data_4F8E
# 
_entry.id   4F8E 
# 
_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   4F8E         
RCSB  RCSB072584   
WWPDB D_1000072584 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4F8E 
_pdbx_database_status.recvd_initial_deposition_date   2012-05-17 
_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                     
'A small disturbance, but a serious disease: the possible mechanism of D52H-mutant of human PRS1 that causes gout' 
_citation.journal_abbrev            'Iubmb Life' 
_citation.journal_volume            65 
_citation.page_first                518 
_citation.page_last                 525 
_citation.year                      2013 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           1521-6543 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23509005 
_citation.pdbx_database_id_DOI      10.1002/iub.1154 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Chen, P.' 1 
primary 'Li, J.'   2 
primary 'Ma, J.'   3 
primary 'Teng, M.' 4 
primary 'Li, X.'   5 
# 
_cell.entry_id           4F8E 
_cell.length_a           170.31 
_cell.length_b           170.31 
_cell.length_c           61.75 
_cell.angle_alpha        90 
_cell.angle_beta         90 
_cell.angle_gamma        120 
_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                         4F8E 
_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' 35973.434 2  2.7.6.1 D52H ? ? 
2 non-polymer syn 'SULFATE ION'                          96.063    6  ?       ?    ? ? 
3 non-polymer syn 'MAGNESIUM ION'                        24.305    2  ?       ?    ? ? 
4 water       nat water                                  18.015    73 ?       ?    ? ? 
# 
_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       
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEHVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEHVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   ASN n 
1 4   ILE n 
1 5   LYS n 
1 6   ILE n 
1 7   PHE n 
1 8   SER n 
1 9   GLY n 
1 10  SER n 
1 11  SER n 
1 12  HIS n 
1 13  GLN n 
1 14  ASP n 
1 15  LEU n 
1 16  SER n 
1 17  GLN n 
1 18  LYS n 
1 19  ILE n 
1 20  ALA n 
1 21  ASP n 
1 22  ARG n 
1 23  LEU n 
1 24  GLY n 
1 25  LEU n 
1 26  GLU n 
1 27  LEU n 
1 28  GLY n 
1 29  LYS n 
1 30  VAL n 
1 31  VAL n 
1 32  THR n 
1 33  LYS n 
1 34  LYS n 
1 35  PHE n 
1 36  SER n 
1 37  ASN n 
1 38  GLN n 
1 39  GLU n 
1 40  THR n 
1 41  CYS n 
1 42  VAL n 
1 43  GLU n 
1 44  ILE n 
1 45  GLY n 
1 46  GLU n 
1 47  SER n 
1 48  VAL n 
1 49  ARG n 
1 50  GLY n 
1 51  GLU n 
1 52  HIS n 
1 53  VAL n 
1 54  TYR n 
1 55  ILE n 
1 56  VAL n 
1 57  GLN n 
1 58  SER n 
1 59  GLY n 
1 60  CYS n 
1 61  GLY n 
1 62  GLU n 
1 63  ILE n 
1 64  ASN n 
1 65  ASP n 
1 66  ASN n 
1 67  LEU n 
1 68  MET n 
1 69  GLU n 
1 70  LEU n 
1 71  LEU n 
1 72  ILE n 
1 73  MET n 
1 74  ILE n 
1 75  ASN n 
1 76  ALA n 
1 77  CYS n 
1 78  LYS n 
1 79  ILE n 
1 80  ALA n 
1 81  SER n 
1 82  ALA n 
1 83  SER n 
1 84  ARG n 
1 85  VAL n 
1 86  THR n 
1 87  ALA n 
1 88  VAL n 
1 89  ILE n 
1 90  PRO n 
1 91  CYS n 
1 92  PHE n 
1 93  PRO n 
1 94  TYR n 
1 95  ALA n 
1 96  ARG n 
1 97  GLN n 
1 98  ASP n 
1 99  LYS n 
1 100 LYS n 
1 101 ASP n 
1 102 LYS n 
1 103 SER n 
1 104 ARG n 
1 105 ALA n 
1 106 PRO n 
1 107 ILE n 
1 108 SER n 
1 109 ALA n 
1 110 LYS n 
1 111 LEU n 
1 112 VAL n 
1 113 ALA n 
1 114 ASN n 
1 115 MET n 
1 116 LEU n 
1 117 SER n 
1 118 VAL n 
1 119 ALA n 
1 120 GLY n 
1 121 ALA n 
1 122 ASP n 
1 123 HIS n 
1 124 ILE n 
1 125 ILE n 
1 126 THR n 
1 127 MET n 
1 128 ASP n 
1 129 LEU n 
1 130 HIS n 
1 131 ALA n 
1 132 SER n 
1 133 GLN n 
1 134 ILE n 
1 135 GLN n 
1 136 GLY n 
1 137 PHE n 
1 138 PHE n 
1 139 ASP n 
1 140 ILE n 
1 141 PRO n 
1 142 VAL n 
1 143 ASP n 
1 144 ASN n 
1 145 LEU n 
1 146 TYR n 
1 147 ALA n 
1 148 GLU n 
1 149 PRO n 
1 150 ALA n 
1 151 VAL n 
1 152 LEU n 
1 153 LYS n 
1 154 TRP n 
1 155 ILE n 
1 156 ARG n 
1 157 GLU n 
1 158 ASN n 
1 159 ILE n 
1 160 SER n 
1 161 GLU n 
1 162 TRP n 
1 163 ARG n 
1 164 ASN n 
1 165 CYS n 
1 166 THR n 
1 167 ILE n 
1 168 VAL n 
1 169 SER n 
1 170 PRO n 
1 171 ASP n 
1 172 ALA n 
1 173 GLY n 
1 174 GLY n 
1 175 ALA n 
1 176 LYS n 
1 177 ARG n 
1 178 VAL n 
1 179 THR n 
1 180 SER n 
1 181 ILE n 
1 182 ALA n 
1 183 ASP n 
1 184 ARG n 
1 185 LEU n 
1 186 ASN n 
1 187 VAL n 
1 188 ASP n 
1 189 PHE n 
1 190 ALA n 
1 191 LEU n 
1 192 ILE n 
1 193 HIS n 
1 194 LYS n 
1 195 GLU n 
1 196 ARG n 
1 197 LYS n 
1 198 LYS n 
1 199 ALA n 
1 200 ASN n 
1 201 GLU n 
1 202 VAL n 
1 203 ASP n 
1 204 ARG n 
1 205 MET n 
1 206 VAL n 
1 207 LEU n 
1 208 VAL n 
1 209 GLY n 
1 210 ASP n 
1 211 VAL n 
1 212 LYS n 
1 213 ASP n 
1 214 ARG n 
1 215 VAL n 
1 216 ALA n 
1 217 ILE n 
1 218 LEU n 
1 219 VAL n 
1 220 ASP n 
1 221 ASP n 
1 222 MET n 
1 223 ALA n 
1 224 ASP n 
1 225 THR n 
1 226 CYS n 
1 227 GLY n 
1 228 THR n 
1 229 ILE n 
1 230 CYS n 
1 231 HIS n 
1 232 ALA n 
1 233 ALA n 
1 234 ASP n 
1 235 LYS n 
1 236 LEU n 
1 237 LEU n 
1 238 SER n 
1 239 ALA n 
1 240 GLY n 
1 241 ALA n 
1 242 THR n 
1 243 ARG n 
1 244 VAL n 
1 245 TYR n 
1 246 ALA n 
1 247 ILE n 
1 248 LEU n 
1 249 THR n 
1 250 HIS n 
1 251 GLY n 
1 252 ILE n 
1 253 PHE n 
1 254 SER n 
1 255 GLY n 
1 256 PRO n 
1 257 ALA n 
1 258 ILE n 
1 259 SER n 
1 260 ARG n 
1 261 ILE n 
1 262 ASN n 
1 263 ASN n 
1 264 ALA n 
1 265 CYS n 
1 266 PHE n 
1 267 GLU n 
1 268 ALA n 
1 269 VAL n 
1 270 VAL n 
1 271 VAL n 
1 272 THR n 
1 273 ASN n 
1 274 THR n 
1 275 ILE n 
1 276 PRO n 
1 277 GLN n 
1 278 GLU n 
1 279 ASP n 
1 280 LYS n 
1 281 MET n 
1 282 LYS n 
1 283 HIS n 
1 284 CYS n 
1 285 SER n 
1 286 LYS n 
1 287 ILE n 
1 288 GLN n 
1 289 VAL n 
1 290 ILE n 
1 291 ASP n 
1 292 ILE n 
1 293 SER n 
1 294 MET n 
1 295 ILE n 
1 296 LEU n 
1 297 ALA n 
1 298 GLU n 
1 299 ALA n 
1 300 ILE n 
1 301 ARG n 
1 302 ARG n 
1 303 THR n 
1 304 HIS n 
1 305 ASN n 
1 306 GLY n 
1 307 GLU n 
1 308 SER n 
1 309 VAL n 
1 310 SER n 
1 311 TYR n 
1 312 LEU n 
1 313 PHE n 
1 314 SER n 
1 315 HIS n 
1 316 VAL n 
1 317 PRO n 
1 318 LEU n 
1 319 LEU n 
1 320 GLU n 
1 321 HIS n 
1 322 HIS n 
1 323 HIS n 
1 324 HIS n 
1 325 HIS n 
1 326 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PRPS1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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 4F8E A 1 ? 318 ? P60891 1 ? 318 ? 1 318 
2 1 4F8E 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 4F8E HIS A 52  ? UNP P60891 ASP 52 'ENGINEERED MUTATION' 52  1  
1 4F8E LEU A 319 ? UNP P60891 ?   ?  'EXPRESSION TAG'      319 2  
1 4F8E GLU A 320 ? UNP P60891 ?   ?  'EXPRESSION TAG'      320 3  
1 4F8E HIS A 321 ? UNP P60891 ?   ?  'EXPRESSION TAG'      321 4  
1 4F8E HIS A 322 ? UNP P60891 ?   ?  'EXPRESSION TAG'      322 5  
1 4F8E HIS A 323 ? UNP P60891 ?   ?  'EXPRESSION TAG'      323 6  
1 4F8E HIS A 324 ? UNP P60891 ?   ?  'EXPRESSION TAG'      324 7  
1 4F8E HIS A 325 ? UNP P60891 ?   ?  'EXPRESSION TAG'      325 8  
1 4F8E HIS A 326 ? UNP P60891 ?   ?  'EXPRESSION TAG'      326 9  
2 4F8E HIS B 52  ? UNP P60891 ASP 52 'ENGINEERED MUTATION' 52  10 
2 4F8E LEU B 319 ? UNP P60891 ?   ?  'EXPRESSION TAG'      319 11 
2 4F8E GLU B 320 ? UNP P60891 ?   ?  'EXPRESSION TAG'      320 12 
2 4F8E HIS B 321 ? UNP P60891 ?   ?  'EXPRESSION TAG'      321 13 
2 4F8E HIS B 322 ? UNP P60891 ?   ?  'EXPRESSION TAG'      322 14 
2 4F8E HIS B 323 ? UNP P60891 ?   ?  'EXPRESSION TAG'      323 15 
2 4F8E HIS B 324 ? UNP P60891 ?   ?  'EXPRESSION TAG'      324 16 
2 4F8E HIS B 325 ? UNP P60891 ?   ?  'EXPRESSION TAG'      325 17 
2 4F8E HIS B 326 ? UNP P60891 ?   ?  'EXPRESSION TAG'      326 18 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
MG  non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'           24.305  
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          4F8E 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.40 
_exptl_crystal.density_percent_sol   48.65 
_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                   'RAYONIX MX-325' 
_diffrn_detector.pdbx_collection_date   2010-06-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_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        1.0 
# 
_reflns.entry_id                     4F8E 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            2.27 
_reflns.number_obs                   30931 
_reflns.number_all                   30957 
_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                  2.27 
_reflns_shell.d_res_low                   ? 
_reflns_shell.percent_possible_all        99.9 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.pdbx_redundancy             ? 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_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                                 4F8E 
_refine.ls_number_reflns_obs                     30931 
_refine.ls_number_reflns_all                     30957 
_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                             50 
_refine.ls_d_res_high                            2.27 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.178 
_refine.ls_R_factor_R_free                       0.2325 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_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        4608 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_refine_hist.number_atoms_solvent             73 
_refine_hist.number_atoms_total               4713 
_refine_hist.d_res_high                       2.27 
_refine_hist.d_res_low                        50 
# 
_struct.entry_id                  4F8E 
_struct.title                     'Crystal structure of human PRS1 D52H 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        4F8E 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'PRPP synthesis, 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 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
# 
_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  GLN A 13  ? GLY A 24  ? GLN A 13  GLY A 24  1 ? 12 
HELX_P HELX_P2  2  GLU A 62  ? ILE A 79  ? GLU A 62  ILE A 79  1 ? 18 
HELX_P HELX_P3  3  ILE A 107 ? GLY A 120 ? ILE A 107 GLY A 120 1 ? 14 
HELX_P HELX_P4  4  ALA A 131 ? PHE A 138 ? ALA A 131 PHE A 138 5 ? 8  
HELX_P HELX_P5  5  ALA A 147 ? GLU A 157 ? ALA A 147 GLU A 157 1 ? 11 
HELX_P HELX_P6  6  ILE A 159 ? ASN A 164 ? ILE A 159 ASN A 164 5 ? 6  
HELX_P HELX_P7  7  ASP A 171 ? GLY A 173 ? ASP A 171 GLY A 173 5 ? 3  
HELX_P HELX_P8  8  GLY A 174 ? ASN A 186 ? GLY A 174 ASN A 186 1 ? 13 
HELX_P HELX_P9  9  CYS A 226 ? ALA A 239 ? CYS A 226 ALA A 239 1 ? 14 
HELX_P HELX_P10 10 PRO A 256 ? ASN A 263 ? PRO A 256 ASN A 263 1 ? 8  
HELX_P HELX_P11 11 GLN A 277 ? HIS A 283 ? GLN A 277 HIS A 283 1 ? 7  
HELX_P HELX_P12 12 ILE A 292 ? GLY A 306 ? ILE A 292 GLY A 306 1 ? 15 
HELX_P HELX_P13 13 SER A 308 ? SER A 314 ? SER A 308 SER A 314 5 ? 7  
HELX_P HELX_P14 14 LEU B 15  ? LEU B 23  ? LEU B 15  LEU B 23  1 ? 9  
HELX_P HELX_P15 15 GLU B 62  ? ALA B 80  ? GLU B 62  ALA B 80  1 ? 19 
HELX_P HELX_P16 16 ILE B 107 ? GLY B 120 ? ILE B 107 GLY B 120 1 ? 14 
HELX_P HELX_P17 17 ALA B 131 ? PHE B 138 ? ALA B 131 PHE B 138 5 ? 8  
HELX_P HELX_P18 18 ALA B 147 ? ILE B 159 ? ALA B 147 ILE B 159 1 ? 13 
HELX_P HELX_P19 19 GLU B 161 ? ASN B 164 ? GLU B 161 ASN B 164 5 ? 4  
HELX_P HELX_P20 20 ASP B 171 ? GLY B 173 ? ASP B 171 GLY B 173 5 ? 3  
HELX_P HELX_P21 21 GLY B 174 ? ASN B 186 ? GLY B 174 ASN B 186 1 ? 13 
HELX_P HELX_P22 22 CYS B 226 ? ALA B 239 ? CYS B 226 ALA B 239 1 ? 14 
HELX_P HELX_P23 23 PRO B 256 ? ASN B 263 ? PRO B 256 ASN B 263 1 ? 8  
HELX_P HELX_P24 24 GLN B 277 ? HIS B 283 ? GLN B 277 HIS B 283 1 ? 7  
HELX_P HELX_P25 25 ILE B 292 ? ASN B 305 ? ILE B 292 ASN B 305 1 ? 14 
HELX_P HELX_P26 26 SER B 310 ? HIS B 315 ? SER B 310 HIS B 315 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 2 ? 
C ? 7 ? 
D ? 5 ? 
E ? 2 ? 
F ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
C 6 7 ? parallel      
D 1 2 ? parallel      
D 2 3 ? parallel      
D 3 4 ? parallel      
D 4 5 ? parallel      
E 1 2 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? parallel      
F 3 4 ? parallel      
F 4 5 ? parallel      
F 5 6 ? parallel      
F 6 7 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ILE A 4   ? SER A 8   ? ILE A 4   SER A 8   
A 2 HIS A 52  ? VAL A 56  ? HIS A 52  VAL A 56  
A 3 ARG A 84  ? ILE A 89  ? ARG A 84  ILE A 89  
A 4 HIS A 123 ? MET A 127 ? HIS A 123 MET A 127 
A 5 VAL A 142 ? LEU A 145 ? VAL A 142 LEU A 145 
B 1 VAL A 30  ? VAL A 31  ? VAL A 30  VAL A 31  
B 2 GLU A 43  ? ILE A 44  ? GLU A 43  ILE A 44  
C 1 MET A 205 ? VAL A 208 ? MET A 205 VAL A 208 
C 2 ASP A 188 ? LYS A 194 ? ASP A 188 LYS A 194 
C 3 THR A 166 ? SER A 169 ? THR A 166 SER A 169 
C 4 ALA A 216 ? ALA A 223 ? ALA A 216 ALA A 223 
C 5 VAL A 244 ? GLY A 251 ? VAL A 244 GLY A 251 
C 6 PHE A 266 ? THR A 272 ? PHE A 266 THR A 272 
C 7 ILE A 287 ? ILE A 290 ? ILE A 287 ILE A 290 
D 1 ILE B 4   ? SER B 8   ? ILE B 4   SER B 8   
D 2 HIS B 52  ? VAL B 56  ? HIS B 52  VAL B 56  
D 3 ARG B 84  ? ILE B 89  ? ARG B 84  ILE B 89  
D 4 HIS B 123 ? MET B 127 ? HIS B 123 MET B 127 
D 5 VAL B 142 ? LEU B 145 ? VAL B 142 LEU B 145 
E 1 VAL B 30  ? LYS B 34  ? VAL B 30  LYS B 34  
E 2 THR B 40  ? ILE B 44  ? THR B 40  ILE B 44  
F 1 MET B 205 ? GLY B 209 ? MET B 205 GLY B 209 
F 2 ASP B 188 ? LYS B 194 ? ASP B 188 LYS B 194 
F 3 THR B 166 ? SER B 169 ? THR B 166 SER B 169 
F 4 VAL B 215 ? ALA B 223 ? VAL B 215 ALA B 223 
F 5 ARG B 243 ? GLY B 251 ? ARG B 243 GLY B 251 
F 6 ALA B 268 ? THR B 272 ? ALA B 268 THR B 272 
F 7 ILE B 287 ? ILE B 290 ? ILE B 287 ILE B 290 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N PHE A 7   ? N PHE A 7   O TYR A 54  ? O TYR A 54  
A 2 3 N VAL A 53  ? N VAL A 53  O THR A 86  ? O THR A 86  
A 3 4 N ILE A 89  ? N ILE A 89  O ILE A 125 ? O ILE A 125 
A 4 5 N THR A 126 ? N THR A 126 O LEU A 145 ? O LEU A 145 
B 1 2 N VAL A 31  ? N VAL A 31  O GLU A 43  ? O GLU A 43  
C 1 2 O VAL A 206 ? O VAL A 206 N HIS A 193 ? N HIS A 193 
C 2 3 O ASP A 188 ? O ASP A 188 N ILE A 167 ? N ILE A 167 
C 3 4 N THR A 166 ? N THR A 166 O ILE A 217 ? O ILE A 217 
C 4 5 N LEU A 218 ? N LEU A 218 O ILE A 247 ? O ILE A 247 
C 5 6 N VAL A 244 ? N VAL A 244 O GLU A 267 ? O GLU A 267 
C 6 7 N VAL A 271 ? N VAL A 271 O GLN A 288 ? O GLN A 288 
D 1 2 N LYS B 5   ? N LYS B 5   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 ASP B 143 ? O ASP B 143 
E 1 2 N VAL B 31  ? N VAL B 31  O GLU B 43  ? O GLU B 43  
F 1 2 O VAL B 208 ? O VAL B 208 N LEU B 191 ? N LEU B 191 
F 2 3 O ILE B 192 ? O ILE B 192 N SER B 169 ? N SER B 169 
F 3 4 N THR B 166 ? N THR B 166 O ILE B 217 ? O ILE B 217 
F 4 5 N LEU B 218 ? N LEU B 218 O ILE B 247 ? O ILE B 247 
F 5 6 N ALA B 246 ? N ALA B 246 O VAL B 270 ? O VAL B 270 
F 6 7 N VAL B 271 ? N VAL B 271 O ILE B 290 ? O ILE B 290 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 A 401'  
AC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 A 402'  
AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 A 403'  
AC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MG A 404'   
AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 B 1001' 
AC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 B 1002' 
AC7 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 B 1003' 
AC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE MG B 1004'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 6 ASP A 224 ? ASP A 224  . ? 1_555 ? 
2  AC1 6 THR A 225 ? THR A 225  . ? 1_555 ? 
3  AC1 6 CYS A 226 ? CYS A 226  . ? 1_555 ? 
4  AC1 6 GLY A 227 ? GLY A 227  . ? 1_555 ? 
5  AC1 6 THR A 228 ? THR A 228  . ? 1_555 ? 
6  AC1 6 HOH K .   ? HOH A 516  . ? 1_555 ? 
7  AC2 8 SER A 47  ? SER A 47   . ? 3_555 ? 
8  AC2 8 ARG A 49  ? ARG A 49   . ? 3_555 ? 
9  AC2 8 SER A 308 ? SER A 308  . ? 1_555 ? 
10 AC2 8 VAL A 309 ? VAL A 309  . ? 1_555 ? 
11 AC2 8 SER A 310 ? SER A 310  . ? 1_555 ? 
12 AC2 8 HOH K .   ? HOH A 511  . ? 3_555 ? 
13 AC2 8 HOH K .   ? HOH A 529  . ? 1_555 ? 
14 AC2 8 ARG B 104 ? ARG B 104  . ? 1_555 ? 
15 AC3 8 SER A 132 ? SER A 132  . ? 1_555 ? 
16 AC3 8 GLN A 135 ? GLN A 135  . ? 1_555 ? 
17 AC3 8 ASN A 144 ? ASN A 144  . ? 1_555 ? 
18 AC3 8 TYR A 146 ? TYR A 146  . ? 1_555 ? 
19 AC3 8 HOH K .   ? HOH A 501  . ? 1_555 ? 
20 AC3 8 LYS B 100 ? LYS B 100  . ? 1_555 ? 
21 AC3 8 ASP B 101 ? ASP B 101  . ? 1_555 ? 
22 AC3 8 LYS B 102 ? LYS B 102  . ? 1_555 ? 
23 AC4 2 HIS A 52  ? HIS A 52   . ? 1_555 ? 
24 AC4 2 TYR A 54  ? TYR A 54   . ? 1_555 ? 
25 AC5 5 ASP B 224 ? ASP B 224  . ? 1_555 ? 
26 AC5 5 THR B 225 ? THR B 225  . ? 1_555 ? 
27 AC5 5 CYS B 226 ? CYS B 226  . ? 1_555 ? 
28 AC5 5 GLY B 227 ? GLY B 227  . ? 1_555 ? 
29 AC5 5 THR B 228 ? THR B 228  . ? 1_555 ? 
30 AC6 7 ARG A 104 ? ARG A 104  . ? 1_555 ? 
31 AC6 7 SER B 47  ? SER B 47   . ? 2_555 ? 
32 AC6 7 ARG B 49  ? ARG B 49   . ? 2_555 ? 
33 AC6 7 SER B 308 ? SER B 308  . ? 1_555 ? 
34 AC6 7 VAL B 309 ? VAL B 309  . ? 1_555 ? 
35 AC6 7 SER B 310 ? SER B 310  . ? 1_555 ? 
36 AC6 7 HOH L .   ? HOH B 1121 . ? 1_555 ? 
37 AC7 7 ASP A 101 ? ASP A 101  . ? 1_555 ? 
38 AC7 7 LYS A 102 ? LYS A 102  . ? 1_555 ? 
39 AC7 7 SER B 132 ? SER B 132  . ? 1_555 ? 
40 AC7 7 GLN B 135 ? GLN B 135  . ? 1_555 ? 
41 AC7 7 ASN B 144 ? ASN B 144  . ? 1_555 ? 
42 AC7 7 TYR B 146 ? TYR B 146  . ? 1_555 ? 
43 AC7 7 HOH L .   ? HOH B 1103 . ? 1_555 ? 
44 AC8 2 HIS B 52  ? HIS B 52   . ? 1_555 ? 
45 AC8 2 TYR B 54  ? TYR B 54   . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4F8E 
_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                    4F8E 
_atom_sites.fract_transf_matrix[1][1]   0.005872 
_atom_sites.fract_transf_matrix[1][2]   0.003390 
_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]   0.006780 
_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]   0.016194 
_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  
MG 
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   . PRO A 1 2   ? 4.881   6.335   -30.147 1.00 62.87  ? 2    PRO A N   1 
ATOM   2    C  CA  . PRO A 1 2   ? 3.780   7.240   -29.844 1.00 75.44  ? 2    PRO A CA  1 
ATOM   3    C  C   . PRO A 1 2   ? 4.246   8.632   -29.471 1.00 84.33  ? 2    PRO A C   1 
ATOM   4    O  O   . PRO A 1 2   ? 5.432   8.907   -29.405 1.00 85.80  ? 2    PRO A O   1 
ATOM   5    C  CB  . PRO A 1 2   ? 3.101   6.560   -28.669 1.00 20.00  ? 2    PRO A CB  1 
ATOM   6    C  CG  . PRO A 1 2   ? 3.348   5.133   -28.930 1.00 20.00  ? 2    PRO A CG  1 
ATOM   7    C  CD  . PRO A 1 2   ? 4.770   5.098   -29.378 1.00 20.00  ? 2    PRO A CD  1 
ATOM   8    N  N   . ASN A 1 3   ? 3.299   9.518   -29.243 0.70 83.44  ? 3    ASN A N   1 
ATOM   9    C  CA  . ASN A 1 3   ? 3.644   10.884  -28.911 0.70 79.77  ? 3    ASN A CA  1 
ATOM   10   C  C   . ASN A 1 3   ? 3.994   11.112  -27.437 0.70 66.36  ? 3    ASN A C   1 
ATOM   11   O  O   . ASN A 1 3   ? 3.403   10.508  -26.546 0.70 64.34  ? 3    ASN A O   1 
ATOM   12   C  CB  . ASN A 1 3   ? 2.492   11.806  -29.301 1.00 20.00  ? 3    ASN A CB  1 
ATOM   13   N  N   . ILE A 1 4   ? 4.935   12.006  -27.183 1.00 53.39  ? 4    ILE A N   1 
ATOM   14   C  CA  . ILE A 1 4   ? 5.080   12.455  -25.797 1.00 56.38  ? 4    ILE A CA  1 
ATOM   15   C  C   . ILE A 1 4   ? 4.897   13.953  -25.567 1.00 53.06  ? 4    ILE A C   1 
ATOM   16   O  O   . ILE A 1 4   ? 4.927   14.720  -26.496 1.00 50.69  ? 4    ILE A O   1 
ATOM   17   C  CB  . ILE A 1 4   ? 6.469   12.146  -25.199 1.00 61.08  ? 4    ILE A CB  1 
ATOM   18   C  CG1 . ILE A 1 4   ? 7.560   12.916  -25.898 1.00 51.37  ? 4    ILE A CG1 1 
ATOM   19   C  CG2 . ILE A 1 4   ? 6.780   10.672  -25.141 1.00 65.88  ? 4    ILE A CG2 1 
ATOM   20   C  CD1 . ILE A 1 4   ? 8.551   13.468  -24.923 1.00 53.03  ? 4    ILE A CD1 1 
ATOM   21   N  N   . LYS A 1 5   ? 4.749   14.364  -24.314 1.00 36.97  ? 5    LYS A N   1 
ATOM   22   C  CA  . LYS A 1 5   ? 4.654   15.775  -23.997 1.00 27.58  ? 5    LYS A CA  1 
ATOM   23   C  C   . LYS A 1 5   ? 5.666   16.132  -22.924 1.00 38.34  ? 5    LYS A C   1 
ATOM   24   O  O   . LYS A 1 5   ? 5.849   15.394  -21.951 1.00 37.06  ? 5    LYS A O   1 
ATOM   25   C  CB  . LYS A 1 5   ? 3.238   16.131  -23.554 1.00 30.62  ? 5    LYS A CB  1 
ATOM   26   C  CG  . LYS A 1 5   ? 2.275   16.322  -24.723 1.00 49.02  ? 5    LYS A CG  1 
ATOM   27   N  N   . ILE A 1 6   ? 6.338   17.260  -23.105 1.00 33.41  ? 6    ILE A N   1 
ATOM   28   C  CA  . ILE A 1 6   ? 7.339   17.674  -22.145 1.00 30.78  ? 6    ILE A CA  1 
ATOM   29   C  C   . ILE A 1 6   ? 6.978   19.029  -21.552 1.00 37.21  ? 6    ILE A C   1 
ATOM   30   O  O   . ILE A 1 6   ? 6.670   19.974  -22.280 1.00 29.86  ? 6    ILE A O   1 
ATOM   31   C  CB  . ILE A 1 6   ? 8.754   17.657  -22.737 1.00 40.73  ? 6    ILE A CB  1 
ATOM   32   C  CG1 . ILE A 1 6   ? 9.727   18.334  -21.779 1.00 44.81  ? 6    ILE A CG1 1 
ATOM   33   C  CG2 . ILE A 1 6   ? 8.782   18.332  -24.096 1.00 40.98  ? 6    ILE A CG2 1 
ATOM   34   C  CD1 . ILE A 1 6   ? 11.161  18.042  -22.104 1.00 55.33  ? 6    ILE A CD1 1 
ATOM   35   N  N   . PHE A 1 7   ? 6.966   19.083  -20.219 1.00 26.76  ? 7    PHE A N   1 
ATOM   36   C  CA  . PHE A 1 7   ? 6.651   20.292  -19.483 1.00 25.41  ? 7    PHE A CA  1 
ATOM   37   C  C   . PHE A 1 7   ? 7.872   20.708  -18.664 1.00 27.00  ? 7    PHE A C   1 
ATOM   38   O  O   . PHE A 1 7   ? 8.720   19.887  -18.337 1.00 33.49  ? 7    PHE A O   1 
ATOM   39   C  CB  . PHE A 1 7   ? 5.467   20.049  -18.538 1.00 23.85  ? 7    PHE A CB  1 
ATOM   40   C  CG  . PHE A 1 7   ? 4.147   19.826  -19.244 1.00 32.96  ? 7    PHE A CG  1 
ATOM   41   C  CD1 . PHE A 1 7   ? 3.747   18.553  -19.625 1.00 31.04  ? 7    PHE A CD1 1 
ATOM   42   C  CD2 . PHE A 1 7   ? 3.297   20.884  -19.498 1.00 21.94  ? 7    PHE A CD2 1 
ATOM   43   C  CE1 . PHE A 1 7   ? 2.543   18.357  -20.264 1.00 32.65  ? 7    PHE A CE1 1 
ATOM   44   C  CE2 . PHE A 1 7   ? 2.071   20.690  -20.128 1.00 26.85  ? 7    PHE A CE2 1 
ATOM   45   C  CZ  . PHE A 1 7   ? 1.701   19.434  -20.519 1.00 28.75  ? 7    PHE A CZ  1 
ATOM   46   N  N   . SER A 1 8   ? 7.948   21.984  -18.331 1.00 28.96  ? 8    SER A N   1 
ATOM   47   C  CA  . SER A 1 8   ? 9.022   22.487  -17.502 1.00 36.11  ? 8    SER A CA  1 
ATOM   48   C  C   . SER A 1 8   ? 8.475   22.938  -16.170 1.00 48.97  ? 8    SER A C   1 
ATOM   49   O  O   . SER A 1 8   ? 7.416   23.557  -16.114 1.00 43.78  ? 8    SER A O   1 
ATOM   50   C  CB  . SER A 1 8   ? 9.677   23.684  -18.169 1.00 51.57  ? 8    SER A CB  1 
ATOM   51   O  OG  . SER A 1 8   ? 10.372  24.449  -17.206 1.00 58.93  ? 8    SER A OG  1 
ATOM   52   N  N   . GLY A 1 9   ? 9.201   22.634  -15.098 0.70 66.91  ? 9    GLY A N   1 
ATOM   53   C  CA  . GLY A 1 9   ? 8.920   23.223  -13.802 0.70 81.16  ? 9    GLY A CA  1 
ATOM   54   C  C   . GLY A 1 9   ? 9.404   24.664  -13.776 0.70 97.16  ? 9    GLY A C   1 
ATOM   55   O  O   . GLY A 1 9   ? 10.427  24.990  -14.373 0.70 101.69 ? 9    GLY A O   1 
ATOM   56   N  N   . SER A 1 10  ? 8.658   25.527  -13.095 1.00 109.57 ? 10   SER A N   1 
ATOM   57   C  CA  . SER A 1 10  ? 9.005   26.945  -12.946 1.00 117.16 ? 10   SER A CA  1 
ATOM   58   C  C   . SER A 1 10  ? 9.164   27.755  -14.221 1.00 120.37 ? 10   SER A C   1 
ATOM   59   O  O   . SER A 1 10  ? 8.501   27.499  -15.226 1.00 123.86 ? 10   SER A O   1 
ATOM   60   C  CB  . SER A 1 10  ? 10.202  27.131  -12.015 1.00 119.41 ? 10   SER A CB  1 
ATOM   61   O  OG  . SER A 1 10  ? 11.405  27.220  -12.761 1.00 118.68 ? 10   SER A OG  1 
ATOM   62   N  N   . SER A 1 11  ? 10.055  28.740  -14.160 1.00 118.14 ? 11   SER A N   1 
ATOM   63   C  CA  . SER A 1 11  ? 10.343  29.582  -15.309 1.00 120.00 ? 11   SER A CA  1 
ATOM   64   C  C   . SER A 1 11  ? 11.839  29.493  -15.596 1.00 121.88 ? 11   SER A C   1 
ATOM   65   O  O   . SER A 1 11  ? 12.354  30.215  -16.451 1.00 127.13 ? 11   SER A O   1 
ATOM   66   C  CB  . SER A 1 11  ? 9.889   31.041  -15.192 1.00 116.91 ? 11   SER A CB  1 
ATOM   67   O  OG  . SER A 1 11  ? 8.778   31.295  -16.039 1.00 110.34 ? 11   SER A OG  1 
ATOM   68   N  N   . HIS A 1 12  ? 12.540  28.617  -14.880 1.00 114.64 ? 12   HIS A N   1 
ATOM   69   C  CA  . HIS A 1 12  ? 13.775  28.089  -15.434 1.00 112.22 ? 12   HIS A CA  1 
ATOM   70   C  C   . HIS A 1 12  ? 13.300  27.276  -16.613 1.00 105.27 ? 12   HIS A C   1 
ATOM   71   O  O   . HIS A 1 12  ? 12.683  26.228  -16.435 1.00 110.56 ? 12   HIS A O   1 
ATOM   72   C  CB  . HIS A 1 12  ? 14.483  27.137  -14.481 1.00 117.59 ? 12   HIS A CB  1 
ATOM   73   C  CG  . HIS A 1 12  ? 15.090  25.946  -15.169 1.00 119.22 ? 12   HIS A CG  1 
ATOM   74   N  ND1 . HIS A 1 12  ? 14.341  24.869  -15.597 1.00 116.26 ? 12   HIS A ND1 1 
ATOM   75   C  CD2 . HIS A 1 12  ? 16.372  25.670  -15.510 1.00 119.00 ? 12   HIS A CD2 1 
ATOM   76   C  CE1 . HIS A 1 12  ? 15.134  23.982  -16.170 1.00 116.16 ? 12   HIS A CE1 1 
ATOM   77   N  NE2 . HIS A 1 12  ? 16.372  24.441  -16.125 1.00 117.27 ? 12   HIS A NE2 1 
ATOM   78   N  N   . GLN A 1 13  ? 13.537  27.756  -17.820 1.00 92.06  ? 13   GLN A N   1 
ATOM   79   C  CA  . GLN A 1 13  ? 13.113  26.987  -18.969 1.00 84.98  ? 13   GLN A CA  1 
ATOM   80   C  C   . GLN A 1 13  ? 14.293  26.694  -19.855 1.00 78.67  ? 13   GLN A C   1 
ATOM   81   O  O   . GLN A 1 13  ? 14.149  26.096  -20.915 1.00 90.42  ? 13   GLN A O   1 
ATOM   82   C  CB  . GLN A 1 13  ? 11.995  27.698  -19.735 1.00 82.17  ? 13   GLN A CB  1 
ATOM   83   C  CG  . GLN A 1 13  ? 10.660  27.675  -19.003 1.00 82.97  ? 13   GLN A CG  1 
ATOM   84   C  CD  . GLN A 1 13  ? 9.474   27.676  -19.950 1.00 84.66  ? 13   GLN A CD  1 
ATOM   85   O  OE1 . GLN A 1 13  ? 8.398   27.169  -19.619 1.00 86.44  ? 13   GLN A OE1 1 
ATOM   86   N  NE2 . GLN A 1 13  ? 9.665   28.241  -21.141 1.00 81.30  ? 13   GLN A NE2 1 
ATOM   87   N  N   . ASP A 1 14  ? 15.475  27.096  -19.409 1.00 62.63  ? 14   ASP A N   1 
ATOM   88   C  CA  . ASP A 1 14  ? 16.650  26.923  -20.244 1.00 59.32  ? 14   ASP A CA  1 
ATOM   89   C  C   . ASP A 1 14  ? 16.912  25.454  -20.544 1.00 45.32  ? 14   ASP A C   1 
ATOM   90   O  O   . ASP A 1 14  ? 16.889  25.058  -21.713 1.00 53.74  ? 14   ASP A O   1 
ATOM   91   C  CB  . ASP A 1 14  ? 17.884  27.586  -19.636 1.00 74.57  ? 14   ASP A CB  1 
ATOM   92   C  CG  . ASP A 1 14  ? 18.992  27.765  -20.653 1.00 88.99  ? 14   ASP A CG  1 
ATOM   93   O  OD1 . ASP A 1 14  ? 19.939  26.945  -20.656 1.00 99.18  ? 14   ASP A OD1 1 
ATOM   94   O  OD2 . ASP A 1 14  ? 18.899  28.708  -21.467 1.00 88.97  ? 14   ASP A OD2 1 
ATOM   95   N  N   . LEU A 1 15  ? 17.155  24.648  -19.507 1.00 33.79  ? 15   LEU A N   1 
ATOM   96   C  CA  . LEU A 1 15  ? 17.355  23.215  -19.710 1.00 32.90  ? 15   LEU A CA  1 
ATOM   97   C  C   . LEU A 1 15  ? 16.147  22.622  -20.419 1.00 44.35  ? 15   LEU A C   1 
ATOM   98   O  O   . LEU A 1 15  ? 16.293  21.958  -21.446 1.00 48.86  ? 15   LEU A O   1 
ATOM   99   C  CB  . LEU A 1 15  ? 17.578  22.476  -18.398 1.00 31.14  ? 15   LEU A CB  1 
ATOM   100  C  CG  . LEU A 1 15  ? 18.837  21.629  -18.240 1.00 36.87  ? 15   LEU A CG  1 
ATOM   101  C  CD1 . LEU A 1 15  ? 18.669  20.610  -17.091 1.00 33.63  ? 15   LEU A CD1 1 
ATOM   102  C  CD2 . LEU A 1 15  ? 19.189  20.922  -19.525 1.00 41.64  ? 15   LEU A CD2 1 
ATOM   103  N  N   . SER A 1 16  ? 14.962  22.865  -19.863 1.00 38.62  ? 16   SER A N   1 
ATOM   104  C  CA  . SER A 1 16  ? 13.714  22.362  -20.432 1.00 40.19  ? 16   SER A CA  1 
ATOM   105  C  C   . SER A 1 16  ? 13.602  22.672  -21.926 1.00 35.74  ? 16   SER A C   1 
ATOM   106  O  O   . SER A 1 16  ? 13.321  21.791  -22.733 1.00 36.78  ? 16   SER A O   1 
ATOM   107  C  CB  . SER A 1 16  ? 12.509  22.966  -19.702 1.00 42.06  ? 16   SER A CB  1 
ATOM   108  O  OG  . SER A 1 16  ? 12.442  22.516  -18.371 1.00 63.30  ? 16   SER A OG  1 
ATOM   109  N  N   . GLN A 1 17  ? 13.805  23.936  -22.274 1.00 30.99  ? 17   GLN A N   1 
ATOM   110  C  CA  . GLN A 1 17  ? 13.708  24.388  -23.658 1.00 37.59  ? 17   GLN A CA  1 
ATOM   111  C  C   . GLN A 1 17  ? 14.838  23.818  -24.511 1.00 46.13  ? 17   GLN A C   1 
ATOM   112  O  O   . GLN A 1 17  ? 14.650  23.514  -25.688 1.00 46.98  ? 17   GLN A O   1 
ATOM   113  C  CB  . GLN A 1 17  ? 13.712  25.918  -23.722 1.00 40.23  ? 17   GLN A CB  1 
ATOM   114  C  CG  . GLN A 1 17  ? 13.423  26.482  -25.094 1.00 52.37  ? 17   GLN A CG  1 
ATOM   115  C  CD  . GLN A 1 17  ? 12.026  26.145  -25.583 1.00 61.99  ? 17   GLN A CD  1 
ATOM   116  O  OE1 . GLN A 1 17  ? 11.031  26.654  -25.055 1.00 59.14  ? 17   GLN A OE1 1 
ATOM   117  N  NE2 . GLN A 1 17  ? 11.943  25.276  -26.599 1.00 61.62  ? 17   GLN A NE2 1 
ATOM   118  N  N   . LYS A 1 18  ? 16.019  23.675  -23.934 1.00 42.88  ? 18   LYS A N   1 
ATOM   119  C  CA  . LYS A 1 18  ? 17.082  23.030  -24.685 1.00 49.05  ? 18   LYS A CA  1 
ATOM   120  C  C   . LYS A 1 18  ? 16.656  21.608  -25.037 1.00 48.77  ? 18   LYS A C   1 
ATOM   121  O  O   . LYS A 1 18  ? 16.706  21.204  -26.194 1.00 40.27  ? 18   LYS A O   1 
ATOM   122  C  CB  . LYS A 1 18  ? 18.392  23.030  -23.910 1.00 44.85  ? 18   LYS A CB  1 
ATOM   123  C  CG  . LYS A 1 18  ? 19.225  24.269  -24.132 1.00 43.05  ? 18   LYS A CG  1 
ATOM   124  C  CD  . LYS A 1 18  ? 20.497  24.218  -23.297 1.00 53.02  ? 18   LYS A CD  1 
ATOM   125  C  CE  . LYS A 1 18  ? 21.433  25.378  -23.608 1.00 57.07  ? 18   LYS A CE  1 
ATOM   126  N  NZ  . LYS A 1 18  ? 20.747  26.711  -23.538 1.00 65.22  ? 18   LYS A NZ  1 
ATOM   127  N  N   . ILE A 1 19  ? 16.222  20.863  -24.024 1.00 46.23  ? 19   ILE A N   1 
ATOM   128  C  CA  . ILE A 1 19  ? 15.781  19.480  -24.185 1.00 34.55  ? 19   ILE A CA  1 
ATOM   129  C  C   . ILE A 1 19  ? 14.689  19.315  -25.255 1.00 32.29  ? 19   ILE A C   1 
ATOM   130  O  O   . ILE A 1 19  ? 14.803  18.462  -26.139 1.00 36.22  ? 19   ILE A O   1 
ATOM   131  C  CB  . ILE A 1 19  ? 15.287  18.916  -22.838 1.00 34.22  ? 19   ILE A CB  1 
ATOM   132  C  CG1 . ILE A 1 19  ? 16.465  18.778  -21.878 1.00 33.55  ? 19   ILE A CG1 1 
ATOM   133  C  CG2 . ILE A 1 19  ? 14.571  17.586  -23.029 1.00 32.75  ? 19   ILE A CG2 1 
ATOM   134  C  CD1 . ILE A 1 19  ? 16.064  18.481  -20.429 1.00 27.81  ? 19   ILE A CD1 1 
ATOM   135  N  N   . ALA A 1 20  ? 13.642  20.133  -25.173 1.00 28.86  ? 20   ALA A N   1 
ATOM   136  C  CA  . ALA A 1 20  ? 12.516  20.043  -26.095 1.00 36.41  ? 20   ALA A CA  1 
ATOM   137  C  C   . ALA A 1 20  ? 12.952  20.329  -27.531 1.00 40.99  ? 20   ALA A C   1 
ATOM   138  O  O   . ALA A 1 20  ? 12.377  19.794  -28.475 1.00 50.56  ? 20   ALA A O   1 
ATOM   139  C  CB  . ALA A 1 20  ? 11.399  20.989  -25.683 1.00 23.61  ? 20   ALA A CB  1 
ATOM   140  N  N   . ASP A 1 21  ? 13.960  21.181  -27.688 1.00 48.23  ? 21   ASP A N   1 
ATOM   141  C  CA  . ASP A 1 21  ? 14.504  21.494  -29.011 1.00 53.52  ? 21   ASP A CA  1 
ATOM   142  C  C   . ASP A 1 21  ? 15.109  20.252  -29.635 1.00 49.64  ? 21   ASP A C   1 
ATOM   143  O  O   . ASP A 1 21  ? 14.754  19.863  -30.744 1.00 50.27  ? 21   ASP A O   1 
ATOM   144  C  CB  . ASP A 1 21  ? 15.580  22.577  -28.921 1.00 54.62  ? 21   ASP A CB  1 
ATOM   145  C  CG  . ASP A 1 21  ? 15.008  23.952  -28.641 1.00 66.33  ? 21   ASP A CG  1 
ATOM   146  O  OD1 . ASP A 1 21  ? 13.778  24.138  -28.796 1.00 73.86  ? 21   ASP A OD1 1 
ATOM   147  O  OD2 . ASP A 1 21  ? 15.799  24.852  -28.270 1.00 70.63  ? 21   ASP A OD2 1 
ATOM   148  N  N   . ARG A 1 22  ? 16.020  19.624  -28.902 1.00 46.55  ? 22   ARG A N   1 
ATOM   149  C  CA  . ARG A 1 22  ? 16.690  18.428  -29.385 1.00 50.21  ? 22   ARG A CA  1 
ATOM   150  C  C   . ARG A 1 22  ? 15.692  17.332  -29.747 1.00 46.01  ? 22   ARG A C   1 
ATOM   151  O  O   . ARG A 1 22  ? 15.998  16.430  -30.520 1.00 49.23  ? 22   ARG A O   1 
ATOM   152  C  CB  . ARG A 1 22  ? 17.685  17.915  -28.343 1.00 41.43  ? 22   ARG A CB  1 
ATOM   153  C  CG  . ARG A 1 22  ? 18.716  18.949  -27.897 1.00 49.89  ? 22   ARG A CG  1 
ATOM   154  C  CD  . ARG A 1 22  ? 19.813  18.309  -27.053 1.00 52.40  ? 22   ARG A CD  1 
ATOM   155  N  NE  . ARG A 1 22  ? 20.846  19.258  -26.643 1.00 65.49  ? 22   ARG A NE  1 
ATOM   156  C  CZ  . ARG A 1 22  ? 21.856  19.653  -27.416 1.00 80.19  ? 22   ARG A CZ  1 
ATOM   157  N  NH1 . ARG A 1 22  ? 21.970  19.190  -28.656 1.00 86.11  ? 22   ARG A NH1 1 
ATOM   158  N  NH2 . ARG A 1 22  ? 22.752  20.519  -26.952 1.00 79.22  ? 22   ARG A NH2 1 
ATOM   159  N  N   . LEU A 1 23  ? 14.493  17.416  -29.190 1.00 43.44  ? 23   LEU A N   1 
ATOM   160  C  CA  . LEU A 1 23  ? 13.476  16.412  -29.449 1.00 40.21  ? 23   LEU A CA  1 
ATOM   161  C  C   . LEU A 1 23  ? 12.451  16.862  -30.494 1.00 42.17  ? 23   LEU A C   1 
ATOM   162  O  O   . LEU A 1 23  ? 11.598  16.074  -30.897 1.00 45.74  ? 23   LEU A O   1 
ATOM   163  C  CB  . LEU A 1 23  ? 12.775  16.006  -28.148 1.00 42.36  ? 23   LEU A CB  1 
ATOM   164  C  CG  . LEU A 1 23  ? 13.615  15.358  -27.037 1.00 46.78  ? 23   LEU A CG  1 
ATOM   165  C  CD1 . LEU A 1 23  ? 12.773  15.135  -25.785 1.00 32.74  ? 23   LEU A CD1 1 
ATOM   166  C  CD2 . LEU A 1 23  ? 14.254  14.046  -27.495 1.00 52.51  ? 23   LEU A CD2 1 
ATOM   167  N  N   . GLY A 1 24  ? 12.528  18.119  -30.929 1.00 38.27  ? 24   GLY A N   1 
ATOM   168  C  CA  . GLY A 1 24  ? 11.638  18.615  -31.970 1.00 42.61  ? 24   GLY A CA  1 
ATOM   169  C  C   . GLY A 1 24  ? 10.245  18.878  -31.430 1.00 48.37  ? 24   GLY A C   1 
ATOM   170  O  O   . GLY A 1 24  ? 9.240   18.757  -32.150 1.00 41.48  ? 24   GLY A O   1 
ATOM   171  N  N   . LEU A 1 25  ? 10.188  19.231  -30.146 1.00 39.49  ? 25   LEU A N   1 
ATOM   172  C  CA  . LEU A 1 25  ? 8.920   19.463  -29.457 1.00 28.93  ? 25   LEU A CA  1 
ATOM   173  C  C   . LEU A 1 25  ? 8.888   20.879  -28.893 1.00 30.42  ? 25   LEU A C   1 
ATOM   174  O  O   . LEU A 1 25  ? 9.937   21.456  -28.591 1.00 32.69  ? 25   LEU A O   1 
ATOM   175  C  CB  . LEU A 1 25  ? 8.752   18.467  -28.312 1.00 36.92  ? 25   LEU A CB  1 
ATOM   176  C  CG  . LEU A 1 25  ? 8.926   16.987  -28.650 1.00 44.48  ? 25   LEU A CG  1 
ATOM   177  C  CD1 . LEU A 1 25  ? 8.758   16.150  -27.389 1.00 46.80  ? 25   LEU A CD1 1 
ATOM   178  C  CD2 . LEU A 1 25  ? 7.937   16.550  -29.731 1.00 38.13  ? 25   LEU A CD2 1 
ATOM   179  N  N   . GLU A 1 26  ? 7.697   21.446  -28.770 0.60 16.05  ? 26   GLU A N   1 
ATOM   180  C  CA  . GLU A 1 26  ? 7.522   22.616  -27.947 0.60 11.04  ? 26   GLU A CA  1 
ATOM   181  C  C   . GLU A 1 26  ? 7.162   22.135  -26.539 0.60 21.81  ? 26   GLU A C   1 
ATOM   182  O  O   . GLU A 1 26  ? 6.502   21.109  -26.376 0.60 15.64  ? 26   GLU A O   1 
ATOM   183  C  CB  . GLU A 1 26  ? 6.402   23.497  -28.480 0.60 29.02  ? 26   GLU A CB  1 
ATOM   184  C  CG  . GLU A 1 26  ? 6.658   24.148  -29.810 0.60 37.07  ? 26   GLU A CG  1 
ATOM   185  C  CD  . GLU A 1 26  ? 5.413   24.823  -30.342 0.60 58.42  ? 26   GLU A CD  1 
ATOM   186  O  OE1 . GLU A 1 26  ? 4.392   24.822  -29.622 0.60 60.61  ? 26   GLU A OE1 1 
ATOM   187  O  OE2 . GLU A 1 26  ? 5.448   25.346  -31.475 0.60 69.74  ? 26   GLU A OE2 1 
ATOM   188  N  N   . LEU A 1 27  ? 7.606   22.877  -25.531 1.00 30.08  ? 27   LEU A N   1 
ATOM   189  C  CA  . LEU A 1 27  ? 7.195   22.635  -24.138 1.00 35.81  ? 27   LEU A CA  1 
ATOM   190  C  C   . LEU A 1 27  ? 5.681   22.760  -24.001 1.00 34.60  ? 27   LEU A C   1 
ATOM   191  O  O   . LEU A 1 27  ? 5.087   23.665  -24.573 1.00 22.10  ? 27   LEU A O   1 
ATOM   192  C  CB  . LEU A 1 27  ? 7.879   23.630  -23.183 1.00 28.17  ? 27   LEU A CB  1 
ATOM   193  C  CG  . LEU A 1 27  ? 9.386   23.474  -22.943 1.00 33.19  ? 27   LEU A CG  1 
ATOM   194  C  CD1 . LEU A 1 27  ? 9.941   24.599  -22.048 1.00 26.47  ? 27   LEU A CD1 1 
ATOM   195  C  CD2 . LEU A 1 27  ? 9.688   22.102  -22.346 1.00 29.16  ? 27   LEU A CD2 1 
ATOM   196  N  N   . GLY A 1 28  ? 5.051   21.854  -23.256 1.00 33.65  ? 28   GLY A N   1 
ATOM   197  C  CA  . GLY A 1 28  ? 3.620   21.951  -23.012 1.00 28.64  ? 28   GLY A CA  1 
ATOM   198  C  C   . GLY A 1 28  ? 3.214   23.270  -22.365 1.00 31.04  ? 28   GLY A C   1 
ATOM   199  O  O   . GLY A 1 28  ? 4.040   23.936  -21.766 1.00 33.44  ? 28   GLY A O   1 
ATOM   200  N  N   . LYS A 1 29  ? 1.942   23.646  -22.487 0.80 27.09  ? 29   LYS A N   1 
ATOM   201  C  CA  . LYS A 1 29  ? 1.405   24.842  -21.839 0.80 28.64  ? 29   LYS A CA  1 
ATOM   202  C  C   . LYS A 1 29  ? 1.010   24.599  -20.376 0.80 25.67  ? 29   LYS A C   1 
ATOM   203  O  O   . LYS A 1 29  ? 0.075   23.858  -20.103 0.80 32.25  ? 29   LYS A O   1 
ATOM   204  C  CB  . LYS A 1 29  ? 0.151   25.325  -22.579 0.80 39.82  ? 29   LYS A CB  1 
ATOM   205  C  CG  . LYS A 1 29  ? 0.356   25.850  -24.008 0.80 45.87  ? 29   LYS A CG  1 
ATOM   206  C  CD  . LYS A 1 29  ? -1.013  26.020  -24.688 0.80 54.30  ? 29   LYS A CD  1 
ATOM   207  C  CE  . LYS A 1 29  ? -1.039  25.314  -26.049 0.80 55.74  ? 29   LYS A CE  1 
ATOM   208  N  NZ  . LYS A 1 29  ? -2.356  24.592  -26.170 0.80 57.76  ? 29   LYS A NZ  1 
ATOM   209  N  N   . VAL A 1 30  ? 1.710   25.229  -19.441 1.00 33.51  ? 30   VAL A N   1 
ATOM   210  C  CA  . VAL A 1 30  ? 1.332   25.191  -18.018 1.00 50.38  ? 30   VAL A CA  1 
ATOM   211  C  C   . VAL A 1 30  ? 1.183   26.595  -17.422 1.00 56.97  ? 30   VAL A C   1 
ATOM   212  O  O   . VAL A 1 30  ? 2.083   27.423  -17.542 1.00 51.98  ? 30   VAL A O   1 
ATOM   213  C  CB  . VAL A 1 30  ? 2.321   24.364  -17.134 1.00 42.78  ? 30   VAL A CB  1 
ATOM   214  C  CG1 . VAL A 1 30  ? 3.759   24.528  -17.587 1.00 40.40  ? 30   VAL A CG1 1 
ATOM   215  C  CG2 . VAL A 1 30  ? 2.192   24.779  -15.676 1.00 42.51  ? 30   VAL A CG2 1 
ATOM   216  N  N   . VAL A 1 31  ? 0.041   26.849  -16.782 1.00 65.81  ? 31   VAL A N   1 
ATOM   217  C  CA  . VAL A 1 31  ? -0.267  28.157  -16.194 1.00 68.91  ? 31   VAL A CA  1 
ATOM   218  C  C   . VAL A 1 31  ? 0.056   28.188  -14.706 1.00 69.88  ? 31   VAL A C   1 
ATOM   219  O  O   . VAL A 1 31  ? -0.485  27.400  -13.934 1.00 67.63  ? 31   VAL A O   1 
ATOM   220  C  CB  . VAL A 1 31  ? -1.755  28.516  -16.377 1.00 72.68  ? 31   VAL A CB  1 
ATOM   221  N  N   . THR A 1 32  ? 0.923   29.112  -14.306 1.00 74.91  ? 32   THR A N   1 
ATOM   222  C  CA  . THR A 1 32  ? 1.501   29.092  -12.964 1.00 75.12  ? 32   THR A CA  1 
ATOM   223  C  C   . THR A 1 32  ? 1.414   30.410  -12.202 1.00 84.95  ? 32   THR A C   1 
ATOM   224  O  O   . THR A 1 32  ? 2.120   31.367  -12.527 1.00 91.31  ? 32   THR A O   1 
ATOM   225  C  CB  . THR A 1 32  ? 2.992   28.726  -13.027 1.00 66.12  ? 32   THR A CB  1 
ATOM   226  O  OG1 . THR A 1 32  ? 3.145   27.438  -13.634 1.00 58.65  ? 32   THR A OG1 1 
ATOM   227  C  CG2 . THR A 1 32  ? 3.597   28.718  -11.625 1.00 65.67  ? 32   THR A CG2 1 
ATOM   228  N  N   . LYS A 1 33  ? 0.578   30.453  -11.168 0.95 85.47  ? 33   LYS A N   1 
ATOM   229  C  CA  . LYS A 1 33  ? 0.548   31.609  -10.269 0.95 83.07  ? 33   LYS A CA  1 
ATOM   230  C  C   . LYS A 1 33  ? 0.952   31.239  -8.833  0.95 88.44  ? 33   LYS A C   1 
ATOM   231  O  O   . LYS A 1 33  ? 0.614   30.164  -8.342  0.95 86.85  ? 33   LYS A O   1 
ATOM   232  C  CB  . LYS A 1 33  ? -0.821  32.306  -10.307 0.95 70.50  ? 33   LYS A CB  1 
ATOM   233  C  CG  . LYS A 1 33  ? -1.979  31.415  -10.726 0.95 64.42  ? 33   LYS A CG  1 
ATOM   234  N  N   . LYS A 1 34  ? 1.699   32.128  -8.180  1.00 89.90  ? 34   LYS A N   1 
ATOM   235  C  CA  . LYS A 1 34  ? 2.071   31.949  -6.780  1.00 82.39  ? 34   LYS A CA  1 
ATOM   236  C  C   . LYS A 1 34  ? 1.297   32.918  -5.905  1.00 81.70  ? 34   LYS A C   1 
ATOM   237  O  O   . LYS A 1 34  ? 1.332   34.138  -6.088  1.00 84.38  ? 34   LYS A O   1 
ATOM   238  C  CB  . LYS A 1 34  ? 3.574   32.072  -6.558  1.00 74.07  ? 34   LYS A CB  1 
ATOM   239  N  N   . PHE A 1 35  ? 0.622   32.337  -4.926  0.70 80.40  ? 35   PHE A N   1 
ATOM   240  C  CA  . PHE A 1 35  ? -0.524  32.950  -4.277  0.70 85.14  ? 35   PHE A CA  1 
ATOM   241  C  C   . PHE A 1 35  ? -0.169  34.042  -3.293  0.70 95.57  ? 35   PHE A C   1 
ATOM   242  O  O   . PHE A 1 35  ? -0.370  35.231  -3.546  0.70 99.54  ? 35   PHE A O   1 
ATOM   243  C  CB  . PHE A 1 35  ? -1.305  31.864  -3.545  0.70 88.74  ? 35   PHE A CB  1 
ATOM   244  C  CG  . PHE A 1 35  ? -2.369  31.205  -4.384  0.70 95.62  ? 35   PHE A CG  1 
ATOM   245  C  CD1 . PHE A 1 35  ? -2.136  30.861  -5.709  0.70 98.01  ? 35   PHE A CD1 1 
ATOM   246  C  CD2 . PHE A 1 35  ? -3.600  30.906  -3.832  0.70 100.15 ? 35   PHE A CD2 1 
ATOM   247  C  CE1 . PHE A 1 35  ? -3.123  30.252  -6.460  0.70 102.31 ? 35   PHE A CE1 1 
ATOM   248  C  CE2 . PHE A 1 35  ? -4.589  30.300  -4.572  0.70 104.56 ? 35   PHE A CE2 1 
ATOM   249  C  CZ  . PHE A 1 35  ? -4.353  29.969  -5.891  0.70 107.30 ? 35   PHE A CZ  1 
ATOM   250  N  N   . SER A 1 36  ? 0.354   33.627  -2.154  1.00 99.03  ? 36   SER A N   1 
ATOM   251  C  CA  . SER A 1 36  ? 0.428   34.511  -1.015  1.00 95.77  ? 36   SER A CA  1 
ATOM   252  C  C   . SER A 1 36  ? 1.662   34.122  -0.240  1.00 97.59  ? 36   SER A C   1 
ATOM   253  O  O   . SER A 1 36  ? 2.667   34.842  -0.237  1.00 103.87 ? 36   SER A O   1 
ATOM   254  C  CB  . SER A 1 36  ? -0.819  34.351  -0.141  1.00 86.61  ? 36   SER A CB  1 
ATOM   255  O  OG  . SER A 1 36  ? -0.905  33.045  0.413   1.00 78.51  ? 36   SER A OG  1 
ATOM   256  N  N   . ASN A 1 37  ? 1.593   32.963  0.400   1.00 89.39  ? 37   ASN A N   1 
ATOM   257  C  CA  . ASN A 1 37  ? 2.722   32.450  1.144   1.00 85.25  ? 37   ASN A CA  1 
ATOM   258  C  C   . ASN A 1 37  ? 3.690   31.756  0.209   1.00 78.23  ? 37   ASN A C   1 
ATOM   259  O  O   . ASN A 1 37  ? 4.481   30.925  0.643   1.00 81.06  ? 37   ASN A O   1 
ATOM   260  C  CB  . ASN A 1 37  ? 2.243   31.482  2.224   1.00 85.76  ? 37   ASN A CB  1 
ATOM   261  N  N   . GLN A 1 38  ? 3.639   32.114  -1.069  1.00 70.84  ? 38   GLN A N   1 
ATOM   262  C  CA  . GLN A 1 38  ? 4.366   31.379  -2.097  1.00 67.19  ? 38   GLN A CA  1 
ATOM   263  C  C   . GLN A 1 38  ? 3.704   30.014  -2.281  1.00 55.65  ? 38   GLN A C   1 
ATOM   264  O  O   . GLN A 1 38  ? 4.302   29.084  -2.823  1.00 59.70  ? 38   GLN A O   1 
ATOM   265  C  CB  . GLN A 1 38  ? 5.858   31.247  -1.754  1.00 70.21  ? 38   GLN A CB  1 
ATOM   266  C  CG  . GLN A 1 38  ? 6.720   30.557  -2.817  1.00 70.72  ? 38   GLN A CG  1 
ATOM   267  C  CD  . GLN A 1 38  ? 6.754   31.308  -4.138  1.00 70.78  ? 38   GLN A CD  1 
ATOM   268  O  OE1 . GLN A 1 38  ? 6.047   30.953  -5.082  1.00 67.83  ? 38   GLN A OE1 1 
ATOM   269  N  NE2 . GLN A 1 38  ? 7.580   32.349  -4.211  1.00 70.90  ? 38   GLN A NE2 1 
ATOM   270  N  N   . GLU A 1 39  ? 2.460   29.902  -1.827  1.00 39.18  ? 39   GLU A N   1 
ATOM   271  C  CA  . GLU A 1 39  ? 1.649   28.735  -2.155  1.00 43.99  ? 39   GLU A CA  1 
ATOM   272  C  C   . GLU A 1 39  ? 1.581   28.587  -3.676  1.00 48.60  ? 39   GLU A C   1 
ATOM   273  O  O   . GLU A 1 39  ? 1.156   29.507  -4.375  1.00 41.19  ? 39   GLU A O   1 
ATOM   274  C  CB  . GLU A 1 39  ? 0.251   28.849  -1.545  1.00 45.04  ? 39   GLU A CB  1 
ATOM   275  C  CG  . GLU A 1 39  ? -0.742  27.818  -2.039  1.00 50.28  ? 39   GLU A CG  1 
ATOM   276  C  CD  . GLU A 1 39  ? -1.989  27.738  -1.170  1.00 56.56  ? 39   GLU A CD  1 
ATOM   277  O  OE1 . GLU A 1 39  ? -3.074  27.410  -1.699  1.00 60.37  ? 39   GLU A OE1 1 
ATOM   278  O  OE2 . GLU A 1 39  ? -1.882  27.986  0.045   1.00 55.06  ? 39   GLU A OE2 1 
ATOM   279  N  N   . THR A 1 40  ? 2.014   27.428  -4.174  1.00 48.68  ? 40   THR A N   1 
ATOM   280  C  CA  . THR A 1 40  ? 2.180   27.195  -5.609  1.00 46.39  ? 40   THR A CA  1 
ATOM   281  C  C   . THR A 1 40  ? 0.875   26.828  -6.320  1.00 40.76  ? 40   THR A C   1 
ATOM   282  O  O   . THR A 1 40  ? 0.217   25.843  -5.968  1.00 41.91  ? 40   THR A O   1 
ATOM   283  C  CB  . THR A 1 40  ? 3.193   26.056  -5.873  1.00 51.50  ? 40   THR A CB  1 
ATOM   284  O  OG1 . THR A 1 40  ? 4.381   26.259  -5.091  1.00 52.60  ? 40   THR A OG1 1 
ATOM   285  C  CG2 . THR A 1 40  ? 3.541   25.980  -7.366  1.00 41.80  ? 40   THR A CG2 1 
ATOM   286  N  N   . CYS A 1 41  ? 0.506   27.614  -7.327  1.00 48.60  ? 41   CYS A N   1 
ATOM   287  C  CA  . CYS A 1 41  ? -0.593  27.235  -8.220  1.00 53.39  ? 41   CYS A CA  1 
ATOM   288  C  C   . CYS A 1 41  ? -0.057  26.771  -9.578  1.00 53.80  ? 41   CYS A C   1 
ATOM   289  O  O   . CYS A 1 41  ? 0.846   27.389  -10.149 1.00 61.30  ? 41   CYS A O   1 
ATOM   290  C  CB  . CYS A 1 41  ? -1.600  28.373  -8.395  1.00 56.35  ? 41   CYS A CB  1 
ATOM   291  N  N   . VAL A 1 42  ? -0.618  25.671  -10.069 1.00 45.36  ? 42   VAL A N   1 
ATOM   292  C  CA  . VAL A 1 42  ? -0.262  25.095  -11.351 1.00 45.51  ? 42   VAL A CA  1 
ATOM   293  C  C   . VAL A 1 42  ? -1.539  24.675  -12.050 1.00 49.34  ? 42   VAL A C   1 
ATOM   294  O  O   . VAL A 1 42  ? -2.460  24.168  -11.411 1.00 54.57  ? 42   VAL A O   1 
ATOM   295  C  CB  . VAL A 1 42  ? 0.615   23.849  -11.184 1.00 49.08  ? 42   VAL A CB  1 
ATOM   296  C  CG1 . VAL A 1 42  ? 0.520   22.961  -12.430 1.00 43.13  ? 42   VAL A CG1 1 
ATOM   297  C  CG2 . VAL A 1 42  ? 2.064   24.237  -10.874 1.00 52.96  ? 42   VAL A CG2 1 
ATOM   298  N  N   . GLU A 1 43  ? -1.610  24.906  -13.357 0.80 44.64  ? 43   GLU A N   1 
ATOM   299  C  CA  . GLU A 1 43  ? -2.725  24.413  -14.156 0.80 40.54  ? 43   GLU A CA  1 
ATOM   300  C  C   . GLU A 1 43  ? -2.208  23.999  -15.529 0.80 43.71  ? 43   GLU A C   1 
ATOM   301  O  O   . GLU A 1 43  ? -1.585  24.786  -16.232 0.80 38.56  ? 43   GLU A O   1 
ATOM   302  C  CB  . GLU A 1 43  ? -3.832  25.467  -14.275 0.80 40.68  ? 43   GLU A CB  1 
ATOM   303  C  CG  . GLU A 1 43  ? -5.254  24.959  -13.952 0.80 51.47  ? 43   GLU A CG  1 
ATOM   304  C  CD  . GLU A 1 43  ? -5.730  25.397  -12.579 0.80 64.76  ? 43   GLU A CD  1 
ATOM   305  O  OE1 . GLU A 1 43  ? -5.128  24.961  -11.521 0.80 59.86  ? 43   GLU A OE1 1 
ATOM   306  O  OE2 . GLU A 1 43  ? -6.715  26.213  -12.554 0.80 63.45  ? 43   GLU A OE2 1 
ATOM   307  N  N   . ILE A 1 44  ? -2.446  22.744  -15.885 1.00 52.63  ? 44   ILE A N   1 
ATOM   308  C  CA  . ILE A 1 44  ? -2.041  22.204  -17.178 1.00 43.75  ? 44   ILE A CA  1 
ATOM   309  C  C   . ILE A 1 44  ? -2.870  22.846  -18.293 1.00 48.91  ? 44   ILE A C   1 
ATOM   310  O  O   . ILE A 1 44  ? -4.083  22.659  -18.370 1.00 53.96  ? 44   ILE A O   1 
ATOM   311  C  CB  . ILE A 1 44  ? -2.217  20.676  -17.205 1.00 43.66  ? 44   ILE A CB  1 
ATOM   312  C  CG1 . ILE A 1 44  ? -1.516  20.036  -15.994 1.00 45.12  ? 44   ILE A CG1 1 
ATOM   313  C  CG2 . ILE A 1 44  ? -1.684  20.087  -18.506 1.00 43.93  ? 44   ILE A CG2 1 
ATOM   314  C  CD1 . ILE A 1 44  ? 0.000   20.270  -15.944 1.00 47.88  ? 44   ILE A CD1 1 
ATOM   315  N  N   . GLY A 1 45  ? -2.207  23.610  -19.156 1.00 38.61  ? 45   GLY A N   1 
ATOM   316  C  CA  . GLY A 1 45  ? -2.892  24.390  -20.167 1.00 31.09  ? 45   GLY A CA  1 
ATOM   317  C  C   . GLY A 1 45  ? -3.398  23.616  -21.365 1.00 33.30  ? 45   GLY A C   1 
ATOM   318  O  O   . GLY A 1 45  ? -3.977  24.207  -22.264 1.00 45.87  ? 45   GLY A O   1 
ATOM   319  N  N   . GLU A 1 46  ? -3.192  22.301  -21.378 1.00 32.51  ? 46   GLU A N   1 
ATOM   320  C  CA  . GLU A 1 46  ? -3.654  21.438  -22.466 1.00 35.44  ? 46   GLU A CA  1 
ATOM   321  C  C   . GLU A 1 46  ? -3.931  20.024  -21.947 1.00 42.42  ? 46   GLU A C   1 
ATOM   322  O  O   . GLU A 1 46  ? -3.456  19.640  -20.879 1.00 29.19  ? 46   GLU A O   1 
ATOM   323  C  CB  . GLU A 1 46  ? -2.596  21.359  -23.562 1.00 36.19  ? 46   GLU A CB  1 
ATOM   324  C  CG  . GLU A 1 46  ? -1.249  20.850  -23.049 1.00 38.42  ? 46   GLU A CG  1 
ATOM   325  C  CD  . GLU A 1 46  ? -0.134  20.958  -24.089 1.00 53.03  ? 46   GLU A CD  1 
ATOM   326  O  OE1 . GLU A 1 46  ? 0.295   19.908  -24.624 1.00 54.35  ? 46   GLU A OE1 1 
ATOM   327  O  OE2 . GLU A 1 46  ? 0.326   22.092  -24.355 1.00 52.13  ? 46   GLU A OE2 1 
ATOM   328  N  N   . SER A 1 47  ? -4.702  19.256  -22.715 1.00 37.07  ? 47   SER A N   1 
ATOM   329  C  CA  . SER A 1 47  ? -5.022  17.878  -22.369 1.00 38.11  ? 47   SER A CA  1 
ATOM   330  C  C   . SER A 1 47  ? -3.765  17.021  -22.357 1.00 38.79  ? 47   SER A C   1 
ATOM   331  O  O   . SER A 1 47  ? -2.930  17.140  -23.251 1.00 28.63  ? 47   SER A O   1 
ATOM   332  C  CB  . SER A 1 47  ? -6.022  17.291  -23.370 1.00 35.38  ? 47   SER A CB  1 
ATOM   333  O  OG  . SER A 1 47  ? -6.253  15.914  -23.111 1.00 42.51  ? 47   SER A OG  1 
ATOM   334  N  N   . VAL A 1 48  ? -3.629  16.157  -21.353 1.00 25.94  ? 48   VAL A N   1 
ATOM   335  C  CA  . VAL A 1 48  ? -2.546  15.178  -21.375 1.00 25.07  ? 48   VAL A CA  1 
ATOM   336  C  C   . VAL A 1 48  ? -3.114  13.774  -21.309 1.00 30.35  ? 48   VAL A C   1 
ATOM   337  O  O   . VAL A 1 48  ? -2.400  12.788  -21.076 1.00 23.71  ? 48   VAL A O   1 
ATOM   338  C  CB  . VAL A 1 48  ? -1.557  15.393  -20.243 1.00 29.70  ? 48   VAL A CB  1 
ATOM   339  C  CG1 . VAL A 1 48  ? -0.912  16.761  -20.409 1.00 29.16  ? 48   VAL A CG1 1 
ATOM   340  C  CG2 . VAL A 1 48  ? -2.261  15.218  -18.850 1.00 19.25  ? 48   VAL A CG2 1 
ATOM   341  N  N   . ARG A 1 49  ? -4.416  13.693  -21.537 1.00 31.39  ? 49   ARG A N   1 
ATOM   342  C  CA  . ARG A 1 49  ? -5.111  12.429  -21.408 1.00 38.46  ? 49   ARG A CA  1 
ATOM   343  C  C   . ARG A 1 49  ? -4.529  11.390  -22.342 1.00 40.96  ? 49   ARG A C   1 
ATOM   344  O  O   . ARG A 1 49  ? -4.511  11.578  -23.556 1.00 36.35  ? 49   ARG A O   1 
ATOM   345  C  CB  . ARG A 1 49  ? -6.589  12.624  -21.692 1.00 35.15  ? 49   ARG A CB  1 
ATOM   346  C  CG  . ARG A 1 49  ? -7.374  11.398  -21.457 1.00 31.69  ? 49   ARG A CG  1 
ATOM   347  C  CD  . ARG A 1 49  ? -8.809  11.635  -21.805 1.00 23.81  ? 49   ARG A CD  1 
ATOM   348  N  NE  . ARG A 1 49  ? -9.422  12.650  -20.966 1.00 26.41  ? 49   ARG A NE  1 
ATOM   349  C  CZ  . ARG A 1 49  ? -9.963  12.407  -19.771 1.00 29.96  ? 49   ARG A CZ  1 
ATOM   350  N  NH1 . ARG A 1 49  ? -9.950  11.185  -19.258 1.00 20.70  ? 49   ARG A NH1 1 
ATOM   351  N  NH2 . ARG A 1 49  ? -10.527 13.387  -19.100 1.00 24.96  ? 49   ARG A NH2 1 
ATOM   352  N  N   . GLY A 1 50  ? -4.036  10.300  -21.773 1.00 32.20  ? 50   GLY A N   1 
ATOM   353  C  CA  . GLY A 1 50  ? -3.509  9.202   -22.567 1.00 29.74  ? 50   GLY A CA  1 
ATOM   354  C  C   . GLY A 1 50  ? -2.106  9.430   -23.088 1.00 40.76  ? 50   GLY A C   1 
ATOM   355  O  O   . GLY A 1 50  ? -1.637  8.712   -23.966 1.00 41.60  ? 50   GLY A O   1 
ATOM   356  N  N   . GLU A 1 51  ? -1.418  10.425  -22.545 1.00 34.79  ? 51   GLU A N   1 
ATOM   357  C  CA  . GLU A 1 51  ? -0.093  10.757  -23.048 1.00 33.77  ? 51   GLU A CA  1 
ATOM   358  C  C   . GLU A 1 51  ? 1.023   10.430  -22.073 1.00 40.96  ? 51   GLU A C   1 
ATOM   359  O  O   . GLU A 1 51  ? 0.807   10.395  -20.857 1.00 36.71  ? 51   GLU A O   1 
ATOM   360  C  CB  . GLU A 1 51  ? -0.046  12.230  -23.406 1.00 43.23  ? 51   GLU A CB  1 
ATOM   361  C  CG  . GLU A 1 51  ? -0.939  12.555  -24.588 1.00 57.58  ? 51   GLU A CG  1 
ATOM   362  C  CD  . GLU A 1 51  ? -0.763  13.967  -25.053 1.00 68.06  ? 51   GLU A CD  1 
ATOM   363  O  OE1 . GLU A 1 51  ? -0.103  14.742  -24.328 1.00 71.26  ? 51   GLU A OE1 1 
ATOM   364  O  OE2 . GLU A 1 51  ? -1.279  14.297  -26.143 1.00 74.35  ? 51   GLU A OE2 1 
ATOM   365  N  N   . HIS A 1 52  ? 2.212   10.193  -22.620 1.00 28.26  ? 52   HIS A N   1 
ATOM   366  C  CA  . HIS A 1 52  ? 3.409   9.996   -21.831 1.00 33.34  ? 52   HIS A CA  1 
ATOM   367  C  C   . HIS A 1 52  ? 4.091   11.333  -21.579 1.00 35.31  ? 52   HIS A C   1 
ATOM   368  O  O   . HIS A 1 52  ? 4.684   11.941  -22.478 1.00 26.52  ? 52   HIS A O   1 
ATOM   369  C  CB  . HIS A 1 52  ? 4.344   9.027   -22.533 1.00 46.88  ? 52   HIS A CB  1 
ATOM   370  C  CG  . HIS A 1 52  ? 3.778   7.649   -22.662 1.00 59.90  ? 52   HIS A CG  1 
ATOM   371  N  ND1 . HIS A 1 52  ? 2.607   7.387   -23.339 1.00 71.31  ? 52   HIS A ND1 1 
ATOM   372  C  CD2 . HIS A 1 52  ? 4.213   6.459   -22.187 1.00 59.94  ? 52   HIS A CD2 1 
ATOM   373  C  CE1 . HIS A 1 52  ? 2.350   6.092   -23.284 1.00 69.14  ? 52   HIS A CE1 1 
ATOM   374  N  NE2 . HIS A 1 52  ? 3.308   5.507   -22.588 1.00 61.12  ? 52   HIS A NE2 1 
ATOM   375  N  N   . VAL A 1 53  ? 3.980   11.788  -20.340 1.00 26.40  ? 53   VAL A N   1 
ATOM   376  C  CA  . VAL A 1 53  ? 4.439   13.110  -19.949 1.00 29.09  ? 53   VAL A CA  1 
ATOM   377  C  C   . VAL A 1 53  ? 5.807   13.049  -19.287 1.00 33.63  ? 53   VAL A C   1 
ATOM   378  O  O   . VAL A 1 53  ? 6.100   12.125  -18.525 1.00 32.65  ? 53   VAL A O   1 
ATOM   379  C  CB  . VAL A 1 53  ? 3.434   13.754  -18.984 1.00 30.00  ? 53   VAL A CB  1 
ATOM   380  C  CG1 . VAL A 1 53  ? 3.867   15.144  -18.610 1.00 28.50  ? 53   VAL A CG1 1 
ATOM   381  C  CG2 . VAL A 1 53  ? 2.054   13.779  -19.628 1.00 36.11  ? 53   VAL A CG2 1 
ATOM   382  N  N   . TYR A 1 54  ? 6.645   14.031  -19.609 1.00 31.70  ? 54   TYR A N   1 
ATOM   383  C  CA  . TYR A 1 54  ? 7.923   14.222  -18.943 1.00 24.33  ? 54   TYR A CA  1 
ATOM   384  C  C   . TYR A 1 54  ? 7.910   15.607  -18.342 1.00 35.66  ? 54   TYR A C   1 
ATOM   385  O  O   . TYR A 1 54  ? 7.700   16.592  -19.054 1.00 38.80  ? 54   TYR A O   1 
ATOM   386  C  CB  . TYR A 1 54  ? 9.084   14.125  -19.939 1.00 27.52  ? 54   TYR A CB  1 
ATOM   387  C  CG  . TYR A 1 54  ? 9.350   12.715  -20.399 1.00 34.86  ? 54   TYR A CG  1 
ATOM   388  C  CD1 . TYR A 1 54  ? 8.470   12.077  -21.271 1.00 28.92  ? 54   TYR A CD1 1 
ATOM   389  C  CD2 . TYR A 1 54  ? 10.472  12.009  -19.951 1.00 25.29  ? 54   TYR A CD2 1 
ATOM   390  C  CE1 . TYR A 1 54  ? 8.698   10.771  -21.698 1.00 30.31  ? 54   TYR A CE1 1 
ATOM   391  C  CE2 . TYR A 1 54  ? 10.710  10.708  -20.380 1.00 29.91  ? 54   TYR A CE2 1 
ATOM   392  C  CZ  . TYR A 1 54  ? 9.815   10.094  -21.253 1.00 39.53  ? 54   TYR A CZ  1 
ATOM   393  O  OH  . TYR A 1 54  ? 10.035  8.805   -21.694 1.00 49.46  ? 54   TYR A OH  1 
ATOM   394  N  N   . ILE A 1 55  ? 8.115   15.684  -17.030 1.00 33.31  ? 55   ILE A N   1 
ATOM   395  C  CA  . ILE A 1 55  ? 8.217   16.974  -16.380 1.00 31.40  ? 55   ILE A CA  1 
ATOM   396  C  C   . ILE A 1 55  ? 9.663   17.198  -15.976 1.00 32.86  ? 55   ILE A C   1 
ATOM   397  O  O   . ILE A 1 55  ? 10.236  16.395  -15.251 1.00 45.03  ? 55   ILE A O   1 
ATOM   398  C  CB  . ILE A 1 55  ? 7.288   17.068  -15.161 1.00 28.63  ? 55   ILE A CB  1 
ATOM   399  C  CG1 . ILE A 1 55  ? 5.840   16.963  -15.629 1.00 20.87  ? 55   ILE A CG1 1 
ATOM   400  C  CG2 . ILE A 1 55  ? 7.520   18.405  -14.396 1.00 17.86  ? 55   ILE A CG2 1 
ATOM   401  C  CD1 . ILE A 1 55  ? 4.895   16.452  -14.585 1.00 34.33  ? 55   ILE A CD1 1 
ATOM   402  N  N   . VAL A 1 56  ? 10.256  18.280  -16.472 1.00 27.21  ? 56   VAL A N   1 
ATOM   403  C  CA  . VAL A 1 56  ? 11.642  18.580  -16.176 1.00 29.19  ? 56   VAL A CA  1 
ATOM   404  C  C   . VAL A 1 56  ? 11.665  19.540  -15.009 1.00 38.24  ? 56   VAL A C   1 
ATOM   405  O  O   . VAL A 1 56  ? 11.152  20.649  -15.133 1.00 31.33  ? 56   VAL A O   1 
ATOM   406  C  CB  . VAL A 1 56  ? 12.329  19.231  -17.369 1.00 34.30  ? 56   VAL A CB  1 
ATOM   407  C  CG1 . VAL A 1 56  ? 13.820  19.411  -17.089 1.00 37.12  ? 56   VAL A CG1 1 
ATOM   408  C  CG2 . VAL A 1 56  ? 12.147  18.376  -18.569 1.00 35.03  ? 56   VAL A CG2 1 
ATOM   409  N  N   . GLN A 1 57  ? 12.219  19.108  -13.873 1.00 43.98  ? 57   GLN A N   1 
ATOM   410  C  CA  . GLN A 1 57  ? 12.244  19.939  -12.666 1.00 46.55  ? 57   GLN A CA  1 
ATOM   411  C  C   . GLN A 1 57  ? 12.929  21.256  -12.968 1.00 43.33  ? 57   GLN A C   1 
ATOM   412  O  O   . GLN A 1 57  ? 13.908  21.299  -13.720 1.00 44.67  ? 57   GLN A O   1 
ATOM   413  C  CB  . GLN A 1 57  ? 13.001  19.253  -11.523 1.00 51.17  ? 57   GLN A CB  1 
ATOM   414  C  CG  . GLN A 1 57  ? 14.514  19.238  -11.737 1.00 67.44  ? 57   GLN A CG  1 
ATOM   415  C  CD  . GLN A 1 57  ? 15.323  19.387  -10.450 1.00 76.83  ? 57   GLN A CD  1 
ATOM   416  O  OE1 . GLN A 1 57  ? 14.770  19.422  -9.346  1.00 74.24  ? 57   GLN A OE1 1 
ATOM   417  N  NE2 . GLN A 1 57  ? 16.643  19.484  -10.595 1.00 75.90  ? 57   GLN A NE2 1 
ATOM   418  N  N   . SER A 1 58  ? 12.426  22.324  -12.351 1.00 43.82  ? 58   SER A N   1 
ATOM   419  C  CA  . SER A 1 58  ? 12.946  23.675  -12.555 1.00 56.80  ? 58   SER A CA  1 
ATOM   420  C  C   . SER A 1 58  ? 14.342  23.918  -11.980 1.00 49.99  ? 58   SER A C   1 
ATOM   421  O  O   . SER A 1 58  ? 15.010  23.004  -11.497 1.00 61.30  ? 58   SER A O   1 
ATOM   422  C  CB  . SER A 1 58  ? 11.994  24.688  -11.934 1.00 68.72  ? 58   SER A CB  1 
ATOM   423  O  OG  . SER A 1 58  ? 12.316  24.924  -10.575 1.00 77.28  ? 58   SER A OG  1 
ATOM   424  N  N   . GLY A 1 59  ? 14.775  25.169  -12.043 0.60 49.35  ? 59   GLY A N   1 
ATOM   425  C  CA  . GLY A 1 59  ? 16.047  25.563  -11.472 0.60 62.56  ? 59   GLY A CA  1 
ATOM   426  C  C   . GLY A 1 59  ? 15.883  26.857  -10.706 0.60 72.33  ? 59   GLY A C   1 
ATOM   427  O  O   . GLY A 1 59  ? 16.822  27.642  -10.585 0.60 72.57  ? 59   GLY A O   1 
ATOM   428  N  N   . CYS A 1 60  ? 14.677  27.074  -10.188 0.50 78.63  ? 60   CYS A N   1 
ATOM   429  C  CA  . CYS A 1 60  ? 14.340  28.311  -9.489  0.50 79.65  ? 60   CYS A CA  1 
ATOM   430  C  C   . CYS A 1 60  ? 14.997  28.430  -8.121  0.50 78.05  ? 60   CYS A C   1 
ATOM   431  O  O   . CYS A 1 60  ? 14.535  29.190  -7.272  0.50 81.79  ? 60   CYS A O   1 
ATOM   432  C  CB  . CYS A 1 60  ? 12.823  28.468  -9.361  0.50 79.82  ? 60   CYS A CB  1 
ATOM   433  S  SG  . CYS A 1 60  ? 12.128  29.762  -10.414 0.50 83.13  ? 60   CYS A SG  1 
ATOM   434  N  N   . GLY A 1 61  ? 16.067  27.670  -7.911  1.00 69.72  ? 61   GLY A N   1 
ATOM   435  C  CA  . GLY A 1 61  ? 16.894  27.805  -6.726  1.00 66.68  ? 61   GLY A CA  1 
ATOM   436  C  C   . GLY A 1 61  ? 16.276  27.353  -5.417  1.00 66.19  ? 61   GLY A C   1 
ATOM   437  O  O   . GLY A 1 61  ? 16.839  26.500  -4.728  1.00 73.37  ? 61   GLY A O   1 
ATOM   438  N  N   . GLU A 1 62  ? 15.124  27.927  -5.071  1.00 49.20  ? 62   GLU A N   1 
ATOM   439  C  CA  . GLU A 1 62  ? 14.449  27.639  -3.812  1.00 43.92  ? 62   GLU A CA  1 
ATOM   440  C  C   . GLU A 1 62  ? 13.946  26.193  -3.839  1.00 33.41  ? 62   GLU A C   1 
ATOM   441  O  O   . GLU A 1 62  ? 12.969  25.878  -4.517  1.00 36.93  ? 62   GLU A O   1 
ATOM   442  C  CB  . GLU A 1 62  ? 13.294  28.632  -3.596  1.00 47.11  ? 62   GLU A CB  1 
ATOM   443  C  CG  . GLU A 1 62  ? 13.071  29.073  -2.141  1.00 48.45  ? 62   GLU A CG  1 
ATOM   444  C  CD  . GLU A 1 62  ? 12.502  27.960  -1.255  1.00 53.25  ? 62   GLU A CD  1 
ATOM   445  O  OE1 . GLU A 1 62  ? 12.288  26.834  -1.761  1.00 55.51  ? 62   GLU A OE1 1 
ATOM   446  O  OE2 . GLU A 1 62  ? 12.271  28.210  -0.052  1.00 46.27  ? 62   GLU A OE2 1 
ATOM   447  N  N   . ILE A 1 63  ? 14.619  25.322  -3.092  1.00 27.70  ? 63   ILE A N   1 
ATOM   448  C  CA  . ILE A 1 63  ? 14.490  23.875  -3.254  1.00 30.90  ? 63   ILE A CA  1 
ATOM   449  C  C   . ILE A 1 63  ? 13.125  23.312  -2.869  1.00 36.57  ? 63   ILE A C   1 
ATOM   450  O  O   . ILE A 1 63  ? 12.636  22.370  -3.499  1.00 38.35  ? 63   ILE A O   1 
ATOM   451  C  CB  . ILE A 1 63  ? 15.600  23.141  -2.475  1.00 36.58  ? 63   ILE A CB  1 
ATOM   452  C  CG1 . ILE A 1 63  ? 15.699  21.684  -2.902  1.00 43.58  ? 63   ILE A CG1 1 
ATOM   453  C  CG2 . ILE A 1 63  ? 15.357  23.218  -0.994  1.00 39.87  ? 63   ILE A CG2 1 
ATOM   454  C  CD1 . ILE A 1 63  ? 16.647  20.864  -2.025  1.00 51.30  ? 63   ILE A CD1 1 
ATOM   455  N  N   . ASN A 1 64  ? 12.505  23.885  -1.845  1.00 31.32  ? 64   ASN A N   1 
ATOM   456  C  CA  . ASN A 1 64  ? 11.185  23.434  -1.434  1.00 31.77  ? 64   ASN A CA  1 
ATOM   457  C  C   . ASN A 1 64  ? 10.057  23.903  -2.374  1.00 35.30  ? 64   ASN A C   1 
ATOM   458  O  O   . ASN A 1 64  ? 9.054   23.198  -2.580  1.00 30.09  ? 64   ASN A O   1 
ATOM   459  C  CB  . ASN A 1 64  ? 10.920  23.851  0.008   1.00 28.68  ? 64   ASN A CB  1 
ATOM   460  C  CG  . ASN A 1 64  ? 11.922  23.248  0.969   1.00 32.62  ? 64   ASN A CG  1 
ATOM   461  O  OD1 . ASN A 1 64  ? 12.320  22.088  0.823   1.00 30.30  ? 64   ASN A OD1 1 
ATOM   462  N  ND2 . ASN A 1 64  ? 12.353  24.039  1.954   1.00 27.74  ? 64   ASN A ND2 1 
ATOM   463  N  N   . ASP A 1 65  ? 10.225  25.096  -2.932  1.00 25.14  ? 65   ASP A N   1 
ATOM   464  C  CA  . ASP A 1 65  ? 9.319   25.599  -3.962  1.00 28.05  ? 65   ASP A CA  1 
ATOM   465  C  C   . ASP A 1 65  ? 9.426   24.738  -5.217  1.00 31.11  ? 65   ASP A C   1 
ATOM   466  O  O   . ASP A 1 65  ? 8.421   24.323  -5.778  1.00 30.58  ? 65   ASP A O   1 
ATOM   467  C  CB  . ASP A 1 65  ? 9.647   27.057  -4.295  1.00 25.53  ? 65   ASP A CB  1 
ATOM   468  C  CG  . ASP A 1 65  ? 9.331   27.998  -3.133  1.00 33.14  ? 65   ASP A CG  1 
ATOM   469  O  OD1 . ASP A 1 65  ? 8.440   27.662  -2.320  1.00 32.75  ? 65   ASP A OD1 1 
ATOM   470  O  OD2 . ASP A 1 65  ? 9.962   29.070  -3.029  1.00 35.49  ? 65   ASP A OD2 1 
ATOM   471  N  N   . ASN A 1 66  ? 10.654  24.458  -5.634  1.00 26.71  ? 66   ASN A N   1 
ATOM   472  C  CA  . ASN A 1 66  ? 10.878  23.606  -6.784  1.00 34.06  ? 66   ASN A CA  1 
ATOM   473  C  C   . ASN A 1 66  ? 10.284  22.235  -6.573  1.00 29.76  ? 66   ASN A C   1 
ATOM   474  O  O   . ASN A 1 66  ? 9.631   21.697  -7.463  1.00 31.31  ? 66   ASN A O   1 
ATOM   475  C  CB  . ASN A 1 66  ? 12.369  23.496  -7.085  1.00 36.73  ? 66   ASN A CB  1 
ATOM   476  C  CG  . ASN A 1 66  ? 12.918  24.751  -7.735  1.00 57.74  ? 66   ASN A CG  1 
ATOM   477  O  OD1 . ASN A 1 66  ? 12.211  25.752  -7.886  1.00 51.44  ? 66   ASN A OD1 1 
ATOM   478  N  ND2 . ASN A 1 66  ? 14.189  24.702  -8.128  1.00 72.74  ? 66   ASN A ND2 1 
ATOM   479  N  N   . LEU A 1 67  ? 10.487  21.670  -5.386  1.00 28.81  ? 67   LEU A N   1 
ATOM   480  C  CA  . LEU A 1 67  ? 10.014  20.318  -5.128  1.00 24.60  ? 67   LEU A CA  1 
ATOM   481  C  C   . LEU A 1 67  ? 8.489   20.263  -5.075  1.00 21.84  ? 67   LEU A C   1 
ATOM   482  O  O   . LEU A 1 67  ? 7.881   19.362  -5.651  1.00 22.06  ? 67   LEU A O   1 
ATOM   483  C  CB  . LEU A 1 67  ? 10.666  19.729  -3.869  1.00 24.27  ? 67   LEU A CB  1 
ATOM   484  C  CG  . LEU A 1 67  ? 10.163  18.360  -3.405  1.00 23.20  ? 67   LEU A CG  1 
ATOM   485  C  CD1 . LEU A 1 67  ? 10.532  17.269  -4.386  1.00 19.08  ? 67   LEU A CD1 1 
ATOM   486  C  CD2 . LEU A 1 67  ? 10.728  18.041  -2.028  1.00 26.72  ? 67   LEU A CD2 1 
ATOM   487  N  N   . MET A 1 68  ? 7.853   21.235  -4.428  1.00 24.06  ? 68   MET A N   1 
ATOM   488  C  CA  . MET A 1 68  ? 6.387   21.242  -4.413  1.00 24.46  ? 68   MET A CA  1 
ATOM   489  C  C   . MET A 1 68  ? 5.789   21.449  -5.810  1.00 25.23  ? 68   MET A C   1 
ATOM   490  O  O   . MET A 1 68  ? 4.812   20.802  -6.183  1.00 30.69  ? 68   MET A O   1 
ATOM   491  C  CB  . MET A 1 68  ? 5.843   22.299  -3.464  1.00 20.99  ? 68   MET A CB  1 
ATOM   492  C  CG  . MET A 1 68  ? 6.028   21.960  -2.002  1.00 47.39  ? 68   MET A CG  1 
ATOM   493  S  SD  . MET A 1 68  ? 5.366   20.328  -1.634  1.00 67.58  ? 68   MET A SD  1 
ATOM   494  C  CE  . MET A 1 68  ? 3.728   20.524  -2.326  1.00 15.56  ? 68   MET A CE  1 
ATOM   495  N  N   . GLU A 1 69  ? 6.369   22.357  -6.579  1.00 25.05  ? 69   GLU A N   1 
ATOM   496  C  CA  . GLU A 1 69  ? 5.895   22.573  -7.943  1.00 30.65  ? 69   GLU A CA  1 
ATOM   497  C  C   . GLU A 1 69  ? 5.986   21.284  -8.777  1.00 26.72  ? 69   GLU A C   1 
ATOM   498  O  O   . GLU A 1 69  ? 5.057   20.945  -9.517  1.00 26.35  ? 69   GLU A O   1 
ATOM   499  C  CB  . GLU A 1 69  ? 6.633   23.743  -8.619  1.00 23.94  ? 69   GLU A CB  1 
ATOM   500  C  CG  . GLU A 1 69  ? 6.007   24.124  -9.970  1.00 42.44  ? 69   GLU A CG  1 
ATOM   501  C  CD  . GLU A 1 69  ? 6.773   25.201  -10.730 1.00 55.40  ? 69   GLU A CD  1 
ATOM   502  O  OE1 . GLU A 1 69  ? 7.943   25.474  -10.380 1.00 57.37  ? 69   GLU A OE1 1 
ATOM   503  O  OE2 . GLU A 1 69  ? 6.199   25.773  -11.684 1.00 62.55  ? 69   GLU A OE2 1 
ATOM   504  N  N   . LEU A 1 70  ? 7.090   20.555  -8.628  1.00 26.42  ? 70   LEU A N   1 
ATOM   505  C  CA  . LEU A 1 70  ? 7.264   19.274  -9.318  1.00 29.00  ? 70   LEU A CA  1 
ATOM   506  C  C   . LEU A 1 70  ? 6.201   18.270  -8.897  1.00 35.60  ? 70   LEU A C   1 
ATOM   507  O  O   . LEU A 1 70  ? 5.559   17.640  -9.746  1.00 28.45  ? 70   LEU A O   1 
ATOM   508  C  CB  . LEU A 1 70  ? 8.650   18.706  -9.037  1.00 27.99  ? 70   LEU A CB  1 
ATOM   509  C  CG  . LEU A 1 70  ? 9.058   17.363  -9.644  1.00 30.94  ? 70   LEU A CG  1 
ATOM   510  C  CD1 . LEU A 1 70  ? 9.030   17.391  -11.153 1.00 27.12  ? 70   LEU A CD1 1 
ATOM   511  C  CD2 . LEU A 1 70  ? 10.447  17.003  -9.184  1.00 32.96  ? 70   LEU A CD2 1 
ATOM   512  N  N   . LEU A 1 71  ? 6.008   18.121  -7.584  1.00 24.37  ? 71   LEU A N   1 
ATOM   513  C  CA  . LEU A 1 71  ? 5.009   17.196  -7.076  1.00 21.04  ? 71   LEU A CA  1 
ATOM   514  C  C   . LEU A 1 71  ? 3.607   17.545  -7.560  1.00 25.20  ? 71   LEU A C   1 
ATOM   515  O  O   . LEU A 1 71  ? 2.826   16.669  -7.938  1.00 24.25  ? 71   LEU A O   1 
ATOM   516  C  CB  . LEU A 1 71  ? 5.019   17.200  -5.555  1.00 25.07  ? 71   LEU A CB  1 
ATOM   517  C  CG  . LEU A 1 71  ? 6.324   16.716  -4.929  1.00 25.10  ? 71   LEU A CG  1 
ATOM   518  C  CD1 . LEU A 1 71  ? 6.276   16.889  -3.416  1.00 24.43  ? 71   LEU A CD1 1 
ATOM   519  C  CD2 . LEU A 1 71  ? 6.543   15.261  -5.303  1.00 18.74  ? 71   LEU A CD2 1 
ATOM   520  N  N   . ILE A 1 72  ? 3.287   18.831  -7.534  1.00 25.33  ? 72   ILE A N   1 
ATOM   521  C  CA  . ILE A 1 72  ? 1.977   19.297  -7.964  1.00 30.18  ? 72   ILE A CA  1 
ATOM   522  C  C   . ILE A 1 72  ? 1.746   19.090  -9.465  1.00 27.47  ? 72   ILE A C   1 
ATOM   523  O  O   . ILE A 1 72  ? 0.648   18.731  -9.899  1.00 29.60  ? 72   ILE A O   1 
ATOM   524  C  CB  . ILE A 1 72  ? 1.777   20.764  -7.586  1.00 32.70  ? 72   ILE A CB  1 
ATOM   525  C  CG1 . ILE A 1 72  ? 1.650   20.888  -6.071  1.00 28.88  ? 72   ILE A CG1 1 
ATOM   526  C  CG2 . ILE A 1 72  ? 0.532   21.327  -8.259  1.00 23.97  ? 72   ILE A CG2 1 
ATOM   527  C  CD1 . ILE A 1 72  ? 1.769   22.302  -5.564  1.00 33.84  ? 72   ILE A CD1 1 
ATOM   528  N  N   . MET A 1 73  ? 2.778   19.298  -10.268 1.00 23.72  ? 73   MET A N   1 
ATOM   529  C  CA  . MET A 1 73  ? 2.641   19.008  -11.685 1.00 26.34  ? 73   MET A CA  1 
ATOM   530  C  C   . MET A 1 73  ? 2.421   17.529  -11.927 1.00 33.43  ? 73   MET A C   1 
ATOM   531  O  O   . MET A 1 73  ? 1.489   17.157  -12.650 1.00 32.60  ? 73   MET A O   1 
ATOM   532  C  CB  . MET A 1 73  ? 3.841   19.524  -12.462 1.00 20.24  ? 73   MET A CB  1 
ATOM   533  C  CG  . MET A 1 73  ? 3.797   21.026  -12.572 1.00 30.20  ? 73   MET A CG  1 
ATOM   534  S  SD  . MET A 1 73  ? 5.044   21.670  -13.680 1.00 53.01  ? 73   MET A SD  1 
ATOM   535  C  CE  . MET A 1 73  ? 4.457   20.932  -15.195 1.00 36.71  ? 73   MET A CE  1 
ATOM   536  N  N   . ILE A 1 74  ? 3.260   16.686  -11.318 1.00 24.80  ? 74   ILE A N   1 
ATOM   537  C  CA  . ILE A 1 74  ? 3.091   15.250  -11.448 1.00 19.77  ? 74   ILE A CA  1 
ATOM   538  C  C   . ILE A 1 74  ? 1.667   14.929  -11.057 1.00 24.02  ? 74   ILE A C   1 
ATOM   539  O  O   . ILE A 1 74  ? 0.968   14.234  -11.776 1.00 30.64  ? 74   ILE A O   1 
ATOM   540  C  CB  . ILE A 1 74  ? 4.072   14.429  -10.567 1.00 27.44  ? 74   ILE A CB  1 
ATOM   541  C  CG1 . ILE A 1 74  ? 5.526   14.690  -10.964 1.00 25.13  ? 74   ILE A CG1 1 
ATOM   542  C  CG2 . ILE A 1 74  ? 3.803   12.951  -10.726 1.00 22.99  ? 74   ILE A CG2 1 
ATOM   543  C  CD1 . ILE A 1 74  ? 6.531   14.417  -9.838  1.00 20.70  ? 74   ILE A CD1 1 
ATOM   544  N  N   . ASN A 1 75  ? 1.207   15.453  -9.930  1.00 28.91  ? 75   ASN A N   1 
ATOM   545  C  CA  . ASN A 1 75  ? -0.149  15.121  -9.518  1.00 28.87  ? 75   ASN A CA  1 
ATOM   546  C  C   . ASN A 1 75  ? -1.210  15.570  -10.522 1.00 34.26  ? 75   ASN A C   1 
ATOM   547  O  O   . ASN A 1 75  ? -2.137  14.814  -10.848 1.00 24.92  ? 75   ASN A O   1 
ATOM   548  C  CB  . ASN A 1 75  ? -0.482  15.701  -8.150  1.00 28.67  ? 75   ASN A CB  1 
ATOM   549  C  CG  . ASN A 1 75  ? -1.851  15.272  -7.680  1.00 34.65  ? 75   ASN A CG  1 
ATOM   550  O  OD1 . ASN A 1 75  ? -2.782  16.078  -7.592  1.00 46.73  ? 75   ASN A OD1 1 
ATOM   551  N  ND2 . ASN A 1 75  ? -1.993  13.981  -7.421  1.00 31.77  ? 75   ASN A ND2 1 
ATOM   552  N  N   . ALA A 1 76  ? -1.091  16.815  -10.983 1.00 29.94  ? 76   ALA A N   1 
ATOM   553  C  CA  . ALA A 1 76  ? -2.084  17.375  -11.890 1.00 22.27  ? 76   ALA A CA  1 
ATOM   554  C  C   . ALA A 1 76  ? -2.195  16.520  -13.143 1.00 22.68  ? 76   ALA A C   1 
ATOM   555  O  O   . ALA A 1 76  ? -3.293  16.344  -13.669 1.00 26.61  ? 76   ALA A O   1 
ATOM   556  C  CB  . ALA A 1 76  ? -1.745  18.836  -12.254 1.00 25.05  ? 76   ALA A CB  1 
ATOM   557  N  N   . CYS A 1 77  ? -1.070  15.969  -13.598 1.00 25.89  ? 77   CYS A N   1 
ATOM   558  C  CA  . CYS A 1 77  ? -1.049  15.173  -14.831 1.00 32.66  ? 77   CYS A CA  1 
ATOM   559  C  C   . CYS A 1 77  ? -1.689  13.817  -14.611 1.00 37.97  ? 77   CYS A C   1 
ATOM   560  O  O   . CYS A 1 77  ? -2.478  13.359  -15.435 1.00 35.57  ? 77   CYS A O   1 
ATOM   561  C  CB  . CYS A 1 77  ? 0.371   14.998  -15.377 1.00 21.88  ? 77   CYS A CB  1 
ATOM   562  S  SG  . CYS A 1 77  ? 1.087   16.487  -16.119 1.00 29.94  ? 77   CYS A SG  1 
ATOM   563  N  N   . LYS A 1 78  ? -1.352  13.188  -13.489 1.00 32.77  ? 78   LYS A N   1 
ATOM   564  C  CA  . LYS A 1 78  ? -1.918  11.897  -13.116 1.00 30.32  ? 78   LYS A CA  1 
ATOM   565  C  C   . LYS A 1 78  ? -3.447  11.921  -13.046 1.00 25.81  ? 78   LYS A C   1 
ATOM   566  O  O   . LYS A 1 78  ? -4.123  11.083  -13.636 1.00 38.21  ? 78   LYS A O   1 
ATOM   567  C  CB  . LYS A 1 78  ? -1.339  11.432  -11.777 1.00 33.74  ? 78   LYS A CB  1 
ATOM   568  C  CG  . LYS A 1 78  ? -0.816  10.005  -11.813 1.00 52.55  ? 78   LYS A CG  1 
ATOM   569  C  CD  . LYS A 1 78  ? 0.074   9.808   -13.039 1.00 58.03  ? 78   LYS A CD  1 
ATOM   570  C  CE  . LYS A 1 78  ? 0.279   8.342   -13.380 1.00 58.38  ? 78   LYS A CE  1 
ATOM   571  N  NZ  . LYS A 1 78  ? 0.921   7.583   -12.273 1.00 59.41  ? 78   LYS A NZ  1 
ATOM   572  N  N   . ILE A 1 79  ? -4.005  12.889  -12.340 1.00 28.52  ? 79   ILE A N   1 
ATOM   573  C  CA  . ILE A 1 79  ? -5.461  12.958  -12.242 1.00 35.01  ? 79   ILE A CA  1 
ATOM   574  C  C   . ILE A 1 79  ? -6.114  13.492  -13.525 1.00 34.93  ? 79   ILE A C   1 
ATOM   575  O  O   . ILE A 1 79  ? -7.349  13.461  -13.667 1.00 30.77  ? 79   ILE A O   1 
ATOM   576  C  CB  . ILE A 1 79  ? -5.908  13.773  -11.011 1.00 40.86  ? 79   ILE A CB  1 
ATOM   577  C  CG1 . ILE A 1 79  ? -5.584  15.252  -11.193 1.00 42.05  ? 79   ILE A CG1 1 
ATOM   578  C  CG2 . ILE A 1 79  ? -5.243  13.223  -9.750  1.00 43.84  ? 79   ILE A CG2 1 
ATOM   579  C  CD1 . ILE A 1 79  ? -6.109  16.125  -10.065 1.00 48.83  ? 79   ILE A CD1 1 
ATOM   580  N  N   . ALA A 1 80  ? -5.287  13.981  -14.452 1.00 29.89  ? 80   ALA A N   1 
ATOM   581  C  CA  . ALA A 1 80  ? -5.768  14.369  -15.781 1.00 34.85  ? 80   ALA A CA  1 
ATOM   582  C  C   . ALA A 1 80  ? -5.611  13.204  -16.743 1.00 39.28  ? 80   ALA A C   1 
ATOM   583  O  O   . ALA A 1 80  ? -5.694  13.382  -17.960 1.00 34.86  ? 80   ALA A O   1 
ATOM   584  C  CB  . ALA A 1 80  ? -5.027  15.580  -16.302 1.00 21.27  ? 80   ALA A CB  1 
ATOM   585  N  N   . SER A 1 81  ? -5.359  12.014  -16.196 1.00 30.49  ? 81   SER A N   1 
ATOM   586  C  CA  . SER A 1 81  ? -5.382  10.796  -17.003 1.00 29.56  ? 81   SER A CA  1 
ATOM   587  C  C   . SER A 1 81  ? -4.222  10.695  -17.989 1.00 31.75  ? 81   SER A C   1 
ATOM   588  O  O   . SER A 1 81  ? -4.332  10.021  -19.007 1.00 34.73  ? 81   SER A O   1 
ATOM   589  C  CB  . SER A 1 81  ? -6.711  10.667  -17.755 1.00 31.31  ? 81   SER A CB  1 
ATOM   590  O  OG  . SER A 1 81  ? -7.807  10.497  -16.864 1.00 28.59  ? 81   SER A OG  1 
ATOM   591  N  N   . ALA A 1 82  ? -3.107  11.357  -17.695 1.00 35.42  ? 82   ALA A N   1 
ATOM   592  C  CA  . ALA A 1 82  ? -1.883  11.040  -18.414 1.00 34.29  ? 82   ALA A CA  1 
ATOM   593  C  C   . ALA A 1 82  ? -1.678  9.548   -18.221 1.00 40.49  ? 82   ALA A C   1 
ATOM   594  O  O   . ALA A 1 82  ? -1.972  9.008   -17.156 1.00 39.67  ? 82   ALA A O   1 
ATOM   595  C  CB  . ALA A 1 82  ? -0.706  11.808  -17.859 1.00 23.80  ? 82   ALA A CB  1 
ATOM   596  N  N   . SER A 1 83  ? -1.175  8.870   -19.239 1.00 35.44  ? 83   SER A N   1 
ATOM   597  C  CA  . SER A 1 83  ? -1.025  7.431   -19.133 1.00 39.82  ? 83   SER A CA  1 
ATOM   598  C  C   . SER A 1 83  ? 0.261   7.095   -18.399 1.00 37.05  ? 83   SER A C   1 
ATOM   599  O  O   . SER A 1 83  ? 0.386   6.019   -17.808 1.00 41.32  ? 83   SER A O   1 
ATOM   600  C  CB  . SER A 1 83  ? -1.081  6.765   -20.516 1.00 46.02  ? 83   SER A CB  1 
ATOM   601  O  OG  . SER A 1 83  ? 0.194   6.714   -21.128 1.00 53.62  ? 83   SER A OG  1 
ATOM   602  N  N   . ARG A 1 84  ? 1.209   8.028   -18.402 1.00 33.30  ? 84   ARG A N   1 
ATOM   603  C  CA  . ARG A 1 84  ? 2.488   7.781   -17.751 1.00 30.37  ? 84   ARG A CA  1 
ATOM   604  C  C   . ARG A 1 84  ? 3.158   9.113   -17.446 1.00 39.29  ? 84   ARG A C   1 
ATOM   605  O  O   . ARG A 1 84  ? 3.057   10.057  -18.248 1.00 37.59  ? 84   ARG A O   1 
ATOM   606  C  CB  . ARG A 1 84  ? 3.354   6.908   -18.664 1.00 35.44  ? 84   ARG A CB  1 
ATOM   607  C  CG  . ARG A 1 84  ? 4.661   6.435   -18.098 1.00 42.38  ? 84   ARG A CG  1 
ATOM   608  C  CD  . ARG A 1 84  ? 5.140   5.175   -18.830 1.00 50.32  ? 84   ARG A CD  1 
ATOM   609  N  NE  . ARG A 1 84  ? 6.404   4.654   -18.290 1.00 54.29  ? 84   ARG A NE  1 
ATOM   610  C  CZ  . ARG A 1 84  ? 6.494   3.843   -17.235 1.00 61.00  ? 84   ARG A CZ  1 
ATOM   611  N  NH1 . ARG A 1 84  ? 5.393   3.464   -16.598 1.00 55.62  ? 84   ARG A NH1 1 
ATOM   612  N  NH2 . ARG A 1 84  ? 7.683   3.408   -16.812 1.00 62.92  ? 84   ARG A NH2 1 
ATOM   613  N  N   . VAL A 1 85  ? 3.805   9.216   -16.283 1.00 32.16  ? 85   VAL A N   1 
ATOM   614  C  CA  . VAL A 1 85  ? 4.502   10.458  -15.944 1.00 24.24  ? 85   VAL A CA  1 
ATOM   615  C  C   . VAL A 1 85  ? 5.919   10.217  -15.472 1.00 24.19  ? 85   VAL A C   1 
ATOM   616  O  O   . VAL A 1 85  ? 6.138   9.548   -14.483 1.00 28.41  ? 85   VAL A O   1 
ATOM   617  C  CB  . VAL A 1 85  ? 3.768   11.278  -14.869 1.00 27.68  ? 85   VAL A CB  1 
ATOM   618  C  CG1 . VAL A 1 85  ? 4.508   12.605  -14.623 1.00 24.88  ? 85   VAL A CG1 1 
ATOM   619  C  CG2 . VAL A 1 85  ? 2.325   11.522  -15.269 1.00 21.67  ? 85   VAL A CG2 1 
ATOM   620  N  N   . THR A 1 86  ? 6.885   10.774  -16.187 1.00 18.61  ? 86   THR A N   1 
ATOM   621  C  CA  . THR A 1 86  ? 8.277   10.611  -15.821 1.00 20.05  ? 86   THR A CA  1 
ATOM   622  C  C   . THR A 1 86  ? 8.796   11.914  -15.266 1.00 31.79  ? 86   THR A C   1 
ATOM   623  O  O   . THR A 1 86  ? 8.631   12.960  -15.889 1.00 25.06  ? 86   THR A O   1 
ATOM   624  C  CB  . THR A 1 86  ? 9.141   10.249  -17.033 1.00 24.81  ? 86   THR A CB  1 
ATOM   625  O  OG1 . THR A 1 86  ? 8.755   8.966   -17.527 1.00 32.93  ? 86   THR A OG1 1 
ATOM   626  C  CG2 . THR A 1 86  ? 10.613  10.229  -16.644 1.00 21.32  ? 86   THR A CG2 1 
ATOM   627  N  N   . ALA A 1 87  ? 9.418   11.864  -14.089 1.00 30.82  ? 87   ALA A N   1 
ATOM   628  C  CA  . ALA A 1 87  ? 10.046  13.058  -13.567 1.00 23.55  ? 87   ALA A CA  1 
ATOM   629  C  C   . ALA A 1 87  ? 11.511  13.076  -13.977 1.00 23.32  ? 87   ALA A C   1 
ATOM   630  O  O   . ALA A 1 87  ? 12.247  12.096  -13.791 1.00 26.64  ? 87   ALA A O   1 
ATOM   631  C  CB  . ALA A 1 87  ? 9.889   13.154  -12.050 1.00 25.45  ? 87   ALA A CB  1 
ATOM   632  N  N   . VAL A 1 88  ? 11.918  14.192  -14.566 1.00 22.24  ? 88   VAL A N   1 
ATOM   633  C  CA  . VAL A 1 88  ? 13.293  14.384  -14.996 1.00 24.50  ? 88   VAL A CA  1 
ATOM   634  C  C   . VAL A 1 88  ? 13.879  15.382  -14.031 1.00 24.57  ? 88   VAL A C   1 
ATOM   635  O  O   . VAL A 1 88  ? 13.470  16.525  -13.998 1.00 24.22  ? 88   VAL A O   1 
ATOM   636  C  CB  . VAL A 1 88  ? 13.381  14.964  -16.417 1.00 23.94  ? 88   VAL A CB  1 
ATOM   637  C  CG1 . VAL A 1 88  ? 14.847  15.096  -16.857 1.00 18.31  ? 88   VAL A CG1 1 
ATOM   638  C  CG2 . VAL A 1 88  ? 12.619  14.079  -17.400 1.00 26.49  ? 88   VAL A CG2 1 
ATOM   639  N  N   . ILE A 1 89  ? 14.824  14.934  -13.224 1.00 27.40  ? 89   ILE A N   1 
ATOM   640  C  CA  . ILE A 1 89  ? 15.319  15.742  -12.128 1.00 26.22  ? 89   ILE A CA  1 
ATOM   641  C  C   . ILE A 1 89  ? 16.833  15.687  -12.156 1.00 23.62  ? 89   ILE A C   1 
ATOM   642  O  O   . ILE A 1 89  ? 17.435  14.835  -11.512 1.00 27.27  ? 89   ILE A O   1 
ATOM   643  C  CB  . ILE A 1 89  ? 14.850  15.174  -10.787 1.00 38.70  ? 89   ILE A CB  1 
ATOM   644  C  CG1 . ILE A 1 89  ? 13.355  14.909  -10.809 1.00 33.12  ? 89   ILE A CG1 1 
ATOM   645  C  CG2 . ILE A 1 89  ? 15.212  16.111  -9.629  1.00 36.20  ? 89   ILE A CG2 1 
ATOM   646  C  CD1 . ILE A 1 89  ? 12.879  14.160  -9.561  1.00 31.09  ? 89   ILE A CD1 1 
ATOM   647  N  N   . PRO A 1 90  ? 17.454  16.604  -12.910 1.00 30.21  ? 90   PRO A N   1 
ATOM   648  C  CA  . PRO A 1 90  ? 18.905  16.599  -13.092 1.00 32.14  ? 90   PRO A CA  1 
ATOM   649  C  C   . PRO A 1 90  ? 19.632  16.568  -11.744 1.00 31.06  ? 90   PRO A C   1 
ATOM   650  O  O   . PRO A 1 90  ? 20.592  15.817  -11.608 1.00 41.16  ? 90   PRO A O   1 
ATOM   651  C  CB  . PRO A 1 90  ? 19.168  17.929  -13.813 1.00 30.36  ? 90   PRO A CB  1 
ATOM   652  C  CG  . PRO A 1 90  ? 17.877  18.263  -14.474 1.00 30.49  ? 90   PRO A CG  1 
ATOM   653  C  CD  . PRO A 1 90  ? 16.803  17.741  -13.590 1.00 28.57  ? 90   PRO A CD  1 
ATOM   654  N  N   . CYS A 1 91  ? 19.176  17.362  -10.775 1.00 30.53  ? 91   CYS A N   1 
ATOM   655  C  CA  . CYS A 1 91  ? 19.800  17.421  -9.453  1.00 35.46  ? 91   CYS A CA  1 
ATOM   656  C  C   . CYS A 1 91  ? 18.816  17.015  -8.321  1.00 35.82  ? 91   CYS A C   1 
ATOM   657  O  O   . CYS A 1 91  ? 17.967  17.793  -7.915  1.00 31.87  ? 91   CYS A O   1 
ATOM   658  C  CB  . CYS A 1 91  ? 20.390  18.817  -9.209  1.00 39.09  ? 91   CYS A CB  1 
ATOM   659  S  SG  . CYS A 1 91  ? 21.240  18.999  -7.597  1.00 45.14  ? 91   CYS A SG  1 
ATOM   660  N  N   . PHE A 1 92  ? 18.941  15.791  -7.820  1.00 27.74  ? 92   PHE A N   1 
ATOM   661  C  CA  . PHE A 1 92  ? 17.939  15.231  -6.925  1.00 29.94  ? 92   PHE A CA  1 
ATOM   662  C  C   . PHE A 1 92  ? 17.963  15.971  -5.593  1.00 30.52  ? 92   PHE A C   1 
ATOM   663  O  O   . PHE A 1 92  ? 18.982  15.972  -4.904  1.00 32.59  ? 92   PHE A O   1 
ATOM   664  C  CB  . PHE A 1 92  ? 18.210  13.744  -6.714  1.00 29.65  ? 92   PHE A CB  1 
ATOM   665  C  CG  . PHE A 1 92  ? 17.073  12.993  -6.057  1.00 35.00  ? 92   PHE A CG  1 
ATOM   666  C  CD1 . PHE A 1 92  ? 16.126  12.315  -6.827  1.00 30.48  ? 92   PHE A CD1 1 
ATOM   667  C  CD2 . PHE A 1 92  ? 16.968  12.938  -4.666  1.00 33.88  ? 92   PHE A CD2 1 
ATOM   668  C  CE1 . PHE A 1 92  ? 15.086  11.612  -6.226  1.00 34.47  ? 92   PHE A CE1 1 
ATOM   669  C  CE2 . PHE A 1 92  ? 15.920  12.236  -4.046  1.00 26.99  ? 92   PHE A CE2 1 
ATOM   670  C  CZ  . PHE A 1 92  ? 14.975  11.569  -4.831  1.00 31.94  ? 92   PHE A CZ  1 
ATOM   671  N  N   . PRO A 1 93  ? 16.843  16.616  -5.233  1.00 30.76  ? 93   PRO A N   1 
ATOM   672  C  CA  . PRO A 1 93  ? 16.804  17.410  -4.002  1.00 29.18  ? 93   PRO A CA  1 
ATOM   673  C  C   . PRO A 1 93  ? 16.942  16.516  -2.768  1.00 34.19  ? 93   PRO A C   1 
ATOM   674  O  O   . PRO A 1 93  ? 16.417  15.400  -2.758  1.00 36.35  ? 93   PRO A O   1 
ATOM   675  C  CB  . PRO A 1 93  ? 15.422  18.059  -4.052  1.00 35.36  ? 93   PRO A CB  1 
ATOM   676  C  CG  . PRO A 1 93  ? 14.609  17.176  -4.951  1.00 37.84  ? 93   PRO A CG  1 
ATOM   677  C  CD  . PRO A 1 93  ? 15.566  16.666  -5.970  1.00 35.85  ? 93   PRO A CD  1 
ATOM   678  N  N   . TYR A 1 94  ? 17.671  17.005  -1.765  1.00 33.50  ? 94   TYR A N   1 
ATOM   679  C  CA  . TYR A 1 94  ? 17.855  16.344  -0.465  1.00 25.45  ? 94   TYR A CA  1 
ATOM   680  C  C   . TYR A 1 94  ? 18.688  15.085  -0.586  1.00 25.70  ? 94   TYR A C   1 
ATOM   681  O  O   . TYR A 1 94  ? 18.747  14.285  0.330   1.00 29.43  ? 94   TYR A O   1 
ATOM   682  C  CB  . TYR A 1 94  ? 16.517  16.060  0.220   1.00 24.50  ? 94   TYR A CB  1 
ATOM   683  C  CG  . TYR A 1 94  ? 15.867  17.310  0.757   1.00 25.12  ? 94   TYR A CG  1 
ATOM   684  C  CD1 . TYR A 1 94  ? 14.996  18.041  -0.017  1.00 31.04  ? 94   TYR A CD1 1 
ATOM   685  C  CD2 . TYR A 1 94  ? 16.150  17.772  2.044   1.00 28.13  ? 94   TYR A CD2 1 
ATOM   686  C  CE1 . TYR A 1 94  ? 14.409  19.189  0.460   1.00 27.26  ? 94   TYR A CE1 1 
ATOM   687  C  CE2 . TYR A 1 94  ? 15.573  18.931  2.534   1.00 29.25  ? 94   TYR A CE2 1 
ATOM   688  C  CZ  . TYR A 1 94  ? 14.699  19.637  1.736   1.00 35.63  ? 94   TYR A CZ  1 
ATOM   689  O  OH  . TYR A 1 94  ? 14.101  20.789  2.203   1.00 31.95  ? 94   TYR A OH  1 
ATOM   690  N  N   . ALA A 1 95  ? 19.362  14.936  -1.722  1.00 27.23  ? 95   ALA A N   1 
ATOM   691  C  CA  . ALA A 1 95  ? 20.231  13.782  -1.952  1.00 25.33  ? 95   ALA A CA  1 
ATOM   692  C  C   . ALA A 1 95  ? 21.331  13.631  -0.902  1.00 22.08  ? 95   ALA A C   1 
ATOM   693  O  O   . ALA A 1 95  ? 21.737  12.514  -0.597  1.00 37.35  ? 95   ALA A O   1 
ATOM   694  C  CB  . ALA A 1 95  ? 20.846  13.827  -3.374  1.00 26.01  ? 95   ALA A CB  1 
ATOM   695  N  N   . ARG A 1 96  ? 21.828  14.733  -0.358  0.60 14.65  ? 96   ARG A N   1 
ATOM   696  C  CA  . ARG A 1 96  ? 22.818  14.631  0.701   0.60 22.60  ? 96   ARG A CA  1 
ATOM   697  C  C   . ARG A 1 96  ? 22.236  14.027  1.986   0.60 34.01  ? 96   ARG A C   1 
ATOM   698  O  O   . ARG A 1 96  ? 22.961  13.438  2.783   0.60 28.40  ? 96   ARG A O   1 
ATOM   699  C  CB  . ARG A 1 96  ? 23.476  15.983  0.964   0.60 28.07  ? 96   ARG A CB  1 
ATOM   700  C  CG  . ARG A 1 96  ? 24.559  16.315  -0.043  0.60 36.17  ? 96   ARG A CG  1 
ATOM   701  C  CD  . ARG A 1 96  ? 25.188  17.666  0.225   0.60 51.56  ? 96   ARG A CD  1 
ATOM   702  N  NE  . ARG A 1 96  ? 24.377  18.765  -0.295  0.60 58.19  ? 96   ARG A NE  1 
ATOM   703  C  CZ  . ARG A 1 96  ? 23.727  19.644  0.460   0.60 59.08  ? 96   ARG A CZ  1 
ATOM   704  N  NH1 . ARG A 1 96  ? 23.793  19.563  1.781   0.60 66.20  ? 96   ARG A NH1 1 
ATOM   705  N  NH2 . ARG A 1 96  ? 23.017  20.607  -0.107  0.60 50.79  ? 96   ARG A NH2 1 
ATOM   706  N  N   . GLN A 1 97  ? 20.924  14.161  2.174   0.84 40.81  ? 97   GLN A N   1 
ATOM   707  C  CA  . GLN A 1 97  ? 20.254  13.603  3.350   0.84 33.39  ? 97   GLN A CA  1 
ATOM   708  C  C   . GLN A 1 97  ? 19.763  12.197  3.053   0.84 24.65  ? 97   GLN A C   1 
ATOM   709  O  O   . GLN A 1 97  ? 18.568  11.956  2.914   0.84 25.42  ? 97   GLN A O   1 
ATOM   710  C  CB  . GLN A 1 97  ? 19.113  14.517  3.821   0.84 28.89  ? 97   GLN A CB  1 
ATOM   711  C  CG  . GLN A 1 97  ? 19.617  15.915  4.213   0.84 41.57  ? 97   GLN A CG  1 
ATOM   712  C  CD  . GLN A 1 97  ? 18.515  16.876  4.669   0.84 48.52  ? 97   GLN A CD  1 
ATOM   713  O  OE1 . GLN A 1 97  ? 17.538  16.477  5.309   0.84 40.63  ? 97   GLN A OE1 1 
ATOM   714  N  NE2 . GLN A 1 97  ? 18.680  18.154  4.340   0.84 54.13  ? 97   GLN A NE2 1 
ATOM   715  N  N   . ASP A 1 98  ? 20.713  11.273  2.950   1.00 30.99  ? 98   ASP A N   1 
ATOM   716  C  CA  . ASP A 1 98  ? 20.428  9.917   2.499   1.00 33.17  ? 98   ASP A CA  1 
ATOM   717  C  C   . ASP A 1 98  ? 20.812  8.829   3.512   1.00 37.80  ? 98   ASP A C   1 
ATOM   718  O  O   . ASP A 1 98  ? 20.755  7.631   3.199   1.00 29.25  ? 98   ASP A O   1 
ATOM   719  C  CB  . ASP A 1 98  ? 21.093  9.651   1.145   1.00 34.96  ? 98   ASP A CB  1 
ATOM   720  C  CG  . ASP A 1 98  ? 22.610  9.679   1.216   1.00 44.49  ? 98   ASP A CG  1 
ATOM   721  O  OD1 . ASP A 1 98  ? 23.169  10.382  2.083   1.00 52.53  ? 98   ASP A OD1 1 
ATOM   722  O  OD2 . ASP A 1 98  ? 23.245  9.005   0.386   1.00 42.49  ? 98   ASP A OD2 1 
ATOM   723  N  N   . LYS A 1 99  ? 21.191  9.252   4.716   1.00 32.68  ? 99   LYS A N   1 
ATOM   724  C  CA  . LYS A 1 99  ? 21.447  8.332   5.819   1.00 40.93  ? 99   LYS A CA  1 
ATOM   725  C  C   . LYS A 1 99  ? 21.356  9.074   7.149   1.00 34.52  ? 99   LYS A C   1 
ATOM   726  O  O   . LYS A 1 99  ? 21.326  10.300  7.176   1.00 35.12  ? 99   LYS A O   1 
ATOM   727  C  CB  . LYS A 1 99  ? 22.814  7.671   5.657   1.00 37.18  ? 99   LYS A CB  1 
ATOM   728  C  CG  . LYS A 1 99  ? 23.983  8.652   5.618   1.00 49.56  ? 99   LYS A CG  1 
ATOM   729  C  CD  . LYS A 1 99  ? 25.212  7.975   5.030   1.00 60.54  ? 99   LYS A CD  1 
ATOM   730  C  CE  . LYS A 1 99  ? 26.308  8.972   4.696   1.00 72.56  ? 99   LYS A CE  1 
ATOM   731  N  NZ  . LYS A 1 99  ? 27.451  8.299   3.988   1.00 79.08  ? 99   LYS A NZ  1 
ATOM   732  N  N   . LYS A 1 100 ? 21.283  8.330   8.247   1.00 42.49  ? 100  LYS A N   1 
ATOM   733  C  CA  . LYS A 1 100 ? 21.213  8.936   9.584   1.00 44.27  ? 100  LYS A CA  1 
ATOM   734  C  C   . LYS A 1 100 ? 22.596  9.390   10.075  1.00 41.12  ? 100  LYS A C   1 
ATOM   735  O  O   . LYS A 1 100 ? 22.735  10.408  10.750  1.00 40.23  ? 100  LYS A O   1 
ATOM   736  C  CB  . LYS A 1 100 ? 20.615  7.948   10.594  1.00 37.24  ? 100  LYS A CB  1 
ATOM   737  C  CG  . LYS A 1 100 ? 19.120  7.671   10.453  1.00 29.50  ? 100  LYS A CG  1 
ATOM   738  C  CD  . LYS A 1 100 ? 18.676  6.757   11.572  1.00 35.10  ? 100  LYS A CD  1 
ATOM   739  C  CE  . LYS A 1 100 ? 17.277  6.247   11.361  1.00 42.53  ? 100  LYS A CE  1 
ATOM   740  N  NZ  . LYS A 1 100 ? 16.965  5.088   12.285  1.00 42.85  ? 100  LYS A NZ  1 
ATOM   741  N  N   . ASP A 1 101 ? 23.615  8.609   9.739   1.00 42.00  ? 101  ASP A N   1 
ATOM   742  C  CA  . ASP A 1 101 ? 24.985  8.915   10.135  1.00 59.41  ? 101  ASP A CA  1 
ATOM   743  C  C   . ASP A 1 101 ? 25.132  9.085   11.641  1.00 48.28  ? 101  ASP A C   1 
ATOM   744  O  O   . ASP A 1 101 ? 25.724  10.059  12.097  1.00 50.95  ? 101  ASP A O   1 
ATOM   745  C  CB  . ASP A 1 101 ? 25.478  10.180  9.431   1.00 73.17  ? 101  ASP A CB  1 
ATOM   746  C  CG  . ASP A 1 101 ? 26.968  10.375  9.580   1.00 84.27  ? 101  ASP A CG  1 
ATOM   747  O  OD1 . ASP A 1 101 ? 27.711  9.378   9.439   1.00 84.44  ? 101  ASP A OD1 1 
ATOM   748  O  OD2 . ASP A 1 101 ? 27.394  11.516  9.857   1.00 91.59  ? 101  ASP A OD2 1 
ATOM   749  N  N   . LYS A 1 102 ? 24.577  8.148   12.404  1.00 42.10  ? 102  LYS A N   1 
ATOM   750  C  CA  . LYS A 1 102 ? 24.696  8.170   13.870  1.00 56.95  ? 102  LYS A CA  1 
ATOM   751  C  C   . LYS A 1 102 ? 23.938  9.322   14.555  1.00 59.39  ? 102  LYS A C   1 
ATOM   752  O  O   . LYS A 1 102 ? 24.307  9.754   15.653  1.00 58.59  ? 102  LYS A O   1 
ATOM   753  C  CB  . LYS A 1 102 ? 26.171  8.167   14.304  1.00 49.10  ? 102  LYS A CB  1 
ATOM   754  N  N   . SER A 1 103 ? 22.870  9.798   13.921  1.00 55.69  ? 103  SER A N   1 
ATOM   755  C  CA  . SER A 1 103 ? 22.048  10.852  14.501  1.00 49.33  ? 103  SER A CA  1 
ATOM   756  C  C   . SER A 1 103 ? 20.569  10.518  14.375  1.00 42.68  ? 103  SER A C   1 
ATOM   757  O  O   . SER A 1 103 ? 20.183  9.667   13.573  1.00 46.05  ? 103  SER A O   1 
ATOM   758  C  CB  . SER A 1 103 ? 22.326  12.193  13.813  1.00 49.20  ? 103  SER A CB  1 
ATOM   759  O  OG  . SER A 1 103 ? 23.710  12.494  13.817  1.00 55.70  ? 103  SER A OG  1 
ATOM   760  N  N   . ARG A 1 104 ? 19.753  11.203  15.172  1.00 31.51  ? 104  ARG A N   1 
ATOM   761  C  CA  . ARG A 1 104 ? 18.305  11.152  15.052  1.00 36.61  ? 104  ARG A CA  1 
ATOM   762  C  C   . ARG A 1 104 ? 17.934  12.110  13.923  1.00 39.50  ? 104  ARG A C   1 
ATOM   763  O  O   . ARG A 1 104 ? 17.255  13.119  14.121  1.00 44.86  ? 104  ARG A O   1 
ATOM   764  C  CB  . ARG A 1 104 ? 17.616  11.517  16.386  1.00 39.13  ? 104  ARG A CB  1 
ATOM   765  C  CG  . ARG A 1 104 ? 17.738  10.429  17.461  1.00 40.37  ? 104  ARG A CG  1 
ATOM   766  C  CD  . ARG A 1 104 ? 17.126  10.803  18.835  1.00 39.27  ? 104  ARG A CD  1 
ATOM   767  N  NE  . ARG A 1 104 ? 17.988  11.704  19.606  1.00 39.15  ? 104  ARG A NE  1 
ATOM   768  C  CZ  . ARG A 1 104 ? 18.803  11.324  20.579  1.00 44.47  ? 104  ARG A CZ  1 
ATOM   769  N  NH1 . ARG A 1 104 ? 18.875  10.054  20.930  1.00 41.49  ? 104  ARG A NH1 1 
ATOM   770  N  NH2 . ARG A 1 104 ? 19.548  12.220  21.220  1.00 65.42  ? 104  ARG A NH2 1 
ATOM   771  N  N   . ALA A 1 105 ? 18.418  11.770  12.731  1.00 32.82  ? 105  ALA A N   1 
ATOM   772  C  CA  . ALA A 1 105 ? 18.250  12.580  11.534  1.00 40.09  ? 105  ALA A CA  1 
ATOM   773  C  C   . ALA A 1 105 ? 17.226  11.948  10.610  1.00 32.17  ? 105  ALA A C   1 
ATOM   774  O  O   . ALA A 1 105 ? 17.045  10.732  10.610  1.00 36.81  ? 105  ALA A O   1 
ATOM   775  C  CB  . ALA A 1 105 ? 19.592  12.723  10.800  1.00 43.14  ? 105  ALA A CB  1 
ATOM   776  N  N   . PRO A 1 106 ? 16.555  12.769  9.805   1.00 27.48  ? 106  PRO A N   1 
ATOM   777  C  CA  . PRO A 1 106 ? 15.649  12.213  8.794   1.00 35.10  ? 106  PRO A CA  1 
ATOM   778  C  C   . PRO A 1 106 ? 16.454  11.637  7.629   1.00 23.27  ? 106  PRO A C   1 
ATOM   779  O  O   . PRO A 1 106 ? 17.583  12.057  7.415   1.00 32.72  ? 106  PRO A O   1 
ATOM   780  C  CB  . PRO A 1 106 ? 14.872  13.447  8.322   1.00 41.13  ? 106  PRO A CB  1 
ATOM   781  C  CG  . PRO A 1 106 ? 15.862  14.564  8.451   1.00 38.79  ? 106  PRO A CG  1 
ATOM   782  C  CD  . PRO A 1 106 ? 16.668  14.236  9.707   1.00 32.54  ? 106  PRO A CD  1 
ATOM   783  N  N   . ILE A 1 107 ? 15.903  10.680  6.900   1.00 32.62  ? 107  ILE A N   1 
ATOM   784  C  CA  . ILE A 1 107 ? 16.521  10.276  5.637   1.00 34.08  ? 107  ILE A CA  1 
ATOM   785  C  C   . ILE A 1 107 ? 15.668  10.914  4.552   1.00 30.09  ? 107  ILE A C   1 
ATOM   786  O  O   . ILE A 1 107 ? 14.813  10.268  3.949   1.00 38.69  ? 107  ILE A O   1 
ATOM   787  C  CB  . ILE A 1 107 ? 16.613  8.751   5.506   1.00 27.76  ? 107  ILE A CB  1 
ATOM   788  C  CG1 . ILE A 1 107 ? 17.405  8.177   6.685   1.00 31.90  ? 107  ILE A CG1 1 
ATOM   789  C  CG2 . ILE A 1 107 ? 17.286  8.351   4.171   1.00 26.97  ? 107  ILE A CG2 1 
ATOM   790  C  CD1 . ILE A 1 107 ? 17.355  6.666   6.810   1.00 26.37  ? 107  ILE A CD1 1 
ATOM   791  N  N   . SER A 1 108 ? 15.898  12.208  4.347   1.00 29.85  ? 108  SER A N   1 
ATOM   792  C  CA  . SER A 1 108 ? 15.006  13.059  3.570   1.00 23.38  ? 108  SER A CA  1 
ATOM   793  C  C   . SER A 1 108 ? 14.932  12.675  2.100   1.00 27.88  ? 108  SER A C   1 
ATOM   794  O  O   . SER A 1 108 ? 13.923  12.939  1.436   1.00 30.85  ? 108  SER A O   1 
ATOM   795  C  CB  . SER A 1 108 ? 15.442  14.512  3.685   1.00 29.12  ? 108  SER A CB  1 
ATOM   796  O  OG  . SER A 1 108 ? 15.473  14.950  5.028   1.00 33.90  ? 108  SER A OG  1 
ATOM   797  N  N   . ALA A 1 109 ? 15.998  12.056  1.589   1.00 22.23  ? 109  ALA A N   1 
ATOM   798  C  CA  . ALA A 1 109 ? 16.013  11.648  0.193   1.00 21.61  ? 109  ALA A CA  1 
ATOM   799  C  C   . ALA A 1 109 ? 15.007  10.507  -0.017  1.00 25.41  ? 109  ALA A C   1 
ATOM   800  O  O   . ALA A 1 109 ? 14.445  10.338  -1.106  1.00 26.40  ? 109  ALA A O   1 
ATOM   801  C  CB  . ALA A 1 109 ? 17.423  11.238  -0.223  1.00 15.85  ? 109  ALA A CB  1 
ATOM   802  N  N   . LYS A 1 110 ? 14.784  9.729   1.039   1.00 25.74  ? 110  LYS A N   1 
ATOM   803  C  CA  . LYS A 1 110 ? 13.782  8.673   1.009   1.00 25.19  ? 110  LYS A CA  1 
ATOM   804  C  C   . LYS A 1 110 ? 12.391  9.271   1.128   1.00 26.18  ? 110  LYS A C   1 
ATOM   805  O  O   . LYS A 1 110 ? 11.459  8.803   0.497   1.00 32.80  ? 110  LYS A O   1 
ATOM   806  C  CB  . LYS A 1 110 ? 14.021  7.648   2.126   1.00 20.39  ? 110  LYS A CB  1 
ATOM   807  C  CG  . LYS A 1 110 ? 12.949  6.559   2.212   1.00 17.23  ? 110  LYS A CG  1 
ATOM   808  C  CD  . LYS A 1 110 ? 12.764  5.842   0.861   1.00 20.28  ? 110  LYS A CD  1 
ATOM   809  C  CE  . LYS A 1 110 ? 11.705  4.744   0.911   1.00 22.34  ? 110  LYS A CE  1 
ATOM   810  N  NZ  . LYS A 1 110 ? 11.896  3.895   2.127   1.00 32.72  ? 110  LYS A NZ  1 
ATOM   811  N  N   . LEU A 1 111 ? 12.252  10.292  1.964   1.00 20.63  ? 111  LEU A N   1 
ATOM   812  C  CA  . LEU A 1 111 ? 11.009  11.026  2.041   1.00 21.23  ? 111  LEU A CA  1 
ATOM   813  C  C   . LEU A 1 111 ? 10.682  11.526  0.617   1.00 25.31  ? 111  LEU A C   1 
ATOM   814  O  O   . LEU A 1 111 ? 9.569   11.329  0.111   1.00 23.97  ? 111  LEU A O   1 
ATOM   815  C  CB  . LEU A 1 111 ? 11.177  12.215  2.988   1.00 24.85  ? 111  LEU A CB  1 
ATOM   816  C  CG  . LEU A 1 111 ? 9.968   12.917  3.631   1.00 30.35  ? 111  LEU A CG  1 
ATOM   817  C  CD1 . LEU A 1 111 ? 10.028  14.417  3.458   1.00 35.50  ? 111  LEU A CD1 1 
ATOM   818  C  CD2 . LEU A 1 111 ? 8.657   12.373  3.129   1.00 25.14  ? 111  LEU A CD2 1 
ATOM   819  N  N   . VAL A 1 112 ? 11.657  12.166  -0.022  1.00 18.45  ? 112  VAL A N   1 
ATOM   820  C  CA  . VAL A 1 112 ? 11.462  12.729  -1.357  1.00 27.15  ? 112  VAL A CA  1 
ATOM   821  C  C   . VAL A 1 112 ? 11.071  11.628  -2.349  1.00 21.43  ? 112  VAL A C   1 
ATOM   822  O  O   . VAL A 1 112 ? 10.099  11.774  -3.081  1.00 26.87  ? 112  VAL A O   1 
ATOM   823  C  CB  . VAL A 1 112 ? 12.704  13.523  -1.832  1.00 25.52  ? 112  VAL A CB  1 
ATOM   824  C  CG1 . VAL A 1 112 ? 12.540  14.008  -3.306  1.00 31.49  ? 112  VAL A CG1 1 
ATOM   825  C  CG2 . VAL A 1 112 ? 12.948  14.714  -0.891  1.00 24.27  ? 112  VAL A CG2 1 
ATOM   826  N  N   . ALA A 1 113 ? 11.788  10.505  -2.347  1.00 26.78  ? 113  ALA A N   1 
ATOM   827  C  CA  . ALA A 1 113 ? 11.420  9.409   -3.247  1.00 25.18  ? 113  ALA A CA  1 
ATOM   828  C  C   . ALA A 1 113 ? 9.985   9.002   -2.990  1.00 29.60  ? 113  ALA A C   1 
ATOM   829  O  O   . ALA A 1 113 ? 9.223   8.777   -3.934  1.00 27.76  ? 113  ALA A O   1 
ATOM   830  C  CB  . ALA A 1 113 ? 12.352  8.217   -3.090  1.00 17.25  ? 113  ALA A CB  1 
ATOM   831  N  N   . ASN A 1 114 ? 9.610   8.900   -1.715  1.00 23.56  ? 114  ASN A N   1 
ATOM   832  C  CA  . ASN A 1 114 ? 8.244   8.507   -1.369  1.00 22.54  ? 114  ASN A CA  1 
ATOM   833  C  C   . ASN A 1 114 ? 7.221   9.530   -1.846  1.00 21.82  ? 114  ASN A C   1 
ATOM   834  O  O   . ASN A 1 114 ? 6.152   9.174   -2.337  1.00 29.81  ? 114  ASN A O   1 
ATOM   835  C  CB  . ASN A 1 114 ? 8.078   8.302   0.141   1.00 32.02  ? 114  ASN A CB  1 
ATOM   836  C  CG  . ASN A 1 114 ? 8.627   6.972   0.621   1.00 34.47  ? 114  ASN A CG  1 
ATOM   837  O  OD1 . ASN A 1 114 ? 8.737   6.001   -0.136  1.00 31.08  ? 114  ASN A OD1 1 
ATOM   838  N  ND2 . ASN A 1 114 ? 8.948   6.915   1.896   1.00 28.09  ? 114  ASN A ND2 1 
ATOM   839  N  N   . MET A 1 115 ? 7.546   10.807  -1.700  1.00 19.44  ? 115  MET A N   1 
ATOM   840  C  CA  . MET A 1 115 ? 6.633   11.854  -2.137  1.00 21.49  ? 115  MET A CA  1 
ATOM   841  C  C   . MET A 1 115 ? 6.430   11.877  -3.660  1.00 16.96  ? 115  MET A C   1 
ATOM   842  O  O   . MET A 1 115 ? 5.319   12.046  -4.142  1.00 22.79  ? 115  MET A O   1 
ATOM   843  C  CB  . MET A 1 115 ? 7.134   13.196  -1.642  1.00 22.65  ? 115  MET A CB  1 
ATOM   844  C  CG  . MET A 1 115 ? 7.142   13.260  -0.125  1.00 33.11  ? 115  MET A CG  1 
ATOM   845  S  SD  . MET A 1 115 ? 7.268   14.930  0.444   1.00 46.46  ? 115  MET A SD  1 
ATOM   846  C  CE  . MET A 1 115 ? 8.986   15.245  0.204   1.00 15.65  ? 115  MET A CE  1 
ATOM   847  N  N   . LEU A 1 116 ? 7.510   11.703  -4.409  1.00 24.12  ? 116  LEU A N   1 
ATOM   848  C  CA  . LEU A 1 116 ? 7.425   11.587  -5.863  1.00 21.29  ? 116  LEU A CA  1 
ATOM   849  C  C   . LEU A 1 116 ? 6.585   10.384  -6.232  1.00 24.50  ? 116  LEU A C   1 
ATOM   850  O  O   . LEU A 1 116 ? 5.710   10.453  -7.105  1.00 27.58  ? 116  LEU A O   1 
ATOM   851  C  CB  . LEU A 1 116 ? 8.829   11.450  -6.454  1.00 20.41  ? 116  LEU A CB  1 
ATOM   852  C  CG  . LEU A 1 116 ? 9.643   12.743  -6.405  1.00 19.26  ? 116  LEU A CG  1 
ATOM   853  C  CD1 . LEU A 1 116 ? 11.133  12.496  -6.499  1.00 17.59  ? 116  LEU A CD1 1 
ATOM   854  C  CD2 . LEU A 1 116 ? 9.191   13.675  -7.530  1.00 19.83  ? 116  LEU A CD2 1 
ATOM   855  N  N   . SER A 1 117 ? 6.837   9.269   -5.560  1.00 24.27  ? 117  SER A N   1 
ATOM   856  C  CA  . SER A 1 117 ? 6.067   8.068   -5.840  1.00 23.59  ? 117  SER A CA  1 
ATOM   857  C  C   . SER A 1 117 ? 4.583   8.299   -5.565  1.00 25.88  ? 117  SER A C   1 
ATOM   858  O  O   . SER A 1 117 ? 3.733   8.066   -6.424  1.00 31.90  ? 117  SER A O   1 
ATOM   859  C  CB  . SER A 1 117 ? 6.599   6.884   -5.031  1.00 31.73  ? 117  SER A CB  1 
ATOM   860  O  OG  . SER A 1 117 ? 7.991   6.697   -5.250  1.00 32.31  ? 117  SER A OG  1 
ATOM   861  N  N   . VAL A 1 118 ? 4.256   8.788   -4.379  1.00 23.34  ? 118  VAL A N   1 
ATOM   862  C  CA  . VAL A 1 118 ? 2.845   9.021   -4.067  1.00 19.20  ? 118  VAL A CA  1 
ATOM   863  C  C   . VAL A 1 118 ? 2.253   10.145  -4.940  1.00 24.27  ? 118  VAL A C   1 
ATOM   864  O  O   . VAL A 1 118 ? 1.070   10.141  -5.239  1.00 34.56  ? 118  VAL A O   1 
ATOM   865  C  CB  . VAL A 1 118 ? 2.615   9.289   -2.556  1.00 29.51  ? 118  VAL A CB  1 
ATOM   866  C  CG1 . VAL A 1 118 ? 2.788   10.781  -2.220  1.00 24.53  ? 118  VAL A CG1 1 
ATOM   867  C  CG2 . VAL A 1 118 ? 1.236   8.823   -2.163  1.00 29.31  ? 118  VAL A CG2 1 
ATOM   868  N  N   . ALA A 1 119 ? 3.071   11.100  -5.369  1.00 25.38  ? 119  ALA A N   1 
ATOM   869  C  CA  . ALA A 1 119 ? 2.568   12.108  -6.306  1.00 31.91  ? 119  ALA A CA  1 
ATOM   870  C  C   . ALA A 1 119 ? 2.137   11.453  -7.625  1.00 31.77  ? 119  ALA A C   1 
ATOM   871  O  O   . ALA A 1 119 ? 1.368   12.030  -8.378  1.00 36.74  ? 119  ALA A O   1 
ATOM   872  C  CB  . ALA A 1 119 ? 3.612   13.190  -6.569  1.00 29.60  ? 119  ALA A CB  1 
ATOM   873  N  N   . GLY A 1 120 ? 2.641   10.253  -7.904  1.00 24.29  ? 120  GLY A N   1 
ATOM   874  C  CA  . GLY A 1 120 ? 2.244   9.544   -9.112  1.00 21.77  ? 120  GLY A CA  1 
ATOM   875  C  C   . GLY A 1 120 ? 3.313   9.381   -10.189 1.00 27.16  ? 120  GLY A C   1 
ATOM   876  O  O   . GLY A 1 120 ? 2.992   8.998   -11.309 1.00 34.44  ? 120  GLY A O   1 
ATOM   877  N  N   . ALA A 1 121 ? 4.578   9.633   -9.872  1.00 22.43  ? 121  ALA A N   1 
ATOM   878  C  CA  . ALA A 1 121 ? 5.654   9.422   -10.852 1.00 26.26  ? 121  ALA A CA  1 
ATOM   879  C  C   . ALA A 1 121 ? 5.845   7.953   -11.180 1.00 33.69  ? 121  ALA A C   1 
ATOM   880  O  O   . ALA A 1 121 ? 5.881   7.117   -10.291 1.00 27.90  ? 121  ALA A O   1 
ATOM   881  C  CB  . ALA A 1 121 ? 6.946   10.000  -10.356 1.00 22.94  ? 121  ALA A CB  1 
ATOM   882  N  N   . ASP A 1 122 ? 5.997   7.647   -12.464 1.00 23.31  ? 122  ASP A N   1 
ATOM   883  C  CA  . ASP A 1 122 ? 6.098   6.269   -12.904 1.00 15.09  ? 122  ASP A CA  1 
ATOM   884  C  C   . ASP A 1 122 ? 7.524   5.881   -13.191 1.00 21.78  ? 122  ASP A C   1 
ATOM   885  O  O   . ASP A 1 122 ? 7.827   4.709   -13.407 1.00 21.16  ? 122  ASP A O   1 
ATOM   886  C  CB  . ASP A 1 122 ? 5.224   6.033   -14.137 1.00 23.30  ? 122  ASP A CB  1 
ATOM   887  C  CG  . ASP A 1 122 ? 3.758   6.208   -13.831 1.00 29.09  ? 122  ASP A CG  1 
ATOM   888  O  OD1 . ASP A 1 122 ? 3.090   7.025   -14.495 1.00 32.90  ? 122  ASP A OD1 1 
ATOM   889  O  OD2 . ASP A 1 122 ? 3.275   5.540   -12.894 1.00 37.49  ? 122  ASP A OD2 1 
ATOM   890  N  N   . HIS A 1 123 ? 8.405   6.872   -13.178 1.00 15.51  ? 123  HIS A N   1 
ATOM   891  C  CA  . HIS A 1 123 ? 9.758   6.681   -13.683 1.00 21.83  ? 123  HIS A CA  1 
ATOM   892  C  C   . HIS A 1 123 ? 10.535  7.938   -13.355 1.00 17.81  ? 123  HIS A C   1 
ATOM   893  O  O   . HIS A 1 123 ? 9.985   9.041   -13.390 1.00 21.25  ? 123  HIS A O   1 
ATOM   894  C  CB  . HIS A 1 123 ? 9.747   6.471   -15.219 1.00 24.94  ? 123  HIS A CB  1 
ATOM   895  C  CG  . HIS A 1 123 ? 11.097  6.157   -15.798 1.00 29.11  ? 123  HIS A CG  1 
ATOM   896  N  ND1 . HIS A 1 123 ? 11.422  6.399   -17.117 1.00 51.71  ? 123  HIS A ND1 1 
ATOM   897  C  CD2 . HIS A 1 123 ? 12.209  5.631   -15.235 1.00 41.62  ? 123  HIS A CD2 1 
ATOM   898  C  CE1 . HIS A 1 123 ? 12.670  6.032   -17.338 1.00 51.97  ? 123  HIS A CE1 1 
ATOM   899  N  NE2 . HIS A 1 123 ? 13.171  5.558   -16.212 1.00 32.05  ? 123  HIS A NE2 1 
ATOM   900  N  N   . ILE A 1 124 ? 11.816  7.779   -13.041 1.00 22.22  ? 124  ILE A N   1 
ATOM   901  C  CA  . ILE A 1 124 ? 12.648  8.921   -12.687 1.00 19.21  ? 124  ILE A CA  1 
ATOM   902  C  C   . ILE A 1 124 ? 13.872  8.920   -13.579 1.00 22.43  ? 124  ILE A C   1 
ATOM   903  O  O   . ILE A 1 124 ? 14.527  7.893   -13.722 1.00 24.65  ? 124  ILE A O   1 
ATOM   904  C  CB  . ILE A 1 124 ? 13.192  8.848   -11.220 1.00 30.03  ? 124  ILE A CB  1 
ATOM   905  C  CG1 . ILE A 1 124 ? 12.071  8.626   -10.195 1.00 25.96  ? 124  ILE A CG1 1 
ATOM   906  C  CG2 . ILE A 1 124 ? 14.009  10.111  -10.892 1.00 16.61  ? 124  ILE A CG2 1 
ATOM   907  C  CD1 . ILE A 1 124 ? 11.213  9.835   -9.962  1.00 27.55  ? 124  ILE A CD1 1 
ATOM   908  N  N   . ILE A 1 125 ? 14.195  10.076  -14.147 1.00 27.01  ? 125  ILE A N   1 
ATOM   909  C  CA  . ILE A 1 125 ? 15.471  10.262  -14.820 1.00 26.65  ? 125  ILE A CA  1 
ATOM   910  C  C   . ILE A 1 125 ? 16.288  11.314  -14.088 1.00 24.56  ? 125  ILE A C   1 
ATOM   911  O  O   . ILE A 1 125 ? 15.820  12.419  -13.853 1.00 25.22  ? 125  ILE A O   1 
ATOM   912  C  CB  . ILE A 1 125 ? 15.281  10.702  -16.282 1.00 34.59  ? 125  ILE A CB  1 
ATOM   913  C  CG1 . ILE A 1 125 ? 14.592  9.593   -17.082 1.00 29.39  ? 125  ILE A CG1 1 
ATOM   914  C  CG2 . ILE A 1 125 ? 16.627  11.053  -16.907 1.00 30.11  ? 125  ILE A CG2 1 
ATOM   915  C  CD1 . ILE A 1 125 ? 14.074  10.047  -18.426 1.00 27.10  ? 125  ILE A CD1 1 
ATOM   916  N  N   . THR A 1 126 ? 17.523  10.986  -13.739 1.00 27.31  ? 126  THR A N   1 
ATOM   917  C  CA  . THR A 1 126 ? 18.322  11.926  -12.969 1.00 16.96  ? 126  THR A CA  1 
ATOM   918  C  C   . THR A 1 126 ? 19.788  11.823  -13.348 1.00 29.27  ? 126  THR A C   1 
ATOM   919  O  O   . THR A 1 126 ? 20.186  10.890  -14.046 1.00 33.97  ? 126  THR A O   1 
ATOM   920  C  CB  . THR A 1 126 ? 18.149  11.667  -11.446 1.00 37.53  ? 126  THR A CB  1 
ATOM   921  O  OG1 . THR A 1 126 ? 18.688  12.762  -10.699 1.00 36.83  ? 126  THR A OG1 1 
ATOM   922  C  CG2 . THR A 1 126 ? 18.846  10.370  -11.034 1.00 26.59  ? 126  THR A CG2 1 
ATOM   923  N  N   . MET A 1 127 ? 20.595  12.774  -12.887 1.00 27.40  ? 127  MET A N   1 
ATOM   924  C  CA  . MET A 1 127 ? 22.026  12.701  -13.127 1.00 27.70  ? 127  MET A CA  1 
ATOM   925  C  C   . MET A 1 127 ? 22.896  12.707  -11.869 1.00 29.54  ? 127  MET A C   1 
ATOM   926  O  O   . MET A 1 127 ? 22.719  13.546  -10.990 1.00 31.87  ? 127  MET A O   1 
ATOM   927  C  CB  . MET A 1 127 ? 22.470  13.850  -14.019 1.00 23.77  ? 127  MET A CB  1 
ATOM   928  C  CG  . MET A 1 127 ? 23.962  13.825  -14.284 1.00 41.38  ? 127  MET A CG  1 
ATOM   929  S  SD  . MET A 1 127 ? 24.376  14.816  -15.727 1.00 60.62  ? 127  MET A SD  1 
ATOM   930  C  CE  . MET A 1 127 ? 23.248  14.087  -16.908 1.00 37.57  ? 127  MET A CE  1 
ATOM   931  N  N   . ASP A 1 128 ? 23.874  11.808  -11.831 1.00 24.02  ? 128  ASP A N   1 
ATOM   932  C  CA  . ASP A 1 128 ? 24.831  11.706  -10.726 1.00 37.10  ? 128  ASP A CA  1 
ATOM   933  C  C   . ASP A 1 128 ? 24.196  11.797  -9.343  1.00 41.33  ? 128  ASP A C   1 
ATOM   934  O  O   . ASP A 1 128 ? 24.436  12.756  -8.605  1.00 33.75  ? 128  ASP A O   1 
ATOM   935  C  CB  . ASP A 1 128 ? 25.934  12.752  -10.858 1.00 39.23  ? 128  ASP A CB  1 
ATOM   936  C  CG  . ASP A 1 128 ? 26.812  12.512  -12.065 1.00 57.70  ? 128  ASP A CG  1 
ATOM   937  O  OD1 . ASP A 1 128 ? 26.994  13.459  -12.865 1.00 67.22  ? 128  ASP A OD1 1 
ATOM   938  O  OD2 . ASP A 1 128 ? 27.316  11.377  -12.215 1.00 54.00  ? 128  ASP A OD2 1 
ATOM   939  N  N   . LEU A 1 129 ? 23.380  10.804  -9.004  1.00 30.07  ? 129  LEU A N   1 
ATOM   940  C  CA  . LEU A 1 129 ? 22.841  10.690  -7.648  1.00 32.50  ? 129  LEU A CA  1 
ATOM   941  C  C   . LEU A 1 129 ? 23.974  10.763  -6.644  1.00 34.72  ? 129  LEU A C   1 
ATOM   942  O  O   . LEU A 1 129 ? 25.014  10.128  -6.851  1.00 33.65  ? 129  LEU A O   1 
ATOM   943  C  CB  . LEU A 1 129 ? 22.114  9.361   -7.491  1.00 31.67  ? 129  LEU A CB  1 
ATOM   944  C  CG  . LEU A 1 129 ? 20.740  9.398   -8.144  1.00 38.34  ? 129  LEU A CG  1 
ATOM   945  C  CD1 . LEU A 1 129 ? 20.097  8.018   -8.154  1.00 44.07  ? 129  LEU A CD1 1 
ATOM   946  C  CD2 . LEU A 1 129 ? 19.884  10.432  -7.397  1.00 31.56  ? 129  LEU A CD2 1 
ATOM   947  N  N   . HIS A 1 130 ? 23.792  11.536  -5.570  1.00 35.85  ? 130  HIS A N   1 
ATOM   948  C  CA  . HIS A 1 130 ? 24.856  11.693  -4.566  1.00 33.31  ? 130  HIS A CA  1 
ATOM   949  C  C   . HIS A 1 130 ? 25.378  10.331  -4.109  1.00 33.65  ? 130  HIS A C   1 
ATOM   950  O  O   . HIS A 1 130 ? 26.582  10.122  -4.028  1.00 42.43  ? 130  HIS A O   1 
ATOM   951  C  CB  . HIS A 1 130 ? 24.407  12.531  -3.366  1.00 34.20  ? 130  HIS A CB  1 
ATOM   952  C  CG  . HIS A 1 130 ? 25.486  12.742  -2.350  1.00 46.71  ? 130  HIS A CG  1 
ATOM   953  N  ND1 . HIS A 1 130 ? 25.387  12.293  -1.051  1.00 53.25  ? 130  HIS A ND1 1 
ATOM   954  C  CD2 . HIS A 1 130 ? 26.704  13.328  -2.453  1.00 45.43  ? 130  HIS A CD2 1 
ATOM   955  C  CE1 . HIS A 1 130 ? 26.489  12.606  -0.392  1.00 46.44  ? 130  HIS A CE1 1 
ATOM   956  N  NE2 . HIS A 1 130 ? 27.304  13.236  -1.220  1.00 44.73  ? 130  HIS A NE2 1 
ATOM   957  N  N   . ALA A 1 131 ? 24.465  9.413   -3.821  1.00 29.28  ? 131  ALA A N   1 
ATOM   958  C  CA  . ALA A 1 131 ? 24.802  8.004   -3.621  1.00 31.27  ? 131  ALA A CA  1 
ATOM   959  C  C   . ALA A 1 131 ? 23.928  7.135   -4.531  1.00 31.21  ? 131  ALA A C   1 
ATOM   960  O  O   . ALA A 1 131 ? 22.742  7.389   -4.664  1.00 33.46  ? 131  ALA A O   1 
ATOM   961  C  CB  . ALA A 1 131 ? 24.611  7.606   -2.152  1.00 26.15  ? 131  ALA A CB  1 
ATOM   962  N  N   . SER A 1 132 ? 24.509  6.111   -5.147  1.00 37.42  ? 132  SER A N   1 
ATOM   963  C  CA  . SER A 1 132 ? 23.758  5.224   -6.035  1.00 41.44  ? 132  SER A CA  1 
ATOM   964  C  C   . SER A 1 132 ? 22.620  4.482   -5.323  1.00 43.95  ? 132  SER A C   1 
ATOM   965  O  O   . SER A 1 132 ? 21.593  4.149   -5.933  1.00 35.29  ? 132  SER A O   1 
ATOM   966  C  CB  . SER A 1 132 ? 24.699  4.206   -6.658  1.00 34.72  ? 132  SER A CB  1 
ATOM   967  O  OG  . SER A 1 132 ? 25.829  4.853   -7.191  1.00 63.60  ? 132  SER A OG  1 
ATOM   968  N  N   . GLN A 1 133 ? 22.815  4.198   -4.040  1.00 33.49  ? 133  GLN A N   1 
ATOM   969  C  CA  . GLN A 1 133 ? 21.781  3.528   -3.261  1.00 34.63  ? 133  GLN A CA  1 
ATOM   970  C  C   . GLN A 1 133 ? 20.452  4.272   -3.288  1.00 30.80  ? 133  GLN A C   1 
ATOM   971  O  O   . GLN A 1 133 ? 19.415  3.703   -2.963  1.00 43.54  ? 133  GLN A O   1 
ATOM   972  C  CB  . GLN A 1 133 ? 22.238  3.317   -1.818  1.00 35.11  ? 133  GLN A CB  1 
ATOM   973  C  CG  . GLN A 1 133 ? 23.395  2.323   -1.685  1.00 30.76  ? 133  GLN A CG  1 
ATOM   974  C  CD  . GLN A 1 133 ? 24.743  2.984   -1.869  1.00 38.48  ? 133  GLN A CD  1 
ATOM   975  O  OE1 . GLN A 1 133 ? 24.827  4.191   -2.109  1.00 40.95  ? 133  GLN A OE1 1 
ATOM   976  N  NE2 . GLN A 1 133 ? 25.809  2.201   -1.741  1.00 34.37  ? 133  GLN A NE2 1 
ATOM   977  N  N   . ILE A 1 134 ? 20.470  5.540   -3.674  1.00 28.08  ? 134  ILE A N   1 
ATOM   978  C  CA  . ILE A 1 134 ? 19.234  6.315   -3.698  1.00 32.38  ? 134  ILE A CA  1 
ATOM   979  C  C   . ILE A 1 134 ? 18.227  5.730   -4.697  1.00 37.37  ? 134  ILE A C   1 
ATOM   980  O  O   . ILE A 1 134 ? 17.020  5.805   -4.470  1.00 37.18  ? 134  ILE A O   1 
ATOM   981  C  CB  . ILE A 1 134 ? 19.499  7.825   -3.946  1.00 31.28  ? 134  ILE A CB  1 
ATOM   982  C  CG1 . ILE A 1 134 ? 20.230  8.429   -2.747  1.00 25.06  ? 134  ILE A CG1 1 
ATOM   983  C  CG2 . ILE A 1 134 ? 18.196  8.601   -4.197  1.00 23.88  ? 134  ILE A CG2 1 
ATOM   984  C  CD1 . ILE A 1 134 ? 20.648  9.861   -2.948  1.00 32.72  ? 134  ILE A CD1 1 
ATOM   985  N  N   . GLN A 1 135 ? 18.714  5.125   -5.780  1.00 24.30  ? 135  GLN A N   1 
ATOM   986  C  CA  . GLN A 1 135 ? 17.823  4.395   -6.677  1.00 24.01  ? 135  GLN A CA  1 
ATOM   987  C  C   . GLN A 1 135 ? 17.007  3.386   -5.895  1.00 31.26  ? 135  GLN A C   1 
ATOM   988  O  O   . GLN A 1 135 ? 15.849  3.117   -6.226  1.00 37.76  ? 135  GLN A O   1 
ATOM   989  C  CB  . GLN A 1 135 ? 18.616  3.648   -7.744  1.00 26.09  ? 135  GLN A CB  1 
ATOM   990  C  CG  . GLN A 1 135 ? 19.424  4.546   -8.683  1.00 36.82  ? 135  GLN A CG  1 
ATOM   991  C  CD  . GLN A 1 135 ? 19.841  3.821   -9.966  1.00 47.00  ? 135  GLN A CD  1 
ATOM   992  O  OE1 . GLN A 1 135 ? 19.036  3.134   -10.603 1.00 44.26  ? 135  GLN A OE1 1 
ATOM   993  N  NE2 . GLN A 1 135 ? 21.100  3.976   -10.343 1.00 43.98  ? 135  GLN A NE2 1 
ATOM   994  N  N   . GLY A 1 136 ? 17.629  2.804   -4.870  1.00 25.04  ? 136  GLY A N   1 
ATOM   995  C  CA  . GLY A 1 136 ? 16.970  1.813   -4.033  1.00 25.83  ? 136  GLY A CA  1 
ATOM   996  C  C   . GLY A 1 136 ? 15.841  2.381   -3.191  1.00 24.73  ? 136  GLY A C   1 
ATOM   997  O  O   . GLY A 1 136 ? 15.022  1.632   -2.659  1.00 25.98  ? 136  GLY A O   1 
ATOM   998  N  N   . PHE A 1 137 ? 15.797  3.706   -3.069  1.00 17.09  ? 137  PHE A N   1 
ATOM   999  C  CA  . PHE A 1 137 ? 14.735  4.394   -2.314  1.00 15.86  ? 137  PHE A CA  1 
ATOM   1000 C  C   . PHE A 1 137 ? 13.409  4.401   -3.039  1.00 26.60  ? 137  PHE A C   1 
ATOM   1001 O  O   . PHE A 1 137 ? 12.393  4.836   -2.498  1.00 20.58  ? 137  PHE A O   1 
ATOM   1002 C  CB  . PHE A 1 137 ? 15.122  5.850   -2.034  1.00 12.10  ? 137  PHE A CB  1 
ATOM   1003 C  CG  . PHE A 1 137 ? 16.253  5.990   -1.055  1.00 23.97  ? 137  PHE A CG  1 
ATOM   1004 C  CD1 . PHE A 1 137 ? 16.681  7.233   -0.640  1.00 29.25  ? 137  PHE A CD1 1 
ATOM   1005 C  CD2 . PHE A 1 137 ? 16.885  4.871   -0.555  1.00 27.35  ? 137  PHE A CD2 1 
ATOM   1006 C  CE1 . PHE A 1 137 ? 17.721  7.354   0.256   1.00 20.59  ? 137  PHE A CE1 1 
ATOM   1007 C  CE2 . PHE A 1 137 ? 17.925  4.985   0.327   1.00 23.29  ? 137  PHE A CE2 1 
ATOM   1008 C  CZ  . PHE A 1 137 ? 18.339  6.243   0.739   1.00 20.61  ? 137  PHE A CZ  1 
ATOM   1009 N  N   . PHE A 1 138 ? 13.428  3.941   -4.282  1.00 23.09  ? 138  PHE A N   1 
ATOM   1010 C  CA  . PHE A 1 138 ? 12.226  3.910   -5.109  1.00 22.21  ? 138  PHE A CA  1 
ATOM   1011 C  C   . PHE A 1 138 ? 11.830  2.480   -5.329  1.00 22.79  ? 138  PHE A C   1 
ATOM   1012 O  O   . PHE A 1 138 ? 12.686  1.587   -5.319  1.00 25.48  ? 138  PHE A O   1 
ATOM   1013 C  CB  . PHE A 1 138 ? 12.535  4.523   -6.485  1.00 17.46  ? 138  PHE A CB  1 
ATOM   1014 C  CG  . PHE A 1 138 ? 12.671  6.001   -6.456  1.00 22.58  ? 138  PHE A CG  1 
ATOM   1015 C  CD1 . PHE A 1 138 ? 13.908  6.587   -6.274  1.00 22.82  ? 138  PHE A CD1 1 
ATOM   1016 C  CD2 . PHE A 1 138 ? 11.550  6.806   -6.570  1.00 28.09  ? 138  PHE A CD2 1 
ATOM   1017 C  CE1 . PHE A 1 138 ? 14.038  7.946   -6.230  1.00 24.90  ? 138  PHE A CE1 1 
ATOM   1018 C  CE2 . PHE A 1 138 ? 11.664  8.189   -6.526  1.00 22.57  ? 138  PHE A CE2 1 
ATOM   1019 C  CZ  . PHE A 1 138 ? 12.904  8.760   -6.364  1.00 23.21  ? 138  PHE A CZ  1 
ATOM   1020 N  N   . ASP A 1 139 ? 10.547  2.255   -5.579  1.00 22.82  ? 139  ASP A N   1 
ATOM   1021 C  CA  . ASP A 1 139 ? 10.149  0.998   -6.193  1.00 28.43  ? 139  ASP A CA  1 
ATOM   1022 C  C   . ASP A 1 139 ? 9.961   1.142   -7.721  1.00 35.19  ? 139  ASP A C   1 
ATOM   1023 O  O   . ASP A 1 139 ? 9.904   0.149   -8.449  1.00 44.99  ? 139  ASP A O   1 
ATOM   1024 C  CB  . ASP A 1 139 ? 8.906   0.430   -5.508  1.00 34.55  ? 139  ASP A CB  1 
ATOM   1025 C  CG  . ASP A 1 139 ? 9.185   -0.018  -4.052  1.00 45.93  ? 139  ASP A CG  1 
ATOM   1026 O  OD1 . ASP A 1 139 ? 10.297  -0.517  -3.767  1.00 37.52  ? 139  ASP A OD1 1 
ATOM   1027 O  OD2 . ASP A 1 139 ? 8.290   0.134   -3.190  1.00 48.06  ? 139  ASP A OD2 1 
ATOM   1028 N  N   . ILE A 1 140 ? 9.885   2.373   -8.210  1.00 27.01  ? 140  ILE A N   1 
ATOM   1029 C  CA  . ILE A 1 140 ? 9.737   2.605   -9.647  1.00 24.91  ? 140  ILE A CA  1 
ATOM   1030 C  C   . ILE A 1 140 ? 11.114  2.659   -10.293 1.00 28.28  ? 140  ILE A C   1 
ATOM   1031 O  O   . ILE A 1 140 ? 12.112  2.915   -9.614  1.00 26.27  ? 140  ILE A O   1 
ATOM   1032 C  CB  . ILE A 1 140 ? 8.991   3.936   -9.939  1.00 25.66  ? 140  ILE A CB  1 
ATOM   1033 C  CG1 . ILE A 1 140 ? 9.716   5.105   -9.258  1.00 23.64  ? 140  ILE A CG1 1 
ATOM   1034 C  CG2 . ILE A 1 140 ? 7.537   3.857   -9.500  1.00 18.75  ? 140  ILE A CG2 1 
ATOM   1035 C  CD1 . ILE A 1 140 ? 9.054   6.451   -9.433  1.00 21.58  ? 140  ILE A CD1 1 
ATOM   1036 N  N   . PRO A 1 141 ? 11.189  2.421   -11.614 1.00 28.03  ? 141  PRO A N   1 
ATOM   1037 C  CA  . PRO A 1 141 ? 12.497  2.517   -12.278 1.00 20.22  ? 141  PRO A CA  1 
ATOM   1038 C  C   . PRO A 1 141 ? 13.113  3.919   -12.175 1.00 23.73  ? 141  PRO A C   1 
ATOM   1039 O  O   . PRO A 1 141 ? 12.395  4.909   -12.286 1.00 26.60  ? 141  PRO A O   1 
ATOM   1040 C  CB  . PRO A 1 141 ? 12.167  2.224   -13.749 1.00 23.70  ? 141  PRO A CB  1 
ATOM   1041 C  CG  . PRO A 1 141 ? 10.892  1.483   -13.722 1.00 32.42  ? 141  PRO A CG  1 
ATOM   1042 C  CD  . PRO A 1 141 ? 10.130  1.957   -12.525 1.00 32.48  ? 141  PRO A CD  1 
ATOM   1043 N  N   . VAL A 1 142 ? 14.430  3.981   -11.974 1.00 24.56  ? 142  VAL A N   1 
ATOM   1044 C  CA  . VAL A 1 142 ? 15.183  5.224   -11.965 1.00 21.25  ? 142  VAL A CA  1 
ATOM   1045 C  C   . VAL A 1 142 ? 16.328  5.032   -12.943 1.00 37.38  ? 142  VAL A C   1 
ATOM   1046 O  O   . VAL A 1 142 ? 16.980  3.993   -12.922 1.00 26.11  ? 142  VAL A O   1 
ATOM   1047 C  CB  . VAL A 1 142 ? 15.838  5.496   -10.595 1.00 27.21  ? 142  VAL A CB  1 
ATOM   1048 C  CG1 . VAL A 1 142 ? 16.667  6.775   -10.656 1.00 22.20  ? 142  VAL A CG1 1 
ATOM   1049 C  CG2 . VAL A 1 142 ? 14.797  5.572   -9.474  1.00 18.52  ? 142  VAL A CG2 1 
ATOM   1050 N  N   . ASP A 1 143 ? 16.559  6.008   -13.814 1.00 34.51  ? 143  ASP A N   1 
ATOM   1051 C  CA  . ASP A 1 143 ? 17.768  6.007   -14.635 1.00 35.99  ? 143  ASP A CA  1 
ATOM   1052 C  C   . ASP A 1 143 ? 18.715  7.106   -14.167 1.00 32.04  ? 143  ASP A C   1 
ATOM   1053 O  O   . ASP A 1 143 ? 18.392  8.295   -14.245 1.00 29.20  ? 143  ASP A O   1 
ATOM   1054 C  CB  . ASP A 1 143 ? 17.436  6.187   -16.113 1.00 37.33  ? 143  ASP A CB  1 
ATOM   1055 C  CG  . ASP A 1 143 ? 16.701  4.993   -16.694 1.00 41.55  ? 143  ASP A CG  1 
ATOM   1056 O  OD1 . ASP A 1 143 ? 17.161  3.850   -16.479 1.00 44.57  ? 143  ASP A OD1 1 
ATOM   1057 O  OD2 . ASP A 1 143 ? 15.664  5.199   -17.360 1.00 37.22  ? 143  ASP A OD2 1 
ATOM   1058 N  N   . ASN A 1 144 ? 19.875  6.687   -13.673 1.00 26.56  ? 144  ASN A N   1 
ATOM   1059 C  CA  . ASN A 1 144 ? 20.878  7.576   -13.104 1.00 26.08  ? 144  ASN A CA  1 
ATOM   1060 C  C   . ASN A 1 144 ? 21.987  7.834   -14.139 1.00 38.64  ? 144  ASN A C   1 
ATOM   1061 O  O   . ASN A 1 144 ? 22.911  7.045   -14.265 1.00 35.05  ? 144  ASN A O   1 
ATOM   1062 C  CB  . ASN A 1 144 ? 21.472  6.930   -11.835 1.00 26.36  ? 144  ASN A CB  1 
ATOM   1063 C  CG  . ASN A 1 144 ? 22.453  7.845   -11.109 1.00 33.66  ? 144  ASN A CG  1 
ATOM   1064 O  OD1 . ASN A 1 144 ? 22.336  9.064   -11.160 1.00 31.81  ? 144  ASN A OD1 1 
ATOM   1065 N  ND2 . ASN A 1 144 ? 23.427  7.252   -10.437 1.00 27.71  ? 144  ASN A ND2 1 
ATOM   1066 N  N   . LEU A 1 145 ? 21.874  8.931   -14.890 1.00 34.21  ? 145  LEU A N   1 
ATOM   1067 C  CA  . LEU A 1 145 ? 22.850  9.303   -15.914 1.00 31.94  ? 145  LEU A CA  1 
ATOM   1068 C  C   . LEU A 1 145 ? 24.172  9.774   -15.327 1.00 39.99  ? 145  LEU A C   1 
ATOM   1069 O  O   . LEU A 1 145 ? 24.235  10.226  -14.185 1.00 40.47  ? 145  LEU A O   1 
ATOM   1070 C  CB  . LEU A 1 145 ? 22.280  10.408  -16.804 1.00 29.96  ? 145  LEU A CB  1 
ATOM   1071 C  CG  . LEU A 1 145 ? 20.983  9.989   -17.483 1.00 30.72  ? 145  LEU A CG  1 
ATOM   1072 C  CD1 . LEU A 1 145 ? 20.267  11.151  -18.134 1.00 37.92  ? 145  LEU A CD1 1 
ATOM   1073 C  CD2 . LEU A 1 145 ? 21.283  8.876   -18.474 1.00 37.91  ? 145  LEU A CD2 1 
ATOM   1074 N  N   . TYR A 1 146 ? 25.235  9.683   -16.120 1.00 43.14  ? 146  TYR A N   1 
ATOM   1075 C  CA  . TYR A 1 146 ? 26.550  10.090  -15.645 1.00 47.22  ? 146  TYR A CA  1 
ATOM   1076 C  C   . TYR A 1 146 ? 27.109  11.265  -16.412 1.00 43.28  ? 146  TYR A C   1 
ATOM   1077 O  O   . TYR A 1 146 ? 27.005  11.321  -17.634 1.00 53.34  ? 146  TYR A O   1 
ATOM   1078 C  CB  . TYR A 1 146 ? 27.522  8.920   -15.716 1.00 47.12  ? 146  TYR A CB  1 
ATOM   1079 C  CG  . TYR A 1 146 ? 27.103  7.798   -14.829 1.00 54.25  ? 146  TYR A CG  1 
ATOM   1080 C  CD1 . TYR A 1 146 ? 26.394  6.722   -15.336 1.00 68.34  ? 146  TYR A CD1 1 
ATOM   1081 C  CD2 . TYR A 1 146 ? 27.378  7.830   -13.470 1.00 62.65  ? 146  TYR A CD2 1 
ATOM   1082 C  CE1 . TYR A 1 146 ? 25.984  5.690   -14.514 1.00 80.21  ? 146  TYR A CE1 1 
ATOM   1083 C  CE2 . TYR A 1 146 ? 26.975  6.808   -12.637 1.00 71.68  ? 146  TYR A CE2 1 
ATOM   1084 C  CZ  . TYR A 1 146 ? 26.281  5.739   -13.163 1.00 80.24  ? 146  TYR A CZ  1 
ATOM   1085 O  OH  . TYR A 1 146 ? 25.879  4.714   -12.343 1.00 86.83  ? 146  TYR A OH  1 
ATOM   1086 N  N   . ALA A 1 147 ? 27.708  12.196  -15.679 1.00 38.98  ? 147  ALA A N   1 
ATOM   1087 C  CA  . ALA A 1 147 ? 28.453  13.286  -16.282 1.00 44.84  ? 147  ALA A CA  1 
ATOM   1088 C  C   . ALA A 1 147 ? 29.877  12.841  -16.601 1.00 43.73  ? 147  ALA A C   1 
ATOM   1089 O  O   . ALA A 1 147 ? 30.591  13.529  -17.329 1.00 41.99  ? 147  ALA A O   1 
ATOM   1090 C  CB  . ALA A 1 147 ? 28.481  14.486  -15.350 1.00 36.52  ? 147  ALA A CB  1 
ATOM   1091 N  N   . GLU A 1 148 ? 30.276  11.692  -16.054 1.00 31.69  ? 148  GLU A N   1 
ATOM   1092 C  CA  . GLU A 1 148 ? 31.651  11.223  -16.138 1.00 37.28  ? 148  GLU A CA  1 
ATOM   1093 C  C   . GLU A 1 148 ? 32.221  11.289  -17.560 1.00 44.08  ? 148  GLU A C   1 
ATOM   1094 O  O   . GLU A 1 148 ? 33.275  11.880  -17.777 1.00 44.50  ? 148  GLU A O   1 
ATOM   1095 C  CB  . GLU A 1 148 ? 31.784  9.807   -15.581 1.00 37.05  ? 148  GLU A CB  1 
ATOM   1096 C  CG  . GLU A 1 148 ? 33.224  9.300   -15.562 1.00 51.88  ? 148  GLU A CG  1 
ATOM   1097 C  CD  . GLU A 1 148 ? 33.391  7.950   -14.864 1.00 67.48  ? 148  GLU A CD  1 
ATOM   1098 O  OE1 . GLU A 1 148 ? 32.637  7.661   -13.902 1.00 79.70  ? 148  GLU A OE1 1 
ATOM   1099 O  OE2 . GLU A 1 148 ? 34.282  7.175   -15.274 1.00 66.77  ? 148  GLU A OE2 1 
ATOM   1100 N  N   . PRO A 1 149 ? 31.528  10.679  -18.531 1.00 42.32  ? 149  PRO A N   1 
ATOM   1101 C  CA  . PRO A 1 149 ? 32.058  10.730  -19.896 1.00 38.08  ? 149  PRO A CA  1 
ATOM   1102 C  C   . PRO A 1 149 ? 32.323  12.170  -20.346 1.00 40.80  ? 149  PRO A C   1 
ATOM   1103 O  O   . PRO A 1 149 ? 33.393  12.457  -20.883 1.00 48.95  ? 149  PRO A O   1 
ATOM   1104 C  CB  . PRO A 1 149 ? 30.944  10.087  -20.716 1.00 40.65  ? 149  PRO A CB  1 
ATOM   1105 C  CG  . PRO A 1 149 ? 30.259  9.158   -19.744 1.00 38.68  ? 149  PRO A CG  1 
ATOM   1106 C  CD  . PRO A 1 149 ? 30.295  9.871   -18.442 1.00 40.09  ? 149  PRO A CD  1 
ATOM   1107 N  N   . ALA A 1 150 ? 31.381  13.070  -20.094 1.00 39.19  ? 150  ALA A N   1 
ATOM   1108 C  CA  . ALA A 1 150 ? 31.544  14.471  -20.479 1.00 46.37  ? 150  ALA A CA  1 
ATOM   1109 C  C   . ALA A 1 150 ? 32.744  15.137  -19.789 1.00 46.11  ? 150  ALA A C   1 
ATOM   1110 O  O   . ALA A 1 150 ? 33.441  15.964  -20.388 1.00 48.78  ? 150  ALA A O   1 
ATOM   1111 C  CB  . ALA A 1 150 ? 30.268  15.246  -20.188 1.00 49.36  ? 150  ALA A CB  1 
ATOM   1112 N  N   . VAL A 1 151 ? 32.965  14.777  -18.527 1.00 39.14  ? 151  VAL A N   1 
ATOM   1113 C  CA  . VAL A 1 151 ? 34.047  15.329  -17.716 1.00 34.48  ? 151  VAL A CA  1 
ATOM   1114 C  C   . VAL A 1 151 ? 35.400  14.829  -18.233 1.00 45.79  ? 151  VAL A C   1 
ATOM   1115 O  O   . VAL A 1 151 ? 36.361  15.595  -18.369 1.00 44.74  ? 151  VAL A O   1 
ATOM   1116 C  CB  . VAL A 1 151 ? 33.883  14.898  -16.231 1.00 42.85  ? 151  VAL A CB  1 
ATOM   1117 C  CG1 . VAL A 1 151 ? 35.153  15.166  -15.430 1.00 37.03  ? 151  VAL A CG1 1 
ATOM   1118 C  CG2 . VAL A 1 151 ? 32.689  15.587  -15.603 1.00 42.92  ? 151  VAL A CG2 1 
ATOM   1119 N  N   . LEU A 1 152 ? 35.453  13.525  -18.501 1.00 38.31  ? 152  LEU A N   1 
ATOM   1120 C  CA  . LEU A 1 152 ? 36.637  12.870  -19.021 1.00 38.65  ? 152  LEU A CA  1 
ATOM   1121 C  C   . LEU A 1 152 ? 37.035  13.522  -20.337 1.00 48.65  ? 152  LEU A C   1 
ATOM   1122 O  O   . LEU A 1 152 ? 38.216  13.785  -20.585 1.00 47.29  ? 152  LEU A O   1 
ATOM   1123 C  CB  . LEU A 1 152 ? 36.347  11.390  -19.246 1.00 38.05  ? 152  LEU A CB  1 
ATOM   1124 C  CG  . LEU A 1 152 ? 36.994  10.377  -18.304 1.00 43.23  ? 152  LEU A CG  1 
ATOM   1125 C  CD1 . LEU A 1 152 ? 37.311  11.011  -16.972 1.00 42.63  ? 152  LEU A CD1 1 
ATOM   1126 C  CD2 . LEU A 1 152 ? 36.106  9.153   -18.145 1.00 38.43  ? 152  LEU A CD2 1 
ATOM   1127 N  N   . LYS A 1 153 ? 36.038  13.783  -21.176 1.00 48.36  ? 153  LYS A N   1 
ATOM   1128 C  CA  . LYS A 1 153 ? 36.269  14.411  -22.465 1.00 42.32  ? 153  LYS A CA  1 
ATOM   1129 C  C   . LYS A 1 153 ? 36.846  15.812  -22.257 1.00 47.18  ? 153  LYS A C   1 
ATOM   1130 O  O   . LYS A 1 153 ? 37.842  16.184  -22.879 1.00 53.67  ? 153  LYS A O   1 
ATOM   1131 C  CB  . LYS A 1 153 ? 34.965  14.462  -23.270 1.00 45.93  ? 153  LYS A CB  1 
ATOM   1132 C  CG  . LYS A 1 153 ? 35.141  14.835  -24.735 1.00 53.75  ? 153  LYS A CG  1 
ATOM   1133 C  CD  . LYS A 1 153 ? 33.852  14.665  -25.515 1.00 52.66  ? 153  LYS A CD  1 
ATOM   1134 N  N   . TRP A 1 154 ? 36.229  16.574  -21.363 1.00 47.23  ? 154  TRP A N   1 
ATOM   1135 C  CA  . TRP A 1 154 ? 36.658  17.937  -21.088 1.00 52.01  ? 154  TRP A CA  1 
ATOM   1136 C  C   . TRP A 1 154 ? 38.064  17.985  -20.476 1.00 53.65  ? 154  TRP A C   1 
ATOM   1137 O  O   . TRP A 1 154 ? 38.860  18.875  -20.792 1.00 49.96  ? 154  TRP A O   1 
ATOM   1138 C  CB  . TRP A 1 154 ? 35.647  18.646  -20.172 1.00 41.75  ? 154  TRP A CB  1 
ATOM   1139 C  CG  . TRP A 1 154 ? 35.965  20.082  -19.965 1.00 47.12  ? 154  TRP A CG  1 
ATOM   1140 C  CD1 . TRP A 1 154 ? 35.358  21.149  -20.558 1.00 48.73  ? 154  TRP A CD1 1 
ATOM   1141 C  CD2 . TRP A 1 154 ? 36.995  20.620  -19.123 1.00 54.81  ? 154  TRP A CD2 1 
ATOM   1142 N  NE1 . TRP A 1 154 ? 35.939  22.323  -20.132 1.00 53.39  ? 154  TRP A NE1 1 
ATOM   1143 C  CE2 . TRP A 1 154 ? 36.945  22.025  -19.254 1.00 56.08  ? 154  TRP A CE2 1 
ATOM   1144 C  CE3 . TRP A 1 154 ? 37.951  20.051  -18.274 1.00 53.63  ? 154  TRP A CE3 1 
ATOM   1145 C  CZ2 . TRP A 1 154 ? 37.813  22.868  -18.560 1.00 56.12  ? 154  TRP A CZ2 1 
ATOM   1146 C  CZ3 . TRP A 1 154 ? 38.807  20.887  -17.586 1.00 53.33  ? 154  TRP A CZ3 1 
ATOM   1147 C  CH2 . TRP A 1 154 ? 38.734  22.283  -17.735 1.00 54.28  ? 154  TRP A CH2 1 
ATOM   1148 N  N   . ILE A 1 155 ? 38.371  17.038  -19.597 1.00 48.26  ? 155  ILE A N   1 
ATOM   1149 C  CA  . ILE A 1 155 ? 39.701  16.992  -19.000 1.00 46.74  ? 155  ILE A CA  1 
ATOM   1150 C  C   . ILE A 1 155 ? 40.775  16.793  -20.071 1.00 52.30  ? 155  ILE A C   1 
ATOM   1151 O  O   . ILE A 1 155 ? 41.814  17.450  -20.048 1.00 47.27  ? 155  ILE A O   1 
ATOM   1152 C  CB  . ILE A 1 155 ? 39.818  15.885  -17.953 1.00 49.07  ? 155  ILE A CB  1 
ATOM   1153 C  CG1 . ILE A 1 155 ? 39.001  16.238  -16.698 1.00 50.29  ? 155  ILE A CG1 1 
ATOM   1154 C  CG2 . ILE A 1 155 ? 41.277  15.639  -17.594 1.00 40.03  ? 155  ILE A CG2 1 
ATOM   1155 C  CD1 . ILE A 1 155 ? 39.120  15.201  -15.588 1.00 39.98  ? 155  ILE A CD1 1 
ATOM   1156 N  N   . ARG A 1 156 ? 40.514  15.890  -21.009 1.00 49.95  ? 156  ARG A N   1 
ATOM   1157 C  CA  . ARG A 1 156 ? 41.483  15.570  -22.049 1.00 53.64  ? 156  ARG A CA  1 
ATOM   1158 C  C   . ARG A 1 156 ? 41.635  16.703  -23.052 1.00 59.30  ? 156  ARG A C   1 
ATOM   1159 O  O   . ARG A 1 156 ? 42.681  16.836  -23.695 1.00 64.59  ? 156  ARG A O   1 
ATOM   1160 C  CB  . ARG A 1 156 ? 41.074  14.300  -22.796 1.00 57.77  ? 156  ARG A CB  1 
ATOM   1161 C  CG  . ARG A 1 156 ? 41.210  13.004  -22.016 1.00 59.24  ? 156  ARG A CG  1 
ATOM   1162 C  CD  . ARG A 1 156 ? 40.845  11.836  -22.922 1.00 65.57  ? 156  ARG A CD  1 
ATOM   1163 N  NE  . ARG A 1 156 ? 40.838  10.544  -22.238 1.00 74.70  ? 156  ARG A NE  1 
ATOM   1164 C  CZ  . ARG A 1 156 ? 39.737  9.909   -21.845 1.00 69.33  ? 156  ARG A CZ  1 
ATOM   1165 N  NH1 . ARG A 1 156 ? 38.542  10.445  -22.059 1.00 60.32  ? 156  ARG A NH1 1 
ATOM   1166 N  NH2 . ARG A 1 156 ? 39.832  8.732   -21.242 1.00 69.16  ? 156  ARG A NH2 1 
ATOM   1167 N  N   . GLU A 1 157 ? 40.590  17.512  -23.193 1.00 60.72  ? 157  GLU A N   1 
ATOM   1168 C  CA  . GLU A 1 157 ? 40.573  18.565  -24.203 1.00 69.06  ? 157  GLU A CA  1 
ATOM   1169 C  C   . GLU A 1 157 ? 40.875  19.959  -23.657 1.00 65.29  ? 157  GLU A C   1 
ATOM   1170 O  O   . GLU A 1 157 ? 40.705  20.954  -24.361 1.00 70.55  ? 157  GLU A O   1 
ATOM   1171 C  CB  . GLU A 1 157 ? 39.226  18.580  -24.929 1.00 71.40  ? 157  GLU A CB  1 
ATOM   1172 C  CG  . GLU A 1 157 ? 38.977  17.349  -25.780 1.00 77.92  ? 157  GLU A CG  1 
ATOM   1173 C  CD  . GLU A 1 157 ? 37.624  17.376  -26.476 1.00 83.01  ? 157  GLU A CD  1 
ATOM   1174 O  OE1 . GLU A 1 157 ? 36.879  18.368  -26.313 1.00 78.33  ? 157  GLU A OE1 1 
ATOM   1175 O  OE2 . GLU A 1 157 ? 37.306  16.394  -27.183 1.00 84.81  ? 157  GLU A OE2 1 
ATOM   1176 N  N   . ASN A 1 158 ? 41.322  20.041  -22.410 1.00 53.40  ? 158  ASN A N   1 
ATOM   1177 C  CA  . ASN A 1 158 ? 41.509  21.345  -21.793 1.00 54.81  ? 158  ASN A CA  1 
ATOM   1178 C  C   . ASN A 1 158 ? 42.683  21.399  -20.844 1.00 56.08  ? 158  ASN A C   1 
ATOM   1179 O  O   . ASN A 1 158 ? 43.159  22.479  -20.490 1.00 61.30  ? 158  ASN A O   1 
ATOM   1180 C  CB  . ASN A 1 158 ? 40.233  21.770  -21.065 1.00 64.37  ? 158  ASN A CB  1 
ATOM   1181 C  CG  . ASN A 1 158 ? 39.093  22.046  -22.014 1.00 60.89  ? 158  ASN A CG  1 
ATOM   1182 O  OD1 . ASN A 1 158 ? 38.842  23.190  -22.379 1.00 64.76  ? 158  ASN A OD1 1 
ATOM   1183 N  ND2 . ASN A 1 158 ? 38.403  20.995  -22.430 1.00 59.20  ? 158  ASN A ND2 1 
ATOM   1184 N  N   . ILE A 1 159 ? 43.140  20.228  -20.419 1.00 53.07  ? 159  ILE A N   1 
ATOM   1185 C  CA  . ILE A 1 159 ? 44.314  20.146  -19.568 1.00 49.36  ? 159  ILE A CA  1 
ATOM   1186 C  C   . ILE A 1 159 ? 45.442  19.468  -20.342 1.00 56.48  ? 159  ILE A C   1 
ATOM   1187 O  O   . ILE A 1 159 ? 45.400  18.257  -20.584 1.00 51.83  ? 159  ILE A O   1 
ATOM   1188 C  CB  . ILE A 1 159 ? 44.022  19.364  -18.267 1.00 54.52  ? 159  ILE A CB  1 
ATOM   1189 C  CG1 . ILE A 1 159 ? 42.745  19.888  -17.595 1.00 58.14  ? 159  ILE A CG1 1 
ATOM   1190 C  CG2 . ILE A 1 159 ? 45.207  19.455  -17.321 1.00 49.24  ? 159  ILE A CG2 1 
ATOM   1191 N  N   . SER A 1 160 ? 46.446  20.247  -20.738 1.00 53.87  ? 160  SER A N   1 
ATOM   1192 C  CA  . SER A 1 160 ? 47.516  19.704  -21.567 1.00 57.83  ? 160  SER A CA  1 
ATOM   1193 C  C   . SER A 1 160 ? 48.323  18.645  -20.819 1.00 59.36  ? 160  SER A C   1 
ATOM   1194 O  O   . SER A 1 160 ? 48.634  17.586  -21.367 1.00 54.43  ? 160  SER A O   1 
ATOM   1195 C  CB  . SER A 1 160 ? 48.416  20.818  -22.111 1.00 64.13  ? 160  SER A CB  1 
ATOM   1196 O  OG  . SER A 1 160 ? 48.939  21.625  -21.071 1.00 72.40  ? 160  SER A OG  1 
ATOM   1197 N  N   . GLU A 1 161 ? 48.636  18.923  -19.559 1.00 57.85  ? 161  GLU A N   1 
ATOM   1198 C  CA  . GLU A 1 161 ? 49.414  17.987  -18.756 1.00 61.77  ? 161  GLU A CA  1 
ATOM   1199 C  C   . GLU A 1 161 ? 48.528  16.913  -18.109 1.00 68.07  ? 161  GLU A C   1 
ATOM   1200 O  O   . GLU A 1 161 ? 48.819  16.435  -17.012 1.00 76.77  ? 161  GLU A O   1 
ATOM   1201 C  CB  . GLU A 1 161 ? 50.206  18.745  -17.685 1.00 55.41  ? 161  GLU A CB  1 
ATOM   1202 C  CG  . GLU A 1 161 ? 51.230  19.732  -18.238 1.00 56.02  ? 161  GLU A CG  1 
ATOM   1203 N  N   . TRP A 1 162 ? 47.455  16.524  -18.793 1.00 56.63  ? 162  TRP A N   1 
ATOM   1204 C  CA  . TRP A 1 162 ? 46.473  15.632  -18.186 1.00 56.85  ? 162  TRP A CA  1 
ATOM   1205 C  C   . TRP A 1 162 ? 46.961  14.190  -18.024 1.00 62.36  ? 162  TRP A C   1 
ATOM   1206 O  O   . TRP A 1 162 ? 46.498  13.475  -17.133 1.00 53.87  ? 162  TRP A O   1 
ATOM   1207 C  CB  . TRP A 1 162 ? 45.133  15.678  -18.931 1.00 48.15  ? 162  TRP A CB  1 
ATOM   1208 C  CG  . TRP A 1 162 ? 45.103  14.948  -20.237 1.00 47.36  ? 162  TRP A CG  1 
ATOM   1209 C  CD1 . TRP A 1 162 ? 45.180  15.497  -21.487 1.00 47.58  ? 162  TRP A CD1 1 
ATOM   1210 C  CD2 . TRP A 1 162 ? 44.961  13.532  -20.429 1.00 46.77  ? 162  TRP A CD2 1 
ATOM   1211 N  NE1 . TRP A 1 162 ? 45.107  14.509  -22.442 1.00 47.09  ? 162  TRP A NE1 1 
ATOM   1212 C  CE2 . TRP A 1 162 ? 44.975  13.300  -21.821 1.00 49.56  ? 162  TRP A CE2 1 
ATOM   1213 C  CE3 . TRP A 1 162 ? 44.832  12.444  -19.560 1.00 50.40  ? 162  TRP A CE3 1 
ATOM   1214 C  CZ2 . TRP A 1 162 ? 44.857  12.021  -22.361 1.00 55.66  ? 162  TRP A CZ2 1 
ATOM   1215 C  CZ3 . TRP A 1 162 ? 44.717  11.178  -20.097 1.00 56.76  ? 162  TRP A CZ3 1 
ATOM   1216 C  CH2 . TRP A 1 162 ? 44.729  10.975  -21.487 1.00 60.48  ? 162  TRP A CH2 1 
ATOM   1217 N  N   . ARG A 1 163 ? 47.899  13.778  -18.874 1.00 62.63  ? 163  ARG A N   1 
ATOM   1218 C  CA  . ARG A 1 163 ? 48.395  12.403  -18.870 1.00 56.09  ? 163  ARG A CA  1 
ATOM   1219 C  C   . ARG A 1 163 ? 49.226  12.085  -17.634 1.00 56.62  ? 163  ARG A C   1 
ATOM   1220 O  O   . ARG A 1 163 ? 49.449  10.918  -17.312 1.00 61.30  ? 163  ARG A O   1 
ATOM   1221 C  CB  . ARG A 1 163 ? 49.181  12.098  -20.152 1.00 50.85  ? 163  ARG A CB  1 
ATOM   1222 C  CG  . ARG A 1 163 ? 48.326  12.162  -21.419 1.00 52.14  ? 163  ARG A CG  1 
ATOM   1223 C  CD  . ARG A 1 163 ? 48.991  11.463  -22.589 1.00 58.47  ? 163  ARG A CD  1 
ATOM   1224 N  NE  . ARG A 1 163 ? 48.162  11.492  -23.795 1.00 62.21  ? 163  ARG A NE  1 
ATOM   1225 C  CZ  . ARG A 1 163 ? 47.392  10.485  -24.202 1.00 61.83  ? 163  ARG A CZ  1 
ATOM   1226 N  NH1 . ARG A 1 163 ? 47.333  9.359   -23.499 1.00 49.87  ? 163  ARG A NH1 1 
ATOM   1227 N  NH2 . ARG A 1 163 ? 46.676  10.611  -25.314 1.00 68.14  ? 163  ARG A NH2 1 
ATOM   1228 N  N   . ASN A 1 164 ? 49.671  13.121  -16.936 0.60 46.07  ? 164  ASN A N   1 
ATOM   1229 C  CA  . ASN A 1 164 ? 50.382  12.925  -15.688 0.60 44.46  ? 164  ASN A CA  1 
ATOM   1230 C  C   . ASN A 1 164 ? 49.812  13.806  -14.593 0.60 43.79  ? 164  ASN A C   1 
ATOM   1231 O  O   . ASN A 1 164 ? 50.549  14.390  -13.807 0.60 45.61  ? 164  ASN A O   1 
ATOM   1232 C  CB  . ASN A 1 164 ? 51.886  13.178  -15.866 0.60 57.00  ? 164  ASN A CB  1 
ATOM   1233 C  CG  . ASN A 1 164 ? 52.496  12.333  -16.976 0.60 56.30  ? 164  ASN A CG  1 
ATOM   1234 O  OD1 . ASN A 1 164 ? 52.649  11.118  -16.839 0.60 54.26  ? 164  ASN A OD1 1 
ATOM   1235 N  ND2 . ASN A 1 164 ? 52.854  12.978  -18.082 0.60 54.99  ? 164  ASN A ND2 1 
ATOM   1236 N  N   . CYS A 1 165 ? 48.486  13.893  -14.550 1.00 50.13  ? 165  CYS A N   1 
ATOM   1237 C  CA  . CYS A 1 165 ? 47.796  14.679  -13.532 1.00 57.49  ? 165  CYS A CA  1 
ATOM   1238 C  C   . CYS A 1 165 ? 47.241  13.792  -12.415 1.00 57.88  ? 165  CYS A C   1 
ATOM   1239 O  O   . CYS A 1 165 ? 47.192  12.565  -12.549 1.00 52.10  ? 165  CYS A O   1 
ATOM   1240 C  CB  . CYS A 1 165 ? 46.640  15.458  -14.158 1.00 54.45  ? 165  CYS A CB  1 
ATOM   1241 S  SG  . CYS A 1 165 ? 45.137  14.466  -14.373 1.00 52.07  ? 165  CYS A SG  1 
ATOM   1242 N  N   . THR A 1 166 ? 46.808  14.425  -11.324 1.00 53.62  ? 166  THR A N   1 
ATOM   1243 C  CA  . THR A 1 166 ? 46.184  13.717  -10.205 1.00 51.58  ? 166  THR A CA  1 
ATOM   1244 C  C   . THR A 1 166 ? 44.735  14.151  -10.013 1.00 49.55  ? 166  THR A C   1 
ATOM   1245 O  O   . THR A 1 166 ? 44.428  15.347  -10.019 1.00 53.32  ? 166  THR A O   1 
ATOM   1246 C  CB  . THR A 1 166 ? 46.940  13.957  -8.876  1.00 50.13  ? 166  THR A CB  1 
ATOM   1247 O  OG1 . THR A 1 166 ? 48.309  13.561  -9.020  1.00 60.22  ? 166  THR A OG1 1 
ATOM   1248 C  CG2 . THR A 1 166 ? 46.301  13.157  -7.732  1.00 47.35  ? 166  THR A CG2 1 
ATOM   1249 N  N   . ILE A 1 167 ? 43.849  13.174  -9.831  1.00 43.84  ? 167  ILE A N   1 
ATOM   1250 C  CA  . ILE A 1 167 ? 42.451  13.454  -9.513  1.00 41.82  ? 167  ILE A CA  1 
ATOM   1251 C  C   . ILE A 1 167 ? 42.271  13.405  -8.011  1.00 42.87  ? 167  ILE A C   1 
ATOM   1252 O  O   . ILE A 1 167 ? 42.569  12.393  -7.386  1.00 45.85  ? 167  ILE A O   1 
ATOM   1253 C  CB  . ILE A 1 167 ? 41.515  12.427  -10.147 1.00 39.64  ? 167  ILE A CB  1 
ATOM   1254 C  CG1 . ILE A 1 167 ? 41.880  12.239  -11.620 1.00 44.06  ? 167  ILE A CG1 1 
ATOM   1255 C  CG2 . ILE A 1 167 ? 40.053  12.858  -9.973  1.00 34.76  ? 167  ILE A CG2 1 
ATOM   1256 C  CD1 . ILE A 1 167 ? 42.078  13.542  -12.358 1.00 43.72  ? 167  ILE A CD1 1 
ATOM   1257 N  N   . VAL A 1 168 ? 41.783  14.499  -7.435  1.00 42.09  ? 168  VAL A N   1 
ATOM   1258 C  CA  . VAL A 1 168 ? 41.762  14.647  -5.986  1.00 43.80  ? 168  VAL A CA  1 
ATOM   1259 C  C   . VAL A 1 168 ? 40.346  14.766  -5.451  1.00 42.42  ? 168  VAL A C   1 
ATOM   1260 O  O   . VAL A 1 168 ? 39.543  15.535  -5.971  1.00 42.77  ? 168  VAL A O   1 
ATOM   1261 C  CB  . VAL A 1 168 ? 42.554  15.886  -5.552  1.00 42.77  ? 168  VAL A CB  1 
ATOM   1262 C  CG1 . VAL A 1 168 ? 42.599  15.994  -4.031  1.00 42.06  ? 168  VAL A CG1 1 
ATOM   1263 C  CG2 . VAL A 1 168 ? 43.956  15.847  -6.136  1.00 36.27  ? 168  VAL A CG2 1 
ATOM   1264 N  N   . SER A 1 169 ? 40.041  13.994  -4.414  1.00 44.11  ? 169  SER A N   1 
ATOM   1265 C  CA  . SER A 1 169 ? 38.751  14.094  -3.746  1.00 39.79  ? 169  SER A CA  1 
ATOM   1266 C  C   . SER A 1 169 ? 38.884  15.031  -2.558  1.00 38.77  ? 169  SER A C   1 
ATOM   1267 O  O   . SER A 1 169 ? 39.825  14.901  -1.780  1.00 36.64  ? 169  SER A O   1 
ATOM   1268 C  CB  . SER A 1 169 ? 38.285  12.719  -3.261  1.00 48.71  ? 169  SER A CB  1 
ATOM   1269 O  OG  . SER A 1 169 ? 36.987  12.792  -2.699  1.00 44.15  ? 169  SER A OG  1 
ATOM   1270 N  N   . PRO A 1 170 ? 37.937  15.975  -2.420  1.00 43.75  ? 170  PRO A N   1 
ATOM   1271 C  CA  . PRO A 1 170 ? 37.879  16.975  -1.348  1.00 47.71  ? 170  PRO A CA  1 
ATOM   1272 C  C   . PRO A 1 170 ? 37.584  16.347  0.001   1.00 49.06  ? 170  PRO A C   1 
ATOM   1273 O  O   . PRO A 1 170 ? 37.768  16.984  1.034   1.00 51.69  ? 170  PRO A O   1 
ATOM   1274 C  CB  . PRO A 1 170 ? 36.692  17.858  -1.749  1.00 46.03  ? 170  PRO A CB  1 
ATOM   1275 C  CG  . PRO A 1 170 ? 36.496  17.598  -3.215  1.00 55.26  ? 170  PRO A CG  1 
ATOM   1276 C  CD  . PRO A 1 170 ? 36.859  16.163  -3.403  1.00 49.08  ? 170  PRO A CD  1 
ATOM   1277 N  N   . ASP A 1 171 ? 37.112  15.110  -0.006  1.00 50.35  ? 171  ASP A N   1 
ATOM   1278 C  CA  . ASP A 1 171 ? 36.786  14.445  1.249   1.00 49.97  ? 171  ASP A CA  1 
ATOM   1279 C  C   . ASP A 1 171 ? 36.914  12.932  1.140   1.00 50.22  ? 171  ASP A C   1 
ATOM   1280 O  O   . ASP A 1 171 ? 37.159  12.393  0.060   1.00 48.17  ? 171  ASP A O   1 
ATOM   1281 C  CB  . ASP A 1 171 ? 35.394  14.859  1.747   1.00 49.23  ? 171  ASP A CB  1 
ATOM   1282 C  CG  . ASP A 1 171 ? 34.294  14.611  0.719   1.00 50.92  ? 171  ASP A CG  1 
ATOM   1283 O  OD1 . ASP A 1 171 ? 33.431  15.495  0.556   1.00 50.52  ? 171  ASP A OD1 1 
ATOM   1284 O  OD2 . ASP A 1 171 ? 34.279  13.537  0.087   1.00 52.27  ? 171  ASP A OD2 1 
ATOM   1285 N  N   . ALA A 1 172 ? 36.760  12.260  2.274   1.00 47.05  ? 172  ALA A N   1 
ATOM   1286 C  CA  . ALA A 1 172 ? 36.909  10.815  2.345   1.00 54.03  ? 172  ALA A CA  1 
ATOM   1287 C  C   . ALA A 1 172 ? 35.833  10.067  1.545   1.00 52.61  ? 172  ALA A C   1 
ATOM   1288 O  O   . ALA A 1 172 ? 36.104  9.032   0.930   1.00 58.13  ? 172  ALA A O   1 
ATOM   1289 C  CB  . ALA A 1 172 ? 36.897  10.372  3.796   1.00 54.52  ? 172  ALA A CB  1 
ATOM   1290 N  N   . GLY A 1 173 ? 34.614  10.593  1.557   1.00 49.73  ? 173  GLY A N   1 
ATOM   1291 C  CA  . GLY A 1 173 ? 33.502  9.955   0.876   1.00 57.08  ? 173  GLY A CA  1 
ATOM   1292 C  C   . GLY A 1 173 ? 33.509  10.062  -0.641  1.00 62.74  ? 173  GLY A C   1 
ATOM   1293 O  O   . GLY A 1 173 ? 32.707  9.413   -1.316  1.00 64.98  ? 173  GLY A O   1 
ATOM   1294 N  N   . GLY A 1 174 ? 34.405  10.880  -1.183  1.00 60.28  ? 174  GLY A N   1 
ATOM   1295 C  CA  . GLY A 1 174 ? 34.487  11.057  -2.622  1.00 53.48  ? 174  GLY A CA  1 
ATOM   1296 C  C   . GLY A 1 174 ? 35.469  10.096  -3.269  1.00 50.34  ? 174  GLY A C   1 
ATOM   1297 O  O   . GLY A 1 174 ? 35.673  10.148  -4.478  1.00 49.36  ? 174  GLY A O   1 
ATOM   1298 N  N   . ALA A 1 175 ? 36.065  9.218   -2.461  1.00 37.42  ? 175  ALA A N   1 
ATOM   1299 C  CA  . ALA A 1 175 ? 37.105  8.310   -2.928  1.00 36.04  ? 175  ALA A CA  1 
ATOM   1300 C  C   . ALA A 1 175 ? 36.732  7.577   -4.211  1.00 45.46  ? 175  ALA A C   1 
ATOM   1301 O  O   . ALA A 1 175 ? 37.477  7.617   -5.190  1.00 45.85  ? 175  ALA A O   1 
ATOM   1302 C  CB  . ALA A 1 175 ? 37.456  7.315   -1.850  1.00 39.81  ? 175  ALA A CB  1 
ATOM   1303 N  N   . LYS A 1 176 ? 35.584  6.903   -4.190  1.00 48.88  ? 176  LYS A N   1 
ATOM   1304 C  CA  . LYS A 1 176 ? 35.152  6.037   -5.287  1.00 47.68  ? 176  LYS A CA  1 
ATOM   1305 C  C   . LYS A 1 176 ? 34.958  6.819   -6.592  1.00 52.96  ? 176  LYS A C   1 
ATOM   1306 O  O   . LYS A 1 176 ? 35.271  6.335   -7.689  1.00 48.18  ? 176  LYS A O   1 
ATOM   1307 C  CB  . LYS A 1 176 ? 33.854  5.329   -4.893  1.00 48.62  ? 176  LYS A CB  1 
ATOM   1308 C  CG  . LYS A 1 176 ? 33.739  3.893   -5.399  1.00 51.68  ? 176  LYS A CG  1 
ATOM   1309 N  N   . ARG A 1 177 ? 34.446  8.035   -6.461  0.80 44.42  ? 177  ARG A N   1 
ATOM   1310 C  CA  . ARG A 1 177 ? 34.233  8.898   -7.610  0.80 40.43  ? 177  ARG A CA  1 
ATOM   1311 C  C   . ARG A 1 177 ? 35.558  9.199   -8.284  0.80 42.69  ? 177  ARG A C   1 
ATOM   1312 O  O   . ARG A 1 177 ? 35.724  8.960   -9.482  0.80 48.40  ? 177  ARG A O   1 
ATOM   1313 C  CB  . ARG A 1 177 ? 33.574  10.195  -7.164  0.80 52.19  ? 177  ARG A CB  1 
ATOM   1314 C  CG  . ARG A 1 177 ? 32.924  10.989  -8.271  0.80 60.22  ? 177  ARG A CG  1 
ATOM   1315 C  CD  . ARG A 1 177 ? 32.292  12.242  -7.703  0.80 62.32  ? 177  ARG A CD  1 
ATOM   1316 N  NE  . ARG A 1 177 ? 31.517  11.943  -6.504  0.80 66.61  ? 177  ARG A NE  1 
ATOM   1317 C  CZ  . ARG A 1 177 ? 30.262  11.508  -6.518  0.80 75.14  ? 177  ARG A CZ  1 
ATOM   1318 N  NH1 . ARG A 1 177 ? 29.638  11.328  -7.678  0.80 74.51  ? 177  ARG A NH1 1 
ATOM   1319 N  NH2 . ARG A 1 177 ? 29.629  11.256  -5.375  0.80 73.01  ? 177  ARG A NH2 1 
ATOM   1320 N  N   . VAL A 1 178 ? 36.512  9.714   -7.512  1.00 46.54  ? 178  VAL A N   1 
ATOM   1321 C  CA  . VAL A 1 178 ? 37.793  10.102  -8.088  1.00 44.52  ? 178  VAL A CA  1 
ATOM   1322 C  C   . VAL A 1 178 ? 38.626  8.922   -8.596  1.00 39.26  ? 178  VAL A C   1 
ATOM   1323 O  O   . VAL A 1 178 ? 39.297  9.054   -9.611  1.00 41.19  ? 178  VAL A O   1 
ATOM   1324 C  CB  . VAL A 1 178 ? 38.647  11.053  -7.169  1.00 42.17  ? 178  VAL A CB  1 
ATOM   1325 C  CG1 . VAL A 1 178 ? 37.792  12.154  -6.588  1.00 35.46  ? 178  VAL A CG1 1 
ATOM   1326 C  CG2 . VAL A 1 178 ? 39.369  10.291  -6.068  1.00 41.48  ? 178  VAL A CG2 1 
ATOM   1327 N  N   . THR A 1 179 ? 38.585  7.771   -7.922  1.00 38.56  ? 179  THR A N   1 
ATOM   1328 C  CA  . THR A 1 179 ? 39.379  6.628   -8.391  1.00 35.33  ? 179  THR A CA  1 
ATOM   1329 C  C   . THR A 1 179 ? 38.852  6.053   -9.705  1.00 40.77  ? 179  THR A C   1 
ATOM   1330 O  O   . THR A 1 179 ? 39.607  5.490   -10.490 1.00 47.98  ? 179  THR A O   1 
ATOM   1331 C  CB  . THR A 1 179 ? 39.490  5.482   -7.366  1.00 37.87  ? 179  THR A CB  1 
ATOM   1332 O  OG1 . THR A 1 179 ? 38.182  5.011   -7.015  1.00 44.38  ? 179  THR A OG1 1 
ATOM   1333 C  CG2 . THR A 1 179 ? 40.265  5.923   -6.127  1.00 32.55  ? 179  THR A CG2 1 
ATOM   1334 N  N   . SER A 1 180 ? 37.553  6.189   -9.935  1.00 46.23  ? 180  SER A N   1 
ATOM   1335 C  CA  . SER A 1 180 ? 36.950  5.732   -11.176 1.00 49.22  ? 180  SER A CA  1 
ATOM   1336 C  C   . SER A 1 180 ? 37.427  6.592   -12.348 1.00 54.82  ? 180  SER A C   1 
ATOM   1337 O  O   . SER A 1 180 ? 37.732  6.083   -13.418 1.00 51.69  ? 180  SER A O   1 
ATOM   1338 C  CB  . SER A 1 180 ? 35.427  5.759   -11.066 1.00 50.61  ? 180  SER A CB  1 
ATOM   1339 O  OG  . SER A 1 180 ? 34.834  5.739   -12.350 1.00 65.25  ? 180  SER A OG  1 
ATOM   1340 N  N   . ILE A 1 181 ? 37.493  7.899   -12.123 1.00 54.81  ? 181  ILE A N   1 
ATOM   1341 C  CA  . ILE A 1 181 ? 37.991  8.850   -13.106 1.00 47.18  ? 181  ILE A CA  1 
ATOM   1342 C  C   . ILE A 1 181 ? 39.488  8.682   -13.334 1.00 54.71  ? 181  ILE A C   1 
ATOM   1343 O  O   . ILE A 1 181 ? 39.958  8.638   -14.479 1.00 52.83  ? 181  ILE A O   1 
ATOM   1344 C  CB  . ILE A 1 181 ? 37.733  10.289  -12.628 1.00 52.98  ? 181  ILE A CB  1 
ATOM   1345 C  CG1 . ILE A 1 181 ? 36.233  10.598  -12.675 1.00 52.91  ? 181  ILE A CG1 1 
ATOM   1346 C  CG2 . ILE A 1 181 ? 38.517  11.289  -13.463 1.00 53.62  ? 181  ILE A CG2 1 
ATOM   1347 C  CD1 . ILE A 1 181 ? 35.866  11.925  -12.065 1.00 51.77  ? 181  ILE A CD1 1 
ATOM   1348 N  N   . ALA A 1 182 ? 40.229  8.599   -12.234 1.00 53.37  ? 182  ALA A N   1 
ATOM   1349 C  CA  . ALA A 1 182 ? 41.675  8.435   -12.267 1.00 50.14  ? 182  ALA A CA  1 
ATOM   1350 C  C   . ALA A 1 182 ? 42.058  7.165   -13.008 1.00 47.17  ? 182  ALA A C   1 
ATOM   1351 O  O   . ALA A 1 182 ? 43.016  7.147   -13.781 1.00 51.25  ? 182  ALA A O   1 
ATOM   1352 C  CB  . ALA A 1 182 ? 42.241  8.412   -10.843 1.00 51.12  ? 182  ALA A CB  1 
ATOM   1353 N  N   . ASP A 1 183 ? 41.313  6.099   -12.759 1.00 38.62  ? 183  ASP A N   1 
ATOM   1354 C  CA  . ASP A 1 183 ? 41.571  4.831   -13.422 1.00 47.25  ? 183  ASP A CA  1 
ATOM   1355 C  C   . ASP A 1 183 ? 41.306  4.902   -14.923 1.00 49.76  ? 183  ASP A C   1 
ATOM   1356 O  O   . ASP A 1 183 ? 41.945  4.200   -15.698 1.00 57.22  ? 183  ASP A O   1 
ATOM   1357 C  CB  . ASP A 1 183 ? 40.723  3.717   -12.808 1.00 44.72  ? 183  ASP A CB  1 
ATOM   1358 C  CG  . ASP A 1 183 ? 41.281  3.205   -11.493 1.00 48.37  ? 183  ASP A CG  1 
ATOM   1359 O  OD1 . ASP A 1 183 ? 42.307  3.733   -11.007 1.00 49.60  ? 183  ASP A OD1 1 
ATOM   1360 O  OD2 . ASP A 1 183 ? 40.671  2.273   -10.932 1.00 50.36  ? 183  ASP A OD2 1 
ATOM   1361 N  N   . ARG A 1 184 ? 40.363  5.739   -15.336 0.80 47.10  ? 184  ARG A N   1 
ATOM   1362 C  CA  . ARG A 1 184 ? 39.993  5.809   -16.742 0.80 45.15  ? 184  ARG A CA  1 
ATOM   1363 C  C   . ARG A 1 184 ? 40.980  6.684   -17.508 0.80 49.22  ? 184  ARG A C   1 
ATOM   1364 O  O   . ARG A 1 184 ? 41.368  6.366   -18.628 0.80 50.45  ? 184  ARG A O   1 
ATOM   1365 C  CB  . ARG A 1 184 ? 38.561  6.313   -16.894 0.80 48.27  ? 184  ARG A CB  1 
ATOM   1366 C  CG  . ARG A 1 184 ? 37.893  5.911   -18.197 0.80 63.38  ? 184  ARG A CG  1 
ATOM   1367 C  CD  . ARG A 1 184 ? 36.468  5.425   -17.951 0.80 73.89  ? 184  ARG A CD  1 
ATOM   1368 N  NE  . ARG A 1 184 ? 35.569  5.738   -19.062 0.80 82.29  ? 184  ARG A NE  1 
ATOM   1369 C  CZ  . ARG A 1 184 ? 35.196  4.873   -20.000 0.80 88.43  ? 184  ARG A CZ  1 
ATOM   1370 N  NH1 . ARG A 1 184 ? 35.641  3.622   -19.964 0.80 87.85  ? 184  ARG A NH1 1 
ATOM   1371 N  NH2 . ARG A 1 184 ? 34.370  5.260   -20.970 0.80 91.35  ? 184  ARG A NH2 1 
ATOM   1372 N  N   . LEU A 1 185 ? 41.390  7.783   -16.887 1.00 55.10  ? 185  LEU A N   1 
ATOM   1373 C  CA  . LEU A 1 185 ? 42.425  8.641   -17.443 1.00 53.62  ? 185  LEU A CA  1 
ATOM   1374 C  C   . LEU A 1 185 ? 43.788  7.970   -17.331 1.00 67.77  ? 185  LEU A C   1 
ATOM   1375 O  O   . LEU A 1 185 ? 44.755  8.386   -17.976 1.00 71.47  ? 185  LEU A O   1 
ATOM   1376 C  CB  . LEU A 1 185 ? 42.458  9.985   -16.707 1.00 45.46  ? 185  LEU A CB  1 
ATOM   1377 C  CG  . LEU A 1 185 ? 41.302  10.954  -16.958 1.00 51.18  ? 185  LEU A CG  1 
ATOM   1378 C  CD1 . LEU A 1 185 ? 41.420  12.159  -16.032 1.00 49.54  ? 185  LEU A CD1 1 
ATOM   1379 C  CD2 . LEU A 1 185 ? 41.253  11.393  -18.426 1.00 47.06  ? 185  LEU A CD2 1 
ATOM   1380 N  N   . ASN A 1 186 ? 43.858  6.936   -16.497 1.00 71.35  ? 186  ASN A N   1 
ATOM   1381 C  CA  . ASN A 1 186 ? 45.113  6.249   -16.210 1.00 65.91  ? 186  ASN A CA  1 
ATOM   1382 C  C   . ASN A 1 186 ? 46.115  7.146   -15.503 1.00 57.67  ? 186  ASN A C   1 
ATOM   1383 O  O   . ASN A 1 186 ? 47.287  7.209   -15.882 1.00 57.91  ? 186  ASN A O   1 
ATOM   1384 C  CB  . ASN A 1 186 ? 45.726  5.687   -17.492 1.00 71.54  ? 186  ASN A CB  1 
ATOM   1385 C  CG  . ASN A 1 186 ? 45.723  4.175   -17.517 1.00 83.13  ? 186  ASN A CG  1 
ATOM   1386 O  OD1 . ASN A 1 186 ? 46.113  3.521   -16.544 1.00 85.30  ? 186  ASN A OD1 1 
ATOM   1387 N  ND2 . ASN A 1 186 ? 45.270  3.605   -18.630 1.00 87.99  ? 186  ASN A ND2 1 
ATOM   1388 N  N   . VAL A 1 187 ? 45.648  7.851   -14.480 1.00 45.71  ? 187  VAL A N   1 
ATOM   1389 C  CA  . VAL A 1 187 ? 46.521  8.732   -13.722 1.00 37.88  ? 187  VAL A CA  1 
ATOM   1390 C  C   . VAL A 1 187 ? 46.442  8.435   -12.229 1.00 48.13  ? 187  VAL A C   1 
ATOM   1391 O  O   . VAL A 1 187 ? 45.871  7.421   -11.816 1.00 44.03  ? 187  VAL A O   1 
ATOM   1392 C  CB  . VAL A 1 187 ? 46.225  10.213  -14.004 1.00 33.45  ? 187  VAL A CB  1 
ATOM   1393 C  CG1 . VAL A 1 187 ? 46.173  10.440  -15.497 1.00 35.71  ? 187  VAL A CG1 1 
ATOM   1394 C  CG2 . VAL A 1 187 ? 44.914  10.648  -13.345 1.00 37.77  ? 187  VAL A CG2 1 
ATOM   1395 N  N   . ASP A 1 188 ? 47.034  9.316   -11.430 1.00 50.00  ? 188  ASP A N   1 
ATOM   1396 C  CA  . ASP A 1 188 ? 47.079  9.147   -9.987  1.00 50.54  ? 188  ASP A CA  1 
ATOM   1397 C  C   . ASP A 1 188 ? 45.840  9.736   -9.328  1.00 48.72  ? 188  ASP A C   1 
ATOM   1398 O  O   . ASP A 1 188 ? 45.192  10.618  -9.890  1.00 42.25  ? 188  ASP A O   1 
ATOM   1399 C  CB  . ASP A 1 188 ? 48.326  9.830   -9.426  1.00 55.58  ? 188  ASP A CB  1 
ATOM   1400 C  CG  . ASP A 1 188 ? 49.611  9.155   -9.864  1.00 64.63  ? 188  ASP A CG  1 
ATOM   1401 O  OD1 . ASP A 1 188 ? 49.558  8.002   -10.355 1.00 64.85  ? 188  ASP A OD1 1 
ATOM   1402 O  OD2 . ASP A 1 188 ? 50.680  9.779   -9.704  1.00 68.60  ? 188  ASP A OD2 1 
ATOM   1403 N  N   . PHE A 1 189 ? 45.502  9.252   -8.138  1.00 46.98  ? 189  PHE A N   1 
ATOM   1404 C  CA  . PHE A 1 189 ? 44.434  9.879   -7.364  1.00 41.59  ? 189  PHE A CA  1 
ATOM   1405 C  C   . PHE A 1 189 ? 44.985  10.209  -6.000  1.00 38.83  ? 189  PHE A C   1 
ATOM   1406 O  O   . PHE A 1 189 ? 46.022  9.683   -5.598  1.00 33.04  ? 189  PHE A O   1 
ATOM   1407 C  CB  . PHE A 1 189 ? 43.201  8.964   -7.225  1.00 36.61  ? 189  PHE A CB  1 
ATOM   1408 C  CG  . PHE A 1 189 ? 43.384  7.852   -6.234  1.00 34.56  ? 189  PHE A CG  1 
ATOM   1409 C  CD1 . PHE A 1 189 ? 43.006  8.014   -4.912  1.00 41.79  ? 189  PHE A CD1 1 
ATOM   1410 C  CD2 . PHE A 1 189 ? 43.967  6.657   -6.618  1.00 36.04  ? 189  PHE A CD2 1 
ATOM   1411 C  CE1 . PHE A 1 189 ? 43.185  6.998   -3.997  1.00 46.01  ? 189  PHE A CE1 1 
ATOM   1412 C  CE2 . PHE A 1 189 ? 44.157  5.634   -5.704  1.00 41.30  ? 189  PHE A CE2 1 
ATOM   1413 C  CZ  . PHE A 1 189 ? 43.763  5.801   -4.394  1.00 38.91  ? 189  PHE A CZ  1 
ATOM   1414 N  N   . ALA A 1 190 ? 44.291  11.090  -5.292  1.00 40.92  ? 190  ALA A N   1 
ATOM   1415 C  CA  . ALA A 1 190 ? 44.643  11.417  -3.923  1.00 40.59  ? 190  ALA A CA  1 
ATOM   1416 C  C   . ALA A 1 190 ? 43.401  11.929  -3.211  1.00 43.77  ? 190  ALA A C   1 
ATOM   1417 O  O   . ALA A 1 190 ? 42.408  12.303  -3.843  1.00 44.15  ? 190  ALA A O   1 
ATOM   1418 C  CB  . ALA A 1 190 ? 45.762  12.444  -3.878  1.00 30.41  ? 190  ALA A CB  1 
ATOM   1419 N  N   . LEU A 1 191 ? 43.450  11.937  -1.890  1.00 49.96  ? 191  LEU A N   1 
ATOM   1420 C  CA  . LEU A 1 191 ? 42.257  12.241  -1.125  1.00 47.13  ? 191  LEU A CA  1 
ATOM   1421 C  C   . LEU A 1 191 ? 42.573  13.218  -0.014  1.00 43.99  ? 191  LEU A C   1 
ATOM   1422 O  O   . LEU A 1 191 ? 43.656  13.198  0.565   1.00 43.84  ? 191  LEU A O   1 
ATOM   1423 C  CB  . LEU A 1 191 ? 41.640  10.952  -0.576  1.00 52.14  ? 191  LEU A CB  1 
ATOM   1424 C  CG  . LEU A 1 191 ? 40.270  11.057  0.094   1.00 69.15  ? 191  LEU A CG  1 
ATOM   1425 C  CD1 . LEU A 1 191 ? 39.412  9.850   -0.245  1.00 75.17  ? 191  LEU A CD1 1 
ATOM   1426 C  CD2 . LEU A 1 191 ? 40.415  11.209  1.599   1.00 71.50  ? 191  LEU A CD2 1 
ATOM   1427 N  N   . ILE A 1 192 ? 41.620  14.089  0.267   1.00 39.77  ? 192  ILE A N   1 
ATOM   1428 C  CA  . ILE A 1 192 ? 41.772  15.032  1.348   1.00 41.79  ? 192  ILE A CA  1 
ATOM   1429 C  C   . ILE A 1 192 ? 40.803  14.679  2.468   1.00 41.70  ? 192  ILE A C   1 
ATOM   1430 O  O   . ILE A 1 192 ? 39.726  14.154  2.229   1.00 47.01  ? 192  ILE A O   1 
ATOM   1431 C  CB  . ILE A 1 192 ? 41.545  16.469  0.862   1.00 47.18  ? 192  ILE A CB  1 
ATOM   1432 C  CG1 . ILE A 1 192 ? 42.729  16.909  0.005   1.00 50.38  ? 192  ILE A CG1 1 
ATOM   1433 C  CG2 . ILE A 1 192 ? 41.347  17.411  2.038   1.00 47.65  ? 192  ILE A CG2 1 
ATOM   1434 C  CD1 . ILE A 1 192 ? 42.702  18.355  -0.391  1.00 50.82  ? 192  ILE A CD1 1 
ATOM   1435 N  N   . HIS A 1 193 ? 41.207  14.950  3.697   1.00 43.83  ? 193  HIS A N   1 
ATOM   1436 C  CA  . HIS A 1 193 ? 40.369  14.688  4.843   1.00 44.14  ? 193  HIS A CA  1 
ATOM   1437 C  C   . HIS A 1 193 ? 40.540  15.821  5.844   1.00 44.91  ? 193  HIS A C   1 
ATOM   1438 O  O   . HIS A 1 193 ? 41.665  16.154  6.211   1.00 46.01  ? 193  HIS A O   1 
ATOM   1439 C  CB  . HIS A 1 193 ? 40.764  13.349  5.475   1.00 50.67  ? 193  HIS A CB  1 
ATOM   1440 C  CG  . HIS A 1 193 ? 40.072  13.066  6.774   1.00 50.57  ? 193  HIS A CG  1 
ATOM   1441 N  ND1 . HIS A 1 193 ? 38.699  13.120  6.917   1.00 47.66  ? 193  HIS A ND1 1 
ATOM   1442 C  CD2 . HIS A 1 193 ? 40.560  12.722  7.990   1.00 46.22  ? 193  HIS A CD2 1 
ATOM   1443 C  CE1 . HIS A 1 193 ? 38.373  12.827  8.162   1.00 47.43  ? 193  HIS A CE1 1 
ATOM   1444 N  NE2 . HIS A 1 193 ? 39.485  12.581  8.835   1.00 52.89  ? 193  HIS A NE2 1 
ATOM   1445 N  N   . LYS A 1 194 ? 39.429  16.426  6.262   1.00 51.35  ? 194  LYS A N   1 
ATOM   1446 C  CA  . LYS A 1 194 ? 39.459  17.403  7.346   1.00 50.54  ? 194  LYS A CA  1 
ATOM   1447 C  C   . LYS A 1 194 ? 39.402  16.653  8.670   1.00 58.41  ? 194  LYS A C   1 
ATOM   1448 O  O   . LYS A 1 194 ? 38.389  16.027  9.013   1.00 54.88  ? 194  LYS A O   1 
ATOM   1449 C  CB  . LYS A 1 194 ? 38.314  18.415  7.236   1.00 50.49  ? 194  LYS A CB  1 
ATOM   1450 N  N   . GLU A 1 195 ? 40.504  16.706  9.409   1.00 67.13  ? 195  GLU A N   1 
ATOM   1451 C  CA  . GLU A 1 195 ? 40.620  15.959  10.652  1.00 71.07  ? 195  GLU A CA  1 
ATOM   1452 C  C   . GLU A 1 195 ? 39.614  16.458  11.690  1.00 71.99  ? 195  GLU A C   1 
ATOM   1453 O  O   . GLU A 1 195 ? 39.542  17.657  11.969  1.00 72.97  ? 195  GLU A O   1 
ATOM   1454 C  CB  . GLU A 1 195 ? 42.052  16.027  11.182  1.00 72.87  ? 195  GLU A CB  1 
ATOM   1455 C  CG  . GLU A 1 195 ? 42.579  14.694  11.685  1.00 80.95  ? 195  GLU A CG  1 
ATOM   1456 C  CD  . GLU A 1 195 ? 43.772  14.189  10.887  1.00 89.03  ? 195  GLU A CD  1 
ATOM   1457 O  OE1 . GLU A 1 195 ? 43.557  13.514  9.854   1.00 96.20  ? 195  GLU A OE1 1 
ATOM   1458 O  OE2 . GLU A 1 195 ? 44.925  14.459  11.298  1.00 84.70  ? 195  GLU A OE2 1 
ATOM   1459 N  N   . ARG A 1 196 ? 38.837  15.528  12.248  0.87 72.12  ? 196  ARG A N   1 
ATOM   1460 C  CA  . ARG A 1 196 ? 37.810  15.850  13.247  0.87 67.59  ? 196  ARG A CA  1 
ATOM   1461 C  C   . ARG A 1 196 ? 38.255  15.554  14.684  0.87 70.91  ? 196  ARG A C   1 
ATOM   1462 O  O   . ARG A 1 196 ? 39.330  14.994  14.920  0.87 74.50  ? 196  ARG A O   1 
ATOM   1463 C  CB  . ARG A 1 196 ? 36.500  15.110  12.936  0.87 48.94  ? 196  ARG A CB  1 
ATOM   1464 N  N   . ARG A 1 204 ? 42.113  21.160  10.413  1.00 76.74  ? 204  ARG A N   1 
ATOM   1465 C  CA  . ARG A 1 204 ? 43.264  20.936  9.538   1.00 82.49  ? 204  ARG A CA  1 
ATOM   1466 C  C   . ARG A 1 204 ? 42.996  19.849  8.495   1.00 72.77  ? 204  ARG A C   1 
ATOM   1467 O  O   . ARG A 1 204 ? 42.376  18.826  8.792   1.00 69.92  ? 204  ARG A O   1 
ATOM   1468 C  CB  . ARG A 1 204 ? 44.499  20.563  10.368  1.00 87.78  ? 204  ARG A CB  1 
ATOM   1469 N  N   . MET A 1 205 ? 43.477  20.067  7.276   1.00 61.76  ? 205  MET A N   1 
ATOM   1470 C  CA  . MET A 1 205 ? 43.309  19.080  6.215   1.00 58.48  ? 205  MET A CA  1 
ATOM   1471 C  C   . MET A 1 205 ? 44.545  18.201  6.026   1.00 63.53  ? 205  MET A C   1 
ATOM   1472 O  O   . MET A 1 205 ? 45.684  18.675  6.082   1.00 60.31  ? 205  MET A O   1 
ATOM   1473 C  CB  . MET A 1 205 ? 42.943  19.759  4.894   1.00 52.45  ? 205  MET A CB  1 
ATOM   1474 C  CG  . MET A 1 205 ? 41.609  20.490  4.916   1.00 56.09  ? 205  MET A CG  1 
ATOM   1475 S  SD  . MET A 1 205 ? 41.068  20.995  3.271   1.00 81.72  ? 205  MET A SD  1 
ATOM   1476 N  N   . VAL A 1 206 ? 44.310  16.914  5.795   1.00 60.15  ? 206  VAL A N   1 
ATOM   1477 C  CA  . VAL A 1 206 ? 45.386  15.989  5.478   1.00 55.60  ? 206  VAL A CA  1 
ATOM   1478 C  C   . VAL A 1 206 ? 45.233  15.523  4.033   1.00 50.81  ? 206  VAL A C   1 
ATOM   1479 O  O   . VAL A 1 206 ? 44.123  15.300  3.570   1.00 47.24  ? 206  VAL A O   1 
ATOM   1480 C  CB  . VAL A 1 206 ? 45.383  14.769  6.429   1.00 57.15  ? 206  VAL A CB  1 
ATOM   1481 C  CG1 . VAL A 1 206 ? 46.350  13.706  5.946   1.00 63.26  ? 206  VAL A CG1 1 
ATOM   1482 C  CG2 . VAL A 1 206 ? 45.745  15.194  7.830   1.00 51.22  ? 206  VAL A CG2 1 
ATOM   1483 N  N   . LEU A 1 207 ? 46.348  15.386  3.324   1.00 55.34  ? 207  LEU A N   1 
ATOM   1484 C  CA  . LEU A 1 207 ? 46.321  14.852  1.970   1.00 60.55  ? 207  LEU A CA  1 
ATOM   1485 C  C   . LEU A 1 207 ? 47.135  13.565  1.866   1.00 57.82  ? 207  LEU A C   1 
ATOM   1486 O  O   . LEU A 1 207 ? 48.301  13.519  2.261   1.00 55.46  ? 207  LEU A O   1 
ATOM   1487 C  CB  . LEU A 1 207 ? 46.844  15.889  0.976   1.00 67.65  ? 207  LEU A CB  1 
ATOM   1488 C  CG  . LEU A 1 207 ? 46.726  15.574  -0.520  1.00 68.15  ? 207  LEU A CG  1 
ATOM   1489 C  CD1 . LEU A 1 207 ? 46.814  16.851  -1.336  1.00 76.13  ? 207  LEU A CD1 1 
ATOM   1490 C  CD2 . LEU A 1 207 ? 47.791  14.590  -0.952  1.00 59.35  ? 207  LEU A CD2 1 
ATOM   1491 N  N   . VAL A 1 208 ? 46.505  12.519  1.341   1.00 48.09  ? 208  VAL A N   1 
ATOM   1492 C  CA  . VAL A 1 208 ? 47.188  11.261  1.087   1.00 49.62  ? 208  VAL A CA  1 
ATOM   1493 C  C   . VAL A 1 208 ? 47.199  10.972  -0.412  1.00 52.02  ? 208  VAL A C   1 
ATOM   1494 O  O   . VAL A 1 208 ? 46.170  11.076  -1.083  1.00 50.60  ? 208  VAL A O   1 
ATOM   1495 C  CB  . VAL A 1 208 ? 46.540  10.086  1.855   1.00 41.20  ? 208  VAL A CB  1 
ATOM   1496 C  CG1 . VAL A 1 208 ? 46.532  10.376  3.350   1.00 42.68  ? 208  VAL A CG1 1 
ATOM   1497 C  CG2 . VAL A 1 208 ? 45.128  9.826   1.349   1.00 35.45  ? 208  VAL A CG2 1 
ATOM   1498 N  N   . GLY A 1 209 ? 48.367  10.606  -0.928  1.00 43.83  ? 209  GLY A N   1 
ATOM   1499 C  CA  . GLY A 1 209 ? 48.558  10.424  -2.359  1.00 52.08  ? 209  GLY A CA  1 
ATOM   1500 C  C   . GLY A 1 209 ? 49.416  11.571  -2.846  1.00 51.64  ? 209  GLY A C   1 
ATOM   1501 O  O   . GLY A 1 209 ? 49.545  12.570  -2.148  1.00 56.95  ? 209  GLY A O   1 
ATOM   1502 N  N   . ASP A 1 210 ? 50.021  11.457  -4.018  0.80 50.83  ? 210  ASP A N   1 
ATOM   1503 C  CA  . ASP A 1 210 ? 50.912  12.535  -4.421  0.80 56.18  ? 210  ASP A CA  1 
ATOM   1504 C  C   . ASP A 1 210 ? 50.403  13.490  -5.486  0.80 51.82  ? 210  ASP A C   1 
ATOM   1505 O  O   . ASP A 1 210 ? 49.697  13.101  -6.412  0.80 47.47  ? 210  ASP A O   1 
ATOM   1506 C  CB  . ASP A 1 210 ? 52.299  12.046  -4.811  0.80 70.66  ? 210  ASP A CB  1 
ATOM   1507 C  CG  . ASP A 1 210 ? 53.259  13.198  -4.953  0.80 76.00  ? 210  ASP A CG  1 
ATOM   1508 O  OD1 . ASP A 1 210 ? 53.559  13.818  -3.894  0.80 74.07  ? 210  ASP A OD1 1 
ATOM   1509 O  OD2 . ASP A 1 210 ? 53.644  13.533  -6.115  0.80 84.73  ? 210  ASP A OD2 1 
ATOM   1510 N  N   . VAL A 1 211 ? 50.806  14.748  -5.344  1.00 52.98  ? 211  VAL A N   1 
ATOM   1511 C  CA  . VAL A 1 211 ? 50.361  15.819  -6.233  1.00 59.16  ? 211  VAL A CA  1 
ATOM   1512 C  C   . VAL A 1 211 ? 51.479  16.795  -6.595  1.00 58.09  ? 211  VAL A C   1 
ATOM   1513 O  O   . VAL A 1 211 ? 51.265  17.732  -7.372  1.00 64.72  ? 211  VAL A O   1 
ATOM   1514 C  CB  . VAL A 1 211 ? 49.212  16.643  -5.602  1.00 60.70  ? 211  VAL A CB  1 
ATOM   1515 C  CG1 . VAL A 1 211 ? 48.027  15.753  -5.266  1.00 55.59  ? 211  VAL A CG1 1 
ATOM   1516 C  CG2 . VAL A 1 211 ? 49.704  17.391  -4.362  1.00 62.25  ? 211  VAL A CG2 1 
ATOM   1517 N  N   . LYS A 1 212 ? 52.663  16.587  -6.023  1.00 59.63  ? 212  LYS A N   1 
ATOM   1518 C  CA  . LYS A 1 212 ? 53.779  17.507  -6.225  1.00 69.00  ? 212  LYS A CA  1 
ATOM   1519 C  C   . LYS A 1 212 ? 54.168  17.611  -7.698  1.00 68.58  ? 212  LYS A C   1 
ATOM   1520 O  O   . LYS A 1 212 ? 54.370  16.594  -8.372  1.00 61.67  ? 212  LYS A O   1 
ATOM   1521 C  CB  . LYS A 1 212 ? 54.992  17.088  -5.380  1.00 70.65  ? 212  LYS A CB  1 
ATOM   1522 N  N   . ASP A 1 213 ? 54.269  18.844  -8.192  1.00 68.28  ? 213  ASP A N   1 
ATOM   1523 C  CA  . ASP A 1 213 ? 54.687  19.090  -9.569  1.00 70.54  ? 213  ASP A CA  1 
ATOM   1524 C  C   . ASP A 1 213 ? 53.809  18.346  -10.558 1.00 69.56  ? 213  ASP A C   1 
ATOM   1525 O  O   . ASP A 1 213 ? 54.306  17.683  -11.472 1.00 77.95  ? 213  ASP A O   1 
ATOM   1526 C  CB  . ASP A 1 213 ? 56.145  18.673  -9.786  1.00 69.75  ? 213  ASP A CB  1 
ATOM   1527 C  CG  . ASP A 1 213 ? 57.083  19.277  -8.766  1.00 76.15  ? 213  ASP A CG  1 
ATOM   1528 O  OD1 . ASP A 1 213 ? 57.999  18.553  -8.322  1.00 80.27  ? 213  ASP A OD1 1 
ATOM   1529 O  OD2 . ASP A 1 213 ? 56.906  20.464  -8.408  1.00 76.12  ? 213  ASP A OD2 1 
ATOM   1530 N  N   . ARG A 1 214 ? 52.504  18.445  -10.365 0.80 55.35  ? 214  ARG A N   1 
ATOM   1531 C  CA  . ARG A 1 214 ? 51.559  17.887  -11.312 0.80 59.95  ? 214  ARG A CA  1 
ATOM   1532 C  C   . ARG A 1 214 ? 50.227  18.595  -11.144 0.80 53.72  ? 214  ARG A C   1 
ATOM   1533 O  O   . ARG A 1 214 ? 49.927  19.125  -10.078 0.80 53.41  ? 214  ARG A O   1 
ATOM   1534 C  CB  . ARG A 1 214 ? 51.425  16.373  -11.130 0.80 67.52  ? 214  ARG A CB  1 
ATOM   1535 C  CG  . ARG A 1 214 ? 51.206  15.931  -9.702  0.80 74.95  ? 214  ARG A CG  1 
ATOM   1536 C  CD  . ARG A 1 214 ? 51.634  14.481  -9.479  0.80 73.44  ? 214  ARG A CD  1 
ATOM   1537 N  NE  . ARG A 1 214 ? 50.807  13.533  -10.216 0.80 68.93  ? 214  ARG A NE  1 
ATOM   1538 C  CZ  . ARG A 1 214 ? 51.190  12.911  -11.325 0.80 63.59  ? 214  ARG A CZ  1 
ATOM   1539 N  NH1 . ARG A 1 214 ? 52.402  13.129  -11.819 0.80 65.21  ? 214  ARG A NH1 1 
ATOM   1540 N  NH2 . ARG A 1 214 ? 50.367  12.062  -11.934 0.80 52.65  ? 214  ARG A NH2 1 
ATOM   1541 N  N   . VAL A 1 215 ? 49.442  18.640  -12.208 1.00 48.78  ? 215  VAL A N   1 
ATOM   1542 C  CA  . VAL A 1 215 ? 48.168  19.330  -12.143 1.00 50.12  ? 215  VAL A CA  1 
ATOM   1543 C  C   . VAL A 1 215 ? 47.199  18.511  -11.309 1.00 54.43  ? 215  VAL A C   1 
ATOM   1544 O  O   . VAL A 1 215 ? 47.099  17.296  -11.476 1.00 56.28  ? 215  VAL A O   1 
ATOM   1545 C  CB  . VAL A 1 215 ? 47.607  19.597  -13.541 1.00 47.16  ? 215  VAL A CB  1 
ATOM   1546 C  CG1 . VAL A 1 215 ? 46.241  20.266  -13.454 1.00 49.49  ? 215  VAL A CG1 1 
ATOM   1547 C  CG2 . VAL A 1 215 ? 48.579  20.469  -14.317 1.00 43.70  ? 215  VAL A CG2 1 
ATOM   1548 N  N   . ALA A 1 216 ? 46.496  19.176  -10.401 1.00 56.59  ? 216  ALA A N   1 
ATOM   1549 C  CA  . ALA A 1 216 ? 45.541  18.485  -9.542  1.00 52.61  ? 216  ALA A CA  1 
ATOM   1550 C  C   . ALA A 1 216 ? 44.111  18.889  -9.862  1.00 54.65  ? 216  ALA A C   1 
ATOM   1551 O  O   . ALA A 1 216 ? 43.761  20.070  -9.832  1.00 51.01  ? 216  ALA A O   1 
ATOM   1552 C  CB  . ALA A 1 216 ? 45.858  18.733  -8.075  1.00 41.89  ? 216  ALA A CB  1 
ATOM   1553 N  N   . ILE A 1 217 ? 43.290  17.892  -10.174 1.00 53.62  ? 217  ILE A N   1 
ATOM   1554 C  CA  . ILE A 1 217 ? 41.898  18.136  -10.516 1.00 55.69  ? 217  ILE A CA  1 
ATOM   1555 C  C   . ILE A 1 217 ? 40.991  17.691  -9.384  1.00 53.09  ? 217  ILE A C   1 
ATOM   1556 O  O   . ILE A 1 217 ? 40.804  16.499  -9.163  1.00 51.71  ? 217  ILE A O   1 
ATOM   1557 C  CB  . ILE A 1 217 ? 41.496  17.384  -11.798 1.00 56.39  ? 217  ILE A CB  1 
ATOM   1558 C  CG1 . ILE A 1 217 ? 42.559  17.566  -12.880 1.00 46.53  ? 217  ILE A CG1 1 
ATOM   1559 C  CG2 . ILE A 1 217 ? 40.122  17.841  -12.296 1.00 50.85  ? 217  ILE A CG2 1 
ATOM   1560 C  CD1 . ILE A 1 217 ? 42.259  16.793  -14.131 1.00 46.72  ? 217  ILE A CD1 1 
ATOM   1561 N  N   . LEU A 1 218 ? 40.433  18.654  -8.661  1.00 46.07  ? 218  LEU A N   1 
ATOM   1562 C  CA  . LEU A 1 218 ? 39.473  18.333  -7.622  1.00 39.21  ? 218  LEU A CA  1 
ATOM   1563 C  C   . LEU A 1 218 ? 38.156  17.963  -8.280  1.00 49.60  ? 218  LEU A C   1 
ATOM   1564 O  O   . LEU A 1 218 ? 37.619  18.721  -9.089  1.00 47.56  ? 218  LEU A O   1 
ATOM   1565 C  CB  . LEU A 1 218 ? 39.278  19.501  -6.672  1.00 35.92  ? 218  LEU A CB  1 
ATOM   1566 C  CG  . LEU A 1 218 ? 40.363  19.682  -5.616  1.00 42.75  ? 218  LEU A CG  1 
ATOM   1567 C  CD1 . LEU A 1 218 ? 40.298  21.100  -5.038  1.00 49.58  ? 218  LEU A CD1 1 
ATOM   1568 C  CD2 . LEU A 1 218 ? 40.273  18.614  -4.504  1.00 38.82  ? 218  LEU A CD2 1 
ATOM   1569 N  N   . VAL A 1 219 ? 37.654  16.781  -7.944  1.00 47.87  ? 219  VAL A N   1 
ATOM   1570 C  CA  . VAL A 1 219 ? 36.413  16.290  -8.514  1.00 46.64  ? 219  VAL A CA  1 
ATOM   1571 C  C   . VAL A 1 219 ? 35.431  15.946  -7.417  1.00 45.02  ? 219  VAL A C   1 
ATOM   1572 O  O   . VAL A 1 219 ? 35.781  15.282  -6.444  1.00 46.40  ? 219  VAL A O   1 
ATOM   1573 C  CB  . VAL A 1 219 ? 36.630  15.035  -9.366  1.00 47.78  ? 219  VAL A CB  1 
ATOM   1574 C  CG1 . VAL A 1 219 ? 35.297  14.498  -9.841  1.00 50.67  ? 219  VAL A CG1 1 
ATOM   1575 C  CG2 . VAL A 1 219 ? 37.538  15.343  -10.539 1.00 42.82  ? 219  VAL A CG2 1 
ATOM   1576 N  N   . ASP A 1 220 ? 34.195  16.381  -7.604  1.00 46.95  ? 220  ASP A N   1 
ATOM   1577 C  CA  . ASP A 1 220 ? 33.146  16.212  -6.618  1.00 49.55  ? 220  ASP A CA  1 
ATOM   1578 C  C   . ASP A 1 220 ? 31.812  16.132  -7.369  1.00 48.53  ? 220  ASP A C   1 
ATOM   1579 O  O   . ASP A 1 220 ? 31.718  16.537  -8.539  1.00 41.67  ? 220  ASP A O   1 
ATOM   1580 C  CB  . ASP A 1 220 ? 33.172  17.401  -5.654  1.00 50.37  ? 220  ASP A CB  1 
ATOM   1581 C  CG  . ASP A 1 220 ? 32.434  17.128  -4.361  1.00 64.66  ? 220  ASP A CG  1 
ATOM   1582 O  OD1 . ASP A 1 220 ? 32.076  15.956  -4.106  1.00 59.86  ? 220  ASP A OD1 1 
ATOM   1583 O  OD2 . ASP A 1 220 ? 32.222  18.095  -3.591  1.00 76.00  ? 220  ASP A OD2 1 
ATOM   1584 N  N   . ASP A 1 221 ? 30.788  15.591  -6.723  1.00 47.91  ? 221  ASP A N   1 
ATOM   1585 C  CA  . ASP A 1 221 ? 29.491  15.497  -7.379  1.00 48.83  ? 221  ASP A CA  1 
ATOM   1586 C  C   . ASP A 1 221 ? 28.735  16.813  -7.251  1.00 51.87  ? 221  ASP A C   1 
ATOM   1587 O  O   . ASP A 1 221 ? 27.939  17.158  -8.126  1.00 54.63  ? 221  ASP A O   1 
ATOM   1588 C  CB  . ASP A 1 221 ? 28.662  14.351  -6.816  1.00 53.45  ? 221  ASP A CB  1 
ATOM   1589 C  CG  . ASP A 1 221 ? 28.243  14.589  -5.381  1.00 60.58  ? 221  ASP A CG  1 
ATOM   1590 O  OD1 . ASP A 1 221 ? 27.047  14.388  -5.080  1.00 59.29  ? 221  ASP A OD1 1 
ATOM   1591 O  OD2 . ASP A 1 221 ? 29.107  14.983  -4.564  1.00 64.74  ? 221  ASP A OD2 1 
ATOM   1592 N  N   . MET A 1 222 ? 28.995  17.550  -6.170  1.00 47.27  ? 222  MET A N   1 
ATOM   1593 C  CA  . MET A 1 222 ? 28.338  18.835  -5.958  1.00 55.09  ? 222  MET A CA  1 
ATOM   1594 C  C   . MET A 1 222 ? 29.082  19.747  -4.988  1.00 56.42  ? 222  MET A C   1 
ATOM   1595 O  O   . MET A 1 222 ? 29.734  19.280  -4.061  1.00 65.21  ? 222  MET A O   1 
ATOM   1596 C  CB  . MET A 1 222 ? 26.899  18.624  -5.482  1.00 61.29  ? 222  MET A CB  1 
ATOM   1597 C  CG  . MET A 1 222 ? 26.754  18.240  -4.012  1.00 56.69  ? 222  MET A CG  1 
ATOM   1598 S  SD  . MET A 1 222 ? 25.105  17.577  -3.669  1.00 87.87  ? 222  MET A SD  1 
ATOM   1599 C  CE  . MET A 1 222 ? 24.082  18.589  -4.750  1.00 51.86  ? 222  MET A CE  1 
ATOM   1600 N  N   . ALA A 1 223 ? 28.985  21.053  -5.218  1.00 57.89  ? 223  ALA A N   1 
ATOM   1601 C  CA  . ALA A 1 223 ? 29.594  22.051  -4.336  1.00 60.01  ? 223  ALA A CA  1 
ATOM   1602 C  C   . ALA A 1 223 ? 28.570  23.108  -4.003  1.00 68.06  ? 223  ALA A C   1 
ATOM   1603 O  O   . ALA A 1 223 ? 27.973  23.700  -4.893  1.00 71.25  ? 223  ALA A O   1 
ATOM   1604 C  CB  . ALA A 1 223 ? 30.800  22.692  -4.981  1.00 46.34  ? 223  ALA A CB  1 
ATOM   1605 N  N   . ASP A 1 224 ? 28.367  23.336  -2.714  1.00 72.81  ? 224  ASP A N   1 
ATOM   1606 C  CA  . ASP A 1 224 ? 27.383  24.267  -2.257  1.00 73.40  ? 224  ASP A CA  1 
ATOM   1607 C  C   . ASP A 1 224 ? 27.867  25.681  -1.881  1.00 74.95  ? 224  ASP A C   1 
ATOM   1608 O  O   . ASP A 1 224 ? 27.521  26.668  -2.524  1.00 80.05  ? 224  ASP A O   1 
ATOM   1609 C  CB  . ASP A 1 224 ? 26.687  23.760  -1.004  1.00 74.21  ? 224  ASP A CB  1 
ATOM   1610 C  CG  . ASP A 1 224 ? 25.488  24.579  -0.626  1.00 77.06  ? 224  ASP A CG  1 
ATOM   1611 O  OD1 . ASP A 1 224 ? 25.075  25.407  -1.461  1.00 79.63  ? 224  ASP A OD1 1 
ATOM   1612 O  OD2 . ASP A 1 224 ? 24.958  24.395  0.489   1.00 78.42  ? 224  ASP A OD2 1 
ATOM   1613 N  N   . THR A 1 225 ? 28.692  25.749  -0.843  1.00 68.57  ? 225  THR A N   1 
ATOM   1614 C  CA  . THR A 1 225 ? 29.246  26.995  -0.371  1.00 68.39  ? 225  THR A CA  1 
ATOM   1615 C  C   . THR A 1 225 ? 30.723  27.045  -0.755  1.00 69.59  ? 225  THR A C   1 
ATOM   1616 O  O   . THR A 1 225 ? 31.385  28.076  -0.625  1.00 66.70  ? 225  THR A O   1 
ATOM   1617 C  CB  . THR A 1 225 ? 29.088  27.241  1.129   1.00 70.82  ? 225  THR A CB  1 
ATOM   1618 O  OG1 . THR A 1 225 ? 29.529  26.069  1.830   1.00 70.36  ? 225  THR A OG1 1 
ATOM   1619 C  CG2 . THR A 1 225 ? 27.629  27.499  1.464   1.00 72.47  ? 225  THR A CG2 1 
ATOM   1620 N  N   . CYS A 1 226 ? 31.230  25.903  -1.220  1.00 66.05  ? 226  CYS A N   1 
ATOM   1621 C  CA  . CYS A 1 226 ? 32.589  25.783  -1.753  1.00 59.11  ? 226  CYS A CA  1 
ATOM   1622 C  C   . CYS A 1 226 ? 33.669  25.949  -0.703  1.00 59.82  ? 226  CYS A C   1 
ATOM   1623 O  O   . CYS A 1 226 ? 34.840  26.121  -1.040  1.00 57.20  ? 226  CYS A O   1 
ATOM   1624 C  CB  . CYS A 1 226 ? 32.826  26.785  -2.882  1.00 59.75  ? 226  CYS A CB  1 
ATOM   1625 S  SG  . CYS A 1 226 ? 31.848  26.469  -4.349  1.00 65.72  ? 226  CYS A SG  1 
ATOM   1626 N  N   . GLY A 1 227 ? 33.276  25.907  0.565   1.00 58.88  ? 227  GLY A N   1 
ATOM   1627 C  CA  . GLY A 1 227 ? 34.228  26.061  1.644   1.00 61.57  ? 227  GLY A CA  1 
ATOM   1628 C  C   . GLY A 1 227 ? 35.207  24.909  1.665   1.00 63.93  ? 227  GLY A C   1 
ATOM   1629 O  O   . GLY A 1 227 ? 36.408  25.092  1.878   1.00 72.99  ? 227  GLY A O   1 
ATOM   1630 N  N   . THR A 1 228 ? 34.678  23.716  1.428   1.00 59.48  ? 228  THR A N   1 
ATOM   1631 C  CA  . THR A 1 228 ? 35.468  22.497  1.432   1.00 58.65  ? 228  THR A CA  1 
ATOM   1632 C  C   . THR A 1 228 ? 36.379  22.433  0.204   1.00 62.51  ? 228  THR A C   1 
ATOM   1633 O  O   . THR A 1 228 ? 37.583  22.210  0.320   1.00 54.49  ? 228  THR A O   1 
ATOM   1634 C  CB  . THR A 1 228 ? 34.543  21.263  1.520   1.00 49.63  ? 228  THR A CB  1 
ATOM   1635 O  OG1 . THR A 1 228 ? 34.253  20.991  2.897   1.00 56.73  ? 228  THR A OG1 1 
ATOM   1636 C  CG2 . THR A 1 228 ? 35.178  20.038  0.887   1.00 41.76  ? 228  THR A CG2 1 
ATOM   1637 N  N   . ILE A 1 229 ? 35.803  22.662  -0.970  1.00 68.99  ? 229  ILE A N   1 
ATOM   1638 C  CA  . ILE A 1 229 ? 36.564  22.587  -2.208  1.00 72.55  ? 229  ILE A CA  1 
ATOM   1639 C  C   . ILE A 1 229 ? 37.657  23.664  -2.274  1.00 67.88  ? 229  ILE A C   1 
ATOM   1640 O  O   . ILE A 1 229 ? 38.743  23.425  -2.807  1.00 61.64  ? 229  ILE A O   1 
ATOM   1641 C  CB  . ILE A 1 229 ? 35.631  22.653  -3.447  1.00 63.28  ? 229  ILE A CB  1 
ATOM   1642 C  CG1 . ILE A 1 229 ? 36.103  21.672  -4.527  1.00 61.41  ? 229  ILE A CG1 1 
ATOM   1643 C  CG2 . ILE A 1 229 ? 35.504  24.087  -3.969  1.00 57.26  ? 229  ILE A CG2 1 
ATOM   1644 N  N   . CYS A 1 230 ? 37.373  24.836  -1.706  1.00 65.88  ? 230  CYS A N   1 
ATOM   1645 C  CA  . CYS A 1 230 ? 38.311  25.960  -1.718  1.00 56.30  ? 230  CYS A CA  1 
ATOM   1646 C  C   . CYS A 1 230 ? 39.459  25.790  -0.732  1.00 54.74  ? 230  CYS A C   1 
ATOM   1647 O  O   . CYS A 1 230 ? 40.585  26.195  -1.011  1.00 49.30  ? 230  CYS A O   1 
ATOM   1648 C  CB  . CYS A 1 230 ? 37.582  27.277  -1.444  1.00 63.08  ? 230  CYS A CB  1 
ATOM   1649 S  SG  . CYS A 1 230 ? 36.796  27.996  -2.909  1.00 78.45  ? 230  CYS A SG  1 
ATOM   1650 N  N   . HIS A 1 231 ? 39.184  25.202  0.426   1.00 54.01  ? 231  HIS A N   1 
ATOM   1651 C  CA  . HIS A 1 231 ? 40.269  24.817  1.317   1.00 67.15  ? 231  HIS A CA  1 
ATOM   1652 C  C   . HIS A 1 231 ? 41.161  23.781  0.639   1.00 66.16  ? 231  HIS A C   1 
ATOM   1653 O  O   . HIS A 1 231 ? 42.367  23.972  0.520   1.00 72.97  ? 231  HIS A O   1 
ATOM   1654 C  CB  . HIS A 1 231 ? 39.731  24.275  2.641   1.00 77.11  ? 231  HIS A CB  1 
ATOM   1655 C  CG  . HIS A 1 231 ? 39.213  25.338  3.555   1.00 87.17  ? 231  HIS A CG  1 
ATOM   1656 N  ND1 . HIS A 1 231 ? 39.896  26.513  3.785   1.00 90.26  ? 231  HIS A ND1 1 
ATOM   1657 C  CD2 . HIS A 1 231 ? 38.082  25.408  4.294   1.00 92.48  ? 231  HIS A CD2 1 
ATOM   1658 C  CE1 . HIS A 1 231 ? 39.207  27.263  4.626   1.00 92.23  ? 231  HIS A CE1 1 
ATOM   1659 N  NE2 . HIS A 1 231 ? 38.102  26.615  4.951   1.00 94.56  ? 231  HIS A NE2 1 
ATOM   1660 N  N   . ALA A 1 232 ? 40.555  22.689  0.186   1.00 58.47  ? 232  ALA A N   1 
ATOM   1661 C  CA  . ALA A 1 232 ? 41.288  21.630  -0.492  1.00 50.71  ? 232  ALA A CA  1 
ATOM   1662 C  C   . ALA A 1 232 ? 42.260  22.187  -1.524  1.00 51.67  ? 232  ALA A C   1 
ATOM   1663 O  O   . ALA A 1 232 ? 43.372  21.670  -1.677  1.00 53.27  ? 232  ALA A O   1 
ATOM   1664 C  CB  . ALA A 1 232 ? 40.321  20.642  -1.145  1.00 42.98  ? 232  ALA A CB  1 
ATOM   1665 N  N   . ALA A 1 233 ? 41.838  23.240  -2.225  1.00 47.28  ? 233  ALA A N   1 
ATOM   1666 C  CA  . ALA A 1 233 ? 42.671  23.871  -3.247  1.00 54.03  ? 233  ALA A CA  1 
ATOM   1667 C  C   . ALA A 1 233 ? 43.959  24.482  -2.681  1.00 58.48  ? 233  ALA A C   1 
ATOM   1668 O  O   . ALA A 1 233 ? 45.033  24.322  -3.260  1.00 59.11  ? 233  ALA A O   1 
ATOM   1669 C  CB  . ALA A 1 233 ? 41.870  24.922  -4.018  1.00 57.52  ? 233  ALA A CB  1 
ATOM   1670 N  N   . ASP A 1 234 ? 43.837  25.193  -1.562  1.00 61.50  ? 234  ASP A N   1 
ATOM   1671 C  CA  . ASP A 1 234 ? 44.988  25.727  -0.834  1.00 63.12  ? 234  ASP A CA  1 
ATOM   1672 C  C   . ASP A 1 234 ? 45.971  24.622  -0.477  1.00 54.20  ? 234  ASP A C   1 
ATOM   1673 O  O   . ASP A 1 234 ? 47.143  24.658  -0.861  1.00 52.39  ? 234  ASP A O   1 
ATOM   1674 C  CB  . ASP A 1 234 ? 44.533  26.403  0.459   1.00 73.97  ? 234  ASP A CB  1 
ATOM   1675 C  CG  . ASP A 1 234 ? 43.932  27.778  0.226   1.00 84.64  ? 234  ASP A CG  1 
ATOM   1676 O  OD1 . ASP A 1 234 ? 44.561  28.584  -0.499  1.00 86.49  ? 234  ASP A OD1 1 
ATOM   1677 O  OD2 . ASP A 1 234 ? 42.839  28.053  0.777   1.00 87.69  ? 234  ASP A OD2 1 
ATOM   1678 N  N   . LYS A 1 235 ? 45.485  23.651  0.284   0.60 44.26  ? 235  LYS A N   1 
ATOM   1679 C  CA  . LYS A 1 235 ? 46.289  22.509  0.692   0.60 43.34  ? 235  LYS A CA  1 
ATOM   1680 C  C   . LYS A 1 235 ? 46.948  21.879  -0.522  0.60 40.58  ? 235  LYS A C   1 
ATOM   1681 O  O   . LYS A 1 235 ? 48.116  21.504  -0.486  0.60 33.71  ? 235  LYS A O   1 
ATOM   1682 C  CB  . LYS A 1 235 ? 45.403  21.491  1.413   0.60 43.48  ? 235  LYS A CB  1 
ATOM   1683 C  CG  . LYS A 1 235 ? 46.081  20.144  1.791   0.60 48.55  ? 235  LYS A CG  1 
ATOM   1684 C  CD  . LYS A 1 235 ? 46.950  20.289  3.019   0.60 40.19  ? 235  LYS A CD  1 
ATOM   1685 C  CE  . LYS A 1 235 ? 47.725  19.002  3.321   0.60 43.46  ? 235  LYS A CE  1 
ATOM   1686 N  NZ  . LYS A 1 235 ? 48.351  19.105  4.694   0.60 45.96  ? 235  LYS A NZ  1 
ATOM   1687 N  N   . LEU A 1 236 ? 46.188  21.778  -1.604  1.00 56.24  ? 236  LEU A N   1 
ATOM   1688 C  CA  . LEU A 1 236 ? 46.701  21.220  -2.850  1.00 64.03  ? 236  LEU A CA  1 
ATOM   1689 C  C   . LEU A 1 236 ? 47.873  22.036  -3.393  1.00 72.27  ? 236  LEU A C   1 
ATOM   1690 O  O   . LEU A 1 236 ? 48.810  21.484  -3.977  1.00 77.48  ? 236  LEU A O   1 
ATOM   1691 C  CB  . LEU A 1 236 ? 45.590  21.122  -3.901  1.00 61.44  ? 236  LEU A CB  1 
ATOM   1692 C  CG  . LEU A 1 236 ? 44.669  19.899  -3.872  1.00 59.30  ? 236  LEU A CG  1 
ATOM   1693 C  CD1 . LEU A 1 236 ? 43.667  19.984  -5.004  1.00 55.53  ? 236  LEU A CD1 1 
ATOM   1694 C  CD2 . LEU A 1 236 ? 45.483  18.608  -3.973  1.00 53.57  ? 236  LEU A CD2 1 
ATOM   1695 N  N   . LEU A 1 237 ? 47.816  23.349  -3.205  1.00 68.78  ? 237  LEU A N   1 
ATOM   1696 C  CA  . LEU A 1 237 ? 48.920  24.219  -3.591  1.00 67.93  ? 237  LEU A CA  1 
ATOM   1697 C  C   . LEU A 1 237 ? 50.065  24.125  -2.596  1.00 68.40  ? 237  LEU A C   1 
ATOM   1698 O  O   . LEU A 1 237 ? 51.227  23.979  -2.984  1.00 71.48  ? 237  LEU A O   1 
ATOM   1699 C  CB  . LEU A 1 237 ? 48.452  25.662  -3.728  1.00 64.84  ? 237  LEU A CB  1 
ATOM   1700 C  CG  . LEU A 1 237 ? 47.881  25.962  -5.112  1.00 68.55  ? 237  LEU A CG  1 
ATOM   1701 C  CD1 . LEU A 1 237 ? 47.544  27.438  -5.246  1.00 72.56  ? 237  LEU A CD1 1 
ATOM   1702 C  CD2 . LEU A 1 237 ? 48.887  25.556  -6.178  1.00 64.06  ? 237  LEU A CD2 1 
ATOM   1703 N  N   . SER A 1 238 ? 49.729  24.214  -1.314  1.00 65.44  ? 238  SER A N   1 
ATOM   1704 C  CA  . SER A 1 238 ? 50.696  23.967  -0.251  1.00 72.16  ? 238  SER A CA  1 
ATOM   1705 C  C   . SER A 1 238 ? 51.465  22.674  -0.523  1.00 71.80  ? 238  SER A C   1 
ATOM   1706 O  O   . SER A 1 238 ? 52.667  22.578  -0.269  1.00 74.72  ? 238  SER A O   1 
ATOM   1707 C  CB  . SER A 1 238 ? 49.979  23.872  1.096   1.00 76.88  ? 238  SER A CB  1 
ATOM   1708 O  OG  . SER A 1 238 ? 49.103  24.972  1.278   1.00 82.80  ? 238  SER A OG  1 
ATOM   1709 N  N   . ALA A 1 239 ? 50.761  21.679  -1.051  1.00 66.94  ? 239  ALA A N   1 
ATOM   1710 C  CA  . ALA A 1 239 ? 51.353  20.373  -1.322  1.00 61.60  ? 239  ALA A CA  1 
ATOM   1711 C  C   . ALA A 1 239 ? 52.245  20.381  -2.556  1.00 62.04  ? 239  ALA A C   1 
ATOM   1712 O  O   . ALA A 1 239 ? 53.008  19.446  -2.776  1.00 68.36  ? 239  ALA A O   1 
ATOM   1713 C  CB  . ALA A 1 239 ? 50.265  19.315  -1.462  1.00 57.64  ? 239  ALA A CB  1 
ATOM   1714 N  N   . GLY A 1 240 ? 52.144  21.422  -3.372  1.00 60.57  ? 240  GLY A N   1 
ATOM   1715 C  CA  . GLY A 1 240 ? 53.023  21.544  -4.521  1.00 64.29  ? 240  GLY A CA  1 
ATOM   1716 C  C   . GLY A 1 240 ? 52.384  21.222  -5.857  1.00 70.43  ? 240  GLY A C   1 
ATOM   1717 O  O   . GLY A 1 240 ? 53.089  20.968  -6.842  1.00 67.26  ? 240  GLY A O   1 
ATOM   1718 N  N   . ALA A 1 241 ? 51.053  21.232  -5.892  1.00 67.08  ? 241  ALA A N   1 
ATOM   1719 C  CA  . ALA A 1 241 ? 50.325  21.043  -7.142  1.00 69.26  ? 241  ALA A CA  1 
ATOM   1720 C  C   . ALA A 1 241 ? 50.636  22.197  -8.079  1.00 69.82  ? 241  ALA A C   1 
ATOM   1721 O  O   . ALA A 1 241 ? 50.708  23.342  -7.649  1.00 77.03  ? 241  ALA A O   1 
ATOM   1722 C  CB  . ALA A 1 241 ? 48.828  20.960  -6.890  1.00 66.58  ? 241  ALA A CB  1 
ATOM   1723 N  N   . THR A 1 242 ? 50.823  21.885  -9.355  1.00 65.93  ? 242  THR A N   1 
ATOM   1724 C  CA  . THR A 1 242 ? 51.129  22.889  -10.365 1.00 72.48  ? 242  THR A CA  1 
ATOM   1725 C  C   . THR A 1 242 ? 49.967  23.865  -10.488 1.00 81.23  ? 242  THR A C   1 
ATOM   1726 O  O   . THR A 1 242 ? 50.081  25.044  -10.153 1.00 83.22  ? 242  THR A O   1 
ATOM   1727 C  CB  . THR A 1 242 ? 51.368  22.214  -11.726 1.00 70.37  ? 242  THR A CB  1 
ATOM   1728 O  OG1 . THR A 1 242 ? 52.428  21.260  -11.606 1.00 75.37  ? 242  THR A OG1 1 
ATOM   1729 C  CG2 . THR A 1 242 ? 51.724  23.232  -12.783 1.00 68.91  ? 242  THR A CG2 1 
ATOM   1730 N  N   . ARG A 1 243 ? 48.849  23.346  -10.981 1.00 81.08  ? 243  ARG A N   1 
ATOM   1731 C  CA  . ARG A 1 243 ? 47.616  24.095  -11.118 1.00 75.69  ? 243  ARG A CA  1 
ATOM   1732 C  C   . ARG A 1 243 ? 46.523  23.223  -10.533 1.00 67.84  ? 243  ARG A C   1 
ATOM   1733 O  O   . ARG A 1 243 ? 46.602  21.996  -10.602 1.00 60.40  ? 243  ARG A O   1 
ATOM   1734 C  CB  . ARG A 1 243 ? 47.299  24.337  -12.592 1.00 75.57  ? 243  ARG A CB  1 
ATOM   1735 C  CG  . ARG A 1 243 ? 48.337  25.133  -13.352 1.00 85.48  ? 243  ARG A CG  1 
ATOM   1736 C  CD  . ARG A 1 243 ? 47.967  25.212  -14.827 1.00 87.93  ? 243  ARG A CD  1 
ATOM   1737 N  NE  . ARG A 1 243 ? 48.080  23.913  -15.486 1.00 90.67  ? 243  ARG A NE  1 
ATOM   1738 C  CZ  . ARG A 1 243 ? 47.666  23.664  -16.723 1.00 90.79  ? 243  ARG A CZ  1 
ATOM   1739 N  NH1 . ARG A 1 243 ? 47.101  24.631  -17.435 1.00 96.86  ? 243  ARG A NH1 1 
ATOM   1740 N  NH2 . ARG A 1 243 ? 47.812  22.451  -17.247 1.00 83.90  ? 243  ARG A NH2 1 
ATOM   1741 N  N   . VAL A 1 244 ? 45.507  23.855  -9.957  1.00 65.83  ? 244  VAL A N   1 
ATOM   1742 C  CA  . VAL A 1 244 ? 44.360  23.116  -9.457  1.00 67.62  ? 244  VAL A CA  1 
ATOM   1743 C  C   . VAL A 1 244 ? 43.073  23.522  -10.171 1.00 57.75  ? 244  VAL A C   1 
ATOM   1744 O  O   . VAL A 1 244 ? 42.750  24.703  -10.291 1.00 54.31  ? 244  VAL A O   1 
ATOM   1745 C  CB  . VAL A 1 244 ? 44.210  23.222  -7.911  1.00 62.68  ? 244  VAL A CB  1 
ATOM   1746 C  CG1 . VAL A 1 244 ? 44.537  24.617  -7.429  1.00 63.22  ? 244  VAL A CG1 1 
ATOM   1747 C  CG2 . VAL A 1 244 ? 42.811  22.802  -7.478  1.00 65.67  ? 244  VAL A CG2 1 
ATOM   1748 N  N   . TYR A 1 245 ? 42.362  22.521  -10.670 1.00 56.42  ? 245  TYR A N   1 
ATOM   1749 C  CA  . TYR A 1 245 ? 41.032  22.715  -11.227 1.00 58.93  ? 245  TYR A CA  1 
ATOM   1750 C  C   . TYR A 1 245 ? 40.026  22.108  -10.253 1.00 58.28  ? 245  TYR A C   1 
ATOM   1751 O  O   . TYR A 1 245 ? 40.393  21.286  -9.410  1.00 60.49  ? 245  TYR A O   1 
ATOM   1752 C  CB  . TYR A 1 245 ? 40.917  22.016  -12.586 1.00 61.49  ? 245  TYR A CB  1 
ATOM   1753 C  CG  . TYR A 1 245 ? 41.858  22.544  -13.656 1.00 65.05  ? 245  TYR A CG  1 
ATOM   1754 C  CD1 . TYR A 1 245 ? 43.237  22.505  -13.481 1.00 70.02  ? 245  TYR A CD1 1 
ATOM   1755 C  CD2 . TYR A 1 245 ? 41.364  23.060  -14.847 1.00 60.73  ? 245  TYR A CD2 1 
ATOM   1756 C  CE1 . TYR A 1 245 ? 44.096  22.979  -14.456 1.00 72.56  ? 245  TYR A CE1 1 
ATOM   1757 C  CE2 . TYR A 1 245 ? 42.212  23.531  -15.828 1.00 60.03  ? 245  TYR A CE2 1 
ATOM   1758 C  CZ  . TYR A 1 245 ? 43.578  23.489  -15.630 1.00 69.62  ? 245  TYR A CZ  1 
ATOM   1759 O  OH  . TYR A 1 245 ? 44.424  23.968  -16.605 1.00 74.12  ? 245  TYR A OH  1 
ATOM   1760 N  N   . ALA A 1 246 ? 38.768  22.522  -10.362 1.00 53.96  ? 246  ALA A N   1 
ATOM   1761 C  CA  . ALA A 1 246 ? 37.685  21.903  -9.604  1.00 52.65  ? 246  ALA A CA  1 
ATOM   1762 C  C   . ALA A 1 246 ? 36.583  21.502  -10.573 1.00 48.46  ? 246  ALA A C   1 
ATOM   1763 O  O   . ALA A 1 246 ? 36.158  22.313  -11.400 1.00 42.90  ? 246  ALA A O   1 
ATOM   1764 C  CB  . ALA A 1 246 ? 37.149  22.865  -8.551  1.00 51.56  ? 246  ALA A CB  1 
ATOM   1765 N  N   . ILE A 1 247 ? 36.134  20.252  -10.493 1.00 52.92  ? 247  ILE A N   1 
ATOM   1766 C  CA  . ILE A 1 247 ? 35.067  19.776  -11.378 1.00 46.68  ? 247  ILE A CA  1 
ATOM   1767 C  C   . ILE A 1 247 ? 33.897  19.176  -10.616 1.00 47.26  ? 247  ILE A C   1 
ATOM   1768 O  O   . ILE A 1 247 ? 34.003  18.091  -10.054 1.00 56.45  ? 247  ILE A O   1 
ATOM   1769 C  CB  . ILE A 1 247 ? 35.568  18.735  -12.377 1.00 45.97  ? 247  ILE A CB  1 
ATOM   1770 C  CG1 . ILE A 1 247 ? 36.660  19.340  -13.261 1.00 45.97  ? 247  ILE A CG1 1 
ATOM   1771 C  CG2 . ILE A 1 247 ? 34.403  18.234  -13.227 1.00 45.74  ? 247  ILE A CG2 1 
ATOM   1772 C  CD1 . ILE A 1 247 ? 37.082  18.454  -14.406 1.00 41.32  ? 247  ILE A CD1 1 
ATOM   1773 N  N   . LEU A 1 248 ? 32.778  19.887  -10.604 1.00 45.20  ? 248  LEU A N   1 
ATOM   1774 C  CA  . LEU A 1 248 ? 31.578  19.411  -9.924  1.00 54.60  ? 248  LEU A CA  1 
ATOM   1775 C  C   . LEU A 1 248 ? 30.484  19.205  -10.949 1.00 56.19  ? 248  LEU A C   1 
ATOM   1776 O  O   . LEU A 1 248 ? 30.345  20.011  -11.871 1.00 59.24  ? 248  LEU A O   1 
ATOM   1777 C  CB  . LEU A 1 248 ? 31.117  20.448  -8.922  1.00 50.40  ? 248  LEU A CB  1 
ATOM   1778 C  CG  . LEU A 1 248 ? 32.273  21.339  -8.484  1.00 57.66  ? 248  LEU A CG  1 
ATOM   1779 C  CD1 . LEU A 1 248 ? 31.766  22.728  -8.159  1.00 58.66  ? 248  LEU A CD1 1 
ATOM   1780 C  CD2 . LEU A 1 248 ? 33.007  20.713  -7.306  1.00 59.22  ? 248  LEU A CD2 1 
ATOM   1781 N  N   . THR A 1 249 ? 29.702  18.140  -10.806 1.00 49.83  ? 249  THR A N   1 
ATOM   1782 C  CA  . THR A 1 249 ? 28.583  17.964  -11.718 1.00 47.95  ? 249  THR A CA  1 
ATOM   1783 C  C   . THR A 1 249 ? 27.438  18.910  -11.351 1.00 49.69  ? 249  THR A C   1 
ATOM   1784 O  O   . THR A 1 249 ? 26.854  19.563  -12.224 1.00 51.30  ? 249  THR A O   1 
ATOM   1785 C  CB  . THR A 1 249 ? 28.123  16.498  -11.835 1.00 45.78  ? 249  THR A CB  1 
ATOM   1786 O  OG1 . THR A 1 249 ? 26.702  16.451  -12.052 1.00 46.71  ? 249  THR A OG1 1 
ATOM   1787 C  CG2 . THR A 1 249 ? 28.472  15.734  -10.584 1.00 60.81  ? 249  THR A CG2 1 
ATOM   1788 N  N   . HIS A 1 250 ? 27.149  19.018  -10.059 1.00 44.96  ? 250  HIS A N   1 
ATOM   1789 C  CA  . HIS A 1 250 ? 26.082  19.902  -9.607  1.00 44.01  ? 250  HIS A CA  1 
ATOM   1790 C  C   . HIS A 1 250 ? 26.673  21.140  -8.953  1.00 53.30  ? 250  HIS A C   1 
ATOM   1791 O  O   . HIS A 1 250 ? 27.246  21.066  -7.860  1.00 55.70  ? 250  HIS A O   1 
ATOM   1792 C  CB  . HIS A 1 250 ? 25.133  19.190  -8.626  1.00 35.37  ? 250  HIS A CB  1 
ATOM   1793 C  CG  . HIS A 1 250 ? 24.609  17.879  -9.122  1.00 36.51  ? 250  HIS A CG  1 
ATOM   1794 N  ND1 . HIS A 1 250 ? 23.808  17.771  -10.242 1.00 37.64  ? 250  HIS A ND1 1 
ATOM   1795 C  CD2 . HIS A 1 250 ? 24.768  16.617  -8.648  1.00 34.02  ? 250  HIS A CD2 1 
ATOM   1796 C  CE1 . HIS A 1 250 ? 23.500  16.498  -10.439 1.00 33.32  ? 250  HIS A CE1 1 
ATOM   1797 N  NE2 . HIS A 1 250 ? 24.070  15.778  -9.486  1.00 41.25  ? 250  HIS A NE2 1 
ATOM   1798 N  N   . GLY A 1 251 ? 26.536  22.277  -9.629  1.00 51.91  ? 251  GLY A N   1 
ATOM   1799 C  CA  . GLY A 1 251 ? 27.026  23.536  -9.101  1.00 53.61  ? 251  GLY A CA  1 
ATOM   1800 C  C   . GLY A 1 251 ? 25.953  24.346  -8.396  1.00 57.94  ? 251  GLY A C   1 
ATOM   1801 O  O   . GLY A 1 251 ? 25.328  25.226  -8.990  1.00 54.82  ? 251  GLY A O   1 
ATOM   1802 N  N   . ILE A 1 252 ? 25.732  24.048  -7.121  1.00 68.01  ? 252  ILE A N   1 
ATOM   1803 C  CA  . ILE A 1 252 ? 24.742  24.780  -6.334  1.00 71.03  ? 252  ILE A CA  1 
ATOM   1804 C  C   . ILE A 1 252 ? 25.207  26.217  -6.064  1.00 76.74  ? 252  ILE A C   1 
ATOM   1805 O  O   . ILE A 1 252 ? 24.437  27.162  -6.227  1.00 80.13  ? 252  ILE A O   1 
ATOM   1806 C  CB  . ILE A 1 252 ? 24.381  24.023  -5.036  1.00 66.76  ? 252  ILE A CB  1 
ATOM   1807 C  CG1 . ILE A 1 252 ? 24.087  22.558  -5.352  1.00 64.51  ? 252  ILE A CG1 1 
ATOM   1808 C  CG2 . ILE A 1 252 ? 23.173  24.646  -4.361  1.00 61.44  ? 252  ILE A CG2 1 
ATOM   1809 C  CD1 . ILE A 1 252 ? 23.503  21.795  -4.189  1.00 68.74  ? 252  ILE A CD1 1 
ATOM   1810 N  N   . PHE A 1 253 ? 26.465  26.372  -5.658  1.00 79.15  ? 253  PHE A N   1 
ATOM   1811 C  CA  . PHE A 1 253 ? 27.132  27.675  -5.667  1.00 81.88  ? 253  PHE A CA  1 
ATOM   1812 C  C   . PHE A 1 253 ? 26.365  28.774  -4.938  1.00 84.28  ? 253  PHE A C   1 
ATOM   1813 O  O   . PHE A 1 253 ? 25.957  29.761  -5.537  1.00 87.68  ? 253  PHE A O   1 
ATOM   1814 C  CB  . PHE A 1 253 ? 27.408  28.121  -7.110  1.00 80.72  ? 253  PHE A CB  1 
ATOM   1815 C  CG  . PHE A 1 253 ? 28.499  27.349  -7.795  1.00 78.88  ? 253  PHE A CG  1 
ATOM   1816 C  CD1 . PHE A 1 253 ? 28.592  27.333  -9.176  1.00 83.32  ? 253  PHE A CD1 1 
ATOM   1817 C  CD2 . PHE A 1 253 ? 29.440  26.654  -7.061  1.00 83.06  ? 253  PHE A CD2 1 
ATOM   1818 C  CE1 . PHE A 1 253 ? 29.601  26.629  -9.812  1.00 83.89  ? 253  PHE A CE1 1 
ATOM   1819 C  CE2 . PHE A 1 253 ? 30.452  25.950  -7.690  1.00 85.23  ? 253  PHE A CE2 1 
ATOM   1820 C  CZ  . PHE A 1 253 ? 30.532  25.936  -9.066  1.00 84.71  ? 253  PHE A CZ  1 
ATOM   1821 N  N   . SER A 1 254 ? 26.198  28.622  -3.635  1.00 84.61  ? 254  SER A N   1 
ATOM   1822 C  CA  . SER A 1 254 ? 25.461  29.626  -2.887  1.00 88.59  ? 254  SER A CA  1 
ATOM   1823 C  C   . SER A 1 254 ? 26.284  30.298  -1.789  1.00 94.77  ? 254  SER A C   1 
ATOM   1824 O  O   . SER A 1 254 ? 27.347  29.806  -1.399  1.00 102.36 ? 254  SER A O   1 
ATOM   1825 C  CB  . SER A 1 254 ? 24.233  28.986  -2.270  1.00 84.39  ? 254  SER A CB  1 
ATOM   1826 O  OG  . SER A 1 254 ? 24.624  27.924  -1.423  1.00 82.99  ? 254  SER A OG  1 
ATOM   1827 N  N   . GLY A 1 255 ? 25.770  31.419  -1.286  1.00 90.56  ? 255  GLY A N   1 
ATOM   1828 C  CA  . GLY A 1 255 ? 26.337  32.088  -0.128  1.00 88.74  ? 255  GLY A CA  1 
ATOM   1829 C  C   . GLY A 1 255 ? 27.695  32.704  -0.397  1.00 91.53  ? 255  GLY A C   1 
ATOM   1830 O  O   . GLY A 1 255 ? 27.821  33.575  -1.258  1.00 96.01  ? 255  GLY A O   1 
ATOM   1831 N  N   . PRO A 1 256 ? 28.721  32.265  0.355   1.00 85.86  ? 256  PRO A N   1 
ATOM   1832 C  CA  . PRO A 1 256 ? 30.103  32.667  0.071   1.00 83.15  ? 256  PRO A CA  1 
ATOM   1833 C  C   . PRO A 1 256 ? 30.390  32.396  -1.405  1.00 84.15  ? 256  PRO A C   1 
ATOM   1834 O  O   . PRO A 1 256 ? 31.273  32.991  -2.016  1.00 81.04  ? 256  PRO A O   1 
ATOM   1835 C  CB  . PRO A 1 256 ? 30.927  31.752  0.986   1.00 82.18  ? 256  PRO A CB  1 
ATOM   1836 C  CG  . PRO A 1 256 ? 30.003  31.421  2.122   1.00 80.64  ? 256  PRO A CG  1 
ATOM   1837 C  CD  . PRO A 1 256 ? 28.627  31.375  1.526   1.00 81.54  ? 256  PRO A CD  1 
ATOM   1838 N  N   . ALA A 1 257 ? 29.643  31.440  -1.948  1.00 85.66  ? 257  ALA A N   1 
ATOM   1839 C  CA  . ALA A 1 257 ? 29.448  31.282  -3.394  1.00 88.99  ? 257  ALA A CA  1 
ATOM   1840 C  C   . ALA A 1 257 ? 30.661  31.512  -4.283  1.00 84.38  ? 257  ALA A C   1 
ATOM   1841 O  O   . ALA A 1 257 ? 31.755  31.006  -4.019  1.00 73.40  ? 257  ALA A O   1 
ATOM   1842 C  CB  . ALA A 1 257 ? 28.296  32.193  -3.866  1.00 92.34  ? 257  ALA A CB  1 
ATOM   1843 N  N   . ILE A 1 258 ? 30.426  32.276  -5.352  1.00 92.41  ? 258  ILE A N   1 
ATOM   1844 C  CA  . ILE A 1 258 ? 31.451  32.643  -6.330  1.00 97.55  ? 258  ILE A CA  1 
ATOM   1845 C  C   . ILE A 1 258 ? 32.560  33.546  -5.743  1.00 96.00  ? 258  ILE A C   1 
ATOM   1846 O  O   . ILE A 1 258 ? 33.662  33.591  -6.261  1.00 91.37  ? 258  ILE A O   1 
ATOM   1847 C  CB  . ILE A 1 258 ? 30.829  33.282  -7.599  1.00 87.20  ? 258  ILE A CB  1 
ATOM   1848 N  N   . SER A 1 259 ? 32.257  34.246  -4.653  1.00 96.59  ? 259  SER A N   1 
ATOM   1849 C  CA  . SER A 1 259 ? 33.288  34.981  -3.915  1.00 96.45  ? 259  SER A CA  1 
ATOM   1850 C  C   . SER A 1 259 ? 34.523  34.098  -3.759  1.00 96.67  ? 259  SER A C   1 
ATOM   1851 O  O   . SER A 1 259 ? 35.589  34.366  -4.320  1.00 92.95  ? 259  SER A O   1 
ATOM   1852 C  CB  . SER A 1 259 ? 32.759  35.374  -2.523  1.00 90.36  ? 259  SER A CB  1 
ATOM   1853 O  OG  . SER A 1 259 ? 33.742  36.049  -1.738  1.00 86.33  ? 259  SER A OG  1 
ATOM   1854 N  N   . ARG A 1 260 ? 34.333  33.008  -3.025  1.00 93.02  ? 260  ARG A N   1 
ATOM   1855 C  CA  . ARG A 1 260 ? 35.392  32.062  -2.701  1.00 82.49  ? 260  ARG A CA  1 
ATOM   1856 C  C   . ARG A 1 260 ? 36.178  31.568  -3.915  1.00 80.65  ? 260  ARG A C   1 
ATOM   1857 O  O   . ARG A 1 260 ? 37.405  31.541  -3.879  1.00 79.37  ? 260  ARG A O   1 
ATOM   1858 C  CB  . ARG A 1 260 ? 34.806  30.890  -1.914  1.00 77.42  ? 260  ARG A CB  1 
ATOM   1859 C  CG  . ARG A 1 260 ? 34.248  31.304  -0.565  1.00 74.93  ? 260  ARG A CG  1 
ATOM   1860 C  CD  . ARG A 1 260 ? 33.763  30.111  0.230   1.00 74.90  ? 260  ARG A CD  1 
ATOM   1861 N  NE  . ARG A 1 260 ? 33.661  30.423  1.650   1.00 78.93  ? 260  ARG A NE  1 
ATOM   1862 C  CZ  . ARG A 1 260 ? 33.041  29.661  2.546   1.00 90.41  ? 260  ARG A CZ  1 
ATOM   1863 N  NH1 . ARG A 1 260 ? 32.449  28.535  2.170   1.00 94.40  ? 260  ARG A NH1 1 
ATOM   1864 N  NH2 . ARG A 1 260 ? 33.005  30.032  3.821   1.00 92.95  ? 260  ARG A NH2 1 
ATOM   1865 N  N   . ILE A 1 261 ? 35.488  31.191  -4.991  1.00 82.87  ? 261  ILE A N   1 
ATOM   1866 C  CA  . ILE A 1 261 ? 36.183  30.656  -6.166  1.00 90.61  ? 261  ILE A CA  1 
ATOM   1867 C  C   . ILE A 1 261 ? 37.155  31.675  -6.766  1.00 96.82  ? 261  ILE A C   1 
ATOM   1868 O  O   . ILE A 1 261 ? 38.279  31.331  -7.134  1.00 102.94 ? 261  ILE A O   1 
ATOM   1869 C  CB  . ILE A 1 261 ? 35.216  30.153  -7.270  1.00 69.52  ? 261  ILE A CB  1 
ATOM   1870 C  CG1 . ILE A 1 261 ? 34.586  31.331  -8.009  1.00 76.33  ? 261  ILE A CG1 1 
ATOM   1871 C  CG2 . ILE A 1 261 ? 34.150  29.237  -6.691  1.00 64.21  ? 261  ILE A CG2 1 
ATOM   1872 N  N   . ASN A 1 262 ? 36.718  32.928  -6.851  0.92 95.86  ? 262  ASN A N   1 
ATOM   1873 C  CA  . ASN A 1 262 ? 37.563  34.012  -7.348  0.92 94.98  ? 262  ASN A CA  1 
ATOM   1874 C  C   . ASN A 1 262 ? 38.809  34.191  -6.488  0.92 96.15  ? 262  ASN A C   1 
ATOM   1875 O  O   . ASN A 1 262 ? 39.935  34.133  -6.982  0.92 93.11  ? 262  ASN A O   1 
ATOM   1876 C  CB  . ASN A 1 262 ? 36.775  35.321  -7.388  0.92 91.69  ? 262  ASN A CB  1 
ATOM   1877 C  CG  . ASN A 1 262 ? 35.582  35.253  -8.320  0.92 89.63  ? 262  ASN A CG  1 
ATOM   1878 O  OD1 . ASN A 1 262 ? 35.654  34.656  -9.398  0.92 89.39  ? 262  ASN A OD1 1 
ATOM   1879 N  ND2 . ASN A 1 262 ? 34.475  35.867  -7.911  0.92 86.08  ? 262  ASN A ND2 1 
ATOM   1880 N  N   . ASN A 1 263 ? 38.589  34.407  -5.194  1.00 99.84  ? 263  ASN A N   1 
ATOM   1881 C  CA  . ASN A 1 263 ? 39.676  34.535  -4.236  1.00 103.30 ? 263  ASN A CA  1 
ATOM   1882 C  C   . ASN A 1 263 ? 40.382  33.202  -3.965  1.00 103.15 ? 263  ASN A C   1 
ATOM   1883 O  O   . ASN A 1 263 ? 41.187  33.090  -3.040  1.00 105.29 ? 263  ASN A O   1 
ATOM   1884 C  CB  . ASN A 1 263 ? 39.165  35.153  -2.931  1.00 101.53 ? 263  ASN A CB  1 
ATOM   1885 N  N   . ALA A 1 264 ? 40.073  32.192  -4.773  1.00 95.71  ? 264  ALA A N   1 
ATOM   1886 C  CA  . ALA A 1 264 ? 40.763  30.910  -4.683  1.00 87.16  ? 264  ALA A CA  1 
ATOM   1887 C  C   . ALA A 1 264 ? 41.592  30.680  -5.938  1.00 78.81  ? 264  ALA A C   1 
ATOM   1888 O  O   . ALA A 1 264 ? 41.424  31.369  -6.943  1.00 72.52  ? 264  ALA A O   1 
ATOM   1889 C  CB  . ALA A 1 264 ? 39.774  29.771  -4.466  1.00 86.42  ? 264  ALA A CB  1 
ATOM   1890 N  N   . CYS A 1 265 ? 42.475  29.692  -5.876  1.00 77.02  ? 265  CYS A N   1 
ATOM   1891 C  CA  . CYS A 1 265 ? 43.530  29.536  -6.873  1.00 74.74  ? 265  CYS A CA  1 
ATOM   1892 C  C   . CYS A 1 265 ? 43.179  28.670  -8.080  1.00 74.70  ? 265  CYS A C   1 
ATOM   1893 O  O   . CYS A 1 265 ? 44.074  28.290  -8.840  1.00 77.07  ? 265  CYS A O   1 
ATOM   1894 C  CB  . CYS A 1 265 ? 44.757  28.950  -6.194  1.00 70.41  ? 265  CYS A CB  1 
ATOM   1895 S  SG  . CYS A 1 265 ? 44.328  27.672  -4.986  1.00 111.27 ? 265  CYS A SG  1 
ATOM   1896 N  N   . PHE A 1 266 ? 41.897  28.356  -8.261  1.00 66.02  ? 266  PHE A N   1 
ATOM   1897 C  CA  . PHE A 1 266 ? 41.488  27.488  -9.369  1.00 61.58  ? 266  PHE A CA  1 
ATOM   1898 C  C   . PHE A 1 266 ? 41.862  28.070  -10.731 1.00 63.10  ? 266  PHE A C   1 
ATOM   1899 O  O   . PHE A 1 266 ? 41.507  29.202  -11.050 1.00 62.83  ? 266  PHE A O   1 
ATOM   1900 C  CB  . PHE A 1 266 ? 39.978  27.225  -9.356  1.00 56.71  ? 266  PHE A CB  1 
ATOM   1901 C  CG  . PHE A 1 266 ? 39.465  26.649  -8.072  1.00 53.44  ? 266  PHE A CG  1 
ATOM   1902 C  CD1 . PHE A 1 266 ? 38.538  27.344  -7.314  1.00 50.83  ? 266  PHE A CD1 1 
ATOM   1903 C  CD2 . PHE A 1 266 ? 39.901  25.411  -7.625  1.00 52.92  ? 266  PHE A CD2 1 
ATOM   1904 C  CE1 . PHE A 1 266 ? 38.054  26.815  -6.135  1.00 50.24  ? 266  PHE A CE1 1 
ATOM   1905 C  CE2 . PHE A 1 266 ? 39.429  24.882  -6.440  1.00 46.80  ? 266  PHE A CE2 1 
ATOM   1906 C  CZ  . PHE A 1 266 ? 38.506  25.588  -5.695  1.00 50.56  ? 266  PHE A CZ  1 
ATOM   1907 N  N   . GLU A 1 267 ? 42.575  27.286  -11.531 1.00 59.24  ? 267  GLU A N   1 
ATOM   1908 C  CA  . GLU A 1 267 ? 42.742  27.608  -12.937 1.00 57.15  ? 267  GLU A CA  1 
ATOM   1909 C  C   . GLU A 1 267 ? 41.359  27.738  -13.577 1.00 61.39  ? 267  GLU A C   1 
ATOM   1910 O  O   . GLU A 1 267 ? 41.035  28.751  -14.193 1.00 66.39  ? 267  GLU A O   1 
ATOM   1911 C  CB  . GLU A 1 267 ? 43.562  26.528  -13.634 1.00 55.99  ? 267  GLU A CB  1 
ATOM   1912 C  CG  . GLU A 1 267 ? 43.729  26.758  -15.119 1.00 66.34  ? 267  GLU A CG  1 
ATOM   1913 C  CD  . GLU A 1 267 ? 44.397  28.082  -15.424 1.00 75.03  ? 267  GLU A CD  1 
ATOM   1914 O  OE1 . GLU A 1 267 ? 45.107  28.598  -14.532 1.00 74.96  ? 267  GLU A OE1 1 
ATOM   1915 O  OE2 . GLU A 1 267 ? 44.210  28.607  -16.548 1.00 75.90  ? 267  GLU A OE2 1 
ATOM   1916 N  N   . ALA A 1 268 ? 40.534  26.709  -13.409 1.00 63.53  ? 268  ALA A N   1 
ATOM   1917 C  CA  . ALA A 1 268 ? 39.144  26.759  -13.861 1.00 60.40  ? 268  ALA A CA  1 
ATOM   1918 C  C   . ALA A 1 268 ? 38.222  26.008  -12.895 1.00 60.70  ? 268  ALA A C   1 
ATOM   1919 O  O   . ALA A 1 268 ? 38.671  25.181  -12.100 1.00 55.40  ? 268  ALA A O   1 
ATOM   1920 C  CB  . ALA A 1 268 ? 39.015  26.193  -15.274 1.00 53.38  ? 268  ALA A CB  1 
ATOM   1921 N  N   . VAL A 1 269 ? 36.933  26.315  -12.960 1.00 57.49  ? 269  VAL A N   1 
ATOM   1922 C  CA  . VAL A 1 269 ? 35.936  25.570  -12.207 1.00 54.90  ? 269  VAL A CA  1 
ATOM   1923 C  C   . VAL A 1 269 ? 34.830  25.118  -13.153 1.00 56.90  ? 269  VAL A C   1 
ATOM   1924 O  O   . VAL A 1 269 ? 34.043  25.930  -13.631 1.00 61.55  ? 269  VAL A O   1 
ATOM   1925 C  CB  . VAL A 1 269 ? 35.355  26.409  -11.078 1.00 51.84  ? 269  VAL A CB  1 
ATOM   1926 C  CG1 . VAL A 1 269 ? 34.328  25.594  -10.282 1.00 51.54  ? 269  VAL A CG1 1 
ATOM   1927 C  CG2 . VAL A 1 269 ? 36.483  26.924  -10.182 1.00 47.25  ? 269  VAL A CG2 1 
ATOM   1928 N  N   . VAL A 1 270 ? 34.794  23.822  -13.443 1.00 51.63  ? 270  VAL A N   1 
ATOM   1929 C  CA  . VAL A 1 270 ? 33.823  23.279  -14.389 1.00 48.70  ? 270  VAL A CA  1 
ATOM   1930 C  C   . VAL A 1 270 ? 32.594  22.685  -13.695 1.00 48.42  ? 270  VAL A C   1 
ATOM   1931 O  O   . VAL A 1 270 ? 32.706  21.990  -12.684 1.00 52.48  ? 270  VAL A O   1 
ATOM   1932 C  CB  . VAL A 1 270 ? 34.440  22.191  -15.270 1.00 43.96  ? 270  VAL A CB  1 
ATOM   1933 C  CG1 . VAL A 1 270 ? 33.526  21.889  -16.425 1.00 42.17  ? 270  VAL A CG1 1 
ATOM   1934 C  CG2 . VAL A 1 270 ? 35.797  22.627  -15.772 1.00 45.78  ? 270  VAL A CG2 1 
ATOM   1935 N  N   . VAL A 1 271 ? 31.423  22.968  -14.250 1.00 42.70  ? 271  VAL A N   1 
ATOM   1936 C  CA  . VAL A 1 271 ? 30.175  22.412  -13.753 1.00 33.18  ? 271  VAL A CA  1 
ATOM   1937 C  C   . VAL A 1 271 ? 29.286  22.119  -14.934 1.00 35.99  ? 271  VAL A C   1 
ATOM   1938 O  O   . VAL A 1 271 ? 29.561  22.550  -16.058 1.00 46.29  ? 271  VAL A O   1 
ATOM   1939 C  CB  . VAL A 1 271 ? 29.461  23.386  -12.817 1.00 43.44  ? 271  VAL A CB  1 
ATOM   1940 C  CG1 . VAL A 1 271 ? 30.127  23.371  -11.439 1.00 44.63  ? 271  VAL A CG1 1 
ATOM   1941 C  CG2 . VAL A 1 271 ? 29.467  24.790  -13.417 1.00 41.08  ? 271  VAL A CG2 1 
ATOM   1942 N  N   . THR A 1 272 ? 28.233  21.358  -14.692 1.00 29.77  ? 272  THR A N   1 
ATOM   1943 C  CA  . THR A 1 272 ? 27.251  21.101  -15.723 1.00 36.16  ? 272  THR A CA  1 
ATOM   1944 C  C   . THR A 1 272 ? 26.096  22.046  -15.492 1.00 41.34  ? 272  THR A C   1 
ATOM   1945 O  O   . THR A 1 272 ? 26.038  22.739  -14.480 1.00 47.34  ? 272  THR A O   1 
ATOM   1946 C  CB  . THR A 1 272 ? 26.709  19.677  -15.651 1.00 42.95  ? 272  THR A CB  1 
ATOM   1947 O  OG1 . THR A 1 272 ? 25.723  19.596  -14.612 1.00 40.54  ? 272  THR A OG1 1 
ATOM   1948 C  CG2 . THR A 1 272 ? 27.844  18.698  -15.389 1.00 42.94  ? 272  THR A CG2 1 
ATOM   1949 N  N   . ASN A 1 273 ? 25.161  22.069  -16.423 1.00 43.39  ? 273  ASN A N   1 
ATOM   1950 C  CA  . ASN A 1 273 ? 24.021  22.941  -16.263 1.00 46.60  ? 273  ASN A CA  1 
ATOM   1951 C  C   . ASN A 1 273 ? 22.816  22.176  -15.733 1.00 46.01  ? 273  ASN A C   1 
ATOM   1952 O  O   . ASN A 1 273 ? 21.682  22.478  -16.107 1.00 53.41  ? 273  ASN A O   1 
ATOM   1953 C  CB  . ASN A 1 273 ? 23.703  23.673  -17.577 1.00 42.06  ? 273  ASN A CB  1 
ATOM   1954 C  CG  . ASN A 1 273 ? 23.494  22.721  -18.744 1.00 41.17  ? 273  ASN A CG  1 
ATOM   1955 O  OD1 . ASN A 1 273 ? 23.818  21.540  -18.657 1.00 48.70  ? 273  ASN A OD1 1 
ATOM   1956 N  ND2 . ASN A 1 273 ? 22.951  23.237  -19.847 1.00 41.73  ? 273  ASN A ND2 1 
ATOM   1957 N  N   . THR A 1 274 ? 23.055  21.185  -14.870 1.00 43.73  ? 274  THR A N   1 
ATOM   1958 C  CA  . THR A 1 274 ? 21.941  20.535  -14.162 1.00 45.43  ? 274  THR A CA  1 
ATOM   1959 C  C   . THR A 1 274 ? 21.249  21.596  -13.308 1.00 44.43  ? 274  THR A C   1 
ATOM   1960 O  O   . THR A 1 274 ? 20.049  21.523  -13.028 1.00 47.90  ? 274  THR A O   1 
ATOM   1961 C  CB  . THR A 1 274 ? 22.363  19.285  -13.311 1.00 40.46  ? 274  THR A CB  1 
ATOM   1962 O  OG1 . THR A 1 274 ? 23.316  19.643  -12.300 1.00 50.18  ? 274  THR A OG1 1 
ATOM   1963 C  CG2 . THR A 1 274 ? 22.952  18.197  -14.191 1.00 35.24  ? 274  THR A CG2 1 
ATOM   1964 N  N   . ILE A 1 275 ? 22.030  22.599  -12.920 1.00 47.23  ? 275  ILE A N   1 
ATOM   1965 C  CA  . ILE A 1 275 ? 21.534  23.782  -12.222 1.00 45.96  ? 275  ILE A CA  1 
ATOM   1966 C  C   . ILE A 1 275 ? 21.942  24.995  -13.063 1.00 49.16  ? 275  ILE A C   1 
ATOM   1967 O  O   . ILE A 1 275 ? 23.026  24.996  -13.656 1.00 46.19  ? 275  ILE A O   1 
ATOM   1968 C  CB  . ILE A 1 275 ? 22.141  23.860  -10.803 1.00 52.76  ? 275  ILE A CB  1 
ATOM   1969 C  CG1 . ILE A 1 275 ? 21.739  22.622  -9.996  1.00 48.80  ? 275  ILE A CG1 1 
ATOM   1970 C  CG2 . ILE A 1 275 ? 21.728  25.139  -10.091 1.00 53.74  ? 275  ILE A CG2 1 
ATOM   1971 C  CD1 . ILE A 1 275 ? 22.217  22.620  -8.565  1.00 46.20  ? 275  ILE A CD1 1 
ATOM   1972 N  N   . PRO A 1 276 ? 21.065  26.014  -13.162 1.00 58.43  ? 276  PRO A N   1 
ATOM   1973 C  CA  . PRO A 1 276 ? 21.375  27.175  -14.014 1.00 59.83  ? 276  PRO A CA  1 
ATOM   1974 C  C   . PRO A 1 276 ? 22.611  27.936  -13.535 1.00 58.67  ? 276  PRO A C   1 
ATOM   1975 O  O   . PRO A 1 276 ? 22.708  28.255  -12.355 1.00 56.63  ? 276  PRO A O   1 
ATOM   1976 C  CB  . PRO A 1 276 ? 20.117  28.047  -13.895 1.00 47.49  ? 276  PRO A CB  1 
ATOM   1977 C  CG  . PRO A 1 276 ? 19.027  27.068  -13.566 1.00 51.48  ? 276  PRO A CG  1 
ATOM   1978 C  CD  . PRO A 1 276 ? 19.681  26.066  -12.654 1.00 57.96  ? 276  PRO A CD  1 
ATOM   1979 N  N   . GLN A 1 277 ? 23.537  28.217  -14.447 1.00 62.91  ? 277  GLN A N   1 
ATOM   1980 C  CA  . GLN A 1 277 ? 24.811  28.827  -14.076 1.00 70.92  ? 277  GLN A CA  1 
ATOM   1981 C  C   . GLN A 1 277 ? 25.027  30.208  -14.710 1.00 84.32  ? 277  GLN A C   1 
ATOM   1982 O  O   . GLN A 1 277 ? 26.012  30.885  -14.406 1.00 85.66  ? 277  GLN A O   1 
ATOM   1983 C  CB  . GLN A 1 277 ? 25.973  27.900  -14.451 1.00 65.71  ? 277  GLN A CB  1 
ATOM   1984 C  CG  . GLN A 1 277 ? 25.848  26.470  -13.940 1.00 62.57  ? 277  GLN A CG  1 
ATOM   1985 C  CD  . GLN A 1 277 ? 25.793  26.385  -12.423 1.00 61.68  ? 277  GLN A CD  1 
ATOM   1986 O  OE1 . GLN A 1 277 ? 25.164  25.486  -11.861 1.00 62.26  ? 277  GLN A OE1 1 
ATOM   1987 N  NE2 . GLN A 1 277 ? 26.449  27.323  -11.754 1.00 58.61  ? 277  GLN A NE2 1 
ATOM   1988 N  N   . GLU A 1 278 ? 24.104  30.612  -15.581 1.00 90.85  ? 278  GLU A N   1 
ATOM   1989 C  CA  . GLU A 1 278 ? 24.179  31.889  -16.305 1.00 93.98  ? 278  GLU A CA  1 
ATOM   1990 C  C   . GLU A 1 278 ? 24.538  33.100  -15.430 1.00 91.78  ? 278  GLU A C   1 
ATOM   1991 O  O   . GLU A 1 278 ? 25.495  33.821  -15.717 1.00 83.78  ? 278  GLU A O   1 
ATOM   1992 C  CB  . GLU A 1 278 ? 22.860  32.144  -17.041 1.00 98.04  ? 278  GLU A CB  1 
ATOM   1993 C  CG  . GLU A 1 278 ? 21.691  31.295  -16.527 1.00 101.80 ? 278  GLU A CG  1 
ATOM   1994 C  CD  . GLU A 1 278 ? 21.234  31.686  -15.128 1.00 103.12 ? 278  GLU A CD  1 
ATOM   1995 O  OE1 . GLU A 1 278 ? 20.222  32.412  -15.023 1.00 103.38 ? 278  GLU A OE1 1 
ATOM   1996 O  OE2 . GLU A 1 278 ? 21.874  31.264  -14.137 1.00 101.95 ? 278  GLU A OE2 1 
ATOM   1997 N  N   . ASP A 1 279 ? 23.757  33.315  -14.372 1.00 94.01  ? 279  ASP A N   1 
ATOM   1998 C  CA  . ASP A 1 279 ? 23.984  34.410  -13.431 1.00 99.31  ? 279  ASP A CA  1 
ATOM   1999 C  C   . ASP A 1 279 ? 25.337  34.292  -12.729 1.00 98.65  ? 279  ASP A C   1 
ATOM   2000 O  O   . ASP A 1 279 ? 26.099  35.258  -12.664 1.00 101.81 ? 279  ASP A O   1 
ATOM   2001 C  CB  . ASP A 1 279 ? 22.853  34.450  -12.395 1.00 105.74 ? 279  ASP A CB  1 
ATOM   2002 C  CG  . ASP A 1 279 ? 23.098  35.469  -11.289 1.00 111.28 ? 279  ASP A CG  1 
ATOM   2003 O  OD1 . ASP A 1 279 ? 23.877  35.167  -10.357 1.00 111.79 ? 279  ASP A OD1 1 
ATOM   2004 O  OD2 . ASP A 1 279 ? 22.497  36.566  -11.343 1.00 113.59 ? 279  ASP A OD2 1 
ATOM   2005 N  N   . LYS A 1 280 ? 25.622  33.103  -12.203 1.00 91.55  ? 280  LYS A N   1 
ATOM   2006 C  CA  . LYS A 1 280 ? 26.874  32.838  -11.500 1.00 82.54  ? 280  LYS A CA  1 
ATOM   2007 C  C   . LYS A 1 280 ? 28.107  33.152  -12.351 1.00 81.91  ? 280  LYS A C   1 
ATOM   2008 O  O   . LYS A 1 280 ? 29.089  33.705  -11.855 1.00 80.21  ? 280  LYS A O   1 
ATOM   2009 C  CB  . LYS A 1 280 ? 26.922  31.381  -11.029 1.00 77.23  ? 280  LYS A CB  1 
ATOM   2010 C  CG  . LYS A 1 280 ? 26.712  31.194  -9.533  1.00 75.91  ? 280  LYS A CG  1 
ATOM   2011 C  CD  . LYS A 1 280 ? 25.237  31.185  -9.149  1.00 73.25  ? 280  LYS A CD  1 
ATOM   2012 C  CE  . LYS A 1 280 ? 25.071  31.273  -7.636  1.00 70.04  ? 280  LYS A CE  1 
ATOM   2013 N  NZ  . LYS A 1 280 ? 23.772  30.721  -7.135  1.00 70.18  ? 280  LYS A NZ  1 
ATOM   2014 N  N   . MET A 1 281 ? 28.053  32.798  -13.631 0.60 80.84  ? 281  MET A N   1 
ATOM   2015 C  CA  . MET A 1 281 ? 29.180  33.010  -14.529 0.60 83.80  ? 281  MET A CA  1 
ATOM   2016 C  C   . MET A 1 281 ? 29.479  34.489  -14.740 0.60 86.73  ? 281  MET A C   1 
ATOM   2017 O  O   . MET A 1 281 ? 30.611  34.865  -15.045 0.60 83.97  ? 281  MET A O   1 
ATOM   2018 C  CB  . MET A 1 281 ? 28.930  32.330  -15.873 0.60 83.96  ? 281  MET A CB  1 
ATOM   2019 C  CG  . MET A 1 281 ? 28.852  30.821  -15.785 0.60 82.34  ? 281  MET A CG  1 
ATOM   2020 S  SD  . MET A 1 281 ? 28.727  30.056  -17.406 0.60 87.12  ? 281  MET A SD  1 
ATOM   2021 C  CE  . MET A 1 281 ? 27.193  30.766  -17.995 0.60 83.35  ? 281  MET A CE  1 
ATOM   2022 N  N   . LYS A 1 282 ? 28.459  35.324  -14.584 1.00 92.63  ? 282  LYS A N   1 
ATOM   2023 C  CA  . LYS A 1 282 ? 28.642  36.763  -14.693 1.00 98.24  ? 282  LYS A CA  1 
ATOM   2024 C  C   . LYS A 1 282 ? 29.712  37.222  -13.706 1.00 101.08 ? 282  LYS A C   1 
ATOM   2025 O  O   . LYS A 1 282 ? 30.616  37.979  -14.064 1.00 99.20  ? 282  LYS A O   1 
ATOM   2026 C  CB  . LYS A 1 282 ? 27.322  37.497  -14.436 1.00 94.35  ? 282  LYS A CB  1 
ATOM   2027 N  N   . HIS A 1 283 ? 29.610  36.746  -12.467 1.00 104.03 ? 283  HIS A N   1 
ATOM   2028 C  CA  . HIS A 1 283 ? 30.524  37.152  -11.400 1.00 109.41 ? 283  HIS A CA  1 
ATOM   2029 C  C   . HIS A 1 283 ? 31.689  36.181  -11.223 1.00 106.79 ? 283  HIS A C   1 
ATOM   2030 O  O   . HIS A 1 283 ? 32.328  36.156  -10.171 1.00 104.68 ? 283  HIS A O   1 
ATOM   2031 C  CB  . HIS A 1 283 ? 29.775  37.290  -10.071 1.00 113.49 ? 283  HIS A CB  1 
ATOM   2032 C  CG  . HIS A 1 283 ? 28.717  38.349  -10.079 1.00 115.96 ? 283  HIS A CG  1 
ATOM   2033 N  ND1 . HIS A 1 283 ? 29.000  39.685  -9.884  1.00 117.08 ? 283  HIS A ND1 1 
ATOM   2034 C  CD2 . HIS A 1 283 ? 27.377  38.268  -10.256 1.00 114.09 ? 283  HIS A CD2 1 
ATOM   2035 C  CE1 . HIS A 1 283 ? 27.878  40.381  -9.940  1.00 116.19 ? 283  HIS A CE1 1 
ATOM   2036 N  NE2 . HIS A 1 283 ? 26.879  39.546  -10.163 1.00 113.93 ? 283  HIS A NE2 1 
ATOM   2037 N  N   . CYS A 1 284 ? 31.963  35.384  -12.250 1.00 103.92 ? 284  CYS A N   1 
ATOM   2038 C  CA  . CYS A 1 284 ? 33.032  34.398  -12.165 1.00 97.44  ? 284  CYS A CA  1 
ATOM   2039 C  C   . CYS A 1 284 ? 33.568  33.982  -13.535 1.00 85.09  ? 284  CYS A C   1 
ATOM   2040 O  O   . CYS A 1 284 ? 32.949  33.190  -14.256 1.00 74.38  ? 284  CYS A O   1 
ATOM   2041 C  CB  . CYS A 1 284 ? 32.569  33.171  -11.378 1.00 99.81  ? 284  CYS A CB  1 
ATOM   2042 S  SG  . CYS A 1 284 ? 33.890  32.007  -11.022 1.00 101.66 ? 284  CYS A SG  1 
ATOM   2043 N  N   . SER A 1 285 ? 34.731  34.525  -13.878 1.00 82.62  ? 285  SER A N   1 
ATOM   2044 C  CA  . SER A 1 285 ? 35.387  34.222  -15.139 1.00 82.15  ? 285  SER A CA  1 
ATOM   2045 C  C   . SER A 1 285 ? 35.876  32.772  -15.200 1.00 82.42  ? 285  SER A C   1 
ATOM   2046 O  O   . SER A 1 285 ? 35.836  32.142  -16.257 1.00 82.18  ? 285  SER A O   1 
ATOM   2047 C  CB  . SER A 1 285 ? 36.562  35.180  -15.357 1.00 82.77  ? 285  SER A CB  1 
ATOM   2048 O  OG  . SER A 1 285 ? 37.323  34.813  -16.495 1.00 83.49  ? 285  SER A OG  1 
ATOM   2049 N  N   . LYS A 1 286 ? 36.329  32.240  -14.070 1.00 78.51  ? 286  LYS A N   1 
ATOM   2050 C  CA  . LYS A 1 286 ? 36.962  30.924  -14.077 1.00 80.23  ? 286  LYS A CA  1 
ATOM   2051 C  C   . LYS A 1 286 ? 35.977  29.752  -14.139 1.00 80.05  ? 286  LYS A C   1 
ATOM   2052 O  O   . LYS A 1 286 ? 36.392  28.592  -14.150 1.00 77.64  ? 286  LYS A O   1 
ATOM   2053 C  CB  . LYS A 1 286 ? 37.935  30.770  -12.901 1.00 79.52  ? 286  LYS A CB  1 
ATOM   2054 C  CG  . LYS A 1 286 ? 37.309  30.928  -11.528 1.00 77.23  ? 286  LYS A CG  1 
ATOM   2055 C  CD  . LYS A 1 286 ? 38.354  30.760  -10.428 1.00 74.76  ? 286  LYS A CD  1 
ATOM   2056 C  CE  . LYS A 1 286 ? 39.468  31.786  -10.560 1.00 73.90  ? 286  LYS A CE  1 
ATOM   2057 N  N   . ILE A 1 287 ? 34.680  30.053  -14.198 1.00 77.55  ? 287  ILE A N   1 
ATOM   2058 C  CA  . ILE A 1 287 ? 33.658  29.006  -14.291 1.00 65.58  ? 287  ILE A CA  1 
ATOM   2059 C  C   . ILE A 1 287 ? 33.315  28.632  -15.730 1.00 58.92  ? 287  ILE A C   1 
ATOM   2060 O  O   . ILE A 1 287 ? 33.177  29.492  -16.598 1.00 65.73  ? 287  ILE A O   1 
ATOM   2061 C  CB  . ILE A 1 287 ? 32.365  29.377  -13.531 1.00 64.51  ? 287  ILE A CB  1 
ATOM   2062 C  CG1 . ILE A 1 287 ? 32.584  29.251  -12.021 1.00 64.05  ? 287  ILE A CG1 1 
ATOM   2063 C  CG2 . ILE A 1 287 ? 31.207  28.481  -13.968 1.00 57.39  ? 287  ILE A CG2 1 
ATOM   2064 C  CD1 . ILE A 1 287 ? 31.396  29.678  -11.189 1.00 61.69  ? 287  ILE A CD1 1 
ATOM   2065 N  N   . GLN A 1 288 ? 33.185  27.337  -15.979 1.00 49.86  ? 288  GLN A N   1 
ATOM   2066 C  CA  . GLN A 1 288 ? 32.802  26.858  -17.295 1.00 53.01  ? 288  GLN A CA  1 
ATOM   2067 C  C   . GLN A 1 288 ? 31.749  25.772  -17.150 1.00 56.23  ? 288  GLN A C   1 
ATOM   2068 O  O   . GLN A 1 288 ? 31.715  25.055  -16.144 1.00 54.38  ? 288  GLN A O   1 
ATOM   2069 C  CB  . GLN A 1 288 ? 34.021  26.326  -18.046 1.00 56.01  ? 288  GLN A CB  1 
ATOM   2070 C  CG  . GLN A 1 288 ? 35.144  27.331  -18.145 1.00 65.14  ? 288  GLN A CG  1 
ATOM   2071 C  CD  . GLN A 1 288 ? 36.272  26.843  -19.015 1.00 76.42  ? 288  GLN A CD  1 
ATOM   2072 O  OE1 . GLN A 1 288 ? 36.121  25.873  -19.764 1.00 77.75  ? 288  GLN A OE1 1 
ATOM   2073 N  NE2 . GLN A 1 288 ? 37.417  27.509  -18.925 1.00 81.43  ? 288  GLN A NE2 1 
ATOM   2074 N  N   . VAL A 1 289 ? 30.887  25.654  -18.154 1.00 50.45  ? 289  VAL A N   1 
ATOM   2075 C  CA  . VAL A 1 289 ? 29.806  24.691  -18.083 1.00 45.35  ? 289  VAL A CA  1 
ATOM   2076 C  C   . VAL A 1 289 ? 29.791  23.680  -19.217 1.00 51.52  ? 289  VAL A C   1 
ATOM   2077 O  O   . VAL A 1 289 ? 29.832  24.030  -20.396 1.00 58.65  ? 289  VAL A O   1 
ATOM   2078 C  CB  . VAL A 1 289 ? 28.421  25.370  -17.954 1.00 45.30  ? 289  VAL A CB  1 
ATOM   2079 C  CG1 . VAL A 1 289 ? 28.445  26.749  -18.543 1.00 47.37  ? 289  VAL A CG1 1 
ATOM   2080 C  CG2 . VAL A 1 289 ? 27.348  24.514  -18.600 1.00 41.50  ? 289  VAL A CG2 1 
ATOM   2081 N  N   . ILE A 1 290 ? 29.753  22.412  -18.832 1.00 48.42  ? 290  ILE A N   1 
ATOM   2082 C  CA  . ILE A 1 290 ? 29.468  21.342  -19.756 1.00 42.03  ? 290  ILE A CA  1 
ATOM   2083 C  C   . ILE A 1 290 ? 27.953  21.256  -19.884 1.00 43.78  ? 290  ILE A C   1 
ATOM   2084 O  O   . ILE A 1 290 ? 27.245  21.063  -18.901 1.00 46.50  ? 290  ILE A O   1 
ATOM   2085 C  CB  . ILE A 1 290 ? 30.001  20.008  -19.213 1.00 52.14  ? 290  ILE A CB  1 
ATOM   2086 C  CG1 . ILE A 1 290 ? 31.498  20.129  -18.900 1.00 53.08  ? 290  ILE A CG1 1 
ATOM   2087 C  CG2 . ILE A 1 290 ? 29.682  18.871  -20.185 1.00 47.77  ? 290  ILE A CG2 1 
ATOM   2088 C  CD1 . ILE A 1 290 ? 32.160  18.839  -18.454 1.00 46.82  ? 290  ILE A CD1 1 
ATOM   2089 N  N   . ASP A 1 291 ? 27.457  21.419  -21.097 1.00 49.95  ? 291  ASP A N   1 
ATOM   2090 C  CA  . ASP A 1 291 ? 26.028  21.322  -21.357 1.00 52.42  ? 291  ASP A CA  1 
ATOM   2091 C  C   . ASP A 1 291 ? 25.604  19.850  -21.330 1.00 49.74  ? 291  ASP A C   1 
ATOM   2092 O  O   . ASP A 1 291 ? 26.190  19.020  -22.018 1.00 52.44  ? 291  ASP A O   1 
ATOM   2093 C  CB  . ASP A 1 291 ? 25.716  21.969  -22.710 1.00 48.82  ? 291  ASP A CB  1 
ATOM   2094 C  CG  . ASP A 1 291 ? 24.251  21.886  -23.083 1.00 55.22  ? 291  ASP A CG  1 
ATOM   2095 O  OD1 . ASP A 1 291 ? 23.408  21.606  -22.209 1.00 47.28  ? 291  ASP A OD1 1 
ATOM   2096 O  OD2 . ASP A 1 291 ? 23.940  22.121  -24.270 1.00 68.47  ? 291  ASP A OD2 1 
ATOM   2097 N  N   . ILE A 1 292 ? 24.599  19.524  -20.524 1.00 42.62  ? 292  ILE A N   1 
ATOM   2098 C  CA  . ILE A 1 292 ? 24.176  18.136  -20.394 1.00 50.35  ? 292  ILE A CA  1 
ATOM   2099 C  C   . ILE A 1 292 ? 22.783  17.886  -20.975 1.00 50.90  ? 292  ILE A C   1 
ATOM   2100 O  O   . ILE A 1 292 ? 22.259  16.772  -20.909 1.00 42.29  ? 292  ILE A O   1 
ATOM   2101 C  CB  . ILE A 1 292 ? 24.340  17.595  -18.930 1.00 48.81  ? 292  ILE A CB  1 
ATOM   2102 C  CG1 . ILE A 1 292 ? 23.695  18.514  -17.891 1.00 31.48  ? 292  ILE A CG1 1 
ATOM   2103 C  CG2 . ILE A 1 292 ? 25.809  17.452  -18.604 1.00 46.33  ? 292  ILE A CG2 1 
ATOM   2104 C  CD1 . ILE A 1 292 ? 22.215  18.520  -17.916 1.00 27.06  ? 292  ILE A CD1 1 
ATOM   2105 N  N   . SER A 1 293 ? 22.212  18.927  -21.574 1.00 46.93  ? 293  SER A N   1 
ATOM   2106 C  CA  . SER A 1 293 ? 20.882  18.855  -22.169 1.00 41.24  ? 293  SER A CA  1 
ATOM   2107 C  C   . SER A 1 293 ? 20.764  17.755  -23.223 1.00 42.72  ? 293  SER A C   1 
ATOM   2108 O  O   . SER A 1 293 ? 19.709  17.140  -23.378 1.00 47.49  ? 293  SER A O   1 
ATOM   2109 C  CB  . SER A 1 293 ? 20.508  20.203  -22.785 1.00 46.08  ? 293  SER A CB  1 
ATOM   2110 O  OG  . SER A 1 293 ? 21.482  20.622  -23.722 1.00 41.10  ? 293  SER A OG  1 
ATOM   2111 N  N   . MET A 1 294 ? 21.851  17.516  -23.943 0.86 33.58  ? 294  MET A N   1 
ATOM   2112 C  CA  . MET A 1 294 ? 21.889  16.482  -24.967 0.86 38.24  ? 294  MET A CA  1 
ATOM   2113 C  C   . MET A 1 294 ? 21.761  15.089  -24.357 0.86 36.84  ? 294  MET A C   1 
ATOM   2114 O  O   . MET A 1 294 ? 21.021  14.245  -24.854 0.86 34.97  ? 294  MET A O   1 
ATOM   2115 C  CB  . MET A 1 294 ? 23.197  16.583  -25.754 0.86 51.19  ? 294  MET A CB  1 
ATOM   2116 C  CG  . MET A 1 294 ? 24.450  16.631  -24.869 0.86 60.43  ? 294  MET A CG  1 
ATOM   2117 N  N   . ILE A 1 295 ? 22.498  14.839  -23.286 1.00 38.06  ? 295  ILE A N   1 
ATOM   2118 C  CA  . ILE A 1 295 ? 22.361  13.577  -22.566 1.00 40.24  ? 295  ILE A CA  1 
ATOM   2119 C  C   . ILE A 1 295 ? 20.920  13.349  -22.102 1.00 35.89  ? 295  ILE A C   1 
ATOM   2120 O  O   . ILE A 1 295 ? 20.367  12.266  -22.279 1.00 38.84  ? 295  ILE A O   1 
ATOM   2121 C  CB  . ILE A 1 295 ? 23.300  13.527  -21.371 1.00 31.88  ? 295  ILE A CB  1 
ATOM   2122 C  CG1 . ILE A 1 295 ? 24.693  13.958  -21.809 1.00 32.37  ? 295  ILE A CG1 1 
ATOM   2123 C  CG2 . ILE A 1 295 ? 23.329  12.141  -20.785 1.00 44.33  ? 295  ILE A CG2 1 
ATOM   2124 C  CD1 . ILE A 1 295 ? 25.739  13.927  -20.708 1.00 48.04  ? 295  ILE A CD1 1 
ATOM   2125 N  N   . LEU A 1 296 ? 20.299  14.372  -21.537 1.00 37.85  ? 296  LEU A N   1 
ATOM   2126 C  CA  . LEU A 1 296 ? 18.956  14.204  -20.993 1.00 34.66  ? 296  LEU A CA  1 
ATOM   2127 C  C   . LEU A 1 296 ? 17.948  14.038  -22.114 1.00 35.25  ? 296  LEU A C   1 
ATOM   2128 O  O   . LEU A 1 296 ? 17.033  13.221  -22.028 1.00 31.82  ? 296  LEU A O   1 
ATOM   2129 C  CB  . LEU A 1 296 ? 18.576  15.382  -20.087 1.00 30.20  ? 296  LEU A CB  1 
ATOM   2130 C  CG  . LEU A 1 296 ? 19.399  15.578  -18.803 1.00 34.26  ? 296  LEU A CG  1 
ATOM   2131 C  CD1 . LEU A 1 296 ? 19.100  16.946  -18.177 1.00 26.42  ? 296  LEU A CD1 1 
ATOM   2132 C  CD2 . LEU A 1 296 ? 19.132  14.459  -17.798 1.00 29.15  ? 296  LEU A CD2 1 
ATOM   2133 N  N   . ALA A 1 297 ? 18.120  14.826  -23.171 1.00 33.39  ? 297  ALA A N   1 
ATOM   2134 C  CA  . ALA A 1 297 ? 17.299  14.688  -24.362 1.00 29.64  ? 297  ALA A CA  1 
ATOM   2135 C  C   . ALA A 1 297 ? 17.406  13.256  -24.846 1.00 33.25  ? 297  ALA A C   1 
ATOM   2136 O  O   . ALA A 1 297 ? 16.404  12.575  -25.051 1.00 43.45  ? 297  ALA A O   1 
ATOM   2137 C  CB  . ALA A 1 297 ? 17.774  15.647  -25.443 1.00 29.60  ? 297  ALA A CB  1 
ATOM   2138 N  N   . GLU A 1 298 ? 18.636  12.798  -25.004 1.00 32.23  ? 298  GLU A N   1 
ATOM   2139 C  CA  . GLU A 1 298 ? 18.883  11.476  -25.549 1.00 39.81  ? 298  GLU A CA  1 
ATOM   2140 C  C   . GLU A 1 298 ? 18.343  10.356  -24.642 1.00 43.40  ? 298  GLU A C   1 
ATOM   2141 O  O   . GLU A 1 298 ? 17.837  9.340   -25.132 1.00 37.35  ? 298  GLU A O   1 
ATOM   2142 C  CB  . GLU A 1 298 ? 20.371  11.299  -25.860 1.00 39.22  ? 298  GLU A CB  1 
ATOM   2143 C  CG  . GLU A 1 298 ? 20.721  9.970   -26.492 1.00 58.34  ? 298  GLU A CG  1 
ATOM   2144 C  CD  . GLU A 1 298 ? 20.317  9.873   -27.953 1.00 70.28  ? 298  GLU A CD  1 
ATOM   2145 O  OE1 . GLU A 1 298 ? 19.346  10.548  -28.367 1.00 64.74  ? 298  GLU A OE1 1 
ATOM   2146 O  OE2 . GLU A 1 298 ? 20.985  9.117   -28.692 1.00 83.50  ? 298  GLU A OE2 1 
ATOM   2147 N  N   . ALA A 1 299 ? 18.437  10.548  -23.328 1.00 41.66  ? 299  ALA A N   1 
ATOM   2148 C  CA  . ALA A 1 299 ? 17.859  9.598   -22.378 1.00 39.27  ? 299  ALA A CA  1 
ATOM   2149 C  C   . ALA A 1 299 ? 16.334  9.552   -22.494 1.00 38.29  ? 299  ALA A C   1 
ATOM   2150 O  O   . ALA A 1 299 ? 15.732  8.483   -22.445 1.00 35.39  ? 299  ALA A O   1 
ATOM   2151 C  CB  . ALA A 1 299 ? 18.273  9.938   -20.951 1.00 40.46  ? 299  ALA A CB  1 
ATOM   2152 N  N   . ILE A 1 300 ? 15.711  10.715  -22.644 1.00 28.53  ? 300  ILE A N   1 
ATOM   2153 C  CA  . ILE A 1 300 ? 14.260  10.786  -22.810 1.00 32.42  ? 300  ILE A CA  1 
ATOM   2154 C  C   . ILE A 1 300 ? 13.779  10.111  -24.100 1.00 37.57  ? 300  ILE A C   1 
ATOM   2155 O  O   . ILE A 1 300 ? 12.848  9.299   -24.073 1.00 40.08  ? 300  ILE A O   1 
ATOM   2156 C  CB  . ILE A 1 300 ? 13.785  12.242  -22.801 1.00 38.57  ? 300  ILE A CB  1 
ATOM   2157 C  CG1 . ILE A 1 300 ? 14.059  12.858  -21.430 1.00 30.41  ? 300  ILE A CG1 1 
ATOM   2158 C  CG2 . ILE A 1 300 ? 12.301  12.337  -23.156 1.00 38.24  ? 300  ILE A CG2 1 
ATOM   2159 C  CD1 . ILE A 1 300 ? 13.739  14.331  -21.362 1.00 30.33  ? 300  ILE A CD1 1 
ATOM   2160 N  N   . ARG A 1 301 ? 14.411  10.474  -25.216 0.60 33.04  ? 301  ARG A N   1 
ATOM   2161 C  CA  . ARG A 1 301 ? 14.124  9.907   -26.534 0.60 26.10  ? 301  ARG A CA  1 
ATOM   2162 C  C   . ARG A 1 301 ? 14.217  8.391   -26.500 0.60 28.13  ? 301  ARG A C   1 
ATOM   2163 O  O   . ARG A 1 301 ? 13.305  7.690   -26.924 0.60 21.07  ? 301  ARG A O   1 
ATOM   2164 C  CB  . ARG A 1 301 ? 15.144  10.437  -27.550 0.60 23.91  ? 301  ARG A CB  1 
ATOM   2165 C  CG  . ARG A 1 301 ? 14.748  10.268  -29.014 0.60 35.50  ? 301  ARG A CG  1 
ATOM   2166 C  CD  . ARG A 1 301 ? 15.965  10.204  -29.935 0.60 31.79  ? 301  ARG A CD  1 
ATOM   2167 N  NE  . ARG A 1 301 ? 16.191  8.841   -30.414 0.60 40.06  ? 301  ARG A NE  1 
ATOM   2168 C  CZ  . ARG A 1 301 ? 17.388  8.302   -30.619 0.60 54.32  ? 301  ARG A CZ  1 
ATOM   2169 N  NH1 . ARG A 1 301 ? 18.487  9.006   -30.390 0.60 54.56  ? 301  ARG A NH1 1 
ATOM   2170 N  NH2 . ARG A 1 301 ? 17.487  7.054   -31.058 0.60 60.50  ? 301  ARG A NH2 1 
ATOM   2171 N  N   . ARG A 1 302 ? 15.338  7.897   -25.984 1.00 44.26  ? 302  ARG A N   1 
ATOM   2172 C  CA  . ARG A 1 302 ? 15.620  6.460   -25.933 1.00 50.67  ? 302  ARG A CA  1 
ATOM   2173 C  C   . ARG A 1 302 ? 14.694  5.737   -24.962 1.00 49.24  ? 302  ARG A C   1 
ATOM   2174 O  O   . ARG A 1 302 ? 14.141  4.686   -25.269 1.00 56.13  ? 302  ARG A O   1 
ATOM   2175 C  CB  . ARG A 1 302 ? 17.089  6.218   -25.571 1.00 53.86  ? 302  ARG A CB  1 
ATOM   2176 C  CG  . ARG A 1 302 ? 18.053  6.700   -26.661 1.00 62.60  ? 302  ARG A CG  1 
ATOM   2177 C  CD  . ARG A 1 302 ? 19.506  6.371   -26.357 1.00 71.33  ? 302  ARG A CD  1 
ATOM   2178 N  NE  . ARG A 1 302 ? 20.239  6.088   -27.587 1.00 82.72  ? 302  ARG A NE  1 
ATOM   2179 C  CZ  . ARG A 1 302 ? 20.595  4.869   -27.984 1.00 87.02  ? 302  ARG A CZ  1 
ATOM   2180 N  NH1 . ARG A 1 302 ? 20.307  3.818   -27.231 1.00 78.74  ? 302  ARG A NH1 1 
ATOM   2181 N  NH2 . ARG A 1 302 ? 21.253  4.702   -29.129 1.00 89.54  ? 302  ARG A NH2 1 
ATOM   2182 N  N   . THR A 1 303 ? 14.529  6.313   -23.784 1.00 50.27  ? 303  THR A N   1 
ATOM   2183 C  CA  . THR A 1 303 ? 13.561  5.816   -22.829 1.00 45.04  ? 303  THR A CA  1 
ATOM   2184 C  C   . THR A 1 303 ? 12.227  5.582   -23.528 1.00 45.28  ? 303  THR A C   1 
ATOM   2185 O  O   . THR A 1 303 ? 11.685  4.481   -23.486 1.00 45.39  ? 303  THR A O   1 
ATOM   2186 C  CB  . THR A 1 303 ? 13.345  6.838   -21.709 1.00 34.03  ? 303  THR A CB  1 
ATOM   2187 O  OG1 . THR A 1 303 ? 14.312  6.616   -20.686 1.00 56.15  ? 303  THR A OG1 1 
ATOM   2188 C  CG2 . THR A 1 303 ? 11.938  6.708   -21.139 1.00 28.77  ? 303  THR A CG2 1 
ATOM   2189 N  N   . HIS A 1 304 ? 11.703  6.627   -24.166 0.80 32.86  ? 304  HIS A N   1 
ATOM   2190 C  CA  . HIS A 1 304 ? 10.393  6.555   -24.789 0.80 28.96  ? 304  HIS A CA  1 
ATOM   2191 C  C   . HIS A 1 304 ? 10.328  5.474   -25.863 0.80 34.39  ? 304  HIS A C   1 
ATOM   2192 O  O   . HIS A 1 304 ? 9.286   4.860   -26.071 0.80 44.01  ? 304  HIS A O   1 
ATOM   2193 C  CB  . HIS A 1 304 ? 10.008  7.906   -25.385 0.80 35.02  ? 304  HIS A CB  1 
ATOM   2194 C  CG  . HIS A 1 304 ? 8.687   7.895   -26.087 0.80 47.54  ? 304  HIS A CG  1 
ATOM   2195 N  ND1 . HIS A 1 304 ? 7.501   7.636   -25.435 0.80 52.12  ? 304  HIS A ND1 1 
ATOM   2196 C  CD2 . HIS A 1 304 ? 8.366   8.097   -27.388 0.80 48.86  ? 304  HIS A CD2 1 
ATOM   2197 C  CE1 . HIS A 1 304 ? 6.504   7.683   -26.303 0.80 51.00  ? 304  HIS A CE1 1 
ATOM   2198 N  NE2 . HIS A 1 304 ? 7.002   7.965   -27.494 0.80 46.86  ? 304  HIS A NE2 1 
ATOM   2199 N  N   . ASN A 1 305 ? 11.451  5.238   -26.529 1.00 33.09  ? 305  ASN A N   1 
ATOM   2200 C  CA  . ASN A 1 305 ? 11.501  4.338   -27.685 1.00 36.95  ? 305  ASN A CA  1 
ATOM   2201 C  C   . ASN A 1 305 ? 11.959  2.904   -27.383 1.00 53.09  ? 305  ASN A C   1 
ATOM   2202 O  O   . ASN A 1 305 ? 11.977  2.058   -28.270 1.00 55.50  ? 305  ASN A O   1 
ATOM   2203 C  CB  . ASN A 1 305 ? 12.379  4.939   -28.784 1.00 41.62  ? 305  ASN A CB  1 
ATOM   2204 C  CG  . ASN A 1 305 ? 11.758  6.198   -29.417 1.00 63.28  ? 305  ASN A CG  1 
ATOM   2205 O  OD1 . ASN A 1 305 ? 10.536  6.381   -29.400 1.00 72.11  ? 305  ASN A OD1 1 
ATOM   2206 N  ND2 . ASN A 1 305 ? 12.603  7.065   -29.977 1.00 57.49  ? 305  ASN A ND2 1 
ATOM   2207 N  N   . GLY A 1 306 ? 12.336  2.622   -26.139 1.00 48.47  ? 306  GLY A N   1 
ATOM   2208 C  CA  . GLY A 1 306 ? 12.725  1.273   -25.784 1.00 34.46  ? 306  GLY A CA  1 
ATOM   2209 C  C   . GLY A 1 306 ? 14.161  0.901   -26.113 1.00 40.16  ? 306  GLY A C   1 
ATOM   2210 O  O   . GLY A 1 306 ? 14.527  -0.275  -26.047 1.00 46.21  ? 306  GLY A O   1 
ATOM   2211 N  N   . GLU A 1 307 ? 14.987  1.884   -26.461 1.00 45.39  ? 307  GLU A N   1 
ATOM   2212 C  CA  . GLU A 1 307 ? 16.400  1.604   -26.716 1.00 48.66  ? 307  GLU A CA  1 
ATOM   2213 C  C   . GLU A 1 307 ? 17.260  1.741   -25.458 1.00 52.75  ? 307  GLU A C   1 
ATOM   2214 O  O   . GLU A 1 307 ? 16.814  2.234   -24.412 1.00 46.01  ? 307  GLU A O   1 
ATOM   2215 C  CB  . GLU A 1 307 ? 16.968  2.457   -27.858 1.00 48.72  ? 307  GLU A CB  1 
ATOM   2216 C  CG  . GLU A 1 307 ? 17.557  1.636   -29.045 1.00 88.18  ? 307  GLU A CG  1 
ATOM   2217 C  CD  . GLU A 1 307 ? 18.953  1.030   -28.779 1.00 81.11  ? 307  GLU A CD  1 
ATOM   2218 O  OE1 . GLU A 1 307 ? 19.061  -0.206  -28.589 1.00 63.57  ? 307  GLU A OE1 1 
ATOM   2219 O  OE2 . GLU A 1 307 ? 19.947  1.788   -28.787 1.00 81.76  ? 307  GLU A OE2 1 
ATOM   2220 N  N   . SER A 1 308 ? 18.497  1.290   -25.583 1.00 53.14  ? 308  SER A N   1 
ATOM   2221 C  CA  . SER A 1 308 ? 19.402  1.191   -24.464 1.00 57.69  ? 308  SER A CA  1 
ATOM   2222 C  C   . SER A 1 308 ? 19.948  2.557   -24.052 1.00 63.89  ? 308  SER A C   1 
ATOM   2223 O  O   . SER A 1 308 ? 20.796  3.129   -24.729 1.00 69.80  ? 308  SER A O   1 
ATOM   2224 C  CB  . SER A 1 308 ? 20.547  0.244   -24.820 1.00 55.58  ? 308  SER A CB  1 
ATOM   2225 O  OG  . SER A 1 308 ? 21.535  0.246   -23.809 1.00 64.50  ? 308  SER A OG  1 
ATOM   2226 N  N   . VAL A 1 309 ? 19.457  3.068   -22.929 1.00 62.40  ? 309  VAL A N   1 
ATOM   2227 C  CA  . VAL A 1 309 ? 19.966  4.301   -22.360 1.00 60.32  ? 309  VAL A CA  1 
ATOM   2228 C  C   . VAL A 1 309 ? 21.318  4.030   -21.702 1.00 62.71  ? 309  VAL A C   1 
ATOM   2229 O  O   . VAL A 1 309 ? 22.082  4.953   -21.421 1.00 57.57  ? 309  VAL A O   1 
ATOM   2230 C  CB  . VAL A 1 309 ? 18.998  4.849   -21.295 1.00 69.53  ? 309  VAL A CB  1 
ATOM   2231 C  CG1 . VAL A 1 309 ? 19.323  6.289   -20.973 1.00 71.96  ? 309  VAL A CG1 1 
ATOM   2232 C  CG2 . VAL A 1 309 ? 17.561  4.736   -21.780 1.00 74.17  ? 309  VAL A CG2 1 
ATOM   2233 N  N   . SER A 1 310 ? 21.613  2.756   -21.461 0.79 66.66  ? 310  SER A N   1 
ATOM   2234 C  CA  . SER A 1 310 ? 22.814  2.377   -20.722 0.79 71.15  ? 310  SER A CA  1 
ATOM   2235 C  C   . SER A 1 310 ? 24.078  2.798   -21.454 0.79 67.39  ? 310  SER A C   1 
ATOM   2236 O  O   . SER A 1 310 ? 25.075  3.140   -20.830 0.79 58.94  ? 310  SER A O   1 
ATOM   2237 C  CB  . SER A 1 310 ? 22.847  0.868   -20.473 0.79 73.62  ? 310  SER A CB  1 
ATOM   2238 O  OG  . SER A 1 310 ? 23.175  0.168   -21.662 0.79 72.11  ? 310  SER A OG  1 
ATOM   2239 N  N   . TYR A 1 311 ? 24.039  2.763   -22.781 1.00 71.62  ? 311  TYR A N   1 
ATOM   2240 C  CA  . TYR A 1 311 ? 25.190  3.186   -23.569 1.00 75.03  ? 311  TYR A CA  1 
ATOM   2241 C  C   . TYR A 1 311 ? 25.653  4.599   -23.180 1.00 71.01  ? 311  TYR A C   1 
ATOM   2242 O  O   . TYR A 1 311 ? 26.854  4.869   -23.128 1.00 68.82  ? 311  TYR A O   1 
ATOM   2243 C  CB  . TYR A 1 311 ? 24.892  3.090   -25.071 1.00 72.78  ? 311  TYR A CB  1 
ATOM   2244 C  CG  . TYR A 1 311 ? 24.666  4.416   -25.747 1.00 81.91  ? 311  TYR A CG  1 
ATOM   2245 C  CD1 . TYR A 1 311 ? 25.738  5.195   -26.164 1.00 90.45  ? 311  TYR A CD1 1 
ATOM   2246 C  CD2 . TYR A 1 311 ? 23.381  4.888   -25.980 1.00 89.94  ? 311  TYR A CD2 1 
ATOM   2247 C  CE1 . TYR A 1 311 ? 25.534  6.416   -26.789 1.00 99.26  ? 311  TYR A CE1 1 
ATOM   2248 C  CE2 . TYR A 1 311 ? 23.167  6.106   -26.608 1.00 96.34  ? 311  TYR A CE2 1 
ATOM   2249 C  CZ  . TYR A 1 311 ? 24.245  6.866   -27.011 1.00 99.71  ? 311  TYR A CZ  1 
ATOM   2250 O  OH  . TYR A 1 311 ? 24.032  8.080   -27.633 1.00 99.54  ? 311  TYR A OH  1 
ATOM   2251 N  N   . LEU A 1 312 ? 24.699  5.485   -22.894 1.00 66.28  ? 312  LEU A N   1 
ATOM   2252 C  CA  . LEU A 1 312 ? 25.006  6.847   -22.448 1.00 55.26  ? 312  LEU A CA  1 
ATOM   2253 C  C   . LEU A 1 312 ? 25.898  6.879   -21.210 1.00 55.79  ? 312  LEU A C   1 
ATOM   2254 O  O   . LEU A 1 312 ? 26.567  7.882   -20.948 1.00 55.64  ? 312  LEU A O   1 
ATOM   2255 C  CB  . LEU A 1 312 ? 23.726  7.629   -22.153 1.00 45.13  ? 312  LEU A CB  1 
ATOM   2256 C  CG  . LEU A 1 312 ? 22.856  8.096   -23.316 1.00 47.18  ? 312  LEU A CG  1 
ATOM   2257 C  CD1 . LEU A 1 312 ? 21.592  8.770   -22.798 1.00 35.63  ? 312  LEU A CD1 1 
ATOM   2258 C  CD2 . LEU A 1 312 ? 23.644  9.041   -24.198 1.00 54.41  ? 312  LEU A CD2 1 
ATOM   2259 N  N   . PHE A 1 313 ? 25.897  5.793   -20.441 1.00 63.27  ? 313  PHE A N   1 
ATOM   2260 C  CA  . PHE A 1 313 ? 26.634  5.748   -19.172 1.00 67.49  ? 313  PHE A CA  1 
ATOM   2261 C  C   . PHE A 1 313 ? 28.137  5.881   -19.385 1.00 63.89  ? 313  PHE A C   1 
ATOM   2262 O  O   . PHE A 1 313 ? 28.858  6.403   -18.530 1.00 70.80  ? 313  PHE A O   1 
ATOM   2263 C  CB  . PHE A 1 313 ? 26.341  4.449   -18.397 1.00 68.41  ? 313  PHE A CB  1 
ATOM   2264 C  CG  . PHE A 1 313 ? 24.947  4.371   -17.820 1.00 67.70  ? 313  PHE A CG  1 
ATOM   2265 C  CD1 . PHE A 1 313 ? 24.530  3.229   -17.150 1.00 60.11  ? 313  PHE A CD1 1 
ATOM   2266 C  CD2 . PHE A 1 313 ? 24.054  5.427   -17.956 1.00 66.83  ? 313  PHE A CD2 1 
ATOM   2267 C  CE1 . PHE A 1 313 ? 23.259  3.146   -16.616 1.00 58.41  ? 313  PHE A CE1 1 
ATOM   2268 C  CE2 . PHE A 1 313 ? 22.773  5.349   -17.425 1.00 61.26  ? 313  PHE A CE2 1 
ATOM   2269 C  CZ  . PHE A 1 313 ? 22.376  4.210   -16.755 1.00 61.96  ? 313  PHE A CZ  1 
ATOM   2270 N  N   . SER A 1 314 ? 28.603  5.398   -20.532 0.50 58.61  ? 314  SER A N   1 
ATOM   2271 C  CA  . SER A 1 314 ? 30.034  5.335   -20.811 0.50 55.28  ? 314  SER A CA  1 
ATOM   2272 C  C   . SER A 1 314 ? 30.443  6.341   -21.884 0.50 54.15  ? 314  SER A C   1 
ATOM   2273 O  O   . SER A 1 314 ? 31.604  6.761   -21.940 0.50 53.41  ? 314  SER A O   1 
ATOM   2274 C  CB  . SER A 1 314 ? 30.421  3.911   -21.242 0.50 57.12  ? 314  SER A CB  1 
ATOM   2275 O  OG  . SER A 1 314 ? 29.720  3.533   -22.426 0.50 59.03  ? 314  SER A OG  1 
ATOM   2276 N  N   . HIS A 1 315 ? 29.484  6.725   -22.729 0.50 51.40  ? 315  HIS A N   1 
ATOM   2277 C  CA  . HIS A 1 315 ? 29.752  7.607   -23.860 0.50 51.25  ? 315  HIS A CA  1 
ATOM   2278 C  C   . HIS A 1 315 ? 28.982  8.926   -23.781 0.50 58.34  ? 315  HIS A C   1 
ATOM   2279 O  O   . HIS A 1 315 ? 28.156  9.127   -22.896 0.50 51.61  ? 315  HIS A O   1 
ATOM   2280 C  CB  . HIS A 1 315 ? 29.400  6.897   -25.168 0.50 50.54  ? 315  HIS A CB  1 
ATOM   2281 N  N   . VAL A 1 316 ? 29.233  9.817   -24.741 1.00 74.20  ? 316  VAL A N   1 
ATOM   2282 C  CA  . VAL A 1 316 ? 28.630  11.149  -24.728 1.00 79.30  ? 316  VAL A CA  1 
ATOM   2283 C  C   . VAL A 1 316 ? 27.900  11.315  -26.035 1.00 81.98  ? 316  VAL A C   1 
ATOM   2284 O  O   . VAL A 1 316 ? 28.552  11.448  -27.084 1.00 83.27  ? 316  VAL A O   1 
ATOM   2285 C  CB  . VAL A 1 316 ? 29.706  12.264  -24.605 1.00 74.09  ? 316  VAL A CB  1 
ATOM   2286 C  CG1 . VAL A 1 316 ? 29.203  13.390  -23.614 1.00 66.63  ? 316  VAL A CG1 1 
ATOM   2287 C  CG2 . VAL A 1 316 ? 31.016  11.692  -23.997 1.00 53.40  ? 316  VAL A CG2 1 
ATOM   2288 N  N   . ASN B 1 3   ? 5.320   -10.089 28.030  1.00 73.25  ? 3    ASN B N   1 
ATOM   2289 C  CA  . ASN B 1 3   ? 6.290   -9.033  27.752  1.00 75.40  ? 3    ASN B CA  1 
ATOM   2290 C  C   . ASN B 1 3   ? 7.033   -9.192  26.407  1.00 62.10  ? 3    ASN B C   1 
ATOM   2291 O  O   . ASN B 1 3   ? 6.481   -8.917  25.331  1.00 58.84  ? 3    ASN B O   1 
ATOM   2292 C  CB  . ASN B 1 3   ? 7.295   -8.959  28.901  1.00 84.58  ? 3    ASN B CB  1 
ATOM   2293 C  CG  . ASN B 1 3   ? 8.008   -7.630  28.965  1.00 90.65  ? 3    ASN B CG  1 
ATOM   2294 O  OD1 . ASN B 1 3   ? 7.371   -6.573  28.942  1.00 101.02 ? 3    ASN B OD1 1 
ATOM   2295 N  ND2 . ASN B 1 3   ? 9.338   -7.671  29.050  1.00 81.72  ? 3    ASN B ND2 1 
ATOM   2296 N  N   . ILE B 1 4   ? 8.282   -9.649  26.491  1.00 45.50  ? 4    ILE B N   1 
ATOM   2297 C  CA  . ILE B 1 4   ? 9.146   -9.869  25.335  1.00 48.31  ? 4    ILE B CA  1 
ATOM   2298 C  C   . ILE B 1 4   ? 9.378   -11.372 25.088  1.00 42.36  ? 4    ILE B C   1 
ATOM   2299 O  O   . ILE B 1 4   ? 9.488   -12.159 26.027  1.00 34.18  ? 4    ILE B O   1 
ATOM   2300 C  CB  . ILE B 1 4   ? 10.520  -9.231  25.593  1.00 54.44  ? 4    ILE B CB  1 
ATOM   2301 C  CG1 . ILE B 1 4   ? 11.305  -9.068  24.306  1.00 55.14  ? 4    ILE B CG1 1 
ATOM   2302 C  CG2 . ILE B 1 4   ? 11.315  -10.084 26.559  1.00 61.02  ? 4    ILE B CG2 1 
ATOM   2303 C  CD1 . ILE B 1 4   ? 12.781  -9.307  24.513  1.00 48.30  ? 4    ILE B CD1 1 
ATOM   2304 N  N   . LYS B 1 5   ? 9.445   -11.769 23.823  1.00 37.97  ? 5    LYS B N   1 
ATOM   2305 C  CA  . LYS B 1 5   ? 9.711   -13.160 23.469  1.00 31.68  ? 5    LYS B CA  1 
ATOM   2306 C  C   . LYS B 1 5   ? 10.834  -13.226 22.427  1.00 34.13  ? 5    LYS B C   1 
ATOM   2307 O  O   . LYS B 1 5   ? 10.741  -12.570 21.391  1.00 34.40  ? 5    LYS B O   1 
ATOM   2308 C  CB  . LYS B 1 5   ? 8.436   -13.809 22.916  1.00 32.86  ? 5    LYS B CB  1 
ATOM   2309 C  CG  . LYS B 1 5   ? 7.817   -14.902 23.773  1.00 47.65  ? 5    LYS B CG  1 
ATOM   2310 C  CD  . LYS B 1 5   ? 7.243   -14.350 25.073  1.00 61.70  ? 5    LYS B CD  1 
ATOM   2311 C  CE  . LYS B 1 5   ? 6.522   -15.421 25.877  1.00 61.78  ? 5    LYS B CE  1 
ATOM   2312 N  N   . ILE B 1 6   ? 11.887  -13.999 22.693  1.00 31.39  ? 6    ILE B N   1 
ATOM   2313 C  CA  . ILE B 1 6   ? 12.971  -14.145 21.717  1.00 28.91  ? 6    ILE B CA  1 
ATOM   2314 C  C   . ILE B 1 6   ? 12.913  -15.517 21.072  1.00 26.23  ? 6    ILE B C   1 
ATOM   2315 O  O   . ILE B 1 6   ? 12.813  -16.523 21.764  1.00 29.04  ? 6    ILE B O   1 
ATOM   2316 C  CB  . ILE B 1 6   ? 14.380  -14.031 22.329  1.00 36.92  ? 6    ILE B CB  1 
ATOM   2317 C  CG1 . ILE B 1 6   ? 14.396  -13.127 23.556  1.00 46.30  ? 6    ILE B CG1 1 
ATOM   2318 C  CG2 . ILE B 1 6   ? 15.380  -13.546 21.270  1.00 29.10  ? 6    ILE B CG2 1 
ATOM   2319 C  CD1 . ILE B 1 6   ? 14.899  -11.730 23.249  1.00 54.64  ? 6    ILE B CD1 1 
ATOM   2320 N  N   . PHE B 1 7   ? 12.975  -15.555 19.745  1.00 25.74  ? 7    PHE B N   1 
ATOM   2321 C  CA  . PHE B 1 7   ? 13.041  -16.818 19.027  1.00 27.47  ? 7    PHE B CA  1 
ATOM   2322 C  C   . PHE B 1 7   ? 14.298  -16.820 18.192  1.00 30.82  ? 7    PHE B C   1 
ATOM   2323 O  O   . PHE B 1 7   ? 14.791  -15.764 17.804  1.00 38.46  ? 7    PHE B O   1 
ATOM   2324 C  CB  . PHE B 1 7   ? 11.835  -16.995 18.105  1.00 23.45  ? 7    PHE B CB  1 
ATOM   2325 C  CG  . PHE B 1 7   ? 10.539  -17.217 18.823  1.00 29.42  ? 7    PHE B CG  1 
ATOM   2326 C  CD1 . PHE B 1 7   ? 9.731   -16.151 19.170  1.00 31.12  ? 7    PHE B CD1 1 
ATOM   2327 C  CD2 . PHE B 1 7   ? 10.118  -18.493 19.127  1.00 22.98  ? 7    PHE B CD2 1 
ATOM   2328 C  CE1 . PHE B 1 7   ? 8.533   -16.362 19.811  1.00 33.23  ? 7    PHE B CE1 1 
ATOM   2329 C  CE2 . PHE B 1 7   ? 8.909   -18.709 19.768  1.00 31.67  ? 7    PHE B CE2 1 
ATOM   2330 C  CZ  . PHE B 1 7   ? 8.120   -17.640 20.108  1.00 25.06  ? 7    PHE B CZ  1 
ATOM   2331 N  N   . SER B 1 8   ? 14.820  -18.000 17.906  1.00 25.86  ? 8    SER B N   1 
ATOM   2332 C  CA  . SER B 1 8   ? 15.999  -18.077 17.067  1.00 35.58  ? 8    SER B CA  1 
ATOM   2333 C  C   . SER B 1 8   ? 15.618  -18.578 15.682  1.00 52.23  ? 8    SER B C   1 
ATOM   2334 O  O   . SER B 1 8   ? 14.791  -19.489 15.549  1.00 44.91  ? 8    SER B O   1 
ATOM   2335 C  CB  . SER B 1 8   ? 17.036  -18.994 17.677  1.00 42.89  ? 8    SER B CB  1 
ATOM   2336 O  OG  . SER B 1 8   ? 18.042  -19.254 16.727  1.00 46.32  ? 8    SER B OG  1 
ATOM   2337 N  N   . GLY B 1 9   ? 16.221  -17.967 14.662  1.00 62.33  ? 9    GLY B N   1 
ATOM   2338 C  CA  . GLY B 1 9   ? 15.981  -18.317 13.274  1.00 60.01  ? 9    GLY B CA  1 
ATOM   2339 C  C   . GLY B 1 9   ? 16.000  -19.813 13.016  1.00 72.67  ? 9    GLY B C   1 
ATOM   2340 O  O   . GLY B 1 9   ? 15.076  -20.342 12.402  1.00 76.18  ? 9    GLY B O   1 
ATOM   2341 N  N   . SER B 1 10  ? 17.034  -20.503 13.496  1.00 79.48  ? 10   SER B N   1 
ATOM   2342 C  CA  . SER B 1 10  ? 17.172  -21.938 13.244  1.00 88.49  ? 10   SER B CA  1 
ATOM   2343 C  C   . SER B 1 10  ? 18.129  -22.645 14.190  1.00 94.11  ? 10   SER B C   1 
ATOM   2344 O  O   . SER B 1 10  ? 18.304  -22.240 15.338  1.00 91.77  ? 10   SER B O   1 
ATOM   2345 C  CB  . SER B 1 10  ? 17.620  -22.204 11.797  1.00 95.18  ? 10   SER B CB  1 
ATOM   2346 O  OG  . SER B 1 10  ? 19.033  -22.120 11.637  1.00 96.65  ? 10   SER B OG  1 
ATOM   2347 N  N   . SER B 1 11  ? 18.748  -23.704 13.673  1.00 100.64 ? 11   SER B N   1 
ATOM   2348 C  CA  . SER B 1 11  ? 19.605  -24.578 14.458  1.00 107.94 ? 11   SER B CA  1 
ATOM   2349 C  C   . SER B 1 11  ? 20.760  -23.823 15.109  1.00 113.67 ? 11   SER B C   1 
ATOM   2350 O  O   . SER B 1 11  ? 21.308  -24.271 16.116  1.00 122.18 ? 11   SER B O   1 
ATOM   2351 C  CB  . SER B 1 11  ? 20.129  -25.734 13.600  1.00 108.59 ? 11   SER B CB  1 
ATOM   2352 O  OG  . SER B 1 11  ? 20.746  -26.726 14.405  1.00 105.29 ? 11   SER B OG  1 
ATOM   2353 N  N   . HIS B 1 12  ? 21.143  -22.688 14.537  1.00 106.87 ? 12   HIS B N   1 
ATOM   2354 C  CA  . HIS B 1 12  ? 22.075  -21.818 15.236  1.00 108.72 ? 12   HIS B CA  1 
ATOM   2355 C  C   . HIS B 1 12  ? 21.340  -21.084 16.348  1.00 109.99 ? 12   HIS B C   1 
ATOM   2356 O  O   . HIS B 1 12  ? 20.612  -20.124 16.096  1.00 118.66 ? 12   HIS B O   1 
ATOM   2357 C  CB  . HIS B 1 12  ? 22.707  -20.790 14.308  1.00 109.78 ? 12   HIS B CB  1 
ATOM   2358 C  CG  . HIS B 1 12  ? 23.016  -19.495 14.993  1.00 108.59 ? 12   HIS B CG  1 
ATOM   2359 N  ND1 . HIS B 1 12  ? 22.106  -18.466 15.081  1.00 104.96 ? 12   HIS B ND1 1 
ATOM   2360 C  CD2 . HIS B 1 12  ? 24.119  -19.080 15.658  1.00 107.98 ? 12   HIS B CD2 1 
ATOM   2361 C  CE1 . HIS B 1 12  ? 22.639  -17.466 15.761  1.00 104.28 ? 12   HIS B CE1 1 
ATOM   2362 N  NE2 . HIS B 1 12  ? 23.862  -17.812 16.116  1.00 106.30 ? 12   HIS B NE2 1 
ATOM   2363 N  N   . GLN B 1 13  ? 21.507  -21.552 17.577  1.00 98.23  ? 13   GLN B N   1 
ATOM   2364 C  CA  . GLN B 1 13  ? 20.954  -20.846 18.723  1.00 82.55  ? 13   GLN B CA  1 
ATOM   2365 C  C   . GLN B 1 13  ? 22.105  -20.051 19.322  1.00 67.07  ? 13   GLN B C   1 
ATOM   2366 O  O   . GLN B 1 13  ? 21.901  -19.085 20.045  1.00 67.13  ? 13   GLN B O   1 
ATOM   2367 C  CB  . GLN B 1 13  ? 20.397  -21.834 19.749  1.00 76.66  ? 13   GLN B CB  1 
ATOM   2368 C  CG  . GLN B 1 13  ? 19.546  -22.962 19.156  1.00 74.04  ? 13   GLN B CG  1 
ATOM   2369 C  CD  . GLN B 1 13  ? 18.054  -22.694 19.255  1.00 73.59  ? 13   GLN B CD  1 
ATOM   2370 O  OE1 . GLN B 1 13  ? 17.496  -21.939 18.459  1.00 78.06  ? 13   GLN B OE1 1 
ATOM   2371 N  NE2 . GLN B 1 13  ? 17.399  -23.317 20.231  1.00 65.52  ? 13   GLN B NE2 1 
ATOM   2372 N  N   . ASP B 1 14  ? 23.299  -20.441 18.945  1.00 46.91  ? 14   ASP B N   1 
ATOM   2373 C  CA  . ASP B 1 14  ? 24.506  -19.835 19.414  1.00 47.89  ? 14   ASP B CA  1 
ATOM   2374 C  C   . ASP B 1 14  ? 24.733  -18.395 19.785  1.00 41.85  ? 14   ASP B C   1 
ATOM   2375 O  O   . ASP B 1 14  ? 25.470  -18.117 20.674  1.00 39.34  ? 14   ASP B O   1 
ATOM   2376 C  CB  . ASP B 1 14  ? 25.541  -19.891 18.321  1.00 64.59  ? 14   ASP B CB  1 
ATOM   2377 C  CG  . ASP B 1 14  ? 26.922  -20.080 18.852  1.00 79.68  ? 14   ASP B CG  1 
ATOM   2378 O  OD1 . ASP B 1 14  ? 27.119  -19.832 20.052  1.00 77.95  ? 14   ASP B OD1 1 
ATOM   2379 O  OD2 . ASP B 1 14  ? 27.802  -20.466 18.061  1.00 82.97  ? 14   ASP B OD2 1 
ATOM   2380 N  N   . LEU B 1 15  ? 24.089  -17.493 19.071  1.00 35.93  ? 15   LEU B N   1 
ATOM   2381 C  CA  . LEU B 1 15  ? 24.189  -16.079 19.296  1.00 28.36  ? 15   LEU B CA  1 
ATOM   2382 C  C   . LEU B 1 15  ? 22.873  -15.763 19.945  1.00 30.72  ? 15   LEU B C   1 
ATOM   2383 O  O   . LEU B 1 15  ? 22.838  -14.997 20.837  1.00 39.36  ? 15   LEU B O   1 
ATOM   2384 C  CB  . LEU B 1 15  ? 24.331  -15.258 18.037  1.00 34.67  ? 15   LEU B CB  1 
ATOM   2385 C  CG  . LEU B 1 15  ? 24.986  -13.889 17.966  1.00 39.63  ? 15   LEU B CG  1 
ATOM   2386 C  CD1 . LEU B 1 15  ? 24.456  -13.101 16.841  1.00 31.80  ? 15   LEU B CD1 1 
ATOM   2387 C  CD2 . LEU B 1 15  ? 25.072  -13.094 19.197  1.00 25.32  ? 15   LEU B CD2 1 
ATOM   2388 N  N   . SER B 1 16  ? 21.791  -16.355 19.492  1.00 25.91  ? 16   SER B N   1 
ATOM   2389 C  CA  . SER B 1 16  ? 20.473  -16.091 20.062  1.00 34.95  ? 16   SER B CA  1 
ATOM   2390 C  C   . SER B 1 16  ? 20.362  -16.539 21.523  1.00 30.04  ? 16   SER B C   1 
ATOM   2391 O  O   . SER B 1 16  ? 19.756  -15.854 22.345  1.00 31.99  ? 16   SER B O   1 
ATOM   2392 C  CB  . SER B 1 16  ? 19.364  -16.690 19.187  1.00 31.27  ? 16   SER B CB  1 
ATOM   2393 O  OG  . SER B 1 16  ? 19.639  -18.036 18.844  1.00 37.92  ? 16   SER B OG  1 
ATOM   2394 N  N   . GLN B 1 17  ? 20.977  -17.675 21.829  1.00 33.40  ? 17   GLN B N   1 
ATOM   2395 C  CA  . GLN B 1 17  ? 21.088  -18.194 23.188  1.00 27.73  ? 17   GLN B CA  1 
ATOM   2396 C  C   . GLN B 1 17  ? 21.933  -17.256 24.054  1.00 31.69  ? 17   GLN B C   1 
ATOM   2397 O  O   . GLN B 1 17  ? 21.550  -16.937 25.183  1.00 39.24  ? 17   GLN B O   1 
ATOM   2398 C  CB  . GLN B 1 17  ? 21.662  -19.620 23.158  1.00 33.96  ? 17   GLN B CB  1 
ATOM   2399 C  CG  . GLN B 1 17  ? 21.601  -20.371 24.481  1.00 42.00  ? 17   GLN B CG  1 
ATOM   2400 C  CD  . GLN B 1 17  ? 20.191  -20.470 25.043  1.00 52.83  ? 17   GLN B CD  1 
ATOM   2401 O  OE1 . GLN B 1 17  ? 19.363  -21.241 24.547  1.00 54.41  ? 17   GLN B OE1 1 
ATOM   2402 N  NE2 . GLN B 1 17  ? 19.911  -19.689 26.090  1.00 52.69  ? 17   GLN B NE2 1 
ATOM   2403 N  N   . LYS B 1 18  ? 23.063  -16.781 23.541  1.00 33.09  ? 18   LYS B N   1 
ATOM   2404 C  CA  . LYS B 1 18  ? 23.837  -15.776 24.291  1.00 38.55  ? 18   LYS B CA  1 
ATOM   2405 C  C   . LYS B 1 18  ? 23.017  -14.534 24.635  1.00 39.64  ? 18   LYS B C   1 
ATOM   2406 O  O   . LYS B 1 18  ? 23.101  -13.993 25.741  1.00 38.45  ? 18   LYS B O   1 
ATOM   2407 C  CB  . LYS B 1 18  ? 25.082  -15.337 23.523  1.00 41.40  ? 18   LYS B CB  1 
ATOM   2408 C  CG  . LYS B 1 18  ? 26.160  -16.380 23.443  1.00 40.77  ? 18   LYS B CG  1 
ATOM   2409 C  CD  . LYS B 1 18  ? 27.465  -15.765 22.987  1.00 48.82  ? 18   LYS B CD  1 
ATOM   2410 C  CE  . LYS B 1 18  ? 28.584  -16.791 22.972  1.00 60.64  ? 18   LYS B CE  1 
ATOM   2411 N  NZ  . LYS B 1 18  ? 29.885  -16.174 22.573  1.00 73.69  ? 18   LYS B NZ  1 
ATOM   2412 N  N   . ILE B 1 19  ? 22.235  -14.080 23.663  1.00 37.15  ? 19   ILE B N   1 
ATOM   2413 C  CA  . ILE B 1 19  ? 21.416  -12.888 23.808  1.00 31.07  ? 19   ILE B CA  1 
ATOM   2414 C  C   . ILE B 1 19  ? 20.291  -13.089 24.819  1.00 32.47  ? 19   ILE B C   1 
ATOM   2415 O  O   . ILE B 1 19  ? 20.056  -12.235 25.666  1.00 30.18  ? 19   ILE B O   1 
ATOM   2416 C  CB  . ILE B 1 19  ? 20.805  -12.457 22.446  1.00 31.31  ? 19   ILE B CB  1 
ATOM   2417 C  CG1 . ILE B 1 19  ? 21.900  -11.962 21.498  1.00 30.07  ? 19   ILE B CG1 1 
ATOM   2418 C  CG2 . ILE B 1 19  ? 19.794  -11.381 22.657  1.00 22.22  ? 19   ILE B CG2 1 
ATOM   2419 C  CD1 . ILE B 1 19  ? 21.477  -11.807 20.035  1.00 15.08  ? 19   ILE B CD1 1 
ATOM   2420 N  N   . ALA B 1 20  ? 19.580  -14.206 24.706  1.00 33.02  ? 20   ALA B N   1 
ATOM   2421 C  CA  . ALA B 1 20  ? 18.482  -14.506 25.613  1.00 37.89  ? 20   ALA B CA  1 
ATOM   2422 C  C   . ALA B 1 20  ? 18.997  -14.629 27.049  1.00 35.03  ? 20   ALA B C   1 
ATOM   2423 O  O   . ALA B 1 20  ? 18.369  -14.133 27.978  1.00 34.77  ? 20   ALA B O   1 
ATOM   2424 C  CB  . ALA B 1 20  ? 17.751  -15.785 25.178  1.00 26.29  ? 20   ALA B CB  1 
ATOM   2425 N  N   . ASP B 1 21  ? 20.144  -15.280 27.215  1.00 34.00  ? 21   ASP B N   1 
ATOM   2426 C  CA  . ASP B 1 21  ? 20.785  -15.392 28.526  1.00 41.95  ? 21   ASP B CA  1 
ATOM   2427 C  C   . ASP B 1 21  ? 20.963  -14.009 29.111  1.00 48.16  ? 21   ASP B C   1 
ATOM   2428 O  O   . ASP B 1 21  ? 20.475  -13.726 30.212  1.00 42.98  ? 21   ASP B O   1 
ATOM   2429 C  CB  . ASP B 1 21  ? 22.151  -16.089 28.437  1.00 44.16  ? 21   ASP B CB  1 
ATOM   2430 C  CG  . ASP B 1 21  ? 22.036  -17.578 28.139  1.00 53.57  ? 21   ASP B CG  1 
ATOM   2431 O  OD1 . ASP B 1 21  ? 20.920  -18.127 28.266  1.00 58.17  ? 21   ASP B OD1 1 
ATOM   2432 O  OD2 . ASP B 1 21  ? 23.064  -18.205 27.786  1.00 56.49  ? 21   ASP B OD2 1 
ATOM   2433 N  N   . ARG B 1 22  ? 21.636  -13.137 28.360  1.00 40.90  ? 22   ARG B N   1 
ATOM   2434 C  CA  . ARG B 1 22  ? 21.931  -11.794 28.849  1.00 38.41  ? 22   ARG B CA  1 
ATOM   2435 C  C   . ARG B 1 22  ? 20.667  -11.028 29.205  1.00 42.24  ? 22   ARG B C   1 
ATOM   2436 O  O   . ARG B 1 22  ? 20.715  -10.041 29.938  1.00 53.76  ? 22   ARG B O   1 
ATOM   2437 C  CB  . ARG B 1 22  ? 22.765  -11.008 27.839  1.00 32.50  ? 22   ARG B CB  1 
ATOM   2438 C  CG  . ARG B 1 22  ? 24.210  -11.484 27.721  1.00 40.52  ? 22   ARG B CG  1 
ATOM   2439 C  CD  . ARG B 1 22  ? 24.983  -10.720 26.638  1.00 51.61  ? 22   ARG B CD  1 
ATOM   2440 N  NE  . ARG B 1 22  ? 26.304  -10.295 27.096  1.00 70.91  ? 22   ARG B NE  1 
ATOM   2441 C  CZ  . ARG B 1 22  ? 27.372  -11.088 27.165  1.00 79.96  ? 22   ARG B CZ  1 
ATOM   2442 N  NH1 . ARG B 1 22  ? 27.286  -12.364 26.813  1.00 79.16  ? 22   ARG B NH1 1 
ATOM   2443 N  NH2 . ARG B 1 22  ? 28.532  -10.607 27.590  1.00 81.21  ? 22   ARG B NH2 1 
ATOM   2444 N  N   . LEU B 1 23  ? 19.530  -11.484 28.701  1.00 33.26  ? 23   LEU B N   1 
ATOM   2445 C  CA  . LEU B 1 23  ? 18.276  -10.793 28.969  1.00 30.51  ? 23   LEU B CA  1 
ATOM   2446 C  C   . LEU B 1 23  ? 17.476  -11.453 30.076  1.00 34.48  ? 23   LEU B C   1 
ATOM   2447 O  O   . LEU B 1 23  ? 16.416  -10.956 30.453  1.00 29.79  ? 23   LEU B O   1 
ATOM   2448 C  CB  . LEU B 1 23  ? 17.428  -10.722 27.703  1.00 37.30  ? 23   LEU B CB  1 
ATOM   2449 C  CG  . LEU B 1 23  ? 17.938  -9.795  26.596  1.00 36.04  ? 23   LEU B CG  1 
ATOM   2450 C  CD1 . LEU B 1 23  ? 17.130  -9.986  25.336  1.00 27.42  ? 23   LEU B CD1 1 
ATOM   2451 C  CD2 . LEU B 1 23  ? 17.883  -8.343  27.034  1.00 40.65  ? 23   LEU B CD2 1 
ATOM   2452 N  N   . GLY B 1 24  ? 17.979  -12.573 30.584  1.00 37.84  ? 24   GLY B N   1 
ATOM   2453 C  CA  . GLY B 1 24  ? 17.289  -13.329 31.618  1.00 39.74  ? 24   GLY B CA  1 
ATOM   2454 C  C   . GLY B 1 24  ? 16.133  -14.154 31.086  1.00 38.84  ? 24   GLY B C   1 
ATOM   2455 O  O   . GLY B 1 24  ? 15.161  -14.381 31.800  1.00 39.15  ? 24   GLY B O   1 
ATOM   2456 N  N   . LEU B 1 25  ? 16.246  -14.610 29.837  1.00 36.98  ? 25   LEU B N   1 
ATOM   2457 C  CA  . LEU B 1 25  ? 15.132  -15.263 29.133  1.00 33.00  ? 25   LEU B CA  1 
ATOM   2458 C  C   . LEU B 1 25  ? 15.534  -16.608 28.537  1.00 32.62  ? 25   LEU B C   1 
ATOM   2459 O  O   . LEU B 1 25  ? 16.708  -16.854 28.274  1.00 30.09  ? 25   LEU B O   1 
ATOM   2460 C  CB  . LEU B 1 25  ? 14.613  -14.359 28.001  1.00 28.10  ? 25   LEU B CB  1 
ATOM   2461 C  CG  . LEU B 1 25  ? 14.067  -12.994 28.432  1.00 34.24  ? 25   LEU B CG  1 
ATOM   2462 C  CD1 . LEU B 1 25  ? 13.750  -12.133 27.219  1.00 39.38  ? 25   LEU B CD1 1 
ATOM   2463 C  CD2 . LEU B 1 25  ? 12.817  -13.150 29.320  1.00 27.48  ? 25   LEU B CD2 1 
ATOM   2464 N  N   . GLU B 1 26  ? 14.554  -17.477 28.332  0.80 20.78  ? 26   GLU B N   1 
ATOM   2465 C  CA  . GLU B 1 26  ? 14.769  -18.639 27.504  0.80 17.32  ? 26   GLU B CA  1 
ATOM   2466 C  C   . GLU B 1 26  ? 14.219  -18.338 26.117  0.80 26.36  ? 26   GLU B C   1 
ATOM   2467 O  O   . GLU B 1 26  ? 13.213  -17.652 25.969  0.80 22.15  ? 26   GLU B O   1 
ATOM   2468 C  CB  . GLU B 1 26  ? 14.065  -19.860 28.060  0.80 15.11  ? 26   GLU B CB  1 
ATOM   2469 C  CG  . GLU B 1 26  ? 14.510  -20.256 29.451  0.80 35.89  ? 26   GLU B CG  1 
ATOM   2470 C  CD  . GLU B 1 26  ? 13.746  -21.460 29.962  0.80 52.22  ? 26   GLU B CD  1 
ATOM   2471 O  OE1 . GLU B 1 26  ? 12.800  -21.902 29.263  0.80 45.96  ? 26   GLU B OE1 1 
ATOM   2472 O  OE2 . GLU B 1 26  ? 14.094  -21.962 31.056  0.80 64.66  ? 26   GLU B OE2 1 
ATOM   2473 N  N   . LEU B 1 27  ? 14.902  -18.843 25.103  1.00 25.96  ? 27   LEU B N   1 
ATOM   2474 C  CA  . LEU B 1 27  ? 14.394  -18.784 23.734  1.00 33.11  ? 27   LEU B CA  1 
ATOM   2475 C  C   . LEU B 1 27  ? 13.041  -19.497 23.645  1.00 25.43  ? 27   LEU B C   1 
ATOM   2476 O  O   . LEU B 1 27  ? 12.857  -20.581 24.197  1.00 29.90  ? 27   LEU B O   1 
ATOM   2477 C  CB  . LEU B 1 27  ? 15.397  -19.420 22.772  1.00 25.70  ? 27   LEU B CB  1 
ATOM   2478 C  CG  . LEU B 1 27  ? 16.683  -18.622 22.531  1.00 22.76  ? 27   LEU B CG  1 
ATOM   2479 C  CD1 . LEU B 1 27  ? 17.743  -19.475 21.777  1.00 24.53  ? 27   LEU B CD1 1 
ATOM   2480 C  CD2 . LEU B 1 27  ? 16.402  -17.317 21.750  1.00 32.93  ? 27   LEU B CD2 1 
ATOM   2481 N  N   . GLY B 1 28  ? 12.086  -18.873 22.969  1.00 30.75  ? 28   GLY B N   1 
ATOM   2482 C  CA  . GLY B 1 28  ? 10.786  -19.479 22.761  1.00 24.21  ? 28   GLY B CA  1 
ATOM   2483 C  C   . GLY B 1 28  ? 10.827  -20.780 21.973  1.00 34.94  ? 28   GLY B C   1 
ATOM   2484 O  O   . GLY B 1 28  ? 11.789  -21.071 21.247  1.00 34.17  ? 28   GLY B O   1 
ATOM   2485 N  N   . LYS B 1 29  ? 9.771   -21.572 22.116  1.00 29.14  ? 29   LYS B N   1 
ATOM   2486 C  CA  . LYS B 1 29  ? 9.723   -22.884 21.495  1.00 35.70  ? 29   LYS B CA  1 
ATOM   2487 C  C   . LYS B 1 29  ? 9.332   -22.756 20.012  1.00 37.76  ? 29   LYS B C   1 
ATOM   2488 O  O   . LYS B 1 29  ? 8.373   -22.056 19.679  1.00 31.81  ? 29   LYS B O   1 
ATOM   2489 C  CB  . LYS B 1 29  ? 8.746   -23.792 22.250  1.00 38.86  ? 29   LYS B CB  1 
ATOM   2490 N  N   . VAL B 1 30  ? 10.096  -23.404 19.133  1.00 40.38  ? 30   VAL B N   1 
ATOM   2491 C  CA  . VAL B 1 30  ? 9.784   -23.457 17.696  1.00 41.59  ? 30   VAL B CA  1 
ATOM   2492 C  C   . VAL B 1 30  ? 9.934   -24.872 17.165  1.00 43.11  ? 30   VAL B C   1 
ATOM   2493 O  O   . VAL B 1 30  ? 10.980  -25.491 17.345  1.00 43.00  ? 30   VAL B O   1 
ATOM   2494 C  CB  . VAL B 1 30  ? 10.721  -22.579 16.844  1.00 38.73  ? 30   VAL B CB  1 
ATOM   2495 C  CG1 . VAL B 1 30  ? 10.304  -22.654 15.390  1.00 48.19  ? 30   VAL B CG1 1 
ATOM   2496 C  CG2 . VAL B 1 30  ? 10.711  -21.140 17.315  1.00 42.96  ? 30   VAL B CG2 1 
ATOM   2497 N  N   . VAL B 1 31  ? 8.895   -25.368 16.499  1.00 38.88  ? 31   VAL B N   1 
ATOM   2498 C  CA  . VAL B 1 31  ? 8.906   -26.695 15.893  1.00 49.89  ? 31   VAL B CA  1 
ATOM   2499 C  C   . VAL B 1 31  ? 9.225   -26.613 14.397  1.00 51.46  ? 31   VAL B C   1 
ATOM   2500 O  O   . VAL B 1 31  ? 8.425   -26.097 13.599  1.00 37.88  ? 31   VAL B O   1 
ATOM   2501 C  CB  . VAL B 1 31  ? 7.538   -27.383 16.047  1.00 64.37  ? 31   VAL B CB  1 
ATOM   2502 C  CG1 . VAL B 1 31  ? 7.563   -28.758 15.394  1.00 68.90  ? 31   VAL B CG1 1 
ATOM   2503 C  CG2 . VAL B 1 31  ? 7.138   -27.468 17.522  1.00 59.86  ? 31   VAL B CG2 1 
ATOM   2504 N  N   . THR B 1 32  ? 10.393  -27.132 14.026  1.00 56.97  ? 32   THR B N   1 
ATOM   2505 C  CA  . THR B 1 32  ? 10.880  -27.047 12.652  1.00 66.99  ? 32   THR B CA  1 
ATOM   2506 C  C   . THR B 1 32  ? 10.900  -28.404 11.945  1.00 72.86  ? 32   THR B C   1 
ATOM   2507 O  O   . THR B 1 32  ? 11.262  -29.421 12.530  1.00 71.01  ? 32   THR B O   1 
ATOM   2508 C  CB  . THR B 1 32  ? 12.291  -26.420 12.589  1.00 70.78  ? 32   THR B CB  1 
ATOM   2509 O  OG1 . THR B 1 32  ? 12.218  -25.031 12.946  1.00 69.05  ? 32   THR B OG1 1 
ATOM   2510 C  CG2 . THR B 1 32  ? 12.872  -26.543 11.187  1.00 74.89  ? 32   THR B CG2 1 
ATOM   2511 N  N   . LYS B 1 33  ? 10.493  -28.408 10.680  1.00 77.64  ? 33   LYS B N   1 
ATOM   2512 C  CA  . LYS B 1 33  ? 10.577  -29.598 9.848   1.00 73.61  ? 33   LYS B CA  1 
ATOM   2513 C  C   . LYS B 1 33  ? 11.062  -29.194 8.459   1.00 82.55  ? 33   LYS B C   1 
ATOM   2514 O  O   . LYS B 1 33  ? 10.517  -28.275 7.845   1.00 81.69  ? 33   LYS B O   1 
ATOM   2515 C  CB  . LYS B 1 33  ? 9.224   -30.297 9.768   1.00 62.27  ? 33   LYS B CB  1 
ATOM   2516 N  N   . LYS B 1 34  ? 12.105  -29.858 7.975   1.00 86.43  ? 34   LYS B N   1 
ATOM   2517 C  CA  . LYS B 1 34  ? 12.647  -29.531 6.661   1.00 87.35  ? 34   LYS B CA  1 
ATOM   2518 C  C   . LYS B 1 34  ? 12.501  -30.700 5.698   1.00 85.10  ? 34   LYS B C   1 
ATOM   2519 O  O   . LYS B 1 34  ? 13.001  -31.796 5.951   1.00 80.91  ? 34   LYS B O   1 
ATOM   2520 C  CB  . LYS B 1 34  ? 14.116  -29.116 6.755   1.00 80.69  ? 34   LYS B CB  1 
ATOM   2521 C  CG  . LYS B 1 34  ? 14.464  -27.914 5.900   1.00 74.06  ? 34   LYS B CG  1 
ATOM   2522 C  CD  . LYS B 1 34  ? 13.985  -26.627 6.570   1.00 71.59  ? 34   LYS B CD  1 
ATOM   2523 N  N   . PHE B 1 35  ? 11.805  -30.463 4.595   1.00 81.37  ? 35   PHE B N   1 
ATOM   2524 C  CA  . PHE B 1 35  ? 11.732  -31.455 3.541   1.00 81.66  ? 35   PHE B CA  1 
ATOM   2525 C  C   . PHE B 1 35  ? 13.068  -31.535 2.814   1.00 77.24  ? 35   PHE B C   1 
ATOM   2526 O  O   . PHE B 1 35  ? 14.046  -30.891 3.195   1.00 65.37  ? 35   PHE B O   1 
ATOM   2527 C  CB  . PHE B 1 35  ? 10.616  -31.115 2.555   1.00 92.00  ? 35   PHE B CB  1 
ATOM   2528 C  CG  . PHE B 1 35  ? 9.249   -31.094 3.170   1.00 103.29 ? 35   PHE B CG  1 
ATOM   2529 C  CD1 . PHE B 1 35  ? 8.584   -29.897 3.369   1.00 107.62 ? 35   PHE B CD1 1 
ATOM   2530 C  CD2 . PHE B 1 35  ? 8.631   -32.272 3.554   1.00 109.96 ? 35   PHE B CD2 1 
ATOM   2531 C  CE1 . PHE B 1 35  ? 7.321   -29.875 3.932   1.00 110.20 ? 35   PHE B CE1 1 
ATOM   2532 C  CE2 . PHE B 1 35  ? 7.369   -32.257 4.118   1.00 112.22 ? 35   PHE B CE2 1 
ATOM   2533 C  CZ  . PHE B 1 35  ? 6.714   -31.056 4.308   1.00 110.74 ? 35   PHE B CZ  1 
ATOM   2534 N  N   . SER B 1 36  ? 13.091  -32.329 1.752   1.00 89.38  ? 36   SER B N   1 
ATOM   2535 C  CA  . SER B 1 36  ? 14.289  -32.543 0.951   1.00 92.96  ? 36   SER B CA  1 
ATOM   2536 C  C   . SER B 1 36  ? 14.694  -31.286 0.193   1.00 86.57  ? 36   SER B C   1 
ATOM   2537 O  O   . SER B 1 36  ? 15.854  -30.871 0.218   1.00 88.53  ? 36   SER B O   1 
ATOM   2538 C  CB  . SER B 1 36  ? 13.989  -33.623 -0.063  1.00 94.22  ? 36   SER B CB  1 
ATOM   2539 O  OG  . SER B 1 36  ? 12.824  -33.251 -0.778  1.00 92.84  ? 36   SER B OG  1 
ATOM   2540 N  N   . ASN B 1 37  ? 13.727  -30.703 -0.505  1.00 76.94  ? 37   ASN B N   1 
ATOM   2541 C  CA  . ASN B 1 37  ? 13.946  -29.480 -1.262  1.00 72.12  ? 37   ASN B CA  1 
ATOM   2542 C  C   . ASN B 1 37  ? 14.339  -28.324 -0.357  1.00 64.74  ? 37   ASN B C   1 
ATOM   2543 O  O   . ASN B 1 37  ? 14.395  -27.179 -0.792  1.00 66.74  ? 37   ASN B O   1 
ATOM   2544 C  CB  . ASN B 1 37  ? 12.687  -29.120 -2.057  1.00 77.41  ? 37   ASN B CB  1 
ATOM   2545 C  CG  . ASN B 1 37  ? 11.403  -29.352 -1.264  1.00 80.53  ? 37   ASN B CG  1 
ATOM   2546 O  OD1 . ASN B 1 37  ? 11.433  -29.571 -0.049  1.00 75.34  ? 37   ASN B OD1 1 
ATOM   2547 N  ND2 . ASN B 1 37  ? 10.266  -29.299 -1.955  1.00 81.56  ? 37   ASN B ND2 1 
ATOM   2548 N  N   . GLN B 1 38  ? 14.613  -28.641 0.904   1.00 63.07  ? 38   GLN B N   1 
ATOM   2549 C  CA  . GLN B 1 38  ? 14.884  -27.635 1.919   1.00 65.07  ? 38   GLN B CA  1 
ATOM   2550 C  C   . GLN B 1 38  ? 13.693  -26.712 2.138   1.00 57.57  ? 38   GLN B C   1 
ATOM   2551 O  O   . GLN B 1 38  ? 13.851  -25.631 2.707   1.00 53.78  ? 38   GLN B O   1 
ATOM   2552 C  CB  . GLN B 1 38  ? 16.130  -26.816 1.572   1.00 75.70  ? 38   GLN B CB  1 
ATOM   2553 C  CG  . GLN B 1 38  ? 17.433  -27.455 2.020   1.00 85.07  ? 38   GLN B CG  1 
ATOM   2554 C  CD  . GLN B 1 38  ? 17.460  -27.725 3.514   1.00 89.00  ? 38   GLN B CD  1 
ATOM   2555 O  OE1 . GLN B 1 38  ? 17.466  -28.879 3.943   1.00 92.57  ? 38   GLN B OE1 1 
ATOM   2556 N  NE2 . GLN B 1 38  ? 17.474  -26.660 4.313   1.00 86.71  ? 38   GLN B NE2 1 
ATOM   2557 N  N   . GLU B 1 39  ? 12.510  -27.131 1.684   1.00 48.33  ? 39   GLU B N   1 
ATOM   2558 C  CA  . GLU B 1 39  ? 11.297  -26.366 1.949   1.00 45.12  ? 39   GLU B CA  1 
ATOM   2559 C  C   . GLU B 1 39  ? 11.104  -26.263 3.454   1.00 56.49  ? 39   GLU B C   1 
ATOM   2560 O  O   . GLU B 1 39  ? 10.919  -27.277 4.142   1.00 49.06  ? 39   GLU B O   1 
ATOM   2561 C  CB  . GLU B 1 39  ? 10.078  -27.023 1.315   1.00 40.12  ? 39   GLU B CB  1 
ATOM   2562 C  CG  . GLU B 1 39  ? 8.777   -26.277 1.571   1.00 39.08  ? 39   GLU B CG  1 
ATOM   2563 C  CD  . GLU B 1 39  ? 7.580   -26.905 0.860   1.00 59.83  ? 39   GLU B CD  1 
ATOM   2564 O  OE1 . GLU B 1 39  ? 6.497   -27.011 1.490   1.00 60.07  ? 39   GLU B OE1 1 
ATOM   2565 O  OE2 . GLU B 1 39  ? 7.719   -27.283 -0.326  1.00 65.31  ? 39   GLU B OE2 1 
ATOM   2566 N  N   . THR B 1 40  ? 11.157  -25.033 3.957   1.00 59.04  ? 40   THR B N   1 
ATOM   2567 C  CA  . THR B 1 40  ? 11.169  -24.780 5.392   1.00 62.75  ? 40   THR B CA  1 
ATOM   2568 C  C   . THR B 1 40  ? 9.782   -24.877 6.020   1.00 54.52  ? 40   THR B C   1 
ATOM   2569 O  O   . THR B 1 40  ? 8.827   -24.256 5.545   1.00 48.27  ? 40   THR B O   1 
ATOM   2570 C  CB  . THR B 1 40  ? 11.741  -23.379 5.704   1.00 66.51  ? 40   THR B CB  1 
ATOM   2571 O  OG1 . THR B 1 40  ? 13.004  -23.206 5.043   1.00 65.42  ? 40   THR B OG1 1 
ATOM   2572 C  CG2 . THR B 1 40  ? 11.911  -23.208 7.208   1.00 65.90  ? 40   THR B CG2 1 
ATOM   2573 N  N   . CYS B 1 41  ? 9.674   -25.661 7.087   1.00 53.44  ? 41   CYS B N   1 
ATOM   2574 C  CA  . CYS B 1 41  ? 8.449   -25.689 7.880   1.00 55.40  ? 41   CYS B CA  1 
ATOM   2575 C  C   . CYS B 1 41  ? 8.710   -25.094 9.256   1.00 56.80  ? 41   CYS B C   1 
ATOM   2576 O  O   . CYS B 1 41  ? 9.747   -25.343 9.868   1.00 53.31  ? 41   CYS B O   1 
ATOM   2577 C  CB  . CYS B 1 41  ? 7.898   -27.105 8.024   1.00 63.79  ? 41   CYS B CB  1 
ATOM   2578 S  SG  . CYS B 1 41  ? 7.355   -27.856 6.480   1.00 121.03 ? 41   CYS B SG  1 
ATOM   2579 N  N   . VAL B 1 42  ? 7.762   -24.295 9.725   1.00 58.18  ? 42   VAL B N   1 
ATOM   2580 C  CA  . VAL B 1 42  ? 7.842   -23.707 11.049  1.00 54.78  ? 42   VAL B CA  1 
ATOM   2581 C  C   . VAL B 1 42  ? 6.493   -23.808 11.742  1.00 56.03  ? 42   VAL B C   1 
ATOM   2582 O  O   . VAL B 1 42  ? 5.438   -23.798 11.096  1.00 58.20  ? 42   VAL B O   1 
ATOM   2583 C  CB  . VAL B 1 42  ? 8.326   -22.239 10.986  1.00 49.75  ? 42   VAL B CB  1 
ATOM   2584 C  CG1 . VAL B 1 42  ? 7.812   -21.442 12.156  1.00 37.52  ? 42   VAL B CG1 1 
ATOM   2585 C  CG2 . VAL B 1 42  ? 9.840   -22.195 10.939  1.00 54.13  ? 42   VAL B CG2 1 
ATOM   2586 N  N   . GLU B 1 43  ? 6.531   -23.964 13.057  1.00 42.14  ? 43   GLU B N   1 
ATOM   2587 C  CA  . GLU B 1 43  ? 5.338   -23.796 13.866  1.00 39.53  ? 43   GLU B CA  1 
ATOM   2588 C  C   . GLU B 1 43  ? 5.779   -23.215 15.207  1.00 46.41  ? 43   GLU B C   1 
ATOM   2589 O  O   . GLU B 1 43  ? 6.586   -23.820 15.907  1.00 41.09  ? 43   GLU B O   1 
ATOM   2590 C  CB  . GLU B 1 43  ? 4.601   -25.126 14.044  1.00 38.89  ? 43   GLU B CB  1 
ATOM   2591 N  N   . ILE B 1 44  ? 5.283   -22.026 15.538  1.00 50.57  ? 44   ILE B N   1 
ATOM   2592 C  CA  . ILE B 1 44  ? 5.602   -21.393 16.815  1.00 44.09  ? 44   ILE B CA  1 
ATOM   2593 C  C   . ILE B 1 44  ? 5.021   -22.241 17.936  1.00 40.15  ? 44   ILE B C   1 
ATOM   2594 O  O   . ILE B 1 44  ? 3.810   -22.466 17.980  1.00 42.87  ? 44   ILE B O   1 
ATOM   2595 C  CB  . ILE B 1 44  ? 5.014   -19.968 16.917  1.00 40.51  ? 44   ILE B CB  1 
ATOM   2596 C  CG1 . ILE B 1 44  ? 5.322   -19.164 15.654  1.00 39.40  ? 44   ILE B CG1 1 
ATOM   2597 C  CG2 . ILE B 1 44  ? 5.553   -19.256 18.167  1.00 29.14  ? 44   ILE B CG2 1 
ATOM   2598 C  CD1 . ILE B 1 44  ? 6.814   -19.021 15.368  1.00 37.14  ? 44   ILE B CD1 1 
ATOM   2599 N  N   . GLY B 1 45  ? 5.877   -22.696 18.849  1.00 33.35  ? 45   GLY B N   1 
ATOM   2600 C  CA  . GLY B 1 45  ? 5.470   -23.660 19.860  1.00 24.00  ? 45   GLY B CA  1 
ATOM   2601 C  C   . GLY B 1 45  ? 4.785   -23.093 21.085  1.00 34.31  ? 45   GLY B C   1 
ATOM   2602 O  O   . GLY B 1 45  ? 4.442   -23.838 22.001  1.00 41.12  ? 45   GLY B O   1 
ATOM   2603 N  N   . GLU B 1 46  ? 4.599   -21.779 21.124  1.00 32.52  ? 46   GLU B N   1 
ATOM   2604 C  CA  . GLU B 1 46  ? 3.872   -21.142 22.217  1.00 31.57  ? 46   GLU B CA  1 
ATOM   2605 C  C   . GLU B 1 46  ? 3.132   -19.928 21.687  1.00 36.65  ? 46   GLU B C   1 
ATOM   2606 O  O   . GLU B 1 46  ? 3.436   -19.427 20.609  1.00 29.92  ? 46   GLU B O   1 
ATOM   2607 C  CB  . GLU B 1 46  ? 4.828   -20.724 23.343  1.00 30.37  ? 46   GLU B CB  1 
ATOM   2608 C  CG  . GLU B 1 46  ? 5.938   -19.777 22.896  1.00 42.26  ? 46   GLU B CG  1 
ATOM   2609 C  CD  . GLU B 1 46  ? 7.059   -19.640 23.922  1.00 51.02  ? 46   GLU B CD  1 
ATOM   2610 O  OE1 . GLU B 1 46  ? 7.107   -18.599 24.610  1.00 57.64  ? 46   GLU B OE1 1 
ATOM   2611 O  OE2 . GLU B 1 46  ? 7.907   -20.561 24.032  1.00 43.36  ? 46   GLU B OE2 1 
ATOM   2612 N  N   . SER B 1 47  ? 2.156   -19.455 22.449  1.00 34.86  ? 47   SER B N   1 
ATOM   2613 C  CA  . SER B 1 47  ? 1.397   -18.287 22.061  1.00 24.19  ? 47   SER B CA  1 
ATOM   2614 C  C   . SER B 1 47  ? 2.303   -17.072 22.004  1.00 29.35  ? 47   SER B C   1 
ATOM   2615 O  O   . SER B 1 47  ? 3.201   -16.923 22.833  1.00 29.04  ? 47   SER B O   1 
ATOM   2616 C  CB  . SER B 1 47  ? 0.294   -18.025 23.075  1.00 26.53  ? 47   SER B CB  1 
ATOM   2617 O  OG  . SER B 1 47  ? -0.449  -16.874 22.717  1.00 24.98  ? 47   SER B OG  1 
ATOM   2618 N  N   . VAL B 1 48  ? 2.075   -16.203 21.028  1.00 29.07  ? 48   VAL B N   1 
ATOM   2619 C  CA  . VAL B 1 48  ? 2.759   -14.918 21.004  1.00 23.33  ? 48   VAL B CA  1 
ATOM   2620 C  C   . VAL B 1 48  ? 1.735   -13.800 20.928  1.00 21.56  ? 48   VAL B C   1 
ATOM   2621 O  O   . VAL B 1 48  ? 2.067   -12.633 20.686  1.00 24.25  ? 48   VAL B O   1 
ATOM   2622 C  CB  . VAL B 1 48  ? 3.742   -14.818 19.836  1.00 29.74  ? 48   VAL B CB  1 
ATOM   2623 C  CG1 . VAL B 1 48  ? 4.810   -15.909 19.958  1.00 32.65  ? 48   VAL B CG1 1 
ATOM   2624 C  CG2 . VAL B 1 48  ? 2.987   -14.879 18.488  1.00 17.39  ? 48   VAL B CG2 1 
ATOM   2625 N  N   . ARG B 1 49  ? 0.479   -14.171 21.152  1.00 24.99  ? 49   ARG B N   1 
ATOM   2626 C  CA  . ARG B 1 49  ? -0.617  -13.238 21.036  1.00 24.21  ? 49   ARG B CA  1 
ATOM   2627 C  C   . ARG B 1 49  ? -0.417  -12.061 21.985  1.00 36.30  ? 49   ARG B C   1 
ATOM   2628 O  O   . ARG B 1 49  ? -0.241  -12.255 23.173  1.00 27.32  ? 49   ARG B O   1 
ATOM   2629 C  CB  . ARG B 1 49  ? -1.927  -13.947 21.342  1.00 22.54  ? 49   ARG B CB  1 
ATOM   2630 C  CG  . ARG B 1 49  ? -3.129  -13.080 21.131  1.00 21.86  ? 49   ARG B CG  1 
ATOM   2631 C  CD  . ARG B 1 49  ? -4.386  -13.875 21.386  1.00 22.23  ? 49   ARG B CD  1 
ATOM   2632 N  NE  . ARG B 1 49  ? -4.482  -15.108 20.596  1.00 25.93  ? 49   ARG B NE  1 
ATOM   2633 C  CZ  . ARG B 1 49  ? -5.045  -15.168 19.386  1.00 33.18  ? 49   ARG B CZ  1 
ATOM   2634 N  NH1 . ARG B 1 49  ? -5.519  -14.079 18.822  1.00 22.68  ? 49   ARG B NH1 1 
ATOM   2635 N  NH2 . ARG B 1 49  ? -5.127  -16.310 18.733  1.00 29.70  ? 49   ARG B NH2 1 
ATOM   2636 N  N   . GLY B 1 50  ? -0.428  -10.844 21.456  1.00 34.48  ? 50   GLY B N   1 
ATOM   2637 C  CA  . GLY B 1 50  ? -0.316  -9.661  22.286  1.00 31.68  ? 50   GLY B CA  1 
ATOM   2638 C  C   . GLY B 1 50  ? 1.103   -9.312  22.680  1.00 39.26  ? 50   GLY B C   1 
ATOM   2639 O  O   . GLY B 1 50  ? 1.342   -8.350  23.399  1.00 35.00  ? 50   GLY B O   1 
ATOM   2640 N  N   . GLU B 1 51  ? 2.063   -10.077 22.194  1.00 38.34  ? 51   GLU B N   1 
ATOM   2641 C  CA  . GLU B 1 51  ? 3.425   -9.902  22.659  1.00 25.29  ? 51   GLU B CA  1 
ATOM   2642 C  C   . GLU B 1 51  ? 4.385   -9.245  21.678  1.00 30.50  ? 51   GLU B C   1 
ATOM   2643 O  O   . GLU B 1 51  ? 4.193   -9.301  20.465  1.00 24.80  ? 51   GLU B O   1 
ATOM   2644 C  CB  . GLU B 1 51  ? 3.962   -11.242 23.115  1.00 21.32  ? 51   GLU B CB  1 
ATOM   2645 C  CG  . GLU B 1 51  ? 3.546   -11.510 24.557  1.00 48.19  ? 51   GLU B CG  1 
ATOM   2646 C  CD  . GLU B 1 51  ? 3.701   -12.940 24.948  1.00 62.84  ? 51   GLU B CD  1 
ATOM   2647 O  OE1 . GLU B 1 51  ? 3.434   -13.263 26.124  1.00 66.45  ? 51   GLU B OE1 1 
ATOM   2648 O  OE2 . GLU B 1 51  ? 4.084   -13.742 24.071  1.00 73.77  ? 51   GLU B OE2 1 
ATOM   2649 N  N   . HIS B 1 52  ? 5.425   -8.623  22.220  1.00 23.41  ? 52   HIS B N   1 
ATOM   2650 C  CA  . HIS B 1 52  ? 6.500   -8.078  21.408  1.00 36.67  ? 52   HIS B CA  1 
ATOM   2651 C  C   . HIS B 1 52  ? 7.562   -9.151  21.185  1.00 39.69  ? 52   HIS B C   1 
ATOM   2652 O  O   . HIS B 1 52  ? 8.200   -9.648  22.126  1.00 27.25  ? 52   HIS B O   1 
ATOM   2653 C  CB  . HIS B 1 52  ? 7.065   -6.808  22.037  1.00 45.26  ? 52   HIS B CB  1 
ATOM   2654 C  CG  . HIS B 1 52  ? 6.046   -5.719  22.176  1.00 61.52  ? 52   HIS B CG  1 
ATOM   2655 N  ND1 . HIS B 1 52  ? 4.829   -5.916  22.796  1.00 69.13  ? 52   HIS B ND1 1 
ATOM   2656 C  CD2 . HIS B 1 52  ? 6.046   -4.433  21.753  1.00 67.12  ? 52   HIS B CD2 1 
ATOM   2657 C  CE1 . HIS B 1 52  ? 4.131   -4.795  22.760  1.00 67.47  ? 52   HIS B CE1 1 
ATOM   2658 N  NE2 . HIS B 1 52  ? 4.847   -3.880  22.131  1.00 67.77  ? 52   HIS B NE2 1 
ATOM   2659 N  N   . VAL B 1 53  ? 7.698   -9.537  19.920  1.00 33.74  ? 53   VAL B N   1 
ATOM   2660 C  CA  . VAL B 1 53  ? 8.520   -10.675 19.526  1.00 21.43  ? 53   VAL B CA  1 
ATOM   2661 C  C   . VAL B 1 53  ? 9.800   -10.200 18.850  1.00 31.87  ? 53   VAL B C   1 
ATOM   2662 O  O   . VAL B 1 53  ? 9.789   -9.246  18.059  1.00 28.48  ? 53   VAL B O   1 
ATOM   2663 C  CB  . VAL B 1 53  ? 7.725   -11.576 18.565  1.00 23.52  ? 53   VAL B CB  1 
ATOM   2664 C  CG1 . VAL B 1 53  ? 8.622   -12.636 17.920  1.00 23.47  ? 53   VAL B CG1 1 
ATOM   2665 C  CG2 . VAL B 1 53  ? 6.546   -12.198 19.308  1.00 32.63  ? 53   VAL B CG2 1 
ATOM   2666 N  N   . TYR B 1 54  ? 10.905  -10.860 19.171  1.00 23.44  ? 54   TYR B N   1 
ATOM   2667 C  CA  . TYR B 1 54  ? 12.165  -10.594 18.505  1.00 20.22  ? 54   TYR B CA  1 
ATOM   2668 C  C   . TYR B 1 54  ? 12.589  -11.916 17.900  1.00 28.14  ? 54   TYR B C   1 
ATOM   2669 O  O   . TYR B 1 54  ? 12.533  -12.949 18.561  1.00 25.79  ? 54   TYR B O   1 
ATOM   2670 C  CB  . TYR B 1 54  ? 13.221  -10.072 19.496  1.00 23.17  ? 54   TYR B CB  1 
ATOM   2671 C  CG  . TYR B 1 54  ? 12.938  -8.676  20.003  1.00 21.17  ? 54   TYR B CG  1 
ATOM   2672 C  CD1 . TYR B 1 54  ? 11.916  -8.442  20.911  1.00 28.20  ? 54   TYR B CD1 1 
ATOM   2673 C  CD2 . TYR B 1 54  ? 13.674  -7.586  19.554  1.00 16.49  ? 54   TYR B CD2 1 
ATOM   2674 C  CE1 . TYR B 1 54  ? 11.636  -7.163  21.368  1.00 24.22  ? 54   TYR B CE1 1 
ATOM   2675 C  CE2 . TYR B 1 54  ? 13.403  -6.300  20.006  1.00 23.92  ? 54   TYR B CE2 1 
ATOM   2676 C  CZ  . TYR B 1 54  ? 12.379  -6.095  20.916  1.00 33.03  ? 54   TYR B CZ  1 
ATOM   2677 O  OH  . TYR B 1 54  ? 12.100  -4.827  21.384  1.00 37.64  ? 54   TYR B OH  1 
ATOM   2678 N  N   . ILE B 1 55  ? 12.948  -11.894 16.622  1.00 30.48  ? 55   ILE B N   1 
ATOM   2679 C  CA  . ILE B 1 55  ? 13.432  -13.093 15.969  1.00 25.86  ? 55   ILE B CA  1 
ATOM   2680 C  C   . ILE B 1 55  ? 14.838  -12.829 15.475  1.00 27.38  ? 55   ILE B C   1 
ATOM   2681 O  O   . ILE B 1 55  ? 15.076  -11.882 14.721  1.00 25.17  ? 55   ILE B O   1 
ATOM   2682 C  CB  . ILE B 1 55  ? 12.539  -13.514 14.783  1.00 29.39  ? 55   ILE B CB  1 
ATOM   2683 C  CG1 . ILE B 1 55  ? 11.138  -13.892 15.275  1.00 23.34  ? 55   ILE B CG1 1 
ATOM   2684 C  CG2 . ILE B 1 55  ? 13.186  -14.689 14.023  1.00 19.49  ? 55   ILE B CG2 1 
ATOM   2685 C  CD1 . ILE B 1 55  ? 10.080  -13.872 14.178  1.00 29.86  ? 55   ILE B CD1 1 
ATOM   2686 N  N   . VAL B 1 56  ? 15.763  -13.676 15.908  1.00 27.68  ? 56   VAL B N   1 
ATOM   2687 C  CA  . VAL B 1 56  ? 17.171  -13.488 15.610  1.00 30.19  ? 56   VAL B CA  1 
ATOM   2688 C  C   . VAL B 1 56  ? 17.521  -14.443 14.491  1.00 35.97  ? 56   VAL B C   1 
ATOM   2689 O  O   . VAL B 1 56  ? 17.364  -15.649 14.639  1.00 30.98  ? 56   VAL B O   1 
ATOM   2690 C  CB  . VAL B 1 56  ? 18.046  -13.767 16.850  1.00 27.09  ? 56   VAL B CB  1 
ATOM   2691 C  CG1 . VAL B 1 56  ? 19.510  -13.498 16.544  1.00 34.66  ? 56   VAL B CG1 1 
ATOM   2692 C  CG2 . VAL B 1 56  ? 17.582  -12.901 18.019  1.00 22.18  ? 56   VAL B CG2 1 
ATOM   2693 N  N   . GLN B 1 57  ? 17.968  -13.900 13.364  1.00 38.00  ? 57   GLN B N   1 
ATOM   2694 C  CA  . GLN B 1 57  ? 18.244  -14.719 12.189  1.00 42.87  ? 57   GLN B CA  1 
ATOM   2695 C  C   . GLN B 1 57  ? 19.395  -15.670 12.462  1.00 45.27  ? 57   GLN B C   1 
ATOM   2696 O  O   . GLN B 1 57  ? 20.343  -15.310 13.161  1.00 44.90  ? 57   GLN B O   1 
ATOM   2697 C  CB  . GLN B 1 57  ? 18.587  -13.833 10.989  1.00 47.94  ? 57   GLN B CB  1 
ATOM   2698 C  CG  . GLN B 1 57  ? 18.767  -14.606 9.691   1.00 58.73  ? 57   GLN B CG  1 
ATOM   2699 C  CD  . GLN B 1 57  ? 19.290  -13.732 8.555   1.00 70.45  ? 57   GLN B CD  1 
ATOM   2700 O  OE1 . GLN B 1 57  ? 20.291  -13.017 8.708   1.00 76.89  ? 57   GLN B OE1 1 
ATOM   2701 N  NE2 . GLN B 1 57  ? 18.611  -13.784 7.409   1.00 60.87  ? 57   GLN B NE2 1 
ATOM   2702 N  N   . SER B 1 58  ? 19.318  -16.876 11.903  1.00 52.55  ? 58   SER B N   1 
ATOM   2703 C  CA  . SER B 1 58  ? 20.371  -17.882 12.090  1.00 67.39  ? 58   SER B CA  1 
ATOM   2704 C  C   . SER B 1 58  ? 21.686  -17.575 11.397  1.00 67.81  ? 58   SER B C   1 
ATOM   2705 O  O   . SER B 1 58  ? 21.765  -16.724 10.513  1.00 74.65  ? 58   SER B O   1 
ATOM   2706 C  CB  . SER B 1 58  ? 19.903  -19.247 11.599  1.00 70.34  ? 58   SER B CB  1 
ATOM   2707 O  OG  . SER B 1 58  ? 19.011  -19.812 12.526  1.00 75.65  ? 58   SER B OG  1 
ATOM   2708 N  N   . GLY B 1 59  ? 22.721  -18.290 11.817  1.00 62.05  ? 59   GLY B N   1 
ATOM   2709 C  CA  . GLY B 1 59  ? 23.983  -18.289 11.105  1.00 67.80  ? 59   GLY B CA  1 
ATOM   2710 C  C   . GLY B 1 59  ? 24.238  -19.682 10.573  1.00 74.49  ? 59   GLY B C   1 
ATOM   2711 O  O   . GLY B 1 59  ? 25.377  -20.152 10.568  1.00 79.91  ? 59   GLY B O   1 
ATOM   2712 N  N   . CYS B 1 60  ? 23.169  -20.342 10.131  0.60 77.25  ? 60   CYS B N   1 
ATOM   2713 C  CA  . CYS B 1 60  ? 23.228  -21.732 9.681   0.60 76.83  ? 60   CYS B CA  1 
ATOM   2714 C  C   . CYS B 1 60  ? 24.047  -21.915 8.406   0.60 78.20  ? 60   CYS B C   1 
ATOM   2715 O  O   . CYS B 1 60  ? 24.478  -23.026 8.095   0.60 81.67  ? 60   CYS B O   1 
ATOM   2716 C  CB  . CYS B 1 60  ? 21.819  -22.287 9.476   0.60 78.17  ? 60   CYS B CB  1 
ATOM   2717 S  SG  . CYS B 1 60  ? 21.416  -22.623 7.746   0.60 103.73 ? 60   CYS B SG  1 
ATOM   2718 N  N   . GLY B 1 61  ? 24.255  -20.828 7.669   0.80 76.92  ? 61   GLY B N   1 
ATOM   2719 C  CA  . GLY B 1 61  ? 25.128  -20.855 6.507   0.80 74.38  ? 61   GLY B CA  1 
ATOM   2720 C  C   . GLY B 1 61  ? 24.434  -20.552 5.195   0.80 68.24  ? 61   GLY B C   1 
ATOM   2721 O  O   . GLY B 1 61  ? 24.730  -19.551 4.533   0.80 68.06  ? 61   GLY B O   1 
ATOM   2722 N  N   . GLU B 1 62  ? 23.509  -21.425 4.812   0.86 52.70  ? 62   GLU B N   1 
ATOM   2723 C  CA  . GLU B 1 62  ? 22.784  -21.251 3.564   0.86 38.40  ? 62   GLU B CA  1 
ATOM   2724 C  C   . GLU B 1 62  ? 21.911  -20.009 3.648   0.86 28.39  ? 62   GLU B C   1 
ATOM   2725 O  O   . GLU B 1 62  ? 20.822  -20.035 4.223   0.86 31.87  ? 62   GLU B O   1 
ATOM   2726 C  CB  . GLU B 1 62  ? 21.928  -22.477 3.260   0.86 40.82  ? 62   GLU B CB  1 
ATOM   2727 C  CG  . GLU B 1 62  ? 22.001  -22.942 1.813   0.86 40.72  ? 62   GLU B CG  1 
ATOM   2728 C  CD  . GLU B 1 62  ? 21.181  -22.085 0.855   0.86 43.03  ? 62   GLU B CD  1 
ATOM   2729 O  OE1 . GLU B 1 62  ? 20.716  -20.989 1.242   0.86 36.89  ? 62   GLU B OE1 1 
ATOM   2730 O  OE2 . GLU B 1 62  ? 21.001  -22.522 -0.301  0.86 42.06  ? 62   GLU B OE2 1 
ATOM   2731 N  N   . ILE B 1 63  ? 22.395  -18.926 3.052   1.00 31.50  ? 63   ILE B N   1 
ATOM   2732 C  CA  . ILE B 1 63  ? 21.749  -17.625 3.148   1.00 35.86  ? 63   ILE B CA  1 
ATOM   2733 C  C   . ILE B 1 63  ? 20.275  -17.594 2.687   1.00 40.09  ? 63   ILE B C   1 
ATOM   2734 O  O   . ILE B 1 63  ? 19.435  -16.942 3.322   1.00 40.86  ? 63   ILE B O   1 
ATOM   2735 C  CB  . ILE B 1 63  ? 22.557  -16.576 2.384   1.00 42.38  ? 63   ILE B CB  1 
ATOM   2736 C  CG1 . ILE B 1 63  ? 22.119  -15.175 2.769   1.00 46.48  ? 63   ILE B CG1 1 
ATOM   2737 C  CG2 . ILE B 1 63  ? 22.410  -16.768 0.883   1.00 47.94  ? 63   ILE B CG2 1 
ATOM   2738 C  CD1 . ILE B 1 63  ? 22.620  -14.130 1.797   1.00 58.12  ? 63   ILE B CD1 1 
ATOM   2739 N  N   . ASN B 1 64  ? 19.941  -18.287 1.599   1.00 29.70  ? 64   ASN B N   1 
ATOM   2740 C  CA  . ASN B 1 64  ? 18.553  -18.259 1.147   1.00 27.10  ? 64   ASN B CA  1 
ATOM   2741 C  C   . ASN B 1 64  ? 17.630  -19.063 2.068   1.00 27.08  ? 64   ASN B C   1 
ATOM   2742 O  O   . ASN B 1 64  ? 16.457  -18.716 2.263   1.00 30.62  ? 64   ASN B O   1 
ATOM   2743 C  CB  . ASN B 1 64  ? 18.423  -18.728 -0.311  1.00 26.81  ? 64   ASN B CB  1 
ATOM   2744 C  CG  . ASN B 1 64  ? 19.177  -17.834 -1.279  1.00 24.22  ? 64   ASN B CG  1 
ATOM   2745 O  OD1 . ASN B 1 64  ? 19.838  -18.318 -2.195  1.00 36.98  ? 64   ASN B OD1 1 
ATOM   2746 N  ND2 . ASN B 1 64  ? 19.088  -16.530 -1.076  1.00 22.00  ? 64   ASN B ND2 1 
ATOM   2747 N  N   . ASP B 1 65  ? 18.162  -20.149 2.612   1.00 20.48  ? 65   ASP B N   1 
ATOM   2748 C  CA  . ASP B 1 65  ? 17.452  -20.914 3.633   1.00 35.81  ? 65   ASP B CA  1 
ATOM   2749 C  C   . ASP B 1 65  ? 17.211  -20.071 4.891   1.00 27.11  ? 65   ASP B C   1 
ATOM   2750 O  O   . ASP B 1 65  ? 16.099  -20.050 5.427   1.00 31.01  ? 65   ASP B O   1 
ATOM   2751 C  CB  . ASP B 1 65  ? 18.217  -22.194 3.992   1.00 33.69  ? 65   ASP B CB  1 
ATOM   2752 C  CG  . ASP B 1 65  ? 18.241  -23.206 2.847   1.00 40.35  ? 65   ASP B CG  1 
ATOM   2753 O  OD1 . ASP B 1 65  ? 17.359  -23.135 1.955   1.00 32.51  ? 65   ASP B OD1 1 
ATOM   2754 O  OD2 . ASP B 1 65  ? 19.138  -24.086 2.855   1.00 37.43  ? 65   ASP B OD2 1 
ATOM   2755 N  N   . ASN B 1 66  ? 18.245  -19.362 5.344   1.00 24.65  ? 66   ASN B N   1 
ATOM   2756 C  CA  . ASN B 1 66  ? 18.132  -18.566 6.565   1.00 32.74  ? 66   ASN B CA  1 
ATOM   2757 C  C   . ASN B 1 66  ? 17.139  -17.447 6.368   1.00 31.42  ? 66   ASN B C   1 
ATOM   2758 O  O   . ASN B 1 66  ? 16.343  -17.142 7.261   1.00 34.34  ? 66   ASN B O   1 
ATOM   2759 C  CB  . ASN B 1 66  ? 19.479  -17.974 6.975   1.00 35.81  ? 66   ASN B CB  1 
ATOM   2760 C  CG  . ASN B 1 66  ? 20.441  -19.016 7.480   1.00 47.17  ? 66   ASN B CG  1 
ATOM   2761 O  OD1 . ASN B 1 66  ? 20.033  -20.038 8.038   1.00 44.68  ? 66   ASN B OD1 1 
ATOM   2762 N  ND2 . ASN B 1 66  ? 21.737  -18.765 7.289   1.00 50.35  ? 66   ASN B ND2 1 
ATOM   2763 N  N   . LEU B 1 67  ? 17.177  -16.844 5.184   1.00 23.59  ? 67   LEU B N   1 
ATOM   2764 C  CA  . LEU B 1 67  ? 16.302  -15.726 4.900   1.00 23.75  ? 67   LEU B CA  1 
ATOM   2765 C  C   . LEU B 1 67  ? 14.854  -16.177 4.875   1.00 30.72  ? 67   LEU B C   1 
ATOM   2766 O  O   . LEU B 1 67  ? 13.997  -15.548 5.489   1.00 29.67  ? 67   LEU B O   1 
ATOM   2767 C  CB  . LEU B 1 67  ? 16.662  -15.067 3.576   1.00 23.04  ? 67   LEU B CB  1 
ATOM   2768 C  CG  . LEU B 1 67  ? 15.751  -13.916 3.141   1.00 27.03  ? 67   LEU B CG  1 
ATOM   2769 C  CD1 . LEU B 1 67  ? 15.758  -12.797 4.169   1.00 26.34  ? 67   LEU B CD1 1 
ATOM   2770 C  CD2 . LEU B 1 67  ? 16.207  -13.382 1.809   1.00 36.74  ? 67   LEU B CD2 1 
ATOM   2771 N  N   . MET B 1 68  ? 14.575  -17.273 4.175   1.00 23.93  ? 68   MET B N   1 
ATOM   2772 C  CA  . MET B 1 68  ? 13.206  -17.698 4.048   1.00 27.24  ? 68   MET B CA  1 
ATOM   2773 C  C   . MET B 1 68  ? 12.690  -18.088 5.420   1.00 22.59  ? 68   MET B C   1 
ATOM   2774 O  O   . MET B 1 68  ? 11.544  -17.800 5.776   1.00 22.07  ? 68   MET B O   1 
ATOM   2775 C  CB  . MET B 1 68  ? 13.083  -18.873 3.075   1.00 26.39  ? 68   MET B CB  1 
ATOM   2776 C  CG  . MET B 1 68  ? 13.187  -18.465 1.615   1.00 49.71  ? 68   MET B CG  1 
ATOM   2777 S  SD  . MET B 1 68  ? 11.921  -17.259 1.188   1.00 58.76  ? 68   MET B SD  1 
ATOM   2778 C  CE  . MET B 1 68  ? 10.476  -18.072 1.913   1.00 17.30  ? 68   MET B CE  1 
ATOM   2779 N  N   . GLU B 1 69  ? 13.540  -18.746 6.190   1.00 21.89  ? 69   GLU B N   1 
ATOM   2780 C  CA  . GLU B 1 69  ? 13.134  -19.216 7.510   1.00 28.91  ? 69   GLU B CA  1 
ATOM   2781 C  C   . GLU B 1 69  ? 12.706  -18.050 8.380   1.00 28.40  ? 69   GLU B C   1 
ATOM   2782 O  O   . GLU B 1 69  ? 11.658  -18.089 9.040   1.00 30.50  ? 69   GLU B O   1 
ATOM   2783 C  CB  . GLU B 1 69  ? 14.282  -19.955 8.178   1.00 20.20  ? 69   GLU B CB  1 
ATOM   2784 C  CG  . GLU B 1 69  ? 13.879  -20.678 9.456   1.00 42.85  ? 69   GLU B CG  1 
ATOM   2785 C  CD  . GLU B 1 69  ? 15.043  -21.453 10.068  1.00 63.87  ? 69   GLU B CD  1 
ATOM   2786 O  OE1 . GLU B 1 69  ? 16.212  -21.036 9.878   1.00 57.19  ? 69   GLU B OE1 1 
ATOM   2787 O  OE2 . GLU B 1 69  ? 14.782  -22.480 10.735  1.00 74.44  ? 69   GLU B OE2 1 
ATOM   2788 N  N   . LEU B 1 70  ? 13.540  -17.019 8.387   1.00 24.48  ? 70   LEU B N   1 
ATOM   2789 C  CA  . LEU B 1 70  ? 13.245  -15.782 9.090   1.00 24.81  ? 70   LEU B CA  1 
ATOM   2790 C  C   . LEU B 1 70  ? 11.931  -15.191 8.613   1.00 30.15  ? 70   LEU B C   1 
ATOM   2791 O  O   . LEU B 1 70  ? 11.097  -14.794 9.423   1.00 21.94  ? 70   LEU B O   1 
ATOM   2792 C  CB  . LEU B 1 70  ? 14.372  -14.798 8.826   1.00 13.00  ? 70   LEU B CB  1 
ATOM   2793 C  CG  . LEU B 1 70  ? 14.342  -13.359 9.322   1.00 27.60  ? 70   LEU B CG  1 
ATOM   2794 C  CD1 . LEU B 1 70  ? 14.180  -13.267 10.846  1.00 22.56  ? 70   LEU B CD1 1 
ATOM   2795 C  CD2 . LEU B 1 70  ? 15.631  -12.698 8.875   1.00 24.45  ? 70   LEU B CD2 1 
ATOM   2796 N  N   . LEU B 1 71  ? 11.745  -15.127 7.292   1.00 27.08  ? 71   LEU B N   1 
ATOM   2797 C  CA  . LEU B 1 71  ? 10.558  -14.491 6.746   1.00 23.72  ? 71   LEU B CA  1 
ATOM   2798 C  C   . LEU B 1 71  ? 9.340   -15.261 7.193   1.00 21.36  ? 71   LEU B C   1 
ATOM   2799 O  O   . LEU B 1 71  ? 8.306   -14.677 7.515   1.00 20.17  ? 71   LEU B O   1 
ATOM   2800 C  CB  . LEU B 1 71  ? 10.606  -14.444 5.221   1.00 17.67  ? 71   LEU B CB  1 
ATOM   2801 C  CG  . LEU B 1 71  ? 11.668  -13.540 4.600   1.00 21.69  ? 71   LEU B CG  1 
ATOM   2802 C  CD1 . LEU B 1 71  ? 11.715  -13.765 3.057   1.00 22.64  ? 71   LEU B CD1 1 
ATOM   2803 C  CD2 . LEU B 1 71  ? 11.410  -12.083 4.944   1.00 17.42  ? 71   LEU B CD2 1 
ATOM   2804 N  N   . ILE B 1 72  ? 9.478   -16.585 7.213   1.00 18.24  ? 72   ILE B N   1 
ATOM   2805 C  CA  . ILE B 1 72  ? 8.377   -17.480 7.554   1.00 26.15  ? 72   ILE B CA  1 
ATOM   2806 C  C   . ILE B 1 72  ? 7.991   -17.349 9.041   1.00 31.15  ? 72   ILE B C   1 
ATOM   2807 O  O   . ILE B 1 72  ? 6.802   -17.286 9.387   1.00 23.63  ? 72   ILE B O   1 
ATOM   2808 C  CB  . ILE B 1 72  ? 8.726   -18.941 7.162   1.00 26.03  ? 72   ILE B CB  1 
ATOM   2809 C  CG1 . ILE B 1 72  ? 8.598   -19.136 5.650   1.00 28.93  ? 72   ILE B CG1 1 
ATOM   2810 C  CG2 . ILE B 1 72  ? 7.823   -19.936 7.850   1.00 18.57  ? 72   ILE B CG2 1 
ATOM   2811 C  CD1 . ILE B 1 72  ? 9.271   -20.398 5.141   1.00 24.89  ? 72   ILE B CD1 1 
ATOM   2812 N  N   . MET B 1 73  ? 8.992   -17.275 9.912   1.00 20.02  ? 73   MET B N   1 
ATOM   2813 C  CA  . MET B 1 73  ? 8.728   -17.063 11.333  1.00 27.61  ? 73   MET B CA  1 
ATOM   2814 C  C   . MET B 1 73  ? 8.101   -15.700 11.620  1.00 22.39  ? 73   MET B C   1 
ATOM   2815 O  O   . MET B 1 73  ? 7.224   -15.580 12.474  1.00 27.89  ? 73   MET B O   1 
ATOM   2816 C  CB  . MET B 1 73  ? 10.004  -17.209 12.149  1.00 26.22  ? 73   MET B CB  1 
ATOM   2817 C  CG  . MET B 1 73  ? 10.406  -18.646 12.383  1.00 38.27  ? 73   MET B CG  1 
ATOM   2818 S  SD  . MET B 1 73  ? 12.008  -18.746 13.192  1.00 47.21  ? 73   MET B SD  1 
ATOM   2819 C  CE  . MET B 1 73  ? 12.977  -17.703 12.109  1.00 224.93 ? 73   MET B CE  1 
ATOM   2820 N  N   . ILE B 1 74  ? 8.572   -14.666 10.926  1.00 25.42  ? 74   ILE B N   1 
ATOM   2821 C  CA  . ILE B 1 74  ? 7.952   -13.353 11.032  1.00 27.48  ? 74   ILE B CA  1 
ATOM   2822 C  C   . ILE B 1 74  ? 6.480   -13.475 10.656  1.00 24.59  ? 74   ILE B C   1 
ATOM   2823 O  O   . ILE B 1 74  ? 5.599   -13.044 11.387  1.00 25.05  ? 74   ILE B O   1 
ATOM   2824 C  CB  . ILE B 1 74  ? 8.682   -12.302 10.165  1.00 31.04  ? 74   ILE B CB  1 
ATOM   2825 C  CG1 . ILE B 1 74  ? 10.051  -12.015 10.776  1.00 27.59  ? 74   ILE B CG1 1 
ATOM   2826 C  CG2 . ILE B 1 74  ? 7.866   -11.000 10.055  1.00 26.77  ? 74   ILE B CG2 1 
ATOM   2827 C  CD1 . ILE B 1 74  ? 10.961  -11.181 9.895   1.00 28.44  ? 74   ILE B CD1 1 
ATOM   2828 N  N   . ASN B 1 75  ? 6.215   -14.118 9.530   1.00 23.21  ? 75   ASN B N   1 
ATOM   2829 C  CA  . ASN B 1 75  ? 4.847   -14.281 9.082   1.00 20.71  ? 75   ASN B CA  1 
ATOM   2830 C  C   . ASN B 1 75  ? 3.997   -15.068 10.082  1.00 21.01  ? 75   ASN B C   1 
ATOM   2831 O  O   . ASN B 1 75  ? 2.878   -14.696 10.400  1.00 24.47  ? 75   ASN B O   1 
ATOM   2832 C  CB  . ASN B 1 75  ? 4.827   -14.969 7.716   1.00 28.72  ? 75   ASN B CB  1 
ATOM   2833 C  CG  . ASN B 1 75  ? 3.430   -15.231 7.231   1.00 32.98  ? 75   ASN B CG  1 
ATOM   2834 O  OD1 . ASN B 1 75  ? 2.713   -14.303 6.873   1.00 37.28  ? 75   ASN B OD1 1 
ATOM   2835 N  ND2 . ASN B 1 75  ? 3.020   -16.498 7.239   1.00 42.77  ? 75   ASN B ND2 1 
ATOM   2836 N  N   . ALA B 1 76  ? 4.533   -16.179 10.556  1.00 27.64  ? 76   ALA B N   1 
ATOM   2837 C  CA  . ALA B 1 76  ? 3.821   -17.005 11.509  1.00 26.08  ? 76   ALA B CA  1 
ATOM   2838 C  C   . ALA B 1 76  ? 3.489   -16.198 12.769  1.00 18.65  ? 76   ALA B C   1 
ATOM   2839 O  O   . ALA B 1 76  ? 2.363   -16.245 13.249  1.00 27.79  ? 76   ALA B O   1 
ATOM   2840 C  CB  . ALA B 1 76  ? 4.642   -18.226 11.849  1.00 24.47  ? 76   ALA B CB  1 
ATOM   2841 N  N   . CYS B 1 77  ? 4.446   -15.433 13.275  1.00 24.30  ? 77   CYS B N   1 
ATOM   2842 C  CA  . CYS B 1 77  ? 4.196   -14.609 14.467  1.00 39.49  ? 77   CYS B CA  1 
ATOM   2843 C  C   . CYS B 1 77  ? 3.127   -13.544 14.252  1.00 32.34  ? 77   CYS B C   1 
ATOM   2844 O  O   . CYS B 1 77  ? 2.258   -13.359 15.099  1.00 25.70  ? 77   CYS B O   1 
ATOM   2845 C  CB  . CYS B 1 77  ? 5.486   -13.979 15.008  1.00 28.07  ? 77   CYS B CB  1 
ATOM   2846 S  SG  . CYS B 1 77  ? 6.557   -15.195 15.734  1.00 31.51  ? 77   CYS B SG  1 
ATOM   2847 N  N   . LYS B 1 78  ? 3.192   -12.857 13.118  1.00 20.36  ? 78   LYS B N   1 
ATOM   2848 C  CA  . LYS B 1 78  ? 2.185   -11.852 12.769  1.00 19.61  ? 78   LYS B CA  1 
ATOM   2849 C  C   . LYS B 1 78  ? 0.760   -12.372 12.652  1.00 28.06  ? 78   LYS B C   1 
ATOM   2850 O  O   . LYS B 1 78  ? -0.181  -11.760 13.163  1.00 29.59  ? 78   LYS B O   1 
ATOM   2851 C  CB  . LYS B 1 78  ? 2.561   -11.120 11.478  1.00 22.79  ? 78   LYS B CB  1 
ATOM   2852 C  CG  . LYS B 1 78  ? 3.525   -9.975  11.718  1.00 34.78  ? 78   LYS B CG  1 
ATOM   2853 C  CD  . LYS B 1 78  ? 2.774   -8.794  12.303  1.00 50.79  ? 78   LYS B CD  1 
ATOM   2854 C  CE  . LYS B 1 78  ? 3.701   -7.731  12.847  1.00 53.14  ? 78   LYS B CE  1 
ATOM   2855 N  NZ  . LYS B 1 78  ? 3.240   -6.369  12.465  1.00 51.94  ? 78   LYS B NZ  1 
ATOM   2856 N  N   . ILE B 1 79  ? 0.574   -13.497 11.986  1.00 27.06  ? 79   ILE B N   1 
ATOM   2857 C  CA  . ILE B 1 79  ? -0.790  -13.974 11.830  1.00 26.57  ? 79   ILE B CA  1 
ATOM   2858 C  C   . ILE B 1 79  ? -1.225  -14.739 13.085  1.00 26.71  ? 79   ILE B C   1 
ATOM   2859 O  O   . ILE B 1 79  ? -2.385  -15.136 13.211  1.00 29.34  ? 79   ILE B O   1 
ATOM   2860 C  CB  . ILE B 1 79  ? -0.976  -14.784 10.531  1.00 34.48  ? 79   ILE B CB  1 
ATOM   2861 C  CG1 . ILE B 1 79  ? -0.285  -16.133 10.636  1.00 40.66  ? 79   ILE B CG1 1 
ATOM   2862 C  CG2 . ILE B 1 79  ? -0.428  -14.000 9.314   1.00 21.98  ? 79   ILE B CG2 1 
ATOM   2863 C  CD1 . ILE B 1 79  ? -0.195  -16.824 9.297   1.00 44.76  ? 79   ILE B CD1 1 
ATOM   2864 N  N   . ALA B 1 80  ? -0.285  -14.935 14.012  1.00 21.80  ? 80   ALA B N   1 
ATOM   2865 C  CA  . ALA B 1 80  ? -0.622  -15.424 15.352  1.00 28.70  ? 80   ALA B CA  1 
ATOM   2866 C  C   . ALA B 1 80  ? -0.856  -14.262 16.327  1.00 32.65  ? 80   ALA B C   1 
ATOM   2867 O  O   . ALA B 1 80  ? -0.836  -14.452 17.548  1.00 32.02  ? 80   ALA B O   1 
ATOM   2868 C  CB  . ALA B 1 80  ? 0.455   -16.356 15.875  1.00 14.82  ? 80   ALA B CB  1 
ATOM   2869 N  N   . SER B 1 81  ? -1.076  -13.064 15.780  1.00 21.09  ? 81   SER B N   1 
ATOM   2870 C  CA  . SER B 1 81  ? -1.465  -11.887 16.564  1.00 27.49  ? 81   SER B CA  1 
ATOM   2871 C  C   . SER B 1 81  ? -0.377  -11.344 17.498  1.00 32.84  ? 81   SER B C   1 
ATOM   2872 O  O   . SER B 1 81  ? -0.682  -10.727 18.527  1.00 36.63  ? 81   SER B O   1 
ATOM   2873 C  CB  . SER B 1 81  ? -2.745  -12.144 17.366  1.00 27.96  ? 81   SER B CB  1 
ATOM   2874 O  OG  . SER B 1 81  ? -3.891  -12.106 16.534  1.00 31.74  ? 81   SER B OG  1 
ATOM   2875 N  N   . ALA B 1 82  ? 0.884   -11.562 17.150  1.00 27.87  ? 82   ALA B N   1 
ATOM   2876 C  CA  . ALA B 1 82  ? 1.934   -10.871 17.866  1.00 26.72  ? 82   ALA B CA  1 
ATOM   2877 C  C   . ALA B 1 82  ? 1.638   -9.387  17.717  1.00 32.99  ? 82   ALA B C   1 
ATOM   2878 O  O   . ALA B 1 82  ? 1.353   -8.900  16.624  1.00 31.83  ? 82   ALA B O   1 
ATOM   2879 C  CB  . ALA B 1 82  ? 3.305   -11.210 17.313  1.00 20.14  ? 82   ALA B CB  1 
ATOM   2880 N  N   . SER B 1 83  ? 1.681   -8.673  18.827  1.00 29.31  ? 83   SER B N   1 
ATOM   2881 C  CA  . SER B 1 83  ? 1.511   -7.229  18.816  1.00 31.07  ? 83   SER B CA  1 
ATOM   2882 C  C   . SER B 1 83  ? 2.604   -6.520  18.032  1.00 29.70  ? 83   SER B C   1 
ATOM   2883 O  O   . SER B 1 83  ? 2.363   -5.474  17.427  1.00 36.47  ? 83   SER B O   1 
ATOM   2884 C  CB  . SER B 1 83  ? 1.492   -6.711  20.254  1.00 42.03  ? 83   SER B CB  1 
ATOM   2885 O  OG  . SER B 1 83  ? 1.760   -5.331  20.279  1.00 54.75  ? 83   SER B OG  1 
ATOM   2886 N  N   . ARG B 1 84  ? 3.813   -7.074  18.039  0.96 30.14  ? 84   ARG B N   1 
ATOM   2887 C  CA  . ARG B 1 84  ? 4.910   -6.469  17.280  0.96 32.10  ? 84   ARG B CA  1 
ATOM   2888 C  C   . ARG B 1 84  ? 5.974   -7.519  17.007  0.96 27.43  ? 84   ARG B C   1 
ATOM   2889 O  O   . ARG B 1 84  ? 6.150   -8.440  17.800  0.96 26.35  ? 84   ARG B O   1 
ATOM   2890 C  CB  . ARG B 1 84  ? 5.493   -5.276  18.048  0.96 32.65  ? 84   ARG B CB  1 
ATOM   2891 C  CG  . ARG B 1 84  ? 6.457   -4.402  17.269  0.96 47.86  ? 84   ARG B CG  1 
ATOM   2892 C  CD  . ARG B 1 84  ? 6.681   -3.084  18.024  0.96 57.31  ? 84   ARG B CD  1 
ATOM   2893 N  NE  . ARG B 1 84  ? 7.745   -2.228  17.478  0.96 52.50  ? 84   ARG B NE  1 
ATOM   2894 C  CZ  . ARG B 1 84  ? 7.546   -1.248  16.597  0.96 50.31  ? 84   ARG B CZ  1 
ATOM   2895 N  NH1 . ARG B 1 84  ? 6.320   -1.008  16.133  0.96 41.47  ? 84   ARG B NH1 1 
ATOM   2896 N  NH2 . ARG B 1 84  ? 8.569   -0.509  16.174  0.96 50.84  ? 84   ARG B NH2 1 
ATOM   2897 N  N   . VAL B 1 85  ? 6.660   -7.397  15.872  1.00 27.35  ? 85   VAL B N   1 
ATOM   2898 C  CA  . VAL B 1 85  ? 7.719   -8.333  15.519  1.00 23.17  ? 85   VAL B CA  1 
ATOM   2899 C  C   . VAL B 1 85  ? 8.946   -7.586  15.031  1.00 26.43  ? 85   VAL B C   1 
ATOM   2900 O  O   . VAL B 1 85  ? 8.888   -6.829  14.068  1.00 24.48  ? 85   VAL B O   1 
ATOM   2901 C  CB  . VAL B 1 85  ? 7.294   -9.320  14.413  1.00 26.73  ? 85   VAL B CB  1 
ATOM   2902 C  CG1 . VAL B 1 85  ? 8.447   -10.303 14.109  1.00 19.86  ? 85   VAL B CG1 1 
ATOM   2903 C  CG2 . VAL B 1 85  ? 6.023   -10.071 14.800  1.00 12.87  ? 85   VAL B CG2 1 
ATOM   2904 N  N   . THR B 1 86  ? 10.063  -7.812  15.703  1.00 23.39  ? 86   THR B N   1 
ATOM   2905 C  CA  . THR B 1 86  ? 11.292  -7.126  15.385  1.00 23.74  ? 86   THR B CA  1 
ATOM   2906 C  C   . THR B 1 86  ? 12.238  -8.178  14.863  1.00 31.57  ? 86   THR B C   1 
ATOM   2907 O  O   . THR B 1 86  ? 12.369  -9.240  15.471  1.00 24.61  ? 86   THR B O   1 
ATOM   2908 C  CB  . THR B 1 86  ? 11.872  -6.446  16.631  1.00 22.66  ? 86   THR B CB  1 
ATOM   2909 O  OG1 . THR B 1 86  ? 11.034  -5.347  16.986  1.00 24.88  ? 86   THR B OG1 1 
ATOM   2910 C  CG2 . THR B 1 86  ? 13.292  -5.936  16.376  1.00 17.53  ? 86   THR B CG2 1 
ATOM   2911 N  N   . ALA B 1 87  ? 12.862  -7.905  13.717  1.00 29.28  ? 87   ALA B N   1 
ATOM   2912 C  CA  . ALA B 1 87  ? 13.854  -8.821  13.174  1.00 19.36  ? 87   ALA B CA  1 
ATOM   2913 C  C   . ALA B 1 87  ? 15.235  -8.401  13.638  1.00 20.87  ? 87   ALA B C   1 
ATOM   2914 O  O   . ALA B 1 87  ? 15.644  -7.264  13.447  1.00 23.58  ? 87   ALA B O   1 
ATOM   2915 C  CB  . ALA B 1 87  ? 13.794  -8.847  11.656  1.00 25.55  ? 87   ALA B CB  1 
ATOM   2916 N  N   . VAL B 1 88  ? 15.955  -9.318  14.271  1.00 29.33  ? 88   VAL B N   1 
ATOM   2917 C  CA  . VAL B 1 88  ? 17.321  -9.032  14.677  1.00 22.39  ? 88   VAL B CA  1 
ATOM   2918 C  C   . VAL B 1 88  ? 18.227  -9.726  13.683  1.00 21.91  ? 88   VAL B C   1 
ATOM   2919 O  O   . VAL B 1 88  ? 18.306  -10.948 13.643  1.00 22.45  ? 88   VAL B O   1 
ATOM   2920 C  CB  . VAL B 1 88  ? 17.608  -9.514  16.101  1.00 24.70  ? 88   VAL B CB  1 
ATOM   2921 C  CG1 . VAL B 1 88  ? 18.991  -9.036  16.550  1.00 18.01  ? 88   VAL B CG1 1 
ATOM   2922 C  CG2 . VAL B 1 88  ? 16.531  -8.984  17.065  1.00 21.55  ? 88   VAL B CG2 1 
ATOM   2923 N  N   . ILE B 1 89  ? 18.883  -8.936  12.843  1.00 22.91  ? 89   ILE B N   1 
ATOM   2924 C  CA  . ILE B 1 89  ? 19.626  -9.494  11.725  1.00 25.52  ? 89   ILE B CA  1 
ATOM   2925 C  C   . ILE B 1 89  ? 21.045  -8.979  11.758  1.00 27.07  ? 89   ILE B C   1 
ATOM   2926 O  O   . ILE B 1 89  ? 21.377  -8.047  11.027  1.00 26.89  ? 89   ILE B O   1 
ATOM   2927 C  CB  . ILE B 1 89  ? 19.036  -9.062  10.386  1.00 30.53  ? 89   ILE B CB  1 
ATOM   2928 C  CG1 . ILE B 1 89  ? 17.559  -9.426  10.297  1.00 28.63  ? 89   ILE B CG1 1 
ATOM   2929 C  CG2 . ILE B 1 89  ? 19.820  -9.705  9.227   1.00 29.32  ? 89   ILE B CG2 1 
ATOM   2930 C  CD1 . ILE B 1 89  ? 16.867  -8.821  9.048   1.00 25.54  ? 89   ILE B CD1 1 
ATOM   2931 N  N   . PRO B 1 90  ? 21.893  -9.613  12.580  1.00 25.88  ? 90   PRO B N   1 
ATOM   2932 C  CA  . PRO B 1 90  ? 23.255  -9.132  12.816  1.00 28.50  ? 90   PRO B CA  1 
ATOM   2933 C  C   . PRO B 1 90  ? 23.998  -8.871  11.491  1.00 33.19  ? 90   PRO B C   1 
ATOM   2934 O  O   . PRO B 1 90  ? 24.615  -7.822  11.345  1.00 29.57  ? 90   PRO B O   1 
ATOM   2935 C  CB  . PRO B 1 90  ? 23.907  -10.278 13.609  1.00 24.77  ? 90   PRO B CB  1 
ATOM   2936 C  CG  . PRO B 1 90  ? 22.799  -11.085 14.163  1.00 25.99  ? 90   PRO B CG  1 
ATOM   2937 C  CD  . PRO B 1 90  ? 21.625  -10.909 13.237  1.00 25.77  ? 90   PRO B CD  1 
ATOM   2938 N  N   . CYS B 1 91  ? 23.934  -9.801  10.542  1.00 27.63  ? 91   CYS B N   1 
ATOM   2939 C  CA  . CYS B 1 91  ? 24.562  -9.587  9.237   1.00 27.43  ? 91   CYS B CA  1 
ATOM   2940 C  C   . CYS B 1 91  ? 23.507  -9.525  8.116   1.00 28.94  ? 91   CYS B C   1 
ATOM   2941 O  O   . CYS B 1 91  ? 22.932  -10.540 7.731   1.00 26.22  ? 91   CYS B O   1 
ATOM   2942 C  CB  . CYS B 1 91  ? 25.585  -10.694 8.943   1.00 26.14  ? 91   CYS B CB  1 
ATOM   2943 S  SG  . CYS B 1 91  ? 26.573  -10.422 7.409   1.00 38.13  ? 91   CYS B SG  1 
ATOM   2944 N  N   . PHE B 1 92  ? 23.252  -8.337  7.588   1.00 32.36  ? 92   PHE B N   1 
ATOM   2945 C  CA  . PHE B 1 92  ? 22.123  -8.159  6.676   1.00 27.89  ? 92   PHE B CA  1 
ATOM   2946 C  C   . PHE B 1 92  ? 22.395  -8.790  5.305   1.00 23.10  ? 92   PHE B C   1 
ATOM   2947 O  O   . PHE B 1 92  ? 23.325  -8.401  4.610   1.00 39.09  ? 92   PHE B O   1 
ATOM   2948 C  CB  . PHE B 1 92  ? 21.793  -6.670  6.553   1.00 26.35  ? 92   PHE B CB  1 
ATOM   2949 C  CG  . PHE B 1 92  ? 20.494  -6.383  5.851   1.00 28.84  ? 92   PHE B CG  1 
ATOM   2950 C  CD1 . PHE B 1 92  ? 19.310  -6.236  6.577   1.00 30.30  ? 92   PHE B CD1 1 
ATOM   2951 C  CD2 . PHE B 1 92  ? 20.460  -6.235  4.465   1.00 24.75  ? 92   PHE B CD2 1 
ATOM   2952 C  CE1 . PHE B 1 92  ? 18.108  -5.966  5.924   1.00 31.42  ? 92   PHE B CE1 1 
ATOM   2953 C  CE2 . PHE B 1 92  ? 19.266  -5.957  3.798   1.00 27.59  ? 92   PHE B CE2 1 
ATOM   2954 C  CZ  . PHE B 1 92  ? 18.081  -5.824  4.529   1.00 35.22  ? 92   PHE B CZ  1 
ATOM   2955 N  N   . PRO B 1 93  ? 21.564  -9.758  4.912   1.00 28.54  ? 93   PRO B N   1 
ATOM   2956 C  CA  . PRO B 1 93  ? 21.740  -10.554 3.687   1.00 29.92  ? 93   PRO B CA  1 
ATOM   2957 C  C   . PRO B 1 93  ? 21.670  -9.686  2.428   1.00 26.19  ? 93   PRO B C   1 
ATOM   2958 O  O   . PRO B 1 93  ? 20.826  -8.797  2.379   1.00 31.50  ? 93   PRO B O   1 
ATOM   2959 C  CB  . PRO B 1 93  ? 20.534  -11.504 3.705   1.00 30.71  ? 93   PRO B CB  1 
ATOM   2960 C  CG  . PRO B 1 93  ? 19.834  -11.291 5.027   1.00 34.78  ? 93   PRO B CG  1 
ATOM   2961 C  CD  . PRO B 1 93  ? 20.246  -9.965  5.536   1.00 35.65  ? 93   PRO B CD  1 
ATOM   2962 N  N   . TYR B 1 94  ? 22.543  -9.932  1.452   1.00 28.79  ? 94   TYR B N   1 
ATOM   2963 C  CA  . TYR B 1 94  ? 22.492  -9.274  0.146   1.00 23.60  ? 94   TYR B CA  1 
ATOM   2964 C  C   . TYR B 1 94  ? 22.826  -7.800  0.238   1.00 28.67  ? 94   TYR B C   1 
ATOM   2965 O  O   . TYR B 1 94  ? 22.597  -7.042  -0.700  1.00 24.99  ? 94   TYR B O   1 
ATOM   2966 C  CB  . TYR B 1 94  ? 21.129  -9.476  -0.518  1.00 24.17  ? 94   TYR B CB  1 
ATOM   2967 C  CG  . TYR B 1 94  ? 20.944  -10.886 -1.049  1.00 29.21  ? 94   TYR B CG  1 
ATOM   2968 C  CD1 . TYR B 1 94  ? 20.333  -11.858 -0.284  1.00 24.66  ? 94   TYR B CD1 1 
ATOM   2969 C  CD2 . TYR B 1 94  ? 21.410  -11.249 -2.310  1.00 29.28  ? 94   TYR B CD2 1 
ATOM   2970 C  CE1 . TYR B 1 94  ? 20.171  -13.154 -0.752  1.00 22.47  ? 94   TYR B CE1 1 
ATOM   2971 C  CE2 . TYR B 1 94  ? 21.252  -12.551 -2.787  1.00 31.20  ? 94   TYR B CE2 1 
ATOM   2972 C  CZ  . TYR B 1 94  ? 20.629  -13.493 -1.998  1.00 29.72  ? 94   TYR B CZ  1 
ATOM   2973 O  OH  . TYR B 1 94  ? 20.455  -14.784 -2.440  1.00 29.82  ? 94   TYR B OH  1 
ATOM   2974 N  N   . ALA B 1 95  ? 23.393  -7.415  1.376   1.00 30.37  ? 95   ALA B N   1 
ATOM   2975 C  CA  . ALA B 1 95  ? 23.763  -6.032  1.653   1.00 33.33  ? 95   ALA B CA  1 
ATOM   2976 C  C   . ALA B 1 95  ? 24.736  -5.458  0.632   1.00 34.45  ? 95   ALA B C   1 
ATOM   2977 O  O   . ALA B 1 95  ? 24.700  -4.260  0.342   1.00 38.80  ? 95   ALA B O   1 
ATOM   2978 C  CB  . ALA B 1 95  ? 24.337  -5.908  3.067   1.00 26.20  ? 95   ALA B CB  1 
ATOM   2979 N  N   . ARG B 1 96  ? 25.614  -6.303  0.104   1.00 30.66  ? 96   ARG B N   1 
ATOM   2980 C  CA  . ARG B 1 96  ? 26.534  -5.879  -0.947  1.00 41.17  ? 96   ARG B CA  1 
ATOM   2981 C  C   . ARG B 1 96  ? 25.833  -5.667  -2.293  1.00 43.17  ? 96   ARG B C   1 
ATOM   2982 O  O   . ARG B 1 96  ? 26.450  -5.207  -3.245  1.00 47.16  ? 96   ARG B O   1 
ATOM   2983 C  CB  . ARG B 1 96  ? 27.660  -6.894  -1.132  1.00 39.05  ? 96   ARG B CB  1 
ATOM   2984 C  CG  . ARG B 1 96  ? 28.770  -6.808  -0.108  1.00 43.01  ? 96   ARG B CG  1 
ATOM   2985 C  CD  . ARG B 1 96  ? 29.628  -8.055  -0.188  1.00 56.51  ? 96   ARG B CD  1 
ATOM   2986 N  NE  . ARG B 1 96  ? 28.801  -9.257  -0.086  1.00 64.72  ? 96   ARG B NE  1 
ATOM   2987 C  CZ  . ARG B 1 96  ? 29.244  -10.492 -0.296  1.00 67.72  ? 96   ARG B CZ  1 
ATOM   2988 N  NH1 . ARG B 1 96  ? 30.512  -10.701 -0.631  1.00 59.48  ? 96   ARG B NH1 1 
ATOM   2989 N  NH2 . ARG B 1 96  ? 28.417  -11.520 -0.175  1.00 73.49  ? 96   ARG B NH2 1 
ATOM   2990 N  N   . GLN B 1 97  ? 24.555  -6.017  -2.381  1.00 41.75  ? 97   GLN B N   1 
ATOM   2991 C  CA  . GLN B 1 97  ? 23.786  -5.779  -3.611  1.00 40.31  ? 97   GLN B CA  1 
ATOM   2992 C  C   . GLN B 1 97  ? 22.790  -4.634  -3.407  1.00 31.65  ? 97   GLN B C   1 
ATOM   2993 O  O   . GLN B 1 97  ? 21.581  -4.836  -3.359  1.00 36.04  ? 97   GLN B O   1 
ATOM   2994 C  CB  . GLN B 1 97  ? 23.100  -7.066  -4.081  1.00 33.03  ? 97   GLN B CB  1 
ATOM   2995 C  CG  . GLN B 1 97  ? 24.074  -8.242  -4.190  1.00 44.55  ? 97   GLN B CG  1 
ATOM   2996 C  CD  . GLN B 1 97  ? 23.509  -9.405  -4.987  1.00 60.04  ? 97   GLN B CD  1 
ATOM   2997 O  OE1 . GLN B 1 97  ? 22.538  -9.249  -5.739  1.00 64.50  ? 97   GLN B OE1 1 
ATOM   2998 N  NE2 . GLN B 1 97  ? 24.106  -10.585 -4.819  1.00 60.61  ? 97   GLN B NE2 1 
ATOM   2999 N  N   . ASP B 1 98  ? 23.330  -3.426  -3.291  1.00 37.32  ? 98   ASP B N   1 
ATOM   3000 C  CA  . ASP B 1 98  ? 22.570  -2.269  -2.839  1.00 42.28  ? 98   ASP B CA  1 
ATOM   3001 C  C   . ASP B 1 98  ? 22.567  -1.105  -3.851  1.00 43.16  ? 98   ASP B C   1 
ATOM   3002 O  O   . ASP B 1 98  ? 22.032  -0.028  -3.567  1.00 54.59  ? 98   ASP B O   1 
ATOM   3003 C  CB  . ASP B 1 98  ? 23.097  -1.807  -1.471  1.00 39.67  ? 98   ASP B CB  1 
ATOM   3004 C  CG  . ASP B 1 98  ? 24.559  -1.361  -1.515  1.00 52.14  ? 98   ASP B CG  1 
ATOM   3005 O  OD1 . ASP B 1 98  ? 25.351  -1.862  -2.353  1.00 52.01  ? 98   ASP B OD1 1 
ATOM   3006 O  OD2 . ASP B 1 98  ? 24.926  -0.505  -0.688  1.00 51.54  ? 98   ASP B OD2 1 
ATOM   3007 N  N   . LYS B 1 99  ? 23.151  -1.341  -5.026  1.00 38.64  ? 99   LYS B N   1 
ATOM   3008 C  CA  . LYS B 1 99  ? 23.175  -0.364  -6.126  1.00 39.61  ? 99   LYS B CA  1 
ATOM   3009 C  C   . LYS B 1 99  ? 23.296  -1.091  -7.473  1.00 42.90  ? 99   LYS B C   1 
ATOM   3010 O  O   . LYS B 1 99  ? 23.657  -2.279  -7.517  1.00 38.30  ? 99   LYS B O   1 
ATOM   3011 C  CB  . LYS B 1 99  ? 24.343  0.609   -5.956  1.00 34.41  ? 99   LYS B CB  1 
ATOM   3012 C  CG  . LYS B 1 99  ? 25.710  -0.078  -5.973  1.00 38.72  ? 99   LYS B CG  1 
ATOM   3013 C  CD  . LYS B 1 99  ? 26.819  0.863   -5.485  1.00 47.76  ? 99   LYS B CD  1 
ATOM   3014 N  N   . LYS B 1 100 ? 22.992  -0.385  -8.564  1.00 41.71  ? 100  LYS B N   1 
ATOM   3015 C  CA  . LYS B 1 100 ? 23.081  -0.966  -9.908  1.00 52.30  ? 100  LYS B CA  1 
ATOM   3016 C  C   . LYS B 1 100 ? 24.522  -0.994  -10.440 1.00 57.29  ? 100  LYS B C   1 
ATOM   3017 O  O   . LYS B 1 100 ? 24.925  -1.948  -11.125 1.00 51.31  ? 100  LYS B O   1 
ATOM   3018 C  CB  . LYS B 1 100 ? 22.177  -0.222  -10.901 1.00 57.16  ? 100  LYS B CB  1 
ATOM   3019 C  CG  . LYS B 1 100 ? 20.686  -0.591  -10.867 1.00 55.01  ? 100  LYS B CG  1 
ATOM   3020 C  CD  . LYS B 1 100 ? 19.938  0.087   -12.023 1.00 51.92  ? 100  LYS B CD  1 
ATOM   3021 C  CE  . LYS B 1 100 ? 18.428  -0.147  -11.962 1.00 55.16  ? 100  LYS B CE  1 
ATOM   3022 N  NZ  . LYS B 1 100 ? 17.640  0.821   -12.804 1.00 52.83  ? 100  LYS B NZ  1 
ATOM   3023 N  N   . ASP B 1 101 ? 25.289  0.051   -10.133 0.80 54.12  ? 101  ASP B N   1 
ATOM   3024 C  CA  . ASP B 1 101 ? 26.687  0.118   -10.545 0.80 60.52  ? 101  ASP B CA  1 
ATOM   3025 C  C   . ASP B 1 101 ? 26.833  -0.021  -12.065 0.80 58.43  ? 101  ASP B C   1 
ATOM   3026 O  O   . ASP B 1 101 ? 27.627  -0.836  -12.540 0.80 58.39  ? 101  ASP B O   1 
ATOM   3027 C  CB  . ASP B 1 101 ? 27.496  -0.993  -9.858  0.80 65.60  ? 101  ASP B CB  1 
ATOM   3028 C  CG  . ASP B 1 101 ? 28.825  -0.493  -9.270  0.80 73.65  ? 101  ASP B CG  1 
ATOM   3029 O  OD1 . ASP B 1 101 ? 29.764  -0.084  -10.040 0.80 67.49  ? 101  ASP B OD1 1 
ATOM   3030 O  OD2 . ASP B 1 101 ? 28.937  -0.535  -8.011  0.80 85.00  ? 101  ASP B OD2 1 
ATOM   3031 N  N   . LYS B 1 102 ? 26.061  0.760   -12.821 1.00 51.72  ? 102  LYS B N   1 
ATOM   3032 C  CA  . LYS B 1 102 ? 26.168  0.789   -14.287 1.00 59.59  ? 102  LYS B CA  1 
ATOM   3033 C  C   . LYS B 1 102 ? 25.931  -0.577  -14.940 1.00 62.19  ? 102  LYS B C   1 
ATOM   3034 O  O   . LYS B 1 102 ? 26.486  -0.870  -16.000 1.00 62.34  ? 102  LYS B O   1 
ATOM   3035 C  CB  . LYS B 1 102 ? 27.529  1.347   -14.725 1.00 61.79  ? 102  LYS B CB  1 
ATOM   3036 C  CG  . LYS B 1 102 ? 27.972  2.595   -13.968 1.00 63.94  ? 102  LYS B CG  1 
ATOM   3037 N  N   . SER B 1 103 ? 25.111  -1.401  -14.293 1.00 58.66  ? 103  SER B N   1 
ATOM   3038 C  CA  . SER B 1 103 ? 24.739  -2.717  -14.807 1.00 52.28  ? 103  SER B CA  1 
ATOM   3039 C  C   . SER B 1 103 ? 23.224  -2.869  -14.762 1.00 53.57  ? 103  SER B C   1 
ATOM   3040 O  O   . SER B 1 103 ? 22.538  -2.086  -14.101 1.00 59.99  ? 103  SER B O   1 
ATOM   3041 C  CB  . SER B 1 103 ? 25.370  -3.823  -13.960 1.00 60.93  ? 103  SER B CB  1 
ATOM   3042 O  OG  . SER B 1 103 ? 26.780  -3.702  -13.912 1.00 67.99  ? 103  SER B OG  1 
ATOM   3043 N  N   . ARG B 1 104 ? 22.701  -3.870  -15.469 1.00 48.46  ? 104  ARG B N   1 
ATOM   3044 C  CA  . ARG B 1 104 ? 21.293  -4.235  -15.335 1.00 41.79  ? 104  ARG B CA  1 
ATOM   3045 C  C   . ARG B 1 104 ? 21.172  -5.250  -14.178 1.00 48.25  ? 104  ARG B C   1 
ATOM   3046 O  O   . ARG B 1 104 ? 20.847  -6.426  -14.372 1.00 52.75  ? 104  ARG B O   1 
ATOM   3047 C  CB  . ARG B 1 104 ? 20.720  -4.751  -16.668 1.00 42.75  ? 104  ARG B CB  1 
ATOM   3048 C  CG  . ARG B 1 104 ? 20.586  -3.650  -17.730 1.00 48.82  ? 104  ARG B CG  1 
ATOM   3049 C  CD  . ARG B 1 104 ? 19.968  -4.122  -19.049 1.00 46.09  ? 104  ARG B CD  1 
ATOM   3050 N  NE  . ARG B 1 104 ? 20.968  -4.680  -19.960 1.00 55.53  ? 104  ARG B NE  1 
ATOM   3051 C  CZ  . ARG B 1 104 ? 21.562  -4.001  -20.936 1.00 56.99  ? 104  ARG B CZ  1 
ATOM   3052 N  NH1 . ARG B 1 104 ? 21.259  -2.733  -21.144 1.00 53.00  ? 104  ARG B NH1 1 
ATOM   3053 N  NH2 . ARG B 1 104 ? 22.462  -4.592  -21.717 1.00 73.58  ? 104  ARG B NH2 1 
ATOM   3054 N  N   . ALA B 1 105 ? 21.461  -4.758  -12.974 1.00 42.99  ? 105  ALA B N   1 
ATOM   3055 C  CA  . ALA B 1 105 ? 21.547  -5.569  -11.755 1.00 47.61  ? 105  ALA B CA  1 
ATOM   3056 C  C   . ALA B 1 105 ? 20.340  -5.384  -10.840 1.00 41.64  ? 105  ALA B C   1 
ATOM   3057 O  O   . ALA B 1 105 ? 19.759  -4.299  -10.767 1.00 33.06  ? 105  ALA B O   1 
ATOM   3058 C  CB  . ALA B 1 105 ? 22.810  -5.219  -10.986 1.00 38.33  ? 105  ALA B CB  1 
ATOM   3059 N  N   . PRO B 1 106 ? 19.976  -6.431  -10.098 1.00 46.52  ? 106  PRO B N   1 
ATOM   3060 C  CA  . PRO B 1 106 ? 18.930  -6.171  -9.100  1.00 46.93  ? 106  PRO B CA  1 
ATOM   3061 C  C   . PRO B 1 106 ? 19.509  -5.285  -7.990  1.00 41.06  ? 106  PRO B C   1 
ATOM   3062 O  O   . PRO B 1 106 ? 20.716  -5.307  -7.779  1.00 42.03  ? 106  PRO B O   1 
ATOM   3063 C  CB  . PRO B 1 106 ? 18.620  -7.573  -8.562  1.00 40.81  ? 106  PRO B CB  1 
ATOM   3064 C  CG  . PRO B 1 106 ? 19.932  -8.317  -8.717  1.00 42.69  ? 106  PRO B CG  1 
ATOM   3065 C  CD  . PRO B 1 106 ? 20.618  -7.751  -9.929  1.00 36.58  ? 106  PRO B CD  1 
ATOM   3066 N  N   . ILE B 1 107 ? 18.691  -4.492  -7.313  1.00 38.85  ? 107  ILE B N   1 
ATOM   3067 C  CA  . ILE B 1 107 ? 19.140  -3.954  -6.037  1.00 37.29  ? 107  ILE B CA  1 
ATOM   3068 C  C   . ILE B 1 107 ? 18.518  -4.851  -4.968  1.00 33.56  ? 107  ILE B C   1 
ATOM   3069 O  O   . ILE B 1 107 ? 17.486  -4.520  -4.376  1.00 32.38  ? 107  ILE B O   1 
ATOM   3070 C  CB  . ILE B 1 107 ? 18.764  -2.486  -5.834  1.00 43.70  ? 107  ILE B CB  1 
ATOM   3071 C  CG1 . ILE B 1 107 ? 19.314  -1.632  -6.978  1.00 35.83  ? 107  ILE B CG1 1 
ATOM   3072 C  CG2 . ILE B 1 107 ? 19.300  -1.978  -4.478  1.00 37.39  ? 107  ILE B CG2 1 
ATOM   3073 C  CD1 . ILE B 1 107 ? 18.841  -0.190  -6.922  1.00 36.93  ? 107  ILE B CD1 1 
ATOM   3074 N  N   . SER B 1 108 ? 19.162  -5.997  -4.763  1.00 24.54  ? 108  SER B N   1 
ATOM   3075 C  CA  . SER B 1 108 ? 18.626  -7.112  -3.974  1.00 30.04  ? 108  SER B CA  1 
ATOM   3076 C  C   . SER B 1 108 ? 18.499  -6.824  -2.490  1.00 28.38  ? 108  SER B C   1 
ATOM   3077 O  O   . SER B 1 108 ? 17.745  -7.495  -1.796  1.00 33.21  ? 108  SER B O   1 
ATOM   3078 C  CB  . SER B 1 108 ? 19.507  -8.348  -4.139  1.00 24.35  ? 108  SER B CB  1 
ATOM   3079 O  OG  . SER B 1 108 ? 19.853  -8.546  -5.492  1.00 35.56  ? 108  SER B OG  1 
ATOM   3080 N  N   . ALA B 1 109 ? 19.253  -5.853  -1.994  1.00 29.83  ? 109  ALA B N   1 
ATOM   3081 C  CA  . ALA B 1 109 ? 19.118  -5.467  -0.594  1.00 24.48  ? 109  ALA B CA  1 
ATOM   3082 C  C   . ALA B 1 109 ? 17.788  -4.742  -0.408  1.00 30.82  ? 109  ALA B C   1 
ATOM   3083 O  O   . ALA B 1 109 ? 17.155  -4.859  0.635   1.00 29.55  ? 109  ALA B O   1 
ATOM   3084 C  CB  . ALA B 1 109 ? 20.293  -4.607  -0.162  1.00 19.63  ? 109  ALA B CB  1 
ATOM   3085 N  N   . LYS B 1 110 ? 17.353  -4.016  -1.439  1.00 26.04  ? 110  LYS B N   1 
ATOM   3086 C  CA  . LYS B 1 110 ? 16.014  -3.417  -1.439  1.00 22.52  ? 110  LYS B CA  1 
ATOM   3087 C  C   . LYS B 1 110 ? 14.917  -4.478  -1.509  1.00 27.49  ? 110  LYS B C   1 
ATOM   3088 O  O   . LYS B 1 110 ? 13.885  -4.377  -0.820  1.00 26.81  ? 110  LYS B O   1 
ATOM   3089 C  CB  . LYS B 1 110 ? 15.851  -2.410  -2.586  1.00 19.73  ? 110  LYS B CB  1 
ATOM   3090 C  CG  . LYS B 1 110 ? 14.458  -1.772  -2.672  1.00 17.06  ? 110  LYS B CG  1 
ATOM   3091 C  CD  . LYS B 1 110 ? 14.065  -1.124  -1.345  1.00 18.54  ? 110  LYS B CD  1 
ATOM   3092 C  CE  . LYS B 1 110 ? 12.685  -0.488  -1.399  1.00 23.91  ? 110  LYS B CE  1 
ATOM   3093 N  NZ  . LYS B 1 110 ? 12.624  0.471   -2.534  1.00 32.50  ? 110  LYS B NZ  1 
ATOM   3094 N  N   . LEU B 1 111 ? 15.133  -5.492  -2.347  1.00 20.36  ? 111  LEU B N   1 
ATOM   3095 C  CA  . LEU B 1 111 ? 14.173  -6.577  -2.452  1.00 24.61  ? 111  LEU B CA  1 
ATOM   3096 C  C   . LEU B 1 111 ? 14.063  -7.264  -1.069  1.00 22.49  ? 111  LEU B C   1 
ATOM   3097 O  O   . LEU B 1 111 ? 12.983  -7.559  -0.597  1.00 23.07  ? 111  LEU B O   1 
ATOM   3098 C  CB  . LEU B 1 111 ? 14.626  -7.573  -3.529  1.00 33.89  ? 111  LEU B CB  1 
ATOM   3099 C  CG  . LEU B 1 111 ? 13.969  -8.958  -3.593  1.00 29.18  ? 111  LEU B CG  1 
ATOM   3100 C  CD1 . LEU B 1 111 ? 12.497  -8.847  -3.927  1.00 27.17  ? 111  LEU B CD1 1 
ATOM   3101 C  CD2 . LEU B 1 111 ? 14.685  -9.857  -4.598  1.00 32.65  ? 111  LEU B CD2 1 
ATOM   3102 N  N   . VAL B 1 112 ? 15.199  -7.519  -0.443  1.00 23.22  ? 112  VAL B N   1 
ATOM   3103 C  CA  . VAL B 1 112 ? 15.230  -8.101  0.890   1.00 29.81  ? 112  VAL B CA  1 
ATOM   3104 C  C   . VAL B 1 112 ? 14.488  -7.208  1.887   1.00 28.67  ? 112  VAL B C   1 
ATOM   3105 O  O   . VAL B 1 112 ? 13.649  -7.694  2.639   1.00 28.00  ? 112  VAL B O   1 
ATOM   3106 C  CB  . VAL B 1 112 ? 16.676  -8.386  1.341   1.00 23.36  ? 112  VAL B CB  1 
ATOM   3107 C  CG1 . VAL B 1 112 ? 16.735  -8.719  2.842   1.00 23.60  ? 112  VAL B CG1 1 
ATOM   3108 C  CG2 . VAL B 1 112 ? 17.243  -9.538  0.511   1.00 21.26  ? 112  VAL B CG2 1 
ATOM   3109 N  N   . ALA B 1 113 ? 14.752  -5.905  1.875   1.00 21.27  ? 113  ALA B N   1 
ATOM   3110 C  CA  . ALA B 1 113 ? 13.992  -5.009  2.745   1.00 19.70  ? 113  ALA B CA  1 
ATOM   3111 C  C   . ALA B 1 113 ? 12.488  -5.118  2.474   1.00 32.57  ? 113  ALA B C   1 
ATOM   3112 O  O   . ALA B 1 113 ? 11.698  -5.171  3.405   1.00 25.64  ? 113  ALA B O   1 
ATOM   3113 C  CB  . ALA B 1 113 ? 14.462  -3.594  2.585   1.00 15.70  ? 113  ALA B CB  1 
ATOM   3114 N  N   . ASN B 1 114 ? 12.098  -5.170  1.197   1.00 28.60  ? 114  ASN B N   1 
ATOM   3115 C  CA  . ASN B 1 114 ? 10.690  -5.306  0.820   1.00 27.22  ? 114  ASN B CA  1 
ATOM   3116 C  C   . ASN B 1 114 ? 10.090  -6.615  1.289   1.00 15.15  ? 114  ASN B C   1 
ATOM   3117 O  O   . ASN B 1 114 ? 8.963   -6.655  1.762   1.00 26.08  ? 114  ASN B O   1 
ATOM   3118 C  CB  . ASN B 1 114 ? 10.490  -5.192  -0.706  1.00 24.66  ? 114  ASN B CB  1 
ATOM   3119 C  CG  . ASN B 1 114 ? 10.508  -3.755  -1.199  1.00 33.77  ? 114  ASN B CG  1 
ATOM   3120 O  OD1 . ASN B 1 114 ? 10.350  -2.808  -0.427  1.00 29.97  ? 114  ASN B OD1 1 
ATOM   3121 N  ND2 . ASN B 1 114 ? 10.673  -3.591  -2.503  1.00 26.07  ? 114  ASN B ND2 1 
ATOM   3122 N  N   . MET B 1 115 ? 10.824  -7.700  1.147   0.98 16.69  ? 115  MET B N   1 
ATOM   3123 C  CA  . MET B 1 115 ? 10.297  -8.979  1.608   0.98 21.57  ? 115  MET B CA  1 
ATOM   3124 C  C   . MET B 1 115 ? 10.082  -8.949  3.140   0.98 25.51  ? 115  MET B C   1 
ATOM   3125 O  O   . MET B 1 115 ? 9.054   -9.386  3.629   0.98 25.34  ? 115  MET B O   1 
ATOM   3126 C  CB  . MET B 1 115 ? 11.245  -10.107 1.201   0.98 17.65  ? 115  MET B CB  1 
ATOM   3127 C  CG  . MET B 1 115 ? 11.350  -10.372 -0.347  0.98 20.03  ? 115  MET B CG  1 
ATOM   3128 S  SD  . MET B 1 115 ? 12.884  -11.265 -0.700  0.98 35.48  ? 115  MET B SD  1 
ATOM   3129 C  CE  . MET B 1 115 ? 12.517  -12.905 -0.095  0.98 50.12  ? 115  MET B CE  1 
ATOM   3130 N  N   . LEU B 1 116 ? 11.056  -8.442  3.889   1.00 20.28  ? 116  LEU B N   1 
ATOM   3131 C  CA  . LEU B 1 116 ? 10.937  -8.333  5.351   1.00 23.47  ? 116  LEU B CA  1 
ATOM   3132 C  C   . LEU B 1 116 ? 9.729   -7.498  5.747   1.00 23.73  ? 116  LEU B C   1 
ATOM   3133 O  O   . LEU B 1 116 ? 8.983   -7.848  6.650   1.00 26.10  ? 116  LEU B O   1 
ATOM   3134 C  CB  . LEU B 1 116 ? 12.202  -7.711  5.948   1.00 20.96  ? 116  LEU B CB  1 
ATOM   3135 C  CG  . LEU B 1 116 ? 13.431  -8.622  5.983   1.00 27.26  ? 116  LEU B CG  1 
ATOM   3136 C  CD1 . LEU B 1 116 ? 14.714  -7.810  6.026   1.00 19.05  ? 116  LEU B CD1 1 
ATOM   3137 C  CD2 . LEU B 1 116 ? 13.354  -9.590  7.171   1.00 21.45  ? 116  LEU B CD2 1 
ATOM   3138 N  N   . SER B 1 117 ? 9.522   -6.392  5.046   1.00 30.37  ? 117  SER B N   1 
ATOM   3139 C  CA  . SER B 1 117 ? 8.340   -5.582  5.261   1.00 27.53  ? 117  SER B CA  1 
ATOM   3140 C  C   . SER B 1 117 ? 7.034   -6.345  4.966   1.00 28.70  ? 117  SER B C   1 
ATOM   3141 O  O   . SER B 1 117 ? 6.146   -6.401  5.815   1.00 25.98  ? 117  SER B O   1 
ATOM   3142 C  CB  . SER B 1 117 ? 8.427   -4.286  4.452   1.00 35.46  ? 117  SER B CB  1 
ATOM   3143 O  OG  . SER B 1 117 ? 9.682   -3.630  4.659   1.00 37.10  ? 117  SER B OG  1 
ATOM   3144 N  N   . VAL B 1 118 ? 6.895   -6.938  3.782   1.00 18.55  ? 118  VAL B N   1 
ATOM   3145 C  CA  . VAL B 1 118 ? 5.643   -7.628  3.500   1.00 21.39  ? 118  VAL B CA  1 
ATOM   3146 C  C   . VAL B 1 118 ? 5.442   -8.833  4.402   1.00 22.41  ? 118  VAL B C   1 
ATOM   3147 O  O   . VAL B 1 118 ? 4.310   -9.245  4.640   1.00 30.00  ? 118  VAL B O   1 
ATOM   3148 C  CB  . VAL B 1 118 ? 5.471   -8.046  2.019   1.00 34.50  ? 118  VAL B CB  1 
ATOM   3149 C  CG1 . VAL B 1 118 ? 5.610   -6.842  1.121   1.00 41.30  ? 118  VAL B CG1 1 
ATOM   3150 C  CG2 . VAL B 1 118 ? 6.464   -9.174  1.624   1.00 28.74  ? 118  VAL B CG2 1 
ATOM   3151 N  N   . ALA B 1 119 ? 6.531   -9.416  4.892   1.00 16.44  ? 119  ALA B N   1 
ATOM   3152 C  CA  . ALA B 1 119 ? 6.388   -10.534 5.825   1.00 22.01  ? 119  ALA B CA  1 
ATOM   3153 C  C   . ALA B 1 119 ? 5.768   -10.056 7.135   1.00 22.15  ? 119  ALA B C   1 
ATOM   3154 O  O   . ALA B 1 119 ? 5.164   -10.843 7.838   1.00 24.91  ? 119  ALA B O   1 
ATOM   3155 C  CB  . ALA B 1 119 ? 7.719   -11.227 6.081   1.00 18.05  ? 119  ALA B CB  1 
ATOM   3156 N  N   . GLY B 1 120 ? 5.912   -8.773  7.460   1.00 24.95  ? 120  GLY B N   1 
ATOM   3157 C  CA  . GLY B 1 120 ? 5.290   -8.228  8.660   1.00 27.80  ? 120  GLY B CA  1 
ATOM   3158 C  C   . GLY B 1 120 ? 6.195   -7.657  9.756   1.00 28.02  ? 120  GLY B C   1 
ATOM   3159 O  O   . GLY B 1 120 ? 5.722   -7.381  10.857  1.00 32.67  ? 120  GLY B O   1 
ATOM   3160 N  N   . ALA B 1 121 ? 7.479   -7.444  9.453   1.00 22.72  ? 121  ALA B N   1 
ATOM   3161 C  CA  . ALA B 1 121 ? 8.426   -6.838  10.399  1.00 26.47  ? 121  ALA B CA  1 
ATOM   3162 C  C   . ALA B 1 121 ? 8.101   -5.376  10.702  1.00 28.88  ? 121  ALA B C   1 
ATOM   3163 O  O   . ALA B 1 121 ? 7.784   -4.603  9.792   1.00 21.01  ? 121  ALA B O   1 
ATOM   3164 C  CB  . ALA B 1 121 ? 9.866   -6.971  9.886   1.00 24.58  ? 121  ALA B CB  1 
ATOM   3165 N  N   . ASP B 1 122 ? 8.191   -4.999  11.976  0.80 12.19  ? 122  ASP B N   1 
ATOM   3166 C  CA  . ASP B 1 122 ? 7.825   -3.664  12.398  0.80 7.92   ? 122  ASP B CA  1 
ATOM   3167 C  C   . ASP B 1 122 ? 9.067   -2.856  12.717  0.80 14.94  ? 122  ASP B C   1 
ATOM   3168 O  O   . ASP B 1 122 ? 9.033   -1.649  12.868  0.80 20.39  ? 122  ASP B O   1 
ATOM   3169 C  CB  . ASP B 1 122 ? 6.874   -3.726  13.601  0.80 14.25  ? 122  ASP B CB  1 
ATOM   3170 C  CG  . ASP B 1 122 ? 5.639   -4.568  13.318  0.80 24.74  ? 122  ASP B CG  1 
ATOM   3171 O  OD1 . ASP B 1 122 ? 4.860   -4.163  12.432  0.80 24.16  ? 122  ASP B OD1 1 
ATOM   3172 O  OD2 . ASP B 1 122 ? 5.449   -5.637  13.963  0.80 19.28  ? 122  ASP B OD2 1 
ATOM   3173 N  N   . HIS B 1 123 ? 10.189  -3.544  12.786  1.00 20.69  ? 123  HIS B N   1 
ATOM   3174 C  CA  . HIS B 1 123 ? 11.409  -2.928  13.277  1.00 24.20  ? 123  HIS B CA  1 
ATOM   3175 C  C   . HIS B 1 123 ? 12.531  -3.873  12.909  1.00 22.83  ? 123  HIS B C   1 
ATOM   3176 O  O   . HIS B 1 123 ? 12.355  -5.089  12.925  1.00 28.50  ? 123  HIS B O   1 
ATOM   3177 C  CB  . HIS B 1 123 ? 11.331  -2.722  14.811  1.00 21.47  ? 123  HIS B CB  1 
ATOM   3178 C  CG  . HIS B 1 123 ? 12.452  -1.898  15.377  1.00 33.34  ? 123  HIS B CG  1 
ATOM   3179 N  ND1 . HIS B 1 123 ? 13.740  -1.960  14.896  1.00 51.37  ? 123  HIS B ND1 1 
ATOM   3180 C  CD2 . HIS B 1 123 ? 12.474  -0.993  16.383  1.00 41.92  ? 123  HIS B CD2 1 
ATOM   3181 C  CE1 . HIS B 1 123 ? 14.509  -1.129  15.579  1.00 39.84  ? 123  HIS B CE1 1 
ATOM   3182 N  NE2 . HIS B 1 123 ? 13.767  -0.534  16.489  1.00 39.35  ? 123  HIS B NE2 1 
ATOM   3183 N  N   . ILE B 1 124 ? 13.676  -3.308  12.539  1.00 22.15  ? 124  ILE B N   1 
ATOM   3184 C  CA  . ILE B 1 124 ? 14.847  -4.102  12.227  1.00 19.25  ? 124  ILE B CA  1 
ATOM   3185 C  C   . ILE B 1 124 ? 15.930  -3.664  13.189  1.00 19.40  ? 124  ILE B C   1 
ATOM   3186 O  O   . ILE B 1 124 ? 16.072  -2.484  13.451  1.00 22.44  ? 124  ILE B O   1 
ATOM   3187 C  CB  . ILE B 1 124 ? 15.402  -3.817  10.800  1.00 24.21  ? 124  ILE B CB  1 
ATOM   3188 C  CG1 . ILE B 1 124 ? 14.351  -4.047  9.717   1.00 23.41  ? 124  ILE B CG1 1 
ATOM   3189 C  CG2 . ILE B 1 124 ? 16.630  -4.705  10.525  1.00 19.88  ? 124  ILE B CG2 1 
ATOM   3190 C  CD1 . ILE B 1 124 ? 13.875  -5.464  9.641   1.00 22.32  ? 124  ILE B CD1 1 
ATOM   3191 N  N   . ILE B 1 125 ? 16.702  -4.610  13.699  1.00 21.59  ? 125  ILE B N   1 
ATOM   3192 C  CA  . ILE B 1 125 ? 17.908  -4.284  14.455  1.00 17.80  ? 125  ILE B CA  1 
ATOM   3193 C  C   . ILE B 1 125 ? 19.039  -5.008  13.741  1.00 20.87  ? 125  ILE B C   1 
ATOM   3194 O  O   . ILE B 1 125 ? 19.002  -6.223  13.591  1.00 26.09  ? 125  ILE B O   1 
ATOM   3195 C  CB  . ILE B 1 125 ? 17.801  -4.762  15.928  1.00 29.64  ? 125  ILE B CB  1 
ATOM   3196 C  CG1 . ILE B 1 125 ? 16.805  -3.889  16.696  1.00 26.23  ? 125  ILE B CG1 1 
ATOM   3197 C  CG2 . ILE B 1 125 ? 19.152  -4.715  16.623  1.00 25.25  ? 125  ILE B CG2 1 
ATOM   3198 C  CD1 . ILE B 1 125 ? 16.298  -4.504  17.995  1.00 29.29  ? 125  ILE B CD1 1 
ATOM   3199 N  N   . THR B 1 126 ? 20.039  -4.276  13.277  1.00 24.58  ? 126  THR B N   1 
ATOM   3200 C  CA  . THR B 1 126 ? 21.131  -4.921  12.566  1.00 19.29  ? 126  THR B CA  1 
ATOM   3201 C  C   . THR B 1 126 ? 22.461  -4.358  13.044  1.00 24.07  ? 126  THR B C   1 
ATOM   3202 O  O   . THR B 1 126 ? 22.495  -3.420  13.849  1.00 26.02  ? 126  THR B O   1 
ATOM   3203 C  CB  . THR B 1 126 ? 20.949  -4.798  10.998  1.00 26.57  ? 126  THR B CB  1 
ATOM   3204 O  OG1 . THR B 1 126 ? 21.918  -5.603  10.312  1.00 31.54  ? 126  THR B OG1 1 
ATOM   3205 C  CG2 . THR B 1 126 ? 21.053  -3.340  10.524  1.00 26.08  ? 126  THR B CG2 1 
ATOM   3206 N  N   . MET B 1 127 ? 23.552  -4.940  12.554  1.00 24.15  ? 127  MET B N   1 
ATOM   3207 C  CA  . MET B 1 127 ? 24.874  -4.416  12.835  1.00 23.77  ? 127  MET B CA  1 
ATOM   3208 C  C   . MET B 1 127 ? 25.719  -4.118  11.594  1.00 21.21  ? 127  MET B C   1 
ATOM   3209 O  O   . MET B 1 127 ? 25.897  -4.965  10.718  1.00 27.70  ? 127  MET B O   1 
ATOM   3210 C  CB  . MET B 1 127 ? 25.655  -5.346  13.770  1.00 23.28  ? 127  MET B CB  1 
ATOM   3211 C  CG  . MET B 1 127 ? 27.023  -4.750  14.112  1.00 34.47  ? 127  MET B CG  1 
ATOM   3212 S  SD  . MET B 1 127 ? 27.831  -5.539  15.519  1.00 42.56  ? 127  MET B SD  1 
ATOM   3213 C  CE  . MET B 1 127 ? 26.763  -4.945  16.829  1.00 24.93  ? 127  MET B CE  1 
ATOM   3214 N  N   . ASP B 1 128 ? 26.274  -2.914  11.568  1.00 18.36  ? 128  ASP B N   1 
ATOM   3215 C  CA  . ASP B 1 128 ? 27.109  -2.427  10.472  1.00 27.20  ? 128  ASP B CA  1 
ATOM   3216 C  C   . ASP B 1 128 ? 26.594  -2.769  9.087   1.00 30.54  ? 128  ASP B C   1 
ATOM   3217 O  O   . ASP B 1 128 ? 27.169  -3.598  8.387   1.00 30.57  ? 128  ASP B O   1 
ATOM   3218 C  CB  . ASP B 1 128 ? 28.557  -2.873  10.653  1.00 32.29  ? 128  ASP B CB  1 
ATOM   3219 C  CG  . ASP B 1 128 ? 29.218  -2.171  11.809  1.00 49.75  ? 128  ASP B CG  1 
ATOM   3220 O  OD1 . ASP B 1 128 ? 29.154  -0.921  11.847  1.00 59.07  ? 128  ASP B OD1 1 
ATOM   3221 O  OD2 . ASP B 1 128 ? 29.770  -2.858  12.691  1.00 52.37  ? 128  ASP B OD2 1 
ATOM   3222 N  N   . LEU B 1 129 ? 25.499  -2.124  8.698   1.00 34.81  ? 129  LEU B N   1 
ATOM   3223 C  CA  . LEU B 1 129 ? 25.016  -2.242  7.334   1.00 31.86  ? 129  LEU B CA  1 
ATOM   3224 C  C   . LEU B 1 129 ? 26.169  -1.909  6.418   1.00 35.68  ? 129  LEU B C   1 
ATOM   3225 O  O   . LEU B 1 129 ? 26.932  -0.970  6.692   1.00 33.55  ? 129  LEU B O   1 
ATOM   3226 C  CB  . LEU B 1 129 ? 23.890  -1.263  7.087   1.00 26.54  ? 129  LEU B CB  1 
ATOM   3227 C  CG  . LEU B 1 129 ? 22.578  -1.738  7.661   1.00 28.13  ? 129  LEU B CG  1 
ATOM   3228 C  CD1 . LEU B 1 129 ? 21.556  -0.626  7.514   1.00 36.27  ? 129  LEU B CD1 1 
ATOM   3229 C  CD2 . LEU B 1 129 ? 22.168  -3.035  6.951   1.00 17.08  ? 129  LEU B CD2 1 
ATOM   3230 N  N   . HIS B 1 130 ? 26.307  -2.683  5.345   1.00 29.76  ? 130  HIS B N   1 
ATOM   3231 C  CA  . HIS B 1 130 ? 27.424  -2.505  4.425   1.00 28.97  ? 130  HIS B CA  1 
ATOM   3232 C  C   . HIS B 1 130 ? 27.440  -1.084  3.875   1.00 32.91  ? 130  HIS B C   1 
ATOM   3233 O  O   . HIS B 1 130 ? 28.502  -0.490  3.699   1.00 31.13  ? 130  HIS B O   1 
ATOM   3234 C  CB  . HIS B 1 130 ? 27.340  -3.510  3.278   1.00 42.36  ? 130  HIS B CB  1 
ATOM   3235 C  CG  . HIS B 1 130 ? 28.337  -3.262  2.190   1.00 42.49  ? 130  HIS B CG  1 
ATOM   3236 N  ND1 . HIS B 1 130 ? 27.971  -2.838  0.930   1.00 47.02  ? 130  HIS B ND1 1 
ATOM   3237 C  CD2 . HIS B 1 130 ? 29.686  -3.367  2.178   1.00 41.29  ? 130  HIS B CD2 1 
ATOM   3238 C  CE1 . HIS B 1 130 ? 29.055  -2.699  0.184   1.00 47.86  ? 130  HIS B CE1 1 
ATOM   3239 N  NE2 . HIS B 1 130 ? 30.106  -3.015  0.917   1.00 52.07  ? 130  HIS B NE2 1 
ATOM   3240 N  N   . ALA B 1 131 ? 26.254  -0.549  3.602   1.00 29.45  ? 131  ALA B N   1 
ATOM   3241 C  CA  . ALA B 1 131 ? 26.090  0.863   3.269   1.00 30.29  ? 131  ALA B CA  1 
ATOM   3242 C  C   . ALA B 1 131 ? 24.948  1.359   4.114   1.00 30.95  ? 131  ALA B C   1 
ATOM   3243 O  O   . ALA B 1 131 ? 23.897  0.736   4.149   1.00 37.75  ? 131  ALA B O   1 
ATOM   3244 C  CB  . ALA B 1 131 ? 25.770  1.034   1.797   1.00 24.21  ? 131  ALA B CB  1 
ATOM   3245 N  N   . SER B 1 132 ? 25.141  2.461   4.825   1.00 35.76  ? 132  SER B N   1 
ATOM   3246 C  CA  . SER B 1 132 ? 24.105  2.899   5.748   1.00 41.50  ? 132  SER B CA  1 
ATOM   3247 C  C   . SER B 1 132 ? 22.832  3.375   5.015   1.00 42.95  ? 132  SER B C   1 
ATOM   3248 O  O   . SER B 1 132 ? 21.755  3.450   5.626   1.00 35.04  ? 132  SER B O   1 
ATOM   3249 C  CB  . SER B 1 132 ? 24.643  3.960   6.715   1.00 38.45  ? 132  SER B CB  1 
ATOM   3250 O  OG  . SER B 1 132 ? 24.899  5.178   6.047   1.00 43.75  ? 132  SER B OG  1 
ATOM   3251 N  N   . GLN B 1 133 ? 22.953  3.673   3.714   1.00 27.20  ? 133  GLN B N   1 
ATOM   3252 C  CA  . GLN B 1 133 ? 21.781  4.003   2.895   1.00 22.25  ? 133  GLN B CA  1 
ATOM   3253 C  C   . GLN B 1 133 ? 20.719  2.915   2.931   1.00 23.34  ? 133  GLN B C   1 
ATOM   3254 O  O   . GLN B 1 133 ? 19.563  3.138   2.579   1.00 31.04  ? 133  GLN B O   1 
ATOM   3255 C  CB  . GLN B 1 133 ? 22.162  4.281   1.445   1.00 31.30  ? 133  GLN B CB  1 
ATOM   3256 C  CG  . GLN B 1 133 ? 22.777  5.656   1.211   1.00 29.02  ? 133  GLN B CG  1 
ATOM   3257 C  CD  . GLN B 1 133 ? 24.257  5.680   1.522   1.00 41.82  ? 133  GLN B CD  1 
ATOM   3258 O  OE1 . GLN B 1 133 ? 24.862  4.650   1.827   1.00 40.33  ? 133  GLN B OE1 1 
ATOM   3259 N  NE2 . GLN B 1 133 ? 24.852  6.859   1.437   1.00 35.34  ? 133  GLN B NE2 1 
ATOM   3260 N  N   . ILE B 1 134 ? 21.112  1.733   3.370   1.00 22.77  ? 134  ILE B N   1 
ATOM   3261 C  CA  . ILE B 1 134 ? 20.209  0.604   3.359   1.00 23.97  ? 134  ILE B CA  1 
ATOM   3262 C  C   . ILE B 1 134 ? 19.071  0.822   4.363   1.00 30.79  ? 134  ILE B C   1 
ATOM   3263 O  O   . ILE B 1 134 ? 17.991  0.247   4.232   1.00 30.27  ? 134  ILE B O   1 
ATOM   3264 C  CB  . ILE B 1 134 ? 21.000  -0.690  3.604   1.00 26.90  ? 134  ILE B CB  1 
ATOM   3265 C  CG1 . ILE B 1 134 ? 21.965  -0.888  2.437   1.00 23.58  ? 134  ILE B CG1 1 
ATOM   3266 C  CG2 . ILE B 1 134 ? 20.069  -1.893  3.803   1.00 18.29  ? 134  ILE B CG2 1 
ATOM   3267 C  CD1 . ILE B 1 134 ? 22.714  -2.193  2.454   1.00 18.61  ? 134  ILE B CD1 1 
ATOM   3268 N  N   . GLN B 1 135 ? 19.301  1.679   5.356   1.00 25.77  ? 135  GLN B N   1 
ATOM   3269 C  CA  . GLN B 1 135 ? 18.214  2.051   6.252   1.00 24.22  ? 135  GLN B CA  1 
ATOM   3270 C  C   . GLN B 1 135 ? 17.078  2.640   5.441   1.00 25.93  ? 135  GLN B C   1 
ATOM   3271 O  O   . GLN B 1 135 ? 15.926  2.390   5.737   1.00 29.35  ? 135  GLN B O   1 
ATOM   3272 C  CB  . GLN B 1 135 ? 18.680  3.065   7.300   1.00 21.83  ? 135  GLN B CB  1 
ATOM   3273 C  CG  . GLN B 1 135 ? 19.387  2.432   8.487   1.00 27.96  ? 135  GLN B CG  1 
ATOM   3274 C  CD  . GLN B 1 135 ? 19.403  3.349   9.713   1.00 34.09  ? 135  GLN B CD  1 
ATOM   3275 O  OE1 . GLN B 1 135 ? 18.363  3.804   10.175  1.00 36.56  ? 135  GLN B OE1 1 
ATOM   3276 N  NE2 . GLN B 1 135 ? 20.585  3.630   10.222  1.00 27.48  ? 135  GLN B NE2 1 
ATOM   3277 N  N   . GLY B 1 136 ? 17.413  3.448   4.433   1.00 28.73  ? 136  GLY B N   1 
ATOM   3278 C  CA  . GLY B 1 136 ? 16.420  4.056   3.563   1.00 27.62  ? 136  GLY B CA  1 
ATOM   3279 C  C   . GLY B 1 136 ? 15.668  3.077   2.678   1.00 25.73  ? 136  GLY B C   1 
ATOM   3280 O  O   . GLY B 1 136 ? 14.636  3.420   2.092   1.00 29.55  ? 136  GLY B O   1 
ATOM   3281 N  N   . PHE B 1 137 ? 16.174  1.851   2.570   1.00 21.94  ? 137  PHE B N   1 
ATOM   3282 C  CA  . PHE B 1 137 ? 15.467  0.821   1.824   1.00 20.38  ? 137  PHE B CA  1 
ATOM   3283 C  C   . PHE B 1 137 ? 14.170  0.403   2.501   1.00 21.36  ? 137  PHE B C   1 
ATOM   3284 O  O   . PHE B 1 137 ? 13.320  -0.240  1.878   1.00 23.18  ? 137  PHE B O   1 
ATOM   3285 C  CB  . PHE B 1 137 ? 16.390  -0.381  1.543   1.00 17.49  ? 137  PHE B CB  1 
ATOM   3286 C  CG  . PHE B 1 137 ? 17.485  -0.083  0.518   1.00 18.79  ? 137  PHE B CG  1 
ATOM   3287 C  CD1 . PHE B 1 137 ? 18.381  -1.069  0.115   1.00 16.15  ? 137  PHE B CD1 1 
ATOM   3288 C  CD2 . PHE B 1 137 ? 17.611  1.179   -0.033  1.00 16.17  ? 137  PHE B CD2 1 
ATOM   3289 C  CE1 . PHE B 1 137 ? 19.379  -0.797  -0.802  1.00 19.92  ? 137  PHE B CE1 1 
ATOM   3290 C  CE2 . PHE B 1 137 ? 18.621  1.463   -0.960  1.00 22.83  ? 137  PHE B CE2 1 
ATOM   3291 C  CZ  . PHE B 1 137 ? 19.506  0.473   -1.338  1.00 17.42  ? 137  PHE B CZ  1 
ATOM   3292 N  N   . PHE B 1 138 ? 14.014  0.777   3.781   1.00 17.80  ? 138  PHE B N   1 
ATOM   3293 C  CA  . PHE B 1 138 ? 12.794  0.458   4.556   1.00 24.49  ? 138  PHE B CA  1 
ATOM   3294 C  C   . PHE B 1 138 ? 11.977  1.691   4.833   1.00 23.55  ? 138  PHE B C   1 
ATOM   3295 O  O   . PHE B 1 138 ? 12.485  2.808   4.786   1.00 25.63  ? 138  PHE B O   1 
ATOM   3296 C  CB  . PHE B 1 138 ? 13.130  -0.102  5.946   1.00 14.68  ? 138  PHE B CB  1 
ATOM   3297 C  CG  . PHE B 1 138 ? 13.891  -1.366  5.919   1.00 25.84  ? 138  PHE B CG  1 
ATOM   3298 C  CD1 . PHE B 1 138 ? 15.273  -1.344  5.784   1.00 24.40  ? 138  PHE B CD1 1 
ATOM   3299 C  CD2 . PHE B 1 138 ? 13.236  -2.580  6.046   1.00 24.62  ? 138  PHE B CD2 1 
ATOM   3300 C  CE1 . PHE B 1 138 ? 15.976  -2.508  5.756   1.00 18.95  ? 138  PHE B CE1 1 
ATOM   3301 C  CE2 . PHE B 1 138 ? 13.935  -3.767  6.024   1.00 19.07  ? 138  PHE B CE2 1 
ATOM   3302 C  CZ  . PHE B 1 138 ? 15.307  -3.733  5.885   1.00 20.39  ? 138  PHE B CZ  1 
ATOM   3303 N  N   . ASP B 1 139 ? 10.723  1.486   5.210   1.00 24.98  ? 139  ASP B N   1 
ATOM   3304 C  CA  . ASP B 1 139 ? 9.947   2.577   5.777   1.00 31.35  ? 139  ASP B CA  1 
ATOM   3305 C  C   . ASP B 1 139 ? 9.741   2.414   7.285   1.00 33.14  ? 139  ASP B C   1 
ATOM   3306 O  O   . ASP B 1 139 ? 9.408   3.371   7.979   1.00 44.69  ? 139  ASP B O   1 
ATOM   3307 C  CB  . ASP B 1 139 ? 8.624   2.745   5.033   1.00 38.21  ? 139  ASP B CB  1 
ATOM   3308 C  CG  . ASP B 1 139 ? 8.813   3.386   3.657   1.00 45.65  ? 139  ASP B CG  1 
ATOM   3309 O  OD1 . ASP B 1 139 ? 9.519   4.419   3.551   1.00 47.63  ? 139  ASP B OD1 1 
ATOM   3310 O  OD2 . ASP B 1 139 ? 8.267   2.850   2.678   1.00 43.17  ? 139  ASP B OD2 1 
ATOM   3311 N  N   . ILE B 1 140 ? 9.961   1.200   7.783   1.00 32.80  ? 140  ILE B N   1 
ATOM   3312 C  CA  . ILE B 1 140 ? 9.917   0.907   9.216   1.00 23.68  ? 140  ILE B CA  1 
ATOM   3313 C  C   . ILE B 1 140 ? 11.222  1.356   9.840   1.00 27.01  ? 140  ILE B C   1 
ATOM   3314 O  O   . ILE B 1 140 ? 12.231  1.511   9.140   1.00 21.65  ? 140  ILE B O   1 
ATOM   3315 C  CB  . ILE B 1 140 ? 9.770   -0.610  9.460   1.00 21.35  ? 140  ILE B CB  1 
ATOM   3316 C  CG1 . ILE B 1 140 ? 10.811  -1.368  8.623   1.00 24.74  ? 140  ILE B CG1 1 
ATOM   3317 C  CG2 . ILE B 1 140 ? 8.367   -1.064  9.115   1.00 19.42  ? 140  ILE B CG2 1 
ATOM   3318 C  CD1 . ILE B 1 140 ? 10.817  -2.884  8.802   1.00 18.11  ? 140  ILE B CD1 1 
ATOM   3319 N  N   . PRO B 1 141 ? 11.224  1.547   11.166  1.00 28.18  ? 141  PRO B N   1 
ATOM   3320 C  CA  . PRO B 1 141 ? 12.467  1.928   11.844  1.00 21.09  ? 141  PRO B CA  1 
ATOM   3321 C  C   . PRO B 1 141 ? 13.542  0.836   11.769  1.00 20.37  ? 141  PRO B C   1 
ATOM   3322 O  O   . PRO B 1 141 ? 13.261  -0.359  11.855  1.00 19.88  ? 141  PRO B O   1 
ATOM   3323 C  CB  . PRO B 1 141 ? 12.015  2.196   13.295  1.00 19.99  ? 141  PRO B CB  1 
ATOM   3324 C  CG  . PRO B 1 141 ? 10.754  1.452   13.426  1.00 23.31  ? 141  PRO B CG  1 
ATOM   3325 C  CD  . PRO B 1 141 ? 10.085  1.513   12.093  1.00 31.04  ? 141  PRO B CD  1 
ATOM   3326 N  N   . VAL B 1 142 ? 14.783  1.271   11.561  1.00 24.66  ? 142  VAL B N   1 
ATOM   3327 C  CA  . VAL B 1 142 ? 15.942  0.389   11.554  1.00 20.20  ? 142  VAL B CA  1 
ATOM   3328 C  C   . VAL B 1 142 ? 16.945  0.937   12.577  1.00 28.13  ? 142  VAL B C   1 
ATOM   3329 O  O   . VAL B 1 142 ? 17.217  2.134   12.614  1.00 24.79  ? 142  VAL B O   1 
ATOM   3330 C  CB  . VAL B 1 142 ? 16.629  0.324   10.153  1.00 24.03  ? 142  VAL B CB  1 
ATOM   3331 C  CG1 . VAL B 1 142 ? 17.917  -0.505  10.232  1.00 15.31  ? 142  VAL B CG1 1 
ATOM   3332 C  CG2 . VAL B 1 142 ? 15.680  -0.244  9.064   1.00 18.49  ? 142  VAL B CG2 1 
ATOM   3333 N  N   . ASP B 1 143 ? 17.465  0.078   13.437  1.00 26.31  ? 143  ASP B N   1 
ATOM   3334 C  CA  . ASP B 1 143 ? 18.584  0.477   14.279  1.00 25.64  ? 143  ASP B CA  1 
ATOM   3335 C  C   . ASP B 1 143 ? 19.819  -0.254  13.780  1.00 22.59  ? 143  ASP B C   1 
ATOM   3336 O  O   . ASP B 1 143 ? 19.891  -1.490  13.811  1.00 26.86  ? 143  ASP B O   1 
ATOM   3337 C  CB  . ASP B 1 143 ? 18.322  0.171   15.758  1.00 27.16  ? 143  ASP B CB  1 
ATOM   3338 C  CG  . ASP B 1 143 ? 17.241  1.062   16.361  1.00 32.18  ? 143  ASP B CG  1 
ATOM   3339 O  OD1 . ASP B 1 143 ? 17.336  2.300   16.219  1.00 34.80  ? 143  ASP B OD1 1 
ATOM   3340 O  OD2 . ASP B 1 143 ? 16.295  0.527   16.979  1.00 38.54  ? 143  ASP B OD2 1 
ATOM   3341 N  N   . ASN B 1 144 ? 20.775  0.524   13.294  1.00 25.80  ? 144  ASN B N   1 
ATOM   3342 C  CA  . ASN B 1 144 ? 22.000  -0.011  12.724  1.00 29.71  ? 144  ASN B CA  1 
ATOM   3343 C  C   . ASN B 1 144 ? 23.127  0.177   13.731  1.00 27.22  ? 144  ASN B C   1 
ATOM   3344 O  O   . ASN B 1 144 ? 23.727  1.233   13.798  1.00 26.35  ? 144  ASN B O   1 
ATOM   3345 C  CB  . ASN B 1 144 ? 22.311  0.696   11.393  1.00 24.11  ? 144  ASN B CB  1 
ATOM   3346 C  CG  . ASN B 1 144 ? 23.619  0.254   10.789  1.00 26.25  ? 144  ASN B CG  1 
ATOM   3347 O  OD1 . ASN B 1 144 ? 23.980  -0.921  10.833  1.00 29.57  ? 144  ASN B OD1 1 
ATOM   3348 N  ND2 . ASN B 1 144 ? 24.342  1.200   10.213  1.00 26.56  ? 144  ASN B ND2 1 
ATOM   3349 N  N   . LEU B 1 145 ? 23.379  -0.855  14.533  1.00 30.85  ? 145  LEU B N   1 
ATOM   3350 C  CA  . LEU B 1 145 ? 24.389  -0.808  15.579  1.00 28.69  ? 145  LEU B CA  1 
ATOM   3351 C  C   . LEU B 1 145 ? 25.780  -0.815  14.979  1.00 33.47  ? 145  LEU B C   1 
ATOM   3352 O  O   . LEU B 1 145 ? 26.011  -1.390  13.920  1.00 32.76  ? 145  LEU B O   1 
ATOM   3353 C  CB  . LEU B 1 145 ? 24.238  -2.013  16.515  1.00 33.94  ? 145  LEU B CB  1 
ATOM   3354 C  CG  . LEU B 1 145 ? 22.860  -2.228  17.138  1.00 29.79  ? 145  LEU B CG  1 
ATOM   3355 C  CD1 . LEU B 1 145 ? 22.784  -3.572  17.823  1.00 38.42  ? 145  LEU B CD1 1 
ATOM   3356 C  CD2 . LEU B 1 145 ? 22.575  -1.106  18.111  1.00 31.25  ? 145  LEU B CD2 1 
ATOM   3357 N  N   . TYR B 1 146 ? 26.713  -0.178  15.671  1.00 37.50  ? 146  TYR B N   1 
ATOM   3358 C  CA  . TYR B 1 146 ? 28.088  -0.116  15.202  1.00 29.15  ? 146  TYR B CA  1 
ATOM   3359 C  C   . TYR B 1 146 ? 28.946  -1.049  16.022  1.00 39.29  ? 146  TYR B C   1 
ATOM   3360 O  O   . TYR B 1 146 ? 28.764  -1.154  17.235  1.00 31.78  ? 146  TYR B O   1 
ATOM   3361 C  CB  . TYR B 1 146 ? 28.622  1.302   15.335  1.00 34.29  ? 146  TYR B CB  1 
ATOM   3362 C  CG  . TYR B 1 146 ? 28.104  2.228   14.277  1.00 60.28  ? 146  TYR B CG  1 
ATOM   3363 C  CD1 . TYR B 1 146 ? 27.119  3.159   14.560  1.00 70.25  ? 146  TYR B CD1 1 
ATOM   3364 C  CD2 . TYR B 1 146 ? 28.593  2.161   12.980  1.00 77.62  ? 146  TYR B CD2 1 
ATOM   3365 C  CE1 . TYR B 1 146 ? 26.644  4.010   13.580  1.00 80.63  ? 146  TYR B CE1 1 
ATOM   3366 C  CE2 . TYR B 1 146 ? 28.125  2.999   11.996  1.00 84.20  ? 146  TYR B CE2 1 
ATOM   3367 C  CZ  . TYR B 1 146 ? 27.153  3.922   12.301  1.00 87.44  ? 146  TYR B CZ  1 
ATOM   3368 O  OH  . TYR B 1 146 ? 26.694  4.763   11.318  1.00 97.21  ? 146  TYR B OH  1 
ATOM   3369 N  N   . ALA B 1 147 ? 29.869  -1.744  15.364  1.00 24.80  ? 147  ALA B N   1 
ATOM   3370 C  CA  . ALA B 1 147 ? 30.866  -2.494  16.102  1.00 34.04  ? 147  ALA B CA  1 
ATOM   3371 C  C   . ALA B 1 147 ? 32.035  -1.583  16.513  1.00 23.63  ? 147  ALA B C   1 
ATOM   3372 O  O   . ALA B 1 147 ? 32.870  -1.977  17.324  1.00 27.95  ? 147  ALA B O   1 
ATOM   3373 C  CB  . ALA B 1 147 ? 31.362  -3.695  15.279  1.00 30.15  ? 147  ALA B CB  1 
ATOM   3374 N  N   . GLU B 1 148 ? 32.077  -0.374  15.955  1.00 23.63  ? 148  GLU B N   1 
ATOM   3375 C  CA  . GLU B 1 148 ? 33.180  0.577   16.180  1.00 37.33  ? 148  GLU B CA  1 
ATOM   3376 C  C   . GLU B 1 148 ? 33.643  0.712   17.650  1.00 37.59  ? 148  GLU B C   1 
ATOM   3377 O  O   . GLU B 1 148 ? 34.834  0.564   17.939  1.00 33.87  ? 148  GLU B O   1 
ATOM   3378 C  CB  . GLU B 1 148 ? 32.839  1.942   15.587  1.00 35.58  ? 148  GLU B CB  1 
ATOM   3379 C  CG  . GLU B 1 148 ? 33.876  3.025   15.859  1.00 41.33  ? 148  GLU B CG  1 
ATOM   3380 C  CD  . GLU B 1 148 ? 33.835  4.141   14.826  1.00 47.62  ? 148  GLU B CD  1 
ATOM   3381 O  OE1 . GLU B 1 148 ? 33.158  3.950   13.795  1.00 62.78  ? 148  GLU B OE1 1 
ATOM   3382 O  OE2 . GLU B 1 148 ? 34.475  5.202   15.027  1.00 44.07  ? 148  GLU B OE2 1 
ATOM   3383 N  N   . PRO B 1 149 ? 32.706  0.985   18.581  1.00 33.99  ? 149  PRO B N   1 
ATOM   3384 C  CA  . PRO B 1 149 ? 33.161  1.069   19.974  1.00 33.71  ? 149  PRO B CA  1 
ATOM   3385 C  C   . PRO B 1 149 ? 33.920  -0.187  20.415  1.00 33.02  ? 149  PRO B C   1 
ATOM   3386 O  O   . PRO B 1 149 ? 34.947  -0.069  21.077  1.00 31.16  ? 149  PRO B O   1 
ATOM   3387 C  CB  . PRO B 1 149 ? 31.852  1.240   20.758  1.00 33.80  ? 149  PRO B CB  1 
ATOM   3388 C  CG  . PRO B 1 149 ? 30.947  1.975   19.781  1.00 27.20  ? 149  PRO B CG  1 
ATOM   3389 C  CD  . PRO B 1 149 ? 31.278  1.336   18.444  1.00 32.00  ? 149  PRO B CD  1 
ATOM   3390 N  N   . ALA B 1 150 ? 33.439  -1.368  20.032  1.00 35.75  ? 150  ALA B N   1 
ATOM   3391 C  CA  . ALA B 1 150 ? 34.062  -2.630  20.441  1.00 38.79  ? 150  ALA B CA  1 
ATOM   3392 C  C   . ALA B 1 150 ? 35.416  -2.855  19.760  1.00 41.68  ? 150  ALA B C   1 
ATOM   3393 O  O   . ALA B 1 150 ? 36.308  -3.530  20.298  1.00 42.31  ? 150  ALA B O   1 
ATOM   3394 C  CB  . ALA B 1 150 ? 33.127  -3.798  20.142  1.00 29.00  ? 150  ALA B CB  1 
ATOM   3395 N  N   . VAL B 1 151 ? 35.545  -2.307  18.560  1.00 30.43  ? 151  VAL B N   1 
ATOM   3396 C  CA  . VAL B 1 151 ? 36.766  -2.429  17.768  1.00 33.75  ? 151  VAL B CA  1 
ATOM   3397 C  C   . VAL B 1 151 ? 37.845  -1.517  18.344  1.00 31.19  ? 151  VAL B C   1 
ATOM   3398 O  O   . VAL B 1 151 ? 38.984  -1.946  18.551  1.00 35.18  ? 151  VAL B O   1 
ATOM   3399 C  CB  . VAL B 1 151 ? 36.480  -2.116  16.275  1.00 35.38  ? 151  VAL B CB  1 
ATOM   3400 C  CG1 . VAL B 1 151 ? 37.775  -1.841  15.487  1.00 28.69  ? 151  VAL B CG1 1 
ATOM   3401 C  CG2 . VAL B 1 151 ? 35.681  -3.266  15.657  1.00 31.98  ? 151  VAL B CG2 1 
ATOM   3402 N  N   . LEU B 1 152 ? 37.464  -0.270  18.635  1.00 33.06  ? 152  LEU B N   1 
ATOM   3403 C  CA  . LEU B 1 152 ? 38.373  0.697   19.251  1.00 39.22  ? 152  LEU B CA  1 
ATOM   3404 C  C   . LEU B 1 152 ? 38.892  0.195   20.598  1.00 40.08  ? 152  LEU B C   1 
ATOM   3405 O  O   . LEU B 1 152 ? 40.031  0.459   20.973  1.00 44.28  ? 152  LEU B O   1 
ATOM   3406 C  CB  . LEU B 1 152 ? 37.692  2.064   19.423  1.00 29.57  ? 152  LEU B CB  1 
ATOM   3407 C  CG  . LEU B 1 152 ? 37.358  2.880   18.166  1.00 40.09  ? 152  LEU B CG  1 
ATOM   3408 C  CD1 . LEU B 1 152 ? 36.422  4.027   18.485  1.00 32.40  ? 152  LEU B CD1 1 
ATOM   3409 C  CD2 . LEU B 1 152 ? 38.609  3.404   17.516  1.00 43.74  ? 152  LEU B CD2 1 
ATOM   3410 N  N   . LYS B 1 153 ? 38.041  -0.521  21.325  1.00 41.13  ? 153  LYS B N   1 
ATOM   3411 C  CA  . LYS B 1 153 ? 38.409  -1.107  22.607  1.00 37.93  ? 153  LYS B CA  1 
ATOM   3412 C  C   . LYS B 1 153 ? 39.379  -2.272  22.416  1.00 35.54  ? 153  LYS B C   1 
ATOM   3413 O  O   . LYS B 1 153 ? 40.378  -2.385  23.124  1.00 44.88  ? 153  LYS B O   1 
ATOM   3414 C  CB  . LYS B 1 153 ? 37.155  -1.593  23.326  1.00 35.09  ? 153  LYS B CB  1 
ATOM   3415 C  CG  . LYS B 1 153 ? 37.393  -2.192  24.701  1.00 42.30  ? 153  LYS B CG  1 
ATOM   3416 C  CD  . LYS B 1 153 ? 36.073  -2.316  25.460  1.00 46.19  ? 153  LYS B CD  1 
ATOM   3417 C  CE  . LYS B 1 153 ? 36.275  -2.901  26.842  1.00 56.44  ? 153  LYS B CE  1 
ATOM   3418 N  NZ  . LYS B 1 153 ? 36.804  -4.285  26.760  1.00 64.33  ? 153  LYS B NZ  1 
ATOM   3419 N  N   . TRP B 1 154 ? 39.081  -3.140  21.456  1.00 31.94  ? 154  TRP B N   1 
ATOM   3420 C  CA  . TRP B 1 154 ? 39.960  -4.257  21.163  1.00 30.42  ? 154  TRP B CA  1 
ATOM   3421 C  C   . TRP B 1 154 ? 41.334  -3.716  20.742  1.00 34.37  ? 154  TRP B C   1 
ATOM   3422 O  O   . TRP B 1 154 ? 42.380  -4.239  21.150  1.00 36.20  ? 154  TRP B O   1 
ATOM   3423 C  CB  . TRP B 1 154 ? 39.358  -5.191  20.087  1.00 31.17  ? 154  TRP B CB  1 
ATOM   3424 C  CG  . TRP B 1 154 ? 40.150  -6.466  19.952  1.00 34.79  ? 154  TRP B CG  1 
ATOM   3425 C  CD1 . TRP B 1 154 ? 39.901  -7.672  20.564  1.00 28.01  ? 154  TRP B CD1 1 
ATOM   3426 C  CD2 . TRP B 1 154 ? 41.358  -6.643  19.205  1.00 31.72  ? 154  TRP B CD2 1 
ATOM   3427 N  NE1 . TRP B 1 154 ? 40.879  -8.586  20.224  1.00 30.90  ? 154  TRP B NE1 1 
ATOM   3428 C  CE2 . TRP B 1 154 ? 41.778  -7.976  19.389  1.00 31.29  ? 154  TRP B CE2 1 
ATOM   3429 C  CE3 . TRP B 1 154 ? 42.124  -5.803  18.395  1.00 34.86  ? 154  TRP B CE3 1 
ATOM   3430 C  CZ2 . TRP B 1 154 ? 42.921  -8.478  18.792  1.00 35.96  ? 154  TRP B CZ2 1 
ATOM   3431 C  CZ3 . TRP B 1 154 ? 43.250  -6.304  17.806  1.00 34.31  ? 154  TRP B CZ3 1 
ATOM   3432 C  CH2 . TRP B 1 154 ? 43.644  -7.627  18.008  1.00 34.38  ? 154  TRP B CH2 1 
ATOM   3433 N  N   . ILE B 1 155 ? 41.331  -2.651  19.946  1.00 30.18  ? 155  ILE B N   1 
ATOM   3434 C  CA  . ILE B 1 155 ? 42.580  -2.079  19.459  1.00 28.98  ? 155  ILE B CA  1 
ATOM   3435 C  C   . ILE B 1 155 ? 43.405  -1.534  20.617  1.00 34.49  ? 155  ILE B C   1 
ATOM   3436 O  O   . ILE B 1 155 ? 44.570  -1.895  20.772  1.00 31.29  ? 155  ILE B O   1 
ATOM   3437 C  CB  . ILE B 1 155 ? 42.347  -0.968  18.438  1.00 27.24  ? 155  ILE B CB  1 
ATOM   3438 C  CG1 . ILE B 1 155 ? 41.765  -1.550  17.135  1.00 28.47  ? 155  ILE B CG1 1 
ATOM   3439 C  CG2 . ILE B 1 155 ? 43.650  -0.219  18.161  1.00 25.44  ? 155  ILE B CG2 1 
ATOM   3440 C  CD1 . ILE B 1 155 ? 41.385  -0.482  16.109  1.00 25.81  ? 155  ILE B CD1 1 
ATOM   3441 N  N   . ARG B 1 156 ? 42.800  -0.678  21.436  1.00 31.55  ? 156  ARG B N   1 
ATOM   3442 C  CA  . ARG B 1 156 ? 43.515  -0.101  22.577  1.00 35.77  ? 156  ARG B CA  1 
ATOM   3443 C  C   . ARG B 1 156 ? 44.052  -1.152  23.546  1.00 36.81  ? 156  ARG B C   1 
ATOM   3444 O  O   . ARG B 1 156 ? 45.047  -0.908  24.230  1.00 48.06  ? 156  ARG B O   1 
ATOM   3445 C  CB  . ARG B 1 156 ? 42.640  0.891   23.340  1.00 26.67  ? 156  ARG B CB  1 
ATOM   3446 C  CG  . ARG B 1 156 ? 42.380  2.195   22.626  1.00 24.89  ? 156  ARG B CG  1 
ATOM   3447 C  CD  . ARG B 1 156 ? 41.614  3.117   23.553  1.00 38.70  ? 156  ARG B CD  1 
ATOM   3448 N  NE  . ARG B 1 156 ? 41.196  4.346   22.896  1.00 49.08  ? 156  ARG B NE  1 
ATOM   3449 C  CZ  . ARG B 1 156 ? 39.950  4.583   22.507  1.00 53.90  ? 156  ARG B CZ  1 
ATOM   3450 N  NH1 . ARG B 1 156 ? 39.006  3.669   22.721  1.00 52.19  ? 156  ARG B NH1 1 
ATOM   3451 N  NH2 . ARG B 1 156 ? 39.647  5.732   21.915  1.00 52.34  ? 156  ARG B NH2 1 
ATOM   3452 N  N   . GLU B 1 157 ? 43.412  -2.320  23.599  1.00 43.01  ? 157  GLU B N   1 
ATOM   3453 C  CA  . GLU B 1 157 ? 43.797  -3.366  24.554  1.00 36.64  ? 157  GLU B CA  1 
ATOM   3454 C  C   . GLU B 1 157 ? 44.704  -4.465  23.984  1.00 44.51  ? 157  GLU B C   1 
ATOM   3455 O  O   . GLU B 1 157 ? 45.350  -5.192  24.744  1.00 37.66  ? 157  GLU B O   1 
ATOM   3456 C  CB  . GLU B 1 157 ? 42.561  -4.010  25.196  1.00 34.49  ? 157  GLU B CB  1 
ATOM   3457 C  CG  . GLU B 1 157 ? 41.703  -3.047  25.996  1.00 53.32  ? 157  GLU B CG  1 
ATOM   3458 C  CD  . GLU B 1 157 ? 40.473  -3.704  26.601  1.00 65.03  ? 157  GLU B CD  1 
ATOM   3459 O  OE1 . GLU B 1 157 ? 40.257  -4.916  26.375  1.00 63.09  ? 157  GLU B OE1 1 
ATOM   3460 O  OE2 . GLU B 1 157 ? 39.721  -2.996  27.307  1.00 74.27  ? 157  GLU B OE2 1 
ATOM   3461 N  N   . ASN B 1 158 ? 44.776  -4.595  22.663  1.00 41.28  ? 158  ASN B N   1 
ATOM   3462 C  CA  . ASN B 1 158 ? 45.576  -5.688  22.103  1.00 38.23  ? 158  ASN B CA  1 
ATOM   3463 C  C   . ASN B 1 158 ? 46.769  -5.237  21.265  1.00 33.47  ? 158  ASN B C   1 
ATOM   3464 O  O   . ASN B 1 158 ? 47.625  -6.042  20.904  1.00 37.61  ? 158  ASN B O   1 
ATOM   3465 C  CB  . ASN B 1 158 ? 44.694  -6.675  21.325  1.00 42.52  ? 158  ASN B CB  1 
ATOM   3466 C  CG  . ASN B 1 158 ? 43.571  -7.246  22.174  1.00 47.41  ? 158  ASN B CG  1 
ATOM   3467 O  OD1 . ASN B 1 158 ? 43.590  -8.418  22.534  1.00 52.09  ? 158  ASN B OD1 1 
ATOM   3468 N  ND2 . ASN B 1 158 ? 42.587  -6.415  22.497  1.00 43.23  ? 158  ASN B ND2 1 
ATOM   3469 N  N   . ILE B 1 159 ? 46.830  -3.947  20.965  1.00 30.44  ? 159  ILE B N   1 
ATOM   3470 C  CA  . ILE B 1 159 ? 47.920  -3.429  20.150  1.00 34.52  ? 159  ILE B CA  1 
ATOM   3471 C  C   . ILE B 1 159 ? 48.682  -2.334  20.878  1.00 32.90  ? 159  ILE B C   1 
ATOM   3472 O  O   . ILE B 1 159 ? 48.226  -1.189  20.948  1.00 29.69  ? 159  ILE B O   1 
ATOM   3473 C  CB  . ILE B 1 159 ? 47.410  -2.895  18.795  1.00 39.09  ? 159  ILE B CB  1 
ATOM   3474 C  CG1 . ILE B 1 159 ? 46.769  -4.033  17.996  1.00 35.27  ? 159  ILE B CG1 1 
ATOM   3475 C  CG2 . ILE B 1 159 ? 48.554  -2.243  18.011  1.00 24.74  ? 159  ILE B CG2 1 
ATOM   3476 C  CD1 . ILE B 1 159 ? 45.816  -3.541  16.938  1.00 40.06  ? 159  ILE B CD1 1 
ATOM   3477 N  N   . SER B 1 160 ? 49.843  -2.704  21.424  1.00 43.59  ? 160  SER B N   1 
ATOM   3478 C  CA  . SER B 1 160 ? 50.685  -1.793  22.204  1.00 42.56  ? 160  SER B CA  1 
ATOM   3479 C  C   . SER B 1 160 ? 50.874  -0.458  21.485  1.00 40.55  ? 160  SER B C   1 
ATOM   3480 O  O   . SER B 1 160 ? 50.852  0.611   22.091  1.00 37.55  ? 160  SER B O   1 
ATOM   3481 C  CB  . SER B 1 160 ? 52.053  -2.435  22.428  1.00 47.39  ? 160  SER B CB  1 
ATOM   3482 O  OG  . SER B 1 160 ? 51.921  -3.784  22.846  1.00 52.44  ? 160  SER B OG  1 
ATOM   3483 N  N   . GLU B 1 161 ? 51.031  -0.544  20.172  1.00 40.07  ? 161  GLU B N   1 
ATOM   3484 C  CA  . GLU B 1 161 ? 51.436  0.587   19.368  1.00 41.98  ? 161  GLU B CA  1 
ATOM   3485 C  C   . GLU B 1 161 ? 50.250  1.355   18.814  1.00 38.92  ? 161  GLU B C   1 
ATOM   3486 O  O   . GLU B 1 161 ? 50.407  2.139   17.880  1.00 39.14  ? 161  GLU B O   1 
ATOM   3487 C  CB  . GLU B 1 161 ? 52.317  0.100   18.213  1.00 48.09  ? 161  GLU B CB  1 
ATOM   3488 C  CG  . GLU B 1 161 ? 53.458  -0.821  18.628  1.00 54.07  ? 161  GLU B CG  1 
ATOM   3489 C  CD  . GLU B 1 161 ? 53.068  -2.299  18.696  1.00 65.33  ? 161  GLU B CD  1 
ATOM   3490 O  OE1 . GLU B 1 161 ? 51.893  -2.624  18.970  1.00 62.11  ? 161  GLU B OE1 1 
ATOM   3491 O  OE2 . GLU B 1 161 ? 53.958  -3.149  18.472  1.00 74.03  ? 161  GLU B OE2 1 
ATOM   3492 N  N   . TRP B 1 162 ? 49.062  1.152   19.380  1.00 35.28  ? 162  TRP B N   1 
ATOM   3493 C  CA  . TRP B 1 162 ? 47.871  1.732   18.760  1.00 39.71  ? 162  TRP B CA  1 
ATOM   3494 C  C   . TRP B 1 162 ? 47.978  3.240   18.622  1.00 40.14  ? 162  TRP B C   1 
ATOM   3495 O  O   . TRP B 1 162 ? 47.368  3.827   17.732  1.00 38.47  ? 162  TRP B O   1 
ATOM   3496 C  CB  . TRP B 1 162 ? 46.574  1.344   19.486  1.00 41.26  ? 162  TRP B CB  1 
ATOM   3497 C  CG  . TRP B 1 162 ? 46.412  1.902   20.889  1.00 31.24  ? 162  TRP B CG  1 
ATOM   3498 C  CD1 . TRP B 1 162 ? 46.735  1.276   22.051  1.00 26.85  ? 162  TRP B CD1 1 
ATOM   3499 C  CD2 . TRP B 1 162 ? 45.854  3.176   21.260  1.00 33.00  ? 162  TRP B CD2 1 
ATOM   3500 N  NE1 . TRP B 1 162 ? 46.434  2.078   23.121  1.00 35.28  ? 162  TRP B NE1 1 
ATOM   3501 C  CE2 . TRP B 1 162 ? 45.889  3.251   22.667  1.00 43.42  ? 162  TRP B CE2 1 
ATOM   3502 C  CE3 . TRP B 1 162 ? 45.336  4.266   20.540  1.00 33.54  ? 162  TRP B CE3 1 
ATOM   3503 C  CZ2 . TRP B 1 162 ? 45.422  4.370   23.377  1.00 34.06  ? 162  TRP B CZ2 1 
ATOM   3504 C  CZ3 . TRP B 1 162 ? 44.875  5.379   21.246  1.00 35.79  ? 162  TRP B CZ3 1 
ATOM   3505 C  CH2 . TRP B 1 162 ? 44.919  5.419   22.654  1.00 24.91  ? 162  TRP B CH2 1 
ATOM   3506 N  N   . ARG B 1 163 ? 48.757  3.870   19.495  1.00 39.72  ? 163  ARG B N   1 
ATOM   3507 C  CA  . ARG B 1 163 ? 48.868  5.320   19.459  1.00 34.57  ? 163  ARG B CA  1 
ATOM   3508 C  C   . ARG B 1 163 ? 49.707  5.807   18.288  1.00 37.42  ? 163  ARG B C   1 
ATOM   3509 O  O   . ARG B 1 163 ? 49.667  6.984   17.950  1.00 42.03  ? 163  ARG B O   1 
ATOM   3510 C  CB  . ARG B 1 163 ? 49.378  5.880   20.789  1.00 35.12  ? 163  ARG B CB  1 
ATOM   3511 C  CG  . ARG B 1 163 ? 48.269  6.123   21.802  1.00 39.60  ? 163  ARG B CG  1 
ATOM   3512 C  CD  . ARG B 1 163 ? 48.804  6.600   23.165  1.00 39.14  ? 163  ARG B CD  1 
ATOM   3513 N  NE  . ARG B 1 163 ? 48.750  5.539   24.168  1.00 47.85  ? 163  ARG B NE  1 
ATOM   3514 C  CZ  . ARG B 1 163 ? 47.851  5.483   25.148  1.00 57.80  ? 163  ARG B CZ  1 
ATOM   3515 N  NH1 . ARG B 1 163 ? 46.924  6.438   25.267  1.00 57.26  ? 163  ARG B NH1 1 
ATOM   3516 N  NH2 . ARG B 1 163 ? 47.880  4.473   26.015  1.00 51.30  ? 163  ARG B NH2 1 
ATOM   3517 N  N   . ASN B 1 164 ? 50.444  4.903   17.651  1.00 34.12  ? 164  ASN B N   1 
ATOM   3518 C  CA  . ASN B 1 164 ? 51.192  5.275   16.450  1.00 47.05  ? 164  ASN B CA  1 
ATOM   3519 C  C   . ASN B 1 164 ? 50.919  4.365   15.251  1.00 42.18  ? 164  ASN B C   1 
ATOM   3520 O  O   . ASN B 1 164 ? 51.812  4.084   14.453  1.00 36.64  ? 164  ASN B O   1 
ATOM   3521 C  CB  . ASN B 1 164 ? 52.697  5.367   16.750  1.00 47.36  ? 164  ASN B CB  1 
ATOM   3522 C  CG  . ASN B 1 164 ? 53.050  6.617   17.542  1.00 61.30  ? 164  ASN B CG  1 
ATOM   3523 O  OD1 . ASN B 1 164 ? 53.334  7.670   16.970  1.00 69.40  ? 164  ASN B OD1 1 
ATOM   3524 N  ND2 . ASN B 1 164 ? 53.013  6.510   18.868  1.00 59.83  ? 164  ASN B ND2 1 
ATOM   3525 N  N   . CYS B 1 165 ? 49.679  3.917   15.120  1.00 34.85  ? 165  CYS B N   1 
ATOM   3526 C  CA  . CYS B 1 165 ? 49.354  2.953   14.085  1.00 39.65  ? 165  CYS B CA  1 
ATOM   3527 C  C   . CYS B 1 165 ? 48.669  3.660   12.921  1.00 35.03  ? 165  CYS B C   1 
ATOM   3528 O  O   . CYS B 1 165 ? 48.373  4.854   13.013  1.00 34.05  ? 165  CYS B O   1 
ATOM   3529 C  CB  . CYS B 1 165 ? 48.467  1.846   14.655  1.00 28.43  ? 165  CYS B CB  1 
ATOM   3530 S  SG  . CYS B 1 165 ? 46.766  2.354   14.993  1.00 39.20  ? 165  CYS B SG  1 
ATOM   3531 N  N   . THR B 1 166 ? 48.432  2.939   11.826  1.00 43.01  ? 166  THR B N   1 
ATOM   3532 C  CA  . THR B 1 166 ? 47.644  3.481   10.712  1.00 35.15  ? 166  THR B CA  1 
ATOM   3533 C  C   . THR B 1 166 ? 46.449  2.581   10.437  1.00 40.28  ? 166  THR B C   1 
ATOM   3534 O  O   . THR B 1 166 ? 46.603  1.363   10.287  1.00 38.56  ? 166  THR B O   1 
ATOM   3535 C  CB  . THR B 1 166 ? 48.455  3.593   9.428   1.00 35.49  ? 166  THR B CB  1 
ATOM   3536 O  OG1 . THR B 1 166 ? 49.578  4.455   9.643   1.00 46.48  ? 166  THR B OG1 1 
ATOM   3537 C  CG2 . THR B 1 166 ? 47.595  4.168   8.293   1.00 32.72  ? 166  THR B CG2 1 
ATOM   3538 N  N   . ILE B 1 167 ? 45.264  3.185   10.392  1.00 34.27  ? 167  ILE B N   1 
ATOM   3539 C  CA  . ILE B 1 167 ? 44.054  2.472   10.007  1.00 30.29  ? 167  ILE B CA  1 
ATOM   3540 C  C   . ILE B 1 167 ? 43.933  2.495   8.483   1.00 39.13  ? 167  ILE B C   1 
ATOM   3541 O  O   . ILE B 1 167 ? 43.879  3.565   7.886   1.00 34.03  ? 167  ILE B O   1 
ATOM   3542 C  CB  . ILE B 1 167 ? 42.794  3.103   10.631  1.00 27.83  ? 167  ILE B CB  1 
ATOM   3543 C  CG1 . ILE B 1 167 ? 43.032  3.438   12.122  1.00 22.99  ? 167  ILE B CG1 1 
ATOM   3544 C  CG2 . ILE B 1 167 ? 41.570  2.182   10.434  1.00 24.81  ? 167  ILE B CG2 1 
ATOM   3545 C  CD1 . ILE B 1 167 ? 43.535  2.250   12.960  1.00 26.10  ? 167  ILE B CD1 1 
ATOM   3546 N  N   . VAL B 1 168 ? 43.894  1.312   7.870   1.00 29.13  ? 168  VAL B N   1 
ATOM   3547 C  CA  . VAL B 1 168 ? 43.874  1.179   6.422   1.00 31.10  ? 168  VAL B CA  1 
ATOM   3548 C  C   . VAL B 1 168 ? 42.545  0.650   5.903   1.00 34.68  ? 168  VAL B C   1 
ATOM   3549 O  O   . VAL B 1 168 ? 42.011  -0.333  6.420   1.00 32.05  ? 168  VAL B O   1 
ATOM   3550 C  CB  . VAL B 1 168 ? 44.953  0.195   5.936   1.00 27.51  ? 168  VAL B CB  1 
ATOM   3551 C  CG1 . VAL B 1 168 ? 45.047  0.256   4.422   1.00 29.26  ? 168  VAL B CG1 1 
ATOM   3552 C  CG2 . VAL B 1 168 ? 46.296  0.513   6.572   1.00 31.16  ? 168  VAL B CG2 1 
ATOM   3553 N  N   . SER B 1 169 ? 42.026  1.290   4.863   1.00 33.65  ? 169  SER B N   1 
ATOM   3554 C  CA  . SER B 1 169 ? 40.847  0.773   4.177   1.00 32.27  ? 169  SER B CA  1 
ATOM   3555 C  C   . SER B 1 169 ? 41.315  -0.091  3.025   1.00 28.67  ? 169  SER B C   1 
ATOM   3556 O  O   . SER B 1 169 ? 42.186  0.334   2.269   1.00 36.84  ? 169  SER B O   1 
ATOM   3557 C  CB  . SER B 1 169 ? 39.992  1.915   3.629   1.00 33.34  ? 169  SER B CB  1 
ATOM   3558 O  OG  . SER B 1 169 ? 38.810  1.395   3.053   1.00 36.36  ? 169  SER B OG  1 
ATOM   3559 N  N   . PRO B 1 170 ? 40.760  -1.311  2.889   1.00 39.45  ? 170  PRO B N   1 
ATOM   3560 C  CA  . PRO B 1 170 ? 41.174  -2.197  1.791   1.00 37.54  ? 170  PRO B CA  1 
ATOM   3561 C  C   . PRO B 1 170 ? 40.645  -1.755  0.432   1.00 39.14  ? 170  PRO B C   1 
ATOM   3562 O  O   . PRO B 1 170 ? 41.114  -2.249  -0.585  1.00 47.60  ? 170  PRO B O   1 
ATOM   3563 C  CB  . PRO B 1 170 ? 40.544  -3.537  2.162   1.00 30.79  ? 170  PRO B CB  1 
ATOM   3564 C  CG  . PRO B 1 170 ? 39.367  -3.168  2.985   1.00 34.79  ? 170  PRO B CG  1 
ATOM   3565 C  CD  . PRO B 1 170 ? 39.795  -1.974  3.784   1.00 32.84  ? 170  PRO B CD  1 
ATOM   3566 N  N   . ASP B 1 171 ? 39.681  -0.845  0.409   1.00 41.71  ? 171  ASP B N   1 
ATOM   3567 C  CA  . ASP B 1 171 ? 39.174  -0.334  -0.862  1.00 38.53  ? 171  ASP B CA  1 
ATOM   3568 C  C   . ASP B 1 171 ? 38.875  1.150   -0.782  1.00 43.77  ? 171  ASP B C   1 
ATOM   3569 O  O   . ASP B 1 171 ? 39.030  1.776   0.267   1.00 43.85  ? 171  ASP B O   1 
ATOM   3570 C  CB  . ASP B 1 171 ? 37.925  -1.095  -1.310  1.00 38.81  ? 171  ASP B CB  1 
ATOM   3571 C  CG  . ASP B 1 171 ? 36.801  -1.041  -0.284  1.00 57.45  ? 171  ASP B CG  1 
ATOM   3572 O  OD1 . ASP B 1 171 ? 36.811  -0.126  0.572   1.00 69.15  ? 171  ASP B OD1 1 
ATOM   3573 O  OD2 . ASP B 1 171 ? 35.904  -1.914  -0.335  1.00 59.64  ? 171  ASP B OD2 1 
ATOM   3574 N  N   . ALA B 1 172 ? 38.434  1.698   -1.908  1.00 49.13  ? 172  ALA B N   1 
ATOM   3575 C  CA  . ALA B 1 172 ? 38.131  3.115   -2.020  1.00 55.57  ? 172  ALA B CA  1 
ATOM   3576 C  C   . ALA B 1 172 ? 36.913  3.493   -1.180  1.00 51.67  ? 172  ALA B C   1 
ATOM   3577 O  O   . ALA B 1 172 ? 36.916  4.498   -0.468  1.00 47.27  ? 172  ALA B O   1 
ATOM   3578 C  CB  . ALA B 1 172 ? 37.905  3.475   -3.487  1.00 69.17  ? 172  ALA B CB  1 
ATOM   3579 N  N   . GLY B 1 173 ? 35.875  2.672   -1.255  1.00 56.83  ? 173  GLY B N   1 
ATOM   3580 C  CA  . GLY B 1 173 ? 34.640  2.953   -0.550  1.00 60.11  ? 173  GLY B CA  1 
ATOM   3581 C  C   . GLY B 1 173 ? 34.619  2.616   0.931   1.00 57.87  ? 173  GLY B C   1 
ATOM   3582 O  O   . GLY B 1 173 ? 33.549  2.362   1.491   1.00 59.19  ? 173  GLY B O   1 
ATOM   3583 N  N   . GLY B 1 174 ? 35.786  2.606   1.569   1.00 46.36  ? 174  GLY B N   1 
ATOM   3584 C  CA  . GLY B 1 174 ? 35.861  2.329   2.995   1.00 35.04  ? 174  GLY B CA  1 
ATOM   3585 C  C   . GLY B 1 174 ? 36.522  3.462   3.763   1.00 31.59  ? 174  GLY B C   1 
ATOM   3586 O  O   . GLY B 1 174 ? 36.761  3.354   4.958   1.00 43.01  ? 174  GLY B O   1 
ATOM   3587 N  N   . ALA B 1 175 ? 36.818  4.552   3.062   1.00 33.47  ? 175  ALA B N   1 
ATOM   3588 C  CA  . ALA B 1 175 ? 37.542  5.669   3.648   1.00 41.68  ? 175  ALA B CA  1 
ATOM   3589 C  C   . ALA B 1 175 ? 36.857  6.186   4.895   1.00 49.01  ? 175  ALA B C   1 
ATOM   3590 O  O   . ALA B 1 175 ? 37.457  6.246   5.962   1.00 54.44  ? 175  ALA B O   1 
ATOM   3591 C  CB  . ALA B 1 175 ? 37.684  6.797   2.636   1.00 30.86  ? 175  ALA B CB  1 
ATOM   3592 N  N   . LYS B 1 176 ? 35.600  6.583   4.744   1.00 56.42  ? 176  LYS B N   1 
ATOM   3593 C  CA  . LYS B 1 176 ? 34.842  7.185   5.832   1.00 48.70  ? 176  LYS B CA  1 
ATOM   3594 C  C   . LYS B 1 176 ? 35.002  6.359   7.105   1.00 42.05  ? 176  LYS B C   1 
ATOM   3595 O  O   . LYS B 1 176 ? 35.396  6.875   8.151   1.00 45.82  ? 176  LYS B O   1 
ATOM   3596 C  CB  . LYS B 1 176 ? 33.365  7.325   5.431   1.00 44.11  ? 176  LYS B CB  1 
ATOM   3597 N  N   . ARG B 1 177 ? 34.738  5.062   7.009   1.00 37.33  ? 177  ARG B N   1 
ATOM   3598 C  CA  . ARG B 1 177 ? 34.892  4.185   8.157   1.00 45.33  ? 177  ARG B CA  1 
ATOM   3599 C  C   . ARG B 1 177 ? 36.269  4.290   8.808   1.00 46.08  ? 177  ARG B C   1 
ATOM   3600 O  O   . ARG B 1 177 ? 36.365  4.470   10.023  1.00 42.10  ? 177  ARG B O   1 
ATOM   3601 C  CB  . ARG B 1 177 ? 34.601  2.738   7.777   1.00 53.08  ? 177  ARG B CB  1 
ATOM   3602 C  CG  . ARG B 1 177 ? 34.800  1.763   8.917   1.00 59.63  ? 177  ARG B CG  1 
ATOM   3603 C  CD  . ARG B 1 177 ? 34.911  0.340   8.394   1.00 66.12  ? 177  ARG B CD  1 
ATOM   3604 N  NE  . ARG B 1 177 ? 34.091  0.145   7.204   1.00 64.18  ? 177  ARG B NE  1 
ATOM   3605 C  CZ  . ARG B 1 177 ? 32.774  -0.023  7.225   1.00 72.28  ? 177  ARG B CZ  1 
ATOM   3606 N  NH1 . ARG B 1 177 ? 32.122  -0.015  8.385   1.00 67.43  ? 177  ARG B NH1 1 
ATOM   3607 N  NH2 . ARG B 1 177 ? 32.111  -0.194  6.084   1.00 77.03  ? 177  ARG B NH2 1 
ATOM   3608 N  N   . VAL B 1 178 ? 37.337  4.179   8.021   1.00 41.45  ? 178  VAL B N   1 
ATOM   3609 C  CA  . VAL B 1 178 ? 38.670  4.209   8.627   1.00 35.82  ? 178  VAL B CA  1 
ATOM   3610 C  C   . VAL B 1 178 ? 39.084  5.584   9.117   1.00 34.83  ? 178  VAL B C   1 
ATOM   3611 O  O   . VAL B 1 178 ? 39.740  5.689   10.146  1.00 38.81  ? 178  VAL B O   1 
ATOM   3612 C  CB  . VAL B 1 178 ? 39.786  3.599   7.735   1.00 40.36  ? 178  VAL B CB  1 
ATOM   3613 C  CG1 . VAL B 1 178 ? 39.417  2.187   7.318   1.00 31.23  ? 178  VAL B CG1 1 
ATOM   3614 C  CG2 . VAL B 1 178 ? 40.085  4.483   6.536   1.00 33.63  ? 178  VAL B CG2 1 
ATOM   3615 N  N   . THR B 1 179 ? 38.723  6.632   8.378   1.00 33.05  ? 179  THR B N   1 
ATOM   3616 C  CA  . THR B 1 179 ? 39.028  7.988   8.818   1.00 42.36  ? 179  THR B CA  1 
ATOM   3617 C  C   . THR B 1 179 ? 38.339  8.271   10.152  1.00 43.02  ? 179  THR B C   1 
ATOM   3618 O  O   . THR B 1 179 ? 38.905  8.914   11.038  1.00 42.12  ? 179  THR B O   1 
ATOM   3619 C  CB  . THR B 1 179 ? 38.613  9.070   7.782   1.00 47.22  ? 179  THR B CB  1 
ATOM   3620 O  OG1 . THR B 1 179 ? 37.223  8.939   7.458   1.00 44.72  ? 179  THR B OG1 1 
ATOM   3621 C  CG2 . THR B 1 179 ? 39.452  8.969   6.522   1.00 40.08  ? 179  THR B CG2 1 
ATOM   3622 N  N   . SER B 1 180 ? 37.119  7.778   10.294  1.00 44.17  ? 180  SER B N   1 
ATOM   3623 C  CA  . SER B 1 180 ? 36.378  7.942   11.538  1.00 43.85  ? 180  SER B CA  1 
ATOM   3624 C  C   . SER B 1 180 ? 37.104  7.253   12.693  1.00 44.28  ? 180  SER B C   1 
ATOM   3625 O  O   . SER B 1 180 ? 37.254  7.823   13.772  1.00 45.66  ? 180  SER B O   1 
ATOM   3626 C  CB  . SER B 1 180 ? 34.951  7.407   11.386  1.00 47.13  ? 180  SER B CB  1 
ATOM   3627 O  OG  . SER B 1 180 ? 34.331  7.272   12.656  1.00 58.74  ? 180  SER B OG  1 
ATOM   3628 N  N   . ILE B 1 181 ? 37.568  6.029   12.462  1.00 37.60  ? 181  ILE B N   1 
ATOM   3629 C  CA  . ILE B 1 181 ? 38.359  5.315   13.462  1.00 34.85  ? 181  ILE B CA  1 
ATOM   3630 C  C   . ILE B 1 181 ? 39.722  5.980   13.716  1.00 43.70  ? 181  ILE B C   1 
ATOM   3631 O  O   . ILE B 1 181 ? 40.151  6.104   14.866  1.00 40.58  ? 181  ILE B O   1 
ATOM   3632 C  CB  . ILE B 1 181 ? 38.544  3.831   13.074  1.00 42.26  ? 181  ILE B CB  1 
ATOM   3633 C  CG1 . ILE B 1 181 ? 37.178  3.145   12.991  1.00 48.36  ? 181  ILE B CG1 1 
ATOM   3634 C  CG2 . ILE B 1 181 ? 39.426  3.109   14.084  1.00 37.92  ? 181  ILE B CG2 1 
ATOM   3635 C  CD1 . ILE B 1 181 ? 37.215  1.768   12.371  1.00 53.54  ? 181  ILE B CD1 1 
ATOM   3636 N  N   . ALA B 1 182 ? 40.399  6.415   12.653  1.00 41.68  ? 182  ALA B N   1 
ATOM   3637 C  CA  . ALA B 1 182 ? 41.700  7.080   12.795  1.00 41.86  ? 182  ALA B CA  1 
ATOM   3638 C  C   . ALA B 1 182 ? 41.595  8.367   13.611  1.00 45.88  ? 182  ALA B C   1 
ATOM   3639 O  O   . ALA B 1 182 ? 42.432  8.645   14.467  1.00 46.51  ? 182  ALA B O   1 
ATOM   3640 C  CB  . ALA B 1 182 ? 42.316  7.364   11.440  1.00 36.79  ? 182  ALA B CB  1 
ATOM   3641 N  N   . ASP B 1 183 ? 40.556  9.147   13.347  1.00 43.97  ? 183  ASP B N   1 
ATOM   3642 C  CA  . ASP B 1 183 ? 40.320  10.370  14.107  1.00 44.05  ? 183  ASP B CA  1 
ATOM   3643 C  C   . ASP B 1 183 ? 40.006  10.108  15.593  1.00 39.50  ? 183  ASP B C   1 
ATOM   3644 O  O   . ASP B 1 183 ? 40.508  10.821  16.462  1.00 40.27  ? 183  ASP B O   1 
ATOM   3645 C  CB  . ASP B 1 183 ? 39.219  11.207  13.446  1.00 49.32  ? 183  ASP B CB  1 
ATOM   3646 C  CG  . ASP B 1 183 ? 39.672  11.853  12.131  1.00 56.18  ? 183  ASP B CG  1 
ATOM   3647 O  OD1 . ASP B 1 183 ? 40.766  11.515  11.619  1.00 48.13  ? 183  ASP B OD1 1 
ATOM   3648 O  OD2 . ASP B 1 183 ? 38.915  12.696  11.603  1.00 62.19  ? 183  ASP B OD2 1 
ATOM   3649 N  N   . ARG B 1 184 ? 39.183  9.099   15.882  1.00 31.97  ? 184  ARG B N   1 
ATOM   3650 C  CA  . ARG B 1 184 ? 38.902  8.723   17.276  1.00 41.58  ? 184  ARG B CA  1 
ATOM   3651 C  C   . ARG B 1 184 ? 40.176  8.338   18.026  1.00 47.91  ? 184  ARG B C   1 
ATOM   3652 O  O   . ARG B 1 184 ? 40.445  8.843   19.111  1.00 52.87  ? 184  ARG B O   1 
ATOM   3653 C  CB  . ARG B 1 184 ? 37.872  7.592   17.364  1.00 42.68  ? 184  ARG B CB  1 
ATOM   3654 C  CG  . ARG B 1 184 ? 36.439  8.049   17.074  1.00 56.95  ? 184  ARG B CG  1 
ATOM   3655 C  CD  . ARG B 1 184 ? 35.440  7.486   18.080  1.00 55.46  ? 184  ARG B CD  1 
ATOM   3656 N  N   . LEU B 1 185 ? 40.966  7.453   17.434  1.00 43.18  ? 185  LEU B N   1 
ATOM   3657 C  CA  . LEU B 1 185 ? 42.237  7.057   18.014  1.00 40.03  ? 185  LEU B CA  1 
ATOM   3658 C  C   . LEU B 1 185 ? 43.276  8.171   17.892  1.00 48.40  ? 185  LEU B C   1 
ATOM   3659 O  O   . LEU B 1 185 ? 44.316  8.135   18.549  1.00 48.09  ? 185  LEU B O   1 
ATOM   3660 C  CB  . LEU B 1 185 ? 42.749  5.796   17.321  1.00 27.63  ? 185  LEU B CB  1 
ATOM   3661 C  CG  . LEU B 1 185 ? 41.875  4.566   17.537  1.00 40.37  ? 185  LEU B CG  1 
ATOM   3662 C  CD1 . LEU B 1 185 ? 42.427  3.344   16.789  1.00 38.31  ? 185  LEU B CD1 1 
ATOM   3663 C  CD2 . LEU B 1 185 ? 41.741  4.293   19.037  1.00 39.75  ? 185  LEU B CD2 1 
ATOM   3664 N  N   . ASN B 1 186 ? 42.988  9.156   17.045  1.00 46.65  ? 186  ASN B N   1 
ATOM   3665 C  CA  . ASN B 1 186 ? 43.955  10.203  16.707  1.00 44.32  ? 186  ASN B CA  1 
ATOM   3666 C  C   . ASN B 1 186 ? 45.230  9.625   16.094  1.00 42.89  ? 186  ASN B C   1 
ATOM   3667 O  O   . ASN B 1 186 ? 46.331  9.870   16.576  1.00 37.45  ? 186  ASN B O   1 
ATOM   3668 C  CB  . ASN B 1 186 ? 44.282  11.087  17.919  1.00 46.27  ? 186  ASN B CB  1 
ATOM   3669 C  CG  . ASN B 1 186 ? 45.085  12.328  17.541  1.00 54.31  ? 186  ASN B CG  1 
ATOM   3670 O  OD1 . ASN B 1 186 ? 46.197  12.547  18.039  1.00 47.83  ? 186  ASN B OD1 1 
ATOM   3671 N  ND2 . ASN B 1 186 ? 44.531  13.138  16.637  1.00 55.58  ? 186  ASN B ND2 1 
ATOM   3672 N  N   . VAL B 1 187 ? 45.070  8.850   15.025  1.00 43.68  ? 187  VAL B N   1 
ATOM   3673 C  CA  . VAL B 1 187 ? 46.211  8.347   14.277  1.00 33.08  ? 187  VAL B CA  1 
ATOM   3674 C  C   . VAL B 1 187 ? 46.071  8.611   12.778  1.00 35.55  ? 187  VAL B C   1 
ATOM   3675 O  O   . VAL B 1 187 ? 45.213  9.388   12.341  1.00 38.41  ? 187  VAL B O   1 
ATOM   3676 C  CB  . VAL B 1 187 ? 46.416  6.848   14.527  1.00 38.42  ? 187  VAL B CB  1 
ATOM   3677 C  CG1 . VAL B 1 187 ? 46.603  6.607   15.994  1.00 32.71  ? 187  VAL B CG1 1 
ATOM   3678 C  CG2 . VAL B 1 187 ? 45.210  6.045   14.001  1.00 40.46  ? 187  VAL B CG2 1 
ATOM   3679 N  N   . ASP B 1 188 ? 46.924  7.957   11.999  1.00 36.18  ? 188  ASP B N   1 
ATOM   3680 C  CA  . ASP B 1 188 ? 46.906  8.082   10.548  1.00 34.04  ? 188  ASP B CA  1 
ATOM   3681 C  C   . ASP B 1 188 ? 45.939  7.088   9.944   1.00 29.54  ? 188  ASP B C   1 
ATOM   3682 O  O   . ASP B 1 188 ? 45.549  6.107   10.583  1.00 33.09  ? 188  ASP B O   1 
ATOM   3683 C  CB  . ASP B 1 188 ? 48.302  7.836   9.969   1.00 48.22  ? 188  ASP B CB  1 
ATOM   3684 C  CG  . ASP B 1 188 ? 49.330  8.845   10.457  1.00 54.01  ? 188  ASP B CG  1 
ATOM   3685 O  OD1 . ASP B 1 188 ? 48.940  9.973   10.812  1.00 52.02  ? 188  ASP B OD1 1 
ATOM   3686 O  OD2 . ASP B 1 188 ? 50.531  8.515   10.477  1.00 58.80  ? 188  ASP B OD2 1 
ATOM   3687 N  N   . PHE B 1 189 ? 45.547  7.344   8.705   1.00 33.90  ? 189  PHE B N   1 
ATOM   3688 C  CA  . PHE B 1 189 ? 44.733  6.393   7.965   1.00 37.51  ? 189  PHE B CA  1 
ATOM   3689 C  C   . PHE B 1 189 ? 45.372  6.278   6.600   1.00 36.44  ? 189  PHE B C   1 
ATOM   3690 O  O   . PHE B 1 189 ? 46.139  7.149   6.195   1.00 34.94  ? 189  PHE B O   1 
ATOM   3691 C  CB  . PHE B 1 189 ? 43.289  6.889   7.819   1.00 34.70  ? 189  PHE B CB  1 
ATOM   3692 C  CG  . PHE B 1 189 ? 43.123  7.934   6.754   1.00 38.20  ? 189  PHE B CG  1 
ATOM   3693 C  CD1 . PHE B 1 189 ? 42.836  7.571   5.445   1.00 34.91  ? 189  PHE B CD1 1 
ATOM   3694 C  CD2 . PHE B 1 189 ? 43.267  9.277   7.053   1.00 37.41  ? 189  PHE B CD2 1 
ATOM   3695 C  CE1 . PHE B 1 189 ? 42.695  8.535   4.456   1.00 40.06  ? 189  PHE B CE1 1 
ATOM   3696 C  CE2 . PHE B 1 189 ? 43.130  10.247  6.066   1.00 40.63  ? 189  PHE B CE2 1 
ATOM   3697 C  CZ  . PHE B 1 189 ? 42.843  9.876   4.773   1.00 40.19  ? 189  PHE B CZ  1 
ATOM   3698 N  N   . ALA B 1 190 ? 45.056  5.205   5.892   1.00 33.07  ? 190  ALA B N   1 
ATOM   3699 C  CA  . ALA B 1 190 ? 45.579  5.000   4.555   1.00 33.77  ? 190  ALA B CA  1 
ATOM   3700 C  C   . ALA B 1 190 ? 44.553  4.192   3.790   1.00 32.52  ? 190  ALA B C   1 
ATOM   3701 O  O   . ALA B 1 190 ? 43.662  3.577   4.393   1.00 36.26  ? 190  ALA B O   1 
ATOM   3702 C  CB  . ALA B 1 190 ? 46.914  4.273   4.595   1.00 24.56  ? 190  ALA B CB  1 
ATOM   3703 N  N   . LEU B 1 191 ? 44.669  4.203   2.466   1.00 31.07  ? 191  LEU B N   1 
ATOM   3704 C  CA  . LEU B 1 191 ? 43.688  3.550   1.613   1.00 32.55  ? 191  LEU B CA  1 
ATOM   3705 C  C   . LEU B 1 191 ? 44.361  2.724   0.551   1.00 31.48  ? 191  LEU B C   1 
ATOM   3706 O  O   . LEU B 1 191 ? 45.286  3.181   -0.108  1.00 44.26  ? 191  LEU B O   1 
ATOM   3707 C  CB  . LEU B 1 191 ? 42.817  4.579   0.902   1.00 41.16  ? 191  LEU B CB  1 
ATOM   3708 C  CG  . LEU B 1 191 ? 42.069  5.616   1.721   1.00 50.12  ? 191  LEU B CG  1 
ATOM   3709 C  CD1 . LEU B 1 191 ? 41.701  6.802   0.827   1.00 58.87  ? 191  LEU B CD1 1 
ATOM   3710 C  CD2 . LEU B 1 191 ? 40.851  4.979   2.340   1.00 51.12  ? 191  LEU B CD2 1 
ATOM   3711 N  N   . ILE B 1 192 ? 43.854  1.517   0.368   1.00 34.96  ? 192  ILE B N   1 
ATOM   3712 C  CA  . ILE B 1 192 ? 44.226  0.673   -0.742  1.00 38.44  ? 192  ILE B CA  1 
ATOM   3713 C  C   . ILE B 1 192 ? 43.169  0.849   -1.818  1.00 37.56  ? 192  ILE B C   1 
ATOM   3714 O  O   . ILE B 1 192 ? 41.993  1.001   -1.520  1.00 40.55  ? 192  ILE B O   1 
ATOM   3715 C  CB  . ILE B 1 192 ? 44.240  -0.800  -0.316  1.00 41.98  ? 192  ILE B CB  1 
ATOM   3716 C  CG1 . ILE B 1 192 ? 45.271  -1.025  0.793   1.00 39.60  ? 192  ILE B CG1 1 
ATOM   3717 C  CG2 . ILE B 1 192 ? 44.531  -1.705  -1.511  1.00 37.61  ? 192  ILE B CG2 1 
ATOM   3718 C  CD1 . ILE B 1 192 ? 46.514  -1.666  0.303   1.00 37.30  ? 192  ILE B CD1 1 
ATOM   3719 N  N   . HIS B 1 193 ? 43.593  0.825   -3.069  1.00 41.38  ? 193  HIS B N   1 
ATOM   3720 C  CA  . HIS B 1 193 ? 42.671  0.802   -4.193  1.00 36.92  ? 193  HIS B CA  1 
ATOM   3721 C  C   . HIS B 1 193 ? 43.171  -0.198  -5.246  1.00 41.50  ? 193  HIS B C   1 
ATOM   3722 O  O   . HIS B 1 193 ? 44.324  -0.149  -5.683  1.00 40.80  ? 193  HIS B O   1 
ATOM   3723 C  CB  . HIS B 1 193 ? 42.526  2.207   -4.783  1.00 39.97  ? 193  HIS B CB  1 
ATOM   3724 C  CG  . HIS B 1 193 ? 41.836  2.240   -6.110  1.00 42.32  ? 193  HIS B CG  1 
ATOM   3725 N  ND1 . HIS B 1 193 ? 40.571  1.728   -6.306  1.00 44.92  ? 193  HIS B ND1 1 
ATOM   3726 C  CD2 . HIS B 1 193 ? 42.233  2.726   -7.308  1.00 42.23  ? 193  HIS B CD2 1 
ATOM   3727 C  CE1 . HIS B 1 193 ? 40.221  1.893   -7.568  1.00 47.87  ? 193  HIS B CE1 1 
ATOM   3728 N  NE2 . HIS B 1 193 ? 41.211  2.499   -8.199  1.00 52.46  ? 193  HIS B NE2 1 
ATOM   3729 N  N   . LYS B 1 194 ? 42.309  -1.133  -5.616  1.00 50.04  ? 194  LYS B N   1 
ATOM   3730 C  CA  . LYS B 1 194 ? 42.616  -2.065  -6.690  1.00 53.31  ? 194  LYS B CA  1 
ATOM   3731 C  C   . LYS B 1 194 ? 42.305  -1.392  -8.027  1.00 50.07  ? 194  LYS B C   1 
ATOM   3732 O  O   . LYS B 1 194 ? 41.199  -0.884  -8.226  1.00 43.66  ? 194  LYS B O   1 
ATOM   3733 C  CB  . LYS B 1 194 ? 41.790  -3.340  -6.535  1.00 53.14  ? 194  LYS B CB  1 
ATOM   3734 C  CG  . LYS B 1 194 ? 42.517  -4.601  -6.958  1.00 61.92  ? 194  LYS B CG  1 
ATOM   3735 C  CD  . LYS B 1 194 ? 41.587  -5.543  -7.710  1.00 67.27  ? 194  LYS B CD  1 
ATOM   3736 N  N   . GLU B 1 195 ? 43.292  -1.374  -8.923  1.00 59.38  ? 195  GLU B N   1 
ATOM   3737 C  CA  . GLU B 1 195 ? 43.156  -0.758  -10.249 1.00 68.96  ? 195  GLU B CA  1 
ATOM   3738 C  C   . GLU B 1 195 ? 42.872  -1.789  -11.340 1.00 72.80  ? 195  GLU B C   1 
ATOM   3739 O  O   . GLU B 1 195 ? 42.186  -2.784  -11.108 1.00 72.10  ? 195  GLU B O   1 
ATOM   3740 C  CB  . GLU B 1 195 ? 44.413  0.052   -10.604 1.00 63.40  ? 195  GLU B CB  1 
ATOM   3741 C  CG  . GLU B 1 195 ? 44.394  1.477   -10.074 1.00 69.89  ? 195  GLU B CG  1 
ATOM   3742 C  CD  . GLU B 1 195 ? 45.713  2.201   -10.266 1.00 81.74  ? 195  GLU B CD  1 
ATOM   3743 O  OE1 . GLU B 1 195 ? 46.632  1.599   -10.865 1.00 85.71  ? 195  GLU B OE1 1 
ATOM   3744 O  OE2 . GLU B 1 195 ? 45.830  3.371   -9.816  1.00 81.90  ? 195  GLU B OE2 1 
ATOM   3745 N  N   . ASP B 1 203 ? 45.105  -5.105  -12.751 1.00 121.97 ? 203  ASP B N   1 
ATOM   3746 C  CA  . ASP B 1 203 ? 45.102  -5.883  -11.516 1.00 120.31 ? 203  ASP B CA  1 
ATOM   3747 C  C   . ASP B 1 203 ? 46.308  -5.544  -10.644 1.00 111.10 ? 203  ASP B C   1 
ATOM   3748 O  O   . ASP B 1 203 ? 47.201  -6.373  -10.453 1.00 115.96 ? 203  ASP B O   1 
ATOM   3749 C  CB  . ASP B 1 203 ? 45.087  -7.384  -11.825 1.00 124.75 ? 203  ASP B CB  1 
ATOM   3750 C  CG  . ASP B 1 203 ? 44.565  -8.219  -10.660 1.00 124.55 ? 203  ASP B CG  1 
ATOM   3751 O  OD1 . ASP B 1 203 ? 45.330  -8.468  -9.704  1.00 122.81 ? 203  ASP B OD1 1 
ATOM   3752 O  OD2 . ASP B 1 203 ? 43.386  -8.628  -10.707 1.00 124.21 ? 203  ASP B OD2 1 
ATOM   3753 N  N   . ARG B 1 204 ? 46.336  -4.319  -10.128 0.80 92.15  ? 204  ARG B N   1 
ATOM   3754 C  CA  . ARG B 1 204 ? 47.379  -3.905  -9.196  0.80 75.47  ? 204  ARG B CA  1 
ATOM   3755 C  C   . ARG B 1 204 ? 46.824  -2.984  -8.120  0.80 59.57  ? 204  ARG B C   1 
ATOM   3756 O  O   . ARG B 1 204 ? 46.047  -2.079  -8.403  0.80 52.32  ? 204  ARG B O   1 
ATOM   3757 C  CB  . ARG B 1 204 ? 48.547  -3.235  -9.928  0.80 75.55  ? 204  ARG B CB  1 
ATOM   3758 C  CG  . ARG B 1 204 ? 49.682  -4.195  -10.313 0.80 78.96  ? 204  ARG B CG  1 
ATOM   3759 C  CD  . ARG B 1 204 ? 50.560  -4.564  -9.120  0.80 73.95  ? 204  ARG B CD  1 
ATOM   3760 N  NE  . ARG B 1 204 ? 49.843  -5.336  -8.107  0.80 63.86  ? 204  ARG B NE  1 
ATOM   3761 C  CZ  . ARG B 1 204 ? 50.130  -5.312  -6.810  0.80 52.73  ? 204  ARG B CZ  1 
ATOM   3762 N  NH1 . ARG B 1 204 ? 51.114  -4.547  -6.363  0.80 47.47  ? 204  ARG B NH1 1 
ATOM   3763 N  NH2 . ARG B 1 204 ? 49.429  -6.053  -5.961  0.80 52.80  ? 204  ARG B NH2 1 
ATOM   3764 N  N   . MET B 1 205 ? 47.226  -3.235  -6.882  1.00 50.87  ? 205  MET B N   1 
ATOM   3765 C  CA  . MET B 1 205 ? 46.806  -2.423  -5.754  1.00 46.45  ? 205  MET B CA  1 
ATOM   3766 C  C   . MET B 1 205 ? 47.698  -1.209  -5.610  1.00 40.34  ? 205  MET B C   1 
ATOM   3767 O  O   . MET B 1 205 ? 48.920  -1.300  -5.777  1.00 41.17  ? 205  MET B O   1 
ATOM   3768 C  CB  . MET B 1 205 ? 46.865  -3.237  -4.459  1.00 44.88  ? 205  MET B CB  1 
ATOM   3769 C  CG  . MET B 1 205 ? 45.600  -4.008  -4.160  1.00 47.26  ? 205  MET B CG  1 
ATOM   3770 S  SD  . MET B 1 205 ? 45.771  -5.121  -2.748  1.00 41.64  ? 205  MET B SD  1 
ATOM   3771 C  CE  . MET B 1 205 ? 44.060  -5.629  -2.566  1.00 39.95  ? 205  MET B CE  1 
ATOM   3772 N  N   . VAL B 1 206 ? 47.089  -0.071  -5.293  1.00 37.11  ? 206  VAL B N   1 
ATOM   3773 C  CA  . VAL B 1 206 ? 47.866  1.110   -4.963  1.00 44.03  ? 206  VAL B CA  1 
ATOM   3774 C  C   . VAL B 1 206 ? 47.535  1.595   -3.555  1.00 41.81  ? 206  VAL B C   1 
ATOM   3775 O  O   . VAL B 1 206 ? 46.397  1.545   -3.111  1.00 44.92  ? 206  VAL B O   1 
ATOM   3776 C  CB  . VAL B 1 206 ? 47.698  2.246   -5.995  1.00 43.90  ? 206  VAL B CB  1 
ATOM   3777 C  CG1 . VAL B 1 206 ? 47.923  1.714   -7.407  1.00 56.53  ? 206  VAL B CG1 1 
ATOM   3778 C  CG2 . VAL B 1 206 ? 46.338  2.873   -5.886  1.00 38.34  ? 206  VAL B CG2 1 
ATOM   3779 N  N   . LEU B 1 207 ? 48.554  2.049   -2.848  1.00 42.57  ? 207  LEU B N   1 
ATOM   3780 C  CA  . LEU B 1 207 ? 48.368  2.516   -1.495  1.00 43.73  ? 207  LEU B CA  1 
ATOM   3781 C  C   . LEU B 1 207 ? 48.621  4.006   -1.448  1.00 44.20  ? 207  LEU B C   1 
ATOM   3782 O  O   . LEU B 1 207 ? 49.628  4.487   -1.983  1.00 44.49  ? 207  LEU B O   1 
ATOM   3783 C  CB  . LEU B 1 207 ? 49.351  1.798   -0.573  1.00 46.85  ? 207  LEU B CB  1 
ATOM   3784 C  CG  . LEU B 1 207 ? 49.417  2.254   0.880   1.00 46.03  ? 207  LEU B CG  1 
ATOM   3785 C  CD1 . LEU B 1 207 ? 48.053  2.077   1.581   1.00 36.89  ? 207  LEU B CD1 1 
ATOM   3786 C  CD2 . LEU B 1 207 ? 50.504  1.466   1.583   1.00 53.43  ? 207  LEU B CD2 1 
ATOM   3787 N  N   . VAL B 1 208 ? 47.698  4.739   -0.833  1.00 39.46  ? 208  VAL B N   1 
ATOM   3788 C  CA  . VAL B 1 208 ? 47.937  6.138   -0.498  1.00 39.56  ? 208  VAL B CA  1 
ATOM   3789 C  C   . VAL B 1 208 ? 47.842  6.313   1.018   1.00 46.36  ? 208  VAL B C   1 
ATOM   3790 O  O   . VAL B 1 208 ? 46.881  5.862   1.645   1.00 48.76  ? 208  VAL B O   1 
ATOM   3791 C  CB  . VAL B 1 208 ? 46.974  7.118   -1.224  1.00 41.94  ? 208  VAL B CB  1 
ATOM   3792 C  CG1 . VAL B 1 208 ? 47.105  6.992   -2.745  1.00 47.02  ? 208  VAL B CG1 1 
ATOM   3793 C  CG2 . VAL B 1 208 ? 45.539  6.917   -0.775  1.00 36.91  ? 208  VAL B CG2 1 
ATOM   3794 N  N   . GLY B 1 209 ? 48.850  6.942   1.609   1.00 40.03  ? 209  GLY B N   1 
ATOM   3795 C  CA  . GLY B 1 209 ? 48.834  7.194   3.037   1.00 38.94  ? 209  GLY B CA  1 
ATOM   3796 C  C   . GLY B 1 209 ? 50.065  6.589   3.661   1.00 44.63  ? 209  GLY B C   1 
ATOM   3797 O  O   . GLY B 1 209 ? 50.755  5.804   3.024   1.00 42.06  ? 209  GLY B O   1 
ATOM   3798 N  N   . ASP B 1 210 ? 50.335  6.939   4.912   1.00 55.13  ? 210  ASP B N   1 
ATOM   3799 C  CA  . ASP B 1 210 ? 51.595  6.569   5.550   1.00 57.82  ? 210  ASP B CA  1 
ATOM   3800 C  C   . ASP B 1 210 ? 51.468  5.340   6.447   1.00 48.08  ? 210  ASP B C   1 
ATOM   3801 O  O   . ASP B 1 210 ? 50.749  5.372   7.447   1.00 47.45  ? 210  ASP B O   1 
ATOM   3802 C  CB  . ASP B 1 210 ? 52.116  7.749   6.372   1.00 71.03  ? 210  ASP B CB  1 
ATOM   3803 C  CG  . ASP B 1 210 ? 53.541  7.547   6.844   1.00 84.09  ? 210  ASP B CG  1 
ATOM   3804 O  OD1 . ASP B 1 210 ? 53.831  7.878   8.016   1.00 83.90  ? 210  ASP B OD1 1 
ATOM   3805 O  OD2 . ASP B 1 210 ? 54.369  7.068   6.036   1.00 86.44  ? 210  ASP B OD2 1 
ATOM   3806 N  N   . VAL B 1 211 ? 52.176  4.264   6.096   1.00 40.29  ? 211  VAL B N   1 
ATOM   3807 C  CA  . VAL B 1 211 ? 52.218  3.073   6.949   1.00 44.91  ? 211  VAL B CA  1 
ATOM   3808 C  C   . VAL B 1 211 ? 53.623  2.655   7.386   1.00 42.08  ? 211  VAL B C   1 
ATOM   3809 O  O   . VAL B 1 211 ? 53.769  1.680   8.130   1.00 40.15  ? 211  VAL B O   1 
ATOM   3810 C  CB  . VAL B 1 211 ? 51.554  1.850   6.281   1.00 45.70  ? 211  VAL B CB  1 
ATOM   3811 C  CG1 . VAL B 1 211 ? 50.145  2.187   5.843   1.00 41.18  ? 211  VAL B CG1 1 
ATOM   3812 C  CG2 . VAL B 1 211 ? 52.395  1.371   5.109   1.00 38.10  ? 211  VAL B CG2 1 
ATOM   3813 N  N   . LYS B 1 212 ? 54.649  3.379   6.935   1.00 43.48  ? 212  LYS B N   1 
ATOM   3814 C  CA  . LYS B 1 212 ? 56.025  2.933   7.158   1.00 49.62  ? 212  LYS B CA  1 
ATOM   3815 C  C   . LYS B 1 212 ? 56.431  2.908   8.633   1.00 45.72  ? 212  LYS B C   1 
ATOM   3816 O  O   . LYS B 1 212 ? 56.285  3.898   9.342   1.00 42.57  ? 212  LYS B O   1 
ATOM   3817 C  CB  . LYS B 1 212 ? 57.033  3.752   6.349   1.00 56.39  ? 212  LYS B CB  1 
ATOM   3818 C  CG  . LYS B 1 212 ? 58.465  3.200   6.460   1.00 61.40  ? 212  LYS B CG  1 
ATOM   3819 C  CD  . LYS B 1 212 ? 59.430  3.888   5.509   1.00 63.45  ? 212  LYS B CD  1 
ATOM   3820 N  N   . ASP B 1 213 ? 56.933  1.759   9.078   1.00 48.70  ? 213  ASP B N   1 
ATOM   3821 C  CA  . ASP B 1 213 ? 57.357  1.571   10.458  1.00 50.75  ? 213  ASP B CA  1 
ATOM   3822 C  C   . ASP B 1 213 ? 56.234  1.773   11.448  1.00 50.72  ? 213  ASP B C   1 
ATOM   3823 O  O   . ASP B 1 213 ? 56.484  1.970   12.639  1.00 49.33  ? 213  ASP B O   1 
ATOM   3824 C  CB  . ASP B 1 213 ? 58.533  2.487   10.795  1.00 62.42  ? 213  ASP B CB  1 
ATOM   3825 C  CG  . ASP B 1 213 ? 59.831  2.022   10.153  1.00 72.58  ? 213  ASP B CG  1 
ATOM   3826 O  OD1 . ASP B 1 213 ? 60.378  2.755   9.296   1.00 65.15  ? 213  ASP B OD1 1 
ATOM   3827 O  OD2 . ASP B 1 213 ? 60.301  0.917   10.506  1.00 82.39  ? 213  ASP B OD2 1 
ATOM   3828 N  N   . ARG B 1 214 ? 54.999  1.722   10.951  1.00 47.55  ? 214  ARG B N   1 
ATOM   3829 C  CA  . ARG B 1 214 ? 53.819  1.740   11.811  1.00 43.76  ? 214  ARG B CA  1 
ATOM   3830 C  C   . ARG B 1 214 ? 53.124  0.388   11.779  1.00 46.30  ? 214  ARG B C   1 
ATOM   3831 O  O   . ARG B 1 214 ? 53.262  -0.366  10.814  1.00 35.78  ? 214  ARG B O   1 
ATOM   3832 C  CB  . ARG B 1 214 ? 52.829  2.811   11.357  1.00 47.80  ? 214  ARG B CB  1 
ATOM   3833 C  CG  . ARG B 1 214 ? 53.395  4.220   11.333  1.00 52.75  ? 214  ARG B CG  1 
ATOM   3834 C  CD  . ARG B 1 214 ? 52.331  5.247   10.972  1.00 57.56  ? 214  ARG B CD  1 
ATOM   3835 N  NE  . ARG B 1 214 ? 52.508  6.454   11.773  1.00 75.33  ? 214  ARG B NE  1 
ATOM   3836 C  CZ  . ARG B 1 214 ? 51.658  6.876   12.703  1.00 78.18  ? 214  ARG B CZ  1 
ATOM   3837 N  NH1 . ARG B 1 214 ? 50.539  6.208   12.946  1.00 73.76  ? 214  ARG B NH1 1 
ATOM   3838 N  NH2 . ARG B 1 214 ? 51.924  7.982   13.385  1.00 83.74  ? 214  ARG B NH2 1 
ATOM   3839 N  N   . VAL B 1 215 ? 52.389  0.070   12.839  1.00 36.63  ? 215  VAL B N   1 
ATOM   3840 C  CA  . VAL B 1 215 ? 51.476  -1.055  12.770  1.00 34.58  ? 215  VAL B CA  1 
ATOM   3841 C  C   . VAL B 1 215 ? 50.354  -0.646  11.825  1.00 36.18  ? 215  VAL B C   1 
ATOM   3842 O  O   . VAL B 1 215 ? 49.911  0.501   11.839  1.00 39.15  ? 215  VAL B O   1 
ATOM   3843 C  CB  . VAL B 1 215 ? 50.903  -1.416  14.152  1.00 36.29  ? 215  VAL B CB  1 
ATOM   3844 C  CG1 . VAL B 1 215 ? 49.822  -2.459  14.017  1.00 33.42  ? 215  VAL B CG1 1 
ATOM   3845 C  CG2 . VAL B 1 215 ? 52.005  -1.902  15.067  1.00 34.97  ? 215  VAL B CG2 1 
ATOM   3846 N  N   . ALA B 1 216 ? 49.922  -1.566  10.971  1.00 31.40  ? 216  ALA B N   1 
ATOM   3847 C  CA  . ALA B 1 216 ? 48.826  -1.282  10.056  1.00 34.56  ? 216  ALA B CA  1 
ATOM   3848 C  C   . ALA B 1 216 ? 47.601  -2.084  10.465  1.00 28.16  ? 216  ALA B C   1 
ATOM   3849 O  O   . ALA B 1 216 ? 47.697  -3.281  10.711  1.00 32.56  ? 216  ALA B O   1 
ATOM   3850 C  CB  . ALA B 1 216 ? 49.229  -1.604  8.611   1.00 34.75  ? 216  ALA B CB  1 
ATOM   3851 N  N   . ILE B 1 217 ? 46.445  -1.435  10.542  1.00 27.31  ? 217  ILE B N   1 
ATOM   3852 C  CA  . ILE B 1 217 ? 45.240  -2.171  10.886  1.00 31.04  ? 217  ILE B CA  1 
ATOM   3853 C  C   . ILE B 1 217 ? 44.234  -2.050  9.761   1.00 35.01  ? 217  ILE B C   1 
ATOM   3854 O  O   . ILE B 1 217 ? 43.639  -0.989  9.567   1.00 31.58  ? 217  ILE B O   1 
ATOM   3855 C  CB  . ILE B 1 217 ? 44.593  -1.656  12.189  1.00 35.63  ? 217  ILE B CB  1 
ATOM   3856 C  CG1 . ILE B 1 217 ? 45.642  -1.438  13.280  1.00 36.63  ? 217  ILE B CG1 1 
ATOM   3857 C  CG2 . ILE B 1 217 ? 43.525  -2.626  12.677  1.00 36.76  ? 217  ILE B CG2 1 
ATOM   3858 C  CD1 . ILE B 1 217 ? 45.044  -0.935  14.600  1.00 36.16  ? 217  ILE B CD1 1 
ATOM   3859 N  N   . LEU B 1 218 ? 44.054  -3.127  9.005   1.00 34.02  ? 218  LEU B N   1 
ATOM   3860 C  CA  . LEU B 1 218 ? 43.030  -3.134  7.968   1.00 35.48  ? 218  LEU B CA  1 
ATOM   3861 C  C   . LEU B 1 218 ? 41.679  -3.296  8.637   1.00 35.97  ? 218  LEU B C   1 
ATOM   3862 O  O   . LEU B 1 218 ? 41.427  -4.293  9.332   1.00 29.15  ? 218  LEU B O   1 
ATOM   3863 C  CB  . LEU B 1 218 ? 43.242  -4.270  6.974   1.00 27.37  ? 218  LEU B CB  1 
ATOM   3864 C  CG  . LEU B 1 218 ? 44.284  -4.073  5.889   1.00 30.15  ? 218  LEU B CG  1 
ATOM   3865 C  CD1 . LEU B 1 218 ? 44.925  -5.430  5.545   1.00 27.18  ? 218  LEU B CD1 1 
ATOM   3866 C  CD2 . LEU B 1 218 ? 43.683  -3.383  4.645   1.00 24.57  ? 218  LEU B CD2 1 
ATOM   3867 N  N   . VAL B 1 219 ? 40.823  -2.301  8.429   1.00 32.19  ? 219  VAL B N   1 
ATOM   3868 C  CA  . VAL B 1 219 ? 39.487  -2.308  8.979   1.00 32.52  ? 219  VAL B CA  1 
ATOM   3869 C  C   . VAL B 1 219 ? 38.473  -2.336  7.842   1.00 46.48  ? 219  VAL B C   1 
ATOM   3870 O  O   . VAL B 1 219 ? 38.601  -1.605  6.868   1.00 45.20  ? 219  VAL B O   1 
ATOM   3871 C  CB  . VAL B 1 219 ? 39.249  -1.087  9.850   1.00 33.81  ? 219  VAL B CB  1 
ATOM   3872 C  CG1 . VAL B 1 219 ? 37.853  -1.140  10.461  1.00 36.47  ? 219  VAL B CG1 1 
ATOM   3873 C  CG2 . VAL B 1 219 ? 40.327  -1.004  10.957  1.00 29.98  ? 219  VAL B CG2 1 
ATOM   3874 N  N   . ASP B 1 220 ? 37.484  -3.212  7.961   1.00 52.22  ? 220  ASP B N   1 
ATOM   3875 C  CA  . ASP B 1 220 ? 36.425  -3.320  6.969   1.00 48.75  ? 220  ASP B CA  1 
ATOM   3876 C  C   . ASP B 1 220 ? 35.135  -3.838  7.626   1.00 43.33  ? 220  ASP B C   1 
ATOM   3877 O  O   . ASP B 1 220 ? 35.137  -4.260  8.785   1.00 34.11  ? 220  ASP B O   1 
ATOM   3878 C  CB  . ASP B 1 220 ? 36.867  -4.228  5.819   1.00 53.30  ? 220  ASP B CB  1 
ATOM   3879 C  CG  . ASP B 1 220 ? 36.200  -3.870  4.508   1.00 60.51  ? 220  ASP B CG  1 
ATOM   3880 O  OD1 . ASP B 1 220 ? 35.781  -2.704  4.355   1.00 56.10  ? 220  ASP B OD1 1 
ATOM   3881 O  OD2 . ASP B 1 220 ? 36.097  -4.754  3.629   1.00 66.77  ? 220  ASP B OD2 1 
ATOM   3882 N  N   . ASP B 1 221 ? 34.030  -3.789  6.898   1.00 38.27  ? 221  ASP B N   1 
ATOM   3883 C  CA  . ASP B 1 221 ? 32.764  -4.230  7.462   1.00 33.11  ? 221  ASP B CA  1 
ATOM   3884 C  C   . ASP B 1 221 ? 32.634  -5.752  7.409   1.00 39.67  ? 221  ASP B C   1 
ATOM   3885 O  O   . ASP B 1 221 ? 32.079  -6.377  8.322   1.00 36.71  ? 221  ASP B O   1 
ATOM   3886 C  CB  . ASP B 1 221 ? 31.595  -3.570  6.746   1.00 32.90  ? 221  ASP B CB  1 
ATOM   3887 C  CG  . ASP B 1 221 ? 31.621  -3.821  5.262   1.00 41.80  ? 221  ASP B CG  1 
ATOM   3888 O  OD1 . ASP B 1 221 ? 32.724  -3.760  4.668   1.00 49.52  ? 221  ASP B OD1 1 
ATOM   3889 O  OD2 . ASP B 1 221 ? 30.544  -4.102  4.691   1.00 42.52  ? 221  ASP B OD2 1 
ATOM   3890 N  N   . MET B 1 222 ? 33.167  -6.352  6.351   1.00 40.53  ? 222  MET B N   1 
ATOM   3891 C  CA  . MET B 1 222 ? 33.053  -7.789  6.182   1.00 42.31  ? 222  MET B CA  1 
ATOM   3892 C  C   . MET B 1 222 ? 34.174  -8.374  5.326   1.00 45.32  ? 222  MET B C   1 
ATOM   3893 O  O   . MET B 1 222 ? 34.683  -7.721  4.420   1.00 40.95  ? 222  MET B O   1 
ATOM   3894 C  CB  . MET B 1 222 ? 31.707  -8.119  5.539   1.00 49.32  ? 222  MET B CB  1 
ATOM   3895 C  CG  . MET B 1 222 ? 31.602  -7.643  4.102   1.00 44.98  ? 222  MET B CG  1 
ATOM   3896 S  SD  . MET B 1 222 ? 30.108  -8.229  3.280   1.00 71.31  ? 222  MET B SD  1 
ATOM   3897 C  CE  . MET B 1 222 ? 28.844  -7.270  4.122   1.00 50.07  ? 222  MET B CE  1 
ATOM   3898 N  N   . ALA B 1 223 ? 34.545  -9.614  5.616   1.00 49.05  ? 223  ALA B N   1 
ATOM   3899 C  CA  . ALA B 1 223 ? 35.490  -10.330 4.774   1.00 50.08  ? 223  ALA B CA  1 
ATOM   3900 C  C   . ALA B 1 223 ? 34.831  -11.605 4.343   1.00 43.83  ? 223  ALA B C   1 
ATOM   3901 O  O   . ALA B 1 223 ? 34.312  -12.361 5.173   1.00 41.29  ? 223  ALA B O   1 
ATOM   3902 C  CB  . ALA B 1 223 ? 36.768  -10.633 5.515   1.00 51.30  ? 223  ALA B CB  1 
ATOM   3903 N  N   . ASP B 1 224 ? 34.848  -11.846 3.041   1.00 41.45  ? 224  ASP B N   1 
ATOM   3904 C  CA  . ASP B 1 224 ? 34.259  -13.050 2.493   1.00 42.22  ? 224  ASP B CA  1 
ATOM   3905 C  C   . ASP B 1 224 ? 35.200  -14.153 2.013   1.00 43.12  ? 224  ASP B C   1 
ATOM   3906 O  O   . ASP B 1 224 ? 35.337  -15.184 2.670   1.00 44.28  ? 224  ASP B O   1 
ATOM   3907 C  CB  . ASP B 1 224 ? 33.382  -12.692 1.302   1.00 50.46  ? 224  ASP B CB  1 
ATOM   3908 C  CG  . ASP B 1 224 ? 32.618  -13.868 0.774   1.00 56.43  ? 224  ASP B CG  1 
ATOM   3909 O  OD1 . ASP B 1 224 ? 32.499  -14.878 1.505   1.00 52.27  ? 224  ASP B OD1 1 
ATOM   3910 O  OD2 . ASP B 1 224 ? 32.140  -13.776 -0.379  1.00 63.57  ? 224  ASP B OD2 1 
ATOM   3911 N  N   . THR B 1 225 ? 35.859  -13.930 0.879   1.00 38.39  ? 225  THR B N   1 
ATOM   3912 C  CA  . THR B 1 225 ? 36.816  -14.899 0.333   1.00 37.48  ? 225  THR B CA  1 
ATOM   3913 C  C   . THR B 1 225 ? 38.231  -14.450 0.753   1.00 41.18  ? 225  THR B C   1 
ATOM   3914 O  O   . THR B 1 225 ? 39.171  -15.242 0.713   1.00 41.81  ? 225  THR B O   1 
ATOM   3915 C  CB  . THR B 1 225 ? 36.762  -15.053 -1.212  1.00 49.70  ? 225  THR B CB  1 
ATOM   3916 O  OG1 . THR B 1 225 ? 37.000  -13.781 -1.829  1.00 48.95  ? 225  THR B OG1 1 
ATOM   3917 C  CG2 . THR B 1 225 ? 35.397  -15.582 -1.653  1.00 45.89  ? 225  THR B CG2 1 
ATOM   3918 N  N   . CYS B 1 226 ? 38.367  -13.184 1.142   1.00 39.32  ? 226  CYS B N   1 
ATOM   3919 C  CA  . CYS B 1 226 ? 39.602  -12.661 1.742   1.00 45.05  ? 226  CYS B CA  1 
ATOM   3920 C  C   . CYS B 1 226 ? 40.739  -12.486 0.747   1.00 44.27  ? 226  CYS B C   1 
ATOM   3921 O  O   . CYS B 1 226 ? 41.869  -12.205 1.143   1.00 50.98  ? 226  CYS B O   1 
ATOM   3922 C  CB  . CYS B 1 226 ? 40.075  -13.527 2.927   1.00 46.69  ? 226  CYS B CB  1 
ATOM   3923 S  SG  . CYS B 1 226 ? 38.924  -13.580 4.326   1.00 51.35  ? 226  CYS B SG  1 
ATOM   3924 N  N   . GLY B 1 227 ? 40.443  -12.645 -0.538  1.00 48.11  ? 227  GLY B N   1 
ATOM   3925 C  CA  . GLY B 1 227 ? 41.425  -12.374 -1.574  1.00 42.29  ? 227  GLY B CA  1 
ATOM   3926 C  C   . GLY B 1 227 ? 41.975  -10.972 -1.392  1.00 48.27  ? 227  GLY B C   1 
ATOM   3927 O  O   . GLY B 1 227 ? 43.186  -10.761 -1.386  1.00 48.43  ? 227  GLY B O   1 
ATOM   3928 N  N   . THR B 1 228 ? 41.070  -10.015 -1.208  1.00 51.50  ? 228  THR B N   1 
ATOM   3929 C  CA  . THR B 1 228 ? 41.436  -8.606  -1.100  1.00 50.83  ? 228  THR B CA  1 
ATOM   3930 C  C   . THR B 1 228 ? 42.284  -8.295  0.135   1.00 40.27  ? 228  THR B C   1 
ATOM   3931 O  O   . THR B 1 228 ? 43.339  -7.672  0.024   1.00 38.78  ? 228  THR B O   1 
ATOM   3932 C  CB  . THR B 1 228 ? 40.183  -7.700  -1.109  1.00 53.64  ? 228  THR B CB  1 
ATOM   3933 O  OG1 . THR B 1 228 ? 39.547  -7.778  -2.392  1.00 53.54  ? 228  THR B OG1 1 
ATOM   3934 C  CG2 . THR B 1 228 ? 40.556  -6.252  -0.824  1.00 47.01  ? 228  THR B CG2 1 
ATOM   3935 N  N   . ILE B 1 229 ? 41.834  -8.726  1.308   1.00 35.66  ? 229  ILE B N   1 
ATOM   3936 C  CA  . ILE B 1 229 ? 42.559  -8.385  2.534   1.00 48.45  ? 229  ILE B CA  1 
ATOM   3937 C  C   . ILE B 1 229 ? 43.955  -8.992  2.576   1.00 45.28  ? 229  ILE B C   1 
ATOM   3938 O  O   . ILE B 1 229 ? 44.904  -8.349  3.022   1.00 41.57  ? 229  ILE B O   1 
ATOM   3939 C  CB  . ILE B 1 229 ? 41.799  -8.774  3.829   1.00 53.37  ? 229  ILE B CB  1 
ATOM   3940 C  CG1 . ILE B 1 229 ? 41.304  -10.226 3.765   1.00 42.78  ? 229  ILE B CG1 1 
ATOM   3941 C  CG2 . ILE B 1 229 ? 40.682  -7.767  4.131   1.00 50.23  ? 229  ILE B CG2 1 
ATOM   3942 C  CD1 . ILE B 1 229 ? 41.080  -10.840 5.153   1.00 39.85  ? 229  ILE B CD1 1 
ATOM   3943 N  N   . CYS B 1 230 ? 44.070  -10.232 2.112   1.00 45.97  ? 230  CYS B N   1 
ATOM   3944 C  CA  . CYS B 1 230 ? 45.353  -10.922 2.081   1.00 43.02  ? 230  CYS B CA  1 
ATOM   3945 C  C   . CYS B 1 230 ? 46.341  -10.181 1.207   1.00 42.02  ? 230  CYS B C   1 
ATOM   3946 O  O   . CYS B 1 230 ? 47.494  -9.971  1.601   1.00 40.20  ? 230  CYS B O   1 
ATOM   3947 C  CB  . CYS B 1 230 ? 45.179  -12.354 1.588   1.00 44.48  ? 230  CYS B CB  1 
ATOM   3948 S  SG  . CYS B 1 230 ? 44.404  -13.405 2.804   1.00 50.22  ? 230  CYS B SG  1 
ATOM   3949 N  N   . HIS B 1 231 ? 45.890  -9.776  0.023   1.00 41.62  ? 231  HIS B N   1 
ATOM   3950 C  CA  . HIS B 1 231 ? 46.743  -8.989  -0.866  1.00 42.94  ? 231  HIS B CA  1 
ATOM   3951 C  C   . HIS B 1 231 ? 47.107  -7.623  -0.276  1.00 34.77  ? 231  HIS B C   1 
ATOM   3952 O  O   . HIS B 1 231 ? 48.248  -7.204  -0.366  1.00 38.36  ? 231  HIS B O   1 
ATOM   3953 C  CB  . HIS B 1 231 ? 46.119  -8.858  -2.256  1.00 44.02  ? 231  HIS B CB  1 
ATOM   3954 C  CG  . HIS B 1 231 ? 46.229  -10.108 -3.067  1.00 59.75  ? 231  HIS B CG  1 
ATOM   3955 N  ND1 . HIS B 1 231 ? 45.130  -10.801 -3.525  1.00 67.29  ? 231  HIS B ND1 1 
ATOM   3956 C  CD2 . HIS B 1 231 ? 47.313  -10.809 -3.479  1.00 67.78  ? 231  HIS B CD2 1 
ATOM   3957 C  CE1 . HIS B 1 231 ? 45.531  -11.869 -4.192  1.00 68.23  ? 231  HIS B CE1 1 
ATOM   3958 N  NE2 . HIS B 1 231 ? 46.851  -11.897 -4.178  1.00 68.56  ? 231  HIS B NE2 1 
ATOM   3959 N  N   . ALA B 1 232 ? 46.136  -6.948  0.338   1.00 31.62  ? 232  ALA B N   1 
ATOM   3960 C  CA  . ALA B 1 232 ? 46.387  -5.691  1.038   1.00 30.39  ? 232  ALA B CA  1 
ATOM   3961 C  C   . ALA B 1 232 ? 47.458  -5.825  2.131   1.00 25.96  ? 232  ALA B C   1 
ATOM   3962 O  O   . ALA B 1 232 ? 48.315  -4.956  2.268   1.00 36.08  ? 232  ALA B O   1 
ATOM   3963 C  CB  . ALA B 1 232 ? 45.074  -5.123  1.625   1.00 34.84  ? 232  ALA B CB  1 
ATOM   3964 N  N   . ALA B 1 233 ? 47.427  -6.907  2.904   1.00 28.42  ? 233  ALA B N   1 
ATOM   3965 C  CA  . ALA B 1 233 ? 48.476  -7.144  3.916   1.00 33.16  ? 233  ALA B CA  1 
ATOM   3966 C  C   . ALA B 1 233 ? 49.901  -7.182  3.336   1.00 43.38  ? 233  ALA B C   1 
ATOM   3967 O  O   . ALA B 1 233 ? 50.827  -6.571  3.890   1.00 45.72  ? 233  ALA B O   1 
ATOM   3968 C  CB  . ALA B 1 233 ? 48.190  -8.427  4.727   1.00 23.54  ? 233  ALA B CB  1 
ATOM   3969 N  N   . ASP B 1 234 ? 50.079  -7.911  2.235   1.00 37.31  ? 234  ASP B N   1 
ATOM   3970 C  CA  . ASP B 1 234 ? 51.359  -7.917  1.521   1.00 41.09  ? 234  ASP B CA  1 
ATOM   3971 C  C   . ASP B 1 234 ? 51.784  -6.507  1.145   1.00 38.81  ? 234  ASP B C   1 
ATOM   3972 O  O   . ASP B 1 234 ? 52.896  -6.069  1.446   1.00 39.72  ? 234  ASP B O   1 
ATOM   3973 C  CB  . ASP B 1 234 ? 51.261  -8.726  0.223   1.00 44.22  ? 234  ASP B CB  1 
ATOM   3974 C  CG  . ASP B 1 234 ? 51.043  -10.199 0.467   1.00 50.58  ? 234  ASP B CG  1 
ATOM   3975 O  OD1 . ASP B 1 234 ? 51.419  -10.683 1.555   1.00 53.44  ? 234  ASP B OD1 1 
ATOM   3976 O  OD2 . ASP B 1 234 ? 50.490  -10.866 -0.432  1.00 51.76  ? 234  ASP B OD2 1 
ATOM   3977 N  N   . LYS B 1 235 ? 50.891  -5.822  0.441   1.00 31.28  ? 235  LYS B N   1 
ATOM   3978 C  CA  . LYS B 1 235 ? 51.147  -4.479  -0.023  1.00 31.66  ? 235  LYS B CA  1 
ATOM   3979 C  C   . LYS B 1 235 ? 51.588  -3.612  1.146   1.00 30.10  ? 235  LYS B C   1 
ATOM   3980 O  O   . LYS B 1 235 ? 52.534  -2.836  1.042   1.00 37.15  ? 235  LYS B O   1 
ATOM   3981 C  CB  . LYS B 1 235 ? 49.895  -3.899  -0.684  1.00 30.92  ? 235  LYS B CB  1 
ATOM   3982 C  CG  . LYS B 1 235 ? 50.114  -2.511  -1.267  1.00 46.04  ? 235  LYS B CG  1 
ATOM   3983 C  CD  . LYS B 1 235 ? 50.639  -2.565  -2.688  1.00 55.34  ? 235  LYS B CD  1 
ATOM   3984 C  CE  . LYS B 1 235 ? 51.107  -1.184  -3.147  1.00 57.78  ? 235  LYS B CE  1 
ATOM   3985 N  NZ  . LYS B 1 235 ? 51.590  -1.185  -4.565  1.00 51.91  ? 235  LYS B NZ  1 
ATOM   3986 N  N   . LEU B 1 236 ? 50.907  -3.755  2.270   1.00 28.36  ? 236  LEU B N   1 
ATOM   3987 C  CA  . LEU B 1 236 ? 51.207  -2.915  3.418   1.00 28.63  ? 236  LEU B CA  1 
ATOM   3988 C  C   . LEU B 1 236 ? 52.597  -3.225  3.941   1.00 30.75  ? 236  LEU B C   1 
ATOM   3989 O  O   . LEU B 1 236 ? 53.357  -2.313  4.268   1.00 37.43  ? 236  LEU B O   1 
ATOM   3990 C  CB  . LEU B 1 236 ? 50.152  -3.101  4.512   1.00 30.20  ? 236  LEU B CB  1 
ATOM   3991 C  CG  . LEU B 1 236 ? 48.817  -2.402  4.245   1.00 27.50  ? 236  LEU B CG  1 
ATOM   3992 C  CD1 . LEU B 1 236 ? 47.733  -2.909  5.196   1.00 33.14  ? 236  LEU B CD1 1 
ATOM   3993 C  CD2 . LEU B 1 236 ? 48.971  -0.904  4.377   1.00 32.98  ? 236  LEU B CD2 1 
ATOM   3994 N  N   . LEU B 1 237 ? 52.931  -4.513  4.006   1.00 27.45  ? 237  LEU B N   1 
ATOM   3995 C  CA  . LEU B 1 237 ? 54.265  -4.936  4.420   1.00 30.04  ? 237  LEU B CA  1 
ATOM   3996 C  C   . LEU B 1 237 ? 55.351  -4.488  3.437   1.00 34.74  ? 237  LEU B C   1 
ATOM   3997 O  O   . LEU B 1 237 ? 56.434  -4.082  3.857   1.00 33.01  ? 237  LEU B O   1 
ATOM   3998 C  CB  . LEU B 1 237 ? 54.321  -6.448  4.638   1.00 33.60  ? 237  LEU B CB  1 
ATOM   3999 C  CG  . LEU B 1 237 ? 53.701  -7.034  5.914   1.00 46.36  ? 237  LEU B CG  1 
ATOM   4000 C  CD1 . LEU B 1 237 ? 53.815  -8.545  5.899   1.00 42.90  ? 237  LEU B CD1 1 
ATOM   4001 C  CD2 . LEU B 1 237 ? 54.330  -6.477  7.195   1.00 41.32  ? 237  LEU B CD2 1 
ATOM   4002 N  N   . SER B 1 238 ? 55.059  -4.542  2.139   1.00 32.17  ? 238  SER B N   1 
ATOM   4003 C  CA  . SER B 1 238 ? 56.012  -4.097  1.110   1.00 32.99  ? 238  SER B CA  1 
ATOM   4004 C  C   . SER B 1 238 ? 56.266  -2.608  1.204   1.00 32.89  ? 238  SER B C   1 
ATOM   4005 O  O   . SER B 1 238 ? 57.288  -2.112  0.737   1.00 36.32  ? 238  SER B O   1 
ATOM   4006 C  CB  . SER B 1 238 ? 55.490  -4.410  -0.292  1.00 31.71  ? 238  SER B CB  1 
ATOM   4007 O  OG  . SER B 1 238 ? 55.226  -5.790  -0.425  1.00 45.91  ? 238  SER B OG  1 
ATOM   4008 N  N   . ALA B 1 239 ? 55.310  -1.894  1.784   1.00 32.21  ? 239  ALA B N   1 
ATOM   4009 C  CA  . ALA B 1 239 ? 55.397  -0.444  1.911   1.00 37.14  ? 239  ALA B CA  1 
ATOM   4010 C  C   . ALA B 1 239 ? 55.983  -0.044  3.272   1.00 43.22  ? 239  ALA B C   1 
ATOM   4011 O  O   . ALA B 1 239 ? 56.096  1.142   3.576   1.00 49.77  ? 239  ALA B O   1 
ATOM   4012 C  CB  . ALA B 1 239 ? 54.025  0.176   1.732   1.00 36.00  ? 239  ALA B CB  1 
ATOM   4013 N  N   . GLY B 1 240 ? 56.334  -1.035  4.090   1.00 37.16  ? 240  GLY B N   1 
ATOM   4014 C  CA  . GLY B 1 240 ? 57.054  -0.777  5.325   1.00 43.23  ? 240  GLY B CA  1 
ATOM   4015 C  C   . GLY B 1 240 ? 56.302  -0.911  6.636   1.00 42.49  ? 240  GLY B C   1 
ATOM   4016 O  O   . GLY B 1 240 ? 56.873  -0.651  7.692   1.00 46.88  ? 240  GLY B O   1 
ATOM   4017 N  N   . ALA B 1 241 ? 55.031  -1.300  6.595   1.00 28.40  ? 241  ALA B N   1 
ATOM   4018 C  CA  . ALA B 1 241 ? 54.322  -1.552  7.850   1.00 30.61  ? 241  ALA B CA  1 
ATOM   4019 C  C   . ALA B 1 241 ? 55.055  -2.602  8.674   1.00 30.17  ? 241  ALA B C   1 
ATOM   4020 O  O   . ALA B 1 241 ? 55.643  -3.544  8.138   1.00 39.91  ? 241  ALA B O   1 
ATOM   4021 C  CB  . ALA B 1 241 ? 52.870  -1.979  7.606   1.00 20.83  ? 241  ALA B CB  1 
ATOM   4022 N  N   . THR B 1 242 ? 54.983  -2.439  9.986   1.00 34.62  ? 242  THR B N   1 
ATOM   4023 C  CA  . THR B 1 242 ? 55.710  -3.265  10.941  1.00 37.54  ? 242  THR B CA  1 
ATOM   4024 C  C   . THR B 1 242 ? 55.047  -4.628  11.074  1.00 39.33  ? 242  THR B C   1 
ATOM   4025 O  O   . THR B 1 242 ? 55.708  -5.667  11.145  1.00 35.13  ? 242  THR B O   1 
ATOM   4026 C  CB  . THR B 1 242 ? 55.751  -2.550  12.300  1.00 39.47  ? 242  THR B CB  1 
ATOM   4027 O  OG1 . THR B 1 242 ? 56.709  -1.488  12.228  1.00 53.02  ? 242  THR B OG1 1 
ATOM   4028 C  CG2 . THR B 1 242 ? 56.145  -3.495  13.404  1.00 50.72  ? 242  THR B CG2 1 
ATOM   4029 N  N   . ARG B 1 243 ? 53.726  -4.607  11.114  1.00 38.55  ? 243  ARG B N   1 
ATOM   4030 C  CA  . ARG B 1 243 ? 52.931  -5.820  11.118  1.00 39.34  ? 243  ARG B CA  1 
ATOM   4031 C  C   . ARG B 1 243 ? 51.530  -5.379  10.764  1.00 34.80  ? 243  ARG B C   1 
ATOM   4032 O  O   . ARG B 1 243 ? 51.240  -4.185  10.775  1.00 39.42  ? 243  ARG B O   1 
ATOM   4033 C  CB  . ARG B 1 243 ? 52.985  -6.545  12.473  1.00 48.66  ? 243  ARG B CB  1 
ATOM   4034 C  CG  . ARG B 1 243 ? 52.306  -5.835  13.624  1.00 58.26  ? 243  ARG B CG  1 
ATOM   4035 C  CD  . ARG B 1 243 ? 52.495  -6.609  14.923  1.00 62.34  ? 243  ARG B CD  1 
ATOM   4036 N  NE  . ARG B 1 243 ? 53.904  -6.903  15.144  1.00 64.23  ? 243  ARG B NE  1 
ATOM   4037 C  CZ  . ARG B 1 243 ? 54.750  -6.072  15.744  1.00 73.10  ? 243  ARG B CZ  1 
ATOM   4038 N  NH1 . ARG B 1 243 ? 54.316  -4.902  16.192  1.00 71.59  ? 243  ARG B NH1 1 
ATOM   4039 N  NH2 . ARG B 1 243 ? 56.028  -6.409  15.897  1.00 74.91  ? 243  ARG B NH2 1 
ATOM   4040 N  N   . VAL B 1 244 ? 50.679  -6.334  10.413  1.00 35.89  ? 244  VAL B N   1 
ATOM   4041 C  CA  . VAL B 1 244 ? 49.364  -6.025  9.886   1.00 33.83  ? 244  VAL B CA  1 
ATOM   4042 C  C   . VAL B 1 244 ? 48.319  -6.850  10.600  1.00 33.63  ? 244  VAL B C   1 
ATOM   4043 O  O   . VAL B 1 244 ? 48.495  -8.059  10.790  1.00 34.62  ? 244  VAL B O   1 
ATOM   4044 C  CB  . VAL B 1 244 ? 49.285  -6.328  8.371   1.00 38.89  ? 244  VAL B CB  1 
ATOM   4045 C  CG1 . VAL B 1 244 ? 47.872  -6.075  7.836   1.00 34.82  ? 244  VAL B CG1 1 
ATOM   4046 C  CG2 . VAL B 1 244 ? 50.291  -5.489  7.617   1.00 27.42  ? 244  VAL B CG2 1 
ATOM   4047 N  N   . TYR B 1 245 ? 47.245  -6.176  11.007  1.00 35.67  ? 245  TYR B N   1 
ATOM   4048 C  CA  . TYR B 1 245 ? 46.057  -6.812  11.571  1.00 35.95  ? 245  TYR B CA  1 
ATOM   4049 C  C   . TYR B 1 245 ? 44.902  -6.566  10.599  1.00 35.52  ? 245  TYR B C   1 
ATOM   4050 O  O   . TYR B 1 245 ? 44.905  -5.586  9.869   1.00 32.84  ? 245  TYR B O   1 
ATOM   4051 C  CB  . TYR B 1 245 ? 45.706  -6.204  12.946  1.00 32.73  ? 245  TYR B CB  1 
ATOM   4052 C  CG  . TYR B 1 245 ? 46.728  -6.467  14.063  1.00 39.91  ? 245  TYR B CG  1 
ATOM   4053 C  CD1 . TYR B 1 245 ? 47.937  -5.771  14.114  1.00 36.15  ? 245  TYR B CD1 1 
ATOM   4054 C  CD2 . TYR B 1 245 ? 46.465  -7.387  15.076  1.00 25.20  ? 245  TYR B CD2 1 
ATOM   4055 C  CE1 . TYR B 1 245 ? 48.867  -6.002  15.128  1.00 37.72  ? 245  TYR B CE1 1 
ATOM   4056 C  CE2 . TYR B 1 245 ? 47.394  -7.623  16.093  1.00 34.01  ? 245  TYR B CE2 1 
ATOM   4057 C  CZ  . TYR B 1 245 ? 48.588  -6.925  16.110  1.00 37.93  ? 245  TYR B CZ  1 
ATOM   4058 O  OH  . TYR B 1 245 ? 49.503  -7.152  17.109  1.00 48.47  ? 245  TYR B OH  1 
ATOM   4059 N  N   . ALA B 1 246 ? 43.914  -7.452  10.588  1.00 40.05  ? 246  ALA B N   1 
ATOM   4060 C  CA  . ALA B 1 246 ? 42.687  -7.193  9.857   1.00 38.69  ? 246  ALA B CA  1 
ATOM   4061 C  C   . ALA B 1 246 ? 41.531  -7.320  10.833  1.00 36.44  ? 246  ALA B C   1 
ATOM   4062 O  O   . ALA B 1 246 ? 41.459  -8.287  11.581  1.00 37.56  ? 246  ALA B O   1 
ATOM   4063 C  CB  . ALA B 1 246 ? 42.535  -8.176  8.693   1.00 37.04  ? 246  ALA B CB  1 
ATOM   4064 N  N   . ILE B 1 247 ? 40.651  -6.326  10.846  1.00 35.01  ? 247  ILE B N   1 
ATOM   4065 C  CA  . ILE B 1 247 ? 39.477  -6.335  11.712  1.00 29.77  ? 247  ILE B CA  1 
ATOM   4066 C  C   . ILE B 1 247 ? 38.224  -6.128  10.873  1.00 28.71  ? 247  ILE B C   1 
ATOM   4067 O  O   . ILE B 1 247 ? 38.026  -5.054  10.330  1.00 35.84  ? 247  ILE B O   1 
ATOM   4068 C  CB  . ILE B 1 247 ? 39.537  -5.197  12.763  1.00 35.14  ? 247  ILE B CB  1 
ATOM   4069 C  CG1 . ILE B 1 247 ? 40.741  -5.361  13.688  1.00 34.79  ? 247  ILE B CG1 1 
ATOM   4070 C  CG2 . ILE B 1 247 ? 38.241  -5.153  13.593  1.00 34.00  ? 247  ILE B CG2 1 
ATOM   4071 C  CD1 . ILE B 1 247 ? 40.961  -4.168  14.577  1.00 38.56  ? 247  ILE B CD1 1 
ATOM   4072 N  N   . LEU B 1 248 ? 37.398  -7.167  10.763  1.00 30.95  ? 248  LEU B N   1 
ATOM   4073 C  CA  . LEU B 1 248 ? 36.161  -7.128  9.989   1.00 36.07  ? 248  LEU B CA  1 
ATOM   4074 C  C   . LEU B 1 248 ? 34.977  -7.253  10.934  1.00 41.93  ? 248  LEU B C   1 
ATOM   4075 O  O   . LEU B 1 248 ? 35.027  -8.073  11.850  1.00 56.46  ? 248  LEU B O   1 
ATOM   4076 C  CB  . LEU B 1 248 ? 36.123  -8.314  9.028   1.00 37.97  ? 248  LEU B CB  1 
ATOM   4077 C  CG  . LEU B 1 248 ? 37.260  -8.476  8.016   1.00 48.59  ? 248  LEU B CG  1 
ATOM   4078 C  CD1 . LEU B 1 248 ? 37.661  -7.126  7.457   1.00 54.17  ? 248  LEU B CD1 1 
ATOM   4079 C  CD2 . LEU B 1 248 ? 38.458  -9.181  8.613   1.00 45.57  ? 248  LEU B CD2 1 
ATOM   4080 N  N   . THR B 1 249 ? 33.907  -6.479  10.750  1.00 27.61  ? 249  THR B N   1 
ATOM   4081 C  CA  . THR B 1 249 ? 32.741  -6.774  11.583  1.00 31.26  ? 249  THR B CA  1 
ATOM   4082 C  C   . THR B 1 249 ? 32.118  -8.154  11.269  1.00 39.89  ? 249  THR B C   1 
ATOM   4083 O  O   . THR B 1 249 ? 31.919  -8.971  12.176  1.00 36.42  ? 249  THR B O   1 
ATOM   4084 C  CB  . THR B 1 249 ? 31.706  -5.608  11.710  1.00 58.11  ? 249  THR B CB  1 
ATOM   4085 O  OG1 . THR B 1 249 ? 30.380  -6.142  11.877  1.00 51.24  ? 249  THR B OG1 1 
ATOM   4086 C  CG2 . THR B 1 249 ? 31.754  -4.680  10.518  1.00 65.16  ? 249  THR B CG2 1 
ATOM   4087 N  N   . HIS B 1 250 ? 31.887  -8.441  9.988   1.00 38.47  ? 250  HIS B N   1 
ATOM   4088 C  CA  . HIS B 1 250 ? 31.268  -9.710  9.596   1.00 38.45  ? 250  HIS B CA  1 
ATOM   4089 C  C   . HIS B 1 250 ? 32.253  -10.680 8.952   1.00 37.36  ? 250  HIS B C   1 
ATOM   4090 O  O   . HIS B 1 250 ? 32.740  -10.428 7.842   1.00 35.77  ? 250  HIS B O   1 
ATOM   4091 C  CB  . HIS B 1 250 ? 30.090  -9.465  8.635   1.00 31.37  ? 250  HIS B CB  1 
ATOM   4092 C  CG  . HIS B 1 250 ? 29.121  -8.438  9.120   1.00 29.66  ? 250  HIS B CG  1 
ATOM   4093 N  ND1 . HIS B 1 250 ? 28.340  -8.617  10.248  1.00 27.70  ? 250  HIS B ND1 1 
ATOM   4094 C  CD2 . HIS B 1 250 ? 28.804  -7.208  8.645   1.00 26.91  ? 250  HIS B CD2 1 
ATOM   4095 C  CE1 . HIS B 1 250 ? 27.586  -7.556  10.434  1.00 23.32  ? 250  HIS B CE1 1 
ATOM   4096 N  NE2 . HIS B 1 250 ? 27.855  -6.679  9.476   1.00 32.02  ? 250  HIS B NE2 1 
ATOM   4097 N  N   . GLY B 1 251 ? 32.513  -11.799 9.631   1.00 37.65  ? 251  GLY B N   1 
ATOM   4098 C  CA  . GLY B 1 251 ? 33.423  -12.817 9.123   1.00 43.69  ? 251  GLY B CA  1 
ATOM   4099 C  C   . GLY B 1 251 ? 32.755  -13.940 8.341   1.00 41.28  ? 251  GLY B C   1 
ATOM   4100 O  O   . GLY B 1 251 ? 32.400  -14.985 8.900   1.00 29.78  ? 251  GLY B O   1 
ATOM   4101 N  N   . ILE B 1 252 ? 32.575  -13.717 7.043   1.00 41.49  ? 252  ILE B N   1 
ATOM   4102 C  CA  . ILE B 1 252 ? 31.981  -14.719 6.158   1.00 46.04  ? 252  ILE B CA  1 
ATOM   4103 C  C   . ILE B 1 252 ? 32.963  -15.862 5.927   1.00 35.97  ? 252  ILE B C   1 
ATOM   4104 O  O   . ILE B 1 252 ? 32.653  -17.017 6.181   1.00 33.36  ? 252  ILE B O   1 
ATOM   4105 C  CB  . ILE B 1 252 ? 31.600  -14.114 4.793   1.00 52.48  ? 252  ILE B CB  1 
ATOM   4106 C  CG1 . ILE B 1 252 ? 30.988  -12.726 4.973   1.00 47.52  ? 252  ILE B CG1 1 
ATOM   4107 C  CG2 . ILE B 1 252 ? 30.633  -15.028 4.052   1.00 50.36  ? 252  ILE B CG2 1 
ATOM   4108 C  CD1 . ILE B 1 252 ? 29.516  -12.760 5.177   1.00 45.04  ? 252  ILE B CD1 1 
ATOM   4109 N  N   . PHE B 1 253 ? 34.156  -15.547 5.440   1.00 43.42  ? 253  PHE B N   1 
ATOM   4110 C  CA  . PHE B 1 253 ? 35.183  -16.576 5.354   1.00 44.45  ? 253  PHE B CA  1 
ATOM   4111 C  C   . PHE B 1 253 ? 34.678  -17.806 4.589   1.00 49.18  ? 253  PHE B C   1 
ATOM   4112 O  O   . PHE B 1 253 ? 34.851  -18.938 5.047   1.00 50.63  ? 253  PHE B O   1 
ATOM   4113 C  CB  . PHE B 1 253 ? 35.595  -17.019 6.765   1.00 40.01  ? 253  PHE B CB  1 
ATOM   4114 C  CG  . PHE B 1 253 ? 36.184  -15.926 7.606   1.00 34.19  ? 253  PHE B CG  1 
ATOM   4115 C  CD1 . PHE B 1 253 ? 35.989  -15.909 8.977   1.00 37.01  ? 253  PHE B CD1 1 
ATOM   4116 C  CD2 . PHE B 1 253 ? 36.951  -14.924 7.029   1.00 46.20  ? 253  PHE B CD2 1 
ATOM   4117 C  CE1 . PHE B 1 253 ? 36.546  -14.914 9.755   1.00 38.09  ? 253  PHE B CE1 1 
ATOM   4118 C  CE2 . PHE B 1 253 ? 37.508  -13.927 7.799   1.00 39.79  ? 253  PHE B CE2 1 
ATOM   4119 C  CZ  . PHE B 1 253 ? 37.305  -13.921 9.160   1.00 41.97  ? 253  PHE B CZ  1 
ATOM   4120 N  N   . SER B 1 254 ? 34.036  -17.593 3.444   1.00 43.51  ? 254  SER B N   1 
ATOM   4121 C  CA  . SER B 1 254 ? 33.686  -18.711 2.571   1.00 53.05  ? 254  SER B CA  1 
ATOM   4122 C  C   . SER B 1 254 ? 34.862  -19.059 1.660   1.00 56.27  ? 254  SER B C   1 
ATOM   4123 O  O   . SER B 1 254 ? 35.917  -18.429 1.727   1.00 58.09  ? 254  SER B O   1 
ATOM   4124 C  CB  . SER B 1 254 ? 32.466  -18.375 1.710   1.00 45.21  ? 254  SER B CB  1 
ATOM   4125 O  OG  . SER B 1 254 ? 32.788  -17.365 0.773   1.00 45.59  ? 254  SER B OG  1 
ATOM   4126 N  N   . GLY B 1 255 ? 34.668  -20.056 0.802   1.00 54.64  ? 255  GLY B N   1 
ATOM   4127 C  CA  . GLY B 1 255 ? 35.669  -20.421 -0.186  1.00 50.21  ? 255  GLY B CA  1 
ATOM   4128 C  C   . GLY B 1 255 ? 37.008  -20.755 0.429   1.00 48.92  ? 255  GLY B C   1 
ATOM   4129 O  O   . GLY B 1 255 ? 37.077  -21.498 1.406   1.00 58.56  ? 255  GLY B O   1 
ATOM   4130 N  N   . PRO B 1 256 ? 38.085  -20.204 -0.139  1.00 42.87  ? 256  PRO B N   1 
ATOM   4131 C  CA  . PRO B 1 256 ? 39.446  -20.453 0.350   1.00 49.62  ? 256  PRO B CA  1 
ATOM   4132 C  C   . PRO B 1 256 ? 39.899  -19.463 1.427   1.00 55.71  ? 256  PRO B C   1 
ATOM   4133 O  O   . PRO B 1 256 ? 41.080  -19.446 1.756   1.00 61.25  ? 256  PRO B O   1 
ATOM   4134 C  CB  . PRO B 1 256 ? 40.291  -20.265 -0.908  1.00 46.93  ? 256  PRO B CB  1 
ATOM   4135 C  CG  . PRO B 1 256 ? 39.556  -19.183 -1.670  1.00 49.73  ? 256  PRO B CG  1 
ATOM   4136 C  CD  . PRO B 1 256 ? 38.077  -19.403 -1.376  1.00 52.53  ? 256  PRO B CD  1 
ATOM   4137 N  N   . ALA B 1 257 ? 38.987  -18.654 1.957   1.00 53.15  ? 257  ALA B N   1 
ATOM   4138 C  CA  . ALA B 1 257 ? 39.340  -17.682 2.988   1.00 49.73  ? 257  ALA B CA  1 
ATOM   4139 C  C   . ALA B 1 257 ? 40.232  -18.279 4.068   1.00 50.50  ? 257  ALA B C   1 
ATOM   4140 O  O   . ALA B 1 257 ? 41.337  -17.778 4.314   1.00 47.26  ? 257  ALA B O   1 
ATOM   4141 C  CB  . ALA B 1 257 ? 38.090  -17.088 3.625   1.00 40.05  ? 257  ALA B CB  1 
ATOM   4142 N  N   . ILE B 1 258 ? 39.744  -19.326 4.734   1.00 42.77  ? 258  ILE B N   1 
ATOM   4143 C  CA  . ILE B 1 258 ? 40.474  -19.908 5.860   1.00 44.69  ? 258  ILE B CA  1 
ATOM   4144 C  C   . ILE B 1 258 ? 41.869  -20.377 5.447   1.00 47.60  ? 258  ILE B C   1 
ATOM   4145 O  O   . ILE B 1 258 ? 42.805  -20.329 6.241   1.00 55.80  ? 258  ILE B O   1 
ATOM   4146 C  CB  . ILE B 1 258 ? 39.685  -21.043 6.559   1.00 48.79  ? 258  ILE B CB  1 
ATOM   4147 C  CG1 . ILE B 1 258 ? 38.495  -20.463 7.328   1.00 43.42  ? 258  ILE B CG1 1 
ATOM   4148 C  CG2 . ILE B 1 258 ? 40.576  -21.806 7.536   1.00 50.13  ? 258  ILE B CG2 1 
ATOM   4149 C  CD1 . ILE B 1 258 ? 38.872  -19.416 8.366   1.00 41.20  ? 258  ILE B CD1 1 
ATOM   4150 N  N   . SER B 1 259 ? 42.004  -20.810 4.198   1.00 44.56  ? 259  SER B N   1 
ATOM   4151 C  CA  . SER B 1 259 ? 43.303  -21.178 3.657   1.00 53.86  ? 259  SER B CA  1 
ATOM   4152 C  C   . SER B 1 259 ? 44.121  -19.935 3.324   1.00 51.99  ? 259  SER B C   1 
ATOM   4153 O  O   . SER B 1 259 ? 45.310  -19.867 3.635   1.00 49.58  ? 259  SER B O   1 
ATOM   4154 C  CB  . SER B 1 259 ? 43.139  -22.049 2.410   1.00 68.07  ? 259  SER B CB  1 
ATOM   4155 O  OG  . SER B 1 259 ? 42.527  -23.289 2.741   1.00 79.18  ? 259  SER B OG  1 
ATOM   4156 N  N   . ARG B 1 260 ? 43.477  -18.965 2.680   1.00 45.95  ? 260  ARG B N   1 
ATOM   4157 C  CA  . ARG B 1 260 ? 44.098  -17.681 2.385   1.00 47.75  ? 260  ARG B CA  1 
ATOM   4158 C  C   . ARG B 1 260 ? 44.591  -16.981 3.650   1.00 48.98  ? 260  ARG B C   1 
ATOM   4159 O  O   . ARG B 1 260 ? 45.606  -16.299 3.629   1.00 49.52  ? 260  ARG B O   1 
ATOM   4160 C  CB  . ARG B 1 260 ? 43.123  -16.768 1.641   1.00 54.19  ? 260  ARG B CB  1 
ATOM   4161 C  CG  . ARG B 1 260 ? 43.445  -16.590 0.167   1.00 52.96  ? 260  ARG B CG  1 
ATOM   4162 C  CD  . ARG B 1 260 ? 42.427  -17.281 -0.694  1.00 49.96  ? 260  ARG B CD  1 
ATOM   4163 N  NE  . ARG B 1 260 ? 41.380  -16.361 -1.097  1.00 52.89  ? 260  ARG B NE  1 
ATOM   4164 C  CZ  . ARG B 1 260 ? 41.072  -16.101 -2.359  1.00 60.97  ? 260  ARG B CZ  1 
ATOM   4165 N  NH1 . ARG B 1 260 ? 41.733  -16.709 -3.331  1.00 59.29  ? 260  ARG B NH1 1 
ATOM   4166 N  NH2 . ARG B 1 260 ? 40.097  -15.242 -2.651  1.00 64.24  ? 260  ARG B NH2 1 
ATOM   4167 N  N   . ILE B 1 261 ? 43.873  -17.149 4.754   1.00 57.16  ? 261  ILE B N   1 
ATOM   4168 C  CA  . ILE B 1 261 ? 44.261  -16.485 5.992   1.00 58.36  ? 261  ILE B CA  1 
ATOM   4169 C  C   . ILE B 1 261 ? 45.467  -17.166 6.628   1.00 63.69  ? 261  ILE B C   1 
ATOM   4170 O  O   . ILE B 1 261 ? 46.455  -16.508 6.964   1.00 65.65  ? 261  ILE B O   1 
ATOM   4171 C  CB  . ILE B 1 261 ? 43.084  -16.372 6.981   1.00 54.25  ? 261  ILE B CB  1 
ATOM   4172 C  CG1 . ILE B 1 261 ? 42.100  -15.313 6.479   1.00 51.54  ? 261  ILE B CG1 1 
ATOM   4173 C  CG2 . ILE B 1 261 ? 43.581  -16.012 8.378   1.00 52.61  ? 261  ILE B CG2 1 
ATOM   4174 C  CD1 . ILE B 1 261 ? 40.845  -15.212 7.294   1.00 51.48  ? 261  ILE B CD1 1 
ATOM   4175 N  N   . ASN B 1 262 ? 45.386  -18.484 6.773   1.00 63.94  ? 262  ASN B N   1 
ATOM   4176 C  CA  . ASN B 1 262 ? 46.486  -19.276 7.319   1.00 52.50  ? 262  ASN B CA  1 
ATOM   4177 C  C   . ASN B 1 262 ? 47.817  -19.091 6.590   1.00 50.80  ? 262  ASN B C   1 
ATOM   4178 O  O   . ASN B 1 262 ? 48.878  -19.201 7.199   1.00 56.68  ? 262  ASN B O   1 
ATOM   4179 C  CB  . ASN B 1 262 ? 46.107  -20.756 7.355   1.00 49.93  ? 262  ASN B CB  1 
ATOM   4180 C  CG  . ASN B 1 262 ? 45.167  -21.092 8.504   1.00 53.07  ? 262  ASN B CG  1 
ATOM   4181 O  OD1 . ASN B 1 262 ? 45.226  -20.479 9.580   1.00 52.80  ? 262  ASN B OD1 1 
ATOM   4182 N  ND2 . ASN B 1 262 ? 44.304  -22.082 8.286   1.00 42.46  ? 262  ASN B ND2 1 
ATOM   4183 N  N   . ASN B 1 263 ? 47.764  -18.807 5.292   1.00 51.47  ? 263  ASN B N   1 
ATOM   4184 C  CA  . ASN B 1 263 ? 48.978  -18.572 4.515   1.00 57.08  ? 263  ASN B CA  1 
ATOM   4185 C  C   . ASN B 1 263 ? 49.366  -17.101 4.461   1.00 64.10  ? 263  ASN B C   1 
ATOM   4186 O  O   . ASN B 1 263 ? 50.443  -16.755 3.968   1.00 61.75  ? 263  ASN B O   1 
ATOM   4187 C  CB  . ASN B 1 263 ? 48.829  -19.093 3.079   1.00 63.23  ? 263  ASN B CB  1 
ATOM   4188 C  CG  . ASN B 1 263 ? 48.710  -20.604 3.012   1.00 68.20  ? 263  ASN B CG  1 
ATOM   4189 O  OD1 . ASN B 1 263 ? 48.006  -21.143 2.159   1.00 68.71  ? 263  ASN B OD1 1 
ATOM   4190 N  ND2 . ASN B 1 263 ? 49.399  -21.296 3.917   1.00 68.17  ? 263  ASN B ND2 1 
ATOM   4191 N  N   . ALA B 1 264 ? 48.487  -16.232 4.955   1.00 61.72  ? 264  ALA B N   1 
ATOM   4192 C  CA  . ALA B 1 264 ? 48.717  -14.793 4.853   1.00 54.56  ? 264  ALA B CA  1 
ATOM   4193 C  C   . ALA B 1 264 ? 49.538  -14.268 6.020   1.00 54.52  ? 264  ALA B C   1 
ATOM   4194 O  O   . ALA B 1 264 ? 49.617  -14.897 7.080   1.00 48.82  ? 264  ALA B O   1 
ATOM   4195 C  CB  . ALA B 1 264 ? 47.402  -14.045 4.746   1.00 45.36  ? 264  ALA B CB  1 
ATOM   4196 N  N   . CYS B 1 265 ? 50.130  -13.097 5.822   1.00 46.93  ? 265  CYS B N   1 
ATOM   4197 C  CA  . CYS B 1 265 ? 51.055  -12.537 6.785   1.00 45.78  ? 265  CYS B CA  1 
ATOM   4198 C  C   . CYS B 1 265 ? 50.366  -11.646 7.810   1.00 47.35  ? 265  CYS B C   1 
ATOM   4199 O  O   . CYS B 1 265 ? 50.891  -10.585 8.142   1.00 50.32  ? 265  CYS B O   1 
ATOM   4200 C  CB  . CYS B 1 265 ? 52.092  -11.714 6.044   1.00 45.54  ? 265  CYS B CB  1 
ATOM   4201 S  SG  . CYS B 1 265 ? 51.317  -10.461 4.992   1.00 80.83  ? 265  CYS B SG  1 
ATOM   4202 N  N   . PHE B 1 266 ? 49.198  -12.061 8.298   1.00 49.78  ? 266  PHE B N   1 
ATOM   4203 C  CA  . PHE B 1 266 ? 48.501  -11.330 9.360   1.00 47.98  ? 266  PHE B CA  1 
ATOM   4204 C  C   . PHE B 1 266 ? 49.064  -11.690 10.726  1.00 45.27  ? 266  PHE B C   1 
ATOM   4205 O  O   . PHE B 1 266 ? 49.410  -12.839 10.976  1.00 49.54  ? 266  PHE B O   1 
ATOM   4206 C  CB  . PHE B 1 266 ? 46.997  -11.641 9.377   1.00 41.79  ? 266  PHE B CB  1 
ATOM   4207 C  CG  . PHE B 1 266 ? 46.254  -11.164 8.161   1.00 46.12  ? 266  PHE B CG  1 
ATOM   4208 C  CD1 . PHE B 1 266 ? 45.736  -12.072 7.251   1.00 43.83  ? 266  PHE B CD1 1 
ATOM   4209 C  CD2 . PHE B 1 266 ? 46.079  -9.812  7.928   1.00 36.11  ? 266  PHE B CD2 1 
ATOM   4210 C  CE1 . PHE B 1 266 ? 45.057  -11.640 6.131   1.00 41.27  ? 266  PHE B CE1 1 
ATOM   4211 C  CE2 . PHE B 1 266 ? 45.403  -9.370  6.809   1.00 43.24  ? 266  PHE B CE2 1 
ATOM   4212 C  CZ  . PHE B 1 266 ? 44.890  -10.286 5.908   1.00 46.70  ? 266  PHE B CZ  1 
ATOM   4213 N  N   . GLU B 1 267 ? 49.132  -10.714 11.622  1.00 48.78  ? 267  GLU B N   1 
ATOM   4214 C  CA  . GLU B 1 267 ? 49.395  -11.026 13.018  1.00 47.01  ? 267  GLU B CA  1 
ATOM   4215 C  C   . GLU B 1 267 ? 48.147  -11.689 13.583  1.00 46.57  ? 267  GLU B C   1 
ATOM   4216 O  O   . GLU B 1 267 ? 48.232  -12.682 14.298  1.00 54.51  ? 267  GLU B O   1 
ATOM   4217 C  CB  . GLU B 1 267 ? 49.725  -9.763  13.809  1.00 54.42  ? 267  GLU B CB  1 
ATOM   4218 C  CG  . GLU B 1 267 ? 50.123  -10.017 15.253  1.00 66.57  ? 267  GLU B CG  1 
ATOM   4219 C  CD  . GLU B 1 267 ? 51.629  -10.099 15.445  1.00 73.69  ? 267  GLU B CD  1 
ATOM   4220 O  OE1 . GLU B 1 267 ? 52.088  -9.961  16.599  1.00 85.46  ? 267  GLU B OE1 1 
ATOM   4221 O  OE2 . GLU B 1 267 ? 52.355  -10.292 14.448  1.00 67.88  ? 267  GLU B OE2 1 
ATOM   4222 N  N   . ALA B 1 268 ? 46.987  -11.131 13.239  1.00 43.37  ? 268  ALA B N   1 
ATOM   4223 C  CA  . ALA B 1 268 ? 45.692  -11.624 13.710  1.00 35.61  ? 268  ALA B CA  1 
ATOM   4224 C  C   . ALA B 1 268 ? 44.573  -11.119 12.812  1.00 36.45  ? 268  ALA B C   1 
ATOM   4225 O  O   . ALA B 1 268 ? 44.688  -10.080 12.168  1.00 30.08  ? 268  ALA B O   1 
ATOM   4226 C  CB  . ALA B 1 268 ? 45.427  -11.185 15.165  1.00 29.13  ? 268  ALA B CB  1 
ATOM   4227 N  N   . VAL B 1 269 ? 43.472  -11.851 12.801  1.00 36.41  ? 269  VAL B N   1 
ATOM   4228 C  CA  . VAL B 1 269 ? 42.305  -11.453 12.054  1.00 37.02  ? 269  VAL B CA  1 
ATOM   4229 C  C   . VAL B 1 269 ? 41.168  -11.443 13.042  1.00 42.03  ? 269  VAL B C   1 
ATOM   4230 O  O   . VAL B 1 269 ? 40.840  -12.476 13.627  1.00 46.60  ? 269  VAL B O   1 
ATOM   4231 C  CB  . VAL B 1 269 ? 42.026  -12.436 10.924  1.00 33.78  ? 269  VAL B CB  1 
ATOM   4232 C  CG1 . VAL B 1 269 ? 40.764  -12.040 10.163  1.00 30.74  ? 269  VAL B CG1 1 
ATOM   4233 C  CG2 . VAL B 1 269 ? 43.241  -12.489 10.000  1.00 31.01  ? 269  VAL B CG2 1 
ATOM   4234 N  N   . VAL B 1 270 ? 40.595  -10.264 13.253  1.00 33.89  ? 270  VAL B N   1 
ATOM   4235 C  CA  . VAL B 1 270 ? 39.576  -10.080 14.281  1.00 29.79  ? 270  VAL B CA  1 
ATOM   4236 C  C   . VAL B 1 270 ? 38.201  -9.871  13.657  1.00 27.76  ? 270  VAL B C   1 
ATOM   4237 O  O   . VAL B 1 270 ? 38.049  -9.069  12.715  1.00 31.37  ? 270  VAL B O   1 
ATOM   4238 C  CB  . VAL B 1 270 ? 39.932  -8.887  15.182  1.00 34.43  ? 270  VAL B CB  1 
ATOM   4239 C  CG1 . VAL B 1 270 ? 38.893  -8.706  16.260  1.00 37.32  ? 270  VAL B CG1 1 
ATOM   4240 C  CG2 . VAL B 1 270 ? 41.323  -9.084  15.791  1.00 31.65  ? 270  VAL B CG2 1 
ATOM   4241 N  N   . VAL B 1 271 ? 37.207  -10.602 14.165  1.00 22.59  ? 271  VAL B N   1 
ATOM   4242 C  CA  . VAL B 1 271 ? 35.832  -10.494 13.667  1.00 25.75  ? 271  VAL B CA  1 
ATOM   4243 C  C   . VAL B 1 271 ? 34.869  -10.536 14.846  1.00 34.74  ? 271  VAL B C   1 
ATOM   4244 O  O   . VAL B 1 271 ? 35.237  -10.987 15.934  1.00 35.26  ? 271  VAL B O   1 
ATOM   4245 C  CB  . VAL B 1 271 ? 35.466  -11.643 12.662  1.00 28.15  ? 271  VAL B CB  1 
ATOM   4246 C  CG1 . VAL B 1 271 ? 36.184  -11.464 11.348  1.00 32.12  ? 271  VAL B CG1 1 
ATOM   4247 C  CG2 . VAL B 1 271 ? 35.791  -13.005 13.246  1.00 32.72  ? 271  VAL B CG2 1 
ATOM   4248 N  N   . THR B 1 272 ? 33.643  -10.062 14.649  1.00 27.43  ? 272  THR B N   1 
ATOM   4249 C  CA  . THR B 1 272 ? 32.630  -10.219 15.685  1.00 32.54  ? 272  THR B CA  1 
ATOM   4250 C  C   . THR B 1 272 ? 31.947  -11.566 15.501  1.00 34.25  ? 272  THR B C   1 
ATOM   4251 O  O   . THR B 1 272 ? 32.205  -12.275 14.538  1.00 27.10  ? 272  THR B O   1 
ATOM   4252 C  CB  . THR B 1 272 ? 31.548  -9.141  15.618  1.00 25.31  ? 272  THR B CB  1 
ATOM   4253 O  OG1 . THR B 1 272 ? 30.797  -9.308  14.410  1.00 34.45  ? 272  THR B OG1 1 
ATOM   4254 C  CG2 . THR B 1 272 ? 32.158  -7.758  15.678  1.00 20.10  ? 272  THR B CG2 1 
ATOM   4255 N  N   . ASN B 1 273 ? 31.075  -11.926 16.428  1.00 34.75  ? 273  ASN B N   1 
ATOM   4256 C  CA  . ASN B 1 273 ? 30.313  -13.145 16.253  1.00 37.38  ? 273  ASN B CA  1 
ATOM   4257 C  C   . ASN B 1 273 ? 28.918  -12.894 15.669  1.00 32.01  ? 273  ASN B C   1 
ATOM   4258 O  O   . ASN B 1 273 ? 27.981  -13.614 15.989  1.00 39.04  ? 273  ASN B O   1 
ATOM   4259 C  CB  . ASN B 1 273 ? 30.249  -13.950 17.569  1.00 37.68  ? 273  ASN B CB  1 
ATOM   4260 C  CG  . ASN B 1 273 ? 29.645  -13.154 18.725  1.00 40.17  ? 273  ASN B CG  1 
ATOM   4261 O  OD1 . ASN B 1 273 ? 29.570  -11.924 18.688  1.00 35.47  ? 273  ASN B OD1 1 
ATOM   4262 N  ND2 . ASN B 1 273 ? 29.217  -13.860 19.761  1.00 42.33  ? 273  ASN B ND2 1 
ATOM   4263 N  N   . THR B 1 274 ? 28.780  -11.880 14.809  1.00 29.74  ? 274  THR B N   1 
ATOM   4264 C  CA  . THR B 1 274 ? 27.546  -11.706 14.026  1.00 27.06  ? 274  THR B CA  1 
ATOM   4265 C  C   . THR B 1 274 ? 27.322  -12.945 13.135  1.00 37.68  ? 274  THR B C   1 
ATOM   4266 O  O   . THR B 1 274 ? 26.198  -13.280 12.747  1.00 34.73  ? 274  THR B O   1 
ATOM   4267 C  CB  . THR B 1 274 ? 27.566  -10.420 13.151  1.00 34.80  ? 274  THR B CB  1 
ATOM   4268 O  OG1 . THR B 1 274 ? 28.689  -10.440 12.264  1.00 34.46  ? 274  THR B OG1 1 
ATOM   4269 C  CG2 . THR B 1 274 ? 27.625  -9.172  14.003  1.00 27.93  ? 274  THR B CG2 1 
ATOM   4270 N  N   . ILE B 1 275 ? 28.423  -13.610 12.817  1.00 35.25  ? 275  ILE B N   1 
ATOM   4271 C  CA  . ILE B 1 275 ? 28.418  -14.887 12.123  1.00 30.46  ? 275  ILE B CA  1 
ATOM   4272 C  C   . ILE B 1 275 ? 29.236  -15.834 12.992  1.00 44.54  ? 275  ILE B C   1 
ATOM   4273 O  O   . ILE B 1 275 ? 30.277  -15.446 13.515  1.00 51.13  ? 275  ILE B O   1 
ATOM   4274 C  CB  . ILE B 1 275 ? 29.050  -14.741 10.731  1.00 30.45  ? 275  ILE B CB  1 
ATOM   4275 C  CG1 . ILE B 1 275 ? 28.196  -13.794 9.878   1.00 37.22  ? 275  ILE B CG1 1 
ATOM   4276 C  CG2 . ILE B 1 275 ? 29.195  -16.096 10.045  1.00 38.95  ? 275  ILE B CG2 1 
ATOM   4277 C  CD1 . ILE B 1 275 ? 28.766  -13.523 8.500   1.00 40.80  ? 275  ILE B CD1 1 
ATOM   4278 N  N   . PRO B 1 276 ? 28.753  -17.070 13.184  1.00 46.99  ? 276  PRO B N   1 
ATOM   4279 C  CA  . PRO B 1 276 ? 29.405  -18.014 14.108  1.00 45.31  ? 276  PRO B CA  1 
ATOM   4280 C  C   . PRO B 1 276 ? 30.793  -18.412 13.619  1.00 44.37  ? 276  PRO B C   1 
ATOM   4281 O  O   . PRO B 1 276 ? 30.967  -18.640 12.422  1.00 34.56  ? 276  PRO B O   1 
ATOM   4282 C  CB  . PRO B 1 276 ? 28.454  -19.220 14.124  1.00 39.15  ? 276  PRO B CB  1 
ATOM   4283 C  CG  . PRO B 1 276 ? 27.646  -19.105 12.874  1.00 41.78  ? 276  PRO B CG  1 
ATOM   4284 C  CD  . PRO B 1 276 ? 27.545  -17.635 12.561  1.00 41.25  ? 276  PRO B CD  1 
ATOM   4285 N  N   . GLN B 1 277 ? 31.762  -18.491 14.529  1.00 42.09  ? 277  GLN B N   1 
ATOM   4286 C  CA  . GLN B 1 277 ? 33.159  -18.637 14.120  1.00 45.99  ? 277  GLN B CA  1 
ATOM   4287 C  C   . GLN B 1 277 ? 33.877  -19.875 14.660  1.00 44.59  ? 277  GLN B C   1 
ATOM   4288 O  O   . GLN B 1 277 ? 35.020  -20.144 14.279  1.00 45.49  ? 277  GLN B O   1 
ATOM   4289 C  CB  . GLN B 1 277 ? 33.939  -17.371 14.493  1.00 41.01  ? 277  GLN B CB  1 
ATOM   4290 C  CG  . GLN B 1 277 ? 33.259  -16.084 14.035  1.00 44.00  ? 277  GLN B CG  1 
ATOM   4291 C  CD  . GLN B 1 277 ? 33.205  -15.933 12.509  1.00 48.14  ? 277  GLN B CD  1 
ATOM   4292 O  OE1 . GLN B 1 277 ? 32.472  -15.097 11.985  1.00 45.09  ? 277  GLN B OE1 1 
ATOM   4293 N  NE2 . GLN B 1 277 ? 33.998  -16.728 11.802  1.00 48.75  ? 277  GLN B NE2 1 
ATOM   4294 N  N   . GLU B 1 278 ? 33.205  -20.628 15.532  0.87 43.34  ? 278  GLU B N   1 
ATOM   4295 C  CA  . GLU B 1 278 ? 33.840  -21.735 16.251  0.87 47.19  ? 278  GLU B CA  1 
ATOM   4296 C  C   . GLU B 1 278 ? 34.504  -22.709 15.291  0.87 51.93  ? 278  GLU B C   1 
ATOM   4297 O  O   . GLU B 1 278 ? 35.722  -22.916 15.344  0.87 46.57  ? 278  GLU B O   1 
ATOM   4298 C  CB  . GLU B 1 278 ? 32.835  -22.473 17.143  0.87 42.03  ? 278  GLU B CB  1 
ATOM   4299 C  CG  . GLU B 1 278 ? 31.911  -21.544 17.941  0.87 60.26  ? 278  GLU B CG  1 
ATOM   4300 C  CD  . GLU B 1 278 ? 30.835  -20.891 17.061  0.87 70.15  ? 278  GLU B CD  1 
ATOM   4301 O  OE1 . GLU B 1 278 ? 30.469  -21.496 16.027  0.87 70.55  ? 278  GLU B OE1 1 
ATOM   4302 O  OE2 . GLU B 1 278 ? 30.367  -19.776 17.395  0.87 71.31  ? 278  GLU B OE2 1 
ATOM   4303 N  N   . ASP B 1 279 ? 33.699  -23.297 14.412  1.00 50.80  ? 279  ASP B N   1 
ATOM   4304 C  CA  . ASP B 1 279 ? 34.204  -24.229 13.414  1.00 59.89  ? 279  ASP B CA  1 
ATOM   4305 C  C   . ASP B 1 279 ? 35.375  -23.620 12.660  1.00 56.74  ? 279  ASP B C   1 
ATOM   4306 O  O   . ASP B 1 279 ? 36.409  -24.261 12.488  1.00 56.99  ? 279  ASP B O   1 
ATOM   4307 C  CB  . ASP B 1 279 ? 33.095  -24.615 12.425  1.00 68.95  ? 279  ASP B CB  1 
ATOM   4308 N  N   . LYS B 1 280 ? 35.205  -22.377 12.219  1.00 54.12  ? 280  LYS B N   1 
ATOM   4309 C  CA  . LYS B 1 280 ? 36.231  -21.680 11.454  1.00 54.64  ? 280  LYS B CA  1 
ATOM   4310 C  C   . LYS B 1 280 ? 37.527  -21.506 12.250  1.00 59.60  ? 280  LYS B C   1 
ATOM   4311 O  O   . LYS B 1 280 ? 38.621  -21.554 11.687  1.00 62.68  ? 280  LYS B O   1 
ATOM   4312 C  CB  . LYS B 1 280 ? 35.712  -20.320 10.979  1.00 54.14  ? 280  LYS B CB  1 
ATOM   4313 C  CG  . LYS B 1 280 ? 34.604  -20.396 9.926   1.00 57.69  ? 280  LYS B CG  1 
ATOM   4314 C  CD  . LYS B 1 280 ? 35.166  -20.730 8.554   1.00 61.75  ? 280  LYS B CD  1 
ATOM   4315 C  CE  . LYS B 1 280 ? 34.069  -20.925 7.517   1.00 60.51  ? 280  LYS B CE  1 
ATOM   4316 N  NZ  . LYS B 1 280 ? 33.169  -19.744 7.452   1.00 62.65  ? 280  LYS B NZ  1 
ATOM   4317 N  N   . MET B 1 281 ? 37.406  -21.301 13.559  1.00 59.22  ? 281  MET B N   1 
ATOM   4318 C  CA  . MET B 1 281 ? 38.581  -21.061 14.392  1.00 59.97  ? 281  MET B CA  1 
ATOM   4319 C  C   . MET B 1 281 ? 39.416  -22.325 14.602  1.00 57.97  ? 281  MET B C   1 
ATOM   4320 O  O   . MET B 1 281 ? 40.647  -22.266 14.640  1.00 55.53  ? 281  MET B O   1 
ATOM   4321 C  CB  . MET B 1 281 ? 38.181  -20.436 15.735  1.00 63.44  ? 281  MET B CB  1 
ATOM   4322 C  CG  . MET B 1 281 ? 37.573  -19.047 15.596  1.00 62.97  ? 281  MET B CG  1 
ATOM   4323 S  SD  . MET B 1 281 ? 37.035  -18.323 17.156  1.00 62.64  ? 281  MET B SD  1 
ATOM   4324 C  CE  . MET B 1 281 ? 38.613  -18.027 17.955  1.00 77.15  ? 281  MET B CE  1 
ATOM   4325 N  N   . LYS B 1 282 ? 38.745  -23.467 14.721  0.97 58.11  ? 282  LYS B N   1 
ATOM   4326 C  CA  . LYS B 1 282 ? 39.436  -24.745 14.877  0.97 65.14  ? 282  LYS B CA  1 
ATOM   4327 C  C   . LYS B 1 282 ? 40.480  -24.953 13.784  0.97 69.90  ? 282  LYS B C   1 
ATOM   4328 O  O   . LYS B 1 282 ? 41.490  -25.620 14.004  0.97 67.96  ? 282  LYS B O   1 
ATOM   4329 C  CB  . LYS B 1 282 ? 38.439  -25.911 14.866  0.97 66.18  ? 282  LYS B CB  1 
ATOM   4330 C  CG  . LYS B 1 282 ? 37.391  -25.856 15.974  0.97 73.34  ? 282  LYS B CG  1 
ATOM   4331 C  CD  . LYS B 1 282 ? 36.397  -27.006 15.869  0.97 76.21  ? 282  LYS B CD  1 
ATOM   4332 C  CE  . LYS B 1 282 ? 37.033  -28.341 16.248  0.97 77.09  ? 282  LYS B CE  1 
ATOM   4333 N  N   . HIS B 1 283 ? 40.234  -24.375 12.611  1.00 72.85  ? 283  HIS B N   1 
ATOM   4334 C  CA  . HIS B 1 283 ? 41.099  -24.586 11.452  1.00 75.55  ? 283  HIS B CA  1 
ATOM   4335 C  C   . HIS B 1 283 ? 41.875  -23.322 11.073  1.00 68.52  ? 283  HIS B C   1 
ATOM   4336 O  O   . HIS B 1 283 ? 42.476  -23.238 9.995   1.00 63.36  ? 283  HIS B O   1 
ATOM   4337 C  CB  . HIS B 1 283 ? 40.266  -25.098 10.274  1.00 87.74  ? 283  HIS B CB  1 
ATOM   4338 C  CG  . HIS B 1 283 ? 39.406  -26.276 10.622  1.00 101.17 ? 283  HIS B CG  1 
ATOM   4339 N  ND1 . HIS B 1 283 ? 39.782  -27.576 10.363  1.00 104.20 ? 283  HIS B ND1 1 
ATOM   4340 C  CD2 . HIS B 1 283 ? 38.201  -26.348 11.237  1.00 105.58 ? 283  HIS B CD2 1 
ATOM   4341 C  CE1 . HIS B 1 283 ? 38.838  -28.398 10.790  1.00 106.23 ? 283  HIS B CE1 1 
ATOM   4342 N  NE2 . HIS B 1 283 ? 37.868  -27.678 11.325  1.00 106.22 ? 283  HIS B NE2 1 
ATOM   4343 N  N   . CYS B 1 284 ? 41.861  -22.345 11.975  1.00 57.23  ? 284  CYS B N   1 
ATOM   4344 C  CA  . CYS B 1 284 ? 42.511  -21.069 11.731  1.00 56.89  ? 284  CYS B CA  1 
ATOM   4345 C  C   . CYS B 1 284 ? 42.785  -20.366 13.055  1.00 61.88  ? 284  CYS B C   1 
ATOM   4346 O  O   . CYS B 1 284 ? 41.869  -19.880 13.716  1.00 58.68  ? 284  CYS B O   1 
ATOM   4347 C  CB  . CYS B 1 284 ? 41.643  -20.194 10.823  1.00 58.49  ? 284  CYS B CB  1 
ATOM   4348 S  SG  . CYS B 1 284 ? 42.499  -18.745 10.154  1.00 50.80  ? 284  CYS B SG  1 
ATOM   4349 N  N   . SER B 1 285 ? 44.057  -20.315 13.436  1.00 71.06  ? 285  SER B N   1 
ATOM   4350 C  CA  . SER B 1 285 ? 44.447  -19.785 14.741  1.00 70.80  ? 285  SER B CA  1 
ATOM   4351 C  C   . SER B 1 285 ? 44.758  -18.281 14.738  1.00 60.22  ? 285  SER B C   1 
ATOM   4352 O  O   . SER B 1 285 ? 44.923  -17.672 15.801  1.00 57.43  ? 285  SER B O   1 
ATOM   4353 C  CB  . SER B 1 285 ? 45.622  -20.584 15.307  1.00 70.69  ? 285  SER B CB  1 
ATOM   4354 O  OG  . SER B 1 285 ? 46.554  -20.889 14.285  1.00 72.14  ? 285  SER B OG  1 
ATOM   4355 N  N   . LYS B 1 286 ? 44.832  -17.684 13.550  1.00 49.18  ? 286  LYS B N   1 
ATOM   4356 C  CA  . LYS B 1 286 ? 44.946  -16.227 13.452  1.00 47.10  ? 286  LYS B CA  1 
ATOM   4357 C  C   . LYS B 1 286 ? 43.661  -15.508 13.883  1.00 46.70  ? 286  LYS B C   1 
ATOM   4358 O  O   . LYS B 1 286 ? 43.676  -14.315 14.178  1.00 50.33  ? 286  LYS B O   1 
ATOM   4359 C  CB  . LYS B 1 286 ? 45.324  -15.801 12.039  1.00 41.54  ? 286  LYS B CB  1 
ATOM   4360 C  CG  . LYS B 1 286 ? 46.748  -16.171 11.646  1.00 52.95  ? 286  LYS B CG  1 
ATOM   4361 C  CD  . LYS B 1 286 ? 47.137  -15.508 10.333  1.00 58.73  ? 286  LYS B CD  1 
ATOM   4362 C  CE  . LYS B 1 286 ? 48.575  -15.827 9.956   1.00 65.12  ? 286  LYS B CE  1 
ATOM   4363 N  NZ  . LYS B 1 286 ? 48.651  -16.773 8.808   1.00 69.76  ? 286  LYS B NZ  1 
ATOM   4364 N  N   . ILE B 1 287 ? 42.558  -16.247 13.941  1.00 43.60  ? 287  ILE B N   1 
ATOM   4365 C  CA  . ILE B 1 287 ? 41.257  -15.647 14.200  1.00 49.01  ? 287  ILE B CA  1 
ATOM   4366 C  C   . ILE B 1 287 ? 40.934  -15.411 15.674  1.00 46.62  ? 287  ILE B C   1 
ATOM   4367 O  O   . ILE B 1 287 ? 41.010  -16.314 16.509  1.00 48.58  ? 287  ILE B O   1 
ATOM   4368 C  CB  . ILE B 1 287 ? 40.115  -16.459 13.548  1.00 43.66  ? 287  ILE B CB  1 
ATOM   4369 C  CG1 . ILE B 1 287 ? 40.191  -16.350 12.024  1.00 43.50  ? 287  ILE B CG1 1 
ATOM   4370 C  CG2 . ILE B 1 287 ? 38.761  -15.954 14.025  1.00 35.77  ? 287  ILE B CG2 1 
ATOM   4371 C  CD1 . ILE B 1 287 ? 39.227  -17.254 11.311  1.00 45.36  ? 287  ILE B CD1 1 
ATOM   4372 N  N   . GLN B 1 288 ? 40.557  -14.179 15.973  1.00 39.05  ? 288  GLN B N   1 
ATOM   4373 C  CA  . GLN B 1 288 ? 40.037  -13.839 17.283  1.00 38.86  ? 288  GLN B CA  1 
ATOM   4374 C  C   . GLN B 1 288 ? 38.654  -13.241 17.147  1.00 36.16  ? 288  GLN B C   1 
ATOM   4375 O  O   . GLN B 1 288 ? 38.368  -12.547 16.176  1.00 41.36  ? 288  GLN B O   1 
ATOM   4376 C  CB  . GLN B 1 288 ? 40.988  -12.887 18.014  1.00 31.37  ? 288  GLN B CB  1 
ATOM   4377 C  CG  . GLN B 1 288 ? 42.270  -13.592 18.448  1.00 34.13  ? 288  GLN B CG  1 
ATOM   4378 C  CD  . GLN B 1 288 ? 43.303  -12.636 18.963  1.00 41.59  ? 288  GLN B CD  1 
ATOM   4379 O  OE1 . GLN B 1 288 ? 44.440  -12.620 18.494  1.00 41.29  ? 288  GLN B OE1 1 
ATOM   4380 N  NE2 . GLN B 1 288 ? 42.915  -11.818 19.931  1.00 40.50  ? 288  GLN B NE2 1 
ATOM   4381 N  N   . VAL B 1 289 ? 37.796  -13.521 18.122  1.00 37.25  ? 289  VAL B N   1 
ATOM   4382 C  CA  . VAL B 1 289 ? 36.396  -13.130 18.046  1.00 36.31  ? 289  VAL B CA  1 
ATOM   4383 C  C   . VAL B 1 289 ? 36.009  -12.140 19.115  1.00 34.38  ? 289  VAL B C   1 
ATOM   4384 O  O   . VAL B 1 289 ? 36.260  -12.363 20.295  1.00 47.84  ? 289  VAL B O   1 
ATOM   4385 C  CB  . VAL B 1 289 ? 35.468  -14.347 18.180  1.00 44.07  ? 289  VAL B CB  1 
ATOM   4386 C  CG1 . VAL B 1 289 ? 34.025  -13.896 18.245  1.00 41.08  ? 289  VAL B CG1 1 
ATOM   4387 C  CG2 . VAL B 1 289 ? 35.672  -15.292 17.011  1.00 45.72  ? 289  VAL B CG2 1 
ATOM   4388 N  N   . ILE B 1 290 ? 35.396  -11.040 18.699  1.00 34.23  ? 290  ILE B N   1 
ATOM   4389 C  CA  . ILE B 1 290 ? 34.769  -10.126 19.636  1.00 33.31  ? 290  ILE B CA  1 
ATOM   4390 C  C   . ILE B 1 290 ? 33.309  -10.539 19.804  1.00 38.99  ? 290  ILE B C   1 
ATOM   4391 O  O   . ILE B 1 290 ? 32.567  -10.643 18.829  1.00 26.76  ? 290  ILE B O   1 
ATOM   4392 C  CB  . ILE B 1 290 ? 34.802  -8.680  19.128  1.00 34.36  ? 290  ILE B CB  1 
ATOM   4393 C  CG1 . ILE B 1 290 ? 36.236  -8.187  18.976  1.00 40.07  ? 290  ILE B CG1 1 
ATOM   4394 C  CG2 . ILE B 1 290 ? 34.023  -7.748  20.075  1.00 32.38  ? 290  ILE B CG2 1 
ATOM   4395 C  CD1 . ILE B 1 290 ? 36.339  -6.840  18.255  1.00 37.99  ? 290  ILE B CD1 1 
ATOM   4396 N  N   . ASP B 1 291 ? 32.894  -10.761 21.045  1.00 42.36  ? 291  ASP B N   1 
ATOM   4397 C  CA  . ASP B 1 291 ? 31.505  -11.091 21.320  1.00 41.71  ? 291  ASP B CA  1 
ATOM   4398 C  C   . ASP B 1 291 ? 30.619  -9.850  21.254  1.00 40.37  ? 291  ASP B C   1 
ATOM   4399 O  O   . ASP B 1 291 ? 30.789  -8.928  22.036  1.00 39.77  ? 291  ASP B O   1 
ATOM   4400 C  CB  . ASP B 1 291 ? 31.387  -11.734 22.696  1.00 41.82  ? 291  ASP B CB  1 
ATOM   4401 C  CG  . ASP B 1 291 ? 29.952  -11.970 23.103  1.00 55.40  ? 291  ASP B CG  1 
ATOM   4402 O  OD1 . ASP B 1 291 ? 29.106  -12.197 22.208  1.00 53.39  ? 291  ASP B OD1 1 
ATOM   4403 O  OD2 . ASP B 1 291 ? 29.669  -11.916 24.320  1.00 65.56  ? 291  ASP B OD2 1 
ATOM   4404 N  N   . ILE B 1 292 ? 29.664  -9.814  20.330  1.00 33.56  ? 292  ILE B N   1 
ATOM   4405 C  CA  . ILE B 1 292 ? 28.784  -8.653  20.269  1.00 34.26  ? 292  ILE B CA  1 
ATOM   4406 C  C   . ILE B 1 292 ? 27.375  -8.921  20.814  1.00 41.72  ? 292  ILE B C   1 
ATOM   4407 O  O   . ILE B 1 292 ? 26.474  -8.094  20.656  1.00 41.77  ? 292  ILE B O   1 
ATOM   4408 C  CB  . ILE B 1 292 ? 28.756  -7.979  18.852  1.00 41.08  ? 292  ILE B CB  1 
ATOM   4409 C  CG1 . ILE B 1 292 ? 28.358  -8.961  17.743  1.00 32.76  ? 292  ILE B CG1 1 
ATOM   4410 C  CG2 . ILE B 1 292 ? 30.121  -7.386  18.537  1.00 40.67  ? 292  ILE B CG2 1 
ATOM   4411 C  CD1 . ILE B 1 292 ? 27.006  -9.608  17.923  1.00 28.48  ? 292  ILE B CD1 1 
ATOM   4412 N  N   . SER B 1 293 ? 27.199  -10.059 21.483  1.00 32.72  ? 293  SER B N   1 
ATOM   4413 C  CA  . SER B 1 293 ? 25.893  -10.408 22.023  1.00 31.24  ? 293  SER B CA  1 
ATOM   4414 C  C   . SER B 1 293 ? 25.382  -9.375  23.022  1.00 34.05  ? 293  SER B C   1 
ATOM   4415 O  O   . SER B 1 293 ? 24.175  -9.150  23.108  1.00 32.20  ? 293  SER B O   1 
ATOM   4416 C  CB  . SER B 1 293 ? 25.881  -11.823 22.624  1.00 36.35  ? 293  SER B CB  1 
ATOM   4417 O  OG  . SER B 1 293 ? 26.866  -11.997 23.634  1.00 36.75  ? 293  SER B OG  1 
ATOM   4418 N  N   . MET B 1 294 ? 26.286  -8.722  23.745  0.70 18.25  ? 294  MET B N   1 
ATOM   4419 C  CA  . MET B 1 294 ? 25.861  -7.821  24.810  0.70 27.95  ? 294  MET B CA  1 
ATOM   4420 C  C   . MET B 1 294 ? 25.238  -6.580  24.209  0.70 22.98  ? 294  MET B C   1 
ATOM   4421 O  O   . MET B 1 294 ? 24.248  -6.050  24.703  0.70 23.87  ? 294  MET B O   1 
ATOM   4422 C  CB  . MET B 1 294 ? 27.036  -7.442  25.724  0.70 36.44  ? 294  MET B CB  1 
ATOM   4423 C  CG  . MET B 1 294 ? 28.391  -7.947  25.236  0.70 51.03  ? 294  MET B CG  1 
ATOM   4424 S  SD  . MET B 1 294 ? 29.009  -7.080  23.776  0.70 92.38  ? 294  MET B SD  1 
ATOM   4425 C  CE  . MET B 1 294 ? 29.987  -5.787  24.542  0.70 85.65  ? 294  MET B CE  1 
ATOM   4426 N  N   . ILE B 1 295 ? 25.849  -6.124  23.130  1.00 24.44  ? 295  ILE B N   1 
ATOM   4427 C  CA  . ILE B 1 295 ? 25.367  -4.970  22.384  1.00 32.71  ? 295  ILE B CA  1 
ATOM   4428 C  C   . ILE B 1 295 ? 23.975  -5.234  21.814  1.00 30.38  ? 295  ILE B C   1 
ATOM   4429 O  O   . ILE B 1 295 ? 23.045  -4.435  21.977  1.00 38.29  ? 295  ILE B O   1 
ATOM   4430 C  CB  . ILE B 1 295 ? 26.353  -4.632  21.262  1.00 33.10  ? 295  ILE B CB  1 
ATOM   4431 C  CG1 . ILE B 1 295 ? 27.700  -4.242  21.882  1.00 37.40  ? 295  ILE B CG1 1 
ATOM   4432 C  CG2 . ILE B 1 295 ? 25.794  -3.551  20.352  1.00 29.67  ? 295  ILE B CG2 1 
ATOM   4433 C  CD1 . ILE B 1 295 ? 28.890  -4.433  20.971  1.00 39.78  ? 295  ILE B CD1 1 
ATOM   4434 N  N   . LEU B 1 296 ? 23.825  -6.385  21.179  1.00 25.28  ? 296  LEU B N   1 
ATOM   4435 C  CA  . LEU B 1 296 ? 22.536  -6.757  20.631  1.00 25.74  ? 296  LEU B CA  1 
ATOM   4436 C  C   . LEU B 1 296 ? 21.518  -6.913  21.754  1.00 25.50  ? 296  LEU B C   1 
ATOM   4437 O  O   . LEU B 1 296 ? 20.420  -6.360  21.686  1.00 25.55  ? 296  LEU B O   1 
ATOM   4438 C  CB  . LEU B 1 296 ? 22.665  -8.033  19.814  1.00 17.03  ? 296  LEU B CB  1 
ATOM   4439 C  CG  . LEU B 1 296 ? 23.430  -7.900  18.480  1.00 30.51  ? 296  LEU B CG  1 
ATOM   4440 C  CD1 . LEU B 1 296 ? 23.693  -9.269  17.894  1.00 18.12  ? 296  LEU B CD1 1 
ATOM   4441 C  CD2 . LEU B 1 296 ? 22.671  -7.050  17.469  1.00 25.33  ? 296  LEU B CD2 1 
ATOM   4442 N  N   . ALA B 1 297 ? 21.897  -7.656  22.795  1.00 21.89  ? 297  ALA B N   1 
ATOM   4443 C  CA  . ALA B 1 297 ? 21.037  -7.840  23.981  1.00 28.99  ? 297  ALA B CA  1 
ATOM   4444 C  C   . ALA B 1 297 ? 20.634  -6.505  24.578  1.00 18.22  ? 297  ALA B C   1 
ATOM   4445 O  O   . ALA B 1 297 ? 19.477  -6.284  24.915  1.00 28.62  ? 297  ALA B O   1 
ATOM   4446 C  CB  . ALA B 1 297 ? 21.735  -8.714  25.034  1.00 20.73  ? 297  ALA B CB  1 
ATOM   4447 N  N   . GLU B 1 298 ? 21.590  -5.595  24.670  1.00 28.13  ? 298  GLU B N   1 
ATOM   4448 C  CA  . GLU B 1 298 ? 21.328  -4.257  25.178  1.00 38.85  ? 298  GLU B CA  1 
ATOM   4449 C  C   . GLU B 1 298 ? 20.373  -3.440  24.290  1.00 41.39  ? 298  GLU B C   1 
ATOM   4450 O  O   . GLU B 1 298 ? 19.493  -2.748  24.801  1.00 36.66  ? 298  GLU B O   1 
ATOM   4451 C  CB  . GLU B 1 298 ? 22.651  -3.513  25.384  1.00 46.27  ? 298  GLU B CB  1 
ATOM   4452 C  CG  . GLU B 1 298 ? 22.524  -2.216  26.139  1.00 54.72  ? 298  GLU B CG  1 
ATOM   4453 C  CD  . GLU B 1 298 ? 22.463  -2.412  27.645  1.00 68.11  ? 298  GLU B CD  1 
ATOM   4454 O  OE1 . GLU B 1 298 ? 22.424  -3.580  28.102  1.00 64.62  ? 298  GLU B OE1 1 
ATOM   4455 O  OE2 . GLU B 1 298 ? 22.457  -1.388  28.369  1.00 73.11  ? 298  GLU B OE2 1 
ATOM   4456 N  N   . ALA B 1 299 ? 20.542  -3.514  22.968  1.00 38.98  ? 299  ALA B N   1 
ATOM   4457 C  CA  . ALA B 1 299 ? 19.643  -2.810  22.039  1.00 29.93  ? 299  ALA B CA  1 
ATOM   4458 C  C   . ALA B 1 299 ? 18.206  -3.314  22.135  1.00 23.81  ? 299  ALA B C   1 
ATOM   4459 O  O   . ALA B 1 299 ? 17.250  -2.528  22.127  1.00 27.61  ? 299  ALA B O   1 
ATOM   4460 C  CB  . ALA B 1 299 ? 20.143  -2.924  20.592  1.00 29.95  ? 299  ALA B CB  1 
ATOM   4461 N  N   . ILE B 1 300 ? 18.055  -4.631  22.207  1.00 26.41  ? 300  ILE B N   1 
ATOM   4462 C  CA  . ILE B 1 300 ? 16.747  -5.246  22.398  1.00 31.47  ? 300  ILE B CA  1 
ATOM   4463 C  C   . ILE B 1 300 ? 16.111  -4.750  23.701  1.00 35.13  ? 300  ILE B C   1 
ATOM   4464 O  O   . ILE B 1 300 ? 14.972  -4.270  23.706  1.00 32.93  ? 300  ILE B O   1 
ATOM   4465 C  CB  . ILE B 1 300 ? 16.848  -6.792  22.422  1.00 33.26  ? 300  ILE B CB  1 
ATOM   4466 C  CG1 . ILE B 1 300 ? 17.161  -7.339  21.021  1.00 22.82  ? 300  ILE B CG1 1 
ATOM   4467 C  CG2 . ILE B 1 300 ? 15.555  -7.390  22.931  1.00 36.22  ? 300  ILE B CG2 1 
ATOM   4468 C  CD1 . ILE B 1 300 ? 17.637  -8.780  21.018  1.00 17.14  ? 300  ILE B CD1 1 
ATOM   4469 N  N   . ARG B 1 301 ? 16.865  -4.856  24.791  1.00 38.73  ? 301  ARG B N   1 
ATOM   4470 C  CA  . ARG B 1 301 ? 16.437  -4.377  26.105  1.00 37.66  ? 301  ARG B CA  1 
ATOM   4471 C  C   . ARG B 1 301 ? 15.974  -2.921  26.077  1.00 39.82  ? 301  ARG B C   1 
ATOM   4472 O  O   . ARG B 1 301 ? 14.931  -2.582  26.640  1.00 32.35  ? 301  ARG B O   1 
ATOM   4473 C  CB  . ARG B 1 301 ? 17.589  -4.504  27.110  1.00 40.46  ? 301  ARG B CB  1 
ATOM   4474 C  CG  . ARG B 1 301 ? 17.151  -4.741  28.571  1.00 52.07  ? 301  ARG B CG  1 
ATOM   4475 C  CD  . ARG B 1 301 ? 18.253  -4.385  29.584  1.00 44.14  ? 301  ARG B CD  1 
ATOM   4476 N  NE  . ARG B 1 301 ? 17.972  -3.081  30.193  1.00 61.75  ? 301  ARG B NE  1 
ATOM   4477 C  CZ  . ARG B 1 301 ? 18.683  -1.974  29.998  1.00 64.38  ? 301  ARG B CZ  1 
ATOM   4478 N  NH1 . ARG B 1 301 ? 19.755  -1.997  29.224  1.00 71.79  ? 301  ARG B NH1 1 
ATOM   4479 N  NH2 . ARG B 1 301 ? 18.323  -0.840  30.590  1.00 70.43  ? 301  ARG B NH2 1 
ATOM   4480 N  N   . ARG B 1 302 ? 16.757  -2.056  25.435  1.00 48.19  ? 302  ARG B N   1 
ATOM   4481 C  CA  . ARG B 1 302 ? 16.465  -0.622  25.445  1.00 50.92  ? 302  ARG B CA  1 
ATOM   4482 C  C   . ARG B 1 302 ? 15.257  -0.332  24.560  1.00 58.13  ? 302  ARG B C   1 
ATOM   4483 O  O   . ARG B 1 302 ? 14.392  0.469   24.910  1.00 64.15  ? 302  ARG B O   1 
ATOM   4484 C  CB  . ARG B 1 302 ? 17.667  0.199   24.954  1.00 53.77  ? 302  ARG B CB  1 
ATOM   4485 C  CG  . ARG B 1 302 ? 19.029  -0.203  25.508  1.00 58.56  ? 302  ARG B CG  1 
ATOM   4486 C  CD  . ARG B 1 302 ? 19.388  0.444   26.837  1.00 63.49  ? 302  ARG B CD  1 
ATOM   4487 N  NE  . ARG B 1 302 ? 20.840  0.591   26.948  1.00 68.72  ? 302  ARG B NE  1 
ATOM   4488 C  CZ  . ARG B 1 302 ? 21.474  1.761   27.000  1.00 67.91  ? 302  ARG B CZ  1 
ATOM   4489 N  NH1 . ARG B 1 302 ? 20.780  2.892   26.979  1.00 64.95  ? 302  ARG B NH1 1 
ATOM   4490 N  NH2 . ARG B 1 302 ? 22.799  1.805   27.086  1.00 57.51  ? 302  ARG B NH2 1 
ATOM   4491 N  N   . THR B 1 303 ? 15.212  -0.994  23.410  1.00 45.17  ? 303  THR B N   1 
ATOM   4492 C  CA  . THR B 1 303 ? 14.145  -0.794  22.447  1.00 41.12  ? 303  THR B CA  1 
ATOM   4493 C  C   . THR B 1 303 ? 12.829  -1.100  23.097  1.00 38.85  ? 303  THR B C   1 
ATOM   4494 O  O   . THR B 1 303 ? 11.916  -0.277  23.104  1.00 39.21  ? 303  THR B O   1 
ATOM   4495 C  CB  . THR B 1 303 ? 14.268  -1.772  21.285  1.00 47.15  ? 303  THR B CB  1 
ATOM   4496 O  OG1 . THR B 1 303 ? 15.452  -1.480  20.546  1.00 58.94  ? 303  THR B OG1 1 
ATOM   4497 C  CG2 . THR B 1 303 ? 13.065  -1.661  20.389  1.00 54.70  ? 303  THR B CG2 1 
ATOM   4498 N  N   . HIS B 1 304 ? 12.732  -2.314  23.628  1.00 38.89  ? 304  HIS B N   1 
ATOM   4499 C  CA  . HIS B 1 304 ? 11.536  -2.735  24.331  1.00 40.18  ? 304  HIS B CA  1 
ATOM   4500 C  C   . HIS B 1 304 ? 11.125  -1.729  25.407  1.00 49.03  ? 304  HIS B C   1 
ATOM   4501 O  O   . HIS B 1 304 ? 9.933   -1.481  25.610  1.00 51.24  ? 304  HIS B O   1 
ATOM   4502 C  CB  . HIS B 1 304 ? 11.738  -4.110  24.956  1.00 41.67  ? 304  HIS B CB  1 
ATOM   4503 C  CG  . HIS B 1 304 ? 10.566  -4.575  25.759  1.00 49.59  ? 304  HIS B CG  1 
ATOM   4504 N  ND1 . HIS B 1 304 ? 9.290   -4.640  25.241  1.00 58.00  ? 304  HIS B ND1 1 
ATOM   4505 C  CD2 . HIS B 1 304 ? 10.473  -4.976  27.049  1.00 39.87  ? 304  HIS B CD2 1 
ATOM   4506 C  CE1 . HIS B 1 304 ? 8.460   -5.066  26.179  1.00 57.56  ? 304  HIS B CE1 1 
ATOM   4507 N  NE2 . HIS B 1 304 ? 9.154   -5.280  27.284  1.00 46.53  ? 304  HIS B NE2 1 
ATOM   4508 N  N   . ASN B 1 305 ? 12.103  -1.133  26.083  1.00 43.14  ? 305  ASN B N   1 
ATOM   4509 C  CA  . ASN B 1 305 ? 11.801  -0.249  27.213  1.00 44.87  ? 305  ASN B CA  1 
ATOM   4510 C  C   . ASN B 1 305 ? 11.663  1.223   26.857  1.00 49.33  ? 305  ASN B C   1 
ATOM   4511 O  O   . ASN B 1 305 ? 11.568  2.078   27.739  1.00 42.60  ? 305  ASN B O   1 
ATOM   4512 C  CB  . ASN B 1 305 ? 12.840  -0.408  28.320  1.00 36.54  ? 305  ASN B CB  1 
ATOM   4513 C  CG  . ASN B 1 305 ? 12.647  -1.681  29.096  1.00 49.08  ? 305  ASN B CG  1 
ATOM   4514 O  OD1 . ASN B 1 305 ? 11.545  -2.231  29.127  1.00 59.38  ? 305  ASN B OD1 1 
ATOM   4515 N  ND2 . ASN B 1 305 ? 13.713  -2.176  29.706  1.00 45.10  ? 305  ASN B ND2 1 
ATOM   4516 N  N   . GLY B 1 306 ? 11.651  1.518   25.566  1.00 46.80  ? 306  GLY B N   1 
ATOM   4517 C  CA  . GLY B 1 306 ? 11.584  2.897   25.135  1.00 46.09  ? 306  GLY B CA  1 
ATOM   4518 C  C   . GLY B 1 306 ? 12.795  3.665   25.615  1.00 42.33  ? 306  GLY B C   1 
ATOM   4519 O  O   . GLY B 1 306 ? 12.765  4.890   25.735  1.00 47.98  ? 306  GLY B O   1 
ATOM   4520 N  N   . GLU B 1 307 ? 13.877  2.953   25.896  0.76 36.37  ? 307  GLU B N   1 
ATOM   4521 C  CA  . GLU B 1 307 ? 15.086  3.628   26.343  0.76 42.77  ? 307  GLU B CA  1 
ATOM   4522 C  C   . GLU B 1 307 ? 15.912  4.046   25.144  0.76 52.24  ? 307  GLU B C   1 
ATOM   4523 O  O   . GLU B 1 307 ? 15.577  3.734   24.007  0.76 51.44  ? 307  GLU B O   1 
ATOM   4524 C  CB  . GLU B 1 307 ? 15.904  2.747   27.290  0.76 43.23  ? 307  GLU B CB  1 
ATOM   4525 C  CG  . GLU B 1 307 ? 15.644  3.045   28.763  0.76 55.29  ? 307  GLU B CG  1 
ATOM   4526 C  CD  . GLU B 1 307 ? 15.146  1.836   29.542  0.76 66.01  ? 307  GLU B CD  1 
ATOM   4527 O  OE1 . GLU B 1 307 ? 14.214  2.006   30.367  0.76 57.37  ? 307  GLU B OE1 1 
ATOM   4528 O  OE2 . GLU B 1 307 ? 15.681  0.722   29.321  0.76 70.09  ? 307  GLU B OE2 1 
ATOM   4529 N  N   . SER B 1 308 ? 16.998  4.756   25.414  1.00 57.06  ? 308  SER B N   1 
ATOM   4530 C  CA  . SER B 1 308 ? 17.854  5.255   24.350  1.00 52.21  ? 308  SER B CA  1 
ATOM   4531 C  C   . SER B 1 308 ? 18.887  4.205   23.953  1.00 53.51  ? 308  SER B C   1 
ATOM   4532 O  O   . SER B 1 308 ? 19.427  3.493   24.794  1.00 53.28  ? 308  SER B O   1 
ATOM   4533 C  CB  . SER B 1 308 ? 18.527  6.562   24.773  1.00 56.32  ? 308  SER B CB  1 
ATOM   4534 O  OG  . SER B 1 308 ? 19.449  7.007   23.810  1.00 54.54  ? 308  SER B OG  1 
ATOM   4535 N  N   . VAL B 1 309 ? 19.153  4.134   22.656  1.00 55.71  ? 309  VAL B N   1 
ATOM   4536 C  CA  . VAL B 1 309 ? 20.064  3.172   22.077  1.00 55.21  ? 309  VAL B CA  1 
ATOM   4537 C  C   . VAL B 1 309 ? 21.298  3.922   21.579  1.00 58.97  ? 309  VAL B C   1 
ATOM   4538 O  O   . VAL B 1 309 ? 22.307  3.312   21.250  1.00 58.51  ? 309  VAL B O   1 
ATOM   4539 C  CB  . VAL B 1 309 ? 19.389  2.448   20.890  1.00 58.62  ? 309  VAL B CB  1 
ATOM   4540 C  CG1 . VAL B 1 309 ? 20.389  1.620   20.130  1.00 67.04  ? 309  VAL B CG1 1 
ATOM   4541 C  CG2 . VAL B 1 309 ? 18.238  1.578   21.367  1.00 59.97  ? 309  VAL B CG2 1 
ATOM   4542 N  N   . SER B 1 310 ? 21.209  5.249   21.519  1.00 60.85  ? 310  SER B N   1 
ATOM   4543 C  CA  . SER B 1 310 ? 22.286  6.071   20.964  1.00 61.49  ? 310  SER B CA  1 
ATOM   4544 C  C   . SER B 1 310 ? 23.580  5.818   21.708  1.00 52.01  ? 310  SER B C   1 
ATOM   4545 O  O   . SER B 1 310 ? 24.656  5.797   21.123  1.00 47.39  ? 310  SER B O   1 
ATOM   4546 C  CB  . SER B 1 310 ? 21.941  7.557   21.053  1.00 60.75  ? 310  SER B CB  1 
ATOM   4547 O  OG  . SER B 1 310 ? 21.181  7.961   19.933  1.00 66.70  ? 310  SER B OG  1 
ATOM   4548 N  N   . TYR B 1 311 ? 23.439  5.672   23.018  0.94 48.67  ? 311  TYR B N   1 
ATOM   4549 C  CA  . TYR B 1 311 ? 24.496  5.232   23.912  0.94 53.79  ? 311  TYR B CA  1 
ATOM   4550 C  C   . TYR B 1 311 ? 25.455  4.248   23.229  0.94 45.94  ? 311  TYR B C   1 
ATOM   4551 O  O   . TYR B 1 311 ? 26.663  4.429   23.265  0.94 38.51  ? 311  TYR B O   1 
ATOM   4552 C  CB  . TYR B 1 311 ? 23.838  4.572   25.128  0.94 63.62  ? 311  TYR B CB  1 
ATOM   4553 C  CG  . TYR B 1 311 ? 24.766  4.196   26.245  0.94 76.40  ? 311  TYR B CG  1 
ATOM   4554 C  CD1 . TYR B 1 311 ? 24.750  4.897   27.449  0.94 89.68  ? 311  TYR B CD1 1 
ATOM   4555 C  CD2 . TYR B 1 311 ? 25.643  3.131   26.117  0.94 82.14  ? 311  TYR B CD2 1 
ATOM   4556 C  CE1 . TYR B 1 311 ? 25.594  4.554   28.488  0.94 91.66  ? 311  TYR B CE1 1 
ATOM   4557 C  CE2 . TYR B 1 311 ? 26.493  2.782   27.148  0.94 91.98  ? 311  TYR B CE2 1 
ATOM   4558 C  CZ  . TYR B 1 311 ? 26.468  3.496   28.330  0.94 93.85  ? 311  TYR B CZ  1 
ATOM   4559 O  OH  . TYR B 1 311 ? 27.319  3.139   29.351  0.94 94.25  ? 311  TYR B OH  1 
ATOM   4560 N  N   . LEU B 1 312 ? 24.906  3.219   22.591  1.00 41.42  ? 312  LEU B N   1 
ATOM   4561 C  CA  . LEU B 1 312 ? 25.708  2.103   22.092  1.00 43.68  ? 312  LEU B CA  1 
ATOM   4562 C  C   . LEU B 1 312 ? 26.581  2.448   20.887  1.00 45.61  ? 312  LEU B C   1 
ATOM   4563 O  O   . LEU B 1 312 ? 27.460  1.671   20.511  1.00 41.23  ? 312  LEU B O   1 
ATOM   4564 C  CB  . LEU B 1 312 ? 24.807  0.916   21.759  1.00 40.36  ? 312  LEU B CB  1 
ATOM   4565 C  CG  . LEU B 1 312 ? 24.022  0.383   22.952  1.00 39.51  ? 312  LEU B CG  1 
ATOM   4566 C  CD1 . LEU B 1 312 ? 22.939  -0.589  22.506  1.00 29.42  ? 312  LEU B CD1 1 
ATOM   4567 C  CD2 . LEU B 1 312 ? 25.006  -0.273  23.903  1.00 30.22  ? 312  LEU B CD2 1 
ATOM   4568 N  N   . PHE B 1 313 ? 26.355  3.608   20.286  1.00 51.05  ? 313  PHE B N   1 
ATOM   4569 C  CA  . PHE B 1 313 ? 27.108  3.969   19.086  1.00 58.11  ? 313  PHE B CA  1 
ATOM   4570 C  C   . PHE B 1 313 ? 28.529  4.419   19.411  1.00 62.98  ? 313  PHE B C   1 
ATOM   4571 O  O   . PHE B 1 313 ? 29.441  4.260   18.598  1.00 71.31  ? 313  PHE B O   1 
ATOM   4572 C  CB  . PHE B 1 313 ? 26.364  5.023   18.258  1.00 56.75  ? 313  PHE B CB  1 
ATOM   4573 C  CG  . PHE B 1 313 ? 25.069  4.531   17.678  1.00 58.13  ? 313  PHE B CG  1 
ATOM   4574 C  CD1 . PHE B 1 313 ? 24.684  3.207   17.833  1.00 66.13  ? 313  PHE B CD1 1 
ATOM   4575 C  CD2 . PHE B 1 313 ? 24.240  5.387   16.979  1.00 60.43  ? 313  PHE B CD2 1 
ATOM   4576 C  CE1 . PHE B 1 313 ? 23.489  2.750   17.305  1.00 71.12  ? 313  PHE B CE1 1 
ATOM   4577 C  CE2 . PHE B 1 313 ? 23.047  4.935   16.441  1.00 64.16  ? 313  PHE B CE2 1 
ATOM   4578 C  CZ  . PHE B 1 313 ? 22.669  3.614   16.606  1.00 67.28  ? 313  PHE B CZ  1 
ATOM   4579 N  N   . SER B 1 314 ? 28.718  4.959   20.609  1.00 61.94  ? 314  SER B N   1 
ATOM   4580 C  CA  . SER B 1 314 ? 30.032  5.437   21.024  1.00 71.01  ? 314  SER B CA  1 
ATOM   4581 C  C   . SER B 1 314 ? 30.570  4.666   22.222  1.00 68.96  ? 314  SER B C   1 
ATOM   4582 O  O   . SER B 1 314 ? 31.677  4.933   22.694  1.00 71.41  ? 314  SER B O   1 
ATOM   4583 C  CB  . SER B 1 314 ? 29.976  6.929   21.359  1.00 81.08  ? 314  SER B CB  1 
ATOM   4584 O  OG  . SER B 1 314 ? 29.087  7.181   22.435  1.00 82.78  ? 314  SER B OG  1 
ATOM   4585 N  N   . HIS B 1 315 ? 29.790  3.707   22.710  1.00 64.66  ? 315  HIS B N   1 
ATOM   4586 C  CA  . HIS B 1 315 ? 30.155  3.004   23.929  1.00 64.71  ? 315  HIS B CA  1 
ATOM   4587 C  C   . HIS B 1 315 ? 29.758  1.538   23.926  1.00 70.17  ? 315  HIS B C   1 
ATOM   4588 O  O   . HIS B 1 315 ? 28.729  1.150   23.370  1.00 73.79  ? 315  HIS B O   1 
ATOM   4589 C  CB  . HIS B 1 315 ? 29.543  3.703   25.141  1.00 70.92  ? 315  HIS B CB  1 
ATOM   4590 C  CG  . HIS B 1 315 ? 29.875  5.160   25.223  1.00 84.67  ? 315  HIS B CG  1 
ATOM   4591 N  ND1 . HIS B 1 315 ? 28.952  6.149   24.960  1.00 86.16  ? 315  HIS B ND1 1 
ATOM   4592 C  CD2 . HIS B 1 315 ? 31.034  5.794   25.524  1.00 90.20  ? 315  HIS B CD2 1 
ATOM   4593 C  CE1 . HIS B 1 315 ? 29.527  7.331   25.104  1.00 91.02  ? 315  HIS B CE1 1 
ATOM   4594 N  NE2 . HIS B 1 315 ? 30.790  7.143   25.442  1.00 91.40  ? 315  HIS B NE2 1 
ATOM   4595 N  N   . VAL B 1 316 ? 30.592  0.735   24.576  1.00 69.97  ? 316  VAL B N   1 
ATOM   4596 C  CA  . VAL B 1 316 ? 30.391  -0.698  24.694  1.00 62.59  ? 316  VAL B CA  1 
ATOM   4597 C  C   . VAL B 1 316 ? 29.733  -0.997  26.032  1.00 69.51  ? 316  VAL B C   1 
ATOM   4598 O  O   . VAL B 1 316 ? 30.236  -0.579  27.074  1.00 68.49  ? 316  VAL B O   1 
ATOM   4599 C  CB  . VAL B 1 316 ? 31.750  -1.424  24.641  1.00 58.25  ? 316  VAL B CB  1 
ATOM   4600 C  CG1 . VAL B 1 316 ? 31.779  -2.422  23.498  1.00 66.87  ? 316  VAL B CG1 1 
ATOM   4601 C  CG2 . VAL B 1 316 ? 32.872  -0.416  24.470  1.00 51.54  ? 316  VAL B CG2 1 
ATOM   4602 N  N   . PRO B 1 317 ? 28.614  -1.739  26.017  1.00 72.33  ? 317  PRO B N   1 
ATOM   4603 C  CA  . PRO B 1 317 ? 27.943  -2.077  27.278  1.00 77.73  ? 317  PRO B CA  1 
ATOM   4604 C  C   . PRO B 1 317 ? 28.788  -3.041  28.111  1.00 81.80  ? 317  PRO B C   1 
ATOM   4605 O  O   . PRO B 1 317 ? 29.352  -2.620  29.125  1.00 79.25  ? 317  PRO B O   1 
ATOM   4606 C  CB  . PRO B 1 317 ? 26.663  -2.767  26.814  1.00 71.93  ? 317  PRO B CB  1 
ATOM   4607 C  CG  . PRO B 1 317 ? 27.042  -3.390  25.514  1.00 67.48  ? 317  PRO B CG  1 
ATOM   4608 C  CD  . PRO B 1 317 ? 28.013  -2.435  24.868  1.00 64.87  ? 317  PRO B CD  1 
HETATM 4609 S  S   . SO4 C 2 .   ? 30.381  22.780  0.486   1.00 86.18  ? 401  SO4 A S   1 
HETATM 4610 O  O1  . SO4 C 2 .   ? 31.325  23.266  1.491   1.00 83.84  ? 401  SO4 A O1  1 
HETATM 4611 O  O2  . SO4 C 2 .   ? 29.017  23.088  0.915   1.00 87.57  ? 401  SO4 A O2  1 
HETATM 4612 O  O3  . SO4 C 2 .   ? 30.661  23.447  -0.780  1.00 84.84  ? 401  SO4 A O3  1 
HETATM 4613 O  O4  . SO4 C 2 .   ? 30.518  21.335  0.301   1.00 83.92  ? 401  SO4 A O4  1 
HETATM 4614 S  S   . SO4 D 2 .   ? 18.850  -0.271  -20.916 1.00 38.34  ? 402  SO4 A S   1 
HETATM 4615 O  O1  . SO4 D 2 .   ? 17.555  -0.304  -21.577 1.00 40.60  ? 402  SO4 A O1  1 
HETATM 4616 O  O2  . SO4 D 2 .   ? 18.880  -1.234  -19.831 1.00 41.10  ? 402  SO4 A O2  1 
HETATM 4617 O  O3  . SO4 D 2 .   ? 19.885  -0.653  -21.867 1.00 41.91  ? 402  SO4 A O3  1 
HETATM 4618 O  O4  . SO4 D 2 .   ? 19.086  1.063   -20.422 1.00 32.87  ? 402  SO4 A O4  1 
HETATM 4619 S  S   . SO4 E 2 .   ? 24.416  3.164   -10.140 1.00 86.03  ? 403  SO4 A S   1 
HETATM 4620 O  O1  . SO4 E 2 .   ? 24.431  2.574   -11.478 1.00 92.33  ? 403  SO4 A O1  1 
HETATM 4621 O  O2  . SO4 E 2 .   ? 23.720  4.449   -10.180 1.00 63.17  ? 403  SO4 A O2  1 
HETATM 4622 O  O3  . SO4 E 2 .   ? 23.734  2.251   -9.234  1.00 91.14  ? 403  SO4 A O3  1 
HETATM 4623 O  O4  . SO4 E 2 .   ? 25.781  3.361   -9.654  1.00 95.81  ? 403  SO4 A O4  1 
HETATM 4624 MG MG  . MG  F 3 .   ? 7.200   7.015   -21.733 1.00 54.01  ? 404  MG  A MG  1 
HETATM 4625 S  S   . SO4 G 2 .   ? 36.841  -10.429 -0.190  1.00 77.76  ? 1001 SO4 B S   1 
HETATM 4626 O  O1  . SO4 G 2 .   ? 38.072  -10.761 -0.907  1.00 79.54  ? 1001 SO4 B O1  1 
HETATM 4627 O  O2  . SO4 G 2 .   ? 36.956  -10.830 1.213   1.00 72.61  ? 1001 SO4 B O2  1 
HETATM 4628 O  O3  . SO4 G 2 .   ? 36.623  -8.988  -0.235  1.00 87.30  ? 1001 SO4 B O3  1 
HETATM 4629 O  O4  . SO4 G 2 .   ? 35.712  -11.108 -0.828  1.00 69.40  ? 1001 SO4 B O4  1 
HETATM 4630 S  S   . SO4 H 2 .   ? 17.527  6.690   20.542  1.00 34.35  ? 1002 SO4 B S   1 
HETATM 4631 O  O1  . SO4 H 2 .   ? 18.274  5.544   20.058  1.00 37.08  ? 1002 SO4 B O1  1 
HETATM 4632 O  O2  . SO4 H 2 .   ? 16.356  6.259   21.276  1.00 35.73  ? 1002 SO4 B O2  1 
HETATM 4633 O  O3  . SO4 H 2 .   ? 18.394  7.459   21.422  1.00 35.13  ? 1002 SO4 B O3  1 
HETATM 4634 O  O4  . SO4 H 2 .   ? 17.131  7.515   19.401  1.00 33.99  ? 1002 SO4 B O4  1 
HETATM 4635 S  S   . SO4 I 2 .   ? 23.854  5.251   9.937   1.00 60.09  ? 1003 SO4 B S   1 
HETATM 4636 O  O1  . SO4 I 2 .   ? 24.669  4.051   9.953   1.00 49.31  ? 1003 SO4 B O1  1 
HETATM 4637 O  O2  . SO4 I 2 .   ? 22.602  4.912   9.284   1.00 68.91  ? 1003 SO4 B O2  1 
HETATM 4638 O  O3  . SO4 I 2 .   ? 23.587  5.738   11.297  1.00 68.64  ? 1003 SO4 B O3  1 
HETATM 4639 O  O4  . SO4 I 2 .   ? 24.557  6.272   9.158   1.00 60.75  ? 1003 SO4 B O4  1 
HETATM 4640 MG MG  . MG  J 3 .   ? 9.061   -3.909  21.054  1.00 45.07  ? 1004 MG  B MG  1 
HETATM 4641 O  O   . HOH K 4 .   ? 21.660  2.318   -8.168  1.00 41.94  ? 501  HOH A O   1 
HETATM 4642 O  O   . HOH K 4 .   ? 6.488   9.385   -19.119 1.00 38.47  ? 502  HOH A O   1 
HETATM 4643 O  O   . HOH K 4 .   ? 6.089   23.763  -19.901 1.00 36.23  ? 503  HOH A O   1 
HETATM 4644 O  O   . HOH K 4 .   ? 8.514   8.625   3.752   1.00 29.97  ? 504  HOH A O   1 
HETATM 4645 O  O   . HOH K 4 .   ? 15.527  3.870   10.366  1.00 34.40  ? 505  HOH A O   1 
HETATM 4646 O  O   . HOH K 4 .   ? 4.047   6.176   -8.370  1.00 32.32  ? 506  HOH A O   1 
HETATM 4647 O  O   . HOH K 4 .   ? 15.720  9.810   13.077  1.00 34.98  ? 507  HOH A O   1 
HETATM 4648 O  O   . HOH K 4 .   ? 21.543  17.417  -1.124  1.00 41.96  ? 508  HOH A O   1 
HETATM 4649 O  O   . HOH K 4 .   ? 21.093  14.224  -8.878  1.00 31.85  ? 509  HOH A O   1 
HETATM 4650 O  O   . HOH K 4 .   ? 25.677  8.531   -8.826  1.00 43.12  ? 510  HOH A O   1 
HETATM 4651 O  O   . HOH K 4 .   ? -5.705  15.865  -19.627 1.00 23.09  ? 511  HOH A O   1 
HETATM 4652 O  O   . HOH K 4 .   ? 8.999   25.371  -26.268 1.00 39.03  ? 512  HOH A O   1 
HETATM 4653 O  O   . HOH K 4 .   ? 5.635   18.765  -25.422 1.00 27.05  ? 513  HOH A O   1 
HETATM 4654 O  O   . HOH K 4 .   ? 18.479  4.424   14.615  1.00 41.75  ? 514  HOH A O   1 
HETATM 4655 O  O   . HOH K 4 .   ? 14.540  1.758   -8.477  1.00 36.46  ? 515  HOH A O   1 
HETATM 4656 O  O   . HOH K 4 .   ? 32.728  22.033  -1.404  1.00 57.46  ? 516  HOH A O   1 
HETATM 4657 O  O   . HOH K 4 .   ? -9.246  12.721  -16.065 1.00 42.69  ? 517  HOH A O   1 
HETATM 4658 O  O   . HOH K 4 .   ? 47.390  7.175   -7.326  1.00 46.37  ? 518  HOH A O   1 
HETATM 4659 O  O   . HOH K 4 .   ? 28.500  12.248  -19.924 1.00 43.26  ? 519  HOH A O   1 
HETATM 4660 O  O   . HOH K 4 .   ? 6.613   2.417   -13.094 1.00 39.59  ? 520  HOH A O   1 
HETATM 4661 O  O   . HOH K 4 .   ? 14.551  -0.159  -6.458  1.00 34.96  ? 521  HOH A O   1 
HETATM 4662 O  O   . HOH K 4 .   ? 10.024  21.986  -10.368 1.00 40.01  ? 522  HOH A O   1 
HETATM 4663 O  O   . HOH K 4 .   ? 9.923   5.371   -2.554  1.00 25.61  ? 523  HOH A O   1 
HETATM 4664 O  O   . HOH K 4 .   ? 8.429   3.988   -5.912  1.00 34.15  ? 524  HOH A O   1 
HETATM 4665 O  O   . HOH K 4 .   ? 17.232  7.460   14.362  1.00 36.65  ? 525  HOH A O   1 
HETATM 4666 O  O   . HOH K 4 .   ? 49.060  16.448  4.504   1.00 49.59  ? 526  HOH A O   1 
HETATM 4667 O  O   . HOH K 4 .   ? 6.843   11.451  -29.605 1.00 51.39  ? 527  HOH A O   1 
HETATM 4668 O  O   . HOH K 4 .   ? 8.339   16.961  -34.246 1.00 39.23  ? 528  HOH A O   1 
HETATM 4669 O  O   . HOH K 4 .   ? 18.325  -0.240  -17.239 1.00 41.80  ? 529  HOH A O   1 
HETATM 4670 O  O   . HOH L 4 .   ? 31.007  -12.334 12.209  1.00 27.55  ? 1101 HOH B O   1 
HETATM 4671 O  O   . HOH L 4 .   ? 5.987   -4.388  7.682   1.00 30.15  ? 1102 HOH B O   1 
HETATM 4672 O  O   . HOH L 4 .   ? 20.955  5.205   7.716   1.00 32.29  ? 1103 HOH B O   1 
HETATM 4673 O  O   . HOH L 4 .   ? 10.899  -1.768  2.024   1.00 27.85  ? 1104 HOH B O   1 
HETATM 4674 O  O   . HOH L 4 .   ? 26.118  -9.292  0.621   1.00 34.83  ? 1105 HOH B O   1 
HETATM 4675 O  O   . HOH L 4 .   ? 27.085  0.881   8.563   1.00 36.84  ? 1106 HOH B O   1 
HETATM 4676 O  O   . HOH L 4 .   ? 13.514  -20.004 19.504  1.00 30.06  ? 1107 HOH B O   1 
HETATM 4677 O  O   . HOH L 4 .   ? 9.243   -6.561  18.850  1.00 43.77  ? 1108 HOH B O   1 
HETATM 4678 O  O   . HOH L 4 .   ? -4.157  -14.776 15.560  1.00 34.45  ? 1109 HOH B O   1 
HETATM 4679 O  O   . HOH L 4 .   ? 24.459  -5.690  8.644   1.00 26.97  ? 1110 HOH B O   1 
HETATM 4680 O  O   . HOH L 4 .   ? 14.136  3.270   8.015   1.00 28.31  ? 1111 HOH B O   1 
HETATM 4681 O  O   . HOH L 4 .   ? 23.097  -4.831  -6.951  1.00 53.75  ? 1112 HOH B O   1 
HETATM 4682 O  O   . HOH L 4 .   ? 32.616  -17.654 9.441   1.00 42.93  ? 1113 HOH B O   1 
HETATM 4683 O  O   . HOH L 4 .   ? 9.284   -0.920  5.298   1.00 40.72  ? 1114 HOH B O   1 
HETATM 4684 O  O   . HOH L 4 .   ? 28.293  -5.024  6.239   1.00 44.54  ? 1115 HOH B O   1 
HETATM 4685 O  O   . HOH L 4 .   ? 13.644  4.841   5.977   1.00 28.65  ? 1116 HOH B O   1 
HETATM 4686 O  O   . HOH L 4 .   ? 11.875  -15.539 25.059  1.00 31.66  ? 1117 HOH B O   1 
HETATM 4687 O  O   . HOH L 4 .   ? 22.647  -15.389 14.071  1.00 52.44  ? 1118 HOH B O   1 
HETATM 4688 O  O   . HOH L 4 .   ? -0.209  -9.396  14.350  1.00 39.62  ? 1119 HOH B O   1 
HETATM 4689 O  O   . HOH L 4 .   ? 11.020  -5.346  -4.401  1.00 30.86  ? 1120 HOH B O   1 
HETATM 4690 O  O   . HOH L 4 .   ? 17.264  6.708   16.784  1.00 33.91  ? 1121 HOH B O   1 
HETATM 4691 O  O   . HOH L 4 .   ? 10.236  1.051   1.582   1.00 42.56  ? 1122 HOH B O   1 
HETATM 4692 O  O   . HOH L 4 .   ? 23.301  -12.813 6.274   1.00 40.48  ? 1123 HOH B O   1 
HETATM 4693 O  O   . HOH L 4 .   ? 50.448  8.975   15.406  1.00 48.80  ? 1124 HOH B O   1 
HETATM 4694 O  O   . HOH L 4 .   ? 20.532  3.578   13.367  1.00 41.49  ? 1125 HOH B O   1 
HETATM 4695 O  O   . HOH L 4 .   ? 16.963  -20.800 25.825  1.00 38.63  ? 1126 HOH B O   1 
HETATM 4696 O  O   . HOH L 4 .   ? 19.649  -17.529 15.296  1.00 56.12  ? 1127 HOH B O   1 
HETATM 4697 O  O   . HOH L 4 .   ? 35.904  -5.181  22.530  1.00 36.90  ? 1128 HOH B O   1 
HETATM 4698 O  O   . HOH L 4 .   ? 27.721  -16.298 16.291  1.00 41.25  ? 1129 HOH B O   1 
HETATM 4699 O  O   . HOH L 4 .   ? 16.682  -17.705 10.196  1.00 32.77  ? 1130 HOH B O   1 
HETATM 4700 O  O   . HOH L 4 .   ? 26.799  -0.156  18.792  1.00 41.67  ? 1131 HOH B O   1 
HETATM 4701 O  O   . HOH L 4 .   ? 13.403  -13.156 33.662  1.00 42.98  ? 1132 HOH B O   1 
HETATM 4702 O  O   . HOH L 4 .   ? 35.577  10.037  14.552  1.00 44.79  ? 1133 HOH B O   1 
HETATM 4703 O  O   . HOH L 4 .   ? 6.940   -0.219  12.588  1.00 36.34  ? 1134 HOH B O   1 
HETATM 4704 O  O   . HOH L 4 .   ? 34.845  -6.313  26.806  1.00 45.48  ? 1135 HOH B O   1 
HETATM 4705 O  O   . HOH L 4 .   ? 51.887  -9.099  10.259  1.00 42.09  ? 1136 HOH B O   1 
HETATM 4706 O  O   . HOH L 4 .   ? 25.768  -5.772  5.957   1.00 41.38  ? 1137 HOH B O   1 
HETATM 4707 O  O   . HOH L 4 .   ? 41.314  -19.036 15.986  1.00 50.85  ? 1138 HOH B O   1 
HETATM 4708 O  O   . HOH L 4 .   ? 16.012  1.631   -10.794 1.00 48.73  ? 1139 HOH B O   1 
HETATM 4709 O  O   . HOH L 4 .   ? 38.380  -14.370 -4.994  1.00 52.49  ? 1140 HOH B O   1 
HETATM 4710 O  O   . HOH L 4 .   ? 34.593  -3.141  11.413  1.00 46.88  ? 1141 HOH B O   1 
HETATM 4711 O  O   . HOH L 4 .   ? 35.176  2.203   22.754  1.00 34.55  ? 1142 HOH B O   1 
HETATM 4712 O  O   . HOH L 4 .   ? 29.721  1.174   1.605   1.00 45.99  ? 1143 HOH B O   1 
HETATM 4713 O  O   . HOH L 4 .   ? 22.387  -12.230 10.350  1.00 56.94  ? 1144 HOH B O   1 
# 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   2   PRO PRO 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  HIS 52  52  52  HIS HIS A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  MET 68  68  68  MET MET A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  CYS 91  91  91  CYS CYS A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 MET 115 115 115 MET MET A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 HIS 123 123 123 HIS HIS A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 MET 127 127 127 MET MET A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 TRP 162 162 162 TRP TRP A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 CYS 165 165 165 CYS CYS A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 LYS 197 197 ?   ?   ?   A . n 
A 1 198 LYS 198 198 ?   ?   ?   A . n 
A 1 199 ALA 199 199 ?   ?   ?   A . n 
A 1 200 ASN 200 200 ?   ?   ?   A . n 
A 1 201 GLU 201 201 ?   ?   ?   A . n 
A 1 202 VAL 202 202 ?   ?   ?   A . n 
A 1 203 ASP 203 203 ?   ?   ?   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 314 314 314 SER SER A . n 
A 1 315 HIS 315 315 315 HIS HIS A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 PRO 317 317 ?   ?   ?   A . n 
A 1 318 LEU 318 318 ?   ?   ?   A . n 
A 1 319 LEU 319 319 ?   ?   ?   A . n 
A 1 320 GLU 320 320 ?   ?   ?   A . n 
A 1 321 HIS 321 321 ?   ?   ?   A . n 
A 1 322 HIS 322 322 ?   ?   ?   A . n 
A 1 323 HIS 323 323 ?   ?   ?   A . n 
A 1 324 HIS 324 324 ?   ?   ?   A . n 
A 1 325 HIS 325 325 ?   ?   ?   A . n 
A 1 326 HIS 326 326 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   ASN 3   3   3   ASN ASN B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  SER 11  11  11  SER SER B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  GLN 13  13  13  GLN GLN B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  GLN 17  17  17  GLN GLN B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  LYS 33  33  33  LYS LYS B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  PHE 35  35  35  PHE PHE B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  CYS 41  41  41  CYS CYS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  HIS 52  52  52  HIS HIS B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  CYS 60  60  60  CYS CYS B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  MET 68  68  68  MET MET B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ILE 72  72  72  ILE ILE B . n 
B 1 73  MET 73  73  73  MET MET B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  CYS 77  77  77  CYS CYS B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  PRO 90  90  90  PRO PRO B . n 
B 1 91  CYS 91  91  91  CYS CYS B . n 
B 1 92  PHE 92  92  92  PHE PHE B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  GLN 97  97  97  GLN GLN B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ASN 114 114 114 ASN ASN B . n 
B 1 115 MET 115 115 115 MET MET B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 HIS 123 123 123 HIS HIS B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 THR 126 126 126 THR THR B . n 
B 1 127 MET 127 127 127 MET MET B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 HIS 130 130 130 HIS HIS B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 SER 132 132 132 SER SER B . n 
B 1 133 GLN 133 133 133 GLN GLN B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 PHE 137 137 137 PHE PHE B . n 
B 1 138 PHE 138 138 138 PHE PHE B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 ILE 140 140 140 ILE ILE B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 TYR 146 146 146 TYR TYR B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 TRP 154 154 154 TRP TRP B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 GLU 157 157 157 GLU GLU B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 ILE 159 159 159 ILE ILE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 TRP 162 162 162 TRP TRP B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 ASN 164 164 164 ASN ASN B . n 
B 1 165 CYS 165 165 165 CYS CYS B . n 
B 1 166 THR 166 166 166 THR THR B . n 
B 1 167 ILE 167 167 167 ILE ILE B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 ASP 171 171 171 ASP ASP B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 LYS 176 176 176 LYS LYS B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 SER 180 180 180 SER SER B . n 
B 1 181 ILE 181 181 181 ILE ILE B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 ASP 183 183 183 ASP ASP B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 PHE 189 189 189 PHE PHE B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 HIS 193 193 193 HIS HIS B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 ARG 196 196 ?   ?   ?   B . n 
B 1 197 LYS 197 197 ?   ?   ?   B . n 
B 1 198 LYS 198 198 ?   ?   ?   B . n 
B 1 199 ALA 199 199 ?   ?   ?   B . n 
B 1 200 ASN 200 200 ?   ?   ?   B . n 
B 1 201 GLU 201 201 ?   ?   ?   B . n 
B 1 202 VAL 202 202 ?   ?   ?   B . n 
B 1 203 ASP 203 203 203 ASP ASP B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 MET 205 205 205 MET MET B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 VAL 208 208 208 VAL VAL B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 ASP 210 210 210 ASP ASP B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 ASP 213 213 213 ASP ASP B . n 
B 1 214 ARG 214 214 214 ARG ARG B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 ALA 216 216 216 ALA ALA B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 VAL 219 219 219 VAL VAL B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 MET 222 222 222 MET MET B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 ASP 224 224 224 ASP ASP B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 CYS 226 226 226 CYS CYS B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 THR 228 228 228 THR THR B . n 
B 1 229 ILE 229 229 229 ILE ILE B . n 
B 1 230 CYS 230 230 230 CYS CYS B . n 
B 1 231 HIS 231 231 231 HIS HIS B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 ASP 234 234 234 ASP ASP B . n 
B 1 235 LYS 235 235 235 LYS LYS B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 ALA 239 239 239 ALA ALA B . n 
B 1 240 GLY 240 240 240 GLY GLY B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 ARG 243 243 243 ARG ARG B . n 
B 1 244 VAL 244 244 244 VAL VAL B . n 
B 1 245 TYR 245 245 245 TYR TYR B . n 
B 1 246 ALA 246 246 246 ALA ALA B . n 
B 1 247 ILE 247 247 247 ILE ILE B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 THR 249 249 249 THR THR B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 ILE 252 252 252 ILE ILE B . n 
B 1 253 PHE 253 253 253 PHE PHE B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 PRO 256 256 256 PRO PRO B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 SER 259 259 259 SER SER B . n 
B 1 260 ARG 260 260 260 ARG ARG B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 ASN 262 262 262 ASN ASN B . n 
B 1 263 ASN 263 263 263 ASN ASN B . n 
B 1 264 ALA 264 264 264 ALA ALA B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 PHE 266 266 266 PHE PHE B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 ALA 268 268 268 ALA ALA B . n 
B 1 269 VAL 269 269 269 VAL VAL B . n 
B 1 270 VAL 270 270 270 VAL VAL B . n 
B 1 271 VAL 271 271 271 VAL VAL B . n 
B 1 272 THR 272 272 272 THR THR B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 THR 274 274 274 THR THR B . n 
B 1 275 ILE 275 275 275 ILE ILE B . n 
B 1 276 PRO 276 276 276 PRO PRO B . n 
B 1 277 GLN 277 277 277 GLN GLN B . n 
B 1 278 GLU 278 278 278 GLU GLU B . n 
B 1 279 ASP 279 279 279 ASP ASP B . n 
B 1 280 LYS 280 280 280 LYS LYS B . n 
B 1 281 MET 281 281 281 MET MET B . n 
B 1 282 LYS 282 282 282 LYS LYS B . n 
B 1 283 HIS 283 283 283 HIS HIS B . n 
B 1 284 CYS 284 284 284 CYS CYS B . n 
B 1 285 SER 285 285 285 SER SER B . n 
B 1 286 LYS 286 286 286 LYS LYS B . n 
B 1 287 ILE 287 287 287 ILE ILE B . n 
B 1 288 GLN 288 288 288 GLN GLN B . n 
B 1 289 VAL 289 289 289 VAL VAL B . n 
B 1 290 ILE 290 290 290 ILE ILE B . n 
B 1 291 ASP 291 291 291 ASP ASP B . n 
B 1 292 ILE 292 292 292 ILE ILE B . n 
B 1 293 SER 293 293 293 SER SER B . n 
B 1 294 MET 294 294 294 MET MET B . n 
B 1 295 ILE 295 295 295 ILE ILE B . n 
B 1 296 LEU 296 296 296 LEU LEU B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 GLU 298 298 298 GLU GLU B . n 
B 1 299 ALA 299 299 299 ALA ALA B . n 
B 1 300 ILE 300 300 300 ILE ILE B . n 
B 1 301 ARG 301 301 301 ARG ARG B . n 
B 1 302 ARG 302 302 302 ARG ARG B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 HIS 304 304 304 HIS HIS B . n 
B 1 305 ASN 305 305 305 ASN ASN B . n 
B 1 306 GLY 306 306 306 GLY GLY B . n 
B 1 307 GLU 307 307 307 GLU GLU B . n 
B 1 308 SER 308 308 308 SER SER B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 SER 310 310 310 SER SER B . n 
B 1 311 TYR 311 311 311 TYR TYR B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 PHE 313 313 313 PHE PHE B . n 
B 1 314 SER 314 314 314 SER SER B . n 
B 1 315 HIS 315 315 315 HIS HIS B . n 
B 1 316 VAL 316 316 316 VAL VAL B . n 
B 1 317 PRO 317 317 317 PRO PRO B . n 
B 1 318 LEU 318 318 ?   ?   ?   B . n 
B 1 319 LEU 319 319 ?   ?   ?   B . n 
B 1 320 GLU 320 320 ?   ?   ?   B . n 
B 1 321 HIS 321 321 ?   ?   ?   B . n 
B 1 322 HIS 322 322 ?   ?   ?   B . n 
B 1 323 HIS 323 323 ?   ?   ?   B . n 
B 1 324 HIS 324 324 ?   ?   ?   B . n 
B 1 325 HIS 325 325 ?   ?   ?   B . n 
B 1 326 HIS 326 326 ?   ?   ?   B . n 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
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)' 28330 ? 
1 MORE         -495  ? 
1 'SSA (A^2)'  58730 ? 
# 
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 2013-05-22 
2 'Structure model' 1 1 2014-03-12 
# 
_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' 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         25.539 
_pdbx_refine_tls.origin_y         4.327 
_pdbx_refine_tls.origin_z         0.184 
_pdbx_refine_tls.T[1][1]          0.1386 
_pdbx_refine_tls.T[2][2]          0.1155 
_pdbx_refine_tls.T[3][3]          0.0453 
_pdbx_refine_tls.T[1][2]          -0.0016 
_pdbx_refine_tls.T[1][3]          0.0050 
_pdbx_refine_tls.T[2][3]          0.0031 
_pdbx_refine_tls.L[1][1]          0.3440 
_pdbx_refine_tls.L[2][2]          0.2537 
_pdbx_refine_tls.L[3][3]          0.0275 
_pdbx_refine_tls.L[1][2]          -0.1699 
_pdbx_refine_tls.L[1][3]          -0.0068 
_pdbx_refine_tls.L[2][3]          -0.0641 
_pdbx_refine_tls.S[1][1]          0.0174 
_pdbx_refine_tls.S[2][2]          -0.0244 
_pdbx_refine_tls.S[3][3]          0.0070 
_pdbx_refine_tls.S[1][2]          -0.0057 
_pdbx_refine_tls.S[1][3]          0.0624 
_pdbx_refine_tls.S[2][3]          -0.0374 
_pdbx_refine_tls.S[2][1]          -0.0211 
_pdbx_refine_tls.S[3][1]          0.0058 
_pdbx_refine_tls.S[3][2]          0.0085 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 2    A 316  ? . . . . ? 
'X-RAY DIFFRACTION' 2 1 B 3    B 317  ? . . . . ? 
'X-RAY DIFFRACTION' 3 1 A 401  A 404  ? . . . . ? 
'X-RAY DIFFRACTION' 4 1 B 1001 B 1004 ? . . . . ? 
'X-RAY DIFFRACTION' 5 1 A 501  A 529  ? . . . . ? 
'X-RAY DIFFRACTION' 6 1 B 1101 B 1144 ? . . . . ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .   ? 1 
MOLREP   phasing           .   ? 2 
REFMAC   refinement        5.0 ? 3 
HKL-2000 'data reduction'  .   ? 4 
HKL-2000 'data scaling'    .   ? 5 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB B ASP 14 ? ? CA B ASP 14 ? ? C B ASP 14 ? ? 96.36  110.40 -14.04 2.00 N 
2 1 N  B ASP 14 ? ? CA B ASP 14 ? ? C B ASP 14 ? ? 127.88 111.00 16.88  2.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 10  ? ? 58.33   -148.25 
2  1 PHE A 35  ? ? -76.35  -73.44  
3  1 SER A 36  ? ? -148.31 -70.96  
4  1 SER A 58  ? ? -69.25  -173.81 
5  1 CYS A 60  ? ? -71.96  20.31   
6  1 ILE A 107 ? ? -103.27 78.57   
7  1 HIS A 123 ? ? -172.79 144.75  
8  1 ASN A 158 ? ? -145.54 -17.83  
9  1 GLU A 161 ? ? -84.63  32.84   
10 1 VAL A 187 ? ? -127.23 -169.72 
11 1 ASP A 224 ? ? -97.96  -64.62  
12 1 ALA A 257 ? ? 39.82   -133.95 
13 1 ASN A 273 ? ? -99.17  34.79   
14 1 SER B 10  ? ? -161.89 -150.25 
15 1 ASP B 14  ? ? -32.79  -35.45  
16 1 ASN B 37  ? ? -62.44  9.69    
17 1 GLN B 97  ? ? -107.37 70.12   
18 1 ASP B 128 ? ? 42.15   70.62   
19 1 VAL B 187 ? ? -129.55 -167.01 
20 1 ASP B 224 ? ? -105.78 -73.01  
21 1 CYS B 265 ? ? -90.82  41.40   
22 1 ASN B 273 ? ? -97.03  32.95   
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ASN 3   ? CG  ? A ASN 3   CG  
2   1 Y 1 A ASN 3   ? OD1 ? A ASN 3   OD1 
3   1 Y 1 A ASN 3   ? ND2 ? A ASN 3   ND2 
4   1 Y 1 A LYS 5   ? CD  ? A LYS 5   CD  
5   1 Y 1 A LYS 5   ? CE  ? A LYS 5   CE  
6   1 Y 1 A LYS 5   ? NZ  ? A LYS 5   NZ  
7   1 Y 1 A VAL 31  ? CG1 ? A VAL 31  CG1 
8   1 Y 1 A VAL 31  ? CG2 ? A VAL 31  CG2 
9   1 Y 1 A LYS 33  ? CD  ? A LYS 33  CD  
10  1 Y 1 A LYS 33  ? CE  ? A LYS 33  CE  
11  1 Y 1 A LYS 33  ? NZ  ? A LYS 33  NZ  
12  1 Y 1 A LYS 34  ? CG  ? A LYS 34  CG  
13  1 Y 1 A LYS 34  ? CD  ? A LYS 34  CD  
14  1 Y 1 A LYS 34  ? CE  ? A LYS 34  CE  
15  1 Y 1 A LYS 34  ? NZ  ? A LYS 34  NZ  
16  1 Y 1 A ASN 37  ? CG  ? A ASN 37  CG  
17  1 Y 1 A ASN 37  ? OD1 ? A ASN 37  OD1 
18  1 Y 1 A ASN 37  ? ND2 ? A ASN 37  ND2 
19  1 Y 1 A CYS 41  ? SG  ? A CYS 41  SG  
20  1 Y 1 A LYS 102 ? CG  ? A LYS 102 CG  
21  1 Y 1 A LYS 102 ? CD  ? A LYS 102 CD  
22  1 Y 1 A LYS 102 ? CE  ? A LYS 102 CE  
23  1 Y 1 A LYS 102 ? NZ  ? A LYS 102 NZ  
24  1 Y 1 A LYS 153 ? CE  ? A LYS 153 CE  
25  1 Y 1 A LYS 153 ? NZ  ? A LYS 153 NZ  
26  1 Y 1 A ILE 159 ? CD1 ? A ILE 159 CD1 
27  1 Y 1 A GLU 161 ? CD  ? A GLU 161 CD  
28  1 Y 1 A GLU 161 ? OE1 ? A GLU 161 OE1 
29  1 Y 1 A GLU 161 ? OE2 ? A GLU 161 OE2 
30  1 Y 1 A LYS 176 ? CD  ? A LYS 176 CD  
31  1 Y 1 A LYS 176 ? CE  ? A LYS 176 CE  
32  1 Y 1 A LYS 176 ? NZ  ? A LYS 176 NZ  
33  1 Y 1 A LYS 194 ? CG  ? A LYS 194 CG  
34  1 Y 1 A LYS 194 ? CD  ? A LYS 194 CD  
35  1 Y 1 A LYS 194 ? CE  ? A LYS 194 CE  
36  1 Y 1 A LYS 194 ? NZ  ? A LYS 194 NZ  
37  1 Y 1 A ARG 196 ? CG  ? A ARG 196 CG  
38  1 Y 1 A ARG 196 ? CD  ? A ARG 196 CD  
39  1 Y 1 A ARG 196 ? NE  ? A ARG 196 NE  
40  1 Y 1 A ARG 196 ? CZ  ? A ARG 196 CZ  
41  1 Y 1 A ARG 196 ? NH1 ? A ARG 196 NH1 
42  1 Y 1 A ARG 196 ? NH2 ? A ARG 196 NH2 
43  1 Y 1 A ARG 204 ? CG  ? A ARG 204 CG  
44  1 Y 1 A ARG 204 ? CD  ? A ARG 204 CD  
45  1 Y 1 A ARG 204 ? NE  ? A ARG 204 NE  
46  1 Y 1 A ARG 204 ? CZ  ? A ARG 204 CZ  
47  1 Y 1 A ARG 204 ? NH1 ? A ARG 204 NH1 
48  1 Y 1 A ARG 204 ? NH2 ? A ARG 204 NH2 
49  1 Y 1 A MET 205 ? CE  ? A MET 205 CE  
50  1 Y 1 A LYS 212 ? CG  ? A LYS 212 CG  
51  1 Y 1 A LYS 212 ? CD  ? A LYS 212 CD  
52  1 Y 1 A LYS 212 ? CE  ? A LYS 212 CE  
53  1 Y 1 A LYS 212 ? NZ  ? A LYS 212 NZ  
54  1 Y 1 A ILE 229 ? CD1 ? A ILE 229 CD1 
55  1 Y 1 A ILE 258 ? CG1 ? A ILE 258 CG1 
56  1 Y 1 A ILE 258 ? CG2 ? A ILE 258 CG2 
57  1 Y 1 A ILE 258 ? CD1 ? A ILE 258 CD1 
58  1 Y 1 A ILE 261 ? CD1 ? A ILE 261 CD1 
59  1 Y 1 A ASN 263 ? CG  ? A ASN 263 CG  
60  1 Y 1 A ASN 263 ? OD1 ? A ASN 263 OD1 
61  1 Y 1 A ASN 263 ? ND2 ? A ASN 263 ND2 
62  1 Y 1 A LYS 282 ? CG  ? A LYS 282 CG  
63  1 Y 1 A LYS 282 ? CD  ? A LYS 282 CD  
64  1 Y 1 A LYS 282 ? CE  ? A LYS 282 CE  
65  1 Y 1 A LYS 282 ? NZ  ? A LYS 282 NZ  
66  1 Y 1 A LYS 286 ? NZ  ? A LYS 286 NZ  
67  1 Y 1 A MET 294 ? SD  ? A MET 294 SD  
68  1 Y 1 A MET 294 ? CE  ? A MET 294 CE  
69  1 Y 1 A HIS 315 ? CG  ? A HIS 315 CG  
70  1 Y 1 A HIS 315 ? ND1 ? A HIS 315 ND1 
71  1 Y 1 A HIS 315 ? CD2 ? A HIS 315 CD2 
72  1 Y 1 A HIS 315 ? CE1 ? A HIS 315 CE1 
73  1 Y 1 A HIS 315 ? NE2 ? A HIS 315 NE2 
74  1 Y 1 B LYS 5   ? NZ  ? B LYS 5   NZ  
75  1 Y 1 B LYS 29  ? CG  ? B LYS 29  CG  
76  1 Y 1 B LYS 29  ? CD  ? B LYS 29  CD  
77  1 Y 1 B LYS 29  ? CE  ? B LYS 29  CE  
78  1 Y 1 B LYS 29  ? NZ  ? B LYS 29  NZ  
79  1 Y 1 B LYS 33  ? CG  ? B LYS 33  CG  
80  1 Y 1 B LYS 33  ? CD  ? B LYS 33  CD  
81  1 Y 1 B LYS 33  ? CE  ? B LYS 33  CE  
82  1 Y 1 B LYS 33  ? NZ  ? B LYS 33  NZ  
83  1 Y 1 B LYS 34  ? CE  ? B LYS 34  CE  
84  1 Y 1 B LYS 34  ? NZ  ? B LYS 34  NZ  
85  1 Y 1 B GLU 43  ? CG  ? B GLU 43  CG  
86  1 Y 1 B GLU 43  ? CD  ? B GLU 43  CD  
87  1 Y 1 B GLU 43  ? OE1 ? B GLU 43  OE1 
88  1 Y 1 B GLU 43  ? OE2 ? B GLU 43  OE2 
89  1 Y 1 B LYS 99  ? CE  ? B LYS 99  CE  
90  1 Y 1 B LYS 99  ? NZ  ? B LYS 99  NZ  
91  1 Y 1 B LYS 102 ? CD  ? B LYS 102 CD  
92  1 Y 1 B LYS 102 ? CE  ? B LYS 102 CE  
93  1 Y 1 B LYS 102 ? NZ  ? B LYS 102 NZ  
94  1 Y 1 B LYS 176 ? CG  ? B LYS 176 CG  
95  1 Y 1 B LYS 176 ? CD  ? B LYS 176 CD  
96  1 Y 1 B LYS 176 ? CE  ? B LYS 176 CE  
97  1 Y 1 B LYS 176 ? NZ  ? B LYS 176 NZ  
98  1 Y 1 B ARG 184 ? NE  ? B ARG 184 NE  
99  1 Y 1 B ARG 184 ? CZ  ? B ARG 184 CZ  
100 1 Y 1 B ARG 184 ? NH1 ? B ARG 184 NH1 
101 1 Y 1 B ARG 184 ? NH2 ? B ARG 184 NH2 
102 1 Y 1 B LYS 194 ? CE  ? B LYS 194 CE  
103 1 Y 1 B LYS 194 ? NZ  ? B LYS 194 NZ  
104 1 Y 1 B LYS 212 ? CE  ? B LYS 212 CE  
105 1 Y 1 B LYS 212 ? NZ  ? B LYS 212 NZ  
106 1 Y 1 B ASP 279 ? CG  ? B ASP 279 CG  
107 1 Y 1 B ASP 279 ? OD1 ? B ASP 279 OD1 
108 1 Y 1 B ASP 279 ? OD2 ? B ASP 279 OD2 
109 1 Y 1 B LYS 282 ? NZ  ? B LYS 282 NZ  
# 
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 LYS 197 ? A LYS 197 
3  1 Y 1 A LYS 198 ? A LYS 198 
4  1 Y 1 A ALA 199 ? A ALA 199 
5  1 Y 1 A ASN 200 ? A ASN 200 
6  1 Y 1 A GLU 201 ? A GLU 201 
7  1 Y 1 A VAL 202 ? A VAL 202 
8  1 Y 1 A ASP 203 ? A ASP 203 
9  1 Y 1 A PRO 317 ? A PRO 317 
10 1 Y 1 A LEU 318 ? A LEU 318 
11 1 Y 1 A LEU 319 ? A LEU 319 
12 1 Y 1 A GLU 320 ? A GLU 320 
13 1 Y 1 A HIS 321 ? A HIS 321 
14 1 Y 1 A HIS 322 ? A HIS 322 
15 1 Y 1 A HIS 323 ? A HIS 323 
16 1 Y 1 A HIS 324 ? A HIS 324 
17 1 Y 1 A HIS 325 ? A HIS 325 
18 1 Y 1 A HIS 326 ? A HIS 326 
19 1 Y 1 B MET 1   ? B MET 1   
20 1 Y 1 B PRO 2   ? B PRO 2   
21 1 Y 1 B ARG 196 ? B ARG 196 
22 1 Y 1 B LYS 197 ? B LYS 197 
23 1 Y 1 B LYS 198 ? B LYS 198 
24 1 Y 1 B ALA 199 ? B ALA 199 
25 1 Y 1 B ASN 200 ? B ASN 200 
26 1 Y 1 B GLU 201 ? B GLU 201 
27 1 Y 1 B VAL 202 ? B VAL 202 
28 1 Y 1 B LEU 318 ? B LEU 318 
29 1 Y 1 B LEU 319 ? B LEU 319 
30 1 Y 1 B GLU 320 ? B GLU 320 
31 1 Y 1 B HIS 321 ? B HIS 321 
32 1 Y 1 B HIS 322 ? B HIS 322 
33 1 Y 1 B HIS 323 ? B HIS 323 
34 1 Y 1 B HIS 324 ? B HIS 324 
35 1 Y 1 B HIS 325 ? B HIS 325 
36 1 Y 1 B HIS 326 ? B HIS 326 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'   SO4 
3 'MAGNESIUM ION' MG  
4 water           HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SO4 1  401  1002 SO4 SO4 A . 
D 2 SO4 1  402  1004 SO4 SO4 A . 
E 2 SO4 1  403  1006 SO4 SO4 A . 
F 3 MG  1  404  1    MG  MG  A . 
G 2 SO4 1  1001 1001 SO4 SO4 B . 
H 2 SO4 1  1002 1003 SO4 SO4 B . 
I 2 SO4 1  1003 1005 SO4 SO4 B . 
J 3 MG  1  1004 1    MG  MG  B . 
K 4 HOH 1  501  6    HOH HOH A . 
K 4 HOH 2  502  9    HOH HOH A . 
K 4 HOH 3  503  12   HOH HOH A . 
K 4 HOH 4  504  13   HOH HOH A . 
K 4 HOH 5  505  17   HOH HOH A . 
K 4 HOH 6  506  20   HOH HOH A . 
K 4 HOH 7  507  22   HOH HOH A . 
K 4 HOH 8  508  24   HOH HOH A . 
K 4 HOH 9  509  26   HOH HOH A . 
K 4 HOH 10 510  27   HOH HOH A . 
K 4 HOH 11 511  28   HOH HOH A . 
K 4 HOH 12 512  30   HOH HOH A . 
K 4 HOH 13 513  31   HOH HOH A . 
K 4 HOH 14 514  32   HOH HOH A . 
K 4 HOH 15 515  33   HOH HOH A . 
K 4 HOH 16 516  34   HOH HOH A . 
K 4 HOH 17 517  42   HOH HOH A . 
K 4 HOH 18 518  43   HOH HOH A . 
K 4 HOH 19 519  47   HOH HOH A . 
K 4 HOH 20 520  50   HOH HOH A . 
K 4 HOH 21 521  51   HOH HOH A . 
K 4 HOH 22 522  59   HOH HOH A . 
K 4 HOH 23 523  61   HOH HOH A . 
K 4 HOH 24 524  63   HOH HOH A . 
K 4 HOH 25 525  65   HOH HOH A . 
K 4 HOH 26 526  66   HOH HOH A . 
K 4 HOH 27 527  69   HOH HOH A . 
K 4 HOH 28 528  70   HOH HOH A . 
K 4 HOH 29 529  76   HOH HOH A . 
L 4 HOH 1  1101 1    HOH HOH B . 
L 4 HOH 2  1102 2    HOH HOH B . 
L 4 HOH 3  1103 3    HOH HOH B . 
L 4 HOH 4  1104 4    HOH HOH B . 
L 4 HOH 5  1105 5    HOH HOH B . 
L 4 HOH 6  1106 7    HOH HOH B . 
L 4 HOH 7  1107 8    HOH HOH B . 
L 4 HOH 8  1108 10   HOH HOH B . 
L 4 HOH 9  1109 11   HOH HOH B . 
L 4 HOH 10 1110 14   HOH HOH B . 
L 4 HOH 11 1111 15   HOH HOH B . 
L 4 HOH 12 1112 16   HOH HOH B . 
L 4 HOH 13 1113 18   HOH HOH B . 
L 4 HOH 14 1114 19   HOH HOH B . 
L 4 HOH 15 1115 21   HOH HOH B . 
L 4 HOH 16 1116 23   HOH HOH B . 
L 4 HOH 17 1117 25   HOH HOH B . 
L 4 HOH 18 1118 29   HOH HOH B . 
L 4 HOH 19 1119 35   HOH HOH B . 
L 4 HOH 20 1120 36   HOH HOH B . 
L 4 HOH 21 1121 37   HOH HOH B . 
L 4 HOH 22 1122 38   HOH HOH B . 
L 4 HOH 23 1123 39   HOH HOH B . 
L 4 HOH 24 1124 41   HOH HOH B . 
L 4 HOH 25 1125 44   HOH HOH B . 
L 4 HOH 26 1126 45   HOH HOH B . 
L 4 HOH 27 1127 46   HOH HOH B . 
L 4 HOH 28 1128 48   HOH HOH B . 
L 4 HOH 29 1129 49   HOH HOH B . 
L 4 HOH 30 1130 52   HOH HOH B . 
L 4 HOH 31 1131 53   HOH HOH B . 
L 4 HOH 32 1132 54   HOH HOH B . 
L 4 HOH 33 1133 55   HOH HOH B . 
L 4 HOH 34 1134 56   HOH HOH B . 
L 4 HOH 35 1135 57   HOH HOH B . 
L 4 HOH 36 1136 58   HOH HOH B . 
L 4 HOH 37 1137 60   HOH HOH B . 
L 4 HOH 38 1138 62   HOH HOH B . 
L 4 HOH 39 1139 67   HOH HOH B . 
L 4 HOH 40 1140 68   HOH HOH B . 
L 4 HOH 41 1141 71   HOH HOH B . 
L 4 HOH 42 1142 72   HOH HOH B . 
L 4 HOH 43 1143 73   HOH HOH B . 
L 4 HOH 44 1144 74   HOH HOH B . 
# 
