data_4HT2
# 
_entry.id   4HT2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4HT2         pdb_00004ht2 10.2210/pdb4ht2/pdb 
RCSB  RCSB075885   ?            ?                   
WWPDB D_1000075885 ?            ?                   
# 
_pdbx_database_status.entry_id                        4HT2 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2012-10-31 
_pdbx_database_status.status_code                     REL 
_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.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'4-Substituted-2,3,5,6-tetrafluorobenzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, XII, and XIII.' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            21 
_citation.page_first                2093 
_citation.page_last                 2106 
_citation.year                      2013 
_citation.journal_id_ASTM           BMECEP 
_citation.country                   UK 
_citation.journal_id_ISSN           0968-0896 
_citation.journal_id_CSD            1200 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23394791 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2013.01.008 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dudutiene, V.' 1 ? 
primary 'Zubriene, A.'  2 ? 
primary 'Smirnov, A.'   3 ? 
primary 'Gylyte, J.'    4 ? 
primary 'Timm, D.'      5 ? 
primary 'Manakova, E.'  6 ? 
primary 'Grazulis, S.'  7 ? 
primary 'Matulis, D.'   8 ? 
# 
_cell.entry_id           4HT2 
_cell.length_a           46.709 
_cell.length_b           67.261 
_cell.length_c           80.689 
_cell.angle_alpha        81.78 
_cell.angle_beta         84.01 
_cell.angle_gamma        86.48 
_cell.Z_PDB              4 
_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                         4HT2 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_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 'Carbonic anhydrase 12'                                                      29917.318 4    4.2.1.1 ? 
'human carbonic anhydrase XII' ? 
2 non-polymer syn 'ZINC ION'                                                                   65.409    4    ?       ? ? ? 
3 non-polymer syn '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' 367.342   4    ?       ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                      106.120   3    ?       ? ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                               62.068    12   ?       ? ? ? 
6 water       nat water                                                                        18.015    1504 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3' 
# 
_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       
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   SER n 
1 3   LYS n 
1 4   TRP n 
1 5   THR n 
1 6   TYR n 
1 7   PHE n 
1 8   GLY n 
1 9   PRO n 
1 10  ASP n 
1 11  GLY n 
1 12  GLU n 
1 13  ASN n 
1 14  SER n 
1 15  TRP n 
1 16  SER n 
1 17  LYS n 
1 18  LYS n 
1 19  TYR n 
1 20  PRO n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  GLY n 
1 25  LEU n 
1 26  LEU n 
1 27  GLN n 
1 28  SER n 
1 29  PRO n 
1 30  ILE n 
1 31  ASP n 
1 32  LEU n 
1 33  HIS n 
1 34  SER n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLN n 
1 39  TYR n 
1 40  ASP n 
1 41  ALA n 
1 42  SER n 
1 43  LEU n 
1 44  THR n 
1 45  PRO n 
1 46  LEU n 
1 47  GLU n 
1 48  PHE n 
1 49  GLN n 
1 50  GLY n 
1 51  TYR n 
1 52  ASN n 
1 53  LEU n 
1 54  SER n 
1 55  ALA n 
1 56  ASN n 
1 57  LYS n 
1 58  GLN n 
1 59  PHE n 
1 60  LEU n 
1 61  LEU n 
1 62  THR n 
1 63  ASN n 
1 64  ASN n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  VAL n 
1 69  LYS n 
1 70  LEU n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  ASP n 
1 76  MET n 
1 77  HIS n 
1 78  ILE n 
1 79  GLN n 
1 80  GLY n 
1 81  LEU n 
1 82  GLN n 
1 83  SER n 
1 84  ARG n 
1 85  TYR n 
1 86  SER n 
1 87  ALA n 
1 88  THR n 
1 89  GLN n 
1 90  LEU n 
1 91  HIS n 
1 92  LEU n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  ASN n 
1 97  PRO n 
1 98  ASN n 
1 99  ASP n 
1 100 PRO n 
1 101 HIS n 
1 102 GLY n 
1 103 SER n 
1 104 GLU n 
1 105 HIS n 
1 106 THR n 
1 107 VAL n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 HIS n 
1 112 PHE n 
1 113 ALA n 
1 114 ALA n 
1 115 GLU n 
1 116 LEU n 
1 117 HIS n 
1 118 ILE n 
1 119 VAL n 
1 120 HIS n 
1 121 TYR n 
1 122 ASN n 
1 123 SER n 
1 124 ASP n 
1 125 LEU n 
1 126 TYR n 
1 127 PRO n 
1 128 ASP n 
1 129 ALA n 
1 130 SER n 
1 131 THR n 
1 132 ALA n 
1 133 SER n 
1 134 ASN n 
1 135 LYS n 
1 136 SER n 
1 137 GLU n 
1 138 GLY n 
1 139 LEU n 
1 140 ALA n 
1 141 VAL n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 LEU n 
1 146 ILE n 
1 147 GLU n 
1 148 MET n 
1 149 GLY n 
1 150 SER n 
1 151 PHE n 
1 152 ASN n 
1 153 PRO n 
1 154 SER n 
1 155 TYR n 
1 156 ASP n 
1 157 LYS n 
1 158 ILE n 
1 159 PHE n 
1 160 SER n 
1 161 HIS n 
1 162 LEU n 
1 163 GLN n 
1 164 HIS n 
1 165 VAL n 
1 166 LYS n 
1 167 TYR n 
1 168 LYS n 
1 169 GLY n 
1 170 GLN n 
1 171 GLU n 
1 172 ALA n 
1 173 PHE n 
1 174 VAL n 
1 175 PRO n 
1 176 GLY n 
1 177 PHE n 
1 178 ASN n 
1 179 ILE n 
1 180 GLU n 
1 181 GLU n 
1 182 LEU n 
1 183 LEU n 
1 184 PRO n 
1 185 GLU n 
1 186 ARG n 
1 187 THR n 
1 188 ALA n 
1 189 GLU n 
1 190 TYR n 
1 191 TYR n 
1 192 ARG n 
1 193 TYR n 
1 194 ARG n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 CYS n 
1 203 ASN n 
1 204 PRO n 
1 205 THR n 
1 206 VAL n 
1 207 LEU n 
1 208 TRP n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 ARG n 
1 213 ASN n 
1 214 PRO n 
1 215 VAL n 
1 216 GLN n 
1 217 ILE n 
1 218 SER n 
1 219 GLN n 
1 220 GLU n 
1 221 GLN n 
1 222 LEU n 
1 223 LEU n 
1 224 ALA n 
1 225 LEU n 
1 226 GLU n 
1 227 THR n 
1 228 ALA n 
1 229 LEU n 
1 230 TYR n 
1 231 CYS n 
1 232 THR n 
1 233 HIS n 
1 234 MET n 
1 235 ASP n 
1 236 ASP n 
1 237 PRO n 
1 238 SER n 
1 239 PRO n 
1 240 ARG n 
1 241 GLU n 
1 242 MET n 
1 243 ILE n 
1 244 ASN n 
1 245 ASN n 
1 246 PHE n 
1 247 ARG n 
1 248 GLN n 
1 249 VAL n 
1 250 GLN n 
1 251 LYS n 
1 252 PHE n 
1 253 ASP n 
1 254 GLU n 
1 255 ARG n 
1 256 LEU n 
1 257 VAL n 
1 258 TYR n 
1 259 THR n 
1 260 SER n 
1 261 PHE n 
1 262 SER n 
1 263 GLN 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                 CA12 
_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     469008 
_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               'Rosetta(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET21a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH12_HUMAN 
_struct_ref.pdbx_db_accession          O43570 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGL
QSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSH
LQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPRE
MINNFRQVQKFDERLVYTSFSQ
;
_struct_ref.pdbx_align_begin           30 
_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 4HT2 A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 4HT2 B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 4HT2 C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 4HT2 D 2 ? 263 ? O43570 30 ? 291 ? 2 263 
# 
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 4HT2 MET A 1 ? UNP O43570 ? ? 'expression tag' 1 1 
2 4HT2 MET B 1 ? UNP O43570 ? ? 'expression tag' 1 2 
3 4HT2 MET C 1 ? UNP O43570 ? ? 'expression tag' 1 3 
4 4HT2 MET D 1 ? UNP O43570 ? ? 'expression tag' 1 4 
# 
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 
EDO non-polymer         . 1,2-ETHANEDIOL                                                               'ETHYLENE GLYCOL' 
'C2 H6 O2'           62.068  
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                      ?                 
'C4 H10 O3'          106.120 
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 
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 
V50 non-polymer         . '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' ?                 
'C12 H9 F4 N3 O2 S2' 367.342 
VAL 'L-peptide linking' y VALINE                                                                       ?                 
'C5 H11 N O2'        117.146 
ZN  non-polymer         . 'ZINC ION'                                                                   ?                 'Zn 2' 
65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4HT2 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   41.0 
_exptl_crystal.density_Matthews      2.1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              5.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
'0.1M ammonium citrate with pH 5.0 and 16% of PEG4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.temp_details    ? 
_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                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2011-11-15 
_diffrn_detector.details                'Mirror Bent, vertically focussing' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8123 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.pdbx_wavelength_list        0.8123 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
# 
_reflns.entry_id                     4HT2 
_reflns.d_resolution_high            1.450 
_reflns.d_resolution_low             27.164 
_reflns.number_all                   ? 
_reflns.number_obs                   166179 
_reflns.pdbx_netI_over_sigmaI        14.100 
_reflns.pdbx_Rsym_value              0.039 
_reflns.pdbx_redundancy              4.000 
_reflns.percent_possible_obs         97.100 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            0.039 
_reflns.B_iso_Wilson_estimate        11.3 
_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 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.45 1.53  ? 94703 ? 0.219 3.4  0.219 ? 4.00 ? 23905 95.60 1  1 
1.53 1.62  ? 90400 ? 0.148 4.9  0.148 ? 4.00 ? 22817 96.20 2  1 
1.62 1.73  ? 84748 ? 0.106 6.7  0.106 ? 4.00 ? 21391 96.50 3  1 
1.73 1.87  ? 79680 ? 0.072 8.8  0.072 ? 4.00 ? 20133 96.90 4  1 
1.87 2.05  ? 73179 ? 0.048 12.4 0.048 ? 4.00 ? 18484 97.30 5  1 
2.05 2.29  ? 66575 ? 0.036 16.2 0.036 ? 4.00 ? 16820 97.70 6  1 
2.29 2.65  ? 59016 ? 0.031 17.9 0.031 ? 4.00 ? 14905 98.10 7  1 
2.65 3.24  ? 49986 ? 0.025 15.4 0.025 ? 4.00 ? 12632 98.50 8  1 
3.24 4.59  ? 38705 ? 0.022 18.5 0.022 ? 4.00 ? 9784  98.90 9  1 
4.59 27.16 ? 19987 ? 0.022 15.7 0.022 ? 3.80 ? 5308  97.90 10 1 
# 
_refine.entry_id                                 4HT2 
_refine.ls_d_res_high                            1.450 
_refine.ls_d_res_low                             26.500 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    97.080 
_refine.ls_number_reflns_obs                     166177 
_refine.ls_number_reflns_all                     166179 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          0.154 
_refine.ls_R_factor_obs                          0.154 
_refine.ls_R_factor_R_work                       0.150 
_refine.ls_wR_factor_R_work                      0.157 
_refine.ls_R_factor_R_free                       0.188 
_refine.ls_wR_factor_R_free                      0.196 
_refine.ls_percent_reflns_R_free                 9.900 
_refine.ls_number_reflns_R_free                  16455 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               12.981 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.330 
_refine.aniso_B[2][2]                            -0.100 
_refine.aniso_B[3][3]                            0.270 
_refine.aniso_B[1][2]                            0.050 
_refine.aniso_B[1][3]                            0.020 
_refine.aniso_B[2][3]                            0.490 
_refine.correlation_coeff_Fo_to_Fc               0.970 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.overall_SU_R_Cruickshank_DPI             0.071 
_refine.overall_SU_R_free                        0.075 
_refine.pdbx_overall_ESU_R                       0.071 
_refine.pdbx_overall_ESU_R_Free                  0.075 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.900 
_refine.B_iso_max                                51.63 
_refine.B_iso_min                                2.00 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 1JD0' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_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        8392 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         165 
_refine_hist.number_atoms_solvent             1504 
_refine_hist.number_atoms_total               10061 
_refine_hist.d_res_high                       1.450 
_refine_hist.d_res_low                        26.500 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d         9207  0.031  0.021  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      12582 2.462  1.960  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   1120  7.373  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   457   37.671 24.683 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   1431  13.132 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   34    18.181 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr           1299  0.200  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     7325  0.016  0.020  ? ? 'X-RAY DIFFRACTION' 
r_nbd_refined            4473  0.228  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          6186  0.311  0.200  ? ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    1176  0.167  0.200  ? ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      13    0.037  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   165   0.260  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 126   0.175  0.200  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_it              5480  1.432  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcangle_it             8927  2.214  2.000  ? ? 'X-RAY DIFFRACTION' 
r_scbond_it              3727  3.129  3.000  ? ? 'X-RAY DIFFRACTION' 
r_scangle_it             3655  4.448  4.500  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.450 
_refine_ls_shell.d_res_low                        1.488 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               95.550 
_refine_ls_shell.number_reflns_R_work             10865 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.197 
_refine_ls_shell.R_factor_R_free                  0.271 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             1155 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                12020 
_refine_ls_shell.number_reflns_obs                10865 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4HT2 
_struct.title                     'Crystal structure of human carbonic anhydrase isozyme XII with the inhibitor.' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4HT2 
_struct_keywords.text            
;drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, catalytic activity, carbon-oxygen lyase activity, carbonate dehydratase activity, Membrane
;
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
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 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 5 ? 
I  N N 5 ? 
J  N N 5 ? 
K  N N 2 ? 
L  N N 3 ? 
M  N N 4 ? 
N  N N 5 ? 
O  N N 5 ? 
P  N N 5 ? 
Q  N N 5 ? 
R  N N 5 ? 
S  N N 2 ? 
T  N N 3 ? 
U  N N 5 ? 
V  N N 2 ? 
W  N N 3 ? 
X  N N 4 ? 
Y  N N 5 ? 
Z  N N 5 ? 
AA N N 5 ? 
BA N N 6 ? 
CA N N 6 ? 
DA N N 6 ? 
EA N N 6 ? 
# 
_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  GLY A 11  ? ASN A 13  ? GLY A 11  ASN A 13  5 ? 3  
HELX_P HELX_P2  2  SER A 14  ? TYR A 19  ? SER A 14  TYR A 19  1 ? 6  
HELX_P HELX_P3  3  PRO A 20  ? GLY A 24  ? PRO A 20  GLY A 24  5 ? 5  
HELX_P HELX_P4  4  HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P5  5  ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P6  6  ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P7  7  HIS A 161 ? VAL A 165 ? HIS A 161 VAL A 165 5 ? 5  
HELX_P HELX_P8  8  ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P9  9  GLN A 219 ? ALA A 228 ? GLN A 219 ALA A 228 1 ? 10 
HELX_P HELX_P10 10 GLY B 11  ? ASN B 13  ? GLY B 11  ASN B 13  5 ? 3  
HELX_P HELX_P11 11 SER B 14  ? TYR B 19  ? SER B 14  TYR B 19  1 ? 6  
HELX_P HELX_P12 12 PRO B 20  ? GLY B 24  ? PRO B 20  GLY B 24  5 ? 5  
HELX_P HELX_P13 13 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P14 14 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P15 15 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P16 16 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P17 17 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P18 18 GLN B 219 ? ALA B 228 ? GLN B 219 ALA B 228 1 ? 10 
HELX_P HELX_P19 19 GLY C 11  ? ASN C 13  ? GLY C 11  ASN C 13  5 ? 3  
HELX_P HELX_P20 20 SER C 14  ? TYR C 19  ? SER C 14  TYR C 19  1 ? 6  
HELX_P HELX_P21 21 PRO C 20  ? GLY C 24  ? PRO C 20  GLY C 24  5 ? 5  
HELX_P HELX_P22 22 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P23 23 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P24 24 ASN C 152 ? SER C 160 ? ASN C 152 SER C 160 1 ? 9  
HELX_P HELX_P25 25 HIS C 161 ? VAL C 165 ? HIS C 161 VAL C 165 5 ? 5  
HELX_P HELX_P26 26 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P27 27 SER C 218 ? ALA C 228 ? SER C 218 ALA C 228 1 ? 11 
HELX_P HELX_P28 28 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P29 29 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P30 30 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P31 31 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P32 32 TYR D 155 ? SER D 160 ? TYR D 155 SER D 160 1 ? 6  
HELX_P HELX_P33 33 HIS D 161 ? VAL D 165 ? HIS D 161 VAL D 165 5 ? 5  
HELX_P HELX_P34 34 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P35 35 SER D 218 ? LEU D 229 ? SER D 218 LEU D 229 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG  ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG  ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG  ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG  ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F V50 .   N23 C ? A ZN  301 A V50 302 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc5  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F V50 .   N23 B ? A ZN  301 A V50 302 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
metalc6  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F V50 .   S7  C ? A ZN  301 A V50 302 1_555 ? ? ? ? ? ? ? 2.997 ? ? 
metalc7  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 K ZN  .   ZN  ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
metalc8  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 K ZN  .   ZN  ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc9  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 K ZN  .   ZN  ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc10 metalc ? ? K ZN  .   ZN  ? ? ? 1_555 L V50 .   N23 ? ? B ZN  301 B V50 302 1_555 ? ? ? ? ? ? ? 1.986 ? ? 
metalc11 metalc ? ? C HIS 91  NE2 ? ? ? 1_555 S ZN  .   ZN  ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc12 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 S ZN  .   ZN  ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc13 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 S ZN  .   ZN  ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc14 metalc ? ? S ZN  .   ZN  ? ? ? 1_555 T V50 .   N23 ? ? C ZN  301 C V50 302 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc15 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 V ZN  .   ZN  ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc16 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 V ZN  .   ZN  ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc17 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 V ZN  .   ZN  ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
metalc18 metalc ? ? V ZN  .   ZN  ? ? ? 1_555 W V50 .   N23 ? ? D ZN  301 D V50 302 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 28  A . ? SER 28  A PRO 29  A ? PRO 29  A 1 -0.41 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 3.99  
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 -0.15 
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 5.09  
5 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 -1.47 
6 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 9.59  
7 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 -2.65 
8 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 4.07  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
D ? 2  ? 
E ? 10 ? 
F ? 6  ? 
G ? 2  ? 
H ? 10 ? 
I ? 6  ? 
J ? 2  ? 
K ? 10 ? 
L ? 6  ? 
# 
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      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
D 1 2  ? parallel      
E 1 2  ? parallel      
E 2 3  ? anti-parallel 
E 3 4  ? anti-parallel 
E 4 5  ? parallel      
E 5 6  ? anti-parallel 
E 6 7  ? anti-parallel 
E 7 8  ? anti-parallel 
E 8 9  ? anti-parallel 
E 9 10 ? anti-parallel 
F 1 2  ? anti-parallel 
F 2 3  ? anti-parallel 
F 3 4  ? anti-parallel 
F 4 5  ? anti-parallel 
F 5 6  ? parallel      
G 1 2  ? parallel      
H 1 2  ? parallel      
H 2 3  ? anti-parallel 
H 3 4  ? anti-parallel 
H 4 5  ? parallel      
H 5 6  ? anti-parallel 
H 6 7  ? anti-parallel 
H 7 8  ? anti-parallel 
H 8 9  ? anti-parallel 
H 9 10 ? anti-parallel 
I 1 2  ? anti-parallel 
I 2 3  ? anti-parallel 
I 3 4  ? anti-parallel 
I 4 5  ? anti-parallel 
I 5 6  ? parallel      
J 1 2  ? parallel      
K 1 2  ? parallel      
K 2 3  ? anti-parallel 
K 3 4  ? anti-parallel 
K 4 5  ? parallel      
K 5 6  ? anti-parallel 
K 6 7  ? anti-parallel 
K 7 8  ? anti-parallel 
K 8 9  ? anti-parallel 
K 9 10 ? anti-parallel 
L 1 2  ? anti-parallel 
L 2 3  ? anti-parallel 
L 3 4  ? anti-parallel 
L 4 5  ? anti-parallel 
L 5 6  ? 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  ASP A 31  ? LEU A 32  ? ASP A 31  LEU A 32  
A 2  THR A 106 ? VAL A 107 ? THR A 106 VAL A 107 
B 1  LEU A 37  ? TYR A 39  ? LEU A 37  TYR A 39  
B 2  VAL A 257 ? THR A 259 ? VAL A 257 THR A 259 
B 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
B 4  VAL A 206 ? PHE A 211 ? VAL A 206 PHE A 211 
B 5  LEU A 139 ? GLY A 149 ? LEU A 139 GLY A 149 
B 6  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
B 7  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
B 8  VAL A 68  ? ASN A 71  ? VAL A 68  ASN A 71  
B 9  GLN A 58  ? ASN A 63  ? GLN A 58  ASN A 63  
B 10 GLU A 171 ? PRO A 175 ? GLU A 171 PRO A 175 
C 1  GLU A 47  ? GLN A 49  ? GLU A 47  GLN A 49  
C 2  HIS A 77  ? GLN A 79  ? HIS A 77  GLN A 79  
C 3  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
C 4  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
C 5  LEU A 139 ? GLY A 149 ? LEU A 139 GLY A 149 
C 6  VAL A 215 ? SER A 218 ? VAL A 215 SER A 218 
D 1  ASP B 31  ? LEU B 32  ? ASP B 31  LEU B 32  
D 2  THR B 106 ? VAL B 107 ? THR B 106 VAL B 107 
E 1  LEU B 37  ? TYR B 39  ? LEU B 37  TYR B 39  
E 2  VAL B 257 ? THR B 259 ? VAL B 257 THR B 259 
E 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
E 4  VAL B 206 ? PHE B 211 ? VAL B 206 PHE B 211 
E 5  LEU B 139 ? GLY B 149 ? LEU B 139 GLY B 149 
E 6  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
E 7  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
E 8  VAL B 68  ? ASN B 71  ? VAL B 68  ASN B 71  
E 9  GLN B 58  ? ASN B 63  ? GLN B 58  ASN B 63  
E 10 GLU B 171 ? PRO B 175 ? GLU B 171 PRO B 175 
F 1  GLU B 47  ? GLN B 49  ? GLU B 47  GLN B 49  
F 2  HIS B 77  ? GLN B 79  ? HIS B 77  GLN B 79  
F 3  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
F 4  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
F 5  LEU B 139 ? GLY B 149 ? LEU B 139 GLY B 149 
F 6  VAL B 215 ? SER B 218 ? VAL B 215 SER B 218 
G 1  ASP C 31  ? LEU C 32  ? ASP C 31  LEU C 32  
G 2  THR C 106 ? VAL C 107 ? THR C 106 VAL C 107 
H 1  LEU C 37  ? TYR C 39  ? LEU C 37  TYR C 39  
H 2  VAL C 257 ? THR C 259 ? VAL C 257 THR C 259 
H 3  TYR C 190 ? GLY C 195 ? TYR C 190 GLY C 195 
H 4  VAL C 206 ? PHE C 211 ? VAL C 206 PHE C 211 
H 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
H 6  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
H 7  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
H 8  VAL C 68  ? ASN C 71  ? VAL C 68  ASN C 71  
H 9  GLN C 58  ? ASN C 63  ? GLN C 58  ASN C 63  
H 10 GLU C 171 ? PRO C 175 ? GLU C 171 PRO C 175 
I 1  GLU C 47  ? GLN C 49  ? GLU C 47  GLN C 49  
I 2  HIS C 77  ? GLN C 79  ? HIS C 77  GLN C 79  
I 3  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
I 4  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
I 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
I 6  VAL C 215 ? ILE C 217 ? VAL C 215 ILE C 217 
J 1  ASP D 31  ? LEU D 32  ? ASP D 31  LEU D 32  
J 2  THR D 106 ? VAL D 107 ? THR D 106 VAL D 107 
K 1  LEU D 37  ? TYR D 39  ? LEU D 37  TYR D 39  
K 2  VAL D 257 ? THR D 259 ? VAL D 257 THR D 259 
K 3  TYR D 190 ? GLY D 195 ? TYR D 190 GLY D 195 
K 4  VAL D 206 ? PHE D 211 ? VAL D 206 PHE D 211 
K 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
K 6  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
K 7  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
K 8  VAL D 68  ? ASN D 71  ? VAL D 68  ASN D 71  
K 9  GLN D 58  ? ASN D 63  ? GLN D 58  ASN D 63  
K 10 GLU D 171 ? PRO D 175 ? GLU D 171 PRO D 175 
L 1  GLU D 47  ? GLN D 49  ? GLU D 47  GLN D 49  
L 2  HIS D 77  ? GLN D 79  ? HIS D 77  GLN D 79  
L 3  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
L 4  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
L 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
L 6  VAL D 215 ? ILE D 217 ? VAL D 215 ILE D 217 
# 
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 LEU A 32  ? N LEU A 32  O THR A 106 ? O THR A 106 
B 1 2  N GLN A 38  ? N GLN A 38  O VAL A 257 ? O VAL A 257 
B 2 3  O TYR A 258 ? O TYR A 258 N ARG A 192 ? N ARG A 192 
B 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
B 4 5  O THR A 209 ? O THR A 209 N ALA A 143 ? N ALA A 143 
B 5 6  O ILE A 146 ? O ILE A 146 N ALA A 114 ? N ALA A 114 
B 6 7  O VAL A 119 ? O VAL A 119 N GLN A 89  ? N GLN A 89  
B 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
B 8 9  O ASN A 71  ? O ASN A 71  N LEU A 60  ? N LEU A 60  
B 9 10 N LEU A 61  ? N LEU A 61  O ALA A 172 ? O ALA A 172 
C 1 2  N GLU A 47  ? N GLU A 47  O GLN A 79  ? O GLN A 79  
C 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
C 3 4  N GLN A 89  ? N GLN A 89  O VAL A 119 ? O VAL A 119 
C 4 5  N ALA A 114 ? N ALA A 114 O ILE A 146 ? O ILE A 146 
C 5 6  N GLY A 149 ? N GLY A 149 O ILE A 217 ? O ILE A 217 
D 1 2  N LEU B 32  ? N LEU B 32  O THR B 106 ? O THR B 106 
E 1 2  N GLN B 38  ? N GLN B 38  O THR B 259 ? O THR B 259 
E 2 3  O TYR B 258 ? O TYR B 258 N ARG B 192 ? N ARG B 192 
E 3 4  N GLY B 195 ? N GLY B 195 O VAL B 206 ? O VAL B 206 
E 4 5  O THR B 209 ? O THR B 209 N ALA B 143 ? N ALA B 143 
E 5 6  O LEU B 142 ? O LEU B 142 N ILE B 118 ? N ILE B 118 
E 6 7  O VAL B 119 ? O VAL B 119 N GLN B 89  ? N GLN B 89  
E 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
E 8 9  O LYS B 69  ? O LYS B 69  N THR B 62  ? N THR B 62  
E 9 10 N LEU B 61  ? N LEU B 61  O ALA B 172 ? O ALA B 172 
F 1 2  N GLN B 49  ? N GLN B 49  O HIS B 77  ? O HIS B 77  
F 2 3  N ILE B 78  ? N ILE B 78  O TYR B 85  ? O TYR B 85  
F 3 4  N GLN B 89  ? N GLN B 89  O VAL B 119 ? O VAL B 119 
F 4 5  N ILE B 118 ? N ILE B 118 O LEU B 142 ? O LEU B 142 
F 5 6  N GLY B 149 ? N GLY B 149 O ILE B 217 ? O ILE B 217 
G 1 2  N LEU C 32  ? N LEU C 32  O THR C 106 ? O THR C 106 
H 1 2  N GLN C 38  ? N GLN C 38  O VAL C 257 ? O VAL C 257 
H 2 3  O TYR C 258 ? O TYR C 258 N ARG C 192 ? N ARG C 192 
H 3 4  N GLY C 195 ? N GLY C 195 O VAL C 206 ? O VAL C 206 
H 4 5  O THR C 209 ? O THR C 209 N ALA C 143 ? N ALA C 143 
H 5 6  O ILE C 146 ? O ILE C 146 N ALA C 114 ? N ALA C 114 
H 6 7  O VAL C 119 ? O VAL C 119 N GLN C 89  ? N GLN C 89  
H 7 8  O LEU C 90  ? O LEU C 90  N LEU C 70  ? N LEU C 70  
H 8 9  O LYS C 69  ? O LYS C 69  N THR C 62  ? N THR C 62  
H 9 10 N LEU C 61  ? N LEU C 61  O ALA C 172 ? O ALA C 172 
I 1 2  N GLU C 47  ? N GLU C 47  O GLN C 79  ? O GLN C 79  
I 2 3  N ILE C 78  ? N ILE C 78  O TYR C 85  ? O TYR C 85  
I 3 4  N GLN C 89  ? N GLN C 89  O VAL C 119 ? O VAL C 119 
I 4 5  N ALA C 114 ? N ALA C 114 O ILE C 146 ? O ILE C 146 
I 5 6  N GLU C 147 ? N GLU C 147 O VAL C 215 ? O VAL C 215 
J 1 2  N LEU D 32  ? N LEU D 32  O THR D 106 ? O THR D 106 
K 1 2  N GLN D 38  ? N GLN D 38  O THR D 259 ? O THR D 259 
K 2 3  O TYR D 258 ? O TYR D 258 N ARG D 192 ? N ARG D 192 
K 3 4  N GLY D 195 ? N GLY D 195 O VAL D 206 ? O VAL D 206 
K 4 5  O THR D 209 ? O THR D 209 N ALA D 143 ? N ALA D 143 
K 5 6  O ILE D 146 ? O ILE D 146 N ALA D 114 ? N ALA D 114 
K 6 7  O VAL D 119 ? O VAL D 119 N GLN D 89  ? N GLN D 89  
K 7 8  O LEU D 90  ? O LEU D 90  N LEU D 70  ? N LEU D 70  
K 8 9  O LYS D 69  ? O LYS D 69  N THR D 62  ? N THR D 62  
K 9 10 N PHE D 59  ? N PHE D 59  O VAL D 174 ? O VAL D 174 
L 1 2  N GLN D 49  ? N GLN D 49  O HIS D 77  ? O HIS D 77  
L 2 3  N ILE D 78  ? N ILE D 78  O TYR D 85  ? O TYR D 85  
L 3 4  N GLN D 89  ? N GLN D 89  O VAL D 119 ? O VAL D 119 
L 4 5  N ALA D 114 ? N ALA D 114 O ILE D 146 ? O ILE D 146 
L 5 6  N GLU D 147 ? N GLU D 147 O VAL D 215 ? O VAL D 215 
# 
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 A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A V50 302 ? 20 'BINDING SITE FOR RESIDUE V50 A 302' 
AC3 Software A PEG 303 ? 6  'BINDING SITE FOR RESIDUE PEG A 303' 
AC4 Software A EDO 304 ? 9  'BINDING SITE FOR RESIDUE EDO A 304' 
AC5 Software A EDO 305 ? 6  'BINDING SITE FOR RESIDUE EDO A 305' 
AC6 Software A EDO 306 ? 3  'BINDING SITE FOR RESIDUE EDO A 306' 
AC7 Software B ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN B 301'  
AC8 Software B V50 302 ? 14 'BINDING SITE FOR RESIDUE V50 B 302' 
AC9 Software B PEG 303 ? 9  'BINDING SITE FOR RESIDUE PEG B 303' 
BC1 Software B EDO 304 ? 8  'BINDING SITE FOR RESIDUE EDO B 304' 
BC2 Software B EDO 305 ? 6  'BINDING SITE FOR RESIDUE EDO B 305' 
BC3 Software B EDO 306 ? 6  'BINDING SITE FOR RESIDUE EDO B 306' 
BC4 Software B EDO 307 ? 4  'BINDING SITE FOR RESIDUE EDO B 307' 
BC5 Software B EDO 308 ? 4  'BINDING SITE FOR RESIDUE EDO B 308' 
BC6 Software C ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN C 301'  
BC7 Software C V50 302 ? 16 'BINDING SITE FOR RESIDUE V50 C 302' 
BC8 Software C EDO 303 ? 7  'BINDING SITE FOR RESIDUE EDO C 303' 
BC9 Software D ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN D 301'  
CC1 Software D V50 302 ? 14 'BINDING SITE FOR RESIDUE V50 D 302' 
CC2 Software D PEG 303 ? 9  'BINDING SITE FOR RESIDUE PEG D 303' 
CC3 Software D EDO 304 ? 8  'BINDING SITE FOR RESIDUE EDO D 304' 
CC4 Software D EDO 305 ? 7  'BINDING SITE FOR RESIDUE EDO D 305' 
CC5 Software D EDO 306 ? 8  'BINDING SITE FOR RESIDUE EDO D 306' 
# 
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 4  HIS A  91  ? HIS A 91  . ? 1_555 ? 
2   AC1 4  HIS A  93  ? HIS A 93  . ? 1_555 ? 
3   AC1 4  HIS A  117 ? HIS A 117 . ? 1_555 ? 
4   AC1 4  V50 F  .   ? V50 A 302 . ? 1_555 ? 
5   AC2 20 GLN A  89  ? GLN A 89  . ? 1_555 ? 
6   AC2 20 HIS A  91  ? HIS A 91  . ? 1_555 ? 
7   AC2 20 HIS A  93  ? HIS A 93  . ? 1_555 ? 
8   AC2 20 HIS A  117 ? HIS A 117 . ? 1_555 ? 
9   AC2 20 VAL A  119 ? VAL A 119 . ? 1_555 ? 
10  AC2 20 SER A  130 ? SER A 130 . ? 1_555 ? 
11  AC2 20 LEU A  139 ? LEU A 139 . ? 1_555 ? 
12  AC2 20 VAL A  141 ? VAL A 141 . ? 1_555 ? 
13  AC2 20 LEU A  197 ? LEU A 197 . ? 1_555 ? 
14  AC2 20 THR A  198 ? THR A 198 . ? 1_555 ? 
15  AC2 20 THR A  199 ? THR A 199 . ? 1_555 ? 
16  AC2 20 PRO A  200 ? PRO A 200 . ? 1_555 ? 
17  AC2 20 ASN A  203 ? ASN A 203 . ? 1_555 ? 
18  AC2 20 TRP A  208 ? TRP A 208 . ? 1_555 ? 
19  AC2 20 ZN  E  .   ? ZN  A 301 . ? 1_555 ? 
20  AC2 20 PEG G  .   ? PEG A 303 . ? 1_555 ? 
21  AC2 20 EDO H  .   ? EDO A 304 . ? 1_555 ? 
22  AC2 20 HOH BA .   ? HOH A 543 . ? 1_555 ? 
23  AC2 20 HOH BA .   ? HOH A 592 . ? 1_555 ? 
24  AC2 20 HOH BA .   ? HOH A 604 . ? 1_555 ? 
25  AC3 6  ASN A  64  ? ASN A 64  . ? 1_555 ? 
26  AC3 6  LYS A  69  ? LYS A 69  . ? 1_555 ? 
27  AC3 6  GLN A  89  ? GLN A 89  . ? 1_555 ? 
28  AC3 6  THR A  199 ? THR A 199 . ? 1_555 ? 
29  AC3 6  V50 F  .   ? V50 A 302 . ? 1_555 ? 
30  AC3 6  EDO H  .   ? EDO A 304 . ? 1_555 ? 
31  AC4 9  ASN A  64  ? ASN A 64  . ? 1_555 ? 
32  AC4 9  SER A  67  ? SER A 67  . ? 1_555 ? 
33  AC4 9  GLN A  89  ? GLN A 89  . ? 1_555 ? 
34  AC4 9  HIS A  91  ? HIS A 91  . ? 1_555 ? 
35  AC4 9  HIS A  93  ? HIS A 93  . ? 1_555 ? 
36  AC4 9  THR A  199 ? THR A 199 . ? 1_555 ? 
37  AC4 9  V50 F  .   ? V50 A 302 . ? 1_555 ? 
38  AC4 9  PEG G  .   ? PEG A 303 . ? 1_555 ? 
39  AC4 9  HOH BA .   ? HOH A 498 . ? 1_555 ? 
40  AC5 6  SER A  42  ? SER A 42  . ? 1_555 ? 
41  AC5 6  LEU A  43  ? LEU A 43  . ? 1_555 ? 
42  AC5 6  THR A  44  ? THR A 44  . ? 1_555 ? 
43  AC5 6  GLY A  80  ? GLY A 80  . ? 1_555 ? 
44  AC5 6  TYR A  190 ? TYR A 190 . ? 1_555 ? 
45  AC5 6  ARG A  192 ? ARG A 192 . ? 1_555 ? 
46  AC6 3  ASP A  40  ? ASP A 40  . ? 1_555 ? 
47  AC6 3  TYR A  258 ? TYR A 258 . ? 1_555 ? 
48  AC6 3  HOH BA .   ? HOH A 488 . ? 1_555 ? 
49  AC7 4  HIS B  91  ? HIS B 91  . ? 1_555 ? 
50  AC7 4  HIS B  93  ? HIS B 93  . ? 1_555 ? 
51  AC7 4  HIS B  117 ? HIS B 117 . ? 1_555 ? 
52  AC7 4  V50 L  .   ? V50 B 302 . ? 1_555 ? 
53  AC8 14 GLN B  89  ? GLN B 89  . ? 1_555 ? 
54  AC8 14 HIS B  91  ? HIS B 91  . ? 1_555 ? 
55  AC8 14 HIS B  93  ? HIS B 93  . ? 1_555 ? 
56  AC8 14 HIS B  117 ? HIS B 117 . ? 1_555 ? 
57  AC8 14 VAL B  119 ? VAL B 119 . ? 1_555 ? 
58  AC8 14 SER B  133 ? SER B 133 . ? 1_555 ? 
59  AC8 14 LEU B  197 ? LEU B 197 . ? 1_555 ? 
60  AC8 14 THR B  198 ? THR B 198 . ? 1_555 ? 
61  AC8 14 THR B  199 ? THR B 199 . ? 1_555 ? 
62  AC8 14 PRO B  200 ? PRO B 200 . ? 1_555 ? 
63  AC8 14 ZN  K  .   ? ZN  B 301 . ? 1_555 ? 
64  AC8 14 EDO N  .   ? EDO B 304 . ? 1_555 ? 
65  AC8 14 EDO O  .   ? EDO B 305 . ? 1_555 ? 
66  AC8 14 HOH CA .   ? HOH B 492 . ? 1_555 ? 
67  AC9 9  HIS B  164 ? HIS B 164 . ? 1_555 ? 
68  AC9 9  PHE B  173 ? PHE B 173 . ? 1_555 ? 
69  AC9 9  HOH CA .   ? HOH B 499 . ? 1_555 ? 
70  AC9 9  HOH CA .   ? HOH B 573 . ? 1_555 ? 
71  AC9 9  HOH CA .   ? HOH B 769 . ? 1_555 ? 
72  AC9 9  GLN C  58  ? GLN C 58  . ? 1_445 ? 
73  AC9 9  HIS C  161 ? HIS C 161 . ? 1_445 ? 
74  AC9 9  PHE C  173 ? PHE C 173 . ? 1_445 ? 
75  AC9 9  PRO C  175 ? PRO C 175 . ? 1_445 ? 
76  BC1 8  ASN B  64  ? ASN B 64  . ? 1_555 ? 
77  BC1 8  HIS B  66  ? HIS B 66  . ? 1_555 ? 
78  BC1 8  GLN B  89  ? GLN B 89  . ? 1_555 ? 
79  BC1 8  HIS B  91  ? HIS B 91  . ? 1_555 ? 
80  BC1 8  V50 L  .   ? V50 B 302 . ? 1_555 ? 
81  BC1 8  EDO O  .   ? EDO B 305 . ? 1_555 ? 
82  BC1 8  HOH CA .   ? HOH B 450 . ? 1_555 ? 
83  BC1 8  HOH CA .   ? HOH B 642 . ? 1_555 ? 
84  BC2 6  ASN B  64  ? ASN B 64  . ? 1_555 ? 
85  BC2 6  LYS B  69  ? LYS B 69  . ? 1_555 ? 
86  BC2 6  V50 L  .   ? V50 B 302 . ? 1_555 ? 
87  BC2 6  EDO N  .   ? EDO B 304 . ? 1_555 ? 
88  BC2 6  HOH CA .   ? HOH B 641 . ? 1_555 ? 
89  BC2 6  HOH CA .   ? HOH B 648 . ? 1_555 ? 
90  BC3 6  ASN B  71  ? ASN B 71  . ? 1_555 ? 
91  BC3 6  LEU B  72  ? LEU B 72  . ? 1_555 ? 
92  BC3 6  THR B  88  ? THR B 88  . ? 1_555 ? 
93  BC3 6  HOH CA .   ? HOH B 437 . ? 1_555 ? 
94  BC3 6  HOH CA .   ? HOH B 445 . ? 1_555 ? 
95  BC3 6  HOH CA .   ? HOH B 456 . ? 1_555 ? 
96  BC4 4  SER B  83  ? SER B 83  . ? 1_555 ? 
97  BC4 4  ASP B  124 ? ASP B 124 . ? 1_555 ? 
98  BC4 4  MET B  234 ? MET B 234 . ? 1_655 ? 
99  BC4 4  ASP B  235 ? ASP B 235 . ? 1_655 ? 
100 BC5 4  LYS B  57  ? LYS B 57  . ? 1_555 ? 
101 BC5 4  GLN B  58  ? GLN B 58  . ? 1_555 ? 
102 BC5 4  HOH CA .   ? HOH B 617 . ? 1_555 ? 
103 BC5 4  HIS C  164 ? HIS C 164 . ? 1_445 ? 
104 BC6 4  HIS C  91  ? HIS C 91  . ? 1_555 ? 
105 BC6 4  HIS C  93  ? HIS C 93  . ? 1_555 ? 
106 BC6 4  HIS C  117 ? HIS C 117 . ? 1_555 ? 
107 BC6 4  V50 T  .   ? V50 C 302 . ? 1_555 ? 
108 BC7 16 GLN C  89  ? GLN C 89  . ? 1_555 ? 
109 BC7 16 HIS C  91  ? HIS C 91  . ? 1_555 ? 
110 BC7 16 HIS C  93  ? HIS C 93  . ? 1_555 ? 
111 BC7 16 HIS C  117 ? HIS C 117 . ? 1_555 ? 
112 BC7 16 VAL C  119 ? VAL C 119 . ? 1_555 ? 
113 BC7 16 SER C  133 ? SER C 133 . ? 1_555 ? 
114 BC7 16 LEU C  139 ? LEU C 139 . ? 1_555 ? 
115 BC7 16 LEU C  197 ? LEU C 197 . ? 1_555 ? 
116 BC7 16 THR C  198 ? THR C 198 . ? 1_555 ? 
117 BC7 16 THR C  199 ? THR C 199 . ? 1_555 ? 
118 BC7 16 PRO C  200 ? PRO C 200 . ? 1_555 ? 
119 BC7 16 PRO C  201 ? PRO C 201 . ? 1_555 ? 
120 BC7 16 TRP C  208 ? TRP C 208 . ? 1_555 ? 
121 BC7 16 ZN  S  .   ? ZN  C 301 . ? 1_555 ? 
122 BC7 16 EDO U  .   ? EDO C 303 . ? 1_555 ? 
123 BC7 16 HOH DA .   ? HOH C 608 . ? 1_555 ? 
124 BC8 7  ASN C  64  ? ASN C 64  . ? 1_555 ? 
125 BC8 7  HIS C  66  ? HIS C 66  . ? 1_555 ? 
126 BC8 7  GLN C  89  ? GLN C 89  . ? 1_555 ? 
127 BC8 7  HIS C  91  ? HIS C 91  . ? 1_555 ? 
128 BC8 7  V50 T  .   ? V50 C 302 . ? 1_555 ? 
129 BC8 7  HOH DA .   ? HOH C 609 . ? 1_555 ? 
130 BC8 7  HOH DA .   ? HOH C 611 . ? 1_555 ? 
131 BC9 4  HIS D  91  ? HIS D 91  . ? 1_555 ? 
132 BC9 4  HIS D  93  ? HIS D 93  . ? 1_555 ? 
133 BC9 4  HIS D  117 ? HIS D 117 . ? 1_555 ? 
134 BC9 4  V50 W  .   ? V50 D 302 . ? 1_555 ? 
135 CC1 14 GLN D  89  ? GLN D 89  . ? 1_555 ? 
136 CC1 14 HIS D  91  ? HIS D 91  . ? 1_555 ? 
137 CC1 14 HIS D  93  ? HIS D 93  . ? 1_555 ? 
138 CC1 14 HIS D  117 ? HIS D 117 . ? 1_555 ? 
139 CC1 14 VAL D  119 ? VAL D 119 . ? 1_555 ? 
140 CC1 14 SER D  133 ? SER D 133 . ? 1_555 ? 
141 CC1 14 LEU D  197 ? LEU D 197 . ? 1_555 ? 
142 CC1 14 THR D  198 ? THR D 198 . ? 1_555 ? 
143 CC1 14 THR D  199 ? THR D 199 . ? 1_555 ? 
144 CC1 14 PRO D  200 ? PRO D 200 . ? 1_555 ? 
145 CC1 14 ZN  V  .   ? ZN  D 301 . ? 1_555 ? 
146 CC1 14 EDO Y  .   ? EDO D 304 . ? 1_555 ? 
147 CC1 14 EDO Z  .   ? EDO D 305 . ? 1_555 ? 
148 CC1 14 HOH EA .   ? HOH D 662 . ? 1_555 ? 
149 CC2 9  GLN D  163 ? GLN D 163 . ? 1_555 ? 
150 CC2 9  GLU D  220 ? GLU D 220 . ? 1_555 ? 
151 CC2 9  ALA D  224 ? ALA D 224 . ? 1_555 ? 
152 CC2 9  HOH EA .   ? HOH D 531 . ? 1_555 ? 
153 CC2 9  HOH EA .   ? HOH D 551 . ? 1_555 ? 
154 CC2 9  HOH EA .   ? HOH D 582 . ? 1_555 ? 
155 CC2 9  HOH EA .   ? HOH D 606 . ? 1_555 ? 
156 CC2 9  HOH EA .   ? HOH D 626 . ? 1_555 ? 
157 CC2 9  HOH EA .   ? HOH D 786 . ? 1_555 ? 
158 CC3 8  ASN D  64  ? ASN D 64  . ? 1_555 ? 
159 CC3 8  HIS D  66  ? HIS D 66  . ? 1_555 ? 
160 CC3 8  SER D  67  ? SER D 67  . ? 1_555 ? 
161 CC3 8  GLN D  89  ? GLN D 89  . ? 1_555 ? 
162 CC3 8  HIS D  91  ? HIS D 91  . ? 1_555 ? 
163 CC3 8  V50 W  .   ? V50 D 302 . ? 1_555 ? 
164 CC3 8  EDO Z  .   ? EDO D 305 . ? 1_555 ? 
165 CC3 8  HOH EA .   ? HOH D 664 . ? 1_555 ? 
166 CC4 7  ASN D  64  ? ASN D 64  . ? 1_555 ? 
167 CC4 7  LYS D  69  ? LYS D 69  . ? 1_555 ? 
168 CC4 7  GLN D  89  ? GLN D 89  . ? 1_555 ? 
169 CC4 7  V50 W  .   ? V50 D 302 . ? 1_555 ? 
170 CC4 7  EDO Y  .   ? EDO D 304 . ? 1_555 ? 
171 CC4 7  HOH EA .   ? HOH D 663 . ? 1_555 ? 
172 CC4 7  HOH EA .   ? HOH D 665 . ? 1_555 ? 
173 CC5 8  ALA A  55  ? ALA A 55  . ? 1_546 ? 
174 CC5 8  PRO A  175 ? PRO A 175 . ? 1_546 ? 
175 CC5 8  HOH BA .   ? HOH A 677 . ? 1_546 ? 
176 CC5 8  HOH BA .   ? HOH A 728 . ? 1_546 ? 
177 CC5 8  HOH BA .   ? HOH A 729 . ? 1_546 ? 
178 CC5 8  SER D  160 ? SER D 160 . ? 1_555 ? 
179 CC5 8  HIS D  161 ? HIS D 161 . ? 1_555 ? 
180 CC5 8  HIS D  164 ? HIS D 164 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4HT2 
_atom_sites.fract_transf_matrix[1][1]   0.021409 
_atom_sites.fract_transf_matrix[1][2]   -0.001317 
_atom_sites.fract_transf_matrix[1][3]   -0.002085 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014896 
_atom_sites.fract_transf_matrix[2][3]   -0.002069 
_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]   0.012581 
_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  
F  
N  
O  
S  
ZN 
# 
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   . LYS A  1 3   ? 1.233   21.099  9.460   1.00 25.45 ? 3   LYS A N   1 
ATOM   2     C  CA  . LYS A  1 3   ? 2.388   20.810  8.503   1.00 25.46 ? 3   LYS A CA  1 
ATOM   3     C  C   . LYS A  1 3   ? 2.197   19.314  8.127   1.00 23.04 ? 3   LYS A C   1 
ATOM   4     O  O   . LYS A  1 3   ? 1.797   18.502  8.999   1.00 22.92 ? 3   LYS A O   1 
ATOM   5     C  CB  . LYS A  1 3   ? 3.782   21.071  9.158   1.00 24.21 ? 3   LYS A CB  1 
ATOM   6     C  CG  . LYS A  1 3   ? 4.004   20.133  10.371  1.00 32.80 ? 3   LYS A CG  1 
ATOM   7     C  CD  . LYS A  1 3   ? 4.636   20.808  11.611  1.00 41.19 ? 3   LYS A CD  1 
ATOM   8     C  CE  . LYS A  1 3   ? 3.813   20.515  12.912  1.00 47.02 ? 3   LYS A CE  1 
ATOM   9     N  NZ  . LYS A  1 3   ? 3.209   19.114  13.072  1.00 48.12 ? 3   LYS A NZ  1 
ATOM   10    N  N   . TRP A  1 4   ? 2.411   18.980  6.853   1.00 17.38 ? 4   TRP A N   1 
ATOM   11    C  CA  . TRP A  1 4   ? 2.402   17.541  6.539   1.00 12.87 ? 4   TRP A CA  1 
ATOM   12    C  C   . TRP A  1 4   ? 3.520   17.215  5.539   1.00 10.95 ? 4   TRP A C   1 
ATOM   13    O  O   . TRP A  1 4   ? 3.969   18.097  4.808   1.00 11.60 ? 4   TRP A O   1 
ATOM   14    C  CB  . TRP A  1 4   ? 0.991   17.145  5.983   1.00 10.85 ? 4   TRP A CB  1 
ATOM   15    C  CG  . TRP A  1 4   ? 0.552   17.911  4.730   1.00 10.92 ? 4   TRP A CG  1 
ATOM   16    C  CD1 . TRP A  1 4   ? -0.068  19.133  4.662   1.00 9.52  ? 4   TRP A CD1 1 
ATOM   17    C  CD2 . TRP A  1 4   ? 0.835   17.486  3.348   1.00 8.94  ? 4   TRP A CD2 1 
ATOM   18    N  NE1 . TRP A  1 4   ? -0.312  19.418  3.293   1.00 10.04 ? 4   TRP A NE1 1 
ATOM   19    C  CE2 . TRP A  1 4   ? 0.316   18.475  2.486   1.00 10.21 ? 4   TRP A CE2 1 
ATOM   20    C  CE3 . TRP A  1 4   ? 1.462   16.342  2.795   1.00 8.91  ? 4   TRP A CE3 1 
ATOM   21    C  CZ2 . TRP A  1 4   ? 0.322   18.340  1.093   1.00 10.85 ? 4   TRP A CZ2 1 
ATOM   22    C  CZ3 . TRP A  1 4   ? 1.495   16.222  1.357   1.00 9.54  ? 4   TRP A CZ3 1 
ATOM   23    C  CH2 . TRP A  1 4   ? 0.949   17.203  0.560   1.00 8.73  ? 4   TRP A CH2 1 
ATOM   24    N  N   . THR A  1 5   ? 3.935   15.955  5.563   1.00 9.61  ? 5   THR A N   1 
ATOM   25    C  CA  . THR A  1 5   ? 5.033   15.508  4.717   1.00 9.68  ? 5   THR A CA  1 
ATOM   26    C  C   . THR A  1 5   ? 4.761   14.073  4.212   1.00 9.31  ? 5   THR A C   1 
ATOM   27    O  O   . THR A  1 5   ? 3.638   13.520  4.555   1.00 8.63  ? 5   THR A O   1 
ATOM   28    C  CB  . THR A  1 5   ? 6.404   15.391  5.441   1.00 9.17  ? 5   THR A CB  1 
ATOM   29    O  OG1 . THR A  1 5   ? 6.274   14.425  6.494   1.00 11.69 ? 5   THR A OG1 1 
ATOM   30    C  CG2 . THR A  1 5   ? 6.729   16.677  6.178   1.00 11.25 ? 5   THR A CG2 1 
ATOM   31    N  N   . TYR A  1 6   ? 5.718   13.441  3.547   1.00 8.89  ? 6   TYR A N   1 
ATOM   32    C  CA  . TYR A  1 6   ? 5.638   12.057  3.182   1.00 8.38  ? 6   TYR A CA  1 
ATOM   33    C  C   . TYR A  1 6   ? 6.567   11.144  3.956   1.00 7.76  ? 6   TYR A C   1 
ATOM   34    O  O   . TYR A  1 6   ? 6.756   9.964   3.647   1.00 9.06  ? 6   TYR A O   1 
ATOM   35    C  CB  . TYR A  1 6   ? 5.838   11.858  1.644   1.00 7.30  ? 6   TYR A CB  1 
ATOM   36    C  CG  . TYR A  1 6   ? 4.704   12.441  0.798   1.00 6.64  ? 6   TYR A CG  1 
ATOM   37    C  CD1 . TYR A  1 6   ? 4.748   13.759  0.370   1.00 5.95  ? 6   TYR A CD1 1 
ATOM   38    C  CD2 . TYR A  1 6   ? 3.615   11.622  0.405   1.00 5.52  ? 6   TYR A CD2 1 
ATOM   39    C  CE1 . TYR A  1 6   ? 3.772   14.299  -0.484  1.00 7.06  ? 6   TYR A CE1 1 
ATOM   40    C  CE2 . TYR A  1 6   ? 2.670   12.135  -0.397  1.00 4.98  ? 6   TYR A CE2 1 
ATOM   41    C  CZ  . TYR A  1 6   ? 2.720   13.415  -0.852  1.00 6.29  ? 6   TYR A CZ  1 
ATOM   42    O  OH  . TYR A  1 6   ? 1.811   13.941  -1.691  1.00 6.32  ? 6   TYR A OH  1 
ATOM   43    N  N   . PHE A  1 7   ? 7.250   11.717  4.989   1.00 9.75  ? 7   PHE A N   1 
ATOM   44    C  CA  . PHE A  1 7   ? 8.322   10.955  5.644   1.00 11.85 ? 7   PHE A CA  1 
ATOM   45    C  C   . PHE A  1 7   ? 8.515   11.497  7.062   1.00 14.33 ? 7   PHE A C   1 
ATOM   46    O  O   . PHE A  1 7   ? 8.581   12.730  7.253   1.00 13.16 ? 7   PHE A O   1 
ATOM   47    C  CB  . PHE A  1 7   ? 9.639   11.189  4.864   1.00 13.37 ? 7   PHE A CB  1 
ATOM   48    C  CG  . PHE A  1 7   ? 10.840  10.429  5.486   1.00 15.74 ? 7   PHE A CG  1 
ATOM   49    C  CD1 . PHE A  1 7   ? 10.905  9.084   5.543   1.00 17.77 ? 7   PHE A CD1 1 
ATOM   50    C  CD2 . PHE A  1 7   ? 11.857  11.154  6.145   1.00 25.69 ? 7   PHE A CD2 1 
ATOM   51    C  CE1 . PHE A  1 7   ? 11.969  8.404   6.124   1.00 21.12 ? 7   PHE A CE1 1 
ATOM   52    C  CE2 . PHE A  1 7   ? 12.942  10.481  6.761   1.00 27.51 ? 7   PHE A CE2 1 
ATOM   53    C  CZ  . PHE A  1 7   ? 12.982  9.090   6.727   1.00 25.14 ? 7   PHE A CZ  1 
ATOM   54    N  N   . GLY A  1 8   ? 8.450   10.549  7.985   1.00 13.75 ? 8   GLY A N   1 
ATOM   55    C  CA  . GLY A  1 8   ? 8.656   10.906  9.422   1.00 13.00 ? 8   GLY A CA  1 
ATOM   56    C  C   . GLY A  1 8   ? 7.382   11.234  10.191  1.00 13.91 ? 8   GLY A C   1 
ATOM   57    O  O   . GLY A  1 8   ? 6.278   10.766  9.798   1.00 11.96 ? 8   GLY A O   1 
ATOM   58    N  N   . PRO A  1 9   ? 7.451   11.929  11.335  1.00 12.71 ? 9   PRO A N   1 
ATOM   59    C  CA  . PRO A  1 9   ? 6.265   12.057  12.216  1.00 12.27 ? 9   PRO A CA  1 
ATOM   60    C  C   . PRO A  1 9   ? 5.104   12.744  11.556  1.00 11.24 ? 9   PRO A C   1 
ATOM   61    O  O   . PRO A  1 9   ? 3.969   12.512  12.014  1.00 14.36 ? 9   PRO A O   1 
ATOM   62    C  CB  . PRO A  1 9   ? 6.778   12.948  13.448  1.00 13.10 ? 9   PRO A CB  1 
ATOM   63    C  CG  . PRO A  1 9   ? 8.061   13.514  12.976  1.00 16.76 ? 9   PRO A CG  1 
ATOM   64    C  CD  . PRO A  1 9   ? 8.684   12.558  11.925  1.00 14.74 ? 9   PRO A CD  1 
ATOM   65    N  N   . ASP A  1 10  ? 5.310   13.560  10.487  1.00 10.74 ? 10  ASP A N   1 
ATOM   66    C  CA  . ASP A  1 10  ? 4.184   14.235  9.884   1.00 9.90  ? 10  ASP A CA  1 
ATOM   67    C  C   . ASP A  1 10  ? 3.753   13.500  8.547   1.00 8.38  ? 10  ASP A C   1 
ATOM   68    O  O   . ASP A  1 10  ? 3.009   14.120  7.745   1.00 10.30 ? 10  ASP A O   1 
ATOM   69    C  CB  . ASP A  1 10  ? 4.498   15.737  9.593   1.00 11.39 ? 10  ASP A CB  1 
ATOM   70    C  CG  . ASP A  1 10  ? 4.677   16.519  10.943  1.00 17.50 ? 10  ASP A CG  1 
ATOM   71    O  OD1 . ASP A  1 10  ? 3.926   16.212  11.907  1.00 18.20 ? 10  ASP A OD1 1 
ATOM   72    O  OD2 . ASP A  1 10  ? 5.700   17.285  10.965  1.00 23.80 ? 10  ASP A OD2 1 
ATOM   73    N  N   . GLY A  1 11  ? 4.257   12.268  8.415   1.00 7.89  ? 11  GLY A N   1 
ATOM   74    C  CA  . GLY A  1 11  ? 3.989   11.443  7.221   1.00 7.29  ? 11  GLY A CA  1 
ATOM   75    C  C   . GLY A  1 11  ? 2.569   10.842  7.214   1.00 7.15  ? 11  GLY A C   1 
ATOM   76    O  O   . GLY A  1 11  ? 1.706   11.168  8.070   1.00 8.44  ? 11  GLY A O   1 
ATOM   77    N  N   . GLU A  1 12  ? 2.333   10.016  6.174   1.00 6.45  ? 12  GLU A N   1 
ATOM   78    C  CA  . GLU A  1 12  ? 0.910   9.795   5.861   1.00 5.53  ? 12  GLU A CA  1 
ATOM   79    C  C   . GLU A  1 12  ? 0.111   8.992   6.903   1.00 4.53  ? 12  GLU A C   1 
ATOM   80    O  O   . GLU A  1 12  ? -1.108  9.128   6.949   1.00 5.75  ? 12  GLU A O   1 
ATOM   81    C  CB  . GLU A  1 12  ? 0.865   9.029   4.439   1.00 6.43  ? 12  GLU A CB  1 
ATOM   82    C  CG  . GLU A  1 12  ? 1.389   7.560   4.538   1.00 5.92  ? 12  GLU A CG  1 
ATOM   83    C  CD  . GLU A  1 12  ? 1.632   7.015   3.109   1.00 5.07  ? 12  GLU A CD  1 
ATOM   84    O  OE1 . GLU A  1 12  ? 0.646   6.558   2.483   1.00 6.03  ? 12  GLU A OE1 1 
ATOM   85    O  OE2 . GLU A  1 12  ? 2.800   7.264   2.669   1.00 5.63  ? 12  GLU A OE2 1 
ATOM   86    N  N   . ASN A  1 13  ? 0.775   8.166   7.746   1.00 5.55  ? 13  ASN A N   1 
ATOM   87    C  CA  . ASN A  1 13  ? -0.026  7.476   8.788   1.00 5.31  ? 13  ASN A CA  1 
ATOM   88    C  C   . ASN A  1 13  ? -0.480  8.449   9.891   1.00 6.26  ? 13  ASN A C   1 
ATOM   89    O  O   . ASN A  1 13  ? -1.352  8.060   10.695  1.00 6.06  ? 13  ASN A O   1 
ATOM   90    C  CB  . ASN A  1 13  ? 0.751   6.348   9.457   1.00 5.09  ? 13  ASN A CB  1 
ATOM   91    C  CG  . ASN A  1 13  ? 0.950   5.117   8.525   1.00 5.29  ? 13  ASN A CG  1 
ATOM   92    O  OD1 . ASN A  1 13  ? 0.416   5.147   7.374   1.00 5.71  ? 13  ASN A OD1 1 
ATOM   93    N  ND2 . ASN A  1 13  ? 1.700   4.150   8.945   1.00 5.09  ? 13  ASN A ND2 1 
ATOM   94    N  N   . SER A  1 14  ? 0.070   9.660   9.865   1.00 6.72  ? 14  SER A N   1 
ATOM   95    C  CA  . SER A  1 14  ? -0.313  10.727  10.864  1.00 5.39  ? 14  SER A CA  1 
ATOM   96    C  C   . SER A  1 14  ? -1.124  11.800  10.256  1.00 6.54  ? 14  SER A C   1 
ATOM   97    O  O   . SER A  1 14  ? -1.644  12.627  10.999  1.00 6.81  ? 14  SER A O   1 
ATOM   98    C  CB  . SER A  1 14  ? 1.002   11.353  11.490  1.00 8.45  ? 14  SER A CB  1 
ATOM   99    O  OG  . SER A  1 14  ? 1.626   10.351  12.298  1.00 10.76 ? 14  SER A OG  1 
ATOM   100   N  N   . TRP A  1 15  ? -1.442  11.789  8.939   1.00 5.46  ? 15  TRP A N   1 
ATOM   101   C  CA  . TRP A  1 15  ? -2.231  12.898  8.361   1.00 6.62  ? 15  TRP A CA  1 
ATOM   102   C  C   . TRP A  1 15  ? -3.580  13.000  9.048   1.00 8.02  ? 15  TRP A C   1 
ATOM   103   O  O   . TRP A  1 15  ? -4.103  14.113  9.194   1.00 9.15  ? 15  TRP A O   1 
ATOM   104   C  CB  . TRP A  1 15  ? -2.442  12.611  6.862   1.00 6.98  ? 15  TRP A CB  1 
ATOM   105   C  CG  . TRP A  1 15  ? -1.248  12.760  6.032   1.00 5.16  ? 15  TRP A CG  1 
ATOM   106   C  CD1 . TRP A  1 15  ? -0.023  13.268  6.393   1.00 6.94  ? 15  TRP A CD1 1 
ATOM   107   C  CD2 . TRP A  1 15  ? -1.144  12.459  4.625   1.00 5.09  ? 15  TRP A CD2 1 
ATOM   108   N  NE1 . TRP A  1 15  ? 0.878   13.212  5.309   1.00 7.16  ? 15  TRP A NE1 1 
ATOM   109   C  CE2 . TRP A  1 15  ? 0.171   12.786  4.206   1.00 5.76  ? 15  TRP A CE2 1 
ATOM   110   C  CE3 . TRP A  1 15  ? -2.054  11.946  3.694   1.00 4.68  ? 15  TRP A CE3 1 
ATOM   111   C  CZ2 . TRP A  1 15  ? 0.558   12.625  2.839   1.00 6.64  ? 15  TRP A CZ2 1 
ATOM   112   C  CZ3 . TRP A  1 15  ? -1.666  11.769  2.369   1.00 6.60  ? 15  TRP A CZ3 1 
ATOM   113   C  CH2 . TRP A  1 15  ? -0.360  12.099  1.960   1.00 5.42  ? 15  TRP A CH2 1 
ATOM   114   N  N   . SER A  1 16  ? -4.188  11.883  9.427   1.00 7.13  ? 16  SER A N   1 
ATOM   115   C  CA  . SER A  1 16  ? -5.564  11.909  10.056  1.00 7.69  ? 16  SER A CA  1 
ATOM   116   C  C   . SER A  1 16  ? -5.555  12.734  11.329  1.00 10.04 ? 16  SER A C   1 
ATOM   117   O  O   . SER A  1 16  ? -6.685  13.130  11.709  1.00 9.59  ? 16  SER A O   1 
ATOM   118   C  CB  . SER A  1 16  ? -6.030  10.438  10.322  1.00 8.19  ? 16  SER A CB  1 
ATOM   119   O  OG  . SER A  1 16  ? -5.186  9.907   11.336  1.00 7.52  ? 16  SER A OG  1 
ATOM   120   N  N   . LYS A  1 17  ? -4.405  12.917  12.002  1.00 8.64  ? 17  LYS A N   1 
ATOM   121   C  CA  . LYS A  1 17  ? -4.400  13.782  13.214  1.00 10.75 ? 17  LYS A CA  1 
ATOM   122   C  C   . LYS A  1 17  ? -4.699  15.238  12.863  1.00 13.32 ? 17  LYS A C   1 
ATOM   123   O  O   . LYS A  1 17  ? -5.675  15.907  13.408  1.00 17.52 ? 17  LYS A O   1 
ATOM   124   C  CB  . LYS A  1 17  ? -3.103  13.619  14.025  1.00 11.47 ? 17  LYS A CB  1 
ATOM   125   C  CG  . LYS A  1 17  ? -2.893  12.185  14.438  1.00 16.38 ? 17  LYS A CG  1 
ATOM   126   C  CD  . LYS A  1 17  ? -1.621  12.133  15.241  1.00 20.12 ? 17  LYS A CD  1 
ATOM   127   C  CE  . LYS A  1 17  ? -0.612  11.134  14.823  1.00 17.78 ? 17  LYS A CE  1 
ATOM   128   N  NZ  . LYS A  1 17  ? 0.815   11.406  15.285  1.00 20.98 ? 17  LYS A NZ  1 
ATOM   129   N  N   . LYS A  1 18  ? -4.100  15.816  11.840  1.00 9.99  ? 18  LYS A N   1 
ATOM   130   C  CA  . LYS A  1 18  ? -4.452  17.208  11.516  1.00 11.70 ? 18  LYS A CA  1 
ATOM   131   C  C   . LYS A  1 18  ? -5.559  17.318  10.538  1.00 9.56  ? 18  LYS A C   1 
ATOM   132   O  O   . LYS A  1 18  ? -6.234  18.381  10.429  1.00 14.21 ? 18  LYS A O   1 
ATOM   133   C  CB  . LYS A  1 18  ? -3.279  18.050  10.983  1.00 14.40 ? 18  LYS A CB  1 
ATOM   134   C  CG  . LYS A  1 18  ? -2.339  18.557  12.058  0.01 12.25 ? 18  LYS A CG  1 
ATOM   135   C  CD  . LYS A  1 18  ? -1.126  19.243  11.446  0.01 12.13 ? 18  LYS A CD  1 
ATOM   136   C  CE  . LYS A  1 18  ? -0.267  19.915  12.507  0.01 12.05 ? 18  LYS A CE  1 
ATOM   137   N  NZ  . LYS A  1 18  ? 0.256   18.950  13.516  0.01 11.82 ? 18  LYS A NZ  1 
ATOM   138   N  N   . TYR A  1 19  ? -5.884  16.236  9.745   1.00 9.37  ? 19  TYR A N   1 
ATOM   139   C  CA  . TYR A  1 19  ? -6.852  16.341  8.632   1.00 9.55  ? 19  TYR A CA  1 
ATOM   140   C  C   . TYR A  1 19  ? -7.796  15.172  8.734   1.00 9.85  ? 19  TYR A C   1 
ATOM   141   O  O   . TYR A  1 19  ? -7.457  14.068  8.274   1.00 10.26 ? 19  TYR A O   1 
ATOM   142   C  CB  . TYR A  1 19  ? -6.067  16.305  7.301   1.00 10.33 ? 19  TYR A CB  1 
ATOM   143   C  CG  . TYR A  1 19  ? -5.040  17.460  7.155   1.00 11.57 ? 19  TYR A CG  1 
ATOM   144   C  CD1 . TYR A  1 19  ? -3.685  17.264  7.462   1.00 10.35 ? 19  TYR A CD1 1 
ATOM   145   C  CD2 . TYR A  1 19  ? -5.457  18.694  6.676   1.00 12.42 ? 19  TYR A CD2 1 
ATOM   146   C  CE1 . TYR A  1 19  ? -2.747  18.325  7.401   1.00 13.69 ? 19  TYR A CE1 1 
ATOM   147   C  CE2 . TYR A  1 19  ? -4.478  19.760  6.552   1.00 13.22 ? 19  TYR A CE2 1 
ATOM   148   C  CZ  . TYR A  1 19  ? -3.188  19.518  6.955   1.00 12.45 ? 19  TYR A CZ  1 
ATOM   149   O  OH  . TYR A  1 19  ? -2.270  20.631  6.848   1.00 17.84 ? 19  TYR A OH  1 
ATOM   150   N  N   . PRO A  1 20  ? -8.901  15.309  9.424   1.00 7.41  ? 20  PRO A N   1 
ATOM   151   C  CA  . PRO A  1 20  ? -9.657  14.137  9.704   1.00 8.59  ? 20  PRO A CA  1 
ATOM   152   C  C   . PRO A  1 20  ? -10.160 13.342  8.490   1.00 7.58  ? 20  PRO A C   1 
ATOM   153   O  O   . PRO A  1 20  ? -10.326 12.087  8.632   1.00 7.24  ? 20  PRO A O   1 
ATOM   154   C  CB  . PRO A  1 20  ? -10.818 14.665  10.537  1.00 11.03 ? 20  PRO A CB  1 
ATOM   155   C  CG  . PRO A  1 20  ? -10.450 16.099  10.982  1.00 10.44 ? 20  PRO A CG  1 
ATOM   156   C  CD  . PRO A  1 20  ? -9.381  16.537  10.168  1.00 8.81  ? 20  PRO A CD  1 
ATOM   157   N  N   . SER A  1 21  ? -10.392 14.002  7.366   1.00 7.59  ? 21  SER A N   1 
ATOM   158   C  CA  . SER A  1 21  ? -10.873 13.236  6.214   1.00 7.22  ? 21  SER A CA  1 
ATOM   159   C  C   . SER A  1 21  ? -9.799  12.192  5.768   1.00 7.45  ? 21  SER A C   1 
ATOM   160   O  O   . SER A  1 21  ? -10.204 11.189  5.105   1.00 6.92  ? 21  SER A O   1 
ATOM   161   C  CB  . SER A  1 21  ? -11.252 14.099  5.077   1.00 8.11  ? 21  SER A CB  1 
ATOM   162   O  OG  . SER A  1 21  ? -12.388 14.911  5.444   1.00 9.31  ? 21  SER A OG  1 
ATOM   163   N  N   . CYS A  1 22  ? -8.516  12.383  6.104   1.00 6.87  ? 22  CYS A N   1 
ATOM   164   C  CA  . CYS A  1 22  ? -7.498  11.364  5.731   1.00 5.85  ? 22  CYS A CA  1 
ATOM   165   C  C   . CYS A  1 22  ? -7.703  10.039  6.363   1.00 7.13  ? 22  CYS A C   1 
ATOM   166   O  O   . CYS A  1 22  ? -7.149  9.021   5.817   1.00 7.12  ? 22  CYS A O   1 
ATOM   167   C  CB  . CYS A  1 22  ? -6.062  11.912  5.979   1.00 6.27  ? 22  CYS A CB  1 
ATOM   168   S  SG  . CYS A  1 22  ? -5.693  13.484  5.081   1.00 7.88  ? 22  CYS A SG  1 
ATOM   169   N  N   . GLY A  1 23  ? -8.498  9.959   7.483   1.00 6.46  ? 23  GLY A N   1 
ATOM   170   C  CA  . GLY A  1 23  ? -8.908  8.693   8.053   1.00 7.31  ? 23  GLY A CA  1 
ATOM   171   C  C   . GLY A  1 23  ? -10.352 8.327   7.724   1.00 8.69  ? 23  GLY A C   1 
ATOM   172   O  O   . GLY A  1 23  ? -10.907 7.398   8.340   1.00 8.84  ? 23  GLY A O   1 
ATOM   173   N  N   . GLY A  1 24  ? -10.983 9.047   6.828   1.00 8.02  ? 24  GLY A N   1 
ATOM   174   C  CA  . GLY A  1 24  ? -12.345 8.793   6.510   1.00 8.58  ? 24  GLY A CA  1 
ATOM   175   C  C   . GLY A  1 24  ? -12.562 7.834   5.337   1.00 8.72  ? 24  GLY A C   1 
ATOM   176   O  O   . GLY A  1 24  ? -11.651 7.050   4.971   1.00 9.84  ? 24  GLY A O   1 
ATOM   177   N  N   . LEU A  1 25  ? -13.754 7.988   4.772   1.00 9.84  ? 25  LEU A N   1 
ATOM   178   C  CA  . LEU A  1 25  ? -14.123 7.118   3.711   1.00 9.94  ? 25  LEU A CA  1 
ATOM   179   C  C   . LEU A  1 25  ? -13.589 7.580   2.346   1.00 9.95  ? 25  LEU A C   1 
ATOM   180   O  O   . LEU A  1 25  ? -13.154 8.753   2.141   1.00 9.21  ? 25  LEU A O   1 
ATOM   181   C  CB  . LEU A  1 25  ? -15.671 7.056   3.600   1.00 11.56 ? 25  LEU A CB  1 
ATOM   182   C  CG  . LEU A  1 25  ? -16.346 6.456   4.867   1.00 16.01 ? 25  LEU A CG  1 
ATOM   183   C  CD1 . LEU A  1 25  ? -17.842 6.661   4.705   1.00 17.64 ? 25  LEU A CD1 1 
ATOM   184   C  CD2 . LEU A  1 25  ? -16.020 4.963   5.129   1.00 14.22 ? 25  LEU A CD2 1 
ATOM   185   N  N   . LEU A  1 26  ? -13.761 6.690   1.347   1.00 10.54 ? 26  LEU A N   1 
ATOM   186   C  CA  . LEU A  1 26  ? -13.546 7.033   -0.134  1.00 10.04 ? 26  LEU A CA  1 
ATOM   187   C  C   . LEU A  1 26  ? -12.078 7.512   -0.447  1.00 7.91  ? 26  LEU A C   1 
ATOM   188   O  O   . LEU A  1 26  ? -11.888 8.326   -1.366  1.00 8.44  ? 26  LEU A O   1 
ATOM   189   C  CB  . LEU A  1 26  ? -14.559 8.067   -0.645  1.00 10.96 ? 26  LEU A CB  1 
ATOM   190   C  CG  . LEU A  1 26  ? -16.059 7.686   -0.590  1.00 14.91 ? 26  LEU A CG  1 
ATOM   191   C  CD1 . LEU A  1 26  ? -16.939 8.887   -1.054  1.00 18.04 ? 26  LEU A CD1 1 
ATOM   192   C  CD2 . LEU A  1 26  ? -16.368 6.459   -1.357  1.00 18.28 ? 26  LEU A CD2 1 
ATOM   193   N  N   . GLN A  1 27  ? -11.136 7.014   0.303   1.00 7.12  ? 27  GLN A N   1 
ATOM   194   C  CA  . GLN A  1 27  ? -9.759  7.547   0.105   1.00 6.67  ? 27  GLN A CA  1 
ATOM   195   C  C   . GLN A  1 27  ? -9.066  6.925   -1.147  1.00 6.91  ? 27  GLN A C   1 
ATOM   196   O  O   . GLN A  1 27  ? -9.291  5.797   -1.563  1.00 6.57  ? 27  GLN A O   1 
ATOM   197   C  CB  . GLN A  1 27  ? -8.888  7.232   1.333   1.00 6.18  ? 27  GLN A CB  1 
ATOM   198   C  CG  . GLN A  1 27  ? -9.355  7.962   2.553   1.00 7.44  ? 27  GLN A CG  1 
ATOM   199   C  CD  . GLN A  1 27  ? -9.216  9.450   2.441   1.00 6.42  ? 27  GLN A CD  1 
ATOM   200   O  OE1 . GLN A  1 27  ? -10.310 10.114  2.153   1.00 9.29  ? 27  GLN A OE1 1 
ATOM   201   N  NE2 . GLN A  1 27  ? -8.099  9.969   2.545   1.00 3.72  ? 27  GLN A NE2 1 
ATOM   202   N  N   . SER A  1 28  ? -8.256  7.813   -1.738  1.00 5.31  ? 28  SER A N   1 
ATOM   203   C  CA  . SER A  1 28  ? -7.396  7.497   -2.883  1.00 5.87  ? 28  SER A CA  1 
ATOM   204   C  C   . SER A  1 28  ? -5.948  7.650   -2.452  1.00 5.98  ? 28  SER A C   1 
ATOM   205   O  O   . SER A  1 28  ? -5.628  8.316   -1.484  1.00 5.18  ? 28  SER A O   1 
ATOM   206   C  CB  . SER A  1 28  ? -7.702  8.542   -3.977  1.00 5.87  ? 28  SER A CB  1 
ATOM   207   O  OG  . SER A  1 28  ? -9.028  8.364   -4.473  1.00 5.35  ? 28  SER A OG  1 
ATOM   208   N  N   . PRO A  1 29  ? -4.972  7.067   -3.226  1.00 4.13  ? 29  PRO A N   1 
ATOM   209   C  CA  . PRO A  1 29  ? -5.149  6.277   -4.460  1.00 5.92  ? 29  PRO A CA  1 
ATOM   210   C  C   . PRO A  1 29  ? -5.408  4.801   -4.091  1.00 3.99  ? 29  PRO A C   1 
ATOM   211   O  O   . PRO A  1 29  ? -5.513  4.420   -2.902  1.00 4.73  ? 29  PRO A O   1 
ATOM   212   C  CB  . PRO A  1 29  ? -3.779  6.447   -5.133  1.00 4.80  ? 29  PRO A CB  1 
ATOM   213   C  CG  . PRO A  1 29  ? -2.791  6.323   -3.919  1.00 4.61  ? 29  PRO A CG  1 
ATOM   214   C  CD  . PRO A  1 29  ? -3.539  7.199   -2.857  1.00 5.55  ? 29  PRO A CD  1 
ATOM   215   N  N   . ILE A  1 30  ? -5.627  4.015   -5.141  1.00 4.57  ? 30  ILE A N   1 
ATOM   216   C  CA  . ILE A  1 30  ? -6.029  2.568   -4.985  1.00 5.39  ? 30  ILE A CA  1 
ATOM   217   C  C   . ILE A  1 30  ? -5.230  1.769   -6.012  1.00 4.56  ? 30  ILE A C   1 
ATOM   218   O  O   . ILE A  1 30  ? -4.690  2.281   -7.022  1.00 5.67  ? 30  ILE A O   1 
ATOM   219   C  CB  . ILE A  1 30  ? -7.570  2.344   -5.104  1.00 5.52  ? 30  ILE A CB  1 
ATOM   220   C  CG1 . ILE A  1 30  ? -7.949  2.802   -6.527  1.00 5.06  ? 30  ILE A CG1 1 
ATOM   221   C  CG2 . ILE A  1 30  ? -8.316  3.113   -4.038  1.00 8.94  ? 30  ILE A CG2 1 
ATOM   222   C  CD1 . ILE A  1 30  ? -9.445  2.411   -6.846  1.00 7.73  ? 30  ILE A CD1 1 
ATOM   223   N  N   . ASP A  1 31  ? -5.198  0.435   -5.742  1.00 4.73  ? 31  ASP A N   1 
ATOM   224   C  CA  . ASP A  1 31  ? -4.669  -0.534  -6.769  1.00 5.10  ? 31  ASP A CA  1 
ATOM   225   C  C   . ASP A  1 31  ? -5.859  -0.956  -7.655  1.00 6.16  ? 31  ASP A C   1 
ATOM   226   O  O   . ASP A  1 31  ? -6.865  -1.416  -7.217  1.00 7.37  ? 31  ASP A O   1 
ATOM   227   C  CB  . ASP A  1 31  ? -4.038  -1.761  -6.072  1.00 6.69  ? 31  ASP A CB  1 
ATOM   228   C  CG  . ASP A  1 31  ? -3.607  -2.761  -7.074  1.00 6.24  ? 31  ASP A CG  1 
ATOM   229   O  OD1 . ASP A  1 31  ? -2.760  -2.450  -7.869  1.00 7.63  ? 31  ASP A OD1 1 
ATOM   230   O  OD2 . ASP A  1 31  ? -4.160  -3.904  -6.992  1.00 10.80 ? 31  ASP A OD2 1 
ATOM   231   N  N   . LEU A  1 32  ? -5.588  -0.796  -8.959  1.00 7.03  ? 32  LEU A N   1 
ATOM   232   C  CA  . LEU A  1 32  ? -6.609  -1.114  -9.964  1.00 8.19  ? 32  LEU A CA  1 
ATOM   233   C  C   . LEU A  1 32  ? -6.357  -2.532  -10.387 1.00 6.02  ? 32  LEU A C   1 
ATOM   234   O  O   . LEU A  1 32  ? -5.336  -2.827  -11.037 1.00 7.76  ? 32  LEU A O   1 
ATOM   235   C  CB  . LEU A  1 32  ? -6.439  -0.141  -11.194 1.00 6.73  ? 32  LEU A CB  1 
ATOM   236   C  CG  . LEU A  1 32  ? -6.563  1.331   -10.695 1.00 7.70  ? 32  LEU A CG  1 
ATOM   237   C  CD1 . LEU A  1 32  ? -5.926  2.377   -11.783 1.00 9.81  ? 32  LEU A CD1 1 
ATOM   238   C  CD2 . LEU A  1 32  ? -7.966  1.759   -10.421 1.00 8.72  ? 32  LEU A CD2 1 
ATOM   239   N  N   . HIS A  1 33  ? -7.225  -3.484  -9.990  1.00 8.43  ? 33  HIS A N   1 
ATOM   240   C  CA  . HIS A  1 33  ? -6.954  -4.880  -10.223 1.00 7.28  ? 33  HIS A CA  1 
ATOM   241   C  C   . HIS A  1 33  ? -8.314  -5.548  -10.539 1.00 8.09  ? 33  HIS A C   1 
ATOM   242   O  O   . HIS A  1 33  ? -9.349  -5.023  -10.151 1.00 9.06  ? 33  HIS A O   1 
ATOM   243   C  CB  . HIS A  1 33  ? -6.234  -5.592  -9.054  1.00 9.65  ? 33  HIS A CB  1 
ATOM   244   C  CG  . HIS A  1 33  ? -6.994  -5.581  -7.750  1.00 11.48 ? 33  HIS A CG  1 
ATOM   245   N  ND1 . HIS A  1 33  ? -7.044  -4.472  -6.912  1.00 16.32 ? 33  HIS A ND1 1 
ATOM   246   C  CD2 . HIS A  1 33  ? -7.695  -6.572  -7.119  1.00 11.68 ? 33  HIS A CD2 1 
ATOM   247   C  CE1 . HIS A  1 33  ? -7.735  -4.800  -5.807  1.00 16.20 ? 33  HIS A CE1 1 
ATOM   248   N  NE2 . HIS A  1 33  ? -8.150  -6.065  -5.937  1.00 11.74 ? 33  HIS A NE2 1 
ATOM   249   N  N   A SER A  1 34  ? -8.198  -6.759  -11.158 0.50 9.65  ? 34  SER A N   1 
ATOM   250   N  N   B SER A  1 34  ? -8.312  -6.723  -11.241 0.50 10.59 ? 34  SER A N   1 
ATOM   251   C  CA  A SER A  1 34  ? -9.370  -7.389  -11.783 0.50 10.58 ? 34  SER A CA  1 
ATOM   252   C  CA  B SER A  1 34  ? -9.595  -7.304  -11.786 0.50 10.27 ? 34  SER A CA  1 
ATOM   253   C  C   A SER A  1 34  ? -10.581 -7.540  -10.878 0.50 11.31 ? 34  SER A C   1 
ATOM   254   C  C   B SER A  1 34  ? -10.732 -7.404  -10.778 0.50 11.21 ? 34  SER A C   1 
ATOM   255   O  O   A SER A  1 34  ? -11.697 -7.401  -11.334 0.50 11.21 ? 34  SER A O   1 
ATOM   256   O  O   B SER A  1 34  ? -11.943 -7.148  -11.037 0.50 10.27 ? 34  SER A O   1 
ATOM   257   C  CB  A SER A  1 34  ? -8.982  -8.753  -12.306 0.50 11.13 ? 34  SER A CB  1 
ATOM   258   C  CB  B SER A  1 34  ? -9.333  -8.720  -12.281 0.50 11.82 ? 34  SER A CB  1 
ATOM   259   O  OG  A SER A  1 34  ? -8.618  -9.583  -11.237 0.50 11.93 ? 34  SER A OG  1 
ATOM   260   O  OG  B SER A  1 34  ? -8.197  -8.747  -13.142 0.50 14.31 ? 34  SER A OG  1 
ATOM   261   N  N   . ASP A  1 35  ? -10.373 -7.885  -9.593  1.00 11.08 ? 35  ASP A N   1 
ATOM   262   C  CA  . ASP A  1 35  ? -11.455 -8.208  -8.668  1.00 11.59 ? 35  ASP A CA  1 
ATOM   263   C  C   . ASP A  1 35  ? -12.374 -7.052  -8.390  1.00 12.64 ? 35  ASP A C   1 
ATOM   264   O  O   . ASP A  1 35  ? -13.567 -7.209  -7.903  1.00 14.87 ? 35  ASP A O   1 
ATOM   265   C  CB  . ASP A  1 35  ? -10.843 -8.708  -7.282  1.00 10.76 ? 35  ASP A CB  1 
ATOM   266   C  CG  . ASP A  1 35  ? -9.802  -9.795  -7.438  1.00 16.24 ? 35  ASP A CG  1 
ATOM   267   O  OD1 . ASP A  1 35  ? -8.690  -9.535  -7.916  1.00 18.67 ? 35  ASP A OD1 1 
ATOM   268   O  OD2 . ASP A  1 35  ? -10.070 -10.990 -6.991  1.00 14.45 ? 35  ASP A OD2 1 
ATOM   269   N  N   A ILE A  1 36  ? -11.856 -5.875  -8.733  0.50 11.91 ? 36  ILE A N   1 
ATOM   270   N  N   B ILE A  1 36  ? -11.877 -5.795  -8.547  0.50 10.32 ? 36  ILE A N   1 
ATOM   271   C  CA  A ILE A  1 36  ? -12.511 -4.731  -8.342  0.50 11.69 ? 36  ILE A CA  1 
ATOM   272   C  CA  B ILE A  1 36  ? -12.687 -4.603  -8.310  0.50 10.88 ? 36  ILE A CA  1 
ATOM   273   C  C   A ILE A  1 36  ? -12.925 -3.853  -9.541  0.50 11.49 ? 36  ILE A C   1 
ATOM   274   C  C   B ILE A  1 36  ? -13.099 -3.838  -9.586  0.50 9.96  ? 36  ILE A C   1 
ATOM   275   O  O   A ILE A  1 36  ? -13.446 -2.787  -9.330  0.50 10.46 ? 36  ILE A O   1 
ATOM   276   O  O   B ILE A  1 36  ? -13.758 -2.798  -9.450  0.50 11.65 ? 36  ILE A O   1 
ATOM   277   C  CB  A ILE A  1 36  ? -11.735 -4.079  -7.157  0.50 12.65 ? 36  ILE A CB  1 
ATOM   278   C  CB  B ILE A  1 36  ? -12.145 -3.621  -7.148  0.50 8.35  ? 36  ILE A CB  1 
ATOM   279   C  CG1 A ILE A  1 36  ? -10.328 -3.673  -7.620  0.50 12.47 ? 36  ILE A CG1 1 
ATOM   280   C  CG1 B ILE A  1 36  ? -10.779 -3.018  -7.591  0.50 9.94  ? 36  ILE A CG1 1 
ATOM   281   C  CG2 A ILE A  1 36  ? -11.757 -5.062  -5.960  0.50 13.87 ? 36  ILE A CG2 1 
ATOM   282   C  CG2 B ILE A  1 36  ? -12.094 -4.469  -5.800  0.50 11.27 ? 36  ILE A CG2 1 
ATOM   283   C  CD1 A ILE A  1 36  ? -10.330 -2.429  -8.409  0.50 12.09 ? 36  ILE A CD1 1 
ATOM   284   C  CD1 B ILE A  1 36  ? -10.186 -1.941  -6.772  0.50 11.23 ? 36  ILE A CD1 1 
ATOM   285   N  N   . LEU A  1 37  ? -12.702 -4.385  -10.746 1.00 11.10 ? 37  LEU A N   1 
ATOM   286   C  CA  . LEU A  1 37  ? -13.012 -3.675  -12.047 1.00 11.80 ? 37  LEU A CA  1 
ATOM   287   C  C   . LEU A  1 37  ? -14.325 -4.088  -12.657 1.00 14.20 ? 37  LEU A C   1 
ATOM   288   O  O   . LEU A  1 37  ? -14.614 -5.271  -12.626 1.00 14.89 ? 37  LEU A O   1 
ATOM   289   C  CB  . LEU A  1 37  ? -11.904 -3.916  -13.032 1.00 10.04 ? 37  LEU A CB  1 
ATOM   290   C  CG  . LEU A  1 37  ? -10.553 -3.330  -12.587 1.00 11.22 ? 37  LEU A CG  1 
ATOM   291   C  CD1 . LEU A  1 37  ? -9.567  -3.792  -13.600 1.00 17.16 ? 37  LEU A CD1 1 
ATOM   292   C  CD2 . LEU A  1 37  ? -10.551 -1.851  -12.526 1.00 11.54 ? 37  LEU A CD2 1 
ATOM   293   N  N   . GLN A  1 38  ? -15.046 -3.171  -13.271 1.00 9.24  ? 38  GLN A N   1 
ATOM   294   C  CA  . GLN A  1 38  ? -16.166 -3.660  -14.110 1.00 10.38 ? 38  GLN A CA  1 
ATOM   295   C  C   . GLN A  1 38  ? -16.276 -2.697  -15.322 1.00 10.32 ? 38  GLN A C   1 
ATOM   296   O  O   . GLN A  1 38  ? -16.367 -1.484  -15.146 1.00 9.02  ? 38  GLN A O   1 
ATOM   297   C  CB  . GLN A  1 38  ? -17.409 -3.654  -13.304 1.00 13.39 ? 38  GLN A CB  1 
ATOM   298   C  CG  . GLN A  1 38  ? -18.622 -4.240  -14.006 1.00 16.82 ? 38  GLN A CG  1 
ATOM   299   C  CD  . GLN A  1 38  ? -19.796 -4.336  -13.087 1.00 22.15 ? 38  GLN A CD  1 
ATOM   300   O  OE1 . GLN A  1 38  ? -20.547 -3.350  -12.943 1.00 23.76 ? 38  GLN A OE1 1 
ATOM   301   N  NE2 . GLN A  1 38  ? -19.904 -5.485  -12.343 1.00 24.50 ? 38  GLN A NE2 1 
ATOM   302   N  N   . TYR A  1 39  ? -16.399 -3.323  -16.518 1.00 9.18  ? 39  TYR A N   1 
ATOM   303   C  CA  . TYR A  1 39  ? -16.682 -2.527  -17.719 1.00 6.62  ? 39  TYR A CA  1 
ATOM   304   C  C   . TYR A  1 39  ? -18.064 -1.844  -17.669 1.00 7.87  ? 39  TYR A C   1 
ATOM   305   O  O   . TYR A  1 39  ? -19.116 -2.452  -17.349 1.00 8.59  ? 39  TYR A O   1 
ATOM   306   C  CB  . TYR A  1 39  ? -16.666 -3.489  -18.878 1.00 7.36  ? 39  TYR A CB  1 
ATOM   307   C  CG  . TYR A  1 39  ? -17.055 -2.873  -20.220 1.00 7.32  ? 39  TYR A CG  1 
ATOM   308   C  CD1 . TYR A  1 39  ? -16.397 -1.753  -20.720 1.00 7.74  ? 39  TYR A CD1 1 
ATOM   309   C  CD2 . TYR A  1 39  ? -18.077 -3.420  -20.990 1.00 8.05  ? 39  TYR A CD2 1 
ATOM   310   C  CE1 . TYR A  1 39  ? -16.754 -1.196  -21.951 1.00 6.54  ? 39  TYR A CE1 1 
ATOM   311   C  CE2 . TYR A  1 39  ? -18.436 -2.871  -22.214 1.00 6.89  ? 39  TYR A CE2 1 
ATOM   312   C  CZ  . TYR A  1 39  ? -17.777 -1.762  -22.690 1.00 7.51  ? 39  TYR A CZ  1 
ATOM   313   O  OH  . TYR A  1 39  ? -18.153 -1.235  -23.908 1.00 8.68  ? 39  TYR A OH  1 
ATOM   314   N  N   . ASP A  1 40  ? -18.073 -0.525  -17.942 1.00 6.90  ? 40  ASP A N   1 
ATOM   315   C  CA  . ASP A  1 40  ? -19.281 0.263   -18.090 1.00 6.55  ? 40  ASP A CA  1 
ATOM   316   C  C   . ASP A  1 40  ? -19.281 0.930   -19.457 1.00 6.65  ? 40  ASP A C   1 
ATOM   317   O  O   . ASP A  1 40  ? -18.618 1.902   -19.694 1.00 6.92  ? 40  ASP A O   1 
ATOM   318   C  CB  . ASP A  1 40  ? -19.337 1.392   -16.985 1.00 6.65  ? 40  ASP A CB  1 
ATOM   319   C  CG  . ASP A  1 40  ? -20.544 2.271   -17.095 1.00 12.04 ? 40  ASP A CG  1 
ATOM   320   O  OD1 . ASP A  1 40  ? -20.626 3.198   -16.204 1.00 15.25 ? 40  ASP A OD1 1 
ATOM   321   O  OD2 . ASP A  1 40  ? -21.389 2.096   -17.965 1.00 10.92 ? 40  ASP A OD2 1 
ATOM   322   N  N   . ALA A  1 41  ? -20.118 0.353   -20.329 1.00 5.95  ? 41  ALA A N   1 
ATOM   323   C  CA  . ALA A  1 41  ? -20.177 0.784   -21.706 1.00 6.54  ? 41  ALA A CA  1 
ATOM   324   C  C   . ALA A  1 41  ? -20.752 2.170   -21.861 1.00 7.10  ? 41  ALA A C   1 
ATOM   325   O  O   . ALA A  1 41  ? -20.596 2.744   -22.985 1.00 10.13 ? 41  ALA A O   1 
ATOM   326   C  CB  . ALA A  1 41  ? -21.059 -0.222  -22.519 1.00 7.78  ? 41  ALA A CB  1 
ATOM   327   N  N   A SER A  1 42  ? -21.372 2.739   -20.821 0.50 7.23  ? 42  SER A N   1 
ATOM   328   N  N   B SER A  1 42  ? -21.370 2.724   -20.818 0.50 7.75  ? 42  SER A N   1 
ATOM   329   C  CA  A SER A  1 42  ? -21.904 4.144   -20.925 0.50 8.15  ? 42  SER A CA  1 
ATOM   330   C  CA  B SER A  1 42  ? -21.889 4.119   -20.894 0.50 9.62  ? 42  SER A CA  1 
ATOM   331   C  C   A SER A  1 42  ? -20.798 5.205   -20.635 0.50 9.11  ? 42  SER A C   1 
ATOM   332   C  C   B SER A  1 42  ? -20.735 5.162   -20.929 0.50 9.11  ? 42  SER A C   1 
ATOM   333   O  O   A SER A  1 42  ? -21.056 6.410   -20.647 0.50 8.96  ? 42  SER A O   1 
ATOM   334   O  O   B SER A  1 42  ? -20.977 6.342   -21.320 0.50 10.38 ? 42  SER A O   1 
ATOM   335   C  CB  A SER A  1 42  ? -23.051 4.339   -19.954 0.50 9.36  ? 42  SER A CB  1 
ATOM   336   C  CB  B SER A  1 42  ? -22.760 4.388   -19.668 0.50 11.00 ? 42  SER A CB  1 
ATOM   337   O  OG  A SER A  1 42  ? -22.555 4.396   -18.612 0.50 11.67 ? 42  SER A OG  1 
ATOM   338   O  OG  B SER A  1 42  ? -23.936 3.600   -19.687 0.50 17.63 ? 42  SER A OG  1 
ATOM   339   N  N   . LEU A  1 43  ? -19.576 4.757   -20.361 1.00 8.19  ? 43  LEU A N   1 
ATOM   340   C  CA  . LEU A  1 43  ? -18.434 5.736   -20.182 1.00 8.31  ? 43  LEU A CA  1 
ATOM   341   C  C   . LEU A  1 43  ? -17.915 6.206   -21.555 1.00 9.70  ? 43  LEU A C   1 
ATOM   342   O  O   . LEU A  1 43  ? -17.242 5.479   -22.301 1.00 11.84 ? 43  LEU A O   1 
ATOM   343   C  CB  . LEU A  1 43  ? -17.337 5.106   -19.341 1.00 7.57  ? 43  LEU A CB  1 
ATOM   344   C  CG  . LEU A  1 43  ? -17.696 4.850   -17.867 1.00 8.64  ? 43  LEU A CG  1 
ATOM   345   C  CD1 . LEU A  1 43  ? -16.575 4.098   -17.235 1.00 10.09 ? 43  LEU A CD1 1 
ATOM   346   C  CD2 . LEU A  1 43  ? -18.012 6.117   -17.060 1.00 10.31 ? 43  LEU A CD2 1 
ATOM   347   N  N   . THR A  1 44  ? -18.140 7.469   -21.866 1.00 10.45 ? 44  THR A N   1 
ATOM   348   C  CA  . THR A  1 44  ? -17.823 8.014   -23.188 1.00 9.82  ? 44  THR A CA  1 
ATOM   349   C  C   . THR A  1 44  ? -16.516 8.842   -23.118 1.00 10.58 ? 44  THR A C   1 
ATOM   350   O  O   . THR A  1 44  ? -15.989 9.154   -22.036 1.00 9.24  ? 44  THR A O   1 
ATOM   351   C  CB  . THR A  1 44  ? -18.924 8.979   -23.704 1.00 11.17 ? 44  THR A CB  1 
ATOM   352   O  OG1 . THR A  1 44  ? -19.164 10.052  -22.709 1.00 16.51 ? 44  THR A OG1 1 
ATOM   353   C  CG2 . THR A  1 44  ? -20.295 8.189   -23.963 1.00 15.16 ? 44  THR A CG2 1 
ATOM   354   N  N   . PRO A  1 45  ? -15.933 9.178   -24.240 1.00 9.16  ? 45  PRO A N   1 
ATOM   355   C  CA  . PRO A  1 45  ? -14.683 9.948   -24.240 1.00 10.48 ? 45  PRO A CA  1 
ATOM   356   C  C   . PRO A  1 45  ? -14.931 11.306  -23.611 1.00 11.61 ? 45  PRO A C   1 
ATOM   357   O  O   . PRO A  1 45  ? -15.958 11.997  -23.871 1.00 15.26 ? 45  PRO A O   1 
ATOM   358   C  CB  . PRO A  1 45  ? -14.320 10.146  -25.707 1.00 12.63 ? 45  PRO A CB  1 
ATOM   359   C  CG  . PRO A  1 45  ? -15.031 8.963   -26.440 1.00 13.35 ? 45  PRO A CG  1 
ATOM   360   C  CD  . PRO A  1 45  ? -16.370 8.828   -25.629 1.00 9.61  ? 45  PRO A CD  1 
ATOM   361   N  N   . LEU A  1 46  ? -14.007 11.726  -22.760 1.00 10.11 ? 46  LEU A N   1 
ATOM   362   C  CA  . LEU A  1 46  ? -14.017 13.125  -22.371 1.00 11.80 ? 46  LEU A CA  1 
ATOM   363   C  C   . LEU A  1 46  ? -13.571 14.015  -23.569 1.00 9.78  ? 46  LEU A C   1 
ATOM   364   O  O   . LEU A  1 46  ? -12.785 13.593  -24.433 1.00 11.88 ? 46  LEU A O   1 
ATOM   365   C  CB  . LEU A  1 46  ? -13.067 13.304  -21.164 1.00 10.23 ? 46  LEU A CB  1 
ATOM   366   C  CG  . LEU A  1 46  ? -13.613 12.613  -19.896 1.00 12.14 ? 46  LEU A CG  1 
ATOM   367   C  CD1 . LEU A  1 46  ? -12.456 12.843  -18.847 1.00 13.91 ? 46  LEU A CD1 1 
ATOM   368   C  CD2 . LEU A  1 46  ? -14.802 13.431  -19.336 1.00 13.20 ? 46  LEU A CD2 1 
ATOM   369   N  N   . GLU A  1 47  ? -14.049 15.263  -23.573 1.00 11.71 ? 47  GLU A N   1 
ATOM   370   C  CA  . GLU A  1 47  ? -13.407 16.202  -24.536 1.00 12.38 ? 47  GLU A CA  1 
ATOM   371   C  C   . GLU A  1 47  ? -12.639 17.259  -23.759 1.00 12.11 ? 47  GLU A C   1 
ATOM   372   O  O   . GLU A  1 47  ? -13.114 17.788  -22.745 1.00 13.04 ? 47  GLU A O   1 
ATOM   373   C  CB  . GLU A  1 47  ? -14.452 16.929  -25.356 1.00 17.22 ? 47  GLU A CB  1 
ATOM   374   C  CG  . GLU A  1 47  ? -15.346 16.032  -26.140 1.00 24.05 ? 47  GLU A CG  1 
ATOM   375   C  CD  . GLU A  1 47  ? -16.600 16.799  -26.525 1.00 37.84 ? 47  GLU A CD  1 
ATOM   376   O  OE1 . GLU A  1 47  ? -16.550 18.065  -26.506 1.00 44.11 ? 47  GLU A OE1 1 
ATOM   377   O  OE2 . GLU A  1 47  ? -17.634 16.149  -26.781 1.00 40.65 ? 47  GLU A OE2 1 
ATOM   378   N  N   . PHE A  1 48  ? -11.487 17.547  -24.268 1.00 11.77 ? 48  PHE A N   1 
ATOM   379   C  CA  . PHE A  1 48  ? -10.503 18.408  -23.609 1.00 11.93 ? 48  PHE A CA  1 
ATOM   380   C  C   . PHE A  1 48  ? -10.501 19.699  -24.359 1.00 15.56 ? 48  PHE A C   1 
ATOM   381   O  O   . PHE A  1 48  ? -9.856  19.797  -25.463 1.00 18.19 ? 48  PHE A O   1 
ATOM   382   C  CB  . PHE A  1 48  ? -9.076  17.813  -23.619 1.00 14.21 ? 48  PHE A CB  1 
ATOM   383   C  CG  . PHE A  1 48  ? -9.076  16.375  -23.155 1.00 12.65 ? 48  PHE A CG  1 
ATOM   384   C  CD1 . PHE A  1 48  ? -8.961  15.354  -24.113 1.00 14.38 ? 48  PHE A CD1 1 
ATOM   385   C  CD2 . PHE A  1 48  ? -9.203  16.031  -21.819 1.00 13.19 ? 48  PHE A CD2 1 
ATOM   386   C  CE1 . PHE A  1 48  ? -8.998  14.004  -23.687 1.00 12.58 ? 48  PHE A CE1 1 
ATOM   387   C  CE2 . PHE A  1 48  ? -9.337  14.732  -21.435 1.00 16.08 ? 48  PHE A CE2 1 
ATOM   388   C  CZ  . PHE A  1 48  ? -9.163  13.720  -22.362 1.00 15.39 ? 48  PHE A CZ  1 
ATOM   389   N  N   . GLN A  1 49  ? -11.120 20.724  -23.753 1.00 10.67 ? 49  GLN A N   1 
ATOM   390   C  CA  . GLN A  1 49  ? -11.304 22.018  -24.387 1.00 11.84 ? 49  GLN A CA  1 
ATOM   391   C  C   . GLN A  1 49  ? -10.455 23.089  -23.805 1.00 8.83  ? 49  GLN A C   1 
ATOM   392   O  O   . GLN A  1 49  ? -10.280 23.195  -22.608 1.00 9.18  ? 49  GLN A O   1 
ATOM   393   C  CB  . GLN A  1 49  ? -12.744 22.452  -24.204 1.00 16.25 ? 49  GLN A CB  1 
ATOM   394   C  CG  . GLN A  1 49  ? -13.544 21.309  -24.883 1.00 22.98 ? 49  GLN A CG  1 
ATOM   395   C  CD  . GLN A  1 49  ? -15.035 21.535  -25.096 1.00 29.87 ? 49  GLN A CD  1 
ATOM   396   O  OE1 . GLN A  1 49  ? -15.723 22.390  -24.433 1.00 26.36 ? 49  GLN A OE1 1 
ATOM   397   N  NE2 . GLN A  1 49  ? -15.575 20.689  -26.033 1.00 33.22 ? 49  GLN A NE2 1 
ATOM   398   N  N   . GLY A  1 50  ? -9.859  23.882  -24.731 1.00 9.27  ? 50  GLY A N   1 
ATOM   399   C  CA  . GLY A  1 50  ? -8.930  24.926  -24.303 1.00 8.45  ? 50  GLY A CA  1 
ATOM   400   C  C   . GLY A  1 50  ? -7.601  24.433  -23.722 1.00 9.82  ? 50  GLY A C   1 
ATOM   401   O  O   . GLY A  1 50  ? -6.885  25.187  -22.997 1.00 11.19 ? 50  GLY A O   1 
ATOM   402   N  N   . TYR A  1 51  ? -7.308  23.164  -24.034 1.00 8.28  ? 51  TYR A N   1 
ATOM   403   C  CA  . TYR A  1 51  ? -6.045  22.596  -23.480 1.00 7.63  ? 51  TYR A CA  1 
ATOM   404   C  C   . TYR A  1 51  ? -4.808  23.098  -24.311 1.00 9.90  ? 51  TYR A C   1 
ATOM   405   O  O   . TYR A  1 51  ? -3.666  23.010  -23.824 1.00 9.21  ? 51  TYR A O   1 
ATOM   406   C  CB  . TYR A  1 51  ? -6.036  21.056  -23.597 1.00 8.20  ? 51  TYR A CB  1 
ATOM   407   C  CG  . TYR A  1 51  ? -6.675  20.352  -22.372 1.00 8.10  ? 51  TYR A CG  1 
ATOM   408   C  CD1 . TYR A  1 51  ? -7.883  20.746  -21.794 1.00 8.66  ? 51  TYR A CD1 1 
ATOM   409   C  CD2 . TYR A  1 51  ? -5.988  19.218  -21.790 1.00 7.73  ? 51  TYR A CD2 1 
ATOM   410   C  CE1 . TYR A  1 51  ? -8.413  20.092  -20.637 1.00 8.12  ? 51  TYR A CE1 1 
ATOM   411   C  CE2 . TYR A  1 51  ? -6.480  18.581  -20.631 1.00 7.19  ? 51  TYR A CE2 1 
ATOM   412   C  CZ  . TYR A  1 51  ? -7.652  19.056  -20.064 1.00 8.95  ? 51  TYR A CZ  1 
ATOM   413   O  OH  . TYR A  1 51  ? -8.096  18.396  -18.904 1.00 8.38  ? 51  TYR A OH  1 
ATOM   414   N  N   . ASN A  1 52  ? -5.047  23.573  -25.553 1.00 11.21 ? 52  ASN A N   1 
ATOM   415   C  CA  . ASN A  1 52  ? -3.940  24.114  -26.420 1.00 10.28 ? 52  ASN A CA  1 
ATOM   416   C  C   . ASN A  1 52  ? -3.679  25.553  -25.969 1.00 11.67 ? 52  ASN A C   1 
ATOM   417   O  O   . ASN A  1 52  ? -4.197  26.532  -26.536 1.00 13.32 ? 52  ASN A O   1 
ATOM   418   C  CB  . ASN A  1 52  ? -4.331  24.023  -27.878 1.00 12.36 ? 52  ASN A CB  1 
ATOM   419   C  CG  . ASN A  1 52  ? -3.180  24.422  -28.745 1.00 19.82 ? 52  ASN A CG  1 
ATOM   420   O  OD1 . ASN A  1 52  ? -2.047  24.147  -28.400 1.00 18.15 ? 52  ASN A OD1 1 
ATOM   421   N  ND2 . ASN A  1 52  ? -3.462  25.158  -29.853 1.00 26.89 ? 52  ASN A ND2 1 
ATOM   422   N  N   . LEU A  1 53  ? -2.916  25.669  -24.914 1.00 9.56  ? 53  LEU A N   1 
ATOM   423   C  CA  . LEU A  1 53  ? -2.749  26.945  -24.164 1.00 9.44  ? 53  LEU A CA  1 
ATOM   424   C  C   . LEU A  1 53  ? -1.960  27.941  -25.118 1.00 10.24 ? 53  LEU A C   1 
ATOM   425   O  O   . LEU A  1 53  ? -1.010  27.558  -25.800 1.00 10.84 ? 53  LEU A O   1 
ATOM   426   C  CB  . LEU A  1 53  ? -1.980  26.760  -22.900 1.00 10.85 ? 53  LEU A CB  1 
ATOM   427   C  CG  . LEU A  1 53  ? -2.538  25.832  -21.795 1.00 11.63 ? 53  LEU A CG  1 
ATOM   428   C  CD1 . LEU A  1 53  ? -1.609  25.755  -20.628 1.00 11.47 ? 53  LEU A CD1 1 
ATOM   429   C  CD2 . LEU A  1 53  ? -3.952  26.414  -21.377 1.00 13.65 ? 53  LEU A CD2 1 
ATOM   430   N  N   . SER A  1 54  ? -2.327  29.216  -25.036 1.00 9.66  ? 54  SER A N   1 
ATOM   431   C  CA  . SER A  1 54  ? -1.639  30.183  -25.899 1.00 10.04 ? 54  SER A CA  1 
ATOM   432   C  C   . SER A  1 54  ? -0.149  30.201  -25.637 1.00 8.56  ? 54  SER A C   1 
ATOM   433   O  O   . SER A  1 54  ? 0.244   30.425  -24.518 1.00 8.60  ? 54  SER A O   1 
ATOM   434   C  CB  . SER A  1 54  ? -2.203  31.525  -25.550 1.00 10.77 ? 54  SER A CB  1 
ATOM   435   O  OG  . SER A  1 54  ? -1.563  32.483  -26.452 1.00 10.80 ? 54  SER A OG  1 
ATOM   436   N  N   . ALA A  1 55  ? 0.588   30.122  -26.736 1.00 8.78  ? 55  ALA A N   1 
ATOM   437   C  CA  . ALA A  1 55  ? 2.034   30.272  -26.654 1.00 10.04 ? 55  ALA A CA  1 
ATOM   438   C  C   . ALA A  1 55  ? 2.482   31.706  -26.310 1.00 9.61  ? 55  ALA A C   1 
ATOM   439   O  O   . ALA A  1 55  ? 3.624   31.883  -25.891 1.00 11.04 ? 55  ALA A O   1 
ATOM   440   C  CB  . ALA A  1 55  ? 2.653   29.794  -27.901 1.00 11.84 ? 55  ALA A CB  1 
ATOM   441   N  N   . ASN A  1 56  ? 1.544   32.674  -26.506 1.00 9.26  ? 56  ASN A N   1 
ATOM   442   C  CA  . ASN A  1 56  ? 1.811   34.048  -26.150 1.00 11.49 ? 56  ASN A CA  1 
ATOM   443   C  C   . ASN A  1 56  ? 1.451   34.395  -24.758 1.00 12.06 ? 56  ASN A C   1 
ATOM   444   O  O   . ASN A  1 56  ? 1.619   35.575  -24.339 1.00 12.00 ? 56  ASN A O   1 
ATOM   445   C  CB  . ASN A  1 56  ? 1.074   35.030  -27.087 1.00 11.74 ? 56  ASN A CB  1 
ATOM   446   C  CG  . ASN A  1 56  ? 1.538   34.874  -28.513 1.00 14.69 ? 56  ASN A CG  1 
ATOM   447   O  OD1 . ASN A  1 56  ? 2.687   34.558  -28.787 1.00 12.98 ? 56  ASN A OD1 1 
ATOM   448   N  ND2 . ASN A  1 56  ? 0.554   34.867  -29.432 1.00 21.30 ? 56  ASN A ND2 1 
ATOM   449   N  N   . LYS A  1 57  ? 0.992   33.439  -23.967 1.00 10.28 ? 57  LYS A N   1 
ATOM   450   C  CA  . LYS A  1 57  ? 0.656   33.567  -22.561 1.00 9.88  ? 57  LYS A CA  1 
ATOM   451   C  C   . LYS A  1 57  ? 1.686   32.781  -21.682 1.00 9.10  ? 57  LYS A C   1 
ATOM   452   O  O   . LYS A  1 57  ? 2.262   31.835  -22.225 1.00 10.98 ? 57  LYS A O   1 
ATOM   453   C  CB  . LYS A  1 57  ? -0.819  33.097  -22.356 1.00 10.36 ? 57  LYS A CB  1 
ATOM   454   C  CG  . LYS A  1 57  ? -1.322  33.382  -20.928 1.00 12.38 ? 57  LYS A CG  1 
ATOM   455   C  CD  . LYS A  1 57  ? -2.847  33.104  -20.903 1.00 11.62 ? 57  LYS A CD  1 
ATOM   456   C  CE  . LYS A  1 57  ? -3.445  33.129  -19.542 1.00 13.98 ? 57  LYS A CE  1 
ATOM   457   N  NZ  . LYS A  1 57  ? -4.927  32.935  -19.491 1.00 14.31 ? 57  LYS A NZ  1 
ATOM   458   N  N   . GLN A  1 58  ? 1.889   33.179  -20.440 1.00 8.55  ? 58  GLN A N   1 
ATOM   459   C  CA  . GLN A  1 58  ? 2.788   32.412  -19.552 1.00 8.72  ? 58  GLN A CA  1 
ATOM   460   C  C   . GLN A  1 58  ? 1.983   31.902  -18.422 1.00 10.09 ? 58  GLN A C   1 
ATOM   461   O  O   . GLN A  1 58  ? 1.018   32.570  -17.951 1.00 11.24 ? 58  GLN A O   1 
ATOM   462   C  CB  . GLN A  1 58  ? 3.974   33.273  -19.025 1.00 10.91 ? 58  GLN A CB  1 
ATOM   463   C  CG  . GLN A  1 58  ? 4.815   33.815  -20.169 1.00 12.36 ? 58  GLN A CG  1 
ATOM   464   C  CD  . GLN A  1 58  ? 5.762   34.897  -19.672 1.00 14.78 ? 58  GLN A CD  1 
ATOM   465   O  OE1 . GLN A  1 58  ? 5.342   36.007  -19.182 1.00 19.13 ? 58  GLN A OE1 1 
ATOM   466   N  NE2 . GLN A  1 58  ? 6.979   34.583  -19.683 1.00 12.73 ? 58  GLN A NE2 1 
ATOM   467   N  N   . PHE A  1 59  ? 2.408   30.711  -17.923 1.00 8.65  ? 59  PHE A N   1 
ATOM   468   C  CA  . PHE A  1 59  ? 1.735   30.094  -16.770 1.00 9.54  ? 59  PHE A CA  1 
ATOM   469   C  C   . PHE A  1 59  ? 2.665   29.848  -15.669 1.00 8.09  ? 59  PHE A C   1 
ATOM   470   O  O   . PHE A  1 59  ? 3.820   29.433  -15.934 1.00 8.41  ? 59  PHE A O   1 
ATOM   471   C  CB  . PHE A  1 59  ? 1.084   28.808  -17.265 1.00 7.69  ? 59  PHE A CB  1 
ATOM   472   C  CG  . PHE A  1 59  ? 0.079   29.076  -18.400 1.00 8.30  ? 59  PHE A CG  1 
ATOM   473   C  CD1 . PHE A  1 59  ? 0.468   29.247  -19.740 1.00 9.22  ? 59  PHE A CD1 1 
ATOM   474   C  CD2 . PHE A  1 59  ? -1.217  29.284  -18.037 1.00 9.24  ? 59  PHE A CD2 1 
ATOM   475   C  CE1 . PHE A  1 59  ? -0.486  29.523  -20.735 1.00 10.27 ? 59  PHE A CE1 1 
ATOM   476   C  CE2 . PHE A  1 59  ? -2.177  29.615  -19.019 1.00 8.98  ? 59  PHE A CE2 1 
ATOM   477   C  CZ  . PHE A  1 59  ? -1.806  29.743  -20.376 1.00 9.89  ? 59  PHE A CZ  1 
ATOM   478   N  N   . LEU A  1 60  ? 2.237   30.053  -14.418 1.00 7.81  ? 60  LEU A N   1 
ATOM   479   C  CA  . LEU A  1 60  ? 3.140   30.051  -13.294 1.00 9.00  ? 60  LEU A CA  1 
ATOM   480   C  C   . LEU A  1 60  ? 3.483   28.592  -12.845 1.00 9.11  ? 60  LEU A C   1 
ATOM   481   O  O   . LEU A  1 60  ? 2.516   27.801  -12.552 1.00 8.29  ? 60  LEU A O   1 
ATOM   482   C  CB  . LEU A  1 60  ? 2.456   30.795  -12.145 1.00 11.10 ? 60  LEU A CB  1 
ATOM   483   C  CG  . LEU A  1 60  ? 3.409   31.063  -11.004 1.00 9.57  ? 60  LEU A CG  1 
ATOM   484   C  CD1 . LEU A  1 60  ? 4.493   32.075  -11.383 1.00 13.40 ? 60  LEU A CD1 1 
ATOM   485   C  CD2 . LEU A  1 60  ? 2.639   31.655  -9.795  1.00 14.71 ? 60  LEU A CD2 1 
ATOM   486   N  N   . LEU A  1 61  ? 4.736   28.240  -12.760 1.00 7.57  ? 61  LEU A N   1 
ATOM   487   C  CA  . LEU A  1 61  ? 5.223   27.001  -12.195 1.00 8.28  ? 61  LEU A CA  1 
ATOM   488   C  C   . LEU A  1 61  ? 5.756   27.229  -10.808 1.00 8.19  ? 61  LEU A C   1 
ATOM   489   O  O   . LEU A  1 61  ? 6.634   28.086  -10.696 1.00 10.10 ? 61  LEU A O   1 
ATOM   490   C  CB  . LEU A  1 61  ? 6.333   26.404  -13.093 1.00 7.55  ? 61  LEU A CB  1 
ATOM   491   C  CG  . LEU A  1 61  ? 6.797   25.018  -12.737 1.00 8.86  ? 61  LEU A CG  1 
ATOM   492   C  CD1 . LEU A  1 61  ? 5.800   23.963  -13.245 1.00 9.52  ? 61  LEU A CD1 1 
ATOM   493   C  CD2 . LEU A  1 61  ? 8.166   24.764  -13.527 1.00 11.48 ? 61  LEU A CD2 1 
ATOM   494   N  N   . THR A  1 62  ? 5.330   26.495  -9.779  1.00 7.96  ? 62  THR A N   1 
ATOM   495   C  CA  . THR A  1 62  ? 5.756   26.772  -8.430  1.00 7.92  ? 62  THR A CA  1 
ATOM   496   C  C   . THR A  1 62  ? 6.183   25.496  -7.720  1.00 9.54  ? 62  THR A C   1 
ATOM   497   O  O   . THR A  1 62  ? 5.497   24.451  -7.864  1.00 9.32  ? 62  THR A O   1 
ATOM   498   C  CB  . THR A  1 62  ? 4.530   27.362  -7.594  1.00 11.76 ? 62  THR A CB  1 
ATOM   499   O  OG1 . THR A  1 62  ? 4.027   28.542  -8.247  1.00 12.53 ? 62  THR A OG1 1 
ATOM   500   C  CG2 . THR A  1 62  ? 4.880   27.735  -6.099  1.00 12.12 ? 62  THR A CG2 1 
ATOM   501   N  N   . ASN A  1 63  ? 7.254   25.564  -6.933  1.00 7.68  ? 63  ASN A N   1 
ATOM   502   C  CA  . ASN A  1 63  ? 7.588   24.544  -5.975  1.00 8.19  ? 63  ASN A CA  1 
ATOM   503   C  C   . ASN A  1 63  ? 6.877   24.887  -4.706  1.00 9.36  ? 63  ASN A C   1 
ATOM   504   O  O   . ASN A  1 63  ? 7.173   25.945  -4.134  1.00 9.85  ? 63  ASN A O   1 
ATOM   505   C  CB  . ASN A  1 63  ? 9.107   24.489  -5.827  1.00 6.81  ? 63  ASN A CB  1 
ATOM   506   C  CG  . ASN A  1 63  ? 9.552   23.555  -4.700  1.00 7.50  ? 63  ASN A CG  1 
ATOM   507   O  OD1 . ASN A  1 63  ? 8.757   23.248  -3.775  1.00 8.65  ? 63  ASN A OD1 1 
ATOM   508   N  ND2 . ASN A  1 63  ? 10.832  23.122  -4.777  1.00 7.98  ? 63  ASN A ND2 1 
ATOM   509   N  N   . ASN A  1 64  ? 5.869   24.161  -4.293  1.00 9.33  ? 64  ASN A N   1 
ATOM   510   C  CA  . ASN A  1 64  ? 5.093   24.542  -3.155  1.00 9.64  ? 64  ASN A CA  1 
ATOM   511   C  C   . ASN A  1 64  ? 5.477   23.787  -1.873  1.00 9.64  ? 64  ASN A C   1 
ATOM   512   O  O   . ASN A  1 64  ? 4.748   23.796  -0.896  1.00 12.07 ? 64  ASN A O   1 
ATOM   513   C  CB  . ASN A  1 64  ? 3.606   24.435  -3.418  1.00 10.53 ? 64  ASN A CB  1 
ATOM   514   C  CG  . ASN A  1 64  ? 3.139   23.000  -3.550  1.00 11.68 ? 64  ASN A CG  1 
ATOM   515   O  OD1 . ASN A  1 64  ? 3.888   22.018  -3.415  1.00 8.84  ? 64  ASN A OD1 1 
ATOM   516   N  ND2 . ASN A  1 64  ? 1.784   22.851  -3.698  1.00 19.48 ? 64  ASN A ND2 1 
ATOM   517   N  N   . GLY A  1 65  ? 6.614   23.066  -1.936  1.00 9.03  ? 65  GLY A N   1 
ATOM   518   C  CA  . GLY A  1 65  ? 7.032   22.331  -0.738  1.00 10.42 ? 65  GLY A CA  1 
ATOM   519   C  C   . GLY A  1 65  ? 6.588   20.854  -0.720  1.00 10.53 ? 65  GLY A C   1 
ATOM   520   O  O   . GLY A  1 65  ? 7.131   20.033  0.074   1.00 10.75 ? 65  GLY A O   1 
ATOM   521   N  N   . HIS A  1 66  ? 5.580   20.542  -1.575  1.00 8.07  ? 66  HIS A N   1 
ATOM   522   C  CA  . HIS A  1 66  ? 5.017   19.191  -1.645  1.00 8.45  ? 66  HIS A CA  1 
ATOM   523   C  C   . HIS A  1 66  ? 5.099   18.585  -3.059  1.00 7.46  ? 66  HIS A C   1 
ATOM   524   O  O   . HIS A  1 66  ? 5.205   17.348  -3.195  1.00 8.75  ? 66  HIS A O   1 
ATOM   525   C  CB  . HIS A  1 66  ? 3.537   19.187  -1.246  1.00 8.13  ? 66  HIS A CB  1 
ATOM   526   C  CG  . HIS A  1 66  ? 3.292   19.698  0.179   1.00 8.98  ? 66  HIS A CG  1 
ATOM   527   N  ND1 . HIS A  1 66  ? 3.672   19.068  1.371   1.00 12.17 ? 66  HIS A ND1 1 
ATOM   528   C  CD2 . HIS A  1 66  ? 2.629   20.838  0.549   1.00 11.23 ? 66  HIS A CD2 1 
ATOM   529   C  CE1 . HIS A  1 66  ? 3.277   19.812  2.406   1.00 11.28 ? 66  HIS A CE1 1 
ATOM   530   N  NE2 . HIS A  1 66  ? 2.602   20.850  1.937   1.00 12.16 ? 66  HIS A NE2 1 
ATOM   531   N  N   . SER A  1 67  ? 5.060   19.415  -4.095  1.00 6.98  ? 67  SER A N   1 
ATOM   532   C  CA  . SER A  1 67  ? 5.240   18.978  -5.468  1.00 6.00  ? 67  SER A CA  1 
ATOM   533   C  C   . SER A  1 67  ? 5.710   20.195  -6.343  1.00 6.89  ? 67  SER A C   1 
ATOM   534   O  O   . SER A  1 67  ? 5.964   21.312  -5.723  1.00 7.65  ? 67  SER A O   1 
ATOM   535   C  CB  . SER A  1 67  ? 3.867   18.409  -6.001  1.00 8.11  ? 67  SER A CB  1 
ATOM   536   O  OG  . SER A  1 67  ? 3.970   17.901  -7.303  1.00 7.56  ? 67  SER A OG  1 
ATOM   537   N  N   . VAL A  1 68  ? 5.774   19.979  -7.671  1.00 6.74  ? 68  VAL A N   1 
ATOM   538   C  CA  . VAL A  1 68  ? 5.956   21.106  -8.615  1.00 8.25  ? 68  VAL A CA  1 
ATOM   539   C  C   . VAL A  1 68  ? 4.555   21.251  -9.282  1.00 7.62  ? 68  VAL A C   1 
ATOM   540   O  O   . VAL A  1 68  ? 3.985   20.227  -9.714  1.00 6.66  ? 68  VAL A O   1 
ATOM   541   C  CB  . VAL A  1 68  ? 7.134   20.920  -9.501  1.00 8.18  ? 68  VAL A CB  1 
ATOM   542   C  CG1 . VAL A  1 68  ? 7.014   19.656  -10.393 1.00 10.36 ? 68  VAL A CG1 1 
ATOM   543   C  CG2 . VAL A  1 68  ? 7.352   22.182  -10.321 1.00 10.90 ? 68  VAL A CG2 1 
ATOM   544   N  N   . LYS A  1 69  ? 3.993   22.458  -9.275  1.00 8.20  ? 69  LYS A N   1 
ATOM   545   C  CA  . LYS A  1 69  ? 2.662   22.695  -9.791  1.00 10.01 ? 69  LYS A CA  1 
ATOM   546   C  C   . LYS A  1 69  ? 2.632   23.753  -10.897 1.00 8.51  ? 69  LYS A C   1 
ATOM   547   O  O   . LYS A  1 69  ? 3.373   24.765  -10.745 1.00 9.85  ? 69  LYS A O   1 
ATOM   548   C  CB  . LYS A  1 69  ? 1.712   22.982  -8.672  1.00 12.08 ? 69  LYS A CB  1 
ATOM   549   C  CG  . LYS A  1 69  ? 1.695   24.221  -8.082  1.00 18.45 ? 69  LYS A CG  1 
ATOM   550   C  CD  . LYS A  1 69  ? 0.181   24.524  -7.489  1.00 13.30 ? 69  LYS A CD  1 
ATOM   551   C  CE  . LYS A  1 69  ? 0.498   25.701  -6.553  1.00 20.47 ? 69  LYS A CE  1 
ATOM   552   N  NZ  . LYS A  1 69  ? -0.694  26.310  -5.849  1.00 19.01 ? 69  LYS A NZ  1 
ATOM   553   N  N   . LEU A  1 70  ? 1.873   23.519  -11.942 1.00 6.00  ? 70  LEU A N   1 
ATOM   554   C  CA  . LEU A  1 70  ? 1.692   24.504  -13.056 1.00 6.82  ? 70  LEU A CA  1 
ATOM   555   C  C   . LEU A  1 70  ? 0.256   25.015  -12.950 1.00 7.29  ? 70  LEU A C   1 
ATOM   556   O  O   . LEU A  1 70  ? -0.714  24.233  -12.952 1.00 6.59  ? 70  LEU A O   1 
ATOM   557   C  CB  . LEU A  1 70  ? 1.906   23.816  -14.339 1.00 7.88  ? 70  LEU A CB  1 
ATOM   558   C  CG  . LEU A  1 70  ? 1.772   24.753  -15.610 1.00 9.12  ? 70  LEU A CG  1 
ATOM   559   C  CD1 . LEU A  1 70  ? 2.956   25.778  -15.606 1.00 9.08  ? 70  LEU A CD1 1 
ATOM   560   C  CD2 . LEU A  1 70  ? 1.784   23.879  -16.885 1.00 9.16  ? 70  LEU A CD2 1 
ATOM   561   N  N   . ASN A  1 71  ? 0.077   26.343  -12.766 1.00 8.03  ? 71  ASN A N   1 
ATOM   562   C  CA  . ASN A  1 71  ? -1.284  26.879  -12.773 1.00 8.03  ? 71  ASN A CA  1 
ATOM   563   C  C   . ASN A  1 71  ? -1.881  26.849  -14.166 1.00 8.71  ? 71  ASN A C   1 
ATOM   564   O  O   . ASN A  1 71  ? -1.139  26.977  -15.180 1.00 8.39  ? 71  ASN A O   1 
ATOM   565   C  CB  . ASN A  1 71  ? -1.285  28.363  -12.290 1.00 10.18 ? 71  ASN A CB  1 
ATOM   566   C  CG  . ASN A  1 71  ? -1.011  28.486  -10.803 1.00 15.33 ? 71  ASN A CG  1 
ATOM   567   O  OD1 . ASN A  1 71  ? -1.003  27.512  -10.051 1.00 15.73 ? 71  ASN A OD1 1 
ATOM   568   N  ND2 . ASN A  1 71  ? -0.899  29.779  -10.341 1.00 21.04 ? 71  ASN A ND2 1 
ATOM   569   N  N   . LEU A  1 72  ? -3.205  26.565  -14.194 1.00 8.02  ? 72  LEU A N   1 
ATOM   570   C  CA  . LEU A  1 72  ? -3.874  26.389  -15.506 1.00 7.52  ? 72  LEU A CA  1 
ATOM   571   C  C   . LEU A  1 72  ? -5.061  27.416  -15.475 1.00 9.26  ? 72  LEU A C   1 
ATOM   572   O  O   . LEU A  1 72  ? -5.575  27.758  -14.424 1.00 9.08  ? 72  LEU A O   1 
ATOM   573   C  CB  . LEU A  1 72  ? -4.464  24.965  -15.666 1.00 7.00  ? 72  LEU A CB  1 
ATOM   574   C  CG  . LEU A  1 72  ? -3.318  23.915  -15.732 1.00 5.83  ? 72  LEU A CG  1 
ATOM   575   C  CD1 . LEU A  1 72  ? -3.933  22.556  -15.669 1.00 7.01  ? 72  LEU A CD1 1 
ATOM   576   C  CD2 . LEU A  1 72  ? -2.378  24.172  -17.038 1.00 7.43  ? 72  LEU A CD2 1 
ATOM   577   N  N   . PRO A  1 73  ? -5.511  27.789  -16.700 1.00 8.78  ? 73  PRO A N   1 
ATOM   578   C  CA  . PRO A  1 73  ? -6.564  28.846  -16.796 1.00 8.67  ? 73  PRO A CA  1 
ATOM   579   C  C   . PRO A  1 73  ? -7.961  28.284  -16.763 1.00 10.48 ? 73  PRO A C   1 
ATOM   580   O  O   . PRO A  1 73  ? -8.209  27.162  -17.159 1.00 9.44  ? 73  PRO A O   1 
ATOM   581   C  CB  . PRO A  1 73  ? -6.251  29.490  -18.149 1.00 9.86  ? 73  PRO A CB  1 
ATOM   582   C  CG  . PRO A  1 73  ? -5.829  28.181  -19.063 1.00 8.81  ? 73  PRO A CG  1 
ATOM   583   C  CD  . PRO A  1 73  ? -4.938  27.391  -18.032 1.00 8.03  ? 73  PRO A CD  1 
ATOM   584   N  N   . SER A  1 74  ? -8.903  29.223  -16.474 1.00 10.40 ? 74  SER A N   1 
ATOM   585   C  CA  . SER A  1 74  ? -10.295 28.810  -16.275 1.00 13.36 ? 74  SER A CA  1 
ATOM   586   C  C   . SER A  1 74  ? -10.966 28.376  -17.559 1.00 12.41 ? 74  SER A C   1 
ATOM   587   O  O   . SER A  1 74  ? -12.040 27.677  -17.560 1.00 13.44 ? 74  SER A O   1 
ATOM   588   C  CB  . SER A  1 74  ? -11.101 29.955  -15.605 1.00 13.50 ? 74  SER A CB  1 
ATOM   589   O  OG  . SER A  1 74  ? -11.044 31.099  -16.439 1.00 18.83 ? 74  SER A OG  1 
ATOM   590   N  N   . ASP A  1 75  ? -10.458 28.814  -18.698 1.00 9.18  ? 75  ASP A N   1 
ATOM   591   C  CA  . ASP A  1 75  ? -11.076 28.452  -19.958 1.00 8.51  ? 75  ASP A CA  1 
ATOM   592   C  C   . ASP A  1 75  ? -10.734 27.042  -20.423 1.00 9.51  ? 75  ASP A C   1 
ATOM   593   O  O   . ASP A  1 75  ? -11.258 26.542  -21.450 1.00 10.63 ? 75  ASP A O   1 
ATOM   594   C  CB  . ASP A  1 75  ? -10.734 29.482  -21.076 1.00 10.65 ? 75  ASP A CB  1 
ATOM   595   C  CG  . ASP A  1 75  ? -9.210  29.562  -21.401 1.00 10.38 ? 75  ASP A CG  1 
ATOM   596   O  OD1 . ASP A  1 75  ? -8.521  29.969  -20.507 1.00 9.68  ? 75  ASP A OD1 1 
ATOM   597   O  OD2 . ASP A  1 75  ? -8.907  29.214  -22.575 1.00 11.67 ? 75  ASP A OD2 1 
ATOM   598   N  N   . MET A  1 76  ? -9.807  26.337  -19.686 1.00 8.87  ? 76  MET A N   1 
ATOM   599   C  CA  . MET A  1 76  ? -9.536  24.994  -19.997 1.00 8.64  ? 76  MET A CA  1 
ATOM   600   C  C   . MET A  1 76  ? -10.565 24.103  -19.268 1.00 7.40  ? 76  MET A C   1 
ATOM   601   O  O   . MET A  1 76  ? -10.780 24.372  -18.085 1.00 9.00  ? 76  MET A O   1 
ATOM   602   C  CB  . MET A  1 76  ? -8.140  24.737  -19.389 1.00 14.38 ? 76  MET A CB  1 
ATOM   603   C  CG  . MET A  1 76  ? -7.594  23.393  -19.658 1.00 12.54 ? 76  MET A CG  1 
ATOM   604   S  SD  . MET A  1 76  ? -5.732  23.446  -19.235 1.00 10.93 ? 76  MET A SD  1 
ATOM   605   C  CE  . MET A  1 76  ? -5.629  21.684  -19.001 1.00 11.08 ? 76  MET A CE  1 
ATOM   606   N  N   A HIS A  1 77  ? -11.142 23.134  -19.909 0.50 8.05  ? 77  HIS A N   1 
ATOM   607   N  N   B HIS A  1 77  ? -11.263 23.254  -20.025 0.50 9.59  ? 77  HIS A N   1 
ATOM   608   C  CA  A HIS A  1 77  ? -12.084 22.331  -19.119 0.50 6.24  ? 77  HIS A CA  1 
ATOM   609   C  CA  B HIS A  1 77  ? -12.396 22.472  -19.448 0.50 10.95 ? 77  HIS A CA  1 
ATOM   610   C  C   A HIS A  1 77  ? -12.209 21.007  -19.761 0.50 7.04  ? 77  HIS A C   1 
ATOM   611   C  C   B HIS A  1 77  ? -12.451 21.015  -19.879 0.50 11.47 ? 77  HIS A C   1 
ATOM   612   O  O   A HIS A  1 77  ? -11.762 20.857  -20.850 0.50 5.99  ? 77  HIS A O   1 
ATOM   613   O  O   B HIS A  1 77  ? -12.057 20.690  -20.999 0.50 11.26 ? 77  HIS A O   1 
ATOM   614   C  CB  A HIS A  1 77  ? -13.508 22.954  -19.100 0.50 7.49  ? 77  HIS A CB  1 
ATOM   615   C  CB  B HIS A  1 77  ? -13.803 23.038  -19.816 0.50 12.53 ? 77  HIS A CB  1 
ATOM   616   C  CG  A HIS A  1 77  ? -14.065 23.325  -20.473 0.50 6.50  ? 77  HIS A CG  1 
ATOM   617   C  CG  B HIS A  1 77  ? -13.910 24.547  -19.970 0.50 9.58  ? 77  HIS A CG  1 
ATOM   618   N  ND1 A HIS A  1 77  ? -14.010 24.636  -20.892 0.50 11.59 ? 77  HIS A ND1 1 
ATOM   619   N  ND1 B HIS A  1 77  ? -14.412 25.108  -21.141 0.50 10.80 ? 77  HIS A ND1 1 
ATOM   620   C  CD2 A HIS A  1 77  ? -14.760 22.659  -21.439 0.50 9.47  ? 77  HIS A CD2 1 
ATOM   621   C  CD2 B HIS A  1 77  ? -13.736 25.578  -19.091 0.50 9.85  ? 77  HIS A CD2 1 
ATOM   622   C  CE1 A HIS A  1 77  ? -14.571 24.771  -22.069 0.50 8.58  ? 77  HIS A CE1 1 
ATOM   623   C  CE1 B HIS A  1 77  ? -14.513 26.412  -20.959 0.50 10.28 ? 77  HIS A CE1 1 
ATOM   624   N  NE2 A HIS A  1 77  ? -15.083 23.597  -22.420 0.50 9.68  ? 77  HIS A NE2 1 
ATOM   625   N  NE2 B HIS A  1 77  ? -14.111 26.716  -19.738 0.50 8.53  ? 77  HIS A NE2 1 
ATOM   626   N  N   A ILE A  1 78  ? -12.948 20.119  -19.096 0.50 7.89  ? 78  ILE A N   1 
ATOM   627   N  N   B ILE A  1 78  ? -13.039 20.175  -19.011 0.50 11.03 ? 78  ILE A N   1 
ATOM   628   C  CA  A ILE A  1 78  ? -13.377 18.888  -19.729 0.50 7.29  ? 78  ILE A CA  1 
ATOM   629   C  CA  B ILE A  1 78  ? -13.497 18.840  -19.456 0.50 10.96 ? 78  ILE A CA  1 
ATOM   630   C  C   A ILE A  1 78  ? -14.913 18.912  -19.840 0.50 8.26  ? 78  ILE A C   1 
ATOM   631   C  C   B ILE A  1 78  ? -14.995 18.870  -19.762 0.50 10.04 ? 78  ILE A C   1 
ATOM   632   O  O   A ILE A  1 78  ? -15.586 19.451  -18.958 0.50 8.00  ? 78  ILE A O   1 
ATOM   633   O  O   B ILE A  1 78  ? -15.751 19.328  -18.874 0.50 9.90  ? 78  ILE A O   1 
ATOM   634   C  CB  A ILE A  1 78  ? -12.987 17.627  -18.908 0.50 7.67  ? 78  ILE A CB  1 
ATOM   635   C  CB  B ILE A  1 78  ? -13.334 17.693  -18.362 0.50 11.02 ? 78  ILE A CB  1 
ATOM   636   C  CG1 A ILE A  1 78  ? -13.336 17.789  -17.429 0.50 6.69  ? 78  ILE A CG1 1 
ATOM   637   C  CG1 B ILE A  1 78  ? -11.886 17.382  -18.069 0.50 12.09 ? 78  ILE A CG1 1 
ATOM   638   C  CG2 A ILE A  1 78  ? -11.524 17.273  -19.149 0.50 7.17  ? 78  ILE A CG2 1 
ATOM   639   C  CG2 B ILE A  1 78  ? -14.049 16.413  -18.892 0.50 12.25 ? 78  ILE A CG2 1 
ATOM   640   C  CD1 A ILE A  1 78  ? -12.716 16.571  -16.649 0.50 7.57  ? 78  ILE A CD1 1 
ATOM   641   C  CD1 B ILE A  1 78  ? -11.014 18.085  -19.028 0.50 12.56 ? 78  ILE A CD1 1 
ATOM   642   N  N   . GLN A  1 79  ? -15.367 18.352  -20.957 1.00 11.20 ? 79  GLN A N   1 
ATOM   643   C  CA  . GLN A  1 79  ? -16.736 18.202  -21.270 1.00 14.02 ? 79  GLN A CA  1 
ATOM   644   C  C   . GLN A  1 79  ? -17.006 16.691  -21.330 1.00 11.88 ? 79  GLN A C   1 
ATOM   645   O  O   . GLN A  1 79  ? -16.164 15.871  -21.754 1.00 11.95 ? 79  GLN A O   1 
ATOM   646   C  CB  . GLN A  1 79  ? -17.072 18.906  -22.653 1.00 17.12 ? 79  GLN A CB  1 
ATOM   647   C  CG  . GLN A  1 79  ? -18.414 19.721  -22.643 1.00 27.37 ? 79  GLN A CG  1 
ATOM   648   C  CD  . GLN A  1 79  ? -18.317 21.105  -21.867 1.00 30.08 ? 79  GLN A CD  1 
ATOM   649   O  OE1 . GLN A  1 79  ? -17.318 21.440  -21.246 1.00 28.74 ? 79  GLN A OE1 1 
ATOM   650   N  NE2 . GLN A  1 79  ? -19.382 21.898  -21.942 1.00 36.32 ? 79  GLN A NE2 1 
ATOM   651   N  N   . GLY A  1 80  ? -18.206 16.363  -20.913 1.00 12.74 ? 80  GLY A N   1 
ATOM   652   C  CA  . GLY A  1 80  ? -18.696 14.980  -20.902 1.00 11.78 ? 80  GLY A CA  1 
ATOM   653   C  C   . GLY A  1 80  ? -19.311 14.466  -19.648 1.00 13.68 ? 80  GLY A C   1 
ATOM   654   O  O   . GLY A  1 80  ? -20.070 13.487  -19.680 1.00 14.91 ? 80  GLY A O   1 
ATOM   655   N  N   . LEU A  1 81  ? -18.983 15.082  -18.496 1.00 12.24 ? 81  LEU A N   1 
ATOM   656   C  CA  . LEU A  1 81  ? -19.566 14.731  -17.195 1.00 12.32 ? 81  LEU A CA  1 
ATOM   657   C  C   . LEU A  1 81  ? -20.931 15.480  -17.072 1.00 12.94 ? 81  LEU A C   1 
ATOM   658   O  O   . LEU A  1 81  ? -21.282 16.291  -17.939 1.00 15.10 ? 81  LEU A O   1 
ATOM   659   C  CB  . LEU A  1 81  ? -18.614 15.034  -16.030 1.00 12.00 ? 81  LEU A CB  1 
ATOM   660   C  CG  . LEU A  1 81  ? -17.303 14.246  -16.189 1.00 13.02 ? 81  LEU A CG  1 
ATOM   661   C  CD1 . LEU A  1 81  ? -16.235 14.790  -15.194 1.00 14.40 ? 81  LEU A CD1 1 
ATOM   662   C  CD2 . LEU A  1 81  ? -17.592 12.744  -15.992 1.00 15.13 ? 81  LEU A CD2 1 
ATOM   663   N  N   . GLN A  1 82  ? -21.697 15.222  -16.020 1.00 13.64 ? 82  GLN A N   1 
ATOM   664   C  CA  . GLN A  1 82  ? -23.018 15.929  -15.782 1.00 13.81 ? 82  GLN A CA  1 
ATOM   665   C  C   . GLN A  1 82  ? -22.899 17.460  -15.801 1.00 13.05 ? 82  GLN A C   1 
ATOM   666   O  O   . GLN A  1 82  ? -23.794 18.154  -16.335 1.00 13.64 ? 82  GLN A O   1 
ATOM   667   C  CB  . GLN A  1 82  ? -23.700 15.510  -14.456 1.00 12.53 ? 82  GLN A CB  1 
ATOM   668   C  CG  . GLN A  1 82  ? -25.108 16.160  -14.303 1.00 16.00 ? 82  GLN A CG  1 
ATOM   669   C  CD  . GLN A  1 82  ? -25.800 15.782  -12.945 1.00 18.31 ? 82  GLN A CD  1 
ATOM   670   O  OE1 . GLN A  1 82  ? -26.886 15.046  -12.875 1.00 18.83 ? 82  GLN A OE1 1 
ATOM   671   N  NE2 . GLN A  1 82  ? -25.234 16.328  -11.860 1.00 15.67 ? 82  GLN A NE2 1 
ATOM   672   N  N   . SER A  1 83  ? -21.761 17.938  -15.230 1.00 11.85 ? 83  SER A N   1 
ATOM   673   C  CA  . SER A  1 83  ? -21.382 19.337  -15.224 1.00 10.54 ? 83  SER A CA  1 
ATOM   674   C  C   . SER A  1 83  ? -20.095 19.518  -15.969 1.00 10.90 ? 83  SER A C   1 
ATOM   675   O  O   . SER A  1 83  ? -19.331 18.567  -16.089 1.00 11.22 ? 83  SER A O   1 
ATOM   676   C  CB  . SER A  1 83  ? -21.100 19.885  -13.822 1.00 11.54 ? 83  SER A CB  1 
ATOM   677   O  OG  . SER A  1 83  ? -22.384 19.858  -13.138 1.00 13.66 ? 83  SER A OG  1 
ATOM   678   N  N   . ARG A  1 84  ? -19.843 20.724  -16.432 1.00 10.72 ? 84  ARG A N   1 
ATOM   679   C  CA  . ARG A  1 84  ? -18.525 21.151  -16.971 1.00 10.58 ? 84  ARG A CA  1 
ATOM   680   C  C   . ARG A  1 84  ? -17.587 21.298  -15.769 1.00 8.25  ? 84  ARG A C   1 
ATOM   681   O  O   . ARG A  1 84  ? -17.928 21.825  -14.716 1.00 8.10  ? 84  ARG A O   1 
ATOM   682   C  CB  . ARG A  1 84  ? -18.596 22.558  -17.588 1.00 9.95  ? 84  ARG A CB  1 
ATOM   683   C  CG  . ARG A  1 84  ? -17.214 23.072  -18.093 1.00 9.99  ? 84  ARG A CG  1 
ATOM   684   C  CD  . ARG A  1 84  ? -17.337 24.445  -18.705 1.00 9.22  ? 84  ARG A CD  1 
ATOM   685   N  NE  . ARG A  1 84  ? -17.737 24.298  -20.100 1.00 10.40 ? 84  ARG A NE  1 
ATOM   686   C  CZ  . ARG A  1 84  ? -17.869 25.307  -20.947 1.00 12.19 ? 84  ARG A CZ  1 
ATOM   687   N  NH1 . ARG A  1 84  ? -17.638 26.536  -20.520 1.00 11.11 ? 84  ARG A NH1 1 
ATOM   688   N  NH2 . ARG A  1 84  ? -18.235 25.091  -22.208 1.00 11.51 ? 84  ARG A NH2 1 
ATOM   689   N  N   . TYR A  1 85  ? -16.335 20.762  -15.911 1.00 8.84  ? 85  TYR A N   1 
ATOM   690   C  CA  . TYR A  1 85  ? -15.309 20.949  -14.915 1.00 8.42  ? 85  TYR A CA  1 
ATOM   691   C  C   . TYR A  1 85  ? -14.132 21.819  -15.507 1.00 7.95  ? 85  TYR A C   1 
ATOM   692   O  O   . TYR A  1 85  ? -13.679 21.527  -16.608 1.00 11.07 ? 85  TYR A O   1 
ATOM   693   C  CB  . TYR A  1 85  ? -14.694 19.584  -14.382 1.00 9.40  ? 85  TYR A CB  1 
ATOM   694   C  CG  . TYR A  1 85  ? -15.682 18.833  -13.497 1.00 7.91  ? 85  TYR A CG  1 
ATOM   695   C  CD1 . TYR A  1 85  ? -16.793 18.216  -14.077 1.00 10.51 ? 85  TYR A CD1 1 
ATOM   696   C  CD2 . TYR A  1 85  ? -15.449 18.791  -12.128 1.00 5.65  ? 85  TYR A CD2 1 
ATOM   697   C  CE1 . TYR A  1 85  ? -17.709 17.579  -13.254 1.00 9.52  ? 85  TYR A CE1 1 
ATOM   698   C  CE2 . TYR A  1 85  ? -16.365 18.087  -11.241 1.00 7.65  ? 85  TYR A CE2 1 
ATOM   699   C  CZ  . TYR A  1 85  ? -17.448 17.527  -11.857 1.00 7.80  ? 85  TYR A CZ  1 
ATOM   700   O  OH  . TYR A  1 85  ? -18.407 16.798  -11.132 1.00 8.99  ? 85  TYR A OH  1 
ATOM   701   N  N   . SER A  1 86  ? -13.703 22.834  -14.805 1.00 7.18  ? 86  SER A N   1 
ATOM   702   C  CA  . SER A  1 86  ? -12.680 23.771  -15.334 1.00 7.44  ? 86  SER A CA  1 
ATOM   703   C  C   . SER A  1 86  ? -11.338 23.489  -14.609 1.00 8.53  ? 86  SER A C   1 
ATOM   704   O  O   . SER A  1 86  ? -11.329 23.205  -13.379 1.00 7.20  ? 86  SER A O   1 
ATOM   705   C  CB  . SER A  1 86  ? -13.073 25.224  -15.041 1.00 7.77  ? 86  SER A CB  1 
ATOM   706   O  OG  . SER A  1 86  ? -14.280 25.524  -15.799 1.00 10.06 ? 86  SER A OG  1 
ATOM   707   N  N   . ALA A  1 87  ? -10.264 23.601  -15.390 1.00 6.90  ? 87  ALA A N   1 
ATOM   708   C  CA  . ALA A  1 87  ? -8.922  23.251  -14.788 1.00 7.19  ? 87  ALA A CA  1 
ATOM   709   C  C   . ALA A  1 87  ? -8.492  24.321  -13.813 1.00 8.62  ? 87  ALA A C   1 
ATOM   710   O  O   . ALA A  1 87  ? -8.862  25.511  -13.936 1.00 9.05  ? 87  ALA A O   1 
ATOM   711   C  CB  . ALA A  1 87  ? -7.913  23.172  -15.906 1.00 8.99  ? 87  ALA A CB  1 
ATOM   712   N  N   A THR A  1 88  ? -7.655  23.914  -12.860 0.50 7.84  ? 88  THR A N   1 
ATOM   713   N  N   B THR A  1 88  ? -7.703  23.921  -12.810 0.50 6.61  ? 88  THR A N   1 
ATOM   714   C  CA  A THR A  1 88  ? -7.077  24.842  -11.924 0.50 9.07  ? 88  THR A CA  1 
ATOM   715   C  CA  B THR A  1 88  ? -7.021  24.890  -11.970 0.50 6.84  ? 88  THR A CA  1 
ATOM   716   C  C   A THR A  1 88  ? -5.547  24.708  -11.824 0.50 7.84  ? 88  THR A C   1 
ATOM   717   C  C   B THR A  1 88  ? -5.507  24.715  -12.018 0.50 6.19  ? 88  THR A C   1 
ATOM   718   O  O   A THR A  1 88  ? -4.860  25.754  -11.568 0.50 7.58  ? 88  THR A O   1 
ATOM   719   O  O   B THR A  1 88  ? -4.771  25.709  -12.020 0.50 5.83  ? 88  THR A O   1 
ATOM   720   C  CB  A THR A  1 88  ? -7.697  24.715  -10.542 0.50 10.33 ? 88  THR A CB  1 
ATOM   721   C  CB  B THR A  1 88  ? -7.489  24.872  -10.505 0.50 6.97  ? 88  THR A CB  1 
ATOM   722   O  OG1 A THR A  1 88  ? -7.105  25.706  -9.694  0.50 14.64 ? 88  THR A OG1 1 
ATOM   723   O  OG1 B THR A  1 88  ? -7.246  23.598  -9.879  0.50 7.28  ? 88  THR A OG1 1 
ATOM   724   C  CG2 A THR A  1 88  ? -7.536  23.304  -9.978  0.50 11.36 ? 88  THR A CG2 1 
ATOM   725   C  CG2 B THR A  1 88  ? -8.976  25.147  -10.456 0.50 6.76  ? 88  THR A CG2 1 
ATOM   726   N  N   . GLN A  1 89  ? -4.992  23.469  -12.002 1.00 5.90  ? 89  GLN A N   1 
ATOM   727   C  CA  . GLN A  1 89  ? -3.528  23.301  -11.880 1.00 7.16  ? 89  GLN A CA  1 
ATOM   728   C  C   . GLN A  1 89  ? -3.238  21.846  -12.267 1.00 6.84  ? 89  GLN A C   1 
ATOM   729   O  O   . GLN A  1 89  ? -4.150  20.994  -12.232 1.00 6.90  ? 89  GLN A O   1 
ATOM   730   C  CB  . GLN A  1 89  ? -2.998  23.597  -10.487 1.00 6.31  ? 89  GLN A CB  1 
ATOM   731   C  CG  . GLN A  1 89  ? -3.756  22.804  -9.348  1.00 7.35  ? 89  GLN A CG  1 
ATOM   732   C  CD  . GLN A  1 89  ? -2.803  21.760  -8.784  1.00 7.30  ? 89  GLN A CD  1 
ATOM   733   O  OE1 . GLN A  1 89  ? -2.253  20.957  -9.525  1.00 8.47  ? 89  GLN A OE1 1 
ATOM   734   N  NE2 . GLN A  1 89  ? -2.616  21.789  -7.502  1.00 14.20 ? 89  GLN A NE2 1 
ATOM   735   N  N   . LEU A  1 90  ? -1.952  21.616  -12.598 1.00 5.44  ? 90  LEU A N   1 
ATOM   736   C  CA  . LEU A  1 90  ? -1.438  20.200  -12.707 1.00 5.50  ? 90  LEU A CA  1 
ATOM   737   C  C   . LEU A  1 90  ? -0.238  20.119  -11.816 1.00 4.74  ? 90  LEU A C   1 
ATOM   738   O  O   . LEU A  1 90  ? 0.479   21.103  -11.576 1.00 7.05  ? 90  LEU A O   1 
ATOM   739   C  CB  . LEU A  1 90  ? -1.249  19.722  -14.165 1.00 6.18  ? 90  LEU A CB  1 
ATOM   740   C  CG  . LEU A  1 90  ? -0.277  20.554  -15.002 1.00 6.91  ? 90  LEU A CG  1 
ATOM   741   C  CD1 . LEU A  1 90  ? 1.274   20.254  -14.638 1.00 7.30  ? 90  LEU A CD1 1 
ATOM   742   C  CD2 . LEU A  1 90  ? -0.497  20.103  -16.463 1.00 6.35  ? 90  LEU A CD2 1 
ATOM   743   N  N   . HIS A  1 91  ? 0.121   18.878  -11.428 1.00 4.32  ? 91  HIS A N   1 
ATOM   744   C  CA  . HIS A  1 91  ? 1.345   18.649  -10.635 1.00 5.65  ? 91  HIS A CA  1 
ATOM   745   C  C   . HIS A  1 91  ? 1.668   17.151  -10.731 1.00 4.85  ? 91  HIS A C   1 
ATOM   746   O  O   . HIS A  1 91  ? 0.954   16.349  -11.398 1.00 5.00  ? 91  HIS A O   1 
ATOM   747   C  CB  . HIS A  1 91  ? 1.073   19.027  -9.130  1.00 4.72  ? 91  HIS A CB  1 
ATOM   748   C  CG  . HIS A  1 91  ? -0.053  18.161  -8.541  1.00 4.79  ? 91  HIS A CG  1 
ATOM   749   N  ND1 . HIS A  1 91  ? -1.389  18.511  -8.609  1.00 5.35  ? 91  HIS A ND1 1 
ATOM   750   C  CD2 . HIS A  1 91  ? -0.021  16.905  -7.962  1.00 5.96  ? 91  HIS A CD2 1 
ATOM   751   C  CE1 . HIS A  1 91  ? -2.118  17.486  -8.146  1.00 4.06  ? 91  HIS A CE1 1 
ATOM   752   N  NE2 . HIS A  1 91  ? -1.296  16.503  -7.749  1.00 3.98  ? 91  HIS A NE2 1 
ATOM   753   N  N   . LEU A  1 92  ? 2.789   16.743  -10.092 1.00 4.95  ? 92  LEU A N   1 
ATOM   754   C  CA  . LEU A  1 92  ? 3.286   15.336  -10.231 1.00 5.01  ? 92  LEU A CA  1 
ATOM   755   C  C   . LEU A  1 92  ? 3.601   14.706  -8.875  1.00 3.83  ? 92  LEU A C   1 
ATOM   756   O  O   . LEU A  1 92  ? 3.749   15.400  -7.846  1.00 5.03  ? 92  LEU A O   1 
ATOM   757   C  CB  . LEU A  1 92  ? 4.560   15.270  -11.143 1.00 4.90  ? 92  LEU A CB  1 
ATOM   758   C  CG  . LEU A  1 92  ? 4.273   15.779  -12.568 1.00 5.72  ? 92  LEU A CG  1 
ATOM   759   C  CD1 . LEU A  1 92  ? 4.696   17.171  -12.792 1.00 9.36  ? 92  LEU A CD1 1 
ATOM   760   C  CD2 . LEU A  1 92  ? 4.920   14.931  -13.574 1.00 8.92  ? 92  LEU A CD2 1 
ATOM   761   N  N   . HIS A  1 93  ? 3.706   13.379  -8.927  1.00 4.48  ? 93  HIS A N   1 
ATOM   762   C  CA  . HIS A  1 93  ? 4.153   12.552  -7.762  1.00 5.26  ? 93  HIS A CA  1 
ATOM   763   C  C   . HIS A  1 93  ? 5.198   11.552  -8.287  1.00 4.92  ? 93  HIS A C   1 
ATOM   764   O  O   . HIS A  1 93  ? 5.067   11.104  -9.415  1.00 5.45  ? 93  HIS A O   1 
ATOM   765   C  CB  . HIS A  1 93  ? 2.938   11.752  -7.239  1.00 5.39  ? 93  HIS A CB  1 
ATOM   766   C  CG  . HIS A  1 93  ? 1.782   12.614  -6.797  1.00 4.01  ? 93  HIS A CG  1 
ATOM   767   N  ND1 . HIS A  1 93  ? 1.702   13.106  -5.497  1.00 5.96  ? 93  HIS A ND1 1 
ATOM   768   C  CD2 . HIS A  1 93  ? 0.714   13.119  -7.438  1.00 4.12  ? 93  HIS A CD2 1 
ATOM   769   C  CE1 . HIS A  1 93  ? 0.581   13.838  -5.366  1.00 5.60  ? 93  HIS A CE1 1 
ATOM   770   N  NE2 . HIS A  1 93  ? -0.010  13.894  -6.535  1.00 4.97  ? 93  HIS A NE2 1 
ATOM   771   N  N   . TRP A  1 94  ? 6.232   11.296  -7.505  1.00 4.10  ? 94  TRP A N   1 
ATOM   772   C  CA  . TRP A  1 94  ? 7.343   10.429  -7.970  1.00 4.35  ? 94  TRP A CA  1 
ATOM   773   C  C   . TRP A  1 94  ? 8.051   9.833   -6.773  1.00 5.14  ? 94  TRP A C   1 
ATOM   774   O  O   . TRP A  1 94  ? 7.711   10.061  -5.562  1.00 5.29  ? 94  TRP A O   1 
ATOM   775   C  CB  . TRP A  1 94  ? 8.319   11.289  -8.837  1.00 5.16  ? 94  TRP A CB  1 
ATOM   776   C  CG  . TRP A  1 94  ? 8.955   12.446  -8.085  1.00 4.13  ? 94  TRP A CG  1 
ATOM   777   C  CD1 . TRP A  1 94  ? 10.071  12.419  -7.260  1.00 4.38  ? 94  TRP A CD1 1 
ATOM   778   C  CD2 . TRP A  1 94  ? 8.411   13.826  -8.067  1.00 4.30  ? 94  TRP A CD2 1 
ATOM   779   N  NE1 . TRP A  1 94  ? 10.280  13.711  -6.716  1.00 4.79  ? 94  TRP A NE1 1 
ATOM   780   C  CE2 . TRP A  1 94  ? 9.274   14.570  -7.204  1.00 3.98  ? 94  TRP A CE2 1 
ATOM   781   C  CE3 . TRP A  1 94  ? 7.303   14.462  -8.665  1.00 4.68  ? 94  TRP A CE3 1 
ATOM   782   C  CZ2 . TRP A  1 94  ? 9.082   15.899  -7.013  1.00 4.83  ? 94  TRP A CZ2 1 
ATOM   783   C  CZ3 . TRP A  1 94  ? 7.070   15.841  -8.428  1.00 4.94  ? 94  TRP A CZ3 1 
ATOM   784   C  CH2 . TRP A  1 94  ? 8.004   16.547  -7.599  1.00 4.40  ? 94  TRP A CH2 1 
ATOM   785   N  N   . GLY A  1 95  ? 9.010   8.938   -7.094  1.00 4.86  ? 95  GLY A N   1 
ATOM   786   C  CA  . GLY A  1 95  ? 9.772   8.207   -6.085  1.00 6.40  ? 95  GLY A CA  1 
ATOM   787   C  C   . GLY A  1 95  ? 11.145  8.755   -5.775  1.00 5.04  ? 95  GLY A C   1 
ATOM   788   O  O   . GLY A  1 95  ? 11.275  9.893   -5.417  1.00 6.01  ? 95  GLY A O   1 
ATOM   789   N  N   . ASN A  1 96  ? 12.120  7.884   -6.024  1.00 5.62  ? 96  ASN A N   1 
ATOM   790   C  CA  . ASN A  1 96  ? 13.505  8.326   -5.798  1.00 6.25  ? 96  ASN A CA  1 
ATOM   791   C  C   . ASN A  1 96  ? 14.462  7.428   -6.616  1.00 5.86  ? 96  ASN A C   1 
ATOM   792   O  O   . ASN A  1 96  ? 14.062  6.392   -7.126  1.00 6.44  ? 96  ASN A O   1 
ATOM   793   C  CB  . ASN A  1 96  ? 13.855  8.237   -4.298  1.00 9.28  ? 96  ASN A CB  1 
ATOM   794   C  CG  . ASN A  1 96  ? 14.002  6.750   -3.769  1.00 8.98  ? 96  ASN A CG  1 
ATOM   795   O  OD1 . ASN A  1 96  ? 15.181  6.173   -3.908  1.00 13.66 ? 96  ASN A OD1 1 
ATOM   796   N  ND2 . ASN A  1 96  ? 12.941  6.106   -3.302  1.00 9.58  ? 96  ASN A ND2 1 
ATOM   797   N  N   . PRO A  1 97  ? 15.730  7.902   -6.783  1.00 8.08  ? 97  PRO A N   1 
ATOM   798   C  CA  . PRO A  1 97  ? 16.585  7.163   -7.740  1.00 8.05  ? 97  PRO A CA  1 
ATOM   799   C  C   . PRO A  1 97  ? 16.916  5.756   -7.370  1.00 8.30  ? 97  PRO A C   1 
ATOM   800   O  O   . PRO A  1 97  ? 17.139  4.936   -8.251  1.00 10.32 ? 97  PRO A O   1 
ATOM   801   C  CB  . PRO A  1 97  ? 17.899  7.961   -7.799  1.00 10.14 ? 97  PRO A CB  1 
ATOM   802   C  CG  . PRO A  1 97  ? 17.436  9.435   -7.395  1.00 8.29  ? 97  PRO A CG  1 
ATOM   803   C  CD  . PRO A  1 97  ? 16.318  9.201   -6.344  1.00 9.44  ? 97  PRO A CD  1 
ATOM   804   N  N   . ASN A  1 98  ? 16.881  5.459   -6.090  1.00 7.93  ? 98  ASN A N   1 
ATOM   805   C  CA  . ASN A  1 98  ? 17.181  4.035   -5.659  1.00 11.44 ? 98  ASN A CA  1 
ATOM   806   C  C   . ASN A  1 98  ? 15.944  3.098   -5.778  1.00 11.78 ? 98  ASN A C   1 
ATOM   807   O  O   . ASN A  1 98  ? 16.048  1.863   -5.857  1.00 15.70 ? 98  ASN A O   1 
ATOM   808   C  CB  . ASN A  1 98  ? 17.739  4.001   -4.280  1.00 13.69 ? 98  ASN A CB  1 
ATOM   809   C  CG  . ASN A  1 98  ? 19.211  4.571   -4.234  1.00 18.67 ? 98  ASN A CG  1 
ATOM   810   O  OD1 . ASN A  1 98  ? 19.871  4.688   -5.257  1.00 26.75 ? 98  ASN A OD1 1 
ATOM   811   N  ND2 . ASN A  1 98  ? 19.710  4.857   -3.047  1.00 29.96 ? 98  ASN A ND2 1 
ATOM   812   N  N   . ASP A  1 99  ? 14.767  3.689   -5.946  1.00 8.78  ? 99  ASP A N   1 
ATOM   813   C  CA  . ASP A  1 99  ? 13.573  2.869   -6.141  1.00 8.18  ? 99  ASP A CA  1 
ATOM   814   C  C   . ASP A  1 99  ? 12.604  3.754   -6.881  1.00 6.80  ? 99  ASP A C   1 
ATOM   815   O  O   . ASP A  1 99  ? 11.696  4.465   -6.320  1.00 6.55  ? 99  ASP A O   1 
ATOM   816   C  CB  . ASP A  1 99  ? 13.021  2.543   -4.751  1.00 8.97  ? 99  ASP A CB  1 
ATOM   817   C  CG  . ASP A  1 99  ? 11.957  1.453   -4.815  1.00 13.30 ? 99  ASP A CG  1 
ATOM   818   O  OD1 . ASP A  1 99  ? 11.393  1.164   -5.977  1.00 12.95 ? 99  ASP A OD1 1 
ATOM   819   O  OD2 . ASP A  1 99  ? 11.599  0.930   -3.707  1.00 13.57 ? 99  ASP A OD2 1 
ATOM   820   N  N   . PRO A  1 100 ? 12.760  3.797   -8.221  1.00 6.39  ? 100 PRO A N   1 
ATOM   821   C  CA  . PRO A  1 100 ? 12.067  4.834   -9.059  1.00 7.08  ? 100 PRO A CA  1 
ATOM   822   C  C   . PRO A  1 100 ? 10.664  4.425   -9.500  1.00 7.89  ? 100 PRO A C   1 
ATOM   823   O  O   . PRO A  1 100 ? 10.332  4.252   -10.713 1.00 9.32  ? 100 PRO A O   1 
ATOM   824   C  CB  . PRO A  1 100 ? 13.018  4.987   -10.273 1.00 7.88  ? 100 PRO A CB  1 
ATOM   825   C  CG  . PRO A  1 100 ? 13.564  3.458   -10.415 1.00 7.87  ? 100 PRO A CG  1 
ATOM   826   C  CD  . PRO A  1 100 ? 13.839  3.047   -8.987  1.00 7.28  ? 100 PRO A CD  1 
ATOM   827   N  N   . HIS A  1 101 ? 9.846   4.214   -8.468  1.00 6.88  ? 101 HIS A N   1 
ATOM   828   C  CA  . HIS A  1 101 ? 8.443   3.691   -8.581  1.00 8.78  ? 101 HIS A CA  1 
ATOM   829   C  C   . HIS A  1 101 ? 7.621   4.550   -7.613  1.00 11.18 ? 101 HIS A C   1 
ATOM   830   O  O   . HIS A  1 101 ? 7.607   4.360   -6.336  1.00 15.96 ? 101 HIS A O   1 
ATOM   831   C  CB  . HIS A  1 101 ? 8.393   2.201   -8.233  1.00 10.31 ? 101 HIS A CB  1 
ATOM   832   C  CG  . HIS A  1 101 ? 9.424   1.393   -8.977  1.00 12.33 ? 101 HIS A CG  1 
ATOM   833   N  ND1 . HIS A  1 101 ? 9.313   1.099   -10.325 1.00 17.28 ? 101 HIS A ND1 1 
ATOM   834   C  CD2 . HIS A  1 101 ? 10.604  0.851   -8.562  1.00 9.99  ? 101 HIS A CD2 1 
ATOM   835   C  CE1 . HIS A  1 101 ? 10.410  0.458   -10.716 1.00 17.78 ? 101 HIS A CE1 1 
ATOM   836   N  NE2 . HIS A  1 101 ? 11.208  0.325   -9.680  1.00 16.22 ? 101 HIS A NE2 1 
ATOM   837   N  N   . GLY A  1 102 ? 7.133   5.654   -8.115  1.00 6.20  ? 102 GLY A N   1 
ATOM   838   C  CA  . GLY A  1 102 ? 6.404   6.537   -7.270  1.00 5.99  ? 102 GLY A CA  1 
ATOM   839   C  C   . GLY A  1 102 ? 5.120   7.070   -7.860  1.00 3.89  ? 102 GLY A C   1 
ATOM   840   O  O   . GLY A  1 102 ? 4.658   8.157   -7.495  1.00 5.97  ? 102 GLY A O   1 
ATOM   841   N  N   . SER A  1 103 ? 4.488   6.279   -8.735  1.00 4.21  ? 103 SER A N   1 
ATOM   842   C  CA  . SER A  1 103 ? 3.050   6.674   -8.997  1.00 4.53  ? 103 SER A CA  1 
ATOM   843   C  C   . SER A  1 103 ? 2.170   6.512   -7.743  1.00 4.38  ? 103 SER A C   1 
ATOM   844   O  O   . SER A  1 103 ? 2.623   5.891   -6.741  1.00 5.56  ? 103 SER A O   1 
ATOM   845   C  CB  . SER A  1 103 ? 2.485   5.826   -10.141 1.00 5.49  ? 103 SER A CB  1 
ATOM   846   O  OG  . SER A  1 103 ? 2.353   4.435   -9.779  1.00 5.54  ? 103 SER A OG  1 
ATOM   847   N  N   . GLU A  1 104 ? 0.964   7.043   -7.807  1.00 4.23  ? 104 GLU A N   1 
ATOM   848   C  CA  . GLU A  1 104 ? 0.026   6.880   -6.706  1.00 4.01  ? 104 GLU A CA  1 
ATOM   849   C  C   . GLU A  1 104 ? -0.866  5.718   -6.951  1.00 4.58  ? 104 GLU A C   1 
ATOM   850   O  O   . GLU A  1 104 ? -0.897  4.764   -6.149  1.00 5.24  ? 104 GLU A O   1 
ATOM   851   C  CB  . GLU A  1 104 ? -0.755  8.194   -6.534  1.00 3.77  ? 104 GLU A CB  1 
ATOM   852   C  CG  . GLU A  1 104 ? 0.173   9.402   -6.266  1.00 4.23  ? 104 GLU A CG  1 
ATOM   853   C  CD  . GLU A  1 104 ? -0.453  10.314  -5.260  1.00 5.60  ? 104 GLU A CD  1 
ATOM   854   O  OE1 . GLU A  1 104 ? -1.369  11.074  -5.653  1.00 6.00  ? 104 GLU A OE1 1 
ATOM   855   O  OE2 . GLU A  1 104 ? -0.030  10.280  -4.059  1.00 5.67  ? 104 GLU A OE2 1 
ATOM   856   N  N   . HIS A  1 105 ? -1.554  5.731   -8.084  1.00 3.98  ? 105 HIS A N   1 
ATOM   857   C  CA  . HIS A  1 105 ? -2.313  4.526   -8.456  1.00 4.18  ? 105 HIS A CA  1 
ATOM   858   C  C   . HIS A  1 105 ? -1.341  3.416   -8.918  1.00 4.61  ? 105 HIS A C   1 
ATOM   859   O  O   . HIS A  1 105 ? -0.265  3.676   -9.439  1.00 5.38  ? 105 HIS A O   1 
ATOM   860   C  CB  . HIS A  1 105 ? -3.287  4.880   -9.547  1.00 4.59  ? 105 HIS A CB  1 
ATOM   861   C  CG  . HIS A  1 105 ? -4.411  5.760   -9.106  1.00 4.68  ? 105 HIS A CG  1 
ATOM   862   N  ND1 . HIS A  1 105 ? -4.322  7.140   -9.077  1.00 4.56  ? 105 HIS A ND1 1 
ATOM   863   C  CD2 . HIS A  1 105 ? -5.606  5.465   -8.488  1.00 4.53  ? 105 HIS A CD2 1 
ATOM   864   C  CE1 . HIS A  1 105 ? -5.411  7.658   -8.514  1.00 4.60  ? 105 HIS A CE1 1 
ATOM   865   N  NE2 . HIS A  1 105 ? -6.230  6.651   -8.151  1.00 4.13  ? 105 HIS A NE2 1 
ATOM   866   N  N   . THR A  1 106 ? -1.749  2.169   -8.643  1.00 5.31  ? 106 THR A N   1 
ATOM   867   C  CA  . THR A  1 106 ? -1.001  1.041   -9.209  1.00 5.85  ? 106 THR A CA  1 
ATOM   868   C  C   . THR A  1 106 ? -2.015  0.214   -10.035 1.00 6.41  ? 106 THR A C   1 
ATOM   869   O  O   . THR A  1 106 ? -3.199  0.346   -9.892  1.00 6.48  ? 106 THR A O   1 
ATOM   870   C  CB  . THR A  1 106 ? -0.413  0.194   -8.047  1.00 6.80  ? 106 THR A CB  1 
ATOM   871   O  OG1 . THR A  1 106 ? -1.478  -0.265  -7.211  1.00 6.54  ? 106 THR A OG1 1 
ATOM   872   C  CG2 . THR A  1 106 ? 0.613   1.085   -7.180  1.00 8.01  ? 106 THR A CG2 1 
ATOM   873   N  N   . VAL A  1 107 ? -1.439  -0.565  -10.935 1.00 5.71  ? 107 VAL A N   1 
ATOM   874   C  CA  . VAL A  1 107 ? -2.264  -1.440  -11.799 1.00 6.79  ? 107 VAL A CA  1 
ATOM   875   C  C   . VAL A  1 107 ? -1.821  -2.889  -11.606 1.00 6.69  ? 107 VAL A C   1 
ATOM   876   O  O   . VAL A  1 107 ? -0.633  -3.164  -11.844 1.00 8.05  ? 107 VAL A O   1 
ATOM   877   C  CB  . VAL A  1 107 ? -2.179  -1.028  -13.305 1.00 5.79  ? 107 VAL A CB  1 
ATOM   878   C  CG1 . VAL A  1 107 ? -2.951  -2.135  -14.169 1.00 8.67  ? 107 VAL A CG1 1 
ATOM   879   C  CG2 . VAL A  1 107 ? -2.656  0.397   -13.549 1.00 7.61  ? 107 VAL A CG2 1 
ATOM   880   N  N   . SER A  1 108 ? -2.703  -3.750  -11.090 1.00 7.06  ? 108 SER A N   1 
ATOM   881   C  CA  . SER A  1 108 ? -2.316  -5.188  -10.757 1.00 8.75  ? 108 SER A CA  1 
ATOM   882   C  C   . SER A  1 108 ? -1.020  -5.259  -9.961  1.00 8.61  ? 108 SER A C   1 
ATOM   883   O  O   . SER A  1 108 ? -0.072  -6.024  -10.259 1.00 10.11 ? 108 SER A O   1 
ATOM   884   C  CB  . SER A  1 108 ? -2.187  -6.033  -12.070 1.00 9.36  ? 108 SER A CB  1 
ATOM   885   O  OG  . SER A  1 108 ? -3.402  -5.970  -12.752 1.00 13.07 ? 108 SER A OG  1 
ATOM   886   N  N   . GLY A  1 109 ? -0.994  -4.333  -8.945  1.00 7.57  ? 109 GLY A N   1 
ATOM   887   C  CA  . GLY A  1 109 ? 0.137   -4.277  -7.977  1.00 9.66  ? 109 GLY A CA  1 
ATOM   888   C  C   . GLY A  1 109 ? 1.379   -3.522  -8.480  1.00 12.04 ? 109 GLY A C   1 
ATOM   889   O  O   . GLY A  1 109 ? 2.358   -3.376  -7.664  1.00 16.22 ? 109 GLY A O   1 
ATOM   890   N  N   A GLN A  1 110 ? 1.447   -3.031  -9.651  0.50 9.58  ? 110 GLN A N   1 
ATOM   891   N  N   B GLN A  1 110 ? 1.398   -3.268  -9.822  0.50 10.56 ? 110 GLN A N   1 
ATOM   892   C  CA  A GLN A  1 110 ? 2.726   -2.467  -9.999  0.50 8.86  ? 110 GLN A CA  1 
ATOM   893   C  CA  B GLN A  1 110 ? 2.457   -2.530  -10.635 0.50 10.19 ? 110 GLN A CA  1 
ATOM   894   C  C   A GLN A  1 110 ? 2.609   -0.997  -9.951  0.50 7.78  ? 110 GLN A C   1 
ATOM   895   C  C   B GLN A  1 110 ? 2.489   -1.034  -10.266 0.50 9.02  ? 110 GLN A C   1 
ATOM   896   O  O   A GLN A  1 110 ? 1.717   -0.364  -10.571 0.50 6.84  ? 110 GLN A O   1 
ATOM   897   O  O   B GLN A  1 110 ? 1.496   -0.302  -10.428 0.50 7.43  ? 110 GLN A O   1 
ATOM   898   C  CB  A GLN A  1 110 ? 3.092   -2.917  -11.386 0.50 10.27 ? 110 GLN A CB  1 
ATOM   899   C  CB  B GLN A  1 110 ? 2.358   -2.622  -12.188 0.50 10.13 ? 110 GLN A CB  1 
ATOM   900   C  CG  A GLN A  1 110 ? 2.869   -4.466  -11.584 0.50 12.27 ? 110 GLN A CG  1 
ATOM   901   C  CG  B GLN A  1 110 ? 3.704   -2.149  -12.867 0.50 12.04 ? 110 GLN A CG  1 
ATOM   902   C  CD  A GLN A  1 110 ? 3.676   -5.256  -10.559 0.50 10.01 ? 110 GLN A CD  1 
ATOM   903   C  CD  B GLN A  1 110 ? 3.667   -2.002  -14.371 0.50 12.90 ? 110 GLN A CD  1 
ATOM   904   O  OE1 A GLN A  1 110 ? 4.883   -4.998  -10.421 0.50 8.72  ? 110 GLN A OE1 1 
ATOM   905   O  OE1 B GLN A  1 110 ? 2.802   -2.561  -15.031 0.50 10.41 ? 110 GLN A OE1 1 
ATOM   906   N  NE2 A GLN A  1 110 ? 2.986   -6.087  -9.752  0.50 12.38 ? 110 GLN A NE2 1 
ATOM   907   N  NE2 B GLN A  1 110 ? 4.622   -1.243  -14.907 0.50 16.76 ? 110 GLN A NE2 1 
ATOM   908   N  N   A HIS A  1 111 ? 3.523   -0.419  -9.204  0.50 6.53  ? 111 HIS A N   1 
ATOM   909   N  N   B HIS A  1 111 ? 3.667   -0.570  -9.865  0.50 8.39  ? 111 HIS A N   1 
ATOM   910   C  CA  A HIS A  1 111 ? 3.731   0.976   -9.441  0.50 6.37  ? 111 HIS A CA  1 
ATOM   911   C  CA  B HIS A  1 111 ? 3.854   0.797   -9.404  0.50 6.76  ? 111 HIS A CA  1 
ATOM   912   C  C   A HIS A  1 111 ? 4.305   1.258   -10.826 0.50 8.14  ? 111 HIS A C   1 
ATOM   913   C  C   B HIS A  1 111 ? 4.652   1.468   -10.499 0.50 7.80  ? 111 HIS A C   1 
ATOM   914   O  O   A HIS A  1 111 ? 4.924   0.439   -11.524 0.50 8.39  ? 111 HIS A O   1 
ATOM   915   O  O   B HIS A  1 111 ? 5.798   0.998   -10.734 0.50 6.78  ? 111 HIS A O   1 
ATOM   916   C  CB  A HIS A  1 111 ? 4.654   1.614   -8.417  0.50 7.28  ? 111 HIS A CB  1 
ATOM   917   C  CB  B HIS A  1 111 ? 4.658   0.708   -8.087  0.50 7.49  ? 111 HIS A CB  1 
ATOM   918   C  CG  A HIS A  1 111 ? 4.058   1.781   -7.038  0.50 6.51  ? 111 HIS A CG  1 
ATOM   919   C  CG  B HIS A  1 111 ? 4.631   1.943   -7.240  0.50 7.88  ? 111 HIS A CG  1 
ATOM   920   N  ND1 A HIS A  1 111 ? 3.488   2.964   -6.579  0.50 7.06  ? 111 HIS A ND1 1 
ATOM   921   N  ND1 B HIS A  1 111 ? 5.442   2.076   -6.139  0.50 10.92 ? 111 HIS A ND1 1 
ATOM   922   C  CD2 A HIS A  1 111 ? 3.859   0.867   -6.064  0.50 5.83  ? 111 HIS A CD2 1 
ATOM   923   C  CD2 B HIS A  1 111 ? 3.887   3.066   -7.322  0.50 7.50  ? 111 HIS A CD2 1 
ATOM   924   C  CE1 A HIS A  1 111 ? 3.054   2.776   -5.331  0.50 6.40  ? 111 HIS A CE1 1 
ATOM   925   C  CE1 B HIS A  1 111 ? 5.156   3.228   -5.541  0.50 7.37  ? 111 HIS A CE1 1 
ATOM   926   N  NE2 A HIS A  1 111 ? 3.275   1.508   -4.994  0.50 10.84 ? 111 HIS A NE2 1 
ATOM   927   N  NE2 B HIS A  1 111 ? 4.256   3.863   -6.274  0.50 8.86  ? 111 HIS A NE2 1 
ATOM   928   N  N   . PHE A  1 112 ? 4.050   2.483   -11.227 1.00 6.53  ? 112 PHE A N   1 
ATOM   929   C  CA  . PHE A  1 112 ? 4.760   3.147   -12.361 1.00 6.30  ? 112 PHE A CA  1 
ATOM   930   C  C   . PHE A  1 112 ? 5.790   4.139   -11.795 1.00 5.75  ? 112 PHE A C   1 
ATOM   931   O  O   . PHE A  1 112 ? 5.833   4.343   -10.534 1.00 5.22  ? 112 PHE A O   1 
ATOM   932   C  CB  . PHE A  1 112 ? 3.689   3.842   -13.255 1.00 7.28  ? 112 PHE A CB  1 
ATOM   933   C  CG  . PHE A  1 112 ? 2.816   2.800   -13.964 1.00 9.49  ? 112 PHE A CG  1 
ATOM   934   C  CD1 . PHE A  1 112 ? 1.769   2.174   -13.299 1.00 11.15 ? 112 PHE A CD1 1 
ATOM   935   C  CD2 . PHE A  1 112 ? 3.115   2.511   -15.264 1.00 13.93 ? 112 PHE A CD2 1 
ATOM   936   C  CE1 . PHE A  1 112 ? 1.000   1.143   -13.925 1.00 13.27 ? 112 PHE A CE1 1 
ATOM   937   C  CE2 . PHE A  1 112 ? 2.292   1.475   -15.953 1.00 13.58 ? 112 PHE A CE2 1 
ATOM   938   C  CZ  . PHE A  1 112 ? 1.275   0.827   -15.253 1.00 12.50 ? 112 PHE A CZ  1 
ATOM   939   N  N   . ALA A  1 113 ? 6.555   4.729   -12.686 1.00 5.46  ? 113 ALA A N   1 
ATOM   940   C  CA  . ALA A  1 113 ? 7.645   5.561   -12.184 1.00 4.68  ? 113 ALA A CA  1 
ATOM   941   C  C   . ALA A  1 113 ? 7.118   6.851   -11.503 1.00 5.17  ? 113 ALA A C   1 
ATOM   942   O  O   . ALA A  1 113 ? 7.653   7.357   -10.517 1.00 5.78  ? 113 ALA A O   1 
ATOM   943   C  CB  . ALA A  1 113 ? 8.574   5.946   -13.333 1.00 6.92  ? 113 ALA A CB  1 
ATOM   944   N  N   . ALA A  1 114 ? 6.045   7.412   -12.075 1.00 4.25  ? 114 ALA A N   1 
ATOM   945   C  CA  . ALA A  1 114 ? 5.554   8.708   -11.568 1.00 4.34  ? 114 ALA A CA  1 
ATOM   946   C  C   . ALA A  1 114 ? 4.088   8.862   -12.024 1.00 3.59  ? 114 ALA A C   1 
ATOM   947   O  O   . ALA A  1 114 ? 3.512   7.974   -12.722 1.00 4.40  ? 114 ALA A O   1 
ATOM   948   C  CB  . ALA A  1 114 ? 6.427   9.828   -12.134 1.00 5.11  ? 114 ALA A CB  1 
ATOM   949   N  N   . GLU A  1 115 ? 3.444   9.990   -11.645 1.00 4.64  ? 115 GLU A N   1 
ATOM   950   C  CA  . GLU A  1 115 ? 2.011   10.185  -12.026 1.00 4.50  ? 115 GLU A CA  1 
ATOM   951   C  C   . GLU A  1 115 ? 1.806   11.695  -12.131 1.00 4.57  ? 115 GLU A C   1 
ATOM   952   O  O   . GLU A  1 115 ? 2.219   12.462  -11.266 1.00 5.11  ? 115 GLU A O   1 
ATOM   953   C  CB  . GLU A  1 115 ? 1.126   9.552   -10.899 1.00 4.44  ? 115 GLU A CB  1 
ATOM   954   C  CG  . GLU A  1 115 ? -0.436  9.529   -11.248 1.00 4.78  ? 115 GLU A CG  1 
ATOM   955   C  CD  . GLU A  1 115 ? -1.196  8.607   -10.368 1.00 3.19  ? 115 GLU A CD  1 
ATOM   956   O  OE1 . GLU A  1 115 ? -2.386  8.866   -10.140 1.00 5.33  ? 115 GLU A OE1 1 
ATOM   957   O  OE2 . GLU A  1 115 ? -0.632  7.560   -10.062 1.00 4.62  ? 115 GLU A OE2 1 
ATOM   958   N  N   . LEU A  1 116 ? 1.102   12.050  -13.163 1.00 4.63  ? 116 LEU A N   1 
ATOM   959   C  CA  . LEU A  1 116 ? 0.654   13.438  -13.405 1.00 4.85  ? 116 LEU A CA  1 
ATOM   960   C  C   . LEU A  1 116 ? -0.844  13.535  -13.017 1.00 5.38  ? 116 LEU A C   1 
ATOM   961   O  O   . LEU A  1 116 ? -1.678  12.721  -13.468 1.00 4.27  ? 116 LEU A O   1 
ATOM   962   C  CB  . LEU A  1 116 ? 0.796   13.840  -14.905 1.00 6.54  ? 116 LEU A CB  1 
ATOM   963   C  CG  . LEU A  1 116 ? 0.143   15.156  -15.306 1.00 6.04  ? 116 LEU A CG  1 
ATOM   964   C  CD1 . LEU A  1 116 ? 1.054   16.266  -14.902 1.00 9.71  ? 116 LEU A CD1 1 
ATOM   965   C  CD2 . LEU A  1 116 ? 0.024   15.229  -16.839 1.00 7.86  ? 116 LEU A CD2 1 
ATOM   966   N  N   . HIS A  1 117 ? -1.205  14.591  -12.318 1.00 4.33  ? 117 HIS A N   1 
ATOM   967   C  CA  . HIS A  1 117 ? -2.612  14.942  -12.013 1.00 4.45  ? 117 HIS A CA  1 
ATOM   968   C  C   . HIS A  1 117 ? -3.020  16.318  -12.604 1.00 4.06  ? 117 HIS A C   1 
ATOM   969   O  O   . HIS A  1 117 ? -2.233  17.284  -12.390 1.00 4.26  ? 117 HIS A O   1 
ATOM   970   C  CB  . HIS A  1 117 ? -2.820  14.999  -10.495 1.00 6.03  ? 117 HIS A CB  1 
ATOM   971   C  CG  . HIS A  1 117 ? -2.719  13.653  -9.846  1.00 4.95  ? 117 HIS A CG  1 
ATOM   972   N  ND1 . HIS A  1 117 ? -2.410  13.392  -8.526  1.00 5.15  ? 117 HIS A ND1 1 
ATOM   973   C  CD2 . HIS A  1 117 ? -2.854  12.440  -10.461 1.00 5.11  ? 117 HIS A CD2 1 
ATOM   974   C  CE1 . HIS A  1 117 ? -2.404  12.063  -8.314  1.00 5.11  ? 117 HIS A CE1 1 
ATOM   975   N  NE2 . HIS A  1 117 ? -2.678  11.472  -9.472  1.00 5.23  ? 117 HIS A NE2 1 
ATOM   976   N  N   . ILE A  1 118 ? -4.139  16.371  -13.332 1.00 6.04  ? 118 ILE A N   1 
ATOM   977   C  CA  . ILE A  1 118 ? -4.652  17.648  -13.907 1.00 5.80  ? 118 ILE A CA  1 
ATOM   978   C  C   . ILE A  1 118 ? -5.991  17.872  -13.188 1.00 6.39  ? 118 ILE A C   1 
ATOM   979   O  O   . ILE A  1 118 ? -6.930  17.057  -13.296 1.00 5.79  ? 118 ILE A O   1 
ATOM   980   C  CB  . ILE A  1 118 ? -4.896  17.563  -15.386 1.00 5.75  ? 118 ILE A CB  1 
ATOM   981   C  CG1 . ILE A  1 118 ? -3.618  17.074  -16.139 1.00 6.46  ? 118 ILE A CG1 1 
ATOM   982   C  CG2 . ILE A  1 118 ? -5.207  18.998  -15.935 1.00 7.93  ? 118 ILE A CG2 1 
ATOM   983   C  CD1 . ILE A  1 118 ? -3.814  16.945  -17.713 1.00 8.64  ? 118 ILE A CD1 1 
ATOM   984   N  N   . VAL A  1 119 ? -5.935  18.826  -12.255 1.00 4.74  ? 119 VAL A N   1 
ATOM   985   C  CA  . VAL A  1 119 ? -7.046  19.062  -11.329 1.00 5.39  ? 119 VAL A CA  1 
ATOM   986   C  C   . VAL A  1 119 ? -8.085  20.000  -11.933 1.00 7.25  ? 119 VAL A C   1 
ATOM   987   O  O   . VAL A  1 119 ? -7.712  21.065  -12.490 1.00 7.16  ? 119 VAL A O   1 
ATOM   988   C  CB  . VAL A  1 119 ? -6.473  19.721  -10.040 1.00 5.75  ? 119 VAL A CB  1 
ATOM   989   C  CG1 . VAL A  1 119 ? -7.631  20.043  -9.014  1.00 8.24  ? 119 VAL A CG1 1 
ATOM   990   C  CG2 . VAL A  1 119 ? -5.376  18.812  -9.403  1.00 7.07  ? 119 VAL A CG2 1 
ATOM   991   N  N   . HIS A  1 120 ? -9.363  19.630  -11.786 1.00 6.19  ? 120 HIS A N   1 
ATOM   992   C  CA  . HIS A  1 120 ? -10.477 20.472  -12.266 1.00 6.02  ? 120 HIS A CA  1 
ATOM   993   C  C   . HIS A  1 120 ? -11.555 20.510  -11.187 1.00 8.47  ? 120 HIS A C   1 
ATOM   994   O  O   . HIS A  1 120 ? -11.625 19.680  -10.259 1.00 7.91  ? 120 HIS A O   1 
ATOM   995   C  CB  . HIS A  1 120 ? -11.164 19.870  -13.461 1.00 6.89  ? 120 HIS A CB  1 
ATOM   996   C  CG  . HIS A  1 120 ? -10.260 19.531  -14.656 1.00 5.90  ? 120 HIS A CG  1 
ATOM   997   N  ND1 . HIS A  1 120 ? -9.277  18.536  -14.615 1.00 6.14  ? 120 HIS A ND1 1 
ATOM   998   C  CD2 . HIS A  1 120 ? -10.194 20.085  -15.919 1.00 6.14  ? 120 HIS A CD2 1 
ATOM   999   C  CE1 . HIS A  1 120 ? -8.658  18.494  -15.799 1.00 7.51  ? 120 HIS A CE1 1 
ATOM   1000  N  NE2 . HIS A  1 120 ? -9.198  19.424  -16.620 1.00 7.94  ? 120 HIS A NE2 1 
ATOM   1001  N  N   . TYR A  1 121 ? -12.432 21.544  -11.290 1.00 8.32  ? 121 TYR A N   1 
ATOM   1002  C  CA  . TYR A  1 121 ? -13.580 21.657  -10.313 1.00 9.45  ? 121 TYR A CA  1 
ATOM   1003  C  C   . TYR A  1 121 ? -14.848 21.922  -11.119 1.00 7.59  ? 121 TYR A C   1 
ATOM   1004  O  O   . TYR A  1 121 ? -14.829 22.395  -12.260 1.00 7.54  ? 121 TYR A O   1 
ATOM   1005  C  CB  . TYR A  1 121 ? -13.347 22.765  -9.266  1.00 11.40 ? 121 TYR A CB  1 
ATOM   1006  C  CG  . TYR A  1 121 ? -13.567 24.147  -9.775  1.00 13.74 ? 121 TYR A CG  1 
ATOM   1007  C  CD1 . TYR A  1 121 ? -14.752 24.853  -9.468  1.00 15.67 ? 121 TYR A CD1 1 
ATOM   1008  C  CD2 . TYR A  1 121 ? -12.551 24.784  -10.500 1.00 12.75 ? 121 TYR A CD2 1 
ATOM   1009  C  CE1 . TYR A  1 121 ? -14.950 26.110  -9.860  1.00 14.94 ? 121 TYR A CE1 1 
ATOM   1010  C  CE2 . TYR A  1 121 ? -12.724 26.088  -10.960 1.00 15.56 ? 121 TYR A CE2 1 
ATOM   1011  C  CZ  . TYR A  1 121 ? -13.955 26.702  -10.635 1.00 13.04 ? 121 TYR A CZ  1 
ATOM   1012  O  OH  . TYR A  1 121 ? -14.209 28.015  -11.027 1.00 17.01 ? 121 TYR A OH  1 
ATOM   1013  N  N   . ASN A  1 122 ? -15.954 21.587  -10.465 1.00 9.55  ? 122 ASN A N   1 
ATOM   1014  C  CA  . ASN A  1 122 ? -17.299 21.815  -11.078 1.00 9.66  ? 122 ASN A CA  1 
ATOM   1015  C  C   . ASN A  1 122 ? -17.688 23.300  -11.062 1.00 10.25 ? 122 ASN A C   1 
ATOM   1016  O  O   . ASN A  1 122 ? -18.118 23.847  -10.020 1.00 10.56 ? 122 ASN A O   1 
ATOM   1017  C  CB  . ASN A  1 122 ? -18.344 21.001  -10.259 1.00 9.52  ? 122 ASN A CB  1 
ATOM   1018  C  CG  . ASN A  1 122 ? -19.718 21.073  -10.887 1.00 12.15 ? 122 ASN A CG  1 
ATOM   1019  O  OD1 . ASN A  1 122 ? -20.006 22.010  -11.647 1.00 11.02 ? 122 ASN A OD1 1 
ATOM   1020  N  ND2 . ASN A  1 122 ? -20.601 20.085  -10.599 1.00 12.36 ? 122 ASN A ND2 1 
ATOM   1021  N  N   . SER A  1 123 ? -17.428 23.925  -12.206 1.00 9.45  ? 123 SER A N   1 
ATOM   1022  C  CA  . SER A  1 123 ? -17.593 25.360  -12.302 1.00 10.92 ? 123 SER A CA  1 
ATOM   1023  C  C   . SER A  1 123 ? -19.045 25.707  -12.715 1.00 9.47  ? 123 SER A C   1 
ATOM   1024  O  O   . SER A  1 123 ? -19.387 26.899  -12.628 1.00 11.29 ? 123 SER A O   1 
ATOM   1025  C  CB  . SER A  1 123 ? -16.601 25.919  -13.357 1.00 10.17 ? 123 SER A CB  1 
ATOM   1026  O  OG  . SER A  1 123 ? -16.671 25.222  -14.527 1.00 8.43  ? 123 SER A OG  1 
ATOM   1027  N  N   . ASP A  1 124 ? -19.843 24.726  -13.128 1.00 10.33 ? 124 ASP A N   1 
ATOM   1028  C  CA  . ASP A  1 124 ? -21.271 25.089  -13.311 1.00 8.93  ? 124 ASP A CA  1 
ATOM   1029  C  C   . ASP A  1 124 ? -21.917 25.281  -11.937 1.00 12.05 ? 124 ASP A C   1 
ATOM   1030  O  O   . ASP A  1 124 ? -22.844 26.129  -11.846 1.00 13.31 ? 124 ASP A O   1 
ATOM   1031  C  CB  . ASP A  1 124 ? -21.911 23.887  -13.943 1.00 10.08 ? 124 ASP A CB  1 
ATOM   1032  C  CG  . ASP A  1 124 ? -21.633 23.701  -15.439 1.00 10.73 ? 124 ASP A CG  1 
ATOM   1033  O  OD1 . ASP A  1 124 ? -21.209 24.719  -16.074 1.00 10.68 ? 124 ASP A OD1 1 
ATOM   1034  O  OD2 . ASP A  1 124 ? -21.836 22.626  -16.047 1.00 11.08 ? 124 ASP A OD2 1 
ATOM   1035  N  N   . LEU A  1 125 ? -21.586 24.537  -10.913 1.00 11.92 ? 125 LEU A N   1 
ATOM   1036  C  CA  . LEU A  1 125 ? -22.333 24.542  -9.642  1.00 12.30 ? 125 LEU A CA  1 
ATOM   1037  C  C   . LEU A  1 125 ? -21.623 25.343  -8.599  1.00 15.41 ? 125 LEU A C   1 
ATOM   1038  O  O   . LEU A  1 125 ? -22.265 25.797  -7.627  1.00 17.43 ? 125 LEU A O   1 
ATOM   1039  C  CB  . LEU A  1 125 ? -22.531 23.091  -9.143  1.00 15.33 ? 125 LEU A CB  1 
ATOM   1040  C  CG  . LEU A  1 125 ? -23.445 22.209  -9.968  1.00 16.28 ? 125 LEU A CG  1 
ATOM   1041  C  CD1 . LEU A  1 125 ? -23.761 20.990  -9.194  1.00 15.61 ? 125 LEU A CD1 1 
ATOM   1042  C  CD2 . LEU A  1 125 ? -24.795 22.923  -10.231 1.00 14.69 ? 125 LEU A CD2 1 
ATOM   1043  N  N   . TYR A  1 126 ? -20.348 25.608  -8.728  1.00 12.58 ? 126 TYR A N   1 
ATOM   1044  C  CA  . TYR A  1 126 ? -19.577 26.279  -7.663  1.00 14.95 ? 126 TYR A CA  1 
ATOM   1045  C  C   . TYR A  1 126 ? -18.680 27.400  -8.190  1.00 13.65 ? 126 TYR A C   1 
ATOM   1046  O  O   . TYR A  1 126 ? -18.228 27.368  -9.350  1.00 15.48 ? 126 TYR A O   1 
ATOM   1047  C  CB  . TYR A  1 126 ? -18.719 25.280  -6.867  1.00 14.33 ? 126 TYR A CB  1 
ATOM   1048  C  CG  . TYR A  1 126 ? -19.542 24.064  -6.508  1.00 14.67 ? 126 TYR A CG  1 
ATOM   1049  C  CD1 . TYR A  1 126 ? -19.290 22.858  -7.101  1.00 14.43 ? 126 TYR A CD1 1 
ATOM   1050  C  CD2 . TYR A  1 126 ? -20.582 24.162  -5.583  1.00 16.41 ? 126 TYR A CD2 1 
ATOM   1051  C  CE1 . TYR A  1 126 ? -20.028 21.694  -6.775  1.00 14.94 ? 126 TYR A CE1 1 
ATOM   1052  C  CE2 . TYR A  1 126 ? -21.363 23.038  -5.224  1.00 16.97 ? 126 TYR A CE2 1 
ATOM   1053  C  CZ  . TYR A  1 126 ? -21.105 21.790  -5.868  1.00 17.32 ? 126 TYR A CZ  1 
ATOM   1054  O  OH  . TYR A  1 126 ? -21.959 20.708  -5.535  1.00 17.78 ? 126 TYR A OH  1 
ATOM   1055  N  N   . PRO A  1 127 ? -18.476 28.443  -7.344  1.00 17.07 ? 127 PRO A N   1 
ATOM   1056  C  CA  . PRO A  1 127 ? -17.773 29.641  -7.817  1.00 17.60 ? 127 PRO A CA  1 
ATOM   1057  C  C   . PRO A  1 127 ? -16.243 29.471  -7.907  1.00 18.75 ? 127 PRO A C   1 
ATOM   1058  O  O   . PRO A  1 127 ? -15.555 30.201  -8.610  1.00 21.60 ? 127 PRO A O   1 
ATOM   1059  C  CB  . PRO A  1 127 ? -18.122 30.674  -6.714  1.00 18.86 ? 127 PRO A CB  1 
ATOM   1060  C  CG  . PRO A  1 127 ? -18.325 29.830  -5.416  1.00 18.26 ? 127 PRO A CG  1 
ATOM   1061  C  CD  . PRO A  1 127 ? -19.158 28.700  -6.066  1.00 16.79 ? 127 PRO A CD  1 
ATOM   1062  N  N   . ASP A  1 128 ? -15.687 28.519  -7.184  1.00 19.17 ? 128 ASP A N   1 
ATOM   1063  C  CA  . ASP A  1 128 ? -14.277 28.334  -7.233  1.00 18.21 ? 128 ASP A CA  1 
ATOM   1064  C  C   . ASP A  1 128 ? -13.988 26.867  -6.679  1.00 15.42 ? 128 ASP A C   1 
ATOM   1065  O  O   . ASP A  1 128 ? -14.891 26.150  -6.166  1.00 18.13 ? 128 ASP A O   1 
ATOM   1066  C  CB  . ASP A  1 128 ? -13.542 29.366  -6.347  1.00 21.56 ? 128 ASP A CB  1 
ATOM   1067  C  CG  . ASP A  1 128 ? -14.159 29.450  -5.000  1.00 24.68 ? 128 ASP A CG  1 
ATOM   1068  O  OD1 . ASP A  1 128 ? -14.269 28.430  -4.215  1.00 23.21 ? 128 ASP A OD1 1 
ATOM   1069  O  OD2 . ASP A  1 128 ? -14.620 30.570  -4.733  1.00 30.45 ? 128 ASP A OD2 1 
ATOM   1070  N  N   . ALA A  1 129 ? -12.729 26.494  -6.790  1.00 17.84 ? 129 ALA A N   1 
ATOM   1071  C  CA  . ALA A  1 129 ? -12.264 25.135  -6.404  1.00 18.31 ? 129 ALA A CA  1 
ATOM   1072  C  C   . ALA A  1 129 ? -12.312 24.861  -4.893  1.00 18.98 ? 129 ALA A C   1 
ATOM   1073  O  O   . ALA A  1 129 ? -12.709 23.726  -4.457  1.00 16.44 ? 129 ALA A O   1 
ATOM   1074  C  CB  . ALA A  1 129 ? -10.922 24.954  -6.926  1.00 20.44 ? 129 ALA A CB  1 
ATOM   1075  N  N   . SER A  1 130 ? -12.095 25.924  -4.075  1.00 20.16 ? 130 SER A N   1 
ATOM   1076  C  CA  . SER A  1 130 ? -12.253 25.799  -2.608  1.00 19.36 ? 130 SER A CA  1 
ATOM   1077  C  C   . SER A  1 130 ? -13.681 25.425  -2.226  1.00 19.24 ? 130 SER A C   1 
ATOM   1078  O  O   . SER A  1 130 ? -13.893 24.452  -1.482  1.00 19.64 ? 130 SER A O   1 
ATOM   1079  C  CB  . SER A  1 130 ? -11.860 27.121  -1.912  1.00 21.15 ? 130 SER A CB  1 
ATOM   1080  O  OG  . SER A  1 130 ? -11.880 26.826  -0.543  1.00 24.17 ? 130 SER A OG  1 
ATOM   1081  N  N   . THR A  1 131 ? -14.669 26.096  -2.812  1.00 16.10 ? 131 THR A N   1 
ATOM   1082  C  CA  . THR A  1 131 ? -16.035 25.728  -2.502  1.00 18.10 ? 131 THR A CA  1 
ATOM   1083  C  C   . THR A  1 131 ? -16.383 24.329  -2.992  1.00 14.24 ? 131 THR A C   1 
ATOM   1084  O  O   . THR A  1 131 ? -17.036 23.535  -2.286  1.00 18.42 ? 131 THR A O   1 
ATOM   1085  C  CB  . THR A  1 131 ? -17.076 26.775  -3.079  1.00 18.40 ? 131 THR A CB  1 
ATOM   1086  O  OG1 . THR A  1 131 ? -16.743 28.032  -2.492  1.00 21.55 ? 131 THR A OG1 1 
ATOM   1087  C  CG2 . THR A  1 131 ? -18.500 26.422  -2.759  1.00 17.50 ? 131 THR A CG2 1 
ATOM   1088  N  N   . ALA A  1 132 ? -15.879 23.978  -4.206  1.00 17.75 ? 132 ALA A N   1 
ATOM   1089  C  CA  . ALA A  1 132 ? -16.214 22.737  -4.816  1.00 16.05 ? 132 ALA A CA  1 
ATOM   1090  C  C   . ALA A  1 132 ? -15.593 21.587  -4.035  1.00 12.58 ? 132 ALA A C   1 
ATOM   1091  O  O   . ALA A  1 132 ? -16.193 20.496  -3.963  1.00 15.61 ? 132 ALA A O   1 
ATOM   1092  C  CB  . ALA A  1 132 ? -15.670 22.782  -6.250  1.00 15.85 ? 132 ALA A CB  1 
ATOM   1093  N  N   . SER A  1 133 ? -14.515 21.884  -3.344  1.00 12.76 ? 133 SER A N   1 
ATOM   1094  C  CA  . SER A  1 133 ? -13.705 20.826  -2.739  1.00 14.74 ? 133 SER A CA  1 
ATOM   1095  C  C   . SER A  1 133 ? -14.425 20.159  -1.562  1.00 15.59 ? 133 SER A C   1 
ATOM   1096  O  O   . SER A  1 133 ? -14.029 19.016  -1.205  1.00 15.88 ? 133 SER A O   1 
ATOM   1097  C  CB  . SER A  1 133 ? -12.308 21.336  -2.359  1.00 13.03 ? 133 SER A CB  1 
ATOM   1098  O  OG  . SER A  1 133 ? -12.373 22.206  -1.227  1.00 18.81 ? 133 SER A OG  1 
ATOM   1099  N  N   . ASN A  1 134 ? -15.520 20.757  -1.031  1.00 16.58 ? 134 ASN A N   1 
ATOM   1100  C  CA  . ASN A  1 134 ? -16.319 20.140  -0.011  1.00 18.36 ? 134 ASN A CA  1 
ATOM   1101  C  C   . ASN A  1 134 ? -17.649 19.581  -0.456  1.00 21.24 ? 134 ASN A C   1 
ATOM   1102  O  O   . ASN A  1 134 ? -18.477 19.256  0.412   1.00 23.08 ? 134 ASN A O   1 
ATOM   1103  C  CB  . ASN A  1 134 ? -16.560 21.178  1.099   1.00 20.07 ? 134 ASN A CB  1 
ATOM   1104  C  CG  . ASN A  1 134 ? -15.284 21.659  1.679   1.00 23.24 ? 134 ASN A CG  1 
ATOM   1105  O  OD1 . ASN A  1 134 ? -15.027 22.872  1.741   1.00 33.67 ? 134 ASN A OD1 1 
ATOM   1106  N  ND2 . ASN A  1 134 ? -14.451 20.731  2.096   1.00 22.61 ? 134 ASN A ND2 1 
ATOM   1107  N  N   . LYS A  1 135 ? -17.883 19.417  -1.758  1.00 19.52 ? 135 LYS A N   1 
ATOM   1108  C  CA  . LYS A  1 135 ? -19.132 18.921  -2.263  1.00 20.20 ? 135 LYS A CA  1 
ATOM   1109  C  C   . LYS A  1 135 ? -18.869 17.639  -3.002  1.00 20.27 ? 135 LYS A C   1 
ATOM   1110  O  O   . LYS A  1 135 ? -17.817 17.530  -3.602  1.00 15.68 ? 135 LYS A O   1 
ATOM   1111  C  CB  . LYS A  1 135 ? -19.786 20.018  -3.136  1.00 22.06 ? 135 LYS A CB  1 
ATOM   1112  C  CG  . LYS A  1 135 ? -19.816 21.484  -2.464  1.00 27.33 ? 135 LYS A CG  1 
ATOM   1113  C  CD  . LYS A  1 135 ? -20.859 21.590  -1.358  0.01 24.75 ? 135 LYS A CD  1 
ATOM   1114  C  CE  . LYS A  1 135 ? -20.974 23.016  -0.835  0.01 24.04 ? 135 LYS A CE  1 
ATOM   1115  N  NZ  . LYS A  1 135 ? -19.735 23.481  -0.147  0.01 23.92 ? 135 LYS A NZ  1 
ATOM   1116  N  N   . SER A  1 136 ? -19.792 16.675  -2.931  1.00 20.24 ? 136 SER A N   1 
ATOM   1117  C  CA  . SER A  1 136 ? -19.627 15.385  -3.583  1.00 20.53 ? 136 SER A CA  1 
ATOM   1118  C  C   . SER A  1 136 ? -19.484 15.706  -5.077  1.00 19.66 ? 136 SER A C   1 
ATOM   1119  O  O   . SER A  1 136 ? -20.162 16.585  -5.604  1.00 18.18 ? 136 SER A O   1 
ATOM   1120  C  CB  . SER A  1 136 ? -20.879 14.462  -3.366  1.00 21.18 ? 136 SER A CB  1 
ATOM   1121  O  OG  . SER A  1 136 ? -20.617 13.098  -3.844  1.00 30.17 ? 136 SER A OG  1 
ATOM   1122  N  N   . GLU A  1 137 ? -18.621 14.934  -5.751  1.00 17.59 ? 137 GLU A N   1 
ATOM   1123  C  CA  . GLU A  1 137 ? -18.251 15.200  -7.193  1.00 18.53 ? 137 GLU A CA  1 
ATOM   1124  C  C   . GLU A  1 137 ? -17.837 16.669  -7.482  1.00 17.14 ? 137 GLU A C   1 
ATOM   1125  O  O   . GLU A  1 137 ? -17.920 17.063  -8.689  1.00 15.21 ? 137 GLU A O   1 
ATOM   1126  C  CB  . GLU A  1 137 ? -19.400 14.822  -8.154  1.00 21.81 ? 137 GLU A CB  1 
ATOM   1127  C  CG  . GLU A  1 137 ? -20.354 13.694  -7.709  1.00 30.04 ? 137 GLU A CG  1 
ATOM   1128  C  CD  . GLU A  1 137 ? -19.836 12.309  -8.012  1.00 39.80 ? 137 GLU A CD  1 
ATOM   1129  O  OE1 . GLU A  1 137 ? -19.797 11.934  -9.219  1.00 40.57 ? 137 GLU A OE1 1 
ATOM   1130  O  OE2 . GLU A  1 137 ? -19.531 11.584  -7.028  1.00 43.83 ? 137 GLU A OE2 1 
ATOM   1131  N  N   . GLY A  1 138 ? -17.494 17.514  -6.461  1.00 12.85 ? 138 GLY A N   1 
ATOM   1132  C  CA  . GLY A  1 138 ? -17.013 18.865  -6.657  1.00 12.30 ? 138 GLY A CA  1 
ATOM   1133  C  C   . GLY A  1 138 ? -15.724 19.028  -7.516  1.00 11.30 ? 138 GLY A C   1 
ATOM   1134  O  O   . GLY A  1 138 ? -15.483 20.050  -8.163  1.00 11.96 ? 138 GLY A O   1 
ATOM   1135  N  N   . LEU A  1 139 ? -14.879 17.967  -7.484  1.00 9.19  ? 139 LEU A N   1 
ATOM   1136  C  CA  . LEU A  1 139 ? -13.568 17.986  -8.188  1.00 8.61  ? 139 LEU A CA  1 
ATOM   1137  C  C   . LEU A  1 139 ? -13.546 16.830  -9.161  1.00 7.35  ? 139 LEU A C   1 
ATOM   1138  O  O   . LEU A  1 139 ? -14.173 15.766  -8.879  1.00 8.57  ? 139 LEU A O   1 
ATOM   1139  C  CB  . LEU A  1 139 ? -12.457 17.798  -7.145  1.00 8.89  ? 139 LEU A CB  1 
ATOM   1140  C  CG  . LEU A  1 139 ? -12.426 18.927  -6.055  1.00 7.92  ? 139 LEU A CG  1 
ATOM   1141  C  CD1 . LEU A  1 139 ? -11.315 18.557  -4.952  1.00 10.71 ? 139 LEU A CD1 1 
ATOM   1142  C  CD2 . LEU A  1 139 ? -12.131 20.337  -6.653  1.00 12.38 ? 139 LEU A CD2 1 
ATOM   1143  N  N   . ALA A  1 140 ? -12.771 16.974  -10.261 1.00 5.81  ? 140 ALA A N   1 
ATOM   1144  C  CA  . ALA A  1 140 ? -12.520 15.877  -11.209 1.00 6.45  ? 140 ALA A CA  1 
ATOM   1145  C  C   . ALA A  1 140 ? -11.023 16.001  -11.496 1.00 6.38  ? 140 ALA A C   1 
ATOM   1146  O  O   . ALA A  1 140 ? -10.514 17.049  -11.922 1.00 7.17  ? 140 ALA A O   1 
ATOM   1147  C  CB  . ALA A  1 140 ? -13.300 16.058  -12.503 1.00 7.15  ? 140 ALA A CB  1 
ATOM   1148  N  N   . VAL A  1 141 ? -10.312 14.871  -11.233 1.00 5.74  ? 141 VAL A N   1 
ATOM   1149  C  CA  . VAL A  1 141 ? -8.863  14.862  -11.499 1.00 5.94  ? 141 VAL A CA  1 
ATOM   1150  C  C   . VAL A  1 141 ? -8.573  13.826  -12.575 1.00 6.28  ? 141 VAL A C   1 
ATOM   1151  O  O   . VAL A  1 141 ? -9.156  12.723  -12.535 1.00 6.00  ? 141 VAL A O   1 
ATOM   1152  C  CB  . VAL A  1 141 ? -8.006  14.512  -10.261 1.00 5.49  ? 141 VAL A CB  1 
ATOM   1153  C  CG1 . VAL A  1 141 ? -6.494  14.584  -10.536 1.00 7.00  ? 141 VAL A CG1 1 
ATOM   1154  C  CG2 . VAL A  1 141 ? -8.354  15.544  -9.129  1.00 6.99  ? 141 VAL A CG2 1 
ATOM   1155  N  N   . LEU A  1 142 ? -7.759  14.230  -13.549 1.00 5.39  ? 142 LEU A N   1 
ATOM   1156  C  CA  . LEU A  1 142 ? -7.262  13.300  -14.575 1.00 6.36  ? 142 LEU A CA  1 
ATOM   1157  C  C   . LEU A  1 142 ? -5.881  12.782  -14.145 1.00 5.66  ? 142 LEU A C   1 
ATOM   1158  O  O   . LEU A  1 142 ? -5.024  13.637  -13.787 1.00 6.68  ? 142 LEU A O   1 
ATOM   1159  C  CB  . LEU A  1 142 ? -7.073  14.006  -15.952 1.00 7.07  ? 142 LEU A CB  1 
ATOM   1160  C  CG  . LEU A  1 142 ? -8.384  14.625  -16.545 1.00 6.49  ? 142 LEU A CG  1 
ATOM   1161  C  CD1 . LEU A  1 142 ? -8.015  15.220  -17.884 1.00 7.69  ? 142 LEU A CD1 1 
ATOM   1162  C  CD2 . LEU A  1 142 ? -9.498  13.736  -16.603 1.00 7.38  ? 142 LEU A CD2 1 
ATOM   1163  N  N   . ALA A  1 143 ? -5.675  11.467  -14.194 1.00 3.82  ? 143 ALA A N   1 
ATOM   1164  C  CA  . ALA A  1 143 ? -4.320  10.903  -13.800 1.00 4.35  ? 143 ALA A CA  1 
ATOM   1165  C  C   . ALA A  1 143 ? -3.680  10.285  -15.007 1.00 4.45  ? 143 ALA A C   1 
ATOM   1166  O  O   . ALA A  1 143 ? -4.325  9.413   -15.685 1.00 4.83  ? 143 ALA A O   1 
ATOM   1167  C  CB  . ALA A  1 143 ? -4.473  9.890   -12.742 1.00 6.21  ? 143 ALA A CB  1 
ATOM   1168  N  N   . VAL A  1 144 ? -2.419  10.592  -15.264 1.00 4.83  ? 144 VAL A N   1 
ATOM   1169  C  CA  . VAL A  1 144 ? -1.581  9.942   -16.295 1.00 4.45  ? 144 VAL A CA  1 
ATOM   1170  C  C   . VAL A  1 144 ? -0.434  9.202   -15.615 1.00 4.97  ? 144 VAL A C   1 
ATOM   1171  O  O   . VAL A  1 144 ? 0.303   9.810   -14.842 1.00 5.11  ? 144 VAL A O   1 
ATOM   1172  C  CB  . VAL A  1 144 ? -0.984  10.931  -17.300 1.00 5.26  ? 144 VAL A CB  1 
ATOM   1173  C  CG1 . VAL A  1 144 ? -0.179  10.171  -18.383 1.00 6.25  ? 144 VAL A CG1 1 
ATOM   1174  C  CG2 . VAL A  1 144 ? -2.159  11.783  -17.959 1.00 5.58  ? 144 VAL A CG2 1 
ATOM   1175  N  N   . LEU A  1 145 ? -0.430  7.886   -15.813 1.00 7.00  ? 145 LEU A N   1 
ATOM   1176  C  CA  . LEU A  1 145 ? 0.695   7.022   -15.284 1.00 5.27  ? 145 LEU A CA  1 
ATOM   1177  C  C   . LEU A  1 145 ? 1.934   7.257   -16.131 1.00 4.96  ? 145 LEU A C   1 
ATOM   1178  O  O   . LEU A  1 145 ? 1.819   7.332   -17.385 1.00 6.01  ? 145 LEU A O   1 
ATOM   1179  C  CB  . LEU A  1 145 ? 0.250   5.620   -15.323 1.00 7.32  ? 145 LEU A CB  1 
ATOM   1180  C  CG  . LEU A  1 145 ? -1.005  5.244   -14.462 1.00 6.14  ? 145 LEU A CG  1 
ATOM   1181  C  CD1 . LEU A  1 145 ? -1.536  3.813   -14.873 1.00 8.26  ? 145 LEU A CD1 1 
ATOM   1182  C  CD2 . LEU A  1 145 ? -0.661  5.385   -12.989 1.00 7.94  ? 145 LEU A CD2 1 
ATOM   1183  N  N   . ILE A  1 146 ? 3.127   7.358   -15.537 1.00 5.20  ? 146 ILE A N   1 
ATOM   1184  C  CA  . ILE A  1 146 ? 4.321   7.678   -16.253 1.00 5.20  ? 146 ILE A CA  1 
ATOM   1185  C  C   . ILE A  1 146 ? 5.346   6.558   -16.035 1.00 7.02  ? 146 ILE A C   1 
ATOM   1186  O  O   . ILE A  1 146 ? 5.616   6.129   -14.903 1.00 7.21  ? 146 ILE A O   1 
ATOM   1187  C  CB  . ILE A  1 146 ? 4.936   9.002   -15.733 1.00 5.10  ? 146 ILE A CB  1 
ATOM   1188  C  CG1 . ILE A  1 146 ? 3.923   10.141  -15.988 1.00 5.33  ? 146 ILE A CG1 1 
ATOM   1189  C  CG2 . ILE A  1 146 ? 6.288   9.311   -16.383 1.00 7.48  ? 146 ILE A CG2 1 
ATOM   1190  C  CD1 . ILE A  1 146 ? 4.305   11.444  -15.234 1.00 5.22  ? 146 ILE A CD1 1 
ATOM   1191  N  N   . GLU A  1 147 ? 5.929   6.080   -17.164 1.00 5.59  ? 147 GLU A N   1 
ATOM   1192  C  CA  . GLU A  1 147 ? 6.942   5.043   -17.088 1.00 6.05  ? 147 GLU A CA  1 
ATOM   1193  C  C   . GLU A  1 147 ? 8.248   5.628   -17.684 1.00 6.33  ? 147 GLU A C   1 
ATOM   1194  O  O   . GLU A  1 147 ? 8.240   6.537   -18.521 1.00 6.51  ? 147 GLU A O   1 
ATOM   1195  C  CB  . GLU A  1 147 ? 6.540   3.772   -17.802 1.00 11.74 ? 147 GLU A CB  1 
ATOM   1196  C  CG  . GLU A  1 147 ? 6.228   3.856   -19.255 1.00 15.47 ? 147 GLU A CG  1 
ATOM   1197  C  CD  . GLU A  1 147 ? 5.716   2.530   -19.783 1.00 25.67 ? 147 GLU A CD  1 
ATOM   1198  O  OE1 . GLU A  1 147 ? 5.396   1.633   -18.965 1.00 18.37 ? 147 GLU A OE1 1 
ATOM   1199  O  OE2 . GLU A  1 147 ? 5.636   2.389   -21.016 1.00 21.85 ? 147 GLU A OE2 1 
ATOM   1200  N  N   . MET A  1 148 ? 9.385   5.048   -17.217 1.00 5.42  ? 148 MET A N   1 
ATOM   1201  C  CA  . MET A  1 148 ? 10.657  5.430   -17.819 1.00 6.14  ? 148 MET A CA  1 
ATOM   1202  C  C   . MET A  1 148 ? 10.837  4.773   -19.196 1.00 7.27  ? 148 MET A C   1 
ATOM   1203  O  O   . MET A  1 148 ? 10.703  3.558   -19.292 1.00 8.95  ? 148 MET A O   1 
ATOM   1204  C  CB  . MET A  1 148 ? 11.778  5.035   -16.848 1.00 8.09  ? 148 MET A CB  1 
ATOM   1205  C  CG  . MET A  1 148 ? 13.106  5.599   -17.182 1.00 9.81  ? 148 MET A CG  1 
ATOM   1206  S  SD  . MET A  1 148 ? 13.987  4.609   -18.489 1.00 12.52 ? 148 MET A SD  1 
ATOM   1207  C  CE  . MET A  1 148 ? 14.641  3.331   -17.429 1.00 12.91 ? 148 MET A CE  1 
ATOM   1208  N  N   . GLY A  1 149 ? 11.261  5.531   -20.185 1.00 5.81  ? 149 GLY A N   1 
ATOM   1209  C  CA  . GLY A  1 149 ? 11.613  4.933   -21.516 1.00 6.98  ? 149 GLY A CA  1 
ATOM   1210  C  C   . GLY A  1 149 ? 12.097  6.076   -22.404 1.00 7.03  ? 149 GLY A C   1 
ATOM   1211  O  O   . GLY A  1 149 ? 13.199  6.613   -22.210 1.00 6.11  ? 149 GLY A O   1 
ATOM   1212  N  N   . SER A  1 150 ? 11.242  6.442   -23.377 1.00 5.63  ? 150 SER A N   1 
ATOM   1213  C  CA  . SER A  1 150 ? 11.617  7.458   -24.366 1.00 5.68  ? 150 SER A CA  1 
ATOM   1214  C  C   . SER A  1 150 ? 11.478  8.878   -23.739 1.00 5.49  ? 150 SER A C   1 
ATOM   1215  O  O   . SER A  1 150 ? 10.444  9.213   -23.038 1.00 6.93  ? 150 SER A O   1 
ATOM   1216  C  CB  . SER A  1 150 ? 10.655  7.472   -25.568 1.00 6.43  ? 150 SER A CB  1 
ATOM   1217  O  OG  . SER A  1 150 ? 10.714  6.187   -26.209 1.00 6.12  ? 150 SER A OG  1 
ATOM   1218  N  N   . PHE A  1 151 ? 12.384  9.733   -24.167 1.00 5.30  ? 151 PHE A N   1 
ATOM   1219  C  CA  . PHE A  1 151 ? 12.282  11.181  -23.921 1.00 5.32  ? 151 PHE A CA  1 
ATOM   1220  C  C   . PHE A  1 151 ? 10.930  11.652  -24.395 1.00 7.41  ? 151 PHE A C   1 
ATOM   1221  O  O   . PHE A  1 151 ? 10.409  11.221  -25.448 1.00 6.70  ? 151 PHE A O   1 
ATOM   1222  C  CB  . PHE A  1 151 ? 13.392  11.938  -24.706 1.00 6.96  ? 151 PHE A CB  1 
ATOM   1223  C  CG  . PHE A  1 151 ? 13.355  13.411  -24.555 1.00 5.61  ? 151 PHE A CG  1 
ATOM   1224  C  CD1 . PHE A  1 151 ? 13.863  13.994  -23.438 1.00 8.88  ? 151 PHE A CD1 1 
ATOM   1225  C  CD2 . PHE A  1 151 ? 12.890  14.219  -25.583 1.00 8.99  ? 151 PHE A CD2 1 
ATOM   1226  C  CE1 . PHE A  1 151 ? 13.776  15.450  -23.215 1.00 7.45  ? 151 PHE A CE1 1 
ATOM   1227  C  CE2 . PHE A  1 151 ? 12.904  15.660  -25.445 1.00 7.86  ? 151 PHE A CE2 1 
ATOM   1228  C  CZ  . PHE A  1 151 ? 13.340  16.206  -24.282 1.00 7.48  ? 151 PHE A CZ  1 
ATOM   1229  N  N   . ASN A  1 152 ? 10.353  12.638  -23.655 1.00 7.45  ? 152 ASN A N   1 
ATOM   1230  C  CA  . ASN A  1 152 ? 9.034   13.208  -24.005 1.00 6.32  ? 152 ASN A CA  1 
ATOM   1231  C  C   . ASN A  1 152 ? 9.146   14.716  -24.184 1.00 7.18  ? 152 ASN A C   1 
ATOM   1232  O  O   . ASN A  1 152 ? 9.350   15.441  -23.198 1.00 7.32  ? 152 ASN A O   1 
ATOM   1233  C  CB  . ASN A  1 152 ? 8.037   12.814  -22.889 1.00 6.53  ? 152 ASN A CB  1 
ATOM   1234  C  CG  . ASN A  1 152 ? 6.642   13.063  -23.292 1.00 6.30  ? 152 ASN A CG  1 
ATOM   1235  O  OD1 . ASN A  1 152 ? 6.276   14.192  -23.693 1.00 7.22  ? 152 ASN A OD1 1 
ATOM   1236  N  ND2 . ASN A  1 152 ? 5.794   12.064  -23.147 1.00 7.72  ? 152 ASN A ND2 1 
ATOM   1237  N  N   . PRO A  1 153 ? 9.131   15.216  -25.437 1.00 7.74  ? 153 PRO A N   1 
ATOM   1238  C  CA  . PRO A  1 153 ? 9.296   16.656  -25.607 1.00 6.59  ? 153 PRO A CA  1 
ATOM   1239  C  C   . PRO A  1 153 ? 8.229   17.477  -24.872 1.00 7.81  ? 153 PRO A C   1 
ATOM   1240  O  O   . PRO A  1 153 ? 8.511   18.606  -24.372 1.00 9.18  ? 153 PRO A O   1 
ATOM   1241  C  CB  . PRO A  1 153 ? 9.168   16.857  -27.111 1.00 8.87  ? 153 PRO A CB  1 
ATOM   1242  C  CG  . PRO A  1 153 ? 9.634   15.512  -27.716 1.00 10.54 ? 153 PRO A CG  1 
ATOM   1243  C  CD  . PRO A  1 153 ? 9.151   14.424  -26.697 1.00 8.12  ? 153 PRO A CD  1 
ATOM   1244  N  N   . SER A  1 154 ? 7.003   16.957  -24.773 1.00 6.89  ? 154 SER A N   1 
ATOM   1245  C  CA  . SER A  1 154 ? 5.927   17.775  -24.202 1.00 8.33  ? 154 SER A CA  1 
ATOM   1246  C  C   . SER A  1 154 ? 6.106   17.858  -22.661 1.00 6.80  ? 154 SER A C   1 
ATOM   1247  O  O   . SER A  1 154 ? 6.042   18.968  -22.047 1.00 7.54  ? 154 SER A O   1 
ATOM   1248  C  CB  . SER A  1 154 ? 4.577   17.138  -24.520 1.00 9.02  ? 154 SER A CB  1 
ATOM   1249  O  OG  . SER A  1 154 ? 4.412   17.306  -25.951 1.00 15.43 ? 154 SER A OG  1 
ATOM   1250  N  N   . TYR A  1 155 ? 6.447   16.713  -22.000 1.00 6.75  ? 155 TYR A N   1 
ATOM   1251  C  CA  . TYR A  1 155 ? 6.736   16.824  -20.569 1.00 6.17  ? 155 TYR A CA  1 
ATOM   1252  C  C   . TYR A  1 155 ? 7.981   17.738  -20.334 1.00 5.60  ? 155 TYR A C   1 
ATOM   1253  O  O   . TYR A  1 155 ? 8.116   18.385  -19.302 1.00 6.49  ? 155 TYR A O   1 
ATOM   1254  C  CB  . TYR A  1 155 ? 6.958   15.459  -19.903 1.00 6.01  ? 155 TYR A CB  1 
ATOM   1255  C  CG  . TYR A  1 155 ? 5.654   14.822  -19.575 1.00 4.06  ? 155 TYR A CG  1 
ATOM   1256  C  CD1 . TYR A  1 155 ? 4.866   14.133  -20.533 1.00 3.92  ? 155 TYR A CD1 1 
ATOM   1257  C  CD2 . TYR A  1 155 ? 5.182   14.842  -18.287 1.00 5.15  ? 155 TYR A CD2 1 
ATOM   1258  C  CE1 . TYR A  1 155 ? 3.609   13.597  -20.227 1.00 7.81  ? 155 TYR A CE1 1 
ATOM   1259  C  CE2 . TYR A  1 155 ? 3.903   14.259  -17.966 1.00 4.68  ? 155 TYR A CE2 1 
ATOM   1260  C  CZ  . TYR A  1 155 ? 3.157   13.632  -18.939 1.00 6.10  ? 155 TYR A CZ  1 
ATOM   1261  O  OH  . TYR A  1 155 ? 1.940   13.103  -18.610 1.00 6.78  ? 155 TYR A OH  1 
ATOM   1262  N  N   . ASP A  1 156 ? 8.931   17.814  -21.297 1.00 6.09  ? 156 ASP A N   1 
ATOM   1263  C  CA  . ASP A  1 156 ? 10.111  18.659  -21.119 1.00 8.07  ? 156 ASP A CA  1 
ATOM   1264  C  C   . ASP A  1 156 ? 9.745   20.163  -21.068 1.00 5.00  ? 156 ASP A C   1 
ATOM   1265  O  O   . ASP A  1 156 ? 10.585  20.918  -20.528 1.00 7.03  ? 156 ASP A O   1 
ATOM   1266  C  CB  . ASP A  1 156 ? 11.243  18.365  -22.149 1.00 8.34  ? 156 ASP A CB  1 
ATOM   1267  C  CG  . ASP A  1 156 ? 12.614  18.306  -21.507 1.00 9.67  ? 156 ASP A CG  1 
ATOM   1268  O  OD1 . ASP A  1 156 ? 13.538  18.971  -22.018 1.00 12.79 ? 156 ASP A OD1 1 
ATOM   1269  O  OD2 . ASP A  1 156 ? 12.770  17.592  -20.495 1.00 9.13  ? 156 ASP A OD2 1 
ATOM   1270  N  N   . LYS A  1 157 ? 8.564   20.480  -21.607 1.00 6.12  ? 157 LYS A N   1 
ATOM   1271  C  CA  . LYS A  1 157 ? 8.158   21.922  -21.525 1.00 7.35  ? 157 LYS A CA  1 
ATOM   1272  C  C   . LYS A  1 157 ? 8.007   22.290  -20.055 1.00 8.36  ? 157 LYS A C   1 
ATOM   1273  O  O   . LYS A  1 157 ? 8.112   23.483  -19.656 1.00 9.77  ? 157 LYS A O   1 
ATOM   1274  C  CB  . LYS A  1 157 ? 6.826   22.163  -22.195 1.00 9.15  ? 157 LYS A CB  1 
ATOM   1275  C  CG  . LYS A  1 157 ? 6.894   21.913  -23.736 1.00 13.20 ? 157 LYS A CG  1 
ATOM   1276  C  CD  . LYS A  1 157 ? 7.787   22.807  -24.452 1.00 17.16 ? 157 LYS A CD  1 
ATOM   1277  C  CE  . LYS A  1 157 ? 7.399   22.643  -25.890 1.00 20.23 ? 157 LYS A CE  1 
ATOM   1278  N  NZ  . LYS A  1 157 ? 8.038   23.755  -26.629 1.00 22.81 ? 157 LYS A NZ  1 
ATOM   1279  N  N   . ILE A  1 158 ? 7.721   21.316  -19.166 1.00 8.03  ? 158 ILE A N   1 
ATOM   1280  C  CA  . ILE A  1 158 ? 7.702   21.565  -17.689 1.00 7.24  ? 158 ILE A CA  1 
ATOM   1281  C  C   . ILE A  1 158 ? 9.088   21.259  -17.110 1.00 6.74  ? 158 ILE A C   1 
ATOM   1282  O  O   . ILE A  1 158 ? 9.679   22.049  -16.375 1.00 7.06  ? 158 ILE A O   1 
ATOM   1283  C  CB  . ILE A  1 158 ? 6.671   20.616  -17.002 1.00 7.77  ? 158 ILE A CB  1 
ATOM   1284  C  CG1 . ILE A  1 158 ? 5.234   21.028  -17.461 1.00 9.55  ? 158 ILE A CG1 1 
ATOM   1285  C  CG2 . ILE A  1 158 ? 6.816   20.679  -15.431 1.00 6.00  ? 158 ILE A CG2 1 
ATOM   1286  C  CD1 . ILE A  1 158 ? 4.291   19.891  -17.143 1.00 11.46 ? 158 ILE A CD1 1 
ATOM   1287  N  N   . PHE A  1 159 ? 9.638   20.051  -17.410 1.00 6.27  ? 159 PHE A N   1 
ATOM   1288  C  CA  . PHE A  1 159 ? 10.879  19.610  -16.719 1.00 6.88  ? 159 PHE A CA  1 
ATOM   1289  C  C   . PHE A  1 159 ? 12.133  20.486  -17.009 1.00 6.87  ? 159 PHE A C   1 
ATOM   1290  O  O   . PHE A  1 159 ? 13.021  20.541  -16.164 1.00 8.61  ? 159 PHE A O   1 
ATOM   1291  C  CB  . PHE A  1 159 ? 11.253  18.203  -17.117 1.00 7.77  ? 159 PHE A CB  1 
ATOM   1292  C  CG  . PHE A  1 159 ? 10.220  17.157  -16.705 1.00 6.84  ? 159 PHE A CG  1 
ATOM   1293  C  CD1 . PHE A  1 159 ? 9.280   17.360  -15.690 1.00 7.78  ? 159 PHE A CD1 1 
ATOM   1294  C  CD2 . PHE A  1 159 ? 10.150  15.935  -17.409 1.00 8.65  ? 159 PHE A CD2 1 
ATOM   1295  C  CE1 . PHE A  1 159 ? 8.342   16.401  -15.326 1.00 8.53  ? 159 PHE A CE1 1 
ATOM   1296  C  CE2 . PHE A  1 159 ? 9.165   14.969  -17.031 1.00 8.49  ? 159 PHE A CE2 1 
ATOM   1297  C  CZ  . PHE A  1 159 ? 8.315   15.210  -15.976 1.00 8.37  ? 159 PHE A CZ  1 
ATOM   1298  N  N   . SER A  1 160 ? 12.137  21.123  -18.171 1.00 8.39  ? 160 SER A N   1 
ATOM   1299  C  CA  . SER A  1 160 ? 13.314  22.004  -18.470 1.00 8.01  ? 160 SER A CA  1 
ATOM   1300  C  C   . SER A  1 160 ? 13.437  23.122  -17.480 1.00 8.27  ? 160 SER A C   1 
ATOM   1301  O  O   . SER A  1 160 ? 14.507  23.799  -17.485 1.00 11.32 ? 160 SER A O   1 
ATOM   1302  C  CB  . SER A  1 160 ? 13.243  22.489  -19.918 1.00 9.05  ? 160 SER A CB  1 
ATOM   1303  O  OG  . SER A  1 160 ? 12.153  23.420  -20.080 1.00 11.44 ? 160 SER A OG  1 
ATOM   1304  N  N   . HIS A  1 161 ? 12.372  23.394  -16.686 1.00 7.71  ? 161 HIS A N   1 
ATOM   1305  C  CA  . HIS A  1 161 ? 12.416  24.494  -15.660 1.00 7.71  ? 161 HIS A CA  1 
ATOM   1306  C  C   . HIS A  1 161 ? 12.780  24.075  -14.277 1.00 7.36  ? 161 HIS A C   1 
ATOM   1307  O  O   . HIS A  1 161 ? 12.945  24.908  -13.332 1.00 8.93  ? 161 HIS A O   1 
ATOM   1308  C  CB  . HIS A  1 161 ? 11.051  25.185  -15.599 1.00 8.83  ? 161 HIS A CB  1 
ATOM   1309  C  CG  . HIS A  1 161 ? 10.661  25.869  -16.886 1.00 9.65  ? 161 HIS A CG  1 
ATOM   1310  N  ND1 . HIS A  1 161 ? 11.065  27.179  -17.191 1.00 11.30 ? 161 HIS A ND1 1 
ATOM   1311  C  CD2 . HIS A  1 161 ? 9.987   25.406  -17.966 1.00 11.73 ? 161 HIS A CD2 1 
ATOM   1312  C  CE1 . HIS A  1 161 ? 10.599  27.472  -18.408 1.00 11.15 ? 161 HIS A CE1 1 
ATOM   1313  N  NE2 . HIS A  1 161 ? 9.979   26.409  -18.908 1.00 10.52 ? 161 HIS A NE2 1 
ATOM   1314  N  N   . LEU A  1 162 ? 12.946  22.739  -14.051 1.00 7.47  ? 162 LEU A N   1 
ATOM   1315  C  CA  . LEU A  1 162 ? 13.132  22.206  -12.688 1.00 9.19  ? 162 LEU A CA  1 
ATOM   1316  C  C   . LEU A  1 162 ? 14.324  22.773  -11.929 1.00 8.71  ? 162 LEU A C   1 
ATOM   1317  O  O   . LEU A  1 162 ? 14.148  23.076  -10.774 1.00 8.17  ? 162 LEU A O   1 
ATOM   1318  C  CB  . LEU A  1 162 ? 13.304  20.672  -12.665 1.00 8.44  ? 162 LEU A CB  1 
ATOM   1319  C  CG  . LEU A  1 162 ? 12.019  19.917  -13.107 1.00 8.47  ? 162 LEU A CG  1 
ATOM   1320  C  CD1 . LEU A  1 162 ? 12.458  18.429  -13.391 1.00 9.13  ? 162 LEU A CD1 1 
ATOM   1321  C  CD2 . LEU A  1 162 ? 11.030  19.973  -12.001 1.00 12.54 ? 162 LEU A CD2 1 
ATOM   1322  N  N   . GLN A  1 163 ? 15.479  22.942  -12.601 1.00 8.35  ? 163 GLN A N   1 
ATOM   1323  C  CA  . GLN A  1 163 ? 16.680  23.459  -11.905 1.00 8.33  ? 163 GLN A CA  1 
ATOM   1324  C  C   . GLN A  1 163 ? 16.511  24.933  -11.580 1.00 9.45  ? 163 GLN A C   1 
ATOM   1325  O  O   . GLN A  1 163 ? 17.410  25.479  -10.962 1.00 10.82 ? 163 GLN A O   1 
ATOM   1326  C  CB  . GLN A  1 163 ? 17.974  23.191  -12.662 1.00 8.74  ? 163 GLN A CB  1 
ATOM   1327  C  CG  . GLN A  1 163 ? 18.248  21.703  -12.957 1.00 10.24 ? 163 GLN A CG  1 
ATOM   1328  C  CD  . GLN A  1 163 ? 18.472  20.857  -11.712 1.00 12.06 ? 163 GLN A CD  1 
ATOM   1329  O  OE1 . GLN A  1 163 ? 18.652  21.369  -10.604 1.00 11.45 ? 163 GLN A OE1 1 
ATOM   1330  N  NE2 . GLN A  1 163 ? 18.613  19.542  -11.924 1.00 12.04 ? 163 GLN A NE2 1 
ATOM   1331  N  N   . HIS A  1 164 ? 15.366  25.567  -11.950 1.00 9.25  ? 164 HIS A N   1 
ATOM   1332  C  CA  . HIS A  1 164 ? 15.126  26.916  -11.585 1.00 10.83 ? 164 HIS A CA  1 
ATOM   1333  C  C   . HIS A  1 164 ? 13.964  27.123  -10.628 1.00 12.54 ? 164 HIS A C   1 
ATOM   1334  O  O   . HIS A  1 164 ? 13.616  28.284  -10.288 1.00 12.23 ? 164 HIS A O   1 
ATOM   1335  C  CB  . HIS A  1 164 ? 14.992  27.790  -12.880 1.00 10.13 ? 164 HIS A CB  1 
ATOM   1336  C  CG  . HIS A  1 164 ? 16.115  27.553  -13.887 1.00 9.02  ? 164 HIS A CG  1 
ATOM   1337  N  ND1 . HIS A  1 164 ? 17.439  27.803  -13.586 1.00 11.74 ? 164 HIS A ND1 1 
ATOM   1338  C  CD2 . HIS A  1 164 ? 16.113  26.969  -15.113 1.00 11.79 ? 164 HIS A CD2 1 
ATOM   1339  C  CE1 . HIS A  1 164 ? 18.207  27.406  -14.590 1.00 12.56 ? 164 HIS A CE1 1 
ATOM   1340  N  NE2 . HIS A  1 164 ? 17.435  26.923  -15.553 1.00 11.55 ? 164 HIS A NE2 1 
ATOM   1341  N  N   . VAL A  1 165 ? 13.381  25.993  -10.135 1.00 8.68  ? 165 VAL A N   1 
ATOM   1342  C  CA  . VAL A  1 165 ? 12.396  26.063  -9.029  1.00 10.14 ? 165 VAL A CA  1 
ATOM   1343  C  C   . VAL A  1 165 ? 12.789  25.035  -7.947  1.00 9.34  ? 165 VAL A C   1 
ATOM   1344  O  O   . VAL A  1 165 ? 11.942  24.314  -7.356  1.00 9.37  ? 165 VAL A O   1 
ATOM   1345  C  CB  . VAL A  1 165 ? 10.936  25.860  -9.505  1.00 8.89  ? 165 VAL A CB  1 
ATOM   1346  C  CG1 . VAL A  1 165 ? 10.565  27.077  -10.384 1.00 10.91 ? 165 VAL A CG1 1 
ATOM   1347  C  CG2 . VAL A  1 165 ? 10.759  24.516  -10.291 1.00 9.92  ? 165 VAL A CG2 1 
ATOM   1348  N  N   . LYS A  1 166 ? 14.085  24.971  -7.666  1.00 9.77  ? 166 LYS A N   1 
ATOM   1349  C  CA  . LYS A  1 166 ? 14.642  23.912  -6.798  1.00 9.26  ? 166 LYS A CA  1 
ATOM   1350  C  C   . LYS A  1 166 ? 14.082  23.936  -5.359  1.00 9.18  ? 166 LYS A C   1 
ATOM   1351  O  O   . LYS A  1 166 ? 14.018  22.886  -4.684  1.00 9.92  ? 166 LYS A O   1 
ATOM   1352  C  CB  . LYS A  1 166 ? 16.206  23.982  -6.788  1.00 9.68  ? 166 LYS A CB  1 
ATOM   1353  C  CG  . LYS A  1 166 ? 16.812  23.639  -8.130  1.00 10.95 ? 166 LYS A CG  1 
ATOM   1354  C  CD  . LYS A  1 166 ? 18.371  23.697  -8.167  1.00 11.28 ? 166 LYS A CD  1 
ATOM   1355  C  CE  . LYS A  1 166 ? 18.964  22.689  -7.249  1.00 11.63 ? 166 LYS A CE  1 
ATOM   1356  N  NZ  . LYS A  1 166 ? 18.661  21.288  -7.850  1.00 9.93  ? 166 LYS A NZ  1 
ATOM   1357  N  N   . TYR A  1 167 ? 13.667  25.157  -4.920  1.00 8.41  ? 167 TYR A N   1 
ATOM   1358  C  CA  . TYR A  1 167 ? 13.362  25.323  -3.456  1.00 7.86  ? 167 TYR A CA  1 
ATOM   1359  C  C   . TYR A  1 167 ? 11.937  25.854  -3.232  1.00 7.66  ? 167 TYR A C   1 
ATOM   1360  O  O   . TYR A  1 167 ? 11.380  26.468  -4.124  1.00 9.97  ? 167 TYR A O   1 
ATOM   1361  C  CB  . TYR A  1 167 ? 14.419  26.291  -2.772  1.00 11.19 ? 167 TYR A CB  1 
ATOM   1362  C  CG  . TYR A  1 167 ? 15.782  25.719  -2.822  1.00 12.78 ? 167 TYR A CG  1 
ATOM   1363  C  CD1 . TYR A  1 167 ? 16.717  26.158  -3.809  1.00 14.68 ? 167 TYR A CD1 1 
ATOM   1364  C  CD2 . TYR A  1 167 ? 16.178  24.760  -1.909  1.00 11.55 ? 167 TYR A CD2 1 
ATOM   1365  C  CE1 . TYR A  1 167 ? 17.984  25.631  -3.839  1.00 14.21 ? 167 TYR A CE1 1 
ATOM   1366  C  CE2 . TYR A  1 167 ? 17.463  24.192  -1.993  1.00 13.76 ? 167 TYR A CE2 1 
ATOM   1367  C  CZ  . TYR A  1 167 ? 18.315  24.589  -2.973  1.00 15.78 ? 167 TYR A CZ  1 
ATOM   1368  O  OH  . TYR A  1 167 ? 19.569  23.954  -2.916  1.00 17.97 ? 167 TYR A OH  1 
ATOM   1369  N  N   . LYS A  1 168 ? 11.383  25.500  -2.079  1.00 9.10  ? 168 LYS A N   1 
ATOM   1370  C  CA  . LYS A  1 168 ? 10.029  25.907  -1.764  1.00 9.94  ? 168 LYS A CA  1 
ATOM   1371  C  C   . LYS A  1 168 ? 9.775   27.411  -1.993  1.00 11.05 ? 168 LYS A C   1 
ATOM   1372  O  O   . LYS A  1 168 ? 10.640  28.240  -1.475  1.00 11.99 ? 168 LYS A O   1 
ATOM   1373  C  CB  . LYS A  1 168 ? 9.729   25.516  -0.259  1.00 11.83 ? 168 LYS A CB  1 
ATOM   1374  C  CG  . LYS A  1 168 ? 8.319   25.970  0.097   1.00 12.92 ? 168 LYS A CG  1 
ATOM   1375  C  CD  . LYS A  1 168 ? 7.968   25.456  1.530   1.00 12.61 ? 168 LYS A CD  1 
ATOM   1376  C  CE  . LYS A  1 168 ? 6.548   25.855  1.900   1.00 22.02 ? 168 LYS A CE  1 
ATOM   1377  N  NZ  . LYS A  1 168 ? 6.048   25.406  3.234   1.00 22.99 ? 168 LYS A NZ  1 
ATOM   1378  N  N   . GLY A  1 169 ? 8.654   27.776  -2.637  1.00 9.36  ? 169 GLY A N   1 
ATOM   1379  C  CA  . GLY A  1 169 ? 8.344   29.144  -2.845  1.00 11.49 ? 169 GLY A CA  1 
ATOM   1380  C  C   . GLY A  1 169 ? 8.899   29.708  -4.143  1.00 13.38 ? 169 GLY A C   1 
ATOM   1381  O  O   . GLY A  1 169 ? 8.385   30.759  -4.619  1.00 15.07 ? 169 GLY A O   1 
ATOM   1382  N  N   . GLN A  1 170 ? 9.835   28.992  -4.789  1.00 10.85 ? 170 GLN A N   1 
ATOM   1383  C  CA  . GLN A  1 170 ? 10.349  29.513  -6.073  1.00 10.56 ? 170 GLN A CA  1 
ATOM   1384  C  C   . GLN A  1 170 ? 9.363   29.340  -7.217  1.00 11.47 ? 170 GLN A C   1 
ATOM   1385  O  O   . GLN A  1 170 ? 8.562   28.344  -7.202  1.00 11.88 ? 170 GLN A O   1 
ATOM   1386  C  CB  . GLN A  1 170 ? 11.736  28.907  -6.341  1.00 10.44 ? 170 GLN A CB  1 
ATOM   1387  C  CG  . GLN A  1 170 ? 12.770  29.385  -5.271  1.00 10.53 ? 170 GLN A CG  1 
ATOM   1388  C  CD  . GLN A  1 170 ? 14.134  28.821  -5.558  1.00 12.35 ? 170 GLN A CD  1 
ATOM   1389  O  OE1 . GLN A  1 170 ? 14.329  27.795  -6.140  1.00 12.05 ? 170 GLN A OE1 1 
ATOM   1390  N  NE2 . GLN A  1 170 ? 15.195  29.650  -5.237  1.00 13.99 ? 170 GLN A NE2 1 
ATOM   1391  N  N   . GLU A  1 171 ? 9.418   30.136  -8.255  1.00 11.50 ? 171 GLU A N   1 
ATOM   1392  C  CA  . GLU A  1 171 ? 8.455   30.186  -9.347  1.00 11.18 ? 171 GLU A CA  1 
ATOM   1393  C  C   . GLU A  1 171 ? 9.159   30.382  -10.643 1.00 9.97  ? 171 GLU A C   1 
ATOM   1394  O  O   . GLU A  1 171 ? 10.201  31.104  -10.637 1.00 11.52 ? 171 GLU A O   1 
ATOM   1395  C  CB  . GLU A  1 171 ? 7.575   31.472  -9.215  1.00 15.05 ? 171 GLU A CB  1 
ATOM   1396  C  CG  . GLU A  1 171 ? 6.667   31.436  -8.046  1.00 17.99 ? 171 GLU A CG  1 
ATOM   1397  C  CD  . GLU A  1 171 ? 5.874   32.803  -7.823  1.00 16.33 ? 171 GLU A CD  1 
ATOM   1398  O  OE1 . GLU A  1 171 ? 5.072   32.745  -6.877  1.00 25.81 ? 171 GLU A OE1 1 
ATOM   1399  O  OE2 . GLU A  1 171 ? 6.167   33.780  -8.535  1.00 26.26 ? 171 GLU A OE2 1 
ATOM   1400  N  N   . ALA A  1 172 ? 8.640   29.857  -11.736 1.00 10.06 ? 172 ALA A N   1 
ATOM   1401  C  CA  . ALA A  1 172 ? 9.085   30.123  -13.076 1.00 8.73  ? 172 ALA A CA  1 
ATOM   1402  C  C   . ALA A  1 172 ? 7.872   30.388  -13.929 1.00 10.75 ? 172 ALA A C   1 
ATOM   1403  O  O   . ALA A  1 172 ? 6.714   30.144  -13.497 1.00 11.16 ? 172 ALA A O   1 
ATOM   1404  C  CB  . ALA A  1 172 ? 9.893   28.934  -13.565 1.00 9.61  ? 172 ALA A CB  1 
ATOM   1405  N  N   . PHE A  1 173 ? 8.092   30.828  -15.160 1.00 10.12 ? 173 PHE A N   1 
ATOM   1406  C  CA  . PHE A  1 173 ? 7.034   31.092  -16.059 1.00 11.54 ? 173 PHE A CA  1 
ATOM   1407  C  C   . PHE A  1 173 ? 7.229   30.213  -17.164 1.00 13.27 ? 173 PHE A C   1 
ATOM   1408  O  O   . PHE A  1 173 ? 8.366   30.139  -17.694 1.00 16.25 ? 173 PHE A O   1 
ATOM   1409  C  CB  . PHE A  1 173 ? 7.044   32.613  -16.467 1.00 13.01 ? 173 PHE A CB  1 
ATOM   1410  C  CG  . PHE A  1 173 ? 6.676   33.524  -15.301 1.00 14.99 ? 173 PHE A CG  1 
ATOM   1411  C  CD1 . PHE A  1 173 ? 7.678   33.905  -14.385 1.00 16.99 ? 173 PHE A CD1 1 
ATOM   1412  C  CD2 . PHE A  1 173 ? 5.340   33.841  -15.022 1.00 24.18 ? 173 PHE A CD2 1 
ATOM   1413  C  CE1 . PHE A  1 173 ? 7.355   34.632  -13.207 1.00 20.16 ? 173 PHE A CE1 1 
ATOM   1414  C  CE2 . PHE A  1 173 ? 5.038   34.656  -13.876 1.00 22.75 ? 173 PHE A CE2 1 
ATOM   1415  C  CZ  . PHE A  1 173 ? 6.068   35.007  -12.975 1.00 20.23 ? 173 PHE A CZ  1 
ATOM   1416  N  N   . VAL A  1 174 ? 6.171   29.494  -17.562 1.00 9.07  ? 174 VAL A N   1 
ATOM   1417  C  CA  . VAL A  1 174 ? 6.151   28.571  -18.670 1.00 8.52  ? 174 VAL A CA  1 
ATOM   1418  C  C   . VAL A  1 174 ? 5.245   29.050  -19.826 1.00 10.73 ? 174 VAL A C   1 
ATOM   1419  O  O   . VAL A  1 174 ? 4.076   29.246  -19.598 1.00 10.02 ? 174 VAL A O   1 
ATOM   1420  C  CB  . VAL A  1 174 ? 5.589   27.202  -18.108 1.00 9.21  ? 174 VAL A CB  1 
ATOM   1421  C  CG1 . VAL A  1 174 ? 5.501   26.156  -19.170 1.00 12.63 ? 174 VAL A CG1 1 
ATOM   1422  C  CG2 . VAL A  1 174 ? 6.467   26.753  -16.947 1.00 10.52 ? 174 VAL A CG2 1 
ATOM   1423  N  N   . PRO A  1 175 ? 5.796   29.300  -21.049 1.00 8.46  ? 175 PRO A N   1 
ATOM   1424  C  CA  . PRO A  1 175 ? 4.924   29.650  -22.165 1.00 10.25 ? 175 PRO A CA  1 
ATOM   1425  C  C   . PRO A  1 175 ? 3.865   28.595  -22.421 1.00 10.58 ? 175 PRO A C   1 
ATOM   1426  O  O   . PRO A  1 175 ? 4.119   27.378  -22.223 1.00 8.90  ? 175 PRO A O   1 
ATOM   1427  C  CB  . PRO A  1 175 ? 5.920   29.731  -23.357 1.00 9.70  ? 175 PRO A CB  1 
ATOM   1428  C  CG  . PRO A  1 175 ? 7.235   30.018  -22.696 1.00 11.19 ? 175 PRO A CG  1 
ATOM   1429  C  CD  . PRO A  1 175 ? 7.249   29.266  -21.396 1.00 11.42 ? 175 PRO A CD  1 
ATOM   1430  N  N   . GLY A  1 176 ? 2.684   28.987  -22.854 1.00 8.49  ? 176 GLY A N   1 
ATOM   1431  C  CA  . GLY A  1 176 ? 1.704   27.997  -22.999 1.00 10.30 ? 176 GLY A CA  1 
ATOM   1432  C  C   . GLY A  1 176 ? 2.094   26.959  -24.055 1.00 10.28 ? 176 GLY A C   1 
ATOM   1433  O  O   . GLY A  1 176 ? 2.800   27.248  -25.044 1.00 9.61  ? 176 GLY A O   1 
ATOM   1434  N  N   . PHE A  1 177 ? 1.618   25.715  -23.883 1.00 9.52  ? 177 PHE A N   1 
ATOM   1435  C  CA  . PHE A  1 177 ? 1.827   24.650  -24.845 1.00 8.83  ? 177 PHE A CA  1 
ATOM   1436  C  C   . PHE A  1 177 ? 0.634   23.745  -24.736 1.00 9.71  ? 177 PHE A C   1 
ATOM   1437  O  O   . PHE A  1 177 ? -0.264  24.001  -23.919 1.00 9.66  ? 177 PHE A O   1 
ATOM   1438  C  CB  . PHE A  1 177 ? 3.132   23.865  -24.510 1.00 9.72  ? 177 PHE A CB  1 
ATOM   1439  C  CG  . PHE A  1 177 ? 3.089   23.091  -23.188 1.00 9.64  ? 177 PHE A CG  1 
ATOM   1440  C  CD1 . PHE A  1 177 ? 2.789   21.680  -23.158 1.00 10.19 ? 177 PHE A CD1 1 
ATOM   1441  C  CD2 . PHE A  1 177 ? 3.412   23.742  -22.028 1.00 9.34  ? 177 PHE A CD2 1 
ATOM   1442  C  CE1 . PHE A  1 177 ? 2.783   21.058  -21.943 1.00 9.82  ? 177 PHE A CE1 1 
ATOM   1443  C  CE2 . PHE A  1 177 ? 3.391   23.132  -20.755 1.00 9.29  ? 177 PHE A CE2 1 
ATOM   1444  C  CZ  . PHE A  1 177 ? 3.125   21.742  -20.761 1.00 8.81  ? 177 PHE A CZ  1 
ATOM   1445  N  N   . ASN A  1 178 ? 0.526   22.768  -25.618 1.00 10.60 ? 178 ASN A N   1 
ATOM   1446  C  CA  . ASN A  1 178 ? -0.680  21.940  -25.682 1.00 10.76 ? 178 ASN A CA  1 
ATOM   1447  C  C   . ASN A  1 178 ? -0.674  20.847  -24.559 1.00 10.37 ? 178 ASN A C   1 
ATOM   1448  O  O   . ASN A  1 178 ? 0.007   19.822  -24.660 1.00 9.66  ? 178 ASN A O   1 
ATOM   1449  C  CB  . ASN A  1 178 ? -0.809  21.305  -27.078 1.00 11.86 ? 178 ASN A CB  1 
ATOM   1450  C  CG  . ASN A  1 178 ? -2.121  20.623  -27.256 1.00 12.71 ? 178 ASN A CG  1 
ATOM   1451  O  OD1 . ASN A  1 178 ? -2.981  20.620  -26.377 1.00 11.79 ? 178 ASN A OD1 1 
ATOM   1452  N  ND2 . ASN A  1 178 ? -2.326  20.028  -28.470 1.00 16.81 ? 178 ASN A ND2 1 
ATOM   1453  N  N   . ILE A  1 179 ? -1.451  21.081  -23.538 1.00 8.37  ? 179 ILE A N   1 
ATOM   1454  C  CA  . ILE A  1 179 ? -1.535  20.179  -22.365 1.00 8.70  ? 179 ILE A CA  1 
ATOM   1455  C  C   . ILE A  1 179 ? -2.080  18.793  -22.855 1.00 9.62  ? 179 ILE A C   1 
ATOM   1456  O  O   . ILE A  1 179 ? -1.747  17.777  -22.240 1.00 8.01  ? 179 ILE A O   1 
ATOM   1457  C  CB  . ILE A  1 179 ? -2.440  20.811  -21.269 1.00 8.57  ? 179 ILE A CB  1 
ATOM   1458  C  CG1 . ILE A  1 179 ? -1.874  22.153  -20.830 1.00 8.91  ? 179 ILE A CG1 1 
ATOM   1459  C  CG2 . ILE A  1 179 ? -2.546  19.787  -20.033 1.00 8.56  ? 179 ILE A CG2 1 
ATOM   1460  C  CD1 . ILE A  1 179 ? -0.452  22.087  -20.314 1.00 7.86  ? 179 ILE A CD1 1 
ATOM   1461  N  N   . GLU A  1 180 ? -2.845  18.724  -23.982 1.00 8.58  ? 180 GLU A N   1 
ATOM   1462  C  CA  . GLU A  1 180 ? -3.260  17.423  -24.461 1.00 10.57 ? 180 GLU A CA  1 
ATOM   1463  C  C   . GLU A  1 180 ? -2.083  16.519  -24.830 1.00 8.90  ? 180 GLU A C   1 
ATOM   1464  O  O   . GLU A  1 180 ? -2.241  15.264  -24.869 1.00 9.78  ? 180 GLU A O   1 
ATOM   1465  C  CB  . GLU A  1 180 ? -4.304  17.592  -25.599 1.00 12.43 ? 180 GLU A CB  1 
ATOM   1466  C  CG  . GLU A  1 180 ? -4.916  16.298  -26.108 1.00 15.90 ? 180 GLU A CG  1 
ATOM   1467  C  CD  . GLU A  1 180 ? -6.198  16.542  -26.965 1.00 23.01 ? 180 GLU A CD  1 
ATOM   1468  O  OE1 . GLU A  1 180 ? -6.837  15.520  -27.398 1.00 33.78 ? 180 GLU A OE1 1 
ATOM   1469  O  OE2 . GLU A  1 180 ? -6.532  17.765  -27.140 1.00 27.55 ? 180 GLU A OE2 1 
ATOM   1470  N  N   . GLU A  1 181 ? -0.935  17.138  -25.128 1.00 8.57  ? 181 GLU A N   1 
ATOM   1471  C  CA  . GLU A  1 181 ? 0.238   16.273  -25.475 1.00 9.09  ? 181 GLU A CA  1 
ATOM   1472  C  C   . GLU A  1 181 ? 0.835   15.576  -24.254 1.00 9.17  ? 181 GLU A C   1 
ATOM   1473  O  O   . GLU A  1 181 ? 1.717   14.729  -24.448 1.00 9.66  ? 181 GLU A O   1 
ATOM   1474  C  CB  . GLU A  1 181 ? 1.309   17.075  -26.113 1.00 12.17 ? 181 GLU A CB  1 
ATOM   1475  C  CG  . GLU A  1 181 ? 1.020   17.861  -27.437 1.00 21.01 ? 181 GLU A CG  1 
ATOM   1476  C  CD  . GLU A  1 181 ? 2.062   19.032  -27.687 1.00 22.14 ? 181 GLU A CD  1 
ATOM   1477  O  OE1 . GLU A  1 181 ? 3.064   19.292  -26.887 1.00 29.92 ? 181 GLU A OE1 1 
ATOM   1478  O  OE2 . GLU A  1 181 ? 1.843   19.779  -28.692 1.00 27.90 ? 181 GLU A OE2 1 
ATOM   1479  N  N   . LEU A  1 182 ? 0.370   15.924  -23.032 1.00 6.95  ? 182 LEU A N   1 
ATOM   1480  C  CA  . LEU A  1 182 ? 0.778   15.173  -21.844 1.00 7.31  ? 182 LEU A CA  1 
ATOM   1481  C  C   . LEU A  1 182 ? -0.039  13.903  -21.626 1.00 8.11  ? 182 LEU A C   1 
ATOM   1482  O  O   . LEU A  1 182 ? 0.317   13.078  -20.788 1.00 7.73  ? 182 LEU A O   1 
ATOM   1483  C  CB  . LEU A  1 182 ? 0.653   16.072  -20.597 1.00 7.41  ? 182 LEU A CB  1 
ATOM   1484  C  CG  . LEU A  1 182 ? 1.397   17.408  -20.652 1.00 7.81  ? 182 LEU A CG  1 
ATOM   1485  C  CD1 . LEU A  1 182 ? 1.199   18.195  -19.341 1.00 7.56  ? 182 LEU A CD1 1 
ATOM   1486  C  CD2 . LEU A  1 182 ? 2.931   17.174  -20.833 1.00 8.59  ? 182 LEU A CD2 1 
ATOM   1487  N  N   . LEU A  1 183 ? -1.132  13.790  -22.372 1.00 7.81  ? 183 LEU A N   1 
ATOM   1488  C  CA  . LEU A  1 183 ? -2.028  12.621  -22.238 1.00 9.27  ? 183 LEU A CA  1 
ATOM   1489  C  C   . LEU A  1 183 ? -1.524  11.450  -23.061 1.00 8.13  ? 183 LEU A C   1 
ATOM   1490  O  O   . LEU A  1 183 ? -0.834  11.638  -24.087 1.00 9.37  ? 183 LEU A O   1 
ATOM   1491  C  CB  . LEU A  1 183 ? -3.417  13.054  -22.771 1.00 8.71  ? 183 LEU A CB  1 
ATOM   1492  C  CG  . LEU A  1 183 ? -4.012  14.237  -21.971 1.00 9.57  ? 183 LEU A CG  1 
ATOM   1493  C  CD1 . LEU A  1 183 ? -5.461  14.533  -22.404 1.00 10.49 ? 183 LEU A CD1 1 
ATOM   1494  C  CD2 . LEU A  1 183 ? -3.963  14.027  -20.472 1.00 10.51 ? 183 LEU A CD2 1 
ATOM   1495  N  N   . PRO A  1 184 ? -1.899  10.248  -22.657 1.00 6.61  ? 184 PRO A N   1 
ATOM   1496  C  CA  . PRO A  1 184 ? -1.365  9.038   -23.304 1.00 7.28  ? 184 PRO A CA  1 
ATOM   1497  C  C   . PRO A  1 184 ? -2.186  8.667   -24.587 1.00 8.85  ? 184 PRO A C   1 
ATOM   1498  O  O   . PRO A  1 184 ? -3.164  9.412   -24.930 1.00 9.43  ? 184 PRO A O   1 
ATOM   1499  C  CB  . PRO A  1 184 ? -1.572  7.936   -22.219 1.00 7.28  ? 184 PRO A CB  1 
ATOM   1500  C  CG  . PRO A  1 184 ? -2.812  8.400   -21.516 1.00 8.25  ? 184 PRO A CG  1 
ATOM   1501  C  CD  . PRO A  1 184 ? -2.708  9.902   -21.469 1.00 8.63  ? 184 PRO A CD  1 
ATOM   1502  N  N   . GLU A  1 185 ? -1.755  7.591   -25.237 1.00 10.37 ? 185 GLU A N   1 
ATOM   1503  C  CA  . GLU A  1 185 ? -2.573  7.088   -26.336 1.00 11.66 ? 185 GLU A CA  1 
ATOM   1504  C  C   . GLU A  1 185 ? -3.970  6.547   -25.853 1.00 10.03 ? 185 GLU A C   1 
ATOM   1505  O  O   . GLU A  1 185 ? -4.095  6.091   -24.704 1.00 8.98  ? 185 GLU A O   1 
ATOM   1506  C  CB  . GLU A  1 185 ? -1.858  5.965   -27.071 1.00 13.25 ? 185 GLU A CB  1 
ATOM   1507  C  CG  . GLU A  1 185 ? -0.560  6.349   -27.663 1.00 14.99 ? 185 GLU A CG  1 
ATOM   1508  C  CD  . GLU A  1 185 ? 0.159   5.200   -28.362 1.00 25.78 ? 185 GLU A CD  1 
ATOM   1509  O  OE1 . GLU A  1 185 ? -0.289  4.008   -28.434 1.00 31.29 ? 185 GLU A OE1 1 
ATOM   1510  O  OE2 . GLU A  1 185 ? 1.299   5.479   -28.775 1.00 32.49 ? 185 GLU A OE2 1 
ATOM   1511  N  N   . ARG A  1 186 ? -4.990  6.686   -26.731 1.00 9.37  ? 186 ARG A N   1 
ATOM   1512  C  CA  . ARG A  1 186 ? -6.300  6.123   -26.491 1.00 8.76  ? 186 ARG A CA  1 
ATOM   1513  C  C   . ARG A  1 186 ? -6.891  6.667   -25.162 1.00 8.11  ? 186 ARG A C   1 
ATOM   1514  O  O   . ARG A  1 186 ? -7.301  5.914   -24.259 1.00 9.55  ? 186 ARG A O   1 
ATOM   1515  C  CB  . ARG A  1 186 ? -6.295  4.578   -26.570 1.00 11.08 ? 186 ARG A CB  1 
ATOM   1516  C  CG  . ARG A  1 186 ? -5.890  4.236   -27.997 1.00 13.20 ? 186 ARG A CG  1 
ATOM   1517  C  CD  . ARG A  1 186 ? -5.906  2.695   -28.229 1.00 17.12 ? 186 ARG A CD  1 
ATOM   1518  N  NE  . ARG A  1 186 ? -4.700  2.142   -27.548 1.00 25.05 ? 186 ARG A NE  1 
ATOM   1519  C  CZ  . ARG A  1 186 ? -3.410  2.289   -27.994 1.00 29.88 ? 186 ARG A CZ  1 
ATOM   1520  N  NH1 . ARG A  1 186 ? -2.352  1.848   -27.291 1.00 34.04 ? 186 ARG A NH1 1 
ATOM   1521  N  NH2 . ARG A  1 186 ? -3.162  2.924   -29.133 1.00 32.47 ? 186 ARG A NH2 1 
ATOM   1522  N  N   . THR A  1 187 ? -7.049  7.983   -25.129 1.00 7.97  ? 187 THR A N   1 
ATOM   1523  C  CA  . THR A  1 187 ? -7.621  8.598   -23.926 1.00 7.60  ? 187 THR A CA  1 
ATOM   1524  C  C   . THR A  1 187 ? -9.109  8.171   -23.688 1.00 7.43  ? 187 THR A C   1 
ATOM   1525  O  O   . THR A  1 187 ? -9.642  8.361   -22.563 1.00 8.81  ? 187 THR A O   1 
ATOM   1526  C  CB  . THR A  1 187 ? -7.574  10.114  -23.865 1.00 8.60  ? 187 THR A CB  1 
ATOM   1527  O  OG1 . THR A  1 187 ? -8.048  10.603  -25.132 1.00 10.76 ? 187 THR A OG1 1 
ATOM   1528  C  CG2 . THR A  1 187 ? -6.089  10.580  -23.557 1.00 11.42 ? 187 THR A CG2 1 
ATOM   1529  N  N   . ALA A  1 188 ? -9.762  7.561   -24.709 1.00 8.11  ? 188 ALA A N   1 
ATOM   1530  C  CA  . ALA A  1 188 ? -11.091 7.064   -24.441 1.00 6.79  ? 188 ALA A CA  1 
ATOM   1531  C  C   . ALA A  1 188 ? -11.131 5.882   -23.504 1.00 7.48  ? 188 ALA A C   1 
ATOM   1532  O  O   . ALA A  1 188 ? -12.188 5.553   -23.033 1.00 7.02  ? 188 ALA A O   1 
ATOM   1533  C  CB  . ALA A  1 188 ? -11.764 6.627   -25.782 1.00 8.99  ? 188 ALA A CB  1 
ATOM   1534  N  N   . GLU A  1 189 ? -9.977  5.292   -23.300 1.00 7.25  ? 189 GLU A N   1 
ATOM   1535  C  CA  . GLU A  1 189 ? -9.826  4.107   -22.401 1.00 7.68  ? 189 GLU A CA  1 
ATOM   1536  C  C   . GLU A  1 189 ? -9.286  4.601   -21.039 1.00 6.07  ? 189 GLU A C   1 
ATOM   1537  O  O   . GLU A  1 189 ? -8.124  5.086   -20.893 1.00 7.19  ? 189 GLU A O   1 
ATOM   1538  C  CB  . GLU A  1 189 ? -8.816  3.176   -22.973 1.00 7.50  ? 189 GLU A CB  1 
ATOM   1539  C  CG  . GLU A  1 189 ? -9.373  2.669   -24.343 1.00 10.61 ? 189 GLU A CG  1 
ATOM   1540  C  CD  . GLU A  1 189 ? -8.505  1.581   -24.966 1.00 11.87 ? 189 GLU A CD  1 
ATOM   1541  O  OE1 . GLU A  1 189 ? -7.613  0.985   -24.374 1.00 11.15 ? 189 GLU A OE1 1 
ATOM   1542  O  OE2 . GLU A  1 189 ? -8.769  1.270   -26.212 1.00 14.53 ? 189 GLU A OE2 1 
ATOM   1543  N  N   . TYR A  1 190 ? -10.142 4.392   -20.005 1.00 6.41  ? 190 TYR A N   1 
ATOM   1544  C  CA  . TYR A  1 190 ? -9.775  4.868   -18.656 1.00 5.88  ? 190 TYR A CA  1 
ATOM   1545  C  C   . TYR A  1 190 ? -10.516 4.109   -17.573 1.00 6.52  ? 190 TYR A C   1 
ATOM   1546  O  O   . TYR A  1 190 ? -11.492 3.405   -17.808 1.00 6.50  ? 190 TYR A O   1 
ATOM   1547  C  CB  . TYR A  1 190 ? -10.073 6.381   -18.543 1.00 5.38  ? 190 TYR A CB  1 
ATOM   1548  C  CG  . TYR A  1 190 ? -11.520 6.790   -18.855 1.00 4.20  ? 190 TYR A CG  1 
ATOM   1549  C  CD1 . TYR A  1 190 ? -12.563 6.643   -17.880 1.00 5.83  ? 190 TYR A CD1 1 
ATOM   1550  C  CD2 . TYR A  1 190 ? -11.882 7.375   -20.119 1.00 6.61  ? 190 TYR A CD2 1 
ATOM   1551  C  CE1 . TYR A  1 190 ? -13.892 7.034   -18.184 1.00 5.61  ? 190 TYR A CE1 1 
ATOM   1552  C  CE2 . TYR A  1 190 ? -13.211 7.734   -20.395 1.00 7.78  ? 190 TYR A CE2 1 
ATOM   1553  C  CZ  . TYR A  1 190 ? -14.183 7.561   -19.418 1.00 5.98  ? 190 TYR A CZ  1 
ATOM   1554  O  OH  . TYR A  1 190 ? -15.509 7.923   -19.735 1.00 6.93  ? 190 TYR A OH  1 
ATOM   1555  N  N   . TYR A  1 191 ? -10.040 4.279   -16.339 1.00 6.34  ? 191 TYR A N   1 
ATOM   1556  C  CA  . TYR A  1 191 ? -10.682 3.807   -15.114 1.00 5.53  ? 191 TYR A CA  1 
ATOM   1557  C  C   . TYR A  1 191 ? -11.353 4.929   -14.477 1.00 5.16  ? 191 TYR A C   1 
ATOM   1558  O  O   . TYR A  1 191 ? -10.801 6.084   -14.480 1.00 5.89  ? 191 TYR A O   1 
ATOM   1559  C  CB  . TYR A  1 191 ? -9.570  3.352   -14.110 1.00 6.59  ? 191 TYR A CB  1 
ATOM   1560  C  CG  . TYR A  1 191 ? -8.607  2.274   -14.583 1.00 5.54  ? 191 TYR A CG  1 
ATOM   1561  C  CD1 . TYR A  1 191 ? -7.366  2.569   -15.214 1.00 7.69  ? 191 TYR A CD1 1 
ATOM   1562  C  CD2 . TYR A  1 191 ? -8.923  0.908   -14.409 1.00 6.81  ? 191 TYR A CD2 1 
ATOM   1563  C  CE1 . TYR A  1 191 ? -6.472  1.606   -15.609 1.00 6.88  ? 191 TYR A CE1 1 
ATOM   1564  C  CE2 . TYR A  1 191 ? -8.007  -0.039  -14.753 1.00 6.36  ? 191 TYR A CE2 1 
ATOM   1565  C  CZ  . TYR A  1 191 ? -6.852  0.247   -15.407 1.00 5.62  ? 191 TYR A CZ  1 
ATOM   1566  O  OH  . TYR A  1 191 ? -5.912  -0.636  -15.807 1.00 8.78  ? 191 TYR A OH  1 
ATOM   1567  N  N   . ARG A  1 192 ? -12.534 4.762   -13.911 1.00 6.37  ? 192 ARG A N   1 
ATOM   1568  C  CA  . ARG A  1 192 ? -13.338 5.843   -13.358 1.00 6.35  ? 192 ARG A CA  1 
ATOM   1569  C  C   . ARG A  1 192 ? -13.836 5.406   -11.977 1.00 6.12  ? 192 ARG A C   1 
ATOM   1570  O  O   . ARG A  1 192 ? -14.485 4.301   -11.817 1.00 7.06  ? 192 ARG A O   1 
ATOM   1571  C  CB  . ARG A  1 192 ? -14.586 6.076   -14.274 1.00 6.04  ? 192 ARG A CB  1 
ATOM   1572  C  CG  . ARG A  1 192 ? -15.652 6.924   -13.631 1.00 7.41  ? 192 ARG A CG  1 
ATOM   1573  C  CD  . ARG A  1 192 ? -15.314 8.404   -13.289 1.00 6.96  ? 192 ARG A CD  1 
ATOM   1574  N  NE  . ARG A  1 192 ? -14.650 9.110   -14.436 1.00 8.53  ? 192 ARG A NE  1 
ATOM   1575  C  CZ  . ARG A  1 192 ? -15.279 9.541   -15.552 1.00 8.62  ? 192 ARG A CZ  1 
ATOM   1576  N  NH1 . ARG A  1 192 ? -14.577 10.132  -16.559 1.00 9.01  ? 192 ARG A NH1 1 
ATOM   1577  N  NH2 . ARG A  1 192 ? -16.605 9.341   -15.698 1.00 7.91  ? 192 ARG A NH2 1 
ATOM   1578  N  N   . TYR A  1 193 ? -13.614 6.213   -10.932 1.00 5.28  ? 193 TYR A N   1 
ATOM   1579  C  CA  . TYR A  1 193 ? -14.223 5.911   -9.622  1.00 5.38  ? 193 TYR A CA  1 
ATOM   1580  C  C   . TYR A  1 193 ? -14.325 7.125   -8.747  1.00 5.25  ? 193 TYR A C   1 
ATOM   1581  O  O   . TYR A  1 193 ? -13.692 8.135   -9.028  1.00 6.88  ? 193 TYR A O   1 
ATOM   1582  C  CB  . TYR A  1 193 ? -13.380 4.771   -8.938  1.00 5.63  ? 193 TYR A CB  1 
ATOM   1583  C  CG  . TYR A  1 193 ? -12.017 5.272   -8.308  1.00 4.22  ? 193 TYR A CG  1 
ATOM   1584  C  CD1 . TYR A  1 193 ? -11.940 5.531   -6.930  1.00 4.64  ? 193 TYR A CD1 1 
ATOM   1585  C  CD2 . TYR A  1 193 ? -10.880 5.439   -9.094  1.00 5.42  ? 193 TYR A CD2 1 
ATOM   1586  C  CE1 . TYR A  1 193 ? -10.727 5.984   -6.364  1.00 5.21  ? 193 TYR A CE1 1 
ATOM   1587  C  CE2 . TYR A  1 193 ? -9.681  5.938   -8.576  1.00 4.14  ? 193 TYR A CE2 1 
ATOM   1588  C  CZ  . TYR A  1 193 ? -9.628  6.182   -7.223  1.00 4.35  ? 193 TYR A CZ  1 
ATOM   1589  O  OH  . TYR A  1 193 ? -8.450  6.635   -6.610  1.00 5.57  ? 193 TYR A OH  1 
ATOM   1590  N  N   . ARG A  1 194 ? -15.110 7.024   -7.696  1.00 6.47  ? 194 ARG A N   1 
ATOM   1591  C  CA  . ARG A  1 194 ? -15.298 8.119   -6.752  1.00 6.58  ? 194 ARG A CA  1 
ATOM   1592  C  C   . ARG A  1 194 ? -14.299 7.935   -5.637  1.00 7.53  ? 194 ARG A C   1 
ATOM   1593  O  O   . ARG A  1 194 ? -14.241 6.899   -4.978  1.00 6.90  ? 194 ARG A O   1 
ATOM   1594  C  CB  . ARG A  1 194 ? -16.711 8.077   -6.109  1.00 8.12  ? 194 ARG A CB  1 
ATOM   1595  C  CG  . ARG A  1 194 ? -17.739 8.457   -7.182  1.00 12.07 ? 194 ARG A CG  1 
ATOM   1596  C  CD  . ARG A  1 194 ? -19.244 8.416   -6.690  1.00 16.44 ? 194 ARG A CD  1 
ATOM   1597  N  NE  . ARG A  1 194 ? -19.395 7.768   -5.386  1.00 32.56 ? 194 ARG A NE  1 
ATOM   1598  C  CZ  . ARG A  1 194 ? -19.534 8.415   -4.231  1.00 33.51 ? 194 ARG A CZ  1 
ATOM   1599  N  NH1 . ARG A  1 194 ? -19.538 9.741   -4.201  1.00 37.66 ? 194 ARG A NH1 1 
ATOM   1600  N  NH2 . ARG A  1 194 ? -19.668 7.733   -3.101  1.00 26.88 ? 194 ARG A NH2 1 
ATOM   1601  N  N   . GLY A  1 195 ? -13.461 8.975   -5.399  1.00 5.25  ? 195 GLY A N   1 
ATOM   1602  C  CA  . GLY A  1 195 ? -12.451 8.892   -4.346  1.00 5.92  ? 195 GLY A CA  1 
ATOM   1603  C  C   . GLY A  1 195 ? -12.184 10.237  -3.754  1.00 5.26  ? 195 GLY A C   1 
ATOM   1604  O  O   . GLY A  1 195 ? -13.093 11.054  -3.583  1.00 6.01  ? 195 GLY A O   1 
ATOM   1605  N  N   . SER A  1 196 ? -10.899 10.467  -3.414  1.00 5.16  ? 196 SER A N   1 
ATOM   1606  C  CA  . SER A  1 196 ? -10.549 11.603  -2.539  1.00 4.73  ? 196 SER A CA  1 
ATOM   1607  C  C   . SER A  1 196 ? -9.324  12.283  -3.092  1.00 6.01  ? 196 SER A C   1 
ATOM   1608  O  O   . SER A  1 196 ? -8.581  11.762  -3.984  1.00 6.44  ? 196 SER A O   1 
ATOM   1609  C  CB  . SER A  1 196 ? -10.223 11.098  -1.153  1.00 5.32  ? 196 SER A CB  1 
ATOM   1610  O  OG  . SER A  1 196 ? -8.921  10.529  -1.028  1.00 5.24  ? 196 SER A OG  1 
ATOM   1611  N  N   A LEU A  1 197 ? -9.023  13.468  -2.555  0.50 5.74  ? 197 LEU A N   1 
ATOM   1612  N  N   B LEU A  1 197 ? -9.022  13.486  -2.589  0.50 5.61  ? 197 LEU A N   1 
ATOM   1613  C  CA  A LEU A  1 197 ? -7.693  14.046  -2.732  0.50 5.83  ? 197 LEU A CA  1 
ATOM   1614  C  CA  B LEU A  1 197 ? -7.663  13.990  -2.754  0.50 5.60  ? 197 LEU A CA  1 
ATOM   1615  C  C   A LEU A  1 197 ? -6.640  13.095  -2.084  0.50 5.58  ? 197 LEU A C   1 
ATOM   1616  C  C   B LEU A  1 197 ? -6.679  12.965  -2.153  0.50 5.19  ? 197 LEU A C   1 
ATOM   1617  O  O   A LEU A  1 197 ? -6.881  12.556  -0.963  0.50 5.60  ? 197 LEU A O   1 
ATOM   1618  O  O   B LEU A  1 197 ? -6.984  12.269  -1.126  0.50 4.80  ? 197 LEU A O   1 
ATOM   1619  C  CB  A LEU A  1 197 ? -7.640  15.416  -2.011  0.50 6.82  ? 197 LEU A CB  1 
ATOM   1620  C  CB  B LEU A  1 197 ? -7.467  15.301  -1.965  0.50 6.95  ? 197 LEU A CB  1 
ATOM   1621  C  CG  A LEU A  1 197 ? -8.537  16.517  -2.638  0.50 6.46  ? 197 LEU A CG  1 
ATOM   1622  C  CG  B LEU A  1 197 ? -7.548  16.606  -2.762  0.50 7.25  ? 197 LEU A CG  1 
ATOM   1623  C  CD1 A LEU A  1 197 ? -8.748  17.718  -1.678  0.50 9.73  ? 197 LEU A CD1 1 
ATOM   1624  C  CD1 B LEU A  1 197 ? -8.897  16.916  -3.098  0.50 12.26 ? 197 LEU A CD1 1 
ATOM   1625  C  CD2 A LEU A  1 197 ? -8.184  16.905  -4.041  0.50 6.50  ? 197 LEU A CD2 1 
ATOM   1626  C  CD2 B LEU A  1 197 ? -7.043  17.704  -1.906  0.50 11.82 ? 197 LEU A CD2 1 
ATOM   1627  N  N   . THR A  1 198 ? -5.507  12.888  -2.757  1.00 5.00  ? 198 THR A N   1 
ATOM   1628  C  CA  . THR A  1 198 ? -4.508  11.977  -2.199  1.00 4.25  ? 198 THR A CA  1 
ATOM   1629  C  C   . THR A  1 198 ? -3.489  12.627  -1.268  1.00 5.97  ? 198 THR A C   1 
ATOM   1630  O  O   . THR A  1 198 ? -2.530  12.009  -0.800  1.00 5.41  ? 198 THR A O   1 
ATOM   1631  C  CB  . THR A  1 198 ? -3.667  11.364  -3.332  1.00 5.08  ? 198 THR A CB  1 
ATOM   1632  O  OG1 . THR A  1 198 ? -2.966  12.430  -3.984  1.00 4.95  ? 198 THR A OG1 1 
ATOM   1633  C  CG2 . THR A  1 198 ? -4.503  10.633  -4.386  1.00 4.65  ? 198 THR A CG2 1 
ATOM   1634  N  N   A THR A  1 199 ? -3.689  13.962  -1.134  0.50 4.95  ? 199 THR A N   1 
ATOM   1635  N  N   B THR A  1 199 ? -3.793  13.879  -0.955  0.50 6.75  ? 199 THR A N   1 
ATOM   1636  C  CA  A THR A  1 199 ? -2.974  14.774  -0.134  0.50 5.34  ? 199 THR A CA  1 
ATOM   1637  C  CA  B THR A  1 199 ? -2.954  14.658  -0.110  0.50 7.10  ? 199 THR A CA  1 
ATOM   1638  C  C   A THR A  1 199 ? -3.956  15.298  0.920   0.50 5.98  ? 199 THR A C   1 
ATOM   1639  C  C   B THR A  1 199 ? -3.907  15.408  0.832   0.50 7.01  ? 199 THR A C   1 
ATOM   1640  O  O   A THR A  1 199 ? -5.163  15.298  0.720   0.50 5.78  ? 199 THR A O   1 
ATOM   1641  O  O   B THR A  1 199 ? -5.043  15.764  0.390   0.50 5.74  ? 199 THR A O   1 
ATOM   1642  C  CB  A THR A  1 199 ? -2.260  16.028  -0.835  0.50 7.56  ? 199 THR A CB  1 
ATOM   1643  C  CB  B THR A  1 199 ? -2.339  15.685  -1.092  0.50 12.03 ? 199 THR A CB  1 
ATOM   1644  O  OG1 A THR A  1 199 ? -3.264  16.744  -1.591  0.50 6.41  ? 199 THR A OG1 1 
ATOM   1645  O  OG1 B THR A  1 199 ? -1.040  15.280  -1.656  0.50 12.26 ? 199 THR A OG1 1 
ATOM   1646  C  CG2 A THR A  1 199 ? -1.420  15.500  -2.070  0.50 6.17  ? 199 THR A CG2 1 
ATOM   1647  C  CG2 B THR A  1 199 ? -2.548  17.044  -0.618  0.50 6.94  ? 199 THR A CG2 1 
ATOM   1648  N  N   . PRO A  1 200 ? -3.421  15.720  2.069   1.00 7.95  ? 200 PRO A N   1 
ATOM   1649  C  CA  . PRO A  1 200 ? -4.301  16.551  2.965   1.00 7.07  ? 200 PRO A CA  1 
ATOM   1650  C  C   . PRO A  1 200 ? -4.888  17.723  2.188   1.00 7.98  ? 200 PRO A C   1 
ATOM   1651  O  O   . PRO A  1 200 ? -4.163  18.302  1.361   1.00 9.60  ? 200 PRO A O   1 
ATOM   1652  C  CB  . PRO A  1 200 ? -3.299  17.020  4.066   1.00 7.78  ? 200 PRO A CB  1 
ATOM   1653  C  CG  . PRO A  1 200 ? -2.292  15.873  4.139   1.00 6.89  ? 200 PRO A CG  1 
ATOM   1654  C  CD  . PRO A  1 200 ? -2.116  15.464  2.677   1.00 8.23  ? 200 PRO A CD  1 
ATOM   1655  N  N   . PRO A  1 201 ? -6.155  18.088  2.443   1.00 8.06  ? 201 PRO A N   1 
ATOM   1656  C  CA  . PRO A  1 201 ? -7.057  17.538  3.462   1.00 6.50  ? 201 PRO A CA  1 
ATOM   1657  C  C   . PRO A  1 201 ? -7.826  16.252  3.151   1.00 8.61  ? 201 PRO A C   1 
ATOM   1658  O  O   . PRO A  1 201 ? -8.643  15.856  4.003   1.00 7.62  ? 201 PRO A O   1 
ATOM   1659  C  CB  . PRO A  1 201 ? -8.088  18.707  3.650   1.00 8.10  ? 201 PRO A CB  1 
ATOM   1660  C  CG  . PRO A  1 201 ? -7.690  19.729  2.827   1.00 13.56 ? 201 PRO A CG  1 
ATOM   1661  C  CD  . PRO A  1 201 ? -6.711  19.291  1.793   1.00 8.49  ? 201 PRO A CD  1 
ATOM   1662  N  N   . CYS A  1 202 ? -7.458  15.571  2.019   1.00 7.29  ? 202 CYS A N   1 
ATOM   1663  C  CA  . CYS A  1 202 ? -8.010  14.207  1.691   1.00 6.67  ? 202 CYS A CA  1 
ATOM   1664  C  C   . CYS A  1 202 ? -9.525  14.215  1.487   1.00 6.94  ? 202 CYS A C   1 
ATOM   1665  O  O   . CYS A  1 202 ? -10.192 13.187  1.667   1.00 6.82  ? 202 CYS A O   1 
ATOM   1666  C  CB  . CYS A  1 202 ? -7.712  13.216  2.834   1.00 10.34 ? 202 CYS A CB  1 
ATOM   1667  S  SG  . CYS A  1 202 ? -5.865  12.984  3.095   1.00 6.56  ? 202 CYS A SG  1 
ATOM   1668  N  N   A ASN A  1 203 ? -10.065 15.338  1.033   0.50 7.35  ? 203 ASN A N   1 
ATOM   1669  N  N   B ASN A  1 203 ? -10.098 15.345  1.076   0.50 7.18  ? 203 ASN A N   1 
ATOM   1670  C  CA  A ASN A  1 203 ? -11.525 15.456  0.917   0.50 7.78  ? 203 ASN A CA  1 
ATOM   1671  C  CA  B ASN A  1 203 ? -11.577 15.430  1.019   0.50 7.19  ? 203 ASN A CA  1 
ATOM   1672  C  C   A ASN A  1 203 ? -12.068 14.334  0.031   0.50 7.90  ? 203 ASN A C   1 
ATOM   1673  C  C   B ASN A  1 203 ? -12.083 14.384  0.045   0.50 7.80  ? 203 ASN A C   1 
ATOM   1674  O  O   A ASN A  1 203 ? -11.511 14.103  -1.050  0.50 6.64  ? 203 ASN A O   1 
ATOM   1675  O  O   B ASN A  1 203 ? -11.526 14.284  -1.102  0.50 6.79  ? 203 ASN A O   1 
ATOM   1676  C  CB  A ASN A  1 203 ? -11.864 16.789  0.196   0.50 9.51  ? 203 ASN A CB  1 
ATOM   1677  C  CB  B ASN A  1 203 ? -12.045 16.789  0.408   0.50 8.59  ? 203 ASN A CB  1 
ATOM   1678  C  CG  A ASN A  1 203 ? -11.193 17.997  0.802   0.50 13.05 ? 203 ASN A CG  1 
ATOM   1679  C  CG  B ASN A  1 203 ? -11.466 18.022  1.106   0.50 12.57 ? 203 ASN A CG  1 
ATOM   1680  O  OD1 A ASN A  1 203 ? -9.955  18.090  0.935   0.50 11.58 ? 203 ASN A OD1 1 
ATOM   1681  O  OD1 B ASN A  1 203 ? -10.804 17.901  2.070   0.50 11.48 ? 203 ASN A OD1 1 
ATOM   1682  N  ND2 A ASN A  1 203 ? -12.032 18.958  1.190   0.50 12.12 ? 203 ASN A ND2 1 
ATOM   1683  N  ND2 B ASN A  1 203 ? -11.706 19.221  0.547   0.50 11.23 ? 203 ASN A ND2 1 
ATOM   1684  N  N   . PRO A  1 204 ? -13.175 13.680  0.428   1.00 7.89  ? 204 PRO A N   1 
ATOM   1685  C  CA  . PRO A  1 204 ? -13.715 12.585  -0.418  1.00 7.65  ? 204 PRO A CA  1 
ATOM   1686  C  C   . PRO A  1 204 ? -14.640 13.065  -1.526  1.00 9.88  ? 204 PRO A C   1 
ATOM   1687  O  O   . PRO A  1 204 ? -15.787 12.632  -1.598  1.00 9.32  ? 204 PRO A O   1 
ATOM   1688  C  CB  . PRO A  1 204 ? -14.368 11.706  0.622   1.00 8.71  ? 204 PRO A CB  1 
ATOM   1689  C  CG  . PRO A  1 204 ? -14.937 12.717  1.606   1.00 7.67  ? 204 PRO A CG  1 
ATOM   1690  C  CD  . PRO A  1 204 ? -13.870 13.799  1.731   1.00 7.47  ? 204 PRO A CD  1 
ATOM   1691  N  N   . THR A  1 205 ? -14.111 13.964  -2.360  1.00 8.20  ? 205 THR A N   1 
ATOM   1692  C  CA  . THR A  1 205 ? -15.006 14.762  -3.268  1.00 8.71  ? 205 THR A CA  1 
ATOM   1693  C  C   . THR A  1 205 ? -14.503 14.702  -4.720  1.00 7.52  ? 205 THR A C   1 
ATOM   1694  O  O   . THR A  1 205 ? -14.890 15.624  -5.493  1.00 8.99  ? 205 THR A O   1 
ATOM   1695  C  CB  . THR A  1 205 ? -15.021 16.189  -2.745  1.00 9.73  ? 205 THR A CB  1 
ATOM   1696  O  OG1 . THR A  1 205 ? -13.698 16.633  -2.634  1.00 9.14  ? 205 THR A OG1 1 
ATOM   1697  C  CG2 . THR A  1 205 ? -15.792 16.259  -1.377  1.00 10.37 ? 205 THR A CG2 1 
ATOM   1698  N  N   . VAL A  1 206 ? -13.563 13.747  -5.018  1.00 6.43  ? 206 VAL A N   1 
ATOM   1699  C  CA  . VAL A  1 206 ? -12.955 13.675  -6.359  1.00 6.08  ? 206 VAL A CA  1 
ATOM   1700  C  C   . VAL A  1 206 ? -13.582 12.599  -7.211  1.00 7.00  ? 206 VAL A C   1 
ATOM   1701  O  O   . VAL A  1 206 ? -13.604 11.437  -6.788  1.00 7.79  ? 206 VAL A O   1 
ATOM   1702  C  CB  . VAL A  1 206 ? -11.435 13.404  -6.271  1.00 5.69  ? 206 VAL A CB  1 
ATOM   1703  C  CG1 . VAL A  1 206 ? -10.788 13.363  -7.635  1.00 7.36  ? 206 VAL A CG1 1 
ATOM   1704  C  CG2 . VAL A  1 206 ? -10.745 14.549  -5.453  1.00 7.84  ? 206 VAL A CG2 1 
ATOM   1705  N  N   . LEU A  1 207 ? -14.011 12.951  -8.423  1.00 6.03  ? 207 LEU A N   1 
ATOM   1706  C  CA  . LEU A  1 207 ? -14.311 11.932  -9.461  1.00 6.20  ? 207 LEU A CA  1 
ATOM   1707  C  C   . LEU A  1 207 ? -12.993 11.663  -10.210 1.00 5.43  ? 207 LEU A C   1 
ATOM   1708  O  O   . LEU A  1 207 ? -12.467 12.602  -10.858 1.00 6.15  ? 207 LEU A O   1 
ATOM   1709  C  CB  . LEU A  1 207 ? -15.362 12.540  -10.404 1.00 8.05  ? 207 LEU A CB  1 
ATOM   1710  C  CG  . LEU A  1 207 ? -15.855 11.428  -11.294 1.00 9.75  ? 207 LEU A CG  1 
ATOM   1711  C  CD1 . LEU A  1 207 ? -16.701 10.295  -10.528 1.00 13.95 ? 207 LEU A CD1 1 
ATOM   1712  C  CD2 . LEU A  1 207 ? -16.775 12.168  -12.331 1.00 14.56 ? 207 LEU A CD2 1 
ATOM   1713  N  N   . TRP A  1 208 ? -12.406 10.478  -10.046 1.00 5.55  ? 208 TRP A N   1 
ATOM   1714  C  CA  . TRP A  1 208 ? -11.118 10.175  -10.665 1.00 5.92  ? 208 TRP A CA  1 
ATOM   1715  C  C   . TRP A  1 208 ? -11.299 9.615   -12.079 1.00 5.72  ? 208 TRP A C   1 
ATOM   1716  O  O   . TRP A  1 208 ? -12.215 8.767   -12.284 1.00 6.25  ? 208 TRP A O   1 
ATOM   1717  C  CB  . TRP A  1 208 ? -10.363 9.091   -9.833  1.00 5.88  ? 208 TRP A CB  1 
ATOM   1718  C  CG  . TRP A  1 208 ? -9.663  9.737   -8.664  1.00 5.55  ? 208 TRP A CG  1 
ATOM   1719  C  CD1 . TRP A  1 208 ? -10.134 9.830   -7.376  1.00 4.27  ? 208 TRP A CD1 1 
ATOM   1720  C  CD2 . TRP A  1 208 ? -8.388  10.426  -8.710  1.00 4.82  ? 208 TRP A CD2 1 
ATOM   1721  N  NE1 . TRP A  1 208 ? -9.225  10.621  -6.594  1.00 5.27  ? 208 TRP A NE1 1 
ATOM   1722  C  CE2 . TRP A  1 208 ? -8.140  10.920  -7.399  1.00 3.55  ? 208 TRP A CE2 1 
ATOM   1723  C  CE3 . TRP A  1 208 ? -7.447  10.702  -9.708  1.00 5.72  ? 208 TRP A CE3 1 
ATOM   1724  C  CZ2 . TRP A  1 208 ? -6.994  11.694  -7.090  1.00 5.19  ? 208 TRP A CZ2 1 
ATOM   1725  C  CZ3 . TRP A  1 208 ? -6.299  11.459  -9.374  1.00 5.04  ? 208 TRP A CZ3 1 
ATOM   1726  C  CH2 . TRP A  1 208 ? -6.114  11.960  -8.096  1.00 5.40  ? 208 TRP A CH2 1 
ATOM   1727  N  N   . THR A  1 209 ? -10.411 9.993   -12.986 1.00 4.70  ? 209 THR A N   1 
ATOM   1728  C  CA  . THR A  1 209 ? -10.279 9.323   -14.304 1.00 5.06  ? 209 THR A CA  1 
ATOM   1729  C  C   . THR A  1 209 ? -8.830  9.021   -14.434 1.00 5.46  ? 209 THR A C   1 
ATOM   1730  O  O   . THR A  1 209 ? -8.029  9.966   -14.538 1.00 5.40  ? 209 THR A O   1 
ATOM   1731  C  CB  . THR A  1 209 ? -10.729 10.337  -15.454 1.00 5.76  ? 209 THR A CB  1 
ATOM   1732  O  OG1 . THR A  1 209 ? -12.107 10.668  -15.167 1.00 6.82  ? 209 THR A OG1 1 
ATOM   1733  C  CG2 . THR A  1 209 ? -10.514 9.704   -16.803 1.00 6.92  ? 209 THR A CG2 1 
ATOM   1734  N  N   . VAL A  1 210 ? -8.447  7.757   -14.429 1.00 4.06  ? 210 VAL A N   1 
ATOM   1735  C  CA  . VAL A  1 210 ? -7.028  7.379   -14.568 1.00 5.07  ? 210 VAL A CA  1 
ATOM   1736  C  C   . VAL A  1 210 ? -6.894  6.760   -15.957 1.00 4.75  ? 210 VAL A C   1 
ATOM   1737  O  O   . VAL A  1 210 ? -7.610  5.741   -16.272 1.00 6.44  ? 210 VAL A O   1 
ATOM   1738  C  CB  . VAL A  1 210 ? -6.607  6.334   -13.500 1.00 4.70  ? 210 VAL A CB  1 
ATOM   1739  C  CG1 . VAL A  1 210 ? -5.136  5.827   -13.698 1.00 5.55  ? 210 VAL A CG1 1 
ATOM   1740  C  CG2 . VAL A  1 210 ? -6.873  6.855   -12.101 1.00 5.84  ? 210 VAL A CG2 1 
ATOM   1741  N  N   . PHE A  1 211 ? -6.158  7.359   -16.829 1.00 4.50  ? 211 PHE A N   1 
ATOM   1742  C  CA  . PHE A  1 211 ? -6.068  6.754   -18.189 1.00 4.78  ? 211 PHE A CA  1 
ATOM   1743  C  C   . PHE A  1 211 ? -5.412  5.384   -18.146 1.00 5.22  ? 211 PHE A C   1 
ATOM   1744  O  O   . PHE A  1 211 ? -4.491  5.082   -17.366 1.00 6.25  ? 211 PHE A O   1 
ATOM   1745  C  CB  . PHE A  1 211 ? -5.349  7.707   -19.149 1.00 7.15  ? 211 PHE A CB  1 
ATOM   1746  C  CG  . PHE A  1 211 ? -6.135  8.981   -19.327 1.00 6.16  ? 211 PHE A CG  1 
ATOM   1747  C  CD1 . PHE A  1 211 ? -5.703  10.192  -18.720 1.00 5.25  ? 211 PHE A CD1 1 
ATOM   1748  C  CD2 . PHE A  1 211 ? -7.347  9.016   -20.015 1.00 6.04  ? 211 PHE A CD2 1 
ATOM   1749  C  CE1 . PHE A  1 211 ? -6.443  11.397  -18.910 1.00 7.14  ? 211 PHE A CE1 1 
ATOM   1750  C  CE2 . PHE A  1 211 ? -8.119  10.149  -20.175 1.00 7.12  ? 211 PHE A CE2 1 
ATOM   1751  C  CZ  . PHE A  1 211 ? -7.684  11.374  -19.643 1.00 6.45  ? 211 PHE A CZ  1 
ATOM   1752  N  N   . ARG A  1 212 ? -5.896  4.482   -19.043 1.00 5.78  ? 212 ARG A N   1 
ATOM   1753  C  CA  . ARG A  1 212 ? -5.398  3.096   -19.094 1.00 6.47  ? 212 ARG A CA  1 
ATOM   1754  C  C   . ARG A  1 212 ? -3.909  3.039   -19.448 1.00 6.00  ? 212 ARG A C   1 
ATOM   1755  O  O   . ARG A  1 212 ? -3.180  2.271   -18.827 1.00 7.16  ? 212 ARG A O   1 
ATOM   1756  C  CB  . ARG A  1 212 ? -6.241  2.336   -20.139 1.00 6.64  ? 212 ARG A CB  1 
ATOM   1757  C  CG  . ARG A  1 212 ? -5.784  0.892   -20.238 1.00 9.30  ? 212 ARG A CG  1 
ATOM   1758  C  CD  . ARG A  1 212 ? -6.478  0.193   -21.416 1.00 10.90 ? 212 ARG A CD  1 
ATOM   1759  N  NE  . ARG A  1 212 ? -6.192  -1.243  -21.303 1.00 10.84 ? 212 ARG A NE  1 
ATOM   1760  C  CZ  . ARG A  1 212 ? -6.769  -2.136  -22.145 1.00 13.84 ? 212 ARG A CZ  1 
ATOM   1761  N  NH1 . ARG A  1 212 ? -7.481  -1.684  -23.206 1.00 11.16 ? 212 ARG A NH1 1 
ATOM   1762  N  NH2 . ARG A  1 212 ? -6.538  -3.469  -21.915 1.00 15.18 ? 212 ARG A NH2 1 
ATOM   1763  N  N   . ASN A  1 213 ? -3.515  3.808   -20.431 1.00 5.85  ? 213 ASN A N   1 
ATOM   1764  C  CA  . ASN A  1 213 ? -2.119  3.664   -20.945 1.00 7.39  ? 213 ASN A CA  1 
ATOM   1765  C  C   . ASN A  1 213 ? -1.158  4.664   -20.336 1.00 7.46  ? 213 ASN A C   1 
ATOM   1766  O  O   . ASN A  1 213 ? -1.524  5.843   -20.185 1.00 7.40  ? 213 ASN A O   1 
ATOM   1767  C  CB  . ASN A  1 213 ? -2.160  3.861   -22.454 1.00 9.07  ? 213 ASN A CB  1 
ATOM   1768  C  CG  . ASN A  1 213 ? -2.945  2.727   -23.168 1.00 13.08 ? 213 ASN A CG  1 
ATOM   1769  O  OD1 . ASN A  1 213 ? -2.759  1.547   -22.867 1.00 17.77 ? 213 ASN A OD1 1 
ATOM   1770  N  ND2 . ASN A  1 213 ? -3.807  3.110   -24.017 1.00 16.03 ? 213 ASN A ND2 1 
ATOM   1771  N  N   . PRO A  1 214 ? 0.076   4.237   -20.048 1.00 6.85  ? 214 PRO A N   1 
ATOM   1772  C  CA  . PRO A  1 214 ? 1.030   5.186   -19.478 1.00 7.20  ? 214 PRO A CA  1 
ATOM   1773  C  C   . PRO A  1 214 ? 1.668   5.987   -20.598 1.00 7.31  ? 214 PRO A C   1 
ATOM   1774  O  O   . PRO A  1 214 ? 1.616   5.579   -21.783 1.00 8.07  ? 214 PRO A O   1 
ATOM   1775  C  CB  . PRO A  1 214 ? 2.139   4.346   -18.886 1.00 7.07  ? 214 PRO A CB  1 
ATOM   1776  C  CG  . PRO A  1 214 ? 2.092   3.032   -19.759 1.00 10.49 ? 214 PRO A CG  1 
ATOM   1777  C  CD  . PRO A  1 214 ? 0.562   2.847   -20.056 1.00 9.04  ? 214 PRO A CD  1 
ATOM   1778  N  N   . VAL A  1 215 ? 2.322   7.124   -20.235 1.00 5.08  ? 215 VAL A N   1 
ATOM   1779  C  CA  . VAL A  1 215 ? 3.242   7.758   -21.169 1.00 6.86  ? 215 VAL A CA  1 
ATOM   1780  C  C   . VAL A  1 215 ? 4.686   7.426   -20.721 1.00 6.27  ? 215 VAL A C   1 
ATOM   1781  O  O   . VAL A  1 215 ? 4.880   6.851   -19.651 1.00 5.75  ? 215 VAL A O   1 
ATOM   1782  C  CB  . VAL A  1 215 ? 3.105   9.325   -21.127 1.00 6.19  ? 215 VAL A CB  1 
ATOM   1783  C  CG1 . VAL A  1 215 ? 1.754   9.703   -21.591 1.00 8.81  ? 215 VAL A CG1 1 
ATOM   1784  C  CG2 . VAL A  1 215 ? 3.432   9.853   -19.690 1.00 8.72  ? 215 VAL A CG2 1 
ATOM   1785  N  N   . GLN A  1 216 ? 5.643   7.734   -21.586 1.00 5.45  ? 216 GLN A N   1 
ATOM   1786  C  CA  . GLN A  1 216 ? 7.040   7.557   -21.263 1.00 4.93  ? 216 GLN A CA  1 
ATOM   1787  C  C   . GLN A  1 216 ? 7.770   8.914   -21.201 1.00 5.55  ? 216 GLN A C   1 
ATOM   1788  O  O   . GLN A  1 216 ? 7.515   9.813   -21.976 1.00 5.80  ? 216 GLN A O   1 
ATOM   1789  C  CB  . GLN A  1 216 ? 7.781   6.648   -22.340 1.00 7.49  ? 216 GLN A CB  1 
ATOM   1790  C  CG  . GLN A  1 216 ? 7.331   5.139   -22.192 1.00 7.39  ? 216 GLN A CG  1 
ATOM   1791  C  CD  . GLN A  1 216 ? 8.058   4.287   -23.149 1.00 7.86  ? 216 GLN A CD  1 
ATOM   1792  O  OE1 . GLN A  1 216 ? 9.029   4.634   -23.791 1.00 6.60  ? 216 GLN A OE1 1 
ATOM   1793  N  NE2 . GLN A  1 216 ? 7.574   3.061   -23.219 1.00 11.69 ? 216 GLN A NE2 1 
ATOM   1794  N  N   . ILE A  1 217 ? 8.675   8.978   -20.219 1.00 4.71  ? 217 ILE A N   1 
ATOM   1795  C  CA  . ILE A  1 217 ? 9.719   10.044  -20.161 1.00 6.34  ? 217 ILE A CA  1 
ATOM   1796  C  C   . ILE A  1 217 ? 11.077  9.420   -20.069 1.00 5.15  ? 217 ILE A C   1 
ATOM   1797  O  O   . ILE A  1 217 ? 11.162  8.233   -19.684 1.00 6.89  ? 217 ILE A O   1 
ATOM   1798  C  CB  . ILE A  1 217 ? 9.495   11.013  -18.926 1.00 5.87  ? 217 ILE A CB  1 
ATOM   1799  C  CG1 . ILE A  1 217 ? 9.647   10.249  -17.597 1.00 5.15  ? 217 ILE A CG1 1 
ATOM   1800  C  CG2 . ILE A  1 217 ? 8.024   11.621  -19.068 1.00 6.76  ? 217 ILE A CG2 1 
ATOM   1801  C  CD1 . ILE A  1 217 ? 9.591   11.236  -16.310 1.00 4.37  ? 217 ILE A CD1 1 
ATOM   1802  N  N   . SER A  1 218 ? 12.181  10.127  -20.450 1.00 5.93  ? 218 SER A N   1 
ATOM   1803  C  CA  . SER A  1 218 ? 13.467  9.447   -20.446 1.00 5.49  ? 218 SER A CA  1 
ATOM   1804  C  C   . SER A  1 218 ? 14.026  9.199   -19.044 1.00 6.71  ? 218 SER A C   1 
ATOM   1805  O  O   . SER A  1 218 ? 13.542  9.705   -18.026 1.00 7.76  ? 218 SER A O   1 
ATOM   1806  C  CB  . SER A  1 218 ? 14.482  10.223  -21.281 1.00 7.49  ? 218 SER A CB  1 
ATOM   1807  O  OG  . SER A  1 218 ? 14.814  11.443  -20.646 1.00 7.43  ? 218 SER A OG  1 
ATOM   1808  N  N   A GLN A  1 219 ? 15.118  8.427   -19.026 0.50 7.53  ? 219 GLN A N   1 
ATOM   1809  N  N   B GLN A  1 219 ? 14.948  8.257   -18.878 0.50 7.91  ? 219 GLN A N   1 
ATOM   1810  C  CA  A GLN A  1 219 ? 15.874  8.149   -17.809 0.50 7.41  ? 219 GLN A CA  1 
ATOM   1811  C  CA  B GLN A  1 219 ? 15.685  8.152   -17.632 0.50 7.67  ? 219 GLN A CA  1 
ATOM   1812  C  C   A GLN A  1 219 ? 16.298  9.467   -17.236 0.50 6.35  ? 219 GLN A C   1 
ATOM   1813  C  C   B GLN A  1 219 ? 16.296  9.523   -17.205 0.50 6.70  ? 219 GLN A C   1 
ATOM   1814  O  O   A GLN A  1 219 ? 16.187  9.685   -16.003 0.50 7.89  ? 219 GLN A O   1 
ATOM   1815  O  O   B GLN A  1 219 ? 16.266  9.896   -16.032 0.50 7.42  ? 219 GLN A O   1 
ATOM   1816  C  CB  A GLN A  1 219 ? 17.148  7.322   -18.093 0.50 6.93  ? 219 GLN A CB  1 
ATOM   1817  C  CB  B GLN A  1 219 ? 16.726  7.028   -17.794 0.50 7.86  ? 219 GLN A CB  1 
ATOM   1818  C  CG  A GLN A  1 219 ? 18.021  7.226   -16.784 0.50 10.27 ? 219 GLN A CG  1 
ATOM   1819  C  CG  B GLN A  1 219 ? 17.728  6.766   -16.658 0.50 12.22 ? 219 GLN A CG  1 
ATOM   1820  C  CD  A GLN A  1 219 ? 17.206  6.501   -15.647 0.50 13.90 ? 219 GLN A CD  1 
ATOM   1821  C  CD  B GLN A  1 219 ? 17.125  6.351   -15.314 0.50 18.82 ? 219 GLN A CD  1 
ATOM   1822  O  OE1 A GLN A  1 219 ? 17.201  5.243   -15.611 0.50 17.59 ? 219 GLN A OE1 1 
ATOM   1823  O  OE1 B GLN A  1 219 ? 17.831  6.430   -14.268 0.50 22.53 ? 219 GLN A OE1 1 
ATOM   1824  N  NE2 A GLN A  1 219 ? 16.542  7.306   -14.670 0.50 15.47 ? 219 GLN A NE2 1 
ATOM   1825  N  NE2 B GLN A  1 219 ? 15.846  5.937   -15.300 0.50 13.92 ? 219 GLN A NE2 1 
ATOM   1826  N  N   . GLU A  1 220 ? 16.827  10.325  -18.102 1.00 7.45  ? 220 GLU A N   1 
ATOM   1827  C  CA  . GLU A  1 220 ? 17.392  11.619  -17.639 1.00 8.87  ? 220 GLU A CA  1 
ATOM   1828  C  C   . GLU A  1 220 ? 16.273  12.546  -17.118 1.00 6.75  ? 220 GLU A C   1 
ATOM   1829  O  O   . GLU A  1 220 ? 16.452  13.285  -16.091 1.00 8.19  ? 220 GLU A O   1 
ATOM   1830  C  CB  . GLU A  1 220 ? 18.188  12.301  -18.777 1.00 10.29 ? 220 GLU A CB  1 
ATOM   1831  C  CG  . GLU A  1 220 ? 19.513  11.531  -19.018 1.00 13.68 ? 220 GLU A CG  1 
ATOM   1832  C  CD  . GLU A  1 220 ? 19.328  10.407  -19.991 1.00 27.86 ? 220 GLU A CD  1 
ATOM   1833  O  OE1 . GLU A  1 220 ? 18.271  10.305  -20.684 1.00 25.04 ? 220 GLU A OE1 1 
ATOM   1834  O  OE2 . GLU A  1 220 ? 20.287  9.587   -20.085 1.00 28.65 ? 220 GLU A OE2 1 
ATOM   1835  N  N   . GLN A  1 221 ? 15.117  12.533  -17.788 1.00 7.13  ? 221 GLN A N   1 
ATOM   1836  C  CA  . GLN A  1 221 ? 14.010  13.390  -17.306 1.00 5.68  ? 221 GLN A CA  1 
ATOM   1837  C  C   . GLN A  1 221 ? 13.535  12.907  -15.967 1.00 6.35  ? 221 GLN A C   1 
ATOM   1838  O  O   . GLN A  1 221 ? 13.271  13.752  -15.093 1.00 7.14  ? 221 GLN A O   1 
ATOM   1839  C  CB  . GLN A  1 221 ? 12.837  13.303  -18.307 1.00 5.66  ? 221 GLN A CB  1 
ATOM   1840  C  CG  . GLN A  1 221 ? 13.062  14.138  -19.558 1.00 6.26  ? 221 GLN A CG  1 
ATOM   1841  C  CD  . GLN A  1 221 ? 11.849  14.051  -20.547 1.00 6.05  ? 221 GLN A CD  1 
ATOM   1842  O  OE1 . GLN A  1 221 ? 11.516  12.902  -20.962 1.00 6.09  ? 221 GLN A OE1 1 
ATOM   1843  N  NE2 . GLN A  1 221 ? 11.222  15.124  -20.958 1.00 6.65  ? 221 GLN A NE2 1 
ATOM   1844  N  N   . LEU A  1 222 ? 13.355  11.557  -15.779 1.00 6.73  ? 222 LEU A N   1 
ATOM   1845  C  CA  . LEU A  1 222 ? 12.898  11.012  -14.452 1.00 5.51  ? 222 LEU A CA  1 
ATOM   1846  C  C   . LEU A  1 222 ? 13.928  11.348  -13.421 1.00 6.35  ? 222 LEU A C   1 
ATOM   1847  O  O   . LEU A  1 222 ? 13.530  11.767  -12.322 1.00 7.23  ? 222 LEU A O   1 
ATOM   1848  C  CB  . LEU A  1 222 ? 12.670  9.496   -14.625 1.00 5.96  ? 222 LEU A CB  1 
ATOM   1849  C  CG  . LEU A  1 222 ? 12.187  8.821   -13.316 1.00 5.25  ? 222 LEU A CG  1 
ATOM   1850  C  CD1 . LEU A  1 222 ? 10.862  9.433   -12.775 1.00 6.79  ? 222 LEU A CD1 1 
ATOM   1851  C  CD2 . LEU A  1 222 ? 12.124  7.319   -13.600 1.00 8.52  ? 222 LEU A CD2 1 
ATOM   1852  N  N   . LEU A  1 223 ? 15.213  11.219  -13.715 1.00 6.42  ? 223 LEU A N   1 
ATOM   1853  C  CA  . LEU A  1 223 ? 16.225  11.517  -12.647 1.00 6.56  ? 223 LEU A CA  1 
ATOM   1854  C  C   . LEU A  1 223 ? 16.213  13.028  -12.341 1.00 7.25  ? 223 LEU A C   1 
ATOM   1855  O  O   . LEU A  1 223 ? 16.354  13.376  -11.173 1.00 8.49  ? 223 LEU A O   1 
ATOM   1856  C  CB  . LEU A  1 223 ? 17.596  11.032  -13.164 1.00 8.26  ? 223 LEU A CB  1 
ATOM   1857  C  CG  . LEU A  1 223 ? 18.667  11.194  -12.090 1.00 9.44  ? 223 LEU A CG  1 
ATOM   1858  C  CD1 . LEU A  1 223 ? 18.381  10.047  -11.034 1.00 10.88 ? 223 LEU A CD1 1 
ATOM   1859  C  CD2 . LEU A  1 223 ? 20.058  10.889  -12.862 1.00 10.43 ? 223 LEU A CD2 1 
ATOM   1860  N  N   . ALA A  1 224 ? 16.006  13.916  -13.341 1.00 7.16  ? 224 ALA A N   1 
ATOM   1861  C  CA  . ALA A  1 224 ? 15.866  15.364  -12.989 1.00 6.74  ? 224 ALA A CA  1 
ATOM   1862  C  C   . ALA A  1 224 ? 14.684  15.566  -12.049 1.00 8.18  ? 224 ALA A C   1 
ATOM   1863  O  O   . ALA A  1 224 ? 14.803  16.305  -11.048 1.00 7.57  ? 224 ALA A O   1 
ATOM   1864  C  CB  . ALA A  1 224 ? 15.734  16.129  -14.245 1.00 7.55  ? 224 ALA A CB  1 
ATOM   1865  N  N   . LEU A  1 225 ? 13.551  14.930  -12.326 1.00 6.39  ? 225 LEU A N   1 
ATOM   1866  C  CA  . LEU A  1 225 ? 12.356  15.140  -11.521 1.00 7.21  ? 225 LEU A CA  1 
ATOM   1867  C  C   . LEU A  1 225 ? 12.650  14.650  -10.073 1.00 5.91  ? 225 LEU A C   1 
ATOM   1868  O  O   . LEU A  1 225 ? 12.214  15.322  -9.084  1.00 7.40  ? 225 LEU A O   1 
ATOM   1869  C  CB  . LEU A  1 225 ? 11.217  14.341  -12.145 1.00 6.21  ? 225 LEU A CB  1 
ATOM   1870  C  CG  . LEU A  1 225 ? 9.890   14.538  -11.378 1.00 6.40  ? 225 LEU A CG  1 
ATOM   1871  C  CD1 . LEU A  1 225 ? 9.408   16.013  -11.321 1.00 7.10  ? 225 LEU A CD1 1 
ATOM   1872  C  CD2 . LEU A  1 225 ? 8.855   13.617  -12.017 1.00 8.39  ? 225 LEU A CD2 1 
ATOM   1873  N  N   . GLU A  1 226 ? 13.416  13.544  -9.915  1.00 6.60  ? 226 GLU A N   1 
ATOM   1874  C  CA  . GLU A  1 226 ? 13.642  12.947  -8.587  1.00 7.57  ? 226 GLU A CA  1 
ATOM   1875  C  C   . GLU A  1 226 ? 14.779  13.641  -7.865  1.00 8.42  ? 226 GLU A C   1 
ATOM   1876  O  O   . GLU A  1 226 ? 14.926  13.343  -6.640  1.00 9.87  ? 226 GLU A O   1 
ATOM   1877  C  CB  . GLU A  1 226 ? 14.055  11.456  -8.743  1.00 7.25  ? 226 GLU A CB  1 
ATOM   1878  C  CG  . GLU A  1 226 ? 12.940  10.504  -9.253  1.00 7.31  ? 226 GLU A CG  1 
ATOM   1879  C  CD  . GLU A  1 226 ? 13.479  9.266   -9.894  1.00 7.62  ? 226 GLU A CD  1 
ATOM   1880  O  OE1 . GLU A  1 226 ? 14.707  9.195   -10.288 1.00 6.81  ? 226 GLU A OE1 1 
ATOM   1881  O  OE2 . GLU A  1 226 ? 12.727  8.308   -10.005 1.00 7.79  ? 226 GLU A OE2 1 
ATOM   1882  N  N   . THR A  1 227 ? 15.612  14.427  -8.561  1.00 6.94  ? 227 THR A N   1 
ATOM   1883  C  CA  . THR A  1 227 ? 16.830  14.964  -7.821  1.00 8.71  ? 227 THR A CA  1 
ATOM   1884  C  C   . THR A  1 227 ? 16.897  16.481  -7.796  1.00 9.27  ? 227 THR A C   1 
ATOM   1885  O  O   . THR A  1 227 ? 17.737  17.021  -7.028  1.00 11.11 ? 227 THR A O   1 
ATOM   1886  C  CB  . THR A  1 227 ? 18.155  14.494  -8.517  1.00 8.44  ? 227 THR A CB  1 
ATOM   1887  O  OG1 . THR A  1 227 ? 18.208  14.866  -9.911  1.00 8.82  ? 227 THR A OG1 1 
ATOM   1888  C  CG2 . THR A  1 227 ? 18.316  12.994  -8.423  1.00 9.00  ? 227 THR A CG2 1 
ATOM   1889  N  N   . ALA A  1 228 ? 16.050  17.199  -8.543  1.00 7.02  ? 228 ALA A N   1 
ATOM   1890  C  CA  . ALA A  1 228 ? 16.299  18.668  -8.667  1.00 7.22  ? 228 ALA A CA  1 
ATOM   1891  C  C   . ALA A  1 228 ? 15.683  19.358  -7.519  1.00 8.10  ? 228 ALA A C   1 
ATOM   1892  O  O   . ALA A  1 228 ? 16.095  20.496  -7.283  1.00 8.35  ? 228 ALA A O   1 
ATOM   1893  C  CB  . ALA A  1 228 ? 15.622  19.218  -9.911  1.00 7.67  ? 228 ALA A CB  1 
ATOM   1894  N  N   . LEU A  1 229 ? 14.625  18.811  -6.884  1.00 7.13  ? 229 LEU A N   1 
ATOM   1895  C  CA  . LEU A  1 229 ? 13.768  19.624  -6.025  1.00 6.09  ? 229 LEU A CA  1 
ATOM   1896  C  C   . LEU A  1 229 ? 13.927  19.304  -4.537  1.00 6.31  ? 229 LEU A C   1 
ATOM   1897  O  O   . LEU A  1 229 ? 14.177  18.176  -4.122  1.00 7.43  ? 229 LEU A O   1 
ATOM   1898  C  CB  . LEU A  1 229 ? 12.244  19.468  -6.385  1.00 6.27  ? 229 LEU A CB  1 
ATOM   1899  C  CG  . LEU A  1 229 ? 11.957  19.696  -7.908  1.00 8.37  ? 229 LEU A CG  1 
ATOM   1900  C  CD1 . LEU A  1 229 ? 10.451  19.507  -8.166  1.00 9.83  ? 229 LEU A CD1 1 
ATOM   1901  C  CD2 . LEU A  1 229 ? 12.375  21.155  -8.394  1.00 10.00 ? 229 LEU A CD2 1 
ATOM   1902  N  N   . TYR A  1 230 ? 13.682  20.368  -3.752  1.00 7.44  ? 230 TYR A N   1 
ATOM   1903  C  CA  . TYR A  1 230 ? 13.619  20.253  -2.259  1.00 8.01  ? 230 TYR A CA  1 
ATOM   1904  C  C   . TYR A  1 230 ? 12.263  20.779  -1.687  1.00 6.03  ? 230 TYR A C   1 
ATOM   1905  O  O   . TYR A  1 230 ? 11.679  21.663  -2.232  1.00 7.61  ? 230 TYR A O   1 
ATOM   1906  C  CB  . TYR A  1 230 ? 14.789  21.102  -1.609  1.00 9.28  ? 230 TYR A CB  1 
ATOM   1907  C  CG  . TYR A  1 230 ? 16.126  20.522  -2.127  1.00 11.48 ? 230 TYR A CG  1 
ATOM   1908  C  CD1 . TYR A  1 230 ? 16.649  20.873  -3.429  1.00 12.51 ? 230 TYR A CD1 1 
ATOM   1909  C  CD2 . TYR A  1 230 ? 16.822  19.613  -1.327  1.00 12.58 ? 230 TYR A CD2 1 
ATOM   1910  C  CE1 . TYR A  1 230 ? 17.791  20.276  -3.942  1.00 12.85 ? 230 TYR A CE1 1 
ATOM   1911  C  CE2 . TYR A  1 230 ? 17.986  19.002  -1.843  1.00 12.44 ? 230 TYR A CE2 1 
ATOM   1912  C  CZ  . TYR A  1 230 ? 18.423  19.356  -3.130  1.00 16.93 ? 230 TYR A CZ  1 
ATOM   1913  O  OH  . TYR A  1 230 ? 19.551  18.766  -3.713  1.00 16.43 ? 230 TYR A OH  1 
ATOM   1914  N  N   . CYS A  1 231 ? 11.900  20.152  -0.572  1.00 7.21  ? 231 CYS A N   1 
ATOM   1915  C  CA  . CYS A  1 231 ? 10.678  20.613  0.146   1.00 7.71  ? 231 CYS A CA  1 
ATOM   1916  C  C   . CYS A  1 231 ? 10.904  21.887  0.952   1.00 10.44 ? 231 CYS A C   1 
ATOM   1917  O  O   . CYS A  1 231 ? 9.887   22.535  1.337   1.00 11.01 ? 231 CYS A O   1 
ATOM   1918  C  CB  . CYS A  1 231 ? 10.229  19.580  1.186   1.00 7.44  ? 231 CYS A CB  1 
ATOM   1919  S  SG  . CYS A  1 231 ? 9.802   17.946  0.401   1.00 9.95  ? 231 CYS A SG  1 
ATOM   1920  N  N   . THR A  1 232 ? 12.173  22.187  1.204   1.00 10.37 ? 232 THR A N   1 
ATOM   1921  C  CA  . THR A  1 232 ? 12.574  23.331  2.071   1.00 9.87  ? 232 THR A CA  1 
ATOM   1922  C  C   . THR A  1 232 ? 12.965  24.533  1.256   1.00 12.29 ? 232 THR A C   1 
ATOM   1923  O  O   . THR A  1 232 ? 13.184  24.496  0.044   1.00 11.34 ? 232 THR A O   1 
ATOM   1924  C  CB  . THR A  1 232 ? 13.676  22.820  2.934   1.00 12.25 ? 232 THR A CB  1 
ATOM   1925  O  OG1 . THR A  1 232 ? 14.635  22.083  2.135   1.00 11.86 ? 232 THR A OG1 1 
ATOM   1926  C  CG2 . THR A  1 232 ? 13.163  21.983  4.034   1.00 13.53 ? 232 THR A CG2 1 
ATOM   1927  N  N   . HIS A  1 233 ? 12.899  25.709  1.962   1.00 13.92 ? 233 HIS A N   1 
ATOM   1928  C  CA  . HIS A  1 233 ? 13.382  26.987  1.363   1.00 14.93 ? 233 HIS A CA  1 
ATOM   1929  C  C   . HIS A  1 233 ? 14.910  27.031  1.100   1.00 14.46 ? 233 HIS A C   1 
ATOM   1930  O  O   . HIS A  1 233 ? 15.634  26.287  1.702   1.00 16.08 ? 233 HIS A O   1 
ATOM   1931  C  CB  . HIS A  1 233 ? 12.980  28.155  2.323   1.00 15.19 ? 233 HIS A CB  1 
ATOM   1932  C  CG  . HIS A  1 233 ? 11.520  28.334  2.497   1.00 17.37 ? 233 HIS A CG  1 
ATOM   1933  N  ND1 . HIS A  1 233 ? 10.692  29.001  1.598   1.00 19.13 ? 233 HIS A ND1 1 
ATOM   1934  C  CD2 . HIS A  1 233 ? 10.729  28.001  3.545   1.00 20.15 ? 233 HIS A CD2 1 
ATOM   1935  C  CE1 . HIS A  1 233 ? 9.451   29.033  2.089   1.00 18.69 ? 233 HIS A CE1 1 
ATOM   1936  N  NE2 . HIS A  1 233 ? 9.449   28.418  3.246   1.00 22.78 ? 233 HIS A NE2 1 
ATOM   1937  N  N   . MET A  1 234 ? 15.289  27.856  0.118   1.00 16.18 ? 234 MET A N   1 
ATOM   1938  C  CA  . MET A  1 234 ? 16.704  28.005  -0.257  1.00 20.80 ? 234 MET A CA  1 
ATOM   1939  C  C   . MET A  1 234 ? 17.452  28.369  1.030   1.00 23.42 ? 234 MET A C   1 
ATOM   1940  O  O   . MET A  1 234 ? 16.951  29.145  1.848   1.00 24.76 ? 234 MET A O   1 
ATOM   1941  C  CB  . MET A  1 234 ? 16.835  29.093  -1.309  1.00 19.59 ? 234 MET A CB  1 
ATOM   1942  C  CG  . MET A  1 234 ? 18.259  29.311  -1.828  1.00 23.48 ? 234 MET A CG  1 
ATOM   1943  S  SD  . MET A  1 234 ? 18.194  30.551  -3.139  1.00 27.73 ? 234 MET A SD  1 
ATOM   1944  C  CE  . MET A  1 234 ? 17.488  31.893  -2.121  1.00 30.87 ? 234 MET A CE  1 
ATOM   1945  N  N   . ASP A  1 235 ? 18.593  27.791  1.304   1.00 28.16 ? 235 ASP A N   1 
ATOM   1946  C  CA  . ASP A  1 235 ? 19.291  28.363  2.482   1.00 32.77 ? 235 ASP A CA  1 
ATOM   1947  C  C   . ASP A  1 235 ? 18.715  28.006  3.845   1.00 33.37 ? 235 ASP A C   1 
ATOM   1948  O  O   . ASP A  1 235 ? 19.281  28.384  4.874   1.00 35.43 ? 235 ASP A O   1 
ATOM   1949  C  CB  . ASP A  1 235 ? 19.311  29.914  2.402   1.00 34.44 ? 235 ASP A CB  1 
ATOM   1950  C  CG  . ASP A  1 235 ? 20.125  30.438  1.213   1.00 38.10 ? 235 ASP A CG  1 
ATOM   1951  O  OD1 . ASP A  1 235 ? 21.179  29.801  0.936   1.00 44.31 ? 235 ASP A OD1 1 
ATOM   1952  O  OD2 . ASP A  1 235 ? 19.677  31.441  0.569   1.00 41.11 ? 235 ASP A OD2 1 
ATOM   1953  N  N   . ASP A  1 236 ? 17.594  27.272  3.874   1.00 33.69 ? 236 ASP A N   1 
ATOM   1954  C  CA  . ASP A  1 236 ? 17.335  26.383  5.004   1.00 31.59 ? 236 ASP A CA  1 
ATOM   1955  C  C   . ASP A  1 236 ? 18.589  25.516  5.212   1.00 32.47 ? 236 ASP A C   1 
ATOM   1956  O  O   . ASP A  1 236 ? 19.103  24.920  4.248   1.00 33.46 ? 236 ASP A O   1 
ATOM   1957  C  CB  . ASP A  1 236 ? 16.102  25.485  4.747   1.00 30.31 ? 236 ASP A CB  1 
ATOM   1958  C  CG  . ASP A  1 236 ? 15.744  24.649  5.953   1.00 26.88 ? 236 ASP A CG  1 
ATOM   1959  O  OD1 . ASP A  1 236 ? 16.676  24.127  6.689   1.00 26.43 ? 236 ASP A OD1 1 
ATOM   1960  O  OD2 . ASP A  1 236 ? 14.515  24.564  6.222   1.00 25.14 ? 236 ASP A OD2 1 
ATOM   1961  N  N   . PRO A  1 237 ? 19.186  25.560  6.441   1.00 33.70 ? 237 PRO A N   1 
ATOM   1962  C  CA  . PRO A  1 237 ? 20.479  24.870  6.609   1.00 32.98 ? 237 PRO A CA  1 
ATOM   1963  C  C   . PRO A  1 237 ? 20.422  23.320  6.603   1.00 32.28 ? 237 PRO A C   1 
ATOM   1964  O  O   . PRO A  1 237 ? 21.510  22.665  6.508   1.00 33.10 ? 237 PRO A O   1 
ATOM   1965  C  CB  . PRO A  1 237 ? 21.070  25.443  7.944   1.00 33.22 ? 237 PRO A CB  1 
ATOM   1966  C  CG  . PRO A  1 237 ? 20.080  26.453  8.418   1.00 33.50 ? 237 PRO A CG  1 
ATOM   1967  C  CD  . PRO A  1 237 ? 18.747  26.256  7.671   1.00 33.77 ? 237 PRO A CD  1 
ATOM   1968  N  N   A SER A  1 238 ? 19.210  22.764  6.667   0.50 30.53 ? 238 SER A N   1 
ATOM   1969  N  N   B SER A  1 238 ? 19.213  22.757  6.735   0.50 30.88 ? 238 SER A N   1 
ATOM   1970  C  CA  A SER A  1 238 ? 19.016  21.310  6.668   0.50 28.64 ? 238 SER A CA  1 
ATOM   1971  C  CA  B SER A  1 238 ? 18.999  21.297  6.687   0.50 29.36 ? 238 SER A CA  1 
ATOM   1972  C  C   A SER A  1 238 ? 18.005  20.946  5.597   0.50 27.42 ? 238 SER A C   1 
ATOM   1973  C  C   B SER A  1 238 ? 17.990  20.969  5.593   0.50 27.79 ? 238 SER A C   1 
ATOM   1974  O  O   A SER A  1 238 ? 16.829  20.722  5.905   0.50 27.38 ? 238 SER A O   1 
ATOM   1975  O  O   B SER A  1 238 ? 16.797  20.798  5.880   0.50 27.94 ? 238 SER A O   1 
ATOM   1976  C  CB  A SER A  1 238 ? 18.505  20.843  8.024   0.50 28.44 ? 238 SER A CB  1 
ATOM   1977  C  CB  B SER A  1 238 ? 18.469  20.750  8.020   0.50 29.05 ? 238 SER A CB  1 
ATOM   1978  O  OG  A SER A  1 238 ? 19.321  21.414  9.032   0.50 26.24 ? 238 SER A OG  1 
ATOM   1979  O  OG  B SER A  1 238 ? 17.303  21.437  8.438   0.50 29.86 ? 238 SER A OG  1 
ATOM   1980  N  N   . PRO A  1 239 ? 18.470  20.890  4.352   1.00 27.94 ? 239 PRO A N   1 
ATOM   1981  C  CA  . PRO A  1 239 ? 17.503  20.629  3.293   1.00 24.37 ? 239 PRO A CA  1 
ATOM   1982  C  C   . PRO A  1 239 ? 16.748  19.270  3.471   1.00 23.73 ? 239 PRO A C   1 
ATOM   1983  O  O   . PRO A  1 239 ? 17.227  18.321  4.137   1.00 22.02 ? 239 PRO A O   1 
ATOM   1984  C  CB  . PRO A  1 239 ? 18.325  20.756  2.014   1.00 25.48 ? 239 PRO A CB  1 
ATOM   1985  C  CG  . PRO A  1 239 ? 19.821  20.754  2.401   1.00 28.87 ? 239 PRO A CG  1 
ATOM   1986  C  CD  . PRO A  1 239 ? 19.871  21.007  3.878   1.00 27.59 ? 239 PRO A CD  1 
ATOM   1987  N  N   . ARG A  1 240 ? 15.519  19.228  2.939   1.00 17.72 ? 240 ARG A N   1 
ATOM   1988  C  CA  . ARG A  1 240 ? 14.786  17.937  2.765   1.00 12.57 ? 240 ARG A CA  1 
ATOM   1989  C  C   . ARG A  1 240 ? 14.557  17.772  1.229   1.00 10.88 ? 240 ARG A C   1 
ATOM   1990  O  O   . ARG A  1 240 ? 13.930  18.632  0.626   1.00 10.67 ? 240 ARG A O   1 
ATOM   1991  C  CB  . ARG A  1 240 ? 13.474  17.883  3.528   1.00 13.99 ? 240 ARG A CB  1 
ATOM   1992  C  CG  . ARG A  1 240 ? 13.577  17.673  5.067   1.00 16.69 ? 240 ARG A CG  1 
ATOM   1993  C  CD  . ARG A  1 240 ? 12.196  17.731  5.672   1.00 16.42 ? 240 ARG A CD  1 
ATOM   1994  N  NE  . ARG A  1 240 ? 11.449  18.989  5.561   1.00 15.11 ? 240 ARG A NE  1 
ATOM   1995  C  CZ  . ARG A  1 240 ? 10.278  19.172  4.949   1.00 16.19 ? 240 ARG A CZ  1 
ATOM   1996  N  NH1 . ARG A  1 240 ? 9.773   18.180  4.204   1.00 12.91 ? 240 ARG A NH1 1 
ATOM   1997  N  NH2 . ARG A  1 240 ? 9.725   20.400  4.937   1.00 15.27 ? 240 ARG A NH2 1 
ATOM   1998  N  N   . GLU A  1 241 ? 15.095  16.691  0.668   1.00 9.94  ? 241 GLU A N   1 
ATOM   1999  C  CA  . GLU A  1 241 ? 14.858  16.368  -0.752  1.00 8.93  ? 241 GLU A CA  1 
ATOM   2000  C  C   . GLU A  1 241 ? 13.344  16.070  -0.984  1.00 7.77  ? 241 GLU A C   1 
ATOM   2001  O  O   . GLU A  1 241 ? 12.659  15.394  -0.182  1.00 8.56  ? 241 GLU A O   1 
ATOM   2002  C  CB  . GLU A  1 241 ? 15.583  15.123  -1.160  1.00 9.08  ? 241 GLU A CB  1 
ATOM   2003  C  CG  . GLU A  1 241 ? 17.066  15.330  -1.057  1.00 13.64 ? 241 GLU A CG  1 
ATOM   2004  C  CD  . GLU A  1 241 ? 17.818  14.082  -1.504  1.00 20.55 ? 241 GLU A CD  1 
ATOM   2005  O  OE1 . GLU A  1 241 ? 17.301  12.935  -1.317  1.00 26.75 ? 241 GLU A OE1 1 
ATOM   2006  O  OE2 . GLU A  1 241 ? 18.913  14.225  -2.070  1.00 28.88 ? 241 GLU A OE2 1 
ATOM   2007  N  N   . MET A  1 242 ? 12.827  16.604  -2.071  1.00 6.40  ? 242 MET A N   1 
ATOM   2008  C  CA  . MET A  1 242 ? 11.448  16.249  -2.528  1.00 6.26  ? 242 MET A CA  1 
ATOM   2009  C  C   . MET A  1 242 ? 11.461  14.960  -3.351  1.00 6.27  ? 242 MET A C   1 
ATOM   2010  O  O   . MET A  1 242 ? 11.699  14.963  -4.571  1.00 6.38  ? 242 MET A O   1 
ATOM   2011  C  CB  . MET A  1 242 ? 10.850  17.434  -3.223  1.00 6.12  ? 242 MET A CB  1 
ATOM   2012  C  CG  . MET A  1 242 ? 9.347   17.207  -3.549  1.00 6.41  ? 242 MET A CG  1 
ATOM   2013  S  SD  . MET A  1 242 ? 8.602   18.516  -4.554  1.00 7.28  ? 242 MET A SD  1 
ATOM   2014  C  CE  . MET A  1 242 ? 8.863   19.932  -3.450  1.00 7.29  ? 242 MET A CE  1 
ATOM   2015  N  N   . ILE A  1 243 ? 11.335  13.876  -2.576  1.00 5.30  ? 243 ILE A N   1 
ATOM   2016  C  CA  . ILE A  1 243 ? 11.296  12.525  -3.067  1.00 6.06  ? 243 ILE A CA  1 
ATOM   2017  C  C   . ILE A  1 243 ? 10.121  11.734  -2.440  1.00 5.40  ? 243 ILE A C   1 
ATOM   2018  O  O   . ILE A  1 243 ? 9.646   12.048  -1.323  1.00 5.51  ? 243 ILE A O   1 
ATOM   2019  C  CB  . ILE A  1 243 ? 12.619  11.758  -2.801  1.00 6.24  ? 243 ILE A CB  1 
ATOM   2020  C  CG1 . ILE A  1 243 ? 12.963  11.743  -1.300  1.00 8.64  ? 243 ILE A CG1 1 
ATOM   2021  C  CG2 . ILE A  1 243 ? 13.749  12.374  -3.701  1.00 7.45  ? 243 ILE A CG2 1 
ATOM   2022  C  CD1 . ILE A  1 243 ? 14.299  10.965  -1.020  1.00 9.93  ? 243 ILE A CD1 1 
ATOM   2023  N  N   . ASN A  1 244 ? 9.731   10.669  -3.137  1.00 5.95  ? 244 ASN A N   1 
ATOM   2024  C  CA  . ASN A  1 244 ? 8.704   9.748   -2.551  1.00 5.04  ? 244 ASN A CA  1 
ATOM   2025  C  C   . ASN A  1 244 ? 7.461   10.539  -2.142  1.00 5.46  ? 244 ASN A C   1 
ATOM   2026  O  O   . ASN A  1 244 ? 6.857   10.208  -1.117  1.00 6.54  ? 244 ASN A O   1 
ATOM   2027  C  CB  . ASN A  1 244 ? 9.272   8.933   -1.356  1.00 5.25  ? 244 ASN A CB  1 
ATOM   2028  C  CG  . ASN A  1 244 ? 10.590  8.230   -1.764  1.00 6.15  ? 244 ASN A CG  1 
ATOM   2029  O  OD1 . ASN A  1 244 ? 10.648  7.740   -2.910  1.00 6.50  ? 244 ASN A OD1 1 
ATOM   2030  N  ND2 . ASN A  1 244 ? 11.635  8.186   -0.850  1.00 7.53  ? 244 ASN A ND2 1 
ATOM   2031  N  N   . ASN A  1 245 ? 7.042   11.471  -2.989  1.00 4.64  ? 245 ASN A N   1 
ATOM   2032  C  CA  . ASN A  1 245 ? 5.843   12.340  -2.584  1.00 3.71  ? 245 ASN A CA  1 
ATOM   2033  C  C   . ASN A  1 245 ? 4.599   11.724  -3.216  1.00 3.58  ? 245 ASN A C   1 
ATOM   2034  O  O   . ASN A  1 245 ? 3.868   12.360  -3.960  1.00 5.52  ? 245 ASN A O   1 
ATOM   2035  C  CB  . ASN A  1 245 ? 6.091   13.752  -3.096  1.00 4.50  ? 245 ASN A CB  1 
ATOM   2036  C  CG  . ASN A  1 245 ? 6.275   13.904  -4.575  1.00 4.84  ? 245 ASN A CG  1 
ATOM   2037  O  OD1 . ASN A  1 245 ? 6.644   12.949  -5.235  1.00 4.91  ? 245 ASN A OD1 1 
ATOM   2038  N  ND2 . ASN A  1 245 ? 6.107   15.136  -5.076  1.00 7.16  ? 245 ASN A ND2 1 
ATOM   2039  N  N   . PHE A  1 246 ? 4.357   10.472  -2.846  1.00 3.66  ? 246 PHE A N   1 
ATOM   2040  C  CA  . PHE A  1 246 ? 3.158   9.719   -3.299  1.00 5.88  ? 246 PHE A CA  1 
ATOM   2041  C  C   . PHE A  1 246 ? 2.579   9.057   -2.058  1.00 5.48  ? 246 PHE A C   1 
ATOM   2042  O  O   . PHE A  1 246 ? 3.334   8.658   -1.136  1.00 5.05  ? 246 PHE A O   1 
ATOM   2043  C  CB  . PHE A  1 246 ? 3.506   8.632   -4.374  1.00 6.09  ? 246 PHE A CB  1 
ATOM   2044  C  CG  . PHE A  1 246 ? 4.466   7.599   -3.854  1.00 4.42  ? 246 PHE A CG  1 
ATOM   2045  C  CD1 . PHE A  1 246 ? 3.998   6.329   -3.431  1.00 4.61  ? 246 PHE A CD1 1 
ATOM   2046  C  CD2 . PHE A  1 246 ? 5.802   7.781   -3.931  1.00 4.89  ? 246 PHE A CD2 1 
ATOM   2047  C  CE1 . PHE A  1 246 ? 4.819   5.331   -2.987  1.00 5.95  ? 246 PHE A CE1 1 
ATOM   2048  C  CE2 . PHE A  1 246 ? 6.712   6.765   -3.513  1.00 5.74  ? 246 PHE A CE2 1 
ATOM   2049  C  CZ  . PHE A  1 246 ? 6.187   5.548   -2.978  1.00 5.19  ? 246 PHE A CZ  1 
ATOM   2050  N  N   . ARG A  1 247 ? 1.276   8.840   -2.064  1.00 3.02  ? 247 ARG A N   1 
ATOM   2051  C  CA  . ARG A  1 247 ? 0.620   8.183   -0.919  1.00 3.02  ? 247 ARG A CA  1 
ATOM   2052  C  C   . ARG A  1 247 ? 0.536   6.629   -1.231  1.00 3.47  ? 247 ARG A C   1 
ATOM   2053  O  O   . ARG A  1 247 ? 0.347   6.266   -2.386  1.00 5.00  ? 247 ARG A O   1 
ATOM   2054  C  CB  . ARG A  1 247 ? -0.783  8.763   -0.726  1.00 4.13  ? 247 ARG A CB  1 
ATOM   2055  C  CG  . ARG A  1 247 ? -1.496  8.316   0.568   1.00 4.07  ? 247 ARG A CG  1 
ATOM   2056  C  CD  . ARG A  1 247 ? -2.939  8.843   0.616   1.00 4.05  ? 247 ARG A CD  1 
ATOM   2057  N  NE  . ARG A  1 247 ? -3.508  8.800   1.963   1.00 4.67  ? 247 ARG A NE  1 
ATOM   2058  C  CZ  . ARG A  1 247 ? -4.765  9.101   2.214   1.00 5.49  ? 247 ARG A CZ  1 
ATOM   2059  N  NH1 . ARG A  1 247 ? -5.664  9.373   1.224   1.00 5.58  ? 247 ARG A NH1 1 
ATOM   2060  N  NH2 . ARG A  1 247 ? -5.172  9.132   3.491   1.00 5.67  ? 247 ARG A NH2 1 
ATOM   2061  N  N   . GLN A  1 248 ? 0.681   5.800   -0.188  1.00 4.34  ? 248 GLN A N   1 
ATOM   2062  C  CA  . GLN A  1 248 ? 0.391   4.342   -0.346  1.00 4.82  ? 248 GLN A CA  1 
ATOM   2063  C  C   . GLN A  1 248 ? -1.060  4.150   -0.828  1.00 5.67  ? 248 GLN A C   1 
ATOM   2064  O  O   . GLN A  1 248 ? -1.982  4.960   -0.514  1.00 5.70  ? 248 GLN A O   1 
ATOM   2065  C  CB  . GLN A  1 248 ? 0.599   3.607   0.984   1.00 4.03  ? 248 GLN A CB  1 
ATOM   2066  C  CG  . GLN A  1 248 ? 2.047   3.665   1.493   1.00 4.90  ? 248 GLN A CG  1 
ATOM   2067  C  CD  . GLN A  1 248 ? 3.052   2.964   0.587   1.00 4.83  ? 248 GLN A CD  1 
ATOM   2068  O  OE1 . GLN A  1 248 ? 3.196   1.705   0.682   1.00 7.56  ? 248 GLN A OE1 1 
ATOM   2069  N  NE2 . GLN A  1 248 ? 3.707   3.671   -0.251  1.00 3.42  ? 248 GLN A NE2 1 
ATOM   2070  N  N   . VAL A  1 249 ? -1.258  3.051   -1.557  1.00 5.42  ? 249 VAL A N   1 
ATOM   2071  C  CA  . VAL A  1 249 ? -2.612  2.680   -1.916  1.00 6.45  ? 249 VAL A CA  1 
ATOM   2072  C  C   . VAL A  1 249 ? -3.508  2.381   -0.676  1.00 6.16  ? 249 VAL A C   1 
ATOM   2073  O  O   . VAL A  1 249 ? -2.995  1.939   0.358   1.00 6.05  ? 249 VAL A O   1 
ATOM   2074  C  CB  . VAL A  1 249 ? -2.683  1.527   -2.920  1.00 5.72  ? 249 VAL A CB  1 
ATOM   2075  C  CG1 . VAL A  1 249 ? -2.172  1.965   -4.311  1.00 5.62  ? 249 VAL A CG1 1 
ATOM   2076  C  CG2 . VAL A  1 249 ? -1.960  0.263   -2.423  1.00 7.47  ? 249 VAL A CG2 1 
ATOM   2077  N  N   . GLN A  1 250 ? -4.781  2.685   -0.799  1.00 4.94  ? 250 GLN A N   1 
ATOM   2078  C  CA  . GLN A  1 250 ? -5.765  2.540   0.251   1.00 4.78  ? 250 GLN A CA  1 
ATOM   2079  C  C   . GLN A  1 250 ? -6.593  1.259   0.107   1.00 5.76  ? 250 GLN A C   1 
ATOM   2080  O  O   . GLN A  1 250 ? -6.799  0.780   -1.000  1.00 6.75  ? 250 GLN A O   1 
ATOM   2081  C  CB  . GLN A  1 250 ? -6.663  3.781   0.229   1.00 4.80  ? 250 GLN A CB  1 
ATOM   2082  C  CG  . GLN A  1 250 ? -5.938  5.092   0.201   1.00 5.52  ? 250 GLN A CG  1 
ATOM   2083  C  CD  . GLN A  1 250 ? -5.240  5.352   1.523   1.00 4.44  ? 250 GLN A CD  1 
ATOM   2084  O  OE1 . GLN A  1 250 ? -5.936  5.612   2.530   1.00 6.19  ? 250 GLN A OE1 1 
ATOM   2085  N  NE2 . GLN A  1 250 ? -3.970  5.479   1.495   1.00 4.65  ? 250 GLN A NE2 1 
ATOM   2086  N  N   . LYS A  1 251 ? -7.166  0.809   1.235   1.00 5.31  ? 251 LYS A N   1 
ATOM   2087  C  CA  . LYS A  1 251 ? -8.211  -0.247  1.120   1.00 7.04  ? 251 LYS A CA  1 
ATOM   2088  C  C   . LYS A  1 251 ? -9.263  0.200   0.142   1.00 7.04  ? 251 LYS A C   1 
ATOM   2089  O  O   . LYS A  1 251 ? -9.681  1.376   0.142   1.00 8.62  ? 251 LYS A O   1 
ATOM   2090  C  CB  . LYS A  1 251 ? -8.878  -0.524  2.515   1.00 6.46  ? 251 LYS A CB  1 
ATOM   2091  C  CG  . LYS A  1 251 ? -7.955  -1.157  3.576   1.00 9.86  ? 251 LYS A CG  1 
ATOM   2092  C  CD  . LYS A  1 251 ? -7.806  -2.630  3.335   1.00 9.95  ? 251 LYS A CD  1 
ATOM   2093  C  CE  . LYS A  1 251 ? -7.142  -3.464  4.511   1.00 6.10  ? 251 LYS A CE  1 
ATOM   2094  N  NZ  . LYS A  1 251 ? -5.702  -2.968  4.666   1.00 5.32  ? 251 LYS A NZ  1 
ATOM   2095  N  N   . PHE A  1 252 ? -9.866  -0.787  -0.559  1.00 8.02  ? 252 PHE A N   1 
ATOM   2096  C  CA  . PHE A  1 252 ? -10.979 -0.462  -1.466  1.00 9.80  ? 252 PHE A CA  1 
ATOM   2097  C  C   . PHE A  1 252 ? -11.822 -1.744  -1.506  1.00 12.08 ? 252 PHE A C   1 
ATOM   2098  O  O   . PHE A  1 252 ? -11.528 -2.706  -2.245  1.00 12.05 ? 252 PHE A O   1 
ATOM   2099  C  CB  . PHE A  1 252 ? -10.440 -0.174  -2.914  1.00 10.35 ? 252 PHE A CB  1 
ATOM   2100  C  CG  . PHE A  1 252 ? -11.476 0.429   -3.823  1.00 9.85  ? 252 PHE A CG  1 
ATOM   2101  C  CD1 . PHE A  1 252 ? -11.788 1.767   -3.772  1.00 10.74 ? 252 PHE A CD1 1 
ATOM   2102  C  CD2 . PHE A  1 252 ? -12.093 -0.409  -4.822  1.00 12.22 ? 252 PHE A CD2 1 
ATOM   2103  C  CE1 . PHE A  1 252 ? -12.740 2.352   -4.631  1.00 15.05 ? 252 PHE A CE1 1 
ATOM   2104  C  CE2 . PHE A  1 252 ? -12.981 0.185   -5.712  1.00 12.91 ? 252 PHE A CE2 1 
ATOM   2105  C  CZ  . PHE A  1 252 ? -13.321 1.517   -5.617  1.00 14.48 ? 252 PHE A CZ  1 
ATOM   2106  N  N   . ASP A  1 253 ? -12.836 -1.749  -0.645  1.00 15.10 ? 253 ASP A N   1 
ATOM   2107  C  CA  . ASP A  1 253 ? -13.747 -2.932  -0.415  1.00 18.92 ? 253 ASP A CA  1 
ATOM   2108  C  C   . ASP A  1 253 ? -15.182 -2.620  -0.551  1.00 21.43 ? 253 ASP A C   1 
ATOM   2109  O  O   . ASP A  1 253 ? -15.531 -1.492  -0.280  1.00 21.72 ? 253 ASP A O   1 
ATOM   2110  C  CB  . ASP A  1 253 ? -13.532 -3.380  1.052   1.00 18.80 ? 253 ASP A CB  1 
ATOM   2111  C  CG  . ASP A  1 253 ? -12.084 -3.782  1.363   1.00 21.95 ? 253 ASP A CG  1 
ATOM   2112  O  OD1 . ASP A  1 253 ? -11.560 -4.664  0.655   1.00 24.14 ? 253 ASP A OD1 1 
ATOM   2113  O  OD2 . ASP A  1 253 ? -11.480 -3.250  2.327   1.00 23.17 ? 253 ASP A OD2 1 
ATOM   2114  N  N   A GLU A  1 254 ? -15.985 -3.605  -0.999  0.50 21.92 ? 254 GLU A N   1 
ATOM   2115  N  N   B GLU A  1 254 ? -16.053 -3.546  -0.974  0.50 23.05 ? 254 GLU A N   1 
ATOM   2116  C  CA  A GLU A  1 254 ? -17.461 -3.443  -1.248  0.50 21.85 ? 254 GLU A CA  1 
ATOM   2117  C  CA  B GLU A  1 254 ? -17.505 -3.179  -1.228  0.50 23.26 ? 254 GLU A CA  1 
ATOM   2118  C  C   A GLU A  1 254 ? -17.768 -2.516  -2.413  0.50 21.13 ? 254 GLU A C   1 
ATOM   2119  C  C   B GLU A  1 254 ? -17.617 -1.914  -2.145  0.50 23.59 ? 254 GLU A C   1 
ATOM   2120  O  O   A GLU A  1 254 ? -18.876 -2.014  -2.503  0.50 19.92 ? 254 GLU A O   1 
ATOM   2121  O  O   B GLU A  1 254 ? -18.414 -0.975  -1.919  0.50 25.81 ? 254 GLU A O   1 
ATOM   2122  C  CB  A GLU A  1 254 ? -18.187 -2.864  -0.030  0.50 23.56 ? 254 GLU A CB  1 
ATOM   2123  C  CB  B GLU A  1 254 ? -18.316 -3.087  0.099   0.50 25.32 ? 254 GLU A CB  1 
ATOM   2124  C  CG  A GLU A  1 254 ? -18.069 -3.633  1.269   0.50 24.40 ? 254 GLU A CG  1 
ATOM   2125  C  CG  B GLU A  1 254 ? -18.178 -1.758  0.896   0.50 27.16 ? 254 GLU A CG  1 
ATOM   2126  C  CD  A GLU A  1 254 ? -19.344 -3.546  2.053   0.50 29.45 ? 254 GLU A CD  1 
ATOM   2127  C  CD  B GLU A  1 254 ? -18.000 -1.931  2.424   0.50 30.61 ? 254 GLU A CD  1 
ATOM   2128  O  OE1 A GLU A  1 254 ? -19.734 -2.421  2.476   0.50 28.35 ? 254 GLU A OE1 1 
ATOM   2129  O  OE1 B GLU A  1 254 ? -16.843 -1.872  2.909   0.50 26.29 ? 254 GLU A OE1 1 
ATOM   2130  O  OE2 A GLU A  1 254 ? -19.970 -4.610  2.216   0.50 32.18 ? 254 GLU A OE2 1 
ATOM   2131  O  OE2 B GLU A  1 254 ? -19.017 -2.073  3.142   0.50 32.32 ? 254 GLU A OE2 1 
ATOM   2132  N  N   A ARG A  1 255 ? -16.775 -2.261  -3.255  0.50 21.11 ? 255 ARG A N   1 
ATOM   2133  N  N   B ARG A  1 255 ? -16.787 -1.912  -3.186  0.50 23.87 ? 255 ARG A N   1 
ATOM   2134  C  CA  A ARG A  1 255 ? -16.890 -1.210  -4.300  0.50 19.96 ? 255 ARG A CA  1 
ATOM   2135  C  CA  B ARG A  1 255 ? -16.721 -0.801  -4.179  0.50 22.61 ? 255 ARG A CA  1 
ATOM   2136  C  C   A ARG A  1 255 ? -16.236 -1.565  -5.589  0.50 19.94 ? 255 ARG A C   1 
ATOM   2137  C  C   B ARG A  1 255 ? -16.066 -1.270  -5.466  0.50 20.87 ? 255 ARG A C   1 
ATOM   2138  O  O   A ARG A  1 255 ? -15.468 -2.540  -5.637  0.50 17.75 ? 255 ARG A O   1 
ATOM   2139  O  O   B ARG A  1 255 ? -15.156 -2.078  -5.369  0.50 16.48 ? 255 ARG A O   1 
ATOM   2140  C  CB  A ARG A  1 255 ? -16.224 0.106   -3.801  0.50 19.25 ? 255 ARG A CB  1 
ATOM   2141  C  CB  B ARG A  1 255 ? -15.962 0.379   -3.629  0.50 22.61 ? 255 ARG A CB  1 
ATOM   2142  C  CG  A ARG A  1 255 ? -16.902 0.750   -2.558  0.50 19.95 ? 255 ARG A CG  1 
ATOM   2143  C  CG  B ARG A  1 255 ? -16.471 0.714   -2.224  0.50 25.82 ? 255 ARG A CG  1 
ATOM   2144  C  CD  A ARG A  1 255 ? -16.100 2.033   -2.147  0.50 16.45 ? 255 ARG A CD  1 
ATOM   2145  C  CD  B ARG A  1 255 ? -15.364 1.310   -1.406  0.50 22.23 ? 255 ARG A CD  1 
ATOM   2146  N  NE  A ARG A  1 255 ? -16.310 2.964   -3.221  0.50 19.58 ? 255 ARG A NE  1 
ATOM   2147  N  NE  B ARG A  1 255 ? -14.779 2.474   -2.065  0.50 23.62 ? 255 ARG A NE  1 
ATOM   2148  C  CZ  A ARG A  1 255 ? -15.487 3.945   -3.524  0.50 14.38 ? 255 ARG A CZ  1 
ATOM   2149  C  CZ  B ARG A  1 255 ? -13.799 3.207   -1.552  0.50 14.30 ? 255 ARG A CZ  1 
ATOM   2150  N  NH1 A ARG A  1 255 ? -14.384 4.151   -2.815  0.50 12.04 ? 255 ARG A NH1 1 
ATOM   2151  N  NH1 B ARG A  1 255 ? -13.288 2.899   -0.367  0.50 8.54  ? 255 ARG A NH1 1 
ATOM   2152  N  NH2 A ARG A  1 255 ? -15.777 4.725   -4.545  0.50 3.80  ? 255 ARG A NH2 1 
ATOM   2153  N  NH2 B ARG A  1 255 ? -13.328 4.250   -2.222  0.50 21.26 ? 255 ARG A NH2 1 
ATOM   2154  N  N   . LEU A  1 256 ? -16.554 -0.746  -6.631  1.00 19.94 ? 256 LEU A N   1 
ATOM   2155  C  CA  . LEU A  1 256 ? -16.070 -0.975  -7.938  1.00 16.47 ? 256 LEU A CA  1 
ATOM   2156  C  C   . LEU A  1 256 ? -15.486 0.323   -8.636  1.00 11.92 ? 256 LEU A C   1 
ATOM   2157  O  O   . LEU A  1 256 ? -15.827 1.501   -8.354  1.00 13.94 ? 256 LEU A O   1 
ATOM   2158  C  CB  . LEU A  1 256 ? -17.149 -1.610  -8.910  1.00 19.71 ? 256 LEU A CB  1 
ATOM   2159  C  CG  . LEU A  1 256 ? -17.746 -2.962  -8.485  1.00 21.73 ? 256 LEU A CG  1 
ATOM   2160  C  CD1 . LEU A  1 256 ? -19.098 -3.049  -9.311  1.00 25.18 ? 256 LEU A CD1 1 
ATOM   2161  C  CD2 . LEU A  1 256 ? -16.833 -4.259  -8.681  1.00 22.45 ? 256 LEU A CD2 1 
ATOM   2162  N  N   . VAL A  1 257 ? -14.464 -0.037  -9.349  1.00 11.12 ? 257 VAL A N   1 
ATOM   2163  C  CA  . VAL A  1 257 ? -13.895 0.875   -10.341 1.00 10.22 ? 257 VAL A CA  1 
ATOM   2164  C  C   . VAL A  1 257 ? -14.496 0.548   -11.690 1.00 10.80 ? 257 VAL A C   1 
ATOM   2165  O  O   . VAL A  1 257 ? -14.517 -0.640  -12.039 1.00 11.95 ? 257 VAL A O   1 
ATOM   2166  C  CB  . VAL A  1 257 ? -12.406 0.707   -10.368 1.00 9.12  ? 257 VAL A CB  1 
ATOM   2167  C  CG1 . VAL A  1 257 ? -11.830 1.563   -11.488 1.00 10.22 ? 257 VAL A CG1 1 
ATOM   2168  C  CG2 . VAL A  1 257 ? -11.783 1.114   -9.006  1.00 11.95 ? 257 VAL A CG2 1 
ATOM   2169  N  N   . TYR A  1 258 ? -14.963 1.563   -12.412 1.00 8.22  ? 258 TYR A N   1 
ATOM   2170  C  CA  . TYR A  1 258 ? -15.642 1.318   -13.761 1.00 8.04  ? 258 TYR A CA  1 
ATOM   2171  C  C   . TYR A  1 258 ? -14.608 1.538   -14.819 1.00 8.23  ? 258 TYR A C   1 
ATOM   2172  O  O   . TYR A  1 258 ? -13.849 2.505   -14.779 1.00 9.85  ? 258 TYR A O   1 
ATOM   2173  C  CB  . TYR A  1 258 ? -16.879 2.157   -13.878 1.00 10.18 ? 258 TYR A CB  1 
ATOM   2174  C  CG  . TYR A  1 258 ? -17.818 1.825   -12.784 1.00 12.25 ? 258 TYR A CG  1 
ATOM   2175  C  CD1 . TYR A  1 258 ? -17.783 2.528   -11.585 1.00 12.85 ? 258 TYR A CD1 1 
ATOM   2176  C  CD2 . TYR A  1 258 ? -18.634 0.704   -12.906 1.00 16.13 ? 258 TYR A CD2 1 
ATOM   2177  C  CE1 . TYR A  1 258 ? -18.717 2.196   -10.523 1.00 16.76 ? 258 TYR A CE1 1 
ATOM   2178  C  CE2 . TYR A  1 258 ? -19.550 0.348   -11.862 1.00 19.90 ? 258 TYR A CE2 1 
ATOM   2179  C  CZ  . TYR A  1 258 ? -19.526 1.060   -10.715 1.00 18.33 ? 258 TYR A CZ  1 
ATOM   2180  O  OH  . TYR A  1 258 ? -20.405 0.722   -9.705  1.00 22.93 ? 258 TYR A OH  1 
ATOM   2181  N  N   . THR A  1 259 ? -14.562 0.720   -15.838 1.00 7.83  ? 259 THR A N   1 
ATOM   2182  C  CA  . THR A  1 259 ? -13.615 0.875   -16.936 1.00 6.95  ? 259 THR A CA  1 
ATOM   2183  C  C   . THR A  1 259 ? -14.354 1.209   -18.259 1.00 7.10  ? 259 THR A C   1 
ATOM   2184  O  O   . THR A  1 259 ? -15.474 0.674   -18.489 1.00 7.78  ? 259 THR A O   1 
ATOM   2185  C  CB  . THR A  1 259 ? -12.726 -0.321  -17.182 1.00 7.26  ? 259 THR A CB  1 
ATOM   2186  O  OG1 . THR A  1 259 ? -13.550 -1.500  -17.431 1.00 8.60  ? 259 THR A OG1 1 
ATOM   2187  C  CG2 . THR A  1 259 ? -11.882 -0.626  -15.942 1.00 10.30 ? 259 THR A CG2 1 
ATOM   2188  N  N   . SER A  1 260 ? -13.781 1.991   -19.190 1.00 6.39  ? 260 SER A N   1 
ATOM   2189  C  CA  . SER A  1 260 ? -14.449 2.393   -20.439 1.00 6.83  ? 260 SER A CA  1 
ATOM   2190  C  C   . SER A  1 260 ? -13.917 1.448   -21.513 1.00 9.90  ? 260 SER A C   1 
ATOM   2191  O  O   . SER A  1 260 ? -14.359 1.570   -22.631 1.00 12.52 ? 260 SER A O   1 
ATOM   2192  C  CB  . SER A  1 260 ? -14.113 3.784   -20.804 1.00 7.41  ? 260 SER A CB  1 
ATOM   2193  O  OG  . SER A  1 260 ? -12.698 3.926   -20.991 1.00 7.31  ? 260 SER A OG  1 
ATOM   2194  N  N   . PHE A  1 261 ? -13.039 0.536   -21.157 1.00 8.20  ? 261 PHE A N   1 
ATOM   2195  C  CA  . PHE A  1 261 ? -12.464 -0.467  -21.998 1.00 9.19  ? 261 PHE A CA  1 
ATOM   2196  C  C   . PHE A  1 261 ? -12.851 -1.847  -21.476 1.00 9.37  ? 261 PHE A C   1 
ATOM   2197  O  O   . PHE A  1 261 ? -13.126 -2.003  -20.248 1.00 9.06  ? 261 PHE A O   1 
ATOM   2198  C  CB  . PHE A  1 261 ? -10.919 -0.305  -22.141 1.00 9.08  ? 261 PHE A CB  1 
ATOM   2199  C  CG  . PHE A  1 261 ? -10.159 -0.460  -20.820 1.00 7.78  ? 261 PHE A CG  1 
ATOM   2200  C  CD1 . PHE A  1 261 ? -9.654  -1.674  -20.422 1.00 10.36 ? 261 PHE A CD1 1 
ATOM   2201  C  CD2 . PHE A  1 261 ? -10.022 0.701   -20.011 1.00 9.01  ? 261 PHE A CD2 1 
ATOM   2202  C  CE1 . PHE A  1 261 ? -8.994  -1.824  -19.181 1.00 9.65  ? 261 PHE A CE1 1 
ATOM   2203  C  CE2 . PHE A  1 261 ? -9.387  0.600   -18.799 1.00 9.03  ? 261 PHE A CE2 1 
ATOM   2204  C  CZ  . PHE A  1 261 ? -8.799  -0.647  -18.410 1.00 9.96  ? 261 PHE A CZ  1 
ATOM   2205  N  N   . SER A  1 262 ? -12.791 -2.865  -22.345 1.00 12.30 ? 262 SER A N   1 
ATOM   2206  C  CA  . SER A  1 262 ? -13.292 -4.175  -21.832 1.00 12.96 ? 262 SER A CA  1 
ATOM   2207  C  C   . SER A  1 262 ? -12.004 -5.023  -21.744 1.00 16.06 ? 262 SER A C   1 
ATOM   2208  O  O   . SER A  1 262 ? -11.021 -4.749  -22.398 1.00 18.58 ? 262 SER A O   1 
ATOM   2209  C  CB  . SER A  1 262 ? -14.417 -4.831  -22.711 1.00 14.41 ? 262 SER A CB  1 
ATOM   2210  O  OG  . SER A  1 262 ? -13.881 -5.230  -23.939 1.00 14.52 ? 262 SER A OG  1 
ATOM   2211  N  N   . GLN A  1 263 ? -12.070 -6.108  -20.968 1.00 19.89 ? 263 GLN A N   1 
ATOM   2212  C  CA  . GLN A  1 263 ? -10.874 -6.928  -20.720 1.00 23.40 ? 263 GLN A CA  1 
ATOM   2213  C  C   . GLN A  1 263 ? -11.224 -8.428  -20.939 1.00 22.10 ? 263 GLN A C   1 
ATOM   2214  O  O   . GLN A  1 263 ? -12.438 -8.720  -21.146 1.00 18.12 ? 263 GLN A O   1 
ATOM   2215  C  CB  . GLN A  1 263 ? -10.433 -6.725  -19.263 1.00 23.75 ? 263 GLN A CB  1 
ATOM   2216  C  CG  . GLN A  1 263 ? -10.073 -5.248  -19.001 1.00 28.64 ? 263 GLN A CG  1 
ATOM   2217  C  CD  . GLN A  1 263 ? -9.615  -4.960  -17.543 1.00 27.18 ? 263 GLN A CD  1 
ATOM   2218  O  OE1 . GLN A  1 263 ? -10.430 -5.024  -16.610 1.00 33.96 ? 263 GLN A OE1 1 
ATOM   2219  N  NE2 . GLN A  1 263 ? -8.307  -4.654  -17.353 1.00 32.55 ? 263 GLN A NE2 1 
ATOM   2220  O  OXT . GLN A  1 263 ? -10.353 -9.330  -20.872 1.00 22.49 ? 263 GLN A OXT 1 
ATOM   2221  N  N   . LYS B  1 3   ? -12.719 0.964   19.691  1.00 27.15 ? 3   LYS B N   1 
ATOM   2222  C  CA  . LYS B  1 3   ? -11.458 0.167   19.686  1.00 26.98 ? 3   LYS B CA  1 
ATOM   2223  C  C   . LYS B  1 3   ? -11.072 0.057   18.205  1.00 24.20 ? 3   LYS B C   1 
ATOM   2224  O  O   . LYS B  1 3   ? -11.977 0.190   17.304  1.00 25.23 ? 3   LYS B O   1 
ATOM   2225  C  CB  . LYS B  1 3   ? -11.622 -1.224  20.297  1.00 31.31 ? 3   LYS B CB  1 
ATOM   2226  C  CG  . LYS B  1 3   ? -10.249 -1.836  20.740  1.00 34.00 ? 3   LYS B CG  1 
ATOM   2227  C  CD  . LYS B  1 3   ? -10.085 -3.309  20.355  1.00 37.16 ? 3   LYS B CD  1 
ATOM   2228  C  CE  . LYS B  1 3   ? -8.824  -3.891  21.054  1.00 40.68 ? 3   LYS B CE  1 
ATOM   2229  N  NZ  . LYS B  1 3   ? -8.957  -3.971  22.561  1.00 45.16 ? 3   LYS B NZ  1 
ATOM   2230  N  N   . TRP B  1 4   ? -9.770  -0.209  17.983  1.00 16.52 ? 4   TRP B N   1 
ATOM   2231  C  CA  . TRP B  1 4   ? -9.212  -0.165  16.629  1.00 13.28 ? 4   TRP B CA  1 
ATOM   2232  C  C   . TRP B  1 4   ? -9.793  -1.295  15.771  1.00 11.71 ? 4   TRP B C   1 
ATOM   2233  O  O   . TRP B  1 4   ? -10.190 -2.378  16.283  1.00 12.26 ? 4   TRP B O   1 
ATOM   2234  C  CB  . TRP B  1 4   ? -7.675  -0.203  16.654  1.00 12.48 ? 4   TRP B CB  1 
ATOM   2235  C  CG  . TRP B  1 4   ? -7.084  -1.492  17.147  1.00 11.95 ? 4   TRP B CG  1 
ATOM   2236  C  CD1 . TRP B  1 4   ? -6.705  -1.824  18.459  1.00 10.93 ? 4   TRP B CD1 1 
ATOM   2237  C  CD2 . TRP B  1 4   ? -6.741  -2.662  16.358  1.00 9.63  ? 4   TRP B CD2 1 
ATOM   2238  N  NE1 . TRP B  1 4   ? -6.179  -3.081  18.479  1.00 10.95 ? 4   TRP B NE1 1 
ATOM   2239  C  CE2 . TRP B  1 4   ? -6.218  -3.639  17.227  1.00 8.96  ? 4   TRP B CE2 1 
ATOM   2240  C  CE3 . TRP B  1 4   ? -6.809  -2.969  14.991  1.00 8.73  ? 4   TRP B CE3 1 
ATOM   2241  C  CZ2 . TRP B  1 4   ? -5.693  -4.894  16.739  1.00 8.55  ? 4   TRP B CZ2 1 
ATOM   2242  C  CZ3 . TRP B  1 4   ? -6.406  -4.179  14.544  1.00 9.06  ? 4   TRP B CZ3 1 
ATOM   2243  C  CH2 . TRP B  1 4   ? -5.841  -5.107  15.383  1.00 8.86  ? 4   TRP B CH2 1 
ATOM   2244  N  N   . THR B  1 5   ? -9.882  -0.998  14.460  1.00 11.90 ? 5   THR B N   1 
ATOM   2245  C  CA  . THR B  1 5   ? -10.427 -1.908  13.478  1.00 9.92  ? 5   THR B CA  1 
ATOM   2246  C  C   . THR B  1 5   ? -9.630  -1.828  12.208  1.00 10.00 ? 5   THR B C   1 
ATOM   2247  O  O   . THR B  1 5   ? -8.673  -0.997  12.106  1.00 9.35  ? 5   THR B O   1 
ATOM   2248  C  CB  . THR B  1 5   ? -11.890 -1.496  13.070  1.00 11.99 ? 5   THR B CB  1 
ATOM   2249  O  OG1 . THR B  1 5   ? -11.837 -0.259  12.303  1.00 12.67 ? 5   THR B OG1 1 
ATOM   2250  C  CG2 . THR B  1 5   ? -12.797 -1.370  14.289  1.00 13.23 ? 5   THR B CG2 1 
ATOM   2251  N  N   . TYR B  1 6   ? -9.997  -2.584  11.174  1.00 9.47  ? 6   TYR B N   1 
ATOM   2252  C  CA  . TYR B  1 6   ? -9.463  -2.392  9.765   1.00 10.54 ? 6   TYR B CA  1 
ATOM   2253  C  C   . TYR B  1 6   ? -10.399 -1.714  8.769   1.00 11.77 ? 6   TYR B C   1 
ATOM   2254  O  O   . TYR B  1 6   ? -10.169 -1.651  7.548   1.00 11.90 ? 6   TYR B O   1 
ATOM   2255  C  CB  . TYR B  1 6   ? -9.152  -3.813  9.194   1.00 9.30  ? 6   TYR B CB  1 
ATOM   2256  C  CG  . TYR B  1 6   ? -8.011  -4.534  9.932   1.00 6.56  ? 6   TYR B CG  1 
ATOM   2257  C  CD1 . TYR B  1 6   ? -8.217  -5.408  11.005  1.00 5.31  ? 6   TYR B CD1 1 
ATOM   2258  C  CD2 . TYR B  1 6   ? -6.701  -4.362  9.479   1.00 7.67  ? 6   TYR B CD2 1 
ATOM   2259  C  CE1 . TYR B  1 6   ? -7.214  -6.172  11.553  1.00 7.86  ? 6   TYR B CE1 1 
ATOM   2260  C  CE2 . TYR B  1 6   ? -5.648  -5.061  10.040  1.00 8.09  ? 6   TYR B CE2 1 
ATOM   2261  C  CZ  . TYR B  1 6   ? -5.877  -6.004  11.070  1.00 5.86  ? 6   TYR B CZ  1 
ATOM   2262  O  OH  . TYR B  1 6   ? -4.883  -6.729  11.622  1.00 8.01  ? 6   TYR B OH  1 
ATOM   2263  N  N   . PHE B  1 7   ? -11.495 -1.148  9.292   1.00 11.85 ? 7   PHE B N   1 
ATOM   2264  C  CA  . PHE B  1 7   ? -12.467 -0.562  8.393   1.00 16.66 ? 7   PHE B CA  1 
ATOM   2265  C  C   . PHE B  1 7   ? -13.181 0.520   9.124   1.00 18.04 ? 7   PHE B C   1 
ATOM   2266  O  O   . PHE B  1 7   ? -13.695 0.258   10.243  1.00 17.72 ? 7   PHE B O   1 
ATOM   2267  C  CB  . PHE B  1 7   ? -13.498 -1.622  7.979   1.00 18.76 ? 7   PHE B CB  1 
ATOM   2268  C  CG  . PHE B  1 7   ? -14.607 -1.072  7.120   1.00 25.87 ? 7   PHE B CG  1 
ATOM   2269  C  CD1 . PHE B  1 7   ? -14.432 -0.863  5.736   1.00 29.23 ? 7   PHE B CD1 1 
ATOM   2270  C  CD2 . PHE B  1 7   ? -15.853 -0.703  7.720   1.00 32.70 ? 7   PHE B CD2 1 
ATOM   2271  C  CE1 . PHE B  1 7   ? -15.464 -0.330  4.956   1.00 32.68 ? 7   PHE B CE1 1 
ATOM   2272  C  CE2 . PHE B  1 7   ? -16.892 -0.163  6.944   1.00 33.60 ? 7   PHE B CE2 1 
ATOM   2273  C  CZ  . PHE B  1 7   ? -16.698 -0.006  5.559   1.00 32.90 ? 7   PHE B CZ  1 
ATOM   2274  N  N   . GLY B  1 8   ? -13.323 1.669   8.462   1.00 20.96 ? 8   GLY B N   1 
ATOM   2275  C  CA  . GLY B  1 8   ? -14.214 2.713   8.989   1.00 18.83 ? 8   GLY B CA  1 
ATOM   2276  C  C   . GLY B  1 8   ? -13.405 3.695   9.858   1.00 22.82 ? 8   GLY B C   1 
ATOM   2277  O  O   . GLY B  1 8   ? -12.139 3.778   9.732   1.00 19.71 ? 8   GLY B O   1 
ATOM   2278  N  N   . PRO B  1 9   ? -14.085 4.487   10.717  1.00 21.34 ? 9   PRO B N   1 
ATOM   2279  C  CA  . PRO B  1 9   ? -13.453 5.588   11.451  1.00 20.92 ? 9   PRO B CA  1 
ATOM   2280  C  C   . PRO B  1 9   ? -12.198 5.222   12.222  1.00 19.27 ? 9   PRO B C   1 
ATOM   2281  O  O   . PRO B  1 9   ? -11.326 6.083   12.482  1.00 17.68 ? 9   PRO B O   1 
ATOM   2282  C  CB  . PRO B  1 9   ? -14.576 6.093   12.448  1.00 21.79 ? 9   PRO B CB  1 
ATOM   2283  C  CG  . PRO B  1 9   ? -15.753 5.187   12.257  1.00 24.09 ? 9   PRO B CG  1 
ATOM   2284  C  CD  . PRO B  1 9   ? -15.552 4.432   10.953  1.00 23.52 ? 9   PRO B CD  1 
ATOM   2285  N  N   . ASP B  1 10  ? -12.153 3.994   12.697  1.00 17.51 ? 10  ASP B N   1 
ATOM   2286  C  CA  . ASP B  1 10  ? -11.117 3.559   13.626  1.00 15.62 ? 10  ASP B CA  1 
ATOM   2287  C  C   . ASP B  1 10  ? -10.118 2.633   12.907  1.00 11.31 ? 10  ASP B C   1 
ATOM   2288  O  O   . ASP B  1 10  ? -9.313  1.945   13.579  1.00 13.85 ? 10  ASP B O   1 
ATOM   2289  C  CB  . ASP B  1 10  ? -11.727 2.855   14.863  1.00 18.13 ? 10  ASP B CB  1 
ATOM   2290  C  CG  . ASP B  1 10  ? -12.672 3.776   15.610  1.00 23.35 ? 10  ASP B CG  1 
ATOM   2291  O  OD1 . ASP B  1 10  ? -12.272 4.929   15.905  1.00 27.80 ? 10  ASP B OD1 1 
ATOM   2292  O  OD2 . ASP B  1 10  ? -13.827 3.332   15.840  1.00 28.26 ? 10  ASP B OD2 1 
ATOM   2293  N  N   . GLY B  1 11  ? -10.176 2.688   11.584  1.00 11.31 ? 11  GLY B N   1 
ATOM   2294  C  CA  . GLY B  1 11  ? -9.296  1.873   10.708  1.00 8.17  ? 11  GLY B CA  1 
ATOM   2295  C  C   . GLY B  1 11  ? -7.857  2.401   10.623  1.00 6.72  ? 11  GLY B C   1 
ATOM   2296  O  O   . GLY B  1 11  ? -7.449  3.337   11.382  1.00 7.32  ? 11  GLY B O   1 
ATOM   2297  N  N   . GLU B  1 12  ? -7.068  1.764   9.784   1.00 7.08  ? 12  GLU B N   1 
ATOM   2298  C  CA  . GLU B  1 12  ? -5.611  1.867   9.922   1.00 5.76  ? 12  GLU B CA  1 
ATOM   2299  C  C   . GLU B  1 12  ? -5.041  3.264   9.739   1.00 6.45  ? 12  GLU B C   1 
ATOM   2300  O  O   . GLU B  1 12  ? -3.975  3.535   10.347  1.00 5.32  ? 12  GLU B O   1 
ATOM   2301  C  CB  . GLU B  1 12  ? -4.875  0.879   8.986   1.00 5.30  ? 12  GLU B CB  1 
ATOM   2302  C  CG  . GLU B  1 12  ? -4.978  1.238   7.506   1.00 5.31  ? 12  GLU B CG  1 
ATOM   2303  C  CD  . GLU B  1 12  ? -4.600  0.034   6.689   1.00 4.96  ? 12  GLU B CD  1 
ATOM   2304  O  OE1 . GLU B  1 12  ? -3.431  -0.217  6.422   1.00 5.41  ? 12  GLU B OE1 1 
ATOM   2305  O  OE2 . GLU B  1 12  ? -5.565  -0.677  6.235   1.00 6.79  ? 12  GLU B OE2 1 
ATOM   2306  N  N   . ASN B  1 13  ? -5.660  4.179   8.994   1.00 4.29  ? 13  ASN B N   1 
ATOM   2307  C  CA  . ASN B  1 13  ? -5.073  5.539   8.876   1.00 5.29  ? 13  ASN B CA  1 
ATOM   2308  C  C   . ASN B  1 13  ? -5.265  6.306   10.224  1.00 6.71  ? 13  ASN B C   1 
ATOM   2309  O  O   . ASN B  1 13  ? -4.596  7.388   10.320  1.00 6.83  ? 13  ASN B O   1 
ATOM   2310  C  CB  . ASN B  1 13  ? -5.699  6.325   7.697   1.00 6.38  ? 13  ASN B CB  1 
ATOM   2311  C  CG  . ASN B  1 13  ? -5.274  5.779   6.357   1.00 5.72  ? 13  ASN B CG  1 
ATOM   2312  O  OD1 . ASN B  1 13  ? -4.392  4.912   6.263   1.00 6.21  ? 13  ASN B OD1 1 
ATOM   2313  N  ND2 . ASN B  1 13  ? -5.917  6.318   5.312   1.00 6.06  ? 13  ASN B ND2 1 
ATOM   2314  N  N   . SER B  1 14  ? -6.159  5.823   11.105  1.00 5.60  ? 14  SER B N   1 
ATOM   2315  C  CA  . SER B  1 14  ? -6.369  6.512   12.409  1.00 5.98  ? 14  SER B CA  1 
ATOM   2316  C  C   . SER B  1 14  ? -5.660  5.839   13.555  1.00 7.54  ? 14  SER B C   1 
ATOM   2317  O  O   . SER B  1 14  ? -5.641  6.330   14.672  1.00 8.46  ? 14  SER B O   1 
ATOM   2318  C  CB  . SER B  1 14  ? -7.826  6.628   12.720  1.00 7.23  ? 14  SER B CB  1 
ATOM   2319  O  OG  . SER B  1 14  ? -8.452  7.551   11.822  1.00 8.28  ? 14  SER B OG  1 
ATOM   2320  N  N   . TRP B  1 15  ? -5.023  4.678   13.362  1.00 5.67  ? 15  TRP B N   1 
ATOM   2321  C  CA  . TRP B  1 15  ? -4.356  3.963   14.482  1.00 7.21  ? 15  TRP B CA  1 
ATOM   2322  C  C   . TRP B  1 15  ? -3.295  4.874   15.158  1.00 8.37  ? 15  TRP B C   1 
ATOM   2323  O  O   . TRP B  1 15  ? -3.182  4.743   16.401  1.00 8.20  ? 15  TRP B O   1 
ATOM   2324  C  CB  . TRP B  1 15  ? -3.612  2.762   13.943  1.00 6.81  ? 15  TRP B CB  1 
ATOM   2325  C  CG  . TRP B  1 15  ? -4.441  1.636   13.439  1.00 6.16  ? 15  TRP B CG  1 
ATOM   2326  C  CD1 . TRP B  1 15  ? -5.820  1.511   13.537  1.00 7.48  ? 15  TRP B CD1 1 
ATOM   2327  C  CD2 . TRP B  1 15  ? -3.945  0.463   12.822  1.00 4.77  ? 15  TRP B CD2 1 
ATOM   2328  N  NE1 . TRP B  1 15  ? -6.184  0.287   12.978  1.00 5.74  ? 15  TRP B NE1 1 
ATOM   2329  C  CE2 . TRP B  1 15  ? -5.069  -0.375  12.523  1.00 5.37  ? 15  TRP B CE2 1 
ATOM   2330  C  CE3 . TRP B  1 15  ? -2.660  -0.019  12.482  1.00 5.40  ? 15  TRP B CE3 1 
ATOM   2331  C  CZ2 . TRP B  1 15  ? -4.944  -1.661  11.873  1.00 5.96  ? 15  TRP B CZ2 1 
ATOM   2332  C  CZ3 . TRP B  1 15  ? -2.553  -1.315  11.852  1.00 6.16  ? 15  TRP B CZ3 1 
ATOM   2333  C  CH2 . TRP B  1 15  ? -3.694  -2.118  11.565  1.00 5.58  ? 15  TRP B CH2 1 
ATOM   2334  N  N   . SER B  1 16  ? -2.640  5.785   14.435  1.00 7.70  ? 16  SER B N   1 
ATOM   2335  C  CA  . SER B  1 16  ? -1.516  6.615   15.054  1.00 7.61  ? 16  SER B CA  1 
ATOM   2336  C  C   . SER B  1 16  ? -2.130  7.547   16.090  1.00 8.18  ? 16  SER B C   1 
ATOM   2337  O  O   . SER B  1 16  ? -1.322  8.105   16.909  1.00 9.52  ? 16  SER B O   1 
ATOM   2338  C  CB  . SER B  1 16  ? -0.819  7.435   13.950  1.00 8.58  ? 16  SER B CB  1 
ATOM   2339  O  OG  . SER B  1 16  ? -1.735  8.337   13.358  1.00 7.74  ? 16  SER B OG  1 
ATOM   2340  N  N   . LYS B  1 17  ? -3.425  7.753   16.101  1.00 7.83  ? 17  LYS B N   1 
ATOM   2341  C  CA  . LYS B  1 17  ? -3.970  8.783   17.129  1.00 9.60  ? 17  LYS B CA  1 
ATOM   2342  C  C   . LYS B  1 17  ? -3.740  8.173   18.516  1.00 12.00 ? 17  LYS B C   1 
ATOM   2343  O  O   . LYS B  1 17  ? -3.159  8.808   19.452  1.00 13.76 ? 17  LYS B O   1 
ATOM   2344  C  CB  . LYS B  1 17  ? -5.453  9.017   16.876  1.00 11.02 ? 17  LYS B CB  1 
ATOM   2345  C  CG  . LYS B  1 17  ? -5.739  9.673   15.567  1.00 10.92 ? 17  LYS B CG  1 
ATOM   2346  C  CD  . LYS B  1 17  ? -7.220  9.535   15.141  1.00 9.06  ? 17  LYS B CD  1 
ATOM   2347  C  CE  . LYS B  1 17  ? -7.589  10.173  13.763  1.00 7.94  ? 17  LYS B CE  1 
ATOM   2348  N  NZ  . LYS B  1 17  ? -9.066  10.342  13.590  1.00 8.65  ? 17  LYS B NZ  1 
ATOM   2349  N  N   . LYS B  1 18  ? -4.189  6.953   18.733  1.00 10.13 ? 18  LYS B N   1 
ATOM   2350  C  CA  . LYS B  1 18  ? -4.088  6.307   20.068  1.00 11.14 ? 18  LYS B CA  1 
ATOM   2351  C  C   . LYS B  1 18  ? -2.845  5.511   20.234  1.00 11.95 ? 18  LYS B C   1 
ATOM   2352  O  O   . LYS B  1 18  ? -2.389  5.249   21.392  1.00 12.50 ? 18  LYS B O   1 
ATOM   2353  C  CB  . LYS B  1 18  ? -5.286  5.384   20.396  1.00 11.96 ? 18  LYS B CB  1 
ATOM   2354  C  CG  . LYS B  1 18  ? -6.558  6.175   20.439  1.00 20.31 ? 18  LYS B CG  1 
ATOM   2355  C  CD  . LYS B  1 18  ? -7.563  5.590   21.476  1.00 26.72 ? 18  LYS B CD  1 
ATOM   2356  C  CE  . LYS B  1 18  ? -8.758  6.573   21.764  1.00 26.84 ? 18  LYS B CE  1 
ATOM   2357  N  NZ  . LYS B  1 18  ? -8.289  7.816   22.546  1.00 21.56 ? 18  LYS B NZ  1 
ATOM   2358  N  N   . TYR B  1 19  ? -2.179  5.127   19.139  1.00 9.60  ? 19  TYR B N   1 
ATOM   2359  C  CA  . TYR B  1 19  ? -1.014  4.250   19.158  1.00 8.54  ? 19  TYR B CA  1 
ATOM   2360  C  C   . TYR B  1 19  ? 0.089   4.887   18.363  1.00 10.11 ? 19  TYR B C   1 
ATOM   2361  O  O   . TYR B  1 19  ? 0.253   4.653   17.156  1.00 8.80  ? 19  TYR B O   1 
ATOM   2362  C  CB  . TYR B  1 19  ? -1.391  2.877   18.542  1.00 8.52  ? 19  TYR B CB  1 
ATOM   2363  C  CG  . TYR B  1 19  ? -2.537  2.165   19.311  1.00 10.62 ? 19  TYR B CG  1 
ATOM   2364  C  CD1 . TYR B  1 19  ? -3.860  2.317   18.881  1.00 11.04 ? 19  TYR B CD1 1 
ATOM   2365  C  CD2 . TYR B  1 19  ? -2.263  1.410   20.479  1.00 9.46  ? 19  TYR B CD2 1 
ATOM   2366  C  CE1 . TYR B  1 19  ? -4.881  1.684   19.491  1.00 11.35 ? 19  TYR B CE1 1 
ATOM   2367  C  CE2 . TYR B  1 19  ? -3.327  0.702   21.089  1.00 11.31 ? 19  TYR B CE2 1 
ATOM   2368  C  CZ  . TYR B  1 19  ? -4.619  0.904   20.572  1.00 11.24 ? 19  TYR B CZ  1 
ATOM   2369  O  OH  . TYR B  1 19  ? -5.749  0.293   21.200  1.00 16.82 ? 19  TYR B OH  1 
ATOM   2370  N  N   . PRO B  1 20  ? 0.816   5.821   18.923  1.00 9.32  ? 20  PRO B N   1 
ATOM   2371  C  CA  . PRO B  1 20  ? 1.779   6.653   18.161  1.00 9.39  ? 20  PRO B CA  1 
ATOM   2372  C  C   . PRO B  1 20  ? 2.782   5.858   17.348  1.00 8.32  ? 20  PRO B C   1 
ATOM   2373  O  O   . PRO B  1 20  ? 3.186   6.364   16.256  1.00 8.05  ? 20  PRO B O   1 
ATOM   2374  C  CB  . PRO B  1 20  ? 2.460   7.534   19.307  1.00 10.39 ? 20  PRO B CB  1 
ATOM   2375  C  CG  . PRO B  1 20  ? 1.284   7.635   20.280  1.00 11.82 ? 20  PRO B CG  1 
ATOM   2376  C  CD  . PRO B  1 20  ? 0.795   6.206   20.367  1.00 11.20 ? 20  PRO B CD  1 
ATOM   2377  N  N   . SER B  1 21  ? 3.160   4.632   17.774  1.00 8.28  ? 21  SER B N   1 
ATOM   2378  C  CA  . SER B  1 21  ? 4.159   3.852   17.037  1.00 6.84  ? 21  SER B CA  1 
ATOM   2379  C  C   . SER B  1 21  ? 3.612   3.459   15.667  1.00 7.41  ? 21  SER B C   1 
ATOM   2380  O  O   . SER B  1 21  ? 4.426   3.256   14.744  1.00 7.84  ? 21  SER B O   1 
ATOM   2381  C  CB  . SER B  1 21  ? 4.532   2.655   17.775  1.00 8.47  ? 21  SER B CB  1 
ATOM   2382  O  OG  . SER B  1 21  ? 5.310   3.118   18.958  1.00 9.10  ? 21  SER B OG  1 
ATOM   2383  N  N   . CYS B  1 22  ? 2.286   3.420   15.505  1.00 6.41  ? 22  CYS B N   1 
ATOM   2384  C  CA  . CYS B  1 22  ? 1.747   3.127   14.178  1.00 6.81  ? 22  CYS B CA  1 
ATOM   2385  C  C   . CYS B  1 22  ? 2.112   4.220   13.189  1.00 5.98  ? 22  CYS B C   1 
ATOM   2386  O  O   . CYS B  1 22  ? 1.962   3.979   11.945  1.00 6.93  ? 22  CYS B O   1 
ATOM   2387  C  CB  . CYS B  1 22  ? 0.201   2.919   14.228  1.00 5.37  ? 22  CYS B CB  1 
ATOM   2388  S  SG  . CYS B  1 22  ? -0.258  1.540   15.353  1.00 6.91  ? 22  CYS B SG  1 
ATOM   2389  N  N   . GLY B  1 23  ? 2.427   5.471   13.562  1.00 7.98  ? 23  GLY B N   1 
ATOM   2390  C  CA  . GLY B  1 23  ? 3.019   6.383   12.638  1.00 7.95  ? 23  GLY B CA  1 
ATOM   2391  C  C   . GLY B  1 23  ? 4.541   6.592   12.845  1.00 8.67  ? 23  GLY B C   1 
ATOM   2392  O  O   . GLY B  1 23  ? 5.004   7.656   12.386  1.00 8.30  ? 23  GLY B O   1 
ATOM   2393  N  N   . GLY B  1 24  ? 5.216   5.648   13.471  1.00 7.61  ? 24  GLY B N   1 
ATOM   2394  C  CA  . GLY B  1 24  ? 6.621   5.807   13.740  1.00 7.64  ? 24  GLY B CA  1 
ATOM   2395  C  C   . GLY B  1 24  ? 7.502   5.049   12.820  1.00 8.92  ? 24  GLY B C   1 
ATOM   2396  O  O   . GLY B  1 24  ? 7.121   4.770   11.609  1.00 9.27  ? 24  GLY B O   1 
ATOM   2397  N  N   . LEU B  1 25  ? 8.673   4.710   13.241  1.00 7.50  ? 25  LEU B N   1 
ATOM   2398  C  CA  . LEU B  1 25  ? 9.695   4.031   12.448  1.00 8.23  ? 25  LEU B CA  1 
ATOM   2399  C  C   . LEU B  1 25  ? 9.467   2.582   12.319  1.00 7.37  ? 25  LEU B C   1 
ATOM   2400  O  O   . LEU B  1 25  ? 8.720   1.963   13.091  1.00 6.29  ? 25  LEU B O   1 
ATOM   2401  C  CB  . LEU B  1 25  ? 11.091  4.164   13.180  1.00 9.69  ? 25  LEU B CB  1 
ATOM   2402  C  CG  . LEU B  1 25  ? 11.611  5.567   13.436  1.00 12.96 ? 25  LEU B CG  1 
ATOM   2403  C  CD1 . LEU B  1 25  ? 12.764  5.552   14.436  1.00 11.95 ? 25  LEU B CD1 1 
ATOM   2404  C  CD2 . LEU B  1 25  ? 12.067  6.115   12.106  1.00 13.28 ? 25  LEU B CD2 1 
ATOM   2405  N  N   . LEU B  1 26  ? 10.131  1.998   11.300  1.00 7.34  ? 26  LEU B N   1 
ATOM   2406  C  CA  . LEU B  1 26  ? 10.261  0.543   11.099  1.00 7.77  ? 26  LEU B CA  1 
ATOM   2407  C  C   . LEU B  1 26  ? 8.926   -0.196  10.925  1.00 6.15  ? 26  LEU B C   1 
ATOM   2408  O  O   . LEU B  1 26  ? 8.817   -1.348  11.342  1.00 7.60  ? 26  LEU B O   1 
ATOM   2409  C  CB  . LEU B  1 26  ? 11.060  -0.150  12.211  1.00 9.21  ? 26  LEU B CB  1 
ATOM   2410  C  CG  . LEU B  1 26  ? 12.501  0.424   12.365  1.00 10.02 ? 26  LEU B CG  1 
ATOM   2411  C  CD1 . LEU B  1 26  ? 13.219  -0.449  13.488  1.00 12.10 ? 26  LEU B CD1 1 
ATOM   2412  C  CD2 . LEU B  1 26  ? 13.301  0.137   11.187  1.00 11.32 ? 26  LEU B CD2 1 
ATOM   2413  N  N   . GLN B  1 27  ? 7.950   0.447   10.292  1.00 7.15  ? 27  GLN B N   1 
ATOM   2414  C  CA  . GLN B  1 27  ? 6.579   -0.161  10.215  1.00 5.96  ? 27  GLN B CA  1 
ATOM   2415  C  C   . GLN B  1 27  ? 6.562   -1.307  9.210   1.00 6.36  ? 27  GLN B C   1 
ATOM   2416  O  O   . GLN B  1 27  ? 7.142   -1.218  8.136   1.00 7.32  ? 27  GLN B O   1 
ATOM   2417  C  CB  . GLN B  1 27  ? 5.528   0.900   9.933   1.00 6.17  ? 27  GLN B CB  1 
ATOM   2418  C  CG  . GLN B  1 27  ? 5.397   1.924   11.093  1.00 5.92  ? 27  GLN B CG  1 
ATOM   2419  C  CD  . GLN B  1 27  ? 4.940   1.206   12.332  1.00 6.57  ? 27  GLN B CD  1 
ATOM   2420  O  OE1 . GLN B  1 27  ? 5.792   0.970   13.270  1.00 9.40  ? 27  GLN B OE1 1 
ATOM   2421  N  NE2 . GLN B  1 27  ? 3.715   0.836   12.412  1.00 4.38  ? 27  GLN B NE2 1 
ATOM   2422  N  N   . SER B  1 28  ? 5.731   -2.286  9.565   1.00 4.68  ? 28  SER B N   1 
ATOM   2423  C  CA  . SER B  1 28  ? 5.501   -3.425  8.646   1.00 4.92  ? 28  SER B CA  1 
ATOM   2424  C  C   . SER B  1 28  ? 3.963   -3.476  8.426   1.00 4.36  ? 28  SER B C   1 
ATOM   2425  O  O   . SER B  1 28  ? 3.174   -2.880  9.190   1.00 5.21  ? 28  SER B O   1 
ATOM   2426  C  CB  . SER B  1 28  ? 5.879   -4.703  9.450   1.00 6.05  ? 28  SER B CB  1 
ATOM   2427  O  OG  . SER B  1 28  ? 7.288   -4.801  9.637   1.00 5.66  ? 28  SER B OG  1 
ATOM   2428  N  N   . PRO B  1 29  ? 3.511   -4.222  7.419   1.00 4.71  ? 29  PRO B N   1 
ATOM   2429  C  CA  . PRO B  1 29  ? 4.265   -5.017  6.465   1.00 3.97  ? 29  PRO B CA  1 
ATOM   2430  C  C   . PRO B  1 29  ? 4.743   -4.190  5.263   1.00 5.03  ? 29  PRO B C   1 
ATOM   2431  O  O   . PRO B  1 29  ? 4.506   -2.953  5.254   1.00 5.83  ? 29  PRO B O   1 
ATOM   2432  C  CB  . PRO B  1 29  ? 3.201   -6.032  5.920   1.00 5.30  ? 29  PRO B CB  1 
ATOM   2433  C  CG  . PRO B  1 29  ? 1.912   -5.193  5.908   1.00 4.88  ? 29  PRO B CG  1 
ATOM   2434  C  CD  . PRO B  1 29  ? 2.071   -4.260  7.148   1.00 4.98  ? 29  PRO B CD  1 
ATOM   2435  N  N   . ILE B  1 30  ? 5.509   -4.834  4.370   1.00 5.61  ? 30  ILE B N   1 
ATOM   2436  C  CA  . ILE B  1 30  ? 6.123   -4.081  3.221   1.00 5.99  ? 30  ILE B CA  1 
ATOM   2437  C  C   . ILE B  1 30  ? 5.988   -4.956  1.986   1.00 5.94  ? 30  ILE B C   1 
ATOM   2438  O  O   . ILE B  1 30  ? 5.698   -6.167  2.041   1.00 6.27  ? 30  ILE B O   1 
ATOM   2439  C  CB  . ILE B  1 30  ? 7.677   -3.849  3.494   1.00 5.94  ? 30  ILE B CB  1 
ATOM   2440  C  CG1 . ILE B  1 30  ? 8.393   -5.181  3.746   1.00 5.29  ? 30  ILE B CG1 1 
ATOM   2441  C  CG2 . ILE B  1 30  ? 7.823   -2.918  4.703   1.00 8.47  ? 30  ILE B CG2 1 
ATOM   2442  C  CD1 . ILE B  1 30  ? 9.981   -4.973  3.796   1.00 7.49  ? 30  ILE B CD1 1 
ATOM   2443  N  N   . ASP B  1 31  ? 6.212   -4.267  0.832   1.00 5.43  ? 31  ASP B N   1 
ATOM   2444  C  CA  . ASP B  1 31  ? 6.338   -4.989  -0.454  1.00 5.56  ? 31  ASP B CA  1 
ATOM   2445  C  C   . ASP B  1 31  ? 7.752   -5.400  -0.666  1.00 7.09  ? 31  ASP B C   1 
ATOM   2446  O  O   . ASP B  1 31  ? 8.665   -4.594  -0.607  1.00 7.81  ? 31  ASP B O   1 
ATOM   2447  C  CB  . ASP B  1 31  ? 5.881   -4.077  -1.623  1.00 5.89  ? 31  ASP B CB  1 
ATOM   2448  C  CG  . ASP B  1 31  ? 6.066   -4.766  -2.948  1.00 6.76  ? 31  ASP B CG  1 
ATOM   2449  O  OD1 . ASP B  1 31  ? 5.476   -5.836  -3.117  1.00 8.89  ? 31  ASP B OD1 1 
ATOM   2450  O  OD2 . ASP B  1 31  ? 6.704   -4.206  -3.840  1.00 10.28 ? 31  ASP B OD2 1 
ATOM   2451  N  N   . LEU B  1 32  ? 7.918   -6.707  -0.893  1.00 6.87  ? 32  LEU B N   1 
ATOM   2452  C  CA  . LEU B  1 32  ? 9.249   -7.287  -1.081  1.00 7.78  ? 32  LEU B CA  1 
ATOM   2453  C  C   . LEU B  1 32  ? 9.461   -7.261  -2.609  1.00 6.97  ? 32  LEU B C   1 
ATOM   2454  O  O   . LEU B  1 32  ? 8.835   -8.008  -3.379  1.00 8.26  ? 32  LEU B O   1 
ATOM   2455  C  CB  . LEU B  1 32  ? 9.223   -8.743  -0.499  1.00 7.29  ? 32  LEU B CB  1 
ATOM   2456  C  CG  . LEU B  1 32  ? 8.824   -8.806  0.959   1.00 8.77  ? 32  LEU B CG  1 
ATOM   2457  C  CD1 . LEU B  1 32  ? 8.434   -10.187 1.328   1.00 10.15 ? 32  LEU B CD1 1 
ATOM   2458  C  CD2 . LEU B  1 32  ? 10.016  -8.304  1.890   1.00 10.44 ? 32  LEU B CD2 1 
ATOM   2459  N  N   . HIS B  1 33  ? 10.435  -6.395  -3.086  1.00 9.34  ? 33  HIS B N   1 
ATOM   2460  C  CA  . HIS B  1 33  ? 10.633  -6.223  -4.498  1.00 8.10  ? 33  HIS B CA  1 
ATOM   2461  C  C   . HIS B  1 33  ? 12.149  -5.890  -4.696  1.00 8.22  ? 33  HIS B C   1 
ATOM   2462  O  O   . HIS B  1 33  ? 12.807  -5.458  -3.784  1.00 9.53  ? 33  HIS B O   1 
ATOM   2463  C  CB  . HIS B  1 33  ? 9.746   -5.064  -5.117  1.00 10.16 ? 33  HIS B CB  1 
ATOM   2464  C  CG  . HIS B  1 33  ? 10.038  -3.688  -4.520  1.00 11.17 ? 33  HIS B CG  1 
ATOM   2465  N  ND1 . HIS B  1 33  ? 9.555   -3.316  -3.275  1.00 16.30 ? 33  HIS B ND1 1 
ATOM   2466  C  CD2 . HIS B  1 33  ? 10.709  -2.608  -5.026  1.00 10.24 ? 33  HIS B CD2 1 
ATOM   2467  C  CE1 . HIS B  1 33  ? 9.925   -2.054  -3.064  1.00 17.20 ? 33  HIS B CE1 1 
ATOM   2468  N  NE2 . HIS B  1 33  ? 10.575  -1.604  -4.122  1.00 11.43 ? 33  HIS B NE2 1 
ATOM   2469  N  N   . SER B  1 34  ? 12.587  -6.062  -5.958  1.00 10.37 ? 34  SER B N   1 
ATOM   2470  C  CA  . SER B  1 34  ? 14.031  -6.240  -6.257  1.00 11.32 ? 34  SER B CA  1 
ATOM   2471  C  C   . SER B  1 34  ? 14.863  -5.030  -5.801  1.00 12.25 ? 34  SER B C   1 
ATOM   2472  O  O   . SER B  1 34  ? 15.961  -5.212  -5.243  1.00 12.16 ? 34  SER B O   1 
ATOM   2473  C  CB  . SER B  1 34  ? 14.252  -6.528  -7.739  1.00 14.66 ? 34  SER B CB  1 
ATOM   2474  O  OG  . SER B  1 34  ? 13.691  -5.501  -8.531  1.00 22.99 ? 34  SER B OG  1 
ATOM   2475  N  N   . ASP B  1 35  ? 14.294  -3.790  -5.915  1.00 9.79  ? 35  ASP B N   1 
ATOM   2476  C  CA  . ASP B  1 35  ? 15.089  -2.604  -5.646  1.00 12.93 ? 35  ASP B CA  1 
ATOM   2477  C  C   . ASP B  1 35  ? 15.588  -2.521  -4.207  1.00 12.02 ? 35  ASP B C   1 
ATOM   2478  O  O   . ASP B  1 35  ? 16.494  -1.727  -3.847  1.00 14.93 ? 35  ASP B O   1 
ATOM   2479  C  CB  . ASP B  1 35  ? 14.233  -1.315  -5.949  1.00 12.55 ? 35  ASP B CB  1 
ATOM   2480  C  CG  . ASP B  1 35  ? 13.592  -1.313  -7.261  1.00 16.81 ? 35  ASP B CG  1 
ATOM   2481  O  OD1 . ASP B  1 35  ? 14.027  -0.445  -8.130  1.00 15.49 ? 35  ASP B OD1 1 
ATOM   2482  O  OD2 . ASP B  1 35  ? 12.649  -2.136  -7.499  1.00 15.75 ? 35  ASP B OD2 1 
ATOM   2483  N  N   . ILE B  1 36  ? 14.874  -3.209  -3.269  1.00 10.38 ? 36  ILE B N   1 
ATOM   2484  C  CA  . ILE B  1 36  ? 15.205  -3.110  -1.801  1.00 11.88 ? 36  ILE B CA  1 
ATOM   2485  C  C   . ILE B  1 36  ? 15.803  -4.437  -1.242  1.00 11.35 ? 36  ILE B C   1 
ATOM   2486  O  O   . ILE B  1 36  ? 15.964  -4.529  -0.045  1.00 11.33 ? 36  ILE B O   1 
ATOM   2487  C  CB  . ILE B  1 36  ? 13.989  -2.655  -0.936  1.00 14.31 ? 36  ILE B CB  1 
ATOM   2488  C  CG1 . ILE B  1 36  ? 12.778  -3.661  -1.125  1.00 13.35 ? 36  ILE B CG1 1 
ATOM   2489  C  CG2 . ILE B  1 36  ? 13.665  -1.247  -1.418  1.00 16.40 ? 36  ILE B CG2 1 
ATOM   2490  C  CD1 . ILE B  1 36  ? 11.904  -3.783  0.043   1.00 20.21 ? 36  ILE B CD1 1 
ATOM   2491  N  N   . LEU B  1 37  ? 16.021  -5.391  -2.139  1.00 11.78 ? 37  LEU B N   1 
ATOM   2492  C  CA  . LEU B  1 37  ? 16.545  -6.734  -1.702  1.00 12.10 ? 37  LEU B CA  1 
ATOM   2493  C  C   . LEU B  1 37  ? 18.079  -6.721  -1.784  1.00 14.28 ? 37  LEU B C   1 
ATOM   2494  O  O   . LEU B  1 37  ? 18.698  -6.121  -2.690  1.00 13.87 ? 37  LEU B O   1 
ATOM   2495  C  CB  . LEU B  1 37  ? 16.031  -7.863  -2.593  1.00 11.54 ? 37  LEU B CB  1 
ATOM   2496  C  CG  . LEU B  1 37  ? 14.549  -8.021  -2.634  1.00 14.39 ? 37  LEU B CG  1 
ATOM   2497  C  CD1 . LEU B  1 37  ? 14.124  -9.105  -3.566  1.00 15.38 ? 37  LEU B CD1 1 
ATOM   2498  C  CD2 . LEU B  1 37  ? 13.875  -8.040  -1.213  1.00 14.74 ? 37  LEU B CD2 1 
ATOM   2499  N  N   . GLN B  1 38  ? 18.727  -7.392  -0.840  1.00 11.39 ? 38  GLN B N   1 
ATOM   2500  C  CA  . GLN B  1 38  ? 20.215  -7.622  -0.954  1.00 10.25 ? 38  GLN B CA  1 
ATOM   2501  C  C   . GLN B  1 38  ? 20.484  -9.044  -0.413  1.00 10.83 ? 38  GLN B C   1 
ATOM   2502  O  O   . GLN B  1 38  ? 20.172  -9.345  0.755   1.00 10.33 ? 38  GLN B O   1 
ATOM   2503  C  CB  . GLN B  1 38  ? 20.993  -6.610  -0.160  1.00 13.42 ? 38  GLN B CB  1 
ATOM   2504  C  CG  . GLN B  1 38  ? 22.535  -6.781  -0.290  1.00 18.53 ? 38  GLN B CG  1 
ATOM   2505  C  CD  . GLN B  1 38  ? 23.183  -5.587  0.249   1.00 22.58 ? 38  GLN B CD  1 
ATOM   2506  O  OE1 . GLN B  1 38  ? 23.622  -5.567  1.422   1.00 31.86 ? 38  GLN B OE1 1 
ATOM   2507  N  NE2 . GLN B  1 38  ? 23.133  -4.489  -0.557  1.00 23.48 ? 38  GLN B NE2 1 
ATOM   2508  N  N   . TYR B  1 39  ? 21.080  -9.897  -1.188  1.00 10.17 ? 39  TYR B N   1 
ATOM   2509  C  CA  . TYR B  1 39  ? 21.558  -11.216 -0.719  1.00 10.12 ? 39  TYR B CA  1 
ATOM   2510  C  C   . TYR B  1 39  ? 22.599  -11.039 0.411   1.00 11.80 ? 39  TYR B C   1 
ATOM   2511  O  O   . TYR B  1 39  ? 23.525  -10.230 0.352   1.00 10.59 ? 39  TYR B O   1 
ATOM   2512  C  CB  . TYR B  1 39  ? 22.158  -11.987 -1.905  1.00 11.36 ? 39  TYR B CB  1 
ATOM   2513  C  CG  . TYR B  1 39  ? 22.778  -13.312 -1.520  1.00 10.13 ? 39  TYR B CG  1 
ATOM   2514  C  CD1 . TYR B  1 39  ? 22.002  -14.292 -0.925  1.00 12.13 ? 39  TYR B CD1 1 
ATOM   2515  C  CD2 . TYR B  1 39  ? 24.128  -13.587 -1.759  1.00 12.21 ? 39  TYR B CD2 1 
ATOM   2516  C  CE1 . TYR B  1 39  ? 22.514  -15.509 -0.580  1.00 14.44 ? 39  TYR B CE1 1 
ATOM   2517  C  CE2 . TYR B  1 39  ? 24.673  -14.820 -1.415  1.00 16.24 ? 39  TYR B CE2 1 
ATOM   2518  C  CZ  . TYR B  1 39  ? 23.867  -15.775 -0.820  1.00 14.15 ? 39  TYR B CZ  1 
ATOM   2519  O  OH  . TYR B  1 39  ? 24.364  -16.995 -0.463  1.00 15.47 ? 39  TYR B OH  1 
ATOM   2520  N  N   . ASP B  1 40  ? 22.377  -11.817 1.496   1.00 9.59  ? 40  ASP B N   1 
ATOM   2521  C  CA  . ASP B  1 40  ? 23.318  -11.881 2.623   1.00 10.53 ? 40  ASP B CA  1 
ATOM   2522  C  C   . ASP B  1 40  ? 23.707  -13.306 2.831   1.00 10.21 ? 40  ASP B C   1 
ATOM   2523  O  O   . ASP B  1 40  ? 22.917  -14.202 3.321   1.00 10.84 ? 40  ASP B O   1 
ATOM   2524  C  CB  . ASP B  1 40  ? 22.668  -11.265 3.845   1.00 9.89  ? 40  ASP B CB  1 
ATOM   2525  C  CG  . ASP B  1 40  ? 23.595  -11.199 5.093   1.00 12.04 ? 40  ASP B CG  1 
ATOM   2526  O  OD1 . ASP B  1 40  ? 23.158  -10.596 6.102   1.00 18.58 ? 40  ASP B OD1 1 
ATOM   2527  O  OD2 . ASP B  1 40  ? 24.695  -11.810 5.057   1.00 14.43 ? 40  ASP B OD2 1 
ATOM   2528  N  N   . ALA B  1 41  ? 24.962  -13.644 2.406   1.00 9.92  ? 41  ALA B N   1 
ATOM   2529  C  CA  . ALA B  1 41  ? 25.440  -15.024 2.448   1.00 10.71 ? 41  ALA B CA  1 
ATOM   2530  C  C   . ALA B  1 41  ? 25.655  -15.570 3.875   1.00 9.08  ? 41  ALA B C   1 
ATOM   2531  O  O   . ALA B  1 41  ? 25.828  -16.795 3.992   1.00 11.04 ? 41  ALA B O   1 
ATOM   2532  C  CB  . ALA B  1 41  ? 26.815  -15.134 1.676   1.00 13.79 ? 41  ALA B CB  1 
ATOM   2533  N  N   . SER B  1 42  ? 25.652  -14.669 4.879   1.00 9.80  ? 42  SER B N   1 
ATOM   2534  C  CA  . SER B  1 42  ? 25.839  -15.136 6.281   1.00 11.14 ? 42  SER B CA  1 
ATOM   2535  C  C   . SER B  1 42  ? 24.489  -15.583 6.886   1.00 13.69 ? 42  SER B C   1 
ATOM   2536  O  O   . SER B  1 42  ? 24.462  -16.143 8.009   1.00 13.73 ? 42  SER B O   1 
ATOM   2537  C  CB  . SER B  1 42  ? 26.472  -14.094 7.155   1.00 11.73 ? 42  SER B CB  1 
ATOM   2538  O  OG  . SER B  1 42  ? 27.764  -13.766 6.674   1.00 12.56 ? 42  SER B OG  1 
ATOM   2539  N  N   . LEU B  1 43  ? 23.368  -15.379 6.197   1.00 11.64 ? 43  LEU B N   1 
ATOM   2540  C  CA  . LEU B  1 43  ? 22.058  -15.830 6.783   1.00 14.46 ? 43  LEU B CA  1 
ATOM   2541  C  C   . LEU B  1 43  ? 21.961  -17.398 6.805   1.00 13.44 ? 43  LEU B C   1 
ATOM   2542  O  O   . LEU B  1 43  ? 22.033  -17.998 5.803   1.00 21.02 ? 43  LEU B O   1 
ATOM   2543  C  CB  . LEU B  1 43  ? 20.888  -15.278 5.906   1.00 12.56 ? 43  LEU B CB  1 
ATOM   2544  C  CG  . LEU B  1 43  ? 20.676  -13.870 6.180   1.00 11.11 ? 43  LEU B CG  1 
ATOM   2545  C  CD1 . LEU B  1 43  ? 19.660  -13.218 5.204   1.00 13.06 ? 43  LEU B CD1 1 
ATOM   2546  C  CD2 . LEU B  1 43  ? 20.278  -13.494 7.600   1.00 15.13 ? 43  LEU B CD2 1 
ATOM   2547  N  N   . THR B  1 44  ? 21.661  -18.031 7.930   1.00 18.53 ? 44  THR B N   1 
ATOM   2548  C  CA  . THR B  1 44  ? 21.617  -19.541 7.895   1.00 18.55 ? 44  THR B CA  1 
ATOM   2549  C  C   . THR B  1 44  ? 20.189  -20.109 8.081   1.00 14.77 ? 44  THR B C   1 
ATOM   2550  O  O   . THR B  1 44  ? 19.216  -19.266 8.424   1.00 16.79 ? 44  THR B O   1 
ATOM   2551  C  CB  . THR B  1 44  ? 22.414  -20.111 9.104   1.00 17.89 ? 44  THR B CB  1 
ATOM   2552  O  OG1 . THR B  1 44  ? 21.930  -19.520 10.368  1.00 25.09 ? 44  THR B OG1 1 
ATOM   2553  C  CG2 . THR B  1 44  ? 23.973  -19.779 8.933   1.00 22.83 ? 44  THR B CG2 1 
ATOM   2554  N  N   . PRO B  1 45  ? 19.979  -21.360 7.769   1.00 18.24 ? 45  PRO B N   1 
ATOM   2555  C  CA  . PRO B  1 45  ? 18.639  -21.810 7.971   1.00 16.98 ? 45  PRO B CA  1 
ATOM   2556  C  C   . PRO B  1 45  ? 18.220  -21.773 9.422   1.00 16.36 ? 45  PRO B C   1 
ATOM   2557  O  O   . PRO B  1 45  ? 19.024  -22.042 10.335  1.00 16.66 ? 45  PRO B O   1 
ATOM   2558  C  CB  . PRO B  1 45  ? 18.612  -23.203 7.371   1.00 18.13 ? 45  PRO B CB  1 
ATOM   2559  C  CG  . PRO B  1 45  ? 19.888  -23.273 6.478   1.00 18.83 ? 45  PRO B CG  1 
ATOM   2560  C  CD  . PRO B  1 45  ? 20.846  -22.366 7.091   1.00 13.37 ? 45  PRO B CD  1 
ATOM   2561  N  N   . LEU B  1 46  ? 17.001  -21.299 9.674   1.00 12.67 ? 46  LEU B N   1 
ATOM   2562  C  CA  . LEU B  1 46  ? 16.424  -21.601 11.002  1.00 12.82 ? 46  LEU B CA  1 
ATOM   2563  C  C   . LEU B  1 46  ? 16.140  -23.132 11.197  1.00 11.84 ? 46  LEU B C   1 
ATOM   2564  O  O   . LEU B  1 46  ? 15.888  -23.865 10.290  1.00 12.90 ? 46  LEU B O   1 
ATOM   2565  C  CB  . LEU B  1 46  ? 15.066  -20.842 11.174  1.00 14.45 ? 46  LEU B CB  1 
ATOM   2566  C  CG  . LEU B  1 46  ? 15.232  -19.319 10.923  1.00 14.77 ? 46  LEU B CG  1 
ATOM   2567  C  CD1 . LEU B  1 46  ? 13.826  -18.721 10.852  1.00 16.29 ? 46  LEU B CD1 1 
ATOM   2568  C  CD2 . LEU B  1 46  ? 16.063  -18.615 11.993  1.00 19.39 ? 46  LEU B CD2 1 
ATOM   2569  N  N   . GLU B  1 47  ? 16.219  -23.491 12.495  1.00 12.77 ? 47  GLU B N   1 
ATOM   2570  C  CA  . GLU B  1 47  ? 15.862  -24.795 12.989  1.00 13.95 ? 47  GLU B CA  1 
ATOM   2571  C  C   . GLU B  1 47  ? 14.697  -24.634 13.982  1.00 11.23 ? 47  GLU B C   1 
ATOM   2572  O  O   . GLU B  1 47  ? 14.692  -23.703 14.762  1.00 13.80 ? 47  GLU B O   1 
ATOM   2573  C  CB  . GLU B  1 47  ? 17.056  -25.536 13.658  1.00 16.04 ? 47  GLU B CB  1 
ATOM   2574  C  CG  . GLU B  1 47  ? 18.237  -25.790 12.613  1.00 19.52 ? 47  GLU B CG  1 
ATOM   2575  C  CD  . GLU B  1 47  ? 19.633  -26.198 13.209  1.00 23.61 ? 47  GLU B CD  1 
ATOM   2576  O  OE1 . GLU B  1 47  ? 19.641  -27.133 13.976  1.00 28.66 ? 47  GLU B OE1 1 
ATOM   2577  O  OE2 . GLU B  1 47  ? 20.674  -25.498 12.946  1.00 31.75 ? 47  GLU B OE2 1 
ATOM   2578  N  N   . PHE B  1 48  ? 13.718  -25.517 13.779  1.00 13.64 ? 48  PHE B N   1 
ATOM   2579  C  CA  . PHE B  1 48  ? 12.409  -25.450 14.499  1.00 13.73 ? 48  PHE B CA  1 
ATOM   2580  C  C   . PHE B  1 48  ? 12.386  -26.556 15.558  1.00 13.96 ? 48  PHE B C   1 
ATOM   2581  O  O   . PHE B  1 48  ? 12.450  -27.711 15.142  1.00 16.02 ? 48  PHE B O   1 
ATOM   2582  C  CB  . PHE B  1 48  ? 11.299  -25.575 13.506  1.00 15.22 ? 48  PHE B CB  1 
ATOM   2583  C  CG  . PHE B  1 48  ? 11.457  -24.603 12.346  1.00 13.49 ? 48  PHE B CG  1 
ATOM   2584  C  CD1 . PHE B  1 48  ? 11.866  -25.092 11.142  1.00 15.34 ? 48  PHE B CD1 1 
ATOM   2585  C  CD2 . PHE B  1 48  ? 11.346  -23.211 12.569  1.00 13.97 ? 48  PHE B CD2 1 
ATOM   2586  C  CE1 . PHE B  1 48  ? 12.084  -24.223 10.043  1.00 14.63 ? 48  PHE B CE1 1 
ATOM   2587  C  CE2 . PHE B  1 48  ? 11.585  -22.314 11.440  1.00 13.07 ? 48  PHE B CE2 1 
ATOM   2588  C  CZ  . PHE B  1 48  ? 11.931  -22.832 10.260  1.00 13.35 ? 48  PHE B CZ  1 
ATOM   2589  N  N   . GLN B  1 49  ? 12.452  -26.117 16.833  1.00 12.23 ? 49  GLN B N   1 
ATOM   2590  C  CA  . GLN B  1 49  ? 12.611  -27.121 17.974  1.00 13.72 ? 49  GLN B CA  1 
ATOM   2591  C  C   . GLN B  1 49  ? 11.283  -27.145 18.791  1.00 12.62 ? 49  GLN B C   1 
ATOM   2592  O  O   . GLN B  1 49  ? 10.737  -26.071 19.195  1.00 12.19 ? 49  GLN B O   1 
ATOM   2593  C  CB  . GLN B  1 49  ? 13.789  -26.731 18.839  1.00 14.40 ? 49  GLN B CB  1 
ATOM   2594  C  CG  . GLN B  1 49  ? 15.150  -27.009 18.023  1.00 20.62 ? 49  GLN B CG  1 
ATOM   2595  C  CD  . GLN B  1 49  ? 16.261  -26.187 18.526  1.00 27.82 ? 49  GLN B CD  1 
ATOM   2596  O  OE1 . GLN B  1 49  ? 16.013  -25.260 19.332  1.00 26.42 ? 49  GLN B OE1 1 
ATOM   2597  N  NE2 . GLN B  1 49  ? 17.487  -26.389 17.960  1.00 29.61 ? 49  GLN B NE2 1 
ATOM   2598  N  N   . GLY B  1 50  ? 10.815  -28.333 19.061  1.00 11.61 ? 50  GLY B N   1 
ATOM   2599  C  CA  . GLY B  1 50  ? 9.611   -28.404 19.884  1.00 10.91 ? 50  GLY B CA  1 
ATOM   2600  C  C   . GLY B  1 50  ? 8.338   -28.139 19.077  1.00 13.22 ? 50  GLY B C   1 
ATOM   2601  O  O   . GLY B  1 50  ? 7.290   -28.113 19.726  1.00 13.40 ? 50  GLY B O   1 
ATOM   2602  N  N   . TYR B  1 51  ? 8.394   -28.005 17.760  1.00 11.05 ? 51  TYR B N   1 
ATOM   2603  C  CA  . TYR B  1 51  ? 7.173   -27.719 16.934  1.00 9.82  ? 51  TYR B CA  1 
ATOM   2604  C  C   . TYR B  1 51  ? 6.201   -28.830 16.927  1.00 11.55 ? 51  TYR B C   1 
ATOM   2605  O  O   . TYR B  1 51  ? 5.007   -28.651 16.656  1.00 11.16 ? 51  TYR B O   1 
ATOM   2606  C  CB  . TYR B  1 51  ? 7.581   -27.247 15.518  1.00 8.97  ? 51  TYR B CB  1 
ATOM   2607  C  CG  . TYR B  1 51  ? 7.901   -25.765 15.390  1.00 8.21  ? 51  TYR B CG  1 
ATOM   2608  C  CD1 . TYR B  1 51  ? 8.743   -25.117 16.292  1.00 10.22 ? 51  TYR B CD1 1 
ATOM   2609  C  CD2 . TYR B  1 51  ? 7.370   -25.019 14.348  1.00 9.49  ? 51  TYR B CD2 1 
ATOM   2610  C  CE1 . TYR B  1 51  ? 9.032   -23.759 16.156  1.00 9.72  ? 51  TYR B CE1 1 
ATOM   2611  C  CE2 . TYR B  1 51  ? 7.651   -23.674 14.206  1.00 11.44 ? 51  TYR B CE2 1 
ATOM   2612  C  CZ  . TYR B  1 51  ? 8.479   -23.047 15.106  1.00 9.38  ? 51  TYR B CZ  1 
ATOM   2613  O  OH  . TYR B  1 51  ? 8.742   -21.705 14.941  1.00 11.08 ? 51  TYR B OH  1 
ATOM   2614  N  N   . ASN B  1 52  ? 6.701   -30.068 17.149  1.00 12.12 ? 52  ASN B N   1 
ATOM   2615  C  CA  . ASN B  1 52  ? 5.810   -31.269 17.062  1.00 11.11 ? 52  ASN B CA  1 
ATOM   2616  C  C   . ASN B  1 52  ? 5.081   -31.446 18.376  1.00 13.31 ? 52  ASN B C   1 
ATOM   2617  O  O   . ASN B  1 52  ? 5.555   -32.187 19.248  1.00 14.21 ? 52  ASN B O   1 
ATOM   2618  C  CB  . ASN B  1 52  ? 6.628   -32.583 16.718  1.00 14.11 ? 52  ASN B CB  1 
ATOM   2619  C  CG  . ASN B  1 52  ? 5.709   -33.713 16.382  1.00 16.02 ? 52  ASN B CG  1 
ATOM   2620  O  OD1 . ASN B  1 52  ? 4.479   -33.559 16.374  1.00 24.52 ? 52  ASN B OD1 1 
ATOM   2621  N  ND2 . ASN B  1 52  ? 6.276   -34.870 16.078  1.00 20.44 ? 52  ASN B ND2 1 
ATOM   2622  N  N   . LEU B  1 53  ? 3.991   -30.675 18.597  1.00 10.81 ? 53  LEU B N   1 
ATOM   2623  C  CA  . LEU B  1 53  ? 3.266   -30.717 19.892  1.00 10.24 ? 53  LEU B CA  1 
ATOM   2624  C  C   . LEU B  1 53  ? 2.550   -32.037 20.108  1.00 9.74  ? 53  LEU B C   1 
ATOM   2625  O  O   . LEU B  1 53  ? 1.980   -32.637 19.203  1.00 11.41 ? 53  LEU B O   1 
ATOM   2626  C  CB  . LEU B  1 53  ? 2.247   -29.549 19.892  1.00 10.41 ? 53  LEU B CB  1 
ATOM   2627  C  CG  . LEU B  1 53  ? 2.824   -28.170 19.584  1.00 11.56 ? 53  LEU B CG  1 
ATOM   2628  C  CD1 . LEU B  1 53  ? 1.559   -27.137 19.368  1.00 12.58 ? 53  LEU B CD1 1 
ATOM   2629  C  CD2 . LEU B  1 53  ? 3.830   -27.754 20.627  1.00 11.56 ? 53  LEU B CD2 1 
ATOM   2630  N  N   . SER B  1 54  ? 2.632   -32.515 21.367  1.00 9.17  ? 54  SER B N   1 
ATOM   2631  C  CA  . SER B  1 54  ? 2.020   -33.817 21.668  1.00 9.97  ? 54  SER B CA  1 
ATOM   2632  C  C   . SER B  1 54  ? 0.528   -33.805 21.404  1.00 10.93 ? 54  SER B C   1 
ATOM   2633  O  O   . SER B  1 54  ? -0.158  -32.860 21.879  1.00 9.74  ? 54  SER B O   1 
ATOM   2634  C  CB  . SER B  1 54  ? 2.287   -34.107 23.149  1.00 10.60 ? 54  SER B CB  1 
ATOM   2635  O  OG  . SER B  1 54  ? 1.537   -35.241 23.529  1.00 11.00 ? 54  SER B OG  1 
ATOM   2636  N  N   . ALA B  1 55  ? 0.037   -34.868 20.765  1.00 11.68 ? 55  ALA B N   1 
ATOM   2637  C  CA  . ALA B  1 55  ? -1.442  -34.988 20.546  1.00 12.43 ? 55  ALA B CA  1 
ATOM   2638  C  C   . ALA B  1 55  ? -2.181  -35.207 21.830  1.00 14.57 ? 55  ALA B C   1 
ATOM   2639  O  O   . ALA B  1 55  ? -3.418  -34.996 21.824  1.00 14.43 ? 55  ALA B O   1 
ATOM   2640  C  CB  . ALA B  1 55  ? -1.736  -36.085 19.631  1.00 16.31 ? 55  ALA B CB  1 
ATOM   2641  N  N   . ASN B  1 56  ? -1.491  -35.622 22.933  1.00 12.43 ? 56  ASN B N   1 
ATOM   2642  C  CA  . ASN B  1 56  ? -2.243  -35.750 24.218  1.00 13.32 ? 56  ASN B CA  1 
ATOM   2643  C  C   . ASN B  1 56  ? -2.303  -34.439 24.959  1.00 13.60 ? 56  ASN B C   1 
ATOM   2644  O  O   . ASN B  1 56  ? -2.941  -34.313 26.041  1.00 12.76 ? 56  ASN B O   1 
ATOM   2645  C  CB  . ASN B  1 56  ? -1.562  -36.741 25.216  1.00 12.25 ? 56  ASN B CB  1 
ATOM   2646  C  CG  . ASN B  1 56  ? -1.764  -38.134 24.811  1.00 17.44 ? 56  ASN B CG  1 
ATOM   2647  O  OD1 . ASN B  1 56  ? -0.818  -39.027 24.966  1.00 24.42 ? 56  ASN B OD1 1 
ATOM   2648  N  ND2 . ASN B  1 56  ? -2.941  -38.404 24.260  1.00 17.24 ? 56  ASN B ND2 1 
ATOM   2649  N  N   A LYS B  1 57  ? -1.584  -33.376 24.516  0.50 10.13 ? 57  LYS B N   1 
ATOM   2650  N  N   B LYS B  1 57  ? -1.653  -33.406 24.398  0.50 10.95 ? 57  LYS B N   1 
ATOM   2651  C  CA  A LYS B  1 57  ? -1.799  -32.032 25.124  0.50 9.40  ? 57  LYS B CA  1 
ATOM   2652  C  CA  B LYS B  1 57  ? -1.699  -32.069 24.967  0.50 10.63 ? 57  LYS B CA  1 
ATOM   2653  C  C   A LYS B  1 57  ? -2.753  -31.234 24.210  0.50 9.05  ? 57  LYS B C   1 
ATOM   2654  C  C   B LYS B  1 57  ? -2.731  -31.221 24.164  0.50 9.29  ? 57  LYS B C   1 
ATOM   2655  O  O   A LYS B  1 57  ? -3.084  -31.660 23.100  0.50 10.36 ? 57  LYS B O   1 
ATOM   2656  O  O   B LYS B  1 57  ? -3.120  -31.630 23.070  0.50 10.89 ? 57  LYS B O   1 
ATOM   2657  C  CB  A LYS B  1 57  ? -0.472  -31.237 25.292  0.50 9.97  ? 57  LYS B CB  1 
ATOM   2658  C  CB  B LYS B  1 57  ? -0.283  -31.466 24.831  0.50 10.75 ? 57  LYS B CB  1 
ATOM   2659  C  CG  A LYS B  1 57  ? 0.451   -31.874 26.322  0.50 8.93  ? 57  LYS B CG  1 
ATOM   2660  C  CG  B LYS B  1 57  ? 0.650   -32.028 25.934  0.50 10.06 ? 57  LYS B CG  1 
ATOM   2661  C  CD  A LYS B  1 57  ? 1.833   -31.227 26.329  0.50 10.47 ? 57  LYS B CD  1 
ATOM   2662  C  CD  B LYS B  1 57  ? 2.115   -31.506 25.780  0.50 11.54 ? 57  LYS B CD  1 
ATOM   2663  C  CE  A LYS B  1 57  ? 2.849   -31.978 27.169  0.50 13.15 ? 57  LYS B CE  1 
ATOM   2664  C  CE  B LYS B  1 57  ? 2.762   -31.231 27.199  0.50 13.56 ? 57  LYS B CE  1 
ATOM   2665  N  NZ  A LYS B  1 57  ? 2.427   -31.928 28.544  0.50 13.36 ? 57  LYS B NZ  1 
ATOM   2666  N  NZ  B LYS B  1 57  ? 4.265   -31.169 27.217  0.50 16.18 ? 57  LYS B NZ  1 
ATOM   2667  N  N   . GLN B  1 58  ? -3.208  -30.113 24.769  1.00 9.38  ? 58  GLN B N   1 
ATOM   2668  C  CA  . GLN B  1 58  ? -4.179  -29.250 24.052  1.00 10.26 ? 58  GLN B CA  1 
ATOM   2669  C  C   . GLN B  1 58  ? -3.703  -27.832 24.194  1.00 8.44  ? 58  GLN B C   1 
ATOM   2670  O  O   . GLN B  1 58  ? -3.015  -27.425 25.130  1.00 9.82  ? 58  GLN B O   1 
ATOM   2671  C  CB  . GLN B  1 58  ? -5.620  -29.368 24.731  1.00 11.89 ? 58  GLN B CB  1 
ATOM   2672  C  CG  . GLN B  1 58  ? -5.636  -28.864 26.134  1.00 14.33 ? 58  GLN B CG  1 
ATOM   2673  C  CD  . GLN B  1 58  ? -6.942  -28.988 26.856  1.00 17.38 ? 58  GLN B CD  1 
ATOM   2674  O  OE1 . GLN B  1 58  ? -7.823  -29.557 26.311  1.00 12.73 ? 58  GLN B OE1 1 
ATOM   2675  N  NE2 . GLN B  1 58  ? -7.022  -28.439 28.124  1.00 18.16 ? 58  GLN B NE2 1 
ATOM   2676  N  N   . PHE B  1 59  ? -4.190  -26.997 23.212  1.00 9.32  ? 59  PHE B N   1 
ATOM   2677  C  CA  . PHE B  1 59  ? -3.689  -25.630 23.027  1.00 8.38  ? 59  PHE B CA  1 
ATOM   2678  C  C   . PHE B  1 59  ? -4.895  -24.708 22.756  1.00 7.91  ? 59  PHE B C   1 
ATOM   2679  O  O   . PHE B  1 59  ? -5.795  -25.066 22.038  1.00 9.14  ? 59  PHE B O   1 
ATOM   2680  C  CB  . PHE B  1 59  ? -2.634  -25.611 21.909  1.00 8.04  ? 59  PHE B CB  1 
ATOM   2681  C  CG  . PHE B  1 59  ? -1.447  -26.451 22.307  1.00 6.20  ? 59  PHE B CG  1 
ATOM   2682  C  CD1 . PHE B  1 59  ? -1.488  -27.811 22.004  1.00 8.24  ? 59  PHE B CD1 1 
ATOM   2683  C  CD2 . PHE B  1 59  ? -0.425  -25.908 23.117  1.00 8.79  ? 59  PHE B CD2 1 
ATOM   2684  C  CE1 . PHE B  1 59  ? -0.481  -28.664 22.419  1.00 8.44  ? 59  PHE B CE1 1 
ATOM   2685  C  CE2 . PHE B  1 59  ? 0.619   -26.840 23.549  1.00 8.37  ? 59  PHE B CE2 1 
ATOM   2686  C  CZ  . PHE B  1 59  ? 0.517   -28.195 23.222  1.00 7.41  ? 59  PHE B CZ  1 
ATOM   2687  N  N   . LEU B  1 60  ? -4.850  -23.566 23.419  1.00 7.79  ? 60  LEU B N   1 
ATOM   2688  C  CA  . LEU B  1 60  ? -6.018  -22.630 23.412  1.00 9.24  ? 60  LEU B CA  1 
ATOM   2689  C  C   . LEU B  1 60  ? -6.220  -21.867 22.090  1.00 9.26  ? 60  LEU B C   1 
ATOM   2690  O  O   . LEU B  1 60  ? -5.277  -21.130 21.695  1.00 8.46  ? 60  LEU B O   1 
ATOM   2691  C  CB  . LEU B  1 60  ? -6.019  -21.715 24.624  1.00 9.97  ? 60  LEU B CB  1 
ATOM   2692  C  CG  . LEU B  1 60  ? -7.225  -20.787 24.849  1.00 9.81  ? 60  LEU B CG  1 
ATOM   2693  C  CD1 . LEU B  1 60  ? -8.352  -21.757 25.191  1.00 11.88 ? 60  LEU B CD1 1 
ATOM   2694  C  CD2 . LEU B  1 60  ? -6.911  -19.844 26.009  1.00 12.03 ? 60  LEU B CD2 1 
ATOM   2695  N  N   . LEU B  1 61  ? -7.379  -22.009 21.446  1.00 8.80  ? 61  LEU B N   1 
ATOM   2696  C  CA  . LEU B  1 61  ? -7.701  -21.235 20.254  1.00 8.02  ? 61  LEU B CA  1 
ATOM   2697  C  C   . LEU B  1 61  ? -8.673  -20.117 20.662  1.00 8.60  ? 61  LEU B C   1 
ATOM   2698  O  O   . LEU B  1 61  ? -9.643  -20.368 21.399  1.00 9.71  ? 61  LEU B O   1 
ATOM   2699  C  CB  . LEU B  1 61  ? -8.382  -22.069 19.248  1.00 7.71  ? 61  LEU B CB  1 
ATOM   2700  C  CG  . LEU B  1 61  ? -8.581  -21.489 17.858  1.00 9.83  ? 61  LEU B CG  1 
ATOM   2701  C  CD1 . LEU B  1 61  ? -7.209  -21.444 17.053  1.00 10.42 ? 61  LEU B CD1 1 
ATOM   2702  C  CD2 . LEU B  1 61  ? -9.582  -22.301 17.098  1.00 10.30 ? 61  LEU B CD2 1 
ATOM   2703  N  N   . THR B  1 62  ? -8.390  -18.864 20.341  1.00 9.71  ? 62  THR B N   1 
ATOM   2704  C  CA  . THR B  1 62  ? -9.221  -17.747 20.821  1.00 9.58  ? 62  THR B CA  1 
ATOM   2705  C  C   . THR B  1 62  ? -9.508  -16.784 19.648  1.00 10.12 ? 62  THR B C   1 
ATOM   2706  O  O   . THR B  1 62  ? -8.628  -16.453 18.809  1.00 9.57  ? 62  THR B O   1 
ATOM   2707  C  CB  . THR B  1 62  ? -8.352  -16.884 21.796  1.00 11.55 ? 62  THR B CB  1 
ATOM   2708  O  OG1 . THR B  1 62  ? -7.944  -17.684 22.946  1.00 12.50 ? 62  THR B OG1 1 
ATOM   2709  C  CG2 . THR B  1 62  ? -9.146  -15.657 22.330  1.00 14.66 ? 62  THR B CG2 1 
ATOM   2710  N  N   . ASN B  1 63  ? -10.727 -16.339 19.516  1.00 8.76  ? 63  ASN B N   1 
ATOM   2711  C  CA  . ASN B  1 63  ? -11.076 -15.172 18.666  1.00 8.37  ? 63  ASN B CA  1 
ATOM   2712  C  C   . ASN B  1 63  ? -10.833 -13.921 19.502  1.00 8.42  ? 63  ASN B C   1 
ATOM   2713  O  O   . ASN B  1 63  ? -11.528 -13.694 20.520  1.00 8.63  ? 63  ASN B O   1 
ATOM   2714  C  CB  . ASN B  1 63  ? -12.524 -15.304 18.206  1.00 8.58  ? 63  ASN B CB  1 
ATOM   2715  C  CG  . ASN B  1 63  ? -13.012 -14.080 17.424  1.00 7.42  ? 63  ASN B CG  1 
ATOM   2716  O  OD1 . ASN B  1 63  ? -12.457 -12.960 17.546  1.00 8.26  ? 63  ASN B OD1 1 
ATOM   2717  N  ND2 . ASN B  1 63  ? -14.032 -14.359 16.632  1.00 7.10  ? 63  ASN B ND2 1 
ATOM   2718  N  N   . ASN B  1 64  ? -9.813  -13.106 19.139  1.00 8.61  ? 64  ASN B N   1 
ATOM   2719  C  CA  . ASN B  1 64  ? -9.471  -11.979 19.963  1.00 9.59  ? 64  ASN B CA  1 
ATOM   2720  C  C   . ASN B  1 64  ? -10.135 -10.644 19.447  1.00 8.97  ? 64  ASN B C   1 
ATOM   2721  O  O   . ASN B  1 64  ? -9.749  -9.540  19.856  1.00 10.77 ? 64  ASN B O   1 
ATOM   2722  C  CB  . ASN B  1 64  ? -7.956  -11.791 20.145  1.00 10.10 ? 64  ASN B CB  1 
ATOM   2723  C  CG  . ASN B  1 64  ? -7.249  -11.476 18.841  1.00 10.60 ? 64  ASN B CG  1 
ATOM   2724  O  OD1 . ASN B  1 64  ? -7.923  -11.198 17.800  1.00 8.19  ? 64  ASN B OD1 1 
ATOM   2725  N  ND2 . ASN B  1 64  ? -5.894  -11.421 18.861  1.00 13.22 ? 64  ASN B ND2 1 
ATOM   2726  N  N   . GLY B  1 65  ? -11.073 -10.816 18.512  1.00 7.76  ? 65  GLY B N   1 
ATOM   2727  C  CA  . GLY B  1 65  ? -11.717 -9.642  17.920  1.00 8.89  ? 65  GLY B CA  1 
ATOM   2728  C  C   . GLY B  1 65  ? -10.997 -9.117  16.676  1.00 8.53  ? 65  GLY B C   1 
ATOM   2729  O  O   . GLY B  1 65  ? -11.560 -8.232  15.993  1.00 9.69  ? 65  GLY B O   1 
ATOM   2730  N  N   . HIS B  1 66  ? -9.781  -9.586  16.387  1.00 7.95  ? 66  HIS B N   1 
ATOM   2731  C  CA  . HIS B  1 66  ? -8.969  -9.064  15.245  1.00 8.33  ? 66  HIS B CA  1 
ATOM   2732  C  C   . HIS B  1 66  ? -8.438  -10.160 14.366  1.00 7.75  ? 66  HIS B C   1 
ATOM   2733  O  O   . HIS B  1 66  ? -8.222  -9.939  13.193  1.00 9.56  ? 66  HIS B O   1 
ATOM   2734  C  CB  . HIS B  1 66  ? -7.732  -8.219  15.784  1.00 7.95  ? 66  HIS B CB  1 
ATOM   2735  C  CG  . HIS B  1 66  ? -8.135  -7.153  16.756  1.00 12.35 ? 66  HIS B CG  1 
ATOM   2736  N  ND1 . HIS B  1 66  ? -8.821  -6.012  16.380  1.00 12.55 ? 66  HIS B ND1 1 
ATOM   2737  C  CD2 . HIS B  1 66  ? -7.947  -7.045  18.097  1.00 14.26 ? 66  HIS B CD2 1 
ATOM   2738  C  CE1 . HIS B  1 66  ? -9.052  -5.238  17.430  1.00 10.99 ? 66  HIS B CE1 1 
ATOM   2739  N  NE2 . HIS B  1 66  ? -8.522  -5.829  18.494  1.00 13.26 ? 66  HIS B NE2 1 
ATOM   2740  N  N   . SER B  1 67  ? -8.295  -11.375 14.925  1.00 8.17  ? 67  SER B N   1 
ATOM   2741  C  CA  . SER B  1 67  ? -7.846  -12.561 14.176  1.00 7.29  ? 67  SER B CA  1 
ATOM   2742  C  C   . SER B  1 67  ? -8.280  -13.787 15.026  1.00 7.86  ? 67  SER B C   1 
ATOM   2743  O  O   . SER B  1 67  ? -8.944  -13.589 16.105  1.00 8.91  ? 67  SER B O   1 
ATOM   2744  C  CB  . SER B  1 67  ? -6.287  -12.509 14.044  1.00 7.73  ? 67  SER B CB  1 
ATOM   2745  O  OG  . SER B  1 67  ? -5.831  -13.610 13.287  1.00 7.11  ? 67  SER B OG  1 
ATOM   2746  N  N   . VAL B  1 68  ? -7.977  -14.951 14.528  1.00 8.14  ? 68  VAL B N   1 
ATOM   2747  C  CA  . VAL B  1 68  ? -8.075  -16.113 15.386  1.00 8.08  ? 68  VAL B CA  1 
ATOM   2748  C  C   . VAL B  1 68  ? -6.609  -16.521 15.761  1.00 7.91  ? 68  VAL B C   1 
ATOM   2749  O  O   . VAL B  1 68  ? -5.741  -16.610 14.858  1.00 7.24  ? 68  VAL B O   1 
ATOM   2750  C  CB  . VAL B  1 68  ? -8.802  -17.255 14.619  1.00 10.76 ? 68  VAL B CB  1 
ATOM   2751  C  CG1 . VAL B  1 68  ? -8.172  -17.618 13.290  1.00 10.11 ? 68  VAL B CG1 1 
ATOM   2752  C  CG2 . VAL B  1 68  ? -8.990  -18.501 15.609  1.00 10.89 ? 68  VAL B CG2 1 
ATOM   2753  N  N   . LYS B  1 69  ? -6.324  -16.718 17.075  1.00 7.94  ? 69  LYS B N   1 
ATOM   2754  C  CA  . LYS B  1 69  ? -4.981  -17.098 17.517  1.00 9.10  ? 69  LYS B CA  1 
ATOM   2755  C  C   . LYS B  1 69  ? -4.972  -18.444 18.196  1.00 9.02  ? 69  LYS B C   1 
ATOM   2756  O  O   . LYS B  1 69  ? -5.986  -18.860 18.903  1.00 8.54  ? 69  LYS B O   1 
ATOM   2757  C  CB  . LYS B  1 69  ? -4.338  -16.022 18.419  1.00 13.02 ? 69  LYS B CB  1 
ATOM   2758  C  CG  . LYS B  1 69  ? -4.967  -15.874 19.717  1.00 16.51 ? 69  LYS B CG  1 
ATOM   2759  C  CD  . LYS B  1 69  ? -4.082  -14.844 20.631  1.00 12.92 ? 69  LYS B CD  1 
ATOM   2760  C  CE  . LYS B  1 69  ? -4.736  -14.807 21.976  1.00 15.08 ? 69  LYS B CE  1 
ATOM   2761  N  NZ  . LYS B  1 69  ? -4.023  -13.774 22.884  1.00 14.95 ? 69  LYS B NZ  1 
ATOM   2762  N  N   . LEU B  1 70  ? -3.898  -19.192 18.040  1.00 7.38  ? 70  LEU B N   1 
ATOM   2763  C  CA  . LEU B  1 70  ? -3.663  -20.408 18.779  1.00 6.52  ? 70  LEU B CA  1 
ATOM   2764  C  C   . LEU B  1 70  ? -2.447  -20.163 19.695  1.00 7.96  ? 70  LEU B C   1 
ATOM   2765  O  O   . LEU B  1 70  ? -1.334  -19.774 19.193  1.00 8.31  ? 70  LEU B O   1 
ATOM   2766  C  CB  . LEU B  1 70  ? -3.371  -21.492 17.771  1.00 8.51  ? 70  LEU B CB  1 
ATOM   2767  C  CG  . LEU B  1 70  ? -3.048  -22.842 18.410  1.00 7.44  ? 70  LEU B CG  1 
ATOM   2768  C  CD1 . LEU B  1 70  ? -4.290  -23.422 19.152  1.00 9.32  ? 70  LEU B CD1 1 
ATOM   2769  C  CD2 . LEU B  1 70  ? -2.539  -23.887 17.340  1.00 9.01  ? 70  LEU B CD2 1 
ATOM   2770  N  N   . ASN B  1 71  ? -2.628  -20.361 21.000  1.00 7.70  ? 71  ASN B N   1 
ATOM   2771  C  CA  . ASN B  1 71  ? -1.511  -20.228 21.929  1.00 9.31  ? 71  ASN B CA  1 
ATOM   2772  C  C   . ASN B  1 71  ? -0.546  -21.388 21.807  1.00 8.28  ? 71  ASN B C   1 
ATOM   2773  O  O   . ASN B  1 71  ? -0.951  -22.507 21.475  1.00 7.52  ? 71  ASN B O   1 
ATOM   2774  C  CB  . ASN B  1 71  ? -2.046  -20.184 23.372  1.00 8.55  ? 71  ASN B CB  1 
ATOM   2775  C  CG  . ASN B  1 71  ? -2.576  -18.810 23.755  1.00 10.49 ? 71  ASN B CG  1 
ATOM   2776  O  OD1 . ASN B  1 71  ? -2.593  -17.859 22.981  1.00 11.74 ? 71  ASN B OD1 1 
ATOM   2777  N  ND2 . ASN B  1 71  ? -3.123  -18.720 25.000  1.00 14.49 ? 71  ASN B ND2 1 
ATOM   2778  N  N   . LEU B  1 72  ? 0.742   -21.012 21.952  1.00 7.22  ? 72  LEU B N   1 
ATOM   2779  C  CA  . LEU B  1 72  ? 1.811   -22.034 21.720  1.00 8.06  ? 72  LEU B CA  1 
ATOM   2780  C  C   . LEU B  1 72  ? 2.684   -22.058 22.969  1.00 7.58  ? 72  LEU B C   1 
ATOM   2781  O  O   . LEU B  1 72  ? 2.802   -21.025 23.604  1.00 9.47  ? 72  LEU B O   1 
ATOM   2782  C  CB  . LEU B  1 72  ? 2.674   -21.647 20.474  1.00 6.70  ? 72  LEU B CB  1 
ATOM   2783  C  CG  . LEU B  1 72  ? 1.839   -21.661 19.164  1.00 7.86  ? 72  LEU B CG  1 
ATOM   2784  C  CD1 . LEU B  1 72  ? 2.761   -20.957 18.092  1.00 8.48  ? 72  LEU B CD1 1 
ATOM   2785  C  CD2 . LEU B  1 72  ? 1.494   -23.068 18.669  1.00 9.88  ? 72  LEU B CD2 1 
ATOM   2786  N  N   . PRO B  1 73  ? 3.294   -23.253 23.231  1.00 9.34  ? 73  PRO B N   1 
ATOM   2787  C  CA  . PRO B  1 73  ? 4.036   -23.367 24.514  1.00 10.11 ? 73  PRO B CA  1 
ATOM   2788  C  C   . PRO B  1 73  ? 5.468   -22.845 24.363  1.00 12.24 ? 73  PRO B C   1 
ATOM   2789  O  O   . PRO B  1 73  ? 6.070   -22.924 23.257  1.00 11.12 ? 73  PRO B O   1 
ATOM   2790  C  CB  . PRO B  1 73  ? 4.048   -24.869 24.686  1.00 11.31 ? 73  PRO B CB  1 
ATOM   2791  C  CG  . PRO B  1 73  ? 3.981   -25.507 23.273  1.00 11.31 ? 73  PRO B CG  1 
ATOM   2792  C  CD  . PRO B  1 73  ? 3.200   -24.480 22.444  1.00 7.91  ? 73  PRO B CD  1 
ATOM   2793  N  N   . SER B  1 74  ? 5.971   -22.290 25.487  1.00 12.07 ? 74  SER B N   1 
ATOM   2794  C  CA  . SER B  1 74  ? 7.342   -21.681 25.418  1.00 11.55 ? 74  SER B CA  1 
ATOM   2795  C  C   . SER B  1 74  ? 8.430   -22.711 25.270  1.00 10.76 ? 74  SER B C   1 
ATOM   2796  O  O   . SER B  1 74  ? 9.588   -22.244 24.993  1.00 13.10 ? 74  SER B O   1 
ATOM   2797  C  CB  . SER B  1 74  ? 7.588   -20.810 26.663  1.00 12.92 ? 74  SER B CB  1 
ATOM   2798  O  OG  . SER B  1 74  ? 7.573   -21.661 27.834  1.00 14.64 ? 74  SER B OG  1 
ATOM   2799  N  N   . ASP B  1 75  ? 8.156   -24.015 25.335  1.00 12.52 ? 75  ASP B N   1 
ATOM   2800  C  CA  . ASP B  1 75  ? 9.245   -24.949 25.054  1.00 16.37 ? 75  ASP B CA  1 
ATOM   2801  C  C   . ASP B  1 75  ? 9.491   -25.039 23.485  1.00 16.24 ? 75  ASP B C   1 
ATOM   2802  O  O   . ASP B  1 75  ? 10.515  -25.626 23.049  1.00 17.66 ? 75  ASP B O   1 
ATOM   2803  C  CB  . ASP B  1 75  ? 8.974   -26.315 25.703  1.00 15.83 ? 75  ASP B CB  1 
ATOM   2804  C  CG  . ASP B  1 75  ? 7.825   -27.079 25.001  1.00 20.21 ? 75  ASP B CG  1 
ATOM   2805  O  OD1 . ASP B  1 75  ? 6.652   -26.669 25.155  1.00 20.58 ? 75  ASP B OD1 1 
ATOM   2806  O  OD2 . ASP B  1 75  ? 8.092   -28.070 24.283  1.00 26.36 ? 75  ASP B OD2 1 
ATOM   2807  N  N   . MET B  1 76  ? 8.576   -24.500 22.626  1.00 12.03 ? 76  MET B N   1 
ATOM   2808  C  CA  . MET B  1 76  ? 8.783   -24.479 21.199  1.00 13.85 ? 76  MET B CA  1 
ATOM   2809  C  C   . MET B  1 76  ? 9.694   -23.257 20.922  1.00 11.77 ? 76  MET B C   1 
ATOM   2810  O  O   . MET B  1 76  ? 9.525   -22.130 21.421  1.00 11.46 ? 76  MET B O   1 
ATOM   2811  C  CB  . MET B  1 76  ? 7.336   -24.379 20.609  1.00 15.56 ? 76  MET B CB  1 
ATOM   2812  C  CG  . MET B  1 76  ? 7.247   -24.396 19.240  1.00 17.07 ? 76  MET B CG  1 
ATOM   2813  S  SD  . MET B  1 76  ? 5.407   -24.338 18.863  1.00 15.79 ? 76  MET B SD  1 
ATOM   2814  C  CE  . MET B  1 76  ? 5.672   -23.384 17.289  1.00 14.66 ? 76  MET B CE  1 
ATOM   2815  N  N   . HIS B  1 77  ? 10.783  -23.490 20.168  1.00 12.48 ? 77  HIS B N   1 
ATOM   2816  C  CA  . HIS B  1 77  ? 11.631  -22.355 19.871  1.00 15.79 ? 77  HIS B CA  1 
ATOM   2817  C  C   . HIS B  1 77  ? 12.352  -22.427 18.540  1.00 12.65 ? 77  HIS B C   1 
ATOM   2818  O  O   . HIS B  1 77  ? 12.307  -23.467 17.862  1.00 13.28 ? 77  HIS B O   1 
ATOM   2819  C  CB  . HIS B  1 77  ? 12.570  -22.027 20.983  1.00 18.58 ? 77  HIS B CB  1 
ATOM   2820  C  CG  . HIS B  1 77  ? 13.421  -23.164 21.381  1.00 22.74 ? 77  HIS B CG  1 
ATOM   2821  N  ND1 . HIS B  1 77  ? 13.024  -24.044 22.353  1.00 26.14 ? 77  HIS B ND1 1 
ATOM   2822  C  CD2 . HIS B  1 77  ? 14.667  -23.552 20.987  1.00 30.69 ? 77  HIS B CD2 1 
ATOM   2823  C  CE1 . HIS B  1 77  ? 13.962  -24.959 22.524  1.00 27.96 ? 77  HIS B CE1 1 
ATOM   2824  N  NE2 . HIS B  1 77  ? 14.977  -24.687 21.706  1.00 33.19 ? 77  HIS B NE2 1 
ATOM   2825  N  N   A ILE B  1 78  ? 12.946  -21.246 18.203  0.50 11.78 ? 78  ILE B N   1 
ATOM   2826  N  N   B ILE B  1 78  ? 12.956  -21.316 18.138  0.50 12.29 ? 78  ILE B N   1 
ATOM   2827  C  CA  A ILE B  1 78  ? 13.711  -21.079 16.954  0.50 13.32 ? 78  ILE B CA  1 
ATOM   2828  C  CA  B ILE B  1 78  ? 13.682  -21.437 16.881  0.50 12.35 ? 78  ILE B CA  1 
ATOM   2829  C  C   A ILE B  1 78  ? 15.221  -21.031 17.310  0.50 12.77 ? 78  ILE B C   1 
ATOM   2830  C  C   B ILE B  1 78  ? 15.153  -21.186 17.308  0.50 12.73 ? 78  ILE B C   1 
ATOM   2831  O  O   A ILE B  1 78  ? 15.614  -20.194 18.166  0.50 12.85 ? 78  ILE B O   1 
ATOM   2832  O  O   B ILE B  1 78  ? 15.453  -20.438 18.227  0.50 12.14 ? 78  ILE B O   1 
ATOM   2833  C  CB  A ILE B  1 78  ? 13.452  -19.686 16.297  0.50 12.04 ? 78  ILE B CB  1 
ATOM   2834  C  CB  B ILE B  1 78  ? 13.175  -20.388 15.855  0.50 11.76 ? 78  ILE B CB  1 
ATOM   2835  C  CG1 A ILE B  1 78  ? 12.002  -19.414 15.917  0.50 12.91 ? 78  ILE B CG1 1 
ATOM   2836  C  CG1 B ILE B  1 78  ? 13.230  -18.966 16.472  0.50 10.33 ? 78  ILE B CG1 1 
ATOM   2837  C  CG2 A ILE B  1 78  ? 14.363  -19.454 15.057  0.50 13.55 ? 78  ILE B CG2 1 
ATOM   2838  C  CG2 B ILE B  1 78  ? 11.802  -20.772 15.368  0.50 9.91  ? 78  ILE B CG2 1 
ATOM   2839  C  CD1 A ILE B  1 78  ? 11.831  -17.911 15.470  0.50 10.83 ? 78  ILE B CD1 1 
ATOM   2840  C  CD1 B ILE B  1 78  ? 14.499  -18.269 16.111  0.50 19.60 ? 78  ILE B CD1 1 
ATOM   2841  N  N   . GLN B  1 79  ? 16.011  -21.830 16.548  1.00 13.62 ? 79  GLN B N   1 
ATOM   2842  C  CA  . GLN B  1 79  ? 17.456  -21.656 16.604  1.00 18.41 ? 79  GLN B CA  1 
ATOM   2843  C  C   . GLN B  1 79  ? 17.920  -21.077 15.241  1.00 18.70 ? 79  GLN B C   1 
ATOM   2844  O  O   . GLN B  1 79  ? 17.348  -21.422 14.187  1.00 16.82 ? 79  GLN B O   1 
ATOM   2845  C  CB  . GLN B  1 79  ? 18.053  -23.023 16.794  1.00 17.75 ? 79  GLN B CB  1 
ATOM   2846  C  CG  . GLN B  1 79  ? 19.409  -23.159 16.131  1.00 25.61 ? 79  GLN B CG  1 
ATOM   2847  C  CD  . GLN B  1 79  ? 20.212  -24.209 16.816  1.00 32.93 ? 79  GLN B CD  1 
ATOM   2848  O  OE1 . GLN B  1 79  ? 20.001  -24.499 18.029  1.00 30.13 ? 79  GLN B OE1 1 
ATOM   2849  N  NE2 . GLN B  1 79  ? 21.137  -24.829 16.048  1.00 28.92 ? 79  GLN B NE2 1 
ATOM   2850  N  N   . GLY B  1 80  ? 19.003  -20.313 15.275  1.00 18.75 ? 80  GLY B N   1 
ATOM   2851  C  CA  . GLY B  1 80  ? 19.523  -19.683 14.078  1.00 21.19 ? 80  GLY B CA  1 
ATOM   2852  C  C   . GLY B  1 80  ? 19.497  -18.170 14.134  1.00 19.85 ? 80  GLY B C   1 
ATOM   2853  O  O   . GLY B  1 80  ? 19.955  -17.491 13.192  1.00 23.65 ? 80  GLY B O   1 
ATOM   2854  N  N   . LEU B  1 81  ? 18.918  -17.613 15.179  1.00 17.21 ? 81  LEU B N   1 
ATOM   2855  C  CA  . LEU B  1 81  ? 19.006  -16.187 15.430  1.00 16.30 ? 81  LEU B CA  1 
ATOM   2856  C  C   . LEU B  1 81  ? 20.063  -15.995 16.546  1.00 18.22 ? 81  LEU B C   1 
ATOM   2857  O  O   . LEU B  1 81  ? 20.518  -16.968 17.181  1.00 17.40 ? 81  LEU B O   1 
ATOM   2858  C  CB  . LEU B  1 81  ? 17.635  -15.617 15.883  1.00 15.32 ? 81  LEU B CB  1 
ATOM   2859  C  CG  . LEU B  1 81  ? 16.597  -15.686 14.752  1.00 14.63 ? 81  LEU B CG  1 
ATOM   2860  C  CD1 . LEU B  1 81  ? 15.221  -15.271 15.249  1.00 15.99 ? 81  LEU B CD1 1 
ATOM   2861  C  CD2 . LEU B  1 81  ? 17.071  -14.942 13.399  1.00 13.61 ? 81  LEU B CD2 1 
ATOM   2862  N  N   . GLN B  1 82  ? 20.388  -14.757 16.805  1.00 18.53 ? 82  GLN B N   1 
ATOM   2863  C  CA  . GLN B  1 82  ? 21.511  -14.603 17.743  1.00 19.09 ? 82  GLN B CA  1 
ATOM   2864  C  C   . GLN B  1 82  ? 21.081  -14.901 19.179  1.00 19.26 ? 82  GLN B C   1 
ATOM   2865  O  O   . GLN B  1 82  ? 21.929  -15.425 19.973  1.00 20.52 ? 82  GLN B O   1 
ATOM   2866  C  CB  . GLN B  1 82  ? 22.189  -13.243 17.673  1.00 17.64 ? 82  GLN B CB  1 
ATOM   2867  C  CG  . GLN B  1 82  ? 21.286  -12.148 17.678  1.00 15.31 ? 82  GLN B CG  1 
ATOM   2868  C  CD  . GLN B  1 82  ? 21.980  -10.828 17.536  1.00 23.60 ? 82  GLN B CD  1 
ATOM   2869  O  OE1 . GLN B  1 82  ? 21.744  -9.972  18.374  1.00 20.28 ? 82  GLN B OE1 1 
ATOM   2870  N  NE2 . GLN B  1 82  ? 22.766  -10.619 16.458  1.00 21.31 ? 82  GLN B NE2 1 
ATOM   2871  N  N   . SER B  1 83  ? 19.806  -14.561 19.536  1.00 15.88 ? 83  SER B N   1 
ATOM   2872  C  CA  . SER B  1 83  ? 19.212  -15.017 20.847  1.00 15.36 ? 83  SER B CA  1 
ATOM   2873  C  C   . SER B  1 83  ? 18.291  -16.179 20.563  1.00 14.03 ? 83  SER B C   1 
ATOM   2874  O  O   . SER B  1 83  ? 17.822  -16.398 19.396  1.00 13.49 ? 83  SER B O   1 
ATOM   2875  C  CB  . SER B  1 83  ? 18.389  -13.936 21.520  1.00 16.13 ? 83  SER B CB  1 
ATOM   2876  O  OG  . SER B  1 83  ? 19.094  -12.684 21.730  1.00 17.95 ? 83  SER B OG  1 
ATOM   2877  N  N   . ARG B  1 84  ? 17.959  -16.918 21.625  1.00 14.63 ? 84  ARG B N   1 
ATOM   2878  C  CA  . ARG B  1 84  ? 16.886  -17.888 21.566  1.00 13.99 ? 84  ARG B CA  1 
ATOM   2879  C  C   . ARG B  1 84  ? 15.543  -17.201 21.573  1.00 10.30 ? 84  ARG B C   1 
ATOM   2880  O  O   . ARG B  1 84  ? 15.357  -16.294 22.422  1.00 13.76 ? 84  ARG B O   1 
ATOM   2881  C  CB  . ARG B  1 84  ? 16.867  -18.775 22.822  1.00 16.22 ? 84  ARG B CB  1 
ATOM   2882  C  CG  . ARG B  1 84  ? 15.560  -19.609 22.847  1.00 22.70 ? 84  ARG B CG  1 
ATOM   2883  C  CD  . ARG B  1 84  ? 15.608  -20.571 24.039  1.00 23.43 ? 84  ARG B CD  1 
ATOM   2884  N  NE  . ARG B  1 84  ? 16.353  -21.743 23.616  1.00 26.31 ? 84  ARG B NE  1 
ATOM   2885  C  CZ  . ARG B  1 84  ? 16.475  -22.830 24.394  1.00 31.06 ? 84  ARG B CZ  1 
ATOM   2886  N  NH1 . ARG B  1 84  ? 15.952  -22.772 25.617  1.00 26.96 ? 84  ARG B NH1 1 
ATOM   2887  N  NH2 . ARG B  1 84  ? 17.161  -23.915 23.976  1.00 29.47 ? 84  ARG B NH2 1 
ATOM   2888  N  N   . TYR B  1 85  ? 14.702  -17.590 20.563  1.00 9.83  ? 85  TYR B N   1 
ATOM   2889  C  CA  . TYR B  1 85  ? 13.279  -17.036 20.640  1.00 9.82  ? 85  TYR B CA  1 
ATOM   2890  C  C   . TYR B  1 85  ? 12.317  -18.182 20.865  1.00 10.42 ? 85  TYR B C   1 
ATOM   2891  O  O   . TYR B  1 85  ? 12.421  -19.243 20.259  1.00 12.04 ? 85  TYR B O   1 
ATOM   2892  C  CB  . TYR B  1 85  ? 12.949  -16.253 19.307  1.00 9.33  ? 85  TYR B CB  1 
ATOM   2893  C  CG  . TYR B  1 85  ? 13.572  -14.979 19.157  1.00 8.54  ? 85  TYR B CG  1 
ATOM   2894  C  CD1 . TYR B  1 85  ? 14.938  -14.885 18.748  1.00 9.67  ? 85  TYR B CD1 1 
ATOM   2895  C  CD2 . TYR B  1 85  ? 12.918  -13.765 19.458  1.00 7.59  ? 85  TYR B CD2 1 
ATOM   2896  C  CE1 . TYR B  1 85  ? 15.575  -13.606 18.673  1.00 11.49 ? 85  TYR B CE1 1 
ATOM   2897  C  CE2 . TYR B  1 85  ? 13.520  -12.466 19.387  1.00 8.34  ? 85  TYR B CE2 1 
ATOM   2898  C  CZ  . TYR B  1 85  ? 14.885  -12.408 18.961  1.00 10.03 ? 85  TYR B CZ  1 
ATOM   2899  O  OH  . TYR B  1 85  ? 15.421  -11.165 18.873  1.00 14.42 ? 85  TYR B OH  1 
ATOM   2900  N  N   . SER B  1 86  ? 11.345  -18.040 21.782  1.00 9.27  ? 86  SER B N   1 
ATOM   2901  C  CA  . SER B  1 86  ? 10.394  -19.126 22.101  1.00 8.84  ? 86  SER B CA  1 
ATOM   2902  C  C   . SER B  1 86  ? 8.984   -18.703 21.613  1.00 8.67  ? 86  SER B C   1 
ATOM   2903  O  O   . SER B  1 86  ? 8.687   -17.500 21.598  1.00 9.60  ? 86  SER B O   1 
ATOM   2904  C  CB  . SER B  1 86  ? 10.335  -19.234 23.674  1.00 11.02 ? 86  SER B CB  1 
ATOM   2905  O  OG  . SER B  1 86  ? 11.580  -19.655 24.204  1.00 13.53 ? 86  SER B OG  1 
ATOM   2906  N  N   . ALA B  1 87  ? 8.233   -19.727 21.241  1.00 9.11  ? 87  ALA B N   1 
ATOM   2907  C  CA  . ALA B  1 87  ? 6.825   -19.491 20.721  1.00 10.46 ? 87  ALA B CA  1 
ATOM   2908  C  C   . ALA B  1 87  ? 5.940   -18.834 21.779  1.00 10.92 ? 87  ALA B C   1 
ATOM   2909  O  O   . ALA B  1 87  ? 6.096   -19.094 23.013  1.00 11.43 ? 87  ALA B O   1 
ATOM   2910  C  CB  . ALA B  1 87  ? 6.212   -20.795 20.229  1.00 11.08 ? 87  ALA B CB  1 
ATOM   2911  N  N   . THR B  1 88  ? 4.977   -17.986 21.314  1.00 9.04  ? 88  THR B N   1 
ATOM   2912  C  CA  . THR B  1 88  ? 3.873   -17.536 22.138  1.00 7.51  ? 88  THR B CA  1 
ATOM   2913  C  C   . THR B  1 88  ? 2.506   -17.818 21.492  1.00 8.51  ? 88  THR B C   1 
ATOM   2914  O  O   . THR B  1 88  ? 1.558   -18.197 22.194  1.00 7.90  ? 88  THR B O   1 
ATOM   2915  C  CB  . THR B  1 88  ? 4.047   -16.048 22.617  1.00 9.60  ? 88  THR B CB  1 
ATOM   2916  O  OG1 . THR B  1 88  ? 2.891   -15.641 23.328  1.00 10.03 ? 88  THR B OG1 1 
ATOM   2917  C  CG2 . THR B  1 88  ? 4.239   -15.037 21.466  1.00 10.84 ? 88  THR B CG2 1 
ATOM   2918  N  N   . GLN B  1 89  ? 2.319   -17.592 20.196  1.00 7.06  ? 89  GLN B N   1 
ATOM   2919  C  CA  . GLN B  1 89  ? 1.029   -17.813 19.512  1.00 6.16  ? 89  GLN B CA  1 
ATOM   2920  C  C   . GLN B  1 89  ? 1.228   -17.736 17.992  1.00 7.23  ? 89  GLN B C   1 
ATOM   2921  O  O   . GLN B  1 89  ? 2.240   -17.185 17.526  1.00 7.85  ? 89  GLN B O   1 
ATOM   2922  C  CB  . GLN B  1 89  ? -0.034  -16.811 19.967  1.00 7.11  ? 89  GLN B CB  1 
ATOM   2923  C  CG  . GLN B  1 89  ? 0.355   -15.355 19.830  1.00 9.65  ? 89  GLN B CG  1 
ATOM   2924  C  CD  . GLN B  1 89  ? -0.335  -14.600 18.643  1.00 8.38  ? 89  GLN B CD  1 
ATOM   2925  O  OE1 . GLN B  1 89  ? -0.810  -13.389 18.829  1.00 14.45 ? 89  GLN B OE1 1 
ATOM   2926  N  NE2 . GLN B  1 89  ? -0.432  -15.205 17.552  1.00 6.34  ? 89  GLN B NE2 1 
ATOM   2927  N  N   . LEU B  1 90  ? 0.261   -18.317 17.288  1.00 6.55  ? 90  LEU B N   1 
ATOM   2928  C  CA  . LEU B  1 90  ? 0.130   -18.107 15.847  1.00 7.43  ? 90  LEU B CA  1 
ATOM   2929  C  C   . LEU B  1 90  ? -1.230  -17.574 15.542  1.00 6.79  ? 90  LEU B C   1 
ATOM   2930  O  O   . LEU B  1 90  ? -2.171  -17.798 16.284  1.00 6.56  ? 90  LEU B O   1 
ATOM   2931  C  CB  . LEU B  1 90  ? 0.503   -19.342 15.038  1.00 6.68  ? 90  LEU B CB  1 
ATOM   2932  C  CG  . LEU B  1 90  ? -0.257  -20.611 15.285  1.00 7.58  ? 90  LEU B CG  1 
ATOM   2933  C  CD1 . LEU B  1 90  ? -1.696  -20.594 14.590  1.00 7.79  ? 90  LEU B CD1 1 
ATOM   2934  C  CD2 . LEU B  1 90  ? 0.553   -21.828 14.643  1.00 7.50  ? 90  LEU B CD2 1 
ATOM   2935  N  N   . HIS B  1 91  ? -1.328  -16.845 14.411  1.00 6.95  ? 91  HIS B N   1 
ATOM   2936  C  CA  . HIS B  1 91  ? -2.663  -16.327 13.952  1.00 4.42  ? 91  HIS B CA  1 
ATOM   2937  C  C   . HIS B  1 91  ? -2.539  -16.046 12.478  1.00 5.68  ? 91  HIS B C   1 
ATOM   2938  O  O   . HIS B  1 91  ? -1.513  -16.267 11.827  1.00 5.99  ? 91  HIS B O   1 
ATOM   2939  C  CB  . HIS B  1 91  ? -3.027  -15.064 14.678  1.00 7.27  ? 91  HIS B CB  1 
ATOM   2940  C  CG  . HIS B  1 91  ? -2.013  -13.980 14.452  1.00 5.94  ? 91  HIS B CG  1 
ATOM   2941  N  ND1 . HIS B  1 91  ? -0.870  -13.859 15.247  1.00 5.76  ? 91  HIS B ND1 1 
ATOM   2942  C  CD2 . HIS B  1 91  ? -1.883  -13.067 13.459  1.00 9.08  ? 91  HIS B CD2 1 
ATOM   2943  C  CE1 . HIS B  1 91  ? -0.076  -12.916 14.721  1.00 5.74  ? 91  HIS B CE1 1 
ATOM   2944  N  NE2 . HIS B  1 91  ? -0.666  -12.423 13.627  1.00 5.05  ? 91  HIS B NE2 1 
ATOM   2945  N  N   . LEU B  1 92  ? -3.651  -15.633 11.863  1.00 6.25  ? 92  LEU B N   1 
ATOM   2946  C  CA  . LEU B  1 92  ? -3.692  -15.400 10.399  1.00 5.97  ? 92  LEU B CA  1 
ATOM   2947  C  C   . LEU B  1 92  ? -4.301  -14.050 10.047  1.00 5.38  ? 92  LEU B C   1 
ATOM   2948  O  O   . LEU B  1 92  ? -4.989  -13.409 10.823  1.00 6.57  ? 92  LEU B O   1 
ATOM   2949  C  CB  . LEU B  1 92  ? -4.511  -16.528 9.716   1.00 7.09  ? 92  LEU B CB  1 
ATOM   2950  C  CG  . LEU B  1 92  ? -4.014  -17.928 9.865   1.00 6.57  ? 92  LEU B CG  1 
ATOM   2951  C  CD1 . LEU B  1 92  ? -4.861  -18.683 10.893  1.00 12.29 ? 92  LEU B CD1 1 
ATOM   2952  C  CD2 . LEU B  1 92  ? -3.868  -18.691 8.534   1.00 10.45 ? 92  LEU B CD2 1 
ATOM   2953  N  N   . HIS B  1 93  ? -4.044  -13.691 8.777   1.00 5.15  ? 93  HIS B N   1 
ATOM   2954  C  CA  . HIS B  1 93  ? -4.634  -12.539 8.198   1.00 5.20  ? 93  HIS B CA  1 
ATOM   2955  C  C   . HIS B  1 93  ? -5.195  -12.903 6.826   1.00 6.01  ? 93  HIS B C   1 
ATOM   2956  O  O   . HIS B  1 93  ? -4.561  -13.683 6.075   1.00 6.26  ? 93  HIS B O   1 
ATOM   2957  C  CB  . HIS B  1 93  ? -3.555  -11.380 7.953   1.00 5.52  ? 93  HIS B CB  1 
ATOM   2958  C  CG  . HIS B  1 93  ? -2.843  -11.004 9.210   1.00 5.02  ? 93  HIS B CG  1 
ATOM   2959  N  ND1 . HIS B  1 93  ? -3.319  -9.969  10.021  1.00 5.52  ? 93  HIS B ND1 1 
ATOM   2960  C  CD2 . HIS B  1 93  ? -1.778  -11.536 9.849   1.00 5.24  ? 93  HIS B CD2 1 
ATOM   2961  C  CE1 . HIS B  1 93  ? -2.500  -9.836  11.097  1.00 5.39  ? 93  HIS B CE1 1 
ATOM   2962  N  NE2 . HIS B  1 93  ? -1.573  -10.760 11.009  1.00 3.99  ? 93  HIS B NE2 1 
ATOM   2963  N  N   . TRP B  1 94  ? -6.329  -12.317 6.435   1.00 4.93  ? 94  TRP B N   1 
ATOM   2964  C  CA  . TRP B  1 94  ? -6.984  -12.697 5.140   1.00 4.42  ? 94  TRP B CA  1 
ATOM   2965  C  C   . TRP B  1 94  ? -7.797  -11.545 4.599   1.00 4.94  ? 94  TRP B C   1 
ATOM   2966  O  O   . TRP B  1 94  ? -7.962  -10.488 5.255   1.00 5.66  ? 94  TRP B O   1 
ATOM   2967  C  CB  . TRP B  1 94  ? -7.830  -14.011 5.333   1.00 5.66  ? 94  TRP B CB  1 
ATOM   2968  C  CG  . TRP B  1 94  ? -8.929  -13.820 6.415   1.00 6.23  ? 94  TRP B CG  1 
ATOM   2969  C  CD1 . TRP B  1 94  ? -10.203 -13.341 6.230   1.00 6.58  ? 94  TRP B CD1 1 
ATOM   2970  C  CD2 . TRP B  1 94  ? -8.794  -14.137 7.821   1.00 4.52  ? 94  TRP B CD2 1 
ATOM   2971  N  NE1 . TRP B  1 94  ? -10.899 -13.326 7.456   1.00 4.98  ? 94  TRP B NE1 1 
ATOM   2972  C  CE2 . TRP B  1 94  ? -10.065 -13.840 8.443   1.00 5.22  ? 94  TRP B CE2 1 
ATOM   2973  C  CE3 . TRP B  1 94  ? -7.748  -14.666 8.626   1.00 5.60  ? 94  TRP B CE3 1 
ATOM   2974  C  CZ2 . TRP B  1 94  ? -10.280 -14.066 9.802   1.00 4.70  ? 94  TRP B CZ2 1 
ATOM   2975  C  CZ3 . TRP B  1 94  ? -7.964  -14.838 9.962   1.00 4.72  ? 94  TRP B CZ3 1 
ATOM   2976  C  CH2 . TRP B  1 94  ? -9.236  -14.522 10.556  1.00 5.06  ? 94  TRP B CH2 1 
ATOM   2977  N  N   . GLY B  1 95  ? -8.381  -11.768 3.372   1.00 5.10  ? 95  GLY B N   1 
ATOM   2978  C  CA  . GLY B  1 95  ? -9.153  -10.725 2.665   1.00 7.17  ? 95  GLY B CA  1 
ATOM   2979  C  C   . GLY B  1 95  ? -10.653 -11.026 2.743   1.00 6.36  ? 95  GLY B C   1 
ATOM   2980  O  O   . GLY B  1 95  ? -11.207 -11.072 3.846   1.00 5.96  ? 95  GLY B O   1 
ATOM   2981  N  N   . ASN B  1 96  ? -11.278 -11.224 1.574   1.00 7.01  ? 96  ASN B N   1 
ATOM   2982  C  CA  . ASN B  1 96  ? -12.746 -11.396 1.645   1.00 7.85  ? 96  ASN B CA  1 
ATOM   2983  C  C   . ASN B  1 96  ? -13.176 -12.127 0.364   1.00 8.47  ? 96  ASN B C   1 
ATOM   2984  O  O   . ASN B  1 96  ? -12.348 -12.239 -0.566  1.00 8.51  ? 96  ASN B O   1 
ATOM   2985  C  CB  . ASN B  1 96  ? -13.517 -10.040 1.776   1.00 9.61  ? 96  ASN B CB  1 
ATOM   2986  C  CG  . ASN B  1 96  ? -13.383 -9.140  0.501   1.00 9.78  ? 96  ASN B CG  1 
ATOM   2987  O  OD1 . ASN B  1 96  ? -14.151 -9.366  -0.501  1.00 18.01 ? 96  ASN B OD1 1 
ATOM   2988  N  ND2 . ASN B  1 96  ? -12.414 -8.256  0.431   1.00 11.89 ? 96  ASN B ND2 1 
ATOM   2989  N  N   . PRO B  1 97  ? -14.415 -12.721 0.365   1.00 8.63  ? 97  PRO B N   1 
ATOM   2990  C  CA  . PRO B  1 97  ? -14.723 -13.566 -0.770  1.00 8.54  ? 97  PRO B CA  1 
ATOM   2991  C  C   . PRO B  1 97  ? -14.717 -12.880 -2.103  1.00 10.70 ? 97  PRO B C   1 
ATOM   2992  O  O   . PRO B  1 97  ? -14.363 -13.562 -3.110  1.00 11.81 ? 97  PRO B O   1 
ATOM   2993  C  CB  . PRO B  1 97  ? -16.081 -14.202 -0.440  1.00 9.81  ? 97  PRO B CB  1 
ATOM   2994  C  CG  . PRO B  1 97  ? -16.067 -14.155 1.151   1.00 11.36 ? 97  PRO B CG  1 
ATOM   2995  C  CD  . PRO B  1 97  ? -15.342 -12.804 1.539   1.00 9.64  ? 97  PRO B CD  1 
ATOM   2996  N  N   . ASN B  1 98  ? -15.047 -11.603 -2.139  1.00 9.30  ? 98  ASN B N   1 
ATOM   2997  C  CA  . ASN B  1 98  ? -15.031 -10.925 -3.493  1.00 13.41 ? 98  ASN B CA  1 
ATOM   2998  C  C   . ASN B  1 98  ? -13.602 -10.474 -3.939  1.00 14.61 ? 98  ASN B C   1 
ATOM   2999  O  O   . ASN B  1 98  ? -13.428 -10.158 -5.128  1.00 16.96 ? 98  ASN B O   1 
ATOM   3000  C  CB  . ASN B  1 98  ? -15.869 -9.630  -3.342  1.00 14.76 ? 98  ASN B CB  1 
ATOM   3001  C  CG  . ASN B  1 98  ? -17.420 -9.880  -3.310  1.00 26.28 ? 98  ASN B CG  1 
ATOM   3002  O  OD1 . ASN B  1 98  ? -17.922 -10.876 -3.857  1.00 33.32 ? 98  ASN B OD1 1 
ATOM   3003  N  ND2 . ASN B  1 98  ? -18.158 -8.931  -2.756  1.00 34.09 ? 98  ASN B ND2 1 
ATOM   3004  N  N   . ASP B  1 99  ? -12.614 -10.468 -3.000  1.00 10.29 ? 99  ASP B N   1 
ATOM   3005  C  CA  . ASP B  1 99  ? -11.249 -10.094 -3.337  1.00 9.40  ? 99  ASP B CA  1 
ATOM   3006  C  C   . ASP B  1 99  ? -10.351 -10.863 -2.411  1.00 8.92  ? 99  ASP B C   1 
ATOM   3007  O  O   . ASP B  1 99  ? -9.821  -10.310 -1.371  1.00 8.63  ? 99  ASP B O   1 
ATOM   3008  C  CB  . ASP B  1 99  ? -11.026 -8.600  -3.139  1.00 9.53  ? 99  ASP B CB  1 
ATOM   3009  C  CG  . ASP B  1 99  ? -9.775  -8.099  -3.833  1.00 12.68 ? 99  ASP B CG  1 
ATOM   3010  O  OD1 . ASP B  1 99  ? -8.990  -8.938  -4.323  1.00 13.78 ? 99  ASP B OD1 1 
ATOM   3011  O  OD2 . ASP B  1 99  ? -9.579  -6.867  -3.892  1.00 14.75 ? 99  ASP B OD2 1 
ATOM   3012  N  N   . PRO B  1 100 ? -10.150 -12.149 -2.716  1.00 8.47  ? 100 PRO B N   1 
ATOM   3013  C  CA  . PRO B  1 100 ? -9.501  -13.086 -1.756  1.00 8.19  ? 100 PRO B CA  1 
ATOM   3014  C  C   . PRO B  1 100 ? -7.992  -13.004 -1.826  1.00 8.63  ? 100 PRO B C   1 
ATOM   3015  O  O   . PRO B  1 100 ? -7.266  -13.911 -2.137  1.00 8.26  ? 100 PRO B O   1 
ATOM   3016  C  CB  . PRO B  1 100 ? -10.037 -14.453 -2.196  1.00 9.14  ? 100 PRO B CB  1 
ATOM   3017  C  CG  . PRO B  1 100 ? -10.181 -14.220 -3.746  1.00 7.85  ? 100 PRO B CG  1 
ATOM   3018  C  CD  . PRO B  1 100 ? -10.683 -12.874 -3.931  1.00 8.73  ? 100 PRO B CD  1 
ATOM   3019  N  N   . HIS B  1 101 ? -7.484  -11.826 -1.472  1.00 7.03  ? 101 HIS B N   1 
ATOM   3020  C  CA  . HIS B  1 101 ? -6.065  -11.490 -1.563  1.00 8.75  ? 101 HIS B CA  1 
ATOM   3021  C  C   . HIS B  1 101 ? -5.616  -10.625 -0.390  1.00 9.31  ? 101 HIS B C   1 
ATOM   3022  O  O   . HIS B  1 101 ? -5.297  -9.392  -0.565  1.00 14.31 ? 101 HIS B O   1 
ATOM   3023  C  CB  . HIS B  1 101 ? -5.728  -10.712 -2.859  1.00 10.01 ? 101 HIS B CB  1 
ATOM   3024  C  CG  . HIS B  1 101 ? -6.255  -11.408 -4.087  1.00 10.71 ? 101 HIS B CG  1 
ATOM   3025  N  ND1 . HIS B  1 101 ? -5.661  -12.516 -4.672  1.00 15.86 ? 101 HIS B ND1 1 
ATOM   3026  C  CD2 . HIS B  1 101 ? -7.429  -11.199 -4.754  1.00 8.39  ? 101 HIS B CD2 1 
ATOM   3027  C  CE1 . HIS B  1 101 ? -6.445  -12.937 -5.680  1.00 14.67 ? 101 HIS B CE1 1 
ATOM   3028  N  NE2 . HIS B  1 101 ? -7.507  -12.153 -5.746  1.00 15.74 ? 101 HIS B NE2 1 
ATOM   3029  N  N   . GLY B  1 102 ? -5.561  -11.264 0.759   1.00 5.81  ? 102 GLY B N   1 
ATOM   3030  C  CA  . GLY B  1 102 ? -5.382  -10.562 2.058   1.00 7.79  ? 102 GLY B CA  1 
ATOM   3031  C  C   . GLY B  1 102 ? -4.089  -10.904 2.876   1.00 5.00  ? 102 GLY B C   1 
ATOM   3032  O  O   . GLY B  1 102 ? -4.084  -10.753 4.121   1.00 6.73  ? 102 GLY B O   1 
ATOM   3033  N  N   . SER B  1 103 ? -2.996  -11.267 2.166   1.00 6.93  ? 103 SER B N   1 
ATOM   3034  C  CA  . SER B  1 103 ? -1.738  -11.349 2.846   1.00 6.58  ? 103 SER B CA  1 
ATOM   3035  C  C   . SER B  1 103 ? -1.361  -9.935  3.331   1.00 5.82  ? 103 SER B C   1 
ATOM   3036  O  O   . SER B  1 103 ? -1.902  -8.968  2.825   1.00 6.47  ? 103 SER B O   1 
ATOM   3037  C  CB  . SER B  1 103 ? -0.610  -11.967 2.013   1.00 6.72  ? 103 SER B CB  1 
ATOM   3038  O  OG  . SER B  1 103 ? -0.297  -11.071 0.892   1.00 5.72  ? 103 SER B OG  1 
ATOM   3039  N  N   . GLU B  1 104 ? -0.430  -9.909  4.279   1.00 4.34  ? 104 GLU B N   1 
ATOM   3040  C  CA  . GLU B  1 104 ? 0.109   -8.603  4.735   1.00 5.13  ? 104 GLU B CA  1 
ATOM   3041  C  C   . GLU B  1 104 ? 1.285   -8.179  3.870   1.00 5.17  ? 104 GLU B C   1 
ATOM   3042  O  O   . GLU B  1 104 ? 1.297   -7.106  3.232   1.00 6.16  ? 104 GLU B O   1 
ATOM   3043  C  CB  . GLU B  1 104 ? 0.517   -8.689  6.247   1.00 5.36  ? 104 GLU B CB  1 
ATOM   3044  C  CG  . GLU B  1 104 ? -0.745  -9.136  7.128   1.00 4.21  ? 104 GLU B CG  1 
ATOM   3045  C  CD  . GLU B  1 104 ? -0.736  -8.261  8.360   1.00 4.86  ? 104 GLU B CD  1 
ATOM   3046  O  OE1 . GLU B  1 104 ? 0.066   -8.592  9.300   1.00 5.49  ? 104 GLU B OE1 1 
ATOM   3047  O  OE2 . GLU B  1 104 ? -1.458  -7.259  8.394   1.00 6.38  ? 104 GLU B OE2 1 
ATOM   3048  N  N   . HIS B  1 105 ? 2.317   -9.031  3.831   1.00 5.40  ? 105 HIS B N   1 
ATOM   3049  C  CA  . HIS B  1 105 ? 3.450   -8.799  2.899   1.00 5.32  ? 105 HIS B CA  1 
ATOM   3050  C  C   . HIS B  1 105 ? 3.006   -9.105  1.462   1.00 6.48  ? 105 HIS B C   1 
ATOM   3051  O  O   . HIS B  1 105 ? 2.116   -9.945  1.237   1.00 7.17  ? 105 HIS B O   1 
ATOM   3052  C  CB  . HIS B  1 105 ? 4.671   -9.653  3.273   1.00 5.87  ? 105 HIS B CB  1 
ATOM   3053  C  CG  . HIS B  1 105 ? 5.234   -9.265  4.592   1.00 5.22  ? 105 HIS B CG  1 
ATOM   3054  N  ND1 . HIS B  1 105 ? 4.824   -9.787  5.823   1.00 5.48  ? 105 HIS B ND1 1 
ATOM   3055  C  CD2 . HIS B  1 105 ? 6.223   -8.352  4.873   1.00 5.37  ? 105 HIS B CD2 1 
ATOM   3056  C  CE1 . HIS B  1 105 ? 5.492   -9.151  6.805   1.00 5.53  ? 105 HIS B CE1 1 
ATOM   3057  N  NE2 . HIS B  1 105 ? 6.356   -8.263  6.258   1.00 6.03  ? 105 HIS B NE2 1 
ATOM   3058  N  N   . THR B  1 106 ? 3.580   -8.300  0.535   1.00 6.69  ? 106 THR B N   1 
ATOM   3059  C  CA  . THR B  1 106 ? 3.369   -8.607  -0.914  1.00 6.07  ? 106 THR B CA  1 
ATOM   3060  C  C   . THR B  1 106 ? 4.748   -8.863  -1.505  1.00 6.66  ? 106 THR B C   1 
ATOM   3061  O  O   . THR B  1 106 ? 5.777   -8.508  -0.937  1.00 6.67  ? 106 THR B O   1 
ATOM   3062  C  CB  . THR B  1 106 ? 2.645   -7.428  -1.583  1.00 7.26  ? 106 THR B CB  1 
ATOM   3063  O  OG1 . THR B  1 106 ? 3.462   -6.197  -1.463  1.00 6.64  ? 106 THR B OG1 1 
ATOM   3064  C  CG2 . THR B  1 106 ? 1.267   -7.179  -0.978  1.00 6.70  ? 106 THR B CG2 1 
ATOM   3065  N  N   . VAL B  1 107 ? 4.727   -9.532  -2.674  1.00 6.23  ? 107 VAL B N   1 
ATOM   3066  C  CA  . VAL B  1 107 ? 6.010   -9.858  -3.359  1.00 6.24  ? 107 VAL B CA  1 
ATOM   3067  C  C   . VAL B  1 107 ? 5.869   -9.322  -4.790  1.00 8.84  ? 107 VAL B C   1 
ATOM   3068  O  O   . VAL B  1 107 ? 4.922   -9.688  -5.532  1.00 9.51  ? 107 VAL B O   1 
ATOM   3069  C  CB  . VAL B  1 107 ? 6.313   -11.415 -3.397  1.00 7.02  ? 107 VAL B CB  1 
ATOM   3070  C  CG1 . VAL B  1 107 ? 7.599   -11.586 -4.187  1.00 9.83  ? 107 VAL B CG1 1 
ATOM   3071  C  CG2 . VAL B  1 107 ? 6.417   -11.958 -1.967  1.00 9.16  ? 107 VAL B CG2 1 
ATOM   3072  N  N   . SER B  1 108 ? 6.766   -8.381  -5.139  1.00 8.81  ? 108 SER B N   1 
ATOM   3073  C  CA  . SER B  1 108 ? 6.714   -7.680  -6.475  1.00 9.67  ? 108 SER B CA  1 
ATOM   3074  C  C   . SER B  1 108 ? 5.300   -7.186  -6.713  1.00 9.22  ? 108 SER B C   1 
ATOM   3075  O  O   . SER B  1 108 ? 4.716   -7.300  -7.784  1.00 10.05 ? 108 SER B O   1 
ATOM   3076  C  CB  . SER B  1 108 ? 7.184   -8.607  -7.548  1.00 10.53 ? 108 SER B CB  1 
ATOM   3077  O  OG  . SER B  1 108 ? 8.492   -8.990  -7.334  1.00 12.29 ? 108 SER B OG  1 
ATOM   3078  N  N   . GLY B  1 109 ? 4.710   -6.562  -5.686  1.00 8.87  ? 109 GLY B N   1 
ATOM   3079  C  CA  . GLY B  1 109 ? 3.397   -5.930  -5.754  1.00 8.10  ? 109 GLY B CA  1 
ATOM   3080  C  C   . GLY B  1 109 ? 2.196   -6.846  -5.628  1.00 10.22 ? 109 GLY B C   1 
ATOM   3081  O  O   . GLY B  1 109 ? 1.009   -6.312  -5.508  1.00 11.37 ? 109 GLY B O   1 
ATOM   3082  N  N   . GLN B  1 110 ? 2.410   -8.159  -5.559  1.00 8.79  ? 110 GLN B N   1 
ATOM   3083  C  CA  . GLN B  1 110 ? 1.313   -9.108  -5.530  1.00 10.63 ? 110 GLN B CA  1 
ATOM   3084  C  C   . GLN B  1 110 ? 0.983   -9.528  -4.082  1.00 7.44  ? 110 GLN B C   1 
ATOM   3085  O  O   . GLN B  1 110 ? 1.852   -9.986  -3.331  1.00 7.85  ? 110 GLN B O   1 
ATOM   3086  C  CB  . GLN B  1 110 ? 1.708   -10.321 -6.313  1.00 12.91 ? 110 GLN B CB  1 
ATOM   3087  C  CG  . GLN B  1 110 ? 2.161   -9.948  -7.783  1.00 14.14 ? 110 GLN B CG  1 
ATOM   3088  C  CD  . GLN B  1 110 ? 1.261   -8.872  -8.436  1.00 16.51 ? 110 GLN B CD  1 
ATOM   3089  O  OE1 . GLN B  1 110 ? 1.748   -7.715  -8.739  1.00 19.48 ? 110 GLN B OE1 1 
ATOM   3090  N  NE2 . GLN B  1 110 ? 0.063   -9.227  -8.712  1.00 14.59 ? 110 GLN B NE2 1 
ATOM   3091  N  N   . HIS B  1 111 ? -0.340  -9.493  -3.759  1.00 8.35  ? 111 HIS B N   1 
ATOM   3092  C  CA  . HIS B  1 111 ? -0.852  -10.094 -2.519  1.00 8.88  ? 111 HIS B CA  1 
ATOM   3093  C  C   . HIS B  1 111 ? -0.946  -11.562 -2.745  1.00 11.99 ? 111 HIS B C   1 
ATOM   3094  O  O   . HIS B  1 111 ? -1.063  -12.049 -3.911  1.00 15.78 ? 111 HIS B O   1 
ATOM   3095  C  CB  . HIS B  1 111 ? -2.264  -9.594  -2.112  1.00 12.40 ? 111 HIS B CB  1 
ATOM   3096  C  CG  . HIS B  1 111 ? -2.246  -8.311  -1.396  1.00 8.88  ? 111 HIS B CG  1 
ATOM   3097  N  ND1 . HIS B  1 111 ? -2.122  -8.223  -0.008  1.00 12.10 ? 111 HIS B ND1 1 
ATOM   3098  C  CD2 . HIS B  1 111 ? -2.123  -7.046  -1.903  1.00 13.89 ? 111 HIS B CD2 1 
ATOM   3099  C  CE1 . HIS B  1 111 ? -2.068  -6.917  0.288   1.00 12.27 ? 111 HIS B CE1 1 
ATOM   3100  N  NE2 . HIS B  1 111 ? -2.057  -6.197  -0.837  1.00 18.25 ? 111 HIS B NE2 1 
ATOM   3101  N  N   . PHE B  1 112 ? -0.767  -12.272 -1.687  1.00 7.67  ? 112 PHE B N   1 
ATOM   3102  C  CA  . PHE B  1 112 ? -1.170  -13.668 -1.592  1.00 7.29  ? 112 PHE B CA  1 
ATOM   3103  C  C   . PHE B  1 112 ? -2.582  -13.763 -0.954  1.00 7.03  ? 112 PHE B C   1 
ATOM   3104  O  O   . PHE B  1 112 ? -3.172  -12.745 -0.478  1.00 7.43  ? 112 PHE B O   1 
ATOM   3105  C  CB  . PHE B  1 112 ? -0.112  -14.535 -0.854  1.00 7.47  ? 112 PHE B CB  1 
ATOM   3106  C  CG  . PHE B  1 112 ? 1.123   -14.713 -1.685  1.00 8.07  ? 112 PHE B CG  1 
ATOM   3107  C  CD1 . PHE B  1 112 ? 2.013   -13.646 -1.820  1.00 11.41 ? 112 PHE B CD1 1 
ATOM   3108  C  CD2 . PHE B  1 112 ? 1.328   -15.956 -2.352  1.00 11.43 ? 112 PHE B CD2 1 
ATOM   3109  C  CE1 . PHE B  1 112 ? 3.183   -13.779 -2.683  1.00 12.91 ? 112 PHE B CE1 1 
ATOM   3110  C  CE2 . PHE B  1 112 ? 2.537   -16.123 -3.185  1.00 15.31 ? 112 PHE B CE2 1 
ATOM   3111  C  CZ  . PHE B  1 112 ? 3.390   -15.027 -3.332  1.00 17.28 ? 112 PHE B CZ  1 
ATOM   3112  N  N   . ALA B  1 113 ? -3.179  -14.984 -1.027  1.00 6.22  ? 113 ALA B N   1 
ATOM   3113  C  CA  . ALA B  1 113 ? -4.542  -15.121 -0.463  1.00 6.19  ? 113 ALA B CA  1 
ATOM   3114  C  C   . ALA B  1 113 ? -4.630  -14.752 1.044   1.00 5.55  ? 113 ALA B C   1 
ATOM   3115  O  O   . ALA B  1 113 ? -5.607  -14.145 1.513   1.00 6.39  ? 113 ALA B O   1 
ATOM   3116  C  CB  . ALA B  1 113 ? -5.148  -16.515 -0.687  1.00 7.61  ? 113 ALA B CB  1 
ATOM   3117  N  N   . ALA B  1 114 ? -3.642  -15.225 1.829   1.00 6.32  ? 114 ALA B N   1 
ATOM   3118  C  CA  . ALA B  1 114 ? -3.632  -14.993 3.275   1.00 5.40  ? 114 ALA B CA  1 
ATOM   3119  C  C   . ALA B  1 114 ? -2.203  -15.124 3.755   1.00 4.88  ? 114 ALA B C   1 
ATOM   3120  O  O   . ALA B  1 114 ? -1.296  -15.371 3.001   1.00 5.35  ? 114 ALA B O   1 
ATOM   3121  C  CB  . ALA B  1 114 ? -4.547  -16.103 3.962   1.00 6.47  ? 114 ALA B CB  1 
ATOM   3122  N  N   . GLU B  1 115 ? -2.062  -14.946 5.080   1.00 4.61  ? 115 GLU B N   1 
ATOM   3123  C  CA  . GLU B  1 115 ? -0.702  -15.062 5.659   1.00 5.26  ? 115 GLU B CA  1 
ATOM   3124  C  C   . GLU B  1 115 ? -0.840  -15.569 7.083   1.00 5.09  ? 115 GLU B C   1 
ATOM   3125  O  O   . GLU B  1 115 ? -1.710  -15.149 7.859   1.00 6.37  ? 115 GLU B O   1 
ATOM   3126  C  CB  . GLU B  1 115 ? -0.069  -13.647 5.664   1.00 6.57  ? 115 GLU B CB  1 
ATOM   3127  C  CG  . GLU B  1 115 ? 1.429   -13.569 6.083   1.00 5.66  ? 115 GLU B CG  1 
ATOM   3128  C  CD  . GLU B  1 115 ? 2.095   -12.237 5.731   1.00 5.59  ? 115 GLU B CD  1 
ATOM   3129  O  OE1 . GLU B  1 115 ? 2.990   -11.771 6.474   1.00 6.25  ? 115 GLU B OE1 1 
ATOM   3130  O  OE2 . GLU B  1 115 ? 1.708   -11.661 4.660   1.00 5.52  ? 115 GLU B OE2 1 
ATOM   3131  N  N   . LEU B  1 116 ? 0.078   -16.521 7.444   1.00 5.77  ? 116 LEU B N   1 
ATOM   3132  C  CA  . LEU B  1 116 ? 0.215   -17.047 8.809   1.00 5.99  ? 116 LEU B CA  1 
ATOM   3133  C  C   . LEU B  1 116 ? 1.390   -16.378 9.487   1.00 5.91  ? 116 LEU B C   1 
ATOM   3134  O  O   . LEU B  1 116 ? 2.492   -16.260 8.882   1.00 5.34  ? 116 LEU B O   1 
ATOM   3135  C  CB  . LEU B  1 116 ? 0.399   -18.551 8.760   1.00 6.86  ? 116 LEU B CB  1 
ATOM   3136  C  CG  . LEU B  1 116 ? 0.800   -19.243 10.068  1.00 6.43  ? 116 LEU B CG  1 
ATOM   3137  C  CD1 . LEU B  1 116 ? -0.430  -19.470 10.881  1.00 7.67  ? 116 LEU B CD1 1 
ATOM   3138  C  CD2 . LEU B  1 116 ? 1.460   -20.659 9.750   1.00 8.77  ? 116 LEU B CD2 1 
ATOM   3139  N  N   . HIS B  1 117 ? 1.204   -16.006 10.731  1.00 6.42  ? 117 HIS B N   1 
ATOM   3140  C  CA  . HIS B  1 117 ? 2.262   -15.449 11.610  1.00 5.34  ? 117 HIS B CA  1 
ATOM   3141  C  C   . HIS B  1 117 ? 2.501   -16.350 12.828  1.00 6.12  ? 117 HIS B C   1 
ATOM   3142  O  O   . HIS B  1 117 ? 1.500   -16.646 13.563  1.00 6.62  ? 117 HIS B O   1 
ATOM   3143  C  CB  . HIS B  1 117 ? 1.857   -14.038 12.110  1.00 6.14  ? 117 HIS B CB  1 
ATOM   3144  C  CG  . HIS B  1 117 ? 1.997   -13.034 10.978  1.00 5.50  ? 117 HIS B CG  1 
ATOM   3145  N  ND1 . HIS B  1 117 ? 1.351   -11.814 10.972  1.00 6.47  ? 117 HIS B ND1 1 
ATOM   3146  C  CD2 . HIS B  1 117 ? 2.589   -13.144 9.763   1.00 5.00  ? 117 HIS B CD2 1 
ATOM   3147  C  CE1 . HIS B  1 117 ? 1.602   -11.187 9.845   1.00 5.66  ? 117 HIS B CE1 1 
ATOM   3148  N  NE2 . HIS B  1 117 ? 2.392   -11.948 9.099   1.00 5.64  ? 117 HIS B NE2 1 
ATOM   3149  N  N   . ILE B  1 118 ? 3.729   -16.859 12.972  1.00 6.31  ? 118 ILE B N   1 
ATOM   3150  C  CA  . ILE B  1 118 ? 4.129   -17.600 14.167  1.00 7.00  ? 118 ILE B CA  1 
ATOM   3151  C  C   . ILE B  1 118 ? 5.000   -16.719 15.066  1.00 6.63  ? 118 ILE B C   1 
ATOM   3152  O  O   . ILE B  1 118 ? 6.118   -16.318 14.645  1.00 6.88  ? 118 ILE B O   1 
ATOM   3153  C  CB  . ILE B  1 118 ? 4.812   -18.900 13.785  1.00 6.71  ? 118 ILE B CB  1 
ATOM   3154  C  CG1 . ILE B  1 118 ? 3.998   -19.678 12.813  1.00 6.58  ? 118 ILE B CG1 1 
ATOM   3155  C  CG2 . ILE B  1 118 ? 5.031   -19.811 15.114  1.00 8.81  ? 118 ILE B CG2 1 
ATOM   3156  C  CD1 . ILE B  1 118 ? 4.679   -21.067 12.292  1.00 10.11 ? 118 ILE B CD1 1 
ATOM   3157  N  N   . VAL B  1 119 ? 4.440   -16.239 16.175  1.00 8.35  ? 119 VAL B N   1 
ATOM   3158  C  CA  . VAL B  1 119 ? 5.001   -15.224 16.958  1.00 6.99  ? 119 VAL B CA  1 
ATOM   3159  C  C   . VAL B  1 119 ? 5.912   -15.882 18.019  1.00 8.14  ? 119 VAL B C   1 
ATOM   3160  O  O   . VAL B  1 119 ? 5.445   -16.733 18.765  1.00 9.01  ? 119 VAL B O   1 
ATOM   3161  C  CB  . VAL B  1 119 ? 3.913   -14.360 17.653  1.00 6.53  ? 119 VAL B CB  1 
ATOM   3162  C  CG1 . VAL B  1 119 ? 4.528   -13.207 18.313  1.00 7.88  ? 119 VAL B CG1 1 
ATOM   3163  C  CG2 . VAL B  1 119 ? 2.930   -13.822 16.491  1.00 7.12  ? 119 VAL B CG2 1 
ATOM   3164  N  N   . HIS B  1 120 ? 7.065   -15.236 18.263  1.00 8.31  ? 120 HIS B N   1 
ATOM   3165  C  CA  . HIS B  1 120 ? 8.065   -15.677 19.268  1.00 8.24  ? 120 HIS B CA  1 
ATOM   3166  C  C   . HIS B  1 120 ? 8.578   -14.533 20.023  1.00 9.27  ? 120 HIS B C   1 
ATOM   3167  O  O   . HIS B  1 120 ? 8.634   -13.344 19.546  1.00 8.88  ? 120 HIS B O   1 
ATOM   3168  C  CB  . HIS B  1 120 ? 9.314   -16.437 18.634  1.00 8.63  ? 120 HIS B CB  1 
ATOM   3169  C  CG  . HIS B  1 120 ? 8.994   -17.557 17.765  1.00 7.55  ? 120 HIS B CG  1 
ATOM   3170  N  ND1 . HIS B  1 120 ? 8.287   -17.485 16.540  1.00 8.91  ? 120 HIS B ND1 1 
ATOM   3171  C  CD2 . HIS B  1 120 ? 9.210   -18.874 17.953  1.00 9.81  ? 120 HIS B CD2 1 
ATOM   3172  C  CE1 . HIS B  1 120 ? 8.220   -18.677 15.994  1.00 8.80  ? 120 HIS B CE1 1 
ATOM   3173  N  NE2 . HIS B  1 120 ? 8.777   -19.555 16.865  1.00 10.08 ? 120 HIS B NE2 1 
ATOM   3174  N  N   . TYR B  1 121 ? 9.116   -14.806 21.251  1.00 8.46  ? 121 TYR B N   1 
ATOM   3175  C  CA  . TYR B  1 121 ? 9.732   -13.654 21.986  1.00 10.30 ? 121 TYR B CA  1 
ATOM   3176  C  C   . TYR B  1 121 ? 11.158  -14.038 22.425  1.00 9.94  ? 121 TYR B C   1 
ATOM   3177  O  O   . TYR B  1 121 ? 11.452  -15.254 22.509  1.00 10.30 ? 121 TYR B O   1 
ATOM   3178  C  CB  . TYR B  1 121 ? 8.876   -13.272 23.272  1.00 10.01 ? 121 TYR B CB  1 
ATOM   3179  C  CG  . TYR B  1 121 ? 8.779   -14.418 24.311  1.00 10.35 ? 121 TYR B CG  1 
ATOM   3180  C  CD1 . TYR B  1 121 ? 9.608   -14.335 25.469  1.00 10.23 ? 121 TYR B CD1 1 
ATOM   3181  C  CD2 . TYR B  1 121 ? 7.912   -15.512 24.166  1.00 11.58 ? 121 TYR B CD2 1 
ATOM   3182  C  CE1 . TYR B  1 121 ? 9.555   -15.374 26.412  1.00 10.07 ? 121 TYR B CE1 1 
ATOM   3183  C  CE2 . TYR B  1 121 ? 7.834   -16.528 25.126  1.00 9.55  ? 121 TYR B CE2 1 
ATOM   3184  C  CZ  . TYR B  1 121 ? 8.735   -16.456 26.220  1.00 10.90 ? 121 TYR B CZ  1 
ATOM   3185  O  OH  . TYR B  1 121 ? 8.631   -17.446 27.222  1.00 13.24 ? 121 TYR B OH  1 
ATOM   3186  N  N   . ASN B  1 122 ? 11.889  -12.988 22.748  1.00 10.97 ? 122 ASN B N   1 
ATOM   3187  C  CA  . ASN B  1 122 ? 13.349  -13.197 23.154  1.00 11.75 ? 122 ASN B CA  1 
ATOM   3188  C  C   . ASN B  1 122 ? 13.356  -13.735 24.661  1.00 10.76 ? 122 ASN B C   1 
ATOM   3189  O  O   . ASN B  1 122 ? 13.273  -12.892 25.587  1.00 11.77 ? 122 ASN B O   1 
ATOM   3190  C  CB  . ASN B  1 122 ? 14.132  -11.947 22.976  1.00 11.54 ? 122 ASN B CB  1 
ATOM   3191  C  CG  . ASN B  1 122 ? 15.615  -12.204 23.082  1.00 14.15 ? 122 ASN B CG  1 
ATOM   3192  O  OD1 . ASN B  1 122 ? 16.050  -13.088 23.851  1.00 14.93 ? 122 ASN B OD1 1 
ATOM   3193  N  ND2 . ASN B  1 122 ? 16.401  -11.393 22.366  1.00 15.88 ? 122 ASN B ND2 1 
ATOM   3194  N  N   . SER B  1 123 ? 13.531  -15.055 24.734  1.00 11.16 ? 123 SER B N   1 
ATOM   3195  C  CA  . SER B  1 123 ? 13.388  -15.731 26.065  1.00 15.79 ? 123 SER B CA  1 
ATOM   3196  C  C   . SER B  1 123 ? 14.755  -15.597 26.801  1.00 17.75 ? 123 SER B C   1 
ATOM   3197  O  O   . SER B  1 123 ? 14.800  -15.820 28.054  1.00 18.72 ? 123 SER B O   1 
ATOM   3198  C  CB  . SER B  1 123 ? 12.893  -17.156 25.936  1.00 14.87 ? 123 SER B CB  1 
ATOM   3199  O  OG  . SER B  1 123 ? 13.505  -17.858 24.958  1.00 15.05 ? 123 SER B OG  1 
ATOM   3200  N  N   . ASP B  1 124 ? 15.863  -15.282 26.092  1.00 18.27 ? 124 ASP B N   1 
ATOM   3201  C  CA  . ASP B  1 124 ? 17.113  -14.960 26.804  1.00 15.32 ? 124 ASP B CA  1 
ATOM   3202  C  C   . ASP B  1 124 ? 17.081  -13.641 27.531  1.00 19.38 ? 124 ASP B C   1 
ATOM   3203  O  O   . ASP B  1 124 ? 17.710  -13.549 28.618  1.00 20.92 ? 124 ASP B O   1 
ATOM   3204  C  CB  . ASP B  1 124 ? 18.252  -14.948 25.766  1.00 17.57 ? 124 ASP B CB  1 
ATOM   3205  C  CG  . ASP B  1 124 ? 18.569  -16.355 25.135  1.00 15.66 ? 124 ASP B CG  1 
ATOM   3206  O  OD1 . ASP B  1 124 ? 18.196  -17.487 25.669  1.00 20.99 ? 124 ASP B OD1 1 
ATOM   3207  O  OD2 . ASP B  1 124 ? 19.304  -16.420 24.107  1.00 22.72 ? 124 ASP B OD2 1 
ATOM   3208  N  N   . LEU B  1 125 ? 16.384  -12.589 27.024  1.00 16.94 ? 125 LEU B N   1 
ATOM   3209  C  CA  . LEU B  1 125 ? 16.417  -11.258 27.602  1.00 14.42 ? 125 LEU B CA  1 
ATOM   3210  C  C   . LEU B  1 125 ? 15.192  -11.005 28.500  1.00 14.17 ? 125 LEU B C   1 
ATOM   3211  O  O   . LEU B  1 125 ? 15.212  -10.149 29.408  1.00 17.56 ? 125 LEU B O   1 
ATOM   3212  C  CB  . LEU B  1 125 ? 16.522  -10.137 26.570  1.00 15.01 ? 125 LEU B CB  1 
ATOM   3213  C  CG  . LEU B  1 125 ? 17.827  -10.096 25.740  1.00 13.87 ? 125 LEU B CG  1 
ATOM   3214  C  CD1 . LEU B  1 125 ? 17.771  -9.004  24.638  1.00 18.95 ? 125 LEU B CD1 1 
ATOM   3215  C  CD2 . LEU B  1 125 ? 19.070  -9.918  26.742  1.00 17.06 ? 125 LEU B CD2 1 
ATOM   3216  N  N   . TYR B  1 126 ? 14.079  -11.711 28.151  1.00 14.14 ? 126 TYR B N   1 
ATOM   3217  C  CA  . TYR B  1 126 ? 12.749  -11.363 28.748  1.00 12.92 ? 126 TYR B CA  1 
ATOM   3218  C  C   . TYR B  1 126 ? 11.957  -12.582 29.263  1.00 10.30 ? 126 TYR B C   1 
ATOM   3219  O  O   . TYR B  1 126 ? 12.054  -13.657 28.734  1.00 12.52 ? 126 TYR B O   1 
ATOM   3220  C  CB  . TYR B  1 126 ? 11.892  -10.557 27.715  1.00 12.57 ? 126 TYR B CB  1 
ATOM   3221  C  CG  . TYR B  1 126 ? 12.650  -9.372  27.138  1.00 14.38 ? 126 TYR B CG  1 
ATOM   3222  C  CD1 . TYR B  1 126 ? 12.998  -9.341  25.755  1.00 12.63 ? 126 TYR B CD1 1 
ATOM   3223  C  CD2 . TYR B  1 126 ? 13.066  -8.344  27.938  1.00 13.63 ? 126 TYR B CD2 1 
ATOM   3224  C  CE1 . TYR B  1 126 ? 13.837  -8.298  25.272  1.00 11.77 ? 126 TYR B CE1 1 
ATOM   3225  C  CE2 . TYR B  1 126 ? 13.855  -7.247  27.483  1.00 14.62 ? 126 TYR B CE2 1 
ATOM   3226  C  CZ  . TYR B  1 126 ? 14.250  -7.211  26.094  1.00 14.98 ? 126 TYR B CZ  1 
ATOM   3227  O  OH  . TYR B  1 126 ? 15.022  -6.099  25.610  1.00 14.59 ? 126 TYR B OH  1 
ATOM   3228  N  N   . PRO B  1 127 ? 11.135  -12.315 30.329  1.00 14.99 ? 127 PRO B N   1 
ATOM   3229  C  CA  . PRO B  1 127 ? 10.432  -13.412 30.964  1.00 14.10 ? 127 PRO B CA  1 
ATOM   3230  C  C   . PRO B  1 127 ? 9.241   -14.003 30.164  1.00 14.81 ? 127 PRO B C   1 
ATOM   3231  O  O   . PRO B  1 127 ? 8.942   -15.147 30.274  1.00 14.73 ? 127 PRO B O   1 
ATOM   3232  C  CB  . PRO B  1 127 ? 9.941   -12.774 32.285  1.00 14.41 ? 127 PRO B CB  1 
ATOM   3233  C  CG  . PRO B  1 127 ? 9.852   -11.331 32.107  1.00 13.10 ? 127 PRO B CG  1 
ATOM   3234  C  CD  . PRO B  1 127 ? 11.052  -11.086 31.092  1.00 14.49 ? 127 PRO B CD  1 
ATOM   3235  N  N   . ASP B  1 128 ? 8.609   -13.142 29.346  1.00 12.39 ? 128 ASP B N   1 
ATOM   3236  C  CA  . ASP B  1 128 ? 7.398   -13.537 28.630  1.00 11.64 ? 128 ASP B CA  1 
ATOM   3237  C  C   . ASP B  1 128 ? 7.192   -12.606 27.460  1.00 11.08 ? 128 ASP B C   1 
ATOM   3238  O  O   . ASP B  1 128 ? 7.887   -11.555 27.269  1.00 9.83  ? 128 ASP B O   1 
ATOM   3239  C  CB  . ASP B  1 128 ? 6.199   -13.563 29.662  1.00 13.14 ? 128 ASP B CB  1 
ATOM   3240  C  CG  . ASP B  1 128 ? 5.979   -12.261 30.394  1.00 15.19 ? 128 ASP B CG  1 
ATOM   3241  O  OD1 . ASP B  1 128 ? 6.048   -11.179 29.772  1.00 14.36 ? 128 ASP B OD1 1 
ATOM   3242  O  OD2 . ASP B  1 128 ? 5.678   -12.335 31.603  1.00 23.45 ? 128 ASP B OD2 1 
ATOM   3243  N  N   . ALA B  1 129 ? 6.140   -13.006 26.695  1.00 8.62  ? 129 ALA B N   1 
ATOM   3244  C  CA  . ALA B  1 129 ? 5.946   -12.252 25.472  1.00 10.57 ? 129 ALA B CA  1 
ATOM   3245  C  C   . ALA B  1 129 ? 5.397   -10.843 25.698  1.00 9.88  ? 129 ALA B C   1 
ATOM   3246  O  O   . ALA B  1 129 ? 5.738   -9.883  24.943  1.00 11.56 ? 129 ALA B O   1 
ATOM   3247  C  CB  . ALA B  1 129 ? 4.984   -12.996 24.553  1.00 12.74 ? 129 ALA B CB  1 
ATOM   3248  N  N   A SER B  1 130 ? 4.513   -10.669 26.685  0.50 10.59 ? 130 SER B N   1 
ATOM   3249  N  N   B SER B  1 130 ? 4.507   -10.645 26.688  0.50 10.65 ? 130 SER B N   1 
ATOM   3250  C  CA  A SER B  1 130 ? 4.009   -9.355  26.898  0.50 10.76 ? 130 SER B CA  1 
ATOM   3251  C  CA  B SER B  1 130 ? 4.026   -9.307  26.935  0.50 11.59 ? 130 SER B CA  1 
ATOM   3252  C  C   A SER B  1 130 ? 5.152   -8.353  27.346  0.50 11.28 ? 130 SER B C   1 
ATOM   3253  C  C   B SER B  1 130 ? 5.226   -8.393  27.272  0.50 11.44 ? 130 SER B C   1 
ATOM   3254  O  O   A SER B  1 130 ? 5.207   -7.158  26.940  0.50 12.14 ? 130 SER B O   1 
ATOM   3255  O  O   B SER B  1 130 ? 5.403   -7.320  26.727  0.50 11.88 ? 130 SER B O   1 
ATOM   3256  C  CB  A SER B  1 130 ? 2.805   -9.386  27.875  0.50 13.37 ? 130 SER B CB  1 
ATOM   3257  C  CB  B SER B  1 130 ? 3.031   -9.267  28.116  0.50 13.29 ? 130 SER B CB  1 
ATOM   3258  O  OG  A SER B  1 130 ? 2.644   -8.108  28.425  0.50 14.70 ? 130 SER B OG  1 
ATOM   3259  O  OG  B SER B  1 130 ? 3.641   -9.888  29.209  0.50 19.48 ? 130 SER B OG  1 
ATOM   3260  N  N   . THR B  1 131 ? 6.090   -8.852  28.188  1.00 12.26 ? 131 THR B N   1 
ATOM   3261  C  CA  . THR B  1 131 ? 7.184   -7.980  28.656  1.00 13.86 ? 131 THR B CA  1 
ATOM   3262  C  C   . THR B  1 131 ? 8.156   -7.685  27.520  1.00 12.22 ? 131 THR B C   1 
ATOM   3263  O  O   . THR B  1 131 ? 8.683   -6.561  27.403  1.00 13.88 ? 131 THR B O   1 
ATOM   3264  C  CB  . THR B  1 131 ? 7.883   -8.677  29.873  1.00 15.49 ? 131 THR B CB  1 
ATOM   3265  O  OG1 . THR B  1 131 ? 6.872   -8.984  30.887  1.00 15.94 ? 131 THR B OG1 1 
ATOM   3266  C  CG2 . THR B  1 131 ? 8.884   -7.761  30.424  1.00 16.01 ? 131 THR B CG2 1 
ATOM   3267  N  N   . ALA B  1 132 ? 8.336   -8.677  26.717  1.00 11.87 ? 132 ALA B N   1 
ATOM   3268  C  CA  . ALA B  1 132 ? 9.281   -8.586  25.456  1.00 11.87 ? 132 ALA B CA  1 
ATOM   3269  C  C   . ALA B  1 132 ? 8.755   -7.567  24.396  1.00 14.40 ? 132 ALA B C   1 
ATOM   3270  O  O   . ALA B  1 132 ? 9.560   -6.932  23.687  1.00 12.24 ? 132 ALA B O   1 
ATOM   3271  C  CB  . ALA B  1 132 ? 9.451   -9.907  24.797  1.00 11.78 ? 132 ALA B CB  1 
ATOM   3272  N  N   . SER B  1 133 ? 7.406   -7.504  24.310  1.00 11.84 ? 133 SER B N   1 
ATOM   3273  C  CA  . SER B  1 133 ? 6.790   -6.837  23.152  1.00 11.27 ? 133 SER B CA  1 
ATOM   3274  C  C   . SER B  1 133 ? 7.207   -5.373  22.935  1.00 11.07 ? 133 SER B C   1 
ATOM   3275  O  O   . SER B  1 133 ? 7.196   -4.918  21.764  1.00 11.52 ? 133 SER B O   1 
ATOM   3276  C  CB  . SER B  1 133 ? 5.290   -7.066  23.323  1.00 11.90 ? 133 SER B CB  1 
ATOM   3277  O  OG  . SER B  1 133 ? 4.845   -6.234  24.276  1.00 14.21 ? 133 SER B OG  1 
ATOM   3278  N  N   . ASN B  1 134 ? 7.489   -4.575  23.950  1.00 12.15 ? 134 ASN B N   1 
ATOM   3279  C  CA  . ASN B  1 134 ? 7.883   -3.195  23.729  1.00 12.87 ? 134 ASN B CA  1 
ATOM   3280  C  C   . ASN B  1 134 ? 9.338   -2.965  24.103  1.00 13.29 ? 134 ASN B C   1 
ATOM   3281  O  O   . ASN B  1 134 ? 9.655   -1.815  24.522  1.00 14.93 ? 134 ASN B O   1 
ATOM   3282  C  CB  . ASN B  1 134 ? 6.957   -2.126  24.394  1.00 13.69 ? 134 ASN B CB  1 
ATOM   3283  C  CG  . ASN B  1 134 ? 6.930   -2.238  25.883  1.00 17.10 ? 134 ASN B CG  1 
ATOM   3284  O  OD1 . ASN B  1 134 ? 7.422   -3.272  26.472  1.00 18.58 ? 134 ASN B OD1 1 
ATOM   3285  N  ND2 . ASN B  1 134 ? 6.293   -1.204  26.529  1.00 18.00 ? 134 ASN B ND2 1 
ATOM   3286  N  N   . LYS B  1 135 ? 10.149  -4.058  23.988  1.00 12.78 ? 135 LYS B N   1 
ATOM   3287  C  CA  . LYS B  1 135 ? 11.572  -3.871  24.338  1.00 15.65 ? 135 LYS B CA  1 
ATOM   3288  C  C   . LYS B  1 135 ? 12.446  -4.188  23.136  1.00 13.01 ? 135 LYS B C   1 
ATOM   3289  O  O   . LYS B  1 135 ? 12.102  -5.006  22.305  1.00 13.02 ? 135 LYS B O   1 
ATOM   3290  C  CB  . LYS B  1 135 ? 11.899  -4.691  25.657  1.00 16.57 ? 135 LYS B CB  1 
ATOM   3291  C  CG  . LYS B  1 135 ? 11.300  -3.920  26.861  1.00 17.89 ? 135 LYS B CG  1 
ATOM   3292  C  CD  . LYS B  1 135 ? 11.359  -4.703  28.183  1.00 20.43 ? 135 LYS B CD  1 
ATOM   3293  C  CE  . LYS B  1 135 ? 10.321  -4.126  29.217  1.00 20.56 ? 135 LYS B CE  1 
ATOM   3294  N  NZ  . LYS B  1 135 ? 8.746   -4.347  28.899  1.00 26.02 ? 135 LYS B NZ  1 
ATOM   3295  N  N   . SER B  1 136 ? 13.675  -3.715  23.254  1.00 12.99 ? 136 SER B N   1 
ATOM   3296  C  CA  . SER B  1 136 ? 14.665  -3.893  22.169  1.00 13.23 ? 136 SER B CA  1 
ATOM   3297  C  C   . SER B  1 136 ? 14.870  -5.402  21.975  1.00 13.57 ? 136 SER B C   1 
ATOM   3298  O  O   . SER B  1 136 ? 15.058  -6.198  22.964  1.00 13.76 ? 136 SER B O   1 
ATOM   3299  C  CB  . SER B  1 136 ? 15.987  -3.263  22.684  1.00 14.29 ? 136 SER B CB  1 
ATOM   3300  O  OG  . SER B  1 136 ? 16.972  -3.583  21.675  1.00 13.67 ? 136 SER B OG  1 
ATOM   3301  N  N   . GLU B  1 137 ? 14.897  -5.845  20.744  1.00 12.33 ? 137 GLU B N   1 
ATOM   3302  C  CA  . GLU B  1 137 ? 15.115  -7.167  20.417  1.00 10.29 ? 137 GLU B CA  1 
ATOM   3303  C  C   . GLU B  1 137 ? 14.061  -8.125  20.962  1.00 12.19 ? 137 GLU B C   1 
ATOM   3304  O  O   . GLU B  1 137 ? 14.286  -9.356  21.063  1.00 13.18 ? 137 GLU B O   1 
ATOM   3305  C  CB  . GLU B  1 137 ? 16.530  -7.649  20.827  1.00 11.34 ? 137 GLU B CB  1 
ATOM   3306  C  CG  . GLU B  1 137 ? 17.600  -6.758  20.308  1.00 14.94 ? 137 GLU B CG  1 
ATOM   3307  C  CD  . GLU B  1 137 ? 18.974  -7.234  20.850  1.00 21.51 ? 137 GLU B CD  1 
ATOM   3308  O  OE1 . GLU B  1 137 ? 19.292  -8.475  20.817  1.00 24.15 ? 137 GLU B OE1 1 
ATOM   3309  O  OE2 . GLU B  1 137 ? 19.738  -6.361  21.336  1.00 16.83 ? 137 GLU B OE2 1 
ATOM   3310  N  N   . GLY B  1 138 ? 12.860  -7.551  21.178  1.00 10.70 ? 138 GLY B N   1 
ATOM   3311  C  CA  . GLY B  1 138 ? 11.865  -8.400  21.873  1.00 11.93 ? 138 GLY B CA  1 
ATOM   3312  C  C   . GLY B  1 138 ? 11.218  -9.563  21.159  1.00 10.47 ? 138 GLY B C   1 
ATOM   3313  O  O   . GLY B  1 138 ? 10.913  -10.634 21.744  1.00 11.10 ? 138 GLY B O   1 
ATOM   3314  N  N   . LEU B  1 139 ? 10.927  -9.382  19.812  1.00 9.73  ? 139 LEU B N   1 
ATOM   3315  C  CA  . LEU B  1 139 ? 10.108  -10.330 19.158  1.00 9.07  ? 139 LEU B CA  1 
ATOM   3316  C  C   . LEU B  1 139 ? 10.683  -10.856 17.829  1.00 7.60  ? 139 LEU B C   1 
ATOM   3317  O  O   . LEU B  1 139 ? 11.465  -10.072 17.204  1.00 7.64  ? 139 LEU B O   1 
ATOM   3318  C  CB  . LEU B  1 139 ? 8.696   -9.657  18.853  1.00 10.36 ? 139 LEU B CB  1 
ATOM   3319  C  CG  . LEU B  1 139 ? 7.962   -9.149  20.123  1.00 9.44  ? 139 LEU B CG  1 
ATOM   3320  C  CD1 . LEU B  1 139 ? 6.680   -8.388  19.665  1.00 12.40 ? 139 LEU B CD1 1 
ATOM   3321  C  CD2 . LEU B  1 139 ? 7.530   -10.409 20.988  1.00 11.99 ? 139 LEU B CD2 1 
ATOM   3322  N  N   . ALA B  1 140 ? 10.304  -12.053 17.394  1.00 7.42  ? 140 ALA B N   1 
ATOM   3323  C  CA  . ALA B  1 140 ? 10.655  -12.616 16.107  1.00 7.53  ? 140 ALA B CA  1 
ATOM   3324  C  C   . ALA B  1 140 ? 9.404   -13.263 15.585  1.00 9.48  ? 140 ALA B C   1 
ATOM   3325  O  O   . ALA B  1 140 ? 8.809   -14.137 16.254  1.00 9.39  ? 140 ALA B O   1 
ATOM   3326  C  CB  . ALA B  1 140 ? 11.812  -13.603 16.158  1.00 10.32 ? 140 ALA B CB  1 
ATOM   3327  N  N   . VAL B  1 141 ? 8.982   -12.880 14.354  1.00 7.15  ? 141 VAL B N   1 
ATOM   3328  C  CA  . VAL B  1 141 ? 7.792   -13.509 13.766  1.00 7.76  ? 141 VAL B CA  1 
ATOM   3329  C  C   . VAL B  1 141 ? 8.139   -14.213 12.497  1.00 6.26  ? 141 VAL B C   1 
ATOM   3330  O  O   . VAL B  1 141 ? 8.940   -13.635 11.691  1.00 7.59  ? 141 VAL B O   1 
ATOM   3331  C  CB  . VAL B  1 141 ? 6.657   -12.458 13.458  1.00 6.37  ? 141 VAL B CB  1 
ATOM   3332  C  CG1 . VAL B  1 141 ? 5.394   -13.144 12.922  1.00 8.53  ? 141 VAL B CG1 1 
ATOM   3333  C  CG2 . VAL B  1 141 ? 6.335   -11.689 14.762  1.00 7.44  ? 141 VAL B CG2 1 
ATOM   3334  N  N   . LEU B  1 142 ? 7.620   -15.403 12.279  1.00 7.55  ? 142 LEU B N   1 
ATOM   3335  C  CA  . LEU B  1 142 ? 7.782   -16.123 11.061  1.00 6.77  ? 142 LEU B CA  1 
ATOM   3336  C  C   . LEU B  1 142 ? 6.499   -15.919 10.214  1.00 7.52  ? 142 LEU B C   1 
ATOM   3337  O  O   . LEU B  1 142 ? 5.378   -16.098 10.768  1.00 8.98  ? 142 LEU B O   1 
ATOM   3338  C  CB  . LEU B  1 142 ? 7.939   -17.681 11.247  1.00 7.97  ? 142 LEU B CB  1 
ATOM   3339  C  CG  . LEU B  1 142 ? 9.040   -18.080 12.297  1.00 9.79  ? 142 LEU B CG  1 
ATOM   3340  C  CD1 . LEU B  1 142 ? 9.027   -19.596 12.304  1.00 11.32 ? 142 LEU B CD1 1 
ATOM   3341  C  CD2 . LEU B  1 142 ? 10.358  -17.542 11.734  1.00 12.76 ? 142 LEU B CD2 1 
ATOM   3342  N  N   . ALA B  1 143 ? 6.647   -15.519 8.941   1.00 6.78  ? 143 ALA B N   1 
ATOM   3343  C  CA  . ALA B  1 143 ? 5.442   -15.335 8.047   1.00 6.41  ? 143 ALA B CA  1 
ATOM   3344  C  C   . ALA B  1 143 ? 5.443   -16.369 6.935   1.00 7.68  ? 143 ALA B C   1 
ATOM   3345  O  O   . ALA B  1 143 ? 6.465   -16.539 6.200   1.00 8.24  ? 143 ALA B O   1 
ATOM   3346  C  CB  . ALA B  1 143 ? 5.461   -13.922 7.462   1.00 7.95  ? 143 ALA B CB  1 
ATOM   3347  N  N   . VAL B  1 144 ? 4.307   -17.023 6.766   1.00 6.37  ? 144 VAL B N   1 
ATOM   3348  C  CA  . VAL B  1 144 ? 4.106   -17.933 5.671   1.00 5.49  ? 144 VAL B CA  1 
ATOM   3349  C  C   . VAL B  1 144 ? 3.022   -17.350 4.797   1.00 5.84  ? 144 VAL B C   1 
ATOM   3350  O  O   . VAL B  1 144 ? 1.910   -17.073 5.226   1.00 6.64  ? 144 VAL B O   1 
ATOM   3351  C  CB  . VAL B  1 144 ? 3.620   -19.373 6.189   1.00 7.04  ? 144 VAL B CB  1 
ATOM   3352  C  CG1 . VAL B  1 144 ? 3.390   -20.306 4.996   1.00 9.37  ? 144 VAL B CG1 1 
ATOM   3353  C  CG2 . VAL B  1 144 ? 4.649   -19.956 7.177   1.00 8.67  ? 144 VAL B CG2 1 
ATOM   3354  N  N   . LEU B  1 145 ? 3.343   -17.184 3.479   1.00 6.65  ? 145 LEU B N   1 
ATOM   3355  C  CA  . LEU B  1 145 ? 2.419   -16.733 2.457   1.00 6.09  ? 145 LEU B CA  1 
ATOM   3356  C  C   . LEU B  1 145 ? 1.532   -17.919 2.042   1.00 6.38  ? 145 LEU B C   1 
ATOM   3357  O  O   . LEU B  1 145 ? 2.063   -19.040 1.860   1.00 8.67  ? 145 LEU B O   1 
ATOM   3358  C  CB  . LEU B  1 145 ? 3.196   -16.131 1.270   1.00 7.65  ? 145 LEU B CB  1 
ATOM   3359  C  CG  . LEU B  1 145 ? 4.135   -14.976 1.648   1.00 8.61  ? 145 LEU B CG  1 
ATOM   3360  C  CD1 . LEU B  1 145 ? 5.155   -14.690 0.465   1.00 10.16 ? 145 LEU B CD1 1 
ATOM   3361  C  CD2 . LEU B  1 145 ? 3.352   -13.701 1.968   1.00 8.77  ? 145 LEU B CD2 1 
ATOM   3362  N  N   . ILE B  1 146 ? 0.214   -17.671 1.889   1.00 7.38  ? 146 ILE B N   1 
ATOM   3363  C  CA  . ILE B  1 146 ? -0.743  -18.718 1.604   1.00 7.35  ? 146 ILE B CA  1 
ATOM   3364  C  C   . ILE B  1 146 ? -1.460  -18.390 0.280   1.00 8.95  ? 146 ILE B C   1 
ATOM   3365  O  O   . ILE B  1 146 ? -2.002  -17.305 0.112   1.00 10.10 ? 146 ILE B O   1 
ATOM   3366  C  CB  . ILE B  1 146 ? -1.801  -18.820 2.763   1.00 7.27  ? 146 ILE B CB  1 
ATOM   3367  C  CG1 . ILE B  1 146 ? -1.160  -19.200 4.058   1.00 6.81  ? 146 ILE B CG1 1 
ATOM   3368  C  CG2 . ILE B  1 146 ? -2.881  -19.931 2.358   1.00 8.99  ? 146 ILE B CG2 1 
ATOM   3369  C  CD1 . ILE B  1 146 ? -2.011  -19.020 5.274   1.00 6.93  ? 146 ILE B CD1 1 
ATOM   3370  N  N   . GLU B  1 147 ? -1.446  -19.352 -0.643  1.00 10.70 ? 147 GLU B N   1 
ATOM   3371  C  CA  . GLU B  1 147 ? -2.225  -19.185 -1.893  1.00 11.46 ? 147 GLU B CA  1 
ATOM   3372  C  C   . GLU B  1 147 ? -3.254  -20.337 -2.039  1.00 11.40 ? 147 GLU B C   1 
ATOM   3373  O  O   . GLU B  1 147 ? -3.160  -21.370 -1.345  1.00 11.04 ? 147 GLU B O   1 
ATOM   3374  C  CB  . GLU B  1 147 ? -1.227  -19.162 -3.075  1.00 12.42 ? 147 GLU B CB  1 
ATOM   3375  C  CG  . GLU B  1 147 ? -0.562  -20.462 -3.335  1.00 11.92 ? 147 GLU B CG  1 
ATOM   3376  C  CD  . GLU B  1 147 ? 0.502   -20.365 -4.386  1.00 18.18 ? 147 GLU B CD  1 
ATOM   3377  O  OE1 . GLU B  1 147 ? 0.964   -19.212 -4.725  1.00 16.49 ? 147 GLU B OE1 1 
ATOM   3378  O  OE2 . GLU B  1 147 ? 0.900   -21.469 -4.822  1.00 20.72 ? 147 GLU B OE2 1 
ATOM   3379  N  N   . MET B  1 148 ? -4.227  -20.082 -2.913  1.00 12.47 ? 148 MET B N   1 
ATOM   3380  C  CA  . MET B  1 148 ? -5.303  -21.090 -3.148  1.00 11.52 ? 148 MET B CA  1 
ATOM   3381  C  C   . MET B  1 148 ? -4.701  -22.191 -4.028  1.00 14.39 ? 148 MET B C   1 
ATOM   3382  O  O   . MET B  1 148 ? -4.038  -21.903 -5.000  1.00 18.68 ? 148 MET B O   1 
ATOM   3383  C  CB  . MET B  1 148 ? -6.483  -20.319 -3.758  1.00 15.19 ? 148 MET B CB  1 
ATOM   3384  C  CG  . MET B  1 148 ? -7.732  -21.146 -3.898  1.00 20.04 ? 148 MET B CG  1 
ATOM   3385  S  SD  . MET B  1 148 ? -7.746  -22.394 -5.268  1.00 26.76 ? 148 MET B SD  1 
ATOM   3386  C  CE  . MET B  1 148 ? -7.578  -21.347 -6.675  1.00 25.77 ? 148 MET B CE  1 
ATOM   3387  N  N   . GLY B  1 149 ? -4.904  -23.458 -3.602  1.00 15.19 ? 149 GLY B N   1 
ATOM   3388  C  CA  . GLY B  1 149 ? -4.470  -24.607 -4.376  1.00 14.63 ? 149 GLY B CA  1 
ATOM   3389  C  C   . GLY B  1 149 ? -5.023  -25.895 -3.775  1.00 14.54 ? 149 GLY B C   1 
ATOM   3390  O  O   . GLY B  1 149 ? -6.285  -26.096 -3.589  1.00 14.29 ? 149 GLY B O   1 
ATOM   3391  N  N   . SER B  1 150 ? -4.122  -26.816 -3.497  1.00 17.06 ? 150 SER B N   1 
ATOM   3392  C  CA  . SER B  1 150 ? -4.588  -28.096 -2.990  1.00 17.02 ? 150 SER B CA  1 
ATOM   3393  C  C   . SER B  1 150 ? -4.991  -27.979 -1.502  1.00 17.07 ? 150 SER B C   1 
ATOM   3394  O  O   . SER B  1 150 ? -4.458  -27.181 -0.764  1.00 17.10 ? 150 SER B O   1 
ATOM   3395  C  CB  . SER B  1 150 ? -3.440  -29.111 -3.039  1.00 18.12 ? 150 SER B CB  1 
ATOM   3396  O  OG  . SER B  1 150 ? -2.269  -28.599 -2.396  1.00 22.78 ? 150 SER B OG  1 
ATOM   3397  N  N   . PHE B  1 151 ? -5.899  -28.878 -1.111  1.00 15.09 ? 151 PHE B N   1 
ATOM   3398  C  CA  . PHE B  1 151 ? -6.335  -29.046 0.237   1.00 14.91 ? 151 PHE B CA  1 
ATOM   3399  C  C   . PHE B  1 151 ? -5.181  -29.298 1.195   1.00 14.75 ? 151 PHE B C   1 
ATOM   3400  O  O   . PHE B  1 151 ? -4.235  -30.087 0.941   1.00 17.37 ? 151 PHE B O   1 
ATOM   3401  C  CB  . PHE B  1 151 ? -7.472  -30.133 0.357   1.00 15.89 ? 151 PHE B CB  1 
ATOM   3402  C  CG  . PHE B  1 151 ? -7.916  -30.389 1.803   1.00 14.11 ? 151 PHE B CG  1 
ATOM   3403  C  CD1 . PHE B  1 151 ? -8.837  -29.514 2.401   1.00 17.70 ? 151 PHE B CD1 1 
ATOM   3404  C  CD2 . PHE B  1 151 ? -7.405  -31.458 2.562   1.00 15.04 ? 151 PHE B CD2 1 
ATOM   3405  C  CE1 . PHE B  1 151 ? -9.231  -29.699 3.734   1.00 18.14 ? 151 PHE B CE1 1 
ATOM   3406  C  CE2 . PHE B  1 151 ? -7.819  -31.699 3.899   1.00 17.23 ? 151 PHE B CE2 1 
ATOM   3407  C  CZ  . PHE B  1 151 ? -8.730  -30.762 4.511   1.00 18.38 ? 151 PHE B CZ  1 
ATOM   3408  N  N   . ASN B  1 152 ? -5.159  -28.660 2.349   1.00 14.32 ? 152 ASN B N   1 
ATOM   3409  C  CA  . ASN B  1 152 ? -4.020  -28.781 3.231   1.00 12.27 ? 152 ASN B CA  1 
ATOM   3410  C  C   . ASN B  1 152 ? -4.506  -29.352 4.583   1.00 14.59 ? 152 ASN B C   1 
ATOM   3411  O  O   . ASN B  1 152 ? -5.130  -28.667 5.459   1.00 12.21 ? 152 ASN B O   1 
ATOM   3412  C  CB  . ASN B  1 152 ? -3.368  -27.415 3.399   1.00 11.56 ? 152 ASN B CB  1 
ATOM   3413  C  CG  . ASN B  1 152 ? -2.045  -27.477 4.133   1.00 11.08 ? 152 ASN B CG  1 
ATOM   3414  O  OD1 . ASN B  1 152 ? -1.912  -28.109 5.186   1.00 14.01 ? 152 ASN B OD1 1 
ATOM   3415  N  ND2 . ASN B  1 152 ? -1.023  -26.696 3.636   1.00 13.31 ? 152 ASN B ND2 1 
ATOM   3416  N  N   . PRO B  1 153 ? -4.263  -30.640 4.812   1.00 16.15 ? 153 PRO B N   1 
ATOM   3417  C  CA  . PRO B  1 153 ? -4.734  -31.257 6.058   1.00 15.69 ? 153 PRO B CA  1 
ATOM   3418  C  C   . PRO B  1 153 ? -4.201  -30.608 7.336   1.00 16.23 ? 153 PRO B C   1 
ATOM   3419  O  O   . PRO B  1 153 ? -4.861  -30.571 8.399   1.00 15.94 ? 153 PRO B O   1 
ATOM   3420  C  CB  . PRO B  1 153 ? -4.190  -32.732 5.888   1.00 17.36 ? 153 PRO B CB  1 
ATOM   3421  C  CG  . PRO B  1 153 ? -4.120  -32.965 4.386   1.00 21.39 ? 153 PRO B CG  1 
ATOM   3422  C  CD  . PRO B  1 153 ? -3.659  -31.600 3.817   1.00 16.87 ? 153 PRO B CD  1 
ATOM   3423  N  N   . SER B  1 154 ? -2.979  -30.048 7.276   1.00 13.92 ? 154 SER B N   1 
ATOM   3424  C  CA  . SER B  1 154 ? -2.369  -29.534 8.459   1.00 13.86 ? 154 SER B CA  1 
ATOM   3425  C  C   . SER B  1 154 ? -3.058  -28.219 8.836   1.00 11.72 ? 154 SER B C   1 
ATOM   3426  O  O   . SER B  1 154 ? -3.354  -28.006 10.020  1.00 10.76 ? 154 SER B O   1 
ATOM   3427  C  CB  . SER B  1 154 ? -0.892  -29.311 8.194   1.00 15.46 ? 154 SER B CB  1 
ATOM   3428  O  OG  . SER B  1 154 ? -0.304  -30.643 8.040   1.00 22.36 ? 154 SER B OG  1 
ATOM   3429  N  N   . TYR B  1 155 ? -3.296  -27.314 7.846   1.00 12.01 ? 155 TYR B N   1 
ATOM   3430  C  CA  . TYR B  1 155 ? -4.085  -26.068 8.200   1.00 9.43  ? 155 TYR B CA  1 
ATOM   3431  C  C   . TYR B  1 155 ? -5.497  -26.379 8.606   1.00 11.25 ? 155 TYR B C   1 
ATOM   3432  O  O   . TYR B  1 155 ? -6.014  -25.734 9.492   1.00 10.71 ? 155 TYR B O   1 
ATOM   3433  C  CB  . TYR B  1 155 ? -4.138  -25.168 6.978   1.00 9.33  ? 155 TYR B CB  1 
ATOM   3434  C  CG  . TYR B  1 155 ? -2.903  -24.301 6.875   1.00 10.01 ? 155 TYR B CG  1 
ATOM   3435  C  CD1 . TYR B  1 155 ? -1.694  -24.841 6.369   1.00 9.05  ? 155 TYR B CD1 1 
ATOM   3436  C  CD2 . TYR B  1 155 ? -2.843  -22.997 7.441   1.00 8.88  ? 155 TYR B CD2 1 
ATOM   3437  C  CE1 . TYR B  1 155 ? -0.457  -24.050 6.291   1.00 10.68 ? 155 TYR B CE1 1 
ATOM   3438  C  CE2 . TYR B  1 155 ? -1.631  -22.218 7.405   1.00 8.65  ? 155 TYR B CE2 1 
ATOM   3439  C  CZ  . TYR B  1 155 ? -0.482  -22.770 6.825   1.00 7.60  ? 155 TYR B CZ  1 
ATOM   3440  O  OH  . TYR B  1 155 ? 0.669   -21.946 6.847   1.00 8.73  ? 155 TYR B OH  1 
ATOM   3441  N  N   . ASP B  1 156 ? -6.051  -27.485 8.098   1.00 10.52 ? 156 ASP B N   1 
ATOM   3442  C  CA  . ASP B  1 156 ? -7.361  -27.933 8.645   1.00 10.75 ? 156 ASP B CA  1 
ATOM   3443  C  C   . ASP B  1 156 ? -7.372  -28.315 10.131  1.00 10.48 ? 156 ASP B C   1 
ATOM   3444  O  O   . ASP B  1 156 ? -8.471  -28.274 10.743  1.00 10.99 ? 156 ASP B O   1 
ATOM   3445  C  CB  . ASP B  1 156 ? -8.026  -29.050 7.792   1.00 11.49 ? 156 ASP B CB  1 
ATOM   3446  C  CG  . ASP B  1 156 ? -9.411  -28.622 7.306   1.00 15.83 ? 156 ASP B CG  1 
ATOM   3447  O  OD1 . ASP B  1 156 ? -10.388 -29.386 7.390   1.00 19.72 ? 156 ASP B OD1 1 
ATOM   3448  O  OD2 . ASP B  1 156 ? -9.539  -27.463 6.854   1.00 14.70 ? 156 ASP B OD2 1 
ATOM   3449  N  N   . LYS B  1 157 ? -6.237  -28.674 10.734  1.00 9.76  ? 157 LYS B N   1 
ATOM   3450  C  CA  . LYS B  1 157 ? -6.217  -28.876 12.149  1.00 11.06 ? 157 LYS B CA  1 
ATOM   3451  C  C   . LYS B  1 157 ? -6.568  -27.638 12.947  1.00 11.13 ? 157 LYS B C   1 
ATOM   3452  O  O   . LYS B  1 157 ? -6.945  -27.756 14.155  1.00 14.14 ? 157 LYS B O   1 
ATOM   3453  C  CB  . LYS B  1 157 ? -4.832  -29.459 12.584  1.00 13.39 ? 157 LYS B CB  1 
ATOM   3454  C  CG  . LYS B  1 157 ? -4.539  -30.746 11.712  1.00 14.95 ? 157 LYS B CG  1 
ATOM   3455  C  CD  . LYS B  1 157 ? -3.194  -31.349 11.935  1.00 15.35 ? 157 LYS B CD  1 
ATOM   3456  C  CE  . LYS B  1 157 ? -3.064  -32.661 11.105  1.00 18.57 ? 157 LYS B CE  1 
ATOM   3457  N  NZ  . LYS B  1 157 ? -1.595  -33.123 11.326  1.00 21.27 ? 157 LYS B NZ  1 
ATOM   3458  N  N   . ILE B  1 158 ? -6.409  -26.462 12.259  1.00 10.37 ? 158 ILE B N   1 
ATOM   3459  C  CA  . ILE B  1 158 ? -6.890  -25.209 12.903  1.00 10.02 ? 158 ILE B CA  1 
ATOM   3460  C  C   . ILE B  1 158 ? -8.271  -24.971 12.362  1.00 10.36 ? 158 ILE B C   1 
ATOM   3461  O  O   . ILE B  1 158 ? -9.188  -24.640 13.146  1.00 9.83  ? 158 ILE B O   1 
ATOM   3462  C  CB  . ILE B  1 158 ? -5.975  -24.013 12.529  1.00 11.05 ? 158 ILE B CB  1 
ATOM   3463  C  CG1 . ILE B  1 158 ? -4.538  -24.169 13.186  1.00 13.08 ? 158 ILE B CG1 1 
ATOM   3464  C  CG2 . ILE B  1 158 ? -6.574  -22.608 13.016  1.00 9.72  ? 158 ILE B CG2 1 
ATOM   3465  C  CD1 . ILE B  1 158 ? -3.420  -23.335 12.462  1.00 14.64 ? 158 ILE B CD1 1 
ATOM   3466  N  N   . PHE B  1 159 ? -8.455  -25.000 11.042  1.00 8.71  ? 159 PHE B N   1 
ATOM   3467  C  CA  . PHE B  1 159 ? -9.748  -24.447 10.528  1.00 9.02  ? 159 PHE B CA  1 
ATOM   3468  C  C   . PHE B  1 159 ? -10.943 -25.278 10.926  1.00 10.23 ? 159 PHE B C   1 
ATOM   3469  O  O   . PHE B  1 159 ? -12.063 -24.769 10.977  1.00 9.98  ? 159 PHE B O   1 
ATOM   3470  C  CB  . PHE B  1 159 ? -9.702  -24.408 8.978   1.00 7.79  ? 159 PHE B CB  1 
ATOM   3471  C  CG  . PHE B  1 159 ? -8.592  -23.528 8.410   1.00 9.60  ? 159 PHE B CG  1 
ATOM   3472  C  CD1 . PHE B  1 159 ? -7.988  -22.491 9.112   1.00 10.91 ? 159 PHE B CD1 1 
ATOM   3473  C  CD2 . PHE B  1 159 ? -8.169  -23.794 7.105   1.00 8.88  ? 159 PHE B CD2 1 
ATOM   3474  C  CE1 . PHE B  1 159 ? -7.035  -21.699 8.505   1.00 11.25 ? 159 PHE B CE1 1 
ATOM   3475  C  CE2 . PHE B  1 159 ? -7.197  -22.985 6.499   1.00 11.86 ? 159 PHE B CE2 1 
ATOM   3476  C  CZ  . PHE B  1 159 ? -6.679  -21.911 7.205   1.00 9.68  ? 159 PHE B CZ  1 
ATOM   3477  N  N   . SER B  1 160 ? -10.736 -26.565 11.206  1.00 9.07  ? 160 SER B N   1 
ATOM   3478  C  CA  . SER B  1 160 ? -11.955 -27.375 11.470  1.00 9.98  ? 160 SER B CA  1 
ATOM   3479  C  C   . SER B  1 160 ? -12.534 -26.971 12.863  1.00 9.63  ? 160 SER B C   1 
ATOM   3480  O  O   . SER B  1 160 ? -13.653 -27.455 13.192  1.00 13.85 ? 160 SER B O   1 
ATOM   3481  C  CB  . SER B  1 160 ? -11.543 -28.888 11.574  1.00 11.43 ? 160 SER B CB  1 
ATOM   3482  O  OG  . SER B  1 160 ? -10.572 -29.029 12.669  1.00 13.37 ? 160 SER B OG  1 
ATOM   3483  N  N   . HIS B  1 161 ? -11.917 -26.085 13.660  1.00 8.87  ? 161 HIS B N   1 
ATOM   3484  C  CA  . HIS B  1 161 ? -12.450 -25.634 14.933  1.00 9.61  ? 161 HIS B CA  1 
ATOM   3485  C  C   . HIS B  1 161 ? -13.052 -24.241 14.865  1.00 9.73  ? 161 HIS B C   1 
ATOM   3486  O  O   . HIS B  1 161 ? -13.513 -23.768 15.882  1.00 10.90 ? 161 HIS B O   1 
ATOM   3487  C  CB  . HIS B  1 161 ? -11.356 -25.575 16.064  1.00 11.36 ? 161 HIS B CB  1 
ATOM   3488  C  CG  . HIS B  1 161 ? -10.677 -26.889 16.319  1.00 14.31 ? 161 HIS B CG  1 
ATOM   3489  N  ND1 . HIS B  1 161 ? -11.107 -27.736 17.344  1.00 18.99 ? 161 HIS B ND1 1 
ATOM   3490  C  CD2 . HIS B  1 161 ? -9.677  -27.541 15.658  1.00 11.84 ? 161 HIS B CD2 1 
ATOM   3491  C  CE1 . HIS B  1 161 ? -10.365 -28.837 17.311  1.00 22.17 ? 161 HIS B CE1 1 
ATOM   3492  N  NE2 . HIS B  1 161 ? -9.567  -28.782 16.253  1.00 16.91 ? 161 HIS B NE2 1 
ATOM   3493  N  N   . LEU B  1 162 ? -13.099 -23.615 13.675  1.00 9.14  ? 162 LEU B N   1 
ATOM   3494  C  CA  . LEU B  1 162 ? -13.466 -22.189 13.586  1.00 10.34 ? 162 LEU B CA  1 
ATOM   3495  C  C   . LEU B  1 162 ? -14.855 -21.918 14.084  1.00 9.95  ? 162 LEU B C   1 
ATOM   3496  O  O   . LEU B  1 162 ? -15.110 -20.805 14.603  1.00 10.73 ? 162 LEU B O   1 
ATOM   3497  C  CB  . LEU B  1 162 ? -13.348 -21.637 12.114  1.00 10.50 ? 162 LEU B CB  1 
ATOM   3498  C  CG  . LEU B  1 162 ? -11.864 -21.517 11.622  1.00 12.36 ? 162 LEU B CG  1 
ATOM   3499  C  CD1 . LEU B  1 162 ? -11.793 -20.984 10.301  1.00 15.11 ? 162 LEU B CD1 1 
ATOM   3500  C  CD2 . LEU B  1 162 ? -11.082 -20.632 12.539  1.00 16.51 ? 162 LEU B CD2 1 
ATOM   3501  N  N   . GLN B  1 163 ? -15.792 -22.896 13.853  1.00 9.73  ? 163 GLN B N   1 
ATOM   3502  C  CA  . GLN B  1 163 ? -17.201 -22.606 14.224  1.00 11.80 ? 163 GLN B CA  1 
ATOM   3503  C  C   . GLN B  1 163 ? -17.390 -22.557 15.728  1.00 12.21 ? 163 GLN B C   1 
ATOM   3504  O  O   . GLN B  1 163 ? -18.526 -22.240 16.161  1.00 14.91 ? 163 GLN B O   1 
ATOM   3505  C  CB  . GLN B  1 163 ? -18.198 -23.561 13.615  1.00 13.25 ? 163 GLN B CB  1 
ATOM   3506  C  CG  . GLN B  1 163 ? -18.025 -23.675 12.032  1.00 15.05 ? 163 GLN B CG  1 
ATOM   3507  C  CD  . GLN B  1 163 ? -18.162 -22.359 11.232  1.00 16.93 ? 163 GLN B CD  1 
ATOM   3508  O  OE1 . GLN B  1 163 ? -19.071 -21.576 11.476  1.00 19.20 ? 163 GLN B OE1 1 
ATOM   3509  N  NE2 . GLN B  1 163 ? -17.168 -22.104 10.319  1.00 22.15 ? 163 GLN B NE2 1 
ATOM   3510  N  N   . HIS B  1 164 ? -16.387 -22.909 16.547  1.00 9.57  ? 164 HIS B N   1 
ATOM   3511  C  CA  . HIS B  1 164 ? -16.494 -22.786 17.978  1.00 9.95  ? 164 HIS B CA  1 
ATOM   3512  C  C   . HIS B  1 164 ? -15.889 -21.507 18.541  1.00 9.83  ? 164 HIS B C   1 
ATOM   3513  O  O   . HIS B  1 164 ? -15.915 -21.271 19.752  1.00 11.61 ? 164 HIS B O   1 
ATOM   3514  C  CB  . HIS B  1 164 ? -15.866 -23.990 18.688  1.00 11.36 ? 164 HIS B CB  1 
ATOM   3515  C  CG  . HIS B  1 164 ? -16.422 -25.274 18.142  1.00 10.78 ? 164 HIS B CG  1 
ATOM   3516  N  ND1 . HIS B  1 164 ? -17.732 -25.671 18.358  1.00 13.08 ? 164 HIS B ND1 1 
ATOM   3517  C  CD2 . HIS B  1 164 ? -15.850 -26.244 17.357  1.00 14.78 ? 164 HIS B CD2 1 
ATOM   3518  C  CE1 . HIS B  1 164 ? -17.960 -26.803 17.685  1.00 12.95 ? 164 HIS B CE1 1 
ATOM   3519  N  NE2 . HIS B  1 164 ? -16.856 -27.150 17.057  1.00 15.01 ? 164 HIS B NE2 1 
ATOM   3520  N  N   . VAL B  1 165 ? -15.272 -20.667 17.668  1.00 7.85  ? 165 VAL B N   1 
ATOM   3521  C  CA  . VAL B  1 165 ? -14.705 -19.367 18.142  1.00 9.21  ? 165 VAL B CA  1 
ATOM   3522  C  C   . VAL B  1 165 ? -15.272 -18.259 17.219  1.00 8.09  ? 165 VAL B C   1 
ATOM   3523  O  O   . VAL B  1 165 ? -14.542 -17.334 16.864  1.00 8.48  ? 165 VAL B O   1 
ATOM   3524  C  CB  . VAL B  1 165 ? -13.161 -19.405 18.184  1.00 11.34 ? 165 VAL B CB  1 
ATOM   3525  C  CG1 . VAL B  1 165 ? -12.747 -20.378 19.283  1.00 10.82 ? 165 VAL B CG1 1 
ATOM   3526  C  CG2 . VAL B  1 165 ? -12.601 -19.854 16.827  1.00 11.07 ? 165 VAL B CG2 1 
ATOM   3527  N  N   . LYS B  1 166 ? -16.552 -18.326 16.859  1.00 7.19  ? 166 LYS B N   1 
ATOM   3528  C  CA  . LYS B  1 166 ? -17.072 -17.369 15.869  1.00 8.56  ? 166 LYS B CA  1 
ATOM   3529  C  C   . LYS B  1 166 ? -17.074 -15.952 16.344  1.00 7.90  ? 166 LYS B C   1 
ATOM   3530  O  O   . LYS B  1 166 ? -16.902 -15.018 15.509  1.00 9.42  ? 166 LYS B O   1 
ATOM   3531  C  CB  . LYS B  1 166 ? -18.533 -17.774 15.377  1.00 8.49  ? 166 LYS B CB  1 
ATOM   3532  C  CG  . LYS B  1 166 ? -18.569 -19.113 14.698  1.00 13.14 ? 166 LYS B CG  1 
ATOM   3533  C  CD  . LYS B  1 166 ? -19.917 -19.497 14.107  1.00 14.29 ? 166 LYS B CD  1 
ATOM   3534  C  CE  . LYS B  1 166 ? -20.537 -18.569 13.152  1.00 15.61 ? 166 LYS B CE  1 
ATOM   3535  N  NZ  . LYS B  1 166 ? -19.834 -18.750 11.834  1.00 14.82 ? 166 LYS B NZ  1 
ATOM   3536  N  N   . TYR B  1 167 ? -17.274 -15.713 17.647  1.00 7.95  ? 167 TYR B N   1 
ATOM   3537  C  CA  . TYR B  1 167 ? -17.383 -14.366 18.182  1.00 6.25  ? 167 TYR B CA  1 
ATOM   3538  C  C   . TYR B  1 167 ? -16.232 -13.991 19.135  1.00 8.67  ? 167 TYR B C   1 
ATOM   3539  O  O   . TYR B  1 167 ? -15.632 -14.905 19.770  1.00 8.30  ? 167 TYR B O   1 
ATOM   3540  C  CB  . TYR B  1 167 ? -18.777 -14.224 18.922  1.00 9.22  ? 167 TYR B CB  1 
ATOM   3541  C  CG  . TYR B  1 167 ? -19.905 -14.362 17.946  1.00 9.80  ? 167 TYR B CG  1 
ATOM   3542  C  CD1 . TYR B  1 167 ? -20.594 -15.581 17.792  1.00 9.57  ? 167 TYR B CD1 1 
ATOM   3543  C  CD2 . TYR B  1 167 ? -20.245 -13.289 17.152  1.00 9.41  ? 167 TYR B CD2 1 
ATOM   3544  C  CE1 . TYR B  1 167 ? -21.592 -15.705 16.764  1.00 10.61 ? 167 TYR B CE1 1 
ATOM   3545  C  CE2 . TYR B  1 167 ? -21.209 -13.408 16.185  1.00 12.65 ? 167 TYR B CE2 1 
ATOM   3546  C  CZ  . TYR B  1 167 ? -21.903 -14.533 16.102  1.00 10.50 ? 167 TYR B CZ  1 
ATOM   3547  O  OH  . TYR B  1 167 ? -22.901 -14.704 15.067  1.00 15.83 ? 167 TYR B OH  1 
ATOM   3548  N  N   . LYS B  1 168 ? -16.013 -12.679 19.294  1.00 8.78  ? 168 LYS B N   1 
ATOM   3549  C  CA  . LYS B  1 168 ? -14.902 -12.168 20.158  1.00 10.27 ? 168 LYS B CA  1 
ATOM   3550  C  C   . LYS B  1 168 ? -14.983 -12.741 21.554  1.00 11.91 ? 168 LYS B C   1 
ATOM   3551  O  O   . LYS B  1 168 ? -16.087 -12.787 22.143  1.00 10.43 ? 168 LYS B O   1 
ATOM   3552  C  CB  . LYS B  1 168 ? -14.923 -10.633 20.238  1.00 10.32 ? 168 LYS B CB  1 
ATOM   3553  C  CG  . LYS B  1 168 ? -13.889 -10.098 21.169  1.00 12.60 ? 168 LYS B CG  1 
ATOM   3554  C  CD  . LYS B  1 168 ? -13.736 -8.545  21.019  1.00 13.24 ? 168 LYS B CD  1 
ATOM   3555  C  CE  . LYS B  1 168 ? -12.615 -8.021  21.947  1.00 20.31 ? 168 LYS B CE  1 
ATOM   3556  N  NZ  . LYS B  1 168 ? -12.559 -6.524  21.738  1.00 24.28 ? 168 LYS B NZ  1 
ATOM   3557  N  N   . GLY B  1 169 ? -13.843 -13.213 22.044  1.00 11.83 ? 169 GLY B N   1 
ATOM   3558  C  CA  . GLY B  1 169 ? -13.785 -13.740 23.383  1.00 12.61 ? 169 GLY B CA  1 
ATOM   3559  C  C   . GLY B  1 169 ? -14.048 -15.225 23.486  1.00 13.87 ? 169 GLY B C   1 
ATOM   3560  O  O   . GLY B  1 169 ? -13.799 -15.891 24.574  1.00 14.47 ? 169 GLY B O   1 
ATOM   3561  N  N   . GLN B  1 170 ? -14.604 -15.861 22.410  1.00 10.08 ? 170 GLN B N   1 
ATOM   3562  C  CA  . GLN B  1 170 ? -14.861 -17.285 22.487  1.00 10.56 ? 170 GLN B CA  1 
ATOM   3563  C  C   . GLN B  1 170 ? -13.576 -18.144 22.338  1.00 9.96  ? 170 GLN B C   1 
ATOM   3564  O  O   . GLN B  1 170 ? -12.634 -17.741 21.608  1.00 10.27 ? 170 GLN B O   1 
ATOM   3565  C  CB  . GLN B  1 170 ? -15.845 -17.757 21.461  1.00 8.96  ? 170 GLN B CB  1 
ATOM   3566  C  CG  . GLN B  1 170 ? -17.257 -17.130 21.778  1.00 11.80 ? 170 GLN B CG  1 
ATOM   3567  C  CD  . GLN B  1 170 ? -18.328 -17.543 20.813  1.00 14.40 ? 170 GLN B CD  1 
ATOM   3568  O  OE1 . GLN B  1 170 ? -18.108 -17.811 19.659  1.00 11.61 ? 170 GLN B OE1 1 
ATOM   3569  N  NE2 . GLN B  1 170 ? -19.586 -17.631 21.336  1.00 18.32 ? 170 GLN B NE2 1 
ATOM   3570  N  N   . GLU B  1 171 ? -13.509 -19.304 22.959  1.00 12.58 ? 171 GLU B N   1 
ATOM   3571  C  CA  . GLU B  1 171 ? -12.246 -20.137 23.044  1.00 11.92 ? 171 GLU B CA  1 
ATOM   3572  C  C   . GLU B  1 171 ? -12.599 -21.552 22.800  1.00 12.38 ? 171 GLU B C   1 
ATOM   3573  O  O   . GLU B  1 171 ? -13.773 -22.016 23.092  1.00 12.40 ? 171 GLU B O   1 
ATOM   3574  C  CB  . GLU B  1 171 ? -11.640 -20.000 24.453  1.00 13.39 ? 171 GLU B CB  1 
ATOM   3575  C  CG  . GLU B  1 171 ? -11.096 -18.579 24.843  1.00 14.51 ? 171 GLU B CG  1 
ATOM   3576  C  CD  . GLU B  1 171 ? -10.632 -18.460 26.349  1.00 17.84 ? 171 GLU B CD  1 
ATOM   3577  O  OE1 . GLU B  1 171 ? -9.935  -17.492 26.686  1.00 27.67 ? 171 GLU B OE1 1 
ATOM   3578  O  OE2 . GLU B  1 171 ? -11.008 -19.363 27.058  1.00 23.09 ? 171 GLU B OE2 1 
ATOM   3579  N  N   . ALA B  1 172 ? -11.657 -22.332 22.283  1.00 11.53 ? 172 ALA B N   1 
ATOM   3580  C  CA  . ALA B  1 172 ? -11.854 -23.782 22.129  1.00 11.44 ? 172 ALA B CA  1 
ATOM   3581  C  C   . ALA B  1 172 ? -10.436 -24.375 22.301  1.00 11.18 ? 172 ALA B C   1 
ATOM   3582  O  O   . ALA B  1 172 ? -9.464  -23.695 22.020  1.00 13.82 ? 172 ALA B O   1 
ATOM   3583  C  CB  . ALA B  1 172 ? -12.393 -24.105 20.764  1.00 14.13 ? 172 ALA B CB  1 
ATOM   3584  N  N   . PHE B  1 173 ? -10.297 -25.615 22.682  1.00 10.92 ? 173 PHE B N   1 
ATOM   3585  C  CA  . PHE B  1 173 ? -8.988  -26.235 22.721  1.00 10.29 ? 173 PHE B CA  1 
ATOM   3586  C  C   . PHE B  1 173 ? -8.762  -27.040 21.465  1.00 10.78 ? 173 PHE B C   1 
ATOM   3587  O  O   . PHE B  1 173 ? -9.702  -27.642 20.876  1.00 12.72 ? 173 PHE B O   1 
ATOM   3588  C  CB  . PHE B  1 173 ? -8.860  -27.211 23.907  1.00 9.94  ? 173 PHE B CB  1 
ATOM   3589  C  CG  . PHE B  1 173 ? -8.550  -26.517 25.179  1.00 10.86 ? 173 PHE B CG  1 
ATOM   3590  C  CD1 . PHE B  1 173 ? -9.549  -26.380 26.221  1.00 16.17 ? 173 PHE B CD1 1 
ATOM   3591  C  CD2 . PHE B  1 173 ? -7.312  -25.857 25.349  1.00 11.67 ? 173 PHE B CD2 1 
ATOM   3592  C  CE1 . PHE B  1 173 ? -9.288  -25.690 27.377  1.00 16.00 ? 173 PHE B CE1 1 
ATOM   3593  C  CE2 . PHE B  1 173 ? -7.018  -25.147 26.501  1.00 13.38 ? 173 PHE B CE2 1 
ATOM   3594  C  CZ  . PHE B  1 173 ? -8.033  -25.020 27.571  1.00 19.12 ? 173 PHE B CZ  1 
ATOM   3595  N  N   . VAL B  1 174 ? -7.504  -27.080 21.013  1.00 8.51  ? 174 VAL B N   1 
ATOM   3596  C  CA  . VAL B  1 174 ? -7.040  -27.824 19.831  1.00 11.56 ? 174 VAL B CA  1 
ATOM   3597  C  C   . VAL B  1 174 ? -5.942  -28.840 20.332  1.00 10.42 ? 174 VAL B C   1 
ATOM   3598  O  O   . VAL B  1 174 ? -5.006  -28.455 20.930  1.00 10.57 ? 174 VAL B O   1 
ATOM   3599  C  CB  . VAL B  1 174 ? -6.399  -26.859 18.802  1.00 11.50 ? 174 VAL B CB  1 
ATOM   3600  C  CG1 . VAL B  1 174 ? -5.831  -27.519 17.572  1.00 12.02 ? 174 VAL B CG1 1 
ATOM   3601  C  CG2 . VAL B  1 174 ? -7.474  -25.832 18.323  1.00 14.65 ? 174 VAL B CG2 1 
ATOM   3602  N  N   . PRO B  1 175 ? -6.119  -30.141 20.014  1.00 10.21 ? 175 PRO B N   1 
ATOM   3603  C  CA  . PRO B  1 175 ? -5.052  -31.134 20.382  1.00 9.93  ? 175 PRO B CA  1 
ATOM   3604  C  C   . PRO B  1 175 ? -3.763  -30.765 19.654  1.00 10.61 ? 175 PRO B C   1 
ATOM   3605  O  O   . PRO B  1 175 ? -3.766  -30.246 18.538  1.00 10.08 ? 175 PRO B O   1 
ATOM   3606  C  CB  . PRO B  1 175 ? -5.600  -32.425 19.723  1.00 11.54 ? 175 PRO B CB  1 
ATOM   3607  C  CG  . PRO B  1 175 ? -7.122  -32.207 19.641  1.00 14.89 ? 175 PRO B CG  1 
ATOM   3608  C  CD  . PRO B  1 175 ? -7.207  -30.726 19.220  1.00 11.33 ? 175 PRO B CD  1 
ATOM   3609  N  N   . GLY B  1 176 ? -2.676  -31.065 20.315  1.00 10.22 ? 176 GLY B N   1 
ATOM   3610  C  CA  . GLY B  1 176 ? -1.320  -30.814 19.721  1.00 11.18 ? 176 GLY B CA  1 
ATOM   3611  C  C   . GLY B  1 176 ? -1.270  -31.491 18.355  1.00 11.63 ? 176 GLY B C   1 
ATOM   3612  O  O   . GLY B  1 176 ? -1.741  -32.613 18.085  1.00 10.80 ? 176 GLY B O   1 
ATOM   3613  N  N   . PHE B  1 177 ? -0.588  -30.767 17.421  1.00 11.99 ? 177 PHE B N   1 
ATOM   3614  C  CA  . PHE B  1 177 ? -0.181  -31.349 16.149  1.00 11.49 ? 177 PHE B CA  1 
ATOM   3615  C  C   . PHE B  1 177 ? 1.239   -30.730 15.785  1.00 8.77  ? 177 PHE B C   1 
ATOM   3616  O  O   . PHE B  1 177 ? 1.768   -29.851 16.449  1.00 10.44 ? 177 PHE B O   1 
ATOM   3617  C  CB  . PHE B  1 177 ? -1.247  -31.098 15.025  1.00 11.38 ? 177 PHE B CB  1 
ATOM   3618  C  CG  . PHE B  1 177 ? -1.405  -29.592 14.634  1.00 12.09 ? 177 PHE B CG  1 
ATOM   3619  C  CD1 . PHE B  1 177 ? -0.779  -29.115 13.440  1.00 11.36 ? 177 PHE B CD1 1 
ATOM   3620  C  CD2 . PHE B  1 177 ? -2.163  -28.696 15.449  1.00 11.21 ? 177 PHE B CD2 1 
ATOM   3621  C  CE1 . PHE B  1 177 ? -0.945  -27.739 13.081  1.00 11.21 ? 177 PHE B CE1 1 
ATOM   3622  C  CE2 . PHE B  1 177 ? -2.377  -27.414 15.034  1.00 10.98 ? 177 PHE B CE2 1 
ATOM   3623  C  CZ  . PHE B  1 177 ? -1.776  -26.936 13.872  1.00 12.58 ? 177 PHE B CZ  1 
ATOM   3624  N  N   . ASN B  1 178 ? 1.724   -31.178 14.617  1.00 10.64 ? 178 ASN B N   1 
ATOM   3625  C  CA  . ASN B  1 178 ? 3.102   -30.711 14.236  1.00 10.28 ? 178 ASN B CA  1 
ATOM   3626  C  C   . ASN B  1 178 ? 3.018   -29.313 13.502  1.00 9.26  ? 178 ASN B C   1 
ATOM   3627  O  O   . ASN B  1 178 ? 2.685   -29.325 12.329  1.00 10.49 ? 178 ASN B O   1 
ATOM   3628  C  CB  . ASN B  1 178 ? 3.818   -31.776 13.359  1.00 12.37 ? 178 ASN B CB  1 
ATOM   3629  C  CG  . ASN B  1 178 ? 5.217   -31.382 12.988  1.00 12.40 ? 178 ASN B CG  1 
ATOM   3630  O  OD1 . ASN B  1 178 ? 5.752   -30.456 13.496  1.00 12.09 ? 178 ASN B OD1 1 
ATOM   3631  N  ND2 . ASN B  1 178 ? 5.863   -32.235 12.135  1.00 16.68 ? 178 ASN B ND2 1 
ATOM   3632  N  N   . ILE B  1 179 ? 3.457   -28.285 14.234  1.00 8.26  ? 179 ILE B N   1 
ATOM   3633  C  CA  . ILE B  1 179 ? 3.317   -26.891 13.740  1.00 9.99  ? 179 ILE B CA  1 
ATOM   3634  C  C   . ILE B  1 179 ? 4.191   -26.786 12.469  1.00 11.99 ? 179 ILE B C   1 
ATOM   3635  O  O   . ILE B  1 179 ? 3.929   -25.950 11.599  1.00 12.19 ? 179 ILE B O   1 
ATOM   3636  C  CB  . ILE B  1 179 ? 3.594   -25.908 14.792  1.00 9.07  ? 179 ILE B CB  1 
ATOM   3637  C  CG1 . ILE B  1 179 ? 2.697   -26.117 15.960  1.00 9.77  ? 179 ILE B CG1 1 
ATOM   3638  C  CG2 . ILE B  1 179 ? 3.568   -24.418 14.256  1.00 11.41 ? 179 ILE B CG2 1 
ATOM   3639  C  CD1 . ILE B  1 179 ? 1.148   -25.938 15.679  1.00 11.78 ? 179 ILE B CD1 1 
ATOM   3640  N  N   . GLU B  1 180 ? 5.308   -27.564 12.432  1.00 10.30 ? 180 GLU B N   1 
ATOM   3641  C  CA  . GLU B  1 180 ? 6.215   -27.409 11.291  1.00 12.62 ? 180 GLU B CA  1 
ATOM   3642  C  C   . GLU B  1 180 ? 5.511   -27.829 9.988   1.00 10.96 ? 180 GLU B C   1 
ATOM   3643  O  O   . GLU B  1 180 ? 5.906   -27.389 8.889   1.00 13.36 ? 180 GLU B O   1 
ATOM   3644  C  CB  . GLU B  1 180 ? 7.476   -28.250 11.557  1.00 13.00 ? 180 GLU B CB  1 
ATOM   3645  C  CG  . GLU B  1 180 ? 8.595   -27.828 10.658  1.00 16.85 ? 180 GLU B CG  1 
ATOM   3646  C  CD  . GLU B  1 180 ? 9.851   -28.687 10.935  1.00 19.60 ? 180 GLU B CD  1 
ATOM   3647  O  OE1 . GLU B  1 180 ? 9.880   -29.377 11.967  1.00 19.85 ? 180 GLU B OE1 1 
ATOM   3648  O  OE2 . GLU B  1 180 ? 10.768  -28.492 10.107  1.00 22.91 ? 180 GLU B OE2 1 
ATOM   3649  N  N   . GLU B  1 181 ? 4.408   -28.585 10.024  1.00 11.58 ? 181 GLU B N   1 
ATOM   3650  C  CA  . GLU B  1 181 ? 3.623   -28.856 8.812   1.00 12.14 ? 181 GLU B CA  1 
ATOM   3651  C  C   . GLU B  1 181 ? 2.931   -27.631 8.161   1.00 9.14  ? 181 GLU B C   1 
ATOM   3652  O  O   . GLU B  1 181 ? 2.517   -27.682 7.004   1.00 12.11 ? 181 GLU B O   1 
ATOM   3653  C  CB  . GLU B  1 181 ? 2.504   -29.865 9.080   1.00 13.21 ? 181 GLU B CB  1 
ATOM   3654  C  CG  . GLU B  1 181 ? 2.936   -31.326 9.523   1.00 17.62 ? 181 GLU B CG  1 
ATOM   3655  C  CD  . GLU B  1 181 ? 1.776   -32.072 10.198  1.00 20.62 ? 181 GLU B CD  1 
ATOM   3656  O  OE1 . GLU B  1 181 ? 0.566   -31.627 10.113  1.00 25.97 ? 181 GLU B OE1 1 
ATOM   3657  O  OE2 . GLU B  1 181 ? 2.080   -33.147 10.818  1.00 24.03 ? 181 GLU B OE2 1 
ATOM   3658  N  N   . LEU B  1 182 ? 2.859   -26.554 8.968   1.00 10.16 ? 182 LEU B N   1 
ATOM   3659  C  CA  . LEU B  1 182 ? 2.263   -25.316 8.428   1.00 9.63  ? 182 LEU B CA  1 
ATOM   3660  C  C   . LEU B  1 182 ? 3.285   -24.513 7.591   1.00 12.27 ? 182 LEU B C   1 
ATOM   3661  O  O   . LEU B  1 182 ? 2.932   -23.514 6.931   1.00 11.73 ? 182 LEU B O   1 
ATOM   3662  C  CB  . LEU B  1 182 ? 1.729   -24.393 9.521   1.00 10.83 ? 182 LEU B CB  1 
ATOM   3663  C  CG  . LEU B  1 182 ? 0.763   -25.034 10.513  1.00 8.33  ? 182 LEU B CG  1 
ATOM   3664  C  CD1 . LEU B  1 182 ? 0.342   -24.060 11.667  1.00 8.84  ? 182 LEU B CD1 1 
ATOM   3665  C  CD2 . LEU B  1 182 ? -0.435  -25.438 9.691   1.00 10.32 ? 182 LEU B CD2 1 
ATOM   3666  N  N   . LEU B  1 183 ? 4.568   -24.925 7.637   1.00 12.66 ? 183 LEU B N   1 
ATOM   3667  C  CA  . LEU B  1 183 ? 5.630   -24.137 6.966   1.00 11.71 ? 183 LEU B CA  1 
ATOM   3668  C  C   . LEU B  1 183 ? 5.819   -24.712 5.562   1.00 10.12 ? 183 LEU B C   1 
ATOM   3669  O  O   . LEU B  1 183 ? 5.404   -25.902 5.251   1.00 11.44 ? 183 LEU B O   1 
ATOM   3670  C  CB  . LEU B  1 183 ? 6.939   -24.323 7.739   1.00 13.65 ? 183 LEU B CB  1 
ATOM   3671  C  CG  . LEU B  1 183 ? 6.968   -23.812 9.168   1.00 13.93 ? 183 LEU B CG  1 
ATOM   3672  C  CD1 . LEU B  1 183 ? 8.400   -24.060 9.804   1.00 14.45 ? 183 LEU B CD1 1 
ATOM   3673  C  CD2 . LEU B  1 183 ? 6.519   -22.404 9.370   1.00 15.11 ? 183 LEU B CD2 1 
ATOM   3674  N  N   . PRO B  1 184 ? 6.330   -23.894 4.613   1.00 11.93 ? 184 PRO B N   1 
ATOM   3675  C  CA  . PRO B  1 184 ? 6.498   -24.335 3.213   1.00 12.49 ? 184 PRO B CA  1 
ATOM   3676  C  C   . PRO B  1 184 ? 7.744   -25.161 3.070   1.00 17.70 ? 184 PRO B C   1 
ATOM   3677  O  O   . PRO B  1 184 ? 8.527   -25.406 4.048   1.00 17.50 ? 184 PRO B O   1 
ATOM   3678  C  CB  . PRO B  1 184 ? 6.761   -22.984 2.455   1.00 15.67 ? 184 PRO B CB  1 
ATOM   3679  C  CG  . PRO B  1 184 ? 7.442   -22.075 3.507   1.00 12.59 ? 184 PRO B CG  1 
ATOM   3680  C  CD  . PRO B  1 184 ? 6.757   -22.517 4.887   1.00 10.98 ? 184 PRO B CD  1 
ATOM   3681  N  N   . GLU B  1 185 ? 7.916   -25.453 1.762   1.00 19.46 ? 185 GLU B N   1 
ATOM   3682  C  CA  . GLU B  1 185 ? 9.194   -26.008 1.313   1.00 21.20 ? 185 GLU B CA  1 
ATOM   3683  C  C   . GLU B  1 185 ? 10.422  -25.022 1.345   1.00 21.86 ? 185 GLU B C   1 
ATOM   3684  O  O   . GLU B  1 185 ? 10.335  -23.765 1.231   1.00 21.25 ? 185 GLU B O   1 
ATOM   3685  C  CB  . GLU B  1 185 ? 9.030   -26.615 -0.062  1.00 24.63 ? 185 GLU B CB  1 
ATOM   3686  C  CG  . GLU B  1 185 ? 8.512   -25.814 -1.159  1.00 28.96 ? 185 GLU B CG  1 
ATOM   3687  C  CD  . GLU B  1 185 ? 8.799   -26.548 -2.428  1.00 39.33 ? 185 GLU B CD  1 
ATOM   3688  O  OE1 . GLU B  1 185 ? 8.116   -27.557 -2.696  1.00 39.02 ? 185 GLU B OE1 1 
ATOM   3689  O  OE2 . GLU B  1 185 ? 9.748   -26.152 -3.123  1.00 43.84 ? 185 GLU B OE2 1 
ATOM   3690  N  N   . ARG B  1 186 ? 11.595  -25.648 1.461   1.00 18.23 ? 186 ARG B N   1 
ATOM   3691  C  CA  . ARG B  1 186 ? 12.821  -24.909 1.369   1.00 20.11 ? 186 ARG B CA  1 
ATOM   3692  C  C   . ARG B  1 186 ? 12.683  -23.731 2.326   1.00 19.31 ? 186 ARG B C   1 
ATOM   3693  O  O   . ARG B  1 186 ? 12.921  -22.495 1.914   1.00 18.89 ? 186 ARG B O   1 
ATOM   3694  C  CB  . ARG B  1 186 ? 13.121  -24.548 -0.137  1.00 22.30 ? 186 ARG B CB  1 
ATOM   3695  C  CG  . ARG B  1 186 ? 13.487  -25.798 -0.942  1.00 27.97 ? 186 ARG B CG  1 
ATOM   3696  C  CD  . ARG B  1 186 ? 13.766  -25.404 -2.374  1.00 37.36 ? 186 ARG B CD  1 
ATOM   3697  N  NE  . ARG B  1 186 ? 12.527  -25.330 -3.152  1.00 42.71 ? 186 ARG B NE  1 
ATOM   3698  C  CZ  . ARG B  1 186 ? 12.096  -24.269 -3.833  1.00 46.13 ? 186 ARG B CZ  1 
ATOM   3699  N  NH1 . ARG B  1 186 ? 10.876  -24.282 -4.350  1.00 49.69 ? 186 ARG B NH1 1 
ATOM   3700  N  NH2 . ARG B  1 186 ? 12.870  -23.205 -4.010  1.00 49.42 ? 186 ARG B NH2 1 
ATOM   3701  N  N   . THR B  1 187 ? 12.329  -24.040 3.613   1.00 13.91 ? 187 THR B N   1 
ATOM   3702  C  CA  . THR B  1 187 ? 12.370  -22.893 4.574   1.00 12.44 ? 187 THR B CA  1 
ATOM   3703  C  C   . THR B  1 187 ? 13.707  -22.105 4.588   1.00 11.27 ? 187 THR B C   1 
ATOM   3704  O  O   . THR B  1 187 ? 13.839  -21.046 5.146   1.00 12.00 ? 187 THR B O   1 
ATOM   3705  C  CB  . THR B  1 187 ? 12.050  -23.265 6.011   1.00 12.48 ? 187 THR B CB  1 
ATOM   3706  O  OG1 . THR B  1 187 ? 12.859  -24.407 6.403   1.00 12.80 ? 187 THR B OG1 1 
ATOM   3707  C  CG2 . THR B  1 187 ? 10.536  -23.673 6.113   1.00 12.34 ? 187 THR B CG2 1 
ATOM   3708  N  N   . ALA B  1 188 ? 14.795  -22.751 4.056   1.00 13.64 ? 188 ALA B N   1 
ATOM   3709  C  CA  . ALA B  1 188 ? 16.083  -22.068 4.023   1.00 11.89 ? 188 ALA B CA  1 
ATOM   3710  C  C   . ALA B  1 188 ? 16.097  -20.757 3.254   1.00 11.02 ? 188 ALA B C   1 
ATOM   3711  O  O   . ALA B  1 188 ? 16.953  -19.888 3.587   1.00 11.41 ? 188 ALA B O   1 
ATOM   3712  C  CB  . ALA B  1 188 ? 17.218  -23.037 3.433   1.00 13.85 ? 188 ALA B CB  1 
ATOM   3713  N  N   A GLU B  1 189 ? 15.146  -20.617 2.344   0.50 10.67 ? 189 GLU B N   1 
ATOM   3714  N  N   B GLU B  1 189 ? 15.189  -20.661 2.279   0.50 10.45 ? 189 GLU B N   1 
ATOM   3715  C  CA  A GLU B  1 189 ? 15.092  -19.373 1.513   0.50 9.53  ? 189 GLU B CA  1 
ATOM   3716  C  CA  B GLU B  1 189 ? 14.972  -19.497 1.430   0.50 10.18 ? 189 GLU B CA  1 
ATOM   3717  C  C   A GLU B  1 189 ? 13.997  -18.441 1.996   0.50 9.47  ? 189 GLU B C   1 
ATOM   3718  C  C   B GLU B  1 189 ? 14.014  -18.506 2.130   0.50 9.04  ? 189 GLU B C   1 
ATOM   3719  O  O   A GLU B  1 189 ? 12.787  -18.789 1.944   0.50 9.37  ? 189 GLU B O   1 
ATOM   3720  O  O   B GLU B  1 189 ? 12.858  -18.839 2.387   0.50 8.64  ? 189 GLU B O   1 
ATOM   3721  C  CB  A GLU B  1 189 ? 14.949  -19.664 0.060   0.50 10.17 ? 189 GLU B CB  1 
ATOM   3722  C  CB  B GLU B  1 189 ? 14.385  -19.930 0.112   0.50 9.51  ? 189 GLU B CB  1 
ATOM   3723  C  CG  A GLU B  1 189 ? 16.034  -20.648 -0.433  0.50 9.81  ? 189 GLU B CG  1 
ATOM   3724  C  CG  B GLU B  1 189 ? 15.166  -20.976 -0.785  0.50 14.14 ? 189 GLU B CG  1 
ATOM   3725  C  CD  A GLU B  1 189 ? 15.653  -21.158 -1.765  0.50 20.76 ? 189 GLU B CD  1 
ATOM   3726  C  CD  B GLU B  1 189 ? 14.432  -21.224 -2.073  0.50 13.51 ? 189 GLU B CD  1 
ATOM   3727  O  OE1 A GLU B  1 189 ? 15.192  -20.299 -2.542  0.50 16.18 ? 189 GLU B OE1 1 
ATOM   3728  O  OE1 B GLU B  1 189 ? 14.686  -20.497 -3.052  0.50 18.51 ? 189 GLU B OE1 1 
ATOM   3729  O  OE2 A GLU B  1 189 ? 15.781  -22.397 -2.037  0.50 19.47 ? 189 GLU B OE2 1 
ATOM   3730  O  OE2 B GLU B  1 189 ? 13.585  -22.138 -2.102  0.50 23.51 ? 189 GLU B OE2 1 
ATOM   3731  N  N   . TYR B  1 190 ? 14.481  -17.290 2.438   1.00 9.02  ? 190 TYR B N   1 
ATOM   3732  C  CA  . TYR B  1 190 ? 13.611  -16.296 3.100   1.00 8.28  ? 190 TYR B CA  1 
ATOM   3733  C  C   . TYR B  1 190 ? 14.085  -14.904 2.933   1.00 10.17 ? 190 TYR B C   1 
ATOM   3734  O  O   . TYR B  1 190 ? 15.262  -14.587 2.570   1.00 9.45  ? 190 TYR B O   1 
ATOM   3735  C  CB  . TYR B  1 190 ? 13.436  -16.660 4.598   1.00 9.12  ? 190 TYR B CB  1 
ATOM   3736  C  CG  . TYR B  1 190 ? 14.724  -16.706 5.382   1.00 7.03  ? 190 TYR B CG  1 
ATOM   3737  C  CD1 . TYR B  1 190 ? 15.352  -15.533 5.810   1.00 7.64  ? 190 TYR B CD1 1 
ATOM   3738  C  CD2 . TYR B  1 190 ? 15.321  -17.961 5.718   1.00 10.52 ? 190 TYR B CD2 1 
ATOM   3739  C  CE1 . TYR B  1 190 ? 16.554  -15.607 6.565   1.00 8.25  ? 190 TYR B CE1 1 
ATOM   3740  C  CE2 . TYR B  1 190 ? 16.555  -17.995 6.447   1.00 8.13  ? 190 TYR B CE2 1 
ATOM   3741  C  CZ  . TYR B  1 190 ? 17.146  -16.848 6.824   1.00 8.23  ? 190 TYR B CZ  1 
ATOM   3742  O  OH  . TYR B  1 190 ? 18.330  -16.909 7.577   1.00 11.10 ? 190 TYR B OH  1 
ATOM   3743  N  N   . TYR B  1 191 ? 13.149  -13.988 3.253   1.00 7.38  ? 191 TYR B N   1 
ATOM   3744  C  CA  . TYR B  1 191 ? 13.475  -12.563 3.382   1.00 8.47  ? 191 TYR B CA  1 
ATOM   3745  C  C   . TYR B  1 191 ? 13.615  -12.175 4.867   1.00 8.10  ? 191 TYR B C   1 
ATOM   3746  O  O   . TYR B  1 191 ? 12.771  -12.672 5.676   1.00 7.75  ? 191 TYR B O   1 
ATOM   3747  C  CB  . TYR B  1 191 ? 12.279  -11.712 2.815   1.00 7.27  ? 191 TYR B CB  1 
ATOM   3748  C  CG  . TYR B  1 191 ? 11.851  -12.051 1.427   1.00 7.31  ? 191 TYR B CG  1 
ATOM   3749  C  CD1 . TYR B  1 191 ? 10.891  -13.054 1.180   1.00 8.41  ? 191 TYR B CD1 1 
ATOM   3750  C  CD2 . TYR B  1 191 ? 12.406  -11.346 0.303   1.00 8.54  ? 191 TYR B CD2 1 
ATOM   3751  C  CE1 . TYR B  1 191 ? 10.417  -13.360 -0.114  1.00 9.47  ? 191 TYR B CE1 1 
ATOM   3752  C  CE2 . TYR B  1 191 ? 11.932  -11.647 -0.975  1.00 8.40  ? 191 TYR B CE2 1 
ATOM   3753  C  CZ  . TYR B  1 191 ? 10.977  -12.670 -1.165  1.00 10.25 ? 191 TYR B CZ  1 
ATOM   3754  O  OH  . TYR B  1 191 ? 10.518  -12.944 -2.465  1.00 13.27 ? 191 TYR B OH  1 
ATOM   3755  N  N   . ARG B  1 192 ? 14.523  -11.309 5.270   1.00 7.99  ? 192 ARG B N   1 
ATOM   3756  C  CA  . ARG B  1 192 ? 14.723  -11.002 6.710   1.00 9.00  ? 192 ARG B CA  1 
ATOM   3757  C  C   . ARG B  1 192 ? 14.832  -9.492  6.808   1.00 8.03  ? 192 ARG B C   1 
ATOM   3758  O  O   . ARG B  1 192 ? 15.634  -8.863  6.055   1.00 8.08  ? 192 ARG B O   1 
ATOM   3759  C  CB  . ARG B  1 192 ? 16.049  -11.667 7.174   1.00 10.08 ? 192 ARG B CB  1 
ATOM   3760  C  CG  . ARG B  1 192 ? 16.652  -11.175 8.509   1.00 14.13 ? 192 ARG B CG  1 
ATOM   3761  C  CD  . ARG B  1 192 ? 15.782  -11.626 9.612   1.00 12.35 ? 192 ARG B CD  1 
ATOM   3762  N  NE  . ARG B  1 192 ? 15.558  -13.104 9.698   1.00 12.99 ? 192 ARG B NE  1 
ATOM   3763  C  CZ  . ARG B  1 192 ? 16.429  -14.087 9.907   1.00 10.93 ? 192 ARG B CZ  1 
ATOM   3764  N  NH1 . ARG B  1 192 ? 16.010  -15.350 9.941   1.00 14.64 ? 192 ARG B NH1 1 
ATOM   3765  N  NH2 . ARG B  1 192 ? 17.742  -13.828 10.184  1.00 11.85 ? 192 ARG B NH2 1 
ATOM   3766  N  N   . TYR B  1 193 ? 14.123  -8.839  7.717   1.00 6.16  ? 193 TYR B N   1 
ATOM   3767  C  CA  . TYR B  1 193 ? 14.269  -7.414  7.955   1.00 7.25  ? 193 TYR B CA  1 
ATOM   3768  C  C   . TYR B  1 193 ? 13.773  -6.989  9.354   1.00 6.40  ? 193 TYR B C   1 
ATOM   3769  O  O   . TYR B  1 193 ? 12.941  -7.721  9.959   1.00 7.87  ? 193 TYR B O   1 
ATOM   3770  C  CB  . TYR B  1 193 ? 13.568  -6.588  6.793   1.00 7.93  ? 193 TYR B CB  1 
ATOM   3771  C  CG  . TYR B  1 193 ? 12.019  -6.572  6.914   1.00 5.31  ? 193 TYR B CG  1 
ATOM   3772  C  CD1 . TYR B  1 193 ? 11.409  -5.517  7.495   1.00 4.45  ? 193 TYR B CD1 1 
ATOM   3773  C  CD2 . TYR B  1 193 ? 11.227  -7.618  6.484   1.00 5.85  ? 193 TYR B CD2 1 
ATOM   3774  C  CE1 . TYR B  1 193 ? 10.036  -5.426  7.666   1.00 5.57  ? 193 TYR B CE1 1 
ATOM   3775  C  CE2 . TYR B  1 193 ? 9.822   -7.571  6.629   1.00 6.99  ? 193 TYR B CE2 1 
ATOM   3776  C  CZ  . TYR B  1 193 ? 9.231   -6.466  7.230   1.00 5.83  ? 193 TYR B CZ  1 
ATOM   3777  O  OH  . TYR B  1 193 ? 7.859   -6.351  7.382   1.00 5.62  ? 193 TYR B OH  1 
ATOM   3778  N  N   . ARG B  1 194 ? 14.204  -5.847  9.829   1.00 7.62  ? 194 ARG B N   1 
ATOM   3779  C  CA  . ARG B  1 194 ? 13.749  -5.299  11.114  1.00 10.00 ? 194 ARG B CA  1 
ATOM   3780  C  C   . ARG B  1 194 ? 12.458  -4.473  10.815  1.00 8.46  ? 194 ARG B C   1 
ATOM   3781  O  O   . ARG B  1 194 ? 12.430  -3.536  9.977   1.00 8.16  ? 194 ARG B O   1 
ATOM   3782  C  CB  . ARG B  1 194 ? 14.781  -4.267  11.686  1.00 10.95 ? 194 ARG B CB  1 
ATOM   3783  C  CG  . ARG B  1 194 ? 15.884  -4.853  12.606  1.00 16.69 ? 194 ARG B CG  1 
ATOM   3784  C  CD  . ARG B  1 194 ? 16.412  -3.834  13.644  1.00 19.99 ? 194 ARG B CD  1 
ATOM   3785  N  NE  . ARG B  1 194 ? 15.355  -3.382  14.549  1.00 21.94 ? 194 ARG B NE  1 
ATOM   3786  C  CZ  . ARG B  1 194 ? 15.467  -2.381  15.420  1.00 23.48 ? 194 ARG B CZ  1 
ATOM   3787  N  NH1 . ARG B  1 194 ? 14.435  -2.057  16.187  1.00 25.92 ? 194 ARG B NH1 1 
ATOM   3788  N  NH2 . ARG B  1 194 ? 16.602  -1.704  15.531  1.00 25.51 ? 194 ARG B NH2 1 
ATOM   3789  N  N   . GLY B  1 195 ? 11.391  -4.843  11.535  1.00 7.78  ? 195 GLY B N   1 
ATOM   3790  C  CA  . GLY B  1 195 ? 10.101  -4.150  11.334  1.00 7.08  ? 195 GLY B CA  1 
ATOM   3791  C  C   . GLY B  1 195 ? 9.342   -4.047  12.639  1.00 7.94  ? 195 GLY B C   1 
ATOM   3792  O  O   . GLY B  1 195 ? 9.912   -3.940  13.729  1.00 7.60  ? 195 GLY B O   1 
ATOM   3793  N  N   . SER B  1 196 ? 8.031   -4.083  12.529  1.00 6.48  ? 196 SER B N   1 
ATOM   3794  C  CA  . SER B  1 196 ? 7.097   -3.831  13.613  1.00 5.01  ? 196 SER B CA  1 
ATOM   3795  C  C   . SER B  1 196 ? 5.994   -4.850  13.677  1.00 5.00  ? 196 SER B C   1 
ATOM   3796  O  O   . SER B  1 196 ? 5.747   -5.716  12.752  1.00 6.45  ? 196 SER B O   1 
ATOM   3797  C  CB  . SER B  1 196 ? 6.491   -2.415  13.443  1.00 7.17  ? 196 SER B CB  1 
ATOM   3798  O  OG  . SER B  1 196 ? 5.477   -2.425  12.459  1.00 5.99  ? 196 SER B OG  1 
ATOM   3799  N  N   . LEU B  1 197 ? 5.302   -4.756  14.842  1.00 6.05  ? 197 LEU B N   1 
ATOM   3800  C  CA  . LEU B  1 197 ? 3.934   -5.392  14.864  1.00 6.57  ? 197 LEU B CA  1 
ATOM   3801  C  C   . LEU B  1 197 ? 3.133   -4.683  13.751  1.00 5.95  ? 197 LEU B C   1 
ATOM   3802  O  O   . LEU B  1 197 ? 3.172   -3.454  13.599  1.00 5.40  ? 197 LEU B O   1 
ATOM   3803  C  CB  . LEU B  1 197 ? 3.317   -5.088  16.253  1.00 6.35  ? 197 LEU B CB  1 
ATOM   3804  C  CG  . LEU B  1 197 ? 4.063   -5.741  17.450  1.00 7.10  ? 197 LEU B CG  1 
ATOM   3805  C  CD1 . LEU B  1 197 ? 3.429   -5.268  18.770  1.00 11.07 ? 197 LEU B CD1 1 
ATOM   3806  C  CD2 . LEU B  1 197 ? 4.060   -7.256  17.325  1.00 9.00  ? 197 LEU B CD2 1 
ATOM   3807  N  N   . THR B  1 198 ? 2.269   -5.505  13.130  1.00 6.15  ? 198 THR B N   1 
ATOM   3808  C  CA  . THR B  1 198 ? 1.433   -4.980  11.995  1.00 5.36  ? 198 THR B CA  1 
ATOM   3809  C  C   . THR B  1 198 ? 0.029   -4.539  12.436  1.00 7.03  ? 198 THR B C   1 
ATOM   3810  O  O   . THR B  1 198 ? -0.794  -4.137  11.594  1.00 6.34  ? 198 THR B O   1 
ATOM   3811  C  CB  . THR B  1 198 ? 1.247   -6.020  10.897  1.00 4.66  ? 198 THR B CB  1 
ATOM   3812  O  OG1 . THR B  1 198 ? 0.533   -7.127  11.442  1.00 5.14  ? 198 THR B OG1 1 
ATOM   3813  C  CG2 . THR B  1 198 ? 2.569   -6.493  10.247  1.00 4.78  ? 198 THR B CG2 1 
ATOM   3814  N  N   . THR B  1 199 ? -0.258  -4.610  13.748  1.00 6.91  ? 199 THR B N   1 
ATOM   3815  C  CA  . THR B  1 199 ? -1.482  -4.070  14.321  1.00 7.17  ? 199 THR B CA  1 
ATOM   3816  C  C   . THR B  1 199 ? -1.105  -3.218  15.540  1.00 6.58  ? 199 THR B C   1 
ATOM   3817  O  O   . THR B  1 199 ? 0.069   -3.315  16.029  1.00 6.64  ? 199 THR B O   1 
ATOM   3818  C  CB  . THR B  1 199 ? -2.493  -5.108  14.850  1.00 8.69  ? 199 THR B CB  1 
ATOM   3819  O  OG1 . THR B  1 199 ? -2.046  -5.615  16.120  1.00 10.07 ? 199 THR B OG1 1 
ATOM   3820  C  CG2 . THR B  1 199 ? -2.669  -6.335  13.947  1.00 8.01  ? 199 THR B CG2 1 
ATOM   3821  N  N   . PRO B  1 200 ? -2.000  -2.324  15.936  1.00 7.39  ? 200 PRO B N   1 
ATOM   3822  C  CA  . PRO B  1 200 ? -1.703  -1.590  17.203  1.00 7.76  ? 200 PRO B CA  1 
ATOM   3823  C  C   . PRO B  1 200 ? -1.232  -2.625  18.318  1.00 8.22  ? 200 PRO B C   1 
ATOM   3824  O  O   . PRO B  1 200 ? -1.806  -3.668  18.438  1.00 7.43  ? 200 PRO B O   1 
ATOM   3825  C  CB  . PRO B  1 200 ? -3.040  -0.999  17.546  1.00 7.29  ? 200 PRO B CB  1 
ATOM   3826  C  CG  . PRO B  1 200 ? -3.683  -0.710  16.151  1.00 6.47  ? 200 PRO B CG  1 
ATOM   3827  C  CD  . PRO B  1 200 ? -3.353  -2.021  15.406  1.00 7.28  ? 200 PRO B CD  1 
ATOM   3828  N  N   . PRO B  1 201 ? -0.237  -2.276  19.141  1.00 6.55  ? 201 PRO B N   1 
ATOM   3829  C  CA  . PRO B  1 201 ? 0.433   -0.970  19.211  1.00 5.86  ? 201 PRO B CA  1 
ATOM   3830  C  C   . PRO B  1 201 ? 1.544   -0.645  18.177  1.00 7.10  ? 201 PRO B C   1 
ATOM   3831  O  O   . PRO B  1 201 ? 2.188   0.450   18.338  1.00 7.26  ? 201 PRO B O   1 
ATOM   3832  C  CB  . PRO B  1 201 ? 0.961   -0.950  20.695  1.00 7.00  ? 201 PRO B CB  1 
ATOM   3833  C  CG  . PRO B  1 201 ? 1.312   -2.338  20.919  1.00 7.63  ? 201 PRO B CG  1 
ATOM   3834  C  CD  . PRO B  1 201 ? 0.191   -3.218  20.223  1.00 7.20  ? 201 PRO B CD  1 
ATOM   3835  N  N   . CYS B  1 202 ? 1.782   -1.523  17.219  1.00 6.17  ? 202 CYS B N   1 
ATOM   3836  C  CA  . CYS B  1 202 ? 2.738   -1.242  16.120  1.00 6.81  ? 202 CYS B CA  1 
ATOM   3837  C  C   . CYS B  1 202 ? 4.187   -1.050  16.629  1.00 7.29  ? 202 CYS B C   1 
ATOM   3838  O  O   . CYS B  1 202 ? 5.008   -0.468  15.925  1.00 7.55  ? 202 CYS B O   1 
ATOM   3839  C  CB  . CYS B  1 202 ? 2.369   0.052   15.396  1.00 5.86  ? 202 CYS B CB  1 
ATOM   3840  S  SG  . CYS B  1 202 ? 0.687   -0.095  14.569  1.00 6.65  ? 202 CYS B SG  1 
ATOM   3841  N  N   . ASN B  1 203 ? 4.522   -1.706  17.752  1.00 6.48  ? 203 ASN B N   1 
ATOM   3842  C  CA  . ASN B  1 203 ? 5.920   -1.501  18.333  1.00 7.04  ? 203 ASN B CA  1 
ATOM   3843  C  C   . ASN B  1 203 ? 6.949   -1.927  17.299  1.00 7.26  ? 203 ASN B C   1 
ATOM   3844  O  O   . ASN B  1 203 ? 6.820   -3.019  16.694  1.00 6.18  ? 203 ASN B O   1 
ATOM   3845  C  CB  . ASN B  1 203 ? 6.076   -2.442  19.529  1.00 7.63  ? 203 ASN B CB  1 
ATOM   3846  C  CG  . ASN B  1 203 ? 5.049   -2.194  20.635  1.00 8.00  ? 203 ASN B CG  1 
ATOM   3847  O  OD1 . ASN B  1 203 ? 4.433   -1.120  20.686  1.00 10.30 ? 203 ASN B OD1 1 
ATOM   3848  N  ND2 . ASN B  1 203 ? 4.911   -3.150  21.525  1.00 10.36 ? 203 ASN B ND2 1 
ATOM   3849  N  N   . PRO B  1 204 ? 8.020   -1.120  17.164  1.00 7.15  ? 204 PRO B N   1 
ATOM   3850  C  CA  . PRO B  1 204 ? 9.037   -1.509  16.144  1.00 7.98  ? 204 PRO B CA  1 
ATOM   3851  C  C   . PRO B  1 204 ? 10.057  -2.437  16.744  1.00 9.36  ? 204 PRO B C   1 
ATOM   3852  O  O   . PRO B  1 204 ? 11.294  -2.073  16.796  1.00 10.52 ? 204 PRO B O   1 
ATOM   3853  C  CB  . PRO B  1 204 ? 9.669   -0.126  15.862  1.00 7.30  ? 204 PRO B CB  1 
ATOM   3854  C  CG  . PRO B  1 204 ? 9.590   0.677   17.198  1.00 8.90  ? 204 PRO B CG  1 
ATOM   3855  C  CD  . PRO B  1 204 ? 8.165   0.269   17.720  1.00 7.64  ? 204 PRO B CD  1 
ATOM   3856  N  N   . THR B  1 205 ? 9.620   -3.610  17.211  1.00 6.69  ? 205 THR B N   1 
ATOM   3857  C  CA  . THR B  1 205 ? 10.459  -4.533  17.977  1.00 8.37  ? 205 THR B CA  1 
ATOM   3858  C  C   . THR B  1 205 ? 10.480  -5.929  17.372  1.00 7.37  ? 205 THR B C   1 
ATOM   3859  O  O   . THR B  1 205 ? 10.906  -6.902  18.033  1.00 9.79  ? 205 THR B O   1 
ATOM   3860  C  CB  . THR B  1 205 ? 9.918   -4.641  19.433  1.00 8.00  ? 205 THR B CB  1 
ATOM   3861  O  OG1 . THR B  1 205 ? 8.543   -5.026  19.245  1.00 9.62  ? 205 THR B OG1 1 
ATOM   3862  C  CG2 . THR B  1 205 ? 10.072  -3.324  20.089  1.00 9.09  ? 205 THR B CG2 1 
ATOM   3863  N  N   . VAL B  1 206 ? 10.133  -6.073  16.054  1.00 7.42  ? 206 VAL B N   1 
ATOM   3864  C  CA  . VAL B  1 206 ? 10.016  -7.382  15.488  1.00 6.62  ? 206 VAL B CA  1 
ATOM   3865  C  C   . VAL B  1 206 ? 11.106  -7.649  14.441  1.00 8.22  ? 206 VAL B C   1 
ATOM   3866  O  O   . VAL B  1 206 ? 11.280  -6.826  13.491  1.00 9.47  ? 206 VAL B O   1 
ATOM   3867  C  CB  . VAL B  1 206 ? 8.656   -7.573  14.755  1.00 6.94  ? 206 VAL B CB  1 
ATOM   3868  C  CG1 . VAL B  1 206 ? 8.530   -8.916  14.089  1.00 7.73  ? 206 VAL B CG1 1 
ATOM   3869  C  CG2 . VAL B  1 206 ? 7.479   -7.438  15.783  1.00 9.68  ? 206 VAL B CG2 1 
ATOM   3870  N  N   . LEU B  1 207 ? 11.786  -8.787  14.596  1.00 6.75  ? 207 LEU B N   1 
ATOM   3871  C  CA  . LEU B  1 207 ? 12.676  -9.297  13.549  1.00 8.56  ? 207 LEU B CA  1 
ATOM   3872  C  C   . LEU B  1 207 ? 11.776  -10.223 12.649  1.00 8.17  ? 207 LEU B C   1 
ATOM   3873  O  O   . LEU B  1 207 ? 11.315  -11.287 13.096  1.00 6.57  ? 207 LEU B O   1 
ATOM   3874  C  CB  . LEU B  1 207 ? 13.851  -10.016 14.193  1.00 8.45  ? 207 LEU B CB  1 
ATOM   3875  C  CG  . LEU B  1 207 ? 14.864  -10.513 13.114  1.00 13.36 ? 207 LEU B CG  1 
ATOM   3876  C  CD1 . LEU B  1 207 ? 15.530  -9.352  12.324  1.00 14.04 ? 207 LEU B CD1 1 
ATOM   3877  C  CD2 . LEU B  1 207 ? 15.960  -11.343 13.794  1.00 17.16 ? 207 LEU B CD2 1 
ATOM   3878  N  N   . TRP B  1 208 ? 11.582  -9.823  11.374  1.00 8.31  ? 208 TRP B N   1 
ATOM   3879  C  CA  . TRP B  1 208 ? 10.713  -10.596 10.490  1.00 6.50  ? 208 TRP B CA  1 
ATOM   3880  C  C   . TRP B  1 208 ? 11.444  -11.610 9.638   1.00 6.63  ? 208 TRP B C   1 
ATOM   3881  O  O   . TRP B  1 208 ? 12.542  -11.213 9.117   1.00 8.05  ? 208 TRP B O   1 
ATOM   3882  C  CB  . TRP B  1 208 ? 9.964   -9.616  9.484   1.00 6.36  ? 208 TRP B CB  1 
ATOM   3883  C  CG  . TRP B  1 208 ? 8.780   -8.919  10.159  1.00 5.32  ? 208 TRP B CG  1 
ATOM   3884  C  CD1 . TRP B  1 208 ? 8.756   -7.652  10.752  1.00 6.52  ? 208 TRP B CD1 1 
ATOM   3885  C  CD2 . TRP B  1 208 ? 7.481   -9.491  10.345  1.00 5.19  ? 208 TRP B CD2 1 
ATOM   3886  N  NE1 . TRP B  1 208 ? 7.503   -7.436  11.298  1.00 5.51  ? 208 TRP B NE1 1 
ATOM   3887  C  CE2 . TRP B  1 208 ? 6.696   -8.521  11.033  1.00 5.82  ? 208 TRP B CE2 1 
ATOM   3888  C  CE3 . TRP B  1 208 ? 6.909   -10.737 9.994   1.00 6.00  ? 208 TRP B CE3 1 
ATOM   3889  C  CZ2 . TRP B  1 208 ? 5.360   -8.762  11.403  1.00 6.45  ? 208 TRP B CZ2 1 
ATOM   3890  C  CZ3 . TRP B  1 208 ? 5.549   -10.954 10.322  1.00 6.03  ? 208 TRP B CZ3 1 
ATOM   3891  C  CH2 . TRP B  1 208 ? 4.837   -9.983  11.084  1.00 6.02  ? 208 TRP B CH2 1 
ATOM   3892  N  N   . THR B  1 209 ? 10.914  -12.795 9.488   1.00 6.76  ? 209 THR B N   1 
ATOM   3893  C  CA  . THR B  1 209 ? 11.366  -13.757 8.538   1.00 7.19  ? 209 THR B CA  1 
ATOM   3894  C  C   . THR B  1 209 ? 10.192  -14.141 7.669   1.00 7.59  ? 209 THR B C   1 
ATOM   3895  O  O   . THR B  1 209 ? 9.220   -14.729 8.234   1.00 8.60  ? 209 THR B O   1 
ATOM   3896  C  CB  . THR B  1 209 ? 11.998  -15.021 9.199   1.00 6.67  ? 209 THR B CB  1 
ATOM   3897  O  OG1 . THR B  1 209 ? 13.087  -14.545 10.072  1.00 8.72  ? 209 THR B OG1 1 
ATOM   3898  C  CG2 . THR B  1 209 ? 12.433  -15.982 8.112   1.00 7.88  ? 209 THR B CG2 1 
ATOM   3899  N  N   . VAL B  1 210 ? 10.223  -13.837 6.361   1.00 6.77  ? 210 VAL B N   1 
ATOM   3900  C  CA  . VAL B  1 210 ? 9.051   -14.142 5.523   1.00 5.11  ? 210 VAL B CA  1 
ATOM   3901  C  C   . VAL B  1 210 ? 9.598   -15.228 4.558   1.00 7.88  ? 210 VAL B C   1 
ATOM   3902  O  O   . VAL B  1 210 ? 10.570  -15.047 3.767   1.00 7.29  ? 210 VAL B O   1 
ATOM   3903  C  CB  . VAL B  1 210 ? 8.604   -12.915 4.684   1.00 6.13  ? 210 VAL B CB  1 
ATOM   3904  C  CG1 . VAL B  1 210 ? 7.397   -13.330 3.797   1.00 7.21  ? 210 VAL B CG1 1 
ATOM   3905  C  CG2 . VAL B  1 210 ? 8.301   -11.761 5.557   1.00 7.32  ? 210 VAL B CG2 1 
ATOM   3906  N  N   . PHE B  1 211 ? 9.053   -16.425 4.641   1.00 8.08  ? 211 PHE B N   1 
ATOM   3907  C  CA  . PHE B  1 211 ? 9.572   -17.469 3.762   1.00 7.41  ? 211 PHE B CA  1 
ATOM   3908  C  C   . PHE B  1 211 ? 9.306   -17.168 2.311   1.00 7.52  ? 211 PHE B C   1 
ATOM   3909  O  O   . PHE B  1 211 ? 8.268   -16.655 1.972   1.00 8.53  ? 211 PHE B O   1 
ATOM   3910  C  CB  . PHE B  1 211 ? 9.003   -18.874 4.211   1.00 7.92  ? 211 PHE B CB  1 
ATOM   3911  C  CG  . PHE B  1 211 ? 9.446   -19.262 5.589   1.00 8.42  ? 211 PHE B CG  1 
ATOM   3912  C  CD1 . PHE B  1 211 ? 8.544   -19.287 6.651   1.00 8.81  ? 211 PHE B CD1 1 
ATOM   3913  C  CD2 . PHE B  1 211 ? 10.819  -19.542 5.835   1.00 8.98  ? 211 PHE B CD2 1 
ATOM   3914  C  CE1 . PHE B  1 211 ? 8.928   -19.597 7.923   1.00 8.71  ? 211 PHE B CE1 1 
ATOM   3915  C  CE2 . PHE B  1 211 ? 11.233  -19.875 7.174   1.00 10.75 ? 211 PHE B CE2 1 
ATOM   3916  C  CZ  . PHE B  1 211 ? 10.284  -19.907 8.177   1.00 10.13 ? 211 PHE B CZ  1 
ATOM   3917  N  N   . ARG B  1 212 ? 10.234  -17.585 1.407   1.00 8.51  ? 212 ARG B N   1 
ATOM   3918  C  CA  . ARG B  1 212 ? 10.097  -17.286 -0.016  1.00 8.93  ? 212 ARG B CA  1 
ATOM   3919  C  C   . ARG B  1 212 ? 9.005   -18.027 -0.651  1.00 10.74 ? 212 ARG B C   1 
ATOM   3920  O  O   . ARG B  1 212 ? 8.310   -17.456 -1.492  1.00 10.63 ? 212 ARG B O   1 
ATOM   3921  C  CB  . ARG B  1 212 ? 11.407  -17.715 -0.760  1.00 9.23  ? 212 ARG B CB  1 
ATOM   3922  C  CG  . ARG B  1 212 ? 11.465  -17.277 -2.228  1.00 11.68 ? 212 ARG B CG  1 
ATOM   3923  C  CD  . ARG B  1 212 ? 12.640  -18.022 -2.894  1.00 14.25 ? 212 ARG B CD  1 
ATOM   3924  N  NE  . ARG B  1 212 ? 12.813  -17.454 -4.230  1.00 20.61 ? 212 ARG B NE  1 
ATOM   3925  C  CZ  . ARG B  1 212 ? 13.896  -17.678 -5.019  1.00 19.23 ? 212 ARG B CZ  1 
ATOM   3926  N  NH1 . ARG B  1 212 ? 14.845  -18.510 -4.588  1.00 17.57 ? 212 ARG B NH1 1 
ATOM   3927  N  NH2 . ARG B  1 212 ? 13.980  -17.054 -6.235  1.00 23.44 ? 212 ARG B NH2 1 
ATOM   3928  N  N   . ASN B  1 213 ? 8.838   -19.307 -0.267  1.00 9.36  ? 213 ASN B N   1 
ATOM   3929  C  CA  . ASN B  1 213 ? 7.839   -20.143 -0.926  1.00 9.10  ? 213 ASN B CA  1 
ATOM   3930  C  C   . ASN B  1 213 ? 6.535   -20.187 -0.184  1.00 9.75  ? 213 ASN B C   1 
ATOM   3931  O  O   . ASN B  1 213 ? 6.509   -20.241 1.081   1.00 9.23  ? 213 ASN B O   1 
ATOM   3932  C  CB  . ASN B  1 213 ? 8.408   -21.606 -1.008  1.00 11.47 ? 213 ASN B CB  1 
ATOM   3933  C  CG  . ASN B  1 213 ? 9.653   -21.640 -1.854  1.00 14.65 ? 213 ASN B CG  1 
ATOM   3934  O  OD1 . ASN B  1 213 ? 9.662   -21.048 -2.948  1.00 20.09 ? 213 ASN B OD1 1 
ATOM   3935  N  ND2 . ASN B  1 213 ? 10.661  -22.207 -1.333  1.00 20.30 ? 213 ASN B ND2 1 
ATOM   3936  N  N   . PRO B  1 214 ? 5.404   -20.093 -0.940  1.00 10.80 ? 214 PRO B N   1 
ATOM   3937  C  CA  . PRO B  1 214 ? 4.103   -20.144 -0.278  1.00 10.36 ? 214 PRO B CA  1 
ATOM   3938  C  C   . PRO B  1 214 ? 3.683   -21.583 0.002   1.00 11.34 ? 214 PRO B C   1 
ATOM   3939  O  O   . PRO B  1 214 ? 4.240   -22.526 -0.588  1.00 12.77 ? 214 PRO B O   1 
ATOM   3940  C  CB  . PRO B  1 214 ? 3.108   -19.479 -1.326  1.00 9.90  ? 214 PRO B CB  1 
ATOM   3941  C  CG  . PRO B  1 214 ? 3.724   -19.965 -2.713  1.00 15.22 ? 214 PRO B CG  1 
ATOM   3942  C  CD  . PRO B  1 214 ? 5.304   -19.886 -2.419  1.00 11.50 ? 214 PRO B CD  1 
ATOM   3943  N  N   . VAL B  1 215 ? 2.638   -21.751 0.858   1.00 9.54  ? 215 VAL B N   1 
ATOM   3944  C  CA  . VAL B  1 215 ? 1.867   -23.019 1.028   1.00 9.46  ? 215 VAL B CA  1 
ATOM   3945  C  C   . VAL B  1 215 ? 0.543   -22.828 0.334   1.00 9.52  ? 215 VAL B C   1 
ATOM   3946  O  O   . VAL B  1 215 ? 0.161   -21.718 -0.029  1.00 10.67 ? 215 VAL B O   1 
ATOM   3947  C  CB  . VAL B  1 215 ? 1.677   -23.377 2.516   1.00 11.02 ? 215 VAL B CB  1 
ATOM   3948  C  CG1 . VAL B  1 215 ? 3.006   -23.563 3.175   1.00 12.25 ? 215 VAL B CG1 1 
ATOM   3949  C  CG2 . VAL B  1 215 ? 0.737   -22.342 3.176   1.00 12.24 ? 215 VAL B CG2 1 
ATOM   3950  N  N   . GLN B  1 216 ? -0.150  -23.912 0.140   1.00 10.41 ? 216 GLN B N   1 
ATOM   3951  C  CA  . GLN B  1 216 ? -1.492  -23.894 -0.531  1.00 11.01 ? 216 GLN B CA  1 
ATOM   3952  C  C   . GLN B  1 216 ? -2.566  -24.432 0.411   1.00 11.69 ? 216 GLN B C   1 
ATOM   3953  O  O   . GLN B  1 216 ? -2.286  -25.288 1.260   1.00 11.64 ? 216 GLN B O   1 
ATOM   3954  C  CB  . GLN B  1 216 ? -1.574  -24.834 -1.774  1.00 12.43 ? 216 GLN B CB  1 
ATOM   3955  C  CG  . GLN B  1 216 ? -0.632  -24.267 -2.792  1.00 15.34 ? 216 GLN B CG  1 
ATOM   3956  C  CD  . GLN B  1 216 ? -0.744  -24.902 -4.102  1.00 19.94 ? 216 GLN B CD  1 
ATOM   3957  O  OE1 . GLN B  1 216 ? -1.287  -26.042 -4.254  1.00 22.60 ? 216 GLN B OE1 1 
ATOM   3958  N  NE2 . GLN B  1 216 ? -0.294  -24.157 -5.098  1.00 24.53 ? 216 GLN B NE2 1 
ATOM   3959  N  N   . ILE B  1 217 ? -3.735  -23.761 0.412   1.00 11.79 ? 217 ILE B N   1 
ATOM   3960  C  CA  . ILE B  1 217 ? -4.938  -24.291 1.060   1.00 10.85 ? 217 ILE B CA  1 
ATOM   3961  C  C   . ILE B  1 217 ? -5.999  -24.309 -0.061  1.00 9.89  ? 217 ILE B C   1 
ATOM   3962  O  O   . ILE B  1 217 ? -5.889  -23.581 -1.089  1.00 10.04 ? 217 ILE B O   1 
ATOM   3963  C  CB  . ILE B  1 217 ? -5.343  -23.474 2.317   1.00 11.35 ? 217 ILE B CB  1 
ATOM   3964  C  CG1 . ILE B  1 217 ? -5.812  -22.052 1.862   1.00 9.51  ? 217 ILE B CG1 1 
ATOM   3965  C  CG2 . ILE B  1 217 ? -4.224  -23.496 3.426   1.00 10.25 ? 217 ILE B CG2 1 
ATOM   3966  C  CD1 . ILE B  1 217 ? -6.391  -21.249 3.078   1.00 11.08 ? 217 ILE B CD1 1 
ATOM   3967  N  N   . SER B  1 218 ? -7.052  -25.161 0.164   1.00 11.02 ? 218 SER B N   1 
ATOM   3968  C  CA  . SER B  1 218 ? -7.997  -25.252 -0.936  1.00 11.84 ? 218 SER B CA  1 
ATOM   3969  C  C   . SER B  1 218 ? -8.876  -23.993 -1.043  1.00 13.40 ? 218 SER B C   1 
ATOM   3970  O  O   . SER B  1 218 ? -9.020  -23.219 -0.012  1.00 13.68 ? 218 SER B O   1 
ATOM   3971  C  CB  . SER B  1 218 ? -8.874  -26.503 -0.746  1.00 13.04 ? 218 SER B CB  1 
ATOM   3972  O  OG  . SER B  1 218 ? -9.753  -26.388 0.364   1.00 14.30 ? 218 SER B OG  1 
ATOM   3973  N  N   . GLN B  1 219 ? -9.599  -23.874 -2.154  1.00 14.92 ? 219 GLN B N   1 
ATOM   3974  C  CA  . GLN B  1 219 ? -10.609 -22.769 -2.233  1.00 16.61 ? 219 GLN B CA  1 
ATOM   3975  C  C   . GLN B  1 219 ? -11.668 -22.900 -1.142  1.00 13.96 ? 219 GLN B C   1 
ATOM   3976  O  O   . GLN B  1 219 ? -12.119 -21.881 -0.533  1.00 13.34 ? 219 GLN B O   1 
ATOM   3977  C  CB  . GLN B  1 219 ? -11.227 -22.677 -3.640  1.00 18.03 ? 219 GLN B CB  1 
ATOM   3978  C  CG  . GLN B  1 219 ? -12.164 -23.767 -4.077  1.00 22.72 ? 219 GLN B CG  1 
ATOM   3979  C  CD  . GLN B  1 219 ? -12.523 -23.630 -5.650  1.00 21.45 ? 219 GLN B CD  1 
ATOM   3980  O  OE1 . GLN B  1 219 ? -13.687 -23.764 -6.041  1.00 34.58 ? 219 GLN B OE1 1 
ATOM   3981  N  NE2 . GLN B  1 219 ? -11.511 -23.314 -6.511  1.00 31.05 ? 219 GLN B NE2 1 
ATOM   3982  N  N   . GLU B  1 220 ? -12.070 -24.126 -0.796  1.00 12.49 ? 220 GLU B N   1 
ATOM   3983  C  CA  . GLU B  1 220 ? -13.064 -24.302 0.235   1.00 12.53 ? 220 GLU B CA  1 
ATOM   3984  C  C   . GLU B  1 220 ? -12.504 -23.889 1.629   1.00 11.42 ? 220 GLU B C   1 
ATOM   3985  O  O   . GLU B  1 220 ? -13.234 -23.218 2.438   1.00 13.04 ? 220 GLU B O   1 
ATOM   3986  C  CB  . GLU B  1 220 ? -13.553 -25.827 0.291   1.00 14.00 ? 220 GLU B CB  1 
ATOM   3987  C  CG  . GLU B  1 220 ? -14.354 -26.305 -0.999  1.00 14.92 ? 220 GLU B CG  1 
ATOM   3988  C  CD  . GLU B  1 220 ? -13.525 -26.463 -2.223  1.00 22.16 ? 220 GLU B CD  1 
ATOM   3989  O  OE1 . GLU B  1 220 ? -12.237 -26.625 -2.121  1.00 18.43 ? 220 GLU B OE1 1 
ATOM   3990  O  OE2 . GLU B  1 220 ? -14.133 -26.445 -3.334  1.00 28.88 ? 220 GLU B OE2 1 
ATOM   3991  N  N   . GLN B  1 221 ? -11.240 -24.186 1.904   1.00 9.79  ? 221 GLN B N   1 
ATOM   3992  C  CA  . GLN B  1 221 ? -10.652 -23.833 3.214   1.00 9.16  ? 221 GLN B CA  1 
ATOM   3993  C  C   . GLN B  1 221 ? -10.498 -22.300 3.266   1.00 8.75  ? 221 GLN B C   1 
ATOM   3994  O  O   . GLN B  1 221 ? -10.810 -21.739 4.322   1.00 8.50  ? 221 GLN B O   1 
ATOM   3995  C  CB  . GLN B  1 221 ? -9.252  -24.423 3.308   1.00 11.23 ? 221 GLN B CB  1 
ATOM   3996  C  CG  . GLN B  1 221 ? -9.273  -25.974 3.602   1.00 10.93 ? 221 GLN B CG  1 
ATOM   3997  C  CD  . GLN B  1 221 ? -7.846  -26.534 3.764   1.00 9.17  ? 221 GLN B CD  1 
ATOM   3998  O  OE1 . GLN B  1 221 ? -7.043  -26.500 2.738   1.00 11.69 ? 221 GLN B OE1 1 
ATOM   3999  N  NE2 . GLN B  1 221 ? -7.523  -27.010 4.940   1.00 9.93  ? 221 GLN B NE2 1 
ATOM   4000  N  N   . LEU B  1 222 ? -10.103 -21.679 2.181   1.00 9.52  ? 222 LEU B N   1 
ATOM   4001  C  CA  . LEU B  1 222 ? -9.933  -20.207 2.184   1.00 9.58  ? 222 LEU B CA  1 
ATOM   4002  C  C   . LEU B  1 222 ? -11.297 -19.529 2.435   1.00 8.10  ? 222 LEU B C   1 
ATOM   4003  O  O   . LEU B  1 222 ? -11.405 -18.627 3.243   1.00 9.24  ? 222 LEU B O   1 
ATOM   4004  C  CB  . LEU B  1 222 ? -9.320  -19.771 0.828   1.00 10.35 ? 222 LEU B CB  1 
ATOM   4005  C  CG  . LEU B  1 222 ? -9.140  -18.278 0.656   1.00 11.13 ? 222 LEU B CG  1 
ATOM   4006  C  CD1 . LEU B  1 222 ? -8.197  -17.665 1.823   1.00 11.49 ? 222 LEU B CD1 1 
ATOM   4007  C  CD2 . LEU B  1 222 ? -8.583  -18.039 -0.730  1.00 11.56 ? 222 LEU B CD2 1 
ATOM   4008  N  N   . LEU B  1 223 ? -12.360 -19.996 1.750   1.00 9.55  ? 223 LEU B N   1 
ATOM   4009  C  CA  . LEU B  1 223 ? -13.679 -19.434 1.937   1.00 9.17  ? 223 LEU B CA  1 
ATOM   4010  C  C   . LEU B  1 223 ? -14.162 -19.620 3.375   1.00 8.69  ? 223 LEU B C   1 
ATOM   4011  O  O   . LEU B  1 223 ? -14.775 -18.719 3.998   1.00 8.76  ? 223 LEU B O   1 
ATOM   4012  C  CB  . LEU B  1 223 ? -14.708 -20.074 0.986   1.00 11.01 ? 223 LEU B CB  1 
ATOM   4013  C  CG  . LEU B  1 223 ? -16.067 -19.409 0.925   1.00 11.03 ? 223 LEU B CG  1 
ATOM   4014  C  CD1 . LEU B  1 223 ? -16.007 -17.964 0.585   1.00 11.89 ? 223 LEU B CD1 1 
ATOM   4015  C  CD2 . LEU B  1 223 ? -17.061 -20.224 0.034   1.00 14.42 ? 223 LEU B CD2 1 
ATOM   4016  N  N   . ALA B  1 224 ? -13.965 -20.810 3.918   1.00 7.87  ? 224 ALA B N   1 
ATOM   4017  C  CA  . ALA B  1 224 ? -14.315 -21.067 5.275   1.00 8.05  ? 224 ALA B CA  1 
ATOM   4018  C  C   . ALA B  1 224 ? -13.668 -20.022 6.256   1.00 9.34  ? 224 ALA B C   1 
ATOM   4019  O  O   . ALA B  1 224 ? -14.314 -19.439 7.137   1.00 9.68  ? 224 ALA B O   1 
ATOM   4020  C  CB  . ALA B  1 224 ? -13.931 -22.572 5.722   1.00 11.27 ? 224 ALA B CB  1 
ATOM   4021  N  N   . LEU B  1 225 ? -12.325 -19.832 6.090   1.00 8.58  ? 225 LEU B N   1 
ATOM   4022  C  CA  . LEU B  1 225 ? -11.637 -18.850 6.955   1.00 7.39  ? 225 LEU B CA  1 
ATOM   4023  C  C   . LEU B  1 225 ? -12.236 -17.481 6.754   1.00 7.81  ? 225 LEU B C   1 
ATOM   4024  O  O   . LEU B  1 225 ? -12.356 -16.765 7.764   1.00 9.07  ? 225 LEU B O   1 
ATOM   4025  C  CB  . LEU B  1 225 ? -10.117 -18.856 6.544   1.00 6.70  ? 225 LEU B CB  1 
ATOM   4026  C  CG  . LEU B  1 225 ? -9.233  -17.910 7.341   1.00 7.58  ? 225 LEU B CG  1 
ATOM   4027  C  CD1 . LEU B  1 225 ? -9.240  -18.252 8.833   1.00 8.56  ? 225 LEU B CD1 1 
ATOM   4028  C  CD2 . LEU B  1 225 ? -7.816  -17.874 6.683   1.00 6.53  ? 225 LEU B CD2 1 
ATOM   4029  N  N   . GLU B  1 226 ? -12.569 -17.063 5.526   1.00 6.90  ? 226 GLU B N   1 
ATOM   4030  C  CA  . GLU B  1 226 ? -13.084 -15.719 5.271   1.00 6.77  ? 226 GLU B CA  1 
ATOM   4031  C  C   . GLU B  1 226 ? -14.481 -15.460 5.785   1.00 8.05  ? 226 GLU B C   1 
ATOM   4032  O  O   . GLU B  1 226 ? -14.905 -14.298 5.890   1.00 8.88  ? 226 GLU B O   1 
ATOM   4033  C  CB  . GLU B  1 226 ? -13.074 -15.469 3.738   1.00 7.43  ? 226 GLU B CB  1 
ATOM   4034  C  CG  . GLU B  1 226 ? -11.672 -15.289 3.147   1.00 7.06  ? 226 GLU B CG  1 
ATOM   4035  C  CD  . GLU B  1 226 ? -11.644 -15.517 1.649   1.00 8.02  ? 226 GLU B CD  1 
ATOM   4036  O  OE1 . GLU B  1 226 ? -12.633 -16.063 1.118   1.00 8.40  ? 226 GLU B OE1 1 
ATOM   4037  O  OE2 . GLU B  1 226 ? -10.639 -15.153 0.999   1.00 7.86  ? 226 GLU B OE2 1 
ATOM   4038  N  N   . THR B  1 227 ? -15.198 -16.561 6.055   1.00 8.06  ? 227 THR B N   1 
ATOM   4039  C  CA  . THR B  1 227 ? -16.662 -16.430 6.389   1.00 8.47  ? 227 THR B CA  1 
ATOM   4040  C  C   . THR B  1 227 ? -17.016 -16.856 7.807   1.00 8.52  ? 227 THR B C   1 
ATOM   4041  O  O   . THR B  1 227 ? -18.181 -16.671 8.258   1.00 12.01 ? 227 THR B O   1 
ATOM   4042  C  CB  . THR B  1 227 ? -17.535 -17.216 5.414   1.00 7.15  ? 227 THR B CB  1 
ATOM   4043  O  OG1 . THR B  1 227 ? -17.116 -18.602 5.380   1.00 8.92  ? 227 THR B OG1 1 
ATOM   4044  C  CG2 . THR B  1 227 ? -17.372 -16.588 3.985   1.00 10.67 ? 227 THR B CG2 1 
ATOM   4045  N  N   . ALA B  1 228 ? -16.068 -17.451 8.535   1.00 7.98  ? 228 ALA B N   1 
ATOM   4046  C  CA  . ALA B  1 228 ? -16.441 -18.121 9.836   1.00 8.59  ? 228 ALA B CA  1 
ATOM   4047  C  C   . ALA B  1 228 ? -16.553 -17.193 10.998  1.00 9.37  ? 228 ALA B C   1 
ATOM   4048  O  O   . ALA B  1 228 ? -17.278 -17.454 11.924  1.00 10.56 ? 228 ALA B O   1 
ATOM   4049  C  CB  . ALA B  1 228 ? -15.386 -19.210 10.197  1.00 9.94  ? 228 ALA B CB  1 
ATOM   4050  N  N   . LEU B  1 229 ? -15.806 -16.085 10.957  1.00 6.73  ? 229 LEU B N   1 
ATOM   4051  C  CA  . LEU B  1 229 ? -15.601 -15.312 12.172  1.00 8.05  ? 229 LEU B CA  1 
ATOM   4052  C  C   . LEU B  1 229 ? -16.142 -13.895 12.189  1.00 6.33  ? 229 LEU B C   1 
ATOM   4053  O  O   . LEU B  1 229 ? -16.264 -13.241 11.125  1.00 5.97  ? 229 LEU B O   1 
ATOM   4054  C  CB  . LEU B  1 229 ? -14.109 -15.235 12.508  1.00 8.47  ? 229 LEU B CB  1 
ATOM   4055  C  CG  . LEU B  1 229 ? -13.329 -16.548 12.366  1.00 8.73  ? 229 LEU B CG  1 
ATOM   4056  C  CD1 . LEU B  1 229 ? -11.803 -16.270 12.726  1.00 9.85  ? 229 LEU B CD1 1 
ATOM   4057  C  CD2 . LEU B  1 229 ? -13.898 -17.531 13.360  1.00 10.40 ? 229 LEU B CD2 1 
ATOM   4058  N  N   . TYR B  1 230 ? -16.438 -13.388 13.375  1.00 7.33  ? 230 TYR B N   1 
ATOM   4059  C  CA  . TYR B  1 230 ? -16.847 -12.027 13.602  1.00 7.45  ? 230 TYR B CA  1 
ATOM   4060  C  C   . TYR B  1 230 ? -15.912 -11.308 14.546  1.00 8.67  ? 230 TYR B C   1 
ATOM   4061  O  O   . TYR B  1 230 ? -15.282 -11.944 15.402  1.00 8.00  ? 230 TYR B O   1 
ATOM   4062  C  CB  . TYR B  1 230 ? -18.302 -12.049 14.233  1.00 8.42  ? 230 TYR B CB  1 
ATOM   4063  C  CG  . TYR B  1 230 ? -19.350 -12.408 13.223  1.00 10.82 ? 230 TYR B CG  1 
ATOM   4064  C  CD1 . TYR B  1 230 ? -19.565 -13.769 12.877  1.00 12.41 ? 230 TYR B CD1 1 
ATOM   4065  C  CD2 . TYR B  1 230 ? -20.089 -11.382 12.579  1.00 11.63 ? 230 TYR B CD2 1 
ATOM   4066  C  CE1 . TYR B  1 230 ? -20.476 -14.132 11.848  1.00 15.53 ? 230 TYR B CE1 1 
ATOM   4067  C  CE2 . TYR B  1 230 ? -21.006 -11.736 11.524  1.00 12.45 ? 230 TYR B CE2 1 
ATOM   4068  C  CZ  . TYR B  1 230 ? -21.132 -13.100 11.227  1.00 13.26 ? 230 TYR B CZ  1 
ATOM   4069  O  OH  . TYR B  1 230 ? -22.078 -13.439 10.227  1.00 18.76 ? 230 TYR B OH  1 
ATOM   4070  N  N   . CYS B  1 231 ? -15.777 -9.993  14.335  1.00 8.98  ? 231 CYS B N   1 
ATOM   4071  C  CA  . CYS B  1 231 ? -14.942 -9.205  15.299  1.00 9.63  ? 231 CYS B CA  1 
ATOM   4072  C  C   . CYS B  1 231 ? -15.588 -8.902  16.599  1.00 9.24  ? 231 CYS B C   1 
ATOM   4073  O  O   . CYS B  1 231 ? -14.896 -8.451  17.508  1.00 11.72 ? 231 CYS B O   1 
ATOM   4074  C  CB  . CYS B  1 231 ? -14.638 -7.801  14.718  1.00 10.17 ? 231 CYS B CB  1 
ATOM   4075  S  SG  . CYS B  1 231 ? -13.670 -7.958  13.104  1.00 9.98  ? 231 CYS B SG  1 
ATOM   4076  N  N   . THR B  1 232 ? -16.914 -9.043  16.674  1.00 8.11  ? 232 THR B N   1 
ATOM   4077  C  CA  . THR B  1 232 ? -17.686 -8.532  17.841  1.00 9.66  ? 232 THR B CA  1 
ATOM   4078  C  C   . THR B  1 232 ? -18.063 -9.686  18.765  1.00 9.08  ? 232 THR B C   1 
ATOM   4079  O  O   . THR B  1 232 ? -18.139 -10.853 18.389  1.00 8.52  ? 232 THR B O   1 
ATOM   4080  C  CB  . THR B  1 232 ? -18.926 -7.856  17.231  1.00 10.67 ? 232 THR B CB  1 
ATOM   4081  O  OG1 . THR B  1 232 ? -19.391 -8.646  16.118  1.00 10.56 ? 232 THR B OG1 1 
ATOM   4082  C  CG2 . THR B  1 232 ? -18.410 -6.484  16.695  1.00 12.75 ? 232 THR B CG2 1 
ATOM   4083  N  N   . HIS B  1 233 ? -18.450 -9.301  19.987  1.00 11.48 ? 233 HIS B N   1 
ATOM   4084  C  CA  . HIS B  1 233 ? -18.929 -10.223 20.961  1.00 13.09 ? 233 HIS B CA  1 
ATOM   4085  C  C   . HIS B  1 233 ? -20.338 -10.689 20.597  1.00 13.96 ? 233 HIS B C   1 
ATOM   4086  O  O   . HIS B  1 233 ? -21.063 -9.994  19.894  1.00 13.12 ? 233 HIS B O   1 
ATOM   4087  C  CB  . HIS B  1 233 ? -19.071 -9.486  22.345  1.00 12.74 ? 233 HIS B CB  1 
ATOM   4088  C  CG  . HIS B  1 233 ? -17.765 -9.126  23.018  1.00 18.25 ? 233 HIS B CG  1 
ATOM   4089  N  ND1 . HIS B  1 233 ? -16.884 -10.043 23.585  1.00 22.63 ? 233 HIS B ND1 1 
ATOM   4090  C  CD2 . HIS B  1 233 ? -17.242 -7.911  23.272  1.00 17.95 ? 233 HIS B CD2 1 
ATOM   4091  C  CE1 . HIS B  1 233 ? -15.861 -9.387  24.137  1.00 16.78 ? 233 HIS B CE1 1 
ATOM   4092  N  NE2 . HIS B  1 233 ? -16.050 -8.103  23.954  1.00 21.54 ? 233 HIS B NE2 1 
ATOM   4093  N  N   A MET B  1 234 ? -20.675 -11.872 21.140  0.50 16.22 ? 234 MET B N   1 
ATOM   4094  N  N   B MET B  1 234 ? -20.720 -11.842 21.140  0.50 13.48 ? 234 MET B N   1 
ATOM   4095  C  CA  A MET B  1 234 ? -22.074 -12.306 21.202  0.50 19.18 ? 234 MET B CA  1 
ATOM   4096  C  CA  B MET B  1 234 ? -22.017 -12.432 20.772  0.50 13.46 ? 234 MET B CA  1 
ATOM   4097  C  C   A MET B  1 234 ? -22.728 -11.201 22.014  0.50 18.21 ? 234 MET B C   1 
ATOM   4098  C  C   B MET B  1 234 ? -23.194 -11.543 21.223  0.50 13.66 ? 234 MET B C   1 
ATOM   4099  O  O   A MET B  1 234 ? -22.129 -10.691 22.969  0.50 19.01 ? 234 MET B O   1 
ATOM   4100  O  O   B MET B  1 234 ? -24.280 -11.752 20.783  0.50 13.68 ? 234 MET B O   1 
ATOM   4101  C  CB  A MET B  1 234 ? -22.217 -13.584 21.983  0.50 19.51 ? 234 MET B CB  1 
ATOM   4102  C  CB  B MET B  1 234 ? -22.089 -13.815 21.379  0.50 12.44 ? 234 MET B CB  1 
ATOM   4103  C  CG  A MET B  1 234 ? -21.832 -14.784 21.239  0.50 20.24 ? 234 MET B CG  1 
ATOM   4104  C  CG  B MET B  1 234 ? -22.094 -13.771 22.925  0.50 10.68 ? 234 MET B CG  1 
ATOM   4105  S  SD  A MET B  1 234 ? -22.340 -16.283 22.066  0.50 25.20 ? 234 MET B SD  1 
ATOM   4106  S  SD  B MET B  1 234 ? -21.909 -15.375 23.694  0.50 19.61 ? 234 MET B SD  1 
ATOM   4107  C  CE  A MET B  1 234 ? -22.458 -17.249 20.512  0.50 22.74 ? 234 MET B CE  1 
ATOM   4108  C  CE  B MET B  1 234 ? -20.141 -15.568 23.802  0.50 22.93 ? 234 MET B CE  1 
ATOM   4109  N  N   A ASP B  1 235 ? -23.930 -10.813 21.643  0.50 18.77 ? 235 ASP B N   1 
ATOM   4110  N  N   B ASP B  1 235 ? -22.907 -10.549 22.050  0.50 13.82 ? 235 ASP B N   1 
ATOM   4111  C  CA  A ASP B  1 235 ? -24.564 -9.577  22.234  0.50 17.35 ? 235 ASP B CA  1 
ATOM   4112  C  CA  B ASP B  1 235 ? -23.959 -9.648  22.507  0.50 14.91 ? 235 ASP B CA  1 
ATOM   4113  C  C   A ASP B  1 235 ? -24.077 -8.180  21.786  0.50 16.46 ? 235 ASP B C   1 
ATOM   4114  C  C   B ASP B  1 235 ? -24.078 -8.367  21.773  0.50 14.92 ? 235 ASP B C   1 
ATOM   4115  O  O   A ASP B  1 235 ? -24.524 -7.134  22.327  0.50 13.50 ? 235 ASP B O   1 
ATOM   4116  O  O   B ASP B  1 235 ? -24.990 -7.625  22.123  0.50 15.45 ? 235 ASP B O   1 
ATOM   4117  C  CB  A ASP B  1 235 ? -24.711 -9.663  23.787  0.50 16.30 ? 235 ASP B CB  1 
ATOM   4118  C  CB  B ASP B  1 235 ? -24.027 -9.415  24.066  0.50 16.11 ? 235 ASP B CB  1 
ATOM   4119  C  CG  A ASP B  1 235 ? -23.436 -9.255  24.585  0.50 20.44 ? 235 ASP B CG  1 
ATOM   4120  C  CG  B ASP B  1 235 ? -22.937 -8.397  24.636  0.50 18.84 ? 235 ASP B CG  1 
ATOM   4121  O  OD1 A ASP B  1 235 ? -22.365 -8.874  24.021  0.50 17.26 ? 235 ASP B OD1 1 
ATOM   4122  O  OD1 B ASP B  1 235 ? -23.165 -7.862  25.766  0.50 19.28 ? 235 ASP B OD1 1 
ATOM   4123  O  OD2 A ASP B  1 235 ? -23.521 -9.341  25.835  0.50 26.60 ? 235 ASP B OD2 1 
ATOM   4124  O  OD2 B ASP B  1 235 ? -21.834 -8.155  24.069  0.50 17.33 ? 235 ASP B OD2 1 
ATOM   4125  N  N   . ASP B  1 236 ? -23.191 -8.064  20.817  1.00 14.89 ? 236 ASP B N   1 
ATOM   4126  C  CA  . ASP B  1 236 ? -22.973 -6.700  20.275  1.00 16.42 ? 236 ASP B CA  1 
ATOM   4127  C  C   . ASP B  1 236 ? -24.183 -6.370  19.382  1.00 17.72 ? 236 ASP B C   1 
ATOM   4128  O  O   . ASP B  1 236 ? -24.523 -7.205  18.549  1.00 16.58 ? 236 ASP B O   1 
ATOM   4129  C  CB  . ASP B  1 236 ? -21.641 -6.647  19.410  1.00 15.18 ? 236 ASP B CB  1 
ATOM   4130  C  CG  . ASP B  1 236 ? -21.157 -5.232  19.159  1.00 17.30 ? 236 ASP B CG  1 
ATOM   4131  O  OD1 . ASP B  1 236 ? -21.957 -4.404  18.686  1.00 19.19 ? 236 ASP B OD1 1 
ATOM   4132  O  OD2 . ASP B  1 236 ? -19.973 -4.956  19.427  1.00 17.88 ? 236 ASP B OD2 1 
ATOM   4133  N  N   . PRO B  1 237 ? -24.795 -5.165  19.570  1.00 18.49 ? 237 PRO B N   1 
ATOM   4134  C  CA  . PRO B  1 237 ? -25.894 -4.737  18.694  1.00 18.39 ? 237 PRO B CA  1 
ATOM   4135  C  C   . PRO B  1 237 ? -25.472 -4.452  17.206  1.00 20.84 ? 237 PRO B C   1 
ATOM   4136  O  O   . PRO B  1 237 ? -26.349 -4.377  16.297  1.00 22.02 ? 237 PRO B O   1 
ATOM   4137  C  CB  . PRO B  1 237 ? -26.387 -3.471  19.390  1.00 18.77 ? 237 PRO B CB  1 
ATOM   4138  C  CG  . PRO B  1 237 ? -25.255 -2.965  20.073  1.00 17.74 ? 237 PRO B CG  1 
ATOM   4139  C  CD  . PRO B  1 237 ? -24.527 -4.154  20.617  1.00 16.41 ? 237 PRO B CD  1 
ATOM   4140  N  N   . SER B  1 238 ? -24.171 -4.278  16.934  1.00 19.51 ? 238 SER B N   1 
ATOM   4141  C  CA  . SER B  1 238 ? -23.762 -4.010  15.512  1.00 18.96 ? 238 SER B CA  1 
ATOM   4142  C  C   . SER B  1 238 ? -22.641 -5.026  15.119  1.00 16.64 ? 238 SER B C   1 
ATOM   4143  O  O   . SER B  1 238 ? -21.499 -4.659  15.164  1.00 16.91 ? 238 SER B O   1 
ATOM   4144  C  CB  . SER B  1 238 ? -23.194 -2.609  15.360  1.00 22.11 ? 238 SER B CB  1 
ATOM   4145  O  OG  . SER B  1 238 ? -23.952 -1.632  16.079  1.00 27.48 ? 238 SER B OG  1 
ATOM   4146  N  N   . PRO B  1 239 ? -23.027 -6.245  14.760  1.00 15.45 ? 239 PRO B N   1 
ATOM   4147  C  CA  . PRO B  1 239 ? -21.990 -7.266  14.501  1.00 14.29 ? 239 PRO B CA  1 
ATOM   4148  C  C   . PRO B  1 239 ? -21.136 -6.831  13.369  1.00 15.51 ? 239 PRO B C   1 
ATOM   4149  O  O   . PRO B  1 239 ? -21.588 -6.112  12.435  1.00 18.83 ? 239 PRO B O   1 
ATOM   4150  C  CB  . PRO B  1 239 ? -22.767 -8.540  14.103  1.00 12.72 ? 239 PRO B CB  1 
ATOM   4151  C  CG  . PRO B  1 239 ? -24.252 -8.078  14.086  1.00 19.40 ? 239 PRO B CG  1 
ATOM   4152  C  CD  . PRO B  1 239 ? -24.393 -6.772  14.593  1.00 17.62 ? 239 PRO B CD  1 
ATOM   4153  N  N   . ARG B  1 240 ? -19.889 -7.351  13.304  1.00 12.79 ? 240 ARG B N   1 
ATOM   4154  C  CA  . ARG B  1 240 ? -18.962 -6.972  12.195  1.00 11.56 ? 240 ARG B CA  1 
ATOM   4155  C  C   . ARG B  1 240 ? -18.242 -8.261  11.834  1.00 11.05 ? 240 ARG B C   1 
ATOM   4156  O  O   . ARG B  1 240 ? -17.643 -8.889  12.690  1.00 10.37 ? 240 ARG B O   1 
ATOM   4157  C  CB  . ARG B  1 240 ? -17.941 -5.926  12.665  1.00 13.30 ? 240 ARG B CB  1 
ATOM   4158  C  CG  . ARG B  1 240 ? -18.563 -4.527  12.890  1.00 15.04 ? 240 ARG B CG  1 
ATOM   4159  C  CD  . ARG B  1 240 ? -17.489 -3.537  13.384  1.00 17.83 ? 240 ARG B CD  1 
ATOM   4160  N  NE  . ARG B  1 240 ? -17.121 -3.736  14.816  1.00 16.56 ? 240 ARG B NE  1 
ATOM   4161  C  CZ  . ARG B  1 240 ? -15.918 -4.178  15.218  1.00 19.42 ? 240 ARG B CZ  1 
ATOM   4162  N  NH1 . ARG B  1 240 ? -14.980 -4.476  14.353  1.00 15.28 ? 240 ARG B NH1 1 
ATOM   4163  N  NH2 . ARG B  1 240 ? -15.658 -4.334  16.503  1.00 21.36 ? 240 ARG B NH2 1 
ATOM   4164  N  N   . GLU B  1 241 ? -18.292 -8.614  10.575  1.00 10.38 ? 241 GLU B N   1 
ATOM   4165  C  CA  . GLU B  1 241 ? -17.609 -9.831  10.054  1.00 9.67  ? 241 GLU B CA  1 
ATOM   4166  C  C   . GLU B  1 241 ? -16.133 -9.582  10.066  1.00 7.56  ? 241 GLU B C   1 
ATOM   4167  O  O   . GLU B  1 241 ? -15.628 -8.515  9.689   1.00 9.45  ? 241 GLU B O   1 
ATOM   4168  C  CB  . GLU B  1 241 ? -18.030 -10.073 8.621   1.00 11.84 ? 241 GLU B CB  1 
ATOM   4169  C  CG  . GLU B  1 241 ? -19.479 -10.444 8.597   1.00 14.46 ? 241 GLU B CG  1 
ATOM   4170  C  CD  . GLU B  1 241 ? -20.082 -10.381 7.176   1.00 22.90 ? 241 GLU B CD  1 
ATOM   4171  O  OE1 . GLU B  1 241 ? -21.315 -10.582 7.235   1.00 27.24 ? 241 GLU B OE1 1 
ATOM   4172  O  OE2 . GLU B  1 241 ? -19.326 -10.079 6.158   1.00 22.35 ? 241 GLU B OE2 1 
ATOM   4173  N  N   . MET B  1 242 ? -15.393 -10.661 10.403  1.00 7.61  ? 242 MET B N   1 
ATOM   4174  C  CA  . MET B  1 242 ? -13.935 -10.598 10.448  1.00 7.17  ? 242 MET B CA  1 
ATOM   4175  C  C   . MET B  1 242 ? -13.368 -10.907 9.049   1.00 5.83  ? 242 MET B C   1 
ATOM   4176  O  O   . MET B  1 242 ? -13.110 -12.048 8.698   1.00 6.09  ? 242 MET B O   1 
ATOM   4177  C  CB  . MET B  1 242 ? -13.337 -11.541 11.490  1.00 6.09  ? 242 MET B CB  1 
ATOM   4178  C  CG  . MET B  1 242 ? -11.828 -11.292 11.605  1.00 6.01  ? 242 MET B CG  1 
ATOM   4179  S  SD  . MET B  1 242 ? -11.109 -12.399 12.891  1.00 7.48  ? 242 MET B SD  1 
ATOM   4180  C  CE  . MET B  1 242 ? -11.995 -11.833 14.413  1.00 8.56  ? 242 MET B CE  1 
ATOM   4181  N  N   . ILE B  1 243 ? -13.157 -9.789  8.311   1.00 6.37  ? 243 ILE B N   1 
ATOM   4182  C  CA  . ILE B  1 243 ? -12.712 -9.850  6.914   1.00 5.26  ? 243 ILE B CA  1 
ATOM   4183  C  C   . ILE B  1 243 ? -11.670 -8.698  6.716   1.00 5.49  ? 243 ILE B C   1 
ATOM   4184  O  O   . ILE B  1 243 ? -11.689 -7.677  7.454   1.00 6.37  ? 243 ILE B O   1 
ATOM   4185  C  CB  . ILE B  1 243 ? -13.847 -9.644  5.847   1.00 7.59  ? 243 ILE B CB  1 
ATOM   4186  C  CG1 . ILE B  1 243 ? -14.653 -8.395  6.132   1.00 7.27  ? 243 ILE B CG1 1 
ATOM   4187  C  CG2 . ILE B  1 243 ? -14.658 -10.991 5.768   1.00 8.98  ? 243 ILE B CG2 1 
ATOM   4188  C  CD1 . ILE B  1 243 ? -15.711 -8.172  5.006   1.00 9.32  ? 243 ILE B CD1 1 
ATOM   4189  N  N   . ASN B  1 244 ? -10.839 -8.855  5.687   1.00 5.17  ? 244 ASN B N   1 
ATOM   4190  C  CA  . ASN B  1 244 ? -9.829  -7.791  5.327   1.00 6.17  ? 244 ASN B CA  1 
ATOM   4191  C  C   . ASN B  1 244 ? -9.024  -7.346  6.554   1.00 5.64  ? 244 ASN B C   1 
ATOM   4192  O  O   . ASN B  1 244 ? -8.752  -6.140  6.792   1.00 6.14  ? 244 ASN B O   1 
ATOM   4193  C  CB  . ASN B  1 244 ? -10.522 -6.602  4.660   1.00 6.36  ? 244 ASN B CB  1 
ATOM   4194  C  CG  . ASN B  1 244 ? -11.340 -7.059  3.461   1.00 6.95  ? 244 ASN B CG  1 
ATOM   4195  O  OD1 . ASN B  1 244 ? -10.885 -7.883  2.711   1.00 8.10  ? 244 ASN B OD1 1 
ATOM   4196  N  ND2 . ASN B  1 244 ? -12.601 -6.493  3.320   1.00 8.77  ? 244 ASN B ND2 1 
ATOM   4197  N  N   . ASN B  1 245 ? -8.611  -8.346  7.353   1.00 4.88  ? 245 ASN B N   1 
ATOM   4198  C  CA  . ASN B  1 245 ? -7.844  -8.049  8.584   1.00 4.50  ? 245 ASN B CA  1 
ATOM   4199  C  C   . ASN B  1 245 ? -6.345  -8.062  8.331   1.00 5.15  ? 245 ASN B C   1 
ATOM   4200  O  O   . ASN B  1 245 ? -5.603  -8.797  9.007   1.00 5.96  ? 245 ASN B O   1 
ATOM   4201  C  CB  . ASN B  1 245 ? -8.239  -9.007  9.731   1.00 5.51  ? 245 ASN B CB  1 
ATOM   4202  C  CG  . ASN B  1 245 ? -7.965  -10.466 9.417   1.00 6.12  ? 245 ASN B CG  1 
ATOM   4203  O  OD1 . ASN B  1 245 ? -7.840  -10.892 8.278   1.00 6.85  ? 245 ASN B OD1 1 
ATOM   4204  N  ND2 . ASN B  1 245 ? -7.953  -11.297 10.494  1.00 7.01  ? 245 ASN B ND2 1 
ATOM   4205  N  N   . PHE B  1 246 ? -5.919  -7.247  7.400   1.00 5.09  ? 246 PHE B N   1 
ATOM   4206  C  CA  . PHE B  1 246 ? -4.497  -7.123  7.031   1.00 4.77  ? 246 PHE B CA  1 
ATOM   4207  C  C   . PHE B  1 246 ? -4.246  -5.619  6.893   1.00 5.76  ? 246 PHE B C   1 
ATOM   4208  O  O   . PHE B  1 246 ? -5.146  -4.829  6.542   1.00 5.63  ? 246 PHE B O   1 
ATOM   4209  C  CB  . PHE B  1 246 ? -4.179  -7.846  5.697   1.00 6.18  ? 246 PHE B CB  1 
ATOM   4210  C  CG  . PHE B  1 246 ? -4.945  -7.313  4.549   1.00 5.50  ? 246 PHE B CG  1 
ATOM   4211  C  CD1 . PHE B  1 246 ? -4.302  -6.375  3.657   1.00 5.75  ? 246 PHE B CD1 1 
ATOM   4212  C  CD2 . PHE B  1 246 ? -6.207  -7.768  4.212   1.00 6.61  ? 246 PHE B CD2 1 
ATOM   4213  C  CE1 . PHE B  1 246 ? -4.979  -5.863  2.499   1.00 6.42  ? 246 PHE B CE1 1 
ATOM   4214  C  CE2 . PHE B  1 246 ? -6.883  -7.255  3.057   1.00 6.94  ? 246 PHE B CE2 1 
ATOM   4215  C  CZ  . PHE B  1 246 ? -6.220  -6.289  2.231   1.00 6.26  ? 246 PHE B CZ  1 
ATOM   4216  N  N   . ARG B  1 247 ? -2.991  -5.199  7.189   1.00 4.35  ? 247 ARG B N   1 
ATOM   4217  C  CA  . ARG B  1 247 ? -2.603  -3.818  7.039   1.00 4.52  ? 247 ARG B CA  1 
ATOM   4218  C  C   . ARG B  1 247 ? -2.106  -3.587  5.589   1.00 5.13  ? 247 ARG B C   1 
ATOM   4219  O  O   . ARG B  1 247 ? -1.458  -4.460  5.031   1.00 4.26  ? 247 ARG B O   1 
ATOM   4220  C  CB  . ARG B  1 247 ? -1.476  -3.456  8.054   1.00 4.32  ? 247 ARG B CB  1 
ATOM   4221  C  CG  . ARG B  1 247 ? -1.307  -1.902  8.267   1.00 4.90  ? 247 ARG B CG  1 
ATOM   4222  C  CD  . ARG B  1 247 ? -0.039  -1.749  9.192   1.00 5.83  ? 247 ARG B CD  1 
ATOM   4223  N  NE  . ARG B  1 247 ? 0.015   -0.393  9.697   1.00 5.50  ? 247 ARG B NE  1 
ATOM   4224  C  CZ  . ARG B  1 247 ? 1.013   0.079   10.422  1.00 4.00  ? 247 ARG B CZ  1 
ATOM   4225  N  NH1 . ARG B  1 247 ? 2.044   -0.687  10.722  1.00 5.27  ? 247 ARG B NH1 1 
ATOM   4226  N  NH2 . ARG B  1 247 ? 0.976   1.335   10.842  1.00 4.89  ? 247 ARG B NH2 1 
ATOM   4227  N  N   . GLN B  1 248 ? -2.344  -2.382  5.040   1.00 5.23  ? 248 GLN B N   1 
ATOM   4228  C  CA  . GLN B  1 248 ? -1.674  -1.987  3.779   1.00 5.01  ? 248 GLN B CA  1 
ATOM   4229  C  C   . GLN B  1 248 ? -0.162  -2.003  3.941   1.00 5.16  ? 248 GLN B C   1 
ATOM   4230  O  O   . GLN B  1 248 ? 0.350   -1.714  5.053   1.00 5.65  ? 248 GLN B O   1 
ATOM   4231  C  CB  . GLN B  1 248 ? -2.085  -0.560  3.366   1.00 4.28  ? 248 GLN B CB  1 
ATOM   4232  C  CG  . GLN B  1 248 ? -3.637  -0.415  3.038   1.00 5.27  ? 248 GLN B CG  1 
ATOM   4233  C  CD  . GLN B  1 248 ? -4.023  -1.341  1.901   1.00 6.40  ? 248 GLN B CD  1 
ATOM   4234  O  OE1 . GLN B  1 248 ? -4.506  -2.470  2.091   1.00 7.02  ? 248 GLN B OE1 1 
ATOM   4235  N  NE2 . GLN B  1 248 ? -3.832  -0.890  0.653   1.00 6.51  ? 248 GLN B NE2 1 
ATOM   4236  N  N   . VAL B  1 249 ? 0.623   -2.225  2.884   1.00 4.78  ? 249 VAL B N   1 
ATOM   4237  C  CA  . VAL B  1 249 ? 2.075   -2.132  2.978   1.00 4.16  ? 249 VAL B CA  1 
ATOM   4238  C  C   . VAL B  1 249 ? 2.539   -0.685  3.218   1.00 4.77  ? 249 VAL B C   1 
ATOM   4239  O  O   . VAL B  1 249 ? 1.830   0.296   2.874   1.00 4.97  ? 249 VAL B O   1 
ATOM   4240  C  CB  . VAL B  1 249 ? 2.756   -2.663  1.719   1.00 5.91  ? 249 VAL B CB  1 
ATOM   4241  C  CG1 . VAL B  1 249 ? 2.498   -4.204  1.641   1.00 9.98  ? 249 VAL B CG1 1 
ATOM   4242  C  CG2 . VAL B  1 249 ? 2.336   -1.947  0.440   1.00 6.61  ? 249 VAL B CG2 1 
ATOM   4243  N  N   . GLN B  1 250 ? 3.673   -0.618  3.895   1.00 4.45  ? 250 GLN B N   1 
ATOM   4244  C  CA  . GLN B  1 250 ? 4.187   0.682   4.394   1.00 4.43  ? 250 GLN B CA  1 
ATOM   4245  C  C   . GLN B  1 250 ? 5.310   1.139   3.417   1.00 7.26  ? 250 GLN B C   1 
ATOM   4246  O  O   . GLN B  1 250 ? 5.993   0.256   2.827   1.00 7.87  ? 250 GLN B O   1 
ATOM   4247  C  CB  . GLN B  1 250 ? 4.829   0.461   5.811   1.00 5.54  ? 250 GLN B CB  1 
ATOM   4248  C  CG  . GLN B  1 250 ? 3.764   -0.182  6.748   1.00 5.06  ? 250 GLN B CG  1 
ATOM   4249  C  CD  . GLN B  1 250 ? 2.634   0.746   7.103   1.00 6.27  ? 250 GLN B CD  1 
ATOM   4250  O  OE1 . GLN B  1 250 ? 2.879   1.849   7.724   1.00 6.27  ? 250 GLN B OE1 1 
ATOM   4251  N  NE2 . GLN B  1 250 ? 1.377   0.406   6.737   1.00 4.58  ? 250 GLN B NE2 1 
ATOM   4252  N  N   . LYS B  1 251 ? 5.559   2.439   3.527   1.00 5.79  ? 251 LYS B N   1 
ATOM   4253  C  CA  . LYS B  1 251 ? 6.793   2.945   2.890   1.00 6.90  ? 251 LYS B CA  1 
ATOM   4254  C  C   . LYS B  1 251 ? 8.012   2.242   3.458   1.00 7.85  ? 251 LYS B C   1 
ATOM   4255  O  O   . LYS B  1 251 ? 8.089   1.949   4.652   1.00 7.17  ? 251 LYS B O   1 
ATOM   4256  C  CB  . LYS B  1 251 ? 7.008   4.479   3.152   1.00 7.85  ? 251 LYS B CB  1 
ATOM   4257  C  CG  . LYS B  1 251 ? 5.946   5.474   2.462   1.00 9.58  ? 251 LYS B CG  1 
ATOM   4258  C  CD  . LYS B  1 251 ? 6.265   5.667   0.981   1.00 10.62 ? 251 LYS B CD  1 
ATOM   4259  C  CE  . LYS B  1 251 ? 5.459   6.755   0.255   1.00 6.77  ? 251 LYS B CE  1 
ATOM   4260  N  NZ  . LYS B  1 251 ? 3.990   6.481   0.294   1.00 4.35  ? 251 LYS B NZ  1 
ATOM   4261  N  N   . PHE B  1 252 ? 9.079   2.117   2.629   1.00 9.02  ? 252 PHE B N   1 
ATOM   4262  C  CA  . PHE B  1 252 ? 10.281  1.383   3.094   1.00 9.80  ? 252 PHE B CA  1 
ATOM   4263  C  C   . PHE B  1 252 ? 11.343  1.928   2.227   1.00 15.15 ? 252 PHE B C   1 
ATOM   4264  O  O   . PHE B  1 252 ? 11.510  1.530   1.016   1.00 13.13 ? 252 PHE B O   1 
ATOM   4265  C  CB  . PHE B  1 252 ? 10.136  -0.083  2.800   1.00 13.82 ? 252 PHE B CB  1 
ATOM   4266  C  CG  . PHE B  1 252 ? 11.206  -0.919  3.349   1.00 12.16 ? 252 PHE B CG  1 
ATOM   4267  C  CD1 . PHE B  1 252 ? 11.156  -1.310  4.646   1.00 10.26 ? 252 PHE B CD1 1 
ATOM   4268  C  CD2 . PHE B  1 252 ? 12.252  -1.364  2.522   1.00 15.33 ? 252 PHE B CD2 1 
ATOM   4269  C  CE1 . PHE B  1 252 ? 12.167  -2.109  5.219   1.00 15.47 ? 252 PHE B CE1 1 
ATOM   4270  C  CE2 . PHE B  1 252 ? 13.243  -2.181  3.038   1.00 16.60 ? 252 PHE B CE2 1 
ATOM   4271  C  CZ  . PHE B  1 252 ? 13.202  -2.589  4.374   1.00 16.57 ? 252 PHE B CZ  1 
ATOM   4272  N  N   A ASP B  1 253 ? 12.083  2.866   2.804   0.50 15.96 ? 253 ASP B N   1 
ATOM   4273  N  N   B ASP B  1 253 ? 12.011  2.929   2.791   0.50 15.79 ? 253 ASP B N   1 
ATOM   4274  C  CA  A ASP B  1 253 ? 12.725  3.883   2.010   0.50 20.96 ? 253 ASP B CA  1 
ATOM   4275  C  CA  B ASP B  1 253 ? 12.760  3.916   2.043   0.50 20.18 ? 253 ASP B CA  1 
ATOM   4276  C  C   A ASP B  1 253 ? 14.246  3.952   1.834   0.50 23.17 ? 253 ASP B C   1 
ATOM   4277  C  C   B ASP B  1 253 ? 14.243  3.635   1.967   0.50 22.63 ? 253 ASP B C   1 
ATOM   4278  O  O   A ASP B  1 253 ? 14.725  3.748   0.718   0.50 24.04 ? 253 ASP B O   1 
ATOM   4279  O  O   B ASP B  1 253 ? 14.693  2.918   1.074   0.50 22.61 ? 253 ASP B O   1 
ATOM   4280  C  CB  A ASP B  1 253 ? 12.012  5.227   2.198   0.50 19.31 ? 253 ASP B CB  1 
ATOM   4281  C  CB  B ASP B  1 253 ? 12.527  5.312   2.629   0.50 18.84 ? 253 ASP B CB  1 
ATOM   4282  C  CG  A ASP B  1 253 ? 11.019  5.447   1.067   0.50 19.27 ? 253 ASP B CG  1 
ATOM   4283  C  CG  B ASP B  1 253 ? 12.764  5.362   4.125   0.50 18.13 ? 253 ASP B CG  1 
ATOM   4284  O  OD1 A ASP B  1 253 ? 9.891   5.867   1.255   0.50 12.59 ? 253 ASP B OD1 1 
ATOM   4285  O  OD1 B ASP B  1 253 ? 13.113  4.315   4.709   0.50 24.73 ? 253 ASP B OD1 1 
ATOM   4286  O  OD2 A ASP B  1 253 ? 11.405  5.106   -0.060  0.50 18.91 ? 253 ASP B OD2 1 
ATOM   4287  O  OD2 B ASP B  1 253 ? 12.601  6.450   4.718   0.50 26.21 ? 253 ASP B OD2 1 
ATOM   4288  N  N   . GLU B  1 254 ? 15.019  4.214   2.878   1.00 24.37 ? 254 GLU B N   1 
ATOM   4289  C  CA  . GLU B  1 254 ? 16.495  4.152   2.659   1.00 26.80 ? 254 GLU B CA  1 
ATOM   4290  C  C   . GLU B  1 254 ? 17.018  2.911   3.360   1.00 26.43 ? 254 GLU B C   1 
ATOM   4291  O  O   . GLU B  1 254 ? 17.836  3.033   4.244   1.00 28.63 ? 254 GLU B O   1 
ATOM   4292  C  CB  . GLU B  1 254 ? 17.230  5.428   3.132   1.00 29.00 ? 254 GLU B CB  1 
ATOM   4293  C  CG  . GLU B  1 254 ? 16.779  6.676   2.409   1.00 33.57 ? 254 GLU B CG  1 
ATOM   4294  C  CD  . GLU B  1 254 ? 17.922  7.527   1.856   0.01 46.11 ? 254 GLU B CD  1 
ATOM   4295  O  OE1 . GLU B  1 254 ? 17.787  8.779   1.907   0.01 48.81 ? 254 GLU B OE1 1 
ATOM   4296  O  OE2 . GLU B  1 254 ? 18.937  6.953   1.355   0.01 48.41 ? 254 GLU B OE2 1 
ATOM   4297  N  N   . ARG B  1 255 ? 16.417  1.768   3.048   1.00 26.12 ? 255 ARG B N   1 
ATOM   4298  C  CA  . ARG B  1 255 ? 16.550  0.504   3.779   1.00 25.13 ? 255 ARG B CA  1 
ATOM   4299  C  C   . ARG B  1 255 ? 16.513  -0.723  2.876   1.00 23.67 ? 255 ARG B C   1 
ATOM   4300  O  O   . ARG B  1 255 ? 16.053  -0.651  1.737   1.00 21.93 ? 255 ARG B O   1 
ATOM   4301  C  CB  . ARG B  1 255 ? 15.391  0.364   4.747   1.00 23.32 ? 255 ARG B CB  1 
ATOM   4302  C  CG  . ARG B  1 255 ? 15.609  1.062   6.033   1.00 28.44 ? 255 ARG B CG  1 
ATOM   4303  C  CD  . ARG B  1 255 ? 14.631  0.561   7.071   1.00 26.05 ? 255 ARG B CD  1 
ATOM   4304  N  NE  . ARG B  1 255 ? 13.371  1.286   6.994   1.00 32.47 ? 255 ARG B NE  1 
ATOM   4305  C  CZ  . ARG B  1 255 ? 12.207  0.816   7.432   1.00 27.93 ? 255 ARG B CZ  1 
ATOM   4306  N  NH1 . ARG B  1 255 ? 12.138  -0.388  7.984   1.00 22.96 ? 255 ARG B NH1 1 
ATOM   4307  N  NH2 . ARG B  1 255 ? 11.116  1.558   7.316   1.00 16.67 ? 255 ARG B NH2 1 
ATOM   4308  N  N   . LEU B  1 256 ? 16.992  -1.868  3.401   1.00 20.11 ? 256 LEU B N   1 
ATOM   4309  C  CA  . LEU B  1 256 ? 17.151  -3.063  2.701   1.00 16.01 ? 256 LEU B CA  1 
ATOM   4310  C  C   . LEU B  1 256 ? 16.450  -4.284  3.495   1.00 15.20 ? 256 LEU B C   1 
ATOM   4311  O  O   . LEU B  1 256 ? 16.314  -4.372  4.765   1.00 17.35 ? 256 LEU B O   1 
ATOM   4312  C  CB  . LEU B  1 256 ? 18.657  -3.286  2.393   1.00 20.87 ? 256 LEU B CB  1 
ATOM   4313  C  CG  . LEU B  1 256 ? 19.276  -2.328  1.349   1.00 24.59 ? 256 LEU B CG  1 
ATOM   4314  C  CD1 . LEU B  1 256 ? 19.346  -2.959  -0.073  1.00 26.97 ? 256 LEU B CD1 1 
ATOM   4315  C  CD2 . LEU B  1 256 ? 18.482  -1.062  1.139   1.00 29.77 ? 256 LEU B CD2 1 
ATOM   4316  N  N   . VAL B  1 257 ? 16.012  -5.160  2.646   1.00 12.61 ? 257 VAL B N   1 
ATOM   4317  C  CA  . VAL B  1 257 ? 15.554  -6.473  3.061   1.00 10.23 ? 257 VAL B CA  1 
ATOM   4318  C  C   . VAL B  1 257 ? 16.656  -7.403  2.687   1.00 9.21  ? 257 VAL B C   1 
ATOM   4319  O  O   . VAL B  1 257 ? 17.115  -7.312  1.584   1.00 11.39 ? 257 VAL B O   1 
ATOM   4320  C  CB  . VAL B  1 257 ? 14.278  -6.786  2.358   1.00 10.30 ? 257 VAL B CB  1 
ATOM   4321  C  CG1 . VAL B  1 257 ? 13.893  -8.227  2.543   1.00 9.65  ? 257 VAL B CG1 1 
ATOM   4322  C  CG2 . VAL B  1 257 ? 13.201  -5.816  2.830   1.00 11.39 ? 257 VAL B CG2 1 
ATOM   4323  N  N   . TYR B  1 258 ? 17.134  -8.253  3.579   1.00 7.95  ? 258 TYR B N   1 
ATOM   4324  C  CA  . TYR B  1 258 ? 18.200  -9.242  3.257   1.00 10.19 ? 258 TYR B CA  1 
ATOM   4325  C  C   . TYR B  1 258 ? 17.606  -10.556 2.865   1.00 10.16 ? 258 TYR B C   1 
ATOM   4326  O  O   . TYR B  1 258 ? 16.600  -11.031 3.444   1.00 12.28 ? 258 TYR B O   1 
ATOM   4327  C  CB  . TYR B  1 258 ? 19.112  -9.353  4.457   1.00 11.17 ? 258 TYR B CB  1 
ATOM   4328  C  CG  . TYR B  1 258 ? 19.637  -8.018  4.796   1.00 13.23 ? 258 TYR B CG  1 
ATOM   4329  C  CD1 . TYR B  1 258 ? 19.063  -7.237  5.774   1.00 14.83 ? 258 TYR B CD1 1 
ATOM   4330  C  CD2 . TYR B  1 258 ? 20.699  -7.493  4.097   1.00 13.94 ? 258 TYR B CD2 1 
ATOM   4331  C  CE1 . TYR B  1 258 ? 19.528  -5.926  6.056   1.00 18.97 ? 258 TYR B CE1 1 
ATOM   4332  C  CE2 . TYR B  1 258 ? 21.213  -6.195  4.406   1.00 15.63 ? 258 TYR B CE2 1 
ATOM   4333  C  CZ  . TYR B  1 258 ? 20.601  -5.428  5.317   1.00 18.47 ? 258 TYR B CZ  1 
ATOM   4334  O  OH  . TYR B  1 258 ? 21.116  -4.157  5.616   1.00 24.67 ? 258 TYR B OH  1 
ATOM   4335  N  N   . THR B  1 259 ? 18.141  -11.212 1.865   1.00 9.08  ? 259 THR B N   1 
ATOM   4336  C  CA  . THR B  1 259 ? 17.637  -12.504 1.436   1.00 8.54  ? 259 THR B CA  1 
ATOM   4337  C  C   . THR B  1 259 ? 18.698  -13.617 1.640   1.00 10.66 ? 259 THR B C   1 
ATOM   4338  O  O   . THR B  1 259 ? 19.930  -13.353 1.515   1.00 9.54  ? 259 THR B O   1 
ATOM   4339  C  CB  . THR B  1 259 ? 17.222  -12.521 -0.038  1.00 9.85  ? 259 THR B CB  1 
ATOM   4340  O  OG1 . THR B  1 259 ? 18.293  -12.037 -0.882  1.00 12.86 ? 259 THR B OG1 1 
ATOM   4341  C  CG2 . THR B  1 259 ? 16.092  -11.457 -0.227  1.00 10.93 ? 259 THR B CG2 1 
ATOM   4342  N  N   . SER B  1 260 ? 18.202  -14.835 1.867   1.00 9.27  ? 260 SER B N   1 
ATOM   4343  C  CA  . SER B  1 260 ? 19.132  -15.981 2.090   1.00 9.79  ? 260 SER B CA  1 
ATOM   4344  C  C   . SER B  1 260 ? 19.254  -16.667 0.793   1.00 10.90 ? 260 SER B C   1 
ATOM   4345  O  O   . SER B  1 260 ? 19.822  -17.770 0.767   1.00 14.30 ? 260 SER B O   1 
ATOM   4346  C  CB  . SER B  1 260 ? 18.569  -16.895 3.199   1.00 8.82  ? 260 SER B CB  1 
ATOM   4347  O  OG  . SER B  1 260 ? 17.369  -17.415 2.728   1.00 11.69 ? 260 SER B OG  1 
ATOM   4348  N  N   . PHE B  1 261 ? 18.781  -16.068 -0.317  1.00 11.37 ? 261 PHE B N   1 
ATOM   4349  C  CA  . PHE B  1 261 ? 18.873  -16.738 -1.669  1.00 11.30 ? 261 PHE B CA  1 
ATOM   4350  C  C   . PHE B  1 261 ? 19.317  -15.631 -2.639  1.00 16.77 ? 261 PHE B C   1 
ATOM   4351  O  O   . PHE B  1 261 ? 18.895  -14.490 -2.489  1.00 13.27 ? 261 PHE B O   1 
ATOM   4352  C  CB  . PHE B  1 261 ? 17.514  -17.345 -2.089  1.00 13.53 ? 261 PHE B CB  1 
ATOM   4353  C  CG  . PHE B  1 261 ? 16.372  -16.329 -2.065  1.00 12.39 ? 261 PHE B CG  1 
ATOM   4354  C  CD1 . PHE B  1 261 ? 15.988  -15.694 -3.236  1.00 15.81 ? 261 PHE B CD1 1 
ATOM   4355  C  CD2 . PHE B  1 261 ? 15.618  -16.036 -0.896  1.00 14.05 ? 261 PHE B CD2 1 
ATOM   4356  C  CE1 . PHE B  1 261 ? 14.955  -14.722 -3.255  1.00 17.10 ? 261 PHE B CE1 1 
ATOM   4357  C  CE2 . PHE B  1 261 ? 14.584  -15.061 -0.938  1.00 13.99 ? 261 PHE B CE2 1 
ATOM   4358  C  CZ  . PHE B  1 261 ? 14.244  -14.409 -2.109  1.00 14.90 ? 261 PHE B CZ  1 
ATOM   4359  N  N   . SER B  1 262 ? 20.140  -15.990 -3.633  1.00 18.87 ? 262 SER B N   1 
ATOM   4360  C  CA  . SER B  1 262 ? 20.661  -14.971 -4.563  1.00 25.06 ? 262 SER B CA  1 
ATOM   4361  C  C   . SER B  1 262 ? 20.018  -15.047 -5.879  1.00 28.26 ? 262 SER B C   1 
ATOM   4362  O  O   . SER B  1 262 ? 20.334  -14.234 -6.733  1.00 30.84 ? 262 SER B O   1 
ATOM   4363  C  CB  . SER B  1 262 ? 22.150  -15.134 -4.801  1.00 26.86 ? 262 SER B CB  1 
ATOM   4364  O  OG  . SER B  1 262 ? 22.477  -16.463 -5.198  1.00 27.82 ? 262 SER B OG  1 
ATOM   4365  N  N   . GLN B  1 263 ? 19.131  -16.031 -6.036  1.00 31.48 ? 263 GLN B N   1 
ATOM   4366  C  CA  . GLN B  1 263 ? 18.453  -16.354 -7.286  1.00 35.40 ? 263 GLN B CA  1 
ATOM   4367  C  C   . GLN B  1 263 ? 17.419  -17.472 -7.053  1.00 35.15 ? 263 GLN B C   1 
ATOM   4368  O  O   . GLN B  1 263 ? 16.499  -17.607 -7.888  1.00 37.19 ? 263 GLN B O   1 
ATOM   4369  C  CB  . GLN B  1 263 ? 19.449  -16.821 -8.376  1.00 35.30 ? 263 GLN B CB  1 
ATOM   4370  C  CG  . GLN B  1 263 ? 20.122  -18.187 -8.096  1.00 39.00 ? 263 GLN B CG  1 
ATOM   4371  C  CD  . GLN B  1 263 ? 20.938  -18.710 -9.302  1.00 39.48 ? 263 GLN B CD  1 
ATOM   4372  O  OE1 . GLN B  1 263 ? 22.130  -18.999 -9.169  1.00 48.23 ? 263 GLN B OE1 1 
ATOM   4373  N  NE2 . GLN B  1 263 ? 20.286  -18.824 -10.486 1.00 43.57 ? 263 GLN B NE2 1 
ATOM   4374  O  OXT . GLN B  1 263 ? 17.473  -18.252 -6.067  1.00 32.98 ? 263 GLN B OXT 1 
ATOM   4375  N  N   . LYS C  1 3   ? 32.452  24.915  50.929  1.00 29.30 ? 3   LYS C N   1 
ATOM   4376  C  CA  . LYS C  1 3   ? 31.342  24.700  50.000  1.00 26.81 ? 3   LYS C CA  1 
ATOM   4377  C  C   . LYS C  1 3   ? 31.613  23.367  49.232  1.00 22.15 ? 3   LYS C C   1 
ATOM   4378  O  O   . LYS C  1 3   ? 32.647  22.623  49.424  1.00 24.78 ? 3   LYS C O   1 
ATOM   4379  C  CB  . LYS C  1 3   ? 31.120  25.893  49.040  1.00 27.42 ? 3   LYS C CB  1 
ATOM   4380  C  CG  . LYS C  1 3   ? 30.612  27.231  49.769  0.01 31.68 ? 3   LYS C CG  1 
ATOM   4381  C  CD  . LYS C  1 3   ? 30.383  28.528  48.829  0.01 31.99 ? 3   LYS C CD  1 
ATOM   4382  C  CE  . LYS C  1 3   ? 29.870  29.739  49.653  0.01 39.55 ? 3   LYS C CE  1 
ATOM   4383  N  NZ  . LYS C  1 3   ? 29.638  31.013  48.908  0.01 42.94 ? 3   LYS C NZ  1 
ATOM   4384  N  N   . TRP C  1 4   ? 30.724  23.138  48.289  1.00 14.52 ? 4   TRP C N   1 
ATOM   4385  C  CA  . TRP C  1 4   ? 30.670  21.794  47.663  1.00 11.39 ? 4   TRP C CA  1 
ATOM   4386  C  C   . TRP C  1 4   ? 31.780  21.639  46.601  1.00 10.47 ? 4   TRP C C   1 
ATOM   4387  O  O   . TRP C  1 4   ? 32.226  22.587  45.935  1.00 12.01 ? 4   TRP C O   1 
ATOM   4388  C  CB  . TRP C  1 4   ? 29.260  21.590  47.105  1.00 11.51 ? 4   TRP C CB  1 
ATOM   4389  C  CG  . TRP C  1 4   ? 28.891  22.447  45.911  1.00 8.70  ? 4   TRP C CG  1 
ATOM   4390  C  CD1 . TRP C  1 4   ? 28.257  23.653  45.951  1.00 8.88  ? 4   TRP C CD1 1 
ATOM   4391  C  CD2 . TRP C  1 4   ? 29.083  22.135  44.525  1.00 9.68  ? 4   TRP C CD2 1 
ATOM   4392  N  NE1 . TRP C  1 4   ? 27.975  24.119  44.703  1.00 9.14  ? 4   TRP C NE1 1 
ATOM   4393  C  CE2 . TRP C  1 4   ? 28.534  23.209  43.769  1.00 9.45  ? 4   TRP C CE2 1 
ATOM   4394  C  CE3 . TRP C  1 4   ? 29.677  21.051  43.851  1.00 7.81  ? 4   TRP C CE3 1 
ATOM   4395  C  CZ2 . TRP C  1 4   ? 28.528  23.212  42.328  1.00 8.59  ? 4   TRP C CZ2 1 
ATOM   4396  C  CZ3 . TRP C  1 4   ? 29.663  21.067  42.455  1.00 7.85  ? 4   TRP C CZ3 1 
ATOM   4397  C  CH2 . TRP C  1 4   ? 29.127  22.074  41.733  1.00 7.90  ? 4   TRP C CH2 1 
ATOM   4398  N  N   . THR C  1 5   ? 32.221  20.389  46.510  1.00 9.58  ? 5   THR C N   1 
ATOM   4399  C  CA  . THR C  1 5   ? 33.261  19.991  45.496  1.00 9.40  ? 5   THR C CA  1 
ATOM   4400  C  C   . THR C  1 5   ? 32.991  18.610  44.899  1.00 7.84  ? 5   THR C C   1 
ATOM   4401  O  O   . THR C  1 5   ? 31.906  18.037  45.171  1.00 7.78  ? 5   THR C O   1 
ATOM   4402  C  CB  . THR C  1 5   ? 34.633  19.756  46.157  1.00 10.96 ? 5   THR C CB  1 
ATOM   4403  O  OG1 . THR C  1 5   ? 34.566  18.591  46.986  1.00 11.77 ? 5   THR C OG1 1 
ATOM   4404  C  CG2 . THR C  1 5   ? 35.150  21.020  46.943  1.00 13.09 ? 5   THR C CG2 1 
ATOM   4405  N  N   . TYR C  1 6   ? 33.850  18.116  44.033  1.00 7.50  ? 6   TYR C N   1 
ATOM   4406  C  CA  . TYR C  1 6   ? 33.718  16.767  43.460  1.00 7.07  ? 6   TYR C CA  1 
ATOM   4407  C  C   . TYR C  1 6   ? 34.664  15.762  44.062  1.00 7.53  ? 6   TYR C C   1 
ATOM   4408  O  O   . TYR C  1 6   ? 34.746  14.621  43.633  1.00 7.98  ? 6   TYR C O   1 
ATOM   4409  C  CB  . TYR C  1 6   ? 33.935  16.805  41.911  1.00 9.16  ? 6   TYR C CB  1 
ATOM   4410  C  CG  . TYR C  1 6   ? 32.798  17.489  41.151  1.00 7.37  ? 6   TYR C CG  1 
ATOM   4411  C  CD1 . TYR C  1 6   ? 32.778  18.870  40.865  1.00 7.39  ? 6   TYR C CD1 1 
ATOM   4412  C  CD2 . TYR C  1 6   ? 31.719  16.731  40.706  1.00 7.58  ? 6   TYR C CD2 1 
ATOM   4413  C  CE1 . TYR C  1 6   ? 31.785  19.460  40.089  1.00 5.98  ? 6   TYR C CE1 1 
ATOM   4414  C  CE2 . TYR C  1 6   ? 30.719  17.250  39.919  1.00 6.32  ? 6   TYR C CE2 1 
ATOM   4415  C  CZ  . TYR C  1 6   ? 30.737  18.622  39.601  1.00 7.61  ? 6   TYR C CZ  1 
ATOM   4416  O  OH  . TYR C  1 6   ? 29.796  19.240  38.829  1.00 7.24  ? 6   TYR C OH  1 
ATOM   4417  N  N   . PHE C  1 7   ? 35.409  16.218  45.115  1.00 8.65  ? 7   PHE C N   1 
ATOM   4418  C  CA  . PHE C  1 7   ? 36.530  15.431  45.557  1.00 10.73 ? 7   PHE C CA  1 
ATOM   4419  C  C   . PHE C  1 7   ? 36.804  15.690  47.056  1.00 12.72 ? 7   PHE C C   1 
ATOM   4420  O  O   . PHE C  1 7   ? 37.091  16.869  47.422  1.00 13.35 ? 7   PHE C O   1 
ATOM   4421  C  CB  . PHE C  1 7   ? 37.809  15.864  44.825  1.00 12.79 ? 7   PHE C CB  1 
ATOM   4422  C  CG  . PHE C  1 7   ? 39.065  15.080  45.272  1.00 14.87 ? 7   PHE C CG  1 
ATOM   4423  C  CD1 . PHE C  1 7   ? 39.124  13.678  45.310  1.00 15.37 ? 7   PHE C CD1 1 
ATOM   4424  C  CD2 . PHE C  1 7   ? 40.247  15.771  45.512  1.00 20.55 ? 7   PHE C CD2 1 
ATOM   4425  C  CE1 . PHE C  1 7   ? 40.308  12.970  45.707  1.00 18.76 ? 7   PHE C CE1 1 
ATOM   4426  C  CE2 . PHE C  1 7   ? 41.449  15.072  45.895  1.00 20.72 ? 7   PHE C CE2 1 
ATOM   4427  C  CZ  . PHE C  1 7   ? 41.456  13.681  45.993  1.00 17.66 ? 7   PHE C CZ  1 
ATOM   4428  N  N   . GLY C  1 8   ? 36.754  14.613  47.863  1.00 12.03 ? 8   GLY C N   1 
ATOM   4429  C  CA  . GLY C  1 8   ? 37.067  14.829  49.304  1.00 9.41  ? 8   GLY C CA  1 
ATOM   4430  C  C   . GLY C  1 8   ? 35.800  14.976  50.142  1.00 12.96 ? 8   GLY C C   1 
ATOM   4431  O  O   . GLY C  1 8   ? 34.727  14.560  49.689  1.00 11.89 ? 8   GLY C O   1 
ATOM   4432  N  N   . PRO C  1 9   ? 35.918  15.442  51.399  1.00 10.48 ? 9   PRO C N   1 
ATOM   4433  C  CA  . PRO C  1 9   ? 34.848  15.318  52.335  1.00 11.51 ? 9   PRO C CA  1 
ATOM   4434  C  C   . PRO C  1 9   ? 33.656  16.212  52.070  1.00 10.82 ? 9   PRO C C   1 
ATOM   4435  O  O   . PRO C  1 9   ? 32.544  16.004  52.634  1.00 13.62 ? 9   PRO C O   1 
ATOM   4436  C  CB  . PRO C  1 9   ? 35.473  15.752  53.719  1.00 13.37 ? 9   PRO C CB  1 
ATOM   4437  C  CG  . PRO C  1 9   ? 36.825  16.318  53.410  1.00 11.93 ? 9   PRO C CG  1 
ATOM   4438  C  CD  . PRO C  1 9   ? 37.171  15.980  52.024  1.00 11.86 ? 9   PRO C CD  1 
ATOM   4439  N  N   . ASP C  1 10  ? 33.815  17.175  51.128  1.00 10.15 ? 10  ASP C N   1 
ATOM   4440  C  CA  . ASP C  1 10  ? 32.718  18.001  50.590  1.00 9.89  ? 10  ASP C CA  1 
ATOM   4441  C  C   . ASP C  1 10  ? 32.216  17.568  49.151  1.00 9.87  ? 10  ASP C C   1 
ATOM   4442  O  O   . ASP C  1 10  ? 31.431  18.291  48.510  1.00 7.67  ? 10  ASP C O   1 
ATOM   4443  C  CB  . ASP C  1 10  ? 33.008  19.480  50.613  1.00 11.91 ? 10  ASP C CB  1 
ATOM   4444  C  CG  . ASP C  1 10  ? 33.158  19.989  52.006  1.00 15.09 ? 10  ASP C CG  1 
ATOM   4445  O  OD1 . ASP C  1 10  ? 32.181  19.953  52.805  1.00 13.92 ? 10  ASP C OD1 1 
ATOM   4446  O  OD2 . ASP C  1 10  ? 34.294  20.570  52.260  1.00 18.11 ? 10  ASP C OD2 1 
ATOM   4447  N  N   . GLY C  1 11  ? 32.633  16.319  48.809  1.00 9.08  ? 11  GLY C N   1 
ATOM   4448  C  CA  . GLY C  1 11  ? 32.221  15.745  47.506  1.00 6.24  ? 11  GLY C CA  1 
ATOM   4449  C  C   . GLY C  1 11  ? 30.766  15.204  47.492  1.00 5.49  ? 11  GLY C C   1 
ATOM   4450  O  O   . GLY C  1 11  ? 29.900  15.433  48.429  1.00 6.24  ? 11  GLY C O   1 
ATOM   4451  N  N   . GLU C  1 12  ? 30.451  14.486  46.376  1.00 5.39  ? 12  GLU C N   1 
ATOM   4452  C  CA  . GLU C  1 12  ? 29.018  14.327  46.071  1.00 5.32  ? 12  GLU C CA  1 
ATOM   4453  C  C   . GLU C  1 12  ? 28.175  13.516  47.036  1.00 4.21  ? 12  GLU C C   1 
ATOM   4454  O  O   . GLU C  1 12  ? 26.943  13.703  47.076  1.00 5.02  ? 12  GLU C O   1 
ATOM   4455  C  CB  . GLU C  1 12  ? 28.842  13.772  44.607  1.00 5.37  ? 12  GLU C CB  1 
ATOM   4456  C  CG  . GLU C  1 12  ? 29.368  12.288  44.542  1.00 4.64  ? 12  GLU C CG  1 
ATOM   4457  C  CD  . GLU C  1 12  ? 29.554  11.941  43.054  1.00 4.94  ? 12  GLU C CD  1 
ATOM   4458  O  OE1 . GLU C  1 12  ? 28.558  11.632  42.336  1.00 5.71  ? 12  GLU C OE1 1 
ATOM   4459  O  OE2 . GLU C  1 12  ? 30.739  12.124  42.608  1.00 5.51  ? 12  GLU C OE2 1 
ATOM   4460  N  N   . ASN C  1 13  ? 28.821  12.633  47.817  1.00 4.33  ? 13  ASN C N   1 
ATOM   4461  C  CA  . ASN C  1 13  ? 27.999  11.839  48.757  1.00 4.34  ? 13  ASN C CA  1 
ATOM   4462  C  C   . ASN C  1 13  ? 27.539  12.684  49.939  1.00 4.94  ? 13  ASN C C   1 
ATOM   4463  O  O   . ASN C  1 13  ? 26.669  12.249  50.696  1.00 5.59  ? 13  ASN C O   1 
ATOM   4464  C  CB  . ASN C  1 13  ? 28.830  10.659  49.277  1.00 4.88  ? 13  ASN C CB  1 
ATOM   4465  C  CG  . ASN C  1 13  ? 28.962  9.531   48.202  1.00 5.17  ? 13  ASN C CG  1 
ATOM   4466  O  OD1 . ASN C  1 13  ? 28.436  9.643   47.097  1.00 5.92  ? 13  ASN C OD1 1 
ATOM   4467  N  ND2 . ASN C  1 13  ? 29.719  8.520   48.540  1.00 5.44  ? 13  ASN C ND2 1 
ATOM   4468  N  N   A SER C  1 14  ? 28.197  13.848  50.092  0.50 5.44  ? 14  SER C N   1 
ATOM   4469  N  N   B SER C  1 14  ? 28.050  13.896  50.055  0.50 4.66  ? 14  SER C N   1 
ATOM   4470  C  CA  A SER C  1 14  ? 27.871  14.879  51.126  0.50 6.97  ? 14  SER C CA  1 
ATOM   4471  C  CA  B SER C  1 14  ? 27.615  14.731  51.188  0.50 5.46  ? 14  SER C CA  1 
ATOM   4472  C  C   A SER C  1 14  ? 27.080  16.040  50.628  0.50 5.57  ? 14  SER C C   1 
ATOM   4473  C  C   B SER C  1 14  ? 26.957  15.979  50.665  0.50 4.70  ? 14  SER C C   1 
ATOM   4474  O  O   A SER C  1 14  ? 26.675  16.915  51.442  0.50 6.37  ? 14  SER C O   1 
ATOM   4475  O  O   B SER C  1 14  ? 26.520  16.843  51.496  0.50 4.46  ? 14  SER C O   1 
ATOM   4476  C  CB  A SER C  1 14  ? 29.117  15.383  51.885  0.50 6.67  ? 14  SER C CB  1 
ATOM   4477  C  CB  B SER C  1 14  ? 28.768  15.117  52.132  0.50 4.35  ? 14  SER C CB  1 
ATOM   4478  O  OG  A SER C  1 14  ? 29.709  14.278  52.540  0.50 11.28 ? 14  SER C OG  1 
ATOM   4479  O  OG  B SER C  1 14  ? 29.802  15.821  51.422  0.50 3.02  ? 14  SER C OG  1 
ATOM   4480  N  N   . TRP C  1 15  ? 26.742  16.130  49.339  1.00 5.29  ? 15  TRP C N   1 
ATOM   4481  C  CA  . TRP C  1 15  ? 25.986  17.295  48.872  1.00 4.89  ? 15  TRP C CA  1 
ATOM   4482  C  C   . TRP C  1 15  ? 24.603  17.359  49.555  1.00 6.15  ? 15  TRP C C   1 
ATOM   4483  O  O   . TRP C  1 15  ? 24.132  18.496  49.771  1.00 6.31  ? 15  TRP C O   1 
ATOM   4484  C  CB  . TRP C  1 15  ? 25.726  17.170  47.371  1.00 4.85  ? 15  TRP C CB  1 
ATOM   4485  C  CG  . TRP C  1 15  ? 26.920  17.339  46.516  1.00 5.59  ? 15  TRP C CG  1 
ATOM   4486  C  CD1 . TRP C  1 15  ? 28.204  17.794  46.871  1.00 7.95  ? 15  TRP C CD1 1 
ATOM   4487  C  CD2 . TRP C  1 15  ? 26.972  17.216  45.055  1.00 5.89  ? 15  TRP C CD2 1 
ATOM   4488  N  NE1 . TRP C  1 15  ? 29.073  17.855  45.747  1.00 6.66  ? 15  TRP C NE1 1 
ATOM   4489  C  CE2 . TRP C  1 15  ? 28.305  17.533  44.646  1.00 5.79  ? 15  TRP C CE2 1 
ATOM   4490  C  CE3 . TRP C  1 15  ? 26.053  16.852  44.077  1.00 5.37  ? 15  TRP C CE3 1 
ATOM   4491  C  CZ2 . TRP C  1 15  ? 28.732  17.439  43.338  1.00 5.20  ? 15  TRP C CZ2 1 
ATOM   4492  C  CZ3 . TRP C  1 15  ? 26.454  16.770  42.763  1.00 5.94  ? 15  TRP C CZ3 1 
ATOM   4493  C  CH2 . TRP C  1 15  ? 27.747  17.089  42.392  1.00 5.74  ? 15  TRP C CH2 1 
ATOM   4494  N  N   . SER C  1 16  ? 23.974  16.204  49.857  1.00 5.53  ? 16  SER C N   1 
ATOM   4495  C  CA  . SER C  1 16  ? 22.604  16.256  50.457  1.00 4.82  ? 16  SER C CA  1 
ATOM   4496  C  C   . SER C  1 16  ? 22.695  16.946  51.894  1.00 6.34  ? 16  SER C C   1 
ATOM   4497  O  O   . SER C  1 16  ? 21.671  17.360  52.399  1.00 7.07  ? 16  SER C O   1 
ATOM   4498  C  CB  . SER C  1 16  ? 22.096  14.829  50.640  1.00 7.07  ? 16  SER C CB  1 
ATOM   4499  O  OG  . SER C  1 16  ? 22.872  14.135  51.612  1.00 6.55  ? 16  SER C OG  1 
ATOM   4500  N  N   . LYS C  1 17  ? 23.887  17.011  52.541  1.00 6.31  ? 17  LYS C N   1 
ATOM   4501  C  CA  . LYS C  1 17  ? 23.966  17.689  53.841  1.00 6.42  ? 17  LYS C CA  1 
ATOM   4502  C  C   . LYS C  1 17  ? 23.807  19.173  53.626  1.00 5.36  ? 17  LYS C C   1 
ATOM   4503  O  O   . LYS C  1 17  ? 23.439  19.893  54.602  1.00 6.58  ? 17  LYS C O   1 
ATOM   4504  C  CB  . LYS C  1 17  ? 25.315  17.418  54.451  1.00 7.12  ? 17  LYS C CB  1 
ATOM   4505  C  CG  . LYS C  1 17  ? 25.528  16.004  54.965  1.00 9.98  ? 17  LYS C CG  1 
ATOM   4506  C  CD  . LYS C  1 17  ? 26.945  15.904  55.598  1.00 16.56 ? 17  LYS C CD  1 
ATOM   4507  C  CE  . LYS C  1 17  ? 27.566  14.526  55.615  1.00 18.40 ? 17  LYS C CE  1 
ATOM   4508  N  NZ  . LYS C  1 17  ? 28.883  14.606  56.395  1.00 18.09 ? 17  LYS C NZ  1 
ATOM   4509  N  N   . LYS C  1 18  ? 24.117  19.665  52.415  1.00 6.85  ? 18  LYS C N   1 
ATOM   4510  C  CA  . LYS C  1 18  ? 24.100  21.117  52.169  1.00 8.44  ? 18  LYS C CA  1 
ATOM   4511  C  C   . LYS C  1 18  ? 22.967  21.585  51.266  1.00 7.67  ? 18  LYS C C   1 
ATOM   4512  O  O   . LYS C  1 18  ? 22.560  22.733  51.342  1.00 7.97  ? 18  LYS C O   1 
ATOM   4513  C  CB  . LYS C  1 18  ? 25.436  21.482  51.438  1.00 12.03 ? 18  LYS C CB  1 
ATOM   4514  C  CG  . LYS C  1 18  ? 26.766  21.193  52.269  1.00 14.70 ? 18  LYS C CG  1 
ATOM   4515  C  CD  . LYS C  1 18  ? 28.062  21.362  51.352  1.00 17.66 ? 18  LYS C CD  1 
ATOM   4516  C  CE  . LYS C  1 18  ? 29.316  20.985  52.181  1.00 18.36 ? 18  LYS C CE  1 
ATOM   4517  N  NZ  . LYS C  1 18  ? 29.293  19.551  52.652  1.00 26.61 ? 18  LYS C NZ  1 
ATOM   4518  N  N   . TYR C  1 19  ? 22.359  20.630  50.530  1.00 6.61  ? 19  TYR C N   1 
ATOM   4519  C  CA  . TYR C  1 19  ? 21.368  20.954  49.524  1.00 7.03  ? 19  TYR C CA  1 
ATOM   4520  C  C   . TYR C  1 19  ? 20.331  19.827  49.555  1.00 5.88  ? 19  TYR C C   1 
ATOM   4521  O  O   . TYR C  1 19  ? 20.637  18.679  49.057  1.00 6.68  ? 19  TYR C O   1 
ATOM   4522  C  CB  . TYR C  1 19  ? 22.018  21.060  48.059  1.00 7.56  ? 19  TYR C CB  1 
ATOM   4523  C  CG  . TYR C  1 19  ? 23.040  22.153  47.973  1.00 8.06  ? 19  TYR C CG  1 
ATOM   4524  C  CD1 . TYR C  1 19  ? 24.373  21.825  48.219  1.00 8.67  ? 19  TYR C CD1 1 
ATOM   4525  C  CD2 . TYR C  1 19  ? 22.663  23.465  47.754  1.00 8.87  ? 19  TYR C CD2 1 
ATOM   4526  C  CE1 . TYR C  1 19  ? 25.372  22.884  48.275  1.00 7.84  ? 19  TYR C CE1 1 
ATOM   4527  C  CE2 . TYR C  1 19  ? 23.596  24.496  47.708  1.00 8.26  ? 19  TYR C CE2 1 
ATOM   4528  C  CZ  . TYR C  1 19  ? 24.902  24.176  48.034  1.00 8.85  ? 19  TYR C CZ  1 
ATOM   4529  O  OH  . TYR C  1 19  ? 25.918  25.175  47.976  1.00 13.95 ? 19  TYR C OH  1 
ATOM   4530  N  N   . PRO C  1 20  ? 19.166  20.009  50.160  1.00 6.66  ? 20  PRO C N   1 
ATOM   4531  C  CA  . PRO C  1 20  ? 18.273  18.898  50.336  1.00 6.80  ? 20  PRO C CA  1 
ATOM   4532  C  C   . PRO C  1 20  ? 17.859  18.146  49.051  1.00 6.01  ? 20  PRO C C   1 
ATOM   4533  O  O   . PRO C  1 20  ? 17.670  16.944  49.116  1.00 7.43  ? 20  PRO C O   1 
ATOM   4534  C  CB  . PRO C  1 20  ? 17.016  19.486  51.035  1.00 8.62  ? 20  PRO C CB  1 
ATOM   4535  C  CG  . PRO C  1 20  ? 17.156  20.945  50.872  1.00 9.91  ? 20  PRO C CG  1 
ATOM   4536  C  CD  . PRO C  1 20  ? 18.653  21.306  50.716  1.00 7.00  ? 20  PRO C CD  1 
ATOM   4537  N  N   . SER C  1 21  ? 17.680  18.846  47.918  1.00 5.68  ? 21  SER C N   1 
ATOM   4538  C  CA  . SER C  1 21  ? 17.200  18.138  46.739  1.00 5.45  ? 21  SER C CA  1 
ATOM   4539  C  C   . SER C  1 21  ? 18.290  17.139  46.250  1.00 5.72  ? 21  SER C C   1 
ATOM   4540  O  O   . SER C  1 21  ? 17.915  16.246  45.465  1.00 6.27  ? 21  SER C O   1 
ATOM   4541  C  CB  . SER C  1 21  ? 16.888  19.093  45.608  1.00 7.65  ? 21  SER C CB  1 
ATOM   4542  O  OG  . SER C  1 21  ? 15.738  19.890  45.986  1.00 8.86  ? 21  SER C OG  1 
ATOM   4543  N  N   . CYS C  1 22  ? 19.575  17.295  46.629  1.00 5.49  ? 22  CYS C N   1 
ATOM   4544  C  CA  . CYS C  1 22  ? 20.558  16.320  46.138  1.00 6.46  ? 22  CYS C CA  1 
ATOM   4545  C  C   . CYS C  1 22  ? 20.378  14.944  46.665  1.00 6.68  ? 22  CYS C C   1 
ATOM   4546  O  O   . CYS C  1 22  ? 20.943  13.974  46.085  1.00 6.29  ? 22  CYS C O   1 
ATOM   4547  C  CB  . CYS C  1 22  ? 21.986  16.747  46.448  1.00 6.33  ? 22  CYS C CB  1 
ATOM   4548  S  SG  . CYS C  1 22  ? 22.426  18.401  45.675  1.00 6.27  ? 22  CYS C SG  1 
ATOM   4549  N  N   . GLY C  1 23  ? 19.616  14.775  47.764  1.00 5.90  ? 23  GLY C N   1 
ATOM   4550  C  CA  . GLY C  1 23  ? 19.218  13.407  48.219  1.00 6.88  ? 23  GLY C CA  1 
ATOM   4551  C  C   . GLY C  1 23  ? 17.720  13.109  47.921  1.00 7.23  ? 23  GLY C C   1 
ATOM   4552  O  O   . GLY C  1 23  ? 17.157  12.123  48.463  1.00 9.16  ? 23  GLY C O   1 
ATOM   4553  N  N   . GLY C  1 24  ? 17.117  13.918  47.100  1.00 6.72  ? 24  GLY C N   1 
ATOM   4554  C  CA  . GLY C  1 24  ? 15.702  13.796  46.750  1.00 8.29  ? 24  GLY C CA  1 
ATOM   4555  C  C   . GLY C  1 24  ? 15.482  13.021  45.456  1.00 9.97  ? 24  GLY C C   1 
ATOM   4556  O  O   . GLY C  1 24  ? 16.339  12.147  45.043  1.00 9.09  ? 24  GLY C O   1 
ATOM   4557  N  N   . LEU C  1 25  ? 14.290  13.213  44.858  1.00 8.71  ? 25  LEU C N   1 
ATOM   4558  C  CA  . LEU C  1 25  ? 13.832  12.370  43.776  1.00 9.24  ? 25  LEU C CA  1 
ATOM   4559  C  C   . LEU C  1 25  ? 14.409  12.852  42.516  1.00 8.58  ? 25  LEU C C   1 
ATOM   4560  O  O   . LEU C  1 25  ? 14.938  13.974  42.443  1.00 7.82  ? 25  LEU C O   1 
ATOM   4561  C  CB  . LEU C  1 25  ? 12.302  12.353  43.699  1.00 9.68  ? 25  LEU C CB  1 
ATOM   4562  C  CG  . LEU C  1 25  ? 11.437  11.424  44.582  1.00 17.49 ? 25  LEU C CG  1 
ATOM   4563  C  CD1 . LEU C  1 25  ? 12.118  10.360  45.451  1.00 17.61 ? 25  LEU C CD1 1 
ATOM   4564  C  CD2 . LEU C  1 25  ? 10.128  11.973  45.162  1.00 18.72 ? 25  LEU C CD2 1 
ATOM   4565  N  N   . LEU C  1 26  ? 14.263  12.007  41.498  1.00 8.67  ? 26  LEU C N   1 
ATOM   4566  C  CA  . LEU C  1 26  ? 14.409  12.423  40.075  1.00 9.24  ? 26  LEU C CA  1 
ATOM   4567  C  C   . LEU C  1 26  ? 15.845  12.902  39.800  1.00 6.56  ? 26  LEU C C   1 
ATOM   4568  O  O   . LEU C  1 26  ? 16.055  13.762  38.909  1.00 7.23  ? 26  LEU C O   1 
ATOM   4569  C  CB  . LEU C  1 26  ? 13.388  13.507  39.624  1.00 9.27  ? 26  LEU C CB  1 
ATOM   4570  C  CG  . LEU C  1 26  ? 11.895  13.096  39.706  1.00 15.04 ? 26  LEU C CG  1 
ATOM   4571  C  CD1 . LEU C  1 26  ? 10.985  14.272  39.320  1.00 17.61 ? 26  LEU C CD1 1 
ATOM   4572  C  CD2 . LEU C  1 26  ? 11.617  11.970  38.771  1.00 17.32 ? 26  LEU C CD2 1 
ATOM   4573  N  N   . GLN C  1 27  ? 16.824  12.339  40.504  1.00 6.19  ? 27  GLN C N   1 
ATOM   4574  C  CA  . GLN C  1 27  ? 18.171  12.852  40.246  1.00 6.27  ? 27  GLN C CA  1 
ATOM   4575  C  C   . GLN C  1 27  ? 18.840  12.381  38.933  1.00 4.78  ? 27  GLN C C   1 
ATOM   4576  O  O   . GLN C  1 27  ? 18.566  11.300  38.440  1.00 6.54  ? 27  GLN C O   1 
ATOM   4577  C  CB  . GLN C  1 27  ? 19.099  12.468  41.427  1.00 6.32  ? 27  GLN C CB  1 
ATOM   4578  C  CG  . GLN C  1 27  ? 18.703  13.160  42.786  1.00 6.30  ? 27  GLN C CG  1 
ATOM   4579  C  CD  . GLN C  1 27  ? 18.812  14.627  42.668  1.00 5.82  ? 27  GLN C CD  1 
ATOM   4580  O  OE1 . GLN C  1 27  ? 19.933  15.139  42.834  1.00 4.95  ? 27  GLN C OE1 1 
ATOM   4581  N  NE2 . GLN C  1 27  ? 17.661  15.331  42.500  1.00 5.58  ? 27  GLN C NE2 1 
ATOM   4582  N  N   . SER C  1 28  ? 19.692  13.258  38.392  1.00 4.42  ? 28  SER C N   1 
ATOM   4583  C  CA  . SER C  1 28  ? 20.524  13.003  37.201  1.00 5.67  ? 28  SER C CA  1 
ATOM   4584  C  C   . SER C  1 28  ? 21.990  13.130  37.590  1.00 5.11  ? 28  SER C C   1 
ATOM   4585  O  O   . SER C  1 28  ? 22.348  13.744  38.645  1.00 5.61  ? 28  SER C O   1 
ATOM   4586  C  CB  . SER C  1 28  ? 20.222  14.154  36.208  1.00 4.65  ? 28  SER C CB  1 
ATOM   4587  O  OG  . SER C  1 28  ? 18.861  13.961  35.697  1.00 5.19  ? 28  SER C OG  1 
ATOM   4588  N  N   . PRO C  1 29  ? 22.903  12.602  36.776  1.00 4.75  ? 29  PRO C N   1 
ATOM   4589  C  CA  . PRO C  1 29  ? 22.691  11.861  35.522  1.00 4.19  ? 29  PRO C CA  1 
ATOM   4590  C  C   . PRO C  1 29  ? 22.356  10.410  35.751  1.00 4.83  ? 29  PRO C C   1 
ATOM   4591  O  O   . PRO C  1 29  ? 22.325  9.937   36.900  1.00 5.58  ? 29  PRO C O   1 
ATOM   4592  C  CB  . PRO C  1 29  ? 24.046  12.041  34.842  1.00 6.07  ? 29  PRO C CB  1 
ATOM   4593  C  CG  . PRO C  1 29  ? 25.123  11.927  35.990  1.00 4.64  ? 29  PRO C CG  1 
ATOM   4594  C  CD  . PRO C  1 29  ? 24.345  12.710  37.125  1.00 4.66  ? 29  PRO C CD  1 
ATOM   4595  N  N   . ILE C  1 30  ? 22.192  9.664   34.646  1.00 4.74  ? 30  ILE C N   1 
ATOM   4596  C  CA  . ILE C  1 30  ? 21.863  8.261   34.677  1.00 5.14  ? 30  ILE C CA  1 
ATOM   4597  C  C   . ILE C  1 30  ? 22.620  7.515   33.582  1.00 4.52  ? 30  ILE C C   1 
ATOM   4598  O  O   . ILE C  1 30  ? 23.162  8.122   32.695  1.00 5.82  ? 30  ILE C O   1 
ATOM   4599  C  CB  . ILE C  1 30  ? 20.285  7.994   34.533  1.00 5.26  ? 30  ILE C CB  1 
ATOM   4600  C  CG1 . ILE C  1 30  ? 19.856  8.561   33.195  1.00 5.72  ? 30  ILE C CG1 1 
ATOM   4601  C  CG2 . ILE C  1 30  ? 19.525  8.611   35.785  1.00 7.13  ? 30  ILE C CG2 1 
ATOM   4602  C  CD1 . ILE C  1 30  ? 18.386  8.167   32.817  1.00 7.04  ? 30  ILE C CD1 1 
ATOM   4603  N  N   . ASP C  1 31  ? 22.620  6.167   33.749  1.00 5.58  ? 31  ASP C N   1 
ATOM   4604  C  CA  . ASP C  1 31  ? 23.144  5.266   32.713  1.00 4.33  ? 31  ASP C CA  1 
ATOM   4605  C  C   . ASP C  1 31  ? 22.013  4.886   31.776  1.00 7.58  ? 31  ASP C C   1 
ATOM   4606  O  O   . ASP C  1 31  ? 20.938  4.455   32.225  1.00 8.36  ? 31  ASP C O   1 
ATOM   4607  C  CB  . ASP C  1 31  ? 23.759  4.023   33.292  1.00 5.37  ? 31  ASP C CB  1 
ATOM   4608  C  CG  . ASP C  1 31  ? 24.234  3.087   32.200  1.00 8.10  ? 31  ASP C CG  1 
ATOM   4609  O  OD1 . ASP C  1 31  ? 25.145  3.427   31.441  1.00 8.09  ? 31  ASP C OD1 1 
ATOM   4610  O  OD2 . ASP C  1 31  ? 23.636  1.986   32.069  1.00 11.69 ? 31  ASP C OD2 1 
ATOM   4611  N  N   . LEU C  1 32  ? 22.246  5.139   30.486  1.00 6.77  ? 32  LEU C N   1 
ATOM   4612  C  CA  . LEU C  1 32  ? 21.189  4.833   29.485  1.00 7.12  ? 32  LEU C CA  1 
ATOM   4613  C  C   . LEU C  1 32  ? 21.433  3.443   28.978  1.00 7.58  ? 32  LEU C C   1 
ATOM   4614  O  O   . LEU C  1 32  ? 22.457  3.244   28.269  1.00 8.41  ? 32  LEU C O   1 
ATOM   4615  C  CB  . LEU C  1 32  ? 21.362  5.918   28.356  1.00 7.17  ? 32  LEU C CB  1 
ATOM   4616  C  CG  . LEU C  1 32  ? 21.252  7.400   28.919  1.00 7.28  ? 32  LEU C CG  1 
ATOM   4617  C  CD1 . LEU C  1 32  ? 21.796  8.469   27.863  1.00 8.33  ? 32  LEU C CD1 1 
ATOM   4618  C  CD2 . LEU C  1 32  ? 19.826  7.765   29.344  1.00 9.91  ? 32  LEU C CD2 1 
ATOM   4619  N  N   . HIS C  1 33  ? 20.580  2.452   29.314  1.00 8.05  ? 33  HIS C N   1 
ATOM   4620  C  CA  . HIS C  1 33  ? 20.868  1.063   28.872  1.00 8.16  ? 33  HIS C CA  1 
ATOM   4621  C  C   . HIS C  1 33  ? 19.526  0.428   28.476  1.00 8.78  ? 33  HIS C C   1 
ATOM   4622  O  O   . HIS C  1 33  ? 18.463  0.929   28.881  1.00 8.99  ? 33  HIS C O   1 
ATOM   4623  C  CB  . HIS C  1 33  ? 21.588  0.210   29.945  1.00 10.09 ? 33  HIS C CB  1 
ATOM   4624  C  CG  . HIS C  1 33  ? 20.885  0.144   31.272  1.00 9.57  ? 33  HIS C CG  1 
ATOM   4625  N  ND1 . HIS C  1 33  ? 20.973  1.124   32.244  1.00 13.77 ? 33  HIS C ND1 1 
ATOM   4626  C  CD2 . HIS C  1 33  ? 20.074  -0.811  31.797  1.00 9.34  ? 33  HIS C CD2 1 
ATOM   4627  C  CE1 . HIS C  1 33  ? 20.222  0.781   33.287  1.00 16.73 ? 33  HIS C CE1 1 
ATOM   4628  N  NE2 . HIS C  1 33  ? 19.672  -0.390  33.030  1.00 10.13 ? 33  HIS C NE2 1 
ATOM   4629  N  N   A SER C  1 34  ? 19.562  -0.679  27.701  0.50 10.44 ? 34  SER C N   1 
ATOM   4630  N  N   B SER C  1 34  ? 19.636  -0.689  27.742  0.50 10.71 ? 34  SER C N   1 
ATOM   4631  C  CA  A SER C  1 34  ? 18.329  -1.171  27.033  0.50 12.12 ? 34  SER C CA  1 
ATOM   4632  C  CA  B SER C  1 34  ? 18.510  -1.273  27.038  0.50 13.30 ? 34  SER C CA  1 
ATOM   4633  C  C   A SER C  1 34  ? 17.124  -1.395  27.960  0.50 12.26 ? 34  SER C C   1 
ATOM   4634  C  C   B SER C  1 34  ? 17.227  -1.541  27.867  0.50 12.82 ? 34  SER C C   1 
ATOM   4635  O  O   A SER C  1 34  ? 15.964  -1.023  27.647  0.50 12.15 ? 34  SER C O   1 
ATOM   4636  O  O   B SER C  1 34  ? 16.096  -1.310  27.372  0.50 13.84 ? 34  SER C O   1 
ATOM   4637  C  CB  A SER C  1 34  ? 18.647  -2.461  26.260  0.50 12.72 ? 34  SER C CB  1 
ATOM   4638  C  CB  B SER C  1 34  ? 19.024  -2.546  26.367  0.50 13.27 ? 34  SER C CB  1 
ATOM   4639  O  OG  A SER C  1 34  ? 19.235  -3.436  27.105  0.50 11.67 ? 34  SER C OG  1 
ATOM   4640  O  OG  B SER C  1 34  ? 18.074  -3.021  25.462  0.50 16.84 ? 34  SER C OG  1 
ATOM   4641  N  N   . ASP C  1 35  ? 17.380  -1.983  29.129  1.00 11.60 ? 35  ASP C N   1 
ATOM   4642  C  CA  . ASP C  1 35  ? 16.243  -2.479  29.966  1.00 13.60 ? 35  ASP C CA  1 
ATOM   4643  C  C   . ASP C  1 35  ? 15.280  -1.345  30.325  1.00 14.18 ? 35  ASP C C   1 
ATOM   4644  O  O   . ASP C  1 35  ? 14.115  -1.623  30.588  1.00 14.88 ? 35  ASP C O   1 
ATOM   4645  C  CB  . ASP C  1 35  ? 16.791  -3.052  31.312  1.00 13.04 ? 35  ASP C CB  1 
ATOM   4646  C  CG  . ASP C  1 35  ? 17.950  -4.016  31.110  1.00 18.89 ? 35  ASP C CG  1 
ATOM   4647  O  OD1 . ASP C  1 35  ? 18.999  -3.580  30.589  1.00 18.74 ? 35  ASP C OD1 1 
ATOM   4648  O  OD2 . ASP C  1 35  ? 17.803  -5.202  31.469  1.00 12.46 ? 35  ASP C OD2 1 
ATOM   4649  N  N   . ILE C  1 36  ? 15.777  -0.083  30.326  1.00 12.24 ? 36  ILE C N   1 
ATOM   4650  C  CA  . ILE C  1 36  ? 15.019  1.089   30.774  1.00 12.03 ? 36  ILE C CA  1 
ATOM   4651  C  C   . ILE C  1 36  ? 14.664  2.040   29.574  1.00 10.17 ? 36  ILE C C   1 
ATOM   4652  O  O   . ILE C  1 36  ? 14.122  3.078   29.845  1.00 13.45 ? 36  ILE C O   1 
ATOM   4653  C  CB  . ILE C  1 36  ? 15.673  1.850   31.915  1.00 13.32 ? 36  ILE C CB  1 
ATOM   4654  C  CG1 . ILE C  1 36  ? 17.070  2.362   31.453  1.00 16.19 ? 36  ILE C CG1 1 
ATOM   4655  C  CG2 . ILE C  1 36  ? 15.671  0.930   33.256  1.00 12.77 ? 36  ILE C CG2 1 
ATOM   4656  C  CD1 . ILE C  1 36  ? 17.569  3.587   32.065  1.00 21.40 ? 36  ILE C CD1 1 
ATOM   4657  N  N   . LEU C  1 37  ? 14.936  1.617   28.336  1.00 10.52 ? 37  LEU C N   1 
ATOM   4658  C  CA  . LEU C  1 37  ? 14.609  2.463   27.162  1.00 10.55 ? 37  LEU C CA  1 
ATOM   4659  C  C   . LEU C  1 37  ? 13.221  2.028   26.653  1.00 11.83 ? 37  LEU C C   1 
ATOM   4660  O  O   . LEU C  1 37  ? 12.904  0.808   26.535  1.00 12.75 ? 37  LEU C O   1 
ATOM   4661  C  CB  . LEU C  1 37  ? 15.636  2.303   26.092  1.00 12.22 ? 37  LEU C CB  1 
ATOM   4662  C  CG  . LEU C  1 37  ? 17.049  2.666   26.443  1.00 11.15 ? 37  LEU C CG  1 
ATOM   4663  C  CD1 . LEU C  1 37  ? 17.931  2.356   25.220  1.00 15.47 ? 37  LEU C CD1 1 
ATOM   4664  C  CD2 . LEU C  1 37  ? 17.155  4.029   27.012  1.00 12.57 ? 37  LEU C CD2 1 
ATOM   4665  N  N   . GLN C  1 38  ? 12.455  3.045   26.221  1.00 8.66  ? 38  GLN C N   1 
ATOM   4666  C  CA  . GLN C  1 38  ? 11.157  2.777   25.583  1.00 10.58 ? 38  GLN C CA  1 
ATOM   4667  C  C   . GLN C  1 38  ? 11.068  3.735   24.358  1.00 9.66  ? 38  GLN C C   1 
ATOM   4668  O  O   . GLN C  1 38  ? 11.095  4.976   24.560  1.00 9.65  ? 38  GLN C O   1 
ATOM   4669  C  CB  . GLN C  1 38  ? 10.030  3.012   26.528  1.00 10.34 ? 38  GLN C CB  1 
ATOM   4670  C  CG  . GLN C  1 38  ? 8.724   2.478   25.848  1.00 13.64 ? 38  GLN C CG  1 
ATOM   4671  C  CD  . GLN C  1 38  ? 7.599   2.490   26.817  1.00 20.40 ? 38  GLN C CD  1 
ATOM   4672  O  OE1 . GLN C  1 38  ? 6.768   3.445   26.838  1.00 17.09 ? 38  GLN C OE1 1 
ATOM   4673  N  NE2 . GLN C  1 38  ? 7.577   1.463   27.662  1.00 21.52 ? 38  GLN C NE2 1 
ATOM   4674  N  N   . TYR C  1 39  ? 10.847  3.178   23.158  1.00 9.26  ? 39  TYR C N   1 
ATOM   4675  C  CA  . TYR C  1 39  ? 10.676  4.025   21.964  1.00 6.81  ? 39  TYR C CA  1 
ATOM   4676  C  C   . TYR C  1 39  ? 9.363   4.846   22.118  1.00 7.60  ? 39  TYR C C   1 
ATOM   4677  O  O   . TYR C  1 39  ? 8.334   4.295   22.606  1.00 7.97  ? 39  TYR C O   1 
ATOM   4678  C  CB  . TYR C  1 39  ? 10.612  3.083   20.715  1.00 9.98  ? 39  TYR C CB  1 
ATOM   4679  C  CG  . TYR C  1 39  ? 10.190  3.847   19.398  1.00 9.86  ? 39  TYR C CG  1 
ATOM   4680  C  CD1 . TYR C  1 39  ? 10.995  4.807   18.886  1.00 8.03  ? 39  TYR C CD1 1 
ATOM   4681  C  CD2 . TYR C  1 39  ? 8.897   3.672   18.878  1.00 10.76 ? 39  TYR C CD2 1 
ATOM   4682  C  CE1 . TYR C  1 39  ? 10.696  5.507   17.702  1.00 10.48 ? 39  TYR C CE1 1 
ATOM   4683  C  CE2 . TYR C  1 39  ? 8.543   4.368   17.699  1.00 11.87 ? 39  TYR C CE2 1 
ATOM   4684  C  CZ  . TYR C  1 39  ? 9.448   5.283   17.157  1.00 10.58 ? 39  TYR C CZ  1 
ATOM   4685  O  OH  . TYR C  1 39  ? 9.048   6.020   15.986  1.00 10.69 ? 39  TYR C OH  1 
ATOM   4686  N  N   . ASP C  1 40  ? 9.376   6.145   21.723  1.00 6.73  ? 40  ASP C N   1 
ATOM   4687  C  CA  . ASP C  1 40  ? 8.195   6.972   21.775  1.00 6.97  ? 40  ASP C CA  1 
ATOM   4688  C  C   . ASP C  1 40  ? 8.176   7.756   20.476  1.00 8.75  ? 40  ASP C C   1 
ATOM   4689  O  O   . ASP C  1 40  ? 8.964   8.678   20.237  1.00 6.98  ? 40  ASP C O   1 
ATOM   4690  C  CB  . ASP C  1 40  ? 8.367   7.889   23.001  1.00 8.81  ? 40  ASP C CB  1 
ATOM   4691  C  CG  . ASP C  1 40  ? 7.211   8.820   23.161  1.00 13.87 ? 40  ASP C CG  1 
ATOM   4692  O  OD1 . ASP C  1 40  ? 7.187   9.606   24.163  1.00 16.17 ? 40  ASP C OD1 1 
ATOM   4693  O  OD2 . ASP C  1 40  ? 6.305   8.944   22.308  1.00 10.87 ? 40  ASP C OD2 1 
ATOM   4694  N  N   . ALA C  1 41  ? 7.245   7.366   19.605  1.00 7.95  ? 41  ALA C N   1 
ATOM   4695  C  CA  . ALA C  1 41  ? 7.133   8.082   18.330  1.00 8.96  ? 41  ALA C CA  1 
ATOM   4696  C  C   . ALA C  1 41  ? 6.662   9.514   18.429  1.00 10.37 ? 41  ALA C C   1 
ATOM   4697  O  O   . ALA C  1 41  ? 6.798   10.260  17.429  1.00 11.73 ? 41  ALA C O   1 
ATOM   4698  C  CB  . ALA C  1 41  ? 6.175   7.253   17.403  1.00 8.63  ? 41  ALA C CB  1 
ATOM   4699  N  N   A SER C  1 42  ? 6.133   9.943   19.580  0.50 10.58 ? 42  SER C N   1 
ATOM   4700  N  N   B SER C  1 42  ? 6.132   9.944   19.586  0.50 10.07 ? 42  SER C N   1 
ATOM   4701  C  CA  A SER C  1 42  ? 5.725   11.320  19.684  0.50 12.08 ? 42  SER C CA  1 
ATOM   4702  C  CA  B SER C  1 42  ? 5.725   11.328  19.801  0.50 11.25 ? 42  SER C CA  1 
ATOM   4703  C  C   A SER C  1 42  ? 6.913   12.247  19.738  0.50 10.92 ? 42  SER C C   1 
ATOM   4704  C  C   B SER C  1 42  ? 6.900   12.283  20.023  0.50 9.41  ? 42  SER C C   1 
ATOM   4705  O  O   A SER C  1 42  ? 6.761   13.428  19.456  0.50 14.13 ? 42  SER C O   1 
ATOM   4706  O  O   B SER C  1 42  ? 6.743   13.497  20.155  0.50 7.98  ? 42  SER C O   1 
ATOM   4707  C  CB  A SER C  1 42  ? 4.775   11.603  20.887  0.50 12.61 ? 42  SER C CB  1 
ATOM   4708  C  CB  B SER C  1 42  ? 4.748   11.431  21.010  0.50 12.34 ? 42  SER C CB  1 
ATOM   4709  O  OG  A SER C  1 42  ? 5.449   11.555  22.126  0.50 15.16 ? 42  SER C OG  1 
ATOM   4710  O  OG  B SER C  1 42  ? 3.640   10.568  20.820  0.50 17.30 ? 42  SER C OG  1 
ATOM   4711  N  N   . LEU C  1 43  ? 8.108   11.738  20.123  1.00 9.38  ? 43  LEU C N   1 
ATOM   4712  C  CA  . LEU C  1 43  ? 9.329   12.587  20.284  1.00 9.21  ? 43  LEU C CA  1 
ATOM   4713  C  C   . LEU C  1 43  ? 9.821   13.124  18.950  1.00 11.17 ? 43  LEU C C   1 
ATOM   4714  O  O   . LEU C  1 43  ? 10.569  12.433  18.258  1.00 12.93 ? 43  LEU C O   1 
ATOM   4715  C  CB  . LEU C  1 43  ? 10.462  11.843  20.998  1.00 9.59  ? 43  LEU C CB  1 
ATOM   4716  C  CG  . LEU C  1 43  ? 10.132  11.362  22.423  1.00 7.89  ? 43  LEU C CG  1 
ATOM   4717  C  CD1 . LEU C  1 43  ? 11.265  10.618  22.966  1.00 9.14  ? 43  LEU C CD1 1 
ATOM   4718  C  CD2 . LEU C  1 43  ? 9.699   12.581  23.382  1.00 10.02 ? 43  LEU C CD2 1 
ATOM   4719  N  N   . THR C  1 44  ? 9.419   14.346  18.626  1.00 11.06 ? 44  THR C N   1 
ATOM   4720  C  CA  . THR C  1 44  ? 9.691   14.895  17.300  1.00 11.00 ? 44  THR C CA  1 
ATOM   4721  C  C   . THR C  1 44  ? 11.003  15.763  17.401  1.00 10.93 ? 44  THR C C   1 
ATOM   4722  O  O   . THR C  1 44  ? 11.556  16.083  18.514  1.00 10.31 ? 44  THR C O   1 
ATOM   4723  C  CB  . THR C  1 44  ? 8.531   15.780  16.852  1.00 12.84 ? 44  THR C CB  1 
ATOM   4724  O  OG1 . THR C  1 44  ? 8.236   16.731  17.903  1.00 17.21 ? 44  THR C OG1 1 
ATOM   4725  C  CG2 . THR C  1 44  ? 7.368   14.858  16.541  1.00 17.26 ? 44  THR C CG2 1 
ATOM   4726  N  N   . PRO C  1 45  ? 11.545  16.197  16.279  1.00 11.77 ? 45  PRO C N   1 
ATOM   4727  C  CA  . PRO C  1 45  ? 12.751  17.017  16.346  1.00 12.81 ? 45  PRO C CA  1 
ATOM   4728  C  C   . PRO C  1 45  ? 12.566  18.318  17.045  1.00 11.92 ? 45  PRO C C   1 
ATOM   4729  O  O   . PRO C  1 45  ? 11.550  19.008  16.819  1.00 15.20 ? 45  PRO C O   1 
ATOM   4730  C  CB  . PRO C  1 45  ? 13.011  17.267  14.858  1.00 12.79 ? 45  PRO C CB  1 
ATOM   4731  C  CG  . PRO C  1 45  ? 12.501  16.022  14.189  1.00 14.82 ? 45  PRO C CG  1 
ATOM   4732  C  CD  . PRO C  1 45  ? 11.168  15.946  14.859  1.00 14.12 ? 45  PRO C CD  1 
ATOM   4733  N  N   A LEU C  1 46  ? 13.545  18.683  17.854  0.50 10.55 ? 46  LEU C N   1 
ATOM   4734  N  N   B LEU C  1 46  ? 13.543  18.682  17.861  0.50 11.39 ? 46  LEU C N   1 
ATOM   4735  C  CA  A LEU C  1 46  ? 13.597  20.050  18.370  0.50 9.94  ? 46  LEU C CA  1 
ATOM   4736  C  CA  B LEU C  1 46  ? 13.614  20.051  18.385  0.50 11.85 ? 46  LEU C CA  1 
ATOM   4737  C  C   A LEU C  1 46  ? 14.021  21.036  17.253  0.50 10.85 ? 46  LEU C C   1 
ATOM   4738  C  C   B LEU C  1 46  ? 13.952  21.013  17.218  0.50 11.88 ? 46  LEU C C   1 
ATOM   4739  O  O   A LEU C  1 46  ? 14.843  20.716  16.363  0.50 12.35 ? 46  LEU C O   1 
ATOM   4740  O  O   B LEU C  1 46  ? 14.601  20.630  16.224  0.50 13.91 ? 46  LEU C O   1 
ATOM   4741  C  CB  A LEU C  1 46  ? 14.546  20.212  19.581  0.50 11.34 ? 46  LEU C CB  1 
ATOM   4742  C  CB  B LEU C  1 46  ? 14.664  20.225  19.525  0.50 12.96 ? 46  LEU C CB  1 
ATOM   4743  C  CG  A LEU C  1 46  ? 14.073  19.427  20.788  0.50 13.10 ? 46  LEU C CG  1 
ATOM   4744  C  CG  B LEU C  1 46  ? 14.376  19.560  20.862  0.50 16.18 ? 46  LEU C CG  1 
ATOM   4745  C  CD1 A LEU C  1 46  ? 15.259  19.354  21.728  0.50 11.23 ? 46  LEU C CD1 1 
ATOM   4746  C  CD1 B LEU C  1 46  ? 14.404  18.050  20.654  0.50 18.35 ? 46  LEU C CD1 1 
ATOM   4747  C  CD2 A LEU C  1 46  ? 12.832  20.059  21.436  0.50 8.83  ? 46  LEU C CD2 1 
ATOM   4748  C  CD2 B LEU C  1 46  ? 15.429  19.994  21.841  0.50 14.63 ? 46  LEU C CD2 1 
ATOM   4749  N  N   . GLU C  1 47  ? 13.506  22.251  17.345  1.00 12.38 ? 47  GLU C N   1 
ATOM   4750  C  CA  . GLU C  1 47  ? 14.030  23.319  16.500  1.00 14.54 ? 47  GLU C CA  1 
ATOM   4751  C  C   . GLU C  1 47  ? 14.830  24.307  17.327  1.00 11.31 ? 47  GLU C C   1 
ATOM   4752  O  O   . GLU C  1 47  ? 14.355  24.761  18.373  1.00 13.58 ? 47  GLU C O   1 
ATOM   4753  C  CB  . GLU C  1 47  ? 12.902  24.060  15.801  1.00 18.05 ? 47  GLU C CB  1 
ATOM   4754  C  CG  . GLU C  1 47  ? 12.083  23.149  14.970  1.00 29.64 ? 47  GLU C CG  1 
ATOM   4755  C  CD  . GLU C  1 47  ? 12.485  23.160  13.556  1.00 42.00 ? 47  GLU C CD  1 
ATOM   4756  O  OE1 . GLU C  1 47  ? 13.652  23.547  13.265  1.00 46.88 ? 47  GLU C OE1 1 
ATOM   4757  O  OE2 . GLU C  1 47  ? 11.608  22.806  12.732  1.00 50.16 ? 47  GLU C OE2 1 
ATOM   4758  N  N   . PHE C  1 48  ? 16.042  24.564  16.872  1.00 13.32 ? 48  PHE C N   1 
ATOM   4759  C  CA  . PHE C  1 48  ? 17.009  25.364  17.525  1.00 13.92 ? 48  PHE C CA  1 
ATOM   4760  C  C   . PHE C  1 48  ? 16.903  26.729  16.851  1.00 16.33 ? 48  PHE C C   1 
ATOM   4761  O  O   . PHE C  1 48  ? 17.377  26.860  15.674  1.00 19.49 ? 48  PHE C O   1 
ATOM   4762  C  CB  . PHE C  1 48  ? 18.386  24.762  17.353  1.00 13.79 ? 48  PHE C CB  1 
ATOM   4763  C  CG  . PHE C  1 48  ? 18.370  23.261  17.704  1.00 12.42 ? 48  PHE C CG  1 
ATOM   4764  C  CD1 . PHE C  1 48  ? 18.438  22.289  16.718  1.00 13.04 ? 48  PHE C CD1 1 
ATOM   4765  C  CD2 . PHE C  1 48  ? 18.322  22.850  19.020  1.00 12.66 ? 48  PHE C CD2 1 
ATOM   4766  C  CE1 . PHE C  1 48  ? 18.440  20.951  17.057  1.00 11.83 ? 48  PHE C CE1 1 
ATOM   4767  C  CE2 . PHE C  1 48  ? 18.252  21.527  19.355  1.00 13.29 ? 48  PHE C CE2 1 
ATOM   4768  C  CZ  . PHE C  1 48  ? 18.348  20.563  18.392  1.00 9.82  ? 48  PHE C CZ  1 
ATOM   4769  N  N   . GLN C  1 49  ? 16.335  27.703  17.592  1.00 12.81 ? 49  GLN C N   1 
ATOM   4770  C  CA  . GLN C  1 49  ? 16.056  29.033  17.037  1.00 13.55 ? 49  GLN C CA  1 
ATOM   4771  C  C   . GLN C  1 49  ? 16.915  30.070  17.658  1.00 11.42 ? 49  GLN C C   1 
ATOM   4772  O  O   . GLN C  1 49  ? 17.102  30.088  18.874  1.00 10.00 ? 49  GLN C O   1 
ATOM   4773  C  CB  . GLN C  1 49  ? 14.616  29.391  17.255  1.00 15.42 ? 49  GLN C CB  1 
ATOM   4774  C  CG  . GLN C  1 49  ? 13.815  28.352  16.555  1.00 17.69 ? 49  GLN C CG  1 
ATOM   4775  C  CD  . GLN C  1 49  ? 12.342  28.694  16.331  1.00 25.07 ? 49  GLN C CD  1 
ATOM   4776  O  OE1 . GLN C  1 49  ? 11.716  29.457  17.117  1.00 25.63 ? 49  GLN C OE1 1 
ATOM   4777  N  NE2 . GLN C  1 49  ? 11.747  28.081  15.257  1.00 28.18 ? 49  GLN C NE2 1 
ATOM   4778  N  N   . GLY C  1 50  ? 17.534  30.900  16.807  1.00 11.35 ? 50  GLY C N   1 
ATOM   4779  C  CA  . GLY C  1 50  ? 18.434  31.971  17.292  1.00 9.81  ? 50  GLY C CA  1 
ATOM   4780  C  C   . GLY C  1 50  ? 19.752  31.411  17.832  1.00 11.07 ? 50  GLY C C   1 
ATOM   4781  O  O   . GLY C  1 50  ? 20.492  32.071  18.569  1.00 10.06 ? 50  GLY C O   1 
ATOM   4782  N  N   . TYR C  1 51  ? 20.060  30.160  17.427  1.00 8.59  ? 51  TYR C N   1 
ATOM   4783  C  CA  . TYR C  1 51  ? 21.423  29.560  17.800  1.00 9.02  ? 51  TYR C CA  1 
ATOM   4784  C  C   . TYR C  1 51  ? 22.578  30.144  17.001  1.00 10.85 ? 51  TYR C C   1 
ATOM   4785  O  O   . TYR C  1 51  ? 23.724  30.040  17.435  1.00 9.76  ? 51  TYR C O   1 
ATOM   4786  C  CB  . TYR C  1 51  ? 21.420  28.019  17.638  1.00 9.14  ? 51  TYR C CB  1 
ATOM   4787  C  CG  . TYR C  1 51  ? 20.825  27.195  18.770  1.00 9.11  ? 51  TYR C CG  1 
ATOM   4788  C  CD1 . TYR C  1 51  ? 19.641  27.530  19.457  1.00 7.70  ? 51  TYR C CD1 1 
ATOM   4789  C  CD2 . TYR C  1 51  ? 21.543  26.089  19.245  1.00 8.49  ? 51  TYR C CD2 1 
ATOM   4790  C  CE1 . TYR C  1 51  ? 19.161  26.779  20.517  1.00 8.13  ? 51  TYR C CE1 1 
ATOM   4791  C  CE2 . TYR C  1 51  ? 21.097  25.354  20.310  1.00 7.63  ? 51  TYR C CE2 1 
ATOM   4792  C  CZ  . TYR C  1 51  ? 19.925  25.691  20.968  1.00 9.14  ? 51  TYR C CZ  1 
ATOM   4793  O  OH  . TYR C  1 51  ? 19.534  24.978  22.113  1.00 9.08  ? 51  TYR C OH  1 
ATOM   4794  N  N   . ASN C  1 52  ? 22.289  30.741  15.826  1.00 9.64  ? 52  ASN C N   1 
ATOM   4795  C  CA  . ASN C  1 52  ? 23.408  31.333  15.037  1.00 10.78 ? 52  ASN C CA  1 
ATOM   4796  C  C   . ASN C  1 52  ? 23.683  32.713  15.586  1.00 12.99 ? 52  ASN C C   1 
ATOM   4797  O  O   . ASN C  1 52  ? 23.216  33.767  15.055  1.00 12.99 ? 52  ASN C O   1 
ATOM   4798  C  CB  . ASN C  1 52  ? 22.970  31.378  13.573  1.00 12.44 ? 52  ASN C CB  1 
ATOM   4799  C  CG  . ASN C  1 52  ? 24.106  31.808  12.698  1.00 16.29 ? 52  ASN C CG  1 
ATOM   4800  O  OD1 . ASN C  1 52  ? 25.299  31.664  13.051  1.00 16.53 ? 52  ASN C OD1 1 
ATOM   4801  N  ND2 . ASN C  1 52  ? 23.754  32.331  11.500  1.00 24.38 ? 52  ASN C ND2 1 
ATOM   4802  N  N   . LEU C  1 53  ? 24.400  32.779  16.713  1.00 10.90 ? 53  LEU C N   1 
ATOM   4803  C  CA  . LEU C  1 53  ? 24.695  34.036  17.455  1.00 12.02 ? 53  LEU C CA  1 
ATOM   4804  C  C   . LEU C  1 53  ? 25.481  35.009  16.537  1.00 12.03 ? 53  LEU C C   1 
ATOM   4805  O  O   . LEU C  1 53  ? 26.431  34.593  15.804  1.00 14.00 ? 53  LEU C O   1 
ATOM   4806  C  CB  . LEU C  1 53  ? 25.484  33.740  18.738  1.00 10.35 ? 53  LEU C CB  1 
ATOM   4807  C  CG  . LEU C  1 53  ? 24.861  32.659  19.624  1.00 11.36 ? 53  LEU C CG  1 
ATOM   4808  C  CD1 . LEU C  1 53  ? 25.775  32.545  20.920  1.00 11.64 ? 53  LEU C CD1 1 
ATOM   4809  C  CD2 . LEU C  1 53  ? 23.450  33.146  20.052  1.00 11.45 ? 53  LEU C CD2 1 
ATOM   4810  N  N   . SER C  1 54  ? 25.104  36.272  16.640  1.00 12.15 ? 54  SER C N   1 
ATOM   4811  C  CA  . SER C  1 54  ? 25.747  37.271  15.789  1.00 13.71 ? 54  SER C CA  1 
ATOM   4812  C  C   . SER C  1 54  ? 27.243  37.341  16.064  1.00 11.99 ? 54  SER C C   1 
ATOM   4813  O  O   . SER C  1 54  ? 27.702  37.450  17.158  1.00 10.82 ? 54  SER C O   1 
ATOM   4814  C  CB  . SER C  1 54  ? 25.166  38.577  16.172  1.00 14.29 ? 54  SER C CB  1 
ATOM   4815  O  OG  . SER C  1 54  ? 25.751  39.561  15.353  1.00 16.55 ? 54  SER C OG  1 
ATOM   4816  N  N   . ALA C  1 55  ? 27.962  37.251  14.986  1.00 12.72 ? 55  ALA C N   1 
ATOM   4817  C  CA  . ALA C  1 55  ? 29.470  37.313  15.005  1.00 12.23 ? 55  ALA C CA  1 
ATOM   4818  C  C   . ALA C  1 55  ? 29.890  38.728  15.410  1.00 12.26 ? 55  ALA C C   1 
ATOM   4819  O  O   . ALA C  1 55  ? 31.073  38.964  15.797  1.00 14.75 ? 55  ALA C O   1 
ATOM   4820  C  CB  . ALA C  1 55  ? 30.118  36.952  13.591  1.00 13.07 ? 55  ALA C CB  1 
ATOM   4821  N  N   . ASN C  1 56  ? 28.914  39.664  15.332  1.00 13.21 ? 56  ASN C N   1 
ATOM   4822  C  CA  . ASN C  1 56  ? 29.218  41.044  15.683  1.00 12.14 ? 56  ASN C CA  1 
ATOM   4823  C  C   . ASN C  1 56  ? 28.967  41.316  17.150  1.00 15.70 ? 56  ASN C C   1 
ATOM   4824  O  O   . ASN C  1 56  ? 29.195  42.409  17.602  1.00 18.09 ? 56  ASN C O   1 
ATOM   4825  C  CB  . ASN C  1 56  ? 28.448  42.038  14.776  1.00 14.34 ? 56  ASN C CB  1 
ATOM   4826  C  CG  . ASN C  1 56  ? 28.872  41.930  13.275  1.00 17.27 ? 56  ASN C CG  1 
ATOM   4827  O  OD1 . ASN C  1 56  ? 30.021  41.603  12.941  1.00 19.63 ? 56  ASN C OD1 1 
ATOM   4828  N  ND2 . ASN C  1 56  ? 27.902  42.119  12.383  1.00 20.36 ? 56  ASN C ND2 1 
ATOM   4829  N  N   . LYS C  1 57  ? 28.475  40.274  17.878  1.00 12.84 ? 57  LYS C N   1 
ATOM   4830  C  CA  . LYS C  1 57  ? 28.195  40.390  19.293  1.00 14.42 ? 57  LYS C CA  1 
ATOM   4831  C  C   . LYS C  1 57  ? 29.295  39.572  20.010  1.00 11.44 ? 57  LYS C C   1 
ATOM   4832  O  O   . LYS C  1 57  ? 30.022  38.730  19.369  1.00 12.90 ? 57  LYS C O   1 
ATOM   4833  C  CB  . LYS C  1 57  ? 26.818  39.786  19.643  1.00 14.48 ? 57  LYS C CB  1 
ATOM   4834  C  CG  . LYS C  1 57  ? 25.668  40.728  19.524  1.00 20.74 ? 57  LYS C CG  1 
ATOM   4835  C  CD  . LYS C  1 57  ? 24.399  40.114  20.214  1.00 21.01 ? 57  LYS C CD  1 
ATOM   4836  C  CE  . LYS C  1 57  ? 24.310  40.048  21.717  1.00 22.24 ? 57  LYS C CE  1 
ATOM   4837  N  NZ  . LYS C  1 57  ? 22.823  39.737  22.179  1.00 20.99 ? 57  LYS C NZ  1 
ATOM   4838  N  N   . GLN C  1 58  ? 29.443  39.855  21.298  1.00 10.81 ? 58  GLN C N   1 
ATOM   4839  C  CA  . GLN C  1 58  ? 30.380  39.086  22.175  1.00 11.83 ? 58  GLN C CA  1 
ATOM   4840  C  C   . GLN C  1 58  ? 29.678  38.571  23.415  1.00 11.38 ? 58  GLN C C   1 
ATOM   4841  O  O   . GLN C  1 58  ? 28.803  39.226  23.935  1.00 12.60 ? 58  GLN C O   1 
ATOM   4842  C  CB  . GLN C  1 58  ? 31.581  39.892  22.634  1.00 15.69 ? 58  GLN C CB  1 
ATOM   4843  C  CG  . GLN C  1 58  ? 32.320  40.526  21.549  1.00 22.45 ? 58  GLN C CG  1 
ATOM   4844  C  CD  . GLN C  1 58  ? 33.249  41.575  22.186  1.00 22.89 ? 58  GLN C CD  1 
ATOM   4845  O  OE1 . GLN C  1 58  ? 32.837  42.485  22.944  1.00 30.36 ? 58  GLN C OE1 1 
ATOM   4846  N  NE2 . GLN C  1 58  ? 34.463  41.410  21.950  1.00 19.92 ? 58  GLN C NE2 1 
ATOM   4847  N  N   . PHE C  1 59  ? 30.046  37.345  23.852  1.00 9.09  ? 59  PHE C N   1 
ATOM   4848  C  CA  . PHE C  1 59  ? 29.295  36.620  24.921  1.00 8.77  ? 59  PHE C CA  1 
ATOM   4849  C  C   . PHE C  1 59  ? 30.307  36.305  26.004  1.00 8.36  ? 59  PHE C C   1 
ATOM   4850  O  O   . PHE C  1 59  ? 31.475  35.927  25.730  1.00 9.08  ? 59  PHE C O   1 
ATOM   4851  C  CB  . PHE C  1 59  ? 28.623  35.369  24.300  1.00 7.97  ? 59  PHE C CB  1 
ATOM   4852  C  CG  . PHE C  1 59  ? 27.644  35.733  23.274  1.00 7.81  ? 59  PHE C CG  1 
ATOM   4853  C  CD1 . PHE C  1 59  ? 27.975  35.924  21.926  1.00 9.67  ? 59  PHE C CD1 1 
ATOM   4854  C  CD2 . PHE C  1 59  ? 26.316  36.020  23.707  1.00 10.61 ? 59  PHE C CD2 1 
ATOM   4855  C  CE1 . PHE C  1 59  ? 27.058  36.379  21.034  1.00 8.90  ? 59  PHE C CE1 1 
ATOM   4856  C  CE2 . PHE C  1 59  ? 25.410  36.498  22.777  1.00 11.29 ? 59  PHE C CE2 1 
ATOM   4857  C  CZ  . PHE C  1 59  ? 25.728  36.624  21.442  1.00 13.03 ? 59  PHE C CZ  1 
ATOM   4858  N  N   . LEU C  1 60  ? 29.922  36.365  27.265  1.00 10.09 ? 60  LEU C N   1 
ATOM   4859  C  CA  . LEU C  1 60  ? 30.840  36.225  28.403  1.00 8.72  ? 60  LEU C CA  1 
ATOM   4860  C  C   . LEU C  1 60  ? 31.122  34.771  28.749  1.00 10.00 ? 60  LEU C C   1 
ATOM   4861  O  O   . LEU C  1 60  ? 30.192  34.034  28.952  1.00 8.85  ? 60  LEU C O   1 
ATOM   4862  C  CB  . LEU C  1 60  ? 30.172  36.956  29.649  1.00 9.91  ? 60  LEU C CB  1 
ATOM   4863  C  CG  . LEU C  1 60  ? 31.076  37.218  30.772  1.00 11.83 ? 60  LEU C CG  1 
ATOM   4864  C  CD1 . LEU C  1 60  ? 32.154  38.245  30.384  1.00 15.32 ? 60  LEU C CD1 1 
ATOM   4865  C  CD2 . LEU C  1 60  ? 30.293  37.605  32.013  1.00 13.65 ? 60  LEU C CD2 1 
ATOM   4866  N  N   . LEU C  1 61  ? 32.388  34.403  28.849  1.00 9.14  ? 61  LEU C N   1 
ATOM   4867  C  CA  . LEU C  1 61  ? 32.883  33.077  29.229  1.00 9.15  ? 61  LEU C CA  1 
ATOM   4868  C  C   . LEU C  1 61  ? 33.425  33.266  30.647  1.00 9.08  ? 61  LEU C C   1 
ATOM   4869  O  O   . LEU C  1 61  ? 34.226  34.209  30.919  1.00 10.34 ? 61  LEU C O   1 
ATOM   4870  C  CB  . LEU C  1 61  ? 33.972  32.609  28.242  1.00 9.49  ? 61  LEU C CB  1 
ATOM   4871  C  CG  . LEU C  1 61  ? 34.473  31.220  28.534  1.00 10.26 ? 61  LEU C CG  1 
ATOM   4872  C  CD1 . LEU C  1 61  ? 33.452  30.184  28.037  1.00 9.54  ? 61  LEU C CD1 1 
ATOM   4873  C  CD2 . LEU C  1 61  ? 35.846  30.973  27.778  1.00 10.95 ? 61  LEU C CD2 1 
ATOM   4874  N  N   . THR C  1 62  ? 32.992  32.478  31.610  1.00 7.46  ? 62  THR C N   1 
ATOM   4875  C  CA  . THR C  1 62  ? 33.386  32.702  32.997  1.00 8.73  ? 62  THR C CA  1 
ATOM   4876  C  C   . THR C  1 62  ? 33.818  31.366  33.601  1.00 9.75  ? 62  THR C C   1 
ATOM   4877  O  O   . THR C  1 62  ? 33.127  30.290  33.420  1.00 9.11  ? 62  THR C O   1 
ATOM   4878  C  CB  . THR C  1 62  ? 32.143  33.164  33.867  1.00 10.01 ? 62  THR C CB  1 
ATOM   4879  O  OG1 . THR C  1 62  ? 31.591  34.377  33.274  1.00 13.49 ? 62  THR C OG1 1 
ATOM   4880  C  CG2 . THR C  1 62  ? 32.595  33.422  35.325  1.00 13.13 ? 62  THR C CG2 1 
ATOM   4881  N  N   . ASN C  1 63  ? 34.900  31.349  34.336  1.00 8.11  ? 63  ASN C N   1 
ATOM   4882  C  CA  . ASN C  1 63  ? 35.240  30.257  35.241  1.00 9.50  ? 63  ASN C CA  1 
ATOM   4883  C  C   . ASN C  1 63  ? 34.501  30.531  36.552  1.00 10.37 ? 63  ASN C C   1 
ATOM   4884  O  O   . ASN C  1 63  ? 34.794  31.459  37.246  1.00 10.19 ? 63  ASN C O   1 
ATOM   4885  C  CB  . ASN C  1 63  ? 36.791  30.187  35.413  1.00 7.34  ? 63  ASN C CB  1 
ATOM   4886  C  CG  . ASN C  1 63  ? 37.249  29.159  36.422  1.00 8.41  ? 63  ASN C CG  1 
ATOM   4887  O  OD1 . ASN C  1 63  ? 36.469  28.793  37.374  1.00 8.58  ? 63  ASN C OD1 1 
ATOM   4888  N  ND2 . ASN C  1 63  ? 38.511  28.691  36.343  1.00 9.41  ? 63  ASN C ND2 1 
ATOM   4889  N  N   . ASN C  1 64  ? 33.540  29.656  36.884  1.00 9.77  ? 64  ASN C N   1 
ATOM   4890  C  CA  . ASN C  1 64  ? 32.692  29.913  38.113  1.00 10.55 ? 64  ASN C CA  1 
ATOM   4891  C  C   . ASN C  1 64  ? 33.135  29.090  39.316  1.00 10.75 ? 64  ASN C C   1 
ATOM   4892  O  O   . ASN C  1 64  ? 32.421  28.981  40.307  1.00 12.92 ? 64  ASN C O   1 
ATOM   4893  C  CB  . ASN C  1 64  ? 31.217  29.676  37.785  1.00 11.68 ? 64  ASN C CB  1 
ATOM   4894  C  CG  . ASN C  1 64  ? 30.889  28.233  37.527  1.00 11.70 ? 64  ASN C CG  1 
ATOM   4895  O  OD1 . ASN C  1 64  ? 31.714  27.353  37.606  1.00 10.51 ? 64  ASN C OD1 1 
ATOM   4896  N  ND2 . ASN C  1 64  ? 29.644  27.998  37.070  1.00 15.69 ? 64  ASN C ND2 1 
ATOM   4897  N  N   . GLY C  1 65  ? 34.318  28.475  39.255  1.00 10.59 ? 65  GLY C N   1 
ATOM   4898  C  CA  . GLY C  1 65  ? 34.904  27.637  40.294  1.00 9.56  ? 65  GLY C CA  1 
ATOM   4899  C  C   . GLY C  1 65  ? 34.373  26.150  40.259  1.00 7.83  ? 65  GLY C C   1 
ATOM   4900  O  O   . GLY C  1 65  ? 34.986  25.318  40.952  1.00 9.78  ? 65  GLY C O   1 
ATOM   4901  N  N   . HIS C  1 66  ? 33.387  25.848  39.308  1.00 10.24 ? 66  HIS C N   1 
ATOM   4902  C  CA  . HIS C  1 66  ? 32.899  24.416  39.173  1.00 10.37 ? 66  HIS C CA  1 
ATOM   4903  C  C   . HIS C  1 66  ? 32.976  23.966  37.749  1.00 10.27 ? 66  HIS C C   1 
ATOM   4904  O  O   . HIS C  1 66  ? 33.051  22.752  37.471  1.00 8.42  ? 66  HIS C O   1 
ATOM   4905  C  CB  . HIS C  1 66  ? 31.439  24.346  39.669  1.00 11.50 ? 66  HIS C CB  1 
ATOM   4906  C  CG  . HIS C  1 66  ? 31.332  24.757  41.141  1.00 11.21 ? 66  HIS C CG  1 
ATOM   4907  N  ND1 . HIS C  1 66  ? 31.789  23.918  42.149  1.00 15.84 ? 66  HIS C ND1 1 
ATOM   4908  C  CD2 . HIS C  1 66  ? 30.698  25.800  41.764  1.00 15.90 ? 66  HIS C CD2 1 
ATOM   4909  C  CE1 . HIS C  1 66  ? 31.496  24.468  43.322  1.00 16.94 ? 66  HIS C CE1 1 
ATOM   4910  N  NE2 . HIS C  1 66  ? 30.837  25.595  43.102  1.00 14.92 ? 66  HIS C NE2 1 
ATOM   4911  N  N   . SER C  1 67  ? 32.952  24.916  36.795  1.00 8.38  ? 67  SER C N   1 
ATOM   4912  C  CA  . SER C  1 67  ? 32.961  24.586  35.377  1.00 8.61  ? 67  SER C CA  1 
ATOM   4913  C  C   . SER C  1 67  ? 33.437  25.851  34.639  1.00 8.98  ? 67  SER C C   1 
ATOM   4914  O  O   . SER C  1 67  ? 33.739  26.906  35.321  1.00 8.74  ? 67  SER C O   1 
ATOM   4915  C  CB  . SER C  1 67  ? 31.585  24.133  34.839  1.00 8.69  ? 67  SER C CB  1 
ATOM   4916  O  OG  . SER C  1 67  ? 31.636  23.718  33.457  1.00 8.00  ? 67  SER C OG  1 
ATOM   4917  N  N   . VAL C  1 68  ? 33.441  25.747  33.318  1.00 8.07  ? 68  VAL C N   1 
ATOM   4918  C  CA  . VAL C  1 68  ? 33.599  26.995  32.540  1.00 8.35  ? 68  VAL C CA  1 
ATOM   4919  C  C   . VAL C  1 68  ? 32.280  27.168  31.755  1.00 8.00  ? 68  VAL C C   1 
ATOM   4920  O  O   . VAL C  1 68  ? 31.712  26.197  31.174  1.00 8.36  ? 68  VAL C O   1 
ATOM   4921  C  CB  . VAL C  1 68  ? 34.791  26.894  31.552  1.00 9.08  ? 68  VAL C CB  1 
ATOM   4922  C  CG1 . VAL C  1 68  ? 34.718  25.719  30.550  1.00 10.29 ? 68  VAL C CG1 1 
ATOM   4923  C  CG2 . VAL C  1 68  ? 35.009  28.249  30.891  1.00 9.75  ? 68  VAL C CG2 1 
ATOM   4924  N  N   . LYS C  1 69  ? 31.683  28.366  31.866  1.00 8.23  ? 69  LYS C N   1 
ATOM   4925  C  CA  . LYS C  1 69  ? 30.313  28.588  31.299  1.00 8.00  ? 69  LYS C CA  1 
ATOM   4926  C  C   . LYS C  1 69  ? 30.345  29.760  30.277  1.00 7.93  ? 69  LYS C C   1 
ATOM   4927  O  O   . LYS C  1 69  ? 31.102  30.716  30.525  1.00 8.38  ? 69  LYS C O   1 
ATOM   4928  C  CB  . LYS C  1 69  ? 29.253  28.790  32.395  1.00 11.34 ? 69  LYS C CB  1 
ATOM   4929  C  CG  . LYS C  1 69  ? 29.447  30.053  33.133  1.00 13.64 ? 69  LYS C CG  1 
ATOM   4930  C  CD  . LYS C  1 69  ? 28.054  30.284  33.911  1.00 15.93 ? 69  LYS C CD  1 
ATOM   4931  C  CE  . LYS C  1 69  ? 28.278  31.553  34.709  1.00 17.36 ? 69  LYS C CE  1 
ATOM   4932  N  NZ  . LYS C  1 69  ? 26.991  31.966  35.503  1.00 14.58 ? 69  LYS C NZ  1 
ATOM   4933  N  N   . LEU C  1 70  ? 29.563  29.670  29.219  1.00 6.80  ? 70  LEU C N   1 
ATOM   4934  C  CA  . LEU C  1 70  ? 29.348  30.758  28.289  1.00 6.78  ? 70  LEU C CA  1 
ATOM   4935  C  C   . LEU C  1 70  ? 27.904  31.255  28.426  1.00 6.45  ? 70  LEU C C   1 
ATOM   4936  O  O   . LEU C  1 70  ? 26.952  30.443  28.365  1.00 7.04  ? 70  LEU C O   1 
ATOM   4937  C  CB  . LEU C  1 70  ? 29.570  30.261  26.893  1.00 6.55  ? 70  LEU C CB  1 
ATOM   4938  C  CG  . LEU C  1 70  ? 29.372  31.218  25.721  1.00 6.79  ? 70  LEU C CG  1 
ATOM   4939  C  CD1 . LEU C  1 70  ? 30.509  32.312  25.774  1.00 8.49  ? 70  LEU C CD1 1 
ATOM   4940  C  CD2 . LEU C  1 70  ? 29.372  30.492  24.345  1.00 8.07  ? 70  LEU C CD2 1 
ATOM   4941  N  N   . ASN C  1 71  ? 27.721  32.564  28.702  1.00 7.71  ? 71  ASN C N   1 
ATOM   4942  C  CA  . ASN C  1 71  ? 26.399  33.078  28.770  1.00 7.52  ? 71  ASN C CA  1 
ATOM   4943  C  C   . ASN C  1 71  ? 25.756  33.181  27.404  1.00 6.42  ? 71  ASN C C   1 
ATOM   4944  O  O   . ASN C  1 71  ? 26.490  33.420  26.376  1.00 8.97  ? 71  ASN C O   1 
ATOM   4945  C  CB  . ASN C  1 71  ? 26.458  34.543  29.390  1.00 8.04  ? 71  ASN C CB  1 
ATOM   4946  C  CG  . ASN C  1 71  ? 26.774  34.511  30.853  1.00 11.45 ? 71  ASN C CG  1 
ATOM   4947  O  OD1 . ASN C  1 71  ? 26.784  33.511  31.547  1.00 14.78 ? 71  ASN C OD1 1 
ATOM   4948  N  ND2 . ASN C  1 71  ? 27.096  35.769  31.387  1.00 18.89 ? 71  ASN C ND2 1 
ATOM   4949  N  N   . LEU C  1 72  ? 24.490  32.806  27.309  1.00 7.40  ? 72  LEU C N   1 
ATOM   4950  C  CA  . LEU C  1 72  ? 23.784  32.855  26.067  1.00 8.02  ? 72  LEU C CA  1 
ATOM   4951  C  C   . LEU C  1 72  ? 22.563  33.794  26.150  1.00 8.93  ? 72  LEU C C   1 
ATOM   4952  O  O   . LEU C  1 72  ? 22.015  34.029  27.235  1.00 8.47  ? 72  LEU C O   1 
ATOM   4953  C  CB  . LEU C  1 72  ? 23.216  31.429  25.738  1.00 8.46  ? 72  LEU C CB  1 
ATOM   4954  C  CG  . LEU C  1 72  ? 24.314  30.300  25.665  1.00 7.32  ? 72  LEU C CG  1 
ATOM   4955  C  CD1 . LEU C  1 72  ? 23.687  28.986  25.685  1.00 8.21  ? 72  LEU C CD1 1 
ATOM   4956  C  CD2 . LEU C  1 72  ? 25.080  30.499  24.336  1.00 7.66  ? 72  LEU C CD2 1 
ATOM   4957  N  N   . PRO C  1 73  ? 22.165  34.331  24.998  1.00 9.42  ? 73  PRO C N   1 
ATOM   4958  C  CA  . PRO C  1 73  ? 21.109  35.416  25.033  1.00 9.03  ? 73  PRO C CA  1 
ATOM   4959  C  C   . PRO C  1 73  ? 19.740  34.838  25.050  1.00 10.67 ? 73  PRO C C   1 
ATOM   4960  O  O   . PRO C  1 73  ? 19.431  33.776  24.476  1.00 10.28 ? 73  PRO C O   1 
ATOM   4961  C  CB  . PRO C  1 73  ? 21.420  36.206  23.740  1.00 11.10 ? 73  PRO C CB  1 
ATOM   4962  C  CG  . PRO C  1 73  ? 21.852  35.083  22.758  1.00 11.00 ? 73  PRO C CG  1 
ATOM   4963  C  CD  . PRO C  1 73  ? 22.718  34.101  23.643  1.00 9.48  ? 73  PRO C CD  1 
ATOM   4964  N  N   . SER C  1 74  ? 18.852  35.613  25.673  1.00 11.91 ? 74  SER C N   1 
ATOM   4965  C  CA  . SER C  1 74  ? 17.535  34.996  25.861  1.00 15.02 ? 74  SER C CA  1 
ATOM   4966  C  C   . SER C  1 74  ? 16.675  34.917  24.599  1.00 12.39 ? 74  SER C C   1 
ATOM   4967  O  O   . SER C  1 74  ? 15.614  34.240  24.567  1.00 15.13 ? 74  SER C O   1 
ATOM   4968  C  CB  . SER C  1 74  ? 16.822  35.674  27.046  1.00 17.50 ? 74  SER C CB  1 
ATOM   4969  O  OG  . SER C  1 74  ? 16.486  36.950  26.578  1.00 17.68 ? 74  SER C OG  1 
ATOM   4970  N  N   . ASP C  1 75  ? 17.130  35.522  23.469  1.00 13.13 ? 75  ASP C N   1 
ATOM   4971  C  CA  . ASP C  1 75  ? 16.440  35.337  22.225  1.00 11.50 ? 75  ASP C CA  1 
ATOM   4972  C  C   . ASP C  1 75  ? 16.751  33.960  21.540  1.00 11.76 ? 75  ASP C C   1 
ATOM   4973  O  O   . ASP C  1 75  ? 16.094  33.547  20.585  1.00 12.70 ? 75  ASP C O   1 
ATOM   4974  C  CB  . ASP C  1 75  ? 16.752  36.449  21.179  1.00 11.94 ? 75  ASP C CB  1 
ATOM   4975  C  CG  . ASP C  1 75  ? 18.232  36.412  20.731  1.00 11.51 ? 75  ASP C CG  1 
ATOM   4976  O  OD1 . ASP C  1 75  ? 19.051  36.766  21.538  1.00 15.40 ? 75  ASP C OD1 1 
ATOM   4977  O  OD2 . ASP C  1 75  ? 18.512  36.111  19.587  1.00 15.25 ? 75  ASP C OD2 1 
ATOM   4978  N  N   . MET C  1 76  ? 17.782  33.185  21.997  1.00 8.79  ? 76  MET C N   1 
ATOM   4979  C  CA  . MET C  1 76  ? 18.035  31.842  21.598  1.00 8.28  ? 76  MET C CA  1 
ATOM   4980  C  C   . MET C  1 76  ? 17.079  30.855  22.362  1.00 6.93  ? 76  MET C C   1 
ATOM   4981  O  O   . MET C  1 76  ? 16.864  31.060  23.563  1.00 9.03  ? 76  MET C O   1 
ATOM   4982  C  CB  . MET C  1 76  ? 19.469  31.572  22.043  1.00 10.03 ? 76  MET C CB  1 
ATOM   4983  C  CG  . MET C  1 76  ? 19.915  30.177  21.761  1.00 9.44  ? 76  MET C CG  1 
ATOM   4984  S  SD  . MET C  1 76  ? 21.745  30.115  22.141  1.00 9.86  ? 76  MET C SD  1 
ATOM   4985  C  CE  . MET C  1 76  ? 21.927  28.334  22.254  1.00 9.03  ? 76  MET C CE  1 
ATOM   4986  N  N   . HIS C  1 77  ? 16.455  29.953  21.644  1.00 7.50  ? 77  HIS C N   1 
ATOM   4987  C  CA  . HIS C  1 77  ? 15.452  29.094  22.287  1.00 10.17 ? 77  HIS C CA  1 
ATOM   4988  C  C   . HIS C  1 77  ? 15.240  27.789  21.573  1.00 10.15 ? 77  HIS C C   1 
ATOM   4989  O  O   . HIS C  1 77  ? 15.620  27.597  20.387  1.00 10.33 ? 77  HIS C O   1 
ATOM   4990  C  CB  . HIS C  1 77  ? 14.105  29.823  22.541  1.00 13.13 ? 77  HIS C CB  1 
ATOM   4991  C  CG  . HIS C  1 77  ? 13.492  30.321  21.285  1.00 14.97 ? 77  HIS C CG  1 
ATOM   4992  N  ND1 . HIS C  1 77  ? 13.545  31.640  20.906  1.00 17.11 ? 77  HIS C ND1 1 
ATOM   4993  C  CD2 . HIS C  1 77  ? 12.802  29.670  20.326  1.00 18.32 ? 77  HIS C CD2 1 
ATOM   4994  C  CE1 . HIS C  1 77  ? 12.928  31.782  19.748  1.00 17.38 ? 77  HIS C CE1 1 
ATOM   4995  N  NE2 . HIS C  1 77  ? 12.470  30.606  19.362  1.00 17.61 ? 77  HIS C NE2 1 
ATOM   4996  N  N   A ILE C  1 78  ? 14.710  26.830  22.299  0.40 10.16 ? 78  ILE C N   1 
ATOM   4997  N  N   B ILE C  1 78  ? 14.611  26.903  22.336  0.60 10.54 ? 78  ILE C N   1 
ATOM   4998  C  CA  A ILE C  1 78  ? 14.203  25.624  21.612  0.40 9.79  ? 78  ILE C CA  1 
ATOM   4999  C  CA  B ILE C  1 78  ? 14.093  25.575  21.838  0.60 12.38 ? 78  ILE C CA  1 
ATOM   5000  C  C   A ILE C  1 78  ? 12.698  25.842  21.484  0.40 12.16 ? 78  ILE C C   1 
ATOM   5001  C  C   B ILE C  1 78  ? 12.599  25.654  21.592  0.60 14.18 ? 78  ILE C C   1 
ATOM   5002  O  O   A ILE C  1 78  ? 12.055  26.451  22.380  0.40 9.53  ? 78  ILE C O   1 
ATOM   5003  O  O   B ILE C  1 78  ? 11.870  25.996  22.540  0.60 14.95 ? 78  ILE C O   1 
ATOM   5004  C  CB  A ILE C  1 78  ? 14.415  24.316  22.432  0.40 10.44 ? 78  ILE C CB  1 
ATOM   5005  C  CB  B ILE C  1 78  ? 14.263  24.453  22.953  0.60 12.17 ? 78  ILE C CB  1 
ATOM   5006  C  CG1 A ILE C  1 78  ? 15.860  24.050  22.894  0.40 13.36 ? 78  ILE C CG1 1 
ATOM   5007  C  CG1 B ILE C  1 78  ? 15.731  24.087  23.011  0.60 17.23 ? 78  ILE C CG1 1 
ATOM   5008  C  CG2 A ILE C  1 78  ? 13.720  23.135  21.707  0.40 9.35  ? 78  ILE C CG2 1 
ATOM   5009  C  CG2 B ILE C  1 78  ? 13.370  23.230  22.533  0.60 13.49 ? 78  ILE C CG2 1 
ATOM   5010  C  CD1 A ILE C  1 78  ? 15.833  23.197  24.233  0.40 8.49  ? 78  ILE C CD1 1 
ATOM   5011  C  CD1 B ILE C  1 78  ? 16.270  24.127  21.656  0.60 11.10 ? 78  ILE C CD1 1 
ATOM   5012  N  N   . GLN C  1 79  ? 12.226  25.352  20.341  1.00 13.99 ? 79  GLN C N   1 
ATOM   5013  C  CA  . GLN C  1 79  ? 10.872  25.224  19.884  1.00 16.58 ? 79  GLN C CA  1 
ATOM   5014  C  C   . GLN C  1 79  ? 10.595  23.727  19.708  1.00 17.25 ? 79  GLN C C   1 
ATOM   5015  O  O   . GLN C  1 79  ? 11.475  22.905  19.282  1.00 16.57 ? 79  GLN C O   1 
ATOM   5016  C  CB  . GLN C  1 79  ? 10.786  25.886  18.466  1.00 19.75 ? 79  GLN C CB  1 
ATOM   5017  C  CG  . GLN C  1 79  ? 9.403   25.964  17.775  1.00 26.84 ? 79  GLN C CG  1 
ATOM   5018  C  CD  . GLN C  1 79  ? 9.071   24.698  16.962  1.00 37.21 ? 79  GLN C CD  1 
ATOM   5019  O  OE1 . GLN C  1 79  ? 9.973   23.957  16.484  1.00 40.99 ? 79  GLN C OE1 1 
ATOM   5020  N  NE2 . GLN C  1 79  ? 7.751   24.413  16.835  1.00 40.42 ? 79  GLN C NE2 1 
ATOM   5021  N  N   . GLY C  1 80  ? 9.396   23.358  20.040  1.00 17.23 ? 80  GLY C N   1 
ATOM   5022  C  CA  . GLY C  1 80  ? 9.051   21.938  19.827  1.00 18.65 ? 80  GLY C CA  1 
ATOM   5023  C  C   . GLY C  1 80  ? 8.508   21.264  21.108  1.00 19.28 ? 80  GLY C C   1 
ATOM   5024  O  O   . GLY C  1 80  ? 7.777   20.257  21.034  1.00 19.47 ? 80  GLY C O   1 
ATOM   5025  N  N   . LEU C  1 81  ? 8.746   21.859  22.283  1.00 17.38 ? 81  LEU C N   1 
ATOM   5026  C  CA  . LEU C  1 81  ? 8.181   21.342  23.544  1.00 19.28 ? 81  LEU C CA  1 
ATOM   5027  C  C   . LEU C  1 81  ? 6.850   22.105  23.844  1.00 19.77 ? 81  LEU C C   1 
ATOM   5028  O  O   . LEU C  1 81  ? 6.521   23.051  23.077  1.00 21.46 ? 81  LEU C O   1 
ATOM   5029  C  CB  . LEU C  1 81  ? 9.207   21.530  24.650  1.00 15.94 ? 81  LEU C CB  1 
ATOM   5030  C  CG  . LEU C  1 81  ? 10.598  20.801  24.489  1.00 18.47 ? 81  LEU C CG  1 
ATOM   5031  C  CD1 . LEU C  1 81  ? 11.618  21.208  25.422  1.00 19.88 ? 81  LEU C CD1 1 
ATOM   5032  C  CD2 . LEU C  1 81  ? 10.354  19.315  24.641  1.00 15.16 ? 81  LEU C CD2 1 
ATOM   5033  N  N   A GLN C  1 82  ? 6.224   21.754  24.996  0.50 20.19 ? 82  GLN C N   1 
ATOM   5034  N  N   B GLN C  1 82  ? 6.058   21.771  24.868  0.50 21.02 ? 82  GLN C N   1 
ATOM   5035  C  CA  A GLN C  1 82  ? 4.906   22.311  25.427  0.50 21.24 ? 82  GLN C CA  1 
ATOM   5036  C  CA  B GLN C  1 82  ? 4.764   22.521  24.976  0.50 21.70 ? 82  GLN C CA  1 
ATOM   5037  C  C   A GLN C  1 82  ? 4.945   23.838  25.540  0.50 20.60 ? 82  GLN C C   1 
ATOM   5038  C  C   B GLN C  1 82  ? 5.029   24.029  25.235  0.50 20.66 ? 82  GLN C C   1 
ATOM   5039  O  O   A GLN C  1 82  ? 3.978   24.532  25.230  0.50 21.46 ? 82  GLN C O   1 
ATOM   5040  O  O   B GLN C  1 82  ? 4.283   24.912  24.694  0.50 20.36 ? 82  GLN C O   1 
ATOM   5041  C  CB  A GLN C  1 82  ? 4.460   21.800  26.822  0.50 20.41 ? 82  GLN C CB  1 
ATOM   5042  C  CB  B GLN C  1 82  ? 3.807   21.927  26.027  0.50 21.99 ? 82  GLN C CB  1 
ATOM   5043  C  CG  A GLN C  1 82  ? 4.512   20.340  27.109  0.50 22.76 ? 82  GLN C CG  1 
ATOM   5044  C  CG  B GLN C  1 82  ? 2.421   22.562  26.078  0.50 21.67 ? 82  GLN C CG  1 
ATOM   5045  C  CD  A GLN C  1 82  ? 3.666   19.978  28.361  0.50 23.15 ? 82  GLN C CD  1 
ATOM   5046  C  CD  B GLN C  1 82  ? 1.626   22.110  27.289  0.50 25.34 ? 82  GLN C CD  1 
ATOM   5047  O  OE1 A GLN C  1 82  ? 4.192   19.487  29.371  0.50 29.66 ? 82  GLN C OE1 1 
ATOM   5048  O  OE1 B GLN C  1 82  ? 2.196   21.712  28.321  0.50 29.45 ? 82  GLN C OE1 1 
ATOM   5049  N  NE2 A GLN C  1 82  ? 2.345   20.239  28.287  0.50 24.67 ? 82  GLN C NE2 1 
ATOM   5050  N  NE2 B GLN C  1 82  ? 0.310   22.188  27.185  0.50 27.44 ? 82  GLN C NE2 1 
ATOM   5051  N  N   . SER C  1 83  ? 6.082   24.326  26.029  1.00 17.96 ? 83  SER C N   1 
ATOM   5052  C  CA  . SER C  1 83  ? 6.381   25.697  26.271  1.00 14.34 ? 83  SER C CA  1 
ATOM   5053  C  C   . SER C  1 83  ? 7.643   25.995  25.439  1.00 13.08 ? 83  SER C C   1 
ATOM   5054  O  O   . SER C  1 83  ? 8.448   25.064  25.151  1.00 12.59 ? 83  SER C O   1 
ATOM   5055  C  CB  . SER C  1 83  ? 6.691   25.921  27.728  1.00 13.85 ? 83  SER C CB  1 
ATOM   5056  O  OG  . SER C  1 83  ? 5.528   25.593  28.551  1.00 15.86 ? 83  SER C OG  1 
ATOM   5057  N  N   . ARG C  1 84  ? 7.888   27.292  25.240  1.00 10.71 ? 84  ARG C N   1 
ATOM   5058  C  CA  . ARG C  1 84  ? 9.216   27.772  24.780  1.00 10.67 ? 84  ARG C CA  1 
ATOM   5059  C  C   . ARG C  1 84  ? 10.155  27.712  25.949  1.00 9.54  ? 84  ARG C C   1 
ATOM   5060  O  O   . ARG C  1 84  ? 9.868   28.172  27.043  1.00 10.24 ? 84  ARG C O   1 
ATOM   5061  C  CB  . ARG C  1 84  ? 9.072   29.208  24.299  1.00 11.24 ? 84  ARG C CB  1 
ATOM   5062  C  CG  . ARG C  1 84  ? 10.503  29.769  23.820  1.00 11.26 ? 84  ARG C CG  1 
ATOM   5063  C  CD  . ARG C  1 84  ? 10.441  31.232  23.233  1.00 10.93 ? 84  ARG C CD  1 
ATOM   5064  N  NE  . ARG C  1 84  ? 9.870   31.151  21.908  1.00 13.70 ? 84  ARG C NE  1 
ATOM   5065  C  CZ  . ARG C  1 84  ? 9.773   32.228  21.104  1.00 11.75 ? 84  ARG C CZ  1 
ATOM   5066  N  NH1 . ARG C  1 84  ? 10.031  33.413  21.612  1.00 12.94 ? 84  ARG C NH1 1 
ATOM   5067  N  NH2 . ARG C  1 84  ? 9.300   32.046  19.876  1.00 13.55 ? 84  ARG C NH2 1 
ATOM   5068  N  N   . TYR C  1 85  ? 11.400  27.211  25.638  1.00 8.92  ? 85  TYR C N   1 
ATOM   5069  C  CA  . TYR C  1 85  ? 12.516  27.267  26.596  1.00 9.06  ? 85  TYR C CA  1 
ATOM   5070  C  C   . TYR C  1 85  ? 13.622  28.162  26.037  1.00 8.98  ? 85  TYR C C   1 
ATOM   5071  O  O   . TYR C  1 85  ? 14.099  27.888  24.909  1.00 10.64 ? 85  TYR C O   1 
ATOM   5072  C  CB  . TYR C  1 85  ? 13.051  25.850  26.856  1.00 9.87  ? 85  TYR C CB  1 
ATOM   5073  C  CG  . TYR C  1 85  ? 12.074  25.061  27.772  1.00 8.28  ? 85  TYR C CG  1 
ATOM   5074  C  CD1 . TYR C  1 85  ? 11.039  24.451  27.195  1.00 9.44  ? 85  TYR C CD1 1 
ATOM   5075  C  CD2 . TYR C  1 85  ? 12.273  24.926  29.129  1.00 8.06  ? 85  TYR C CD2 1 
ATOM   5076  C  CE1 . TYR C  1 85  ? 10.100  23.678  27.973  1.00 11.79 ? 85  TYR C CE1 1 
ATOM   5077  C  CE2 . TYR C  1 85  ? 11.380  24.133  29.918  1.00 7.53  ? 85  TYR C CE2 1 
ATOM   5078  C  CZ  . TYR C  1 85  ? 10.331  23.569  29.283  1.00 7.86  ? 85  TYR C CZ  1 
ATOM   5079  O  OH  . TYR C  1 85  ? 9.472   22.791  30.111  1.00 13.34 ? 85  TYR C OH  1 
ATOM   5080  N  N   . SER C  1 86  ? 13.980  29.193  26.779  1.00 8.69  ? 86  SER C N   1 
ATOM   5081  C  CA  . SER C  1 86  ? 14.957  30.179  26.279  1.00 9.18  ? 86  SER C CA  1 
ATOM   5082  C  C   . SER C  1 86  ? 16.345  29.845  26.892  1.00 10.45 ? 86  SER C C   1 
ATOM   5083  O  O   . SER C  1 86  ? 16.424  29.452  28.059  1.00 7.92  ? 86  SER C O   1 
ATOM   5084  C  CB  . SER C  1 86  ? 14.567  31.640  26.668  1.00 9.43  ? 86  SER C CB  1 
ATOM   5085  O  OG  . SER C  1 86  ? 13.329  31.934  26.009  1.00 11.37 ? 86  SER C OG  1 
ATOM   5086  N  N   . ALA C  1 87  ? 17.418  30.015  26.095  1.00 9.20  ? 87  ALA C N   1 
ATOM   5087  C  CA  . ALA C  1 87  ? 18.749  29.668  26.594  1.00 7.84  ? 87  ALA C CA  1 
ATOM   5088  C  C   . ALA C  1 87  ? 19.204  30.626  27.641  1.00 8.62  ? 87  ALA C C   1 
ATOM   5089  O  O   . ALA C  1 87  ? 18.772  31.800  27.671  1.00 10.35 ? 87  ALA C O   1 
ATOM   5090  C  CB  . ALA C  1 87  ? 19.776  29.744  25.392  1.00 9.58  ? 87  ALA C CB  1 
ATOM   5091  N  N   . THR C  1 88  ? 20.028  30.122  28.594  1.00 7.01  ? 88  THR C N   1 
ATOM   5092  C  CA  . THR C  1 88  ? 20.694  30.951  29.540  1.00 8.01  ? 88  THR C CA  1 
ATOM   5093  C  C   . THR C  1 88  ? 22.229  30.812  29.568  1.00 7.10  ? 88  THR C C   1 
ATOM   5094  O  O   . THR C  1 88  ? 22.926  31.805  29.698  1.00 7.27  ? 88  THR C O   1 
ATOM   5095  C  CB  . THR C  1 88  ? 20.094  30.708  31.007  1.00 10.00 ? 88  THR C CB  1 
ATOM   5096  O  OG1 . THR C  1 88  ? 20.785  31.510  31.966  1.00 15.17 ? 88  THR C OG1 1 
ATOM   5097  C  CG2 . THR C  1 88  ? 20.171  29.298  31.434  1.00 9.40  ? 88  THR C CG2 1 
ATOM   5098  N  N   . GLN C  1 89  ? 22.771  29.579  29.402  1.00 7.02  ? 89  GLN C N   1 
ATOM   5099  C  CA  . GLN C  1 89  ? 24.227  29.383  29.427  1.00 7.08  ? 89  GLN C CA  1 
ATOM   5100  C  C   . GLN C  1 89  ? 24.505  27.977  28.891  1.00 5.61  ? 89  GLN C C   1 
ATOM   5101  O  O   . GLN C  1 89  ? 23.599  27.096  28.885  1.00 5.90  ? 89  GLN C O   1 
ATOM   5102  C  CB  . GLN C  1 89  ? 24.796  29.614  30.850  1.00 8.01  ? 89  GLN C CB  1 
ATOM   5103  C  CG  . GLN C  1 89  ? 24.180  28.786  32.005  1.00 8.03  ? 89  GLN C CG  1 
ATOM   5104  C  CD  . GLN C  1 89  ? 25.077  27.654  32.426  1.00 9.24  ? 89  GLN C CD  1 
ATOM   5105  O  OE1 . GLN C  1 89  ? 25.558  26.957  31.602  1.00 9.75  ? 89  GLN C OE1 1 
ATOM   5106  N  NE2 . GLN C  1 89  ? 25.238  27.442  33.646  1.00 14.75 ? 89  GLN C NE2 1 
ATOM   5107  N  N   . LEU C  1 90  ? 25.756  27.753  28.481  1.00 6.03  ? 90  LEU C N   1 
ATOM   5108  C  CA  . LEU C  1 90  ? 26.259  26.352  28.281  1.00 6.08  ? 90  LEU C CA  1 
ATOM   5109  C  C   . LEU C  1 90  ? 27.524  26.182  29.115  1.00 6.29  ? 90  LEU C C   1 
ATOM   5110  O  O   . LEU C  1 90  ? 28.222  27.184  29.445  1.00 6.00  ? 90  LEU C O   1 
ATOM   5111  C  CB  . LEU C  1 90  ? 26.470  25.991  26.798  1.00 6.62  ? 90  LEU C CB  1 
ATOM   5112  C  CG  . LEU C  1 90  ? 27.411  26.910  25.946  1.00 5.64  ? 90  LEU C CG  1 
ATOM   5113  C  CD1 . LEU C  1 90  ? 28.928  26.638  26.299  1.00 7.28  ? 90  LEU C CD1 1 
ATOM   5114  C  CD2 . LEU C  1 90  ? 27.061  26.669  24.495  1.00 6.88  ? 90  LEU C CD2 1 
ATOM   5115  N  N   . HIS C  1 91  ? 27.876  24.907  29.378  1.00 6.12  ? 91  HIS C N   1 
ATOM   5116  C  CA  . HIS C  1 91  ? 29.061  24.627  30.153  1.00 5.99  ? 91  HIS C CA  1 
ATOM   5117  C  C   . HIS C  1 91  ? 29.421  23.153  29.911  1.00 6.10  ? 91  HIS C C   1 
ATOM   5118  O  O   . HIS C  1 91  ? 28.712  22.422  29.191  1.00 4.81  ? 91  HIS C O   1 
ATOM   5119  C  CB  . HIS C  1 91  ? 28.893  24.886  31.687  1.00 6.97  ? 91  HIS C CB  1 
ATOM   5120  C  CG  . HIS C  1 91  ? 27.786  24.005  32.242  1.00 5.06  ? 91  HIS C CG  1 
ATOM   5121  N  ND1 . HIS C  1 91  ? 26.469  24.392  32.207  1.00 6.15  ? 91  HIS C ND1 1 
ATOM   5122  C  CD2 . HIS C  1 91  ? 27.815  22.718  32.689  1.00 6.35  ? 91  HIS C CD2 1 
ATOM   5123  C  CE1 . HIS C  1 91  ? 25.707  23.344  32.650  1.00 6.45  ? 91  HIS C CE1 1 
ATOM   5124  N  NE2 . HIS C  1 91  ? 26.512  22.333  32.910  1.00 5.85  ? 91  HIS C NE2 1 
ATOM   5125  N  N   . LEU C  1 92  ? 30.572  22.724  30.458  1.00 5.09  ? 92  LEU C N   1 
ATOM   5126  C  CA  . LEU C  1 92  ? 31.010  21.342  30.222  1.00 4.76  ? 92  LEU C CA  1 
ATOM   5127  C  C   . LEU C  1 92  ? 31.378  20.629  31.565  1.00 4.01  ? 92  LEU C C   1 
ATOM   5128  O  O   . LEU C  1 92  ? 31.545  21.190  32.634  1.00 5.27  ? 92  LEU C O   1 
ATOM   5129  C  CB  . LEU C  1 92  ? 32.241  21.296  29.234  1.00 7.63  ? 92  LEU C CB  1 
ATOM   5130  C  CG  . LEU C  1 92  ? 32.014  21.950  27.874  1.00 7.71  ? 92  LEU C CG  1 
ATOM   5131  C  CD1 . LEU C  1 92  ? 32.497  23.374  27.836  1.00 9.77  ? 92  LEU C CD1 1 
ATOM   5132  C  CD2 . LEU C  1 92  ? 32.692  21.081  26.793  1.00 10.19 ? 92  LEU C CD2 1 
ATOM   5133  N  N   . HIS C  1 93  ? 31.486  19.272  31.372  1.00 5.31  ? 93  HIS C N   1 
ATOM   5134  C  CA  . HIS C  1 93  ? 31.956  18.390  32.490  1.00 5.56  ? 93  HIS C CA  1 
ATOM   5135  C  C   . HIS C  1 93  ? 33.045  17.439  31.863  1.00 5.48  ? 93  HIS C C   1 
ATOM   5136  O  O   . HIS C  1 93  ? 32.845  16.999  30.715  1.00 6.07  ? 93  HIS C O   1 
ATOM   5137  C  CB  . HIS C  1 93  ? 30.793  17.524  32.987  1.00 4.62  ? 93  HIS C CB  1 
ATOM   5138  C  CG  . HIS C  1 93  ? 29.648  18.349  33.547  1.00 4.99  ? 93  HIS C CG  1 
ATOM   5139  N  ND1 . HIS C  1 93  ? 29.567  18.712  34.888  1.00 5.55  ? 93  HIS C ND1 1 
ATOM   5140  C  CD2 . HIS C  1 93  ? 28.558  18.907  32.936  1.00 4.55  ? 93  HIS C CD2 1 
ATOM   5141  C  CE1 . HIS C  1 93  ? 28.442  19.455  35.064  1.00 5.25  ? 93  HIS C CE1 1 
ATOM   5142  N  NE2 . HIS C  1 93  ? 27.822  19.594  33.905  1.00 5.22  ? 93  HIS C NE2 1 
ATOM   5143  N  N   . TRP C  1 94  ? 34.068  17.123  32.672  1.00 4.61  ? 94  TRP C N   1 
ATOM   5144  C  CA  . TRP C  1 94  ? 35.190  16.297  32.143  1.00 5.39  ? 94  TRP C CA  1 
ATOM   5145  C  C   . TRP C  1 94  ? 35.902  15.554  33.281  1.00 5.37  ? 94  TRP C C   1 
ATOM   5146  O  O   . TRP C  1 94  ? 35.607  15.768  34.477  1.00 5.98  ? 94  TRP C O   1 
ATOM   5147  C  CB  . TRP C  1 94  ? 36.192  17.192  31.299  1.00 3.83  ? 94  TRP C CB  1 
ATOM   5148  C  CG  . TRP C  1 94  ? 36.751  18.337  32.149  1.00 5.37  ? 94  TRP C CG  1 
ATOM   5149  C  CD1 . TRP C  1 94  ? 37.893  18.310  33.024  1.00 5.83  ? 94  TRP C CD1 1 
ATOM   5150  C  CD2 . TRP C  1 94  ? 36.205  19.670  32.265  1.00 4.33  ? 94  TRP C CD2 1 
ATOM   5151  N  NE1 . TRP C  1 94  ? 38.070  19.547  33.621  1.00 5.04  ? 94  TRP C NE1 1 
ATOM   5152  C  CE2 . TRP C  1 94  ? 37.090  20.402  33.166  1.00 4.75  ? 94  TRP C CE2 1 
ATOM   5153  C  CE3 . TRP C  1 94  ? 35.093  20.339  31.742  1.00 6.74  ? 94  TRP C CE3 1 
ATOM   5154  C  CZ2 . TRP C  1 94  ? 36.887  21.768  33.490  1.00 5.75  ? 94  TRP C CZ2 1 
ATOM   5155  C  CZ3 . TRP C  1 94  ? 34.890  21.682  32.084  1.00 5.28  ? 94  TRP C CZ3 1 
ATOM   5156  C  CH2 . TRP C  1 94  ? 35.755  22.387  32.938  1.00 5.57  ? 94  TRP C CH2 1 
ATOM   5157  N  N   . GLY C  1 95  ? 36.886  14.726  32.863  1.00 4.26  ? 95  GLY C N   1 
ATOM   5158  C  CA  . GLY C  1 95  ? 37.601  13.831  33.761  1.00 5.45  ? 95  GLY C CA  1 
ATOM   5159  C  C   . GLY C  1 95  ? 38.985  14.397  34.103  1.00 7.10  ? 95  GLY C C   1 
ATOM   5160  O  O   . GLY C  1 95  ? 39.109  15.552  34.518  1.00 6.33  ? 95  GLY C O   1 
ATOM   5161  N  N   . ASN C  1 96  ? 40.017  13.610  33.751  1.00 7.51  ? 96  ASN C N   1 
ATOM   5162  C  CA  . ASN C  1 96  ? 41.405  14.078  34.094  1.00 8.11  ? 96  ASN C CA  1 
ATOM   5163  C  C   . ASN C  1 96  ? 42.320  13.246  33.198  1.00 8.75  ? 96  ASN C C   1 
ATOM   5164  O  O   . ASN C  1 96  ? 41.871  12.211  32.633  1.00 8.64  ? 96  ASN C O   1 
ATOM   5165  C  CB  . ASN C  1 96  ? 41.713  13.828  35.603  1.00 7.92  ? 96  ASN C CB  1 
ATOM   5166  C  CG  . ASN C  1 96  ? 41.873  12.339  35.956  1.00 9.29  ? 96  ASN C CG  1 
ATOM   5167  O  OD1 . ASN C  1 96  ? 43.094  11.835  35.872  1.00 13.66 ? 96  ASN C OD1 1 
ATOM   5168  N  ND2 . ASN C  1 96  ? 40.844  11.656  36.383  1.00 11.51 ? 96  ASN C ND2 1 
ATOM   5169  N  N   . PRO C  1 97  ? 43.574  13.744  33.001  1.00 9.56  ? 97  PRO C N   1 
ATOM   5170  C  CA  . PRO C  1 97  ? 44.402  13.022  32.014  1.00 10.56 ? 97  PRO C CA  1 
ATOM   5171  C  C   . PRO C  1 97  ? 44.690  11.511  32.361  1.00 11.16 ? 97  PRO C C   1 
ATOM   5172  O  O   . PRO C  1 97  ? 44.952  10.750  31.411  1.00 12.88 ? 97  PRO C O   1 
ATOM   5173  C  CB  . PRO C  1 97  ? 45.720  13.803  32.056  1.00 11.18 ? 97  PRO C CB  1 
ATOM   5174  C  CG  . PRO C  1 97  ? 45.251  15.201  32.557  1.00 11.63 ? 97  PRO C CG  1 
ATOM   5175  C  CD  . PRO C  1 97  ? 44.198  14.965  33.556  1.00 9.97  ? 97  PRO C CD  1 
ATOM   5176  N  N   . ASN C  1 98  ? 44.680  11.163  33.656  1.00 10.82 ? 98  ASN C N   1 
ATOM   5177  C  CA  . ASN C  1 98  ? 44.944  9.756   33.978  1.00 14.30 ? 98  ASN C CA  1 
ATOM   5178  C  C   . ASN C  1 98  ? 43.683  8.879   33.835  1.00 12.83 ? 98  ASN C C   1 
ATOM   5179  O  O   . ASN C  1 98  ? 43.754  7.673   33.811  1.00 16.05 ? 98  ASN C O   1 
ATOM   5180  C  CB  . ASN C  1 98  ? 45.448  9.671   35.384  1.00 14.48 ? 98  ASN C CB  1 
ATOM   5181  C  CG  . ASN C  1 98  ? 46.855  10.212  35.529  1.00 23.41 ? 98  ASN C CG  1 
ATOM   5182  O  OD1 . ASN C  1 98  ? 47.673  10.049  34.617  1.00 23.58 ? 98  ASN C OD1 1 
ATOM   5183  N  ND2 . ASN C  1 98  ? 47.156  10.813  36.678  1.00 31.54 ? 98  ASN C ND2 1 
ATOM   5184  N  N   . ASP C  1 99  ? 42.517  9.492   33.704  1.00 10.23 ? 99  ASP C N   1 
ATOM   5185  C  CA  . ASP C  1 99  ? 41.296  8.659   33.453  1.00 9.75  ? 99  ASP C CA  1 
ATOM   5186  C  C   . ASP C  1 99  ? 40.347  9.592   32.705  1.00 10.71 ? 99  ASP C C   1 
ATOM   5187  O  O   . ASP C  1 99  ? 39.449  10.260  33.248  1.00 9.31  ? 99  ASP C O   1 
ATOM   5188  C  CB  . ASP C  1 99  ? 40.662  8.156   34.729  1.00 10.25 ? 99  ASP C CB  1 
ATOM   5189  C  CG  . ASP C  1 99  ? 39.672  7.027   34.515  1.00 14.03 ? 99  ASP C CG  1 
ATOM   5190  O  OD1 . ASP C  1 99  ? 39.093  6.900   33.416  1.00 16.31 ? 99  ASP C OD1 1 
ATOM   5191  O  OD2 . ASP C  1 99  ? 39.452  6.275   35.483  1.00 18.22 ? 99  ASP C OD2 1 
ATOM   5192  N  N   . PRO C  1 100 ? 40.564  9.739   31.386  1.00 9.75  ? 100 PRO C N   1 
ATOM   5193  C  CA  . PRO C  1 100 ? 39.897  10.820  30.576  1.00 9.76  ? 100 PRO C CA  1 
ATOM   5194  C  C   . PRO C  1 100 ? 38.450  10.414  30.171  1.00 9.09  ? 100 PRO C C   1 
ATOM   5195  O  O   . PRO C  1 100 ? 38.107  10.345  28.978  1.00 9.57  ? 100 PRO C O   1 
ATOM   5196  C  CB  . PRO C  1 100 ? 40.847  11.015  29.398  1.00 9.75  ? 100 PRO C CB  1 
ATOM   5197  C  CG  . PRO C  1 100 ? 41.383  9.593   29.224  1.00 10.63 ? 100 PRO C CG  1 
ATOM   5198  C  CD  . PRO C  1 100 ? 41.579  9.011   30.595  1.00 9.35  ? 100 PRO C CD  1 
ATOM   5199  N  N   . HIS C  1 101 ? 37.631  10.136  31.175  1.00 9.24  ? 101 HIS C N   1 
ATOM   5200  C  CA  . HIS C  1 101 ? 36.287  9.596   30.947  1.00 9.02  ? 101 HIS C CA  1 
ATOM   5201  C  C   . HIS C  1 101 ? 35.382  10.320  31.915  1.00 9.04  ? 101 HIS C C   1 
ATOM   5202  O  O   . HIS C  1 101 ? 34.879  9.661   32.860  1.00 13.71 ? 101 HIS C O   1 
ATOM   5203  C  CB  . HIS C  1 101 ? 36.254  8.004   31.150  1.00 10.08 ? 101 HIS C CB  1 
ATOM   5204  C  CG  . HIS C  1 101 ? 37.268  7.330   30.265  1.00 13.67 ? 101 HIS C CG  1 
ATOM   5205  N  ND1 . HIS C  1 101 ? 37.179  7.230   28.873  1.00 20.21 ? 101 HIS C ND1 1 
ATOM   5206  C  CD2 . HIS C  1 101 ? 38.448  6.783   30.610  1.00 14.96 ? 101 HIS C CD2 1 
ATOM   5207  C  CE1 . HIS C  1 101 ? 38.277  6.638   28.413  1.00 19.03 ? 101 HIS C CE1 1 
ATOM   5208  N  NE2 . HIS C  1 101 ? 39.070  6.396   29.442  1.00 20.90 ? 101 HIS C NE2 1 
ATOM   5209  N  N   . GLY C  1 102 ? 34.954  11.500  31.572  1.00 7.19  ? 102 GLY C N   1 
ATOM   5210  C  CA  . GLY C  1 102 ? 34.241  12.389  32.549  1.00 6.27  ? 102 GLY C CA  1 
ATOM   5211  C  C   . GLY C  1 102 ? 32.902  12.919  32.013  1.00 3.93  ? 102 GLY C C   1 
ATOM   5212  O  O   . GLY C  1 102 ? 32.445  13.938  32.516  1.00 5.57  ? 102 GLY C O   1 
ATOM   5213  N  N   . SER C  1 103 ? 32.257  12.191  31.065  1.00 4.98  ? 103 SER C N   1 
ATOM   5214  C  CA  . SER C  1 103 ? 30.841  12.574  30.831  1.00 4.90  ? 103 SER C CA  1 
ATOM   5215  C  C   . SER C  1 103 ? 30.026  12.336  32.143  1.00 5.51  ? 103 SER C C   1 
ATOM   5216  O  O   . SER C  1 103 ? 30.480  11.598  33.041  1.00 7.58  ? 103 SER C O   1 
ATOM   5217  C  CB  . SER C  1 103 ? 30.252  11.810  29.686  1.00 4.16  ? 103 SER C CB  1 
ATOM   5218  O  OG  . SER C  1 103 ? 30.158  10.397  29.978  1.00 4.97  ? 103 SER C OG  1 
ATOM   5219  N  N   . GLU C  1 104 ? 28.852  12.927  32.162  1.00 4.04  ? 104 GLU C N   1 
ATOM   5220  C  CA  . GLU C  1 104 ? 27.950  12.688  33.253  1.00 5.47  ? 104 GLU C CA  1 
ATOM   5221  C  C   . GLU C  1 104 ? 27.049  11.495  32.934  1.00 4.74  ? 104 GLU C C   1 
ATOM   5222  O  O   . GLU C  1 104 ? 26.996  10.475  33.667  1.00 5.98  ? 104 GLU C O   1 
ATOM   5223  C  CB  . GLU C  1 104 ? 27.116  13.905  33.562  1.00 5.80  ? 104 GLU C CB  1 
ATOM   5224  C  CG  . GLU C  1 104 ? 27.993  15.173  33.887  1.00 5.02  ? 104 GLU C CG  1 
ATOM   5225  C  CD  . GLU C  1 104 ? 27.438  15.964  35.035  1.00 4.01  ? 104 GLU C CD  1 
ATOM   5226  O  OE1 . GLU C  1 104 ? 26.517  16.758  34.690  1.00 5.31  ? 104 GLU C OE1 1 
ATOM   5227  O  OE2 . GLU C  1 104 ? 27.828  15.766  36.197  1.00 5.81  ? 104 GLU C OE2 1 
ATOM   5228  N  N   . HIS C  1 105 ? 26.255  11.580  31.828  1.00 3.97  ? 105 HIS C N   1 
ATOM   5229  C  CA  . HIS C  1 105 ? 25.488  10.423  31.393  1.00 3.64  ? 105 HIS C CA  1 
ATOM   5230  C  C   . HIS C  1 105 ? 26.435  9.405   30.804  1.00 6.18  ? 105 HIS C C   1 
ATOM   5231  O  O   . HIS C  1 105 ? 27.530  9.729   30.284  1.00 5.88  ? 105 HIS C O   1 
ATOM   5232  C  CB  . HIS C  1 105 ? 24.492  10.831  30.308  1.00 6.54  ? 105 HIS C CB  1 
ATOM   5233  C  CG  . HIS C  1 105 ? 23.380  11.704  30.867  1.00 5.75  ? 105 HIS C CG  1 
ATOM   5234  N  ND1 . HIS C  1 105 ? 23.512  13.077  31.014  1.00 5.34  ? 105 HIS C ND1 1 
ATOM   5235  C  CD2 . HIS C  1 105 ? 22.180  11.378  31.431  1.00 5.33  ? 105 HIS C CD2 1 
ATOM   5236  C  CE1 . HIS C  1 105 ? 22.381  13.580  31.569  1.00 5.74  ? 105 HIS C CE1 1 
ATOM   5237  N  NE2 . HIS C  1 105 ? 21.589  12.543  31.900  1.00 5.02  ? 105 HIS C NE2 1 
ATOM   5238  N  N   . THR C  1 106 ? 26.053  8.137   30.948  1.00 5.58  ? 106 THR C N   1 
ATOM   5239  C  CA  . THR C  1 106 ? 26.821  6.990   30.377  1.00 5.62  ? 106 THR C CA  1 
ATOM   5240  C  C   . THR C  1 106 ? 25.807  6.174   29.511  1.00 6.25  ? 106 THR C C   1 
ATOM   5241  O  O   . THR C  1 106 ? 24.642  6.308   29.633  1.00 7.60  ? 106 THR C O   1 
ATOM   5242  C  CB  . THR C  1 106 ? 27.465  6.123   31.452  1.00 5.18  ? 106 THR C CB  1 
ATOM   5243  O  OG1 . THR C  1 106 ? 26.430  5.589   32.302  1.00 8.10  ? 106 THR C OG1 1 
ATOM   5244  C  CG2 . THR C  1 106 ? 28.464  6.891   32.326  1.00 8.55  ? 106 THR C CG2 1 
ATOM   5245  N  N   . VAL C  1 107 ? 26.357  5.459   28.545  1.00 6.92  ? 107 VAL C N   1 
ATOM   5246  C  CA  . VAL C  1 107 ? 25.512  4.652   27.589  1.00 8.14  ? 107 VAL C CA  1 
ATOM   5247  C  C   . VAL C  1 107 ? 26.013  3.183   27.700  1.00 8.70  ? 107 VAL C C   1 
ATOM   5248  O  O   . VAL C  1 107 ? 27.132  2.901   27.427  1.00 10.17 ? 107 VAL C O   1 
ATOM   5249  C  CB  . VAL C  1 107 ? 25.665  5.173   26.137  1.00 6.93  ? 107 VAL C CB  1 
ATOM   5250  C  CG1 . VAL C  1 107 ? 24.739  4.215   25.248  1.00 9.09  ? 107 VAL C CG1 1 
ATOM   5251  C  CG2 . VAL C  1 107 ? 25.218  6.633   26.051  1.00 9.80  ? 107 VAL C CG2 1 
ATOM   5252  N  N   . SER C  1 108 ? 25.142  2.303   28.165  1.00 9.42  ? 108 SER C N   1 
ATOM   5253  C  CA  . SER C  1 108 ? 25.511  0.903   28.365  1.00 10.65 ? 108 SER C CA  1 
ATOM   5254  C  C   . SER C  1 108 ? 26.793  0.786   29.194  1.00 10.25 ? 108 SER C C   1 
ATOM   5255  O  O   . SER C  1 108 ? 27.713  -0.004  28.905  1.00 12.63 ? 108 SER C O   1 
ATOM   5256  C  CB  . SER C  1 108 ? 25.638  0.162   26.995  1.00 11.94 ? 108 SER C CB  1 
ATOM   5257  O  OG  . SER C  1 108 ? 24.417  0.227   26.311  1.00 15.74 ? 108 SER C OG  1 
ATOM   5258  N  N   . GLY C  1 109 ? 26.863  1.578   30.268  1.00 9.73  ? 109 GLY C N   1 
ATOM   5259  C  CA  . GLY C  1 109 ? 27.949  1.539   31.219  1.00 12.74 ? 109 GLY C CA  1 
ATOM   5260  C  C   . GLY C  1 109 ? 29.171  2.347   30.754  1.00 13.45 ? 109 GLY C C   1 
ATOM   5261  O  O   . GLY C  1 109 ? 30.097  2.541   31.674  1.00 15.61 ? 109 GLY C O   1 
ATOM   5262  N  N   A GLN C  1 110 ? 29.231  2.818   29.521  0.50 11.91 ? 110 GLN C N   1 
ATOM   5263  N  N   B GLN C  1 110 ? 29.224  2.731   29.429  0.50 12.44 ? 110 GLN C N   1 
ATOM   5264  C  CA  A GLN C  1 110 ? 30.427  3.500   29.090  0.50 13.17 ? 110 GLN C CA  1 
ATOM   5265  C  CA  B GLN C  1 110 ? 30.291  3.552   28.698  0.50 12.30 ? 110 GLN C CA  1 
ATOM   5266  C  C   A GLN C  1 110 ? 30.341  4.974   29.257  0.50 11.07 ? 110 GLN C C   1 
ATOM   5267  C  C   B GLN C  1 110 ? 30.319  5.020   29.187  0.50 10.29 ? 110 GLN C C   1 
ATOM   5268  O  O   A GLN C  1 110 ? 29.402  5.618   28.872  0.50 8.90  ? 110 GLN C O   1 
ATOM   5269  O  O   B GLN C  1 110 ? 29.372  5.731   28.957  0.50 7.78  ? 110 GLN C O   1 
ATOM   5270  C  CB  A GLN C  1 110 ? 30.718  3.167   27.659  0.50 12.95 ? 110 GLN C CB  1 
ATOM   5271  C  CB  B GLN C  1 110 ? 30.141  3.536   27.135  0.50 11.42 ? 110 GLN C CB  1 
ATOM   5272  C  CG  A GLN C  1 110 ? 30.627  1.614   27.378  0.50 12.81 ? 110 GLN C CG  1 
ATOM   5273  C  CG  B GLN C  1 110 ? 31.462  3.871   26.417  0.50 16.90 ? 110 GLN C CG  1 
ATOM   5274  C  CD  A GLN C  1 110 ? 31.442  0.811   28.450  0.50 17.66 ? 110 GLN C CD  1 
ATOM   5275  C  CD  B GLN C  1 110 ? 31.311  4.395   24.994  0.50 15.27 ? 110 GLN C CD  1 
ATOM   5276  O  OE1 A GLN C  1 110 ? 32.656  0.951   28.551  0.50 12.65 ? 110 GLN C OE1 1 
ATOM   5277  O  OE1 B GLN C  1 110 ? 30.464  3.945   24.167  0.50 13.85 ? 110 GLN C OE1 1 
ATOM   5278  N  NE2 A GLN C  1 110 ? 30.737  0.013   29.271  0.50 16.67 ? 110 GLN C NE2 1 
ATOM   5279  N  NE2 B GLN C  1 110 ? 32.129  5.374   24.706  0.50 18.19 ? 110 GLN C NE2 1 
ATOM   5280  N  N   . HIS C  1 111 ? 31.401  5.492   29.856  1.00 11.42 ? 111 HIS C N   1 
ATOM   5281  C  CA  . HIS C  1 111 ? 31.574  6.907   30.057  1.00 10.05 ? 111 HIS C CA  1 
ATOM   5282  C  C   . HIS C  1 111 ? 32.254  7.474   28.841  1.00 13.09 ? 111 HIS C C   1 
ATOM   5283  O  O   . HIS C  1 111 ? 33.355  6.959   28.452  1.00 19.45 ? 111 HIS C O   1 
ATOM   5284  C  CB  . HIS C  1 111 ? 32.658  7.192   31.127  1.00 16.29 ? 111 HIS C CB  1 
ATOM   5285  C  CG  . HIS C  1 111 ? 32.153  7.616   32.449  1.00 12.13 ? 111 HIS C CG  1 
ATOM   5286  N  ND1 . HIS C  1 111 ? 31.590  8.857   32.721  1.00 12.04 ? 111 HIS C ND1 1 
ATOM   5287  C  CD2 . HIS C  1 111 ? 32.031  6.860   33.573  1.00 18.48 ? 111 HIS C CD2 1 
ATOM   5288  C  CE1 . HIS C  1 111 ? 31.168  8.833   33.978  1.00 14.98 ? 111 HIS C CE1 1 
ATOM   5289  N  NE2 . HIS C  1 111 ? 31.393  7.623   34.509  1.00 19.14 ? 111 HIS C NE2 1 
ATOM   5290  N  N   . PHE C  1 112 ? 31.732  8.534   28.297  1.00 7.93  ? 112 PHE C N   1 
ATOM   5291  C  CA  . PHE C  1 112 ? 32.426  9.299   27.248  1.00 6.13  ? 112 PHE C CA  1 
ATOM   5292  C  C   . PHE C  1 112 ? 33.468  10.294  27.901  1.00 6.08  ? 112 PHE C C   1 
ATOM   5293  O  O   . PHE C  1 112 ? 33.580  10.409  29.101  1.00 5.50  ? 112 PHE C O   1 
ATOM   5294  C  CB  . PHE C  1 112 ? 31.445  10.095  26.350  1.00 8.69  ? 112 PHE C CB  1 
ATOM   5295  C  CG  . PHE C  1 112 ? 30.567  9.142   25.577  1.00 9.59  ? 112 PHE C CG  1 
ATOM   5296  C  CD1 . PHE C  1 112 ? 29.572  8.388   26.217  1.00 13.55 ? 112 PHE C CD1 1 
ATOM   5297  C  CD2 . PHE C  1 112 ? 30.853  8.866   24.262  1.00 16.90 ? 112 PHE C CD2 1 
ATOM   5298  C  CE1 . PHE C  1 112 ? 28.813  7.449   25.499  1.00 14.66 ? 112 PHE C CE1 1 
ATOM   5299  C  CE2 . PHE C  1 112 ? 30.121  7.947   23.556  1.00 16.32 ? 112 PHE C CE2 1 
ATOM   5300  C  CZ  . PHE C  1 112 ? 29.096  7.232   24.162  1.00 16.85 ? 112 PHE C CZ  1 
ATOM   5301  N  N   . ALA C  1 113 ? 34.309  10.918  27.038  1.00 5.89  ? 113 ALA C N   1 
ATOM   5302  C  CA  . ALA C  1 113 ? 35.365  11.725  27.569  1.00 6.05  ? 113 ALA C CA  1 
ATOM   5303  C  C   . ALA C  1 113 ? 34.843  12.950  28.294  1.00 5.37  ? 113 ALA C C   1 
ATOM   5304  O  O   . ALA C  1 113 ? 35.401  13.336  29.309  1.00 5.99  ? 113 ALA C O   1 
ATOM   5305  C  CB  . ALA C  1 113 ? 36.317  12.198  26.450  1.00 7.41  ? 113 ALA C CB  1 
ATOM   5306  N  N   . ALA C  1 114 ? 33.764  13.551  27.816  1.00 4.60  ? 114 ALA C N   1 
ATOM   5307  C  CA  . ALA C  1 114 ? 33.261  14.798  28.404  1.00 5.29  ? 114 ALA C CA  1 
ATOM   5308  C  C   . ALA C  1 114 ? 31.815  14.959  27.971  1.00 4.88  ? 114 ALA C C   1 
ATOM   5309  O  O   . ALA C  1 114 ? 31.256  14.148  27.229  1.00 5.35  ? 114 ALA C O   1 
ATOM   5310  C  CB  . ALA C  1 114 ? 34.170  16.012  27.936  1.00 5.77  ? 114 ALA C CB  1 
ATOM   5311  N  N   . GLU C  1 115 ? 31.200  16.064  28.438  1.00 5.63  ? 115 GLU C N   1 
ATOM   5312  C  CA  . GLU C  1 115 ? 29.772  16.313  28.121  1.00 4.47  ? 115 GLU C CA  1 
ATOM   5313  C  C   . GLU C  1 115 ? 29.551  17.809  28.113  1.00 4.69  ? 115 GLU C C   1 
ATOM   5314  O  O   . GLU C  1 115 ? 30.022  18.552  29.035  1.00 5.23  ? 115 GLU C O   1 
ATOM   5315  C  CB  . GLU C  1 115 ? 28.896  15.642  29.203  1.00 5.53  ? 115 GLU C CB  1 
ATOM   5316  C  CG  . GLU C  1 115 ? 27.364  15.622  28.837  1.00 5.16  ? 115 GLU C CG  1 
ATOM   5317  C  CD  . GLU C  1 115 ? 26.577  14.611  29.640  1.00 4.52  ? 115 GLU C CD  1 
ATOM   5318  O  OE1 . GLU C  1 115 ? 25.411  14.837  30.007  1.00 5.43  ? 115 GLU C OE1 1 
ATOM   5319  O  OE2 . GLU C  1 115 ? 27.157  13.544  29.948  1.00 5.18  ? 115 GLU C OE2 1 
ATOM   5320  N  N   . LEU C  1 116 ? 28.777  18.238  27.098  1.00 4.70  ? 116 LEU C N   1 
ATOM   5321  C  CA  . LEU C  1 116 ? 28.355  19.622  27.010  1.00 5.29  ? 116 LEU C CA  1 
ATOM   5322  C  C   . LEU C  1 116 ? 26.866  19.733  27.413  1.00 6.29  ? 116 LEU C C   1 
ATOM   5323  O  O   . LEU C  1 116 ? 26.059  18.919  26.953  1.00 4.92  ? 116 LEU C O   1 
ATOM   5324  C  CB  . LEU C  1 116 ? 28.407  20.136  25.534  1.00 6.51  ? 116 LEU C CB  1 
ATOM   5325  C  CG  . LEU C  1 116 ? 27.858  21.559  25.239  1.00 5.39  ? 116 LEU C CG  1 
ATOM   5326  C  CD1 . LEU C  1 116 ? 28.699  22.669  25.799  1.00 8.63  ? 116 LEU C CD1 1 
ATOM   5327  C  CD2 . LEU C  1 116 ? 27.633  21.699  23.680  1.00 6.46  ? 116 LEU C CD2 1 
ATOM   5328  N  N   . HIS C  1 117 ? 26.554  20.772  28.204  1.00 4.90  ? 117 HIS C N   1 
ATOM   5329  C  CA  . HIS C  1 117 ? 25.153  21.064  28.555  1.00 4.61  ? 117 HIS C CA  1 
ATOM   5330  C  C   . HIS C  1 117 ? 24.720  22.461  28.128  1.00 4.76  ? 117 HIS C C   1 
ATOM   5331  O  O   . HIS C  1 117 ? 25.469  23.436  28.411  1.00 4.73  ? 117 HIS C O   1 
ATOM   5332  C  CB  . HIS C  1 117 ? 24.930  20.995  30.075  1.00 5.71  ? 117 HIS C CB  1 
ATOM   5333  C  CG  . HIS C  1 117 ? 25.086  19.620  30.605  1.00 5.19  ? 117 HIS C CG  1 
ATOM   5334  N  ND1 . HIS C  1 117 ? 25.406  19.340  31.953  1.00 4.84  ? 117 HIS C ND1 1 
ATOM   5335  C  CD2 . HIS C  1 117 ? 24.905  18.428  29.973  1.00 6.21  ? 117 HIS C CD2 1 
ATOM   5336  C  CE1 . HIS C  1 117 ? 25.425  18.010  32.118  1.00 3.82  ? 117 HIS C CE1 1 
ATOM   5337  N  NE2 . HIS C  1 117 ? 25.136  17.441  30.921  1.00 5.29  ? 117 HIS C NE2 1 
ATOM   5338  N  N   . ILE C  1 118 ? 23.606  22.489  27.394  1.00 5.61  ? 118 ILE C N   1 
ATOM   5339  C  CA  . ILE C  1 118 ? 23.067  23.781  26.974  1.00 6.10  ? 118 ILE C CA  1 
ATOM   5340  C  C   . ILE C  1 118 ? 21.764  24.016  27.727  1.00 6.20  ? 118 ILE C C   1 
ATOM   5341  O  O   . ILE C  1 118 ? 20.783  23.251  27.517  1.00 5.22  ? 118 ILE C O   1 
ATOM   5342  C  CB  . ILE C  1 118 ? 22.814  23.866  25.445  1.00 6.27  ? 118 ILE C CB  1 
ATOM   5343  C  CG1 . ILE C  1 118 ? 24.087  23.360  24.656  1.00 5.35  ? 118 ILE C CG1 1 
ATOM   5344  C  CG2 . ILE C  1 118 ? 22.389  25.296  25.051  1.00 7.85  ? 118 ILE C CG2 1 
ATOM   5345  C  CD1 . ILE C  1 118 ? 23.850  23.385  23.104  1.00 8.03  ? 118 ILE C CD1 1 
ATOM   5346  N  N   . VAL C  1 119 ? 21.806  24.983  28.673  1.00 6.30  ? 119 VAL C N   1 
ATOM   5347  C  CA  . VAL C  1 119 ? 20.746  25.125  29.674  1.00 4.78  ? 119 VAL C CA  1 
ATOM   5348  C  C   . VAL C  1 119 ? 19.693  26.181  29.176  1.00 5.72  ? 119 VAL C C   1 
ATOM   5349  O  O   . VAL C  1 119 ? 20.134  27.283  28.725  1.00 6.91  ? 119 VAL C O   1 
ATOM   5350  C  CB  . VAL C  1 119 ? 21.409  25.586  30.980  1.00 5.74  ? 119 VAL C CB  1 
ATOM   5351  C  CG1 . VAL C  1 119 ? 20.372  25.753  32.095  1.00 7.58  ? 119 VAL C CG1 1 
ATOM   5352  C  CG2 . VAL C  1 119 ? 22.508  24.638  31.409  1.00 7.48  ? 119 VAL C CG2 1 
ATOM   5353  N  N   . HIS C  1 120 ? 18.425  25.769  29.298  1.00 7.59  ? 120 HIS C N   1 
ATOM   5354  C  CA  . HIS C  1 120 ? 17.283  26.630  28.908  1.00 8.00  ? 120 HIS C CA  1 
ATOM   5355  C  C   . HIS C  1 120 ? 16.289  26.665  30.084  1.00 8.41  ? 120 HIS C C   1 
ATOM   5356  O  O   . HIS C  1 120 ? 16.220  25.744  30.936  1.00 8.70  ? 120 HIS C O   1 
ATOM   5357  C  CB  . HIS C  1 120 ? 16.583  26.036  27.682  1.00 7.74  ? 120 HIS C CB  1 
ATOM   5358  C  CG  . HIS C  1 120 ? 17.468  25.828  26.478  1.00 8.28  ? 120 HIS C CG  1 
ATOM   5359  N  ND1 . HIS C  1 120 ? 18.441  24.805  26.367  1.00 7.07  ? 120 HIS C ND1 1 
ATOM   5360  C  CD2 . HIS C  1 120 ? 17.484  26.483  25.297  1.00 8.28  ? 120 HIS C CD2 1 
ATOM   5361  C  CE1 . HIS C  1 120 ? 18.958  24.860  25.147  1.00 7.11  ? 120 HIS C CE1 1 
ATOM   5362  N  NE2 . HIS C  1 120 ? 18.432  25.895  24.470  1.00 7.99  ? 120 HIS C NE2 1 
ATOM   5363  N  N   . TYR C  1 121 ? 15.468  27.734  30.074  1.00 8.13  ? 121 TYR C N   1 
ATOM   5364  C  CA  . TYR C  1 121 ? 14.433  27.821  31.091  1.00 11.01 ? 121 TYR C CA  1 
ATOM   5365  C  C   . TYR C  1 121 ? 13.060  28.108  30.435  1.00 9.76  ? 121 TYR C C   1 
ATOM   5366  O  O   . TYR C  1 121 ? 13.003  28.623  29.329  1.00 9.31  ? 121 TYR C O   1 
ATOM   5367  C  CB  . TYR C  1 121 ? 14.673  28.879  32.156  1.00 12.52 ? 121 TYR C CB  1 
ATOM   5368  C  CG  . TYR C  1 121 ? 14.664  30.315  31.576  1.00 12.77 ? 121 TYR C CG  1 
ATOM   5369  C  CD1 . TYR C  1 121 ? 13.567  31.162  31.750  1.00 15.29 ? 121 TYR C CD1 1 
ATOM   5370  C  CD2 . TYR C  1 121 ? 15.746  30.808  30.840  1.00 13.16 ? 121 TYR C CD2 1 
ATOM   5371  C  CE1 . TYR C  1 121 ? 13.554  32.460  31.218  1.00 13.84 ? 121 TYR C CE1 1 
ATOM   5372  C  CE2 . TYR C  1 121 ? 15.737  32.105  30.308  1.00 16.60 ? 121 TYR C CE2 1 
ATOM   5373  C  CZ  . TYR C  1 121 ? 14.640  32.923  30.501  1.00 19.38 ? 121 TYR C CZ  1 
ATOM   5374  O  OH  . TYR C  1 121 ? 14.629  34.200  29.977  1.00 19.62 ? 121 TYR C OH  1 
ATOM   5375  N  N   . ASN C  1 122 ? 12.004  27.766  31.159  1.00 9.74  ? 122 ASN C N   1 
ATOM   5376  C  CA  . ASN C  1 122 ? 10.635  27.883  30.571  1.00 10.40 ? 122 ASN C CA  1 
ATOM   5377  C  C   . ASN C  1 122 ? 10.195  29.365  30.634  1.00 9.36  ? 122 ASN C C   1 
ATOM   5378  O  O   . ASN C  1 122 ? 9.722   29.840  31.704  1.00 11.01 ? 122 ASN C O   1 
ATOM   5379  C  CB  . ASN C  1 122 ? 9.640   26.998  31.372  1.00 9.79  ? 122 ASN C CB  1 
ATOM   5380  C  CG  . ASN C  1 122 ? 8.278   26.911  30.691  1.00 12.29 ? 122 ASN C CG  1 
ATOM   5381  O  OD1 . ASN C  1 122 ? 7.807   27.935  30.028  1.00 10.45 ? 122 ASN C OD1 1 
ATOM   5382  N  ND2 . ASN C  1 122 ? 7.611   25.760  30.814  1.00 12.47 ? 122 ASN C ND2 1 
ATOM   5383  N  N   . SER C  1 123 ? 10.384  30.091  29.501  1.00 9.93  ? 123 SER C N   1 
ATOM   5384  C  CA  . SER C  1 123 ? 10.180  31.532  29.545  1.00 10.18 ? 123 SER C CA  1 
ATOM   5385  C  C   . SER C  1 123 ? 8.679   31.840  29.290  1.00 10.53 ? 123 SER C C   1 
ATOM   5386  O  O   . SER C  1 123 ? 8.304   33.020  29.486  1.00 11.60 ? 123 SER C O   1 
ATOM   5387  C  CB  . SER C  1 123 ? 11.130  32.204  28.441  1.00 10.31 ? 123 SER C CB  1 
ATOM   5388  O  OG  . SER C  1 123 ? 10.904  31.616  27.247  1.00 11.20 ? 123 SER C OG  1 
ATOM   5389  N  N   . ASP C  1 124 ? 7.878   30.851  28.879  1.00 10.73 ? 124 ASP C N   1 
ATOM   5390  C  CA  . ASP C  1 124 ? 6.362   31.033  28.804  1.00 10.96 ? 124 ASP C CA  1 
ATOM   5391  C  C   . ASP C  1 124 ? 5.789   31.112  30.246  1.00 14.02 ? 124 ASP C C   1 
ATOM   5392  O  O   . ASP C  1 124 ? 4.847   31.926  30.528  1.00 15.08 ? 124 ASP C O   1 
ATOM   5393  C  CB  . ASP C  1 124 ? 5.663   29.966  27.996  1.00 10.23 ? 124 ASP C CB  1 
ATOM   5394  C  CG  . ASP C  1 124 ? 5.943   30.108  26.480  1.00 8.83  ? 124 ASP C CG  1 
ATOM   5395  O  OD1 . ASP C  1 124 ? 6.269   31.314  26.069  1.00 11.81 ? 124 ASP C OD1 1 
ATOM   5396  O  OD2 . ASP C  1 124 ? 5.753   29.110  25.767  1.00 10.82 ? 124 ASP C OD2 1 
ATOM   5397  N  N   . LEU C  1 125 ? 6.357   30.320  31.167  1.00 14.62 ? 125 LEU C N   1 
ATOM   5398  C  CA  . LEU C  1 125 ? 5.808   30.283  32.551  1.00 13.03 ? 125 LEU C CA  1 
ATOM   5399  C  C   . LEU C  1 125 ? 6.566   31.233  33.466  1.00 15.70 ? 125 LEU C C   1 
ATOM   5400  O  O   . LEU C  1 125 ? 5.947   31.720  34.469  1.00 18.77 ? 125 LEU C O   1 
ATOM   5401  C  CB  . LEU C  1 125 ? 5.845   28.821  33.121  1.00 13.21 ? 125 LEU C CB  1 
ATOM   5402  C  CG  . LEU C  1 125 ? 5.024   27.751  32.421  1.00 15.87 ? 125 LEU C CG  1 
ATOM   5403  C  CD1 . LEU C  1 125 ? 5.187   26.264  33.009  1.00 17.36 ? 125 LEU C CD1 1 
ATOM   5404  C  CD2 . LEU C  1 125 ? 3.417   28.120  32.338  1.00 16.76 ? 125 LEU C CD2 1 
ATOM   5405  N  N   . TYR C  1 126 ? 7.873   31.518  33.243  1.00 13.45 ? 126 TYR C N   1 
ATOM   5406  C  CA  . TYR C  1 126 ? 8.734   32.188  34.219  1.00 15.07 ? 126 TYR C CA  1 
ATOM   5407  C  C   . TYR C  1 126 ? 9.528   33.278  33.561  1.00 18.17 ? 126 TYR C C   1 
ATOM   5408  O  O   . TYR C  1 126 ? 9.846   33.225  32.396  1.00 18.70 ? 126 TYR C O   1 
ATOM   5409  C  CB  . TYR C  1 126 ? 9.684   31.153  34.996  1.00 15.68 ? 126 TYR C CB  1 
ATOM   5410  C  CG  . TYR C  1 126 ? 8.918   29.953  35.503  1.00 15.83 ? 126 TYR C CG  1 
ATOM   5411  C  CD1 . TYR C  1 126 ? 9.104   28.634  34.973  1.00 14.69 ? 126 TYR C CD1 1 
ATOM   5412  C  CD2 . TYR C  1 126 ? 7.942   30.094  36.505  1.00 14.89 ? 126 TYR C CD2 1 
ATOM   5413  C  CE1 . TYR C  1 126 ? 8.372   27.580  35.370  1.00 16.54 ? 126 TYR C CE1 1 
ATOM   5414  C  CE2 . TYR C  1 126 ? 7.164   29.058  36.881  1.00 18.19 ? 126 TYR C CE2 1 
ATOM   5415  C  CZ  . TYR C  1 126 ? 7.417   27.774  36.407  1.00 18.83 ? 126 TYR C CZ  1 
ATOM   5416  O  OH  . TYR C  1 126 ? 6.677   26.694  36.806  1.00 17.91 ? 126 TYR C OH  1 
ATOM   5417  N  N   . PRO C  1 127 ? 9.816   34.331  34.319  1.00 21.22 ? 127 PRO C N   1 
ATOM   5418  C  CA  . PRO C  1 127 ? 10.568  35.480  33.777  1.00 21.30 ? 127 PRO C CA  1 
ATOM   5419  C  C   . PRO C  1 127 ? 12.072  35.311  33.561  1.00 21.66 ? 127 PRO C C   1 
ATOM   5420  O  O   . PRO C  1 127 ? 12.609  35.970  32.688  1.00 23.80 ? 127 PRO C O   1 
ATOM   5421  C  CB  . PRO C  1 127 ? 10.334  36.562  34.870  1.00 22.24 ? 127 PRO C CB  1 
ATOM   5422  C  CG  . PRO C  1 127 ? 10.226  35.749  36.101  1.00 22.02 ? 127 PRO C CG  1 
ATOM   5423  C  CD  . PRO C  1 127 ? 9.339   34.597  35.698  1.00 22.88 ? 127 PRO C CD  1 
ATOM   5424  N  N   . ASP C  1 128 ? 12.776  34.431  34.284  1.00 21.87 ? 128 ASP C N   1 
ATOM   5425  C  CA  . ASP C  1 128 ? 14.230  34.302  34.053  1.00 19.52 ? 128 ASP C CA  1 
ATOM   5426  C  C   . ASP C  1 128 ? 14.626  32.891  34.600  1.00 17.38 ? 128 ASP C C   1 
ATOM   5427  O  O   . ASP C  1 128 ? 13.801  32.225  35.222  1.00 16.18 ? 128 ASP C O   1 
ATOM   5428  C  CB  . ASP C  1 128 ? 14.992  35.434  34.775  1.00 21.24 ? 128 ASP C CB  1 
ATOM   5429  C  CG  . ASP C  1 128 ? 14.536  35.567  36.220  1.00 27.04 ? 128 ASP C CG  1 
ATOM   5430  O  OD1 . ASP C  1 128 ? 14.201  36.717  36.629  1.00 33.79 ? 128 ASP C OD1 1 
ATOM   5431  O  OD2 . ASP C  1 128 ? 14.447  34.553  36.936  1.00 25.69 ? 128 ASP C OD2 1 
ATOM   5432  N  N   . ALA C  1 129 ? 15.880  32.492  34.333  1.00 18.36 ? 129 ALA C N   1 
ATOM   5433  C  CA  . ALA C  1 129 ? 16.338  31.127  34.734  1.00 18.27 ? 129 ALA C CA  1 
ATOM   5434  C  C   . ALA C  1 129 ? 16.351  30.915  36.258  1.00 19.45 ? 129 ALA C C   1 
ATOM   5435  O  O   . ALA C  1 129 ? 16.049  29.819  36.740  1.00 16.54 ? 129 ALA C O   1 
ATOM   5436  C  CB  . ALA C  1 129 ? 17.707  30.934  34.227  1.00 19.49 ? 129 ALA C CB  1 
ATOM   5437  N  N   . SER C  1 130 ? 16.763  31.985  36.972  1.00 20.00 ? 130 SER C N   1 
ATOM   5438  C  CA  . SER C  1 130 ? 16.836  31.910  38.416  1.00 22.38 ? 130 SER C CA  1 
ATOM   5439  C  C   . SER C  1 130 ? 15.458  31.589  39.009  1.00 22.26 ? 130 SER C C   1 
ATOM   5440  O  O   . SER C  1 130 ? 15.299  30.655  39.777  1.00 22.77 ? 130 SER C O   1 
ATOM   5441  C  CB  . SER C  1 130 ? 17.464  33.170  38.991  1.00 24.53 ? 130 SER C CB  1 
ATOM   5442  O  OG  . SER C  1 130 ? 17.581  32.960  40.394  1.00 29.05 ? 130 SER C OG  1 
ATOM   5443  N  N   A THR C  1 131 ? 14.387  32.331  38.671  0.50 21.36 ? 131 THR C N   1 
ATOM   5444  N  N   B THR C  1 131 ? 14.476  32.364  38.596  0.50 19.88 ? 131 THR C N   1 
ATOM   5445  C  CA  A THR C  1 131 ? 13.049  31.924  39.223  0.50 20.09 ? 131 THR C CA  1 
ATOM   5446  C  CA  B THR C  1 131 ? 13.151  32.103  39.074  0.50 17.57 ? 131 THR C CA  1 
ATOM   5447  C  C   A THR C  1 131 ? 12.458  30.599  38.646  0.50 18.88 ? 131 THR C C   1 
ATOM   5448  C  C   B THR C  1 131 ? 12.596  30.696  38.657  0.50 17.59 ? 131 THR C C   1 
ATOM   5449  O  O   A THR C  1 131 ? 11.604  29.902  39.264  0.50 17.55 ? 131 THR C O   1 
ATOM   5450  O  O   B THR C  1 131 ? 11.961  30.003  39.439  0.50 17.00 ? 131 THR C O   1 
ATOM   5451  C  CB  A THR C  1 131 ? 11.881  32.978  39.031  0.50 21.22 ? 131 THR C CB  1 
ATOM   5452  C  CB  B THR C  1 131 ? 12.230  33.218  38.584  0.50 18.28 ? 131 THR C CB  1 
ATOM   5453  O  OG1 A THR C  1 131 ? 11.544  33.029  37.638  0.50 24.10 ? 131 THR C OG1 1 
ATOM   5454  O  OG1 B THR C  1 131 ? 12.784  34.479  38.972  0.50 19.04 ? 131 THR C OG1 1 
ATOM   5455  C  CG2 A THR C  1 131 ? 12.214  34.353  39.601  0.50 19.91 ? 131 THR C CG2 1 
ATOM   5456  C  CG2 B THR C  1 131 ? 10.816  33.043  39.133  0.50 12.56 ? 131 THR C CG2 1 
ATOM   5457  N  N   . ALA C  1 132 ? 12.857  30.252  37.409  1.00 16.93 ? 132 ALA C N   1 
ATOM   5458  C  CA  . ALA C  1 132 ? 12.371  28.970  36.910  1.00 15.12 ? 132 ALA C CA  1 
ATOM   5459  C  C   . ALA C  1 132 ? 13.042  27.734  37.621  1.00 14.19 ? 132 ALA C C   1 
ATOM   5460  O  O   . ALA C  1 132 ? 12.438  26.652  37.609  1.00 13.73 ? 132 ALA C O   1 
ATOM   5461  C  CB  . ALA C  1 132 ? 12.740  28.899  35.354  1.00 14.75 ? 132 ALA C CB  1 
ATOM   5462  N  N   . SER C  1 133 ? 14.267  27.966  38.151  1.00 14.77 ? 133 SER C N   1 
ATOM   5463  C  CA  . SER C  1 133 ? 15.174  26.821  38.425  1.00 16.64 ? 133 SER C CA  1 
ATOM   5464  C  C   . SER C  1 133 ? 14.615  25.892  39.448  1.00 17.66 ? 133 SER C C   1 
ATOM   5465  O  O   . SER C  1 133 ? 14.993  24.713  39.483  1.00 15.90 ? 133 SER C O   1 
ATOM   5466  C  CB  . SER C  1 133 ? 16.549  27.274  38.891  1.00 18.08 ? 133 SER C CB  1 
ATOM   5467  O  OG  . SER C  1 133 ? 16.455  28.018  40.088  1.00 19.25 ? 133 SER C OG  1 
ATOM   5468  N  N   . ASN C  1 134 ? 13.831  26.425  40.409  1.00 17.61 ? 134 ASN C N   1 
ATOM   5469  C  CA  . ASN C  1 134 ? 13.209  25.613  41.442  1.00 18.37 ? 134 ASN C CA  1 
ATOM   5470  C  C   . ASN C  1 134 ? 11.726  25.383  41.224  1.00 16.53 ? 134 ASN C C   1 
ATOM   5471  O  O   . ASN C  1 134 ? 11.032  24.959  42.124  1.00 20.97 ? 134 ASN C O   1 
ATOM   5472  C  CB  . ASN C  1 134 ? 13.512  26.155  42.874  1.00 18.29 ? 134 ASN C CB  1 
ATOM   5473  C  CG  . ASN C  1 134 ? 12.883  27.584  43.112  1.00 24.57 ? 134 ASN C CG  1 
ATOM   5474  O  OD1 . ASN C  1 134 ? 12.435  28.309  42.177  1.00 26.40 ? 134 ASN C OD1 1 
ATOM   5475  N  ND2 . ASN C  1 134 ? 12.956  28.006  44.368  1.00 30.77 ? 134 ASN C ND2 1 
ATOM   5476  N  N   . LYS C  1 135 ? 11.207  25.599  40.008  1.00 17.02 ? 135 LYS C N   1 
ATOM   5477  C  CA  . LYS C  1 135 ? 9.805   25.498  39.775  1.00 19.00 ? 135 LYS C CA  1 
ATOM   5478  C  C   . LYS C  1 135 ? 9.451   24.464  38.724  1.00 18.86 ? 135 LYS C C   1 
ATOM   5479  O  O   . LYS C  1 135 ? 10.291  24.023  37.899  1.00 16.80 ? 135 LYS C O   1 
ATOM   5480  C  CB  . LYS C  1 135 ? 9.205   26.904  39.366  1.00 18.10 ? 135 LYS C CB  1 
ATOM   5481  C  CG  . LYS C  1 135 ? 9.312   27.920  40.536  1.00 22.22 ? 135 LYS C CG  1 
ATOM   5482  C  CD  . LYS C  1 135 ? 8.744   29.307  40.294  1.00 21.81 ? 135 LYS C CD  1 
ATOM   5483  C  CE  . LYS C  1 135 ? 9.069   30.215  41.502  1.00 23.75 ? 135 LYS C CE  1 
ATOM   5484  N  NZ  . LYS C  1 135 ? 10.541  30.349  41.776  1.00 32.33 ? 135 LYS C NZ  1 
ATOM   5485  N  N   . SER C  1 136 ? 8.213   24.029  38.825  1.00 18.38 ? 136 SER C N   1 
ATOM   5486  C  CA  . SER C  1 136 ? 7.612   23.016  38.004  1.00 18.79 ? 136 SER C CA  1 
ATOM   5487  C  C   . SER C  1 136 ? 7.892   23.295  36.493  1.00 19.71 ? 136 SER C C   1 
ATOM   5488  O  O   . SER C  1 136 ? 7.686   24.467  36.050  1.00 19.51 ? 136 SER C O   1 
ATOM   5489  C  CB  . SER C  1 136 ? 6.101   23.014  38.248  1.00 21.52 ? 136 SER C CB  1 
ATOM   5490  O  OG  . SER C  1 136 ? 5.570   22.020  37.389  1.00 26.54 ? 136 SER C OG  1 
ATOM   5491  N  N   . GLU C  1 137 ? 8.320   22.256  35.753  1.00 16.70 ? 137 GLU C N   1 
ATOM   5492  C  CA  . GLU C  1 137 ? 8.664   22.456  34.314  1.00 17.12 ? 137 GLU C CA  1 
ATOM   5493  C  C   . GLU C  1 137 ? 9.619   23.589  34.047  1.00 17.54 ? 137 GLU C C   1 
ATOM   5494  O  O   . GLU C  1 137 ? 9.563   24.265  32.995  1.00 14.95 ? 137 GLU C O   1 
ATOM   5495  C  CB  . GLU C  1 137 ? 7.353   22.636  33.503  1.00 17.00 ? 137 GLU C CB  1 
ATOM   5496  C  CG  . GLU C  1 137 ? 6.670   21.232  33.565  1.00 25.14 ? 137 GLU C CG  1 
ATOM   5497  C  CD  . GLU C  1 137 ? 5.267   21.234  33.057  1.00 38.00 ? 137 GLU C CD  1 
ATOM   5498  O  OE1 . GLU C  1 137 ? 4.572   22.276  33.113  1.00 41.90 ? 137 GLU C OE1 1 
ATOM   5499  O  OE2 . GLU C  1 137 ? 4.835   20.135  32.628  1.00 45.87 ? 137 GLU C OE2 1 
ATOM   5500  N  N   . GLY C  1 138 ? 10.486  23.890  34.990  1.00 11.54 ? 138 GLY C N   1 
ATOM   5501  C  CA  . GLY C  1 138 ? 11.269  25.051  34.917  1.00 12.33 ? 138 GLY C CA  1 
ATOM   5502  C  C   . GLY C  1 138 ? 12.342  25.113  33.819  1.00 9.57  ? 138 GLY C C   1 
ATOM   5503  O  O   . GLY C  1 138 ? 12.713  26.180  33.308  1.00 11.05 ? 138 GLY C O   1 
ATOM   5504  N  N   . LEU C  1 139 ? 13.030  23.951  33.700  1.00 9.00  ? 139 LEU C N   1 
ATOM   5505  C  CA  . LEU C  1 139 ? 14.294  23.895  32.931  1.00 9.61  ? 139 LEU C CA  1 
ATOM   5506  C  C   . LEU C  1 139 ? 14.296  22.776  31.894  1.00 5.57  ? 139 LEU C C   1 
ATOM   5507  O  O   . LEU C  1 139 ? 13.600  21.742  32.027  1.00 7.41  ? 139 LEU C O   1 
ATOM   5508  C  CB  . LEU C  1 139 ? 15.465  23.597  33.945  1.00 8.43  ? 139 LEU C CB  1 
ATOM   5509  C  CG  . LEU C  1 139 ? 15.632  24.718  35.027  1.00 8.47  ? 139 LEU C CG  1 
ATOM   5510  C  CD1 . LEU C  1 139 ? 16.741  24.232  35.965  1.00 10.11 ? 139 LEU C CD1 1 
ATOM   5511  C  CD2 . LEU C  1 139 ? 15.964  26.112  34.415  1.00 11.54 ? 139 LEU C CD2 1 
ATOM   5512  N  N   . ALA C  1 140 ? 15.063  23.032  30.825  1.00 6.18  ? 140 ALA C N   1 
ATOM   5513  C  CA  . ALA C  1 140 ? 15.323  21.993  29.808  1.00 7.70  ? 140 ALA C CA  1 
ATOM   5514  C  C   . ALA C  1 140 ? 16.805  22.122  29.432  1.00 6.95  ? 140 ALA C C   1 
ATOM   5515  O  O   . ALA C  1 140 ? 17.302  23.219  29.161  1.00 7.73  ? 140 ALA C O   1 
ATOM   5516  C  CB  . ALA C  1 140 ? 14.405  22.164  28.518  1.00 8.37  ? 140 ALA C CB  1 
ATOM   5517  N  N   . VAL C  1 141 ? 17.506  20.981  29.572  1.00 5.72  ? 141 VAL C N   1 
ATOM   5518  C  CA  . VAL C  1 141 ? 18.924  20.932  29.238  1.00 6.52  ? 141 VAL C CA  1 
ATOM   5519  C  C   . VAL C  1 141 ? 19.142  19.999  28.063  1.00 6.71  ? 141 VAL C C   1 
ATOM   5520  O  O   . VAL C  1 141 ? 18.582  18.848  28.055  1.00 7.78  ? 141 VAL C O   1 
ATOM   5521  C  CB  . VAL C  1 141 ? 19.782  20.540  30.472  1.00 6.08  ? 141 VAL C CB  1 
ATOM   5522  C  CG1 . VAL C  1 141 ? 21.266  20.689  30.112  1.00 6.32  ? 141 VAL C CG1 1 
ATOM   5523  C  CG2 . VAL C  1 141 ? 19.438  21.555  31.600  1.00 7.60  ? 141 VAL C CG2 1 
ATOM   5524  N  N   . LEU C  1 142 ? 19.924  20.462  27.118  1.00 5.28  ? 142 LEU C N   1 
ATOM   5525  C  CA  . LEU C  1 142 ? 20.410  19.598  26.035  1.00 6.08  ? 142 LEU C CA  1 
ATOM   5526  C  C   . LEU C  1 142 ? 21.827  19.034  26.379  1.00 5.06  ? 142 LEU C C   1 
ATOM   5527  O  O   . LEU C  1 142 ? 22.678  19.852  26.815  1.00 5.74  ? 142 LEU C O   1 
ATOM   5528  C  CB  . LEU C  1 142 ? 20.554  20.372  24.699  1.00 6.84  ? 142 LEU C CB  1 
ATOM   5529  C  CG  . LEU C  1 142 ? 19.288  21.147  24.268  1.00 7.72  ? 142 LEU C CG  1 
ATOM   5530  C  CD1 . LEU C  1 142 ? 19.593  21.809  22.897  1.00 11.21 ? 142 LEU C CD1 1 
ATOM   5531  C  CD2 . LEU C  1 142 ? 18.123  20.164  24.117  1.00 11.28 ? 142 LEU C CD2 1 
ATOM   5532  N  N   . ALA C  1 143 ? 22.040  17.720  26.264  1.00 5.77  ? 143 ALA C N   1 
ATOM   5533  C  CA  . ALA C  1 143 ? 23.365  17.172  26.583  1.00 5.58  ? 143 ALA C CA  1 
ATOM   5534  C  C   . ALA C  1 143 ? 23.985  16.607  25.292  1.00 6.82  ? 143 ALA C C   1 
ATOM   5535  O  O   . ALA C  1 143 ? 23.304  15.763  24.584  1.00 6.34  ? 143 ALA C O   1 
ATOM   5536  C  CB  . ALA C  1 143 ? 23.221  16.017  27.606  1.00 5.68  ? 143 ALA C CB  1 
ATOM   5537  N  N   . VAL C  1 144 ? 25.243  16.992  25.045  1.00 4.72  ? 144 VAL C N   1 
ATOM   5538  C  CA  . VAL C  1 144 ? 26.047  16.369  23.945  1.00 6.09  ? 144 VAL C CA  1 
ATOM   5539  C  C   . VAL C  1 144 ? 27.195  15.553  24.559  1.00 5.28  ? 144 VAL C C   1 
ATOM   5540  O  O   . VAL C  1 144 ? 27.983  16.108  25.328  1.00 6.15  ? 144 VAL C O   1 
ATOM   5541  C  CB  . VAL C  1 144 ? 26.604  17.466  22.987  1.00 6.24  ? 144 VAL C CB  1 
ATOM   5542  C  CG1 . VAL C  1 144 ? 27.318  16.797  21.851  1.00 6.19  ? 144 VAL C CG1 1 
ATOM   5543  C  CG2 . VAL C  1 144 ? 25.473  18.358  22.481  1.00 6.67  ? 144 VAL C CG2 1 
ATOM   5544  N  N   . LEU C  1 145 ? 27.222  14.275  24.187  1.00 5.86  ? 145 LEU C N   1 
ATOM   5545  C  CA  . LEU C  1 145 ? 28.324  13.411  24.659  1.00 7.55  ? 145 LEU C CA  1 
ATOM   5546  C  C   . LEU C  1 145 ? 29.563  13.719  23.797  1.00 6.76  ? 145 LEU C C   1 
ATOM   5547  O  O   . LEU C  1 145 ? 29.385  13.894  22.564  1.00 7.08  ? 145 LEU C O   1 
ATOM   5548  C  CB  . LEU C  1 145 ? 27.901  11.962  24.553  1.00 6.95  ? 145 LEU C CB  1 
ATOM   5549  C  CG  . LEU C  1 145 ? 26.658  11.569  25.403  1.00 6.90  ? 145 LEU C CG  1 
ATOM   5550  C  CD1 . LEU C  1 145 ? 26.056  10.243  24.940  1.00 7.90  ? 145 LEU C CD1 1 
ATOM   5551  C  CD2 . LEU C  1 145 ? 26.941  11.458  26.839  1.00 9.77  ? 145 LEU C CD2 1 
ATOM   5552  N  N   . ILE C  1 146 ? 30.752  13.814  24.400  1.00 6.23  ? 146 ILE C N   1 
ATOM   5553  C  CA  . ILE C  1 146 ? 31.988  14.147  23.721  1.00 5.30  ? 146 ILE C CA  1 
ATOM   5554  C  C   . ILE C  1 146 ? 33.007  12.971  23.829  1.00 7.07  ? 146 ILE C C   1 
ATOM   5555  O  O   . ILE C  1 146 ? 33.255  12.522  24.900  1.00 7.04  ? 146 ILE C O   1 
ATOM   5556  C  CB  . ILE C  1 146 ? 32.595  15.447  24.316  1.00 7.23  ? 146 ILE C CB  1 
ATOM   5557  C  CG1 . ILE C  1 146 ? 31.590  16.614  24.166  1.00 6.44  ? 146 ILE C CG1 1 
ATOM   5558  C  CG2 . ILE C  1 146 ? 33.945  15.839  23.619  1.00 7.61  ? 146 ILE C CG2 1 
ATOM   5559  C  CD1 . ILE C  1 146 ? 31.958  17.872  24.982  1.00 9.03  ? 146 ILE C CD1 1 
ATOM   5560  N  N   . GLU C  1 147 ? 33.531  12.557  22.666  1.00 6.33  ? 147 GLU C N   1 
ATOM   5561  C  CA  . GLU C  1 147 ? 34.546  11.487  22.640  1.00 8.30  ? 147 GLU C CA  1 
ATOM   5562  C  C   . GLU C  1 147 ? 35.864  12.076  22.096  1.00 7.72  ? 147 GLU C C   1 
ATOM   5563  O  O   . GLU C  1 147 ? 35.852  13.088  21.315  1.00 8.76  ? 147 GLU C O   1 
ATOM   5564  C  CB  . GLU C  1 147 ? 34.059  10.243  21.909  1.00 12.98 ? 147 GLU C CB  1 
ATOM   5565  C  CG  . GLU C  1 147 ? 33.818  10.354  20.461  1.00 15.98 ? 147 GLU C CG  1 
ATOM   5566  C  CD  . GLU C  1 147 ? 33.463  9.008   19.906  1.00 22.32 ? 147 GLU C CD  1 
ATOM   5567  O  OE1 . GLU C  1 147 ? 32.788  8.231   20.624  1.00 17.87 ? 147 GLU C OE1 1 
ATOM   5568  O  OE2 . GLU C  1 147 ? 33.886  8.713   18.769  1.00 25.30 ? 147 GLU C OE2 1 
ATOM   5569  N  N   . MET C  1 148 ? 37.025  11.482  22.464  1.00 9.07  ? 148 MET C N   1 
ATOM   5570  C  CA  . MET C  1 148 ? 38.251  12.018  21.900  1.00 8.89  ? 148 MET C CA  1 
ATOM   5571  C  C   . MET C  1 148 ? 38.426  11.406  20.483  1.00 10.36 ? 148 MET C C   1 
ATOM   5572  O  O   . MET C  1 148 ? 38.210  10.200  20.261  1.00 12.06 ? 148 MET C O   1 
ATOM   5573  C  CB  . MET C  1 148 ? 39.409  11.526  22.810  1.00 12.07 ? 148 MET C CB  1 
ATOM   5574  C  CG  . MET C  1 148 ? 40.708  12.296  22.570  1.00 10.97 ? 148 MET C CG  1 
ATOM   5575  S  SD  . MET C  1 148 ? 41.666  11.523  21.272  1.00 15.19 ? 148 MET C SD  1 
ATOM   5576  C  CE  . MET C  1 148 ? 42.156  10.021  22.317  1.00 12.22 ? 148 MET C CE  1 
ATOM   5577  N  N   . GLY C  1 149 ? 38.719  12.264  19.544  1.00 8.38  ? 149 GLY C N   1 
ATOM   5578  C  CA  . GLY C  1 149 ? 38.889  11.792  18.135  1.00 9.97  ? 149 GLY C CA  1 
ATOM   5579  C  C   . GLY C  1 149 ? 39.402  12.987  17.303  1.00 7.47  ? 149 GLY C C   1 
ATOM   5580  O  O   . GLY C  1 149 ? 40.499  13.519  17.541  1.00 9.39  ? 149 GLY C O   1 
ATOM   5581  N  N   . SER C  1 150 ? 38.583  13.390  16.325  1.00 8.19  ? 150 SER C N   1 
ATOM   5582  C  CA  . SER C  1 150 ? 38.974  14.472  15.411  1.00 7.21  ? 150 SER C CA  1 
ATOM   5583  C  C   . SER C  1 150 ? 38.923  15.842  16.123  1.00 9.21  ? 150 SER C C   1 
ATOM   5584  O  O   . SER C  1 150 ? 38.037  16.132  16.950  1.00 10.26 ? 150 SER C O   1 
ATOM   5585  C  CB  . SER C  1 150 ? 37.989  14.641  14.261  1.00 9.39  ? 150 SER C CB  1 
ATOM   5586  O  OG  . SER C  1 150 ? 38.024  13.392  13.498  1.00 9.11  ? 150 SER C OG  1 
ATOM   5587  N  N   . PHE C  1 151 ? 39.861  16.690  15.723  1.00 7.78  ? 151 PHE C N   1 
ATOM   5588  C  CA  . PHE C  1 151 ? 39.858  18.139  16.108  1.00 6.79  ? 151 PHE C CA  1 
ATOM   5589  C  C   . PHE C  1 151 ? 38.487  18.688  15.669  1.00 7.46  ? 151 PHE C C   1 
ATOM   5590  O  O   . PHE C  1 151 ? 37.885  18.358  14.603  1.00 8.70  ? 151 PHE C O   1 
ATOM   5591  C  CB  . PHE C  1 151 ? 40.959  18.927  15.320  1.00 7.66  ? 151 PHE C CB  1 
ATOM   5592  C  CG  . PHE C  1 151 ? 40.995  20.380  15.669  1.00 7.90  ? 151 PHE C CG  1 
ATOM   5593  C  CD1 . PHE C  1 151 ? 41.530  20.760  16.902  1.00 9.68  ? 151 PHE C CD1 1 
ATOM   5594  C  CD2 . PHE C  1 151 ? 40.557  21.294  14.783  1.00 9.85  ? 151 PHE C CD2 1 
ATOM   5595  C  CE1 . PHE C  1 151 ? 41.512  22.142  17.228  1.00 10.04 ? 151 PHE C CE1 1 
ATOM   5596  C  CE2 . PHE C  1 151 ? 40.553  22.658  15.093  1.00 13.35 ? 151 PHE C CE2 1 
ATOM   5597  C  CZ  . PHE C  1 151 ? 41.058  23.037  16.349  1.00 11.19 ? 151 PHE C CZ  1 
ATOM   5598  N  N   . ASN C  1 152 ? 37.948  19.573  16.560  1.00 8.90  ? 152 ASN C N   1 
ATOM   5599  C  CA  . ASN C  1 152 ? 36.672  20.200  16.297  1.00 9.36  ? 152 ASN C CA  1 
ATOM   5600  C  C   . ASN C  1 152 ? 36.794  21.751  16.327  1.00 7.97  ? 152 ASN C C   1 
ATOM   5601  O  O   . ASN C  1 152 ? 36.960  22.380  17.385  1.00 8.43  ? 152 ASN C O   1 
ATOM   5602  C  CB  . ASN C  1 152 ? 35.703  19.722  17.465  1.00 8.05  ? 152 ASN C CB  1 
ATOM   5603  C  CG  . ASN C  1 152 ? 34.262  20.026  17.155  1.00 10.67 ? 152 ASN C CG  1 
ATOM   5604  O  OD1 . ASN C  1 152 ? 33.936  21.244  16.822  1.00 9.00  ? 152 ASN C OD1 1 
ATOM   5605  N  ND2 . ASN C  1 152 ? 33.385  19.051  17.256  1.00 7.96  ? 152 ASN C ND2 1 
ATOM   5606  N  N   . PRO C  1 153 ? 36.810  22.390  15.134  1.00 11.06 ? 153 PRO C N   1 
ATOM   5607  C  CA  . PRO C  1 153 ? 37.001  23.845  15.110  1.00 11.30 ? 153 PRO C CA  1 
ATOM   5608  C  C   . PRO C  1 153 ? 35.919  24.621  15.863  1.00 9.98  ? 153 PRO C C   1 
ATOM   5609  O  O   . PRO C  1 153 ? 36.216  25.648  16.539  1.00 12.10 ? 153 PRO C O   1 
ATOM   5610  C  CB  . PRO C  1 153 ? 36.963  24.160  13.593  1.00 11.29 ? 153 PRO C CB  1 
ATOM   5611  C  CG  . PRO C  1 153 ? 37.488  22.794  12.931  1.00 15.81 ? 153 PRO C CG  1 
ATOM   5612  C  CD  . PRO C  1 153 ? 36.699  21.800  13.768  1.00 10.32 ? 153 PRO C CD  1 
ATOM   5613  N  N   . SER C  1 154 ? 34.680  24.096  15.827  1.00 11.05 ? 154 SER C N   1 
ATOM   5614  C  CA  . SER C  1 154 ? 33.577  24.806  16.552  1.00 8.77  ? 154 SER C CA  1 
ATOM   5615  C  C   . SER C  1 154 ? 33.763  24.820  18.100  1.00 7.97  ? 154 SER C C   1 
ATOM   5616  O  O   . SER C  1 154 ? 33.625  25.878  18.780  1.00 8.79  ? 154 SER C O   1 
ATOM   5617  C  CB  . SER C  1 154 ? 32.256  24.222  16.139  1.00 10.75 ? 154 SER C CB  1 
ATOM   5618  O  OG  . SER C  1 154 ? 32.091  24.462  14.710  1.00 13.62 ? 154 SER C OG  1 
ATOM   5619  N  N   . TYR C  1 155 ? 34.074  23.660  18.691  1.00 7.87  ? 155 TYR C N   1 
ATOM   5620  C  CA  . TYR C  1 155 ? 34.425  23.645  20.135  1.00 7.56  ? 155 TYR C CA  1 
ATOM   5621  C  C   . TYR C  1 155 ? 35.625  24.492  20.380  1.00 7.93  ? 155 TYR C C   1 
ATOM   5622  O  O   . TYR C  1 155 ? 35.731  25.039  21.434  1.00 8.33  ? 155 TYR C O   1 
ATOM   5623  C  CB  . TYR C  1 155 ? 34.590  22.177  20.656  1.00 5.72  ? 155 TYR C CB  1 
ATOM   5624  C  CG  . TYR C  1 155 ? 33.259  21.513  20.956  1.00 6.43  ? 155 TYR C CG  1 
ATOM   5625  C  CD1 . TYR C  1 155 ? 32.442  20.965  19.940  1.00 5.88  ? 155 TYR C CD1 1 
ATOM   5626  C  CD2 . TYR C  1 155 ? 32.793  21.446  22.257  1.00 6.43  ? 155 TYR C CD2 1 
ATOM   5627  C  CE1 . TYR C  1 155 ? 31.209  20.377  20.226  1.00 7.35  ? 155 TYR C CE1 1 
ATOM   5628  C  CE2 . TYR C  1 155 ? 31.571  20.863  22.580  1.00 6.39  ? 155 TYR C CE2 1 
ATOM   5629  C  CZ  . TYR C  1 155 ? 30.789  20.287  21.544  1.00 6.41  ? 155 TYR C CZ  1 
ATOM   5630  O  OH  . TYR C  1 155 ? 29.571  19.755  21.849  1.00 7.59  ? 155 TYR C OH  1 
ATOM   5631  N  N   . ASP C  1 156 ? 36.575  24.636  19.416  1.00 7.81  ? 156 ASP C N   1 
ATOM   5632  C  CA  . ASP C  1 156 ? 37.724  25.468  19.687  1.00 8.02  ? 156 ASP C CA  1 
ATOM   5633  C  C   . ASP C  1 156 ? 37.375  26.960  19.815  1.00 7.26  ? 156 ASP C C   1 
ATOM   5634  O  O   . ASP C  1 156 ? 38.145  27.682  20.408  1.00 8.58  ? 156 ASP C O   1 
ATOM   5635  C  CB  . ASP C  1 156 ? 38.873  25.249  18.651  1.00 10.16 ? 156 ASP C CB  1 
ATOM   5636  C  CG  . ASP C  1 156 ? 40.222  25.059  19.313  1.00 12.24 ? 156 ASP C CG  1 
ATOM   5637  O  OD1 . ASP C  1 156 ? 41.191  25.728  18.894  1.00 16.66 ? 156 ASP C OD1 1 
ATOM   5638  O  OD2 . ASP C  1 156 ? 40.313  24.243  20.253  1.00 10.63 ? 156 ASP C OD2 1 
ATOM   5639  N  N   A LYS C  1 157 ? 36.237  27.356  19.268  0.50 7.41  ? 157 LYS C N   1 
ATOM   5640  N  N   B LYS C  1 157 ? 36.197  27.326  19.280  0.50 7.73  ? 157 LYS C N   1 
ATOM   5641  C  CA  A LYS C  1 157 ? 35.911  28.779  19.424  0.50 7.02  ? 157 LYS C CA  1 
ATOM   5642  C  CA  B LYS C  1 157 ? 35.679  28.724  19.435  0.50 8.25  ? 157 LYS C CA  1 
ATOM   5643  C  C   A LYS C  1 157 ? 35.729  29.074  20.942  0.50 7.09  ? 157 LYS C C   1 
ATOM   5644  C  C   B LYS C  1 157 ? 35.515  29.080  20.920  0.50 7.71  ? 157 LYS C C   1 
ATOM   5645  O  O   A LYS C  1 157 ? 36.066  30.186  21.430  0.50 8.05  ? 157 LYS C O   1 
ATOM   5646  O  O   B LYS C  1 157 ? 35.532  30.227  21.364  0.50 7.72  ? 157 LYS C O   1 
ATOM   5647  C  CB  A LYS C  1 157 ? 34.686  29.127  18.598  0.50 6.15  ? 157 LYS C CB  1 
ATOM   5648  C  CB  B LYS C  1 157 ? 34.326  28.871  18.728  0.50 8.14  ? 157 LYS C CB  1 
ATOM   5649  C  CG  A LYS C  1 157 ? 35.020  29.130  17.093  0.50 5.97  ? 157 LYS C CG  1 
ATOM   5650  C  CG  B LYS C  1 157 ? 34.489  28.721  17.206  0.50 8.91  ? 157 LYS C CG  1 
ATOM   5651  C  CD  A LYS C  1 157 ? 33.772  29.232  16.179  0.50 9.19  ? 157 LYS C CD  1 
ATOM   5652  C  CD  B LYS C  1 157 ? 33.168  29.009  16.396  0.50 11.01 ? 157 LYS C CD  1 
ATOM   5653  C  CE  A LYS C  1 157 ? 33.997  28.665  14.697  0.50 7.31  ? 157 LYS C CE  1 
ATOM   5654  C  CE  B LYS C  1 157 ? 33.408  28.930  14.884  0.50 16.73 ? 157 LYS C CE  1 
ATOM   5655  N  NZ  A LYS C  1 157 ? 32.670  28.784  13.921  0.50 7.25  ? 157 LYS C NZ  1 
ATOM   5656  N  NZ  B LYS C  1 157 ? 34.708  29.587  14.578  0.50 15.61 ? 157 LYS C NZ  1 
ATOM   5657  N  N   . ILE C  1 158 ? 35.309  28.026  21.714  1.00 7.56  ? 158 ILE C N   1 
ATOM   5658  C  CA  . ILE C  1 158 ? 35.325  28.115  23.207  1.00 7.91  ? 158 ILE C CA  1 
ATOM   5659  C  C   . ILE C  1 158 ? 36.707  27.849  23.777  1.00 7.23  ? 158 ILE C C   1 
ATOM   5660  O  O   . ILE C  1 158 ? 37.272  28.653  24.550  1.00 6.82  ? 158 ILE C O   1 
ATOM   5661  C  CB  . ILE C  1 158 ? 34.274  27.160  23.836  1.00 8.97  ? 158 ILE C CB  1 
ATOM   5662  C  CG1 . ILE C  1 158 ? 32.905  27.617  23.350  1.00 11.13 ? 158 ILE C CG1 1 
ATOM   5663  C  CG2 . ILE C  1 158 ? 34.377  27.190  25.421  1.00 7.83  ? 158 ILE C CG2 1 
ATOM   5664  C  CD1 . ILE C  1 158 ? 31.829  26.627  23.657  1.00 15.77 ? 158 ILE C CD1 1 
ATOM   5665  N  N   . PHE C  1 159 ? 37.276  26.714  23.399  1.00 6.95  ? 159 PHE C N   1 
ATOM   5666  C  CA  . PHE C  1 159 ? 38.498  26.242  24.079  1.00 6.67  ? 159 PHE C CA  1 
ATOM   5667  C  C   . PHE C  1 159 ? 39.736  27.142  23.872  1.00 7.48  ? 159 PHE C C   1 
ATOM   5668  O  O   . PHE C  1 159 ? 40.614  27.166  24.773  1.00 8.67  ? 159 PHE C O   1 
ATOM   5669  C  CB  . PHE C  1 159 ? 38.871  24.826  23.593  1.00 7.05  ? 159 PHE C CB  1 
ATOM   5670  C  CG  . PHE C  1 159 ? 37.814  23.761  23.911  1.00 6.41  ? 159 PHE C CG  1 
ATOM   5671  C  CD1 . PHE C  1 159 ? 36.843  23.922  24.899  1.00 7.31  ? 159 PHE C CD1 1 
ATOM   5672  C  CD2 . PHE C  1 159 ? 37.878  22.527  23.193  1.00 9.22  ? 159 PHE C CD2 1 
ATOM   5673  C  CE1 . PHE C  1 159 ? 35.910  22.886  25.200  1.00 9.65  ? 159 PHE C CE1 1 
ATOM   5674  C  CE2 . PHE C  1 159 ? 36.962  21.515  23.476  1.00 9.54  ? 159 PHE C CE2 1 
ATOM   5675  C  CZ  . PHE C  1 159 ? 36.002  21.669  24.496  1.00 8.85  ? 159 PHE C CZ  1 
ATOM   5676  N  N   . SER C  1 160 ? 39.687  27.879  22.775  1.00 8.18  ? 160 SER C N   1 
ATOM   5677  C  CA  . SER C  1 160 ? 40.886  28.784  22.513  1.00 9.82  ? 160 SER C CA  1 
ATOM   5678  C  C   . SER C  1 160 ? 40.924  29.905  23.531  1.00 10.09 ? 160 SER C C   1 
ATOM   5679  O  O   . SER C  1 160 ? 41.957  30.620  23.601  1.00 11.46 ? 160 SER C O   1 
ATOM   5680  C  CB  . SER C  1 160 ? 40.800  29.412  21.107  1.00 9.02  ? 160 SER C CB  1 
ATOM   5681  O  OG  . SER C  1 160 ? 39.655  30.247  20.990  1.00 11.04 ? 160 SER C OG  1 
ATOM   5682  N  N   . HIS C  1 161 ? 39.917  30.076  24.370  1.00 6.94  ? 161 HIS C N   1 
ATOM   5683  C  CA  . HIS C  1 161 ? 39.965  31.085  25.416  1.00 9.37  ? 161 HIS C CA  1 
ATOM   5684  C  C   . HIS C  1 161 ? 40.248  30.590  26.813  1.00 8.44  ? 161 HIS C C   1 
ATOM   5685  O  O   . HIS C  1 161 ? 40.364  31.372  27.823  1.00 8.59  ? 161 HIS C O   1 
ATOM   5686  C  CB  . HIS C  1 161 ? 38.607  31.845  25.474  1.00 9.72  ? 161 HIS C CB  1 
ATOM   5687  C  CG  . HIS C  1 161 ? 38.287  32.541  24.197  1.00 11.24 ? 161 HIS C CG  1 
ATOM   5688  N  ND1 . HIS C  1 161 ? 38.734  33.845  23.967  1.00 10.86 ? 161 HIS C ND1 1 
ATOM   5689  C  CD2 . HIS C  1 161 ? 37.584  32.143  23.109  1.00 10.16 ? 161 HIS C CD2 1 
ATOM   5690  C  CE1 . HIS C  1 161 ? 38.298  34.196  22.763  1.00 10.83 ? 161 HIS C CE1 1 
ATOM   5691  N  NE2 . HIS C  1 161 ? 37.625  33.181  22.196  1.00 12.82 ? 161 HIS C NE2 1 
ATOM   5692  N  N   . LEU C  1 162 ? 40.485  29.255  26.937  1.00 8.22  ? 162 LEU C N   1 
ATOM   5693  C  CA  . LEU C  1 162 ? 40.621  28.648  28.264  1.00 9.30  ? 162 LEU C CA  1 
ATOM   5694  C  C   . LEU C  1 162 ? 41.810  29.227  29.064  1.00 8.98  ? 162 LEU C C   1 
ATOM   5695  O  O   . LEU C  1 162 ? 41.715  29.437  30.290  1.00 9.97  ? 162 LEU C O   1 
ATOM   5696  C  CB  . LEU C  1 162 ? 40.800  27.119  28.106  1.00 9.05  ? 162 LEU C CB  1 
ATOM   5697  C  CG  . LEU C  1 162 ? 39.598  26.297  27.626  1.00 10.15 ? 162 LEU C CG  1 
ATOM   5698  C  CD1 . LEU C  1 162 ? 40.006  24.824  27.405  1.00 11.66 ? 162 LEU C CD1 1 
ATOM   5699  C  CD2 . LEU C  1 162 ? 38.512  26.422  28.705  1.00 17.20 ? 162 LEU C CD2 1 
ATOM   5700  N  N   . GLN C  1 163 ? 42.912  29.494  28.386  1.00 10.01 ? 163 GLN C N   1 
ATOM   5701  C  CA  . GLN C  1 163 ? 44.091  30.077  29.061  1.00 10.62 ? 163 GLN C CA  1 
ATOM   5702  C  C   . GLN C  1 163 ? 43.880  31.481  29.577  1.00 10.16 ? 163 GLN C C   1 
ATOM   5703  O  O   . GLN C  1 163 ? 44.845  31.978  30.255  1.00 10.98 ? 163 GLN C O   1 
ATOM   5704  C  CB  . GLN C  1 163 ? 45.398  30.126  28.177  1.00 12.32 ? 163 GLN C CB  1 
ATOM   5705  C  CG  . GLN C  1 163 ? 45.735  28.728  27.698  1.00 13.04 ? 163 GLN C CG  1 
ATOM   5706  C  CD  . GLN C  1 163 ? 46.075  27.717  28.878  1.00 10.75 ? 163 GLN C CD  1 
ATOM   5707  O  OE1 . GLN C  1 163 ? 46.580  28.079  29.996  1.00 15.49 ? 163 GLN C OE1 1 
ATOM   5708  N  NE2 . GLN C  1 163 ? 45.795  26.392  28.627  1.00 17.06 ? 163 GLN C NE2 1 
ATOM   5709  N  N   . HIS C  1 164 ? 42.734  32.073  29.359  1.00 8.19  ? 164 HIS C N   1 
ATOM   5710  C  CA  . HIS C  1 164 ? 42.485  33.405  29.858  1.00 9.05  ? 164 HIS C CA  1 
ATOM   5711  C  C   . HIS C  1 164 ? 41.361  33.418  30.920  1.00 11.14 ? 164 HIS C C   1 
ATOM   5712  O  O   . HIS C  1 164 ? 40.990  34.491  31.366  1.00 10.28 ? 164 HIS C O   1 
ATOM   5713  C  CB  . HIS C  1 164 ? 42.189  34.340  28.700  1.00 10.47 ? 164 HIS C CB  1 
ATOM   5714  C  CG  . HIS C  1 164 ? 43.365  34.402  27.779  1.00 10.54 ? 164 HIS C CG  1 
ATOM   5715  N  ND1 . HIS C  1 164 ? 43.445  33.764  26.562  1.00 13.26 ? 164 HIS C ND1 1 
ATOM   5716  C  CD2 . HIS C  1 164 ? 44.611  34.908  28.040  1.00 11.04 ? 164 HIS C CD2 1 
ATOM   5717  C  CE1 . HIS C  1 164 ? 44.688  33.912  26.072  1.00 9.94  ? 164 HIS C CE1 1 
ATOM   5718  N  NE2 . HIS C  1 164 ? 45.408  34.554  26.971  1.00 17.78 ? 164 HIS C NE2 1 
ATOM   5719  N  N   . VAL C  1 165 ? 40.874  32.231  31.320  1.00 9.33  ? 165 VAL C N   1 
ATOM   5720  C  CA  . VAL C  1 165 ? 39.888  32.081  32.383  1.00 8.27  ? 165 VAL C CA  1 
ATOM   5721  C  C   . VAL C  1 165 ? 40.345  30.956  33.305  1.00 9.77  ? 165 VAL C C   1 
ATOM   5722  O  O   . VAL C  1 165 ? 39.536  30.218  33.892  1.00 8.73  ? 165 VAL C O   1 
ATOM   5723  C  CB  . VAL C  1 165 ? 38.436  31.771  31.808  1.00 8.68  ? 165 VAL C CB  1 
ATOM   5724  C  CG1 . VAL C  1 165 ? 37.920  33.060  31.179  1.00 9.77  ? 165 VAL C CG1 1 
ATOM   5725  C  CG2 . VAL C  1 165 ? 38.328  30.562  30.927  1.00 9.69  ? 165 VAL C CG2 1 
ATOM   5726  N  N   . LYS C  1 166 ? 41.653  30.872  33.557  1.00 7.64  ? 166 LYS C N   1 
ATOM   5727  C  CA  . LYS C  1 166 ? 42.260  29.756  34.316  1.00 9.99  ? 166 LYS C CA  1 
ATOM   5728  C  C   . LYS C  1 166 ? 41.719  29.678  35.774  1.00 9.06  ? 166 LYS C C   1 
ATOM   5729  O  O   . LYS C  1 166 ? 41.637  28.588  36.312  1.00 9.93  ? 166 LYS C O   1 
ATOM   5730  C  CB  . LYS C  1 166 ? 43.818  29.828  34.367  1.00 9.83  ? 166 LYS C CB  1 
ATOM   5731  C  CG  . LYS C  1 166 ? 44.385  29.767  32.951  1.00 13.56 ? 166 LYS C CG  1 
ATOM   5732  C  CD  . LYS C  1 166 ? 45.929  29.896  32.925  1.00 12.29 ? 166 LYS C CD  1 
ATOM   5733  C  CE  . LYS C  1 166 ? 46.583  28.602  33.410  1.00 13.92 ? 166 LYS C CE  1 
ATOM   5734  N  NZ  . LYS C  1 166 ? 46.205  27.338  32.596  1.00 13.84 ? 166 LYS C NZ  1 
ATOM   5735  N  N   . TYR C  1 167 ? 41.392  30.867  36.385  1.00 8.44  ? 167 TYR C N   1 
ATOM   5736  C  CA  . TYR C  1 167 ? 41.066  30.857  37.835  1.00 9.03  ? 167 TYR C CA  1 
ATOM   5737  C  C   . TYR C  1 167 ? 39.625  31.372  38.060  1.00 9.10  ? 167 TYR C C   1 
ATOM   5738  O  O   . TYR C  1 167 ? 39.020  32.096  37.215  1.00 9.22  ? 167 TYR C O   1 
ATOM   5739  C  CB  . TYR C  1 167 ? 42.080  31.763  38.603  1.00 12.31 ? 167 TYR C CB  1 
ATOM   5740  C  CG  . TYR C  1 167 ? 43.473  31.260  38.473  1.00 14.76 ? 167 TYR C CG  1 
ATOM   5741  C  CD1 . TYR C  1 167 ? 44.345  31.811  37.530  1.00 16.50 ? 167 TYR C CD1 1 
ATOM   5742  C  CD2 . TYR C  1 167 ? 43.920  30.239  39.327  1.00 15.96 ? 167 TYR C CD2 1 
ATOM   5743  C  CE1 . TYR C  1 167 ? 45.645  31.329  37.418  1.00 15.57 ? 167 TYR C CE1 1 
ATOM   5744  C  CE2 . TYR C  1 167 ? 45.223  29.696  39.189  1.00 16.66 ? 167 TYR C CE2 1 
ATOM   5745  C  CZ  . TYR C  1 167 ? 46.070  30.265  38.241  1.00 20.23 ? 167 TYR C CZ  1 
ATOM   5746  O  OH  . TYR C  1 167 ? 47.387  29.767  38.083  1.00 23.44 ? 167 TYR C OH  1 
ATOM   5747  N  N   . LYS C  1 168 ? 39.084  30.938  39.213  1.00 9.59  ? 168 LYS C N   1 
ATOM   5748  C  CA  . LYS C  1 168 ? 37.732  31.261  39.575  1.00 10.59 ? 168 LYS C CA  1 
ATOM   5749  C  C   . LYS C  1 168 ? 37.522  32.762  39.458  1.00 11.79 ? 168 LYS C C   1 
ATOM   5750  O  O   . LYS C  1 168 ? 38.326  33.573  39.958  1.00 12.31 ? 168 LYS C O   1 
ATOM   5751  C  CB  . LYS C  1 168 ? 37.427  30.765  41.003  1.00 11.39 ? 168 LYS C CB  1 
ATOM   5752  C  CG  . LYS C  1 168 ? 36.000  31.130  41.474  1.00 13.07 ? 168 LYS C CG  1 
ATOM   5753  C  CD  . LYS C  1 168 ? 35.676  30.590  42.847  1.00 15.56 ? 168 LYS C CD  1 
ATOM   5754  C  CE  . LYS C  1 168 ? 34.149  30.722  43.024  1.00 21.88 ? 168 LYS C CE  1 
ATOM   5755  N  NZ  . LYS C  1 168 ? 33.782  30.289  44.434  1.00 28.41 ? 168 LYS C NZ  1 
ATOM   5756  N  N   . GLY C  1 169 ? 36.400  33.120  38.875  1.00 11.07 ? 169 GLY C N   1 
ATOM   5757  C  CA  . GLY C  1 169 ? 35.975  34.515  38.754  1.00 11.97 ? 169 GLY C CA  1 
ATOM   5758  C  C   . GLY C  1 169 ? 36.464  35.213  37.491  1.00 12.34 ? 169 GLY C C   1 
ATOM   5759  O  O   . GLY C  1 169 ? 35.942  36.251  37.079  1.00 16.27 ? 169 GLY C O   1 
ATOM   5760  N  N   . GLN C  1 170 ? 37.460  34.585  36.817  1.00 11.14 ? 170 GLN C N   1 
ATOM   5761  C  CA  . GLN C  1 170 ? 37.936  35.218  35.575  1.00 11.29 ? 170 GLN C CA  1 
ATOM   5762  C  C   . GLN C  1 170 ? 36.983  35.099  34.439  1.00 11.17 ? 170 GLN C C   1 
ATOM   5763  O  O   . GLN C  1 170 ? 36.227  34.105  34.363  1.00 10.61 ? 170 GLN C O   1 
ATOM   5764  C  CB  . GLN C  1 170 ? 39.314  34.577  35.257  1.00 11.65 ? 170 GLN C CB  1 
ATOM   5765  C  CG  . GLN C  1 170 ? 40.402  35.062  36.258  1.00 10.53 ? 170 GLN C CG  1 
ATOM   5766  C  CD  . GLN C  1 170 ? 41.741  34.629  35.944  1.00 12.90 ? 170 GLN C CD  1 
ATOM   5767  O  OE1 . GLN C  1 170 ? 42.009  33.591  35.314  1.00 10.77 ? 170 GLN C OE1 1 
ATOM   5768  N  NE2 . GLN C  1 170 ? 42.719  35.424  36.451  1.00 15.57 ? 170 GLN C NE2 1 
ATOM   5769  N  N   . GLU C  1 171 ? 37.012  36.038  33.490  1.00 10.71 ? 171 GLU C N   1 
ATOM   5770  C  CA  . GLU C  1 171 ? 36.048  36.207  32.417  1.00 11.42 ? 171 GLU C CA  1 
ATOM   5771  C  C   . GLU C  1 171 ? 36.752  36.542  31.124  1.00 11.40 ? 171 GLU C C   1 
ATOM   5772  O  O   . GLU C  1 171 ? 37.799  37.256  31.134  1.00 12.84 ? 171 GLU C O   1 
ATOM   5773  C  CB  . GLU C  1 171 ? 35.103  37.393  32.775  1.00 12.24 ? 171 GLU C CB  1 
ATOM   5774  C  CG  . GLU C  1 171 ? 34.188  37.131  33.939  1.00 12.00 ? 171 GLU C CG  1 
ATOM   5775  C  CD  . GLU C  1 171 ? 33.403  38.351  34.399  1.00 15.38 ? 171 GLU C CD  1 
ATOM   5776  O  OE1 . GLU C  1 171 ? 32.418  38.144  35.139  1.00 22.22 ? 171 GLU C OE1 1 
ATOM   5777  O  OE2 . GLU C  1 171 ? 33.752  39.500  34.045  1.00 20.36 ? 171 GLU C OE2 1 
ATOM   5778  N  N   . ALA C  1 172 ? 36.213  36.086  30.017  1.00 9.61  ? 172 ALA C N   1 
ATOM   5779  C  CA  . ALA C  1 172 ? 36.672  36.464  28.684  1.00 8.61  ? 172 ALA C CA  1 
ATOM   5780  C  C   . ALA C  1 172 ? 35.510  36.659  27.781  1.00 11.44 ? 172 ALA C C   1 
ATOM   5781  O  O   . ALA C  1 172 ? 34.414  36.125  28.022  1.00 11.58 ? 172 ALA C O   1 
ATOM   5782  C  CB  . ALA C  1 172 ? 37.590  35.340  28.057  1.00 12.01 ? 172 ALA C CB  1 
ATOM   5783  N  N   . PHE C  1 173 ? 35.684  37.347  26.666  1.00 10.73 ? 173 PHE C N   1 
ATOM   5784  C  CA  . PHE C  1 173 ? 34.681  37.490  25.658  1.00 9.84  ? 173 PHE C CA  1 
ATOM   5785  C  C   . PHE C  1 173 ? 34.892  36.524  24.509  1.00 10.13 ? 173 PHE C C   1 
ATOM   5786  O  O   . PHE C  1 173 ? 36.017  36.392  24.020  1.00 11.00 ? 173 PHE C O   1 
ATOM   5787  C  CB  . PHE C  1 173 ? 34.580  38.972  25.115  1.00 12.42 ? 173 PHE C CB  1 
ATOM   5788  C  CG  . PHE C  1 173 ? 33.867  39.943  26.085  1.00 11.84 ? 173 PHE C CG  1 
ATOM   5789  C  CD1 . PHE C  1 173 ? 34.568  40.901  26.777  1.00 16.45 ? 173 PHE C CD1 1 
ATOM   5790  C  CD2 . PHE C  1 173 ? 32.552  39.704  26.410  1.00 15.87 ? 173 PHE C CD2 1 
ATOM   5791  C  CE1 . PHE C  1 173 ? 33.921  41.780  27.678  1.00 19.85 ? 173 PHE C CE1 1 
ATOM   5792  C  CE2 . PHE C  1 173 ? 31.873  40.552  27.353  1.00 20.81 ? 173 PHE C CE2 1 
ATOM   5793  C  CZ  . PHE C  1 173 ? 32.575  41.596  27.961  1.00 17.11 ? 173 PHE C CZ  1 
ATOM   5794  N  N   . VAL C  1 174 ? 33.776  35.886  24.039  1.00 9.00  ? 174 VAL C N   1 
ATOM   5795  C  CA  . VAL C  1 174 ? 33.829  35.008  22.869  1.00 9.47  ? 174 VAL C CA  1 
ATOM   5796  C  C   . VAL C  1 174 ? 32.871  35.598  21.852  1.00 11.42 ? 174 VAL C C   1 
ATOM   5797  O  O   . VAL C  1 174 ? 31.697  35.807  22.103  1.00 9.35  ? 174 VAL C O   1 
ATOM   5798  C  CB  . VAL C  1 174 ? 33.270  33.654  23.337  1.00 9.45  ? 174 VAL C CB  1 
ATOM   5799  C  CG1 . VAL C  1 174 ? 33.192  32.693  22.140  1.00 8.97  ? 174 VAL C CG1 1 
ATOM   5800  C  CG2 . VAL C  1 174 ? 34.166  33.086  24.450  1.00 9.13  ? 174 VAL C CG2 1 
ATOM   5801  N  N   . PRO C  1 175 ? 33.382  35.903  20.631  1.00 9.63  ? 175 PRO C N   1 
ATOM   5802  C  CA  . PRO C  1 175 ? 32.489  36.325  19.567  1.00 10.24 ? 175 PRO C CA  1 
ATOM   5803  C  C   . PRO C  1 175 ? 31.382  35.368  19.269  1.00 9.97  ? 175 PRO C C   1 
ATOM   5804  O  O   . PRO C  1 175 ? 31.635  34.099  19.331  1.00 10.50 ? 175 PRO C O   1 
ATOM   5805  C  CB  . PRO C  1 175 ? 33.409  36.545  18.345  1.00 11.94 ? 175 PRO C CB  1 
ATOM   5806  C  CG  . PRO C  1 175 ? 34.745  36.756  18.919  1.00 13.08 ? 175 PRO C CG  1 
ATOM   5807  C  CD  . PRO C  1 175 ? 34.792  35.940  20.265  1.00 11.47 ? 175 PRO C CD  1 
ATOM   5808  N  N   . GLY C  1 176 ? 30.218  35.846  18.811  1.00 9.89  ? 176 GLY C N   1 
ATOM   5809  C  CA  . GLY C  1 176 ? 29.192  34.904  18.531  1.00 9.31  ? 176 GLY C CA  1 
ATOM   5810  C  C   . GLY C  1 176 ? 29.583  33.964  17.406  1.00 8.16  ? 176 GLY C C   1 
ATOM   5811  O  O   . GLY C  1 176 ? 30.303  34.284  16.451  1.00 8.99  ? 176 GLY C O   1 
ATOM   5812  N  N   . PHE C  1 177 ? 29.052  32.741  17.545  1.00 8.96  ? 177 PHE C N   1 
ATOM   5813  C  CA  . PHE C  1 177 ? 29.136  31.741  16.486  1.00 7.91  ? 177 PHE C CA  1 
ATOM   5814  C  C   . PHE C  1 177 ? 27.868  30.879  16.529  1.00 8.91  ? 177 PHE C C   1 
ATOM   5815  O  O   . PHE C  1 177 ? 27.048  31.044  17.495  1.00 10.10 ? 177 PHE C O   1 
ATOM   5816  C  CB  . PHE C  1 177 ? 30.396  30.854  16.588  1.00 8.81  ? 177 PHE C CB  1 
ATOM   5817  C  CG  . PHE C  1 177 ? 30.483  29.959  17.825  1.00 9.64  ? 177 PHE C CG  1 
ATOM   5818  C  CD1 . PHE C  1 177 ? 30.182  28.607  17.780  1.00 9.24  ? 177 PHE C CD1 1 
ATOM   5819  C  CD2 . PHE C  1 177 ? 30.842  30.523  19.036  1.00 7.38  ? 177 PHE C CD2 1 
ATOM   5820  C  CE1 . PHE C  1 177 ? 30.263  27.797  18.930  1.00 8.56  ? 177 PHE C CE1 1 
ATOM   5821  C  CE2 . PHE C  1 177 ? 30.953  29.749  20.270  1.00 8.72  ? 177 PHE C CE2 1 
ATOM   5822  C  CZ  . PHE C  1 177 ? 30.686  28.319  20.103  1.00 8.70  ? 177 PHE C CZ  1 
ATOM   5823  N  N   . ASN C  1 178 ? 27.697  29.941  15.586  1.00 8.70  ? 178 ASN C N   1 
ATOM   5824  C  CA  . ASN C  1 178 ? 26.491  29.167  15.514  1.00 9.91  ? 178 ASN C CA  1 
ATOM   5825  C  C   . ASN C  1 178 ? 26.618  27.993  16.489  1.00 8.41  ? 178 ASN C C   1 
ATOM   5826  O  O   . ASN C  1 178 ? 27.374  27.046  16.271  1.00 8.31  ? 178 ASN C O   1 
ATOM   5827  C  CB  . ASN C  1 178 ? 26.322  28.607  14.057  1.00 11.52 ? 178 ASN C CB  1 
ATOM   5828  C  CG  . ASN C  1 178 ? 25.110  27.920  13.895  1.00 12.23 ? 178 ASN C CG  1 
ATOM   5829  O  OD1 . ASN C  1 178 ? 24.255  27.828  14.816  1.00 10.65 ? 178 ASN C OD1 1 
ATOM   5830  N  ND2 . ASN C  1 178 ? 24.946  27.378  12.679  1.00 17.74 ? 178 ASN C ND2 1 
ATOM   5831  N  N   . ILE C  1 179 ? 25.827  28.091  17.578  1.00 8.21  ? 179 ILE C N   1 
ATOM   5832  C  CA  . ILE C  1 179 ? 25.882  27.047  18.615  1.00 7.88  ? 179 ILE C CA  1 
ATOM   5833  C  C   . ILE C  1 179 ? 25.418  25.677  18.029  1.00 9.18  ? 179 ILE C C   1 
ATOM   5834  O  O   . ILE C  1 179 ? 25.763  24.594  18.616  1.00 9.47  ? 179 ILE C O   1 
ATOM   5835  C  CB  . ILE C  1 179 ? 24.998  27.506  19.798  1.00 8.34  ? 179 ILE C CB  1 
ATOM   5836  C  CG1 . ILE C  1 179 ? 25.528  28.832  20.401  1.00 9.46  ? 179 ILE C CG1 1 
ATOM   5837  C  CG2 . ILE C  1 179 ? 24.909  26.333  20.868  1.00 9.54  ? 179 ILE C CG2 1 
ATOM   5838  C  CD1 . ILE C  1 179 ? 27.015  28.829  20.810  1.00 7.91  ? 179 ILE C CD1 1 
ATOM   5839  N  N   . GLU C  1 180 ? 24.659  25.643  16.938  1.00 7.64  ? 180 GLU C N   1 
ATOM   5840  C  CA  . GLU C  1 180 ? 24.289  24.394  16.402  1.00 8.12  ? 180 GLU C CA  1 
ATOM   5841  C  C   . GLU C  1 180 ? 25.500  23.589  15.937  1.00 9.02  ? 180 GLU C C   1 
ATOM   5842  O  O   . GLU C  1 180 ? 25.393  22.331  15.806  1.00 9.41  ? 180 GLU C O   1 
ATOM   5843  C  CB  . GLU C  1 180 ? 23.343  24.572  15.208  1.00 11.24 ? 180 GLU C CB  1 
ATOM   5844  C  CG  . GLU C  1 180 ? 21.960  24.724  15.581  1.00 18.51 ? 180 GLU C CG  1 
ATOM   5845  C  CD  . GLU C  1 180 ? 21.061  24.260  14.388  1.00 17.29 ? 180 GLU C CD  1 
ATOM   5846  O  OE1 . GLU C  1 180 ? 20.671  25.184  13.727  1.00 29.44 ? 180 GLU C OE1 1 
ATOM   5847  O  OE2 . GLU C  1 180 ? 20.838  23.002  14.126  1.00 26.65 ? 180 GLU C OE2 1 
ATOM   5848  N  N   . GLU C  1 181 ? 26.607  24.298  15.629  1.00 8.59  ? 181 GLU C N   1 
ATOM   5849  C  CA  . GLU C  1 181 ? 27.835  23.577  15.301  1.00 10.05 ? 181 GLU C CA  1 
ATOM   5850  C  C   . GLU C  1 181 ? 28.358  22.696  16.451  1.00 10.08 ? 181 GLU C C   1 
ATOM   5851  O  O   . GLU C  1 181 ? 29.246  21.818  16.187  1.00 10.67 ? 181 GLU C O   1 
ATOM   5852  C  CB  . GLU C  1 181 ? 28.951  24.552  14.948  1.00 10.85 ? 181 GLU C CB  1 
ATOM   5853  C  CG  . GLU C  1 181 ? 28.650  25.451  13.706  1.00 12.99 ? 181 GLU C CG  1 
ATOM   5854  C  CD  . GLU C  1 181 ? 29.681  26.570  13.479  1.00 16.48 ? 181 GLU C CD  1 
ATOM   5855  O  OE1 . GLU C  1 181 ? 30.708  26.684  14.210  1.00 15.15 ? 181 GLU C OE1 1 
ATOM   5856  O  OE2 . GLU C  1 181 ? 29.420  27.441  12.552  1.00 16.61 ? 181 GLU C OE2 1 
ATOM   5857  N  N   . LEU C  1 182 ? 27.851  22.924  17.671  1.00 7.48  ? 182 LEU C N   1 
ATOM   5858  C  CA  . LEU C  1 182 ? 28.299  22.077  18.804  1.00 7.76  ? 182 LEU C CA  1 
ATOM   5859  C  C   . LEU C  1 182 ? 27.505  20.761  18.864  1.00 7.44  ? 182 LEU C C   1 
ATOM   5860  O  O   . LEU C  1 182 ? 27.799  19.932  19.705  1.00 8.28  ? 182 LEU C O   1 
ATOM   5861  C  CB  . LEU C  1 182 ? 28.202  22.880  20.161  1.00 7.25  ? 182 LEU C CB  1 
ATOM   5862  C  CG  . LEU C  1 182 ? 28.986  24.161  20.193  1.00 6.71  ? 182 LEU C CG  1 
ATOM   5863  C  CD1 . LEU C  1 182 ? 28.777  24.848  21.582  1.00 8.76  ? 182 LEU C CD1 1 
ATOM   5864  C  CD2 . LEU C  1 182 ? 30.519  23.959  19.892  1.00 8.17  ? 182 LEU C CD2 1 
ATOM   5865  N  N   . LEU C  1 183 ? 26.441  20.671  18.089  1.00 7.65  ? 183 LEU C N   1 
ATOM   5866  C  CA  . LEU C  1 183 ? 25.529  19.507  18.234  1.00 7.76  ? 183 LEU C CA  1 
ATOM   5867  C  C   . LEU C  1 183 ? 26.049  18.424  17.298  1.00 8.47  ? 183 LEU C C   1 
ATOM   5868  O  O   . LEU C  1 183 ? 26.674  18.714  16.280  1.00 8.99  ? 183 LEU C O   1 
ATOM   5869  C  CB  . LEU C  1 183 ? 24.080  19.903  17.858  1.00 9.53  ? 183 LEU C CB  1 
ATOM   5870  C  CG  . LEU C  1 183 ? 23.510  21.096  18.642  1.00 9.53  ? 183 LEU C CG  1 
ATOM   5871  C  CD1 . LEU C  1 183 ? 22.077  21.301  18.223  1.00 11.53 ? 183 LEU C CD1 1 
ATOM   5872  C  CD2 . LEU C  1 183 ? 23.562  20.775  20.170  1.00 11.03 ? 183 LEU C CD2 1 
ATOM   5873  N  N   . PRO C  1 184 ? 25.693  17.177  17.598  1.00 8.87  ? 184 PRO C N   1 
ATOM   5874  C  CA  . PRO C  1 184 ? 26.107  15.978  16.805  1.00 8.29  ? 184 PRO C CA  1 
ATOM   5875  C  C   . PRO C  1 184 ? 25.217  15.813  15.587  1.00 10.25 ? 184 PRO C C   1 
ATOM   5876  O  O   . PRO C  1 184 ? 24.290  16.603  15.317  1.00 10.87 ? 184 PRO C O   1 
ATOM   5877  C  CB  . PRO C  1 184 ? 25.944  14.849  17.815  1.00 10.61 ? 184 PRO C CB  1 
ATOM   5878  C  CG  . PRO C  1 184 ? 24.716  15.256  18.578  1.00 9.61  ? 184 PRO C CG  1 
ATOM   5879  C  CD  . PRO C  1 184 ? 24.925  16.765  18.799  1.00 7.75  ? 184 PRO C CD  1 
ATOM   5880  N  N   . GLU C  1 185 ? 25.641  14.791  14.840  1.00 10.03 ? 185 GLU C N   1 
ATOM   5881  C  CA  . GLU C  1 185 ? 24.809  14.336  13.730  1.00 12.50 ? 185 GLU C CA  1 
ATOM   5882  C  C   . GLU C  1 185 ? 23.467  13.789  14.191  1.00 13.19 ? 185 GLU C C   1 
ATOM   5883  O  O   . GLU C  1 185 ? 23.381  13.213  15.328  1.00 12.40 ? 185 GLU C O   1 
ATOM   5884  C  CB  . GLU C  1 185 ? 25.544  13.206  12.957  1.00 15.81 ? 185 GLU C CB  1 
ATOM   5885  C  CG  . GLU C  1 185 ? 26.763  13.795  12.353  1.00 18.65 ? 185 GLU C CG  1 
ATOM   5886  C  CD  . GLU C  1 185 ? 27.345  12.864  11.280  1.00 35.52 ? 185 GLU C CD  1 
ATOM   5887  O  OE1 . GLU C  1 185 ? 27.104  11.611  11.341  1.00 36.24 ? 185 GLU C OE1 1 
ATOM   5888  O  OE2 . GLU C  1 185 ? 28.052  13.404  10.369  1.00 41.33 ? 185 GLU C OE2 1 
ATOM   5889  N  N   . ARG C  1 186 ? 22.447  13.967  13.371  1.00 11.08 ? 186 ARG C N   1 
ATOM   5890  C  CA  . ARG C  1 186 ? 21.187  13.279  13.552  1.00 12.37 ? 186 ARG C CA  1 
ATOM   5891  C  C   . ARG C  1 186 ? 20.578  13.679  14.930  1.00 9.78  ? 186 ARG C C   1 
ATOM   5892  O  O   . ARG C  1 186 ? 20.188  12.809  15.762  1.00 10.50 ? 186 ARG C O   1 
ATOM   5893  C  CB  . ARG C  1 186 ? 21.273  11.737  13.355  1.00 12.94 ? 186 ARG C CB  1 
ATOM   5894  C  CG  . ARG C  1 186 ? 21.381  11.316  11.874  1.00 17.26 ? 186 ARG C CG  1 
ATOM   5895  C  CD  . ARG C  1 186 ? 21.599  9.788   11.674  1.00 18.58 ? 186 ARG C CD  1 
ATOM   5896  N  NE  . ARG C  1 186 ? 22.819  9.292   12.318  1.00 25.18 ? 186 ARG C NE  1 
ATOM   5897  C  CZ  . ARG C  1 186 ? 24.083  9.503   11.837  1.00 32.99 ? 186 ARG C CZ  1 
ATOM   5898  N  NH1 . ARG C  1 186 ? 25.176  9.032   12.480  1.00 35.48 ? 186 ARG C NH1 1 
ATOM   5899  N  NH2 . ARG C  1 186 ? 24.284  10.187  10.690  1.00 34.63 ? 186 ARG C NH2 1 
ATOM   5900  N  N   . THR C  1 187 ? 20.438  14.996  15.106  1.00 10.82 ? 187 THR C N   1 
ATOM   5901  C  CA  . THR C  1 187 ? 19.845  15.503  16.352  1.00 10.26 ? 187 THR C CA  1 
ATOM   5902  C  C   . THR C  1 187 ? 18.440  15.050  16.546  1.00 9.47  ? 187 THR C C   1 
ATOM   5903  O  O   . THR C  1 187 ? 17.930  15.146  17.669  1.00 8.34  ? 187 THR C O   1 
ATOM   5904  C  CB  . THR C  1 187 ? 19.909  17.036  16.473  1.00 9.94  ? 187 THR C CB  1 
ATOM   5905  O  OG1 . THR C  1 187 ? 19.459  17.602  15.258  1.00 11.52 ? 187 THR C OG1 1 
ATOM   5906  C  CG2 . THR C  1 187 ? 21.375  17.552  16.803  1.00 9.63  ? 187 THR C CG2 1 
ATOM   5907  N  N   . ALA C  1 188 ? 17.779  14.517  15.509  1.00 8.49  ? 188 ALA C N   1 
ATOM   5908  C  CA  . ALA C  1 188 ? 16.404  14.013  15.748  1.00 8.73  ? 188 ALA C CA  1 
ATOM   5909  C  C   . ALA C  1 188 ? 16.450  12.733  16.624  1.00 7.81  ? 188 ALA C C   1 
ATOM   5910  O  O   . ALA C  1 188 ? 15.346  12.322  17.049  1.00 8.47  ? 188 ALA C O   1 
ATOM   5911  C  CB  . ALA C  1 188 ? 15.707  13.633  14.323  1.00 10.19 ? 188 ALA C CB  1 
ATOM   5912  N  N   . GLU C  1 189 ? 17.610  12.147  16.855  1.00 8.37  ? 189 GLU C N   1 
ATOM   5913  C  CA  . GLU C  1 189 ? 17.727  10.898  17.612  1.00 7.08  ? 189 GLU C CA  1 
ATOM   5914  C  C   . GLU C  1 189 ? 18.263  11.266  18.969  1.00 6.12  ? 189 GLU C C   1 
ATOM   5915  O  O   . GLU C  1 189 ? 19.422  11.696  19.103  1.00 7.87  ? 189 GLU C O   1 
ATOM   5916  C  CB  . GLU C  1 189 ? 18.704  9.929   16.951  1.00 9.77  ? 189 GLU C CB  1 
ATOM   5917  C  CG  . GLU C  1 189 ? 18.143  9.499   15.539  1.00 11.16 ? 189 GLU C CG  1 
ATOM   5918  C  CD  . GLU C  1 189 ? 19.014  8.459   14.807  1.00 12.88 ? 189 GLU C CD  1 
ATOM   5919  O  OE1 . GLU C  1 189 ? 19.961  7.918   15.434  1.00 14.86 ? 189 GLU C OE1 1 
ATOM   5920  O  OE2 . GLU C  1 189 ? 18.706  8.185   13.622  1.00 21.37 ? 189 GLU C OE2 1 
ATOM   5921  N  N   . TYR C  1 190 ? 17.406  11.075  19.973  1.00 5.93  ? 190 TYR C N   1 
ATOM   5922  C  CA  . TYR C  1 190 ? 17.781  11.453  21.350  1.00 5.56  ? 190 TYR C CA  1 
ATOM   5923  C  C   . TYR C  1 190 ? 17.061  10.536  22.334  1.00 6.47  ? 190 TYR C C   1 
ATOM   5924  O  O   . TYR C  1 190 ? 16.050  9.881   22.100  1.00 5.58  ? 190 TYR C O   1 
ATOM   5925  C  CB  . TYR C  1 190 ? 17.516  12.967  21.574  1.00 5.85  ? 190 TYR C CB  1 
ATOM   5926  C  CG  . TYR C  1 190 ? 16.096  13.421  21.357  1.00 5.91  ? 190 TYR C CG  1 
ATOM   5927  C  CD1 . TYR C  1 190 ? 15.049  13.212  22.319  1.00 6.81  ? 190 TYR C CD1 1 
ATOM   5928  C  CD2 . TYR C  1 190 ? 15.750  14.061  20.171  1.00 7.01  ? 190 TYR C CD2 1 
ATOM   5929  C  CE1 . TYR C  1 190 ? 13.747  13.635  22.051  1.00 6.48  ? 190 TYR C CE1 1 
ATOM   5930  C  CE2 . TYR C  1 190 ? 14.397  14.459  19.923  1.00 5.48  ? 190 TYR C CE2 1 
ATOM   5931  C  CZ  . TYR C  1 190 ? 13.399  14.277  20.856  1.00 8.03  ? 190 TYR C CZ  1 
ATOM   5932  O  OH  . TYR C  1 190 ? 12.093  14.684  20.699  1.00 7.17  ? 190 TYR C OH  1 
ATOM   5933  N  N   . TYR C  1 191 ? 17.627  10.608  23.588  1.00 6.57  ? 191 TYR C N   1 
ATOM   5934  C  CA  . TYR C  1 191 ? 16.984  10.138  24.807  1.00 6.13  ? 191 TYR C CA  1 
ATOM   5935  C  C   . TYR C  1 191 ? 16.296  11.284  25.509  1.00 6.25  ? 191 TYR C C   1 
ATOM   5936  O  O   . TYR C  1 191 ? 16.863  12.386  25.571  1.00 6.78  ? 191 TYR C O   1 
ATOM   5937  C  CB  . TYR C  1 191 ? 18.035  9.544   25.740  1.00 6.82  ? 191 TYR C CB  1 
ATOM   5938  C  CG  . TYR C  1 191 ? 19.003  8.558   25.177  1.00 6.00  ? 191 TYR C CG  1 
ATOM   5939  C  CD1 . TYR C  1 191 ? 20.231  9.018   24.581  1.00 7.65  ? 191 TYR C CD1 1 
ATOM   5940  C  CD2 . TYR C  1 191 ? 18.781  7.157   25.278  1.00 7.04  ? 191 TYR C CD2 1 
ATOM   5941  C  CE1 . TYR C  1 191 ? 21.196  8.069   24.107  1.00 8.58  ? 191 TYR C CE1 1 
ATOM   5942  C  CE2 . TYR C  1 191 ? 19.726  6.223   24.839  1.00 6.75  ? 191 TYR C CE2 1 
ATOM   5943  C  CZ  . TYR C  1 191 ? 20.901  6.660   24.212  1.00 7.10  ? 191 TYR C CZ  1 
ATOM   5944  O  OH  . TYR C  1 191 ? 21.877  5.746   23.786  1.00 8.54  ? 191 TYR C OH  1 
ATOM   5945  N  N   . ARG C  1 192 ? 15.112  11.024  26.078  1.00 5.73  ? 192 ARG C N   1 
ATOM   5946  C  CA  . ARG C  1 192 ? 14.396  12.071  26.853  1.00 6.21  ? 192 ARG C CA  1 
ATOM   5947  C  C   . ARG C  1 192 ? 13.931  11.514  28.180  1.00 6.09  ? 192 ARG C C   1 
ATOM   5948  O  O   . ARG C  1 192 ? 13.285  10.468  28.225  1.00 7.10  ? 192 ARG C O   1 
ATOM   5949  C  CB  . ARG C  1 192 ? 13.182  12.467  25.938  1.00 6.98  ? 192 ARG C CB  1 
ATOM   5950  C  CG  . ARG C  1 192 ? 12.077  13.197  26.605  1.00 8.19  ? 192 ARG C CG  1 
ATOM   5951  C  CD  . ARG C  1 192 ? 12.520  14.632  27.055  1.00 9.00  ? 192 ARG C CD  1 
ATOM   5952  N  NE  . ARG C  1 192 ? 13.111  15.422  25.972  1.00 10.23 ? 192 ARG C NE  1 
ATOM   5953  C  CZ  . ARG C  1 192 ? 12.433  15.952  24.961  1.00 9.92  ? 192 ARG C CZ  1 
ATOM   5954  N  NH1 . ARG C  1 192 ? 13.066  16.658  24.032  1.00 11.40 ? 192 ARG C NH1 1 
ATOM   5955  N  NH2 . ARG C  1 192 ? 11.119  15.778  24.867  1.00 11.30 ? 192 ARG C NH2 1 
ATOM   5956  N  N   . TYR C  1 193 ? 14.259  12.226  29.251  1.00 5.66  ? 193 TYR C N   1 
ATOM   5957  C  CA  . TYR C  1 193 ? 13.655  11.836  30.535  1.00 6.61  ? 193 TYR C CA  1 
ATOM   5958  C  C   . TYR C  1 193 ? 13.537  13.014  31.484  1.00 4.81  ? 193 TYR C C   1 
ATOM   5959  O  O   . TYR C  1 193 ? 14.179  14.011  31.288  1.00 6.00  ? 193 TYR C O   1 
ATOM   5960  C  CB  . TYR C  1 193 ? 14.498  10.659  31.153  1.00 7.08  ? 193 TYR C CB  1 
ATOM   5961  C  CG  . TYR C  1 193 ? 15.824  11.115  31.759  1.00 5.69  ? 193 TYR C CG  1 
ATOM   5962  C  CD1 . TYR C  1 193 ? 15.960  11.322  33.150  1.00 5.87  ? 193 TYR C CD1 1 
ATOM   5963  C  CD2 . TYR C  1 193 ? 16.895  11.356  30.975  1.00 6.90  ? 193 TYR C CD2 1 
ATOM   5964  C  CE1 . TYR C  1 193 ? 17.143  11.781  33.724  1.00 4.49  ? 193 TYR C CE1 1 
ATOM   5965  C  CE2 . TYR C  1 193 ? 18.112  11.804  31.498  1.00 5.50  ? 193 TYR C CE2 1 
ATOM   5966  C  CZ  . TYR C  1 193 ? 18.293  12.015  32.894  1.00 5.85  ? 193 TYR C CZ  1 
ATOM   5967  O  OH  . TYR C  1 193 ? 19.455  12.454  33.470  1.00 5.00  ? 193 TYR C OH  1 
ATOM   5968  N  N   . ARG C  1 194 ? 12.730  12.856  32.549  1.00 6.87  ? 194 ARG C N   1 
ATOM   5969  C  CA  . ARG C  1 194 ? 12.620  13.896  33.550  1.00 7.86  ? 194 ARG C CA  1 
ATOM   5970  C  C   . ARG C  1 194 ? 13.669  13.673  34.663  1.00 7.16  ? 194 ARG C C   1 
ATOM   5971  O  O   . ARG C  1 194 ? 13.742  12.551  35.245  1.00 6.04  ? 194 ARG C O   1 
ATOM   5972  C  CB  . ARG C  1 194 ? 11.252  13.931  34.271  1.00 10.92 ? 194 ARG C CB  1 
ATOM   5973  C  CG  . ARG C  1 194 ? 10.208  14.424  33.226  1.00 12.78 ? 194 ARG C CG  1 
ATOM   5974  C  CD  . ARG C  1 194 ? 8.714   14.326  33.679  1.00 19.84 ? 194 ARG C CD  1 
ATOM   5975  N  NE  . ARG C  1 194 ? 8.479   14.549  35.113  1.00 36.54 ? 194 ARG C NE  1 
ATOM   5976  C  CZ  . ARG C  1 194 ? 8.316   15.734  35.728  1.00 43.42 ? 194 ARG C CZ  1 
ATOM   5977  N  NH1 . ARG C  1 194 ? 8.322   16.877  35.032  1.00 47.84 ? 194 ARG C NH1 1 
ATOM   5978  N  NH2 . ARG C  1 194 ? 8.139   15.771  37.061  1.00 40.16 ? 194 ARG C NH2 1 
ATOM   5979  N  N   . GLY C  1 195 ? 14.452  14.716  34.981  1.00 5.59  ? 195 GLY C N   1 
ATOM   5980  C  CA  . GLY C  1 195 ? 15.460  14.548  36.014  1.00 7.11  ? 195 GLY C CA  1 
ATOM   5981  C  C   . GLY C  1 195 ? 15.769  15.877  36.672  1.00 5.94  ? 195 GLY C C   1 
ATOM   5982  O  O   . GLY C  1 195 ? 14.845  16.678  36.924  1.00 7.14  ? 195 GLY C O   1 
ATOM   5983  N  N   . SER C  1 196 ? 17.058  16.053  36.970  1.00 4.88  ? 196 SER C N   1 
ATOM   5984  C  CA  . SER C  1 196 ? 17.434  17.151  37.885  1.00 5.17  ? 196 SER C CA  1 
ATOM   5985  C  C   . SER C  1 196 ? 18.668  17.847  37.381  1.00 4.39  ? 196 SER C C   1 
ATOM   5986  O  O   . SER C  1 196 ? 19.400  17.396  36.466  1.00 5.16  ? 196 SER C O   1 
ATOM   5987  C  CB  . SER C  1 196 ? 17.808  16.596  39.264  1.00 6.68  ? 196 SER C CB  1 
ATOM   5988  O  OG  . SER C  1 196 ? 19.140  15.977  39.287  1.00 5.07  ? 196 SER C OG  1 
ATOM   5989  N  N   . LEU C  1 197 ? 18.942  18.978  38.034  1.00 5.79  ? 197 LEU C N   1 
ATOM   5990  C  CA  . LEU C  1 197 ? 20.320  19.599  37.901  1.00 5.86  ? 197 LEU C CA  1 
ATOM   5991  C  C   . LEU C  1 197 ? 21.326  18.556  38.454  1.00 5.35  ? 197 LEU C C   1 
ATOM   5992  O  O   . LEU C  1 197 ? 21.076  17.870  39.481  1.00 5.49  ? 197 LEU C O   1 
ATOM   5993  C  CB  . LEU C  1 197 ? 20.390  20.888  38.771  1.00 7.39  ? 197 LEU C CB  1 
ATOM   5994  C  CG  . LEU C  1 197 ? 19.430  22.031  38.258  1.00 7.49  ? 197 LEU C CG  1 
ATOM   5995  C  CD1 . LEU C  1 197 ? 19.319  23.181  39.312  1.00 9.52  ? 197 LEU C CD1 1 
ATOM   5996  C  CD2 . LEU C  1 197 ? 19.869  22.602  36.944  1.00 9.49  ? 197 LEU C CD2 1 
ATOM   5997  N  N   . THR C  1 198 ? 22.471  18.435  37.777  1.00 4.94  ? 198 THR C N   1 
ATOM   5998  C  CA  . THR C  1 198 ? 23.460  17.435  38.206  1.00 4.45  ? 198 THR C CA  1 
ATOM   5999  C  C   . THR C  1 198 ? 24.548  17.997  39.192  1.00 4.89  ? 198 THR C C   1 
ATOM   6000  O  O   . THR C  1 198 ? 25.468  17.284  39.574  1.00 6.14  ? 198 THR C O   1 
ATOM   6001  C  CB  . THR C  1 198 ? 24.256  16.921  36.975  1.00 5.31  ? 198 THR C CB  1 
ATOM   6002  O  OG1 . THR C  1 198 ? 24.978  18.023  36.422  1.00 5.51  ? 198 THR C OG1 1 
ATOM   6003  C  CG2 . THR C  1 198 ? 23.363  16.229  35.896  1.00 4.93  ? 198 THR C CG2 1 
ATOM   6004  N  N   . THR C  1 199 ? 24.344  19.280  39.583  1.00 5.92  ? 199 THR C N   1 
ATOM   6005  C  CA  . THR C  1 199 ? 25.174  19.886  40.621  1.00 6.78  ? 199 THR C CA  1 
ATOM   6006  C  C   . THR C  1 199 ? 24.213  20.531  41.650  1.00 6.41  ? 199 THR C C   1 
ATOM   6007  O  O   . THR C  1 199 ? 23.056  20.740  41.340  1.00 6.13  ? 199 THR C O   1 
ATOM   6008  C  CB  . THR C  1 199 ? 26.149  20.965  40.098  1.00 9.33  ? 199 THR C CB  1 
ATOM   6009  O  OG1 . THR C  1 199 ? 25.481  22.185  40.016  1.00 11.08 ? 199 THR C OG1 1 
ATOM   6010  C  CG2 . THR C  1 199 ? 26.831  20.574  38.781  1.00 8.19  ? 199 THR C CG2 1 
ATOM   6011  N  N   . PRO C  1 200 ? 24.781  20.743  42.863  1.00 7.10  ? 200 PRO C N   1 
ATOM   6012  C  CA  . PRO C  1 200 ? 23.909  21.559  43.814  1.00 5.90  ? 200 PRO C CA  1 
ATOM   6013  C  C   . PRO C  1 200 ? 23.354  22.790  43.103  1.00 6.40  ? 200 PRO C C   1 
ATOM   6014  O  O   . PRO C  1 200 ? 24.110  23.465  42.347  1.00 8.12  ? 200 PRO C O   1 
ATOM   6015  C  CB  . PRO C  1 200 ? 24.957  21.927  44.900  1.00 7.08  ? 200 PRO C CB  1 
ATOM   6016  C  CG  . PRO C  1 200 ? 25.899  20.710  44.948  1.00 7.27  ? 200 PRO C CG  1 
ATOM   6017  C  CD  . PRO C  1 200 ? 26.098  20.393  43.441  1.00 7.97  ? 200 PRO C CD  1 
ATOM   6018  N  N   . PRO C  1 201 ? 22.072  23.164  43.301  1.00 7.23  ? 201 PRO C N   1 
ATOM   6019  C  CA  . PRO C  1 201 ? 21.177  22.596  44.318  1.00 6.79  ? 201 PRO C CA  1 
ATOM   6020  C  C   . PRO C  1 201 ? 20.389  21.363  43.908  1.00 7.77  ? 201 PRO C C   1 
ATOM   6021  O  O   . PRO C  1 201 ? 19.524  20.945  44.735  1.00 7.43  ? 201 PRO C O   1 
ATOM   6022  C  CB  . PRO C  1 201 ? 20.238  23.775  44.641  1.00 7.82  ? 201 PRO C CB  1 
ATOM   6023  C  CG  . PRO C  1 201 ? 20.249  24.656  43.356  1.00 12.75 ? 201 PRO C CG  1 
ATOM   6024  C  CD  . PRO C  1 201 ? 21.556  24.444  42.714  1.00 8.29  ? 201 PRO C CD  1 
ATOM   6025  N  N   . CYS C  1 202 ? 20.683  20.730  42.734  1.00 5.83  ? 202 CYS C N   1 
ATOM   6026  C  CA  . CYS C  1 202 ? 20.038  19.437  42.370  1.00 6.36  ? 202 CYS C CA  1 
ATOM   6027  C  C   . CYS C  1 202 ? 18.514  19.437  42.169  1.00 5.78  ? 202 CYS C C   1 
ATOM   6028  O  O   . CYS C  1 202 ? 17.901  18.403  42.273  1.00 6.65  ? 202 CYS C O   1 
ATOM   6029  C  CB  . CYS C  1 202 ? 20.369  18.339  43.413  1.00 6.48  ? 202 CYS C CB  1 
ATOM   6030  S  SG  . CYS C  1 202 ? 22.233  18.063  43.654  1.00 6.11  ? 202 CYS C SG  1 
ATOM   6031  N  N   A ASN C  1 203 ? 17.959  20.586  41.785  0.50 7.00  ? 203 ASN C N   1 
ATOM   6032  N  N   B ASN C  1 203 ? 17.941  20.626  41.925  0.50 6.90  ? 203 ASN C N   1 
ATOM   6033  C  CA  A ASN C  1 203 ? 16.510  20.677  41.705  0.50 6.64  ? 203 ASN C CA  1 
ATOM   6034  C  CA  B ASN C  1 203 ? 16.480  20.760  41.847  0.50 5.93  ? 203 ASN C CA  1 
ATOM   6035  C  C   A ASN C  1 203 ? 15.938  19.690  40.689  0.50 5.74  ? 203 ASN C C   1 
ATOM   6036  C  C   B ASN C  1 203 ? 15.979  19.736  40.788  0.50 5.23  ? 203 ASN C C   1 
ATOM   6037  O  O   A ASN C  1 203 ? 16.422  19.596  39.577  0.50 6.29  ? 203 ASN C O   1 
ATOM   6038  O  O   B ASN C  1 203 ? 16.601  19.666  39.734  0.50 6.04  ? 203 ASN C O   1 
ATOM   6039  C  CB  A ASN C  1 203 ? 16.041  22.110  41.441  0.50 8.08  ? 203 ASN C CB  1 
ATOM   6040  C  CB  B ASN C  1 203 ? 16.078  22.200  41.418  0.50 7.17  ? 203 ASN C CB  1 
ATOM   6041  C  CG  A ASN C  1 203 ? 16.495  23.026  42.496  0.50 12.71 ? 203 ASN C CG  1 
ATOM   6042  C  CG  B ASN C  1 203 ? 16.704  23.304  42.272  0.50 9.64  ? 203 ASN C CG  1 
ATOM   6043  O  OD1 A ASN C  1 203 ? 17.679  23.418  42.506  0.50 13.22 ? 203 ASN C OD1 1 
ATOM   6044  O  OD1 B ASN C  1 203 ? 17.184  23.067  43.388  0.50 10.35 ? 203 ASN C OD1 1 
ATOM   6045  N  ND2 A ASN C  1 203 ? 15.589  23.315  43.471  0.50 15.26 ? 203 ASN C ND2 1 
ATOM   6046  N  ND2 B ASN C  1 203 ? 16.669  24.519  41.761  0.50 14.48 ? 203 ASN C ND2 1 
ATOM   6047  N  N   . PRO C  1 204 ? 14.885  18.977  41.049  1.00 6.60  ? 204 PRO C N   1 
ATOM   6048  C  CA  . PRO C  1 204 ? 14.308  17.966  40.149  1.00 5.58  ? 204 PRO C CA  1 
ATOM   6049  C  C   . PRO C  1 204 ? 13.373  18.590  39.099  1.00 8.36  ? 204 PRO C C   1 
ATOM   6050  O  O   . PRO C  1 204 ? 12.212  18.171  38.985  1.00 9.98  ? 204 PRO C O   1 
ATOM   6051  C  CB  . PRO C  1 204 ? 13.566  17.035  41.143  1.00 9.19  ? 204 PRO C CB  1 
ATOM   6052  C  CG  . PRO C  1 204 ? 13.043  17.962  42.203  1.00 8.40  ? 204 PRO C CG  1 
ATOM   6053  C  CD  . PRO C  1 204 ? 14.194  18.958  42.390  1.00 8.26  ? 204 PRO C CD  1 
ATOM   6054  N  N   . THR C  1 205 ? 13.926  19.523  38.341  1.00 6.80  ? 205 THR C N   1 
ATOM   6055  C  CA  . THR C  1 205 ? 13.038  20.426  37.526  1.00 9.52  ? 205 THR C CA  1 
ATOM   6056  C  C   . THR C  1 205 ? 13.472  20.435  36.063  1.00 8.06  ? 205 THR C C   1 
ATOM   6057  O  O   . THR C  1 205 ? 13.123  21.335  35.309  1.00 9.90  ? 205 THR C O   1 
ATOM   6058  C  CB  . THR C  1 205 ? 13.147  21.829  38.015  1.00 10.01 ? 205 THR C CB  1 
ATOM   6059  O  OG1 . THR C  1 205 ? 14.491  22.273  38.181  1.00 9.90  ? 205 THR C OG1 1 
ATOM   6060  C  CG2 . THR C  1 205 ? 12.397  21.834  39.446  1.00 11.87 ? 205 THR C CG2 1 
ATOM   6061  N  N   . VAL C  1 206 ? 14.366  19.466  35.741  1.00 7.47  ? 206 VAL C N   1 
ATOM   6062  C  CA  . VAL C  1 206 ? 14.932  19.449  34.343  1.00 7.54  ? 206 VAL C CA  1 
ATOM   6063  C  C   . VAL C  1 206 ? 14.348  18.391  33.439  1.00 7.33  ? 206 VAL C C   1 
ATOM   6064  O  O   . VAL C  1 206 ? 14.372  17.225  33.731  1.00 7.56  ? 206 VAL C O   1 
ATOM   6065  C  CB  . VAL C  1 206 ? 16.470  19.232  34.401  1.00 6.13  ? 206 VAL C CB  1 
ATOM   6066  C  CG1 . VAL C  1 206 ? 17.065  19.264  32.984  1.00 6.81  ? 206 VAL C CG1 1 
ATOM   6067  C  CG2 . VAL C  1 206 ? 17.201  20.329  35.223  1.00 8.53  ? 206 VAL C CG2 1 
ATOM   6068  N  N   . LEU C  1 207 ? 13.875  18.831  32.268  1.00 6.94  ? 207 LEU C N   1 
ATOM   6069  C  CA  . LEU C  1 207 ? 13.532  17.944  31.140  1.00 7.41  ? 207 LEU C CA  1 
ATOM   6070  C  C   . LEU C  1 207 ? 14.866  17.728  30.394  1.00 6.81  ? 207 LEU C C   1 
ATOM   6071  O  O   . LEU C  1 207 ? 15.413  18.673  29.799  1.00 6.74  ? 207 LEU C O   1 
ATOM   6072  C  CB  . LEU C  1 207 ? 12.415  18.629  30.351  1.00 8.92  ? 207 LEU C CB  1 
ATOM   6073  C  CG  . LEU C  1 207 ? 11.962  17.589  29.328  1.00 11.80 ? 207 LEU C CG  1 
ATOM   6074  C  CD1 . LEU C  1 207 ? 11.189  16.310  29.898  1.00 16.32 ? 207 LEU C CD1 1 
ATOM   6075  C  CD2 . LEU C  1 207 ? 11.069  18.394  28.281  1.00 14.98 ? 207 LEU C CD2 1 
ATOM   6076  N  N   . TRP C  1 208 ? 15.416  16.510  30.469  1.00 5.81  ? 208 TRP C N   1 
ATOM   6077  C  CA  . TRP C  1 208 ? 16.712  16.198  29.766  1.00 5.87  ? 208 TRP C CA  1 
ATOM   6078  C  C   . TRP C  1 208 ? 16.500  15.694  28.348  1.00 5.38  ? 208 TRP C C   1 
ATOM   6079  O  O   . TRP C  1 208 ? 15.592  14.855  28.111  1.00 6.77  ? 208 TRP C O   1 
ATOM   6080  C  CB  . TRP C  1 208 ? 17.469  15.099  30.515  1.00 4.27  ? 208 TRP C CB  1 
ATOM   6081  C  CG  . TRP C  1 208 ? 18.186  15.682  31.706  1.00 5.14  ? 208 TRP C CG  1 
ATOM   6082  C  CD1 . TRP C  1 208 ? 17.756  15.711  33.060  1.00 4.86  ? 208 TRP C CD1 1 
ATOM   6083  C  CD2 . TRP C  1 208 ? 19.438  16.350  31.666  1.00 4.07  ? 208 TRP C CD2 1 
ATOM   6084  N  NE1 . TRP C  1 208 ? 18.685  16.432  33.812  1.00 5.29  ? 208 TRP C NE1 1 
ATOM   6085  C  CE2 . TRP C  1 208 ? 19.719  16.826  33.003  1.00 3.84  ? 208 TRP C CE2 1 
ATOM   6086  C  CE3 . TRP C  1 208 ? 20.384  16.647  30.675  1.00 4.73  ? 208 TRP C CE3 1 
ATOM   6087  C  CZ2 . TRP C  1 208 ? 20.914  17.611  33.338  1.00 4.74  ? 208 TRP C CZ2 1 
ATOM   6088  C  CZ3 . TRP C  1 208 ? 21.539  17.386  31.015  1.00 4.91  ? 208 TRP C CZ3 1 
ATOM   6089  C  CH2 . TRP C  1 208 ? 21.767  17.842  32.340  1.00 5.12  ? 208 TRP C CH2 1 
ATOM   6090  N  N   . THR C  1 209 ? 17.379  16.132  27.426  1.00 6.28  ? 209 THR C N   1 
ATOM   6091  C  CA  . THR C  1 209 ? 17.398  15.587  26.051  1.00 6.11  ? 209 THR C CA  1 
ATOM   6092  C  C   . THR C  1 209 ? 18.883  15.315  25.840  1.00 5.71  ? 209 THR C C   1 
ATOM   6093  O  O   . THR C  1 209 ? 19.708  16.240  25.858  1.00 5.42  ? 209 THR C O   1 
ATOM   6094  C  CB  . THR C  1 209 ? 16.973  16.673  25.021  1.00 5.42  ? 209 THR C CB  1 
ATOM   6095  O  OG1 . THR C  1 209 ? 15.602  17.002  25.285  1.00 7.32  ? 209 THR C OG1 1 
ATOM   6096  C  CG2 . THR C  1 209 ? 17.098  16.080  23.609  1.00 7.70  ? 209 THR C CG2 1 
ATOM   6097  N  N   . VAL C  1 210 ? 19.220  14.007  25.752  1.00 5.58  ? 210 VAL C N   1 
ATOM   6098  C  CA  . VAL C  1 210 ? 20.603  13.630  25.518  1.00 6.47  ? 210 VAL C CA  1 
ATOM   6099  C  C   . VAL C  1 210 ? 20.714  13.112  24.095  1.00 5.60  ? 210 VAL C C   1 
ATOM   6100  O  O   . VAL C  1 210 ? 20.033  12.133  23.731  1.00 6.34  ? 210 VAL C O   1 
ATOM   6101  C  CB  . VAL C  1 210 ? 21.035  12.465  26.510  1.00 6.60  ? 210 VAL C CB  1 
ATOM   6102  C  CG1 . VAL C  1 210 ? 22.546  12.125  26.323  1.00 6.91  ? 210 VAL C CG1 1 
ATOM   6103  C  CG2 . VAL C  1 210 ? 20.780  12.920  28.050  1.00 8.04  ? 210 VAL C CG2 1 
ATOM   6104  N  N   . PHE C  1 211 ? 21.519  13.754  23.263  1.00 6.00  ? 211 PHE C N   1 
ATOM   6105  C  CA  . PHE C  1 211 ? 21.532  13.246  21.868  1.00 6.51  ? 211 PHE C CA  1 
ATOM   6106  C  C   . PHE C  1 211 ? 22.158  11.901  21.782  1.00 7.97  ? 211 PHE C C   1 
ATOM   6107  O  O   . PHE C  1 211 ? 23.073  11.562  22.562  1.00 7.55  ? 211 PHE C O   1 
ATOM   6108  C  CB  . PHE C  1 211 ? 22.223  14.297  20.979  1.00 6.74  ? 211 PHE C CB  1 
ATOM   6109  C  CG  . PHE C  1 211 ? 21.455  15.599  20.916  1.00 7.30  ? 211 PHE C CG  1 
ATOM   6110  C  CD1 . PHE C  1 211 ? 21.918  16.754  21.533  1.00 7.29  ? 211 PHE C CD1 1 
ATOM   6111  C  CD2 . PHE C  1 211 ? 20.228  15.641  20.279  1.00 7.74  ? 211 PHE C CD2 1 
ATOM   6112  C  CE1 . PHE C  1 211 ? 21.175  17.932  21.482  1.00 6.32  ? 211 PHE C CE1 1 
ATOM   6113  C  CE2 . PHE C  1 211 ? 19.488  16.807  20.224  1.00 7.01  ? 211 PHE C CE2 1 
ATOM   6114  C  CZ  . PHE C  1 211 ? 19.959  17.951  20.823  1.00 7.70  ? 211 PHE C CZ  1 
ATOM   6115  N  N   . ARG C  1 212 ? 21.672  11.110  20.819  1.00 6.01  ? 212 ARG C N   1 
ATOM   6116  C  CA  . ARG C  1 212 ? 22.185  9.760   20.707  1.00 7.46  ? 212 ARG C CA  1 
ATOM   6117  C  C   . ARG C  1 212 ? 23.666  9.675   20.343  1.00 6.96  ? 212 ARG C C   1 
ATOM   6118  O  O   . ARG C  1 212 ? 24.394  8.810   20.825  1.00 8.61  ? 212 ARG C O   1 
ATOM   6119  C  CB  . ARG C  1 212 ? 21.304  9.015   19.685  1.00 8.06  ? 212 ARG C CB  1 
ATOM   6120  C  CG  . ARG C  1 212 ? 21.686  7.528   19.553  1.00 9.42  ? 212 ARG C CG  1 
ATOM   6121  C  CD  . ARG C  1 212 ? 21.093  6.895   18.267  1.00 10.80 ? 212 ARG C CD  1 
ATOM   6122  N  NE  . ARG C  1 212 ? 21.263  5.454   18.300  1.00 13.41 ? 212 ARG C NE  1 
ATOM   6123  C  CZ  . ARG C  1 212 ? 20.698  4.668   17.375  1.00 18.18 ? 212 ARG C CZ  1 
ATOM   6124  N  NH1 . ARG C  1 212 ? 20.010  5.197   16.352  1.00 15.53 ? 212 ARG C NH1 1 
ATOM   6125  N  NH2 . ARG C  1 212 ? 20.818  3.346   17.531  1.00 17.36 ? 212 ARG C NH2 1 
ATOM   6126  N  N   . ASN C  1 213 ? 24.077  10.544  19.417  1.00 7.19  ? 213 ASN C N   1 
ATOM   6127  C  CA  . ASN C  1 213 ? 25.436  10.454  18.829  1.00 7.17  ? 213 ASN C CA  1 
ATOM   6128  C  C   . ASN C  1 213 ? 26.352  11.436  19.502  1.00 6.90  ? 213 ASN C C   1 
ATOM   6129  O  O   . ASN C  1 213 ? 25.953  12.601  19.716  1.00 8.02  ? 213 ASN C O   1 
ATOM   6130  C  CB  . ASN C  1 213 ? 25.343  10.733  17.316  1.00 9.65  ? 213 ASN C CB  1 
ATOM   6131  C  CG  . ASN C  1 213 ? 24.515  9.685   16.602  1.00 12.38 ? 213 ASN C CG  1 
ATOM   6132  O  OD1 . ASN C  1 213 ? 24.740  8.508   16.828  1.00 18.11 ? 213 ASN C OD1 1 
ATOM   6133  N  ND2 . ASN C  1 213 ? 23.486  10.130  15.906  1.00 15.87 ? 213 ASN C ND2 1 
ATOM   6134  N  N   . PRO C  1 214 ? 27.596  11.015  19.772  1.00 7.26  ? 214 PRO C N   1 
ATOM   6135  C  CA  . PRO C  1 214 ? 28.567  11.940  20.334  1.00 6.36  ? 214 PRO C CA  1 
ATOM   6136  C  C   . PRO C  1 214 ? 29.201  12.791  19.233  1.00 7.96  ? 214 PRO C C   1 
ATOM   6137  O  O   . PRO C  1 214 ? 29.135  12.531  17.984  1.00 9.52  ? 214 PRO C O   1 
ATOM   6138  C  CB  . PRO C  1 214 ? 29.638  11.001  20.926  1.00 9.81  ? 214 PRO C CB  1 
ATOM   6139  C  CG  . PRO C  1 214 ? 29.656  9.810   19.941  1.00 11.29 ? 214 PRO C CG  1 
ATOM   6140  C  CD  . PRO C  1 214 ? 28.102  9.605   19.668  1.00 9.99  ? 214 PRO C CD  1 
ATOM   6141  N  N   . VAL C  1 215 ? 29.840  13.868  19.683  1.00 6.40  ? 215 VAL C N   1 
ATOM   6142  C  CA  . VAL C  1 215 ? 30.794  14.670  18.867  1.00 7.87  ? 215 VAL C CA  1 
ATOM   6143  C  C   . VAL C  1 215 ? 32.219  14.281  19.239  1.00 8.27  ? 215 VAL C C   1 
ATOM   6144  O  O   . VAL C  1 215 ? 32.424  13.646  20.306  1.00 7.74  ? 215 VAL C O   1 
ATOM   6145  C  CB  . VAL C  1 215 ? 30.599  16.230  19.008  1.00 6.82  ? 215 VAL C CB  1 
ATOM   6146  C  CG1 . VAL C  1 215 ? 29.223  16.605  18.608  1.00 7.12  ? 215 VAL C CG1 1 
ATOM   6147  C  CG2 . VAL C  1 215 ? 31.008  16.656  20.437  1.00 8.09  ? 215 VAL C CG2 1 
ATOM   6148  N  N   . GLN C  1 216 ? 33.188  14.658  18.391  1.00 6.76  ? 216 GLN C N   1 
ATOM   6149  C  CA  . GLN C  1 216 ? 34.594  14.417  18.680  1.00 7.22  ? 216 GLN C CA  1 
ATOM   6150  C  C   . GLN C  1 216 ? 35.324  15.724  18.892  1.00 7.15  ? 216 GLN C C   1 
ATOM   6151  O  O   . GLN C  1 216 ? 35.024  16.696  18.157  1.00 7.84  ? 216 GLN C O   1 
ATOM   6152  C  CB  . GLN C  1 216 ? 35.308  13.598  17.534  1.00 8.31  ? 216 GLN C CB  1 
ATOM   6153  C  CG  . GLN C  1 216 ? 34.774  12.198  17.517  1.00 9.02  ? 216 GLN C CG  1 
ATOM   6154  C  CD  . GLN C  1 216 ? 35.397  11.338  16.493  1.00 12.50 ? 216 GLN C CD  1 
ATOM   6155  O  OE1 . GLN C  1 216 ? 36.367  11.696  15.849  1.00 10.31 ? 216 GLN C OE1 1 
ATOM   6156  N  NE2 . GLN C  1 216 ? 34.891  10.125  16.435  1.00 14.56 ? 216 GLN C NE2 1 
ATOM   6157  N  N   . ILE C  1 217 ? 36.258  15.704  19.865  1.00 7.19  ? 217 ILE C N   1 
ATOM   6158  C  CA  . ILE C  1 217 ? 37.254  16.761  19.946  1.00 8.02  ? 217 ILE C CA  1 
ATOM   6159  C  C   . ILE C  1 217 ? 38.679  16.025  19.961  1.00 7.49  ? 217 ILE C C   1 
ATOM   6160  O  O   . ILE C  1 217 ? 38.735  14.863  20.291  1.00 7.82  ? 217 ILE C O   1 
ATOM   6161  C  CB  . ILE C  1 217 ? 37.060  17.660  21.241  1.00 7.85  ? 217 ILE C CB  1 
ATOM   6162  C  CG1 . ILE C  1 217 ? 37.327  16.892  22.551  1.00 8.42  ? 217 ILE C CG1 1 
ATOM   6163  C  CG2 . ILE C  1 217 ? 35.654  18.391  21.093  1.00 8.11  ? 217 ILE C CG2 1 
ATOM   6164  C  CD1 . ILE C  1 217 ? 37.257  17.738  23.811  1.00 8.06  ? 217 ILE C CD1 1 
ATOM   6165  N  N   . SER C  1 218 ? 39.714  16.811  19.683  1.00 8.13  ? 218 SER C N   1 
ATOM   6166  C  CA  . SER C  1 218 ? 41.024  16.090  19.574  1.00 8.42  ? 218 SER C CA  1 
ATOM   6167  C  C   . SER C  1 218 ? 41.637  15.805  20.908  1.00 10.16 ? 218 SER C C   1 
ATOM   6168  O  O   . SER C  1 218 ? 41.245  16.378  21.950  1.00 9.25  ? 218 SER C O   1 
ATOM   6169  C  CB  . SER C  1 218 ? 42.029  17.039  18.794  1.00 8.64  ? 218 SER C CB  1 
ATOM   6170  O  OG  . SER C  1 218 ? 42.391  18.155  19.570  1.00 11.16 ? 218 SER C OG  1 
ATOM   6171  N  N   . GLN C  1 219 ? 42.739  14.990  20.873  1.00 10.70 ? 219 GLN C N   1 
ATOM   6172  C  CA  . GLN C  1 219 ? 43.435  14.736  22.117  1.00 11.09 ? 219 GLN C CA  1 
ATOM   6173  C  C   . GLN C  1 219 ? 43.930  15.989  22.725  1.00 10.26 ? 219 GLN C C   1 
ATOM   6174  O  O   . GLN C  1 219 ? 43.852  16.090  23.941  1.00 10.40 ? 219 GLN C O   1 
ATOM   6175  C  CB  . GLN C  1 219 ? 44.657  13.855  21.763  1.00 13.33 ? 219 GLN C CB  1 
ATOM   6176  C  CG  . GLN C  1 219 ? 45.546  13.561  23.021  1.00 17.63 ? 219 GLN C CG  1 
ATOM   6177  C  CD  . GLN C  1 219 ? 44.665  12.950  24.209  1.00 26.41 ? 219 GLN C CD  1 
ATOM   6178  O  OE1 . GLN C  1 219 ? 44.495  11.748  24.214  1.00 38.48 ? 219 GLN C OE1 1 
ATOM   6179  N  NE2 . GLN C  1 219 ? 44.130  13.780  25.193  1.00 30.01 ? 219 GLN C NE2 1 
ATOM   6180  N  N   . GLU C  1 220 ? 44.405  16.958  21.932  1.00 9.90  ? 220 GLU C N   1 
ATOM   6181  C  CA  . GLU C  1 220 ? 44.954  18.168  22.528  1.00 11.03 ? 220 GLU C CA  1 
ATOM   6182  C  C   . GLU C  1 220 ? 43.861  19.056  23.081  1.00 10.04 ? 220 GLU C C   1 
ATOM   6183  O  O   . GLU C  1 220 ? 44.103  19.740  24.120  1.00 10.71 ? 220 GLU C O   1 
ATOM   6184  C  CB  . GLU C  1 220 ? 45.749  18.977  21.501  1.00 11.23 ? 220 GLU C CB  1 
ATOM   6185  C  CG  . GLU C  1 220 ? 47.080  18.219  21.008  1.00 14.16 ? 220 GLU C CG  1 
ATOM   6186  C  CD  . GLU C  1 220 ? 46.806  17.010  20.088  1.00 19.98 ? 220 GLU C CD  1 
ATOM   6187  O  OE1 . GLU C  1 220 ? 45.761  16.966  19.401  1.00 14.86 ? 220 GLU C OE1 1 
ATOM   6188  O  OE2 . GLU C  1 220 ? 47.635  16.071  20.097  1.00 27.60 ? 220 GLU C OE2 1 
ATOM   6189  N  N   . GLN C  1 221 ? 42.709  19.078  22.380  1.00 8.98  ? 221 GLN C N   1 
ATOM   6190  C  CA  . GLN C  1 221 ? 41.573  19.868  22.917  1.00 7.72  ? 221 GLN C CA  1 
ATOM   6191  C  C   . GLN C  1 221 ? 41.140  19.286  24.255  1.00 8.60  ? 221 GLN C C   1 
ATOM   6192  O  O   . GLN C  1 221 ? 40.901  20.074  25.226  1.00 8.86  ? 221 GLN C O   1 
ATOM   6193  C  CB  . GLN C  1 221 ? 40.488  19.815  21.929  1.00 8.95  ? 221 GLN C CB  1 
ATOM   6194  C  CG  . GLN C  1 221 ? 40.707  20.708  20.691  1.00 7.64  ? 221 GLN C CG  1 
ATOM   6195  C  CD  . GLN C  1 221 ? 39.506  20.665  19.779  1.00 6.79  ? 221 GLN C CD  1 
ATOM   6196  O  OE1 . GLN C  1 221 ? 39.145  19.615  19.220  1.00 8.65  ? 221 GLN C OE1 1 
ATOM   6197  N  NE2 . GLN C  1 221 ? 38.903  21.835  19.545  1.00 8.70  ? 221 GLN C NE2 1 
ATOM   6198  N  N   . LEU C  1 222 ? 41.001  17.961  24.338  1.00 7.77  ? 222 LEU C N   1 
ATOM   6199  C  CA  . LEU C  1 222 ? 40.608  17.315  25.564  1.00 9.21  ? 222 LEU C CA  1 
ATOM   6200  C  C   . LEU C  1 222 ? 41.605  17.603  26.648  1.00 8.52  ? 222 LEU C C   1 
ATOM   6201  O  O   . LEU C  1 222 ? 41.211  17.939  27.810  1.00 9.29  ? 222 LEU C O   1 
ATOM   6202  C  CB  . LEU C  1 222 ? 40.369  15.780  25.386  1.00 7.25  ? 222 LEU C CB  1 
ATOM   6203  C  CG  . LEU C  1 222 ? 39.954  15.074  26.670  1.00 7.44  ? 222 LEU C CG  1 
ATOM   6204  C  CD1 . LEU C  1 222 ? 38.594  15.593  27.211  1.00 9.24  ? 222 LEU C CD1 1 
ATOM   6205  C  CD2 . LEU C  1 222 ? 39.836  13.583  26.340  1.00 10.91 ? 222 LEU C CD2 1 
ATOM   6206  N  N   . LEU C  1 223 ? 42.934  17.455  26.377  1.00 8.48  ? 223 LEU C N   1 
ATOM   6207  C  CA  . LEU C  1 223 ? 43.914  17.659  27.432  1.00 8.70  ? 223 LEU C CA  1 
ATOM   6208  C  C   . LEU C  1 223 ? 43.878  19.156  27.844  1.00 8.23  ? 223 LEU C C   1 
ATOM   6209  O  O   . LEU C  1 223 ? 44.034  19.457  29.085  1.00 9.19  ? 223 LEU C O   1 
ATOM   6210  C  CB  . LEU C  1 223 ? 45.332  17.261  26.962  1.00 9.81  ? 223 LEU C CB  1 
ATOM   6211  C  CG  . LEU C  1 223 ? 46.412  17.431  28.010  1.00 13.05 ? 223 LEU C CG  1 
ATOM   6212  C  CD1 . LEU C  1 223 ? 46.215  16.349  29.060  1.00 12.10 ? 223 LEU C CD1 1 
ATOM   6213  C  CD2 . LEU C  1 223 ? 47.777  17.350  27.259  1.00 14.64 ? 223 LEU C CD2 1 
ATOM   6214  N  N   . ALA C  1 224 ? 43.657  20.109  26.886  1.00 9.40  ? 224 ALA C N   1 
ATOM   6215  C  CA  . ALA C  1 224 ? 43.555  21.554  27.321  1.00 9.43  ? 224 ALA C CA  1 
ATOM   6216  C  C   . ALA C  1 224 ? 42.396  21.722  28.267  1.00 9.58  ? 224 ALA C C   1 
ATOM   6217  O  O   . ALA C  1 224 ? 42.519  22.349  29.353  1.00 9.78  ? 224 ALA C O   1 
ATOM   6218  C  CB  . ALA C  1 224 ? 43.393  22.435  26.127  1.00 10.26 ? 224 ALA C CB  1 
ATOM   6219  N  N   . LEU C  1 225 ? 41.243  21.181  27.911  1.00 8.33  ? 225 LEU C N   1 
ATOM   6220  C  CA  . LEU C  1 225 ? 40.041  21.300  28.834  1.00 9.54  ? 225 LEU C CA  1 
ATOM   6221  C  C   . LEU C  1 225 ? 40.338  20.727  30.242  1.00 9.35  ? 225 LEU C C   1 
ATOM   6222  O  O   . LEU C  1 225 ? 39.961  21.311  31.285  1.00 9.78  ? 225 LEU C O   1 
ATOM   6223  C  CB  . LEU C  1 225 ? 38.828  20.589  28.170  1.00 7.69  ? 225 LEU C CB  1 
ATOM   6224  C  CG  . LEU C  1 225 ? 37.560  20.690  28.981  1.00 8.30  ? 225 LEU C CG  1 
ATOM   6225  C  CD1 . LEU C  1 225 ? 37.126  22.181  29.033  1.00 9.14  ? 225 LEU C CD1 1 
ATOM   6226  C  CD2 . LEU C  1 225 ? 36.539  19.845  28.233  1.00 10.64 ? 225 LEU C CD2 1 
ATOM   6227  N  N   . GLU C  1 226 ? 41.086  19.577  30.269  1.00 8.53  ? 226 GLU C N   1 
ATOM   6228  C  CA  . GLU C  1 226 ? 41.339  18.897  31.534  1.00 9.13  ? 226 GLU C CA  1 
ATOM   6229  C  C   . GLU C  1 226 ? 42.434  19.603  32.365  1.00 11.05 ? 226 GLU C C   1 
ATOM   6230  O  O   . GLU C  1 226 ? 42.638  19.220  33.524  1.00 14.79 ? 226 GLU C O   1 
ATOM   6231  C  CB  . GLU C  1 226 ? 41.830  17.436  31.290  1.00 8.11  ? 226 GLU C CB  1 
ATOM   6232  C  CG  . GLU C  1 226 ? 40.736  16.543  30.737  1.00 10.15 ? 226 GLU C CG  1 
ATOM   6233  C  CD  . GLU C  1 226 ? 41.244  15.300  30.136  1.00 10.74 ? 226 GLU C CD  1 
ATOM   6234  O  OE1 . GLU C  1 226 ? 42.470  15.275  29.799  1.00 9.93  ? 226 GLU C OE1 1 
ATOM   6235  O  OE2 . GLU C  1 226 ? 40.500  14.305  29.886  1.00 10.04 ? 226 GLU C OE2 1 
ATOM   6236  N  N   . THR C  1 227 ? 43.285  20.441  31.761  1.00 10.15 ? 227 THR C N   1 
ATOM   6237  C  CA  . THR C  1 227 ? 44.489  20.922  32.492  1.00 9.37  ? 227 THR C CA  1 
ATOM   6238  C  C   . THR C  1 227 ? 44.556  22.432  32.561  1.00 10.22 ? 227 THR C C   1 
ATOM   6239  O  O   . THR C  1 227 ? 45.377  23.000  33.349  1.00 11.37 ? 227 THR C O   1 
ATOM   6240  C  CB  . THR C  1 227 ? 45.821  20.411  31.735  1.00 10.36 ? 227 THR C CB  1 
ATOM   6241  O  OG1 . THR C  1 227 ? 45.877  20.935  30.448  1.00 11.40 ? 227 THR C OG1 1 
ATOM   6242  C  CG2 . THR C  1 227 ? 45.997  18.853  31.791  1.00 12.38 ? 227 THR C CG2 1 
ATOM   6243  N  N   . ALA C  1 228 ? 43.669  23.141  31.869  1.00 10.07 ? 228 ALA C N   1 
ATOM   6244  C  CA  . ALA C  1 228 ? 43.808  24.614  31.839  1.00 9.36  ? 228 ALA C CA  1 
ATOM   6245  C  C   . ALA C  1 228 ? 43.324  25.338  33.116  1.00 9.97  ? 228 ALA C C   1 
ATOM   6246  O  O   . ALA C  1 228 ? 43.740  26.452  33.415  1.00 9.67  ? 228 ALA C O   1 
ATOM   6247  C  CB  . ALA C  1 228 ? 43.015  25.225  30.662  1.00 9.20  ? 228 ALA C CB  1 
ATOM   6248  N  N   . LEU C  1 229 ? 42.329  24.732  33.794  1.00 8.25  ? 229 LEU C N   1 
ATOM   6249  C  CA  . LEU C  1 229 ? 41.531  25.455  34.762  1.00 7.63  ? 229 LEU C CA  1 
ATOM   6250  C  C   . LEU C  1 229 ? 41.664  24.998  36.176  1.00 7.11  ? 229 LEU C C   1 
ATOM   6251  O  O   . LEU C  1 229 ? 41.915  23.848  36.484  1.00 8.35  ? 229 LEU C O   1 
ATOM   6252  C  CB  . LEU C  1 229 ? 40.007  25.345  34.408  1.00 7.89  ? 229 LEU C CB  1 
ATOM   6253  C  CG  . LEU C  1 229 ? 39.696  25.601  32.899  1.00 9.10  ? 229 LEU C CG  1 
ATOM   6254  C  CD1 . LEU C  1 229 ? 38.098  25.552  32.803  1.00 11.22 ? 229 LEU C CD1 1 
ATOM   6255  C  CD2 . LEU C  1 229 ? 40.105  27.037  32.523  1.00 7.87  ? 229 LEU C CD2 1 
ATOM   6256  N  N   . TYR C  1 230 ? 41.489  25.978  37.072  1.00 8.61  ? 230 TYR C N   1 
ATOM   6257  C  CA  . TYR C  1 230 ? 41.531  25.749  38.547  1.00 9.97  ? 230 TYR C CA  1 
ATOM   6258  C  C   . TYR C  1 230 ? 40.149  26.162  39.140  1.00 10.93 ? 230 TYR C C   1 
ATOM   6259  O  O   . TYR C  1 230 ? 39.454  27.031  38.620  1.00 10.76 ? 230 TYR C O   1 
ATOM   6260  C  CB  . TYR C  1 230 ? 42.613  26.704  39.220  1.00 10.84 ? 230 TYR C CB  1 
ATOM   6261  C  CG  . TYR C  1 230 ? 43.957  26.218  38.788  1.00 14.74 ? 230 TYR C CG  1 
ATOM   6262  C  CD1 . TYR C  1 230 ? 44.496  26.587  37.524  1.00 15.45 ? 230 TYR C CD1 1 
ATOM   6263  C  CD2 . TYR C  1 230 ? 44.615  25.279  39.555  1.00 15.60 ? 230 TYR C CD2 1 
ATOM   6264  C  CE1 . TYR C  1 230 ? 45.710  26.070  37.066  1.00 21.30 ? 230 TYR C CE1 1 
ATOM   6265  C  CE2 . TYR C  1 230 ? 45.858  24.696  39.072  1.00 20.23 ? 230 TYR C CE2 1 
ATOM   6266  C  CZ  . TYR C  1 230 ? 46.367  25.109  37.819  1.00 23.22 ? 230 TYR C CZ  1 
ATOM   6267  O  OH  . TYR C  1 230 ? 47.538  24.598  37.252  1.00 27.75 ? 230 TYR C OH  1 
ATOM   6268  N  N   . CYS C  1 231 ? 39.768  25.468  40.233  1.00 12.51 ? 231 CYS C N   1 
ATOM   6269  C  CA  . CYS C  1 231 ? 38.553  25.796  40.950  1.00 12.07 ? 231 CYS C CA  1 
ATOM   6270  C  C   . CYS C  1 231 ? 38.674  27.027  41.812  1.00 13.23 ? 231 CYS C C   1 
ATOM   6271  O  O   . CYS C  1 231 ? 37.624  27.666  42.173  1.00 13.91 ? 231 CYS C O   1 
ATOM   6272  C  CB  . CYS C  1 231 ? 38.106  24.671  41.889  1.00 11.98 ? 231 CYS C CB  1 
ATOM   6273  S  SG  . CYS C  1 231 ? 37.683  23.122  41.056  1.00 11.92 ? 231 CYS C SG  1 
ATOM   6274  N  N   . THR C  1 232 ? 39.916  27.327  42.092  1.00 13.88 ? 232 THR C N   1 
ATOM   6275  C  CA  . THR C  1 232 ? 40.302  28.403  43.021  1.00 13.51 ? 232 THR C CA  1 
ATOM   6276  C  C   . THR C  1 232 ? 40.678  29.756  42.393  1.00 15.93 ? 232 THR C C   1 
ATOM   6277  O  O   . THR C  1 232 ? 41.000  29.842  41.218  1.00 14.30 ? 232 THR C O   1 
ATOM   6278  C  CB  . THR C  1 232 ? 41.414  27.836  43.880  1.00 12.62 ? 232 THR C CB  1 
ATOM   6279  O  OG1 . THR C  1 232 ? 42.412  27.160  43.074  1.00 14.64 ? 232 THR C OG1 1 
ATOM   6280  C  CG2 . THR C  1 232 ? 40.766  26.776  44.956  1.00 13.68 ? 232 THR C CG2 1 
ATOM   6281  N  N   . HIS C  1 233 ? 40.592  30.852  43.154  1.00 18.42 ? 233 HIS C N   1 
ATOM   6282  C  CA  . HIS C  1 233 ? 41.080  32.154  42.733  1.00 19.74 ? 233 HIS C CA  1 
ATOM   6283  C  C   . HIS C  1 233 ? 42.580  32.168  42.521  1.00 18.51 ? 233 HIS C C   1 
ATOM   6284  O  O   . HIS C  1 233 ? 43.307  31.379  43.075  1.00 20.30 ? 233 HIS C O   1 
ATOM   6285  C  CB  . HIS C  1 233 ? 40.717  33.190  43.827  1.00 19.68 ? 233 HIS C CB  1 
ATOM   6286  C  CG  . HIS C  1 233 ? 39.273  33.433  43.889  1.00 21.14 ? 233 HIS C CG  1 
ATOM   6287  N  ND1 . HIS C  1 233 ? 38.602  34.100  42.880  1.00 27.99 ? 233 HIS C ND1 1 
ATOM   6288  C  CD2 . HIS C  1 233 ? 38.333  33.038  44.781  1.00 23.76 ? 233 HIS C CD2 1 
ATOM   6289  C  CE1 . HIS C  1 233 ? 37.308  34.151  43.176  1.00 24.43 ? 233 HIS C CE1 1 
ATOM   6290  N  NE2 . HIS C  1 233 ? 37.118  33.490  44.304  1.00 29.76 ? 233 HIS C NE2 1 
ATOM   6291  N  N   . MET C  1 234 ? 43.011  33.122  41.695  1.00 21.95 ? 234 MET C N   1 
ATOM   6292  C  CA  . MET C  1 234 ? 44.404  33.238  41.227  1.00 27.87 ? 234 MET C CA  1 
ATOM   6293  C  C   . MET C  1 234 ? 45.531  33.212  42.264  1.00 30.52 ? 234 MET C C   1 
ATOM   6294  O  O   . MET C  1 234 ? 46.701  32.947  41.947  1.00 34.45 ? 234 MET C O   1 
ATOM   6295  C  CB  . MET C  1 234 ? 44.525  34.491  40.357  1.00 26.29 ? 234 MET C CB  1 
ATOM   6296  C  CG  . MET C  1 234 ? 45.942  34.758  39.937  1.00 31.16 ? 234 MET C CG  1 
ATOM   6297  S  SD  . MET C  1 234 ? 45.866  36.136  38.790  1.00 34.75 ? 234 MET C SD  1 
ATOM   6298  C  CE  . MET C  1 234 ? 45.944  35.224  37.219  1.00 36.37 ? 234 MET C CE  1 
ATOM   6299  N  N   . ASP C  1 235 ? 45.229  33.481  43.497  1.00 31.20 ? 235 ASP C N   1 
ATOM   6300  C  CA  . ASP C  1 235 ? 46.337  33.415  44.462  1.00 32.57 ? 235 ASP C CA  1 
ATOM   6301  C  C   . ASP C  1 235 ? 45.982  32.551  45.702  1.00 31.16 ? 235 ASP C C   1 
ATOM   6302  O  O   . ASP C  1 235 ? 46.434  32.790  46.835  1.00 31.82 ? 235 ASP C O   1 
ATOM   6303  C  CB  . ASP C  1 235 ? 46.666  34.855  44.838  1.00 33.43 ? 235 ASP C CB  1 
ATOM   6304  C  CG  . ASP C  1 235 ? 45.655  35.409  45.838  1.00 37.46 ? 235 ASP C CG  1 
ATOM   6305  O  OD1 . ASP C  1 235 ? 46.027  35.590  47.021  1.00 43.84 ? 235 ASP C OD1 1 
ATOM   6306  O  OD2 . ASP C  1 235 ? 44.467  35.587  45.464  1.00 45.45 ? 235 ASP C OD2 1 
ATOM   6307  N  N   . ASP C  1 236 ? 45.204  31.498  45.507  1.00 28.68 ? 236 ASP C N   1 
ATOM   6308  C  CA  . ASP C  1 236 ? 44.682  30.791  46.657  1.00 26.08 ? 236 ASP C CA  1 
ATOM   6309  C  C   . ASP C  1 236 ? 45.817  29.978  47.359  1.00 25.99 ? 236 ASP C C   1 
ATOM   6310  O  O   . ASP C  1 236 ? 46.616  29.301  46.701  1.00 25.29 ? 236 ASP C O   1 
ATOM   6311  C  CB  . ASP C  1 236 ? 43.568  29.877  46.193  1.00 26.05 ? 236 ASP C CB  1 
ATOM   6312  C  CG  . ASP C  1 236 ? 42.697  29.383  47.327  1.00 23.77 ? 236 ASP C CG  1 
ATOM   6313  O  OD1 . ASP C  1 236 ? 41.479  29.708  47.230  1.00 28.73 ? 236 ASP C OD1 1 
ATOM   6314  O  OD2 . ASP C  1 236 ? 43.195  28.649  48.216  1.00 20.21 ? 236 ASP C OD2 1 
ATOM   6315  N  N   . PRO C  1 237 ? 45.905  30.063  48.723  1.00 25.11 ? 237 PRO C N   1 
ATOM   6316  C  CA  . PRO C  1 237 ? 46.922  29.256  49.462  1.00 25.73 ? 237 PRO C CA  1 
ATOM   6317  C  C   . PRO C  1 237 ? 46.802  27.731  49.228  1.00 25.56 ? 237 PRO C C   1 
ATOM   6318  O  O   . PRO C  1 237 ? 47.792  26.947  49.419  1.00 24.13 ? 237 PRO C O   1 
ATOM   6319  C  CB  . PRO C  1 237 ? 46.606  29.521  50.959  1.00 25.69 ? 237 PRO C CB  1 
ATOM   6320  C  CG  . PRO C  1 237 ? 45.622  30.727  51.006  1.00 26.72 ? 237 PRO C CG  1 
ATOM   6321  C  CD  . PRO C  1 237 ? 45.062  30.918  49.588  1.00 24.10 ? 237 PRO C CD  1 
ATOM   6322  N  N   . SER C  1 238 ? 45.600  27.291  48.791  1.00 24.23 ? 238 SER C N   1 
ATOM   6323  C  CA  . SER C  1 238 ? 45.316  25.859  48.670  1.00 21.67 ? 238 SER C CA  1 
ATOM   6324  C  C   . SER C  1 238 ? 44.688  25.673  47.244  1.00 20.95 ? 238 SER C C   1 
ATOM   6325  O  O   . SER C  1 238 ? 43.468  25.422  47.139  1.00 20.24 ? 238 SER C O   1 
ATOM   6326  C  CB  . SER C  1 238 ? 44.380  25.363  49.770  1.00 22.33 ? 238 SER C CB  1 
ATOM   6327  O  OG  . SER C  1 238 ? 44.999  25.425  51.116  1.00 20.63 ? 238 SER C OG  1 
ATOM   6328  N  N   . PRO C  1 239 ? 45.493  25.826  46.178  1.00 18.63 ? 239 PRO C N   1 
ATOM   6329  C  CA  . PRO C  1 239 ? 44.868  25.630  44.782  1.00 18.49 ? 239 PRO C CA  1 
ATOM   6330  C  C   . PRO C  1 239 ? 44.259  24.252  44.515  1.00 17.97 ? 239 PRO C C   1 
ATOM   6331  O  O   . PRO C  1 239 ? 44.688  23.244  45.102  1.00 17.69 ? 239 PRO C O   1 
ATOM   6332  C  CB  . PRO C  1 239 ? 46.020  25.807  43.836  1.00 15.66 ? 239 PRO C CB  1 
ATOM   6333  C  CG  . PRO C  1 239 ? 47.235  25.611  44.745  1.00 19.88 ? 239 PRO C CG  1 
ATOM   6334  C  CD  . PRO C  1 239 ? 46.893  26.233  46.043  1.00 20.21 ? 239 PRO C CD  1 
ATOM   6335  N  N   . ARG C  1 240 ? 43.180  24.221  43.680  1.00 15.32 ? 240 ARG C N   1 
ATOM   6336  C  CA  . ARG C  1 240 ? 42.540  22.920  43.447  1.00 15.14 ? 240 ARG C CA  1 
ATOM   6337  C  C   . ARG C  1 240 ? 42.331  22.942  41.889  1.00 12.75 ? 240 ARG C C   1 
ATOM   6338  O  O   . ARG C  1 240 ? 41.715  23.875  41.348  1.00 12.55 ? 240 ARG C O   1 
ATOM   6339  C  CB  . ARG C  1 240 ? 41.159  22.759  44.133  1.00 13.66 ? 240 ARG C CB  1 
ATOM   6340  C  CG  . ARG C  1 240 ? 41.339  22.422  45.675  1.00 16.12 ? 240 ARG C CG  1 
ATOM   6341  C  CD  . ARG C  1 240 ? 40.088  22.379  46.469  1.00 17.46 ? 240 ARG C CD  1 
ATOM   6342  N  NE  . ARG C  1 240 ? 39.370  23.651  46.433  1.00 15.80 ? 240 ARG C NE  1 
ATOM   6343  C  CZ  . ARG C  1 240 ? 38.261  23.902  45.721  1.00 17.76 ? 240 ARG C CZ  1 
ATOM   6344  N  NH1 . ARG C  1 240 ? 37.727  22.958  44.888  1.00 15.85 ? 240 ARG C NH1 1 
ATOM   6345  N  NH2 . ARG C  1 240 ? 37.671  25.103  45.792  1.00 18.10 ? 240 ARG C NH2 1 
ATOM   6346  N  N   . GLU C  1 241 ? 42.916  21.932  41.187  1.00 11.35 ? 241 GLU C N   1 
ATOM   6347  C  CA  . GLU C  1 241 ? 42.693  21.791  39.719  1.00 10.27 ? 241 GLU C CA  1 
ATOM   6348  C  C   . GLU C  1 241 ? 41.229  21.454  39.430  1.00 10.14 ? 241 GLU C C   1 
ATOM   6349  O  O   . GLU C  1 241 ? 40.554  20.673  40.181  1.00 10.99 ? 241 GLU C O   1 
ATOM   6350  C  CB  . GLU C  1 241 ? 43.523  20.700  39.135  1.00 12.60 ? 241 GLU C CB  1 
ATOM   6351  C  CG  . GLU C  1 241 ? 45.015  20.903  39.244  1.00 14.19 ? 241 GLU C CG  1 
ATOM   6352  C  CD  . GLU C  1 241 ? 45.729  19.639  38.781  1.00 24.83 ? 241 GLU C CD  1 
ATOM   6353  O  OE1 . GLU C  1 241 ? 45.140  18.538  38.837  1.00 30.68 ? 241 GLU C OE1 1 
ATOM   6354  O  OE2 . GLU C  1 241 ? 46.920  19.702  38.440  1.00 26.51 ? 241 GLU C OE2 1 
ATOM   6355  N  N   . MET C  1 242 ? 40.680  22.071  38.383  1.00 7.44  ? 242 MET C N   1 
ATOM   6356  C  CA  . MET C  1 242 ? 39.327  21.786  37.982  1.00 8.51  ? 242 MET C CA  1 
ATOM   6357  C  C   . MET C  1 242 ? 39.308  20.537  37.072  1.00 7.81  ? 242 MET C C   1 
ATOM   6358  O  O   . MET C  1 242 ? 39.510  20.592  35.838  1.00 8.57  ? 242 MET C O   1 
ATOM   6359  C  CB  . MET C  1 242 ? 38.697  22.980  37.305  1.00 6.48  ? 242 MET C CB  1 
ATOM   6360  C  CG  . MET C  1 242 ? 37.205  22.676  36.994  1.00 8.53  ? 242 MET C CG  1 
ATOM   6361  S  SD  . MET C  1 242 ? 36.386  24.095  36.133  1.00 8.33  ? 242 MET C SD  1 
ATOM   6362  C  CE  . MET C  1 242 ? 36.550  25.490  37.311  1.00 9.96  ? 242 MET C CE  1 
ATOM   6363  N  N   . ILE C  1 243 ? 39.231  19.401  37.745  1.00 6.17  ? 243 ILE C N   1 
ATOM   6364  C  CA  . ILE C  1 243 ? 39.197  18.059  37.106  1.00 7.53  ? 243 ILE C CA  1 
ATOM   6365  C  C   . ILE C  1 243 ? 38.023  17.218  37.690  1.00 6.20  ? 243 ILE C C   1 
ATOM   6366  O  O   . ILE C  1 243 ? 37.585  17.475  38.811  1.00 6.37  ? 243 ILE C O   1 
ATOM   6367  C  CB  . ILE C  1 243 ? 40.572  17.292  37.304  1.00 6.71  ? 243 ILE C CB  1 
ATOM   6368  C  CG1 . ILE C  1 243 ? 40.910  17.269  38.794  1.00 8.05  ? 243 ILE C CG1 1 
ATOM   6369  C  CG2 . ILE C  1 243 ? 41.661  18.032  36.535  1.00 9.73  ? 243 ILE C CG2 1 
ATOM   6370  C  CD1 . ILE C  1 243 ? 42.181  16.355  39.119  1.00 9.00  ? 243 ILE C CD1 1 
ATOM   6371  N  N   . ASN C  1 244 ? 37.614  16.190  36.899  1.00 6.15  ? 244 ASN C N   1 
ATOM   6372  C  CA  . ASN C  1 244 ? 36.638  15.249  37.447  1.00 5.64  ? 244 ASN C CA  1 
ATOM   6373  C  C   . ASN C  1 244 ? 35.393  15.944  37.977  1.00 6.21  ? 244 ASN C C   1 
ATOM   6374  O  O   . ASN C  1 244 ? 34.830  15.499  38.948  1.00 7.17  ? 244 ASN C O   1 
ATOM   6375  C  CB  . ASN C  1 244 ? 37.290  14.314  38.531  1.00 7.52  ? 244 ASN C CB  1 
ATOM   6376  C  CG  . ASN C  1 244 ? 38.498  13.626  37.988  1.00 5.93  ? 244 ASN C CG  1 
ATOM   6377  O  OD1 . ASN C  1 244 ? 38.532  13.207  36.848  1.00 8.03  ? 244 ASN C OD1 1 
ATOM   6378  N  ND2 . ASN C  1 244 ? 39.543  13.577  38.888  1.00 12.19 ? 244 ASN C ND2 1 
ATOM   6379  N  N   . ASN C  1 245 ? 34.923  16.930  37.207  1.00 5.20  ? 245 ASN C N   1 
ATOM   6380  C  CA  . ASN C  1 245 ? 33.730  17.723  37.645  1.00 6.59  ? 245 ASN C CA  1 
ATOM   6381  C  C   . ASN C  1 245 ? 32.490  17.129  36.998  1.00 5.76  ? 245 ASN C C   1 
ATOM   6382  O  O   . ASN C  1 245 ? 31.729  17.821  36.325  1.00 5.97  ? 245 ASN C O   1 
ATOM   6383  C  CB  . ASN C  1 245 ? 33.937  19.211  37.298  1.00 5.99  ? 245 ASN C CB  1 
ATOM   6384  C  CG  . ASN C  1 245 ? 34.078  19.486  35.805  1.00 7.75  ? 245 ASN C CG  1 
ATOM   6385  O  OD1 . ASN C  1 245 ? 34.461  18.595  35.063  1.00 6.33  ? 245 ASN C OD1 1 
ATOM   6386  N  ND2 . ASN C  1 245 ? 33.932  20.803  35.404  1.00 7.45  ? 245 ASN C ND2 1 
ATOM   6387  N  N   . PHE C  1 246 ? 32.256  15.845  37.284  1.00 4.93  ? 246 PHE C N   1 
ATOM   6388  C  CA  . PHE C  1 246 ? 31.069  15.151  36.821  1.00 5.01  ? 246 PHE C CA  1 
ATOM   6389  C  C   . PHE C  1 246 ? 30.506  14.403  38.037  1.00 4.87  ? 246 PHE C C   1 
ATOM   6390  O  O   . PHE C  1 246 ? 31.280  13.931  38.909  1.00 4.80  ? 246 PHE C O   1 
ATOM   6391  C  CB  . PHE C  1 246 ? 31.408  14.181  35.680  1.00 5.93  ? 246 PHE C CB  1 
ATOM   6392  C  CG  . PHE C  1 246 ? 32.346  13.093  36.086  1.00 4.71  ? 246 PHE C CG  1 
ATOM   6393  C  CD1 . PHE C  1 246 ? 31.864  11.791  36.396  1.00 5.21  ? 246 PHE C CD1 1 
ATOM   6394  C  CD2 . PHE C  1 246 ? 33.727  13.271  35.994  1.00 6.50  ? 246 PHE C CD2 1 
ATOM   6395  C  CE1 . PHE C  1 246 ? 32.765  10.797  36.749  1.00 5.94  ? 246 PHE C CE1 1 
ATOM   6396  C  CE2 . PHE C  1 246 ? 34.615  12.228  36.326  1.00 6.25  ? 246 PHE C CE2 1 
ATOM   6397  C  CZ  . PHE C  1 246 ? 34.072  10.988  36.754  1.00 5.58  ? 246 PHE C CZ  1 
ATOM   6398  N  N   . ARG C  1 247 ? 29.210  14.223  38.010  1.00 4.76  ? 247 ARG C N   1 
ATOM   6399  C  CA  . ARG C  1 247 ? 28.559  13.394  39.086  1.00 4.02  ? 247 ARG C CA  1 
ATOM   6400  C  C   . ARG C  1 247 ? 28.451  11.930  38.680  1.00 5.41  ? 247 ARG C C   1 
ATOM   6401  O  O   . ARG C  1 247 ? 28.219  11.649  37.490  1.00 5.03  ? 247 ARG C O   1 
ATOM   6402  C  CB  . ARG C  1 247 ? 27.139  13.947  39.287  1.00 4.40  ? 247 ARG C CB  1 
ATOM   6403  C  CG  . ARG C  1 247 ? 26.451  13.512  40.651  1.00 4.65  ? 247 ARG C CG  1 
ATOM   6404  C  CD  . ARG C  1 247 ? 25.050  14.038  40.698  1.00 4.66  ? 247 ARG C CD  1 
ATOM   6405  N  NE  . ARG C  1 247 ? 24.484  13.892  42.085  1.00 4.63  ? 247 ARG C NE  1 
ATOM   6406  C  CZ  . ARG C  1 247 ? 23.211  14.232  42.371  1.00 5.91  ? 247 ARG C CZ  1 
ATOM   6407  N  NH1 . ARG C  1 247 ? 22.374  14.659  41.437  1.00 5.79  ? 247 ARG C NH1 1 
ATOM   6408  N  NH2 . ARG C  1 247 ? 22.812  14.190  43.651  1.00 4.72  ? 247 ARG C NH2 1 
ATOM   6409  N  N   . GLN C  1 248 ? 28.603  11.001  39.619  1.00 4.94  ? 248 GLN C N   1 
ATOM   6410  C  CA  . GLN C  1 248 ? 28.277  9.583   39.339  1.00 5.31  ? 248 GLN C CA  1 
ATOM   6411  C  C   . GLN C  1 248 ? 26.826  9.477   38.926  1.00 4.52  ? 248 GLN C C   1 
ATOM   6412  O  O   . GLN C  1 248 ? 25.946  10.229  39.365  1.00 4.49  ? 248 GLN C O   1 
ATOM   6413  C  CB  . GLN C  1 248 ? 28.498  8.747   40.568  1.00 4.29  ? 248 GLN C CB  1 
ATOM   6414  C  CG  . GLN C  1 248 ? 29.949  8.798   41.108  1.00 5.78  ? 248 GLN C CG  1 
ATOM   6415  C  CD  . GLN C  1 248 ? 30.886  8.169   40.139  1.00 5.63  ? 248 GLN C CD  1 
ATOM   6416  O  OE1 . GLN C  1 248 ? 31.542  8.893   39.317  1.00 6.98  ? 248 GLN C OE1 1 
ATOM   6417  N  NE2 . GLN C  1 248 ? 30.985  6.806   40.140  1.00 6.93  ? 248 GLN C NE2 1 
ATOM   6418  N  N   . VAL C  1 249 ? 26.616  8.383   38.097  1.00 4.43  ? 249 VAL C N   1 
ATOM   6419  C  CA  . VAL C  1 249 ? 25.194  8.085   37.720  1.00 3.73  ? 249 VAL C CA  1 
ATOM   6420  C  C   . VAL C  1 249 ? 24.306  7.629   38.922  1.00 5.38  ? 249 VAL C C   1 
ATOM   6421  O  O   . VAL C  1 249 ? 24.859  7.155   39.944  1.00 4.74  ? 249 VAL C O   1 
ATOM   6422  C  CB  . VAL C  1 249 ? 25.094  7.046   36.611  1.00 5.04  ? 249 VAL C CB  1 
ATOM   6423  C  CG1 . VAL C  1 249 ? 25.682  7.628   35.311  1.00 6.11  ? 249 VAL C CG1 1 
ATOM   6424  C  CG2 . VAL C  1 249 ? 25.790  5.755   37.008  1.00 6.55  ? 249 VAL C CG2 1 
ATOM   6425  N  N   . GLN C  1 250 ? 23.013  7.986   38.866  1.00 4.48  ? 250 GLN C N   1 
ATOM   6426  C  CA  . GLN C  1 250 ? 22.085  7.794   39.919  1.00 5.00  ? 250 GLN C CA  1 
ATOM   6427  C  C   . GLN C  1 250 ? 21.222  6.551   39.754  1.00 6.54  ? 250 GLN C C   1 
ATOM   6428  O  O   . GLN C  1 250 ? 21.009  6.123   38.607  1.00 6.74  ? 250 GLN C O   1 
ATOM   6429  C  CB  . GLN C  1 250 ? 21.133  9.002   39.989  1.00 6.72  ? 250 GLN C CB  1 
ATOM   6430  C  CG  . GLN C  1 250 ? 21.888  10.375  40.092  1.00 4.71  ? 250 GLN C CG  1 
ATOM   6431  C  CD  . GLN C  1 250 ? 22.626  10.607  41.393  1.00 4.10  ? 250 GLN C CD  1 
ATOM   6432  O  OE1 . GLN C  1 250 ? 21.941  10.755  42.473  1.00 4.97  ? 250 GLN C OE1 1 
ATOM   6433  N  NE2 . GLN C  1 250 ? 23.969  10.652  41.338  1.00 6.65  ? 250 GLN C NE2 1 
ATOM   6434  N  N   . LYS C  1 251 ? 20.634  6.089   40.861  1.00 4.76  ? 251 LYS C N   1 
ATOM   6435  C  CA  . LYS C  1 251 ? 19.639  5.030   40.728  1.00 6.71  ? 251 LYS C CA  1 
ATOM   6436  C  C   . LYS C  1 251 ? 18.507  5.507   39.805  1.00 6.48  ? 251 LYS C C   1 
ATOM   6437  O  O   . LYS C  1 251 ? 18.104  6.674   39.832  1.00 8.89  ? 251 LYS C O   1 
ATOM   6438  C  CB  . LYS C  1 251 ? 18.983  4.719   42.123  1.00 6.33  ? 251 LYS C CB  1 
ATOM   6439  C  CG  . LYS C  1 251 ? 19.898  3.924   43.106  1.00 7.84  ? 251 LYS C CG  1 
ATOM   6440  C  CD  . LYS C  1 251 ? 19.966  2.421   42.632  1.00 7.22  ? 251 LYS C CD  1 
ATOM   6441  C  CE  . LYS C  1 251 ? 20.756  1.512   43.665  1.00 6.52  ? 251 LYS C CE  1 
ATOM   6442  N  NZ  . LYS C  1 251 ? 22.137  1.981   43.796  1.00 5.47  ? 251 LYS C NZ  1 
ATOM   6443  N  N   . PHE C  1 252 ? 17.877  4.520   39.079  1.00 8.60  ? 252 PHE C N   1 
ATOM   6444  C  CA  . PHE C  1 252 ? 16.796  4.933   38.137  1.00 9.86  ? 252 PHE C CA  1 
ATOM   6445  C  C   . PHE C  1 252 ? 15.966  3.715   38.023  1.00 14.74 ? 252 PHE C C   1 
ATOM   6446  O  O   . PHE C  1 252 ? 16.244  2.820   37.200  1.00 17.31 ? 252 PHE C O   1 
ATOM   6447  C  CB  . PHE C  1 252 ? 17.306  5.123   36.703  1.00 10.72 ? 252 PHE C CB  1 
ATOM   6448  C  CG  . PHE C  1 252 ? 16.339  5.868   35.791  1.00 9.22  ? 252 PHE C CG  1 
ATOM   6449  C  CD1 . PHE C  1 252 ? 16.060  7.235   35.988  1.00 11.09 ? 252 PHE C CD1 1 
ATOM   6450  C  CD2 . PHE C  1 252 ? 15.781  5.139   34.719  1.00 11.81 ? 252 PHE C CD2 1 
ATOM   6451  C  CE1 . PHE C  1 252 ? 15.153  7.899   35.081  1.00 15.94 ? 252 PHE C CE1 1 
ATOM   6452  C  CE2 . PHE C  1 252 ? 14.956  5.769   33.810  1.00 12.88 ? 252 PHE C CE2 1 
ATOM   6453  C  CZ  . PHE C  1 252 ? 14.606  7.146   34.019  1.00 13.04 ? 252 PHE C CZ  1 
ATOM   6454  N  N   . ASP C  1 253 ? 15.010  3.698   38.925  1.00 17.24 ? 253 ASP C N   1 
ATOM   6455  C  CA  . ASP C  1 253 ? 14.084  2.491   39.128  1.00 21.04 ? 253 ASP C CA  1 
ATOM   6456  C  C   . ASP C  1 253 ? 12.685  2.922   39.022  1.00 21.51 ? 253 ASP C C   1 
ATOM   6457  O  O   . ASP C  1 253 ? 12.379  4.033   39.473  1.00 21.36 ? 253 ASP C O   1 
ATOM   6458  C  CB  . ASP C  1 253 ? 14.328  1.906   40.504  1.00 17.85 ? 253 ASP C CB  1 
ATOM   6459  C  CG  . ASP C  1 253 ? 15.707  1.277   40.605  1.00 21.18 ? 253 ASP C CG  1 
ATOM   6460  O  OD1 . ASP C  1 253 ? 16.014  0.377   39.778  1.00 30.50 ? 253 ASP C OD1 1 
ATOM   6461  O  OD2 . ASP C  1 253 ? 16.493  1.727   41.457  1.00 15.84 ? 253 ASP C OD2 1 
ATOM   6462  N  N   . GLU C  1 254 ? 11.887  2.025   38.408  1.00 23.39 ? 254 GLU C N   1 
ATOM   6463  C  CA  . GLU C  1 254 ? 10.419  2.109   38.128  1.00 25.08 ? 254 GLU C CA  1 
ATOM   6464  C  C   . GLU C  1 254 ? 10.163  3.268   37.178  1.00 22.76 ? 254 GLU C C   1 
ATOM   6465  O  O   . GLU C  1 254 ? 9.069   3.851   37.203  1.00 25.48 ? 254 GLU C O   1 
ATOM   6466  C  CB  . GLU C  1 254 ? 9.577   2.360   39.394  1.00 26.67 ? 254 GLU C CB  1 
ATOM   6467  C  CG  . GLU C  1 254 ? 9.781   1.435   40.615  1.00 31.72 ? 254 GLU C CG  1 
ATOM   6468  C  CD  . GLU C  1 254 ? 9.841   2.257   41.954  1.00 42.60 ? 254 GLU C CD  1 
ATOM   6469  O  OE1 . GLU C  1 254 ? 8.771   2.627   42.534  1.00 48.33 ? 254 GLU C OE1 1 
ATOM   6470  O  OE2 . GLU C  1 254 ? 10.972  2.523   42.455  1.00 49.72 ? 254 GLU C OE2 1 
ATOM   6471  N  N   A ARG C  1 255 ? 11.151  3.579   36.371  0.50 19.84 ? 255 ARG C N   1 
ATOM   6472  N  N   B ARG C  1 255 ? 11.197  3.668   36.449  0.50 19.28 ? 255 ARG C N   1 
ATOM   6473  C  CA  A ARG C  1 255 ? 11.029  4.692   35.397  0.50 18.71 ? 255 ARG C CA  1 
ATOM   6474  C  CA  B ARG C  1 255 ? 11.121  4.809   35.454  0.50 17.70 ? 255 ARG C CA  1 
ATOM   6475  C  C   A ARG C  1 255 ? 11.658  4.281   34.122  0.50 16.33 ? 255 ARG C C   1 
ATOM   6476  C  C   B ARG C  1 255 ? 11.876  4.488   34.205  0.50 15.16 ? 255 ARG C C   1 
ATOM   6477  O  O   A ARG C  1 255 ? 12.308  3.258   34.044  0.50 16.58 ? 255 ARG C O   1 
ATOM   6478  O  O   B ARG C  1 255 ? 12.836  3.735   34.234  0.50 13.85 ? 255 ARG C O   1 
ATOM   6479  C  CB  A ARG C  1 255 ? 11.780  5.891   35.911  0.50 16.37 ? 255 ARG C CB  1 
ATOM   6480  C  CB  B ARG C  1 255 ? 11.694  6.079   36.049  0.50 15.75 ? 255 ARG C CB  1 
ATOM   6481  C  CG  A ARG C  1 255 ? 11.469  6.183   37.331  0.50 19.15 ? 255 ARG C CG  1 
ATOM   6482  C  CG  B ARG C  1 255 ? 10.856  6.601   37.162  0.50 17.08 ? 255 ARG C CG  1 
ATOM   6483  C  CD  A ARG C  1 255 ? 12.157  7.445   37.679  0.50 8.90  ? 255 ARG C CD  1 
ATOM   6484  C  CD  B ARG C  1 255 ? 11.462  7.840   37.767  0.50 11.85 ? 255 ARG C CD  1 
ATOM   6485  N  NE  A ARG C  1 255 ? 11.865  8.436   36.652  0.50 14.11 ? 255 ARG C NE  1 
ATOM   6486  N  NE  B ARG C  1 255 ? 12.620  7.647   38.635  0.50 15.41 ? 255 ARG C NE  1 
ATOM   6487  C  CZ  A ARG C  1 255 ? 12.551  9.541   36.451  0.50 18.23 ? 255 ARG C CZ  1 
ATOM   6488  C  CZ  B ARG C  1 255 ? 13.766  8.321   38.562  0.50 11.29 ? 255 ARG C CZ  1 
ATOM   6489  N  NH1 A ARG C  1 255 ? 13.609  9.832   37.213  0.50 12.83 ? 255 ARG C NH1 1 
ATOM   6490  N  NH1 B ARG C  1 255 ? 14.052  9.260   37.647  0.50 10.33 ? 255 ARG C NH1 1 
ATOM   6491  N  NH2 A ARG C  1 255 ? 12.198  10.292  35.458  0.50 4.11  ? 255 ARG C NH2 1 
ATOM   6492  N  NH2 B ARG C  1 255 ? 14.666  8.089   39.520  0.50 9.68  ? 255 ARG C NH2 1 
ATOM   6493  N  N   . LEU C  1 256 ? 11.397  5.110   33.112  1.00 15.86 ? 256 LEU C N   1 
ATOM   6494  C  CA  . LEU C  1 256 ? 11.904  4.830   31.770  1.00 13.31 ? 256 LEU C CA  1 
ATOM   6495  C  C   . LEU C  1 256 ? 12.494  6.106   31.160  1.00 11.34 ? 256 LEU C C   1 
ATOM   6496  O  O   . LEU C  1 256 ? 12.204  7.240   31.514  1.00 11.30 ? 256 LEU C O   1 
ATOM   6497  C  CB  . LEU C  1 256 ? 10.807  4.296   30.795  1.00 16.70 ? 256 LEU C CB  1 
ATOM   6498  C  CG  . LEU C  1 256 ? 10.036  3.069   31.319  1.00 17.92 ? 256 LEU C CG  1 
ATOM   6499  C  CD1 . LEU C  1 256 ? 8.803   2.771   30.383  1.00 21.81 ? 256 LEU C CD1 1 
ATOM   6500  C  CD2 . LEU C  1 256 ? 11.012  1.940   31.282  1.00 24.18 ? 256 LEU C CD2 1 
ATOM   6501  N  N   . VAL C  1 257 ? 13.379  5.790   30.249  1.00 10.53 ? 257 VAL C N   1 
ATOM   6502  C  CA  . VAL C  1 257 ? 13.915  6.825   29.363  1.00 7.25  ? 257 VAL C CA  1 
ATOM   6503  C  C   . VAL C  1 257 ? 13.200  6.550   27.992  1.00 8.08  ? 257 VAL C C   1 
ATOM   6504  O  O   . VAL C  1 257 ? 13.220  5.434   27.463  1.00 10.16 ? 257 VAL C O   1 
ATOM   6505  C  CB  . VAL C  1 257 ? 15.459  6.596   29.185  1.00 9.07  ? 257 VAL C CB  1 
ATOM   6506  C  CG1 . VAL C  1 257 ? 16.008  7.530   28.172  1.00 11.52 ? 257 VAL C CG1 1 
ATOM   6507  C  CG2 . VAL C  1 257 ? 16.205  6.906   30.545  1.00 9.33  ? 257 VAL C CG2 1 
ATOM   6508  N  N   . TYR C  1 258 ? 12.699  7.666   27.424  1.00 6.80  ? 258 TYR C N   1 
ATOM   6509  C  CA  . TYR C  1 258 ? 12.013  7.565   26.119  1.00 7.13  ? 258 TYR C CA  1 
ATOM   6510  C  C   . TYR C  1 258 ? 13.000  7.870   25.018  1.00 7.95  ? 258 TYR C C   1 
ATOM   6511  O  O   . TYR C  1 258 ? 13.803  8.803   25.139  1.00 7.85  ? 258 TYR C O   1 
ATOM   6512  C  CB  . TYR C  1 258 ? 10.778  8.460   26.126  1.00 8.38  ? 258 TYR C CB  1 
ATOM   6513  C  CG  . TYR C  1 258 ? 9.890   8.063   27.293  1.00 10.01 ? 258 TYR C CG  1 
ATOM   6514  C  CD1 . TYR C  1 258 ? 10.005  8.674   28.549  1.00 11.94 ? 258 TYR C CD1 1 
ATOM   6515  C  CD2 . TYR C  1 258 ? 9.004   6.974   27.166  1.00 10.57 ? 258 TYR C CD2 1 
ATOM   6516  C  CE1 . TYR C  1 258 ? 9.232   8.237   29.639  1.00 14.92 ? 258 TYR C CE1 1 
ATOM   6517  C  CE2 . TYR C  1 258 ? 8.231   6.530   28.238  1.00 13.26 ? 258 TYR C CE2 1 
ATOM   6518  C  CZ  . TYR C  1 258 ? 8.386   7.144   29.434  1.00 14.77 ? 258 TYR C CZ  1 
ATOM   6519  O  OH  . TYR C  1 258 ? 7.611   6.721   30.557  1.00 20.53 ? 258 TYR C OH  1 
ATOM   6520  N  N   . THR C  1 259 ? 12.929  7.112   23.930  1.00 7.16  ? 259 THR C N   1 
ATOM   6521  C  CA  . THR C  1 259 ? 13.838  7.366   22.847  1.00 6.69  ? 259 THR C CA  1 
ATOM   6522  C  C   . THR C  1 259 ? 13.045  7.750   21.534  1.00 7.16  ? 259 THR C C   1 
ATOM   6523  O  O   . THR C  1 259 ? 11.993  7.140   21.259  1.00 7.94  ? 259 THR C O   1 
ATOM   6524  C  CB  . THR C  1 259 ? 14.768  6.221   22.587  1.00 7.44  ? 259 THR C CB  1 
ATOM   6525  O  OG1 . THR C  1 259 ? 14.002  5.044   22.230  1.00 8.39  ? 259 THR C OG1 1 
ATOM   6526  C  CG2 . THR C  1 259 ? 15.642  5.828   23.844  1.00 9.30  ? 259 THR C CG2 1 
ATOM   6527  N  N   . SER C  1 260 ? 13.666  8.574   20.703  1.00 6.81  ? 260 SER C N   1 
ATOM   6528  C  CA  . SER C  1 260 ? 13.094  8.947   19.403  1.00 6.69  ? 260 SER C CA  1 
ATOM   6529  C  C   . SER C  1 260 ? 13.603  7.978   18.315  1.00 10.66 ? 260 SER C C   1 
ATOM   6530  O  O   . SER C  1 260 ? 13.119  8.104   17.129  1.00 11.33 ? 260 SER C O   1 
ATOM   6531  C  CB  . SER C  1 260 ? 13.366  10.399  19.065  1.00 7.26  ? 260 SER C CB  1 
ATOM   6532  O  OG  . SER C  1 260 ? 14.760  10.510  18.913  1.00 9.27  ? 260 SER C OG  1 
ATOM   6533  N  N   . PHE C  1 261 ? 14.493  7.073   18.650  1.00 7.78  ? 261 PHE C N   1 
ATOM   6534  C  CA  . PHE C  1 261 ? 14.996  6.031   17.731  1.00 9.14  ? 261 PHE C CA  1 
ATOM   6535  C  C   . PHE C  1 261 ? 14.655  4.672   18.330  1.00 10.46 ? 261 PHE C C   1 
ATOM   6536  O  O   . PHE C  1 261 ? 14.346  4.586   19.507  1.00 11.34 ? 261 PHE C O   1 
ATOM   6537  C  CB  . PHE C  1 261 ? 16.514  6.239   17.606  1.00 8.42  ? 261 PHE C CB  1 
ATOM   6538  C  CG  . PHE C  1 261 ? 17.259  6.157   18.916  1.00 8.47  ? 261 PHE C CG  1 
ATOM   6539  C  CD1 . PHE C  1 261 ? 17.727  4.902   19.327  1.00 10.35 ? 261 PHE C CD1 1 
ATOM   6540  C  CD2 . PHE C  1 261 ? 17.455  7.219   19.733  1.00 8.67  ? 261 PHE C CD2 1 
ATOM   6541  C  CE1 . PHE C  1 261 ? 18.440  4.797   20.612  1.00 9.63  ? 261 PHE C CE1 1 
ATOM   6542  C  CE2 . PHE C  1 261 ? 18.098  7.076   20.900  1.00 9.32  ? 261 PHE C CE2 1 
ATOM   6543  C  CZ  . PHE C  1 261 ? 18.669  5.966   21.337  1.00 10.31 ? 261 PHE C CZ  1 
ATOM   6544  N  N   A SER C  1 262 ? 14.660  3.593   17.530  0.50 12.61 ? 262 SER C N   1 
ATOM   6545  N  N   B SER C  1 262 ? 14.609  3.620   17.492  0.50 12.31 ? 262 SER C N   1 
ATOM   6546  C  CA  A SER C  1 262 ? 14.280  2.274   18.125  0.50 13.73 ? 262 SER C CA  1 
ATOM   6547  C  CA  B SER C  1 262 ? 14.377  2.275   18.068  0.50 12.91 ? 262 SER C CA  1 
ATOM   6548  C  C   A SER C  1 262 ? 15.498  1.369   18.114  0.50 15.30 ? 262 SER C C   1 
ATOM   6549  C  C   B SER C  1 262 ? 15.790  1.740   18.126  0.50 15.76 ? 262 SER C C   1 
ATOM   6550  O  O   A SER C  1 262 ? 15.847  0.805   17.090  0.50 12.94 ? 262 SER C O   1 
ATOM   6551  O  O   B SER C  1 262 ? 16.638  1.917   17.207  0.50 17.08 ? 262 SER C O   1 
ATOM   6552  C  CB  A SER C  1 262 ? 13.072  1.608   17.412  0.50 13.39 ? 262 SER C CB  1 
ATOM   6553  C  CB  B SER C  1 262 ? 13.377  1.378   17.265  0.50 12.73 ? 262 SER C CB  1 
ATOM   6554  O  OG  A SER C  1 262 ? 13.410  1.225   16.067  0.50 20.25 ? 262 SER C OG  1 
ATOM   6555  O  OG  B SER C  1 262 ? 12.842  0.259   17.964  0.50 7.93  ? 262 SER C OG  1 
ATOM   6556  N  N   . GLN C  1 263 ? 16.099  1.179   19.293  1.00 17.91 ? 263 GLN C N   1 
ATOM   6557  C  CA  . GLN C  1 263 ? 17.400  0.507   19.454  1.00 21.23 ? 263 GLN C CA  1 
ATOM   6558  C  C   . GLN C  1 263 ? 17.201  -0.979  19.104  1.00 23.28 ? 263 GLN C C   1 
ATOM   6559  O  O   . GLN C  1 263 ? 16.312  -1.610  19.689  1.00 22.19 ? 263 GLN C O   1 
ATOM   6560  C  CB  . GLN C  1 263 ? 17.841  0.597   20.929  1.00 23.46 ? 263 GLN C CB  1 
ATOM   6561  C  CG  . GLN C  1 263 ? 19.146  -0.101  21.093  1.00 23.73 ? 263 GLN C CG  1 
ATOM   6562  C  CD  . GLN C  1 263 ? 19.948  0.429   22.226  1.00 30.25 ? 263 GLN C CD  1 
ATOM   6563  O  OE1 . GLN C  1 263 ? 20.345  -0.334  23.171  1.00 30.37 ? 263 GLN C OE1 1 
ATOM   6564  N  NE2 . GLN C  1 263 ? 20.140  1.757   22.218  1.00 20.27 ? 263 GLN C NE2 1 
ATOM   6565  O  OXT . GLN C  1 263 ? 17.938  -1.529  18.230  1.00 25.00 ? 263 GLN C OXT 1 
ATOM   6566  N  N   A LYS D  1 3   ? 17.023  3.817   59.825  0.50 23.04 ? 3   LYS D N   1 
ATOM   6567  N  N   B LYS D  1 3   ? 17.758  5.064   60.519  0.50 18.40 ? 3   LYS D N   1 
ATOM   6568  C  CA  A LYS D  1 3   ? 16.052  3.980   58.685  0.50 21.28 ? 3   LYS D CA  1 
ATOM   6569  C  CA  B LYS D  1 3   ? 17.073  4.684   59.214  0.50 18.96 ? 3   LYS D CA  1 
ATOM   6570  C  C   A LYS D  1 3   ? 16.699  4.190   57.297  0.50 19.01 ? 3   LYS D C   1 
ATOM   6571  C  C   B LYS D  1 3   ? 17.844  4.879   57.914  0.50 17.29 ? 3   LYS D C   1 
ATOM   6572  O  O   A LYS D  1 3   ? 15.995  4.670   56.388  0.50 18.93 ? 3   LYS D O   1 
ATOM   6573  O  O   B LYS D  1 3   ? 18.284  5.967   57.631  0.50 18.51 ? 3   LYS D O   1 
ATOM   6574  C  CB  A LYS D  1 3   ? 14.970  5.062   58.954  0.50 22.57 ? 3   LYS D CB  1 
ATOM   6575  C  CB  B LYS D  1 3   ? 15.649  5.278   59.103  0.50 19.87 ? 3   LYS D CB  1 
ATOM   6576  C  CG  A LYS D  1 3   ? 15.440  6.365   59.644  0.50 20.88 ? 3   LYS D CG  1 
ATOM   6577  C  CG  B LYS D  1 3   ? 15.405  6.639   58.430  0.50 21.52 ? 3   LYS D CG  1 
ATOM   6578  C  CD  A LYS D  1 3   ? 14.249  7.383   59.772  0.50 23.65 ? 3   LYS D CD  1 
ATOM   6579  C  CD  B LYS D  1 3   ? 13.864  6.896   58.374  0.50 20.42 ? 3   LYS D CD  1 
ATOM   6580  C  CE  A LYS D  1 3   ? 14.654  8.859   59.546  0.50 26.78 ? 3   LYS D CE  1 
ATOM   6581  C  CE  B LYS D  1 3   ? 13.517  8.379   58.437  0.50 18.72 ? 3   LYS D CE  1 
ATOM   6582  N  NZ  A LYS D  1 3   ? 15.248  9.230   58.204  0.50 22.87 ? 3   LYS D NZ  1 
ATOM   6583  N  NZ  B LYS D  1 3   ? 12.642  8.898   57.328  0.50 17.61 ? 3   LYS D NZ  1 
ATOM   6584  N  N   . TRP D  1 4   ? 17.982  3.810   57.124  1.00 15.83 ? 4   TRP D N   1 
ATOM   6585  C  CA  . TRP D  1 4   ? 18.604  3.947   55.805  1.00 13.22 ? 4   TRP D CA  1 
ATOM   6586  C  C   . TRP D  1 4   ? 17.983  2.909   54.849  1.00 11.84 ? 4   TRP D C   1 
ATOM   6587  O  O   . TRP D  1 4   ? 17.566  1.782   55.280  1.00 11.58 ? 4   TRP D O   1 
ATOM   6588  C  CB  . TRP D  1 4   ? 20.157  3.888   55.867  1.00 12.80 ? 4   TRP D CB  1 
ATOM   6589  C  CG  . TRP D  1 4   ? 20.701  2.568   56.314  1.00 8.78  ? 4   TRP D CG  1 
ATOM   6590  C  CD1 . TRP D  1 4   ? 21.061  2.184   57.603  1.00 10.10 ? 4   TRP D CD1 1 
ATOM   6591  C  CD2 . TRP D  1 4   ? 21.087  1.460   55.438  1.00 8.90  ? 4   TRP D CD2 1 
ATOM   6592  N  NE1 . TRP D  1 4   ? 21.567  0.922   57.575  1.00 10.19 ? 4   TRP D NE1 1 
ATOM   6593  C  CE2 . TRP D  1 4   ? 21.600  0.435   56.269  1.00 7.27  ? 4   TRP D CE2 1 
ATOM   6594  C  CE3 . TRP D  1 4   ? 20.960  1.216   54.015  1.00 6.73  ? 4   TRP D CE3 1 
ATOM   6595  C  CZ2 . TRP D  1 4   ? 22.056  -0.795  55.728  1.00 6.76  ? 4   TRP D CZ2 1 
ATOM   6596  C  CZ3 . TRP D  1 4   ? 21.419  -0.030  53.506  1.00 7.70  ? 4   TRP D CZ3 1 
ATOM   6597  C  CH2 . TRP D  1 4   ? 21.989  -0.968  54.354  1.00 9.79  ? 4   TRP D CH2 1 
ATOM   6598  N  N   . THR D  1 5   ? 17.903  3.271   53.568  1.00 8.90  ? 5   THR D N   1 
ATOM   6599  C  CA  . THR D  1 5   ? 17.357  2.446   52.496  1.00 8.95  ? 5   THR D CA  1 
ATOM   6600  C  C   . THR D  1 5   ? 18.170  2.553   51.215  1.00 8.89  ? 5   THR D C   1 
ATOM   6601  O  O   . THR D  1 5   ? 19.215  3.317   51.175  1.00 9.78  ? 5   THR D O   1 
ATOM   6602  C  CB  . THR D  1 5   ? 15.870  2.865   52.183  1.00 9.93  ? 5   THR D CB  1 
ATOM   6603  O  OG1 . THR D  1 5   ? 15.976  4.117   51.460  1.00 12.73 ? 5   THR D OG1 1 
ATOM   6604  C  CG2 . THR D  1 5   ? 14.984  3.051   53.469  1.00 12.13 ? 5   THR D CG2 1 
ATOM   6605  N  N   . TYR D  1 6   ? 17.761  1.860   50.141  1.00 8.81  ? 6   TYR D N   1 
ATOM   6606  C  CA  . TYR D  1 6   ? 18.294  2.100   48.841  1.00 8.53  ? 6   TYR D CA  1 
ATOM   6607  C  C   . TYR D  1 6   ? 17.397  2.863   47.873  1.00 8.43  ? 6   TYR D C   1 
ATOM   6608  O  O   . TYR D  1 6   ? 17.693  3.042   46.690  1.00 10.12 ? 6   TYR D O   1 
ATOM   6609  C  CB  . TYR D  1 6   ? 18.650  0.779   48.172  1.00 7.04  ? 6   TYR D CB  1 
ATOM   6610  C  CG  . TYR D  1 6   ? 19.804  -0.016  48.833  1.00 5.44  ? 6   TYR D CG  1 
ATOM   6611  C  CD1 . TYR D  1 6   ? 19.594  -0.972  49.892  1.00 6.63  ? 6   TYR D CD1 1 
ATOM   6612  C  CD2 . TYR D  1 6   ? 21.117  0.145   48.393  1.00 7.23  ? 6   TYR D CD2 1 
ATOM   6613  C  CE1 . TYR D  1 6   ? 20.604  -1.747  50.409  1.00 6.19  ? 6   TYR D CE1 1 
ATOM   6614  C  CE2 . TYR D  1 6   ? 22.138  -0.579  48.922  1.00 5.84  ? 6   TYR D CE2 1 
ATOM   6615  C  CZ  . TYR D  1 6   ? 21.909  -1.575  49.885  1.00 5.22  ? 6   TYR D CZ  1 
ATOM   6616  O  OH  . TYR D  1 6   ? 22.930  -2.400  50.337  1.00 7.22  ? 6   TYR D OH  1 
ATOM   6617  N  N   . PHE D  1 7   ? 16.297  3.396   48.415  1.00 10.88 ? 7   PHE D N   1 
ATOM   6618  C  CA  . PHE D  1 7   ? 15.351  4.039   47.542  1.00 13.39 ? 7   PHE D CA  1 
ATOM   6619  C  C   . PHE D  1 7   ? 14.593  5.126   48.214  1.00 14.09 ? 7   PHE D C   1 
ATOM   6620  O  O   . PHE D  1 7   ? 14.021  4.936   49.292  1.00 16.27 ? 7   PHE D O   1 
ATOM   6621  C  CB  . PHE D  1 7   ? 14.432  2.947   46.989  1.00 15.64 ? 7   PHE D CB  1 
ATOM   6622  C  CG  . PHE D  1 7   ? 13.192  3.460   46.249  1.00 19.94 ? 7   PHE D CG  1 
ATOM   6623  C  CD1 . PHE D  1 7   ? 13.340  4.242   45.066  1.00 24.38 ? 7   PHE D CD1 1 
ATOM   6624  C  CD2 . PHE D  1 7   ? 11.891  3.194   46.752  1.00 31.89 ? 7   PHE D CD2 1 
ATOM   6625  C  CE1 . PHE D  1 7   ? 12.224  4.731   44.383  1.00 29.47 ? 7   PHE D CE1 1 
ATOM   6626  C  CE2 . PHE D  1 7   ? 10.732  3.719   46.066  1.00 31.01 ? 7   PHE D CE2 1 
ATOM   6627  C  CZ  . PHE D  1 7   ? 10.912  4.475   44.894  1.00 31.01 ? 7   PHE D CZ  1 
ATOM   6628  N  N   . GLY D  1 8   ? 14.658  6.303   47.586  1.00 14.74 ? 8   GLY D N   1 
ATOM   6629  C  CA  . GLY D  1 8   ? 13.757  7.400   48.124  1.00 15.19 ? 8   GLY D CA  1 
ATOM   6630  C  C   . GLY D  1 8   ? 14.558  8.345   49.057  1.00 18.35 ? 8   GLY D C   1 
ATOM   6631  O  O   . GLY D  1 8   ? 15.791  8.396   48.994  1.00 16.41 ? 8   GLY D O   1 
ATOM   6632  N  N   . PRO D  1 9   ? 13.871  9.074   49.969  1.00 17.38 ? 9   PRO D N   1 
ATOM   6633  C  CA  . PRO D  1 9   ? 14.488  10.098  50.821  1.00 19.06 ? 9   PRO D CA  1 
ATOM   6634  C  C   . PRO D  1 9   ? 15.635  9.679   51.745  1.00 16.50 ? 9   PRO D C   1 
ATOM   6635  O  O   . PRO D  1 9   ? 16.488  10.513  52.128  1.00 16.59 ? 9   PRO D O   1 
ATOM   6636  C  CB  . PRO D  1 9   ? 13.267  10.606  51.665  1.00 20.86 ? 9   PRO D CB  1 
ATOM   6637  C  CG  . PRO D  1 9   ? 12.196  9.637   51.515  1.00 20.74 ? 9   PRO D CG  1 
ATOM   6638  C  CD  . PRO D  1 9   ? 12.391  9.085   50.102  1.00 18.95 ? 9   PRO D CD  1 
ATOM   6639  N  N   . ASP D  1 10  ? 15.678  8.399   52.094  1.00 15.18 ? 10  ASP D N   1 
ATOM   6640  C  CA  . ASP D  1 10  ? 16.650  7.918   53.028  1.00 13.94 ? 10  ASP D CA  1 
ATOM   6641  C  C   . ASP D  1 10  ? 17.677  6.996   52.243  1.00 11.34 ? 10  ASP D C   1 
ATOM   6642  O  O   . ASP D  1 10  ? 18.426  6.209   52.866  1.00 11.71 ? 10  ASP D O   1 
ATOM   6643  C  CB  . ASP D  1 10  ? 15.969  7.100   54.158  1.00 13.08 ? 10  ASP D CB  1 
ATOM   6644  C  CG  . ASP D  1 10  ? 15.129  7.972   55.051  1.00 18.23 ? 10  ASP D CG  1 
ATOM   6645  O  OD1 . ASP D  1 10  ? 15.596  9.072   55.456  1.00 19.22 ? 10  ASP D OD1 1 
ATOM   6646  O  OD2 . ASP D  1 10  ? 13.912  7.629   55.220  1.00 22.95 ? 10  ASP D OD2 1 
ATOM   6647  N  N   . GLY D  1 11  ? 17.668  7.069   50.901  1.00 9.74  ? 11  GLY D N   1 
ATOM   6648  C  CA  . GLY D  1 11  ? 18.619  6.277   50.102  1.00 7.61  ? 11  GLY D CA  1 
ATOM   6649  C  C   . GLY D  1 11  ? 20.039  6.804   50.081  1.00 7.15  ? 11  GLY D C   1 
ATOM   6650  O  O   . GLY D  1 11  ? 20.409  7.700   50.889  1.00 5.89  ? 11  GLY D O   1 
ATOM   6651  N  N   . GLU D  1 12  ? 20.870  6.306   49.178  1.00 6.05  ? 12  GLU D N   1 
ATOM   6652  C  CA  . GLU D  1 12  ? 22.302  6.373   49.433  1.00 4.63  ? 12  GLU D CA  1 
ATOM   6653  C  C   . GLU D  1 12  ? 22.891  7.779   49.415  1.00 4.71  ? 12  GLU D C   1 
ATOM   6654  O  O   . GLU D  1 12  ? 23.953  7.960   50.029  1.00 5.05  ? 12  GLU D O   1 
ATOM   6655  C  CB  . GLU D  1 12  ? 23.024  5.413   48.409  1.00 5.34  ? 12  GLU D CB  1 
ATOM   6656  C  CG  . GLU D  1 12  ? 22.977  5.941   46.980  1.00 5.28  ? 12  GLU D CG  1 
ATOM   6657  C  CD  . GLU D  1 12  ? 23.292  4.775   45.990  1.00 4.63  ? 12  GLU D CD  1 
ATOM   6658  O  OE1 . GLU D  1 12  ? 24.494  4.553   45.757  1.00 4.95  ? 12  GLU D OE1 1 
ATOM   6659  O  OE2 . GLU D  1 12  ? 22.318  4.067   45.597  1.00 5.63  ? 12  GLU D OE2 1 
ATOM   6660  N  N   . ASN D  1 13  ? 22.307  8.734   48.643  1.00 4.91  ? 13  ASN D N   1 
ATOM   6661  C  CA  . ASN D  1 13  ? 22.893  10.085  48.698  1.00 4.92  ? 13  ASN D CA  1 
ATOM   6662  C  C   . ASN D  1 13  ? 22.688  10.693  50.049  1.00 5.58  ? 13  ASN D C   1 
ATOM   6663  O  O   . ASN D  1 13  ? 23.394  11.720  50.326  1.00 5.58  ? 13  ASN D O   1 
ATOM   6664  C  CB  . ASN D  1 13  ? 22.262  10.991  47.665  1.00 5.43  ? 13  ASN D CB  1 
ATOM   6665  C  CG  . ASN D  1 13  ? 22.685  10.620  46.227  1.00 5.41  ? 13  ASN D CG  1 
ATOM   6666  O  OD1 . ASN D  1 13  ? 23.570  9.811   46.035  1.00 5.65  ? 13  ASN D OD1 1 
ATOM   6667  N  ND2 . ASN D  1 13  ? 22.038  11.258  45.264  1.00 6.14  ? 13  ASN D ND2 1 
ATOM   6668  N  N   . SER D  1 14  ? 21.849  10.164  50.907  1.00 4.49  ? 14  SER D N   1 
ATOM   6669  C  CA  . SER D  1 14  ? 21.614  10.745  52.298  1.00 5.14  ? 14  SER D CA  1 
ATOM   6670  C  C   . SER D  1 14  ? 22.249  9.958   53.376  1.00 6.76  ? 14  SER D C   1 
ATOM   6671  O  O   . SER D  1 14  ? 22.208  10.390  54.543  1.00 6.63  ? 14  SER D O   1 
ATOM   6672  C  CB  . SER D  1 14  ? 20.087  10.798  52.543  1.00 6.60  ? 14  SER D CB  1 
ATOM   6673  O  OG  . SER D  1 14  ? 19.501  11.803  51.732  1.00 7.40  ? 14  SER D OG  1 
ATOM   6674  N  N   . TRP D  1 15  ? 22.905  8.806   53.077  1.00 5.69  ? 15  TRP D N   1 
ATOM   6675  C  CA  . TRP D  1 15  ? 23.544  7.998   54.128  1.00 5.71  ? 15  TRP D CA  1 
ATOM   6676  C  C   . TRP D  1 15  ? 24.552  8.836   54.934  1.00 6.37  ? 15  TRP D C   1 
ATOM   6677  O  O   . TRP D  1 15  ? 24.626  8.621   56.151  1.00 6.11  ? 15  TRP D O   1 
ATOM   6678  C  CB  . TRP D  1 15  ? 24.323  6.872   53.504  1.00 5.31  ? 15  TRP D CB  1 
ATOM   6679  C  CG  . TRP D  1 15  ? 23.401  5.792   52.883  1.00 4.02  ? 15  TRP D CG  1 
ATOM   6680  C  CD1 . TRP D  1 15  ? 22.041  5.691   52.947  1.00 6.25  ? 15  TRP D CD1 1 
ATOM   6681  C  CD2 . TRP D  1 15  ? 23.879  4.628   52.174  1.00 4.59  ? 15  TRP D CD2 1 
ATOM   6682  N  NE1 . TRP D  1 15  ? 21.619  4.504   52.291  1.00 6.87  ? 15  TRP D NE1 1 
ATOM   6683  C  CE2 . TRP D  1 15  ? 22.741  3.878   51.773  1.00 4.86  ? 15  TRP D CE2 1 
ATOM   6684  C  CE3 . TRP D  1 15  ? 25.159  4.197   51.756  1.00 3.86  ? 15  TRP D CE3 1 
ATOM   6685  C  CZ2 . TRP D  1 15  ? 22.838  2.650   51.061  1.00 5.24  ? 15  TRP D CZ2 1 
ATOM   6686  C  CZ3 . TRP D  1 15  ? 25.241  2.986   51.026  1.00 4.85  ? 15  TRP D CZ3 1 
ATOM   6687  C  CH2 . TRP D  1 15  ? 24.087  2.230   50.724  1.00 4.91  ? 15  TRP D CH2 1 
ATOM   6688  N  N   . SER D  1 16  ? 25.289  9.775   54.291  1.00 6.41  ? 16  SER D N   1 
ATOM   6689  C  CA  . SER D  1 16  ? 26.349  10.490  55.021  1.00 5.94  ? 16  SER D CA  1 
ATOM   6690  C  C   . SER D  1 16  ? 25.757  11.430  56.114  1.00 5.71  ? 16  SER D C   1 
ATOM   6691  O  O   . SER D  1 16  ? 26.588  11.875  56.962  1.00 7.04  ? 16  SER D O   1 
ATOM   6692  C  CB  . SER D  1 16  ? 27.130  11.342  54.022  1.00 5.50  ? 16  SER D CB  1 
ATOM   6693  O  OG  . SER D  1 16  ? 26.256  12.339  53.441  1.00 6.62  ? 16  SER D OG  1 
ATOM   6694  N  N   . LYS D  1 17  ? 24.469  11.740  56.094  1.00 5.72  ? 17  LYS D N   1 
ATOM   6695  C  CA  . LYS D  1 17  ? 23.945  12.628  57.178  1.00 6.80  ? 17  LYS D CA  1 
ATOM   6696  C  C   . LYS D  1 17  ? 24.138  11.954  58.507  1.00 8.46  ? 17  LYS D C   1 
ATOM   6697  O  O   . LYS D  1 17  ? 24.585  12.642  59.436  1.00 8.28  ? 17  LYS D O   1 
ATOM   6698  C  CB  . LYS D  1 17  ? 22.455  12.933  56.979  1.00 6.39  ? 17  LYS D CB  1 
ATOM   6699  C  CG  . LYS D  1 17  ? 22.095  13.732  55.649  1.00 7.07  ? 17  LYS D CG  1 
ATOM   6700  C  CD  . LYS D  1 17  ? 20.598  13.534  55.322  1.00 6.29  ? 17  LYS D CD  1 
ATOM   6701  C  CE  . LYS D  1 17  ? 20.337  14.303  53.996  1.00 6.87  ? 17  LYS D CE  1 
ATOM   6702  N  NZ  . LYS D  1 17  ? 18.879  14.342  53.637  1.00 6.99  ? 17  LYS D NZ  1 
ATOM   6703  N  N   . LYS D  1 18  ? 23.766  10.675  58.675  1.00 6.73  ? 18  LYS D N   1 
ATOM   6704  C  CA  . LYS D  1 18  ? 23.852  9.979   59.966  1.00 8.71  ? 18  LYS D CA  1 
ATOM   6705  C  C   . LYS D  1 18  ? 25.052  9.075   60.042  1.00 8.17  ? 18  LYS D C   1 
ATOM   6706  O  O   . LYS D  1 18  ? 25.447  8.697   61.164  1.00 9.65  ? 18  LYS D O   1 
ATOM   6707  C  CB  . LYS D  1 18  ? 22.570  9.160   60.177  1.00 11.61 ? 18  LYS D CB  1 
ATOM   6708  C  CG  . LYS D  1 18  ? 21.245  10.028  60.350  1.00 19.11 ? 18  LYS D CG  1 
ATOM   6709  C  CD  . LYS D  1 18  ? 20.068  9.074   60.908  1.00 20.81 ? 18  LYS D CD  1 
ATOM   6710  C  CE  . LYS D  1 18  ? 18.595  9.228   60.301  1.00 28.53 ? 18  LYS D CE  1 
ATOM   6711  N  NZ  . LYS D  1 18  ? 18.016  8.186   59.341  1.00 27.65 ? 18  LYS D NZ  1 
ATOM   6712  N  N   . TYR D  1 19  ? 25.726  8.756   58.902  1.00 6.74  ? 19  TYR D N   1 
ATOM   6713  C  CA  . TYR D  1 19  ? 26.841  7.799   58.854  1.00 6.60  ? 19  TYR D CA  1 
ATOM   6714  C  C   . TYR D  1 19  ? 27.977  8.500   58.074  1.00 8.57  ? 19  TYR D C   1 
ATOM   6715  O  O   . TYR D  1 19  ? 28.110  8.404   56.832  1.00 7.09  ? 19  TYR D O   1 
ATOM   6716  C  CB  . TYR D  1 19  ? 26.420  6.557   58.134  1.00 7.56  ? 19  TYR D CB  1 
ATOM   6717  C  CG  . TYR D  1 19  ? 25.326  5.847   58.866  1.00 9.00  ? 19  TYR D CG  1 
ATOM   6718  C  CD1 . TYR D  1 19  ? 23.970  6.012   58.424  1.00 7.37  ? 19  TYR D CD1 1 
ATOM   6719  C  CD2 . TYR D  1 19  ? 25.601  4.968   59.914  1.00 9.93  ? 19  TYR D CD2 1 
ATOM   6720  C  CE1 . TYR D  1 19  ? 22.965  5.323   59.030  1.00 10.34 ? 19  TYR D CE1 1 
ATOM   6721  C  CE2 . TYR D  1 19  ? 24.604  4.259   60.524  1.00 10.23 ? 19  TYR D CE2 1 
ATOM   6722  C  CZ  . TYR D  1 19  ? 23.291  4.433   60.093  1.00 10.24 ? 19  TYR D CZ  1 
ATOM   6723  O  OH  . TYR D  1 19  ? 22.196  3.716   60.708  1.00 14.67 ? 19  TYR D OH  1 
ATOM   6724  N  N   . PRO D  1 20  ? 28.733  9.429   58.691  1.00 6.55  ? 20  PRO D N   1 
ATOM   6725  C  CA  . PRO D  1 20  ? 29.648  10.318  57.931  1.00 7.10  ? 20  PRO D CA  1 
ATOM   6726  C  C   . PRO D  1 20  ? 30.670  9.595   57.044  1.00 7.10  ? 20  PRO D C   1 
ATOM   6727  O  O   . PRO D  1 20  ? 31.050  10.143  56.022  1.00 6.87  ? 20  PRO D O   1 
ATOM   6728  C  CB  . PRO D  1 20  ? 30.346  11.185  59.036  1.00 9.16  ? 20  PRO D CB  1 
ATOM   6729  C  CG  . PRO D  1 20  ? 29.237  11.210  60.173  1.00 14.11 ? 20  PRO D CG  1 
ATOM   6730  C  CD  . PRO D  1 20  ? 28.621  9.779   60.159  1.00 9.65  ? 20  PRO D CD  1 
ATOM   6731  N  N   . SER D  1 21  ? 31.056  8.358   57.437  1.00 6.46  ? 21  SER D N   1 
ATOM   6732  C  CA  . SER D  1 21  ? 32.034  7.650   56.648  1.00 5.61  ? 21  SER D CA  1 
ATOM   6733  C  C   . SER D  1 21  ? 31.501  7.384   55.226  1.00 5.19  ? 21  SER D C   1 
ATOM   6734  O  O   . SER D  1 21  ? 32.297  7.162   54.314  1.00 5.79  ? 21  SER D O   1 
ATOM   6735  C  CB  . SER D  1 21  ? 32.494  6.435   57.323  1.00 6.36  ? 21  SER D CB  1 
ATOM   6736  O  OG  . SER D  1 21  ? 33.309  6.859   58.488  1.00 8.42  ? 21  SER D OG  1 
ATOM   6737  N  N   . CYS D  1 22  ? 30.165  7.392   55.098  1.00 6.08  ? 22  CYS D N   1 
ATOM   6738  C  CA  . CYS D  1 22  ? 29.626  7.153   53.721  1.00 5.57  ? 22  CYS D CA  1 
ATOM   6739  C  C   . CYS D  1 22  ? 29.933  8.274   52.761  1.00 5.89  ? 22  CYS D C   1 
ATOM   6740  O  O   . CYS D  1 22  ? 29.822  8.095   51.536  1.00 6.66  ? 22  CYS D O   1 
ATOM   6741  C  CB  . CYS D  1 22  ? 28.074  6.939   53.782  1.00 6.09  ? 22  CYS D CB  1 
ATOM   6742  S  SG  . CYS D  1 22  ? 27.622  5.484   54.765  1.00 5.58  ? 22  CYS D SG  1 
ATOM   6743  N  N   . GLY D  1 23  ? 30.358  9.479   53.289  1.00 6.27  ? 23  GLY D N   1 
ATOM   6744  C  CA  . GLY D  1 23  ? 30.885  10.546  52.380  1.00 6.74  ? 23  GLY D CA  1 
ATOM   6745  C  C   . GLY D  1 23  ? 32.397  10.750  52.586  1.00 6.55  ? 23  GLY D C   1 
ATOM   6746  O  O   . GLY D  1 23  ? 32.930  11.811  52.217  1.00 7.60  ? 23  GLY D O   1 
ATOM   6747  N  N   . GLY D  1 24  ? 33.052  9.728   53.152  1.00 5.15  ? 24  GLY D N   1 
ATOM   6748  C  CA  . GLY D  1 24  ? 34.480  9.773   53.433  1.00 5.23  ? 24  GLY D CA  1 
ATOM   6749  C  C   . GLY D  1 24  ? 35.372  9.085   52.407  1.00 5.51  ? 24  GLY D C   1 
ATOM   6750  O  O   . GLY D  1 24  ? 34.952  8.948   51.202  1.00 6.18  ? 24  GLY D O   1 
ATOM   6751  N  N   . LEU D  1 25  ? 36.555  8.715   52.855  1.00 6.11  ? 25  LEU D N   1 
ATOM   6752  C  CA  . LEU D  1 25  ? 37.574  8.138   52.007  1.00 4.79  ? 25  LEU D CA  1 
ATOM   6753  C  C   . LEU D  1 25  ? 37.316  6.641   51.709  1.00 6.94  ? 25  LEU D C   1 
ATOM   6754  O  O   . LEU D  1 25  ? 36.560  5.927   52.424  1.00 6.02  ? 25  LEU D O   1 
ATOM   6755  C  CB  . LEU D  1 25  ? 38.915  8.177   52.794  1.00 8.71  ? 25  LEU D CB  1 
ATOM   6756  C  CG  . LEU D  1 25  ? 39.388  9.564   53.024  1.00 8.70  ? 25  LEU D CG  1 
ATOM   6757  C  CD1 . LEU D  1 25  ? 40.467  9.516   54.205  1.00 10.27 ? 25  LEU D CD1 1 
ATOM   6758  C  CD2 . LEU D  1 25  ? 40.053  10.091  51.820  1.00 11.04 ? 25  LEU D CD2 1 
ATOM   6759  N  N   . LEU D  1 26  ? 37.983  6.183   50.648  1.00 6.17  ? 26  LEU D N   1 
ATOM   6760  C  CA  . LEU D  1 26  ? 38.108  4.734   50.286  1.00 6.49  ? 26  LEU D CA  1 
ATOM   6761  C  C   . LEU D  1 26  ? 36.735  4.072   50.092  1.00 6.09  ? 26  LEU D C   1 
ATOM   6762  O  O   . LEU D  1 26  ? 36.598  2.847   50.415  1.00 6.28  ? 26  LEU D O   1 
ATOM   6763  C  CB  . LEU D  1 26  ? 38.915  3.965   51.368  1.00 7.50  ? 26  LEU D CB  1 
ATOM   6764  C  CG  . LEU D  1 26  ? 40.397  4.428   51.547  1.00 7.13  ? 26  LEU D CG  1 
ATOM   6765  C  CD1 . LEU D  1 26  ? 41.108  3.627   52.593  1.00 7.15  ? 26  LEU D CD1 1 
ATOM   6766  C  CD2 . LEU D  1 26  ? 41.184  4.282   50.236  1.00 8.06  ? 26  LEU D CD2 1 
ATOM   6767  N  N   . GLN D  1 27  ? 35.768  4.780   49.554  1.00 5.76  ? 27  GLN D N   1 
ATOM   6768  C  CA  . GLN D  1 27  ? 34.434  4.109   49.461  1.00 3.82  ? 27  GLN D CA  1 
ATOM   6769  C  C   . GLN D  1 27  ? 34.394  3.112   48.320  1.00 5.69  ? 27  GLN D C   1 
ATOM   6770  O  O   . GLN D  1 27  ? 34.981  3.280   47.237  1.00 6.68  ? 27  GLN D O   1 
ATOM   6771  C  CB  . GLN D  1 27  ? 33.383  5.181   49.210  1.00 5.05  ? 27  GLN D CB  1 
ATOM   6772  C  CG  . GLN D  1 27  ? 33.235  6.134   50.407  1.00 5.04  ? 27  GLN D CG  1 
ATOM   6773  C  CD  . GLN D  1 27  ? 32.765  5.353   51.637  1.00 4.35  ? 27  GLN D CD  1 
ATOM   6774  O  OE1 . GLN D  1 27  ? 31.541  5.044   51.730  1.00 5.51  ? 27  GLN D OE1 1 
ATOM   6775  N  NE2 . GLN D  1 27  ? 33.662  5.011   52.564  1.00 5.23  ? 27  GLN D NE2 1 
ATOM   6776  N  N   . SER D  1 28  ? 33.555  2.081   48.586  1.00 4.09  ? 28  SER D N   1 
ATOM   6777  C  CA  . SER D  1 28  ? 33.262  0.945   47.626  1.00 3.81  ? 28  SER D CA  1 
ATOM   6778  C  C   . SER D  1 28  ? 31.776  0.995   47.334  1.00 4.35  ? 28  SER D C   1 
ATOM   6779  O  O   . SER D  1 28  ? 30.984  1.535   48.131  1.00 4.57  ? 28  SER D O   1 
ATOM   6780  C  CB  . SER D  1 28  ? 33.605  -0.372  48.280  1.00 4.23  ? 28  SER D CB  1 
ATOM   6781  O  OG  . SER D  1 28  ? 35.026  -0.487  48.494  1.00 4.62  ? 28  SER D OG  1 
ATOM   6782  N  N   . PRO D  1 29  ? 31.292  0.333   46.243  1.00 3.99  ? 29  PRO D N   1 
ATOM   6783  C  CA  . PRO D  1 29  ? 32.007  -0.399  45.252  1.00 4.51  ? 29  PRO D CA  1 
ATOM   6784  C  C   . PRO D  1 29  ? 32.528  0.518   44.175  1.00 5.28  ? 29  PRO D C   1 
ATOM   6785  O  O   . PRO D  1 29  ? 32.334  1.784   44.254  1.00 5.49  ? 29  PRO D O   1 
ATOM   6786  C  CB  . PRO D  1 29  ? 30.969  -1.362  44.719  1.00 4.09  ? 29  PRO D CB  1 
ATOM   6787  C  CG  . PRO D  1 29  ? 29.711  -0.503  44.727  1.00 4.99  ? 29  PRO D CG  1 
ATOM   6788  C  CD  . PRO D  1 29  ? 29.828  0.370   45.962  1.00 3.55  ? 29  PRO D CD  1 
ATOM   6789  N  N   . ILE D  1 30  ? 33.239  -0.060  43.214  1.00 4.64  ? 30  ILE D N   1 
ATOM   6790  C  CA  . ILE D  1 30  ? 33.887  0.749   42.153  1.00 4.89  ? 30  ILE D CA  1 
ATOM   6791  C  C   . ILE D  1 30  ? 33.750  0.028   40.836  1.00 6.50  ? 30  ILE D C   1 
ATOM   6792  O  O   . ILE D  1 30  ? 33.411  -1.209  40.799  1.00 6.03  ? 30  ILE D O   1 
ATOM   6793  C  CB  . ILE D  1 30  ? 35.414  0.920   42.428  1.00 4.80  ? 30  ILE D CB  1 
ATOM   6794  C  CG1 . ILE D  1 30  ? 36.157  -0.413  42.500  1.00 6.68  ? 30  ILE D CG1 1 
ATOM   6795  C  CG2 . ILE D  1 30  ? 35.603  1.743   43.721  1.00 6.72  ? 30  ILE D CG2 1 
ATOM   6796  C  CD1 . ILE D  1 30  ? 37.706  -0.211  42.628  1.00 7.47  ? 30  ILE D CD1 1 
ATOM   6797  N  N   . ASP D  1 31  ? 34.021  0.794   39.738  1.00 5.46  ? 31  ASP D N   1 
ATOM   6798  C  CA  . ASP D  1 31  ? 34.089  0.161   38.393  1.00 5.65  ? 31  ASP D CA  1 
ATOM   6799  C  C   . ASP D  1 31  ? 35.522  -0.267  38.145  1.00 7.25  ? 31  ASP D C   1 
ATOM   6800  O  O   . ASP D  1 31  ? 36.477  0.543   38.252  1.00 7.96  ? 31  ASP D O   1 
ATOM   6801  C  CB  . ASP D  1 31  ? 33.730  1.200   37.301  1.00 6.44  ? 31  ASP D CB  1 
ATOM   6802  C  CG  . ASP D  1 31  ? 33.840  0.585   35.902  1.00 8.11  ? 31  ASP D CG  1 
ATOM   6803  O  OD1 . ASP D  1 31  ? 33.303  -0.497  35.665  1.00 8.65  ? 31  ASP D OD1 1 
ATOM   6804  O  OD2 . ASP D  1 31  ? 34.363  1.323   35.064  1.00 11.18 ? 31  ASP D OD2 1 
ATOM   6805  N  N   . LEU D  1 32  ? 35.647  -1.559  37.876  1.00 6.61  ? 32  LEU D N   1 
ATOM   6806  C  CA  . LEU D  1 32  ? 36.987  -2.167  37.631  1.00 8.93  ? 32  LEU D CA  1 
ATOM   6807  C  C   . LEU D  1 32  ? 37.239  -2.025  36.110  1.00 8.76  ? 32  LEU D C   1 
ATOM   6808  O  O   . LEU D  1 32  ? 36.605  -2.698  35.341  1.00 9.58  ? 32  LEU D O   1 
ATOM   6809  C  CB  . LEU D  1 32  ? 36.987  -3.653  38.103  1.00 7.80  ? 32  LEU D CB  1 
ATOM   6810  C  CG  . LEU D  1 32  ? 36.572  -3.860  39.557  1.00 8.37  ? 32  LEU D CG  1 
ATOM   6811  C  CD1 . LEU D  1 32  ? 36.207  -5.333  39.816  1.00 8.27  ? 32  LEU D CD1 1 
ATOM   6812  C  CD2 . LEU D  1 32  ? 37.683  -3.409  40.553  1.00 10.46 ? 32  LEU D CD2 1 
ATOM   6813  N  N   . HIS D  1 33  ? 38.147  -1.099  35.734  1.00 8.50  ? 33  HIS D N   1 
ATOM   6814  C  CA  . HIS D  1 33  ? 38.346  -0.715  34.394  1.00 8.80  ? 33  HIS D CA  1 
ATOM   6815  C  C   . HIS D  1 33  ? 39.855  -0.421  34.210  1.00 10.29 ? 33  HIS D C   1 
ATOM   6816  O  O   . HIS D  1 33  ? 40.526  -0.055  35.118  1.00 11.74 ? 33  HIS D O   1 
ATOM   6817  C  CB  . HIS D  1 33  ? 37.399  0.463   33.953  1.00 10.74 ? 33  HIS D CB  1 
ATOM   6818  C  CG  . HIS D  1 33  ? 37.673  1.773   34.618  1.00 11.18 ? 33  HIS D CG  1 
ATOM   6819  N  ND1 . HIS D  1 33  ? 37.386  2.054   35.964  1.00 12.40 ? 33  HIS D ND1 1 
ATOM   6820  C  CD2 . HIS D  1 33  ? 38.350  2.862   34.144  1.00 11.28 ? 33  HIS D CD2 1 
ATOM   6821  C  CE1 . HIS D  1 33  ? 37.857  3.282   36.245  1.00 12.84 ? 33  HIS D CE1 1 
ATOM   6822  N  NE2 . HIS D  1 33  ? 38.368  3.794   35.127  1.00 11.50 ? 33  HIS D NE2 1 
ATOM   6823  N  N   . SER D  1 34  ? 40.267  -0.494  32.935  1.00 12.45 ? 34  SER D N   1 
ATOM   6824  C  CA  . SER D  1 34  ? 41.693  -0.575  32.606  1.00 12.24 ? 34  SER D CA  1 
ATOM   6825  C  C   . SER D  1 34  ? 42.524  0.595   33.153  1.00 14.05 ? 34  SER D C   1 
ATOM   6826  O  O   . SER D  1 34  ? 43.628  0.341   33.640  1.00 15.99 ? 34  SER D O   1 
ATOM   6827  C  CB  . SER D  1 34  ? 41.814  -0.766  31.107  1.00 17.88 ? 34  SER D CB  1 
ATOM   6828  O  OG  . SER D  1 34  ? 41.441  0.501   30.563  1.00 21.50 ? 34  SER D OG  1 
ATOM   6829  N  N   . ASP D  1 35  ? 41.998  1.853   33.220  1.00 14.00 ? 35  ASP D N   1 
ATOM   6830  C  CA  . ASP D  1 35  ? 42.771  3.057   33.666  1.00 15.28 ? 35  ASP D CA  1 
ATOM   6831  C  C   . ASP D  1 35  ? 43.289  2.987   35.081  1.00 14.84 ? 35  ASP D C   1 
ATOM   6832  O  O   . ASP D  1 35  ? 44.166  3.741   35.513  1.00 15.74 ? 35  ASP D O   1 
ATOM   6833  C  CB  . ASP D  1 35  ? 41.832  4.324   33.571  1.00 13.14 ? 35  ASP D CB  1 
ATOM   6834  C  CG  . ASP D  1 35  ? 41.305  4.500   32.164  1.00 19.62 ? 35  ASP D CG  1 
ATOM   6835  O  OD1 . ASP D  1 35  ? 41.774  5.391   31.408  1.00 17.85 ? 35  ASP D OD1 1 
ATOM   6836  O  OD2 . ASP D  1 35  ? 40.399  3.693   31.755  1.00 22.06 ? 35  ASP D OD2 1 
ATOM   6837  N  N   . ILE D  1 36  ? 42.621  2.168   35.876  1.00 13.05 ? 36  ILE D N   1 
ATOM   6838  C  CA  . ILE D  1 36  ? 42.901  2.053   37.311  1.00 14.95 ? 36  ILE D CA  1 
ATOM   6839  C  C   . ILE D  1 36  ? 43.503  0.700   37.779  1.00 14.50 ? 36  ILE D C   1 
ATOM   6840  O  O   . ILE D  1 36  ? 43.679  0.554   39.004  1.00 13.63 ? 36  ILE D O   1 
ATOM   6841  C  CB  . ILE D  1 36  ? 41.741  2.429   38.184  1.00 16.22 ? 36  ILE D CB  1 
ATOM   6842  C  CG1 . ILE D  1 36  ? 40.527  1.457   38.002  1.00 16.32 ? 36  ILE D CG1 1 
ATOM   6843  C  CG2 . ILE D  1 36  ? 41.420  3.980   37.927  1.00 17.66 ? 36  ILE D CG2 1 
ATOM   6844  C  CD1 . ILE D  1 36  ? 39.441  1.640   39.241  1.00 15.64 ? 36  ILE D CD1 1 
ATOM   6845  N  N   . LEU D  1 37  ? 43.732  -0.170  36.786  1.00 12.71 ? 37  LEU D N   1 
ATOM   6846  C  CA  . LEU D  1 37  ? 44.265  -1.566  37.080  1.00 14.14 ? 37  LEU D CA  1 
ATOM   6847  C  C   . LEU D  1 37  ? 45.778  -1.578  36.974  1.00 16.31 ? 37  LEU D C   1 
ATOM   6848  O  O   . LEU D  1 37  ? 46.399  -0.937  36.103  1.00 17.16 ? 37  LEU D O   1 
ATOM   6849  C  CB  . LEU D  1 37  ? 43.690  -2.603  36.125  1.00 13.60 ? 37  LEU D CB  1 
ATOM   6850  C  CG  . LEU D  1 37  ? 42.152  -2.736  36.042  1.00 12.93 ? 37  LEU D CG  1 
ATOM   6851  C  CD1 . LEU D  1 37  ? 41.721  -3.765  34.991  1.00 20.31 ? 37  LEU D CD1 1 
ATOM   6852  C  CD2 . LEU D  1 37  ? 41.658  -3.197  37.435  1.00 13.64 ? 37  LEU D CD2 1 
ATOM   6853  N  N   . GLN D  1 38  ? 46.372  -2.401  37.798  1.00 13.09 ? 38  GLN D N   1 
ATOM   6854  C  CA  . GLN D  1 38  ? 47.877  -2.635  37.681  1.00 13.70 ? 38  GLN D CA  1 
ATOM   6855  C  C   . GLN D  1 38  ? 48.161  -4.073  38.092  1.00 9.25  ? 38  GLN D C   1 
ATOM   6856  O  O   . GLN D  1 38  ? 47.773  -4.486  39.204  1.00 9.28  ? 38  GLN D O   1 
ATOM   6857  C  CB  . GLN D  1 38  ? 48.649  -1.648  38.555  1.00 15.18 ? 38  GLN D CB  1 
ATOM   6858  C  CG  . GLN D  1 38  ? 50.207  -1.758  38.430  1.00 17.49 ? 38  GLN D CG  1 
ATOM   6859  C  CD  . GLN D  1 38  ? 50.818  -0.661  39.191  1.00 22.19 ? 38  GLN D CD  1 
ATOM   6860  O  OE1 . GLN D  1 38  ? 51.378  -0.871  40.258  1.00 26.13 ? 38  GLN D OE1 1 
ATOM   6861  N  NE2 . GLN D  1 38  ? 50.588  0.562   38.718  1.00 27.92 ? 38  GLN D NE2 1 
ATOM   6862  N  N   . TYR D  1 39  ? 48.846  -4.852  37.250  1.00 9.62  ? 39  TYR D N   1 
ATOM   6863  C  CA  . TYR D  1 39  ? 49.273  -6.228  37.652  1.00 9.71  ? 39  TYR D CA  1 
ATOM   6864  C  C   . TYR D  1 39  ? 50.286  -6.086  38.775  1.00 10.61 ? 39  TYR D C   1 
ATOM   6865  O  O   . TYR D  1 39  ? 51.185  -5.228  38.798  1.00 11.55 ? 39  TYR D O   1 
ATOM   6866  C  CB  . TYR D  1 39  ? 49.869  -6.903  36.464  1.00 11.26 ? 39  TYR D CB  1 
ATOM   6867  C  CG  . TYR D  1 39  ? 50.488  -8.230  36.796  1.00 10.36 ? 39  TYR D CG  1 
ATOM   6868  C  CD1 . TYR D  1 39  ? 49.777  -9.270  37.307  1.00 11.06 ? 39  TYR D CD1 1 
ATOM   6869  C  CD2 . TYR D  1 39  ? 51.831  -8.449  36.517  1.00 12.49 ? 39  TYR D CD2 1 
ATOM   6870  C  CE1 . TYR D  1 39  ? 50.369  -10.498 37.601  1.00 9.88  ? 39  TYR D CE1 1 
ATOM   6871  C  CE2 . TYR D  1 39  ? 52.413  -9.630  36.796  1.00 8.93  ? 39  TYR D CE2 1 
ATOM   6872  C  CZ  . TYR D  1 39  ? 51.714  -10.656 37.324  1.00 10.26 ? 39  TYR D CZ  1 
ATOM   6873  O  OH  . TYR D  1 39  ? 52.303  -11.887 37.581  1.00 12.28 ? 39  TYR D OH  1 
ATOM   6874  N  N   . ASP D  1 40  ? 50.080  -6.917  39.777  1.00 8.08  ? 40  ASP D N   1 
ATOM   6875  C  CA  . ASP D  1 40  ? 50.973  -7.076  40.948  1.00 9.14  ? 40  ASP D CA  1 
ATOM   6876  C  C   . ASP D  1 40  ? 51.394  -8.532  41.080  1.00 9.05  ? 40  ASP D C   1 
ATOM   6877  O  O   . ASP D  1 40  ? 50.604  -9.405  41.520  1.00 7.46  ? 40  ASP D O   1 
ATOM   6878  C  CB  . ASP D  1 40  ? 50.355  -6.502  42.166  1.00 8.25  ? 40  ASP D CB  1 
ATOM   6879  C  CG  . ASP D  1 40  ? 51.257  -6.586  43.408  1.00 12.05 ? 40  ASP D CG  1 
ATOM   6880  O  OD1 . ASP D  1 40  ? 50.755  -6.193  44.505  1.00 16.41 ? 40  ASP D OD1 1 
ATOM   6881  O  OD2 . ASP D  1 40  ? 52.355  -7.153  43.306  1.00 13.02 ? 40  ASP D OD2 1 
ATOM   6882  N  N   . ALA D  1 41  ? 52.649  -8.793  40.668  1.00 8.55  ? 41  ALA D N   1 
ATOM   6883  C  CA  . ALA D  1 41  ? 53.144  -10.184 40.692  1.00 8.41  ? 41  ALA D CA  1 
ATOM   6884  C  C   . ALA D  1 41  ? 53.359  -10.855 42.051  1.00 7.44  ? 41  ALA D C   1 
ATOM   6885  O  O   . ALA D  1 41  ? 53.557  -12.108 42.107  1.00 10.66 ? 41  ALA D O   1 
ATOM   6886  C  CB  . ALA D  1 41  ? 54.472  -10.250 39.840  1.00 9.75  ? 41  ALA D CB  1 
ATOM   6887  N  N   A SER D  1 42  ? 53.252  -10.061 43.099  0.60 8.96  ? 42  SER D N   1 
ATOM   6888  N  N   B SER D  1 42  ? 53.294  -10.036 43.100  0.40 7.53  ? 42  SER D N   1 
ATOM   6889  C  CA  A SER D  1 42  ? 53.443  -10.571 44.443  0.60 9.64  ? 42  SER D CA  1 
ATOM   6890  C  CA  B SER D  1 42  ? 53.439  -10.520 44.474  0.40 6.25  ? 42  SER D CA  1 
ATOM   6891  C  C   A SER D  1 42  ? 52.133  -11.143 45.026  0.60 9.91  ? 42  SER D C   1 
ATOM   6892  C  C   B SER D  1 42  ? 52.121  -10.962 45.114  0.40 7.93  ? 42  SER D C   1 
ATOM   6893  O  O   A SER D  1 42  ? 52.149  -11.897 46.012  0.60 10.18 ? 42  SER D O   1 
ATOM   6894  O  O   B SER D  1 42  ? 52.120  -11.453 46.221  0.40 8.51  ? 42  SER D O   1 
ATOM   6895  C  CB  A SER D  1 42  ? 54.001  -9.485  45.388  0.60 11.70 ? 42  SER D CB  1 
ATOM   6896  C  CB  B SER D  1 42  ? 54.126  -9.504  45.420  0.40 6.97  ? 42  SER D CB  1 
ATOM   6897  O  OG  A SER D  1 42  ? 53.168  -8.333  45.337  0.60 18.61 ? 42  SER D OG  1 
ATOM   6898  O  OG  B SER D  1 42  ? 55.382  -9.122  44.917  0.40 2.00  ? 42  SER D OG  1 
ATOM   6899  N  N   . LEU D  1 43  ? 51.007  -10.790 44.402  1.00 9.51  ? 43  LEU D N   1 
ATOM   6900  C  CA  . LEU D  1 43  ? 49.656  -11.215 44.984  1.00 12.40 ? 43  LEU D CA  1 
ATOM   6901  C  C   . LEU D  1 43  ? 49.680  -12.752 44.853  1.00 13.51 ? 43  LEU D C   1 
ATOM   6902  O  O   . LEU D  1 43  ? 50.149  -13.277 43.832  1.00 15.32 ? 43  LEU D O   1 
ATOM   6903  C  CB  . LEU D  1 43  ? 48.489  -10.681 44.135  1.00 10.24 ? 43  LEU D CB  1 
ATOM   6904  C  CG  . LEU D  1 43  ? 48.327  -9.177  44.312  1.00 9.62  ? 43  LEU D CG  1 
ATOM   6905  C  CD1 . LEU D  1 43  ? 47.291  -8.630  43.375  1.00 9.76  ? 43  LEU D CD1 1 
ATOM   6906  C  CD2 . LEU D  1 43  ? 47.829  -8.850  45.694  1.00 10.59 ? 43  LEU D CD2 1 
ATOM   6907  N  N   . THR D  1 44  ? 49.255  -13.447 45.884  1.00 13.37 ? 44  THR D N   1 
ATOM   6908  C  CA  . THR D  1 44  ? 49.304  -14.919 45.811  1.00 14.10 ? 44  THR D CA  1 
ATOM   6909  C  C   . THR D  1 44  ? 47.891  -15.504 46.046  1.00 10.62 ? 44  THR D C   1 
ATOM   6910  O  O   . THR D  1 44  ? 46.928  -14.747 46.367  1.00 11.33 ? 44  THR D O   1 
ATOM   6911  C  CB  . THR D  1 44  ? 50.121  -15.474 46.954  1.00 15.34 ? 44  THR D CB  1 
ATOM   6912  O  OG1 . THR D  1 44  ? 49.592  -14.986 48.211  1.00 17.10 ? 44  THR D OG1 1 
ATOM   6913  C  CG2 . THR D  1 44  ? 51.607  -15.117 46.854  1.00 18.19 ? 44  THR D CG2 1 
ATOM   6914  N  N   . PRO D  1 45  ? 47.680  -16.754 45.628  1.00 11.26 ? 45  PRO D N   1 
ATOM   6915  C  CA  . PRO D  1 45  ? 46.319  -17.334 45.731  1.00 11.55 ? 45  PRO D CA  1 
ATOM   6916  C  C   . PRO D  1 45  ? 45.888  -17.443 47.169  1.00 11.67 ? 45  PRO D C   1 
ATOM   6917  O  O   . PRO D  1 45  ? 46.684  -17.765 48.098  1.00 12.56 ? 45  PRO D O   1 
ATOM   6918  C  CB  . PRO D  1 45  ? 46.433  -18.691 45.024  1.00 12.43 ? 45  PRO D CB  1 
ATOM   6919  C  CG  . PRO D  1 45  ? 47.796  -18.648 44.186  1.00 16.93 ? 45  PRO D CG  1 
ATOM   6920  C  CD  . PRO D  1 45  ? 48.664  -17.707 45.006  1.00 12.25 ? 45  PRO D CD  1 
ATOM   6921  N  N   . LEU D  1 46  ? 44.638  -17.144 47.391  1.00 8.79  ? 46  LEU D N   1 
ATOM   6922  C  CA  . LEU D  1 46  ? 44.043  -17.357 48.714  1.00 10.49 ? 46  LEU D CA  1 
ATOM   6923  C  C   . LEU D  1 46  ? 43.815  -18.886 48.918  1.00 8.62  ? 46  LEU D C   1 
ATOM   6924  O  O   . LEU D  1 46  ? 43.521  -19.617 47.964  1.00 9.21  ? 46  LEU D O   1 
ATOM   6925  C  CB  . LEU D  1 46  ? 42.660  -16.673 48.895  1.00 9.04  ? 46  LEU D CB  1 
ATOM   6926  C  CG  . LEU D  1 46  ? 42.773  -15.146 48.891  1.00 11.29 ? 46  LEU D CG  1 
ATOM   6927  C  CD1 . LEU D  1 46  ? 41.452  -14.513 48.790  1.00 10.49 ? 46  LEU D CD1 1 
ATOM   6928  C  CD2 . LEU D  1 46  ? 43.522  -14.603 50.114  1.00 16.03 ? 46  LEU D CD2 1 
ATOM   6929  N  N   . GLU D  1 47  ? 43.991  -19.295 50.151  1.00 8.30  ? 47  GLU D N   1 
ATOM   6930  C  CA  . GLU D  1 47  ? 43.559  -20.616 50.552  1.00 7.91  ? 47  GLU D CA  1 
ATOM   6931  C  C   . GLU D  1 47  ? 42.358  -20.530 51.521  1.00 8.18  ? 47  GLU D C   1 
ATOM   6932  O  O   . GLU D  1 47  ? 42.370  -19.720 52.439  1.00 9.80  ? 47  GLU D O   1 
ATOM   6933  C  CB  . GLU D  1 47  ? 44.697  -21.347 51.256  1.00 11.62 ? 47  GLU D CB  1 
ATOM   6934  C  CG  . GLU D  1 47  ? 45.928  -21.524 50.305  1.00 13.61 ? 47  GLU D CG  1 
ATOM   6935  C  CD  . GLU D  1 47  ? 47.072  -22.342 50.944  1.00 17.21 ? 47  GLU D CD  1 
ATOM   6936  O  OE1 . GLU D  1 47  ? 48.210  -21.909 50.742  1.00 31.21 ? 47  GLU D OE1 1 
ATOM   6937  O  OE2 . GLU D  1 47  ? 46.755  -23.328 51.548  1.00 23.63 ? 47  GLU D OE2 1 
ATOM   6938  N  N   . PHE D  1 48  ? 41.356  -21.393 51.284  1.00 9.35  ? 48  PHE D N   1 
ATOM   6939  C  CA  . PHE D  1 48  ? 40.110  -21.315 52.020  1.00 11.24 ? 48  PHE D CA  1 
ATOM   6940  C  C   . PHE D  1 48  ? 40.120  -22.482 53.014  1.00 10.24 ? 48  PHE D C   1 
ATOM   6941  O  O   . PHE D  1 48  ? 40.187  -23.663 52.558  1.00 11.56 ? 48  PHE D O   1 
ATOM   6942  C  CB  . PHE D  1 48  ? 38.897  -21.403 51.031  1.00 11.17 ? 48  PHE D CB  1 
ATOM   6943  C  CG  . PHE D  1 48  ? 39.065  -20.446 49.885  1.00 9.93  ? 48  PHE D CG  1 
ATOM   6944  C  CD1 . PHE D  1 48  ? 39.508  -20.890 48.662  1.00 10.43 ? 48  PHE D CD1 1 
ATOM   6945  C  CD2 . PHE D  1 48  ? 38.912  -19.046 50.053  1.00 8.82  ? 48  PHE D CD2 1 
ATOM   6946  C  CE1 . PHE D  1 48  ? 39.742  -19.946 47.536  1.00 9.50  ? 48  PHE D CE1 1 
ATOM   6947  C  CE2 . PHE D  1 48  ? 39.145  -18.112 49.020  1.00 8.34  ? 48  PHE D CE2 1 
ATOM   6948  C  CZ  . PHE D  1 48  ? 39.542  -18.620 47.735  1.00 8.52  ? 48  PHE D CZ  1 
ATOM   6949  N  N   . GLN D  1 49  ? 39.991  -22.162 54.286  1.00 7.74  ? 49  GLN D N   1 
ATOM   6950  C  CA  . GLN D  1 49  ? 40.172  -23.167 55.391  1.00 10.06 ? 49  GLN D CA  1 
ATOM   6951  C  C   . GLN D  1 49  ? 38.848  -23.268 56.150  1.00 8.75  ? 49  GLN D C   1 
ATOM   6952  O  O   . GLN D  1 49  ? 38.331  -22.251 56.560  1.00 8.48  ? 49  GLN D O   1 
ATOM   6953  C  CB  . GLN D  1 49  ? 41.397  -22.834 56.308  1.00 9.63  ? 49  GLN D CB  1 
ATOM   6954  C  CG  . GLN D  1 49  ? 42.754  -22.862 55.501  1.00 10.93 ? 49  GLN D CG  1 
ATOM   6955  C  CD  . GLN D  1 49  ? 43.881  -22.093 56.165  1.00 12.22 ? 49  GLN D CD  1 
ATOM   6956  O  OE1 . GLN D  1 49  ? 43.643  -21.197 56.971  1.00 14.66 ? 49  GLN D OE1 1 
ATOM   6957  N  NE2 . GLN D  1 49  ? 45.093  -22.395 55.704  1.00 12.29 ? 49  GLN D NE2 1 
ATOM   6958  N  N   . GLY D  1 50  ? 38.381  -24.498 56.363  1.00 8.76  ? 50  GLY D N   1 
ATOM   6959  C  CA  . GLY D  1 50  ? 37.182  -24.697 57.118  1.00 8.27  ? 50  GLY D CA  1 
ATOM   6960  C  C   . GLY D  1 50  ? 35.908  -24.221 56.453  1.00 8.48  ? 50  GLY D C   1 
ATOM   6961  O  O   . GLY D  1 50  ? 34.885  -24.050 57.151  1.00 9.99  ? 50  GLY D O   1 
ATOM   6962  N  N   . TYR D  1 51  ? 35.993  -24.028 55.136  1.00 7.75  ? 51  TYR D N   1 
ATOM   6963  C  CA  . TYR D  1 51  ? 34.795  -23.638 54.409  1.00 6.35  ? 51  TYR D CA  1 
ATOM   6964  C  C   . TYR D  1 51  ? 33.798  -24.786 54.283  1.00 7.03  ? 51  TYR D C   1 
ATOM   6965  O  O   . TYR D  1 51  ? 32.612  -24.539 53.903  1.00 7.22  ? 51  TYR D O   1 
ATOM   6966  C  CB  . TYR D  1 51  ? 35.149  -23.144 52.966  1.00 6.06  ? 51  TYR D CB  1 
ATOM   6967  C  CG  . TYR D  1 51  ? 35.509  -21.647 52.901  1.00 6.55  ? 51  TYR D CG  1 
ATOM   6968  C  CD1 . TYR D  1 51  ? 36.358  -21.028 53.805  1.00 6.93  ? 51  TYR D CD1 1 
ATOM   6969  C  CD2 . TYR D  1 51  ? 35.005  -20.875 51.790  1.00 7.22  ? 51  TYR D CD2 1 
ATOM   6970  C  CE1 . TYR D  1 51  ? 36.668  -19.641 53.718  1.00 6.58  ? 51  TYR D CE1 1 
ATOM   6971  C  CE2 . TYR D  1 51  ? 35.285  -19.471 51.665  1.00 6.61  ? 51  TYR D CE2 1 
ATOM   6972  C  CZ  . TYR D  1 51  ? 36.069  -18.918 52.666  1.00 6.93  ? 51  TYR D CZ  1 
ATOM   6973  O  OH  . TYR D  1 51  ? 36.305  -17.579 52.591  1.00 7.61  ? 51  TYR D OH  1 
ATOM   6974  N  N   . ASN D  1 52  ? 34.263  -26.068 54.423  1.00 8.14  ? 52  ASN D N   1 
ATOM   6975  C  CA  . ASN D  1 52  ? 33.338  -27.196 54.336  1.00 8.43  ? 52  ASN D CA  1 
ATOM   6976  C  C   . ASN D  1 52  ? 32.623  -27.394 55.662  1.00 9.02  ? 52  ASN D C   1 
ATOM   6977  O  O   . ASN D  1 52  ? 33.061  -28.149 56.554  1.00 10.40 ? 52  ASN D O   1 
ATOM   6978  C  CB  . ASN D  1 52  ? 34.129  -28.475 53.921  1.00 8.14  ? 52  ASN D CB  1 
ATOM   6979  C  CG  . ASN D  1 52  ? 33.181  -29.648 53.736  1.00 10.85 ? 52  ASN D CG  1 
ATOM   6980  O  OD1 . ASN D  1 52  ? 32.020  -29.450 53.402  1.00 17.73 ? 52  ASN D OD1 1 
ATOM   6981  N  ND2 . ASN D  1 52  ? 33.741  -30.927 53.792  1.00 18.43 ? 52  ASN D ND2 1 
ATOM   6982  N  N   . LEU D  1 53  ? 31.577  -26.575 55.862  1.00 8.84  ? 53  LEU D N   1 
ATOM   6983  C  CA  . LEU D  1 53  ? 30.895  -26.495 57.182  1.00 7.83  ? 53  LEU D CA  1 
ATOM   6984  C  C   . LEU D  1 53  ? 30.107  -27.812 57.430  1.00 8.64  ? 53  LEU D C   1 
ATOM   6985  O  O   . LEU D  1 53  ? 29.581  -28.422 56.522  1.00 10.11 ? 53  LEU D O   1 
ATOM   6986  C  CB  . LEU D  1 53  ? 29.804  -25.397 57.115  1.00 8.40  ? 53  LEU D CB  1 
ATOM   6987  C  CG  . LEU D  1 53  ? 30.287  -24.003 56.813  1.00 8.03  ? 53  LEU D CG  1 
ATOM   6988  C  CD1 . LEU D  1 53  ? 29.109  -23.068 56.864  1.00 10.56 ? 53  LEU D CD1 1 
ATOM   6989  C  CD2 . LEU D  1 53  ? 31.287  -23.550 57.888  1.00 9.63  ? 53  LEU D CD2 1 
ATOM   6990  N  N   . SER D  1 54  ? 30.261  -28.270 58.678  1.00 8.54  ? 54  SER D N   1 
ATOM   6991  C  CA  . SER D  1 54  ? 29.677  -29.619 59.015  1.00 8.96  ? 54  SER D CA  1 
ATOM   6992  C  C   . SER D  1 54  ? 28.146  -29.555 58.735  1.00 9.54  ? 54  SER D C   1 
ATOM   6993  O  O   . SER D  1 54  ? 27.451  -28.719 59.313  1.00 10.30 ? 54  SER D O   1 
ATOM   6994  C  CB  . SER D  1 54  ? 29.919  -29.915 60.434  1.00 9.79  ? 54  SER D CB  1 
ATOM   6995  O  OG  . SER D  1 54  ? 29.200  -31.168 60.753  1.00 9.32  ? 54  SER D OG  1 
ATOM   6996  N  N   . ALA D  1 55  ? 27.655  -30.571 58.004  1.00 9.69  ? 55  ALA D N   1 
ATOM   6997  C  CA  . ALA D  1 55  ? 26.230  -30.649 57.781  1.00 10.35 ? 55  ALA D CA  1 
ATOM   6998  C  C   . ALA D  1 55  ? 25.454  -30.982 59.074  1.00 10.64 ? 55  ALA D C   1 
ATOM   6999  O  O   . ALA D  1 55  ? 24.179  -30.817 59.097  1.00 12.35 ? 55  ALA D O   1 
ATOM   7000  C  CB  . ALA D  1 55  ? 26.003  -31.783 56.737  1.00 14.38 ? 55  ALA D CB  1 
ATOM   7001  N  N   . ASN D  1 56  ? 26.144  -31.477 60.091  1.00 9.14  ? 56  ASN D N   1 
ATOM   7002  C  CA  . ASN D  1 56  ? 25.473  -31.734 61.362  1.00 11.21 ? 56  ASN D CA  1 
ATOM   7003  C  C   . ASN D  1 56  ? 25.364  -30.544 62.257  1.00 11.51 ? 56  ASN D C   1 
ATOM   7004  O  O   . ASN D  1 56  ? 24.687  -30.548 63.317  1.00 13.41 ? 56  ASN D O   1 
ATOM   7005  C  CB  . ASN D  1 56  ? 26.152  -32.923 62.125  1.00 11.29 ? 56  ASN D CB  1 
ATOM   7006  C  CG  . ASN D  1 56  ? 26.343  -34.122 61.240  1.00 15.58 ? 56  ASN D CG  1 
ATOM   7007  O  OD1 . ASN D  1 56  ? 25.422  -34.513 60.540  1.00 15.42 ? 56  ASN D OD1 1 
ATOM   7008  N  ND2 . ASN D  1 56  ? 27.540  -34.773 61.328  1.00 15.37 ? 56  ASN D ND2 1 
ATOM   7009  N  N   . LYS D  1 57  ? 25.992  -29.414 61.843  1.00 10.59 ? 57  LYS D N   1 
ATOM   7010  C  CA  . LYS D  1 57  ? 25.825  -28.169 62.533  1.00 10.13 ? 57  LYS D CA  1 
ATOM   7011  C  C   . LYS D  1 57  ? 24.809  -27.279 61.776  1.00 10.12 ? 57  LYS D C   1 
ATOM   7012  O  O   . LYS D  1 57  ? 24.448  -27.531 60.662  1.00 10.58 ? 57  LYS D O   1 
ATOM   7013  C  CB  . LYS D  1 57  ? 27.175  -27.384 62.618  1.00 11.28 ? 57  LYS D CB  1 
ATOM   7014  C  CG  . LYS D  1 57  ? 28.175  -28.031 63.621  1.00 9.85  ? 57  LYS D CG  1 
ATOM   7015  C  CD  . LYS D  1 57  ? 29.511  -27.288 63.584  1.00 12.39 ? 57  LYS D CD  1 
ATOM   7016  C  CE  . LYS D  1 57  ? 30.113  -26.950 65.030  1.00 19.53 ? 57  LYS D CE  1 
ATOM   7017  N  NZ  . LYS D  1 57  ? 31.665  -26.891 64.881  1.00 24.11 ? 57  LYS D NZ  1 
ATOM   7018  N  N   . GLN D  1 58  ? 24.381  -26.247 62.470  1.00 7.79  ? 58  GLN D N   1 
ATOM   7019  C  CA  . GLN D  1 58  ? 23.369  -25.334 61.877  1.00 9.86  ? 58  GLN D CA  1 
ATOM   7020  C  C   . GLN D  1 58  ? 23.917  -23.894 61.919  1.00 7.68  ? 58  GLN D C   1 
ATOM   7021  O  O   . GLN D  1 58  ? 24.676  -23.496 62.787  1.00 8.39  ? 58  GLN D O   1 
ATOM   7022  C  CB  . GLN D  1 58  ? 22.026  -25.371 62.757  1.00 9.08  ? 58  GLN D CB  1 
ATOM   7023  C  CG  . GLN D  1 58  ? 22.135  -24.889 64.213  1.00 12.43 ? 58  GLN D CG  1 
ATOM   7024  C  CD  . GLN D  1 58  ? 20.812  -24.850 65.061  1.00 13.38 ? 58  GLN D CD  1 
ATOM   7025  O  OE1 . GLN D  1 58  ? 20.723  -24.270 66.149  1.00 18.92 ? 58  GLN D OE1 1 
ATOM   7026  N  NE2 . GLN D  1 58  ? 19.803  -25.318 64.438  1.00 8.94  ? 58  GLN D NE2 1 
ATOM   7027  N  N   . PHE D  1 59  ? 23.405  -23.087 60.911  1.00 8.03  ? 59  PHE D N   1 
ATOM   7028  C  CA  . PHE D  1 59  ? 23.871  -21.721 60.739  1.00 7.68  ? 59  PHE D CA  1 
ATOM   7029  C  C   . PHE D  1 59  ? 22.723  -20.794 60.478  1.00 6.67  ? 59  PHE D C   1 
ATOM   7030  O  O   . PHE D  1 59  ? 21.861  -21.217 59.716  1.00 8.21  ? 59  PHE D O   1 
ATOM   7031  C  CB  . PHE D  1 59  ? 24.917  -21.700 59.581  1.00 7.68  ? 59  PHE D CB  1 
ATOM   7032  C  CG  . PHE D  1 59  ? 26.068  -22.579 59.938  1.00 5.91  ? 59  PHE D CG  1 
ATOM   7033  C  CD1 . PHE D  1 59  ? 26.075  -23.914 59.523  1.00 7.95  ? 59  PHE D CD1 1 
ATOM   7034  C  CD2 . PHE D  1 59  ? 27.116  -22.037 60.678  1.00 7.82  ? 59  PHE D CD2 1 
ATOM   7035  C  CE1 . PHE D  1 59  ? 27.150  -24.792 59.927  1.00 7.18  ? 59  PHE D CE1 1 
ATOM   7036  C  CE2 . PHE D  1 59  ? 28.148  -22.822 61.019  1.00 9.31  ? 59  PHE D CE2 1 
ATOM   7037  C  CZ  . PHE D  1 59  ? 28.168  -24.233 60.713  1.00 6.93  ? 59  PHE D CZ  1 
ATOM   7038  N  N   . LEU D  1 60  ? 22.731  -19.677 61.128  1.00 6.77  ? 60  LEU D N   1 
ATOM   7039  C  CA  . LEU D  1 60  ? 21.513  -18.869 61.124  1.00 7.71  ? 60  LEU D CA  1 
ATOM   7040  C  C   . LEU D  1 60  ? 21.403  -18.027 59.836  1.00 7.22  ? 60  LEU D C   1 
ATOM   7041  O  O   . LEU D  1 60  ? 22.288  -17.148 59.573  1.00 8.73  ? 60  LEU D O   1 
ATOM   7042  C  CB  . LEU D  1 60  ? 21.515  -17.959 62.329  1.00 8.51  ? 60  LEU D CB  1 
ATOM   7043  C  CG  . LEU D  1 60  ? 20.221  -17.220 62.649  1.00 12.33 ? 60  LEU D CG  1 
ATOM   7044  C  CD1 . LEU D  1 60  ? 19.134  -18.165 63.035  1.00 11.40 ? 60  LEU D CD1 1 
ATOM   7045  C  CD2 . LEU D  1 60  ? 20.462  -16.079 63.661  1.00 14.17 ? 60  LEU D CD2 1 
ATOM   7046  N  N   . LEU D  1 61  ? 20.321  -18.142 59.125  1.00 7.37  ? 61  LEU D N   1 
ATOM   7047  C  CA  . LEU D  1 61  ? 19.911  -17.261 58.006  1.00 7.61  ? 61  LEU D CA  1 
ATOM   7048  C  C   . LEU D  1 61  ? 18.958  -16.194 58.507  1.00 10.04 ? 61  LEU D C   1 
ATOM   7049  O  O   . LEU D  1 61  ? 18.005  -16.493 59.273  1.00 9.87  ? 61  LEU D O   1 
ATOM   7050  C  CB  . LEU D  1 61  ? 19.242  -18.119 56.943  1.00 7.65  ? 61  LEU D CB  1 
ATOM   7051  C  CG  . LEU D  1 61  ? 19.011  -17.530 55.562  1.00 8.26  ? 61  LEU D CG  1 
ATOM   7052  C  CD1 . LEU D  1 61  ? 20.377  -17.424 54.788  1.00 11.43 ? 61  LEU D CD1 1 
ATOM   7053  C  CD2 . LEU D  1 61  ? 18.062  -18.458 54.767  1.00 11.52 ? 61  LEU D CD2 1 
ATOM   7054  N  N   . THR D  1 62  ? 19.250  -14.924 58.228  1.00 9.73  ? 62  THR D N   1 
ATOM   7055  C  CA  . THR D  1 62  ? 18.443  -13.811 58.776  1.00 10.90 ? 62  THR D CA  1 
ATOM   7056  C  C   . THR D  1 62  ? 18.126  -12.791 57.632  1.00 9.93  ? 62  THR D C   1 
ATOM   7057  O  O   . THR D  1 62  ? 19.010  -12.471 56.786  1.00 10.65 ? 62  THR D O   1 
ATOM   7058  C  CB  . THR D  1 62  ? 19.303  -12.991 59.766  1.00 12.70 ? 62  THR D CB  1 
ATOM   7059  O  OG1 . THR D  1 62  ? 19.632  -13.809 60.916  1.00 15.35 ? 62  THR D OG1 1 
ATOM   7060  C  CG2 . THR D  1 62  ? 18.524  -11.796 60.392  1.00 15.63 ? 62  THR D CG2 1 
ATOM   7061  N  N   . ASN D  1 63  ? 16.911  -12.257 57.604  1.00 9.32  ? 63  ASN D N   1 
ATOM   7062  C  CA  . ASN D  1 63  ? 16.632  -11.080 56.766  1.00 9.36  ? 63  ASN D CA  1 
ATOM   7063  C  C   . ASN D  1 63  ? 16.829  -9.896  57.693  1.00 6.73  ? 63  ASN D C   1 
ATOM   7064  O  O   . ASN D  1 63  ? 16.169  -9.706  58.731  1.00 9.20  ? 63  ASN D O   1 
ATOM   7065  C  CB  . ASN D  1 63  ? 15.159  -11.186 56.304  1.00 8.10  ? 63  ASN D CB  1 
ATOM   7066  C  CG  . ASN D  1 63  ? 14.632  -9.951  55.588  1.00 6.79  ? 63  ASN D CG  1 
ATOM   7067  O  OD1 . ASN D  1 63  ? 15.215  -8.836  55.819  1.00 7.84  ? 63  ASN D OD1 1 
ATOM   7068  N  ND2 . ASN D  1 63  ? 13.584  -10.097 54.816  1.00 7.56  ? 63  ASN D ND2 1 
ATOM   7069  N  N   . ASN D  1 64  ? 17.896  -9.107  57.408  1.00 8.89  ? 64  ASN D N   1 
ATOM   7070  C  CA  . ASN D  1 64  ? 18.217  -7.951  58.313  1.00 9.25  ? 64  ASN D CA  1 
ATOM   7071  C  C   . ASN D  1 64  ? 17.605  -6.632  57.877  1.00 9.93  ? 64  ASN D C   1 
ATOM   7072  O  O   . ASN D  1 64  ? 17.988  -5.544  58.347  1.00 11.70 ? 64  ASN D O   1 
ATOM   7073  C  CB  . ASN D  1 64  ? 19.731  -7.806  58.483  1.00 9.61  ? 64  ASN D CB  1 
ATOM   7074  C  CG  . ASN D  1 64  ? 20.437  -7.450  57.193  1.00 11.26 ? 64  ASN D CG  1 
ATOM   7075  O  OD1 . ASN D  1 64  ? 19.810  -7.184  56.182  1.00 10.39 ? 64  ASN D OD1 1 
ATOM   7076  N  ND2 . ASN D  1 64  ? 21.833  -7.432  57.198  1.00 12.84 ? 64  ASN D ND2 1 
ATOM   7077  N  N   . GLY D  1 65  ? 16.638  -6.741  56.954  1.00 8.97  ? 65  GLY D N   1 
ATOM   7078  C  CA  . GLY D  1 65  ? 16.018  -5.501  56.369  1.00 8.88  ? 65  GLY D CA  1 
ATOM   7079  C  C   . GLY D  1 65  ? 16.775  -4.862  55.218  1.00 10.64 ? 65  GLY D C   1 
ATOM   7080  O  O   . GLY D  1 65  ? 16.184  -4.029  54.526  1.00 10.28 ? 65  GLY D O   1 
ATOM   7081  N  N   . HIS D  1 66  ? 17.984  -5.389  54.910  1.00 9.69  ? 66  HIS D N   1 
ATOM   7082  C  CA  . HIS D  1 66  ? 18.825  -4.835  53.801  1.00 8.75  ? 66  HIS D CA  1 
ATOM   7083  C  C   . HIS D  1 66  ? 19.340  -5.908  52.852  1.00 8.59  ? 66  HIS D C   1 
ATOM   7084  O  O   . HIS D  1 66  ? 19.576  -5.588  51.665  1.00 9.82  ? 66  HIS D O   1 
ATOM   7085  C  CB  . HIS D  1 66  ? 20.055  -4.079  54.420  1.00 9.74  ? 66  HIS D CB  1 
ATOM   7086  C  CG  . HIS D  1 66  ? 19.643  -3.089  55.473  1.00 10.97 ? 66  HIS D CG  1 
ATOM   7087  N  ND1 . HIS D  1 66  ? 18.956  -1.899  55.168  1.00 12.26 ? 66  HIS D ND1 1 
ATOM   7088  C  CD2 . HIS D  1 66  ? 19.840  -3.084  56.829  1.00 15.61 ? 66  HIS D CD2 1 
ATOM   7089  C  CE1 . HIS D  1 66  ? 18.783  -1.197  56.311  1.00 13.41 ? 66  HIS D CE1 1 
ATOM   7090  N  NE2 . HIS D  1 66  ? 19.285  -1.921  57.327  1.00 11.92 ? 66  HIS D NE2 1 
ATOM   7091  N  N   . SER D  1 67  ? 19.492  -7.173  53.398  1.00 7.13  ? 67  SER D N   1 
ATOM   7092  C  CA  . SER D  1 67  ? 19.869  -8.306  52.519  1.00 6.45  ? 67  SER D CA  1 
ATOM   7093  C  C   . SER D  1 67  ? 19.426  -9.603  53.226  1.00 7.28  ? 67  SER D C   1 
ATOM   7094  O  O   . SER D  1 67  ? 18.716  -9.485  54.248  1.00 8.34  ? 67  SER D O   1 
ATOM   7095  C  CB  . SER D  1 67  ? 21.434  -8.318  52.449  1.00 8.08  ? 67  SER D CB  1 
ATOM   7096  O  OG  . SER D  1 67  ? 21.810  -9.360  51.489  1.00 8.35  ? 67  SER D OG  1 
ATOM   7097  N  N   . VAL D  1 68  ? 19.782  -10.761 52.607  1.00 7.19  ? 68  VAL D N   1 
ATOM   7098  C  CA  . VAL D  1 68  ? 19.618  -12.016 53.348  1.00 8.29  ? 68  VAL D CA  1 
ATOM   7099  C  C   . VAL D  1 68  ? 21.080  -12.401 53.751  1.00 7.18  ? 68  VAL D C   1 
ATOM   7100  O  O   . VAL D  1 68  ? 21.934  -12.393 52.870  1.00 7.45  ? 68  VAL D O   1 
ATOM   7101  C  CB  . VAL D  1 68  ? 18.912  -13.093 52.515  1.00 9.69  ? 68  VAL D CB  1 
ATOM   7102  C  CG1 . VAL D  1 68  ? 19.531  -13.339 51.128  1.00 10.16 ? 68  VAL D CG1 1 
ATOM   7103  C  CG2 . VAL D  1 68  ? 18.836  -14.428 53.368  1.00 11.16 ? 68  VAL D CG2 1 
ATOM   7104  N  N   . LYS D  1 69  ? 21.287  -12.636 55.056  1.00 7.51  ? 69  LYS D N   1 
ATOM   7105  C  CA  . LYS D  1 69  ? 22.635  -13.002 55.558  1.00 8.47  ? 69  LYS D CA  1 
ATOM   7106  C  C   . LYS D  1 69  ? 22.637  -14.367 56.194  1.00 8.95  ? 69  LYS D C   1 
ATOM   7107  O  O   . LYS D  1 69  ? 21.659  -14.816 56.801  1.00 8.15  ? 69  LYS D O   1 
ATOM   7108  C  CB  . LYS D  1 69  ? 23.208  -11.926 56.482  1.00 11.20 ? 69  LYS D CB  1 
ATOM   7109  C  CG  . LYS D  1 69  ? 22.652  -11.788 57.776  1.00 19.55 ? 69  LYS D CG  1 
ATOM   7110  C  CD  . LYS D  1 69  ? 23.745  -11.016 58.637  1.00 15.72 ? 69  LYS D CD  1 
ATOM   7111  C  CE  . LYS D  1 69  ? 23.030  -11.076 59.984  1.00 18.01 ? 69  LYS D CE  1 
ATOM   7112  N  NZ  . LYS D  1 69  ? 23.658  -10.181 61.024  1.00 16.83 ? 69  LYS D NZ  1 
ATOM   7113  N  N   . LEU D  1 70  ? 23.757  -15.111 55.964  1.00 6.27  ? 70  LEU D N   1 
ATOM   7114  C  CA  . LEU D  1 70  ? 23.976  -16.403 56.583  1.00 6.14  ? 70  LEU D CA  1 
ATOM   7115  C  C   . LEU D  1 70  ? 25.174  -16.248 57.534  1.00 6.72  ? 70  LEU D C   1 
ATOM   7116  O  O   . LEU D  1 70  ? 26.264  -15.783 57.119  1.00 5.94  ? 70  LEU D O   1 
ATOM   7117  C  CB  . LEU D  1 70  ? 24.322  -17.427 55.575  1.00 6.38  ? 70  LEU D CB  1 
ATOM   7118  C  CG  . LEU D  1 70  ? 24.606  -18.839 56.146  1.00 7.20  ? 70  LEU D CG  1 
ATOM   7119  C  CD1 . LEU D  1 70  ? 23.375  -19.455 56.854  1.00 8.12  ? 70  LEU D CD1 1 
ATOM   7120  C  CD2 . LEU D  1 70  ? 25.175  -19.725 55.065  1.00 9.43  ? 70  LEU D CD2 1 
ATOM   7121  N  N   . ASN D  1 71  ? 24.959  -16.412 58.842  1.00 6.33  ? 71  ASN D N   1 
ATOM   7122  C  CA  . ASN D  1 71  ? 26.081  -16.305 59.801  1.00 7.21  ? 71  ASN D CA  1 
ATOM   7123  C  C   . ASN D  1 71  ? 27.042  -17.453 59.535  1.00 8.59  ? 71  ASN D C   1 
ATOM   7124  O  O   . ASN D  1 71  ? 26.658  -18.610 59.185  1.00 9.39  ? 71  ASN D O   1 
ATOM   7125  C  CB  . ASN D  1 71  ? 25.517  -16.325 61.277  1.00 8.14  ? 71  ASN D CB  1 
ATOM   7126  C  CG  . ASN D  1 71  ? 24.988  -15.003 61.686  1.00 13.82 ? 71  ASN D CG  1 
ATOM   7127  O  OD1 . ASN D  1 71  ? 25.132  -13.971 61.010  1.00 18.34 ? 71  ASN D OD1 1 
ATOM   7128  N  ND2 . ASN D  1 71  ? 24.344  -14.997 62.842  1.00 20.21 ? 71  ASN D ND2 1 
ATOM   7129  N  N   . LEU D  1 72  ? 28.345  -17.161 59.710  1.00 6.47  ? 72  LEU D N   1 
ATOM   7130  C  CA  . LEU D  1 72  ? 29.407  -18.142 59.426  1.00 6.58  ? 72  LEU D CA  1 
ATOM   7131  C  C   . LEU D  1 72  ? 30.270  -18.224 60.695  1.00 7.65  ? 72  LEU D C   1 
ATOM   7132  O  O   . LEU D  1 72  ? 30.385  -17.246 61.413  1.00 8.24  ? 72  LEU D O   1 
ATOM   7133  C  CB  . LEU D  1 72  ? 30.312  -17.646 58.279  1.00 6.62  ? 72  LEU D CB  1 
ATOM   7134  C  CG  . LEU D  1 72  ? 29.577  -17.632 56.936  1.00 5.50  ? 72  LEU D CG  1 
ATOM   7135  C  CD1 . LEU D  1 72  ? 30.424  -16.929 55.863  1.00 8.09  ? 72  LEU D CD1 1 
ATOM   7136  C  CD2 . LEU D  1 72  ? 29.103  -19.063 56.412  1.00 6.31  ? 72  LEU D CD2 1 
ATOM   7137  N  N   . PRO D  1 73  ? 30.931  -19.376 60.907  1.00 6.81  ? 73  PRO D N   1 
ATOM   7138  C  CA  . PRO D  1 73  ? 31.724  -19.581 62.128  1.00 9.37  ? 73  PRO D CA  1 
ATOM   7139  C  C   . PRO D  1 73  ? 33.135  -19.000 62.004  1.00 8.75  ? 73  PRO D C   1 
ATOM   7140  O  O   . PRO D  1 73  ? 33.714  -18.968 60.928  1.00 8.86  ? 73  PRO D O   1 
ATOM   7141  C  CB  . PRO D  1 73  ? 31.690  -21.097 62.265  1.00 9.37  ? 73  PRO D CB  1 
ATOM   7142  C  CG  . PRO D  1 73  ? 31.718  -21.627 60.813  1.00 9.59  ? 73  PRO D CG  1 
ATOM   7143  C  CD  . PRO D  1 73  ? 30.808  -20.596 60.069  1.00 7.32  ? 73  PRO D CD  1 
ATOM   7144  N  N   . SER D  1 74  ? 33.713  -18.626 63.201  1.00 10.19 ? 74  SER D N   1 
ATOM   7145  C  CA  . SER D  1 74  ? 35.058  -18.042 63.134  1.00 10.93 ? 74  SER D CA  1 
ATOM   7146  C  C   . SER D  1 74  ? 36.153  -19.100 62.898  1.00 12.09 ? 74  SER D C   1 
ATOM   7147  O  O   . SER D  1 74  ? 37.317  -18.707 62.721  1.00 12.67 ? 74  SER D O   1 
ATOM   7148  C  CB  . SER D  1 74  ? 35.333  -17.289 64.422  1.00 12.94 ? 74  SER D CB  1 
ATOM   7149  O  OG  . SER D  1 74  ? 35.232  -18.247 65.507  1.00 14.75 ? 74  SER D OG  1 
ATOM   7150  N  N   . ASP D  1 75  ? 35.794  -20.376 62.860  1.00 11.05 ? 75  ASP D N   1 
ATOM   7151  C  CA  . ASP D  1 75  ? 36.745  -21.440 62.436  1.00 13.56 ? 75  ASP D CA  1 
ATOM   7152  C  C   . ASP D  1 75  ? 36.920  -21.551 60.937  1.00 12.61 ? 75  ASP D C   1 
ATOM   7153  O  O   . ASP D  1 75  ? 37.740  -22.375 60.405  1.00 15.44 ? 75  ASP D O   1 
ATOM   7154  C  CB  . ASP D  1 75  ? 36.347  -22.804 63.069  1.00 13.55 ? 75  ASP D CB  1 
ATOM   7155  C  CG  . ASP D  1 75  ? 34.940  -23.304 62.639  1.00 14.91 ? 75  ASP D CG  1 
ATOM   7156  O  OD1 . ASP D  1 75  ? 34.258  -23.987 63.416  1.00 22.87 ? 75  ASP D OD1 1 
ATOM   7157  O  OD2 . ASP D  1 75  ? 34.531  -23.166 61.462  1.00 23.38 ? 75  ASP D OD2 1 
ATOM   7158  N  N   . MET D  1 76  ? 36.203  -20.729 60.191  1.00 8.69  ? 76  MET D N   1 
ATOM   7159  C  CA  . MET D  1 76  ? 36.390  -20.632 58.753  1.00 9.13  ? 76  MET D CA  1 
ATOM   7160  C  C   . MET D  1 76  ? 37.355  -19.488 58.514  1.00 7.23  ? 76  MET D C   1 
ATOM   7161  O  O   . MET D  1 76  ? 37.214  -18.415 59.144  1.00 8.27  ? 76  MET D O   1 
ATOM   7162  C  CB  . MET D  1 76  ? 34.981  -20.269 58.188  1.00 12.11 ? 76  MET D CB  1 
ATOM   7163  C  CG  . MET D  1 76  ? 34.903  -20.261 56.804  1.00 15.52 ? 76  MET D CG  1 
ATOM   7164  S  SD  . MET D  1 76  ? 33.027  -20.289 56.372  1.00 12.06 ? 76  MET D SD  1 
ATOM   7165  C  CE  . MET D  1 76  ? 33.318  -19.400 54.938  1.00 10.43 ? 76  MET D CE  1 
ATOM   7166  N  N   . HIS D  1 77  ? 38.443  -19.728 57.708  1.00 7.73  ? 77  HIS D N   1 
ATOM   7167  C  CA  . HIS D  1 77  ? 39.522  -18.727 57.594  1.00 9.03  ? 77  HIS D CA  1 
ATOM   7168  C  C   . HIS D  1 77  ? 39.976  -18.582 56.154  1.00 8.25  ? 77  HIS D C   1 
ATOM   7169  O  O   . HIS D  1 77  ? 39.837  -19.518 55.360  1.00 8.32  ? 77  HIS D O   1 
ATOM   7170  C  CB  . HIS D  1 77  ? 40.790  -19.263 58.395  1.00 11.35 ? 77  HIS D CB  1 
ATOM   7171  C  CG  . HIS D  1 77  ? 40.570  -19.649 59.835  1.00 12.32 ? 77  HIS D CG  1 
ATOM   7172  N  ND1 . HIS D  1 77  ? 40.222  -18.747 60.787  1.00 10.95 ? 77  HIS D ND1 1 
ATOM   7173  C  CD2 . HIS D  1 77  ? 40.643  -20.836 60.480  1.00 17.51 ? 77  HIS D CD2 1 
ATOM   7174  C  CE1 . HIS D  1 77  ? 40.096  -19.321 61.979  1.00 11.95 ? 77  HIS D CE1 1 
ATOM   7175  N  NE2 . HIS D  1 77  ? 40.302  -20.601 61.810  1.00 16.81 ? 77  HIS D NE2 1 
ATOM   7176  N  N   . ILE D  1 78  ? 40.610  -17.455 55.869  1.00 8.04  ? 78  ILE D N   1 
ATOM   7177  C  CA  . ILE D  1 78  ? 41.384  -17.348 54.651  1.00 8.09  ? 78  ILE D CA  1 
ATOM   7178  C  C   . ILE D  1 78  ? 42.842  -17.135 55.044  1.00 8.47  ? 78  ILE D C   1 
ATOM   7179  O  O   . ILE D  1 78  ? 43.160  -16.352 55.939  1.00 8.02  ? 78  ILE D O   1 
ATOM   7180  C  CB  . ILE D  1 78  ? 40.847  -16.254 53.719  1.00 10.18 ? 78  ILE D CB  1 
ATOM   7181  C  CG1 . ILE D  1 78  ? 40.774  -14.910 54.391  1.00 9.96  ? 78  ILE D CG1 1 
ATOM   7182  C  CG2 . ILE D  1 78  ? 39.458  -16.748 53.129  1.00 10.76 ? 78  ILE D CG2 1 
ATOM   7183  C  CD1 . ILE D  1 78  ? 40.068  -13.876 53.390  1.00 10.78 ? 78  ILE D CD1 1 
ATOM   7184  N  N   . GLN D  1 79  ? 43.689  -17.839 54.281  1.00 7.93  ? 79  GLN D N   1 
ATOM   7185  C  CA  . GLN D  1 79  ? 45.148  -17.623 54.292  1.00 10.72 ? 79  GLN D CA  1 
ATOM   7186  C  C   . GLN D  1 79  ? 45.647  -17.026 52.976  1.00 8.87  ? 79  GLN D C   1 
ATOM   7187  O  O   . GLN D  1 79  ? 45.052  -17.310 51.904  1.00 8.51  ? 79  GLN D O   1 
ATOM   7188  C  CB  . GLN D  1 79  ? 45.785  -19.008 54.541  1.00 10.23 ? 79  GLN D CB  1 
ATOM   7189  C  CG  . GLN D  1 79  ? 47.335  -18.875 54.631  1.00 13.67 ? 79  GLN D CG  1 
ATOM   7190  C  CD  . GLN D  1 79  ? 47.948  -20.305 54.760  1.00 13.50 ? 79  GLN D CD  1 
ATOM   7191  O  OE1 . GLN D  1 79  ? 48.688  -20.805 53.851  1.00 16.11 ? 79  GLN D OE1 1 
ATOM   7192  N  NE2 . GLN D  1 79  ? 47.693  -20.928 55.889  1.00 10.44 ? 79  GLN D NE2 1 
ATOM   7193  N  N   . GLY D  1 80  ? 46.701  -16.201 53.059  1.00 10.27 ? 80  GLY D N   1 
ATOM   7194  C  CA  . GLY D  1 80  ? 47.199  -15.565 51.878  1.00 9.52  ? 80  GLY D CA  1 
ATOM   7195  C  C   . GLY D  1 80  ? 47.201  -14.027 51.992  1.00 11.50 ? 80  GLY D C   1 
ATOM   7196  O  O   . GLY D  1 80  ? 47.626  -13.336 50.976  1.00 14.41 ? 80  GLY D O   1 
ATOM   7197  N  N   . LEU D  1 81  ? 46.610  -13.456 53.073  1.00 10.77 ? 81  LEU D N   1 
ATOM   7198  C  CA  . LEU D  1 81  ? 46.808  -12.040 53.369  1.00 11.71 ? 81  LEU D CA  1 
ATOM   7199  C  C   . LEU D  1 81  ? 47.869  -11.884 54.460  1.00 10.11 ? 81  LEU D C   1 
ATOM   7200  O  O   . LEU D  1 81  ? 48.287  -12.884 55.066  1.00 10.82 ? 81  LEU D O   1 
ATOM   7201  C  CB  . LEU D  1 81  ? 45.456  -11.419 53.767  1.00 12.19 ? 81  LEU D CB  1 
ATOM   7202  C  CG  . LEU D  1 81  ? 44.339  -11.632 52.666  1.00 10.72 ? 81  LEU D CG  1 
ATOM   7203  C  CD1 . LEU D  1 81  ? 42.959  -11.050 53.218  1.00 14.95 ? 81  LEU D CD1 1 
ATOM   7204  C  CD2 . LEU D  1 81  ? 44.730  -10.900 51.366  1.00 10.55 ? 81  LEU D CD2 1 
ATOM   7205  N  N   . GLN D  1 82  ? 48.265  -10.639 54.734  1.00 11.53 ? 82  GLN D N   1 
ATOM   7206  C  CA  . GLN D  1 82  ? 49.347  -10.544 55.711  1.00 11.77 ? 82  GLN D CA  1 
ATOM   7207  C  C   . GLN D  1 82  ? 48.947  -10.942 57.096  1.00 11.93 ? 82  GLN D C   1 
ATOM   7208  O  O   . GLN D  1 82  ? 49.805  -11.394 57.873  1.00 13.12 ? 82  GLN D O   1 
ATOM   7209  C  CB  . GLN D  1 82  ? 50.042  -9.166  55.709  1.00 13.60 ? 82  GLN D CB  1 
ATOM   7210  C  CG  . GLN D  1 82  ? 49.077  -8.060  55.852  1.00 14.25 ? 82  GLN D CG  1 
ATOM   7211  C  CD  . GLN D  1 82  ? 49.757  -6.713  55.756  1.00 15.59 ? 82  GLN D CD  1 
ATOM   7212  O  OE1 . GLN D  1 82  ? 50.485  -6.425  54.805  1.00 17.19 ? 82  GLN D OE1 1 
ATOM   7213  N  NE2 . GLN D  1 82  ? 49.494  -5.865  56.741  1.00 14.58 ? 82  GLN D NE2 1 
ATOM   7214  N  N   . SER D  1 83  ? 47.636  -10.748 57.434  1.00 9.75  ? 83  SER D N   1 
ATOM   7215  C  CA  . SER D  1 83  ? 47.100  -11.360 58.621  1.00 9.82  ? 83  SER D CA  1 
ATOM   7216  C  C   . SER D  1 83  ? 46.111  -12.486 58.281  1.00 9.19  ? 83  SER D C   1 
ATOM   7217  O  O   . SER D  1 83  ? 45.593  -12.512 57.155  1.00 8.29  ? 83  SER D O   1 
ATOM   7218  C  CB  . SER D  1 83  ? 46.246  -10.350 59.441  1.00 9.83  ? 83  SER D CB  1 
ATOM   7219  O  OG  . SER D  1 83  ? 47.066  -9.181  59.825  1.00 12.70 ? 83  SER D OG  1 
ATOM   7220  N  N   . ARG D  1 84  ? 45.817  -13.331 59.251  1.00 10.06 ? 84  ARG D N   1 
ATOM   7221  C  CA  . ARG D  1 84  ? 44.775  -14.317 59.082  1.00 8.80  ? 84  ARG D CA  1 
ATOM   7222  C  C   . ARG D  1 84  ? 43.424  -13.617 59.360  1.00 9.20  ? 84  ARG D C   1 
ATOM   7223  O  O   . ARG D  1 84  ? 43.294  -12.784 60.266  1.00 10.02 ? 84  ARG D O   1 
ATOM   7224  C  CB  . ARG D  1 84  ? 44.954  -15.486 60.053  1.00 12.25 ? 84  ARG D CB  1 
ATOM   7225  C  CG  . ARG D  1 84  ? 43.949  -16.574 59.782  1.00 14.04 ? 84  ARG D CG  1 
ATOM   7226  C  CD  . ARG D  1 84  ? 44.257  -17.912 60.327  1.00 21.26 ? 84  ARG D CD  1 
ATOM   7227  N  NE  . ARG D  1 84  ? 43.840  -17.885 61.712  1.00 21.59 ? 84  ARG D NE  1 
ATOM   7228  C  CZ  . ARG D  1 84  ? 43.727  -18.954 62.473  1.00 19.36 ? 84  ARG D CZ  1 
ATOM   7229  N  NH1 . ARG D  1 84  ? 44.015  -20.151 61.981  1.00 20.40 ? 84  ARG D NH1 1 
ATOM   7230  N  NH2 . ARG D  1 84  ? 43.323  -18.827 63.720  1.00 20.62 ? 84  ARG D NH2 1 
ATOM   7231  N  N   . TYR D  1 85  ? 42.465  -13.995 58.528  1.00 7.93  ? 85  TYR D N   1 
ATOM   7232  C  CA  . TYR D  1 85  ? 41.093  -13.478 58.657  1.00 8.13  ? 85  TYR D CA  1 
ATOM   7233  C  C   . TYR D  1 85  ? 40.135  -14.611 58.875  1.00 9.29  ? 85  TYR D C   1 
ATOM   7234  O  O   . TYR D  1 85  ? 40.344  -15.693 58.279  1.00 11.37 ? 85  TYR D O   1 
ATOM   7235  C  CB  . TYR D  1 85  ? 40.678  -12.712 57.378  1.00 9.18  ? 85  TYR D CB  1 
ATOM   7236  C  CG  . TYR D  1 85  ? 41.339  -11.297 57.277  1.00 7.13  ? 85  TYR D CG  1 
ATOM   7237  C  CD1 . TYR D  1 85  ? 42.684  -11.172 56.880  1.00 8.66  ? 85  TYR D CD1 1 
ATOM   7238  C  CD2 . TYR D  1 85  ? 40.628  -10.120 57.574  1.00 6.74  ? 85  TYR D CD2 1 
ATOM   7239  C  CE1 . TYR D  1 85  ? 43.306  -9.896  56.814  1.00 9.08  ? 85  TYR D CE1 1 
ATOM   7240  C  CE2 . TYR D  1 85  ? 41.162  -8.887  57.525  1.00 7.04  ? 85  TYR D CE2 1 
ATOM   7241  C  CZ  . TYR D  1 85  ? 42.542  -8.751  57.094  1.00 6.00  ? 85  TYR D CZ  1 
ATOM   7242  O  OH  . TYR D  1 85  ? 43.138  -7.527  56.945  1.00 9.50  ? 85  TYR D OH  1 
ATOM   7243  N  N   . SER D  1 86  ? 39.087  -14.355 59.634  1.00 7.33  ? 86  SER D N   1 
ATOM   7244  C  CA  . SER D  1 86  ? 38.129  -15.442 60.000  1.00 7.61  ? 86  SER D CA  1 
ATOM   7245  C  C   . SER D  1 86  ? 36.732  -14.954 59.569  1.00 7.29  ? 86  SER D C   1 
ATOM   7246  O  O   . SER D  1 86  ? 36.389  -13.760 59.676  1.00 6.94  ? 86  SER D O   1 
ATOM   7247  C  CB  . SER D  1 86  ? 38.165  -15.635 61.503  1.00 9.75  ? 86  SER D CB  1 
ATOM   7248  O  OG  . SER D  1 86  ? 39.458  -16.247 61.882  1.00 10.15 ? 86  SER D OG  1 
ATOM   7249  N  N   . ALA D  1 87  ? 35.888  -15.888 59.149  1.00 6.44  ? 87  ALA D N   1 
ATOM   7250  C  CA  . ALA D  1 87  ? 34.569  -15.531 58.582  1.00 6.92  ? 87  ALA D CA  1 
ATOM   7251  C  C   . ALA D  1 87  ? 33.657  -15.050 59.681  1.00 7.46  ? 87  ALA D C   1 
ATOM   7252  O  O   . ALA D  1 87  ? 33.719  -15.415 60.880  1.00 7.18  ? 87  ALA D O   1 
ATOM   7253  C  CB  . ALA D  1 87  ? 33.935  -16.745 57.957  1.00 7.87  ? 87  ALA D CB  1 
ATOM   7254  N  N   . THR D  1 88  ? 32.715  -14.184 59.260  1.00 5.84  ? 88  THR D N   1 
ATOM   7255  C  CA  . THR D  1 88  ? 31.557  -13.791 60.098  1.00 5.36  ? 88  THR D CA  1 
ATOM   7256  C  C   . THR D  1 88  ? 30.173  -13.991 59.455  1.00 5.24  ? 88  THR D C   1 
ATOM   7257  O  O   . THR D  1 88  ? 29.227  -14.373 60.166  1.00 6.72  ? 88  THR D O   1 
ATOM   7258  C  CB  . THR D  1 88  ? 31.755  -12.300 60.658  1.00 5.92  ? 88  THR D CB  1 
ATOM   7259  O  OG1 . THR D  1 88  ? 30.637  -11.942 61.439  1.00 6.99  ? 88  THR D OG1 1 
ATOM   7260  C  CG2 . THR D  1 88  ? 31.992  -11.266 59.512  1.00 8.00  ? 88  THR D CG2 1 
ATOM   7261  N  N   . GLN D  1 89  ? 30.051  -13.706 58.144  1.00 5.61  ? 89  GLN D N   1 
ATOM   7262  C  CA  . GLN D  1 89  ? 28.708  -13.942 57.485  1.00 6.17  ? 89  GLN D CA  1 
ATOM   7263  C  C   . GLN D  1 89  ? 28.887  -13.804 56.010  1.00 5.32  ? 89  GLN D C   1 
ATOM   7264  O  O   . GLN D  1 89  ? 29.911  -13.230 55.538  1.00 6.06  ? 89  GLN D O   1 
ATOM   7265  C  CB  . GLN D  1 89  ? 27.644  -12.923 57.965  1.00 7.81  ? 89  GLN D CB  1 
ATOM   7266  C  CG  . GLN D  1 89  ? 28.111  -11.412 57.870  1.00 7.64  ? 89  GLN D CG  1 
ATOM   7267  C  CD  . GLN D  1 89  ? 27.414  -10.674 56.777  1.00 6.47  ? 89  GLN D CD  1 
ATOM   7268  O  OE1 . GLN D  1 89  ? 27.272  -11.189 55.665  1.00 8.48  ? 89  GLN D OE1 1 
ATOM   7269  N  NE2 . GLN D  1 89  ? 26.914  -9.486  57.066  1.00 11.42 ? 89  GLN D NE2 1 
ATOM   7270  N  N   . LEU D  1 90  ? 27.903  -14.286 55.247  1.00 4.76  ? 90  LEU D N   1 
ATOM   7271  C  CA  . LEU D  1 90  ? 27.826  -13.963 53.826  1.00 3.95  ? 90  LEU D CA  1 
ATOM   7272  C  C   . LEU D  1 90  ? 26.412  -13.417 53.548  1.00 4.81  ? 90  LEU D C   1 
ATOM   7273  O  O   . LEU D  1 90  ? 25.441  -13.644 54.290  1.00 5.18  ? 90  LEU D O   1 
ATOM   7274  C  CB  . LEU D  1 90  ? 28.210  -15.170 52.919  1.00 7.00  ? 90  LEU D CB  1 
ATOM   7275  C  CG  . LEU D  1 90  ? 27.335  -16.472 53.082  1.00 6.42  ? 90  LEU D CG  1 
ATOM   7276  C  CD1 . LEU D  1 90  ? 25.951  -16.349 52.405  1.00 6.60  ? 90  LEU D CD1 1 
ATOM   7277  C  CD2 . LEU D  1 90  ? 28.187  -17.632 52.489  1.00 8.32  ? 90  LEU D CD2 1 
ATOM   7278  N  N   . HIS D  1 91  ? 26.318  -12.724 52.395  1.00 4.30  ? 91  HIS D N   1 
ATOM   7279  C  CA  . HIS D  1 91  ? 25.021  -12.144 51.961  1.00 4.30  ? 91  HIS D CA  1 
ATOM   7280  C  C   . HIS D  1 91  ? 25.132  -11.754 50.530  1.00 4.60  ? 91  HIS D C   1 
ATOM   7281  O  O   . HIS D  1 91  ? 26.190  -11.923 49.915  1.00 4.20  ? 91  HIS D O   1 
ATOM   7282  C  CB  . HIS D  1 91  ? 24.689  -10.904 52.850  1.00 4.92  ? 91  HIS D CB  1 
ATOM   7283  C  CG  . HIS D  1 91  ? 25.713  -9.792  52.679  1.00 2.96  ? 91  HIS D CG  1 
ATOM   7284  N  ND1 . HIS D  1 91  ? 26.842  -9.708  53.460  1.00 4.19  ? 91  HIS D ND1 1 
ATOM   7285  C  CD2 . HIS D  1 91  ? 25.820  -8.827  51.719  1.00 4.46  ? 91  HIS D CD2 1 
ATOM   7286  C  CE1 . HIS D  1 91  ? 27.626  -8.742  52.962  1.00 3.36  ? 91  HIS D CE1 1 
ATOM   7287  N  NE2 . HIS D  1 91  ? 27.020  -8.213  51.928  1.00 4.22  ? 91  HIS D NE2 1 
ATOM   7288  N  N   . LEU D  1 92  ? 24.038  -11.252 49.935  1.00 4.42  ? 92  LEU D N   1 
ATOM   7289  C  CA  . LEU D  1 92  ? 24.052  -10.958 48.498  1.00 3.80  ? 92  LEU D CA  1 
ATOM   7290  C  C   . LEU D  1 92  ? 23.415  -9.541  48.242  1.00 3.23  ? 92  LEU D C   1 
ATOM   7291  O  O   . LEU D  1 92  ? 22.792  -8.959  49.106  1.00 5.82  ? 92  LEU D O   1 
ATOM   7292  C  CB  . LEU D  1 92  ? 23.170  -11.988 47.757  1.00 6.48  ? 92  LEU D CB  1 
ATOM   7293  C  CG  . LEU D  1 92  ? 23.766  -13.431 47.811  1.00 5.34  ? 92  LEU D CG  1 
ATOM   7294  C  CD1 . LEU D  1 92  ? 23.057  -14.229 48.967  1.00 8.85  ? 92  LEU D CD1 1 
ATOM   7295  C  CD2 . LEU D  1 92  ? 23.741  -14.127 46.462  1.00 7.55  ? 92  LEU D CD2 1 
ATOM   7296  N  N   . HIS D  1 93  ? 23.672  -9.110  47.017  1.00 3.76  ? 93  HIS D N   1 
ATOM   7297  C  CA  . HIS D  1 93  ? 23.082  -7.845  46.462  1.00 3.20  ? 93  HIS D CA  1 
ATOM   7298  C  C   . HIS D  1 93  ? 22.540  -8.159  45.059  1.00 4.29  ? 93  HIS D C   1 
ATOM   7299  O  O   . HIS D  1 93  ? 23.216  -8.915  44.320  1.00 4.61  ? 93  HIS D O   1 
ATOM   7300  C  CB  . HIS D  1 93  ? 24.181  -6.758  46.341  1.00 4.80  ? 93  HIS D CB  1 
ATOM   7301  C  CG  . HIS D  1 93  ? 24.875  -6.408  47.634  1.00 4.19  ? 93  HIS D CG  1 
ATOM   7302  N  ND1 . HIS D  1 93  ? 24.424  -5.438  48.542  1.00 4.81  ? 93  HIS D ND1 1 
ATOM   7303  C  CD2 . HIS D  1 93  ? 25.913  -7.017  48.261  1.00 4.26  ? 93  HIS D CD2 1 
ATOM   7304  C  CE1 . HIS D  1 93  ? 25.238  -5.414  49.600  1.00 4.85  ? 93  HIS D CE1 1 
ATOM   7305  N  NE2 . HIS D  1 93  ? 26.137  -6.336  49.476  1.00 4.63  ? 93  HIS D NE2 1 
ATOM   7306  N  N   . TRP D  1 94  ? 21.369  -7.515  44.745  1.00 4.07  ? 94  TRP D N   1 
ATOM   7307  C  CA  . TRP D  1 94  ? 20.738  -7.801  43.444  1.00 4.30  ? 94  TRP D CA  1 
ATOM   7308  C  C   . TRP D  1 94  ? 19.889  -6.612  43.009  1.00 5.42  ? 94  TRP D C   1 
ATOM   7309  O  O   . TRP D  1 94  ? 19.773  -5.625  43.734  1.00 4.76  ? 94  TRP D O   1 
ATOM   7310  C  CB  . TRP D  1 94  ? 19.938  -9.127  43.556  1.00 5.16  ? 94  TRP D CB  1 
ATOM   7311  C  CG  . TRP D  1 94  ? 18.851  -8.976  44.624  1.00 4.73  ? 94  TRP D CG  1 
ATOM   7312  C  CD1 . TRP D  1 94  ? 17.560  -8.478  44.479  1.00 7.07  ? 94  TRP D CD1 1 
ATOM   7313  C  CD2 . TRP D  1 94  ? 18.943  -9.445  45.993  1.00 4.58  ? 94  TRP D CD2 1 
ATOM   7314  N  NE1 . TRP D  1 94  ? 16.875  -8.542  45.708  1.00 5.59  ? 94  TRP D NE1 1 
ATOM   7315  C  CE2 . TRP D  1 94  ? 17.728  -9.120  46.660  1.00 4.99  ? 94  TRP D CE2 1 
ATOM   7316  C  CE3 . TRP D  1 94  ? 19.991  -9.997  46.778  1.00 4.23  ? 94  TRP D CE3 1 
ATOM   7317  C  CZ2 . TRP D  1 94  ? 17.500  -9.461  47.950  1.00 4.80  ? 94  TRP D CZ2 1 
ATOM   7318  C  CZ3 . TRP D  1 94  ? 19.779  -10.228 48.148  1.00 4.86  ? 94  TRP D CZ3 1 
ATOM   7319  C  CH2 . TRP D  1 94  ? 18.493  -10.007 48.703  1.00 5.29  ? 94  TRP D CH2 1 
ATOM   7320  N  N   . GLY D  1 95  ? 19.343  -6.787  41.768  1.00 5.28  ? 95  GLY D N   1 
ATOM   7321  C  CA  . GLY D  1 95  ? 18.607  -5.733  41.049  1.00 5.49  ? 95  GLY D CA  1 
ATOM   7322  C  C   . GLY D  1 95  ? 17.095  -5.933  41.218  1.00 6.94  ? 95  GLY D C   1 
ATOM   7323  O  O   . GLY D  1 95  ? 16.561  -6.041  42.318  1.00 6.38  ? 95  GLY D O   1 
ATOM   7324  N  N   . ASN D  1 96  ? 16.448  -5.990  40.028  1.00 6.32  ? 96  ASN D N   1 
ATOM   7325  C  CA  . ASN D  1 96  ? 15.001  -6.192  40.102  1.00 7.54  ? 96  ASN D CA  1 
ATOM   7326  C  C   . ASN D  1 96  ? 14.565  -6.845  38.779  1.00 6.56  ? 96  ASN D C   1 
ATOM   7327  O  O   . ASN D  1 96  ? 15.345  -6.895  37.834  1.00 7.07  ? 96  ASN D O   1 
ATOM   7328  C  CB  . ASN D  1 96  ? 14.220  -4.825  40.281  1.00 8.61  ? 96  ASN D CB  1 
ATOM   7329  C  CG  . ASN D  1 96  ? 14.387  -3.858  39.062  1.00 9.94  ? 96  ASN D CG  1 
ATOM   7330  O  OD1 . ASN D  1 96  ? 13.744  -4.045  38.001  1.00 13.99 ? 96  ASN D OD1 1 
ATOM   7331  N  ND2 . ASN D  1 96  ? 15.289  -2.888  39.135  1.00 9.85  ? 96  ASN D ND2 1 
ATOM   7332  N  N   . PRO D  1 97  ? 13.296  -7.405  38.791  1.00 8.07  ? 97  PRO D N   1 
ATOM   7333  C  CA  . PRO D  1 97  ? 12.984  -8.205  37.603  1.00 8.86  ? 97  PRO D CA  1 
ATOM   7334  C  C   . PRO D  1 97  ? 13.003  -7.502  36.254  1.00 9.49  ? 97  PRO D C   1 
ATOM   7335  O  O   . PRO D  1 97  ? 13.387  -8.124  35.245  1.00 11.99 ? 97  PRO D O   1 
ATOM   7336  C  CB  . PRO D  1 97  ? 11.551  -8.675  37.939  1.00 9.35  ? 97  PRO D CB  1 
ATOM   7337  C  CG  . PRO D  1 97  ? 11.530  -8.765  39.428  1.00 9.42  ? 97  PRO D CG  1 
ATOM   7338  C  CD  . PRO D  1 97  ? 12.337  -7.566  39.888  1.00 9.91  ? 97  PRO D CD  1 
ATOM   7339  N  N   . ASN D  1 98  ? 12.721  -6.221  36.239  1.00 9.84  ? 98  ASN D N   1 
ATOM   7340  C  CA  . ASN D  1 98  ? 12.812  -5.528  34.927  1.00 12.05 ? 98  ASN D CA  1 
ATOM   7341  C  C   . ASN D  1 98  ? 14.184  -5.065  34.548  1.00 13.55 ? 98  ASN D C   1 
ATOM   7342  O  O   . ASN D  1 98  ? 14.412  -4.757  33.340  1.00 15.40 ? 98  ASN D O   1 
ATOM   7343  C  CB  . ASN D  1 98  ? 11.819  -4.460  34.837  1.00 15.86 ? 98  ASN D CB  1 
ATOM   7344  C  CG  . ASN D  1 98  ? 10.406  -5.125  34.450  1.00 22.68 ? 98  ASN D CG  1 
ATOM   7345  O  OD1 . ASN D  1 98  ? 10.280  -6.104  33.534  1.00 28.43 ? 98  ASN D OD1 1 
ATOM   7346  N  ND2 . ASN D  1 98  ? 9.398   -4.655  35.125  1.00 25.69 ? 98  ASN D ND2 1 
ATOM   7347  N  N   . ASP D  1 99  ? 15.108  -5.009  35.536  1.00 9.15  ? 99  ASP D N   1 
ATOM   7348  C  CA  . ASP D  1 99  ? 16.482  -4.590  35.240  1.00 8.68  ? 99  ASP D CA  1 
ATOM   7349  C  C   . ASP D  1 99  ? 17.370  -5.454  36.123  1.00 8.98  ? 99  ASP D C   1 
ATOM   7350  O  O   . ASP D  1 99  ? 17.870  -5.083  37.210  1.00 7.52  ? 99  ASP D O   1 
ATOM   7351  C  CB  . ASP D  1 99  ? 16.658  -3.111  35.610  1.00 9.57  ? 99  ASP D CB  1 
ATOM   7352  C  CG  . ASP D  1 99  ? 17.920  -2.469  34.904  1.00 10.21 ? 99  ASP D CG  1 
ATOM   7353  O  OD1 . ASP D  1 99  ? 18.706  -3.252  34.342  1.00 14.89 ? 99  ASP D OD1 1 
ATOM   7354  O  OD2 . ASP D  1 99  ? 18.014  -1.292  35.041  1.00 15.72 ? 99  ASP D OD2 1 
ATOM   7355  N  N   . PRO D  1 100 ? 17.600  -6.705  35.703  1.00 7.37  ? 100 PRO D N   1 
ATOM   7356  C  CA  . PRO D  1 100 ? 18.234  -7.755  36.544  1.00 7.26  ? 100 PRO D CA  1 
ATOM   7357  C  C   . PRO D  1 100 ? 19.784  -7.671  36.483  1.00 8.02  ? 100 PRO D C   1 
ATOM   7358  O  O   . PRO D  1 100 ? 20.508  -8.587  36.071  1.00 8.94  ? 100 PRO D O   1 
ATOM   7359  C  CB  . PRO D  1 100 ? 17.669  -9.044  35.919  1.00 8.31  ? 100 PRO D CB  1 
ATOM   7360  C  CG  . PRO D  1 100 ? 17.525  -8.711  34.413  1.00 8.19  ? 100 PRO D CG  1 
ATOM   7361  C  CD  . PRO D  1 100 ? 17.043  -7.303  34.424  1.00 7.59  ? 100 PRO D CD  1 
ATOM   7362  N  N   . HIS D  1 101 ? 20.239  -6.510  36.909  1.00 7.35  ? 101 HIS D N   1 
ATOM   7363  C  CA  . HIS D  1 101 ? 21.717  -6.165  36.839  1.00 9.64  ? 101 HIS D CA  1 
ATOM   7364  C  C   . HIS D  1 101 ? 22.137  -5.392  38.082  1.00 9.17  ? 101 HIS D C   1 
ATOM   7365  O  O   . HIS D  1 101 ? 22.580  -4.174  37.965  1.00 13.82 ? 101 HIS D O   1 
ATOM   7366  C  CB  . HIS D  1 101 ? 22.026  -5.304  35.595  1.00 10.23 ? 101 HIS D CB  1 
ATOM   7367  C  CG  . HIS D  1 101 ? 21.407  -5.870  34.364  1.00 12.57 ? 101 HIS D CG  1 
ATOM   7368  N  ND1 . HIS D  1 101 ? 21.939  -6.970  33.706  1.00 13.36 ? 101 HIS D ND1 1 
ATOM   7369  C  CD2 . HIS D  1 101 ? 20.287  -5.485  33.686  1.00 12.05 ? 101 HIS D CD2 1 
ATOM   7370  C  CE1 . HIS D  1 101 ? 21.140  -7.269  32.677  1.00 16.58 ? 101 HIS D CE1 1 
ATOM   7371  N  NE2 . HIS D  1 101 ? 20.143  -6.385  32.652  1.00 14.98 ? 101 HIS D NE2 1 
ATOM   7372  N  N   . GLY D  1 102 ? 22.209  -6.118  39.185  1.00 6.19  ? 102 GLY D N   1 
ATOM   7373  C  CA  . GLY D  1 102 ? 22.336  -5.483  40.504  1.00 6.18  ? 102 GLY D CA  1 
ATOM   7374  C  C   . GLY D  1 102 ? 23.637  -5.930  41.275  1.00 5.95  ? 102 GLY D C   1 
ATOM   7375  O  O   . GLY D  1 102 ? 23.609  -5.820  42.484  1.00 6.43  ? 102 GLY D O   1 
ATOM   7376  N  N   . SER D  1 103 ? 24.697  -6.295  40.559  1.00 5.38  ? 103 SER D N   1 
ATOM   7377  C  CA  . SER D  1 103 ? 25.974  -6.431  41.325  1.00 4.96  ? 103 SER D CA  1 
ATOM   7378  C  C   . SER D  1 103 ? 26.376  -5.023  41.807  1.00 4.91  ? 103 SER D C   1 
ATOM   7379  O  O   . SER D  1 103 ? 25.893  -3.984  41.365  1.00 6.60  ? 103 SER D O   1 
ATOM   7380  C  CB  . SER D  1 103 ? 27.054  -6.917  40.384  1.00 5.36  ? 103 SER D CB  1 
ATOM   7381  O  OG  . SER D  1 103 ? 27.396  -6.019  39.315  1.00 4.78  ? 103 SER D OG  1 
ATOM   7382  N  N   . GLU D  1 104 ? 27.283  -5.056  42.813  1.00 3.77  ? 104 GLU D N   1 
ATOM   7383  C  CA  . GLU D  1 104 ? 27.852  -3.832  43.329  1.00 4.52  ? 104 GLU D CA  1 
ATOM   7384  C  C   . GLU D  1 104 ? 29.034  -3.370  42.510  1.00 3.76  ? 104 GLU D C   1 
ATOM   7385  O  O   . GLU D  1 104 ? 29.046  -2.247  41.966  1.00 4.98  ? 104 GLU D O   1 
ATOM   7386  C  CB  . GLU D  1 104 ? 28.261  -4.049  44.799  1.00 4.44  ? 104 GLU D CB  1 
ATOM   7387  C  CG  . GLU D  1 104 ? 27.050  -4.464  45.633  1.00 4.33  ? 104 GLU D CG  1 
ATOM   7388  C  CD  . GLU D  1 104 ? 27.043  -3.707  46.962  1.00 5.37  ? 104 GLU D CD  1 
ATOM   7389  O  OE1 . GLU D  1 104 ? 27.819  -4.084  47.874  1.00 5.02  ? 104 GLU D OE1 1 
ATOM   7390  O  OE2 . GLU D  1 104 ? 26.338  -2.675  47.097  1.00 5.59  ? 104 GLU D OE2 1 
ATOM   7391  N  N   . HIS D  1 105 ? 30.054  -4.213  42.427  1.00 4.15  ? 105 HIS D N   1 
ATOM   7392  C  CA  . HIS D  1 105 ? 31.129  -3.891  41.459  1.00 4.56  ? 105 HIS D CA  1 
ATOM   7393  C  C   . HIS D  1 105 ? 30.704  -4.078  40.025  1.00 4.60  ? 105 HIS D C   1 
ATOM   7394  O  O   . HIS D  1 105 ? 29.851  -4.955  39.715  1.00 6.08  ? 105 HIS D O   1 
ATOM   7395  C  CB  . HIS D  1 105 ? 32.358  -4.822  41.761  1.00 5.01  ? 105 HIS D CB  1 
ATOM   7396  C  CG  . HIS D  1 105 ? 32.985  -4.508  43.105  1.00 4.34  ? 105 HIS D CG  1 
ATOM   7397  N  ND1 . HIS D  1 105 ? 32.529  -5.056  44.311  1.00 4.10  ? 105 HIS D ND1 1 
ATOM   7398  C  CD2 . HIS D  1 105 ? 33.949  -3.596  43.448  1.00 5.65  ? 105 HIS D CD2 1 
ATOM   7399  C  CE1 . HIS D  1 105 ? 33.239  -4.555  45.322  1.00 5.68  ? 105 HIS D CE1 1 
ATOM   7400  N  NE2 . HIS D  1 105 ? 34.056  -3.611  44.840  1.00 4.98  ? 105 HIS D NE2 1 
ATOM   7401  N  N   . THR D  1 106 ? 31.326  -3.261  39.177  1.00 4.36  ? 106 THR D N   1 
ATOM   7402  C  CA  . THR D  1 106 ? 31.125  -3.351  37.685  1.00 5.50  ? 106 THR D CA  1 
ATOM   7403  C  C   . THR D  1 106 ? 32.486  -3.635  37.049  1.00 6.15  ? 106 THR D C   1 
ATOM   7404  O  O   . THR D  1 106 ? 33.523  -3.372  37.655  1.00 6.43  ? 106 THR D O   1 
ATOM   7405  C  CB  . THR D  1 106 ? 30.481  -2.144  37.075  1.00 6.84  ? 106 THR D CB  1 
ATOM   7406  O  OG1 . THR D  1 106 ? 31.282  -0.989  37.354  1.00 7.66  ? 106 THR D OG1 1 
ATOM   7407  C  CG2 . THR D  1 106 ? 29.094  -1.974  37.676  1.00 6.38  ? 106 THR D CG2 1 
ATOM   7408  N  N   . VAL D  1 107 ? 32.504  -4.321  35.881  1.00 7.21  ? 107 VAL D N   1 
ATOM   7409  C  CA  . VAL D  1 107 ? 33.754  -4.534  35.184  1.00 7.48  ? 107 VAL D CA  1 
ATOM   7410  C  C   . VAL D  1 107 ? 33.617  -3.903  33.789  1.00 8.48  ? 107 VAL D C   1 
ATOM   7411  O  O   . VAL D  1 107 ? 32.689  -4.160  33.016  1.00 9.64  ? 107 VAL D O   1 
ATOM   7412  C  CB  . VAL D  1 107 ? 34.030  -6.065  35.022  1.00 6.90  ? 107 VAL D CB  1 
ATOM   7413  C  CG1 . VAL D  1 107 ? 35.350  -6.231  34.230  1.00 9.86  ? 107 VAL D CG1 1 
ATOM   7414  C  CG2 . VAL D  1 107 ? 34.114  -6.775  36.348  1.00 9.06  ? 107 VAL D CG2 1 
ATOM   7415  N  N   . SER D  1 108 ? 34.535  -2.939  33.552  1.00 8.33  ? 108 SER D N   1 
ATOM   7416  C  CA  . SER D  1 108 ? 34.478  -2.082  32.308  1.00 8.77  ? 108 SER D CA  1 
ATOM   7417  C  C   . SER D  1 108 ? 33.039  -1.546  32.051  1.00 9.50  ? 108 SER D C   1 
ATOM   7418  O  O   . SER D  1 108 ? 32.412  -1.603  30.932  1.00 10.39 ? 108 SER D O   1 
ATOM   7419  C  CB  . SER D  1 108 ? 34.898  -2.911  31.090  1.00 9.70  ? 108 SER D CB  1 
ATOM   7420  O  OG  . SER D  1 108 ? 36.265  -3.358  31.303  1.00 15.07 ? 108 SER D OG  1 
ATOM   7421  N  N   . GLY D  1 109 ? 32.424  -1.092  33.148  1.00 8.76  ? 109 GLY D N   1 
ATOM   7422  C  CA  . GLY D  1 109 ? 31.151  -0.378  33.108  1.00 8.33  ? 109 GLY D CA  1 
ATOM   7423  C  C   . GLY D  1 109 ? 29.940  -1.319  33.219  1.00 10.37 ? 109 GLY D C   1 
ATOM   7424  O  O   . GLY D  1 109 ? 28.806  -0.797  33.331  1.00 11.29 ? 109 GLY D O   1 
ATOM   7425  N  N   . GLN D  1 110 ? 30.172  -2.632  33.176  1.00 9.72  ? 110 GLN D N   1 
ATOM   7426  C  CA  . GLN D  1 110 ? 29.030  -3.551  33.159  1.00 10.12 ? 110 GLN D CA  1 
ATOM   7427  C  C   . GLN D  1 110 ? 28.695  -4.132  34.534  1.00 8.57  ? 110 GLN D C   1 
ATOM   7428  O  O   . GLN D  1 110 ? 29.583  -4.656  35.215  1.00 7.76  ? 110 GLN D O   1 
ATOM   7429  C  CB  . GLN D  1 110 ? 29.344  -4.714  32.275  1.00 11.97 ? 110 GLN D CB  1 
ATOM   7430  C  CG  . GLN D  1 110 ? 29.851  -4.251  30.889  1.00 13.27 ? 110 GLN D CG  1 
ATOM   7431  C  CD  . GLN D  1 110 ? 28.984  -3.106  30.224  1.00 19.06 ? 110 GLN D CD  1 
ATOM   7432  O  OE1 . GLN D  1 110 ? 27.793  -3.310  29.954  1.00 16.35 ? 110 GLN D OE1 1 
ATOM   7433  N  NE2 . GLN D  1 110 ? 29.616  -1.911  29.948  1.00 17.60 ? 110 GLN D NE2 1 
ATOM   7434  N  N   . HIS D  1 111 ? 27.393  -4.090  34.886  1.00 8.40  ? 111 HIS D N   1 
ATOM   7435  C  CA  . HIS D  1 111 ? 26.921  -4.779  36.011  1.00 8.03  ? 111 HIS D CA  1 
ATOM   7436  C  C   . HIS D  1 111 ? 26.823  -6.229  35.697  1.00 9.72  ? 111 HIS D C   1 
ATOM   7437  O  O   . HIS D  1 111 ? 26.638  -6.668  34.501  1.00 13.76 ? 111 HIS D O   1 
ATOM   7438  C  CB  . HIS D  1 111 ? 25.543  -4.332  36.471  1.00 11.00 ? 111 HIS D CB  1 
ATOM   7439  C  CG  . HIS D  1 111 ? 25.560  -3.065  37.214  1.00 8.13  ? 111 HIS D CG  1 
ATOM   7440  N  ND1 . HIS D  1 111 ? 25.644  -3.043  38.606  1.00 10.19 ? 111 HIS D ND1 1 
ATOM   7441  C  CD2 . HIS D  1 111 ? 25.662  -1.773  36.790  1.00 12.71 ? 111 HIS D CD2 1 
ATOM   7442  C  CE1 . HIS D  1 111 ? 25.743  -1.765  38.997  1.00 8.80  ? 111 HIS D CE1 1 
ATOM   7443  N  NE2 . HIS D  1 111 ? 25.679  -0.978  37.918  1.00 17.81 ? 111 HIS D NE2 1 
ATOM   7444  N  N   . PHE D  1 112 ? 26.956  -7.050  36.654  1.00 7.02  ? 112 PHE D N   1 
ATOM   7445  C  CA  . PHE D  1 112 ? 26.513  -8.423  36.659  1.00 6.72  ? 112 PHE D CA  1 
ATOM   7446  C  C   . PHE D  1 112 ? 25.145  -8.546  37.315  1.00 6.30  ? 112 PHE D C   1 
ATOM   7447  O  O   . PHE D  1 112 ? 24.591  -7.540  37.855  1.00 6.58  ? 112 PHE D O   1 
ATOM   7448  C  CB  . PHE D  1 112 ? 27.571  -9.361  37.335  1.00 6.95  ? 112 PHE D CB  1 
ATOM   7449  C  CG  . PHE D  1 112 ? 28.829  -9.551  36.480  1.00 7.69  ? 112 PHE D CG  1 
ATOM   7450  C  CD1 . PHE D  1 112 ? 29.735  -8.537  36.318  1.00 9.84  ? 112 PHE D CD1 1 
ATOM   7451  C  CD2 . PHE D  1 112 ? 28.984  -10.758 35.765  1.00 10.19 ? 112 PHE D CD2 1 
ATOM   7452  C  CE1 . PHE D  1 112 ? 30.835  -8.730  35.455  1.00 12.35 ? 112 PHE D CE1 1 
ATOM   7453  C  CE2 . PHE D  1 112 ? 30.119  -10.969 34.914  1.00 12.03 ? 112 PHE D CE2 1 
ATOM   7454  C  CZ  . PHE D  1 112 ? 30.984  -9.914  34.777  1.00 12.90 ? 112 PHE D CZ  1 
ATOM   7455  N  N   . ALA D  1 113 ? 24.505  -9.733  37.203  1.00 5.15  ? 113 ALA D N   1 
ATOM   7456  C  CA  . ALA D  1 113 ? 23.166  -9.838  37.711  1.00 6.02  ? 113 ALA D CA  1 
ATOM   7457  C  C   . ALA D  1 113 ? 23.066  -9.640  39.194  1.00 7.08  ? 113 ALA D C   1 
ATOM   7458  O  O   . ALA D  1 113 ? 22.129  -9.029  39.703  1.00 6.53  ? 113 ALA D O   1 
ATOM   7459  C  CB  . ALA D  1 113 ? 22.579  -11.264 37.366  1.00 8.00  ? 113 ALA D CB  1 
ATOM   7460  N  N   . ALA D  1 114 ? 24.073  -10.164 39.908  1.00 5.31  ? 114 ALA D N   1 
ATOM   7461  C  CA  . ALA D  1 114 ? 24.031  -10.037 41.422  1.00 4.65  ? 114 ALA D CA  1 
ATOM   7462  C  C   . ALA D  1 114 ? 25.468  -10.232 41.926  1.00 4.68  ? 114 ALA D C   1 
ATOM   7463  O  O   . ALA D  1 114 ? 26.392  -10.454 41.118  1.00 5.00  ? 114 ALA D O   1 
ATOM   7464  C  CB  . ALA D  1 114 ? 23.045  -11.154 41.978  1.00 5.39  ? 114 ALA D CB  1 
ATOM   7465  N  N   . GLU D  1 115 ? 25.650  -10.142 43.254  1.00 4.66  ? 115 GLU D N   1 
ATOM   7466  C  CA  . GLU D  1 115 ? 26.993  -10.320 43.843  1.00 4.59  ? 115 GLU D CA  1 
ATOM   7467  C  C   . GLU D  1 115 ? 26.846  -10.944 45.222  1.00 4.37  ? 115 GLU D C   1 
ATOM   7468  O  O   . GLU D  1 115 ? 25.982  -10.556 45.986  1.00 5.30  ? 115 GLU D O   1 
ATOM   7469  C  CB  . GLU D  1 115 ? 27.613  -8.913  43.910  1.00 4.40  ? 115 GLU D CB  1 
ATOM   7470  C  CG  . GLU D  1 115 ? 29.155  -8.932  44.295  1.00 4.50  ? 115 GLU D CG  1 
ATOM   7471  C  CD  . GLU D  1 115 ? 29.798  -7.529  44.041  1.00 3.91  ? 115 GLU D CD  1 
ATOM   7472  O  OE1 . GLU D  1 115 ? 30.720  -7.153  44.773  1.00 5.19  ? 115 GLU D OE1 1 
ATOM   7473  O  OE2 . GLU D  1 115 ? 29.404  -6.901  43.026  1.00 4.70  ? 115 GLU D OE2 1 
ATOM   7474  N  N   . LEU D  1 116 ? 27.726  -11.909 45.472  1.00 4.19  ? 116 LEU D N   1 
ATOM   7475  C  CA  . LEU D  1 116 ? 27.850  -12.526 46.788  1.00 4.26  ? 116 LEU D CA  1 
ATOM   7476  C  C   . LEU D  1 116 ? 29.045  -11.893 47.552  1.00 4.32  ? 116 LEU D C   1 
ATOM   7477  O  O   . LEU D  1 116 ? 30.140  -11.792 46.953  1.00 4.10  ? 116 LEU D O   1 
ATOM   7478  C  CB  . LEU D  1 116 ? 28.099  -14.081 46.615  1.00 4.20  ? 116 LEU D CB  1 
ATOM   7479  C  CG  . LEU D  1 116 ? 28.487  -14.811 47.903  1.00 4.75  ? 116 LEU D CG  1 
ATOM   7480  C  CD1 . LEU D  1 116 ? 27.256  -15.008 48.774  1.00 6.77  ? 116 LEU D CD1 1 
ATOM   7481  C  CD2 . LEU D  1 116 ? 29.148  -16.206 47.535  1.00 6.56  ? 116 LEU D CD2 1 
ATOM   7482  N  N   . HIS D  1 117 ? 28.856  -11.609 48.835  1.00 4.16  ? 117 HIS D N   1 
ATOM   7483  C  CA  . HIS D  1 117 ? 30.004  -11.135 49.662  1.00 3.58  ? 117 HIS D CA  1 
ATOM   7484  C  C   . HIS D  1 117 ? 30.177  -12.123 50.851  1.00 5.10  ? 117 HIS D C   1 
ATOM   7485  O  O   . HIS D  1 117 ? 29.205  -12.438 51.582  1.00 4.64  ? 117 HIS D O   1 
ATOM   7486  C  CB  . HIS D  1 117 ? 29.668  -9.767  50.261  1.00 3.48  ? 117 HIS D CB  1 
ATOM   7487  C  CG  . HIS D  1 117 ? 29.736  -8.695  49.237  1.00 3.53  ? 117 HIS D CG  1 
ATOM   7488  N  ND1 . HIS D  1 117 ? 29.080  -7.470  49.324  1.00 4.71  ? 117 HIS D ND1 1 
ATOM   7489  C  CD2 . HIS D  1 117 ? 30.319  -8.705  47.994  1.00 4.13  ? 117 HIS D CD2 1 
ATOM   7490  C  CE1 . HIS D  1 117 ? 29.358  -6.726  48.259  1.00 5.89  ? 117 HIS D CE1 1 
ATOM   7491  N  NE2 . HIS D  1 117 ? 30.054  -7.469  47.370  1.00 3.81  ? 117 HIS D NE2 1 
ATOM   7492  N  N   . ILE D  1 118 ? 31.429  -12.618 50.986  1.00 4.32  ? 118 ILE D N   1 
ATOM   7493  C  CA  . ILE D  1 118 ? 31.808  -13.488 52.127  1.00 4.52  ? 118 ILE D CA  1 
ATOM   7494  C  C   . ILE D  1 118 ? 32.723  -12.612 53.023  1.00 4.78  ? 118 ILE D C   1 
ATOM   7495  O  O   . ILE D  1 118 ? 33.837  -12.244 52.623  1.00 3.87  ? 118 ILE D O   1 
ATOM   7496  C  CB  . ILE D  1 118 ? 32.499  -14.768 51.678  1.00 4.82  ? 118 ILE D CB  1 
ATOM   7497  C  CG1 . ILE D  1 118 ? 31.647  -15.476 50.591  1.00 5.31  ? 118 ILE D CG1 1 
ATOM   7498  C  CG2 . ILE D  1 118 ? 32.619  -15.703 52.897  1.00 6.87  ? 118 ILE D CG2 1 
ATOM   7499  C  CD1 . ILE D  1 118 ? 32.318  -16.841 50.053  1.00 6.76  ? 118 ILE D CD1 1 
ATOM   7500  N  N   . VAL D  1 119 ? 32.151  -12.241 54.181  1.00 5.13  ? 119 VAL D N   1 
ATOM   7501  C  CA  . VAL D  1 119 ? 32.758  -11.196 55.055  1.00 4.89  ? 119 VAL D CA  1 
ATOM   7502  C  C   . VAL D  1 119 ? 33.634  -11.894 56.104  1.00 5.74  ? 119 VAL D C   1 
ATOM   7503  O  O   . VAL D  1 119 ? 33.173  -12.840 56.793  1.00 5.50  ? 119 VAL D O   1 
ATOM   7504  C  CB  . VAL D  1 119 ? 31.645  -10.429 55.736  1.00 6.56  ? 119 VAL D CB  1 
ATOM   7505  C  CG1 . VAL D  1 119 ? 32.237  -9.240  56.480  1.00 6.99  ? 119 VAL D CG1 1 
ATOM   7506  C  CG2 . VAL D  1 119 ? 30.688  -9.892  54.648  1.00 6.74  ? 119 VAL D CG2 1 
ATOM   7507  N  N   . HIS D  1 120 ? 34.856  -11.387 56.278  1.00 4.78  ? 120 HIS D N   1 
ATOM   7508  C  CA  . HIS D  1 120 ? 35.810  -11.900 57.283  1.00 5.70  ? 120 HIS D CA  1 
ATOM   7509  C  C   . HIS D  1 120 ? 36.326  -10.689 58.079  1.00 5.75  ? 120 HIS D C   1 
ATOM   7510  O  O   . HIS D  1 120 ? 36.370  -9.551  57.620  1.00 6.82  ? 120 HIS D O   1 
ATOM   7511  C  CB  . HIS D  1 120 ? 36.995  -12.609 56.621  1.00 5.68  ? 120 HIS D CB  1 
ATOM   7512  C  CG  . HIS D  1 120 ? 36.603  -13.714 55.683  1.00 5.40  ? 120 HIS D CG  1 
ATOM   7513  N  ND1 . HIS D  1 120 ? 36.021  -13.536 54.420  1.00 6.60  ? 120 HIS D ND1 1 
ATOM   7514  C  CD2 . HIS D  1 120 ? 36.849  -15.045 55.781  1.00 4.97  ? 120 HIS D CD2 1 
ATOM   7515  C  CE1 . HIS D  1 120 ? 35.859  -14.731 53.841  1.00 7.26  ? 120 HIS D CE1 1 
ATOM   7516  N  NE2 . HIS D  1 120 ? 36.398  -15.671 54.614  1.00 6.61  ? 120 HIS D NE2 1 
ATOM   7517  N  N   . TYR D  1 121 ? 36.853  -11.009 59.266  1.00 5.49  ? 121 TYR D N   1 
ATOM   7518  C  CA  . TYR D  1 121 ? 37.489  -9.946  60.121  1.00 5.76  ? 121 TYR D CA  1 
ATOM   7519  C  C   . TYR D  1 121 ? 38.904  -10.456 60.475  1.00 6.13  ? 121 TYR D C   1 
ATOM   7520  O  O   . TYR D  1 121 ? 39.209  -11.664 60.466  1.00 5.82  ? 121 TYR D O   1 
ATOM   7521  C  CB  . TYR D  1 121 ? 36.703  -9.697  61.384  1.00 7.11  ? 121 TYR D CB  1 
ATOM   7522  C  CG  . TYR D  1 121 ? 36.618  -10.861 62.388  1.00 7.12  ? 121 TYR D CG  1 
ATOM   7523  C  CD1 . TYR D  1 121 ? 37.524  -10.925 63.463  1.00 7.56  ? 121 TYR D CD1 1 
ATOM   7524  C  CD2 . TYR D  1 121 ? 35.711  -11.954 62.207  1.00 10.01 ? 121 TYR D CD2 1 
ATOM   7525  C  CE1 . TYR D  1 121 ? 37.495  -12.048 64.334  1.00 8.47  ? 121 TYR D CE1 1 
ATOM   7526  C  CE2 . TYR D  1 121 ? 35.613  -13.020 63.099  1.00 8.36  ? 121 TYR D CE2 1 
ATOM   7527  C  CZ  . TYR D  1 121 ? 36.514  -12.994 64.203  1.00 9.52  ? 121 TYR D CZ  1 
ATOM   7528  O  OH  . TYR D  1 121 ? 36.434  -14.149 65.017  1.00 11.61 ? 121 TYR D OH  1 
ATOM   7529  N  N   . ASN D  1 122 ? 39.761  -9.506  60.833  1.00 6.04  ? 122 ASN D N   1 
ATOM   7530  C  CA  . ASN D  1 122 ? 41.164  -9.774  61.172  1.00 5.48  ? 122 ASN D CA  1 
ATOM   7531  C  C   . ASN D  1 122 ? 41.279  -10.379 62.614  1.00 8.35  ? 122 ASN D C   1 
ATOM   7532  O  O   . ASN D  1 122 ? 41.221  -9.593  63.565  1.00 7.64  ? 122 ASN D O   1 
ATOM   7533  C  CB  . ASN D  1 122 ? 41.982  -8.440  61.003  1.00 7.13  ? 122 ASN D CB  1 
ATOM   7534  C  CG  . ASN D  1 122 ? 43.446  -8.689  61.120  1.00 8.36  ? 122 ASN D CG  1 
ATOM   7535  O  OD1 . ASN D  1 122 ? 43.897  -9.602  61.809  1.00 8.96  ? 122 ASN D OD1 1 
ATOM   7536  N  ND2 . ASN D  1 122 ? 44.249  -7.878  60.386  1.00 8.83  ? 122 ASN D ND2 1 
ATOM   7537  N  N   . SER D  1 123 ? 41.390  -11.738 62.629  1.00 7.67  ? 123 SER D N   1 
ATOM   7538  C  CA  . SER D  1 123 ? 41.356  -12.459 63.902  1.00 9.53  ? 123 SER D CA  1 
ATOM   7539  C  C   . SER D  1 123 ? 42.735  -12.489 64.501  1.00 9.94  ? 123 SER D C   1 
ATOM   7540  O  O   . SER D  1 123 ? 42.844  -12.877 65.661  1.00 10.72 ? 123 SER D O   1 
ATOM   7541  C  CB  . SER D  1 123 ? 40.770  -13.818 63.640  1.00 9.48  ? 123 SER D CB  1 
ATOM   7542  O  OG  . SER D  1 123 ? 41.333  -14.518 62.571  1.00 10.18 ? 123 SER D OG  1 
ATOM   7543  N  N   . ASP D  1 124 ? 43.753  -11.995 63.805  1.00 9.84  ? 124 ASP D N   1 
ATOM   7544  C  CA  . ASP D  1 124 ? 45.090  -11.889 64.478  1.00 9.25  ? 124 ASP D CA  1 
ATOM   7545  C  C   . ASP D  1 124 ? 45.070  -10.598 65.280  1.00 10.90 ? 124 ASP D C   1 
ATOM   7546  O  O   . ASP D  1 124 ? 45.774  -10.572 66.324  1.00 14.40 ? 124 ASP D O   1 
ATOM   7547  C  CB  . ASP D  1 124 ? 46.176  -11.740 63.409  1.00 12.10 ? 124 ASP D CB  1 
ATOM   7548  C  CG  . ASP D  1 124 ? 46.567  -13.091 62.764  1.00 10.03 ? 124 ASP D CG  1 
ATOM   7549  O  OD1 . ASP D  1 124 ? 46.091  -14.166 63.240  1.00 13.85 ? 124 ASP D OD1 1 
ATOM   7550  O  OD2 . ASP D  1 124 ? 47.330  -12.994 61.743  1.00 11.75 ? 124 ASP D OD2 1 
ATOM   7551  N  N   . LEU D  1 125 ? 44.351  -9.568  64.850  1.00 11.36 ? 125 LEU D N   1 
ATOM   7552  C  CA  . LEU D  1 125 ? 44.366  -8.266  65.560  1.00 10.06 ? 125 LEU D CA  1 
ATOM   7553  C  C   . LEU D  1 125 ? 43.196  -8.102  66.495  1.00 12.32 ? 125 LEU D C   1 
ATOM   7554  O  O   . LEU D  1 125 ? 43.298  -7.310  67.481  1.00 13.39 ? 125 LEU D O   1 
ATOM   7555  C  CB  . LEU D  1 125 ? 44.450  -7.094  64.568  1.00 12.69 ? 125 LEU D CB  1 
ATOM   7556  C  CG  . LEU D  1 125 ? 45.759  -6.914  63.734  1.00 15.84 ? 125 LEU D CG  1 
ATOM   7557  C  CD1 . LEU D  1 125 ? 45.771  -5.615  62.849  1.00 16.90 ? 125 LEU D CD1 1 
ATOM   7558  C  CD2 . LEU D  1 125 ? 46.996  -7.014  64.607  1.00 21.53 ? 125 LEU D CD2 1 
ATOM   7559  N  N   . TYR D  1 126 ? 42.013  -8.674  66.168  1.00 10.01 ? 126 TYR D N   1 
ATOM   7560  C  CA  . TYR D  1 126 ? 40.775  -8.313  66.846  1.00 9.43  ? 126 TYR D CA  1 
ATOM   7561  C  C   . TYR D  1 126 ? 40.015  -9.570  67.263  1.00 9.09  ? 126 TYR D C   1 
ATOM   7562  O  O   . TYR D  1 126 ? 40.088  -10.581 66.630  1.00 9.06  ? 126 TYR D O   1 
ATOM   7563  C  CB  . TYR D  1 126 ? 39.891  -7.446  65.873  1.00 9.71  ? 126 TYR D CB  1 
ATOM   7564  C  CG  . TYR D  1 126 ? 40.646  -6.183  65.391  1.00 9.67  ? 126 TYR D CG  1 
ATOM   7565  C  CD1 . TYR D  1 126 ? 40.990  -6.043  64.032  1.00 8.93  ? 126 TYR D CD1 1 
ATOM   7566  C  CD2 . TYR D  1 126 ? 41.052  -5.186  66.313  1.00 10.29 ? 126 TYR D CD2 1 
ATOM   7567  C  CE1 . TYR D  1 126 ? 41.708  -4.968  63.552  1.00 8.94  ? 126 TYR D CE1 1 
ATOM   7568  C  CE2 . TYR D  1 126 ? 41.795  -4.088  65.919  1.00 9.08  ? 126 TYR D CE2 1 
ATOM   7569  C  CZ  . TYR D  1 126 ? 42.172  -4.006  64.521  1.00 11.36 ? 126 TYR D CZ  1 
ATOM   7570  O  OH  . TYR D  1 126 ? 42.908  -2.926  64.028  1.00 11.04 ? 126 TYR D OH  1 
ATOM   7571  N  N   . PRO D  1 127 ? 39.253  -9.476  68.336  1.00 11.66 ? 127 PRO D N   1 
ATOM   7572  C  CA  . PRO D  1 127 ? 38.580  -10.617 68.883  1.00 10.75 ? 127 PRO D CA  1 
ATOM   7573  C  C   . PRO D  1 127 ? 37.305  -11.053 68.188  1.00 12.60 ? 127 PRO D C   1 
ATOM   7574  O  O   . PRO D  1 127 ? 36.944  -12.212 68.343  1.00 13.72 ? 127 PRO D O   1 
ATOM   7575  C  CB  . PRO D  1 127 ? 38.196  -10.103 70.301  1.00 11.44 ? 127 PRO D CB  1 
ATOM   7576  C  CG  . PRO D  1 127 ? 37.971  -8.682  70.205  1.00 10.89 ? 127 PRO D CG  1 
ATOM   7577  C  CD  . PRO D  1 127 ? 39.156  -8.285  69.241  1.00 11.66 ? 127 PRO D CD  1 
ATOM   7578  N  N   . ASP D  1 128 ? 36.704  -10.128 67.409  1.00 10.09 ? 128 ASP D N   1 
ATOM   7579  C  CA  . ASP D  1 128 ? 35.370  -10.397 66.807  1.00 11.20 ? 128 ASP D CA  1 
ATOM   7580  C  C   . ASP D  1 128 ? 35.149  -9.325  65.716  1.00 10.34 ? 128 ASP D C   1 
ATOM   7581  O  O   . ASP D  1 128 ? 35.910  -8.346  65.615  1.00 10.68 ? 128 ASP D O   1 
ATOM   7582  C  CB  . ASP D  1 128 ? 34.249  -10.528 67.854  1.00 10.98 ? 128 ASP D CB  1 
ATOM   7583  C  CG  . ASP D  1 128 ? 34.052  -9.276  68.685  1.00 17.42 ? 128 ASP D CG  1 
ATOM   7584  O  OD1 . ASP D  1 128 ? 34.139  -8.137  68.210  1.00 16.04 ? 128 ASP D OD1 1 
ATOM   7585  O  OD2 . ASP D  1 128 ? 33.849  -9.462  69.899  1.00 27.10 ? 128 ASP D OD2 1 
ATOM   7586  N  N   . ALA D  1 129 ? 34.131  -9.619  64.860  1.00 7.77  ? 129 ALA D N   1 
ATOM   7587  C  CA  . ALA D  1 129 ? 33.902  -8.764  63.745  1.00 6.93  ? 129 ALA D CA  1 
ATOM   7588  C  C   . ALA D  1 129 ? 33.394  -7.390  64.165  1.00 9.15  ? 129 ALA D C   1 
ATOM   7589  O  O   . ALA D  1 129 ? 33.694  -6.380  63.468  1.00 9.43  ? 129 ALA D O   1 
ATOM   7590  C  CB  . ALA D  1 129 ? 32.902  -9.416  62.743  1.00 10.32 ? 129 ALA D CB  1 
ATOM   7591  N  N   . SER D  1 130 ? 32.571  -7.331  65.251  1.00 9.30  ? 130 SER D N   1 
ATOM   7592  C  CA  . SER D  1 130 ? 32.059  -6.054  65.674  1.00 10.05 ? 130 SER D CA  1 
ATOM   7593  C  C   . SER D  1 130 ? 33.223  -5.121  66.090  1.00 10.98 ? 130 SER D C   1 
ATOM   7594  O  O   . SER D  1 130 ? 33.260  -3.949  65.692  1.00 12.46 ? 130 SER D O   1 
ATOM   7595  C  CB  . SER D  1 130 ? 31.074  -6.269  66.847  1.00 13.99 ? 130 SER D CB  1 
ATOM   7596  O  OG  . SER D  1 130 ? 30.605  -5.005  67.321  1.00 20.36 ? 130 SER D OG  1 
ATOM   7597  N  N   . THR D  1 131 ? 34.154  -5.666  66.859  1.00 11.12 ? 131 THR D N   1 
ATOM   7598  C  CA  . THR D  1 131 ? 35.335  -4.859  67.276  1.00 11.73 ? 131 THR D CA  1 
ATOM   7599  C  C   . THR D  1 131 ? 36.185  -4.513  66.068  1.00 11.92 ? 131 THR D C   1 
ATOM   7600  O  O   . THR D  1 131 ? 36.715  -3.418  65.953  1.00 12.00 ? 131 THR D O   1 
ATOM   7601  C  CB  . THR D  1 131 ? 36.170  -5.676  68.254  1.00 12.20 ? 131 THR D CB  1 
ATOM   7602  O  OG1 . THR D  1 131 ? 35.303  -5.978  69.373  1.00 15.45 ? 131 THR D OG1 1 
ATOM   7603  C  CG2 . THR D  1 131 ? 37.389  -4.795  68.774  1.00 14.36 ? 131 THR D CG2 1 
ATOM   7604  N  N   . ALA D  1 132 ? 36.328  -5.461  65.105  1.00 9.59  ? 132 ALA D N   1 
ATOM   7605  C  CA  . ALA D  1 132 ? 37.213  -5.202  63.915  1.00 8.94  ? 132 ALA D CA  1 
ATOM   7606  C  C   . ALA D  1 132 ? 36.617  -4.169  62.953  1.00 8.53  ? 132 ALA D C   1 
ATOM   7607  O  O   . ALA D  1 132 ? 37.374  -3.504  62.211  1.00 8.03  ? 132 ALA D O   1 
ATOM   7608  C  CB  . ALA D  1 132 ? 37.439  -6.519  63.161  1.00 8.68  ? 132 ALA D CB  1 
ATOM   7609  N  N   A SER D  1 133 ? 35.263  -4.004  62.981  0.60 8.72  ? 133 SER D N   1 
ATOM   7610  N  N   B SER D  1 133 ? 35.289  -3.986  62.975  0.40 7.79  ? 133 SER D N   1 
ATOM   7611  C  CA  A SER D  1 133 ? 34.526  -3.413  61.863  0.60 9.22  ? 133 SER D CA  1 
ATOM   7612  C  CA  B SER D  1 133 ? 34.635  -3.328  61.870  0.40 7.02  ? 133 SER D CA  1 
ATOM   7613  C  C   A SER D  1 133 ? 34.982  -2.011  61.500  0.60 9.05  ? 133 SER D C   1 
ATOM   7614  C  C   B SER D  1 133 ? 35.105  -1.867  61.693  0.40 7.41  ? 133 SER D C   1 
ATOM   7615  O  O   A SER D  1 133 ? 34.980  -1.649  60.306  0.60 8.84  ? 133 SER D O   1 
ATOM   7616  O  O   B SER D  1 133 ? 35.193  -1.367  60.550  0.40 7.40  ? 133 SER D O   1 
ATOM   7617  C  CB  A SER D  1 133 ? 33.015  -3.321  62.201  0.60 11.90 ? 133 SER D CB  1 
ATOM   7618  C  CB  B SER D  1 133 ? 33.115  -3.459  62.056  0.40 9.12  ? 133 SER D CB  1 
ATOM   7619  O  OG  A SER D  1 133 ? 32.352  -2.616  61.125  0.60 14.06 ? 133 SER D OG  1 
ATOM   7620  O  OG  B SER D  1 133 ? 32.734  -2.802  63.230  0.40 6.49  ? 133 SER D OG  1 
ATOM   7621  N  N   A ASN D  1 134 ? 35.271  -1.177  62.527  0.50 9.17  ? 134 ASN D N   1 
ATOM   7622  N  N   B ASN D  1 134 ? 35.440  -1.154  62.770  0.50 8.03  ? 134 ASN D N   1 
ATOM   7623  C  CA  A ASN D  1 134 ? 35.705  0.231   62.321  0.50 8.67  ? 134 ASN D CA  1 
ATOM   7624  C  CA  B ASN D  1 134 ? 35.832  0.230   62.540  0.50 8.56  ? 134 ASN D CA  1 
ATOM   7625  C  C   A ASN D  1 134 ? 37.206  0.461   62.676  0.50 9.36  ? 134 ASN D C   1 
ATOM   7626  C  C   B ASN D  1 134 ? 37.262  0.413   62.997  0.50 9.33  ? 134 ASN D C   1 
ATOM   7627  O  O   A ASN D  1 134 ? 37.627  1.627   62.887  0.50 8.62  ? 134 ASN D O   1 
ATOM   7628  O  O   B ASN D  1 134 ? 37.713  1.444   63.609  0.50 11.61 ? 134 ASN D O   1 
ATOM   7629  C  CB  A ASN D  1 134 ? 34.804  1.236   63.077  0.50 10.35 ? 134 ASN D CB  1 
ATOM   7630  C  CB  B ASN D  1 134 ? 34.893  1.163   63.210  0.50 9.31  ? 134 ASN D CB  1 
ATOM   7631  C  CG  A ASN D  1 134 ? 34.993  1.188   64.599  0.50 13.59 ? 134 ASN D CG  1 
ATOM   7632  C  CG  B ASN D  1 134 ? 35.030  2.505   62.682  0.50 9.08  ? 134 ASN D CG  1 
ATOM   7633  O  OD1 A ASN D  1 134 ? 35.426  0.187   65.123  0.50 18.31 ? 134 ASN D OD1 1 
ATOM   7634  O  OD1 B ASN D  1 134 ? 35.277  2.705   61.474  0.50 9.79  ? 134 ASN D OD1 1 
ATOM   7635  N  ND2 A ASN D  1 134 ? 34.694  2.287   65.318  0.50 15.99 ? 134 ASN D ND2 1 
ATOM   7636  N  ND2 B ASN D  1 134 ? 34.915  3.476   63.565  0.50 12.94 ? 134 ASN D ND2 1 
ATOM   7637  N  N   . LYS D  1 135 ? 38.023  -0.602  62.668  1.00 8.54  ? 135 LYS D N   1 
ATOM   7638  C  CA  . LYS D  1 135 ? 39.450  -0.543  63.015  1.00 10.64 ? 135 LYS D CA  1 
ATOM   7639  C  C   . LYS D  1 135 ? 40.368  -0.747  61.854  1.00 11.34 ? 135 LYS D C   1 
ATOM   7640  O  O   . LYS D  1 135 ? 40.028  -1.466  60.868  1.00 11.29 ? 135 LYS D O   1 
ATOM   7641  C  CB  . LYS D  1 135 ? 39.772  -1.490  64.195  1.00 12.72 ? 135 LYS D CB  1 
ATOM   7642  C  CG  . LYS D  1 135 ? 39.043  -0.997  65.454  1.00 15.08 ? 135 LYS D CG  1 
ATOM   7643  C  CD  . LYS D  1 135 ? 39.363  -1.735  66.750  1.00 20.35 ? 135 LYS D CD  1 
ATOM   7644  C  CE  . LYS D  1 135 ? 38.482  -1.180  67.933  1.00 23.16 ? 135 LYS D CE  1 
ATOM   7645  N  NZ  . LYS D  1 135 ? 36.960  -1.175  67.539  1.00 22.53 ? 135 LYS D NZ  1 
ATOM   7646  N  N   . SER D  1 136 ? 41.551  -0.165  61.921  1.00 10.27 ? 136 SER D N   1 
ATOM   7647  C  CA  . SER D  1 136 ? 42.583  -0.445  60.870  1.00 10.37 ? 136 SER D CA  1 
ATOM   7648  C  C   . SER D  1 136 ? 42.755  -1.916  60.598  1.00 10.53 ? 136 SER D C   1 
ATOM   7649  O  O   . SER D  1 136 ? 42.963  -2.740  61.494  1.00 10.63 ? 136 SER D O   1 
ATOM   7650  C  CB  . SER D  1 136 ? 43.917  0.152   61.435  1.00 9.67  ? 136 SER D CB  1 
ATOM   7651  O  OG  . SER D  1 136 ? 44.960  -0.032  60.462  1.00 12.74 ? 136 SER D OG  1 
ATOM   7652  N  N   . GLU D  1 137 ? 42.780  -2.217  59.285  1.00 9.63  ? 137 GLU D N   1 
ATOM   7653  C  CA  . GLU D  1 137 ? 42.992  -3.576  58.783  1.00 10.05 ? 137 GLU D CA  1 
ATOM   7654  C  C   . GLU D  1 137 ? 41.902  -4.530  59.274  1.00 10.88 ? 137 GLU D C   1 
ATOM   7655  O  O   . GLU D  1 137 ? 42.200  -5.719  59.401  1.00 9.45  ? 137 GLU D O   1 
ATOM   7656  C  CB  . GLU D  1 137 ? 44.408  -4.108  59.161  1.00 10.96 ? 137 GLU D CB  1 
ATOM   7657  C  CG  . GLU D  1 137 ? 45.496  -3.131  58.723  1.00 12.66 ? 137 GLU D CG  1 
ATOM   7658  C  CD  . GLU D  1 137 ? 46.840  -3.364  59.417  1.00 15.89 ? 137 GLU D CD  1 
ATOM   7659  O  OE1 . GLU D  1 137 ? 47.260  -4.554  59.431  1.00 18.49 ? 137 GLU D OE1 1 
ATOM   7660  O  OE2 . GLU D  1 137 ? 47.513  -2.329  59.874  1.00 18.75 ? 137 GLU D OE2 1 
ATOM   7661  N  N   . GLY D  1 138 ? 40.704  -4.034  59.511  1.00 7.31  ? 138 GLY D N   1 
ATOM   7662  C  CA  . GLY D  1 138 ? 39.793  -4.885  60.232  1.00 7.67  ? 138 GLY D CA  1 
ATOM   7663  C  C   . GLY D  1 138 ? 39.105  -5.935  59.447  1.00 6.48  ? 138 GLY D C   1 
ATOM   7664  O  O   . GLY D  1 138 ? 38.744  -6.961  60.094  1.00 7.15  ? 138 GLY D O   1 
ATOM   7665  N  N   . LEU D  1 139 ? 38.826  -5.673  58.176  1.00 6.59  ? 139 LEU D N   1 
ATOM   7666  C  CA  . LEU D  1 139 ? 37.963  -6.591  57.447  1.00 6.46  ? 139 LEU D CA  1 
ATOM   7667  C  C   . LEU D  1 139 ? 38.486  -6.995  56.116  1.00 4.88  ? 139 LEU D C   1 
ATOM   7668  O  O   . LEU D  1 139 ? 39.274  -6.296  55.490  1.00 5.09  ? 139 LEU D O   1 
ATOM   7669  C  CB  . LEU D  1 139 ? 36.576  -5.887  57.190  1.00 6.51  ? 139 LEU D CB  1 
ATOM   7670  C  CG  . LEU D  1 139 ? 35.836  -5.451  58.447  1.00 6.70  ? 139 LEU D CG  1 
ATOM   7671  C  CD1 . LEU D  1 139 ? 34.599  -4.658  58.097  1.00 6.69  ? 139 LEU D CD1 1 
ATOM   7672  C  CD2 . LEU D  1 139 ? 35.414  -6.635  59.435  1.00 7.51  ? 139 LEU D CD2 1 
ATOM   7673  N  N   . ALA D  1 140 ? 38.025  -8.129  55.637  1.00 5.39  ? 140 ALA D N   1 
ATOM   7674  C  CA  . ALA D  1 140 ? 38.369  -8.624  54.221  1.00 5.43  ? 140 ALA D CA  1 
ATOM   7675  C  C   . ALA D  1 140 ? 37.108  -9.266  53.682  1.00 5.78  ? 140 ALA D C   1 
ATOM   7676  O  O   . ALA D  1 140 ? 36.519  -10.143 54.386  1.00 5.38  ? 140 ALA D O   1 
ATOM   7677  C  CB  . ALA D  1 140 ? 39.519  -9.587  54.272  1.00 6.27  ? 140 ALA D CB  1 
ATOM   7678  N  N   . VAL D  1 141 ? 36.644  -8.806  52.531  1.00 4.54  ? 141 VAL D N   1 
ATOM   7679  C  CA  . VAL D  1 141 ? 35.442  -9.424  51.954  1.00 4.67  ? 141 VAL D CA  1 
ATOM   7680  C  C   . VAL D  1 141 ? 35.846  -10.023 50.574  1.00 5.41  ? 141 VAL D C   1 
ATOM   7681  O  O   . VAL D  1 141 ? 36.664  -9.413  49.792  1.00 5.95  ? 141 VAL D O   1 
ATOM   7682  C  CB  . VAL D  1 141 ? 34.345  -8.274  51.736  1.00 4.47  ? 141 VAL D CB  1 
ATOM   7683  C  CG1 . VAL D  1 141 ? 33.089  -8.892  51.152  1.00 5.01  ? 141 VAL D CG1 1 
ATOM   7684  C  CG2 . VAL D  1 141 ? 34.060  -7.595  53.087  1.00 5.05  ? 141 VAL D CG2 1 
ATOM   7685  N  N   . LEU D  1 142 ? 35.292  -11.207 50.338  1.00 4.48  ? 142 LEU D N   1 
ATOM   7686  C  CA  . LEU D  1 142 ? 35.479  -11.847 49.009  1.00 4.98  ? 142 LEU D CA  1 
ATOM   7687  C  C   . LEU D  1 142 ? 34.164  -11.525 48.282  1.00 3.93  ? 142 LEU D C   1 
ATOM   7688  O  O   . LEU D  1 142 ? 33.066  -11.767 48.813  1.00 4.90  ? 142 LEU D O   1 
ATOM   7689  C  CB  . LEU D  1 142 ? 35.568  -13.373 49.118  1.00 4.81  ? 142 LEU D CB  1 
ATOM   7690  C  CG  . LEU D  1 142 ? 36.736  -13.837 50.064  1.00 6.47  ? 142 LEU D CG  1 
ATOM   7691  C  CD1 . LEU D  1 142 ? 36.751  -15.420 50.103  1.00 8.05  ? 142 LEU D CD1 1 
ATOM   7692  C  CD2 . LEU D  1 142 ? 38.040  -13.211 49.616  1.00 7.98  ? 142 LEU D CD2 1 
ATOM   7693  N  N   . ALA D  1 143 ? 34.285  -11.067 47.030  1.00 5.00  ? 143 ALA D N   1 
ATOM   7694  C  CA  . ALA D  1 143 ? 33.116  -10.830 46.155  1.00 4.62  ? 143 ALA D CA  1 
ATOM   7695  C  C   . ALA D  1 143 ? 33.099  -11.770 44.981  1.00 5.15  ? 143 ALA D C   1 
ATOM   7696  O  O   . ALA D  1 143 ? 34.118  -11.894 44.262  1.00 5.74  ? 143 ALA D O   1 
ATOM   7697  C  CB  . ALA D  1 143 ? 33.219  -9.396  45.644  1.00 6.81  ? 143 ALA D CB  1 
ATOM   7698  N  N   . VAL D  1 144 ? 31.938  -12.411 44.802  1.00 4.70  ? 144 VAL D N   1 
ATOM   7699  C  CA  . VAL D  1 144 ? 31.754  -13.309 43.626  1.00 5.14  ? 144 VAL D CA  1 
ATOM   7700  C  C   . VAL D  1 144 ? 30.626  -12.644 42.776  1.00 5.23  ? 144 VAL D C   1 
ATOM   7701  O  O   . VAL D  1 144 ? 29.519  -12.376 43.229  1.00 6.00  ? 144 VAL D O   1 
ATOM   7702  C  CB  . VAL D  1 144 ? 31.259  -14.685 44.096  1.00 5.84  ? 144 VAL D CB  1 
ATOM   7703  C  CG1 . VAL D  1 144 ? 31.094  -15.561 42.823  1.00 8.62  ? 144 VAL D CG1 1 
ATOM   7704  C  CG2 . VAL D  1 144 ? 32.296  -15.336 44.994  1.00 6.36  ? 144 VAL D CG2 1 
ATOM   7705  N  N   . LEU D  1 145 ? 30.999  -12.381 41.525  1.00 6.07  ? 145 LEU D N   1 
ATOM   7706  C  CA  . LEU D  1 145 ? 30.065  -11.823 40.526  1.00 5.89  ? 145 LEU D CA  1 
ATOM   7707  C  C   . LEU D  1 145 ? 29.134  -12.927 40.046  1.00 6.23  ? 145 LEU D C   1 
ATOM   7708  O  O   . LEU D  1 145 ? 29.694  -14.062 39.795  1.00 6.84  ? 145 LEU D O   1 
ATOM   7709  C  CB  . LEU D  1 145 ? 30.859  -11.174 39.362  1.00 6.39  ? 145 LEU D CB  1 
ATOM   7710  C  CG  . LEU D  1 145 ? 31.775  -9.996  39.819  1.00 7.15  ? 145 LEU D CG  1 
ATOM   7711  C  CD1 . LEU D  1 145 ? 32.705  -9.651  38.663  1.00 9.57  ? 145 LEU D CD1 1 
ATOM   7712  C  CD2 . LEU D  1 145 ? 30.904  -8.808  40.190  1.00 8.79  ? 145 LEU D CD2 1 
ATOM   7713  N  N   . ILE D  1 146 ? 27.826  -12.651 39.876  1.00 5.87  ? 146 ILE D N   1 
ATOM   7714  C  CA  . ILE D  1 146 ? 26.903  -13.749 39.475  1.00 4.88  ? 146 ILE D CA  1 
ATOM   7715  C  C   . ILE D  1 146 ? 26.178  -13.304 38.190  1.00 6.72  ? 146 ILE D C   1 
ATOM   7716  O  O   . ILE D  1 146 ? 25.704  -12.178 38.108  1.00 7.29  ? 146 ILE D O   1 
ATOM   7717  C  CB  . ILE D  1 146 ? 25.823  -13.847 40.596  1.00 6.22  ? 146 ILE D CB  1 
ATOM   7718  C  CG1 . ILE D  1 146 ? 26.495  -14.259 41.967  1.00 7.28  ? 146 ILE D CG1 1 
ATOM   7719  C  CG2 . ILE D  1 146 ? 24.773  -14.892 40.163  1.00 6.51  ? 146 ILE D CG2 1 
ATOM   7720  C  CD1 . ILE D  1 146 ? 25.611  -14.212 43.152  1.00 5.56  ? 146 ILE D CD1 1 
ATOM   7721  N  N   . GLU D  1 147 ? 26.098  -14.249 37.247  1.00 7.35  ? 147 GLU D N   1 
ATOM   7722  C  CA  . GLU D  1 147 ? 25.395  -13.922 35.978  1.00 8.89  ? 147 GLU D CA  1 
ATOM   7723  C  C   . GLU D  1 147 ? 24.331  -14.999 35.714  1.00 9.47  ? 147 GLU D C   1 
ATOM   7724  O  O   . GLU D  1 147 ? 24.439  -16.063 36.311  1.00 9.99  ? 147 GLU D O   1 
ATOM   7725  C  CB  . GLU D  1 147 ? 26.385  -13.856 34.824  1.00 10.04 ? 147 GLU D CB  1 
ATOM   7726  C  CG  . GLU D  1 147 ? 27.078  -15.169 34.483  1.00 10.46 ? 147 GLU D CG  1 
ATOM   7727  C  CD  . GLU D  1 147 ? 28.075  -14.950 33.381  1.00 13.65 ? 147 GLU D CD  1 
ATOM   7728  O  OE1 . GLU D  1 147 ? 28.562  -13.843 33.039  1.00 14.83 ? 147 GLU D OE1 1 
ATOM   7729  O  OE2 . GLU D  1 147 ? 28.492  -15.967 32.826  1.00 18.16 ? 147 GLU D OE2 1 
ATOM   7730  N  N   A MET D  1 148 ? 23.226  -14.690 34.987  0.50 10.39 ? 148 MET D N   1 
ATOM   7731  N  N   B MET D  1 148 ? 23.480  -14.705 34.699  0.50 9.65  ? 148 MET D N   1 
ATOM   7732  C  CA  A MET D  1 148 ? 22.204  -15.727 34.711  0.50 11.70 ? 148 MET D CA  1 
ATOM   7733  C  CA  B MET D  1 148 ? 22.475  -15.661 34.380  0.50 10.55 ? 148 MET D CA  1 
ATOM   7734  C  C   A MET D  1 148 ? 22.799  -16.716 33.667  0.50 10.75 ? 148 MET D C   1 
ATOM   7735  C  C   B MET D  1 148 ? 23.101  -16.850 33.600  0.50 9.27  ? 148 MET D C   1 
ATOM   7736  O  O   A MET D  1 148 ? 23.386  -16.263 32.672  0.50 10.89 ? 148 MET D O   1 
ATOM   7737  O  O   B MET D  1 148 ? 24.005  -16.721 32.772  0.50 9.39  ? 148 MET D O   1 
ATOM   7738  C  CB  A MET D  1 148 ? 20.907  -15.017 34.204  0.50 12.38 ? 148 MET D CB  1 
ATOM   7739  C  CB  B MET D  1 148 ? 21.318  -14.963 33.652  0.50 10.55 ? 148 MET D CB  1 
ATOM   7740  C  CG  A MET D  1 148 ? 19.743  -15.959 34.036  0.50 15.18 ? 148 MET D CG  1 
ATOM   7741  C  CG  B MET D  1 148 ? 20.138  -15.833 33.734  0.50 13.86 ? 148 MET D CG  1 
ATOM   7742  S  SD  A MET D  1 148 ? 18.441  -15.264 32.954  0.50 19.54 ? 148 MET D SD  1 
ATOM   7743  S  SD  B MET D  1 148 ? 19.901  -16.799 32.228  0.50 20.64 ? 148 MET D SD  1 
ATOM   7744  C  CE  A MET D  1 148 ? 19.344  -15.045 31.469  0.50 14.31 ? 148 MET D CE  1 
ATOM   7745  C  CE  B MET D  1 148 ? 21.293  -16.430 31.115  0.50 25.01 ? 148 MET D CE  1 
ATOM   7746  N  N   . GLY D  1 149 ? 22.644  -18.033 33.929  1.00 10.11 ? 149 GLY D N   1 
ATOM   7747  C  CA  . GLY D  1 149 ? 23.070  -19.200 33.110  1.00 10.01 ? 149 GLY D CA  1 
ATOM   7748  C  C   . GLY D  1 149 ? 22.476  -20.466 33.602  1.00 9.97  ? 149 GLY D C   1 
ATOM   7749  O  O   . GLY D  1 149 ? 21.248  -20.533 33.781  1.00 9.52  ? 149 GLY D O   1 
ATOM   7750  N  N   . SER D  1 150 ? 23.296  -21.437 33.912  1.00 11.01 ? 150 SER D N   1 
ATOM   7751  C  CA  . SER D  1 150 ? 22.729  -22.707 34.298  1.00 11.36 ? 150 SER D CA  1 
ATOM   7752  C  C   . SER D  1 150 ? 22.241  -22.725 35.761  1.00 12.25 ? 150 SER D C   1 
ATOM   7753  O  O   . SER D  1 150 ? 22.839  -22.000 36.640  1.00 11.65 ? 150 SER D O   1 
ATOM   7754  C  CB  . SER D  1 150 ? 23.707  -23.892 34.178  1.00 12.67 ? 150 SER D CB  1 
ATOM   7755  O  OG  . SER D  1 150 ? 24.936  -23.648 34.846  1.00 19.63 ? 150 SER D OG  1 
ATOM   7756  N  N   . PHE D  1 151 ? 21.312  -23.566 36.142  1.00 11.54 ? 151 PHE D N   1 
ATOM   7757  C  CA  . PHE D  1 151 ? 20.909  -23.795 37.490  1.00 9.87  ? 151 PHE D CA  1 
ATOM   7758  C  C   . PHE D  1 151 ? 22.095  -24.142 38.368  1.00 10.79 ? 151 PHE D C   1 
ATOM   7759  O  O   . PHE D  1 151 ? 22.949  -24.963 37.975  1.00 13.43 ? 151 PHE D O   1 
ATOM   7760  C  CB  . PHE D  1 151 ? 19.809  -24.893 37.584  1.00 10.69 ? 151 PHE D CB  1 
ATOM   7761  C  CG  . PHE D  1 151 ? 19.388  -25.196 39.001  1.00 11.75 ? 151 PHE D CG  1 
ATOM   7762  C  CD1 . PHE D  1 151 ? 18.471  -24.369 39.737  1.00 13.32 ? 151 PHE D CD1 1 
ATOM   7763  C  CD2 . PHE D  1 151 ? 19.860  -26.333 39.608  1.00 13.51 ? 151 PHE D CD2 1 
ATOM   7764  C  CE1 . PHE D  1 151 ? 18.158  -24.719 41.041  1.00 14.51 ? 151 PHE D CE1 1 
ATOM   7765  C  CE2 . PHE D  1 151 ? 19.481  -26.707 40.901  1.00 12.01 ? 151 PHE D CE2 1 
ATOM   7766  C  CZ  . PHE D  1 151 ? 18.643  -25.856 41.631  1.00 14.23 ? 151 PHE D CZ  1 
ATOM   7767  N  N   . ASN D  1 152 ? 22.200  -23.600 39.609  1.00 8.68  ? 152 ASN D N   1 
ATOM   7768  C  CA  . ASN D  1 152 ? 23.375  -23.825 40.430  1.00 8.50  ? 152 ASN D CA  1 
ATOM   7769  C  C   . ASN D  1 152 ? 22.920  -24.444 41.751  1.00 10.23 ? 152 ASN D C   1 
ATOM   7770  O  O   . ASN D  1 152 ? 22.339  -23.777 42.666  1.00 8.73  ? 152 ASN D O   1 
ATOM   7771  C  CB  . ASN D  1 152 ? 24.089  -22.434 40.639  1.00 8.75  ? 152 ASN D CB  1 
ATOM   7772  C  CG  . ASN D  1 152 ? 25.406  -22.595 41.387  1.00 7.66  ? 152 ASN D CG  1 
ATOM   7773  O  OD1 . ASN D  1 152 ? 25.462  -23.293 42.417  1.00 9.14  ? 152 ASN D OD1 1 
ATOM   7774  N  ND2 . ASN D  1 152 ? 26.430  -21.881 40.922  1.00 8.29  ? 152 ASN D ND2 1 
ATOM   7775  N  N   . PRO D  1 153 ? 23.067  -25.773 41.908  1.00 9.92  ? 153 PRO D N   1 
ATOM   7776  C  CA  . PRO D  1 153 ? 22.555  -26.427 43.107  1.00 9.72  ? 153 PRO D CA  1 
ATOM   7777  C  C   . PRO D  1 153 ? 23.159  -25.871 44.399  1.00 9.44  ? 153 PRO D C   1 
ATOM   7778  O  O   . PRO D  1 153 ? 22.529  -25.886 45.470  1.00 12.10 ? 153 PRO D O   1 
ATOM   7779  C  CB  . PRO D  1 153 ? 22.996  -27.932 43.002  1.00 11.69 ? 153 PRO D CB  1 
ATOM   7780  C  CG  . PRO D  1 153 ? 23.168  -28.086 41.497  1.00 14.84 ? 153 PRO D CG  1 
ATOM   7781  C  CD  . PRO D  1 153 ? 23.628  -26.719 40.906  1.00 12.64 ? 153 PRO D CD  1 
ATOM   7782  N  N   . SER D  1 154 ? 24.441  -25.425 44.321  1.00 8.87  ? 154 SER D N   1 
ATOM   7783  C  CA  . SER D  1 154 ? 25.047  -24.926 45.513  1.00 8.44  ? 154 SER D CA  1 
ATOM   7784  C  C   . SER D  1 154 ? 24.458  -23.574 46.016  1.00 7.35  ? 154 SER D C   1 
ATOM   7785  O  O   . SER D  1 154 ? 24.206  -23.462 47.216  1.00 7.36  ? 154 SER D O   1 
ATOM   7786  C  CB  . SER D  1 154 ? 26.520  -24.715 45.328  1.00 9.77  ? 154 SER D CB  1 
ATOM   7787  O  OG  . SER D  1 154 ? 27.120  -26.032 44.958  1.00 13.00 ? 154 SER D OG  1 
ATOM   7788  N  N   . TYR D  1 155 ? 24.165  -22.618 45.099  1.00 7.42  ? 155 TYR D N   1 
ATOM   7789  C  CA  . TYR D  1 155 ? 23.439  -21.460 45.517  1.00 6.79  ? 155 TYR D CA  1 
ATOM   7790  C  C   . TYR D  1 155 ? 22.046  -21.792 46.028  1.00 7.81  ? 155 TYR D C   1 
ATOM   7791  O  O   . TYR D  1 155 ? 21.517  -21.040 46.886  1.00 7.61  ? 155 TYR D O   1 
ATOM   7792  C  CB  . TYR D  1 155 ? 23.404  -20.384 44.472  1.00 7.53  ? 155 TYR D CB  1 
ATOM   7793  C  CG  . TYR D  1 155 ? 24.736  -19.614 44.487  1.00 7.06  ? 155 TYR D CG  1 
ATOM   7794  C  CD1 . TYR D  1 155 ? 25.917  -20.125 43.896  1.00 6.73  ? 155 TYR D CD1 1 
ATOM   7795  C  CD2 . TYR D  1 155 ? 24.796  -18.342 45.025  1.00 7.40  ? 155 TYR D CD2 1 
ATOM   7796  C  CE1 . TYR D  1 155 ? 27.097  -19.344 43.855  1.00 6.40  ? 155 TYR D CE1 1 
ATOM   7797  C  CE2 . TYR D  1 155 ? 25.998  -17.596 44.989  1.00 6.68  ? 155 TYR D CE2 1 
ATOM   7798  C  CZ  . TYR D  1 155 ? 27.124  -18.144 44.460  1.00 5.98  ? 155 TYR D CZ  1 
ATOM   7799  O  OH  . TYR D  1 155 ? 28.340  -17.454 44.472  1.00 7.01  ? 155 TYR D OH  1 
ATOM   7800  N  N   . ASP D  1 156 ? 21.411  -22.900 45.484  1.00 7.75  ? 156 ASP D N   1 
ATOM   7801  C  CA  . ASP D  1 156 ? 20.092  -23.243 45.991  1.00 8.29  ? 156 ASP D CA  1 
ATOM   7802  C  C   . ASP D  1 156 ? 20.126  -23.667 47.463  1.00 7.74  ? 156 ASP D C   1 
ATOM   7803  O  O   . ASP D  1 156 ? 19.068  -23.753 48.079  1.00 9.43  ? 156 ASP D O   1 
ATOM   7804  C  CB  . ASP D  1 156 ? 19.361  -24.288 45.089  1.00 11.26 ? 156 ASP D CB  1 
ATOM   7805  C  CG  . ASP D  1 156 ? 18.036  -23.735 44.627  1.00 12.19 ? 156 ASP D CG  1 
ATOM   7806  O  OD1 . ASP D  1 156 ? 17.046  -24.511 44.763  1.00 14.85 ? 156 ASP D OD1 1 
ATOM   7807  O  OD2 . ASP D  1 156 ? 17.963  -22.500 44.222  1.00 11.78 ? 156 ASP D OD2 1 
ATOM   7808  N  N   . LYS D  1 157 ? 21.317  -24.025 48.021  1.00 8.50  ? 157 LYS D N   1 
ATOM   7809  C  CA  . LYS D  1 157 ? 21.392  -24.285 49.442  1.00 10.19 ? 157 LYS D CA  1 
ATOM   7810  C  C   . LYS D  1 157 ? 21.136  -23.106 50.300  1.00 10.35 ? 157 LYS D C   1 
ATOM   7811  O  O   . LYS D  1 157 ? 20.841  -23.271 51.484  1.00 11.88 ? 157 LYS D O   1 
ATOM   7812  C  CB  . LYS D  1 157 ? 22.762  -24.933 49.799  1.00 10.55 ? 157 LYS D CB  1 
ATOM   7813  C  CG  . LYS D  1 157 ? 22.949  -26.303 48.993  1.00 9.07  ? 157 LYS D CG  1 
ATOM   7814  C  CD  . LYS D  1 157 ? 24.324  -26.933 49.193  1.00 10.06 ? 157 LYS D CD  1 
ATOM   7815  C  CE  . LYS D  1 157 ? 24.443  -28.170 48.307  1.00 11.96 ? 157 LYS D CE  1 
ATOM   7816  N  NZ  . LYS D  1 157 ? 25.786  -28.863 48.498  1.00 12.93 ? 157 LYS D NZ  1 
ATOM   7817  N  N   . ILE D  1 158 ? 21.197  -21.948 49.666  1.00 8.71  ? 158 ILE D N   1 
ATOM   7818  C  CA  . ILE D  1 158 ? 20.775  -20.744 50.335  1.00 8.11  ? 158 ILE D CA  1 
ATOM   7819  C  C   . ILE D  1 158 ? 19.331  -20.440 49.854  1.00 7.08  ? 158 ILE D C   1 
ATOM   7820  O  O   . ILE D  1 158 ? 18.408  -20.235 50.694  1.00 8.30  ? 158 ILE D O   1 
ATOM   7821  C  CB  . ILE D  1 158 ? 21.679  -19.502 50.045  1.00 9.31  ? 158 ILE D CB  1 
ATOM   7822  C  CG1 . ILE D  1 158 ? 23.091  -19.773 50.581  1.00 10.62 ? 158 ILE D CG1 1 
ATOM   7823  C  CG2 . ILE D  1 158 ? 21.073  -18.179 50.619  1.00 8.62  ? 158 ILE D CG2 1 
ATOM   7824  C  CD1 . ILE D  1 158 ? 24.183  -18.842 49.968  1.00 13.40 ? 158 ILE D CD1 1 
ATOM   7825  N  N   . PHE D  1 159 ? 19.092  -20.436 48.541  1.00 6.73  ? 159 PHE D N   1 
ATOM   7826  C  CA  . PHE D  1 159 ? 17.817  -19.828 47.967  1.00 6.96  ? 159 PHE D CA  1 
ATOM   7827  C  C   . PHE D  1 159 ? 16.588  -20.687 48.335  1.00 7.41  ? 159 PHE D C   1 
ATOM   7828  O  O   . PHE D  1 159 ? 15.472  -20.130 48.444  1.00 8.59  ? 159 PHE D O   1 
ATOM   7829  C  CB  . PHE D  1 159 ? 17.862  -19.673 46.462  1.00 5.94  ? 159 PHE D CB  1 
ATOM   7830  C  CG  . PHE D  1 159 ? 19.002  -18.788 45.946  1.00 7.18  ? 159 PHE D CG  1 
ATOM   7831  C  CD1 . PHE D  1 159 ? 19.557  -17.762 46.723  1.00 9.35  ? 159 PHE D CD1 1 
ATOM   7832  C  CD2 . PHE D  1 159 ? 19.412  -18.989 44.637  1.00 7.80  ? 159 PHE D CD2 1 
ATOM   7833  C  CE1 . PHE D  1 159 ? 20.556  -16.965 46.201  1.00 8.42  ? 159 PHE D CE1 1 
ATOM   7834  C  CE2 . PHE D  1 159 ? 20.441  -18.194 44.049  1.00 7.58  ? 159 PHE D CE2 1 
ATOM   7835  C  CZ  . PHE D  1 159 ? 20.988  -17.154 44.860  1.00 8.48  ? 159 PHE D CZ  1 
ATOM   7836  N  N   . SER D  1 160 ? 16.811  -21.966 48.608  1.00 7.35  ? 160 SER D N   1 
ATOM   7837  C  CA  . SER D  1 160 ? 15.627  -22.848 48.940  1.00 8.21  ? 160 SER D CA  1 
ATOM   7838  C  C   . SER D  1 160 ? 15.044  -22.529 50.276  1.00 10.09 ? 160 SER D C   1 
ATOM   7839  O  O   . SER D  1 160 ? 13.916  -23.001 50.538  1.00 11.07 ? 160 SER D O   1 
ATOM   7840  C  CB  . SER D  1 160 ? 16.042  -24.344 48.881  1.00 9.80  ? 160 SER D CB  1 
ATOM   7841  O  OG  . SER D  1 160 ? 17.027  -24.621 49.893  1.00 12.68 ? 160 SER D OG  1 
ATOM   7842  N  N   A HIS D  1 161 ? 15.672  -21.718 51.141  0.50 7.28  ? 161 HIS D N   1 
ATOM   7843  N  N   B HIS D  1 161 ? 15.700  -21.682 51.082  0.50 8.40  ? 161 HIS D N   1 
ATOM   7844  C  CA  A HIS D  1 161 ? 15.068  -21.385 52.408  0.50 7.08  ? 161 HIS D CA  1 
ATOM   7845  C  CA  B HIS D  1 161 ? 15.248  -21.347 52.400  0.50 8.29  ? 161 HIS D CA  1 
ATOM   7846  C  C   A HIS D  1 161 ? 14.501  -19.960 52.434  0.50 7.76  ? 161 HIS D C   1 
ATOM   7847  C  C   B HIS D  1 161 ? 14.660  -19.945 52.488  0.50 8.87  ? 161 HIS D C   1 
ATOM   7848  O  O   A HIS D  1 161 ? 13.960  -19.524 53.423  0.50 6.42  ? 161 HIS D O   1 
ATOM   7849  O  O   B HIS D  1 161 ? 14.265  -19.552 53.603  0.50 9.09  ? 161 HIS D O   1 
ATOM   7850  C  CB  A HIS D  1 161 ? 16.103  -21.547 53.508  0.50 7.68  ? 161 HIS D CB  1 
ATOM   7851  C  CB  B HIS D  1 161 ? 16.430  -21.326 53.348  0.50 9.77  ? 161 HIS D CB  1 
ATOM   7852  C  CG  A HIS D  1 161 ? 16.909  -22.803 53.361  0.50 6.79  ? 161 HIS D CG  1 
ATOM   7853  C  CG  B HIS D  1 161 ? 16.920  -22.689 53.702  0.50 11.46 ? 161 HIS D CG  1 
ATOM   7854  N  ND1 A HIS D  1 161 ? 16.343  -24.060 53.422  0.50 9.77  ? 161 HIS D ND1 1 
ATOM   7855  N  ND1 B HIS D  1 161 ? 18.029  -23.295 53.136  0.50 11.03 ? 161 HIS D ND1 1 
ATOM   7856  C  CD2 A HIS D  1 161 ? 18.223  -22.997 53.100  0.50 10.98 ? 161 HIS D CD2 1 
ATOM   7857  C  CD2 B HIS D  1 161 ? 16.431  -23.563 54.604  0.50 11.43 ? 161 HIS D CD2 1 
ATOM   7858  C  CE1 A HIS D  1 161 ? 17.279  -24.973 53.234  0.50 8.38  ? 161 HIS D CE1 1 
ATOM   7859  C  CE1 B HIS D  1 161 ? 18.207  -24.477 53.702  0.50 7.98  ? 161 HIS D CE1 1 
ATOM   7860  N  NE2 A HIS D  1 161 ? 18.429  -24.355 53.035  0.50 10.74 ? 161 HIS D NE2 1 
ATOM   7861  N  NE2 B HIS D  1 161 ? 17.248  -24.657 54.586  0.50 13.73 ? 161 HIS D NE2 1 
ATOM   7862  N  N   . LEU D  1 162 ? 14.619  -19.207 51.357  1.00 8.00  ? 162 LEU D N   1 
ATOM   7863  C  CA  . LEU D  1 162 ? 14.164  -17.800 51.444  1.00 10.14 ? 162 LEU D CA  1 
ATOM   7864  C  C   . LEU D  1 162 ? 12.712  -17.602 51.865  1.00 9.41  ? 162 LEU D C   1 
ATOM   7865  O  O   . LEU D  1 162 ? 12.407  -16.504 52.385  1.00 8.92  ? 162 LEU D O   1 
ATOM   7866  C  CB  . LEU D  1 162 ? 14.361  -17.110 50.077  1.00 10.66 ? 162 LEU D CB  1 
ATOM   7867  C  CG  . LEU D  1 162 ? 15.829  -17.086 49.622  1.00 13.54 ? 162 LEU D CG  1 
ATOM   7868  C  CD1 . LEU D  1 162 ? 15.860  -16.495 48.164  1.00 13.39 ? 162 LEU D CD1 1 
ATOM   7869  C  CD2 . LEU D  1 162 ? 16.680  -16.328 50.653  1.00 11.62 ? 162 LEU D CD2 1 
ATOM   7870  N  N   . GLN D  1 163 ? 11.813  -18.507 51.598  1.00 8.41  ? 163 GLN D N   1 
ATOM   7871  C  CA  . GLN D  1 163 ? 10.389  -18.205 51.994  1.00 8.25  ? 163 GLN D CA  1 
ATOM   7872  C  C   . GLN D  1 163 ? 10.202  -18.265 53.505  1.00 10.79 ? 163 GLN D C   1 
ATOM   7873  O  O   . GLN D  1 163 ? 9.059   -17.930 53.957  1.00 10.51 ? 163 GLN D O   1 
ATOM   7874  C  CB  . GLN D  1 163 ? 9.413   -19.140 51.317  1.00 9.23  ? 163 GLN D CB  1 
ATOM   7875  C  CG  . GLN D  1 163 ? 9.615   -19.274 49.739  1.00 11.70 ? 163 GLN D CG  1 
ATOM   7876  C  CD  . GLN D  1 163 ? 9.569   -17.910 49.054  1.00 12.47 ? 163 GLN D CD  1 
ATOM   7877  O  OE1 . GLN D  1 163 ? 8.608   -17.110 49.348  1.00 14.80 ? 163 GLN D OE1 1 
ATOM   7878  N  NE2 . GLN D  1 163 ? 10.669  -17.617 48.203  1.00 17.22 ? 163 GLN D NE2 1 
ATOM   7879  N  N   . HIS D  1 164 ? 11.245  -18.574 54.322  1.00 8.73  ? 164 HIS D N   1 
ATOM   7880  C  CA  . HIS D  1 164 ? 11.107  -18.593 55.772  1.00 9.78  ? 164 HIS D CA  1 
ATOM   7881  C  C   . HIS D  1 164 ? 11.702  -17.350 56.366  1.00 10.26 ? 164 HIS D C   1 
ATOM   7882  O  O   . HIS D  1 164 ? 11.665  -17.139 57.585  1.00 11.52 ? 164 HIS D O   1 
ATOM   7883  C  CB  . HIS D  1 164 ? 11.824  -19.802 56.428  1.00 10.49 ? 164 HIS D CB  1 
ATOM   7884  C  CG  . HIS D  1 164 ? 11.304  -21.105 55.885  1.00 9.33  ? 164 HIS D CG  1 
ATOM   7885  N  ND1 . HIS D  1 164 ? 9.974   -21.453 55.955  1.00 9.97  ? 164 HIS D ND1 1 
ATOM   7886  C  CD2 . HIS D  1 164 ? 11.911  -22.069 55.145  1.00 12.22 ? 164 HIS D CD2 1 
ATOM   7887  C  CE1 . HIS D  1 164 ? 9.759   -22.577 55.265  1.00 8.88  ? 164 HIS D CE1 1 
ATOM   7888  N  NE2 . HIS D  1 164 ? 10.934  -22.997 54.807  1.00 12.58 ? 164 HIS D NE2 1 
ATOM   7889  N  N   . VAL D  1 165 ? 12.274  -16.458 55.509  1.00 8.64  ? 165 VAL D N   1 
ATOM   7890  C  CA  . VAL D  1 165 ? 12.905  -15.198 56.058  1.00 8.04  ? 165 VAL D CA  1 
ATOM   7891  C  C   . VAL D  1 165 ? 12.402  -14.006 55.209  1.00 8.35  ? 165 VAL D C   1 
ATOM   7892  O  O   . VAL D  1 165 ? 13.189  -13.071 54.912  1.00 8.66  ? 165 VAL D O   1 
ATOM   7893  C  CB  . VAL D  1 165 ? 14.454  -15.277 56.080  1.00 9.27  ? 165 VAL D CB  1 
ATOM   7894  C  CG1 . VAL D  1 165 ? 14.894  -16.396 57.039  1.00 10.66 ? 165 VAL D CG1 1 
ATOM   7895  C  CG2 . VAL D  1 165 ? 15.096  -15.577 54.715  1.00 10.62 ? 165 VAL D CG2 1 
ATOM   7896  N  N   . LYS D  1 166 ? 11.128  -13.991 54.827  1.00 8.47  ? 166 LYS D N   1 
ATOM   7897  C  CA  . LYS D  1 166 ? 10.637  -13.023 53.821  1.00 7.25  ? 166 LYS D CA  1 
ATOM   7898  C  C   . LYS D  1 166 ? 10.664  -11.619 54.427  1.00 7.88  ? 166 LYS D C   1 
ATOM   7899  O  O   . LYS D  1 166 ? 10.771  -10.625 53.624  1.00 9.01  ? 166 LYS D O   1 
ATOM   7900  C  CB  . LYS D  1 166 ? 9.207   -13.359 53.376  1.00 8.33  ? 166 LYS D CB  1 
ATOM   7901  C  CG  . LYS D  1 166 ? 9.171   -14.673 52.562  1.00 9.89  ? 166 LYS D CG  1 
ATOM   7902  C  CD  . LYS D  1 166 ? 7.742   -15.132 52.088  1.00 10.80 ? 166 LYS D CD  1 
ATOM   7903  C  CE  . LYS D  1 166 ? 7.222   -14.246 50.940  1.00 12.16 ? 166 LYS D CE  1 
ATOM   7904  N  NZ  . LYS D  1 166 ? 8.014   -14.286 49.678  1.00 11.68 ? 166 LYS D NZ  1 
ATOM   7905  N  N   . TYR D  1 167 ? 10.423  -11.467 55.759  1.00 6.07  ? 167 TYR D N   1 
ATOM   7906  C  CA  . TYR D  1 167 ? 10.353  -10.188 56.377  1.00 6.12  ? 167 TYR D CA  1 
ATOM   7907  C  C   . TYR D  1 167 ? 11.459  -9.853  57.355  1.00 5.56  ? 167 TYR D C   1 
ATOM   7908  O  O   . TYR D  1 167 ? 12.063  -10.753 57.934  1.00 7.51  ? 167 TYR D O   1 
ATOM   7909  C  CB  . TYR D  1 167 ? 8.952   -9.942  57.070  1.00 7.93  ? 167 TYR D CB  1 
ATOM   7910  C  CG  . TYR D  1 167 ? 7.854   -9.986  56.000  1.00 8.68  ? 167 TYR D CG  1 
ATOM   7911  C  CD1 . TYR D  1 167 ? 7.137   -11.195 55.680  1.00 9.20  ? 167 TYR D CD1 1 
ATOM   7912  C  CD2 . TYR D  1 167 ? 7.517   -8.827  55.273  1.00 9.16  ? 167 TYR D CD2 1 
ATOM   7913  C  CE1 . TYR D  1 167 ? 6.245   -11.307 54.610  1.00 9.67  ? 167 TYR D CE1 1 
ATOM   7914  C  CE2 . TYR D  1 167 ? 6.562   -8.953  54.229  1.00 10.18 ? 167 TYR D CE2 1 
ATOM   7915  C  CZ  . TYR D  1 167 ? 5.978   -10.189 53.973  1.00 9.58  ? 167 TYR D CZ  1 
ATOM   7916  O  OH  . TYR D  1 167 ? 5.044   -10.157 52.931  1.00 15.82 ? 167 TYR D OH  1 
ATOM   7917  N  N   . LYS D  1 168 ? 11.722  -8.541  57.525  1.00 7.41  ? 168 LYS D N   1 
ATOM   7918  C  CA  . LYS D  1 168 ? 12.773  -8.099  58.464  1.00 9.80  ? 168 LYS D CA  1 
ATOM   7919  C  C   . LYS D  1 168 ? 12.673  -8.729  59.808  1.00 9.94  ? 168 LYS D C   1 
ATOM   7920  O  O   . LYS D  1 168 ? 11.588  -8.742  60.400  1.00 9.87  ? 168 LYS D O   1 
ATOM   7921  C  CB  . LYS D  1 168 ? 12.757  -6.574  58.567  1.00 8.67  ? 168 LYS D CB  1 
ATOM   7922  C  CG  . LYS D  1 168 ? 13.880  -6.008  59.522  1.00 10.88 ? 168 LYS D CG  1 
ATOM   7923  C  CD  . LYS D  1 168 ? 13.867  -4.526  59.477  1.00 15.24 ? 168 LYS D CD  1 
ATOM   7924  C  CE  . LYS D  1 168 ? 15.233  -4.104  60.122  1.00 18.95 ? 168 LYS D CE  1 
ATOM   7925  N  NZ  . LYS D  1 168 ? 15.369  -2.661  60.283  1.00 24.45 ? 168 LYS D NZ  1 
ATOM   7926  N  N   . GLY D  1 169 ? 13.798  -9.231  60.256  1.00 9.54  ? 169 GLY D N   1 
ATOM   7927  C  CA  . GLY D  1 169 ? 13.842  -9.760  61.632  1.00 10.65 ? 169 GLY D CA  1 
ATOM   7928  C  C   . GLY D  1 169 ? 13.550  -11.296 61.633  1.00 10.72 ? 169 GLY D C   1 
ATOM   7929  O  O   . GLY D  1 169 ? 13.760  -11.977 62.696  1.00 13.52 ? 169 GLY D O   1 
ATOM   7930  N  N   . GLN D  1 170 ? 12.978  -11.870 60.562  1.00 8.92  ? 170 GLN D N   1 
ATOM   7931  C  CA  . GLN D  1 170 ? 12.731  -13.343 60.477  1.00 8.18  ? 170 GLN D CA  1 
ATOM   7932  C  C   . GLN D  1 170 ? 14.041  -14.112 60.277  1.00 10.14 ? 170 GLN D C   1 
ATOM   7933  O  O   . GLN D  1 170 ? 14.946  -13.672 59.570  1.00 8.84  ? 170 GLN D O   1 
ATOM   7934  C  CB  . GLN D  1 170 ? 11.727  -13.612 59.378  1.00 8.66  ? 170 GLN D CB  1 
ATOM   7935  C  CG  . GLN D  1 170 ? 10.316  -13.021 59.797  1.00 8.73  ? 170 GLN D CG  1 
ATOM   7936  C  CD  . GLN D  1 170 ? 9.293   -13.369 58.767  1.00 8.30  ? 170 GLN D CD  1 
ATOM   7937  O  OE1 . GLN D  1 170 ? 9.514   -13.570 57.578  1.00 10.19 ? 170 GLN D OE1 1 
ATOM   7938  N  NE2 . GLN D  1 170 ? 8.015   -13.271 59.250  1.00 12.78 ? 170 GLN D NE2 1 
ATOM   7939  N  N   A GLU D  1 171 ? 14.197  -15.180 61.070  0.50 8.08  ? 171 GLU D N   1 
ATOM   7940  N  N   B GLU D  1 171 ? 14.021  -15.395 60.613  0.50 7.58  ? 171 GLU D N   1 
ATOM   7941  C  CA  A GLU D  1 171 ? 15.451  -16.012 61.026  0.50 7.61  ? 171 GLU D CA  1 
ATOM   7942  C  CA  B GLU D  1 171 ? 15.261  -16.136 60.781  0.50 8.33  ? 171 GLU D CA  1 
ATOM   7943  C  C   A GLU D  1 171 ? 15.123  -17.485 60.853  0.50 9.02  ? 171 GLU D C   1 
ATOM   7944  C  C   B GLU D  1 171 ? 14.981  -17.583 60.565  0.50 9.18  ? 171 GLU D C   1 
ATOM   7945  O  O   A GLU D  1 171 ? 13.999  -17.883 61.307  0.50 7.63  ? 171 GLU D O   1 
ATOM   7946  O  O   B GLU D  1 171 ? 13.853  -18.114 60.757  0.50 8.52  ? 171 GLU D O   1 
ATOM   7947  C  CB  A GLU D  1 171 ? 16.246  -15.796 62.308  0.50 9.45  ? 171 GLU D CB  1 
ATOM   7948  C  CB  B GLU D  1 171 ? 15.909  -15.892 62.171  0.50 8.90  ? 171 GLU D CB  1 
ATOM   7949  C  CG  A GLU D  1 171 ? 16.345  -14.365 62.679  0.50 10.49 ? 171 GLU D CG  1 
ATOM   7950  C  CG  B GLU D  1 171 ? 15.098  -16.223 63.445  0.50 10.99 ? 171 GLU D CG  1 
ATOM   7951  C  CD  A GLU D  1 171 ? 17.285  -14.089 63.784  0.50 15.36 ? 171 GLU D CD  1 
ATOM   7952  C  CD  B GLU D  1 171 ? 15.950  -16.151 64.754  0.50 12.89 ? 171 GLU D CD  1 
ATOM   7953  O  OE1 A GLU D  1 171 ? 18.243  -13.266 63.572  0.50 16.88 ? 171 GLU D OE1 1 
ATOM   7954  O  OE1 B GLU D  1 171 ? 16.841  -15.292 64.848  0.50 14.28 ? 171 GLU D OE1 1 
ATOM   7955  O  OE2 A GLU D  1 171 ? 17.118  -14.744 64.800  0.50 18.96 ? 171 GLU D OE2 1 
ATOM   7956  O  OE2 B GLU D  1 171 ? 15.708  -16.953 65.666  0.50 18.27 ? 171 GLU D OE2 1 
ATOM   7957  N  N   . ALA D  1 172 ? 16.024  -18.262 60.194  1.00 9.95  ? 172 ALA D N   1 
ATOM   7958  C  CA  . ALA D  1 172 ? 15.877  -19.743 60.010  1.00 9.25  ? 172 ALA D CA  1 
ATOM   7959  C  C   . ALA D  1 172 ? 17.205  -20.445 60.040  1.00 10.37 ? 172 ALA D C   1 
ATOM   7960  O  O   . ALA D  1 172 ? 18.153  -19.929 59.394  1.00 10.22 ? 172 ALA D O   1 
ATOM   7961  C  CB  . ALA D  1 172 ? 15.210  -20.017 58.688  1.00 9.89  ? 172 ALA D CB  1 
ATOM   7962  N  N   . PHE D  1 173 ? 17.424  -21.444 60.874  1.00 11.28 ? 173 PHE D N   1 
ATOM   7963  C  CA  . PHE D  1 173 ? 18.706  -22.207 60.842  1.00 11.78 ? 173 PHE D CA  1 
ATOM   7964  C  C   . PHE D  1 173 ? 18.715  -23.075 59.665  1.00 11.99 ? 173 PHE D C   1 
ATOM   7965  O  O   . PHE D  1 173 ? 17.690  -23.789 59.393  1.00 13.92 ? 173 PHE D O   1 
ATOM   7966  C  CB  . PHE D  1 173 ? 18.844  -23.061 62.111  1.00 11.14 ? 173 PHE D CB  1 
ATOM   7967  C  CG  . PHE D  1 173 ? 19.286  -22.282 63.322  1.00 11.19 ? 173 PHE D CG  1 
ATOM   7968  C  CD1 . PHE D  1 173 ? 18.433  -21.979 64.428  1.00 10.50 ? 173 PHE D CD1 1 
ATOM   7969  C  CD2 . PHE D  1 173 ? 20.600  -21.778 63.397  1.00 9.83  ? 173 PHE D CD2 1 
ATOM   7970  C  CE1 . PHE D  1 173 ? 18.904  -21.289 65.518  1.00 13.86 ? 173 PHE D CE1 1 
ATOM   7971  C  CE2 . PHE D  1 173 ? 21.078  -21.023 64.486  1.00 14.10 ? 173 PHE D CE2 1 
ATOM   7972  C  CZ  . PHE D  1 173 ? 20.212  -20.812 65.561  1.00 14.21 ? 173 PHE D CZ  1 
ATOM   7973  N  N   . VAL D  1 174 ? 19.876  -23.046 58.952  1.00 11.31 ? 174 VAL D N   1 
ATOM   7974  C  CA  . VAL D  1 174 ? 20.314  -23.823 57.755  1.00 12.73 ? 174 VAL D CA  1 
ATOM   7975  C  C   . VAL D  1 174 ? 21.376  -24.900 58.198  1.00 12.80 ? 174 VAL D C   1 
ATOM   7976  O  O   . VAL D  1 174 ? 22.233  -24.596 58.992  1.00 13.46 ? 174 VAL D O   1 
ATOM   7977  C  CB  . VAL D  1 174 ? 20.939  -22.866 56.736  1.00 12.20 ? 174 VAL D CB  1 
ATOM   7978  C  CG1 . VAL D  1 174 ? 21.556  -23.623 55.572  1.00 18.94 ? 174 VAL D CG1 1 
ATOM   7979  C  CG2 . VAL D  1 174 ? 19.913  -21.814 56.281  1.00 19.58 ? 174 VAL D CG2 1 
ATOM   7980  N  N   . PRO D  1 175 ? 21.362  -26.153 57.667  1.00 10.84 ? 175 PRO D N   1 
ATOM   7981  C  CA  . PRO D  1 175 ? 22.537  -27.031 57.894  1.00 10.92 ? 175 PRO D CA  1 
ATOM   7982  C  C   . PRO D  1 175 ? 23.769  -26.474 57.161  1.00 11.15 ? 175 PRO D C   1 
ATOM   7983  O  O   . PRO D  1 175 ? 23.711  -25.954 56.033  1.00 11.32 ? 175 PRO D O   1 
ATOM   7984  C  CB  . PRO D  1 175 ? 22.089  -28.420 57.309  1.00 11.64 ? 175 PRO D CB  1 
ATOM   7985  C  CG  . PRO D  1 175 ? 20.548  -28.277 57.234  1.00 15.78 ? 175 PRO D CG  1 
ATOM   7986  C  CD  . PRO D  1 175 ? 20.238  -26.831 57.005  1.00 13.49 ? 175 PRO D CD  1 
ATOM   7987  N  N   . GLY D  1 176 ? 24.919  -26.833 57.751  1.00 9.45  ? 176 GLY D N   1 
ATOM   7988  C  CA  . GLY D  1 176 ? 26.172  -26.471 57.039  1.00 8.22  ? 176 GLY D CA  1 
ATOM   7989  C  C   . GLY D  1 176 ? 26.269  -27.141 55.681  1.00 8.36  ? 176 GLY D C   1 
ATOM   7990  O  O   . GLY D  1 176 ? 25.830  -28.296 55.442  1.00 10.49 ? 176 GLY D O   1 
ATOM   7991  N  N   . PHE D  1 177 ? 26.978  -26.459 54.804  1.00 8.64  ? 177 PHE D N   1 
ATOM   7992  C  CA  . PHE D  1 177 ? 27.337  -27.000 53.503  1.00 8.13  ? 177 PHE D CA  1 
ATOM   7993  C  C   . PHE D  1 177 ? 28.742  -26.380 53.104  1.00 7.80  ? 177 PHE D C   1 
ATOM   7994  O  O   . PHE D  1 177 ? 29.235  -25.486 53.844  1.00 8.57  ? 177 PHE D O   1 
ATOM   7995  C  CB  . PHE D  1 177 ? 26.249  -26.768 52.428  1.00 8.54  ? 177 PHE D CB  1 
ATOM   7996  C  CG  . PHE D  1 177 ? 26.054  -25.303 52.060  1.00 9.11  ? 177 PHE D CG  1 
ATOM   7997  C  CD1 . PHE D  1 177 ? 26.698  -24.743 50.958  1.00 8.28  ? 177 PHE D CD1 1 
ATOM   7998  C  CD2 . PHE D  1 177 ? 25.224  -24.491 52.819  1.00 8.94  ? 177 PHE D CD2 1 
ATOM   7999  C  CE1 . PHE D  1 177 ? 26.506  -23.405 50.631  1.00 10.47 ? 177 PHE D CE1 1 
ATOM   8000  C  CE2 . PHE D  1 177 ? 25.032  -23.162 52.496  1.00 9.13  ? 177 PHE D CE2 1 
ATOM   8001  C  CZ  . PHE D  1 177 ? 25.672  -22.619 51.402  1.00 7.94  ? 177 PHE D CZ  1 
ATOM   8002  N  N   . ASN D  1 178 ? 29.283  -26.878 52.004  1.00 7.53  ? 178 ASN D N   1 
ATOM   8003  C  CA  . ASN D  1 178 ? 30.648  -26.448 51.615  1.00 6.96  ? 178 ASN D CA  1 
ATOM   8004  C  C   . ASN D  1 178 ? 30.550  -25.063 50.910  1.00 8.55  ? 178 ASN D C   1 
ATOM   8005  O  O   . ASN D  1 178 ? 30.172  -24.967 49.754  1.00 8.11  ? 178 ASN D O   1 
ATOM   8006  C  CB  . ASN D  1 178 ? 31.310  -27.481 50.752  1.00 8.06  ? 178 ASN D CB  1 
ATOM   8007  C  CG  . ASN D  1 178 ? 32.748  -27.103 50.432  1.00 9.44  ? 178 ASN D CG  1 
ATOM   8008  O  OD1 . ASN D  1 178 ? 33.328  -26.098 50.907  1.00 10.22 ? 178 ASN D OD1 1 
ATOM   8009  N  ND2 . ASN D  1 178 ? 33.374  -27.948 49.593  1.00 13.03 ? 178 ASN D ND2 1 
ATOM   8010  N  N   A ILE D  1 179 ? 30.919  -24.035 51.672  0.50 6.39  ? 179 ILE D N   1 
ATOM   8011  N  N   B ILE D  1 179 ? 30.882  -23.973 51.632  0.50 7.35  ? 179 ILE D N   1 
ATOM   8012  C  CA  A ILE D  1 179 ? 30.877  -22.702 51.155  0.50 6.78  ? 179 ILE D CA  1 
ATOM   8013  C  CA  B ILE D  1 179 ? 30.911  -22.615 51.009  0.50 8.12  ? 179 ILE D CA  1 
ATOM   8014  C  C   A ILE D  1 179 ? 31.774  -22.511 49.936  0.50 6.63  ? 179 ILE D C   1 
ATOM   8015  C  C   B ILE D  1 179 ? 31.817  -22.519 49.809  0.50 8.15  ? 179 ILE D C   1 
ATOM   8016  O  O   A ILE D  1 179 ? 31.467  -21.599 49.129  0.50 7.63  ? 179 ILE D O   1 
ATOM   8017  O  O   B ILE D  1 179 ? 31.631  -21.690 48.920  0.50 8.55  ? 179 ILE D O   1 
ATOM   8018  C  CB  A ILE D  1 179 ? 31.182  -21.723 52.317  0.50 5.54  ? 179 ILE D CB  1 
ATOM   8019  C  CB  B ILE D  1 179 ? 31.357  -21.533 52.023  0.50 8.81  ? 179 ILE D CB  1 
ATOM   8020  C  CG1 A ILE D  1 179 ? 30.222  -21.961 53.480  0.50 4.61  ? 179 ILE D CG1 1 
ATOM   8021  C  CG1 B ILE D  1 179 ? 30.435  -21.568 53.220  0.50 10.02 ? 179 ILE D CG1 1 
ATOM   8022  C  CG2 A ILE D  1 179 ? 30.987  -20.284 51.855  0.50 5.63  ? 179 ILE D CG2 1 
ATOM   8023  C  CG2 B ILE D  1 179 ? 31.337  -20.132 51.381  0.50 8.89  ? 179 ILE D CG2 1 
ATOM   8024  C  CD1 A ILE D  1 179 ? 28.716  -21.776 53.158  0.50 3.16  ? 179 ILE D CD1 1 
ATOM   8025  C  CD1 B ILE D  1 179 ? 30.973  -22.348 54.265  0.50 14.98 ? 179 ILE D CD1 1 
ATOM   8026  N  N   . GLU D  1 180 ? 32.846  -23.349 49.758  1.00 7.63  ? 180 GLU D N   1 
ATOM   8027  C  CA  . GLU D  1 180 ? 33.699  -23.217 48.581  1.00 8.08  ? 180 GLU D CA  1 
ATOM   8028  C  C   . GLU D  1 180 ? 32.948  -23.494 47.300  1.00 7.05  ? 180 GLU D C   1 
ATOM   8029  O  O   . GLU D  1 180 ? 33.389  -23.079 46.228  1.00 9.12  ? 180 GLU D O   1 
ATOM   8030  C  CB  . GLU D  1 180 ? 34.855  -24.172 48.737  1.00 11.83 ? 180 GLU D CB  1 
ATOM   8031  C  CG  . GLU D  1 180 ? 36.035  -23.717 47.940  1.00 17.49 ? 180 GLU D CG  1 
ATOM   8032  C  CD  . GLU D  1 180 ? 37.381  -24.409 48.292  1.00 19.45 ? 180 GLU D CD  1 
ATOM   8033  O  OE1 . GLU D  1 180 ? 37.495  -25.106 49.323  1.00 19.59 ? 180 GLU D OE1 1 
ATOM   8034  O  OE2 . GLU D  1 180 ? 38.310  -24.165 47.445  1.00 22.63 ? 180 GLU D OE2 1 
ATOM   8035  N  N   . GLU D  1 181 ? 31.806  -24.236 47.395  1.00 7.45  ? 181 GLU D N   1 
ATOM   8036  C  CA  . GLU D  1 181 ? 31.029  -24.466 46.153  1.00 9.67  ? 181 GLU D CA  1 
ATOM   8037  C  C   . GLU D  1 181 ? 30.414  -23.167 45.565  1.00 7.71  ? 181 GLU D C   1 
ATOM   8038  O  O   . GLU D  1 181 ? 29.941  -23.196 44.406  1.00 8.96  ? 181 GLU D O   1 
ATOM   8039  C  CB  . GLU D  1 181 ? 29.860  -25.387 46.464  1.00 11.34 ? 181 GLU D CB  1 
ATOM   8040  C  CG  . GLU D  1 181 ? 30.291  -26.740 46.999  1.00 14.42 ? 181 GLU D CG  1 
ATOM   8041  C  CD  . GLU D  1 181 ? 29.092  -27.643 47.503  1.00 14.65 ? 181 GLU D CD  1 
ATOM   8042  O  OE1 . GLU D  1 181 ? 27.894  -27.242 47.480  1.00 14.22 ? 181 GLU D OE1 1 
ATOM   8043  O  OE2 . GLU D  1 181 ? 29.352  -28.766 47.996  1.00 15.36 ? 181 GLU D OE2 1 
ATOM   8044  N  N   . LEU D  1 182 ? 30.397  -22.088 46.368  1.00 7.40  ? 182 LEU D N   1 
ATOM   8045  C  CA  . LEU D  1 182 ? 29.884  -20.798 45.935  1.00 7.37  ? 182 LEU D CA  1 
ATOM   8046  C  C   . LEU D  1 182 ? 30.920  -20.003 45.131  1.00 7.93  ? 182 LEU D C   1 
ATOM   8047  O  O   . LEU D  1 182 ? 30.554  -18.969 44.534  1.00 7.57  ? 182 LEU D O   1 
ATOM   8048  C  CB  . LEU D  1 182 ? 29.423  -19.943 47.132  1.00 7.11  ? 182 LEU D CB  1 
ATOM   8049  C  CG  . LEU D  1 182 ? 28.343  -20.682 47.979  1.00 7.75  ? 182 LEU D CG  1 
ATOM   8050  C  CD1 . LEU D  1 182 ? 27.932  -19.806 49.204  1.00 7.17  ? 182 LEU D CD1 1 
ATOM   8051  C  CD2 . LEU D  1 182 ? 27.074  -21.095 47.226  1.00 9.06  ? 182 LEU D CD2 1 
ATOM   8052  N  N   . LEU D  1 183 ? 32.162  -20.479 45.154  1.00 8.24  ? 183 LEU D N   1 
ATOM   8053  C  CA  . LEU D  1 183 ? 33.277  -19.681 44.489  1.00 8.10  ? 183 LEU D CA  1 
ATOM   8054  C  C   . LEU D  1 183 ? 33.395  -20.062 43.024  1.00 9.17  ? 183 LEU D C   1 
ATOM   8055  O  O   . LEU D  1 183 ? 33.043  -21.173 42.626  1.00 10.06 ? 183 LEU D O   1 
ATOM   8056  C  CB  . LEU D  1 183 ? 34.632  -19.951 45.187  1.00 9.41  ? 183 LEU D CB  1 
ATOM   8057  C  CG  . LEU D  1 183 ? 34.599  -19.615 46.663  1.00 10.29 ? 183 LEU D CG  1 
ATOM   8058  C  CD1 . LEU D  1 183 ? 35.986  -19.978 47.227  1.00 14.29 ? 183 LEU D CD1 1 
ATOM   8059  C  CD2 . LEU D  1 183 ? 34.251  -18.164 46.901  1.00 10.70 ? 183 LEU D CD2 1 
ATOM   8060  N  N   . PRO D  1 184 ? 33.915  -19.201 42.173  1.00 8.51  ? 184 PRO D N   1 
ATOM   8061  C  CA  . PRO D  1 184 ? 34.075  -19.436 40.745  1.00 10.50 ? 184 PRO D CA  1 
ATOM   8062  C  C   . PRO D  1 184 ? 35.343  -20.194 40.428  1.00 11.86 ? 184 PRO D C   1 
ATOM   8063  O  O   . PRO D  1 184 ? 36.121  -20.572 41.332  1.00 13.67 ? 184 PRO D O   1 
ATOM   8064  C  CB  . PRO D  1 184 ? 34.203  -17.992 40.144  1.00 10.90 ? 184 PRO D CB  1 
ATOM   8065  C  CG  . PRO D  1 184 ? 34.945  -17.251 41.309  1.00 8.65  ? 184 PRO D CG  1 
ATOM   8066  C  CD  . PRO D  1 184 ? 34.344  -17.829 42.584  1.00 8.93  ? 184 PRO D CD  1 
ATOM   8067  N  N   . GLU D  1 185 ? 35.462  -20.417 39.079  1.00 13.15 ? 185 GLU D N   1 
ATOM   8068  C  CA  . GLU D  1 185 ? 36.681  -21.059 38.583  1.00 13.23 ? 185 GLU D CA  1 
ATOM   8069  C  C   . GLU D  1 185 ? 37.869  -20.115 38.741  1.00 13.80 ? 185 GLU D C   1 
ATOM   8070  O  O   . GLU D  1 185 ? 37.718  -18.842 38.672  1.00 15.31 ? 185 GLU D O   1 
ATOM   8071  C  CB  . GLU D  1 185 ? 36.516  -21.320 37.111  1.00 14.90 ? 185 GLU D CB  1 
ATOM   8072  C  CG  . GLU D  1 185 ? 35.369  -22.305 36.925  1.00 24.77 ? 185 GLU D CG  1 
ATOM   8073  C  CD  . GLU D  1 185 ? 35.639  -23.675 37.565  1.00 38.97 ? 185 GLU D CD  1 
ATOM   8074  O  OE1 . GLU D  1 185 ? 36.562  -24.375 37.042  1.00 47.64 ? 185 GLU D OE1 1 
ATOM   8075  O  OE2 . GLU D  1 185 ? 34.928  -24.064 38.547  1.00 39.65 ? 185 GLU D OE2 1 
ATOM   8076  N  N   . ARG D  1 186 ? 39.059  -20.717 38.923  1.00 11.61 ? 186 ARG D N   1 
ATOM   8077  C  CA  . ARG D  1 186 ? 40.314  -19.945 38.870  1.00 11.74 ? 186 ARG D CA  1 
ATOM   8078  C  C   . ARG D  1 186 ? 40.276  -18.830 39.919  1.00 11.03 ? 186 ARG D C   1 
ATOM   8079  O  O   . ARG D  1 186 ? 40.600  -17.636 39.563  1.00 11.28 ? 186 ARG D O   1 
ATOM   8080  C  CB  . ARG D  1 186 ? 40.690  -19.474 37.445  1.00 14.50 ? 186 ARG D CB  1 
ATOM   8081  C  CG  . ARG D  1 186 ? 41.025  -20.720 36.530  1.00 14.15 ? 186 ARG D CG  1 
ATOM   8082  C  CD  . ARG D  1 186 ? 41.405  -20.264 35.094  1.00 17.45 ? 186 ARG D CD  1 
ATOM   8083  N  NE  . ARG D  1 186 ? 40.277  -19.679 34.360  1.00 26.73 ? 186 ARG D NE  1 
ATOM   8084  C  CZ  . ARG D  1 186 ? 39.242  -20.392 33.870  1.00 34.14 ? 186 ARG D CZ  1 
ATOM   8085  N  NH1 . ARG D  1 186 ? 38.231  -19.822 33.188  1.00 35.65 ? 186 ARG D NH1 1 
ATOM   8086  N  NH2 . ARG D  1 186 ? 39.175  -21.683 34.109  1.00 33.25 ? 186 ARG D NH2 1 
ATOM   8087  N  N   . THR D  1 187 ? 40.006  -19.228 41.188  1.00 7.77  ? 187 THR D N   1 
ATOM   8088  C  CA  . THR D  1 187 ? 40.036  -18.197 42.221  1.00 8.43  ? 187 THR D CA  1 
ATOM   8089  C  C   . THR D  1 187 ? 41.388  -17.440 42.385  1.00 6.61  ? 187 THR D C   1 
ATOM   8090  O  O   . THR D  1 187 ? 41.464  -16.343 43.002  1.00 8.00  ? 187 THR D O   1 
ATOM   8091  C  CB  . THR D  1 187 ? 39.631  -18.786 43.591  1.00 8.86  ? 187 THR D CB  1 
ATOM   8092  O  OG1 . THR D  1 187 ? 40.473  -19.896 43.977  1.00 10.32 ? 187 THR D OG1 1 
ATOM   8093  C  CG2 . THR D  1 187 ? 38.113  -19.136 43.615  1.00 10.40 ? 187 THR D CG2 1 
ATOM   8094  N  N   . ALA D  1 188 ? 42.501  -18.038 41.854  1.00 8.96  ? 188 ALA D N   1 
ATOM   8095  C  CA  . ALA D  1 188 ? 43.773  -17.339 41.880  1.00 9.10  ? 188 ALA D CA  1 
ATOM   8096  C  C   . ALA D  1 188 ? 43.753  -16.022 41.110  1.00 8.12  ? 188 ALA D C   1 
ATOM   8097  O  O   . ALA D  1 188 ? 44.654  -15.216 41.323  1.00 9.05  ? 188 ALA D O   1 
ATOM   8098  C  CB  . ALA D  1 188 ? 44.859  -18.279 41.277  1.00 8.59  ? 188 ALA D CB  1 
ATOM   8099  N  N   . GLU D  1 189 ? 42.815  -15.855 40.192  1.00 8.29  ? 189 GLU D N   1 
ATOM   8100  C  CA  . GLU D  1 189 ? 42.742  -14.645 39.326  1.00 7.29  ? 189 GLU D CA  1 
ATOM   8101  C  C   . GLU D  1 189 ? 41.713  -13.702 40.020  1.00 5.06  ? 189 GLU D C   1 
ATOM   8102  O  O   . GLU D  1 189 ? 40.538  -14.030 40.046  1.00 8.27  ? 189 GLU D O   1 
ATOM   8103  C  CB  . GLU D  1 189 ? 42.338  -14.975 37.876  1.00 8.41  ? 189 GLU D CB  1 
ATOM   8104  C  CG  . GLU D  1 189 ? 43.402  -15.945 37.313  1.00 11.04 ? 189 GLU D CG  1 
ATOM   8105  C  CD  . GLU D  1 189 ? 43.036  -16.331 35.895  1.00 14.15 ? 189 GLU D CD  1 
ATOM   8106  O  OE1 . GLU D  1 189 ? 42.325  -15.614 35.179  1.00 15.07 ? 189 GLU D OE1 1 
ATOM   8107  O  OE2 . GLU D  1 189 ? 43.467  -17.493 35.496  1.00 17.26 ? 189 GLU D OE2 1 
ATOM   8108  N  N   . TYR D  1 190 ? 42.144  -12.507 40.448  1.00 6.80  ? 190 TYR D N   1 
ATOM   8109  C  CA  . TYR D  1 190 ? 41.230  -11.601 41.164  1.00 6.50  ? 190 TYR D CA  1 
ATOM   8110  C  C   . TYR D  1 190 ? 41.745  -10.138 41.028  1.00 7.01  ? 190 TYR D C   1 
ATOM   8111  O  O   . TYR D  1 190 ? 42.928  -9.872  40.642  1.00 7.08  ? 190 TYR D O   1 
ATOM   8112  C  CB  . TYR D  1 190 ? 41.106  -12.028 42.613  1.00 6.71  ? 190 TYR D CB  1 
ATOM   8113  C  CG  . TYR D  1 190 ? 42.389  -12.124 43.374  1.00 6.62  ? 190 TYR D CG  1 
ATOM   8114  C  CD1 . TYR D  1 190 ? 43.058  -10.998 43.848  1.00 6.42  ? 190 TYR D CD1 1 
ATOM   8115  C  CD2 . TYR D  1 190 ? 42.961  -13.402 43.582  1.00 9.13  ? 190 TYR D CD2 1 
ATOM   8116  C  CE1 . TYR D  1 190 ? 44.259  -11.108 44.547  1.00 6.35  ? 190 TYR D CE1 1 
ATOM   8117  C  CE2 . TYR D  1 190 ? 44.207  -13.513 44.324  1.00 7.41  ? 190 TYR D CE2 1 
ATOM   8118  C  CZ  . TYR D  1 190 ? 44.819  -12.370 44.779  1.00 5.79  ? 190 TYR D CZ  1 
ATOM   8119  O  OH  . TYR D  1 190 ? 46.032  -12.324 45.554  1.00 6.80  ? 190 TYR D OH  1 
ATOM   8120  N  N   . TYR D  1 191 ? 40.833  -9.216  41.396  1.00 6.23  ? 191 TYR D N   1 
ATOM   8121  C  CA  . TYR D  1 191 ? 41.167  -7.819  41.613  1.00 6.11  ? 191 TYR D CA  1 
ATOM   8122  C  C   . TYR D  1 191 ? 41.262  -7.557  43.110  1.00 6.62  ? 191 TYR D C   1 
ATOM   8123  O  O   . TYR D  1 191 ? 40.426  -8.104  43.901  1.00 7.20  ? 191 TYR D O   1 
ATOM   8124  C  CB  . TYR D  1 191 ? 40.019  -6.942  41.054  1.00 7.93  ? 191 TYR D CB  1 
ATOM   8125  C  CG  . TYR D  1 191 ? 39.543  -7.224  39.631  1.00 6.14  ? 191 TYR D CG  1 
ATOM   8126  C  CD1 . TYR D  1 191 ? 38.556  -8.169  39.366  1.00 6.31  ? 191 TYR D CD1 1 
ATOM   8127  C  CD2 . TYR D  1 191 ? 40.109  -6.466  38.583  1.00 6.76  ? 191 TYR D CD2 1 
ATOM   8128  C  CE1 . TYR D  1 191 ? 38.117  -8.383  38.045  1.00 7.04  ? 191 TYR D CE1 1 
ATOM   8129  C  CE2 . TYR D  1 191 ? 39.651  -6.709  37.212  1.00 7.77  ? 191 TYR D CE2 1 
ATOM   8130  C  CZ  . TYR D  1 191 ? 38.686  -7.652  37.019  1.00 6.79  ? 191 TYR D CZ  1 
ATOM   8131  O  OH  . TYR D  1 191 ? 38.197  -7.893  35.737  1.00 10.49 ? 191 TYR D OH  1 
ATOM   8132  N  N   . ARG D  1 192 ? 42.228  -6.746  43.557  1.00 6.19  ? 192 ARG D N   1 
ATOM   8133  C  CA  . ARG D  1 192 ? 42.386  -6.450  44.970  1.00 7.23  ? 192 ARG D CA  1 
ATOM   8134  C  C   . ARG D  1 192 ? 42.496  -4.947  45.181  1.00 6.98  ? 192 ARG D C   1 
ATOM   8135  O  O   . ARG D  1 192 ? 43.287  -4.276  44.471  1.00 6.10  ? 192 ARG D O   1 
ATOM   8136  C  CB  . ARG D  1 192 ? 43.691  -7.130  45.376  1.00 9.31  ? 192 ARG D CB  1 
ATOM   8137  C  CG  . ARG D  1 192 ? 44.264  -6.792  46.679  1.00 14.83 ? 192 ARG D CG  1 
ATOM   8138  C  CD  . ARG D  1 192 ? 43.655  -7.488  47.836  1.00 13.89 ? 192 ARG D CD  1 
ATOM   8139  N  NE  . ARG D  1 192 ? 43.369  -8.897  47.569  1.00 12.45 ? 192 ARG D NE  1 
ATOM   8140  C  CZ  . ARG D  1 192 ? 44.173  -9.907  47.893  1.00 11.84 ? 192 ARG D CZ  1 
ATOM   8141  N  NH1 . ARG D  1 192 ? 43.813  -11.151 47.610  1.00 13.63 ? 192 ARG D NH1 1 
ATOM   8142  N  NH2 . ARG D  1 192 ? 45.335  -9.678  48.495  1.00 18.13 ? 192 ARG D NH2 1 
ATOM   8143  N  N   . TYR D  1 193 ? 41.747  -4.415  46.146  1.00 6.00  ? 193 TYR D N   1 
ATOM   8144  C  CA  . TYR D  1 193 ? 41.982  -2.970  46.486  1.00 5.72  ? 193 TYR D CA  1 
ATOM   8145  C  C   . TYR D  1 193 ? 41.525  -2.679  47.924  1.00 5.32  ? 193 TYR D C   1 
ATOM   8146  O  O   . TYR D  1 193 ? 40.721  -3.510  48.451  1.00 6.17  ? 193 TYR D O   1 
ATOM   8147  C  CB  . TYR D  1 193 ? 41.317  -2.057  45.481  1.00 6.95  ? 193 TYR D CB  1 
ATOM   8148  C  CG  . TYR D  1 193 ? 39.744  -2.005  45.579  1.00 5.00  ? 193 TYR D CG  1 
ATOM   8149  C  CD1 . TYR D  1 193 ? 39.172  -0.932  46.217  1.00 5.62  ? 193 TYR D CD1 1 
ATOM   8150  C  CD2 . TYR D  1 193 ? 38.959  -3.056  45.152  1.00 5.43  ? 193 TYR D CD2 1 
ATOM   8151  C  CE1 . TYR D  1 193 ? 37.757  -0.842  46.425  1.00 5.03  ? 193 TYR D CE1 1 
ATOM   8152  C  CE2 . TYR D  1 193 ? 37.561  -2.960  45.209  1.00 5.17  ? 193 TYR D CE2 1 
ATOM   8153  C  CZ  . TYR D  1 193 ? 36.971  -1.898  45.953  1.00 4.60  ? 193 TYR D CZ  1 
ATOM   8154  O  OH  . TYR D  1 193 ? 35.606  -1.793  46.110  1.00 4.91  ? 193 TYR D OH  1 
ATOM   8155  N  N   . ARG D  1 194 ? 41.950  -1.578  48.513  1.00 5.34  ? 194 ARG D N   1 
ATOM   8156  C  CA  . ARG D  1 194 ? 41.525  -1.187  49.821  1.00 6.01  ? 194 ARG D CA  1 
ATOM   8157  C  C   . ARG D  1 194 ? 40.280  -0.291  49.594  1.00 6.20  ? 194 ARG D C   1 
ATOM   8158  O  O   . ARG D  1 194 ? 40.299  0.728   48.822  1.00 6.60  ? 194 ARG D O   1 
ATOM   8159  C  CB  . ARG D  1 194 ? 42.644  -0.330  50.399  1.00 8.05  ? 194 ARG D CB  1 
ATOM   8160  C  CG  . ARG D  1 194 ? 43.646  -1.299  50.984  1.00 12.82 ? 194 ARG D CG  1 
ATOM   8161  C  CD  . ARG D  1 194 ? 43.450  -1.079  52.556  1.00 28.61 ? 194 ARG D CD  1 
ATOM   8162  N  NE  . ARG D  1 194 ? 43.593  -2.377  53.247  1.00 32.96 ? 194 ARG D NE  1 
ATOM   8163  C  CZ  . ARG D  1 194 ? 42.794  -2.859  54.204  1.00 24.57 ? 194 ARG D CZ  1 
ATOM   8164  N  NH1 . ARG D  1 194 ? 43.040  -4.055  54.735  1.00 24.98 ? 194 ARG D NH1 1 
ATOM   8165  N  NH2 . ARG D  1 194 ? 41.758  -2.159  54.645  1.00 14.97 ? 194 ARG D NH2 1 
ATOM   8166  N  N   . GLY D  1 195 ? 39.197  -0.647  50.308  1.00 4.98  ? 195 GLY D N   1 
ATOM   8167  C  CA  . GLY D  1 195 ? 37.979  0.135   50.205  1.00 5.23  ? 195 GLY D CA  1 
ATOM   8168  C  C   . GLY D  1 195 ? 37.173  0.048   51.480  1.00 4.00  ? 195 GLY D C   1 
ATOM   8169  O  O   . GLY D  1 195 ? 37.748  0.029   52.577  1.00 5.69  ? 195 GLY D O   1 
ATOM   8170  N  N   . SER D  1 196 ? 35.836  0.003   51.364  1.00 4.82  ? 196 SER D N   1 
ATOM   8171  C  CA  . SER D  1 196 ? 34.927  0.294   52.485  1.00 5.61  ? 196 SER D CA  1 
ATOM   8172  C  C   . SER D  1 196 ? 33.796  -0.729  52.576  1.00 5.02  ? 196 SER D C   1 
ATOM   8173  O  O   . SER D  1 196 ? 33.527  -1.448  51.576  1.00 4.92  ? 196 SER D O   1 
ATOM   8174  C  CB  . SER D  1 196 ? 34.308  1.659   52.465  1.00 4.89  ? 196 SER D CB  1 
ATOM   8175  O  OG  . SER D  1 196 ? 33.256  1.711   51.474  1.00 4.87  ? 196 SER D OG  1 
ATOM   8176  N  N   . LEU D  1 197 ? 33.115  -0.758  53.690  1.00 4.41  ? 197 LEU D N   1 
ATOM   8177  C  CA  . LEU D  1 197 ? 31.759  -1.383  53.673  1.00 4.53  ? 197 LEU D CA  1 
ATOM   8178  C  C   . LEU D  1 197 ? 30.894  -0.637  52.636  1.00 3.91  ? 197 LEU D C   1 
ATOM   8179  O  O   . LEU D  1 197 ? 30.972  0.628   52.545  1.00 5.08  ? 197 LEU D O   1 
ATOM   8180  C  CB  . LEU D  1 197 ? 31.179  -1.205  55.072  1.00 6.04  ? 197 LEU D CB  1 
ATOM   8181  C  CG  . LEU D  1 197 ? 31.885  -2.035  56.167  1.00 5.79  ? 197 LEU D CG  1 
ATOM   8182  C  CD1 . LEU D  1 197 ? 31.210  -1.729  57.494  1.00 7.63  ? 197 LEU D CD1 1 
ATOM   8183  C  CD2 . LEU D  1 197 ? 31.921  -3.560  55.909  1.00 9.14  ? 197 LEU D CD2 1 
ATOM   8184  N  N   . THR D  1 198 ? 30.039  -1.326  51.888  1.00 4.90  ? 198 THR D N   1 
ATOM   8185  C  CA  . THR D  1 198 ? 29.211  -0.677  50.837  1.00 4.71  ? 198 THR D CA  1 
ATOM   8186  C  C   . THR D  1 198 ? 27.817  -0.284  51.335  1.00 5.52  ? 198 THR D C   1 
ATOM   8187  O  O   . THR D  1 198 ? 26.993  0.126   50.526  1.00 4.85  ? 198 THR D O   1 
ATOM   8188  C  CB  . THR D  1 198 ? 29.016  -1.627  49.650  1.00 3.94  ? 198 THR D CB  1 
ATOM   8189  O  OG1 . THR D  1 198 ? 28.300  -2.806  50.113  1.00 4.39  ? 198 THR D OG1 1 
ATOM   8190  C  CG2 . THR D  1 198 ? 30.378  -2.096  49.035  1.00 4.89  ? 198 THR D CG2 1 
ATOM   8191  N  N   . THR D  1 199 ? 27.598  -0.468  52.667  1.00 4.82  ? 199 THR D N   1 
ATOM   8192  C  CA  . THR D  1 199 ? 26.390  0.043   53.264  1.00 5.22  ? 199 THR D CA  1 
ATOM   8193  C  C   . THR D  1 199 ? 26.782  0.838   54.543  1.00 5.47  ? 199 THR D C   1 
ATOM   8194  O  O   . THR D  1 199 ? 27.873  0.632   55.049  1.00 5.46  ? 199 THR D O   1 
ATOM   8195  C  CB  . THR D  1 199 ? 25.337  -1.030  53.732  1.00 5.72  ? 199 THR D CB  1 
ATOM   8196  O  OG1 . THR D  1 199 ? 25.762  -1.626  54.931  1.00 7.35  ? 199 THR D OG1 1 
ATOM   8197  C  CG2 . THR D  1 199 ? 25.162  -2.148  52.656  1.00 7.04  ? 199 THR D CG2 1 
ATOM   8198  N  N   . PRO D  1 200 ? 25.892  1.662   55.086  1.00 6.02  ? 200 PRO D N   1 
ATOM   8199  C  CA  . PRO D  1 200 ? 26.153  2.302   56.453  1.00 6.14  ? 200 PRO D CA  1 
ATOM   8200  C  C   . PRO D  1 200 ? 26.635  1.174   57.365  1.00 6.06  ? 200 PRO D C   1 
ATOM   8201  O  O   . PRO D  1 200 ? 26.029  0.079   57.381  1.00 5.79  ? 200 PRO D O   1 
ATOM   8202  C  CB  . PRO D  1 200 ? 24.781  2.824   56.815  1.00 6.13  ? 200 PRO D CB  1 
ATOM   8203  C  CG  . PRO D  1 200 ? 24.187  3.271   55.439  1.00 6.13  ? 200 PRO D CG  1 
ATOM   8204  C  CD  . PRO D  1 200 ? 24.521  2.018   54.602  1.00 6.83  ? 200 PRO D CD  1 
ATOM   8205  N  N   . PRO D  1 201 ? 27.631  1.424   58.201  1.00 5.73  ? 201 PRO D N   1 
ATOM   8206  C  CA  . PRO D  1 201 ? 28.282  2.735   58.403  1.00 5.53  ? 201 PRO D CA  1 
ATOM   8207  C  C   . PRO D  1 201 ? 29.406  3.093   57.403  1.00 5.37  ? 201 PRO D C   1 
ATOM   8208  O  O   . PRO D  1 201 ? 30.071  4.175   57.598  1.00 6.67  ? 201 PRO D O   1 
ATOM   8209  C  CB  . PRO D  1 201 ? 28.848  2.600   59.860  1.00 5.85  ? 201 PRO D CB  1 
ATOM   8210  C  CG  . PRO D  1 201 ? 29.234  1.100   59.958  1.00 6.57  ? 201 PRO D CG  1 
ATOM   8211  C  CD  . PRO D  1 201 ? 28.040  0.407   59.219  1.00 6.84  ? 201 PRO D CD  1 
ATOM   8212  N  N   . CYS D  1 202 ? 29.655  2.265   56.386  1.00 4.40  ? 202 CYS D N   1 
ATOM   8213  C  CA  . CYS D  1 202 ? 30.606  2.634   55.321  1.00 4.48  ? 202 CYS D CA  1 
ATOM   8214  C  C   . CYS D  1 202 ? 32.081  2.753   55.733  1.00 4.48  ? 202 CYS D C   1 
ATOM   8215  O  O   . CYS D  1 202 ? 32.884  3.447   55.125  1.00 4.98  ? 202 CYS D O   1 
ATOM   8216  C  CB  . CYS D  1 202 ? 30.230  3.916   54.572  1.00 6.24  ? 202 CYS D CB  1 
ATOM   8217  S  SG  . CYS D  1 202 ? 28.541  3.907   53.821  1.00 5.98  ? 202 CYS D SG  1 
ATOM   8218  N  N   . ASN D  1 203 ? 32.377  2.014   56.798  1.00 5.75  ? 203 ASN D N   1 
ATOM   8219  C  CA  . ASN D  1 203 ? 33.756  2.218   57.385  1.00 4.29  ? 203 ASN D CA  1 
ATOM   8220  C  C   . ASN D  1 203 ? 34.818  1.886   56.347  1.00 5.58  ? 203 ASN D C   1 
ATOM   8221  O  O   . ASN D  1 203 ? 34.679  0.838   55.640  1.00 5.62  ? 203 ASN D O   1 
ATOM   8222  C  CB  . ASN D  1 203 ? 34.006  1.238   58.542  1.00 6.33  ? 203 ASN D CB  1 
ATOM   8223  C  CG  . ASN D  1 203 ? 32.993  1.399   59.700  1.00 7.96  ? 203 ASN D CG  1 
ATOM   8224  O  OD1 . ASN D  1 203 ? 32.480  2.485   59.896  1.00 10.23 ? 203 ASN D OD1 1 
ATOM   8225  N  ND2 . ASN D  1 203 ? 32.739  0.319   60.466  1.00 9.48  ? 203 ASN D ND2 1 
ATOM   8226  N  N   . PRO D  1 204 ? 35.891  2.606   56.234  1.00 5.53  ? 204 PRO D N   1 
ATOM   8227  C  CA  . PRO D  1 204 ? 36.907  2.382   55.196  1.00 5.58  ? 204 PRO D CA  1 
ATOM   8228  C  C   . PRO D  1 204 ? 37.984  1.383   55.600  1.00 7.11  ? 204 PRO D C   1 
ATOM   8229  O  O   . PRO D  1 204 ? 39.179  1.651   55.626  1.00 7.79  ? 204 PRO D O   1 
ATOM   8230  C  CB  . PRO D  1 204 ? 37.543  3.798   54.995  1.00 6.20  ? 204 PRO D CB  1 
ATOM   8231  C  CG  . PRO D  1 204 ? 37.420  4.388   56.457  1.00 6.70  ? 204 PRO D CG  1 
ATOM   8232  C  CD  . PRO D  1 204 ? 36.030  3.931   56.888  1.00 6.15  ? 204 PRO D CD  1 
ATOM   8233  N  N   . THR D  1 205 ? 37.529  0.175   55.966  1.00 6.01  ? 205 THR D N   1 
ATOM   8234  C  CA  . THR D  1 205 ? 38.358  -0.786  56.676  1.00 5.31  ? 205 THR D CA  1 
ATOM   8235  C  C   . THR D  1 205 ? 38.356  -2.137  55.972  1.00 6.26  ? 205 THR D C   1 
ATOM   8236  O  O   . THR D  1 205 ? 38.864  -3.123  56.494  1.00 7.93  ? 205 THR D O   1 
ATOM   8237  C  CB  . THR D  1 205 ? 37.810  -1.002  58.052  1.00 6.77  ? 205 THR D CB  1 
ATOM   8238  O  OG1 . THR D  1 205 ? 36.436  -1.388  57.957  1.00 6.87  ? 205 THR D OG1 1 
ATOM   8239  C  CG2 . THR D  1 205 ? 37.863  0.275   58.917  1.00 7.40  ? 205 THR D CG2 1 
ATOM   8240  N  N   . VAL D  1 206 ? 37.940  -2.195  54.692  1.00 5.48  ? 206 VAL D N   1 
ATOM   8241  C  CA  . VAL D  1 206 ? 37.833  -3.500  53.958  1.00 5.36  ? 206 VAL D CA  1 
ATOM   8242  C  C   . VAL D  1 206 ? 38.918  -3.676  52.962  1.00 5.26  ? 206 VAL D C   1 
ATOM   8243  O  O   . VAL D  1 206 ? 39.054  -2.870  52.016  1.00 7.43  ? 206 VAL D O   1 
ATOM   8244  C  CB  . VAL D  1 206 ? 36.413  -3.598  53.278  1.00 4.23  ? 206 VAL D CB  1 
ATOM   8245  C  CG1 . VAL D  1 206 ? 36.308  -4.967  52.492  1.00 6.61  ? 206 VAL D CG1 1 
ATOM   8246  C  CG2 . VAL D  1 206 ? 35.284  -3.387  54.257  1.00 5.81  ? 206 VAL D CG2 1 
ATOM   8247  N  N   . LEU D  1 207 ? 39.654  -4.789  53.054  1.00 5.04  ? 207 LEU D N   1 
ATOM   8248  C  CA  . LEU D  1 207 ? 40.497  -5.242  51.892  1.00 5.67  ? 207 LEU D CA  1 
ATOM   8249  C  C   . LEU D  1 207 ? 39.541  -6.112  50.974  1.00 5.06  ? 207 LEU D C   1 
ATOM   8250  O  O   . LEU D  1 207 ? 39.041  -7.215  51.393  1.00 5.29  ? 207 LEU D O   1 
ATOM   8251  C  CB  . LEU D  1 207 ? 41.611  -6.119  52.475  1.00 7.28  ? 207 LEU D CB  1 
ATOM   8252  C  CG  . LEU D  1 207 ? 42.650  -6.556  51.427  1.00 10.11 ? 207 LEU D CG  1 
ATOM   8253  C  CD1 . LEU D  1 207 ? 43.240  -5.329  50.723  1.00 11.71 ? 207 LEU D CD1 1 
ATOM   8254  C  CD2 . LEU D  1 207 ? 43.764  -7.108  52.199  1.00 16.48 ? 207 LEU D CD2 1 
ATOM   8255  N  N   . TRP D  1 208 ? 39.265  -5.609  49.764  1.00 4.65  ? 208 TRP D N   1 
ATOM   8256  C  CA  . TRP D  1 208 ? 38.411  -6.309  48.812  1.00 4.89  ? 208 TRP D CA  1 
ATOM   8257  C  C   . TRP D  1 208 ? 39.168  -7.254  47.933  1.00 5.38  ? 208 TRP D C   1 
ATOM   8258  O  O   . TRP D  1 208 ? 40.209  -6.831  47.371  1.00 5.53  ? 208 TRP D O   1 
ATOM   8259  C  CB  . TRP D  1 208 ? 37.674  -5.243  47.916  1.00 4.08  ? 208 TRP D CB  1 
ATOM   8260  C  CG  . TRP D  1 208 ? 36.540  -4.619  48.588  1.00 3.62  ? 208 TRP D CG  1 
ATOM   8261  C  CD1 . TRP D  1 208 ? 36.550  -3.431  49.301  1.00 5.08  ? 208 TRP D CD1 1 
ATOM   8262  C  CD2 . TRP D  1 208 ? 35.194  -5.181  48.744  1.00 5.25  ? 208 TRP D CD2 1 
ATOM   8263  N  NE1 . TRP D  1 208 ? 35.306  -3.202  49.919  1.00 4.56  ? 208 TRP D NE1 1 
ATOM   8264  C  CE2 . TRP D  1 208 ? 34.452  -4.286  49.566  1.00 3.62  ? 208 TRP D CE2 1 
ATOM   8265  C  CE3 . TRP D  1 208 ? 34.573  -6.361  48.293  1.00 5.34  ? 208 TRP D CE3 1 
ATOM   8266  C  CZ2 . TRP D  1 208 ? 33.097  -4.536  49.909  1.00 6.58  ? 208 TRP D CZ2 1 
ATOM   8267  C  CZ3 . TRP D  1 208 ? 33.238  -6.580  48.655  1.00 4.83  ? 208 TRP D CZ3 1 
ATOM   8268  C  CH2 . TRP D  1 208 ? 32.563  -5.701  49.481  1.00 5.37  ? 208 TRP D CH2 1 
ATOM   8269  N  N   . THR D  1 209 ? 38.583  -8.405  47.668  1.00 4.70  ? 209 THR D N   1 
ATOM   8270  C  CA  . THR D  1 209 ? 39.088  -9.329  46.636  1.00 5.20  ? 209 THR D CA  1 
ATOM   8271  C  C   . THR D  1 209 ? 37.887  -9.663  45.781  1.00 4.71  ? 209 THR D C   1 
ATOM   8272  O  O   . THR D  1 209 ? 36.941  -10.265 46.342  1.00 4.99  ? 209 THR D O   1 
ATOM   8273  C  CB  . THR D  1 209 ? 39.654  -10.606 47.280  1.00 6.76  ? 209 THR D CB  1 
ATOM   8274  O  OG1 . THR D  1 209 ? 40.766  -10.306 48.144  1.00 6.70  ? 209 THR D OG1 1 
ATOM   8275  C  CG2 . THR D  1 209 ? 40.075  -11.619 46.197  1.00 7.23  ? 209 THR D CG2 1 
ATOM   8276  N  N   . VAL D  1 210 ? 37.884  -9.223  44.517  1.00 4.86  ? 210 VAL D N   1 
ATOM   8277  C  CA  . VAL D  1 210 ? 36.797  -9.528  43.616  1.00 5.22  ? 210 VAL D CA  1 
ATOM   8278  C  C   . VAL D  1 210 ? 37.291  -10.587 42.590  1.00 5.18  ? 210 VAL D C   1 
ATOM   8279  O  O   . VAL D  1 210 ? 38.274  -10.294 41.912  1.00 5.80  ? 210 VAL D O   1 
ATOM   8280  C  CB  . VAL D  1 210 ? 36.312  -8.252  42.895  1.00 4.57  ? 210 VAL D CB  1 
ATOM   8281  C  CG1 . VAL D  1 210 ? 35.099  -8.628  41.948  1.00 5.16  ? 210 VAL D CG1 1 
ATOM   8282  C  CG2 . VAL D  1 210 ? 35.981  -7.080  43.946  1.00 4.55  ? 210 VAL D CG2 1 
ATOM   8283  N  N   . PHE D  1 211 ? 36.705  -11.763 42.603  1.00 5.08  ? 211 PHE D N   1 
ATOM   8284  C  CA  . PHE D  1 211 ? 37.213  -12.774 41.688  1.00 5.49  ? 211 PHE D CA  1 
ATOM   8285  C  C   . PHE D  1 211 ? 37.000  -12.360 40.231  1.00 5.85  ? 211 PHE D C   1 
ATOM   8286  O  O   . PHE D  1 211 ? 35.963  -11.771 39.922  1.00 6.39  ? 211 PHE D O   1 
ATOM   8287  C  CB  . PHE D  1 211 ? 36.615  -14.177 42.007  1.00 4.68  ? 211 PHE D CB  1 
ATOM   8288  C  CG  . PHE D  1 211 ? 37.036  -14.640 43.350  1.00 5.65  ? 211 PHE D CG  1 
ATOM   8289  C  CD1 . PHE D  1 211 ? 36.110  -14.700 44.428  1.00 6.94  ? 211 PHE D CD1 1 
ATOM   8290  C  CD2 . PHE D  1 211 ? 38.384  -14.981 43.603  1.00 5.65  ? 211 PHE D CD2 1 
ATOM   8291  C  CE1 . PHE D  1 211 ? 36.570  -15.134 45.673  1.00 6.62  ? 211 PHE D CE1 1 
ATOM   8292  C  CE2 . PHE D  1 211 ? 38.801  -15.374 44.864  1.00 6.59  ? 211 PHE D CE2 1 
ATOM   8293  C  CZ  . PHE D  1 211 ? 37.912  -15.515 45.866  1.00 6.54  ? 211 PHE D CZ  1 
ATOM   8294  N  N   . ARG D  1 212 ? 37.967  -12.728 39.368  1.00 6.45  ? 212 ARG D N   1 
ATOM   8295  C  CA  . ARG D  1 212 ? 37.861  -12.337 37.956  1.00 8.42  ? 212 ARG D CA  1 
ATOM   8296  C  C   . ARG D  1 212 ? 36.670  -13.010 37.252  1.00 7.62  ? 212 ARG D C   1 
ATOM   8297  O  O   . ARG D  1 212 ? 35.998  -12.380 36.435  1.00 8.46  ? 212 ARG D O   1 
ATOM   8298  C  CB  . ARG D  1 212 ? 39.142  -12.744 37.250  1.00 6.81  ? 212 ARG D CB  1 
ATOM   8299  C  CG  . ARG D  1 212 ? 39.165  -12.306 35.757  1.00 7.84  ? 212 ARG D CG  1 
ATOM   8300  C  CD  . ARG D  1 212 ? 40.403  -12.953 35.087  1.00 9.55  ? 212 ARG D CD  1 
ATOM   8301  N  NE  . ARG D  1 212 ? 40.549  -12.288 33.797  1.00 11.96 ? 212 ARG D NE  1 
ATOM   8302  C  CZ  . ARG D  1 212 ? 41.620  -12.514 33.009  1.00 11.62 ? 212 ARG D CZ  1 
ATOM   8303  N  NH1 . ARG D  1 212 ? 42.514  -13.455 33.368  1.00 12.13 ? 212 ARG D NH1 1 
ATOM   8304  N  NH2 . ARG D  1 212 ? 41.728  -11.813 31.828  1.00 13.06 ? 212 ARG D NH2 1 
ATOM   8305  N  N   . ASN D  1 213 ? 36.399  -14.279 37.583  1.00 7.24  ? 213 ASN D N   1 
ATOM   8306  C  CA  . ASN D  1 213 ? 35.332  -15.024 36.898  1.00 7.98  ? 213 ASN D CA  1 
ATOM   8307  C  C   . ASN D  1 213 ? 34.056  -15.053 37.695  1.00 8.85  ? 213 ASN D C   1 
ATOM   8308  O  O   . ASN D  1 213 ? 34.073  -15.294 38.892  1.00 7.99  ? 213 ASN D O   1 
ATOM   8309  C  CB  . ASN D  1 213 ? 35.924  -16.456 36.667  1.00 9.25  ? 213 ASN D CB  1 
ATOM   8310  C  CG  . ASN D  1 213 ? 37.163  -16.414 35.751  1.00 13.26 ? 213 ASN D CG  1 
ATOM   8311  O  OD1 . ASN D  1 213 ? 37.128  -15.758 34.682  1.00 18.78 ? 213 ASN D OD1 1 
ATOM   8312  N  ND2 . ASN D  1 213 ? 38.159  -17.122 36.099  1.00 17.80 ? 213 ASN D ND2 1 
ATOM   8313  N  N   . PRO D  1 214 ? 32.912  -14.920 36.986  1.00 8.78  ? 214 PRO D N   1 
ATOM   8314  C  CA  . PRO D  1 214 ? 31.630  -15.025 37.621  1.00 8.36  ? 214 PRO D CA  1 
ATOM   8315  C  C   . PRO D  1 214 ? 31.197  -16.511 37.781  1.00 8.38  ? 214 PRO D C   1 
ATOM   8316  O  O   . PRO D  1 214 ? 31.809  -17.429 37.175  1.00 10.88 ? 214 PRO D O   1 
ATOM   8317  C  CB  . PRO D  1 214 ? 30.644  -14.300 36.571  1.00 8.95  ? 214 PRO D CB  1 
ATOM   8318  C  CG  . PRO D  1 214 ? 31.268  -14.603 35.275  1.00 10.17 ? 214 PRO D CG  1 
ATOM   8319  C  CD  . PRO D  1 214 ? 32.801  -14.657 35.513  1.00 10.48 ? 214 PRO D CD  1 
ATOM   8320  N  N   . VAL D  1 215 ? 30.197  -16.719 38.612  1.00 7.09  ? 215 VAL D N   1 
ATOM   8321  C  CA  . VAL D  1 215 ? 29.408  -17.964 38.642  1.00 7.53  ? 215 VAL D CA  1 
ATOM   8322  C  C   . VAL D  1 215 ? 28.079  -17.726 37.924  1.00 8.59  ? 215 VAL D C   1 
ATOM   8323  O  O   . VAL D  1 215 ? 27.692  -16.598 37.656  1.00 8.57  ? 215 VAL D O   1 
ATOM   8324  C  CB  . VAL D  1 215 ? 29.179  -18.473 40.083  1.00 8.25  ? 215 VAL D CB  1 
ATOM   8325  C  CG1 . VAL D  1 215 ? 30.512  -18.787 40.732  1.00 9.41  ? 215 VAL D CG1 1 
ATOM   8326  C  CG2 . VAL D  1 215 ? 28.330  -17.449 40.863  1.00 6.98  ? 215 VAL D CG2 1 
ATOM   8327  N  N   . GLN D  1 216 ? 27.417  -18.836 37.601  1.00 8.47  ? 216 GLN D N   1 
ATOM   8328  C  CA  . GLN D  1 216 ? 26.078  -18.734 37.025  1.00 8.58  ? 216 GLN D CA  1 
ATOM   8329  C  C   . GLN D  1 216 ? 25.012  -19.278 37.935  1.00 7.00  ? 216 GLN D C   1 
ATOM   8330  O  O   . GLN D  1 216 ? 25.215  -20.290 38.645  1.00 9.04  ? 216 GLN D O   1 
ATOM   8331  C  CB  . GLN D  1 216 ? 26.027  -19.561 35.699  1.00 11.20 ? 216 GLN D CB  1 
ATOM   8332  C  CG  . GLN D  1 216 ? 26.908  -19.061 34.646  1.00 11.73 ? 216 GLN D CG  1 
ATOM   8333  C  CD  . GLN D  1 216 ? 26.887  -20.089 33.406  1.00 15.06 ? 216 GLN D CD  1 
ATOM   8334  O  OE1 . GLN D  1 216 ? 25.872  -20.775 33.142  1.00 19.45 ? 216 GLN D OE1 1 
ATOM   8335  N  NE2 . GLN D  1 216 ? 28.039  -20.235 32.704  1.00 26.44 ? 216 GLN D NE2 1 
ATOM   8336  N  N   . ILE D  1 217 ? 23.821  -18.618 37.940  1.00 7.56  ? 217 ILE D N   1 
ATOM   8337  C  CA  . ILE D  1 217 ? 22.546  -19.165 38.495  1.00 7.97  ? 217 ILE D CA  1 
ATOM   8338  C  C   . ILE D  1 217 ? 21.446  -19.087 37.433  1.00 8.05  ? 217 ILE D C   1 
ATOM   8339  O  O   . ILE D  1 217 ? 21.642  -18.314 36.471  1.00 8.26  ? 217 ILE D O   1 
ATOM   8340  C  CB  . ILE D  1 217 ? 22.143  -18.423 39.830  1.00 7.29  ? 217 ILE D CB  1 
ATOM   8341  C  CG1 . ILE D  1 217 ? 21.787  -16.993 39.518  1.00 8.23  ? 217 ILE D CG1 1 
ATOM   8342  C  CG2 . ILE D  1 217 ? 23.264  -18.549 40.828  1.00 8.18  ? 217 ILE D CG2 1 
ATOM   8343  C  CD1 . ILE D  1 217 ? 21.272  -16.186 40.832  1.00 9.85  ? 217 ILE D CD1 1 
ATOM   8344  N  N   . SER D  1 218 ? 20.395  -19.916 37.558  1.00 8.81  ? 218 SER D N   1 
ATOM   8345  C  CA  . SER D  1 218 ? 19.457  -19.865 36.410  1.00 11.33 ? 218 SER D CA  1 
ATOM   8346  C  C   . SER D  1 218 ? 18.571  -18.634 36.452  1.00 10.79 ? 218 SER D C   1 
ATOM   8347  O  O   . SER D  1 218 ? 18.467  -17.934 37.515  1.00 10.29 ? 218 SER D O   1 
ATOM   8348  C  CB  . SER D  1 218 ? 18.528  -21.078 36.552  1.00 12.21 ? 218 SER D CB  1 
ATOM   8349  O  OG  . SER D  1 218 ? 17.670  -21.040 37.676  1.00 11.18 ? 218 SER D OG  1 
ATOM   8350  N  N   . GLN D  1 219 ? 17.863  -18.367 35.351  1.00 11.77 ? 219 GLN D N   1 
ATOM   8351  C  CA  . GLN D  1 219 ? 16.848  -17.286 35.310  1.00 13.82 ? 219 GLN D CA  1 
ATOM   8352  C  C   . GLN D  1 219 ? 15.887  -17.459 36.469  1.00 11.85 ? 219 GLN D C   1 
ATOM   8353  O  O   . GLN D  1 219 ? 15.458  -16.481 37.076  1.00 12.29 ? 219 GLN D O   1 
ATOM   8354  C  CB  . GLN D  1 219 ? 16.104  -17.461 33.948  1.00 16.64 ? 219 GLN D CB  1 
ATOM   8355  C  CG  . GLN D  1 219 ? 14.596  -17.131 33.860  1.00 23.33 ? 219 GLN D CG  1 
ATOM   8356  C  CD  . GLN D  1 219 ? 14.133  -17.145 32.367  1.00 23.39 ? 219 GLN D CD  1 
ATOM   8357  O  OE1 . GLN D  1 219 ? 14.970  -17.365 31.470  1.00 22.74 ? 219 GLN D OE1 1 
ATOM   8358  N  NE2 . GLN D  1 219 ? 12.891  -16.775 32.122  1.00 26.99 ? 219 GLN D NE2 1 
ATOM   8359  N  N   . GLU D  1 220 ? 15.433  -18.675 36.729  1.00 11.56 ? 220 GLU D N   1 
ATOM   8360  C  CA  . GLU D  1 220 ? 14.480  -18.910 37.811  1.00 10.70 ? 220 GLU D CA  1 
ATOM   8361  C  C   . GLU D  1 220 ? 15.086  -18.578 39.202  1.00 10.76 ? 220 GLU D C   1 
ATOM   8362  O  O   . GLU D  1 220 ? 14.407  -18.051 40.049  1.00 9.75  ? 220 GLU D O   1 
ATOM   8363  C  CB  . GLU D  1 220 ? 14.004  -20.411 37.825  1.00 15.03 ? 220 GLU D CB  1 
ATOM   8364  C  CG  . GLU D  1 220 ? 13.192  -20.810 36.569  1.00 20.92 ? 220 GLU D CG  1 
ATOM   8365  C  CD  . GLU D  1 220 ? 13.976  -20.987 35.242  1.00 23.44 ? 220 GLU D CD  1 
ATOM   8366  O  OE1 . GLU D  1 220 ? 15.252  -21.127 35.126  1.00 15.87 ? 220 GLU D OE1 1 
ATOM   8367  O  OE2 . GLU D  1 220 ? 13.198  -21.039 34.224  1.00 33.03 ? 220 GLU D OE2 1 
ATOM   8368  N  N   . GLN D  1 221 ? 16.357  -18.938 39.420  1.00 9.13  ? 221 GLN D N   1 
ATOM   8369  C  CA  . GLN D  1 221 ? 16.896  -18.696 40.737  1.00 8.87  ? 221 GLN D CA  1 
ATOM   8370  C  C   . GLN D  1 221 ? 17.063  -17.157 40.932  1.00 6.84  ? 221 GLN D C   1 
ATOM   8371  O  O   . GLN D  1 221 ? 16.784  -16.681 42.016  1.00 7.50  ? 221 GLN D O   1 
ATOM   8372  C  CB  . GLN D  1 221 ? 18.295  -19.317 40.771  1.00 8.15  ? 221 GLN D CB  1 
ATOM   8373  C  CG  . GLN D  1 221 ? 18.288  -20.867 40.966  1.00 8.09  ? 221 GLN D CG  1 
ATOM   8374  C  CD  . GLN D  1 221 ? 19.700  -21.438 41.047  1.00 9.29  ? 221 GLN D CD  1 
ATOM   8375  O  OE1 . GLN D  1 221 ? 20.435  -21.396 40.072  1.00 8.64  ? 221 GLN D OE1 1 
ATOM   8376  N  NE2 . GLN D  1 221 ? 20.051  -21.995 42.221  1.00 8.31  ? 221 GLN D NE2 1 
ATOM   8377  N  N   . LEU D  1 222 ? 17.472  -16.467 39.851  1.00 6.74  ? 222 LEU D N   1 
ATOM   8378  C  CA  . LEU D  1 222 ? 17.709  -15.024 39.942  1.00 7.19  ? 222 LEU D CA  1 
ATOM   8379  C  C   . LEU D  1 222 ? 16.344  -14.387 40.262  1.00 7.39  ? 222 LEU D C   1 
ATOM   8380  O  O   . LEU D  1 222 ? 16.199  -13.506 41.166  1.00 7.87  ? 222 LEU D O   1 
ATOM   8381  C  CB  . LEU D  1 222 ? 18.270  -14.501 38.651  1.00 9.82  ? 222 LEU D CB  1 
ATOM   8382  C  CG  . LEU D  1 222 ? 18.504  -13.001 38.577  1.00 8.82  ? 222 LEU D CG  1 
ATOM   8383  C  CD1 . LEU D  1 222 ? 19.424  -12.497 39.761  1.00 12.20 ? 222 LEU D CD1 1 
ATOM   8384  C  CD2 . LEU D  1 222 ? 19.135  -12.608 37.237  1.00 14.98 ? 222 LEU D CD2 1 
ATOM   8385  N  N   . LEU D  1 223 ? 15.273  -14.765 39.518  1.00 7.60  ? 223 LEU D N   1 
ATOM   8386  C  CA  . LEU D  1 223 ? 13.969  -14.142 39.778  1.00 8.07  ? 223 LEU D CA  1 
ATOM   8387  C  C   . LEU D  1 223 ? 13.481  -14.510 41.164  1.00 7.50  ? 223 LEU D C   1 
ATOM   8388  O  O   . LEU D  1 223 ? 12.901  -13.629 41.904  1.00 7.57  ? 223 LEU D O   1 
ATOM   8389  C  CB  . LEU D  1 223 ? 12.967  -14.693 38.718  1.00 8.84  ? 223 LEU D CB  1 
ATOM   8390  C  CG  . LEU D  1 223 ? 11.570  -14.119 38.900  1.00 9.82  ? 223 LEU D CG  1 
ATOM   8391  C  CD1 . LEU D  1 223 ? 11.521  -12.666 38.700  1.00 9.77  ? 223 LEU D CD1 1 
ATOM   8392  C  CD2 . LEU D  1 223 ? 10.622  -14.888 37.830  1.00 13.71 ? 223 LEU D CD2 1 
ATOM   8393  N  N   . ALA D  1 224 ? 13.742  -15.756 41.661  1.00 6.56  ? 224 ALA D N   1 
ATOM   8394  C  CA  . ALA D  1 224 ? 13.319  -16.089 43.018  1.00 7.55  ? 224 ALA D CA  1 
ATOM   8395  C  C   . ALA D  1 224 ? 13.973  -15.123 44.039  1.00 7.18  ? 224 ALA D C   1 
ATOM   8396  O  O   . ALA D  1 224 ? 13.346  -14.644 44.990  1.00 7.30  ? 224 ALA D O   1 
ATOM   8397  C  CB  . ALA D  1 224 ? 13.668  -17.576 43.373  1.00 8.67  ? 224 ALA D CB  1 
ATOM   8398  N  N   . LEU D  1 225 ? 15.322  -14.907 43.830  1.00 6.79  ? 225 LEU D N   1 
ATOM   8399  C  CA  . LEU D  1 225 ? 16.019  -14.069 44.832  1.00 7.53  ? 225 LEU D CA  1 
ATOM   8400  C  C   . LEU D  1 225 ? 15.458  -12.615 44.794  1.00 7.38  ? 225 LEU D C   1 
ATOM   8401  O  O   . LEU D  1 225 ? 15.282  -12.008 45.865  1.00 7.49  ? 225 LEU D O   1 
ATOM   8402  C  CB  . LEU D  1 225 ? 17.528  -14.015 44.404  1.00 6.55  ? 225 LEU D CB  1 
ATOM   8403  C  CG  . LEU D  1 225 ? 18.457  -13.090 45.220  1.00 6.70  ? 225 LEU D CG  1 
ATOM   8404  C  CD1 . LEU D  1 225 ? 18.393  -13.541 46.705  1.00 7.50  ? 225 LEU D CD1 1 
ATOM   8405  C  CD2 . LEU D  1 225 ? 19.830  -13.127 44.581  1.00 8.70  ? 225 LEU D CD2 1 
ATOM   8406  N  N   . GLU D  1 226 ? 15.191  -12.111 43.566  1.00 5.47  ? 226 GLU D N   1 
ATOM   8407  C  CA  . GLU D  1 226 ? 14.663  -10.773 43.444  1.00 6.60  ? 226 GLU D CA  1 
ATOM   8408  C  C   . GLU D  1 226 ? 13.247  -10.585 43.929  1.00 7.50  ? 226 GLU D C   1 
ATOM   8409  O  O   . GLU D  1 226 ? 12.795  -9.420  44.139  1.00 8.35  ? 226 GLU D O   1 
ATOM   8410  C  CB  . GLU D  1 226 ? 14.629  -10.355 41.949  1.00 6.27  ? 226 GLU D CB  1 
ATOM   8411  C  CG  . GLU D  1 226 ? 16.056  -10.255 41.339  1.00 5.13  ? 226 GLU D CG  1 
ATOM   8412  C  CD  . GLU D  1 226 ? 16.046  -10.322 39.824  1.00 6.88  ? 226 GLU D CD  1 
ATOM   8413  O  OE1 . GLU D  1 226 ? 15.010  -10.723 39.253  1.00 6.69  ? 226 GLU D OE1 1 
ATOM   8414  O  OE2 . GLU D  1 226 ? 17.073  -9.973  39.205  1.00 8.23  ? 226 GLU D OE2 1 
ATOM   8415  N  N   . THR D  1 227 ? 12.502  -11.700 44.133  1.00 6.21  ? 227 THR D N   1 
ATOM   8416  C  CA  . THR D  1 227 ? 11.072  -11.551 44.554  1.00 8.00  ? 227 THR D CA  1 
ATOM   8417  C  C   . THR D  1 227 ? 10.736  -12.116 45.910  1.00 8.53  ? 227 THR D C   1 
ATOM   8418  O  O   . THR D  1 227 ? 9.600   -11.962 46.342  1.00 10.81 ? 227 THR D O   1 
ATOM   8419  C  CB  . THR D  1 227 ? 10.185  -12.315 43.491  1.00 7.07  ? 227 THR D CB  1 
ATOM   8420  O  OG1 . THR D  1 227 ? 10.531  -13.685 43.399  1.00 8.12  ? 227 THR D OG1 1 
ATOM   8421  C  CG2 . THR D  1 227 ? 10.284  -11.534 42.151  1.00 8.33  ? 227 THR D CG2 1 
ATOM   8422  N  N   . ALA D  1 228 ? 11.689  -12.773 46.575  1.00 7.50  ? 228 ALA D N   1 
ATOM   8423  C  CA  . ALA D  1 228 ? 11.372  -13.512 47.810  1.00 9.05  ? 228 ALA D CA  1 
ATOM   8424  C  C   . ALA D  1 228 ? 11.150  -12.589 48.999  1.00 9.38  ? 228 ALA D C   1 
ATOM   8425  O  O   . ALA D  1 228 ? 10.407  -12.944 49.949  1.00 10.44 ? 228 ALA D O   1 
ATOM   8426  C  CB  . ALA D  1 228 ? 12.434  -14.536 48.099  1.00 10.49 ? 228 ALA D CB  1 
ATOM   8427  N  N   . LEU D  1 229 ? 11.900  -11.474 49.040  1.00 7.33  ? 229 LEU D N   1 
ATOM   8428  C  CA  . LEU D  1 229 ? 12.120  -10.814 50.351  1.00 7.79  ? 229 LEU D CA  1 
ATOM   8429  C  C   . LEU D  1 229 ? 11.603  -9.361  50.393  1.00 7.99  ? 229 LEU D C   1 
ATOM   8430  O  O   . LEU D  1 229 ? 11.504  -8.712  49.359  1.00 6.80  ? 229 LEU D O   1 
ATOM   8431  C  CB  . LEU D  1 229 ? 13.631  -10.740 50.651  1.00 6.83  ? 229 LEU D CB  1 
ATOM   8432  C  CG  . LEU D  1 229 ? 14.351  -12.086 50.567  1.00 8.81  ? 229 LEU D CG  1 
ATOM   8433  C  CD1 . LEU D  1 229 ? 15.863  -11.914 50.758  1.00 11.02 ? 229 LEU D CD1 1 
ATOM   8434  C  CD2 . LEU D  1 229 ? 13.749  -13.124 51.504  1.00 10.29 ? 229 LEU D CD2 1 
ATOM   8435  N  N   . TYR D  1 230 ? 11.320  -8.891  51.591  1.00 6.72  ? 230 TYR D N   1 
ATOM   8436  C  CA  . TYR D  1 230 ? 10.864  -7.539  51.893  1.00 7.11  ? 230 TYR D CA  1 
ATOM   8437  C  C   . TYR D  1 230 ? 11.871  -6.917  52.906  1.00 8.44  ? 230 TYR D C   1 
ATOM   8438  O  O   . TYR D  1 230 ? 12.504  -7.591  53.777  1.00 8.23  ? 230 TYR D O   1 
ATOM   8439  C  CB  . TYR D  1 230 ? 9.422   -7.548  52.521  1.00 9.54  ? 230 TYR D CB  1 
ATOM   8440  C  CG  . TYR D  1 230 ? 8.410   -7.940  51.469  1.00 8.85  ? 230 TYR D CG  1 
ATOM   8441  C  CD1 . TYR D  1 230 ? 8.255   -9.268  51.096  1.00 10.51 ? 230 TYR D CD1 1 
ATOM   8442  C  CD2 . TYR D  1 230 ? 7.656   -6.981  50.804  1.00 9.98  ? 230 TYR D CD2 1 
ATOM   8443  C  CE1 . TYR D  1 230 ? 7.352   -9.637  50.120  1.00 8.85  ? 230 TYR D CE1 1 
ATOM   8444  C  CE2 . TYR D  1 230 ? 6.748   -7.342  49.822  1.00 9.18  ? 230 TYR D CE2 1 
ATOM   8445  C  CZ  . TYR D  1 230 ? 6.602   -8.672  49.485  1.00 10.45 ? 230 TYR D CZ  1 
ATOM   8446  O  OH  . TYR D  1 230 ? 5.703   -9.043  48.512  1.00 17.78 ? 230 TYR D OH  1 
ATOM   8447  N  N   . CYS D  1 231 ? 12.033  -5.602  52.814  1.00 7.69  ? 231 CYS D N   1 
ATOM   8448  C  CA  . CYS D  1 231 ? 12.859  -4.850  53.718  1.00 8.93  ? 231 CYS D CA  1 
ATOM   8449  C  C   . CYS D  1 231 ? 12.248  -4.552  55.088  1.00 10.45 ? 231 CYS D C   1 
ATOM   8450  O  O   . CYS D  1 231 ? 12.891  -4.103  56.055  1.00 10.49 ? 231 CYS D O   1 
ATOM   8451  C  CB  . CYS D  1 231 ? 13.174  -3.452  53.151  1.00 11.41 ? 231 CYS D CB  1 
ATOM   8452  S  SG  . CYS D  1 231 ? 14.129  -3.492  51.636  1.00 10.49 ? 231 CYS D SG  1 
ATOM   8453  N  N   . THR D  1 232 ? 10.947  -4.775  55.158  1.00 8.92  ? 232 THR D N   1 
ATOM   8454  C  CA  . THR D  1 232 ? 10.114  -4.289  56.235  1.00 9.05  ? 232 THR D CA  1 
ATOM   8455  C  C   . THR D  1 232 ? 9.625   -5.452  57.148  1.00 9.89  ? 232 THR D C   1 
ATOM   8456  O  O   . THR D  1 232 ? 9.613   -6.617  56.762  1.00 10.18 ? 232 THR D O   1 
ATOM   8457  C  CB  . THR D  1 232 ? 8.866   -3.559  55.630  1.00 9.50  ? 232 THR D CB  1 
ATOM   8458  O  OG1 . THR D  1 232 ? 8.342   -4.320  54.502  1.00 9.41  ? 232 THR D OG1 1 
ATOM   8459  C  CG2 . THR D  1 232 ? 9.323   -2.155  55.229  1.00 12.59 ? 232 THR D CG2 1 
ATOM   8460  N  N   . HIS D  1 233 ? 9.282   -5.110  58.406  1.00 9.85  ? 233 HIS D N   1 
ATOM   8461  C  CA  . HIS D  1 233 ? 8.750   -6.069  59.296  1.00 12.47 ? 233 HIS D CA  1 
ATOM   8462  C  C   . HIS D  1 233 ? 7.373   -6.545  58.868  1.00 13.45 ? 233 HIS D C   1 
ATOM   8463  O  O   . HIS D  1 233 ? 6.637   -5.846  58.137  1.00 12.56 ? 233 HIS D O   1 
ATOM   8464  C  CB  . HIS D  1 233 ? 8.627   -5.435  60.750  1.00 13.52 ? 233 HIS D CB  1 
ATOM   8465  C  CG  . HIS D  1 233 ? 9.924   -5.093  61.405  1.00 14.55 ? 233 HIS D CG  1 
ATOM   8466  N  ND1 . HIS D  1 233 ? 10.799  -6.025  61.935  1.00 19.01 ? 233 HIS D ND1 1 
ATOM   8467  C  CD2 . HIS D  1 233 ? 10.381  -3.884  61.809  1.00 19.89 ? 233 HIS D CD2 1 
ATOM   8468  C  CE1 . HIS D  1 233 ? 11.820  -5.384  62.498  1.00 16.52 ? 233 HIS D CE1 1 
ATOM   8469  N  NE2 . HIS D  1 233 ? 11.589  -4.096  62.432  1.00 22.23 ? 233 HIS D NE2 1 
ATOM   8470  N  N   . MET D  1 234 ? 6.994   -7.705  59.431  1.00 12.33 ? 234 MET D N   1 
ATOM   8471  C  CA  . MET D  1 234 ? 5.771   -8.303  58.997  1.00 17.43 ? 234 MET D CA  1 
ATOM   8472  C  C   . MET D  1 234 ? 4.571   -7.463  59.485  1.00 17.53 ? 234 MET D C   1 
ATOM   8473  O  O   . MET D  1 234 ? 3.475   -7.683  58.923  1.00 19.25 ? 234 MET D O   1 
ATOM   8474  C  CB  . MET D  1 234 ? 5.694   -9.727  59.506  1.00 15.58 ? 234 MET D CB  1 
ATOM   8475  C  CG  . MET D  1 234 ? 5.493   -9.765  60.992  1.00 19.59 ? 234 MET D CG  1 
ATOM   8476  S  SD  . MET D  1 234 ? 5.779   -11.394 61.764  1.00 23.46 ? 234 MET D SD  1 
ATOM   8477  C  CE  . MET D  1 234 ? 4.992   -12.422 60.561  1.00 19.00 ? 234 MET D CE  1 
ATOM   8478  N  N   . ASP D  1 235 ? 4.717   -6.510  60.420  1.00 15.32 ? 235 ASP D N   1 
ATOM   8479  C  CA  . ASP D  1 235 ? 3.617   -5.612  60.769  1.00 16.35 ? 235 ASP D CA  1 
ATOM   8480  C  C   . ASP D  1 235 ? 3.764   -4.177  60.285  1.00 17.73 ? 235 ASP D C   1 
ATOM   8481  O  O   . ASP D  1 235 ? 3.145   -3.274  60.889  1.00 15.27 ? 235 ASP D O   1 
ATOM   8482  C  CB  . ASP D  1 235 ? 3.371   -5.594  62.281  1.00 17.96 ? 235 ASP D CB  1 
ATOM   8483  C  CG  . ASP D  1 235 ? 4.560   -5.037  63.047  1.00 22.60 ? 235 ASP D CG  1 
ATOM   8484  O  OD1 . ASP D  1 235 ? 5.665   -4.794  62.454  1.00 21.56 ? 235 ASP D OD1 1 
ATOM   8485  O  OD2 . ASP D  1 235 ? 4.452   -4.769  64.276  1.00 30.02 ? 235 ASP D OD2 1 
ATOM   8486  N  N   . ASP D  1 236 ? 4.550   -3.942  59.221  1.00 13.73 ? 236 ASP D N   1 
ATOM   8487  C  CA  . ASP D  1 236 ? 4.777   -2.573  58.783  1.00 15.23 ? 236 ASP D CA  1 
ATOM   8488  C  C   . ASP D  1 236 ? 3.545   -2.242  57.885  1.00 14.71 ? 236 ASP D C   1 
ATOM   8489  O  O   . ASP D  1 236 ? 3.248   -2.989  56.898  1.00 14.57 ? 236 ASP D O   1 
ATOM   8490  C  CB  . ASP D  1 236 ? 6.094   -2.496  58.002  1.00 13.28 ? 236 ASP D CB  1 
ATOM   8491  C  CG  . ASP D  1 236 ? 6.564   -1.051  57.732  1.00 16.23 ? 236 ASP D CG  1 
ATOM   8492  O  OD1 . ASP D  1 236 ? 5.783   -0.146  57.261  1.00 13.46 ? 236 ASP D OD1 1 
ATOM   8493  O  OD2 . ASP D  1 236 ? 7.752   -0.795  57.980  1.00 17.85 ? 236 ASP D OD2 1 
ATOM   8494  N  N   . PRO D  1 237 ? 2.880   -1.106  58.148  1.00 17.45 ? 237 PRO D N   1 
ATOM   8495  C  CA  . PRO D  1 237 ? 1.801   -0.679  57.252  1.00 17.06 ? 237 PRO D CA  1 
ATOM   8496  C  C   . PRO D  1 237 ? 2.251   -0.245  55.857  1.00 17.97 ? 237 PRO D C   1 
ATOM   8497  O  O   . PRO D  1 237 ? 1.403   -0.131  54.938  1.00 18.28 ? 237 PRO D O   1 
ATOM   8498  C  CB  . PRO D  1 237 ? 1.169   0.533   58.048  1.00 19.58 ? 237 PRO D CB  1 
ATOM   8499  C  CG  . PRO D  1 237 ? 2.178   1.050   58.951  1.00 18.45 ? 237 PRO D CG  1 
ATOM   8500  C  CD  . PRO D  1 237 ? 3.139   -0.136  59.244  1.00 17.46 ? 237 PRO D CD  1 
ATOM   8501  N  N   . SER D  1 238 ? 3.566   -0.009  55.607  1.00 14.69 ? 238 SER D N   1 
ATOM   8502  C  CA  . SER D  1 238 ? 4.034   0.412   54.268  1.00 15.57 ? 238 SER D CA  1 
ATOM   8503  C  C   . SER D  1 238 ? 5.169   -0.576  53.838  1.00 14.46 ? 238 SER D C   1 
ATOM   8504  O  O   . SER D  1 238 ? 6.384   -0.214  53.921  1.00 14.26 ? 238 SER D O   1 
ATOM   8505  C  CB  . SER D  1 238 ? 4.617   1.882   54.295  1.00 17.63 ? 238 SER D CB  1 
ATOM   8506  O  OG  . SER D  1 238 ? 3.528   2.717   54.637  1.00 23.49 ? 238 SER D OG  1 
ATOM   8507  N  N   . PRO D  1 239 ? 4.774   -1.788  53.412  1.00 11.67 ? 239 PRO D N   1 
ATOM   8508  C  CA  . PRO D  1 239 ? 5.797   -2.804  52.953  1.00 11.33 ? 239 PRO D CA  1 
ATOM   8509  C  C   . PRO D  1 239 ? 6.638   -2.284  51.867  1.00 12.36 ? 239 PRO D C   1 
ATOM   8510  O  O   . PRO D  1 239 ? 6.178   -1.620  50.947  1.00 12.37 ? 239 PRO D O   1 
ATOM   8511  C  CB  . PRO D  1 239 ? 4.976   -4.051  52.530  1.00 9.29  ? 239 PRO D CB  1 
ATOM   8512  C  CG  . PRO D  1 239 ? 3.518   -3.634  52.774  1.00 16.43 ? 239 PRO D CG  1 
ATOM   8513  C  CD  . PRO D  1 239 ? 3.411   -2.334  53.361  1.00 13.29 ? 239 PRO D CD  1 
ATOM   8514  N  N   . ARG D  1 240 ? 7.939   -2.688  51.895  1.00 10.31 ? 240 ARG D N   1 
ATOM   8515  C  CA  . ARG D  1 240 ? 8.876   -2.330  50.811  1.00 10.07 ? 240 ARG D CA  1 
ATOM   8516  C  C   . ARG D  1 240 ? 9.567   -3.642  50.324  1.00 10.88 ? 240 ARG D C   1 
ATOM   8517  O  O   . ARG D  1 240 ? 10.191  -4.330  51.193  1.00 10.08 ? 240 ARG D O   1 
ATOM   8518  C  CB  . ARG D  1 240 ? 9.904   -1.357  51.380  1.00 10.77 ? 240 ARG D CB  1 
ATOM   8519  C  CG  . ARG D  1 240 ? 9.194   0.080   51.667  1.00 12.37 ? 240 ARG D CG  1 
ATOM   8520  C  CD  . ARG D  1 240 ? 10.271  1.053   52.280  1.00 17.87 ? 240 ARG D CD  1 
ATOM   8521  N  NE  . ARG D  1 240 ? 10.619  0.817   53.683  1.00 20.99 ? 240 ARG D NE  1 
ATOM   8522  C  CZ  . ARG D  1 240 ? 11.778  0.311   54.109  1.00 18.59 ? 240 ARG D CZ  1 
ATOM   8523  N  NH1 . ARG D  1 240 ? 12.720  -0.059  53.251  1.00 15.90 ? 240 ARG D NH1 1 
ATOM   8524  N  NH2 . ARG D  1 240 ? 11.995  0.165   55.408  1.00 20.10 ? 240 ARG D NH2 1 
ATOM   8525  N  N   . GLU D  1 241 ? 9.474   -3.986  49.050  1.00 10.62 ? 241 GLU D N   1 
ATOM   8526  C  CA  . GLU D  1 241 ? 10.214  -5.138  48.478  1.00 8.16  ? 241 GLU D CA  1 
ATOM   8527  C  C   . GLU D  1 241 ? 11.690  -4.925  48.520  1.00 9.26  ? 241 GLU D C   1 
ATOM   8528  O  O   . GLU D  1 241 ? 12.236  -3.769  48.311  1.00 8.45  ? 241 GLU D O   1 
ATOM   8529  C  CB  . GLU D  1 241 ? 9.810   -5.327  47.006  1.00 10.31 ? 241 GLU D CB  1 
ATOM   8530  C  CG  . GLU D  1 241 ? 8.362   -5.818  46.976  1.00 15.02 ? 241 GLU D CG  1 
ATOM   8531  C  CD  . GLU D  1 241 ? 7.735   -5.740  45.620  1.00 23.93 ? 241 GLU D CD  1 
ATOM   8532  O  OE1 . GLU D  1 241 ? 6.534   -6.126  45.600  1.00 25.96 ? 241 GLU D OE1 1 
ATOM   8533  O  OE2 . GLU D  1 241 ? 8.411   -5.311  44.626  1.00 23.07 ? 241 GLU D OE2 1 
ATOM   8534  N  N   . MET D  1 242 ? 12.424  -6.029  48.820  1.00 8.54  ? 242 MET D N   1 
ATOM   8535  C  CA  . MET D  1 242 ? 13.905  -5.990  48.893  1.00 7.62  ? 242 MET D CA  1 
ATOM   8536  C  C   . MET D  1 242 ? 14.411  -6.241  47.485  1.00 6.04  ? 242 MET D C   1 
ATOM   8537  O  O   . MET D  1 242 ? 14.655  -7.358  47.047  1.00 6.73  ? 242 MET D O   1 
ATOM   8538  C  CB  . MET D  1 242 ? 14.423  -7.000  49.869  1.00 6.47  ? 242 MET D CB  1 
ATOM   8539  C  CG  . MET D  1 242 ? 15.916  -6.721  50.125  1.00 10.43 ? 242 MET D CG  1 
ATOM   8540  S  SD  . MET D  1 242 ? 16.688  -7.999  51.201  1.00 7.42  ? 242 MET D SD  1 
ATOM   8541  C  CE  . MET D  1 242 ? 15.893  -7.484  52.762  1.00 9.49  ? 242 MET D CE  1 
ATOM   8542  N  N   . ILE D  1 243 ? 14.616  -5.112  46.733  1.00 5.63  ? 243 ILE D N   1 
ATOM   8543  C  CA  . ILE D  1 243 ? 15.129  -4.991  45.372  1.00 5.80  ? 243 ILE D CA  1 
ATOM   8544  C  C   . ILE D  1 243 ? 16.149  -3.823  45.292  1.00 4.75  ? 243 ILE D C   1 
ATOM   8545  O  O   . ILE D  1 243 ? 16.099  -2.924  46.133  1.00 6.13  ? 243 ILE D O   1 
ATOM   8546  C  CB  . ILE D  1 243 ? 13.972  -4.793  44.333  1.00 7.00  ? 243 ILE D CB  1 
ATOM   8547  C  CG1 . ILE D  1 243 ? 13.131  -3.626  44.726  1.00 8.88  ? 243 ILE D CG1 1 
ATOM   8548  C  CG2 . ILE D  1 243 ? 13.061  -6.145  44.197  1.00 7.26  ? 243 ILE D CG2 1 
ATOM   8549  C  CD1 . ILE D  1 243 ? 12.051  -3.204  43.656  1.00 10.65 ? 243 ILE D CD1 1 
ATOM   8550  N  N   . ASN D  1 244 ? 17.026  -3.952  44.309  1.00 5.26  ? 244 ASN D N   1 
ATOM   8551  C  CA  . ASN D  1 244 ? 17.967  -2.865  44.056  1.00 4.71  ? 244 ASN D CA  1 
ATOM   8552  C  C   . ASN D  1 244 ? 18.773  -2.570  45.293  1.00 5.45  ? 244 ASN D C   1 
ATOM   8553  O  O   . ASN D  1 244 ? 19.083  -1.422  45.550  1.00 6.05  ? 244 ASN D O   1 
ATOM   8554  C  CB  . ASN D  1 244 ? 17.234  -1.669  43.525  1.00 5.07  ? 244 ASN D CB  1 
ATOM   8555  C  CG  . ASN D  1 244 ? 16.433  -2.053  42.271  1.00 6.20  ? 244 ASN D CG  1 
ATOM   8556  O  OD1 . ASN D  1 244 ? 16.884  -2.799  41.426  1.00 7.54  ? 244 ASN D OD1 1 
ATOM   8557  N  ND2 . ASN D  1 244 ? 15.210  -1.416  42.225  1.00 7.91  ? 244 ASN D ND2 1 
ATOM   8558  N  N   . ASN D  1 245 ? 19.181  -3.617  46.039  1.00 3.98  ? 245 ASN D N   1 
ATOM   8559  C  CA  . ASN D  1 245 ? 19.949  -3.429  47.271  1.00 4.80  ? 245 ASN D CA  1 
ATOM   8560  C  C   . ASN D  1 245 ? 21.441  -3.462  46.989  1.00 4.18  ? 245 ASN D C   1 
ATOM   8561  O  O   . ASN D  1 245 ? 22.166  -4.276  47.595  1.00 5.15  ? 245 ASN D O   1 
ATOM   8562  C  CB  . ASN D  1 245 ? 19.477  -4.483  48.320  1.00 4.93  ? 245 ASN D CB  1 
ATOM   8563  C  CG  . ASN D  1 245 ? 19.754  -5.920  47.918  1.00 5.37  ? 245 ASN D CG  1 
ATOM   8564  O  OD1 . ASN D  1 245 ? 19.870  -6.215  46.743  1.00 5.35  ? 245 ASN D OD1 1 
ATOM   8565  N  ND2 . ASN D  1 245 ? 19.877  -6.802  48.936  1.00 7.52  ? 245 ASN D ND2 1 
ATOM   8566  N  N   . PHE D  1 246 ? 21.897  -2.606  46.089  1.00 4.12  ? 246 PHE D N   1 
ATOM   8567  C  CA  . PHE D  1 246 ? 23.295  -2.427  45.759  1.00 3.77  ? 246 PHE D CA  1 
ATOM   8568  C  C   . PHE D  1 246 ? 23.526  -0.921  45.714  1.00 3.62  ? 246 PHE D C   1 
ATOM   8569  O  O   . PHE D  1 246 ? 22.625  -0.095  45.460  1.00 4.70  ? 246 PHE D O   1 
ATOM   8570  C  CB  . PHE D  1 246 ? 23.633  -3.027  44.343  1.00 4.59  ? 246 PHE D CB  1 
ATOM   8571  C  CG  . PHE D  1 246 ? 22.888  -2.397  43.202  1.00 4.74  ? 246 PHE D CG  1 
ATOM   8572  C  CD1 . PHE D  1 246 ? 23.488  -1.415  42.383  1.00 4.43  ? 246 PHE D CD1 1 
ATOM   8573  C  CD2 . PHE D  1 246 ? 21.589  -2.793  42.845  1.00 4.47  ? 246 PHE D CD2 1 
ATOM   8574  C  CE1 . PHE D  1 246 ? 22.825  -0.787  41.427  1.00 4.76  ? 246 PHE D CE1 1 
ATOM   8575  C  CE2 . PHE D  1 246 ? 20.891  -2.143  41.789  1.00 4.16  ? 246 PHE D CE2 1 
ATOM   8576  C  CZ  . PHE D  1 246 ? 21.560  -1.119  41.115  1.00 3.49  ? 246 PHE D CZ  1 
ATOM   8577  N  N   . ARG D  1 247 ? 24.819  -0.566  46.036  1.00 3.38  ? 247 ARG D N   1 
ATOM   8578  C  CA  . ARG D  1 247 ? 25.216  0.834   46.004  1.00 4.03  ? 247 ARG D CA  1 
ATOM   8579  C  C   . ARG D  1 247 ? 25.783  1.209   44.616  1.00 4.25  ? 247 ARG D C   1 
ATOM   8580  O  O   . ARG D  1 247 ? 26.386  0.367   43.959  1.00 4.78  ? 247 ARG D O   1 
ATOM   8581  C  CB  . ARG D  1 247 ? 26.279  1.071   47.078  1.00 3.96  ? 247 ARG D CB  1 
ATOM   8582  C  CG  . ARG D  1 247 ? 26.535  2.555   47.403  1.00 3.40  ? 247 ARG D CG  1 
ATOM   8583  C  CD  . ARG D  1 247 ? 27.803  2.663   48.276  1.00 5.31  ? 247 ARG D CD  1 
ATOM   8584  N  NE  . ARG D  1 247 ? 27.856  4.031   48.871  1.00 4.76  ? 247 ARG D NE  1 
ATOM   8585  C  CZ  . ARG D  1 247 ? 28.838  4.379   49.706  1.00 4.49  ? 247 ARG D CZ  1 
ATOM   8586  N  NH1 . ARG D  1 247 ? 29.860  3.582   49.950  1.00 3.59  ? 247 ARG D NH1 1 
ATOM   8587  N  NH2 . ARG D  1 247 ? 28.820  5.610   50.249  1.00 3.77  ? 247 ARG D NH2 1 
ATOM   8588  N  N   . GLN D  1 248 ? 25.488  2.432   44.168  1.00 4.69  ? 248 GLN D N   1 
ATOM   8589  C  CA  . GLN D  1 248 ? 26.137  2.971   42.946  1.00 5.18  ? 248 GLN D CA  1 
ATOM   8590  C  C   . GLN D  1 248 ? 27.640  2.955   43.102  1.00 4.50  ? 248 GLN D C   1 
ATOM   8591  O  O   . GLN D  1 248 ? 28.233  3.070   44.218  1.00 5.26  ? 248 GLN D O   1 
ATOM   8592  C  CB  . GLN D  1 248 ? 25.688  4.405   42.619  1.00 4.18  ? 248 GLN D CB  1 
ATOM   8593  C  CG  . GLN D  1 248 ? 24.209  4.572   42.352  1.00 4.91  ? 248 GLN D CG  1 
ATOM   8594  C  CD  . GLN D  1 248 ? 23.741  3.788   41.157  1.00 5.27  ? 248 GLN D CD  1 
ATOM   8595  O  OE1 . GLN D  1 248 ? 23.209  2.668   41.277  1.00 6.56  ? 248 GLN D OE1 1 
ATOM   8596  N  NE2 . GLN D  1 248 ? 23.924  4.317   39.997  1.00 5.36  ? 248 GLN D NE2 1 
ATOM   8597  N  N   . VAL D  1 249 ? 28.376  2.760   41.990  1.00 3.99  ? 249 VAL D N   1 
ATOM   8598  C  CA  . VAL D  1 249 ? 29.856  2.807   42.052  1.00 4.29  ? 249 VAL D CA  1 
ATOM   8599  C  C   . VAL D  1 249 ? 30.344  4.192   42.461  1.00 4.64  ? 249 VAL D C   1 
ATOM   8600  O  O   . VAL D  1 249 ? 29.674  5.221   42.178  1.00 4.18  ? 249 VAL D O   1 
ATOM   8601  C  CB  . VAL D  1 249 ? 30.507  2.350   40.742  1.00 6.36  ? 249 VAL D CB  1 
ATOM   8602  C  CG1 . VAL D  1 249 ? 30.233  0.814   40.463  1.00 6.90  ? 249 VAL D CG1 1 
ATOM   8603  C  CG2 . VAL D  1 249 ? 30.081  3.178   39.540  1.00 7.47  ? 249 VAL D CG2 1 
ATOM   8604  N  N   . GLN D  1 250 ? 31.499  4.174   43.096  1.00 5.54  ? 250 GLN D N   1 
ATOM   8605  C  CA  . GLN D  1 250 ? 32.065  5.410   43.662  1.00 6.07  ? 250 GLN D CA  1 
ATOM   8606  C  C   . GLN D  1 250 ? 33.198  5.980   42.728  1.00 7.36  ? 250 GLN D C   1 
ATOM   8607  O  O   . GLN D  1 250 ? 33.855  5.199   42.063  1.00 7.88  ? 250 GLN D O   1 
ATOM   8608  C  CB  . GLN D  1 250 ? 32.700  5.038   45.049  1.00 6.24  ? 250 GLN D CB  1 
ATOM   8609  C  CG  . GLN D  1 250 ? 31.696  4.405   45.930  1.00 5.86  ? 250 GLN D CG  1 
ATOM   8610  C  CD  . GLN D  1 250 ? 30.589  5.355   46.395  1.00 5.23  ? 250 GLN D CD  1 
ATOM   8611  O  OE1 . GLN D  1 250 ? 30.822  6.374   47.083  1.00 6.49  ? 250 GLN D OE1 1 
ATOM   8612  N  NE2 . GLN D  1 250 ? 29.324  5.022   46.034  1.00 5.01  ? 250 GLN D NE2 1 
ATOM   8613  N  N   . LYS D  1 251 ? 33.482  7.308   42.907  1.00 6.16  ? 251 LYS D N   1 
ATOM   8614  C  CA  . LYS D  1 251 ? 34.712  7.825   42.350  1.00 7.13  ? 251 LYS D CA  1 
ATOM   8615  C  C   . LYS D  1 251 ? 35.939  7.078   42.885  1.00 7.91  ? 251 LYS D C   1 
ATOM   8616  O  O   . LYS D  1 251 ? 35.910  6.663   44.050  1.00 8.65  ? 251 LYS D O   1 
ATOM   8617  C  CB  . LYS D  1 251 ? 34.908  9.262   42.717  1.00 8.06  ? 251 LYS D CB  1 
ATOM   8618  C  CG  . LYS D  1 251 ? 33.917  10.380  42.101  1.00 13.08 ? 251 LYS D CG  1 
ATOM   8619  C  CD  . LYS D  1 251 ? 34.229  10.688  40.728  1.00 12.11 ? 251 LYS D CD  1 
ATOM   8620  C  CE  . LYS D  1 251 ? 33.436  12.003  40.225  1.00 7.59  ? 251 LYS D CE  1 
ATOM   8621  N  NZ  . LYS D  1 251 ? 31.943  11.663  40.203  1.00 5.93  ? 251 LYS D NZ  1 
ATOM   8622  N  N   . PHE D  1 252 ? 36.979  6.888   42.050  1.00 9.30  ? 252 PHE D N   1 
ATOM   8623  C  CA  . PHE D  1 252 ? 38.185  6.184   42.424  1.00 11.45 ? 252 PHE D CA  1 
ATOM   8624  C  C   . PHE D  1 252 ? 39.223  6.839   41.608  1.00 17.91 ? 252 PHE D C   1 
ATOM   8625  O  O   . PHE D  1 252 ? 39.347  6.464   40.367  1.00 15.30 ? 252 PHE D O   1 
ATOM   8626  C  CB  . PHE D  1 252 ? 38.070  4.746   41.920  1.00 15.63 ? 252 PHE D CB  1 
ATOM   8627  C  CG  . PHE D  1 252 ? 39.046  3.842   42.523  1.00 15.01 ? 252 PHE D CG  1 
ATOM   8628  C  CD1 . PHE D  1 252 ? 38.926  3.403   43.829  1.00 12.88 ? 252 PHE D CD1 1 
ATOM   8629  C  CD2 . PHE D  1 252 ? 40.135  3.462   41.758  1.00 15.31 ? 252 PHE D CD2 1 
ATOM   8630  C  CE1 . PHE D  1 252 ? 39.829  2.490   44.385  1.00 21.13 ? 252 PHE D CE1 1 
ATOM   8631  C  CE2 . PHE D  1 252 ? 41.050  2.604   42.336  1.00 17.16 ? 252 PHE D CE2 1 
ATOM   8632  C  CZ  . PHE D  1 252 ? 40.898  2.116   43.639  1.00 18.64 ? 252 PHE D CZ  1 
ATOM   8633  N  N   . ASP D  1 253 ? 39.836  7.836   42.233  1.00 22.02 ? 253 ASP D N   1 
ATOM   8634  C  CA  . ASP D  1 253 ? 40.665  8.928   41.616  1.00 28.79 ? 253 ASP D CA  1 
ATOM   8635  C  C   . ASP D  1 253 ? 42.044  8.952   42.084  1.00 31.66 ? 253 ASP D C   1 
ATOM   8636  O  O   . ASP D  1 253 ? 42.267  8.979   43.259  1.00 32.26 ? 253 ASP D O   1 
ATOM   8637  C  CB  . ASP D  1 253 ? 39.962  10.295  41.859  1.00 29.50 ? 253 ASP D CB  1 
ATOM   8638  C  CG  . ASP D  1 253 ? 38.887  10.626  40.775  1.00 34.41 ? 253 ASP D CG  1 
ATOM   8639  O  OD1 . ASP D  1 253 ? 39.220  10.507  39.575  1.00 39.62 ? 253 ASP D OD1 1 
ATOM   8640  O  OD2 . ASP D  1 253 ? 37.711  10.955  41.077  1.00 33.90 ? 253 ASP D OD2 1 
ATOM   8641  N  N   . GLU D  1 254 ? 42.983  8.911   41.146  1.00 35.30 ? 254 GLU D N   1 
ATOM   8642  C  CA  . GLU D  1 254 ? 44.409  8.623   41.481  1.00 36.44 ? 254 GLU D CA  1 
ATOM   8643  C  C   . GLU D  1 254 ? 44.589  7.280   42.162  1.00 34.89 ? 254 GLU D C   1 
ATOM   8644  O  O   . GLU D  1 254 ? 45.697  6.933   42.540  1.00 35.39 ? 254 GLU D O   1 
ATOM   8645  C  CB  . GLU D  1 254 ? 45.067  9.645   42.436  1.00 37.39 ? 254 GLU D CB  1 
ATOM   8646  C  CG  . GLU D  1 254 ? 45.286  11.041  41.918  1.00 40.95 ? 254 GLU D CG  1 
ATOM   8647  C  CD  . GLU D  1 254 ? 44.260  11.950  42.561  1.00 47.03 ? 254 GLU D CD  1 
ATOM   8648  O  OE1 . GLU D  1 254 ? 44.222  11.962  43.826  1.00 51.63 ? 254 GLU D OE1 1 
ATOM   8649  O  OE2 . GLU D  1 254 ? 43.472  12.585  41.791  1.00 48.00 ? 254 GLU D OE2 1 
ATOM   8650  N  N   . ARG D  1 255 ? 43.522  6.562   42.458  1.00 32.11 ? 255 ARG D N   1 
ATOM   8651  C  CA  . ARG D  1 255 ? 43.932  5.335   43.097  1.00 28.94 ? 255 ARG D CA  1 
ATOM   8652  C  C   . ARG D  1 255 ? 43.915  4.092   42.221  1.00 24.83 ? 255 ARG D C   1 
ATOM   8653  O  O   . ARG D  1 255 ? 43.537  4.212   41.066  1.00 20.61 ? 255 ARG D O   1 
ATOM   8654  C  CB  . ARG D  1 255 ? 43.458  5.219   44.504  1.00 28.79 ? 255 ARG D CB  1 
ATOM   8655  C  CG  . ARG D  1 255 ? 42.168  4.645   44.741  1.00 27.45 ? 255 ARG D CG  1 
ATOM   8656  C  CD  . ARG D  1 255 ? 42.069  4.811   46.303  1.00 21.53 ? 255 ARG D CD  1 
ATOM   8657  N  NE  . ARG D  1 255 ? 41.131  5.854   46.399  1.00 32.81 ? 255 ARG D NE  1 
ATOM   8658  C  CZ  . ARG D  1 255 ? 39.901  5.518   46.616  1.00 18.92 ? 255 ARG D CZ  1 
ATOM   8659  N  NH1 . ARG D  1 255 ? 39.627  4.187   46.768  1.00 23.77 ? 255 ARG D NH1 1 
ATOM   8660  N  NH2 . ARG D  1 255 ? 39.041  6.442   46.764  1.00 20.30 ? 255 ARG D NH2 1 
ATOM   8661  N  N   A LEU D  1 256 ? 44.571  3.011   42.679  0.50 21.97 ? 256 LEU D N   1 
ATOM   8662  N  N   B LEU D  1 256 ? 43.981  2.940   42.929  0.50 21.77 ? 256 LEU D N   1 
ATOM   8663  C  CA  A LEU D  1 256 ? 44.803  1.801   41.903  0.50 16.52 ? 256 LEU D CA  1 
ATOM   8664  C  CA  B LEU D  1 256 ? 44.831  1.775   42.635  0.50 18.31 ? 256 LEU D CA  1 
ATOM   8665  C  C   A LEU D  1 256 ? 44.168  0.531   42.572  0.50 15.18 ? 256 LEU D C   1 
ATOM   8666  C  C   B LEU D  1 256 ? 44.148  0.327   42.811  0.50 13.97 ? 256 LEU D C   1 
ATOM   8667  O  O   A LEU D  1 256 ? 44.118  0.333   43.763  0.50 15.68 ? 256 LEU D O   1 
ATOM   8668  O  O   B LEU D  1 256 ? 44.016  -0.192  43.977  0.50 14.07 ? 256 LEU D O   1 
ATOM   8669  C  CB  A LEU D  1 256 ? 46.288  1.492   41.648  0.50 17.93 ? 256 LEU D CB  1 
ATOM   8670  C  CB  B LEU D  1 256 ? 46.098  1.939   43.501  0.50 19.66 ? 256 LEU D CB  1 
ATOM   8671  C  CG  A LEU D  1 256 ? 47.072  2.462   40.839  0.50 16.28 ? 256 LEU D CG  1 
ATOM   8672  C  CG  B LEU D  1 256 ? 46.413  2.851   44.805  0.50 16.22 ? 256 LEU D CG  1 
ATOM   8673  C  CD1 A LEU D  1 256 ? 48.294  1.793   40.350  0.50 20.89 ? 256 LEU D CD1 1 
ATOM   8674  C  CD1 B LEU D  1 256 ? 47.762  3.507   44.691  0.50 17.22 ? 256 LEU D CD1 1 
ATOM   8675  C  CD2 A LEU D  1 256 ? 46.223  3.012   39.699  0.50 16.86 ? 256 LEU D CD2 1 
ATOM   8676  C  CD2 B LEU D  1 256 ? 45.468  3.867   45.511  0.50 12.70 ? 256 LEU D CD2 1 
ATOM   8677  N  N   . VAL D  1 257 ? 43.787  -0.308  41.673  1.00 13.01 ? 257 VAL D N   1 
ATOM   8678  C  CA  . VAL D  1 257 ? 43.284  -1.685  41.870  1.00 9.98  ? 257 VAL D CA  1 
ATOM   8679  C  C   . VAL D  1 257 ? 44.371  -2.616  41.320  1.00 10.49 ? 257 VAL D C   1 
ATOM   8680  O  O   . VAL D  1 257 ? 44.795  -2.474  40.166  1.00 12.18 ? 257 VAL D O   1 
ATOM   8681  C  CB  . VAL D  1 257 ? 42.017  -1.880  41.075  1.00 9.91  ? 257 VAL D CB  1 
ATOM   8682  C  CG1 . VAL D  1 257 ? 41.541  -3.390  41.238  1.00 10.33 ? 257 VAL D CG1 1 
ATOM   8683  C  CG2 . VAL D  1 257 ? 40.880  -0.978  41.625  1.00 13.79 ? 257 VAL D CG2 1 
ATOM   8684  N  N   . TYR D  1 258 ? 44.697  -3.650  42.079  1.00 8.66  ? 258 TYR D N   1 
ATOM   8685  C  CA  . TYR D  1 258 ? 45.814  -4.555  41.686  1.00 7.92  ? 258 TYR D CA  1 
ATOM   8686  C  C   . TYR D  1 258 ? 45.223  -5.853  41.217  1.00 9.74  ? 258 TYR D C   1 
ATOM   8687  O  O   . TYR D  1 258 ? 44.242  -6.357  41.809  1.00 11.79 ? 258 TYR D O   1 
ATOM   8688  C  CB  . TYR D  1 258 ? 46.738  -4.753  42.869  1.00 9.52  ? 258 TYR D CB  1 
ATOM   8689  C  CG  . TYR D  1 258 ? 47.316  -3.423  43.325  1.00 12.52 ? 258 TYR D CG  1 
ATOM   8690  C  CD1 . TYR D  1 258 ? 46.755  -2.720  44.381  1.00 13.80 ? 258 TYR D CD1 1 
ATOM   8691  C  CD2 . TYR D  1 258 ? 48.359  -2.876  42.655  1.00 13.72 ? 258 TYR D CD2 1 
ATOM   8692  C  CE1 . TYR D  1 258 ? 47.222  -1.462  44.742  1.00 13.35 ? 258 TYR D CE1 1 
ATOM   8693  C  CE2 . TYR D  1 258 ? 48.895  -1.627  43.027  1.00 14.92 ? 258 TYR D CE2 1 
ATOM   8694  C  CZ  . TYR D  1 258 ? 48.322  -0.985  44.077  1.00 16.81 ? 258 TYR D CZ  1 
ATOM   8695  O  OH  . TYR D  1 258 ? 48.774  0.288   44.508  1.00 20.08 ? 258 TYR D OH  1 
ATOM   8696  N  N   . THR D  1 259 ? 45.751  -6.389  40.122  1.00 8.25  ? 259 THR D N   1 
ATOM   8697  C  CA  . THR D  1 259 ? 45.277  -7.632  39.609  1.00 8.16  ? 259 THR D CA  1 
ATOM   8698  C  C   . THR D  1 259 ? 46.350  -8.775  39.792  1.00 8.07  ? 259 THR D C   1 
ATOM   8699  O  O   . THR D  1 259 ? 47.580  -8.520  39.692  1.00 8.50  ? 259 THR D O   1 
ATOM   8700  C  CB  . THR D  1 259 ? 44.892  -7.567  38.158  1.00 7.41  ? 259 THR D CB  1 
ATOM   8701  O  OG1 . THR D  1 259 ? 46.071  -7.155  37.351  1.00 10.30 ? 259 THR D OG1 1 
ATOM   8702  C  CG2 . THR D  1 259 ? 43.756  -6.538  37.913  1.00 9.62  ? 259 THR D CG2 1 
ATOM   8703  N  N   . SER D  1 260 ? 45.877  -10.007 40.076  1.00 8.01  ? 260 SER D N   1 
ATOM   8704  C  CA  . SER D  1 260 ? 46.796  -11.167 40.207  1.00 8.00  ? 260 SER D CA  1 
ATOM   8705  C  C   . SER D  1 260 ? 47.000  -11.812 38.901  1.00 8.96  ? 260 SER D C   1 
ATOM   8706  O  O   . SER D  1 260 ? 47.704  -12.844 38.905  1.00 13.70 ? 260 SER D O   1 
ATOM   8707  C  CB  . SER D  1 260 ? 46.233  -12.112 41.203  1.00 9.46  ? 260 SER D CB  1 
ATOM   8708  O  OG  . SER D  1 260 ? 45.015  -12.673 40.689  1.00 8.49  ? 260 SER D OG  1 
ATOM   8709  N  N   . PHE D  1 261 ? 46.449  -11.266 37.832  1.00 8.28  ? 261 PHE D N   1 
ATOM   8710  C  CA  . PHE D  1 261 ? 46.627  -11.779 36.478  1.00 10.43 ? 261 PHE D CA  1 
ATOM   8711  C  C   . PHE D  1 261 ? 47.151  -10.668 35.572  1.00 12.19 ? 261 PHE D C   1 
ATOM   8712  O  O   . PHE D  1 261 ? 46.702  -9.527  35.649  1.00 11.21 ? 261 PHE D O   1 
ATOM   8713  C  CB  . PHE D  1 261 ? 45.286  -12.340 35.946  1.00 10.80 ? 261 PHE D CB  1 
ATOM   8714  C  CG  . PHE D  1 261 ? 44.152  -11.397 36.024  1.00 10.80 ? 261 PHE D CG  1 
ATOM   8715  C  CD1 . PHE D  1 261 ? 43.807  -10.619 34.920  1.00 9.92  ? 261 PHE D CD1 1 
ATOM   8716  C  CD2 . PHE D  1 261 ? 43.409  -11.222 37.194  1.00 9.38  ? 261 PHE D CD2 1 
ATOM   8717  C  CE1 . PHE D  1 261 ? 42.716  -9.714  34.958  1.00 11.02 ? 261 PHE D CE1 1 
ATOM   8718  C  CE2 . PHE D  1 261 ? 42.339  -10.337 37.216  1.00 9.59  ? 261 PHE D CE2 1 
ATOM   8719  C  CZ  . PHE D  1 261 ? 41.962  -9.638  36.114  1.00 9.62  ? 261 PHE D CZ  1 
ATOM   8720  N  N   . SER D  1 262 ? 48.127  -11.013 34.709  1.00 16.31 ? 262 SER D N   1 
ATOM   8721  C  CA  . SER D  1 262 ? 48.636  -10.020 33.726  1.00 18.32 ? 262 SER D CA  1 
ATOM   8722  C  C   . SER D  1 262 ? 47.878  -10.024 32.432  1.00 19.14 ? 262 SER D C   1 
ATOM   8723  O  O   . SER D  1 262 ? 47.999  -9.050  31.656  1.00 22.45 ? 262 SER D O   1 
ATOM   8724  C  CB  . SER D  1 262 ? 50.112  -10.266 33.417  1.00 19.98 ? 262 SER D CB  1 
ATOM   8725  O  OG  . SER D  1 262 ? 50.190  -11.629 33.097  1.00 24.65 ? 262 SER D OG  1 
ATOM   8726  N  N   . GLN D  1 263 ? 47.073  -11.062 32.186  1.00 17.98 ? 263 GLN D N   1 
ATOM   8727  C  CA  . GLN D  1 263 ? 46.270  -11.138 31.000  1.00 16.18 ? 263 GLN D CA  1 
ATOM   8728  C  C   . GLN D  1 263 ? 45.129  -12.124 31.202  1.00 17.79 ? 263 GLN D C   1 
ATOM   8729  O  O   . GLN D  1 263 ? 45.178  -12.906 32.186  1.00 17.30 ? 263 GLN D O   1 
ATOM   8730  C  CB  . GLN D  1 263 ? 47.169  -11.553 29.761  1.00 17.01 ? 263 GLN D CB  1 
ATOM   8731  C  CG  . GLN D  1 263 ? 48.012  -12.819 30.075  1.00 16.57 ? 263 GLN D CG  1 
ATOM   8732  C  CD  . GLN D  1 263 ? 48.983  -13.307 28.976  1.00 16.33 ? 263 GLN D CD  1 
ATOM   8733  O  OE1 . GLN D  1 263 ? 49.327  -14.504 28.922  1.00 20.69 ? 263 GLN D OE1 1 
ATOM   8734  N  NE2 . GLN D  1 263 ? 49.447  -12.377 28.095  1.00 17.29 ? 263 GLN D NE2 1 
ATOM   8735  O  OXT . GLN D  1 263 ? 44.251  -12.226 30.341  1.00 19.29 ? 263 GLN D OXT 1 
HETATM 8736  ZN ZN  . ZN  E  2 .   ? -1.836  14.679  -7.057  1.00 5.03  ? 301 ZN  A ZN  1 
HETATM 8737  F  F13 B V50 F  3 .   ? -2.670  17.477  -4.809  0.50 8.54  ? 302 V50 A F13 1 
HETATM 8738  F  F13 C V50 F  3 .   ? -4.603  18.657  -6.623  0.50 10.96 ? 302 V50 A F13 1 
HETATM 8739  C  C4  B V50 F  3 .   ? -3.890  17.867  -5.103  0.50 6.38  ? 302 V50 A C4  1 
HETATM 8740  C  C4  C V50 F  3 .   ? -4.682  18.360  -5.339  0.50 8.40  ? 302 V50 A C4  1 
HETATM 8741  C  C5  B V50 F  3 .   ? -4.910  16.973  -5.550  0.50 3.67  ? 302 V50 A C5  1 
HETATM 8742  C  C5  C V50 F  3 .   ? -4.621  17.013  -4.861  0.50 7.72  ? 302 V50 A C5  1 
HETATM 8743  S  S7  B V50 F  3 .   ? -4.699  15.266  -5.998  0.50 5.16  ? 302 V50 A S7  1 
HETATM 8744  S  S7  C V50 F  3 .   ? -4.433  15.516  -5.817  0.50 8.58  ? 302 V50 A S7  1 
HETATM 8745  O  O9  B V50 F  3 .   ? -4.750  15.334  -7.450  0.50 5.98  ? 302 V50 A O9  1 
HETATM 8746  O  O9  C V50 F  3 .   ? -4.534  15.901  -7.155  0.50 6.36  ? 302 V50 A O9  1 
HETATM 8747  N  N23 B V50 F  3 .   ? -3.267  14.784  -5.536  0.50 3.42  ? 302 V50 A N23 1 
HETATM 8748  N  N23 C V50 F  3 .   ? -3.053  14.792  -5.407  0.50 9.62  ? 302 V50 A N23 1 
HETATM 8749  O  O8  B V50 F  3 .   ? -5.691  14.558  -5.213  0.50 3.59  ? 302 V50 A O8  1 
HETATM 8750  O  O8  C V50 F  3 .   ? -5.454  14.618  -5.259  0.50 8.68  ? 302 V50 A O8  1 
HETATM 8751  C  C6  B V50 F  3 .   ? -6.186  17.511  -5.900  0.50 5.54  ? 302 V50 A C6  1 
HETATM 8752  C  C6  C V50 F  3 .   ? -4.713  16.989  -3.487  0.50 9.56  ? 302 V50 A C6  1 
HETATM 8753  F  F11 B V50 F  3 .   ? -7.202  16.704  -6.274  0.50 6.56  ? 302 V50 A F11 1 
HETATM 8754  F  F11 C V50 F  3 .   ? -4.651  15.831  -2.817  0.50 10.48 ? 302 V50 A F11 1 
HETATM 8755  C  C1  B V50 F  3 .   ? -6.479  18.883  -5.710  0.50 9.73  ? 302 V50 A C1  1 
HETATM 8756  C  C1  C V50 F  3 .   ? -4.921  18.080  -2.642  0.50 12.54 ? 302 V50 A C1  1 
HETATM 8757  F  F10 B V50 F  3 .   ? -7.703  19.347  -5.943  0.50 8.32  ? 302 V50 A F10 1 
HETATM 8758  F  F10 C V50 F  3 .   ? -5.084  17.889  -1.306  0.50 12.14 ? 302 V50 A F10 1 
HETATM 8759  C  C3  B V50 F  3 .   ? -4.206  19.208  -5.025  0.50 5.41  ? 302 V50 A C3  1 
HETATM 8760  C  C3  C V50 F  3 .   ? -4.805  19.492  -4.510  0.50 8.74  ? 302 V50 A C3  1 
HETATM 8761  F  F12 B V50 F  3 .   ? -3.174  19.968  -4.688  0.50 9.64  ? 302 V50 A F12 1 
HETATM 8762  F  F12 C V50 F  3 .   ? -4.870  20.745  -5.034  0.50 11.51 ? 302 V50 A F12 1 
HETATM 8763  C  C2  B V50 F  3 .   ? -5.456  19.752  -5.358  0.50 4.75  ? 302 V50 A C2  1 
HETATM 8764  C  C2  C V50 F  3 .   ? -4.995  19.374  -3.150  0.50 11.34 ? 302 V50 A C2  1 
HETATM 8765  S  S14 B V50 F  3 .   ? -5.634  21.485  -5.371  0.50 11.22 ? 302 V50 A S14 1 
HETATM 8766  S  S14 C V50 F  3 .   ? -5.205  20.762  -2.049  0.50 11.26 ? 302 V50 A S14 1 
HETATM 8767  C  C15 B V50 F  3 .   ? -6.871  21.910  -4.242  0.50 9.01  ? 302 V50 A C15 1 
HETATM 8768  C  C15 C V50 F  3 .   ? -6.679  21.578  -2.557  0.50 12.86 ? 302 V50 A C15 1 
HETATM 8769  N  N20 B V50 F  3 .   ? -7.333  21.079  -3.308  0.50 8.61  ? 302 V50 A N20 1 
HETATM 8770  N  N20 C V50 F  3 .   ? -7.352  21.129  -3.628  0.50 14.70 ? 302 V50 A N20 1 
HETATM 8771  C  C19 B V50 F  3 .   ? -8.277  21.607  -2.497  0.50 12.45 ? 302 V50 A C19 1 
HETATM 8772  C  C19 C V50 F  3 .   ? -8.464  21.837  -3.958  0.50 17.57 ? 302 V50 A C19 1 
HETATM 8773  C  C21 B V50 F  3 .   ? -8.735  20.632  -1.431  0.50 11.63 ? 302 V50 A C21 1 
HETATM 8774  C  C21 C V50 F  3 .   ? -9.174  21.322  -5.173  0.50 18.69 ? 302 V50 A C21 1 
HETATM 8775  C  C18 B V50 F  3 .   ? -8.821  22.877  -2.594  0.50 11.67 ? 302 V50 A C18 1 
HETATM 8776  C  C18 C V50 F  3 .   ? -8.970  22.920  -3.282  0.50 19.37 ? 302 V50 A C18 1 
HETATM 8777  C  C17 B V50 F  3 .   ? -8.245  23.620  -3.651  0.50 8.59  ? 302 V50 A C17 1 
HETATM 8778  C  C17 C V50 F  3 .   ? -8.190  23.248  -2.193  0.50 19.18 ? 302 V50 A C17 1 
HETATM 8779  N  N16 B V50 F  3 .   ? -7.273  23.171  -4.485  0.50 13.48 ? 302 V50 A N16 1 
HETATM 8780  N  N16 C V50 F  3 .   ? -7.052  22.606  -1.802  0.50 17.63 ? 302 V50 A N16 1 
HETATM 8781  C  C22 B V50 F  3 .   ? -8.701  25.055  -3.941  0.50 11.08 ? 302 V50 A C22 1 
HETATM 8782  C  C22 C V50 F  3 .   ? -8.649  24.471  -1.419  0.50 18.64 ? 302 V50 A C22 1 
HETATM 8783  C  C1  . PEG G  4 .   ? -0.395  24.176  -4.208  1.00 29.84 ? 303 PEG A C1  1 
HETATM 8784  O  O1  . PEG G  4 .   ? -0.001  25.146  -3.183  1.00 29.73 ? 303 PEG A O1  1 
HETATM 8785  C  C2  . PEG G  4 .   ? -1.671  23.281  -4.281  1.00 23.28 ? 303 PEG A C2  1 
HETATM 8786  O  O2  . PEG G  4 .   ? -2.153  22.963  -2.964  1.00 38.42 ? 303 PEG A O2  1 
HETATM 8787  C  C3  . PEG G  4 .   ? -1.355  21.981  -2.290  1.00 27.70 ? 303 PEG A C3  1 
HETATM 8788  C  C4  . PEG G  4 .   ? -2.099  21.160  -1.218  1.00 26.26 ? 303 PEG A C4  1 
HETATM 8789  O  O4  . PEG G  4 .   ? -2.027  19.729  -1.528  1.00 33.81 ? 303 PEG A O4  1 
HETATM 8790  C  C1  A EDO H  5 .   ? 0.893   20.227  -5.415  0.50 9.67  ? 304 EDO A C1  1 
HETATM 8791  C  C1  B EDO H  5 .   ? 0.232   19.530  -3.933  0.50 17.14 ? 304 EDO A C1  1 
HETATM 8792  O  O1  A EDO H  5 .   ? -0.310  20.836  -5.701  0.50 12.24 ? 304 EDO A O1  1 
HETATM 8793  O  O1  B EDO H  5 .   ? 0.358   20.391  -2.852  0.50 11.95 ? 304 EDO A O1  1 
HETATM 8794  C  C2  A EDO H  5 .   ? 0.883   19.689  -3.968  0.50 15.37 ? 304 EDO A C2  1 
HETATM 8795  C  C2  B EDO H  5 .   ? 0.528   18.105  -3.529  0.50 19.22 ? 304 EDO A C2  1 
HETATM 8796  O  O2  A EDO H  5 .   ? 0.961   18.313  -4.117  0.50 20.68 ? 304 EDO A O2  1 
HETATM 8797  O  O2  B EDO H  5 .   ? 0.741   17.416  -4.726  0.50 22.48 ? 304 EDO A O2  1 
HETATM 8798  C  C1  . EDO I  5 .   ? -19.019 10.438  -19.183 1.00 14.63 ? 305 EDO A C1  1 
HETATM 8799  O  O1  . EDO I  5 .   ? -19.165 9.056   -19.538 1.00 17.25 ? 305 EDO A O1  1 
HETATM 8800  C  C2  . EDO I  5 .   ? -17.596 10.894  -19.408 1.00 14.48 ? 305 EDO A C2  1 
HETATM 8801  O  O2  . EDO I  5 .   ? -16.686 10.188  -18.539 1.00 10.80 ? 305 EDO A O2  1 
HETATM 8802  C  C1  . EDO J  5 .   ? -19.323 5.910   -11.434 1.00 40.03 ? 306 EDO A C1  1 
HETATM 8803  O  O1  . EDO J  5 .   ? -18.138 6.310   -10.770 1.00 35.58 ? 306 EDO A O1  1 
HETATM 8804  C  C2  . EDO J  5 .   ? -19.188 5.789   -12.957 1.00 37.83 ? 306 EDO A C2  1 
HETATM 8805  O  O2  . EDO J  5 .   ? -19.565 4.523   -13.533 1.00 42.31 ? 306 EDO A O2  1 
HETATM 8806  ZN ZN  . ZN  K  2 .   ? -0.003  -11.009 12.312  1.00 5.76  ? 301 ZN  B ZN  1 
HETATM 8807  F  F13 . V50 L  3 .   ? 0.782   -6.843  15.181  1.00 10.20 ? 302 V50 B F13 1 
HETATM 8808  C  C4  . V50 L  3 .   ? 0.736   -7.694  16.201  1.00 8.75  ? 302 V50 B C4  1 
HETATM 8809  C  C5  . V50 L  3 .   ? 1.049   -9.067  15.964  1.00 7.16  ? 302 V50 B C5  1 
HETATM 8810  S  S7  . V50 L  3 .   ? 1.753   -9.460  14.274  1.00 7.86  ? 302 V50 B S7  1 
HETATM 8811  O  O9  . V50 L  3 .   ? 2.227   -10.780 14.361  1.00 7.96  ? 302 V50 B O9  1 
HETATM 8812  N  N23 . V50 L  3 .   ? 0.564   -9.325  13.200  1.00 7.91  ? 302 V50 B N23 1 
HETATM 8813  O  O8  . V50 L  3 .   ? 2.756   -8.428  14.057  1.00 7.77  ? 302 V50 B O8  1 
HETATM 8814  C  C6  . V50 L  3 .   ? 0.920   -9.949  17.064  1.00 8.00  ? 302 V50 B C6  1 
HETATM 8815  F  F11 . V50 L  3 .   ? 1.178   -11.203 16.909  1.00 10.97 ? 302 V50 B F11 1 
HETATM 8816  C  C1  . V50 L  3 .   ? 0.456   -9.415  18.285  1.00 9.26  ? 302 V50 B C1  1 
HETATM 8817  F  F10 . V50 L  3 .   ? 0.259   -10.365 19.243  1.00 11.69 ? 302 V50 B F10 1 
HETATM 8818  C  C3  . V50 L  3 .   ? 0.355   -7.207  17.430  1.00 7.47  ? 302 V50 B C3  1 
HETATM 8819  F  F12 . V50 L  3 .   ? 0.172   -5.925  17.672  1.00 10.28 ? 302 V50 B F12 1 
HETATM 8820  C  C2  . V50 L  3 .   ? 0.214   -8.101  18.494  1.00 9.31  ? 302 V50 B C2  1 
HETATM 8821  S  S14 . V50 L  3 .   ? -0.320  -7.488  20.074  1.00 11.60 ? 302 V50 B S14 1 
HETATM 8822  C  C15 . V50 L  3 .   ? 0.851   -8.104  21.289  1.00 10.69 ? 302 V50 B C15 1 
HETATM 8823  N  N20 . V50 L  3 .   ? 1.844   -8.843  20.912  1.00 9.66  ? 302 V50 B N20 1 
HETATM 8824  C  C19 . V50 L  3 .   ? 2.660   -9.330  21.924  1.00 13.44 ? 302 V50 B C19 1 
HETATM 8825  C  C21 . V50 L  3 .   ? 3.761   -10.278 21.479  1.00 15.42 ? 302 V50 B C21 1 
HETATM 8826  C  C18 . V50 L  3 .   ? 2.430   -9.032  23.268  1.00 16.90 ? 302 V50 B C18 1 
HETATM 8827  C  C17 . V50 L  3 .   ? 1.373   -8.212  23.470  1.00 14.55 ? 302 V50 B C17 1 
HETATM 8828  N  N16 . V50 L  3 .   ? 0.515   -7.692  22.554  1.00 14.26 ? 302 V50 B N16 1 
HETATM 8829  C  C22 . V50 L  3 .   ? 0.999   -7.637  24.834  1.00 16.75 ? 302 V50 B C22 1 
HETATM 8830  C  C1  . PEG M  4 .   ? -14.517 -27.814 20.921  1.00 19.33 ? 303 PEG B C1  1 
HETATM 8831  O  O1  . PEG M  4 .   ? -15.889 -27.464 20.679  1.00 31.38 ? 303 PEG B O1  1 
HETATM 8832  C  C2  . PEG M  4 .   ? -14.198 -28.280 22.365  1.00 28.28 ? 303 PEG B C2  1 
HETATM 8833  O  O2  . PEG M  4 .   ? -13.259 -29.362 22.528  1.00 25.31 ? 303 PEG B O2  1 
HETATM 8834  C  C3  . PEG M  4 .   ? -12.303 -29.486 23.646  1.00 25.08 ? 303 PEG B C3  1 
HETATM 8835  C  C4  . PEG M  4 .   ? -11.025 -30.180 23.094  1.00 32.06 ? 303 PEG B C4  1 
HETATM 8836  O  O4  . PEG M  4 .   ? -10.817 -30.118 21.655  1.00 25.86 ? 303 PEG B O4  1 
HETATM 8837  C  C1  . EDO N  5 .   ? -3.326  -10.437 15.359  1.00 19.59 ? 304 EDO B C1  1 
HETATM 8838  O  O1  . EDO N  5 .   ? -4.478  -9.888  15.956  1.00 20.26 ? 304 EDO B O1  1 
HETATM 8839  C  C2  . EDO N  5 .   ? -2.299  -10.450 16.486  1.00 15.65 ? 304 EDO B C2  1 
HETATM 8840  O  O2  . EDO N  5 .   ? -2.631  -11.546 17.348  1.00 18.82 ? 304 EDO B O2  1 
HETATM 8841  C  C1  . EDO O  5 .   ? -3.301  -11.715 21.384  1.00 31.98 ? 305 EDO B C1  1 
HETATM 8842  O  O1  . EDO O  5 .   ? -4.676  -11.424 21.443  1.00 18.95 ? 305 EDO B O1  1 
HETATM 8843  C  C2  . EDO O  5 .   ? -2.563  -10.468 21.098  1.00 32.15 ? 305 EDO B C2  1 
HETATM 8844  O  O2  . EDO O  5 .   ? -2.991  -10.121 19.808  1.00 22.69 ? 305 EDO B O2  1 
HETATM 8845  C  C1  . EDO P  5 .   ? 0.628   -17.718 25.420  1.00 12.66 ? 306 EDO B C1  1 
HETATM 8846  O  O1  . EDO P  5 .   ? 0.873   -18.925 24.758  1.00 12.70 ? 306 EDO B O1  1 
HETATM 8847  C  C2  . EDO P  5 .   ? 1.772   -17.296 26.379  1.00 11.45 ? 306 EDO B C2  1 
HETATM 8848  O  O2  . EDO P  5 .   ? 3.059   -17.096 25.686  1.00 10.56 ? 306 EDO B O2  1 
HETATM 8849  C  C1  . EDO Q  5 .   ? 21.126  -14.334 23.418  1.00 25.61 ? 307 EDO B C1  1 
HETATM 8850  O  O1  . EDO Q  5 .   ? 21.612  -15.625 23.734  1.00 37.72 ? 307 EDO B O1  1 
HETATM 8851  C  C2  . EDO Q  5 .   ? 21.133  -13.351 24.545  1.00 35.64 ? 307 EDO B C2  1 
HETATM 8852  O  O2  . EDO Q  5 .   ? 20.921  -12.114 23.934  1.00 36.09 ? 307 EDO B O2  1 
HETATM 8853  C  C1  . EDO R  5 .   ? -2.337  -29.004 28.295  1.00 29.32 ? 308 EDO B C1  1 
HETATM 8854  O  O1  . EDO R  5 .   ? -2.814  -30.091 27.593  1.00 21.63 ? 308 EDO B O1  1 
HETATM 8855  C  C2  . EDO R  5 .   ? -0.873  -28.786 28.018  1.00 31.85 ? 308 EDO B C2  1 
HETATM 8856  O  O2  . EDO R  5 .   ? -0.776  -28.193 26.730  1.00 33.24 ? 308 EDO B O2  1 
HETATM 8857  ZN ZN  . ZN  S  2 .   ? 26.032  20.464  33.509  1.00 5.18  ? 301 ZN  C ZN  1 
HETATM 8858  F  F13 . V50 T  3 .   ? 23.459  21.223  37.845  1.00 10.35 ? 302 V50 C F13 1 
HETATM 8859  C  C4  . V50 T  3 .   ? 23.327  22.484  37.311  1.00 10.04 ? 302 V50 C C4  1 
HETATM 8860  C  C5  . V50 T  3 .   ? 23.357  22.659  35.895  1.00 10.28 ? 302 V50 C C5  1 
HETATM 8861  S  S7  . V50 T  3 .   ? 23.380  21.146  34.832  1.00 7.71  ? 302 V50 C S7  1 
HETATM 8862  O  O9  . V50 T  3 .   ? 23.225  21.649  33.452  1.00 7.94  ? 302 V50 C O9  1 
HETATM 8863  N  N23 . V50 T  3 .   ? 24.795  20.542  35.108  1.00 7.02  ? 302 V50 C N23 1 
HETATM 8864  O  O8  . V50 T  3 .   ? 22.317  20.288  35.365  1.00 6.92  ? 302 V50 C O8  1 
HETATM 8865  C  C6  . V50 T  3 .   ? 23.299  24.040  35.574  1.00 11.86 ? 302 V50 C C6  1 
HETATM 8866  F  F11 . V50 T  3 .   ? 23.303  24.325  34.299  1.00 12.50 ? 302 V50 C F11 1 
HETATM 8867  C  C1  . V50 T  3 .   ? 23.161  25.080  36.456  1.00 13.65 ? 302 V50 C C1  1 
HETATM 8868  F  F10 . V50 T  3 .   ? 23.126  26.362  35.995  1.00 14.93 ? 302 V50 C F10 1 
HETATM 8869  C  C3  . V50 T  3 .   ? 23.168  23.509  38.255  1.00 13.29 ? 302 V50 C C3  1 
HETATM 8870  F  F12 . V50 T  3 .   ? 23.035  23.218  39.587  1.00 11.32 ? 302 V50 C F12 1 
HETATM 8871  C  C2  . V50 T  3 .   ? 23.093  24.841  37.823  1.00 11.68 ? 302 V50 C C2  1 
HETATM 8872  S  S14 . V50 T  3 .   ? 22.995  26.129  39.072  1.00 13.13 ? 302 V50 C S14 1 
HETATM 8873  C  C15 . V50 T  3 .   ? 21.632  27.093  38.543  1.00 16.76 ? 302 V50 C C15 1 
HETATM 8874  N  N20 . V50 T  3 .   ? 20.898  26.754  37.507  1.00 15.82 ? 302 V50 C N20 1 
HETATM 8875  C  C19 . V50 T  3 .   ? 19.890  27.628  37.192  1.00 21.57 ? 302 V50 C C19 1 
HETATM 8876  C  C21 . V50 T  3 .   ? 19.129  27.221  35.947  1.00 21.01 ? 302 V50 C C21 1 
HETATM 8877  C  C18 . V50 T  3 .   ? 19.619  28.805  37.874  1.00 20.23 ? 302 V50 C C18 1 
HETATM 8878  C  C17 . V50 T  3 .   ? 20.467  28.995  38.933  1.00 19.50 ? 302 V50 C C17 1 
HETATM 8879  N  N16 . V50 T  3 .   ? 21.453  28.175  39.307  1.00 19.63 ? 302 V50 C N16 1 
HETATM 8880  C  C22 . V50 T  3 .   ? 20.255  30.245  39.837  1.00 23.16 ? 302 V50 C C22 1 
HETATM 8881  C  C1  . EDO U  5 .   ? 26.674  24.370  36.087  1.00 24.15 ? 303 EDO C C1  1 
HETATM 8882  O  O1  . EDO U  5 .   ? 26.610  25.702  35.620  1.00 23.73 ? 303 EDO C O1  1 
HETATM 8883  C  C2  . EDO U  5 .   ? 28.144  23.981  36.284  1.00 22.58 ? 303 EDO C C2  1 
HETATM 8884  O  O2  . EDO U  5 .   ? 28.693  24.855  37.269  1.00 23.88 ? 303 EDO C O2  1 
HETATM 8885  ZN ZN  . ZN  V  2 .   ? 27.746  -6.717  50.724  1.00 4.61  ? 301 ZN  D ZN  1 
HETATM 8886  F  F13 . V50 W  3 .   ? 29.055  -7.325  55.279  1.00 10.00 ? 302 V50 D F13 1 
HETATM 8887  C  C4  . V50 W  3 .   ? 28.775  -6.006  55.502  1.00 7.43  ? 302 V50 D C4  1 
HETATM 8888  C  C5  . V50 W  3 .   ? 28.855  -5.085  54.474  1.00 6.61  ? 302 V50 D C5  1 
HETATM 8889  S  S7  . V50 W  3 .   ? 29.514  -5.319  52.805  1.00 7.15  ? 302 V50 D S7  1 
HETATM 8890  O  O9  . V50 W  3 .   ? 29.963  -6.712  52.793  1.00 7.77  ? 302 V50 D O9  1 
HETATM 8891  N  N23 . V50 W  3 .   ? 28.266  -5.154  51.852  1.00 6.17  ? 302 V50 D N23 1 
HETATM 8892  O  O8  . V50 W  3 .   ? 30.512  -4.270  52.628  1.00 5.66  ? 302 V50 D O8  1 
HETATM 8893  C  C6  . V50 W  3 .   ? 28.475  -3.763  54.812  1.00 7.70  ? 302 V50 D C6  1 
HETATM 8894  F  F11 . V50 W  3 .   ? 28.522  -2.738  53.940  1.00 7.67  ? 302 V50 D F11 1 
HETATM 8895  C  C1  . V50 W  3 .   ? 28.195  -3.387  56.125  1.00 9.46  ? 302 V50 D C1  1 
HETATM 8896  F  F10 . V50 W  3 .   ? 27.920  -2.122  56.454  1.00 9.09  ? 302 V50 D F10 1 
HETATM 8897  C  C3  . V50 W  3 .   ? 28.362  -5.666  56.756  1.00 8.65  ? 302 V50 D C3  1 
HETATM 8898  F  F12 . V50 W  3 .   ? 28.210  -6.634  57.672  1.00 10.66 ? 302 V50 D F12 1 
HETATM 8899  C  C2  . V50 W  3 .   ? 28.021  -4.333  57.104  1.00 7.93  ? 302 V50 D C2  1 
HETATM 8900  S  S14 . V50 W  3 .   ? 27.510  -3.832  58.752  1.00 10.42 ? 302 V50 D S14 1 
HETATM 8901  C  C15 . V50 W  3 .   ? 28.673  -4.552  59.864  1.00 12.25 ? 302 V50 D C15 1 
HETATM 8902  N  N20 . V50 W  3 .   ? 29.725  -5.257  59.444  1.00 10.56 ? 302 V50 D N20 1 
HETATM 8903  C  C19 . V50 W  3 .   ? 30.549  -5.799  60.408  1.00 11.74 ? 302 V50 D C19 1 
HETATM 8904  C  C21 . V50 W  3 .   ? 31.713  -6.558  59.936  1.00 13.71 ? 302 V50 D C21 1 
HETATM 8905  C  C18 . V50 W  3 .   ? 30.265  -5.726  61.741  1.00 11.85 ? 302 V50 D C18 1 
HETATM 8906  C  C17 . V50 W  3 .   ? 29.132  -4.991  62.043  1.00 12.41 ? 302 V50 D C17 1 
HETATM 8907  N  N16 . V50 W  3 .   ? 28.299  -4.406  61.136  1.00 13.57 ? 302 V50 D N16 1 
HETATM 8908  C  C22 . V50 W  3 .   ? 28.754  -4.727  63.494  1.00 17.36 ? 302 V50 D C22 1 
HETATM 8909  C  C1  . PEG X  4 .   ? 10.979  -17.426 40.861  1.00 29.36 ? 303 PEG D C1  1 
HETATM 8910  O  O1  . PEG X  4 .   ? 11.606  -18.407 40.043  1.00 17.96 ? 303 PEG D O1  1 
HETATM 8911  C  C2  . PEG X  4 .   ? 9.817   -17.959 41.713  1.00 21.11 ? 303 PEG D C2  1 
HETATM 8912  O  O2  . PEG X  4 .   ? 9.811   -17.493 43.101  1.00 35.46 ? 303 PEG D O2  1 
HETATM 8913  C  C3  . PEG X  4 .   ? 10.026  -18.366 44.276  1.00 21.29 ? 303 PEG D C3  1 
HETATM 8914  C  C4  . PEG X  4 .   ? 9.001   -18.002 45.389  1.00 38.26 ? 303 PEG D C4  1 
HETATM 8915  O  O4  . PEG X  4 .   ? 7.645   -18.566 45.398  1.00 36.96 ? 303 PEG D O4  1 
HETATM 8916  C  C1  . EDO Y  5 .   ? 24.214  -6.403  53.813  1.00 20.54 ? 304 EDO D C1  1 
HETATM 8917  O  O1  . EDO Y  5 .   ? 23.222  -5.759  54.635  1.00 19.33 ? 304 EDO D O1  1 
HETATM 8918  C  C2  . EDO Y  5 .   ? 25.458  -6.532  54.706  1.00 19.55 ? 304 EDO D C2  1 
HETATM 8919  O  O2  . EDO Y  5 .   ? 25.215  -7.477  55.755  1.00 18.97 ? 304 EDO D O2  1 
HETATM 8920  C  C1  A EDO Z  5 .   ? 24.814  -7.316  59.856  0.50 13.58 ? 305 EDO D C1  1 
HETATM 8921  C  C1  B EDO Z  5 .   ? 24.285  -7.036  59.037  0.50 20.90 ? 305 EDO D C1  1 
HETATM 8922  O  O1  A EDO Z  5 .   ? 25.221  -6.630  58.684  0.50 17.50 ? 305 EDO D O1  1 
HETATM 8923  O  O1  B EDO Z  5 .   ? 24.582  -6.175  57.984  0.50 13.31 ? 305 EDO D O1  1 
HETATM 8924  C  C2  A EDO Z  5 .   ? 23.318  -7.639  59.612  0.50 8.42  ? 305 EDO D C2  1 
HETATM 8925  C  C2  B EDO Z  5 .   ? 24.627  -6.396  60.373  0.50 22.40 ? 305 EDO D C2  1 
HETATM 8926  O  O2  A EDO Z  5 .   ? 22.451  -7.265  60.563  0.50 17.96 ? 305 EDO D O2  1 
HETATM 8927  O  O2  B EDO Z  5 .   ? 25.907  -6.784  60.756  0.50 21.48 ? 305 EDO D O2  1 
HETATM 8928  C  C1  . EDO AA 5 .   ? 12.727  -25.360 52.889  1.00 29.87 ? 306 EDO D C1  1 
HETATM 8929  O  O1  . EDO AA 5 .   ? 11.377  -25.019 53.014  1.00 21.89 ? 306 EDO D O1  1 
HETATM 8930  C  C2  . EDO AA 5 .   ? 13.384  -24.228 53.570  1.00 14.76 ? 306 EDO D C2  1 
HETATM 8931  O  O2  . EDO AA 5 .   ? 14.343  -24.630 54.371  1.00 34.10 ? 306 EDO D O2  1 
HETATM 8932  O  O   . HOH BA 6 .   ? -2.712  8.206   4.772   1.00 5.22  ? 401 HOH A O   1 
HETATM 8933  O  O   . HOH BA 6 .   ? -2.203  5.453   11.571  1.00 6.02  ? 402 HOH A O   1 
HETATM 8934  O  O   . HOH BA 6 .   ? -2.203  2.952   2.839   1.00 5.63  ? 403 HOH A O   1 
HETATM 8935  O  O   . HOH BA 6 .   ? -1.729  5.719   3.462   1.00 6.65  ? 404 HOH A O   1 
HETATM 8936  O  O   . HOH BA 6 .   ? 9.844   3.909   -28.509 1.00 9.84  ? 405 HOH A O   1 
HETATM 8937  O  O   . HOH BA 6 .   ? 0.969   4.162   -4.104  1.00 5.78  ? 406 HOH A O   1 
HETATM 8938  O  O   . HOH BA 6 .   ? 5.039   -0.108  -1.037  1.00 11.59 ? 407 HOH A O   1 
HETATM 8939  O  O   . HOH BA 6 .   ? 4.263   8.866   4.196   1.00 7.16  ? 408 HOH A O   1 
HETATM 8940  O  O   . HOH BA 6 .   ? -6.962  2.228   3.772   1.00 8.15  ? 409 HOH A O   1 
HETATM 8941  O  O   . HOH BA 6 .   ? 1.513   4.202   4.983   1.00 6.22  ? 410 HOH A O   1 
HETATM 8942  O  O   . HOH BA 6 .   ? -9.163  6.075   5.822   1.00 10.25 ? 411 HOH A O   1 
HETATM 8943  O  O   . HOH BA 6 .   ? -3.723  -0.040  -17.277 1.00 11.46 ? 412 HOH A O   1 
HETATM 8944  O  O   . HOH BA 6 .   ? -6.262  -0.639  -3.196  1.00 10.66 ? 413 HOH A O   1 
HETATM 8945  O  O   . HOH BA 6 .   ? -22.781 3.391   -24.664 1.00 13.68 ? 414 HOH A O   1 
HETATM 8946  O  O   . HOH BA 6 .   ? 9.441   2.821   -15.312 1.00 9.17  ? 415 HOH A O   1 
HETATM 8947  O  O   . HOH BA 6 .   ? -8.266  4.574   3.540   1.00 7.69  ? 416 HOH A O   1 
HETATM 8948  O  O   . HOH BA 6 .   ? -21.705 -1.896  -19.541 1.00 10.09 ? 417 HOH A O   1 
HETATM 8949  O  O   . HOH BA 6 .   ? -3.452  9.225   8.481   1.00 7.63  ? 418 HOH A O   1 
HETATM 8950  O  O   . HOH BA 6 .   ? -9.610  5.791   10.035  1.00 13.37 ? 419 HOH A O   1 
HETATM 8951  O  O   . HOH BA 6 .   ? 1.204   1.893   -2.502  1.00 12.57 ? 420 HOH A O   1 
HETATM 8952  O  O   . HOH BA 6 .   ? -11.332 -2.350  -24.940 1.00 10.98 ? 421 HOH A O   1 
HETATM 8953  O  O   . HOH BA 6 .   ? -1.969  3.979   7.396   1.00 10.94 ? 422 HOH A O   1 
HETATM 8954  O  O   . HOH BA 6 .   ? -0.424  -1.825  -5.117  1.00 16.30 ? 423 HOH A O   1 
HETATM 8955  O  O   . HOH BA 6 .   ? 14.426  7.260   -0.375  1.00 14.97 ? 424 HOH A O   1 
HETATM 8956  O  O   . HOH BA 6 .   ? -5.181  0.629   -25.307 1.00 14.94 ? 425 HOH A O   1 
HETATM 8957  O  O   . HOH BA 6 .   ? 3.602   7.728   8.530   1.00 14.27 ? 426 HOH A O   1 
HETATM 8958  O  O   . HOH BA 6 .   ? 17.081  4.302   -20.402 1.00 12.85 ? 427 HOH A O   1 
HETATM 8959  O  O   . HOH BA 6 .   ? -11.740 -0.887  -28.850 1.00 14.00 ? 428 HOH A O   1 
HETATM 8960  O  O   . HOH BA 6 .   ? -8.497  -3.371  -0.439  1.00 14.61 ? 429 HOH A O   1 
HETATM 8961  O  O   . HOH BA 6 .   ? -12.955 1.897   -25.059 1.00 14.15 ? 430 HOH A O   1 
HETATM 8962  O  O   . HOH BA 6 .   ? -12.720 -3.477  -29.074 1.00 13.63 ? 431 HOH A O   1 
HETATM 8963  O  O   . HOH BA 6 .   ? -6.294  -3.405  -15.928 1.00 21.38 ? 432 HOH A O   1 
HETATM 8964  O  O   . HOH BA 6 .   ? -6.068  -9.847  -7.840  1.00 17.56 ? 433 HOH A O   1 
HETATM 8965  O  O   . HOH BA 6 .   ? -10.817 3.813   -0.596  1.00 13.34 ? 434 HOH A O   1 
HETATM 8966  O  O   . HOH BA 6 .   ? -12.416 -4.360  -26.391 1.00 14.79 ? 435 HOH A O   1 
HETATM 8967  O  O   . HOH BA 6 .   ? -4.764  -8.449  -5.790  1.00 15.71 ? 436 HOH A O   1 
HETATM 8968  O  O   . HOH BA 6 .   ? -16.576 4.401   -7.334  1.00 14.88 ? 437 HOH A O   1 
HETATM 8969  O  O   . HOH BA 6 .   ? -19.743 -5.196  -17.371 1.00 16.63 ? 438 HOH A O   1 
HETATM 8970  O  O   . HOH BA 6 .   ? 11.170  3.472   -13.113 1.00 15.17 ? 439 HOH A O   1 
HETATM 8971  O  O   . HOH BA 6 .   ? -6.274  -7.364  -3.862  1.00 20.37 ? 440 HOH A O   1 
HETATM 8972  O  O   . HOH BA 6 .   ? 5.230   6.981   5.796   1.00 14.52 ? 441 HOH A O   1 
HETATM 8973  O  O   . HOH BA 6 .   ? 9.586   4.473   -4.329  1.00 12.52 ? 442 HOH A O   1 
HETATM 8974  O  O   . HOH BA 6 .   ? 5.846   2.357   -1.574  1.00 17.17 ? 443 HOH A O   1 
HETATM 8975  O  O   . HOH BA 6 .   ? 17.695  5.608   -10.761 1.00 19.10 ? 444 HOH A O   1 
HETATM 8976  O  O   . HOH BA 6 .   ? -11.059 4.853   2.402   1.00 14.85 ? 445 HOH A O   1 
HETATM 8977  O  O   . HOH BA 6 .   ? 6.975   2.293   -14.689 1.00 16.70 ? 446 HOH A O   1 
HETATM 8978  O  O   . HOH BA 6 .   ? -14.757 4.023   1.697   1.00 15.93 ? 447 HOH A O   1 
HETATM 8979  O  O   . HOH BA 6 .   ? -13.673 -7.927  -23.513 1.00 15.99 ? 448 HOH A O   1 
HETATM 8980  O  O   . HOH BA 6 .   ? 6.125   -1.979  -9.534  1.00 21.49 ? 449 HOH A O   1 
HETATM 8981  O  O   . HOH BA 6 .   ? -1.027  -1.266  -17.052 1.00 25.77 ? 450 HOH A O   1 
HETATM 8982  O  O   . HOH BA 6 .   ? -5.480  -7.527  -11.774 1.00 18.98 ? 451 HOH A O   1 
HETATM 8983  O  O   . HOH BA 6 .   ? 1.921   27.381  -9.675  1.00 11.99 ? 452 HOH A O   1 
HETATM 8984  O  O   . HOH BA 6 .   ? 10.082  7.609   -9.296  1.00 6.71  ? 453 HOH A O   1 
HETATM 8985  O  O   . HOH BA 6 .   ? -11.965 12.835  -13.603 1.00 7.64  ? 454 HOH A O   1 
HETATM 8986  O  O   . HOH BA 6 .   ? -2.285  6.859   -17.639 1.00 7.03  ? 455 HOH A O   1 
HETATM 8987  O  O   . HOH BA 6 .   ? -5.345  5.584   -22.093 1.00 8.13  ? 456 HOH A O   1 
HETATM 8988  O  O   . HOH BA 6 .   ? 15.624  7.110   -11.586 1.00 12.46 ? 457 HOH A O   1 
HETATM 8989  O  O   . HOH BA 6 .   ? 18.962  14.161  -15.350 1.00 11.36 ? 458 HOH A O   1 
HETATM 8990  O  O   . HOH BA 6 .   ? 15.792  6.648   -21.238 1.00 8.46  ? 459 HOH A O   1 
HETATM 8991  O  O   . HOH BA 6 .   ? 8.054   9.809   -24.849 1.00 6.91  ? 460 HOH A O   1 
HETATM 8992  O  O   . HOH BA 6 .   ? 8.652   25.619  -21.246 1.00 10.53 ? 461 HOH A O   1 
HETATM 8993  O  O   . HOH BA 6 .   ? 20.372  19.777  -6.278  1.00 18.48 ? 462 HOH A O   1 
HETATM 8994  O  O   . HOH BA 6 .   ? 13.182  29.180  -1.363  1.00 18.51 ? 463 HOH A O   1 
HETATM 8995  O  O   . HOH BA 6 .   ? -0.100  12.202  -2.170  1.00 6.04  ? 464 HOH A O   1 
HETATM 8996  O  O   . HOH BA 6 .   ? -9.405  16.578  6.550   1.00 11.08 ? 465 HOH A O   1 
HETATM 8997  O  O   . HOH BA 6 .   ? 15.445  15.696  -4.644  1.00 11.67 ? 466 HOH A O   1 
HETATM 8998  O  O   . HOH BA 6 .   ? -10.509 -8.694  -27.336 1.00 21.01 ? 467 HOH A O   1 
HETATM 8999  O  O   . HOH BA 6 .   ? -12.183 5.484   -3.070  1.00 16.17 ? 468 HOH A O   1 
HETATM 9000  O  O   . HOH BA 6 .   ? -18.670 5.101   -4.130  1.00 25.58 ? 469 HOH A O   1 
HETATM 9001  O  O   . HOH BA 6 .   ? -7.861  -10.047 -26.927 1.00 22.25 ? 470 HOH A O   1 
HETATM 9002  O  O   . HOH BA 6 .   ? -8.732  1.795   6.100   1.00 17.40 ? 471 HOH A O   1 
HETATM 9003  O  O   . HOH BA 6 .   ? -4.358  -2.073  -19.293 1.00 21.45 ? 472 HOH A O   1 
HETATM 9004  O  O   . HOH BA 6 .   ? -5.057  -4.849  -4.423  1.00 21.67 ? 473 HOH A O   1 
HETATM 9005  O  O   . HOH BA 6 .   ? 6.771   16.488  -0.857  1.00 9.77  ? 474 HOH A O   1 
HETATM 9006  O  O   . HOH BA 6 .   ? -11.531 10.317  -22.707 1.00 13.03 ? 475 HOH A O   1 
HETATM 9007  O  O   . HOH BA 6 .   ? -14.903 6.100   -23.756 1.00 11.90 ? 476 HOH A O   1 
HETATM 9008  O  O   . HOH BA 6 .   ? -9.838  10.502  10.835  1.00 11.52 ? 477 HOH A O   1 
HETATM 9009  O  O   . HOH BA 6 .   ? -12.806 11.026  3.943   1.00 8.90  ? 478 HOH A O   1 
HETATM 9010  O  O   . HOH BA 6 .   ? 8.677   14.589  -0.373  1.00 10.23 ? 479 HOH A O   1 
HETATM 9011  O  O   . HOH BA 6 .   ? 12.046  14.081  2.088   1.00 14.10 ? 480 HOH A O   1 
HETATM 9012  O  O   . HOH BA 6 .   ? 13.225  16.229  -6.744  1.00 9.07  ? 481 HOH A O   1 
HETATM 9013  O  O   . HOH BA 6 .   ? 16.640  23.742  1.329   1.00 17.47 ? 482 HOH A O   1 
HETATM 9014  O  O   . HOH BA 6 .   ? 10.365  14.653  6.424   1.00 17.74 ? 483 HOH A O   1 
HETATM 9015  O  O   . HOH BA 6 .   ? 1.362   10.657  -25.311 1.00 16.55 ? 484 HOH A O   1 
HETATM 9016  O  O   . HOH BA 6 .   ? 11.251  9.470   1.785   1.00 11.66 ? 485 HOH A O   1 
HETATM 9017  O  O   . HOH BA 6 .   ? 7.670   14.446  9.017   1.00 14.16 ? 486 HOH A O   1 
HETATM 9018  O  O   . HOH BA 6 .   ? 3.009   12.358  -23.690 1.00 12.78 ? 487 HOH A O   1 
HETATM 9019  O  O   . HOH BA 6 .   ? -18.775 8.605   -13.860 1.00 15.14 ? 488 HOH A O   1 
HETATM 9020  O  O   . HOH BA 6 .   ? -24.534 21.505  -5.246  1.00 20.63 ? 489 HOH A O   1 
HETATM 9021  O  O   . HOH BA 6 .   ? 0.469   6.140   -24.302 1.00 12.79 ? 490 HOH A O   1 
HETATM 9022  O  O   . HOH BA 6 .   ? 10.193  12.049  1.439   1.00 14.37 ? 491 HOH A O   1 
HETATM 9023  O  O   . HOH BA 6 .   ? -10.743 11.038  -25.352 1.00 19.96 ? 492 HOH A O   1 
HETATM 9024  O  O   . HOH BA 6 .   ? 12.392  25.597  4.645   1.00 19.93 ? 493 HOH A O   1 
HETATM 9025  O  O   . HOH BA 6 .   ? 4.582   8.543   -24.219 1.00 13.83 ? 494 HOH A O   1 
HETATM 9026  O  O   . HOH BA 6 .   ? 7.909   14.976  2.374   1.00 15.20 ? 495 HOH A O   1 
HETATM 9027  O  O   . HOH BA 6 .   ? -8.323  19.382  11.983  1.00 20.56 ? 496 HOH A O   1 
HETATM 9028  O  O   . HOH BA 6 .   ? 10.235  15.436  3.714   1.00 13.56 ? 497 HOH A O   1 
HETATM 9029  O  O   . HOH BA 6 .   ? 2.418   16.179  -3.181  1.00 13.57 ? 498 HOH A O   1 
HETATM 9030  O  O   . HOH BA 6 .   ? -15.731 9.704   5.886   1.00 20.35 ? 499 HOH A O   1 
HETATM 9031  O  O   . HOH BA 6 .   ? 10.422  20.278  -25.505 1.00 15.10 ? 500 HOH A O   1 
HETATM 9032  O  O   . HOH BA 6 .   ? -15.937 11.053  -4.097  1.00 15.33 ? 501 HOH A O   1 
HETATM 9033  O  O   . HOH BA 6 .   ? -10.941 22.020  1.115   1.00 27.32 ? 502 HOH A O   1 
HETATM 9034  O  O   . HOH BA 6 .   ? 16.676  12.770  -21.964 1.00 16.04 ? 503 HOH A O   1 
HETATM 9035  O  O   . HOH BA 6 .   ? -24.040 2.006   -16.976 1.00 23.94 ? 504 HOH A O   1 
HETATM 9036  O  O   . HOH BA 6 .   ? -5.040  28.505  -11.457 1.00 26.51 ? 505 HOH A O   1 
HETATM 9037  O  O   . HOH BA 6 .   ? -7.915  28.516  -13.118 1.00 21.05 ? 506 HOH A O   1 
HETATM 9038  O  O   . HOH BA 6 .   ? -14.380 12.830  5.335   1.00 14.73 ? 507 HOH A O   1 
HETATM 9039  O  O   . HOH BA 6 .   ? 2.139   7.989   -25.183 1.00 14.82 ? 508 HOH A O   1 
HETATM 9040  O  O   . HOH BA 6 .   ? -11.960 13.227  -26.745 1.00 23.02 ? 509 HOH A O   1 
HETATM 9041  O  O   . HOH BA 6 .   ? 7.190   19.240  2.869   1.00 14.66 ? 510 HOH A O   1 
HETATM 9042  O  O   . HOH BA 6 .   ? -8.681  -3.107  -25.375 1.00 20.42 ? 511 HOH A O   1 
HETATM 9043  O  O   . HOH BA 6 .   ? -3.915  11.318  -26.705 1.00 21.41 ? 512 HOH A O   1 
HETATM 9044  O  O   . HOH BA 6 .   ? -16.723 13.985  4.276   1.00 25.44 ? 513 HOH A O   1 
HETATM 9045  O  O   . HOH BA 6 .   ? 20.555  22.245  -0.932  1.00 30.71 ? 514 HOH A O   1 
HETATM 9046  O  O   . HOH BA 6 .   ? -17.506 17.592  -17.796 1.00 15.63 ? 515 HOH A O   1 
HETATM 9047  O  O   . HOH BA 6 .   ? -10.308 23.514  -27.532 1.00 29.33 ? 516 HOH A O   1 
HETATM 9048  O  O   . HOH BA 6 .   ? 5.969   0.480   -16.504 1.00 22.31 ? 517 HOH A O   1 
HETATM 9049  O  O   . HOH BA 6 .   ? -11.279 9.507   -27.870 1.00 25.48 ? 518 HOH A O   1 
HETATM 9050  O  O   . HOH BA 6 .   ? -1.593  13.074  -26.410 1.00 19.85 ? 519 HOH A O   1 
HETATM 9051  O  O   . HOH BA 6 .   ? 4.249   -2.073  -6.521  1.00 17.64 ? 520 HOH A O   1 
HETATM 9052  O  O   . HOH BA 6 .   ? 13.313  25.762  -20.305 1.00 27.47 ? 521 HOH A O   1 
HETATM 9053  O  O   . HOH BA 6 .   ? -21.049 -1.536  -15.323 1.00 24.47 ? 522 HOH A O   1 
HETATM 9054  O  O   . HOH BA 6 .   ? 12.010  14.012  11.763  1.00 27.32 ? 523 HOH A O   1 
HETATM 9055  O  O   . HOH BA 6 .   ? -11.549 -2.528  4.801   1.00 25.07 ? 524 HOH A O   1 
HETATM 9056  O  O   . HOH BA 6 .   ? -21.060 22.633  -20.452 1.00 22.11 ? 525 HOH A O   1 
HETATM 9057  O  O   . HOH BA 6 .   ? -7.792  31.640  -14.998 1.00 25.37 ? 526 HOH A O   1 
HETATM 9058  O  O   . HOH BA 6 .   ? 5.796   20.189  4.957   1.00 17.80 ? 527 HOH A O   1 
HETATM 9059  O  O   . HOH BA 6 .   ? -10.939 19.657  11.122  1.00 24.43 ? 528 HOH A O   1 
HETATM 9060  O  O   . HOH BA 6 .   ? -8.828  -3.384  -3.163  1.00 27.74 ? 529 HOH A O   1 
HETATM 9061  O  O   . HOH BA 6 .   ? -23.308 7.115   -22.226 1.00 28.02 ? 530 HOH A O   1 
HETATM 9062  O  O   . HOH BA 6 .   ? 11.270  22.218  -23.742 1.00 25.06 ? 531 HOH A O   1 
HETATM 9063  O  O   . HOH BA 6 .   ? 6.935   -5.184  -8.366  1.00 24.10 ? 532 HOH A O   1 
HETATM 9064  O  O   . HOH BA 6 .   ? 5.698   15.018  -26.644 1.00 19.15 ? 533 HOH A O   1 
HETATM 9065  O  O   . HOH BA 6 .   ? 17.055  12.264  -5.015  1.00 17.81 ? 534 HOH A O   1 
HETATM 9066  O  O   . HOH BA 6 .   ? 0.246   37.007  -31.995 1.00 27.69 ? 535 HOH A O   1 
HETATM 9067  O  O   . HOH BA 6 .   ? -20.216 18.249  -19.651 1.00 24.46 ? 536 HOH A O   1 
HETATM 9068  O  O   . HOH BA 6 .   ? 7.972   7.870   7.387   1.00 21.26 ? 537 HOH A O   1 
HETATM 9069  O  O   . HOH BA 6 .   ? 2.750   22.181  -27.489 1.00 21.81 ? 538 HOH A O   1 
HETATM 9070  O  O   . HOH BA 6 .   ? 3.883   4.321   -23.009 1.00 20.97 ? 539 HOH A O   1 
HETATM 9071  O  O   . HOH BA 6 .   ? -1.016  -3.879  -16.631 1.00 22.40 ? 540 HOH A O   1 
HETATM 9072  O  O   . HOH BA 6 .   ? -12.744 5.423   7.477   1.00 20.68 ? 541 HOH A O   1 
HETATM 9073  O  O   . HOH BA 6 .   ? 0.689   35.738  -19.759 1.00 20.97 ? 542 HOH A O   1 
HETATM 9074  O  O   . HOH BA 6 .   ? -6.910  24.425  -7.149  1.00 22.86 ? 543 HOH A O   1 
HETATM 9075  O  O   . HOH BA 6 .   ? -6.259  12.421  -26.436 1.00 25.59 ? 544 HOH A O   1 
HETATM 9076  O  O   . HOH BA 6 .   ? 0.272   3.461   -25.250 1.00 22.05 ? 545 HOH A O   1 
HETATM 9077  O  O   . HOH BA 6 .   ? -12.529 17.007  3.893   1.00 28.74 ? 546 HOH A O   1 
HETATM 9078  O  O   . HOH BA 6 .   ? 2.042   13.631  13.653  1.00 26.25 ? 547 HOH A O   1 
HETATM 9079  O  O   . HOH BA 6 .   ? -9.268  32.024  -19.116 1.00 25.43 ? 548 HOH A O   1 
HETATM 9080  O  O   . HOH BA 6 .   ? 6.947   24.043  -29.277 1.00 28.92 ? 549 HOH A O   1 
HETATM 9081  O  O   . HOH BA 6 .   ? 5.399   22.757  2.377   1.00 24.10 ? 550 HOH A O   1 
HETATM 9082  O  O   . HOH BA 6 .   ? -11.004 28.325  -8.456  1.00 37.10 ? 551 HOH A O   1 
HETATM 9083  O  O   . HOH BA 6 .   ? 16.371  14.797  2.324   1.00 20.34 ? 552 HOH A O   1 
HETATM 9084  O  O   . HOH BA 6 .   ? -9.105  7.852   -27.590 1.00 17.58 ? 553 HOH A O   1 
HETATM 9085  O  O   . HOH BA 6 .   ? -25.747 17.029  -17.856 1.00 27.52 ? 554 HOH A O   1 
HETATM 9086  O  O   . HOH BA 6 .   ? 19.117  24.653  1.574   1.00 32.50 ? 555 HOH A O   1 
HETATM 9087  O  O   . HOH BA 6 .   ? 7.659   9.074   1.347   1.00 18.44 ? 556 HOH A O   1 
HETATM 9088  O  O   . HOH BA 6 .   ? 7.530   5.904   -26.565 1.00 25.36 ? 557 HOH A O   1 
HETATM 9089  O  O   . HOH BA 6 .   ? -16.497 0.428   1.356   1.00 27.58 ? 558 HOH A O   1 
HETATM 9090  O  O   . HOH BA 6 .   ? -9.745  3.333   -27.911 1.00 25.69 ? 559 HOH A O   1 
HETATM 9091  O  O   . HOH BA 6 .   ? -4.461  7.645   -29.414 1.00 17.71 ? 560 HOH A O   1 
HETATM 9092  O  O   . HOH BA 6 .   ? -13.928 12.593  -28.665 1.00 23.11 ? 561 HOH A O   1 
HETATM 9093  O  O   . HOH BA 6 .   ? 2.939   7.030   -27.782 1.00 23.38 ? 562 HOH A O   1 
HETATM 9094  O  O   . HOH BA 6 .   ? -6.635  9.270   -27.835 1.00 22.05 ? 563 HOH A O   1 
HETATM 9095  O  O   . HOH BA 6 .   ? 8.105   22.452  3.321   1.00 28.45 ? 564 HOH A O   1 
HETATM 9096  O  O   . HOH BA 6 .   ? -3.751  -1.204  -24.074 1.00 33.22 ? 565 HOH A O   1 
HETATM 9097  O  O   . HOH BA 6 .   ? -21.144 18.543  -7.143  1.00 25.32 ? 566 HOH A O   1 
HETATM 9098  O  O   . HOH BA 6 .   ? -10.651 28.285  -4.653  1.00 31.17 ? 567 HOH A O   1 
HETATM 9099  O  O   . HOH BA 6 .   ? 10.495  25.010  -23.310 1.00 21.57 ? 568 HOH A O   1 
HETATM 9100  O  O   . HOH BA 6 .   ? 19.551  17.408  -10.162 1.00 14.71 ? 569 HOH A O   1 
HETATM 9101  O  O   . HOH BA 6 .   ? 3.199   3.150   -28.043 1.00 28.19 ? 570 HOH A O   1 
HETATM 9102  O  O   . HOH BA 6 .   ? -12.867 -4.211  -16.743 1.00 23.54 ? 571 HOH A O   1 
HETATM 9103  O  O   . HOH BA 6 .   ? 6.630   15.369  -29.828 1.00 24.26 ? 572 HOH A O   1 
HETATM 9104  O  O   . HOH BA 6 .   ? 14.929  27.116  -18.340 1.00 33.63 ? 573 HOH A O   1 
HETATM 9105  O  O   . HOH BA 6 .   ? -7.708  -2.057  -4.719  1.00 18.60 ? 574 HOH A O   1 
HETATM 9106  O  O   . HOH BA 6 .   ? 2.655   21.349  5.210   1.00 27.83 ? 575 HOH A O   1 
HETATM 9107  O  O   . HOH BA 6 .   ? 17.696  2.469   -9.341  1.00 29.64 ? 576 HOH A O   1 
HETATM 9108  O  O   . HOH BA 6 .   ? 18.198  15.910  -4.482  1.00 21.82 ? 577 HOH A O   1 
HETATM 9109  O  O   . HOH BA 6 .   ? -18.145 12.401  -0.389  1.00 25.73 ? 578 HOH A O   1 
HETATM 9110  O  O   . HOH BA 6 .   ? 9.303   20.857  -28.402 1.00 33.99 ? 579 HOH A O   1 
HETATM 9111  O  O   . HOH BA 6 .   ? -9.447  -5.614  0.812   1.00 18.80 ? 580 HOH A O   1 
HETATM 9112  O  O   . HOH BA 6 .   ? 12.566  14.298  7.659   1.00 30.00 ? 581 HOH A O   1 
HETATM 9113  O  O   . HOH BA 6 .   ? 13.155  20.430  7.361   1.00 24.58 ? 582 HOH A O   1 
HETATM 9114  O  O   . HOH BA 6 .   ? 9.796   24.762  4.961   1.00 31.54 ? 583 HOH A O   1 
HETATM 9115  O  O   . HOH BA 6 .   ? -23.703 12.280  -13.877 1.00 28.94 ? 584 HOH A O   1 
HETATM 9116  O  O   . HOH BA 6 .   ? -25.520 17.540  -7.916  1.00 20.95 ? 585 HOH A O   1 
HETATM 9117  O  O   . HOH BA 6 .   ? 5.940   17.074  1.736   1.00 15.39 ? 586 HOH A O   1 
HETATM 9118  O  O   . HOH BA 6 .   ? 0.400   -3.851  -14.379 1.00 18.42 ? 587 HOH A O   1 
HETATM 9119  O  O   . HOH BA 6 .   ? 9.819   1.772   -21.188 1.00 22.47 ? 588 HOH A O   1 
HETATM 9120  O  O   . HOH BA 6 .   ? 7.527   0.791   -20.486 1.00 30.59 ? 589 HOH A O   1 
HETATM 9121  O  O   . HOH BA 6 .   ? 7.124   26.243  -25.408 1.00 17.25 ? 590 HOH A O   1 
HETATM 9122  O  O   . HOH BA 6 .   ? 5.501   27.926  -29.099 1.00 21.32 ? 591 HOH A O   1 
HETATM 9123  O  O   . HOH BA 6 .   ? -5.940  22.765  0.131   1.00 28.59 ? 592 HOH A O   1 
HETATM 9124  O  O   . HOH BA 6 .   ? 2.602   24.864  0.196   1.00 25.46 ? 593 HOH A O   1 
HETATM 9125  O  O   . HOH BA 6 .   ? -2.544  26.945  -7.872  1.00 30.07 ? 594 HOH A O   1 
HETATM 9126  O  O   . HOH BA 6 .   ? -1.301  15.594  10.955  1.00 21.62 ? 595 HOH A O   1 
HETATM 9127  O  O   . HOH BA 6 .   ? -13.531 0.438   0.952   1.00 27.13 ? 596 HOH A O   1 
HETATM 9128  O  O   . HOH BA 6 .   ? 6.709   33.900  -31.644 1.00 30.44 ? 597 HOH A O   1 
HETATM 9129  O  O   . HOH BA 6 .   ? 16.708  8.510   -1.675  1.00 27.71 ? 598 HOH A O   1 
HETATM 9130  O  O   . HOH BA 6 .   ? -11.232 1.379   5.442   1.00 25.69 ? 599 HOH A O   1 
HETATM 9131  O  O   . HOH BA 6 .   ? -16.014 -4.620  3.619   1.00 29.23 ? 600 HOH A O   1 
HETATM 9132  O  O   . HOH BA 6 .   ? 6.858   29.517  0.688   1.00 38.83 ? 601 HOH A O   1 
HETATM 9133  O  O   . HOH BA 6 .   ? 14.600  32.331  -4.173  1.00 28.34 ? 602 HOH A O   1 
HETATM 9134  O  O   . HOH BA 6 .   ? 18.594  27.731  -8.586  1.00 32.24 ? 603 HOH A O   1 
HETATM 9135  O  O   . HOH BA 6 .   ? -8.372  23.072  1.258   1.00 32.33 ? 604 HOH A O   1 
HETATM 9136  O  O   . HOH BA 6 .   ? 7.909   16.647  13.294  1.00 30.56 ? 605 HOH A O   1 
HETATM 9137  O  O   . HOH BA 6 .   ? 9.930   15.644  11.083  1.00 29.78 ? 606 HOH A O   1 
HETATM 9138  O  O   . HOH BA 6 .   ? 14.717  13.811  5.823   1.00 28.66 ? 607 HOH A O   1 
HETATM 9139  O  O   . HOH BA 6 .   ? 4.915   16.265  14.330  1.00 27.55 ? 608 HOH A O   1 
HETATM 9140  O  O   . HOH BA 6 .   ? -12.517 4.072   4.603   1.00 27.21 ? 609 HOH A O   1 
HETATM 9141  O  O   . HOH BA 6 .   ? -15.312 -7.261  -10.622 1.00 27.84 ? 610 HOH A O   1 
HETATM 9142  O  O   . HOH BA 6 .   ? -16.348 -7.728  -14.661 1.00 27.14 ? 611 HOH A O   1 
HETATM 9143  O  O   . HOH BA 6 .   ? -16.498 -6.177  -16.530 1.00 28.47 ? 612 HOH A O   1 
HETATM 9144  O  O   . HOH BA 6 .   ? -23.120 -2.089  -17.198 1.00 28.27 ? 613 HOH A O   1 
HETATM 9145  O  O   . HOH BA 6 .   ? -22.721 1.419   -14.362 1.00 41.63 ? 614 HOH A O   1 
HETATM 9146  O  O   . HOH BA 6 .   ? -17.619 12.074  -26.070 1.00 26.56 ? 615 HOH A O   1 
HETATM 9147  O  O   . HOH BA 6 .   ? -15.373 6.403   -29.077 1.00 28.45 ? 616 HOH A O   1 
HETATM 9148  O  O   . HOH BA 6 .   ? -15.018 4.974   -26.270 1.00 20.65 ? 617 HOH A O   1 
HETATM 9149  O  O   . HOH BA 6 .   ? -18.990 22.719  -26.035 1.00 31.34 ? 618 HOH A O   1 
HETATM 9150  O  O   . HOH BA 6 .   ? 4.710   26.551  -26.710 1.00 20.22 ? 619 HOH A O   1 
HETATM 9151  O  O   . HOH BA 6 .   ? 4.765   24.160  -27.717 1.00 29.81 ? 620 HOH A O   1 
HETATM 9152  O  O   . HOH BA 6 .   ? 4.848   20.758  -27.092 1.00 31.98 ? 621 HOH A O   1 
HETATM 9153  O  O   . HOH BA 6 .   ? -0.152  19.777  -30.203 1.00 28.79 ? 622 HOH A O   1 
HETATM 9154  O  O   . HOH BA 6 .   ? 13.274  28.483  -24.169 1.00 26.51 ? 623 HOH A O   1 
HETATM 9155  O  O   . HOH BA 6 .   ? 16.803  24.059  -19.081 1.00 26.87 ? 624 HOH A O   1 
HETATM 9156  O  O   . HOH BA 6 .   ? -2.255  36.720  -31.046 1.00 27.15 ? 625 HOH A O   1 
HETATM 9157  O  O   . HOH BA 6 .   ? -0.526  37.094  -22.626 1.00 34.58 ? 626 HOH A O   1 
HETATM 9158  O  O   . HOH BA 6 .   ? -2.301  34.724  -16.876 1.00 38.34 ? 627 HOH A O   1 
HETATM 9159  O  O   . HOH BA 6 .   ? 7.889   26.501  5.000   1.00 34.27 ? 628 HOH A O   1 
HETATM 9160  O  O   . HOH BA 6 .   ? -11.080 33.566  -15.518 1.00 40.57 ? 629 HOH A O   1 
HETATM 9161  O  O   . HOH BA 6 .   ? -14.057 28.202  -15.566 1.00 26.18 ? 630 HOH A O   1 
HETATM 9162  O  O   . HOH BA 6 .   ? -24.547 13.743  -18.006 1.00 28.48 ? 631 HOH A O   1 
HETATM 9163  O  O   . HOH BA 6 .   ? -4.027  24.304  -6.246  1.00 27.50 ? 632 HOH A O   1 
HETATM 9164  O  O   . HOH BA 6 .   ? 17.628  10.612  -3.125  1.00 34.06 ? 633 HOH A O   1 
HETATM 9165  O  O   . HOH BA 6 .   ? 7.272   2.566   -4.536  1.00 24.61 ? 634 HOH A O   1 
HETATM 9166  O  O   . HOH BA 6 .   ? 7.523   1.222   -12.406 1.00 29.14 ? 635 HOH A O   1 
HETATM 9167  O  O   . HOH BA 6 .   ? -21.778 27.468  -4.544  1.00 28.25 ? 636 HOH A O   1 
HETATM 9168  O  O   . HOH BA 6 .   ? -22.971 17.342  -8.793  1.00 20.45 ? 637 HOH A O   1 
HETATM 9169  O  O   . HOH BA 6 .   ? -17.325 12.554  -5.473  1.00 26.90 ? 638 HOH A O   1 
HETATM 9170  O  O   . HOH BA 6 .   ? -19.383 4.874   -7.402  1.00 31.67 ? 639 HOH A O   1 
HETATM 9171  O  O   . HOH BA 6 .   ? 4.667   2.135   -23.065 1.00 31.73 ? 640 HOH A O   1 
HETATM 9172  O  O   . HOH BA 6 .   ? 5.530   6.011   -25.068 1.00 27.51 ? 641 HOH A O   1 
HETATM 9173  O  O   . HOH BA 6 .   ? 1.202   1.583   -28.159 1.00 28.51 ? 642 HOH A O   1 
HETATM 9174  O  O   . HOH BA 6 .   ? 17.133  3.188   -12.269 1.00 27.79 ? 643 HOH A O   1 
HETATM 9175  O  O   . HOH BA 6 .   ? 19.927  4.542   -20.373 1.00 23.45 ? 644 HOH A O   1 
HETATM 9176  O  O   . HOH BA 6 .   ? 13.781  21.060  -23.442 1.00 34.13 ? 645 HOH A O   1 
HETATM 9177  O  O   . HOH BA 6 .   ? 17.800  29.020  -6.513  1.00 37.11 ? 646 HOH A O   1 
HETATM 9178  O  O   . HOH BA 6 .   ? 7.839   35.070  -9.502  1.00 43.26 ? 647 HOH A O   1 
HETATM 9179  O  O   . HOH BA 6 .   ? -2.966  16.186  -27.864 1.00 43.40 ? 648 HOH A O   1 
HETATM 9180  O  O   . HOH BA 6 .   ? 18.050  0.077   -5.619  1.00 24.39 ? 649 HOH A O   1 
HETATM 9181  O  O   . HOH BA 6 .   ? -1.676  21.896  2.419   1.00 27.11 ? 650 HOH A O   1 
HETATM 9182  O  O   . HOH BA 6 .   ? -18.221 1.080   -6.148  1.00 44.87 ? 651 HOH A O   1 
HETATM 9183  O  O   . HOH BA 6 .   ? -25.345 24.036  -5.097  1.00 24.13 ? 652 HOH A O   1 
HETATM 9184  O  O   . HOH BA 6 .   ? -18.719 14.978  0.764   1.00 31.00 ? 653 HOH A O   1 
HETATM 9185  O  O   . HOH BA 6 .   ? 8.604   32.629  -20.599 1.00 25.05 ? 654 HOH A O   1 
HETATM 9186  O  O   . HOH BA 6 .   ? 0.590   9.919   17.297  1.00 28.87 ? 655 HOH A O   1 
HETATM 9187  O  O   . HOH BA 6 .   ? 14.765  4.818   -13.390 1.00 27.95 ? 656 HOH A O   1 
HETATM 9188  O  O   . HOH BA 6 .   ? -11.358 0.170   -26.281 1.00 10.65 ? 657 HOH A O   1 
HETATM 9189  O  O   . HOH BA 6 .   ? 10.837  1.305   -17.224 1.00 19.64 ? 658 HOH A O   1 
HETATM 9190  O  O   . HOH BA 6 .   ? -17.053 28.794  -11.224 1.00 20.95 ? 659 HOH A O   1 
HETATM 9191  O  O   . HOH BA 6 .   ? -22.364 12.475  -18.293 1.00 25.51 ? 660 HOH A O   1 
HETATM 9192  O  O   . HOH BA 6 .   ? -9.071  -1.212  -29.693 1.00 23.01 ? 661 HOH A O   1 
HETATM 9193  O  O   . HOH BA 6 .   ? -7.636  -0.907  -27.376 1.00 18.70 ? 662 HOH A O   1 
HETATM 9194  O  O   . HOH BA 6 .   ? 6.486   25.941  -22.837 1.00 11.68 ? 663 HOH A O   1 
HETATM 9195  O  O   . HOH BA 6 .   ? -3.456  28.023  -29.038 1.00 30.26 ? 664 HOH A O   1 
HETATM 9196  O  O   . HOH BA 6 .   ? -0.637  29.557  -29.313 1.00 22.53 ? 665 HOH A O   1 
HETATM 9197  O  O   . HOH BA 6 .   ? 0.100   25.758  -27.600 1.00 19.79 ? 666 HOH A O   1 
HETATM 9198  O  O   . HOH BA 6 .   ? 21.001  12.425  -15.914 1.00 17.10 ? 667 HOH A O   1 
HETATM 9199  O  O   . HOH BA 6 .   ? 18.309  28.993  -11.226 1.00 16.70 ? 668 HOH A O   1 
HETATM 9200  O  O   . HOH BA 6 .   ? 16.029  27.151  -8.189  1.00 15.13 ? 669 HOH A O   1 
HETATM 9201  O  O   . HOH BA 6 .   ? 11.515  32.230  -7.836  1.00 20.93 ? 670 HOH A O   1 
HETATM 9202  O  O   . HOH BA 6 .   ? -9.800  19.280  7.116   1.00 21.30 ? 671 HOH A O   1 
HETATM 9203  O  O   . HOH BA 6 .   ? -10.404 -6.019  -27.140 1.00 24.40 ? 672 HOH A O   1 
HETATM 9204  O  O   . HOH BA 6 .   ? 12.450  1.881   -1.508  1.00 22.77 ? 673 HOH A O   1 
HETATM 9205  O  O   . HOH BA 6 .   ? -13.722 -7.881  -13.364 1.00 26.16 ? 674 HOH A O   1 
HETATM 9206  O  O   . HOH BA 6 .   ? 5.804   9.917   -26.233 1.00 16.45 ? 675 HOH A O   1 
HETATM 9207  O  O   . HOH BA 6 .   ? 2.520   13.995  -26.996 1.00 28.06 ? 676 HOH A O   1 
HETATM 9208  O  O   . HOH BA 6 .   ? 10.376  28.947  -25.725 1.00 26.45 ? 677 HOH A O   1 
HETATM 9209  O  O   . HOH BA 6 .   ? 7.810   17.298  9.807   1.00 36.50 ? 678 HOH A O   1 
HETATM 9210  O  O   . HOH BA 6 .   ? 3.975   14.393  15.878  1.00 25.11 ? 679 HOH A O   1 
HETATM 9211  O  O   . HOH BA 6 .   ? -17.101 2.755   -22.393 1.00 20.56 ? 680 HOH A O   1 
HETATM 9212  O  O   . HOH BA 6 .   ? -18.073 1.300   -24.570 1.00 21.51 ? 681 HOH A O   1 
HETATM 9213  O  O   . HOH BA 6 .   ? -11.179 16.432  -26.954 1.00 17.02 ? 682 HOH A O   1 
HETATM 9214  O  O   . HOH BA 6 .   ? -8.095  21.602  -26.222 1.00 16.09 ? 683 HOH A O   1 
HETATM 9215  O  O   . HOH BA 6 .   ? -5.704  20.415  -27.271 1.00 15.51 ? 684 HOH A O   1 
HETATM 9216  O  O   . HOH BA 6 .   ? -4.837  29.911  -23.743 1.00 13.10 ? 685 HOH A O   1 
HETATM 9217  O  O   . HOH BA 6 .   ? -6.828  27.857  -23.569 1.00 13.57 ? 686 HOH A O   1 
HETATM 9218  O  O   . HOH BA 6 .   ? -5.881  30.918  -21.272 1.00 12.01 ? 687 HOH A O   1 
HETATM 9219  O  O   . HOH BA 6 .   ? -12.482 26.677  -23.807 1.00 26.22 ? 688 HOH A O   1 
HETATM 9220  O  O   . HOH BA 6 .   ? -7.403  24.505  -26.891 1.00 19.51 ? 689 HOH A O   1 
HETATM 9221  O  O   . HOH BA 6 .   ? -7.116  27.743  -26.103 1.00 32.93 ? 690 HOH A O   1 
HETATM 9222  O  O   . HOH BA 6 .   ? 2.090   38.030  -25.663 1.00 14.71 ? 691 HOH A O   1 
HETATM 9223  O  O   . HOH BA 6 .   ? -0.357  31.292  -14.216 1.00 15.79 ? 692 HOH A O   1 
HETATM 9224  O  O   . HOH BA 6 .   ? -1.396  32.360  -16.658 1.00 19.10 ? 693 HOH A O   1 
HETATM 9225  O  O   . HOH BA 6 .   ? -12.735 28.626  -13.204 1.00 22.61 ? 694 HOH A O   1 
HETATM 9226  O  O   . HOH BA 6 .   ? -21.010 13.436  -13.720 1.00 32.88 ? 695 HOH A O   1 
HETATM 9227  O  O   . HOH BA 6 .   ? -20.796 16.050  -12.487 1.00 18.19 ? 696 HOH A O   1 
HETATM 9228  O  O   . HOH BA 6 .   ? -22.843 17.685  -11.586 1.00 18.15 ? 697 HOH A O   1 
HETATM 9229  O  O   . HOH BA 6 .   ? 0.771   -7.862  -12.036 1.00 33.23 ? 698 HOH A O   1 
HETATM 9230  O  O   . HOH BA 6 .   ? -13.075 30.845  -9.879  1.00 35.04 ? 699 HOH A O   1 
HETATM 9231  O  O   . HOH BA 6 .   ? -21.878 17.339  -1.349  1.00 37.56 ? 700 HOH A O   1 
HETATM 9232  O  O   . HOH BA 6 .   ? 16.133  17.977  -21.807 1.00 22.47 ? 701 HOH A O   1 
HETATM 9233  O  O   . HOH BA 6 .   ? 14.823  17.944  -18.350 1.00 23.32 ? 702 HOH A O   1 
HETATM 9234  O  O   . HOH BA 6 .   ? 16.212  20.246  -19.352 1.00 35.85 ? 703 HOH A O   1 
HETATM 9235  O  O   . HOH BA 6 .   ? 16.106  22.731  -15.433 1.00 17.80 ? 704 HOH A O   1 
HETATM 9236  O  O   . HOH BA 6 .   ? 15.860  19.850  -15.569 1.00 21.90 ? 705 HOH A O   1 
HETATM 9237  O  O   . HOH BA 6 .   ? 20.123  25.799  -11.292 1.00 18.16 ? 706 HOH A O   1 
HETATM 9238  O  O   . HOH BA 6 .   ? 14.000  30.478  -8.665  1.00 25.23 ? 707 HOH A O   1 
HETATM 9239  O  O   . HOH BA 6 .   ? 12.799  30.500  -11.595 1.00 16.96 ? 708 HOH A O   1 
HETATM 9240  O  O   . HOH BA 6 .   ? 10.815  31.717  -15.871 1.00 16.85 ? 709 HOH A O   1 
HETATM 9241  O  O   . HOH BA 6 .   ? 12.831  28.370  -15.573 1.00 13.98 ? 710 HOH A O   1 
HETATM 9242  O  O   . HOH BA 6 .   ? 5.924   31.702  -4.062  1.00 36.22 ? 711 HOH A O   1 
HETATM 9243  O  O   . HOH BA 6 .   ? -8.403  -5.327  -23.172 1.00 26.85 ? 712 HOH A O   1 
HETATM 9244  O  O   . HOH BA 6 .   ? 20.248  9.563   -16.379 1.00 22.36 ? 713 HOH A O   1 
HETATM 9245  O  O   . HOH BA 6 .   ? 21.465  8.400   -18.432 1.00 29.90 ? 714 HOH A O   1 
HETATM 9246  O  O   . HOH BA 6 .   ? 20.033  7.173   -20.481 1.00 21.40 ? 715 HOH A O   1 
HETATM 9247  O  O   . HOH BA 6 .   ? 17.909  8.373   -21.664 1.00 25.81 ? 716 HOH A O   1 
HETATM 9248  O  O   . HOH BA 6 .   ? 22.895  10.286  -19.585 1.00 34.36 ? 717 HOH A O   1 
HETATM 9249  O  O   . HOH BA 6 .   ? -7.335  22.213  4.854   1.00 41.53 ? 718 HOH A O   1 
HETATM 9250  O  O   . HOH BA 6 .   ? -3.187  -5.722  -15.519 1.00 30.56 ? 719 HOH A O   1 
HETATM 9251  O  O   . HOH BA 6 .   ? 1.002   -6.424  -14.342 1.00 32.35 ? 720 HOH A O   1 
HETATM 9252  O  O   . HOH BA 6 .   ? -8.516  -8.598  -16.238 1.00 37.75 ? 721 HOH A O   1 
HETATM 9253  O  O   . HOH BA 6 .   ? -9.238  -13.515 -7.710  1.00 31.82 ? 722 HOH A O   1 
HETATM 9254  O  O   . HOH BA 6 .   ? -12.705 -12.044 -7.294  1.00 27.52 ? 723 HOH A O   1 
HETATM 9255  O  O   . HOH BA 6 .   ? -24.816 -4.841  -17.630 1.00 25.23 ? 724 HOH A O   1 
HETATM 9256  O  O   . HOH BA 6 .   ? -13.244 10.270  -29.688 1.00 37.23 ? 725 HOH A O   1 
HETATM 9257  O  O   . HOH BA 6 .   ? -12.777 6.916   -29.326 1.00 33.99 ? 726 HOH A O   1 
HETATM 9258  O  O   . HOH BA 6 .   ? 3.312   27.887  -30.712 1.00 35.34 ? 727 HOH A O   1 
HETATM 9259  O  O   . HOH BA 6 .   ? 6.105   30.598  -28.812 1.00 26.30 ? 728 HOH A O   1 
HETATM 9260  O  O   . HOH BA 6 .   ? 9.917   32.900  -23.105 1.00 28.86 ? 729 HOH A O   1 
HETATM 9261  O  O   . HOH BA 6 .   ? 4.020   30.439  -3.686  1.00 36.29 ? 730 HOH A O   1 
HETATM 9262  O  O   . HOH BA 6 .   ? 4.508   27.991  -2.590  1.00 33.70 ? 731 HOH A O   1 
HETATM 9263  O  O   . HOH BA 6 .   ? -4.714  25.829  -7.674  1.00 42.40 ? 732 HOH A O   1 
HETATM 9264  O  O   . HOH BA 6 .   ? -7.834  26.765  -7.333  1.00 34.04 ? 733 HOH A O   1 
HETATM 9265  O  O   . HOH BA 6 .   ? -4.183  30.371  -13.238 1.00 34.31 ? 734 HOH A O   1 
HETATM 9266  O  O   . HOH BA 6 .   ? -3.911  31.006  -16.314 1.00 31.56 ? 735 HOH A O   1 
HETATM 9267  O  O   . HOH BA 6 .   ? -5.504  34.658  -15.020 1.00 38.12 ? 736 HOH A O   1 
HETATM 9268  O  O   . HOH BA 6 .   ? -22.572 14.422  -8.893  1.00 31.70 ? 737 HOH A O   1 
HETATM 9269  O  O   . HOH BA 6 .   ? -20.676 8.628   -16.475 1.00 39.67 ? 738 HOH A O   1 
HETATM 9270  O  O   . HOH BA 6 .   ? -20.853 11.212  -16.588 1.00 44.47 ? 739 HOH A O   1 
HETATM 9271  O  O   . HOH BA 6 .   ? -16.396 29.275  -15.865 1.00 25.14 ? 740 HOH A O   1 
HETATM 9272  O  O   . HOH BA 6 .   ? 19.840  8.668   -4.602  1.00 37.53 ? 741 HOH A O   1 
HETATM 9273  O  O   . HOH BA 6 .   ? 21.278  9.213   -9.202  1.00 43.59 ? 742 HOH A O   1 
HETATM 9274  O  O   . HOH BA 6 .   ? 20.195  6.643   -10.750 1.00 31.08 ? 743 HOH A O   1 
HETATM 9275  O  O   . HOH BA 6 .   ? 13.453  2.902   -14.096 1.00 26.61 ? 744 HOH A O   1 
HETATM 9276  O  O   . HOH BA 6 .   ? 0.192   -0.486  -18.873 1.00 33.35 ? 745 HOH A O   1 
HETATM 9277  O  O   . HOH BA 6 .   ? -0.884  -0.218  -21.348 1.00 33.79 ? 746 HOH A O   1 
HETATM 9278  O  O   . HOH BA 6 .   ? -20.620 28.941  -10.989 1.00 29.06 ? 747 HOH A O   1 
HETATM 9279  O  O   . HOH BA 6 .   ? -21.320 29.108  -8.533  1.00 26.74 ? 748 HOH A O   1 
HETATM 9280  O  O   . HOH BA 6 .   ? 12.339  18.807  -26.834 1.00 28.63 ? 749 HOH A O   1 
HETATM 9281  O  O   . HOH BA 6 .   ? 16.936  16.790  -24.749 1.00 39.21 ? 750 HOH A O   1 
HETATM 9282  O  O   . HOH BA 6 .   ? 16.407  15.915  -18.211 1.00 22.55 ? 751 HOH A O   1 
HETATM 9283  O  O   . HOH BA 6 .   ? 9.773   33.456  -5.182  1.00 35.37 ? 752 HOH A O   1 
HETATM 9284  O  O   . HOH BA 6 .   ? -11.926 -0.109  3.697   1.00 31.37 ? 753 HOH A O   1 
HETATM 9285  O  O   . HOH BA 6 .   ? -14.000 -3.466  -3.449  1.00 24.51 ? 754 HOH A O   1 
HETATM 9286  O  O   . HOH BA 6 .   ? -17.463 -7.016  -18.739 1.00 23.71 ? 755 HOH A O   1 
HETATM 9287  O  O   . HOH BA 6 .   ? -7.893  -7.418  -24.249 1.00 39.90 ? 756 HOH A O   1 
HETATM 9288  O  O   . HOH BA 6 .   ? 4.123   10.787  14.604  1.00 32.73 ? 757 HOH A O   1 
HETATM 9289  O  O   . HOH BA 6 .   ? 14.215  13.040  3.453   1.00 29.04 ? 758 HOH A O   1 
HETATM 9290  O  O   . HOH BA 6 .   ? 2.795   24.705  3.187   1.00 42.98 ? 759 HOH A O   1 
HETATM 9291  O  O   . HOH BA 6 .   ? -0.328  30.371  -7.282  1.00 36.07 ? 760 HOH A O   1 
HETATM 9292  O  O   . HOH BA 6 .   ? 10.162  16.763  8.019   1.00 30.02 ? 761 HOH A O   1 
HETATM 9293  O  O   . HOH BA 6 .   ? 9.371   26.506  -25.423 1.00 31.42 ? 762 HOH A O   1 
HETATM 9294  O  O   . HOH BA 6 .   ? 17.097  13.109  -24.615 1.00 32.94 ? 763 HOH A O   1 
HETATM 9295  O  O   . HOH BA 6 .   ? 18.637  22.980  10.442  1.00 33.99 ? 764 HOH A O   1 
HETATM 9296  O  O   . HOH BA 6 .   ? 14.132  16.543  8.685   1.00 33.10 ? 765 HOH A O   1 
HETATM 9297  O  O   . HOH BA 6 .   ? 16.785  15.499  -20.700 1.00 24.53 ? 766 HOH A O   1 
HETATM 9298  O  O   . HOH BA 6 .   ? -25.673 3.681   -17.826 1.00 36.25 ? 767 HOH A O   1 
HETATM 9299  O  O   . HOH BA 6 .   ? -24.706 -0.153  -16.169 1.00 34.80 ? 768 HOH A O   1 
HETATM 9300  O  O   . HOH BA 6 .   ? -3.190  -6.409  -6.944  1.00 13.68 ? 769 HOH A O   1 
HETATM 9301  O  O   . HOH CA 6 .   ? -4.398  2.701   4.511   1.00 5.63  ? 401 HOH B O   1 
HETATM 9302  O  O   . HOH CA 6 .   ? 0.010   2.018   4.109   1.00 5.00  ? 402 HOH B O   1 
HETATM 9303  O  O   . HOH CA 6 .   ? -1.296  1.559   6.566   1.00 7.35  ? 403 HOH B O   1 
HETATM 9304  O  O   . HOH CA 6 .   ? 4.947   3.610   7.842   1.00 7.64  ? 404 HOH B O   1 
HETATM 9305  O  O   . HOH CA 6 .   ? -8.325  -13.709 1.426   1.00 8.41  ? 405 HOH B O   1 
HETATM 9306  O  O   . HOH CA 6 .   ? -0.897  -5.462  2.536   1.00 5.70  ? 406 HOH B O   1 
HETATM 9307  O  O   . HOH CA 6 .   ? 11.807  -13.903 12.399  1.00 9.01  ? 407 HOH B O   1 
HETATM 9308  O  O   . HOH CA 6 .   ? -4.402  -2.320  -2.013  1.00 12.19 ? 408 HOH B O   1 
HETATM 9309  O  O   . HOH CA 6 .   ? -14.013 -14.837 9.046   1.00 8.51  ? 409 HOH B O   1 
HETATM 9310  O  O   . HOH CA 6 .   ? -2.541  -6.103  10.551  1.00 7.03  ? 410 HOH B O   1 
HETATM 9311  O  O   . HOH CA 6 .   ? -7.825  -0.165  7.591   1.00 9.12  ? 411 HOH B O   1 
HETATM 9312  O  O   . HOH CA 6 .   ? 6.529   -1.349  0.858   1.00 11.38 ? 412 HOH B O   1 
HETATM 9313  O  O   . HOH CA 6 .   ? -1.573  2.235   9.637   1.00 7.09  ? 413 HOH B O   1 
HETATM 9314  O  O   . HOH CA 6 .   ? -16.660 -13.579 8.219   1.00 11.39 ? 414 HOH B O   1 
HETATM 9315  O  O   . HOH CA 6 .   ? 4.861   5.351   10.000  1.00 8.20  ? 415 HOH B O   1 
HETATM 9316  O  O   . HOH CA 6 .   ? 4.179   4.286   5.284   1.00 7.45  ? 416 HOH B O   1 
HETATM 9317  O  O   . HOH CA 6 .   ? -1.038  -3.339  0.715   1.00 13.00 ? 417 HOH B O   1 
HETATM 9318  O  O   . HOH CA 6 .   ? -8.376  4.271   7.846   1.00 10.75 ? 418 HOH B O   1 
HETATM 9319  O  O   . HOH CA 6 .   ? 12.629  -4.056  14.689  1.00 12.16 ? 419 HOH B O   1 
HETATM 9320  O  O   . HOH CA 6 .   ? -5.108  -31.082 16.103  1.00 15.22 ? 420 HOH B O   1 
HETATM 9321  O  O   . HOH CA 6 .   ? 1.820   2.894   19.715  1.00 9.90  ? 421 HOH B O   1 
HETATM 9322  O  O   . HOH CA 6 .   ? 5.955   -18.061 2.665   1.00 9.78  ? 422 HOH B O   1 
HETATM 9323  O  O   . HOH CA 6 .   ? -4.550  -17.602 -4.291  1.00 12.94 ? 423 HOH B O   1 
HETATM 9324  O  O   . HOH CA 6 .   ? -10.208 -7.986  12.473  1.00 10.51 ? 424 HOH B O   1 
HETATM 9325  O  O   . HOH CA 6 .   ? 8.472   2.659   -0.224  1.00 12.44 ? 425 HOH B O   1 
HETATM 9326  O  O   . HOH CA 6 .   ? -7.499  -30.232 15.383  1.00 16.61 ? 426 HOH B O   1 
HETATM 9327  O  O   . HOH CA 6 .   ? -2.390  -16.055 -3.811  1.00 12.88 ? 427 HOH B O   1 
HETATM 9328  O  O   . HOH CA 6 .   ? -20.317 -17.322 9.646   1.00 15.23 ? 428 HOH B O   1 
HETATM 9329  O  O   . HOH CA 6 .   ? 1.593   -26.392 4.713   1.00 16.55 ? 429 HOH B O   1 
HETATM 9330  O  O   . HOH CA 6 .   ? -11.541 -7.275  10.246  1.00 9.46  ? 430 HOH B O   1 
HETATM 9331  O  O   . HOH CA 6 .   ? 8.638   -30.487 14.045  1.00 17.00 ? 431 HOH B O   1 
HETATM 9332  O  O   . HOH CA 6 .   ? -12.528 -16.897 -1.274  1.00 11.94 ? 432 HOH B O   1 
HETATM 9333  O  O   . HOH CA 6 .   ? 10.318  -29.175 15.987  1.00 13.94 ? 433 HOH B O   1 
HETATM 9334  O  O   . HOH CA 6 .   ? 5.320   5.463   20.359  1.00 10.52 ? 434 HOH B O   1 
HETATM 9335  O  O   . HOH CA 6 .   ? -1.814  -15.305 23.522  1.00 18.51 ? 435 HOH B O   1 
HETATM 9336  O  O   . HOH CA 6 .   ? -10.551 -32.059 25.644  1.00 13.44 ? 436 HOH B O   1 
HETATM 9337  O  O   . HOH CA 6 .   ? 4.369   -19.398 25.169  1.00 10.23 ? 437 HOH B O   1 
HETATM 9338  O  O   . HOH CA 6 .   ? 15.298  -23.823 7.575   1.00 15.04 ? 438 HOH B O   1 
HETATM 9339  O  O   . HOH CA 6 .   ? -15.817 -25.798 13.814  1.00 15.98 ? 439 HOH B O   1 
HETATM 9340  O  O   . HOH CA 6 .   ? 4.276   -30.617 23.138  1.00 16.09 ? 440 HOH B O   1 
HETATM 9341  O  O   . HOH CA 6 .   ? 8.979   0.459   6.950   1.00 13.97 ? 441 HOH B O   1 
HETATM 9342  O  O   . HOH CA 6 .   ? -17.293 -13.227 4.530   1.00 13.09 ? 442 HOH B O   1 
HETATM 9343  O  O   . HOH CA 6 .   ? 6.508   -3.659  -6.458  1.00 14.69 ? 443 HOH B O   1 
HETATM 9344  O  O   . HOH CA 6 .   ? 7.211   2.706   15.414  1.00 10.70 ? 444 HOH B O   1 
HETATM 9345  O  O   . HOH CA 6 .   ? 4.824   -15.539 27.150  1.00 13.13 ? 445 HOH B O   1 
HETATM 9346  O  O   . HOH CA 6 .   ? 14.369  -2.093  8.539   1.00 15.45 ? 446 HOH B O   1 
HETATM 9347  O  O   . HOH CA 6 .   ? -13.499 -4.384  5.241   1.00 17.81 ? 447 HOH B O   1 
HETATM 9348  O  O   . HOH CA 6 .   ? 10.624  -20.787 1.729   1.00 10.98 ? 448 HOH B O   1 
HETATM 9349  O  O   . HOH CA 6 .   ? 11.942  3.376   9.541   1.00 11.90 ? 449 HOH B O   1 
HETATM 9350  O  O   . HOH CA 6 .   ? -5.379  -9.013  13.149  1.00 11.82 ? 450 HOH B O   1 
HETATM 9351  O  O   . HOH CA 6 .   ? -10.562 -29.905 27.351  1.00 17.17 ? 451 HOH B O   1 
HETATM 9352  O  O   . HOH CA 6 .   ? -8.761  -8.040  -0.118  1.00 14.07 ? 452 HOH B O   1 
HETATM 9353  O  O   . HOH CA 6 .   ? 10.734  0.261   22.893  1.00 13.57 ? 453 HOH B O   1 
HETATM 9354  O  O   . HOH CA 6 .   ? -2.626  -23.164 25.273  1.00 11.99 ? 454 HOH B O   1 
HETATM 9355  O  O   . HOH CA 6 .   ? -1.737  -28.051 0.216   1.00 16.04 ? 455 HOH B O   1 
HETATM 9356  O  O   . HOH CA 6 .   ? 1.300   -21.159 26.422  1.00 14.56 ? 456 HOH B O   1 
HETATM 9357  O  O   . HOH CA 6 .   ? 2.653   8.869   15.311  1.00 14.84 ? 457 HOH B O   1 
HETATM 9358  O  O   . HOH CA 6 .   ? 3.767   9.489   10.833  1.00 12.53 ? 458 HOH B O   1 
HETATM 9359  O  O   . HOH CA 6 .   ? 7.976   -1.539  -7.340  1.00 13.95 ? 459 HOH B O   1 
HETATM 9360  O  O   . HOH CA 6 .   ? -18.934 -19.824 18.253  1.00 18.42 ? 460 HOH B O   1 
HETATM 9361  O  O   . HOH CA 6 .   ? -12.723 -28.148 8.349   1.00 24.59 ? 461 HOH B O   1 
HETATM 9362  O  O   . HOH CA 6 .   ? -10.405 -5.599  13.938  1.00 13.59 ? 462 HOH B O   1 
HETATM 9363  O  O   . HOH CA 6 .   ? -13.105 -5.222  7.915   1.00 17.45 ? 463 HOH B O   1 
HETATM 9364  O  O   . HOH CA 6 .   ? 2.069   -34.415 17.167  1.00 18.14 ? 464 HOH B O   1 
HETATM 9365  O  O   . HOH CA 6 .   ? 9.388   -31.082 17.832  1.00 18.73 ? 465 HOH B O   1 
HETATM 9366  O  O   . HOH CA 6 .   ? 3.280   -3.623  23.874  1.00 17.67 ? 466 HOH B O   1 
HETATM 9367  O  O   . HOH CA 6 .   ? -6.765  -16.065 -3.898  1.00 14.35 ? 467 HOH B O   1 
HETATM 9368  O  O   . HOH CA 6 .   ? -18.041 -10.931 3.368   1.00 16.07 ? 468 HOH B O   1 
HETATM 9369  O  O   . HOH CA 6 .   ? 15.128  -20.975 7.593   1.00 14.56 ? 469 HOH B O   1 
HETATM 9370  O  O   . HOH CA 6 .   ? 2.362   -3.979  -2.745  1.00 14.45 ? 470 HOH B O   1 
HETATM 9371  O  O   . HOH CA 6 .   ? 8.696   -31.162 22.309  1.00 18.26 ? 471 HOH B O   1 
HETATM 9372  O  O   . HOH CA 6 .   ? 8.040   3.148   9.057   1.00 13.86 ? 472 HOH B O   1 
HETATM 9373  O  O   . HOH CA 6 .   ? -5.412  -18.307 22.109  1.00 13.39 ? 473 HOH B O   1 
HETATM 9374  O  O   . HOH CA 6 .   ? 4.865   -12.051 -6.896  1.00 15.68 ? 474 HOH B O   1 
HETATM 9375  O  O   . HOH CA 6 .   ? -14.620 -4.237  11.474  1.00 15.69 ? 475 HOH B O   1 
HETATM 9376  O  O   . HOH CA 6 .   ? -13.953 -16.062 -3.490  1.00 14.95 ? 476 HOH B O   1 
HETATM 9377  O  O   . HOH CA 6 .   ? -12.493 -5.372  15.788  1.00 15.90 ? 477 HOH B O   1 
HETATM 9378  O  O   . HOH CA 6 .   ? 9.654   0.164   -0.825  1.00 19.49 ? 478 HOH B O   1 
HETATM 9379  O  O   . HOH CA 6 .   ? -18.726 -13.593 22.499  1.00 18.51 ? 479 HOH B O   1 
HETATM 9380  O  O   . HOH CA 6 .   ? -13.862 1.621   12.623  1.00 22.97 ? 480 HOH B O   1 
HETATM 9381  O  O   . HOH CA 6 .   ? -14.772 -24.716 23.850  1.00 19.09 ? 481 HOH B O   1 
HETATM 9382  O  O   . HOH CA 6 .   ? 10.310  -1.908  8.445   1.00 15.45 ? 482 HOH B O   1 
HETATM 9383  O  O   . HOH CA 6 .   ? -3.132  -25.384 26.953  1.00 19.56 ? 483 HOH B O   1 
HETATM 9384  O  O   . HOH CA 6 .   ? 22.316  -16.918 2.937   1.00 15.36 ? 484 HOH B O   1 
HETATM 9385  O  O   . HOH CA 6 .   ? -14.149 -28.706 16.173  1.00 20.68 ? 485 HOH B O   1 
HETATM 9386  O  O   . HOH CA 6 .   ? 13.875  -6.113  16.258  1.00 27.13 ? 486 HOH B O   1 
HETATM 9387  O  O   . HOH CA 6 .   ? -1.962  -37.757 29.223  1.00 20.41 ? 487 HOH B O   1 
HETATM 9388  O  O   . HOH CA 6 .   ? -17.006 -8.929  1.721   1.00 18.19 ? 488 HOH B O   1 
HETATM 9389  O  O   . HOH CA 6 .   ? -1.493  -6.274  -4.715  1.00 19.66 ? 489 HOH B O   1 
HETATM 9390  O  O   . HOH CA 6 .   ? 13.830  -8.689  17.743  1.00 17.22 ? 490 HOH B O   1 
HETATM 9391  O  O   . HOH CA 6 .   ? -6.446  5.521   17.160  1.00 13.17 ? 491 HOH B O   1 
HETATM 9392  O  O   . HOH CA 6 .   ? -1.322  -5.622  22.832  1.00 20.09 ? 492 HOH B O   1 
HETATM 9393  O  O   . HOH CA 6 .   ? -18.142 -6.540  20.528  1.00 15.97 ? 493 HOH B O   1 
HETATM 9394  O  O   . HOH CA 6 .   ? -21.612 -9.751  17.171  1.00 15.74 ? 494 HOH B O   1 
HETATM 9395  O  O   . HOH CA 6 .   ? 10.653  -18.223 28.626  1.00 19.52 ? 495 HOH B O   1 
HETATM 9396  O  O   . HOH CA 6 .   ? -8.047  3.542   15.163  1.00 21.19 ? 496 HOH B O   1 
HETATM 9397  O  O   . HOH CA 6 .   ? 5.370   1.038   24.879  1.00 15.96 ? 497 HOH B O   1 
HETATM 9398  O  O   . HOH CA 6 .   ? -11.938 -26.082 6.228   1.00 21.86 ? 498 HOH B O   1 
HETATM 9399  O  O   . HOH CA 6 .   ? -12.651 -26.794 23.981  1.00 16.80 ? 499 HOH B O   1 
HETATM 9400  O  O   . HOH CA 6 .   ? -12.665 -28.250 26.502  1.00 17.81 ? 500 HOH B O   1 
HETATM 9401  O  O   . HOH CA 6 .   ? -18.095 -27.088 13.437  1.00 22.25 ? 501 HOH B O   1 
HETATM 9402  O  O   . HOH CA 6 .   ? 6.701   -29.227 22.074  1.00 20.90 ? 502 HOH B O   1 
HETATM 9403  O  O   . HOH CA 6 .   ? -15.534 -1.649  11.258  1.00 18.03 ? 503 HOH B O   1 
HETATM 9404  O  O   . HOH CA 6 .   ? 0.297   -23.328 25.092  1.00 15.02 ? 504 HOH B O   1 
HETATM 9405  O  O   . HOH CA 6 .   ? 8.660   -15.036 -2.839  1.00 15.39 ? 505 HOH B O   1 
HETATM 9406  O  O   . HOH CA 6 .   ? 6.708   -8.413  33.500  1.00 20.91 ? 506 HOH B O   1 
HETATM 9407  O  O   . HOH CA 6 .   ? 16.402  -4.706  8.456   1.00 20.95 ? 507 HOH B O   1 
HETATM 9408  O  O   . HOH CA 6 .   ? 21.850  -8.962  -3.892  1.00 23.61 ? 508 HOH B O   1 
HETATM 9409  O  O   . HOH CA 6 .   ? 10.545  -7.076  -7.837  1.00 17.90 ? 509 HOH B O   1 
HETATM 9410  O  O   . HOH CA 6 .   ? -11.879 -4.700  11.389  1.00 13.53 ? 510 HOH B O   1 
HETATM 9411  O  O   . HOH CA 6 .   ? -9.724  -34.456 20.957  1.00 22.47 ? 511 HOH B O   1 
HETATM 9412  O  O   . HOH CA 6 .   ? -16.520 -21.795 22.340  1.00 16.29 ? 512 HOH B O   1 
HETATM 9413  O  O   . HOH CA 6 .   ? -12.311 -19.613 -2.019  1.00 18.52 ? 513 HOH B O   1 
HETATM 9414  O  O   . HOH CA 6 .   ? -15.184 -6.715  1.729   1.00 17.66 ? 514 HOH B O   1 
HETATM 9415  O  O   . HOH CA 6 .   ? -5.420  -33.735 23.445  1.00 17.44 ? 515 HOH B O   1 
HETATM 9416  O  O   . HOH CA 6 .   ? -15.582 -5.816  9.299   1.00 17.42 ? 516 HOH B O   1 
HETATM 9417  O  O   . HOH CA 6 .   ? 17.055  -5.277  27.229  1.00 21.04 ? 517 HOH B O   1 
HETATM 9418  O  O   . HOH CA 6 .   ? 6.174   -17.377 28.590  1.00 16.11 ? 518 HOH B O   1 
HETATM 9419  O  O   . HOH CA 6 .   ? 17.409  -18.354 17.659  1.00 22.32 ? 519 HOH B O   1 
HETATM 9420  O  O   . HOH CA 6 .   ? 19.043  -11.124 10.833  1.00 21.97 ? 520 HOH B O   1 
HETATM 9421  O  O   . HOH CA 6 .   ? 0.967   -26.564 0.443   1.00 19.11 ? 521 HOH B O   1 
HETATM 9422  O  O   . HOH CA 6 .   ? -0.291  -16.802 -5.561  1.00 19.67 ? 522 HOH B O   1 
HETATM 9423  O  O   . HOH CA 6 .   ? -8.971  6.705   17.078  1.00 26.26 ? 523 HOH B O   1 
HETATM 9424  O  O   . HOH CA 6 .   ? 10.255  -29.255 23.414  1.00 24.09 ? 524 HOH B O   1 
HETATM 9425  O  O   . HOH CA 6 .   ? -17.001 -20.727 7.729   1.00 18.85 ? 525 HOH B O   1 
HETATM 9426  O  O   . HOH CA 6 .   ? 7.200   -13.706 -7.184  1.00 20.34 ? 526 HOH B O   1 
HETATM 9427  O  O   . HOH CA 6 .   ? -19.359 -21.707 20.317  1.00 21.87 ? 527 HOH B O   1 
HETATM 9428  O  O   . HOH CA 6 .   ? -17.668 -22.456 3.997   1.00 24.36 ? 528 HOH B O   1 
HETATM 9429  O  O   . HOH CA 6 .   ? -5.621  -3.865  -0.125  1.00 17.24 ? 529 HOH B O   1 
HETATM 9430  O  O   . HOH CA 6 .   ? 9.678   4.857   -1.636  1.00 19.91 ? 530 HOH B O   1 
HETATM 9431  O  O   . HOH CA 6 .   ? -2.966  -20.892 26.788  1.00 16.63 ? 531 HOH B O   1 
HETATM 9432  O  O   . HOH CA 6 .   ? -0.558  -20.464 28.287  1.00 22.99 ? 532 HOH B O   1 
HETATM 9433  O  O   . HOH CA 6 .   ? 4.244   -28.546 25.087  1.00 19.12 ? 533 HOH B O   1 
HETATM 9434  O  O   . HOH CA 6 .   ? -15.795 -19.931 24.842  1.00 22.49 ? 534 HOH B O   1 
HETATM 9435  O  O   . HOH CA 6 .   ? -4.299  -32.268 -0.688  1.00 25.74 ? 535 HOH B O   1 
HETATM 9436  O  O   . HOH CA 6 .   ? 11.219  5.813   8.559   1.00 23.44 ? 536 HOH B O   1 
HETATM 9437  O  O   . HOH CA 6 .   ? 6.738   -11.180 33.679  1.00 20.26 ? 537 HOH B O   1 
HETATM 9438  O  O   . HOH CA 6 .   ? 2.236   2.713   22.402  1.00 19.91 ? 538 HOH B O   1 
HETATM 9439  O  O   . HOH CA 6 .   ? 0.695   -33.343 13.151  1.00 18.92 ? 539 HOH B O   1 
HETATM 9440  O  O   . HOH CA 6 .   ? -21.703 -19.158 17.570  1.00 27.46 ? 540 HOH B O   1 
HETATM 9441  O  O   . HOH CA 6 .   ? -1.002  -30.031 1.968   1.00 20.81 ? 541 HOH B O   1 
HETATM 9442  O  O   . HOH CA 6 .   ? -11.498 -5.577  -2.403  1.00 25.55 ? 542 HOH B O   1 
HETATM 9443  O  O   . HOH CA 6 .   ? 12.568  -16.234 29.486  1.00 20.48 ? 543 HOH B O   1 
HETATM 9444  O  O   . HOH CA 6 .   ? -2.853  -5.115  20.466  1.00 16.71 ? 544 HOH B O   1 
HETATM 9445  O  O   . HOH CA 6 .   ? -15.977 -23.568 2.299   1.00 20.02 ? 545 HOH B O   1 
HETATM 9446  O  O   . HOH CA 6 .   ? 4.343   -19.319 28.860  1.00 24.61 ? 546 HOH B O   1 
HETATM 9447  O  O   . HOH CA 6 .   ? 18.719  -16.587 10.706  1.00 27.74 ? 547 HOH B O   1 
HETATM 9448  O  O   . HOH CA 6 .   ? -24.005 -12.170 14.084  1.00 25.39 ? 548 HOH B O   1 
HETATM 9449  O  O   . HOH CA 6 .   ? 4.038   5.380   22.808  1.00 22.43 ? 549 HOH B O   1 
HETATM 9450  O  O   . HOH CA 6 .   ? 8.395   -31.832 10.912  1.00 31.20 ? 550 HOH B O   1 
HETATM 9451  O  O   . HOH CA 6 .   ? 2.571   -23.762 -2.831  1.00 30.24 ? 551 HOH B O   1 
HETATM 9452  O  O   . HOH CA 6 .   ? 17.336  -28.634 16.001  1.00 23.70 ? 552 HOH B O   1 
HETATM 9453  O  O   . HOH CA 6 .   ? 3.837   -21.732 27.614  1.00 15.40 ? 553 HOH B O   1 
HETATM 9454  O  O   . HOH CA 6 .   ? 10.318  -2.686  -8.691  1.00 21.65 ? 554 HOH B O   1 
HETATM 9455  O  O   . HOH CA 6 .   ? 2.884   -26.970 2.212   1.00 27.02 ? 555 HOH B O   1 
HETATM 9456  O  O   . HOH CA 6 .   ? 19.475  -20.165 4.820   1.00 21.74 ? 556 HOH B O   1 
HETATM 9457  O  O   . HOH CA 6 .   ? -8.307  -8.455  21.849  1.00 24.18 ? 557 HOH B O   1 
HETATM 9458  O  O   . HOH CA 6 .   ? 4.542   -34.102 10.769  1.00 28.39 ? 558 HOH B O   1 
HETATM 9459  O  O   . HOH CA 6 .   ? -5.992  -6.966  -1.091  1.00 25.64 ? 559 HOH B O   1 
HETATM 9460  O  O   . HOH CA 6 .   ? -18.439 -16.249 -2.032  1.00 22.03 ? 560 HOH B O   1 
HETATM 9461  O  O   . HOH CA 6 .   ? -4.608  -16.449 26.218  1.00 22.69 ? 561 HOH B O   1 
HETATM 9462  O  O   . HOH CA 6 .   ? 9.733   -0.602  27.100  1.00 27.13 ? 562 HOH B O   1 
HETATM 9463  O  O   . HOH CA 6 .   ? -0.939  -40.212 28.777  1.00 25.30 ? 563 HOH B O   1 
HETATM 9464  O  O   . HOH CA 6 .   ? -17.411 -23.045 6.608   1.00 23.87 ? 564 HOH B O   1 
HETATM 9465  O  O   . HOH CA 6 .   ? -19.509 -2.854  16.066  1.00 23.53 ? 565 HOH B O   1 
HETATM 9466  O  O   . HOH CA 6 .   ? 7.857   8.241   11.618  1.00 33.84 ? 566 HOH B O   1 
HETATM 9467  O  O   . HOH CA 6 .   ? -11.695 8.592   11.527  1.00 17.01 ? 567 HOH B O   1 
HETATM 9468  O  O   . HOH CA 6 .   ? 14.212  -4.350  18.515  1.00 23.92 ? 568 HOH B O   1 
HETATM 9469  O  O   . HOH CA 6 .   ? -2.033  11.131  19.057  1.00 14.98 ? 569 HOH B O   1 
HETATM 9470  O  O   . HOH CA 6 .   ? 14.052  -27.536 11.841  1.00 26.24 ? 570 HOH B O   1 
HETATM 9471  O  O   . HOH CA 6 .   ? 8.294   0.362   -5.336  1.00 19.61 ? 571 HOH B O   1 
HETATM 9472  O  O   . HOH CA 6 .   ? 3.356   -0.114  23.199  1.00 21.64 ? 572 HOH B O   1 
HETATM 9473  O  O   . HOH CA 6 .   ? -13.462 -27.404 18.606  1.00 28.06 ? 573 HOH B O   1 
HETATM 9474  O  O   . HOH CA 6 .   ? 22.854  -17.048 14.326  1.00 22.58 ? 574 HOH B O   1 
HETATM 9475  O  O   . HOH CA 6 .   ? -7.524  -16.473 25.418  1.00 31.80 ? 575 HOH B O   1 
HETATM 9476  O  O   . HOH CA 6 .   ? -8.333  -33.572 23.155  1.00 21.35 ? 576 HOH B O   1 
HETATM 9477  O  O   . HOH CA 6 .   ? 5.523   1.234   20.739  1.00 26.97 ? 577 HOH B O   1 
HETATM 9478  O  O   . HOH CA 6 .   ? 15.702  -18.512 26.297  1.00 24.20 ? 578 HOH B O   1 
HETATM 9479  O  O   . HOH CA 6 .   ? -18.863 -20.140 3.847   1.00 18.68 ? 579 HOH B O   1 
HETATM 9480  O  O   . HOH CA 6 .   ? -21.655 -22.083 11.820  1.00 23.16 ? 580 HOH B O   1 
HETATM 9481  O  O   . HOH CA 6 .   ? 15.549  4.979   -1.034  1.00 29.93 ? 581 HOH B O   1 
HETATM 9482  O  O   . HOH CA 6 .   ? 24.044  -8.353  2.667   1.00 23.26 ? 582 HOH B O   1 
HETATM 9483  O  O   . HOH CA 6 .   ? -3.460  -13.540 -4.210  1.00 21.24 ? 583 HOH B O   1 
HETATM 9484  O  O   . HOH CA 6 .   ? 3.200   -18.660 -6.230  1.00 24.84 ? 584 HOH B O   1 
HETATM 9485  O  O   . HOH CA 6 .   ? 13.874  8.596   2.135   1.00 21.79 ? 585 HOH B O   1 
HETATM 9486  O  O   . HOH CA 6 .   ? 15.132  -28.966 15.300  1.00 31.56 ? 586 HOH B O   1 
HETATM 9487  O  O   . HOH CA 6 .   ? 7.089   -1.238  -3.675  1.00 20.29 ? 587 HOH B O   1 
HETATM 9488  O  O   . HOH CA 6 .   ? 10.668  -16.011 -5.194  1.00 27.13 ? 588 HOH B O   1 
HETATM 9489  O  O   . HOH CA 6 .   ? -1.884  5.976   6.027   1.00 18.93 ? 589 HOH B O   1 
HETATM 9490  O  O   . HOH CA 6 .   ? 20.952  -24.132 10.613  1.00 31.48 ? 590 HOH B O   1 
HETATM 9491  O  O   . HOH CA 6 .   ? 7.360   3.591   6.735   1.00 18.71 ? 591 HOH B O   1 
HETATM 9492  O  O   . HOH CA 6 .   ? -8.765  -25.548 -4.390  1.00 20.75 ? 592 HOH B O   1 
HETATM 9493  O  O   . HOH CA 6 .   ? -5.535  -37.627 24.217  1.00 28.46 ? 593 HOH B O   1 
HETATM 9494  O  O   . HOH CA 6 .   ? 18.900  -20.387 25.579  1.00 43.50 ? 594 HOH B O   1 
HETATM 9495  O  O   . HOH CA 6 .   ? 12.498  -29.973 12.871  1.00 29.13 ? 595 HOH B O   1 
HETATM 9496  O  O   . HOH CA 6 .   ? -2.283  -9.831  -5.955  1.00 25.51 ? 596 HOH B O   1 
HETATM 9497  O  O   . HOH CA 6 .   ? -15.080 6.747   8.414   1.00 27.66 ? 597 HOH B O   1 
HETATM 9498  O  O   . HOH CA 6 .   ? 11.485  -20.662 26.923  1.00 24.19 ? 598 HOH B O   1 
HETATM 9499  O  O   . HOH CA 6 .   ? 6.230   -25.664 27.810  1.00 32.25 ? 599 HOH B O   1 
HETATM 9500  O  O   . HOH CA 6 .   ? -14.056 -13.736 -5.954  1.00 35.59 ? 600 HOH B O   1 
HETATM 9501  O  O   . HOH CA 6 .   ? -14.789 -24.662 10.269  1.00 25.54 ? 601 HOH B O   1 
HETATM 9502  O  O   . HOH CA 6 .   ? -29.411 -4.182  17.454  1.00 35.32 ? 602 HOH B O   1 
HETATM 9503  O  O   . HOH CA 6 .   ? 14.055  -0.216  -10.879 1.00 32.13 ? 603 HOH B O   1 
HETATM 9504  O  O   . HOH CA 6 .   ? -4.836  -26.552 29.109  1.00 37.29 ? 604 HOH B O   1 
HETATM 9505  O  O   . HOH CA 6 .   ? 23.165  -2.854  4.433   1.00 36.89 ? 605 HOH B O   1 
HETATM 9506  O  O   . HOH CA 6 .   ? 17.403  -7.412  -6.189  1.00 34.74 ? 606 HOH B O   1 
HETATM 9507  O  O   . HOH CA 6 .   ? 4.933   -8.611  -10.345 1.00 29.60 ? 607 HOH B O   1 
HETATM 9508  O  O   . HOH CA 6 .   ? -5.310  -3.944  21.122  1.00 25.49 ? 608 HOH B O   1 
HETATM 9509  O  O   . HOH CA 6 .   ? -10.077 -3.821  6.031   1.00 24.86 ? 609 HOH B O   1 
HETATM 9510  O  O   . HOH CA 6 .   ? -9.021  -28.097 30.330  1.00 27.26 ? 610 HOH B O   1 
HETATM 9511  O  O   . HOH CA 6 .   ? -10.548 -27.591 -3.995  1.00 25.37 ? 611 HOH B O   1 
HETATM 9512  O  O   . HOH CA 6 .   ? -11.122 -14.935 25.778  1.00 34.80 ? 612 HOH B O   1 
HETATM 9513  O  O   . HOH CA 6 .   ? 8.568   -19.017 -4.810  1.00 33.22 ? 613 HOH B O   1 
HETATM 9514  O  O   . HOH CA 6 .   ? 3.767   -1.620  -3.272  1.00 29.71 ? 614 HOH B O   1 
HETATM 9515  O  O   . HOH CA 6 .   ? 12.006  12.017  9.645   1.00 22.50 ? 615 HOH B O   1 
HETATM 9516  O  O   . HOH CA 6 .   ? 12.802  -32.006 15.683  1.00 34.06 ? 616 HOH B O   1 
HETATM 9517  O  O   . HOH CA 6 .   ? 2.210   -27.495 26.569  1.00 23.45 ? 617 HOH B O   1 
HETATM 9518  O  O   . HOH CA 6 .   ? -14.614 -20.169 -3.161  1.00 24.37 ? 618 HOH B O   1 
HETATM 9519  O  O   . HOH CA 6 .   ? 5.028   -11.389 -9.714  1.00 23.59 ? 619 HOH B O   1 
HETATM 9520  O  O   . HOH CA 6 .   ? -4.241  -9.329  -10.097 1.00 23.83 ? 620 HOH B O   1 
HETATM 9521  O  O   . HOH CA 6 .   ? 0.977   -25.201 26.953  1.00 22.87 ? 621 HOH B O   1 
HETATM 9522  O  O   . HOH CA 6 .   ? -12.581 -16.692 -5.633  1.00 24.31 ? 622 HOH B O   1 
HETATM 9523  O  O   . HOH CA 6 .   ? 9.167   7.833   2.791   1.00 16.82 ? 623 HOH B O   1 
HETATM 9524  O  O   . HOH CA 6 .   ? 16.493  -25.765 6.096   1.00 27.87 ? 624 HOH B O   1 
HETATM 9525  O  O   . HOH CA 6 .   ? 20.411  -19.367 17.739  1.00 31.29 ? 625 HOH B O   1 
HETATM 9526  O  O   . HOH CA 6 .   ? 23.178  -19.117 15.648  1.00 24.70 ? 626 HOH B O   1 
HETATM 9527  O  O   . HOH CA 6 .   ? 6.613   -15.170 -4.866  1.00 27.23 ? 627 HOH B O   1 
HETATM 9528  O  O   . HOH CA 6 .   ? -10.533 -19.447 -4.307  1.00 32.77 ? 628 HOH B O   1 
HETATM 9529  O  O   . HOH CA 6 .   ? -18.207 -20.717 -5.597  1.00 37.38 ? 629 HOH B O   1 
HETATM 9530  O  O   . HOH CA 6 .   ? -17.172 -24.078 0.027   1.00 21.71 ? 630 HOH B O   1 
HETATM 9531  O  O   . HOH CA 6 .   ? -15.568 -26.122 3.579   1.00 26.35 ? 631 HOH B O   1 
HETATM 9532  O  O   . HOH CA 6 .   ? -12.985 -26.729 3.742   1.00 23.67 ? 632 HOH B O   1 
HETATM 9533  O  O   . HOH CA 6 .   ? -6.659  -32.561 8.993   1.00 21.00 ? 633 HOH B O   1 
HETATM 9534  O  O   . HOH CA 6 .   ? 5.902   -24.714 -0.374  1.00 19.32 ? 634 HOH B O   1 
HETATM 9535  O  O   . HOH CA 6 .   ? 5.074   -26.774 0.897   1.00 25.99 ? 635 HOH B O   1 
HETATM 9536  O  O   . HOH CA 6 .   ? 19.507  -2.710  14.583  1.00 28.02 ? 636 HOH B O   1 
HETATM 9537  O  O   . HOH CA 6 .   ? 0.423   -3.832  24.206  1.00 27.76 ? 637 HOH B O   1 
HETATM 9538  O  O   . HOH CA 6 .   ? 2.015   -26.614 -2.053  1.00 29.80 ? 638 HOH B O   1 
HETATM 9539  O  O   . HOH CA 6 .   ? -19.435 -19.765 8.022   1.00 23.01 ? 639 HOH B O   1 
HETATM 9540  O  O   . HOH CA 6 .   ? 14.569  3.571   10.493  1.00 21.79 ? 640 HOH B O   1 
HETATM 9541  O  O   . HOH CA 6 .   ? -4.048  -7.662  19.619  1.00 22.64 ? 641 HOH B O   1 
HETATM 9542  O  O   . HOH CA 6 .   ? -3.768  -7.665  17.253  1.00 23.04 ? 642 HOH B O   1 
HETATM 9543  O  O   . HOH CA 6 .   ? -11.712 12.758  13.203  1.00 22.81 ? 643 HOH B O   1 
HETATM 9544  O  O   . HOH CA 6 .   ? -1.063  -14.336 26.191  1.00 26.45 ? 644 HOH B O   1 
HETATM 9545  O  O   . HOH CA 6 .   ? -9.726  -32.000 16.933  1.00 22.77 ? 645 HOH B O   1 
HETATM 9546  O  O   . HOH CA 6 .   ? -12.806 -31.830 19.646  1.00 26.43 ? 646 HOH B O   1 
HETATM 9547  O  O   . HOH CA 6 .   ? 8.638   5.702   9.254   1.00 27.24 ? 647 HOH B O   1 
HETATM 9548  O  O   . HOH CA 6 .   ? -0.681  -12.532 21.786  1.00 25.39 ? 648 HOH B O   1 
HETATM 9549  O  O   . HOH CA 6 .   ? -0.153  -17.807 29.156  1.00 39.75 ? 649 HOH B O   1 
HETATM 9550  O  O   . HOH CA 6 .   ? 9.764   -17.127 31.999  1.00 32.32 ? 650 HOH B O   1 
HETATM 9551  O  O   . HOH CA 6 .   ? 14.378  8.771   10.291  1.00 28.13 ? 651 HOH B O   1 
HETATM 9552  O  O   . HOH CA 6 .   ? 11.794  9.367   10.904  1.00 33.25 ? 652 HOH B O   1 
HETATM 9553  O  O   . HOH CA 6 .   ? 14.366  1.210   0.533   1.00 23.62 ? 653 HOH B O   1 
HETATM 9554  O  O   . HOH CA 6 .   ? 9.176   6.336   5.049   1.00 25.80 ? 654 HOH B O   1 
HETATM 9555  O  O   . HOH CA 6 .   ? -2.406  -3.570  -3.637  1.00 19.73 ? 655 HOH B O   1 
HETATM 9556  O  O   . HOH CA 6 .   ? -2.322  -7.807  -8.913  1.00 18.08 ? 656 HOH B O   1 
HETATM 9557  O  O   . HOH CA 6 .   ? -4.190  -14.553 -7.385  1.00 31.69 ? 657 HOH B O   1 
HETATM 9558  O  O   . HOH CA 6 .   ? 0.466   -13.959 -5.658  1.00 22.54 ? 658 HOH B O   1 
HETATM 9559  O  O   . HOH CA 6 .   ? 2.643   -13.552 -6.896  1.00 19.68 ? 659 HOH B O   1 
HETATM 9560  O  O   . HOH CA 6 .   ? 9.081   -11.600 -7.799  1.00 33.79 ? 660 HOH B O   1 
HETATM 9561  O  O   . HOH CA 6 .   ? -9.073  2.266   18.857  1.00 29.94 ? 661 HOH B O   1 
HETATM 9562  O  O   . HOH CA 6 .   ? -7.117  3.166   17.377  1.00 29.34 ? 662 HOH B O   1 
HETATM 9563  O  O   . HOH CA 6 .   ? -9.682  8.546   18.453  1.00 27.54 ? 663 HOH B O   1 
HETATM 9564  O  O   . HOH CA 6 .   ? 18.448  -3.802  9.504   1.00 29.37 ? 664 HOH B O   1 
HETATM 9565  O  O   . HOH CA 6 .   ? 21.126  -9.431  7.352   1.00 33.22 ? 665 HOH B O   1 
HETATM 9566  O  O   . HOH CA 6 .   ? 8.781   -1.930  -0.148  1.00 20.07 ? 666 HOH B O   1 
HETATM 9567  O  O   . HOH CA 6 .   ? 10.714  -9.734  -5.484  1.00 24.73 ? 667 HOH B O   1 
HETATM 9568  O  O   . HOH CA 6 .   ? 25.345  -9.711  -1.580  1.00 24.06 ? 668 HOH B O   1 
HETATM 9569  O  O   . HOH CA 6 .   ? 27.759  -13.494 -2.583  1.00 23.87 ? 669 HOH B O   1 
HETATM 9570  O  O   . HOH CA 6 .   ? 16.034  -23.147 -4.823  1.00 30.52 ? 670 HOH B O   1 
HETATM 9571  O  O   . HOH CA 6 .   ? 17.036  -24.103 -0.463  1.00 36.77 ? 671 HOH B O   1 
HETATM 9572  O  O   . HOH CA 6 .   ? 15.129  -25.736 3.700   1.00 21.98 ? 672 HOH B O   1 
HETATM 9573  O  O   . HOH CA 6 .   ? 23.657  -17.492 11.149  1.00 34.33 ? 673 HOH B O   1 
HETATM 9574  O  O   . HOH CA 6 .   ? 23.625  -23.245 9.895   1.00 30.71 ? 674 HOH B O   1 
HETATM 9575  O  O   . HOH CA 6 .   ? 9.035   -33.261 13.900  1.00 29.95 ? 675 HOH B O   1 
HETATM 9576  O  O   . HOH CA 6 .   ? -5.223  -36.029 19.977  1.00 30.28 ? 676 HOH B O   1 
HETATM 9577  O  O   . HOH CA 6 .   ? -2.170  -41.584 26.696  1.00 32.44 ? 677 HOH B O   1 
HETATM 9578  O  O   . HOH CA 6 .   ? -2.243  -33.312 28.632  1.00 30.83 ? 678 HOH B O   1 
HETATM 9579  O  O   . HOH CA 6 .   ? -1.004  -25.152 28.850  1.00 30.65 ? 679 HOH B O   1 
HETATM 9580  O  O   . HOH CA 6 .   ? 12.501  -23.103 24.627  1.00 22.89 ? 680 HOH B O   1 
HETATM 9581  O  O   . HOH CA 6 .   ? 23.881  -21.354 14.107  1.00 28.19 ? 681 HOH B O   1 
HETATM 9582  O  O   . HOH CA 6 .   ? 21.684  -23.019 13.989  1.00 27.03 ? 682 HOH B O   1 
HETATM 9583  O  O   . HOH CA 6 .   ? 19.149  -10.794 20.021  1.00 25.53 ? 683 HOH B O   1 
HETATM 9584  O  O   . HOH CA 6 .   ? 18.023  -11.301 17.844  1.00 25.93 ? 684 HOH B O   1 
HETATM 9585  O  O   . HOH CA 6 .   ? 2.061   -12.593 23.185  1.00 23.32 ? 685 HOH B O   1 
HETATM 9586  O  O   . HOH CA 6 .   ? 11.486  -11.781 -4.546  1.00 31.43 ? 686 HOH B O   1 
HETATM 9587  O  O   . HOH CA 6 .   ? 6.334   -14.962 32.927  1.00 27.45 ? 687 HOH B O   1 
HETATM 9588  O  O   . HOH CA 6 .   ? 6.325   -16.974 31.370  1.00 27.26 ? 688 HOH B O   1 
HETATM 9589  O  O   . HOH CA 6 .   ? 4.122   -6.834  30.561  1.00 40.80 ? 689 HOH B O   1 
HETATM 9590  O  O   . HOH CA 6 .   ? -3.708  -19.728 -6.335  1.00 34.51 ? 690 HOH B O   1 
HETATM 9591  O  O   . HOH CA 6 .   ? -7.253  -30.551 -3.077  1.00 29.61 ? 691 HOH B O   1 
HETATM 9592  O  O   . HOH CA 6 .   ? -11.295 -28.603 0.255   1.00 30.07 ? 692 HOH B O   1 
HETATM 9593  O  O   . HOH CA 6 .   ? -17.780 -26.630 -0.679  1.00 31.39 ? 693 HOH B O   1 
HETATM 9594  O  O   . HOH CA 6 .   ? -15.410 -22.817 -2.241  1.00 34.27 ? 694 HOH B O   1 
HETATM 9595  O  O   . HOH CA 6 .   ? -16.301 -17.578 -3.438  1.00 24.68 ? 695 HOH B O   1 
HETATM 9596  O  O   . HOH CA 6 .   ? 2.381   -30.105 5.499   1.00 35.93 ? 696 HOH B O   1 
HETATM 9597  O  O   . HOH CA 6 .   ? -8.395  -31.584 10.832  1.00 32.59 ? 697 HOH B O   1 
HETATM 9598  O  O   . HOH CA 6 .   ? -15.282 -29.364 12.191  1.00 41.05 ? 698 HOH B O   1 
HETATM 9599  O  O   . HOH CA 6 .   ? -16.515 -29.095 15.322  1.00 24.66 ? 699 HOH B O   1 
HETATM 9600  O  O   . HOH CA 6 .   ? -15.817 -5.228  20.776  1.00 31.42 ? 700 HOH B O   1 
HETATM 9601  O  O   . HOH CA 6 .   ? -9.186  -24.788 -7.143  1.00 35.28 ? 701 HOH B O   1 
HETATM 9602  O  O   . HOH CA 6 .   ? 14.644  7.415   4.413   1.00 31.28 ? 702 HOH B O   1 
HETATM 9603  O  O   . HOH CA 6 .   ? 18.865  -1.529  5.819   1.00 32.05 ? 703 HOH B O   1 
HETATM 9604  O  O   . HOH CA 6 .   ? 11.589  3.694   5.540   1.00 22.53 ? 704 HOH B O   1 
HETATM 9605  O  O   . HOH CA 6 .   ? 18.994  -3.630  -4.037  1.00 28.26 ? 705 HOH B O   1 
HETATM 9606  O  O   . HOH CA 6 .   ? 26.702  -11.519 1.567   1.00 14.59 ? 706 HOH B O   1 
HETATM 9607  O  O   . HOH CA 6 .   ? 26.600  -18.685 2.038   1.00 18.40 ? 707 HOH B O   1 
HETATM 9608  O  O   . HOH CA 6 .   ? 26.724  -17.919 -0.578  1.00 21.96 ? 708 HOH B O   1 
HETATM 9609  O  O   . HOH CA 6 .   ? 20.447  -18.733 -3.900  1.00 30.00 ? 709 HOH B O   1 
HETATM 9610  O  O   . HOH CA 6 .   ? -8.272  0.556   20.822  1.00 32.06 ? 710 HOH B O   1 
HETATM 9611  O  O   . HOH CA 6 .   ? -17.526 1.766   9.877   1.00 38.90 ? 711 HOH B O   1 
HETATM 9612  O  O   . HOH CA 6 .   ? 22.817  -18.660 0.983   1.00 30.46 ? 712 HOH B O   1 
HETATM 9613  O  O   . HOH CA 6 .   ? 9.171   -34.538 16.497  1.00 29.76 ? 713 HOH B O   1 
HETATM 9614  O  O   . HOH CA 6 .   ? -13.539 -10.427 24.880  1.00 25.98 ? 714 HOH B O   1 
HETATM 9615  O  O   . HOH CA 6 .   ? -12.409 -3.326  17.509  1.00 23.67 ? 715 HOH B O   1 
HETATM 9616  O  O   . HOH CA 6 .   ? -14.272 -5.992  18.545  1.00 27.15 ? 716 HOH B O   1 
HETATM 9617  O  O   . HOH CA 6 .   ? -5.621  -13.966 25.053  1.00 39.91 ? 717 HOH B O   1 
HETATM 9618  O  O   . HOH CA 6 .   ? 3.495   -24.323 28.554  1.00 29.09 ? 718 HOH B O   1 
HETATM 9619  O  O   . HOH CA 6 .   ? 19.341  -12.602 15.243  1.00 42.25 ? 719 HOH B O   1 
HETATM 9620  O  O   . HOH CA 6 .   ? 15.156  -10.912 32.132  1.00 39.88 ? 720 HOH B O   1 
HETATM 9621  O  O   . HOH CA 6 .   ? -19.620 -18.016 24.335  1.00 29.69 ? 721 HOH B O   1 
HETATM 9622  O  O   . HOH CA 6 .   ? -14.058 -6.358  -2.719  1.00 36.18 ? 722 HOH B O   1 
HETATM 9623  O  O   . HOH CA 6 .   ? 9.790   7.847   9.955   1.00 37.40 ? 723 HOH B O   1 
HETATM 9624  O  O   . HOH CA 6 .   ? 27.543  -11.660 -1.073  1.00 23.59 ? 724 HOH B O   1 
HETATM 9625  O  O   . HOH CA 6 .   ? 25.335  -19.141 5.357   1.00 31.74 ? 725 HOH B O   1 
HETATM 9626  O  O   . HOH CA 6 .   ? 27.161  -20.201 -2.421  1.00 38.28 ? 726 HOH B O   1 
HETATM 9627  O  O   . HOH CA 6 .   ? -3.465  -34.244 30.541  1.00 30.83 ? 727 HOH B O   1 
HETATM 9628  O  O   . HOH CA 6 .   ? 0.611   -14.379 23.333  1.00 24.16 ? 728 HOH B O   1 
HETATM 9629  O  O   . HOH CA 6 .   ? 2.221   -18.342 30.326  1.00 38.99 ? 729 HOH B O   1 
HETATM 9630  O  O   . HOH CA 6 .   ? 1.773   -15.803 31.330  1.00 30.39 ? 730 HOH B O   1 
HETATM 9631  O  O   . HOH CA 6 .   ? 12.761  -25.865 25.872  1.00 41.59 ? 731 HOH B O   1 
HETATM 9632  O  O   . HOH CA 6 .   ? 17.856  -24.513 21.288  1.00 32.45 ? 732 HOH B O   1 
HETATM 9633  O  O   . HOH CA 6 .   ? -14.846 -20.277 -6.119  1.00 29.14 ? 733 HOH B O   1 
HETATM 9634  O  O   . HOH CA 6 .   ? -16.549 -26.103 -4.352  1.00 37.61 ? 734 HOH B O   1 
HETATM 9635  O  O   . HOH CA 6 .   ? -12.789 -29.089 2.392   1.00 37.66 ? 735 HOH B O   1 
HETATM 9636  O  O   . HOH CA 6 .   ? -7.822  -33.543 6.604   1.00 46.22 ? 736 HOH B O   1 
HETATM 9637  O  O   . HOH CA 6 .   ? -2.113  -34.509 13.939  1.00 33.52 ? 737 HOH B O   1 
HETATM 9638  O  O   . HOH CA 6 .   ? 0.279   -35.301 15.483  1.00 32.70 ? 738 HOH B O   1 
HETATM 9639  O  O   . HOH CA 6 .   ? -0.229  -4.135  -4.042  1.00 28.58 ? 739 HOH B O   1 
HETATM 9640  O  O   . HOH CA 6 .   ? 13.954  -13.152 31.750  1.00 21.15 ? 740 HOH B O   1 
HETATM 9641  O  O   . HOH CA 6 .   ? 6.887   -20.591 30.373  1.00 34.31 ? 741 HOH B O   1 
HETATM 9642  O  O   . HOH CA 6 .   ? 10.121  -22.812 28.339  1.00 33.65 ? 742 HOH B O   1 
HETATM 9643  O  O   . HOH CA 6 .   ? -4.510  -34.039 1.197   1.00 43.96 ? 743 HOH B O   1 
HETATM 9644  O  O   . HOH CA 6 .   ? -10.915 -11.296 23.346  1.00 39.34 ? 744 HOH B O   1 
HETATM 9645  O  O   . HOH CA 6 .   ? -10.726 -32.734 19.340  1.00 38.73 ? 745 HOH B O   1 
HETATM 9646  O  O   . HOH CA 6 .   ? -7.966  -35.477 18.693  1.00 29.74 ? 746 HOH B O   1 
HETATM 9647  O  O   . HOH CA 6 .   ? 6.013   -28.403 6.153   1.00 40.14 ? 747 HOH B O   1 
HETATM 9648  O  O   . HOH CA 6 .   ? 6.631   -25.328 -3.020  1.00 34.00 ? 748 HOH B O   1 
HETATM 9649  O  O   . HOH CA 6 .   ? 8.237   -28.999 2.043   1.00 42.28 ? 749 HOH B O   1 
HETATM 9650  O  O   . HOH CA 6 .   ? -1.173  -1.576  23.442  1.00 27.91 ? 750 HOH B O   1 
HETATM 9651  O  O   . HOH CA 6 .   ? 18.281  -6.969  13.352  1.00 48.54 ? 751 HOH B O   1 
HETATM 9652  O  O   . HOH CA 6 .   ? 20.697  -13.469 27.682  1.00 30.91 ? 752 HOH B O   1 
HETATM 9653  O  O   . HOH CA 6 .   ? -19.486 -6.734  8.875   1.00 27.05 ? 753 HOH B O   1 
HETATM 9654  O  O   . HOH CA 6 .   ? 15.398  2.379   -1.745  1.00 36.97 ? 754 HOH B O   1 
HETATM 9655  O  O   . HOH CA 6 .   ? 19.675  1.869   0.646   1.00 39.01 ? 755 HOH B O   1 
HETATM 9656  O  O   . HOH CA 6 .   ? 22.691  0.009   -0.264  1.00 36.72 ? 756 HOH B O   1 
HETATM 9657  O  O   . HOH CA 6 .   ? 19.053  -26.250 5.067   1.00 47.75 ? 757 HOH B O   1 
HETATM 9658  O  O   . HOH CA 6 .   ? 16.200  -26.283 1.306   1.00 37.29 ? 758 HOH B O   1 
HETATM 9659  O  O   . HOH CA 6 .   ? 14.895  -19.658 -8.165  1.00 50.86 ? 759 HOH B O   1 
HETATM 9660  O  O   . HOH CA 6 .   ? 1.947   -13.575 -9.571  1.00 31.81 ? 760 HOH B O   1 
HETATM 9661  O  O   . HOH CA 6 .   ? -2.840  -6.751  24.628  1.00 33.88 ? 761 HOH B O   1 
HETATM 9662  O  O   . HOH CA 6 .   ? 6.174   -1.196  29.479  1.00 37.46 ? 762 HOH B O   1 
HETATM 9663  O  O   . HOH CA 6 .   ? -19.587 -22.311 -1.045  1.00 36.99 ? 763 HOH B O   1 
HETATM 9664  O  O   . HOH CA 6 .   ? 24.472  -20.482 1.595   1.00 31.38 ? 764 HOH B O   1 
HETATM 9665  O  O   . HOH CA 6 .   ? 23.801  -21.014 5.480   1.00 38.39 ? 765 HOH B O   1 
HETATM 9666  O  O   . HOH CA 6 .   ? 25.552  -10.548 -3.916  1.00 37.03 ? 766 HOH B O   1 
HETATM 9667  O  O   . HOH CA 6 .   ? -0.483  -30.806 5.502   1.00 36.11 ? 767 HOH B O   1 
HETATM 9668  O  O   . HOH CA 6 .   ? -1.171  -32.860 1.817   1.00 36.34 ? 768 HOH B O   1 
HETATM 9669  O  O   . HOH CA 6 .   ? -8.602  -30.961 22.820  1.00 24.07 ? 769 HOH B O   1 
HETATM 9670  O  O   . HOH CA 6 .   ? 2.264   -28.669 29.174  1.00 37.46 ? 770 HOH B O   1 
HETATM 9671  O  O   . HOH CA 6 .   ? 5.591   -31.907 29.915  1.00 33.44 ? 771 HOH B O   1 
HETATM 9672  O  O   . HOH CA 6 .   ? 7.429   -30.823 25.919  1.00 31.56 ? 772 HOH B O   1 
HETATM 9673  O  O   . HOH CA 6 .   ? 15.778  10.282  2.615   1.00 34.11 ? 773 HOH B O   1 
HETATM 9674  O  O   . HOH CA 6 .   ? 20.436  -18.603 23.735  1.00 44.75 ? 774 HOH B O   1 
HETATM 9675  O  O   . HOH CA 6 .   ? 19.481  -20.201 19.888  1.00 39.48 ? 775 HOH B O   1 
HETATM 9676  O  O   . HOH DA 6 .   ? 38.165  31.658  18.068  1.00 27.49 ? 401 HOH C O   1 
HETATM 9677  O  O   . HOH DA 6 .   ? 26.186  10.738  43.336  1.00 6.49  ? 402 HOH C O   1 
HETATM 9678  O  O   . HOH DA 6 .   ? 24.610  13.649  48.598  1.00 5.99  ? 403 HOH C O   1 
HETATM 9679  O  O   . HOH DA 6 .   ? 25.320  13.052  44.830  1.00 6.05  ? 404 HOH C O   1 
HETATM 9680  O  O   . HOH DA 6 .   ? 31.660  12.018  48.336  1.00 9.15  ? 405 HOH C O   1 
HETATM 9681  O  O   . HOH DA 6 .   ? 25.678  8.023   42.509  1.00 5.22  ? 406 HOH C O   1 
HETATM 9682  O  O   . HOH DA 6 .   ? 20.841  7.280   43.483  1.00 7.05  ? 407 HOH C O   1 
HETATM 9683  O  O   . HOH DA 6 .   ? 19.627  9.742   43.414  1.00 6.21  ? 408 HOH C O   1 
HETATM 9684  O  O   . HOH DA 6 .   ? 32.258  13.591  44.198  1.00 7.17  ? 409 HOH C O   1 
HETATM 9685  O  O   . HOH DA 6 .   ? 28.847  9.710   35.662  1.00 5.05  ? 410 HOH C O   1 
HETATM 9686  O  O   . HOH DA 6 .   ? 29.429  8.971   44.636  1.00 5.59  ? 411 HOH C O   1 
HETATM 9687  O  O   . HOH DA 6 .   ? 29.040  7.319   36.951  1.00 9.68  ? 412 HOH C O   1 
HETATM 9688  O  O   . HOH DA 6 .   ? 18.787  10.963  45.751  1.00 7.99  ? 413 HOH C O   1 
HETATM 9689  O  O   . HOH DA 6 .   ? 31.524  13.621  50.722  1.00 9.12  ? 414 HOH C O   1 
HETATM 9690  O  O   . HOH DA 6 .   ? 21.772  5.035   36.305  1.00 11.28 ? 415 HOH C O   1 
HETATM 9691  O  O   . HOH DA 6 .   ? 10.441  8.258   15.743  1.00 13.98 ? 416 HOH C O   1 
HETATM 9692  O  O   . HOH DA 6 .   ? 37.105  9.356   24.333  1.00 13.77 ? 417 HOH C O   1 
HETATM 9693  O  O   . HOH DA 6 .   ? 36.262  8.054   14.589  1.00 12.87 ? 418 HOH C O   1 
HETATM 9694  O  O   . HOH DA 6 .   ? 30.329  12.703  55.262  1.00 11.00 ? 419 HOH C O   1 
HETATM 9695  O  O   . HOH DA 6 .   ? 34.658  8.626   24.857  1.00 15.66 ? 420 HOH C O   1 
HETATM 9696  O  O   . HOH DA 6 .   ? 24.006  6.522   22.321  1.00 12.40 ? 421 HOH C O   1 
HETATM 9697  O  O   . HOH DA 6 .   ? 16.110  6.805   13.701  1.00 14.43 ? 422 HOH C O   1 
HETATM 9698  O  O   . HOH DA 6 .   ? 32.941  5.159   38.211  1.00 12.78 ? 423 HOH C O   1 
HETATM 9699  O  O   . HOH DA 6 .   ? 25.946  8.658   47.100  1.00 9.17  ? 424 HOH C O   1 
HETATM 9700  O  O   . HOH DA 6 .   ? 38.769  9.613   26.407  1.00 14.79 ? 425 HOH C O   1 
HETATM 9701  O  O   . HOH DA 6 .   ? 14.284  -1.406  25.374  1.00 16.35 ? 426 HOH C O   1 
HETATM 9702  O  O   . HOH DA 6 .   ? 23.040  -2.510  33.086  1.00 16.77 ? 427 HOH C O   1 
HETATM 9703  O  O   . HOH DA 6 .   ? 16.212  2.443   43.908  1.00 17.06 ? 428 HOH C O   1 
HETATM 9704  O  O   . HOH DA 6 .   ? 18.724  1.817   35.848  1.00 17.06 ? 429 HOH C O   1 
HETATM 9705  O  O   . HOH DA 6 .   ? 24.644  -0.527  32.189  1.00 14.64 ? 430 HOH C O   1 
HETATM 9706  O  O   . HOH DA 6 .   ? 22.339  -1.608  27.083  1.00 19.01 ? 431 HOH C O   1 
HETATM 9707  O  O   . HOH DA 6 .   ? 22.357  7.847   14.413  1.00 17.93 ? 432 HOH C O   1 
HETATM 9708  O  O   . HOH DA 6 .   ? 16.975  10.067  42.416  1.00 11.25 ? 433 HOH C O   1 
HETATM 9709  O  O   . HOH DA 6 .   ? 15.836  11.064  36.956  1.00 12.40 ? 434 HOH C O   1 
HETATM 9710  O  O   . HOH DA 6 .   ? 19.196  1.996   38.736  1.00 11.71 ? 435 HOH C O   1 
HETATM 9711  O  O   . HOH DA 6 .   ? 6.424   5.235   24.430  1.00 18.04 ? 436 HOH C O   1 
HETATM 9712  O  O   . HOH DA 6 .   ? 14.687  8.745   14.939  1.00 16.97 ? 437 HOH C O   1 
HETATM 9713  O  O   . HOH DA 6 .   ? 37.399  9.961   35.461  1.00 16.28 ? 438 HOH C O   1 
HETATM 9714  O  O   . HOH DA 6 .   ? 17.186  9.224   39.436  1.00 16.89 ? 439 HOH C O   1 
HETATM 9715  O  O   . HOH DA 6 .   ? 35.985  12.018  46.862  1.00 13.79 ? 440 HOH C O   1 
HETATM 9716  O  O   . HOH DA 6 .   ? 15.293  9.047   44.364  1.00 17.31 ? 441 HOH C O   1 
HETATM 9717  O  O   . HOH DA 6 .   ? 35.068  11.999  50.469  1.00 21.70 ? 442 HOH C O   1 
HETATM 9718  O  O   . HOH DA 6 .   ? 27.417  3.885   34.249  1.00 18.60 ? 443 HOH C O   1 
HETATM 9719  O  O   . HOH DA 6 .   ? 7.080   1.764   22.792  1.00 14.62 ? 444 HOH C O   1 
HETATM 9720  O  O   . HOH DA 6 .   ? 33.805  7.667   37.790  1.00 18.30 ? 445 HOH C O   1 
HETATM 9721  O  O   . HOH DA 6 .   ? 18.169  -0.334  39.759  1.00 19.91 ? 446 HOH C O   1 
HETATM 9722  O  O   . HOH DA 6 .   ? 8.239   -0.393  21.448  1.00 14.63 ? 447 HOH C O   1 
HETATM 9723  O  O   . HOH DA 6 .   ? 12.984  9.487   41.545  1.00 17.85 ? 448 HOH C O   1 
HETATM 9724  O  O   . HOH DA 6 .   ? 11.417  9.964   32.747  1.00 21.71 ? 449 HOH C O   1 
HETATM 9725  O  O   . HOH DA 6 .   ? 33.094  11.612  45.757  1.00 14.78 ? 450 HOH C O   1 
HETATM 9726  O  O   . HOH DA 6 .   ? 28.178  2.536   24.843  1.00 19.25 ? 451 HOH C O   1 
HETATM 9727  O  O   . HOH DA 6 .   ? 35.810  4.196   31.818  1.00 16.43 ? 452 HOH C O   1 
HETATM 9728  O  O   . HOH DA 6 .   ? 9.049   6.816   33.201  1.00 24.12 ? 453 HOH C O   1 
HETATM 9729  O  O   . HOH DA 6 .   ? 19.993  3.706   34.737  1.00 17.07 ? 454 HOH C O   1 
HETATM 9730  O  O   . HOH DA 6 .   ? 25.317  13.345  22.360  1.00 7.46  ? 455 HOH C O   1 
HETATM 9731  O  O   . HOH DA 6 .   ? 22.142  12.472  17.932  1.00 10.24 ? 456 HOH C O   1 
HETATM 9732  O  O   . HOH DA 6 .   ? 27.886  17.561  38.176  1.00 6.78  ? 457 HOH C O   1 
HETATM 9733  O  O   . HOH DA 6 .   ? 30.247  21.640  37.461  1.00 12.99 ? 458 HOH C O   1 
HETATM 9734  O  O   . HOH DA 6 .   ? 34.684  21.773  39.667  1.00 11.33 ? 459 HOH C O   1 
HETATM 9735  O  O   . HOH DA 6 .   ? 18.620  21.521  47.325  1.00 8.77  ? 460 HOH C O   1 
HETATM 9736  O  O   . HOH DA 6 .   ? 12.717  13.185  16.569  1.00 10.63 ? 461 HOH C O   1 
HETATM 9737  O  O   . HOH DA 6 .   ? 15.720  19.051  27.030  1.00 9.26  ? 462 HOH C O   1 
HETATM 9738  O  O   . HOH DA 6 .   ? 43.177  21.388  35.707  1.00 13.10 ? 463 HOH C O   1 
HETATM 9739  O  O   . HOH DA 6 .   ? 36.584  19.842  40.026  1.00 12.17 ? 464 HOH C O   1 
HETATM 9740  O  O   . HOH DA 6 .   ? 15.970  17.366  17.601  1.00 16.18 ? 465 HOH C O   1 
HETATM 9741  O  O   . HOH DA 6 .   ? 37.895  13.628  30.566  1.00 7.84  ? 466 HOH C O   1 
HETATM 9742  O  O   . HOH DA 6 .   ? 40.830  22.217  33.662  1.00 10.69 ? 467 HOH C O   1 
HETATM 9743  O  O   . HOH DA 6 .   ? 19.210  28.764  14.933  1.00 18.31 ? 468 HOH C O   1 
HETATM 9744  O  O   . HOH DA 6 .   ? 20.663  24.656  50.452  1.00 11.49 ? 469 HOH C O   1 
HETATM 9745  O  O   . HOH DA 6 .   ? 15.274  16.196  44.357  1.00 7.75  ? 470 HOH C O   1 
HETATM 9746  O  O   . HOH DA 6 .   ? 43.386  13.341  28.371  1.00 12.92 ? 471 HOH C O   1 
HETATM 9747  O  O   . HOH DA 6 .   ? 35.476  16.864  15.207  1.00 12.48 ? 472 HOH C O   1 
HETATM 9748  O  O   . HOH DA 6 .   ? 34.028  21.997  42.364  1.00 14.17 ? 473 HOH C O   1 
HETATM 9749  O  O   . HOH DA 6 .   ? 43.641  33.203  33.162  1.00 14.37 ? 474 HOH C O   1 
HETATM 9750  O  O   . HOH DA 6 .   ? 39.240  14.420  41.629  1.00 12.94 ? 475 HOH C O   1 
HETATM 9751  O  O   . HOH DA 6 .   ? 40.109  19.080  42.330  1.00 13.13 ? 476 HOH C O   1 
HETATM 9752  O  O   . HOH DA 6 .   ? 35.892  18.258  49.407  1.00 13.28 ? 477 HOH C O   1 
HETATM 9753  O  O   . HOH DA 6 .   ? 38.652  19.035  46.595  1.00 16.69 ? 478 HOH C O   1 
HETATM 9754  O  O   . HOH DA 6 .   ? 28.043  13.268  15.631  1.00 12.19 ? 479 HOH C O   1 
HETATM 9755  O  O   . HOH DA 6 .   ? 30.591  19.465  16.798  1.00 14.09 ? 480 HOH C O   1 
HETATM 9756  O  O   . HOH DA 6 .   ? 10.990  16.848  22.042  1.00 16.60 ? 481 HOH C O   1 
HETATM 9757  O  O   . HOH DA 6 .   ? 43.197  13.488  18.432  1.00 11.32 ? 482 HOH C O   1 
HETATM 9758  O  O   . HOH DA 6 .   ? 8.457   15.759  21.105  1.00 24.10 ? 483 HOH C O   1 
HETATM 9759  O  O   . HOH DA 6 .   ? 16.749  18.005  15.104  1.00 14.09 ? 484 HOH C O   1 
HETATM 9760  O  O   . HOH DA 6 .   ? 11.082  20.973  32.849  1.00 20.42 ? 485 HOH C O   1 
HETATM 9761  O  O   . HOH DA 6 .   ? 16.363  23.821  13.994  1.00 22.78 ? 486 HOH C O   1 
HETATM 9762  O  O   . HOH DA 6 .   ? 12.028  16.854  36.329  1.00 14.10 ? 487 HOH C O   1 
HETATM 9763  O  O   . HOH DA 6 .   ? 18.326  14.909  12.669  1.00 15.90 ? 488 HOH C O   1 
HETATM 9764  O  O   . HOH DA 6 .   ? 11.836  12.383  14.033  1.00 16.68 ? 489 HOH C O   1 
HETATM 9765  O  O   . HOH DA 6 .   ? 9.752   28.594  20.642  1.00 25.77 ? 490 HOH C O   1 
HETATM 9766  O  O   . HOH DA 6 .   ? 38.315  20.254  44.233  1.00 13.15 ? 491 HOH C O   1 
HETATM 9767  O  O   . HOH DA 6 .   ? 38.171  17.021  41.553  1.00 15.46 ? 492 HOH C O   1 
HETATM 9768  O  O   . HOH DA 6 .   ? 13.778  17.997  45.823  1.00 14.49 ? 493 HOH C O   1 
HETATM 9769  O  O   . HOH DA 6 .   ? 19.789  31.490  14.598  1.00 18.83 ? 494 HOH C O   1 
HETATM 9770  O  O   . HOH DA 6 .   ? 16.119  16.883  12.476  1.00 21.17 ? 495 HOH C O   1 
HETATM 9771  O  O   . HOH DA 6 .   ? 44.336  28.864  42.674  1.00 21.49 ? 496 HOH C O   1 
HETATM 9772  O  O   . HOH DA 6 .   ? 16.516  31.001  14.040  1.00 20.08 ? 497 HOH C O   1 
HETATM 9773  O  O   . HOH DA 6 .   ? 38.002  27.483  15.493  1.00 17.05 ? 498 HOH C O   1 
HETATM 9774  O  O   . HOH DA 6 .   ? 9.003   14.945  26.586  1.00 18.99 ? 499 HOH C O   1 
HETATM 9775  O  O   . HOH DA 6 .   ? 20.820  16.728  12.592  1.00 23.83 ? 500 HOH C O   1 
HETATM 9776  O  O   . HOH DA 6 .   ? 18.831  24.149  48.517  1.00 12.54 ? 501 HOH C O   1 
HETATM 9777  O  O   . HOH DA 6 .   ? 46.588  20.477  24.890  1.00 16.22 ? 502 HOH C O   1 
HETATM 9778  O  O   . HOH DA 6 .   ? 13.998  5.618   41.046  1.00 25.67 ? 503 HOH C O   1 
HETATM 9779  O  O   . HOH DA 6 .   ? 48.644  18.635  24.214  1.00 23.35 ? 504 HOH C O   1 
HETATM 9780  O  O   . HOH DA 6 .   ? 24.556  24.769  52.377  1.00 23.04 ? 505 HOH C O   1 
HETATM 9781  O  O   . HOH DA 6 .   ? 32.341  15.783  15.840  1.00 14.24 ? 506 HOH C O   1 
HETATM 9782  O  O   . HOH DA 6 .   ? 35.181  8.131   34.938  1.00 21.67 ? 507 HOH C O   1 
HETATM 9783  O  O   . HOH DA 6 .   ? 35.974  19.698  42.808  1.00 15.53 ? 508 HOH C O   1 
HETATM 9784  O  O   . HOH DA 6 .   ? 42.948  26.465  21.299  1.00 25.37 ? 509 HOH C O   1 
HETATM 9785  O  O   . HOH DA 6 .   ? 36.764  20.109  51.037  1.00 20.53 ? 510 HOH C O   1 
HETATM 9786  O  O   . HOH DA 6 .   ? 37.480  12.662  52.228  1.00 19.50 ? 511 HOH C O   1 
HETATM 9787  O  O   . HOH DA 6 .   ? 3.477   8.897   23.063  1.00 27.94 ? 512 HOH C O   1 
HETATM 9788  O  O   . HOH DA 6 .   ? 3.627   2.647   26.416  1.00 32.43 ? 513 HOH C O   1 
HETATM 9789  O  O   . HOH DA 6 .   ? 12.549  22.112  43.291  1.00 25.18 ? 514 HOH C O   1 
HETATM 9790  O  O   . HOH DA 6 .   ? 35.224  24.038  43.723  1.00 15.12 ? 515 HOH C O   1 
HETATM 9791  O  O   . HOH DA 6 .   ? 21.630  27.198  49.916  1.00 23.11 ? 516 HOH C O   1 
HETATM 9792  O  O   . HOH DA 6 .   ? 45.200  15.179  17.397  1.00 17.80 ? 517 HOH C O   1 
HETATM 9793  O  O   . HOH DA 6 .   ? 22.866  15.010  10.768  1.00 20.52 ? 518 HOH C O   1 
HETATM 9794  O  O   . HOH DA 6 .   ? 29.327  18.316  50.134  1.00 15.68 ? 519 HOH C O   1 
HETATM 9795  O  O   . HOH DA 6 .   ? 16.133  23.992  49.322  1.00 20.11 ? 520 HOH C O   1 
HETATM 9796  O  O   . HOH DA 6 .   ? 19.786  6.128   12.332  1.00 22.10 ? 521 HOH C O   1 
HETATM 9797  O  O   . HOH DA 6 .   ? 33.752  6.930   22.939  1.00 20.56 ? 522 HOH C O   1 
HETATM 9798  O  O   . HOH DA 6 .   ? 45.340  11.491  28.895  1.00 25.08 ? 523 HOH C O   1 
HETATM 9799  O  O   . HOH DA 6 .   ? 10.038  24.321  23.058  1.00 17.88 ? 524 HOH C O   1 
HETATM 9800  O  O   . HOH DA 6 .   ? 40.897  34.522  40.378  1.00 22.45 ? 525 HOH C O   1 
HETATM 9801  O  O   . HOH DA 6 .   ? 11.221  18.674  44.976  1.00 32.55 ? 526 HOH C O   1 
HETATM 9802  O  O   . HOH DA 6 .   ? 21.644  -1.824  35.133  1.00 29.29 ? 527 HOH C O   1 
HETATM 9803  O  O   . HOH DA 6 .   ? 24.228  0.917   23.438  1.00 32.27 ? 528 HOH C O   1 
HETATM 9804  O  O   . HOH DA 6 .   ? 10.247  9.692   17.954  1.00 17.04 ? 529 HOH C O   1 
HETATM 9805  O  O   . HOH DA 6 .   ? 9.783   34.434  24.405  1.00 28.03 ? 530 HOH C O   1 
HETATM 9806  O  O   . HOH DA 6 .   ? 44.410  19.224  18.208  1.00 18.84 ? 531 HOH C O   1 
HETATM 9807  O  O   . HOH DA 6 .   ? 46.539  22.777  23.212  1.00 27.15 ? 532 HOH C O   1 
HETATM 9808  O  O   . HOH DA 6 .   ? 29.679  15.269  14.792  1.00 19.17 ? 533 HOH C O   1 
HETATM 9809  O  O   . HOH DA 6 .   ? 12.363  14.980  46.401  1.00 27.24 ? 534 HOH C O   1 
HETATM 9810  O  O   . HOH DA 6 .   ? 27.362  27.176  10.971  1.00 20.57 ? 535 HOH C O   1 
HETATM 9811  O  O   . HOH DA 6 .   ? 23.682  18.431  13.534  1.00 20.68 ? 536 HOH C O   1 
HETATM 9812  O  O   . HOH DA 6 .   ? 21.027  30.406  34.347  1.00 24.59 ? 537 HOH C O   1 
HETATM 9813  O  O   . HOH DA 6 .   ? 19.383  -3.141  23.008  1.00 18.85 ? 538 HOH C O   1 
HETATM 9814  O  O   . HOH DA 6 .   ? 28.152  19.797  55.216  1.00 23.19 ? 539 HOH C O   1 
HETATM 9815  O  O   . HOH DA 6 .   ? 28.834  17.889  15.087  1.00 18.34 ? 540 HOH C O   1 
HETATM 9816  O  O   . HOH DA 6 .   ? 14.313  15.234  11.282  1.00 22.34 ? 541 HOH C O   1 
HETATM 9817  O  O   . HOH DA 6 .   ? 44.894  18.007  35.016  1.00 20.60 ? 542 HOH C O   1 
HETATM 9818  O  O   . HOH DA 6 .   ? 13.848  -1.126  20.329  1.00 19.78 ? 543 HOH C O   1 
HETATM 9819  O  O   . HOH DA 6 .   ? 6.430   25.017  40.933  1.00 25.02 ? 544 HOH C O   1 
HETATM 9820  O  O   . HOH DA 6 .   ? 18.796  26.313  46.886  1.00 21.48 ? 545 HOH C O   1 
HETATM 9821  O  O   . HOH DA 6 .   ? 30.501  17.446  54.004  1.00 29.72 ? 546 HOH C O   1 
HETATM 9822  O  O   . HOH DA 6 .   ? 26.573  2.718   22.680  1.00 29.80 ? 547 HOH C O   1 
HETATM 9823  O  O   . HOH DA 6 .   ? 36.242  5.902   33.918  1.00 23.26 ? 548 HOH C O   1 
HETATM 9824  O  O   . HOH DA 6 .   ? 18.739  3.669   14.473  1.00 27.25 ? 549 HOH C O   1 
HETATM 9825  O  O   . HOH DA 6 .   ? 21.538  27.521  14.016  1.00 18.45 ? 550 HOH C O   1 
HETATM 9826  O  O   . HOH DA 6 .   ? 46.079  23.705  29.478  1.00 31.12 ? 551 HOH C O   1 
HETATM 9827  O  O   . HOH DA 6 .   ? 34.461  40.810  31.741  1.00 21.40 ? 552 HOH C O   1 
HETATM 9828  O  O   . HOH DA 6 .   ? 48.641  29.359  35.895  1.00 40.67 ? 553 HOH C O   1 
HETATM 9829  O  O   . HOH DA 6 .   ? 25.674  21.051  55.843  1.00 18.01 ? 554 HOH C O   1 
HETATM 9830  O  O   . HOH DA 6 .   ? 34.115  4.211   29.879  1.00 32.61 ? 555 HOH C O   1 
HETATM 9831  O  O   . HOH DA 6 .   ? 30.465  21.371  13.739  1.00 26.40 ? 556 HOH C O   1 
HETATM 9832  O  O   . HOH DA 6 .   ? 21.072  19.839  14.234  1.00 25.92 ? 557 HOH C O   1 
HETATM 9833  O  O   . HOH DA 6 .   ? 12.151  -0.954  37.893  1.00 24.08 ? 558 HOH C O   1 
HETATM 9834  O  O   . HOH DA 6 .   ? 5.680   28.736  22.934  1.00 29.45 ? 559 HOH C O   1 
HETATM 9835  O  O   . HOH DA 6 .   ? 10.833  18.700  34.565  1.00 25.33 ? 560 HOH C O   1 
HETATM 9836  O  O   . HOH DA 6 .   ? 26.108  20.404  13.941  1.00 28.79 ? 561 HOH C O   1 
HETATM 9837  O  O   . HOH DA 6 .   ? 44.448  20.017  42.619  1.00 20.94 ? 562 HOH C O   1 
HETATM 9838  O  O   . HOH DA 6 .   ? 22.834  25.532  11.280  1.00 27.19 ? 563 HOH C O   1 
HETATM 9839  O  O   . HOH DA 6 .   ? 34.093  24.612  46.137  1.00 20.12 ? 564 HOH C O   1 
HETATM 9840  O  O   . HOH DA 6 .   ? 7.129   24.684  21.044  1.00 24.18 ? 565 HOH C O   1 
HETATM 9841  O  O   . HOH DA 6 .   ? 35.490  39.519  29.804  1.00 26.69 ? 566 HOH C O   1 
HETATM 9842  O  O   . HOH DA 6 .   ? 9.392   10.520  36.043  1.00 27.76 ? 567 HOH C O   1 
HETATM 9843  O  O   . HOH DA 6 .   ? 45.449  15.963  36.893  1.00 30.77 ? 568 HOH C O   1 
HETATM 9844  O  O   . HOH DA 6 .   ? 23.184  4.380   20.082  1.00 22.32 ? 569 HOH C O   1 
HETATM 9845  O  O   . HOH DA 6 .   ? 9.385   19.945  36.658  1.00 28.84 ? 570 HOH C O   1 
HETATM 9846  O  O   . HOH DA 6 .   ? 39.533  30.314  45.832  1.00 20.33 ? 571 HOH C O   1 
HETATM 9847  O  O   . HOH DA 6 .   ? 22.700  0.805   34.690  1.00 24.31 ? 572 HOH C O   1 
HETATM 9848  O  O   . HOH DA 6 .   ? 31.405  11.374  16.613  1.00 22.57 ? 573 HOH C O   1 
HETATM 9849  O  O   . HOH DA 6 .   ? 16.101  20.411  14.095  1.00 23.03 ? 574 HOH C O   1 
HETATM 9850  O  O   . HOH DA 6 .   ? 34.306  19.119  13.683  1.00 22.89 ? 575 HOH C O   1 
HETATM 9851  O  O   . HOH DA 6 .   ? 15.070  22.141  47.544  1.00 24.45 ? 576 HOH C O   1 
HETATM 9852  O  O   . HOH DA 6 .   ? 10.499  16.041  44.499  1.00 23.76 ? 577 HOH C O   1 
HETATM 9853  O  O   . HOH DA 6 .   ? 31.923  42.224  31.526  1.00 25.22 ? 578 HOH C O   1 
HETATM 9854  O  O   . HOH DA 6 .   ? 25.340  27.353  46.519  1.00 31.92 ? 579 HOH C O   1 
HETATM 9855  O  O   . HOH DA 6 .   ? 41.832  36.632  33.061  1.00 34.79 ? 580 HOH C O   1 
HETATM 9856  O  O   . HOH DA 6 .   ? 44.522  25.771  26.392  1.00 24.10 ? 581 HOH C O   1 
HETATM 9857  O  O   . HOH DA 6 .   ? 30.971  6.408   19.819  1.00 22.06 ? 582 HOH C O   1 
HETATM 9858  O  O   . HOH DA 6 .   ? 21.778  -3.901  30.936  1.00 22.97 ? 583 HOH C O   1 
HETATM 9859  O  O   . HOH DA 6 .   ? 5.137   23.007  29.399  1.00 26.94 ? 584 HOH C O   1 
HETATM 9860  O  O   . HOH DA 6 .   ? 43.171  28.091  25.745  1.00 22.08 ? 585 HOH C O   1 
HETATM 9861  O  O   . HOH DA 6 .   ? 28.262  24.698  49.207  1.00 28.94 ? 586 HOH C O   1 
HETATM 9862  O  O   . HOH DA 6 .   ? 40.566  7.168   24.004  1.00 26.00 ? 587 HOH C O   1 
HETATM 9863  O  O   . HOH DA 6 .   ? 41.333  9.612   25.670  1.00 23.97 ? 588 HOH C O   1 
HETATM 9864  O  O   . HOH DA 6 .   ? 40.965  25.168  48.271  1.00 19.13 ? 589 HOH C O   1 
HETATM 9865  O  O   . HOH DA 6 .   ? 45.241  36.161  30.142  1.00 27.10 ? 590 HOH C O   1 
HETATM 9866  O  O   . HOH DA 6 .   ? 26.617  26.533  44.311  1.00 24.22 ? 591 HOH C O   1 
HETATM 9867  O  O   . HOH DA 6 .   ? 24.833  26.114  42.138  1.00 17.35 ? 592 HOH C O   1 
HETATM 9868  O  O   . HOH DA 6 .   ? 23.775  29.558  35.538  1.00 23.75 ? 593 HOH C O   1 
HETATM 9869  O  O   . HOH DA 6 .   ? 17.685  34.419  32.778  1.00 20.41 ? 594 HOH C O   1 
HETATM 9870  O  O   . HOH DA 6 .   ? 23.310  -3.173  28.743  1.00 23.82 ? 595 HOH C O   1 
HETATM 9871  O  O   . HOH DA 6 .   ? 13.607  20.087  12.595  1.00 43.34 ? 596 HOH C O   1 
HETATM 9872  O  O   . HOH DA 6 .   ? 23.665  35.740  13.126  1.00 30.88 ? 597 HOH C O   1 
HETATM 9873  O  O   . HOH DA 6 .   ? 31.946  3.671   32.853  1.00 26.79 ? 598 HOH C O   1 
HETATM 9874  O  O   . HOH DA 6 .   ? 7.780   19.794  27.298  1.00 37.47 ? 599 HOH C O   1 
HETATM 9875  O  O   . HOH DA 6 .   ? 33.959  15.230  13.692  1.00 17.58 ? 600 HOH C O   1 
HETATM 9876  O  O   . HOH DA 6 .   ? 33.525  22.094  14.052  1.00 25.39 ? 601 HOH C O   1 
HETATM 9877  O  O   . HOH DA 6 .   ? 44.340  16.991  15.523  1.00 21.78 ? 602 HOH C O   1 
HETATM 9878  O  O   . HOH DA 6 .   ? 15.630  6.148   11.179  1.00 17.84 ? 603 HOH C O   1 
HETATM 9879  O  O   . HOH DA 6 .   ? 27.863  10.867  14.239  1.00 25.15 ? 604 HOH C O   1 
HETATM 9880  O  O   . HOH DA 6 .   ? 46.029  21.753  35.847  1.00 27.24 ? 605 HOH C O   1 
HETATM 9881  O  O   . HOH DA 6 .   ? 11.906  0.230   42.626  1.00 26.70 ? 606 HOH C O   1 
HETATM 9882  O  O   . HOH DA 6 .   ? 14.764  2.069   22.052  1.00 20.13 ? 607 HOH C O   1 
HETATM 9883  O  O   . HOH DA 6 .   ? 22.892  28.293  41.907  1.00 21.73 ? 608 HOH C O   1 
HETATM 9884  O  O   . HOH DA 6 .   ? 27.367  24.274  39.362  1.00 21.84 ? 609 HOH C O   1 
HETATM 9885  O  O   . HOH DA 6 .   ? 26.679  26.601  40.192  1.00 29.97 ? 610 HOH C O   1 
HETATM 9886  O  O   . HOH DA 6 .   ? 26.179  27.698  37.434  1.00 22.52 ? 611 HOH C O   1 
HETATM 9887  O  O   . HOH DA 6 .   ? 17.418  26.946  42.512  1.00 24.76 ? 612 HOH C O   1 
HETATM 9888  O  O   . HOH DA 6 .   ? 13.811  -1.065  35.932  1.00 33.55 ? 613 HOH C O   1 
HETATM 9889  O  O   . HOH DA 6 .   ? 16.015  4.193   14.856  1.00 19.04 ? 614 HOH C O   1 
HETATM 9890  O  O   . HOH DA 6 .   ? 21.425  3.022   23.854  1.00 24.04 ? 615 HOH C O   1 
HETATM 9891  O  O   . HOH DA 6 .   ? 26.734  5.432   22.109  1.00 25.29 ? 616 HOH C O   1 
HETATM 9892  O  O   . HOH DA 6 .   ? 27.486  30.020  37.504  1.00 22.71 ? 617 HOH C O   1 
HETATM 9893  O  O   . HOH DA 6 .   ? 17.900  28.193  48.600  1.00 32.01 ? 618 HOH C O   1 
HETATM 9894  O  O   . HOH DA 6 .   ? 27.658  36.687  34.047  1.00 25.30 ? 619 HOH C O   1 
HETATM 9895  O  O   . HOH DA 6 .   ? 23.810  38.541  30.323  1.00 24.06 ? 620 HOH C O   1 
HETATM 9896  O  O   . HOH DA 6 .   ? 20.099  37.488  27.855  1.00 28.72 ? 621 HOH C O   1 
HETATM 9897  O  O   . HOH DA 6 .   ? 19.920  38.632  25.831  1.00 34.56 ? 622 HOH C O   1 
HETATM 9898  O  O   . HOH DA 6 .   ? 13.229  26.603  13.215  1.00 41.38 ? 623 HOH C O   1 
HETATM 9899  O  O   . HOH DA 6 .   ? 9.274   19.144  17.961  1.00 30.22 ? 624 HOH C O   1 
HETATM 9900  O  O   . HOH DA 6 .   ? 7.478   9.682   14.547  1.00 47.67 ? 625 HOH C O   1 
HETATM 9901  O  O   . HOH DA 6 .   ? 13.395  0.067   22.775  1.00 25.88 ? 626 HOH C O   1 
HETATM 9902  O  O   . HOH DA 6 .   ? 9.902   17.434  40.123  1.00 31.29 ? 627 HOH C O   1 
HETATM 9903  O  O   . HOH DA 6 .   ? 13.970  1.930   35.953  1.00 26.12 ? 628 HOH C O   1 
HETATM 9904  O  O   . HOH DA 6 .   ? 22.282  37.891  13.427  1.00 30.50 ? 629 HOH C O   1 
HETATM 9905  O  O   . HOH DA 6 .   ? 33.479  36.861  37.409  1.00 28.63 ? 630 HOH C O   1 
HETATM 9906  O  O   . HOH DA 6 .   ? 24.027  38.822  24.950  1.00 36.04 ? 631 HOH C O   1 
HETATM 9907  O  O   . HOH DA 6 .   ? 22.006  39.981  24.879  1.00 47.89 ? 632 HOH C O   1 
HETATM 9908  O  O   . HOH DA 6 .   ? 30.178  3.174   34.488  1.00 27.44 ? 633 HOH C O   1 
HETATM 9909  O  O   . HOH DA 6 .   ? 2.302   31.645  31.821  1.00 31.67 ? 634 HOH C O   1 
HETATM 9910  O  O   . HOH DA 6 .   ? 40.370  26.223  14.703  1.00 29.40 ? 635 HOH C O   1 
HETATM 9911  O  O   . HOH DA 6 .   ? 43.686  24.514  18.570  1.00 28.20 ? 636 HOH C O   1 
HETATM 9912  O  O   . HOH DA 6 .   ? 42.286  23.557  22.268  1.00 17.93 ? 637 HOH C O   1 
HETATM 9913  O  O   . HOH DA 6 .   ? 42.118  38.081  37.370  1.00 28.24 ? 638 HOH C O   1 
HETATM 9914  O  O   . HOH DA 6 .   ? 46.059  33.653  33.784  1.00 40.29 ? 639 HOH C O   1 
HETATM 9915  O  O   . HOH DA 6 .   ? 18.034  12.817  11.201  1.00 42.02 ? 640 HOH C O   1 
HETATM 9916  O  O   . HOH DA 6 .   ? 18.424  9.588   9.345   1.00 35.93 ? 641 HOH C O   1 
HETATM 9917  O  O   . HOH DA 6 .   ? 9.692   19.184  32.635  1.00 33.03 ? 642 HOH C O   1 
HETATM 9918  O  O   . HOH DA 6 .   ? 44.791  19.246  15.418  1.00 29.84 ? 643 HOH C O   1 
HETATM 9919  O  O   . HOH DA 6 .   ? 47.434  25.160  33.462  1.00 26.38 ? 644 HOH C O   1 
HETATM 9920  O  O   . HOH DA 6 .   ? 48.075  29.895  44.901  1.00 33.61 ? 645 HOH C O   1 
HETATM 9921  O  O   . HOH DA 6 .   ? 42.401  18.332  43.550  1.00 24.81 ? 646 HOH C O   1 
HETATM 9922  O  O   . HOH DA 6 .   ? 41.772  19.074  46.014  1.00 30.05 ? 647 HOH C O   1 
HETATM 9923  O  O   . HOH DA 6 .   ? 39.383  20.131  49.090  1.00 29.26 ? 648 HOH C O   1 
HETATM 9924  O  O   . HOH DA 6 .   ? 9.910   9.979   41.121  1.00 30.87 ? 649 HOH C O   1 
HETATM 9925  O  O   . HOH DA 6 .   ? 18.376  10.287  49.793  1.00 15.90 ? 650 HOH C O   1 
HETATM 9926  O  O   . HOH DA 6 .   ? 19.771  34.390  28.826  1.00 17.63 ? 651 HOH C O   1 
HETATM 9927  O  O   . HOH DA 6 .   ? 20.230  34.080  31.491  1.00 17.57 ? 652 HOH C O   1 
HETATM 9928  O  O   . HOH DA 6 .   ? 22.838  34.487  30.228  1.00 16.90 ? 653 HOH C O   1 
HETATM 9929  O  O   . HOH DA 6 .   ? 22.781  36.708  28.635  1.00 17.89 ? 654 HOH C O   1 
HETATM 9930  O  O   . HOH DA 6 .   ? 25.320  32.656  33.631  1.00 24.56 ? 655 HOH C O   1 
HETATM 9931  O  O   . HOH DA 6 .   ? 29.679  33.321  31.778  1.00 12.08 ? 656 HOH C O   1 
HETATM 9932  O  O   . HOH DA 6 .   ? 26.500  38.143  30.132  1.00 17.90 ? 657 HOH C O   1 
HETATM 9933  O  O   . HOH DA 6 .   ? 27.548  40.382  31.754  1.00 20.56 ? 658 HOH C O   1 
HETATM 9934  O  O   . HOH DA 6 .   ? 27.226  37.599  27.686  1.00 12.62 ? 659 HOH C O   1 
HETATM 9935  O  O   . HOH DA 6 .   ? 24.678  36.909  26.639  1.00 19.86 ? 660 HOH C O   1 
HETATM 9936  O  O   . HOH DA 6 .   ? 30.494  36.244  35.058  1.00 24.00 ? 661 HOH C O   1 
HETATM 9937  O  O   . HOH DA 6 .   ? 40.135  36.985  30.231  1.00 16.29 ? 662 HOH C O   1 
HETATM 9938  O  O   . HOH DA 6 .   ? 39.109  38.104  34.068  1.00 24.47 ? 663 HOH C O   1 
HETATM 9939  O  O   . HOH DA 6 .   ? 27.360  33.263  13.725  1.00 18.72 ? 664 HOH C O   1 
HETATM 9940  O  O   . HOH DA 6 .   ? 26.794  36.450  12.343  1.00 28.28 ? 665 HOH C O   1 
HETATM 9941  O  O   . HOH DA 6 .   ? 29.649  29.809  13.406  1.00 17.18 ? 666 HOH C O   1 
HETATM 9942  O  O   . HOH DA 6 .   ? 32.424  31.804  13.827  1.00 21.02 ? 667 HOH C O   1 
HETATM 9943  O  O   . HOH DA 6 .   ? 34.315  32.968  15.892  1.00 19.40 ? 668 HOH C O   1 
HETATM 9944  O  O   . HOH DA 6 .   ? 33.821  32.713  18.466  1.00 11.40 ? 669 HOH C O   1 
HETATM 9945  O  O   . HOH DA 6 .   ? 36.262  32.420  19.838  1.00 11.99 ? 670 HOH C O   1 
HETATM 9946  O  O   . HOH DA 6 .   ? 28.221  42.287  22.227  1.00 23.62 ? 671 HOH C O   1 
HETATM 9947  O  O   . HOH DA 6 .   ? 42.128  28.640  50.591  1.00 24.26 ? 672 HOH C O   1 
HETATM 9948  O  O   . HOH DA 6 .   ? 5.639   1.418   29.702  1.00 33.47 ? 673 HOH C O   1 
HETATM 9949  O  O   . HOH DA 6 .   ? 5.448   7.394   26.099  1.00 35.93 ? 674 HOH C O   1 
HETATM 9950  O  O   . HOH DA 6 .   ? 33.765  41.760  35.892  1.00 30.35 ? 675 HOH C O   1 
HETATM 9951  O  O   . HOH DA 6 .   ? 30.796  40.372  34.792  1.00 24.41 ? 676 HOH C O   1 
HETATM 9952  O  O   . HOH DA 6 .   ? 29.715  41.937  30.234  1.00 25.96 ? 677 HOH C O   1 
HETATM 9953  O  O   . HOH DA 6 .   ? 17.750  10.323  11.977  1.00 26.42 ? 678 HOH C O   1 
HETATM 9954  O  O   . HOH DA 6 .   ? 35.961  23.638  48.934  1.00 41.48 ? 679 HOH C O   1 
HETATM 9955  O  O   . HOH DA 6 .   ? 37.671  22.282  49.998  1.00 34.46 ? 680 HOH C O   1 
HETATM 9956  O  O   . HOH DA 6 .   ? 32.127  22.106  54.424  1.00 27.58 ? 681 HOH C O   1 
HETATM 9957  O  O   . HOH DA 6 .   ? 13.089  16.788  48.305  1.00 33.79 ? 682 HOH C O   1 
HETATM 9958  O  O   . HOH DA 6 .   ? 18.263  22.111  13.110  1.00 32.63 ? 683 HOH C O   1 
HETATM 9959  O  O   . HOH DA 6 .   ? 22.357  36.798  18.059  1.00 17.86 ? 684 HOH C O   1 
HETATM 9960  O  O   . HOH DA 6 .   ? 20.581  34.766  18.389  1.00 16.76 ? 685 HOH C O   1 
HETATM 9961  O  O   . HOH DA 6 .   ? 21.632  37.681  20.671  1.00 19.76 ? 686 HOH C O   1 
HETATM 9962  O  O   . HOH DA 6 .   ? 18.717  39.184  23.003  1.00 23.74 ? 687 HOH C O   1 
HETATM 9963  O  O   . HOH DA 6 .   ? 13.625  33.062  23.375  1.00 21.82 ? 688 HOH C O   1 
HETATM 9964  O  O   . HOH DA 6 .   ? 31.154  42.838  19.655  1.00 19.88 ? 689 HOH C O   1 
HETATM 9965  O  O   . HOH DA 6 .   ? 29.536  44.765  16.279  1.00 20.35 ? 690 HOH C O   1 
HETATM 9966  O  O   . HOH DA 6 .   ? 16.635  36.535  17.698  1.00 18.86 ? 691 HOH C O   1 
HETATM 9967  O  O   . HOH DA 6 .   ? 14.794  33.563  18.044  1.00 29.97 ? 692 HOH C O   1 
HETATM 9968  O  O   . HOH DA 6 .   ? 8.659   32.555  26.011  1.00 12.77 ? 693 HOH C O   1 
HETATM 9969  O  O   . HOH DA 6 .   ? 18.449  34.363  35.758  1.00 23.91 ? 694 HOH C O   1 
HETATM 9970  O  O   . HOH DA 6 .   ? 44.285  22.113  21.535  1.00 24.73 ? 695 HOH C O   1 
HETATM 9971  O  O   . HOH DA 6 .   ? 39.123  29.555  17.705  1.00 39.77 ? 696 HOH C O   1 
HETATM 9972  O  O   . HOH DA 6 .   ? 37.607  40.374  31.984  1.00 42.53 ? 697 HOH C O   1 
HETATM 9973  O  O   . HOH DA 6 .   ? 4.760   15.031  18.896  1.00 33.97 ? 698 HOH C O   1 
HETATM 9974  O  O   . HOH DA 6 .   ? 12.000  -0.930  28.695  1.00 34.37 ? 699 HOH C O   1 
HETATM 9975  O  O   . HOH DA 6 .   ? 21.015  -5.282  24.525  1.00 30.54 ? 700 HOH C O   1 
HETATM 9976  O  O   . HOH DA 6 .   ? 22.347  -2.597  24.367  1.00 40.38 ? 701 HOH C O   1 
HETATM 9977  O  O   . HOH DA 6 .   ? 19.474  1.439   15.685  1.00 40.86 ? 702 HOH C O   1 
HETATM 9978  O  O   . HOH DA 6 .   ? 23.348  5.540   15.431  1.00 33.58 ? 703 HOH C O   1 
HETATM 9979  O  O   . HOH DA 6 .   ? 22.434  6.198   10.951  1.00 41.32 ? 704 HOH C O   1 
HETATM 9980  O  O   . HOH DA 6 .   ? 31.205  25.401  46.166  1.00 33.29 ? 705 HOH C O   1 
HETATM 9981  O  O   . HOH DA 6 .   ? 35.536  13.998  41.102  1.00 23.15 ? 706 HOH C O   1 
HETATM 9982  O  O   . HOH DA 6 .   ? 25.752  9.712   51.381  1.00 6.19  ? 707 HOH C O   1 
HETATM 9983  O  O   . HOH DA 6 .   ? 30.730  16.464  55.977  1.00 33.82 ? 708 HOH C O   1 
HETATM 9984  O  O   . HOH DA 6 .   ? 8.555   12.906  41.563  1.00 30.04 ? 709 HOH C O   1 
HETATM 9985  O  O   . HOH DA 6 .   ? 8.204   13.033  36.971  1.00 23.15 ? 710 HOH C O   1 
HETATM 9986  O  O   . HOH DA 6 .   ? 9.579   12.495  29.468  1.00 36.93 ? 711 HOH C O   1 
HETATM 9987  O  O   . HOH DA 6 .   ? 7.548   11.945  39.142  1.00 38.19 ? 712 HOH C O   1 
HETATM 9988  O  O   . HOH DA 6 .   ? 25.687  1.929   35.433  1.00 22.41 ? 713 HOH C O   1 
HETATM 9989  O  O   . HOH DA 6 .   ? 31.632  3.813   36.084  1.00 26.30 ? 714 HOH C O   1 
HETATM 9990  O  O   . HOH DA 6 .   ? 9.497   29.534  18.185  1.00 30.13 ? 715 HOH C O   1 
HETATM 9991  O  O   . HOH DA 6 .   ? 17.998  25.028  12.875  1.00 39.91 ? 716 HOH C O   1 
HETATM 9992  O  O   . HOH DA 6 .   ? 20.042  34.795  15.485  1.00 40.44 ? 717 HOH C O   1 
HETATM 9993  O  O   . HOH DA 6 .   ? 13.491  34.949  20.308  1.00 27.29 ? 718 HOH C O   1 
HETATM 9994  O  O   . HOH DA 6 .   ? 32.571  35.351  15.408  1.00 23.11 ? 719 HOH C O   1 
HETATM 9995  O  O   . HOH DA 6 .   ? 36.794  32.416  15.207  1.00 33.37 ? 720 HOH C O   1 
HETATM 9996  O  O   . HOH DA 6 .   ? 28.128  34.148  36.663  1.00 46.86 ? 721 HOH C O   1 
HETATM 9997  O  O   . HOH DA 6 .   ? 32.043  33.511  39.185  1.00 45.76 ? 722 HOH C O   1 
HETATM 9998  O  O   . HOH DA 6 .   ? 34.313  34.810  41.816  1.00 35.51 ? 723 HOH C O   1 
HETATM 9999  O  O   . HOH DA 6 .   ? 36.115  27.130  44.320  1.00 29.59 ? 724 HOH C O   1 
HETATM 10000 O  O   . HOH DA 6 .   ? 33.453  27.616  43.863  1.00 27.21 ? 725 HOH C O   1 
HETATM 10001 O  O   . HOH DA 6 .   ? 18.823  37.378  29.994  1.00 45.16 ? 726 HOH C O   1 
HETATM 10002 O  O   . HOH DA 6 .   ? 16.526  36.168  31.141  1.00 28.14 ? 727 HOH C O   1 
HETATM 10003 O  O   . HOH DA 6 .   ? 7.249   30.255  18.277  1.00 32.08 ? 728 HOH C O   1 
HETATM 10004 O  O   . HOH DA 6 .   ? 7.603   27.255  21.535  1.00 34.52 ? 729 HOH C O   1 
HETATM 10005 O  O   . HOH DA 6 .   ? 48.662  13.774  29.588  1.00 33.92 ? 730 HOH C O   1 
HETATM 10006 O  O   . HOH DA 6 .   ? 46.945  13.784  25.747  1.00 39.17 ? 731 HOH C O   1 
HETATM 10007 O  O   . HOH DA 6 .   ? 44.730  21.992  19.284  1.00 28.45 ? 732 HOH C O   1 
HETATM 10008 O  O   . HOH DA 6 .   ? 44.613  9.390   27.359  1.00 34.18 ? 733 HOH C O   1 
HETATM 10009 O  O   . HOH DA 6 .   ? 35.267  7.379   27.056  1.00 31.24 ? 734 HOH C O   1 
HETATM 10010 O  O   . HOH DA 6 .   ? 6.791   34.538  31.736  1.00 36.54 ? 735 HOH C O   1 
HETATM 10011 O  O   . HOH DA 6 .   ? 8.095   25.826  43.877  1.00 45.79 ? 736 HOH C O   1 
HETATM 10012 O  O   . HOH DA 6 .   ? 9.201   20.633  41.126  1.00 37.10 ? 737 HOH C O   1 
HETATM 10013 O  O   . HOH DA 6 .   ? 37.130  28.554  13.282  1.00 35.66 ? 738 HOH C O   1 
HETATM 10014 O  O   . HOH DA 6 .   ? 47.673  27.851  40.820  1.00 46.54 ? 739 HOH C O   1 
HETATM 10015 O  O   . HOH DA 6 .   ? 37.305  38.805  36.672  1.00 43.02 ? 740 HOH C O   1 
HETATM 10016 O  O   . HOH DA 6 .   ? 17.028  25.863  44.684  1.00 37.03 ? 741 HOH C O   1 
HETATM 10017 O  O   . HOH DA 6 .   ? 44.392  22.282  47.891  1.00 35.25 ? 742 HOH C O   1 
HETATM 10018 O  O   . HOH DA 6 .   ? 13.461  9.843   13.298  1.00 42.88 ? 743 HOH C O   1 
HETATM 10019 O  O   . HOH DA 6 .   ? 29.898  14.912  12.124  1.00 31.25 ? 744 HOH C O   1 
HETATM 10020 O  O   . HOH DA 6 .   ? 39.941  27.735  48.761  1.00 29.52 ? 745 HOH C O   1 
HETATM 10021 O  O   . HOH DA 6 .   ? 38.954  23.999  51.577  1.00 28.09 ? 746 HOH C O   1 
HETATM 10022 O  O   . HOH DA 6 .   ? 38.956  25.980  11.135  1.00 49.25 ? 747 HOH C O   1 
HETATM 10023 O  O   . HOH DA 6 .   ? 42.934  35.972  43.240  1.00 39.03 ? 748 HOH C O   1 
HETATM 10024 O  O   . HOH DA 6 .   ? 28.772  42.200  27.657  1.00 28.38 ? 749 HOH C O   1 
HETATM 10025 O  O   . HOH DA 6 .   ? 17.800  18.613  10.758  1.00 34.10 ? 750 HOH C O   1 
HETATM 10026 O  O   . HOH EA 6 .   ? 12.711  -19.887 47.869  1.00 22.65 ? 401 HOH D O   1 
HETATM 10027 O  O   . HOH EA 6 .   ? 34.855  -9.455  28.747  1.00 31.13 ? 402 HOH D O   1 
HETATM 10028 O  O   . HOH EA 6 .   ? 26.897  -28.862 41.321  1.00 33.44 ? 403 HOH D O   1 
HETATM 10029 O  O   . HOH EA 6 .   ? 27.892  6.880   43.616  1.00 4.64  ? 404 HOH D O   1 
HETATM 10030 O  O   . HOH EA 6 .   ? 26.956  -0.488  41.394  1.00 4.89  ? 405 HOH D O   1 
HETATM 10031 O  O   . HOH EA 6 .   ? 19.365  -8.553  39.696  1.00 7.50  ? 406 HOH D O   1 
HETATM 10032 O  O   . HOH EA 6 .   ? 20.034  4.475   46.917  1.00 6.87  ? 407 HOH D O   1 
HETATM 10033 O  O   . HOH EA 6 .   ? 26.338  6.631   49.118  1.00 6.71  ? 408 HOH D O   1 
HETATM 10034 O  O   . HOH EA 6 .   ? 13.775  -10.185 47.237  1.00 7.44  ? 409 HOH D O   1 
HETATM 10035 O  O   . HOH EA 6 .   ? 39.452  -9.802  50.515  1.00 5.94  ? 410 HOH D O   1 
HETATM 10036 O  O   . HOH EA 6 .   ? 32.941  8.110   47.335  1.00 7.50  ? 411 HOH D O   1 
HETATM 10037 O  O   . HOH EA 6 .   ? 32.108  8.946   44.853  1.00 9.25  ? 412 HOH D O   1 
HETATM 10038 O  O   . HOH EA 6 .   ? 26.604  6.217   45.994  1.00 6.66  ? 413 HOH D O   1 
HETATM 10039 O  O   . HOH EA 6 .   ? 32.666  9.650   49.671  1.00 7.03  ? 414 HOH D O   1 
HETATM 10040 O  O   . HOH EA 6 .   ? 7.711   -6.646  39.918  1.00 12.28 ? 415 HOH D O   1 
HETATM 10041 O  O   . HOH EA 6 .   ? 40.433  -0.097  53.491  1.00 11.96 ? 416 HOH D O   1 
HETATM 10042 O  O   . HOH EA 6 .   ? 33.565  -13.180 40.622  1.00 8.33  ? 417 HOH D O   1 
HETATM 10043 O  O   . HOH EA 6 .   ? 10.971  -8.789  46.517  1.00 10.49 ? 418 HOH D O   1 
HETATM 10044 O  O   . HOH EA 6 .   ? 14.993  -11.340 36.700  1.00 11.19 ? 419 HOH D O   1 
HETATM 10045 O  O   . HOH EA 6 .   ? 23.463  2.953   37.102  1.00 10.99 ? 420 HOH D O   1 
HETATM 10046 O  O   . HOH EA 6 .   ? 31.986  -15.808 63.097  1.00 8.93  ? 421 HOH D O   1 
HETATM 10047 O  O   . HOH EA 6 .   ? 23.474  7.677   44.195  1.00 5.84  ? 422 HOH D O   1 
HETATM 10048 O  O   . HOH EA 6 .   ? 29.119  -21.873 42.159  1.00 11.42 ? 423 HOH D O   1 
HETATM 10049 O  O   . HOH EA 6 .   ? 25.252  -10.663 34.382  1.00 11.07 ? 424 HOH D O   1 
HETATM 10050 O  O   . HOH EA 6 .   ? 34.508  3.675   39.975  1.00 11.97 ? 425 HOH D O   1 
HETATM 10051 O  O   . HOH EA 6 .   ? 32.175  -29.946 63.594  1.00 12.56 ? 426 HOH D O   1 
HETATM 10052 O  O   . HOH EA 6 .   ? 25.228  -1.698  49.321  1.00 7.28  ? 427 HOH D O   1 
HETATM 10053 O  O   . HOH EA 6 .   ? 36.462  7.949   39.297  1.00 13.16 ? 428 HOH D O   1 
HETATM 10054 O  O   . HOH EA 6 .   ? 8.623   -15.526 56.018  1.00 14.41 ? 429 HOH D O   1 
HETATM 10055 O  O   . HOH EA 6 .   ? 19.650  9.000   47.468  1.00 9.03  ? 430 HOH D O   1 
HETATM 10056 O  O   . HOH EA 6 .   ? 29.739  6.470   59.176  1.00 9.36  ? 431 HOH D O   1 
HETATM 10057 O  O   . HOH EA 6 .   ? 37.891  -25.202 53.197  1.00 10.70 ? 432 HOH D O   1 
HETATM 10058 O  O   . HOH EA 6 .   ? 50.025  -12.140 41.126  1.00 13.43 ? 433 HOH D O   1 
HETATM 10059 O  O   . HOH EA 6 .   ? 39.861  7.636   49.048  1.00 9.96  ? 434 HOH D O   1 
HETATM 10060 O  O   . HOH EA 6 .   ? 35.711  7.564   48.262  1.00 9.37  ? 435 HOH D O   1 
HETATM 10061 O  O   . HOH EA 6 .   ? 26.684  1.897   39.856  1.00 10.83 ? 436 HOH D O   1 
HETATM 10062 O  O   . HOH EA 6 .   ? 45.012  -14.372 55.232  1.00 12.67 ? 437 HOH D O   1 
HETATM 10063 O  O   . HOH EA 6 .   ? 11.732  -21.387 51.443  1.00 14.23 ? 438 HOH D O   1 
HETATM 10064 O  O   . HOH EA 6 .   ? 31.937  -26.531 60.425  1.00 11.29 ? 439 HOH D O   1 
HETATM 10065 O  O   . HOH EA 6 .   ? 36.367  -9.885  35.272  1.00 14.63 ? 440 HOH D O   1 
HETATM 10066 O  O   . HOH EA 6 .   ? 41.795  -5.212  56.136  1.00 10.01 ? 441 HOH D O   1 
HETATM 10067 O  O   . HOH EA 6 .   ? 25.675  -22.942 37.398  1.00 13.87 ? 442 HOH D O   1 
HETATM 10068 O  O   . HOH EA 6 .   ? 41.955  -23.524 49.293  1.00 15.34 ? 443 HOH D O   1 
HETATM 10069 O  O   . HOH EA 6 .   ? 42.263  2.185   47.527  1.00 13.41 ? 444 HOH D O   1 
HETATM 10070 O  O   . HOH EA 6 .   ? 16.231  -2.756  48.957  1.00 9.39  ? 445 HOH D O   1 
HETATM 10071 O  O   . HOH EA 6 .   ? 14.218  0.555   44.184  1.00 16.21 ? 446 HOH D O   1 
HETATM 10072 O  O   . HOH EA 6 .   ? 34.309  -25.100 59.570  1.00 13.57 ? 447 HOH D O   1 
HETATM 10073 O  O   . HOH EA 6 .   ? 22.159  -29.689 61.204  1.00 12.61 ? 448 HOH D O   1 
HETATM 10074 O  O   . HOH EA 6 .   ? 36.456  -26.728 60.027  1.00 15.42 ? 449 HOH D O   1 
HETATM 10075 O  O   . HOH EA 6 .   ? 30.997  -9.706  66.136  1.00 16.60 ? 450 HOH D O   1 
HETATM 10076 O  O   . HOH EA 6 .   ? 20.662  -10.681 34.225  1.00 14.28 ? 451 HOH D O   1 
HETATM 10077 O  O   . HOH EA 6 .   ? 40.273  -26.565 54.977  1.00 12.67 ? 452 HOH D O   1 
HETATM 10078 O  O   . HOH EA 6 .   ? 13.886  6.128   51.526  1.00 17.03 ? 453 HOH D O   1 
HETATM 10079 O  O   . HOH EA 6 .   ? 28.488  -21.543 37.835  1.00 16.25 ? 454 HOH D O   1 
HETATM 10080 O  O   . HOH EA 6 .   ? 24.851  -19.335 63.132  1.00 15.48 ? 455 HOH D O   1 
HETATM 10081 O  O   . HOH EA 6 .   ? 22.997  -12.077 33.714  1.00 11.98 ? 456 HOH D O   1 
HETATM 10082 O  O   . HOH EA 6 .   ? 12.634  -1.450  40.519  1.00 14.11 ? 457 HOH D O   1 
HETATM 10083 O  O   . HOH EA 6 .   ? 27.344  -11.367 32.657  1.00 15.67 ? 458 HOH D O   1 
HETATM 10084 O  O   . HOH EA 6 .   ? 28.150  -29.032 50.549  1.00 13.18 ? 459 HOH D O   1 
HETATM 10085 O  O   . HOH EA 6 .   ? 12.855  -20.363 61.819  1.00 11.99 ? 460 HOH D O   1 
HETATM 10086 O  O   . HOH EA 6 .   ? 32.551  -12.028 65.328  1.00 12.54 ? 461 HOH D O   1 
HETATM 10087 O  O   . HOH EA 6 .   ? 17.535  -3.551  51.216  1.00 9.96  ? 462 HOH D O   1 
HETATM 10088 O  O   . HOH EA 6 .   ? 17.096  -25.372 65.231  1.00 12.56 ? 463 HOH D O   1 
HETATM 10089 O  O   . HOH EA 6 .   ? 18.731  -19.780 32.964  1.00 16.94 ? 464 HOH D O   1 
HETATM 10090 O  O   . HOH EA 6 .   ? 14.625  -0.498  46.806  1.00 14.42 ? 465 HOH D O   1 
HETATM 10091 O  O   . HOH EA 6 .   ? 36.935  -26.997 55.216  1.00 12.95 ? 466 HOH D O   1 
HETATM 10092 O  O   . HOH EA 6 .   ? 7.369   -12.735 47.563  1.00 14.23 ? 467 HOH D O   1 
HETATM 10093 O  O   . HOH EA 6 .   ? 42.794  -16.536 45.445  1.00 12.45 ? 468 HOH D O   1 
HETATM 10094 O  O   . HOH EA 6 .   ? 42.908  -19.411 45.209  1.00 11.97 ? 469 HOH D O   1 
HETATM 10095 O  O   . HOH EA 6 .   ? 11.252  -17.553 60.230  1.00 14.66 ? 470 HOH D O   1 
HETATM 10096 O  O   . HOH EA 6 .   ? 36.708  5.181   46.436  1.00 15.11 ? 471 HOH D O   1 
HETATM 10097 O  O   . HOH EA 6 .   ? 9.387   -22.781 51.375  1.00 16.01 ? 472 HOH D O   1 
HETATM 10098 O  O   . HOH EA 6 .   ? 25.200  -26.194 65.343  1.00 16.47 ? 473 HOH D O   1 
HETATM 10099 O  O   . HOH EA 6 .   ? 8.978   -9.307  60.725  1.00 17.56 ? 474 HOH D O   1 
HETATM 10100 O  O   . HOH EA 6 .   ? 30.833  -13.370 63.635  1.00 12.15 ? 475 HOH D O   1 
HETATM 10101 O  O   . HOH EA 6 .   ? 8.177   -17.549 57.959  1.00 18.61 ? 476 HOH D O   1 
HETATM 10102 O  O   . HOH EA 6 .   ? 15.270  -0.879  54.588  1.00 15.28 ? 477 HOH D O   1 
HETATM 10103 O  O   . HOH EA 6 .   ? 38.249  -15.938 39.365  1.00 8.75  ? 478 HOH D O   1 
HETATM 10104 O  O   . HOH EA 6 .   ? 33.472  -28.389 61.718  1.00 14.50 ? 479 HOH D O   1 
HETATM 10105 O  O   . HOH EA 6 .   ? 38.503  -14.839 66.513  1.00 14.66 ? 480 HOH D O   1 
HETATM 10106 O  O   . HOH EA 6 .   ? 19.201  6.720   45.662  1.00 10.42 ? 481 HOH D O   1 
HETATM 10107 O  O   . HOH EA 6 .   ? 6.117   -5.281  55.555  1.00 13.55 ? 482 HOH D O   1 
HETATM 10108 O  O   . HOH EA 6 .   ? 32.599  -6.390  31.304  1.00 15.67 ? 483 HOH D O   1 
HETATM 10109 O  O   . HOH EA 6 .   ? 36.456  10.133  48.794  1.00 15.99 ? 484 HOH D O   1 
HETATM 10110 O  O   . HOH EA 6 .   ? 33.400  -19.583 37.147  1.00 14.54 ? 485 HOH D O   1 
HETATM 10111 O  O   . HOH EA 6 .   ? 40.533  -13.367 67.136  1.00 18.96 ? 486 HOH D O   1 
HETATM 10112 O  O   . HOH EA 6 .   ? 16.133  13.221  51.475  1.00 18.07 ? 487 HOH D O   1 
HETATM 10113 O  O   . HOH EA 6 .   ? 45.059  -24.614 53.658  1.00 14.48 ? 488 HOH D O   1 
HETATM 10114 O  O   . HOH EA 6 .   ? 7.852   -20.102 57.098  1.00 12.87 ? 489 HOH D O   1 
HETATM 10115 O  O   . HOH EA 6 .   ? 28.292  -8.653  32.696  1.00 20.90 ? 490 HOH D O   1 
HETATM 10116 O  O   . HOH EA 6 .   ? 15.829  -0.361  50.470  1.00 15.62 ? 491 HOH D O   1 
HETATM 10117 O  O   . HOH EA 6 .   ? 22.424  -4.686  51.683  1.00 12.84 ? 492 HOH D O   1 
HETATM 10118 O  O   . HOH EA 6 .   ? 43.901  -0.088  46.817  1.00 13.50 ? 493 HOH D O   1 
HETATM 10119 O  O   . HOH EA 6 .   ? 34.309  1.886   32.544  1.00 16.90 ? 494 HOH D O   1 
HETATM 10120 O  O   . HOH EA 6 .   ? 36.154  -26.323 51.338  1.00 16.39 ? 495 HOH D O   1 
HETATM 10121 O  O   . HOH EA 6 .   ? 38.293  -25.017 60.923  1.00 15.62 ? 496 HOH D O   1 
HETATM 10122 O  O   . HOH EA 6 .   ? 48.229  -15.499 55.332  1.00 16.71 ? 497 HOH D O   1 
HETATM 10123 O  O   . HOH EA 6 .   ? 45.682  -7.801  56.124  1.00 16.44 ? 498 HOH D O   1 
HETATM 10124 O  O   . HOH EA 6 .   ? 34.719  4.026   35.486  1.00 16.38 ? 499 HOH D O   1 
HETATM 10125 O  O   . HOH EA 6 .   ? 10.409  -8.235  42.922  1.00 12.48 ? 500 HOH D O   1 
HETATM 10126 O  O   . HOH EA 6 .   ? 21.939  1.684   39.013  1.00 17.04 ? 501 HOH D O   1 
HETATM 10127 O  O   . HOH EA 6 .   ? 8.379   -6.396  37.210  1.00 15.19 ? 502 HOH D O   1 
HETATM 10128 O  O   . HOH EA 6 .   ? 12.470  -11.142 35.061  1.00 18.09 ? 503 HOH D O   1 
HETATM 10129 O  O   . HOH EA 6 .   ? 26.345  -25.003 39.236  1.00 17.62 ? 504 HOH D O   1 
HETATM 10130 O  O   . HOH EA 6 .   ? 17.311  -1.274  52.822  1.00 15.83 ? 505 HOH D O   1 
HETATM 10131 O  O   . HOH EA 6 .   ? 19.159  -2.866  38.524  1.00 15.37 ? 506 HOH D O   1 
HETATM 10132 O  O   . HOH EA 6 .   ? 30.090  1.381   36.325  1.00 14.93 ? 507 HOH D O   1 
HETATM 10133 O  O   . HOH EA 6 .   ? 5.185   -13.206 57.819  1.00 18.42 ? 508 HOH D O   1 
HETATM 10134 O  O   . HOH EA 6 .   ? 31.777  -24.824 62.502  1.00 14.40 ? 509 HOH D O   1 
HETATM 10135 O  O   . HOH EA 6 .   ? 47.683  -19.202 58.317  1.00 19.66 ? 510 HOH D O   1 
HETATM 10136 O  O   . HOH EA 6 .   ? 9.560   -5.865  41.955  1.00 13.15 ? 511 HOH D O   1 
HETATM 10137 O  O   . HOH EA 6 .   ? 25.746  -28.674 66.390  1.00 16.49 ? 512 HOH D O   1 
HETATM 10138 O  O   . HOH EA 6 .   ? 28.494  -15.154 62.739  1.00 19.27 ? 513 HOH D O   1 
HETATM 10139 O  O   . HOH EA 6 .   ? 41.958  -0.295  57.357  1.00 18.10 ? 514 HOH D O   1 
HETATM 10140 O  O   . HOH EA 6 .   ? 42.754  -20.955 41.031  1.00 15.19 ? 515 HOH D O   1 
HETATM 10141 O  O   . HOH EA 6 .   ? 4.881   -17.170 51.666  1.00 17.67 ? 516 HOH D O   1 
HETATM 10142 O  O   . HOH EA 6 .   ? 38.162  2.599   47.348  1.00 14.71 ? 517 HOH D O   1 
HETATM 10143 O  O   . HOH EA 6 .   ? 12.299  2.954   50.215  1.00 14.75 ? 518 HOH D O   1 
HETATM 10144 O  O   . HOH EA 6 .   ? 3.748   -7.475  52.275  1.00 17.25 ? 519 HOH D O   1 
HETATM 10145 O  O   . HOH EA 6 .   ? 13.180  0.344   50.386  1.00 15.42 ? 520 HOH D O   1 
HETATM 10146 O  O   . HOH EA 6 .   ? 14.999  -21.997 62.603  1.00 18.20 ? 521 HOH D O   1 
HETATM 10147 O  O   . HOH EA 6 .   ? 37.101  12.874  42.357  1.00 17.08 ? 522 HOH D O   1 
HETATM 10148 O  O   . HOH EA 6 .   ? 12.312  -1.082  48.117  1.00 14.13 ? 523 HOH D O   1 
HETATM 10149 O  O   . HOH EA 6 .   ? 6.281   -4.379  37.026  1.00 17.71 ? 524 HOH D O   1 
HETATM 10150 O  O   . HOH EA 6 .   ? 44.149  -21.129 43.536  1.00 19.88 ? 525 HOH D O   1 
HETATM 10151 O  O   . HOH EA 6 .   ? 26.006  -11.570 61.564  1.00 21.25 ? 526 HOH D O   1 
HETATM 10152 O  O   . HOH EA 6 .   ? 12.084  -15.836 63.003  1.00 18.47 ? 527 HOH D O   1 
HETATM 10153 O  O   . HOH EA 6 .   ? 38.195  -1.373  31.076  1.00 21.85 ? 528 HOH D O   1 
HETATM 10154 O  O   . HOH EA 6 .   ? 26.344  -0.654  34.116  1.00 15.71 ? 529 HOH D O   1 
HETATM 10155 O  O   . HOH EA 6 .   ? 20.444  -25.853 52.486  1.00 19.49 ? 530 HOH D O   1 
HETATM 10156 O  O   . HOH EA 6 .   ? 8.815   -15.270 41.899  1.00 19.59 ? 531 HOH D O   1 
HETATM 10157 O  O   . HOH EA 6 .   ? 8.328   -14.972 35.142  1.00 17.18 ? 532 HOH D O   1 
HETATM 10158 O  O   . HOH EA 6 .   ? 22.511  -26.908 53.701  1.00 17.35 ? 533 HOH D O   1 
HETATM 10159 O  O   . HOH EA 6 .   ? 9.443   -2.218  59.041  1.00 19.10 ? 534 HOH D O   1 
HETATM 10160 O  O   . HOH EA 6 .   ? 10.712  -3.843  40.408  1.00 17.46 ? 535 HOH D O   1 
HETATM 10161 O  O   . HOH EA 6 .   ? 15.487  -13.906 35.844  1.00 13.72 ? 536 HOH D O   1 
HETATM 10162 O  O   . HOH EA 6 .   ? 25.149  -1.848  29.858  1.00 18.39 ? 537 HOH D O   1 
HETATM 10163 O  O   . HOH EA 6 .   ? 10.742  -4.792  37.820  1.00 16.30 ? 538 HOH D O   1 
HETATM 10164 O  O   . HOH EA 6 .   ? 25.325  -4.033  32.970  1.00 19.54 ? 539 HOH D O   1 
HETATM 10165 O  O   . HOH EA 6 .   ? 24.914  -1.541  59.268  1.00 17.85 ? 540 HOH D O   1 
HETATM 10166 O  O   . HOH EA 6 .   ? 34.047  -13.958 66.521  1.00 21.69 ? 541 HOH D O   1 
HETATM 10167 O  O   . HOH EA 6 .   ? 37.465  10.045  38.090  1.00 24.96 ? 542 HOH D O   1 
HETATM 10168 O  O   . HOH EA 6 .   ? 9.743   -10.717 35.779  1.00 16.29 ? 543 HOH D O   1 
HETATM 10169 O  O   . HOH EA 6 .   ? 29.691  -30.006 54.395  1.00 18.69 ? 544 HOH D O   1 
HETATM 10170 O  O   . HOH EA 6 .   ? 29.666  -9.115  61.498  1.00 20.96 ? 545 HOH D O   1 
HETATM 10171 O  O   . HOH EA 6 .   ? 16.379  6.675   45.088  1.00 14.01 ? 546 HOH D O   1 
HETATM 10172 O  O   . HOH EA 6 .   ? 35.770  -27.580 47.749  1.00 24.19 ? 547 HOH D O   1 
HETATM 10173 O  O   . HOH EA 6 .   ? 20.738  -27.843 46.181  1.00 19.75 ? 548 HOH D O   1 
HETATM 10174 O  O   . HOH EA 6 .   ? 31.604  -18.221 65.319  1.00 22.46 ? 549 HOH D O   1 
HETATM 10175 O  O   . HOH EA 6 .   ? 43.625  -15.476 63.431  1.00 13.33 ? 550 HOH D O   1 
HETATM 10176 O  O   . HOH EA 6 .   ? 10.789  -16.052 45.490  1.00 13.08 ? 551 HOH D O   1 
HETATM 10177 O  O   . HOH EA 6 .   ? 25.467  -32.016 65.761  1.00 15.82 ? 552 HOH D O   1 
HETATM 10178 O  O   . HOH EA 6 .   ? 46.998  -15.364 42.886  1.00 21.39 ? 553 HOH D O   1 
HETATM 10179 O  O   . HOH EA 6 .   ? 49.179  -19.721 60.599  1.00 29.73 ? 554 HOH D O   1 
HETATM 10180 O  O   . HOH EA 6 .   ? 36.548  -30.759 54.238  1.00 23.27 ? 555 HOH D O   1 
HETATM 10181 O  O   . HOH EA 6 .   ? 8.773   -8.075  35.128  1.00 16.66 ? 556 HOH D O   1 
HETATM 10182 O  O   . HOH EA 6 .   ? 31.260  -0.411  62.869  1.00 18.85 ? 557 HOH D O   1 
HETATM 10183 O  O   . HOH EA 6 .   ? 39.298  -17.042 64.830  1.00 19.08 ? 558 HOH D O   1 
HETATM 10184 O  O   . HOH EA 6 .   ? 45.032  -23.333 62.496  1.00 23.58 ? 559 HOH D O   1 
HETATM 10185 O  O   . HOH EA 6 .   ? 22.617  -37.433 64.690  1.00 18.59 ? 560 HOH D O   1 
HETATM 10186 O  O   . HOH EA 6 .   ? 30.317  -18.645 35.022  1.00 19.35 ? 561 HOH D O   1 
HETATM 10187 O  O   . HOH EA 6 .   ? 22.425  -32.003 57.178  1.00 25.14 ? 562 HOH D O   1 
HETATM 10188 O  O   . HOH EA 6 .   ? 22.491  -27.275 36.424  1.00 19.73 ? 563 HOH D O   1 
HETATM 10189 O  O   . HOH EA 6 .   ? 24.336  -8.122  34.129  1.00 17.13 ? 564 HOH D O   1 
HETATM 10190 O  O   . HOH EA 6 .   ? 23.025  -39.703 62.734  1.00 15.33 ? 565 HOH D O   1 
HETATM 10191 O  O   . HOH EA 6 .   ? 23.968  -27.615 34.064  1.00 17.74 ? 566 HOH D O   1 
HETATM 10192 O  O   . HOH EA 6 .   ? 16.104  -0.204  36.908  1.00 27.53 ? 567 HOH D O   1 
HETATM 10193 O  O   . HOH EA 6 .   ? 29.882  -23.681 64.286  1.00 23.47 ? 568 HOH D O   1 
HETATM 10194 O  O   . HOH EA 6 .   ? 6.089   2.430   58.027  1.00 24.73 ? 569 HOH D O   1 
HETATM 10195 O  O   . HOH EA 6 .   ? 38.031  3.166   30.349  1.00 25.33 ? 570 HOH D O   1 
HETATM 10196 O  O   . HOH EA 6 .   ? 5.811   -14.724 55.423  1.00 19.28 ? 571 HOH D O   1 
HETATM 10197 O  O   . HOH EA 6 .   ? 45.383  -20.570 58.938  1.00 17.67 ? 572 HOH D O   1 
HETATM 10198 O  O   . HOH EA 6 .   ? 20.733  6.964   57.050  1.00 20.94 ? 573 HOH D O   1 
HETATM 10199 O  O   . HOH EA 6 .   ? 38.086  -11.149 32.722  1.00 24.40 ? 574 HOH D O   1 
HETATM 10200 O  O   . HOH EA 6 .   ? 37.512  -28.045 57.246  1.00 22.77 ? 575 HOH D O   1 
HETATM 10201 O  O   . HOH EA 6 .   ? 19.009  -26.635 62.207  1.00 16.94 ? 576 HOH D O   1 
HETATM 10202 O  O   . HOH EA 6 .   ? 26.400  -34.597 65.515  1.00 21.16 ? 577 HOH D O   1 
HETATM 10203 O  O   . HOH EA 6 .   ? 25.025  -21.338 64.544  1.00 26.34 ? 578 HOH D O   1 
HETATM 10204 O  O   . HOH EA 6 .   ? 22.222  -14.593 60.090  1.00 15.99 ? 579 HOH D O   1 
HETATM 10205 O  O   . HOH EA 6 .   ? 39.484  -20.103 64.888  1.00 24.81 ? 580 HOH D O   1 
HETATM 10206 O  O   . HOH EA 6 .   ? 37.029  -20.327 66.039  1.00 30.64 ? 581 HOH D O   1 
HETATM 10207 O  O   . HOH EA 6 .   ? 8.145   -15.096 45.866  1.00 20.73 ? 582 HOH D O   1 
HETATM 10208 O  O   . HOH EA 6 .   ? 51.938  -3.622  41.004  1.00 20.20 ? 583 HOH D O   1 
HETATM 10209 O  O   . HOH EA 6 .   ? 28.916  -17.501 64.271  1.00 21.55 ? 584 HOH D O   1 
HETATM 10210 O  O   . HOH EA 6 .   ? 12.967  11.790  48.251  1.00 24.96 ? 585 HOH D O   1 
HETATM 10211 O  O   . HOH EA 6 .   ? 16.376  -25.692 61.247  1.00 24.80 ? 586 HOH D O   1 
HETATM 10212 O  O   . HOH EA 6 .   ? 40.236  7.073   37.919  1.00 24.99 ? 587 HOH D O   1 
HETATM 10213 O  O   . HOH EA 6 .   ? 48.698  -15.176 60.682  1.00 26.13 ? 588 HOH D O   1 
HETATM 10214 O  O   . HOH EA 6 .   ? 31.779  -29.797 48.389  1.00 20.32 ? 589 HOH D O   1 
HETATM 10215 O  O   . HOH EA 6 .   ? 8.130   1.499   54.826  1.00 25.08 ? 590 HOH D O   1 
HETATM 10216 O  O   . HOH EA 6 .   ? 33.369  -22.866 65.532  1.00 30.29 ? 591 HOH D O   1 
HETATM 10217 O  O   . HOH EA 6 .   ? 43.943  -0.712  65.568  1.00 26.22 ? 592 HOH D O   1 
HETATM 10218 O  O   . HOH EA 6 .   ? 27.774  -19.301 62.865  1.00 23.71 ? 593 HOH D O   1 
HETATM 10219 O  O   . HOH EA 6 .   ? 13.479  -5.309  30.621  1.00 28.89 ? 594 HOH D O   1 
HETATM 10220 O  O   . HOH EA 6 .   ? 18.851  -23.897 68.213  1.00 26.02 ? 595 HOH D O   1 
HETATM 10221 O  O   . HOH EA 6 .   ? 15.430  -24.356 58.369  1.00 31.78 ? 596 HOH D O   1 
HETATM 10222 O  O   . HOH EA 6 .   ? 41.753  13.914  42.178  1.00 22.35 ? 597 HOH D O   1 
HETATM 10223 O  O   . HOH EA 6 .   ? 45.776  -5.985  34.908  1.00 38.03 ? 598 HOH D O   1 
HETATM 10224 O  O   . HOH EA 6 .   ? 42.280  12.662  39.329  1.00 21.68 ? 599 HOH D O   1 
HETATM 10225 O  O   . HOH EA 6 .   ? 19.562  4.181   60.230  1.00 27.12 ? 600 HOH D O   1 
HETATM 10226 O  O   . HOH EA 6 .   ? 42.489  -25.446 52.846  1.00 21.22 ? 601 HOH D O   1 
HETATM 10227 O  O   . HOH EA 6 .   ? 15.954  -14.988 30.992  1.00 27.34 ? 602 HOH D O   1 
HETATM 10228 O  O   . HOH EA 6 .   ? 40.016  -25.768 50.236  1.00 27.06 ? 603 HOH D O   1 
HETATM 10229 O  O   . HOH EA 6 .   ? 40.199  -16.928 33.927  1.00 24.55 ? 604 HOH D O   1 
HETATM 10230 O  O   . HOH EA 6 .   ? 30.622  -17.355 32.582  1.00 32.10 ? 605 HOH D O   1 
HETATM 10231 O  O   . HOH EA 6 .   ? 11.924  -20.949 41.142  1.00 23.29 ? 606 HOH D O   1 
HETATM 10232 O  O   . HOH EA 6 .   ? 13.903  13.844  49.780  1.00 26.44 ? 607 HOH D O   1 
HETATM 10233 O  O   . HOH EA 6 .   ? 37.294  7.559   46.012  1.00 26.46 ? 608 HOH D O   1 
HETATM 10234 O  O   . HOH EA 6 .   ? 22.891  -32.929 63.343  1.00 18.25 ? 609 HOH D O   1 
HETATM 10235 O  O   . HOH EA 6 .   ? 13.104  -14.023 34.340  1.00 19.24 ? 610 HOH D O   1 
HETATM 10236 O  O   . HOH EA 6 .   ? 39.261  -23.394 38.957  1.00 25.10 ? 611 HOH D O   1 
HETATM 10237 O  O   . HOH EA 6 .   ? 30.898  -13.156 31.828  1.00 24.24 ? 612 HOH D O   1 
HETATM 10238 O  O   . HOH EA 6 .   ? 54.368  -14.035 39.875  1.00 27.23 ? 613 HOH D O   1 
HETATM 10239 O  O   . HOH EA 6 .   ? 42.220  -16.775 65.326  1.00 23.10 ? 614 HOH D O   1 
HETATM 10240 O  O   . HOH EA 6 .   ? 43.794  -17.701 32.924  1.00 28.12 ? 615 HOH D O   1 
HETATM 10241 O  O   . HOH EA 6 .   ? 16.207  -23.238 37.314  1.00 21.84 ? 616 HOH D O   1 
HETATM 10242 O  O   . HOH EA 6 .   ? 37.265  5.281   38.652  1.00 21.71 ? 617 HOH D O   1 
HETATM 10243 O  O   . HOH EA 6 .   ? 19.953  -24.965 33.976  1.00 18.02 ? 618 HOH D O   1 
HETATM 10244 O  O   . HOH EA 6 .   ? 6.174   -5.397  34.041  1.00 34.00 ? 619 HOH D O   1 
HETATM 10245 O  O   . HOH EA 6 .   ? 44.004  -10.378 28.402  1.00 36.02 ? 620 HOH D O   1 
HETATM 10246 O  O   . HOH EA 6 .   ? 24.701  -29.913 51.090  1.00 22.34 ? 621 HOH D O   1 
HETATM 10247 O  O   . HOH EA 6 .   ? 22.347  -0.309  60.149  1.00 27.60 ? 622 HOH D O   1 
HETATM 10248 O  O   . HOH EA 6 .   ? 24.068  -29.397 53.651  1.00 23.56 ? 623 HOH D O   1 
HETATM 10249 O  O   . HOH EA 6 .   ? 29.351  -32.438 56.596  1.00 20.72 ? 624 HOH D O   1 
HETATM 10250 O  O   . HOH EA 6 .   ? 28.161  -15.605 29.739  1.00 36.83 ? 625 HOH D O   1 
HETATM 10251 O  O   . HOH EA 6 .   ? 10.232  -18.607 37.618  1.00 26.25 ? 626 HOH D O   1 
HETATM 10252 O  O   . HOH EA 6 .   ? 33.789  -23.730 43.604  1.00 24.69 ? 627 HOH D O   1 
HETATM 10253 O  O   . HOH EA 6 .   ? 24.469  -17.132 64.638  1.00 19.41 ? 628 HOH D O   1 
HETATM 10254 O  O   . HOH EA 6 .   ? 44.823  -19.281 37.018  1.00 24.85 ? 629 HOH D O   1 
HETATM 10255 O  O   . HOH EA 6 .   ? 12.281  -24.514 49.039  1.00 24.37 ? 630 HOH D O   1 
HETATM 10256 O  O   . HOH EA 6 .   ? 46.397  -15.096 32.835  1.00 29.02 ? 631 HOH D O   1 
HETATM 10257 O  O   . HOH EA 6 .   ? 6.114   -17.674 49.530  1.00 26.20 ? 632 HOH D O   1 
HETATM 10258 O  O   . HOH EA 6 .   ? 16.958  -26.891 44.939  1.00 32.93 ? 633 HOH D O   1 
HETATM 10259 O  O   . HOH EA 6 .   ? 22.709  -31.521 54.727  1.00 24.44 ? 634 HOH D O   1 
HETATM 10260 O  O   . HOH EA 6 .   ? 12.051  -7.496  31.314  1.00 20.87 ? 635 HOH D O   1 
HETATM 10261 O  O   . HOH EA 6 .   ? 23.308  1.443   61.989  1.00 26.94 ? 636 HOH D O   1 
HETATM 10262 O  O   . HOH EA 6 .   ? 47.953  -12.043 25.638  1.00 27.01 ? 637 HOH D O   1 
HETATM 10263 O  O   . HOH EA 6 .   ? 11.075  -15.693 34.357  1.00 24.20 ? 638 HOH D O   1 
HETATM 10264 O  O   . HOH EA 6 .   ? 44.276  -21.150 38.945  1.00 28.82 ? 639 HOH D O   1 
HETATM 10265 O  O   . HOH EA 6 .   ? 26.789  -16.789 65.966  1.00 30.15 ? 640 HOH D O   1 
HETATM 10266 O  O   . HOH EA 6 .   ? 37.656  -14.098 69.895  1.00 33.83 ? 641 HOH D O   1 
HETATM 10267 O  O   . HOH EA 6 .   ? 30.483  -8.296  31.455  1.00 24.91 ? 642 HOH D O   1 
HETATM 10268 O  O   . HOH EA 6 .   ? 22.576  -18.244 66.470  1.00 31.78 ? 643 HOH D O   1 
HETATM 10269 O  O   . HOH EA 6 .   ? 19.151  -28.162 44.106  1.00 30.53 ? 644 HOH D O   1 
HETATM 10270 O  O   . HOH EA 6 .   ? 18.886  0.854   60.634  1.00 42.22 ? 645 HOH D O   1 
HETATM 10271 O  O   . HOH EA 6 .   ? 39.976  -28.703 53.396  1.00 28.44 ? 646 HOH D O   1 
HETATM 10272 O  O   . HOH EA 6 .   ? 27.890  -30.906 52.769  1.00 26.28 ? 647 HOH D O   1 
HETATM 10273 O  O   . HOH EA 6 .   ? 25.144  -36.155 63.874  1.00 25.09 ? 648 HOH D O   1 
HETATM 10274 O  O   . HOH EA 6 .   ? 29.479  -8.476  64.027  1.00 23.80 ? 649 HOH D O   1 
HETATM 10275 O  O   . HOH EA 6 .   ? 47.218  -16.458 57.734  1.00 25.64 ? 650 HOH D O   1 
HETATM 10276 O  O   . HOH EA 6 .   ? 9.875   -2.030  36.792  1.00 27.87 ? 651 HOH D O   1 
HETATM 10277 O  O   . HOH EA 6 .   ? 31.983  -21.723 38.099  1.00 29.78 ? 652 HOH D O   1 
HETATM 10278 O  O   . HOH EA 6 .   ? 29.512  -21.019 35.424  1.00 32.42 ? 653 HOH D O   1 
HETATM 10279 O  O   . HOH EA 6 .   ? 13.629  -18.505 65.743  1.00 24.34 ? 654 HOH D O   1 
HETATM 10280 O  O   . HOH EA 6 .   ? 11.744  -18.618 63.687  1.00 18.08 ? 655 HOH D O   1 
HETATM 10281 O  O   . HOH EA 6 .   ? 9.001   -18.148 63.963  1.00 25.33 ? 656 HOH D O   1 
HETATM 10282 O  O   . HOH EA 6 .   ? 19.810  -31.659 57.207  1.00 29.88 ? 657 HOH D O   1 
HETATM 10283 O  O   . HOH EA 6 .   ? 14.953  -27.145 58.115  1.00 28.01 ? 658 HOH D O   1 
HETATM 10284 O  O   . HOH EA 6 .   ? 11.819  -17.881 35.652  1.00 24.03 ? 659 HOH D O   1 
HETATM 10285 O  O   . HOH EA 6 .   ? 8.125   -2.241  47.415  1.00 20.20 ? 660 HOH D O   1 
HETATM 10286 O  O   . HOH EA 6 .   ? 47.865  6.667   40.801  1.00 42.90 ? 661 HOH D O   1 
HETATM 10287 O  O   . HOH EA 6 .   ? 26.156  -2.420  61.614  1.00 19.53 ? 662 HOH D O   1 
HETATM 10288 O  O   . HOH EA 6 .   ? 23.896  -3.933  58.372  1.00 25.60 ? 663 HOH D O   1 
HETATM 10289 O  O   . HOH EA 6 .   ? 23.983  -3.640  55.962  1.00 21.28 ? 664 HOH D O   1 
HETATM 10290 O  O   . HOH EA 6 .   ? 27.224  -8.857  60.046  1.00 22.29 ? 665 HOH D O   1 
HETATM 10291 O  O   . HOH EA 6 .   ? 10.135  11.986  48.616  1.00 26.68 ? 666 HOH D O   1 
HETATM 10292 O  O   . HOH EA 6 .   ? 13.843  11.409  55.014  1.00 31.61 ? 667 HOH D O   1 
HETATM 10293 O  O   . HOH EA 6 .   ? 39.105  -6.416  33.623  1.00 23.82 ? 668 HOH D O   1 
HETATM 10294 O  O   . HOH EA 6 .   ? 34.432  -9.720  33.369  1.00 26.14 ? 669 HOH D O   1 
HETATM 10295 O  O   . HOH EA 6 .   ? 34.648  -8.262  31.155  1.00 27.01 ? 670 HOH D O   1 
HETATM 10296 O  O   . HOH EA 6 .   ? 34.637  -19.635 34.707  1.00 40.82 ? 671 HOH D O   1 
HETATM 10297 O  O   . HOH EA 6 .   ? 28.219  -0.686  62.983  1.00 22.47 ? 672 HOH D O   1 
HETATM 10298 O  O   . HOH EA 6 .   ? 7.996   -17.178 36.778  1.00 31.15 ? 673 HOH D O   1 
HETATM 10299 O  O   . HOH EA 6 .   ? 43.535  15.695  42.685  1.00 26.43 ? 674 HOH D O   1 
HETATM 10300 O  O   . HOH EA 6 .   ? 11.774  -1.126  59.522  1.00 23.32 ? 675 HOH D O   1 
HETATM 10301 O  O   . HOH EA 6 .   ? 14.206  -6.694  63.254  1.00 29.02 ? 676 HOH D O   1 
HETATM 10302 O  O   . HOH EA 6 .   ? 14.843  -10.777 64.941  1.00 39.96 ? 677 HOH D O   1 
HETATM 10303 O  O   . HOH EA 6 .   ? 13.477  -1.878  57.173  1.00 26.65 ? 678 HOH D O   1 
HETATM 10304 O  O   . HOH EA 6 .   ? 17.653  0.822   58.451  1.00 29.31 ? 679 HOH D O   1 
HETATM 10305 O  O   . HOH EA 6 .   ? 15.338  0.890   56.659  1.00 26.49 ? 680 HOH D O   1 
HETATM 10306 O  O   . HOH EA 6 .   ? 17.844  1.045   45.065  1.00 20.57 ? 681 HOH D O   1 
HETATM 10307 O  O   . HOH EA 6 .   ? 10.255  6.221   49.208  1.00 34.83 ? 682 HOH D O   1 
HETATM 10308 O  O   . HOH EA 6 .   ? 12.045  6.173   53.624  1.00 30.29 ? 683 HOH D O   1 
HETATM 10309 O  O   . HOH EA 6 .   ? 38.714  -4.059  33.204  1.00 24.61 ? 684 HOH D O   1 
HETATM 10310 O  O   . HOH EA 6 .   ? 50.471  -0.145  34.748  1.00 36.77 ? 685 HOH D O   1 
HETATM 10311 O  O   . HOH EA 6 .   ? 51.252  -7.154  47.161  1.00 25.66 ? 686 HOH D O   1 
HETATM 10312 O  O   . HOH EA 6 .   ? 46.804  -3.493  51.099  1.00 28.18 ? 687 HOH D O   1 
HETATM 10313 O  O   . HOH EA 6 .   ? 45.985  -4.457  53.388  1.00 31.79 ? 688 HOH D O   1 
HETATM 10314 O  O   . HOH EA 6 .   ? 43.323  1.400   54.232  1.00 29.50 ? 689 HOH D O   1 
HETATM 10315 O  O   . HOH EA 6 .   ? 39.833  3.647   59.808  1.00 26.54 ? 690 HOH D O   1 
HETATM 10316 O  O   . HOH EA 6 .   ? 45.845  -13.480 48.589  1.00 25.37 ? 691 HOH D O   1 
HETATM 10317 O  O   . HOH EA 6 .   ? 50.677  -12.461 52.127  1.00 25.16 ? 692 HOH D O   1 
HETATM 10318 O  O   . HOH EA 6 .   ? 43.463  -22.350 47.314  1.00 30.76 ? 693 HOH D O   1 
HETATM 10319 O  O   . HOH EA 6 .   ? 26.959  -24.237 64.173  1.00 23.71 ? 694 HOH D O   1 
HETATM 10320 O  O   . HOH EA 6 .   ? 32.192  -16.195 66.366  1.00 29.48 ? 695 HOH D O   1 
HETATM 10321 O  O   . HOH EA 6 .   ? 48.010  -8.747  52.393  1.00 23.17 ? 696 HOH D O   1 
HETATM 10322 O  O   . HOH EA 6 .   ? 46.254  -7.498  53.527  1.00 33.40 ? 697 HOH D O   1 
HETATM 10323 O  O   . HOH EA 6 .   ? 49.665  -9.600  63.729  1.00 30.28 ? 698 HOH D O   1 
HETATM 10324 O  O   . HOH EA 6 .   ? 24.900  -22.075 30.979  1.00 32.01 ? 699 HOH D O   1 
HETATM 10325 O  O   . HOH EA 6 .   ? 19.902  -27.578 35.025  1.00 29.82 ? 700 HOH D O   1 
HETATM 10326 O  O   . HOH EA 6 .   ? 14.673  -23.826 39.257  1.00 37.78 ? 701 HOH D O   1 
HETATM 10327 O  O   . HOH EA 6 .   ? 14.633  -21.586 41.238  1.00 22.08 ? 702 HOH D O   1 
HETATM 10328 O  O   . HOH EA 6 .   ? 14.683  -23.318 45.624  1.00 20.75 ? 703 HOH D O   1 
HETATM 10329 O  O   . HOH EA 6 .   ? 4.093   -14.421 53.349  1.00 25.69 ? 704 HOH D O   1 
HETATM 10330 O  O   . HOH EA 6 .   ? 31.664  -22.669 40.977  1.00 25.53 ? 705 HOH D O   1 
HETATM 10331 O  O   . HOH EA 6 .   ? 36.508  -22.733 42.715  1.00 30.15 ? 706 HOH D O   1 
HETATM 10332 O  O   . HOH EA 6 .   ? 48.777  -14.050 34.896  1.00 32.77 ? 707 HOH D O   1 
HETATM 10333 O  O   . HOH EA 6 .   ? 15.699  -21.014 43.526  1.00 20.09 ? 708 HOH D O   1 
HETATM 10334 O  O   . HOH EA 6 .   ? 39.198  10.165  48.233  1.00 15.96 ? 709 HOH D O   1 
HETATM 10335 O  O   . HOH EA 6 .   ? 48.703  -10.350 61.577  1.00 18.44 ? 710 HOH D O   1 
HETATM 10336 O  O   . HOH EA 6 .   ? 45.406  -1.517  32.820  1.00 22.12 ? 711 HOH D O   1 
HETATM 10337 O  O   . HOH EA 6 .   ? 49.360  -3.866  34.520  1.00 22.60 ? 712 HOH D O   1 
HETATM 10338 O  O   . HOH EA 6 .   ? 48.723  -11.870 48.318  1.00 26.05 ? 713 HOH D O   1 
HETATM 10339 O  O   . HOH EA 6 .   ? 44.926  -5.257  67.836  1.00 25.08 ? 714 HOH D O   1 
HETATM 10340 O  O   . HOH EA 6 .   ? 15.450  -19.903 65.196  1.00 28.47 ? 715 HOH D O   1 
HETATM 10341 O  O   . HOH EA 6 .   ? 39.255  9.093   45.176  1.00 24.06 ? 716 HOH D O   1 
HETATM 10342 O  O   . HOH EA 6 .   ? 37.062  10.964  44.492  1.00 18.04 ? 717 HOH D O   1 
HETATM 10343 O  O   . HOH EA 6 .   ? 42.306  1.417   64.270  1.00 20.40 ? 718 HOH D O   1 
HETATM 10344 O  O   . HOH EA 6 .   ? 18.561  -8.215  30.703  1.00 29.63 ? 719 HOH D O   1 
HETATM 10345 O  O   . HOH EA 6 .   ? 19.201  -10.510 31.626  1.00 35.31 ? 720 HOH D O   1 
HETATM 10346 O  O   . HOH EA 6 .   ? 41.698  11.504  48.979  1.00 26.97 ? 721 HOH D O   1 
HETATM 10347 O  O   . HOH EA 6 .   ? 23.816  -29.135 38.039  1.00 40.68 ? 722 HOH D O   1 
HETATM 10348 O  O   . HOH EA 6 .   ? 26.035  12.249  61.997  1.00 24.81 ? 723 HOH D O   1 
HETATM 10349 O  O   . HOH EA 6 .   ? 21.636  9.458   57.089  1.00 11.56 ? 724 HOH D O   1 
HETATM 10350 O  O   . HOH EA 6 .   ? 19.905  7.666   54.761  1.00 13.55 ? 725 HOH D O   1 
HETATM 10351 O  O   . HOH EA 6 .   ? 18.038  9.739   55.508  1.00 17.64 ? 726 HOH D O   1 
HETATM 10352 O  O   . HOH EA 6 .   ? 19.312  10.460  57.651  1.00 22.71 ? 727 HOH D O   1 
HETATM 10353 O  O   . HOH EA 6 .   ? 17.326  12.011  54.499  1.00 11.81 ? 728 HOH D O   1 
HETATM 10354 O  O   . HOH EA 6 .   ? 15.023  10.387  47.164  1.00 23.10 ? 729 HOH D O   1 
HETATM 10355 O  O   . HOH EA 6 .   ? 41.980  5.952   28.388  1.00 32.93 ? 730 HOH D O   1 
HETATM 10356 O  O   . HOH EA 6 .   ? 27.113  7.520   62.937  1.00 36.98 ? 731 HOH D O   1 
HETATM 10357 O  O   . HOH EA 6 .   ? 37.170  -6.449  31.201  1.00 34.63 ? 732 HOH D O   1 
HETATM 10358 O  O   . HOH EA 6 .   ? 40.377  -9.458  31.189  1.00 36.31 ? 733 HOH D O   1 
HETATM 10359 O  O   . HOH EA 6 .   ? 50.647  1.765   43.287  1.00 31.92 ? 734 HOH D O   1 
HETATM 10360 O  O   . HOH EA 6 .   ? 54.567  -12.530 35.841  1.00 20.39 ? 735 HOH D O   1 
HETATM 10361 O  O   . HOH EA 6 .   ? 53.147  -14.715 43.505  1.00 31.45 ? 736 HOH D O   1 
HETATM 10362 O  O   . HOH EA 6 .   ? 49.329  -18.966 51.590  1.00 18.59 ? 737 HOH D O   1 
HETATM 10363 O  O   . HOH EA 6 .   ? 37.015  -29.097 51.641  1.00 26.66 ? 738 HOH D O   1 
HETATM 10364 O  O   . HOH EA 6 .   ? 22.741  -34.115 60.740  1.00 31.39 ? 739 HOH D O   1 
HETATM 10365 O  O   . HOH EA 6 .   ? 47.014  -6.949  58.495  1.00 16.79 ? 740 HOH D O   1 
HETATM 10366 O  O   . HOH EA 6 .   ? 42.183  -10.729 69.673  1.00 26.17 ? 741 HOH D O   1 
HETATM 10367 O  O   . HOH EA 6 .   ? 34.691  -12.044 71.374  1.00 31.82 ? 742 HOH D O   1 
HETATM 10368 O  O   . HOH EA 6 .   ? 29.904  -25.430 42.790  1.00 29.45 ? 743 HOH D O   1 
HETATM 10369 O  O   . HOH EA 6 .   ? 26.882  1.773   62.763  1.00 25.98 ? 744 HOH D O   1 
HETATM 10370 O  O   . HOH EA 6 .   ? 29.396  2.662   63.460  1.00 32.91 ? 745 HOH D O   1 
HETATM 10371 O  O   . HOH EA 6 .   ? 31.501  3.824   62.308  1.00 17.40 ? 746 HOH D O   1 
HETATM 10372 O  O   . HOH EA 6 .   ? 34.325  4.830   59.832  1.00 14.47 ? 747 HOH D O   1 
HETATM 10373 O  O   . HOH EA 6 .   ? 35.085  6.661   54.827  1.00 6.92  ? 748 HOH D O   1 
HETATM 10374 O  O   . HOH EA 6 .   ? -0.473  -1.992  55.340  1.00 30.97 ? 749 HOH D O   1 
HETATM 10375 O  O   . HOH EA 6 .   ? 14.107  -8.863  32.760  1.00 29.08 ? 750 HOH D O   1 
HETATM 10376 O  O   . HOH EA 6 .   ? 20.018  -0.862  36.907  1.00 31.36 ? 751 HOH D O   1 
HETATM 10377 O  O   . HOH EA 6 .   ? 32.774  -5.263  28.865  1.00 42.48 ? 752 HOH D O   1 
HETATM 10378 O  O   . HOH EA 6 .   ? 35.605  -14.430 32.856  1.00 38.04 ? 753 HOH D O   1 
HETATM 10379 O  O   . HOH EA 6 .   ? 33.461  -12.121 32.823  1.00 39.08 ? 754 HOH D O   1 
HETATM 10380 O  O   . HOH EA 6 .   ? 41.723  -7.252  32.904  1.00 40.26 ? 755 HOH D O   1 
HETATM 10381 O  O   . HOH EA 6 .   ? 40.550  -3.306  31.116  1.00 42.81 ? 756 HOH D O   1 
HETATM 10382 O  O   . HOH EA 6 .   ? 12.998  -2.161  33.294  1.00 27.57 ? 757 HOH D O   1 
HETATM 10383 O  O   . HOH EA 6 .   ? 51.250  -16.436 42.863  1.00 30.17 ? 758 HOH D O   1 
HETATM 10384 O  O   . HOH EA 6 .   ? 46.557  -21.586 42.819  1.00 36.13 ? 759 HOH D O   1 
HETATM 10385 O  O   . HOH EA 6 .   ? 40.262  -22.080 41.562  1.00 22.21 ? 760 HOH D O   1 
HETATM 10386 O  O   . HOH EA 6 .   ? 34.342  -26.834 45.648  1.00 37.87 ? 761 HOH D O   1 
HETATM 10387 O  O   . HOH EA 6 .   ? 42.080  -23.223 45.477  1.00 39.49 ? 762 HOH D O   1 
HETATM 10388 O  O   . HOH EA 6 .   ? 46.772  -7.330  49.151  1.00 34.81 ? 763 HOH D O   1 
HETATM 10389 O  O   . HOH EA 6 .   ? 46.498  -25.702 50.636  1.00 33.62 ? 764 HOH D O   1 
HETATM 10390 O  O   . HOH EA 6 .   ? 23.215  -22.492 67.028  1.00 24.34 ? 765 HOH D O   1 
HETATM 10391 O  O   . HOH EA 6 .   ? 28.661  -21.206 64.145  1.00 36.07 ? 766 HOH D O   1 
HETATM 10392 O  O   . HOH EA 6 .   ? 17.742  -17.987 66.908  1.00 41.99 ? 767 HOH D O   1 
HETATM 10393 O  O   . HOH EA 6 .   ? 20.500  -12.171 64.097  1.00 33.10 ? 768 HOH D O   1 
HETATM 10394 O  O   . HOH EA 6 .   ? 17.231  -8.462  62.054  1.00 33.80 ? 769 HOH D O   1 
HETATM 10395 O  O   . HOH EA 6 .   ? 21.618  -10.439 62.934  1.00 34.78 ? 770 HOH D O   1 
HETATM 10396 O  O   . HOH EA 6 .   ? 30.095  -15.051 68.029  1.00 32.31 ? 771 HOH D O   1 
HETATM 10397 O  O   . HOH EA 6 .   ? 42.321  -21.659 64.659  1.00 36.67 ? 772 HOH D O   1 
HETATM 10398 O  O   . HOH EA 6 .   ? 42.064  -6.008  69.780  1.00 34.21 ? 773 HOH D O   1 
HETATM 10399 O  O   . HOH EA 6 .   ? 40.673  -3.343  69.438  1.00 35.69 ? 774 HOH D O   1 
HETATM 10400 O  O   . HOH EA 6 .   ? 31.733  -5.111  70.972  1.00 46.87 ? 775 HOH D O   1 
HETATM 10401 O  O   . HOH EA 6 .   ? 27.309  -7.572  65.431  1.00 32.47 ? 776 HOH D O   1 
HETATM 10402 O  O   . HOH EA 6 .   ? 30.675  -2.858  65.185  1.00 36.45 ? 777 HOH D O   1 
HETATM 10403 O  O   . HOH EA 6 .   ? 35.724  1.022   67.467  1.00 37.60 ? 778 HOH D O   1 
HETATM 10404 O  O   . HOH EA 6 .   ? 35.313  -1.493  65.689  1.00 24.87 ? 779 HOH D O   1 
HETATM 10405 O  O   . HOH EA 6 .   ? 33.238  -1.089  66.578  1.00 31.27 ? 780 HOH D O   1 
HETATM 10406 O  O   . HOH EA 6 .   ? 21.533  -24.986 31.748  1.00 27.09 ? 781 HOH D O   1 
HETATM 10407 O  O   . HOH EA 6 .   ? 17.428  -24.215 33.976  1.00 33.92 ? 782 HOH D O   1 
HETATM 10408 O  O   . HOH EA 6 .   ? 16.792  -21.815 32.978  1.00 28.50 ? 783 HOH D O   1 
HETATM 10409 O  O   . HOH EA 6 .   ? 19.049  -27.139 48.260  1.00 31.74 ? 784 HOH D O   1 
HETATM 10410 O  O   . HOH EA 6 .   ? 14.026  -20.932 45.052  1.00 27.42 ? 785 HOH D O   1 
HETATM 10411 O  O   . HOH EA 6 .   ? 11.323  -20.544 43.962  1.00 33.38 ? 786 HOH D O   1 
HETATM 10412 O  O   . HOH EA 6 .   ? 50.931  -13.678 39.115  1.00 28.54 ? 787 HOH D O   1 
HETATM 10413 O  O   . HOH EA 6 .   ? 43.833  6.390   48.350  1.00 22.70 ? 788 HOH D O   1 
HETATM 10414 O  O   . HOH EA 6 .   ? 6.913   -19.823 63.249  1.00 34.95 ? 789 HOH D O   1 
HETATM 10415 O  O   . HOH EA 6 .   ? 6.865   -19.326 60.802  1.00 29.37 ? 790 HOH D O   1 
HETATM 10416 O  O   . HOH EA 6 .   ? 42.568  7.413   25.337  1.00 34.61 ? 791 HOH D O   1 
HETATM 10417 O  O   . HOH EA 6 .   ? 34.624  -14.216 68.961  1.00 37.29 ? 792 HOH D O   1 
HETATM 10418 O  O   . HOH EA 6 .   ? 40.919  -12.249 70.759  1.00 43.54 ? 793 HOH D O   1 
HETATM 10419 O  O   . HOH EA 6 .   ? 13.177  -25.727 46.847  1.00 27.07 ? 794 HOH D O   1 
HETATM 10420 O  O   . HOH EA 6 .   ? 20.634  6.849   61.662  1.00 42.89 ? 795 HOH D O   1 
HETATM 10421 O  O   . HOH EA 6 .   ? 23.311  -9.556  30.698  1.00 43.90 ? 796 HOH D O   1 
HETATM 10422 O  O   . HOH EA 6 .   ? 4.154   0.126   50.554  1.00 37.73 ? 797 HOH D O   1 
HETATM 10423 O  O   . HOH EA 6 .   ? 46.742  1.990   35.050  1.00 30.75 ? 798 HOH D O   1 
HETATM 10424 O  O   . HOH EA 6 .   ? 46.970  -17.005 63.520  1.00 42.56 ? 799 HOH D O   1 
HETATM 10425 O  O   . HOH EA 6 .   ? 16.545  -25.368 36.062  1.00 41.28 ? 800 HOH D O   1 
HETATM 10426 O  O   . HOH EA 6 .   ? 42.168  6.432   39.745  1.00 27.37 ? 801 HOH D O   1 
HETATM 10427 O  O   . HOH EA 6 .   ? 40.546  9.467   38.087  1.00 28.23 ? 802 HOH D O   1 
HETATM 10428 O  O   . HOH EA 6 .   ? 23.497  -13.628 31.320  1.00 31.43 ? 803 HOH D O   1 
HETATM 10429 O  O   . HOH EA 6 .   ? 26.082  -17.924 31.594  1.00 41.68 ? 804 HOH D O   1 
HETATM 10430 O  O   . HOH EA 6 .   ? 32.154  -23.761 36.177  1.00 37.71 ? 805 HOH D O   1 
HETATM 10431 O  O   . HOH EA 6 .   ? 26.716  -26.203 42.276  1.00 31.73 ? 806 HOH D O   1 
HETATM 10432 O  O   . HOH EA 6 .   ? 29.906  -22.345 39.659  1.00 28.02 ? 807 HOH D O   1 
HETATM 10433 O  O   . HOH EA 6 .   ? 21.840  -22.284 30.821  1.00 32.02 ? 808 HOH D O   1 
HETATM 10434 O  O   . HOH EA 6 .   ? 18.026  -18.684 30.472  1.00 34.21 ? 809 HOH D O   1 
HETATM 10435 O  O   . HOH EA 6 .   ? 43.239  -15.099 30.407  1.00 29.03 ? 810 HOH D 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   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   TRP 4   4   4   TRP TRP A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  TRP 15  15  15  TRP TRP A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY 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  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN 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  TYR 85  85  85  TYR TYR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 THR 205 205 205 THR THR 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 TRP 208 208 208 TRP TRP A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   TRP 4   4   4   TRP TRP B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  TRP 15  15  15  TRP TRP B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY 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  LEU 26  26  26  LEU LEU B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASN 52  52  52  ASN ASN B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  MET 76  76  76  MET MET B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  GLN 82  82  82  GLN GLN 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  TYR 85  85  85  TYR TYR B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 GLN 163 163 163 GLN GLN B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLN 170 170 170 GLN GLN B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TYR 191 191 191 TYR TYR B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 CYS 202 202 202 CYS CYS B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 THR 205 205 205 THR THR 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 TRP 208 208 208 TRP TRP B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 ARG 212 212 212 ARG ARG B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 CYS 231 231 231 CYS CYS B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  TRP 15  15  15  TRP TRP C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TYR 19  19  19  TYR TYR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ASP 35  35  35  ASP ASP C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASN 52  52  52  ASN ASN C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  HIS 77  77  77  HIS HIS C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  PRO 97  97  97  PRO PRO C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASP 99  99  99  ASP ASP C . n 
C 1 100 PRO 100 100 100 PRO PRO C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 HIS 105 105 105 HIS HIS C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 TYR 126 126 126 TYR TYR C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 ALA 129 129 129 ALA ALA C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 THR 131 131 131 THR THR C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 MET 148 148 148 MET MET C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 154 SER SER C . n 
C 1 155 TYR 155 155 155 TYR TYR C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LYS 157 157 157 LYS LYS C . n 
C 1 158 ILE 158 158 158 ILE ILE C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 GLN 163 163 163 GLN GLN C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 PHE 173 173 173 PHE PHE C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ARG 192 192 192 ARG ARG C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 CYS 202 202 202 CYS CYS C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 THR 209 209 209 THR THR C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 VAL 215 215 215 VAL VAL C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 GLU 226 226 226 GLU GLU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ASP 236 236 236 ASP ASP C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 SER 238 238 238 SER SER C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 ARG 240 240 240 ARG ARG C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 MET 242 242 242 MET MET C . n 
C 1 243 ILE 243 243 243 ILE ILE C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASN 245 245 245 ASN ASN C . n 
C 1 246 PHE 246 246 246 PHE PHE C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 TYR 258 258 258 TYR TYR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 GLN 263 263 263 GLN GLN C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   SER 2   2   ?   ?   ?   D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   TRP 4   4   4   TRP TRP D . n 
D 1 5   THR 5   5   5   THR THR D . n 
D 1 6   TYR 6   6   6   TYR TYR D . n 
D 1 7   PHE 7   7   7   PHE PHE D . n 
D 1 8   GLY 8   8   8   GLY GLY D . n 
D 1 9   PRO 9   9   9   PRO PRO D . n 
D 1 10  ASP 10  10  10  ASP ASP D . n 
D 1 11  GLY 11  11  11  GLY GLY D . n 
D 1 12  GLU 12  12  12  GLU GLU D . n 
D 1 13  ASN 13  13  13  ASN ASN D . n 
D 1 14  SER 14  14  14  SER SER D . n 
D 1 15  TRP 15  15  15  TRP TRP D . n 
D 1 16  SER 16  16  16  SER SER D . n 
D 1 17  LYS 17  17  17  LYS LYS D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  TYR 19  19  19  TYR TYR D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  CYS 22  22  22  CYS CYS D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLY 24  24  24  GLY GLY D . n 
D 1 25  LEU 25  25  25  LEU LEU D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  GLN 27  27  27  GLN GLN D . n 
D 1 28  SER 28  28  28  SER SER D . n 
D 1 29  PRO 29  29  29  PRO PRO D . n 
D 1 30  ILE 30  30  30  ILE ILE D . n 
D 1 31  ASP 31  31  31  ASP ASP D . n 
D 1 32  LEU 32  32  32  LEU LEU D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ASP 35  35  35  ASP ASP D . n 
D 1 36  ILE 36  36  36  ILE ILE D . n 
D 1 37  LEU 37  37  37  LEU LEU D . n 
D 1 38  GLN 38  38  38  GLN GLN D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  ASP 40  40  40  ASP ASP D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  THR 44  44  44  THR THR D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  GLN 49  49  49  GLN GLN D . n 
D 1 50  GLY 50  50  50  GLY GLY D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ASN 52  52  52  ASN ASN D . n 
D 1 53  LEU 53  53  53  LEU LEU D . n 
D 1 54  SER 54  54  54  SER SER D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  ASN 56  56  56  ASN ASN D . n 
D 1 57  LYS 57  57  57  LYS LYS D . n 
D 1 58  GLN 58  58  58  GLN GLN D . n 
D 1 59  PHE 59  59  59  PHE PHE D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  THR 62  62  62  THR THR D . n 
D 1 63  ASN 63  63  63  ASN ASN D . n 
D 1 64  ASN 64  64  64  ASN ASN D . n 
D 1 65  GLY 65  65  65  GLY GLY D . n 
D 1 66  HIS 66  66  66  HIS HIS D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  ASN 71  71  71  ASN ASN D . n 
D 1 72  LEU 72  72  72  LEU LEU D . n 
D 1 73  PRO 73  73  73  PRO PRO D . n 
D 1 74  SER 74  74  74  SER SER D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  MET 76  76  76  MET MET D . n 
D 1 77  HIS 77  77  77  HIS HIS D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  GLN 79  79  79  GLN GLN D . n 
D 1 80  GLY 80  80  80  GLY GLY D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  GLN 82  82  82  GLN GLN D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  ARG 84  84  84  ARG ARG D . n 
D 1 85  TYR 85  85  85  TYR TYR D . n 
D 1 86  SER 86  86  86  SER SER D . n 
D 1 87  ALA 87  87  87  ALA ALA D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  GLN 89  89  89  GLN GLN D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  HIS 91  91  91  HIS HIS D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  HIS 93  93  93  HIS HIS D . n 
D 1 94  TRP 94  94  94  TRP TRP D . n 
D 1 95  GLY 95  95  95  GLY GLY D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  PRO 97  97  97  PRO PRO D . n 
D 1 98  ASN 98  98  98  ASN ASN D . n 
D 1 99  ASP 99  99  99  ASP ASP D . n 
D 1 100 PRO 100 100 100 PRO PRO D . n 
D 1 101 HIS 101 101 101 HIS HIS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 SER 103 103 103 SER SER D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 HIS 105 105 105 HIS HIS D . n 
D 1 106 THR 106 106 106 THR THR D . n 
D 1 107 VAL 107 107 107 VAL VAL D . n 
D 1 108 SER 108 108 108 SER SER D . n 
D 1 109 GLY 109 109 109 GLY GLY D . n 
D 1 110 GLN 110 110 110 GLN GLN D . n 
D 1 111 HIS 111 111 111 HIS HIS D . n 
D 1 112 PHE 112 112 112 PHE PHE D . n 
D 1 113 ALA 113 113 113 ALA ALA D . n 
D 1 114 ALA 114 114 114 ALA ALA D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 HIS 117 117 117 HIS HIS D . n 
D 1 118 ILE 118 118 118 ILE ILE D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 TYR 121 121 121 TYR TYR D . n 
D 1 122 ASN 122 122 122 ASN ASN D . n 
D 1 123 SER 123 123 123 SER SER D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 TYR 126 126 126 TYR TYR D . n 
D 1 127 PRO 127 127 127 PRO PRO D . n 
D 1 128 ASP 128 128 128 ASP ASP D . n 
D 1 129 ALA 129 129 129 ALA ALA D . n 
D 1 130 SER 130 130 130 SER SER D . n 
D 1 131 THR 131 131 131 THR THR D . n 
D 1 132 ALA 132 132 132 ALA ALA D . n 
D 1 133 SER 133 133 133 SER SER D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 LYS 135 135 135 LYS LYS D . n 
D 1 136 SER 136 136 136 SER SER D . n 
D 1 137 GLU 137 137 137 GLU GLU D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 VAL 141 141 141 VAL VAL D . n 
D 1 142 LEU 142 142 142 LEU LEU D . n 
D 1 143 ALA 143 143 143 ALA ALA D . n 
D 1 144 VAL 144 144 144 VAL VAL D . n 
D 1 145 LEU 145 145 145 LEU LEU D . n 
D 1 146 ILE 146 146 146 ILE ILE D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 MET 148 148 148 MET MET D . n 
D 1 149 GLY 149 149 149 GLY GLY D . n 
D 1 150 SER 150 150 150 SER SER D . n 
D 1 151 PHE 151 151 151 PHE PHE D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 PRO 153 153 153 PRO PRO D . n 
D 1 154 SER 154 154 154 SER SER D . n 
D 1 155 TYR 155 155 155 TYR TYR D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 LYS 157 157 157 LYS LYS D . n 
D 1 158 ILE 158 158 158 ILE ILE D . n 
D 1 159 PHE 159 159 159 PHE PHE D . n 
D 1 160 SER 160 160 160 SER SER D . n 
D 1 161 HIS 161 161 161 HIS HIS D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 GLN 163 163 163 GLN GLN D . n 
D 1 164 HIS 164 164 164 HIS HIS D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 LYS 166 166 166 LYS LYS D . n 
D 1 167 TYR 167 167 167 TYR TYR D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 GLY 169 169 169 GLY GLY D . n 
D 1 170 GLN 170 170 170 GLN GLN D . n 
D 1 171 GLU 171 171 171 GLU GLU D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 PHE 173 173 173 PHE PHE D . n 
D 1 174 VAL 174 174 174 VAL VAL D . n 
D 1 175 PRO 175 175 175 PRO PRO D . n 
D 1 176 GLY 176 176 176 GLY GLY D . n 
D 1 177 PHE 177 177 177 PHE PHE D . n 
D 1 178 ASN 178 178 178 ASN ASN D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 GLU 180 180 180 GLU GLU D . n 
D 1 181 GLU 181 181 181 GLU GLU D . n 
D 1 182 LEU 182 182 182 LEU LEU D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 PRO 184 184 184 PRO PRO D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 ARG 186 186 186 ARG ARG D . n 
D 1 187 THR 187 187 187 THR THR D . n 
D 1 188 ALA 188 188 188 ALA ALA D . n 
D 1 189 GLU 189 189 189 GLU GLU D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 TYR 191 191 191 TYR TYR D . n 
D 1 192 ARG 192 192 192 ARG ARG D . n 
D 1 193 TYR 193 193 193 TYR TYR D . n 
D 1 194 ARG 194 194 194 ARG ARG D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 THR 199 199 199 THR THR D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 PRO 201 201 201 PRO PRO D . n 
D 1 202 CYS 202 202 202 CYS CYS D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 PRO 204 204 204 PRO PRO D . n 
D 1 205 THR 205 205 205 THR THR D . n 
D 1 206 VAL 206 206 206 VAL VAL D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 TRP 208 208 208 TRP TRP D . n 
D 1 209 THR 209 209 209 THR THR D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 PHE 211 211 211 PHE PHE D . n 
D 1 212 ARG 212 212 212 ARG ARG D . n 
D 1 213 ASN 213 213 213 ASN ASN D . n 
D 1 214 PRO 214 214 214 PRO PRO D . n 
D 1 215 VAL 215 215 215 VAL VAL D . n 
D 1 216 GLN 216 216 216 GLN GLN D . n 
D 1 217 ILE 217 217 217 ILE ILE D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 GLN 219 219 219 GLN GLN D . n 
D 1 220 GLU 220 220 220 GLU GLU D . n 
D 1 221 GLN 221 221 221 GLN GLN D . n 
D 1 222 LEU 222 222 222 LEU LEU D . n 
D 1 223 LEU 223 223 223 LEU LEU D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 LEU 225 225 225 LEU LEU D . n 
D 1 226 GLU 226 226 226 GLU GLU D . n 
D 1 227 THR 227 227 227 THR THR D . n 
D 1 228 ALA 228 228 228 ALA ALA D . n 
D 1 229 LEU 229 229 229 LEU LEU D . n 
D 1 230 TYR 230 230 230 TYR TYR D . n 
D 1 231 CYS 231 231 231 CYS CYS D . n 
D 1 232 THR 232 232 232 THR THR D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 MET 234 234 234 MET MET D . n 
D 1 235 ASP 235 235 235 ASP ASP D . n 
D 1 236 ASP 236 236 236 ASP ASP D . n 
D 1 237 PRO 237 237 237 PRO PRO D . n 
D 1 238 SER 238 238 238 SER SER D . n 
D 1 239 PRO 239 239 239 PRO PRO D . n 
D 1 240 ARG 240 240 240 ARG ARG D . n 
D 1 241 GLU 241 241 241 GLU GLU D . n 
D 1 242 MET 242 242 242 MET MET D . n 
D 1 243 ILE 243 243 243 ILE ILE D . n 
D 1 244 ASN 244 244 244 ASN ASN D . n 
D 1 245 ASN 245 245 245 ASN ASN D . n 
D 1 246 PHE 246 246 246 PHE PHE D . n 
D 1 247 ARG 247 247 247 ARG ARG D . n 
D 1 248 GLN 248 248 248 GLN GLN D . n 
D 1 249 VAL 249 249 249 VAL VAL D . n 
D 1 250 GLN 250 250 250 GLN GLN D . n 
D 1 251 LYS 251 251 251 LYS LYS D . n 
D 1 252 PHE 252 252 252 PHE PHE D . n 
D 1 253 ASP 253 253 253 ASP ASP D . n 
D 1 254 GLU 254 254 254 GLU GLU D . n 
D 1 255 ARG 255 255 255 ARG ARG D . n 
D 1 256 LEU 256 256 256 LEU LEU D . n 
D 1 257 VAL 257 257 257 VAL VAL D . n 
D 1 258 TYR 258 258 258 TYR TYR D . n 
D 1 259 THR 259 259 259 THR THR D . n 
D 1 260 SER 260 260 260 SER SER D . n 
D 1 261 PHE 261 261 261 PHE PHE D . n 
D 1 262 SER 262 262 262 SER SER D . n 
D 1 263 GLN 263 263 263 GLN GLN D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 ZN  1   301 1    ZN  ZN  A . 
F  3 V50 1   302 4    V50 V50 A . 
G  4 PEG 1   303 3    PEG PEG A . 
H  5 EDO 1   304 1    EDO EGL A . 
I  5 EDO 1   305 6    EDO EGL A . 
J  5 EDO 1   306 12   EDO EGL A . 
K  2 ZN  1   301 2    ZN  ZN  B . 
L  3 V50 1   302 1    V50 V50 B . 
M  4 PEG 1   303 2    PEG PEG B . 
N  5 EDO 1   304 2    EDO EGL B . 
O  5 EDO 1   305 3    EDO EGL B . 
P  5 EDO 1   306 9    EDO EGL B . 
Q  5 EDO 1   307 10   EDO EGL B . 
R  5 EDO 1   308 11   EDO EGL B . 
S  2 ZN  1   301 3    ZN  ZN  C . 
T  3 V50 1   302 2    V50 V50 C . 
U  5 EDO 1   303 8    EDO EGL C . 
V  2 ZN  1   301 4    ZN  ZN  D . 
W  3 V50 1   302 3    V50 V50 D . 
X  4 PEG 1   303 1    PEG PEG D . 
Y  5 EDO 1   304 4    EDO EGL D . 
Z  5 EDO 1   305 5    EDO EGL D . 
AA 5 EDO 1   306 7    EDO EGL D . 
BA 6 HOH 1   401 3    HOH HOH A . 
BA 6 HOH 2   402 9    HOH HOH A . 
BA 6 HOH 3   403 12   HOH HOH A . 
BA 6 HOH 4   404 13   HOH HOH A . 
BA 6 HOH 5   405 19   HOH HOH A . 
BA 6 HOH 6   406 24   HOH HOH A . 
BA 6 HOH 7   407 26   HOH HOH A . 
BA 6 HOH 8   408 31   HOH HOH A . 
BA 6 HOH 9   409 40   HOH HOH A . 
BA 6 HOH 10  410 50   HOH HOH A . 
BA 6 HOH 11  411 53   HOH HOH A . 
BA 6 HOH 12  412 56   HOH HOH A . 
BA 6 HOH 13  413 57   HOH HOH A . 
BA 6 HOH 14  414 59   HOH HOH A . 
BA 6 HOH 15  415 62   HOH HOH A . 
BA 6 HOH 16  416 65   HOH HOH A . 
BA 6 HOH 17  417 74   HOH HOH A . 
BA 6 HOH 18  418 83   HOH HOH A . 
BA 6 HOH 19  419 89   HOH HOH A . 
BA 6 HOH 20  420 92   HOH HOH A . 
BA 6 HOH 21  421 103  HOH HOH A . 
BA 6 HOH 22  422 106  HOH HOH A . 
BA 6 HOH 23  423 138  HOH HOH A . 
BA 6 HOH 24  424 147  HOH HOH A . 
BA 6 HOH 25  425 157  HOH HOH A . 
BA 6 HOH 26  426 162  HOH HOH A . 
BA 6 HOH 27  427 172  HOH HOH A . 
BA 6 HOH 28  428 176  HOH HOH A . 
BA 6 HOH 29  429 180  HOH HOH A . 
BA 6 HOH 30  430 183  HOH HOH A . 
BA 6 HOH 31  431 198  HOH HOH A . 
BA 6 HOH 32  432 199  HOH HOH A . 
BA 6 HOH 33  433 207  HOH HOH A . 
BA 6 HOH 34  434 208  HOH HOH A . 
BA 6 HOH 35  435 211  HOH HOH A . 
BA 6 HOH 36  436 218  HOH HOH A . 
BA 6 HOH 37  437 230  HOH HOH A . 
BA 6 HOH 38  438 243  HOH HOH A . 
BA 6 HOH 39  439 244  HOH HOH A . 
BA 6 HOH 40  440 252  HOH HOH A . 
BA 6 HOH 41  441 253  HOH HOH A . 
BA 6 HOH 42  442 272  HOH HOH A . 
BA 6 HOH 43  443 284  HOH HOH A . 
BA 6 HOH 44  444 296  HOH HOH A . 
BA 6 HOH 45  445 306  HOH HOH A . 
BA 6 HOH 46  446 340  HOH HOH A . 
BA 6 HOH 47  447 348  HOH HOH A . 
BA 6 HOH 48  448 349  HOH HOH A . 
BA 6 HOH 49  449 351  HOH HOH A . 
BA 6 HOH 50  450 372  HOH HOH A . 
BA 6 HOH 51  451 378  HOH HOH A . 
BA 6 HOH 52  452 383  HOH HOH A . 
BA 6 HOH 53  453 384  HOH HOH A . 
BA 6 HOH 54  454 385  HOH HOH A . 
BA 6 HOH 55  455 386  HOH HOH A . 
BA 6 HOH 56  456 387  HOH HOH A . 
BA 6 HOH 57  457 388  HOH HOH A . 
BA 6 HOH 58  458 389  HOH HOH A . 
BA 6 HOH 59  459 390  HOH HOH A . 
BA 6 HOH 60  460 391  HOH HOH A . 
BA 6 HOH 61  461 392  HOH HOH A . 
BA 6 HOH 62  462 393  HOH HOH A . 
BA 6 HOH 63  463 394  HOH HOH A . 
BA 6 HOH 64  464 395  HOH HOH A . 
BA 6 HOH 65  465 396  HOH HOH A . 
BA 6 HOH 66  466 397  HOH HOH A . 
BA 6 HOH 67  467 408  HOH HOH A . 
BA 6 HOH 68  468 416  HOH HOH A . 
BA 6 HOH 69  469 417  HOH HOH A . 
BA 6 HOH 70  470 418  HOH HOH A . 
BA 6 HOH 71  471 424  HOH HOH A . 
BA 6 HOH 72  472 440  HOH HOH A . 
BA 6 HOH 73  473 451  HOH HOH A . 
BA 6 HOH 74  474 478  HOH HOH A . 
BA 6 HOH 75  475 481  HOH HOH A . 
BA 6 HOH 76  476 483  HOH HOH A . 
BA 6 HOH 77  477 487  HOH HOH A . 
BA 6 HOH 78  478 495  HOH HOH A . 
BA 6 HOH 79  479 496  HOH HOH A . 
BA 6 HOH 80  480 499  HOH HOH A . 
BA 6 HOH 81  481 500  HOH HOH A . 
BA 6 HOH 82  482 502  HOH HOH A . 
BA 6 HOH 83  483 504  HOH HOH A . 
BA 6 HOH 84  484 506  HOH HOH A . 
BA 6 HOH 85  485 507  HOH HOH A . 
BA 6 HOH 86  486 509  HOH HOH A . 
BA 6 HOH 87  487 511  HOH HOH A . 
BA 6 HOH 88  488 517  HOH HOH A . 
BA 6 HOH 89  489 518  HOH HOH A . 
BA 6 HOH 90  490 519  HOH HOH A . 
BA 6 HOH 91  491 520  HOH HOH A . 
BA 6 HOH 92  492 522  HOH HOH A . 
BA 6 HOH 93  493 524  HOH HOH A . 
BA 6 HOH 94  494 526  HOH HOH A . 
BA 6 HOH 95  495 528  HOH HOH A . 
BA 6 HOH 96  496 533  HOH HOH A . 
BA 6 HOH 97  497 536  HOH HOH A . 
BA 6 HOH 98  498 538  HOH HOH A . 
BA 6 HOH 99  499 543  HOH HOH A . 
BA 6 HOH 100 500 545  HOH HOH A . 
BA 6 HOH 101 501 547  HOH HOH A . 
BA 6 HOH 102 502 548  HOH HOH A . 
BA 6 HOH 103 503 554  HOH HOH A . 
BA 6 HOH 104 504 555  HOH HOH A . 
BA 6 HOH 105 505 557  HOH HOH A . 
BA 6 HOH 106 506 558  HOH HOH A . 
BA 6 HOH 107 507 563  HOH HOH A . 
BA 6 HOH 108 508 564  HOH HOH A . 
BA 6 HOH 109 509 569  HOH HOH A . 
BA 6 HOH 110 510 572  HOH HOH A . 
BA 6 HOH 111 511 575  HOH HOH A . 
BA 6 HOH 112 512 579  HOH HOH A . 
BA 6 HOH 113 513 583  HOH HOH A . 
BA 6 HOH 114 514 587  HOH HOH A . 
BA 6 HOH 115 515 594  HOH HOH A . 
BA 6 HOH 116 516 595  HOH HOH A . 
BA 6 HOH 117 517 597  HOH HOH A . 
BA 6 HOH 118 518 598  HOH HOH A . 
BA 6 HOH 119 519 600  HOH HOH A . 
BA 6 HOH 120 520 606  HOH HOH A . 
BA 6 HOH 121 521 615  HOH HOH A . 
BA 6 HOH 122 522 616  HOH HOH A . 
BA 6 HOH 123 523 619  HOH HOH A . 
BA 6 HOH 124 524 621  HOH HOH A . 
BA 6 HOH 125 525 623  HOH HOH A . 
BA 6 HOH 126 526 624  HOH HOH A . 
BA 6 HOH 127 527 625  HOH HOH A . 
BA 6 HOH 128 528 629  HOH HOH A . 
BA 6 HOH 129 529 640  HOH HOH A . 
BA 6 HOH 130 530 641  HOH HOH A . 
BA 6 HOH 131 531 642  HOH HOH A . 
BA 6 HOH 132 532 644  HOH HOH A . 
BA 6 HOH 133 533 647  HOH HOH A . 
BA 6 HOH 134 534 648  HOH HOH A . 
BA 6 HOH 135 535 652  HOH HOH A . 
BA 6 HOH 136 536 653  HOH HOH A . 
BA 6 HOH 137 537 660  HOH HOH A . 
BA 6 HOH 138 538 662  HOH HOH A . 
BA 6 HOH 139 539 664  HOH HOH A . 
BA 6 HOH 140 540 666  HOH HOH A . 
BA 6 HOH 141 541 669  HOH HOH A . 
BA 6 HOH 142 542 670  HOH HOH A . 
BA 6 HOH 143 543 671  HOH HOH A . 
BA 6 HOH 144 544 672  HOH HOH A . 
BA 6 HOH 145 545 675  HOH HOH A . 
BA 6 HOH 146 546 677  HOH HOH A . 
BA 6 HOH 147 547 683  HOH HOH A . 
BA 6 HOH 148 548 693  HOH HOH A . 
BA 6 HOH 149 549 694  HOH HOH A . 
BA 6 HOH 150 550 696  HOH HOH A . 
BA 6 HOH 151 551 700  HOH HOH A . 
BA 6 HOH 152 552 701  HOH HOH A . 
BA 6 HOH 153 553 702  HOH HOH A . 
BA 6 HOH 154 554 706  HOH HOH A . 
BA 6 HOH 155 555 710  HOH HOH A . 
BA 6 HOH 156 556 716  HOH HOH A . 
BA 6 HOH 157 557 721  HOH HOH A . 
BA 6 HOH 158 558 722  HOH HOH A . 
BA 6 HOH 159 559 723  HOH HOH A . 
BA 6 HOH 160 560 725  HOH HOH A . 
BA 6 HOH 161 561 726  HOH HOH A . 
BA 6 HOH 162 562 728  HOH HOH A . 
BA 6 HOH 163 563 730  HOH HOH A . 
BA 6 HOH 164 564 733  HOH HOH A . 
BA 6 HOH 165 565 740  HOH HOH A . 
BA 6 HOH 166 566 741  HOH HOH A . 
BA 6 HOH 167 567 742  HOH HOH A . 
BA 6 HOH 168 568 745  HOH HOH A . 
BA 6 HOH 169 569 746  HOH HOH A . 
BA 6 HOH 170 570 753  HOH HOH A . 
BA 6 HOH 171 571 755  HOH HOH A . 
BA 6 HOH 172 572 766  HOH HOH A . 
BA 6 HOH 173 573 782  HOH HOH A . 
BA 6 HOH 174 574 788  HOH HOH A . 
BA 6 HOH 175 575 797  HOH HOH A . 
BA 6 HOH 176 576 798  HOH HOH A . 
BA 6 HOH 177 577 800  HOH HOH A . 
BA 6 HOH 178 578 801  HOH HOH A . 
BA 6 HOH 179 579 803  HOH HOH A . 
BA 6 HOH 180 580 804  HOH HOH A . 
BA 6 HOH 181 581 807  HOH HOH A . 
BA 6 HOH 182 582 814  HOH HOH A . 
BA 6 HOH 183 583 821  HOH HOH A . 
BA 6 HOH 184 584 826  HOH HOH A . 
BA 6 HOH 185 585 836  HOH HOH A . 
BA 6 HOH 186 586 841  HOH HOH A . 
BA 6 HOH 187 587 842  HOH HOH A . 
BA 6 HOH 188 588 843  HOH HOH A . 
BA 6 HOH 189 589 844  HOH HOH A . 
BA 6 HOH 190 590 845  HOH HOH A . 
BA 6 HOH 191 591 846  HOH HOH A . 
BA 6 HOH 192 592 908  HOH HOH A . 
BA 6 HOH 193 593 909  HOH HOH A . 
BA 6 HOH 194 594 910  HOH HOH A . 
BA 6 HOH 195 595 911  HOH HOH A . 
BA 6 HOH 196 596 913  HOH HOH A . 
BA 6 HOH 197 597 920  HOH HOH A . 
BA 6 HOH 198 598 929  HOH HOH A . 
BA 6 HOH 199 599 930  HOH HOH A . 
BA 6 HOH 200 600 931  HOH HOH A . 
BA 6 HOH 201 601 944  HOH HOH A . 
BA 6 HOH 202 602 945  HOH HOH A . 
BA 6 HOH 203 603 946  HOH HOH A . 
BA 6 HOH 204 604 947  HOH HOH A . 
BA 6 HOH 205 605 950  HOH HOH A . 
BA 6 HOH 206 606 951  HOH HOH A . 
BA 6 HOH 207 607 952  HOH HOH A . 
BA 6 HOH 208 608 957  HOH HOH A . 
BA 6 HOH 209 609 958  HOH HOH A . 
BA 6 HOH 210 610 965  HOH HOH A . 
BA 6 HOH 211 611 966  HOH HOH A . 
BA 6 HOH 212 612 967  HOH HOH A . 
BA 6 HOH 213 613 968  HOH HOH A . 
BA 6 HOH 214 614 969  HOH HOH A . 
BA 6 HOH 215 615 970  HOH HOH A . 
BA 6 HOH 216 616 971  HOH HOH A . 
BA 6 HOH 217 617 972  HOH HOH A . 
BA 6 HOH 218 618 973  HOH HOH A . 
BA 6 HOH 219 619 974  HOH HOH A . 
BA 6 HOH 220 620 975  HOH HOH A . 
BA 6 HOH 221 621 976  HOH HOH A . 
BA 6 HOH 222 622 977  HOH HOH A . 
BA 6 HOH 223 623 978  HOH HOH A . 
BA 6 HOH 224 624 979  HOH HOH A . 
BA 6 HOH 225 625 980  HOH HOH A . 
BA 6 HOH 226 626 981  HOH HOH A . 
BA 6 HOH 227 627 982  HOH HOH A . 
BA 6 HOH 228 628 983  HOH HOH A . 
BA 6 HOH 229 629 984  HOH HOH A . 
BA 6 HOH 230 630 985  HOH HOH A . 
BA 6 HOH 231 631 986  HOH HOH A . 
BA 6 HOH 232 632 987  HOH HOH A . 
BA 6 HOH 233 633 988  HOH HOH A . 
BA 6 HOH 234 634 989  HOH HOH A . 
BA 6 HOH 235 635 990  HOH HOH A . 
BA 6 HOH 236 636 991  HOH HOH A . 
BA 6 HOH 237 637 992  HOH HOH A . 
BA 6 HOH 238 638 993  HOH HOH A . 
BA 6 HOH 239 639 994  HOH HOH A . 
BA 6 HOH 240 640 995  HOH HOH A . 
BA 6 HOH 241 641 996  HOH HOH A . 
BA 6 HOH 242 642 997  HOH HOH A . 
BA 6 HOH 243 643 998  HOH HOH A . 
BA 6 HOH 244 644 999  HOH HOH A . 
BA 6 HOH 245 645 1000 HOH HOH A . 
BA 6 HOH 246 646 1001 HOH HOH A . 
BA 6 HOH 247 647 1002 HOH HOH A . 
BA 6 HOH 248 648 1003 HOH HOH A . 
BA 6 HOH 249 649 1012 HOH HOH A . 
BA 6 HOH 250 650 1106 HOH HOH A . 
BA 6 HOH 251 651 1107 HOH HOH A . 
BA 6 HOH 252 652 1111 HOH HOH A . 
BA 6 HOH 253 653 1112 HOH HOH A . 
BA 6 HOH 254 654 1113 HOH HOH A . 
BA 6 HOH 255 655 1114 HOH HOH A . 
BA 6 HOH 256 656 1115 HOH HOH A . 
BA 6 HOH 257 657 1116 HOH HOH A . 
BA 6 HOH 258 658 1117 HOH HOH A . 
BA 6 HOH 259 659 1123 HOH HOH A . 
BA 6 HOH 260 660 1124 HOH HOH A . 
BA 6 HOH 261 661 1126 HOH HOH A . 
BA 6 HOH 262 662 1127 HOH HOH A . 
BA 6 HOH 263 663 1128 HOH HOH A . 
BA 6 HOH 264 664 1139 HOH HOH A . 
BA 6 HOH 265 665 1140 HOH HOH A . 
BA 6 HOH 266 666 1141 HOH HOH A . 
BA 6 HOH 267 667 1142 HOH HOH A . 
BA 6 HOH 268 668 1143 HOH HOH A . 
BA 6 HOH 269 669 1144 HOH HOH A . 
BA 6 HOH 270 670 1155 HOH HOH A . 
BA 6 HOH 271 671 1157 HOH HOH A . 
BA 6 HOH 272 672 1158 HOH HOH A . 
BA 6 HOH 273 673 1163 HOH HOH A . 
BA 6 HOH 274 674 1170 HOH HOH A . 
BA 6 HOH 275 675 1174 HOH HOH A . 
BA 6 HOH 276 676 1175 HOH HOH A . 
BA 6 HOH 277 677 1180 HOH HOH A . 
BA 6 HOH 278 678 1192 HOH HOH A . 
BA 6 HOH 279 679 1193 HOH HOH A . 
BA 6 HOH 280 680 1194 HOH HOH A . 
BA 6 HOH 281 681 1195 HOH HOH A . 
BA 6 HOH 282 682 1196 HOH HOH A . 
BA 6 HOH 283 683 1197 HOH HOH A . 
BA 6 HOH 284 684 1198 HOH HOH A . 
BA 6 HOH 285 685 1199 HOH HOH A . 
BA 6 HOH 286 686 1200 HOH HOH A . 
BA 6 HOH 287 687 1201 HOH HOH A . 
BA 6 HOH 288 688 1202 HOH HOH A . 
BA 6 HOH 289 689 1203 HOH HOH A . 
BA 6 HOH 290 690 1204 HOH HOH A . 
BA 6 HOH 291 691 1205 HOH HOH A . 
BA 6 HOH 292 692 1206 HOH HOH A . 
BA 6 HOH 293 693 1207 HOH HOH A . 
BA 6 HOH 294 694 1208 HOH HOH A . 
BA 6 HOH 295 695 1209 HOH HOH A . 
BA 6 HOH 296 696 1210 HOH HOH A . 
BA 6 HOH 297 697 1211 HOH HOH A . 
BA 6 HOH 298 698 1212 HOH HOH A . 
BA 6 HOH 299 699 1213 HOH HOH A . 
BA 6 HOH 300 700 1214 HOH HOH A . 
BA 6 HOH 301 701 1215 HOH HOH A . 
BA 6 HOH 302 702 1216 HOH HOH A . 
BA 6 HOH 303 703 1217 HOH HOH A . 
BA 6 HOH 304 704 1218 HOH HOH A . 
BA 6 HOH 305 705 1219 HOH HOH A . 
BA 6 HOH 306 706 1220 HOH HOH A . 
BA 6 HOH 307 707 1221 HOH HOH A . 
BA 6 HOH 308 708 1222 HOH HOH A . 
BA 6 HOH 309 709 1223 HOH HOH A . 
BA 6 HOH 310 710 1224 HOH HOH A . 
BA 6 HOH 311 711 1225 HOH HOH A . 
BA 6 HOH 312 712 1226 HOH HOH A . 
BA 6 HOH 313 713 1227 HOH HOH A . 
BA 6 HOH 314 714 1228 HOH HOH A . 
BA 6 HOH 315 715 1229 HOH HOH A . 
BA 6 HOH 316 716 1230 HOH HOH A . 
BA 6 HOH 317 717 1231 HOH HOH A . 
BA 6 HOH 318 718 1284 HOH HOH A . 
BA 6 HOH 319 719 1285 HOH HOH A . 
BA 6 HOH 320 720 1286 HOH HOH A . 
BA 6 HOH 321 721 1287 HOH HOH A . 
BA 6 HOH 322 722 1288 HOH HOH A . 
BA 6 HOH 323 723 1289 HOH HOH A . 
BA 6 HOH 324 724 1291 HOH HOH A . 
BA 6 HOH 325 725 1292 HOH HOH A . 
BA 6 HOH 326 726 1293 HOH HOH A . 
BA 6 HOH 327 727 1294 HOH HOH A . 
BA 6 HOH 328 728 1295 HOH HOH A . 
BA 6 HOH 329 729 1296 HOH HOH A . 
BA 6 HOH 330 730 1297 HOH HOH A . 
BA 6 HOH 331 731 1298 HOH HOH A . 
BA 6 HOH 332 732 1299 HOH HOH A . 
BA 6 HOH 333 733 1300 HOH HOH A . 
BA 6 HOH 334 734 1301 HOH HOH A . 
BA 6 HOH 335 735 1302 HOH HOH A . 
BA 6 HOH 336 736 1303 HOH HOH A . 
BA 6 HOH 337 737 1304 HOH HOH A . 
BA 6 HOH 338 738 1305 HOH HOH A . 
BA 6 HOH 339 739 1306 HOH HOH A . 
BA 6 HOH 340 740 1307 HOH HOH A . 
BA 6 HOH 341 741 1308 HOH HOH A . 
BA 6 HOH 342 742 1309 HOH HOH A . 
BA 6 HOH 343 743 1310 HOH HOH A . 
BA 6 HOH 344 744 1311 HOH HOH A . 
BA 6 HOH 345 745 1312 HOH HOH A . 
BA 6 HOH 346 746 1313 HOH HOH A . 
BA 6 HOH 347 747 1314 HOH HOH A . 
BA 6 HOH 348 748 1315 HOH HOH A . 
BA 6 HOH 349 749 1316 HOH HOH A . 
BA 6 HOH 350 750 1317 HOH HOH A . 
BA 6 HOH 351 751 1318 HOH HOH A . 
BA 6 HOH 352 752 1319 HOH HOH A . 
BA 6 HOH 353 753 1320 HOH HOH A . 
BA 6 HOH 354 754 1321 HOH HOH A . 
BA 6 HOH 355 755 1322 HOH HOH A . 
BA 6 HOH 356 756 1323 HOH HOH A . 
BA 6 HOH 357 757 1325 HOH HOH A . 
BA 6 HOH 358 758 1454 HOH HOH A . 
BA 6 HOH 359 759 1460 HOH HOH A . 
BA 6 HOH 360 760 1471 HOH HOH A . 
BA 6 HOH 361 761 1472 HOH HOH A . 
BA 6 HOH 362 762 1473 HOH HOH A . 
BA 6 HOH 363 763 1478 HOH HOH A . 
BA 6 HOH 364 764 1491 HOH HOH A . 
BA 6 HOH 365 765 1493 HOH HOH A . 
BA 6 HOH 366 766 840  HOH HOH A . 
BA 6 HOH 367 767 1489 HOH HOH A . 
BA 6 HOH 368 768 1490 HOH HOH A . 
BA 6 HOH 369 769 192  HOH HOH A . 
CA 6 HOH 1   401 47   HOH HOH B . 
CA 6 HOH 2   402 2    HOH HOH B . 
CA 6 HOH 3   403 8    HOH HOH B . 
CA 6 HOH 4   404 11   HOH HOH B . 
CA 6 HOH 5   405 23   HOH HOH B . 
CA 6 HOH 6   406 29   HOH HOH B . 
CA 6 HOH 7   407 30   HOH HOH B . 
CA 6 HOH 8   408 35   HOH HOH B . 
CA 6 HOH 9   409 36   HOH HOH B . 
CA 6 HOH 10  410 38   HOH HOH B . 
CA 6 HOH 11  411 39   HOH HOH B . 
CA 6 HOH 12  412 41   HOH HOH B . 
CA 6 HOH 13  413 43   HOH HOH B . 
CA 6 HOH 14  414 49   HOH HOH B . 
CA 6 HOH 15  415 51   HOH HOH B . 
CA 6 HOH 16  416 54   HOH HOH B . 
CA 6 HOH 17  417 58   HOH HOH B . 
CA 6 HOH 18  418 67   HOH HOH B . 
CA 6 HOH 19  419 70   HOH HOH B . 
CA 6 HOH 20  420 72   HOH HOH B . 
CA 6 HOH 21  421 73   HOH HOH B . 
CA 6 HOH 22  422 76   HOH HOH B . 
CA 6 HOH 23  423 77   HOH HOH B . 
CA 6 HOH 24  424 79   HOH HOH B . 
CA 6 HOH 25  425 85   HOH HOH B . 
CA 6 HOH 26  426 93   HOH HOH B . 
CA 6 HOH 27  427 98   HOH HOH B . 
CA 6 HOH 28  428 100  HOH HOH B . 
CA 6 HOH 29  429 102  HOH HOH B . 
CA 6 HOH 30  430 104  HOH HOH B . 
CA 6 HOH 31  431 107  HOH HOH B . 
CA 6 HOH 32  432 108  HOH HOH B . 
CA 6 HOH 33  433 109  HOH HOH B . 
CA 6 HOH 34  434 110  HOH HOH B . 
CA 6 HOH 35  435 112  HOH HOH B . 
CA 6 HOH 36  436 115  HOH HOH B . 
CA 6 HOH 37  437 117  HOH HOH B . 
CA 6 HOH 38  438 123  HOH HOH B . 
CA 6 HOH 39  439 126  HOH HOH B . 
CA 6 HOH 40  440 129  HOH HOH B . 
CA 6 HOH 41  441 132  HOH HOH B . 
CA 6 HOH 42  442 133  HOH HOH B . 
CA 6 HOH 43  443 145  HOH HOH B . 
CA 6 HOH 44  444 153  HOH HOH B . 
CA 6 HOH 45  445 155  HOH HOH B . 
CA 6 HOH 46  446 156  HOH HOH B . 
CA 6 HOH 47  447 158  HOH HOH B . 
CA 6 HOH 48  448 163  HOH HOH B . 
CA 6 HOH 49  449 164  HOH HOH B . 
CA 6 HOH 50  450 165  HOH HOH B . 
CA 6 HOH 51  451 166  HOH HOH B . 
CA 6 HOH 52  452 167  HOH HOH B . 
CA 6 HOH 53  453 171  HOH HOH B . 
CA 6 HOH 54  454 175  HOH HOH B . 
CA 6 HOH 55  455 178  HOH HOH B . 
CA 6 HOH 56  456 179  HOH HOH B . 
CA 6 HOH 57  457 181  HOH HOH B . 
CA 6 HOH 58  458 189  HOH HOH B . 
CA 6 HOH 59  459 194  HOH HOH B . 
CA 6 HOH 60  460 200  HOH HOH B . 
CA 6 HOH 61  461 209  HOH HOH B . 
CA 6 HOH 62  462 213  HOH HOH B . 
CA 6 HOH 63  463 216  HOH HOH B . 
CA 6 HOH 64  464 217  HOH HOH B . 
CA 6 HOH 65  465 219  HOH HOH B . 
CA 6 HOH 66  466 222  HOH HOH B . 
CA 6 HOH 67  467 223  HOH HOH B . 
CA 6 HOH 68  468 224  HOH HOH B . 
CA 6 HOH 69  469 225  HOH HOH B . 
CA 6 HOH 70  470 227  HOH HOH B . 
CA 6 HOH 71  471 231  HOH HOH B . 
CA 6 HOH 72  472 234  HOH HOH B . 
CA 6 HOH 73  473 235  HOH HOH B . 
CA 6 HOH 74  474 236  HOH HOH B . 
CA 6 HOH 75  475 239  HOH HOH B . 
CA 6 HOH 76  476 249  HOH HOH B . 
CA 6 HOH 77  477 250  HOH HOH B . 
CA 6 HOH 78  478 251  HOH HOH B . 
CA 6 HOH 79  479 256  HOH HOH B . 
CA 6 HOH 80  480 257  HOH HOH B . 
CA 6 HOH 81  481 259  HOH HOH B . 
CA 6 HOH 82  482 264  HOH HOH B . 
CA 6 HOH 83  483 266  HOH HOH B . 
CA 6 HOH 84  484 270  HOH HOH B . 
CA 6 HOH 85  485 273  HOH HOH B . 
CA 6 HOH 86  486 274  HOH HOH B . 
CA 6 HOH 87  487 275  HOH HOH B . 
CA 6 HOH 88  488 279  HOH HOH B . 
CA 6 HOH 89  489 280  HOH HOH B . 
CA 6 HOH 90  490 282  HOH HOH B . 
CA 6 HOH 91  491 285  HOH HOH B . 
CA 6 HOH 92  492 286  HOH HOH B . 
CA 6 HOH 93  493 287  HOH HOH B . 
CA 6 HOH 94  494 290  HOH HOH B . 
CA 6 HOH 95  495 291  HOH HOH B . 
CA 6 HOH 96  496 299  HOH HOH B . 
CA 6 HOH 97  497 301  HOH HOH B . 
CA 6 HOH 98  498 302  HOH HOH B . 
CA 6 HOH 99  499 303  HOH HOH B . 
CA 6 HOH 100 500 305  HOH HOH B . 
CA 6 HOH 101 501 309  HOH HOH B . 
CA 6 HOH 102 502 311  HOH HOH B . 
CA 6 HOH 103 503 314  HOH HOH B . 
CA 6 HOH 104 504 315  HOH HOH B . 
CA 6 HOH 105 505 316  HOH HOH B . 
CA 6 HOH 106 506 319  HOH HOH B . 
CA 6 HOH 107 507 322  HOH HOH B . 
CA 6 HOH 108 508 323  HOH HOH B . 
CA 6 HOH 109 509 324  HOH HOH B . 
CA 6 HOH 110 510 325  HOH HOH B . 
CA 6 HOH 111 511 327  HOH HOH B . 
CA 6 HOH 112 512 333  HOH HOH B . 
CA 6 HOH 113 513 335  HOH HOH B . 
CA 6 HOH 114 514 336  HOH HOH B . 
CA 6 HOH 115 515 341  HOH HOH B . 
CA 6 HOH 116 516 342  HOH HOH B . 
CA 6 HOH 117 517 343  HOH HOH B . 
CA 6 HOH 118 518 344  HOH HOH B . 
CA 6 HOH 119 519 345  HOH HOH B . 
CA 6 HOH 120 520 346  HOH HOH B . 
CA 6 HOH 121 521 347  HOH HOH B . 
CA 6 HOH 122 522 350  HOH HOH B . 
CA 6 HOH 123 523 353  HOH HOH B . 
CA 6 HOH 124 524 354  HOH HOH B . 
CA 6 HOH 125 525 361  HOH HOH B . 
CA 6 HOH 126 526 363  HOH HOH B . 
CA 6 HOH 127 527 364  HOH HOH B . 
CA 6 HOH 128 528 365  HOH HOH B . 
CA 6 HOH 129 529 367  HOH HOH B . 
CA 6 HOH 130 530 368  HOH HOH B . 
CA 6 HOH 131 531 373  HOH HOH B . 
CA 6 HOH 132 532 375  HOH HOH B . 
CA 6 HOH 133 533 376  HOH HOH B . 
CA 6 HOH 134 534 379  HOH HOH B . 
CA 6 HOH 135 535 381  HOH HOH B . 
CA 6 HOH 136 536 400  HOH HOH B . 
CA 6 HOH 137 537 401  HOH HOH B . 
CA 6 HOH 138 538 402  HOH HOH B . 
CA 6 HOH 139 539 403  HOH HOH B . 
CA 6 HOH 140 540 404  HOH HOH B . 
CA 6 HOH 141 541 405  HOH HOH B . 
CA 6 HOH 142 542 421  HOH HOH B . 
CA 6 HOH 143 543 422  HOH HOH B . 
CA 6 HOH 144 544 426  HOH HOH B . 
CA 6 HOH 145 545 428  HOH HOH B . 
CA 6 HOH 146 546 429  HOH HOH B . 
CA 6 HOH 147 547 430  HOH HOH B . 
CA 6 HOH 148 548 436  HOH HOH B . 
CA 6 HOH 149 549 438  HOH HOH B . 
CA 6 HOH 150 550 439  HOH HOH B . 
CA 6 HOH 151 551 441  HOH HOH B . 
CA 6 HOH 152 552 443  HOH HOH B . 
CA 6 HOH 153 553 445  HOH HOH B . 
CA 6 HOH 154 554 446  HOH HOH B . 
CA 6 HOH 155 555 450  HOH HOH B . 
CA 6 HOH 156 556 453  HOH HOH B . 
CA 6 HOH 157 557 455  HOH HOH B . 
CA 6 HOH 158 558 456  HOH HOH B . 
CA 6 HOH 159 559 457  HOH HOH B . 
CA 6 HOH 160 560 459  HOH HOH B . 
CA 6 HOH 161 561 460  HOH HOH B . 
CA 6 HOH 162 562 465  HOH HOH B . 
CA 6 HOH 163 563 466  HOH HOH B . 
CA 6 HOH 164 564 468  HOH HOH B . 
CA 6 HOH 165 565 471  HOH HOH B . 
CA 6 HOH 166 566 503  HOH HOH B . 
CA 6 HOH 167 567 529  HOH HOH B . 
CA 6 HOH 168 568 534  HOH HOH B . 
CA 6 HOH 169 569 540  HOH HOH B . 
CA 6 HOH 170 570 550  HOH HOH B . 
CA 6 HOH 171 571 567  HOH HOH B . 
CA 6 HOH 172 572 582  HOH HOH B . 
CA 6 HOH 173 573 584  HOH HOH B . 
CA 6 HOH 174 574 603  HOH HOH B . 
CA 6 HOH 175 575 604  HOH HOH B . 
CA 6 HOH 176 576 607  HOH HOH B . 
CA 6 HOH 177 577 618  HOH HOH B . 
CA 6 HOH 178 578 626  HOH HOH B . 
CA 6 HOH 179 579 632  HOH HOH B . 
CA 6 HOH 180 580 643  HOH HOH B . 
CA 6 HOH 181 581 649  HOH HOH B . 
CA 6 HOH 182 582 650  HOH HOH B . 
CA 6 HOH 183 583 651  HOH HOH B . 
CA 6 HOH 184 584 668  HOH HOH B . 
CA 6 HOH 185 585 673  HOH HOH B . 
CA 6 HOH 186 586 674  HOH HOH B . 
CA 6 HOH 187 587 676  HOH HOH B . 
CA 6 HOH 188 588 682  HOH HOH B . 
CA 6 HOH 189 589 687  HOH HOH B . 
CA 6 HOH 190 590 690  HOH HOH B . 
CA 6 HOH 191 591 695  HOH HOH B . 
CA 6 HOH 192 592 707  HOH HOH B . 
CA 6 HOH 193 593 714  HOH HOH B . 
CA 6 HOH 194 594 734  HOH HOH B . 
CA 6 HOH 195 595 737  HOH HOH B . 
CA 6 HOH 196 596 748  HOH HOH B . 
CA 6 HOH 197 597 751  HOH HOH B . 
CA 6 HOH 198 598 752  HOH HOH B . 
CA 6 HOH 199 599 757  HOH HOH B . 
CA 6 HOH 200 600 760  HOH HOH B . 
CA 6 HOH 201 601 768  HOH HOH B . 
CA 6 HOH 202 602 776  HOH HOH B . 
CA 6 HOH 203 603 778  HOH HOH B . 
CA 6 HOH 204 604 779  HOH HOH B . 
CA 6 HOH 205 605 784  HOH HOH B . 
CA 6 HOH 206 606 785  HOH HOH B . 
CA 6 HOH 207 607 786  HOH HOH B . 
CA 6 HOH 208 608 787  HOH HOH B . 
CA 6 HOH 209 609 793  HOH HOH B . 
CA 6 HOH 210 610 795  HOH HOH B . 
CA 6 HOH 211 611 809  HOH HOH B . 
CA 6 HOH 212 612 818  HOH HOH B . 
CA 6 HOH 213 613 819  HOH HOH B . 
CA 6 HOH 214 614 822  HOH HOH B . 
CA 6 HOH 215 615 824  HOH HOH B . 
CA 6 HOH 216 616 825  HOH HOH B . 
CA 6 HOH 217 617 827  HOH HOH B . 
CA 6 HOH 218 618 828  HOH HOH B . 
CA 6 HOH 219 619 830  HOH HOH B . 
CA 6 HOH 220 620 834  HOH HOH B . 
CA 6 HOH 221 621 837  HOH HOH B . 
CA 6 HOH 222 622 839  HOH HOH B . 
CA 6 HOH 223 623 847  HOH HOH B . 
CA 6 HOH 224 624 848  HOH HOH B . 
CA 6 HOH 225 625 849  HOH HOH B . 
CA 6 HOH 226 626 850  HOH HOH B . 
CA 6 HOH 227 627 851  HOH HOH B . 
CA 6 HOH 228 628 852  HOH HOH B . 
CA 6 HOH 229 629 853  HOH HOH B . 
CA 6 HOH 230 630 854  HOH HOH B . 
CA 6 HOH 231 631 855  HOH HOH B . 
CA 6 HOH 232 632 856  HOH HOH B . 
CA 6 HOH 233 633 857  HOH HOH B . 
CA 6 HOH 234 634 858  HOH HOH B . 
CA 6 HOH 235 635 859  HOH HOH B . 
CA 6 HOH 236 636 860  HOH HOH B . 
CA 6 HOH 237 637 861  HOH HOH B . 
CA 6 HOH 238 638 862  HOH HOH B . 
CA 6 HOH 239 639 863  HOH HOH B . 
CA 6 HOH 240 640 876  HOH HOH B . 
CA 6 HOH 241 641 898  HOH HOH B . 
CA 6 HOH 242 642 899  HOH HOH B . 
CA 6 HOH 243 643 912  HOH HOH B . 
CA 6 HOH 244 644 924  HOH HOH B . 
CA 6 HOH 245 645 926  HOH HOH B . 
CA 6 HOH 246 646 927  HOH HOH B . 
CA 6 HOH 247 647 928  HOH HOH B . 
CA 6 HOH 248 648 941  HOH HOH B . 
CA 6 HOH 249 649 942  HOH HOH B . 
CA 6 HOH 250 650 943  HOH HOH B . 
CA 6 HOH 251 651 953  HOH HOH B . 
CA 6 HOH 252 652 954  HOH HOH B . 
CA 6 HOH 253 653 955  HOH HOH B . 
CA 6 HOH 254 654 956  HOH HOH B . 
CA 6 HOH 255 655 959  HOH HOH B . 
CA 6 HOH 256 656 960  HOH HOH B . 
CA 6 HOH 257 657 961  HOH HOH B . 
CA 6 HOH 258 658 962  HOH HOH B . 
CA 6 HOH 259 659 963  HOH HOH B . 
CA 6 HOH 260 660 964  HOH HOH B . 
CA 6 HOH 261 661 1004 HOH HOH B . 
CA 6 HOH 262 662 1005 HOH HOH B . 
CA 6 HOH 263 663 1006 HOH HOH B . 
CA 6 HOH 264 664 1008 HOH HOH B . 
CA 6 HOH 265 665 1009 HOH HOH B . 
CA 6 HOH 266 666 1010 HOH HOH B . 
CA 6 HOH 267 667 1011 HOH HOH B . 
CA 6 HOH 268 668 1013 HOH HOH B . 
CA 6 HOH 269 669 1014 HOH HOH B . 
CA 6 HOH 270 670 1015 HOH HOH B . 
CA 6 HOH 271 671 1016 HOH HOH B . 
CA 6 HOH 272 672 1017 HOH HOH B . 
CA 6 HOH 273 673 1018 HOH HOH B . 
CA 6 HOH 274 674 1019 HOH HOH B . 
CA 6 HOH 275 675 1020 HOH HOH B . 
CA 6 HOH 276 676 1021 HOH HOH B . 
CA 6 HOH 277 677 1022 HOH HOH B . 
CA 6 HOH 278 678 1023 HOH HOH B . 
CA 6 HOH 279 679 1024 HOH HOH B . 
CA 6 HOH 280 680 1025 HOH HOH B . 
CA 6 HOH 281 681 1026 HOH HOH B . 
CA 6 HOH 282 682 1027 HOH HOH B . 
CA 6 HOH 283 683 1028 HOH HOH B . 
CA 6 HOH 284 684 1029 HOH HOH B . 
CA 6 HOH 285 685 1030 HOH HOH B . 
CA 6 HOH 286 686 1031 HOH HOH B . 
CA 6 HOH 287 687 1032 HOH HOH B . 
CA 6 HOH 288 688 1034 HOH HOH B . 
CA 6 HOH 289 689 1035 HOH HOH B . 
CA 6 HOH 290 690 1037 HOH HOH B . 
CA 6 HOH 291 691 1038 HOH HOH B . 
CA 6 HOH 292 692 1039 HOH HOH B . 
CA 6 HOH 293 693 1040 HOH HOH B . 
CA 6 HOH 294 694 1041 HOH HOH B . 
CA 6 HOH 295 695 1042 HOH HOH B . 
CA 6 HOH 296 696 1043 HOH HOH B . 
CA 6 HOH 297 697 1044 HOH HOH B . 
CA 6 HOH 298 698 1045 HOH HOH B . 
CA 6 HOH 299 699 1046 HOH HOH B . 
CA 6 HOH 300 700 1047 HOH HOH B . 
CA 6 HOH 301 701 1048 HOH HOH B . 
CA 6 HOH 302 702 1108 HOH HOH B . 
CA 6 HOH 303 703 1109 HOH HOH B . 
CA 6 HOH 304 704 1162 HOH HOH B . 
CA 6 HOH 305 705 1171 HOH HOH B . 
CA 6 HOH 306 706 1187 HOH HOH B . 
CA 6 HOH 307 707 1188 HOH HOH B . 
CA 6 HOH 308 708 1189 HOH HOH B . 
CA 6 HOH 309 709 1190 HOH HOH B . 
CA 6 HOH 310 710 1232 HOH HOH B . 
CA 6 HOH 311 711 1233 HOH HOH B . 
CA 6 HOH 312 712 1234 HOH HOH B . 
CA 6 HOH 313 713 1235 HOH HOH B . 
CA 6 HOH 314 714 1236 HOH HOH B . 
CA 6 HOH 315 715 1237 HOH HOH B . 
CA 6 HOH 316 716 1238 HOH HOH B . 
CA 6 HOH 317 717 1239 HOH HOH B . 
CA 6 HOH 318 718 1240 HOH HOH B . 
CA 6 HOH 319 719 1241 HOH HOH B . 
CA 6 HOH 320 720 1242 HOH HOH B . 
CA 6 HOH 321 721 1243 HOH HOH B . 
CA 6 HOH 322 722 1290 HOH HOH B . 
CA 6 HOH 323 723 1326 HOH HOH B . 
CA 6 HOH 324 724 1327 HOH HOH B . 
CA 6 HOH 325 725 1328 HOH HOH B . 
CA 6 HOH 326 726 1329 HOH HOH B . 
CA 6 HOH 327 727 1330 HOH HOH B . 
CA 6 HOH 328 728 1331 HOH HOH B . 
CA 6 HOH 329 729 1332 HOH HOH B . 
CA 6 HOH 330 730 1333 HOH HOH B . 
CA 6 HOH 331 731 1334 HOH HOH B . 
CA 6 HOH 332 732 1335 HOH HOH B . 
CA 6 HOH 333 733 1336 HOH HOH B . 
CA 6 HOH 334 734 1337 HOH HOH B . 
CA 6 HOH 335 735 1338 HOH HOH B . 
CA 6 HOH 336 736 1339 HOH HOH B . 
CA 6 HOH 337 737 1340 HOH HOH B . 
CA 6 HOH 338 738 1341 HOH HOH B . 
CA 6 HOH 339 739 1342 HOH HOH B . 
CA 6 HOH 340 740 1343 HOH HOH B . 
CA 6 HOH 341 741 1345 HOH HOH B . 
CA 6 HOH 342 742 1346 HOH HOH B . 
CA 6 HOH 343 743 1350 HOH HOH B . 
CA 6 HOH 344 744 1351 HOH HOH B . 
CA 6 HOH 345 745 1354 HOH HOH B . 
CA 6 HOH 346 746 1355 HOH HOH B . 
CA 6 HOH 347 747 1356 HOH HOH B . 
CA 6 HOH 348 748 1357 HOH HOH B . 
CA 6 HOH 349 749 1358 HOH HOH B . 
CA 6 HOH 350 750 1359 HOH HOH B . 
CA 6 HOH 351 751 1360 HOH HOH B . 
CA 6 HOH 352 752 1364 HOH HOH B . 
CA 6 HOH 353 753 1365 HOH HOH B . 
CA 6 HOH 354 754 1366 HOH HOH B . 
CA 6 HOH 355 755 1367 HOH HOH B . 
CA 6 HOH 356 756 1368 HOH HOH B . 
CA 6 HOH 357 757 1369 HOH HOH B . 
CA 6 HOH 358 758 1370 HOH HOH B . 
CA 6 HOH 359 759 1371 HOH HOH B . 
CA 6 HOH 360 760 1450 HOH HOH B . 
CA 6 HOH 361 761 1451 HOH HOH B . 
CA 6 HOH 362 762 1455 HOH HOH B . 
CA 6 HOH 363 763 1461 HOH HOH B . 
CA 6 HOH 364 764 1462 HOH HOH B . 
CA 6 HOH 365 765 1463 HOH HOH B . 
CA 6 HOH 366 766 1474 HOH HOH B . 
CA 6 HOH 367 767 1483 HOH HOH B . 
CA 6 HOH 368 768 1484 HOH HOH B . 
CA 6 HOH 369 769 1485 HOH HOH B . 
CA 6 HOH 370 770 1486 HOH HOH B . 
CA 6 HOH 371 771 1487 HOH HOH B . 
CA 6 HOH 372 772 1488 HOH HOH B . 
CA 6 HOH 373 773 1494 HOH HOH B . 
CA 6 HOH 374 774 1495 HOH HOH B . 
CA 6 HOH 375 775 1496 HOH HOH B . 
DA 6 HOH 1   401 1353 HOH HOH C . 
DA 6 HOH 2   402 1    HOH HOH C . 
DA 6 HOH 3   403 10   HOH HOH C . 
DA 6 HOH 4   404 14   HOH HOH C . 
DA 6 HOH 5   405 16   HOH HOH C . 
DA 6 HOH 6   406 18   HOH HOH C . 
DA 6 HOH 7   407 22   HOH HOH C . 
DA 6 HOH 8   408 27   HOH HOH C . 
DA 6 HOH 9   409 28   HOH HOH C . 
DA 6 HOH 10  410 33   HOH HOH C . 
DA 6 HOH 11  411 34   HOH HOH C . 
DA 6 HOH 12  412 46   HOH HOH C . 
DA 6 HOH 13  413 55   HOH HOH C . 
DA 6 HOH 14  414 60   HOH HOH C . 
DA 6 HOH 15  415 86   HOH HOH C . 
DA 6 HOH 16  416 90   HOH HOH C . 
DA 6 HOH 17  417 95   HOH HOH C . 
DA 6 HOH 18  418 97   HOH HOH C . 
DA 6 HOH 19  419 113  HOH HOH C . 
DA 6 HOH 20  420 120  HOH HOH C . 
DA 6 HOH 21  421 127  HOH HOH C . 
DA 6 HOH 22  422 131  HOH HOH C . 
DA 6 HOH 23  423 134  HOH HOH C . 
DA 6 HOH 24  424 135  HOH HOH C . 
DA 6 HOH 25  425 182  HOH HOH C . 
DA 6 HOH 26  426 185  HOH HOH C . 
DA 6 HOH 27  427 187  HOH HOH C . 
DA 6 HOH 28  428 197  HOH HOH C . 
DA 6 HOH 29  429 203  HOH HOH C . 
DA 6 HOH 30  430 206  HOH HOH C . 
DA 6 HOH 31  431 212  HOH HOH C . 
DA 6 HOH 32  432 215  HOH HOH C . 
DA 6 HOH 33  433 240  HOH HOH C . 
DA 6 HOH 34  434 242  HOH HOH C . 
DA 6 HOH 35  435 248  HOH HOH C . 
DA 6 HOH 36  436 258  HOH HOH C . 
DA 6 HOH 37  437 260  HOH HOH C . 
DA 6 HOH 38  438 263  HOH HOH C . 
DA 6 HOH 39  439 268  HOH HOH C . 
DA 6 HOH 40  440 278  HOH HOH C . 
DA 6 HOH 41  441 289  HOH HOH C . 
DA 6 HOH 42  442 300  HOH HOH C . 
DA 6 HOH 43  443 317  HOH HOH C . 
DA 6 HOH 44  444 326  HOH HOH C . 
DA 6 HOH 45  445 338  HOH HOH C . 
DA 6 HOH 46  446 352  HOH HOH C . 
DA 6 HOH 47  447 358  HOH HOH C . 
DA 6 HOH 48  448 362  HOH HOH C . 
DA 6 HOH 49  449 369  HOH HOH C . 
DA 6 HOH 50  450 374  HOH HOH C . 
DA 6 HOH 51  451 412  HOH HOH C . 
DA 6 HOH 52  452 420  HOH HOH C . 
DA 6 HOH 53  453 432  HOH HOH C . 
DA 6 HOH 54  454 442  HOH HOH C . 
DA 6 HOH 55  455 473  HOH HOH C . 
DA 6 HOH 56  456 474  HOH HOH C . 
DA 6 HOH 57  457 475  HOH HOH C . 
DA 6 HOH 58  458 476  HOH HOH C . 
DA 6 HOH 59  459 477  HOH HOH C . 
DA 6 HOH 60  460 479  HOH HOH C . 
DA 6 HOH 61  461 480  HOH HOH C . 
DA 6 HOH 62  462 482  HOH HOH C . 
DA 6 HOH 63  463 484  HOH HOH C . 
DA 6 HOH 64  464 485  HOH HOH C . 
DA 6 HOH 65  465 486  HOH HOH C . 
DA 6 HOH 66  466 488  HOH HOH C . 
DA 6 HOH 67  467 489  HOH HOH C . 
DA 6 HOH 68  468 490  HOH HOH C . 
DA 6 HOH 69  469 491  HOH HOH C . 
DA 6 HOH 70  470 492  HOH HOH C . 
DA 6 HOH 71  471 493  HOH HOH C . 
DA 6 HOH 72  472 494  HOH HOH C . 
DA 6 HOH 73  473 497  HOH HOH C . 
DA 6 HOH 74  474 498  HOH HOH C . 
DA 6 HOH 75  475 501  HOH HOH C . 
DA 6 HOH 76  476 505  HOH HOH C . 
DA 6 HOH 77  477 508  HOH HOH C . 
DA 6 HOH 78  478 510  HOH HOH C . 
DA 6 HOH 79  479 512  HOH HOH C . 
DA 6 HOH 80  480 513  HOH HOH C . 
DA 6 HOH 81  481 514  HOH HOH C . 
DA 6 HOH 82  482 515  HOH HOH C . 
DA 6 HOH 83  483 516  HOH HOH C . 
DA 6 HOH 84  484 521  HOH HOH C . 
DA 6 HOH 85  485 523  HOH HOH C . 
DA 6 HOH 86  486 525  HOH HOH C . 
DA 6 HOH 87  487 527  HOH HOH C . 
DA 6 HOH 88  488 530  HOH HOH C . 
DA 6 HOH 89  489 531  HOH HOH C . 
DA 6 HOH 90  490 532  HOH HOH C . 
DA 6 HOH 91  491 535  HOH HOH C . 
DA 6 HOH 92  492 537  HOH HOH C . 
DA 6 HOH 93  493 539  HOH HOH C . 
DA 6 HOH 94  494 541  HOH HOH C . 
DA 6 HOH 95  495 542  HOH HOH C . 
DA 6 HOH 96  496 544  HOH HOH C . 
DA 6 HOH 97  497 546  HOH HOH C . 
DA 6 HOH 98  498 549  HOH HOH C . 
DA 6 HOH 99  499 551  HOH HOH C . 
DA 6 HOH 100 500 552  HOH HOH C . 
DA 6 HOH 101 501 553  HOH HOH C . 
DA 6 HOH 102 502 556  HOH HOH C . 
DA 6 HOH 103 503 559  HOH HOH C . 
DA 6 HOH 104 504 560  HOH HOH C . 
DA 6 HOH 105 505 561  HOH HOH C . 
DA 6 HOH 106 506 562  HOH HOH C . 
DA 6 HOH 107 507 565  HOH HOH C . 
DA 6 HOH 108 508 566  HOH HOH C . 
DA 6 HOH 109 509 570  HOH HOH C . 
DA 6 HOH 110 510 571  HOH HOH C . 
DA 6 HOH 111 511 573  HOH HOH C . 
DA 6 HOH 112 512 576  HOH HOH C . 
DA 6 HOH 113 513 580  HOH HOH C . 
DA 6 HOH 114 514 581  HOH HOH C . 
DA 6 HOH 115 515 585  HOH HOH C . 
DA 6 HOH 116 516 586  HOH HOH C . 
DA 6 HOH 117 517 588  HOH HOH C . 
DA 6 HOH 118 518 589  HOH HOH C . 
DA 6 HOH 119 519 593  HOH HOH C . 
DA 6 HOH 120 520 601  HOH HOH C . 
DA 6 HOH 121 521 602  HOH HOH C . 
DA 6 HOH 122 522 608  HOH HOH C . 
DA 6 HOH 123 523 610  HOH HOH C . 
DA 6 HOH 124 524 611  HOH HOH C . 
DA 6 HOH 125 525 614  HOH HOH C . 
DA 6 HOH 126 526 617  HOH HOH C . 
DA 6 HOH 127 527 628  HOH HOH C . 
DA 6 HOH 128 528 630  HOH HOH C . 
DA 6 HOH 129 529 631  HOH HOH C . 
DA 6 HOH 130 530 633  HOH HOH C . 
DA 6 HOH 131 531 634  HOH HOH C . 
DA 6 HOH 132 532 635  HOH HOH C . 
DA 6 HOH 133 533 637  HOH HOH C . 
DA 6 HOH 134 534 638  HOH HOH C . 
DA 6 HOH 135 535 646  HOH HOH C . 
DA 6 HOH 136 536 654  HOH HOH C . 
DA 6 HOH 137 537 655  HOH HOH C . 
DA 6 HOH 138 538 656  HOH HOH C . 
DA 6 HOH 139 539 657  HOH HOH C . 
DA 6 HOH 140 540 658  HOH HOH C . 
DA 6 HOH 141 541 661  HOH HOH C . 
DA 6 HOH 142 542 678  HOH HOH C . 
DA 6 HOH 143 543 679  HOH HOH C . 
DA 6 HOH 144 544 680  HOH HOH C . 
DA 6 HOH 145 545 681  HOH HOH C . 
DA 6 HOH 146 546 685  HOH HOH C . 
DA 6 HOH 147 547 688  HOH HOH C . 
DA 6 HOH 148 548 689  HOH HOH C . 
DA 6 HOH 149 549 691  HOH HOH C . 
DA 6 HOH 150 550 699  HOH HOH C . 
DA 6 HOH 151 551 703  HOH HOH C . 
DA 6 HOH 152 552 705  HOH HOH C . 
DA 6 HOH 153 553 708  HOH HOH C . 
DA 6 HOH 154 554 709  HOH HOH C . 
DA 6 HOH 155 555 711  HOH HOH C . 
DA 6 HOH 156 556 712  HOH HOH C . 
DA 6 HOH 157 557 724  HOH HOH C . 
DA 6 HOH 158 558 727  HOH HOH C . 
DA 6 HOH 159 559 731  HOH HOH C . 
DA 6 HOH 160 560 732  HOH HOH C . 
DA 6 HOH 161 561 736  HOH HOH C . 
DA 6 HOH 162 562 738  HOH HOH C . 
DA 6 HOH 163 563 743  HOH HOH C . 
DA 6 HOH 164 564 744  HOH HOH C . 
DA 6 HOH 165 565 747  HOH HOH C . 
DA 6 HOH 166 566 749  HOH HOH C . 
DA 6 HOH 167 567 754  HOH HOH C . 
DA 6 HOH 168 568 756  HOH HOH C . 
DA 6 HOH 169 569 758  HOH HOH C . 
DA 6 HOH 170 570 761  HOH HOH C . 
DA 6 HOH 171 571 764  HOH HOH C . 
DA 6 HOH 172 572 765  HOH HOH C . 
DA 6 HOH 173 573 769  HOH HOH C . 
DA 6 HOH 174 574 770  HOH HOH C . 
DA 6 HOH 175 575 771  HOH HOH C . 
DA 6 HOH 176 576 772  HOH HOH C . 
DA 6 HOH 177 577 773  HOH HOH C . 
DA 6 HOH 178 578 775  HOH HOH C . 
DA 6 HOH 179 579 780  HOH HOH C . 
DA 6 HOH 180 580 783  HOH HOH C . 
DA 6 HOH 181 581 789  HOH HOH C . 
DA 6 HOH 182 582 791  HOH HOH C . 
DA 6 HOH 183 583 792  HOH HOH C . 
DA 6 HOH 184 584 794  HOH HOH C . 
DA 6 HOH 185 585 808  HOH HOH C . 
DA 6 HOH 186 586 812  HOH HOH C . 
DA 6 HOH 187 587 813  HOH HOH C . 
DA 6 HOH 188 588 831  HOH HOH C . 
DA 6 HOH 189 589 832  HOH HOH C . 
DA 6 HOH 190 590 835  HOH HOH C . 
DA 6 HOH 191 591 864  HOH HOH C . 
DA 6 HOH 192 592 865  HOH HOH C . 
DA 6 HOH 193 593 866  HOH HOH C . 
DA 6 HOH 194 594 867  HOH HOH C . 
DA 6 HOH 195 595 868  HOH HOH C . 
DA 6 HOH 196 596 869  HOH HOH C . 
DA 6 HOH 197 597 870  HOH HOH C . 
DA 6 HOH 198 598 871  HOH HOH C . 
DA 6 HOH 199 599 872  HOH HOH C . 
DA 6 HOH 200 600 873  HOH HOH C . 
DA 6 HOH 201 601 874  HOH HOH C . 
DA 6 HOH 202 602 875  HOH HOH C . 
DA 6 HOH 203 603 877  HOH HOH C . 
DA 6 HOH 204 604 878  HOH HOH C . 
DA 6 HOH 205 605 879  HOH HOH C . 
DA 6 HOH 206 606 880  HOH HOH C . 
DA 6 HOH 207 607 897  HOH HOH C . 
DA 6 HOH 208 608 900  HOH HOH C . 
DA 6 HOH 209 609 901  HOH HOH C . 
DA 6 HOH 210 610 902  HOH HOH C . 
DA 6 HOH 211 611 903  HOH HOH C . 
DA 6 HOH 212 612 922  HOH HOH C . 
DA 6 HOH 213 613 923  HOH HOH C . 
DA 6 HOH 214 614 932  HOH HOH C . 
DA 6 HOH 215 615 933  HOH HOH C . 
DA 6 HOH 216 616 934  HOH HOH C . 
DA 6 HOH 217 617 935  HOH HOH C . 
DA 6 HOH 218 618 936  HOH HOH C . 
DA 6 HOH 219 619 937  HOH HOH C . 
DA 6 HOH 220 620 938  HOH HOH C . 
DA 6 HOH 221 621 939  HOH HOH C . 
DA 6 HOH 222 622 940  HOH HOH C . 
DA 6 HOH 223 623 948  HOH HOH C . 
DA 6 HOH 224 624 949  HOH HOH C . 
DA 6 HOH 225 625 1007 HOH HOH C . 
DA 6 HOH 226 626 1036 HOH HOH C . 
DA 6 HOH 227 627 1049 HOH HOH C . 
DA 6 HOH 228 628 1050 HOH HOH C . 
DA 6 HOH 229 629 1051 HOH HOH C . 
DA 6 HOH 230 630 1052 HOH HOH C . 
DA 6 HOH 231 631 1053 HOH HOH C . 
DA 6 HOH 232 632 1054 HOH HOH C . 
DA 6 HOH 233 633 1055 HOH HOH C . 
DA 6 HOH 234 634 1056 HOH HOH C . 
DA 6 HOH 235 635 1057 HOH HOH C . 
DA 6 HOH 236 636 1058 HOH HOH C . 
DA 6 HOH 237 637 1059 HOH HOH C . 
DA 6 HOH 238 638 1060 HOH HOH C . 
DA 6 HOH 239 639 1061 HOH HOH C . 
DA 6 HOH 240 640 1062 HOH HOH C . 
DA 6 HOH 241 641 1063 HOH HOH C . 
DA 6 HOH 242 642 1064 HOH HOH C . 
DA 6 HOH 243 643 1065 HOH HOH C . 
DA 6 HOH 244 644 1066 HOH HOH C . 
DA 6 HOH 245 645 1067 HOH HOH C . 
DA 6 HOH 246 646 1068 HOH HOH C . 
DA 6 HOH 247 647 1070 HOH HOH C . 
DA 6 HOH 248 648 1071 HOH HOH C . 
DA 6 HOH 249 649 1072 HOH HOH C . 
DA 6 HOH 250 650 1122 HOH HOH C . 
DA 6 HOH 251 651 1129 HOH HOH C . 
DA 6 HOH 252 652 1130 HOH HOH C . 
DA 6 HOH 253 653 1131 HOH HOH C . 
DA 6 HOH 254 654 1132 HOH HOH C . 
DA 6 HOH 255 655 1133 HOH HOH C . 
DA 6 HOH 256 656 1134 HOH HOH C . 
DA 6 HOH 257 657 1135 HOH HOH C . 
DA 6 HOH 258 658 1136 HOH HOH C . 
DA 6 HOH 259 659 1137 HOH HOH C . 
DA 6 HOH 260 660 1138 HOH HOH C . 
DA 6 HOH 261 661 1145 HOH HOH C . 
DA 6 HOH 262 662 1146 HOH HOH C . 
DA 6 HOH 263 663 1147 HOH HOH C . 
DA 6 HOH 264 664 1148 HOH HOH C . 
DA 6 HOH 265 665 1149 HOH HOH C . 
DA 6 HOH 266 666 1150 HOH HOH C . 
DA 6 HOH 267 667 1151 HOH HOH C . 
DA 6 HOH 268 668 1152 HOH HOH C . 
DA 6 HOH 269 669 1153 HOH HOH C . 
DA 6 HOH 270 670 1154 HOH HOH C . 
DA 6 HOH 271 671 1156 HOH HOH C . 
DA 6 HOH 272 672 1160 HOH HOH C . 
DA 6 HOH 273 673 1172 HOH HOH C . 
DA 6 HOH 274 674 1173 HOH HOH C . 
DA 6 HOH 275 675 1176 HOH HOH C . 
DA 6 HOH 276 676 1177 HOH HOH C . 
DA 6 HOH 277 677 1178 HOH HOH C . 
DA 6 HOH 278 678 1191 HOH HOH C . 
DA 6 HOH 279 679 1244 HOH HOH C . 
DA 6 HOH 280 680 1245 HOH HOH C . 
DA 6 HOH 281 681 1246 HOH HOH C . 
DA 6 HOH 282 682 1247 HOH HOH C . 
DA 6 HOH 283 683 1249 HOH HOH C . 
DA 6 HOH 284 684 1250 HOH HOH C . 
DA 6 HOH 285 685 1251 HOH HOH C . 
DA 6 HOH 286 686 1252 HOH HOH C . 
DA 6 HOH 287 687 1253 HOH HOH C . 
DA 6 HOH 288 688 1254 HOH HOH C . 
DA 6 HOH 289 689 1255 HOH HOH C . 
DA 6 HOH 290 690 1256 HOH HOH C . 
DA 6 HOH 291 691 1257 HOH HOH C . 
DA 6 HOH 292 692 1258 HOH HOH C . 
DA 6 HOH 293 693 1260 HOH HOH C . 
DA 6 HOH 294 694 1261 HOH HOH C . 
DA 6 HOH 295 695 1262 HOH HOH C . 
DA 6 HOH 296 696 1263 HOH HOH C . 
DA 6 HOH 297 697 1264 HOH HOH C . 
DA 6 HOH 298 698 1324 HOH HOH C . 
DA 6 HOH 299 699 1347 HOH HOH C . 
DA 6 HOH 300 700 1348 HOH HOH C . 
DA 6 HOH 301 701 1349 HOH HOH C . 
DA 6 HOH 302 702 1361 HOH HOH C . 
DA 6 HOH 303 703 1362 HOH HOH C . 
DA 6 HOH 304 704 1363 HOH HOH C . 
DA 6 HOH 305 705 1372 HOH HOH C . 
DA 6 HOH 306 706 1373 HOH HOH C . 
DA 6 HOH 307 707 1374 HOH HOH C . 
DA 6 HOH 308 708 1375 HOH HOH C . 
DA 6 HOH 309 709 1376 HOH HOH C . 
DA 6 HOH 310 710 1377 HOH HOH C . 
DA 6 HOH 311 711 1378 HOH HOH C . 
DA 6 HOH 312 712 1379 HOH HOH C . 
DA 6 HOH 313 713 1381 HOH HOH C . 
DA 6 HOH 314 714 1382 HOH HOH C . 
DA 6 HOH 315 715 1383 HOH HOH C . 
DA 6 HOH 316 716 1384 HOH HOH C . 
DA 6 HOH 317 717 1385 HOH HOH C . 
DA 6 HOH 318 718 1386 HOH HOH C . 
DA 6 HOH 319 719 1387 HOH HOH C . 
DA 6 HOH 320 720 1388 HOH HOH C . 
DA 6 HOH 321 721 1389 HOH HOH C . 
DA 6 HOH 322 722 1390 HOH HOH C . 
DA 6 HOH 323 723 1391 HOH HOH C . 
DA 6 HOH 324 724 1392 HOH HOH C . 
DA 6 HOH 325 725 1393 HOH HOH C . 
DA 6 HOH 326 726 1394 HOH HOH C . 
DA 6 HOH 327 727 1395 HOH HOH C . 
DA 6 HOH 328 728 1396 HOH HOH C . 
DA 6 HOH 329 729 1397 HOH HOH C . 
DA 6 HOH 330 730 1398 HOH HOH C . 
DA 6 HOH 331 731 1399 HOH HOH C . 
DA 6 HOH 332 732 1400 HOH HOH C . 
DA 6 HOH 333 733 1401 HOH HOH C . 
DA 6 HOH 334 734 1402 HOH HOH C . 
DA 6 HOH 335 735 1408 HOH HOH C . 
DA 6 HOH 336 736 1409 HOH HOH C . 
DA 6 HOH 337 737 1410 HOH HOH C . 
DA 6 HOH 338 738 1411 HOH HOH C . 
DA 6 HOH 339 739 1412 HOH HOH C . 
DA 6 HOH 340 740 1413 HOH HOH C . 
DA 6 HOH 341 741 1415 HOH HOH C . 
DA 6 HOH 342 742 1416 HOH HOH C . 
DA 6 HOH 343 743 1418 HOH HOH C . 
DA 6 HOH 344 744 1456 HOH HOH C . 
DA 6 HOH 345 745 1464 HOH HOH C . 
DA 6 HOH 346 746 1465 HOH HOH C . 
DA 6 HOH 347 747 1475 HOH HOH C . 
DA 6 HOH 348 748 1476 HOH HOH C . 
DA 6 HOH 349 749 1477 HOH HOH C . 
DA 6 HOH 350 750 1492 HOH HOH C . 
EA 6 HOH 1   401 921  HOH HOH D . 
EA 6 HOH 2   402 1352 HOH HOH D . 
EA 6 HOH 3   403 1414 HOH HOH D . 
EA 6 HOH 4   404 4    HOH HOH D . 
EA 6 HOH 5   405 5    HOH HOH D . 
EA 6 HOH 6   406 6    HOH HOH D . 
EA 6 HOH 7   407 7    HOH HOH D . 
EA 6 HOH 8   408 15   HOH HOH D . 
EA 6 HOH 9   409 17   HOH HOH D . 
EA 6 HOH 10  410 20   HOH HOH D . 
EA 6 HOH 11  411 21   HOH HOH D . 
EA 6 HOH 12  412 25   HOH HOH D . 
EA 6 HOH 13  413 32   HOH HOH D . 
EA 6 HOH 14  414 37   HOH HOH D . 
EA 6 HOH 15  415 42   HOH HOH D . 
EA 6 HOH 16  416 44   HOH HOH D . 
EA 6 HOH 17  417 45   HOH HOH D . 
EA 6 HOH 18  418 48   HOH HOH D . 
EA 6 HOH 19  419 52   HOH HOH D . 
EA 6 HOH 20  420 61   HOH HOH D . 
EA 6 HOH 21  421 63   HOH HOH D . 
EA 6 HOH 22  422 64   HOH HOH D . 
EA 6 HOH 23  423 66   HOH HOH D . 
EA 6 HOH 24  424 68   HOH HOH D . 
EA 6 HOH 25  425 69   HOH HOH D . 
EA 6 HOH 26  426 71   HOH HOH D . 
EA 6 HOH 27  427 75   HOH HOH D . 
EA 6 HOH 28  428 78   HOH HOH D . 
EA 6 HOH 29  429 80   HOH HOH D . 
EA 6 HOH 30  430 81   HOH HOH D . 
EA 6 HOH 31  431 82   HOH HOH D . 
EA 6 HOH 32  432 84   HOH HOH D . 
EA 6 HOH 33  433 87   HOH HOH D . 
EA 6 HOH 34  434 88   HOH HOH D . 
EA 6 HOH 35  435 91   HOH HOH D . 
EA 6 HOH 36  436 94   HOH HOH D . 
EA 6 HOH 37  437 96   HOH HOH D . 
EA 6 HOH 38  438 99   HOH HOH D . 
EA 6 HOH 39  439 101  HOH HOH D . 
EA 6 HOH 40  440 105  HOH HOH D . 
EA 6 HOH 41  441 111  HOH HOH D . 
EA 6 HOH 42  442 114  HOH HOH D . 
EA 6 HOH 43  443 116  HOH HOH D . 
EA 6 HOH 44  444 118  HOH HOH D . 
EA 6 HOH 45  445 119  HOH HOH D . 
EA 6 HOH 46  446 121  HOH HOH D . 
EA 6 HOH 47  447 122  HOH HOH D . 
EA 6 HOH 48  448 124  HOH HOH D . 
EA 6 HOH 49  449 125  HOH HOH D . 
EA 6 HOH 50  450 128  HOH HOH D . 
EA 6 HOH 51  451 130  HOH HOH D . 
EA 6 HOH 52  452 136  HOH HOH D . 
EA 6 HOH 53  453 137  HOH HOH D . 
EA 6 HOH 54  454 139  HOH HOH D . 
EA 6 HOH 55  455 140  HOH HOH D . 
EA 6 HOH 56  456 141  HOH HOH D . 
EA 6 HOH 57  457 142  HOH HOH D . 
EA 6 HOH 58  458 143  HOH HOH D . 
EA 6 HOH 59  459 144  HOH HOH D . 
EA 6 HOH 60  460 146  HOH HOH D . 
EA 6 HOH 61  461 148  HOH HOH D . 
EA 6 HOH 62  462 149  HOH HOH D . 
EA 6 HOH 63  463 150  HOH HOH D . 
EA 6 HOH 64  464 151  HOH HOH D . 
EA 6 HOH 65  465 152  HOH HOH D . 
EA 6 HOH 66  466 154  HOH HOH D . 
EA 6 HOH 67  467 159  HOH HOH D . 
EA 6 HOH 68  468 160  HOH HOH D . 
EA 6 HOH 69  469 161  HOH HOH D . 
EA 6 HOH 70  470 168  HOH HOH D . 
EA 6 HOH 71  471 169  HOH HOH D . 
EA 6 HOH 72  472 170  HOH HOH D . 
EA 6 HOH 73  473 173  HOH HOH D . 
EA 6 HOH 74  474 174  HOH HOH D . 
EA 6 HOH 75  475 177  HOH HOH D . 
EA 6 HOH 76  476 184  HOH HOH D . 
EA 6 HOH 77  477 186  HOH HOH D . 
EA 6 HOH 78  478 188  HOH HOH D . 
EA 6 HOH 79  479 190  HOH HOH D . 
EA 6 HOH 80  480 191  HOH HOH D . 
EA 6 HOH 81  481 193  HOH HOH D . 
EA 6 HOH 82  482 195  HOH HOH D . 
EA 6 HOH 83  483 196  HOH HOH D . 
EA 6 HOH 84  484 201  HOH HOH D . 
EA 6 HOH 85  485 202  HOH HOH D . 
EA 6 HOH 86  486 204  HOH HOH D . 
EA 6 HOH 87  487 205  HOH HOH D . 
EA 6 HOH 88  488 210  HOH HOH D . 
EA 6 HOH 89  489 214  HOH HOH D . 
EA 6 HOH 90  490 220  HOH HOH D . 
EA 6 HOH 91  491 221  HOH HOH D . 
EA 6 HOH 92  492 226  HOH HOH D . 
EA 6 HOH 93  493 228  HOH HOH D . 
EA 6 HOH 94  494 229  HOH HOH D . 
EA 6 HOH 95  495 232  HOH HOH D . 
EA 6 HOH 96  496 233  HOH HOH D . 
EA 6 HOH 97  497 237  HOH HOH D . 
EA 6 HOH 98  498 238  HOH HOH D . 
EA 6 HOH 99  499 241  HOH HOH D . 
EA 6 HOH 100 500 245  HOH HOH D . 
EA 6 HOH 101 501 246  HOH HOH D . 
EA 6 HOH 102 502 247  HOH HOH D . 
EA 6 HOH 103 503 254  HOH HOH D . 
EA 6 HOH 104 504 255  HOH HOH D . 
EA 6 HOH 105 505 261  HOH HOH D . 
EA 6 HOH 106 506 262  HOH HOH D . 
EA 6 HOH 107 507 265  HOH HOH D . 
EA 6 HOH 108 508 267  HOH HOH D . 
EA 6 HOH 109 509 269  HOH HOH D . 
EA 6 HOH 110 510 271  HOH HOH D . 
EA 6 HOH 111 511 276  HOH HOH D . 
EA 6 HOH 112 512 277  HOH HOH D . 
EA 6 HOH 113 513 281  HOH HOH D . 
EA 6 HOH 114 514 283  HOH HOH D . 
EA 6 HOH 115 515 288  HOH HOH D . 
EA 6 HOH 116 516 292  HOH HOH D . 
EA 6 HOH 117 517 293  HOH HOH D . 
EA 6 HOH 118 518 294  HOH HOH D . 
EA 6 HOH 119 519 295  HOH HOH D . 
EA 6 HOH 120 520 297  HOH HOH D . 
EA 6 HOH 121 521 298  HOH HOH D . 
EA 6 HOH 122 522 304  HOH HOH D . 
EA 6 HOH 123 523 307  HOH HOH D . 
EA 6 HOH 124 524 308  HOH HOH D . 
EA 6 HOH 125 525 310  HOH HOH D . 
EA 6 HOH 126 526 312  HOH HOH D . 
EA 6 HOH 127 527 313  HOH HOH D . 
EA 6 HOH 128 528 318  HOH HOH D . 
EA 6 HOH 129 529 320  HOH HOH D . 
EA 6 HOH 130 530 321  HOH HOH D . 
EA 6 HOH 131 531 328  HOH HOH D . 
EA 6 HOH 132 532 329  HOH HOH D . 
EA 6 HOH 133 533 330  HOH HOH D . 
EA 6 HOH 134 534 331  HOH HOH D . 
EA 6 HOH 135 535 332  HOH HOH D . 
EA 6 HOH 136 536 334  HOH HOH D . 
EA 6 HOH 137 537 337  HOH HOH D . 
EA 6 HOH 138 538 339  HOH HOH D . 
EA 6 HOH 139 539 355  HOH HOH D . 
EA 6 HOH 140 540 356  HOH HOH D . 
EA 6 HOH 141 541 357  HOH HOH D . 
EA 6 HOH 142 542 359  HOH HOH D . 
EA 6 HOH 143 543 360  HOH HOH D . 
EA 6 HOH 144 544 366  HOH HOH D . 
EA 6 HOH 145 545 370  HOH HOH D . 
EA 6 HOH 146 546 371  HOH HOH D . 
EA 6 HOH 147 547 377  HOH HOH D . 
EA 6 HOH 148 548 380  HOH HOH D . 
EA 6 HOH 149 549 382  HOH HOH D . 
EA 6 HOH 150 550 398  HOH HOH D . 
EA 6 HOH 151 551 399  HOH HOH D . 
EA 6 HOH 152 552 406  HOH HOH D . 
EA 6 HOH 153 553 407  HOH HOH D . 
EA 6 HOH 154 554 409  HOH HOH D . 
EA 6 HOH 155 555 410  HOH HOH D . 
EA 6 HOH 156 556 411  HOH HOH D . 
EA 6 HOH 157 557 413  HOH HOH D . 
EA 6 HOH 158 558 414  HOH HOH D . 
EA 6 HOH 159 559 415  HOH HOH D . 
EA 6 HOH 160 560 419  HOH HOH D . 
EA 6 HOH 161 561 423  HOH HOH D . 
EA 6 HOH 162 562 425  HOH HOH D . 
EA 6 HOH 163 563 427  HOH HOH D . 
EA 6 HOH 164 564 431  HOH HOH D . 
EA 6 HOH 165 565 433  HOH HOH D . 
EA 6 HOH 166 566 434  HOH HOH D . 
EA 6 HOH 167 567 435  HOH HOH D . 
EA 6 HOH 168 568 437  HOH HOH D . 
EA 6 HOH 169 569 444  HOH HOH D . 
EA 6 HOH 170 570 447  HOH HOH D . 
EA 6 HOH 171 571 448  HOH HOH D . 
EA 6 HOH 172 572 449  HOH HOH D . 
EA 6 HOH 173 573 452  HOH HOH D . 
EA 6 HOH 174 574 454  HOH HOH D . 
EA 6 HOH 175 575 575  HOH HOH D . 
EA 6 HOH 176 576 461  HOH HOH D . 
EA 6 HOH 177 577 462  HOH HOH D . 
EA 6 HOH 178 578 463  HOH HOH D . 
EA 6 HOH 179 579 464  HOH HOH D . 
EA 6 HOH 180 580 467  HOH HOH D . 
EA 6 HOH 181 581 469  HOH HOH D . 
EA 6 HOH 182 582 470  HOH HOH D . 
EA 6 HOH 183 583 472  HOH HOH D . 
EA 6 HOH 184 584 568  HOH HOH D . 
EA 6 HOH 185 585 574  HOH HOH D . 
EA 6 HOH 186 586 577  HOH HOH D . 
EA 6 HOH 187 587 578  HOH HOH D . 
EA 6 HOH 188 588 590  HOH HOH D . 
EA 6 HOH 189 589 591  HOH HOH D . 
EA 6 HOH 190 590 592  HOH HOH D . 
EA 6 HOH 191 591 596  HOH HOH D . 
EA 6 HOH 192 592 599  HOH HOH D . 
EA 6 HOH 193 593 605  HOH HOH D . 
EA 6 HOH 194 594 609  HOH HOH D . 
EA 6 HOH 195 595 612  HOH HOH D . 
EA 6 HOH 196 596 613  HOH HOH D . 
EA 6 HOH 197 597 620  HOH HOH D . 
EA 6 HOH 198 598 622  HOH HOH D . 
EA 6 HOH 199 599 627  HOH HOH D . 
EA 6 HOH 200 600 636  HOH HOH D . 
EA 6 HOH 201 601 639  HOH HOH D . 
EA 6 HOH 202 602 645  HOH HOH D . 
EA 6 HOH 203 603 659  HOH HOH D . 
EA 6 HOH 204 604 663  HOH HOH D . 
EA 6 HOH 205 605 665  HOH HOH D . 
EA 6 HOH 206 606 667  HOH HOH D . 
EA 6 HOH 207 607 684  HOH HOH D . 
EA 6 HOH 208 608 686  HOH HOH D . 
EA 6 HOH 209 609 692  HOH HOH D . 
EA 6 HOH 210 610 697  HOH HOH D . 
EA 6 HOH 211 611 698  HOH HOH D . 
EA 6 HOH 212 612 704  HOH HOH D . 
EA 6 HOH 213 613 713  HOH HOH D . 
EA 6 HOH 214 614 715  HOH HOH D . 
EA 6 HOH 215 615 717  HOH HOH D . 
EA 6 HOH 216 616 718  HOH HOH D . 
EA 6 HOH 217 617 719  HOH HOH D . 
EA 6 HOH 218 618 720  HOH HOH D . 
EA 6 HOH 219 619 729  HOH HOH D . 
EA 6 HOH 220 620 735  HOH HOH D . 
EA 6 HOH 221 621 739  HOH HOH D . 
EA 6 HOH 222 622 750  HOH HOH D . 
EA 6 HOH 223 623 759  HOH HOH D . 
EA 6 HOH 224 624 762  HOH HOH D . 
EA 6 HOH 225 625 763  HOH HOH D . 
EA 6 HOH 226 626 767  HOH HOH D . 
EA 6 HOH 227 627 774  HOH HOH D . 
EA 6 HOH 228 628 777  HOH HOH D . 
EA 6 HOH 229 629 781  HOH HOH D . 
EA 6 HOH 230 630 790  HOH HOH D . 
EA 6 HOH 231 631 796  HOH HOH D . 
EA 6 HOH 232 632 799  HOH HOH D . 
EA 6 HOH 233 633 802  HOH HOH D . 
EA 6 HOH 234 634 805  HOH HOH D . 
EA 6 HOH 235 635 806  HOH HOH D . 
EA 6 HOH 236 636 810  HOH HOH D . 
EA 6 HOH 237 637 811  HOH HOH D . 
EA 6 HOH 238 638 815  HOH HOH D . 
EA 6 HOH 239 639 816  HOH HOH D . 
EA 6 HOH 240 640 817  HOH HOH D . 
EA 6 HOH 241 641 820  HOH HOH D . 
EA 6 HOH 242 642 823  HOH HOH D . 
EA 6 HOH 243 643 829  HOH HOH D . 
EA 6 HOH 244 644 833  HOH HOH D . 
EA 6 HOH 245 645 838  HOH HOH D . 
EA 6 HOH 246 646 881  HOH HOH D . 
EA 6 HOH 247 647 882  HOH HOH D . 
EA 6 HOH 248 648 883  HOH HOH D . 
EA 6 HOH 249 649 884  HOH HOH D . 
EA 6 HOH 250 650 885  HOH HOH D . 
EA 6 HOH 251 651 886  HOH HOH D . 
EA 6 HOH 252 652 887  HOH HOH D . 
EA 6 HOH 253 653 888  HOH HOH D . 
EA 6 HOH 254 654 889  HOH HOH D . 
EA 6 HOH 255 655 890  HOH HOH D . 
EA 6 HOH 256 656 891  HOH HOH D . 
EA 6 HOH 257 657 892  HOH HOH D . 
EA 6 HOH 258 658 893  HOH HOH D . 
EA 6 HOH 259 659 894  HOH HOH D . 
EA 6 HOH 260 660 895  HOH HOH D . 
EA 6 HOH 261 661 896  HOH HOH D . 
EA 6 HOH 262 662 904  HOH HOH D . 
EA 6 HOH 263 663 905  HOH HOH D . 
EA 6 HOH 264 664 906  HOH HOH D . 
EA 6 HOH 265 665 907  HOH HOH D . 
EA 6 HOH 266 666 914  HOH HOH D . 
EA 6 HOH 267 667 915  HOH HOH D . 
EA 6 HOH 268 668 916  HOH HOH D . 
EA 6 HOH 269 669 917  HOH HOH D . 
EA 6 HOH 270 670 918  HOH HOH D . 
EA 6 HOH 271 671 919  HOH HOH D . 
EA 6 HOH 272 672 925  HOH HOH D . 
EA 6 HOH 273 673 1033 HOH HOH D . 
EA 6 HOH 274 674 1069 HOH HOH D . 
EA 6 HOH 275 675 1073 HOH HOH D . 
EA 6 HOH 276 676 1074 HOH HOH D . 
EA 6 HOH 277 677 1075 HOH HOH D . 
EA 6 HOH 278 678 1076 HOH HOH D . 
EA 6 HOH 279 679 1077 HOH HOH D . 
EA 6 HOH 280 680 1078 HOH HOH D . 
EA 6 HOH 281 681 1079 HOH HOH D . 
EA 6 HOH 282 682 1080 HOH HOH D . 
EA 6 HOH 283 683 1081 HOH HOH D . 
EA 6 HOH 284 684 1082 HOH HOH D . 
EA 6 HOH 285 685 1083 HOH HOH D . 
EA 6 HOH 286 686 1084 HOH HOH D . 
EA 6 HOH 287 687 1085 HOH HOH D . 
EA 6 HOH 288 688 1086 HOH HOH D . 
EA 6 HOH 289 689 1087 HOH HOH D . 
EA 6 HOH 290 690 1088 HOH HOH D . 
EA 6 HOH 291 691 1089 HOH HOH D . 
EA 6 HOH 292 692 1090 HOH HOH D . 
EA 6 HOH 293 693 1091 HOH HOH D . 
EA 6 HOH 294 694 1092 HOH HOH D . 
EA 6 HOH 295 695 1093 HOH HOH D . 
EA 6 HOH 296 696 1094 HOH HOH D . 
EA 6 HOH 297 697 1095 HOH HOH D . 
EA 6 HOH 298 698 1096 HOH HOH D . 
EA 6 HOH 299 699 1097 HOH HOH D . 
EA 6 HOH 300 700 1098 HOH HOH D . 
EA 6 HOH 301 701 1099 HOH HOH D . 
EA 6 HOH 302 702 1100 HOH HOH D . 
EA 6 HOH 303 703 1101 HOH HOH D . 
EA 6 HOH 304 704 1102 HOH HOH D . 
EA 6 HOH 305 705 1103 HOH HOH D . 
EA 6 HOH 306 706 1104 HOH HOH D . 
EA 6 HOH 307 707 1105 HOH HOH D . 
EA 6 HOH 308 708 708  HOH HOH D . 
EA 6 HOH 309 709 1118 HOH HOH D . 
EA 6 HOH 310 710 1119 HOH HOH D . 
EA 6 HOH 311 711 1120 HOH HOH D . 
EA 6 HOH 312 712 1121 HOH HOH D . 
EA 6 HOH 313 713 1125 HOH HOH D . 
EA 6 HOH 314 714 1159 HOH HOH D . 
EA 6 HOH 315 715 1161 HOH HOH D . 
EA 6 HOH 316 716 1164 HOH HOH D . 
EA 6 HOH 317 717 1165 HOH HOH D . 
EA 6 HOH 318 718 1166 HOH HOH D . 
EA 6 HOH 319 719 1167 HOH HOH D . 
EA 6 HOH 320 720 1168 HOH HOH D . 
EA 6 HOH 321 721 1169 HOH HOH D . 
EA 6 HOH 322 722 1179 HOH HOH D . 
EA 6 HOH 323 723 1181 HOH HOH D . 
EA 6 HOH 324 724 1182 HOH HOH D . 
EA 6 HOH 325 725 1183 HOH HOH D . 
EA 6 HOH 326 726 1184 HOH HOH D . 
EA 6 HOH 327 727 1185 HOH HOH D . 
EA 6 HOH 328 728 1186 HOH HOH D . 
EA 6 HOH 329 729 1248 HOH HOH D . 
EA 6 HOH 330 730 1259 HOH HOH D . 
EA 6 HOH 331 731 1265 HOH HOH D . 
EA 6 HOH 332 732 1266 HOH HOH D . 
EA 6 HOH 333 733 1267 HOH HOH D . 
EA 6 HOH 334 734 1268 HOH HOH D . 
EA 6 HOH 335 735 1269 HOH HOH D . 
EA 6 HOH 336 736 1270 HOH HOH D . 
EA 6 HOH 337 737 1271 HOH HOH D . 
EA 6 HOH 338 738 1272 HOH HOH D . 
EA 6 HOH 339 739 1273 HOH HOH D . 
EA 6 HOH 340 740 1274 HOH HOH D . 
EA 6 HOH 341 741 1275 HOH HOH D . 
EA 6 HOH 342 742 1276 HOH HOH D . 
EA 6 HOH 343 743 1277 HOH HOH D . 
EA 6 HOH 344 744 1278 HOH HOH D . 
EA 6 HOH 345 745 1279 HOH HOH D . 
EA 6 HOH 346 746 1280 HOH HOH D . 
EA 6 HOH 347 747 1281 HOH HOH D . 
EA 6 HOH 348 748 1282 HOH HOH D . 
EA 6 HOH 349 749 1283 HOH HOH D . 
EA 6 HOH 350 750 1344 HOH HOH D . 
EA 6 HOH 351 751 1380 HOH HOH D . 
EA 6 HOH 352 752 1403 HOH HOH D . 
EA 6 HOH 353 753 1404 HOH HOH D . 
EA 6 HOH 354 754 1405 HOH HOH D . 
EA 6 HOH 355 755 1406 HOH HOH D . 
EA 6 HOH 356 756 1407 HOH HOH D . 
EA 6 HOH 357 757 1417 HOH HOH D . 
EA 6 HOH 358 758 1419 HOH HOH D . 
EA 6 HOH 359 759 1420 HOH HOH D . 
EA 6 HOH 360 760 1421 HOH HOH D . 
EA 6 HOH 361 761 1422 HOH HOH D . 
EA 6 HOH 362 762 1423 HOH HOH D . 
EA 6 HOH 363 763 1424 HOH HOH D . 
EA 6 HOH 364 764 1425 HOH HOH D . 
EA 6 HOH 365 765 1426 HOH HOH D . 
EA 6 HOH 366 766 1427 HOH HOH D . 
EA 6 HOH 367 767 1428 HOH HOH D . 
EA 6 HOH 368 768 1429 HOH HOH D . 
EA 6 HOH 369 769 1430 HOH HOH D . 
EA 6 HOH 370 770 1431 HOH HOH D . 
EA 6 HOH 371 771 1432 HOH HOH D . 
EA 6 HOH 372 772 1433 HOH HOH D . 
EA 6 HOH 373 773 1434 HOH HOH D . 
EA 6 HOH 374 774 1435 HOH HOH D . 
EA 6 HOH 375 775 1436 HOH HOH D . 
EA 6 HOH 376 776 1437 HOH HOH D . 
EA 6 HOH 377 777 1438 HOH HOH D . 
EA 6 HOH 378 778 1439 HOH HOH D . 
EA 6 HOH 379 779 1440 HOH HOH D . 
EA 6 HOH 380 780 1441 HOH HOH D . 
EA 6 HOH 381 781 1442 HOH HOH D . 
EA 6 HOH 382 782 1443 HOH HOH D . 
EA 6 HOH 383 783 1444 HOH HOH D . 
EA 6 HOH 384 784 1445 HOH HOH D . 
EA 6 HOH 385 785 1446 HOH HOH D . 
EA 6 HOH 386 786 1447 HOH HOH D . 
EA 6 HOH 387 787 1448 HOH HOH D . 
EA 6 HOH 388 788 1449 HOH HOH D . 
EA 6 HOH 389 789 1452 HOH HOH D . 
EA 6 HOH 390 790 1453 HOH HOH D . 
EA 6 HOH 391 791 1457 HOH HOH D . 
EA 6 HOH 392 792 1458 HOH HOH D . 
EA 6 HOH 393 793 1459 HOH HOH D . 
EA 6 HOH 394 794 1466 HOH HOH D . 
EA 6 HOH 395 795 1467 HOH HOH D . 
EA 6 HOH 396 796 1468 HOH HOH D . 
EA 6 HOH 397 797 1469 HOH HOH D . 
EA 6 HOH 398 798 1470 HOH HOH D . 
EA 6 HOH 399 799 1479 HOH HOH D . 
EA 6 HOH 400 800 1480 HOH HOH D . 
EA 6 HOH 401 801 1481 HOH HOH D . 
EA 6 HOH 402 802 1482 HOH HOH D . 
EA 6 HOH 403 803 1497 HOH HOH D . 
EA 6 HOH 404 804 1498 HOH HOH D . 
EA 6 HOH 405 805 1499 HOH HOH D . 
EA 6 HOH 406 806 1500 HOH HOH D . 
EA 6 HOH 407 807 1501 HOH HOH D . 
EA 6 HOH 408 808 1502 HOH HOH D . 
EA 6 HOH 409 809 1503 HOH HOH D . 
EA 6 HOH 410 810 1504 HOH HOH D . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
3 author_and_software_defined_assembly PISA monomeric 1 
4 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,F,G,H,I,J,BA     
2 1 B,K,L,M,N,O,P,Q,R,CA 
3 1 C,S,T,U,DA           
4 1 D,V,W,X,Y,Z,AA,EA    
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 101.2 ? 
2  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 113.5 ? 
3  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 101.1 ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N23 C F V50 .   ? A V50 302 ? 1_555 112.5 ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N23 C F V50 .   ? A V50 302 ? 1_555 110.1 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N23 C F V50 .   ? A V50 302 ? 1_555 116.6 ? 
7  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N23 B F V50 .   ? A V50 302 ? 1_555 112.7 ? 
8  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N23 B F V50 .   ? A V50 302 ? 1_555 116.3 ? 
9  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N23 B F V50 .   ? A V50 302 ? 1_555 111.3 ? 
10 N23 C F V50 .   ? A V50 302 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N23 B F V50 .   ? A V50 302 ? 1_555 6.8   ? 
11 NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  C F V50 .   ? A V50 302 ? 1_555 96.9  ? 
12 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  C F V50 .   ? A V50 302 ? 1_555 140.5 ? 
13 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  C F V50 .   ? A V50 302 ? 1_555 103.3 ? 
14 N23 C F V50 .   ? A V50 302 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  C F V50 .   ? A V50 302 ? 1_555 30.5  ? 
15 N23 B F V50 .   ? A V50 302 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S7  C F V50 .   ? A V50 302 ? 1_555 24.8  ? 
16 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 104.1 ? 
17 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 111.1 ? 
18 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 97.8  ? 
19 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 N23 ? L V50 .   ? B V50 302 ? 1_555 113.1 ? 
20 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 N23 ? L V50 .   ? B V50 302 ? 1_555 113.5 ? 
21 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? K ZN . ? B ZN 301 ? 1_555 N23 ? L V50 .   ? B V50 302 ? 1_555 115.6 ? 
22 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? S ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 104.2 ? 
23 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? S ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 111.1 ? 
24 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? S ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 100.7 ? 
25 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? S ZN . ? C ZN 301 ? 1_555 N23 ? T V50 .   ? C V50 302 ? 1_555 110.1 ? 
26 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? S ZN . ? C ZN 301 ? 1_555 N23 ? T V50 .   ? C V50 302 ? 1_555 113.7 ? 
27 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? S ZN . ? C ZN 301 ? 1_555 N23 ? T V50 .   ? C V50 302 ? 1_555 116.2 ? 
28 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 102.3 ? 
29 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 111.0 ? 
30 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 99.2  ? 
31 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 N23 ? W V50 .   ? D V50 302 ? 1_555 109.3 ? 
32 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 N23 ? W V50 .   ? D V50 302 ? 1_555 113.5 ? 
33 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 N23 ? W V50 .   ? D V50 302 ? 1_555 119.9 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2013-04-10 
2 'Structure model' 1 1 2023-09-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' diffrn_source                 
5 2 'Structure model' pdbx_initial_refinement_model 
6 2 'Structure model' pdbx_struct_conn_angle        
7 2 'Structure model' struct_conn                   
8 2 'Structure model' struct_ref_seq_dif            
9 2 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_database_2.pdbx_DOI'                        
2  2 'Structure model' '_database_2.pdbx_database_accession'         
3  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_asym_id'  
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_alt_id'  
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_asym_id'  
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_asym_id'  
15 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
16 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
17 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_alt_id'  
18 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
19 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
20 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
21 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
22 2 'Structure model' '_pdbx_struct_conn_angle.value'               
23 2 'Structure model' '_struct_conn.pdbx_dist_value'                
24 2 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
25 2 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
26 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
27 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
28 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
29 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
30 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
31 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
32 2 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
33 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
34 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
35 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
36 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
37 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
38 2 'Structure model' '_struct_ref_seq_dif.details'                 
39 2 'Structure model' '_struct_site.pdbx_auth_asym_id'              
40 2 'Structure model' '_struct_site.pdbx_auth_comp_id'              
41 2 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.3.16 2010/01/06      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
DNA         .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 D ASN 134 ? A O D HOH 779 ? ? 1.78 
2 1 O   B ASP 253 ? B O B HOH 653 ? ? 1.82 
3 1 OD1 B ASP 253 ? B O B HOH 704 ? ? 1.84 
4 1 NH2 A ARG 255 ? B O A HOH 468 ? ? 1.88 
5 1 N   D LYS 3   ? B O D HOH 600 ? ? 2.03 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB B ASP 235 ? B CG B ASP 235 ? B OD2 B ASP 235 ? B 123.91 118.30 5.61  0.90 N 
2 1 NE C ARG 255 ? B CZ C ARG 255 ? B NH1 C ARG 255 ? B 125.10 120.30 4.80  0.50 N 
3 1 NE C ARG 255 ? B CZ C ARG 255 ? B NH2 C ARG 255 ? B 116.94 120.30 -3.36 0.50 N 
4 1 CA D LEU 256 ? B CB D LEU 256 ? B CG  D LEU 256 ? B 132.08 115.30 16.78 2.30 N 
5 1 CB D LEU 256 ? B CG D LEU 256 ? B CD2 D LEU 256 ? B 127.85 111.00 16.85 1.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 99  ? ? -155.56 83.88   
2  1 GLU A 137 ? ? 49.65   16.80   
3  1 ASP A 235 ? ? 74.53   -3.50   
4  1 ASN A 245 ? ? -96.57  59.43   
5  1 ASN B 245 ? ? -91.68  56.74   
6  1 ASP B 253 ? B -98.03  -94.15  
7  1 GLU B 254 ? ? -108.14 53.26   
8  1 GLU B 254 ? ? -91.42  53.26   
9  1 LEU C 43  ? ? -67.83  95.90   
10 1 ASP C 99  ? ? -153.27 80.76   
11 1 ASN C 245 ? ? -95.88  58.89   
12 1 ASN D 245 ? ? -91.76  55.77   
13 1 GLU D 254 ? ? 58.82   -4.01   
14 1 ARG D 255 ? ? -102.21 -164.57 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ARG 
_pdbx_validate_peptide_omega.auth_asym_id_1   D 
_pdbx_validate_peptide_omega.auth_seq_id_1    255 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   LEU 
_pdbx_validate_peptide_omega.auth_asym_id_2   D 
_pdbx_validate_peptide_omega.auth_seq_id_2    256 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   B 
_pdbx_validate_peptide_omega.omega            -134.90 
# 
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 SER 2 ? A SER 2 
3 1 Y 1 B MET 1 ? B MET 1 
4 1 Y 1 B SER 2 ? B SER 2 
5 1 Y 1 C MET 1 ? C MET 1 
6 1 Y 1 C SER 2 ? C SER 2 
7 1 Y 1 D MET 1 ? D MET 1 
8 1 Y 1 D SER 2 ? D SER 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PEG C1   C  N N 260 
PEG O1   O  N N 261 
PEG C2   C  N N 262 
PEG O2   O  N N 263 
PEG C3   C  N N 264 
PEG C4   C  N N 265 
PEG O4   O  N N 266 
PEG H11  H  N N 267 
PEG H12  H  N N 268 
PEG HO1  H  N N 269 
PEG H21  H  N N 270 
PEG H22  H  N N 271 
PEG H31  H  N N 272 
PEG H32  H  N N 273 
PEG H41  H  N N 274 
PEG H42  H  N N 275 
PEG HO4  H  N N 276 
PHE N    N  N N 277 
PHE CA   C  N S 278 
PHE C    C  N N 279 
PHE O    O  N N 280 
PHE CB   C  N N 281 
PHE CG   C  Y N 282 
PHE CD1  C  Y N 283 
PHE CD2  C  Y N 284 
PHE CE1  C  Y N 285 
PHE CE2  C  Y N 286 
PHE CZ   C  Y N 287 
PHE OXT  O  N N 288 
PHE H    H  N N 289 
PHE H2   H  N N 290 
PHE HA   H  N N 291 
PHE HB2  H  N N 292 
PHE HB3  H  N N 293 
PHE HD1  H  N N 294 
PHE HD2  H  N N 295 
PHE HE1  H  N N 296 
PHE HE2  H  N N 297 
PHE HZ   H  N N 298 
PHE HXT  H  N N 299 
PRO N    N  N N 300 
PRO CA   C  N S 301 
PRO C    C  N N 302 
PRO O    O  N N 303 
PRO CB   C  N N 304 
PRO CG   C  N N 305 
PRO CD   C  N N 306 
PRO OXT  O  N N 307 
PRO H    H  N N 308 
PRO HA   H  N N 309 
PRO HB2  H  N N 310 
PRO HB3  H  N N 311 
PRO HG2  H  N N 312 
PRO HG3  H  N N 313 
PRO HD2  H  N N 314 
PRO HD3  H  N N 315 
PRO HXT  H  N N 316 
SER N    N  N N 317 
SER CA   C  N S 318 
SER C    C  N N 319 
SER O    O  N N 320 
SER CB   C  N N 321 
SER OG   O  N N 322 
SER OXT  O  N N 323 
SER H    H  N N 324 
SER H2   H  N N 325 
SER HA   H  N N 326 
SER HB2  H  N N 327 
SER HB3  H  N N 328 
SER HG   H  N N 329 
SER HXT  H  N N 330 
THR N    N  N N 331 
THR CA   C  N S 332 
THR C    C  N N 333 
THR O    O  N N 334 
THR CB   C  N R 335 
THR OG1  O  N N 336 
THR CG2  C  N N 337 
THR OXT  O  N N 338 
THR H    H  N N 339 
THR H2   H  N N 340 
THR HA   H  N N 341 
THR HB   H  N N 342 
THR HG1  H  N N 343 
THR HG21 H  N N 344 
THR HG22 H  N N 345 
THR HG23 H  N N 346 
THR HXT  H  N N 347 
TRP N    N  N N 348 
TRP CA   C  N S 349 
TRP C    C  N N 350 
TRP O    O  N N 351 
TRP CB   C  N N 352 
TRP CG   C  Y N 353 
TRP CD1  C  Y N 354 
TRP CD2  C  Y N 355 
TRP NE1  N  Y N 356 
TRP CE2  C  Y N 357 
TRP CE3  C  Y N 358 
TRP CZ2  C  Y N 359 
TRP CZ3  C  Y N 360 
TRP CH2  C  Y N 361 
TRP OXT  O  N N 362 
TRP H    H  N N 363 
TRP H2   H  N N 364 
TRP HA   H  N N 365 
TRP HB2  H  N N 366 
TRP HB3  H  N N 367 
TRP HD1  H  N N 368 
TRP HE1  H  N N 369 
TRP HE3  H  N N 370 
TRP HZ2  H  N N 371 
TRP HZ3  H  N N 372 
TRP HH2  H  N N 373 
TRP HXT  H  N N 374 
TYR N    N  N N 375 
TYR CA   C  N S 376 
TYR C    C  N N 377 
TYR O    O  N N 378 
TYR CB   C  N N 379 
TYR CG   C  Y N 380 
TYR CD1  C  Y N 381 
TYR CD2  C  Y N 382 
TYR CE1  C  Y N 383 
TYR CE2  C  Y N 384 
TYR CZ   C  Y N 385 
TYR OH   O  N N 386 
TYR OXT  O  N N 387 
TYR H    H  N N 388 
TYR H2   H  N N 389 
TYR HA   H  N N 390 
TYR HB2  H  N N 391 
TYR HB3  H  N N 392 
TYR HD1  H  N N 393 
TYR HD2  H  N N 394 
TYR HE1  H  N N 395 
TYR HE2  H  N N 396 
TYR HH   H  N N 397 
TYR HXT  H  N N 398 
V50 F13  F  N N 399 
V50 C4   C  Y N 400 
V50 C5   C  Y N 401 
V50 S7   S  N N 402 
V50 O9   O  N N 403 
V50 N23  N  N N 404 
V50 O8   O  N N 405 
V50 C6   C  Y N 406 
V50 F11  F  N N 407 
V50 C1   C  Y N 408 
V50 F10  F  N N 409 
V50 C3   C  Y N 410 
V50 F12  F  N N 411 
V50 C2   C  Y N 412 
V50 S14  S  N N 413 
V50 C15  C  Y N 414 
V50 N20  N  Y N 415 
V50 C19  C  Y N 416 
V50 C21  C  N N 417 
V50 C18  C  Y N 418 
V50 C17  C  Y N 419 
V50 N16  N  Y N 420 
V50 C22  C  N N 421 
V50 H1   H  N N 422 
V50 H2   H  N N 423 
V50 H3   H  N N 424 
V50 H4   H  N N 425 
V50 H5   H  N N 426 
V50 H6   H  N N 427 
V50 H7   H  N N 428 
V50 H8   H  N N 429 
V50 H9   H  N N 430 
VAL N    N  N N 431 
VAL CA   C  N S 432 
VAL C    C  N N 433 
VAL O    O  N N 434 
VAL CB   C  N N 435 
VAL CG1  C  N N 436 
VAL CG2  C  N N 437 
VAL OXT  O  N N 438 
VAL H    H  N N 439 
VAL H2   H  N N 440 
VAL HA   H  N N 441 
VAL HB   H  N N 442 
VAL HG11 H  N N 443 
VAL HG12 H  N N 444 
VAL HG13 H  N N 445 
VAL HG21 H  N N 446 
VAL HG22 H  N N 447 
VAL HG23 H  N N 448 
VAL HXT  H  N N 449 
ZN  ZN   ZN N N 450 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PEG C1  O1   sing N N 246 
PEG C1  C2   sing N N 247 
PEG C1  H11  sing N N 248 
PEG C1  H12  sing N N 249 
PEG O1  HO1  sing N N 250 
PEG C2  O2   sing N N 251 
PEG C2  H21  sing N N 252 
PEG C2  H22  sing N N 253 
PEG O2  C3   sing N N 254 
PEG C3  C4   sing N N 255 
PEG C3  H31  sing N N 256 
PEG C3  H32  sing N N 257 
PEG C4  O4   sing N N 258 
PEG C4  H41  sing N N 259 
PEG C4  H42  sing N N 260 
PEG O4  HO4  sing N N 261 
PHE N   CA   sing N N 262 
PHE N   H    sing N N 263 
PHE N   H2   sing N N 264 
PHE CA  C    sing N N 265 
PHE CA  CB   sing N N 266 
PHE CA  HA   sing N N 267 
PHE C   O    doub N N 268 
PHE C   OXT  sing N N 269 
PHE CB  CG   sing N N 270 
PHE CB  HB2  sing N N 271 
PHE CB  HB3  sing N N 272 
PHE CG  CD1  doub Y N 273 
PHE CG  CD2  sing Y N 274 
PHE CD1 CE1  sing Y N 275 
PHE CD1 HD1  sing N N 276 
PHE CD2 CE2  doub Y N 277 
PHE CD2 HD2  sing N N 278 
PHE CE1 CZ   doub Y N 279 
PHE CE1 HE1  sing N N 280 
PHE CE2 CZ   sing Y N 281 
PHE CE2 HE2  sing N N 282 
PHE CZ  HZ   sing N N 283 
PHE OXT HXT  sing N N 284 
PRO N   CA   sing N N 285 
PRO N   CD   sing N N 286 
PRO N   H    sing N N 287 
PRO CA  C    sing N N 288 
PRO CA  CB   sing N N 289 
PRO CA  HA   sing N N 290 
PRO C   O    doub N N 291 
PRO C   OXT  sing N N 292 
PRO CB  CG   sing N N 293 
PRO CB  HB2  sing N N 294 
PRO CB  HB3  sing N N 295 
PRO CG  CD   sing N N 296 
PRO CG  HG2  sing N N 297 
PRO CG  HG3  sing N N 298 
PRO CD  HD2  sing N N 299 
PRO CD  HD3  sing N N 300 
PRO OXT HXT  sing N N 301 
SER N   CA   sing N N 302 
SER N   H    sing N N 303 
SER N   H2   sing N N 304 
SER CA  C    sing N N 305 
SER CA  CB   sing N N 306 
SER CA  HA   sing N N 307 
SER C   O    doub N N 308 
SER C   OXT  sing N N 309 
SER CB  OG   sing N N 310 
SER CB  HB2  sing N N 311 
SER CB  HB3  sing N N 312 
SER OG  HG   sing N N 313 
SER OXT HXT  sing N N 314 
THR N   CA   sing N N 315 
THR N   H    sing N N 316 
THR N   H2   sing N N 317 
THR CA  C    sing N N 318 
THR CA  CB   sing N N 319 
THR CA  HA   sing N N 320 
THR C   O    doub N N 321 
THR C   OXT  sing N N 322 
THR CB  OG1  sing N N 323 
THR CB  CG2  sing N N 324 
THR CB  HB   sing N N 325 
THR OG1 HG1  sing N N 326 
THR CG2 HG21 sing N N 327 
THR CG2 HG22 sing N N 328 
THR CG2 HG23 sing N N 329 
THR OXT HXT  sing N N 330 
TRP N   CA   sing N N 331 
TRP N   H    sing N N 332 
TRP N   H2   sing N N 333 
TRP CA  C    sing N N 334 
TRP CA  CB   sing N N 335 
TRP CA  HA   sing N N 336 
TRP C   O    doub N N 337 
TRP C   OXT  sing N N 338 
TRP CB  CG   sing N N 339 
TRP CB  HB2  sing N N 340 
TRP CB  HB3  sing N N 341 
TRP CG  CD1  doub Y N 342 
TRP CG  CD2  sing Y N 343 
TRP CD1 NE1  sing Y N 344 
TRP CD1 HD1  sing N N 345 
TRP CD2 CE2  doub Y N 346 
TRP CD2 CE3  sing Y N 347 
TRP NE1 CE2  sing Y N 348 
TRP NE1 HE1  sing N N 349 
TRP CE2 CZ2  sing Y N 350 
TRP CE3 CZ3  doub Y N 351 
TRP CE3 HE3  sing N N 352 
TRP CZ2 CH2  doub Y N 353 
TRP CZ2 HZ2  sing N N 354 
TRP CZ3 CH2  sing Y N 355 
TRP CZ3 HZ3  sing N N 356 
TRP CH2 HH2  sing N N 357 
TRP OXT HXT  sing N N 358 
TYR N   CA   sing N N 359 
TYR N   H    sing N N 360 
TYR N   H2   sing N N 361 
TYR CA  C    sing N N 362 
TYR CA  CB   sing N N 363 
TYR CA  HA   sing N N 364 
TYR C   O    doub N N 365 
TYR C   OXT  sing N N 366 
TYR CB  CG   sing N N 367 
TYR CB  HB2  sing N N 368 
TYR CB  HB3  sing N N 369 
TYR CG  CD1  doub Y N 370 
TYR CG  CD2  sing Y N 371 
TYR CD1 CE1  sing Y N 372 
TYR CD1 HD1  sing N N 373 
TYR CD2 CE2  doub Y N 374 
TYR CD2 HD2  sing N N 375 
TYR CE1 CZ   doub Y N 376 
TYR CE1 HE1  sing N N 377 
TYR CE2 CZ   sing Y N 378 
TYR CE2 HE2  sing N N 379 
TYR CZ  OH   sing N N 380 
TYR OH  HH   sing N N 381 
TYR OXT HXT  sing N N 382 
V50 C21 C19  sing N N 383 
V50 C19 N20  doub Y N 384 
V50 C19 C18  sing Y N 385 
V50 N20 C15  sing Y N 386 
V50 C18 C17  doub Y N 387 
V50 S14 C15  sing N N 388 
V50 S14 C2   sing N N 389 
V50 C15 N16  doub Y N 390 
V50 F10 C1   sing N N 391 
V50 C17 N16  sing Y N 392 
V50 C17 C22  sing N N 393 
V50 C1  C2   doub Y N 394 
V50 C1  C6   sing Y N 395 
V50 C2  C3   sing Y N 396 
V50 F12 C3   sing N N 397 
V50 C3  C4   doub Y N 398 
V50 C6  F11  sing N N 399 
V50 C6  C5   doub Y N 400 
V50 C4  C5   sing Y N 401 
V50 C4  F13  sing N N 402 
V50 C5  S7   sing N N 403 
V50 N23 S7   sing N N 404 
V50 O8  S7   doub N N 405 
V50 S7  O9   doub N N 406 
V50 N23 H1   sing N N 407 
V50 N23 H2   sing N N 408 
V50 C21 H3   sing N N 409 
V50 C21 H4   sing N N 410 
V50 C21 H5   sing N N 411 
V50 C18 H6   sing N N 412 
V50 C22 H7   sing N N 413 
V50 C22 H8   sing N N 414 
V50 C22 H9   sing N N 415 
VAL N   CA   sing N N 416 
VAL N   H    sing N N 417 
VAL N   H2   sing N N 418 
VAL CA  C    sing N N 419 
VAL CA  CB   sing N N 420 
VAL CA  HA   sing N N 421 
VAL C   O    doub N N 422 
VAL C   OXT  sing N N 423 
VAL CB  CG1  sing N N 424 
VAL CB  CG2  sing N N 425 
VAL CB  HB   sing N N 426 
VAL CG1 HG11 sing N N 427 
VAL CG1 HG12 sing N N 428 
VAL CG1 HG13 sing N N 429 
VAL CG2 HG21 sing N N 430 
VAL CG2 HG22 sing N N 431 
VAL CG2 HG23 sing N N 432 
VAL OXT HXT  sing N N 433 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                   ZN  
3 '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' V50 
4 'DI(HYDROXYETHYL)ETHER'                                                      PEG 
5 1,2-ETHANEDIOL                                                               EDO 
6 water                                                                        HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1JD0 
_pdbx_initial_refinement_model.details          'PDB ENTRY 1JD0' 
# 
