data_4M0P
# 
_entry.id   4M0P 
# 
_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   4M0P         
RCSB  RCSB081318   
WWPDB D_1000081318 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4LYG . unspecified 
PDB 4LZP . unspecified 
PDB 4LZO . unspecified 
PDB 4M0U . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4M0P 
_pdbx_database_status.recvd_initial_deposition_date   2013-08-01 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Chen, P.' 1 
'Teng, M.' 2 
'Li, X.'   3 
# 
_citation.id                        primary 
_citation.title                     
;Crystal and EM Structures of Human Phosphoribosyl Pyrophosphate Synthase I (PRS1) Provide Novel Insights into the Disease-Associated Mutations
;
_citation.journal_abbrev            'Plos One' 
_citation.journal_volume            10 
_citation.page_first                e0120304 
_citation.page_last                 e0120304 
_citation.year                      2015 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25781187 
_citation.pdbx_database_id_DOI      10.1371/journal.pone.0120304 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Chen, P.'  1  
primary 'Liu, Z.'   2  
primary 'Wang, X.'  3  
primary 'Peng, J.'  4  
primary 'Sun, Q.'   5  
primary 'Li, J.'    6  
primary 'Wang, M.'  7  
primary 'Niu, L.'   8  
primary 'Zhang, Z.' 9  
primary 'Cai, G.'   10 
primary 'Teng, M.'  11 
primary 'Li, X.'    12 
# 
_cell.entry_id           4M0P 
_cell.length_a           170.080 
_cell.length_b           170.080 
_cell.length_c           61.624 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              18 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4M0P 
_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' 35920.281 2  2.7.6.1 M115T ? ? 
2 non-polymer syn 'SULFATE ION'                          96.063    6  ?       ?     ? ? 
3 water       nat water                                  18.015    52 ?       ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'PPRibP, Phosphoribosyl pyrophosphate synthase I, PRS-I' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANTLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANTLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   ASN n 
1 4   ILE n 
1 5   LYS n 
1 6   ILE n 
1 7   PHE n 
1 8   SER n 
1 9   GLY n 
1 10  SER n 
1 11  SER n 
1 12  HIS n 
1 13  GLN n 
1 14  ASP n 
1 15  LEU n 
1 16  SER n 
1 17  GLN n 
1 18  LYS n 
1 19  ILE n 
1 20  ALA n 
1 21  ASP n 
1 22  ARG n 
1 23  LEU n 
1 24  GLY n 
1 25  LEU n 
1 26  GLU n 
1 27  LEU n 
1 28  GLY n 
1 29  LYS n 
1 30  VAL n 
1 31  VAL n 
1 32  THR n 
1 33  LYS n 
1 34  LYS n 
1 35  PHE n 
1 36  SER n 
1 37  ASN n 
1 38  GLN n 
1 39  GLU n 
1 40  THR n 
1 41  CYS n 
1 42  VAL n 
1 43  GLU n 
1 44  ILE n 
1 45  GLY n 
1 46  GLU n 
1 47  SER n 
1 48  VAL n 
1 49  ARG n 
1 50  GLY n 
1 51  GLU n 
1 52  ASP n 
1 53  VAL n 
1 54  TYR n 
1 55  ILE n 
1 56  VAL n 
1 57  GLN n 
1 58  SER n 
1 59  GLY n 
1 60  CYS n 
1 61  GLY n 
1 62  GLU n 
1 63  ILE n 
1 64  ASN n 
1 65  ASP n 
1 66  ASN n 
1 67  LEU n 
1 68  MET n 
1 69  GLU n 
1 70  LEU n 
1 71  LEU n 
1 72  ILE n 
1 73  MET n 
1 74  ILE n 
1 75  ASN n 
1 76  ALA n 
1 77  CYS n 
1 78  LYS n 
1 79  ILE n 
1 80  ALA n 
1 81  SER n 
1 82  ALA n 
1 83  SER n 
1 84  ARG n 
1 85  VAL n 
1 86  THR n 
1 87  ALA n 
1 88  VAL n 
1 89  ILE n 
1 90  PRO n 
1 91  CYS n 
1 92  PHE n 
1 93  PRO n 
1 94  TYR n 
1 95  ALA n 
1 96  ARG n 
1 97  GLN n 
1 98  ASP n 
1 99  LYS n 
1 100 LYS n 
1 101 ASP n 
1 102 LYS n 
1 103 SER n 
1 104 ARG n 
1 105 ALA n 
1 106 PRO n 
1 107 ILE n 
1 108 SER n 
1 109 ALA n 
1 110 LYS n 
1 111 LEU n 
1 112 VAL n 
1 113 ALA n 
1 114 ASN n 
1 115 THR 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 4M0P A 1 ? 318 ? P60891 1 ? 318 ? 1 318 
2 1 4M0P 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 4M0P THR A 115 ? UNP P60891 MET 115 'ENGINEERED MUTATION' 115 1  
1 4M0P LEU A 319 ? UNP P60891 ?   ?   'EXPRESSION TAG'      319 2  
1 4M0P GLU A 320 ? UNP P60891 ?   ?   'EXPRESSION TAG'      320 3  
1 4M0P HIS A 321 ? UNP P60891 ?   ?   'EXPRESSION TAG'      321 4  
1 4M0P HIS A 322 ? UNP P60891 ?   ?   'EXPRESSION TAG'      322 5  
1 4M0P HIS A 323 ? UNP P60891 ?   ?   'EXPRESSION TAG'      323 6  
1 4M0P HIS A 324 ? UNP P60891 ?   ?   'EXPRESSION TAG'      324 7  
1 4M0P HIS A 325 ? UNP P60891 ?   ?   'EXPRESSION TAG'      325 8  
1 4M0P HIS A 326 ? UNP P60891 ?   ?   'EXPRESSION TAG'      326 9  
2 4M0P THR B 115 ? UNP P60891 MET 115 'ENGINEERED MUTATION' 115 10 
2 4M0P LEU B 319 ? UNP P60891 ?   ?   'EXPRESSION TAG'      319 11 
2 4M0P GLU B 320 ? UNP P60891 ?   ?   'EXPRESSION TAG'      320 12 
2 4M0P HIS B 321 ? UNP P60891 ?   ?   'EXPRESSION TAG'      321 13 
2 4M0P HIS B 322 ? UNP P60891 ?   ?   'EXPRESSION TAG'      322 14 
2 4M0P HIS B 323 ? UNP P60891 ?   ?   'EXPRESSION TAG'      323 15 
2 4M0P HIS B 324 ? UNP P60891 ?   ?   'EXPRESSION TAG'      324 16 
2 4M0P HIS B 325 ? UNP P60891 ?   ?   'EXPRESSION TAG'      325 17 
2 4M0P HIS B 326 ? UNP P60891 ?   ?   'EXPRESSION TAG'      326 18 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4M0P 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.39 
_exptl_crystal.density_percent_sol   48.48 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.temp            295 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.1 
_exptl_crystal_grow.pdbx_details    'pH 4.1, VAPOR DIFFUSION, temperature 295K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315r' 
_diffrn_detector.pdbx_collection_date   ? 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   . 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRF BEAMLINE BL17U' 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_synchrotron_beamline   BL17U 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     4M0P 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             49.1 
_reflns.d_resolution_high            2.11 
_reflns.number_obs                   38116 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         ? 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high                  2.11 
_reflns_shell.d_res_low                   ? 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.pdbx_redundancy             ? 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.number_possible             ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
# 
_refine.entry_id                                 4M0P 
_refine.ls_number_reflns_obs                     36190 
_refine.ls_number_reflns_all                     38116 
_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                             49.10 
_refine.ls_d_res_high                            2.11 
_refine.ls_percent_reflns_obs                    99.74 
_refine.ls_R_factor_obs                          0.17238 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.17145 
_refine.ls_R_factor_R_free                       0.19071 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  1893 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_refine.B_iso_mean                               38.721 
_refine.aniso_B[1][1]                            4.02 
_refine.aniso_B[2][2]                            4.02 
_refine.aniso_B[3][3]                            -8.04 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.041 
_refine.pdbx_overall_ESU_R_Free                  0.031 
_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        4669 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             52 
_refine_hist.number_atoms_total               4751 
_refine_hist.d_res_high                       2.11 
_refine_hist.d_res_low                        49.10 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d             0.009  0.022  ? 4754 ? 'X-RAY DIFFRACTION' 
r_bond_other_d               ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg          1.144  1.959  ? 6436 ? 'X-RAY DIFFRACTION' 
r_angle_other_deg            ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg       5.403  5.000  ? 606  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg       36.889 24.523 ? 199  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg       14.830 15.000 ? 842  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg       16.923 15.000 ? 30   ? 'X-RAY DIFFRACTION' 
r_chiral_restr               0.078  0.200  ? 765  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined         0.004  0.021  ? 3470 ? 'X-RAY DIFFRACTION' 
r_gen_planes_other           ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_nbd_refined                ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_nbd_other                  ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_nbtor_refined              ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_nbtor_other                ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined        ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_other          ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined          ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_metal_ion_other            ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined       ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_other         ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined     ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_other       ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_metal_ion_refined ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_symmetry_metal_ion_other   ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_mcbond_it                  0.783  1.500  ? 3034 ? 'X-RAY DIFFRACTION' 
r_mcbond_other               ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_mcangle_it                 1.695  2.000  ? 4908 ? 'X-RAY DIFFRACTION' 
r_mcangle_other              ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_scbond_it                  2.888  3.000  ? 1720 ? 'X-RAY DIFFRACTION' 
r_scbond_other               ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_scangle_it                 3.273  4.500  ? 1528 ? 'X-RAY DIFFRACTION' 
r_scangle_other              ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_long_range_B_refined       ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_long_range_B_other         ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr           ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_sphericity_free            ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded          ?      ?      ? ?    ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.111 
_refine_ls_shell.d_res_low                        2.166 
_refine_ls_shell.number_reflns_R_work             2604 
_refine_ls_shell.R_factor_R_work                  0.296 
_refine_ls_shell.percent_reflns_obs               97.22 
_refine_ls_shell.R_factor_R_free                  0.288 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             163 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  4M0P 
_struct.title                     'Crystal structure of human PRS1 M115T 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        4M0P 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'PRS1, PRPP synthesis enzyme, ATP R5P, TRANSFERASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 3 ? 
# 
_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  ? LEU A 23  ? GLN A 13  LEU A 23  1 ? 11 
HELX_P HELX_P2  2  GLU A 62  ? ALA A 80  ? GLU A 62  ALA A 80  1 ? 19 
HELX_P HELX_P3  3  ILE A 107 ? GLY A 120 ? ILE A 107 GLY A 120 1 ? 14 
HELX_P HELX_P4  4  ALA A 131 ? PHE A 138 ? ALA A 131 PHE A 138 5 ? 8  
HELX_P HELX_P5  5  ALA A 147 ? ILE A 159 ? ALA A 147 ILE A 159 1 ? 13 
HELX_P HELX_P6  6  GLU A 161 ? ASN A 164 ? GLU A 161 ASN A 164 5 ? 4  
HELX_P HELX_P7  7  ASP A 171 ? GLY A 173 ? ASP A 171 GLY A 173 5 ? 3  
HELX_P HELX_P8  8  GLY A 174 ? 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 VAL A 309 ? PHE A 313 ? VAL A 309 PHE A 313 5 ? 5  
HELX_P HELX_P14 14 GLN B 13  ? LEU B 23  ? GLN B 13  LEU B 23  1 ? 11 
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 ? ALA B 264 ? PRO B 256 ALA B 264 1 ? 9  
HELX_P HELX_P24 24 GLN B 277 ? HIS B 283 ? GLN B 277 HIS B 283 1 ? 7  
HELX_P HELX_P25 25 ILE B 292 ? GLY B 306 ? ILE B 292 GLY B 306 1 ? 15 
HELX_P HELX_P26 26 VAL B 309 ? SER B 314 ? VAL B 309 SER B 314 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 2 ? 
C ? 7 ? 
D ? 5 ? 
E ? 2 ? 
F ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
C 6 7 ? parallel      
D 1 2 ? parallel      
D 2 3 ? parallel      
D 3 4 ? parallel      
D 4 5 ? parallel      
E 1 2 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? parallel      
F 3 4 ? parallel      
F 4 5 ? parallel      
F 5 6 ? parallel      
F 6 7 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ILE A 4   ? SER A 8   ? ILE A 4   SER A 8   
A 2 ASP A 52  ? VAL A 56  ? ASP A 52  VAL A 56  
A 3 ARG A 84  ? ILE A 89  ? ARG A 84  ILE A 89  
A 4 HIS A 123 ? MET A 127 ? HIS A 123 MET A 127 
A 5 VAL A 142 ? LEU A 145 ? VAL A 142 LEU A 145 
B 1 VAL A 30  ? LYS A 34  ? VAL A 30  LYS A 34  
B 2 THR A 40  ? ILE A 44  ? THR A 40  ILE A 44  
C 1 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 ALA A 268 ? THR A 272 ? ALA A 268 THR A 272 
C 7 ILE A 287 ? ILE A 290 ? ILE A 287 ILE A 290 
D 1 ILE B 4   ? SER B 8   ? ILE B 4   SER B 8   
D 2 ASP B 52  ? VAL B 56  ? ASP B 52  VAL B 56  
D 3 ARG B 84  ? ILE B 89  ? ARG B 84  ILE B 89  
D 4 HIS B 123 ? MET B 127 ? HIS B 123 MET B 127 
D 5 VAL B 142 ? LEU B 145 ? VAL B 142 LEU B 145 
E 1 VAL B 30  ? LYS B 34  ? VAL B 30  LYS B 34  
E 2 THR B 40  ? ILE B 44  ? THR B 40  ILE B 44  
F 1 MET B 205 ? VAL B 208 ? MET B 205 VAL B 208 
F 2 ASP B 188 ? LYS B 194 ? ASP B 188 LYS B 194 
F 3 THR B 166 ? SER B 169 ? THR B 166 SER B 169 
F 4 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 PHE B 266 ? THR B 272 ? PHE B 266 THR B 272 
F 7 ILE B 287 ? ILE B 290 ? ILE B 287 ILE B 290 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N LYS A 5   ? N LYS A 5   O TYR A 54  ? O TYR A 54  
A 2 3 N ILE A 55  ? N ILE A 55  O VAL A 88  ? O VAL A 88  
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 LYS A 33  ? N LYS A 33  O CYS A 41  ? O CYS A 41  
C 1 2 O VAL A 206 ? O VAL A 206 N HIS A 193 ? N HIS A 193 
C 2 3 O ILE A 192 ? O ILE A 192 N SER A 169 ? N SER A 169 
C 3 4 N VAL A 168 ? N VAL A 168 O ILE A 217 ? O ILE A 217 
C 4 5 N LEU A 218 ? N LEU A 218 O ILE A 247 ? O ILE A 247 
C 5 6 N LEU A 248 ? N LEU A 248 O VAL A 270 ? O VAL A 270 
C 6 7 N VAL A 271 ? N VAL A 271 O ILE A 290 ? O ILE A 290 
D 1 2 N 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 ALA B 87  ? N ALA B 87  O ILE B 125 ? O ILE B 125 
D 4 5 N THR B 126 ? N THR B 126 O LEU B 145 ? O LEU B 145 
E 1 2 N LYS B 33  ? N LYS B 33  O CYS B 41  ? O CYS B 41  
F 1 2 O VAL B 206 ? O VAL B 206 N HIS B 193 ? N HIS B 193 
F 2 3 O ASP B 188 ? O ASP B 188 N ILE B 167 ? N ILE B 167 
F 3 4 N VAL B 168 ? N VAL B 168 O ILE B 217 ? O ILE B 217 
F 4 5 N LEU B 218 ? N LEU B 218 O TYR B 245 ? O TYR B 245 
F 5 6 N ALA B 246 ? N ALA B 246 O VAL B 270 ? O VAL B 270 
F 6 7 N VAL B 271 ? N VAL B 271 O ILE B 290 ? O ILE B 290 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 A 1001' 
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1002' 
AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 A 1003' 
AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 B 401'  
AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 B 402'  
AC6 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE SO4 B 403'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 7 SER A 47  ? SER A 47   . ? 2_555 ? 
2  AC1 7 ARG A 49  ? ARG A 49   . ? 2_555 ? 
3  AC1 7 SER A 308 ? SER A 308  . ? 1_555 ? 
4  AC1 7 VAL A 309 ? VAL A 309  . ? 1_555 ? 
5  AC1 7 SER A 310 ? SER A 310  . ? 1_555 ? 
6  AC1 7 HOH I .   ? HOH A 1111 . ? 1_555 ? 
7  AC1 7 ARG B 104 ? ARG B 104  . ? 2_555 ? 
8  AC2 4 ASP A 224 ? ASP A 224  . ? 1_555 ? 
9  AC2 4 THR A 225 ? THR A 225  . ? 1_555 ? 
10 AC2 4 CYS A 226 ? CYS A 226  . ? 1_555 ? 
11 AC2 4 THR A 228 ? THR A 228  . ? 1_555 ? 
12 AC3 8 SER A 132 ? SER A 132  . ? 1_555 ? 
13 AC3 8 GLN A 135 ? GLN A 135  . ? 1_555 ? 
14 AC3 8 ASN A 144 ? ASN A 144  . ? 1_555 ? 
15 AC3 8 TYR A 146 ? TYR A 146  . ? 1_555 ? 
16 AC3 8 HOH I .   ? HOH A 1102 . ? 1_555 ? 
17 AC3 8 LYS B 100 ? LYS B 100  . ? 2_555 ? 
18 AC3 8 ASP B 101 ? ASP B 101  . ? 2_555 ? 
19 AC3 8 LYS B 102 ? LYS B 102  . ? 2_555 ? 
20 AC4 7 ARG A 104 ? ARG A 104  . ? 3_555 ? 
21 AC4 7 SER B 47  ? SER B 47   . ? 3_555 ? 
22 AC4 7 ARG B 49  ? ARG B 49   . ? 3_555 ? 
23 AC4 7 SER B 308 ? SER B 308  . ? 1_555 ? 
24 AC4 7 VAL B 309 ? VAL B 309  . ? 1_555 ? 
25 AC4 7 SER B 310 ? SER B 310  . ? 1_555 ? 
26 AC4 7 HOH J .   ? HOH B 511  . ? 3_555 ? 
27 AC5 6 ASP B 224 ? ASP B 224  . ? 1_555 ? 
28 AC5 6 THR B 225 ? THR B 225  . ? 1_555 ? 
29 AC5 6 CYS B 226 ? CYS B 226  . ? 1_555 ? 
30 AC5 6 GLY B 227 ? GLY B 227  . ? 1_555 ? 
31 AC5 6 THR B 228 ? THR B 228  . ? 1_555 ? 
32 AC5 6 HOH J .   ? HOH B 512  . ? 1_555 ? 
33 AC6 9 LYS A 99  ? LYS A 99   . ? 3_555 ? 
34 AC6 9 LYS A 100 ? LYS A 100  . ? 3_555 ? 
35 AC6 9 ASP A 101 ? ASP A 101  . ? 3_555 ? 
36 AC6 9 LYS A 102 ? LYS A 102  . ? 3_555 ? 
37 AC6 9 SER B 132 ? SER B 132  . ? 1_555 ? 
38 AC6 9 GLN B 135 ? GLN B 135  . ? 1_555 ? 
39 AC6 9 ASN B 144 ? ASN B 144  . ? 1_555 ? 
40 AC6 9 TYR B 146 ? TYR B 146  . ? 1_555 ? 
41 AC6 9 HOH J .   ? HOH B 504  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4M0P 
_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                    4M0P 
_atom_sites.fract_transf_matrix[1][1]   0.005880 
_atom_sites.fract_transf_matrix[1][2]   0.003395 
_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]   0.006789 
_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]   0.016227 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASN A 1 3   ? 2.524   -12.363 31.086  1.00   42.14  ? 3    ASN A N   1 
ATOM   2    C CA  . ASN A 1 3   ? 2.350   -11.331 30.014  1.00   41.26  ? 3    ASN A CA  1 
ATOM   3    C C   . ASN A 1 3   ? 3.196   -11.668 28.804  1.00   40.58  ? 3    ASN A C   1 
ATOM   4    O O   . ASN A 1 3   ? 2.736   -11.575 27.661  1.00   40.13  ? 3    ASN A O   1 
ATOM   5    C CB  . ASN A 1 3   ? 2.752   -9.957  30.539  1.00   42.25  ? 3    ASN A CB  1 
ATOM   6    C CG  . ASN A 1 3   ? 2.243   -8.830  29.680  1.00   43.44  ? 3    ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 3   ? 1.146   -8.897  29.123  1.00   45.87  ? 3    ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 3   ? 3.031   -7.765  29.588  1.00   46.68  ? 3    ASN A ND2 1 
ATOM   9    N N   . ILE A 1 4   ? 4.447   -12.026 29.065  1.00   39.22  ? 4    ILE A N   1 
ATOM   10   C CA  . ILE A 1 4   ? 5.327   -12.547 28.035  1.00   38.43  ? 4    ILE A CA  1 
ATOM   11   C C   . ILE A 1 4   ? 5.029   -14.026 27.772  1.00   37.44  ? 4    ILE A C   1 
ATOM   12   O O   . ILE A 1 4   ? 4.803   -14.811 28.703  1.00   37.09  ? 4    ILE A O   1 
ATOM   13   C CB  . ILE A 1 4   ? 6.807   -12.364 28.405  1.00   38.70  ? 4    ILE A CB  1 
ATOM   14   C CG1 . ILE A 1 4   ? 7.700   -13.021 27.347  1.00   38.13  ? 4    ILE A CG1 1 
ATOM   15   C CG2 . ILE A 1 4   ? 7.089   -12.913 29.819  1.00   39.24  ? 4    ILE A CG2 1 
ATOM   16   C CD1 . ILE A 1 4   ? 9.124   -12.571 27.403  1.00   40.33  ? 4    ILE A CD1 1 
ATOM   17   N N   . LYS A 1 5   ? 5.038   -14.389 26.495  1.00   35.84  ? 5    LYS A N   1 
ATOM   18   C CA  . LYS A 1 5   ? 4.814   -15.755 26.058  1.00   34.73  ? 5    LYS A CA  1 
ATOM   19   C C   . LYS A 1 5   ? 5.809   -16.142 24.968  1.00   33.94  ? 5    LYS A C   1 
ATOM   20   O O   . LYS A 1 5   ? 5.993   -15.403 23.991  1.00   33.10  ? 5    LYS A O   1 
ATOM   21   C CB  . LYS A 1 5   ? 3.375   -15.927 25.577  1.00   35.08  ? 5    LYS A CB  1 
ATOM   22   C CG  . LYS A 1 5   ? 2.450   -16.461 26.646  1.00   36.80  ? 5    LYS A CG  1 
ATOM   23   C CD  . LYS A 1 5   ? 2.978   -17.805 27.165  1.00   38.52  ? 5    LYS A CD  1 
ATOM   24   C CE  . LYS A 1 5   ? 2.027   -18.463 28.137  1.00   40.54  ? 5    LYS A CE  1 
ATOM   25   N NZ  . LYS A 1 5   ? 2.432   -19.887 28.386  1.00   42.55  ? 5    LYS A NZ  1 
ATOM   26   N N   . ILE A 1 6   ? 6.463   -17.286 25.161  1.00   32.81  ? 6    ILE A N   1 
ATOM   27   C CA  . ILE A 1 6   ? 7.483   -17.775 24.243  1.00   32.58  ? 6    ILE A CA  1 
ATOM   28   C C   . ILE A 1 6   ? 7.037   -19.084 23.606  1.00   32.18  ? 6    ILE A C   1 
ATOM   29   O O   . ILE A 1 6   ? 6.726   -20.043 24.310  1.00   31.33  ? 6    ILE A O   1 
ATOM   30   C CB  . ILE A 1 6   ? 8.839   -18.022 24.938  1.00   32.88  ? 6    ILE A CB  1 
ATOM   31   C CG1 . ILE A 1 6   ? 9.355   -16.747 25.620  1.00   34.41  ? 6    ILE A CG1 1 
ATOM   32   C CG2 . ILE A 1 6   ? 9.868   -18.524 23.923  1.00   31.25  ? 6    ILE A CG2 1 
ATOM   33   C CD1 . ILE A 1 6   ? 10.509  -17.004 26.562  1.00   35.36  ? 6    ILE A CD1 1 
ATOM   34   N N   . PHE A 1 7   ? 7.030   -19.104 22.274  1.00   32.09  ? 7    PHE A N   1 
ATOM   35   C CA  . PHE A 1 7   ? 6.714   -20.291 21.486  1.00   32.48  ? 7    PHE A CA  1 
ATOM   36   C C   . PHE A 1 7   ? 7.912   -20.712 20.632  1.00   33.48  ? 7    PHE A C   1 
ATOM   37   O O   . PHE A 1 7   ? 8.739   -19.882 20.253  1.00   32.26  ? 7    PHE A O   1 
ATOM   38   C CB  . PHE A 1 7   ? 5.520   -20.019 20.565  1.00   32.15  ? 7    PHE A CB  1 
ATOM   39   C CG  . PHE A 1 7   ? 4.215   -19.811 21.290  1.00   30.83  ? 7    PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 7   ? 3.844   -18.546 21.740  1.00   30.26  ? 7    PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 7   ? 3.349   -20.875 21.498  1.00   28.83  ? 7    PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 7   ? 2.631   -18.351 22.404  1.00   30.66  ? 7    PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 7   ? 2.131   -20.696 22.151  1.00   29.32  ? 7    PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 7   ? 1.767   -19.440 22.605  1.00   29.73  ? 7    PHE A CZ  1 
ATOM   45   N N   . SER A 1 8   ? 7.983   -22.007 20.335  1.00   35.45  ? 8    SER A N   1 
ATOM   46   C CA  . SER A 1 8   ? 9.032   -22.579 19.501  1.00   38.30  ? 8    SER A CA  1 
ATOM   47   C C   . SER A 1 8   ? 8.492   -23.084 18.167  1.00   40.04  ? 8    SER A C   1 
ATOM   48   O O   . SER A 1 8   ? 7.330   -23.490 18.078  1.00   40.16  ? 8    SER A O   1 
ATOM   49   C CB  . SER A 1 8   ? 9.677   -23.758 20.224  1.00   38.33  ? 8    SER A CB  1 
ATOM   50   O OG  . SER A 1 8   ? 10.573  -24.439 19.358  1.00   40.38  ? 8    SER A OG  1 
ATOM   51   N N   . GLY A 1 9   ? 9.359   -23.083 17.146  1.00   42.57  ? 9    GLY A N   1 
ATOM   52   C CA  . GLY A 1 9   ? 9.115   -23.785 15.865  1.00   44.79  ? 9    GLY A CA  1 
ATOM   53   C C   . GLY A 1 9   ? 9.031   -25.306 16.007  1.00   46.85  ? 9    GLY A C   1 
ATOM   54   O O   . GLY A 1 9   ? 9.022   -25.839 17.125  1.00   47.42  ? 9    GLY A O   1 
ATOM   55   N N   . SER A 1 10  ? 8.993   -26.011 14.874  0.88   48.42  ? 10   SER A N   1 
ATOM   56   C CA  . SER A 1 10  ? 8.594   -27.435 14.826  0.88   49.77  ? 10   SER A CA  1 
ATOM   57   C C   . SER A 1 10  ? 9.115   -28.516 15.768  0.88   50.47  ? 10   SER A C   1 
ATOM   58   O O   . SER A 1 10  ? 8.344   -29.149 16.500  0.88   50.95  ? 10   SER A O   1 
ATOM   59   C CB  . SER A 1 10  ? 8.814   -28.032 13.423  0.88   49.93  ? 10   SER A CB  1 
ATOM   60   O OG  . SER A 1 10  ? 7.677   -28.760 12.980  0.88   50.57  ? 10   SER A OG  1 
ATOM   61   N N   . SER A 1 11  ? 10.428  -28.750 15.697  1.00   51.17  ? 11   SER A N   1 
ATOM   62   C CA  . SER A 1 11  ? 10.989  -29.925 16.339  1.00   51.82  ? 11   SER A CA  1 
ATOM   63   C C   . SER A 1 11  ? 12.261  -29.549 17.074  1.00   51.85  ? 11   SER A C   1 
ATOM   64   O O   . SER A 1 11  ? 12.559  -30.124 18.125  1.00   52.36  ? 11   SER A O   1 
ATOM   65   C CB  . SER A 1 11  ? 11.234  -31.105 15.393  1.00   51.92  ? 11   SER A CB  1 
ATOM   66   O OG  . SER A 1 11  ? 11.534  -32.285 16.120  1.00   52.94  ? 11   SER A OG  1 
ATOM   67   N N   . HIS A 1 12  ? 13.003  -28.590 16.519  0.62   51.65  ? 12   HIS A N   1 
ATOM   68   C CA  . HIS A 1 12  ? 14.163  -28.017 17.198  0.62   51.44  ? 12   HIS A CA  1 
ATOM   69   C C   . HIS A 1 12  ? 13.697  -27.184 18.391  0.62   50.91  ? 12   HIS A C   1 
ATOM   70   O O   . HIS A 1 12  ? 13.376  -25.998 18.264  0.62   50.98  ? 12   HIS A O   1 
ATOM   71   C CB  . HIS A 1 12  ? 15.018  -27.179 16.235  0.62   51.65  ? 12   HIS A CB  1 
ATOM   72   C CG  . HIS A 1 12  ? 15.781  -26.076 16.906  0.62   52.61  ? 12   HIS A CG  1 
ATOM   73   N ND1 . HIS A 1 12  ? 15.420  -24.749 16.793  0.62   53.52  ? 12   HIS A ND1 1 
ATOM   74   C CD2 . HIS A 1 12  ? 16.865  -26.104 17.721  0.62   53.67  ? 12   HIS A CD2 1 
ATOM   75   C CE1 . HIS A 1 12  ? 16.260  -24.006 17.491  0.62   53.87  ? 12   HIS A CE1 1 
ATOM   76   N NE2 . HIS A 1 12  ? 17.147  -24.804 18.063  0.62   53.88  ? 12   HIS A NE2 1 
ATOM   77   N N   . GLN A 1 13  ? 13.647  -27.827 19.551  1.00   50.03  ? 13   GLN A N   1 
ATOM   78   C CA  . GLN A 1 13  ? 13.227  -27.155 20.766  1.00   49.22  ? 13   GLN A CA  1 
ATOM   79   C C   . GLN A 1 13  ? 14.378  -26.775 21.671  1.00   47.79  ? 13   GLN A C   1 
ATOM   80   O O   . GLN A 1 13  ? 14.193  -25.964 22.577  1.00   47.94  ? 13   GLN A O   1 
ATOM   81   C CB  . GLN A 1 13  ? 12.229  -28.008 21.550  1.00   49.81  ? 13   GLN A CB  1 
ATOM   82   C CG  . GLN A 1 13  ? 10.810  -27.475 21.505  1.00   51.72  ? 13   GLN A CG  1 
ATOM   83   C CD  . GLN A 1 13  ? 9.868   -28.227 22.428  1.00   54.36  ? 13   GLN A CD  1 
ATOM   84   O OE1 . GLN A 1 13  ? 8.726   -28.500 22.065  1.00   55.36  ? 13   GLN A OE1 1 
ATOM   85   N NE2 . GLN A 1 13  ? 10.342  -28.565 23.631  1.00   55.27  ? 13   GLN A NE2 1 
ATOM   86   N N   . ASP A 1 14  ? 15.558  -27.345 21.432  1.00   46.05  ? 14   ASP A N   1 
ATOM   87   C CA  . ASP A 1 14  ? 16.662  -27.178 22.374  1.00   44.58  ? 14   ASP A CA  1 
ATOM   88   C C   . ASP A 1 14  ? 16.957  -25.713 22.673  1.00   42.65  ? 14   ASP A C   1 
ATOM   89   O O   . ASP A 1 14  ? 16.954  -25.318 23.834  1.00   42.29  ? 14   ASP A O   1 
ATOM   90   C CB  . ASP A 1 14  ? 17.928  -27.930 21.941  1.00   45.23  ? 14   ASP A CB  1 
ATOM   91   C CG  . ASP A 1 14  ? 18.946  -28.060 23.073  1.00   46.97  ? 14   ASP A CG  1 
ATOM   92   O OD1 . ASP A 1 14  ? 20.156  -28.161 22.786  1.00   49.89  ? 14   ASP A OD1 1 
ATOM   93   O OD2 . ASP A 1 14  ? 18.542  -28.058 24.259  1.00   50.19  ? 14   ASP A OD2 1 
ATOM   94   N N   . LEU A 1 15  ? 17.186  -24.909 21.635  1.00   40.73  ? 15   LEU A N   1 
ATOM   95   C CA  . LEU A 1 15  ? 17.455  -23.479 21.819  1.00   38.94  ? 15   LEU A CA  1 
ATOM   96   C C   . LEU A 1 15  ? 16.277  -22.777 22.478  1.00   38.13  ? 15   LEU A C   1 
ATOM   97   O O   . LEU A 1 15  ? 16.461  -22.029 23.441  1.00   37.00  ? 15   LEU A O   1 
ATOM   98   C CB  . LEU A 1 15  ? 17.761  -22.792 20.491  1.00   38.87  ? 15   LEU A CB  1 
ATOM   99   C CG  . LEU A 1 15  ? 18.871  -21.738 20.385  1.00   39.49  ? 15   LEU A CG  1 
ATOM   100  C CD1 . LEU A 1 15  ? 18.569  -20.813 19.203  1.00   38.22  ? 15   LEU A CD1 1 
ATOM   101  C CD2 . LEU A 1 15  ? 19.101  -20.923 21.662  1.00   37.56  ? 15   LEU A CD2 1 
ATOM   102  N N   . SER A 1 16  ? 15.075  -23.033 21.963  1.00   37.02  ? 16   SER A N   1 
ATOM   103  C CA  . SER A 1 16  ? 13.857  -22.435 22.501  1.00   37.40  ? 16   SER A CA  1 
ATOM   104  C C   . SER A 1 16  ? 13.666  -22.754 23.985  1.00   36.70  ? 16   SER A C   1 
ATOM   105  O O   . SER A 1 16  ? 13.283  -21.882 24.766  1.00   35.77  ? 16   SER A O   1 
ATOM   106  C CB  . SER A 1 16  ? 12.642  -22.905 21.713  1.00   36.95  ? 16   SER A CB  1 
ATOM   107  O OG  . SER A 1 16  ? 12.686  -22.382 20.405  1.00   41.30  ? 16   SER A OG  1 
ATOM   108  N N   . GLN A 1 17  ? 13.949  -24.003 24.353  1.00   36.75  ? 17   GLN A N   1 
ATOM   109  C CA  . GLN A 1 17  ? 13.793  -24.466 25.730  1.00   37.54  ? 17   GLN A CA  1 
ATOM   110  C C   . GLN A 1 17  ? 14.864  -23.848 26.620  1.00   36.89  ? 17   GLN A C   1 
ATOM   111  O O   . GLN A 1 17  ? 14.575  -23.455 27.741  1.00   37.27  ? 17   GLN A O   1 
ATOM   112  C CB  . GLN A 1 17  ? 13.801  -26.008 25.813  1.00   37.95  ? 17   GLN A CB  1 
ATOM   113  C CG  . GLN A 1 17  ? 13.484  -26.589 27.211  1.00   40.68  ? 17   GLN A CG  1 
ATOM   114  C CD  . GLN A 1 17  ? 12.104  -26.195 27.738  1.00   43.13  ? 17   GLN A CD  1 
ATOM   115  O OE1 . GLN A 1 17  ? 11.080  -26.492 27.118  1.00   44.56  ? 17   GLN A OE1 1 
ATOM   116  N NE2 . GLN A 1 17  ? 12.074  -25.539 28.903  1.00   44.85  ? 17   GLN A NE2 1 
ATOM   117  N N   . LYS A 1 18  ? 16.087  -23.734 26.112  1.00   36.52  ? 18   LYS A N   1 
ATOM   118  C CA  . LYS A 1 18  ? 17.136  -23.014 26.829  1.00   36.21  ? 18   LYS A CA  1 
ATOM   119  C C   . LYS A 1 18  ? 16.736  -21.560 27.105  1.00   35.45  ? 18   LYS A C   1 
ATOM   120  O O   . LYS A 1 18  ? 16.954  -21.052 28.211  1.00   34.91  ? 18   LYS A O   1 
ATOM   121  C CB  . LYS A 1 18  ? 18.463  -23.059 26.069  1.00   36.56  ? 18   LYS A CB  1 
ATOM   122  C CG  . LYS A 1 18  ? 19.215  -24.374 26.203  1.00   38.18  ? 18   LYS A CG  1 
ATOM   123  C CD  . LYS A 1 18  ? 20.506  -24.329 25.350  1.00   40.14  ? 18   LYS A CD  1 
ATOM   124  C CE  . LYS A 1 18  ? 21.478  -25.422 25.766  1.00   43.79  ? 18   LYS A CE  1 
ATOM   125  N NZ  . LYS A 1 18  ? 20.841  -26.795 25.705  1.00   45.28  ? 18   LYS A NZ  1 
ATOM   126  N N   . ILE A 1 19  ? 16.143  -20.905 26.107  1.00   34.40  ? 19   ILE A N   1 
ATOM   127  C CA  . ILE A 1 19  ? 15.708  -19.509 26.242  1.00   33.71  ? 19   ILE A CA  1 
ATOM   128  C C   . ILE A 1 19  ? 14.616  -19.392 27.306  1.00   33.80  ? 19   ILE A C   1 
ATOM   129  O O   . ILE A 1 19  ? 14.719  -18.569 28.213  1.00   33.59  ? 19   ILE A O   1 
ATOM   130  C CB  . ILE A 1 19  ? 15.243  -18.909 24.886  1.00   33.34  ? 19   ILE A CB  1 
ATOM   131  C CG1 . ILE A 1 19  ? 16.450  -18.723 23.954  1.00   33.48  ? 19   ILE A CG1 1 
ATOM   132  C CG2 . ILE A 1 19  ? 14.559  -17.551 25.094  1.00   33.07  ? 19   ILE A CG2 1 
ATOM   133  C CD1 . ILE A 1 19  ? 16.094  -18.446 22.487  1.00   30.88  ? 19   ILE A CD1 1 
ATOM   134  N N   . ALA A 1 20  ? 13.590  -20.236 27.199  1.00   34.08  ? 20   ALA A N   1 
ATOM   135  C CA  . ALA A 1 20  ? 12.478  -20.230 28.141  1.00   34.91  ? 20   ALA A CA  1 
ATOM   136  C C   . ALA A 1 20  ? 12.928  -20.477 29.596  1.00   35.45  ? 20   ALA A C   1 
ATOM   137  O O   . ALA A 1 20  ? 12.469  -19.780 30.507  1.00   35.65  ? 20   ALA A O   1 
ATOM   138  C CB  . ALA A 1 20  ? 11.401  -21.228 27.709  1.00   34.61  ? 20   ALA A CB  1 
ATOM   139  N N   . ASP A 1 21  ? 13.834  -21.441 29.786  1.00   36.32  ? 21   ASP A N   1 
ATOM   140  C CA  . ASP A 1 21  ? 14.441  -21.761 31.098  1.00   36.82  ? 21   ASP A CA  1 
ATOM   141  C C   . ASP A 1 21  ? 15.099  -20.553 31.763  1.00   36.60  ? 21   ASP A C   1 
ATOM   142  O O   . ASP A 1 21  ? 14.898  -20.294 32.961  1.00   36.61  ? 21   ASP A O   1 
ATOM   143  C CB  . ASP A 1 21  ? 15.529  -22.831 30.940  1.00   37.43  ? 21   ASP A CB  1 
ATOM   144  C CG  . ASP A 1 21  ? 14.974  -24.208 30.699  1.00   39.40  ? 21   ASP A CG  1 
ATOM   145  O OD1 . ASP A 1 21  ? 13.744  -24.382 30.791  1.00   41.67  ? 21   ASP A OD1 1 
ATOM   146  O OD2 . ASP A 1 21  ? 15.777  -25.128 30.411  1.00   42.66  ? 21   ASP A OD2 1 
ATOM   147  N N   . ARG A 1 22  ? 15.908  -19.843 30.982  0.94   35.95  ? 22   ARG A N   1 
ATOM   148  C CA  . ARG A 1 22  ? 16.614  -18.655 31.446  0.94   36.27  ? 22   ARG A CA  1 
ATOM   149  C C   . ARG A 1 22  ? 15.675  -17.529 31.839  0.94   36.00  ? 22   ARG A C   1 
ATOM   150  O O   . ARG A 1 22  ? 16.023  -16.679 32.675  0.94   36.48  ? 22   ARG A O   1 
ATOM   151  C CB  . ARG A 1 22  ? 17.589  -18.157 30.377  0.94   36.27  ? 22   ARG A CB  1 
ATOM   152  C CG  . ARG A 1 22  ? 18.777  -19.073 30.172  0.94   37.43  ? 22   ARG A CG  1 
ATOM   153  C CD  . ARG A 1 22  ? 19.796  -18.435 29.254  0.94   37.92  ? 22   ARG A CD  1 
ATOM   154  N NE  . ARG A 1 22  ? 20.889  -19.349 28.923  0.94   40.79  ? 22   ARG A NE  1 
ATOM   155  C CZ  . ARG A 1 22  ? 21.978  -19.535 29.673  0.94   43.01  ? 22   ARG A CZ  1 
ATOM   156  N NH1 . ARG A 1 22  ? 22.137  -18.877 30.820  0.94   44.67  ? 22   ARG A NH1 1 
ATOM   157  N NH2 . ARG A 1 22  ? 22.914  -20.388 29.281  0.94   42.86  ? 22   ARG A NH2 1 
ATOM   158  N N   . LEU A 1 23  ? 14.493  -17.521 31.227  1.00   35.33  ? 23   LEU A N   1 
ATOM   159  C CA  . LEU A 1 23  ? 13.493  -16.496 31.491  1.00   34.41  ? 23   LEU A CA  1 
ATOM   160  C C   . LEU A 1 23  ? 12.492  -16.901 32.583  1.00   33.73  ? 23   LEU A C   1 
ATOM   161  O O   . LEU A 1 23  ? 11.624  -16.109 32.953  1.00   33.42  ? 23   LEU A O   1 
ATOM   162  C CB  . LEU A 1 23  ? 12.768  -16.131 30.190  1.00   34.70  ? 23   LEU A CB  1 
ATOM   163  C CG  . LEU A 1 23  ? 13.585  -15.363 29.131  1.00   35.39  ? 23   LEU A CG  1 
ATOM   164  C CD1 . LEU A 1 23  ? 12.898  -15.361 27.797  1.00   37.22  ? 23   LEU A CD1 1 
ATOM   165  C CD2 . LEU A 1 23  ? 13.833  -13.942 29.575  1.00   36.42  ? 23   LEU A CD2 1 
ATOM   166  N N   . GLY A 1 24  ? 12.622  -18.128 33.090  1.00   32.93  ? 24   GLY A N   1 
ATOM   167  C CA  . GLY A 1 24  ? 11.721  -18.659 34.124  1.00   31.68  ? 24   GLY A CA  1 
ATOM   168  C C   . GLY A 1 24  ? 10.355  -19.031 33.587  1.00   31.00  ? 24   GLY A C   1 
ATOM   169  O O   . GLY A 1 24  ? 9.348   -18.936 34.296  1.00   30.54  ? 24   GLY A O   1 
ATOM   170  N N   . LEU A 1 25  ? 10.317  -19.458 32.326  1.00   29.96  ? 25   LEU A N   1 
ATOM   171  C CA  . LEU A 1 25  ? 9.048   -19.688 31.633  1.00   29.18  ? 25   LEU A CA  1 
ATOM   172  C C   . LEU A 1 25  ? 9.028   -21.068 30.999  1.00   28.16  ? 25   LEU A C   1 
ATOM   173  O O   . LEU A 1 25  ? 10.080  -21.602 30.668  1.00   28.19  ? 25   LEU A O   1 
ATOM   174  C CB  . LEU A 1 25  ? 8.839   -18.634 30.535  1.00   29.49  ? 25   LEU A CB  1 
ATOM   175  C CG  . LEU A 1 25  ? 8.881   -17.143 30.872  1.00   29.02  ? 25   LEU A CG  1 
ATOM   176  C CD1 . LEU A 1 25  ? 8.759   -16.346 29.581  1.00   30.25  ? 25   LEU A CD1 1 
ATOM   177  C CD2 . LEU A 1 25  ? 7.758   -16.757 31.816  1.00   29.64  ? 25   LEU A CD2 1 
ATOM   178  N N   . GLU A 1 26  ? 7.838   -21.646 30.884  0.74   27.41  ? 26   GLU A N   1 
ATOM   179  C CA  . GLU A 1 26  ? 7.612   -22.824 30.043  0.74   27.32  ? 26   GLU A CA  1 
ATOM   180  C C   . GLU A 1 26  ? 7.240   -22.335 28.648  0.74   26.96  ? 26   GLU A C   1 
ATOM   181  O O   . GLU A 1 26  ? 6.576   -21.296 28.511  0.74   24.95  ? 26   GLU A O   1 
ATOM   182  C CB  . GLU A 1 26  ? 6.456   -23.664 30.579  0.74   27.42  ? 26   GLU A CB  1 
ATOM   183  C CG  . GLU A 1 26  ? 6.737   -24.374 31.916  0.74   30.95  ? 26   GLU A CG  1 
ATOM   184  C CD  . GLU A 1 26  ? 5.520   -25.119 32.465  0.74   36.13  ? 26   GLU A CD  1 
ATOM   185  O OE1 . GLU A 1 26  ? 4.446   -25.142 31.801  0.74   36.17  ? 26   GLU A OE1 1 
ATOM   186  O OE2 . GLU A 1 26  ? 5.647   -25.693 33.578  0.74   39.86  ? 26   GLU A OE2 1 
ATOM   187  N N   . LEU A 1 27  ? 7.661   -23.080 27.623  1.00   27.41  ? 27   LEU A N   1 
ATOM   188  C CA  . LEU A 1 27  ? 7.193   -22.825 26.243  1.00   28.07  ? 27   LEU A CA  1 
ATOM   189  C C   . LEU A 1 27  ? 5.673   -22.925 26.133  1.00   28.51  ? 27   LEU A C   1 
ATOM   190  O O   . LEU A 1 27  ? 5.065   -23.837 26.695  1.00   27.88  ? 27   LEU A O   1 
ATOM   191  C CB  . LEU A 1 27  ? 7.844   -23.788 25.245  1.00   27.95  ? 27   LEU A CB  1 
ATOM   192  C CG  . LEU A 1 27  ? 9.362   -23.650 25.008  1.00   28.46  ? 27   LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 27  ? 9.885   -24.797 24.154  1.00   27.70  ? 27   LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 27  ? 9.752   -22.310 24.392  1.00   28.05  ? 27   LEU A CD2 1 
ATOM   195  N N   . GLY A 1 28  ? 5.067   -21.989 25.399  1.00   29.28  ? 28   GLY A N   1 
ATOM   196  C CA  . GLY A 1 28  ? 3.630   -22.017 25.135  1.00   30.06  ? 28   GLY A CA  1 
ATOM   197  C C   . GLY A 1 28  ? 3.151   -23.280 24.429  1.00   31.00  ? 28   GLY A C   1 
ATOM   198  O O   . GLY A 1 28  ? 3.884   -23.855 23.608  1.00   31.20  ? 28   GLY A O   1 
ATOM   199  N N   . LYS A 1 29  ? 1.928   -23.711 24.749  0.61   31.18  ? 29   LYS A N   1 
ATOM   200  C CA  . LYS A 1 29  ? 1.333   -24.901 24.143  0.61   32.57  ? 29   LYS A CA  1 
ATOM   201  C C   . LYS A 1 29  ? 0.986   -24.641 22.674  0.61   33.79  ? 29   LYS A C   1 
ATOM   202  O O   . LYS A 1 29  ? 0.231   -23.719 22.357  0.61   32.12  ? 29   LYS A O   1 
ATOM   203  C CB  . LYS A 1 29  ? 0.052   -25.313 24.883  0.61   32.40  ? 29   LYS A CB  1 
ATOM   204  C CG  . LYS A 1 29  ? 0.244   -25.801 26.316  0.61   33.04  ? 29   LYS A CG  1 
ATOM   205  C CD  . LYS A 1 29  ? -1.093  -26.158 26.986  0.61   34.90  ? 29   LYS A CD  1 
ATOM   206  C CE  . LYS A 1 29  ? -1.862  -24.932 27.471  0.61   35.40  ? 29   LYS A CE  1 
ATOM   207  N NZ  . LYS A 1 29  ? -1.249  -24.309 28.687  0.61   36.84  ? 29   LYS A NZ  1 
ATOM   208  N N   . VAL A 1 30  ? 1.561   -25.441 21.786  1.00   36.10  ? 30   VAL A N   1 
ATOM   209  C CA  . VAL A 1 30  ? 1.191   -25.399 20.368  1.00   39.61  ? 30   VAL A CA  1 
ATOM   210  C C   . VAL A 1 30  ? 1.266   -26.790 19.743  1.00   42.03  ? 30   VAL A C   1 
ATOM   211  O O   . VAL A 1 30  ? 2.244   -27.521 19.943  1.00   42.22  ? 30   VAL A O   1 
ATOM   212  C CB  . VAL A 1 30  ? 2.005   -24.349 19.553  1.00   39.48  ? 30   VAL A CB  1 
ATOM   213  C CG1 . VAL A 1 30  ? 3.503   -24.691 19.491  1.00   39.69  ? 30   VAL A CG1 1 
ATOM   214  C CG2 . VAL A 1 30  ? 1.417   -24.182 18.138  1.00   40.96  ? 30   VAL A CG2 1 
ATOM   215  N N   . VAL A 1 31  ? 0.209   -27.155 19.022  1.00   44.86  ? 31   VAL A N   1 
ATOM   216  C CA  . VAL A 1 31  ? 0.186   -28.386 18.233  1.00   47.94  ? 31   VAL A CA  1 
ATOM   217  C C   . VAL A 1 31  ? 0.681   -28.058 16.831  1.00   49.59  ? 31   VAL A C   1 
ATOM   218  O O   . VAL A 1 31  ? -0.064  -27.471 16.042  1.00   50.26  ? 31   VAL A O   1 
ATOM   219  C CB  . VAL A 1 31  ? -1.242  -28.991 18.144  1.00   47.83  ? 31   VAL A CB  1 
ATOM   220  C CG1 . VAL A 1 31  ? -1.195  -30.385 17.505  1.00   48.87  ? 31   VAL A CG1 1 
ATOM   221  C CG2 . VAL A 1 31  ? -1.896  -29.057 19.525  1.00   48.13  ? 31   VAL A CG2 1 
ATOM   222  N N   . THR A 1 32  ? 1.943   -28.407 16.550  1.00   51.67  ? 32   THR A N   1 
ATOM   223  C CA  . THR A 1 32  ? 2.586   -28.161 15.254  1.00   53.02  ? 32   THR A CA  1 
ATOM   224  C C   . THR A 1 32  ? 2.977   -29.472 14.581  1.00   54.12  ? 32   THR A C   1 
ATOM   225  O O   . THR A 1 32  ? 3.661   -30.304 15.190  1.00   54.62  ? 32   THR A O   1 
ATOM   226  C CB  . THR A 1 32  ? 3.872   -27.309 15.390  1.00   74.35  ? 32   THR A CB  1 
ATOM   227  O OG1 . THR A 1 32  ? 4.742   -27.896 16.366  1.00   73.74  ? 32   THR A OG1 1 
ATOM   228  C CG2 . THR A 1 32  ? 3.549   -25.881 15.792  1.00   73.40  ? 32   THR A CG2 1 
ATOM   229  N N   . LYS A 1 33  ? 2.561   -29.645 13.325  0.41   54.95  ? 33   LYS A N   1 
ATOM   230  C CA  . LYS A 1 33  ? 2.837   -30.874 12.573  0.41   55.84  ? 33   LYS A CA  1 
ATOM   231  C C   . LYS A 1 33  ? 2.897   -30.653 11.055  0.41   56.47  ? 33   LYS A C   1 
ATOM   232  O O   . LYS A 1 33  ? 3.008   -29.516 10.583  0.41   56.48  ? 33   LYS A O   1 
ATOM   233  C CB  . LYS A 1 33  ? 1.791   -31.944 12.909  0.41   55.80  ? 33   LYS A CB  1 
ATOM   234  C CG  . LYS A 1 33  ? 0.359   -31.470 12.754  0.41   55.76  ? 33   LYS A CG  1 
ATOM   235  C CD  . LYS A 1 33  ? -0.612  -32.629 12.858  0.41   55.74  ? 33   LYS A CD  1 
ATOM   236  C CE  . LYS A 1 33  ? -2.030  -32.132 13.056  0.41   55.92  ? 33   LYS A CE  1 
ATOM   237  N NZ  . LYS A 1 33  ? -2.172  -31.399 14.343  0.41   56.47  ? 33   LYS A NZ  1 
ATOM   238  N N   . LYS A 1 34  ? 2.835   -31.755 10.305  1.00   57.28  ? 34   LYS A N   1 
ATOM   239  C CA  . LYS A 1 34  ? 2.803   -31.733 8.844   1.00   57.94  ? 34   LYS A CA  1 
ATOM   240  C C   . LYS A 1 34  ? 1.816   -32.767 8.304   1.00   58.15  ? 34   LYS A C   1 
ATOM   241  O O   . LYS A 1 34  ? 1.863   -33.943 8.690   1.00   58.03  ? 34   LYS A O   1 
ATOM   242  C CB  . LYS A 1 34  ? 4.191   -32.019 8.257   1.00   58.20  ? 34   LYS A CB  1 
ATOM   243  C CG  . LYS A 1 34  ? 5.184   -30.858 8.322   1.00   59.22  ? 34   LYS A CG  1 
ATOM   244  C CD  . LYS A 1 34  ? 5.981   -30.718 7.016   1.00   60.08  ? 34   LYS A CD  1 
ATOM   245  C CE  . LYS A 1 34  ? 6.945   -31.880 6.786   1.00   60.74  ? 34   LYS A CE  1 
ATOM   246  N NZ  . LYS A 1 34  ? 7.367   -31.934 5.351   1.00   61.63  ? 34   LYS A NZ  1 
ATOM   247  N N   . PHE A 1 35  ? 0.928   -32.330 7.410   1.00   58.49  ? 35   PHE A N   1 
ATOM   248  C CA  . PHE A 1 35  ? 0.035   -33.251 6.707   1.00   58.87  ? 35   PHE A CA  1 
ATOM   249  C C   . PHE A 1 35  ? 0.831   -34.214 5.835   1.00   58.74  ? 35   PHE A C   1 
ATOM   250  O O   . PHE A 1 35  ? 1.958   -33.914 5.418   1.00   58.78  ? 35   PHE A O   1 
ATOM   251  C CB  . PHE A 1 35  ? -0.976  -32.512 5.817   1.00   59.03  ? 35   PHE A CB  1 
ATOM   252  C CG  . PHE A 1 35  ? -1.975  -31.674 6.567   1.00   60.25  ? 35   PHE A CG  1 
ATOM   253  C CD1 . PHE A 1 35  ? -2.603  -30.607 5.928   1.00   61.54  ? 35   PHE A CD1 1 
ATOM   254  C CD2 . PHE A 1 35  ? -2.296  -31.942 7.899   1.00   61.22  ? 35   PHE A CD2 1 
ATOM   255  C CE1 . PHE A 1 35  ? -3.531  -29.817 6.596   1.00   61.72  ? 35   PHE A CE1 1 
ATOM   256  C CE2 . PHE A 1 35  ? -3.218  -31.158 8.575   1.00   61.81  ? 35   PHE A CE2 1 
ATOM   257  C CZ  . PHE A 1 35  ? -3.838  -30.090 7.921   1.00   62.29  ? 35   PHE A CZ  1 
ATOM   258  N N   . SER A 1 36  ? 0.227   -35.368 5.559   0.50   58.57  ? 36   SER A N   1 
ATOM   259  C CA  . SER A 1 36  ? 0.772   -36.333 4.610   0.50   58.37  ? 36   SER A CA  1 
ATOM   260  C C   . SER A 1 36  ? 1.172   -35.655 3.298   0.50   58.20  ? 36   SER A C   1 
ATOM   261  O O   . SER A 1 36  ? 2.101   -36.098 2.620   0.50   58.30  ? 36   SER A O   1 
ATOM   262  C CB  . SER A 1 36  ? -0.249  -37.440 4.345   0.50   58.33  ? 36   SER A CB  1 
ATOM   263  O OG  . SER A 1 36  ? 0.285   -38.416 3.473   0.50   58.03  ? 36   SER A OG  1 
ATOM   264  N N   . ASN A 1 37  ? 0.469   -34.576 2.957   0.82   57.99  ? 37   ASN A N   1 
ATOM   265  C CA  . ASN A 1 37  ? 0.787   -33.776 1.778   0.82   57.83  ? 37   ASN A CA  1 
ATOM   266  C C   . ASN A 1 37  ? 1.596   -32.506 2.088   0.82   57.36  ? 37   ASN A C   1 
ATOM   267  O O   . ASN A 1 37  ? 1.388   -31.449 1.481   0.82   57.47  ? 37   ASN A O   1 
ATOM   268  C CB  . ASN A 1 37  ? -0.483  -33.471 0.971   0.82   58.09  ? 37   ASN A CB  1 
ATOM   269  C CG  . ASN A 1 37  ? -1.419  -32.490 1.666   0.82   59.25  ? 37   ASN A CG  1 
ATOM   270  O OD1 . ASN A 1 37  ? -1.511  -32.447 2.894   0.82   61.20  ? 37   ASN A OD1 1 
ATOM   271  N ND2 . ASN A 1 37  ? -2.127  -31.695 0.867   0.82   60.26  ? 37   ASN A ND2 1 
ATOM   272  N N   . GLN A 1 38  ? 2.516   -32.633 3.045   1.00   56.72  ? 38   GLN A N   1 
ATOM   273  C CA  . GLN A 1 38  ? 3.553   -31.621 3.355   1.00   56.28  ? 38   GLN A CA  1 
ATOM   274  C C   . GLN A 1 38  ? 3.093   -30.219 3.829   1.00   55.34  ? 38   GLN A C   1 
ATOM   275  O O   . GLN A 1 38  ? 3.948   -29.302 3.994   1.00   55.64  ? 38   GLN A O   1 
ATOM   276  C CB  . GLN A 1 38  ? 4.446   -31.341 2.129   1.00   56.38  ? 38   GLN A CB  1 
ATOM   277  C CG  . GLN A 1 38  ? 4.640   -32.519 1.153   1.00   57.83  ? 38   GLN A CG  1 
ATOM   278  C CD  . GLN A 1 38  ? 5.469   -33.664 1.723   1.00   59.70  ? 38   GLN A CD  1 
ATOM   279  O OE1 . GLN A 1 38  ? 5.049   -34.357 2.656   1.00   60.92  ? 38   GLN A OE1 1 
ATOM   280  N NE2 . GLN A 1 38  ? 6.645   -33.882 1.141   1.00   62.94  ? 38   GLN A NE2 1 
ATOM   281  N N   . GLU A 1 39  ? 1.774   -30.049 4.046   1.00   54.19  ? 39   GLU A N   1 
ATOM   282  C CA  . GLU A 1 39  ? 1.226   -28.749 4.473   1.00   53.03  ? 39   GLU A CA  1 
ATOM   283  C C   . GLU A 1 39  ? 1.456   -28.642 5.973   1.00   52.06  ? 39   GLU A C   1 
ATOM   284  O O   . GLU A 1 39  ? 1.227   -29.603 6.712   1.00   51.40  ? 39   GLU A O   1 
ATOM   285  C CB  . GLU A 1 39  ? -0.277  -28.610 4.201   1.00   53.12  ? 39   GLU A CB  1 
ATOM   286  C CG  . GLU A 1 39  ? -0.679  -28.585 2.750   1.00   54.37  ? 39   GLU A CG  1 
ATOM   287  C CD  . GLU A 1 39  ? -2.018  -27.896 2.513   1.00   55.15  ? 39   GLU A CD  1 
ATOM   288  O OE1 . GLU A 1 39  ? -2.749  -27.628 3.492   1.00   55.87  ? 39   GLU A OE1 1 
ATOM   289  O OE2 . GLU A 1 39  ? -2.333  -27.608 1.335   1.00   56.40  ? 39   GLU A OE2 1 
ATOM   290  N N   . THR A 1 40  ? 1.898   -27.465 6.412   1.00   50.95  ? 40   THR A N   1 
ATOM   291  C CA  . THR A 1 40  ? 2.144   -27.206 7.829   1.00   49.97  ? 40   THR A CA  1 
ATOM   292  C C   . THR A 1 40  ? 0.849   -26.872 8.556   1.00   49.28  ? 40   THR A C   1 
ATOM   293  O O   . THR A 1 40  ? 0.146   -25.921 8.191   1.00   48.73  ? 40   THR A O   1 
ATOM   294  C CB  . THR A 1 40  ? 3.118   -26.029 8.037   1.00   50.16  ? 40   THR A CB  1 
ATOM   295  O OG1 . THR A 1 40  ? 4.262   -26.183 7.187   1.00   50.65  ? 40   THR A OG1 1 
ATOM   296  C CG2 . THR A 1 40  ? 3.558   -25.941 9.501   1.00   50.32  ? 40   THR A CG2 1 
ATOM   297  N N   . CYS A 1 41  ? 0.551   -27.661 9.584   0.75   48.69  ? 41   CYS A N   1 
ATOM   298  C CA  . CYS A 1 41  ? -0.565  -27.405 10.482  0.75   48.37  ? 41   CYS A CA  1 
ATOM   299  C C   . CYS A 1 41  ? -0.039  -26.856 11.803  0.75   47.96  ? 41   CYS A C   1 
ATOM   300  O O   . CYS A 1 41  ? 0.923   -27.389 12.370  0.75   47.86  ? 41   CYS A O   1 
ATOM   301  C CB  . CYS A 1 41  ? -1.363  -28.690 10.727  0.75   48.59  ? 41   CYS A CB  1 
ATOM   302  S SG  . CYS A 1 41  ? -2.610  -28.573 12.039  0.75   99.04  ? 41   CYS A SG  1 
ATOM   303  N N   . VAL A 1 42  ? -0.675  -25.788 12.279  1.00   47.35  ? 42   VAL A N   1 
ATOM   304  C CA  . VAL A 1 42  ? -0.305  -25.133 13.532  1.00   47.13  ? 42   VAL A CA  1 
ATOM   305  C C   . VAL A 1 42  ? -1.566  -24.725 14.284  1.00   46.58  ? 42   VAL A C   1 
ATOM   306  O O   . VAL A 1 42  ? -2.513  -24.207 13.685  1.00   46.50  ? 42   VAL A O   1 
ATOM   307  C CB  . VAL A 1 42  ? 0.583   -23.887 13.286  1.00   47.28  ? 42   VAL A CB  1 
ATOM   308  C CG1 . VAL A 1 42  ? 0.739   -23.068 14.566  1.00   47.54  ? 42   VAL A CG1 1 
ATOM   309  C CG2 . VAL A 1 42  ? 1.955   -24.293 12.737  1.00   47.77  ? 42   VAL A CG2 1 
ATOM   310  N N   . GLU A 1 43  ? -1.578  -24.971 15.593  0.87   45.65  ? 43   GLU A N   1 
ATOM   311  C CA  . GLU A 1 43  ? -2.719  -24.621 16.425  0.87   44.85  ? 43   GLU A CA  1 
ATOM   312  C C   . GLU A 1 43  ? -2.286  -24.157 17.817  0.87   43.89  ? 43   GLU A C   1 
ATOM   313  O O   . GLU A 1 43  ? -2.022  -24.981 18.691  0.87   43.82  ? 43   GLU A O   1 
ATOM   314  C CB  . GLU A 1 43  ? -3.655  -25.821 16.556  0.87   45.33  ? 43   GLU A CB  1 
ATOM   315  C CG  . GLU A 1 43  ? -5.132  -25.461 16.551  0.87   46.58  ? 43   GLU A CG  1 
ATOM   316  C CD  . GLU A 1 43  ? -5.726  -25.515 15.156  0.87   48.89  ? 43   GLU A CD  1 
ATOM   317  O OE1 . GLU A 1 43  ? -6.734  -26.230 14.962  0.87   50.13  ? 43   GLU A OE1 1 
ATOM   318  O OE2 . GLU A 1 43  ? -5.171  -24.864 14.241  0.87   50.61  ? 43   GLU A OE2 1 
ATOM   319  N N   . ILE A 1 44  ? -2.226  -22.841 18.014  1.00   42.63  ? 44   ILE A N   1 
ATOM   320  C CA  . ILE A 1 44  ? -1.913  -22.251 19.319  1.00   41.46  ? 44   ILE A CA  1 
ATOM   321  C C   . ILE A 1 44  ? -2.847  -22.829 20.388  1.00   40.50  ? 44   ILE A C   1 
ATOM   322  O O   . ILE A 1 44  ? -4.064  -22.659 20.313  1.00   40.35  ? 44   ILE A O   1 
ATOM   323  C CB  . ILE A 1 44  ? -2.038  -20.699 19.304  1.00   41.57  ? 44   ILE A CB  1 
ATOM   324  C CG1 . ILE A 1 44  ? -1.344  -20.084 18.072  1.00   41.33  ? 44   ILE A CG1 1 
ATOM   325  C CG2 . ILE A 1 44  ? -1.516  -20.095 20.619  1.00   41.47  ? 44   ILE A CG2 1 
ATOM   326  C CD1 . ILE A 1 44  ? 0.195   -20.106 18.094  1.00   42.62  ? 44   ILE A CD1 1 
ATOM   327  N N   . GLY A 1 45  ? -2.261  -23.506 21.377  1.00   39.04  ? 45   GLY A N   1 
ATOM   328  C CA  . GLY A 1 45  ? -3.019  -24.242 22.381  1.00   37.64  ? 45   GLY A CA  1 
ATOM   329  C C   . GLY A 1 45  ? -3.423  -23.460 23.616  1.00   36.80  ? 45   GLY A C   1 
ATOM   330  O O   . GLY A 1 45  ? -3.938  -24.036 24.575  1.00   37.23  ? 45   GLY A O   1 
ATOM   331  N N   . GLU A 1 46  ? -3.197  -22.149 23.593  0.64   35.10  ? 46   GLU A N   1 
ATOM   332  C CA  . GLU A 1 46  ? -3.651  -21.266 24.661  0.64   33.48  ? 46   GLU A CA  1 
ATOM   333  C C   . GLU A 1 46  ? -3.927  -19.862 24.129  0.64   32.24  ? 46   GLU A C   1 
ATOM   334  O O   . GLU A 1 46  ? -3.458  -19.492 23.056  0.64   31.09  ? 46   GLU A O   1 
ATOM   335  C CB  . GLU A 1 46  ? -2.623  -21.205 25.788  0.64   33.68  ? 46   GLU A CB  1 
ATOM   336  C CG  . GLU A 1 46  ? -1.195  -20.950 25.310  0.64   34.61  ? 46   GLU A CG  1 
ATOM   337  C CD  . GLU A 1 46  ? -0.211  -21.005 26.444  0.64   35.42  ? 46   GLU A CD  1 
ATOM   338  O OE1 . GLU A 1 46  ? -0.262  -20.100 27.305  0.64   37.66  ? 46   GLU A OE1 1 
ATOM   339  O OE2 . GLU A 1 46  ? 0.594   -21.955 26.489  0.64   35.27  ? 46   GLU A OE2 1 
ATOM   340  N N   . SER A 1 47  ? -4.699  -19.098 24.894  1.00   31.10  ? 47   SER A N   1 
ATOM   341  C CA  . SER A 1 47  ? -4.969  -17.696 24.598  1.00   30.12  ? 47   SER A CA  1 
ATOM   342  C C   . SER A 1 47  ? -3.671  -16.897 24.603  1.00   29.25  ? 47   SER A C   1 
ATOM   343  O O   . SER A 1 47  ? -2.839  -17.064 25.496  1.00   27.82  ? 47   SER A O   1 
ATOM   344  C CB  . SER A 1 47  ? -5.928  -17.120 25.644  1.00   30.16  ? 47   SER A CB  1 
ATOM   345  O OG  . SER A 1 47  ? -6.207  -15.748 25.380  1.00   30.23  ? 47   SER A OG  1 
ATOM   346  N N   . VAL A 1 48  ? -3.486  -16.051 23.589  1.00   28.06  ? 48   VAL A N   1 
ATOM   347  C CA  . VAL A 1 48  ? -2.370  -15.110 23.595  1.00   27.01  ? 48   VAL A CA  1 
ATOM   348  C C   . VAL A 1 48  ? -2.864  -13.666 23.561  1.00   27.53  ? 48   VAL A C   1 
ATOM   349  O O   . VAL A 1 48  ? -2.096  -12.740 23.265  1.00   27.01  ? 48   VAL A O   1 
ATOM   350  C CB  . VAL A 1 48  ? -1.388  -15.381 22.425  1.00   27.89  ? 48   VAL A CB  1 
ATOM   351  C CG1 . VAL A 1 48  ? -0.682  -16.722 22.632  1.00   25.97  ? 48   VAL A CG1 1 
ATOM   352  C CG2 . VAL A 1 48  ? -2.115  -15.320 21.051  1.00   26.08  ? 48   VAL A CG2 1 
ATOM   353  N N   . ARG A 1 49  ? -4.151  -13.483 23.865  1.00   27.44  ? 49   ARG A N   1 
ATOM   354  C CA  . ARG A 1 49  ? -4.796  -12.172 23.811  1.00   28.25  ? 49   ARG A CA  1 
ATOM   355  C C   . ARG A 1 49  ? -4.129  -11.189 24.765  1.00   28.95  ? 49   ARG A C   1 
ATOM   356  O O   . ARG A 1 49  ? -3.922  -11.497 25.938  1.00   28.54  ? 49   ARG A O   1 
ATOM   357  C CB  . ARG A 1 49  ? -6.295  -12.311 24.096  1.00   28.70  ? 49   ARG A CB  1 
ATOM   358  C CG  . ARG A 1 49  ? -7.147  -11.135 23.634  1.00   29.03  ? 49   ARG A CG  1 
ATOM   359  C CD  . ARG A 1 49  ? -8.644  -11.390 23.865  1.00   30.46  ? 49   ARG A CD  1 
ATOM   360  N NE  . ARG A 1 49  ? -9.182  -12.450 23.006  1.00   29.56  ? 49   ARG A NE  1 
ATOM   361  C CZ  . ARG A 1 49  ? -9.790  -12.245 21.837  1.00   29.34  ? 49   ARG A CZ  1 
ATOM   362  N NH1 . ARG A 1 49  ? -9.982  -11.015 21.371  1.00   28.62  ? 49   ARG A NH1 1 
ATOM   363  N NH2 . ARG A 1 49  ? -10.237 -13.279 21.138  1.00   29.36  ? 49   ARG A NH2 1 
ATOM   364  N N   . GLY A 1 50  ? -3.746  -10.023 24.234  1.00   29.36  ? 50   GLY A N   1 
ATOM   365  C CA  . GLY A 1 50  ? -3.062  -8.988  25.022  1.00   28.86  ? 50   GLY A CA  1 
ATOM   366  C C   . GLY A 1 50  ? -1.668  -9.361  25.514  1.00   29.37  ? 50   GLY A C   1 
ATOM   367  O O   . GLY A 1 50  ? -1.112  -8.685  26.386  1.00   29.32  ? 50   GLY A O   1 
ATOM   368  N N   . GLU A 1 51  ? -1.090  -10.435 24.979  1.00   29.10  ? 51   GLU A N   1 
ATOM   369  C CA  . GLU A 1 51  ? 0.227   -10.877 25.453  1.00   29.37  ? 51   GLU A CA  1 
ATOM   370  C C   . GLU A 1 51  ? 1.382   -10.481 24.523  1.00   28.64  ? 51   GLU A C   1 
ATOM   371  O O   . GLU A 1 51  ? 1.177   -10.256 23.323  1.00   28.27  ? 51   GLU A O   1 
ATOM   372  C CB  . GLU A 1 51  ? 0.214   -12.383 25.744  1.00   30.41  ? 51   GLU A CB  1 
ATOM   373  C CG  . GLU A 1 51  ? -0.723  -12.764 26.909  1.00   33.14  ? 51   GLU A CG  1 
ATOM   374  C CD  . GLU A 1 51  ? -0.693  -14.241 27.252  1.00   39.88  ? 51   GLU A CD  1 
ATOM   375  O OE1 . GLU A 1 51  ? -0.370  -15.053 26.360  1.00   42.07  ? 51   GLU A OE1 1 
ATOM   376  O OE2 . GLU A 1 51  ? -1.014  -14.599 28.417  1.00   43.47  ? 51   GLU A OE2 1 
ATOM   377  N N   . ASP A 1 52  ? 2.578   -10.369 25.098  1.00   28.08  ? 52   ASP A N   1 
ATOM   378  C CA  . ASP A 1 52  ? 3.819   -10.058 24.384  1.00   27.79  ? 52   ASP A CA  1 
ATOM   379  C C   . ASP A 1 52  ? 4.450   -11.361 23.880  1.00   27.14  ? 52   ASP A C   1 
ATOM   380  O O   . ASP A 1 52  ? 5.147   -12.052 24.626  1.00   26.96  ? 52   ASP A O   1 
ATOM   381  C CB  . ASP A 1 52  ? 4.793   -9.307  25.321  1.00   27.65  ? 52   ASP A CB  1 
ATOM   382  C CG  . ASP A 1 52  ? 5.896   -8.572  24.566  1.00   29.11  ? 52   ASP A CG  1 
ATOM   383  O OD1 . ASP A 1 52  ? 5.746   -8.355  23.337  1.00   31.62  ? 52   ASP A OD1 1 
ATOM   384  O OD2 . ASP A 1 52  ? 6.924   -8.199  25.191  1.00   29.39  ? 52   ASP A OD2 1 
ATOM   385  N N   . VAL A 1 53  ? 4.198   -11.704 22.616  1.00   26.43  ? 53   VAL A N   1 
ATOM   386  C CA  . VAL A 1 53  ? 4.555   -13.037 22.099  1.00   25.52  ? 53   VAL A CA  1 
ATOM   387  C C   . VAL A 1 53  ? 5.875   -13.081 21.319  1.00   25.78  ? 53   VAL A C   1 
ATOM   388  O O   . VAL A 1 53  ? 6.084   -12.295 20.380  1.00   25.08  ? 53   VAL A O   1 
ATOM   389  C CB  . VAL A 1 53  ? 3.422   -13.616 21.216  1.00   25.71  ? 53   VAL A CB  1 
ATOM   390  C CG1 . VAL A 1 53  ? 3.801   -14.980 20.661  1.00   25.36  ? 53   VAL A CG1 1 
ATOM   391  C CG2 . VAL A 1 53  ? 2.126   -13.695 21.999  1.00   25.13  ? 53   VAL A CG2 1 
ATOM   392  N N   . TYR A 1 54  ? 6.736   -14.032 21.696  1.00   25.25  ? 54   TYR A N   1 
ATOM   393  C CA  . TYR A 1 54  ? 8.030   -14.252 21.051  1.00   25.12  ? 54   TYR A CA  1 
ATOM   394  C C   . TYR A 1 54  ? 8.071   -15.624 20.374  1.00   25.63  ? 54   TYR A C   1 
ATOM   395  O O   . TYR A 1 54  ? 7.954   -16.652 21.040  1.00   25.49  ? 54   TYR A O   1 
ATOM   396  C CB  . TYR A 1 54  ? 9.164   -14.103 22.088  1.00   25.38  ? 54   TYR A CB  1 
ATOM   397  C CG  . TYR A 1 54  ? 9.285   -12.696 22.631  1.00   24.54  ? 54   TYR A CG  1 
ATOM   398  C CD1 . TYR A 1 54  ? 8.381   -12.218 23.571  1.00   24.83  ? 54   TYR A CD1 1 
ATOM   399  C CD2 . TYR A 1 54  ? 10.267  -11.825 22.166  1.00   23.31  ? 54   TYR A CD2 1 
ATOM   400  C CE1 . TYR A 1 54  ? 8.464   -10.921 24.067  1.00   23.66  ? 54   TYR A CE1 1 
ATOM   401  C CE2 . TYR A 1 54  ? 10.351  -10.510 22.660  1.00   24.70  ? 54   TYR A CE2 1 
ATOM   402  C CZ  . TYR A 1 54  ? 9.443   -10.076 23.604  1.00   23.49  ? 54   TYR A CZ  1 
ATOM   403  O OH  . TYR A 1 54  ? 9.507   -8.790  24.112  1.00   24.76  ? 54   TYR A OH  1 
ATOM   404  N N   . ILE A 1 55  ? 8.223   -15.653 19.047  1.00   26.04  ? 55   ILE A N   1 
ATOM   405  C CA  . ILE A 1 55  ? 8.328   -16.938 18.347  1.00   26.25  ? 55   ILE A CA  1 
ATOM   406  C C   . ILE A 1 55  ? 9.762   -17.192 17.901  1.00   26.87  ? 55   ILE A C   1 
ATOM   407  O O   . ILE A 1 55  ? 10.292  -16.451 17.077  1.00   27.75  ? 55   ILE A O   1 
ATOM   408  C CB  . ILE A 1 55  ? 7.349   -17.036 17.150  1.00   26.41  ? 55   ILE A CB  1 
ATOM   409  C CG1 . ILE A 1 55  ? 5.919   -16.724 17.618  1.00   25.70  ? 55   ILE A CG1 1 
ATOM   410  C CG2 . ILE A 1 55  ? 7.433   -18.438 16.510  1.00   26.06  ? 55   ILE A CG2 1 
ATOM   411  C CD1 . ILE A 1 55  ? 4.951   -16.386 16.518  1.00   23.55  ? 55   ILE A CD1 1 
ATOM   412  N N   . VAL A 1 56  ? 10.380  -18.236 18.451  1.00   27.47  ? 56   VAL A N   1 
ATOM   413  C CA  . VAL A 1 56  ? 11.759  -18.580 18.167  1.00   28.23  ? 56   VAL A CA  1 
ATOM   414  C C   . VAL A 1 56  ? 11.776  -19.634 17.062  1.00   29.96  ? 56   VAL A C   1 
ATOM   415  O O   . VAL A 1 56  ? 11.190  -20.712 17.227  1.00   29.74  ? 56   VAL A O   1 
ATOM   416  C CB  . VAL A 1 56  ? 12.481  -19.125 19.436  1.00   28.44  ? 56   VAL A CB  1 
ATOM   417  C CG1 . VAL A 1 56  ? 13.970  -19.329 19.158  1.00   27.67  ? 56   VAL A CG1 1 
ATOM   418  C CG2 . VAL A 1 56  ? 12.292  -18.173 20.612  1.00   27.52  ? 56   VAL A CG2 1 
ATOM   419  N N   . GLN A 1 57  ? 12.437  -19.301 15.976  0.93   31.49  ? 57   GLN A N   1 
ATOM   420  C CA  . GLN A 1 57  ? 12.415  -20.112 14.793  0.93   33.73  ? 57   GLN A CA  1 
ATOM   421  C C   . GLN A 1 57  ? 13.180  -21.390 14.947  0.93   34.33  ? 57   GLN A C   1 
ATOM   422  O O   . GLN A 1 57  ? 14.284  -21.422 15.449  0.93   35.11  ? 57   GLN A O   1 
ATOM   423  C CB  . GLN A 1 57  ? 12.827  -19.367 13.532  0.93   33.87  ? 57   GLN A CB  1 
ATOM   424  C CG  . GLN A 1 57  ? 12.508  -20.123 12.243  0.93   36.74  ? 57   GLN A CG  1 
ATOM   425  C CD  . GLN A 1 57  ? 13.334  -19.720 11.011  0.93   39.23  ? 57   GLN A CD  1 
ATOM   426  O OE1 . GLN A 1 57  ? 12.784  -19.567 9.933   0.93   39.22  ? 57   GLN A OE1 1 
ATOM   427  N NE2 . GLN A 1 57  ? 14.648  -19.562 11.171  0.93   38.92  ? 57   GLN A NE2 1 
ATOM   428  N N   . SER A 1 58  ? 12.497  -22.425 14.450  0.43   34.83  ? 58   SER A N   1 
ATOM   429  C CA  . SER A 1 58  ? 12.823  -23.837 14.533  0.43   35.21  ? 58   SER A CA  1 
ATOM   430  C C   . SER A 1 58  ? 14.031  -24.192 13.739  0.43   35.29  ? 58   SER A C   1 
ATOM   431  O O   . SER A 1 58  ? 14.360  -23.547 12.789  0.43   35.75  ? 58   SER A O   1 
ATOM   432  C CB  . SER A 1 58  ? 11.680  -24.658 13.960  0.43   35.13  ? 58   SER A CB  1 
ATOM   433  O OG  . SER A 1 58  ? 12.068  -25.976 13.664  0.43   35.38  ? 58   SER A OG  1 
ATOM   434  N N   . GLY A 1 59  ? 14.666  -25.275 14.105  0.0000 48.28  ? 59   GLY A N   1 
ATOM   435  C CA  . GLY A 1 59  ? 15.803  -25.730 13.338  0.0000 49.92  ? 59   GLY A CA  1 
ATOM   436  C C   . GLY A 1 59  ? 15.665  -27.092 12.692  0.0000 51.57  ? 59   GLY A C   1 
ATOM   437  O O   . GLY A 1 59  ? 16.585  -27.895 12.837  0.0000 50.72  ? 59   GLY A O   1 
ATOM   438  N N   . CYS A 1 60  ? 14.565  -27.354 11.968  0.63   43.13  ? 60   CYS A N   1 
ATOM   439  C CA  . CYS A 1 60  ? 14.442  -28.604 11.314  0.63   42.77  ? 60   CYS A CA  1 
ATOM   440  C C   . CYS A 1 60  ? 15.371  -28.604 10.112  0.63   41.34  ? 60   CYS A C   1 
ATOM   441  O O   . CYS A 1 60  ? 15.401  -29.585 9.406   0.63   41.96  ? 60   CYS A O   1 
ATOM   442  C CB  . CYS A 1 60  ? 13.022  -28.821 10.855  0.63   43.33  ? 60   CYS A CB  1 
ATOM   443  S SG  . CYS A 1 60  ? 12.926  -28.641 9.084   0.63   47.32  ? 60   CYS A SG  1 
ATOM   444  N N   . GLY A 1 61  ? 16.114  -27.525 9.868   0.48   39.47  ? 61   GLY A N   1 
ATOM   445  C CA  . GLY A 1 61  ? 17.048  -27.550 8.747   0.48   36.74  ? 61   GLY A CA  1 
ATOM   446  C C   . GLY A 1 61  ? 16.412  -27.225 7.405   0.48   34.83  ? 61   GLY A C   1 
ATOM   447  O O   . GLY A 1 61  ? 17.010  -26.539 6.577   0.48   34.32  ? 61   GLY A O   1 
ATOM   448  N N   . GLU A 1 62  ? 15.199  -27.719 7.181   0.52   32.78  ? 62   GLU A N   1 
ATOM   449  C CA  . GLU A 1 62  ? 14.520  -27.453 5.921   0.52   30.73  ? 62   GLU A CA  1 
ATOM   450  C C   . GLU A 1 62  ? 14.020  -26.007 5.923   0.52   29.86  ? 62   GLU A C   1 
ATOM   451  O O   . GLU A 1 62  ? 13.013  -25.681 6.547   0.52   28.68  ? 62   GLU A O   1 
ATOM   452  C CB  . GLU A 1 62  ? 13.377  -28.447 5.691   0.52   30.29  ? 62   GLU A CB  1 
ATOM   453  C CG  . GLU A 1 62  ? 13.213  -28.894 4.230   0.52   28.13  ? 62   GLU A CG  1 
ATOM   454  C CD  . GLU A 1 62  ? 12.515  -27.869 3.327   0.52   25.88  ? 62   GLU A CD  1 
ATOM   455  O OE1 . GLU A 1 62  ? 12.444  -26.668 3.667   0.52   22.93  ? 62   GLU A OE1 1 
ATOM   456  O OE2 . GLU A 1 62  ? 12.035  -28.282 2.252   0.52   24.54  ? 62   GLU A OE2 1 
ATOM   457  N N   . ILE A 1 63  ? 14.735  -25.150 5.203   1.00   29.37  ? 63   ILE A N   1 
ATOM   458  C CA  . ILE A 1 63  ? 14.545  -23.700 5.312   1.00   29.14  ? 63   ILE A CA  1 
ATOM   459  C C   . ILE A 1 63  ? 13.141  -23.189 4.947   1.00   28.46  ? 63   ILE A C   1 
ATOM   460  O O   . ILE A 1 63  ? 12.622  -22.272 5.592   1.00   27.85  ? 63   ILE A O   1 
ATOM   461  C CB  . ILE A 1 63  ? 15.612  -22.915 4.522   1.00   29.72  ? 63   ILE A CB  1 
ATOM   462  C CG1 . ILE A 1 63  ? 15.641  -21.466 5.007   1.00   30.60  ? 63   ILE A CG1 1 
ATOM   463  C CG2 . ILE A 1 63  ? 15.380  -23.023 3.007   1.00   28.93  ? 63   ILE A CG2 1 
ATOM   464  C CD1 . ILE A 1 63  ? 16.607  -20.562 4.246   1.00   34.88  ? 63   ILE A CD1 1 
ATOM   465  N N   . ASN A 1 64  ? 12.541  -23.776 3.921   1.00   27.63  ? 64   ASN A N   1 
ATOM   466  C CA  . ASN A 1 64  ? 11.218  -23.348 3.502   1.00   27.56  ? 64   ASN A CA  1 
ATOM   467  C C   . ASN A 1 64  ? 10.103  -23.784 4.469   1.00   27.42  ? 64   ASN A C   1 
ATOM   468  O O   . ASN A 1 64  ? 9.191   -23.001 4.749   1.00   26.43  ? 64   ASN A O   1 
ATOM   469  C CB  . ASN A 1 64  ? 10.946  -23.780 2.056   1.00   27.82  ? 64   ASN A CB  1 
ATOM   470  C CG  . ASN A 1 64  ? 11.987  -23.230 1.089   1.00   28.24  ? 64   ASN A CG  1 
ATOM   471  O OD1 . ASN A 1 64  ? 12.390  -22.059 1.175   1.00   26.78  ? 64   ASN A OD1 1 
ATOM   472  N ND2 . ASN A 1 64  ? 12.441  -24.078 0.169   1.00   29.72  ? 64   ASN A ND2 1 
ATOM   473  N N   . ASP A 1 65  ? 10.189  -25.020 4.970   1.00   27.30  ? 65   ASP A N   1 
ATOM   474  C CA  . ASP A 1 65  ? 9.275   -25.524 6.004   1.00   28.11  ? 65   ASP A CA  1 
ATOM   475  C C   . ASP A 1 65  ? 9.343   -24.670 7.266   1.00   27.68  ? 65   ASP A C   1 
ATOM   476  O O   . ASP A 1 65  ? 8.310   -24.319 7.829   1.00   27.41  ? 65   ASP A O   1 
ATOM   477  C CB  . ASP A 1 65  ? 9.619   -26.969 6.386   1.00   28.70  ? 65   ASP A CB  1 
ATOM   478  C CG  . ASP A 1 65  ? 9.323   -27.972 5.277   1.00   30.79  ? 65   ASP A CG  1 
ATOM   479  O OD1 . ASP A 1 65  ? 8.525   -27.684 4.344   1.00   32.60  ? 65   ASP A OD1 1 
ATOM   480  O OD2 . ASP A 1 65  ? 9.886   -29.083 5.362   1.00   34.14  ? 65   ASP A OD2 1 
ATOM   481  N N   . ASN A 1 66  ? 10.565  -24.353 7.697   1.00   27.60  ? 66   ASN A N   1 
ATOM   482  C CA  . ASN A 1 66  ? 10.798  -23.559 8.904   1.00   27.88  ? 66   ASN A CA  1 
ATOM   483  C C   . ASN A 1 66  ? 10.269  -22.137 8.781   1.00   26.07  ? 66   ASN A C   1 
ATOM   484  O O   . ASN A 1 66  ? 9.615   -21.639 9.695   1.00   25.03  ? 66   ASN A O   1 
ATOM   485  C CB  . ASN A 1 66  ? 12.290  -23.559 9.274   1.00   28.76  ? 66   ASN A CB  1 
ATOM   486  C CG  . ASN A 1 66  ? 12.768  -24.927 9.771   1.00   32.54  ? 66   ASN A CG  1 
ATOM   487  O OD1 . ASN A 1 66  ? 12.055  -25.626 10.500  1.00   38.53  ? 66   ASN A OD1 1 
ATOM   488  N ND2 . ASN A 1 66  ? 13.976  -25.302 9.394   1.00   35.55  ? 66   ASN A ND2 1 
ATOM   489  N N   . LEU A 1 67  ? 10.527  -21.510 7.630   1.00   24.88  ? 67   LEU A N   1 
ATOM   490  C CA  . LEU A 1 67  ? 10.002  -20.172 7.341   1.00   24.22  ? 67   LEU A CA  1 
ATOM   491  C C   . LEU A 1 67  ? 8.466   -20.145 7.275   1.00   23.39  ? 67   LEU A C   1 
ATOM   492  O O   . LEU A 1 67  ? 7.833   -19.281 7.883   1.00   23.36  ? 67   LEU A O   1 
ATOM   493  C CB  . LEU A 1 67  ? 10.618  -19.597 6.053   1.00   23.68  ? 67   LEU A CB  1 
ATOM   494  C CG  . LEU A 1 67  ? 10.072  -18.236 5.603   1.00   23.07  ? 67   LEU A CG  1 
ATOM   495  C CD1 . LEU A 1 67  ? 10.283  -17.128 6.665   1.00   22.88  ? 67   LEU A CD1 1 
ATOM   496  C CD2 . LEU A 1 67  ? 10.691  -17.828 4.265   1.00   24.93  ? 67   LEU A CD2 1 
ATOM   497  N N   . MET A 1 68  ? 7.869   -21.087 6.550   0.83   23.31  ? 68   MET A N   1 
ATOM   498  C CA  . MET A 1 68  ? 6.404   -21.146 6.461   0.83   22.73  ? 68   MET A CA  1 
ATOM   499  C C   . MET A 1 68  ? 5.745   -21.375 7.841   0.83   22.41  ? 68   MET A C   1 
ATOM   500  O O   . MET A 1 68  ? 4.777   -20.720 8.180   0.83   21.77  ? 68   MET A O   1 
ATOM   501  C CB  . MET A 1 68  ? 5.945   -22.186 5.428   0.83   22.98  ? 68   MET A CB  1 
ATOM   502  C CG  . MET A 1 68  ? 6.088   -21.712 3.956   0.83   24.31  ? 68   MET A CG  1 
ATOM   503  S SD  . MET A 1 68  ? 5.376   -20.071 3.586   0.83   28.39  ? 68   MET A SD  1 
ATOM   504  C CE  . MET A 1 68  ? 3.691   -20.322 4.190   0.83   22.73  ? 68   MET A CE  1 
ATOM   505  N N   . GLU A 1 69  ? 6.297   -22.289 8.631   1.00   23.04  ? 69   GLU A N   1 
ATOM   506  C CA  . GLU A 1 69  ? 5.819   -22.525 10.002  1.00   24.51  ? 69   GLU A CA  1 
ATOM   507  C C   . GLU A 1 69  ? 5.895   -21.290 10.895  1.00   23.23  ? 69   GLU A C   1 
ATOM   508  O O   . GLU A 1 69  ? 4.962   -20.995 11.628  1.00   23.70  ? 69   GLU A O   1 
ATOM   509  C CB  . GLU A 1 69  ? 6.573   -23.692 10.635  1.00   25.32  ? 69   GLU A CB  1 
ATOM   510  C CG  . GLU A 1 69  ? 5.924   -24.214 11.903  1.00   30.39  ? 69   GLU A CG  1 
ATOM   511  C CD  . GLU A 1 69  ? 6.697   -25.362 12.519  1.00   37.08  ? 69   GLU A CD  1 
ATOM   512  O OE1 . GLU A 1 69  ? 7.944   -25.380 12.408  1.00   39.63  ? 69   GLU A OE1 1 
ATOM   513  O OE2 . GLU A 1 69  ? 6.053   -26.245 13.122  1.00   41.41  ? 69   GLU A OE2 1 
ATOM   514  N N   . LEU A 1 70  ? 6.999   -20.560 10.804  1.00   22.94  ? 70   LEU A N   1 
ATOM   515  C CA  . LEU A 1 70  ? 7.144   -19.288 11.492  1.00   22.36  ? 70   LEU A CA  1 
ATOM   516  C C   . LEU A 1 70  ? 6.100   -18.254 11.043  1.00   22.77  ? 70   LEU A C   1 
ATOM   517  O O   . LEU A 1 70  ? 5.472   -17.590 11.884  1.00   22.73  ? 70   LEU A O   1 
ATOM   518  C CB  . LEU A 1 70  ? 8.566   -18.748 11.289  1.00   22.57  ? 70   LEU A CB  1 
ATOM   519  C CG  . LEU A 1 70  ? 8.930   -17.347 11.812  1.00   23.94  ? 70   LEU A CG  1 
ATOM   520  C CD1 . LEU A 1 70  ? 8.839   -17.272 13.334  1.00   23.75  ? 70   LEU A CD1 1 
ATOM   521  C CD2 . LEU A 1 70  ? 10.314  -16.966 11.360  1.00   22.86  ? 70   LEU A CD2 1 
ATOM   522  N N   . LEU A 1 71  ? 5.901   -18.116 9.727   1.00   21.75  ? 71   LEU A N   1 
ATOM   523  C CA  . LEU A 1 71  ? 4.951   -17.136 9.212   1.00   21.22  ? 71   LEU A CA  1 
ATOM   524  C C   . LEU A 1 71  ? 3.526   -17.442 9.688   1.00   21.43  ? 71   LEU A C   1 
ATOM   525  O O   . LEU A 1 71  ? 2.760   -16.536 10.029  1.00   20.34  ? 71   LEU A O   1 
ATOM   526  C CB  . LEU A 1 71  ? 4.980   -17.101 7.678   1.00   21.01  ? 71   LEU A CB  1 
ATOM   527  C CG  . LEU A 1 71  ? 6.260   -16.585 6.992   1.00   21.06  ? 71   LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 71  ? 6.118   -16.698 5.471   1.00   20.07  ? 71   LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 71  ? 6.587   -15.144 7.394   1.00   16.80  ? 71   LEU A CD2 1 
ATOM   530  N N   . ILE A 1 72  ? 3.197   -18.733 9.702   1.00   21.70  ? 72   ILE A N   1 
ATOM   531  C CA  . ILE A 1 72  ? 1.877   -19.225 10.089  1.00   22.66  ? 72   ILE A CA  1 
ATOM   532  C C   . ILE A 1 72  ? 1.626   -18.981 11.594  1.00   22.61  ? 72   ILE A C   1 
ATOM   533  O O   . ILE A 1 72  ? 0.536   -18.540 11.997  1.00   22.47  ? 72   ILE A O   1 
ATOM   534  C CB  . ILE A 1 72  ? 1.751   -20.729 9.690   1.00   23.28  ? 72   ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 72  ? 1.552   -20.868 8.174   1.00   24.36  ? 72   ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 72  ? 0.615   -21.418 10.440  1.00   24.31  ? 72   ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 72  ? 1.930   -22.250 7.607   1.00   27.77  ? 72   ILE A CD1 1 
ATOM   538  N N   . MET A 1 73  ? 2.642   -19.248 12.416  1.00   22.89  ? 73   MET A N   1 
ATOM   539  C CA  . MET A 1 73  ? 2.568   -18.988 13.855  1.00   23.46  ? 73   MET A CA  1 
ATOM   540  C C   . MET A 1 73  ? 2.442   -17.491 14.149  1.00   22.98  ? 73   MET A C   1 
ATOM   541  O O   . MET A 1 73  ? 1.705   -17.091 15.050  1.00   22.48  ? 73   MET A O   1 
ATOM   542  C CB  . MET A 1 73  ? 3.804   -19.540 14.571  1.00   24.38  ? 73   MET A CB  1 
ATOM   543  C CG  . MET A 1 73  ? 3.893   -21.052 14.582  1.00   28.15  ? 73   MET A CG  1 
ATOM   544  S SD  . MET A 1 73  ? 5.258   -21.630 15.609  1.00   39.07  ? 73   MET A SD  1 
ATOM   545  C CE  . MET A 1 73  ? 4.624   -21.156 17.220  1.00   33.68  ? 73   MET A CE  1 
ATOM   546  N N   . ILE A 1 74  ? 3.177   -16.667 13.404  1.00   23.01  ? 74   ILE A N   1 
ATOM   547  C CA  . ILE A 1 74  ? 3.040   -15.215 13.533  1.00   22.84  ? 74   ILE A CA  1 
ATOM   548  C C   . ILE A 1 74  ? 1.598   -14.803 13.222  1.00   23.46  ? 74   ILE A C   1 
ATOM   549  O O   . ILE A 1 74  ? 0.976   -14.078 14.003  1.00   23.39  ? 74   ILE A O   1 
ATOM   550  C CB  . ILE A 1 74  ? 4.042   -14.447 12.646  1.00   22.77  ? 74   ILE A CB  1 
ATOM   551  C CG1 . ILE A 1 74  ? 5.465   -14.632 13.173  1.00   22.43  ? 74   ILE A CG1 1 
ATOM   552  C CG2 . ILE A 1 74  ? 3.703   -12.938 12.615  1.00   22.14  ? 74   ILE A CG2 1 
ATOM   553  C CD1 . ILE A 1 74  ? 6.539   -14.336 12.141  1.00   21.10  ? 74   ILE A CD1 1 
ATOM   554  N N   . ASN A 1 75  ? 1.071   -15.275 12.093  1.00   24.04  ? 75   ASN A N   1 
ATOM   555  C CA  . ASN A 1 75  ? -0.287  -14.926 11.681  1.00   25.11  ? 75   ASN A CA  1 
ATOM   556  C C   . ASN A 1 75  ? -1.362  -15.363 12.694  1.00   25.33  ? 75   ASN A C   1 
ATOM   557  O O   . ASN A 1 75  ? -2.276  -14.595 13.032  1.00   24.90  ? 75   ASN A O   1 
ATOM   558  C CB  . ASN A 1 75  ? -0.597  -15.492 10.299  1.00   25.72  ? 75   ASN A CB  1 
ATOM   559  C CG  . ASN A 1 75  ? -1.945  -15.033 9.782   1.00   28.42  ? 75   ASN A CG  1 
ATOM   560  O OD1 . ASN A 1 75  ? -2.878  -15.836 9.641   1.00   31.53  ? 75   ASN A OD1 1 
ATOM   561  N ND2 . ASN A 1 75  ? -2.078  -13.732 9.558   1.00   31.73  ? 75   ASN A ND2 1 
ATOM   562  N N   . ALA A 1 76  ? -1.233  -16.595 13.178  1.00   25.56  ? 76   ALA A N   1 
ATOM   563  C CA  . ALA A 1 76  ? -2.167  -17.146 14.156  1.00   25.55  ? 76   ALA A CA  1 
ATOM   564  C C   . ALA A 1 76  ? -2.153  -16.301 15.427  1.00   25.77  ? 76   ALA A C   1 
ATOM   565  O O   . ALA A 1 76  ? -3.211  -15.984 15.958  1.00   25.79  ? 76   ALA A O   1 
ATOM   566  C CB  . ALA A 1 76  ? -1.824  -18.590 14.478  1.00   24.89  ? 76   ALA A CB  1 
ATOM   567  N N   . CYS A 1 77  ? -0.965  -15.916 15.885  1.00   25.89  ? 77   CYS A N   1 
ATOM   568  C CA  . CYS A 1 77  ? -0.848  -15.078 17.086  1.00   27.76  ? 77   CYS A CA  1 
ATOM   569  C C   . CYS A 1 77  ? -1.444  -13.682 16.879  1.00   27.80  ? 77   CYS A C   1 
ATOM   570  O O   . CYS A 1 77  ? -2.111  -13.150 17.758  1.00   27.64  ? 77   CYS A O   1 
ATOM   571  C CB  . CYS A 1 77  ? 0.607   -14.980 17.547  1.00   27.51  ? 77   CYS A CB  1 
ATOM   572  S SG  . CYS A 1 77  ? 1.204   -16.511 18.306  1.00   30.39  ? 77   CYS A SG  1 
ATOM   573  N N   . LYS A 1 78  ? -1.209  -13.114 15.704  1.00   28.17  ? 78   LYS A N   1 
ATOM   574  C CA  . LYS A 1 78  ? -1.733  -11.801 15.358  1.00   29.39  ? 78   LYS A CA  1 
ATOM   575  C C   . LYS A 1 78  ? -3.255  -11.804 15.304  1.00   28.72  ? 78   LYS A C   1 
ATOM   576  O O   . LYS A 1 78  ? -3.880  -10.955 15.913  1.00   29.84  ? 78   LYS A O   1 
ATOM   577  C CB  . LYS A 1 78  ? -1.139  -11.321 14.023  1.00   29.72  ? 78   LYS A CB  1 
ATOM   578  C CG  . LYS A 1 78  ? -1.253  -9.834  13.786  1.00   33.02  ? 78   LYS A CG  1 
ATOM   579  C CD  . LYS A 1 78  ? -0.109  -9.088  14.469  1.00   37.18  ? 78   LYS A CD  1 
ATOM   580  C CE  . LYS A 1 78  ? -0.285  -7.593  14.324  1.00   39.65  ? 78   LYS A CE  1 
ATOM   581  N NZ  . LYS A 1 78  ? 1.049   -6.904  14.338  1.00   42.18  ? 78   LYS A NZ  1 
ATOM   582  N N   . ILE A 1 79  ? -3.853  -12.762 14.595  1.00   29.12  ? 79   ILE A N   1 
ATOM   583  C CA  . ILE A 1 79  ? -5.313  -12.822 14.484  1.00   29.38  ? 79   ILE A CA  1 
ATOM   584  C C   . ILE A 1 79  ? -6.030  -13.348 15.749  1.00   29.38  ? 79   ILE A C   1 
ATOM   585  O O   . ILE A 1 79  ? -7.259  -13.289 15.833  1.00   29.27  ? 79   ILE A O   1 
ATOM   586  C CB  . ILE A 1 79  ? -5.808  -13.553 13.188  1.00   30.18  ? 79   ILE A CB  1 
ATOM   587  C CG1 . ILE A 1 79  ? -5.388  -15.025 13.182  1.00   30.92  ? 79   ILE A CG1 1 
ATOM   588  C CG2 . ILE A 1 79  ? -5.300  -12.821 11.919  1.00   30.64  ? 79   ILE A CG2 1 
ATOM   589  C CD1 . ILE A 1 79  ? -6.057  -15.846 12.102  1.00   35.92  ? 79   ILE A CD1 1 
ATOM   590  N N   . ALA A 1 80  ? -5.249  -13.831 16.722  1.00   29.32  ? 80   ALA A N   1 
ATOM   591  C CA  . ALA A 1 80  ? -5.741  -14.211 18.057  1.00   29.35  ? 80   ALA A CA  1 
ATOM   592  C C   . ALA A 1 80  ? -5.521  -13.060 19.050  1.00   29.63  ? 80   ALA A C   1 
ATOM   593  O O   . ALA A 1 80  ? -5.580  -13.260 20.272  1.00   30.07  ? 80   ALA A O   1 
ATOM   594  C CB  . ALA A 1 80  ? -5.035  -15.480 18.548  1.00   28.79  ? 80   ALA A CB  1 
ATOM   595  N N   . SER A 1 81  ? -5.243  -11.868 18.510  1.00   29.43  ? 81   SER A N   1 
ATOM   596  C CA  . SER A 1 81  ? -5.154  -10.613 19.269  1.00   29.03  ? 81   SER A CA  1 
ATOM   597  C C   . SER A 1 81  ? -3.989  -10.493 20.258  1.00   29.30  ? 81   SER A C   1 
ATOM   598  O O   . SER A 1 81  ? -4.122  -9.831  21.296  1.00   28.84  ? 81   SER A O   1 
ATOM   599  C CB  . SER A 1 81  ? -6.489  -10.287 19.966  1.00   29.62  ? 81   SER A CB  1 
ATOM   600  O OG  . SER A 1 81  ? -7.545  -10.156 19.025  1.00   28.85  ? 81   SER A OG  1 
ATOM   601  N N   . ALA A 1 82  ? -2.852  -11.120 19.940  1.00   29.34  ? 82   ALA A N   1 
ATOM   602  C CA  . ALA A 1 82  ? -1.616  -10.846 20.683  1.00   29.75  ? 82   ALA A CA  1 
ATOM   603  C C   . ALA A 1 82  ? -1.363  -9.342  20.643  1.00   29.96  ? 82   ALA A C   1 
ATOM   604  O O   . ALA A 1 82  ? -1.664  -8.696  19.646  1.00   30.24  ? 82   ALA A O   1 
ATOM   605  C CB  . ALA A 1 82  ? -0.422  -11.600 20.092  1.00   29.00  ? 82   ALA A CB  1 
ATOM   606  N N   . SER A 1 83  ? -0.844  -8.794  21.743  1.00   30.67  ? 83   SER A N   1 
ATOM   607  C CA  . SER A 1 83  ? -0.501  -7.377  21.821  1.00   31.46  ? 83   SER A CA  1 
ATOM   608  C C   . SER A 1 83  ? 0.660   -7.047  20.882  1.00   31.41  ? 83   SER A C   1 
ATOM   609  O O   . SER A 1 83  ? 0.664   -6.007  20.211  1.00   31.96  ? 83   SER A O   1 
ATOM   610  C CB  . SER A 1 83  ? -0.123  -7.019  23.250  1.00   31.45  ? 83   SER A CB  1 
ATOM   611  O OG  . SER A 1 83  ? 0.443   -5.722  23.312  1.00   35.30  ? 83   SER A OG  1 
ATOM   612  N N   . ARG A 1 84  ? 1.646   -7.942  20.843  1.00   30.48  ? 84   ARG A N   1 
ATOM   613  C CA  . ARG A 1 84  ? 2.816   -7.766  19.997  1.00   29.89  ? 84   ARG A CA  1 
ATOM   614  C C   . ARG A 1 84  ? 3.387   -9.139  19.660  1.00   28.74  ? 84   ARG A C   1 
ATOM   615  O O   . ARG A 1 84  ? 3.297   -10.071 20.476  1.00   27.82  ? 84   ARG A O   1 
ATOM   616  C CB  . ARG A 1 84  ? 3.859   -6.884  20.712  1.00   30.17  ? 84   ARG A CB  1 
ATOM   617  C CG  . ARG A 1 84  ? 5.089   -6.553  19.876  1.00   32.85  ? 84   ARG A CG  1 
ATOM   618  C CD  . ARG A 1 84  ? 5.913   -5.436  20.506  1.00   37.56  ? 84   ARG A CD  1 
ATOM   619  N NE  . ARG A 1 84  ? 6.549   -5.878  21.742  1.00   41.84  ? 84   ARG A NE  1 
ATOM   620  C CZ  . ARG A 1 84  ? 7.171   -5.081  22.609  1.00   44.07  ? 84   ARG A CZ  1 
ATOM   621  N NH1 . ARG A 1 84  ? 7.248   -3.767  22.400  1.00   45.72  ? 84   ARG A NH1 1 
ATOM   622  N NH2 . ARG A 1 84  ? 7.713   -5.608  23.699  1.00   43.48  ? 84   ARG A NH2 1 
ATOM   623  N N   . VAL A 1 85  ? 3.946   -9.259  18.451  1.00   27.34  ? 85   VAL A N   1 
ATOM   624  C CA  . VAL A 1 85  ? 4.617   -10.478 18.017  1.00   25.96  ? 85   VAL A CA  1 
ATOM   625  C C   . VAL A 1 85  ? 6.044   -10.158 17.561  1.00   25.21  ? 85   VAL A C   1 
ATOM   626  O O   . VAL A 1 85  ? 6.253   -9.324  16.677  1.00   24.55  ? 85   VAL A O   1 
ATOM   627  C CB  . VAL A 1 85  ? 3.858   -11.197 16.856  1.00   26.50  ? 85   VAL A CB  1 
ATOM   628  C CG1 . VAL A 1 85  ? 4.564   -12.495 16.499  1.00   25.89  ? 85   VAL A CG1 1 
ATOM   629  C CG2 . VAL A 1 85  ? 2.389   -11.471 17.224  1.00   25.90  ? 85   VAL A CG2 1 
ATOM   630  N N   . THR A 1 86  ? 7.010   -10.835 18.167  1.00   23.57  ? 86   THR A N   1 
ATOM   631  C CA  . THR A 1 86  ? 8.397   -10.718 17.789  1.00   23.66  ? 86   THR A CA  1 
ATOM   632  C C   . THR A 1 86  ? 8.846   -12.035 17.211  1.00   23.74  ? 86   THR A C   1 
ATOM   633  O O   . THR A 1 86  ? 8.639   -13.083 17.829  1.00   23.73  ? 86   THR A O   1 
ATOM   634  C CB  . THR A 1 86  ? 9.290   -10.383 19.011  1.00   23.43  ? 86   THR A CB  1 
ATOM   635  O OG1 . THR A 1 86  ? 8.871   -9.138  19.550  1.00   24.84  ? 86   THR A OG1 1 
ATOM   636  C CG2 . THR A 1 86  ? 10.755  -10.294 18.630  1.00   22.26  ? 86   THR A CG2 1 
ATOM   637  N N   . ALA A 1 87  ? 9.440   -11.987 16.020  1.00   23.27  ? 87   ALA A N   1 
ATOM   638  C CA  . ALA A 1 87  ? 10.123  -13.164 15.493  1.00   23.30  ? 87   ALA A CA  1 
ATOM   639  C C   . ALA A 1 87  ? 11.569  -13.143 15.957  1.00   22.71  ? 87   ALA A C   1 
ATOM   640  O O   . ALA A 1 87  ? 12.279  -12.152 15.781  1.00   23.01  ? 87   ALA A O   1 
ATOM   641  C CB  . ALA A 1 87  ? 10.032  -13.228 13.953  1.00   23.06  ? 87   ALA A CB  1 
ATOM   642  N N   . VAL A 1 88  ? 11.973  -14.232 16.600  1.00   22.79  ? 88   VAL A N   1 
ATOM   643  C CA  . VAL A 1 88  ? 13.324  -14.397 17.096  1.00   22.40  ? 88   VAL A CA  1 
ATOM   644  C C   . VAL A 1 88  ? 13.971  -15.413 16.160  1.00   23.16  ? 88   VAL A C   1 
ATOM   645  O O   . VAL A 1 88  ? 13.641  -16.608 16.177  1.00   21.87  ? 88   VAL A O   1 
ATOM   646  C CB  . VAL A 1 88  ? 13.346  -14.893 18.565  1.00   22.42  ? 88   VAL A CB  1 
ATOM   647  C CG1 . VAL A 1 88  ? 14.775  -15.085 19.044  1.00   21.53  ? 88   VAL A CG1 1 
ATOM   648  C CG2 . VAL A 1 88  ? 12.584  -13.913 19.499  1.00   21.65  ? 88   VAL A CG2 1 
ATOM   649  N N   . ILE A 1 89  ? 14.863  -14.908 15.319  1.00   24.20  ? 89   ILE A N   1 
ATOM   650  C CA  . ILE A 1 89  ? 15.414  -15.675 14.209  1.00   26.60  ? 89   ILE A CA  1 
ATOM   651  C C   . ILE A 1 89  ? 16.936  -15.623 14.254  1.00   27.32  ? 89   ILE A C   1 
ATOM   652  O O   . ILE A 1 89  ? 17.544  -14.766 13.629  1.00   27.13  ? 89   ILE A O   1 
ATOM   653  C CB  . ILE A 1 89  ? 14.925  -15.131 12.840  1.00   26.89  ? 89   ILE A CB  1 
ATOM   654  C CG1 . ILE A 1 89  ? 13.417  -14.907 12.837  1.00   28.40  ? 89   ILE A CG1 1 
ATOM   655  C CG2 . ILE A 1 89  ? 15.305  -16.098 11.699  1.00   28.51  ? 89   ILE A CG2 1 
ATOM   656  C CD1 . ILE A 1 89  ? 12.917  -14.107 11.587  1.00   30.79  ? 89   ILE A CD1 1 
ATOM   657  N N   . PRO A 1 90  ? 17.561  -16.543 15.009  1.00   28.79  ? 90   PRO A N   1 
ATOM   658  C CA  . PRO A 1 90  ? 19.021  -16.574 15.131  1.00   29.60  ? 90   PRO A CA  1 
ATOM   659  C C   . PRO A 1 90  ? 19.742  -16.542 13.768  1.00   29.72  ? 90   PRO A C   1 
ATOM   660  O O   . PRO A 1 90  ? 20.720  -15.810 13.605  1.00   30.33  ? 90   PRO A O   1 
ATOM   661  C CB  . PRO A 1 90  ? 19.271  -17.897 15.857  1.00   29.80  ? 90   PRO A CB  1 
ATOM   662  C CG  . PRO A 1 90  ? 18.037  -18.083 16.687  1.00   30.48  ? 90   PRO A CG  1 
ATOM   663  C CD  . PRO A 1 90  ? 16.923  -17.604 15.808  1.00   29.41  ? 90   PRO A CD  1 
ATOM   664  N N   . CYS A 1 91  ? 19.245  -17.297 12.795  1.00   29.81  ? 91   CYS A N   1 
ATOM   665  C CA  . CYS A 1 91  ? 19.849  -17.307 11.461  1.00   30.66  ? 91   CYS A CA  1 
ATOM   666  C C   . CYS A 1 91  ? 18.805  -16.933 10.400  1.00   29.38  ? 91   CYS A C   1 
ATOM   667  O O   . CYS A 1 91  ? 17.917  -17.719 10.069  1.00   28.77  ? 91   CYS A O   1 
ATOM   668  C CB  . CYS A 1 91  ? 20.503  -18.663 11.175  1.00   31.25  ? 91   CYS A CB  1 
ATOM   669  S SG  . CYS A 1 91  ? 21.294  -18.774 9.543   1.00   38.25  ? 91   CYS A SG  1 
ATOM   670  N N   . PHE A 1 92  ? 18.915  -15.712 9.884   1.00   28.56  ? 92   PHE A N   1 
ATOM   671  C CA  . PHE A 1 92  ? 17.883  -15.147 9.025   1.00   27.69  ? 92   PHE A CA  1 
ATOM   672  C C   . PHE A 1 92  ? 17.840  -15.891 7.680   1.00   28.01  ? 92   PHE A C   1 
ATOM   673  O O   . PHE A 1 92  ? 18.863  -15.991 6.988   1.00   27.63  ? 92   PHE A O   1 
ATOM   674  C CB  . PHE A 1 92  ? 18.111  -13.645 8.862   1.00   27.15  ? 92   PHE A CB  1 
ATOM   675  C CG  . PHE A 1 92  ? 16.985  -12.920 8.193   1.00   27.16  ? 92   PHE A CG  1 
ATOM   676  C CD1 . PHE A 1 92  ? 15.947  -12.365 8.944   1.00   26.51  ? 92   PHE A CD1 1 
ATOM   677  C CD2 . PHE A 1 92  ? 16.972  -12.766 6.804   1.00   25.65  ? 92   PHE A CD2 1 
ATOM   678  C CE1 . PHE A 1 92  ? 14.906  -11.679 8.319   1.00   28.48  ? 92   PHE A CE1 1 
ATOM   679  C CE2 . PHE A 1 92  ? 15.934  -12.082 6.165   1.00   26.16  ? 92   PHE A CE2 1 
ATOM   680  C CZ  . PHE A 1 92  ? 14.905  -11.534 6.916   1.00   27.16  ? 92   PHE A CZ  1 
ATOM   681  N N   . PRO A 1 93  ? 16.658  -16.437 7.322   1.00   27.77  ? 93   PRO A N   1 
ATOM   682  C CA  . PRO A 1 93  ? 16.504  -17.237 6.107   1.00   27.50  ? 93   PRO A CA  1 
ATOM   683  C C   . PRO A 1 93  ? 16.813  -16.406 4.861   1.00   27.11  ? 93   PRO A C   1 
ATOM   684  O O   . PRO A 1 93  ? 16.416  -15.234 4.789   1.00   26.26  ? 93   PRO A O   1 
ATOM   685  C CB  . PRO A 1 93  ? 15.010  -17.611 6.122   1.00   28.07  ? 93   PRO A CB  1 
ATOM   686  C CG  . PRO A 1 93  ? 14.579  -17.432 7.550   1.00   28.52  ? 93   PRO A CG  1 
ATOM   687  C CD  . PRO A 1 93  ? 15.373  -16.261 8.026   1.00   27.89  ? 93   PRO A CD  1 
ATOM   688  N N   . TYR A 1 94  ? 17.537  -17.010 3.915   1.00   26.50  ? 94   TYR A N   1 
ATOM   689  C CA  . TYR A 1 94  ? 17.902  -16.380 2.631   1.00   26.46  ? 94   TYR A CA  1 
ATOM   690  C C   . TYR A 1 94  ? 18.759  -15.125 2.773   1.00   26.87  ? 94   TYR A C   1 
ATOM   691  O O   . TYR A 1 94  ? 18.839  -14.313 1.837   1.00   26.95  ? 94   TYR A O   1 
ATOM   692  C CB  . TYR A 1 94  ? 16.646  -16.078 1.779   1.00   25.97  ? 94   TYR A CB  1 
ATOM   693  C CG  . TYR A 1 94  ? 15.975  -17.315 1.218   1.00   24.91  ? 94   TYR A CG  1 
ATOM   694  C CD1 . TYR A 1 94  ? 15.091  -18.066 1.994   1.00   24.88  ? 94   TYR A CD1 1 
ATOM   695  C CD2 . TYR A 1 94  ? 16.217  -17.729 -0.091  1.00   25.58  ? 94   TYR A CD2 1 
ATOM   696  C CE1 . TYR A 1 94  ? 14.481  -19.212 1.495   1.00   24.49  ? 94   TYR A CE1 1 
ATOM   697  C CE2 . TYR A 1 94  ? 15.609  -18.878 -0.608  1.00   24.17  ? 94   TYR A CE2 1 
ATOM   698  C CZ  . TYR A 1 94  ? 14.745  -19.608 0.194   1.00   25.27  ? 94   TYR A CZ  1 
ATOM   699  O OH  . TYR A 1 94  ? 14.126  -20.731 -0.300  1.00   26.54  ? 94   TYR A OH  1 
ATOM   700  N N   . ALA A 1 95  ? 19.413  -14.957 3.925   1.00   26.95  ? 95   ALA A N   1 
ATOM   701  C CA  . ALA A 1 95  ? 20.248  -13.759 4.152   1.00   27.89  ? 95   ALA A CA  1 
ATOM   702  C C   . ALA A 1 95  ? 21.278  -13.498 3.050   1.00   28.24  ? 95   ALA A C   1 
ATOM   703  O O   . ALA A 1 95  ? 21.526  -12.340 2.710   1.00   29.02  ? 95   ALA A O   1 
ATOM   704  C CB  . ALA A 1 95  ? 20.939  -13.815 5.517   1.00   27.20  ? 95   ALA A CB  1 
ATOM   705  N N   . ARG A 1 96  ? 21.870  -14.557 2.499   0.61   28.69  ? 96   ARG A N   1 
ATOM   706  C CA  . ARG A 1 96  ? 22.871  -14.430 1.432   0.61   29.87  ? 96   ARG A CA  1 
ATOM   707  C C   . ARG A 1 96  ? 22.336  -13.814 0.134   0.61   30.25  ? 96   ARG A C   1 
ATOM   708  O O   . ARG A 1 96  ? 23.101  -13.265 -0.665  0.61   29.82  ? 96   ARG A O   1 
ATOM   709  C CB  . ARG A 1 96  ? 23.495  -15.784 1.102   0.61   29.95  ? 96   ARG A CB  1 
ATOM   710  C CG  . ARG A 1 96  ? 24.985  -15.835 1.345   0.61   32.56  ? 96   ARG A CG  1 
ATOM   711  C CD  . ARG A 1 96  ? 25.361  -16.784 2.471   0.61   35.42  ? 96   ARG A CD  1 
ATOM   712  N NE  . ARG A 1 96  ? 26.608  -16.377 3.123   0.61   38.32  ? 96   ARG A NE  1 
ATOM   713  C CZ  . ARG A 1 96  ? 27.832  -16.545 2.612   0.61   39.72  ? 96   ARG A CZ  1 
ATOM   714  N NH1 . ARG A 1 96  ? 28.006  -17.118 1.421   0.61   40.58  ? 96   ARG A NH1 1 
ATOM   715  N NH2 . ARG A 1 96  ? 28.887  -16.122 3.295   0.61   40.50  ? 96   ARG A NH2 1 
ATOM   716  N N   . GLN A 1 97  ? 21.026  -13.934 -0.067  0.93   30.57  ? 97   GLN A N   1 
ATOM   717  C CA  . GLN A 1 97  ? 20.359  -13.397 -1.246  0.93   31.29  ? 97   GLN A CA  1 
ATOM   718  C C   . GLN A 1 97  ? 19.827  -11.987 -0.937  0.93   31.19  ? 97   GLN A C   1 
ATOM   719  O O   . GLN A 1 97  ? 18.618  -11.751 -0.929  0.93   29.45  ? 97   GLN A O   1 
ATOM   720  C CB  . GLN A 1 97  ? 19.239  -14.350 -1.694  0.93   31.53  ? 97   GLN A CB  1 
ATOM   721  C CG  . GLN A 1 97  ? 19.772  -15.683 -2.281  0.93   34.33  ? 97   GLN A CG  1 
ATOM   722  C CD  . GLN A 1 97  ? 18.675  -16.628 -2.772  0.93   37.96  ? 97   GLN A CD  1 
ATOM   723  O OE1 . GLN A 1 97  ? 17.773  -16.240 -3.524  0.93   39.56  ? 97   GLN A OE1 1 
ATOM   724  N NE2 . GLN A 1 97  ? 18.764  -17.889 -2.354  0.93   39.12  ? 97   GLN A NE2 1 
ATOM   725  N N   . ASP A 1 98  ? 20.757  -11.059 -0.685  1.00   31.95  ? 98   ASP A N   1 
ATOM   726  C CA  . ASP A 1 98  ? 20.408  -9.694  -0.285  1.00   33.34  ? 98   ASP A CA  1 
ATOM   727  C C   . ASP A 1 98  ? 20.718  -8.638  -1.356  1.00   33.88  ? 98   ASP A C   1 
ATOM   728  O O   . ASP A 1 98  ? 20.573  -7.430  -1.112  1.00   33.72  ? 98   ASP A O   1 
ATOM   729  C CB  . ASP A 1 98  ? 21.072  -9.332  1.049   1.00   33.52  ? 98   ASP A CB  1 
ATOM   730  C CG  . ASP A 1 98  ? 22.600  -9.353  0.983   1.00   35.81  ? 98   ASP A CG  1 
ATOM   731  O OD1 . ASP A 1 98  ? 23.186  -9.861  -0.003  1.00   37.51  ? 98   ASP A OD1 1 
ATOM   732  O OD2 . ASP A 1 98  ? 23.220  -8.850  1.936   1.00   37.33  ? 98   ASP A OD2 1 
ATOM   733  N N   . LYS A 1 99  ? 21.136  -9.103  -2.535  1.00   34.24  ? 99   LYS A N   1 
ATOM   734  C CA  . LYS A 1 99  ? 21.420  -8.222  -3.666  1.00   35.48  ? 99   LYS A CA  1 
ATOM   735  C C   . LYS A 1 99  ? 21.373  -8.986  -4.996  1.00   35.40  ? 99   LYS A C   1 
ATOM   736  O O   . LYS A 1 99  ? 21.460  -10.215 -5.016  1.00   35.68  ? 99   LYS A O   1 
ATOM   737  C CB  . LYS A 1 99  ? 22.766  -7.506  -3.472  1.00   35.16  ? 99   LYS A CB  1 
ATOM   738  C CG  . LYS A 1 99  ? 23.963  -8.425  -3.567  1.00   37.70  ? 99   LYS A CG  1 
ATOM   739  C CD  . LYS A 1 99  ? 25.193  -7.781  -2.962  1.00   41.31  ? 99   LYS A CD  1 
ATOM   740  C CE  . LYS A 1 99  ? 26.413  -8.644  -3.204  1.00   44.51  ? 99   LYS A CE  1 
ATOM   741  N NZ  . LYS A 1 99  ? 26.194  -10.043 -2.716  1.00   46.23  ? 99   LYS A NZ  1 
ATOM   742  N N   . LYS A 1 100 ? 21.220  -8.258  -6.100  0.90   35.88  ? 100  LYS A N   1 
ATOM   743  C CA  . LYS A 1 100 ? 21.105  -8.881  -7.437  0.90   35.98  ? 100  LYS A CA  1 
ATOM   744  C C   . LYS A 1 100 ? 22.426  -9.469  -7.951  0.90   36.27  ? 100  LYS A C   1 
ATOM   745  O O   . LYS A 1 100 ? 22.419  -10.451 -8.701  0.90   36.37  ? 100  LYS A O   1 
ATOM   746  C CB  . LYS A 1 100 ? 20.575  -7.878  -8.465  0.90   35.96  ? 100  LYS A CB  1 
ATOM   747  C CG  . LYS A 1 100 ? 19.105  -7.487  -8.320  0.90   35.35  ? 100  LYS A CG  1 
ATOM   748  C CD  . LYS A 1 100 ? 18.701  -6.637  -9.516  0.90   34.65  ? 100  LYS A CD  1 
ATOM   749  C CE  . LYS A 1 100 ? 17.251  -6.223  -9.439  0.90   35.85  ? 100  LYS A CE  1 
ATOM   750  N NZ  . LYS A 1 100 ? 16.923  -5.088  -10.373 0.90   35.62  ? 100  LYS A NZ  1 
ATOM   751  N N   . ASP A 1 101 ? 23.545  -8.852  -7.569  0.50   36.50  ? 101  ASP A N   1 
ATOM   752  C CA  . ASP A 1 101 ? 24.879  -9.302  -7.986  0.50   37.01  ? 101  ASP A CA  1 
ATOM   753  C C   . ASP A 1 101 ? 25.045  -9.279  -9.515  0.50   37.01  ? 101  ASP A C   1 
ATOM   754  O O   . ASP A 1 101 ? 25.613  -10.203 -10.094 0.50   36.85  ? 101  ASP A O   1 
ATOM   755  C CB  . ASP A 1 101 ? 25.152  -10.712 -7.441  0.50   37.19  ? 101  ASP A CB  1 
ATOM   756  C CG  . ASP A 1 101 ? 26.628  -11.046 -7.393  0.50   37.81  ? 101  ASP A CG  1 
ATOM   757  O OD1 . ASP A 1 101 ? 27.431  -10.115 -7.163  0.50   38.27  ? 101  ASP A OD1 1 
ATOM   758  O OD2 . ASP A 1 101 ? 26.982  -12.244 -7.575  0.50   38.53  ? 101  ASP A OD2 1 
ATOM   759  N N   . LYS A 1 102 ? 24.524  -8.235  -10.165 0.50   37.36  ? 102  LYS A N   1 
ATOM   760  C CA  . LYS A 1 102 ? 24.605  -8.114  -11.631 0.50   37.90  ? 102  LYS A CA  1 
ATOM   761  C C   . LYS A 1 102 ? 23.776  -9.136  -12.415 0.50   38.07  ? 102  LYS A C   1 
ATOM   762  O O   . LYS A 1 102 ? 23.839  -9.176  -13.649 0.50   38.20  ? 102  LYS A O   1 
ATOM   763  C CB  . LYS A 1 102 ? 26.058  -8.188  -12.108 0.50   37.89  ? 102  LYS A CB  1 
ATOM   764  C CG  . LYS A 1 102 ? 26.985  -7.184  -11.465 0.50   38.77  ? 102  LYS A CG  1 
ATOM   765  C CD  . LYS A 1 102 ? 28.040  -6.709  -12.453 0.50   40.74  ? 102  LYS A CD  1 
ATOM   766  C CE  . LYS A 1 102 ? 28.662  -7.886  -13.195 0.50   40.75  ? 102  LYS A CE  1 
ATOM   767  N NZ  . LYS A 1 102 ? 29.538  -7.398  -14.297 0.50   42.78  ? 102  LYS A NZ  1 
ATOM   768  N N   . SER A 1 103 ? 23.016  -9.961  -11.698 1.00   38.31  ? 103  SER A N   1 
ATOM   769  C CA  . SER A 1 103 ? 22.173  -10.997 -12.296 1.00   38.75  ? 103  SER A CA  1 
ATOM   770  C C   . SER A 1 103 ? 20.699  -10.594 -12.286 1.00   38.16  ? 103  SER A C   1 
ATOM   771  O O   . SER A 1 103 ? 20.286  -9.714  -11.523 1.00   38.32  ? 103  SER A O   1 
ATOM   772  C CB  . SER A 1 103 ? 22.326  -12.310 -11.513 1.00   38.97  ? 103  SER A CB  1 
ATOM   773  O OG  . SER A 1 103 ? 23.626  -12.857 -11.669 1.00   41.58  ? 103  SER A OG  1 
ATOM   774  N N   . ARG A 1 104 ? 19.906  -11.257 -13.122 1.00   37.85  ? 104  ARG A N   1 
ATOM   775  C CA  . ARG A 1 104 ? 18.454  -11.117 -13.083 1.00   37.73  ? 104  ARG A CA  1 
ATOM   776  C C   . ARG A 1 104 ? 17.922  -11.999 -11.953 1.00   36.82  ? 104  ARG A C   1 
ATOM   777  O O   . ARG A 1 104 ? 17.179  -12.962 -12.177 1.00   37.17  ? 104  ARG A O   1 
ATOM   778  C CB  . ARG A 1 104 ? 17.818  -11.461 -14.440 1.00   38.01  ? 104  ARG A CB  1 
ATOM   779  C CG  . ARG A 1 104 ? 17.591  -10.244 -15.336 1.00   40.11  ? 104  ARG A CG  1 
ATOM   780  C CD  . ARG A 1 104 ? 17.067  -10.616 -16.729 1.00   40.20  ? 104  ARG A CD  1 
ATOM   781  N NE  . ARG A 1 104 ? 17.979  -11.540 -17.405 1.00   43.79  ? 104  ARG A NE  1 
ATOM   782  C CZ  . ARG A 1 104 ? 18.756  -11.232 -18.437 1.00   44.19  ? 104  ARG A CZ  1 
ATOM   783  N NH1 . ARG A 1 104 ? 18.740  -10.015 -18.967 1.00   43.46  ? 104  ARG A NH1 1 
ATOM   784  N NH2 . ARG A 1 104 ? 19.548  -12.164 -18.954 1.00   47.17  ? 104  ARG A NH2 1 
ATOM   785  N N   . ALA A 1 105 ? 18.311  -11.632 -10.733 1.00   35.38  ? 105  ALA A N   1 
ATOM   786  C CA  . ALA A 1 105 ? 18.134  -12.459 -9.557  1.00   34.78  ? 105  ALA A CA  1 
ATOM   787  C C   . ALA A 1 105 ? 17.110  -11.848 -8.599  1.00   33.51  ? 105  ALA A C   1 
ATOM   788  O O   . ALA A 1 105 ? 16.873  -10.638 -8.623  1.00   33.45  ? 105  ALA A O   1 
ATOM   789  C CB  . ALA A 1 105 ? 19.483  -12.651 -8.846  1.00   34.97  ? 105  ALA A CB  1 
ATOM   790  N N   . PRO A 1 106 ? 16.489  -12.685 -7.757  1.00   32.36  ? 106  PRO A N   1 
ATOM   791  C CA  . PRO A 1 106 ? 15.668  -12.104 -6.715  1.00   31.44  ? 106  PRO A CA  1 
ATOM   792  C C   . PRO A 1 106 ? 16.548  -11.546 -5.595  1.00   30.41  ? 106  PRO A C   1 
ATOM   793  O O   . PRO A 1 106 ? 17.697  -11.960 -5.444  1.00   30.73  ? 106  PRO A O   1 
ATOM   794  C CB  . PRO A 1 106 ? 14.880  -13.303 -6.196  1.00   31.50  ? 106  PRO A CB  1 
ATOM   795  C CG  . PRO A 1 106 ? 15.783  -14.461 -6.441  1.00   32.14  ? 106  PRO A CG  1 
ATOM   796  C CD  . PRO A 1 106 ? 16.544  -14.158 -7.674  1.00   32.31  ? 106  PRO A CD  1 
ATOM   797  N N   . ILE A 1 107 ? 16.016  -10.596 -4.844  1.00   29.25  ? 107  ILE A N   1 
ATOM   798  C CA  . ILE A 1 107 ? 16.609  -10.186 -3.578  1.00   27.89  ? 107  ILE A CA  1 
ATOM   799  C C   . ILE A 1 107 ? 15.704  -10.891 -2.577  1.00   27.03  ? 107  ILE A C   1 
ATOM   800  O O   . ILE A 1 107 ? 14.753  -10.298 -2.068  1.00   26.74  ? 107  ILE A O   1 
ATOM   801  C CB  . ILE A 1 107 ? 16.609  -8.643  -3.418  1.00   28.08  ? 107  ILE A CB  1 
ATOM   802  C CG1 . ILE A 1 107 ? 17.366  -7.993  -4.593  1.00   28.02  ? 107  ILE A CG1 1 
ATOM   803  C CG2 . ILE A 1 107 ? 17.234  -8.234  -2.089  1.00   28.06  ? 107  ILE A CG2 1 
ATOM   804  C CD1 . ILE A 1 107 ? 17.216  -6.486  -4.714  1.00   29.41  ? 107  ILE A CD1 1 
ATOM   805  N N   . SER A 1 108 ? 15.976  -12.185 -2.370  1.00   25.79  ? 108  SER A N   1 
ATOM   806  C CA  . SER A 1 108 ? 15.078  -13.063 -1.629  1.00   25.36  ? 108  SER A CA  1 
ATOM   807  C C   . SER A 1 108 ? 15.040  -12.699 -0.155  1.00   24.11  ? 108  SER A C   1 
ATOM   808  O O   . SER A 1 108 ? 14.045  -12.945 0.504   1.00   24.15  ? 108  SER A O   1 
ATOM   809  C CB  . SER A 1 108 ? 15.481  -14.540 -1.776  1.00   25.52  ? 108  SER A CB  1 
ATOM   810  O OG  . SER A 1 108 ? 15.528  -14.922 -3.135  1.00   27.01  ? 108  SER A OG  1 
ATOM   811  N N   . ALA A 1 109 ? 16.118  -12.101 0.351   1.00   23.04  ? 109  ALA A N   1 
ATOM   812  C CA  . ALA A 1 109 ? 16.130  -11.613 1.733   1.00   22.35  ? 109  ALA A CA  1 
ATOM   813  C C   . ALA A 1 109 ? 15.089  -10.509 1.958   1.00   22.08  ? 109  ALA A C   1 
ATOM   814  O O   . ALA A 1 109 ? 14.472  -10.451 3.028   1.00   22.35  ? 109  ALA A O   1 
ATOM   815  C CB  . ALA A 1 109 ? 17.513  -11.144 2.120   1.00   21.92  ? 109  ALA A CB  1 
ATOM   816  N N   . LYS A 1 110 ? 14.886  -9.649  0.953   1.00   21.79  ? 110  LYS A N   1 
ATOM   817  C CA  . LYS A 1 110 ? 13.845  -8.624  1.041   1.00   21.62  ? 110  LYS A CA  1 
ATOM   818  C C   . LYS A 1 110 ? 12.461  -9.264  0.938   1.00   21.54  ? 110  LYS A C   1 
ATOM   819  O O   . LYS A 1 110 ? 11.527  -8.867  1.632   1.00   19.92  ? 110  LYS A O   1 
ATOM   820  C CB  . LYS A 1 110 ? 14.030  -7.530  -0.027  1.00   21.93  ? 110  LYS A CB  1 
ATOM   821  C CG  . LYS A 1 110 ? 12.875  -6.526  -0.095  1.00   22.00  ? 110  LYS A CG  1 
ATOM   822  C CD  . LYS A 1 110 ? 12.662  -5.814  1.267   1.00   23.85  ? 110  LYS A CD  1 
ATOM   823  C CE  . LYS A 1 110 ? 11.583  -4.748  1.194   1.00   24.44  ? 110  LYS A CE  1 
ATOM   824  N NZ  . LYS A 1 110 ? 11.916  -3.740  0.120   1.00   28.39  ? 110  LYS A NZ  1 
ATOM   825  N N   . LEU A 1 111 ? 12.329  -10.269 0.075   1.00   21.46  ? 111  LEU A N   1 
ATOM   826  C CA  . LEU A 1 111 ? 11.070  -10.993 0.004   1.00   22.44  ? 111  LEU A CA  1 
ATOM   827  C C   . LEU A 1 111 ? 10.745  -11.588 1.385   1.00   21.72  ? 111  LEU A C   1 
ATOM   828  O O   . LEU A 1 111 ? 9.624   -11.421 1.895   1.00   21.93  ? 111  LEU A O   1 
ATOM   829  C CB  . LEU A 1 111 ? 11.138  -12.083 -1.073  1.00   22.89  ? 111  LEU A CB  1 
ATOM   830  C CG  . LEU A 1 111 ? 9.949   -13.000 -1.399  1.00   26.11  ? 111  LEU A CG  1 
ATOM   831  C CD1 . LEU A 1 111 ? 9.922   -14.255 -0.527  1.00   28.53  ? 111  LEU A CD1 1 
ATOM   832  C CD2 . LEU A 1 111 ? 8.596   -12.286 -1.361  1.00   25.89  ? 111  LEU A CD2 1 
ATOM   833  N N   . VAL A 1 112 ? 11.735  -12.237 2.005   1.00   20.84  ? 112  VAL A N   1 
ATOM   834  C CA  . VAL A 1 112 ? 11.538  -12.830 3.327   1.00   20.44  ? 112  VAL A CA  1 
ATOM   835  C C   . VAL A 1 112 ? 11.129  -11.779 4.364   1.00   20.38  ? 112  VAL A C   1 
ATOM   836  O O   . VAL A 1 112 ? 10.214  -12.015 5.153   1.00   20.14  ? 112  VAL A O   1 
ATOM   837  C CB  . VAL A 1 112 ? 12.762  -13.653 3.811   1.00   20.38  ? 112  VAL A CB  1 
ATOM   838  C CG1 . VAL A 1 112 ? 12.553  -14.122 5.256   1.00   21.15  ? 112  VAL A CG1 1 
ATOM   839  C CG2 . VAL A 1 112 ? 12.952  -14.866 2.911   1.00   20.92  ? 112  VAL A CG2 1 
ATOM   840  N N   . ALA A 1 113 ? 11.777  -10.615 4.329   1.00   19.87  ? 113  ALA A N   1 
ATOM   841  C CA  . ALA A 1 113 ? 11.405  -9.485  5.212   1.00   20.64  ? 113  ALA A CA  1 
ATOM   842  C C   . ALA A 1 113 ? 9.950   -9.022  5.033   1.00   20.33  ? 113  ALA A C   1 
ATOM   843  O O   . ALA A 1 113 ? 9.234   -8.783  6.015   1.00   20.20  ? 113  ALA A O   1 
ATOM   844  C CB  . ALA A 1 113 ? 12.346  -8.317  4.992   1.00   19.83  ? 113  ALA A CB  1 
ATOM   845  N N   . ASN A 1 114 ? 9.536   -8.877  3.775   1.00   20.26  ? 114  ASN A N   1 
ATOM   846  C CA  . ASN A 1 114 ? 8.133   -8.611  3.433   1.00   20.32  ? 114  ASN A CA  1 
ATOM   847  C C   . ASN A 1 114 ? 7.156   -9.691  3.897   1.00   19.85  ? 114  ASN A C   1 
ATOM   848  O O   . ASN A 1 114 ? 6.075   -9.366  4.390   1.00   19.82  ? 114  ASN A O   1 
ATOM   849  C CB  . ASN A 1 114 ? 7.976   -8.384  1.918   1.00   20.38  ? 114  ASN A CB  1 
ATOM   850  C CG  . ASN A 1 114 ? 8.508   -7.016  1.468   1.00   22.75  ? 114  ASN A CG  1 
ATOM   851  O OD1 . ASN A 1 114 ? 8.635   -6.088  2.267   1.00   24.74  ? 114  ASN A OD1 1 
ATOM   852  N ND2 . ASN A 1 114 ? 8.792   -6.888  0.187   1.00   22.77  ? 114  ASN A ND2 1 
ATOM   853  N N   . THR A 1 115 ? 7.505   -10.970 3.740   1.00   20.13  ? 115  THR A N   1 
ATOM   854  C CA  . THR A 1 115 ? 6.599   -12.030 4.234   1.00   20.93  ? 115  THR A CA  1 
ATOM   855  C C   . THR A 1 115 ? 6.414   -11.936 5.760   1.00   20.87  ? 115  THR A C   1 
ATOM   856  O O   . THR A 1 115 ? 5.287   -12.056 6.276   1.00   20.48  ? 115  THR A O   1 
ATOM   857  C CB  . THR A 1 115 ? 7.029   -13.466 3.829   1.00   20.73  ? 115  THR A CB  1 
ATOM   858  O OG1 . THR A 1 115 ? 8.312   -13.763 4.380   1.00   21.91  ? 115  THR A OG1 1 
ATOM   859  C CG2 . THR A 1 115 ? 7.085   -13.622 2.304   1.00   21.94  ? 115  THR A CG2 1 
ATOM   860  N N   . LEU A 1 116 ? 7.520   -11.714 6.472   1.00   21.33  ? 116  LEU A N   1 
ATOM   861  C CA  . LEU A 1 116 ? 7.464   -11.533 7.932   1.00   22.52  ? 116  LEU A CA  1 
ATOM   862  C C   . LEU A 1 116 ? 6.599   -10.350 8.321   1.00   22.97  ? 116  LEU A C   1 
ATOM   863  O O   . LEU A 1 116 ? 5.801   -10.447 9.244   1.00   23.37  ? 116  LEU A O   1 
ATOM   864  C CB  . LEU A 1 116 ? 8.862   -11.402 8.533   1.00   21.93  ? 116  LEU A CB  1 
ATOM   865  C CG  . LEU A 1 116 ? 9.639   -12.726 8.522   1.00   23.04  ? 116  LEU A CG  1 
ATOM   866  C CD1 . LEU A 1 116 ? 11.147  -12.511 8.661   1.00   20.08  ? 116  LEU A CD1 1 
ATOM   867  C CD2 . LEU A 1 116 ? 9.093   -13.688 9.583   1.00   22.88  ? 116  LEU A CD2 1 
ATOM   868  N N   . SER A 1 117 ? 6.754   -9.245  7.595   1.00   24.20  ? 117  SER A N   1 
ATOM   869  C CA  . SER A 1 117 ? 5.990   -8.033  7.866   1.00   25.56  ? 117  SER A CA  1 
ATOM   870  C C   . SER A 1 117 ? 4.501   -8.217  7.565   1.00   25.17  ? 117  SER A C   1 
ATOM   871  O O   . SER A 1 117 ? 3.654   -7.838  8.367   1.00   25.91  ? 117  SER A O   1 
ATOM   872  C CB  . SER A 1 117 ? 6.553   -6.864  7.053   1.00   26.25  ? 117  SER A CB  1 
ATOM   873  O OG  . SER A 1 117 ? 7.935   -6.704  7.326   1.00   29.35  ? 117  SER A OG  1 
ATOM   874  N N   . VAL A 1 118 ? 4.176   -8.819  6.430   1.00   24.89  ? 118  VAL A N   1 
ATOM   875  C CA  . VAL A 1 118 ? 2.773   -9.053  6.102   1.00   25.62  ? 118  VAL A CA  1 
ATOM   876  C C   . VAL A 1 118 ? 2.132   -10.113 7.029   1.00   25.41  ? 118  VAL A C   1 
ATOM   877  O O   . VAL A 1 118 ? 0.941   -10.022 7.348   1.00   25.53  ? 118  VAL A O   1 
ATOM   878  C CB  . VAL A 1 118 ? 2.568   -9.340  4.578   1.00   25.75  ? 118  VAL A CB  1 
ATOM   879  C CG1 . VAL A 1 118 ? 2.786   -10.817 4.234   1.00   26.01  ? 118  VAL A CG1 1 
ATOM   880  C CG2 . VAL A 1 118 ? 1.192   -8.864  4.121   1.00   27.60  ? 118  VAL A CG2 1 
ATOM   881  N N   . ALA A 1 119 ? 2.926   -11.078 7.502   1.00   25.14  ? 119  ALA A N   1 
ATOM   882  C CA  . ALA A 1 119 ? 2.411   -12.082 8.443   1.00   25.46  ? 119  ALA A CA  1 
ATOM   883  C C   . ALA A 1 119 ? 1.981   -11.444 9.764   1.00   25.60  ? 119  ALA A C   1 
ATOM   884  O O   . ALA A 1 119 ? 1.176   -12.012 10.499  1.00   26.52  ? 119  ALA A O   1 
ATOM   885  C CB  . ALA A 1 119 ? 3.422   -13.187 8.681   1.00   25.02  ? 119  ALA A CB  1 
ATOM   886  N N   . GLY A 1 120 ? 2.521   -10.263 10.061  1.00   25.83  ? 120  GLY A N   1 
ATOM   887  C CA  . GLY A 1 120 ? 2.151   -9.529  11.267  1.00   25.71  ? 120  GLY A CA  1 
ATOM   888  C C   . GLY A 1 120 ? 3.239   -9.349  12.320  1.00   25.52  ? 120  GLY A C   1 
ATOM   889  O O   . GLY A 1 120 ? 2.938   -8.964  13.440  1.00   26.38  ? 120  GLY A O   1 
ATOM   890  N N   . ALA A 1 121 ? 4.502   -9.617  11.988  1.00   25.19  ? 121  ALA A N   1 
ATOM   891  C CA  . ALA A 1 121 ? 5.578   -9.402  12.966  1.00   24.36  ? 121  ALA A CA  1 
ATOM   892  C C   . ALA A 1 121 ? 5.753   -7.907  13.253  1.00   23.99  ? 121  ALA A C   1 
ATOM   893  O O   . ALA A 1 121 ? 5.736   -7.089  12.319  1.00   24.63  ? 121  ALA A O   1 
ATOM   894  C CB  . ALA A 1 121 ? 6.882   -10.008 12.489  1.00   24.31  ? 121  ALA A CB  1 
ATOM   895  N N   . ASP A 1 122 ? 5.892   -7.555  14.533  0.79   22.20  ? 122  ASP A N   1 
ATOM   896  C CA  . ASP A 1 122 ? 6.090   -6.174  14.945  0.79   22.02  ? 122  ASP A CA  1 
ATOM   897  C C   . ASP A 1 122 ? 7.553   -5.888  15.242  0.79   21.59  ? 122  ASP A C   1 
ATOM   898  O O   . ASP A 1 122 ? 7.946   -4.743  15.387  0.79   21.21  ? 122  ASP A O   1 
ATOM   899  C CB  . ASP A 1 122 ? 5.267   -5.850  16.197  0.79   22.74  ? 122  ASP A CB  1 
ATOM   900  C CG  . ASP A 1 122 ? 3.782   -6.118  16.022  0.79   24.04  ? 122  ASP A CG  1 
ATOM   901  O OD1 . ASP A 1 122 ? 3.245   -6.936  16.805  0.79   27.08  ? 122  ASP A OD1 1 
ATOM   902  O OD2 . ASP A 1 122 ? 3.148   -5.529  15.116  0.79   23.53  ? 122  ASP A OD2 1 
ATOM   903  N N   . HIS A 1 123 ? 8.362   -6.936  15.354  1.00   21.78  ? 123  HIS A N   1 
ATOM   904  C CA  . HIS A 1 123 ? 9.735   -6.776  15.830  1.00   22.99  ? 123  HIS A CA  1 
ATOM   905  C C   . HIS A 1 123 ? 10.501  -8.022  15.499  1.00   22.63  ? 123  HIS A C   1 
ATOM   906  O O   . HIS A 1 123 ? 9.933   -9.113  15.518  1.00   22.98  ? 123  HIS A O   1 
ATOM   907  C CB  . HIS A 1 123 ? 9.755   -6.523  17.351  1.00   24.27  ? 123  HIS A CB  1 
ATOM   908  C CG  . HIS A 1 123 ? 11.133  -6.342  17.909  1.00   27.68  ? 123  HIS A CG  1 
ATOM   909  N ND1 . HIS A 1 123 ? 11.522  -6.872  19.118  1.00   32.27  ? 123  HIS A ND1 1 
ATOM   910  C CD2 . HIS A 1 123 ? 12.219  -5.703  17.410  1.00   31.16  ? 123  HIS A CD2 1 
ATOM   911  C CE1 . HIS A 1 123 ? 12.785  -6.551  19.350  1.00   33.69  ? 123  HIS A CE1 1 
ATOM   912  N NE2 . HIS A 1 123 ? 13.232  -5.848  18.325  1.00   32.77  ? 123  HIS A NE2 1 
ATOM   913  N N   . ILE A 1 124 ? 11.766  -7.855  15.130  1.00   22.47  ? 124  ILE A N   1 
ATOM   914  C CA  . ILE A 1 124 ? 12.622  -8.975  14.812  1.00   22.92  ? 124  ILE A CA  1 
ATOM   915  C C   . ILE A 1 124 ? 13.812  -8.939  15.726  1.00   23.38  ? 124  ILE A C   1 
ATOM   916  O O   . ILE A 1 124 ? 14.387  -7.883  15.944  1.00   23.47  ? 124  ILE A O   1 
ATOM   917  C CB  . ILE A 1 124 ? 13.168  -8.938  13.353  1.00   23.36  ? 124  ILE A CB  1 
ATOM   918  C CG1 . ILE A 1 124 ? 12.047  -8.697  12.323  1.00   23.46  ? 124  ILE A CG1 1 
ATOM   919  C CG2 . ILE A 1 124 ? 13.995  -10.210 13.057  1.00   23.72  ? 124  ILE A CG2 1 
ATOM   920  C CD1 . ILE A 1 124 ? 10.959  -9.786  12.276  1.00   24.98  ? 124  ILE A CD1 1 
ATOM   921  N N   . ILE A 1 125 ? 14.179  -10.104 16.252  1.00   24.44  ? 125  ILE A N   1 
ATOM   922  C CA  . ILE A 1 125 ? 15.467  -10.290 16.889  1.00   25.18  ? 125  ILE A CA  1 
ATOM   923  C C   . ILE A 1 125 ? 16.234  -11.339 16.107  1.00   25.82  ? 125  ILE A C   1 
ATOM   924  O O   . ILE A 1 125 ? 15.734  -12.446 15.868  1.00   25.54  ? 125  ILE A O   1 
ATOM   925  C CB  . ILE A 1 125 ? 15.312  -10.743 18.377  1.00   25.76  ? 125  ILE A CB  1 
ATOM   926  C CG1 . ILE A 1 125 ? 14.572  -9.673  19.178  1.00   24.04  ? 125  ILE A CG1 1 
ATOM   927  C CG2 . ILE A 1 125 ? 16.687  -11.022 18.979  1.00   25.19  ? 125  ILE A CG2 1 
ATOM   928  C CD1 . ILE A 1 125 ? 14.129  -10.112 20.593  1.00   24.56  ? 125  ILE A CD1 1 
ATOM   929  N N   . THR A 1 126 ? 17.451  -10.987 15.707  1.00   26.53  ? 126  THR A N   1 
ATOM   930  C CA  . THR A 1 126 ? 18.293  -11.879 14.933  1.00   27.54  ? 126  THR A CA  1 
ATOM   931  C C   . THR A 1 126 ? 19.753  -11.750 15.368  1.00   28.01  ? 126  THR A C   1 
ATOM   932  O O   . THR A 1 126 ? 20.090  -10.839 16.132  1.00   27.57  ? 126  THR A O   1 
ATOM   933  C CB  . THR A 1 126 ? 18.142  -11.584 13.427  1.00   28.09  ? 126  THR A CB  1 
ATOM   934  O OG1 . THR A 1 126 ? 18.707  -12.661 12.671  1.00   31.01  ? 126  THR A OG1 1 
ATOM   935  C CG2 . THR A 1 126 ? 18.815  -10.263 13.058  1.00   27.42  ? 126  THR A CG2 1 
ATOM   936  N N   . MET A 1 127 ? 20.603  -12.669 14.904  1.00   28.12  ? 127  MET A N   1 
ATOM   937  C CA  . MET A 1 127 ? 22.037  -12.647 15.217  1.00   29.14  ? 127  MET A CA  1 
ATOM   938  C C   . MET A 1 127 ? 22.916  -12.673 13.971  1.00   29.09  ? 127  MET A C   1 
ATOM   939  O O   . MET A 1 127 ? 22.705  -13.503 13.074  1.00   29.97  ? 127  MET A O   1 
ATOM   940  C CB  . MET A 1 127 ? 22.413  -13.830 16.121  1.00   29.58  ? 127  MET A CB  1 
ATOM   941  C CG  . MET A 1 127 ? 23.890  -13.858 16.485  1.00   33.09  ? 127  MET A CG  1 
ATOM   942  S SD  . MET A 1 127 ? 24.280  -14.791 17.968  1.00   43.46  ? 127  MET A SD  1 
ATOM   943  C CE  . MET A 1 127 ? 23.176  -14.004 19.153  1.00   39.49  ? 127  MET A CE  1 
ATOM   944  N N   . ASP A 1 128 ? 23.908  -11.784 13.935  0.86   28.94  ? 128  ASP A N   1 
ATOM   945  C CA  . ASP A 1 128 ? 24.891  -11.711 12.843  0.86   29.52  ? 128  ASP A CA  1 
ATOM   946  C C   . ASP A 1 128 ? 24.282  -11.849 11.453  0.86   29.69  ? 128  ASP A C   1 
ATOM   947  O O   . ASP A 1 128 ? 24.529  -12.833 10.735  0.86   29.83  ? 128  ASP A O   1 
ATOM   948  C CB  . ASP A 1 128 ? 26.018  -12.726 13.041  0.86   29.53  ? 128  ASP A CB  1 
ATOM   949  C CG  . ASP A 1 128 ? 26.803  -12.460 14.304  0.86   31.09  ? 128  ASP A CG  1 
ATOM   950  O OD1 . ASP A 1 128 ? 26.833  -13.356 15.171  0.86   32.33  ? 128  ASP A OD1 1 
ATOM   951  O OD2 . ASP A 1 128 ? 27.361  -11.344 14.437  0.86   31.21  ? 128  ASP A OD2 1 
ATOM   952  N N   . LEU A 1 129 ? 23.460  -10.870 11.099  1.00   29.58  ? 129  LEU A N   1 
ATOM   953  C CA  . LEU A 1 129 ? 22.928  -10.768 9.754   1.00   30.08  ? 129  LEU A CA  1 
ATOM   954  C C   . LEU A 1 129 ? 24.084  -10.798 8.775   1.00   30.20  ? 129  LEU A C   1 
ATOM   955  O O   . LEU A 1 129 ? 25.069  -10.075 8.958   1.00   30.09  ? 129  LEU A O   1 
ATOM   956  C CB  . LEU A 1 129 ? 22.157  -9.458  9.598   1.00   30.17  ? 129  LEU A CB  1 
ATOM   957  C CG  . LEU A 1 129 ? 20.775  -9.442  10.260  1.00   29.39  ? 129  LEU A CG  1 
ATOM   958  C CD1 . LEU A 1 129 ? 20.236  -8.022  10.303  1.00   28.72  ? 129  LEU A CD1 1 
ATOM   959  C CD2 . LEU A 1 129 ? 19.805  -10.356 9.512   1.00   28.65  ? 129  LEU A CD2 1 
ATOM   960  N N   . HIS A 1 130 ? 23.971  -11.638 7.744   1.00   30.70  ? 130  HIS A N   1 
ATOM   961  C CA  . HIS A 1 130 ? 25.018  -11.728 6.720   1.00   31.43  ? 130  HIS A CA  1 
ATOM   962  C C   . HIS A 1 130 ? 25.426  -10.328 6.261   1.00   31.37  ? 130  HIS A C   1 
ATOM   963  O O   . HIS A 1 130 ? 26.612  -10.047 6.076   1.00   31.44  ? 130  HIS A O   1 
ATOM   964  C CB  . HIS A 1 130 ? 24.575  -12.602 5.542   1.00   31.60  ? 130  HIS A CB  1 
ATOM   965  C CG  . HIS A 1 130 ? 25.558  -12.636 4.410   1.00   33.21  ? 130  HIS A CG  1 
ATOM   966  N ND1 . HIS A 1 130 ? 26.773  -13.285 4.495   1.00   33.75  ? 130  HIS A ND1 1 
ATOM   967  C CD2 . HIS A 1 130 ? 25.503  -12.104 3.165   1.00   33.64  ? 130  HIS A CD2 1 
ATOM   968  C CE1 . HIS A 1 130 ? 27.425  -13.147 3.354   1.00   34.07  ? 130  HIS A CE1 1 
ATOM   969  N NE2 . HIS A 1 130 ? 26.675  -12.438 2.529   1.00   33.49  ? 130  HIS A NE2 1 
ATOM   970  N N   . ALA A 1 131 ? 24.439  -9.449  6.114   1.00   31.22  ? 131  ALA A N   1 
ATOM   971  C CA  . ALA A 1 131 ? 24.693  -8.038  5.808   1.00   31.33  ? 131  ALA A CA  1 
ATOM   972  C C   . ALA A 1 131 ? 23.819  -7.123  6.667   1.00   31.16  ? 131  ALA A C   1 
ATOM   973  O O   . ALA A 1 131 ? 22.618  -7.344  6.805   1.00   31.21  ? 131  ALA A O   1 
ATOM   974  C CB  . ALA A 1 131 ? 24.460  -7.767  4.331   1.00   31.34  ? 131  ALA A CB  1 
ATOM   975  N N   . SER A 1 132 ? 24.439  -6.087  7.220   1.00   31.17  ? 132  SER A N   1 
ATOM   976  C CA  . SER A 1 132 ? 23.772  -5.137  8.115   1.00   31.44  ? 132  SER A CA  1 
ATOM   977  C C   . SER A 1 132 ? 22.612  -4.338  7.471   1.00   30.30  ? 132  SER A C   1 
ATOM   978  O O   . SER A 1 132 ? 21.651  -3.956  8.159   1.00   30.05  ? 132  SER A O   1 
ATOM   979  C CB  . SER A 1 132 ? 24.813  -4.186  8.715   1.00   31.74  ? 132  SER A CB  1 
ATOM   980  O OG  . SER A 1 132 ? 24.199  -3.303  9.636   1.00   35.27  ? 132  SER A OG  1 
ATOM   981  N N   . GLN A 1 133 ? 22.703  -4.103  6.161   0.90   28.53  ? 133  GLN A N   1 
ATOM   982  C CA  . GLN A 1 133 ? 21.631  -3.447  5.401   0.90   27.59  ? 133  GLN A CA  1 
ATOM   983  C C   . GLN A 1 133 ? 20.297  -4.218  5.412   0.90   27.12  ? 133  GLN A C   1 
ATOM   984  O O   . GLN A 1 133 ? 19.246  -3.635  5.148   0.90   26.80  ? 133  GLN A O   1 
ATOM   985  C CB  . GLN A 1 133 ? 22.063  -3.203  3.943   0.90   27.37  ? 133  GLN A CB  1 
ATOM   986  C CG  . GLN A 1 133 ? 23.224  -2.228  3.765   0.90   27.55  ? 133  GLN A CG  1 
ATOM   987  C CD  . GLN A 1 133 ? 24.596  -2.875  3.946   0.90   30.50  ? 133  GLN A CD  1 
ATOM   988  O OE1 . GLN A 1 133 ? 24.703  -4.057  4.281   0.90   31.68  ? 133  GLN A OE1 1 
ATOM   989  N NE2 . GLN A 1 133 ? 25.657  -2.095  3.719   0.90   30.34  ? 133  GLN A NE2 1 
ATOM   990  N N   . ILE A 1 134 ? 20.342  -5.516  5.703   1.00   26.34  ? 134  ILE A N   1 
ATOM   991  C CA  . ILE A 1 134 ? 19.114  -6.330  5.817   1.00   26.37  ? 134  ILE A CA  1 
ATOM   992  C C   . ILE A 1 134 ? 18.130  -5.750  6.845   1.00   26.14  ? 134  ILE A C   1 
ATOM   993  O O   . ILE A 1 134 ? 16.911  -5.896  6.703   1.00   25.71  ? 134  ILE A O   1 
ATOM   994  C CB  . ILE A 1 134 ? 19.433  -7.839  6.084   1.00   26.34  ? 134  ILE A CB  1 
ATOM   995  C CG1 . ILE A 1 134 ? 20.107  -8.459  4.849   1.00   26.65  ? 134  ILE A CG1 1 
ATOM   996  C CG2 . ILE A 1 134 ? 18.165  -8.625  6.477   1.00   26.33  ? 134  ILE A CG2 1 
ATOM   997  C CD1 . ILE A 1 134 ? 20.728  -9.854  5.067   1.00   25.38  ? 134  ILE A CD1 1 
ATOM   998  N N   . GLN A 1 135 ? 18.657  -5.060  7.855   1.00   25.99  ? 135  GLN A N   1 
ATOM   999  C CA  . GLN A 1 135 ? 17.805  -4.309  8.779   1.00   26.13  ? 135  GLN A CA  1 
ATOM   1000 C C   . GLN A 1 135 ? 16.909  -3.322  8.035   1.00   25.85  ? 135  GLN A C   1 
ATOM   1001 O O   . GLN A 1 135 ? 15.745  -3.111  8.408   1.00   25.50  ? 135  GLN A O   1 
ATOM   1002 C CB  . GLN A 1 135 ? 18.648  -3.536  9.787   1.00   26.78  ? 135  GLN A CB  1 
ATOM   1003 C CG  . GLN A 1 135 ? 19.313  -4.390  10.857  1.00   28.61  ? 135  GLN A CG  1 
ATOM   1004 C CD  . GLN A 1 135 ? 19.622  -3.565  12.101  1.00   32.99  ? 135  GLN A CD  1 
ATOM   1005 O OE1 . GLN A 1 135 ? 18.747  -2.883  12.632  1.00   36.01  ? 135  GLN A OE1 1 
ATOM   1006 N NE2 . GLN A 1 135 ? 20.869  -3.599  12.550  1.00   34.42  ? 135  GLN A NE2 1 
ATOM   1007 N N   . GLY A 1 136 ? 17.452  -2.714  6.985   1.00   25.14  ? 136  GLY A N   1 
ATOM   1008 C CA  . GLY A 1 136 ? 16.679  -1.752  6.198   1.00   24.71  ? 136  GLY A CA  1 
ATOM   1009 C C   . GLY A 1 136 ? 15.664  -2.388  5.264   1.00   24.01  ? 136  GLY A C   1 
ATOM   1010 O O   . GLY A 1 136 ? 14.903  -1.680  4.621   1.00   23.89  ? 136  GLY A O   1 
ATOM   1011 N N   . PHE A 1 137 ? 15.651  -3.720  5.177   1.00   23.31  ? 137  PHE A N   1 
ATOM   1012 C CA  . PHE A 1 137 ? 14.645  -4.415  4.377   1.00   23.07  ? 137  PHE A CA  1 
ATOM   1013 C C   . PHE A 1 137 ? 13.276  -4.390  5.074   1.00   23.55  ? 137  PHE A C   1 
ATOM   1014 O O   . PHE A 1 137 ? 12.256  -4.678  4.448   1.00   22.88  ? 137  PHE A O   1 
ATOM   1015 C CB  . PHE A 1 137 ? 15.073  -5.863  4.084   1.00   23.18  ? 137  PHE A CB  1 
ATOM   1016 C CG  . PHE A 1 137 ? 16.225  -5.986  3.099   1.00   22.06  ? 137  PHE A CG  1 
ATOM   1017 C CD1 . PHE A 1 137 ? 16.652  -7.219  2.690   1.00   21.08  ? 137  PHE A CD1 1 
ATOM   1018 C CD2 . PHE A 1 137 ? 16.846  -4.855  2.559   1.00   22.82  ? 137  PHE A CD2 1 
ATOM   1019 C CE1 . PHE A 1 137 ? 17.717  -7.347  1.773   1.00   24.16  ? 137  PHE A CE1 1 
ATOM   1020 C CE2 . PHE A 1 137 ? 17.890  -4.967  1.666   1.00   20.45  ? 137  PHE A CE2 1 
ATOM   1021 C CZ  . PHE A 1 137 ? 18.324  -6.216  1.264   1.00   22.66  ? 137  PHE A CZ  1 
ATOM   1022 N N   . PHE A 1 138 ? 13.272  -4.019  6.361   1.00   23.47  ? 138  PHE A N   1 
ATOM   1023 C CA  . PHE A 1 138 ? 12.060  -3.910  7.182   1.00   24.29  ? 138  PHE A CA  1 
ATOM   1024 C C   . PHE A 1 138 ? 11.706  -2.454  7.451   1.00   25.25  ? 138  PHE A C   1 
ATOM   1025 O O   . PHE A 1 138 ? 12.577  -1.593  7.382   1.00   25.93  ? 138  PHE A O   1 
ATOM   1026 C CB  . PHE A 1 138 ? 12.297  -4.567  8.555   1.00   23.38  ? 138  PHE A CB  1 
ATOM   1027 C CG  . PHE A 1 138 ? 12.469  -6.052  8.494   1.00   22.37  ? 138  PHE A CG  1 
ATOM   1028 C CD1 . PHE A 1 138 ? 13.721  -6.613  8.273   1.00   20.86  ? 138  PHE A CD1 1 
ATOM   1029 C CD2 . PHE A 1 138 ? 11.368  -6.888  8.636   1.00   20.95  ? 138  PHE A CD2 1 
ATOM   1030 C CE1 . PHE A 1 138 ? 13.881  -7.998  8.220   1.00   20.49  ? 138  PHE A CE1 1 
ATOM   1031 C CE2 . PHE A 1 138 ? 11.512  -8.280  8.578   1.00   20.67  ? 138  PHE A CE2 1 
ATOM   1032 C CZ  . PHE A 1 138 ? 12.769  -8.832  8.380   1.00   18.72  ? 138  PHE A CZ  1 
ATOM   1033 N N   . ASP A 1 139 ? 10.442  -2.196  7.778   1.00   25.94  ? 139  ASP A N   1 
ATOM   1034 C CA  . ASP A 1 139 ? 10.031  -0.922  8.389   1.00   27.28  ? 139  ASP A CA  1 
ATOM   1035 C C   . ASP A 1 139 ? 9.778   -1.091  9.901   1.00   27.01  ? 139  ASP A C   1 
ATOM   1036 O O   . ASP A 1 139 ? 9.594   -0.117  10.627  1.00   28.18  ? 139  ASP A O   1 
ATOM   1037 C CB  . ASP A 1 139 ? 8.799   -0.330  7.686   1.00   27.78  ? 139  ASP A CB  1 
ATOM   1038 C CG  . ASP A 1 139 ? 9.081   0.060   6.214   1.00   30.03  ? 139  ASP A CG  1 
ATOM   1039 O OD1 . ASP A 1 139 ? 10.171  0.578   5.909   1.00   32.06  ? 139  ASP A OD1 1 
ATOM   1040 O OD2 . ASP A 1 139 ? 8.206   -0.144  5.363   1.00   33.64  ? 139  ASP A OD2 1 
ATOM   1041 N N   . ILE A 1 140 ? 9.772   -2.331  10.364  1.00   26.53  ? 140  ILE A N   1 
ATOM   1042 C CA  . ILE A 1 140 ? 9.630   -2.631  11.792  1.00   25.72  ? 140  ILE A CA  1 
ATOM   1043 C C   . ILE A 1 140 ? 11.013  -2.666  12.416  1.00   25.39  ? 140  ILE A C   1 
ATOM   1044 O O   . ILE A 1 140 ? 11.998  -2.894  11.711  1.00   24.93  ? 140  ILE A O   1 
ATOM   1045 C CB  . ILE A 1 140 ? 8.889   -3.985  12.032  1.00   25.42  ? 140  ILE A CB  1 
ATOM   1046 C CG1 . ILE A 1 140 ? 9.645   -5.139  11.348  1.00   24.76  ? 140  ILE A CG1 1 
ATOM   1047 C CG2 . ILE A 1 140 ? 7.431   -3.865  11.574  1.00   26.03  ? 140  ILE A CG2 1 
ATOM   1048 C CD1 . ILE A 1 140 ? 9.068   -6.528  11.593  1.00   25.52  ? 140  ILE A CD1 1 
ATOM   1049 N N   . PRO A 1 141 ? 11.101  -2.434  13.743  1.00   25.74  ? 141  PRO A N   1 
ATOM   1050 C CA  . PRO A 1 141 ? 12.419  -2.490  14.382  1.00   25.31  ? 141  PRO A CA  1 
ATOM   1051 C C   . PRO A 1 141 ? 13.044  -3.877  14.292  1.00   25.13  ? 141  PRO A C   1 
ATOM   1052 O O   . PRO A 1 141 ? 12.342  -4.888  14.424  1.00   24.23  ? 141  PRO A O   1 
ATOM   1053 C CB  . PRO A 1 141 ? 12.133  -2.149  15.848  1.00   25.09  ? 141  PRO A CB  1 
ATOM   1054 C CG  . PRO A 1 141 ? 10.790  -1.546  15.873  1.00   26.47  ? 141  PRO A CG  1 
ATOM   1055 C CD  . PRO A 1 141 ? 10.031  -2.069  14.692  1.00   25.52  ? 141  PRO A CD  1 
ATOM   1056 N N   . VAL A 1 142 ? 14.353  -3.899  14.046  1.00   25.29  ? 142  VAL A N   1 
ATOM   1057 C CA  . VAL A 1 142 ? 15.166  -5.111  14.063  1.00   25.88  ? 142  VAL A CA  1 
ATOM   1058 C C   . VAL A 1 142 ? 16.322  -4.920  15.054  1.00   26.89  ? 142  VAL A C   1 
ATOM   1059 O O   . VAL A 1 142 ? 17.044  -3.921  14.985  1.00   26.92  ? 142  VAL A O   1 
ATOM   1060 C CB  . VAL A 1 142 ? 15.766  -5.423  12.658  1.00   26.17  ? 142  VAL A CB  1 
ATOM   1061 C CG1 . VAL A 1 142 ? 16.544  -6.754  12.662  1.00   25.37  ? 142  VAL A CG1 1 
ATOM   1062 C CG2 . VAL A 1 142 ? 14.678  -5.451  11.588  1.00   24.77  ? 142  VAL A CG2 1 
ATOM   1063 N N   . ASP A 1 143 ? 16.485  -5.870  15.975  0.97   27.34  ? 143  ASP A N   1 
ATOM   1064 C CA  . ASP A 1 143 ? 17.681  -5.924  16.812  0.97   28.20  ? 143  ASP A CA  1 
ATOM   1065 C C   . ASP A 1 143 ? 18.591  -7.044  16.330  0.97   28.40  ? 143  ASP A C   1 
ATOM   1066 O O   . ASP A 1 143 ? 18.217  -8.221  16.360  0.97   27.81  ? 143  ASP A O   1 
ATOM   1067 C CB  . ASP A 1 143 ? 17.330  -6.098  18.290  0.97   28.78  ? 143  ASP A CB  1 
ATOM   1068 C CG  . ASP A 1 143 ? 16.543  -4.915  18.840  0.97   29.13  ? 143  ASP A CG  1 
ATOM   1069 O OD1 . ASP A 1 143 ? 16.991  -3.766  18.683  0.97   31.94  ? 143  ASP A OD1 1 
ATOM   1070 O OD2 . ASP A 1 143 ? 15.471  -5.132  19.426  0.97   32.42  ? 143  ASP A OD2 1 
ATOM   1071 N N   . ASN A 1 144 ? 19.771  -6.644  15.868  1.00   28.21  ? 144  ASN A N   1 
ATOM   1072 C CA  . ASN A 1 144 ? 20.771  -7.541  15.312  1.00   29.35  ? 144  ASN A CA  1 
ATOM   1073 C C   . ASN A 1 144 ? 21.883  -7.793  16.328  1.00   30.24  ? 144  ASN A C   1 
ATOM   1074 O O   . ASN A 1 144 ? 22.794  -6.972  16.476  1.00   29.64  ? 144  ASN A O   1 
ATOM   1075 C CB  . ASN A 1 144 ? 21.353  -6.932  14.031  1.00   29.02  ? 144  ASN A CB  1 
ATOM   1076 C CG  . ASN A 1 144 ? 22.370  -7.847  13.345  1.00   30.28  ? 144  ASN A CG  1 
ATOM   1077 O OD1 . ASN A 1 144 ? 22.203  -9.070  13.287  1.00   30.48  ? 144  ASN A OD1 1 
ATOM   1078 N ND2 . ASN A 1 144 ? 23.432  -7.247  12.824  1.00   29.38  ? 144  ASN A ND2 1 
ATOM   1079 N N   . LEU A 1 145 ? 21.787  -8.916  17.037  1.00   31.10  ? 145  LEU A N   1 
ATOM   1080 C CA  . LEU A 1 145 ? 22.763  -9.292  18.057  1.00   32.77  ? 145  LEU A CA  1 
ATOM   1081 C C   . LEU A 1 145 ? 24.094  -9.767  17.465  1.00   34.08  ? 145  LEU A C   1 
ATOM   1082 O O   . LEU A 1 145 ? 24.150  -10.197 16.302  1.00   34.20  ? 145  LEU A O   1 
ATOM   1083 C CB  . LEU A 1 145 ? 22.177  -10.364 18.976  1.00   32.85  ? 145  LEU A CB  1 
ATOM   1084 C CG  . LEU A 1 145 ? 20.816  -10.025 19.592  1.00   33.37  ? 145  LEU A CG  1 
ATOM   1085 C CD1 . LEU A 1 145 ? 20.222  -11.231 20.263  1.00   34.24  ? 145  LEU A CD1 1 
ATOM   1086 C CD2 . LEU A 1 145 ? 20.937  -8.859  20.571  1.00   33.54  ? 145  LEU A CD2 1 
ATOM   1087 N N   . TYR A 1 146 ? 25.162  -9.690  18.267  1.00   35.59  ? 146  TYR A N   1 
ATOM   1088 C CA  . TYR A 1 146 ? 26.501  -10.069 17.796  1.00   37.12  ? 146  TYR A CA  1 
ATOM   1089 C C   . TYR A 1 146 ? 27.078  -11.237 18.563  1.00   37.56  ? 146  TYR A C   1 
ATOM   1090 O O   . TYR A 1 146 ? 27.009  -11.287 19.794  1.00   37.59  ? 146  TYR A O   1 
ATOM   1091 C CB  . TYR A 1 146 ? 27.471  -8.887  17.871  1.00   37.63  ? 146  TYR A CB  1 
ATOM   1092 C CG  . TYR A 1 146 ? 26.977  -7.688  17.113  1.00   40.29  ? 146  TYR A CG  1 
ATOM   1093 C CD1 . TYR A 1 146 ? 26.416  -6.604  17.788  1.00   43.00  ? 146  TYR A CD1 1 
ATOM   1094 C CD2 . TYR A 1 146 ? 27.028  -7.650  15.720  1.00   42.10  ? 146  TYR A CD2 1 
ATOM   1095 C CE1 . TYR A 1 146 ? 25.929  -5.509  17.100  1.00   44.35  ? 146  TYR A CE1 1 
ATOM   1096 C CE2 . TYR A 1 146 ? 26.544  -6.550  15.016  1.00   44.40  ? 146  TYR A CE2 1 
ATOM   1097 C CZ  . TYR A 1 146 ? 25.997  -5.488  15.714  1.00   45.01  ? 146  TYR A CZ  1 
ATOM   1098 O OH  . TYR A 1 146 ? 25.520  -4.393  15.036  1.00   47.48  ? 146  TYR A OH  1 
ATOM   1099 N N   . ALA A 1 147 ? 27.654  -12.175 17.823  1.00   38.19  ? 147  ALA A N   1 
ATOM   1100 C CA  . ALA A 1 147 ? 28.384  -13.274 18.424  1.00   38.82  ? 147  ALA A CA  1 
ATOM   1101 C C   . ALA A 1 147 ? 29.790  -12.800 18.780  1.00   39.28  ? 147  ALA A C   1 
ATOM   1102 O O   . ALA A 1 147 ? 30.473  -13.430 19.583  1.00   39.38  ? 147  ALA A O   1 
ATOM   1103 C CB  . ALA A 1 147 ? 28.449  -14.453 17.467  1.00   38.92  ? 147  ALA A CB  1 
ATOM   1104 N N   . GLU A 1 148 ? 30.189  -11.679 18.186  1.00   39.54  ? 148  GLU A N   1 
ATOM   1105 C CA  . GLU A 1 148 ? 31.538  -11.141 18.290  1.00   40.68  ? 148  GLU A CA  1 
ATOM   1106 C C   . GLU A 1 148 ? 32.136  -11.184 19.709  1.00   40.55  ? 148  GLU A C   1 
ATOM   1107 O O   . GLU A 1 148 ? 33.206  -11.769 19.888  1.00   40.99  ? 148  GLU A O   1 
ATOM   1108 C CB  . GLU A 1 148 ? 31.605  -9.727  17.699  1.00   40.90  ? 148  GLU A CB  1 
ATOM   1109 C CG  . GLU A 1 148 ? 33.024  -9.210  17.512  1.00   44.01  ? 148  GLU A CG  1 
ATOM   1110 C CD  . GLU A 1 148 ? 33.083  -7.765  17.034  1.00   47.28  ? 148  GLU A CD  1 
ATOM   1111 O OE1 . GLU A 1 148 ? 32.036  -7.200  16.650  1.00   49.51  ? 148  GLU A OE1 1 
ATOM   1112 O OE2 . GLU A 1 148 ? 34.195  -7.196  17.037  1.00   49.09  ? 148  GLU A OE2 1 
ATOM   1113 N N   . PRO A 1 149 ? 31.449  -10.591 20.713  1.00   40.48  ? 149  PRO A N   1 
ATOM   1114 C CA  . PRO A 1 149 ? 32.000  -10.618 22.075  1.00   40.52  ? 149  PRO A CA  1 
ATOM   1115 C C   . PRO A 1 149 ? 32.254  -12.031 22.610  1.00   40.59  ? 149  PRO A C   1 
ATOM   1116 O O   . PRO A 1 149 ? 33.225  -12.233 23.345  1.00   40.47  ? 149  PRO A O   1 
ATOM   1117 C CB  . PRO A 1 149 ? 30.918  -9.923  22.908  1.00   40.66  ? 149  PRO A CB  1 
ATOM   1118 C CG  . PRO A 1 149 ? 30.168  -9.070  21.921  1.00   40.79  ? 149  PRO A CG  1 
ATOM   1119 C CD  . PRO A 1 149 ? 30.166  -9.860  20.663  1.00   40.30  ? 149  PRO A CD  1 
ATOM   1120 N N   . ALA A 1 150 ? 31.408  -12.993 22.230  1.00   39.97  ? 150  ALA A N   1 
ATOM   1121 C CA  . ALA A 1 150 ? 31.567  -14.378 22.661  1.00   39.76  ? 150  ALA A CA  1 
ATOM   1122 C C   . ALA A 1 150 ? 32.665  -15.104 21.879  1.00   39.88  ? 150  ALA A C   1 
ATOM   1123 O O   . ALA A 1 150 ? 33.267  -16.061 22.384  1.00   39.41  ? 150  ALA A O   1 
ATOM   1124 C CB  . ALA A 1 150 ? 30.248  -15.128 22.550  1.00   40.05  ? 150  ALA A CB  1 
ATOM   1125 N N   . VAL A 1 151 ? 32.916  -14.649 20.650  1.00   39.38  ? 151  VAL A N   1 
ATOM   1126 C CA  . VAL A 1 151 ? 33.985  -15.204 19.817  1.00   39.65  ? 151  VAL A CA  1 
ATOM   1127 C C   . VAL A 1 151 ? 35.365  -14.774 20.336  1.00   39.92  ? 151  VAL A C   1 
ATOM   1128 O O   . VAL A 1 151 ? 36.308  -15.569 20.343  1.00   39.94  ? 151  VAL A O   1 
ATOM   1129 C CB  . VAL A 1 151 ? 33.834  -14.775 18.339  1.00   39.46  ? 151  VAL A CB  1 
ATOM   1130 C CG1 . VAL A 1 151 ? 35.077  -15.132 17.530  1.00   39.40  ? 151  VAL A CG1 1 
ATOM   1131 C CG2 . VAL A 1 151 ? 32.588  -15.409 17.712  1.00   39.41  ? 151  VAL A CG2 1 
ATOM   1132 N N   . LEU A 1 152 ? 35.461  -13.512 20.754  1.00   40.20  ? 152  LEU A N   1 
ATOM   1133 C CA  . LEU A 1 152 ? 36.704  -12.919 21.229  1.00   40.75  ? 152  LEU A CA  1 
ATOM   1134 C C   . LEU A 1 152 ? 37.103  -13.527 22.560  1.00   41.23  ? 152  LEU A C   1 
ATOM   1135 O O   . LEU A 1 152 ? 38.277  -13.837 22.778  1.00   41.55  ? 152  LEU A O   1 
ATOM   1136 C CB  . LEU A 1 152 ? 36.557  -11.409 21.360  1.00   40.57  ? 152  LEU A CB  1 
ATOM   1137 C CG  . LEU A 1 152 ? 37.017  -10.486 20.221  1.00   41.31  ? 152  LEU A CG  1 
ATOM   1138 C CD1 . LEU A 1 152 ? 36.817  -11.074 18.835  1.00   41.11  ? 152  LEU A CD1 1 
ATOM   1139 C CD2 . LEU A 1 152 ? 36.282  -9.165  20.349  1.00   41.21  ? 152  LEU A CD2 1 
ATOM   1140 N N   . LYS A 1 153 ? 36.113  -13.703 23.436  0.89   41.55  ? 153  LYS A N   1 
ATOM   1141 C CA  . LYS A 1 153 ? 36.301  -14.414 24.691  0.89   41.73  ? 153  LYS A CA  1 
ATOM   1142 C C   . LYS A 1 153 ? 36.891  -15.799 24.442  0.89   41.79  ? 153  LYS A C   1 
ATOM   1143 O O   . LYS A 1 153 ? 37.890  -16.159 25.072  0.89   42.05  ? 153  LYS A O   1 
ATOM   1144 C CB  . LYS A 1 153 ? 34.978  -14.511 25.460  0.89   41.98  ? 153  LYS A CB  1 
ATOM   1145 C CG  . LYS A 1 153 ? 35.113  -15.076 26.865  0.89   42.74  ? 153  LYS A CG  1 
ATOM   1146 C CD  . LYS A 1 153 ? 33.797  -14.991 27.625  0.89   44.70  ? 153  LYS A CD  1 
ATOM   1147 C CE  . LYS A 1 153 ? 33.944  -15.496 29.065  0.89   45.64  ? 153  LYS A CE  1 
ATOM   1148 N NZ  . LYS A 1 153 ? 34.240  -16.962 29.138  0.89   46.20  ? 153  LYS A NZ  1 
ATOM   1149 N N   . TRP A 1 154 ? 36.292  -16.554 23.513  1.00   41.63  ? 154  TRP A N   1 
ATOM   1150 C CA  . TRP A 1 154 ? 36.726  -17.921 23.203  1.00   41.65  ? 154  TRP A CA  1 
ATOM   1151 C C   . TRP A 1 154 ? 38.140  -17.983 22.624  1.00   42.12  ? 154  TRP A C   1 
ATOM   1152 O O   . TRP A 1 154 ? 38.909  -18.890 22.952  1.00   41.87  ? 154  TRP A O   1 
ATOM   1153 C CB  . TRP A 1 154 ? 35.744  -18.610 22.242  1.00   41.47  ? 154  TRP A CB  1 
ATOM   1154 C CG  . TRP A 1 154 ? 35.971  -20.098 22.090  1.00   40.06  ? 154  TRP A CG  1 
ATOM   1155 C CD1 . TRP A 1 154 ? 35.280  -21.090 22.717  1.00   39.34  ? 154  TRP A CD1 1 
ATOM   1156 C CD2 . TRP A 1 154 ? 36.945  -20.755 21.254  1.00   39.21  ? 154  TRP A CD2 1 
ATOM   1157 N NE1 . TRP A 1 154 ? 35.757  -22.321 22.329  1.00   38.97  ? 154  TRP A NE1 1 
ATOM   1158 C CE2 . TRP A 1 154 ? 36.781  -22.144 21.438  1.00   38.93  ? 154  TRP A CE2 1 
ATOM   1159 C CE3 . TRP A 1 154 ? 37.940  -20.303 20.375  1.00   38.71  ? 154  TRP A CE3 1 
ATOM   1160 C CZ2 . TRP A 1 154 ? 37.580  -23.089 20.782  1.00   39.68  ? 154  TRP A CZ2 1 
ATOM   1161 C CZ3 . TRP A 1 154 ? 38.732  -21.242 19.718  1.00   38.74  ? 154  TRP A CZ3 1 
ATOM   1162 C CH2 . TRP A 1 154 ? 38.544  -22.619 19.924  1.00   39.64  ? 154  TRP A CH2 1 
ATOM   1163 N N   . ILE A 1 155 ? 38.465  -17.043 21.737  1.00   42.76  ? 155  ILE A N   1 
ATOM   1164 C CA  . ILE A 1 155 ? 39.810  -16.948 21.165  1.00   43.01  ? 155  ILE A CA  1 
ATOM   1165 C C   . ILE A 1 155 ? 40.869  -16.808 22.268  1.00   43.78  ? 155  ILE A C   1 
ATOM   1166 O O   . ILE A 1 155 ? 41.813  -17.593 22.324  1.00   43.65  ? 155  ILE A O   1 
ATOM   1167 C CB  . ILE A 1 155 ? 39.931  -15.797 20.131  1.00   42.95  ? 155  ILE A CB  1 
ATOM   1168 C CG1 . ILE A 1 155 ? 39.127  -16.128 18.866  1.00   42.43  ? 155  ILE A CG1 1 
ATOM   1169 C CG2 . ILE A 1 155 ? 41.399  -15.540 19.772  1.00   42.49  ? 155  ILE A CG2 1 
ATOM   1170 C CD1 . ILE A 1 155 ? 39.055  -14.987 17.844  1.00   39.64  ? 155  ILE A CD1 1 
ATOM   1171 N N   . ARG A 1 156 ? 40.690  -15.826 23.148  1.00   44.95  ? 156  ARG A N   1 
ATOM   1172 C CA  . ARG A 1 156 ? 41.645  -15.568 24.231  1.00   46.17  ? 156  ARG A CA  1 
ATOM   1173 C C   . ARG A 1 156 ? 41.772  -16.767 25.170  1.00   46.75  ? 156  ARG A C   1 
ATOM   1174 O O   . ARG A 1 156 ? 42.876  -17.105 25.614  1.00   46.75  ? 156  ARG A O   1 
ATOM   1175 C CB  . ARG A 1 156 ? 41.222  -14.345 25.047  1.00   46.38  ? 156  ARG A CB  1 
ATOM   1176 C CG  . ARG A 1 156 ? 41.271  -13.014 24.327  1.00   47.57  ? 156  ARG A CG  1 
ATOM   1177 C CD  . ARG A 1 156 ? 40.698  -11.936 25.237  1.00   50.36  ? 156  ARG A CD  1 
ATOM   1178 N NE  . ARG A 1 156 ? 40.700  -10.606 24.624  1.00   52.65  ? 156  ARG A NE  1 
ATOM   1179 C CZ  . ARG A 1 156 ? 39.607  -9.930  24.267  1.00   53.20  ? 156  ARG A CZ  1 
ATOM   1180 N NH1 . ARG A 1 156 ? 38.395  -10.445 24.456  1.00   53.38  ? 156  ARG A NH1 1 
ATOM   1181 N NH2 . ARG A 1 156 ? 39.728  -8.726  23.721  1.00   53.59  ? 156  ARG A NH2 1 
ATOM   1182 N N   . GLU A 1 157 ? 40.635  -17.407 25.453  1.00   47.30  ? 157  GLU A N   1 
ATOM   1183 C CA  . GLU A 1 157 ? 40.561  -18.486 26.441  1.00   48.03  ? 157  GLU A CA  1 
ATOM   1184 C C   . GLU A 1 157 ? 40.909  -19.868 25.883  1.00   48.18  ? 157  GLU A C   1 
ATOM   1185 O O   . GLU A 1 157 ? 40.934  -20.855 26.634  1.00   48.93  ? 157  GLU A O   1 
ATOM   1186 C CB  . GLU A 1 157 ? 39.173  -18.510 27.101  1.00   48.20  ? 157  GLU A CB  1 
ATOM   1187 C CG  . GLU A 1 157 ? 38.907  -17.311 28.019  1.00   50.37  ? 157  GLU A CG  1 
ATOM   1188 C CD  . GLU A 1 157 ? 37.492  -17.268 28.594  1.00   53.14  ? 157  GLU A CD  1 
ATOM   1189 O OE1 . GLU A 1 157 ? 37.206  -16.327 29.377  1.00   53.32  ? 157  GLU A OE1 1 
ATOM   1190 O OE2 . GLU A 1 157 ? 36.665  -18.154 28.263  1.00   53.82  ? 157  GLU A OE2 1 
ATOM   1191 N N   . ASN A 1 158 ? 41.178  -19.953 24.580  1.00   47.87  ? 158  ASN A N   1 
ATOM   1192 C CA  . ASN A 1 158 ? 41.431  -21.252 23.958  1.00   47.84  ? 158  ASN A CA  1 
ATOM   1193 C C   . ASN A 1 158 ? 42.634  -21.336 23.028  1.00   47.68  ? 158  ASN A C   1 
ATOM   1194 O O   . ASN A 1 158 ? 43.078  -22.434 22.689  1.00   47.77  ? 158  ASN A O   1 
ATOM   1195 C CB  . ASN A 1 158 ? 40.177  -21.766 23.243  1.00   47.99  ? 158  ASN A CB  1 
ATOM   1196 C CG  . ASN A 1 158 ? 39.053  -22.083 24.205  1.00   48.27  ? 158  ASN A CG  1 
ATOM   1197 O OD1 . ASN A 1 158 ? 38.370  -21.186 24.709  1.00   49.34  ? 158  ASN A OD1 1 
ATOM   1198 N ND2 . ASN A 1 158 ? 38.851  -23.365 24.465  1.00   48.96  ? 158  ASN A ND2 1 
ATOM   1199 N N   . ILE A 1 159 ? 43.152  -20.184 22.613  1.00   47.67  ? 159  ILE A N   1 
ATOM   1200 C CA  . ILE A 1 159 ? 44.309  -20.138 21.720  1.00   47.73  ? 159  ILE A CA  1 
ATOM   1201 C C   . ILE A 1 159 ? 45.469  -19.470 22.457  1.00   47.74  ? 159  ILE A C   1 
ATOM   1202 O O   . ILE A 1 159 ? 45.472  -18.249 22.648  1.00   47.27  ? 159  ILE A O   1 
ATOM   1203 C CB  . ILE A 1 159 ? 43.970  -19.410 20.383  1.00   47.90  ? 159  ILE A CB  1 
ATOM   1204 C CG1 . ILE A 1 159 ? 42.726  -20.050 19.744  1.00   48.37  ? 159  ILE A CG1 1 
ATOM   1205 C CG2 . ILE A 1 159 ? 45.168  -19.426 19.429  1.00   47.54  ? 159  ILE A CG2 1 
ATOM   1206 C CD1 . ILE A 1 159 ? 42.294  -19.451 18.413  1.00   48.59  ? 159  ILE A CD1 1 
ATOM   1207 N N   . SER A 1 160 ? 46.434  -20.281 22.901  1.00   48.00  ? 160  SER A N   1 
ATOM   1208 C CA  . SER A 1 160 ? 47.550  -19.770 23.710  1.00   48.31  ? 160  SER A CA  1 
ATOM   1209 C C   . SER A 1 160 ? 48.319  -18.650 23.003  1.00   48.44  ? 160  SER A C   1 
ATOM   1210 O O   . SER A 1 160 ? 48.655  -17.634 23.621  1.00   48.25  ? 160  SER A O   1 
ATOM   1211 C CB  . SER A 1 160 ? 48.492  -20.897 24.176  1.00   48.30  ? 160  SER A CB  1 
ATOM   1212 O OG  . SER A 1 160 ? 48.992  -21.678 23.093  1.00   48.73  ? 160  SER A OG  1 
ATOM   1213 N N   . GLU A 1 161 ? 48.550  -18.826 21.704  0.97   48.71  ? 161  GLU A N   1 
ATOM   1214 C CA  . GLU A 1 161 ? 49.308  -17.863 20.904  0.97   49.34  ? 161  GLU A CA  1 
ATOM   1215 C C   . GLU A 1 161 ? 48.409  -16.834 20.201  0.97   49.22  ? 161  GLU A C   1 
ATOM   1216 O O   . GLU A 1 161 ? 48.677  -16.451 19.060  0.97   49.34  ? 161  GLU A O   1 
ATOM   1217 C CB  . GLU A 1 161 ? 50.176  -18.592 19.864  0.97   49.57  ? 161  GLU A CB  1 
ATOM   1218 C CG  . GLU A 1 161 ? 50.771  -19.931 20.319  0.97   51.14  ? 161  GLU A CG  1 
ATOM   1219 C CD  . GLU A 1 161 ? 49.853  -21.120 20.036  0.97   53.35  ? 161  GLU A CD  1 
ATOM   1220 O OE1 . GLU A 1 161 ? 48.617  -20.996 20.231  0.97   54.19  ? 161  GLU A OE1 1 
ATOM   1221 O OE2 . GLU A 1 161 ? 50.369  -22.191 19.619  0.97   54.42  ? 161  GLU A OE2 1 
ATOM   1222 N N   . TRP A 1 162 ? 47.350  -16.385 20.877  1.00   48.92  ? 162  TRP A N   1 
ATOM   1223 C CA  . TRP A 1 162 ? 46.380  -15.481 20.252  1.00   48.61  ? 162  TRP A CA  1 
ATOM   1224 C C   . TRP A 1 162 ? 46.902  -14.054 20.084  1.00   48.63  ? 162  TRP A C   1 
ATOM   1225 O O   . TRP A 1 162 ? 46.509  -13.345 19.143  1.00   48.62  ? 162  TRP A O   1 
ATOM   1226 C CB  . TRP A 1 162 ? 45.036  -15.480 21.004  1.00   48.26  ? 162  TRP A CB  1 
ATOM   1227 C CG  . TRP A 1 162 ? 45.035  -14.781 22.347  1.00   47.20  ? 162  TRP A CG  1 
ATOM   1228 C CD1 . TRP A 1 162 ? 45.215  -15.362 23.571  1.00   46.55  ? 162  TRP A CD1 1 
ATOM   1229 C CD2 . TRP A 1 162 ? 44.816  -13.382 22.598  1.00   46.14  ? 162  TRP A CD2 1 
ATOM   1230 N NE1 . TRP A 1 162 ? 45.125  -14.419 24.566  1.00   45.49  ? 162  TRP A NE1 1 
ATOM   1231 C CE2 . TRP A 1 162 ? 44.885  -13.195 23.997  1.00   45.92  ? 162  TRP A CE2 1 
ATOM   1232 C CE3 . TRP A 1 162 ? 44.573  -12.269 21.776  1.00   46.30  ? 162  TRP A CE3 1 
ATOM   1233 C CZ2 . TRP A 1 162 ? 44.721  -11.938 24.596  1.00   46.71  ? 162  TRP A CZ2 1 
ATOM   1234 C CZ3 . TRP A 1 162 ? 44.409  -11.020 22.370  1.00   46.17  ? 162  TRP A CZ3 1 
ATOM   1235 C CH2 . TRP A 1 162 ? 44.486  -10.866 23.768  1.00   46.65  ? 162  TRP A CH2 1 
ATOM   1236 N N   . ARG A 1 163 ? 47.781  -13.639 20.994  1.00   48.33  ? 163  ARG A N   1 
ATOM   1237 C CA  . ARG A 1 163 ? 48.299  -12.268 20.998  1.00   48.09  ? 163  ARG A CA  1 
ATOM   1238 C C   . ARG A 1 163 ? 49.107  -11.910 19.747  1.00   47.95  ? 163  ARG A C   1 
ATOM   1239 O O   . ARG A 1 163 ? 49.291  -10.726 19.439  1.00   47.93  ? 163  ARG A O   1 
ATOM   1240 C CB  . ARG A 1 163 ? 49.087  -11.984 22.279  1.00   48.19  ? 163  ARG A CB  1 
ATOM   1241 C CG  . ARG A 1 163 ? 48.194  -11.841 23.501  1.00   47.90  ? 163  ARG A CG  1 
ATOM   1242 C CD  . ARG A 1 163 ? 48.989  -11.642 24.771  1.00   47.82  ? 163  ARG A CD  1 
ATOM   1243 N NE  . ARG A 1 163 ? 48.148  -11.797 25.960  1.00   47.44  ? 163  ARG A NE  1 
ATOM   1244 C CZ  . ARG A 1 163 ? 47.441  -10.816 26.522  1.00   46.80  ? 163  ARG A CZ  1 
ATOM   1245 N NH1 . ARG A 1 163 ? 47.467  -9.584  26.020  1.00   45.20  ? 163  ARG A NH1 1 
ATOM   1246 N NH2 . ARG A 1 163 ? 46.709  -11.071 27.600  1.00   47.69  ? 163  ARG A NH2 1 
ATOM   1247 N N   . ASN A 1 164 ? 49.556  -12.932 19.018  0.97   47.76  ? 164  ASN A N   1 
ATOM   1248 C CA  . ASN A 1 164 ? 50.280  -12.727 17.764  0.97   47.69  ? 164  ASN A CA  1 
ATOM   1249 C C   . ASN A 1 164 ? 49.745  -13.552 16.584  0.97   47.27  ? 164  ASN A C   1 
ATOM   1250 O O   . ASN A 1 164 ? 50.499  -13.893 15.671  0.97   47.50  ? 164  ASN A O   1 
ATOM   1251 C CB  . ASN A 1 164 ? 51.791  -12.969 17.961  0.97   48.21  ? 164  ASN A CB  1 
ATOM   1252 C CG  . ASN A 1 164 ? 52.434  -11.964 18.912  0.97   48.87  ? 164  ASN A CG  1 
ATOM   1253 O OD1 . ASN A 1 164 ? 53.120  -12.347 19.860  0.97   51.83  ? 164  ASN A OD1 1 
ATOM   1254 N ND2 . ASN A 1 164 ? 52.211  -10.676 18.663  0.97   49.72  ? 164  ASN A ND2 1 
ATOM   1255 N N   . CYS A 1 165 ? 48.446  -13.855 16.589  1.00   46.53  ? 165  CYS A N   1 
ATOM   1256 C CA  . CYS A 1 165 ? 47.842  -14.638 15.505  1.00   45.97  ? 165  CYS A CA  1 
ATOM   1257 C C   . CYS A 1 165 ? 47.320  -13.740 14.370  1.00   45.30  ? 165  CYS A C   1 
ATOM   1258 O O   . CYS A 1 165 ? 47.463  -12.516 14.426  1.00   45.63  ? 165  CYS A O   1 
ATOM   1259 C CB  . CYS A 1 165 ? 46.716  -15.521 16.047  1.00   45.97  ? 165  CYS A CB  1 
ATOM   1260 S SG  . CYS A 1 165 ? 45.154  -14.639 16.294  1.00   46.49  ? 165  CYS A SG  1 
ATOM   1261 N N   . THR A 1 166 ? 46.717  -14.352 13.352  1.00   44.40  ? 166  THR A N   1 
ATOM   1262 C CA  . THR A 1 166 ? 46.120  -13.608 12.239  1.00   43.48  ? 166  THR A CA  1 
ATOM   1263 C C   . THR A 1 166 ? 44.688  -14.059 11.927  1.00   42.73  ? 166  THR A C   1 
ATOM   1264 O O   . THR A 1 166 ? 44.439  -15.237 11.654  1.00   42.75  ? 166  THR A O   1 
ATOM   1265 C CB  . THR A 1 166 ? 47.006  -13.669 10.969  1.00   43.41  ? 166  THR A CB  1 
ATOM   1266 O OG1 . THR A 1 166 ? 48.224  -12.953 11.210  1.00   43.89  ? 166  THR A OG1 1 
ATOM   1267 C CG2 . THR A 1 166 ? 46.309  -13.017 9.775   1.00   43.13  ? 166  THR A CG2 1 
ATOM   1268 N N   . ILE A 1 167 ? 43.758  -13.106 11.967  1.00   41.68  ? 167  ILE A N   1 
ATOM   1269 C CA  . ILE A 1 167 ? 42.355  -13.366 11.650  1.00   40.52  ? 167  ILE A CA  1 
ATOM   1270 C C   . ILE A 1 167 ? 42.190  -13.284 10.137  1.00   39.99  ? 167  ILE A C   1 
ATOM   1271 O O   . ILE A 1 167 ? 42.503  -12.261 9.540   1.00   39.74  ? 167  ILE A O   1 
ATOM   1272 C CB  . ILE A 1 167 ? 41.424  -12.344 12.341  1.00   40.55  ? 167  ILE A CB  1 
ATOM   1273 C CG1 . ILE A 1 167 ? 41.772  -12.201 13.831  1.00   40.99  ? 167  ILE A CG1 1 
ATOM   1274 C CG2 . ILE A 1 167 ? 39.947  -12.706 12.130  1.00   39.57  ? 167  ILE A CG2 1 
ATOM   1275 C CD1 . ILE A 1 167 ? 41.675  -13.501 14.662  1.00   40.68  ? 167  ILE A CD1 1 
ATOM   1276 N N   . VAL A 1 168 ? 41.699  -14.365 9.532   1.00   39.22  ? 168  VAL A N   1 
ATOM   1277 C CA  . VAL A 1 168 ? 41.698  -14.533 8.077   1.00   39.01  ? 168  VAL A CA  1 
ATOM   1278 C C   . VAL A 1 168 ? 40.281  -14.672 7.530   1.00   38.83  ? 168  VAL A C   1 
ATOM   1279 O O   . VAL A 1 168 ? 39.472  -15.417 8.084   1.00   38.26  ? 168  VAL A O   1 
ATOM   1280 C CB  . VAL A 1 168 ? 42.485  -15.813 7.655   1.00   38.71  ? 168  VAL A CB  1 
ATOM   1281 C CG1 . VAL A 1 168 ? 42.533  -15.954 6.139   1.00   38.92  ? 168  VAL A CG1 1 
ATOM   1282 C CG2 . VAL A 1 168 ? 43.896  -15.812 8.229   1.00   38.93  ? 168  VAL A CG2 1 
ATOM   1283 N N   . SER A 1 169 ? 40.002  -13.967 6.431   1.00   38.93  ? 169  SER A N   1 
ATOM   1284 C CA  . SER A 1 169 ? 38.727  -14.078 5.725   1.00   38.94  ? 169  SER A CA  1 
ATOM   1285 C C   . SER A 1 169 ? 38.813  -15.043 4.545   1.00   39.15  ? 169  SER A C   1 
ATOM   1286 O O   . SER A 1 169 ? 39.716  -14.921 3.716   1.00   38.98  ? 169  SER A O   1 
ATOM   1287 C CB  . SER A 1 169 ? 38.259  -12.708 5.222   1.00   39.15  ? 169  SER A CB  1 
ATOM   1288 O OG  . SER A 1 169 ? 36.948  -12.799 4.680   1.00   39.23  ? 169  SER A OG  1 
ATOM   1289 N N   . PRO A 1 170 ? 37.856  -15.989 4.452   1.00   39.30  ? 170  PRO A N   1 
ATOM   1290 C CA  . PRO A 1 170 ? 37.766  -16.970 3.369   1.00   39.71  ? 170  PRO A CA  1 
ATOM   1291 C C   . PRO A 1 170 ? 37.503  -16.346 1.995   1.00   40.24  ? 170  PRO A C   1 
ATOM   1292 O O   . PRO A 1 170 ? 37.766  -16.976 0.972   1.00   40.07  ? 170  PRO A O   1 
ATOM   1293 C CB  . PRO A 1 170 ? 36.554  -17.825 3.765   1.00   39.84  ? 170  PRO A CB  1 
ATOM   1294 C CG  . PRO A 1 170 ? 36.324  -17.551 5.216   1.00   39.96  ? 170  PRO A CG  1 
ATOM   1295 C CD  . PRO A 1 170 ? 36.765  -16.152 5.432   1.00   39.38  ? 170  PRO A CD  1 
ATOM   1296 N N   . ASP A 1 171 ? 36.980  -15.124 1.983   1.00   40.96  ? 171  ASP A N   1 
ATOM   1297 C CA  . ASP A 1 171 ? 36.590  -14.451 0.749   1.00   41.79  ? 171  ASP A CA  1 
ATOM   1298 C C   . ASP A 1 171 ? 36.773  -12.941 0.878   1.00   42.18  ? 171  ASP A C   1 
ATOM   1299 O O   . ASP A 1 171 ? 37.081  -12.426 1.963   1.00   41.94  ? 171  ASP A O   1 
ATOM   1300 C CB  . ASP A 1 171 ? 35.138  -14.797 0.368   1.00   41.95  ? 171  ASP A CB  1 
ATOM   1301 C CG  . ASP A 1 171 ? 34.134  -14.483 1.481   1.00   42.69  ? 171  ASP A CG  1 
ATOM   1302 O OD1 . ASP A 1 171 ? 33.030  -15.078 1.473   1.00   45.16  ? 171  ASP A OD1 1 
ATOM   1303 O OD2 . ASP A 1 171 ? 34.432  -13.650 2.362   1.00   42.64  ? 171  ASP A OD2 1 
ATOM   1304 N N   . ALA A 1 172 ? 36.572  -12.243 -0.236  1.00   42.75  ? 172  ALA A N   1 
ATOM   1305 C CA  . ALA A 1 172 ? 36.702  -10.791 -0.294  1.00   43.26  ? 172  ALA A CA  1 
ATOM   1306 C C   . ALA A 1 172 ? 35.618  -10.091 0.533   1.00   43.48  ? 172  ALA A C   1 
ATOM   1307 O O   . ALA A 1 172 ? 35.868  -9.060  1.155   1.00   43.89  ? 172  ALA A O   1 
ATOM   1308 C CB  . ALA A 1 172 ? 36.655  -10.329 -1.741  1.00   43.33  ? 172  ALA A CB  1 
ATOM   1309 N N   . GLY A 1 173 ? 34.424  -10.677 0.553   1.00   43.96  ? 173  GLY A N   1 
ATOM   1310 C CA  . GLY A 1 173 ? 33.266  -10.092 1.233   1.00   43.83  ? 173  GLY A CA  1 
ATOM   1311 C C   . GLY A 1 173 ? 33.330  -10.082 2.748   1.00   43.81  ? 173  GLY A C   1 
ATOM   1312 O O   . GLY A 1 173 ? 32.656  -9.270  3.397   1.00   44.13  ? 173  GLY A O   1 
ATOM   1313 N N   . GLY A 1 174 ? 34.130  -10.979 3.322   1.00   43.47  ? 174  GLY A N   1 
ATOM   1314 C CA  . GLY A 1 174 ? 34.265  -11.057 4.781   1.00   42.64  ? 174  GLY A CA  1 
ATOM   1315 C C   . GLY A 1 174 ? 35.300  -10.110 5.374   1.00   42.30  ? 174  GLY A C   1 
ATOM   1316 O O   . GLY A 1 174 ? 35.640  -10.219 6.555   1.00   41.84  ? 174  GLY A O   1 
ATOM   1317 N N   . ALA A 1 175 ? 35.794  -9.176  4.561   1.00   42.13  ? 175  ALA A N   1 
ATOM   1318 C CA  . ALA A 1 175 ? 36.868  -8.263  4.966   1.00   42.24  ? 175  ALA A CA  1 
ATOM   1319 C C   . ALA A 1 175 ? 36.568  -7.468  6.237   1.00   42.49  ? 175  ALA A C   1 
ATOM   1320 O O   . ALA A 1 175 ? 37.389  -7.438  7.155   1.00   42.63  ? 175  ALA A O   1 
ATOM   1321 C CB  . ALA A 1 175 ? 37.236  -7.327  3.824   1.00   42.51  ? 175  ALA A CB  1 
ATOM   1322 N N   . LYS A 1 176 ? 35.395  -6.835  6.288   1.00   42.37  ? 176  LYS A N   1 
ATOM   1323 C CA  . LYS A 1 176 ? 34.997  -5.983  7.415   1.00   42.28  ? 176  LYS A CA  1 
ATOM   1324 C C   . LYS A 1 176 ? 34.881  -6.760  8.723   1.00   41.99  ? 176  LYS A C   1 
ATOM   1325 O O   . LYS A 1 176 ? 35.244  -6.261  9.793   1.00   41.63  ? 176  LYS A O   1 
ATOM   1326 C CB  . LYS A 1 176 ? 33.641  -5.345  7.127   1.00   42.72  ? 176  LYS A CB  1 
ATOM   1327 C CG  . LYS A 1 176 ? 33.439  -3.992  7.772   1.00   43.54  ? 176  LYS A CG  1 
ATOM   1328 C CD  . LYS A 1 176 ? 33.490  -2.887  6.729   1.00   46.37  ? 176  LYS A CD  1 
ATOM   1329 C CE  . LYS A 1 176 ? 32.300  -3.001  5.757   1.00   48.40  ? 176  LYS A CE  1 
ATOM   1330 N NZ  . LYS A 1 176 ? 32.088  -1.714  5.016   1.00   49.23  ? 176  LYS A NZ  1 
ATOM   1331 N N   . ARG A 1 177 ? 34.343  -7.971  8.622   0.95   41.69  ? 177  ARG A N   1 
ATOM   1332 C CA  . ARG A 1 177 ? 34.143  -8.840  9.764   0.95   41.71  ? 177  ARG A CA  1 
ATOM   1333 C C   . ARG A 1 177 ? 35.471  -9.238  10.413  0.95   41.23  ? 177  ARG A C   1 
ATOM   1334 O O   . ARG A 1 177 ? 35.591  -9.222  11.636  0.95   41.05  ? 177  ARG A O   1 
ATOM   1335 C CB  . ARG A 1 177 ? 33.354  -10.079 9.340   0.95   41.98  ? 177  ARG A CB  1 
ATOM   1336 C CG  . ARG A 1 177 ? 32.650  -10.796 10.491  0.95   44.22  ? 177  ARG A CG  1 
ATOM   1337 C CD  . ARG A 1 177 ? 31.880  -12.030 10.014  0.95   47.03  ? 177  ARG A CD  1 
ATOM   1338 N NE  . ARG A 1 177 ? 30.716  -11.679 9.197   0.95   49.95  ? 177  ARG A NE  1 
ATOM   1339 C CZ  . ARG A 1 177 ? 30.663  -11.752 7.865   0.95   51.10  ? 177  ARG A CZ  1 
ATOM   1340 N NH1 . ARG A 1 177 ? 31.711  -12.176 7.165   0.95   51.94  ? 177  ARG A NH1 1 
ATOM   1341 N NH2 . ARG A 1 177 ? 29.551  -11.403 7.226   0.95   51.72  ? 177  ARG A NH2 1 
ATOM   1342 N N   . VAL A 1 178 ? 36.466  -9.572  9.596   1.00   40.86  ? 178  VAL A N   1 
ATOM   1343 C CA  . VAL A 1 178 ? 37.770  -9.968  10.125  1.00   40.59  ? 178  VAL A CA  1 
ATOM   1344 C C   . VAL A 1 178 ? 38.621  -8.798  10.625  1.00   40.36  ? 178  VAL A C   1 
ATOM   1345 O O   . VAL A 1 178 ? 39.359  -8.960  11.600  1.00   40.53  ? 178  VAL A O   1 
ATOM   1346 C CB  . VAL A 1 178 ? 38.586  -10.888 9.145   1.00   40.84  ? 178  VAL A CB  1 
ATOM   1347 C CG1 . VAL A 1 178 ? 37.705  -12.006 8.599   1.00   40.05  ? 178  VAL A CG1 1 
ATOM   1348 C CG2 . VAL A 1 178 ? 39.234  -10.090 8.019   1.00   40.92  ? 178  VAL A CG2 1 
ATOM   1349 N N   . THR A 1 179 ? 38.520  -7.631  9.977   1.00   39.55  ? 179  THR A N   1 
ATOM   1350 C CA  . THR A 1 179 ? 39.307  -6.471  10.400  1.00   39.10  ? 179  THR A CA  1 
ATOM   1351 C C   . THR A 1 179 ? 38.803  -5.920  11.727  1.00   39.32  ? 179  THR A C   1 
ATOM   1352 O O   . THR A 1 179 ? 39.580  -5.375  12.504  1.00   38.85  ? 179  THR A O   1 
ATOM   1353 C CB  . THR A 1 179 ? 39.343  -5.321  9.361   1.00   39.24  ? 179  THR A CB  1 
ATOM   1354 O OG1 . THR A 1 179 ? 38.022  -4.800  9.156   1.00   38.34  ? 179  THR A OG1 1 
ATOM   1355 C CG2 . THR A 1 179 ? 39.953  -5.776  8.045   1.00   38.50  ? 179  THR A CG2 1 
ATOM   1356 N N   . SER A 1 180 ? 37.502  -6.070  11.970  1.00   39.62  ? 180  SER A N   1 
ATOM   1357 C CA  . SER A 1 180 ? 36.903  -5.720  13.250  1.00   40.68  ? 180  SER A CA  1 
ATOM   1358 C C   . SER A 1 180 ? 37.435  -6.603  14.381  1.00   40.91  ? 180  SER A C   1 
ATOM   1359 O O   . SER A 1 180 ? 37.822  -6.097  15.427  1.00   41.13  ? 180  SER A O   1 
ATOM   1360 C CB  . SER A 1 180 ? 35.383  -5.812  13.177  1.00   40.75  ? 180  SER A CB  1 
ATOM   1361 O OG  . SER A 1 180 ? 34.821  -5.708  14.471  1.00   42.37  ? 180  SER A OG  1 
ATOM   1362 N N   . ILE A 1 181 ? 37.462  -7.915  14.154  1.00   41.38  ? 181  ILE A N   1 
ATOM   1363 C CA  . ILE A 1 181 ? 37.965  -8.876  15.137  1.00   42.21  ? 181  ILE A CA  1 
ATOM   1364 C C   . ILE A 1 181 ? 39.462  -8.668  15.398  1.00   42.62  ? 181  ILE A C   1 
ATOM   1365 O O   . ILE A 1 181 ? 39.896  -8.602  16.554  1.00   42.60  ? 181  ILE A O   1 
ATOM   1366 C CB  . ILE A 1 181 ? 37.668  -10.344 14.690  1.00   42.28  ? 181  ILE A CB  1 
ATOM   1367 C CG1 . ILE A 1 181 ? 36.164  -10.621 14.762  1.00   42.36  ? 181  ILE A CG1 1 
ATOM   1368 C CG2 . ILE A 1 181 ? 38.433  -11.362 15.549  1.00   42.60  ? 181  ILE A CG2 1 
ATOM   1369 C CD1 . ILE A 1 181 ? 35.713  -11.760 13.877  1.00   42.74  ? 181  ILE A CD1 1 
ATOM   1370 N N   . ALA A 1 182 ? 40.234  -8.552  14.317  1.00   43.33  ? 182  ALA A N   1 
ATOM   1371 C CA  . ALA A 1 182 ? 41.679  -8.301  14.390  1.00   43.87  ? 182  ALA A CA  1 
ATOM   1372 C C   . ALA A 1 182 ? 42.024  -6.997  15.111  1.00   44.22  ? 182  ALA A C   1 
ATOM   1373 O O   . ALA A 1 182 ? 43.010  -6.945  15.855  1.00   44.31  ? 182  ALA A O   1 
ATOM   1374 C CB  . ALA A 1 182 ? 42.304  -8.322  12.997  1.00   43.73  ? 182  ALA A CB  1 
ATOM   1375 N N   . ASP A 1 183 ? 41.214  -5.958  14.902  1.00   44.45  ? 183  ASP A N   1 
ATOM   1376 C CA  . ASP A 1 183 ? 41.439  -4.675  15.571  1.00   45.33  ? 183  ASP A CA  1 
ATOM   1377 C C   . ASP A 1 183 ? 41.263  -4.764  17.090  1.00   45.92  ? 183  ASP A C   1 
ATOM   1378 O O   . ASP A 1 183 ? 42.126  -4.297  17.840  1.00   45.98  ? 183  ASP A O   1 
ATOM   1379 C CB  . ASP A 1 183 ? 40.541  -3.572  14.997  1.00   45.39  ? 183  ASP A CB  1 
ATOM   1380 C CG  . ASP A 1 183 ? 41.076  -2.984  13.690  1.00   46.00  ? 183  ASP A CG  1 
ATOM   1381 O OD1 . ASP A 1 183 ? 42.001  -3.572  13.084  1.00   46.41  ? 183  ASP A OD1 1 
ATOM   1382 O OD2 . ASP A 1 183 ? 40.556  -1.929  13.260  1.00   45.60  ? 183  ASP A OD2 1 
ATOM   1383 N N   . ARG A 1 184 ? 40.156  -5.368  17.531  0.82   46.20  ? 184  ARG A N   1 
ATOM   1384 C CA  . ARG A 1 184 ? 39.840  -5.493  18.959  0.82   46.72  ? 184  ARG A CA  1 
ATOM   1385 C C   . ARG A 1 184 ? 40.859  -6.361  19.709  0.82   46.65  ? 184  ARG A C   1 
ATOM   1386 O O   . ARG A 1 184 ? 41.125  -6.137  20.889  0.82   46.52  ? 184  ARG A O   1 
ATOM   1387 C CB  . ARG A 1 184 ? 38.404  -6.008  19.149  0.82   46.84  ? 184  ARG A CB  1 
ATOM   1388 C CG  . ARG A 1 184 ? 38.032  -6.408  20.580  0.82   48.46  ? 184  ARG A CG  1 
ATOM   1389 C CD  . ARG A 1 184 ? 37.606  -5.239  21.466  0.82   51.09  ? 184  ARG A CD  1 
ATOM   1390 N NE  . ARG A 1 184 ? 36.266  -4.753  21.138  0.82   52.47  ? 184  ARG A NE  1 
ATOM   1391 C CZ  . ARG A 1 184 ? 35.501  -4.032  21.958  0.82   54.05  ? 184  ARG A CZ  1 
ATOM   1392 N NH1 . ARG A 1 184 ? 35.926  -3.709  23.177  0.82   54.76  ? 184  ARG A NH1 1 
ATOM   1393 N NH2 . ARG A 1 184 ? 34.299  -3.634  21.559  0.82   54.21  ? 184  ARG A NH2 1 
ATOM   1394 N N   . LEU A 1 185 ? 41.433  -7.337  19.008  1.00   46.95  ? 185  LEU A N   1 
ATOM   1395 C CA  . LEU A 1 185 ? 42.491  -8.187  19.553  1.00   47.01  ? 185  LEU A CA  1 
ATOM   1396 C C   . LEU A 1 185 ? 43.874  -7.539  19.444  1.00   47.46  ? 185  LEU A C   1 
ATOM   1397 O O   . LEU A 1 185 ? 44.829  -7.985  20.102  1.00   47.64  ? 185  LEU A O   1 
ATOM   1398 C CB  . LEU A 1 185 ? 42.519  -9.536  18.821  1.00   46.67  ? 185  LEU A CB  1 
ATOM   1399 C CG  . LEU A 1 185 ? 41.373  -10.540 18.981  1.00   46.24  ? 185  LEU A CG  1 
ATOM   1400 C CD1 . LEU A 1 185 ? 41.632  -11.762 18.119  1.00   45.23  ? 185  LEU A CD1 1 
ATOM   1401 C CD2 . LEU A 1 185 ? 41.177  -10.956 20.445  1.00   46.18  ? 185  LEU A CD2 1 
ATOM   1402 N N   . ASN A 1 186 ? 43.966  -6.492  18.621  1.00   47.65  ? 186  ASN A N   1 
ATOM   1403 C CA  . ASN A 1 186 ? 45.241  -5.896  18.190  1.00   48.05  ? 186  ASN A CA  1 
ATOM   1404 C C   . ASN A 1 186 ? 46.207  -6.902  17.576  1.00   47.70  ? 186  ASN A C   1 
ATOM   1405 O O   . ASN A 1 186 ? 47.371  -7.019  17.992  1.00   47.85  ? 186  ASN A O   1 
ATOM   1406 C CB  . ASN A 1 186 ? 45.903  -5.060  19.295  1.00   48.44  ? 186  ASN A CB  1 
ATOM   1407 C CG  . ASN A 1 186 ? 45.546  -3.587  19.194  1.00   49.50  ? 186  ASN A CG  1 
ATOM   1408 O OD1 . ASN A 1 186 ? 46.278  -2.799  18.589  1.00   51.13  ? 186  ASN A OD1 1 
ATOM   1409 N ND2 . ASN A 1 186 ? 44.404  -3.212  19.763  1.00   50.40  ? 186  ASN A ND2 1 
ATOM   1410 N N   . VAL A 1 187 ? 45.691  -7.634  16.587  1.00   47.14  ? 187  VAL A N   1 
ATOM   1411 C CA  . VAL A 1 187 ? 46.477  -8.569  15.796  1.00   46.31  ? 187  VAL A CA  1 
ATOM   1412 C C   . VAL A 1 187 ? 46.323  -8.233  14.309  1.00   46.03  ? 187  VAL A C   1 
ATOM   1413 O O   . VAL A 1 187 ? 45.663  -7.251  13.958  1.00   45.77  ? 187  VAL A O   1 
ATOM   1414 C CB  . VAL A 1 187 ? 46.091  -10.051 16.084  1.00   46.54  ? 187  VAL A CB  1 
ATOM   1415 C CG1 . VAL A 1 187 ? 46.293  -10.378 17.566  1.00   46.30  ? 187  VAL A CG1 1 
ATOM   1416 C CG2 . VAL A 1 187 ? 44.651  -10.361 15.637  1.00   46.19  ? 187  VAL A CG2 1 
ATOM   1417 N N   . ASP A 1 188 ? 46.939  -9.049  13.452  1.00   45.57  ? 188  ASP A N   1 
ATOM   1418 C CA  . ASP A 1 188 ? 46.914  -8.849  12.009  1.00   45.29  ? 188  ASP A CA  1 
ATOM   1419 C C   . ASP A 1 188 ? 45.736  -9.561  11.342  1.00   44.54  ? 188  ASP A C   1 
ATOM   1420 O O   . ASP A 1 188 ? 45.103  -10.441 11.938  1.00   44.59  ? 188  ASP A O   1 
ATOM   1421 C CB  . ASP A 1 188 ? 48.226  -9.344  11.381  1.00   45.90  ? 188  ASP A CB  1 
ATOM   1422 C CG  . ASP A 1 188 ? 49.464  -8.676  11.977  1.00   47.45  ? 188  ASP A CG  1 
ATOM   1423 O OD1 . ASP A 1 188 ? 49.327  -7.668  12.723  1.00   49.13  ? 188  ASP A OD1 1 
ATOM   1424 O OD2 . ASP A 1 188 ? 50.581  -9.171  11.690  1.00   49.35  ? 188  ASP A OD2 1 
ATOM   1425 N N   . PHE A 1 189 ? 45.450  -9.173  10.101  1.00   43.25  ? 189  PHE A N   1 
ATOM   1426 C CA  . PHE A 1 189 ? 44.441  -9.852  9.298   1.00   42.34  ? 189  PHE A CA  1 
ATOM   1427 C C   . PHE A 1 189 ? 45.006  -10.210 7.937   1.00   41.85  ? 189  PHE A C   1 
ATOM   1428 O O   . PHE A 1 189 ? 45.994  -9.629  7.489   1.00   41.17  ? 189  PHE A O   1 
ATOM   1429 C CB  . PHE A 1 189 ? 43.166  -9.005  9.149   1.00   42.15  ? 189  PHE A CB  1 
ATOM   1430 C CG  . PHE A 1 189 ? 43.321  -7.830  8.220   1.00   41.77  ? 189  PHE A CG  1 
ATOM   1431 C CD1 . PHE A 1 189 ? 42.967  -7.936  6.876   1.00   40.19  ? 189  PHE A CD1 1 
ATOM   1432 C CD2 . PHE A 1 189 ? 43.827  -6.622  8.690   1.00   40.73  ? 189  PHE A CD2 1 
ATOM   1433 C CE1 . PHE A 1 189 ? 43.116  -6.852  6.016   1.00   41.12  ? 189  PHE A CE1 1 
ATOM   1434 C CE2 . PHE A 1 189 ? 43.979  -5.533  7.837   1.00   41.15  ? 189  PHE A CE2 1 
ATOM   1435 C CZ  . PHE A 1 189 ? 43.628  -5.647  6.501   1.00   40.62  ? 189  PHE A CZ  1 
ATOM   1436 N N   . ALA A 1 190 ? 44.368  -11.181 7.297   1.00   41.68  ? 190  ALA A N   1 
ATOM   1437 C CA  . ALA A 1 190 ? 44.684  -11.567 5.932   1.00   41.49  ? 190  ALA A CA  1 
ATOM   1438 C C   . ALA A 1 190 ? 43.388  -11.938 5.223   1.00   41.67  ? 190  ALA A C   1 
ATOM   1439 O O   . ALA A 1 190 ? 42.349  -12.105 5.854   1.00   41.67  ? 190  ALA A O   1 
ATOM   1440 C CB  . ALA A 1 190 ? 45.662  -12.741 5.918   1.00   41.27  ? 190  ALA A CB  1 
ATOM   1441 N N   . LEU A 1 191 ? 43.451  -12.066 3.907   1.00   41.95  ? 191  LEU A N   1 
ATOM   1442 C CA  . LEU A 1 191 ? 42.256  -12.332 3.135   1.00   42.67  ? 191  LEU A CA  1 
ATOM   1443 C C   . LEU A 1 191 ? 42.568  -13.273 1.992   1.00   42.87  ? 191  LEU A C   1 
ATOM   1444 O O   . LEU A 1 191 ? 43.623  -13.178 1.366   1.00   43.16  ? 191  LEU A O   1 
ATOM   1445 C CB  . LEU A 1 191 ? 41.643  -11.018 2.627   1.00   42.44  ? 191  LEU A CB  1 
ATOM   1446 C CG  . LEU A 1 191 ? 40.327  -11.094 1.849   1.00   43.20  ? 191  LEU A CG  1 
ATOM   1447 C CD1 . LEU A 1 191 ? 39.403  -9.954  2.255   1.00   44.25  ? 191  LEU A CD1 1 
ATOM   1448 C CD2 . LEU A 1 191 ? 40.592  -11.087 0.343   1.00   42.67  ? 191  LEU A CD2 1 
ATOM   1449 N N   . ILE A 1 192 ? 41.634  -14.180 1.736   1.00   43.57  ? 192  ILE A N   1 
ATOM   1450 C CA  . ILE A 1 192 ? 41.730  -15.113 0.628   1.00   44.00  ? 192  ILE A CA  1 
ATOM   1451 C C   . ILE A 1 192 ? 40.700  -14.743 -0.427  1.00   44.45  ? 192  ILE A C   1 
ATOM   1452 O O   . ILE A 1 192 ? 39.582  -14.343 -0.109  1.00   44.42  ? 192  ILE A O   1 
ATOM   1453 C CB  . ILE A 1 192 ? 41.559  -16.574 1.106   1.00   44.05  ? 192  ILE A CB  1 
ATOM   1454 C CG1 . ILE A 1 192 ? 42.769  -16.987 1.953   1.00   44.81  ? 192  ILE A CG1 1 
ATOM   1455 C CG2 . ILE A 1 192 ? 41.384  -17.537 -0.074  1.00   43.81  ? 192  ILE A CG2 1 
ATOM   1456 C CD1 . ILE A 1 192 ? 42.567  -18.253 2.769   1.00   44.87  ? 192  ILE A CD1 1 
ATOM   1457 N N   . HIS A 1 193 ? 41.107  -14.847 -1.685  1.00   44.83  ? 193  HIS A N   1 
ATOM   1458 C CA  . HIS A 1 193 ? 40.225  -14.611 -2.812  1.00   45.43  ? 193  HIS A CA  1 
ATOM   1459 C C   . HIS A 1 193 ? 40.423  -15.712 -3.844  1.00   46.22  ? 193  HIS A C   1 
ATOM   1460 O O   . HIS A 1 193 ? 41.557  -16.151 -4.087  1.00   45.92  ? 193  HIS A O   1 
ATOM   1461 C CB  . HIS A 1 193 ? 40.504  -13.241 -3.432  1.00   45.20  ? 193  HIS A CB  1 
ATOM   1462 C CG  . HIS A 1 193 ? 39.787  -13.005 -4.723  1.00   44.35  ? 193  HIS A CG  1 
ATOM   1463 N ND1 . HIS A 1 193 ? 38.412  -12.963 -4.814  1.00   43.81  ? 193  HIS A ND1 1 
ATOM   1464 C CD2 . HIS A 1 193 ? 40.254  -12.803 -5.978  1.00   43.73  ? 193  HIS A CD2 1 
ATOM   1465 C CE1 . HIS A 1 193 ? 38.061  -12.745 -6.069  1.00   43.93  ? 193  HIS A CE1 1 
ATOM   1466 N NE2 . HIS A 1 193 ? 39.160  -12.641 -6.795  1.00   44.87  ? 193  HIS A NE2 1 
ATOM   1467 N N   . LYS A 1 194 ? 39.313  -16.164 -4.429  0.82   47.49  ? 194  LYS A N   1 
ATOM   1468 C CA  . LYS A 1 194 ? 39.341  -17.200 -5.455  0.82   48.82  ? 194  LYS A CA  1 
ATOM   1469 C C   . LYS A 1 194 ? 39.281  -16.555 -6.830  0.82   49.60  ? 194  LYS A C   1 
ATOM   1470 O O   . LYS A 1 194 ? 38.292  -15.905 -7.184  0.82   49.85  ? 194  LYS A O   1 
ATOM   1471 C CB  . LYS A 1 194 ? 38.196  -18.201 -5.261  0.82   49.05  ? 194  LYS A CB  1 
ATOM   1472 C CG  . LYS A 1 194 ? 38.381  -19.515 -6.028  0.82   49.87  ? 194  LYS A CG  1 
ATOM   1473 C CD  . LYS A 1 194 ? 37.222  -20.487 -5.806  0.82   51.11  ? 194  LYS A CD  1 
ATOM   1474 C CE  . LYS A 1 194 ? 37.470  -21.821 -6.520  0.82   52.19  ? 194  LYS A CE  1 
ATOM   1475 N NZ  . LYS A 1 194 ? 36.395  -22.840 -6.288  0.82   52.81  ? 194  LYS A NZ  1 
ATOM   1476 N N   . GLU A 1 195 ? 40.353  -16.747 -7.595  0.81   50.71  ? 195  GLU A N   1 
ATOM   1477 C CA  . GLU A 1 195 ? 40.543  -16.100 -8.892  0.81   51.67  ? 195  GLU A CA  1 
ATOM   1478 C C   . GLU A 1 195 ? 39.436  -16.442 -9.887  0.81   51.93  ? 195  GLU A C   1 
ATOM   1479 O O   . GLU A 1 195 ? 39.164  -17.616 -10.149 0.81   52.33  ? 195  GLU A O   1 
ATOM   1480 C CB  . GLU A 1 195 ? 41.906  -16.485 -9.471  0.81   51.96  ? 195  GLU A CB  1 
ATOM   1481 C CG  . GLU A 1 195 ? 42.727  -15.309 -9.993  0.81   53.69  ? 195  GLU A CG  1 
ATOM   1482 C CD  . GLU A 1 195 ? 43.487  -14.586 -8.890  0.81   55.01  ? 195  GLU A CD  1 
ATOM   1483 O OE1 . GLU A 1 195 ? 42.889  -14.284 -7.832  0.81   56.23  ? 195  GLU A OE1 1 
ATOM   1484 O OE2 . GLU A 1 195 ? 44.691  -14.314 -9.086  0.81   55.85  ? 195  GLU A OE2 1 
ATOM   1485 N N   . ASP A 1 203 ? 39.607  -22.937 -10.059 0.84   60.41  ? 203  ASP A N   1 
ATOM   1486 C CA  . ASP A 1 203 ? 40.320  -21.675 -9.854  0.84   60.47  ? 203  ASP A CA  1 
ATOM   1487 C C   . ASP A 1 203 ? 41.505  -21.842 -8.905  0.84   60.16  ? 203  ASP A C   1 
ATOM   1488 O O   . ASP A 1 203 ? 41.686  -22.910 -8.298  0.84   60.45  ? 203  ASP A O   1 
ATOM   1489 C CB  . ASP A 1 203 ? 39.376  -20.609 -9.281  0.84   60.76  ? 203  ASP A CB  1 
ATOM   1490 C CG  . ASP A 1 203 ? 38.111  -20.426 -10.103 0.84   61.21  ? 203  ASP A CG  1 
ATOM   1491 O OD1 . ASP A 1 203 ? 38.162  -20.582 -11.344 0.84   61.66  ? 203  ASP A OD1 1 
ATOM   1492 O OD2 . ASP A 1 203 ? 37.064  -20.107 -9.496  0.84   61.93  ? 203  ASP A OD2 1 
ATOM   1493 N N   . ARG A 1 204 ? 42.306  -20.784 -8.781  0.74   59.60  ? 204  ARG A N   1 
ATOM   1494 C CA  . ARG A 1 204 ? 43.377  -20.742 -7.785  0.74   58.96  ? 204  ARG A CA  1 
ATOM   1495 C C   . ARG A 1 204 ? 43.042  -19.747 -6.676  0.74   58.12  ? 204  ARG A C   1 
ATOM   1496 O O   . ARG A 1 204 ? 42.414  -18.712 -6.924  0.74   57.97  ? 204  ARG A O   1 
ATOM   1497 C CB  . ARG A 1 204 ? 44.730  -20.413 -8.435  0.74   59.26  ? 204  ARG A CB  1 
ATOM   1498 C CG  . ARG A 1 204 ? 44.948  -18.939 -8.779  0.74   60.12  ? 204  ARG A CG  1 
ATOM   1499 C CD  . ARG A 1 204 ? 46.358  -18.687 -9.291  0.74   61.69  ? 204  ARG A CD  1 
ATOM   1500 N NE  . ARG A 1 204 ? 46.838  -17.350 -8.932  0.74   62.46  ? 204  ARG A NE  1 
ATOM   1501 C CZ  . ARG A 1 204 ? 47.875  -16.739 -9.502  0.74   62.97  ? 204  ARG A CZ  1 
ATOM   1502 N NH1 . ARG A 1 204 ? 48.552  -17.328 -10.482 0.74   63.83  ? 204  ARG A NH1 1 
ATOM   1503 N NH2 . ARG A 1 204 ? 48.232  -15.527 -9.098  0.74   62.96  ? 204  ARG A NH2 1 
ATOM   1504 N N   . MET A 1 205 ? 43.454  -20.075 -5.454  0.82   57.19  ? 205  MET A N   1 
ATOM   1505 C CA  . MET A 1 205 ? 43.255  -19.192 -4.314  0.82   56.27  ? 205  MET A CA  1 
ATOM   1506 C C   . MET A 1 205 ? 44.460  -18.281 -4.098  0.82   55.52  ? 205  MET A C   1 
ATOM   1507 O O   . MET A 1 205 ? 45.612  -18.715 -4.198  0.82   55.40  ? 205  MET A O   1 
ATOM   1508 C CB  . MET A 1 205 ? 42.951  -19.999 -3.051  0.82   56.53  ? 205  MET A CB  1 
ATOM   1509 C CG  . MET A 1 205 ? 41.481  -20.347 -2.890  0.82   57.33  ? 205  MET A CG  1 
ATOM   1510 S SD  . MET A 1 205 ? 41.169  -21.419 -1.471  0.82   59.59  ? 205  MET A SD  1 
ATOM   1511 C CE  . MET A 1 205 ? 39.506  -20.907 -1.025  0.82   59.14  ? 205  MET A CE  1 
ATOM   1512 N N   . VAL A 1 206 ? 44.179  -17.014 -3.810  1.00   54.39  ? 206  VAL A N   1 
ATOM   1513 C CA  . VAL A 1 206 ? 45.214  -16.015 -3.564  1.00   53.42  ? 206  VAL A CA  1 
ATOM   1514 C C   . VAL A 1 206 ? 45.105  -15.502 -2.126  1.00   52.69  ? 206  VAL A C   1 
ATOM   1515 O O   . VAL A 1 206 ? 44.006  -15.293 -1.611  1.00   52.13  ? 206  VAL A O   1 
ATOM   1516 C CB  . VAL A 1 206 ? 45.119  -14.851 -4.589  1.00   53.52  ? 206  VAL A CB  1 
ATOM   1517 C CG1 . VAL A 1 206 ? 45.954  -13.643 -4.162  1.00   53.50  ? 206  VAL A CG1 1 
ATOM   1518 C CG2 . VAL A 1 206 ? 45.551  -15.328 -5.969  1.00   53.93  ? 206  VAL A CG2 1 
ATOM   1519 N N   . LEU A 1 207 ? 46.254  -15.306 -1.489  1.00   52.07  ? 207  LEU A N   1 
ATOM   1520 C CA  . LEU A 1 207 ? 46.308  -14.815 -0.118  1.00   51.67  ? 207  LEU A CA  1 
ATOM   1521 C C   . LEU A 1 207 ? 47.003  -13.460 -0.038  1.00   51.38  ? 207  LEU A C   1 
ATOM   1522 O O   . LEU A 1 207 ? 48.161  -13.318 -0.452  1.00   51.19  ? 207  LEU A O   1 
ATOM   1523 C CB  . LEU A 1 207 ? 47.044  -15.820 0.773   1.00   51.68  ? 207  LEU A CB  1 
ATOM   1524 C CG  . LEU A 1 207 ? 46.837  -15.823 2.293   1.00   51.78  ? 207  LEU A CG  1 
ATOM   1525 C CD1 . LEU A 1 207 ? 47.455  -17.086 2.872   1.00   52.33  ? 207  LEU A CD1 1 
ATOM   1526 C CD2 . LEU A 1 207 ? 47.439  -14.598 2.967   1.00   52.47  ? 207  LEU A CD2 1 
ATOM   1527 N N   . VAL A 1 208 ? 46.292  -12.470 0.503   1.00   50.85  ? 208  VAL A N   1 
ATOM   1528 C CA  . VAL A 1 208 ? 46.899  -11.181 0.821   1.00   50.45  ? 208  VAL A CA  1 
ATOM   1529 C C   . VAL A 1 208 ? 47.035  -11.031 2.332   1.00   50.50  ? 208  VAL A C   1 
ATOM   1530 O O   . VAL A 1 208 ? 46.070  -11.231 3.076   1.00   50.42  ? 208  VAL A O   1 
ATOM   1531 C CB  . VAL A 1 208 ? 46.125  -9.976  0.208   1.00   50.42  ? 208  VAL A CB  1 
ATOM   1532 C CG1 . VAL A 1 208 ? 45.991  -10.141 -1.303  1.00   50.31  ? 208  VAL A CG1 1 
ATOM   1533 C CG2 . VAL A 1 208 ? 44.749  -9.800  0.856   1.00   49.86  ? 208  VAL A CG2 1 
ATOM   1534 N N   . GLY A 1 209 ? 48.236  -10.685 2.780   1.00   50.23  ? 209  GLY A N   1 
ATOM   1535 C CA  . GLY A 1 209 ? 48.505  -10.537 4.204   1.00   50.72  ? 209  GLY A CA  1 
ATOM   1536 C C   . GLY A 1 209 ? 49.398  -11.644 4.725   1.00   50.84  ? 209  GLY A C   1 
ATOM   1537 O O   . GLY A 1 209 ? 49.610  -12.654 4.056   1.00   50.84  ? 209  GLY A O   1 
ATOM   1538 N N   . ASP A 1 210 ? 49.917  -11.457 5.931   1.00   51.26  ? 210  ASP A N   1 
ATOM   1539 C CA  . ASP A 1 210 ? 50.932  -12.355 6.466   1.00   51.82  ? 210  ASP A CA  1 
ATOM   1540 C C   . ASP A 1 210 ? 50.364  -13.327 7.496   1.00   51.61  ? 210  ASP A C   1 
ATOM   1541 O O   . ASP A 1 210 ? 49.671  -12.918 8.429   1.00   51.53  ? 210  ASP A O   1 
ATOM   1542 C CB  . ASP A 1 210 ? 52.090  -11.550 7.069   1.00   52.08  ? 210  ASP A CB  1 
ATOM   1543 C CG  . ASP A 1 210 ? 53.314  -12.406 7.349   1.00   56.23  ? 210  ASP A CG  1 
ATOM   1544 O OD1 . ASP A 1 210 ? 53.576  -13.352 6.568   1.00   56.52  ? 210  ASP A OD1 1 
ATOM   1545 O OD2 . ASP A 1 210 ? 54.016  -12.127 8.349   1.00   61.21  ? 210  ASP A OD2 1 
ATOM   1546 N N   . VAL A 1 211 ? 50.665  -14.611 7.303   1.00   51.50  ? 211  VAL A N   1 
ATOM   1547 C CA  . VAL A 1 211 ? 50.270  -15.674 8.234   1.00   51.66  ? 211  VAL A CA  1 
ATOM   1548 C C   . VAL A 1 211 ? 51.453  -16.566 8.650   1.00   51.88  ? 211  VAL A C   1 
ATOM   1549 O O   . VAL A 1 211 ? 51.274  -17.524 9.416   1.00   51.74  ? 211  VAL A O   1 
ATOM   1550 C CB  . VAL A 1 211 ? 49.137  -16.576 7.654   1.00   51.49  ? 211  VAL A CB  1 
ATOM   1551 C CG1 . VAL A 1 211 ? 47.952  -15.732 7.171   1.00   51.65  ? 211  VAL A CG1 1 
ATOM   1552 C CG2 . VAL A 1 211 ? 49.663  -17.460 6.531   1.00   51.01  ? 211  VAL A CG2 1 
ATOM   1553 N N   . LYS A 1 212 ? 52.647  -16.248 8.146   0.85   51.95  ? 212  LYS A N   1 
ATOM   1554 C CA  . LYS A 1 212 ? 53.829  -17.096 8.335   0.85   52.26  ? 212  LYS A CA  1 
ATOM   1555 C C   . LYS A 1 212 ? 54.189  -17.260 9.805   0.85   52.32  ? 212  LYS A C   1 
ATOM   1556 O O   . LYS A 1 212 ? 54.347  -16.271 10.531  0.85   52.19  ? 212  LYS A O   1 
ATOM   1557 C CB  . LYS A 1 212 ? 55.035  -16.560 7.544   0.85   52.47  ? 212  LYS A CB  1 
ATOM   1558 C CG  . LYS A 1 212 ? 56.255  -17.496 7.515   0.85   52.94  ? 212  LYS A CG  1 
ATOM   1559 C CD  . LYS A 1 212 ? 55.903  -18.838 6.839   0.85   54.16  ? 212  LYS A CD  1 
ATOM   1560 C CE  . LYS A 1 212 ? 57.089  -19.811 6.854   0.85   54.79  ? 212  LYS A CE  1 
ATOM   1561 N NZ  . LYS A 1 212 ? 56.676  -21.177 6.392   0.85   54.52  ? 212  LYS A NZ  1 
ATOM   1562 N N   . ASP A 1 213 ? 54.294  -18.523 10.223  1.00   52.55  ? 213  ASP A N   1 
ATOM   1563 C CA  . ASP A 1 213 ? 54.723  -18.912 11.571  1.00   52.73  ? 213  ASP A CA  1 
ATOM   1564 C C   . ASP A 1 213 ? 53.827  -18.402 12.696  1.00   52.57  ? 213  ASP A C   1 
ATOM   1565 O O   . ASP A 1 213 ? 54.277  -18.217 13.831  1.00   52.89  ? 213  ASP A O   1 
ATOM   1566 C CB  . ASP A 1 213 ? 56.188  -18.523 11.818  1.00   53.07  ? 213  ASP A CB  1 
ATOM   1567 C CG  . ASP A 1 213 ? 57.156  -19.301 10.945  1.00   53.78  ? 213  ASP A CG  1 
ATOM   1568 O OD1 . ASP A 1 213 ? 58.161  -18.703 10.509  1.00   55.19  ? 213  ASP A OD1 1 
ATOM   1569 O OD2 . ASP A 1 213 ? 56.914  -20.503 10.689  1.00   54.57  ? 213  ASP A OD2 1 
ATOM   1570 N N   . ARG A 1 214 ? 52.558  -18.176 12.381  0.73   52.08  ? 214  ARG A N   1 
ATOM   1571 C CA  . ARG A 1 214 ? 51.596  -17.732 13.379  0.73   51.65  ? 214  ARG A CA  1 
ATOM   1572 C C   . ARG A 1 214 ? 50.293  -18.512 13.231  0.73   50.94  ? 214  ARG A C   1 
ATOM   1573 O O   . ARG A 1 214 ? 50.038  -19.123 12.188  0.73   50.66  ? 214  ARG A O   1 
ATOM   1574 C CB  . ARG A 1 214 ? 51.382  -16.209 13.297  0.73   51.97  ? 214  ARG A CB  1 
ATOM   1575 C CG  . ARG A 1 214 ? 50.838  -15.702 11.965  0.73   52.89  ? 214  ARG A CG  1 
ATOM   1576 C CD  . ARG A 1 214 ? 51.368  -14.310 11.595  0.73   54.01  ? 214  ARG A CD  1 
ATOM   1577 N NE  . ARG A 1 214 ? 50.743  -13.244 12.375  0.73   54.51  ? 214  ARG A NE  1 
ATOM   1578 C CZ  . ARG A 1 214 ? 51.399  -12.420 13.189  0.73   55.69  ? 214  ARG A CZ  1 
ATOM   1579 N NH1 . ARG A 1 214 ? 52.719  -12.524 13.338  0.73   55.99  ? 214  ARG A NH1 1 
ATOM   1580 N NH2 . ARG A 1 214 ? 50.732  -11.484 13.855  0.73   55.93  ? 214  ARG A NH2 1 
ATOM   1581 N N   . VAL A 1 215 ? 49.487  -18.516 14.289  1.00   50.14  ? 215  VAL A N   1 
ATOM   1582 C CA  . VAL A 1 215 ? 48.210  -19.214 14.266  1.00   49.41  ? 215  VAL A CA  1 
ATOM   1583 C C   . VAL A 1 215 ? 47.233  -18.456 13.361  1.00   48.69  ? 215  VAL A C   1 
ATOM   1584 O O   . VAL A 1 215 ? 47.103  -17.241 13.458  1.00   48.73  ? 215  VAL A O   1 
ATOM   1585 C CB  . VAL A 1 215 ? 47.633  -19.385 15.690  1.00   49.43  ? 215  VAL A CB  1 
ATOM   1586 C CG1 . VAL A 1 215 ? 46.380  -20.240 15.664  1.00   49.52  ? 215  VAL A CG1 1 
ATOM   1587 C CG2 . VAL A 1 215 ? 48.670  -20.018 16.616  1.00   49.96  ? 215  VAL A CG2 1 
ATOM   1588 N N   . ALA A 1 216 ? 46.572  -19.176 12.463  1.00   47.88  ? 216  ALA A N   1 
ATOM   1589 C CA  . ALA A 1 216 ? 45.589  -18.568 11.574  1.00   47.16  ? 216  ALA A CA  1 
ATOM   1590 C C   . ALA A 1 216 ? 44.167  -18.911 12.018  1.00   46.51  ? 216  ALA A C   1 
ATOM   1591 O O   . ALA A 1 216 ? 43.847  -20.079 12.227  1.00   46.66  ? 216  ALA A O   1 
ATOM   1592 C CB  . ALA A 1 216 ? 45.823  -19.018 10.143  1.00   47.10  ? 216  ALA A CB  1 
ATOM   1593 N N   . ILE A 1 217 ? 43.330  -17.890 12.178  1.00   45.62  ? 217  ILE A N   1 
ATOM   1594 C CA  . ILE A 1 217 ? 41.917  -18.108 12.506  1.00   44.97  ? 217  ILE A CA  1 
ATOM   1595 C C   . ILE A 1 217 ? 40.989  -17.667 11.367  1.00   44.43  ? 217  ILE A C   1 
ATOM   1596 O O   . ILE A 1 217 ? 40.814  -16.471 11.126  1.00   44.05  ? 217  ILE A O   1 
ATOM   1597 C CB  . ILE A 1 217 ? 41.499  -17.395 13.812  1.00   44.64  ? 217  ILE A CB  1 
ATOM   1598 C CG1 . ILE A 1 217 ? 42.507  -17.665 14.936  1.00   44.46  ? 217  ILE A CG1 1 
ATOM   1599 C CG2 . ILE A 1 217 ? 40.103  -17.837 14.216  1.00   44.58  ? 217  ILE A CG2 1 
ATOM   1600 C CD1 . ILE A 1 217 ? 42.349  -16.759 16.149  1.00   42.83  ? 217  ILE A CD1 1 
ATOM   1601 N N   . LEU A 1 218 ? 40.407  -18.641 10.671  1.00   44.05  ? 218  LEU A N   1 
ATOM   1602 C CA  . LEU A 1 218 ? 39.400  -18.368 9.651   1.00   43.98  ? 218  LEU A CA  1 
ATOM   1603 C C   . LEU A 1 218 ? 38.086  -17.978 10.305  1.00   44.40  ? 218  LEU A C   1 
ATOM   1604 O O   . LEU A 1 218 ? 37.540  -18.724 11.121  1.00   44.00  ? 218  LEU A O   1 
ATOM   1605 C CB  . LEU A 1 218 ? 39.181  -19.572 8.747   1.00   43.67  ? 218  LEU A CB  1 
ATOM   1606 C CG  . LEU A 1 218 ? 40.109  -19.736 7.543   1.00   44.30  ? 218  LEU A CG  1 
ATOM   1607 C CD1 . LEU A 1 218 ? 40.105  -21.179 7.058   1.00   43.98  ? 218  LEU A CD1 1 
ATOM   1608 C CD2 . LEU A 1 218 ? 39.749  -18.778 6.402   1.00   43.83  ? 218  LEU A CD2 1 
ATOM   1609 N N   . VAL A 1 219 ? 37.588  -16.799 9.945   1.00   44.70  ? 219  VAL A N   1 
ATOM   1610 C CA  . VAL A 1 219 ? 36.364  -16.283 10.530  1.00   45.67  ? 219  VAL A CA  1 
ATOM   1611 C C   . VAL A 1 219 ? 35.367  -15.925 9.440   1.00   46.49  ? 219  VAL A C   1 
ATOM   1612 O O   . VAL A 1 219 ? 35.646  -15.091 8.566   1.00   46.26  ? 219  VAL A O   1 
ATOM   1613 C CB  . VAL A 1 219 ? 36.620  -15.062 11.447  1.00   45.41  ? 219  VAL A CB  1 
ATOM   1614 C CG1 . VAL A 1 219 ? 35.299  -14.504 11.976  1.00   45.39  ? 219  VAL A CG1 1 
ATOM   1615 C CG2 . VAL A 1 219 ? 37.534  -15.439 12.599  1.00   45.67  ? 219  VAL A CG2 1 
ATOM   1616 N N   . ASP A 1 220 ? 34.216  -16.586 9.498   1.00   47.44  ? 220  ASP A N   1 
ATOM   1617 C CA  . ASP A 1 220 ? 33.099  -16.305 8.615   1.00   48.62  ? 220  ASP A CA  1 
ATOM   1618 C C   . ASP A 1 220 ? 31.788  -16.262 9.407   1.00   49.43  ? 220  ASP A C   1 
ATOM   1619 O O   . ASP A 1 220 ? 31.685  -16.833 10.500  1.00   49.12  ? 220  ASP A O   1 
ATOM   1620 C CB  . ASP A 1 220 ? 33.025  -17.351 7.508   1.00   48.55  ? 220  ASP A CB  1 
ATOM   1621 C CG  . ASP A 1 220 ? 32.572  -16.768 6.182   1.00   49.42  ? 220  ASP A CG  1 
ATOM   1622 O OD1 . ASP A 1 220 ? 32.578  -15.526 6.031   1.00   50.17  ? 220  ASP A OD1 1 
ATOM   1623 O OD2 . ASP A 1 220 ? 32.219  -17.558 5.280   1.00   51.76  ? 220  ASP A OD2 1 
ATOM   1624 N N   . ASP A 1 221 ? 30.794  -15.569 8.859   1.00   50.49  ? 221  ASP A N   1 
ATOM   1625 C CA  . ASP A 1 221 ? 29.476  -15.501 9.488   1.00   51.85  ? 221  ASP A CA  1 
ATOM   1626 C C   . ASP A 1 221 ? 28.772  -16.845 9.395   1.00   52.53  ? 221  ASP A C   1 
ATOM   1627 O O   . ASP A 1 221 ? 27.983  -17.199 10.275  1.00   52.65  ? 221  ASP A O   1 
ATOM   1628 C CB  . ASP A 1 221 ? 28.614  -14.405 8.860   1.00   51.76  ? 221  ASP A CB  1 
ATOM   1629 C CG  . ASP A 1 221 ? 28.403  -14.604 7.366   1.00   52.62  ? 221  ASP A CG  1 
ATOM   1630 O OD1 . ASP A 1 221 ? 27.279  -14.329 6.896   1.00   53.56  ? 221  ASP A OD1 1 
ATOM   1631 O OD2 . ASP A 1 221 ? 29.347  -15.042 6.664   1.00   53.37  ? 221  ASP A OD2 1 
ATOM   1632 N N   . MET A 1 222 ? 29.073  -17.582 8.325   1.00   53.75  ? 222  MET A N   1 
ATOM   1633 C CA  . MET A 1 222 ? 28.452  -18.877 8.056   1.00   54.96  ? 222  MET A CA  1 
ATOM   1634 C C   . MET A 1 222 ? 29.258  -19.751 7.095   1.00   55.54  ? 222  MET A C   1 
ATOM   1635 O O   . MET A 1 222 ? 30.008  -19.250 6.252   1.00   55.69  ? 222  MET A O   1 
ATOM   1636 C CB  . MET A 1 222 ? 27.023  -18.700 7.529   1.00   55.31  ? 222  MET A CB  1 
ATOM   1637 C CG  . MET A 1 222 ? 26.907  -17.995 6.184   1.00   56.16  ? 222  MET A CG  1 
ATOM   1638 S SD  . MET A 1 222 ? 25.185  -17.933 5.638   1.00   59.74  ? 222  MET A SD  1 
ATOM   1639 C CE  . MET A 1 222 ? 24.574  -16.479 6.494   1.00   58.23  ? 222  MET A CE  1 
ATOM   1640 N N   . ALA A 1 223 ? 29.100  -21.062 7.247   1.00   56.14  ? 223  ALA A N   1 
ATOM   1641 C CA  . ALA A 1 223 ? 29.677  -22.035 6.331   1.00   56.83  ? 223  ALA A CA  1 
ATOM   1642 C C   . ALA A 1 223 ? 28.633  -23.090 6.026   1.00   57.28  ? 223  ALA A C   1 
ATOM   1643 O O   . ALA A 1 223 ? 27.976  -23.605 6.930   1.00   57.44  ? 223  ALA A O   1 
ATOM   1644 C CB  . ALA A 1 223 ? 30.911  -22.672 6.925   1.00   56.82  ? 223  ALA A CB  1 
ATOM   1645 N N   . ASP A 1 224 ? 28.484  -23.399 4.743   1.00   57.94  ? 224  ASP A N   1 
ATOM   1646 C CA  . ASP A 1 224 ? 27.455  -24.316 4.279   1.00   58.57  ? 224  ASP A CA  1 
ATOM   1647 C C   . ASP A 1 224 ? 28.062  -25.688 3.971   1.00   58.77  ? 224  ASP A C   1 
ATOM   1648 O O   . ASP A 1 224 ? 28.013  -26.603 4.804   1.00   58.99  ? 224  ASP A O   1 
ATOM   1649 C CB  . ASP A 1 224 ? 26.752  -23.722 3.051   1.00   58.88  ? 224  ASP A CB  1 
ATOM   1650 C CG  . ASP A 1 224 ? 25.671  -24.631 2.488   1.00   59.80  ? 224  ASP A CG  1 
ATOM   1651 O OD1 . ASP A 1 224 ? 25.111  -25.451 3.249   1.00   60.78  ? 224  ASP A OD1 1 
ATOM   1652 O OD2 . ASP A 1 224 ? 25.379  -24.511 1.277   1.00   60.96  ? 224  ASP A OD2 1 
ATOM   1653 N N   . THR A 1 225 ? 28.636  -25.825 2.779   1.00   58.82  ? 225  THR A N   1 
ATOM   1654 C CA  . THR A 1 225 ? 29.283  -27.068 2.366   1.00   58.86  ? 225  THR A CA  1 
ATOM   1655 C C   . THR A 1 225 ? 30.699  -27.122 2.924   1.00   58.78  ? 225  THR A C   1 
ATOM   1656 O O   . THR A 1 225 ? 31.313  -28.191 2.980   1.00   58.81  ? 225  THR A O   1 
ATOM   1657 C CB  . THR A 1 225 ? 29.366  -27.186 0.833   1.00   58.84  ? 225  THR A CB  1 
ATOM   1658 O OG1 . THR A 1 225 ? 30.288  -26.211 0.329   1.00   59.09  ? 225  THR A OG1 1 
ATOM   1659 C CG2 . THR A 1 225 ? 27.998  -26.962 0.195   1.00   59.02  ? 225  THR A CG2 1 
ATOM   1660 N N   . CYS A 1 226 ? 31.210  -25.953 3.311   1.00   58.50  ? 226  CYS A N   1 
ATOM   1661 C CA  . CYS A 1 226 ? 32.566  -25.794 3.838   1.00   58.36  ? 226  CYS A CA  1 
ATOM   1662 C C   . CYS A 1 226 ? 33.661  -25.976 2.787   1.00   58.41  ? 226  CYS A C   1 
ATOM   1663 O O   . CYS A 1 226 ? 34.835  -26.067 3.134   1.00   58.32  ? 226  CYS A O   1 
ATOM   1664 C CB  . CYS A 1 226 ? 32.812  -26.723 5.033   1.00   58.46  ? 226  CYS A CB  1 
ATOM   1665 S SG  . CYS A 1 226 ? 31.890  -26.269 6.498   1.00   57.20  ? 226  CYS A SG  1 
ATOM   1666 N N   . GLY A 1 227 ? 33.272  -26.016 1.512   1.00   58.56  ? 227  GLY A N   1 
ATOM   1667 C CA  . GLY A 1 227 ? 34.229  -26.124 0.409   1.00   58.78  ? 227  GLY A CA  1 
ATOM   1668 C C   . GLY A 1 227 ? 35.254  -25.009 0.450   1.00   58.89  ? 227  GLY A C   1 
ATOM   1669 O O   . GLY A 1 227 ? 36.461  -25.264 0.459   1.00   58.84  ? 227  GLY A O   1 
ATOM   1670 N N   . THR A 1 228 ? 34.756  -23.773 0.501   1.00   58.99  ? 228  THR A N   1 
ATOM   1671 C CA  . THR A 1 228 ? 35.594  -22.580 0.600   1.00   59.11  ? 228  THR A CA  1 
ATOM   1672 C C   . THR A 1 228 ? 36.484  -22.595 1.849   1.00   59.07  ? 228  THR A C   1 
ATOM   1673 O O   . THR A 1 228 ? 37.697  -22.415 1.743   1.00   58.96  ? 228  THR A O   1 
ATOM   1674 C CB  . THR A 1 228 ? 34.734  -21.289 0.544   1.00   59.13  ? 228  THR A CB  1 
ATOM   1675 O OG1 . THR A 1 228 ? 34.122  -21.184 -0.748  1.00   59.71  ? 228  THR A OG1 1 
ATOM   1676 C CG2 . THR A 1 228 ? 35.580  -20.047 0.792   1.00   59.20  ? 228  THR A CG2 1 
ATOM   1677 N N   . ILE A 1 229 ? 35.889  -22.832 3.019   1.00   59.16  ? 229  ILE A N   1 
ATOM   1678 C CA  . ILE A 1 229 ? 36.644  -22.782 4.276   1.00   59.37  ? 229  ILE A CA  1 
ATOM   1679 C C   . ILE A 1 229 ? 37.711  -23.882 4.381   1.00   59.41  ? 229  ILE A C   1 
ATOM   1680 O O   . ILE A 1 229 ? 38.770  -23.669 4.981   1.00   59.23  ? 229  ILE A O   1 
ATOM   1681 C CB  . ILE A 1 229 ? 35.717  -22.740 5.528   1.00   59.46  ? 229  ILE A CB  1 
ATOM   1682 C CG1 . ILE A 1 229 ? 36.415  -22.008 6.677   1.00   59.66  ? 229  ILE A CG1 1 
ATOM   1683 C CG2 . ILE A 1 229 ? 35.259  -24.141 5.940   1.00   59.30  ? 229  ILE A CG2 1 
ATOM   1684 C CD1 . ILE A 1 229 ? 35.477  -21.287 7.624   1.00   59.90  ? 229  ILE A CD1 1 
ATOM   1685 N N   . CYS A 1 230 ? 37.429  -25.040 3.781   1.00   59.42  ? 230  CYS A N   1 
ATOM   1686 C CA  . CYS A 1 230 ? 38.366  -26.160 3.772   1.00   59.48  ? 230  CYS A CA  1 
ATOM   1687 C C   . CYS A 1 230 ? 39.519  -25.937 2.798   1.00   59.22  ? 230  CYS A C   1 
ATOM   1688 O O   . CYS A 1 230 ? 40.675  -26.204 3.135   1.00   59.04  ? 230  CYS A O   1 
ATOM   1689 C CB  . CYS A 1 230 ? 37.644  -27.480 3.490   1.00   59.56  ? 230  CYS A CB  1 
ATOM   1690 S SG  . CYS A 1 230 ? 36.600  -28.025 4.881   1.00   60.82  ? 230  CYS A SG  1 
ATOM   1691 N N   . HIS A 1 231 ? 39.205  -25.441 1.601   1.00   59.11  ? 231  HIS A N   1 
ATOM   1692 C CA  . HIS A 1 231 ? 40.250  -25.042 0.652   1.00   59.14  ? 231  HIS A CA  1 
ATOM   1693 C C   . HIS A 1 231 ? 41.091  -23.893 1.217   1.00   58.79  ? 231  HIS A C   1 
ATOM   1694 O O   . HIS A 1 231 ? 42.309  -23.863 1.023   1.00   58.93  ? 231  HIS A O   1 
ATOM   1695 C CB  . HIS A 1 231 ? 39.660  -24.656 -0.708  1.00   59.45  ? 231  HIS A CB  1 
ATOM   1696 C CG  . HIS A 1 231 ? 39.008  -25.790 -1.437  1.00   60.38  ? 231  HIS A CG  1 
ATOM   1697 N ND1 . HIS A 1 231 ? 39.526  -27.085 -1.428  1.00   61.21  ? 231  HIS A ND1 1 
ATOM   1698 C CD2 . HIS A 1 231 ? 37.886  -25.817 -2.217  1.00   61.29  ? 231  HIS A CD2 1 
ATOM   1699 C CE1 . HIS A 1 231 ? 38.745  -27.863 -2.157  1.00   63.29  ? 231  HIS A CE1 1 
ATOM   1700 N NE2 . HIS A 1 231 ? 37.743  -27.118 -2.648  1.00   63.74  ? 231  HIS A NE2 1 
ATOM   1701 N N   . ALA A 1 232 ? 40.435  -22.965 1.921   1.00   58.10  ? 232  ALA A N   1 
ATOM   1702 C CA  . ALA A 1 232 ? 41.113  -21.851 2.591   1.00   57.59  ? 232  ALA A CA  1 
ATOM   1703 C C   . ALA A 1 232 ? 42.139  -22.339 3.604   1.00   57.32  ? 232  ALA A C   1 
ATOM   1704 O O   . ALA A 1 232 ? 43.246  -21.795 3.687   1.00   57.11  ? 232  ALA A O   1 
ATOM   1705 C CB  . ALA A 1 232 ? 40.101  -20.941 3.271   1.00   57.52  ? 232  ALA A CB  1 
ATOM   1706 N N   . ALA A 1 233 ? 41.759  -23.362 4.370   1.00   57.00  ? 233  ALA A N   1 
ATOM   1707 C CA  . ALA A 1 233 ? 42.621  -23.942 5.398   1.00   57.09  ? 233  ALA A CA  1 
ATOM   1708 C C   . ALA A 1 233 ? 43.900  -24.559 4.826   1.00   57.06  ? 233  ALA A C   1 
ATOM   1709 O O   . ALA A 1 233 ? 44.950  -24.523 5.472   1.00   56.86  ? 233  ALA A O   1 
ATOM   1710 C CB  . ALA A 1 233 ? 41.856  -24.974 6.203   1.00   56.95  ? 233  ALA A CB  1 
ATOM   1711 N N   . ASP A 1 234 ? 43.797  -25.125 3.624   1.00   57.34  ? 234  ASP A N   1 
ATOM   1712 C CA  . ASP A 1 234 ? 44.939  -25.743 2.946   1.00   57.78  ? 234  ASP A CA  1 
ATOM   1713 C C   . ASP A 1 234 ? 45.927  -24.678 2.506   1.00   57.71  ? 234  ASP A C   1 
ATOM   1714 O O   . ASP A 1 234 ? 47.133  -24.800 2.747   1.00   57.71  ? 234  ASP A O   1 
ATOM   1715 C CB  . ASP A 1 234 ? 44.482  -26.556 1.729   1.00   57.95  ? 234  ASP A CB  1 
ATOM   1716 C CG  . ASP A 1 234 ? 43.364  -27.532 2.058   1.00   59.04  ? 234  ASP A CG  1 
ATOM   1717 O OD1 . ASP A 1 234 ? 43.244  -27.942 3.237   1.00   60.63  ? 234  ASP A OD1 1 
ATOM   1718 O OD2 . ASP A 1 234 ? 42.599  -27.890 1.130   1.00   59.92  ? 234  ASP A OD2 1 
ATOM   1719 N N   . LYS A 1 235 ? 45.401  -23.630 1.874   1.00   57.70  ? 235  LYS A N   1 
ATOM   1720 C CA  . LYS A 1 235 ? 46.208  -22.503 1.417   1.00   57.79  ? 235  LYS A CA  1 
ATOM   1721 C C   . LYS A 1 235 ? 46.939  -21.856 2.593   1.00   57.67  ? 235  LYS A C   1 
ATOM   1722 O O   . LYS A 1 235 ? 48.119  -21.519 2.485   1.00   57.65  ? 235  LYS A O   1 
ATOM   1723 C CB  . LYS A 1 235 ? 45.329  -21.471 0.698   1.00   57.98  ? 235  LYS A CB  1 
ATOM   1724 C CG  . LYS A 1 235 ? 45.948  -20.850 -0.565  1.00   58.67  ? 235  LYS A CG  1 
ATOM   1725 C CD  . LYS A 1 235 ? 47.096  -19.890 -0.248  1.00   60.15  ? 235  LYS A CD  1 
ATOM   1726 C CE  . LYS A 1 235 ? 47.774  -19.398 -1.520  1.00   60.82  ? 235  LYS A CE  1 
ATOM   1727 N NZ  . LYS A 1 235 ? 48.863  -18.413 -1.199  1.00   61.60  ? 235  LYS A NZ  1 
ATOM   1728 N N   . LEU A 1 236 ? 46.242  -21.698 3.716   1.00   57.58  ? 236  LEU A N   1 
ATOM   1729 C CA  . LEU A 1 236 ? 46.844  -21.131 4.923   1.00   57.72  ? 236  LEU A CA  1 
ATOM   1730 C C   . LEU A 1 236 ? 48.011  -21.971 5.445   1.00   57.80  ? 236  LEU A C   1 
ATOM   1731 O O   . LEU A 1 236 ? 49.031  -21.424 5.867   1.00   57.89  ? 236  LEU A O   1 
ATOM   1732 C CB  . LEU A 1 236 ? 45.796  -20.941 6.024   1.00   57.61  ? 236  LEU A CB  1 
ATOM   1733 C CG  . LEU A 1 236 ? 44.835  -19.752 5.912   1.00   57.81  ? 236  LEU A CG  1 
ATOM   1734 C CD1 . LEU A 1 236 ? 43.819  -19.796 7.041   1.00   57.16  ? 236  LEU A CD1 1 
ATOM   1735 C CD2 . LEU A 1 236 ? 45.584  -18.421 5.913   1.00   57.89  ? 236  LEU A CD2 1 
ATOM   1736 N N   . LEU A 1 237 ? 47.854  -23.293 5.411   1.00   57.88  ? 237  LEU A N   1 
ATOM   1737 C CA  . LEU A 1 237 ? 48.920  -24.203 5.834   1.00   58.09  ? 237  LEU A CA  1 
ATOM   1738 C C   . LEU A 1 237 ? 50.135  -24.128 4.911   1.00   58.05  ? 237  LEU A C   1 
ATOM   1739 O O   . LEU A 1 237 ? 51.277  -24.127 5.380   1.00   58.38  ? 237  LEU A O   1 
ATOM   1740 C CB  . LEU A 1 237 ? 48.417  -25.646 5.911   1.00   57.93  ? 237  LEU A CB  1 
ATOM   1741 C CG  . LEU A 1 237 ? 47.751  -26.186 7.182   1.00   57.97  ? 237  LEU A CG  1 
ATOM   1742 C CD1 . LEU A 1 237 ? 47.710  -27.699 7.073   1.00   58.43  ? 237  LEU A CD1 1 
ATOM   1743 C CD2 . LEU A 1 237 ? 48.475  -25.786 8.462   1.00   57.25  ? 237  LEU A CD2 1 
ATOM   1744 N N   . SER A 1 238 ? 49.872  -24.063 3.605   1.00   58.03  ? 238  SER A N   1 
ATOM   1745 C CA  . SER A 1 238 ? 50.910  -23.910 2.578   1.00   57.95  ? 238  SER A CA  1 
ATOM   1746 C C   . SER A 1 238 ? 51.719  -22.621 2.738   1.00   57.86  ? 238  SER A C   1 
ATOM   1747 O O   . SER A 1 238 ? 52.887  -22.556 2.340   1.00   58.00  ? 238  SER A O   1 
ATOM   1748 C CB  . SER A 1 238 ? 50.280  -23.941 1.184   1.00   57.89  ? 238  SER A CB  1 
ATOM   1749 O OG  . SER A 1 238 ? 49.463  -25.093 1.012   1.00   58.30  ? 238  SER A OG  1 
ATOM   1750 N N   . ALA A 1 239 ? 51.086  -21.600 3.312   1.00   57.58  ? 239  ALA A N   1 
ATOM   1751 C CA  . ALA A 1 239 ? 51.712  -20.299 3.522   1.00   57.30  ? 239  ALA A CA  1 
ATOM   1752 C C   . ALA A 1 239 ? 52.424  -20.223 4.871   1.00   57.29  ? 239  ALA A C   1 
ATOM   1753 O O   . ALA A 1 239 ? 52.933  -19.164 5.254   1.00   57.23  ? 239  ALA A O   1 
ATOM   1754 C CB  . ALA A 1 239 ? 50.675  -19.188 3.392   1.00   57.26  ? 239  ALA A CB  1 
ATOM   1755 N N   . GLY A 1 240 ? 52.442  -21.347 5.592   1.00   57.29  ? 240  GLY A N   1 
ATOM   1756 C CA  . GLY A 1 240 ? 53.241  -21.480 6.807   1.00   57.04  ? 240  GLY A CA  1 
ATOM   1757 C C   . GLY A 1 240 ? 52.566  -21.062 8.096   1.00   57.11  ? 240  GLY A C   1 
ATOM   1758 O O   . GLY A 1 240 ? 53.239  -20.614 9.038   1.00   56.92  ? 240  GLY A O   1 
ATOM   1759 N N   . ALA A 1 241 ? 51.238  -21.195 8.145   1.00   56.98  ? 241  ALA A N   1 
ATOM   1760 C CA  . ALA A 1 241 ? 50.503  -20.968 9.383   1.00   56.81  ? 241  ALA A CA  1 
ATOM   1761 C C   . ALA A 1 241 ? 50.788  -22.122 10.333  1.00   56.74  ? 241  ALA A C   1 
ATOM   1762 O O   . ALA A 1 241 ? 50.764  -23.286 9.924   1.00   56.61  ? 241  ALA A O   1 
ATOM   1763 C CB  . ALA A 1 241 ? 49.011  -20.862 9.114   1.00   57.00  ? 241  ALA A CB  1 
ATOM   1764 N N   . THR A 1 242 ? 51.065  -21.787 11.592  1.00   56.49  ? 242  THR A N   1 
ATOM   1765 C CA  . THR A 1 242 ? 51.337  -22.778 12.633  1.00   56.52  ? 242  THR A CA  1 
ATOM   1766 C C   . THR A 1 242 ? 50.187  -23.782 12.729  1.00   56.22  ? 242  THR A C   1 
ATOM   1767 O O   . THR A 1 242 ? 50.353  -24.969 12.443  1.00   56.37  ? 242  THR A O   1 
ATOM   1768 C CB  . THR A 1 242 ? 51.536  -22.102 14.007  1.00   56.52  ? 242  THR A CB  1 
ATOM   1769 O OG1 . THR A 1 242 ? 52.488  -21.035 13.891  1.00   57.30  ? 242  THR A OG1 1 
ATOM   1770 C CG2 . THR A 1 242 ? 52.022  -23.113 15.038  1.00   56.73  ? 242  THR A CG2 1 
ATOM   1771 N N   . ARG A 1 243 ? 49.021  -23.282 13.133  1.00   55.75  ? 243  ARG A N   1 
ATOM   1772 C CA  . ARG A 1 243 ? 47.787  -24.062 13.192  1.00   55.05  ? 243  ARG A CA  1 
ATOM   1773 C C   . ARG A 1 243 ? 46.642  -23.200 12.666  1.00   54.35  ? 243  ARG A C   1 
ATOM   1774 O O   . ARG A 1 243 ? 46.692  -21.966 12.747  1.00   54.04  ? 243  ARG A O   1 
ATOM   1775 C CB  . ARG A 1 243 ? 47.485  -24.491 14.629  1.00   55.14  ? 243  ARG A CB  1 
ATOM   1776 C CG  . ARG A 1 243 ? 48.559  -25.371 15.280  1.00   56.31  ? 243  ARG A CG  1 
ATOM   1777 C CD  . ARG A 1 243 ? 48.274  -25.585 16.758  1.00   57.66  ? 243  ARG A CD  1 
ATOM   1778 N NE  . ARG A 1 243 ? 48.226  -24.324 17.497  1.00   58.52  ? 243  ARG A NE  1 
ATOM   1779 C CZ  . ARG A 1 243 ? 47.494  -24.124 18.590  1.00   58.86  ? 243  ARG A CZ  1 
ATOM   1780 N NH1 . ARG A 1 243 ? 46.741  -25.100 19.080  1.00   59.45  ? 243  ARG A NH1 1 
ATOM   1781 N NH2 . ARG A 1 243 ? 47.507  -22.942 19.192  1.00   58.99  ? 243  ARG A NH2 1 
ATOM   1782 N N   . VAL A 1 244 ? 45.608  -23.853 12.144  1.00   53.43  ? 244  VAL A N   1 
ATOM   1783 C CA  . VAL A 1 244 ? 44.454  -23.147 11.597  1.00   52.79  ? 244  VAL A CA  1 
ATOM   1784 C C   . VAL A 1 244 ? 43.149  -23.466 12.346  1.00   52.18  ? 244  VAL A C   1 
ATOM   1785 O O   . VAL A 1 244 ? 42.819  -24.627 12.586  1.00   52.04  ? 244  VAL A O   1 
ATOM   1786 C CB  . VAL A 1 244 ? 44.320  -23.368 10.061  1.00   52.69  ? 244  VAL A CB  1 
ATOM   1787 C CG1 . VAL A 1 244 ? 44.456  -24.836 9.704   1.00   53.09  ? 244  VAL A CG1 1 
ATOM   1788 C CG2 . VAL A 1 244 ? 43.031  -22.774 9.520   1.00   52.39  ? 244  VAL A CG2 1 
ATOM   1789 N N   . TYR A 1 245 ? 42.433  -22.411 12.728  0.99   51.42  ? 245  TYR A N   1 
ATOM   1790 C CA  . TYR A 1 245 ? 41.115  -22.529 13.340  0.99   50.74  ? 245  TYR A CA  1 
ATOM   1791 C C   . TYR A 1 245 ? 40.047  -21.962 12.410  0.99   50.35  ? 245  TYR A C   1 
ATOM   1792 O O   . TYR A 1 245 ? 40.338  -21.124 11.545  0.99   49.93  ? 245  TYR A O   1 
ATOM   1793 C CB  . TYR A 1 245 ? 41.067  -21.785 14.672  0.99   50.65  ? 245  TYR A CB  1 
ATOM   1794 C CG  . TYR A 1 245 ? 41.921  -22.381 15.769  0.99   51.43  ? 245  TYR A CG  1 
ATOM   1795 C CD1 . TYR A 1 245 ? 43.287  -22.100 15.847  0.99   51.80  ? 245  TYR A CD1 1 
ATOM   1796 C CD2 . TYR A 1 245 ? 41.359  -23.211 16.742  0.99   51.42  ? 245  TYR A CD2 1 
ATOM   1797 C CE1 . TYR A 1 245 ? 44.076  -22.638 16.860  0.99   52.35  ? 245  TYR A CE1 1 
ATOM   1798 C CE2 . TYR A 1 245 ? 42.137  -23.750 17.760  0.99   51.45  ? 245  TYR A CE2 1 
ATOM   1799 C CZ  . TYR A 1 245 ? 43.497  -23.458 17.810  0.99   52.53  ? 245  TYR A CZ  1 
ATOM   1800 O OH  . TYR A 1 245 ? 44.283  -23.984 18.806  0.99   53.73  ? 245  TYR A OH  1 
ATOM   1801 N N   . ALA A 1 246 ? 38.813  -22.423 12.594  1.00   49.62  ? 246  ALA A N   1 
ATOM   1802 C CA  . ALA A 1 246 ? 37.674  -21.918 11.827  1.00   49.26  ? 246  ALA A CA  1 
ATOM   1803 C C   . ALA A 1 246 ? 36.551  -21.496 12.769  1.00   48.95  ? 246  ALA A C   1 
ATOM   1804 O O   . ALA A 1 246 ? 36.048  -22.305 13.551  1.00   48.58  ? 246  ALA A O   1 
ATOM   1805 C CB  . ALA A 1 246 ? 37.186  -22.958 10.839  1.00   49.15  ? 246  ALA A CB  1 
ATOM   1806 N N   . ILE A 1 247 ? 36.187  -20.219 12.705  1.00   48.74  ? 247  ILE A N   1 
ATOM   1807 C CA  . ILE A 1 247 ? 35.142  -19.672 13.562  1.00   48.85  ? 247  ILE A CA  1 
ATOM   1808 C C   . ILE A 1 247 ? 33.966  -19.187 12.727  1.00   49.13  ? 247  ILE A C   1 
ATOM   1809 O O   . ILE A 1 247 ? 34.109  -18.341 11.839  1.00   48.91  ? 247  ILE A O   1 
ATOM   1810 C CB  . ILE A 1 247 ? 35.663  -18.549 14.493  1.00   48.79  ? 247  ILE A CB  1 
ATOM   1811 C CG1 . ILE A 1 247 ? 36.759  -19.096 15.416  1.00   48.23  ? 247  ILE A CG1 1 
ATOM   1812 C CG2 . ILE A 1 247 ? 34.513  -17.944 15.288  1.00   48.64  ? 247  ILE A CG2 1 
ATOM   1813 C CD1 . ILE A 1 247 ? 37.323  -18.096 16.406  1.00   48.81  ? 247  ILE A CD1 1 
ATOM   1814 N N   . LEU A 1 248 ? 32.803  -19.753 13.022  1.00   49.72  ? 248  LEU A N   1 
ATOM   1815 C CA  . LEU A 1 248 ? 31.590  -19.501 12.258  1.00   50.52  ? 248  LEU A CA  1 
ATOM   1816 C C   . LEU A 1 248 ? 30.446  -19.277 13.226  1.00   50.98  ? 248  LEU A C   1 
ATOM   1817 O O   . LEU A 1 248 ? 30.191  -20.119 14.089  1.00   51.03  ? 248  LEU A O   1 
ATOM   1818 C CB  . LEU A 1 248 ? 31.279  -20.706 11.373  1.00   50.31  ? 248  LEU A CB  1 
ATOM   1819 C CG  . LEU A 1 248 ? 32.405  -21.172 10.456  1.00   50.73  ? 248  LEU A CG  1 
ATOM   1820 C CD1 . LEU A 1 248 ? 32.379  -22.681 10.274  1.00   51.29  ? 248  LEU A CD1 1 
ATOM   1821 C CD2 . LEU A 1 248 ? 32.316  -20.449 9.126   1.00   51.01  ? 248  LEU A CD2 1 
ATOM   1822 N N   . THR A 1 249 ? 29.763  -18.145 13.108  1.00   51.42  ? 249  THR A N   1 
ATOM   1823 C CA  . THR A 1 249 ? 28.594  -17.917 13.954  1.00   52.04  ? 249  THR A CA  1 
ATOM   1824 C C   . THR A 1 249 ? 27.439  -18.833 13.546  1.00   52.30  ? 249  THR A C   1 
ATOM   1825 O O   . THR A 1 249 ? 26.795  -19.452 14.405  1.00   52.25  ? 249  THR A O   1 
ATOM   1826 C CB  . THR A 1 249 ? 28.167  -16.424 14.043  1.00   52.15  ? 249  THR A CB  1 
ATOM   1827 O OG1 . THR A 1 249 ? 26.732  -16.327 14.005  1.00   53.23  ? 249  THR A OG1 1 
ATOM   1828 C CG2 . THR A 1 249 ? 28.765  -15.602 12.911  1.00   52.52  ? 249  THR A CG2 1 
ATOM   1829 N N   . HIS A 1 250 ? 27.207  -18.955 12.241  1.00   52.48  ? 250  HIS A N   1 
ATOM   1830 C CA  . HIS A 1 250 ? 26.172  -19.856 11.740  1.00   52.81  ? 250  HIS A CA  1 
ATOM   1831 C C   . HIS A 1 250 ? 26.797  -21.090 11.094  1.00   53.58  ? 250  HIS A C   1 
ATOM   1832 O O   . HIS A 1 250 ? 27.455  -20.993 10.053  1.00   53.27  ? 250  HIS A O   1 
ATOM   1833 C CB  . HIS A 1 250 ? 25.236  -19.135 10.761  1.00   52.32  ? 250  HIS A CB  1 
ATOM   1834 C CG  . HIS A 1 250 ? 24.661  -17.861 11.298  1.00   51.11  ? 250  HIS A CG  1 
ATOM   1835 N ND1 . HIS A 1 250 ? 23.813  -17.827 12.384  1.00   49.99  ? 250  HIS A ND1 1 
ATOM   1836 C CD2 . HIS A 1 250 ? 24.808  -16.573 10.892  1.00   50.07  ? 250  HIS A CD2 1 
ATOM   1837 C CE1 . HIS A 1 250 ? 23.470  -16.575 12.633  1.00   49.22  ? 250  HIS A CE1 1 
ATOM   1838 N NE2 . HIS A 1 250 ? 24.057  -15.795 11.740  1.00   50.38  ? 250  HIS A NE2 1 
ATOM   1839 N N   . GLY A 1 251 ? 26.600  -22.243 11.730  1.00   54.52  ? 251  GLY A N   1 
ATOM   1840 C CA  . GLY A 1 251 ? 27.157  -23.500 11.239  1.00   56.09  ? 251  GLY A CA  1 
ATOM   1841 C C   . GLY A 1 251 ? 26.022  -24.308 10.642  1.00   57.29  ? 251  GLY A C   1 
ATOM   1842 O O   . GLY A 1 251 ? 25.254  -24.947 11.367  1.00   57.43  ? 251  GLY A O   1 
ATOM   1843 N N   . ILE A 1 252 ? 25.914  -24.282 9.316   1.00   58.48  ? 252  ILE A N   1 
ATOM   1844 C CA  . ILE A 1 252 ? 24.872  -25.033 8.615   1.00   59.77  ? 252  ILE A CA  1 
ATOM   1845 C C   . ILE A 1 252 ? 25.397  -26.461 8.388   1.00   60.60  ? 252  ILE A C   1 
ATOM   1846 O O   . ILE A 1 252 ? 24.675  -27.434 8.622   1.00   60.61  ? 252  ILE A O   1 
ATOM   1847 C CB  . ILE A 1 252 ? 24.434  -24.375 7.282   1.00   59.90  ? 252  ILE A CB  1 
ATOM   1848 C CG1 . ILE A 1 252 ? 23.953  -22.937 7.526   1.00   60.00  ? 252  ILE A CG1 1 
ATOM   1849 C CG2 . ILE A 1 252 ? 23.346  -25.209 6.613   1.00   59.83  ? 252  ILE A CG2 1 
ATOM   1850 C CD1 . ILE A 1 252 ? 23.964  -22.049 6.299   1.00   60.78  ? 252  ILE A CD1 1 
ATOM   1851 N N   . PHE A 1 253 ? 26.649  -26.564 7.934   1.00   61.66  ? 253  PHE A N   1 
ATOM   1852 C CA  . PHE A 1 253 ? 27.377  -27.839 7.808   1.00   62.71  ? 253  PHE A CA  1 
ATOM   1853 C C   . PHE A 1 253 ? 26.650  -28.960 7.053   1.00   63.42  ? 253  PHE A C   1 
ATOM   1854 O O   . PHE A 1 253 ? 26.735  -30.128 7.439   1.00   63.63  ? 253  PHE A O   1 
ATOM   1855 C CB  . PHE A 1 253 ? 27.816  -28.358 9.186   1.00   62.77  ? 253  PHE A CB  1 
ATOM   1856 C CG  . PHE A 1 253 ? 28.805  -27.479 9.893   1.00   63.10  ? 253  PHE A CG  1 
ATOM   1857 C CD1 . PHE A 1 253 ? 28.708  -27.283 11.264  1.00   63.54  ? 253  PHE A CD1 1 
ATOM   1858 C CD2 . PHE A 1 253 ? 29.837  -26.859 9.199   1.00   63.41  ? 253  PHE A CD2 1 
ATOM   1859 C CE1 . PHE A 1 253 ? 29.623  -26.482 11.932  1.00   63.80  ? 253  PHE A CE1 1 
ATOM   1860 C CE2 . PHE A 1 253 ? 30.752  -26.051 9.857   1.00   63.58  ? 253  PHE A CE2 1 
ATOM   1861 C CZ  . PHE A 1 253 ? 30.647  -25.863 11.223  1.00   63.67  ? 253  PHE A CZ  1 
ATOM   1862 N N   . SER A 1 254 ? 25.959  -28.615 5.975   1.00   64.34  ? 254  SER A N   1 
ATOM   1863 C CA  . SER A 1 254 ? 25.217  -29.614 5.209   1.00   65.35  ? 254  SER A CA  1 
ATOM   1864 C C   . SER A 1 254 ? 26.075  -30.287 4.140   1.00   66.07  ? 254  SER A C   1 
ATOM   1865 O O   . SER A 1 254 ? 27.124  -29.762 3.751   1.00   66.15  ? 254  SER A O   1 
ATOM   1866 C CB  . SER A 1 254 ? 23.985  -28.981 4.570   1.00   65.28  ? 254  SER A CB  1 
ATOM   1867 O OG  . SER A 1 254 ? 24.363  -27.962 3.663   1.00   65.31  ? 254  SER A OG  1 
ATOM   1868 N N   . GLY A 1 255 ? 25.615  -31.447 3.671   1.00   66.85  ? 255  GLY A N   1 
ATOM   1869 C CA  . GLY A 1 255 ? 26.271  -32.179 2.587   1.00   67.63  ? 255  GLY A CA  1 
ATOM   1870 C C   . GLY A 1 255 ? 27.590  -32.813 2.997   1.00   68.27  ? 255  GLY A C   1 
ATOM   1871 O O   . GLY A 1 255 ? 27.642  -33.554 3.985   1.00   68.37  ? 255  GLY A O   1 
ATOM   1872 N N   . PRO A 1 256 ? 28.667  -32.518 2.240   1.00   68.74  ? 256  PRO A N   1 
ATOM   1873 C CA  . PRO A 1 256 ? 30.000  -33.071 2.496   1.00   69.11  ? 256  PRO A CA  1 
ATOM   1874 C C   . PRO A 1 256 ? 30.746  -32.363 3.628   1.00   69.47  ? 256  PRO A C   1 
ATOM   1875 O O   . PRO A 1 256 ? 31.855  -32.783 3.997   1.00   69.60  ? 256  PRO A O   1 
ATOM   1876 C CB  . PRO A 1 256 ? 30.726  -32.834 1.169   1.00   69.10  ? 256  PRO A CB  1 
ATOM   1877 C CG  . PRO A 1 256 ? 30.096  -31.603 0.623   1.00   68.98  ? 256  PRO A CG  1 
ATOM   1878 C CD  . PRO A 1 256 ? 28.652  -31.654 1.042   1.00   68.77  ? 256  PRO A CD  1 
ATOM   1879 N N   . ALA A 1 257 ? 30.129  -31.308 4.170   1.00   69.79  ? 257  ALA A N   1 
ATOM   1880 C CA  . ALA A 1 257 ? 30.779  -30.418 5.136   1.00   70.13  ? 257  ALA A CA  1 
ATOM   1881 C C   . ALA A 1 257 ? 31.432  -31.123 6.315   1.00   70.34  ? 257  ALA A C   1 
ATOM   1882 O O   . ALA A 1 257 ? 32.607  -30.892 6.599   1.00   70.43  ? 257  ALA A O   1 
ATOM   1883 C CB  . ALA A 1 257 ? 29.801  -29.359 5.628   1.00   70.12  ? 257  ALA A CB  1 
ATOM   1884 N N   . ILE A 1 258 ? 30.673  -31.988 6.987   1.00   70.57  ? 258  ILE A N   1 
ATOM   1885 C CA  . ILE A 1 258 ? 31.164  -32.674 8.185   1.00   70.87  ? 258  ILE A CA  1 
ATOM   1886 C C   . ILE A 1 258 ? 32.388  -33.551 7.897   1.00   70.98  ? 258  ILE A C   1 
ATOM   1887 O O   . ILE A 1 258 ? 33.326  -33.589 8.700   1.00   71.05  ? 258  ILE A O   1 
ATOM   1888 C CB  . ILE A 1 258 ? 30.036  -33.469 8.897   1.00   70.92  ? 258  ILE A CB  1 
ATOM   1889 C CG1 . ILE A 1 258 ? 28.953  -32.516 9.427   1.00   70.99  ? 258  ILE A CG1 1 
ATOM   1890 C CG2 . ILE A 1 258 ? 30.590  -34.358 10.017  1.00   71.03  ? 258  ILE A CG2 1 
ATOM   1891 C CD1 . ILE A 1 258 ? 29.448  -31.458 10.426  1.00   70.74  ? 258  ILE A CD1 1 
ATOM   1892 N N   . SER A 1 259 ? 32.383  -34.228 6.749   1.00   71.05  ? 259  SER A N   1 
ATOM   1893 C CA  . SER A 1 259 ? 33.524  -35.052 6.336   1.00   71.20  ? 259  SER A CA  1 
ATOM   1894 C C   . SER A 1 259 ? 34.707  -34.188 5.897   1.00   71.20  ? 259  SER A C   1 
ATOM   1895 O O   . SER A 1 259 ? 35.851  -34.461 6.269   1.00   71.13  ? 259  SER A O   1 
ATOM   1896 C CB  . SER A 1 259 ? 33.131  -36.048 5.233   1.00   71.16  ? 259  SER A CB  1 
ATOM   1897 O OG  . SER A 1 259 ? 32.755  -35.390 4.030   1.00   71.16  ? 259  SER A OG  1 
ATOM   1898 N N   . ARG A 1 260 ? 34.412  -33.146 5.116   1.00   71.21  ? 260  ARG A N   1 
ATOM   1899 C CA  . ARG A 1 260 ? 35.415  -32.183 4.652   1.00   71.17  ? 260  ARG A CA  1 
ATOM   1900 C C   . ARG A 1 260 ? 36.186  -31.541 5.807   1.00   71.01  ? 260  ARG A C   1 
ATOM   1901 O O   . ARG A 1 260 ? 37.377  -31.256 5.675   1.00   71.05  ? 260  ARG A O   1 
ATOM   1902 C CB  . ARG A 1 260 ? 34.756  -31.091 3.805   1.00   71.21  ? 260  ARG A CB  1 
ATOM   1903 C CG  . ARG A 1 260 ? 34.505  -31.468 2.356   1.00   71.57  ? 260  ARG A CG  1 
ATOM   1904 C CD  . ARG A 1 260 ? 33.740  -30.362 1.645   1.00   72.36  ? 260  ARG A CD  1 
ATOM   1905 N NE  . ARG A 1 260 ? 33.831  -30.466 0.187   1.00   73.18  ? 260  ARG A NE  1 
ATOM   1906 C CZ  . ARG A 1 260 ? 33.163  -29.696 -0.671  1.00   73.47  ? 260  ARG A CZ  1 
ATOM   1907 N NH1 . ARG A 1 260 ? 32.336  -28.754 -0.230  1.00   73.97  ? 260  ARG A NH1 1 
ATOM   1908 N NH2 . ARG A 1 260 ? 33.316  -29.872 -1.978  1.00   73.63  ? 260  ARG A NH2 1 
ATOM   1909 N N   . ILE A 1 261 ? 35.498  -31.325 6.930   1.00   70.81  ? 261  ILE A N   1 
ATOM   1910 C CA  . ILE A 1 261 ? 36.100  -30.741 8.133   1.00   70.66  ? 261  ILE A CA  1 
ATOM   1911 C C   . ILE A 1 261 ? 37.132  -31.678 8.765   1.00   70.47  ? 261  ILE A C   1 
ATOM   1912 O O   . ILE A 1 261 ? 38.267  -31.270 9.033   1.00   70.56  ? 261  ILE A O   1 
ATOM   1913 C CB  . ILE A 1 261 ? 35.031  -30.361 9.186   1.00   70.65  ? 261  ILE A CB  1 
ATOM   1914 C CG1 . ILE A 1 261 ? 34.090  -29.282 8.641   1.00   70.77  ? 261  ILE A CG1 1 
ATOM   1915 C CG2 . ILE A 1 261 ? 35.689  -29.855 10.455  1.00   70.74  ? 261  ILE A CG2 1 
ATOM   1916 C CD1 . ILE A 1 261 ? 32.791  -29.136 9.446   1.00   70.91  ? 261  ILE A CD1 1 
ATOM   1917 N N   . ASN A 1 262 ? 36.725  -32.924 9.009   1.00   70.17  ? 262  ASN A N   1 
ATOM   1918 C CA  . ASN A 1 262 ? 37.622  -33.952 9.539   1.00   69.75  ? 262  ASN A CA  1 
ATOM   1919 C C   . ASN A 1 262 ? 38.831  -34.156 8.631   1.00   69.40  ? 262  ASN A C   1 
ATOM   1920 O O   . ASN A 1 262 ? 39.970  -34.160 9.100   1.00   69.55  ? 262  ASN A O   1 
ATOM   1921 C CB  . ASN A 1 262 ? 36.877  -35.277 9.730   1.00   69.77  ? 262  ASN A CB  1 
ATOM   1922 C CG  . ASN A 1 262 ? 35.687  -35.154 10.670  1.00   69.85  ? 262  ASN A CG  1 
ATOM   1923 O OD1 . ASN A 1 262 ? 35.762  -34.504 11.717  1.00   69.57  ? 262  ASN A OD1 1 
ATOM   1924 N ND2 . ASN A 1 262 ? 34.582  -35.796 10.304  1.00   69.78  ? 262  ASN A ND2 1 
ATOM   1925 N N   . ASN A 1 263 ? 38.565  -34.299 7.331   1.00   68.84  ? 263  ASN A N   1 
ATOM   1926 C CA  . ASN A 1 263 ? 39.599  -34.426 6.299   1.00   68.29  ? 263  ASN A CA  1 
ATOM   1927 C C   . ASN A 1 263 ? 40.475  -33.178 6.138   1.00   67.74  ? 263  ASN A C   1 
ATOM   1928 O O   . ASN A 1 263 ? 41.434  -33.178 5.353   1.00   67.63  ? 263  ASN A O   1 
ATOM   1929 C CB  . ASN A 1 263 ? 38.961  -34.800 4.954   1.00   68.38  ? 263  ASN A CB  1 
ATOM   1930 C CG  . ASN A 1 263 ? 38.663  -36.285 4.837   1.00   68.62  ? 263  ASN A CG  1 
ATOM   1931 O OD1 . ASN A 1 263 ? 39.547  -37.125 5.030   1.00   68.95  ? 263  ASN A OD1 1 
ATOM   1932 N ND2 . ASN A 1 263 ? 37.416  -36.617 4.507   1.00   68.38  ? 263  ASN A ND2 1 
ATOM   1933 N N   . ALA A 1 264 ? 40.135  -32.123 6.882   1.00   66.91  ? 264  ALA A N   1 
ATOM   1934 C CA  . ALA A 1 264 ? 40.906  -30.882 6.888   1.00   66.02  ? 264  ALA A CA  1 
ATOM   1935 C C   . ALA A 1 264 ? 41.740  -30.739 8.158   1.00   65.37  ? 264  ALA A C   1 
ATOM   1936 O O   . ALA A 1 264 ? 41.630  -31.542 9.094   1.00   65.36  ? 264  ALA A O   1 
ATOM   1937 C CB  . ALA A 1 264 ? 39.992  -29.673 6.701   1.00   66.17  ? 264  ALA A CB  1 
ATOM   1938 N N   . CYS A 1 265 ? 42.556  -29.688 8.181   1.00   64.37  ? 265  CYS A N   1 
ATOM   1939 C CA  . CYS A 1 265 ? 43.610  -29.529 9.173   1.00   63.46  ? 265  CYS A CA  1 
ATOM   1940 C C   . CYS A 1 265 ? 43.204  -28.758 10.428  1.00   62.22  ? 265  CYS A C   1 
ATOM   1941 O O   . CYS A 1 265 ? 44.018  -28.592 11.342  1.00   62.15  ? 265  CYS A O   1 
ATOM   1942 C CB  . CYS A 1 265 ? 44.800  -28.845 8.514   1.00   63.54  ? 265  CYS A CB  1 
ATOM   1943 S SG  . CYS A 1 265 ? 44.312  -27.655 7.239   1.00   65.78  ? 265  CYS A SG  1 
ATOM   1944 N N   . PHE A 1 266 ? 41.954  -28.297 10.474  1.00   60.69  ? 266  PHE A N   1 
ATOM   1945 C CA  . PHE A 1 266 ? 41.468  -27.483 11.589  1.00   59.08  ? 266  PHE A CA  1 
ATOM   1946 C C   . PHE A 1 266 ? 41.798  -28.088 12.952  1.00   58.23  ? 266  PHE A C   1 
ATOM   1947 O O   . PHE A 1 266 ? 41.457  -29.243 13.229  1.00   58.07  ? 266  PHE A O   1 
ATOM   1948 C CB  . PHE A 1 266 ? 39.952  -27.252 11.493  1.00   58.81  ? 266  PHE A CB  1 
ATOM   1949 C CG  . PHE A 1 266 ? 39.511  -26.583 10.219  1.00   57.83  ? 266  PHE A CG  1 
ATOM   1950 C CD1 . PHE A 1 266 ? 38.729  -27.274 9.303   1.00   56.79  ? 266  PHE A CD1 1 
ATOM   1951 C CD2 . PHE A 1 266 ? 39.865  -25.262 9.941   1.00   57.15  ? 266  PHE A CD2 1 
ATOM   1952 C CE1 . PHE A 1 266 ? 38.310  -26.668 8.126   1.00   57.30  ? 266  PHE A CE1 1 
ATOM   1953 C CE2 . PHE A 1 266 ? 39.451  -24.646 8.764   1.00   56.99  ? 266  PHE A CE2 1 
ATOM   1954 C CZ  . PHE A 1 266 ? 38.673  -25.349 7.857   1.00   57.19  ? 266  PHE A CZ  1 
ATOM   1955 N N   . GLU A 1 267 ? 42.470  -27.303 13.789  1.00   56.94  ? 267  GLU A N   1 
ATOM   1956 C CA  . GLU A 1 267 ? 42.634  -27.646 15.193  1.00   55.97  ? 267  GLU A CA  1 
ATOM   1957 C C   . GLU A 1 267 ? 41.259  -27.668 15.874  1.00   55.01  ? 267  GLU A C   1 
ATOM   1958 O O   . GLU A 1 267 ? 41.005  -28.490 16.765  1.00   55.00  ? 267  GLU A O   1 
ATOM   1959 C CB  . GLU A 1 267 ? 43.576  -26.652 15.880  1.00   56.17  ? 267  GLU A CB  1 
ATOM   1960 C CG  . GLU A 1 267 ? 43.760  -26.864 17.393  1.00   57.42  ? 267  GLU A CG  1 
ATOM   1961 C CD  . GLU A 1 267 ? 44.584  -28.102 17.761  1.00   58.78  ? 267  GLU A CD  1 
ATOM   1962 O OE1 . GLU A 1 267 ? 45.146  -28.759 16.855  1.00   58.83  ? 267  GLU A OE1 1 
ATOM   1963 O OE2 . GLU A 1 267 ? 44.670  -28.411 18.974  1.00   59.55  ? 267  GLU A OE2 1 
ATOM   1964 N N   . ALA A 1 268 ? 40.380  -26.762 15.440  1.00   53.49  ? 268  ALA A N   1 
ATOM   1965 C CA  . ALA A 1 268 ? 38.997  -26.704 15.913  1.00   52.08  ? 268  ALA A CA  1 
ATOM   1966 C C   . ALA A 1 268 ? 38.088  -25.931 14.949  1.00   51.14  ? 268  ALA A C   1 
ATOM   1967 O O   . ALA A 1 268 ? 38.546  -25.060 14.192  1.00   50.89  ? 268  ALA A O   1 
ATOM   1968 C CB  . ALA A 1 268 ? 38.933  -26.089 17.305  1.00   51.98  ? 268  ALA A CB  1 
ATOM   1969 N N   . VAL A 1 269 ? 36.803  -26.277 14.973  1.00   49.86  ? 269  VAL A N   1 
ATOM   1970 C CA  . VAL A 1 269 ? 35.779  -25.517 14.260  1.00   48.66  ? 269  VAL A CA  1 
ATOM   1971 C C   . VAL A 1 269 ? 34.742  -25.051 15.273  1.00   48.12  ? 269  VAL A C   1 
ATOM   1972 O O   . VAL A 1 269 ? 33.982  -25.854 15.831  1.00   48.20  ? 269  VAL A O   1 
ATOM   1973 C CB  . VAL A 1 269 ? 35.125  -26.330 13.125  1.00   48.64  ? 269  VAL A CB  1 
ATOM   1974 C CG1 . VAL A 1 269 ? 34.109  -25.468 12.369  1.00   48.05  ? 269  VAL A CG1 1 
ATOM   1975 C CG2 . VAL A 1 269 ? 36.185  -26.848 12.164  1.00   48.05  ? 269  VAL A CG2 1 
ATOM   1976 N N   . VAL A 1 270 ? 34.731  -23.747 15.521  1.00   47.16  ? 270  VAL A N   1 
ATOM   1977 C CA  . VAL A 1 270 ? 33.865  -23.168 16.541  1.00   46.52  ? 270  VAL A CA  1 
ATOM   1978 C C   . VAL A 1 270 ? 32.627  -22.538 15.916  1.00   46.17  ? 270  VAL A C   1 
ATOM   1979 O O   . VAL A 1 270 ? 32.730  -21.677 15.030  1.00   46.22  ? 270  VAL A O   1 
ATOM   1980 C CB  . VAL A 1 270 ? 34.611  -22.115 17.375  1.00   46.36  ? 270  VAL A CB  1 
ATOM   1981 C CG1 . VAL A 1 270 ? 33.783  -21.692 18.570  1.00   46.03  ? 270  VAL A CG1 1 
ATOM   1982 C CG2 . VAL A 1 270 ? 35.935  -22.670 17.833  1.00   47.02  ? 270  VAL A CG2 1 
ATOM   1983 N N   . VAL A 1 271 ? 31.462  -22.982 16.381  1.00   45.46  ? 271  VAL A N   1 
ATOM   1984 C CA  . VAL A 1 271 ? 30.186  -22.427 15.939  1.00   44.99  ? 271  VAL A CA  1 
ATOM   1985 C C   . VAL A 1 271 ? 29.313  -22.058 17.130  1.00   44.28  ? 271  VAL A C   1 
ATOM   1986 O O   . VAL A 1 271 ? 29.596  -22.463 18.264  1.00   43.81  ? 271  VAL A O   1 
ATOM   1987 C CB  . VAL A 1 271 ? 29.411  -23.382 14.986  1.00   44.99  ? 271  VAL A CB  1 
ATOM   1988 C CG1 . VAL A 1 271 ? 30.107  -23.488 13.647  1.00   45.70  ? 271  VAL A CG1 1 
ATOM   1989 C CG2 . VAL A 1 271 ? 29.213  -24.764 15.614  1.00   45.63  ? 271  VAL A CG2 1 
ATOM   1990 N N   . THR A 1 272 ? 28.274  -21.268 16.870  1.00   43.33  ? 272  THR A N   1 
ATOM   1991 C CA  . THR A 1 272 ? 27.238  -21.020 17.866  1.00   43.15  ? 272  THR A CA  1 
ATOM   1992 C C   . THR A 1 272 ? 26.117  -22.038 17.692  1.00   43.24  ? 272  THR A C   1 
ATOM   1993 O O   . THR A 1 272 ? 26.057  -22.734 16.679  1.00   43.26  ? 272  THR A O   1 
ATOM   1994 C CB  . THR A 1 272 ? 26.640  -19.590 17.789  1.00   42.91  ? 272  THR A CB  1 
ATOM   1995 O OG1 . THR A 1 272 ? 25.886  -19.446 16.581  1.00   42.60  ? 272  THR A OG1 1 
ATOM   1996 C CG2 . THR A 1 272 ? 27.728  -18.522 17.857  1.00   42.85  ? 272  THR A CG2 1 
ATOM   1997 N N   . ASN A 1 273 ? 25.240  -22.130 18.685  1.00   43.70  ? 273  ASN A N   1 
ATOM   1998 C CA  . ASN A 1 273 ? 24.068  -22.992 18.590  1.00   44.50  ? 273  ASN A CA  1 
ATOM   1999 C C   . ASN A 1 273 ? 22.816  -22.275 18.044  1.00   45.07  ? 273  ASN A C   1 
ATOM   2000 O O   . ASN A 1 273 ? 21.691  -22.586 18.445  1.00   45.22  ? 273  ASN A O   1 
ATOM   2001 C CB  . ASN A 1 273 ? 23.806  -23.744 19.921  1.00   44.20  ? 273  ASN A CB  1 
ATOM   2002 C CG  . ASN A 1 273 ? 23.426  -22.816 21.080  1.00   44.41  ? 273  ASN A CG  1 
ATOM   2003 O OD1 . ASN A 1 273 ? 22.842  -23.262 22.078  1.00   44.95  ? 273  ASN A OD1 1 
ATOM   2004 N ND2 . ASN A 1 273 ? 23.742  -21.532 20.953  1.00   41.76  ? 273  ASN A ND2 1 
ATOM   2005 N N   . THR A 1 274 ? 23.020  -21.326 17.124  1.00   46.04  ? 274  THR A N   1 
ATOM   2006 C CA  . THR A 1 274 ? 21.899  -20.686 16.402  1.00   47.11  ? 274  THR A CA  1 
ATOM   2007 C C   . THR A 1 274 ? 21.208  -21.717 15.514  1.00   47.94  ? 274  THR A C   1 
ATOM   2008 O O   . THR A 1 274 ? 20.035  -21.574 15.167  1.00   47.70  ? 274  THR A O   1 
ATOM   2009 C CB  . THR A 1 274 ? 22.322  -19.463 15.523  1.00   46.85  ? 274  THR A CB  1 
ATOM   2010 O OG1 . THR A 1 274 ? 23.224  -19.874 14.483  1.00   47.25  ? 274  THR A OG1 1 
ATOM   2011 C CG2 . THR A 1 274 ? 22.947  -18.352 16.364  1.00   46.36  ? 274  THR A CG2 1 
ATOM   2012 N N   . ILE A 1 275 ? 21.969  -22.751 15.159  1.00   49.22  ? 275  ILE A N   1 
ATOM   2013 C CA  . ILE A 1 275 ? 21.484  -23.922 14.428  1.00   50.52  ? 275  ILE A CA  1 
ATOM   2014 C C   . ILE A 1 275 ? 21.910  -25.143 15.260  1.00   51.51  ? 275  ILE A C   1 
ATOM   2015 O O   . ILE A 1 275 ? 23.016  -25.147 15.808  1.00   51.45  ? 275  ILE A O   1 
ATOM   2016 C CB  . ILE A 1 275 ? 22.098  -23.969 12.991  1.00   50.51  ? 275  ILE A CB  1 
ATOM   2017 C CG1 . ILE A 1 275 ? 21.616  -22.762 12.169  1.00   50.53  ? 275  ILE A CG1 1 
ATOM   2018 C CG2 . ILE A 1 275 ? 21.776  -25.295 12.265  1.00   50.65  ? 275  ILE A CG2 1 
ATOM   2019 C CD1 . ILE A 1 275 ? 22.381  -22.545 10.873  1.00   50.79  ? 275  ILE A CD1 1 
ATOM   2020 N N   . PRO A 1 276 ? 21.030  -26.163 15.388  1.00   52.59  ? 276  PRO A N   1 
ATOM   2021 C CA  . PRO A 1 276 ? 21.377  -27.359 16.176  1.00   53.62  ? 276  PRO A CA  1 
ATOM   2022 C C   . PRO A 1 276 ? 22.671  -28.022 15.690  1.00   54.58  ? 276  PRO A C   1 
ATOM   2023 O O   . PRO A 1 276 ? 22.917  -28.087 14.482  1.00   54.65  ? 276  PRO A O   1 
ATOM   2024 C CB  . PRO A 1 276 ? 20.185  -28.295 15.945  1.00   53.44  ? 276  PRO A CB  1 
ATOM   2025 C CG  . PRO A 1 276 ? 19.070  -27.407 15.584  1.00   53.21  ? 276  PRO A CG  1 
ATOM   2026 C CD  . PRO A 1 276 ? 19.663  -26.249 14.840  1.00   52.71  ? 276  PRO A CD  1 
ATOM   2027 N N   . GLN A 1 277 ? 23.494  -28.484 16.628  0.64   55.84  ? 277  GLN A N   1 
ATOM   2028 C CA  . GLN A 1 277 ? 24.812  -29.035 16.295  0.64   57.12  ? 277  GLN A CA  1 
ATOM   2029 C C   . GLN A 1 277 ? 25.057  -30.404 16.924  0.64   58.31  ? 277  GLN A C   1 
ATOM   2030 O O   . GLN A 1 277 ? 26.050  -31.067 16.610  0.64   58.21  ? 277  GLN A O   1 
ATOM   2031 C CB  . GLN A 1 277 ? 25.930  -28.075 16.728  0.64   57.03  ? 277  GLN A CB  1 
ATOM   2032 C CG  . GLN A 1 277 ? 25.795  -26.623 16.253  0.64   56.31  ? 277  GLN A CG  1 
ATOM   2033 C CD  . GLN A 1 277 ? 26.000  -26.435 14.756  0.64   55.71  ? 277  GLN A CD  1 
ATOM   2034 O OE1 . GLN A 1 277 ? 25.594  -25.417 14.194  0.64   55.46  ? 277  GLN A OE1 1 
ATOM   2035 N NE2 . GLN A 1 277 ? 26.634  -27.408 14.107  0.64   55.58  ? 277  GLN A NE2 1 
ATOM   2036 N N   . GLU A 1 278 ? 24.144  -30.815 17.806  0.83   59.90  ? 278  GLU A N   1 
ATOM   2037 C CA  . GLU A 1 278 ? 24.284  -32.027 18.623  0.83   61.44  ? 278  GLU A CA  1 
ATOM   2038 C C   . GLU A 1 278 ? 24.543  -33.293 17.801  0.83   62.39  ? 278  GLU A C   1 
ATOM   2039 O O   . GLU A 1 278 ? 25.331  -34.155 18.208  0.83   62.63  ? 278  GLU A O   1 
ATOM   2040 C CB  . GLU A 1 278 ? 23.058  -32.211 19.534  0.83   61.56  ? 278  GLU A CB  1 
ATOM   2041 C CG  . GLU A 1 278 ? 22.829  -31.072 20.543  0.83   62.04  ? 278  GLU A CG  1 
ATOM   2042 C CD  . GLU A 1 278 ? 22.152  -29.849 19.926  0.83   62.91  ? 278  GLU A CD  1 
ATOM   2043 O OE1 . GLU A 1 278 ? 22.834  -28.815 19.737  0.83   63.79  ? 278  GLU A OE1 1 
ATOM   2044 O OE2 . GLU A 1 278 ? 20.940  -29.921 19.621  0.83   63.22  ? 278  GLU A OE2 1 
ATOM   2045 N N   . ASP A 1 279 ? 23.880  -33.389 16.646  1.00   63.53  ? 279  ASP A N   1 
ATOM   2046 C CA  . ASP A 1 279 ? 24.069  -34.500 15.713  1.00   64.69  ? 279  ASP A CA  1 
ATOM   2047 C C   . ASP A 1 279 ? 25.428  -34.417 15.010  1.00   65.27  ? 279  ASP A C   1 
ATOM   2048 O O   . ASP A 1 279 ? 26.083  -35.439 14.780  1.00   65.45  ? 279  ASP A O   1 
ATOM   2049 C CB  . ASP A 1 279 ? 22.931  -34.516 14.680  1.00   64.82  ? 279  ASP A CB  1 
ATOM   2050 C CG  . ASP A 1 279 ? 22.935  -35.766 13.799  1.00   74.87  ? 279  ASP A CG  1 
ATOM   2051 O OD1 . ASP A 1 279 ? 23.600  -36.767 14.145  1.00   77.89  ? 279  ASP A OD1 1 
ATOM   2052 O OD2 . ASP A 1 279 ? 22.254  -35.745 12.749  1.00   77.79  ? 279  ASP A OD2 1 
ATOM   2053 N N   . LYS A 1 280 ? 25.843  -33.195 14.683  0.77   65.93  ? 280  LYS A N   1 
ATOM   2054 C CA  . LYS A 1 280 ? 27.076  -32.949 13.932  0.77   66.51  ? 280  LYS A CA  1 
ATOM   2055 C C   . LYS A 1 280 ? 28.342  -32.935 14.802  0.77   66.92  ? 280  LYS A C   1 
ATOM   2056 O O   . LYS A 1 280 ? 29.458  -32.887 14.274  0.77   67.07  ? 280  LYS A O   1 
ATOM   2057 C CB  . LYS A 1 280 ? 26.952  -31.644 13.137  0.77   66.47  ? 280  LYS A CB  1 
ATOM   2058 C CG  . LYS A 1 280 ? 25.917  -31.704 12.021  0.77   66.68  ? 280  LYS A CG  1 
ATOM   2059 C CD  . LYS A 1 280 ? 25.686  -30.345 11.385  0.77   66.88  ? 280  LYS A CD  1 
ATOM   2060 C CE  . LYS A 1 280 ? 24.567  -30.395 10.347  0.77   66.95  ? 280  LYS A CE  1 
ATOM   2061 N NZ  . LYS A 1 280 ? 24.876  -31.292 9.195   0.77   66.62  ? 280  LYS A NZ  1 
ATOM   2062 N N   . MET A 1 281 ? 28.163  -32.976 16.124  1.00   67.33  ? 281  MET A N   1 
ATOM   2063 C CA  . MET A 1 281 ? 29.286  -32.999 17.066  1.00   67.84  ? 281  MET A CA  1 
ATOM   2064 C C   . MET A 1 281 ? 29.754  -34.424 17.352  1.00   68.00  ? 281  MET A C   1 
ATOM   2065 O O   . MET A 1 281 ? 30.935  -34.662 17.626  1.00   68.05  ? 281  MET A O   1 
ATOM   2066 C CB  . MET A 1 281 ? 28.916  -32.291 18.372  1.00   68.00  ? 281  MET A CB  1 
ATOM   2067 C CG  . MET A 1 281 ? 28.981  -30.771 18.292  1.00   68.41  ? 281  MET A CG  1 
ATOM   2068 S SD  . MET A 1 281 ? 28.718  -29.966 19.881  1.00   116.89 ? 281  MET A SD  1 
ATOM   2069 C CE  . MET A 1 281 ? 26.926  -29.951 19.971  1.00   70.36  ? 281  MET A CE  1 
ATOM   2070 N N   . LYS A 1 282 ? 28.816  -35.364 17.286  0.86   68.08  ? 282  LYS A N   1 
ATOM   2071 C CA  . LYS A 1 282 ? 29.115  -36.783 17.450  0.86   68.19  ? 282  LYS A CA  1 
ATOM   2072 C C   . LYS A 1 282 ? 29.870  -37.317 16.233  0.86   68.07  ? 282  LYS A C   1 
ATOM   2073 O O   . LYS A 1 282 ? 30.677  -38.242 16.349  0.86   68.08  ? 282  LYS A O   1 
ATOM   2074 C CB  . LYS A 1 282 ? 27.820  -37.573 17.664  0.86   68.30  ? 282  LYS A CB  1 
ATOM   2075 C CG  . LYS A 1 282 ? 27.005  -37.114 18.870  0.86   68.71  ? 282  LYS A CG  1 
ATOM   2076 C CD  . LYS A 1 282 ? 25.591  -37.669 18.839  0.86   69.40  ? 282  LYS A CD  1 
ATOM   2077 C CE  . LYS A 1 282 ? 24.785  -37.180 20.038  0.86   69.69  ? 282  LYS A CE  1 
ATOM   2078 N NZ  . LYS A 1 282 ? 23.376  -37.653 19.984  0.86   69.74  ? 282  LYS A NZ  1 
ATOM   2079 N N   . HIS A 1 283 ? 29.604  -36.717 15.072  0.80   67.86  ? 283  HIS A N   1 
ATOM   2080 C CA  . HIS A 1 283 ? 30.224  -37.120 13.810  0.80   67.62  ? 283  HIS A CA  1 
ATOM   2081 C C   . HIS A 1 283 ? 31.484  -36.301 13.493  0.80   67.19  ? 283  HIS A C   1 
ATOM   2082 O O   . HIS A 1 283 ? 32.172  -36.570 12.499  0.80   67.21  ? 283  HIS A O   1 
ATOM   2083 C CB  . HIS A 1 283 ? 29.211  -36.986 12.669  0.80   67.77  ? 283  HIS A CB  1 
ATOM   2084 C CG  . HIS A 1 283 ? 29.175  -38.164 11.747  0.80   68.40  ? 283  HIS A CG  1 
ATOM   2085 N ND1 . HIS A 1 283 ? 30.257  -38.550 10.984  0.80   68.99  ? 283  HIS A ND1 1 
ATOM   2086 C CD2 . HIS A 1 283 ? 28.181  -39.039 11.460  0.80   68.90  ? 283  HIS A CD2 1 
ATOM   2087 C CE1 . HIS A 1 283 ? 29.933  -39.615 10.271  0.80   69.35  ? 283  HIS A CE1 1 
ATOM   2088 N NE2 . HIS A 1 283 ? 28.678  -39.930 10.540  0.80   69.39  ? 283  HIS A NE2 1 
ATOM   2089 N N   . CYS A 1 284 ? 31.774  -35.305 14.336  0.78   66.59  ? 284  CYS A N   1 
ATOM   2090 C CA  . CYS A 1 284 ? 32.942  -34.434 14.167  0.78   66.01  ? 284  CYS A CA  1 
ATOM   2091 C C   . CYS A 1 284 ? 33.449  -33.924 15.518  0.78   65.28  ? 284  CYS A C   1 
ATOM   2092 O O   . CYS A 1 284 ? 32.795  -33.108 16.178  0.78   65.21  ? 284  CYS A O   1 
ATOM   2093 C CB  . CYS A 1 284 ? 32.610  -33.262 13.238  0.78   66.16  ? 284  CYS A CB  1 
ATOM   2094 S SG  . CYS A 1 284 ? 34.015  -32.191 12.832  0.78   67.21  ? 284  CYS A SG  1 
ATOM   2095 N N   . SER A 1 285 ? 34.627  -34.403 15.914  1.00   64.40  ? 285  SER A N   1 
ATOM   2096 C CA  . SER A 1 285 ? 35.158  -34.160 17.254  1.00   63.47  ? 285  SER A CA  1 
ATOM   2097 C C   . SER A 1 285 ? 35.805  -32.784 17.435  1.00   62.64  ? 285  SER A C   1 
ATOM   2098 O O   . SER A 1 285 ? 35.884  -32.275 18.554  1.00   62.69  ? 285  SER A O   1 
ATOM   2099 C CB  . SER A 1 285 ? 36.150  -35.265 17.634  1.00   63.73  ? 285  SER A CB  1 
ATOM   2100 O OG  . SER A 1 285 ? 36.340  -35.309 19.043  1.00   64.07  ? 285  SER A OG  1 
ATOM   2101 N N   . LYS A 1 286 ? 36.260  -32.178 16.340  1.00   61.54  ? 286  LYS A N   1 
ATOM   2102 C CA  . LYS A 1 286 ? 36.929  -30.875 16.423  1.00   60.37  ? 286  LYS A CA  1 
ATOM   2103 C C   . LYS A 1 286 ? 35.963  -29.687 16.581  1.00   59.24  ? 286  LYS A C   1 
ATOM   2104 O O   . LYS A 1 286 ? 36.397  -28.563 16.865  1.00   58.80  ? 286  LYS A O   1 
ATOM   2105 C CB  . LYS A 1 286 ? 37.897  -30.673 15.250  1.00   60.63  ? 286  LYS A CB  1 
ATOM   2106 C CG  . LYS A 1 286 ? 37.272  -30.813 13.862  1.00   61.18  ? 286  LYS A CG  1 
ATOM   2107 C CD  . LYS A 1 286 ? 38.282  -30.518 12.749  1.00   62.35  ? 286  LYS A CD  1 
ATOM   2108 C CE  . LYS A 1 286 ? 39.167  -31.718 12.419  1.00   62.99  ? 286  LYS A CE  1 
ATOM   2109 N NZ  . LYS A 1 286 ? 40.347  -31.826 13.327  1.00   64.16  ? 286  LYS A NZ  1 
ATOM   2110 N N   . ILE A 1 287 ? 34.662  -29.946 16.419  1.00   57.88  ? 287  ILE A N   1 
ATOM   2111 C CA  . ILE A 1 287 ? 33.636  -28.910 16.588  1.00   56.68  ? 287  ILE A CA  1 
ATOM   2112 C C   . ILE A 1 287 ? 33.427  -28.535 18.057  1.00   55.72  ? 287  ILE A C   1 
ATOM   2113 O O   . ILE A 1 287 ? 33.286  -29.404 18.921  1.00   55.70  ? 287  ILE A O   1 
ATOM   2114 C CB  . ILE A 1 287 ? 32.274  -29.303 15.935  1.00   56.84  ? 287  ILE A CB  1 
ATOM   2115 C CG1 . ILE A 1 287 ? 32.409  -29.386 14.407  1.00   57.21  ? 287  ILE A CG1 1 
ATOM   2116 C CG2 . ILE A 1 287 ? 31.175  -28.299 16.316  1.00   56.38  ? 287  ILE A CG2 1 
ATOM   2117 C CD1 . ILE A 1 287 ? 31.177  -29.949 13.686  1.00   57.70  ? 287  ILE A CD1 1 
ATOM   2118 N N   . GLN A 1 288 ? 33.429  -27.234 18.325  1.00   54.40  ? 288  GLN A N   1 
ATOM   2119 C CA  . GLN A 1 288 ? 33.058  -26.714 19.633  1.00   53.59  ? 288  GLN A CA  1 
ATOM   2120 C C   . GLN A 1 288 ? 31.915  -25.717 19.480  1.00   52.69  ? 288  GLN A C   1 
ATOM   2121 O O   . GLN A 1 288 ? 31.860  -24.968 18.500  1.00   52.35  ? 288  GLN A O   1 
ATOM   2122 C CB  . GLN A 1 288 ? 34.255  -26.067 20.333  1.00   53.65  ? 288  GLN A CB  1 
ATOM   2123 C CG  . GLN A 1 288 ? 35.300  -27.073 20.826  1.00   55.17  ? 288  GLN A CG  1 
ATOM   2124 C CD  . GLN A 1 288 ? 36.332  -26.451 21.762  1.00   56.99  ? 288  GLN A CD  1 
ATOM   2125 O OE1 . GLN A 1 288 ? 35.990  -25.736 22.711  1.00   57.56  ? 288  GLN A OE1 1 
ATOM   2126 N NE2 . GLN A 1 288 ? 37.606  -26.737 21.507  1.00   57.67  ? 288  GLN A NE2 1 
ATOM   2127 N N   . VAL A 1 289 ? 31.008  -25.713 20.453  1.00   51.62  ? 289  VAL A N   1 
ATOM   2128 C CA  . VAL A 1 289 ? 29.826  -24.856 20.400  1.00   50.75  ? 289  VAL A CA  1 
ATOM   2129 C C   . VAL A 1 289 ? 29.821  -23.758 21.457  1.00   49.78  ? 289  VAL A C   1 
ATOM   2130 O O   . VAL A 1 289 ? 30.060  -24.008 22.641  1.00   49.98  ? 289  VAL A O   1 
ATOM   2131 C CB  . VAL A 1 289 ? 28.495  -25.659 20.502  1.00   50.82  ? 289  VAL A CB  1 
ATOM   2132 C CG1 . VAL A 1 289 ? 28.133  -26.259 19.167  1.00   51.19  ? 289  VAL A CG1 1 
ATOM   2133 C CG2 . VAL A 1 289 ? 28.580  -26.743 21.581  1.00   51.37  ? 289  VAL A CG2 1 
ATOM   2134 N N   . ILE A 1 290 ? 29.541  -22.541 21.008  1.00   48.41  ? 290  ILE A N   1 
ATOM   2135 C CA  . ILE A 1 290 ? 29.285  -21.425 21.900  1.00   47.22  ? 290  ILE A CA  1 
ATOM   2136 C C   . ILE A 1 290 ? 27.774  -21.283 22.054  1.00   46.45  ? 290  ILE A C   1 
ATOM   2137 O O   . ILE A 1 290 ? 27.058  -21.097 21.069  1.00   46.39  ? 290  ILE A O   1 
ATOM   2138 C CB  . ILE A 1 290 ? 29.879  -20.108 21.359  1.00   47.29  ? 290  ILE A CB  1 
ATOM   2139 C CG1 . ILE A 1 290 ? 31.397  -20.243 21.155  1.00   47.73  ? 290  ILE A CG1 1 
ATOM   2140 C CG2 . ILE A 1 290 ? 29.524  -18.934 22.288  1.00   46.95  ? 290  ILE A CG2 1 
ATOM   2141 C CD1 . ILE A 1 290 ? 32.066  -19.027 20.491  1.00   47.08  ? 290  ILE A CD1 1 
ATOM   2142 N N   . ASP A 1 291 ? 27.304  -21.388 23.294  1.00   45.26  ? 291  ASP A N   1 
ATOM   2143 C CA  . ASP A 1 291 ? 25.897  -21.218 23.634  1.00   44.33  ? 291  ASP A CA  1 
ATOM   2144 C C   . ASP A 1 291 ? 25.516  -19.740 23.561  1.00   43.09  ? 291  ASP A C   1 
ATOM   2145 O O   . ASP A 1 291 ? 26.148  -18.897 24.200  1.00   42.71  ? 291  ASP A O   1 
ATOM   2146 C CB  . ASP A 1 291 ? 25.643  -21.766 25.046  1.00   44.56  ? 291  ASP A CB  1 
ATOM   2147 C CG  . ASP A 1 291 ? 24.158  -21.807 25.421  1.00   45.80  ? 291  ASP A CG  1 
ATOM   2148 O OD1 . ASP A 1 291 ? 23.284  -21.451 24.592  1.00   46.89  ? 291  ASP A OD1 1 
ATOM   2149 O OD2 . ASP A 1 291 ? 23.866  -22.200 26.570  1.00   45.49  ? 291  ASP A OD2 1 
ATOM   2150 N N   . ILE A 1 292 ? 24.489  -19.427 22.774  1.00   41.45  ? 292  ILE A N   1 
ATOM   2151 C CA  . ILE A 1 292 ? 24.032  -18.045 22.652  1.00   40.19  ? 292  ILE A CA  1 
ATOM   2152 C C   . ILE A 1 292 ? 22.623  -17.830 23.216  1.00   39.29  ? 292  ILE A C   1 
ATOM   2153 O O   . ILE A 1 292 ? 22.043  -16.747 23.076  1.00   38.44  ? 292  ILE A O   1 
ATOM   2154 C CB  . ILE A 1 292 ? 24.203  -17.467 21.191  1.00   40.35  ? 292  ILE A CB  1 
ATOM   2155 C CG1 . ILE A 1 292 ? 23.626  -18.391 20.121  1.00   39.77  ? 292  ILE A CG1 1 
ATOM   2156 C CG2 . ILE A 1 292 ? 25.680  -17.238 20.882  1.00   40.36  ? 292  ILE A CG2 1 
ATOM   2157 C CD1 . ILE A 1 292 ? 22.114  -18.529 20.131  1.00   36.81  ? 292  ILE A CD1 1 
ATOM   2158 N N   . SER A 1 293 ? 22.085  -18.866 23.861  1.00   37.96  ? 293  SER A N   1 
ATOM   2159 C CA  . SER A 1 293 ? 20.757  -18.789 24.470  1.00   37.06  ? 293  SER A CA  1 
ATOM   2160 C C   . SER A 1 293 ? 20.645  -17.670 25.497  1.00   36.34  ? 293  SER A C   1 
ATOM   2161 O O   . SER A 1 293 ? 19.561  -17.114 25.692  1.00   36.18  ? 293  SER A O   1 
ATOM   2162 C CB  . SER A 1 293 ? 20.375  -20.118 25.127  1.00   37.15  ? 293  SER A CB  1 
ATOM   2163 O OG  . SER A 1 293 ? 21.135  -20.348 26.305  1.00   36.66  ? 293  SER A OG  1 
ATOM   2164 N N   . MET A 1 294 ? 21.753  -17.349 26.164  0.76   35.70  ? 294  MET A N   1 
ATOM   2165 C CA  . MET A 1 294 ? 21.735  -16.295 27.175  0.76   35.48  ? 294  MET A CA  1 
ATOM   2166 C C   . MET A 1 294 ? 21.669  -14.916 26.532  0.76   34.32  ? 294  MET A C   1 
ATOM   2167 O O   . MET A 1 294 ? 20.983  -14.028 27.031  0.76   33.92  ? 294  MET A O   1 
ATOM   2168 C CB  . MET A 1 294 ? 22.930  -16.403 28.136  0.76   36.13  ? 294  MET A CB  1 
ATOM   2169 C CG  . MET A 1 294 ? 22.985  -15.295 29.197  0.76   38.69  ? 294  MET A CG  1 
ATOM   2170 S SD  . MET A 1 294 ? 21.435  -15.023 30.100  0.76   45.91  ? 294  MET A SD  1 
ATOM   2171 C CE  . MET A 1 294 ? 21.776  -15.845 31.665  0.76   45.26  ? 294  MET A CE  1 
ATOM   2172 N N   . ILE A 1 295 ? 22.379  -14.745 25.422  1.00   33.54  ? 295  ILE A N   1 
ATOM   2173 C CA  . ILE A 1 295 ? 22.304  -13.505 24.651  1.00   33.00  ? 295  ILE A CA  1 
ATOM   2174 C C   . ILE A 1 295 ? 20.871  -13.275 24.153  1.00   31.77  ? 295  ILE A C   1 
ATOM   2175 O O   . ILE A 1 295 ? 20.329  -12.181 24.289  1.00   31.91  ? 295  ILE A O   1 
ATOM   2176 C CB  . ILE A 1 295 ? 23.322  -13.494 23.487  1.00   32.87  ? 295  ILE A CB  1 
ATOM   2177 C CG1 . ILE A 1 295 ? 24.748  -13.590 24.039  1.00   33.89  ? 295  ILE A CG1 1 
ATOM   2178 C CG2 . ILE A 1 295 ? 23.178  -12.216 22.659  1.00   34.00  ? 295  ILE A CG2 1 
ATOM   2179 C CD1 . ILE A 1 295 ? 25.776  -14.170 23.064  1.00   33.40  ? 295  ILE A CD1 1 
ATOM   2180 N N   . LEU A 1 296 ? 20.262  -14.318 23.603  1.00   31.26  ? 296  LEU A N   1 
ATOM   2181 C CA  . LEU A 1 296 ? 18.887  -14.236 23.079  1.00   30.50  ? 296  LEU A CA  1 
ATOM   2182 C C   . LEU A 1 296 ? 17.813  -14.051 24.167  1.00   30.16  ? 296  LEU A C   1 
ATOM   2183 O O   . LEU A 1 296 ? 16.880  -13.277 23.984  1.00   29.25  ? 296  LEU A O   1 
ATOM   2184 C CB  . LEU A 1 296 ? 18.563  -15.456 22.207  1.00   29.99  ? 296  LEU A CB  1 
ATOM   2185 C CG  . LEU A 1 296 ? 19.273  -15.557 20.845  1.00   29.98  ? 296  LEU A CG  1 
ATOM   2186 C CD1 . LEU A 1 296 ? 18.987  -16.913 20.222  1.00   29.15  ? 296  LEU A CD1 1 
ATOM   2187 C CD2 . LEU A 1 296 ? 18.825  -14.445 19.911  1.00   30.44  ? 296  LEU A CD2 1 
ATOM   2188 N N   . ALA A 1 297 ? 17.939  -14.765 25.287  1.00   29.96  ? 297  ALA A N   1 
ATOM   2189 C CA  . ALA A 1 297 ? 16.996  -14.596 26.403  1.00   30.85  ? 297  ALA A CA  1 
ATOM   2190 C C   . ALA A 1 297 ? 17.022  -13.164 26.942  1.00   31.45  ? 297  ALA A C   1 
ATOM   2191 O O   . ALA A 1 297 ? 15.974  -12.571 27.239  1.00   31.62  ? 297  ALA A O   1 
ATOM   2192 C CB  . ALA A 1 297 ? 17.303  -15.596 27.543  1.00   30.60  ? 297  ALA A CB  1 
ATOM   2193 N N   . GLU A 1 298 ? 18.231  -12.630 27.065  1.00   32.16  ? 298  GLU A N   1 
ATOM   2194 C CA  . GLU A 1 298 ? 18.448  -11.284 27.574  1.00   33.46  ? 298  GLU A CA  1 
ATOM   2195 C C   . GLU A 1 298 ? 17.863  -10.237 26.632  1.00   32.72  ? 298  GLU A C   1 
ATOM   2196 O O   . GLU A 1 298 ? 17.335  -9.220  27.082  1.00   32.92  ? 298  GLU A O   1 
ATOM   2197 C CB  . GLU A 1 298 ? 19.952  -11.055 27.803  1.00   33.94  ? 298  GLU A CB  1 
ATOM   2198 C CG  . GLU A 1 298 ? 20.317  -9.829  28.647  1.00   37.37  ? 298  GLU A CG  1 
ATOM   2199 C CD  . GLU A 1 298 ? 19.741  -9.861  30.063  1.00   41.20  ? 298  GLU A CD  1 
ATOM   2200 O OE1 . GLU A 1 298 ? 19.251  -10.924 30.518  1.00   43.02  ? 298  GLU A OE1 1 
ATOM   2201 O OE2 . GLU A 1 298 ? 19.779  -8.808  30.731  1.00   43.46  ? 298  GLU A OE2 1 
ATOM   2202 N N   . ALA A 1 299 ? 17.946  -10.504 25.327  1.00   32.10  ? 299  ALA A N   1 
ATOM   2203 C CA  . ALA A 1 299 ? 17.358  -9.635  24.318  1.00   31.05  ? 299  ALA A CA  1 
ATOM   2204 C C   . ALA A 1 299 ? 15.835  -9.624  24.419  1.00   30.62  ? 299  ALA A C   1 
ATOM   2205 O O   . ALA A 1 299 ? 15.218  -8.566  24.300  1.00   30.56  ? 299  ALA A O   1 
ATOM   2206 C CB  . ALA A 1 299 ? 17.806  -10.056 22.923  1.00   30.83  ? 299  ALA A CB  1 
ATOM   2207 N N   . ILE A 1 300 ? 15.237  -10.792 24.654  1.00   30.11  ? 300  ILE A N   1 
ATOM   2208 C CA  . ILE A 1 300 ? 13.783  -10.902 24.801  1.00   30.41  ? 300  ILE A CA  1 
ATOM   2209 C C   . ILE A 1 300 ? 13.337  -10.185 26.077  1.00   30.95  ? 300  ILE A C   1 
ATOM   2210 O O   . ILE A 1 300 ? 12.458  -9.324  26.038  1.00   30.06  ? 300  ILE A O   1 
ATOM   2211 C CB  . ILE A 1 300 ? 13.307  -12.379 24.800  1.00   30.11  ? 300  ILE A CB  1 
ATOM   2212 C CG1 . ILE A 1 300 ? 13.351  -12.953 23.374  1.00   30.06  ? 300  ILE A CG1 1 
ATOM   2213 C CG2 . ILE A 1 300 ? 11.892  -12.511 25.383  1.00   28.79  ? 300  ILE A CG2 1 
ATOM   2214 C CD1 . ILE A 1 300 ? 13.399  -14.463 23.326  1.00   27.15  ? 300  ILE A CD1 1 
ATOM   2215 N N   . ARG A 1 301 ? 13.962  -10.547 27.198  1.00   32.41  ? 301  ARG A N   1 
ATOM   2216 C CA  . ARG A 1 301 ? 13.699  -9.903  28.485  1.00   33.95  ? 301  ARG A CA  1 
ATOM   2217 C C   . ARG A 1 301 ? 13.853  -8.390  28.386  1.00   33.87  ? 301  ARG A C   1 
ATOM   2218 O O   . ARG A 1 301 ? 12.997  -7.651  28.856  1.00   34.57  ? 301  ARG A O   1 
ATOM   2219 C CB  . ARG A 1 301 ? 14.634  -10.459 29.569  1.00   34.83  ? 301  ARG A CB  1 
ATOM   2220 C CG  . ARG A 1 301 ? 14.115  -10.285 30.997  1.00   37.40  ? 301  ARG A CG  1 
ATOM   2221 C CD  . ARG A 1 301 ? 15.255  -10.356 32.004  1.00   42.00  ? 301  ARG A CD  1 
ATOM   2222 N NE  . ARG A 1 301 ? 15.814  -9.024  32.245  1.00   46.31  ? 301  ARG A NE  1 
ATOM   2223 C CZ  . ARG A 1 301 ? 17.079  -8.781  32.575  1.00   48.39  ? 301  ARG A CZ  1 
ATOM   2224 N NH1 . ARG A 1 301 ? 17.946  -9.785  32.707  1.00   51.04  ? 301  ARG A NH1 1 
ATOM   2225 N NH2 . ARG A 1 301 ? 17.483  -7.530  32.769  1.00   49.18  ? 301  ARG A NH2 1 
ATOM   2226 N N   . ARG A 1 302 ? 14.928  -7.924  27.756  0.76   34.73  ? 302  ARG A N   1 
ATOM   2227 C CA  . ARG A 1 302 ? 15.150  -6.481  27.638  0.76   35.50  ? 302  ARG A CA  1 
ATOM   2228 C C   . ARG A 1 302 ? 14.156  -5.808  26.694  0.76   35.60  ? 302  ARG A C   1 
ATOM   2229 O O   . ARG A 1 302 ? 13.654  -4.735  27.005  0.76   35.69  ? 302  ARG A O   1 
ATOM   2230 C CB  . ARG A 1 302 ? 16.601  -6.157  27.280  0.76   35.46  ? 302  ARG A CB  1 
ATOM   2231 C CG  . ARG A 1 302 ? 17.551  -6.355  28.459  0.76   37.81  ? 302  ARG A CG  1 
ATOM   2232 C CD  . ARG A 1 302 ? 19.010  -6.433  28.015  0.76   40.64  ? 302  ARG A CD  1 
ATOM   2233 N NE  . ARG A 1 302 ? 19.904  -6.602  29.162  0.76   42.06  ? 302  ARG A NE  1 
ATOM   2234 C CZ  . ARG A 1 302 ? 20.576  -5.613  29.755  0.76   43.11  ? 302  ARG A CZ  1 
ATOM   2235 N NH1 . ARG A 1 302 ? 20.467  -4.360  29.316  0.76   42.73  ? 302  ARG A NH1 1 
ATOM   2236 N NH2 . ARG A 1 302 ? 21.360  -5.879  30.795  0.76   42.91  ? 302  ARG A NH2 1 
ATOM   2237 N N   . THR A 1 303 ? 13.869  -6.451  25.559  1.00   36.19  ? 303  THR A N   1 
ATOM   2238 C CA  . THR A 1 303 ? 12.813  -6.008  24.636  1.00   36.69  ? 303  THR A CA  1 
ATOM   2239 C C   . THR A 1 303 ? 11.472  -5.879  25.346  1.00   37.11  ? 303  THR A C   1 
ATOM   2240 O O   . THR A 1 303 ? 10.709  -4.942  25.095  1.00   37.13  ? 303  THR A O   1 
ATOM   2241 C CB  . THR A 1 303 ? 12.604  -7.019  23.484  1.00   36.62  ? 303  THR A CB  1 
ATOM   2242 O OG1 . THR A 1 303 ? 13.784  -7.092  22.683  1.00   36.16  ? 303  THR A OG1 1 
ATOM   2243 C CG2 . THR A 1 303 ? 11.430  -6.601  22.610  1.00   36.86  ? 303  THR A CG2 1 
ATOM   2244 N N   . HIS A 1 304 ? 11.179  -6.845  26.214  1.00   37.57  ? 304  HIS A N   1 
ATOM   2245 C CA  . HIS A 1 304 ? 9.914   -6.864  26.921  1.00   38.51  ? 304  HIS A CA  1 
ATOM   2246 C C   . HIS A 1 304 ? 9.825   -5.711  27.927  1.00   39.11  ? 304  HIS A C   1 
ATOM   2247 O O   . HIS A 1 304 ? 8.771   -5.076  28.045  1.00   38.94  ? 304  HIS A O   1 
ATOM   2248 C CB  . HIS A 1 304 ? 9.721   -8.216  27.613  1.00   38.42  ? 304  HIS A CB  1 
ATOM   2249 C CG  . HIS A 1 304 ? 8.453   -8.322  28.399  1.00   38.91  ? 304  HIS A CG  1 
ATOM   2250 N ND1 . HIS A 1 304 ? 7.205   -8.291  27.811  1.00   39.11  ? 304  HIS A ND1 1 
ATOM   2251 C CD2 . HIS A 1 304 ? 8.240   -8.487  29.729  1.00   39.45  ? 304  HIS A CD2 1 
ATOM   2252 C CE1 . HIS A 1 304 ? 6.278   -8.418  28.745  1.00   38.13  ? 304  HIS A CE1 1 
ATOM   2253 N NE2 . HIS A 1 304 ? 6.880   -8.542  29.916  1.00   39.39  ? 304  HIS A NE2 1 
ATOM   2254 N N   . ASN A 1 305 ? 10.939  -5.437  28.611  1.00   40.01  ? 305  ASN A N   1 
ATOM   2255 C CA  . ASN A 1 305 ? 10.985  -4.501  29.751  1.00   41.35  ? 305  ASN A CA  1 
ATOM   2256 C C   . ASN A 1 305 ? 11.371  -3.069  29.385  1.00   42.09  ? 305  ASN A C   1 
ATOM   2257 O O   . ASN A 1 305 ? 11.551  -2.231  30.267  1.00   42.08  ? 305  ASN A O   1 
ATOM   2258 C CB  . ASN A 1 305 ? 11.962  -5.016  30.828  1.00   41.26  ? 305  ASN A CB  1 
ATOM   2259 C CG  . ASN A 1 305 ? 11.487  -6.299  31.504  1.00   42.90  ? 305  ASN A CG  1 
ATOM   2260 O OD1 . ASN A 1 305 ? 10.304  -6.455  31.814  1.00   43.80  ? 305  ASN A OD1 1 
ATOM   2261 N ND2 . ASN A 1 305 ? 12.420  -7.219  31.753  1.00   44.52  ? 305  ASN A ND2 1 
ATOM   2262 N N   . GLY A 1 306 ? 11.515  -2.787  28.091  1.00   43.01  ? 306  GLY A N   1 
ATOM   2263 C CA  . GLY A 1 306 ? 11.957  -1.464  27.647  1.00   44.24  ? 306  GLY A CA  1 
ATOM   2264 C C   . GLY A 1 306 ? 13.387  -1.150  28.046  1.00   45.26  ? 306  GLY A C   1 
ATOM   2265 O O   . GLY A 1 306 ? 13.771  0.012   28.148  1.00   45.37  ? 306  GLY A O   1 
ATOM   2266 N N   . GLU A 1 307 ? 14.180  -2.195  28.265  1.00   46.60  ? 307  GLU A N   1 
ATOM   2267 C CA  . GLU A 1 307 ? 15.570  -2.045  28.692  1.00   48.01  ? 307  GLU A CA  1 
ATOM   2268 C C   . GLU A 1 307 ? 16.509  -2.082  27.480  1.00   48.31  ? 307  GLU A C   1 
ATOM   2269 O O   . GLU A 1 307 ? 16.111  -2.508  26.390  1.00   48.14  ? 307  GLU A O   1 
ATOM   2270 C CB  . GLU A 1 307 ? 15.922  -3.115  29.742  1.00   48.38  ? 307  GLU A CB  1 
ATOM   2271 C CG  . GLU A 1 307 ? 17.383  -3.149  30.229  1.00   51.27  ? 307  GLU A CG  1 
ATOM   2272 C CD  . GLU A 1 307 ? 17.899  -1.820  30.793  1.00   54.29  ? 307  GLU A CD  1 
ATOM   2273 O OE1 . GLU A 1 307 ? 17.077  -0.975  31.221  1.00   56.41  ? 307  GLU A OE1 1 
ATOM   2274 O OE2 . GLU A 1 307 ? 19.145  -1.623  30.809  1.00   55.55  ? 307  GLU A OE2 1 
ATOM   2275 N N   . SER A 1 308 ? 17.746  -1.625  27.683  1.00   48.46  ? 308  SER A N   1 
ATOM   2276 C CA  . SER A 1 308 ? 18.705  -1.442  26.603  1.00   48.62  ? 308  SER A CA  1 
ATOM   2277 C C   . SER A 1 308 ? 19.295  -2.763  26.086  1.00   48.49  ? 308  SER A C   1 
ATOM   2278 O O   . SER A 1 308 ? 20.026  -3.460  26.798  1.00   48.47  ? 308  SER A O   1 
ATOM   2279 C CB  . SER A 1 308 ? 19.816  -0.484  27.048  1.00   48.60  ? 308  SER A CB  1 
ATOM   2280 O OG  . SER A 1 308 ? 20.798  -0.350  26.034  1.00   49.84  ? 308  SER A OG  1 
ATOM   2281 N N   . VAL A 1 309 ? 18.971  -3.094  24.840  1.00   48.11  ? 309  VAL A N   1 
ATOM   2282 C CA  . VAL A 1 309 ? 19.515  -4.286  24.200  1.00   48.26  ? 309  VAL A CA  1 
ATOM   2283 C C   . VAL A 1 309 ? 20.927  -4.004  23.662  1.00   48.58  ? 309  VAL A C   1 
ATOM   2284 O O   . VAL A 1 309 ? 21.738  -4.925  23.510  1.00   48.60  ? 309  VAL A O   1 
ATOM   2285 C CB  . VAL A 1 309 ? 18.570  -4.810  23.087  1.00   48.25  ? 309  VAL A CB  1 
ATOM   2286 C CG1 . VAL A 1 309 ? 19.099  -6.101  22.481  1.00   47.99  ? 309  VAL A CG1 1 
ATOM   2287 C CG2 . VAL A 1 309 ? 17.153  -5.028  23.647  1.00   47.75  ? 309  VAL A CG2 1 
ATOM   2288 N N   . SER A 1 310 ? 21.225  -2.727  23.410  0.74   48.82  ? 310  SER A N   1 
ATOM   2289 C CA  . SER A 1 310 ? 22.533  -2.313  22.884  0.74   49.35  ? 310  SER A CA  1 
ATOM   2290 C C   . SER A 1 310 ? 23.698  -2.771  23.766  0.74   49.28  ? 310  SER A C   1 
ATOM   2291 O O   . SER A 1 310 ? 24.783  -3.071  23.264  0.74   49.32  ? 310  SER A O   1 
ATOM   2292 C CB  . SER A 1 310 ? 22.582  -0.793  22.671  0.74   49.38  ? 310  SER A CB  1 
ATOM   2293 O OG  . SER A 1 310 ? 22.442  -0.097  23.901  0.74   50.03  ? 310  SER A OG  1 
ATOM   2294 N N   . TYR A 1 311 ? 23.456  -2.833  25.075  0.64   49.26  ? 311  TYR A N   1 
ATOM   2295 C CA  . TYR A 1 311 ? 24.435  -3.338  26.043  0.64   49.26  ? 311  TYR A CA  1 
ATOM   2296 C C   . TYR A 1 311 ? 25.028  -4.699  25.650  0.64   48.92  ? 311  TYR A C   1 
ATOM   2297 O O   . TYR A 1 311 ? 26.225  -4.929  25.818  0.64   48.61  ? 311  TYR A O   1 
ATOM   2298 C CB  . TYR A 1 311 ? 23.808  -3.403  27.441  0.64   49.45  ? 311  TYR A CB  1 
ATOM   2299 C CG  . TYR A 1 311 ? 24.679  -4.052  28.492  0.64   50.52  ? 311  TYR A CG  1 
ATOM   2300 C CD1 . TYR A 1 311 ? 25.929  -3.519  28.822  0.64   51.50  ? 311  TYR A CD1 1 
ATOM   2301 C CD2 . TYR A 1 311 ? 24.250  -5.194  29.166  0.64   51.19  ? 311  TYR A CD2 1 
ATOM   2302 C CE1 . TYR A 1 311 ? 26.733  -4.114  29.788  0.64   52.57  ? 311  TYR A CE1 1 
ATOM   2303 C CE2 . TYR A 1 311 ? 25.045  -5.795  30.139  0.64   52.46  ? 311  TYR A CE2 1 
ATOM   2304 C CZ  . TYR A 1 311 ? 26.284  -5.251  30.443  0.64   52.79  ? 311  TYR A CZ  1 
ATOM   2305 O OH  . TYR A 1 311 ? 27.075  -5.840  31.402  0.64   53.37  ? 311  TYR A OH  1 
ATOM   2306 N N   . LEU A 1 312 ? 24.186  -5.583  25.115  1.00   48.64  ? 312  LEU A N   1 
ATOM   2307 C CA  . LEU A 1 312 ? 24.624  -6.904  24.652  1.00   48.24  ? 312  LEU A CA  1 
ATOM   2308 C C   . LEU A 1 312 ? 25.548  -6.882  23.427  1.00   48.12  ? 312  LEU A C   1 
ATOM   2309 O O   . LEU A 1 312 ? 26.192  -7.891  23.134  1.00   48.55  ? 312  LEU A O   1 
ATOM   2310 C CB  . LEU A 1 312 ? 23.418  -7.800  24.357  1.00   48.14  ? 312  LEU A CB  1 
ATOM   2311 C CG  . LEU A 1 312 ? 22.541  -8.336  25.493  1.00   48.64  ? 312  LEU A CG  1 
ATOM   2312 C CD1 . LEU A 1 312 ? 21.295  -8.995  24.910  1.00   48.69  ? 312  LEU A CD1 1 
ATOM   2313 C CD2 . LEU A 1 312 ? 23.310  -9.323  26.380  1.00   48.19  ? 312  LEU A CD2 1 
ATOM   2314 N N   . PHE A 1 313 ? 25.615  -5.756  22.713  0.59   47.83  ? 313  PHE A N   1 
ATOM   2315 C CA  . PHE A 1 313 ? 26.447  -5.665  21.503  0.59   47.50  ? 313  PHE A CA  1 
ATOM   2316 C C   . PHE A 1 313 ? 27.939  -5.830  21.803  0.59   47.75  ? 313  PHE A C   1 
ATOM   2317 O O   . PHE A 1 313 ? 28.764  -5.949  20.873  0.59   48.02  ? 313  PHE A O   1 
ATOM   2318 C CB  . PHE A 1 313 ? 26.209  -4.355  20.732  0.59   47.13  ? 313  PHE A CB  1 
ATOM   2319 C CG  . PHE A 1 313 ? 24.833  -4.228  20.125  0.59   45.66  ? 313  PHE A CG  1 
ATOM   2320 C CD1 . PHE A 1 313 ? 24.415  -3.012  19.593  0.59   43.74  ? 313  PHE A CD1 1 
ATOM   2321 C CD2 . PHE A 1 313 ? 23.951  -5.313  20.088  0.59   44.43  ? 313  PHE A CD2 1 
ATOM   2322 C CE1 . PHE A 1 313 ? 23.152  -2.876  19.028  0.59   43.11  ? 313  PHE A CE1 1 
ATOM   2323 C CE2 . PHE A 1 313 ? 22.684  -5.187  19.527  0.59   43.04  ? 313  PHE A CE2 1 
ATOM   2324 C CZ  . PHE A 1 313 ? 22.284  -3.965  18.995  0.59   43.45  ? 313  PHE A CZ  1 
ATOM   2325 N N   . ASN B 1 3   ? 5.593   -10.186 -26.189 0.87   36.35  ? 3    ASN B N   1 
ATOM   2326 C CA  . ASN B 1 3   ? 5.067   -9.525  -24.975 0.87   35.58  ? 3    ASN B CA  1 
ATOM   2327 C C   . ASN B 1 3   ? 4.763   -10.586 -23.917 0.87   34.85  ? 3    ASN B C   1 
ATOM   2328 O O   . ASN B 1 3   ? 4.904   -10.320 -22.734 0.87   34.15  ? 3    ASN B O   1 
ATOM   2329 C CB  . ASN B 1 3   ? 3.817   -8.691  -25.299 0.87   36.00  ? 3    ASN B CB  1 
ATOM   2330 C CG  . ASN B 1 3   ? 3.843   -7.292  -24.665 0.87   37.96  ? 3    ASN B CG  1 
ATOM   2331 O OD1 . ASN B 1 3   ? 3.624   -6.288  -25.353 0.87   40.36  ? 3    ASN B OD1 1 
ATOM   2332 N ND2 . ASN B 1 3   ? 4.092   -7.219  -23.358 0.87   40.72  ? 3    ASN B ND2 1 
ATOM   2333 N N   . ILE B 1 4   ? 4.374   -11.781 -24.366 1.00   33.71  ? 4    ILE B N   1 
ATOM   2334 C CA  . ILE B 1 4   ? 4.020   -12.898 -23.494 1.00   33.22  ? 4    ILE B CA  1 
ATOM   2335 C C   . ILE B 1 4   ? 5.236   -13.791 -23.141 1.00   31.97  ? 4    ILE B C   1 
ATOM   2336 O O   . ILE B 1 4   ? 6.030   -14.142 -24.015 1.00   31.79  ? 4    ILE B O   1 
ATOM   2337 C CB  . ILE B 1 4   ? 2.864   -13.723 -24.152 1.00   33.75  ? 4    ILE B CB  1 
ATOM   2338 C CG1 . ILE B 1 4   ? 1.945   -14.415 -23.120 1.00   33.93  ? 4    ILE B CG1 1 
ATOM   2339 C CG2 . ILE B 1 4   ? 3.387   -14.624 -25.304 1.00   35.50  ? 4    ILE B CG2 1 
ATOM   2340 C CD1 . ILE B 1 4   ? 2.490   -15.669 -22.458 1.00   35.45  ? 4    ILE B CD1 1 
ATOM   2341 N N   . LYS B 1 5   ? 5.372   -14.157 -21.861 0.87   29.55  ? 5    LYS B N   1 
ATOM   2342 C CA  . LYS B 1 5   ? 6.489   -14.985 -21.417 0.87   27.96  ? 5    LYS B CA  1 
ATOM   2343 C C   . LYS B 1 5   ? 6.064   -15.963 -20.317 0.87   27.75  ? 5    LYS B C   1 
ATOM   2344 O O   . LYS B 1 5   ? 5.547   -15.560 -19.268 0.87   26.33  ? 5    LYS B O   1 
ATOM   2345 C CB  . LYS B 1 5   ? 7.665   -14.117 -20.950 0.87   27.88  ? 5    LYS B CB  1 
ATOM   2346 N N   . ILE B 1 6   ? 6.294   -17.250 -20.563 1.00   26.74  ? 6    ILE B N   1 
ATOM   2347 C CA  . ILE B 1 6   ? 5.858   -18.289 -19.637 1.00   27.49  ? 6    ILE B CA  1 
ATOM   2348 C C   . ILE B 1 6   ? 7.057   -18.950 -18.985 1.00   27.00  ? 6    ILE B C   1 
ATOM   2349 O O   . ILE B 1 6   ? 8.005   -19.327 -19.666 1.00   26.69  ? 6    ILE B O   1 
ATOM   2350 C CB  . ILE B 1 6   ? 5.038   -19.408 -20.318 1.00   27.12  ? 6    ILE B CB  1 
ATOM   2351 C CG1 . ILE B 1 6   ? 3.897   -18.835 -21.145 1.00   30.87  ? 6    ILE B CG1 1 
ATOM   2352 C CG2 . ILE B 1 6   ? 4.452   -20.367 -19.260 1.00   27.00  ? 6    ILE B CG2 1 
ATOM   2353 C CD1 . ILE B 1 6   ? 3.410   -19.810 -22.211 1.00   32.54  ? 6    ILE B CD1 1 
ATOM   2354 N N   . PHE B 1 7   ? 6.988   -19.100 -17.669 1.00   27.12  ? 7    PHE B N   1 
ATOM   2355 C CA  . PHE B 1 7   ? 8.051   -19.747 -16.895 1.00   28.21  ? 7    PHE B CA  1 
ATOM   2356 C C   . PHE B 1 7   ? 7.442   -20.834 -16.030 1.00   29.57  ? 7    PHE B C   1 
ATOM   2357 O O   . PHE B 1 7   ? 6.290   -20.722 -15.593 1.00   28.80  ? 7    PHE B O   1 
ATOM   2358 C CB  . PHE B 1 7   ? 8.776   -18.747 -15.978 1.00   27.76  ? 7    PHE B CB  1 
ATOM   2359 C CG  . PHE B 1 7   ? 9.618   -17.729 -16.703 1.00   27.80  ? 7    PHE B CG  1 
ATOM   2360 C CD1 . PHE B 1 7   ? 9.086   -16.496 -17.056 1.00   28.65  ? 7    PHE B CD1 1 
ATOM   2361 C CD2 . PHE B 1 7   ? 10.947  -17.995 -17.009 1.00   26.93  ? 7    PHE B CD2 1 
ATOM   2362 C CE1 . PHE B 1 7   ? 9.867   -15.543 -17.712 1.00   28.83  ? 7    PHE B CE1 1 
ATOM   2363 C CE2 . PHE B 1 7   ? 11.740  -17.050 -17.659 1.00   28.00  ? 7    PHE B CE2 1 
ATOM   2364 C CZ  . PHE B 1 7   ? 11.200  -15.825 -18.019 1.00   27.71  ? 7    PHE B CZ  1 
ATOM   2365 N N   . SER B 1 8   ? 8.229   -21.871 -15.776 1.00   31.52  ? 8    SER B N   1 
ATOM   2366 C CA  . SER B 1 8   ? 7.843   -22.960 -14.899 1.00   34.19  ? 8    SER B CA  1 
ATOM   2367 C C   . SER B 1 8   ? 8.602   -22.925 -13.582 1.00   35.83  ? 8    SER B C   1 
ATOM   2368 O O   . SER B 1 8   ? 9.732   -22.440 -13.529 1.00   36.07  ? 8    SER B O   1 
ATOM   2369 C CB  . SER B 1 8   ? 8.172   -24.293 -15.556 1.00   34.21  ? 8    SER B CB  1 
ATOM   2370 O OG  . SER B 1 8   ? 7.934   -25.344 -14.629 1.00   35.67  ? 8    SER B OG  1 
ATOM   2371 N N   . GLY B 1 9   ? 7.983   -23.483 -12.540 0.60   37.89  ? 9    GLY B N   1 
ATOM   2372 C CA  . GLY B 1 9   ? 8.672   -23.818 -11.288 0.60   40.02  ? 9    GLY B CA  1 
ATOM   2373 C C   . GLY B 1 9   ? 9.269   -25.221 -11.201 0.60   41.87  ? 9    GLY B C   1 
ATOM   2374 O O   . GLY B 1 9   ? 8.684   -26.191 -11.699 0.60   42.18  ? 9    GLY B O   1 
ATOM   2375 N N   . SER B 1 10  ? 10.462  -25.315 -10.629 0.69   43.59  ? 10   SER B N   1 
ATOM   2376 C CA  . SER B 1 10  ? 11.215  -26.571 -10.452 0.69   45.19  ? 10   SER B CA  1 
ATOM   2377 C C   . SER B 1 10  ? 11.644  -27.406 -11.668 0.69   46.11  ? 10   SER B C   1 
ATOM   2378 O O   . SER B 1 10  ? 12.465  -26.961 -12.479 0.69   46.53  ? 10   SER B O   1 
ATOM   2379 C CB  . SER B 1 10  ? 10.649  -27.481 -9.348  0.69   45.35  ? 10   SER B CB  1 
ATOM   2380 O OG  . SER B 1 10  ? 9.651   -28.357 -9.847  0.69   47.21  ? 10   SER B OG  1 
ATOM   2381 N N   . SER B 1 11  ? 11.113  -28.629 -11.756 0.86   47.11  ? 11   SER B N   1 
ATOM   2382 C CA  . SER B 1 11  ? 11.463  -29.555 -12.831 0.86   47.94  ? 11   SER B CA  1 
ATOM   2383 C C   . SER B 1 11  ? 10.295  -30.526 -12.959 0.86   48.06  ? 11   SER B C   1 
ATOM   2384 O O   . SER B 1 11  ? 10.459  -31.630 -13.514 0.86   48.82  ? 11   SER B O   1 
ATOM   2385 C CB  . SER B 1 11  ? 12.708  -30.427 -12.624 0.86   48.25  ? 11   SER B CB  1 
ATOM   2386 O OG  . SER B 1 11  ? 12.975  -31.203 -13.781 0.86   48.88  ? 11   SER B OG  1 
ATOM   2387 N N   . HIS B 1 12  ? 9.128   -30.126 -12.441 0.69   47.72  ? 12   HIS B N   1 
ATOM   2388 C CA  . HIS B 1 12  ? 7.880   -30.856 -12.687 0.69   47.31  ? 12   HIS B CA  1 
ATOM   2389 C C   . HIS B 1 12  ? 7.190   -30.019 -13.760 0.69   46.66  ? 12   HIS B C   1 
ATOM   2390 O O   . HIS B 1 12  ? 6.092   -29.477 -13.556 0.69   46.71  ? 12   HIS B O   1 
ATOM   2391 C CB  . HIS B 1 12  ? 7.002   -30.986 -11.438 0.69   47.68  ? 12   HIS B CB  1 
ATOM   2392 C CG  . HIS B 1 12  ? 7.388   -32.125 -10.547 0.69   48.23  ? 12   HIS B CG  1 
ATOM   2393 N ND1 . HIS B 1 12  ? 6.788   -33.363 -10.623 0.69   49.15  ? 12   HIS B ND1 1 
ATOM   2394 C CD2 . HIS B 1 12  ? 8.323   -32.217 -9.571  0.69   48.90  ? 12   HIS B CD2 1 
ATOM   2395 C CE1 . HIS B 1 12  ? 7.329   -34.166 -9.723  0.69   50.35  ? 12   HIS B CE1 1 
ATOM   2396 N NE2 . HIS B 1 12  ? 8.260   -33.494 -9.068  0.69   49.78  ? 12   HIS B NE2 1 
ATOM   2397 N N   . GLN B 1 13  ? 7.854   -29.934 -14.912 1.00   46.13  ? 13   GLN B N   1 
ATOM   2398 C CA  . GLN B 1 13  ? 7.492   -28.996 -15.974 1.00   44.83  ? 13   GLN B CA  1 
ATOM   2399 C C   . GLN B 1 13  ? 6.474   -29.530 -16.970 1.00   43.23  ? 13   GLN B C   1 
ATOM   2400 O O   . GLN B 1 13  ? 6.233   -28.888 -18.006 1.00   43.49  ? 13   GLN B O   1 
ATOM   2401 C CB  . GLN B 1 13  ? 8.749   -28.541 -16.733 1.00   45.50  ? 13   GLN B CB  1 
ATOM   2402 C CG  . GLN B 1 13  ? 9.740   -27.727 -15.898 1.00   47.64  ? 13   GLN B CG  1 
ATOM   2403 C CD  . GLN B 1 13  ? 10.796  -27.047 -16.756 1.00   50.57  ? 13   GLN B CD  1 
ATOM   2404 O OE1 . GLN B 1 13  ? 10.873  -25.816 -16.809 1.00   51.84  ? 13   GLN B OE1 1 
ATOM   2405 N NE2 . GLN B 1 13  ? 11.611  -27.847 -17.443 1.00   51.71  ? 13   GLN B NE2 1 
ATOM   2406 N N   . ASP B 1 14  ? 5.863   -30.676 -16.673 0.66   40.88  ? 14   ASP B N   1 
ATOM   2407 C CA  . ASP B 1 14  ? 4.961   -31.303 -17.631 0.66   38.91  ? 14   ASP B CA  1 
ATOM   2408 C C   . ASP B 1 14  ? 3.796   -30.388 -17.993 0.66   37.06  ? 14   ASP B C   1 
ATOM   2409 O O   . ASP B 1 14  ? 3.597   -30.078 -19.166 0.66   36.02  ? 14   ASP B O   1 
ATOM   2410 C CB  . ASP B 1 14  ? 4.449   -32.658 -17.140 0.66   39.45  ? 14   ASP B CB  1 
ATOM   2411 C CG  . ASP B 1 14  ? 3.822   -33.469 -18.257 0.66   41.05  ? 14   ASP B CG  1 
ATOM   2412 O OD1 . ASP B 1 14  ? 4.577   -34.053 -19.069 0.66   42.75  ? 14   ASP B OD1 1 
ATOM   2413 O OD2 . ASP B 1 14  ? 2.574   -33.514 -18.334 0.66   43.64  ? 14   ASP B OD2 1 
ATOM   2414 N N   . LEU B 1 15  ? 3.048   -29.949 -16.979 1.00   35.18  ? 15   LEU B N   1 
ATOM   2415 C CA  . LEU B 1 15  ? 1.915   -29.057 -17.179 1.00   33.55  ? 15   LEU B CA  1 
ATOM   2416 C C   . LEU B 1 15  ? 2.369   -27.768 -17.859 1.00   32.36  ? 15   LEU B C   1 
ATOM   2417 O O   . LEU B 1 15  ? 1.780   -27.363 -18.854 1.00   31.36  ? 15   LEU B O   1 
ATOM   2418 C CB  . LEU B 1 15  ? 1.225   -28.733 -15.852 1.00   33.31  ? 15   LEU B CB  1 
ATOM   2419 C CG  . LEU B 1 15  ? -0.309  -28.618 -15.814 1.00   34.47  ? 15   LEU B CG  1 
ATOM   2420 C CD1 . LEU B 1 15  ? -0.752  -27.778 -14.605 1.00   33.39  ? 15   LEU B CD1 1 
ATOM   2421 C CD2 . LEU B 1 15  ? -0.958  -28.091 -17.091 1.00   32.15  ? 15   LEU B CD2 1 
ATOM   2422 N N   . SER B 1 16  ? 3.425   -27.155 -17.321 1.00   31.69  ? 16   SER B N   1 
ATOM   2423 C CA  . SER B 1 16  ? 4.001   -25.921 -17.870 1.00   32.28  ? 16   SER B CA  1 
ATOM   2424 C C   . SER B 1 16  ? 4.346   -26.053 -19.358 1.00   31.60  ? 16   SER B C   1 
ATOM   2425 O O   . SER B 1 16  ? 4.061   -25.154 -20.142 1.00   31.25  ? 16   SER B O   1 
ATOM   2426 C CB  . SER B 1 16  ? 5.265   -25.519 -17.106 1.00   31.99  ? 16   SER B CB  1 
ATOM   2427 O OG  . SER B 1 16  ? 5.010   -25.372 -15.718 1.00   36.79  ? 16   SER B OG  1 
ATOM   2428 N N   . GLN B 1 17  ? 4.972   -27.172 -19.722 1.00   31.81  ? 17   GLN B N   1 
ATOM   2429 C CA  . GLN B 1 17  ? 5.355   -27.442 -21.114 1.00   31.90  ? 17   GLN B CA  1 
ATOM   2430 C C   . GLN B 1 17  ? 4.135   -27.633 -21.992 1.00   30.98  ? 17   GLN B C   1 
ATOM   2431 O O   . GLN B 1 17  ? 4.085   -27.120 -23.110 1.00   31.75  ? 17   GLN B O   1 
ATOM   2432 C CB  . GLN B 1 17  ? 6.307   -28.643 -21.211 1.00   32.24  ? 17   GLN B CB  1 
ATOM   2433 C CG  . GLN B 1 17  ? 6.885   -28.879 -22.613 1.00   35.49  ? 17   GLN B CG  1 
ATOM   2434 C CD  . GLN B 1 17  ? 7.623   -27.657 -23.149 1.00   38.41  ? 17   GLN B CD  1 
ATOM   2435 O OE1 . GLN B 1 17  ? 8.638   -27.239 -22.593 1.00   41.91  ? 17   GLN B OE1 1 
ATOM   2436 N NE2 . GLN B 1 17  ? 7.103   -27.072 -24.224 1.00   40.08  ? 17   GLN B NE2 1 
ATOM   2437 N N   . LYS B 1 18  ? 3.143   -28.353 -21.482 1.00   30.37  ? 18   LYS B N   1 
ATOM   2438 C CA  . LYS B 1 18  ? 1.887   -28.541 -22.204 1.00   30.00  ? 18   LYS B CA  1 
ATOM   2439 C C   . LYS B 1 18  ? 1.212   -27.196 -22.523 1.00   29.11  ? 18   LYS B C   1 
ATOM   2440 O O   . LYS B 1 18  ? 0.713   -26.986 -23.637 1.00   28.69  ? 18   LYS B O   1 
ATOM   2441 C CB  . LYS B 1 18  ? 0.930   -29.438 -21.412 1.00   30.46  ? 18   LYS B CB  1 
ATOM   2442 C CG  . LYS B 1 18  ? 1.167   -30.936 -21.539 1.00   31.62  ? 18   LYS B CG  1 
ATOM   2443 C CD  . LYS B 1 18  ? 0.039   -31.718 -20.852 1.00   34.37  ? 18   LYS B CD  1 
ATOM   2444 C CE  . LYS B 1 18  ? 0.251   -33.236 -20.915 1.00   35.11  ? 18   LYS B CE  1 
ATOM   2445 N N   . ILE B 1 19  ? 1.219   -26.291 -21.542 1.00   28.09  ? 19   ILE B N   1 
ATOM   2446 C CA  . ILE B 1 19  ? 0.612   -24.967 -21.694 1.00   27.37  ? 19   ILE B CA  1 
ATOM   2447 C C   . ILE B 1 19  ? 1.401   -24.138 -22.694 1.00   26.83  ? 19   ILE B C   1 
ATOM   2448 O O   . ILE B 1 19  ? 0.816   -23.508 -23.569 1.00   26.05  ? 19   ILE B O   1 
ATOM   2449 C CB  . ILE B 1 19  ? 0.527   -24.200 -20.342 1.00   27.41  ? 19   ILE B CB  1 
ATOM   2450 C CG1 . ILE B 1 19  ? -0.483  -24.868 -19.409 1.00   27.44  ? 19   ILE B CG1 1 
ATOM   2451 C CG2 . ILE B 1 19  ? 0.126   -22.758 -20.569 1.00   27.42  ? 19   ILE B CG2 1 
ATOM   2452 C CD1 . ILE B 1 19  ? -0.290  -24.535 -17.930 1.00   25.81  ? 19   ILE B CD1 1 
ATOM   2453 N N   . ALA B 1 20  ? 2.725   -24.129 -22.536 1.00   26.42  ? 20   ALA B N   1 
ATOM   2454 C CA  . ALA B 1 20  ? 3.598   -23.385 -23.433 1.00   27.33  ? 20   ALA B CA  1 
ATOM   2455 C C   . ALA B 1 20  ? 3.397   -23.881 -24.877 1.00   27.17  ? 20   ALA B C   1 
ATOM   2456 O O   . ALA B 1 20  ? 3.142   -23.069 -25.768 1.00   26.56  ? 20   ALA B O   1 
ATOM   2457 C CB  . ALA B 1 20  ? 5.059   -23.490 -22.987 1.00   27.41  ? 20   ALA B CB  1 
ATOM   2458 N N   . ASP B 1 21  ? 3.429   -25.205 -25.068 0.67   27.68  ? 21   ASP B N   1 
ATOM   2459 C CA  . ASP B 1 21  ? 3.105   -25.842 -26.362 0.67   28.72  ? 21   ASP B CA  1 
ATOM   2460 C C   . ASP B 1 21  ? 1.818   -25.293 -26.975 0.67   29.35  ? 21   ASP B C   1 
ATOM   2461 O O   . ASP B 1 21  ? 1.812   -24.848 -28.123 0.67   28.69  ? 21   ASP B O   1 
ATOM   2462 C CB  . ASP B 1 21  ? 2.950   -27.368 -26.219 0.67   28.95  ? 21   ASP B CB  1 
ATOM   2463 C CG  . ASP B 1 21  ? 4.266   -28.089 -25.976 0.67   30.23  ? 21   ASP B CG  1 
ATOM   2464 O OD1 . ASP B 1 21  ? 5.330   -27.435 -25.950 0.67   32.17  ? 21   ASP B OD1 1 
ATOM   2465 O OD2 . ASP B 1 21  ? 4.235   -29.336 -25.808 0.67   31.50  ? 21   ASP B OD2 1 
ATOM   2466 N N   . ARG B 1 22  ? 0.730   -25.325 -26.200 1.00   30.58  ? 22   ARG B N   1 
ATOM   2467 C CA  . ARG B 1 22  ? -0.580  -24.874 -26.690 1.00   31.57  ? 22   ARG B CA  1 
ATOM   2468 C C   . ARG B 1 22  ? -0.598  -23.402 -27.102 1.00   31.62  ? 22   ARG B C   1 
ATOM   2469 O O   . ARG B 1 22  ? -1.371  -23.008 -27.989 1.00   32.25  ? 22   ARG B O   1 
ATOM   2470 C CB  . ARG B 1 22  ? -1.687  -25.174 -25.687 1.00   31.88  ? 22   ARG B CB  1 
ATOM   2471 C CG  . ARG B 1 22  ? -1.826  -26.658 -25.384 1.00   35.91  ? 22   ARG B CG  1 
ATOM   2472 C CD  . ARG B 1 22  ? -3.070  -26.976 -24.581 1.00   41.60  ? 22   ARG B CD  1 
ATOM   2473 N NE  . ARG B 1 22  ? -4.173  -27.334 -25.464 1.00   48.12  ? 22   ARG B NE  1 
ATOM   2474 C CZ  . ARG B 1 22  ? -4.532  -28.582 -25.766 1.00   49.69  ? 22   ARG B CZ  1 
ATOM   2475 N NH1 . ARG B 1 22  ? -3.890  -29.622 -25.243 1.00   50.92  ? 22   ARG B NH1 1 
ATOM   2476 N NH2 . ARG B 1 22  ? -5.554  -28.787 -26.586 1.00   50.39  ? 22   ARG B NH2 1 
ATOM   2477 N N   . LEU B 1 23  ? 0.265   -22.599 -26.485 1.00   30.84  ? 23   LEU B N   1 
ATOM   2478 C CA  . LEU B 1 23  ? 0.373   -21.180 -26.838 1.00   30.52  ? 23   LEU B CA  1 
ATOM   2479 C C   . LEU B 1 23  ? 1.417   -20.907 -27.926 1.00   30.05  ? 23   LEU B C   1 
ATOM   2480 O O   . LEU B 1 23  ? 1.580   -19.769 -28.362 1.00   30.12  ? 23   LEU B O   1 
ATOM   2481 C CB  . LEU B 1 23  ? 0.685   -20.353 -25.598 1.00   30.30  ? 23   LEU B CB  1 
ATOM   2482 C CG  . LEU B 1 23  ? -0.328  -20.397 -24.440 1.00   30.54  ? 23   LEU B CG  1 
ATOM   2483 C CD1 . LEU B 1 23  ? 0.341   -19.963 -23.160 1.00   31.86  ? 23   LEU B CD1 1 
ATOM   2484 C CD2 . LEU B 1 23  ? -1.527  -19.508 -24.724 1.00   30.50  ? 23   LEU B CD2 1 
ATOM   2485 N N   . GLY B 1 24  ? 2.137   -21.945 -28.339 1.00   29.65  ? 24   GLY B N   1 
ATOM   2486 C CA  . GLY B 1 24  ? 3.139   -21.802 -29.395 1.00   28.93  ? 24   GLY B CA  1 
ATOM   2487 C C   . GLY B 1 24  ? 4.413   -21.173 -28.890 1.00   27.99  ? 24   GLY B C   1 
ATOM   2488 O O   . GLY B 1 24  ? 5.092   -20.463 -29.629 1.00   27.91  ? 24   GLY B O   1 
ATOM   2489 N N   . LEU B 1 25  ? 4.736   -21.429 -27.622 1.00   27.31  ? 25   LEU B N   1 
ATOM   2490 C CA  . LEU B 1 25  ? 5.893   -20.808 -26.995 1.00   26.95  ? 25   LEU B CA  1 
ATOM   2491 C C   . LEU B 1 25  ? 6.823   -21.849 -26.356 1.00   26.71  ? 25   LEU B C   1 
ATOM   2492 O O   . LEU B 1 25  ? 6.400   -22.951 -26.025 1.00   25.95  ? 25   LEU B O   1 
ATOM   2493 C CB  . LEU B 1 25  ? 5.446   -19.768 -25.948 1.00   27.62  ? 25   LEU B CB  1 
ATOM   2494 C CG  . LEU B 1 25  ? 4.457   -18.664 -26.365 1.00   28.39  ? 25   LEU B CG  1 
ATOM   2495 C CD1 . LEU B 1 25  ? 3.950   -17.912 -25.138 1.00   29.38  ? 25   LEU B CD1 1 
ATOM   2496 C CD2 . LEU B 1 25  ? 5.048   -17.687 -27.395 1.00   29.02  ? 25   LEU B CD2 1 
ATOM   2497 N N   . GLU B 1 26  ? 8.094   -21.488 -26.236 1.00   26.26  ? 26   GLU B N   1 
ATOM   2498 C CA  . GLU B 1 26  ? 9.031   -22.197 -25.393 1.00   27.06  ? 26   GLU B CA  1 
ATOM   2499 C C   . GLU B 1 26  ? 8.999   -21.576 -24.005 1.00   26.82  ? 26   GLU B C   1 
ATOM   2500 O O   . GLU B 1 26  ? 8.887   -20.360 -23.881 1.00   25.52  ? 26   GLU B O   1 
ATOM   2501 C CB  . GLU B 1 26  ? 10.441  -22.070 -25.940 1.00   27.35  ? 26   GLU B CB  1 
ATOM   2502 C CG  . GLU B 1 26  ? 10.718  -23.002 -27.108 1.00   31.35  ? 26   GLU B CG  1 
ATOM   2503 C CD  . GLU B 1 26  ? 12.155  -22.864 -27.606 1.00   35.68  ? 26   GLU B CD  1 
ATOM   2504 O OE1 . GLU B 1 26  ? 12.950  -22.104 -26.988 1.00   39.25  ? 26   GLU B OE1 1 
ATOM   2505 O OE2 . GLU B 1 26  ? 12.487  -23.537 -28.619 1.00   38.26  ? 26   GLU B OE2 1 
ATOM   2506 N N   . LEU B 1 27  ? 9.074   -22.420 -22.976 1.00   27.10  ? 27   LEU B N   1 
ATOM   2507 C CA  . LEU B 1 27  ? 9.241   -21.951 -21.601 1.00   27.81  ? 27   LEU B CA  1 
ATOM   2508 C C   . LEU B 1 27  ? 10.507  -21.103 -21.483 1.00   28.36  ? 27   LEU B C   1 
ATOM   2509 O O   . LEU B 1 27  ? 11.541  -21.448 -22.057 1.00   28.37  ? 27   LEU B O   1 
ATOM   2510 C CB  . LEU B 1 27  ? 9.305   -23.144 -20.627 1.00   27.91  ? 27   LEU B CB  1 
ATOM   2511 C CG  . LEU B 1 27  ? 8.018   -23.924 -20.327 1.00   26.30  ? 27   LEU B CG  1 
ATOM   2512 C CD1 . LEU B 1 27  ? 8.322   -25.144 -19.427 1.00   27.06  ? 27   LEU B CD1 1 
ATOM   2513 C CD2 . LEU B 1 27  ? 6.971   -23.023 -19.670 1.00   27.05  ? 27   LEU B CD2 1 
ATOM   2514 N N   . GLY B 1 28  ? 10.417  -19.997 -20.746 1.00   29.19  ? 28   GLY B N   1 
ATOM   2515 C CA  . GLY B 1 28  ? 11.564  -19.124 -20.487 1.00   30.02  ? 28   GLY B CA  1 
ATOM   2516 C C   . GLY B 1 28  ? 12.697  -19.793 -19.720 1.00   31.03  ? 28   GLY B C   1 
ATOM   2517 O O   . GLY B 1 28  ? 12.472  -20.695 -18.912 1.00   29.81  ? 28   GLY B O   1 
ATOM   2518 N N   . LYS B 1 29  ? 13.923  -19.355 -19.997 1.00   32.43  ? 29   LYS B N   1 
ATOM   2519 C CA  . LYS B 1 29  ? 15.116  -19.920 -19.360 1.00   34.75  ? 29   LYS B CA  1 
ATOM   2520 C C   . LYS B 1 29  ? 15.210  -19.482 -17.896 1.00   35.45  ? 29   LYS B C   1 
ATOM   2521 O O   . LYS B 1 29  ? 15.145  -18.290 -17.609 1.00   35.14  ? 29   LYS B O   1 
ATOM   2522 C CB  . LYS B 1 29  ? 16.378  -19.461 -20.097 1.00   34.72  ? 29   LYS B CB  1 
ATOM   2523 C CG  . LYS B 1 29  ? 16.290  -19.563 -21.603 1.00   37.83  ? 29   LYS B CG  1 
ATOM   2524 C CD  . LYS B 1 29  ? 17.310  -18.636 -22.283 1.00   40.47  ? 29   LYS B CD  1 
ATOM   2525 C CE  . LYS B 1 29  ? 17.189  -18.704 -23.792 1.00   43.18  ? 29   LYS B CE  1 
ATOM   2526 N NZ  . LYS B 1 29  ? 17.516  -20.079 -24.311 1.00   44.30  ? 29   LYS B NZ  1 
ATOM   2527 N N   . VAL B 1 30  ? 15.340  -20.452 -16.988 1.00   37.05  ? 30   VAL B N   1 
ATOM   2528 C CA  . VAL B 1 30  ? 15.545  -20.193 -15.557 1.00   39.22  ? 30   VAL B CA  1 
ATOM   2529 C C   . VAL B 1 30  ? 16.675  -21.090 -15.058 1.00   40.72  ? 30   VAL B C   1 
ATOM   2530 O O   . VAL B 1 30  ? 16.677  -22.291 -15.334 1.00   40.77  ? 30   VAL B O   1 
ATOM   2531 C CB  . VAL B 1 30  ? 14.279  -20.508 -14.703 1.00   39.21  ? 30   VAL B CB  1 
ATOM   2532 C CG1 . VAL B 1 30  ? 14.406  -19.918 -13.305 1.00   38.69  ? 30   VAL B CG1 1 
ATOM   2533 C CG2 . VAL B 1 30  ? 13.019  -19.988 -15.364 1.00   39.49  ? 30   VAL B CG2 1 
ATOM   2534 N N   . VAL B 1 31  ? 17.639  -20.504 -14.351 1.00   42.49  ? 31   VAL B N   1 
ATOM   2535 C CA  . VAL B 1 31  ? 18.688  -21.272 -13.668 1.00   44.95  ? 31   VAL B CA  1 
ATOM   2536 C C   . VAL B 1 31  ? 18.236  -21.415 -12.224 1.00   46.22  ? 31   VAL B C   1 
ATOM   2537 O O   . VAL B 1 31  ? 18.340  -20.469 -11.442 1.00   46.45  ? 31   VAL B O   1 
ATOM   2538 C CB  . VAL B 1 31  ? 20.082  -20.577 -13.727 1.00   44.75  ? 31   VAL B CB  1 
ATOM   2539 C CG1 . VAL B 1 31  ? 21.120  -21.348 -12.893 1.00   46.14  ? 31   VAL B CG1 1 
ATOM   2540 C CG2 . VAL B 1 31  ? 20.562  -20.447 -15.160 1.00   45.50  ? 31   VAL B CG2 1 
ATOM   2541 N N   . THR B 1 32  ? 17.733  -22.601 -11.889 0.84   48.04  ? 32   THR B N   1 
ATOM   2542 C CA  . THR B 1 32  ? 16.909  -22.796 -10.694 0.84   49.81  ? 32   THR B CA  1 
ATOM   2543 C C   . THR B 1 32  ? 17.325  -24.029 -9.896  0.84   50.63  ? 32   THR B C   1 
ATOM   2544 O O   . THR B 1 32  ? 16.908  -25.152 -10.198 0.84   51.46  ? 32   THR B O   1 
ATOM   2545 C CB  . THR B 1 32  ? 15.384  -22.819 -11.055 0.84   49.78  ? 32   THR B CB  1 
ATOM   2546 O OG1 . THR B 1 32  ? 14.626  -23.425 -9.997  0.84   51.45  ? 32   THR B OG1 1 
ATOM   2547 C CG2 . THR B 1 32  ? 15.126  -23.578 -12.365 0.84   50.81  ? 32   THR B CG2 1 
ATOM   2548 N N   . LYS B 1 33  ? 18.151  -23.805 -8.874  0.35   51.37  ? 33   LYS B N   1 
ATOM   2549 C CA  . LYS B 1 33  ? 18.727  -24.888 -8.074  0.35   51.86  ? 33   LYS B CA  1 
ATOM   2550 C C   . LYS B 1 33  ? 18.552  -24.653 -6.577  0.35   52.19  ? 33   LYS B C   1 
ATOM   2551 O O   . LYS B 1 33  ? 18.396  -23.511 -6.134  0.35   52.24  ? 33   LYS B O   1 
ATOM   2552 C CB  . LYS B 1 33  ? 20.213  -25.043 -8.398  0.35   51.88  ? 33   LYS B CB  1 
ATOM   2553 C CG  . LYS B 1 33  ? 21.033  -23.789 -8.114  0.35   51.91  ? 33   LYS B CG  1 
ATOM   2554 C CD  . LYS B 1 33  ? 22.484  -24.002 -8.508  0.35   52.41  ? 33   LYS B CD  1 
ATOM   2555 C CE  . LYS B 1 33  ? 23.284  -22.710 -8.404  0.35   52.46  ? 33   LYS B CE  1 
ATOM   2556 N NZ  . LYS B 1 33  ? 24.657  -22.890 -8.975  0.35   52.70  ? 33   LYS B NZ  1 
ATOM   2557 N N   . LYS B 1 34  ? 18.584  -25.741 -5.807  0.67   52.58  ? 34   LYS B N   1 
ATOM   2558 C CA  . LYS B 1 34  ? 18.469  -25.675 -4.352  0.67   52.86  ? 34   LYS B CA  1 
ATOM   2559 C C   . LYS B 1 34  ? 19.836  -25.820 -3.685  0.67   53.25  ? 34   LYS B C   1 
ATOM   2560 O O   . LYS B 1 34  ? 20.563  -26.793 -3.930  0.67   53.27  ? 34   LYS B O   1 
ATOM   2561 C CB  . LYS B 1 34  ? 17.497  -26.739 -3.828  0.67   52.64  ? 34   LYS B CB  1 
ATOM   2562 N N   . PHE B 1 35  ? 20.179  -24.844 -2.845  0.52   53.62  ? 35   PHE B N   1 
ATOM   2563 C CA  . PHE B 1 35  ? 21.437  -24.854 -2.101  0.52   54.02  ? 35   PHE B CA  1 
ATOM   2564 C C   . PHE B 1 35  ? 21.573  -26.091 -1.227  0.52   54.12  ? 35   PHE B C   1 
ATOM   2565 O O   . PHE B 1 35  ? 20.586  -26.780 -0.933  0.52   54.16  ? 35   PHE B O   1 
ATOM   2566 C CB  . PHE B 1 35  ? 21.580  -23.602 -1.222  0.52   54.13  ? 35   PHE B CB  1 
ATOM   2567 C CG  . PHE B 1 35  ? 22.126  -22.396 -1.943  0.52   54.77  ? 35   PHE B CG  1 
ATOM   2568 C CD1 . PHE B 1 35  ? 21.618  -21.129 -1.677  0.52   55.27  ? 35   PHE B CD1 1 
ATOM   2569 C CD2 . PHE B 1 35  ? 23.153  -22.521 -2.879  0.52   55.56  ? 35   PHE B CD2 1 
ATOM   2570 C CE1 . PHE B 1 35  ? 22.116  -20.004 -2.334  0.52   55.68  ? 35   PHE B CE1 1 
ATOM   2571 C CE2 . PHE B 1 35  ? 23.657  -21.399 -3.542  0.52   55.80  ? 35   PHE B CE2 1 
ATOM   2572 C CZ  . PHE B 1 35  ? 23.136  -20.140 -3.269  0.52   55.60  ? 35   PHE B CZ  1 
ATOM   2573 N N   . SER B 1 36  ? 22.813  -26.359 -0.814  0.61   54.47  ? 36   SER B N   1 
ATOM   2574 C CA  . SER B 1 36  ? 23.111  -27.470 0.076   0.61   54.57  ? 36   SER B CA  1 
ATOM   2575 C C   . SER B 1 36  ? 22.334  -27.293 1.373   0.61   54.56  ? 36   SER B C   1 
ATOM   2576 O O   . SER B 1 36  ? 22.082  -28.259 2.092   0.61   54.77  ? 36   SER B O   1 
ATOM   2577 C CB  . SER B 1 36  ? 24.610  -27.527 0.356   0.61   54.60  ? 36   SER B CB  1 
ATOM   2578 O OG  . SER B 1 36  ? 24.980  -28.771 0.926   0.61   55.12  ? 36   SER B OG  1 
ATOM   2579 N N   . ASN B 1 37  ? 21.950  -26.051 1.658   0.38   54.31  ? 37   ASN B N   1 
ATOM   2580 C CA  . ASN B 1 37  ? 21.128  -25.753 2.824   0.38   53.96  ? 37   ASN B CA  1 
ATOM   2581 C C   . ASN B 1 37  ? 19.684  -25.395 2.463   0.38   53.68  ? 37   ASN B C   1 
ATOM   2582 O O   . ASN B 1 37  ? 19.103  -24.456 3.035   0.38   53.72  ? 37   ASN B O   1 
ATOM   2583 C CB  . ASN B 1 37  ? 21.750  -24.637 3.660   0.38   53.99  ? 37   ASN B CB  1 
ATOM   2584 C CG  . ASN B 1 37  ? 21.393  -23.261 3.149   0.38   54.08  ? 37   ASN B CG  1 
ATOM   2585 O OD1 . ASN B 1 37  ? 21.557  -22.967 1.959   0.38   54.30  ? 37   ASN B OD1 1 
ATOM   2586 N ND2 . ASN B 1 37  ? 20.901  -22.409 4.046   0.38   53.83  ? 37   ASN B ND2 1 
ATOM   2587 N N   . GLN B 1 38  ? 19.129  -26.144 1.499   0.78   53.33  ? 38   GLN B N   1 
ATOM   2588 C CA  . GLN B 1 38  ? 17.685  -26.147 1.162   0.78   52.67  ? 38   GLN B CA  1 
ATOM   2589 C C   . GLN B 1 38  ? 17.100  -24.749 0.862   0.78   51.75  ? 38   GLN B C   1 
ATOM   2590 O O   . GLN B 1 38  ? 15.880  -24.518 1.062   0.78   51.90  ? 38   GLN B O   1 
ATOM   2591 C CB  . GLN B 1 38  ? 16.817  -26.543 2.379   0.78   52.88  ? 38   GLN B CB  1 
ATOM   2592 C CG  . GLN B 1 38  ? 17.425  -27.580 3.347   0.78   54.19  ? 38   GLN B CG  1 
ATOM   2593 C CD  . GLN B 1 38  ? 18.284  -28.645 2.656   0.78   55.73  ? 38   GLN B CD  1 
ATOM   2594 O OE1 . GLN B 1 38  ? 19.510  -28.628 2.769   0.78   55.61  ? 38   GLN B OE1 1 
ATOM   2595 N NE2 . GLN B 1 38  ? 17.643  -29.563 1.931   0.78   56.30  ? 38   GLN B NE2 1 
ATOM   2596 N N   . GLU B 1 39  ? 17.965  -23.829 0.393   0.67   50.58  ? 39   GLU B N   1 
ATOM   2597 C CA  . GLU B 1 39  ? 17.533  -22.480 0.037   0.67   49.55  ? 39   GLU B CA  1 
ATOM   2598 C C   . GLU B 1 39  ? 17.453  -22.630 -1.468  0.67   49.17  ? 39   GLU B C   1 
ATOM   2599 O O   . GLU B 1 39  ? 18.297  -23.291 -2.081  0.67   48.51  ? 39   GLU B O   1 
ATOM   2600 C CB  . GLU B 1 39  ? 18.546  -21.383 0.354   0.67   49.44  ? 39   GLU B CB  1 
ATOM   2601 C CG  . GLU B 1 39  ? 18.797  -21.151 1.818   0.67   49.72  ? 39   GLU B CG  1 
ATOM   2602 C CD  . GLU B 1 39  ? 19.705  -19.963 2.088   0.67   49.90  ? 39   GLU B CD  1 
ATOM   2603 O OE1 . GLU B 1 39  ? 20.205  -19.339 1.121   0.67   49.46  ? 39   GLU B OE1 1 
ATOM   2604 O OE2 . GLU B 1 39  ? 19.911  -19.650 3.280   0.67   51.07  ? 39   GLU B OE2 1 
ATOM   2605 N N   . THR B 1 40  ? 16.434  -22.016 -2.057  1.00   48.57  ? 40   THR B N   1 
ATOM   2606 C CA  . THR B 1 40  ? 16.282  -22.052 -3.499  1.00   48.31  ? 40   THR B CA  1 
ATOM   2607 C C   . THR B 1 40  ? 16.893  -20.805 -4.114  1.00   47.83  ? 40   THR B C   1 
ATOM   2608 O O   . THR B 1 40  ? 16.553  -19.680 -3.743  1.00   47.51  ? 40   THR B O   1 
ATOM   2609 C CB  . THR B 1 40  ? 14.811  -22.214 -3.915  1.00   48.49  ? 40   THR B CB  1 
ATOM   2610 O OG1 . THR B 1 40  ? 14.255  -23.341 -3.230  1.00   49.48  ? 40   THR B OG1 1 
ATOM   2611 C CG2 . THR B 1 40  ? 14.702  -22.444 -5.418  1.00   48.23  ? 40   THR B CG2 1 
ATOM   2612 N N   . CYS B 1 41  ? 17.816  -21.020 -5.042  1.00   47.50  ? 41   CYS B N   1 
ATOM   2613 C CA  . CYS B 1 41  ? 18.437  -19.937 -5.774  1.00   47.29  ? 41   CYS B CA  1 
ATOM   2614 C C   . CYS B 1 41  ? 17.858  -19.934 -7.180  1.00   46.75  ? 41   CYS B C   1 
ATOM   2615 O O   . CYS B 1 41  ? 17.760  -20.983 -7.825  1.00   46.83  ? 41   CYS B O   1 
ATOM   2616 C CB  . CYS B 1 41  ? 19.954  -20.121 -5.815  1.00   47.55  ? 41   CYS B CB  1 
ATOM   2617 S SG  . CYS B 1 41  ? 20.880  -18.579 -5.953  1.00   84.93  ? 41   CYS B SG  1 
ATOM   2618 N N   . VAL B 1 42  ? 17.459  -18.753 -7.643  1.00   45.84  ? 42   VAL B N   1 
ATOM   2619 C CA  . VAL B 1 42  ? 16.839  -18.610 -8.951  1.00   44.99  ? 42   VAL B CA  1 
ATOM   2620 C C   . VAL B 1 42  ? 17.495  -17.475 -9.735  1.00   44.40  ? 42   VAL B C   1 
ATOM   2621 O O   . VAL B 1 42  ? 17.892  -16.459 -9.162  1.00   44.43  ? 42   VAL B O   1 
ATOM   2622 C CB  . VAL B 1 42  ? 15.297  -18.424 -8.822  1.00   45.01  ? 42   VAL B CB  1 
ATOM   2623 C CG1 . VAL B 1 42  ? 14.699  -17.803 -10.072 1.00   44.41  ? 42   VAL B CG1 1 
ATOM   2624 C CG2 . VAL B 1 42  ? 14.626  -19.770 -8.514  1.00   44.75  ? 42   VAL B CG2 1 
ATOM   2625 N N   . GLU B 1 43  ? 17.634  -17.676 -11.041 0.70   43.41  ? 43   GLU B N   1 
ATOM   2626 C CA  . GLU B 1 43  ? 18.146  -16.654 -11.935 0.70   42.65  ? 43   GLU B CA  1 
ATOM   2627 C C   . GLU B 1 43  ? 17.361  -16.728 -13.244 0.70   41.75  ? 43   GLU B C   1 
ATOM   2628 O O   . GLU B 1 43  ? 17.378  -17.760 -13.923 0.70   41.19  ? 43   GLU B O   1 
ATOM   2629 C CB  . GLU B 1 43  ? 19.641  -16.877 -12.178 0.70   42.99  ? 43   GLU B CB  1 
ATOM   2630 C CG  . GLU B 1 43  ? 20.328  -15.823 -13.054 0.70   44.26  ? 43   GLU B CG  1 
ATOM   2631 C CD  . GLU B 1 43  ? 21.835  -16.059 -13.175 0.70   46.69  ? 43   GLU B CD  1 
ATOM   2632 O OE1 . GLU B 1 43  ? 22.440  -15.572 -14.159 0.70   47.82  ? 43   GLU B OE1 1 
ATOM   2633 O OE2 . GLU B 1 43  ? 22.417  -16.731 -12.290 0.70   46.96  ? 43   GLU B OE2 1 
ATOM   2634 N N   . ILE B 1 44  ? 16.664  -15.637 -13.579 1.00   40.71  ? 44   ILE B N   1 
ATOM   2635 C CA  . ILE B 1 44  ? 15.905  -15.550 -14.825 1.00   39.39  ? 44   ILE B CA  1 
ATOM   2636 C C   . ILE B 1 44  ? 16.906  -15.358 -15.967 1.00   38.71  ? 44   ILE B C   1 
ATOM   2637 O O   . ILE B 1 44  ? 17.628  -14.361 -16.009 1.00   39.16  ? 44   ILE B O   1 
ATOM   2638 C CB  . ILE B 1 44  ? 14.848  -14.396 -14.799 1.00   39.39  ? 44   ILE B CB  1 
ATOM   2639 C CG1 . ILE B 1 44  ? 13.980  -14.446 -13.528 1.00   39.39  ? 44   ILE B CG1 1 
ATOM   2640 C CG2 . ILE B 1 44  ? 13.990  -14.398 -16.065 1.00   38.88  ? 44   ILE B CG2 1 
ATOM   2641 C CD1 . ILE B 1 44  ? 13.170  -15.749 -13.312 1.00   41.00  ? 44   ILE B CD1 1 
ATOM   2642 N N   . GLY B 1 45  ? 16.940  -16.319 -16.889 1.00   37.22  ? 45   GLY B N   1 
ATOM   2643 C CA  . GLY B 1 45  ? 17.983  -16.393 -17.902 1.00   35.49  ? 45   GLY B CA  1 
ATOM   2644 C C   . GLY B 1 45  ? 17.805  -15.484 -19.099 1.00   34.72  ? 45   GLY B C   1 
ATOM   2645 O O   . GLY B 1 45  ? 18.671  -15.426 -19.971 1.00   34.56  ? 45   GLY B O   1 
ATOM   2646 N N   . GLU B 1 46  ? 16.679  -14.779 -19.149 1.00   33.30  ? 46   GLU B N   1 
ATOM   2647 C CA  . GLU B 1 46  ? 16.412  -13.820 -20.202 1.00   32.49  ? 46   GLU B CA  1 
ATOM   2648 C C   . GLU B 1 46  ? 15.739  -12.586 -19.604 1.00   31.11  ? 46   GLU B C   1 
ATOM   2649 O O   . GLU B 1 46  ? 15.142  -12.651 -18.520 1.00   30.05  ? 46   GLU B O   1 
ATOM   2650 C CB  . GLU B 1 46  ? 15.512  -14.449 -21.280 1.00   33.13  ? 46   GLU B CB  1 
ATOM   2651 C CG  . GLU B 1 46  ? 14.333  -15.249 -20.696 1.00   36.41  ? 46   GLU B CG  1 
ATOM   2652 C CD  . GLU B 1 46  ? 13.689  -16.181 -21.714 1.00   40.47  ? 46   GLU B CD  1 
ATOM   2653 O OE1 . GLU B 1 46  ? 12.659  -15.780 -22.301 1.00   43.42  ? 46   GLU B OE1 1 
ATOM   2654 O OE2 . GLU B 1 46  ? 14.216  -17.303 -21.943 1.00   41.35  ? 46   GLU B OE2 1 
ATOM   2655 N N   . SER B 1 47  ? 15.834  -11.471 -20.325 1.00   29.05  ? 47   SER B N   1 
ATOM   2656 C CA  . SER B 1 47  ? 15.174  -10.236 -19.940 1.00   27.25  ? 47   SER B CA  1 
ATOM   2657 C C   . SER B 1 47  ? 13.655  -10.409 -19.944 1.00   26.53  ? 47   SER B C   1 
ATOM   2658 O O   . SER B 1 47  ? 13.091  -11.010 -20.858 1.00   26.00  ? 47   SER B O   1 
ATOM   2659 C CB  . SER B 1 47  ? 15.570  -9.107  -20.890 1.00   27.15  ? 47   SER B CB  1 
ATOM   2660 O OG  . SER B 1 47  ? 14.743  -7.968  -20.695 1.00   26.17  ? 47   SER B OG  1 
ATOM   2661 N N   . VAL B 1 48  ? 12.998  -9.889  -18.909 1.00   25.08  ? 48   VAL B N   1 
ATOM   2662 C CA  . VAL B 1 48  ? 11.540  -9.889  -18.877 1.00   24.02  ? 48   VAL B CA  1 
ATOM   2663 C C   . VAL B 1 48  ? 11.009  -8.458  -18.924 1.00   23.94  ? 48   VAL B C   1 
ATOM   2664 O O   . VAL B 1 48  ? 9.821   -8.225  -18.680 1.00   23.37  ? 48   VAL B O   1 
ATOM   2665 C CB  . VAL B 1 48  ? 10.981  -10.648 -17.643 1.00   23.92  ? 48   VAL B CB  1 
ATOM   2666 C CG1 . VAL B 1 48  ? 11.318  -12.140 -17.736 1.00   23.88  ? 48   VAL B CG1 1 
ATOM   2667 C CG2 . VAL B 1 48  ? 11.495  -10.027 -16.329 1.00   21.40  ? 48   VAL B CG2 1 
ATOM   2668 N N   . ARG B 1 49  ? 11.897  -7.514  -19.250 1.00   23.79  ? 49   ARG B N   1 
ATOM   2669 C CA  . ARG B 1 49  ? 11.596  -6.078  -19.183 1.00   24.15  ? 49   ARG B CA  1 
ATOM   2670 C C   . ARG B 1 49  ? 10.440  -5.727  -20.117 1.00   24.75  ? 49   ARG B C   1 
ATOM   2671 O O   . ARG B 1 49  ? 10.475  -6.033  -21.312 1.00   24.58  ? 49   ARG B O   1 
ATOM   2672 C CB  . ARG B 1 49  ? 12.859  -5.236  -19.472 1.00   23.97  ? 49   ARG B CB  1 
ATOM   2673 C CG  . ARG B 1 49  ? 12.737  -3.728  -19.201 1.00   24.00  ? 49   ARG B CG  1 
ATOM   2674 C CD  . ARG B 1 49  ? 14.085  -2.976  -19.351 1.00   23.28  ? 49   ARG B CD  1 
ATOM   2675 N NE  . ARG B 1 49  ? 15.109  -3.476  -18.422 1.00   22.40  ? 49   ARG B NE  1 
ATOM   2676 C CZ  . ARG B 1 49  ? 15.352  -2.989  -17.207 1.00   23.09  ? 49   ARG B CZ  1 
ATOM   2677 N NH1 . ARG B 1 49  ? 14.687  -1.931  -16.744 1.00   24.13  ? 49   ARG B NH1 1 
ATOM   2678 N NH2 . ARG B 1 49  ? 16.301  -3.537  -16.457 1.00   22.84  ? 49   ARG B NH2 1 
ATOM   2679 N N   . GLY B 1 50  ? 9.391   -5.143  -19.542 1.00   24.98  ? 50   GLY B N   1 
ATOM   2680 C CA  . GLY B 1 50  ? 8.204   -4.730  -20.299 1.00   24.70  ? 50   GLY B CA  1 
ATOM   2681 C C   . GLY B 1 50  ? 7.324   -5.874  -20.784 1.00   25.07  ? 50   GLY B C   1 
ATOM   2682 O O   . GLY B 1 50  ? 6.448   -5.668  -21.636 1.00   25.28  ? 50   GLY B O   1 
ATOM   2683 N N   . GLU B 1 51  ? 7.545   -7.080  -20.262 0.79   23.62  ? 51   GLU B N   1 
ATOM   2684 C CA  . GLU B 1 51  ? 6.842   -8.255  -20.764 0.79   22.71  ? 51   GLU B CA  1 
ATOM   2685 C C   . GLU B 1 51  ? 5.668   -8.667  -19.869 0.79   21.81  ? 51   GLU B C   1 
ATOM   2686 O O   . GLU B 1 51  ? 5.627   -8.313  -18.694 0.79   19.77  ? 51   GLU B O   1 
ATOM   2687 C CB  . GLU B 1 51  ? 7.813   -9.419  -20.886 0.79   23.47  ? 51   GLU B CB  1 
ATOM   2688 C CG  . GLU B 1 51  ? 9.047   -9.104  -21.699 0.79   25.87  ? 51   GLU B CG  1 
ATOM   2689 C CD  . GLU B 1 51  ? 8.938   -9.576  -23.103 0.79   31.40  ? 51   GLU B CD  1 
ATOM   2690 O OE1 . GLU B 1 51  ? 8.291   -8.866  -23.919 0.79   33.08  ? 51   GLU B OE1 1 
ATOM   2691 O OE2 . GLU B 1 51  ? 9.508   -10.657 -23.393 0.79   33.58  ? 51   GLU B OE2 1 
ATOM   2692 N N   . ASP B 1 52  ? 4.732   -9.424  -20.454 1.00   21.55  ? 52   ASP B N   1 
ATOM   2693 C CA  . ASP B 1 52  ? 3.602   -10.012 -19.742 1.00   22.52  ? 52   ASP B CA  1 
ATOM   2694 C C   . ASP B 1 52  ? 4.051   -11.404 -19.263 1.00   22.30  ? 52   ASP B C   1 
ATOM   2695 O O   . ASP B 1 52  ? 4.113   -12.349 -20.043 1.00   22.56  ? 52   ASP B O   1 
ATOM   2696 C CB  . ASP B 1 52  ? 2.364   -10.079 -20.670 1.00   22.19  ? 52   ASP B CB  1 
ATOM   2697 C CG  . ASP B 1 52  ? 1.053   -10.258 -19.914 1.00   24.76  ? 52   ASP B CG  1 
ATOM   2698 O OD1 . ASP B 1 52  ? 1.007   -10.005 -18.675 1.00   25.50  ? 52   ASP B OD1 1 
ATOM   2699 O OD2 . ASP B 1 52  ? 0.041   -10.657 -20.562 1.00   27.80  ? 52   ASP B OD2 1 
ATOM   2700 N N   . VAL B 1 53  ? 4.383   -11.523 -17.976 1.00   21.87  ? 53   VAL B N   1 
ATOM   2701 C CA  . VAL B 1 53  ? 4.994   -12.763 -17.457 1.00   21.36  ? 53   VAL B CA  1 
ATOM   2702 C C   . VAL B 1 53  ? 3.968   -13.675 -16.776 1.00   21.70  ? 53   VAL B C   1 
ATOM   2703 O O   . VAL B 1 53  ? 3.150   -13.205 -15.968 1.00   22.78  ? 53   VAL B O   1 
ATOM   2704 C CB  . VAL B 1 53  ? 6.174   -12.458 -16.487 1.00   20.98  ? 53   VAL B CB  1 
ATOM   2705 C CG1 . VAL B 1 53  ? 6.739   -13.746 -15.833 1.00   21.18  ? 53   VAL B CG1 1 
ATOM   2706 C CG2 . VAL B 1 53  ? 7.270   -11.690 -17.208 1.00   19.54  ? 53   VAL B CG2 1 
ATOM   2707 N N   . TYR B 1 54  ? 4.018   -14.967 -17.098 1.00   20.66  ? 54   TYR B N   1 
ATOM   2708 C CA  . TYR B 1 54  ? 3.182   -15.976 -16.460 1.00   21.18  ? 54   TYR B CA  1 
ATOM   2709 C C   . TYR B 1 54  ? 4.048   -17.025 -15.789 1.00   21.80  ? 54   TYR B C   1 
ATOM   2710 O O   . TYR B 1 54  ? 4.849   -17.694 -16.452 1.00   21.91  ? 54   TYR B O   1 
ATOM   2711 C CB  . TYR B 1 54  ? 2.215   -16.620 -17.485 1.00   21.17  ? 54   TYR B CB  1 
ATOM   2712 C CG  . TYR B 1 54  ? 1.214   -15.611 -17.995 1.00   20.28  ? 54   TYR B CG  1 
ATOM   2713 C CD1 . TYR B 1 54  ? 1.581   -14.679 -18.966 1.00   21.13  ? 54   TYR B CD1 1 
ATOM   2714 C CD2 . TYR B 1 54  ? -0.070  -15.535 -17.465 1.00   18.71  ? 54   TYR B CD2 1 
ATOM   2715 C CE1 . TYR B 1 54  ? 0.687   -13.716 -19.420 1.00   19.74  ? 54   TYR B CE1 1 
ATOM   2716 C CE2 . TYR B 1 54  ? -0.978  -14.566 -17.924 1.00   19.83  ? 54   TYR B CE2 1 
ATOM   2717 C CZ  . TYR B 1 54  ? -0.588  -13.666 -18.896 1.00   21.23  ? 54   TYR B CZ  1 
ATOM   2718 O OH  . TYR B 1 54  ? -1.476  -12.699 -19.364 1.00   23.30  ? 54   TYR B OH  1 
ATOM   2719 N N   . ILE B 1 55  ? 3.908   -17.165 -14.469 1.00   22.18  ? 55   ILE B N   1 
ATOM   2720 C CA  . ILE B 1 55  ? 4.686   -18.185 -13.747 1.00   22.02  ? 55   ILE B CA  1 
ATOM   2721 C C   . ILE B 1 55  ? 3.767   -19.304 -13.303 1.00   22.59  ? 55   ILE B C   1 
ATOM   2722 O O   . ILE B 1 55  ? 2.855   -19.079 -12.504 1.00   22.35  ? 55   ILE B O   1 
ATOM   2723 C CB  . ILE B 1 55  ? 5.465   -17.598 -12.529 1.00   22.19  ? 55   ILE B CB  1 
ATOM   2724 C CG1 . ILE B 1 55  ? 6.366   -16.447 -12.996 1.00   22.39  ? 55   ILE B CG1 1 
ATOM   2725 C CG2 . ILE B 1 55  ? 6.283   -18.723 -11.802 1.00   20.44  ? 55   ILE B CG2 1 
ATOM   2726 C CD1 . ILE B 1 55  ? 6.859   -15.564 -11.881 1.00   24.07  ? 55   ILE B CD1 1 
ATOM   2727 N N   . VAL B 1 56  ? 4.005   -20.501 -13.833 1.00   23.78  ? 56   VAL B N   1 
ATOM   2728 C CA  . VAL B 1 56  ? 3.157   -21.659 -13.558 1.00   26.00  ? 56   VAL B CA  1 
ATOM   2729 C C   . VAL B 1 56  ? 3.818   -22.448 -12.438 1.00   27.49  ? 56   VAL B C   1 
ATOM   2730 O O   . VAL B 1 56  ? 4.970   -22.879 -12.587 1.00   27.70  ? 56   VAL B O   1 
ATOM   2731 C CB  . VAL B 1 56  ? 2.975   -22.558 -14.810 1.00   26.26  ? 56   VAL B CB  1 
ATOM   2732 C CG1 . VAL B 1 56  ? 1.966   -23.678 -14.529 1.00   26.83  ? 56   VAL B CG1 1 
ATOM   2733 C CG2 . VAL B 1 56  ? 2.539   -21.726 -16.014 1.00   25.86  ? 56   VAL B CG2 1 
ATOM   2734 N N   . GLN B 1 57  ? 3.103   -22.619 -11.329 0.58   29.63  ? 57   GLN B N   1 
ATOM   2735 C CA  . GLN B 1 57  ? 3.671   -23.242 -10.128 0.58   32.63  ? 57   GLN B CA  1 
ATOM   2736 C C   . GLN B 1 57  ? 3.896   -24.738 -10.300 0.58   34.22  ? 57   GLN B C   1 
ATOM   2737 O O   . GLN B 1 57  ? 3.038   -25.460 -10.807 0.58   34.47  ? 57   GLN B O   1 
ATOM   2738 C CB  . GLN B 1 57  ? 2.828   -22.956 -8.877  0.58   32.47  ? 57   GLN B CB  1 
ATOM   2739 C CG  . GLN B 1 57  ? 1.678   -23.939 -8.610  0.58   34.54  ? 57   GLN B CG  1 
ATOM   2740 C CD  . GLN B 1 57  ? 1.502   -24.271 -7.126  0.58   36.36  ? 57   GLN B CD  1 
ATOM   2741 O OE1 . GLN B 1 57  ? 1.012   -25.342 -6.773  0.58   38.38  ? 57   GLN B OE1 1 
ATOM   2742 N NE2 . GLN B 1 57  ? 1.904   -23.351 -6.255  0.58   37.09  ? 57   GLN B NE2 1 
ATOM   2743 N N   . SER B 1 58  ? 5.062   -25.190 -9.847  1.00   36.83  ? 58   SER B N   1 
ATOM   2744 C CA  . SER B 1 58  ? 5.490   -26.576 -10.027 1.00   39.17  ? 58   SER B CA  1 
ATOM   2745 C C   . SER B 1 58  ? 4.550   -27.600 -9.390  1.00   39.89  ? 58   SER B C   1 
ATOM   2746 O O   . SER B 1 58  ? 3.849   -27.304 -8.409  1.00   40.84  ? 58   SER B O   1 
ATOM   2747 C CB  . SER B 1 58  ? 6.915   -26.760 -9.500  1.00   39.27  ? 58   SER B CB  1 
ATOM   2748 O OG  . SER B 1 58  ? 7.257   -28.135 -9.472  1.00   41.70  ? 58   SER B OG  1 
ATOM   2749 N N   . GLY B 1 59  ? 4.537   -28.800 -9.977  0.56   40.68  ? 59   GLY B N   1 
ATOM   2750 C CA  . GLY B 1 59  ? 3.734   -29.914 -9.480  0.56   41.36  ? 59   GLY B CA  1 
ATOM   2751 C C   . GLY B 1 59  ? 4.484   -30.779 -8.473  0.56   41.81  ? 59   GLY B C   1 
ATOM   2752 O O   . GLY B 1 59  ? 3.951   -31.785 -7.994  0.56   42.10  ? 59   GLY B O   1 
ATOM   2753 N N   . CYS B 1 60  ? 5.722   -30.388 -8.147  0.58   42.22  ? 60   CYS B N   1 
ATOM   2754 C CA  . CYS B 1 60  ? 6.485   -31.033 -7.071  0.58   42.34  ? 60   CYS B CA  1 
ATOM   2755 C C   . CYS B 1 60  ? 5.624   -31.096 -5.809  0.58   42.18  ? 60   CYS B C   1 
ATOM   2756 O O   . CYS B 1 60  ? 4.831   -30.161 -5.526  0.58   42.52  ? 60   CYS B O   1 
ATOM   2757 C CB  . CYS B 1 60  ? 7.772   -30.253 -6.793  0.58   42.47  ? 60   CYS B CB  1 
ATOM   2758 S SG  . CYS B 1 60  ? 8.893   -31.048 -5.624  0.58   58.89  ? 60   CYS B SG  1 
ATOM   2759 N N   . GLY B 1 61  ? 5.669   -32.217 -5.045  1.00   41.86  ? 61   GLY B N   1 
ATOM   2760 C CA  . GLY B 1 61  ? 4.835   -32.419 -3.817  1.00   40.61  ? 61   GLY B CA  1 
ATOM   2761 C C   . GLY B 1 61  ? 5.098   -31.542 -2.608  1.00   39.64  ? 61   GLY B C   1 
ATOM   2762 O O   . GLY B 1 61  ? 4.174   -31.275 -1.828  1.00   40.24  ? 61   GLY B O   1 
ATOM   2763 N N   . GLU B 1 62  ? 6.346   -31.096 -2.445  0.78   37.83  ? 62   GLU B N   1 
ATOM   2764 C CA  . GLU B 1 62  ? 6.731   -30.330 -1.261  0.78   35.78  ? 62   GLU B CA  1 
ATOM   2765 C C   . GLU B 1 62  ? 6.184   -28.909 -1.330  0.78   34.51  ? 62   GLU B C   1 
ATOM   2766 O O   . GLU B 1 62  ? 6.769   -28.026 -1.956  0.78   33.64  ? 62   GLU B O   1 
ATOM   2767 C CB  . GLU B 1 62  ? 8.248   -30.330 -1.067  0.78   35.64  ? 62   GLU B CB  1 
ATOM   2768 C CG  . GLU B 1 62  ? 8.684   -30.578 0.371   0.78   34.96  ? 62   GLU B CG  1 
ATOM   2769 C CD  . GLU B 1 62  ? 8.616   -29.347 1.294   0.78   34.61  ? 62   GLU B CD  1 
ATOM   2770 O OE1 . GLU B 1 62  ? 7.898   -28.356 1.014   0.78   31.74  ? 62   GLU B OE1 1 
ATOM   2771 O OE2 . GLU B 1 62  ? 9.297   -29.386 2.334   0.78   35.09  ? 62   GLU B OE2 1 
ATOM   2772 N N   . ILE B 1 63  ? 5.054   -28.706 -0.656  1.00   33.41  ? 63   ILE B N   1 
ATOM   2773 C CA  . ILE B 1 63  ? 4.292   -27.468 -0.767  1.00   32.28  ? 63   ILE B CA  1 
ATOM   2774 C C   . ILE B 1 63  ? 5.074   -26.194 -0.378  1.00   31.36  ? 63   ILE B C   1 
ATOM   2775 O O   . ILE B 1 63  ? 4.966   -25.167 -1.053  1.00   30.66  ? 63   ILE B O   1 
ATOM   2776 C CB  . ILE B 1 63  ? 2.941   -27.581 -0.013  1.00   32.54  ? 63   ILE B CB  1 
ATOM   2777 C CG1 . ILE B 1 63  ? 2.025   -26.418 -0.379  1.00   32.89  ? 63   ILE B CG1 1 
ATOM   2778 C CG2 . ILE B 1 63  ? 3.152   -27.724 1.512   1.00   32.81  ? 63   ILE B CG2 1 
ATOM   2779 C CD1 . ILE B 1 63  ? 0.738   -26.388 0.420   1.00   35.05  ? 63   ILE B CD1 1 
ATOM   2780 N N   . ASN B 1 64  ? 5.870   -26.256 0.684   1.00   29.83  ? 64   ASN B N   1 
ATOM   2781 C CA  . ASN B 1 64  ? 6.603   -25.063 1.113   1.00   29.01  ? 64   ASN B CA  1 
ATOM   2782 C C   . ASN B 1 64  ? 7.745   -24.693 0.161   1.00   28.52  ? 64   ASN B C   1 
ATOM   2783 O O   . ASN B 1 64  ? 7.987   -23.503 -0.092  1.00   27.70  ? 64   ASN B O   1 
ATOM   2784 C CB  . ASN B 1 64  ? 7.087   -25.184 2.566   1.00   28.76  ? 64   ASN B CB  1 
ATOM   2785 C CG  . ASN B 1 64  ? 5.955   -25.505 3.547   1.00   28.45  ? 64   ASN B CG  1 
ATOM   2786 O OD1 . ASN B 1 64  ? 6.103   -26.387 4.398   1.00   32.89  ? 64   ASN B OD1 1 
ATOM   2787 N ND2 . ASN B 1 64  ? 4.826   -24.800 3.435   1.00   24.60  ? 64   ASN B ND2 1 
ATOM   2788 N N   . ASP B 1 65  ? 8.435   -25.703 -0.372  1.00   27.83  ? 65   ASP B N   1 
ATOM   2789 C CA  . ASP B 1 65  ? 9.470   -25.474 -1.389  1.00   28.38  ? 65   ASP B CA  1 
ATOM   2790 C C   . ASP B 1 65  ? 8.893   -24.854 -2.660  1.00   27.58  ? 65   ASP B C   1 
ATOM   2791 O O   . ASP B 1 65  ? 9.493   -23.952 -3.236  1.00   27.12  ? 65   ASP B O   1 
ATOM   2792 C CB  . ASP B 1 65  ? 10.185  -26.775 -1.780  1.00   28.34  ? 65   ASP B CB  1 
ATOM   2793 C CG  . ASP B 1 65  ? 11.027  -27.344 -0.658  1.00   30.10  ? 65   ASP B CG  1 
ATOM   2794 O OD1 . ASP B 1 65  ? 11.408  -26.589 0.276   1.00   30.45  ? 65   ASP B OD1 1 
ATOM   2795 O OD2 . ASP B 1 65  ? 11.326  -28.556 -0.727  1.00   29.69  ? 65   ASP B OD2 1 
ATOM   2796 N N   . ASN B 1 66  ? 7.758   -25.372 -3.087  1.00   27.26  ? 66   ASN B N   1 
ATOM   2797 C CA  . ASN B 1 66  ? 7.055   -24.938 -4.263  1.00   27.41  ? 66   ASN B CA  1 
ATOM   2798 C C   . ASN B 1 66  ? 6.561   -23.521 -4.103  1.00   25.75  ? 66   ASN B C   1 
ATOM   2799 O O   . ASN B 1 66  ? 6.721   -22.745 -4.957  1.00   24.82  ? 66   ASN B O   1 
ATOM   2800 C CB  . ASN B 1 66  ? 5.881   -25.841 -4.635  1.00   27.84  ? 66   ASN B CB  1 
ATOM   2801 C CG  . ASN B 1 66  ? 6.303   -27.222 -5.100  1.00   31.70  ? 66   ASN B CG  1 
ATOM   2802 O OD1 . ASN B 1 66  ? 7.353   -27.418 -5.639  1.00   34.57  ? 66   ASN B OD1 1 
ATOM   2803 N ND2 . ASN B 1 66  ? 5.467   -28.171 -4.866  1.00   32.92  ? 66   ASN B ND2 1 
ATOM   2804 N N   . LEU B 1 67  ? 5.955   -23.231 -2.982  1.00   24.33  ? 67   LEU B N   1 
ATOM   2805 C CA  . LEU B 1 67  ? 5.472   -21.892 -2.699  1.00   23.13  ? 67   LEU B CA  1 
ATOM   2806 C C   . LEU B 1 67  ? 6.621   -20.886 -2.688  1.00   21.75  ? 67   LEU B C   1 
ATOM   2807 O O   . LEU B 1 67  ? 6.520   -19.835 -3.313  1.00   20.89  ? 67   LEU B O   1 
ATOM   2808 C CB  . LEU B 1 67  ? 4.690   -21.841 -1.383  1.00   23.51  ? 67   LEU B CB  1 
ATOM   2809 C CG  . LEU B 1 67  ? 4.193   -20.451 -0.960  1.00   23.52  ? 67   LEU B CG  1 
ATOM   2810 C CD1 . LEU B 1 67  ? 3.298   -19.811 -2.036  1.00   23.69  ? 67   LEU B CD1 1 
ATOM   2811 C CD2 . LEU B 1 67  ? 3.464   -20.516 0.367   1.00   26.55  ? 67   LEU B CD2 1 
ATOM   2812 N N   . MET B 1 68  ? 7.704   -21.204 -1.981  0.67   20.76  ? 68   MET B N   1 
ATOM   2813 C CA  . MET B 1 68  ? 8.808   -20.261 -1.847  0.67   20.36  ? 68   MET B CA  1 
ATOM   2814 C C   . MET B 1 68  ? 9.437   -19.965 -3.207  0.67   20.08  ? 68   MET B C   1 
ATOM   2815 O O   . MET B 1 68  ? 9.680   -18.812 -3.528  0.67   18.75  ? 68   MET B O   1 
ATOM   2816 C CB  . MET B 1 68  ? 9.865   -20.758 -0.849  0.67   20.01  ? 68   MET B CB  1 
ATOM   2817 C CG  . MET B 1 68  ? 9.489   -20.556 0.635   0.67   21.89  ? 68   MET B CG  1 
ATOM   2818 S SD  . MET B 1 68  ? 8.966   -18.882 1.098   0.67   24.22  ? 68   MET B SD  1 
ATOM   2819 C CE  . MET B 1 68  ? 10.268  -17.910 0.342   0.67   20.62  ? 68   MET B CE  1 
ATOM   2820 N N   . GLU B 1 69  ? 9.681   -21.020 -3.989  1.00   20.99  ? 69   GLU B N   1 
ATOM   2821 C CA  . GLU B 1 69  ? 10.186  -20.915 -5.374  1.00   22.58  ? 69   GLU B CA  1 
ATOM   2822 C C   . GLU B 1 69  ? 9.321   -19.976 -6.218  1.00   21.81  ? 69   GLU B C   1 
ATOM   2823 O O   . GLU B 1 69  ? 9.835   -19.110 -6.946  1.00   22.78  ? 69   GLU B O   1 
ATOM   2824 C CB  . GLU B 1 69  ? 10.232  -22.317 -6.021  1.00   23.02  ? 69   GLU B CB  1 
ATOM   2825 C CG  . GLU B 1 69  ? 10.859  -22.384 -7.418  1.00   29.06  ? 69   GLU B CG  1 
ATOM   2826 C CD  . GLU B 1 69  ? 11.104  -23.823 -7.880  1.00   36.21  ? 69   GLU B CD  1 
ATOM   2827 O OE1 . GLU B 1 69  ? 10.126  -24.616 -7.927  1.00   39.05  ? 69   GLU B OE1 1 
ATOM   2828 O OE2 . GLU B 1 69  ? 12.272  -24.161 -8.198  1.00   39.55  ? 69   GLU B OE2 1 
ATOM   2829 N N   . LEU B 1 70  ? 8.008   -20.157 -6.129  1.00   20.94  ? 70   LEU B N   1 
ATOM   2830 C CA  . LEU B 1 70  ? 7.059   -19.306 -6.843  1.00   19.94  ? 70   LEU B CA  1 
ATOM   2831 C C   . LEU B 1 70  ? 7.174   -17.842 -6.420  1.00   19.54  ? 70   LEU B C   1 
ATOM   2832 O O   . LEU B 1 70  ? 7.259   -16.960 -7.262  1.00   18.88  ? 70   LEU B O   1 
ATOM   2833 C CB  . LEU B 1 70  ? 5.622   -19.806 -6.620  1.00   19.41  ? 70   LEU B CB  1 
ATOM   2834 C CG  . LEU B 1 70  ? 4.468   -18.956 -7.162  1.00   19.50  ? 70   LEU B CG  1 
ATOM   2835 C CD1 . LEU B 1 70  ? 4.565   -18.747 -8.700  1.00   18.77  ? 70   LEU B CD1 1 
ATOM   2836 C CD2 . LEU B 1 70  ? 3.147   -19.601 -6.794  1.00   18.69  ? 70   LEU B CD2 1 
ATOM   2837 N N   . LEU B 1 71  ? 7.173   -17.597 -5.106  1.00   19.30  ? 71   LEU B N   1 
ATOM   2838 C CA  . LEU B 1 71  ? 7.332   -16.245 -4.577  1.00   19.34  ? 71   LEU B CA  1 
ATOM   2839 C C   . LEU B 1 71  ? 8.625   -15.609 -5.069  1.00   19.49  ? 71   LEU B C   1 
ATOM   2840 O O   . LEU B 1 71  ? 8.647   -14.430 -5.437  1.00   18.81  ? 71   LEU B O   1 
ATOM   2841 C CB  . LEU B 1 71  ? 7.289   -16.236 -3.042  1.00   18.86  ? 71   LEU B CB  1 
ATOM   2842 C CG  . LEU B 1 71  ? 5.948   -16.662 -2.429  1.00   19.78  ? 71   LEU B CG  1 
ATOM   2843 C CD1 . LEU B 1 71  ? 6.051   -16.871 -0.928  1.00   23.12  ? 71   LEU B CD1 1 
ATOM   2844 C CD2 . LEU B 1 71  ? 4.841   -15.664 -2.741  1.00   16.86  ? 71   LEU B CD2 1 
ATOM   2845 N N   . ILE B 1 72  ? 9.694   -16.399 -5.071  1.00   20.44  ? 72   ILE B N   1 
ATOM   2846 C CA  . ILE B 1 72  ? 11.029  -15.910 -5.427  1.00   21.28  ? 72   ILE B CA  1 
ATOM   2847 C C   . ILE B 1 72  ? 11.055  -15.495 -6.907  1.00   21.41  ? 72   ILE B C   1 
ATOM   2848 O O   . ILE B 1 72  ? 11.564  -14.423 -7.256  1.00   20.94  ? 72   ILE B O   1 
ATOM   2849 C CB  . ILE B 1 72  ? 12.116  -16.976 -5.080  1.00   21.82  ? 72   ILE B CB  1 
ATOM   2850 C CG1 . ILE B 1 72  ? 12.331  -17.034 -3.559  1.00   23.59  ? 72   ILE B CG1 1 
ATOM   2851 C CG2 . ILE B 1 72  ? 13.441  -16.684 -5.792  1.00   21.77  ? 72   ILE B CG2 1 
ATOM   2852 C CD1 . ILE B 1 72  ? 13.013  -18.347 -3.084  1.00   25.44  ? 72   ILE B CD1 1 
ATOM   2853 N N   . MET B 1 73  ? 10.447  -16.325 -7.754  1.00   22.14  ? 73   MET B N   1 
ATOM   2854 C CA  . MET B 1 73  ? 10.353  -16.064 -9.201  1.00   22.42  ? 73   MET B CA  1 
ATOM   2855 C C   . MET B 1 73  ? 9.486   -14.849 -9.526  1.00   21.85  ? 73   MET B C   1 
ATOM   2856 O O   . MET B 1 73  ? 9.828   -14.049 -10.396 1.00   21.52  ? 73   MET B O   1 
ATOM   2857 C CB  . MET B 1 73  ? 9.823   -17.301 -9.918  1.00   23.21  ? 73   MET B CB  1 
ATOM   2858 C CG  . MET B 1 73  ? 10.854  -18.434 -10.027 1.00   27.02  ? 73   MET B CG  1 
ATOM   2859 S SD  . MET B 1 73  ? 10.191  -19.897 -10.879 1.00   34.70  ? 73   MET B SD  1 
ATOM   2860 C CE  . MET B 1 73  ? 10.227  -19.308 -12.570 1.00   30.16  ? 73   MET B CE  1 
ATOM   2861 N N   . ILE B 1 74  ? 8.367   -14.715 -8.816  1.00   21.85  ? 74   ILE B N   1 
ATOM   2862 C CA  . ILE B 1 74  ? 7.536   -13.515 -8.899  1.00   21.56  ? 74   ILE B CA  1 
ATOM   2863 C C   . ILE B 1 74  ? 8.386   -12.280 -8.561  1.00   21.84  ? 74   ILE B C   1 
ATOM   2864 O O   . ILE B 1 74  ? 8.402   -11.303 -9.312  1.00   20.39  ? 74   ILE B O   1 
ATOM   2865 C CB  . ILE B 1 74  ? 6.278   -13.627 -7.988  1.00   21.73  ? 74   ILE B CB  1 
ATOM   2866 C CG1 . ILE B 1 74  ? 5.258   -14.605 -8.599  1.00   21.97  ? 74   ILE B CG1 1 
ATOM   2867 C CG2 . ILE B 1 74  ? 5.617   -12.262 -7.770  1.00   21.47  ? 74   ILE B CG2 1 
ATOM   2868 C CD1 . ILE B 1 74  ? 4.193   -15.110 -7.592  1.00   23.51  ? 74   ILE B CD1 1 
ATOM   2869 N N   . ASN B 1 75  ? 9.108   -12.346 -7.442  1.00   22.74  ? 75   ASN B N   1 
ATOM   2870 C CA  . ASN B 1 75  ? 9.931   -11.226 -7.015  1.00   24.09  ? 75   ASN B CA  1 
ATOM   2871 C C   . ASN B 1 75  ? 10.981  -10.872 -8.061  1.00   23.56  ? 75   ASN B C   1 
ATOM   2872 O O   . ASN B 1 75  ? 11.145  -9.707  -8.424  1.00   23.96  ? 75   ASN B O   1 
ATOM   2873 C CB  . ASN B 1 75  ? 10.632  -11.538 -5.704  1.00   24.93  ? 75   ASN B CB  1 
ATOM   2874 C CG  . ASN B 1 75  ? 11.404  -10.354 -5.191  1.00   27.37  ? 75   ASN B CG  1 
ATOM   2875 O OD1 . ASN B 1 75  ? 10.813  -9.340  -4.821  1.00   30.92  ? 75   ASN B OD1 1 
ATOM   2876 N ND2 . ASN B 1 75  ? 12.732  -10.462 -5.194  1.00   28.16  ? 75   ASN B ND2 1 
ATOM   2877 N N   . ALA B 1 76  ? 11.681  -11.899 -8.544  1.00   23.19  ? 76   ALA B N   1 
ATOM   2878 C CA  . ALA B 1 76  ? 12.746  -11.726 -9.520  1.00   22.78  ? 76   ALA B CA  1 
ATOM   2879 C C   . ALA B 1 76  ? 12.202  -11.031 -10.778 1.00   22.56  ? 76   ALA B C   1 
ATOM   2880 O O   . ALA B 1 76  ? 12.787  -10.068 -11.264 1.00   22.22  ? 76   ALA B O   1 
ATOM   2881 C CB  . ALA B 1 76  ? 13.359  -13.078 -9.856  1.00   22.68  ? 76   ALA B CB  1 
ATOM   2882 N N   . CYS B 1 77  ? 11.040  -11.468 -11.246 1.00   22.08  ? 77   CYS B N   1 
ATOM   2883 C CA  . CYS B 1 77  ? 10.445  -10.874 -12.439 1.00   23.30  ? 77   CYS B CA  1 
ATOM   2884 C C   . CYS B 1 77  ? 9.991   -9.428  -12.214 1.00   22.66  ? 77   CYS B C   1 
ATOM   2885 O O   . CYS B 1 77  ? 10.213  -8.573  -13.074 1.00   22.23  ? 77   CYS B O   1 
ATOM   2886 C CB  . CYS B 1 77  ? 9.293   -11.729 -12.946 1.00   23.39  ? 77   CYS B CB  1 
ATOM   2887 S SG  . CYS B 1 77  ? 9.849   -13.292 -13.634 1.00   27.09  ? 77   CYS B SG  1 
ATOM   2888 N N   . LYS B 1 78  ? 9.389   -9.166  -11.057 0.88   22.24  ? 78   LYS B N   1 
ATOM   2889 C CA  . LYS B 1 78  ? 8.965   -7.817  -10.696 0.88   23.63  ? 78   LYS B CA  1 
ATOM   2890 C C   . LYS B 1 78  ? 10.118  -6.804  -10.650 0.88   23.49  ? 78   LYS B C   1 
ATOM   2891 O O   . LYS B 1 78  ? 10.015  -5.717  -11.215 0.88   23.04  ? 78   LYS B O   1 
ATOM   2892 C CB  . LYS B 1 78  ? 8.195   -7.816  -9.369  0.88   23.83  ? 78   LYS B CB  1 
ATOM   2893 C CG  . LYS B 1 78  ? 6.692   -7.909  -9.532  0.88   27.94  ? 78   LYS B CG  1 
ATOM   2894 C CD  . LYS B 1 78  ? 6.133   -6.625  -10.168 0.88   31.84  ? 78   LYS B CD  1 
ATOM   2895 C CE  . LYS B 1 78  ? 4.735   -6.831  -10.688 0.88   34.53  ? 78   LYS B CE  1 
ATOM   2896 N NZ  . LYS B 1 78  ? 4.396   -5.927  -11.839 0.88   37.44  ? 78   LYS B NZ  1 
ATOM   2897 N N   . ILE B 1 79  ? 11.210  -7.164  -9.982  1.00   24.57  ? 79   ILE B N   1 
ATOM   2898 C CA  . ILE B 1 79  ? 12.337  -6.243  -9.825  1.00   24.58  ? 79   ILE B CA  1 
ATOM   2899 C C   . ILE B 1 79  ? 13.180  -6.169  -11.109 1.00   25.07  ? 79   ILE B C   1 
ATOM   2900 O O   . ILE B 1 79  ? 14.005  -5.266  -11.266 1.00   24.97  ? 79   ILE B O   1 
ATOM   2901 C CB  . ILE B 1 79  ? 13.213  -6.553  -8.564  1.00   24.99  ? 79   ILE B CB  1 
ATOM   2902 C CG1 . ILE B 1 79  ? 13.973  -7.883  -8.713  1.00   25.66  ? 79   ILE B CG1 1 
ATOM   2903 C CG2 . ILE B 1 79  ? 12.352  -6.497  -7.243  1.00   25.48  ? 79   ILE B CG2 1 
ATOM   2904 C CD1 . ILE B 1 79  ? 14.911  -8.206  -7.533  1.00   27.09  ? 79   ILE B CD1 1 
ATOM   2905 N N   . ALA B 1 80  ? 12.965  -7.128  -12.008 1.00   24.89  ? 80   ALA B N   1 
ATOM   2906 C CA  . ALA B 1 80  ? 13.518  -7.066  -13.361 1.00   24.93  ? 80   ALA B CA  1 
ATOM   2907 C C   . ALA B 1 80  ? 12.590  -6.324  -14.354 1.00   24.99  ? 80   ALA B C   1 
ATOM   2908 O O   . ALA B 1 80  ? 12.785  -6.404  -15.576 1.00   25.01  ? 80   ALA B O   1 
ATOM   2909 C CB  . ALA B 1 80  ? 13.892  -8.471  -13.869 1.00   24.09  ? 80   ALA B CB  1 
ATOM   2910 N N   . SER B 1 81  ? 11.616  -5.581  -13.816 1.00   24.65  ? 81   SER B N   1 
ATOM   2911 C CA  . SER B 1 81  ? 10.748  -4.672  -14.596 1.00   25.01  ? 81   SER B CA  1 
ATOM   2912 C C   . SER B 1 81  ? 9.806   -5.328  -15.619 1.00   25.32  ? 81   SER B C   1 
ATOM   2913 O O   . SER B 1 81  ? 9.504   -4.738  -16.673 1.00   24.68  ? 81   SER B O   1 
ATOM   2914 C CB  . SER B 1 81  ? 11.559  -3.567  -15.290 1.00   24.97  ? 81   SER B CB  1 
ATOM   2915 O OG  . SER B 1 81  ? 12.184  -2.717  -14.350 1.00   26.12  ? 81   SER B OG  1 
ATOM   2916 N N   . ALA B 1 82  ? 9.350   -6.539  -15.321 1.00   24.92  ? 82   ALA B N   1 
ATOM   2917 C CA  . ALA B 1 82  ? 8.215   -7.101  -16.042 1.00   25.48  ? 82   ALA B CA  1 
ATOM   2918 C C   . ALA B 1 82  ? 7.046   -6.105  -16.040 1.00   26.11  ? 82   ALA B C   1 
ATOM   2919 O O   . ALA B 1 82  ? 6.830   -5.393  -15.064 1.00   26.35  ? 82   ALA B O   1 
ATOM   2920 C CB  . ALA B 1 82  ? 7.788   -8.434  -15.412 1.00   24.89  ? 82   ALA B CB  1 
ATOM   2921 N N   . SER B 1 83  ? 6.312   -6.035  -17.143 1.00   26.68  ? 83   SER B N   1 
ATOM   2922 C CA  . SER B 1 83  ? 5.145   -5.167  -17.214 1.00   28.24  ? 83   SER B CA  1 
ATOM   2923 C C   . SER B 1 83  ? 4.030   -5.667  -16.272 1.00   28.24  ? 83   SER B C   1 
ATOM   2924 O O   . SER B 1 83  ? 3.386   -4.870  -15.568 1.00   28.36  ? 83   SER B O   1 
ATOM   2925 C CB  . SER B 1 83  ? 4.639   -5.103  -18.652 1.00   28.59  ? 83   SER B CB  1 
ATOM   2926 O OG  . SER B 1 83  ? 3.501   -4.275  -18.756 1.00   32.81  ? 83   SER B OG  1 
ATOM   2927 N N   . ARG B 1 84  ? 3.802   -6.983  -16.291 1.00   26.79  ? 84   ARG B N   1 
ATOM   2928 C CA  . ARG B 1 84  ? 2.815   -7.632  -15.425 1.00   25.90  ? 84   ARG B CA  1 
ATOM   2929 C C   . ARG B 1 84  ? 3.330   -9.020  -15.068 1.00   24.05  ? 84   ARG B C   1 
ATOM   2930 O O   . ARG B 1 84  ? 4.042   -9.631  -15.870 1.00   22.77  ? 84   ARG B O   1 
ATOM   2931 C CB  . ARG B 1 84  ? 1.459   -7.725  -16.133 1.00   26.00  ? 84   ARG B CB  1 
ATOM   2932 C CG  . ARG B 1 84  ? 0.331   -8.345  -15.280 1.00   28.48  ? 84   ARG B CG  1 
ATOM   2933 C CD  . ARG B 1 84  ? -1.051  -8.092  -15.910 1.00   33.24  ? 84   ARG B CD  1 
ATOM   2934 N NE  . ARG B 1 84  ? -1.149  -8.687  -17.246 1.00   34.11  ? 84   ARG B NE  1 
ATOM   2935 C CZ  . ARG B 1 84  ? -2.241  -8.678  -18.008 1.00   37.34  ? 84   ARG B CZ  1 
ATOM   2936 N NH1 . ARG B 1 84  ? -3.373  -8.111  -17.585 1.00   39.96  ? 84   ARG B NH1 1 
ATOM   2937 N NH2 . ARG B 1 84  ? -2.207  -9.249  -19.195 1.00   35.60  ? 84   ARG B NH2 1 
ATOM   2938 N N   . VAL B 1 85  ? 3.016   -9.484  -13.855 1.00   22.50  ? 85   VAL B N   1 
ATOM   2939 C CA  . VAL B 1 85  ? 3.354   -10.847 -13.436 1.00   21.87  ? 85   VAL B CA  1 
ATOM   2940 C C   . VAL B 1 85  ? 2.100   -11.547 -12.930 1.00   21.36  ? 85   VAL B C   1 
ATOM   2941 O O   . VAL B 1 85  ? 1.416   -11.064 -12.030 1.00   20.75  ? 85   VAL B O   1 
ATOM   2942 C CB  . VAL B 1 85  ? 4.454   -10.925 -12.336 1.00   22.65  ? 85   VAL B CB  1 
ATOM   2943 C CG1 . VAL B 1 85  ? 4.813   -12.392 -12.045 1.00   22.97  ? 85   VAL B CG1 1 
ATOM   2944 C CG2 . VAL B 1 85  ? 5.713   -10.164 -12.734 1.00   21.46  ? 85   VAL B CG2 1 
ATOM   2945 N N   . THR B 1 86  ? 1.805   -12.692 -13.527 1.00   20.23  ? 86   THR B N   1 
ATOM   2946 C CA  . THR B 1 86  ? 0.623   -13.439 -13.189 1.00   19.76  ? 86   THR B CA  1 
ATOM   2947 C C   . THR B 1 86  ? 1.082   -14.749 -12.608 1.00   19.78  ? 86   THR B C   1 
ATOM   2948 O O   . THR B 1 86  ? 1.949   -15.402 -13.184 1.00   19.50  ? 86   THR B O   1 
ATOM   2949 C CB  . THR B 1 86  ? -0.249  -13.642 -14.453 1.00   19.53  ? 86   THR B CB  1 
ATOM   2950 O OG1 . THR B 1 86  ? -0.762  -12.366 -14.851 1.00   20.56  ? 86   THR B OG1 1 
ATOM   2951 C CG2 . THR B 1 86  ? -1.411  -14.589 -14.179 1.00   19.38  ? 86   THR B CG2 1 
ATOM   2952 N N   . ALA B 1 87  ? 0.558   -15.107 -11.434 1.00   19.95  ? 87   ALA B N   1 
ATOM   2953 C CA  . ALA B 1 87  ? 0.810   -16.424 -10.903 1.00   19.93  ? 87   ALA B CA  1 
ATOM   2954 C C   . ALA B 1 87  ? -0.266  -17.369 -11.404 1.00   20.71  ? 87   ALA B C   1 
ATOM   2955 O O   . ALA B 1 87  ? -1.467  -17.125 -11.216 1.00   20.78  ? 87   ALA B O   1 
ATOM   2956 C CB  . ALA B 1 87  ? 0.865   -16.414 -9.379  1.00   20.37  ? 87   ALA B CB  1 
ATOM   2957 N N   . VAL B 1 88  ? 0.167   -18.442 -12.056 1.00   20.20  ? 88   VAL B N   1 
ATOM   2958 C CA  . VAL B 1 88  ? -0.733  -19.503 -12.482 1.00   20.18  ? 88   VAL B CA  1 
ATOM   2959 C C   . VAL B 1 88  ? -0.572  -20.674 -11.517 1.00   20.78  ? 88   VAL B C   1 
ATOM   2960 O O   . VAL B 1 88  ? 0.439   -21.386 -11.542 1.00   19.72  ? 88   VAL B O   1 
ATOM   2961 C CB  . VAL B 1 88  ? -0.427  -19.969 -13.937 1.00   19.83  ? 88   VAL B CB  1 
ATOM   2962 C CG1 . VAL B 1 88  ? -1.417  -21.046 -14.377 1.00   19.15  ? 88   VAL B CG1 1 
ATOM   2963 C CG2 . VAL B 1 88  ? -0.467  -18.771 -14.913 1.00   20.12  ? 88   VAL B CG2 1 
ATOM   2964 N N   . ILE B 1 89  ? -1.570  -20.846 -10.658 1.00   21.12  ? 89   ILE B N   1 
ATOM   2965 C CA  . ILE B 1 89  ? -1.473  -21.755 -9.549  1.00   22.87  ? 89   ILE B CA  1 
ATOM   2966 C C   . ILE B 1 89  ? -2.633  -22.731 -9.654  1.00   23.69  ? 89   ILE B C   1 
ATOM   2967 O O   . ILE B 1 89  ? -3.680  -22.501 -9.070  1.00   23.99  ? 89   ILE B O   1 
ATOM   2968 C CB  . ILE B 1 89  ? -1.558  -21.017 -8.178  1.00   23.87  ? 89   ILE B CB  1 
ATOM   2969 C CG1 . ILE B 1 89  ? -0.666  -19.782 -8.143  1.00   22.85  ? 89   ILE B CG1 1 
ATOM   2970 C CG2 . ILE B 1 89  ? -1.167  -21.960 -7.048  1.00   23.79  ? 89   ILE B CG2 1 
ATOM   2971 C CD1 . ILE B 1 89  ? -0.855  -18.908 -6.893  1.00   25.31  ? 89   ILE B CD1 1 
ATOM   2972 N N   . PRO B 1 90  ? -2.452  -23.824 -10.412 1.00   24.66  ? 90   PRO B N   1 
ATOM   2973 C CA  . PRO B 1 90  ? -3.565  -24.740 -10.653 1.00   25.77  ? 90   PRO B CA  1 
ATOM   2974 C C   . PRO B 1 90  ? -4.189  -25.220 -9.335  1.00   26.40  ? 90   PRO B C   1 
ATOM   2975 O O   . PRO B 1 90  ? -5.418  -25.237 -9.207  1.00   26.45  ? 90   PRO B O   1 
ATOM   2976 C CB  . PRO B 1 90  ? -2.914  -25.890 -11.436 1.00   25.70  ? 90   PRO B CB  1 
ATOM   2977 C CG  . PRO B 1 90  ? -1.716  -25.270 -12.089 1.00   26.26  ? 90   PRO B CG  1 
ATOM   2978 C CD  . PRO B 1 90  ? -1.207  -24.299 -11.032 1.00   24.72  ? 90   PRO B CD  1 
ATOM   2979 N N   . CYS B 1 91  ? -3.359  -25.571 -8.358  1.00   26.91  ? 91   CYS B N   1 
ATOM   2980 C CA  . CYS B 1 91  ? -3.873  -26.019 -7.053  1.00   28.10  ? 91   CYS B CA  1 
ATOM   2981 C C   . CYS B 1 91  ? -3.380  -25.078 -5.956  1.00   27.48  ? 91   CYS B C   1 
ATOM   2982 O O   . CYS B 1 91  ? -2.196  -25.077 -5.611  1.00   27.45  ? 91   CYS B O   1 
ATOM   2983 C CB  . CYS B 1 91  ? -3.469  -27.474 -6.757  1.00   28.10  ? 91   CYS B CB  1 
ATOM   2984 S SG  . CYS B 1 91  ? -4.266  -28.196 -5.261  1.00   32.84  ? 91   CYS B SG  1 
ATOM   2985 N N   . PHE B 1 92  ? -4.297  -24.278 -5.409  1.00   26.77  ? 92   PHE B N   1 
ATOM   2986 C CA  . PHE B 1 92  ? -3.922  -23.224 -4.478  1.00   26.57  ? 92   PHE B CA  1 
ATOM   2987 C C   . PHE B 1 92  ? -3.438  -23.756 -3.116  1.00   26.83  ? 92   PHE B C   1 
ATOM   2988 O O   . PHE B 1 92  ? -4.171  -24.441 -2.424  1.00   27.31  ? 92   PHE B O   1 
ATOM   2989 C CB  . PHE B 1 92  ? -5.058  -22.210 -4.313  1.00   25.86  ? 92   PHE B CB  1 
ATOM   2990 C CG  . PHE B 1 92  ? -4.632  -20.931 -3.652  1.00   25.33  ? 92   PHE B CG  1 
ATOM   2991 C CD1 . PHE B 1 92  ? -4.257  -19.826 -4.415  1.00   26.14  ? 92   PHE B CD1 1 
ATOM   2992 C CD2 . PHE B 1 92  ? -4.601  -20.827 -2.261  1.00   24.34  ? 92   PHE B CD2 1 
ATOM   2993 C CE1 . PHE B 1 92  ? -3.851  -18.631 -3.789  1.00   26.62  ? 92   PHE B CE1 1 
ATOM   2994 C CE2 . PHE B 1 92  ? -4.209  -19.634 -1.626  1.00   24.72  ? 92   PHE B CE2 1 
ATOM   2995 C CZ  . PHE B 1 92  ? -3.837  -18.540 -2.390  1.00   24.29  ? 92   PHE B CZ  1 
ATOM   2996 N N   . PRO B 1 93  ? -2.193  -23.435 -2.731  1.00   27.39  ? 93   PRO B N   1 
ATOM   2997 C CA  . PRO B 1 93  ? -1.629  -24.034 -1.511  1.00   27.68  ? 93   PRO B CA  1 
ATOM   2998 C C   . PRO B 1 93  ? -2.295  -23.524 -0.238  1.00   27.43  ? 93   PRO B C   1 
ATOM   2999 O O   . PRO B 1 93  ? -2.617  -22.336 -0.136  1.00   26.87  ? 93   PRO B O   1 
ATOM   3000 C CB  . PRO B 1 93  ? -0.149  -23.637 -1.561  1.00   28.65  ? 93   PRO B CB  1 
ATOM   3001 C CG  . PRO B 1 93  ? -0.051  -22.535 -2.538  1.00   28.81  ? 93   PRO B CG  1 
ATOM   3002 C CD  . PRO B 1 93  ? -1.230  -22.575 -3.440  1.00   27.32  ? 93   PRO B CD  1 
ATOM   3003 N N   . TYR B 1 94  ? -2.539  -24.443 0.695   1.00   27.38  ? 94   TYR B N   1 
ATOM   3004 C CA  . TYR B 1 94  ? -3.154  -24.142 1.989   1.00   28.30  ? 94   TYR B CA  1 
ATOM   3005 C C   . TYR B 1 94  ? -4.600  -23.679 1.850   1.00   28.91  ? 94   TYR B C   1 
ATOM   3006 O O   . TYR B 1 94  ? -5.147  -23.076 2.763   1.00   28.85  ? 94   TYR B O   1 
ATOM   3007 C CB  . TYR B 1 94  ? -2.341  -23.094 2.757   1.00   27.53  ? 94   TYR B CB  1 
ATOM   3008 C CG  . TYR B 1 94  ? -1.035  -23.622 3.297   1.00   28.02  ? 94   TYR B CG  1 
ATOM   3009 C CD1 . TYR B 1 94  ? 0.132   -23.544 2.534   1.00   27.54  ? 94   TYR B CD1 1 
ATOM   3010 C CD2 . TYR B 1 94  ? -0.961  -24.194 4.577   1.00   25.44  ? 94   TYR B CD2 1 
ATOM   3011 C CE1 . TYR B 1 94  ? 1.336   -24.026 3.017   1.00   27.84  ? 94   TYR B CE1 1 
ATOM   3012 C CE2 . TYR B 1 94  ? 0.249   -24.688 5.074   1.00   25.42  ? 94   TYR B CE2 1 
ATOM   3013 C CZ  . TYR B 1 94  ? 1.387   -24.599 4.283   1.00   26.89  ? 94   TYR B CZ  1 
ATOM   3014 O OH  . TYR B 1 94  ? 2.592   -25.062 4.734   1.00   27.95  ? 94   TYR B OH  1 
ATOM   3015 N N   . ALA B 1 95  ? -5.202  -23.962 0.696   1.00   29.74  ? 95   ALA B N   1 
ATOM   3016 C CA  . ALA B 1 95  ? -6.593  -23.595 0.419   1.00   30.51  ? 95   ALA B CA  1 
ATOM   3017 C C   . ALA B 1 95  ? -7.585  -24.153 1.449   1.00   31.21  ? 95   ALA B C   1 
ATOM   3018 O O   . ALA B 1 95  ? -8.616  -23.531 1.723   1.00   31.69  ? 95   ALA B O   1 
ATOM   3019 C CB  . ALA B 1 95  ? -6.977  -24.051 -0.966  1.00   29.92  ? 95   ALA B CB  1 
ATOM   3020 N N   . ARG B 1 96  ? -7.276  -25.316 2.017   0.83   31.19  ? 96   ARG B N   1 
ATOM   3021 C CA  . ARG B 1 96  ? -8.138  -25.902 3.043   0.83   31.83  ? 96   ARG B CA  1 
ATOM   3022 C C   . ARG B 1 96  ? -8.043  -25.177 4.387   0.83   31.65  ? 96   ARG B C   1 
ATOM   3023 O O   . ARG B 1 96  ? -8.841  -25.445 5.279   0.83   32.13  ? 96   ARG B O   1 
ATOM   3024 C CB  . ARG B 1 96  ? -7.816  -27.379 3.256   0.83   32.24  ? 96   ARG B CB  1 
ATOM   3025 C CG  . ARG B 1 96  ? -8.213  -28.296 2.110   0.83   33.49  ? 96   ARG B CG  1 
ATOM   3026 C CD  . ARG B 1 96  ? -7.723  -29.715 2.373   0.83   37.23  ? 96   ARG B CD  1 
ATOM   3027 N NE  . ARG B 1 96  ? -6.257  -29.779 2.435   0.83   40.75  ? 96   ARG B NE  1 
ATOM   3028 C CZ  . ARG B 1 96  ? -5.557  -30.807 2.910   0.83   41.23  ? 96   ARG B CZ  1 
ATOM   3029 N NH1 . ARG B 1 96  ? -6.170  -31.884 3.386   0.83   41.10  ? 96   ARG B NH1 1 
ATOM   3030 N NH2 . ARG B 1 96  ? -4.232  -30.749 2.918   0.83   43.98  ? 96   ARG B NH2 1 
ATOM   3031 N N   . GLN B 1 97  ? -7.053  -24.290 4.538   0.94   31.15  ? 97   GLN B N   1 
ATOM   3032 C CA  . GLN B 1 97  ? -6.918  -23.495 5.762   0.94   30.88  ? 97   GLN B CA  1 
ATOM   3033 C C   . GLN B 1 97  ? -7.423  -22.068 5.506   0.94   29.54  ? 97   GLN B C   1 
ATOM   3034 O O   . GLN B 1 97  ? -6.656  -21.110 5.501   0.94   28.98  ? 97   GLN B O   1 
ATOM   3035 C CB  . GLN B 1 97  ? -5.476  -23.531 6.295   0.94   31.19  ? 97   GLN B CB  1 
ATOM   3036 C CG  . GLN B 1 97  ? -5.004  -24.962 6.675   0.94   34.87  ? 97   GLN B CG  1 
ATOM   3037 C CD  . GLN B 1 97  ? -3.535  -25.055 7.100   0.94   39.95  ? 97   GLN B CD  1 
ATOM   3038 O OE1 . GLN B 1 97  ? -3.007  -24.185 7.817   0.94   41.96  ? 97   GLN B OE1 1 
ATOM   3039 N NE2 . GLN B 1 97  ? -2.873  -26.135 6.678   0.94   39.80  ? 97   GLN B NE2 1 
ATOM   3040 N N   . ASP B 1 98  ? -8.728  -21.952 5.277   0.42   28.62  ? 98   ASP B N   1 
ATOM   3041 C CA  . ASP B 1 98  ? -9.321  -20.699 4.836   0.42   28.27  ? 98   ASP B CA  1 
ATOM   3042 C C   . ASP B 1 98  ? -10.282 -20.117 5.868   0.42   28.44  ? 98   ASP B C   1 
ATOM   3043 O O   . ASP B 1 98  ? -10.966 -19.132 5.601   0.42   27.70  ? 98   ASP B O   1 
ATOM   3044 C CB  . ASP B 1 98  ? -10.034 -20.901 3.503   0.42   27.66  ? 98   ASP B CB  1 
ATOM   3045 C CG  . ASP B 1 98  ? -11.228 -21.837 3.616   0.42   26.70  ? 98   ASP B CG  1 
ATOM   3046 O OD1 . ASP B 1 98  ? -11.200 -22.777 4.445   0.42   23.75  ? 98   ASP B OD1 1 
ATOM   3047 O OD2 . ASP B 1 98  ? -12.197 -21.630 2.864   0.42   24.62  ? 98   ASP B OD2 1 
ATOM   3048 N N   . LYS B 1 99  ? -10.316 -20.728 7.047   0.53   29.24  ? 99   LYS B N   1 
ATOM   3049 C CA  . LYS B 1 99  ? -11.146 -20.242 8.153   0.53   30.60  ? 99   LYS B CA  1 
ATOM   3050 C C   . LYS B 1 99  ? -10.622 -20.755 9.500   0.53   31.59  ? 99   LYS B C   1 
ATOM   3051 O O   . LYS B 1 99  ? -9.767  -21.652 9.547   0.53   30.91  ? 99   LYS B O   1 
ATOM   3052 C CB  . LYS B 1 99  ? -12.614 -20.635 7.941   0.53   30.40  ? 99   LYS B CB  1 
ATOM   3053 C CG  . LYS B 1 99  ? -12.842 -22.137 7.755   0.53   31.45  ? 99   LYS B CG  1 
ATOM   3054 C CD  . LYS B 1 99  ? -14.277 -22.454 7.355   0.53   32.63  ? 99   LYS B CD  1 
ATOM   3055 C CE  . LYS B 1 99  ? -14.381 -23.860 6.764   0.53   34.27  ? 99   LYS B CE  1 
ATOM   3056 N NZ  . LYS B 1 99  ? -15.779 -24.184 6.310   0.53   36.14  ? 99   LYS B NZ  1 
ATOM   3057 N N   . LYS B 1 100 ? -11.140 -20.187 10.593  1.00   33.36  ? 100  LYS B N   1 
ATOM   3058 C CA  . LYS B 1 100 ? -10.644 -20.521 11.927  1.00   35.46  ? 100  LYS B CA  1 
ATOM   3059 C C   . LYS B 1 100 ? -11.276 -21.772 12.527  1.00   36.64  ? 100  LYS B C   1 
ATOM   3060 O O   . LYS B 1 100 ? -10.681 -22.400 13.413  1.00   37.39  ? 100  LYS B O   1 
ATOM   3061 C CB  . LYS B 1 100 ? -10.832 -19.344 12.892  1.00   35.43  ? 100  LYS B CB  1 
ATOM   3062 C CG  . LYS B 1 100 ? -9.840  -18.197 12.736  1.00   35.29  ? 100  LYS B CG  1 
ATOM   3063 C CD  . LYS B 1 100 ? -9.941  -17.295 13.970  1.00   35.77  ? 100  LYS B CD  1 
ATOM   3064 C CE  . LYS B 1 100 ? -9.139  -16.025 13.839  1.00   35.37  ? 100  LYS B CE  1 
ATOM   3065 N NZ  . LYS B 1 100 ? -9.677  -14.950 14.756  1.00   37.53  ? 100  LYS B NZ  1 
ATOM   3066 N N   . ASP B 1 101 ? -12.480 -22.116 12.069  0.57   37.98  ? 101  ASP B N   1 
ATOM   3067 C CA  . ASP B 1 101 ? -13.197 -23.306 12.546  0.57   39.52  ? 101  ASP B CA  1 
ATOM   3068 C C   . ASP B 1 101 ? -13.248 -23.406 14.077  0.57   39.91  ? 101  ASP B C   1 
ATOM   3069 O O   . ASP B 1 101 ? -12.933 -24.454 14.646  0.57   40.14  ? 101  ASP B O   1 
ATOM   3070 C CB  . ASP B 1 101 ? -12.583 -24.585 11.950  0.57   39.92  ? 101  ASP B CB  1 
ATOM   3071 C CG  . ASP B 1 101 ? -12.834 -24.717 10.456  0.57   41.12  ? 101  ASP B CG  1 
ATOM   3072 O OD1 . ASP B 1 101 ? -14.003 -24.568 10.024  0.57   43.13  ? 101  ASP B OD1 1 
ATOM   3073 O OD2 . ASP B 1 101 ? -11.862 -24.988 9.712   0.57   42.91  ? 101  ASP B OD2 1 
ATOM   3074 N N   . LYS B 1 102 ? -13.632 -22.303 14.726  1.00   40.54  ? 102  LYS B N   1 
ATOM   3075 C CA  . LYS B 1 102 ? -13.786 -22.216 16.198  1.00   41.33  ? 102  LYS B CA  1 
ATOM   3076 C C   . LYS B 1 102 ? -12.496 -22.431 17.002  1.00   41.28  ? 102  LYS B C   1 
ATOM   3077 O O   . LYS B 1 102 ? -12.523 -22.501 18.238  1.00   41.68  ? 102  LYS B O   1 
ATOM   3078 C CB  . LYS B 1 102 ? -14.896 -23.152 16.716  1.00   41.54  ? 102  LYS B CB  1 
ATOM   3079 C CG  . LYS B 1 102 ? -16.252 -22.992 16.033  1.00   42.98  ? 102  LYS B CG  1 
ATOM   3080 C CD  . LYS B 1 102 ? -17.408 -23.391 16.949  1.00   45.23  ? 102  LYS B CD  1 
ATOM   3081 C CE  . LYS B 1 102 ? -17.445 -24.896 17.217  1.00   52.15  ? 102  LYS B CE  1 
ATOM   3082 N NZ  . LYS B 1 102 ? -18.601 -25.277 18.080  1.00   57.40  ? 102  LYS B NZ  1 
ATOM   3083 N N   . SER B 1 103 ? -11.372 -22.536 16.304  0.67   41.00  ? 103  SER B N   1 
ATOM   3084 C CA  . SER B 1 103 ? -10.094 -22.762 16.959  0.67   40.67  ? 103  SER B CA  1 
ATOM   3085 C C   . SER B 1 103 ? -9.158  -21.557 16.812  0.67   40.21  ? 103  SER B C   1 
ATOM   3086 O O   . SER B 1 103 ? -9.412  -20.650 16.018  0.67   39.86  ? 103  SER B O   1 
ATOM   3087 C CB  . SER B 1 103 ? -9.445  -24.036 16.413  0.67   40.74  ? 103  SER B CB  1 
ATOM   3088 O OG  . SER B 1 103 ? -8.138  -24.203 16.940  0.67   41.87  ? 103  SER B OG  1 
ATOM   3089 N N   . ARG B 1 104 ? -8.078  -21.564 17.591  1.00   40.05  ? 104  ARG B N   1 
ATOM   3090 C CA  . ARG B 1 104 ? -7.071  -20.515 17.551  1.00   39.80  ? 104  ARG B CA  1 
ATOM   3091 C C   . ARG B 1 104 ? -6.116  -20.814 16.387  1.00   39.57  ? 104  ARG B C   1 
ATOM   3092 O O   . ARG B 1 104 ? -4.911  -21.028 16.566  1.00   39.92  ? 104  ARG B O   1 
ATOM   3093 C CB  . ARG B 1 104 ? -6.344  -20.460 18.899  1.00   40.09  ? 104  ARG B CB  1 
ATOM   3094 C CG  . ARG B 1 104 ? -6.085  -19.053 19.435  1.00   41.57  ? 104  ARG B CG  1 
ATOM   3095 C CD  . ARG B 1 104 ? -6.410  -18.939 20.936  1.00   43.99  ? 104  ARG B CD  1 
ATOM   3096 N NE  . ARG B 1 104 ? -6.216  -20.216 21.611  1.00   45.91  ? 104  ARG B NE  1 
ATOM   3097 C CZ  . ARG B 1 104 ? -6.898  -20.650 22.665  1.00   44.62  ? 104  ARG B CZ  1 
ATOM   3098 N NH1 . ARG B 1 104 ? -7.844  -19.912 23.239  1.00   44.64  ? 104  ARG B NH1 1 
ATOM   3099 N NH2 . ARG B 1 104 ? -6.616  -21.846 23.148  1.00   46.87  ? 104  ARG B NH2 1 
ATOM   3100 N N   . ALA B 1 105 ? -6.684  -20.824 15.183  1.00   38.76  ? 105  ALA B N   1 
ATOM   3101 C CA  . ALA B 1 105 ? -5.987  -21.287 14.002  1.00   37.89  ? 105  ALA B CA  1 
ATOM   3102 C C   . ALA B 1 105 ? -5.585  -20.127 13.086  1.00   36.85  ? 105  ALA B C   1 
ATOM   3103 O O   . ALA B 1 105 ? -6.237  -19.077 13.073  1.00   36.63  ? 105  ALA B O   1 
ATOM   3104 C CB  . ALA B 1 105 ? -6.857  -22.286 13.245  1.00   38.14  ? 105  ALA B CB  1 
ATOM   3105 N N   . PRO B 1 106 ? -4.502  -20.314 12.319  0.99   35.78  ? 106  PRO B N   1 
ATOM   3106 C CA  . PRO B 1 106 ? -4.204  -19.348 11.275  0.99   34.95  ? 106  PRO B CA  1 
ATOM   3107 C C   . PRO B 1 106 ? -5.170  -19.517 10.098  0.99   33.35  ? 106  PRO B C   1 
ATOM   3108 O O   . PRO B 1 106 ? -5.640  -20.620 9.825   0.99   33.52  ? 106  PRO B O   1 
ATOM   3109 C CB  . PRO B 1 106 ? -2.790  -19.738 10.850  0.99   34.81  ? 106  PRO B CB  1 
ATOM   3110 C CG  . PRO B 1 106 ? -2.739  -21.208 11.090  0.99   35.64  ? 106  PRO B CG  1 
ATOM   3111 C CD  . PRO B 1 106 ? -3.570  -21.460 12.295  0.99   35.89  ? 106  PRO B CD  1 
ATOM   3112 N N   . ILE B 1 107 ? -5.483  -18.427 9.419   1.00   32.23  ? 107  ILE B N   1 
ATOM   3113 C CA  . ILE B 1 107 ? -6.118  -18.547 8.110   1.00   30.10  ? 107  ILE B CA  1 
ATOM   3114 C C   . ILE B 1 107 ? -4.949  -18.541 7.128   1.00   29.32  ? 107  ILE B C   1 
ATOM   3115 O O   . ILE B 1 107 ? -4.598  -17.513 6.559   1.00   28.45  ? 107  ILE B O   1 
ATOM   3116 C CB  . ILE B 1 107 ? -7.139  -17.443 7.870   1.00   30.68  ? 107  ILE B CB  1 
ATOM   3117 C CG1 . ILE B 1 107 ? -8.141  -17.407 9.037   1.00   30.05  ? 107  ILE B CG1 1 
ATOM   3118 C CG2 . ILE B 1 107 ? -7.868  -17.653 6.511   1.00   29.44  ? 107  ILE B CG2 1 
ATOM   3119 C CD1 . ILE B 1 107 ? -9.186  -16.285 8.938   1.00   31.54  ? 107  ILE B CD1 1 
ATOM   3120 N N   . SER B 1 108 ? -4.322  -19.710 6.993   1.00   28.10  ? 108  SER B N   1 
ATOM   3121 C CA  . SER B 1 108 ? -3.095  -19.861 6.217   1.00   27.57  ? 108  SER B CA  1 
ATOM   3122 C C   . SER B 1 108 ? -3.246  -19.505 4.745   1.00   26.81  ? 108  SER B C   1 
ATOM   3123 O O   . SER B 1 108 ? -2.289  -19.044 4.124   1.00   26.90  ? 108  SER B O   1 
ATOM   3124 C CB  . SER B 1 108 ? -2.554  -21.279 6.350   1.00   27.28  ? 108  SER B CB  1 
ATOM   3125 O OG  . SER B 1 108 ? -2.298  -21.570 7.704   1.00   29.45  ? 108  SER B OG  1 
ATOM   3126 N N   . ALA B 1 109 ? -4.446  -19.709 4.196   1.00   25.80  ? 109  ALA B N   1 
ATOM   3127 C CA  . ALA B 1 109 ? -4.728  -19.300 2.817   1.00   25.27  ? 109  ALA B CA  1 
ATOM   3128 C C   . ALA B 1 109 ? -4.681  -17.775 2.667   1.00   24.58  ? 109  ALA B C   1 
ATOM   3129 O O   . ALA B 1 109 ? -4.280  -17.268 1.611   1.00   24.96  ? 109  ALA B O   1 
ATOM   3130 C CB  . ALA B 1 109 ? -6.067  -19.848 2.342   1.00   24.86  ? 109  ALA B CB  1 
ATOM   3131 N N   . LYS B 1 110 ? -5.087  -17.045 3.712   1.00   24.06  ? 110  LYS B N   1 
ATOM   3132 C CA  . LYS B 1 110 ? -4.975  -15.583 3.676   1.00   23.17  ? 110  LYS B CA  1 
ATOM   3133 C C   . LYS B 1 110 ? -3.507  -15.170 3.780   1.00   23.13  ? 110  LYS B C   1 
ATOM   3134 O O   . LYS B 1 110 ? -3.065  -14.229 3.116   1.00   22.66  ? 110  LYS B O   1 
ATOM   3135 C CB  . LYS B 1 110 ? -5.797  -14.900 4.770   1.00   23.58  ? 110  LYS B CB  1 
ATOM   3136 C CG  . LYS B 1 110 ? -5.640  -13.357 4.811   1.00   22.73  ? 110  LYS B CG  1 
ATOM   3137 C CD  . LYS B 1 110 ? -6.049  -12.712 3.453   1.00   24.98  ? 110  LYS B CD  1 
ATOM   3138 C CE  . LYS B 1 110 ? -5.910  -11.184 3.444   1.00   25.53  ? 110  LYS B CE  1 
ATOM   3139 N NZ  . LYS B 1 110 ? -6.499  -10.607 4.684   1.00   26.80  ? 110  LYS B NZ  1 
ATOM   3140 N N   . LEU B 1 111 ? -2.746  -15.869 4.617   1.00   22.22  ? 111  LEU B N   1 
ATOM   3141 C CA  . LEU B 1 111 ? -1.323  -15.590 4.653   1.00   22.22  ? 111  LEU B CA  1 
ATOM   3142 C C   . LEU B 1 111 ? -0.681  -15.869 3.257   1.00   21.36  ? 111  LEU B C   1 
ATOM   3143 O O   . LEU B 1 111 ? 0.112   -15.072 2.764   1.00   20.19  ? 111  LEU B O   1 
ATOM   3144 C CB  . LEU B 1 111 ? -0.648  -16.407 5.749   1.00   22.65  ? 111  LEU B CB  1 
ATOM   3145 C CG  . LEU B 1 111 ? 0.888   -16.413 5.760   1.00   24.96  ? 111  LEU B CG  1 
ATOM   3146 C CD1 . LEU B 1 111 ? 1.445   -15.011 6.074   1.00   25.83  ? 111  LEU B CD1 1 
ATOM   3147 C CD2 . LEU B 1 111 ? 1.369   -17.459 6.793   1.00   25.72  ? 111  LEU B CD2 1 
ATOM   3148 N N   . VAL B 1 112 ? -1.030  -16.995 2.642   1.00   20.25  ? 112  VAL B N   1 
ATOM   3149 C CA  . VAL B 1 112 ? -0.480  -17.326 1.323   1.00   20.61  ? 112  VAL B CA  1 
ATOM   3150 C C   . VAL B 1 112 ? -0.817  -16.223 0.311   1.00   19.97  ? 112  VAL B C   1 
ATOM   3151 O O   . VAL B 1 112 ? 0.060   -15.793 -0.418  1.00   20.11  ? 112  VAL B O   1 
ATOM   3152 C CB  . VAL B 1 112 ? -0.954  -18.698 0.801   1.00   20.16  ? 112  VAL B CB  1 
ATOM   3153 C CG1 . VAL B 1 112 ? -0.649  -18.850 -0.695  1.00   20.85  ? 112  VAL B CG1 1 
ATOM   3154 C CG2 . VAL B 1 112 ? -0.299  -19.831 1.583   1.00   21.55  ? 112  VAL B CG2 1 
ATOM   3155 N N   . ALA B 1 113 ? -2.070  -15.764 0.293   1.00   19.48  ? 113  ALA B N   1 
ATOM   3156 C CA  . ALA B 1 113 ? -2.486  -14.683 -0.613  1.00   20.16  ? 113  ALA B CA  1 
ATOM   3157 C C   . ALA B 1 113 ? -1.708  -13.394 -0.345  1.00   20.42  ? 113  ALA B C   1 
ATOM   3158 O O   . ALA B 1 113 ? -1.330  -12.673 -1.282  1.00   19.39  ? 113  ALA B O   1 
ATOM   3159 C CB  . ALA B 1 113 ? -3.986  -14.424 -0.493  1.00   19.88  ? 113  ALA B CB  1 
ATOM   3160 N N   . ASN B 1 114 ? -1.494  -13.097 0.939   1.00   20.15  ? 114  ASN B N   1 
ATOM   3161 C CA  . ASN B 1 114 ? -0.650  -11.959 1.307   1.00   20.56  ? 114  ASN B CA  1 
ATOM   3162 C C   . ASN B 1 114 ? 0.785   -12.084 0.833   1.00   20.02  ? 114  ASN B C   1 
ATOM   3163 O O   . ASN B 1 114 ? 1.341   -11.112 0.353   1.00   20.12  ? 114  ASN B O   1 
ATOM   3164 C CB  . ASN B 1 114 ? -0.670  -11.692 2.811   1.00   20.67  ? 114  ASN B CB  1 
ATOM   3165 C CG  . ASN B 1 114 ? -1.920  -10.965 3.255   1.00   21.22  ? 114  ASN B CG  1 
ATOM   3166 O OD1 . ASN B 1 114 ? -2.595  -10.309 2.454   1.00   23.47  ? 114  ASN B OD1 1 
ATOM   3167 N ND2 . ASN B 1 114 ? -2.219  -11.051 4.530   1.00   20.37  ? 114  ASN B ND2 1 
ATOM   3168 N N   . THR B 1 115 ? 1.381   -13.267 0.958   1.00   20.16  ? 115  THR B N   1 
ATOM   3169 C CA  . THR B 1 115 ? 2.750   -13.453 0.473   1.00   20.82  ? 115  THR B CA  1 
ATOM   3170 C C   . THR B 1 115 ? 2.820   -13.243 -1.061  1.00   20.83  ? 115  THR B C   1 
ATOM   3171 O O   . THR B 1 115 ? 3.724   -12.577 -1.540  1.00   20.35  ? 115  THR B O   1 
ATOM   3172 C CB  . THR B 1 115 ? 3.389   -14.800 0.922   1.00   20.80  ? 115  THR B CB  1 
ATOM   3173 O OG1 . THR B 1 115 ? 2.678   -15.895 0.334   1.00   22.35  ? 115  THR B OG1 1 
ATOM   3174 C CG2 . THR B 1 115 ? 3.345   -14.943 2.464   1.00   21.17  ? 115  THR B CG2 1 
ATOM   3175 N N   . LEU B 1 116 ? 1.850   -13.771 -1.807  1.00   21.05  ? 116  LEU B N   1 
ATOM   3176 C CA  . LEU B 1 116 ? 1.808   -13.574 -3.279  1.00   21.69  ? 116  LEU B CA  1 
ATOM   3177 C C   . LEU B 1 116 ? 1.671   -12.094 -3.660  1.00   22.07  ? 116  LEU B C   1 
ATOM   3178 O O   . LEU B 1 116 ? 2.327   -11.613 -4.579  1.00   22.37  ? 116  LEU B O   1 
ATOM   3179 C CB  . LEU B 1 116 ? 0.679   -14.399 -3.906  1.00   21.30  ? 116  LEU B CB  1 
ATOM   3180 C CG  . LEU B 1 116 ? 0.840   -15.930 -3.856  1.00   21.23  ? 116  LEU B CG  1 
ATOM   3181 C CD1 . LEU B 1 116 ? -0.511  -16.641 -3.909  1.00   18.44  ? 116  LEU B CD1 1 
ATOM   3182 C CD2 . LEU B 1 116 ? 1.725   -16.434 -4.993  1.00   20.27  ? 116  LEU B CD2 1 
ATOM   3183 N N   . SER B 1 117 ? 0.831   -11.377 -2.928  1.00   23.13  ? 117  SER B N   1 
ATOM   3184 C CA  . SER B 1 117 ? 0.662   -9.945  -3.119  1.00   24.59  ? 117  SER B CA  1 
ATOM   3185 C C   . SER B 1 117 ? 1.936   -9.131  -2.828  1.00   24.46  ? 117  SER B C   1 
ATOM   3186 O O   . SER B 1 117 ? 2.324   -8.285  -3.635  1.00   24.37  ? 117  SER B O   1 
ATOM   3187 C CB  . SER B 1 117 ? -0.513  -9.429  -2.292  1.00   24.56  ? 117  SER B CB  1 
ATOM   3188 O OG  . SER B 1 117 ? -1.687  -10.193 -2.569  1.00   28.07  ? 117  SER B OG  1 
ATOM   3189 N N   . VAL B 1 118 ? 2.595   -9.380  -1.700  1.00   24.45  ? 118  VAL B N   1 
ATOM   3190 C CA  . VAL B 1 118 ? 3.836   -8.636  -1.423  1.00   24.74  ? 118  VAL B CA  1 
ATOM   3191 C C   . VAL B 1 118 ? 5.019   -9.055  -2.301  1.00   24.48  ? 118  VAL B C   1 
ATOM   3192 O O   . VAL B 1 118 ? 5.934   -8.250  -2.519  1.00   24.17  ? 118  VAL B O   1 
ATOM   3193 C CB  . VAL B 1 118 ? 4.272   -8.658  0.062   1.00   24.85  ? 118  VAL B CB  1 
ATOM   3194 C CG1 . VAL B 1 118 ? 3.222   -8.006  0.937   1.00   26.17  ? 118  VAL B CG1 1 
ATOM   3195 C CG2 . VAL B 1 118 ? 4.624   -10.084 0.543   1.00   24.80  ? 118  VAL B CG2 1 
ATOM   3196 N N   . ALA B 1 119 ? 5.015   -10.296 -2.798  1.00   23.46  ? 119  ALA B N   1 
ATOM   3197 C CA  . ALA B 1 119 ? 6.073   -10.709 -3.737  1.00   23.73  ? 119  ALA B CA  1 
ATOM   3198 C C   . ALA B 1 119 ? 5.927   -9.940  -5.042  1.00   23.45  ? 119  ALA B C   1 
ATOM   3199 O O   . ALA B 1 119 ? 6.866   -9.819  -5.802  1.00   24.48  ? 119  ALA B O   1 
ATOM   3200 C CB  . ALA B 1 119 ? 6.045   -12.235 -3.983  1.00   23.28  ? 119  ALA B CB  1 
ATOM   3201 N N   . GLY B 1 120 ? 4.740   -9.400  -5.288  1.00   23.66  ? 120  GLY B N   1 
ATOM   3202 C CA  . GLY B 1 120 ? 4.494   -8.615  -6.501  1.00   23.61  ? 120  GLY B CA  1 
ATOM   3203 C C   . GLY B 1 120 ? 3.574   -9.211  -7.572  1.00   22.80  ? 120  GLY B C   1 
ATOM   3204 O O   . GLY B 1 120 ? 3.579   -8.747  -8.702  1.00   22.87  ? 120  GLY B O   1 
ATOM   3205 N N   . ALA B 1 121 ? 2.774   -10.220 -7.240  1.00   22.27  ? 121  ALA B N   1 
ATOM   3206 C CA  . ALA B 1 121 ? 1.782   -10.732 -8.197  1.00   21.67  ? 121  ALA B CA  1 
ATOM   3207 C C   . ALA B 1 121 ? 0.742   -9.647  -8.522  1.00   21.11  ? 121  ALA B C   1 
ATOM   3208 O O   . ALA B 1 121 ? 0.276   -8.975  -7.618  1.00   19.57  ? 121  ALA B O   1 
ATOM   3209 C CB  . ALA B 1 121 ? 1.100   -11.988 -7.660  1.00   21.60  ? 121  ALA B CB  1 
ATOM   3210 N N   . ASP B 1 122 ? 0.438   -9.463  -9.815  1.00   20.51  ? 122  ASP B N   1 
ATOM   3211 C CA  . ASP B 1 122 ? -0.581  -8.509  -10.279 1.00   20.50  ? 122  ASP B CA  1 
ATOM   3212 C C   . ASP B 1 122 ? -1.882  -9.218  -10.609 1.00   20.39  ? 122  ASP B C   1 
ATOM   3213 O O   . ASP B 1 122 ? -2.934  -8.587  -10.795 1.00   19.46  ? 122  ASP B O   1 
ATOM   3214 C CB  . ASP B 1 122 ? -0.101  -7.766  -11.532 1.00   21.30  ? 122  ASP B CB  1 
ATOM   3215 C CG  . ASP B 1 122 ? 1.191   -7.000  -11.296 1.00   23.20  ? 122  ASP B CG  1 
ATOM   3216 O OD1 . ASP B 1 122 ? 1.225   -6.127  -10.391 1.00   25.32  ? 122  ASP B OD1 1 
ATOM   3217 O OD2 . ASP B 1 122 ? 2.194   -7.293  -11.986 1.00   25.22  ? 122  ASP B OD2 1 
ATOM   3218 N N   . HIS B 1 123 ? -1.814  -10.544 -10.692 1.00   20.24  ? 123  HIS B N   1 
ATOM   3219 C CA  . HIS B 1 123 ? -2.948  -11.314 -11.169 1.00   20.35  ? 123  HIS B CA  1 
ATOM   3220 C C   . HIS B 1 123 ? -2.716  -12.773 -10.812 1.00   19.65  ? 123  HIS B C   1 
ATOM   3221 O O   . HIS B 1 123 ? -1.590  -13.239 -10.865 1.00   20.24  ? 123  HIS B O   1 
ATOM   3222 C CB  . HIS B 1 123 ? -3.068  -11.132 -12.697 1.00   20.93  ? 123  HIS B CB  1 
ATOM   3223 C CG  . HIS B 1 123 ? -4.247  -11.821 -13.306 1.00   24.02  ? 123  HIS B CG  1 
ATOM   3224 N ND1 . HIS B 1 123 ? -5.502  -11.796 -12.735 1.00   29.19  ? 123  HIS B ND1 1 
ATOM   3225 C CD2 . HIS B 1 123 ? -4.373  -12.533 -14.452 1.00   27.66  ? 123  HIS B CD2 1 
ATOM   3226 C CE1 . HIS B 1 123 ? -6.350  -12.466 -13.497 1.00   27.97  ? 123  HIS B CE1 1 
ATOM   3227 N NE2 . HIS B 1 123 ? -5.691  -12.925 -14.544 1.00   29.33  ? 123  HIS B NE2 1 
ATOM   3228 N N   . ILE B 1 124 ? -3.784  -13.470 -10.444 1.00   19.00  ? 124  ILE B N   1 
ATOM   3229 C CA  . ILE B 1 124 ? -3.733  -14.887 -10.141 1.00   19.79  ? 124  ILE B CA  1 
ATOM   3230 C C   . ILE B 1 124 ? -4.662  -15.632 -11.084 1.00   19.71  ? 124  ILE B C   1 
ATOM   3231 O O   . ILE B 1 124 ? -5.776  -15.186 -11.340 1.00   20.53  ? 124  ILE B O   1 
ATOM   3232 C CB  . ILE B 1 124 ? -4.212  -15.204 -8.679  1.00   19.89  ? 124  ILE B CB  1 
ATOM   3233 C CG1 . ILE B 1 124 ? -3.502  -14.316 -7.644  1.00   20.08  ? 124  ILE B CG1 1 
ATOM   3234 C CG2 . ILE B 1 124 ? -4.049  -16.713 -8.357  1.00   19.80  ? 124  ILE B CG2 1 
ATOM   3235 C CD1 . ILE B 1 124 ? -1.970  -14.534 -7.573  1.00   21.33  ? 124  ILE B CD1 1 
ATOM   3236 N N   . ILE B 1 125 ? -4.201  -16.767 -11.588 1.00   19.86  ? 125  ILE B N   1 
ATOM   3237 C CA  . ILE B 1 125 ? -5.073  -17.693 -12.305 1.00   19.76  ? 125  ILE B CA  1 
ATOM   3238 C C   . ILE B 1 125 ? -5.025  -18.991 -11.529 1.00   20.20  ? 125  ILE B C   1 
ATOM   3239 O O   . ILE B 1 125 ? -3.948  -19.555 -11.299 1.00   19.62  ? 125  ILE B O   1 
ATOM   3240 C CB  . ILE B 1 125 ? -4.600  -17.936 -13.764 1.00   19.43  ? 125  ILE B CB  1 
ATOM   3241 C CG1 . ILE B 1 125 ? -4.558  -16.617 -14.546 1.00   19.43  ? 125  ILE B CG1 1 
ATOM   3242 C CG2 . ILE B 1 125 ? -5.484  -18.995 -14.453 1.00   18.97  ? 125  ILE B CG2 1 
ATOM   3243 C CD1 . ILE B 1 125 ? -3.988  -16.741 -15.964 1.00   20.62  ? 125  ILE B CD1 1 
ATOM   3244 N N   . THR B 1 126 ? -6.196  -19.470 -11.123 1.00   20.89  ? 126  THR B N   1 
ATOM   3245 C CA  . THR B 1 126 ? -6.267  -20.698 -10.359 1.00   21.48  ? 126  THR B CA  1 
ATOM   3246 C C   . THR B 1 126 ? -7.455  -21.535 -10.838 1.00   22.39  ? 126  THR B C   1 
ATOM   3247 O O   . THR B 1 126 ? -8.278  -21.062 -11.642 1.00   22.00  ? 126  THR B O   1 
ATOM   3248 C CB  . THR B 1 126 ? -6.302  -20.385 -8.818  1.00   21.77  ? 126  THR B CB  1 
ATOM   3249 O OG1 . THR B 1 126 ? -6.115  -21.591 -8.070  1.00   24.74  ? 126  THR B OG1 1 
ATOM   3250 C CG2 . THR B 1 126 ? -7.592  -19.694 -8.402  1.00   20.15  ? 126  THR B CG2 1 
ATOM   3251 N N   . MET B 1 127 ? -7.525  -22.786 -10.387 1.00   23.33  ? 127  MET B N   1 
ATOM   3252 C CA  . MET B 1 127 ? -8.624  -23.665 -10.774 1.00   24.74  ? 127  MET B CA  1 
ATOM   3253 C C   . MET B 1 127 ? -9.298  -24.304 -9.567  1.00   25.55  ? 127  MET B C   1 
ATOM   3254 O O   . MET B 1 127 ? -8.634  -24.945 -8.741  1.00   25.07  ? 127  MET B O   1 
ATOM   3255 C CB  . MET B 1 127 ? -8.172  -24.756 -11.757 1.00   25.77  ? 127  MET B CB  1 
ATOM   3256 C CG  . MET B 1 127 ? -9.306  -25.755 -12.087 1.00   27.48  ? 127  MET B CG  1 
ATOM   3257 S SD  . MET B 1 127 ? -8.972  -26.847 -13.465 1.00   34.57  ? 127  MET B SD  1 
ATOM   3258 C CE  . MET B 1 127 ? -9.109  -25.696 -14.841 1.00   31.11  ? 127  MET B CE  1 
ATOM   3259 N N   . ASP B 1 128 ? -10.616 -24.112 -9.489  1.00   26.24  ? 128  ASP B N   1 
ATOM   3260 C CA  . ASP B 1 128 ? -11.470 -24.667 -8.439  1.00   27.24  ? 128  ASP B CA  1 
ATOM   3261 C C   . ASP B 1 128 ? -10.910 -24.475 -7.036  1.00   27.21  ? 128  ASP B C   1 
ATOM   3262 O O   . ASP B 1 128 ? -10.557 -25.447 -6.361  1.00   27.06  ? 128  ASP B O   1 
ATOM   3263 C CB  . ASP B 1 128 ? -11.763 -26.149 -8.701  1.00   28.58  ? 128  ASP B CB  1 
ATOM   3264 C CG  . ASP B 1 128 ? -12.769 -26.356 -9.823  1.00   30.76  ? 128  ASP B CG  1 
ATOM   3265 O OD1 . ASP B 1 128 ? -13.893 -25.812 -9.755  1.00   34.70  ? 128  ASP B OD1 1 
ATOM   3266 O OD2 . ASP B 1 128 ? -12.437 -27.079 -10.773 1.00   35.49  ? 128  ASP B OD2 1 
ATOM   3267 N N   . LEU B 1 129 ? -10.823 -23.215 -6.613  1.00   26.65  ? 129  LEU B N   1 
ATOM   3268 C CA  . LEU B 1 129 ? -10.471 -22.888 -5.242  1.00   26.29  ? 129  LEU B CA  1 
ATOM   3269 C C   . LEU B 1 129 ? -11.390 -23.652 -4.314  1.00   26.35  ? 129  LEU B C   1 
ATOM   3270 O O   . LEU B 1 129 ? -12.606 -23.704 -4.547  1.00   25.37  ? 129  LEU B O   1 
ATOM   3271 C CB  . LEU B 1 129 ? -10.624 -21.395 -4.978  1.00   26.16  ? 129  LEU B CB  1 
ATOM   3272 C CG  . LEU B 1 129 ? -9.532  -20.515 -5.592  1.00   25.97  ? 129  LEU B CG  1 
ATOM   3273 C CD1 . LEU B 1 129 ? -9.991  -19.064 -5.653  1.00   25.66  ? 129  LEU B CD1 1 
ATOM   3274 C CD2 . LEU B 1 129 ? -8.231  -20.664 -4.817  1.00   25.05  ? 129  LEU B CD2 1 
ATOM   3275 N N   . HIS B 1 130 ? -10.800 -24.237 -3.269  1.00   26.73  ? 130  HIS B N   1 
ATOM   3276 C CA  . HIS B 1 130 ? -11.544 -25.039 -2.299  1.00   27.34  ? 130  HIS B CA  1 
ATOM   3277 C C   . HIS B 1 130 ? -12.741 -24.251 -1.783  1.00   27.22  ? 130  HIS B C   1 
ATOM   3278 O O   . HIS B 1 130 ? -13.827 -24.804 -1.590  1.00   26.90  ? 130  HIS B O   1 
ATOM   3279 C CB  . HIS B 1 130 ? -10.631 -25.448 -1.142  1.00   28.05  ? 130  HIS B CB  1 
ATOM   3280 C CG  . HIS B 1 130 ? -11.351 -26.139 -0.025  1.00   30.63  ? 130  HIS B CG  1 
ATOM   3281 N ND1 . HIS B 1 130 ? -11.904 -27.395 -0.161  1.00   32.53  ? 130  HIS B ND1 1 
ATOM   3282 C CD2 . HIS B 1 130 ? -11.618 -25.743 1.242   1.00   31.98  ? 130  HIS B CD2 1 
ATOM   3283 C CE1 . HIS B 1 130 ? -12.465 -27.749 0.983   1.00   34.23  ? 130  HIS B CE1 1 
ATOM   3284 N NE2 . HIS B 1 130 ? -12.311 -26.762 1.848   1.00   33.17  ? 130  HIS B NE2 1 
ATOM   3285 N N   . ALA B 1 131 ? -12.525 -22.952 -1.583  1.00   26.67  ? 131  ALA B N   1 
ATOM   3286 C CA  . ALA B 1 131 ? -13.590 -22.024 -1.232  1.00   27.15  ? 131  ALA B CA  1 
ATOM   3287 C C   . ALA B 1 131 ? -13.465 -20.777 -2.097  1.00   27.23  ? 131  ALA B C   1 
ATOM   3288 O O   . ALA B 1 131 ? -12.402 -20.185 -2.185  1.00   26.87  ? 131  ALA B O   1 
ATOM   3289 C CB  . ALA B 1 131 ? -13.508 -21.664 0.241   1.00   27.27  ? 131  ALA B CB  1 
ATOM   3290 N N   . SER B 1 132 ? -14.567 -20.394 -2.725  1.00   28.00  ? 132  SER B N   1 
ATOM   3291 C CA  . SER B 1 132 ? -14.609 -19.257 -3.644  1.00   28.76  ? 132  SER B CA  1 
ATOM   3292 C C   . SER B 1 132 ? -14.320 -17.937 -2.933  1.00   28.25  ? 132  SER B C   1 
ATOM   3293 O O   . SER B 1 132 ? -13.814 -16.994 -3.549  1.00   28.06  ? 132  SER B O   1 
ATOM   3294 C CB  . SER B 1 132 ? -15.974 -19.204 -4.328  1.00   28.94  ? 132  SER B CB  1 
ATOM   3295 O OG  . SER B 1 132 ? -16.177 -20.426 -5.040  1.00   32.94  ? 132  SER B OG  1 
ATOM   3296 N N   . GLN B 1 133 ? -14.612 -17.894 -1.632  1.00   27.32  ? 133  GLN B N   1 
ATOM   3297 C CA  . GLN B 1 133 ? -14.272 -16.737 -0.805  1.00   27.38  ? 133  GLN B CA  1 
ATOM   3298 C C   . GLN B 1 133 ? -12.782 -16.390 -0.843  1.00   26.70  ? 133  GLN B C   1 
ATOM   3299 O O   . GLN B 1 133 ? -12.399 -15.249 -0.590  1.00   27.08  ? 133  GLN B O   1 
ATOM   3300 C CB  . GLN B 1 133 ? -14.723 -16.948 0.648   1.00   27.40  ? 133  GLN B CB  1 
ATOM   3301 C CG  . GLN B 1 133 ? -16.244 -16.968 0.862   1.00   29.36  ? 133  GLN B CG  1 
ATOM   3302 C CD  . GLN B 1 133 ? -16.901 -18.314 0.530   1.00   32.47  ? 133  GLN B CD  1 
ATOM   3303 O OE1 . GLN B 1 133 ? -16.224 -19.320 0.282   1.00   33.22  ? 133  GLN B OE1 1 
ATOM   3304 N NE2 . GLN B 1 133 ? -18.234 -18.325 0.514   1.00   32.78  ? 133  GLN B NE2 1 
ATOM   3305 N N   . ILE B 1 134 ? -11.944 -17.372 -1.159  1.00   26.18  ? 134  ILE B N   1 
ATOM   3306 C CA  . ILE B 1 134 ? -10.498 -17.144 -1.225  1.00   25.35  ? 134  ILE B CA  1 
ATOM   3307 C C   . ILE B 1 134 ? -10.134 -16.043 -2.230  1.00   24.72  ? 134  ILE B C   1 
ATOM   3308 O O   . ILE B 1 134 ? -9.136  -15.351 -2.049  1.00   24.09  ? 134  ILE B O   1 
ATOM   3309 C CB  . ILE B 1 134 ? -9.714  -18.460 -1.489  1.00   25.41  ? 134  ILE B CB  1 
ATOM   3310 C CG1 . ILE B 1 134 ? -9.736  -19.349 -0.227  1.00   26.07  ? 134  ILE B CG1 1 
ATOM   3311 C CG2 . ILE B 1 134 ? -8.266  -18.173 -1.912  1.00   25.14  ? 134  ILE B CG2 1 
ATOM   3312 C CD1 . ILE B 1 134 ? -9.229  -20.778 -0.459  1.00   26.35  ? 134  ILE B CD1 1 
ATOM   3313 N N   . GLN B 1 135 ? -10.952 -15.860 -3.268  1.00   24.02  ? 135  GLN B N   1 
ATOM   3314 C CA  . GLN B 1 135 ? -10.772 -14.705 -4.153  1.00   23.87  ? 135  GLN B CA  1 
ATOM   3315 C C   . GLN B 1 135 ? -10.769 -13.389 -3.366  1.00   22.83  ? 135  GLN B C   1 
ATOM   3316 O O   . GLN B 1 135 ? -10.026 -12.474 -3.688  1.00   21.94  ? 135  GLN B O   1 
ATOM   3317 C CB  . GLN B 1 135 ? -11.848 -14.647 -5.231  1.00   24.40  ? 135  GLN B CB  1 
ATOM   3318 C CG  . GLN B 1 135 ? -11.708 -15.664 -6.358  1.00   26.76  ? 135  GLN B CG  1 
ATOM   3319 C CD  . GLN B 1 135 ? -12.438 -15.195 -7.624  1.00   29.05  ? 135  GLN B CD  1 
ATOM   3320 O OE1 . GLN B 1 135 ? -12.398 -14.018 -7.974  1.00   32.04  ? 135  GLN B OE1 1 
ATOM   3321 N NE2 . GLN B 1 135 ? -13.114 -16.110 -8.295  1.00   29.78  ? 135  GLN B NE2 1 
ATOM   3322 N N   . GLY B 1 136 ? -11.604 -13.311 -2.333  1.00   21.88  ? 136  GLY B N   1 
ATOM   3323 C CA  . GLY B 1 136 ? -11.649 -12.135 -1.458  1.00   21.78  ? 136  GLY B CA  1 
ATOM   3324 C C   . GLY B 1 136 ? -10.432 -11.923 -0.568  1.00   21.17  ? 136  GLY B C   1 
ATOM   3325 O O   . GLY B 1 136 ? -10.310 -10.877 0.066   1.00   20.88  ? 136  GLY B O   1 
ATOM   3326 N N   . PHE B 1 137 ? -9.525  -12.901 -0.535  1.00   21.00  ? 137  PHE B N   1 
ATOM   3327 C CA  . PHE B 1 137 ? -8.288  -12.795 0.240   1.00   21.02  ? 137  PHE B CA  1 
ATOM   3328 C C   . PHE B 1 137 ? -7.257  -11.921 -0.452  1.00   21.83  ? 137  PHE B C   1 
ATOM   3329 O O   . PHE B 1 137 ? -6.220  -11.603 0.130   1.00   21.77  ? 137  PHE B O   1 
ATOM   3330 C CB  . PHE B 1 137 ? -7.673  -14.182 0.504   1.00   20.93  ? 137  PHE B CB  1 
ATOM   3331 C CG  . PHE B 1 137 ? -8.450  -15.028 1.474   1.00   19.92  ? 137  PHE B CG  1 
ATOM   3332 C CD1 . PHE B 1 137 ? -8.038  -16.320 1.761   1.00   21.32  ? 137  PHE B CD1 1 
ATOM   3333 C CD2 . PHE B 1 137 ? -9.589  -14.540 2.095   1.00   19.10  ? 137  PHE B CD2 1 
ATOM   3334 C CE1 . PHE B 1 137 ? -8.749  -17.112 2.678   1.00   21.72  ? 137  PHE B CE1 1 
ATOM   3335 C CE2 . PHE B 1 137 ? -10.314 -15.321 2.994   1.00   19.42  ? 137  PHE B CE2 1 
ATOM   3336 C CZ  . PHE B 1 137 ? -9.903  -16.607 3.276   1.00   20.94  ? 137  PHE B CZ  1 
ATOM   3337 N N   . PHE B 1 138 ? -7.534  -11.564 -1.706  1.00   21.54  ? 138  PHE B N   1 
ATOM   3338 C CA  . PHE B 1 138 ? -6.645  -10.724 -2.513  1.00   21.26  ? 138  PHE B CA  1 
ATOM   3339 C C   . PHE B 1 138 ? -7.309  -9.385  -2.752  1.00   21.43  ? 138  PHE B C   1 
ATOM   3340 O O   . PHE B 1 138 ? -8.543  -9.278  -2.717  1.00   21.08  ? 138  PHE B O   1 
ATOM   3341 C CB  . PHE B 1 138 ? -6.415  -11.369 -3.898  1.00   21.33  ? 138  PHE B CB  1 
ATOM   3342 C CG  . PHE B 1 138 ? -5.598  -12.636 -3.852  1.00   21.85  ? 138  PHE B CG  1 
ATOM   3343 C CD1 . PHE B 1 138 ? -6.215  -13.872 -3.664  1.00   21.22  ? 138  PHE B CD1 1 
ATOM   3344 C CD2 . PHE B 1 138 ? -4.210  -12.589 -3.956  1.00   21.94  ? 138  PHE B CD2 1 
ATOM   3345 C CE1 . PHE B 1 138 ? -5.463  -15.030 -3.622  1.00   21.59  ? 138  PHE B CE1 1 
ATOM   3346 C CE2 . PHE B 1 138 ? -3.446  -13.769 -3.925  1.00   20.78  ? 138  PHE B CE2 1 
ATOM   3347 C CZ  . PHE B 1 138 ? -4.083  -14.981 -3.755  1.00   18.85  ? 138  PHE B CZ  1 
ATOM   3348 N N   . ASP B 1 139 ? -6.497  -8.371  -3.028  0.69   20.73  ? 139  ASP B N   1 
ATOM   3349 C CA  . ASP B 1 139 ? -7.017  -7.146  -3.608  0.69   21.31  ? 139  ASP B CA  1 
ATOM   3350 C C   . ASP B 1 139 ? -6.805  -7.090  -5.126  0.69   21.20  ? 139  ASP B C   1 
ATOM   3351 O O   . ASP B 1 139 ? -7.471  -6.334  -5.816  0.69   21.99  ? 139  ASP B O   1 
ATOM   3352 C CB  . ASP B 1 139 ? -6.444  -5.924  -2.895  0.69   21.76  ? 139  ASP B CB  1 
ATOM   3353 C CG  . ASP B 1 139 ? -7.062  -5.723  -1.519  0.69   22.66  ? 139  ASP B CG  1 
ATOM   3354 O OD1 . ASP B 1 139 ? -8.306  -5.804  -1.395  0.69   22.66  ? 139  ASP B OD1 1 
ATOM   3355 O OD2 . ASP B 1 139 ? -6.301  -5.513  -0.561  0.69   24.74  ? 139  ASP B OD2 1 
ATOM   3356 N N   . ILE B 1 140 ? -5.910  -7.926  -5.637  1.00   21.59  ? 140  ILE B N   1 
ATOM   3357 C CA  . ILE B 1 140 ? -5.657  -8.036  -7.098  1.00   20.96  ? 140  ILE B CA  1 
ATOM   3358 C C   . ILE B 1 140 ? -6.663  -8.976  -7.737  1.00   21.24  ? 140  ILE B C   1 
ATOM   3359 O O   . ILE B 1 140 ? -7.237  -9.801  -7.036  1.00   19.98  ? 140  ILE B O   1 
ATOM   3360 C CB  . ILE B 1 140 ? -4.252  -8.592  -7.375  1.00   20.34  ? 140  ILE B CB  1 
ATOM   3361 C CG1 . ILE B 1 140 ? -4.012  -9.909  -6.607  1.00   19.83  ? 140  ILE B CG1 1 
ATOM   3362 C CG2 . ILE B 1 140 ? -3.186  -7.525  -7.049  1.00   20.97  ? 140  ILE B CG2 1 
ATOM   3363 C CD1 . ILE B 1 140 ? -2.773  -10.691 -7.073  1.00   18.76  ? 140  ILE B CD1 1 
ATOM   3364 N N   . PRO B 1 141 ? -6.844  -8.891  -9.083  1.00   21.76  ? 141  PRO B N   1 
ATOM   3365 C CA  . PRO B 1 141 ? -7.834  -9.793  -9.659  1.00   21.57  ? 141  PRO B CA  1 
ATOM   3366 C C   . PRO B 1 141 ? -7.421  -11.264 -9.650  1.00   22.18  ? 141  PRO B C   1 
ATOM   3367 O O   . PRO B 1 141 ? -6.251  -11.610 -9.868  1.00   21.41  ? 141  PRO B O   1 
ATOM   3368 C CB  . PRO B 1 141 ? -8.058  -9.264  -11.085 1.00   21.70  ? 141  PRO B CB  1 
ATOM   3369 C CG  . PRO B 1 141 ? -6.966  -8.275  -11.357 1.00   22.38  ? 141  PRO B CG  1 
ATOM   3370 C CD  . PRO B 1 141 ? -6.271  -7.939  -10.066 1.00   21.45  ? 141  PRO B CD  1 
ATOM   3371 N N   . VAL B 1 142 ? -8.398  -12.115 -9.346  1.00   22.39  ? 142  VAL B N   1 
ATOM   3372 C CA  . VAL B 1 142 ? -8.227  -13.567 -9.390  1.00   22.52  ? 142  VAL B CA  1 
ATOM   3373 C C   . VAL B 1 142 ? -9.229  -14.130 -10.437 1.00   23.54  ? 142  VAL B C   1 
ATOM   3374 O O   . VAL B 1 142 ? -10.422 -13.813 -10.402 1.00   24.28  ? 142  VAL B O   1 
ATOM   3375 C CB  . VAL B 1 142 ? -8.488  -14.183 -7.990  1.00   23.13  ? 142  VAL B CB  1 
ATOM   3376 C CG1 . VAL B 1 142 ? -8.326  -15.715 -8.004  1.00   21.39  ? 142  VAL B CG1 1 
ATOM   3377 C CG2 . VAL B 1 142 ? -7.559  -13.520 -6.889  1.00   20.49  ? 142  VAL B CG2 1 
ATOM   3378 N N   . ASP B 1 143 ? -8.741  -14.923 -11.384 1.00   23.78  ? 143  ASP B N   1 
ATOM   3379 C CA  . ASP B 1 143 ? -9.627  -15.753 -12.197 1.00   24.04  ? 143  ASP B CA  1 
ATOM   3380 C C   . ASP B 1 143 ? -9.585  -17.185 -11.689 1.00   24.22  ? 143  ASP B C   1 
ATOM   3381 O O   . ASP B 1 143 ? -8.526  -17.831 -11.702 1.00   23.89  ? 143  ASP B O   1 
ATOM   3382 C CB  . ASP B 1 143 ? -9.269  -15.669 -13.680 1.00   24.66  ? 143  ASP B CB  1 
ATOM   3383 C CG  . ASP B 1 143 ? -9.491  -14.277 -14.241 1.00   25.17  ? 143  ASP B CG  1 
ATOM   3384 O OD1 . ASP B 1 143 ? -10.616 -13.747 -14.102 1.00   25.65  ? 143  ASP B OD1 1 
ATOM   3385 O OD2 . ASP B 1 143 ? -8.528  -13.709 -14.793 1.00   27.76  ? 143  ASP B OD2 1 
ATOM   3386 N N   . ASN B 1 144 ? -10.742 -17.636 -11.195 1.00   24.20  ? 144  ASN B N   1 
ATOM   3387 C CA  . ASN B 1 144 ? -10.927 -18.974 -10.653 1.00   24.72  ? 144  ASN B CA  1 
ATOM   3388 C C   . ASN B 1 144 ? -11.625 -19.842 -11.695 1.00   24.92  ? 144  ASN B C   1 
ATOM   3389 O O   . ASN B 1 144 ? -12.840 -19.767 -11.868 1.00   24.06  ? 144  ASN B O   1 
ATOM   3390 C CB  . ASN B 1 144 ? -11.756 -18.923 -9.358  1.00   24.42  ? 144  ASN B CB  1 
ATOM   3391 C CG  . ASN B 1 144 ? -11.953 -20.314 -8.711  1.00   24.98  ? 144  ASN B CG  1 
ATOM   3392 O OD1 . ASN B 1 144 ? -11.059 -21.166 -8.723  1.00   23.98  ? 144  ASN B OD1 1 
ATOM   3393 N ND2 . ASN B 1 144 ? -13.124 -20.523 -8.118  1.00   25.82  ? 144  ASN B ND2 1 
ATOM   3394 N N   . LEU B 1 145 ? -10.836 -20.647 -12.401 1.00   25.21  ? 145  LEU B N   1 
ATOM   3395 C CA  . LEU B 1 145 ? -11.344 -21.503 -13.468 1.00   25.22  ? 145  LEU B CA  1 
ATOM   3396 C C   . LEU B 1 145 ? -12.030 -22.739 -12.889 1.00   25.97  ? 145  LEU B C   1 
ATOM   3397 O O   . LEU B 1 145 ? -11.741 -23.152 -11.770 1.00   25.54  ? 145  LEU B O   1 
ATOM   3398 C CB  . LEU B 1 145 ? -10.192 -21.916 -14.398 1.00   25.00  ? 145  LEU B CB  1 
ATOM   3399 C CG  . LEU B 1 145 ? -9.463  -20.759 -15.086 1.00   25.84  ? 145  LEU B CG  1 
ATOM   3400 C CD1 . LEU B 1 145 ? -8.114  -21.206 -15.614 1.00   25.73  ? 145  LEU B CD1 1 
ATOM   3401 C CD2 . LEU B 1 145 ? -10.313 -20.205 -16.213 1.00   27.75  ? 145  LEU B CD2 1 
ATOM   3402 N N   . TYR B 1 146 ? -12.956 -23.318 -13.647 0.90   26.94  ? 146  TYR B N   1 
ATOM   3403 C CA  . TYR B 1 146 ? -13.671 -24.510 -13.187 0.90   28.02  ? 146  TYR B CA  1 
ATOM   3404 C C   . TYR B 1 146 ? -13.361 -25.702 -14.055 0.90   28.08  ? 146  TYR B C   1 
ATOM   3405 O O   . TYR B 1 146 ? -13.325 -25.598 -15.285 0.90   27.57  ? 146  TYR B O   1 
ATOM   3406 C CB  . TYR B 1 146 ? -15.176 -24.275 -13.173 0.90   28.39  ? 146  TYR B CB  1 
ATOM   3407 C CG  . TYR B 1 146 ? -15.575 -23.082 -12.365 0.90   31.48  ? 146  TYR B CG  1 
ATOM   3408 C CD1 . TYR B 1 146 ? -15.880 -21.879 -12.994 0.90   35.01  ? 146  TYR B CD1 1 
ATOM   3409 C CD2 . TYR B 1 146 ? -15.642 -23.139 -10.970 0.90   33.98  ? 146  TYR B CD2 1 
ATOM   3410 C CE1 . TYR B 1 146 ? -16.229 -20.772 -12.271 0.90   36.75  ? 146  TYR B CE1 1 
ATOM   3411 C CE2 . TYR B 1 146 ? -16.005 -22.025 -10.233 0.90   36.02  ? 146  TYR B CE2 1 
ATOM   3412 C CZ  . TYR B 1 146 ? -16.301 -20.849 -10.899 0.90   37.78  ? 146  TYR B CZ  1 
ATOM   3413 O OH  . TYR B 1 146 ? -16.664 -19.721 -10.209 0.90   41.40  ? 146  TYR B OH  1 
ATOM   3414 N N   . ALA B 1 147 ? -13.126 -26.836 -13.404 1.00   28.67  ? 147  ALA B N   1 
ATOM   3415 C CA  . ALA B 1 147 ? -13.048 -28.108 -14.116 1.00   29.31  ? 147  ALA B CA  1 
ATOM   3416 C C   . ALA B 1 147 ? -14.441 -28.604 -14.500 1.00   29.12  ? 147  ALA B C   1 
ATOM   3417 O O   . ALA B 1 147 ? -14.564 -29.533 -15.279 1.00   29.43  ? 147  ALA B O   1 
ATOM   3418 C CB  . ALA B 1 147 ? -12.340 -29.160 -13.267 1.00   29.36  ? 147  ALA B CB  1 
ATOM   3419 N N   . GLU B 1 148 ? -15.481 -27.998 -13.932 1.00   29.65  ? 148  GLU B N   1 
ATOM   3420 C CA  . GLU B 1 148 ? -16.862 -28.458 -14.161 1.00   31.07  ? 148  GLU B CA  1 
ATOM   3421 C C   . GLU B 1 148 ? -17.224 -28.767 -15.637 1.00   30.55  ? 148  GLU B C   1 
ATOM   3422 O O   . GLU B 1 148 ? -17.725 -29.863 -15.923 1.00   31.39  ? 148  GLU B O   1 
ATOM   3423 C CB  . GLU B 1 148 ? -17.897 -27.504 -13.550 1.00   31.06  ? 148  GLU B CB  1 
ATOM   3424 C CG  . GLU B 1 148 ? -19.333 -27.986 -13.780 1.00   33.87  ? 148  GLU B CG  1 
ATOM   3425 C CD  . GLU B 1 148 ? -20.360 -27.243 -12.951 1.00   38.39  ? 148  GLU B CD  1 
ATOM   3426 O OE1 . GLU B 1 148 ? -19.978 -26.473 -12.048 1.00   40.94  ? 148  GLU B OE1 1 
ATOM   3427 O OE2 . GLU B 1 148 ? -21.568 -27.442 -13.198 1.00   41.01  ? 148  GLU B OE2 1 
ATOM   3428 N N   . PRO B 1 149 ? -16.978 -27.818 -16.569 1.00   30.55  ? 149  PRO B N   1 
ATOM   3429 C CA  . PRO B 1 149 ? -17.291 -28.139 -17.974 1.00   30.15  ? 149  PRO B CA  1 
ATOM   3430 C C   . PRO B 1 149 ? -16.572 -29.393 -18.468 1.00   29.89  ? 149  PRO B C   1 
ATOM   3431 O O   . PRO B 1 149 ? -17.176 -30.205 -19.168 1.00   30.09  ? 149  PRO B O   1 
ATOM   3432 C CB  . PRO B 1 149 ? -16.799 -26.900 -18.733 1.00   30.51  ? 149  PRO B CB  1 
ATOM   3433 C CG  . PRO B 1 149 ? -16.966 -25.788 -17.740 1.00   30.84  ? 149  PRO B CG  1 
ATOM   3434 C CD  . PRO B 1 149 ? -16.566 -26.402 -16.418 1.00   30.68  ? 149  PRO B CD  1 
ATOM   3435 N N   . ALA B 1 150 ? -15.304 -29.557 -18.103 1.00   29.29  ? 150  ALA B N   1 
ATOM   3436 C CA  . ALA B 1 150 ? -14.560 -30.758 -18.467 1.00   29.49  ? 150  ALA B CA  1 
ATOM   3437 C C   . ALA B 1 150 ? -15.073 -32.010 -17.738 1.00   29.44  ? 150  ALA B C   1 
ATOM   3438 O O   . ALA B 1 150 ? -15.029 -33.102 -18.297 1.00   29.58  ? 150  ALA B O   1 
ATOM   3439 C CB  . ALA B 1 150 ? -13.068 -30.563 -18.233 1.00   29.49  ? 150  ALA B CB  1 
ATOM   3440 N N   . VAL B 1 151 ? -15.572 -31.837 -16.509 1.00   29.18  ? 151  VAL B N   1 
ATOM   3441 C CA  . VAL B 1 151 ? -16.190 -32.935 -15.747 1.00   29.35  ? 151  VAL B CA  1 
ATOM   3442 C C   . VAL B 1 151 ? -17.509 -33.397 -16.398 1.00   29.67  ? 151  VAL B C   1 
ATOM   3443 O O   . VAL B 1 151 ? -17.701 -34.592 -16.669 1.00   29.83  ? 151  VAL B O   1 
ATOM   3444 C CB  . VAL B 1 151 ? -16.441 -32.546 -14.253 1.00   28.94  ? 151  VAL B CB  1 
ATOM   3445 C CG1 . VAL B 1 151 ? -17.176 -33.665 -13.509 1.00   28.05  ? 151  VAL B CG1 1 
ATOM   3446 C CG2 . VAL B 1 151 ? -15.123 -32.198 -13.549 1.00   28.64  ? 151  VAL B CG2 1 
ATOM   3447 N N   . LEU B 1 152 ? -18.411 -32.449 -16.639 1.00   30.31  ? 152  LEU B N   1 
ATOM   3448 C CA  . LEU B 1 152 ? -19.679 -32.742 -17.322 1.00   31.38  ? 152  LEU B CA  1 
ATOM   3449 C C   . LEU B 1 152 ? -19.442 -33.479 -18.645 1.00   31.99  ? 152  LEU B C   1 
ATOM   3450 O O   . LEU B 1 152 ? -20.148 -34.446 -18.956 1.00   31.94  ? 152  LEU B O   1 
ATOM   3451 C CB  . LEU B 1 152 ? -20.500 -31.467 -17.543 1.00   31.56  ? 152  LEU B CB  1 
ATOM   3452 C CG  . LEU B 1 152 ? -21.007 -30.718 -16.302 1.00   32.73  ? 152  LEU B CG  1 
ATOM   3453 C CD1 . LEU B 1 152 ? -21.548 -29.346 -16.670 1.00   34.43  ? 152  LEU B CD1 1 
ATOM   3454 C CD2 . LEU B 1 152 ? -22.064 -31.509 -15.557 1.00   36.05  ? 152  LEU B CD2 1 
ATOM   3455 N N   . LYS B 1 153 ? -18.423 -33.045 -19.394 1.00   32.36  ? 153  LYS B N   1 
ATOM   3456 C CA  . LYS B 1 153 ? -18.046 -33.691 -20.648 1.00   32.99  ? 153  LYS B CA  1 
ATOM   3457 C C   . LYS B 1 153 ? -17.573 -35.109 -20.408 1.00   32.96  ? 153  LYS B C   1 
ATOM   3458 O O   . LYS B 1 153 ? -18.024 -36.043 -21.095 1.00   33.00  ? 153  LYS B O   1 
ATOM   3459 C CB  . LYS B 1 153 ? -16.960 -32.893 -21.392 1.00   33.41  ? 153  LYS B CB  1 
ATOM   3460 C CG  . LYS B 1 153 ? -16.507 -33.528 -22.712 1.00   34.73  ? 153  LYS B CG  1 
ATOM   3461 C CD  . LYS B 1 153 ? -15.619 -32.576 -23.510 1.00   38.25  ? 153  LYS B CD  1 
ATOM   3462 C CE  . LYS B 1 153 ? -15.096 -33.226 -24.778 1.00   40.14  ? 153  LYS B CE  1 
ATOM   3463 N NZ  . LYS B 1 153 ? -13.928 -34.113 -24.492 1.00   43.19  ? 153  LYS B NZ  1 
ATOM   3464 N N   . TRP B 1 154 ? -16.670 -35.286 -19.440 1.00   32.61  ? 154  TRP B N   1 
ATOM   3465 C CA  . TRP B 1 154 ? -16.185 -36.616 -19.124 1.00   32.09  ? 154  TRP B CA  1 
ATOM   3466 C C   . TRP B 1 154 ? -17.347 -37.569 -18.770 1.00   32.04  ? 154  TRP B C   1 
ATOM   3467 O O   . TRP B 1 154 ? -17.386 -38.712 -19.238 1.00   32.43  ? 154  TRP B O   1 
ATOM   3468 C CB  . TRP B 1 154 ? -15.127 -36.597 -18.008 1.00   31.89  ? 154  TRP B CB  1 
ATOM   3469 C CG  . TRP B 1 154 ? -14.388 -37.899 -17.937 1.00   31.23  ? 154  TRP B CG  1 
ATOM   3470 C CD1 . TRP B 1 154 ? -13.218 -38.211 -18.570 1.00   30.40  ? 154  TRP B CD1 1 
ATOM   3471 C CD2 . TRP B 1 154 ? -14.795 -39.087 -17.236 1.00   31.09  ? 154  TRP B CD2 1 
ATOM   3472 N NE1 . TRP B 1 154 ? -12.851 -39.506 -18.278 1.00   31.59  ? 154  TRP B NE1 1 
ATOM   3473 C CE2 . TRP B 1 154 ? -13.804 -40.068 -17.468 1.00   31.09  ? 154  TRP B CE2 1 
ATOM   3474 C CE3 . TRP B 1 154 ? -15.886 -39.408 -16.411 1.00   30.47  ? 154  TRP B CE3 1 
ATOM   3475 C CZ2 . TRP B 1 154 ? -13.881 -41.360 -16.926 1.00   31.17  ? 154  TRP B CZ2 1 
ATOM   3476 C CZ3 . TRP B 1 154 ? -15.960 -40.695 -15.871 1.00   30.85  ? 154  TRP B CZ3 1 
ATOM   3477 C CH2 . TRP B 1 154 ? -14.963 -41.654 -16.135 1.00   29.63  ? 154  TRP B CH2 1 
ATOM   3478 N N   . ILE B 1 155 ? -18.279 -37.092 -17.950 1.00   31.88  ? 155  ILE B N   1 
ATOM   3479 C CA  . ILE B 1 155 ? -19.420 -37.900 -17.500 1.00   32.05  ? 155  ILE B CA  1 
ATOM   3480 C C   . ILE B 1 155 ? -20.285 -38.352 -18.690 1.00   32.54  ? 155  ILE B C   1 
ATOM   3481 O O   . ILE B 1 155 ? -20.526 -39.556 -18.869 1.00   31.86  ? 155  ILE B O   1 
ATOM   3482 C CB  . ILE B 1 155 ? -20.276 -37.143 -16.457 1.00   31.73  ? 155  ILE B CB  1 
ATOM   3483 C CG1 . ILE B 1 155 ? -19.518 -37.029 -15.123 1.00   31.61  ? 155  ILE B CG1 1 
ATOM   3484 C CG2 . ILE B 1 155 ? -21.622 -37.830 -16.238 1.00   31.30  ? 155  ILE B CG2 1 
ATOM   3485 C CD1 . ILE B 1 155 ? -20.107 -35.992 -14.152 1.00   28.01  ? 155  ILE B CD1 1 
ATOM   3486 N N   . ARG B 1 156 ? -20.731 -37.390 -19.498 1.00   32.84  ? 156  ARG B N   1 
ATOM   3487 C CA  . ARG B 1 156 ? -21.550 -37.694 -20.674 1.00   33.76  ? 156  ARG B CA  1 
ATOM   3488 C C   . ARG B 1 156 ? -20.917 -38.705 -21.635 1.00   34.19  ? 156  ARG B C   1 
ATOM   3489 O O   . ARG B 1 156 ? -21.633 -39.518 -22.220 1.00   34.68  ? 156  ARG B O   1 
ATOM   3490 C CB  . ARG B 1 156 ? -21.961 -36.418 -21.428 1.00   34.04  ? 156  ARG B CB  1 
ATOM   3491 C CG  . ARG B 1 156 ? -22.928 -35.525 -20.666 1.00   34.42  ? 156  ARG B CG  1 
ATOM   3492 C CD  . ARG B 1 156 ? -23.428 -34.373 -21.547 1.00   37.67  ? 156  ARG B CD  1 
ATOM   3493 N NE  . ARG B 1 156 ? -24.346 -33.488 -20.824 1.00   39.09  ? 156  ARG B NE  1 
ATOM   3494 C CZ  . ARG B 1 156 ? -24.001 -32.302 -20.313 1.00   40.85  ? 156  ARG B CZ  1 
ATOM   3495 N NH1 . ARG B 1 156 ? -22.755 -31.837 -20.448 1.00   41.56  ? 156  ARG B NH1 1 
ATOM   3496 N NH2 . ARG B 1 156 ? -24.905 -31.570 -19.676 1.00   40.87  ? 156  ARG B NH2 1 
ATOM   3497 N N   . GLU B 1 157 ? -19.592 -38.676 -21.777 0.71   34.44  ? 157  GLU B N   1 
ATOM   3498 C CA  . GLU B 1 157 ? -18.903 -39.570 -22.714 0.71   34.78  ? 157  GLU B CA  1 
ATOM   3499 C C   . GLU B 1 157 ? -18.392 -40.894 -22.120 0.71   34.79  ? 157  GLU B C   1 
ATOM   3500 O O   . GLU B 1 157 ? -17.988 -41.786 -22.864 0.71   34.77  ? 157  GLU B O   1 
ATOM   3501 C CB  . GLU B 1 157 ? -17.769 -38.829 -23.452 0.71   35.14  ? 157  GLU B CB  1 
ATOM   3502 C CG  . GLU B 1 157 ? -16.623 -38.359 -22.559 0.71   36.79  ? 157  GLU B CG  1 
ATOM   3503 C CD  . GLU B 1 157 ? -15.469 -37.696 -23.311 0.71   38.77  ? 157  GLU B CD  1 
ATOM   3504 O OE1 . GLU B 1 157 ? -14.316 -37.816 -22.829 0.71   39.60  ? 157  GLU B OE1 1 
ATOM   3505 O OE2 . GLU B 1 157 ? -15.701 -37.062 -24.367 0.71   39.08  ? 157  GLU B OE2 1 
ATOM   3506 N N   . ASN B 1 158 ? -18.410 -41.037 -20.797 1.00   34.58  ? 158  ASN B N   1 
ATOM   3507 C CA  . ASN B 1 158 ? -17.812 -42.227 -20.169 1.00   34.91  ? 158  ASN B CA  1 
ATOM   3508 C C   . ASN B 1 158 ? -18.761 -43.052 -19.311 1.00   34.55  ? 158  ASN B C   1 
ATOM   3509 O O   . ASN B 1 158 ? -18.510 -44.227 -19.066 1.00   34.52  ? 158  ASN B O   1 
ATOM   3510 C CB  . ASN B 1 158 ? -16.575 -41.856 -19.339 1.00   35.36  ? 158  ASN B CB  1 
ATOM   3511 C CG  . ASN B 1 158 ? -15.411 -41.423 -20.196 1.00   36.09  ? 158  ASN B CG  1 
ATOM   3512 O OD1 . ASN B 1 158 ? -14.608 -42.248 -20.637 1.00   38.95  ? 158  ASN B OD1 1 
ATOM   3513 N ND2 . ASN B 1 158 ? -15.302 -40.123 -20.427 1.00   35.68  ? 158  ASN B ND2 1 
ATOM   3514 N N   . ILE B 1 159 ? -19.836 -42.429 -18.839 1.00   34.29  ? 159  ILE B N   1 
ATOM   3515 C CA  . ILE B 1 159 ? -20.820 -43.130 -18.022 1.00   33.87  ? 159  ILE B CA  1 
ATOM   3516 C C   . ILE B 1 159 ? -22.125 -43.248 -18.811 1.00   34.06  ? 159  ILE B C   1 
ATOM   3517 O O   . ILE B 1 159 ? -22.845 -42.264 -18.979 1.00   33.26  ? 159  ILE B O   1 
ATOM   3518 C CB  . ILE B 1 159 ? -21.017 -42.432 -16.650 1.00   33.88  ? 159  ILE B CB  1 
ATOM   3519 C CG1 . ILE B 1 159 ? -19.660 -42.337 -15.927 1.00   32.92  ? 159  ILE B CG1 1 
ATOM   3520 C CG2 . ILE B 1 159 ? -22.063 -43.176 -15.800 1.00   33.06  ? 159  ILE B CG2 1 
ATOM   3521 C CD1 . ILE B 1 159 ? -19.648 -41.435 -14.700 1.00   32.78  ? 159  ILE B CD1 1 
ATOM   3522 N N   . SER B 1 160 ? -22.397 -44.461 -19.314 1.00   34.35  ? 160  SER B N   1 
ATOM   3523 C CA  . SER B 1 160 ? -23.600 -44.737 -20.127 1.00   35.07  ? 160  SER B CA  1 
ATOM   3524 C C   . SER B 1 160 ? -24.885 -44.324 -19.420 1.00   34.73  ? 160  SER B C   1 
ATOM   3525 O O   . SER B 1 160 ? -25.791 -43.779 -20.041 1.00   34.10  ? 160  SER B O   1 
ATOM   3526 C CB  . SER B 1 160 ? -23.692 -46.224 -20.509 1.00   35.04  ? 160  SER B CB  1 
ATOM   3527 O OG  . SER B 1 160 ? -22.419 -46.862 -20.439 1.00   37.14  ? 160  SER B OG  1 
ATOM   3528 N N   . GLU B 1 161 ? -24.947 -44.571 -18.113 1.00   35.24  ? 161  GLU B N   1 
ATOM   3529 C CA  . GLU B 1 161 ? -26.149 -44.275 -17.328 1.00   35.34  ? 161  GLU B CA  1 
ATOM   3530 C C   . GLU B 1 161 ? -26.193 -42.849 -16.759 1.00   35.28  ? 161  GLU B C   1 
ATOM   3531 O O   . GLU B 1 161 ? -26.895 -42.607 -15.773 1.00   34.80  ? 161  GLU B O   1 
ATOM   3532 C CB  . GLU B 1 161 ? -26.327 -45.290 -16.184 1.00   35.45  ? 161  GLU B CB  1 
ATOM   3533 C CG  . GLU B 1 161 ? -26.204 -46.759 -16.587 1.00   37.57  ? 161  GLU B CG  1 
ATOM   3534 C CD  . GLU B 1 161 ? -24.781 -47.295 -16.511 1.00   39.90  ? 161  GLU B CD  1 
ATOM   3535 O OE1 . GLU B 1 161 ? -23.808 -46.501 -16.577 1.00   39.35  ? 161  GLU B OE1 1 
ATOM   3536 O OE2 . GLU B 1 161 ? -24.634 -48.534 -16.372 1.00   43.60  ? 161  GLU B OE2 1 
ATOM   3537 N N   . TRP B 1 162 ? -25.483 -41.903 -17.377 1.00   35.17  ? 162  TRP B N   1 
ATOM   3538 C CA  . TRP B 1 162 ? -25.394 -40.547 -16.794 1.00   35.47  ? 162  TRP B CA  1 
ATOM   3539 C C   . TRP B 1 162 ? -26.740 -39.852 -16.591 1.00   35.68  ? 162  TRP B C   1 
ATOM   3540 O O   . TRP B 1 162 ? -26.889 -39.032 -15.677 1.00   35.36  ? 162  TRP B O   1 
ATOM   3541 C CB  . TRP B 1 162 ? -24.422 -39.631 -17.559 1.00   35.33  ? 162  TRP B CB  1 
ATOM   3542 C CG  . TRP B 1 162 ? -24.856 -39.149 -18.932 1.00   34.63  ? 162  TRP B CG  1 
ATOM   3543 C CD1 . TRP B 1 162 ? -24.518 -39.708 -20.130 1.00   35.01  ? 162  TRP B CD1 1 
ATOM   3544 C CD2 . TRP B 1 162 ? -25.655 -37.991 -19.244 1.00   33.73  ? 162  TRP B CD2 1 
ATOM   3545 N NE1 . TRP B 1 162 ? -25.069 -38.990 -21.163 1.00   34.06  ? 162  TRP B NE1 1 
ATOM   3546 C CE2 . TRP B 1 162 ? -25.770 -37.931 -20.650 1.00   34.03  ? 162  TRP B CE2 1 
ATOM   3547 C CE3 . TRP B 1 162 ? -26.290 -37.006 -18.473 1.00   33.81  ? 162  TRP B CE3 1 
ATOM   3548 C CZ2 . TRP B 1 162 ? -26.496 -36.921 -21.309 1.00   33.66  ? 162  TRP B CZ2 1 
ATOM   3549 C CZ3 . TRP B 1 162 ? -27.011 -36.002 -19.126 1.00   33.88  ? 162  TRP B CZ3 1 
ATOM   3550 C CH2 . TRP B 1 162 ? -27.109 -35.972 -20.532 1.00   33.99  ? 162  TRP B CH2 1 
ATOM   3551 N N   . ARG B 1 163 ? -27.719 -40.193 -17.428 1.00   35.73  ? 163  ARG B N   1 
ATOM   3552 C CA  . ARG B 1 163 ? -29.047 -39.574 -17.352 1.00   35.69  ? 163  ARG B CA  1 
ATOM   3553 C C   . ARG B 1 163 ? -29.872 -39.997 -16.145 1.00   35.77  ? 163  ARG B C   1 
ATOM   3554 O O   . ARG B 1 163 ? -30.861 -39.335 -15.805 1.00   35.75  ? 163  ARG B O   1 
ATOM   3555 C CB  . ARG B 1 163 ? -29.826 -39.829 -18.645 1.00   35.99  ? 163  ARG B CB  1 
ATOM   3556 C CG  . ARG B 1 163 ? -29.326 -38.991 -19.796 1.00   36.10  ? 163  ARG B CG  1 
ATOM   3557 C CD  . ARG B 1 163 ? -30.056 -39.297 -21.087 1.00   36.04  ? 163  ARG B CD  1 
ATOM   3558 N NE  . ARG B 1 163 ? -29.341 -38.739 -22.237 1.00   37.86  ? 163  ARG B NE  1 
ATOM   3559 C CZ  . ARG B 1 163 ? -28.355 -39.356 -22.892 1.00   38.85  ? 163  ARG B CZ  1 
ATOM   3560 N NH1 . ARG B 1 163 ? -27.946 -40.570 -22.522 1.00   38.56  ? 163  ARG B NH1 1 
ATOM   3561 N NH2 . ARG B 1 163 ? -27.776 -38.759 -23.930 1.00   39.23  ? 163  ARG B NH2 1 
ATOM   3562 N N   . ASN B 1 164 ? -29.461 -41.087 -15.499 1.00   35.70  ? 164  ASN B N   1 
ATOM   3563 C CA  . ASN B 1 164 ? -30.156 -41.613 -14.324 1.00   36.03  ? 164  ASN B CA  1 
ATOM   3564 C C   . ASN B 1 164 ? -29.258 -41.804 -13.113 1.00   35.38  ? 164  ASN B C   1 
ATOM   3565 O O   . ASN B 1 164 ? -29.557 -42.620 -12.235 1.00   35.56  ? 164  ASN B O   1 
ATOM   3566 C CB  . ASN B 1 164 ? -30.841 -42.943 -14.664 1.00   36.66  ? 164  ASN B CB  1 
ATOM   3567 C CG  . ASN B 1 164 ? -32.089 -42.746 -15.468 1.00   37.94  ? 164  ASN B CG  1 
ATOM   3568 O OD1 . ASN B 1 164 ? -33.160 -42.472 -14.918 1.00   39.09  ? 164  ASN B OD1 1 
ATOM   3569 N ND2 . ASN B 1 164 ? -31.958 -42.855 -16.789 1.00   39.06  ? 164  ASN B ND2 1 
ATOM   3570 N N   . CYS B 1 165 ? -28.167 -41.042 -13.064 1.00   34.34  ? 165  CYS B N   1 
ATOM   3571 C CA  . CYS B 1 165 ? -27.177 -41.182 -12.009 1.00   32.89  ? 165  CYS B CA  1 
ATOM   3572 C C   . CYS B 1 165 ? -27.484 -40.240 -10.844 1.00   32.53  ? 165  CYS B C   1 
ATOM   3573 O O   . CYS B 1 165 ? -28.404 -39.421 -10.922 1.00   31.97  ? 165  CYS B O   1 
ATOM   3574 C CB  . CYS B 1 165 ? -25.771 -40.928 -12.569 1.00   32.97  ? 165  CYS B CB  1 
ATOM   3575 S SG  . CYS B 1 165 ? -25.355 -39.174 -12.906 1.00   32.24  ? 165  CYS B SG  1 
ATOM   3576 N N   . THR B 1 166 ? -26.740 -40.392 -9.751  1.00   31.50  ? 166  THR B N   1 
ATOM   3577 C CA  . THR B 1 166 ? -26.817 -39.455 -8.643  1.00   31.03  ? 166  THR B CA  1 
ATOM   3578 C C   . THR B 1 166 ? -25.441 -38.848 -8.405  1.00   30.07  ? 166  THR B C   1 
ATOM   3579 O O   . THR B 1 166 ? -24.434 -39.561 -8.251  1.00   29.61  ? 166  THR B O   1 
ATOM   3580 C CB  . THR B 1 166 ? -27.323 -40.112 -7.336  1.00   31.30  ? 166  THR B CB  1 
ATOM   3581 O OG1 . THR B 1 166 ? -28.592 -40.733 -7.567  1.00   32.61  ? 166  THR B OG1 1 
ATOM   3582 C CG2 . THR B 1 166 ? -27.495 -39.063 -6.230  1.00   31.79  ? 166  THR B CG2 1 
ATOM   3583 N N   . ILE B 1 167 ? -25.404 -37.523 -8.376  1.00   29.15  ? 167  ILE B N   1 
ATOM   3584 C CA  . ILE B 1 167 ? -24.182 -36.817 -7.995  1.00   27.89  ? 167  ILE B CA  1 
ATOM   3585 C C   . ILE B 1 167 ? -24.150 -36.709 -6.476  1.00   27.39  ? 167  ILE B C   1 
ATOM   3586 O O   . ILE B 1 167 ? -25.109 -36.268 -5.854  1.00   27.29  ? 167  ILE B O   1 
ATOM   3587 C CB  . ILE B 1 167 ? -24.067 -35.430 -8.679  1.00   27.81  ? 167  ILE B CB  1 
ATOM   3588 C CG1 . ILE B 1 167 ? -24.407 -35.530 -10.179 1.00   27.14  ? 167  ILE B CG1 1 
ATOM   3589 C CG2 . ILE B 1 167 ? -22.667 -34.830 -8.462  1.00   27.81  ? 167  ILE B CG2 1 
ATOM   3590 C CD1 . ILE B 1 167 ? -23.537 -36.506 -10.983 1.00   27.79  ? 167  ILE B CD1 1 
ATOM   3591 N N   . VAL B 1 168 ? -23.040 -37.142 -5.888  1.00   27.00  ? 168  VAL B N   1 
ATOM   3592 C CA  . VAL B 1 168 ? -22.939 -37.287 -4.446  1.00   26.33  ? 168  VAL B CA  1 
ATOM   3593 C C   . VAL B 1 168 ? -21.805 -36.441 -3.885  1.00   26.60  ? 168  VAL B C   1 
ATOM   3594 O O   . VAL B 1 168 ? -20.659 -36.515 -4.361  1.00   26.05  ? 168  VAL B O   1 
ATOM   3595 C CB  . VAL B 1 168 ? -22.696 -38.763 -4.013  1.00   26.19  ? 168  VAL B CB  1 
ATOM   3596 C CG1 . VAL B 1 168 ? -22.843 -38.891 -2.494  1.00   25.31  ? 168  VAL B CG1 1 
ATOM   3597 C CG2 . VAL B 1 168 ? -23.667 -39.720 -4.708  1.00   25.76  ? 168  VAL B CG2 1 
ATOM   3598 N N   . SER B 1 169 ? -22.122 -35.641 -2.873  1.00   26.95  ? 169  SER B N   1 
ATOM   3599 C CA  . SER B 1 169 ? -21.091 -34.928 -2.140  1.00   28.75  ? 169  SER B CA  1 
ATOM   3600 C C   . SER B 1 169 ? -20.567 -35.838 -1.043  1.00   29.48  ? 169  SER B C   1 
ATOM   3601 O O   . SER B 1 169 ? -21.351 -36.446 -0.333  1.00   29.69  ? 169  SER B O   1 
ATOM   3602 C CB  . SER B 1 169 ? -21.624 -33.624 -1.520  1.00   29.09  ? 169  SER B CB  1 
ATOM   3603 O OG  . SER B 1 169 ? -20.549 -32.904 -0.921  1.00   28.87  ? 169  SER B OG  1 
ATOM   3604 N N   . PRO B 1 170 ? -19.236 -35.948 -0.914  1.00   30.67  ? 170  PRO B N   1 
ATOM   3605 C CA  . PRO B 1 170 ? -18.641 -36.720 0.177   1.00   31.42  ? 170  PRO B CA  1 
ATOM   3606 C C   . PRO B 1 170 ? -18.704 -36.007 1.528   1.00   32.52  ? 170  PRO B C   1 
ATOM   3607 O O   . PRO B 1 170 ? -18.430 -36.636 2.550   1.00   33.33  ? 170  PRO B O   1 
ATOM   3608 C CB  . PRO B 1 170 ? -17.182 -36.894 -0.259  1.00   32.07  ? 170  PRO B CB  1 
ATOM   3609 C CG  . PRO B 1 170 ? -16.931 -35.821 -1.237  1.00   31.67  ? 170  PRO B CG  1 
ATOM   3610 C CD  . PRO B 1 170 ? -18.230 -35.470 -1.878  1.00   30.46  ? 170  PRO B CD  1 
ATOM   3611 N N   . ASP B 1 171 ? -19.061 -34.724 1.546   0.70   32.69  ? 171  ASP B N   1 
ATOM   3612 C CA  . ASP B 1 171 ? -19.212 -34.003 2.818   0.70   33.76  ? 171  ASP B CA  1 
ATOM   3613 C C   . ASP B 1 171 ? -20.258 -32.893 2.760   0.70   34.07  ? 171  ASP B C   1 
ATOM   3614 O O   . ASP B 1 171 ? -20.878 -32.670 1.719   0.70   33.12  ? 171  ASP B O   1 
ATOM   3615 C CB  . ASP B 1 171 ? -17.870 -33.470 3.337   0.70   33.62  ? 171  ASP B CB  1 
ATOM   3616 C CG  . ASP B 1 171 ? -17.086 -32.701 2.286   0.70   34.93  ? 171  ASP B CG  1 
ATOM   3617 O OD1 . ASP B 1 171 ? -17.692 -31.970 1.465   0.70   35.35  ? 171  ASP B OD1 1 
ATOM   3618 O OD2 . ASP B 1 171 ? -15.841 -32.833 2.291   0.70   37.00  ? 171  ASP B OD2 1 
ATOM   3619 N N   . ALA B 1 172 ? -20.442 -32.210 3.890   1.00   35.43  ? 172  ALA B N   1 
ATOM   3620 C CA  . ALA B 1 172 ? -21.424 -31.124 4.010   1.00   36.94  ? 172  ALA B CA  1 
ATOM   3621 C C   . ALA B 1 172 ? -21.047 -29.924 3.153   1.00   37.84  ? 172  ALA B C   1 
ATOM   3622 O O   . ALA B 1 172 ? -21.909 -29.303 2.532   1.00   38.27  ? 172  ALA B O   1 
ATOM   3623 C CB  . ALA B 1 172 ? -21.585 -30.702 5.478   1.00   37.26  ? 172  ALA B CB  1 
ATOM   3624 N N   . GLY B 1 173 ? -19.750 -29.626 3.107   1.00   39.19  ? 173  GLY B N   1 
ATOM   3625 C CA  . GLY B 1 173 ? -19.230 -28.469 2.373   1.00   40.00  ? 173  GLY B CA  1 
ATOM   3626 C C   . GLY B 1 173 ? -19.315 -28.539 0.856   1.00   40.47  ? 173  GLY B C   1 
ATOM   3627 O O   . GLY B 1 173 ? -19.059 -27.542 0.173   1.00   40.73  ? 173  GLY B O   1 
ATOM   3628 N N   . GLY B 1 174 ? -19.667 -29.706 0.318   1.00   40.63  ? 174  GLY B N   1 
ATOM   3629 C CA  . GLY B 1 174 ? -19.697 -29.896 -1.140  1.00   40.39  ? 174  GLY B CA  1 
ATOM   3630 C C   . GLY B 1 174 ? -21.071 -29.828 -1.784  1.00   40.14  ? 174  GLY B C   1 
ATOM   3631 O O   . GLY B 1 174 ? -21.209 -30.044 -2.992  1.00   40.28  ? 174  GLY B O   1 
ATOM   3632 N N   . ALA B 1 175 ? -22.086 -29.511 -0.985  1.00   40.12  ? 175  ALA B N   1 
ATOM   3633 C CA  . ALA B 1 175 ? -23.477 -29.528 -1.439  1.00   40.15  ? 175  ALA B CA  1 
ATOM   3634 C C   . ALA B 1 175 ? -23.725 -28.650 -2.664  1.00   40.51  ? 175  ALA B C   1 
ATOM   3635 O O   . ALA B 1 175 ? -24.261 -29.121 -3.676  1.00   40.83  ? 175  ALA B O   1 
ATOM   3636 C CB  . ALA B 1 175 ? -24.408 -29.129 -0.308  1.00   39.98  ? 175  ALA B CB  1 
ATOM   3637 N N   . LYS B 1 176 ? -23.326 -27.378 -2.571  0.56   40.37  ? 176  LYS B N   1 
ATOM   3638 C CA  . LYS B 1 176 ? -23.555 -26.419 -3.651  0.56   40.28  ? 176  LYS B CA  1 
ATOM   3639 C C   . LYS B 1 176 ? -22.909 -26.880 -4.944  0.56   40.05  ? 176  LYS B C   1 
ATOM   3640 O O   . LYS B 1 176 ? -23.470 -26.711 -6.023  0.56   39.84  ? 176  LYS B O   1 
ATOM   3641 C CB  . LYS B 1 176 ? -23.056 -25.023 -3.260  0.56   40.24  ? 176  LYS B CB  1 
ATOM   3642 C CG  . LYS B 1 176 ? -24.070 -24.238 -2.459  0.56   40.50  ? 176  LYS B CG  1 
ATOM   3643 C CD  . LYS B 1 176 ? -23.698 -22.765 -2.342  0.56   41.65  ? 176  LYS B CD  1 
ATOM   3644 C CE  . LYS B 1 176 ? -24.928 -21.862 -2.490  0.56   41.63  ? 176  LYS B CE  1 
ATOM   3645 N NZ  . LYS B 1 176 ? -26.134 -22.341 -1.712  0.56   41.67  ? 176  LYS B NZ  1 
ATOM   3646 N N   . ARG B 1 177 ? -21.735 -27.489 -4.812  1.00   40.01  ? 177  ARG B N   1 
ATOM   3647 C CA  . ARG B 1 177 ? -20.978 -28.006 -5.942  1.00   40.10  ? 177  ARG B CA  1 
ATOM   3648 C C   . ARG B 1 177 ? -21.668 -29.188 -6.641  1.00   39.48  ? 177  ARG B C   1 
ATOM   3649 O O   . ARG B 1 177 ? -21.715 -29.230 -7.878  1.00   39.38  ? 177  ARG B O   1 
ATOM   3650 C CB  . ARG B 1 177 ? -19.577 -28.411 -5.473  1.00   40.54  ? 177  ARG B CB  1 
ATOM   3651 C CG  . ARG B 1 177 ? -18.682 -28.983 -6.546  1.00   42.25  ? 177  ARG B CG  1 
ATOM   3652 C CD  . ARG B 1 177 ? -17.340 -29.454 -5.960  1.00   45.47  ? 177  ARG B CD  1 
ATOM   3653 N NE  . ARG B 1 177 ? -16.538 -28.355 -5.418  1.00   46.89  ? 177  ARG B NE  1 
ATOM   3654 C CZ  . ARG B 1 177 ? -15.816 -27.505 -6.152  1.00   48.14  ? 177  ARG B CZ  1 
ATOM   3655 N NH1 . ARG B 1 177 ? -15.786 -27.614 -7.475  1.00   47.75  ? 177  ARG B NH1 1 
ATOM   3656 N NH2 . ARG B 1 177 ? -15.118 -26.539 -5.558  1.00   48.23  ? 177  ARG B NH2 1 
ATOM   3657 N N   . VAL B 1 178 ? -22.189 -30.146 -5.869  1.00   38.43  ? 178  VAL B N   1 
ATOM   3658 C CA  . VAL B 1 178 ? -22.885 -31.289 -6.489  1.00   37.74  ? 178  VAL B CA  1 
ATOM   3659 C C   . VAL B 1 178 ? -24.276 -30.931 -7.014  1.00   37.39  ? 178  VAL B C   1 
ATOM   3660 O O   . VAL B 1 178 ? -24.655 -31.400 -8.078  1.00   36.88  ? 178  VAL B O   1 
ATOM   3661 C CB  . VAL B 1 178 ? -22.939 -32.584 -5.611  1.00   37.29  ? 178  VAL B CB  1 
ATOM   3662 C CG1 . VAL B 1 178 ? -21.534 -33.047 -5.243  1.00   37.58  ? 178  VAL B CG1 1 
ATOM   3663 C CG2 . VAL B 1 178 ? -23.823 -32.420 -4.388  1.00   37.39  ? 178  VAL B CG2 1 
ATOM   3664 N N   . THR B 1 179 ? -25.028 -30.108 -6.279  1.00   37.36  ? 179  THR B N   1 
ATOM   3665 C CA  . THR B 1 179 ? -26.346 -29.662 -6.767  1.00   37.54  ? 179  THR B CA  1 
ATOM   3666 C C   . THR B 1 179 ? -26.210 -28.955 -8.113  1.00   37.47  ? 179  THR B C   1 
ATOM   3667 O O   . THR B 1 179 ? -27.084 -29.054 -8.964  1.00   37.48  ? 179  THR B O   1 
ATOM   3668 C CB  . THR B 1 179 ? -27.091 -28.733 -5.774  1.00   37.92  ? 179  THR B CB  1 
ATOM   3669 O OG1 . THR B 1 179 ? -26.288 -27.580 -5.471  1.00   37.92  ? 179  THR B OG1 1 
ATOM   3670 C CG2 . THR B 1 179 ? -27.448 -29.482 -4.489  1.00   37.27  ? 179  THR B CG2 1 
ATOM   3671 N N   . SER B 1 180 ? -25.092 -28.264 -8.301  1.00   37.54  ? 180  SER B N   1 
ATOM   3672 C CA  . SER B 1 180 ? -24.839 -27.545 -9.539  1.00   37.30  ? 180  SER B CA  1 
ATOM   3673 C C   . SER B 1 180 ? -24.629 -28.503 -10.711 1.00   36.92  ? 180  SER B C   1 
ATOM   3674 O O   . SER B 1 180 ? -25.172 -28.289 -11.792 1.00   36.36  ? 180  SER B O   1 
ATOM   3675 C CB  . SER B 1 180 ? -23.627 -26.626 -9.375  1.00   37.47  ? 180  SER B CB  1 
ATOM   3676 O OG  . SER B 1 180 ? -23.483 -25.793 -10.516 1.00   38.02  ? 180  SER B OG  1 
ATOM   3677 N N   . ILE B 1 181 ? -23.836 -29.553 -10.488 1.00   36.76  ? 181  ILE B N   1 
ATOM   3678 C CA  . ILE B 1 181 ? -23.627 -30.586 -11.505 1.00   36.79  ? 181  ILE B CA  1 
ATOM   3679 C C   . ILE B 1 181 ? -24.928 -31.360 -11.738 1.00   36.77  ? 181  ILE B C   1 
ATOM   3680 O O   . ILE B 1 181 ? -25.317 -31.611 -12.883 1.00   36.37  ? 181  ILE B O   1 
ATOM   3681 C CB  . ILE B 1 181 ? -22.432 -31.514 -11.140 1.00   37.06  ? 181  ILE B CB  1 
ATOM   3682 C CG1 . ILE B 1 181 ? -21.112 -30.721 -11.216 1.00   37.16  ? 181  ILE B CG1 1 
ATOM   3683 C CG2 . ILE B 1 181 ? -22.368 -32.735 -12.067 1.00   36.16  ? 181  ILE B CG2 1 
ATOM   3684 C CD1 . ILE B 1 181 ? -19.927 -31.408 -10.572 1.00   38.58  ? 181  ILE B CD1 1 
ATOM   3685 N N   . ALA B 1 182 ? -25.612 -31.703 -10.648 1.00   37.04  ? 182  ALA B N   1 
ATOM   3686 C CA  . ALA B 1 182 ? -26.892 -32.405 -10.731 1.00   37.60  ? 182  ALA B CA  1 
ATOM   3687 C C   . ALA B 1 182 ? -27.894 -31.643 -11.597 1.00   37.92  ? 182  ALA B C   1 
ATOM   3688 O O   . ALA B 1 182 ? -28.517 -32.223 -12.485 1.00   37.38  ? 182  ALA B O   1 
ATOM   3689 C CB  . ALA B 1 182 ? -27.462 -32.658 -9.359  1.00   37.14  ? 182  ALA B CB  1 
ATOM   3690 N N   . ASP B 1 183 ? -28.019 -30.340 -11.352 0.93   38.66  ? 183  ASP B N   1 
ATOM   3691 C CA  . ASP B 1 183 ? -28.980 -29.514 -12.085 0.93   39.74  ? 183  ASP B CA  1 
ATOM   3692 C C   . ASP B 1 183 ? -28.659 -29.436 -13.569 0.93   39.94  ? 183  ASP B C   1 
ATOM   3693 O O   . ASP B 1 183 ? -29.562 -29.539 -14.408 0.93   40.00  ? 183  ASP B O   1 
ATOM   3694 C CB  . ASP B 1 183 ? -29.099 -28.122 -11.458 0.93   39.90  ? 183  ASP B CB  1 
ATOM   3695 C CG  . ASP B 1 183 ? -29.812 -28.154 -10.117 0.93   41.68  ? 183  ASP B CG  1 
ATOM   3696 O OD1 . ASP B 1 183 ? -30.461 -29.188 -9.810  0.93   42.96  ? 183  ASP B OD1 1 
ATOM   3697 O OD2 . ASP B 1 183 ? -29.724 -27.156 -9.363  0.93   42.55  ? 183  ASP B OD2 1 
ATOM   3698 N N   . ARG B 1 184 ? -27.375 -29.297 -13.892 1.00   40.47  ? 184  ARG B N   1 
ATOM   3699 C CA  . ARG B 1 184 ? -26.951 -29.225 -15.292 1.00   41.20  ? 184  ARG B CA  1 
ATOM   3700 C C   . ARG B 1 184 ? -27.185 -30.524 -16.052 1.00   41.00  ? 184  ARG B C   1 
ATOM   3701 O O   . ARG B 1 184 ? -27.591 -30.498 -17.217 1.00   41.20  ? 184  ARG B O   1 
ATOM   3702 C CB  . ARG B 1 184 ? -25.495 -28.775 -15.410 1.00   41.59  ? 184  ARG B CB  1 
ATOM   3703 C CG  . ARG B 1 184 ? -25.317 -27.304 -15.043 1.00   44.20  ? 184  ARG B CG  1 
ATOM   3704 C CD  . ARG B 1 184 ? -24.057 -26.688 -15.647 1.00   48.93  ? 184  ARG B CD  1 
ATOM   3705 N NE  . ARG B 1 184 ? -23.913 -25.284 -15.245 1.00   52.91  ? 184  ARG B NE  1 
ATOM   3706 C CZ  . ARG B 1 184 ? -23.625 -24.875 -14.008 1.00   53.99  ? 184  ARG B CZ  1 
ATOM   3707 N NH1 . ARG B 1 184 ? -23.445 -25.754 -13.029 1.00   54.64  ? 184  ARG B NH1 1 
ATOM   3708 N NH2 . ARG B 1 184 ? -23.521 -23.581 -13.745 1.00   55.01  ? 184  ARG B NH2 1 
ATOM   3709 N N   . LEU B 1 185 ? -26.933 -31.652 -15.391 1.00   40.63  ? 185  LEU B N   1 
ATOM   3710 C CA  . LEU B 1 185 ? -27.168 -32.965 -15.984 1.00   40.46  ? 185  LEU B CA  1 
ATOM   3711 C C   . LEU B 1 185 ? -28.636 -33.383 -15.882 1.00   40.65  ? 185  LEU B C   1 
ATOM   3712 O O   . LEU B 1 185 ? -29.034 -34.388 -16.465 1.00   40.65  ? 185  LEU B O   1 
ATOM   3713 C CB  . LEU B 1 185 ? -26.280 -34.023 -15.318 1.00   40.19  ? 185  LEU B CB  1 
ATOM   3714 C CG  . LEU B 1 185 ? -24.763 -33.947 -15.558 1.00   40.03  ? 185  LEU B CG  1 
ATOM   3715 C CD1 . LEU B 1 185 ? -23.999 -34.996 -14.739 1.00   39.54  ? 185  LEU B CD1 1 
ATOM   3716 C CD2 . LEU B 1 185 ? -24.424 -34.076 -17.038 1.00   38.40  ? 185  LEU B CD2 1 
ATOM   3717 N N   . ASN B 1 186 ? -29.426 -32.603 -15.141 1.00   40.76  ? 186  ASN B N   1 
ATOM   3718 C CA  . ASN B 1 186 ? -30.816 -32.945 -14.794 1.00   41.00  ? 186  ASN B CA  1 
ATOM   3719 C C   . ASN B 1 186 ? -30.950 -34.319 -14.138 1.00   40.41  ? 186  ASN B C   1 
ATOM   3720 O O   . ASN B 1 186 ? -31.690 -35.190 -14.615 1.00   40.62  ? 186  ASN B O   1 
ATOM   3721 C CB  . ASN B 1 186 ? -31.762 -32.813 -15.999 1.00   41.12  ? 186  ASN B CB  1 
ATOM   3722 C CG  . ASN B 1 186 ? -33.222 -32.708 -15.580 1.00   43.46  ? 186  ASN B CG  1 
ATOM   3723 O OD1 . ASN B 1 186 ? -34.088 -33.400 -16.125 1.00   46.22  ? 186  ASN B OD1 1 
ATOM   3724 N ND2 . ASN B 1 186 ? -33.500 -31.855 -14.589 1.00   43.95  ? 186  ASN B ND2 1 
ATOM   3725 N N   . VAL B 1 187 ? -30.222 -34.512 -13.045 1.00   39.62  ? 187  VAL B N   1 
ATOM   3726 C CA  . VAL B 1 187 ? -30.252 -35.783 -12.316 1.00   38.98  ? 187  VAL B CA  1 
ATOM   3727 C C   . VAL B 1 187 ? -30.392 -35.532 -10.814 1.00   38.29  ? 187  VAL B C   1 
ATOM   3728 O O   . VAL B 1 187 ? -30.560 -34.393 -10.385 1.00   38.27  ? 187  VAL B O   1 
ATOM   3729 C CB  . VAL B 1 187 ? -28.984 -36.627 -12.607 1.00   39.05  ? 187  VAL B CB  1 
ATOM   3730 C CG1 . VAL B 1 187 ? -28.956 -37.075 -14.066 1.00   39.06  ? 187  VAL B CG1 1 
ATOM   3731 C CG2 . VAL B 1 187 ? -27.711 -35.834 -12.262 1.00   38.66  ? 187  VAL B CG2 1 
ATOM   3732 N N   . ASP B 1 188 ? -30.302 -36.594 -10.018 1.00   37.77  ? 188  ASP B N   1 
ATOM   3733 C CA  . ASP B 1 188 ? -30.406 -36.475 -8.564  1.00   37.37  ? 188  ASP B CA  1 
ATOM   3734 C C   . ASP B 1 188 ? -29.078 -36.145 -7.905  1.00   36.33  ? 188  ASP B C   1 
ATOM   3735 O O   . ASP B 1 188 ? -28.018 -36.277 -8.514  1.00   36.40  ? 188  ASP B O   1 
ATOM   3736 C CB  . ASP B 1 188 ? -30.990 -37.753 -7.968  1.00   38.00  ? 188  ASP B CB  1 
ATOM   3737 C CG  . ASP B 1 188 ? -32.414 -37.994 -8.410  1.00   39.98  ? 188  ASP B CG  1 
ATOM   3738 O OD1 . ASP B 1 188 ? -33.155 -37.005 -8.592  1.00   42.17  ? 188  ASP B OD1 1 
ATOM   3739 O OD2 . ASP B 1 188 ? -32.792 -39.168 -8.580  1.00   42.49  ? 188  ASP B OD2 1 
ATOM   3740 N N   . PHE B 1 189 ? -29.143 -35.696 -6.659  1.00   35.42  ? 189  PHE B N   1 
ATOM   3741 C CA  . PHE B 1 189 ? -27.938 -35.484 -5.873  1.00   34.89  ? 189  PHE B CA  1 
ATOM   3742 C C   . PHE B 1 189 ? -28.166 -36.117 -4.515  1.00   34.27  ? 189  PHE B C   1 
ATOM   3743 O O   . PHE B 1 189 ? -29.312 -36.352 -4.110  1.00   33.58  ? 189  PHE B O   1 
ATOM   3744 C CB  . PHE B 1 189 ? -27.590 -33.992 -5.739  1.00   35.06  ? 189  PHE B CB  1 
ATOM   3745 C CG  . PHE B 1 189 ? -28.447 -33.272 -4.758  1.00   36.04  ? 189  PHE B CG  1 
ATOM   3746 C CD1 . PHE B 1 189 ? -28.046 -33.147 -3.428  1.00   37.66  ? 189  PHE B CD1 1 
ATOM   3747 C CD2 . PHE B 1 189 ? -29.678 -32.755 -5.142  1.00   37.14  ? 189  PHE B CD2 1 
ATOM   3748 C CE1 . PHE B 1 189 ? -28.851 -32.501 -2.504  1.00   37.81  ? 189  PHE B CE1 1 
ATOM   3749 C CE2 . PHE B 1 189 ? -30.494 -32.106 -4.215  1.00   38.30  ? 189  PHE B CE2 1 
ATOM   3750 C CZ  . PHE B 1 189 ? -30.073 -31.981 -2.896  1.00   38.08  ? 189  PHE B CZ  1 
ATOM   3751 N N   . ALA B 1 190 ? -27.063 -36.411 -3.836  1.00   33.29  ? 190  ALA B N   1 
ATOM   3752 C CA  . ALA B 1 190 ? -27.091 -36.947 -2.492  1.00   33.36  ? 190  ALA B CA  1 
ATOM   3753 C C   . ALA B 1 190 ? -25.913 -36.361 -1.722  1.00   33.23  ? 190  ALA B C   1 
ATOM   3754 O O   . ALA B 1 190 ? -24.991 -35.789 -2.309  1.00   32.49  ? 190  ALA B O   1 
ATOM   3755 C CB  . ALA B 1 190 ? -27.026 -38.489 -2.518  1.00   32.52  ? 190  ALA B CB  1 
ATOM   3756 N N   . LEU B 1 191 ? -25.953 -36.499 -0.406  1.00   34.25  ? 191  LEU B N   1 
ATOM   3757 C CA  . LEU B 1 191 ? -24.893 -35.968 0.437   1.00   35.02  ? 191  LEU B CA  1 
ATOM   3758 C C   . LEU B 1 191 ? -24.538 -36.938 1.558   1.00   35.24  ? 191  LEU B C   1 
ATOM   3759 O O   . LEU B 1 191 ? -25.411 -37.494 2.220   1.00   35.18  ? 191  LEU B O   1 
ATOM   3760 C CB  . LEU B 1 191 ? -25.308 -34.605 0.992   1.00   35.75  ? 191  LEU B CB  1 
ATOM   3761 C CG  . LEU B 1 191 ? -24.275 -33.821 1.799   1.00   36.83  ? 191  LEU B CG  1 
ATOM   3762 C CD1 . LEU B 1 191 ? -24.265 -32.373 1.352   1.00   37.71  ? 191  LEU B CD1 1 
ATOM   3763 C CD2 . LEU B 1 191 ? -24.565 -33.960 3.296   1.00   37.29  ? 191  LEU B CD2 1 
ATOM   3764 N N   . ILE B 1 192 ? -23.244 -37.136 1.751   1.00   35.89  ? 192  ILE B N   1 
ATOM   3765 C CA  . ILE B 1 192 ? -22.726 -37.903 2.874   1.00   36.93  ? 192  ILE B CA  1 
ATOM   3766 C C   . ILE B 1 192 ? -22.174 -36.957 3.940   1.00   37.59  ? 192  ILE B C   1 
ATOM   3767 O O   . ILE B 1 192 ? -21.483 -35.986 3.630   1.00   38.23  ? 192  ILE B O   1 
ATOM   3768 C CB  . ILE B 1 192 ? -21.643 -38.914 2.398   1.00   36.89  ? 192  ILE B CB  1 
ATOM   3769 C CG1 . ILE B 1 192 ? -22.310 -40.143 1.777   1.00   37.45  ? 192  ILE B CG1 1 
ATOM   3770 C CG2 . ILE B 1 192 ? -20.762 -39.378 3.550   1.00   37.03  ? 192  ILE B CG2 1 
ATOM   3771 C CD1 . ILE B 1 192 ? -21.551 -40.739 0.609   1.00   37.71  ? 192  ILE B CD1 1 
ATOM   3772 N N   . HIS B 1 193 ? -22.492 -37.235 5.198   1.00   38.65  ? 193  HIS B N   1 
ATOM   3773 C CA  . HIS B 1 193 ? -21.956 -36.460 6.311   1.00   39.64  ? 193  HIS B CA  1 
ATOM   3774 C C   . HIS B 1 193 ? -21.341 -37.404 7.336   1.00   40.25  ? 193  HIS B C   1 
ATOM   3775 O O   . HIS B 1 193 ? -21.993 -38.348 7.784   1.00   39.95  ? 193  HIS B O   1 
ATOM   3776 C CB  . HIS B 1 193 ? -23.044 -35.577 6.948   1.00   39.71  ? 193  HIS B CB  1 
ATOM   3777 C CG  . HIS B 1 193 ? -22.664 -35.012 8.285   1.00   40.08  ? 193  HIS B CG  1 
ATOM   3778 N ND1 . HIS B 1 193 ? -21.561 -34.202 8.468   1.00   41.12  ? 193  HIS B ND1 1 
ATOM   3779 C CD2 . HIS B 1 193 ? -23.237 -35.147 9.506   1.00   40.77  ? 193  HIS B CD2 1 
ATOM   3780 C CE1 . HIS B 1 193 ? -21.471 -33.862 9.743   1.00   41.62  ? 193  HIS B CE1 1 
ATOM   3781 N NE2 . HIS B 1 193 ? -22.475 -34.425 10.395  1.00   41.51  ? 193  HIS B NE2 1 
ATOM   3782 N N   . LYS B 1 194 ? -20.081 -37.160 7.683   0.60   41.10  ? 194  LYS B N   1 
ATOM   3783 C CA  . LYS B 1 194 ? -19.418 -37.943 8.716   0.60   42.35  ? 194  LYS B CA  1 
ATOM   3784 C C   . LYS B 1 194 ? -19.667 -37.323 10.089  0.60   43.24  ? 194  LYS B C   1 
ATOM   3785 O O   . LYS B 1 194 ? -19.399 -36.141 10.311  0.60   43.09  ? 194  LYS B O   1 
ATOM   3786 C CB  . LYS B 1 194 ? -17.914 -38.081 8.439   0.60   42.28  ? 194  LYS B CB  1 
ATOM   3787 C CG  . LYS B 1 194 ? -17.184 -38.955 9.454   0.60   42.60  ? 194  LYS B CG  1 
ATOM   3788 C CD  . LYS B 1 194 ? -15.933 -39.608 8.870   0.60   42.90  ? 194  LYS B CD  1 
ATOM   3789 C CE  . LYS B 1 194 ? -15.478 -40.764 9.759   0.60   43.35  ? 194  LYS B CE  1 
ATOM   3790 N NZ  . LYS B 1 194 ? -14.402 -41.603 9.140   0.60   43.78  ? 194  LYS B NZ  1 
ATOM   3791 N N   . GLU B 1 195 ? -20.187 -38.139 11.000  1.00   44.64  ? 195  GLU B N   1 
ATOM   3792 C CA  . GLU B 1 195 ? -20.480 -37.713 12.374  1.00   46.16  ? 195  GLU B CA  1 
ATOM   3793 C C   . GLU B 1 195 ? -19.268 -37.870 13.297  1.00   46.32  ? 195  GLU B C   1 
ATOM   3794 O O   . GLU B 1 195 ? -18.118 -37.883 12.841  1.00   46.92  ? 195  GLU B O   1 
ATOM   3795 C CB  . GLU B 1 195 ? -21.654 -38.519 12.929  1.00   46.41  ? 195  GLU B CB  1 
ATOM   3796 C CG  . GLU B 1 195 ? -22.982 -38.206 12.265  1.00   48.16  ? 195  GLU B CG  1 
ATOM   3797 C CD  . GLU B 1 195 ? -24.030 -39.264 12.540  1.00   51.33  ? 195  GLU B CD  1 
ATOM   3798 O OE1 . GLU B 1 195 ? -23.729 -40.471 12.366  1.00   53.43  ? 195  GLU B OE1 1 
ATOM   3799 O OE2 . GLU B 1 195 ? -25.162 -38.890 12.922  1.00   52.08  ? 195  GLU B OE2 1 
ATOM   3800 N N   . ASP B 1 203 ? -18.126 -41.166 14.482  0.59   47.45  ? 203  ASP B N   1 
ATOM   3801 C CA  . ASP B 1 203 ? -17.208 -41.882 13.587  0.59   47.29  ? 203  ASP B CA  1 
ATOM   3802 C C   . ASP B 1 203 ? -17.979 -42.689 12.534  0.59   47.02  ? 203  ASP B C   1 
ATOM   3803 O O   . ASP B 1 203 ? -17.505 -43.727 12.057  0.59   47.40  ? 203  ASP B O   1 
ATOM   3804 C CB  . ASP B 1 203 ? -16.277 -42.800 14.398  0.59   47.39  ? 203  ASP B CB  1 
ATOM   3805 C CG  . ASP B 1 203 ? -14.936 -43.052 13.705  0.59   47.91  ? 203  ASP B CG  1 
ATOM   3806 O OD1 . ASP B 1 203 ? -14.849 -42.929 12.460  0.59   47.61  ? 203  ASP B OD1 1 
ATOM   3807 O OD2 . ASP B 1 203 ? -13.962 -43.381 14.421  0.59   48.78  ? 203  ASP B OD2 1 
ATOM   3808 N N   . ARG B 1 204 ? -19.166 -42.200 12.173  0.74   46.44  ? 204  ARG B N   1 
ATOM   3809 C CA  . ARG B 1 204 ? -20.001 -42.853 11.169  0.74   45.91  ? 204  ARG B CA  1 
ATOM   3810 C C   . ARG B 1 204 ? -20.507 -41.888 10.104  0.74   45.01  ? 204  ARG B C   1 
ATOM   3811 O O   . ARG B 1 204 ? -20.676 -40.699 10.352  0.74   44.87  ? 204  ARG B O   1 
ATOM   3812 C CB  . ARG B 1 204 ? -21.185 -43.561 11.829  0.74   46.12  ? 204  ARG B CB  1 
ATOM   3813 C CG  . ARG B 1 204 ? -20.888 -44.984 12.302  0.74   47.41  ? 204  ARG B CG  1 
ATOM   3814 C CD  . ARG B 1 204 ? -20.625 -45.960 11.140  0.74   49.01  ? 204  ARG B CD  1 
ATOM   3815 N NE  . ARG B 1 204 ? -21.759 -46.230 10.234  0.74   50.29  ? 204  ARG B NE  1 
ATOM   3816 C CZ  . ARG B 1 204 ? -23.058 -46.229 10.558  0.74   50.76  ? 204  ARG B CZ  1 
ATOM   3817 N NH1 . ARG B 1 204 ? -23.470 -45.960 11.796  0.74   51.66  ? 204  ARG B NH1 1 
ATOM   3818 N NH2 . ARG B 1 204 ? -23.963 -46.497 9.621   0.74   50.56  ? 204  ARG B NH2 1 
ATOM   3819 N N   . MET B 1 205 ? -20.752 -42.426 8.916   1.00   44.23  ? 205  MET B N   1 
ATOM   3820 C CA  . MET B 1 205 ? -21.274 -41.643 7.809   1.00   43.42  ? 205  MET B CA  1 
ATOM   3821 C C   . MET B 1 205 ? -22.780 -41.781 7.724   1.00   42.99  ? 205  MET B C   1 
ATOM   3822 O O   . MET B 1 205 ? -23.332 -42.869 7.935   1.00   43.34  ? 205  MET B O   1 
ATOM   3823 C CB  . MET B 1 205 ? -20.650 -42.098 6.489   1.00   43.14  ? 205  MET B CB  1 
ATOM   3824 C CG  . MET B 1 205 ? -19.197 -41.739 6.335   1.00   42.87  ? 205  MET B CG  1 
ATOM   3825 S SD  . MET B 1 205 ? -18.565 -42.204 4.715   1.00   40.53  ? 205  MET B SD  1 
ATOM   3826 C CE  . MET B 1 205 ? -17.182 -41.049 4.554   1.00   41.76  ? 205  MET B CE  1 
ATOM   3827 N N   . VAL B 1 206 ? -23.443 -40.673 7.421   1.00   41.91  ? 206  VAL B N   1 
ATOM   3828 C CA  . VAL B 1 206 ? -24.866 -40.703 7.122   1.00   41.04  ? 206  VAL B CA  1 
ATOM   3829 C C   . VAL B 1 206 ? -25.085 -40.173 5.716   1.00   40.19  ? 206  VAL B C   1 
ATOM   3830 O O   . VAL B 1 206 ? -24.436 -39.214 5.282   1.00   39.89  ? 206  VAL B O   1 
ATOM   3831 C CB  . VAL B 1 206 ? -25.715 -39.899 8.133   1.00   41.26  ? 206  VAL B CB  1 
ATOM   3832 C CG1 . VAL B 1 206 ? -25.704 -40.570 9.511   1.00   41.61  ? 206  VAL B CG1 1 
ATOM   3833 C CG2 . VAL B 1 206 ? -25.237 -38.476 8.234   1.00   41.85  ? 206  VAL B CG2 1 
ATOM   3834 N N   . LEU B 1 207 ? -25.997 -40.816 5.006   1.00   39.23  ? 207  LEU B N   1 
ATOM   3835 C CA  . LEU B 1 207 ? -26.300 -40.452 3.644   1.00   38.44  ? 207  LEU B CA  1 
ATOM   3836 C C   . LEU B 1 207 ? -27.735 -39.961 3.553   1.00   38.15  ? 207  LEU B C   1 
ATOM   3837 O O   . LEU B 1 207 ? -28.664 -40.623 4.034   1.00   37.77  ? 207  LEU B O   1 
ATOM   3838 C CB  . LEU B 1 207 ? -26.073 -41.653 2.722   1.00   38.35  ? 207  LEU B CB  1 
ATOM   3839 C CG  . LEU B 1 207 ? -26.515 -41.583 1.255   1.00   37.98  ? 207  LEU B CG  1 
ATOM   3840 C CD1 . LEU B 1 207 ? -25.680 -40.615 0.427   1.00   36.38  ? 207  LEU B CD1 1 
ATOM   3841 C CD2 . LEU B 1 207 ? -26.451 -42.967 0.648   1.00   36.60  ? 207  LEU B CD2 1 
ATOM   3842 N N   . VAL B 1 208 ? -27.897 -38.783 2.955   1.00   37.55  ? 208  VAL B N   1 
ATOM   3843 C CA  . VAL B 1 208 ? -29.212 -38.257 2.601   1.00   37.12  ? 208  VAL B CA  1 
ATOM   3844 C C   . VAL B 1 208 ? -29.349 -38.150 1.086   1.00   36.97  ? 208  VAL B C   1 
ATOM   3845 O O   . VAL B 1 208 ? -28.494 -37.567 0.410   1.00   37.09  ? 208  VAL B O   1 
ATOM   3846 C CB  . VAL B 1 208 ? -29.509 -36.883 3.268   1.00   36.82  ? 208  VAL B CB  1 
ATOM   3847 C CG1 . VAL B 1 208 ? -29.653 -37.049 4.768   1.00   37.37  ? 208  VAL B CG1 1 
ATOM   3848 C CG2 . VAL B 1 208 ? -28.433 -35.848 2.939   1.00   36.52  ? 208  VAL B CG2 1 
ATOM   3849 N N   . GLY B 1 209 ? -30.429 -38.710 0.560   1.00   36.91  ? 209  GLY B N   1 
ATOM   3850 C CA  . GLY B 1 209 ? -30.681 -38.702 -0.878  1.00   37.31  ? 209  GLY B CA  1 
ATOM   3851 C C   . GLY B 1 209 ? -30.670 -40.103 -1.453  1.00   37.62  ? 209  GLY B C   1 
ATOM   3852 O O   . GLY B 1 209 ? -29.995 -40.987 -0.934  1.00   37.79  ? 209  GLY B O   1 
ATOM   3853 N N   . ASP B 1 210 ? -31.409 -40.302 -2.538  0.78   38.17  ? 210  ASP B N   1 
ATOM   3854 C CA  . ASP B 1 210 ? -31.555 -41.631 -3.117  0.78   38.64  ? 210  ASP B CA  1 
ATOM   3855 C C   . ASP B 1 210 ? -30.468 -41.967 -4.129  0.78   37.79  ? 210  ASP B C   1 
ATOM   3856 O O   . ASP B 1 210 ? -30.226 -41.217 -5.077  0.78   37.82  ? 210  ASP B O   1 
ATOM   3857 C CB  . ASP B 1 210 ? -32.941 -41.809 -3.749  0.78   39.34  ? 210  ASP B CB  1 
ATOM   3858 C CG  . ASP B 1 210 ? -33.286 -43.273 -3.978  0.78   41.36  ? 210  ASP B CG  1 
ATOM   3859 O OD1 . ASP B 1 210 ? -33.485 -43.663 -5.147  0.78   43.84  ? 210  ASP B OD1 1 
ATOM   3860 O OD2 . ASP B 1 210 ? -33.333 -44.039 -2.986  0.78   44.39  ? 210  ASP B OD2 1 
ATOM   3861 N N   . VAL B 1 211 ? -29.816 -43.102 -3.901  1.00   37.24  ? 211  VAL B N   1 
ATOM   3862 C CA  . VAL B 1 211 ? -28.828 -43.635 -4.824  1.00   36.96  ? 211  VAL B CA  1 
ATOM   3863 C C   . VAL B 1 211 ? -29.172 -45.062 -5.276  1.00   36.67  ? 211  VAL B C   1 
ATOM   3864 O O   . VAL B 1 211 ? -28.451 -45.633 -6.096  1.00   35.81  ? 211  VAL B O   1 
ATOM   3865 C CB  . VAL B 1 211 ? -27.398 -43.633 -4.217  1.00   37.04  ? 211  VAL B CB  1 
ATOM   3866 C CG1 . VAL B 1 211 ? -26.905 -42.202 -3.938  1.00   37.35  ? 211  VAL B CG1 1 
ATOM   3867 C CG2 . VAL B 1 211 ? -27.339 -44.494 -2.965  1.00   36.67  ? 211  VAL B CG2 1 
ATOM   3868 N N   . LYS B 1 212 ? -30.257 -45.624 -4.727  0.87   36.50  ? 212  LYS B N   1 
ATOM   3869 C CA  . LYS B 1 212 ? -30.628 -47.026 -4.966  0.87   37.23  ? 212  LYS B CA  1 
ATOM   3870 C C   . LYS B 1 212 ? -30.777 -47.335 -6.453  0.87   36.83  ? 212  LYS B C   1 
ATOM   3871 O O   . LYS B 1 212 ? -31.501 -46.644 -7.168  0.87   36.53  ? 212  LYS B O   1 
ATOM   3872 C CB  . LYS B 1 212 ? -31.912 -47.400 -4.214  0.87   37.51  ? 212  LYS B CB  1 
ATOM   3873 C CG  . LYS B 1 212 ? -32.204 -48.912 -4.169  0.87   39.64  ? 212  LYS B CG  1 
ATOM   3874 C CD  . LYS B 1 212 ? -33.530 -49.214 -3.466  0.87   42.91  ? 212  LYS B CD  1 
ATOM   3875 C CE  . LYS B 1 212 ? -33.892 -50.711 -3.530  0.87   45.83  ? 212  LYS B CE  1 
ATOM   3876 N NZ  . LYS B 1 212 ? -33.328 -51.542 -2.405  0.87   46.90  ? 212  LYS B NZ  1 
ATOM   3877 N N   . ASP B 1 213 ? -30.061 -48.365 -6.899  1.00   37.07  ? 213  ASP B N   1 
ATOM   3878 C CA  . ASP B 1 213 ? -30.097 -48.848 -8.286  1.00   37.66  ? 213  ASP B CA  1 
ATOM   3879 C C   . ASP B 1 213 ? -29.684 -47.819 -9.338  1.00   36.99  ? 213  ASP B C   1 
ATOM   3880 O O   . ASP B 1 213 ? -30.037 -47.948 -10.511 1.00   37.45  ? 213  ASP B O   1 
ATOM   3881 C CB  . ASP B 1 213 ? -31.469 -49.446 -8.629  1.00   38.19  ? 213  ASP B CB  1 
ATOM   3882 C CG  . ASP B 1 213 ? -31.793 -50.679 -7.799  1.00   40.56  ? 213  ASP B CG  1 
ATOM   3883 O OD1 . ASP B 1 213 ? -32.969 -50.832 -7.399  1.00   43.70  ? 213  ASP B OD1 1 
ATOM   3884 O OD2 . ASP B 1 213 ? -30.875 -51.494 -7.546  1.00   43.65  ? 213  ASP B OD2 1 
ATOM   3885 N N   . ARG B 1 214 ? -28.943 -46.803 -8.910  1.00   36.14  ? 214  ARG B N   1 
ATOM   3886 C CA  . ARG B 1 214 ? -28.394 -45.788 -9.821  1.00   35.36  ? 214  ARG B CA  1 
ATOM   3887 C C   . ARG B 1 214 ? -26.875 -45.809 -9.739  1.00   33.78  ? 214  ARG B C   1 
ATOM   3888 O O   . ARG B 1 214 ? -26.311 -46.250 -8.733  1.00   32.67  ? 214  ARG B O   1 
ATOM   3889 C CB  . ARG B 1 214 ? -28.882 -44.389 -9.421  1.00   35.74  ? 214  ARG B CB  1 
ATOM   3890 C CG  . ARG B 1 214 ? -30.389 -44.241 -9.363  1.00   38.37  ? 214  ARG B CG  1 
ATOM   3891 C CD  . ARG B 1 214 ? -30.820 -42.892 -8.814  1.00   42.80  ? 214  ARG B CD  1 
ATOM   3892 N NE  . ARG B 1 214 ? -32.014 -42.430 -9.518  1.00   48.15  ? 214  ARG B NE  1 
ATOM   3893 C CZ  . ARG B 1 214 ? -32.037 -41.444 -10.414 1.00   48.83  ? 214  ARG B CZ  1 
ATOM   3894 N NH1 . ARG B 1 214 ? -30.934 -40.767 -10.706 1.00   50.48  ? 214  ARG B NH1 1 
ATOM   3895 N NH2 . ARG B 1 214 ? -33.180 -41.111 -10.997 1.00   49.48  ? 214  ARG B NH2 1 
ATOM   3896 N N   . VAL B 1 215 ? -26.213 -45.339 -10.792 1.00   32.42  ? 215  VAL B N   1 
ATOM   3897 C CA  . VAL B 1 215 ? -24.781 -45.079 -10.715 1.00   31.48  ? 215  VAL B CA  1 
ATOM   3898 C C   . VAL B 1 215 ? -24.586 -43.860 -9.795  1.00   31.00  ? 215  VAL B C   1 
ATOM   3899 O O   . VAL B 1 215 ? -25.331 -42.882 -9.889  1.00   31.18  ? 215  VAL B O   1 
ATOM   3900 C CB  . VAL B 1 215 ? -24.164 -44.826 -12.114 1.00   31.56  ? 215  VAL B CB  1 
ATOM   3901 C CG1 . VAL B 1 215 ? -22.752 -44.269 -11.993 1.00   30.88  ? 215  VAL B CG1 1 
ATOM   3902 C CG2 . VAL B 1 215 ? -24.175 -46.114 -12.963 1.00   31.34  ? 215  VAL B CG2 1 
ATOM   3903 N N   . ALA B 1 216 ? -23.611 -43.936 -8.894  1.00   29.97  ? 216  ALA B N   1 
ATOM   3904 C CA  . ALA B 1 216 ? -23.276 -42.809 -8.036  1.00   29.58  ? 216  ALA B CA  1 
ATOM   3905 C C   . ALA B 1 216 ? -21.938 -42.193 -8.433  1.00   29.52  ? 216  ALA B C   1 
ATOM   3906 O O   . ALA B 1 216 ? -20.948 -42.896 -8.657  1.00   29.45  ? 216  ALA B O   1 
ATOM   3907 C CB  . ALA B 1 216 ? -23.267 -43.225 -6.564  1.00   28.78  ? 216  ALA B CB  1 
ATOM   3908 N N   . ILE B 1 217 ? -21.921 -40.873 -8.535  1.00   29.29  ? 217  ILE B N   1 
ATOM   3909 C CA  . ILE B 1 217 ? -20.694 -40.163 -8.844  1.00   29.09  ? 217  ILE B CA  1 
ATOM   3910 C C   . ILE B 1 217 ? -20.345 -39.241 -7.690  1.00   29.38  ? 217  ILE B C   1 
ATOM   3911 O O   . ILE B 1 217 ? -20.997 -38.205 -7.478  1.00   29.47  ? 217  ILE B O   1 
ATOM   3912 C CB  . ILE B 1 217 ? -20.802 -39.351 -10.138 1.00   29.16  ? 217  ILE B CB  1 
ATOM   3913 C CG1 . ILE B 1 217 ? -21.373 -40.208 -11.274 1.00   29.21  ? 217  ILE B CG1 1 
ATOM   3914 C CG2 . ILE B 1 217 ? -19.420 -38.796 -10.528 1.00   28.62  ? 217  ILE B CG2 1 
ATOM   3915 C CD1 . ILE B 1 217 ? -21.634 -39.434 -12.557 1.00   29.53  ? 217  ILE B CD1 1 
ATOM   3916 N N   . LEU B 1 218 ? -19.327 -39.633 -6.935  1.00   29.49  ? 218  LEU B N   1 
ATOM   3917 C CA  . LEU B 1 218 ? -18.766 -38.763 -5.908  1.00   29.90  ? 218  LEU B CA  1 
ATOM   3918 C C   . LEU B 1 218 ? -17.984 -37.660 -6.600  1.00   30.26  ? 218  LEU B C   1 
ATOM   3919 O O   . LEU B 1 218 ? -17.091 -37.933 -7.404  1.00   29.77  ? 218  LEU B O   1 
ATOM   3920 C CB  . LEU B 1 218 ? -17.838 -39.537 -4.979  1.00   29.39  ? 218  LEU B CB  1 
ATOM   3921 C CG  . LEU B 1 218 ? -18.515 -40.382 -3.905  1.00   29.79  ? 218  LEU B CG  1 
ATOM   3922 C CD1 . LEU B 1 218 ? -17.596 -41.525 -3.449  1.00   29.99  ? 218  LEU B CD1 1 
ATOM   3923 C CD2 . LEU B 1 218 ? -18.953 -39.512 -2.719  1.00   26.71  ? 218  LEU B CD2 1 
ATOM   3924 N N   . VAL B 1 219 ? -18.356 -36.419 -6.316  1.00   30.75  ? 219  VAL B N   1 
ATOM   3925 C CA  . VAL B 1 219 ? -17.657 -35.275 -6.862  1.00   31.57  ? 219  VAL B CA  1 
ATOM   3926 C C   . VAL B 1 219 ? -17.147 -34.439 -5.705  1.00   32.56  ? 219  VAL B C   1 
ATOM   3927 O O   . VAL B 1 219 ? -17.931 -34.063 -4.825  1.00   32.88  ? 219  VAL B O   1 
ATOM   3928 C CB  . VAL B 1 219 ? -18.574 -34.429 -7.789  1.00   31.44  ? 219  VAL B CB  1 
ATOM   3929 C CG1 . VAL B 1 219 ? -17.879 -33.099 -8.169  1.00   32.10  ? 219  VAL B CG1 1 
ATOM   3930 C CG2 . VAL B 1 219 ? -18.929 -35.206 -9.035  1.00   30.82  ? 219  VAL B CG2 1 
ATOM   3931 N N   . ASP B 1 220 ? -15.834 -34.198 -5.681  1.00   33.39  ? 220  ASP B N   1 
ATOM   3932 C CA  . ASP B 1 220 ? -15.212 -33.299 -4.711  1.00   34.68  ? 220  ASP B CA  1 
ATOM   3933 C C   . ASP B 1 220 ? -14.220 -32.371 -5.443  1.00   35.07  ? 220  ASP B C   1 
ATOM   3934 O O   . ASP B 1 220 ? -13.903 -32.594 -6.619  1.00   34.14  ? 220  ASP B O   1 
ATOM   3935 C CB  . ASP B 1 220 ? -14.499 -34.110 -3.620  1.00   35.53  ? 220  ASP B CB  1 
ATOM   3936 C CG  . ASP B 1 220 ? -14.563 -33.448 -2.243  1.00   37.99  ? 220  ASP B CG  1 
ATOM   3937 O OD1 . ASP B 1 220 ? -15.541 -32.719 -1.961  1.00   41.01  ? 220  ASP B OD1 1 
ATOM   3938 O OD2 . ASP B 1 220 ? -13.637 -33.673 -1.429  1.00   40.44  ? 220  ASP B OD2 1 
ATOM   3939 N N   . ASP B 1 221 ? -13.743 -31.331 -4.762  1.00   35.24  ? 221  ASP B N   1 
ATOM   3940 C CA  . ASP B 1 221 ? -12.717 -30.465 -5.346  1.00   36.31  ? 221  ASP B CA  1 
ATOM   3941 C C   . ASP B 1 221 ? -11.339 -31.127 -5.285  1.00   36.52  ? 221  ASP B C   1 
ATOM   3942 O O   . ASP B 1 221 ? -10.512 -30.943 -6.174  1.00   35.79  ? 221  ASP B O   1 
ATOM   3943 C CB  . ASP B 1 221 ? -12.684 -29.082 -4.677  1.00   36.50  ? 221  ASP B CB  1 
ATOM   3944 C CG  . ASP B 1 221 ? -12.411 -29.156 -3.186  1.00   38.39  ? 221  ASP B CG  1 
ATOM   3945 O OD1 . ASP B 1 221 ? -13.082 -29.949 -2.487  1.00   41.36  ? 221  ASP B OD1 1 
ATOM   3946 O OD2 . ASP B 1 221 ? -11.528 -28.413 -2.704  1.00   40.64  ? 221  ASP B OD2 1 
ATOM   3947 N N   . MET B 1 222 ? -11.106 -31.903 -4.230  1.00   37.57  ? 222  MET B N   1 
ATOM   3948 C CA  . MET B 1 222 ? -9.821  -32.549 -4.031  1.00   38.68  ? 222  MET B CA  1 
ATOM   3949 C C   . MET B 1 222 ? -9.926  -33.774 -3.138  1.00   39.12  ? 222  MET B C   1 
ATOM   3950 O O   . MET B 1 222 ? -10.813 -33.859 -2.282  1.00   39.23  ? 222  MET B O   1 
ATOM   3951 C CB  . MET B 1 222 ? -8.799  -31.559 -3.445  1.00   39.03  ? 222  MET B CB  1 
ATOM   3952 C CG  . MET B 1 222 ? -8.978  -31.213 -1.970  1.00   40.72  ? 222  MET B CG  1 
ATOM   3953 S SD  . MET B 1 222 ? -7.652  -30.134 -1.359  1.00   47.85  ? 222  MET B SD  1 
ATOM   3954 C CE  . MET B 1 222 ? -8.125  -28.554 -2.079  1.00   43.85  ? 222  MET B CE  1 
ATOM   3955 N N   . ALA B 1 223 ? -9.004  -34.710 -3.345  1.00   39.59  ? 223  ALA B N   1 
ATOM   3956 C CA  . ALA B 1 223 ? -8.821  -35.832 -2.439  1.00   40.18  ? 223  ALA B CA  1 
ATOM   3957 C C   . ALA B 1 223 ? -7.365  -35.917 -2.050  1.00   40.67  ? 223  ALA B C   1 
ATOM   3958 O O   . ALA B 1 223 ? -6.472  -35.835 -2.900  1.00   40.43  ? 223  ALA B O   1 
ATOM   3959 C CB  . ALA B 1 223 ? -9.270  -37.132 -3.073  1.00   40.23  ? 223  ALA B CB  1 
ATOM   3960 N N   . ASP B 1 224 ? -7.137  -36.083 -0.753  1.00   41.38  ? 224  ASP B N   1 
ATOM   3961 C CA  . ASP B 1 224 ? -5.795  -36.244 -0.238  1.00   42.53  ? 224  ASP B CA  1 
ATOM   3962 C C   . ASP B 1 224 ? -5.325  -37.649 0.139   1.00   42.58  ? 224  ASP B C   1 
ATOM   3963 O O   . ASP B 1 224 ? -4.499  -38.235 -0.578  1.00   43.01  ? 224  ASP B O   1 
ATOM   3964 C CB  . ASP B 1 224 ? -5.573  -35.369 0.998   1.00   43.08  ? 224  ASP B CB  1 
ATOM   3965 C CG  . ASP B 1 224 ? -4.107  -35.191 1.319   1.00   44.81  ? 224  ASP B CG  1 
ATOM   3966 O OD1 . ASP B 1 224 ? -3.268  -35.689 0.531   1.00   45.05  ? 224  ASP B OD1 1 
ATOM   3967 O OD2 . ASP B 1 224 ? -3.795  -34.549 2.353   1.00   47.78  ? 224  ASP B OD2 1 
ATOM   3968 N N   . THR B 1 225 ? -5.844  -38.188 1.244   1.00   42.61  ? 225  THR B N   1 
ATOM   3969 C CA  . THR B 1 225 ? -5.440  -39.526 1.703   1.00   43.24  ? 225  THR B CA  1 
ATOM   3970 C C   . THR B 1 225 ? -6.543  -40.497 1.250   1.00   43.52  ? 225  THR B C   1 
ATOM   3971 O O   . THR B 1 225 ? -6.386  -41.715 1.350   1.00   43.97  ? 225  THR B O   1 
ATOM   3972 C CB  . THR B 1 225 ? -5.215  -39.672 3.223   1.00   43.29  ? 225  THR B CB  1 
ATOM   3973 O OG1 . THR B 1 225 ? -6.473  -39.591 3.910   1.00   43.60  ? 225  THR B OG1 1 
ATOM   3974 C CG2 . THR B 1 225 ? -4.260  -38.589 3.746   1.00   42.97  ? 225  THR B CG2 1 
ATOM   3975 N N   . CYS B 1 226 ? -7.647  -39.942 0.746   1.00   43.65  ? 226  CYS B N   1 
ATOM   3976 C CA  . CYS B 1 226 ? -8.758  -40.705 0.171   1.00   43.95  ? 226  CYS B CA  1 
ATOM   3977 C C   . CYS B 1 226 ? -9.547  -41.528 1.184   1.00   43.54  ? 226  CYS B C   1 
ATOM   3978 O O   . CYS B 1 226 ? -10.404 -42.325 0.799   1.00   43.60  ? 226  CYS B O   1 
ATOM   3979 C CB  . CYS B 1 226 ? -8.292  -41.585 -0.997  1.00   43.86  ? 226  CYS B CB  1 
ATOM   3980 S SG  . CYS B 1 226 ? -7.664  -40.647 -2.386  1.00   46.62  ? 226  CYS B SG  1 
ATOM   3981 N N   . GLY B 1 227 ? -9.268  -41.326 2.471   1.00   43.19  ? 227  GLY B N   1 
ATOM   3982 C CA  . GLY B 1 227 ? -10.018 -41.994 3.529   1.00   42.51  ? 227  GLY B CA  1 
ATOM   3983 C C   . GLY B 1 227 ? -11.506 -41.769 3.339   1.00   42.34  ? 227  GLY B C   1 
ATOM   3984 O O   . GLY B 1 227 ? -12.297 -42.717 3.397   1.00   42.17  ? 227  GLY B O   1 
ATOM   3985 N N   . THR B 1 228 ? -11.869 -40.511 3.067   1.00   41.71  ? 228  THR B N   1 
ATOM   3986 C CA  . THR B 1 228 ? -13.266 -40.084 2.958   1.00   41.16  ? 228  THR B CA  1 
ATOM   3987 C C   . THR B 1 228 ? -13.968 -40.686 1.744   1.00   40.01  ? 228  THR B C   1 
ATOM   3988 O O   . THR B 1 228 ? -14.989 -41.355 1.901   1.00   39.82  ? 228  THR B O   1 
ATOM   3989 C CB  . THR B 1 228 ? -13.395 -38.529 2.975   1.00   41.55  ? 228  THR B CB  1 
ATOM   3990 O OG1 . THR B 1 228 ? -13.018 -38.044 4.265   1.00   42.00  ? 228  THR B OG1 1 
ATOM   3991 C CG2 . THR B 1 228 ? -14.831 -38.072 2.682   1.00   41.87  ? 228  THR B CG2 1 
ATOM   3992 N N   . ILE B 1 229 ? -13.415 -40.478 0.552   1.00   38.98  ? 229  ILE B N   1 
ATOM   3993 C CA  . ILE B 1 229 ? -14.038 -41.009 -0.667  1.00   38.55  ? 229  ILE B CA  1 
ATOM   3994 C C   . ILE B 1 229 ? -14.167 -42.533 -0.666  1.00   37.65  ? 229  ILE B C   1 
ATOM   3995 O O   . ILE B 1 229 ? -15.146 -43.064 -1.184  1.00   36.64  ? 229  ILE B O   1 
ATOM   3996 C CB  . ILE B 1 229 ? -13.350 -40.530 -1.983  1.00   38.95  ? 229  ILE B CB  1 
ATOM   3997 C CG1 . ILE B 1 229 ? -11.850 -40.861 -1.975  1.00   39.18  ? 229  ILE B CG1 1 
ATOM   3998 C CG2 . ILE B 1 229 ? -13.625 -39.042 -2.210  1.00   39.02  ? 229  ILE B CG2 1 
ATOM   3999 C CD1 . ILE B 1 229 ? -11.239 -40.949 -3.359  1.00   41.14  ? 229  ILE B CD1 1 
ATOM   4000 N N   . CYS B 1 230 ? -13.187 -43.217 -0.066  1.00   37.19  ? 230  CYS B N   1 
ATOM   4001 C CA  . CYS B 1 230 ? -13.197 -44.679 0.001   1.00   37.00  ? 230  CYS B CA  1 
ATOM   4002 C C   . CYS B 1 230 ? -14.313 -45.199 0.880   1.00   35.94  ? 230  CYS B C   1 
ATOM   4003 O O   . CYS B 1 230 ? -15.010 -46.139 0.501   1.00   35.99  ? 230  CYS B O   1 
ATOM   4004 C CB  . CYS B 1 230 ? -11.845 -45.217 0.462   1.00   37.27  ? 230  CYS B CB  1 
ATOM   4005 S SG  . CYS B 1 230 ? -10.597 -45.097 -0.835  1.00   39.20  ? 230  CYS B SG  1 
ATOM   4006 N N   . HIS B 1 231 ? -14.478 -44.577 2.048   0.84   34.92  ? 231  HIS B N   1 
ATOM   4007 C CA  . HIS B 1 231 ? -15.563 -44.908 2.972   0.84   34.23  ? 231  HIS B CA  1 
ATOM   4008 C C   . HIS B 1 231 ? -16.918 -44.541 2.374   0.84   32.97  ? 231  HIS B C   1 
ATOM   4009 O O   . HIS B 1 231 ? -17.873 -45.294 2.506   0.84   32.57  ? 231  HIS B O   1 
ATOM   4010 C CB  . HIS B 1 231 ? -15.358 -44.205 4.323   0.84   34.48  ? 231  HIS B CB  1 
ATOM   4011 C CG  . HIS B 1 231 ? -14.301 -44.840 5.175   0.84   36.99  ? 231  HIS B CG  1 
ATOM   4012 N ND1 . HIS B 1 231 ? -13.019 -45.073 4.718   0.84   39.39  ? 231  HIS B ND1 1 
ATOM   4013 C CD2 . HIS B 1 231 ? -14.337 -45.300 6.451   0.84   38.61  ? 231  HIS B CD2 1 
ATOM   4014 C CE1 . HIS B 1 231 ? -12.310 -45.646 5.676   0.84   40.08  ? 231  HIS B CE1 1 
ATOM   4015 N NE2 . HIS B 1 231 ? -13.084 -45.791 6.740   0.84   40.46  ? 231  HIS B NE2 1 
ATOM   4016 N N   . ALA B 1 232 ? -16.980 -43.387 1.709   1.00   31.95  ? 232  ALA B N   1 
ATOM   4017 C CA  . ALA B 1 232 ? -18.183 -42.956 0.998   1.00   30.88  ? 232  ALA B CA  1 
ATOM   4018 C C   . ALA B 1 232 ? -18.614 -43.944 -0.093  1.00   30.46  ? 232  ALA B C   1 
ATOM   4019 O O   . ALA B 1 232 ? -19.803 -44.169 -0.273  1.00   29.81  ? 232  ALA B O   1 
ATOM   4020 C CB  . ALA B 1 232 ? -17.990 -41.571 0.408   1.00   31.09  ? 232  ALA B CB  1 
ATOM   4021 N N   . ALA B 1 233 ? -17.648 -44.509 -0.815  1.00   29.82  ? 233  ALA B N   1 
ATOM   4022 C CA  . ALA B 1 233 ? -17.927 -45.507 -1.856  1.00   30.80  ? 233  ALA B CA  1 
ATOM   4023 C C   . ALA B 1 233 ? -18.602 -46.765 -1.289  1.00   31.02  ? 233  ALA B C   1 
ATOM   4024 O O   . ALA B 1 233 ? -19.595 -47.244 -1.842  1.00   30.88  ? 233  ALA B O   1 
ATOM   4025 C CB  . ALA B 1 233 ? -16.649 -45.884 -2.607  1.00   30.37  ? 233  ALA B CB  1 
ATOM   4026 N N   . ASP B 1 234 ? -18.050 -47.286 -0.194  1.00   31.47  ? 234  ASP B N   1 
ATOM   4027 C CA  . ASP B 1 234 ? -18.665 -48.399 0.544   1.00   32.19  ? 234  ASP B CA  1 
ATOM   4028 C C   . ASP B 1 234 ? -20.095 -48.066 0.930   1.00   31.73  ? 234  ASP B C   1 
ATOM   4029 O O   . ASP B 1 234 ? -21.020 -48.832 0.653   1.00   31.56  ? 234  ASP B O   1 
ATOM   4030 C CB  . ASP B 1 234 ? -17.867 -48.712 1.815   1.00   32.74  ? 234  ASP B CB  1 
ATOM   4031 C CG  . ASP B 1 234 ? -16.548 -49.389 1.525   1.00   35.59  ? 234  ASP B CG  1 
ATOM   4032 O OD1 . ASP B 1 234 ? -16.378 -49.906 0.400   1.00   38.83  ? 234  ASP B OD1 1 
ATOM   4033 O OD2 . ASP B 1 234 ? -15.674 -49.404 2.426   1.00   39.54  ? 234  ASP B OD2 1 
ATOM   4034 N N   . LYS B 1 235 ? -20.256 -46.905 1.562   1.00   31.26  ? 235  LYS B N   1 
ATOM   4035 C CA  . LYS B 1 235 ? -21.547 -46.432 2.037   1.00   30.67  ? 235  LYS B CA  1 
ATOM   4036 C C   . LYS B 1 235 ? -22.560 -46.345 0.899   1.00   30.04  ? 235  LYS B C   1 
ATOM   4037 O O   . LYS B 1 235 ? -23.729 -46.716 1.063   1.00   30.17  ? 235  LYS B O   1 
ATOM   4038 C CB  . LYS B 1 235 ? -21.383 -45.075 2.740   1.00   30.83  ? 235  LYS B CB  1 
ATOM   4039 C CG  . LYS B 1 235 ? -22.681 -44.458 3.253   1.00   32.18  ? 235  LYS B CG  1 
ATOM   4040 C CD  . LYS B 1 235 ? -23.032 -44.971 4.638   1.00   34.39  ? 235  LYS B CD  1 
ATOM   4041 C CE  . LYS B 1 235 ? -24.412 -44.499 5.080   1.00   36.35  ? 235  LYS B CE  1 
ATOM   4042 N NZ  . LYS B 1 235 ? -24.722 -44.969 6.470   1.00   39.28  ? 235  LYS B NZ  1 
ATOM   4043 N N   . LEU B 1 236 ? -22.106 -45.877 -0.257  1.00   28.70  ? 236  LEU B N   1 
ATOM   4044 C CA  . LEU B 1 236 ? -22.984 -45.749 -1.411  1.00   28.50  ? 236  LEU B CA  1 
ATOM   4045 C C   . LEU B 1 236 ? -23.422 -47.114 -1.957  1.00   28.48  ? 236  LEU B C   1 
ATOM   4046 O O   . LEU B 1 236 ? -24.605 -47.326 -2.235  1.00   28.09  ? 236  LEU B O   1 
ATOM   4047 C CB  . LEU B 1 236 ? -22.313 -44.904 -2.500  1.00   27.84  ? 236  LEU B CB  1 
ATOM   4048 C CG  . LEU B 1 236 ? -22.201 -43.405 -2.187  1.00   28.14  ? 236  LEU B CG  1 
ATOM   4049 C CD1 . LEU B 1 236 ? -21.228 -42.727 -3.138  1.00   27.46  ? 236  LEU B CD1 1 
ATOM   4050 C CD2 . LEU B 1 236 ? -23.570 -42.712 -2.227  1.00   28.82  ? 236  LEU B CD2 1 
ATOM   4051 N N   . LEU B 1 237 ? -22.467 -48.033 -2.099  1.00   28.80  ? 237  LEU B N   1 
ATOM   4052 C CA  . LEU B 1 237 ? -22.788 -49.415 -2.477  1.00   29.82  ? 237  LEU B CA  1 
ATOM   4053 C C   . LEU B 1 237 ? -23.770 -50.068 -1.501  1.00   29.99  ? 237  LEU B C   1 
ATOM   4054 O O   . LEU B 1 237 ? -24.745 -50.672 -1.928  1.00   30.42  ? 237  LEU B O   1 
ATOM   4055 C CB  . LEU B 1 237 ? -21.519 -50.248 -2.645  1.00   29.60  ? 237  LEU B CB  1 
ATOM   4056 C CG  . LEU B 1 237 ? -20.666 -49.950 -3.888  1.00   31.40  ? 237  LEU B CG  1 
ATOM   4057 C CD1 . LEU B 1 237 ? -19.493 -50.885 -3.918  1.00   33.34  ? 237  LEU B CD1 1 
ATOM   4058 C CD2 . LEU B 1 237 ? -21.444 -50.061 -5.205  1.00   30.95  ? 237  LEU B CD2 1 
ATOM   4059 N N   . SER B 1 238 ? -23.543 -49.902 -0.200  1.00   30.31  ? 238  SER B N   1 
ATOM   4060 C CA  . SER B 1 238 ? -24.472 -50.432 0.823   1.00   30.76  ? 238  SER B CA  1 
ATOM   4061 C C   . SER B 1 238 ? -25.882 -49.872 0.714   1.00   31.02  ? 238  SER B C   1 
ATOM   4062 O O   . SER B 1 238 ? -26.851 -50.545 1.070   1.00   31.65  ? 238  SER B O   1 
ATOM   4063 C CB  . SER B 1 238 ? -23.932 -50.163 2.225   1.00   30.44  ? 238  SER B CB  1 
ATOM   4064 O OG  . SER B 1 238 ? -22.711 -50.846 2.381   1.00   31.58  ? 238  SER B OG  1 
ATOM   4065 N N   . ALA B 1 239 ? -25.983 -48.634 0.234   1.00   30.97  ? 239  ALA B N   1 
ATOM   4066 C CA  . ALA B 1 239 ? -27.261 -47.994 -0.001  1.00   31.08  ? 239  ALA B CA  1 
ATOM   4067 C C   . ALA B 1 239 ? -27.890 -48.445 -1.334  1.00   31.18  ? 239  ALA B C   1 
ATOM   4068 O O   . ALA B 1 239 ? -28.980 -48.012 -1.689  1.00   30.94  ? 239  ALA B O   1 
ATOM   4069 C CB  . ALA B 1 239 ? -27.099 -46.482 0.040   1.00   31.13  ? 239  ALA B CB  1 
ATOM   4070 N N   . GLY B 1 240 ? -27.199 -49.319 -2.060  1.00   31.19  ? 240  GLY B N   1 
ATOM   4071 C CA  . GLY B 1 240 ? -27.738 -49.887 -3.288  1.00   31.45  ? 240  GLY B CA  1 
ATOM   4072 C C   . GLY B 1 240 ? -27.358 -49.214 -4.593  1.00   31.87  ? 240  GLY B C   1 
ATOM   4073 O O   . GLY B 1 240 ? -27.980 -49.492 -5.626  1.00   32.07  ? 240  GLY B O   1 
ATOM   4074 N N   . ALA B 1 241 ? -26.360 -48.326 -4.567  1.00   31.72  ? 241  ALA B N   1 
ATOM   4075 C CA  . ALA B 1 241 ? -25.819 -47.776 -5.819  1.00   31.97  ? 241  ALA B CA  1 
ATOM   4076 C C   . ALA B 1 241 ? -25.275 -48.921 -6.672  1.00   32.31  ? 241  ALA B C   1 
ATOM   4077 O O   . ALA B 1 241 ? -24.694 -49.877 -6.148  1.00   32.07  ? 241  ALA B O   1 
ATOM   4078 C CB  . ALA B 1 241 ? -24.720 -46.758 -5.545  1.00   31.74  ? 241  ALA B CB  1 
ATOM   4079 N N   . THR B 1 242 ? -25.478 -48.813 -7.979  1.00   32.41  ? 242  THR B N   1 
ATOM   4080 C CA  . THR B 1 242 ? -25.078 -49.841 -8.937  1.00   33.80  ? 242  THR B CA  1 
ATOM   4081 C C   . THR B 1 242 ? -23.554 -49.901 -9.015  1.00   32.94  ? 242  THR B C   1 
ATOM   4082 O O   . THR B 1 242 ? -22.964 -50.972 -9.013  1.00   32.70  ? 242  THR B O   1 
ATOM   4083 C CB  . THR B 1 242 ? -25.710 -49.565 -10.315 1.00   33.39  ? 242  THR B CB  1 
ATOM   4084 O OG1 . THR B 1 242 ? -27.135 -49.698 -10.201 1.00   38.26  ? 242  THR B OG1 1 
ATOM   4085 C CG2 . THR B 1 242 ? -25.235 -50.557 -11.354 1.00   35.96  ? 242  THR B CG2 1 
ATOM   4086 N N   . ARG B 1 243 ? -22.929 -48.731 -9.067  1.00   32.63  ? 243  ARG B N   1 
ATOM   4087 C CA  . ARG B 1 243 ? -21.473 -48.624 -8.994  1.00   32.46  ? 243  ARG B CA  1 
ATOM   4088 C C   . ARG B 1 243 ? -21.100 -47.180 -8.712  1.00   31.03  ? 243  ARG B C   1 
ATOM   4089 O O   . ARG B 1 243 ? -21.949 -46.290 -8.812  1.00   30.49  ? 243  ARG B O   1 
ATOM   4090 C CB  . ARG B 1 243 ? -20.780 -49.159 -10.252 1.00   32.85  ? 243  ARG B CB  1 
ATOM   4091 C CG  . ARG B 1 243 ? -21.327 -48.625 -11.541 1.00   36.80  ? 243  ARG B CG  1 
ATOM   4092 C CD  . ARG B 1 243 ? -21.211 -49.661 -12.676 1.00   41.36  ? 243  ARG B CD  1 
ATOM   4093 N NE  . ARG B 1 243 ? -21.760 -49.091 -13.904 1.00   45.86  ? 243  ARG B NE  1 
ATOM   4094 C CZ  . ARG B 1 243 ? -21.082 -48.267 -14.696 1.00   49.45  ? 243  ARG B CZ  1 
ATOM   4095 N NH1 . ARG B 1 243 ? -19.834 -47.957 -14.389 1.00   50.29  ? 243  ARG B NH1 1 
ATOM   4096 N NH2 . ARG B 1 243 ? -21.636 -47.760 -15.796 1.00   51.53  ? 243  ARG B NH2 1 
ATOM   4097 N N   . VAL B 1 244 ? -19.845 -46.969 -8.331  1.00   29.84  ? 244  VAL B N   1 
ATOM   4098 C CA  . VAL B 1 244 ? -19.412 -45.676 -7.804  1.00   29.60  ? 244  VAL B CA  1 
ATOM   4099 C C   . VAL B 1 244 ? -18.234 -45.116 -8.588  1.00   29.26  ? 244  VAL B C   1 
ATOM   4100 O O   . VAL B 1 244 ? -17.248 -45.805 -8.856  1.00   29.36  ? 244  VAL B O   1 
ATOM   4101 C CB  . VAL B 1 244 ? -19.056 -45.740 -6.287  1.00   29.81  ? 244  VAL B CB  1 
ATOM   4102 C CG1 . VAL B 1 244 ? -18.687 -44.360 -5.739  1.00   29.24  ? 244  VAL B CG1 1 
ATOM   4103 C CG2 . VAL B 1 244 ? -20.206 -46.323 -5.473  1.00   29.05  ? 244  VAL B CG2 1 
ATOM   4104 N N   . TYR B 1 245 ? -18.360 -43.849 -8.949  1.00   28.91  ? 245  TYR B N   1 
ATOM   4105 C CA  . TYR B 1 245 ? -17.258 -43.099 -9.522  1.00   29.21  ? 245  TYR B CA  1 
ATOM   4106 C C   . TYR B 1 245 ? -16.825 -41.995 -8.565  1.00   29.02  ? 245  TYR B C   1 
ATOM   4107 O O   . TYR B 1 245 ? -17.639 -41.468 -7.798  1.00   29.17  ? 245  TYR B O   1 
ATOM   4108 C CB  . TYR B 1 245 ? -17.678 -42.505 -10.859 1.00   28.89  ? 245  TYR B CB  1 
ATOM   4109 C CG  . TYR B 1 245 ? -17.911 -43.533 -11.938 1.00   29.85  ? 245  TYR B CG  1 
ATOM   4110 C CD1 . TYR B 1 245 ? -19.139 -44.189 -12.058 1.00   29.02  ? 245  TYR B CD1 1 
ATOM   4111 C CD2 . TYR B 1 245 ? -16.908 -43.828 -12.861 1.00   29.76  ? 245  TYR B CD2 1 
ATOM   4112 C CE1 . TYR B 1 245 ? -19.351 -45.123 -13.062 1.00   30.53  ? 245  TYR B CE1 1 
ATOM   4113 C CE2 . TYR B 1 245 ? -17.109 -44.742 -13.865 1.00   31.97  ? 245  TYR B CE2 1 
ATOM   4114 C CZ  . TYR B 1 245 ? -18.326 -45.393 -13.963 1.00   32.94  ? 245  TYR B CZ  1 
ATOM   4115 O OH  . TYR B 1 245 ? -18.492 -46.303 -14.982 1.00   33.54  ? 245  TYR B OH  1 
ATOM   4116 N N   . ALA B 1 246 ? -15.539 -41.666 -8.595  1.00   28.95  ? 246  ALA B N   1 
ATOM   4117 C CA  . ALA B 1 246 ? -15.030 -40.498 -7.896  1.00   28.89  ? 246  ALA B CA  1 
ATOM   4118 C C   . ALA B 1 246 ? -14.382 -39.575 -8.928  1.00   29.29  ? 246  ALA B C   1 
ATOM   4119 O O   . ALA B 1 246 ? -13.563 -40.007 -9.743  1.00   28.58  ? 246  ALA B O   1 
ATOM   4120 C CB  . ALA B 1 246 ? -14.031 -40.901 -6.820  1.00   29.14  ? 246  ALA B CB  1 
ATOM   4121 N N   . ILE B 1 247 ? -14.798 -38.317 -8.920  1.00   29.66  ? 247  ILE B N   1 
ATOM   4122 C CA  . ILE B 1 247 ? -14.223 -37.320 -9.792  1.00   30.63  ? 247  ILE B CA  1 
ATOM   4123 C C   . ILE B 1 247 ? -13.771 -36.164 -8.910  1.00   31.42  ? 247  ILE B C   1 
ATOM   4124 O O   . ILE B 1 247 ? -14.585 -35.512 -8.261  1.00   31.41  ? 247  ILE B O   1 
ATOM   4125 C CB  . ILE B 1 247 ? -15.219 -36.849 -10.895 1.00   30.34  ? 247  ILE B CB  1 
ATOM   4126 C CG1 . ILE B 1 247 ? -15.809 -38.048 -11.654 1.00   30.56  ? 247  ILE B CG1 1 
ATOM   4127 C CG2 . ILE B 1 247 ? -14.523 -35.912 -11.888 1.00   30.49  ? 247  ILE B CG2 1 
ATOM   4128 C CD1 . ILE B 1 247 ? -16.838 -37.665 -12.701 1.00   31.07  ? 247  ILE B CD1 1 
ATOM   4129 N N   . LEU B 1 248 ? -12.462 -35.950 -8.861  1.00   32.40  ? 248  LEU B N   1 
ATOM   4130 C CA  . LEU B 1 248 ? -11.883 -34.841 -8.119  1.00   33.80  ? 248  LEU B CA  1 
ATOM   4131 C C   . LEU B 1 248 ? -11.153 -33.939 -9.092  1.00   34.21  ? 248  LEU B C   1 
ATOM   4132 O O   . LEU B 1 248 ? -10.607 -34.426 -10.086 1.00   35.05  ? 248  LEU B O   1 
ATOM   4133 C CB  . LEU B 1 248 ? -10.899 -35.345 -7.057  1.00   34.13  ? 248  LEU B CB  1 
ATOM   4134 C CG  . LEU B 1 248 ? -11.245 -36.487 -6.077  1.00   35.80  ? 248  LEU B CG  1 
ATOM   4135 C CD1 . LEU B 1 248 ? -12.702 -36.432 -5.595  1.00   36.58  ? 248  LEU B CD1 1 
ATOM   4136 C CD2 . LEU B 1 248 ? -10.932 -37.872 -6.655  1.00   36.75  ? 248  LEU B CD2 1 
ATOM   4137 N N   . THR B 1 249 ? -11.128 -32.631 -8.846  1.00   34.20  ? 249  THR B N   1 
ATOM   4138 C CA  . THR B 1 249 ? -10.246 -31.814 -9.688  1.00   34.64  ? 249  THR B CA  1 
ATOM   4139 C C   . THR B 1 249 ? -8.769  -31.979 -9.288  1.00   34.29  ? 249  THR B C   1 
ATOM   4140 O O   . THR B 1 249 ? -7.930  -32.298 -10.140 1.00   33.99  ? 249  THR B O   1 
ATOM   4141 C CB  . THR B 1 249 ? -10.727 -30.342 -9.933  1.00   34.96  ? 249  THR B CB  1 
ATOM   4142 O OG1 . THR B 1 249 ? -9.595  -29.481 -10.160 1.00   36.80  ? 249  THR B OG1 1 
ATOM   4143 C CG2 . THR B 1 249 ? -11.576 -29.817 -8.799  1.00   35.85  ? 249  THR B CG2 1 
ATOM   4144 N N   . HIS B 1 250 ? -8.474  -31.818 -7.996  1.00   33.93  ? 250  HIS B N   1 
ATOM   4145 C CA  . HIS B 1 250 ? -7.103  -31.909 -7.496  1.00   33.99  ? 250  HIS B CA  1 
ATOM   4146 C C   . HIS B 1 250 ? -6.793  -33.275 -6.857  1.00   34.25  ? 250  HIS B C   1 
ATOM   4147 O O   . HIS B 1 250 ? -7.266  -33.583 -5.757  1.00   33.92  ? 250  HIS B O   1 
ATOM   4148 C CB  . HIS B 1 250 ? -6.788  -30.765 -6.502  1.00   33.42  ? 250  HIS B CB  1 
ATOM   4149 C CG  . HIS B 1 250 ? -7.210  -29.400 -6.975  1.00   32.28  ? 250  HIS B CG  1 
ATOM   4150 N ND1 . HIS B 1 250 ? -6.660  -28.786 -8.084  1.00   31.65  ? 250  HIS B ND1 1 
ATOM   4151 C CD2 . HIS B 1 250 ? -8.129  -28.533 -6.485  1.00   30.21  ? 250  HIS B CD2 1 
ATOM   4152 C CE1 . HIS B 1 250 ? -7.224  -27.603 -8.258  1.00   28.78  ? 250  HIS B CE1 1 
ATOM   4153 N NE2 . HIS B 1 250 ? -8.117  -27.423 -7.300  1.00   30.97  ? 250  HIS B NE2 1 
ATOM   4154 N N   . GLY B 1 251 ? -5.984  -34.081 -7.541  1.00   34.89  ? 251  GLY B N   1 
ATOM   4155 C CA  . GLY B 1 251 ? -5.570  -35.377 -7.001  1.00   35.92  ? 251  GLY B CA  1 
ATOM   4156 C C   . GLY B 1 251 ? -4.243  -35.332 -6.262  1.00   36.92  ? 251  GLY B C   1 
ATOM   4157 O O   . GLY B 1 251 ? -3.192  -35.591 -6.849  1.00   36.98  ? 251  GLY B O   1 
ATOM   4158 N N   . ILE B 1 252 ? -4.285  -34.999 -4.975  1.00   37.88  ? 252  ILE B N   1 
ATOM   4159 C CA  . ILE B 1 252 ? -3.079  -35.009 -4.138  1.00   39.33  ? 252  ILE B CA  1 
ATOM   4160 C C   . ILE B 1 252 ? -2.555  -36.443 -3.924  1.00   39.72  ? 252  ILE B C   1 
ATOM   4161 O O   . ILE B 1 252 ? -1.383  -36.728 -4.196  1.00   39.64  ? 252  ILE B O   1 
ATOM   4162 C CB  . ILE B 1 252 ? -3.300  -34.296 -2.780  1.00   39.68  ? 252  ILE B CB  1 
ATOM   4163 C CG1 . ILE B 1 252 ? -3.878  -32.889 -2.999  1.00   40.35  ? 252  ILE B CG1 1 
ATOM   4164 C CG2 . ILE B 1 252 ? -1.979  -34.196 -2.016  1.00   40.42  ? 252  ILE B CG2 1 
ATOM   4165 C CD1 . ILE B 1 252 ? -4.376  -32.214 -1.734  1.00   42.00  ? 252  ILE B CD1 1 
ATOM   4166 N N   . PHE B 1 253 ? -3.432  -37.333 -3.452  1.00   40.47  ? 253  PHE B N   1 
ATOM   4167 C CA  . PHE B 1 253 ? -3.112  -38.757 -3.302  1.00   40.93  ? 253  PHE B CA  1 
ATOM   4168 C C   . PHE B 1 253 ? -1.821  -38.989 -2.509  1.00   41.96  ? 253  PHE B C   1 
ATOM   4169 O O   . PHE B 1 253 ? -0.920  -39.708 -2.960  1.00   41.51  ? 253  PHE B O   1 
ATOM   4170 C CB  . PHE B 1 253 ? -3.025  -39.463 -4.669  1.00   40.69  ? 253  PHE B CB  1 
ATOM   4171 C CG  . PHE B 1 253 ? -4.283  -39.382 -5.492  1.00   39.90  ? 253  PHE B CG  1 
ATOM   4172 C CD1 . PHE B 1 253 ? -4.208  -39.172 -6.865  1.00   39.77  ? 253  PHE B CD1 1 
ATOM   4173 C CD2 . PHE B 1 253 ? -5.538  -39.531 -4.909  1.00   39.77  ? 253  PHE B CD2 1 
ATOM   4174 C CE1 . PHE B 1 253 ? -5.362  -39.108 -7.638  1.00   39.52  ? 253  PHE B CE1 1 
ATOM   4175 C CE2 . PHE B 1 253 ? -6.700  -39.452 -5.680  1.00   38.54  ? 253  PHE B CE2 1 
ATOM   4176 C CZ  . PHE B 1 253 ? -6.606  -39.252 -7.040  1.00   37.96  ? 253  PHE B CZ  1 
ATOM   4177 N N   . SER B 1 254 ? -1.729  -38.359 -1.338  1.00   43.05  ? 254  SER B N   1 
ATOM   4178 C CA  . SER B 1 254 ? -0.561  -38.537 -0.481  1.00   44.25  ? 254  SER B CA  1 
ATOM   4179 C C   . SER B 1 254 ? -0.759  -39.714 0.477   1.00   45.01  ? 254  SER B C   1 
ATOM   4180 O O   . SER B 1 254 ? -1.883  -40.216 0.642   1.00   45.07  ? 254  SER B O   1 
ATOM   4181 C CB  . SER B 1 254 ? -0.237  -37.249 0.285   1.00   44.23  ? 254  SER B CB  1 
ATOM   4182 O OG  . SER B 1 254 ? -1.250  -36.931 1.222   1.00   44.19  ? 254  SER B OG  1 
ATOM   4183 N N   . GLY B 1 255 ? 0.339   -40.155 1.092   1.00   45.78  ? 255  GLY B N   1 
ATOM   4184 C CA  . GLY B 1 255 ? 0.306   -41.256 2.056   1.00   46.72  ? 255  GLY B CA  1 
ATOM   4185 C C   . GLY B 1 255 ? -0.347  -42.510 1.502   1.00   47.16  ? 255  GLY B C   1 
ATOM   4186 O O   . GLY B 1 255 ? 0.010   -42.957 0.415   1.00   47.66  ? 255  GLY B O   1 
ATOM   4187 N N   . PRO B 1 256 ? -1.332  -43.064 2.233   1.00   47.62  ? 256  PRO B N   1 
ATOM   4188 C CA  . PRO B 1 256 ? -1.942  -44.361 1.915   1.00   47.93  ? 256  PRO B CA  1 
ATOM   4189 C C   . PRO B 1 256 ? -2.948  -44.350 0.752   1.00   48.35  ? 256  PRO B C   1 
ATOM   4190 O O   . PRO B 1 256 ? -3.455  -45.413 0.379   1.00   48.56  ? 256  PRO B O   1 
ATOM   4191 C CB  . PRO B 1 256 ? -2.664  -44.721 3.215   1.00   47.95  ? 256  PRO B CB  1 
ATOM   4192 C CG  . PRO B 1 256 ? -3.051  -43.396 3.791   1.00   47.90  ? 256  PRO B CG  1 
ATOM   4193 C CD  . PRO B 1 256 ? -1.943  -42.446 3.428   1.00   47.50  ? 256  PRO B CD  1 
ATOM   4194 N N   . ALA B 1 257 ? -3.222  -43.172 0.191   1.00   48.39  ? 257  ALA B N   1 
ATOM   4195 C CA  . ALA B 1 257 ? -4.253  -42.994 -0.841  1.00   48.55  ? 257  ALA B CA  1 
ATOM   4196 C C   . ALA B 1 257 ? -4.241  -44.047 -1.947  1.00   48.72  ? 257  ALA B C   1 
ATOM   4197 O O   . ALA B 1 257 ? -5.268  -44.673 -2.213  1.00   48.56  ? 257  ALA B O   1 
ATOM   4198 C CB  . ALA B 1 257 ? -4.171  -41.594 -1.445  1.00   48.59  ? 257  ALA B CB  1 
ATOM   4199 N N   . ILE B 1 258 ? -3.085  -44.234 -2.586  1.00   49.07  ? 258  ILE B N   1 
ATOM   4200 C CA  . ILE B 1 258 ? -2.956  -45.179 -3.696  1.00   49.77  ? 258  ILE B CA  1 
ATOM   4201 C C   . ILE B 1 258 ? -3.256  -46.621 -3.274  1.00   50.16  ? 258  ILE B C   1 
ATOM   4202 O O   . ILE B 1 258 ? -3.764  -47.407 -4.073  1.00   50.51  ? 258  ILE B O   1 
ATOM   4203 C CB  . ILE B 1 258 ? -1.574  -45.057 -4.396  1.00   49.89  ? 258  ILE B CB  1 
ATOM   4204 C CG1 . ILE B 1 258 ? -1.397  -43.656 -5.008  1.00   49.86  ? 258  ILE B CG1 1 
ATOM   4205 C CG2 . ILE B 1 258 ? -1.382  -46.140 -5.468  1.00   50.15  ? 258  ILE B CG2 1 
ATOM   4206 C CD1 . ILE B 1 258 ? -2.509  -43.205 -5.981  1.00   48.77  ? 258  ILE B CD1 1 
ATOM   4207 N N   . SER B 1 259 ? -2.961  -46.954 -2.020  1.00   50.44  ? 259  SER B N   1 
ATOM   4208 C CA  . SER B 1 259 ? -3.327  -48.252 -1.457  1.00   50.85  ? 259  SER B CA  1 
ATOM   4209 C C   . SER B 1 259 ? -4.836  -48.334 -1.257  1.00   50.82  ? 259  SER B C   1 
ATOM   4210 O O   . SER B 1 259 ? -5.469  -49.327 -1.636  1.00   50.69  ? 259  SER B O   1 
ATOM   4211 C CB  . SER B 1 259 ? -2.611  -48.493 -0.121  1.00   50.97  ? 259  SER B CB  1 
ATOM   4212 O OG  . SER B 1 259 ? -1.205  -48.568 -0.297  1.00   51.91  ? 259  SER B OG  1 
ATOM   4213 N N   . ARG B 1 260 ? -5.403  -47.285 -0.662  1.00   50.83  ? 260  ARG B N   1 
ATOM   4214 C CA  . ARG B 1 260 ? -6.843  -47.202 -0.437  1.00   50.86  ? 260  ARG B CA  1 
ATOM   4215 C C   . ARG B 1 260 ? -7.664  -47.288 -1.720  1.00   50.55  ? 260  ARG B C   1 
ATOM   4216 O O   . ARG B 1 260 ? -8.683  -47.972 -1.750  1.00   50.78  ? 260  ARG B O   1 
ATOM   4217 C CB  . ARG B 1 260 ? -7.208  -45.937 0.344   1.00   51.18  ? 260  ARG B CB  1 
ATOM   4218 C CG  . ARG B 1 260 ? -7.451  -46.179 1.817   1.00   51.68  ? 260  ARG B CG  1 
ATOM   4219 C CD  . ARG B 1 260 ? -6.238  -45.840 2.647   1.00   53.74  ? 260  ARG B CD  1 
ATOM   4220 N NE  . ARG B 1 260 ? -6.270  -44.456 3.116   1.00   55.11  ? 260  ARG B NE  1 
ATOM   4221 C CZ  . ARG B 1 260 ? -6.953  -44.036 4.179   1.00   56.22  ? 260  ARG B CZ  1 
ATOM   4222 N NH1 . ARG B 1 260 ? -7.683  -44.893 4.890   1.00   57.05  ? 260  ARG B NH1 1 
ATOM   4223 N NH2 . ARG B 1 260 ? -6.917  -42.754 4.526   1.00   55.65  ? 260  ARG B NH2 1 
ATOM   4224 N N   . ILE B 1 261 ? -7.219  -46.608 -2.775  1.00   50.23  ? 261  ILE B N   1 
ATOM   4225 C CA  . ILE B 1 261 ? -7.942  -46.631 -4.047  1.00   50.06  ? 261  ILE B CA  1 
ATOM   4226 C C   . ILE B 1 261 ? -7.928  -48.034 -4.678  1.00   50.20  ? 261  ILE B C   1 
ATOM   4227 O O   . ILE B 1 261 ? -8.980  -48.554 -5.063  1.00   50.05  ? 261  ILE B O   1 
ATOM   4228 C CB  . ILE B 1 261 ? -7.429  -45.560 -5.032  1.00   49.78  ? 261  ILE B CB  1 
ATOM   4229 C CG1 . ILE B 1 261 ? -7.699  -44.153 -4.475  1.00   49.22  ? 261  ILE B CG1 1 
ATOM   4230 C CG2 . ILE B 1 261 ? -8.093  -45.729 -6.397  1.00   50.20  ? 261  ILE B CG2 1 
ATOM   4231 C CD1 . ILE B 1 261 ? -6.835  -43.072 -5.086  1.00   47.74  ? 261  ILE B CD1 1 
ATOM   4232 N N   . ASN B 1 262 ? -6.741  -48.639 -4.750  1.00   50.27  ? 262  ASN B N   1 
ATOM   4233 C CA  . ASN B 1 262 ? -6.568  -50.013 -5.245  1.00   50.25  ? 262  ASN B CA  1 
ATOM   4234 C C   . ASN B 1 262 ? -7.495  -51.036 -4.598  1.00   50.02  ? 262  ASN B C   1 
ATOM   4235 O O   . ASN B 1 262 ? -7.906  -51.996 -5.248  1.00   50.53  ? 262  ASN B O   1 
ATOM   4236 C CB  . ASN B 1 262 ? -5.117  -50.475 -5.068  1.00   50.29  ? 262  ASN B CB  1 
ATOM   4237 C CG  . ASN B 1 262 ? -4.144  -49.753 -5.991  1.00   50.24  ? 262  ASN B CG  1 
ATOM   4238 O OD1 . ASN B 1 262 ? -4.496  -49.323 -7.089  1.00   50.55  ? 262  ASN B OD1 1 
ATOM   4239 N ND2 . ASN B 1 262 ? -2.903  -49.629 -5.544  1.00   50.35  ? 262  ASN B ND2 1 
ATOM   4240 N N   . ASN B 1 263 ? -7.818  -50.828 -3.324  1.00   49.87  ? 263  ASN B N   1 
ATOM   4241 C CA  . ASN B 1 263 ? -8.662  -51.755 -2.575  1.00   49.89  ? 263  ASN B CA  1 
ATOM   4242 C C   . ASN B 1 263 ? -10.128 -51.332 -2.515  1.00   49.61  ? 263  ASN B C   1 
ATOM   4243 O O   . ASN B 1 263 ? -10.996 -52.104 -2.084  1.00   49.75  ? 263  ASN B O   1 
ATOM   4244 C CB  . ASN B 1 263 ? -8.119  -51.944 -1.153  1.00   50.21  ? 263  ASN B CB  1 
ATOM   4245 C CG  . ASN B 1 263 ? -6.767  -52.646 -1.124  1.00   51.04  ? 263  ASN B CG  1 
ATOM   4246 O OD1 . ASN B 1 263 ? -5.862  -52.232 -0.396  1.00   52.16  ? 263  ASN B OD1 1 
ATOM   4247 N ND2 . ASN B 1 263 ? -6.623  -53.710 -1.917  1.00   52.18  ? 263  ASN B ND2 1 
ATOM   4248 N N   . ALA B 1 264 ? -10.401 -50.105 -2.946  1.00   48.75  ? 264  ALA B N   1 
ATOM   4249 C CA  . ALA B 1 264 ? -11.746 -49.558 -2.863  1.00   47.98  ? 264  ALA B CA  1 
ATOM   4250 C C   . ALA B 1 264 ? -12.604 -49.991 -4.047  1.00   47.51  ? 264  ALA B C   1 
ATOM   4251 O O   . ALA B 1 264 ? -12.099 -50.371 -5.107  1.00   47.77  ? 264  ALA B O   1 
ATOM   4252 C CB  . ALA B 1 264 ? -11.702 -48.042 -2.747  1.00   47.82  ? 264  ALA B CB  1 
ATOM   4253 N N   . CYS B 1 265 ? -13.911 -49.906 -3.852  1.00   46.73  ? 265  CYS B N   1 
ATOM   4254 C CA  . CYS B 1 265 ? -14.873 -50.433 -4.791  1.00   46.65  ? 265  CYS B CA  1 
ATOM   4255 C C   . CYS B 1 265 ? -15.250 -49.438 -5.898  1.00   45.61  ? 265  CYS B C   1 
ATOM   4256 O O   . CYS B 1 265 ? -16.350 -49.507 -6.453  1.00   45.72  ? 265  CYS B O   1 
ATOM   4257 C CB  . CYS B 1 265 ? -16.110 -50.862 -4.011  1.00   46.75  ? 265  CYS B CB  1 
ATOM   4258 S SG  . CYS B 1 265 ? -16.717 -49.558 -2.901  1.00   50.92  ? 265  CYS B SG  1 
ATOM   4259 N N   . PHE B 1 266 ? -14.337 -48.522 -6.218  1.00   44.34  ? 266  PHE B N   1 
ATOM   4260 C CA  . PHE B 1 266 ? -14.537 -47.570 -7.304  1.00   43.11  ? 266  PHE B CA  1 
ATOM   4261 C C   . PHE B 1 266 ? -14.478 -48.263 -8.649  1.00   42.55  ? 266  PHE B C   1 
ATOM   4262 O O   . PHE B 1 266 ? -13.682 -49.177 -8.845  1.00   42.40  ? 266  PHE B O   1 
ATOM   4263 C CB  . PHE B 1 266 ? -13.456 -46.487 -7.295  1.00   42.90  ? 266  PHE B CB  1 
ATOM   4264 C CG  . PHE B 1 266 ? -13.504 -45.588 -6.109  1.00   41.75  ? 266  PHE B CG  1 
ATOM   4265 C CD1 . PHE B 1 266 ? -12.446 -45.549 -5.220  1.00   41.64  ? 266  PHE B CD1 1 
ATOM   4266 C CD2 . PHE B 1 266 ? -14.601 -44.772 -5.883  1.00   41.45  ? 266  PHE B CD2 1 
ATOM   4267 C CE1 . PHE B 1 266 ? -12.477 -44.712 -4.117  1.00   41.63  ? 266  PHE B CE1 1 
ATOM   4268 C CE2 . PHE B 1 266 ? -14.639 -43.929 -4.781  1.00   42.05  ? 266  PHE B CE2 1 
ATOM   4269 C CZ  . PHE B 1 266 ? -13.575 -43.902 -3.898  1.00   41.59  ? 266  PHE B CZ  1 
ATOM   4270 N N   . GLU B 1 267 ? -15.319 -47.812 -9.572  1.00   41.49  ? 267  GLU B N   1 
ATOM   4271 C CA  . GLU B 1 267 ? -15.228 -48.222 -10.961 1.00   40.81  ? 267  GLU B CA  1 
ATOM   4272 C C   . GLU B 1 267 ? -14.092 -47.443 -11.630 1.00   39.89  ? 267  GLU B C   1 
ATOM   4273 O O   . GLU B 1 267 ? -13.388 -47.966 -12.495 1.00   39.94  ? 267  GLU B O   1 
ATOM   4274 C CB  . GLU B 1 267 ? -16.553 -47.944 -11.664 1.00   41.04  ? 267  GLU B CB  1 
ATOM   4275 C CG  . GLU B 1 267 ? -16.637 -48.464 -13.087 1.00   43.58  ? 267  GLU B CG  1 
ATOM   4276 C CD  . GLU B 1 267 ? -17.211 -49.865 -13.186 1.00   46.13  ? 267  GLU B CD  1 
ATOM   4277 O OE1 . GLU B 1 267 ? -17.392 -50.535 -12.139 1.00   46.62  ? 267  GLU B OE1 1 
ATOM   4278 O OE2 . GLU B 1 267 ? -17.487 -50.294 -14.330 1.00   47.81  ? 267  GLU B OE2 1 
ATOM   4279 N N   . ALA B 1 268 ? -13.935 -46.183 -11.222 1.00   38.70  ? 268  ALA B N   1 
ATOM   4280 C CA  . ALA B 1 268 ? -12.895 -45.298 -11.736 1.00   37.27  ? 268  ALA B CA  1 
ATOM   4281 C C   . ALA B 1 268 ? -12.754 -44.096 -10.813 1.00   36.58  ? 268  ALA B C   1 
ATOM   4282 O O   . ALA B 1 268 ? -13.711 -43.703 -10.142 1.00   36.42  ? 268  ALA B O   1 
ATOM   4283 C CB  . ALA B 1 268 ? -13.221 -44.836 -13.154 1.00   37.26  ? 268  ALA B CB  1 
ATOM   4284 N N   . VAL B 1 269 ? -11.540 -43.552 -10.770 1.00   35.45  ? 269  VAL B N   1 
ATOM   4285 C CA  . VAL B 1 269 ? -11.223 -42.344 -10.033 1.00   34.46  ? 269  VAL B CA  1 
ATOM   4286 C C   . VAL B 1 269 ? -10.656 -41.381 -11.055 1.00   33.70  ? 269  VAL B C   1 
ATOM   4287 O O   . VAL B 1 269 ? -9.617  -41.648 -11.662 1.00   34.02  ? 269  VAL B O   1 
ATOM   4288 C CB  . VAL B 1 269 ? -10.207 -42.612 -8.898  1.00   34.36  ? 269  VAL B CB  1 
ATOM   4289 C CG1 . VAL B 1 269 ? -9.830  -41.320 -8.199  1.00   33.93  ? 269  VAL B CG1 1 
ATOM   4290 C CG2 . VAL B 1 269 ? -10.794 -43.602 -7.886  1.00   35.16  ? 269  VAL B CG2 1 
ATOM   4291 N N   . VAL B 1 270 ? -11.362 -40.278 -11.266 1.00   33.01  ? 270  VAL B N   1 
ATOM   4292 C CA  . VAL B 1 270 ? -11.001 -39.318 -12.298 1.00   32.16  ? 270  VAL B CA  1 
ATOM   4293 C C   . VAL B 1 270 ? -10.484 -38.044 -11.650 1.00   31.51  ? 270  VAL B C   1 
ATOM   4294 O O   . VAL B 1 270 ? -11.128 -37.485 -10.758 1.00   32.05  ? 270  VAL B O   1 
ATOM   4295 C CB  . VAL B 1 270 ? -12.198 -39.010 -13.230 1.00   32.05  ? 270  VAL B CB  1 
ATOM   4296 C CG1 . VAL B 1 270 ? -11.807 -38.025 -14.310 1.00   31.67  ? 270  VAL B CG1 1 
ATOM   4297 C CG2 . VAL B 1 270 ? -12.724 -40.297 -13.855 1.00   33.01  ? 270  VAL B CG2 1 
ATOM   4298 N N   . VAL B 1 271 ? -9.310  -37.607 -12.090 1.00   30.40  ? 271  VAL B N   1 
ATOM   4299 C CA  . VAL B 1 271 ? -8.689  -36.374 -11.594 1.00   29.67  ? 271  VAL B CA  1 
ATOM   4300 C C   . VAL B 1 271 ? -8.205  -35.534 -12.774 1.00   29.46  ? 271  VAL B C   1 
ATOM   4301 O O   . VAL B 1 271 ? -8.108  -36.033 -13.894 1.00   29.21  ? 271  VAL B O   1 
ATOM   4302 C CB  . VAL B 1 271 ? -7.498  -36.648 -10.621 1.00   29.71  ? 271  VAL B CB  1 
ATOM   4303 C CG1 . VAL B 1 271 ? -7.979  -37.260 -9.335  1.00   29.30  ? 271  VAL B CG1 1 
ATOM   4304 C CG2 . VAL B 1 271 ? -6.433  -37.537 -11.265 1.00   29.05  ? 271  VAL B CG2 1 
ATOM   4305 N N   . THR B 1 272 ? -7.918  -34.258 -12.536 1.00   29.11  ? 272  THR B N   1 
ATOM   4306 C CA  . THR B 1 272 ? -7.268  -33.446 -13.568 1.00   28.67  ? 272  THR B CA  1 
ATOM   4307 C C   . THR B 1 272 ? -5.755  -33.490 -13.407 1.00   28.89  ? 272  THR B C   1 
ATOM   4308 O O   . THR B 1 272 ? -5.241  -33.985 -12.409 1.00   28.92  ? 272  THR B O   1 
ATOM   4309 C CB  . THR B 1 272 ? -7.746  -31.978 -13.576 1.00   28.20  ? 272  THR B CB  1 
ATOM   4310 O OG1 . THR B 1 272 ? -7.248  -31.305 -12.415 1.00   27.87  ? 272  THR B OG1 1 
ATOM   4311 C CG2 . THR B 1 272 ? -9.267  -31.895 -13.619 1.00   27.97  ? 272  THR B CG2 1 
ATOM   4312 N N   . ASN B 1 273 ? -5.037  -32.977 -14.399 1.00   29.54  ? 273  ASN B N   1 
ATOM   4313 C CA  . ASN B 1 273 ? -3.590  -32.872 -14.280 1.00   30.12  ? 273  ASN B CA  1 
ATOM   4314 C C   . ASN B 1 273 ? -3.122  -31.551 -13.642 1.00   30.68  ? 273  ASN B C   1 
ATOM   4315 O O   . ASN B 1 273 ? -2.014  -31.109 -13.913 1.00   31.19  ? 273  ASN B O   1 
ATOM   4316 C CB  . ASN B 1 273 ? -2.898  -33.125 -15.636 1.00   30.11  ? 273  ASN B CB  1 
ATOM   4317 C CG  . ASN B 1 273 ? -3.323  -32.136 -16.721 1.00   29.82  ? 273  ASN B CG  1 
ATOM   4318 O OD1 . ASN B 1 273 ? -4.299  -31.394 -16.572 1.00   29.90  ? 273  ASN B OD1 1 
ATOM   4319 N ND2 . ASN B 1 273 ? -2.584  -32.131 -17.828 1.00   30.23  ? 273  ASN B ND2 1 
ATOM   4320 N N   . THR B 1 274 ? -3.952  -30.937 -12.790 1.00   30.94  ? 274  THR B N   1 
ATOM   4321 C CA  . THR B 1 274 ? -3.504  -29.781 -12.005 1.00   31.59  ? 274  THR B CA  1 
ATOM   4322 C C   . THR B 1 274 ? -2.309  -30.172 -11.146 1.00   32.71  ? 274  THR B C   1 
ATOM   4323 O O   . THR B 1 274 ? -1.456  -29.342 -10.855 1.00   32.29  ? 274  THR B O   1 
ATOM   4324 C CB  . THR B 1 274 ? -4.607  -29.165 -11.103 1.00   31.33  ? 274  THR B CB  1 
ATOM   4325 O OG1 . THR B 1 274 ? -5.074  -30.131 -10.157 1.00   30.87  ? 274  THR B OG1 1 
ATOM   4326 C CG2 . THR B 1 274 ? -5.779  -28.633 -11.939 1.00   30.45  ? 274  THR B CG2 1 
ATOM   4327 N N   . ILE B 1 275 ? -2.281  -31.446 -10.744 1.00   33.86  ? 275  ILE B N   1 
ATOM   4328 C CA  . ILE B 1 275 ? -1.151  -32.065 -10.054 1.00   34.99  ? 275  ILE B CA  1 
ATOM   4329 C C   . ILE B 1 275 ? -0.686  -33.259 -10.897 1.00   35.91  ? 275  ILE B C   1 
ATOM   4330 O O   . ILE B 1 275 ? -1.519  -34.019 -11.392 1.00   35.65  ? 275  ILE B O   1 
ATOM   4331 C CB  . ILE B 1 275 ? -1.562  -32.520 -8.627  1.00   35.14  ? 275  ILE B CB  1 
ATOM   4332 C CG1 . ILE B 1 275 ? -1.932  -31.301 -7.767  1.00   34.75  ? 275  ILE B CG1 1 
ATOM   4333 C CG2 . ILE B 1 275 ? -0.457  -33.347 -7.959  1.00   35.53  ? 275  ILE B CG2 1 
ATOM   4334 C CD1 . ILE B 1 275 ? -2.831  -31.612 -6.591  1.00   33.40  ? 275  ILE B CD1 1 
ATOM   4335 N N   . PRO B 1 276 ? 0.642   -33.423 -11.086 1.00   37.20  ? 276  PRO B N   1 
ATOM   4336 C CA  . PRO B 1 276 ? 1.173   -34.532 -11.893 1.00   38.06  ? 276  PRO B CA  1 
ATOM   4337 C C   . PRO B 1 276 ? 0.716   -35.904 -11.387 1.00   38.90  ? 276  PRO B C   1 
ATOM   4338 O O   . PRO B 1 276 ? 0.802   -36.192 -10.189 1.00   39.11  ? 276  PRO B O   1 
ATOM   4339 C CB  . PRO B 1 276 ? 2.697   -34.385 -11.747 1.00   38.38  ? 276  PRO B CB  1 
ATOM   4340 C CG  . PRO B 1 276 ? 2.900   -33.506 -10.570 1.00   38.03  ? 276  PRO B CG  1 
ATOM   4341 C CD  . PRO B 1 276 ? 1.728   -32.567 -10.581 1.00   37.66  ? 276  PRO B CD  1 
ATOM   4342 N N   . GLN B 1 277 ? 0.224   -36.733 -12.303 1.00   40.00  ? 277  GLN B N   1 
ATOM   4343 C CA  . GLN B 1 277 ? -0.395  -38.006 -11.945 1.00   41.12  ? 277  GLN B CA  1 
ATOM   4344 C C   . GLN B 1 277 ? 0.348   -39.228 -12.489 1.00   42.06  ? 277  GLN B C   1 
ATOM   4345 O O   . GLN B 1 277 ? 0.020   -40.358 -12.128 1.00   42.65  ? 277  GLN B O   1 
ATOM   4346 C CB  . GLN B 1 277 ? -1.857  -38.036 -12.416 1.00   40.59  ? 277  GLN B CB  1 
ATOM   4347 C CG  . GLN B 1 277 ? -2.726  -36.884 -11.914 1.00   41.10  ? 277  GLN B CG  1 
ATOM   4348 C CD  . GLN B 1 277 ? -2.928  -36.878 -10.395 1.00   40.85  ? 277  GLN B CD  1 
ATOM   4349 O OE1 . GLN B 1 277 ? -3.242  -35.839 -9.803  1.00   41.13  ? 277  GLN B OE1 1 
ATOM   4350 N NE2 . GLN B 1 277 ? -2.757  -38.037 -9.766  1.00   39.39  ? 277  GLN B NE2 1 
ATOM   4351 N N   . GLU B 1 278 ? 1.348   -38.990 -13.334 0.59   43.62  ? 278  GLU B N   1 
ATOM   4352 C CA  . GLU B 1 278 ? 2.019   -40.045 -14.109 0.59   45.17  ? 278  GLU B CA  1 
ATOM   4353 C C   . GLU B 1 278 ? 2.586   -41.162 -13.235 0.59   46.04  ? 278  GLU B C   1 
ATOM   4354 O O   . GLU B 1 278 ? 2.352   -42.340 -13.501 0.59   46.00  ? 278  GLU B O   1 
ATOM   4355 C CB  . GLU B 1 278 ? 3.114   -39.448 -15.008 0.59   45.19  ? 278  GLU B CB  1 
ATOM   4356 C CG  . GLU B 1 278 ? 2.630   -38.354 -15.977 0.59   46.44  ? 278  GLU B CG  1 
ATOM   4357 C CD  . GLU B 1 278 ? 2.084   -37.117 -15.260 0.59   48.24  ? 278  GLU B CD  1 
ATOM   4358 O OE1 . GLU B 1 278 ? 2.765   -36.600 -14.343 0.59   48.08  ? 278  GLU B OE1 1 
ATOM   4359 O OE2 . GLU B 1 278 ? 0.963   -36.673 -15.603 0.59   49.63  ? 278  GLU B OE2 1 
ATOM   4360 N N   . ASP B 1 279 ? 3.316   -40.783 -12.187 0.90   47.53  ? 279  ASP B N   1 
ATOM   4361 C CA  . ASP B 1 279 ? 3.861   -41.749 -11.230 0.90   48.77  ? 279  ASP B CA  1 
ATOM   4362 C C   . ASP B 1 279 ? 2.746   -42.509 -10.507 0.90   49.33  ? 279  ASP B C   1 
ATOM   4363 O O   . ASP B 1 279 ? 2.829   -43.728 -10.333 0.90   49.57  ? 279  ASP B O   1 
ATOM   4364 C CB  . ASP B 1 279 ? 4.775   -41.046 -10.217 0.90   49.13  ? 279  ASP B CB  1 
ATOM   4365 C CG  . ASP B 1 279 ? 5.694   -42.015 -9.473  0.90   50.40  ? 279  ASP B CG  1 
ATOM   4366 O OD1 . ASP B 1 279 ? 5.946   -41.783 -8.266  0.90   51.58  ? 279  ASP B OD1 1 
ATOM   4367 O OD2 . ASP B 1 279 ? 6.173   -42.995 -10.094 0.90   50.72  ? 279  ASP B OD2 1 
ATOM   4368 N N   . LYS B 1 280 ? 1.701   -41.785 -10.105 1.00   49.75  ? 280  LYS B N   1 
ATOM   4369 C CA  . LYS B 1 280 ? 0.579   -42.364 -9.362  1.00   50.20  ? 280  LYS B CA  1 
ATOM   4370 C C   . LYS B 1 280 ? -0.258  -43.338 -10.195 1.00   50.60  ? 280  LYS B C   1 
ATOM   4371 O O   . LYS B 1 280 ? -0.869  -44.258 -9.649  1.00   50.75  ? 280  LYS B O   1 
ATOM   4372 C CB  . LYS B 1 280 ? -0.328  -41.264 -8.790  1.00   50.23  ? 280  LYS B CB  1 
ATOM   4373 C CG  . LYS B 1 280 ? 0.359   -40.289 -7.822  1.00   50.04  ? 280  LYS B CG  1 
ATOM   4374 C CD  . LYS B 1 280 ? 0.530   -40.894 -6.433  1.00   50.42  ? 280  LYS B CD  1 
ATOM   4375 C CE  . LYS B 1 280 ? 1.355   -39.996 -5.527  1.00   50.43  ? 280  LYS B CE  1 
ATOM   4376 N NZ  . LYS B 1 280 ? 0.723   -38.658 -5.346  1.00   49.99  ? 280  LYS B NZ  1 
ATOM   4377 N N   . MET B 1 281 ? -0.297  -43.122 -11.509 1.00   51.03  ? 281  MET B N   1 
ATOM   4378 C CA  . MET B 1 281 ? -1.088  -43.963 -12.406 1.00   51.18  ? 281  MET B CA  1 
ATOM   4379 C C   . MET B 1 281 ? -0.438  -45.325 -12.623 1.00   51.51  ? 281  MET B C   1 
ATOM   4380 O O   . MET B 1 281 ? -1.132  -46.339 -12.758 1.00   51.49  ? 281  MET B O   1 
ATOM   4381 C CB  . MET B 1 281 ? -1.333  -43.251 -13.738 1.00   51.06  ? 281  MET B CB  1 
ATOM   4382 C CG  . MET B 1 281 ? -2.349  -42.122 -13.631 1.00   50.95  ? 281  MET B CG  1 
ATOM   4383 S SD  . MET B 1 281 ? -2.493  -41.134 -15.124 1.00   50.97  ? 281  MET B SD  1 
ATOM   4384 C CE  . MET B 1 281 ? -3.504  -42.191 -16.170 1.00   51.13  ? 281  MET B CE  1 
ATOM   4385 N N   . LYS B 1 282 ? 0.894   -45.341 -12.634 0.90   51.82  ? 282  LYS B N   1 
ATOM   4386 C CA  . LYS B 1 282 ? 1.669   -46.578 -12.752 0.90   52.27  ? 282  LYS B CA  1 
ATOM   4387 C C   . LYS B 1 282 ? 1.355   -47.582 -11.635 0.90   52.19  ? 282  LYS B C   1 
ATOM   4388 O O   . LYS B 1 282 ? 1.392   -48.795 -11.854 0.90   52.27  ? 282  LYS B O   1 
ATOM   4389 C CB  . LYS B 1 282 ? 3.170   -46.269 -12.771 0.90   52.67  ? 282  LYS B CB  1 
ATOM   4390 C CG  . LYS B 1 282 ? 3.685   -45.649 -14.070 0.90   53.63  ? 282  LYS B CG  1 
ATOM   4391 C CD  . LYS B 1 282 ? 5.195   -45.432 -13.998 0.90   55.47  ? 282  LYS B CD  1 
ATOM   4392 C CE  . LYS B 1 282 ? 5.770   -44.979 -15.336 0.90   56.79  ? 282  LYS B CE  1 
ATOM   4393 N NZ  . LYS B 1 282 ? 7.268   -45.042 -15.348 0.90   57.23  ? 282  LYS B NZ  1 
ATOM   4394 N N   . HIS B 1 283 ? 1.045   -47.073 -10.443 1.00   52.16  ? 283  HIS B N   1 
ATOM   4395 C CA  . HIS B 1 283 ? 0.710   -47.928 -9.297  1.00   52.02  ? 283  HIS B CA  1 
ATOM   4396 C C   . HIS B 1 283 ? -0.800  -48.044 -9.038  1.00   51.34  ? 283  HIS B C   1 
ATOM   4397 O O   . HIS B 1 283 ? -1.228  -48.776 -8.141  1.00   51.31  ? 283  HIS B O   1 
ATOM   4398 C CB  . HIS B 1 283 ? 1.431   -47.435 -8.035  1.00   52.44  ? 283  HIS B CB  1 
ATOM   4399 C CG  . HIS B 1 283 ? 2.921   -47.373 -8.176  1.00   54.27  ? 283  HIS B CG  1 
ATOM   4400 N ND1 . HIS B 1 283 ? 3.706   -48.504 -8.299  1.00   55.40  ? 283  HIS B ND1 1 
ATOM   4401 C CD2 . HIS B 1 283 ? 3.770   -46.318 -8.210  1.00   55.41  ? 283  HIS B CD2 1 
ATOM   4402 C CE1 . HIS B 1 283 ? 4.974   -48.147 -8.407  1.00   56.31  ? 283  HIS B CE1 1 
ATOM   4403 N NE2 . HIS B 1 283 ? 5.040   -46.825 -8.357  1.00   56.41  ? 283  HIS B NE2 1 
ATOM   4404 N N   . CYS B 1 284 ? -1.601  -47.324 -9.823  1.00   50.62  ? 284  CYS B N   1 
ATOM   4405 C CA  . CYS B 1 284 ? -3.049  -47.306 -9.627  1.00   49.89  ? 284  CYS B CA  1 
ATOM   4406 C C   . CYS B 1 284 ? -3.803  -47.250 -10.958 1.00   48.91  ? 284  CYS B C   1 
ATOM   4407 O O   . CYS B 1 284 ? -4.000  -46.174 -11.538 1.00   48.67  ? 284  CYS B O   1 
ATOM   4408 C CB  . CYS B 1 284 ? -3.451  -46.143 -8.717  1.00   50.04  ? 284  CYS B CB  1 
ATOM   4409 S SG  . CYS B 1 284 ? -5.130  -46.254 -8.072  1.00   51.72  ? 284  CYS B SG  1 
ATOM   4410 N N   . SER B 1 285 ? -4.229  -48.422 -11.426 1.00   47.70  ? 285  SER B N   1 
ATOM   4411 C CA  . SER B 1 285 ? -4.912  -48.565 -12.717 1.00   46.39  ? 285  SER B CA  1 
ATOM   4412 C C   . SER B 1 285 ? -6.308  -47.924 -12.777 1.00   45.60  ? 285  SER B C   1 
ATOM   4413 O O   . SER B 1 285 ? -6.806  -47.607 -13.866 1.00   45.66  ? 285  SER B O   1 
ATOM   4414 C CB  . SER B 1 285 ? -5.001  -50.040 -13.103 1.00   46.64  ? 285  SER B CB  1 
ATOM   4415 O OG  . SER B 1 285 ? -5.483  -50.815 -12.013 1.00   46.77  ? 285  SER B OG  1 
ATOM   4416 N N   . LYS B 1 286 ? -6.930  -47.737 -11.615 1.00   44.11  ? 286  LYS B N   1 
ATOM   4417 C CA  . LYS B 1 286 ? -8.255  -47.115 -11.529 1.00   43.09  ? 286  LYS B CA  1 
ATOM   4418 C C   . LYS B 1 286 ? -8.268  -45.623 -11.890 1.00   41.89  ? 286  LYS B C   1 
ATOM   4419 O O   . LYS B 1 286 ? -9.328  -45.060 -12.170 1.00   41.78  ? 286  LYS B O   1 
ATOM   4420 C CB  . LYS B 1 286 ? -8.845  -47.301 -10.131 1.00   43.21  ? 286  LYS B CB  1 
ATOM   4421 C CG  . LYS B 1 286 ? -9.288  -48.715 -9.819  1.00   44.49  ? 286  LYS B CG  1 
ATOM   4422 C CD  . LYS B 1 286 ? -10.389 -48.697 -8.770  1.00   46.42  ? 286  LYS B CD  1 
ATOM   4423 C CE  . LYS B 1 286 ? -10.685 -50.092 -8.251  1.00   47.76  ? 286  LYS B CE  1 
ATOM   4424 N NZ  . LYS B 1 286 ? -9.767  -50.462 -7.145  1.00   49.19  ? 286  LYS B NZ  1 
ATOM   4425 N N   . ILE B 1 287 ? -7.098  -44.991 -11.883 1.00   40.52  ? 287  ILE B N   1 
ATOM   4426 C CA  . ILE B 1 287 ? -7.003  -43.557 -12.140 1.00   39.10  ? 287  ILE B CA  1 
ATOM   4427 C C   . ILE B 1 287 ? -7.025  -43.197 -13.631 1.00   38.21  ? 287  ILE B C   1 
ATOM   4428 O O   . ILE B 1 287 ? -6.284  -43.759 -14.437 1.00   38.08  ? 287  ILE B O   1 
ATOM   4429 C CB  . ILE B 1 287 ? -5.773  -42.908 -11.433 1.00   39.26  ? 287  ILE B CB  1 
ATOM   4430 C CG1 . ILE B 1 287 ? -5.868  -43.109 -9.912  1.00   39.64  ? 287  ILE B CG1 1 
ATOM   4431 C CG2 . ILE B 1 287 ? -5.666  -41.406 -11.789 1.00   38.35  ? 287  ILE B CG2 1 
ATOM   4432 C CD1 . ILE B 1 287 ? -4.663  -42.601 -9.112  1.00   40.33  ? 287  ILE B CD1 1 
ATOM   4433 N N   . GLN B 1 288 ? -7.902  -42.261 -13.978 1.00   36.65  ? 288  GLN B N   1 
ATOM   4434 C CA  . GLN B 1 288 ? -7.888  -41.616 -15.278 1.00   35.53  ? 288  GLN B CA  1 
ATOM   4435 C C   . GLN B 1 288 ? -7.705  -40.117 -15.086 1.00   35.20  ? 288  GLN B C   1 
ATOM   4436 O O   . GLN B 1 288 ? -8.119  -39.555 -14.059 1.00   35.15  ? 288  GLN B O   1 
ATOM   4437 C CB  . GLN B 1 288 ? -9.179  -41.918 -16.049 1.00   35.53  ? 288  GLN B CB  1 
ATOM   4438 C CG  . GLN B 1 288 ? -9.314  -43.396 -16.410 1.00   34.59  ? 288  GLN B CG  1 
ATOM   4439 C CD  . GLN B 1 288 ? -10.633 -43.736 -17.056 1.00   34.37  ? 288  GLN B CD  1 
ATOM   4440 O OE1 . GLN B 1 288 ? -11.324 -44.647 -16.615 1.00   35.15  ? 288  GLN B OE1 1 
ATOM   4441 N NE2 . GLN B 1 288 ? -10.988 -43.015 -18.114 1.00   33.66  ? 288  GLN B NE2 1 
ATOM   4442 N N   . VAL B 1 289 ? -7.078  -39.476 -16.070 1.00   34.87  ? 289  VAL B N   1 
ATOM   4443 C CA  . VAL B 1 289 ? -6.729  -38.058 -15.980 1.00   34.72  ? 289  VAL B CA  1 
ATOM   4444 C C   . VAL B 1 289 ? -7.412  -37.216 -17.055 1.00   34.47  ? 289  VAL B C   1 
ATOM   4445 O O   . VAL B 1 289 ? -7.377  -37.554 -18.247 1.00   34.79  ? 289  VAL B O   1 
ATOM   4446 C CB  . VAL B 1 289 ? -5.188  -37.844 -16.018 1.00   34.85  ? 289  VAL B CB  1 
ATOM   4447 C CG1 . VAL B 1 289 ? -4.833  -36.368 -15.939 1.00   35.23  ? 289  VAL B CG1 1 
ATOM   4448 C CG2 . VAL B 1 289 ? -4.527  -38.566 -14.870 1.00   35.24  ? 289  VAL B CG2 1 
ATOM   4449 N N   . ILE B 1 290 ? -8.054  -36.132 -16.629 1.00   33.80  ? 290  ILE B N   1 
ATOM   4450 C CA  . ILE B 1 290 ? -8.553  -35.122 -17.563 1.00   33.14  ? 290  ILE B CA  1 
ATOM   4451 C C   . ILE B 1 290 ? -7.474  -34.052 -17.719 1.00   33.24  ? 290  ILE B C   1 
ATOM   4452 O O   . ILE B 1 290 ? -7.029  -33.457 -16.734 1.00   32.56  ? 290  ILE B O   1 
ATOM   4453 C CB  . ILE B 1 290 ? -9.876  -34.465 -17.081 1.00   33.35  ? 290  ILE B CB  1 
ATOM   4454 C CG1 . ILE B 1 290 ? -11.014 -35.492 -16.980 1.00   32.77  ? 290  ILE B CG1 1 
ATOM   4455 C CG2 . ILE B 1 290 ? -10.285 -33.322 -18.027 1.00   33.68  ? 290  ILE B CG2 1 
ATOM   4456 C CD1 . ILE B 1 290 ? -12.286 -34.962 -16.266 1.00   32.65  ? 290  ILE B CD1 1 
ATOM   4457 N N   . ASP B 1 291 ? -7.037  -33.832 -18.956 1.00   32.87  ? 291  ASP B N   1 
ATOM   4458 C CA  . ASP B 1 291 ? -6.048  -32.802 -19.263 1.00   33.02  ? 291  ASP B CA  1 
ATOM   4459 C C   . ASP B 1 291 ? -6.697  -31.411 -19.197 1.00   32.24  ? 291  ASP B C   1 
ATOM   4460 O O   . ASP B 1 291 ? -7.678  -31.160 -19.883 1.00   32.43  ? 291  ASP B O   1 
ATOM   4461 C CB  . ASP B 1 291 ? -5.452  -33.067 -20.656 1.00   33.31  ? 291  ASP B CB  1 
ATOM   4462 C CG  . ASP B 1 291 ? -4.356  -32.067 -21.048 1.00   34.63  ? 291  ASP B CG  1 
ATOM   4463 O OD1 . ASP B 1 291 ? -3.927  -31.233 -20.222 1.00   34.77  ? 291  ASP B OD1 1 
ATOM   4464 O OD2 . ASP B 1 291 ? -3.908  -32.133 -22.211 1.00   36.97  ? 291  ASP B OD2 1 
ATOM   4465 N N   . ILE B 1 292 ? -6.162  -30.523 -18.358 1.00   31.43  ? 292  ILE B N   1 
ATOM   4466 C CA  . ILE B 1 292 ? -6.698  -29.154 -18.252 1.00   30.92  ? 292  ILE B CA  1 
ATOM   4467 C C   . ILE B 1 292 ? -5.752  -28.073 -18.802 1.00   30.20  ? 292  ILE B C   1 
ATOM   4468 O O   . ILE B 1 292 ? -6.031  -26.869 -18.677 1.00   29.58  ? 292  ILE B O   1 
ATOM   4469 C CB  . ILE B 1 292 ? -7.192  -28.788 -16.802 1.00   30.97  ? 292  ILE B CB  1 
ATOM   4470 C CG1 . ILE B 1 292 ? -6.175  -29.169 -15.722 1.00   31.00  ? 292  ILE B CG1 1 
ATOM   4471 C CG2 . ILE B 1 292 ? -8.503  -29.485 -16.493 1.00   32.01  ? 292  ILE B CG2 1 
ATOM   4472 C CD1 . ILE B 1 292 ? -5.004  -28.221 -15.560 1.00   27.29  ? 292  ILE B CD1 1 
ATOM   4473 N N   . SER B 1 293 ? -4.654  -28.509 -19.425 1.00   29.14  ? 293  SER B N   1 
ATOM   4474 C CA  . SER B 1 293 ? -3.687  -27.591 -20.032 1.00   28.92  ? 293  SER B CA  1 
ATOM   4475 C C   . SER B 1 293 ? -4.325  -26.613 -21.025 1.00   28.65  ? 293  SER B C   1 
ATOM   4476 O O   . SER B 1 293 ? -3.880  -25.476 -21.137 1.00   28.15  ? 293  SER B O   1 
ATOM   4477 C CB  . SER B 1 293 ? -2.537  -28.350 -20.703 1.00   28.85  ? 293  SER B CB  1 
ATOM   4478 O OG  . SER B 1 293 ? -2.992  -29.206 -21.739 1.00   28.98  ? 293  SER B OG  1 
ATOM   4479 N N   . MET B 1 294 ? -5.373  -27.046 -21.721 1.00   28.60  ? 294  MET B N   1 
ATOM   4480 C CA  . MET B 1 294 ? -6.004  -26.190 -22.728 1.00   29.46  ? 294  MET B CA  1 
ATOM   4481 C C   . MET B 1 294 ? -6.801  -25.089 -22.061 1.00   28.51  ? 294  MET B C   1 
ATOM   4482 O O   . MET B 1 294 ? -6.807  -23.956 -22.534 1.00   28.64  ? 294  MET B O   1 
ATOM   4483 C CB  . MET B 1 294 ? -6.866  -26.989 -23.736 1.00   30.03  ? 294  MET B CB  1 
ATOM   4484 C CG  . MET B 1 294 ? -8.114  -27.688 -23.162 1.00   33.62  ? 294  MET B CG  1 
ATOM   4485 S SD  . MET B 1 294 ? -7.771  -28.940 -21.899 1.00   42.65  ? 294  MET B SD  1 
ATOM   4486 C CE  . MET B 1 294 ? -6.643  -30.035 -22.777 1.00   41.60  ? 294  MET B CE  1 
ATOM   4487 N N   . ILE B 1 295 ? -7.447  -25.424 -20.946 1.00   27.96  ? 295  ILE B N   1 
ATOM   4488 C CA  . ILE B 1 295 ? -8.215  -24.443 -20.187 1.00   26.99  ? 295  ILE B CA  1 
ATOM   4489 C C   . ILE B 1 295 ? -7.249  -23.398 -19.639 1.00   26.20  ? 295  ILE B C   1 
ATOM   4490 O O   . ILE B 1 295 ? -7.484  -22.198 -19.777 1.00   26.41  ? 295  ILE B O   1 
ATOM   4491 C CB  . ILE B 1 295 ? -9.036  -25.105 -19.053 1.00   27.28  ? 295  ILE B CB  1 
ATOM   4492 C CG1 . ILE B 1 295 ? -10.096 -26.053 -19.651 1.00   28.52  ? 295  ILE B CG1 1 
ATOM   4493 C CG2 . ILE B 1 295 ? -9.680  -24.049 -18.143 1.00   25.58  ? 295  ILE B CG2 1 
ATOM   4494 C CD1 . ILE B 1 295 ? -10.666 -27.056 -18.647 1.00   28.88  ? 295  ILE B CD1 1 
ATOM   4495 N N   . LEU B 1 296 ? -6.156  -23.864 -19.041 1.00   25.22  ? 296  LEU B N   1 
ATOM   4496 C CA  . LEU B 1 296 ? -5.118  -22.967 -18.527 1.00   24.52  ? 296  LEU B CA  1 
ATOM   4497 C C   . LEU B 1 296 ? -4.464  -22.112 -19.634 1.00   24.13  ? 296  LEU B C   1 
ATOM   4498 O O   . LEU B 1 296 ? -4.321  -20.906 -19.474 1.00   23.54  ? 296  LEU B O   1 
ATOM   4499 C CB  . LEU B 1 296 ? -4.067  -23.753 -17.726 1.00   23.63  ? 296  LEU B CB  1 
ATOM   4500 C CG  . LEU B 1 296 ? -4.526  -24.339 -16.376 1.00   24.13  ? 296  LEU B CG  1 
ATOM   4501 C CD1 . LEU B 1 296 ? -3.357  -24.965 -15.632 1.00   24.40  ? 296  LEU B CD1 1 
ATOM   4502 C CD2 . LEU B 1 296 ? -5.178  -23.302 -15.494 1.00   25.27  ? 296  LEU B CD2 1 
ATOM   4503 N N   . ALA B 1 297 ? -4.095  -22.742 -20.751 1.00   24.07  ? 297  ALA B N   1 
ATOM   4504 C CA  . ALA B 1 297 ? -3.493  -22.026 -21.895 1.00   24.84  ? 297  ALA B CA  1 
ATOM   4505 C C   . ALA B 1 297 ? -4.412  -20.931 -22.428 1.00   24.74  ? 297  ALA B C   1 
ATOM   4506 O O   . ALA B 1 297 ? -3.982  -19.804 -22.692 1.00   25.52  ? 297  ALA B O   1 
ATOM   4507 C CB  . ALA B 1 297 ? -3.123  -23.013 -23.018 1.00   24.23  ? 297  ALA B CB  1 
ATOM   4508 N N   . GLU B 1 298 ? -5.688  -21.267 -22.553 0.92   24.95  ? 298  GLU B N   1 
ATOM   4509 C CA  . GLU B 1 298 ? -6.695  -20.348 -23.063 0.92   25.64  ? 298  GLU B CA  1 
ATOM   4510 C C   . GLU B 1 298 ? -6.973  -19.175 -22.109 0.92   24.90  ? 298  GLU B C   1 
ATOM   4511 O O   . GLU B 1 298 ? -7.148  -18.047 -22.551 0.92   24.21  ? 298  GLU B O   1 
ATOM   4512 C CB  . GLU B 1 298 ? -7.980  -21.127 -23.376 0.92   26.02  ? 298  GLU B CB  1 
ATOM   4513 C CG  . GLU B 1 298 ? -9.061  -20.332 -24.079 0.92   29.70  ? 298  GLU B CG  1 
ATOM   4514 C CD  . GLU B 1 298 ? -8.720  -19.956 -25.521 0.92   34.06  ? 298  GLU B CD  1 
ATOM   4515 O OE1 . GLU B 1 298 ? -7.691  -20.419 -26.086 0.92   35.58  ? 298  GLU B OE1 1 
ATOM   4516 O OE2 . GLU B 1 298 ? -9.511  -19.179 -26.098 0.92   37.01  ? 298  GLU B OE2 1 
ATOM   4517 N N   . ALA B 1 299 ? -7.026  -19.446 -20.806 1.00   24.27  ? 299  ALA B N   1 
ATOM   4518 C CA  . ALA B 1 299 ? -7.116  -18.365 -19.809 1.00   24.26  ? 299  ALA B CA  1 
ATOM   4519 C C   . ALA B 1 299 ? -5.902  -17.421 -19.877 1.00   23.99  ? 299  ALA B C   1 
ATOM   4520 O O   . ALA B 1 299 ? -6.054  -16.208 -19.787 1.00   24.62  ? 299  ALA B O   1 
ATOM   4521 C CB  . ALA B 1 299 ? -7.303  -18.935 -18.390 1.00   23.66  ? 299  ALA B CB  1 
ATOM   4522 N N   . ILE B 1 300 ? -4.711  -17.976 -20.058 1.00   23.60  ? 300  ILE B N   1 
ATOM   4523 C CA  . ILE B 1 300 ? -3.500  -17.164 -20.254 1.00   24.01  ? 300  ILE B CA  1 
ATOM   4524 C C   . ILE B 1 300 ? -3.574  -16.313 -21.532 1.00   24.64  ? 300  ILE B C   1 
ATOM   4525 O O   . ILE B 1 300 ? -3.288  -15.114 -21.516 1.00   23.71  ? 300  ILE B O   1 
ATOM   4526 C CB  . ILE B 1 300 ? -2.224  -18.042 -20.257 1.00   23.29  ? 300  ILE B CB  1 
ATOM   4527 C CG1 . ILE B 1 300 ? -1.943  -18.569 -18.840 1.00   23.33  ? 300  ILE B CG1 1 
ATOM   4528 C CG2 . ILE B 1 300 ? -1.024  -17.252 -20.775 1.00   23.24  ? 300  ILE B CG2 1 
ATOM   4529 C CD1 . ILE B 1 300 ? -0.920  -19.692 -18.788 1.00   21.79  ? 300  ILE B CD1 1 
ATOM   4530 N N   . ARG B 1 301 ? -3.984  -16.954 -22.624 1.00   26.31  ? 301  ARG B N   1 
ATOM   4531 C CA  . ARG B 1 301 ? -4.179  -16.296 -23.917 1.00   28.55  ? 301  ARG B CA  1 
ATOM   4532 C C   . ARG B 1 301 ? -5.202  -15.159 -23.815 1.00   29.17  ? 301  ARG B C   1 
ATOM   4533 O O   . ARG B 1 301 ? -4.941  -14.039 -24.268 1.00   28.87  ? 301  ARG B O   1 
ATOM   4534 C CB  . ARG B 1 301 ? -4.610  -17.343 -24.961 1.00   29.01  ? 301  ARG B CB  1 
ATOM   4535 C CG  . ARG B 1 301 ? -4.761  -16.815 -26.390 1.00   32.59  ? 301  ARG B CG  1 
ATOM   4536 C CD  . ARG B 1 301 ? -5.473  -17.843 -27.279 1.00   36.37  ? 301  ARG B CD  1 
ATOM   4537 N NE  . ARG B 1 301 ? -6.300  -17.185 -28.297 1.00   42.11  ? 301  ARG B NE  1 
ATOM   4538 C CZ  . ARG B 1 301 ? -7.601  -16.930 -28.176 1.00   43.17  ? 301  ARG B CZ  1 
ATOM   4539 N NH1 . ARG B 1 301 ? -8.255  -17.282 -27.085 1.00   45.51  ? 301  ARG B NH1 1 
ATOM   4540 N NH2 . ARG B 1 301 ? -8.256  -16.328 -29.157 1.00   45.38  ? 301  ARG B NH2 1 
ATOM   4541 N N   . ARG B 1 302 ? -6.341  -15.436 -23.176 0.84   30.17  ? 302  ARG B N   1 
ATOM   4542 C CA  . ARG B 1 302 ? -7.422  -14.444 -23.039 0.84   31.40  ? 302  ARG B CA  1 
ATOM   4543 C C   . ARG B 1 302 ? -7.010  -13.281 -22.146 0.84   31.94  ? 302  ARG B C   1 
ATOM   4544 O O   . ARG B 1 302 ? -7.291  -12.119 -22.469 0.84   32.38  ? 302  ARG B O   1 
ATOM   4545 C CB  . ARG B 1 302 ? -8.705  -15.080 -22.495 0.84   31.30  ? 302  ARG B CB  1 
ATOM   4546 C CG  . ARG B 1 302 ? -9.215  -16.289 -23.263 0.84   34.99  ? 302  ARG B CG  1 
ATOM   4547 C CD  . ARG B 1 302 ? -9.955  -15.893 -24.518 0.84   39.21  ? 302  ARG B CD  1 
ATOM   4548 N NE  . ARG B 1 302 ? -10.563 -17.041 -25.190 0.84   42.84  ? 302  ARG B NE  1 
ATOM   4549 C CZ  . ARG B 1 302 ? -11.872 -17.255 -25.316 0.84   42.56  ? 302  ARG B CZ  1 
ATOM   4550 N NH1 . ARG B 1 302 ? -12.760 -16.407 -24.811 0.84   41.02  ? 302  ARG B NH1 1 
ATOM   4551 N NH2 . ARG B 1 302 ? -12.289 -18.328 -25.968 0.84   43.11  ? 302  ARG B NH2 1 
ATOM   4552 N N   . THR B 1 303 ? -6.350  -13.610 -21.030 1.00   32.23  ? 303  THR B N   1 
ATOM   4553 C CA  . THR B 1 303 ? -5.800  -12.628 -20.087 1.00   33.00  ? 303  THR B CA  1 
ATOM   4554 C C   . THR B 1 303 ? -4.888  -11.636 -20.804 1.00   33.41  ? 303  THR B C   1 
ATOM   4555 O O   . THR B 1 303 ? -5.019  -10.421 -20.647 1.00   33.46  ? 303  THR B O   1 
ATOM   4556 C CB  . THR B 1 303 ? -4.969  -13.328 -18.963 1.00   33.03  ? 303  THR B CB  1 
ATOM   4557 O OG1 . THR B 1 303 ? -5.806  -14.227 -18.228 1.00   34.42  ? 303  THR B OG1 1 
ATOM   4558 C CG2 . THR B 1 303 ? -4.376  -12.329 -18.008 1.00   33.34  ? 303  THR B CG2 1 
ATOM   4559 N N   . HIS B 1 304 ? -3.955  -12.177 -21.580 1.00   33.71  ? 304  HIS B N   1 
ATOM   4560 C CA  . HIS B 1 304 ? -2.979  -11.373 -22.295 1.00   34.50  ? 304  HIS B CA  1 
ATOM   4561 C C   . HIS B 1 304 ? -3.629  -10.483 -23.370 1.00   35.48  ? 304  HIS B C   1 
ATOM   4562 O O   . HIS B 1 304 ? -3.216  -9.341  -23.545 1.00   35.23  ? 304  HIS B O   1 
ATOM   4563 C CB  . HIS B 1 304 ? -1.918  -12.283 -22.904 1.00   34.14  ? 304  HIS B CB  1 
ATOM   4564 C CG  . HIS B 1 304 ? -0.944  -11.570 -23.786 1.00   35.06  ? 304  HIS B CG  1 
ATOM   4565 N ND1 . HIS B 1 304 ? 0.115   -10.832 -23.286 1.00   34.77  ? 304  HIS B ND1 1 
ATOM   4566 C CD2 . HIS B 1 304 ? -0.870  -11.478 -25.137 1.00   34.94  ? 304  HIS B CD2 1 
ATOM   4567 C CE1 . HIS B 1 304 ? 0.801   -10.322 -24.296 1.00   35.69  ? 304  HIS B CE1 1 
ATOM   4568 N NE2 . HIS B 1 304 ? 0.223   -10.696 -25.428 1.00   34.84  ? 304  HIS B NE2 1 
ATOM   4569 N N   . ASN B 1 305 ? -4.647  -11.011 -24.053 1.00   36.83  ? 305  ASN B N   1 
ATOM   4570 C CA  . ASN B 1 305 ? -5.333  -10.327 -25.172 1.00   38.75  ? 305  ASN B CA  1 
ATOM   4571 C C   . ASN B 1 305 ? -6.438  -9.371  -24.745 1.00   39.74  ? 305  ASN B C   1 
ATOM   4572 O O   . ASN B 1 305 ? -6.905  -8.552  -25.545 1.00   39.95  ? 305  ASN B O   1 
ATOM   4573 C CB  . ASN B 1 305 ? -5.968  -11.354 -26.126 1.00   38.51  ? 305  ASN B CB  1 
ATOM   4574 C CG  . ASN B 1 305 ? -4.956  -12.051 -27.014 1.00   40.45  ? 305  ASN B CG  1 
ATOM   4575 O OD1 . ASN B 1 305 ? -3.767  -11.731 -27.006 1.00   39.70  ? 305  ASN B OD1 1 
ATOM   4576 N ND2 . ASN B 1 305 ? -5.436  -13.016 -27.805 1.00   42.81  ? 305  ASN B ND2 1 
ATOM   4577 N N   . GLY B 1 306 ? -6.884  -9.503  -23.499 1.00   40.82  ? 306  GLY B N   1 
ATOM   4578 C CA  . GLY B 1 306 ? -8.028  -8.738  -23.015 1.00   42.09  ? 306  GLY B CA  1 
ATOM   4579 C C   . GLY B 1 306 ? -9.351  -9.335  -23.458 1.00   42.86  ? 306  GLY B C   1 
ATOM   4580 O O   . GLY B 1 306 ? -10.358 -8.636  -23.546 1.00   42.81  ? 306  GLY B O   1 
ATOM   4581 N N   . GLU B 1 307 ? -9.351  -10.638 -23.726 1.00   43.80  ? 307  GLU B N   1 
ATOM   4582 C CA  . GLU B 1 307 ? -10.567 -11.339 -24.115 1.00   44.75  ? 307  GLU B CA  1 
ATOM   4583 C C   . GLU B 1 307 ? -11.219 -12.026 -22.917 1.00   45.10  ? 307  GLU B C   1 
ATOM   4584 O O   . GLU B 1 307 ? -10.595 -12.166 -21.860 1.00   44.63  ? 307  GLU B O   1 
ATOM   4585 C CB  . GLU B 1 307 ? -10.271 -12.351 -25.215 1.00   44.82  ? 307  GLU B CB  1 
ATOM   4586 C CG  . GLU B 1 307 ? -9.894  -11.712 -26.535 1.00   46.33  ? 307  GLU B CG  1 
ATOM   4587 C CD  . GLU B 1 307 ? -9.387  -12.717 -27.548 1.00   48.38  ? 307  GLU B CD  1 
ATOM   4588 O OE1 . GLU B 1 307 ? -8.401  -12.388 -28.245 1.00   49.70  ? 307  GLU B OE1 1 
ATOM   4589 O OE2 . GLU B 1 307 ? -9.973  -13.825 -27.655 1.00   49.51  ? 307  GLU B OE2 1 
ATOM   4590 N N   . SER B 1 308 ? -12.465 -12.466 -23.108 1.00   45.55  ? 308  SER B N   1 
ATOM   4591 C CA  . SER B 1 308 ? -13.297 -13.005 -22.036 1.00   45.86  ? 308  SER B CA  1 
ATOM   4592 C C   . SER B 1 308 ? -12.843 -14.386 -21.551 1.00   46.29  ? 308  SER B C   1 
ATOM   4593 O O   . SER B 1 308 ? -12.891 -15.378 -22.293 1.00   47.02  ? 308  SER B O   1 
ATOM   4594 C CB  . SER B 1 308 ? -14.765 -13.034 -22.476 1.00   45.95  ? 308  SER B CB  1 
ATOM   4595 O OG  . SER B 1 308 ? -15.628 -13.419 -21.410 1.00   45.77  ? 308  SER B OG  1 
ATOM   4596 N N   . VAL B 1 309 ? -12.396 -14.432 -20.300 1.00   46.30  ? 309  VAL B N   1 
ATOM   4597 C CA  . VAL B 1 309 ? -12.023 -15.678 -19.634 1.00   46.59  ? 309  VAL B CA  1 
ATOM   4598 C C   . VAL B 1 309 ? -13.288 -16.422 -19.164 1.00   47.22  ? 309  VAL B C   1 
ATOM   4599 O O   . VAL B 1 309 ? -13.256 -17.636 -18.958 1.00   46.87  ? 309  VAL B O   1 
ATOM   4600 C CB  . VAL B 1 309 ? -11.044 -15.409 -18.457 1.00   46.47  ? 309  VAL B CB  1 
ATOM   4601 C CG1 . VAL B 1 309 ? -10.708 -16.686 -17.691 1.00   46.22  ? 309  VAL B CG1 1 
ATOM   4602 C CG2 . VAL B 1 309 ? -9.762  -14.729 -18.960 1.00   45.77  ? 309  VAL B CG2 1 
ATOM   4603 N N   . SER B 1 310 ? -14.394 -15.683 -19.042 1.00   48.03  ? 310  SER B N   1 
ATOM   4604 C CA  . SER B 1 310 ? -15.682 -16.194 -18.535 1.00   49.06  ? 310  SER B CA  1 
ATOM   4605 C C   . SER B 1 310 ? -16.333 -17.255 -19.419 1.00   49.08  ? 310  SER B C   1 
ATOM   4606 O O   . SER B 1 310 ? -17.090 -18.092 -18.936 1.00   48.97  ? 310  SER B O   1 
ATOM   4607 C CB  . SER B 1 310 ? -16.665 -15.037 -18.320 1.00   49.26  ? 310  SER B CB  1 
ATOM   4608 O OG  . SER B 1 310 ? -16.153 -14.112 -17.374 1.00   51.38  ? 310  SER B OG  1 
ATOM   4609 N N   . TYR B 1 311 ? -16.044 -17.191 -20.717 0.77   49.49  ? 311  TYR B N   1 
ATOM   4610 C CA  . TYR B 1 311 ? -16.388 -18.236 -21.682 0.77   49.79  ? 311  TYR B CA  1 
ATOM   4611 C C   . TYR B 1 311 ? -15.992 -19.645 -21.194 0.77   49.70  ? 311  TYR B C   1 
ATOM   4612 O O   . TYR B 1 311 ? -16.712 -20.615 -21.430 0.77   49.21  ? 311  TYR B O   1 
ATOM   4613 C CB  . TYR B 1 311 ? -15.713 -17.895 -23.020 0.77   50.13  ? 311  TYR B CB  1 
ATOM   4614 C CG  . TYR B 1 311 ? -15.589 -19.015 -24.030 0.77   51.84  ? 311  TYR B CG  1 
ATOM   4615 C CD1 . TYR B 1 311 ? -16.544 -19.180 -25.033 0.77   53.67  ? 311  TYR B CD1 1 
ATOM   4616 C CD2 . TYR B 1 311 ? -14.491 -19.883 -24.012 0.77   52.75  ? 311  TYR B CD2 1 
ATOM   4617 C CE1 . TYR B 1 311 ? -16.426 -20.200 -25.978 0.77   54.47  ? 311  TYR B CE1 1 
ATOM   4618 C CE2 . TYR B 1 311 ? -14.366 -20.906 -24.948 0.77   53.94  ? 311  TYR B CE2 1 
ATOM   4619 C CZ  . TYR B 1 311 ? -15.337 -21.056 -25.928 0.77   54.68  ? 311  TYR B CZ  1 
ATOM   4620 O OH  . TYR B 1 311 ? -15.222 -22.063 -26.864 0.77   55.58  ? 311  TYR B OH  1 
ATOM   4621 N N   . LEU B 1 312 ? -14.856 -19.743 -20.503 1.00   49.73  ? 312  LEU B N   1 
ATOM   4622 C CA  . LEU B 1 312 ? -14.328 -21.031 -20.040 1.00   50.09  ? 312  LEU B CA  1 
ATOM   4623 C C   . LEU B 1 312 ? -15.078 -21.634 -18.852 1.00   50.74  ? 312  LEU B C   1 
ATOM   4624 O O   . LEU B 1 312 ? -14.837 -22.788 -18.489 1.00   50.72  ? 312  LEU B O   1 
ATOM   4625 C CB  . LEU B 1 312 ? -12.840 -20.913 -19.698 1.00   49.49  ? 312  LEU B CB  1 
ATOM   4626 C CG  . LEU B 1 312 ? -11.865 -20.602 -20.828 1.00   48.85  ? 312  LEU B CG  1 
ATOM   4627 C CD1 . LEU B 1 312 ? -10.521 -20.184 -20.257 1.00   46.83  ? 312  LEU B CD1 1 
ATOM   4628 C CD2 . LEU B 1 312 ? -11.720 -21.792 -21.769 1.00   47.42  ? 312  LEU B CD2 1 
ATOM   4629 N N   . PHE B 1 313 ? -15.983 -20.858 -18.257 1.00   51.70  ? 313  PHE B N   1 
ATOM   4630 C CA  . PHE B 1 313 ? -16.713 -21.285 -17.057 1.00   52.93  ? 313  PHE B CA  1 
ATOM   4631 C C   . PHE B 1 313 ? -17.822 -22.302 -17.344 1.00   53.58  ? 313  PHE B C   1 
ATOM   4632 O O   . PHE B 1 313 ? -18.240 -23.041 -16.444 1.00   54.04  ? 313  PHE B O   1 
ATOM   4633 C CB  . PHE B 1 313 ? -17.295 -20.070 -16.321 1.00   52.92  ? 313  PHE B CB  1 
ATOM   4634 C CG  . PHE B 1 313 ? -16.266 -19.221 -15.614 1.00   53.12  ? 313  PHE B CG  1 
ATOM   4635 C CD1 . PHE B 1 313 ? -14.899 -19.390 -15.848 1.00   53.76  ? 313  PHE B CD1 1 
ATOM   4636 C CD2 . PHE B 1 313 ? -16.670 -18.225 -14.732 1.00   53.39  ? 313  PHE B CD2 1 
ATOM   4637 C CE1 . PHE B 1 313 ? -13.957 -18.594 -15.198 1.00   53.97  ? 313  PHE B CE1 1 
ATOM   4638 C CE2 . PHE B 1 313 ? -15.733 -17.423 -14.081 1.00   53.87  ? 313  PHE B CE2 1 
ATOM   4639 C CZ  . PHE B 1 313 ? -14.374 -17.611 -14.315 1.00   53.62  ? 313  PHE B CZ  1 
ATOM   4640 N N   . SER B 1 314 ? -18.290 -22.342 -18.588 0.73   54.29  ? 314  SER B N   1 
ATOM   4641 C CA  . SER B 1 314 ? -19.362 -23.253 -18.985 0.73   55.03  ? 314  SER B CA  1 
ATOM   4642 C C   . SER B 1 314 ? -19.013 -24.041 -20.246 0.73   55.49  ? 314  SER B C   1 
ATOM   4643 O O   . SER B 1 314 ? -19.707 -25.005 -20.599 0.73   55.50  ? 314  SER B O   1 
ATOM   4644 C CB  . SER B 1 314 ? -20.675 -22.487 -19.182 0.73   55.03  ? 314  SER B CB  1 
ATOM   4645 O OG  . SER B 1 314 ? -20.589 -21.603 -20.291 0.73   55.11  ? 314  SER B OG  1 
ATOM   4646 N N   . HIS B 1 315 ? -17.930 -23.629 -20.906 0.80   56.21  ? 315  HIS B N   1 
ATOM   4647 C CA  . HIS B 1 315 ? -17.516 -24.197 -22.184 0.80   57.05  ? 315  HIS B CA  1 
ATOM   4648 C C   . HIS B 1 315 ? -16.105 -24.769 -22.075 0.80   57.42  ? 315  HIS B C   1 
ATOM   4649 O O   . HIS B 1 315 ? -15.245 -24.200 -21.398 0.80   57.44  ? 315  HIS B O   1 
ATOM   4650 C CB  . HIS B 1 315 ? -17.555 -23.107 -23.267 0.80   57.21  ? 315  HIS B CB  1 
ATOM   4651 C CG  . HIS B 1 315 ? -17.559 -23.627 -24.676 0.80   58.19  ? 315  HIS B CG  1 
ATOM   4652 N ND1 . HIS B 1 315 ? -16.967 -24.821 -25.043 0.80   59.05  ? 315  HIS B ND1 1 
ATOM   4653 C CD2 . HIS B 1 315 ? -18.064 -23.089 -25.816 0.80   58.62  ? 315  HIS B CD2 1 
ATOM   4654 C CE1 . HIS B 1 315 ? -17.121 -25.005 -26.343 0.80   59.01  ? 315  HIS B CE1 1 
ATOM   4655 N NE2 . HIS B 1 315 ? -17.780 -23.963 -26.839 0.80   58.78  ? 315  HIS B NE2 1 
ATOM   4656 N N   . VAL B 1 316 ? -15.887 -25.901 -22.746 1.00   57.89  ? 316  VAL B N   1 
ATOM   4657 C CA  . VAL B 1 316 ? -14.579 -26.545 -22.853 1.00   58.44  ? 316  VAL B CA  1 
ATOM   4658 C C   . VAL B 1 316 ? -13.932 -26.118 -24.171 1.00   58.90  ? 316  VAL B C   1 
ATOM   4659 O O   . VAL B 1 316 ? -14.486 -26.397 -25.238 1.00   59.18  ? 316  VAL B O   1 
ATOM   4660 C CB  . VAL B 1 316 ? -14.712 -28.094 -22.860 1.00   58.36  ? 316  VAL B CB  1 
ATOM   4661 C CG1 . VAL B 1 316 ? -13.343 -28.764 -22.948 1.00   58.53  ? 316  VAL B CG1 1 
ATOM   4662 C CG2 . VAL B 1 316 ? -15.474 -28.583 -21.641 1.00   58.31  ? 316  VAL B CG2 1 
ATOM   4663 N N   . PRO B 1 317 ? -12.752 -25.462 -24.110 1.00   59.31  ? 317  PRO B N   1 
ATOM   4664 C CA  . PRO B 1 317 ? -12.099 -24.923 -25.314 1.00   59.43  ? 317  PRO B CA  1 
ATOM   4665 C C   . PRO B 1 317 ? -11.663 -26.015 -26.292 1.00   59.74  ? 317  PRO B C   1 
ATOM   4666 O O   . PRO B 1 317 ? -12.321 -26.222 -27.315 1.00   59.80  ? 317  PRO B O   1 
ATOM   4667 C CB  . PRO B 1 317 ? -10.873 -24.197 -24.754 1.00   59.45  ? 317  PRO B CB  1 
ATOM   4668 C CG  . PRO B 1 317 ? -10.580 -24.896 -23.473 1.00   59.40  ? 317  PRO B CG  1 
ATOM   4669 C CD  . PRO B 1 317 ? -11.918 -25.273 -22.907 1.00   59.26  ? 317  PRO B CD  1 
HETATM 4670 S S   . SO4 C 2 .   ? 18.705  0.226   23.124  1.00   36.96  ? 1001 SO4 A S   1 
HETATM 4671 O O1  . SO4 C 2 .   ? 18.611  1.161   22.010  1.00   37.11  ? 1001 SO4 A O1  1 
HETATM 4672 O O2  . SO4 C 2 .   ? 19.047  -1.084  22.619  1.00   36.47  ? 1001 SO4 A O2  1 
HETATM 4673 O O3  . SO4 C 2 .   ? 19.749  0.697   24.019  1.00   38.16  ? 1001 SO4 A O3  1 
HETATM 4674 O O4  . SO4 C 2 .   ? 17.439  0.173   23.840  1.00   37.32  ? 1001 SO4 A O4  1 
HETATM 4675 S S   . SO4 D 2 .   ? 30.204  -22.829 1.400   0.97   93.85  ? 1002 SO4 A S   1 
HETATM 4676 O O1  . SO4 D 2 .   ? 29.541  -21.526 1.358   0.97   93.75  ? 1002 SO4 A O1  1 
HETATM 4677 O O2  . SO4 D 2 .   ? 31.354  -22.830 0.492   0.97   94.03  ? 1002 SO4 A O2  1 
HETATM 4678 O O3  . SO4 D 2 .   ? 30.663  -23.095 2.769   0.97   93.78  ? 1002 SO4 A O3  1 
HETATM 4679 O O4  . SO4 D 2 .   ? 29.262  -23.861 0.968   0.97   93.47  ? 1002 SO4 A O4  1 
HETATM 4680 S S   . SO4 E 2 .   ? 24.282  -3.399  12.494  0.58   43.40  ? 1003 SO4 A S   1 
HETATM 4681 O O1  . SO4 E 2 .   ? 24.497  -2.241  11.619  0.58   44.01  ? 1003 SO4 A O1  1 
HETATM 4682 O O2  . SO4 E 2 .   ? 25.464  -4.261  12.476  0.58   44.58  ? 1003 SO4 A O2  1 
HETATM 4683 O O3  . SO4 E 2 .   ? 24.025  -2.890  13.838  0.58   45.38  ? 1003 SO4 A O3  1 
HETATM 4684 O O4  . SO4 E 2 .   ? 23.143  -4.185  12.033  0.58   44.06  ? 1003 SO4 A O4  1 
HETATM 4685 S S   . SO4 F 2 .   ? -14.323 -11.762 -18.497 1.00   32.46  ? 401  SO4 B S   1 
HETATM 4686 O O1  . SO4 F 2 .   ? -13.274 -11.019 -19.185 1.00   34.03  ? 401  SO4 B O1  1 
HETATM 4687 O O2  . SO4 F 2 .   ? -15.463 -11.984 -19.376 1.00   33.50  ? 401  SO4 B O2  1 
HETATM 4688 O O3  . SO4 F 2 .   ? -13.797 -13.038 -18.062 1.00   33.96  ? 401  SO4 B O3  1 
HETATM 4689 O O4  . SO4 F 2 .   ? -14.779 -10.958 -17.388 1.00   32.47  ? 401  SO4 B O4  1 
HETATM 4690 S S   . SO4 G 2 .   ? -9.391  -37.294 2.352   1.00   61.81  ? 402  SO4 B S   1 
HETATM 4691 O O1  . SO4 G 2 .   ? -8.222  -36.656 2.951   1.00   60.64  ? 402  SO4 B O1  1 
HETATM 4692 O O2  . SO4 G 2 .   ? -9.168  -37.512 0.920   1.00   60.54  ? 402  SO4 B O2  1 
HETATM 4693 O O3  . SO4 G 2 .   ? -9.625  -38.573 3.026   1.00   61.37  ? 402  SO4 B O3  1 
HETATM 4694 O O4  . SO4 G 2 .   ? -10.555 -36.425 2.532   1.00   62.25  ? 402  SO4 B O4  1 
HETATM 4695 S S   . SO4 H 2 .   ? -16.464 -18.140 -7.837  0.65   38.23  ? 403  SO4 B S   1 
HETATM 4696 O O1  . SO4 H 2 .   ? -15.058 -17.791 -7.733  0.65   39.69  ? 403  SO4 B O1  1 
HETATM 4697 O O2  . SO4 H 2 .   ? -16.966 -17.663 -9.119  0.65   40.00  ? 403  SO4 B O2  1 
HETATM 4698 O O3  . SO4 H 2 .   ? -16.596 -19.584 -7.734  0.65   39.29  ? 403  SO4 B O3  1 
HETATM 4699 O O4  . SO4 H 2 .   ? -17.229 -17.517 -6.763  0.65   39.45  ? 403  SO4 B O4  1 
HETATM 4700 O O   . HOH I 3 .   ? 8.681   -17.152 36.220  1.00   19.37  ? 1101 HOH A O   1 
HETATM 4701 O O   . HOH I 3 .   ? 21.801  -2.392  10.210  1.00   37.45  ? 1102 HOH A O   1 
HETATM 4702 O O   . HOH I 3 .   ? 20.992  -13.893 10.755  1.00   30.87  ? 1103 HOH A O   1 
HETATM 4703 O O   . HOH I 3 .   ? 1.531   -6.879  27.556  1.00   53.39  ? 1104 HOH A O   1 
HETATM 4704 O O   . HOH I 3 .   ? 47.120  -6.858  9.426   1.00   43.49  ? 1105 HOH A O   1 
HETATM 4705 O O   . HOH I 3 .   ? 4.098   -6.136  10.375  1.00   31.21  ? 1106 HOH A O   1 
HETATM 4706 O O   . HOH I 3 .   ? -4.920  -27.138 1.309   1.00   33.66  ? 1107 HOH A O   1 
HETATM 4707 O O   . HOH I 3 .   ? 9.761   -5.668  4.681   1.00   25.51  ? 1108 HOH A O   1 
HETATM 4708 O O   . HOH I 3 .   ? 6.656   -9.456  20.947  1.00   24.41  ? 1109 HOH A O   1 
HETATM 4709 O O   . HOH I 3 .   ? 8.444   -4.201  7.990   1.00   29.41  ? 1110 HOH A O   1 
HETATM 4710 O O   . HOH I 3 .   ? 16.387  2.763   21.869  1.00   26.76  ? 1111 HOH A O   1 
HETATM 4711 O O   . HOH I 3 .   ? 10.230  -1.390  1.018   1.00   37.78  ? 1112 HOH A O   1 
HETATM 4712 O O   . HOH I 3 .   ? 6.200   -23.711 21.900  1.00   21.67  ? 1113 HOH A O   1 
HETATM 4713 O O   . HOH I 3 .   ? 28.345  -12.405 21.886  1.00   38.54  ? 1114 HOH A O   1 
HETATM 4714 O O   . HOH I 3 .   ? 15.513  -3.842  -8.070  1.00   19.86  ? 1115 HOH A O   1 
HETATM 4715 O O   . HOH I 3 .   ? -5.522  -17.702 15.598  1.00   37.68  ? 1116 HOH A O   1 
HETATM 4716 O O   . HOH I 3 .   ? 20.204  -3.690  15.551  1.00   38.79  ? 1117 HOH A O   1 
HETATM 4717 O O   . HOH I 3 .   ? 9.683   -26.817 10.322  1.00   47.96  ? 1118 HOH A O   1 
HETATM 4718 O O   . HOH I 3 .   ? 6.592   -26.654 8.012   1.00   42.83  ? 1119 HOH A O   1 
HETATM 4719 O O   . HOH I 3 .   ? -3.725  -11.653 8.064   1.00   55.16  ? 1120 HOH A O   1 
HETATM 4720 O O   . HOH I 3 .   ? 22.299  -13.823 8.468   1.00   39.20  ? 1121 HOH A O   1 
HETATM 4721 O O   . HOH I 3 .   ? 24.870  -19.013 27.217  1.00   55.44  ? 1122 HOH A O   1 
HETATM 4722 O O   . HOH J 3 .   ? -4.742  -33.023 -9.930  1.00   26.14  ? 501  HOH B O   1 
HETATM 4723 O O   . HOH J 3 .   ? -13.216 -23.226 -16.547 1.00   35.72  ? 502  HOH B O   1 
HETATM 4724 O O   . HOH J 3 .   ? -3.768  -10.573 -0.149  1.00   35.95  ? 503  HOH B O   1 
HETATM 4725 O O   . HOH J 3 .   ? -15.138 -15.615 -5.738  1.00   28.50  ? 504  HOH B O   1 
HETATM 4726 O O   . HOH J 3 .   ? -3.769  -8.464  -3.218  1.00   27.32  ? 505  HOH B O   1 
HETATM 4727 O O   . HOH J 3 .   ? -18.213 -31.894 -3.367  1.00   36.61  ? 506  HOH B O   1 
HETATM 4728 O O   . HOH J 3 .   ? -15.657 -26.935 -11.263 1.00   44.04  ? 507  HOH B O   1 
HETATM 4729 O O   . HOH J 3 .   ? -13.543 -25.338 -19.689 1.00   40.30  ? 508  HOH B O   1 
HETATM 4730 O O   . HOH J 3 .   ? 1.007   -7.297  -5.624  1.00   23.60  ? 509  HOH B O   1 
HETATM 4731 O O   . HOH J 3 .   ? -5.619  -26.583 -3.096  1.00   42.96  ? 510  HOH B O   1 
HETATM 4732 O O   . HOH J 3 .   ? 14.234  -8.096  -17.287 1.00   24.49  ? 511  HOH B O   1 
HETATM 4733 O O   . HOH J 3 .   ? -10.710 -34.624 0.561   1.00   53.34  ? 512  HOH B O   1 
HETATM 4734 O O   . HOH J 3 .   ? -27.685 -42.044 -19.882 1.00   36.73  ? 513  HOH B O   1 
HETATM 4735 O O   . HOH J 3 .   ? -9.659  -13.041 12.654  1.00   31.29  ? 514  HOH B O   1 
HETATM 4736 O O   . HOH J 3 .   ? 6.865   -14.384 -26.451 1.00   34.38  ? 515  HOH B O   1 
HETATM 4737 O O   . HOH J 3 .   ? 12.731  -19.899 -24.197 1.00   46.99  ? 516  HOH B O   1 
HETATM 4738 O O   . HOH J 3 .   ? -18.162 -49.412 -8.123  1.00   30.94  ? 517  HOH B O   1 
HETATM 4739 O O   . HOH J 3 .   ? 15.588  -9.520  -11.045 1.00   28.08  ? 518  HOH B O   1 
HETATM 4740 O O   . HOH J 3 .   ? 12.136  -0.785  -17.864 1.00   39.39  ? 519  HOH B O   1 
HETATM 4741 O O   . HOH J 3 .   ? -13.114 -15.997 -11.306 1.00   33.79  ? 520  HOH B O   1 
HETATM 4742 O O   . HOH J 3 .   ? -14.955 -51.877 -10.101 1.00   63.23  ? 521  HOH B O   1 
HETATM 4743 O O   . HOH J 3 .   ? -4.700  -21.562 -26.991 1.00   55.08  ? 522  HOH B O   1 
HETATM 4744 O O   . HOH J 3 .   ? 1.185   -11.366 -16.471 1.00   20.78  ? 523  HOH B O   1 
HETATM 4745 O O   . HOH J 3 .   ? 6.646   -23.307 -7.868  1.00   39.46  ? 524  HOH B O   1 
HETATM 4746 O O   . HOH J 3 .   ? -4.138  -45.452 -13.827 1.00   47.34  ? 525  HOH B O   1 
HETATM 4747 O O   . HOH J 3 .   ? -0.925  -5.015  -9.162  1.00   36.29  ? 526  HOH B O   1 
HETATM 4748 O O   . HOH J 3 .   ? -8.006  -24.855 -3.746  1.00   30.53  ? 527  HOH B O   1 
HETATM 4749 O O   . HOH J 3 .   ? -14.217 -22.742 -6.429  1.00   30.51  ? 528  HOH B O   1 
HETATM 4750 O O   . HOH J 3 .   ? 7.190   -6.842  -25.150 1.00   47.04  ? 529  HOH B O   1 
HETATM 4751 O O   . HOH J 3 .   ? -26.732 -36.999 11.504  1.00   56.17  ? 530  HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  CYS 41  41  41  CYS CYS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  MET 68  68  68  MET MET A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  CYS 91  91  91  CYS CYS A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 HIS 123 123 123 HIS HIS A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 MET 127 127 127 MET MET A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 TRP 162 162 162 TRP TRP A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 CYS 165 165 165 CYS CYS A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 ARG 196 196 ?   ?   ?   A . n 
A 1 197 LYS 197 197 ?   ?   ?   A . n 
A 1 198 LYS 198 198 ?   ?   ?   A . n 
A 1 199 ALA 199 199 ?   ?   ?   A . n 
A 1 200 ASN 200 200 ?   ?   ?   A . n 
A 1 201 GLU 201 201 ?   ?   ?   A . n 
A 1 202 VAL 202 202 ?   ?   ?   A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 MET 205 205 205 MET MET A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 MET 222 222 222 MET MET A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 CYS 226 226 226 CYS CYS A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 CYS 230 230 230 CYS CYS A . n 
A 1 231 HIS 231 231 231 HIS HIS A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 ARG 243 243 243 ARG ARG A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 VAL 271 271 271 VAL VAL A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 PRO 276 276 276 PRO PRO A . n 
A 1 277 GLN 277 277 277 GLN GLN A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 MET 281 281 281 MET MET A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 CYS 284 284 284 CYS CYS A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 LYS 286 286 286 LYS LYS A . n 
A 1 287 ILE 287 287 287 ILE ILE A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 MET 294 294 294 MET MET A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 ILE 300 300 300 ILE ILE A . n 
A 1 301 ARG 301 301 301 ARG ARG A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 ASN 305 305 305 ASN ASN A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 PHE 313 313 313 PHE PHE A . n 
A 1 314 SER 314 314 ?   ?   ?   A . n 
A 1 315 HIS 315 315 ?   ?   ?   A . n 
A 1 316 VAL 316 316 ?   ?   ?   A . n 
A 1 317 PRO 317 317 ?   ?   ?   A . n 
A 1 318 LEU 318 318 ?   ?   ?   A . n 
A 1 319 LEU 319 319 ?   ?   ?   A . n 
A 1 320 GLU 320 320 ?   ?   ?   A . n 
A 1 321 HIS 321 321 ?   ?   ?   A . n 
A 1 322 HIS 322 322 ?   ?   ?   A . n 
A 1 323 HIS 323 323 ?   ?   ?   A . n 
A 1 324 HIS 324 324 ?   ?   ?   A . n 
A 1 325 HIS 325 325 ?   ?   ?   A . n 
A 1 326 HIS 326 326 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   ASN 3   3   3   ASN ASN B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  SER 11  11  11  SER SER B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  GLN 13  13  13  GLN GLN B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  GLN 17  17  17  GLN GLN B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  LYS 33  33  33  LYS LYS B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  PHE 35  35  35  PHE PHE B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  CYS 41  41  41  CYS CYS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  CYS 60  60  60  CYS CYS B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  MET 68  68  68  MET MET B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ILE 72  72  72  ILE ILE B . n 
B 1 73  MET 73  73  73  MET MET B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  CYS 77  77  77  CYS CYS B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  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 THR 115 115 115 THR THR 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 
# 
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)' 29400 ? 
1 MORE         -436  ? 
1 'SSA (A^2)'  59680 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -y,x-y,z  -0.5000000000 -0.8660254038 0.0000000000 0.0000000000 0.8660254038  -0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_555 -x+y,-x,z -0.5000000000 0.8660254038  0.0000000000 0.0000000000 -0.8660254038 -0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-02-04 
2 'Structure model' 1 1 2015-03-25 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .        ? 1 
MOLREP   phasing           .        ? 2 
REFMAC   refinement        5.5.0109 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   CYS 
_pdbx_validate_close_contact.auth_seq_id_1    60 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   ND2 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   ASN 
_pdbx_validate_close_contact.auth_seq_id_2    66 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
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 11  ? ? -136.01 -33.83  
2  1 HIS A 12  ? ? -69.48  92.86   
3  1 ASN A 37  ? ? -99.17  37.54   
4  1 GLU A 161 ? ? -93.57  38.18   
5  1 ASP A 224 ? ? -102.54 -82.54  
6  1 ASN A 273 ? ? -92.17  34.14   
7  1 SER B 10  ? ? 60.90   -116.49 
8  1 SER B 11  ? ? -156.22 19.72   
9  1 HIS B 12  ? ? -101.50 62.61   
10 1 ASN B 37  ? ? -107.42 41.37   
11 1 GLN B 97  ? ? -102.90 67.03   
12 1 ASP B 224 ? ? -102.38 -72.33  
# 
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 B LYS 5  ? CG ? B LYS 5  CG 
2 1 Y 1 B LYS 5  ? CD ? B LYS 5  CD 
3 1 Y 1 B LYS 5  ? CE ? B LYS 5  CE 
4 1 Y 1 B LYS 5  ? NZ ? B LYS 5  NZ 
5 1 Y 1 B LYS 18 ? NZ ? B LYS 18 NZ 
6 1 Y 1 B LYS 34 ? CG ? B LYS 34 CG 
7 1 Y 1 B LYS 34 ? CD ? B LYS 34 CD 
8 1 Y 1 B LYS 34 ? CE ? B LYS 34 CE 
9 1 Y 1 B LYS 34 ? NZ ? B LYS 34 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 PRO 2   ? A PRO 2   
3  1 Y 0 A GLY 59  ? A GLY 59  
4  1 Y 1 A ARG 196 ? A ARG 196 
5  1 Y 1 A LYS 197 ? A LYS 197 
6  1 Y 1 A LYS 198 ? A LYS 198 
7  1 Y 1 A ALA 199 ? A ALA 199 
8  1 Y 1 A ASN 200 ? A ASN 200 
9  1 Y 1 A GLU 201 ? A GLU 201 
10 1 Y 1 A VAL 202 ? A VAL 202 
11 1 Y 1 A SER 314 ? A SER 314 
12 1 Y 1 A HIS 315 ? A HIS 315 
13 1 Y 1 A VAL 316 ? A VAL 316 
14 1 Y 1 A PRO 317 ? A PRO 317 
15 1 Y 1 A LEU 318 ? A LEU 318 
16 1 Y 1 A LEU 319 ? A LEU 319 
17 1 Y 1 A GLU 320 ? A GLU 320 
18 1 Y 1 A HIS 321 ? A HIS 321 
19 1 Y 1 A HIS 322 ? A HIS 322 
20 1 Y 1 A HIS 323 ? A HIS 323 
21 1 Y 1 A HIS 324 ? A HIS 324 
22 1 Y 1 A HIS 325 ? A HIS 325 
23 1 Y 1 A HIS 326 ? A HIS 326 
24 1 Y 1 B MET 1   ? B MET 1   
25 1 Y 1 B PRO 2   ? B PRO 2   
26 1 Y 1 B ARG 196 ? B ARG 196 
27 1 Y 1 B LYS 197 ? B LYS 197 
28 1 Y 1 B LYS 198 ? B LYS 198 
29 1 Y 1 B ALA 199 ? B ALA 199 
30 1 Y 1 B ASN 200 ? B ASN 200 
31 1 Y 1 B GLU 201 ? B GLU 201 
32 1 Y 1 B VAL 202 ? B VAL 202 
33 1 Y 1 B LEU 318 ? B LEU 318 
34 1 Y 1 B LEU 319 ? B LEU 319 
35 1 Y 1 B GLU 320 ? B GLU 320 
36 1 Y 1 B HIS 321 ? B HIS 321 
37 1 Y 1 B HIS 322 ? B HIS 322 
38 1 Y 1 B HIS 323 ? B HIS 323 
39 1 Y 1 B HIS 324 ? B HIS 324 
40 1 Y 1 B HIS 325 ? B HIS 325 
41 1 Y 1 B HIS 326 ? B HIS 326 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_pdbx_reflns_twin.domain_id 
_pdbx_reflns_twin.crystal_id 
_pdbx_reflns_twin.diffrn_id 
_pdbx_reflns_twin.type 
_pdbx_reflns_twin.operator 
_pdbx_reflns_twin.fraction 
1 1 1 ? 'H, K, L'  0.673 
2 1 1 ? 'K, H, -L' 0.327 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SO4 1  1001 1001 SO4 SO4 A . 
D 2 SO4 1  1002 1004 SO4 SO4 A . 
E 2 SO4 1  1003 1006 SO4 SO4 A . 
F 2 SO4 1  401  1002 SO4 SO4 B . 
G 2 SO4 1  402  1003 SO4 SO4 B . 
H 2 SO4 1  403  1005 SO4 SO4 B . 
I 3 HOH 1  1101 5    HOH HOH A . 
I 3 HOH 2  1102 7    HOH HOH A . 
I 3 HOH 3  1103 8    HOH HOH A . 
I 3 HOH 4  1104 11   HOH HOH A . 
I 3 HOH 5  1105 13   HOH HOH A . 
I 3 HOH 6  1106 14   HOH HOH A . 
I 3 HOH 7  1107 18   HOH HOH A . 
I 3 HOH 8  1108 19   HOH HOH A . 
I 3 HOH 9  1109 22   HOH HOH A . 
I 3 HOH 10 1110 23   HOH HOH A . 
I 3 HOH 11 1111 27   HOH HOH A . 
I 3 HOH 12 1112 30   HOH HOH A . 
I 3 HOH 13 1113 31   HOH HOH A . 
I 3 HOH 14 1114 36   HOH HOH A . 
I 3 HOH 15 1115 37   HOH HOH A . 
I 3 HOH 16 1116 40   HOH HOH A . 
I 3 HOH 17 1117 46   HOH HOH A . 
I 3 HOH 18 1118 47   HOH HOH A . 
I 3 HOH 19 1119 52   HOH HOH A . 
I 3 HOH 20 1120 63   HOH HOH A . 
I 3 HOH 21 1121 65   HOH HOH A . 
I 3 HOH 22 1122 72   HOH HOH A . 
J 3 HOH 1  501  1    HOH HOH B . 
J 3 HOH 2  502  2    HOH HOH B . 
J 3 HOH 3  503  3    HOH HOH B . 
J 3 HOH 4  504  4    HOH HOH B . 
J 3 HOH 5  505  9    HOH HOH B . 
J 3 HOH 6  506  12   HOH HOH B . 
J 3 HOH 7  507  16   HOH HOH B . 
J 3 HOH 8  508  20   HOH HOH B . 
J 3 HOH 9  509  25   HOH HOH B . 
J 3 HOH 10 510  26   HOH HOH B . 
J 3 HOH 11 511  28   HOH HOH B . 
J 3 HOH 12 512  32   HOH HOH B . 
J 3 HOH 13 513  38   HOH HOH B . 
J 3 HOH 14 514  39   HOH HOH B . 
J 3 HOH 15 515  41   HOH HOH B . 
J 3 HOH 16 516  42   HOH HOH B . 
J 3 HOH 17 517  45   HOH HOH B . 
J 3 HOH 18 518  48   HOH HOH B . 
J 3 HOH 19 519  49   HOH HOH B . 
J 3 HOH 20 520  51   HOH HOH B . 
J 3 HOH 21 521  53   HOH HOH B . 
J 3 HOH 22 522  58   HOH HOH B . 
J 3 HOH 23 523  62   HOH HOH B . 
J 3 HOH 24 524  67   HOH HOH B . 
J 3 HOH 25 525  69   HOH HOH B . 
J 3 HOH 26 526  70   HOH HOH B . 
J 3 HOH 27 527  71   HOH HOH B . 
J 3 HOH 28 528  73   HOH HOH B . 
J 3 HOH 29 529  75   HOH HOH B . 
J 3 HOH 30 530  76   HOH HOH B . 
# 
