOM   4317 C CB  . VAL B 1 271 ? -7.491  36.688 33.566  1.00  33.23 ? 271  VAL B CB  1 
ATOM   4318 C CG1 . VAL B 1 271 ? -8.014  37.200 32.246  1.00  33.09 ? 271  VAL B CG1 1 
ATOM   4319 C CG2 . VAL B 1 271 ? -6.410  37.596 34.127  1.00  32.73 ? 271  VAL B CG2 1 
ATOM   4320 N N   . THR B 1 272 ? -8.074  34.356 35.578  1.00  34.03 ? 272  THR B N   1 
ATOM   4321 C CA  . THR B 1 272 ? -7.434  33.486 36.558  1.00  34.49 ? 272  THR B CA  1 
ATOM   4322 C C   . THR B 1 272 ? -5.931  33.464 36.297  1.00  35.03 ? 272  THR B C   1 
ATOM   4323 O O   . THR B 1 272 ? -5.468  33.880 35.227  1.00  35.00 ? 272  THR B O   1 
ATOM   4324 C CB  . THR B 1 272 ? -7.944  32.037 36.489  1.00  34.33 ? 272  THR B CB  1 
ATOM   4325 O OG1 . THR B 1 272 ? -7.361  31.386 35.357  1.00  34.39 ? 272  THR B OG1 1 
ATOM   4326 C CG2 . THR B 1 272 ? -9.473  31.982 36.399  1.00  34.07 ? 272  THR B CG2 1 
ATOM   4327 N N   . ASN B 1 273 ? -5.173  32.958 37.266  1.00  35.76 ? 273  ASN B N   1 
ATOM   4328 C CA  . ASN B 1 273 ? -3.738  32.807 37.089  1.00  36.60 ? 273  ASN B CA  1 
ATOM   4329 C C   . ASN B 1 273 ? -3.368  31.409 36.589  1.00  37.22 ? 273  ASN B C   1 
ATOM   4330 O O   . ASN B 1 273 ? -2.449  30.774 37.101  1.00  37.29 ? 273  ASN B O   1 
ATOM   4331 C CB  . ASN B 1 273 ? -2.973  33.191 38.365  1.00  36.56 ? 273  ASN B CB  1 
ATOM   4332 C CG  . ASN B 1 273 ? -3.464  32.442 39.598  1.00  37.23 ? 273  ASN B CG  1 
ATOM   4333 O OD1 . ASN B 1 273 ? -4.492  31.760 39.561  1.00  37.84 ? 273  ASN B OD1 1 
ATOM   4334 N ND2 . ASN B 1 273 ? -2.723  32.567 40.701  1.00  37.45 ? 273  ASN B ND2 1 
ATOM   4335 N N   . THR B 1 274 ? -4.102  30.927 35.586  1.00  38.16 ? 274  THR B N   1 
ATOM   4336 C CA  . THR B 1 274 ? -3.654  29.776 34.801  1.00  38.92 ? 274  THR B CA  1 
ATOM   4337 C C   . THR B 1 274 ? -2.488  30.252 33.949  1.00  39.69 ? 274  THR B C   1 
ATOM   4338 O O   . THR B 1 274 ? -1.640  29.461 33.542  1.00  39.84 ? 274  THR B O   1 
ATOM   4339 C CB  . THR B 1 274 ? -4.749  29.193 33.863  1.00  38.82 ? 274  THR B CB  1 
ATOM   4340 O OG1 . THR B 1 274 ? -5.282  30.229 33.029  1.00  38.74 ? 274  THR B OG1 1 
ATOM   4341 C CG2 . THR B 1 274 ? -5.878  28.544 34.656  1.00  39.01 ? 274  THR B CG2 1 
ATOM   4342 N N   . ILE B 1 275 ? -2.456  31.554 33.678  1.00  40.65 ? 275  ILE B N   1 
ATOM   4343 C CA  . ILE B 1 275 ? -1.317  32.175 33.018  1.00  41.70 ? 275  ILE B CA  1 
ATOM   4344 C C   . ILE B 1 275 ? -0.819  33.342 33.878  1.00  42.45 ? 275  ILE B C   1 
ATOM   4345 O O   . ILE B 1 275 ? -1.628  34.051 34.479  1.00  42.43 ? 275  ILE B O   1 
ATOM   4346 C CB  . ILE B 1 275 ? -1.667  32.599 31.555  1.00  41.74 ? 275  ILE B CB  1 
ATOM   4347 C CG1 . ILE B 1 275 ? -1.677  31.363 30.641  1.00  41.75 ? 275  ILE B CG1 1 
ATOM   4348 C CG2 . ILE B 1 275 ? -0.678  33.648 31.010  1.00  41.95 ? 275  ILE B CG2 1 
ATOM   4349 C CD1 . ILE B 1 275 ? -2.487  31.522 29.335  1.00  41.48 ? 275  ILE B CD1 1 
ATOM   4350 N N   . PRO B 1 276 ? 0.516   33.511 33.978  1.00  43.28 ? 276  PRO B N   1 
ATOM   4351 C CA  . PRO B 1 276 ? 1.116   34.651 34.665  1.00  44.05 ? 276  PRO B CA  1 
ATOM   4352 C C   . PRO B 1 276 ? 0.511   35.973 34.216  1.00  44.85 ? 276  PRO B C   1 
ATOM   4353 O O   . PRO B 1 276 ? 0.280   36.174 33.021  1.00  44.85 ? 276  PRO B O   1 
ATOM   4354 C CB  . PRO B 1 276 ? 2.593   34.586 34.244  1.00  44.12 ? 276  PRO B CB  1 
ATOM   4355 C CG  . PRO B 1 276 ? 2.739   33.359 33.378  1.00  43.58 ? 276  PRO B CG  1 
ATOM   4356 C CD  . PRO B 1 276 ? 1.538   32.514 33.618  1.00  43.32 ? 276  PRO B CD  1 
ATOM   4357 N N   . GLN B 1 277 ? 0.259   36.857 35.180  1.00  45.86 ? 277  GLN B N   1 
ATOM   4358 C CA  . GLN B 1 277 ? -0.390  38.147 34.924  1.00  46.84 ? 277  GLN B CA  1 
ATOM   4359 C C   . GLN B 1 277 ? 0.407   39.328 35.490  1.00  47.57 ? 277  GLN B C   1 
ATOM   4360 O O   . GLN B 1 277 ? 0.286   40.454 35.011  1.00  47.44 ? 277  GLN B O   1 
ATOM   4361 C CB  . GLN B 1 277 ? -1.815  38.155 35.501  1.00  46.65 ? 277  GLN B CB  1 
ATOM   4362 C CG  . GLN B 1 277 ? -2.751  37.071 34.961  1.00  46.34 ? 277  GLN B CG  1 
ATOM   4363 C CD  . GLN B 1 277 ? -2.936  37.118 33.447  1.00  46.20 ? 277  GLN B CD  1 
ATOM   4364 O OE1 . GLN B 1 277 ? -2.809  36.092 32.766  1.00  46.18 ? 277  GLN B OE1 1 
ATOM   4365 N NE2 . GLN B 1 277 ? -3.242  38.310 32.920  1.00  46.10 ? 277  GLN B NE2 1 
ATOM   4366 N N   . GLU B 1 278 ? 1.216   39.043 36.510  0.20  48.75 ? 278  GLU B N   1 
ATOM   4367 C CA  . GLU B 1 278 ? 1.983   40.042 37.264  0.20  49.94 ? 278  GLU B CA  1 
ATOM   4368 C C   . GLU B 1 278 ? 2.628   41.132 36.403  0.20  50.88 ? 278  GLU B C   1 
ATOM   4369 O O   . GLU B 1 278 ? 2.622   42.309 36.772  0.20  50.97 ? 278  GLU B O   1 
ATOM   4370 C CB  . GLU B 1 278 ? 3.049   39.338 38.110  0.20  49.84 ? 278  GLU B CB  1 
ATOM   4371 C CG  . GLU B 1 278 ? 2.520   38.149 38.914  0.20  49.91 ? 278  GLU B CG  1 
ATOM   4372 C CD  . GLU B 1 278 ? 2.122   36.964 38.040  0.20  49.84 ? 278  GLU B CD  1 
ATOM   4373 O OE1 . GLU B 1 278 ? 2.944   36.531 37.202  0.20  49.71 ? 278  GLU B OE1 1 
ATOM   4374 O OE2 . GLU B 1 278 ? 0.989   36.457 38.201  0.20  49.78 ? 278  GLU B OE2 1 
ATOM   4375 N N   . ASP B 1 279 ? 3.175   40.725 35.260  0.96  52.13 ? 279  ASP B N   1 
ATOM   4376 C CA  . ASP B 1 279 ? 3.828   41.634 34.312  0.96  53.39 ? 279  ASP B CA  1 
ATOM   4377 C C   . ASP B 1 279 ? 2.800   42.506 33.577  0.96  54.02 ? 279  ASP B C   1 
ATOM   4378 O O   . ASP B 1 279 ? 2.985   43.716 33.451  0.96  54.19 ? 279  ASP B O   1 
ATOM   4379 C CB  . ASP B 1 279 ? 4.663   40.822 33.308  0.96  53.55 ? 279  ASP B CB  1 
ATOM   4380 C CG  . ASP B 1 279 ? 5.937   41.538 32.871  0.96  54.14 ? 279  ASP B CG  1 
ATOM   4381 O OD1 . ASP B 1 279 ? 6.249   41.497 31.655  0.96  55.04 ? 279  ASP B OD1 1 
ATOM   4382 O OD2 . ASP B 1 279 ? 6.637   42.119 33.738  0.96  54.58 ? 279  ASP B OD2 1 
ATOM   4383 N N   . LYS B 1 280 ? 1.716   41.881 33.113  1.00  54.87 ? 280  LYS B N   1 
ATOM   4384 C CA  . LYS B 1 280 ? 0.627   42.566 32.400  1.00  55.66 ? 280  LYS B CA  1 
ATOM   4385 C C   . LYS B 1 280 ? -0.150  43.525 33.294  1.00  56.09 ? 280  LYS B C   1 
ATOM   4386 O O   . LYS B 1 280 ? -0.683  44.533 32.819  1.00  56.26 ? 280  LYS B O   1 
ATOM   4387 C CB  . LYS B 1 280 ? -0.356  41.548 31.810  1.00  55.61 ? 280  LYS B CB  1 
ATOM   4388 C CG  . LYS B 1 280 ? 0.275   40.478 30.927  1.00  56.44 ? 280  LYS B CG  1 
ATOM   4389 C CD  . LYS B 1 280 ? 0.682   41.017 29.552  1.00  57.21 ? 280  LYS B CD  1 
ATOM   4390 C CE  . LYS B 1 280 ? 1.043   39.880 28.614  1.00  57.82 ? 280  LYS B CE  1 
ATOM   4391 N NZ  . LYS B 1 280 ? -0.047  38.835 28.570  1.00  57.75 ? 280  LYS B NZ  1 
ATOM   4392 N N   . MET B 1 281 ? -0.223  43.197 34.583  1.00  56.55 ? 281  MET B N   1 
ATOM   4393 C CA  . MET B 1 281 ? -0.981  43.987 35.551  1.00  56.79 ? 281  MET B CA  1 
ATOM   4394 C C   . MET B 1 281 ? -0.347  45.349 35.819  1.00  56.96 ? 281  MET B C   1 
ATOM   4395 O O   . MET B 1 281 ? -1.067  46.308 36.088  1.00  57.06 ? 281  MET B O   1 
ATOM   4396 C CB  . MET B 1 281 ? -1.178  43.221 36.864  1.00  56.91 ? 281  MET B CB  1 
ATOM   4397 C CG  . MET B 1 281 ? -2.138  42.028 36.776  1.00  56.95 ? 281  MET B CG  1 
ATOM   4398 S SD  . MET B 1 281 ? -2.030  40.919 38.206  1.00  56.85 ? 281  MET B SD  1 
ATOM   4399 C CE  . MET B 1 281 ? -2.914  41.863 39.452  1.00  56.82 ? 281  MET B CE  1 
ATOM   4400 N N   . LYS B 1 282 ? 0.984   45.437 35.745  0.99  57.14 ? 282  LYS B N   1 
ATOM   4401 C CA  . LYS B 1 282 ? 1.682   46.725 35.899  0.99  57.29 ? 282  LYS B CA  1 
ATOM   4402 C C   . LYS B 1 282 ? 1.226   47.718 34.833  0.99  57.05 ? 282  LYS B C   1 
ATOM   4403 O O   . LYS B 1 282 ? 0.887   48.863 35.142  0.99  57.03 ? 282  LYS B O   1 
ATOM   4404 C CB  . LYS B 1 282 ? 3.209   46.561 35.824  0.99  57.47 ? 282  LYS B CB  1 
ATOM   4405 C CG  . LYS B 1 282 ? 3.870   45.982 37.077  0.99  58.22 ? 282  LYS B CG  1 
ATOM   4406 C CD  . LYS B 1 282 ? 5.400   46.145 37.017  0.99  58.93 ? 282  LYS B CD  1 
ATOM   4407 C CE  . LYS B 1 282 ? 6.097   45.351 38.122  0.99  59.45 ? 282  LYS B CE  1 
ATOM   4408 N NZ  . LYS B 1 282 ? 7.559   45.712 38.249  0.99  59.28 ? 282  LYS B NZ  1 
ATOM   4409 N N   . HIS B 1 283 ? 1.198   47.255 33.585  1.00  56.72 ? 283  HIS B N   1 
ATOM   4410 C CA  . HIS B 1 283 ? 0.889   48.106 32.436  1.00  56.23 ? 283  HIS B CA  1 
ATOM   4411 C C   . HIS B 1 283 ? -0.610  48.241 32.131  1.00  55.45 ? 283  HIS B C   1 
ATOM   4412 O O   . HIS B 1 283 ? -0.991  49.037 31.272  1.00  55.23 ? 283  HIS B O   1 
ATOM   4413 C CB  . HIS B 1 283 ? 1.642   47.610 31.195  1.00  56.56 ? 283  HIS B CB  1 
ATOM   4414 C CG  . HIS B 1 283 ? 3.125   47.501 31.386  1.00  57.44 ? 283  HIS B CG  1 
ATOM   4415 N ND1 . HIS B 1 283 ? 3.945   48.603 31.523  1.00  58.30 ? 283  HIS B ND1 1 
ATOM   4416 C CD2 . HIS B 1 283 ? 3.938   46.419 31.447  1.00  58.14 ? 283  HIS B CD2 1 
ATOM   4417 C CE1 . HIS B 1 283 ? 5.196   48.205 31.669  1.00  58.41 ? 283  HIS B CE1 1 
ATOM   4418 N NE2 . HIS B 1 283 ? 5.219   46.884 31.627  1.00  58.75 ? 283  HIS B NE2 1 
ATOM   4419 N N   . CYS B 1 284 ? -1.444  47.464 32.828  1.00  54.51 ? 284  CYS B N   1 
ATOM   4420 C CA  . CYS B 1 284 ? -2.903  47.490 32.638  1.00  53.51 ? 284  CYS B CA  1 
ATOM   4421 C C   . CYS B 1 284 ? -3.668  47.416 33.966  1.00  52.40 ? 284  CYS B C   1 
ATOM   4422 O O   . CYS B 1 284 ? -3.652  46.386 34.647  1.00  52.21 ? 284  CYS B O   1 
ATOM   4423 C CB  . CYS B 1 284 ? -3.344  46.366 31.695  1.00  53.71 ? 284  CYS B CB  1 
ATOM   4424 S SG  . CYS B 1 284 ? -5.122  46.351 31.305  1.00  54.99 ? 284  CYS B SG  1 
ATOM   4425 N N   . SER B 1 285 ? -4.347  48.513 34.309  1.00  51.09 ? 285  SER B N   1 
ATOM   4426 C CA  . SER B 1 285 ? -4.984  48.690 35.627  1.00  49.64 ? 285  SER B CA  1 
ATOM   4427 C C   . SER B 1 285 ? -6.409  48.139 35.728  1.00  48.50 ? 285  SER B C   1 
ATOM   4428 O O   . SER B 1 285 ? -7.043  48.238 36.789  1.00  48.48 ? 285  SER B O   1 
ATOM   4429 C CB  . SER B 1 285 ? -4.980  50.175 36.027  1.00  49.74 ? 285  SER B CB  1 
ATOM   4430 O OG  . SER B 1 285 ? -5.975  50.903 35.324  1.00  49.38 ? 285  SER B OG  1 
ATOM   4431 N N   . LYS B 1 286 ? -6.902  47.562 34.631  1.00  46.79 ? 286  LYS B N   1 
ATOM   4432 C CA  . LYS B 1 286 ? -8.247  46.994 34.589  1.00  45.01 ? 286  LYS B CA  1 
ATOM   4433 C C   . LYS B 1 286 ? -8.260  45.491 34.847  1.00  43.83 ? 286  LYS B C   1 
ATOM   4434 O O   . LYS B 1 286 ? -9.324  44.899 35.031  1.00  43.71 ? 286  LYS B O   1 
ATOM   4435 C CB  . LYS B 1 286 ? -8.926  47.304 33.257  1.00  45.08 ? 286  LYS B CB  1 
ATOM   4436 C CG  . LYS B 1 286 ? -9.258  48.772 33.053  1.00  44.96 ? 286  LYS B CG  1 
ATOM   4437 C CD  . LYS B 1 286 ? -10.693 48.932 32.572  1.00  44.71 ? 286  LYS B CD  1 
ATOM   4438 C CE  . LYS B 1 286 ? -10.933 50.296 31.952  1.00  44.86 ? 286  LYS B CE  1 
ATOM   4439 N NZ  . LYS B 1 286 ? -10.594 50.317 30.493  1.00  45.19 ? 286  LYS B NZ  1 
ATOM   4440 N N   . ILE B 1 287 ? -7.074  44.884 34.866  1.00  42.35 ? 287  ILE B N   1 
ATOM   4441 C CA  . ILE B 1 287 ? -6.936  43.436 35.060  1.00  40.88 ? 287  ILE B CA  1 
ATOM   4442 C C   . ILE B 1 287 ? -6.919  43.016 36.535  1.00  39.94 ? 287  ILE B C   1 
ATOM   4443 O O   . ILE B 1 287 ? -6.034  43.392 37.305  1.00  39.85 ? 287  ILE B O   1 
ATOM   4444 C CB  . ILE B 1 287 ? -5.704  42.856 34.300  1.00  40.79 ? 287  ILE B CB  1 
ATOM   4445 C CG1 . ILE B 1 287 ? -5.894  43.018 32.786  1.00  40.49 ? 287  ILE B CG1 1 
ATOM   4446 C CG2 . ILE B 1 287 ? -5.487  41.388 34.651  1.00  40.64 ? 287  ILE B CG2 1 
ATOM   4447 C CD1 . ILE B 1 287 ? -4.684  42.661 31.939  1.00  40.22 ? 287  ILE B CD1 1 
ATOM   4448 N N   . GLN B 1 288 ? -7.921  42.233 36.907  1.00  38.75 ? 288  GLN B N   1 
ATOM   4449 C CA  . GLN B 1 288 ? -7.978  41.621 38.218  1.00  37.78 ? 288  GLN B CA  1 
ATOM   4450 C C   . GLN B 1 288 ? -7.709  40.134 38.046  1.00  37.05 ? 288  GLN B C   1 
ATOM   4451 O O   . GLN B 1 288 ? -8.008  39.565 36.994  1.00  37.03 ? 288  GLN B O   1 
ATOM   4452 C CB  . GLN B 1 288 ? -9.333  41.882 38.868  1.00  37.72 ? 288  GLN B CB  1 
ATOM   4453 C CG  . GLN B 1 288 ? -9.582  43.365 39.080  1.00  38.05 ? 288  GLN B CG  1 
ATOM   4454 C CD  . GLN B 1 288 ? -10.889 43.665 39.771  1.00  38.35 ? 288  GLN B CD  1 
ATOM   4455 O OE1 . GLN B 1 288 ? -11.633 44.547 39.349  1.00  38.53 ? 288  GLN B OE1 1 
ATOM   4456 N NE2 . GLN B 1 288 ? -11.174 42.937 40.845  1.00  38.64 ? 288  GLN B NE2 1 
ATOM   4457 N N   . VAL B 1 289 ? -7.123  39.517 39.071  1.00  36.10 ? 289  VAL B N   1 
ATOM   4458 C CA  . VAL B 1 289 ? -6.683  38.136 38.989  1.00  35.12 ? 289  VAL B CA  1 
ATOM   4459 C C   . VAL B 1 289 ? -7.294  37.290 40.089  1.00  34.61 ? 289  VAL B C   1 
ATOM   4460 O O   . VAL B 1 289 ? -7.128  37.590 41.271  1.00  34.54 ? 289  VAL B O   1 
ATOM   4461 C CB  . VAL B 1 289 ? -5.148  38.042 39.069  1.00  35.02 ? 289  VAL B CB  1 
ATOM   4462 C CG1 . VAL B 1 289 ? -4.684  36.575 39.105  1.00  35.07 ? 289  VAL B CG1 1 
ATOM   4463 C CG2 . VAL B 1 289 ? -4.530  38.765 37.898  1.00  34.88 ? 289  VAL B CG2 1 
ATOM   4464 N N   . ILE B 1 290 ? -8.009  36.240 39.689  1.00  33.97 ? 290  ILE B N   1 
ATOM   4465 C CA  . ILE B 1 290 ? -8.413  35.194 40.618  1.00  33.58 ? 290  ILE B CA  1 
ATOM   4466 C C   . ILE B 1 290 ? -7.268  34.207 40.807  1.00  33.21 ? 290  ILE B C   1 
ATOM   4467 O O   . ILE B 1 290 ? -6.622  33.803 39.844  1.00  33.13 ? 290  ILE B O   1 
ATOM   4468 C CB  . ILE B 1 290 ? -9.631  34.401 40.106  1.00  33.66 ? 290  ILE B CB  1 
ATOM   4469 C CG1 . ILE B 1 290 ? -10.581 35.317 39.321  1.00  34.00 ? 290  ILE B CG1 1 
ATOM   4470 C CG2 . ILE B 1 290 ? -10.341 33.695 41.280  1.00  33.70 ? 290  ILE B CG2 1 
ATOM   4471 C CD1 . ILE B 1 290 ? -11.825 34.616 38.784  1.00  34.58 ? 290  ILE B CD1 1 
ATOM   4472 N N   . ASP B 1 291 ? -7.014  33.823 42.050  1.00  32.93 ? 291  ASP B N   1 
ATOM   4473 C CA  . ASP B 1 291 ? -6.038  32.782 42.314  1.00  32.80 ? 291  ASP B CA  1 
ATOM   4474 C C   . ASP B 1 291 ? -6.730  31.439 42.266  1.00  32.59 ? 291  ASP B C   1 
ATOM   4475 O O   . ASP B 1 291 ? -7.707  31.217 42.967  1.00  32.68 ? 291  ASP B O   1 
ATOM   4476 C CB  . ASP B 1 291 ? -5.375  32.976 43.671  1.00  32.96 ? 291  ASP B CB  1 
ATOM   4477 C CG  . ASP B 1 291 ? -4.240  32.004 43.906  1.00  33.38 ? 291  ASP B CG  1 
ATOM   4478 O OD1 . ASP B 1 291 ? -3.824  31.320 42.946  1.00  33.23 ? 291  ASP B OD1 1 
ATOM   4479 O OD2 . ASP B 1 291 ? -3.760  31.922 45.056  1.00  34.78 ? 291  ASP B OD2 1 
ATOM   4480 N N   . ILE B 1 292 ? -6.223  30.546 41.429  1.00  32.44 ? 292  ILE B N   1 
ATOM   4481 C CA  . ILE B 1 292 ? -6.842  29.232 41.253  1.00  32.25 ? 292  ILE B CA  1 
ATOM   4482 C C   . ILE B 1 292 ? -5.974  28.094 41.807  1.00  31.99 ? 292  ILE B C   1 
ATOM   4483 O O   . ILE B 1 292 ? -6.269  26.911 41.595  1.00  32.09 ? 292  ILE B O   1 
ATOM   4484 C CB  . ILE B 1 292 ? -7.263  28.981 39.770  1.00  32.32 ? 292  ILE B CB  1 
ATOM   4485 C CG1 . ILE B 1 292 ? -6.140  29.333 38.784  1.00  32.21 ? 292  ILE B CG1 1 
ATOM   4486 C CG2 . ILE B 1 292 ? -8.510  29.776 39.437  1.00  32.62 ? 292  ILE B CG2 1 
ATOM   4487 C CD1 . ILE B 1 292 ? -5.248  28.150 38.394  1.00  32.18 ? 292  ILE B CD1 1 
ATOM   4488 N N   . SER B 1 293 ? -4.928  28.473 42.543  1.00  31.53 ? 293  SER B N   1 
ATOM   4489 C CA  . SER B 1 293 ? -3.948  27.529 43.080  1.00  30.86 ? 293  SER B CA  1 
ATOM   4490 C C   . SER B 1 293 ? -4.530  26.558 44.109  1.00  30.55 ? 293  SER B C   1 
ATOM   4491 O O   . SER B 1 293 ? -4.118  25.405 44.163  1.00  30.48 ? 293  SER B O   1 
ATOM   4492 C CB  . SER B 1 293 ? -2.741  28.273 43.656  1.00  30.76 ? 293  SER B CB  1 
ATOM   4493 O OG  . SER B 1 293 ? -3.137  29.222 44.626  1.00  30.44 ? 293  SER B OG  1 
ATOM   4494 N N   . MET B 1 294 ? -5.487  27.019 44.908  0.80  30.18 ? 294  MET B N   1 
ATOM   4495 C CA  . MET B 1 294 ? -6.185  26.149 45.855  0.80  29.96 ? 294  MET B CA  1 
ATOM   4496 C C   . MET B 1 294 ? -7.031  25.098 45.136  0.80  29.20 ? 294  MET B C   1 
ATOM   4497 O O   . MET B 1 294 ? -7.165  23.967 45.608  0.80  29.08 ? 294  MET B O   1 
ATOM   4498 C CB  . MET B 1 294 ? -7.051  26.967 46.822  0.80  30.32 ? 294  MET B CB  1 
ATOM   4499 C CG  . MET B 1 294 ? -8.198  27.748 46.176  0.80  31.88 ? 294  MET B CG  1 
ATOM   4500 S SD  . MET B 1 294 ? -7.665  28.767 44.785  0.80  35.12 ? 294  MET B SD  1 
ATOM   4501 C CE  . MET B 1 294 ? -6.716  30.027 45.650  0.80  34.25 ? 294  MET B CE  1 
ATOM   4502 N N   . ILE B 1 295 ? -7.594  25.481 43.995  1.00  28.32 ? 295  ILE B N   1 
ATOM   4503 C CA  . ILE B 1 295 ? -8.361  24.554 43.175  1.00  27.78 ? 295  ILE B CA  1 
ATOM   4504 C C   . ILE B 1 295 ? -7.437  23.496 42.570  1.00  27.31 ? 295  ILE B C   1 
ATOM   4505 O O   . ILE B 1 295 ? -7.762  22.311 42.579  1.00  27.37 ? 295  ILE B O   1 
ATOM   4506 C CB  . ILE B 1 295 ? -9.174  25.279 42.071  1.00  27.86 ? 295  ILE B CB  1 
ATOM   4507 C CG1 . ILE B 1 295 ? -10.086 26.344 42.697  1.00  27.96 ? 295  ILE B CG1 1 
ATOM   4508 C CG2 . ILE B 1 295 ? -9.997  24.274 41.264  1.00  27.56 ? 295  ILE B CG2 1 
ATOM   4509 C CD1 . ILE B 1 295 ? -10.556 27.418 41.741  1.00  28.69 ? 295  ILE B CD1 1 
ATOM   4510 N N   . LEU B 1 296 ? -6.284  23.926 42.064  1.00  26.58 ? 296  LEU B N   1 
ATOM   4511 C CA  . LEU B 1 296 ? -5.315  22.998 41.501  1.00  25.74 ? 296  LEU B CA  1 
ATOM   4512 C C   . LEU B 1 296 ? -4.659  22.145 42.584  1.00  25.40 ? 296  LEU B C   1 
ATOM   4513 O O   . LEU B 1 296 ? -4.528  20.934 42.423  1.00  25.09 ? 296  LEU B O   1 
ATOM   4514 C CB  . LEU B 1 296 ? -4.275  23.732 40.643  1.00  25.73 ? 296  LEU B CB  1 
ATOM   4515 C CG  . LEU B 1 296 ? -4.727  24.251 39.270  1.00  25.10 ? 296  LEU B CG  1 
ATOM   4516 C CD1 . LEU B 1 296 ? -3.524  24.716 38.465  1.00  24.22 ? 296  LEU B CD1 1 
ATOM   4517 C CD2 . LEU B 1 296 ? -5.490  23.191 38.498  1.00  24.72 ? 296  LEU B CD2 1 
ATOM   4518 N N   . ALA B 1 297 ? -4.275  22.777 43.692  1.00  25.31 ? 297  ALA B N   1 
ATOM   4519 C CA  . ALA B 1 297 ? -3.710  22.063 44.850  1.00  25.12 ? 297  ALA B CA  1 
ATOM   4520 C C   . ALA B 1 297 ? -4.637  20.964 45.349  1.00  24.92 ? 297  ALA B C   1 
ATOM   4521 O O   . ALA B 1 297 ? -4.211  19.816 45.495  1.00  24.94 ? 297  ALA B O   1 
ATOM   4522 C CB  . ALA B 1 297 ? -3.386  23.026 45.981  1.00  24.96 ? 297  ALA B CB  1 
ATOM   4523 N N   . GLU B 1 298 ? -5.898  21.322 45.591  0.50  24.68 ? 298  GLU B N   1 
ATOM   4524 C CA  . GLU B 1 298 ? -6.905  20.365 46.041  0.50  24.51 ? 298  GLU B CA  1 
ATOM   4525 C C   . GLU B 1 298 ? -7.042  19.212 45.055  0.50  24.45 ? 298  GLU B C   1 
ATOM   4526 O O   . GLU B 1 298 ? -7.121  18.055 45.463  0.50  24.31 ? 298  GLU B O   1 
ATOM   4527 C CB  . GLU B 1 298 ? -8.258  21.048 46.248  0.50  24.40 ? 298  GLU B CB  1 
ATOM   4528 C CG  . GLU B 1 298 ? -9.267  20.194 47.000  0.50  24.66 ? 298  GLU B CG  1 
ATOM   4529 C CD  . GLU B 1 298 ? -8.981  20.108 48.497  0.50  25.31 ? 298  GLU B CD  1 
ATOM   4530 O OE1 . GLU B 1 298 ? -7.807  20.262 48.904  0.50  25.93 ? 298  GLU B OE1 1 
ATOM   4531 O OE2 . GLU B 1 298 ? -9.939  19.895 49.269  0.50  25.36 ? 298  GLU B OE2 1 
ATOM   4532 N N   . ALA B 1 299 ? -7.035  19.536 43.762  1.00  24.57 ? 299  ALA B N   1 
ATOM   4533 C CA  . ALA B 1 299 ? -7.148  18.535 42.698  1.00  24.62 ? 299  ALA B CA  1 
ATOM   4534 C C   . ALA B 1 299 ? -6.041  17.497 42.799  1.00  24.78 ? 299  ALA B C   1 
ATOM   4535 O O   . ALA B 1 299 ? -6.316  16.302 42.832  1.00  24.74 ? 299  ALA B O   1 
ATOM   4536 C CB  . ALA B 1 299 ? -7.142  19.193 41.331  1.00  24.53 ? 299  ALA B CB  1 
ATOM   4537 N N   . ILE B 1 300 ? -4.795  17.962 42.858  1.00  25.17 ? 300  ILE B N   1 
ATOM   4538 C CA  . ILE B 1 300 ? -3.640  17.092 43.073  1.00  25.56 ? 300  ILE B CA  1 
ATOM   4539 C C   . ILE B 1 300 ? -3.840  16.276 44.346  1.00  26.20 ? 300  ILE B C   1 
ATOM   4540 O O   . ILE B 1 300 ? -3.736  15.043 44.332  1.00  26.15 ? 300  ILE B O   1 
ATOM   4541 C CB  . ILE B 1 300 ? -2.331  17.904 43.198  1.00  25.34 ? 300  ILE B CB  1 
ATOM   4542 C CG1 . ILE B 1 300 ? -1.978  18.554 41.864  1.00  25.10 ? 300  ILE B CG1 1 
ATOM   4543 C CG2 . ILE B 1 300 ? -1.174  17.015 43.662  1.00  25.01 ? 300  ILE B CG2 1 
ATOM   4544 C CD1 . ILE B 1 300 ? -1.240  19.867 42.014  1.00  24.36 ? 300  ILE B CD1 1 
ATOM   4545 N N   . ARG B 1 301 ? -4.138  16.983 45.436  1.00  26.92 ? 301  ARG B N   1 
ATOM   4546 C CA  . ARG B 1 301 ? -4.324  16.382 46.750  1.00  27.50 ? 301  ARG B CA  1 
ATOM   4547 C C   . ARG B 1 301 ? -5.362  15.268 46.708  1.00  27.87 ? 301  ARG B C   1 
ATOM   4548 O O   . ARG B 1 301 ? -5.098  14.172 47.203  1.00  27.73 ? 301  ARG B O   1 
ATOM   4549 C CB  . ARG B 1 301 ? -4.737  17.453 47.758  1.00  27.74 ? 301  ARG B CB  1 
ATOM   4550 C CG  . ARG B 1 301 ? -4.702  17.010 49.216  1.00  28.61 ? 301  ARG B CG  1 
ATOM   4551 C CD  . ARG B 1 301 ? -5.515  17.963 50.074  1.00  29.99 ? 301  ARG B CD  1 
ATOM   4552 N NE  . ARG B 1 301 ? -6.292  17.230 51.068  1.00  31.61 ? 301  ARG B NE  1 
ATOM   4553 C CZ  . ARG B 1 301 ? -7.522  16.755 50.871  1.00  32.41 ? 301  ARG B CZ  1 
ATOM   4554 N NH1 . ARG B 1 301 ? -8.134  16.934 49.707  1.00  33.09 ? 301  ARG B NH1 1 
ATOM   4555 N NH2 . ARG B 1 301 ? -8.146  16.095 51.840  1.00  32.82 ? 301  ARG B NH2 1 
ATOM   4556 N N   . ARG B 1 302 ? -6.525  15.551 46.111  0.70  28.39 ? 302  ARG B N   1 
ATOM   4557 C CA  . ARG B 1 302 ? -7.596  14.563 45.969  0.70  28.87 ? 302  ARG B CA  1 
ATOM   4558 C C   . ARG B 1 302 ? -7.116  13.396 45.124  0.70  29.34 ? 302  ARG B C   1 
ATOM   4559 O O   . ARG B 1 302 ? -7.321  12.236 45.482  0.70  29.44 ? 302  ARG B O   1 
ATOM   4560 C CB  . ARG B 1 302 ? -8.840  15.177 45.315  0.70  28.79 ? 302  ARG B CB  1 
ATOM   4561 C CG  . ARG B 1 302 ? -9.444  16.373 46.032  0.70  28.79 ? 302  ARG B CG  1 
ATOM   4562 C CD  . ARG B 1 302 ? -10.311 15.969 47.206  0.70  28.51 ? 302  ARG B CD  1 
ATOM   4563 N NE  . ARG B 1 302 ? -10.720 17.127 47.996  0.70  28.14 ? 302  ARG B NE  1 
ATOM   4564 C CZ  . ARG B 1 302 ? -11.973 17.551 48.134  0.70  28.70 ? 302  ARG B CZ  1 
ATOM   4565 N NH1 . ARG B 1 302 ? -12.983 16.912 47.548  0.70  28.96 ? 302  ARG B NH1 1 
ATOM   4566 N NH2 . ARG B 1 302 ? -12.215 18.618 48.880  0.70  29.33 ? 302  ARG B NH2 1 
ATOM   4567 N N   . THR B 1 303 ? -6.472  13.720 44.003  1.00  30.00 ? 303  THR B N   1 
ATOM   4568 C CA  . THR B 1 303 ? -5.976  12.716 43.067  1.00  30.71 ? 303  THR B CA  1 
ATOM   4569 C C   . THR B 1 303 ? -5.104  11.706 43.795  1.00  31.44 ? 303  THR B C   1 
ATOM   4570 O O   . THR B 1 303 ? -5.372  10.504 43.764  1.00  31.63 ? 303  THR B O   1 
ATOM   4571 C CB  . THR B 1 303 ? -5.181  13.357 41.900  1.00  30.66 ? 303  THR B CB  1 
ATOM   4572 O OG1 . THR B 1 303 ? -6.047  14.217 41.144  1.00  30.08 ? 303  THR B OG1 1 
ATOM   4573 C CG2 . THR B 1 303 ? -4.603  12.282 40.976  1.00  30.33 ? 303  THR B CG2 1 
ATOM   4574 N N   . HIS B 1 304 ? -4.083  12.208 44.478  1.00  32.38 ? 304  HIS B N   1 
ATOM   4575 C CA  . HIS B 1 304 ? -3.122  11.358 45.167  1.00  33.31 ? 304  HIS B CA  1 
ATOM   4576 C C   . HIS B 1 304 ? -3.754  10.466 46.228  1.00  33.92 ? 304  HIS B C   1 
ATOM   4577 O O   . HIS B 1 304 ? -3.205  9.419  46.556  1.00  34.05 ? 304  HIS B O   1 
ATOM   4578 C CB  . HIS B 1 304 ? -2.022  12.210 45.798  1.00  33.33 ? 304  HIS B CB  1 
ATOM   4579 C CG  . HIS B 1 304 ? -0.986  11.409 46.515  1.00  33.60 ? 304  HIS B CG  1 
ATOM   4580 N ND1 . HIS B 1 304 ? -0.153  10.523 45.867  1.00  34.40 ? 304  HIS B ND1 1 
ATOM   4581 C CD2 . HIS B 1 304 ? -0.651  11.351 47.824  1.00  34.04 ? 304  HIS B CD2 1 
ATOM   4582 C CE1 . HIS B 1 304 ? 0.656   9.957  46.745  1.00  34.20 ? 304  HIS B CE1 1 
ATOM   4583 N NE2 . HIS B 1 304 ? 0.374   10.441 47.940  1.00  34.27 ? 304  HIS B NE2 1 
ATOM   4584 N N   . ASN B 1 305 ? -4.902  10.881 46.755  1.00  34.81 ? 305  ASN B N   1 
ATOM   4585 C CA  . ASN B 1 305 ? -5.558  10.158 47.837  1.00  35.78 ? 305  ASN B CA  1 
ATOM   4586 C C   . ASN B 1 305 ? -6.700  9.278  47.361  1.00  36.40 ? 305  ASN B C   1 
ATOM   4587 O O   . ASN B 1 305 ? -7.140  8.386  48.086  1.00  36.83 ? 305  ASN B O   1 
ATOM   4588 C CB  . ASN B 1 305 ? -6.083  11.127 48.900  1.00  35.81 ? 305  ASN B CB  1 
ATOM   4589 C CG  . ASN B 1 305 ? -4.976  11.936 49.560  1.00  36.58 ? 305  ASN B CG  1 
ATOM   4590 O OD1 . ASN B 1 305 ? -3.852  11.455 49.735  1.00  37.27 ? 305  ASN B OD1 1 
ATOM   4591 N ND2 . ASN B 1 305 ? -5.293  13.175 49.939  1.00  36.93 ? 305  ASN B ND2 1 
ATOM   4592 N N   . GLY B 1 306 ? -7.188  9.528  46.153  1.00  37.00 ? 306  GLY B N   1 
ATOM   4593 C CA  . GLY B 1 306 ? -8.389  8.852  45.671  1.00  37.82 ? 306  GLY B CA  1 
ATOM   4594 C C   . GLY B 1 306 ? -9.674  9.471  46.208  1.00  38.38 ? 306  GLY B C   1 
ATOM   4595 O O   . GLY B 1 306 ? -10.720 8.819  46.246  1.00  38.40 ? 306  GLY B O   1 
ATOM   4596 N N   . GLU B 1 307 ? -9.591  10.730 46.633  1.00  38.90 ? 307  GLU B N   1 
ATOM   4597 C CA  . GLU B 1 307 ? -10.769 11.490 47.038  1.00  39.55 ? 307  GLU B CA  1 
ATOM   4598 C C   . GLU B 1 307 ? -11.387 12.110 45.801  1.00  39.67 ? 307  GLU B C   1 
ATOM   4599 O O   . GLU B 1 307 ? -10.726 12.241 44.772  1.00  39.83 ? 307  GLU B O   1 
ATOM   4600 C CB  . GLU B 1 307 ? -10.407 12.600 48.024  1.00  39.73 ? 307  GLU B CB  1 
ATOM   4601 C CG  . GLU B 1 307 ? -9.793  12.153 49.342  1.00  40.86 ? 307  GLU B CG  1 
ATOM   4602 C CD  . GLU B 1 307 ? -9.171  13.318 50.103  1.00  42.34 ? 307  GLU B CD  1 
ATOM   4603 O OE1 . GLU B 1 307 ? -8.091  13.135 50.702  1.00  42.40 ? 307  GLU B OE1 1 
ATOM   4604 O OE2 . GLU B 1 307 ? -9.752  14.427 50.095  1.00  43.55 ? 307  GLU B OE2 1 
ATOM   4605 N N   . SER B 1 308 ? -12.645 12.520 45.924  1.00  39.85 ? 308  SER B N   1 
ATOM   4606 C CA  . SER B 1 308 ? -13.442 12.955 44.784  1.00  39.95 ? 308  SER B CA  1 
ATOM   4607 C C   . SER B 1 308 ? -13.074 14.363 44.313  1.00  39.96 ? 308  SER B C   1 
ATOM   4608 O O   . SER B 1 308 ? -13.383 15.361 44.970  1.00  40.03 ? 308  SER B O   1 
ATOM   4609 C CB  . SER B 1 308 ? -14.939 12.831 45.107  1.00  40.04 ? 308  SER B CB  1 
ATOM   4610 O OG  . SER B 1 308 ? -15.759 13.175 43.992  1.00  40.36 ? 308  SER B OG  1 
ATOM   4611 N N   . VAL B 1 309 ? -12.397 14.424 43.170  1.00  39.97 ? 309  VAL B N   1 
ATOM   4612 C CA  . VAL B 1 309 ? -12.054 15.685 42.508  1.00  39.95 ? 309  VAL B CA  1 
ATOM   4613 C C   . VAL B 1 309 ? -13.312 16.420 41.970  1.00  40.04 ? 309  VAL B C   1 
ATOM   4614 O O   . VAL B 1 309 ? -13.247 17.605 41.606  1.00  39.91 ? 309  VAL B O   1 
ATOM   4615 C CB  . VAL B 1 309 ? -11.005 15.448 41.384  1.00  39.81 ? 309  VAL B CB  1 
ATOM   4616 C CG1 . VAL B 1 309 ? -10.503 16.757 40.814  1.00  39.70 ? 309  VAL B CG1 1 
ATOM   4617 C CG2 . VAL B 1 309 ? -9.837  14.636 41.912  1.00  39.47 ? 309  VAL B CG2 1 
ATOM   4618 N N   . SER B 1 310 ? -14.449 15.716 41.950  1.00  40.03 ? 310  SER B N   1 
ATOM   4619 C CA  . SER B 1 310 ? -15.732 16.282 41.511  1.00  40.20 ? 310  SER B CA  1 
ATOM   4620 C C   . SER B 1 310 ? -16.186 17.455 42.368  1.00  40.18 ? 310  SER B C   1 
ATOM   4621 O O   . SER B 1 310 ? -16.710 18.446 41.850  1.00  40.17 ? 310  SER B O   1 
ATOM   4622 C CB  . SER B 1 310 ? -16.831 15.218 41.517  1.00  40.19 ? 310  SER B CB  1 
ATOM   4623 O OG  . SER B 1 310 ? -16.436 14.083 40.780  1.00  40.77 ? 310  SER B OG  1 
ATOM   4624 N N   . TYR B 1 311 ? -15.985 17.325 43.677  0.50  40.18 ? 311  TYR B N   1 
ATOM   4625 C CA  . TYR B 1 311 ? -16.405 18.320 44.663  0.50  40.30 ? 311  TYR B CA  1 
ATOM   4626 C C   . TYR B 1 311 ? -15.867 19.736 44.401  0.50  40.44 ? 311  TYR B C   1 
ATOM   4627 O O   . TYR B 1 311 ? -16.190 20.674 45.133  0.50  40.42 ? 311  TYR B O   1 
ATOM   4628 C CB  . TYR B 1 311 ? -16.010 17.838 46.061  0.50  40.26 ? 311  TYR B CB  1 
ATOM   4629 C CG  . TYR B 1 311 ? -15.781 18.942 47.061  0.50  40.31 ? 311  TYR B CG  1 
ATOM   4630 C CD1 . TYR B 1 311 ? -16.673 19.160 48.101  0.50  40.51 ? 311  TYR B CD1 1 
ATOM   4631 C CD2 . TYR B 1 311 ? -14.668 19.766 46.966  0.50  40.26 ? 311  TYR B CD2 1 
ATOM   4632 C CE1 . TYR B 1 311 ? -16.463 20.169 49.020  0.50  40.81 ? 311  TYR B CE1 1 
ATOM   4633 C CE2 . TYR B 1 311 ? -14.448 20.777 47.878  0.50  40.48 ? 311  TYR B CE2 1 
ATOM   4634 C CZ  . TYR B 1 311 ? -15.347 20.975 48.904  0.50  40.92 ? 311  TYR B CZ  1 
ATOM   4635 O OH  . TYR B 1 311 ? -15.134 21.984 49.819  0.50  41.28 ? 311  TYR B OH  1 
ATOM   4636 N N   . LEU B 1 312 ? -15.064 19.875 43.347  1.00  40.73 ? 312  LEU B N   1 
ATOM   4637 C CA  . LEU B 1 312 ? -14.455 21.148 42.961  1.00  41.02 ? 312  LEU B CA  1 
ATOM   4638 C C   . LEU B 1 312 ? -15.105 21.746 41.721  1.00  41.59 ? 312  LEU B C   1 
ATOM   4639 O O   . LEU B 1 312 ? -14.831 22.902 41.370  1.00  41.71 ? 312  LEU B O   1 
ATOM   4640 C CB  . LEU B 1 312 ? -12.977 20.940 42.661  1.00  40.76 ? 312  LEU B CB  1 
ATOM   4641 C CG  . LEU B 1 312 ? -12.069 20.602 43.829  1.00  40.28 ? 312  LEU B CG  1 
ATOM   4642 C CD1 . LEU B 1 312 ? -11.028 19.570 43.403  1.00  39.92 ? 312  LEU B CD1 1 
ATOM   4643 C CD2 . LEU B 1 312 ? -11.422 21.871 44.315  1.00  39.21 ? 312  LEU B CD2 1 
ATOM   4644 N N   . PHE B 1 313 ? -15.939 20.945 41.051  1.00  42.13 ? 313  PHE B N   1 
ATOM   4645 C CA  . PHE B 1 313 ? -16.605 21.354 39.815  1.00  42.68 ? 313  PHE B CA  1 
ATOM   4646 C C   . PHE B 1 313 ? -17.708 22.381 40.057  1.00  43.01 ? 313  PHE B C   1 
ATOM   4647 O O   . PHE B 1 313 ? -18.061 23.143 39.150  1.00  43.17 ? 313  PHE B O   1 
ATOM   4648 C CB  . PHE B 1 313 ? -17.182 20.145 39.066  1.00  42.78 ? 313  PHE B CB  1 
ATOM   4649 C CG  . PHE B 1 313 ? -16.147 19.179 38.552  1.00  43.15 ? 313  PHE B CG  1 
ATOM   4650 C CD1 . PHE B 1 313 ? -14.858 19.607 38.227  1.00  43.90 ? 313  PHE B CD1 1 
ATOM   4651 C CD2 . PHE B 1 313 ? -16.476 17.842 38.355  1.00  43.53 ? 313  PHE B CD2 1 
ATOM   4652 C CE1 . PHE B 1 313 ? -13.902 18.711 37.740  1.00  44.14 ? 313  PHE B CE1 1 
ATOM   4653 C CE2 . PHE B 1 313 ? -15.532 16.936 37.867  1.00  44.19 ? 313  PHE B CE2 1 
ATOM   4654 C CZ  . PHE B 1 313 ? -14.239 17.374 37.560  1.00  44.43 ? 313  PHE B CZ  1 
ATOM   4655 N N   . SER B 1 314 ? -18.253 22.386 41.274  0.50  43.42 ? 314  SER B N   1 
ATOM   4656 C CA  . SER B 1 314 ? -19.267 23.359 41.679  0.50  43.84 ? 314  SER B CA  1 
ATOM   4657 C C   . SER B 1 314 ? -19.090 23.763 43.138  0.50  44.19 ? 314  SER B C   1 
ATOM   4658 O O   . SER B 1 314 ? -20.067 24.044 43.834  0.50  44.24 ? 314  SER B O   1 
ATOM   4659 C CB  . SER B 1 314 ? -20.682 22.824 41.438  0.50  43.75 ? 314  SER B CB  1 
ATOM   4660 O OG  . SER B 1 314 ? -20.909 21.624 42.161  0.50  43.70 ? 314  SER B OG  1 
ATOM   4661 N N   . HIS B 1 315 ? -17.842 23.771 43.597  0.50  44.64 ? 315  HIS B N   1 
ATOM   4662 C CA  . HIS B 1 315 ? -17.509 24.284 44.922  0.50  45.17 ? 315  HIS B CA  1 
ATOM   4663 C C   . HIS B 1 315 ? -16.093 24.862 44.910  0.50  45.35 ? 315  HIS B C   1 
ATOM   4664 O O   . HIS B 1 315 ? -15.201 24.329 44.246  0.50  45.41 ? 315  HIS B O   1 
ATOM   4665 C CB  . HIS B 1 315 ? -17.637 23.192 45.990  0.50  45.29 ? 315  HIS B CB  1 
ATOM   4666 C CG  . HIS B 1 315 ? -17.714 23.721 47.393  0.50  46.06 ? 315  HIS B CG  1 
ATOM   4667 N ND1 . HIS B 1 315 ? -17.160 24.928 47.764  0.50  46.51 ? 315  HIS B ND1 1 
ATOM   4668 C CD2 . HIS B 1 315 ? -18.261 23.199 48.518  0.50  46.43 ? 315  HIS B CD2 1 
ATOM   4669 C CE1 . HIS B 1 315 ? -17.375 25.134 49.051  0.50  46.50 ? 315  HIS B CE1 1 
ATOM   4670 N NE2 . HIS B 1 315 ? -18.038 24.098 49.534  0.50  46.40 ? 315  HIS B NE2 1 
ATOM   4671 N N   . VAL B 1 316 ? -15.906 25.962 45.637  1.00  45.65 ? 316  VAL B N   1 
ATOM   4672 C CA  . VAL B 1 316 ? -14.619 26.665 45.721  1.00  45.88 ? 316  VAL B CA  1 
ATOM   4673 C C   . VAL B 1 316 ? -13.892 26.337 47.031  1.00  45.95 ? 316  VAL B C   1 
ATOM   4674 O O   . VAL B 1 316 ? -14.300 26.810 48.100  1.00  46.12 ? 316  VAL B O   1 
ATOM   4675 C CB  . VAL B 1 316 ? -14.799 28.205 45.633  1.00  45.83 ? 316  VAL B CB  1 
ATOM   4676 C CG1 . VAL B 1 316 ? -13.447 28.897 45.560  1.00  45.70 ? 316  VAL B CG1 1 
ATOM   4677 C CG2 . VAL B 1 316 ? -15.677 28.588 44.441  1.00  46.09 ? 316  VAL B CG2 1 
ATOM   4678 N N   . PRO B 1 317 ? -12.797 25.549 46.950  0.80  45.89 ? 317  PRO B N   1 
ATOM   4679 C CA  . PRO B 1 317 ? -12.088 25.048 48.130  0.80  45.74 ? 317  PRO B CA  1 
ATOM   4680 C C   . PRO B 1 317 ? -11.492 26.159 48.976  0.80  45.63 ? 317  PRO B C   1 
ATOM   4681 O O   . PRO B 1 317 ? -11.853 26.276 50.146  0.80  45.60 ? 317  PRO B O   1 
ATOM   4682 C CB  . PRO B 1 317 ? -10.968 24.201 47.527  0.80  45.62 ? 317  PRO B CB  1 
ATOM   4683 C CG  . PRO B 1 317 ? -10.708 24.824 46.226  0.80  45.65 ? 317  PRO B CG  1 
ATOM   4684 C CD  . PRO B 1 317 ? -12.061 25.230 45.715  0.80  45.85 ? 317  PRO B CD  1 
HETATM 4685 S S   . SO4 C 2 .   ? 18.771  -0.182 -0.490  1.00  30.64 ? 1001 SO4 A S   1 
HETATM 4686 O O1  . SO4 C 2 .   ? 18.435  -1.334 0.323   1.00  30.50 ? 1001 SO4 A O1  1 
HETATM 4687 O O2  . SO4 C 2 .   ? 19.014  0.971  0.374   1.00  30.74 ? 1001 SO4 A O2  1 
HETATM 4688 O O3  . SO4 C 2 .   ? 19.979  -0.486 -1.246  1.00  30.80 ? 1001 SO4 A O3  1 
HETATM 4689 O O4  . SO4 C 2 .   ? 17.656  0.079  -1.395  1.00  30.69 ? 1001 SO4 A O4  1 
HETATM 4690 S S   . SO4 D 2 .   ? 30.464  22.814 20.964  0.20  34.87 ? 1002 SO4 A S   1 
HETATM 4691 O O1  . SO4 D 2 .   ? 30.352  21.367 20.785  0.20  35.06 ? 1002 SO4 A O1  1 
HETATM 4692 O O2  . SO4 D 2 .   ? 31.599  23.106 21.838  0.20  34.96 ? 1002 SO4 A O2  1 
HETATM 4693 O O3  . SO4 D 2 .   ? 30.671  23.447 19.662  0.20  35.08 ? 1002 SO4 A O3  1 
HETATM 4694 O O4  . SO4 D 2 .   ? 29.236  23.323 21.569  0.20  34.92 ? 1002 SO4 A O4  1 
HETATM 4695 S S   . SO4 E 2 .   ? 24.212  2.837  10.445  0.30  13.35 ? 1003 SO4 A S   1 
HETATM 4696 O O1  . SO4 E 2 .   ? 23.068  2.461  11.275  0.30  12.70 ? 1003 SO4 A O1  1 
HETATM 4697 O O2  . SO4 E 2 .   ? 25.448  2.291  11.003  0.30  13.37 ? 1003 SO4 A O2  1 
HETATM 4698 O O3  . SO4 E 2 .   ? 24.047  2.289  9.102   0.30  13.56 ? 1003 SO4 A O3  1 
HETATM 4699 O O4  . SO4 E 2 .   ? 24.296  4.295  10.362  0.30  12.97 ? 1003 SO4 A O4  1 
HETATM 4700 S S   . SO4 F 2 .   ? -14.440 11.871 41.366  1.00  23.90 ? 401  SO4 B S   1 
HETATM 4701 O O1  . SO4 F 2 .   ? -14.043 10.636 42.046  1.00  24.36 ? 401  SO4 B O1  1 
HETATM 4702 O O2  . SO4 F 2 .   ? -15.862 12.093 41.605  1.00  23.58 ? 401  SO4 B O2  1 
HETATM 4703 O O3  . SO4 F 2 .   ? -13.663 12.998 41.843  1.00  23.43 ? 401  SO4 B O3  1 
HETATM 4704 O O4  . SO4 F 2 .   ? -14.211 11.761 39.929  1.00  24.33 ? 401  SO4 B O4  1 
HETATM 4705 S S   . SO4 G 2 .   ? -9.406  37.343 20.774  1.00  81.05 ? 402  SO4 B S   1 
HETATM 4706 O O1  . SO4 G 2 .   ? -8.329  36.794 19.956  1.00  81.07 ? 402  SO4 B O1  1 
HETATM 4707 O O2  . SO4 G 2 .   ? -8.883  37.740 22.077  1.00  81.45 ? 402  SO4 B O2  1 
HETATM 4708 O O3  . SO4 G 2 .   ? -9.956  38.510 20.099  1.00  81.26 ? 402  SO4 B O3  1 
HETATM 4709 O O4  . SO4 G 2 .   ? -10.451 36.341 20.966  1.00  80.87 ? 402  SO4 B O4  1 
HETATM 4710 S S   . SO4 H 2 .   ? -16.749 18.152 30.687  0.53  9.10  ? 403  SO4 B S   1 
HETATM 4711 O O1  . SO4 H 2 .   ? -15.328 17.851 30.871  0.53  9.96  ? 403  SO4 B O1  1 
HETATM 4712 O O2  . SO4 H 2 .   ? -17.507 17.778 31.886  0.53  8.55  ? 403  SO4 B O2  1 
HETATM 4713 O O3  . SO4 H 2 .   ? -16.921 19.574 30.398  0.53  8.33  ? 403  SO4 B O3  1 
HETATM 4714 O O4  . SO4 H 2 .   ? -17.233 17.383 29.545  0.53  8.95  ? 403  SO4 B O4  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  THR 87  87  87  THR THR 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 ?   ?   ?   A . n 
A 1 197 LYS 197 197 ?   ?   ?   A . n 
A 1 198 LYS 198 198 ?   ?   ?   A . n 
A 1 199 ALA 199 199 ?   ?   ?   A . n 
A 1 200 ASN 200 200 ?   ?   ?   A . n 
A 1 201 GLU 201 201 ?   ?   ?   A . n 
A 1 202 VAL 202 202 ?   ?   ?   A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 MET 205 205 205 MET MET A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 MET 222 222 222 MET MET A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 CYS 226 226 226 CYS CYS A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 CYS 230 230 230 CYS CYS A . n 
A 1 231 HIS 231 231 231 HIS HIS A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 VAL 271 271 271 VAL VAL A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 PRO 276 276 276 PRO PRO A . n 
A 1 277 GLN 277 277 277 GLN GLN A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 MET 281 281 281 MET MET A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 CYS 284 284 284 CYS CYS A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 LYS 286 286 286 LYS LYS A . n 
A 1 287 ILE 287 287 287 ILE ILE A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 MET 294 294 294 MET MET A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 ILE 300 300 300 ILE ILE A . n 
A 1 301 ARG 301 301 301 ARG ARG A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 ASN 305 305 305 ASN ASN A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 PHE 313 313 313 PHE PHE A . n 
A 1 314 SER 314 314 ?   ?   ?   A . n 
A 1 315 HIS 315 315 ?   ?   ?   A . n 
A 1 316 VAL 316 316 ?   ?   ?   A . n 
A 1 317 PRO 317 317 ?   ?   ?   A . n 
A 1 318 LEU 318 318 ?   ?   ?   A . n 
A 1 319 LEU 319 319 ?   ?   ?   A . n 
A 1 320 GLU 320 320 ?   ?   ?   A . n 
A 1 321 HIS 321 321 ?   ?   ?   A . n 
A 1 322 HIS 322 322 ?   ?   ?   A . n 
A 1 323 HIS 323 323 ?   ?   ?   A . n 
A 1 324 HIS 324 324 ?   ?   ?   A . n 
A 1 325 HIS 325 325 ?   ?   ?   A . n 
A 1 326 HIS 326 326 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   ASN 3   3   3   ASN ASN B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  SER 11  11  11  SER SER B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  GLN 13  13  13  GLN GLN B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  GLN 17  17  17  GLN GLN B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  LYS 33  33  33  LYS LYS B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  PHE 35  35  35  PHE PHE B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  CYS 41  41  41  CYS CYS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  CYS 60  60  60  CYS CYS B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  MET 68  68  68  MET MET B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ILE 72  72  72  ILE ILE B . n 
B 1 73  MET 73  73  73  MET MET B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  CYS 77  77  77  CYS CYS B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  PRO 90  90  90  PRO PRO B . n 
B 1 91  CYS 91  91  91  CYS CYS B . n 
B 1 92  PHE 92  92  92  PHE PHE B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  GLN 97  97  97  GLN GLN B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ASN 114 114 114 ASN ASN B . n 
B 1 115 MET 115 115 115 MET MET B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 HIS 123 123 123 HIS HIS B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 THR 126 126 126 THR THR B . n 
B 1 127 MET 127 127 127 MET MET B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 HIS 130 130 130 HIS HIS B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 SER 132 132 132 SER SER B . n 
B 1 133 GLN 133 133 133 GLN GLN B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 PHE 137 137 137 PHE PHE B . n 
B 1 138 PHE 138 138 138 PHE PHE B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 ILE 140 140 140 ILE ILE B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 TYR 146 146 146 TYR TYR B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 TRP 154 154 154 TRP TRP B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 GLU 157 157 157 GLU GLU B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 ILE 159 159 159 ILE ILE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 TRP 162 162 162 TRP TRP B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 ASN 164 164 164 ASN ASN B . n 
B 1 165 CYS 165 165 165 CYS CYS B . n 
B 1 166 THR 166 166 166 THR THR B . n 
B 1 167 ILE 167 167 167 ILE ILE B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 ASP 171 171 171 ASP ASP B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 LYS 176 176 176 LYS LYS B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 SER 180 180 180 SER SER B . n 
B 1 181 ILE 181 181 181 ILE ILE B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 ASP 183 183 183 ASP ASP B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 PHE 189 189 189 PHE PHE B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 HIS 193 193 193 HIS HIS B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 ARG 196 196 ?   ?   ?   B . n 
B 1 197 LYS 197 197 ?   ?   ?   B . n 
B 1 198 LYS 198 198 ?   ?   ?   B . n 
B 1 199 ALA 199 199 ?   ?   ?   B . n 
B 1 200 ASN 200 200 ?   ?   ?   B . n 
B 1 201 GLU 201 201 ?   ?   ?   B . n 
B 1 202 VAL 202 202 ?   ?   ?   B . n 
B 1 203 ASP 203 203 203 ASP ASP B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 MET 205 205 205 MET MET B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 VAL 208 208 208 VAL VAL B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 ASP 210 210 210 ASP ASP B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 ASP 213 213 213 ASP ASP B . n 
B 1 214 ARG 214 214 214 ARG ARG B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 ALA 216 216 216 ALA ALA B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 VAL 219 219 219 VAL VAL B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 MET 222 222 222 MET MET B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 ASP 224 224 224 ASP ASP B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 CYS 226 226 226 CYS CYS B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 THR 228 228 228 THR THR B . n 
B 1 229 ILE 229 229 229 ILE ILE B . n 
B 1 230 CYS 230 230 230 CYS CYS B . n 
B 1 231 HIS 231 231 231 HIS HIS B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 ASP 234 234 234 ASP ASP B . n 
B 1 235 LYS 235 235 235 LYS LYS B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 ALA 239 239 239 ALA ALA B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 ARG 243 243 243 ARG ARG B . n 
B 1 244 VAL 244 244 244 VAL VAL B . n 
B 1 245 TYR 245 245 245 TYR TYR B . n 
B 1 246 ALA 246 246 246 ALA ALA B . n 
B 1 247 ILE 247 247 247 ILE ILE B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 THR 249 249 249 THR THR B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 ILE 252 252 252 ILE ILE B . n 
B 1 253 PHE 253 253 253 PHE PHE B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 PRO 256 256 256 PRO PRO B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 SER 259 259 259 SER SER B . n 
B 1 260 ARG 260 260 260 ARG ARG B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 ASN 262 262 262 ASN ASN B . n 
B 1 263 ASN 263 263 263 ASN ASN B . n 
B 1 264 ALA 264 264 264 ALA ALA B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 PHE 266 266 266 PHE PHE B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 ALA 268 268 268 ALA ALA B . n 
B 1 269 VAL 269 269 269 VAL VAL B . n 
B 1 270 VAL 270 270 270 VAL VAL B . n 
B 1 271 VAL 271 271 271 VAL VAL B . n 
B 1 272 THR 272 272 272 THR THR B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 THR 274 274 274 THR THR B . n 
B 1 275 ILE 275 275 275 ILE ILE B . n 
B 1 276 PRO 276 276 276 PRO PRO B . n 
B 1 277 GLN 277 277 277 GLN GLN B . n 
B 1 278 GLU 278 278 278 GLU GLU B . n 
B 1 279 ASP 279 279 279 ASP ASP B . n 
B 1 280 LYS 280 280 280 LYS LYS B . n 
B 1 281 MET 281 281 281 MET MET B . n 
B 1 282 LYS 282 282 282 LYS LYS B . n 
B 1 283 HIS 283 283 283 HIS HIS B . n 
B 1 284 CYS 284 284 284 CYS CYS B . n 
B 1 285 SER 285 285 285 SER SER B . n 
B 1 286 LYS 286 286 286 LYS LYS B . n 
B 1 287 ILE 287 287 287 ILE ILE B . n 
B 1 288 GLN 288 288 288 GLN GLN B . n 
B 1 289 VAL 289 289 289 VAL VAL B . n 
B 1 290 ILE 290 290 290 ILE ILE B . n 
B 1 291 ASP 291 291 291 ASP ASP B . n 
B 1 292 ILE 292 292 292 ILE ILE B . n 
B 1 293 SER 293 293 293 SER SER B . n 
B 1 294 MET 294 294 294 MET MET B . n 
B 1 295 ILE 295 295 295 ILE ILE B . n 
B 1 296 LEU 296 296 296 LEU LEU B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 GLU 298 298 298 GLU GLU B . n 
B 1 299 ALA 299 299 299 ALA ALA B . n 
B 1 300 ILE 300 300 300 ILE ILE B . n 
B 1 301 ARG 301 301 301 ARG ARG B . n 
B 1 302 ARG 302 302 302 ARG ARG B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 HIS 304 304 304 HIS HIS B . n 
B 1 305 ASN 305 305 305 ASN ASN B . n 
B 1 306 GLY 306 306 306 GLY GLY B . n 
B 1 307 GLU 307 307 307 GLU GLU B . n 
B 1 308 SER 308 308 308 SER SER B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 SER 310 310 310 SER SER B . n 
B 1 311 TYR 311 311 311 TYR TYR B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 PHE 313 313 313 PHE PHE B . n 
B 1 314 SER 314 314 314 SER SER B . n 
B 1 315 HIS 315 315 315 HIS HIS B . n 
B 1 316 VAL 316 316 316 VAL VAL B . n 
B 1 317 PRO 317 317 317 PRO PRO B . n 
B 1 318 LEU 318 318 ?   ?   ?   B . n 
B 1 319 LEU 319 319 ?   ?   ?   B . n 
B 1 320 GLU 320 320 ?   ?   ?   B . n 
B 1 321 HIS 321 321 ?   ?   ?   B . n 
B 1 322 HIS 322 322 ?   ?   ?   B . n 
B 1 323 HIS 323 323 ?   ?   ?   B . n 
B 1 324 HIS 324 324 ?   ?   ?   B . n 
B 1 325 HIS 325 325 ?   ?   ?   B . n 
B 1 326 HIS 326 326 ?   ?   ?   B . n 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 28890 ? 
1 MORE         -431  ? 
1 'SSA (A^2)'  60180 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -y,x-y,z  -0.5000000000 -0.8660254038 0.0000000000 0.0000000000 0.8660254038  -0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_555 -x+y,-x,z -0.5000000000 0.8660254038  0.0000000000 0.0000000000 -0.8660254038 -0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-02-04 
2 'Structure model' 1 1 2015-03-25 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .        ? 1 
MOLREP   phasing           .        ? 2 
REFMAC   refinement        5.5.0109 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             SER 
_pdbx_validate_rmsd_angle.auth_seq_id_1              11 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             SER 
_pdbx_validate_rmsd_angle.auth_seq_id_2              11 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             SER 
_pdbx_validate_rmsd_angle.auth_seq_id_3              11 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                81.36 
_pdbx_validate_rmsd_angle.angle_target_value         111.00 
_pdbx_validate_rmsd_angle.angle_deviation            -29.64 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.70 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 8   ? ? -104.84 -168.03 
2  1 SER A 11  ? ? -139.47 -158.45 
3  1 GLN A 38  ? ? 71.04   -0.87   
4  1 ARG A 84  ? ? -173.71 144.47  
5  1 LYS A 102 ? ? 71.62   -0.22   
6  1 ASP A 128 ? ? 34.90   62.87   
7  1 ILE A 134 ? ? -64.68  63.22   
8  1 GLN A 135 ? ? -140.08 -24.40  
9  1 ALA A 232 ? ? -39.91  -37.47  
10 1 SER B 10  ? ? 60.00   -140.84 
11 1 HIS B 12  ? ? -69.34  80.05   
12 1 GLN B 38  ? ? 86.45   14.60   
13 1 GLU B 46  ? ? -174.78 127.62  
14 1 SER B 47  ? ? -37.69  119.66  
15 1 ARG B 49  ? ? -55.25  106.34  
16 1 GLN B 97  ? ? -109.77 61.43   
17 1 LYS B 102 ? ? 52.31   14.20   
18 1 ASP B 128 ? ? 44.16   73.04   
19 1 ASN B 164 ? ? -147.35 29.81   
20 1 ASP B 224 ? ? -109.03 -78.54  
21 1 ASN B 273 ? ? -94.01  45.80   
22 1 TYR B 311 ? ? -55.28  -1.89   
23 1 SER B 314 ? ? -143.64 31.95   
# 
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 ARG 196 ? A ARG 196 
4  1 Y 1 A LYS 197 ? A LYS 197 
5  1 Y 1 A LYS 198 ? A LYS 198 
6  1 Y 1 A ALA 199 ? A ALA 199 
7  1 Y 1 A ASN 200 ? A ASN 200 
8  1 Y 1 A GLU 201 ? A GLU 201 
9  1 Y 1 A VAL 202 ? A VAL 202 
10 1 Y 1 A SER 314 ? A SER 314 
11 1 Y 1 A HIS 315 ? A HIS 315 
12 1 Y 1 A VAL 316 ? A VAL 316 
13 1 Y 1 A PRO 317 ? A PRO 317 
14 1 Y 1 A LEU 318 ? A LEU 318 
15 1 Y 1 A LEU 319 ? A LEU 319 
16 1 Y 1 A GLU 320 ? A GLU 320 
17 1 Y 1 A HIS 321 ? A HIS 321 
18 1 Y 1 A HIS 322 ? A HIS 322 
19 1 Y 1 A HIS 323 ? A HIS 323 
20 1 Y 1 A HIS 324 ? A HIS 324 
21 1 Y 1 A HIS 325 ? A HIS 325 
22 1 Y 1 A HIS 326 ? A HIS 326 
23 1 Y 1 B MET 1   ? B MET 1   
24 1 Y 1 B PRO 2   ? B PRO 2   
25 1 Y 1 B ARG 196 ? B ARG 196 
26 1 Y 1 B LYS 197 ? B LYS 197 
27 1 Y 1 B LYS 198 ? B LYS 198 
28 1 Y 1 B ALA 199 ? B ALA 199 
29 1 Y 1 B ASN 200 ? B ASN 200 
30 1 Y 1 B GLU 201 ? B GLU 201 
31 1 Y 1 B VAL 202 ? B VAL 202 
32 1 Y 1 B LEU 318 ? B LEU 318 
33 1 Y 1 B LEU 319 ? B LEU 319 
34 1 Y 1 B GLU 320 ? B GLU 320 
35 1 Y 1 B HIS 321 ? B HIS 321 
36 1 Y 1 B HIS 322 ? B HIS 322 
37 1 Y 1 B HIS 323 ? B HIS 323 
38 1 Y 1 B HIS 324 ? B HIS 324 
39 1 Y 1 B HIS 325 ? B HIS 325 
40 1 Y 1 B HIS 326 ? B HIS 326 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'SULFATE ION' 
_pdbx_entity_nonpoly.comp_id     SO4 
# 
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 1001 1001 SO4 SO4 A . 
D 2 SO4 1 1002 1004 SO4 SO4 A . 
E 2 SO4 1 1003 1006 SO4 SO4 A . 
F 2 SO4 1 401  1002 SO4 SO4 B . 
G 2 SO4 1 402  1003 SO4 SO4 B . 
H 2 SO4 1 403  1005 SO4 SO4 B . 
# 
