data_4QJX
# 
_entry.id   4QJX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.381 
_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   4QJX         pdb_00004qjx 10.2210/pdb4qjx/pdb 
RCSB  RCSB086148   ?            ?                   
WWPDB D_1000086148 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4QIY . unspecified 
PDB 4QIZ . unspecified 
PDB 4QJ0 . unspecified 
PDB 4QJM . unspecified 
PDB 4QJO . unspecified 
PDB 4QJP . unspecified 
PDB 4QJW . unspecified 
PDB 4QTL . unspecified 
# 
_pdbx_database_status.entry_id                        4QJX 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2014-06-05 
_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.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                     
'Functionalization of Fluorinated Benzenesulfonamides and Their Inhibitory Properties toward Carbonic Anhydrases' 
_citation.journal_abbrev            Chemmedchem 
_citation.journal_volume            10 
_citation.page_first                662 
_citation.page_last                 687 
_citation.year                      2015 
_citation.journal_id_ASTM           ? 
_citation.country                   DE 
_citation.journal_id_ISSN           1860-7179 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25758852 
_citation.pdbx_database_id_DOI      10.1002/cmdc.201402490 
# 
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 'Timm, D.D.'        4  ? 
primary 'Smirnoviene, J.'   5  ? 
primary 'Kazokaite, J.'     6  ? 
primary 'Michailoviene, V.' 7  ? 
primary 'Zaksauskas, A.'    8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Matulis, D.'       11 ? 
# 
_cell.entry_id           4QJX 
_cell.length_a           56.822 
_cell.length_b           56.822 
_cell.length_c           159.608 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              8 
_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                         4QJX 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_symmetry.Int_Tables_number                96 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_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 13'                                                          29613.318 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                       65.409    1   ?       ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                          106.120   1   ?       ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                                   62.068    1   ?       ? ? ? 
5 non-polymer syn '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 424.415   1   ?       ? ? ? 
6 water       nat water                                                                            18.015    253 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XIII, Carbonic anhydrase XIII, CA-XIII' 
# 
_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       
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_strand_id                 A 
_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   MET n 
1 3   SER n 
1 4   ARG n 
1 5   LEU n 
1 6   SER n 
1 7   TRP n 
1 8   GLY n 
1 9   TYR n 
1 10  ARG n 
1 11  GLU n 
1 12  HIS n 
1 13  ASN n 
1 14  GLY n 
1 15  PRO n 
1 16  ILE n 
1 17  HIS n 
1 18  TRP n 
1 19  LYS n 
1 20  GLU n 
1 21  PHE n 
1 22  PHE n 
1 23  PRO n 
1 24  ILE n 
1 25  ALA n 
1 26  ASP n 
1 27  GLY n 
1 28  ASP n 
1 29  GLN n 
1 30  GLN n 
1 31  SER n 
1 32  PRO n 
1 33  ILE n 
1 34  GLU n 
1 35  ILE n 
1 36  LYS n 
1 37  THR n 
1 38  LYS n 
1 39  GLU n 
1 40  VAL n 
1 41  LYS n 
1 42  TYR n 
1 43  ASP n 
1 44  SER n 
1 45  SER n 
1 46  LEU n 
1 47  ARG n 
1 48  PRO n 
1 49  LEU n 
1 50  SER n 
1 51  ILE n 
1 52  LYS n 
1 53  TYR n 
1 54  ASP n 
1 55  PRO n 
1 56  SER n 
1 57  SER n 
1 58  ALA n 
1 59  LYS n 
1 60  ILE n 
1 61  ILE n 
1 62  SER n 
1 63  ASN n 
1 64  SER n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  PHE n 
1 69  ASN n 
1 70  VAL n 
1 71  ASP n 
1 72  PHE n 
1 73  ASP n 
1 74  ASP n 
1 75  THR n 
1 76  GLU n 
1 77  ASN n 
1 78  LYS n 
1 79  SER n 
1 80  VAL n 
1 81  LEU n 
1 82  ARG n 
1 83  GLY n 
1 84  GLY n 
1 85  PRO n 
1 86  LEU n 
1 87  THR n 
1 88  GLY n 
1 89  SER n 
1 90  TYR n 
1 91  ARG n 
1 92  LEU n 
1 93  ARG n 
1 94  GLN n 
1 95  VAL n 
1 96  HIS n 
1 97  LEU n 
1 98  HIS n 
1 99  TRP n 
1 100 GLY n 
1 101 SER n 
1 102 ALA n 
1 103 ASP n 
1 104 ASP n 
1 105 HIS n 
1 106 GLY n 
1 107 SER n 
1 108 GLU n 
1 109 HIS n 
1 110 ILE n 
1 111 VAL n 
1 112 ASP n 
1 113 GLY n 
1 114 VAL n 
1 115 SER n 
1 116 TYR n 
1 117 ALA n 
1 118 ALA n 
1 119 GLU n 
1 120 LEU n 
1 121 HIS n 
1 122 VAL n 
1 123 VAL n 
1 124 HIS n 
1 125 TRP n 
1 126 ASN n 
1 127 SER n 
1 128 ASP n 
1 129 LYS n 
1 130 TYR n 
1 131 PRO n 
1 132 SER n 
1 133 PHE n 
1 134 VAL n 
1 135 GLU n 
1 136 ALA n 
1 137 ALA n 
1 138 HIS n 
1 139 GLU n 
1 140 PRO n 
1 141 ASP n 
1 142 GLY n 
1 143 LEU n 
1 144 ALA n 
1 145 VAL n 
1 146 LEU n 
1 147 GLY n 
1 148 VAL n 
1 149 PHE n 
1 150 LEU n 
1 151 GLN n 
1 152 ILE n 
1 153 GLY n 
1 154 GLU n 
1 155 PRO n 
1 156 ASN n 
1 157 SER n 
1 158 GLN n 
1 159 LEU n 
1 160 GLN n 
1 161 LYS n 
1 162 ILE n 
1 163 THR n 
1 164 ASP n 
1 165 THR n 
1 166 LEU n 
1 167 ASP n 
1 168 SER n 
1 169 ILE n 
1 170 LYS n 
1 171 GLU n 
1 172 LYS n 
1 173 GLY n 
1 174 LYS n 
1 175 GLN n 
1 176 THR n 
1 177 ARG n 
1 178 PHE n 
1 179 THR n 
1 180 ASN n 
1 181 PHE n 
1 182 ASP n 
1 183 LEU n 
1 184 LEU n 
1 185 SER n 
1 186 LEU n 
1 187 LEU n 
1 188 PRO n 
1 189 PRO n 
1 190 SER n 
1 191 TRP n 
1 192 ASP n 
1 193 TYR n 
1 194 TRP n 
1 195 THR n 
1 196 TYR n 
1 197 PRO n 
1 198 GLY n 
1 199 SER n 
1 200 LEU n 
1 201 THR n 
1 202 VAL n 
1 203 PRO n 
1 204 PRO n 
1 205 LEU n 
1 206 LEU n 
1 207 GLU n 
1 208 SER n 
1 209 VAL n 
1 210 THR n 
1 211 TRP n 
1 212 ILE n 
1 213 VAL n 
1 214 LEU n 
1 215 LYS n 
1 216 GLN n 
1 217 PRO n 
1 218 ILE n 
1 219 ASN n 
1 220 ILE n 
1 221 SER n 
1 222 SER n 
1 223 GLN n 
1 224 GLN n 
1 225 LEU n 
1 226 ALA n 
1 227 LYS n 
1 228 PHE n 
1 229 ARG n 
1 230 SER n 
1 231 LEU n 
1 232 LEU n 
1 233 CYS n 
1 234 THR n 
1 235 ALA n 
1 236 GLU n 
1 237 GLY n 
1 238 GLU n 
1 239 ALA n 
1 240 ALA n 
1 241 ALA n 
1 242 PHE n 
1 243 LEU n 
1 244 VAL n 
1 245 SER n 
1 246 ASN n 
1 247 HIS n 
1 248 ARG n 
1 249 PRO n 
1 250 PRO n 
1 251 GLN n 
1 252 PRO n 
1 253 LEU n 
1 254 LYS n 
1 255 GLY n 
1 256 ARG n 
1 257 LYS n 
1 258 VAL n 
1 259 ARG n 
1 260 ALA n 
1 261 SER n 
1 262 PHE n 
1 263 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA13 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH13_HUMAN 
_struct_ref.pdbx_db_accession          Q8N1Q1 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSVL
RGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQK
ITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAAA
FLVSNHRPPQPLKGRKVRASFH
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4QJX 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 263 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8N1Q1 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  262 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       263 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             4QJX 
_struct_ref_seq_dif.mon_id                       MET 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q8N1Q1 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'expression tag' 
_struct_ref_seq_dif.pdbx_auth_seq_num            1 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
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 
VAL 'L-peptide linking' y VALINE                                                                           ?                 
'C5 H11 N O2'         117.146 
WWO non-polymer         . '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ?                 
'C15 H15 F3 N2 O5 S2' 424.415 
ZN  non-polymer         . 'ZINC ION'                                                                       ?                 
'Zn 2'                65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4QJX 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   42.3 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.pdbx_mosaicity        0.59 
_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 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    
'0.1M sodium citrate (pH 5.5), 0.2M sodium acetate (pH 4.5), 28% PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR555 FLAT PANEL' 
_diffrn_detector.pdbx_collection_date   2011-11-20 
_diffrn_detector.details                'Detector swing-out angle up to 30 degrees' 
# 
_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   0.815 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X11' 
_diffrn_source.pdbx_wavelength_list        0.815 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X11 
# 
_reflns.entry_id                     4QJX 
_reflns.d_resolution_high            1.950 
_reflns.d_resolution_low             56.822 
_reflns.number_all                   ? 
_reflns.number_obs                   19979 
_reflns.pdbx_netI_over_sigmaI        20.900 
_reflns.pdbx_Rsym_value              0.095 
_reflns.pdbx_redundancy              14.000 
_reflns.percent_possible_obs         100.000 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        23.708 
_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.pdbx_rejects 
_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.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.95 2.06  ? 40195 ? ? 0.537 1.3  0.537 ? 14.20 ? 5.80  ? 2830 ? ? 0.568 ? 100.00 0.57 0.15 1  1 
2.06 2.18  ? 38622 ? ? 0.376 1.8  0.376 ? 14.30 ? 8.50  ? 2693 ? ? 0.397 ? 100.00 0.40 0.10 2  1 
2.18 2.33  ? 36065 ? ? 0.279 2.4  0.279 ? 14.30 ? 11.20 ? 2518 ? ? 0.295 ? 100.00 0.29 0.08 3  1 
2.33 2.52  ? 34055 ? ? 0.205 3.4  0.205 ? 14.20 ? 14.40 ? 2390 ? ? 0.218 ? 100.00 0.22 0.06 4  1 
2.52 2.76  ? 31387 ? ? 0.141 4.8  0.141 ? 14.20 ? 18.70 ? 2212 ? ? 0.150 ? 100.00 0.15 0.04 5  1 
2.76 3.08  ? 28306 ? ? 0.087 7.8  0.087 ? 14.10 ? 26.20 ? 2007 ? ? 0.093 ? 100.00 0.09 0.02 6  1 
3.08 3.56  ? 24978 ? ? 0.055 11.5 0.055 ? 14.00 ? 37.60 ? 1789 ? ? 0.059 ? 100.00 0.06 0.02 7  1 
3.56 4.36  ? 21326 ? ? 0.042 13.6 0.042 ? 13.70 ? 47.10 ? 1554 ? ? 0.045 ? 100.00 0.05 0.01 8  1 
4.36 6.17  ? 16324 ? ? 0.037 15.9 0.037 ? 13.30 ? 43.90 ? 1228 ? ? 0.040 ? 100.00 0.04 0.01 9  1 
6.17 56.82 ? 8319  ? ? 0.040 10.8 0.040 ? 11.00 ? 37.10 ? 758  ? ? 0.044 ? 99.90  0.04 0.01 10 1 
# 
_refine.entry_id                                 4QJX 
_refine.ls_d_res_high                            1.950 
_refine.ls_d_res_low                             53.530 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.960 
_refine.ls_number_reflns_obs                     19911 
_refine.ls_number_reflns_all                     19911 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES' 
_refine.ls_R_factor_all                          0.195 
_refine.ls_R_factor_obs                          0.195 
_refine.ls_R_factor_R_work                       0.190 
_refine.ls_wR_factor_R_work                      0.170 
_refine.ls_R_factor_R_free                       0.237 
_refine.ls_wR_factor_R_free                      0.217 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  2001 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.570 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.270 
_refine.aniso_B[2][2]                            0.270 
_refine.aniso_B[3][3]                            -0.540 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.945 
_refine.correlation_coeff_Fo_to_Fc_free          0.927 
_refine.overall_SU_R_Cruickshank_DPI             0.208 
_refine.overall_SU_R_free                        0.176 
_refine.pdbx_overall_ESU_R                       0.208 
_refine.pdbx_overall_ESU_R_Free                  0.176 
_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                   0.842 
_refine.B_iso_max                                64.16 
_refine.B_iso_min                                8.87 
_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                      2NNO 
_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        2054 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.number_atoms_solvent             253 
_refine_hist.number_atoms_total               2346 
_refine_hist.d_res_high                       1.950 
_refine_hist.d_res_low                        53.530 
# 
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       2225 0.018  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3036 1.890  1.959  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 271  7.081  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 103  33.588 24.078 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 357  15.290 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 11   18.550 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         316  0.155  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1735 0.011  0.021  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.950 
_refine_ls_shell.d_res_low                        2.001 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               99.860 
_refine_ls_shell.number_reflns_R_work             1294 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.281 
_refine_ls_shell.R_factor_R_free                  0.316 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             126 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1420 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  4QJX 
_struct.title                     'Crystal structure of human carbonic anhydrase isozyme XIII with inhibitor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4QJX 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, LYASE-LYASE INHIBITOR complex' 
_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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
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 14  ? PHE A 21  ? GLY A 14  PHE A 21  5 ? 8 
HELX_P HELX_P2 2 PHE A 22  ? GLY A 27  ? PHE A 22  GLY A 27  5 ? 6 
HELX_P HELX_P3 3 SER A 132 ? ALA A 137 ? SER A 132 ALA A 137 1 ? 6 
HELX_P HELX_P4 4 ASN A 156 ? ASP A 164 ? ASN A 156 ASP A 164 1 ? 9 
HELX_P HELX_P5 5 THR A 165 ? LYS A 170 ? THR A 165 LYS A 170 5 ? 6 
HELX_P HELX_P6 6 LEU A 183 ? LEU A 187 ? LEU A 183 LEU A 187 5 ? 5 
HELX_P HELX_P7 7 SER A 221 ? ARG A 229 ? SER A 221 ARG A 229 1 ? 9 
# 
_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 
metalc1 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc2 metalc ? ? A HIS 98  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 98  A ZN  301 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc3 metalc ? ? A HIS 121 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 121 A ZN  301 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E WWO . N10 ? ? A ZN  301 A WWO 304 1_555 ? ? ? ? ? ? ? 1.725 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E WWO . S7  ? ? A ZN  301 A WWO 304 1_555 ? ? ? ? ? ? ? 2.989 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 31  A . ? SER 31  A PRO 32  A ? PRO 32  A 1 -0.82 
2 PRO 203 A . ? PRO 203 A PRO 204 A ? PRO 204 A 1 11.75 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 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      
# 
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  GLU A 34  ? ILE A 35  ? GLU A 34  ILE A 35  
A 2  ILE A 110 ? VAL A 111 ? ILE A 110 VAL A 111 
B 1  LYS A 41  ? TYR A 42  ? LYS A 41  TYR A 42  
B 2  ARG A 259 ? ALA A 260 ? ARG A 259 ALA A 260 
B 3  TYR A 193 ? GLY A 198 ? TYR A 193 GLY A 198 
B 4  VAL A 209 ? LEU A 214 ? VAL A 209 LEU A 214 
B 5  LEU A 143 ? ILE A 152 ? LEU A 143 ILE A 152 
B 6  ALA A 118 ? ASN A 126 ? ALA A 118 ASN A 126 
B 7  TYR A 90  ? TRP A 99  ? TYR A 90  TRP A 99  
B 8  PHE A 68  ? PHE A 72  ? PHE A 68  PHE A 72  
B 9  ALA A 58  ? ASN A 63  ? ALA A 58  ASN A 63  
B 10 GLN A 175 ? ARG A 177 ? GLN A 175 ARG A 177 
C 1  LEU A 49  ? LYS A 52  ? LEU A 49  LYS A 52  
C 2  VAL A 80  ? GLY A 83  ? VAL A 80  GLY A 83  
C 3  TYR A 90  ? TRP A 99  ? TYR A 90  TRP A 99  
C 4  ALA A 118 ? ASN A 126 ? ALA A 118 ASN A 126 
C 5  LEU A 143 ? ILE A 152 ? LEU A 143 ILE A 152 
C 6  ILE A 218 ? ILE A 220 ? ILE A 218 ILE A 220 
# 
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 ILE A 35  ? N ILE A 35  O ILE A 110 ? O ILE A 110 
B 1 2  N LYS A 41  ? N LYS A 41  O ALA A 260 ? O ALA A 260 
B 2 3  O ARG A 259 ? O ARG A 259 N THR A 195 ? N THR A 195 
B 3 4  N GLY A 198 ? N GLY A 198 O VAL A 209 ? O VAL A 209 
B 4 5  O LEU A 214 ? O LEU A 214 N GLY A 147 ? N GLY A 147 
B 5 6  O VAL A 148 ? O VAL A 148 N LEU A 120 ? N LEU A 120 
B 6 7  O VAL A 123 ? O VAL A 123 N ARG A 93  ? N ARG A 93  
B 7 8  O VAL A 95  ? O VAL A 95  N VAL A 70  ? N VAL A 70  
B 8 9  O ASN A 69  ? O ASN A 69  N SER A 62  ? N SER A 62  
B 9 10 N ILE A 61  ? N ILE A 61  O THR A 176 ? O THR A 176 
C 1 2  N SER A 50  ? N SER A 50  O ARG A 82  ? O ARG A 82  
C 2 3  N LEU A 81  ? N LEU A 81  O TYR A 90  ? O TYR A 90  
C 3 4  N ARG A 93  ? N ARG A 93  O VAL A 123 ? O VAL A 123 
C 4 5  N LEU A 120 ? N LEU A 120 O VAL A 148 ? O VAL A 148 
C 5 6  N GLN A 151 ? N GLN A 151 O ILE A 218 ? O ILE A 218 
# 
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 PEG 302 ? 4  'BINDING SITE FOR RESIDUE PEG A 302' 
AC3 Software A EDO 303 ? 5  'BINDING SITE FOR RESIDUE EDO A 303' 
AC4 Software A WWO 304 ? 13 'BINDING SITE FOR RESIDUE WWO A 304' 
# 
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 96  ? HIS A 96  . ? 1_555 ? 
2  AC1 4  HIS A 98  ? HIS A 98  . ? 1_555 ? 
3  AC1 4  HIS A 121 ? HIS A 121 . ? 1_555 ? 
4  AC1 4  WWO E .   ? WWO A 304 . ? 1_555 ? 
5  AC2 4  SER A 190 ? SER A 190 . ? 1_555 ? 
6  AC2 4  GLN A 216 ? GLN A 216 . ? 1_555 ? 
7  AC2 4  HOH F .   ? HOH A 503 . ? 1_555 ? 
8  AC2 4  HOH F .   ? HOH A 598 . ? 1_555 ? 
9  AC3 5  LYS A 161 ? LYS A 161 . ? 1_555 ? 
10 AC3 5  ARG A 177 ? ARG A 177 . ? 1_555 ? 
11 AC3 5  PHE A 178 ? PHE A 178 . ? 1_555 ? 
12 AC3 5  THR A 179 ? THR A 179 . ? 1_555 ? 
13 AC3 5  HOH F .   ? HOH A 593 . ? 1_555 ? 
14 AC4 13 SER A 64  ? SER A 64  . ? 1_555 ? 
15 AC4 13 HIS A 66  ? HIS A 66  . ? 1_555 ? 
16 AC4 13 ASN A 69  ? ASN A 69  . ? 1_555 ? 
17 AC4 13 HIS A 96  ? HIS A 96  . ? 1_555 ? 
18 AC4 13 HIS A 98  ? HIS A 98  . ? 1_555 ? 
19 AC4 13 HIS A 121 ? HIS A 121 . ? 1_555 ? 
20 AC4 13 PHE A 133 ? PHE A 133 . ? 1_555 ? 
21 AC4 13 ALA A 137 ? ALA A 137 . ? 1_555 ? 
22 AC4 13 LEU A 200 ? LEU A 200 . ? 1_555 ? 
23 AC4 13 THR A 201 ? THR A 201 . ? 1_555 ? 
24 AC4 13 VAL A 202 ? VAL A 202 . ? 1_555 ? 
25 AC4 13 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
26 AC4 13 HOH F .   ? HOH A 546 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4QJX 
_atom_sites.fract_transf_matrix[1][1]   0.017599 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017599 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006265 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
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   . SER A 1 6   ? 14.886 9.973   5.825   1.00  37.68 ? 6   SER A N   1 
ATOM   2    C  CA  . SER A 1 6   ? 15.251 9.911   7.276   1.00  31.73 ? 6   SER A CA  1 
ATOM   3    C  C   . SER A 1 6   ? 14.633 8.706   8.107   1.00  28.39 ? 6   SER A C   1 
ATOM   4    O  O   . SER A 1 6   ? 14.385 8.794   9.320   1.00  26.90 ? 6   SER A O   1 
ATOM   5    C  CB  . SER A 1 6   ? 15.113 11.300  7.916   1.00  36.55 ? 6   SER A CB  1 
ATOM   6    O  OG  . SER A 1 6   ? 13.758 11.711  7.968   1.00  40.77 ? 6   SER A OG  1 
ATOM   7    N  N   . TRP A 1 7   ? 14.459 7.563   7.448   1.00  20.53 ? 7   TRP A N   1 
ATOM   8    C  CA  . TRP A 1 7   ? 14.259 6.299   8.148   1.00  17.83 ? 7   TRP A CA  1 
ATOM   9    C  C   . TRP A 1 7   ? 15.342 5.919   9.130   1.00  16.86 ? 7   TRP A C   1 
ATOM   10   O  O   . TRP A 1 7   ? 16.542 6.278   8.987   1.00  16.87 ? 7   TRP A O   1 
ATOM   11   C  CB  . TRP A 1 7   ? 14.064 5.196   7.151   1.00  17.78 ? 7   TRP A CB  1 
ATOM   12   C  CG  . TRP A 1 7   ? 15.302 4.821   6.434   1.00  17.28 ? 7   TRP A CG  1 
ATOM   13   C  CD1 . TRP A 1 7   ? 15.764 5.312   5.227   1.00  18.24 ? 7   TRP A CD1 1 
ATOM   14   C  CD2 . TRP A 1 7   ? 16.261 3.803   6.834   1.00  16.01 ? 7   TRP A CD2 1 
ATOM   15   N  NE1 . TRP A 1 7   ? 16.914 4.674   4.867   1.00  17.34 ? 7   TRP A NE1 1 
ATOM   16   C  CE2 . TRP A 1 7   ? 17.274 3.771   5.794   1.00  17.72 ? 7   TRP A CE2 1 
ATOM   17   C  CE3 . TRP A 1 7   ? 16.351 2.921   7.909   1.00  15.75 ? 7   TRP A CE3 1 
ATOM   18   C  CZ2 . TRP A 1 7   ? 18.371 2.900   5.844   1.00  16.41 ? 7   TRP A CZ2 1 
ATOM   19   C  CZ3 . TRP A 1 7   ? 17.461 2.077   7.971   1.00  16.53 ? 7   TRP A CZ3 1 
ATOM   20   C  CH2 . TRP A 1 7   ? 18.442 2.062   6.952   1.00  15.65 ? 7   TRP A CH2 1 
ATOM   21   N  N   . GLY A 1 8   ? 14.971 5.167   10.144  1.00  15.79 ? 8   GLY A N   1 
ATOM   22   C  CA  . GLY A 1 8   ? 16.000 4.707   11.078  1.00  16.44 ? 8   GLY A CA  1 
ATOM   23   C  C   . GLY A 1 8   ? 15.450 3.566   11.910  1.00  16.28 ? 8   GLY A C   1 
ATOM   24   O  O   . GLY A 1 8   ? 14.628 2.784   11.424  1.00  15.98 ? 8   GLY A O   1 
ATOM   25   N  N   . TYR A 1 9   ? 15.902 3.440   13.157  1.00  14.79 ? 9   TYR A N   1 
ATOM   26   C  CA  . TYR A 1 9   ? 15.409 2.390   14.056  1.00  15.74 ? 9   TYR A CA  1 
ATOM   27   C  C   . TYR A 1 9   ? 14.904 3.018   15.363  1.00  18.47 ? 9   TYR A C   1 
ATOM   28   O  O   . TYR A 1 9   ? 14.712 2.309   16.363  1.00  15.83 ? 9   TYR A O   1 
ATOM   29   C  CB  . TYR A 1 9   ? 16.567 1.432   14.420  1.00  14.40 ? 9   TYR A CB  1 
ATOM   30   C  CG  . TYR A 1 9   ? 17.049 0.652   13.210  1.00  14.03 ? 9   TYR A CG  1 
ATOM   31   C  CD1 . TYR A 1 9   ? 16.391 -0.480  12.773  1.00  13.12 ? 9   TYR A CD1 1 
ATOM   32   C  CD2 . TYR A 1 9   ? 18.171 1.121   12.471  1.00  13.33 ? 9   TYR A CD2 1 
ATOM   33   C  CE1 . TYR A 1 9   ? 16.856 -1.171  11.638  1.00  12.93 ? 9   TYR A CE1 1 
ATOM   34   C  CE2 . TYR A 1 9   ? 18.637 0.427   11.352  1.00  13.03 ? 9   TYR A CE2 1 
ATOM   35   C  CZ  . TYR A 1 9   ? 17.967 -0.692  10.936  1.00  12.15 ? 9   TYR A CZ  1 
ATOM   36   O  OH  . TYR A 1 9   ? 18.501 -1.357  9.824   1.00  13.15 ? 9   TYR A OH  1 
ATOM   37   N  N   . ARG A 1 10  ? 14.791 4.348   15.371  1.00  23.61 ? 10  ARG A N   1 
ATOM   38   C  CA  . ARG A 1 10  ? 14.268 5.039   16.575  1.00  26.27 ? 10  ARG A CA  1 
ATOM   39   C  C   . ARG A 1 10  ? 12.721 4.915   16.597  1.00  27.33 ? 10  ARG A C   1 
ATOM   40   O  O   . ARG A 1 10  ? 12.107 4.326   15.670  1.00  21.99 ? 10  ARG A O   1 
ATOM   41   C  CB  . ARG A 1 10  ? 14.802 6.478   16.627  1.00  29.33 ? 10  ARG A CB  1 
ATOM   42   C  CG  . ARG A 1 10  ? 16.333 6.549   16.746  1.00  30.70 ? 10  ARG A CG  1 
ATOM   43   C  CD  . ARG A 1 10  ? 16.932 7.912   16.429  1.00  37.57 ? 10  ARG A CD  1 
ATOM   44   N  NE  . ARG A 1 10  ? 16.811 8.861   17.540  1.00  43.18 ? 10  ARG A NE  1 
ATOM   45   C  CZ  . ARG A 1 10  ? 16.850 10.202  17.418  1.00  47.21 ? 10  ARG A CZ  1 
ATOM   46   N  NH1 . ARG A 1 10  ? 16.987 10.782  16.226  1.00  46.06 ? 10  ARG A NH1 1 
ATOM   47   N  NH2 . ARG A 1 10  ? 16.729 10.987  18.494  1.00  43.46 ? 10  ARG A NH2 1 
ATOM   48   N  N   . GLU A 1 11  ? 12.085 5.381   17.677  1.00  26.07 ? 11  GLU A N   1 
ATOM   49   C  CA  . GLU A 1 11  ? 10.603 5.221   17.844  1.00  25.32 ? 11  GLU A CA  1 
ATOM   50   C  C   . GLU A 1 11  ? 9.788  5.768   16.687  1.00  22.94 ? 11  GLU A C   1 
ATOM   51   O  O   . GLU A 1 11  ? 8.876  5.093   16.176  1.00  23.39 ? 11  GLU A O   1 
ATOM   52   C  CB  . GLU A 1 11  ? 10.135 5.927   19.135  1.00  27.76 ? 11  GLU A CB  1 
ATOM   53   C  CG  . GLU A 1 11  ? 8.646  5.717   19.428  1.00  27.57 ? 11  GLU A CG  1 
ATOM   54   C  CD  . GLU A 1 11  ? 8.307  4.290   19.834  0.010 27.32 ? 11  GLU A CD  1 
ATOM   55   O  OE1 . GLU A 1 11  ? 7.207  3.819   19.476  0.010 27.27 ? 11  GLU A OE1 1 
ATOM   56   O  OE2 . GLU A 1 11  ? 9.134  3.637   20.508  0.010 27.22 ? 11  GLU A OE2 1 
ATOM   57   N  N   A HIS A 1 12  ? 10.189 6.966   16.273  0.50  23.39 ? 12  HIS A N   1 
ATOM   58   N  N   B HIS A 1 12  ? 10.041 6.990   16.242  0.50  23.24 ? 12  HIS A N   1 
ATOM   59   C  CA  A HIS A 1 12  ? 9.470  7.803   15.318  0.50  25.81 ? 12  HIS A CA  1 
ATOM   60   C  CA  B HIS A 1 12  ? 9.153  7.548   15.197  0.50  24.15 ? 12  HIS A CA  1 
ATOM   61   C  C   A HIS A 1 12  ? 9.732  7.478   13.862  0.50  24.46 ? 12  HIS A C   1 
ATOM   62   C  C   B HIS A 1 12  ? 9.549  7.176   13.794  0.50  23.71 ? 12  HIS A C   1 
ATOM   63   O  O   A HIS A 1 12  ? 9.018  7.950   12.976  0.50  24.27 ? 12  HIS A O   1 
ATOM   64   O  O   B HIS A 1 12  ? 8.757  7.358   12.857  0.50  23.82 ? 12  HIS A O   1 
ATOM   65   C  CB  A HIS A 1 12  ? 9.871  9.265   15.576  0.50  27.10 ? 12  HIS A CB  1 
ATOM   66   C  CB  B HIS A 1 12  ? 9.088  9.073   15.282  0.50  27.37 ? 12  HIS A CB  1 
ATOM   67   C  CG  A HIS A 1 12  ? 11.372 9.494   15.630  0.50  30.85 ? 12  HIS A CG  1 
ATOM   68   C  CG  B HIS A 1 12  ? 8.470  9.589   16.550  0.50  27.31 ? 12  HIS A CG  1 
ATOM   69   N  ND1 A HIS A 1 12  ? 12.091 9.887   14.550  0.50  31.70 ? 12  HIS A ND1 1 
ATOM   70   N  ND1 B HIS A 1 12  ? 7.236  9.247   16.935  0.50  26.12 ? 12  HIS A ND1 1 
ATOM   71   C  CD2 A HIS A 1 12  ? 12.285 9.370   16.683  0.50  30.11 ? 12  HIS A CD2 1 
ATOM   72   C  CD2 B HIS A 1 12  ? 8.955  10.479  17.516  0.50  29.96 ? 12  HIS A CD2 1 
ATOM   73   C  CE1 A HIS A 1 12  ? 13.385 10.018  14.888  0.50  29.59 ? 12  HIS A CE1 1 
ATOM   74   C  CE1 B HIS A 1 12  ? 6.942  9.856   18.099  0.50  28.36 ? 12  HIS A CE1 1 
ATOM   75   N  NE2 A HIS A 1 12  ? 13.508 9.707   16.192  0.50  34.07 ? 12  HIS A NE2 1 
ATOM   76   N  NE2 B HIS A 1 12  ? 7.991  10.620  18.449  0.50  28.98 ? 12  HIS A NE2 1 
ATOM   77   N  N   . ASN A 1 13  ? 10.787 6.706   13.604  1.00  22.92 ? 13  ASN A N   1 
ATOM   78   C  CA  . ASN A 1 13  ? 11.249 6.376   12.229  1.00  20.77 ? 13  ASN A CA  1 
ATOM   79   C  C   . ASN A 1 13  ? 11.647 4.921   11.944  1.00  20.15 ? 13  ASN A C   1 
ATOM   80   O  O   . ASN A 1 13  ? 12.284 4.629   10.882  1.00  16.19 ? 13  ASN A O   1 
ATOM   81   C  CB  . ASN A 1 13  ? 12.363 7.348   11.797  1.00  20.23 ? 13  ASN A CB  1 
ATOM   82   C  CG  . ASN A 1 13  ? 13.697 7.085   12.504  1.00  19.62 ? 13  ASN A CG  1 
ATOM   83   O  OD1 . ASN A 1 13  ? 13.789 6.236   13.377  1.00  19.35 ? 13  ASN A OD1 1 
ATOM   84   N  ND2 . ASN A 1 13  ? 14.740 7.822   12.100  1.00  18.94 ? 13  ASN A ND2 1 
ATOM   85   N  N   . GLY A 1 14  ? 11.256 4.025   12.867  1.00  18.35 ? 14  GLY A N   1 
ATOM   86   C  CA  . GLY A 1 14  ? 11.763 2.656   12.908  1.00  17.13 ? 14  GLY A CA  1 
ATOM   87   C  C   . GLY A 1 14  ? 10.952 1.784   11.968  1.00  17.38 ? 14  GLY A C   1 
ATOM   88   O  O   . GLY A 1 14  ? 10.065 2.315   11.234  1.00  19.33 ? 14  GLY A O   1 
ATOM   89   N  N   . PRO A 1 15  ? 11.229 0.470   11.981  1.00  15.63 ? 15  PRO A N   1 
ATOM   90   C  CA  . PRO A 1 15  ? 10.671 -0.507  11.027  1.00  15.56 ? 15  PRO A CA  1 
ATOM   91   C  C   . PRO A 1 15  ? 9.140  -0.454  10.869  1.00  16.85 ? 15  PRO A C   1 
ATOM   92   O  O   . PRO A 1 15  ? 8.637  -0.618  9.751   1.00  15.27 ? 15  PRO A O   1 
ATOM   93   C  CB  . PRO A 1 15  ? 11.098 -1.875  11.637  1.00  17.06 ? 15  PRO A CB  1 
ATOM   94   C  CG  . PRO A 1 15  ? 12.441 -1.575  12.264  1.00  18.40 ? 15  PRO A CG  1 
ATOM   95   C  CD  . PRO A 1 15  ? 12.367 -0.085  12.746  1.00  16.81 ? 15  PRO A CD  1 
ATOM   96   N  N   . ILE A 1 16  ? 8.353  -0.210  11.943  1.00  16.40 ? 16  ILE A N   1 
ATOM   97   C  CA  . ILE A 1 16  ? 6.903  -0.236  11.707  1.00  18.81 ? 16  ILE A CA  1 
ATOM   98   C  C   . ILE A 1 16  ? 6.441  0.950   10.900  1.00  15.71 ? 16  ILE A C   1 
ATOM   99   O  O   . ILE A 1 16  ? 5.355  0.940   10.390  1.00  16.95 ? 16  ILE A O   1 
ATOM   100  C  CB  . ILE A 1 16  ? 6.030  -0.353  12.993  1.00  22.27 ? 16  ILE A CB  1 
ATOM   101  C  CG1 . ILE A 1 16  ? 6.183  0.892   13.860  1.00  25.09 ? 16  ILE A CG1 1 
ATOM   102  C  CG2 . ILE A 1 16  ? 6.297  -1.691  13.751  1.00  27.31 ? 16  ILE A CG2 1 
ATOM   103  C  CD1 . ILE A 1 16  ? 4.910  1.150   14.654  1.00  33.63 ? 16  ILE A CD1 1 
ATOM   104  N  N   . HIS A 1 17  ? 7.256  1.973   10.802  1.00  16.40 ? 17  HIS A N   1 
ATOM   105  C  CA  . HIS A 1 17  ? 6.885  3.180   10.046  1.00  15.95 ? 17  HIS A CA  1 
ATOM   106  C  C   . HIS A 1 17  ? 7.394  3.181   8.615   1.00  14.95 ? 17  HIS A C   1 
ATOM   107  O  O   . HIS A 1 17  ? 6.972  4.015   7.855   1.00  13.32 ? 17  HIS A O   1 
ATOM   108  C  CB  . HIS A 1 17  ? 7.445  4.434   10.680  1.00  17.33 ? 17  HIS A CB  1 
ATOM   109  C  CG  . HIS A 1 17  ? 6.859  4.730   12.038  1.00  19.41 ? 17  HIS A CG  1 
ATOM   110  N  ND1 . HIS A 1 17  ? 5.612  5.208   12.201  1.00  20.24 ? 17  HIS A ND1 1 
ATOM   111  C  CD2 . HIS A 1 17  ? 7.391  4.578   13.320  1.00  20.06 ? 17  HIS A CD2 1 
ATOM   112  C  CE1 . HIS A 1 17  ? 5.360  5.364   13.514  1.00  22.81 ? 17  HIS A CE1 1 
ATOM   113  N  NE2 . HIS A 1 17  ? 6.447  4.980   14.197  1.00  20.03 ? 17  HIS A NE2 1 
ATOM   114  N  N   . TRP A 1 18  ? 8.301  2.282   8.247   1.00  14.98 ? 18  TRP A N   1 
ATOM   115  C  CA  . TRP A 1 18  ? 8.923  2.357   6.891   1.00  14.10 ? 18  TRP A CA  1 
ATOM   116  C  C   . TRP A 1 18  ? 7.919  2.264   5.766   1.00  13.81 ? 18  TRP A C   1 
ATOM   117  O  O   . TRP A 1 18  ? 8.076  2.903   4.700   1.00  14.34 ? 18  TRP A O   1 
ATOM   118  C  CB  . TRP A 1 18  ? 9.940  1.257   6.722   1.00  13.57 ? 18  TRP A CB  1 
ATOM   119  C  CG  . TRP A 1 18  ? 11.132 1.337   7.670   1.00  12.78 ? 18  TRP A CG  1 
ATOM   120  C  CD1 . TRP A 1 18  ? 11.543 2.441   8.461   1.00  14.49 ? 18  TRP A CD1 1 
ATOM   121  C  CD2 . TRP A 1 18  ? 12.157 0.294   7.895   1.00  12.64 ? 18  TRP A CD2 1 
ATOM   122  N  NE1 . TRP A 1 18  ? 12.712 2.168   9.130   1.00  12.55 ? 18  TRP A NE1 1 
ATOM   123  C  CE2 . TRP A 1 18  ? 13.136 0.864   8.822   1.00  12.65 ? 18  TRP A CE2 1 
ATOM   124  C  CE3 . TRP A 1 18  ? 12.358 -1.039  7.418   1.00  13.44 ? 18  TRP A CE3 1 
ATOM   125  C  CZ2 . TRP A 1 18  ? 14.292 0.118   9.258   1.00  11.87 ? 18  TRP A CZ2 1 
ATOM   126  C  CZ3 . TRP A 1 18  ? 13.500 -1.766  7.873   1.00  12.27 ? 18  TRP A CZ3 1 
ATOM   127  C  CH2 . TRP A 1 18  ? 14.424 -1.203  8.806   1.00  12.06 ? 18  TRP A CH2 1 
ATOM   128  N  N   . LYS A 1 19  ? 6.871  1.508   5.982   1.00  13.40 ? 19  LYS A N   1 
ATOM   129  C  CA  . LYS A 1 19  ? 5.798  1.407   4.956   1.00  14.94 ? 19  LYS A CA  1 
ATOM   130  C  C   . LYS A 1 19  ? 5.154  2.759   4.568   1.00  15.43 ? 19  LYS A C   1 
ATOM   131  O  O   . LYS A 1 19  ? 4.531  2.886   3.500   1.00  15.14 ? 19  LYS A O   1 
ATOM   132  C  CB  . LYS A 1 19  ? 4.758  0.437   5.409   1.00  16.50 ? 19  LYS A CB  1 
ATOM   133  C  CG  . LYS A 1 19  ? 4.162  0.830   6.751   1.00  20.91 ? 19  LYS A CG  1 
ATOM   134  C  CD  . LYS A 1 19  ? 2.670  0.925   6.609   1.00  25.83 ? 19  LYS A CD  1 
ATOM   135  C  CE  . LYS A 1 19  ? 1.961  -0.342  6.992   1.00  32.49 ? 19  LYS A CE  1 
ATOM   136  N  NZ  . LYS A 1 19  ? 0.734  -0.504  6.126   1.00  30.05 ? 19  LYS A NZ  1 
ATOM   137  N  N   . GLU A 1 20  ? 5.218  3.743   5.474   1.00  15.50 ? 20  GLU A N   1 
ATOM   138  C  CA  . GLU A 1 20  ? 4.574  5.037   5.205   1.00  16.58 ? 20  GLU A CA  1 
ATOM   139  C  C   . GLU A 1 20  ? 5.308  5.691   4.039   1.00  16.55 ? 20  GLU A C   1 
ATOM   140  O  O   . GLU A 1 20  ? 4.756  6.532   3.345   1.00  17.05 ? 20  GLU A O   1 
ATOM   141  C  CB  . GLU A 1 20  ? 4.618  5.932   6.470   1.00  16.49 ? 20  GLU A CB  1 
ATOM   142  C  CG  . GLU A 1 20  ? 3.914  5.293   7.641   1.00  17.49 ? 20  GLU A CG  1 
ATOM   143  C  CD  . GLU A 1 20  ? 4.242  5.960   8.986   1.00  20.18 ? 20  GLU A CD  1 
ATOM   144  O  OE1 . GLU A 1 20  ? 4.808  7.056   8.988   1.00  20.66 ? 20  GLU A OE1 1 
ATOM   145  O  OE2 . GLU A 1 20  ? 3.907  5.355   10.010  1.00  19.71 ? 20  GLU A OE2 1 
ATOM   146  N  N   . PHE A 1 21  ? 6.575  5.316   3.852   1.00  16.02 ? 21  PHE A N   1 
ATOM   147  C  CA  . PHE A 1 21  ? 7.428  5.895   2.824   1.00  18.65 ? 21  PHE A CA  1 
ATOM   148  C  C   . PHE A 1 21  ? 7.894  4.923   1.761   1.00  17.26 ? 21  PHE A C   1 
ATOM   149  O  O   . PHE A 1 21  ? 8.263  5.370   0.691   1.00  17.88 ? 21  PHE A O   1 
ATOM   150  C  CB  . PHE A 1 21  ? 8.606  6.590   3.497   1.00  23.24 ? 21  PHE A CB  1 
ATOM   151  C  CG  . PHE A 1 21  ? 8.156  7.775   4.338   1.00  27.64 ? 21  PHE A CG  1 
ATOM   152  C  CD1 . PHE A 1 21  ? 7.948  7.635   5.708   1.00  32.90 ? 21  PHE A CD1 1 
ATOM   153  C  CD2 . PHE A 1 21  ? 7.795  8.969   3.721   1.00  29.98 ? 21  PHE A CD2 1 
ATOM   154  C  CE1 . PHE A 1 21  ? 7.445  8.706   6.460   1.00  36.38 ? 21  PHE A CE1 1 
ATOM   155  C  CE2 . PHE A 1 21  ? 7.323  10.044  4.459   1.00  34.60 ? 21  PHE A CE2 1 
ATOM   156  C  CZ  . PHE A 1 21  ? 7.149  9.908   5.832   1.00  34.47 ? 21  PHE A CZ  1 
ATOM   157  N  N   . PHE A 1 22  ? 7.891  3.617   2.075   1.00  15.41 ? 22  PHE A N   1 
ATOM   158  C  CA  . PHE A 1 22  ? 8.346  2.553   1.174   1.00  15.08 ? 22  PHE A CA  1 
ATOM   159  C  C   . PHE A 1 22  ? 7.275  1.448   1.252   1.00  16.63 ? 22  PHE A C   1 
ATOM   160  O  O   . PHE A 1 22  ? 7.324  0.580   2.127   1.00  17.11 ? 22  PHE A O   1 
ATOM   161  C  CB  . PHE A 1 22  ? 9.737  2.046   1.598   1.00  16.22 ? 22  PHE A CB  1 
ATOM   162  C  CG  . PHE A 1 22  ? 10.786 3.133   1.717   1.00  15.70 ? 22  PHE A CG  1 
ATOM   163  C  CD1 . PHE A 1 22  ? 11.600 3.458   0.637   1.00  16.47 ? 22  PHE A CD1 1 
ATOM   164  C  CD2 . PHE A 1 22  ? 10.984 3.797   2.922   1.00  16.89 ? 22  PHE A CD2 1 
ATOM   165  C  CE1 . PHE A 1 22  ? 12.555 4.455   0.749   1.00  17.36 ? 22  PHE A CE1 1 
ATOM   166  C  CE2 . PHE A 1 22  ? 11.946 4.790   3.042   1.00  17.11 ? 22  PHE A CE2 1 
ATOM   167  C  CZ  . PHE A 1 22  ? 12.697 5.145   1.935   1.00  19.46 ? 22  PHE A CZ  1 
ATOM   168  N  N   . PRO A 1 23  ? 6.240  1.533   0.377   1.00  15.84 ? 23  PRO A N   1 
ATOM   169  C  CA  . PRO A 1 23  ? 5.126  0.624   0.424   1.00  14.11 ? 23  PRO A CA  1 
ATOM   170  C  C   . PRO A 1 23  ? 5.544  -0.819  0.149   1.00  13.85 ? 23  PRO A C   1 
ATOM   171  O  O   . PRO A 1 23  ? 4.825  -1.716  0.521   1.00  14.98 ? 23  PRO A O   1 
ATOM   172  C  CB  . PRO A 1 23  ? 4.158  1.128   -0.670  1.00  15.52 ? 23  PRO A CB  1 
ATOM   173  C  CG  . PRO A 1 23  ? 4.777  2.341   -1.268  1.00  16.87 ? 23  PRO A CG  1 
ATOM   174  C  CD  . PRO A 1 23  ? 6.036  2.700   -0.524  1.00  15.42 ? 23  PRO A CD  1 
ATOM   175  N  N   . ILE A 1 24  ? 6.715  -1.048  -0.437  1.00  12.51 ? 24  ILE A N   1 
ATOM   176  C  CA  . ILE A 1 24  ? 7.132  -2.394  -0.650  1.00  13.04 ? 24  ILE A CA  1 
ATOM   177  C  C   . ILE A 1 24  ? 7.460  -3.033  0.740   1.00  12.80 ? 24  ILE A C   1 
ATOM   178  O  O   . ILE A 1 24  ? 7.593  -4.252  0.815   1.00  13.70 ? 24  ILE A O   1 
ATOM   179  C  CB  . ILE A 1 24  ? 8.283  -2.527  -1.670  1.00  12.88 ? 24  ILE A CB  1 
ATOM   180  C  CG1 . ILE A 1 24  ? 8.379  -3.935  -2.264  1.00  14.04 ? 24  ILE A CG1 1 
ATOM   181  C  CG2 . ILE A 1 24  ? 9.592  -2.179  -1.008  1.00  12.89 ? 24  ILE A CG2 1 
ATOM   182  C  CD1 . ILE A 1 24  ? 7.159  -4.316  -3.053  1.00  18.86 ? 24  ILE A CD1 1 
ATOM   183  N  N   . ALA A 1 25  ? 7.483  -2.265  1.840   1.00  12.27 ? 25  ALA A N   1 
ATOM   184  C  CA  . ALA A 1 25  ? 7.670  -2.890  3.218   1.00  13.63 ? 25  ALA A CA  1 
ATOM   185  C  C   . ALA A 1 25  ? 6.663  -4.011  3.519   1.00  14.24 ? 25  ALA A C   1 
ATOM   186  O  O   . ALA A 1 25  ? 6.958  -4.917  4.323   1.00  14.17 ? 25  ALA A O   1 
ATOM   187  C  CB  . ALA A 1 25  ? 7.578  -1.810  4.334   1.00  13.42 ? 25  ALA A CB  1 
ATOM   188  N  N   . ASP A 1 26  ? 5.448  -3.883  2.954   1.00  14.64 ? 26  ASP A N   1 
ATOM   189  C  CA  . ASP A 1 26  ? 4.410  -4.923  2.984   1.00  16.62 ? 26  ASP A CA  1 
ATOM   190  C  C   . ASP A 1 26  ? 4.369  -5.903  1.776   1.00  17.66 ? 26  ASP A C   1 
ATOM   191  O  O   . ASP A 1 26  ? 3.341  -6.588  1.560   1.00  18.02 ? 26  ASP A O   1 
ATOM   192  C  CB  . ASP A 1 26  ? 3.040  -4.262  3.153   1.00  18.13 ? 26  ASP A CB  1 
ATOM   193  C  CG  . ASP A 1 26  ? 2.953  -3.463  4.420   1.00  19.57 ? 26  ASP A CG  1 
ATOM   194  O  OD1 . ASP A 1 26  ? 3.368  -4.013  5.477   1.00  18.56 ? 26  ASP A OD1 1 
ATOM   195  O  OD2 . ASP A 1 26  ? 2.455  -2.309  4.367   1.00  21.30 ? 26  ASP A OD2 1 
ATOM   196  N  N   . GLY A 1 27  ? 5.487  -6.066  1.071   1.00  17.09 ? 27  GLY A N   1 
ATOM   197  C  CA  . GLY A 1 27  ? 5.514  -6.873  -0.156  1.00  16.99 ? 27  GLY A CA  1 
ATOM   198  C  C   . GLY A 1 27  ? 5.453  -8.386  0.071   1.00  17.21 ? 27  GLY A C   1 
ATOM   199  O  O   . GLY A 1 27  ? 5.438  -8.837  1.202   1.00  18.68 ? 27  GLY A O   1 
ATOM   200  N  N   . ASP A 1 28  ? 5.364  -9.137  -1.034  1.00  19.13 ? 28  ASP A N   1 
ATOM   201  C  CA  . ASP A 1 28  ? 5.304  -10.617 -1.108  1.00  19.14 ? 28  ASP A CA  1 
ATOM   202  C  C   . ASP A 1 28  ? 6.598  -11.303 -0.640  1.00  16.03 ? 28  ASP A C   1 
ATOM   203  O  O   . ASP A 1 28  ? 6.577  -12.479 -0.300  1.00  15.73 ? 28  ASP A O   1 
ATOM   204  C  CB  . ASP A 1 28  ? 5.264  -11.047 -2.608  1.00  22.08 ? 28  ASP A CB  1 
ATOM   205  C  CG  . ASP A 1 28  ? 3.988  -10.630 -3.358  1.00  30.13 ? 28  ASP A CG  1 
ATOM   206  O  OD1 . ASP A 1 28  ? 2.951  -10.366 -2.673  1.00  25.14 ? 28  ASP A OD1 1 
ATOM   207  O  OD2 . ASP A 1 28  ? 4.041  -10.691 -4.648  1.00  29.41 ? 28  ASP A OD2 1 
ATOM   208  N  N   . GLN A 1 29  ? 7.737  -10.623 -0.708  1.00  12.90 ? 29  GLN A N   1 
ATOM   209  C  CA  . GLN A 1 29  ? 9.033  -11.327 -0.482  1.00  13.24 ? 29  GLN A CA  1 
ATOM   210  C  C   . GLN A 1 29  ? 9.935  -10.475 0.403   1.00  11.93 ? 29  GLN A C   1 
ATOM   211  O  O   . GLN A 1 29  ? 11.062 -10.136 -0.015  1.00  11.44 ? 29  GLN A O   1 
ATOM   212  C  CB  . GLN A 1 29  ? 9.746  -11.652 -1.803  1.00  13.22 ? 29  GLN A CB  1 
ATOM   213  C  CG  . GLN A 1 29  ? 8.940  -12.610 -2.662  1.00  14.91 ? 29  GLN A CG  1 
ATOM   214  C  CD  . GLN A 1 29  ? 9.803  -13.347 -3.690  1.00  16.51 ? 29  GLN A CD  1 
ATOM   215  O  OE1 . GLN A 1 29  ? 10.757 -12.795 -4.244  1.00  15.37 ? 29  GLN A OE1 1 
ATOM   216  N  NE2 . GLN A 1 29  ? 9.506  -14.633 -3.862  1.00  18.75 ? 29  GLN A NE2 1 
ATOM   217  N  N   . GLN A 1 30  ? 9.417  -10.096 1.586   1.00  11.47 ? 30  GLN A N   1 
ATOM   218  C  CA  . GLN A 1 30  ? 10.201 -9.251  2.551   1.00  10.64 ? 30  GLN A CA  1 
ATOM   219  C  C   . GLN A 1 30  ? 11.080 -10.097 3.517   1.00  9.61  ? 30  GLN A C   1 
ATOM   220  O  O   . GLN A 1 30  ? 10.790 -11.265 3.816   1.00  10.20 ? 30  GLN A O   1 
ATOM   221  C  CB  . GLN A 1 30  ? 9.308  -8.306  3.345   1.00  10.10 ? 30  GLN A CB  1 
ATOM   222  C  CG  . GLN A 1 30  ? 8.680  -7.177  2.500   1.00  10.39 ? 30  GLN A CG  1 
ATOM   223  C  CD  . GLN A 1 30  ? 9.721  -6.215  2.028   1.00  10.51 ? 30  GLN A CD  1 
ATOM   224  O  OE1 . GLN A 1 30  ? 10.336 -5.453  2.836   1.00  10.12 ? 30  GLN A OE1 1 
ATOM   225  N  NE2 . GLN A 1 30  ? 9.994  -6.256  0.688   1.00  9.83  ? 30  GLN A NE2 1 
ATOM   226  N  N   . SER A 1 31  ? 12.178 -9.482  3.973   1.00  9.36  ? 31  SER A N   1 
ATOM   227  C  CA  . SER A 1 31  ? 13.191 -10.162 4.829   1.00  8.87  ? 31  SER A CA  1 
ATOM   228  C  C   . SER A 1 31  ? 13.421 -9.262  6.046   1.00  8.95  ? 31  SER A C   1 
ATOM   229  O  O   . SER A 1 31  ? 13.174 -8.049  5.950   1.00  9.95  ? 31  SER A O   1 
ATOM   230  C  CB  . SER A 1 31  ? 14.540 -10.272 4.083   1.00  9.49  ? 31  SER A CB  1 
ATOM   231  O  OG  . SER A 1 31  ? 14.405 -11.237 3.037   1.00  9.34  ? 31  SER A OG  1 
ATOM   232  N  N   . PRO A 1 32  ? 13.937 -9.790  7.180   1.00  9.43  ? 32  PRO A N   1 
ATOM   233  C  CA  . PRO A 1 32  ? 14.321 -11.151 7.466   1.00  9.53  ? 32  PRO A CA  1 
ATOM   234  C  C   . PRO A 1 32  ? 13.081 -12.000 7.719   1.00  10.13 ? 32  PRO A C   1 
ATOM   235  O  O   . PRO A 1 32  ? 11.923 -11.489 7.629   1.00  10.36 ? 32  PRO A O   1 
ATOM   236  C  CB  . PRO A 1 32  ? 15.166 -11.005 8.742   1.00  9.21  ? 32  PRO A CB  1 
ATOM   237  C  CG  . PRO A 1 32  ? 14.466 -9.847  9.493   1.00  10.24 ? 32  PRO A CG  1 
ATOM   238  C  CD  . PRO A 1 32  ? 14.170 -8.881  8.339   1.00  8.97  ? 32  PRO A CD  1 
ATOM   239  N  N   . ILE A 1 33  ? 13.286 -13.294 8.021   1.00  9.81  ? 33  ILE A N   1 
ATOM   240  C  CA  . ILE A 1 33  ? 12.145 -14.214 8.295   1.00  11.42 ? 33  ILE A CA  1 
ATOM   241  C  C   . ILE A 1 33  ? 12.548 -15.107 9.464   1.00  11.45 ? 33  ILE A C   1 
ATOM   242  O  O   . ILE A 1 33  ? 13.712 -15.076 9.887   1.00  11.63 ? 33  ILE A O   1 
ATOM   243  C  CB  . ILE A 1 33  ? 11.723 -15.154 7.116   1.00  11.08 ? 33  ILE A CB  1 
ATOM   244  C  CG1 . ILE A 1 33  ? 12.912 -15.998 6.592   1.00  11.59 ? 33  ILE A CG1 1 
ATOM   245  C  CG2 . ILE A 1 33  ? 11.029 -14.349 5.985   1.00  10.27 ? 33  ILE A CG2 1 
ATOM   246  C  CD1 . ILE A 1 33  ? 12.452 -17.225 5.766   1.00  10.82 ? 33  ILE A CD1 1 
ATOM   247  N  N   . GLU A 1 34  ? 11.581 -15.860 9.991   1.00  13.05 ? 34  GLU A N   1 
ATOM   248  C  CA  . GLU A 1 34  ? 11.891 -16.883 10.943  1.00  14.01 ? 34  GLU A CA  1 
ATOM   249  C  C   . GLU A 1 34  ? 12.124 -18.124 10.131  1.00  14.65 ? 34  GLU A C   1 
ATOM   250  O  O   . GLU A 1 34  ? 11.252 -18.534 9.360   1.00  14.69 ? 34  GLU A O   1 
ATOM   251  C  CB  . GLU A 1 34  ? 10.708 -17.173 11.838  1.00  16.91 ? 34  GLU A CB  1 
ATOM   252  C  CG  . GLU A 1 34  ? 11.069 -18.279 12.825  1.00  18.00 ? 34  GLU A CG  1 
ATOM   253  C  CD  . GLU A 1 34  ? 10.066 -18.456 13.962  1.00  18.83 ? 34  GLU A CD  1 
ATOM   254  O  OE1 . GLU A 1 34  ? 10.437 -19.239 14.855  1.00  18.49 ? 34  GLU A OE1 1 
ATOM   255  O  OE2 . GLU A 1 34  ? 8.992  -17.769 13.990  1.00  20.24 ? 34  GLU A OE2 1 
ATOM   256  N  N   . ILE A 1 35  ? 13.276 -18.729 10.294  1.00  13.88 ? 35  ILE A N   1 
ATOM   257  C  CA  . ILE A 1 35  ? 13.513 -20.041 9.668   1.00  15.86 ? 35  ILE A CA  1 
ATOM   258  C  C   . ILE A 1 35  ? 12.950 -21.148 10.584  1.00  17.52 ? 35  ILE A C   1 
ATOM   259  O  O   . ILE A 1 35  ? 13.379 -21.292 11.736  1.00  17.31 ? 35  ILE A O   1 
ATOM   260  C  CB  . ILE A 1 35  ? 15.013 -20.262 9.401   1.00  14.95 ? 35  ILE A CB  1 
ATOM   261  C  CG1 . ILE A 1 35  ? 15.541 -19.261 8.313   1.00  13.62 ? 35  ILE A CG1 1 
ATOM   262  C  CG2 . ILE A 1 35  ? 15.248 -21.730 8.906   1.00  15.04 ? 35  ILE A CG2 1 
ATOM   263  C  CD1 . ILE A 1 35  ? 16.983 -18.790 8.462   1.00  13.32 ? 35  ILE A CD1 1 
ATOM   264  N  N   . LYS A 1 36  ? 11.936 -21.866 10.084  1.00  19.76 ? 36  LYS A N   1 
ATOM   265  C  CA  . LYS A 1 36  ? 11.300 -22.948 10.879  1.00  22.82 ? 36  LYS A CA  1 
ATOM   266  C  C   . LYS A 1 36  ? 11.733 -24.294 10.322  1.00  25.48 ? 36  LYS A C   1 
ATOM   267  O  O   . LYS A 1 36  ? 11.240 -24.729 9.275   1.00  25.04 ? 36  LYS A O   1 
ATOM   268  C  CB  . LYS A 1 36  ? 9.811  -22.849 10.827  1.00  24.56 ? 36  LYS A CB  1 
ATOM   269  C  CG  . LYS A 1 36  ? 9.295  -21.447 11.114  1.00  27.72 ? 36  LYS A CG  1 
ATOM   270  C  CD  . LYS A 1 36  ? 7.845  -21.292 10.685  1.00  26.93 ? 36  LYS A CD  1 
ATOM   271  C  CE  . LYS A 1 36  ? 7.363  -19.911 11.111  1.00  32.68 ? 36  LYS A CE  1 
ATOM   272  N  NZ  . LYS A 1 36  ? 5.880  -19.814 11.175  1.00  33.68 ? 36  LYS A NZ  1 
ATOM   273  N  N   . THR A 1 37  ? 12.641 -24.946 11.018  1.00  24.54 ? 37  THR A N   1 
ATOM   274  C  CA  . THR A 1 37  ? 13.371 -26.032 10.401  1.00  29.16 ? 37  THR A CA  1 
ATOM   275  C  C   . THR A 1 37  ? 12.517 -27.249 10.071  1.00  34.03 ? 37  THR A C   1 
ATOM   276  O  O   . THR A 1 37  ? 12.963 -28.132 9.338   1.00  32.78 ? 37  THR A O   1 
ATOM   277  C  CB  . THR A 1 37  ? 14.524 -26.452 11.282  1.00  26.91 ? 37  THR A CB  1 
ATOM   278  O  OG1 . THR A 1 37  ? 14.010 -26.811 12.551  1.00  28.96 ? 37  THR A OG1 1 
ATOM   279  C  CG2 . THR A 1 37  ? 15.513 -25.316 11.486  1.00  26.43 ? 37  THR A CG2 1 
ATOM   280  N  N   . LYS A 1 38  ? 11.297 -27.314 10.589  1.00  33.62 ? 38  LYS A N   1 
ATOM   281  C  CA  . LYS A 1 38  ? 10.464 -28.453 10.255  1.00  35.30 ? 38  LYS A CA  1 
ATOM   282  C  C   . LYS A 1 38  ? 9.689  -28.211 8.949   1.00  35.62 ? 38  LYS A C   1 
ATOM   283  O  O   . LYS A 1 38  ? 9.181  -29.144 8.362   1.00  33.19 ? 38  LYS A O   1 
ATOM   284  C  CB  . LYS A 1 38  ? 9.548  -28.836 11.435  1.00  39.84 ? 38  LYS A CB  1 
ATOM   285  C  CG  . LYS A 1 38  ? 8.216  -28.095 11.482  1.00  42.77 ? 38  LYS A CG  1 
ATOM   286  C  CD  . LYS A 1 38  ? 7.263  -28.731 12.480  0.010 41.42 ? 38  LYS A CD  1 
ATOM   287  C  CE  . LYS A 1 38  ? 5.890  -28.081 12.418  0.010 41.63 ? 38  LYS A CE  1 
ATOM   288  N  NZ  . LYS A 1 38  ? 4.909  -28.769 13.302  0.010 41.52 ? 38  LYS A NZ  1 
ATOM   289  N  N   . GLU A 1 39  ? 9.602  -26.956 8.510   1.00  31.82 ? 39  GLU A N   1 
ATOM   290  C  CA  . GLU A 1 39  ? 8.933  -26.615 7.259   1.00  33.69 ? 39  GLU A CA  1 
ATOM   291  C  C   . GLU A 1 39  ? 9.963  -26.460 6.161   1.00  31.60 ? 39  GLU A C   1 
ATOM   292  O  O   . GLU A 1 39  ? 9.624  -26.375 4.983   1.00  38.75 ? 39  GLU A O   1 
ATOM   293  C  CB  . GLU A 1 39  ? 8.134  -25.325 7.416   1.00  36.32 ? 39  GLU A CB  1 
ATOM   294  C  CG  . GLU A 1 39  ? 7.043  -25.414 8.487   1.00  42.92 ? 39  GLU A CG  1 
ATOM   295  C  CD  . GLU A 1 39  ? 6.298  -24.090 8.680   1.00  52.29 ? 39  GLU A CD  1 
ATOM   296  O  OE1 . GLU A 1 39  ? 5.730  -23.903 9.791   1.00  54.49 ? 39  GLU A OE1 1 
ATOM   297  O  OE2 . GLU A 1 39  ? 6.303  -23.219 7.749   1.00  51.47 ? 39  GLU A OE2 1 
ATOM   298  N  N   . VAL A 1 40  ? 11.226 -26.435 6.560   1.00  29.34 ? 40  VAL A N   1 
ATOM   299  C  CA  . VAL A 1 40  ? 12.364 -26.336 5.616   1.00  27.42 ? 40  VAL A CA  1 
ATOM   300  C  C   . VAL A 1 40  ? 12.438 -27.563 4.729   1.00  28.93 ? 40  VAL A C   1 
ATOM   301  O  O   . VAL A 1 40  ? 12.239 -28.688 5.210   1.00  27.62 ? 40  VAL A O   1 
ATOM   302  C  CB  . VAL A 1 40  ? 13.670 -26.098 6.387   1.00  27.87 ? 40  VAL A CB  1 
ATOM   303  C  CG1 . VAL A 1 40  ? 14.909 -26.467 5.575   1.00  28.43 ? 40  VAL A CG1 1 
ATOM   304  C  CG2 . VAL A 1 40  ? 13.730 -24.644 6.770   1.00  27.76 ? 40  VAL A CG2 1 
ATOM   305  N  N   . LYS A 1 41  ? 12.686 -27.349 3.435   1.00  27.41 ? 41  LYS A N   1 
ATOM   306  C  CA  . LYS A 1 41  ? 12.802 -28.456 2.491   1.00  29.91 ? 41  LYS A CA  1 
ATOM   307  C  C   . LYS A 1 41  ? 14.270 -28.766 2.118   1.00  24.41 ? 41  LYS A C   1 
ATOM   308  O  O   . LYS A 1 41  ? 14.922 -27.937 1.515   1.00  23.52 ? 41  LYS A O   1 
ATOM   309  C  CB  . LYS A 1 41  ? 11.958 -28.147 1.229   1.00  30.69 ? 41  LYS A CB  1 
ATOM   310  C  CG  . LYS A 1 41  ? 10.463 -28.369 1.397   1.00  34.95 ? 41  LYS A CG  1 
ATOM   311  C  CD  . LYS A 1 41  ? 9.733  -27.124 1.876   0.010 33.33 ? 41  LYS A CD  1 
ATOM   312  C  CE  . LYS A 1 41  ? 8.241  -27.374 2.035   0.010 33.61 ? 41  LYS A CE  1 
ATOM   313  N  NZ  . LYS A 1 41  ? 7.930  -28.266 3.187   0.010 33.55 ? 41  LYS A NZ  1 
ATOM   314  N  N   . TYR A 1 42  ? 14.797 -29.956 2.450   1.00  26.72 ? 42  TYR A N   1 
ATOM   315  C  CA  . TYR A 1 42  ? 16.105 -30.360 1.913   1.00  27.37 ? 42  TYR A CA  1 
ATOM   316  C  C   . TYR A 1 42  ? 16.011 -30.425 0.367   1.00  28.31 ? 42  TYR A C   1 
ATOM   317  O  O   . TYR A 1 42  ? 14.995 -30.866 -0.152  1.00  29.88 ? 42  TYR A O   1 
ATOM   318  C  CB  . TYR A 1 42  ? 16.605 -31.691 2.530   1.00  32.15 ? 42  TYR A CB  1 
ATOM   319  C  CG  . TYR A 1 42  ? 17.752 -32.276 1.719   1.00  34.29 ? 42  TYR A CG  1 
ATOM   320  C  CD1 . TYR A 1 42  ? 19.014 -31.668 1.735   1.00  33.19 ? 42  TYR A CD1 1 
ATOM   321  C  CD2 . TYR A 1 42  ? 17.569 -33.418 0.884   1.00  34.62 ? 42  TYR A CD2 1 
ATOM   322  C  CE1 . TYR A 1 42  ? 20.053 -32.146 0.959   1.00  34.70 ? 42  TYR A CE1 1 
ATOM   323  C  CE2 . TYR A 1 42  ? 18.619 -33.898 0.091   1.00  35.71 ? 42  TYR A CE2 1 
ATOM   324  C  CZ  . TYR A 1 42  ? 19.857 -33.266 0.134   1.00  37.44 ? 42  TYR A CZ  1 
ATOM   325  O  OH  . TYR A 1 42  ? 20.931 -33.715 -0.617  1.00  37.66 ? 42  TYR A OH  1 
ATOM   326  N  N   . ASP A 1 43  ? 17.021 -29.915 -0.363  1.00  25.00 ? 43  ASP A N   1 
ATOM   327  C  CA  . ASP A 1 43  ? 17.018 -29.846 -1.837  1.00  27.43 ? 43  ASP A CA  1 
ATOM   328  C  C   . ASP A 1 43  ? 18.405 -30.278 -2.408  1.00  28.86 ? 43  ASP A C   1 
ATOM   329  O  O   . ASP A 1 43  ? 19.393 -29.583 -2.245  1.00  22.59 ? 43  ASP A O   1 
ATOM   330  C  CB  . ASP A 1 43  ? 16.640 -28.429 -2.323  1.00  29.05 ? 43  ASP A CB  1 
ATOM   331  C  CG  . ASP A 1 43  ? 16.465 -28.339 -3.836  1.00  30.44 ? 43  ASP A CG  1 
ATOM   332  O  OD1 . ASP A 1 43  ? 16.858 -29.291 -4.571  1.00  31.08 ? 43  ASP A OD1 1 
ATOM   333  O  OD2 . ASP A 1 43  ? 15.976 -27.286 -4.297  1.00  29.08 ? 43  ASP A OD2 1 
ATOM   334  N  N   . SER A 1 44  ? 18.450 -31.451 -3.046  1.00  28.89 ? 44  SER A N   1 
ATOM   335  C  CA  . SER A 1 44  ? 19.687 -32.020 -3.614  1.00  27.87 ? 44  SER A CA  1 
ATOM   336  C  C   . SER A 1 44  ? 20.219 -31.312 -4.855  1.00  31.81 ? 44  SER A C   1 
ATOM   337  O  O   . SER A 1 44  ? 21.362 -31.574 -5.265  1.00  35.48 ? 44  SER A O   1 
ATOM   338  C  CB  . SER A 1 44  ? 19.484 -33.511 -3.923  1.00  30.11 ? 44  SER A CB  1 
ATOM   339  O  OG  . SER A 1 44  ? 18.509 -33.648 -4.952  1.00  29.64 ? 44  SER A OG  1 
ATOM   340  N  N   . SER A 1 45  ? 19.420 -30.449 -5.484  1.00  29.88 ? 45  SER A N   1 
ATOM   341  C  CA  . SER A 1 45  ? 19.937 -29.578 -6.525  1.00  27.42 ? 45  SER A CA  1 
ATOM   342  C  C   . SER A 1 45  ? 20.774 -28.394 -6.015  1.00  27.85 ? 45  SER A C   1 
ATOM   343  O  O   . SER A 1 45  ? 21.472 -27.745 -6.811  1.00  25.01 ? 45  SER A O   1 
ATOM   344  C  CB  . SER A 1 45  ? 18.828 -29.086 -7.455  1.00  28.34 ? 45  SER A CB  1 
ATOM   345  O  OG  . SER A 1 45  ? 18.138 -27.957 -6.914  1.00  30.15 ? 45  SER A OG  1 
ATOM   346  N  N   . LEU A 1 46  ? 20.678 -28.066 -4.715  1.00  23.71 ? 46  LEU A N   1 
ATOM   347  C  CA  . LEU A 1 46  ? 21.525 -27.012 -4.159  1.00  20.26 ? 46  LEU A CA  1 
ATOM   348  C  C   . LEU A 1 46  ? 22.992 -27.395 -4.156  1.00  22.36 ? 46  LEU A C   1 
ATOM   349  O  O   . LEU A 1 46  ? 23.350 -28.421 -3.588  1.00  24.60 ? 46  LEU A O   1 
ATOM   350  C  CB  . LEU A 1 46  ? 21.086 -26.640 -2.731  1.00  19.34 ? 46  LEU A CB  1 
ATOM   351  C  CG  . LEU A 1 46  ? 19.786 -25.793 -2.662  1.00  16.74 ? 46  LEU A CG  1 
ATOM   352  C  CD1 . LEU A 1 46  ? 19.369 -25.601 -1.192  1.00  14.72 ? 46  LEU A CD1 1 
ATOM   353  C  CD2 . LEU A 1 46  ? 19.999 -24.407 -3.341  1.00  15.07 ? 46  LEU A CD2 1 
ATOM   354  N  N   . ARG A 1 47  ? 23.813 -26.571 -4.781  1.00  20.80 ? 47  ARG A N   1 
ATOM   355  C  CA  . ARG A 1 47  ? 25.256 -26.719 -4.735  1.00  23.68 ? 47  ARG A CA  1 
ATOM   356  C  C   . ARG A 1 47  ? 25.904 -26.204 -3.415  1.00  20.55 ? 47  ARG A C   1 
ATOM   357  O  O   . ARG A 1 47  ? 25.369 -25.282 -2.741  1.00  20.33 ? 47  ARG A O   1 
ATOM   358  C  CB  . ARG A 1 47  ? 25.878 -25.968 -5.934  1.00  27.58 ? 47  ARG A CB  1 
ATOM   359  C  CG  . ARG A 1 47  ? 25.915 -26.749 -7.245  1.00  41.02 ? 47  ARG A CG  1 
ATOM   360  C  CD  . ARG A 1 47  ? 24.911 -26.284 -8.289  1.00  49.93 ? 47  ARG A CD  1 
ATOM   361  N  NE  . ARG A 1 47  ? 23.741 -27.164 -8.374  1.00  61.52 ? 47  ARG A NE  1 
ATOM   362  C  CZ  . ARG A 1 47  ? 22.976 -27.315 -9.467  1.00  64.16 ? 47  ARG A CZ  1 
ATOM   363  N  NH1 . ARG A 1 47  ? 23.258 -26.645 -10.584 1.00  59.61 ? 47  ARG A NH1 1 
ATOM   364  N  NH2 . ARG A 1 47  ? 21.926 -28.143 -9.442  1.00  58.81 ? 47  ARG A NH2 1 
ATOM   365  N  N   . PRO A 1 48  ? 27.082 -26.755 -3.063  1.00  19.69 ? 48  PRO A N   1 
ATOM   366  C  CA  . PRO A 1 48  ? 27.843 -26.157 -1.976  1.00  19.06 ? 48  PRO A CA  1 
ATOM   367  C  C   . PRO A 1 48  ? 28.208 -24.746 -2.367  1.00  18.59 ? 48  PRO A C   1 
ATOM   368  O  O   . PRO A 1 48  ? 28.205 -24.380 -3.574  1.00  17.54 ? 48  PRO A O   1 
ATOM   369  C  CB  . PRO A 1 48  ? 29.124 -27.042 -1.876  1.00  19.05 ? 48  PRO A CB  1 
ATOM   370  C  CG  . PRO A 1 48  ? 29.202 -27.726 -3.206  1.00  19.58 ? 48  PRO A CG  1 
ATOM   371  C  CD  . PRO A 1 48  ? 27.791 -27.897 -3.698  1.00  17.74 ? 48  PRO A CD  1 
ATOM   372  N  N   . LEU A 1 49  ? 28.531 -23.922 -1.383  1.00  16.23 ? 49  LEU A N   1 
ATOM   373  C  CA  . LEU A 1 49  ? 28.881 -22.532 -1.725  1.00  16.90 ? 49  LEU A CA  1 
ATOM   374  C  C   . LEU A 1 49  ? 30.337 -22.606 -2.174  1.00  19.24 ? 49  LEU A C   1 
ATOM   375  O  O   . LEU A 1 49  ? 31.082 -23.425 -1.681  1.00  18.83 ? 49  LEU A O   1 
ATOM   376  C  CB  . LEU A 1 49  ? 28.805 -21.601 -0.495  1.00  14.32 ? 49  LEU A CB  1 
ATOM   377  C  CG  . LEU A 1 49  ? 27.396 -21.564 0.113   1.00  13.30 ? 49  LEU A CG  1 
ATOM   378  C  CD1 . LEU A 1 49  ? 27.470 -20.733 1.408   1.00  14.13 ? 49  LEU A CD1 1 
ATOM   379  C  CD2 . LEU A 1 49  ? 26.429 -20.944 -0.954  1.00  14.33 ? 49  LEU A CD2 1 
ATOM   380  N  N   . SER A 1 50  ? 30.738 -21.787 -3.127  1.00  18.67 ? 50  SER A N   1 
ATOM   381  C  CA  . SER A 1 50  ? 32.141 -21.708 -3.458  1.00  20.97 ? 50  SER A CA  1 
ATOM   382  C  C   . SER A 1 50  ? 32.456 -20.246 -3.487  1.00  21.25 ? 50  SER A C   1 
ATOM   383  O  O   . SER A 1 50  ? 31.705 -19.455 -4.043  1.00  19.97 ? 50  SER A O   1 
ATOM   384  C  CB  . SER A 1 50  ? 32.472 -22.429 -4.776  1.00  25.88 ? 50  SER A CB  1 
ATOM   385  O  OG  . SER A 1 50  ? 32.147 -21.658 -5.877  1.00  28.56 ? 50  SER A OG  1 
ATOM   386  N  N   . ILE A 1 51  ? 33.510 -19.887 -2.778  1.00  24.81 ? 51  ILE A N   1 
ATOM   387  C  CA  . ILE A 1 51  ? 33.830 -18.497 -2.456  1.00  25.87 ? 51  ILE A CA  1 
ATOM   388  C  C   . ILE A 1 51  ? 35.270 -18.189 -2.806  1.00  33.03 ? 51  ILE A C   1 
ATOM   389  O  O   . ILE A 1 51  ? 36.158 -18.778 -2.178  1.00  38.02 ? 51  ILE A O   1 
ATOM   390  C  CB  . ILE A 1 51  ? 33.590 -18.219 -0.958  1.00  27.49 ? 51  ILE A CB  1 
ATOM   391  C  CG1 . ILE A 1 51  ? 32.111 -18.371 -0.658  1.00  23.58 ? 51  ILE A CG1 1 
ATOM   392  C  CG2 . ILE A 1 51  ? 34.112 -16.818 -0.609  1.00  33.22 ? 51  ILE A CG2 1 
ATOM   393  C  CD1 . ILE A 1 51  ? 31.653 -18.299 0.761   1.00  28.03 ? 51  ILE A CD1 1 
ATOM   394  N  N   . LYS A 1 52  ? 35.500 -17.382 -3.857  1.00  28.41 ? 52  LYS A N   1 
ATOM   395  C  CA  . LYS A 1 52  ? 36.796 -16.702 -4.064  1.00  33.21 ? 52  LYS A CA  1 
ATOM   396  C  C   . LYS A 1 52  ? 36.797 -15.402 -3.298  1.00  31.52 ? 52  LYS A C   1 
ATOM   397  O  O   . LYS A 1 52  ? 35.827 -14.639 -3.334  1.00  25.88 ? 52  LYS A O   1 
ATOM   398  C  CB  . LYS A 1 52  ? 37.001 -16.272 -5.509  1.00  31.15 ? 52  LYS A CB  1 
ATOM   399  C  CG  . LYS A 1 52  ? 37.642 -17.256 -6.450  1.00  38.22 ? 52  LYS A CG  1 
ATOM   400  C  CD  . LYS A 1 52  ? 38.058 -16.500 -7.707  1.00  42.39 ? 52  LYS A CD  1 
ATOM   401  C  CE  . LYS A 1 52  ? 37.070 -16.761 -8.821  1.00  42.85 ? 52  LYS A CE  1 
ATOM   402  N  NZ  . LYS A 1 52  ? 37.192 -18.188 -9.236  1.00  45.61 ? 52  LYS A NZ  1 
ATOM   403  N  N   . TYR A 1 53  ? 37.926 -15.089 -2.698  1.00  32.81 ? 53  TYR A N   1 
ATOM   404  C  CA  . TYR A 1 53  ? 38.032 -13.857 -1.973  1.00  32.14 ? 53  TYR A CA  1 
ATOM   405  C  C   . TYR A 1 53  ? 39.485 -13.343 -1.897  1.00  34.41 ? 53  TYR A C   1 
ATOM   406  O  O   . TYR A 1 53  ? 40.446 -14.126 -1.793  1.00  37.28 ? 53  TYR A O   1 
ATOM   407  C  CB  . TYR A 1 53  ? 37.385 -13.987 -0.594  1.00  29.54 ? 53  TYR A CB  1 
ATOM   408  C  CG  . TYR A 1 53  ? 37.613 -12.751 0.212   1.00  28.10 ? 53  TYR A CG  1 
ATOM   409  C  CD1 . TYR A 1 53  ? 36.869 -11.603 -0.043  1.00  26.68 ? 53  TYR A CD1 1 
ATOM   410  C  CD2 . TYR A 1 53  ? 38.599 -12.692 1.192   1.00  26.38 ? 53  TYR A CD2 1 
ATOM   411  C  CE1 . TYR A 1 53  ? 37.089 -10.441 0.653   1.00  21.91 ? 53  TYR A CE1 1 
ATOM   412  C  CE2 . TYR A 1 53  ? 38.801 -11.527 1.910   1.00  26.67 ? 53  TYR A CE2 1 
ATOM   413  C  CZ  . TYR A 1 53  ? 38.016 -10.399 1.646   1.00  25.34 ? 53  TYR A CZ  1 
ATOM   414  O  OH  . TYR A 1 53  ? 38.201 -9.190  2.335   1.00  25.08 ? 53  TYR A OH  1 
ATOM   415  N  N   . ASP A 1 54  ? 39.614 -12.033 -2.005  1.00  28.23 ? 54  ASP A N   1 
ATOM   416  C  CA  . ASP A 1 54  ? 40.885 -11.371 -2.004  1.00  28.19 ? 54  ASP A CA  1 
ATOM   417  C  C   . ASP A 1 54  ? 40.870 -10.318 -0.916  1.00  26.50 ? 54  ASP A C   1 
ATOM   418  O  O   . ASP A 1 54  ? 40.180 -9.321  -1.034  1.00  24.66 ? 54  ASP A O   1 
ATOM   419  C  CB  . ASP A 1 54  ? 41.134 -10.705 -3.340  1.00  31.55 ? 54  ASP A CB  1 
ATOM   420  C  CG  . ASP A 1 54  ? 42.550 -10.217 -3.504  1.00  35.27 ? 54  ASP A CG  1 
ATOM   421  O  OD1 . ASP A 1 54  ? 43.294 -10.050 -2.504  1.00  36.45 ? 54  ASP A OD1 1 
ATOM   422  O  OD2 . ASP A 1 54  ? 42.926 -9.984  -4.679  1.00  40.52 ? 54  ASP A OD2 1 
ATOM   423  N  N   . PRO A 1 55  ? 41.676 -10.520 0.126   1.00  26.35 ? 55  PRO A N   1 
ATOM   424  C  CA  . PRO A 1 55  ? 41.764 -9.605  1.269   1.00  26.33 ? 55  PRO A CA  1 
ATOM   425  C  C   . PRO A 1 55  ? 42.173 -8.181  0.902   1.00  24.87 ? 55  PRO A C   1 
ATOM   426  O  O   . PRO A 1 55  ? 41.741 -7.271  1.590   1.00  24.06 ? 55  PRO A O   1 
ATOM   427  C  CB  . PRO A 1 55  ? 42.786 -10.290 2.197   1.00  30.50 ? 55  PRO A CB  1 
ATOM   428  C  CG  . PRO A 1 55  ? 42.712 -11.749 1.829   1.00  29.21 ? 55  PRO A CG  1 
ATOM   429  C  CD  . PRO A 1 55  ? 42.509 -11.717 0.323   1.00  28.38 ? 55  PRO A CD  1 
ATOM   430  N  N   . SER A 1 56  ? 42.955 -7.966  -0.163  1.00  24.01 ? 56  SER A N   1 
ATOM   431  C  CA  . SER A 1 56  ? 43.188 -6.620  -0.673  1.00  25.10 ? 56  SER A CA  1 
ATOM   432  C  C   . SER A 1 56  ? 41.951 -6.016  -1.389  1.00  24.92 ? 56  SER A C   1 
ATOM   433  O  O   . SER A 1 56  ? 41.985 -4.832  -1.740  1.00  22.78 ? 56  SER A O   1 
ATOM   434  C  CB  . SER A 1 56  ? 44.396 -6.564  -1.644  1.00  29.53 ? 56  SER A CB  1 
ATOM   435  O  OG  . SER A 1 56  ? 44.068 -7.302  -2.826  1.00  36.19 ? 56  SER A OG  1 
ATOM   436  N  N   . SER A 1 57  ? 40.888 -6.804  -1.622  1.00  22.73 ? 57  SER A N   1 
ATOM   437  C  CA  . SER A 1 57  ? 39.640 -6.244  -2.236  1.00  25.82 ? 57  SER A CA  1 
ATOM   438  C  C   . SER A 1 57  ? 39.012 -5.212  -1.297  1.00  24.69 ? 57  SER A C   1 
ATOM   439  O  O   . SER A 1 57  ? 38.323 -4.315  -1.756  1.00  25.45 ? 57  SER A O   1 
ATOM   440  C  CB  . SER A 1 57  ? 38.577 -7.330  -2.390  1.00  25.01 ? 57  SER A CB  1 
ATOM   441  O  OG  . SER A 1 57  ? 38.917 -8.079  -3.511  1.00  34.82 ? 57  SER A OG  1 
ATOM   442  N  N   . ALA A 1 58  ? 39.184 -5.391  0.024   1.00  23.12 ? 58  ALA A N   1 
ATOM   443  C  CA  . ALA A 1 58  ? 38.565 -4.457  0.979   1.00  22.32 ? 58  ALA A CA  1 
ATOM   444  C  C   . ALA A 1 58  ? 39.213 -3.090  0.796   1.00  20.43 ? 58  ALA A C   1 
ATOM   445  O  O   . ALA A 1 58  ? 40.399 -3.023  0.626   1.00  20.05 ? 58  ALA A O   1 
ATOM   446  C  CB  . ALA A 1 58  ? 38.716 -4.944  2.412   1.00  21.51 ? 58  ALA A CB  1 
ATOM   447  N  N   . LYS A 1 59  ? 38.436 -1.994  0.820   1.00  19.93 ? 59  LYS A N   1 
ATOM   448  C  CA  . LYS A 1 59  ? 39.061 -0.699  0.661   1.00  20.15 ? 59  LYS A CA  1 
ATOM   449  C  C   . LYS A 1 59  ? 38.831 0.292   1.814   1.00  19.82 ? 59  LYS A C   1 
ATOM   450  O  O   . LYS A 1 59  ? 39.783 1.005   2.225   1.00  20.15 ? 59  LYS A O   1 
ATOM   451  C  CB  . LYS A 1 59  ? 38.856 -0.117  -0.773  1.00  22.32 ? 59  LYS A CB  1 
ATOM   452  C  CG  . LYS A 1 59  ? 37.456 0.315   -1.088  1.00  26.00 ? 59  LYS A CG  1 
ATOM   453  C  CD  . LYS A 1 59  ? 37.255 0.601   -2.599  1.00  27.65 ? 59  LYS A CD  1 
ATOM   454  C  CE  . LYS A 1 59  ? 35.763 0.458   -2.880  1.00  23.99 ? 59  LYS A CE  1 
ATOM   455  N  NZ  . LYS A 1 59  ? 35.153 1.404   -3.857  1.00  26.77 ? 59  LYS A NZ  1 
ATOM   456  N  N   . ILE A 1 60  ? 37.598 0.330   2.349   1.00  18.95 ? 60  ILE A N   1 
ATOM   457  C  CA  . ILE A 1 60  ? 37.281 1.283   3.432   1.00  20.51 ? 60  ILE A CA  1 
ATOM   458  C  C   . ILE A 1 60  ? 36.181 0.760   4.327   1.00  15.81 ? 60  ILE A C   1 
ATOM   459  O  O   . ILE A 1 60  ? 35.395 -0.131  3.947   1.00  16.34 ? 60  ILE A O   1 
ATOM   460  C  CB  . ILE A 1 60  ? 36.809 2.719   2.925   1.00  24.87 ? 60  ILE A CB  1 
ATOM   461  C  CG1 . ILE A 1 60  ? 35.997 2.627   1.647   1.00  28.51 ? 60  ILE A CG1 1 
ATOM   462  C  CG2 . ILE A 1 60  ? 37.955 3.768   2.846   1.00  29.02 ? 60  ILE A CG2 1 
ATOM   463  C  CD1 . ILE A 1 60  ? 34.533 2.725   1.907   1.00  30.06 ? 60  ILE A CD1 1 
ATOM   464  N  N   . ILE A 1 61  ? 36.106 1.351   5.500   1.00  15.53 ? 61  ILE A N   1 
ATOM   465  C  CA  . ILE A 1 61  ? 34.947 1.162   6.406   1.00  14.36 ? 61  ILE A CA  1 
ATOM   466  C  C   . ILE A 1 61  ? 34.324 2.526   6.744   1.00  14.22 ? 61  ILE A C   1 
ATOM   467  O  O   . ILE A 1 61  ? 35.016 3.517   6.985   1.00  14.14 ? 61  ILE A O   1 
ATOM   468  C  CB  . ILE A 1 61  ? 35.360 0.381   7.708   1.00  15.21 ? 61  ILE A CB  1 
ATOM   469  C  CG1 . ILE A 1 61  ? 34.129 -0.051  8.523   1.00  13.99 ? 61  ILE A CG1 1 
ATOM   470  C  CG2 . ILE A 1 61  ? 36.307 1.193   8.596   1.00  14.91 ? 61  ILE A CG2 1 
ATOM   471  C  CD1 . ILE A 1 61  ? 34.532 -1.049  9.629   1.00  14.95 ? 61  ILE A CD1 1 
ATOM   472  N  N   . SER A 1 62  ? 33.003 2.554   6.783   1.00  15.83 ? 62  SER A N   1 
ATOM   473  C  CA  . SER A 1 62  ? 32.344 3.803   7.114   1.00  17.21 ? 62  SER A CA  1 
ATOM   474  C  C   . SER A 1 62  ? 31.130 3.529   7.983   1.00  15.45 ? 62  SER A C   1 
ATOM   475  O  O   . SER A 1 62  ? 30.567 2.423   7.962   1.00  15.19 ? 62  SER A O   1 
ATOM   476  C  CB  . SER A 1 62  ? 31.913 4.598   5.828   1.00  18.71 ? 62  SER A CB  1 
ATOM   477  O  OG  . SER A 1 62  ? 30.935 3.861   5.167   1.00  20.50 ? 62  SER A OG  1 
ATOM   478  N  N   . ASN A 1 63  ? 30.674 4.589   8.605   1.00  14.00 ? 63  ASN A N   1 
ATOM   479  C  CA  . ASN A 1 63  ? 29.411 4.575   9.341   1.00  14.16 ? 63  ASN A CA  1 
ATOM   480  C  C   . ASN A 1 63  ? 28.308 5.149   8.472   1.00  15.24 ? 63  ASN A C   1 
ATOM   481  O  O   . ASN A 1 63  ? 28.283 6.349   8.133   1.00  15.37 ? 63  ASN A O   1 
ATOM   482  C  CB  . ASN A 1 63  ? 29.583 5.379   10.633  1.00  13.20 ? 63  ASN A CB  1 
ATOM   483  C  CG  . ASN A 1 63  ? 28.307 5.455   11.439  1.00  14.92 ? 63  ASN A CG  1 
ATOM   484  O  OD1 . ASN A 1 63  ? 27.270 4.942   11.008  1.00  15.96 ? 63  ASN A OD1 1 
ATOM   485  N  ND2 . ASN A 1 63  ? 28.358 6.139   12.599  1.00  13.53 ? 63  ASN A ND2 1 
ATOM   486  N  N   . SER A 1 64  ? 27.370 4.293   8.121   1.00  14.52 ? 64  SER A N   1 
ATOM   487  C  CA  . SER A 1 64  ? 26.280 4.716   7.257   1.00  15.94 ? 64  SER A CA  1 
ATOM   488  C  C   . SER A 1 64  ? 25.204 5.445   8.025   1.00  15.43 ? 64  SER A C   1 
ATOM   489  O  O   . SER A 1 64  ? 24.294 5.991   7.443   1.00  15.88 ? 64  SER A O   1 
ATOM   490  C  CB  . SER A 1 64  ? 25.670 3.497   6.559   1.00  15.13 ? 64  SER A CB  1 
ATOM   491  O  OG  . SER A 1 64  ? 24.961 2.661   7.478   1.00  15.15 ? 64  SER A OG  1 
ATOM   492  N  N   . GLY A 1 65  ? 25.293 5.398   9.345   1.00  15.56 ? 65  GLY A N   1 
ATOM   493  C  CA  . GLY A 1 65  ? 24.196 5.817   10.199  1.00  14.89 ? 65  GLY A CA  1 
ATOM   494  C  C   . GLY A 1 65  ? 23.280 4.671   10.564  1.00  14.67 ? 65  GLY A C   1 
ATOM   495  O  O   . GLY A 1 65  ? 22.417 4.793   11.468  1.00  13.29 ? 65  GLY A O   1 
ATOM   496  N  N   . HIS A 1 66  ? 23.430 3.565   9.841   1.00  13.61 ? 66  HIS A N   1 
ATOM   497  C  CA  . HIS A 1 66  ? 22.564 2.394   10.054  1.00  13.82 ? 66  HIS A CA  1 
ATOM   498  C  C   . HIS A 1 66  ? 23.306 1.186   10.455  1.00  13.93 ? 66  HIS A C   1 
ATOM   499  O  O   . HIS A 1 66  ? 22.722 0.237   10.961  1.00  13.96 ? 66  HIS A O   1 
ATOM   500  C  CB  . HIS A 1 66  ? 21.766 2.099   8.764   1.00  15.52 ? 66  HIS A CB  1 
ATOM   501  C  CG  . HIS A 1 66  ? 21.066 3.333   8.223   1.00  18.54 ? 66  HIS A CG  1 
ATOM   502  N  ND1 . HIS A 1 66  ? 21.374 3.888   7.036   1.00  20.18 ? 66  HIS A ND1 1 
ATOM   503  C  CD2 . HIS A 1 66  ? 20.088 4.151   8.795   1.00  18.58 ? 66  HIS A CD2 1 
ATOM   504  C  CE1 . HIS A 1 66  ? 20.611 4.985   6.840   1.00  20.41 ? 66  HIS A CE1 1 
ATOM   505  N  NE2 . HIS A 1 66  ? 19.827 5.144   7.918   1.00  21.01 ? 66  HIS A NE2 1 
ATOM   506  N  N   . SER A 1 67  ? 24.617 1.198   10.190  1.00  14.03 ? 67  SER A N   1 
ATOM   507  C  CA  . SER A 1 67  ? 25.516 0.068   10.538  1.00  13.92 ? 67  SER A CA  1 
ATOM   508  C  C   . SER A 1 67  ? 26.874 0.595   10.192  1.00  14.72 ? 67  SER A C   1 
ATOM   509  O  O   . SER A 1 67  ? 26.972 1.757   9.837   1.00  13.90 ? 67  SER A O   1 
ATOM   510  C  CB  . SER A 1 67  ? 25.187 -1.247  9.789   1.00  13.66 ? 67  SER A CB  1 
ATOM   511  O  OG  . SER A 1 67  ? 26.138 -2.214  10.320  1.00  14.11 ? 67  SER A OG  1 
ATOM   512  N  N   . PHE A 1 68  ? 27.941 -0.191  10.379  1.00  15.02 ? 68  PHE A N   1 
ATOM   513  C  CA  . PHE A 1 68  ? 29.183 0.149   9.647   1.00  15.08 ? 68  PHE A CA  1 
ATOM   514  C  C   . PHE A 1 68  ? 29.085 -0.572  8.287   1.00  16.15 ? 68  PHE A C   1 
ATOM   515  O  O   . PHE A 1 68  ? 28.364 -1.604  8.229   1.00  16.96 ? 68  PHE A O   1 
ATOM   516  C  CB  . PHE A 1 68  ? 30.459 -0.389  10.422  1.00  14.56 ? 68  PHE A CB  1 
ATOM   517  C  CG  . PHE A 1 68  ? 30.577 -1.930  10.450  1.00  14.54 ? 68  PHE A CG  1 
ATOM   518  C  CD1 . PHE A 1 68  ? 30.033 -2.671  11.495  1.00  14.23 ? 68  PHE A CD1 1 
ATOM   519  C  CD2 . PHE A 1 68  ? 31.203 -2.647  9.390   1.00  15.48 ? 68  PHE A CD2 1 
ATOM   520  C  CE1 . PHE A 1 68  ? 30.150 -4.069  11.497  1.00  13.48 ? 68  PHE A CE1 1 
ATOM   521  C  CE2 . PHE A 1 68  ? 31.256 -4.054  9.353   1.00  14.15 ? 68  PHE A CE2 1 
ATOM   522  C  CZ  . PHE A 1 68  ? 30.759 -4.757  10.431  1.00  14.34 ? 68  PHE A CZ  1 
ATOM   523  N  N   A ASN A 1 69  ? 29.815 -0.102  7.249   0.50  15.41 ? 69  ASN A N   1 
ATOM   524  N  N   B ASN A 1 69  ? 29.793 -0.131  7.232   0.50  14.81 ? 69  ASN A N   1 
ATOM   525  C  CA  A ASN A 1 69  ? 29.966 -0.865  6.005   0.50  16.74 ? 69  ASN A CA  1 
ATOM   526  C  CA  B ASN A 1 69  ? 29.915 -1.005  6.063   0.50  15.59 ? 69  ASN A CA  1 
ATOM   527  C  C   A ASN A 1 69  ? 31.423 -0.978  5.628   0.50  16.04 ? 69  ASN A C   1 
ATOM   528  C  C   B ASN A 1 69  ? 31.335 -1.000  5.529   0.50  15.30 ? 69  ASN A C   1 
ATOM   529  O  O   A ASN A 1 69  ? 32.113 0.026   5.605   0.50  15.78 ? 69  ASN A O   1 
ATOM   530  O  O   B ASN A 1 69  ? 31.927 0.046   5.362   0.50  14.95 ? 69  ASN A O   1 
ATOM   531  C  CB  A ASN A 1 69  ? 29.331 -0.175  4.796   0.50  19.95 ? 69  ASN A CB  1 
ATOM   532  C  CB  B ASN A 1 69  ? 28.919 -0.685  4.931   0.50  17.46 ? 69  ASN A CB  1 
ATOM   533  C  CG  A ASN A 1 69  ? 27.882 0.134   4.982   0.50  21.24 ? 69  ASN A CG  1 
ATOM   534  C  CG  B ASN A 1 69  ? 29.126 0.691   4.357   0.50  18.02 ? 69  ASN A CG  1 
ATOM   535  O  OD1 A ASN A 1 69  ? 27.527 1.286   5.160   0.50  23.83 ? 69  ASN A OD1 1 
ATOM   536  O  OD1 B ASN A 1 69  ? 29.438 0.867   3.169   0.50  19.50 ? 69  ASN A OD1 1 
ATOM   537  N  ND2 A ASN A 1 69  ? 27.025 -0.894  4.941   0.50  22.56 ? 69  ASN A ND2 1 
ATOM   538  N  ND2 B ASN A 1 69  ? 29.005 1.672   5.203   0.50  18.26 ? 69  ASN A ND2 1 
ATOM   539  N  N   . VAL A 1 70  ? 31.876 -2.189  5.324   1.00  15.42 ? 70  VAL A N   1 
ATOM   540  C  CA  . VAL A 1 70  ? 33.158 -2.364  4.667   1.00  15.69 ? 70  VAL A CA  1 
ATOM   541  C  C   . VAL A 1 70  ? 32.812 -2.458  3.141   1.00  15.81 ? 70  VAL A C   1 
ATOM   542  O  O   . VAL A 1 70  ? 32.047 -3.347  2.763   1.00  14.48 ? 70  VAL A O   1 
ATOM   543  C  CB  . VAL A 1 70  ? 33.873 -3.653  5.111   1.00  15.50 ? 70  VAL A CB  1 
ATOM   544  C  CG1 . VAL A 1 70  ? 35.242 -3.731  4.403   1.00  15.79 ? 70  VAL A CG1 1 
ATOM   545  C  CG2 . VAL A 1 70  ? 34.127 -3.587  6.648   1.00  17.26 ? 70  VAL A CG2 1 
ATOM   546  N  N   . ASP A 1 71  ? 33.335 -1.531  2.311   1.00  17.40 ? 71  ASP A N   1 
ATOM   547  C  CA  . ASP A 1 71  ? 33.147 -1.544  0.844   1.00  18.92 ? 71  ASP A CA  1 
ATOM   548  C  C   . ASP A 1 71  ? 34.394 -2.171  0.231   1.00  17.19 ? 71  ASP A C   1 
ATOM   549  O  O   . ASP A 1 71  ? 35.491 -2.043  0.764   1.00  19.65 ? 71  ASP A O   1 
ATOM   550  C  CB  . ASP A 1 71  ? 32.987 -0.132  0.242   1.00  21.23 ? 71  ASP A CB  1 
ATOM   551  C  CG  . ASP A 1 71  ? 31.694 0.582   0.674   1.00  27.34 ? 71  ASP A CG  1 
ATOM   552  O  OD1 . ASP A 1 71  ? 30.671 -0.056  0.966   1.00  28.68 ? 71  ASP A OD1 1 
ATOM   553  O  OD2 . ASP A 1 71  ? 31.715 1.832   0.731   1.00  31.46 ? 71  ASP A OD2 1 
ATOM   554  N  N   . PHE A 1 72  ? 34.206 -2.790  -0.905  1.00  15.60 ? 72  PHE A N   1 
ATOM   555  C  CA  . PHE A 1 72  ? 35.256 -3.518  -1.590  1.00  18.68 ? 72  PHE A CA  1 
ATOM   556  C  C   . PHE A 1 72  ? 35.268 -3.109  -3.058  1.00  18.70 ? 72  PHE A C   1 
ATOM   557  O  O   . PHE A 1 72  ? 34.196 -2.916  -3.655  1.00  16.56 ? 72  PHE A O   1 
ATOM   558  C  CB  . PHE A 1 72  ? 34.921 -5.010  -1.582  1.00  18.14 ? 72  PHE A CB  1 
ATOM   559  C  CG  . PHE A 1 72  ? 34.853 -5.626  -0.204  1.00  17.80 ? 72  PHE A CG  1 
ATOM   560  C  CD1 . PHE A 1 72  ? 33.688 -5.536  0.555   1.00  19.09 ? 72  PHE A CD1 1 
ATOM   561  C  CD2 . PHE A 1 72  ? 35.933 -6.348  0.299   1.00  18.26 ? 72  PHE A CD2 1 
ATOM   562  C  CE1 . PHE A 1 72  ? 33.590 -6.133  1.825   1.00  18.00 ? 72  PHE A CE1 1 
ATOM   563  C  CE2 . PHE A 1 72  ? 35.860 -6.955  1.574   1.00  20.37 ? 72  PHE A CE2 1 
ATOM   564  C  CZ  . PHE A 1 72  ? 34.682 -6.850  2.331   1.00  18.39 ? 72  PHE A CZ  1 
ATOM   565  N  N   . ASP A 1 73  ? 36.457 -3.064  -3.657  1.00  20.48 ? 73  ASP A N   1 
ATOM   566  C  CA  . ASP A 1 73  ? 36.581 -2.936  -5.122  1.00  21.77 ? 73  ASP A CA  1 
ATOM   567  C  C   . ASP A 1 73  ? 35.799 -3.998  -5.832  1.00  19.15 ? 73  ASP A C   1 
ATOM   568  O  O   . ASP A 1 73  ? 35.955 -5.145  -5.575  1.00  22.62 ? 73  ASP A O   1 
ATOM   569  C  CB  . ASP A 1 73  ? 38.025 -3.123  -5.552  1.00  26.05 ? 73  ASP A CB  1 
ATOM   570  C  CG  . ASP A 1 73  ? 38.932 -2.098  -4.962  1.00  35.92 ? 73  ASP A CG  1 
ATOM   571  O  OD1 . ASP A 1 73  ? 40.080 -2.471  -4.571  1.00  41.39 ? 73  ASP A OD1 1 
ATOM   572  O  OD2 . ASP A 1 73  ? 38.488 -0.926  -4.870  1.00  34.90 ? 73  ASP A OD2 1 
ATOM   573  N  N   . ASP A 1 74  ? 34.927 -3.623  -6.744  1.00  20.26 ? 74  ASP A N   1 
ATOM   574  C  CA  . ASP A 1 74  ? 34.115 -4.591  -7.375  1.00  19.84 ? 74  ASP A CA  1 
ATOM   575  C  C   . ASP A 1 74  ? 34.085 -4.370  -8.925  1.00  20.76 ? 74  ASP A C   1 
ATOM   576  O  O   . ASP A 1 74  ? 32.997 -4.403  -9.534  1.00  19.83 ? 74  ASP A O   1 
ATOM   577  C  CB  . ASP A 1 74  ? 32.696 -4.566  -6.786  1.00  20.74 ? 74  ASP A CB  1 
ATOM   578  C  CG  . ASP A 1 74  ? 31.986 -3.242  -7.032  1.00  22.25 ? 74  ASP A CG  1 
ATOM   579  O  OD1 . ASP A 1 74  ? 32.685 -2.219  -7.306  1.00  21.77 ? 74  ASP A OD1 1 
ATOM   580  O  OD2 . ASP A 1 74  ? 30.727 -3.204  -6.964  1.00  21.33 ? 74  ASP A OD2 1 
ATOM   581  N  N   . THR A 1 75  ? 35.272 -4.182  -9.514  1.00  21.04 ? 75  THR A N   1 
ATOM   582  C  CA  . THR A 1 75  ? 35.424 -3.979  -10.970 1.00  21.21 ? 75  THR A CA  1 
ATOM   583  C  C   . THR A 1 75  ? 35.921 -5.299  -11.612 1.00  24.02 ? 75  THR A C   1 
ATOM   584  O  O   . THR A 1 75  ? 35.887 -5.476  -12.849 1.00  22.48 ? 75  THR A O   1 
ATOM   585  C  CB  . THR A 1 75  ? 36.368 -2.790  -11.269 1.00  20.55 ? 75  THR A CB  1 
ATOM   586  O  OG1 . THR A 1 75  ? 37.695 -3.126  -10.885 1.00  20.68 ? 75  THR A OG1 1 
ATOM   587  C  CG2 . THR A 1 75  ? 36.017 -1.503  -10.454 1.00  21.19 ? 75  THR A CG2 1 
ATOM   588  N  N   . GLU A 1 76  ? 36.374 -6.243  -10.771 1.00  22.69 ? 76  GLU A N   1 
ATOM   589  C  CA  . GLU A 1 76  ? 36.928 -7.524  -11.237 1.00  23.42 ? 76  GLU A CA  1 
ATOM   590  C  C   . GLU A 1 76  ? 36.268 -8.697  -10.490 1.00  23.41 ? 76  GLU A C   1 
ATOM   591  O  O   . GLU A 1 76  ? 35.587 -8.492  -9.511  1.00  23.40 ? 76  GLU A O   1 
ATOM   592  C  CB  . GLU A 1 76  ? 38.451 -7.562  -11.027 1.00  25.68 ? 76  GLU A CB  1 
ATOM   593  C  CG  . GLU A 1 76  ? 39.143 -6.296  -11.459 1.00  31.77 ? 76  GLU A CG  1 
ATOM   594  C  CD  . GLU A 1 76  ? 40.614 -6.444  -11.823 1.00  42.08 ? 76  GLU A CD  1 
ATOM   595  O  OE1 . GLU A 1 76  ? 41.310 -7.294  -11.234 1.00  49.10 ? 76  GLU A OE1 1 
ATOM   596  O  OE2 . GLU A 1 76  ? 41.078 -5.684  -12.709 1.00  49.89 ? 76  GLU A OE2 1 
ATOM   597  N  N   . ASN A 1 77  ? 36.464 -9.921  -10.959 1.00  19.18 ? 77  ASN A N   1 
ATOM   598  C  CA  . ASN A 1 77  ? 35.897 -11.042 -10.296 1.00  18.60 ? 77  ASN A CA  1 
ATOM   599  C  C   . ASN A 1 77  ? 36.877 -11.676 -9.326  1.00  17.70 ? 77  ASN A C   1 
ATOM   600  O  O   . ASN A 1 77  ? 36.937 -12.913 -9.242  1.00  19.04 ? 77  ASN A O   1 
ATOM   601  C  CB  . ASN A 1 77  ? 35.340 -12.044 -11.311 1.00  17.71 ? 77  ASN A CB  1 
ATOM   602  C  CG  . ASN A 1 77  ? 34.020 -11.578 -11.899 1.00  16.99 ? 77  ASN A CG  1 
ATOM   603  O  OD1 . ASN A 1 77  ? 33.276 -10.885 -11.232 1.00  15.79 ? 77  ASN A OD1 1 
ATOM   604  N  ND2 . ASN A 1 77  ? 33.722 -11.971 -13.136 1.00  16.76 ? 77  ASN A ND2 1 
ATOM   605  N  N   . LYS A 1 78  ? 37.607 -10.842 -8.584  1.00  18.27 ? 78  LYS A N   1 
ATOM   606  C  CA  . LYS A 1 78  ? 38.545 -11.341 -7.566  1.00  19.25 ? 78  LYS A CA  1 
ATOM   607  C  C   . LYS A 1 78  ? 37.843 -11.852 -6.302  1.00  19.57 ? 78  LYS A C   1 
ATOM   608  O  O   . LYS A 1 78  ? 38.323 -12.802 -5.658  1.00  16.35 ? 78  LYS A O   1 
ATOM   609  C  CB  . LYS A 1 78  ? 39.573 -10.287 -7.225  1.00  24.98 ? 78  LYS A CB  1 
ATOM   610  C  CG  . LYS A 1 78  ? 40.693 -10.182 -8.262  1.00  31.79 ? 78  LYS A CG  1 
ATOM   611  C  CD  . LYS A 1 78  ? 41.638 -9.074  -7.804  1.00  38.65 ? 78  LYS A CD  1 
ATOM   612  C  CE  . LYS A 1 78  ? 42.883 -8.906  -8.662  1.00  48.26 ? 78  LYS A CE  1 
ATOM   613  N  NZ  . LYS A 1 78  ? 43.425 -7.534  -8.395  1.00  55.64 ? 78  LYS A NZ  1 
ATOM   614  N  N   . SER A 1 79  ? 36.699 -11.249 -5.938  1.00  14.50 ? 79  SER A N   1 
ATOM   615  C  CA  . SER A 1 79  ? 35.960 -11.760 -4.729  1.00  15.47 ? 79  SER A CA  1 
ATOM   616  C  C   . SER A 1 79  ? 34.537 -11.994 -5.133  1.00  13.78 ? 79  SER A C   1 
ATOM   617  O  O   . SER A 1 79  ? 33.865 -11.024 -5.506  1.00  14.18 ? 79  SER A O   1 
ATOM   618  C  CB  . SER A 1 79  ? 35.968 -10.758 -3.571  1.00  14.48 ? 79  SER A CB  1 
ATOM   619  O  OG  . SER A 1 79  ? 37.274 -10.291 -3.268  1.00  16.04 ? 79  SER A OG  1 
ATOM   620  N  N   . VAL A 1 80  ? 34.145 -13.260 -5.202  1.00  13.80 ? 80  VAL A N   1 
ATOM   621  C  CA  . VAL A 1 80  ? 32.870 -13.679 -5.760  1.00  14.90 ? 80  VAL A CA  1 
ATOM   622  C  C   . VAL A 1 80  ? 32.286 -14.815 -4.961  1.00  16.13 ? 80  VAL A C   1 
ATOM   623  O  O   . VAL A 1 80  ? 33.004 -15.579 -4.329  1.00  17.88 ? 80  VAL A O   1 
ATOM   624  C  CB  . VAL A 1 80  ? 33.018 -14.131 -7.232  1.00  16.59 ? 80  VAL A CB  1 
ATOM   625  C  CG1 . VAL A 1 80  ? 33.517 -12.985 -8.107  1.00  15.93 ? 80  VAL A CG1 1 
ATOM   626  C  CG2 . VAL A 1 80  ? 34.016 -15.317 -7.356  1.00  19.27 ? 80  VAL A CG2 1 
ATOM   627  N  N   . LEU A 1 81  ? 30.984 -14.938 -5.031  1.00  15.65 ? 81  LEU A N   1 
ATOM   628  C  CA  . LEU A 1 81  ? 30.260 -16.031 -4.511  1.00  15.27 ? 81  LEU A CA  1 
ATOM   629  C  C   . LEU A 1 81  ? 29.562 -16.702 -5.700  1.00  16.25 ? 81  LEU A C   1 
ATOM   630  O  O   . LEU A 1 81  ? 28.933 -16.024 -6.551  1.00  15.25 ? 81  LEU A O   1 
ATOM   631  C  CB  . LEU A 1 81  ? 29.211 -15.556 -3.484  1.00  13.87 ? 81  LEU A CB  1 
ATOM   632  C  CG  . LEU A 1 81  ? 28.167 -16.455 -2.886  1.00  14.28 ? 81  LEU A CG  1 
ATOM   633  C  CD1 . LEU A 1 81  ? 28.836 -17.666 -2.172  1.00  13.74 ? 81  LEU A CD1 1 
ATOM   634  C  CD2 . LEU A 1 81  ? 27.265 -15.578 -1.958  1.00  13.87 ? 81  LEU A CD2 1 
ATOM   635  N  N   A ARG A 1 82  ? 29.669 -18.032 -5.732  0.50  15.75 ? 82  ARG A N   1 
ATOM   636  N  N   B ARG A 1 82  ? 29.722 -18.018 -5.806  0.50  15.57 ? 82  ARG A N   1 
ATOM   637  C  CA  A ARG A 1 82  ? 29.076 -18.874 -6.758  0.50  16.68 ? 82  ARG A CA  1 
ATOM   638  C  CA  B ARG A 1 82  ? 28.958 -18.813 -6.756  0.50  16.41 ? 82  ARG A CA  1 
ATOM   639  C  C   A ARG A 1 82  ? 28.566 -20.128 -6.078  0.50  16.54 ? 82  ARG A C   1 
ATOM   640  C  C   B ARG A 1 82  ? 28.562 -20.113 -6.090  0.50  16.36 ? 82  ARG A C   1 
ATOM   641  O  O   A ARG A 1 82  ? 28.775 -20.329 -4.872  0.50  17.42 ? 82  ARG A O   1 
ATOM   642  O  O   B ARG A 1 82  ? 28.847 -20.329 -4.902  0.50  17.29 ? 82  ARG A O   1 
ATOM   643  C  CB  A ARG A 1 82  ? 30.112 -19.195 -7.870  0.50  18.01 ? 82  ARG A CB  1 
ATOM   644  C  CB  B ARG A 1 82  ? 29.683 -19.010 -8.125  0.50  17.43 ? 82  ARG A CB  1 
ATOM   645  C  CG  A ARG A 1 82  ? 31.001 -17.991 -8.154  0.50  18.73 ? 82  ARG A CG  1 
ATOM   646  C  CG  B ARG A 1 82  ? 31.198 -18.953 -8.085  0.50  18.39 ? 82  ARG A CG  1 
ATOM   647  C  CD  A ARG A 1 82  ? 32.359 -18.329 -8.745  0.50  21.62 ? 82  ARG A CD  1 
ATOM   648  C  CD  B ARG A 1 82  ? 31.807 -18.755 -9.473  0.50  20.17 ? 82  ARG A CD  1 
ATOM   649  N  NE  A ARG A 1 82  ? 33.152 -19.296 -7.977  0.50  24.37 ? 82  ARG A NE  1 
ATOM   650  N  NE  B ARG A 1 82  ? 33.171 -19.289 -9.510  0.50  20.94 ? 82  ARG A NE  1 
ATOM   651  C  CZ  A ARG A 1 82  ? 34.354 -19.709 -8.368  0.50  23.46 ? 82  ARG A CZ  1 
ATOM   652  C  CZ  B ARG A 1 82  ? 33.894 -19.395 -10.618 0.50  22.24 ? 82  ARG A CZ  1 
ATOM   653  N  NH1 A ARG A 1 82  ? 34.862 -19.229 -9.483  0.50  24.11 ? 82  ARG A NH1 1 
ATOM   654  N  NH1 B ARG A 1 82  ? 33.381 -18.998 -11.778 0.50  20.41 ? 82  ARG A NH1 1 
ATOM   655  N  NH2 A ARG A 1 82  ? 35.049 -20.580 -7.657  0.50  25.51 ? 82  ARG A NH2 1 
ATOM   656  N  NH2 B ARG A 1 82  ? 35.118 -19.914 -10.561 0.50  23.09 ? 82  ARG A NH2 1 
ATOM   657  N  N   . GLY A 1 83  ? 27.863 -20.955 -6.841  1.00  16.86 ? 83  GLY A N   1 
ATOM   658  C  CA  . GLY A 1 83  ? 27.343 -22.194 -6.347  1.00  16.35 ? 83  GLY A CA  1 
ATOM   659  C  C   . GLY A 1 83  ? 26.171 -21.872 -5.470  1.00  19.37 ? 83  GLY A C   1 
ATOM   660  O  O   . GLY A 1 83  ? 25.395 -20.898 -5.725  1.00  20.25 ? 83  GLY A O   1 
ATOM   661  N  N   . GLY A 1 84  ? 25.980 -22.686 -4.445  1.00  18.01 ? 84  GLY A N   1 
ATOM   662  C  CA  . GLY A 1 84  ? 24.709 -22.530 -3.691  1.00  18.62 ? 84  GLY A CA  1 
ATOM   663  C  C   . GLY A 1 84  ? 23.460 -22.584 -4.569  1.00  16.85 ? 84  GLY A C   1 
ATOM   664  O  O   . GLY A 1 84  ? 23.411 -23.349 -5.541  1.00  18.94 ? 84  GLY A O   1 
ATOM   665  N  N   . PRO A 1 85  ? 22.457 -21.711 -4.295  1.00  16.12 ? 85  PRO A N   1 
ATOM   666  C  CA  . PRO A 1 85  ? 21.305 -21.634 -5.182  1.00  15.39 ? 85  PRO A CA  1 
ATOM   667  C  C   . PRO A 1 85  ? 21.504 -20.766 -6.431  1.00  14.60 ? 85  PRO A C   1 
ATOM   668  O  O   . PRO A 1 85  ? 20.566 -20.580 -7.186  1.00  14.97 ? 85  PRO A O   1 
ATOM   669  C  CB  . PRO A 1 85  ? 20.253 -20.943 -4.278  1.00  16.11 ? 85  PRO A CB  1 
ATOM   670  C  CG  . PRO A 1 85  ? 21.077 -19.935 -3.558  1.00  15.50 ? 85  PRO A CG  1 
ATOM   671  C  CD  . PRO A 1 85  ? 22.339 -20.750 -3.194  1.00  15.40 ? 85  PRO A CD  1 
ATOM   672  N  N   . LEU A 1 86  ? 22.692 -20.214 -6.631  1.00  15.97 ? 86  LEU A N   1 
ATOM   673  C  CA  . LEU A 1 86  ? 22.879 -19.098 -7.545  1.00  14.67 ? 86  LEU A CA  1 
ATOM   674  C  C   . LEU A 1 86  ? 23.186 -19.590 -8.975  1.00  16.75 ? 86  LEU A C   1 
ATOM   675  O  O   . LEU A 1 86  ? 23.831 -20.599 -9.136  1.00  17.32 ? 86  LEU A O   1 
ATOM   676  C  CB  . LEU A 1 86  ? 24.071 -18.262 -7.067  1.00  14.26 ? 86  LEU A CB  1 
ATOM   677  C  CG  . LEU A 1 86  ? 23.871 -17.703 -5.658  1.00  14.41 ? 86  LEU A CG  1 
ATOM   678  C  CD1 . LEU A 1 86  ? 25.142 -17.008 -5.293  1.00  12.58 ? 86  LEU A CD1 1 
ATOM   679  C  CD2 . LEU A 1 86  ? 22.720 -16.710 -5.560  1.00  13.97 ? 86  LEU A CD2 1 
ATOM   680  N  N   . THR A 1 87  ? 22.704 -18.906 -9.997  1.00  16.30 ? 87  THR A N   1 
ATOM   681  C  CA  . THR A 1 87  ? 23.262 -19.163 -11.324 1.00  17.37 ? 87  THR A CA  1 
ATOM   682  C  C   . THR A 1 87  ? 24.163 -18.025 -11.654 1.00  17.08 ? 87  THR A C   1 
ATOM   683  O  O   . THR A 1 87  ? 23.775 -16.870 -11.501 1.00  19.35 ? 87  THR A O   1 
ATOM   684  C  CB  . THR A 1 87  ? 22.243 -19.557 -12.450 1.00  21.31 ? 87  THR A CB  1 
ATOM   685  O  OG1 . THR A 1 87  ? 22.355 -18.701 -13.609 1.00  24.87 ? 87  THR A OG1 1 
ATOM   686  C  CG2 . THR A 1 87  ? 20.892 -19.737 -12.035 1.00  17.25 ? 87  THR A CG2 1 
ATOM   687  N  N   . GLY A 1 88  ? 25.417 -18.337 -11.969 1.00  17.01 ? 88  GLY A N   1 
ATOM   688  C  CA  . GLY A 1 88  ? 26.360 -17.343 -12.365 1.00  17.47 ? 88  GLY A CA  1 
ATOM   689  C  C   . GLY A 1 88  ? 27.091 -16.798 -11.182 1.00  18.44 ? 88  GLY A C   1 
ATOM   690  O  O   . GLY A 1 88  ? 26.940 -17.345 -10.040 1.00  19.91 ? 88  GLY A O   1 
ATOM   691  N  N   . SER A 1 89  ? 27.835 -15.713 -11.432 1.00  16.00 ? 89  SER A N   1 
ATOM   692  C  CA  . SER A 1 89  ? 28.827 -15.212 -10.457 1.00  16.33 ? 89  SER A CA  1 
ATOM   693  C  C   . SER A 1 89  ? 28.388 -13.909 -9.818  1.00  16.06 ? 89  SER A C   1 
ATOM   694  O  O   . SER A 1 89  ? 28.034 -12.903 -10.521 1.00  14.59 ? 89  SER A O   1 
ATOM   695  C  CB  . SER A 1 89  ? 30.244 -15.169 -11.066 1.00  16.51 ? 89  SER A CB  1 
ATOM   696  O  OG  . SER A 1 89  ? 31.182 -14.488 -10.232 1.00  16.50 ? 89  SER A OG  1 
ATOM   697  N  N   . TYR A 1 90  ? 28.416 -13.922 -8.481  1.00  15.42 ? 90  TYR A N   1 
ATOM   698  C  CA  . TYR A 1 90  ? 27.985 -12.728 -7.698  1.00  15.51 ? 90  TYR A CA  1 
ATOM   699  C  C   . TYR A 1 90  ? 29.150 -12.034 -7.041  1.00  14.41 ? 90  TYR A C   1 
ATOM   700  O  O   . TYR A 1 90  ? 29.849 -12.604 -6.147  1.00  15.36 ? 90  TYR A O   1 
ATOM   701  C  CB  . TYR A 1 90  ? 26.838 -13.082 -6.698  1.00  13.57 ? 90  TYR A CB  1 
ATOM   702  C  CG  . TYR A 1 90  ? 25.495 -13.393 -7.375  1.00  15.57 ? 90  TYR A CG  1 
ATOM   703  C  CD1 . TYR A 1 90  ? 25.312 -14.586 -8.123  1.00  14.90 ? 90  TYR A CD1 1 
ATOM   704  C  CD2 . TYR A 1 90  ? 24.368 -12.508 -7.222  1.00  13.39 ? 90  TYR A CD2 1 
ATOM   705  C  CE1 . TYR A 1 90  ? 24.087 -14.850 -8.754  1.00  14.59 ? 90  TYR A CE1 1 
ATOM   706  C  CE2 . TYR A 1 90  ? 23.134 -12.817 -7.812  1.00  15.14 ? 90  TYR A CE2 1 
ATOM   707  C  CZ  . TYR A 1 90  ? 23.007 -13.957 -8.584  1.00  14.65 ? 90  TYR A CZ  1 
ATOM   708  O  OH  . TYR A 1 90  ? 21.799 -14.255 -9.168  1.00  15.28 ? 90  TYR A OH  1 
ATOM   709  N  N   . ARG A 1 91  ? 29.388 -10.815 -7.495  1.00  12.89 ? 91  ARG A N   1 
ATOM   710  C  CA  . ARG A 1 91  ? 30.521 -10.039 -7.081  1.00  13.26 ? 91  ARG A CA  1 
ATOM   711  C  C   . ARG A 1 91  ? 30.361 -9.356  -5.718  1.00  12.96 ? 91  ARG A C   1 
ATOM   712  O  O   . ARG A 1 91  ? 29.333 -8.726  -5.444  1.00  12.74 ? 91  ARG A O   1 
ATOM   713  C  CB  . ARG A 1 91  ? 30.918 -9.051  -8.183  1.00  14.46 ? 91  ARG A CB  1 
ATOM   714  C  CG  . ARG A 1 91  ? 32.300 -8.418  -7.990  1.00  15.14 ? 91  ARG A CG  1 
ATOM   715  C  CD  . ARG A 1 91  ? 32.569 -7.343  -9.069  1.00  15.62 ? 91  ARG A CD  1 
ATOM   716  N  NE  . ARG A 1 91  ? 32.630 -7.998  -10.381 1.00  15.30 ? 91  ARG A NE  1 
ATOM   717  C  CZ  . ARG A 1 91  ? 32.478 -7.426  -11.569 1.00  16.33 ? 91  ARG A CZ  1 
ATOM   718  N  NH1 . ARG A 1 91  ? 32.255 -6.122  -11.711 1.00  14.46 ? 91  ARG A NH1 1 
ATOM   719  N  NH2 . ARG A 1 91  ? 32.558 -8.217  -12.656 1.00  15.87 ? 91  ARG A NH2 1 
ATOM   720  N  N   . LEU A 1 92  ? 31.374 -9.493  -4.847  1.00  13.59 ? 92  LEU A N   1 
ATOM   721  C  CA  . LEU A 1 92  ? 31.288 -8.937  -3.484  1.00  13.46 ? 92  LEU A CA  1 
ATOM   722  C  C   . LEU A 1 92  ? 31.214 -7.431  -3.559  1.00  15.29 ? 92  LEU A C   1 
ATOM   723  O  O   . LEU A 1 92  ? 32.034 -6.806  -4.240  1.00  12.83 ? 92  LEU A O   1 
ATOM   724  C  CB  . LEU A 1 92  ? 32.542 -9.274  -2.657  1.00  14.47 ? 92  LEU A CB  1 
ATOM   725  C  CG  . LEU A 1 92  ? 32.592 -8.701  -1.228  1.00  14.95 ? 92  LEU A CG  1 
ATOM   726  C  CD1 . LEU A 1 92  ? 31.476 -9.380  -0.390  1.00  14.30 ? 92  LEU A CD1 1 
ATOM   727  C  CD2 . LEU A 1 92  ? 33.959 -9.068  -0.656  1.00  15.01 ? 92  LEU A CD2 1 
ATOM   728  N  N   . ARG A 1 93  ? 30.302 -6.822  -2.773  1.00  14.47 ? 93  ARG A N   1 
ATOM   729  C  CA  . ARG A 1 93  ? 30.196 -5.355  -2.744  1.00  14.51 ? 93  ARG A CA  1 
ATOM   730  C  C   . ARG A 1 93  ? 30.473 -4.777  -1.362  1.00  14.77 ? 93  ARG A C   1 
ATOM   731  O  O   . ARG A 1 93  ? 31.225 -3.810  -1.236  1.00  14.79 ? 93  ARG A O   1 
ATOM   732  C  CB  . ARG A 1 93  ? 28.801 -4.854  -3.227  1.00  19.72 ? 93  ARG A CB  1 
ATOM   733  C  CG  . ARG A 1 93  ? 28.442 -3.471  -2.645  1.00  23.11 ? 93  ARG A CG  1 
ATOM   734  C  CD  . ARG A 1 93  ? 28.063 -2.249  -3.469  1.00  31.44 ? 93  ARG A CD  1 
ATOM   735  N  NE  . ARG A 1 93  ? 28.877 -1.928  -4.603  1.00  34.92 ? 93  ARG A NE  1 
ATOM   736  C  CZ  . ARG A 1 93  ? 29.011 -0.714  -5.148  1.00  31.30 ? 93  ARG A CZ  1 
ATOM   737  N  NH1 . ARG A 1 93  ? 28.446 0.370   -4.648  1.00  33.48 ? 93  ARG A NH1 1 
ATOM   738  N  NH2 . ARG A 1 93  ? 29.729 -0.599  -6.226  1.00  25.75 ? 93  ARG A NH2 1 
ATOM   739  N  N   . GLN A 1 94  ? 29.802 -5.299  -0.313  1.00  14.01 ? 94  GLN A N   1 
ATOM   740  C  CA  . GLN A 1 94  ? 30.044 -4.696  1.016   1.00  14.08 ? 94  GLN A CA  1 
ATOM   741  C  C   . GLN A 1 94  ? 29.696 -5.680  2.122   1.00  13.12 ? 94  GLN A C   1 
ATOM   742  O  O   . GLN A 1 94  ? 29.025 -6.660  1.870   1.00  12.83 ? 94  GLN A O   1 
ATOM   743  C  CB  . GLN A 1 94  ? 29.254 -3.381  1.194   1.00  16.07 ? 94  GLN A CB  1 
ATOM   744  C  CG  . GLN A 1 94  ? 27.768 -3.601  1.041   1.00  19.35 ? 94  GLN A CG  1 
ATOM   745  C  CD  . GLN A 1 94  ? 27.002 -3.083  2.255   1.00  23.84 ? 94  GLN A CD  1 
ATOM   746  O  OE1 . GLN A 1 94  ? 26.954 -3.732  3.268   1.00  27.90 ? 94  GLN A OE1 1 
ATOM   747  N  NE2 . GLN A 1 94  ? 26.423 -1.897  2.143   1.00  26.86 ? 94  GLN A NE2 1 
ATOM   748  N  N   . VAL A 1 95  ? 30.176 -5.412  3.329   1.00  13.21 ? 95  VAL A N   1 
ATOM   749  C  CA  . VAL A 1 95  ? 29.832 -6.261  4.495   1.00  13.86 ? 95  VAL A CA  1 
ATOM   750  C  C   . VAL A 1 95  ? 29.316 -5.311  5.591   1.00  12.84 ? 95  VAL A C   1 
ATOM   751  O  O   . VAL A 1 95  ? 29.853 -4.209  5.748   1.00  13.04 ? 95  VAL A O   1 
ATOM   752  C  CB  . VAL A 1 95  ? 31.110 -6.977  5.010   1.00  13.96 ? 95  VAL A CB  1 
ATOM   753  C  CG1 . VAL A 1 95  ? 30.897 -7.537  6.397   1.00  15.57 ? 95  VAL A CG1 1 
ATOM   754  C  CG2 . VAL A 1 95  ? 31.529 -8.096  4.055   1.00  14.10 ? 95  VAL A CG2 1 
ATOM   755  N  N   . HIS A 1 96  ? 28.290 -5.705  6.340   1.00  12.18 ? 96  HIS A N   1 
ATOM   756  C  CA  . HIS A 1 96  ? 27.853 -4.867  7.465   1.00  11.67 ? 96  HIS A CA  1 
ATOM   757  C  C   . HIS A 1 96  ? 27.289 -5.801  8.550   1.00  12.22 ? 96  HIS A C   1 
ATOM   758  O  O   . HIS A 1 96  ? 27.279 -7.044  8.369   1.00  12.54 ? 96  HIS A O   1 
ATOM   759  C  CB  . HIS A 1 96  ? 26.822 -3.804  6.978   1.00  12.17 ? 96  HIS A CB  1 
ATOM   760  C  CG  . HIS A 1 96  ? 25.589 -4.408  6.341   1.00  12.95 ? 96  HIS A CG  1 
ATOM   761  N  ND1 . HIS A 1 96  ? 25.444 -4.543  4.983   1.00  12.06 ? 96  HIS A ND1 1 
ATOM   762  C  CD2 . HIS A 1 96  ? 24.435 -4.947  6.917   1.00  12.52 ? 96  HIS A CD2 1 
ATOM   763  C  CE1 . HIS A 1 96  ? 24.263 -5.175  4.737   1.00  13.46 ? 96  HIS A CE1 1 
ATOM   764  N  NE2 . HIS A 1 96  ? 23.620 -5.372  5.900   1.00  11.41 ? 96  HIS A NE2 1 
ATOM   765  N  N   . LEU A 1 97  ? 26.779 -5.235  9.660   1.00  10.60 ? 97  LEU A N   1 
ATOM   766  C  CA  . LEU A 1 97  ? 26.359 -6.093  10.780  1.00  10.65 ? 97  LEU A CA  1 
ATOM   767  C  C   . LEU A 1 97  ? 25.052 -5.532  11.398  1.00  10.20 ? 97  LEU A C   1 
ATOM   768  O  O   . LEU A 1 97  ? 24.889 -4.335  11.470  1.00  11.75 ? 97  LEU A O   1 
ATOM   769  C  CB  . LEU A 1 97  ? 27.500 -6.089  11.864  1.00  10.78 ? 97  LEU A CB  1 
ATOM   770  C  CG  . LEU A 1 97  ? 27.206 -6.862  13.167  1.00  11.52 ? 97  LEU A CG  1 
ATOM   771  C  CD1 . LEU A 1 97  ? 27.375 -8.347  12.803  1.00  11.64 ? 97  LEU A CD1 1 
ATOM   772  C  CD2 . LEU A 1 97  ? 28.290 -6.393  14.171  1.00  11.73 ? 97  LEU A CD2 1 
ATOM   773  N  N   . HIS A 1 98  ? 24.196 -6.414  11.932  1.00  10.22 ? 98  HIS A N   1 
ATOM   774  C  CA  . HIS A 1 98  ? 22.996 -5.999  12.657  1.00  10.31 ? 98  HIS A CA  1 
ATOM   775  C  C   . HIS A 1 98  ? 23.101 -6.526  14.090  1.00  10.60 ? 98  HIS A C   1 
ATOM   776  O  O   . HIS A 1 98  ? 23.666 -7.634  14.312  1.00  11.15 ? 98  HIS A O   1 
ATOM   777  C  CB  . HIS A 1 98  ? 21.745 -6.601  11.954  1.00  9.90  ? 98  HIS A CB  1 
ATOM   778  C  CG  . HIS A 1 98  ? 21.550 -6.099  10.524  1.00  10.23 ? 98  HIS A CG  1 
ATOM   779  N  ND1 . HIS A 1 98  ? 20.811 -5.010  10.228  1.00  10.68 ? 98  HIS A ND1 1 
ATOM   780  C  CD2 . HIS A 1 98  ? 22.041 -6.565  9.330   1.00  10.08 ? 98  HIS A CD2 1 
ATOM   781  C  CE1 . HIS A 1 98  ? 20.850 -4.810  8.861   1.00  10.62 ? 98  HIS A CE1 1 
ATOM   782  N  NE2 . HIS A 1 98  ? 21.570 -5.763  8.350   1.00  11.02 ? 98  HIS A NE2 1 
ATOM   783  N  N   . TRP A 1 99  ? 22.662 -5.720  15.053  1.00  10.71 ? 99  TRP A N   1 
ATOM   784  C  CA  . TRP A 1 99  ? 22.607 -6.185  16.465  1.00  11.69 ? 99  TRP A CA  1 
ATOM   785  C  C   . TRP A 1 99  ? 21.425 -5.621  17.135  1.00  10.93 ? 99  TRP A C   1 
ATOM   786  O  O   . TRP A 1 99  ? 20.580 -4.916  16.495  1.00  11.45 ? 99  TRP A O   1 
ATOM   787  C  CB  . TRP A 1 99  ? 23.862 -5.725  17.209  1.00  11.25 ? 99  TRP A CB  1 
ATOM   788  C  CG  . TRP A 1 99  ? 24.059 -4.246  17.024  1.00  12.14 ? 99  TRP A CG  1 
ATOM   789  C  CD1 . TRP A 1 99  ? 23.499 -3.207  17.784  1.00  11.15 ? 99  TRP A CD1 1 
ATOM   790  C  CD2 . TRP A 1 99  ? 24.860 -3.558  15.973  1.00  11.87 ? 99  TRP A CD2 1 
ATOM   791  N  NE1 . TRP A 1 99  ? 23.944 -1.983  17.338  1.00  11.05 ? 99  TRP A NE1 1 
ATOM   792  C  CE2 . TRP A 1 99  ? 24.747 -2.115  16.259  1.00  11.52 ? 99  TRP A CE2 1 
ATOM   793  C  CE3 . TRP A 1 99  ? 25.634 -3.995  14.843  1.00  12.63 ? 99  TRP A CE3 1 
ATOM   794  C  CZ2 . TRP A 1 99  ? 25.373 -1.149  15.483  1.00  11.16 ? 99  TRP A CZ2 1 
ATOM   795  C  CZ3 . TRP A 1 99  ? 26.299 -3.015  14.091  1.00  11.79 ? 99  TRP A CZ3 1 
ATOM   796  C  CH2 . TRP A 1 99  ? 26.116 -1.614  14.356  1.00  12.21 ? 99  TRP A CH2 1 
ATOM   797  N  N   . GLY A 1 100 ? 21.310 -5.907  18.429  1.00  10.42 ? 100 GLY A N   1 
ATOM   798  C  CA  . GLY A 1 100 ? 20.133 -5.400  19.163  1.00  11.61 ? 100 GLY A CA  1 
ATOM   799  C  C   . GLY A 1 100 ? 20.656 -4.731  20.434  1.00  12.50 ? 100 GLY A C   1 
ATOM   800  O  O   . GLY A 1 100 ? 21.901 -4.716  20.651  1.00  13.97 ? 100 GLY A O   1 
ATOM   801  N  N   . SER A 1 101 ? 19.774 -4.188  21.254  1.00  13.05 ? 101 SER A N   1 
ATOM   802  C  CA  . SER A 1 101 ? 20.270 -3.519  22.501  1.00  15.39 ? 101 SER A CA  1 
ATOM   803  C  C   . SER A 1 101 ? 20.660 -4.493  23.613  1.00  16.25 ? 101 SER A C   1 
ATOM   804  O  O   . SER A 1 101 ? 21.254 -4.086  24.640  1.00  15.83 ? 101 SER A O   1 
ATOM   805  C  CB  . SER A 1 101 ? 19.238 -2.502  22.974  1.00  14.94 ? 101 SER A CB  1 
ATOM   806  O  OG  . SER A 1 101 ? 18.077 -3.145  23.518  1.00  16.44 ? 101 SER A OG  1 
ATOM   807  N  N   . ALA A 1 102 ? 20.329 -5.777  23.424  1.00  15.89 ? 102 ALA A N   1 
ATOM   808  C  CA  . ALA A 1 102 ? 20.579 -6.799  24.441  1.00  15.12 ? 102 ALA A CA  1 
ATOM   809  C  C   . ALA A 1 102 ? 21.367 -7.907  23.777  1.00  16.21 ? 102 ALA A C   1 
ATOM   810  O  O   . ALA A 1 102 ? 21.085 -8.233  22.619  1.00  15.30 ? 102 ALA A O   1 
ATOM   811  C  CB  . ALA A 1 102 ? 19.242 -7.311  25.014  1.00  16.55 ? 102 ALA A CB  1 
ATOM   812  N  N   . ASP A 1 103 ? 22.350 -8.482  24.460  1.00  14.03 ? 103 ASP A N   1 
ATOM   813  C  CA  . ASP A 1 103 ? 23.218 -9.484  23.809  1.00  18.02 ? 103 ASP A CA  1 
ATOM   814  C  C   . ASP A 1 103 ? 22.509 -10.727 23.319  1.00  18.70 ? 103 ASP A C   1 
ATOM   815  O  O   . ASP A 1 103 ? 23.122 -11.584 22.672  1.00  20.92 ? 103 ASP A O   1 
ATOM   816  C  CB  . ASP A 1 103 ? 24.395 -9.920  24.701  1.00  16.50 ? 103 ASP A CB  1 
ATOM   817  C  CG  . ASP A 1 103 ? 25.477 -8.845  24.840  1.00  19.30 ? 103 ASP A CG  1 
ATOM   818  O  OD1 . ASP A 1 103 ? 25.355 -7.773  24.231  1.00  17.72 ? 103 ASP A OD1 1 
ATOM   819  O  OD2 . ASP A 1 103 ? 26.496 -9.067  25.521  1.00  19.95 ? 103 ASP A OD2 1 
ATOM   820  N  N   . ASP A 1 104 ? 21.264 -10.909 23.695  1.00  20.49 ? 104 ASP A N   1 
ATOM   821  C  CA  . ASP A 1 104 ? 20.641 -12.203 23.384  1.00  22.76 ? 104 ASP A CA  1 
ATOM   822  C  C   . ASP A 1 104 ? 19.554 -12.097 22.324  1.00  23.78 ? 104 ASP A C   1 
ATOM   823  O  O   . ASP A 1 104 ? 18.842 -13.051 22.100  1.00  22.13 ? 104 ASP A O   1 
ATOM   824  C  CB  . ASP A 1 104 ? 20.075 -12.870 24.654  1.00  25.10 ? 104 ASP A CB  1 
ATOM   825  C  CG  . ASP A 1 104 ? 19.029 -12.047 25.346  1.00  26.77 ? 104 ASP A CG  1 
ATOM   826  O  OD1 . ASP A 1 104 ? 18.928 -10.815 25.136  1.00  27.10 ? 104 ASP A OD1 1 
ATOM   827  O  OD2 . ASP A 1 104 ? 18.306 -12.654 26.158  1.00  29.42 ? 104 ASP A OD2 1 
ATOM   828  N  N   . HIS A 1 105 ? 19.396 -10.909 21.731  1.00  21.31 ? 105 HIS A N   1 
ATOM   829  C  CA  . HIS A 1 105 ? 18.302 -10.667 20.815  1.00  18.66 ? 105 HIS A CA  1 
ATOM   830  C  C   . HIS A 1 105 ? 18.709 -9.600  19.792  1.00  17.61 ? 105 HIS A C   1 
ATOM   831  O  O   . HIS A 1 105 ? 18.171 -8.469  19.817  1.00  18.18 ? 105 HIS A O   1 
ATOM   832  C  CB  . HIS A 1 105 ? 17.091 -10.191 21.638  1.00  21.47 ? 105 HIS A CB  1 
ATOM   833  C  CG  . HIS A 1 105 ? 15.784 -10.243 20.874  1.00  22.88 ? 105 HIS A CG  1 
ATOM   834  N  ND1 . HIS A 1 105 ? 15.000 -11.334 20.866  1.00  27.85 ? 105 HIS A ND1 1 
ATOM   835  C  CD2 . HIS A 1 105 ? 15.145 -9.294  20.071  1.00  24.65 ? 105 HIS A CD2 1 
ATOM   836  C  CE1 . HIS A 1 105 ? 13.914 -11.104 20.105  1.00  23.41 ? 105 HIS A CE1 1 
ATOM   837  N  NE2 . HIS A 1 105 ? 14.003 -9.855  19.618  1.00  23.73 ? 105 HIS A NE2 1 
ATOM   838  N  N   . GLY A 1 106 ? 19.655 -9.923  18.905  1.00  14.48 ? 106 GLY A N   1 
ATOM   839  C  CA  . GLY A 1 106 ? 20.122 -8.918  17.910  1.00  13.38 ? 106 GLY A CA  1 
ATOM   840  C  C   . GLY A 1 106 ? 20.085 -9.319  16.459  1.00  13.82 ? 106 GLY A C   1 
ATOM   841  O  O   . GLY A 1 106 ? 20.223 -8.470  15.575  1.00  12.18 ? 106 GLY A O   1 
ATOM   842  N  N   . SER A 1 107 ? 19.941 -10.615 16.192  1.00  11.99 ? 107 SER A N   1 
ATOM   843  C  CA  . SER A 1 107 ? 19.947 -11.056 14.770  1.00  11.50 ? 107 SER A CA  1 
ATOM   844  C  C   . SER A 1 107 ? 18.687 -10.608 13.981  1.00  11.75 ? 107 SER A C   1 
ATOM   845  O  O   . SER A 1 107 ? 17.660 -10.278 14.579  1.00  11.15 ? 107 SER A O   1 
ATOM   846  C  CB  . SER A 1 107 ? 20.103 -12.580 14.658  1.00  10.21 ? 107 SER A CB  1 
ATOM   847  O  OG  . SER A 1 107 ? 19.035 -13.312 15.311  1.00  10.87 ? 107 SER A OG  1 
ATOM   848  N  N   . GLU A 1 108 ? 18.791 -10.580 12.642  1.00  10.32 ? 108 GLU A N   1 
ATOM   849  C  CA  . GLU A 1 108 ? 17.602 -10.284 11.850  1.00  11.54 ? 108 GLU A CA  1 
ATOM   850  C  C   . GLU A 1 108 ? 16.793 -11.556 11.659  1.00  11.30 ? 108 GLU A C   1 
ATOM   851  O  O   . GLU A 1 108 ? 15.629 -11.633 12.061  1.00  12.22 ? 108 GLU A O   1 
ATOM   852  C  CB  . GLU A 1 108 ? 17.996 -9.636  10.557  1.00  11.17 ? 108 GLU A CB  1 
ATOM   853  C  CG  . GLU A 1 108 ? 18.685 -8.311  10.845  1.00  13.16 ? 108 GLU A CG  1 
ATOM   854  C  CD  . GLU A 1 108 ? 18.363 -7.263  9.757   1.00  13.10 ? 108 GLU A CD  1 
ATOM   855  O  OE1 . GLU A 1 108 ? 18.776 -7.460  8.583   1.00  14.90 ? 108 GLU A OE1 1 
ATOM   856  O  OE2 . GLU A 1 108 ? 17.779 -6.210  10.070  1.00  12.60 ? 108 GLU A OE2 1 
ATOM   857  N  N   . HIS A 1 109 ? 17.391 -12.565 11.035  1.00  11.67 ? 109 HIS A N   1 
ATOM   858  C  CA  . HIS A 1 109 ? 16.737 -13.877 10.959  1.00  12.79 ? 109 HIS A CA  1 
ATOM   859  C  C   . HIS A 1 109 ? 16.669 -14.521 12.325  1.00  12.87 ? 109 HIS A C   1 
ATOM   860  O  O   . HIS A 1 109 ? 17.561 -14.299 13.190  1.00  12.72 ? 109 HIS A O   1 
ATOM   861  C  CB  . HIS A 1 109 ? 17.471 -14.760 9.955   1.00  11.37 ? 109 HIS A CB  1 
ATOM   862  C  CG  . HIS A 1 109 ? 17.394 -14.220 8.545   1.00  11.60 ? 109 HIS A CG  1 
ATOM   863  N  ND1 . HIS A 1 109 ? 18.258 -13.315 8.075   1.00  12.40 ? 109 HIS A ND1 1 
ATOM   864  C  CD2 . HIS A 1 109 ? 16.483 -14.465 7.523   1.00  11.59 ? 109 HIS A CD2 1 
ATOM   865  C  CE1 . HIS A 1 109 ? 17.920 -12.988 6.776   1.00  11.11 ? 109 HIS A CE1 1 
ATOM   866  N  NE2 . HIS A 1 109 ? 16.837 -13.680 6.459   1.00  11.44 ? 109 HIS A NE2 1 
ATOM   867  N  N   . ILE A 1 110 ? 15.628 -15.310 12.561  1.00  13.44 ? 110 ILE A N   1 
ATOM   868  C  CA  . ILE A 1 110 ? 15.604 -16.146 13.805  1.00  14.60 ? 110 ILE A CA  1 
ATOM   869  C  C   . ILE A 1 110 ? 15.415 -17.592 13.379  1.00  15.14 ? 110 ILE A C   1 
ATOM   870  O  O   . ILE A 1 110 ? 14.927 -17.869 12.251  1.00  17.04 ? 110 ILE A O   1 
ATOM   871  C  CB  . ILE A 1 110 ? 14.555 -15.648 14.830  1.00  17.46 ? 110 ILE A CB  1 
ATOM   872  C  CG1 . ILE A 1 110 ? 13.197 -15.757 14.274  1.00  18.97 ? 110 ILE A CG1 1 
ATOM   873  C  CG2 . ILE A 1 110 ? 14.671 -14.136 15.039  1.00  17.46 ? 110 ILE A CG2 1 
ATOM   874  C  CD1 . ILE A 1 110 ? 12.081 -15.561 15.290  1.00  21.05 ? 110 ILE A CD1 1 
ATOM   875  N  N   . VAL A 1 111 ? 15.835 -18.539 14.204  1.00  13.00 ? 111 VAL A N   1 
ATOM   876  C  CA  . VAL A 1 111 ? 15.746 -19.942 13.836  1.00  14.18 ? 111 VAL A CA  1 
ATOM   877  C  C   . VAL A 1 111 ? 14.897 -20.675 14.910  1.00  16.02 ? 111 VAL A C   1 
ATOM   878  O  O   . VAL A 1 111 ? 15.304 -20.725 16.062  1.00  15.63 ? 111 VAL A O   1 
ATOM   879  C  CB  . VAL A 1 111 ? 17.170 -20.602 13.725  1.00  14.43 ? 111 VAL A CB  1 
ATOM   880  C  CG1 . VAL A 1 111 ? 17.011 -22.060 13.272  1.00  14.51 ? 111 VAL A CG1 1 
ATOM   881  C  CG2 . VAL A 1 111 ? 18.075 -19.814 12.747  1.00  14.87 ? 111 VAL A CG2 1 
ATOM   882  N  N   . ASP A 1 112 ? 13.721 -21.166 14.547  1.00  14.78 ? 112 ASP A N   1 
ATOM   883  C  CA  . ASP A 1 112 ? 12.842 -21.857 15.492  1.00  17.76 ? 112 ASP A CA  1 
ATOM   884  C  C   . ASP A 1 112 ? 12.690 -21.065 16.805  1.00  16.67 ? 112 ASP A C   1 
ATOM   885  O  O   . ASP A 1 112 ? 12.962 -21.568 17.881  1.00  16.90 ? 112 ASP A O   1 
ATOM   886  C  CB  . ASP A 1 112 ? 13.449 -23.244 15.787  1.00  21.01 ? 112 ASP A CB  1 
ATOM   887  C  CG  . ASP A 1 112 ? 13.317 -24.213 14.628  1.00  22.92 ? 112 ASP A CG  1 
ATOM   888  O  OD1 . ASP A 1 112 ? 12.376 -24.122 13.810  1.00  24.66 ? 112 ASP A OD1 1 
ATOM   889  O  OD2 . ASP A 1 112 ? 14.170 -25.126 14.587  1.00  29.10 ? 112 ASP A OD2 1 
ATOM   890  N  N   . GLY A 1 113 ? 12.286 -19.821 16.708  1.00  15.65 ? 113 GLY A N   1 
ATOM   891  C  CA  . GLY A 1 113 ? 12.045 -18.993 17.872  1.00  18.97 ? 113 GLY A CA  1 
ATOM   892  C  C   . GLY A 1 113 ? 13.293 -18.324 18.484  1.00  18.58 ? 113 GLY A C   1 
ATOM   893  O  O   . GLY A 1 113 ? 13.178 -17.436 19.361  1.00  20.25 ? 113 GLY A O   1 
ATOM   894  N  N   . VAL A 1 114 ? 14.472 -18.727 18.052  1.00  16.41 ? 114 VAL A N   1 
ATOM   895  C  CA  . VAL A 1 114 ? 15.721 -18.291 18.732  1.00  18.84 ? 114 VAL A CA  1 
ATOM   896  C  C   . VAL A 1 114 ? 16.445 -17.186 17.971  1.00  17.46 ? 114 VAL A C   1 
ATOM   897  O  O   . VAL A 1 114 ? 16.709 -17.360 16.756  1.00  16.16 ? 114 VAL A O   1 
ATOM   898  C  CB  . VAL A 1 114 ? 16.742 -19.457 18.746  1.00  19.78 ? 114 VAL A CB  1 
ATOM   899  C  CG1 . VAL A 1 114 ? 18.147 -18.973 19.197  1.00  19.53 ? 114 VAL A CG1 1 
ATOM   900  C  CG2 . VAL A 1 114 ? 16.244 -20.611 19.597  1.00  20.27 ? 114 VAL A CG2 1 
ATOM   901  N  N   . SER A 1 115 ? 16.816 -16.104 18.663  1.00  16.35 ? 115 SER A N   1 
ATOM   902  C  CA  . SER A 1 115 ? 17.568 -15.024 18.065  1.00  16.93 ? 115 SER A CA  1 
ATOM   903  C  C   . SER A 1 115 ? 19.022 -15.257 18.488  1.00  17.99 ? 115 SER A C   1 
ATOM   904  O  O   . SER A 1 115 ? 19.272 -15.907 19.521  1.00  17.14 ? 115 SER A O   1 
ATOM   905  C  CB  . SER A 1 115 ? 17.167 -13.675 18.623  1.00  18.10 ? 115 SER A CB  1 
ATOM   906  O  OG  . SER A 1 115 ? 15.907 -13.214 18.177  1.00  22.21 ? 115 SER A OG  1 
ATOM   907  N  N   . TYR A 1 116 ? 19.960 -14.713 17.696  1.00  14.74 ? 116 TYR A N   1 
ATOM   908  C  CA  . TYR A 1 116 ? 21.383 -14.727 17.989  1.00  14.53 ? 116 TYR A CA  1 
ATOM   909  C  C   . TYR A 1 116 ? 21.801 -13.343 18.449  1.00  14.15 ? 116 TYR A C   1 
ATOM   910  O  O   . TYR A 1 116 ? 20.977 -12.409 18.439  1.00  15.44 ? 116 TYR A O   1 
ATOM   911  C  CB  . TYR A 1 116 ? 22.173 -15.172 16.725  1.00  13.25 ? 116 TYR A CB  1 
ATOM   912  C  CG  . TYR A 1 116 ? 21.976 -16.631 16.513  1.00  14.42 ? 116 TYR A CG  1 
ATOM   913  C  CD1 . TYR A 1 116 ? 22.801 -17.566 17.150  1.00  14.83 ? 116 TYR A CD1 1 
ATOM   914  C  CD2 . TYR A 1 116 ? 20.926 -17.104 15.723  1.00  15.15 ? 116 TYR A CD2 1 
ATOM   915  C  CE1 . TYR A 1 116 ? 22.629 -18.943 16.968  1.00  16.75 ? 116 TYR A CE1 1 
ATOM   916  C  CE2 . TYR A 1 116 ? 20.700 -18.471 15.573  1.00  18.81 ? 116 TYR A CE2 1 
ATOM   917  C  CZ  . TYR A 1 116 ? 21.568 -19.378 16.187  1.00  19.70 ? 116 TYR A CZ  1 
ATOM   918  O  OH  . TYR A 1 116 ? 21.325 -20.698 15.977  1.00  25.69 ? 116 TYR A OH  1 
ATOM   919  N  N   . ALA A 1 117 ? 23.056 -13.187 18.874  1.00  13.40 ? 117 ALA A N   1 
ATOM   920  C  CA  . ALA A 1 117 ? 23.470 -11.900 19.405  1.00  12.22 ? 117 ALA A CA  1 
ATOM   921  C  C   . ALA A 1 117 ? 23.525 -10.862 18.292  1.00  12.60 ? 117 ALA A C   1 
ATOM   922  O  O   . ALA A 1 117 ? 23.298 -9.666  18.510  1.00  13.40 ? 117 ALA A O   1 
ATOM   923  C  CB  . ALA A 1 117 ? 24.857 -12.001 20.029  1.00  12.33 ? 117 ALA A CB  1 
ATOM   924  N  N   . ALA A 1 118 ? 23.856 -11.323 17.076  1.00  11.59 ? 118 ALA A N   1 
ATOM   925  C  CA  . ALA A 1 118 ? 24.001 -10.390 15.998  1.00  10.93 ? 118 ALA A CA  1 
ATOM   926  C  C   . ALA A 1 118 ? 24.024 -11.160 14.692  1.00  10.58 ? 118 ALA A C   1 
ATOM   927  O  O   . ALA A 1 118 ? 23.808 -12.346 14.680  1.00  10.90 ? 118 ALA A O   1 
ATOM   928  C  CB  . ALA A 1 118 ? 25.266 -9.529  16.167  1.00  10.81 ? 118 ALA A CB  1 
ATOM   929  N  N   . GLU A 1 119 ? 24.165 -10.459 13.567  1.00  11.89 ? 119 GLU A N   1 
ATOM   930  C  CA  . GLU A 1 119 ? 24.087 -11.168 12.304  1.00  11.37 ? 119 GLU A CA  1 
ATOM   931  C  C   . GLU A 1 119 ? 24.856 -10.363 11.258  1.00  11.37 ? 119 GLU A C   1 
ATOM   932  O  O   . GLU A 1 119 ? 24.562 -9.219  11.034  1.00  11.37 ? 119 GLU A O   1 
ATOM   933  C  CB  . GLU A 1 119 ? 22.623 -11.323 11.867  1.00  10.90 ? 119 GLU A CB  1 
ATOM   934  C  CG  . GLU A 1 119 ? 22.440 -12.082 10.522  1.00  11.03 ? 119 GLU A CG  1 
ATOM   935  C  CD  . GLU A 1 119 ? 20.988 -12.313 10.152  1.00  12.43 ? 119 GLU A CD  1 
ATOM   936  O  OE1 . GLU A 1 119 ? 20.137 -12.426 11.067  1.00  11.59 ? 119 GLU A OE1 1 
ATOM   937  O  OE2 . GLU A 1 119 ? 20.684 -12.413 8.928   1.00  13.90 ? 119 GLU A OE2 1 
ATOM   938  N  N   . LEU A 1 120 ? 25.816 -11.003 10.624  1.00  11.85 ? 120 LEU A N   1 
ATOM   939  C  CA  . LEU A 1 120 ? 26.697 -10.343 9.659   1.00  12.40 ? 120 LEU A CA  1 
ATOM   940  C  C   . LEU A 1 120 ? 26.099 -10.557 8.275   1.00  12.97 ? 120 LEU A C   1 
ATOM   941  O  O   . LEU A 1 120 ? 25.632 -11.670 7.978   1.00  12.12 ? 120 LEU A O   1 
ATOM   942  C  CB  . LEU A 1 120 ? 28.122 -10.951 9.721   1.00  13.32 ? 120 LEU A CB  1 
ATOM   943  C  CG  . LEU A 1 120 ? 29.162 -10.323 8.764   1.00  15.61 ? 120 LEU A CG  1 
ATOM   944  C  CD1 . LEU A 1 120 ? 29.692 -9.050  9.424   1.00  15.86 ? 120 LEU A CD1 1 
ATOM   945  C  CD2 . LEU A 1 120 ? 30.317 -11.274 8.606   1.00  18.19 ? 120 LEU A CD2 1 
ATOM   946  N  N   . HIS A 1 121 ? 26.099 -9.485  7.436   1.00  13.60 ? 121 HIS A N   1 
ATOM   947  C  CA  . HIS A 1 121 ? 25.575 -9.624  6.048   1.00  13.31 ? 121 HIS A CA  1 
ATOM   948  C  C   . HIS A 1 121 ? 26.700 -9.338  5.062   1.00  12.76 ? 121 HIS A C   1 
ATOM   949  O  O   . HIS A 1 121 ? 27.503 -8.410  5.228   1.00  12.22 ? 121 HIS A O   1 
ATOM   950  C  CB  . HIS A 1 121 ? 24.333 -8.728  5.764   1.00  13.48 ? 121 HIS A CB  1 
ATOM   951  C  CG  . HIS A 1 121 ? 23.080 -9.182  6.459   1.00  12.79 ? 121 HIS A CG  1 
ATOM   952  N  ND1 . HIS A 1 121 ? 22.004 -8.346  6.697   1.00  11.96 ? 121 HIS A ND1 1 
ATOM   953  C  CD2 . HIS A 1 121 ? 22.777 -10.390 7.069   1.00  11.98 ? 121 HIS A CD2 1 
ATOM   954  C  CE1 . HIS A 1 121 ? 21.080 -9.028  7.369   1.00  11.97 ? 121 HIS A CE1 1 
ATOM   955  N  NE2 . HIS A 1 121 ? 21.542 -10.273 7.600   1.00  12.37 ? 121 HIS A NE2 1 
ATOM   956  N  N   . VAL A 1 122 ? 26.831 -10.227 4.097   1.00  12.25 ? 122 VAL A N   1 
ATOM   957  C  CA  . VAL A 1 122 ? 27.861 -10.049 3.068   1.00  12.64 ? 122 VAL A CA  1 
ATOM   958  C  C   . VAL A 1 122 ? 27.075 -9.959  1.753   1.00  12.07 ? 122 VAL A C   1 
ATOM   959  O  O   . VAL A 1 122 ? 26.498 -10.939 1.320   1.00  10.97 ? 122 VAL A O   1 
ATOM   960  C  CB  . VAL A 1 122 ? 28.783 -11.307 2.922   1.00  12.26 ? 122 VAL A CB  1 
ATOM   961  C  CG1 . VAL A 1 122 ? 29.951 -10.950 1.962   1.00  11.75 ? 122 VAL A CG1 1 
ATOM   962  C  CG2 . VAL A 1 122 ? 29.405 -11.666 4.281   1.00  11.90 ? 122 VAL A CG2 1 
ATOM   963  N  N   . VAL A 1 123 ? 27.166 -8.803  1.114   1.00  12.75 ? 123 VAL A N   1 
ATOM   964  C  CA  . VAL A 1 123 ? 26.250 -8.452  0.023   1.00  11.74 ? 123 VAL A CA  1 
ATOM   965  C  C   . VAL A 1 123 ? 27.013 -8.537  -1.332  1.00  11.24 ? 123 VAL A C   1 
ATOM   966  O  O   . VAL A 1 123 ? 28.123 -8.019  -1.441  1.00  11.29 ? 123 VAL A O   1 
ATOM   967  C  CB  . VAL A 1 123 ? 25.793 -7.008  0.204   1.00  12.82 ? 123 VAL A CB  1 
ATOM   968  C  CG1 . VAL A 1 123 ? 24.937 -6.511  -0.995  1.00  12.10 ? 123 VAL A CG1 1 
ATOM   969  C  CG2 . VAL A 1 123 ? 25.023 -6.878  1.531   1.00  12.70 ? 123 VAL A CG2 1 
ATOM   970  N  N   . HIS A 1 124 ? 26.422 -9.228  -2.300  1.00  11.45 ? 124 HIS A N   1 
ATOM   971  C  CA  . HIS A 1 124 ? 27.040 -9.474  -3.622  1.00  11.84 ? 124 HIS A CA  1 
ATOM   972  C  C   . HIS A 1 124 ? 26.031 -9.151  -4.706  1.00  12.40 ? 124 HIS A C   1 
ATOM   973  O  O   . HIS A 1 124 ? 24.843 -9.215  -4.458  1.00  11.83 ? 124 HIS A O   1 
ATOM   974  C  CB  . HIS A 1 124 ? 27.299 -10.991 -3.759  1.00  12.21 ? 124 HIS A CB  1 
ATOM   975  C  CG  . HIS A 1 124 ? 28.134 -11.608 -2.658  1.00  12.50 ? 124 HIS A CG  1 
ATOM   976  N  ND1 . HIS A 1 124 ? 27.604 -12.039 -1.500  1.00  13.72 ? 124 HIS A ND1 1 
ATOM   977  C  CD2 . HIS A 1 124 ? 29.497 -11.917 -2.601  1.00  12.89 ? 124 HIS A CD2 1 
ATOM   978  C  CE1 . HIS A 1 124 ? 28.575 -12.565 -0.726  1.00  13.43 ? 124 HIS A CE1 1 
ATOM   979  N  NE2 . HIS A 1 124 ? 29.727 -12.491 -1.404  1.00  13.55 ? 124 HIS A NE2 1 
ATOM   980  N  N   . TRP A 1 125 ? 26.505 -8.893  -5.932  1.00  12.46 ? 125 TRP A N   1 
ATOM   981  C  CA  . TRP A 1 125 ? 25.622 -8.572  -7.050  1.00  12.56 ? 125 TRP A CA  1 
ATOM   982  C  C   . TRP A 1 125 ? 25.970 -9.306  -8.304  1.00  11.96 ? 125 TRP A C   1 
ATOM   983  O  O   . TRP A 1 125 ? 27.162 -9.567  -8.535  1.00  12.87 ? 125 TRP A O   1 
ATOM   984  C  CB  . TRP A 1 125 ? 25.630 -7.054  -7.302  1.00  11.37 ? 125 TRP A CB  1 
ATOM   985  C  CG  . TRP A 1 125 ? 26.935 -6.388  -7.610  1.00  12.74 ? 125 TRP A CG  1 
ATOM   986  C  CD1 . TRP A 1 125 ? 27.946 -5.990  -6.748  1.00  11.65 ? 125 TRP A CD1 1 
ATOM   987  C  CD2 . TRP A 1 125 ? 27.377 -5.998  -8.928  1.00  12.76 ? 125 TRP A CD2 1 
ATOM   988  N  NE1 . TRP A 1 125 ? 28.983 -5.406  -7.449  1.00  12.23 ? 125 TRP A NE1 1 
ATOM   989  C  CE2 . TRP A 1 125 ? 28.673 -5.367  -8.770  1.00  13.46 ? 125 TRP A CE2 1 
ATOM   990  C  CE3 . TRP A 1 125 ? 26.805 -6.081  -10.204 1.00  14.73 ? 125 TRP A CE3 1 
ATOM   991  C  CZ2 . TRP A 1 125 ? 29.374 -4.845  -9.855  1.00  13.18 ? 125 TRP A CZ2 1 
ATOM   992  C  CZ3 . TRP A 1 125 ? 27.516 -5.573  -11.271 1.00  12.33 ? 125 TRP A CZ3 1 
ATOM   993  C  CH2 . TRP A 1 125 ? 28.766 -4.951  -11.088 1.00  13.12 ? 125 TRP A CH2 1 
ATOM   994  N  N   . ASN A 1 126 ? 24.981 -9.537  -9.163  1.00  12.81 ? 126 ASN A N   1 
ATOM   995  C  CA  . ASN A 1 126 ? 25.111 -10.457 -10.311 1.00  13.01 ? 126 ASN A CA  1 
ATOM   996  C  C   . ASN A 1 126 ? 25.774 -9.612  -11.428 1.00  13.69 ? 126 ASN A C   1 
ATOM   997  O  O   . ASN A 1 126 ? 25.094 -8.860  -12.153 1.00  12.77 ? 126 ASN A O   1 
ATOM   998  C  CB  . ASN A 1 126 ? 23.705 -11.002 -10.689 1.00  14.62 ? 126 ASN A CB  1 
ATOM   999  C  CG  . ASN A 1 126 ? 23.749 -12.006 -11.843 1.00  13.74 ? 126 ASN A CG  1 
ATOM   1000 O  OD1 . ASN A 1 126 ? 24.733 -12.062 -12.571 1.00  14.14 ? 126 ASN A OD1 1 
ATOM   1001 N  ND2 . ASN A 1 126 ? 22.719 -12.808 -11.986 1.00  15.08 ? 126 ASN A ND2 1 
ATOM   1002 N  N   . SER A 1 127 ? 27.108 -9.610  -11.458 1.00  12.18 ? 127 SER A N   1 
ATOM   1003 C  CA  . SER A 1 127 ? 27.858 -8.945  -12.528 1.00  13.44 ? 127 SER A CA  1 
ATOM   1004 C  C   . SER A 1 127 ? 27.885 -9.690  -13.909 1.00  13.98 ? 127 SER A C   1 
ATOM   1005 O  O   . SER A 1 127 ? 28.331 -9.141  -14.930 1.00  15.55 ? 127 SER A O   1 
ATOM   1006 C  CB  . SER A 1 127 ? 29.280 -8.679  -12.032 1.00  13.15 ? 127 SER A CB  1 
ATOM   1007 O  OG  . SER A 1 127 ? 29.942 -9.895  -11.745 1.00  12.94 ? 127 SER A OG  1 
ATOM   1008 N  N   . ASP A 1 128 ? 27.468 -10.937 -13.928 1.00  14.79 ? 128 ASP A N   1 
ATOM   1009 C  CA  . ASP A 1 128 ? 27.280 -11.663 -15.166 1.00  16.51 ? 128 ASP A CA  1 
ATOM   1010 C  C   . ASP A 1 128 ? 26.094 -11.092 -15.922 1.00  17.76 ? 128 ASP A C   1 
ATOM   1011 O  O   . ASP A 1 128 ? 26.037 -11.253 -17.151 1.00  19.04 ? 128 ASP A O   1 
ATOM   1012 C  CB  . ASP A 1 128 ? 27.007 -13.139 -14.897 1.00  17.42 ? 128 ASP A CB  1 
ATOM   1013 C  CG  . ASP A 1 128 ? 28.296 -13.923 -14.512 1.00  16.61 ? 128 ASP A CG  1 
ATOM   1014 O  OD1 . ASP A 1 128 ? 28.139 -15.098 -14.120 1.00  16.85 ? 128 ASP A OD1 1 
ATOM   1015 O  OD2 . ASP A 1 128 ? 29.396 -13.335 -14.592 1.00  16.03 ? 128 ASP A OD2 1 
ATOM   1016 N  N   . LYS A 1 129 ? 25.127 -10.459 -15.229 1.00  14.80 ? 129 LYS A N   1 
ATOM   1017 C  CA  . LYS A 1 129 ? 23.924 -9.986  -15.941 1.00  16.27 ? 129 LYS A CA  1 
ATOM   1018 C  C   . LYS A 1 129 ? 23.725 -8.461  -15.931 1.00  15.73 ? 129 LYS A C   1 
ATOM   1019 O  O   . LYS A 1 129 ? 23.110 -7.920  -16.830 1.00  16.85 ? 129 LYS A O   1 
ATOM   1020 C  CB  . LYS A 1 129 ? 22.633 -10.667 -15.435 1.00  15.95 ? 129 LYS A CB  1 
ATOM   1021 C  CG  . LYS A 1 129 ? 22.417 -12.094 -15.956 1.00  18.42 ? 129 LYS A CG  1 
ATOM   1022 C  CD  . LYS A 1 129 ? 21.121 -12.689 -15.420 1.00  20.38 ? 129 LYS A CD  1 
ATOM   1023 C  CE  . LYS A 1 129 ? 19.887 -12.005 -16.023 1.00  20.24 ? 129 LYS A CE  1 
ATOM   1024 N  NZ  . LYS A 1 129 ? 18.624 -12.772 -15.682 1.00  22.31 ? 129 LYS A NZ  1 
ATOM   1025 N  N   . TYR A 1 130 ? 24.234 -7.788  -14.902 1.00  16.22 ? 130 TYR A N   1 
ATOM   1026 C  CA  . TYR A 1 130 ? 23.930 -6.383  -14.697 1.00  15.66 ? 130 TYR A CA  1 
ATOM   1027 C  C   . TYR A 1 130 ? 25.196 -5.588  -14.619 1.00  16.63 ? 130 TYR A C   1 
ATOM   1028 O  O   . TYR A 1 130 ? 26.224 -6.132  -14.256 1.00  17.73 ? 130 TYR A O   1 
ATOM   1029 C  CB  . TYR A 1 130 ? 23.072 -6.247  -13.430 1.00  15.67 ? 130 TYR A CB  1 
ATOM   1030 C  CG  . TYR A 1 130 ? 21.840 -7.113  -13.505 1.00  17.44 ? 130 TYR A CG  1 
ATOM   1031 C  CD1 . TYR A 1 130 ? 20.869 -6.909  -14.495 1.00  16.39 ? 130 TYR A CD1 1 
ATOM   1032 C  CD2 . TYR A 1 130 ? 21.677 -8.171  -12.637 1.00  18.06 ? 130 TYR A CD2 1 
ATOM   1033 C  CE1 . TYR A 1 130 ? 19.759 -7.730  -14.598 1.00  17.36 ? 130 TYR A CE1 1 
ATOM   1034 C  CE2 . TYR A 1 130 ? 20.587 -9.015  -12.744 1.00  16.77 ? 130 TYR A CE2 1 
ATOM   1035 C  CZ  . TYR A 1 130 ? 19.613 -8.766  -13.711 1.00  17.69 ? 130 TYR A CZ  1 
ATOM   1036 O  OH  . TYR A 1 130 ? 18.510 -9.601  -13.798 1.00  16.65 ? 130 TYR A OH  1 
ATOM   1037 N  N   . PRO A 1 131 ? 25.144 -4.300  -14.984 1.00  16.43 ? 131 PRO A N   1 
ATOM   1038 C  CA  . PRO A 1 131 ? 26.329 -3.455  -15.122 1.00  17.10 ? 131 PRO A CA  1 
ATOM   1039 C  C   . PRO A 1 131 ? 26.809 -2.873  -13.835 1.00  16.32 ? 131 PRO A C   1 
ATOM   1040 O  O   . PRO A 1 131 ? 27.899 -2.338  -13.764 1.00  14.93 ? 131 PRO A O   1 
ATOM   1041 C  CB  . PRO A 1 131 ? 25.829 -2.282  -15.989 1.00  16.95 ? 131 PRO A CB  1 
ATOM   1042 C  CG  . PRO A 1 131 ? 24.335 -2.199  -15.716 1.00  16.93 ? 131 PRO A CG  1 
ATOM   1043 C  CD  . PRO A 1 131 ? 23.931 -3.652  -15.548 1.00  18.47 ? 131 PRO A CD  1 
ATOM   1044 N  N   . SER A 1 132 ? 25.959 -2.907  -12.818 1.00  16.44 ? 132 SER A N   1 
ATOM   1045 C  CA  . SER A 1 132 ? 26.373 -2.251  -11.569 1.00  15.52 ? 132 SER A CA  1 
ATOM   1046 C  C   . SER A 1 132 ? 25.578 -2.818  -10.413 1.00  15.37 ? 132 SER A C   1 
ATOM   1047 O  O   . SER A 1 132 ? 24.505 -3.398  -10.595 1.00  14.54 ? 132 SER A O   1 
ATOM   1048 C  CB  . SER A 1 132 ? 26.084 -0.765  -11.676 1.00  16.14 ? 132 SER A CB  1 
ATOM   1049 O  OG  . SER A 1 132 ? 24.664 -0.582  -11.670 1.00  16.70 ? 132 SER A OG  1 
ATOM   1050 N  N   . PHE A 1 133 ? 26.088 -2.590  -9.219  1.00  15.80 ? 133 PHE A N   1 
ATOM   1051 C  CA  . PHE A 1 133 ? 25.353 -3.006  -8.013  1.00  16.74 ? 133 PHE A CA  1 
ATOM   1052 C  C   . PHE A 1 133 ? 23.971 -2.342  -7.953  1.00  15.99 ? 133 PHE A C   1 
ATOM   1053 O  O   . PHE A 1 133 ? 22.967 -3.020  -7.718  1.00  14.91 ? 133 PHE A O   1 
ATOM   1054 C  CB  . PHE A 1 133 ? 26.206 -2.667  -6.795  1.00  17.97 ? 133 PHE A CB  1 
ATOM   1055 C  CG  . PHE A 1 133 ? 25.496 -2.816  -5.484  1.00  19.63 ? 133 PHE A CG  1 
ATOM   1056 C  CD1 . PHE A 1 133 ? 25.142 -4.053  -5.005  1.00  19.99 ? 133 PHE A CD1 1 
ATOM   1057 C  CD2 . PHE A 1 133 ? 25.281 -1.690  -4.669  1.00  22.89 ? 133 PHE A CD2 1 
ATOM   1058 C  CE1 . PHE A 1 133 ? 24.503 -4.199  -3.771  1.00  19.67 ? 133 PHE A CE1 1 
ATOM   1059 C  CE2 . PHE A 1 133 ? 24.613 -1.824  -3.426  1.00  24.40 ? 133 PHE A CE2 1 
ATOM   1060 C  CZ  . PHE A 1 133 ? 24.249 -3.092  -2.963  1.00  21.03 ? 133 PHE A CZ  1 
ATOM   1061 N  N   . VAL A 1 134 ? 23.916 -1.039  -8.219  1.00  16.87 ? 134 VAL A N   1 
ATOM   1062 C  CA  . VAL A 1 134 ? 22.632 -0.303  -8.156  1.00  19.64 ? 134 VAL A CA  1 
ATOM   1063 C  C   . VAL A 1 134 ? 21.623 -0.877  -9.118  1.00  19.61 ? 134 VAL A C   1 
ATOM   1064 O  O   . VAL A 1 134 ? 20.463 -1.048  -8.768  1.00  21.33 ? 134 VAL A O   1 
ATOM   1065 C  CB  . VAL A 1 134 ? 22.840 1.197   -8.455  1.00  22.86 ? 134 VAL A CB  1 
ATOM   1066 C  CG1 . VAL A 1 134 ? 21.491 1.892   -8.486  1.00  30.51 ? 134 VAL A CG1 1 
ATOM   1067 C  CG2 . VAL A 1 134 ? 23.685 1.794   -7.340  1.00  27.22 ? 134 VAL A CG2 1 
ATOM   1068 N  N   A GLU A 1 135 ? 22.058 -1.236  -10.320 0.50  19.06 ? 135 GLU A N   1 
ATOM   1069 N  N   B GLU A 1 135 ? 22.034 -1.197  -10.352 0.50  18.16 ? 135 GLU A N   1 
ATOM   1070 C  CA  A GLU A 1 135 ? 21.109 -1.822  -11.239 0.50  19.05 ? 135 GLU A CA  1 
ATOM   1071 C  CA  B GLU A 1 135 ? 21.087 -1.843  -11.266 0.50  17.65 ? 135 GLU A CA  1 
ATOM   1072 C  C   A GLU A 1 135 ? 20.695 -3.278  -10.875 0.50  18.31 ? 135 GLU A C   1 
ATOM   1073 C  C   B GLU A 1 135 ? 20.665 -3.246  -10.767 0.50  17.32 ? 135 GLU A C   1 
ATOM   1074 O  O   A GLU A 1 135 ? 19.532 -3.655  -11.048 0.50  17.53 ? 135 GLU A O   1 
ATOM   1075 O  O   B GLU A 1 135 ? 19.467 -3.554  -10.739 0.50  16.35 ? 135 GLU A O   1 
ATOM   1076 C  CB  A GLU A 1 135 ? 21.594 -1.675  -12.686 0.50  20.77 ? 135 GLU A CB  1 
ATOM   1077 C  CB  B GLU A 1 135 ? 21.595 -1.896  -12.727 0.50  17.92 ? 135 GLU A CB  1 
ATOM   1078 C  CG  A GLU A 1 135 ? 20.439 -1.670  -13.663 0.50  22.61 ? 135 GLU A CG  1 
ATOM   1079 C  CG  B GLU A 1 135 ? 21.699 -0.543  -13.440 0.50  18.14 ? 135 GLU A CG  1 
ATOM   1080 C  CD  A GLU A 1 135 ? 19.734 -3.002  -13.646 0.50  22.69 ? 135 GLU A CD  1 
ATOM   1081 C  CD  B GLU A 1 135 ? 20.367 0.028   -13.947 0.50  18.40 ? 135 GLU A CD  1 
ATOM   1082 O  OE1 A GLU A 1 135 ? 18.485 -3.089  -13.790 0.50  20.47 ? 135 GLU A OE1 1 
ATOM   1083 O  OE1 B GLU A 1 135 ? 20.378 1.161   -14.497 0.50  18.33 ? 135 GLU A OE1 1 
ATOM   1084 O  OE2 A GLU A 1 135 ? 20.474 -3.976  -13.475 0.50  23.87 ? 135 GLU A OE2 1 
ATOM   1085 O  OE2 B GLU A 1 135 ? 19.323 -0.647  -13.824 0.50  17.80 ? 135 GLU A OE2 1 
ATOM   1086 N  N   . ALA A 1 136 ? 21.627 -4.093  -10.360 1.00  16.58 ? 136 ALA A N   1 
ATOM   1087 C  CA  . ALA A 1 136 ? 21.272 -5.441  -9.891  1.00  16.27 ? 136 ALA A CA  1 
ATOM   1088 C  C   . ALA A 1 136 ? 20.255 -5.387  -8.726  1.00  15.68 ? 136 ALA A C   1 
ATOM   1089 O  O   . ALA A 1 136 ? 19.394 -6.248  -8.599  1.00  14.97 ? 136 ALA A O   1 
ATOM   1090 C  CB  . ALA A 1 136 ? 22.513 -6.223  -9.453  1.00  15.18 ? 136 ALA A CB  1 
ATOM   1091 N  N   . ALA A 1 137 ? 20.326 -4.349  -7.918  1.00  14.86 ? 137 ALA A N   1 
ATOM   1092 C  CA  . ALA A 1 137 ? 19.452 -4.289  -6.718  1.00  16.31 ? 137 ALA A CA  1 
ATOM   1093 C  C   . ALA A 1 137 ? 17.978 -4.158  -7.078  1.00  16.53 ? 137 ALA A C   1 
ATOM   1094 O  O   . ALA A 1 137 ? 17.073 -4.337  -6.225  1.00  14.74 ? 137 ALA A O   1 
ATOM   1095 C  CB  . ALA A 1 137 ? 19.919 -3.157  -5.791  1.00  17.13 ? 137 ALA A CB  1 
ATOM   1096 N  N   . HIS A 1 138 ? 17.738 -3.868  -8.360  1.00  17.38 ? 138 HIS A N   1 
ATOM   1097 C  CA  . HIS A 1 138 ? 16.387 -3.723  -8.928  1.00  18.91 ? 138 HIS A CA  1 
ATOM   1098 C  C   . HIS A 1 138 ? 15.886 -4.916  -9.695  1.00  21.07 ? 138 HIS A C   1 
ATOM   1099 O  O   . HIS A 1 138 ? 14.831 -4.829  -10.330 1.00  19.07 ? 138 HIS A O   1 
ATOM   1100 C  CB  . HIS A 1 138 ? 16.309 -2.409  -9.767  1.00  19.41 ? 138 HIS A CB  1 
ATOM   1101 C  CG  . HIS A 1 138 ? 16.384 -1.181  -8.895  1.00  19.97 ? 138 HIS A CG  1 
ATOM   1102 N  ND1 . HIS A 1 138 ? 15.291 -0.642  -8.318  1.00  22.43 ? 138 HIS A ND1 1 
ATOM   1103 C  CD2 . HIS A 1 138 ? 17.470 -0.484  -8.391  1.00  19.84 ? 138 HIS A CD2 1 
ATOM   1104 C  CE1 . HIS A 1 138 ? 15.654 0.391   -7.552  1.00  20.25 ? 138 HIS A CE1 1 
ATOM   1105 N  NE2 . HIS A 1 138 ? 16.986 0.477   -7.579  1.00  20.85 ? 138 HIS A NE2 1 
ATOM   1106 N  N   . GLU A 1 139 ? 16.569 -6.067  -9.578  1.00  18.32 ? 139 GLU A N   1 
ATOM   1107 C  CA  . GLU A 1 139 ? 16.175 -7.288  -10.316 1.00  20.49 ? 139 GLU A CA  1 
ATOM   1108 C  C   . GLU A 1 139 ? 16.037 -8.468  -9.366  1.00  18.74 ? 139 GLU A C   1 
ATOM   1109 O  O   . GLU A 1 139 ? 16.817 -8.585  -8.421  1.00  16.54 ? 139 GLU A O   1 
ATOM   1110 C  CB  . GLU A 1 139 ? 17.278 -7.658  -11.297 1.00  23.71 ? 139 GLU A CB  1 
ATOM   1111 C  CG  . GLU A 1 139 ? 17.748 -6.530  -12.166 1.00  26.37 ? 139 GLU A CG  1 
ATOM   1112 C  CD  . GLU A 1 139 ? 16.834 -6.335  -13.345 1.00  30.12 ? 139 GLU A CD  1 
ATOM   1113 O  OE1 . GLU A 1 139 ? 15.840 -7.087  -13.420 1.00  32.41 ? 139 GLU A OE1 1 
ATOM   1114 O  OE2 . GLU A 1 139 ? 17.138 -5.441  -14.196 1.00  36.57 ? 139 GLU A OE2 1 
ATOM   1115 N  N   . PRO A 1 140 ? 15.090 -9.361  -9.625  1.00  20.46 ? 140 PRO A N   1 
ATOM   1116 C  CA  . PRO A 1 140 ? 14.854 -10.461 -8.659  1.00  19.46 ? 140 PRO A CA  1 
ATOM   1117 C  C   . PRO A 1 140 ? 16.064 -11.376 -8.458  1.00  19.62 ? 140 PRO A C   1 
ATOM   1118 O  O   . PRO A 1 140 ? 16.228 -11.944 -7.384  1.00  20.04 ? 140 PRO A O   1 
ATOM   1119 C  CB  . PRO A 1 140 ? 13.684 -11.227 -9.282  1.00  21.78 ? 140 PRO A CB  1 
ATOM   1120 C  CG  . PRO A 1 140 ? 12.940 -10.153 -10.064 1.00  23.62 ? 140 PRO A CG  1 
ATOM   1121 C  CD  . PRO A 1 140 ? 14.047 -9.319  -10.677 1.00  22.25 ? 140 PRO A CD  1 
ATOM   1122 N  N   . ASP A 1 141 ? 16.880 -11.543 -9.507  1.00  17.05 ? 141 ASP A N   1 
ATOM   1123 C  CA  . ASP A 1 141 ? 18.103 -12.359 -9.426  1.00  16.23 ? 141 ASP A CA  1 
ATOM   1124 C  C   . ASP A 1 141 ? 19.305 -11.513 -9.240  1.00  14.45 ? 141 ASP A C   1 
ATOM   1125 O  O   . ASP A 1 141 ? 20.412 -11.987 -9.465  1.00  15.46 ? 141 ASP A O   1 
ATOM   1126 C  CB  . ASP A 1 141 ? 18.321 -13.255 -10.668 1.00  17.62 ? 141 ASP A CB  1 
ATOM   1127 C  CG  . ASP A 1 141 ? 18.382 -12.461 -11.967 1.00  18.35 ? 141 ASP A CG  1 
ATOM   1128 O  OD1 . ASP A 1 141 ? 18.195 -11.204 -11.933 1.00  16.05 ? 141 ASP A OD1 1 
ATOM   1129 O  OD2 . ASP A 1 141 ? 18.644 -13.106 -13.023 1.00  18.42 ? 141 ASP A OD2 1 
ATOM   1130 N  N   . GLY A 1 142 ? 19.130 -10.258 -8.834  1.00  15.23 ? 142 GLY A N   1 
ATOM   1131 C  CA  . GLY A 1 142 ? 20.281 -9.325  -8.894  1.00  12.79 ? 142 GLY A CA  1 
ATOM   1132 C  C   . GLY A 1 142 ? 21.296 -9.424  -7.756  1.00  13.55 ? 142 GLY A C   1 
ATOM   1133 O  O   . GLY A 1 142 ? 22.471 -9.148  -7.970  1.00  13.85 ? 142 GLY A O   1 
ATOM   1134 N  N   . LEU A 1 143 ? 20.832 -9.673  -6.529  1.00  12.63 ? 143 LEU A N   1 
ATOM   1135 C  CA  . LEU A 1 143 ? 21.679 -9.697  -5.334  1.00  11.61 ? 143 LEU A CA  1 
ATOM   1136 C  C   . LEU A 1 143 ? 21.652 -11.077 -4.613  1.00  11.35 ? 143 LEU A C   1 
ATOM   1137 O  O   . LEU A 1 143 ? 20.649 -11.833 -4.653  1.00  12.35 ? 143 LEU A O   1 
ATOM   1138 C  CB  . LEU A 1 143 ? 21.213 -8.603  -4.316  1.00  12.30 ? 143 LEU A CB  1 
ATOM   1139 C  CG  . LEU A 1 143 ? 21.118 -7.150  -4.785  1.00  12.93 ? 143 LEU A CG  1 
ATOM   1140 C  CD1 . LEU A 1 143 ? 20.741 -6.282  -3.590  1.00  12.42 ? 143 LEU A CD1 1 
ATOM   1141 C  CD2 . LEU A 1 143 ? 22.393 -6.626  -5.438  1.00  11.19 ? 143 LEU A CD2 1 
ATOM   1142 N  N   . ALA A 1 144 ? 22.789 -11.372 -3.987  1.00  11.82 ? 144 ALA A N   1 
ATOM   1143 C  CA  . ALA A 1 144 ? 22.942 -12.558 -3.137  1.00  13.58 ? 144 ALA A CA  1 
ATOM   1144 C  C   . ALA A 1 144 ? 23.584 -12.035 -1.878  1.00  12.91 ? 144 ALA A C   1 
ATOM   1145 O  O   . ALA A 1 144 ? 24.593 -11.339 -1.946  1.00  15.33 ? 144 ALA A O   1 
ATOM   1146 C  CB  . ALA A 1 144 ? 23.825 -13.635 -3.829  1.00  12.72 ? 144 ALA A CB  1 
ATOM   1147 N  N   . VAL A 1 145 ? 22.978 -12.369 -0.736  1.00  14.54 ? 145 VAL A N   1 
ATOM   1148 C  CA  . VAL A 1 145 ? 23.457 -11.908 0.573   1.00  14.21 ? 145 VAL A CA  1 
ATOM   1149 C  C   . VAL A 1 145 ? 23.659 -13.130 1.473   1.00  13.97 ? 145 VAL A C   1 
ATOM   1150 O  O   . VAL A 1 145 ? 22.758 -13.994 1.679   1.00  12.59 ? 145 VAL A O   1 
ATOM   1151 C  CB  . VAL A 1 145 ? 22.498 -10.903 1.253   1.00  15.40 ? 145 VAL A CB  1 
ATOM   1152 C  CG1 . VAL A 1 145 ? 23.008 -10.553 2.658   1.00  14.85 ? 145 VAL A CG1 1 
ATOM   1153 C  CG2 . VAL A 1 145 ? 22.332 -9.606  0.434   1.00  15.93 ? 145 VAL A CG2 1 
ATOM   1154 N  N   . LEU A 1 146 ? 24.873 -13.191 1.968   1.00  13.24 ? 146 LEU A N   1 
ATOM   1155 C  CA  . LEU A 1 146 ? 25.250 -14.284 2.826   1.00  16.74 ? 146 LEU A CA  1 
ATOM   1156 C  C   . LEU A 1 146 ? 25.020 -13.815 4.239   1.00  13.78 ? 146 LEU A C   1 
ATOM   1157 O  O   . LEU A 1 146 ? 25.567 -12.819 4.599   1.00  13.55 ? 146 LEU A O   1 
ATOM   1158 C  CB  . LEU A 1 146 ? 26.725 -14.513 2.622   1.00  19.74 ? 146 LEU A CB  1 
ATOM   1159 C  CG  . LEU A 1 146 ? 27.241 -15.890 2.390   1.00  27.81 ? 146 LEU A CG  1 
ATOM   1160 C  CD1 . LEU A 1 146 ? 28.757 -15.724 2.236   1.00  31.38 ? 146 LEU A CD1 1 
ATOM   1161 C  CD2 . LEU A 1 146 ? 26.909 -16.657 3.625   1.00  28.99 ? 146 LEU A CD2 1 
ATOM   1162 N  N   . GLY A 1 147 ? 24.264 -14.564 5.035   1.00  13.28 ? 147 GLY A N   1 
ATOM   1163 C  CA  . GLY A 1 147 ? 23.988 -14.147 6.438   1.00  14.60 ? 147 GLY A CA  1 
ATOM   1164 C  C   . GLY A 1 147 ? 24.724 -15.091 7.393   1.00  15.15 ? 147 GLY A C   1 
ATOM   1165 O  O   . GLY A 1 147 ? 24.663 -16.321 7.199   1.00  16.22 ? 147 GLY A O   1 
ATOM   1166 N  N   . VAL A 1 148 ? 25.451 -14.544 8.359   1.00  13.66 ? 148 VAL A N   1 
ATOM   1167 C  CA  . VAL A 1 148 ? 26.205 -15.387 9.332   1.00  13.64 ? 148 VAL A CA  1 
ATOM   1168 C  C   . VAL A 1 148 ? 25.759 -14.963 10.728  1.00  12.68 ? 148 VAL A C   1 
ATOM   1169 O  O   . VAL A 1 148 ? 25.855 -13.781 11.063  1.00  12.47 ? 148 VAL A O   1 
ATOM   1170 C  CB  . VAL A 1 148 ? 27.751 -15.119 9.223   1.00  14.41 ? 148 VAL A CB  1 
ATOM   1171 C  CG1 . VAL A 1 148 ? 28.540 -15.926 10.276  1.00  13.17 ? 148 VAL A CG1 1 
ATOM   1172 C  CG2 . VAL A 1 148 ? 28.252 -15.393 7.809   1.00  14.61 ? 148 VAL A CG2 1 
ATOM   1173 N  N   . PHE A 1 149 ? 25.288 -15.902 11.560  1.00  13.14 ? 149 PHE A N   1 
ATOM   1174 C  CA  . PHE A 1 149 ? 24.917 -15.491 12.926  1.00  13.09 ? 149 PHE A CA  1 
ATOM   1175 C  C   . PHE A 1 149 ? 26.152 -15.331 13.803  1.00  14.88 ? 149 PHE A C   1 
ATOM   1176 O  O   . PHE A 1 149 ? 27.141 -16.077 13.617  1.00  14.67 ? 149 PHE A O   1 
ATOM   1177 C  CB  . PHE A 1 149 ? 23.960 -16.518 13.549  1.00  12.02 ? 149 PHE A CB  1 
ATOM   1178 C  CG  . PHE A 1 149 ? 22.669 -16.644 12.820  1.00  11.64 ? 149 PHE A CG  1 
ATOM   1179 C  CD1 . PHE A 1 149 ? 21.828 -15.545 12.703  1.00  11.88 ? 149 PHE A CD1 1 
ATOM   1180 C  CD2 . PHE A 1 149 ? 22.278 -17.864 12.308  1.00  11.36 ? 149 PHE A CD2 1 
ATOM   1181 C  CE1 . PHE A 1 149 ? 20.566 -15.700 12.142  1.00  12.11 ? 149 PHE A CE1 1 
ATOM   1182 C  CE2 . PHE A 1 149 ? 21.055 -17.995 11.624  1.00  12.64 ? 149 PHE A CE2 1 
ATOM   1183 C  CZ  . PHE A 1 149 ? 20.194 -16.917 11.576  1.00  11.09 ? 149 PHE A CZ  1 
ATOM   1184 N  N   . LEU A 1 150 ? 26.074 -14.375 14.761  1.00  14.32 ? 150 LEU A N   1 
ATOM   1185 C  CA  . LEU A 1 150 ? 27.084 -14.277 15.808  1.00  13.77 ? 150 LEU A CA  1 
ATOM   1186 C  C   . LEU A 1 150 ? 26.467 -14.647 17.162  1.00  15.23 ? 150 LEU A C   1 
ATOM   1187 O  O   . LEU A 1 150 ? 25.380 -14.216 17.491  1.00  13.41 ? 150 LEU A O   1 
ATOM   1188 C  CB  . LEU A 1 150 ? 27.665 -12.887 15.896  1.00  14.37 ? 150 LEU A CB  1 
ATOM   1189 C  CG  . LEU A 1 150 ? 28.579 -12.474 14.748  1.00  14.60 ? 150 LEU A CG  1 
ATOM   1190 C  CD1 . LEU A 1 150 ? 27.724 -12.266 13.514  1.00  13.57 ? 150 LEU A CD1 1 
ATOM   1191 C  CD2 . LEU A 1 150 ? 29.260 -11.163 15.150  1.00  15.90 ? 150 LEU A CD2 1 
ATOM   1192 N  N   . GLN A 1 151 ? 27.201 -15.464 17.922  1.00  15.37 ? 151 GLN A N   1 
ATOM   1193 C  CA  . GLN A 1 151 ? 26.818 -15.697 19.320  1.00  16.01 ? 151 GLN A CA  1 
ATOM   1194 C  C   . GLN A 1 151 ? 27.955 -15.243 20.239  1.00  16.14 ? 151 GLN A C   1 
ATOM   1195 O  O   . GLN A 1 151 ? 29.097 -15.158 19.826  1.00  17.97 ? 151 GLN A O   1 
ATOM   1196 C  CB  . GLN A 1 151 ? 26.531 -17.188 19.491  1.00  17.11 ? 151 GLN A CB  1 
ATOM   1197 C  CG  . GLN A 1 151 ? 27.802 -18.002 19.563  1.00  20.15 ? 151 GLN A CG  1 
ATOM   1198 C  CD  . GLN A 1 151 ? 27.554 -19.497 19.476  1.00  23.34 ? 151 GLN A CD  1 
ATOM   1199 O  OE1 . GLN A 1 151 ? 26.414 -19.944 19.432  1.00  24.62 ? 151 GLN A OE1 1 
ATOM   1200 N  NE2 . GLN A 1 151 ? 28.634 -20.270 19.407  1.00  23.47 ? 151 GLN A NE2 1 
ATOM   1201 N  N   . ILE A 1 152 ? 27.638 -14.951 21.489  1.00  17.58 ? 152 ILE A N   1 
ATOM   1202 C  CA  . ILE A 1 152 ? 28.664 -14.534 22.459  1.00  20.24 ? 152 ILE A CA  1 
ATOM   1203 C  C   . ILE A 1 152 ? 29.606 -15.716 22.654  1.00  22.56 ? 152 ILE A C   1 
ATOM   1204 O  O   . ILE A 1 152 ? 29.126 -16.832 22.857  1.00  22.97 ? 152 ILE A O   1 
ATOM   1205 C  CB  . ILE A 1 152 ? 28.028 -14.141 23.802  1.00  21.75 ? 152 ILE A CB  1 
ATOM   1206 C  CG1 . ILE A 1 152 ? 27.038 -12.994 23.627  1.00  19.59 ? 152 ILE A CG1 1 
ATOM   1207 C  CG2 . ILE A 1 152 ? 29.125 -13.842 24.835  1.00  23.20 ? 152 ILE A CG2 1 
ATOM   1208 C  CD1 . ILE A 1 152 ? 27.605 -11.780 22.910  1.00  21.24 ? 152 ILE A CD1 1 
ATOM   1209 N  N   . GLY A 1 153 ? 30.911 -15.488 22.513  1.00  21.29 ? 153 GLY A N   1 
ATOM   1210 C  CA  . GLY A 1 153 ? 31.975 -16.507 22.739  1.00  26.89 ? 153 GLY A CA  1 
ATOM   1211 C  C   . GLY A 1 153 ? 33.389 -15.906 22.607  1.00  28.39 ? 153 GLY A C   1 
ATOM   1212 O  O   . GLY A 1 153 ? 33.572 -14.712 22.798  1.00  32.30 ? 153 GLY A O   1 
ATOM   1213 N  N   . GLU A 1 154 ? 34.389 -16.690 22.211  1.00  32.98 ? 154 GLU A N   1 
ATOM   1214 C  CA  . GLU A 1 154 ? 35.774 -16.130 22.037  1.00  33.59 ? 154 GLU A CA  1 
ATOM   1215 C  C   . GLU A 1 154 ? 35.915 -15.068 20.904  1.00  33.21 ? 154 GLU A C   1 
ATOM   1216 O  O   . GLU A 1 154 ? 35.437 -15.321 19.768  1.00  30.14 ? 154 GLU A O   1 
ATOM   1217 C  CB  . GLU A 1 154 ? 36.778 -17.259 21.816  1.00  37.22 ? 154 GLU A CB  1 
ATOM   1218 C  CG  . GLU A 1 154 ? 36.761 -18.242 22.972  1.00  38.70 ? 154 GLU A CG  1 
ATOM   1219 C  CD  . GLU A 1 154 ? 37.781 -19.345 22.814  1.00  44.07 ? 154 GLU A CD  1 
ATOM   1220 O  OE1 . GLU A 1 154 ? 37.523 -20.452 23.324  1.00  49.71 ? 154 GLU A OE1 1 
ATOM   1221 O  OE2 . GLU A 1 154 ? 38.830 -19.109 22.187  1.00  47.84 ? 154 GLU A OE2 1 
ATOM   1222 N  N   . PRO A 1 155 ? 36.592 -13.907 21.194  1.00  32.73 ? 155 PRO A N   1 
ATOM   1223 C  CA  . PRO A 1 155 ? 36.643 -12.754 20.253  1.00  28.03 ? 155 PRO A CA  1 
ATOM   1224 C  C   . PRO A 1 155 ? 37.210 -13.186 18.948  1.00  31.02 ? 155 PRO A C   1 
ATOM   1225 O  O   . PRO A 1 155 ? 38.183 -13.956 18.972  1.00  30.50 ? 155 PRO A O   1 
ATOM   1226 C  CB  . PRO A 1 155 ? 37.621 -11.781 20.919  1.00  29.98 ? 155 PRO A CB  1 
ATOM   1227 C  CG  . PRO A 1 155 ? 37.850 -12.302 22.307  1.00  29.35 ? 155 PRO A CG  1 
ATOM   1228 C  CD  . PRO A 1 155 ? 36.966 -13.492 22.561  1.00  29.28 ? 155 PRO A CD  1 
ATOM   1229 N  N   . ASN A 1 156 ? 36.595 -12.762 17.838  1.00  27.92 ? 156 ASN A N   1 
ATOM   1230 C  CA  . ASN A 1 156 ? 37.107 -13.079 16.504  1.00  29.98 ? 156 ASN A CA  1 
ATOM   1231 C  C   . ASN A 1 156 ? 38.118 -11.971 16.113  1.00  30.47 ? 156 ASN A C   1 
ATOM   1232 O  O   . ASN A 1 156 ? 37.860 -10.774 16.367  1.00  30.15 ? 156 ASN A O   1 
ATOM   1233 C  CB  . ASN A 1 156 ? 35.974 -13.203 15.501  1.00  29.44 ? 156 ASN A CB  1 
ATOM   1234 C  CG  . ASN A 1 156 ? 36.470 -13.640 14.124  1.00  32.93 ? 156 ASN A CG  1 
ATOM   1235 O  OD1 . ASN A 1 156 ? 37.239 -12.919 13.474  1.00  38.59 ? 156 ASN A OD1 1 
ATOM   1236 N  ND2 . ASN A 1 156 ? 36.063 -14.836 13.678  1.00  31.47 ? 156 ASN A ND2 1 
ATOM   1237 N  N   . SER A 1 157 ? 39.272 -12.346 15.548  1.00  26.66 ? 157 SER A N   1 
ATOM   1238 C  CA  . SER A 1 157 ? 40.340 -11.348 15.369  1.00  27.09 ? 157 SER A CA  1 
ATOM   1239 C  C   . SER A 1 157 ? 39.992 -10.407 14.231  1.00  24.80 ? 157 SER A C   1 
ATOM   1240 O  O   . SER A 1 157 ? 40.455 -9.292  14.219  1.00  21.55 ? 157 SER A O   1 
ATOM   1241 C  CB  . SER A 1 157 ? 41.694 -11.996 15.039  1.00  31.16 ? 157 SER A CB  1 
ATOM   1242 O  OG  . SER A 1 157 ? 41.675 -12.603 13.748  1.00  31.09 ? 157 SER A OG  1 
ATOM   1243 N  N   . GLN A 1 158 ? 39.193 -10.878 13.278  1.00  25.52 ? 158 GLN A N   1 
ATOM   1244 C  CA  . GLN A 1 158 ? 38.766 -9.981  12.223  1.00  24.44 ? 158 GLN A CA  1 
ATOM   1245 C  C   . GLN A 1 158 ? 37.683 -9.071  12.702  1.00  23.34 ? 158 GLN A C   1 
ATOM   1246 O  O   . GLN A 1 158 ? 37.624 -7.956  12.233  1.00  21.98 ? 158 GLN A O   1 
ATOM   1247 C  CB  . GLN A 1 158 ? 38.369 -10.695 10.938  1.00  25.51 ? 158 GLN A CB  1 
ATOM   1248 C  CG  . GLN A 1 158 ? 39.596 -11.251 10.236  1.00  28.97 ? 158 GLN A CG  1 
ATOM   1249 C  CD  . GLN A 1 158 ? 40.633 -10.179 9.896   1.00  30.18 ? 158 GLN A CD  1 
ATOM   1250 O  OE1 . GLN A 1 158 ? 40.413 -9.325  9.030   1.00  33.55 ? 158 GLN A OE1 1 
ATOM   1251 N  NE2 . GLN A 1 158 ? 41.769 -10.235 10.562  1.00  31.18 ? 158 GLN A NE2 1 
ATOM   1252 N  N   . LEU A 1 159 ? 36.851 -9.533  13.639  1.00  21.47 ? 159 LEU A N   1 
ATOM   1253 C  CA  . LEU A 1 159 ? 35.920 -8.618  14.314  1.00  21.47 ? 159 LEU A CA  1 
ATOM   1254 C  C   . LEU A 1 159 ? 36.645 -7.595  15.160  1.00  19.24 ? 159 LEU A C   1 
ATOM   1255 O  O   . LEU A 1 159 ? 36.219 -6.442  15.284  1.00  17.62 ? 159 LEU A O   1 
ATOM   1256 C  CB  . LEU A 1 159 ? 34.925 -9.362  15.194  1.00  19.64 ? 159 LEU A CB  1 
ATOM   1257 C  CG  . LEU A 1 159 ? 33.861 -10.089 14.442  1.00  19.01 ? 159 LEU A CG  1 
ATOM   1258 C  CD1 . LEU A 1 159 ? 32.948 -10.767 15.499  1.00  19.14 ? 159 LEU A CD1 1 
ATOM   1259 C  CD2 . LEU A 1 159 ? 33.097 -9.069  13.640  1.00  18.32 ? 159 LEU A CD2 1 
ATOM   1260 N  N   . GLN A 1 160 ? 37.746 -8.018  15.766  1.00  19.98 ? 160 GLN A N   1 
ATOM   1261 C  CA  . GLN A 1 160 ? 38.606 -7.029  16.431  1.00  19.25 ? 160 GLN A CA  1 
ATOM   1262 C  C   . GLN A 1 160 ? 39.204 -5.939  15.485  1.00  17.79 ? 160 GLN A C   1 
ATOM   1263 O  O   . GLN A 1 160 ? 39.246 -4.773  15.845  1.00  20.19 ? 160 GLN A O   1 
ATOM   1264 C  CB  . GLN A 1 160 ? 39.743 -7.741  17.154  1.00  21.45 ? 160 GLN A CB  1 
ATOM   1265 C  CG  . GLN A 1 160 ? 40.456 -6.829  18.129  1.00  22.40 ? 160 GLN A CG  1 
ATOM   1266 C  CD  . GLN A 1 160 ? 39.591 -6.362  19.278  1.00  21.64 ? 160 GLN A CD  1 
ATOM   1267 O  OE1 . GLN A 1 160 ? 38.741 -7.096  19.780  1.00  22.22 ? 160 GLN A OE1 1 
ATOM   1268 N  NE2 . GLN A 1 160 ? 39.840 -5.158  19.741  1.00  20.98 ? 160 GLN A NE2 1 
ATOM   1269 N  N   . LYS A 1 161 ? 39.681 -6.345  14.310  1.00  17.38 ? 161 LYS A N   1 
ATOM   1270 C  CA  . LYS A 1 161 ? 40.134 -5.424  13.273  1.00  19.14 ? 161 LYS A CA  1 
ATOM   1271 C  C   . LYS A 1 161 ? 38.988 -4.394  13.020  1.00  18.46 ? 161 LYS A C   1 
ATOM   1272 O  O   . LYS A 1 161 ? 39.227 -3.194  13.007  1.00  18.92 ? 161 LYS A O   1 
ATOM   1273 C  CB  . LYS A 1 161 ? 40.523 -6.226  12.008  1.00  19.95 ? 161 LYS A CB  1 
ATOM   1274 C  CG  . LYS A 1 161 ? 41.098 -5.365  10.851  1.00  21.98 ? 161 LYS A CG  1 
ATOM   1275 C  CD  . LYS A 1 161 ? 41.378 -6.189  9.593   1.00  25.79 ? 161 LYS A CD  1 
ATOM   1276 C  CE  . LYS A 1 161 ? 41.633 -5.276  8.384   1.00  24.69 ? 161 LYS A CE  1 
ATOM   1277 N  NZ  . LYS A 1 161 ? 42.828 -4.363  8.459   1.00  26.46 ? 161 LYS A NZ  1 
ATOM   1278 N  N   . ILE A 1 162 ? 37.738 -4.842  12.966  1.00  17.31 ? 162 ILE A N   1 
ATOM   1279 C  CA  . ILE A 1 162 ? 36.606 -3.873  12.820  1.00  16.04 ? 162 ILE A CA  1 
ATOM   1280 C  C   . ILE A 1 162 ? 36.415 -2.994  14.039  1.00  15.90 ? 162 ILE A C   1 
ATOM   1281 O  O   . ILE A 1 162 ? 36.374 -1.747  13.946  1.00  17.21 ? 162 ILE A O   1 
ATOM   1282 C  CB  . ILE A 1 162 ? 35.268 -4.583  12.438  1.00  15.60 ? 162 ILE A CB  1 
ATOM   1283 C  CG1 . ILE A 1 162 ? 35.432 -5.228  11.077  1.00  14.92 ? 162 ILE A CG1 1 
ATOM   1284 C  CG2 . ILE A 1 162 ? 34.074 -3.599  12.589  1.00  14.84 ? 162 ILE A CG2 1 
ATOM   1285 C  CD1 . ILE A 1 162 ? 34.530 -6.383  10.820  1.00  13.04 ? 162 ILE A CD1 1 
ATOM   1286 N  N   . THR A 1 163 ? 36.354 -3.593  15.230  1.00  19.40 ? 163 THR A N   1 
ATOM   1287 C  CA  . THR A 1 163 ? 36.038 -2.785  16.363  1.00  17.23 ? 163 THR A CA  1 
ATOM   1288 C  C   . THR A 1 163 ? 37.082 -1.743  16.649  1.00  17.05 ? 163 THR A C   1 
ATOM   1289 O  O   . THR A 1 163 ? 36.737 -0.675  17.179  1.00  16.24 ? 163 THR A O   1 
ATOM   1290 C  CB  . THR A 1 163 ? 35.671 -3.569  17.652  1.00  19.61 ? 163 THR A CB  1 
ATOM   1291 O  OG1 . THR A 1 163 ? 36.758 -4.384  18.022  1.00  20.04 ? 163 THR A OG1 1 
ATOM   1292 C  CG2 . THR A 1 163 ? 34.432 -4.459  17.448  1.00  20.23 ? 163 THR A CG2 1 
ATOM   1293 N  N   . ASP A 1 164 ? 38.346 -2.036  16.314  1.00  16.80 ? 164 ASP A N   1 
ATOM   1294 C  CA  . ASP A 1 164 ? 39.415 -1.061  16.527  1.00  18.22 ? 164 ASP A CA  1 
ATOM   1295 C  C   . ASP A 1 164 ? 39.232 0.254   15.725  1.00  19.94 ? 164 ASP A C   1 
ATOM   1296 O  O   . ASP A 1 164 ? 39.786 1.270   16.113  1.00  21.15 ? 164 ASP A O   1 
ATOM   1297 C  CB  . ASP A 1 164 ? 40.754 -1.658  16.169  1.00  19.05 ? 164 ASP A CB  1 
ATOM   1298 C  CG  . ASP A 1 164 ? 41.332 -2.576  17.272  1.00  21.54 ? 164 ASP A CG  1 
ATOM   1299 O  OD1 . ASP A 1 164 ? 40.821 -2.603  18.418  1.00  22.83 ? 164 ASP A OD1 1 
ATOM   1300 O  OD2 . ASP A 1 164 ? 42.309 -3.281  16.941  1.00  22.18 ? 164 ASP A OD2 1 
ATOM   1301 N  N   . THR A 1 165 ? 38.387 0.254   14.698  1.00  18.51 ? 165 THR A N   1 
ATOM   1302 C  CA  . THR A 1 165 ? 38.146 1.456   13.890  1.00  18.84 ? 165 THR A CA  1 
ATOM   1303 C  C   . THR A 1 165 ? 36.993 2.315   14.315  1.00  21.34 ? 165 THR A C   1 
ATOM   1304 O  O   . THR A 1 165 ? 36.918 3.494   13.922  1.00  23.56 ? 165 THR A O   1 
ATOM   1305 C  CB  . THR A 1 165 ? 37.972 1.122   12.393  1.00  18.00 ? 165 THR A CB  1 
ATOM   1306 O  OG1 . THR A 1 165 ? 36.690 0.583   12.144  1.00  15.48 ? 165 THR A OG1 1 
ATOM   1307 C  CG2 . THR A 1 165 ? 38.983 0.099   11.914  1.00  19.62 ? 165 THR A CG2 1 
ATOM   1308 N  N   . LEU A 1 166 ? 36.118 1.787   15.185  1.00  21.39 ? 166 LEU A N   1 
ATOM   1309 C  CA  . LEU A 1 166 ? 34.831 2.397   15.436  1.00  20.22 ? 166 LEU A CA  1 
ATOM   1310 C  C   . LEU A 1 166 ? 34.938 3.779   16.090  1.00  23.60 ? 166 LEU A C   1 
ATOM   1311 O  O   . LEU A 1 166 ? 34.128 4.622   15.792  1.00  23.27 ? 166 LEU A O   1 
ATOM   1312 C  CB  . LEU A 1 166 ? 33.931 1.468   16.262  1.00  21.48 ? 166 LEU A CB  1 
ATOM   1313 C  CG  . LEU A 1 166 ? 33.711 0.127   15.532  1.00  23.40 ? 166 LEU A CG  1 
ATOM   1314 C  CD1 . LEU A 1 166 ? 32.874 -0.838  16.352  1.00  20.97 ? 166 LEU A CD1 1 
ATOM   1315 C  CD2 . LEU A 1 166 ? 33.064 0.377   14.171  1.00  23.76 ? 166 LEU A CD2 1 
ATOM   1316 N  N   . ASP A 1 167 ? 35.949 4.042   16.927  1.00  22.69 ? 167 ASP A N   1 
ATOM   1317 C  CA  . ASP A 1 167 ? 36.117 5.416   17.453  1.00  22.89 ? 167 ASP A CA  1 
ATOM   1318 C  C   . ASP A 1 167 ? 36.372 6.438   16.309  1.00  22.27 ? 167 ASP A C   1 
ATOM   1319 O  O   . ASP A 1 167 ? 35.909 7.567   16.392  1.00  24.18 ? 167 ASP A O   1 
ATOM   1320 C  CB  . ASP A 1 167 ? 37.315 5.494   18.433  1.00  28.13 ? 167 ASP A CB  1 
ATOM   1321 C  CG  . ASP A 1 167 ? 37.070 4.761   19.749  1.00  29.29 ? 167 ASP A CG  1 
ATOM   1322 O  OD1 . ASP A 1 167 ? 35.909 4.579   20.141  1.00  31.30 ? 167 ASP A OD1 1 
ATOM   1323 O  OD2 . ASP A 1 167 ? 38.048 4.379   20.400  1.00  34.05 ? 167 ASP A OD2 1 
ATOM   1324 N  N   . SER A 1 168 ? 37.086 6.031   15.254  1.00  22.22 ? 168 SER A N   1 
ATOM   1325 C  CA  . SER A 1 168 ? 37.362 6.916   14.090  1.00  22.07 ? 168 SER A CA  1 
ATOM   1326 C  C   . SER A 1 168 ? 36.144 7.125   13.154  1.00  22.84 ? 168 SER A C   1 
ATOM   1327 O  O   . SER A 1 168 ? 36.142 8.024   12.294  1.00  22.99 ? 168 SER A O   1 
ATOM   1328 C  CB  . SER A 1 168 ? 38.563 6.399   13.283  1.00  25.24 ? 168 SER A CB  1 
ATOM   1329 O  OG  . SER A 1 168 ? 38.182 5.190   12.570  1.00  23.36 ? 168 SER A OG  1 
ATOM   1330 N  N   . ILE A 1 169 ? 35.104 6.305   13.290  1.00  20.22 ? 169 ILE A N   1 
ATOM   1331 C  CA  . ILE A 1 169 ? 33.922 6.508   12.477  1.00  19.15 ? 169 ILE A CA  1 
ATOM   1332 C  C   . ILE A 1 169 ? 32.660 6.684   13.349  1.00  21.38 ? 169 ILE A C   1 
ATOM   1333 O  O   . ILE A 1 169 ? 31.566 6.289   12.969  1.00  19.27 ? 169 ILE A O   1 
ATOM   1334 C  CB  . ILE A 1 169 ? 33.727 5.406   11.429  1.00  18.00 ? 169 ILE A CB  1 
ATOM   1335 C  CG1 . ILE A 1 169 ? 33.606 4.047   12.091  1.00  17.76 ? 169 ILE A CG1 1 
ATOM   1336 C  CG2 . ILE A 1 169 ? 34.889 5.344   10.451  1.00  16.23 ? 169 ILE A CG2 1 
ATOM   1337 C  CD1 . ILE A 1 169 ? 33.491 2.909   11.062  1.00  18.70 ? 169 ILE A CD1 1 
ATOM   1338 N  N   . LYS A 1 170 ? 32.801 7.318   14.499  1.00  18.84 ? 170 LYS A N   1 
ATOM   1339 C  CA  . LYS A 1 170 ? 31.652 7.392   15.436  1.00  21.30 ? 170 LYS A CA  1 
ATOM   1340 C  C   . LYS A 1 170 ? 30.422 8.076   14.844  1.00  21.92 ? 170 LYS A C   1 
ATOM   1341 O  O   . LYS A 1 170 ? 29.284 7.613   15.058  1.00  17.58 ? 170 LYS A O   1 
ATOM   1342 C  CB  . LYS A 1 170 ? 32.077 8.082   16.753  1.00  23.76 ? 170 LYS A CB  1 
ATOM   1343 C  CG  . LYS A 1 170 ? 30.970 8.245   17.811  1.00  26.80 ? 170 LYS A CG  1 
ATOM   1344 C  CD  . LYS A 1 170 ? 31.520 8.867   19.120  1.00  34.91 ? 170 LYS A CD  1 
ATOM   1345 C  CE  . LYS A 1 170 ? 30.659 8.557   20.371  1.00  38.07 ? 170 LYS A CE  1 
ATOM   1346 N  NZ  . LYS A 1 170 ? 30.599 7.081   20.741  1.00  36.02 ? 170 LYS A NZ  1 
ATOM   1347 N  N   . GLU A 1 171 ? 30.643 9.197   14.139  1.00  18.88 ? 171 GLU A N   1 
ATOM   1348 C  CA  . GLU A 1 171 ? 29.524 9.992   13.562  1.00  20.49 ? 171 GLU A CA  1 
ATOM   1349 C  C   . GLU A 1 171 ? 29.133 9.439   12.173  1.00  19.20 ? 171 GLU A C   1 
ATOM   1350 O  O   . GLU A 1 171 ? 29.962 8.950   11.438  1.00  18.58 ? 171 GLU A O   1 
ATOM   1351 C  CB  . GLU A 1 171 ? 29.883 11.497  13.446  1.00  23.22 ? 171 GLU A CB  1 
ATOM   1352 C  CG  . GLU A 1 171 ? 30.419 12.155  14.746  1.00  29.78 ? 171 GLU A CG  1 
ATOM   1353 C  CD  . GLU A 1 171 ? 31.846 11.692  15.186  1.00  34.44 ? 171 GLU A CD  1 
ATOM   1354 O  OE1 . GLU A 1 171 ? 32.680 11.147  14.389  1.00  35.32 ? 171 GLU A OE1 1 
ATOM   1355 O  OE2 . GLU A 1 171 ? 32.158 11.859  16.386  1.00  45.55 ? 171 GLU A OE2 1 
ATOM   1356 N  N   A LYS A 1 172 ? 27.857 9.521   11.850  0.50  20.11 ? 172 LYS A N   1 
ATOM   1357 N  N   B LYS A 1 172 ? 27.852 9.518   11.846  0.50  19.39 ? 172 LYS A N   1 
ATOM   1358 C  CA  A LYS A 1 172 ? 27.354 9.161   10.543  0.50  20.41 ? 172 LYS A CA  1 
ATOM   1359 C  CA  B LYS A 1 172 ? 27.355 9.155   10.528  0.50  19.23 ? 172 LYS A CA  1 
ATOM   1360 C  C   A LYS A 1 172 ? 28.125 9.888   9.447   0.50  19.49 ? 172 LYS A C   1 
ATOM   1361 C  C   B LYS A 1 172 ? 28.156 9.883   9.459   0.50  18.81 ? 172 LYS A C   1 
ATOM   1362 O  O   A LYS A 1 172 ? 28.341 11.084  9.538   0.50  19.92 ? 172 LYS A O   1 
ATOM   1363 O  O   B LYS A 1 172 ? 28.445 11.062  9.590   0.50  19.24 ? 172 LYS A O   1 
ATOM   1364 C  CB  A LYS A 1 172 ? 25.877 9.529   10.469  0.50  20.22 ? 172 LYS A CB  1 
ATOM   1365 C  CB  B LYS A 1 172 ? 25.858 9.479   10.412  0.50  18.01 ? 172 LYS A CB  1 
ATOM   1366 C  CG  A LYS A 1 172 ? 25.231 9.207   9.142   0.50  20.25 ? 172 LYS A CG  1 
ATOM   1367 C  CG  B LYS A 1 172 ? 25.225 9.132   9.069   0.50  17.00 ? 172 LYS A CG  1 
ATOM   1368 C  CD  A LYS A 1 172 ? 23.950 10.022  8.994   0.50  21.68 ? 172 LYS A CD  1 
ATOM   1369 C  CD  B LYS A 1 172 ? 23.700 9.304   9.136   0.50  17.15 ? 172 LYS A CD  1 
ATOM   1370 C  CE  A LYS A 1 172 ? 22.923 9.248   8.217   0.50  22.38 ? 172 LYS A CE  1 
ATOM   1371 C  CE  B LYS A 1 172 ? 23.067 9.768   7.838   0.50  16.79 ? 172 LYS A CE  1 
ATOM   1372 N  NZ  A LYS A 1 172 ? 23.389 9.011   6.839   0.50  24.01 ? 172 LYS A NZ  1 
ATOM   1373 N  NZ  B LYS A 1 172 ? 21.561 9.806   7.944   0.50  16.80 ? 172 LYS A NZ  1 
ATOM   1374 N  N   . GLY A 1 173 ? 28.563 9.148   8.430   1.00  19.13 ? 173 GLY A N   1 
ATOM   1375 C  CA  . GLY A 1 173 ? 29.268 9.734   7.284   1.00  20.62 ? 173 GLY A CA  1 
ATOM   1376 C  C   . GLY A 1 173 ? 30.806 9.657   7.348   1.00  20.46 ? 173 GLY A C   1 
ATOM   1377 O  O   . GLY A 1 173 ? 31.460 9.782   6.317   1.00  21.55 ? 173 GLY A O   1 
ATOM   1378 N  N   . LYS A 1 174 ? 31.362 9.436   8.535   1.00  19.92 ? 174 LYS A N   1 
ATOM   1379 C  CA  . LYS A 1 174 ? 32.798 9.279   8.689   1.00  21.21 ? 174 LYS A CA  1 
ATOM   1380 C  C   . LYS A 1 174 ? 33.259 7.948   8.123   1.00  21.56 ? 174 LYS A C   1 
ATOM   1381 O  O   . LYS A 1 174 ? 32.465 6.995   8.085   1.00  18.00 ? 174 LYS A O   1 
ATOM   1382 C  CB  . LYS A 1 174 ? 33.199 9.346   10.149  1.00  22.54 ? 174 LYS A CB  1 
ATOM   1383 C  CG  . LYS A 1 174 ? 32.873 10.668  10.828  1.00  26.09 ? 174 LYS A CG  1 
ATOM   1384 C  CD  . LYS A 1 174 ? 33.900 11.745  10.529  1.00  33.74 ? 174 LYS A CD  1 
ATOM   1385 C  CE  . LYS A 1 174 ? 34.066 12.683  11.730  1.00  37.52 ? 174 LYS A CE  1 
ATOM   1386 N  NZ  . LYS A 1 174 ? 33.051 13.779  11.687  1.00  40.99 ? 174 LYS A NZ  1 
ATOM   1387 N  N   . GLN A 1 175 ? 34.531 7.882   7.696   1.00  18.33 ? 175 GLN A N   1 
ATOM   1388 C  CA  . GLN A 1 175 ? 35.065 6.638   7.155   1.00  20.04 ? 175 GLN A CA  1 
ATOM   1389 C  C   . GLN A 1 175 ? 36.562 6.548   7.368   1.00  21.21 ? 175 GLN A C   1 
ATOM   1390 O  O   . GLN A 1 175 ? 37.184 7.506   7.819   1.00  26.36 ? 175 GLN A O   1 
ATOM   1391 C  CB  . GLN A 1 175 ? 34.769 6.465   5.663   1.00  20.70 ? 175 GLN A CB  1 
ATOM   1392 C  CG  . GLN A 1 175 ? 35.074 7.673   4.763   1.00  19.03 ? 175 GLN A CG  1 
ATOM   1393 C  CD  . GLN A 1 175 ? 34.929 7.310   3.305   1.00  20.40 ? 175 GLN A CD  1 
ATOM   1394 O  OE1 . GLN A 1 175 ? 35.918 7.159   2.586   1.00  23.54 ? 175 GLN A OE1 1 
ATOM   1395 N  NE2 . GLN A 1 175 ? 33.731 7.125   2.865   1.00  19.03 ? 175 GLN A NE2 1 
ATOM   1396 N  N   . THR A 1 176 ? 37.134 5.397   7.059   1.00  21.14 ? 176 THR A N   1 
ATOM   1397 C  CA  . THR A 1 176 ? 38.562 5.219   7.203   1.00  21.20 ? 176 THR A CA  1 
ATOM   1398 C  C   . THR A 1 176 ? 39.083 4.046   6.373   1.00  21.96 ? 176 THR A C   1 
ATOM   1399 O  O   . THR A 1 176 ? 38.311 3.119   6.033   1.00  20.17 ? 176 THR A O   1 
ATOM   1400 C  CB  . THR A 1 176 ? 38.986 5.144   8.699   1.00  22.31 ? 176 THR A CB  1 
ATOM   1401 O  OG1 . THR A 1 176 ? 40.405 5.250   8.779   1.00  19.07 ? 176 THR A OG1 1 
ATOM   1402 C  CG2 . THR A 1 176 ? 38.538 3.762   9.304   1.00  19.75 ? 176 THR A CG2 1 
ATOM   1403 N  N   . ARG A 1 177 ? 40.372 4.122   5.962   1.00  19.82 ? 177 ARG A N   1 
ATOM   1404 C  CA  . ARG A 1 177 ? 41.024 3.058   5.120   1.00  19.32 ? 177 ARG A CA  1 
ATOM   1405 C  C   . ARG A 1 177 ? 40.832 1.723   5.804   1.00  21.20 ? 177 ARG A C   1 
ATOM   1406 O  O   . ARG A 1 177 ? 40.987 1.619   7.041   1.00  19.03 ? 177 ARG A O   1 
ATOM   1407 C  CB  . ARG A 1 177 ? 42.551 3.298   5.002   1.00  21.80 ? 177 ARG A CB  1 
ATOM   1408 C  CG  . ARG A 1 177 ? 43.346 2.192   4.248   1.00  23.34 ? 177 ARG A CG  1 
ATOM   1409 C  CD  . ARG A 1 177 ? 42.867 2.097   2.804   1.00  22.84 ? 177 ARG A CD  1 
ATOM   1410 N  NE  . ARG A 1 177 ? 43.745 1.288   1.946   1.00  24.20 ? 177 ARG A NE  1 
ATOM   1411 C  CZ  . ARG A 1 177 ? 43.357 0.731   0.802   1.00  25.28 ? 177 ARG A CZ  1 
ATOM   1412 N  NH1 . ARG A 1 177 ? 42.102 0.891   0.362   1.00  21.74 ? 177 ARG A NH1 1 
ATOM   1413 N  NH2 . ARG A 1 177 ? 44.239 0.023   0.071   1.00  27.50 ? 177 ARG A NH2 1 
ATOM   1414 N  N   . PHE A 1 178 ? 40.517 0.691   5.021   1.00  21.12 ? 178 PHE A N   1 
ATOM   1415 C  CA  . PHE A 1 178 ? 40.275 -0.620  5.622   1.00  19.43 ? 178 PHE A CA  1 
ATOM   1416 C  C   . PHE A 1 178 ? 40.548 -1.701  4.596   1.00  19.39 ? 178 PHE A C   1 
ATOM   1417 O  O   . PHE A 1 178 ? 39.793 -1.883  3.656   1.00  21.21 ? 178 PHE A O   1 
ATOM   1418 C  CB  . PHE A 1 178 ? 38.837 -0.663  6.153   1.00  19.08 ? 178 PHE A CB  1 
ATOM   1419 C  CG  . PHE A 1 178 ? 38.550 -1.859  7.037   1.00  17.92 ? 178 PHE A CG  1 
ATOM   1420 C  CD1 . PHE A 1 178 ? 38.834 -1.801  8.427   1.00  18.27 ? 178 PHE A CD1 1 
ATOM   1421 C  CD2 . PHE A 1 178 ? 37.976 -2.997  6.512   1.00  17.74 ? 178 PHE A CD2 1 
ATOM   1422 C  CE1 . PHE A 1 178 ? 38.587 -2.888  9.261   1.00  17.85 ? 178 PHE A CE1 1 
ATOM   1423 C  CE2 . PHE A 1 178 ? 37.731 -4.111  7.357   1.00  18.94 ? 178 PHE A CE2 1 
ATOM   1424 C  CZ  . PHE A 1 178 ? 38.025 -4.038  8.713   1.00  18.15 ? 178 PHE A CZ  1 
ATOM   1425 N  N   . THR A 1 179 ? 41.695 -2.366  4.722   1.00  21.69 ? 179 THR A N   1 
ATOM   1426 C  CA  . THR A 1 179 ? 42.085 -3.369  3.722   1.00  22.27 ? 179 THR A CA  1 
ATOM   1427 C  C   . THR A 1 179 ? 42.849 -4.523  4.365   1.00  21.24 ? 179 THR A C   1 
ATOM   1428 O  O   . THR A 1 179 ? 43.142 -4.503  5.567   1.00  22.55 ? 179 THR A O   1 
ATOM   1429 C  CB  . THR A 1 179 ? 42.938 -2.759  2.561   1.00  20.01 ? 179 THR A CB  1 
ATOM   1430 O  OG1 . THR A 1 179 ? 42.983 -3.683  1.474   1.00  21.22 ? 179 THR A OG1 1 
ATOM   1431 C  CG2 . THR A 1 179 ? 44.359 -2.485  3.018   1.00  23.19 ? 179 THR A CG2 1 
ATOM   1432 N  N   . ASN A 1 180 ? 43.175 -5.537  3.572   1.00  23.35 ? 180 ASN A N   1 
ATOM   1433 C  CA  . ASN A 1 180 ? 43.774 -6.730  4.168   1.00  26.10 ? 180 ASN A CA  1 
ATOM   1434 C  C   . ASN A 1 180 ? 42.831 -7.366  5.165   1.00  23.99 ? 180 ASN A C   1 
ATOM   1435 O  O   . ASN A 1 180 ? 43.199 -7.674  6.317   1.00  20.40 ? 180 ASN A O   1 
ATOM   1436 C  CB  . ASN A 1 180 ? 45.045 -6.338  4.890   1.00  31.52 ? 180 ASN A CB  1 
ATOM   1437 C  CG  . ASN A 1 180 ? 46.221 -6.839  4.183   1.00  41.95 ? 180 ASN A CG  1 
ATOM   1438 O  OD1 . ASN A 1 180 ? 46.711 -7.936  4.507   1.00  49.14 ? 180 ASN A OD1 1 
ATOM   1439 N  ND2 . ASN A 1 180 ? 46.620 -6.127  3.119   1.00  42.17 ? 180 ASN A ND2 1 
ATOM   1440 N  N   . PHE A 1 181 ? 41.585 -7.500  4.715   1.00  26.38 ? 181 PHE A N   1 
ATOM   1441 C  CA  . PHE A 1 181 ? 40.467 -7.939  5.558   1.00  21.72 ? 181 PHE A CA  1 
ATOM   1442 C  C   . PHE A 1 181 ? 40.253 -9.377  5.234   1.00  22.97 ? 181 PHE A C   1 
ATOM   1443 O  O   . PHE A 1 181 ? 39.908 -9.727  4.082   1.00  22.68 ? 181 PHE A O   1 
ATOM   1444 C  CB  . PHE A 1 181 ? 39.255 -7.089  5.199   1.00  24.37 ? 181 PHE A CB  1 
ATOM   1445 C  CG  . PHE A 1 181 ? 37.995 -7.442  5.957   1.00  21.22 ? 181 PHE A CG  1 
ATOM   1446 C  CD1 . PHE A 1 181 ? 38.057 -7.802  7.292   1.00  21.16 ? 181 PHE A CD1 1 
ATOM   1447 C  CD2 . PHE A 1 181 ? 36.753 -7.376  5.312   1.00  22.14 ? 181 PHE A CD2 1 
ATOM   1448 C  CE1 . PHE A 1 181 ? 36.905 -8.127  7.984   1.00  21.89 ? 181 PHE A CE1 1 
ATOM   1449 C  CE2 . PHE A 1 181 ? 35.580 -7.666  6.000   1.00  20.61 ? 181 PHE A CE2 1 
ATOM   1450 C  CZ  . PHE A 1 181 ? 35.662 -8.048  7.332   1.00  20.78 ? 181 PHE A CZ  1 
ATOM   1451 N  N   A ASP A 1 182 ? 40.504 -10.201 6.250   0.50  23.72 ? 182 ASP A N   1 
ATOM   1452 N  N   B ASP A 1 182 ? 40.448 -10.248 6.225   0.50  22.63 ? 182 ASP A N   1 
ATOM   1453 C  CA  A ASP A 1 182 ? 40.219 -11.627 6.247   0.50  25.98 ? 182 ASP A CA  1 
ATOM   1454 C  CA  B ASP A 1 182 ? 40.255 -11.698 6.035   0.50  23.88 ? 182 ASP A CA  1 
ATOM   1455 C  C   A ASP A 1 182 ? 38.721 -11.820 6.536   0.50  25.25 ? 182 ASP A C   1 
ATOM   1456 C  C   B ASP A 1 182 ? 38.820 -12.179 6.285   0.50  24.20 ? 182 ASP A C   1 
ATOM   1457 O  O   A ASP A 1 182 ? 38.314 -12.103 7.679   0.50  22.35 ? 182 ASP A O   1 
ATOM   1458 O  O   B ASP A 1 182 ? 38.549 -13.033 7.145   0.50  22.07 ? 182 ASP A O   1 
ATOM   1459 C  CB  A ASP A 1 182 ? 41.104 -12.314 7.320   0.50  27.36 ? 182 ASP A CB  1 
ATOM   1460 C  CB  B ASP A 1 182 ? 41.253 -12.494 6.889   0.50  23.36 ? 182 ASP A CB  1 
ATOM   1461 C  CG  A ASP A 1 182 ? 41.125 -13.836 7.215   0.50  30.70 ? 182 ASP A CG  1 
ATOM   1462 C  CG  B ASP A 1 182 ? 42.681 -12.217 6.497   0.50  23.86 ? 182 ASP A CG  1 
ATOM   1463 O  OD1 A ASP A 1 182 ? 40.477 -14.394 6.311   0.50  32.18 ? 182 ASP A OD1 1 
ATOM   1464 O  OD1 B ASP A 1 182 ? 42.905 -11.905 5.306   0.50  22.98 ? 182 ASP A OD1 1 
ATOM   1465 O  OD2 A ASP A 1 182 ? 41.793 -14.486 8.051   0.50  31.12 ? 182 ASP A OD2 1 
ATOM   1466 O  OD2 B ASP A 1 182 ? 43.563 -12.266 7.380   0.50  25.23 ? 182 ASP A OD2 1 
ATOM   1467 N  N   . LEU A 1 183 ? 37.911 -11.633 5.495   1.00  25.48 ? 183 LEU A N   1 
ATOM   1468 C  CA  . LEU A 1 183 ? 36.467 -11.981 5.541   1.00  24.55 ? 183 LEU A CA  1 
ATOM   1469 C  C   . LEU A 1 183 ? 36.169 -13.496 5.639   1.00  25.05 ? 183 LEU A C   1 
ATOM   1470 O  O   . LEU A 1 183 ? 35.205 -13.896 6.293   1.00  22.32 ? 183 LEU A O   1 
ATOM   1471 C  CB  . LEU A 1 183 ? 35.733 -11.367 4.334   1.00  21.71 ? 183 LEU A CB  1 
ATOM   1472 C  CG  . LEU A 1 183 ? 34.236 -11.543 4.151   1.00  18.79 ? 183 LEU A CG  1 
ATOM   1473 C  CD1 . LEU A 1 183 ? 33.575 -10.870 5.348   1.00  18.67 ? 183 LEU A CD1 1 
ATOM   1474 C  CD2 . LEU A 1 183 ? 33.779 -10.965 2.799   1.00  18.69 ? 183 LEU A CD2 1 
ATOM   1475 N  N   . LEU A 1 184 ? 36.985 -14.349 5.014   1.00  23.25 ? 184 LEU A N   1 
ATOM   1476 C  CA  . LEU A 1 184 ? 36.706 -15.760 5.090   1.00  22.45 ? 184 LEU A CA  1 
ATOM   1477 C  C   . LEU A 1 184 ? 36.758 -16.265 6.543   1.00  23.32 ? 184 LEU A C   1 
ATOM   1478 O  O   . LEU A 1 184 ? 36.144 -17.310 6.851   1.00  22.79 ? 184 LEU A O   1 
ATOM   1479 C  CB  . LEU A 1 184 ? 37.665 -16.570 4.198   1.00  23.67 ? 184 LEU A CB  1 
ATOM   1480 C  CG  . LEU A 1 184 ? 37.368 -16.465 2.691   1.00  25.51 ? 184 LEU A CG  1 
ATOM   1481 C  CD1 . LEU A 1 184 ? 38.267 -17.394 1.889   1.00  26.56 ? 184 LEU A CD1 1 
ATOM   1482 C  CD2 . LEU A 1 184 ? 35.908 -16.781 2.447   1.00  24.64 ? 184 LEU A CD2 1 
ATOM   1483 N  N   . SER A 1 185 ? 37.477 -15.537 7.398   1.00  19.29 ? 185 SER A N   1 
ATOM   1484 C  CA  . SER A 1 185 ? 37.608 -15.927 8.755   1.00  24.95 ? 185 SER A CA  1 
ATOM   1485 C  C   . SER A 1 185 ? 36.456 -15.472 9.623   1.00  24.48 ? 185 SER A C   1 
ATOM   1486 O  O   . SER A 1 185 ? 36.417 -15.808 10.780  1.00  23.29 ? 185 SER A O   1 
ATOM   1487 C  CB  . SER A 1 185 ? 38.966 -15.487 9.320   1.00  30.98 ? 185 SER A CB  1 
ATOM   1488 O  OG  . SER A 1 185 ? 38.928 -14.101 9.514   1.00  37.61 ? 185 SER A OG  1 
ATOM   1489 N  N   . LEU A 1 186 ? 35.508 -14.708 9.055   1.00  23.88 ? 186 LEU A N   1 
ATOM   1490 C  CA  . LEU A 1 186 ? 34.210 -14.459 9.682   1.00  20.66 ? 186 LEU A CA  1 
ATOM   1491 C  C   . LEU A 1 186 ? 33.131 -15.402 9.184   1.00  21.86 ? 186 LEU A C   1 
ATOM   1492 O  O   . LEU A 1 186 ? 31.909 -15.173 9.406   1.00  19.60 ? 186 LEU A O   1 
ATOM   1493 C  CB  . LEU A 1 186 ? 33.758 -13.029 9.430   1.00  21.01 ? 186 LEU A CB  1 
ATOM   1494 C  CG  . LEU A 1 186 ? 34.663 -11.928 9.955   1.00  21.31 ? 186 LEU A CG  1 
ATOM   1495 C  CD1 . LEU A 1 186 ? 34.149 -10.559 9.563   1.00  21.24 ? 186 LEU A CD1 1 
ATOM   1496 C  CD2 . LEU A 1 186 ? 34.879 -12.033 11.458  1.00  21.45 ? 186 LEU A CD2 1 
ATOM   1497 N  N   . LEU A 1 187 ? 33.550 -16.477 8.540   1.00  20.16 ? 187 LEU A N   1 
ATOM   1498 C  CA  . LEU A 1 187 ? 32.637 -17.534 8.242   1.00  19.63 ? 187 LEU A CA  1 
ATOM   1499 C  C   . LEU A 1 187 ? 32.956 -18.701 9.155   1.00  18.94 ? 187 LEU A C   1 
ATOM   1500 O  O   . LEU A 1 187 ? 34.139 -18.931 9.457   1.00  21.50 ? 187 LEU A O   1 
ATOM   1501 C  CB  . LEU A 1 187 ? 32.753 -17.975 6.768   1.00  21.05 ? 187 LEU A CB  1 
ATOM   1502 C  CG  . LEU A 1 187 ? 32.654 -16.825 5.731   1.00  24.13 ? 187 LEU A CG  1 
ATOM   1503 C  CD1 . LEU A 1 187 ? 33.009 -17.367 4.355   1.00  23.72 ? 187 LEU A CD1 1 
ATOM   1504 C  CD2 . LEU A 1 187 ? 31.292 -16.234 5.712   1.00  21.82 ? 187 LEU A CD2 1 
ATOM   1505 N  N   . PRO A 1 188 ? 31.913 -19.465 9.540   1.00  19.17 ? 188 PRO A N   1 
ATOM   1506 C  CA  . PRO A 1 188 ? 32.099 -20.651 10.344  1.00  19.74 ? 188 PRO A CA  1 
ATOM   1507 C  C   . PRO A 1 188 ? 32.734 -21.794 9.504   1.00  20.32 ? 188 PRO A C   1 
ATOM   1508 O  O   . PRO A 1 188 ? 32.761 -21.731 8.251   1.00  19.38 ? 188 PRO A O   1 
ATOM   1509 C  CB  . PRO A 1 188 ? 30.674 -21.018 10.744  1.00  18.00 ? 188 PRO A CB  1 
ATOM   1510 C  CG  . PRO A 1 188 ? 29.853 -20.610 9.550   1.00  17.25 ? 188 PRO A CG  1 
ATOM   1511 C  CD  . PRO A 1 188 ? 30.491 -19.281 9.173   1.00  16.27 ? 188 PRO A CD  1 
ATOM   1512 N  N   . PRO A 1 189 ? 33.201 -22.846 10.194  1.00  20.17 ? 189 PRO A N   1 
ATOM   1513 C  CA  . PRO A 1 189 ? 33.818 -23.956 9.510   1.00  20.10 ? 189 PRO A CA  1 
ATOM   1514 C  C   . PRO A 1 189 ? 32.833 -24.756 8.723   1.00  21.31 ? 189 PRO A C   1 
ATOM   1515 O  O   . PRO A 1 189 ? 33.200 -25.373 7.714   1.00  23.50 ? 189 PRO A O   1 
ATOM   1516 C  CB  . PRO A 1 189 ? 34.418 -24.825 10.635  1.00  20.13 ? 189 PRO A CB  1 
ATOM   1517 C  CG  . PRO A 1 189 ? 33.982 -24.235 11.942  1.00  19.70 ? 189 PRO A CG  1 
ATOM   1518 C  CD  . PRO A 1 189 ? 33.456 -22.835 11.655  1.00  19.40 ? 189 PRO A CD  1 
ATOM   1519 N  N   . SER A 1 190 ? 31.578 -24.744 9.124   1.00  19.44 ? 190 SER A N   1 
ATOM   1520 C  CA  . SER A 1 190 ? 30.597 -25.486 8.349   1.00  17.89 ? 190 SER A CA  1 
ATOM   1521 C  C   . SER A 1 190 ? 29.831 -24.544 7.429   1.00  21.17 ? 190 SER A C   1 
ATOM   1522 O  O   . SER A 1 190 ? 29.229 -23.580 7.906   1.00  17.92 ? 190 SER A O   1 
ATOM   1523 C  CB  . SER A 1 190 ? 29.612 -26.243 9.258   1.00  19.07 ? 190 SER A CB  1 
ATOM   1524 O  OG  . SER A 1 190 ? 28.438 -26.579 8.506   1.00  19.61 ? 190 SER A OG  1 
ATOM   1525 N  N   . TRP A 1 191 ? 29.867 -24.780 6.117   1.00  19.15 ? 191 TRP A N   1 
ATOM   1526 C  CA  . TRP A 1 191 ? 29.127 -23.878 5.219   1.00  18.19 ? 191 TRP A CA  1 
ATOM   1527 C  C   . TRP A 1 191 ? 27.746 -24.366 4.834   1.00  18.41 ? 191 TRP A C   1 
ATOM   1528 O  O   . TRP A 1 191 ? 27.273 -23.926 3.799   1.00  19.58 ? 191 TRP A O   1 
ATOM   1529 C  CB  . TRP A 1 191 ? 29.939 -23.577 3.958   1.00  17.32 ? 191 TRP A CB  1 
ATOM   1530 C  CG  . TRP A 1 191 ? 31.144 -22.692 4.192   1.00  15.84 ? 191 TRP A CG  1 
ATOM   1531 C  CD1 . TRP A 1 191 ? 31.556 -22.115 5.383   1.00  15.01 ? 191 TRP A CD1 1 
ATOM   1532 C  CD2 . TRP A 1 191 ? 32.118 -22.229 3.188   1.00  16.32 ? 191 TRP A CD2 1 
ATOM   1533 N  NE1 . TRP A 1 191 ? 32.686 -21.377 5.222   1.00  15.72 ? 191 TRP A NE1 1 
ATOM   1534 C  CE2 . TRP A 1 191 ? 33.051 -21.367 3.896   1.00  15.67 ? 191 TRP A CE2 1 
ATOM   1535 C  CE3 . TRP A 1 191 ? 32.267 -22.408 1.808   1.00  15.95 ? 191 TRP A CE3 1 
ATOM   1536 C  CZ2 . TRP A 1 191 ? 34.130 -20.779 3.263   1.00  17.83 ? 191 TRP A CZ2 1 
ATOM   1537 C  CZ3 . TRP A 1 191 ? 33.349 -21.778 1.194   1.00  13.96 ? 191 TRP A CZ3 1 
ATOM   1538 C  CH2 . TRP A 1 191 ? 34.239 -20.988 1.889   1.00  15.47 ? 191 TRP A CH2 1 
ATOM   1539 N  N   . ASP A 1 192 ? 27.079 -25.198 5.663   1.00  16.09 ? 192 ASP A N   1 
ATOM   1540 C  CA  . ASP A 1 192 ? 25.689 -25.619 5.438   1.00  17.43 ? 192 ASP A CA  1 
ATOM   1541 C  C   . ASP A 1 192 ? 24.853 -24.301 5.560   1.00  16.66 ? 192 ASP A C   1 
ATOM   1542 O  O   . ASP A 1 192 ? 25.219 -23.380 6.339   1.00  15.65 ? 192 ASP A O   1 
ATOM   1543 C  CB  . ASP A 1 192 ? 25.155 -26.568 6.544   1.00  19.09 ? 192 ASP A CB  1 
ATOM   1544 C  CG  . ASP A 1 192 ? 25.809 -27.987 6.578   1.00  24.72 ? 192 ASP A CG  1 
ATOM   1545 O  OD1 . ASP A 1 192 ? 26.268 -28.482 5.542   1.00  22.06 ? 192 ASP A OD1 1 
ATOM   1546 O  OD2 . ASP A 1 192 ? 25.793 -28.618 7.679   1.00  24.64 ? 192 ASP A OD2 1 
ATOM   1547 N  N   . TYR A 1 193 ? 23.725 -24.239 4.839   1.00  16.13 ? 193 TYR A N   1 
ATOM   1548 C  CA  . TYR A 1 193 ? 22.936 -23.004 4.711   1.00  15.28 ? 193 TYR A CA  1 
ATOM   1549 C  C   . TYR A 1 193 ? 21.474 -23.300 4.375   1.00  14.79 ? 193 TYR A C   1 
ATOM   1550 O  O   . TYR A 1 193 ? 21.088 -24.401 3.888   1.00  14.54 ? 193 TYR A O   1 
ATOM   1551 C  CB  . TYR A 1 193 ? 23.592 -22.041 3.645   1.00  14.72 ? 193 TYR A CB  1 
ATOM   1552 C  CG  . TYR A 1 193 ? 23.477 -22.632 2.243   1.00  14.93 ? 193 TYR A CG  1 
ATOM   1553 C  CD1 . TYR A 1 193 ? 22.316 -22.433 1.467   1.00  15.20 ? 193 TYR A CD1 1 
ATOM   1554 C  CD2 . TYR A 1 193 ? 24.545 -23.387 1.697   1.00  14.24 ? 193 TYR A CD2 1 
ATOM   1555 C  CE1 . TYR A 1 193 ? 22.201 -22.982 0.191   1.00  16.34 ? 193 TYR A CE1 1 
ATOM   1556 C  CE2 . TYR A 1 193 ? 24.434 -23.952 0.445   1.00  16.32 ? 193 TYR A CE2 1 
ATOM   1557 C  CZ  . TYR A 1 193 ? 23.281 -23.759 -0.313  1.00  16.73 ? 193 TYR A CZ  1 
ATOM   1558 O  OH  . TYR A 1 193 ? 23.189 -24.335 -1.542  1.00  16.17 ? 193 TYR A OH  1 
ATOM   1559 N  N   . TRP A 1 194 ? 20.655 -22.316 4.672   1.00  13.42 ? 194 TRP A N   1 
ATOM   1560 C  CA  . TRP A 1 194 ? 19.286 -22.265 4.211   1.00  13.03 ? 194 TRP A CA  1 
ATOM   1561 C  C   . TRP A 1 194 ? 19.193 -21.178 3.193   1.00  12.15 ? 194 TRP A C   1 
ATOM   1562 O  O   . TRP A 1 194 ? 19.954 -20.217 3.223   1.00  12.92 ? 194 TRP A O   1 
ATOM   1563 C  CB  . TRP A 1 194 ? 18.329 -21.860 5.334   1.00  13.54 ? 194 TRP A CB  1 
ATOM   1564 C  CG  . TRP A 1 194 ? 18.267 -22.843 6.485   1.00  13.73 ? 194 TRP A CG  1 
ATOM   1565 C  CD1 . TRP A 1 194 ? 17.664 -24.087 6.474   1.00  13.95 ? 194 TRP A CD1 1 
ATOM   1566 C  CD2 . TRP A 1 194 ? 18.835 -22.696 7.836   1.00  13.62 ? 194 TRP A CD2 1 
ATOM   1567 N  NE1 . TRP A 1 194 ? 17.796 -24.695 7.704   1.00  13.67 ? 194 TRP A NE1 1 
ATOM   1568 C  CE2 . TRP A 1 194 ? 18.478 -23.897 8.556   1.00  13.84 ? 194 TRP A CE2 1 
ATOM   1569 C  CE3 . TRP A 1 194 ? 19.513 -21.689 8.506   1.00  15.10 ? 194 TRP A CE3 1 
ATOM   1570 C  CZ2 . TRP A 1 194 ? 18.822 -24.088 9.890   1.00  14.38 ? 194 TRP A CZ2 1 
ATOM   1571 C  CZ3 . TRP A 1 194 ? 19.857 -21.885 9.851   1.00  14.75 ? 194 TRP A CZ3 1 
ATOM   1572 C  CH2 . TRP A 1 194 ? 19.504 -23.055 10.515  1.00  14.79 ? 194 TRP A CH2 1 
ATOM   1573 N  N   . THR A 1 195 ? 18.226 -21.294 2.307   1.00  12.84 ? 195 THR A N   1 
ATOM   1574 C  CA  . THR A 1 195 ? 18.093 -20.219 1.280   1.00  12.46 ? 195 THR A CA  1 
ATOM   1575 C  C   . THR A 1 195 ? 16.636 -19.939 0.935   1.00  11.92 ? 195 THR A C   1 
ATOM   1576 O  O   . THR A 1 195 ? 15.824 -20.846 0.877   1.00  14.10 ? 195 THR A O   1 
ATOM   1577 C  CB  . THR A 1 195 ? 18.944 -20.552 0.053   1.00  13.02 ? 195 THR A CB  1 
ATOM   1578 O  OG1 . THR A 1 195 ? 18.788 -19.555 -0.998  1.00  13.12 ? 195 THR A OG1 1 
ATOM   1579 C  CG2 . THR A 1 195 ? 18.581 -21.988 -0.483  1.00  13.73 ? 195 THR A CG2 1 
ATOM   1580 N  N   . TYR A 1 196 ? 16.312 -18.669 0.691   1.00  11.69 ? 196 TYR A N   1 
ATOM   1581 C  CA  . TYR A 1 196 ? 14.940 -18.305 0.267   1.00  11.54 ? 196 TYR A CA  1 
ATOM   1582 C  C   . TYR A 1 196 ? 14.984 -17.009 -0.493  1.00  11.21 ? 196 TYR A C   1 
ATOM   1583 O  O   . TYR A 1 196 ? 15.947 -16.233 -0.368  1.00  10.93 ? 196 TYR A O   1 
ATOM   1584 C  CB  . TYR A 1 196 ? 13.992 -18.204 1.508   1.00  11.31 ? 196 TYR A CB  1 
ATOM   1585 C  CG  . TYR A 1 196 ? 14.272 -16.974 2.352   1.00  11.27 ? 196 TYR A CG  1 
ATOM   1586 C  CD1 . TYR A 1 196 ? 15.271 -16.973 3.311   1.00  11.12 ? 196 TYR A CD1 1 
ATOM   1587 C  CD2 . TYR A 1 196 ? 13.530 -15.800 2.156   1.00  11.33 ? 196 TYR A CD2 1 
ATOM   1588 C  CE1 . TYR A 1 196 ? 15.520 -15.835 4.074   1.00  10.66 ? 196 TYR A CE1 1 
ATOM   1589 C  CE2 . TYR A 1 196 ? 13.755 -14.675 2.932   1.00  11.73 ? 196 TYR A CE2 1 
ATOM   1590 C  CZ  . TYR A 1 196 ? 14.762 -14.695 3.866   1.00  11.17 ? 196 TYR A CZ  1 
ATOM   1591 O  OH  . TYR A 1 196 ? 15.036 -13.540 4.548   1.00  10.39 ? 196 TYR A OH  1 
ATOM   1592 N  N   . PRO A 1 197 ? 13.946 -16.728 -1.301  1.00  12.02 ? 197 PRO A N   1 
ATOM   1593 C  CA  . PRO A 1 197 ? 13.993 -15.413 -1.974  1.00  11.87 ? 197 PRO A CA  1 
ATOM   1594 C  C   . PRO A 1 197 ? 13.400 -14.258 -1.092  1.00  12.35 ? 197 PRO A C   1 
ATOM   1595 O  O   . PRO A 1 197 ? 12.381 -14.448 -0.438  1.00  12.08 ? 197 PRO A O   1 
ATOM   1596 C  CB  . PRO A 1 197 ? 13.086 -15.661 -3.213  1.00  11.72 ? 197 PRO A CB  1 
ATOM   1597 C  CG  . PRO A 1 197 ? 12.056 -16.630 -2.691  1.00  11.69 ? 197 PRO A CG  1 
ATOM   1598 C  CD  . PRO A 1 197 ? 12.897 -17.599 -1.861  1.00  11.53 ? 197 PRO A CD  1 
ATOM   1599 N  N   . GLY A 1 198 ? 14.021 -13.085 -1.081  1.00  11.55 ? 198 GLY A N   1 
ATOM   1600 C  CA  . GLY A 1 198 ? 13.604 -12.032 -0.138  1.00  11.62 ? 198 GLY A CA  1 
ATOM   1601 C  C   . GLY A 1 198 ? 14.128 -10.702 -0.596  1.00  12.08 ? 198 GLY A C   1 
ATOM   1602 O  O   . GLY A 1 198 ? 14.220 -10.432 -1.820  1.00  12.06 ? 198 GLY A O   1 
ATOM   1603 N  N   . SER A 1 199 ? 14.496 -9.847  0.360   1.00  11.80 ? 199 SER A N   1 
ATOM   1604 C  CA  . SER A 1 199 ? 14.626 -8.417  0.072   1.00  10.93 ? 199 SER A CA  1 
ATOM   1605 C  C   . SER A 1 199 ? 15.768 -7.832  0.853   1.00  11.71 ? 199 SER A C   1 
ATOM   1606 O  O   . SER A 1 199 ? 16.283 -8.486  1.769   1.00  11.77 ? 199 SER A O   1 
ATOM   1607 C  CB  . SER A 1 199 ? 13.331 -7.687  0.508   1.00  11.66 ? 199 SER A CB  1 
ATOM   1608 O  OG  . SER A 1 199 ? 13.220 -7.540  1.931   1.00  13.08 ? 199 SER A OG  1 
ATOM   1609 N  N   . LEU A 1 200 ? 16.164 -6.599  0.536   1.00  11.13 ? 200 LEU A N   1 
ATOM   1610 C  CA  . LEU A 1 200 ? 16.907 -5.778  1.510   1.00  11.50 ? 200 LEU A CA  1 
ATOM   1611 C  C   . LEU A 1 200 ? 16.130 -5.671  2.812   1.00  11.08 ? 200 LEU A C   1 
ATOM   1612 O  O   . LEU A 1 200 ? 14.882 -5.686  2.793   1.00  12.06 ? 200 LEU A O   1 
ATOM   1613 C  CB  . LEU A 1 200 ? 17.186 -4.358  0.938   1.00  12.71 ? 200 LEU A CB  1 
ATOM   1614 C  CG  . LEU A 1 200 ? 17.687 -4.302  -0.494  1.00  12.74 ? 200 LEU A CG  1 
ATOM   1615 C  CD1 . LEU A 1 200 ? 17.919 -2.828  -0.836  1.00  13.00 ? 200 LEU A CD1 1 
ATOM   1616 C  CD2 . LEU A 1 200 ? 18.964 -5.142  -0.608  1.00  12.53 ? 200 LEU A CD2 1 
ATOM   1617 N  N   . THR A 1 201 ? 16.832 -5.623  3.943   1.00  11.09 ? 201 THR A N   1 
ATOM   1618 C  CA  . THR A 1 201 ? 16.129 -5.516  5.254   1.00  10.04 ? 201 THR A CA  1 
ATOM   1619 C  C   . THR A 1 201 ? 16.133 -4.041  5.708   1.00  10.13 ? 201 THR A C   1 
ATOM   1620 O  O   . THR A 1 201 ? 15.692 -3.742  6.800   1.00  9.99  ? 201 THR A O   1 
ATOM   1621 C  CB  . THR A 1 201 ? 16.753 -6.412  6.322   1.00  10.05 ? 201 THR A CB  1 
ATOM   1622 O  OG1 . THR A 1 201 ? 18.059 -5.909  6.641   1.00  10.42 ? 201 THR A OG1 1 
ATOM   1623 C  CG2 . THR A 1 201 ? 16.890 -7.906  5.840   1.00  9.82  ? 201 THR A CG2 1 
ATOM   1624 N  N   . VAL A 1 202 ? 16.612 -3.120  4.862   1.00  10.73 ? 202 VAL A N   1 
ATOM   1625 C  CA  . VAL A 1 202 ? 16.504 -1.681  5.110   1.00  11.53 ? 202 VAL A CA  1 
ATOM   1626 C  C   . VAL A 1 202 ? 15.844 -1.087  3.893   1.00  11.42 ? 202 VAL A C   1 
ATOM   1627 O  O   . VAL A 1 202 ? 15.962 -1.663  2.810   1.00  12.31 ? 202 VAL A O   1 
ATOM   1628 C  CB  . VAL A 1 202 ? 17.890 -0.951  5.302   1.00  11.80 ? 202 VAL A CB  1 
ATOM   1629 C  CG1 . VAL A 1 202 ? 18.583 -1.405  6.606   1.00  11.25 ? 202 VAL A CG1 1 
ATOM   1630 C  CG2 . VAL A 1 202 ? 18.834 -1.177  4.114   1.00  13.00 ? 202 VAL A CG2 1 
ATOM   1631 N  N   . PRO A 1 203 ? 15.204 0.079   4.040   1.00  11.53 ? 203 PRO A N   1 
ATOM   1632 C  CA  . PRO A 1 203 ? 14.733 0.824   2.883   1.00  10.91 ? 203 PRO A CA  1 
ATOM   1633 C  C   . PRO A 1 203 ? 15.892 0.984   1.865   1.00  11.60 ? 203 PRO A C   1 
ATOM   1634 O  O   . PRO A 1 203 ? 17.037 1.264   2.285   1.00  10.86 ? 203 PRO A O   1 
ATOM   1635 C  CB  . PRO A 1 203 ? 14.386 2.205   3.518   1.00  11.93 ? 203 PRO A CB  1 
ATOM   1636 C  CG  . PRO A 1 203 ? 13.775 1.819   4.873   1.00  12.04 ? 203 PRO A CG  1 
ATOM   1637 C  CD  . PRO A 1 203 ? 14.827 0.767   5.325   1.00  11.98 ? 203 PRO A CD  1 
ATOM   1638 N  N   . PRO A 1 204 ? 15.631 0.818   0.547   1.00  11.25 ? 204 PRO A N   1 
ATOM   1639 C  CA  . PRO A 1 204 ? 14.372 0.716   -0.202  1.00  11.67 ? 204 PRO A CA  1 
ATOM   1640 C  C   . PRO A 1 204 ? 13.700 -0.659  -0.195  1.00  11.66 ? 204 PRO A C   1 
ATOM   1641 O  O   . PRO A 1 204 ? 12.667 -0.845  -0.872  1.00  11.96 ? 204 PRO A O   1 
ATOM   1642 C  CB  . PRO A 1 204 ? 14.786 1.120   -1.637  1.00  12.27 ? 204 PRO A CB  1 
ATOM   1643 C  CG  . PRO A 1 204 ? 16.223 0.722   -1.733  1.00  11.78 ? 204 PRO A CG  1 
ATOM   1644 C  CD  . PRO A 1 204 ? 16.794 0.894   -0.344  1.00  12.22 ? 204 PRO A CD  1 
ATOM   1645 N  N   . LEU A 1 205 ? 14.202 -1.612  0.610   1.00  11.28 ? 205 LEU A N   1 
ATOM   1646 C  CA  . LEU A 1 205 ? 13.469 -2.876  0.815   1.00  9.48  ? 205 LEU A CA  1 
ATOM   1647 C  C   . LEU A 1 205 ? 13.229 -3.640  -0.495  1.00  10.27 ? 205 LEU A C   1 
ATOM   1648 O  O   . LEU A 1 205 ? 12.297 -4.430  -0.597  1.00  10.37 ? 205 LEU A O   1 
ATOM   1649 C  CB  . LEU A 1 205 ? 12.141 -2.620  1.601   1.00  10.02 ? 205 LEU A CB  1 
ATOM   1650 C  CG  . LEU A 1 205 ? 12.342 -2.030  3.010   1.00  9.57  ? 205 LEU A CG  1 
ATOM   1651 C  CD1 . LEU A 1 205 ? 10.993 -1.504  3.602   1.00  10.38 ? 205 LEU A CD1 1 
ATOM   1652 C  CD2 . LEU A 1 205 ? 12.933 -3.159  3.907   1.00  9.61  ? 205 LEU A CD2 1 
ATOM   1653 N  N   . LEU A 1 206 ? 14.088 -3.453  -1.490  1.00  11.94 ? 206 LEU A N   1 
ATOM   1654 C  CA  . LEU A 1 206 ? 13.896 -4.091  -2.810  1.00  11.70 ? 206 LEU A CA  1 
ATOM   1655 C  C   . LEU A 1 206 ? 13.941 -5.618  -2.748  1.00  12.82 ? 206 LEU A C   1 
ATOM   1656 O  O   . LEU A 1 206 ? 14.763 -6.205  -2.027  1.00  12.59 ? 206 LEU A O   1 
ATOM   1657 C  CB  . LEU A 1 206 ? 14.957 -3.567  -3.774  1.00  11.87 ? 206 LEU A CB  1 
ATOM   1658 C  CG  . LEU A 1 206 ? 14.867 -2.039  -3.980  1.00  12.33 ? 206 LEU A CG  1 
ATOM   1659 C  CD1 . LEU A 1 206 ? 16.146 -1.546  -4.618  1.00  12.39 ? 206 LEU A CD1 1 
ATOM   1660 C  CD2 . LEU A 1 206 ? 13.572 -1.538  -4.695  1.00  11.38 ? 206 LEU A CD2 1 
ATOM   1661 N  N   . GLU A 1 207 ? 13.015 -6.258  -3.477  1.00  13.63 ? 207 GLU A N   1 
ATOM   1662 C  CA  . GLU A 1 207 ? 12.884 -7.718  -3.454  1.00  14.25 ? 207 GLU A CA  1 
ATOM   1663 C  C   . GLU A 1 207 ? 13.803 -8.222  -4.568  1.00  14.07 ? 207 GLU A C   1 
ATOM   1664 O  O   . GLU A 1 207 ? 13.357 -8.713  -5.585  1.00  15.44 ? 207 GLU A O   1 
ATOM   1665 C  CB  . GLU A 1 207 ? 11.416 -8.169  -3.523  1.00  14.42 ? 207 GLU A CB  1 
ATOM   1666 C  CG  . GLU A 1 207 ? 10.569 -7.479  -2.402  1.00  14.65 ? 207 GLU A CG  1 
ATOM   1667 C  CD  . GLU A 1 207 ? 9.101  -7.764  -2.427  1.00  15.39 ? 207 GLU A CD  1 
ATOM   1668 O  OE1 . GLU A 1 207 ? 8.526  -7.935  -3.537  1.00  16.43 ? 207 GLU A OE1 1 
ATOM   1669 O  OE2 . GLU A 1 207 ? 8.494  -7.896  -1.333  1.00  12.92 ? 207 GLU A OE2 1 
ATOM   1670 N  N   . SER A 1 208 ? 15.103 -8.117  -4.297  1.00  13.11 ? 208 SER A N   1 
ATOM   1671 C  CA  . SER A 1 208 ? 16.132 -8.531  -5.229  1.00  13.88 ? 208 SER A CA  1 
ATOM   1672 C  C   . SER A 1 208 ? 17.140 -9.529  -4.645  1.00  13.39 ? 208 SER A C   1 
ATOM   1673 O  O   . SER A 1 208 ? 18.162 -9.783  -5.265  1.00  14.51 ? 208 SER A O   1 
ATOM   1674 C  CB  . SER A 1 208 ? 16.887 -7.299  -5.761  1.00  14.49 ? 208 SER A CB  1 
ATOM   1675 O  OG  . SER A 1 208 ? 17.314 -6.451  -4.678  1.00  16.14 ? 208 SER A OG  1 
ATOM   1676 N  N   . VAL A 1 209 ? 16.843 -10.114 -3.498  1.00  11.91 ? 209 VAL A N   1 
ATOM   1677 C  CA  . VAL A 1 209 ? 17.858 -10.855 -2.737  1.00  11.69 ? 209 VAL A CA  1 
ATOM   1678 C  C   . VAL A 1 209 ? 17.617 -12.359 -2.707  1.00  10.73 ? 209 VAL A C   1 
ATOM   1679 O  O   . VAL A 1 209 ? 16.564 -12.838 -2.274  1.00  11.67 ? 209 VAL A O   1 
ATOM   1680 C  CB  . VAL A 1 209 ? 18.013 -10.356 -1.278  1.00  11.11 ? 209 VAL A CB  1 
ATOM   1681 C  CG1 . VAL A 1 209 ? 19.193 -11.091 -0.604  1.00  10.22 ? 209 VAL A CG1 1 
ATOM   1682 C  CG2 . VAL A 1 209 ? 18.319 -8.855  -1.264  1.00  11.81 ? 209 VAL A CG2 1 
ATOM   1683 N  N   . THR A 1 210 ? 18.605 -13.106 -3.162  1.00  10.97 ? 210 THR A N   1 
ATOM   1684 C  CA  . THR A 1 210 ? 18.631 -14.567 -2.850  1.00  11.10 ? 210 THR A CA  1 
ATOM   1685 C  C   . THR A 1 210 ? 19.392 -14.637 -1.502  1.00  11.50 ? 210 THR A C   1 
ATOM   1686 O  O   . THR A 1 210 ? 20.593 -14.309 -1.424  1.00  11.83 ? 210 THR A O   1 
ATOM   1687 C  CB  . THR A 1 210 ? 19.327 -15.395 -3.936  1.00  11.50 ? 210 THR A CB  1 
ATOM   1688 O  OG1 . THR A 1 210 ? 18.688 -15.151 -5.209  1.00  11.48 ? 210 THR A OG1 1 
ATOM   1689 C  CG2 . THR A 1 210 ? 19.240 -16.943 -3.594  1.00  11.13 ? 210 THR A CG2 1 
ATOM   1690 N  N   . TRP A 1 211 ? 18.648 -14.945 -0.445  1.00  10.75 ? 211 TRP A N   1 
ATOM   1691 C  CA  . TRP A 1 211 ? 19.234 -15.056 0.916   1.00  11.31 ? 211 TRP A CA  1 
ATOM   1692 C  C   . TRP A 1 211 ? 19.867 -16.439 1.067   1.00  10.51 ? 211 TRP A C   1 
ATOM   1693 O  O   . TRP A 1 211 ? 19.300 -17.450 0.731   1.00  10.05 ? 211 TRP A O   1 
ATOM   1694 C  CB  . TRP A 1 211 ? 18.093 -14.931 1.962   1.00  10.98 ? 211 TRP A CB  1 
ATOM   1695 C  CG  . TRP A 1 211 ? 17.884 -13.463 2.209   1.00  10.67 ? 211 TRP A CG  1 
ATOM   1696 C  CD1 . TRP A 1 211 ? 16.923 -12.623 1.655   1.00  10.67 ? 211 TRP A CD1 1 
ATOM   1697 C  CD2 . TRP A 1 211 ? 18.784 -12.611 2.995   1.00  11.32 ? 211 TRP A CD2 1 
ATOM   1698 N  NE1 . TRP A 1 211 ? 17.149 -11.300 2.087   1.00  12.13 ? 211 TRP A NE1 1 
ATOM   1699 C  CE2 . TRP A 1 211 ? 18.261 -11.246 2.903   1.00  11.65 ? 211 TRP A CE2 1 
ATOM   1700 C  CE3 . TRP A 1 211 ? 19.977 -12.842 3.729   1.00  11.87 ? 211 TRP A CE3 1 
ATOM   1701 C  CZ2 . TRP A 1 211 ? 18.912 -10.179 3.505   1.00  12.58 ? 211 TRP A CZ2 1 
ATOM   1702 C  CZ3 . TRP A 1 211 ? 20.583 -11.761 4.365   1.00  13.01 ? 211 TRP A CZ3 1 
ATOM   1703 C  CH2 . TRP A 1 211 ? 20.057 -10.465 4.275   1.00  12.59 ? 211 TRP A CH2 1 
ATOM   1704 N  N   . ILE A 1 212 ? 21.029 -16.445 1.653   1.00  12.59 ? 212 ILE A N   1 
ATOM   1705 C  CA  . ILE A 1 212 ? 21.787 -17.645 1.937   1.00  12.63 ? 212 ILE A CA  1 
ATOM   1706 C  C   . ILE A 1 212 ? 22.234 -17.453 3.413   1.00  11.80 ? 212 ILE A C   1 
ATOM   1707 O  O   . ILE A 1 212 ? 23.145 -16.708 3.692   1.00  12.63 ? 212 ILE A O   1 
ATOM   1708 C  CB  . ILE A 1 212 ? 23.017 -17.744 0.990   1.00  12.60 ? 212 ILE A CB  1 
ATOM   1709 C  CG1 . ILE A 1 212 ? 22.562 -17.995 -0.472  1.00  14.25 ? 212 ILE A CG1 1 
ATOM   1710 C  CG2 . ILE A 1 212 ? 23.947 -18.903 1.405   1.00  13.27 ? 212 ILE A CG2 1 
ATOM   1711 C  CD1 . ILE A 1 212 ? 23.687 -17.720 -1.491  1.00  13.95 ? 212 ILE A CD1 1 
ATOM   1712 N  N   . VAL A 1 213 ? 21.573 -18.130 4.354   1.00  12.98 ? 213 VAL A N   1 
ATOM   1713 C  CA  . VAL A 1 213 ? 21.860 -17.957 5.787   1.00  12.38 ? 213 VAL A CA  1 
ATOM   1714 C  C   . VAL A 1 213 ? 22.576 -19.177 6.306   1.00  12.53 ? 213 VAL A C   1 
ATOM   1715 O  O   . VAL A 1 213 ? 22.022 -20.283 6.212   1.00  12.74 ? 213 VAL A O   1 
ATOM   1716 C  CB  . VAL A 1 213 ? 20.522 -17.736 6.575   1.00  12.88 ? 213 VAL A CB  1 
ATOM   1717 C  CG1 . VAL A 1 213 ? 20.808 -17.581 8.076   1.00  11.94 ? 213 VAL A CG1 1 
ATOM   1718 C  CG2 . VAL A 1 213 ? 19.823 -16.501 6.017   1.00  14.35 ? 213 VAL A CG2 1 
ATOM   1719 N  N   . LEU A 1 214 ? 23.790 -19.008 6.826   1.00  13.10 ? 214 LEU A N   1 
ATOM   1720 C  CA  . LEU A 1 214 ? 24.569 -20.151 7.344   1.00  14.67 ? 214 LEU A CA  1 
ATOM   1721 C  C   . LEU A 1 214 ? 23.979 -20.682 8.670   1.00  14.92 ? 214 LEU A C   1 
ATOM   1722 O  O   . LEU A 1 214 ? 23.613 -19.891 9.555   1.00  15.18 ? 214 LEU A O   1 
ATOM   1723 C  CB  . LEU A 1 214 ? 26.066 -19.795 7.521   1.00  16.13 ? 214 LEU A CB  1 
ATOM   1724 C  CG  . LEU A 1 214 ? 26.953 -20.034 6.247   1.00  18.73 ? 214 LEU A CG  1 
ATOM   1725 C  CD1 . LEU A 1 214 ? 26.367 -19.423 5.024   1.00  19.99 ? 214 LEU A CD1 1 
ATOM   1726 C  CD2 . LEU A 1 214 ? 28.358 -19.483 6.480   1.00  18.74 ? 214 LEU A CD2 1 
ATOM   1727 N  N   . LYS A 1 215 ? 23.890 -22.000 8.807   1.00  14.27 ? 215 LYS A N   1 
ATOM   1728 C  CA  . LYS A 1 215 ? 23.392 -22.595 10.072  1.00  16.14 ? 215 LYS A CA  1 
ATOM   1729 C  C   . LYS A 1 215 ? 24.337 -22.262 11.240  1.00  15.93 ? 215 LYS A C   1 
ATOM   1730 O  O   . LYS A 1 215 ? 23.887 -21.900 12.348  1.00  18.43 ? 215 LYS A O   1 
ATOM   1731 C  CB  . LYS A 1 215 ? 23.265 -24.121 9.929   1.00  16.00 ? 215 LYS A CB  1 
ATOM   1732 C  CG  . LYS A 1 215 ? 22.447 -24.772 11.053  1.00  19.20 ? 215 LYS A CG  1 
ATOM   1733 C  CD  . LYS A 1 215 ? 22.353 -26.272 10.887  1.00  20.98 ? 215 LYS A CD  1 
ATOM   1734 C  CE  . LYS A 1 215 ? 22.273 -26.933 12.264  1.00  24.16 ? 215 LYS A CE  1 
ATOM   1735 N  NZ  . LYS A 1 215 ? 21.611 -28.270 12.061  1.00  31.15 ? 215 LYS A NZ  1 
ATOM   1736 N  N   . GLN A 1 216 ? 25.648 -22.401 11.035  1.00  16.19 ? 216 GLN A N   1 
ATOM   1737 C  CA  . GLN A 1 216 ? 26.549 -22.320 12.190  1.00  16.13 ? 216 GLN A CA  1 
ATOM   1738 C  C   . GLN A 1 216 ? 26.987 -20.896 12.495  1.00  16.34 ? 216 GLN A C   1 
ATOM   1739 O  O   . GLN A 1 216 ? 27.458 -20.205 11.583  1.00  16.97 ? 216 GLN A O   1 
ATOM   1740 C  CB  . GLN A 1 216 ? 27.800 -23.198 11.977  1.00  16.76 ? 216 GLN A CB  1 
ATOM   1741 C  CG  . GLN A 1 216 ? 28.724 -23.168 13.183  1.00  16.51 ? 216 GLN A CG  1 
ATOM   1742 C  CD  . GLN A 1 216 ? 29.941 -24.100 13.009  1.00  16.56 ? 216 GLN A CD  1 
ATOM   1743 O  OE1 . GLN A 1 216 ? 30.256 -24.558 11.891  1.00  15.53 ? 216 GLN A OE1 1 
ATOM   1744 N  NE2 . GLN A 1 216 ? 30.632 -24.374 14.112  1.00  16.36 ? 216 GLN A NE2 1 
ATOM   1745 N  N   . PRO A 1 217 ? 26.862 -20.452 13.780  1.00  16.23 ? 217 PRO A N   1 
ATOM   1746 C  CA  . PRO A 1 217 ? 27.242 -19.114 14.138  1.00  16.14 ? 217 PRO A CA  1 
ATOM   1747 C  C   . PRO A 1 217 ? 28.729 -19.021 14.333  1.00  16.64 ? 217 PRO A C   1 
ATOM   1748 O  O   . PRO A 1 217 ? 29.387 -20.048 14.530  1.00  16.49 ? 217 PRO A O   1 
ATOM   1749 C  CB  . PRO A 1 217 ? 26.544 -18.880 15.492  1.00  16.10 ? 217 PRO A CB  1 
ATOM   1750 C  CG  . PRO A 1 217 ? 26.385 -20.258 16.057  1.00  19.60 ? 217 PRO A CG  1 
ATOM   1751 C  CD  . PRO A 1 217 ? 26.067 -21.106 14.842  1.00  16.86 ? 217 PRO A CD  1 
ATOM   1752 N  N   . ILE A 1 218 ? 29.242 -17.803 14.276  1.00  15.69 ? 218 ILE A N   1 
ATOM   1753 C  CA  . ILE A 1 218 ? 30.574 -17.486 14.723  1.00  16.88 ? 218 ILE A CA  1 
ATOM   1754 C  C   . ILE A 1 218 ? 30.468 -16.832 16.093  1.00  17.41 ? 218 ILE A C   1 
ATOM   1755 O  O   . ILE A 1 218 ? 29.375 -16.579 16.616  1.00  15.74 ? 218 ILE A O   1 
ATOM   1756 C  CB  . ILE A 1 218 ? 31.335 -16.573 13.700  1.00  18.30 ? 218 ILE A CB  1 
ATOM   1757 C  CG1 . ILE A 1 218 ? 30.594 -15.244 13.499  1.00  17.60 ? 218 ILE A CG1 1 
ATOM   1758 C  CG2 . ILE A 1 218 ? 31.557 -17.320 12.385  1.00  18.32 ? 218 ILE A CG2 1 
ATOM   1759 C  CD1 . ILE A 1 218 ? 31.454 -14.192 12.804  1.00  19.66 ? 218 ILE A CD1 1 
ATOM   1760 N  N   . ASN A 1 219 ? 31.639 -16.524 16.663  1.00  17.61 ? 219 ASN A N   1 
ATOM   1761 C  CA  . ASN A 1 219 ? 31.722 -15.995 17.973  1.00  20.08 ? 219 ASN A CA  1 
ATOM   1762 C  C   . ASN A 1 219 ? 32.146 -14.527 18.014  1.00  18.74 ? 219 ASN A C   1 
ATOM   1763 O  O   . ASN A 1 219 ? 33.062 -14.117 17.344  1.00  19.47 ? 219 ASN A O   1 
ATOM   1764 C  CB  . ASN A 1 219 ? 32.698 -16.881 18.793  1.00  25.61 ? 219 ASN A CB  1 
ATOM   1765 C  CG  . ASN A 1 219 ? 32.191 -18.323 18.918  1.00  26.19 ? 219 ASN A CG  1 
ATOM   1766 O  OD1 . ASN A 1 219 ? 32.823 -19.281 18.435  1.00  34.37 ? 219 ASN A OD1 1 
ATOM   1767 N  ND2 . ASN A 1 219 ? 31.046 -18.480 19.537  1.00  26.83 ? 219 ASN A ND2 1 
ATOM   1768 N  N   . ILE A 1 220 ? 31.503 -13.767 18.874  1.00  18.88 ? 220 ILE A N   1 
ATOM   1769 C  CA  . ILE A 1 220 ? 31.927 -12.407 19.183  1.00  18.01 ? 220 ILE A CA  1 
ATOM   1770 C  C   . ILE A 1 220 ? 31.949 -12.303 20.705  1.00  19.13 ? 220 ILE A C   1 
ATOM   1771 O  O   . ILE A 1 220 ? 31.155 -12.984 21.373  1.00  18.45 ? 220 ILE A O   1 
ATOM   1772 C  CB  . ILE A 1 220 ? 30.923 -11.366 18.580  1.00  16.64 ? 220 ILE A CB  1 
ATOM   1773 C  CG1 . ILE A 1 220 ? 31.416 -9.926  18.832  1.00  16.57 ? 220 ILE A CG1 1 
ATOM   1774 C  CG2 . ILE A 1 220 ? 29.541 -11.514 19.198  1.00  15.11 ? 220 ILE A CG2 1 
ATOM   1775 C  CD1 . ILE A 1 220 ? 30.716 -8.898  17.942  1.00  15.95 ? 220 ILE A CD1 1 
ATOM   1776 N  N   . SER A 1 221 ? 32.824 -11.459 21.279  1.00  19.71 ? 221 SER A N   1 
ATOM   1777 C  CA  . SER A 1 221 ? 32.714 -11.182 22.712  1.00  19.58 ? 221 SER A CA  1 
ATOM   1778 C  C   . SER A 1 221 ? 31.700 -10.102 22.982  1.00  21.14 ? 221 SER A C   1 
ATOM   1779 O  O   . SER A 1 221 ? 31.339 -9.345  22.085  1.00  20.03 ? 221 SER A O   1 
ATOM   1780 C  CB  . SER A 1 221 ? 34.078 -10.873 23.374  1.00  21.26 ? 221 SER A CB  1 
ATOM   1781 O  OG  . SER A 1 221 ? 34.580 -9.624  22.931  1.00  19.17 ? 221 SER A OG  1 
ATOM   1782 N  N   . SER A 1 222 ? 31.191 -10.060 24.221  1.00  18.39 ? 222 SER A N   1 
ATOM   1783 C  CA  . SER A 1 222 ? 30.266 -9.023  24.674  1.00  21.51 ? 222 SER A CA  1 
ATOM   1784 C  C   . SER A 1 222 ? 30.869 -7.609  24.546  1.00  22.02 ? 222 SER A C   1 
ATOM   1785 O  O   . SER A 1 222 ? 30.170 -6.647  24.239  1.00  24.77 ? 222 SER A O   1 
ATOM   1786 C  CB  . SER A 1 222 ? 29.940 -9.256  26.130  1.00  22.30 ? 222 SER A CB  1 
ATOM   1787 O  OG  . SER A 1 222 ? 28.766 -8.540  26.426  1.00  28.35 ? 222 SER A OG  1 
ATOM   1788 N  N   . GLN A 1 223 ? 32.161 -7.503  24.826  1.00  24.68 ? 223 GLN A N   1 
ATOM   1789 C  CA  . GLN A 1 223 ? 32.879 -6.233  24.768  1.00  26.56 ? 223 GLN A CA  1 
ATOM   1790 C  C   . GLN A 1 223 ? 32.965 -5.772  23.307  1.00  22.28 ? 223 GLN A C   1 
ATOM   1791 O  O   . GLN A 1 223 ? 32.741 -4.585  23.005  1.00  21.26 ? 223 GLN A O   1 
ATOM   1792 C  CB  . GLN A 1 223 ? 34.290 -6.377  25.390  1.00  29.08 ? 223 GLN A CB  1 
ATOM   1793 C  CG  . GLN A 1 223 ? 35.233 -5.258  24.921  1.00  34.94 ? 223 GLN A CG  1 
ATOM   1794 C  CD  . GLN A 1 223 ? 36.544 -5.140  25.680  1.00  41.59 ? 223 GLN A CD  1 
ATOM   1795 O  OE1 . GLN A 1 223 ? 36.700 -4.236  26.497  1.00  41.76 ? 223 GLN A OE1 1 
ATOM   1796 N  NE2 . GLN A 1 223 ? 37.505 -6.024  25.380  1.00  40.20 ? 223 GLN A NE2 1 
ATOM   1797 N  N   . GLN A 1 224 ? 33.269 -6.720  22.412  1.00  22.51 ? 224 GLN A N   1 
ATOM   1798 C  CA  . GLN A 1 224 ? 33.347 -6.415  20.988  1.00  21.90 ? 224 GLN A CA  1 
ATOM   1799 C  C   . GLN A 1 224 ? 31.958 -5.959  20.566  1.00  22.47 ? 224 GLN A C   1 
ATOM   1800 O  O   . GLN A 1 224 ? 31.801 -4.917  19.912  1.00  21.12 ? 224 GLN A O   1 
ATOM   1801 C  CB  . GLN A 1 224 ? 33.869 -7.593  20.136  1.00  23.47 ? 224 GLN A CB  1 
ATOM   1802 C  CG  . GLN A 1 224 ? 35.370 -7.934  20.279  1.00  23.52 ? 224 GLN A CG  1 
ATOM   1803 C  CD  . GLN A 1 224 ? 35.791 -9.132  19.444  1.00  25.96 ? 224 GLN A CD  1 
ATOM   1804 O  OE1 . GLN A 1 224 ? 35.009 -10.069 19.232  1.00  26.40 ? 224 GLN A OE1 1 
ATOM   1805 N  NE2 . GLN A 1 224 ? 37.041 -9.123  18.966  1.00  26.20 ? 224 GLN A NE2 1 
ATOM   1806 N  N   . LEU A 1 225 ? 30.918 -6.692  20.989  1.00  19.82 ? 225 LEU A N   1 
ATOM   1807 C  CA  . LEU A 1 225 ? 29.579 -6.371  20.498  1.00  17.07 ? 225 LEU A CA  1 
ATOM   1808 C  C   . LEU A 1 225 ? 29.090 -5.038  21.035  1.00  16.63 ? 225 LEU A C   1 
ATOM   1809 O  O   . LEU A 1 225 ? 28.490 -4.232  20.300  1.00  15.72 ? 225 LEU A O   1 
ATOM   1810 C  CB  . LEU A 1 225 ? 28.606 -7.522  20.805  1.00  17.05 ? 225 LEU A CB  1 
ATOM   1811 C  CG  . LEU A 1 225 ? 27.144 -7.383  20.404  1.00  16.46 ? 225 LEU A CG  1 
ATOM   1812 C  CD1 . LEU A 1 225 ? 27.063 -7.142  18.882  1.00  15.45 ? 225 LEU A CD1 1 
ATOM   1813 C  CD2 . LEU A 1 225 ? 26.395 -8.643  20.876  1.00  17.22 ? 225 LEU A CD2 1 
ATOM   1814 N  N   . ALA A 1 226 ? 29.407 -4.748  22.290  1.00  15.63 ? 226 ALA A N   1 
ATOM   1815 C  CA  . ALA A 1 226 ? 29.024 -3.499  22.885  1.00  17.34 ? 226 ALA A CA  1 
ATOM   1816 C  C   . ALA A 1 226 ? 29.577 -2.299  22.131  1.00  17.54 ? 226 ALA A C   1 
ATOM   1817 O  O   . ALA A 1 226 ? 28.942 -1.290  22.103  1.00  18.08 ? 226 ALA A O   1 
ATOM   1818 C  CB  . ALA A 1 226 ? 29.475 -3.440  24.362  1.00  19.12 ? 226 ALA A CB  1 
ATOM   1819 N  N   . LYS A 1 227 ? 30.799 -2.389  21.602  1.00  17.55 ? 227 LYS A N   1 
ATOM   1820 C  CA  . LYS A 1 227 ? 31.443 -1.290  20.861  1.00  18.32 ? 227 LYS A CA  1 
ATOM   1821 C  C   . LYS A 1 227 ? 30.573 -0.816  19.668  1.00  16.57 ? 227 LYS A C   1 
ATOM   1822 O  O   . LYS A 1 227 ? 30.560 0.369   19.317  1.00  15.29 ? 227 LYS A O   1 
ATOM   1823 C  CB  . LYS A 1 227 ? 32.804 -1.771  20.319  1.00  22.56 ? 227 LYS A CB  1 
ATOM   1824 C  CG  . LYS A 1 227 ? 33.743 -0.642  19.978  1.00  31.68 ? 227 LYS A CG  1 
ATOM   1825 C  CD  . LYS A 1 227 ? 34.746 -0.450  21.111  1.00  36.18 ? 227 LYS A CD  1 
ATOM   1826 C  CE  . LYS A 1 227 ? 35.976 0.287   20.618  1.00  36.36 ? 227 LYS A CE  1 
ATOM   1827 N  NZ  . LYS A 1 227 ? 35.669 1.725   20.450  1.00  39.77 ? 227 LYS A NZ  1 
ATOM   1828 N  N   . PHE A 1 228 ? 29.841 -1.719  19.050  1.00  14.28 ? 228 PHE A N   1 
ATOM   1829 C  CA  . PHE A 1 228 ? 28.994 -1.292  17.868  1.00  14.12 ? 228 PHE A CA  1 
ATOM   1830 C  C   . PHE A 1 228 ? 27.920 -0.309  18.280  1.00  14.38 ? 228 PHE A C   1 
ATOM   1831 O  O   . PHE A 1 228 ? 27.536 0.544   17.508  1.00  12.50 ? 228 PHE A O   1 
ATOM   1832 C  CB  . PHE A 1 228 ? 28.418 -2.518  17.196  1.00  14.37 ? 228 PHE A CB  1 
ATOM   1833 C  CG  . PHE A 1 228 ? 29.492 -3.350  16.503  1.00  15.72 ? 228 PHE A CG  1 
ATOM   1834 C  CD1 . PHE A 1 228 ? 29.982 -4.522  17.059  1.00  15.64 ? 228 PHE A CD1 1 
ATOM   1835 C  CD2 . PHE A 1 228 ? 30.065 -2.872  15.337  1.00  15.64 ? 228 PHE A CD2 1 
ATOM   1836 C  CE1 . PHE A 1 228 ? 30.988 -5.236  16.400  1.00  16.12 ? 228 PHE A CE1 1 
ATOM   1837 C  CE2 . PHE A 1 228 ? 31.072 -3.557  14.699  1.00  17.77 ? 228 PHE A CE2 1 
ATOM   1838 C  CZ  . PHE A 1 228 ? 31.546 -4.749  15.226  1.00  15.50 ? 228 PHE A CZ  1 
ATOM   1839 N  N   . ARG A 1 229 ? 27.411 -0.476  19.518  1.00  13.10 ? 229 ARG A N   1 
ATOM   1840 C  CA  . ARG A 1 229 ? 26.281 0.368   20.050  1.00  14.22 ? 229 ARG A CA  1 
ATOM   1841 C  C   . ARG A 1 229 ? 26.618 1.830   20.320  1.00  15.10 ? 229 ARG A C   1 
ATOM   1842 O  O   . ARG A 1 229 ? 25.701 2.681   20.467  1.00  14.28 ? 229 ARG A O   1 
ATOM   1843 C  CB  . ARG A 1 229 ? 25.647 -0.239  21.306  1.00  13.87 ? 229 ARG A CB  1 
ATOM   1844 C  CG  . ARG A 1 229 ? 25.256 -1.725  21.185  1.00  13.47 ? 229 ARG A CG  1 
ATOM   1845 C  CD  . ARG A 1 229 ? 24.315 -2.096  22.365  1.00  14.12 ? 229 ARG A CD  1 
ATOM   1846 N  NE  . ARG A 1 229 ? 23.930 -3.484  22.175  1.00  14.87 ? 229 ARG A NE  1 
ATOM   1847 C  CZ  . ARG A 1 229 ? 24.583 -4.512  22.711  1.00  17.04 ? 229 ARG A CZ  1 
ATOM   1848 N  NH1 . ARG A 1 229 ? 25.616 -4.291  23.560  1.00  17.10 ? 229 ARG A NH1 1 
ATOM   1849 N  NH2 . ARG A 1 229 ? 24.217 -5.769  22.423  1.00  15.97 ? 229 ARG A NH2 1 
ATOM   1850 N  N   . SER A 1 230 ? 27.913 2.122   20.386  1.00  16.37 ? 230 SER A N   1 
ATOM   1851 C  CA  . SER A 1 230 ? 28.421 3.481   20.585  1.00  17.22 ? 230 SER A CA  1 
ATOM   1852 C  C   . SER A 1 230 ? 28.646 4.212   19.260  1.00  18.65 ? 230 SER A C   1 
ATOM   1853 O  O   . SER A 1 230 ? 29.038 5.393   19.279  1.00  17.64 ? 230 SER A O   1 
ATOM   1854 C  CB  . SER A 1 230 ? 29.718 3.445   21.418  1.00  20.59 ? 230 SER A CB  1 
ATOM   1855 O  OG  . SER A 1 230 ? 30.766 2.856   20.620  1.00  29.73 ? 230 SER A OG  1 
ATOM   1856 N  N   . LEU A 1 231 ? 28.381 3.557   18.109  1.00  17.18 ? 231 LEU A N   1 
ATOM   1857 C  CA  . LEU A 1 231 ? 28.311 4.306   16.839  1.00  16.34 ? 231 LEU A CA  1 
ATOM   1858 C  C   . LEU A 1 231 ? 27.068 5.188   16.895  1.00  17.48 ? 231 LEU A C   1 
ATOM   1859 O  O   . LEU A 1 231 ? 26.046 4.795   17.494  1.00  16.05 ? 231 LEU A O   1 
ATOM   1860 C  CB  . LEU A 1 231 ? 28.181 3.381   15.596  1.00  14.91 ? 231 LEU A CB  1 
ATOM   1861 C  CG  . LEU A 1 231 ? 29.423 2.582   15.234  1.00  16.26 ? 231 LEU A CG  1 
ATOM   1862 C  CD1 . LEU A 1 231 ? 29.031 1.420   14.302  1.00  15.13 ? 231 LEU A CD1 1 
ATOM   1863 C  CD2 . LEU A 1 231 ? 30.597 3.429   14.713  1.00  16.45 ? 231 LEU A CD2 1 
ATOM   1864 N  N   . LEU A 1 232 ? 27.150 6.367   16.281  1.00  16.49 ? 232 LEU A N   1 
ATOM   1865 C  CA  . LEU A 1 232 ? 25.996 7.239   16.174  1.00  17.85 ? 232 LEU A CA  1 
ATOM   1866 C  C   . LEU A 1 232 ? 25.207 7.031   14.890  1.00  17.66 ? 232 LEU A C   1 
ATOM   1867 O  O   . LEU A 1 232 ? 25.779 6.683   13.836  1.00  17.67 ? 232 LEU A O   1 
ATOM   1868 C  CB  . LEU A 1 232 ? 26.404 8.684   16.236  1.00  17.75 ? 232 LEU A CB  1 
ATOM   1869 C  CG  . LEU A 1 232 ? 27.244 9.107   17.464  1.00  21.20 ? 232 LEU A CG  1 
ATOM   1870 C  CD1 . LEU A 1 232 ? 27.676 10.554  17.277  1.00  20.86 ? 232 LEU A CD1 1 
ATOM   1871 C  CD2 . LEU A 1 232 ? 26.378 8.906   18.693  1.00  22.33 ? 232 LEU A CD2 1 
ATOM   1872 N  N   . CYS A 1 233 ? 23.901 7.262   14.959  1.00  15.84 ? 233 CYS A N   1 
ATOM   1873 C  CA  . CYS A 1 233 ? 23.069 7.281   13.731  1.00  16.01 ? 233 CYS A CA  1 
ATOM   1874 C  C   . CYS A 1 233 ? 22.904 8.731   13.263  1.00  17.66 ? 233 CYS A C   1 
ATOM   1875 O  O   . CYS A 1 233 ? 22.212 8.998   12.280  1.00  21.20 ? 233 CYS A O   1 
ATOM   1876 C  CB  . CYS A 1 233 ? 21.678 6.635   13.976  1.00  16.40 ? 233 CYS A CB  1 
ATOM   1877 S  SG  . CYS A 1 233 ? 20.645 7.520   15.182  1.00  23.29 ? 233 CYS A SG  1 
ATOM   1878 N  N   . THR A 1 234 ? 23.557 9.652   13.971  1.00  19.76 ? 234 THR A N   1 
ATOM   1879 C  CA  . THR A 1 234 ? 23.503 11.099  13.704  1.00  19.30 ? 234 THR A CA  1 
ATOM   1880 C  C   . THR A 1 234 ? 24.865 11.612  13.278  1.00  20.13 ? 234 THR A C   1 
ATOM   1881 O  O   . THR A 1 234 ? 25.937 11.119  13.697  1.00  17.62 ? 234 THR A O   1 
ATOM   1882 C  CB  . THR A 1 234 ? 23.079 11.859  14.946  1.00  19.07 ? 234 THR A CB  1 
ATOM   1883 O  OG1 . THR A 1 234 ? 23.880 11.414  16.035  1.00  19.55 ? 234 THR A OG1 1 
ATOM   1884 C  CG2 . THR A 1 234 ? 21.614 11.598  15.261  1.00  19.71 ? 234 THR A CG2 1 
ATOM   1885 N  N   . ALA A 1 235 ? 24.843 12.661  12.482  1.00  23.04 ? 235 ALA A N   1 
ATOM   1886 C  CA  . ALA A 1 235 ? 26.080 13.220  11.933  1.00  25.70 ? 235 ALA A CA  1 
ATOM   1887 C  C   . ALA A 1 235 ? 26.745 14.256  12.864  1.00  29.99 ? 235 ALA A C   1 
ATOM   1888 O  O   . ALA A 1 235 ? 26.113 14.733  13.802  1.00  31.34 ? 235 ALA A O   1 
ATOM   1889 C  CB  . ALA A 1 235 ? 25.760 13.844  10.599  1.00  25.90 ? 235 ALA A CB  1 
ATOM   1890 N  N   . GLU A 1 236 ? 28.019 14.584  12.599  1.00  34.18 ? 236 GLU A N   1 
ATOM   1891 C  CA  . GLU A 1 236 ? 28.799 15.562  13.406  1.00  40.00 ? 236 GLU A CA  1 
ATOM   1892 C  C   . GLU A 1 236 ? 27.978 16.851  13.537  1.00  38.66 ? 236 GLU A C   1 
ATOM   1893 O  O   . GLU A 1 236 ? 27.351 17.284  12.558  1.00  35.25 ? 236 GLU A O   1 
ATOM   1894 C  CB  . GLU A 1 236 ? 30.158 15.846  12.761  0.010 38.10 ? 236 GLU A CB  1 
ATOM   1895 C  CG  . GLU A 1 236 ? 31.141 16.573  13.666  0.010 38.28 ? 236 GLU A CG  1 
ATOM   1896 C  CD  . GLU A 1 236 ? 32.457 16.875  12.977  0.010 38.26 ? 236 GLU A CD  1 
ATOM   1897 O  OE1 . GLU A 1 236 ? 32.595 16.540  11.781  0.010 38.28 ? 236 GLU A OE1 1 
ATOM   1898 O  OE2 . GLU A 1 236 ? 33.354 17.447  13.631  0.010 38.12 ? 236 GLU A OE2 1 
ATOM   1899 N  N   . GLY A 1 237 ? 27.930 17.410  14.750  1.00  41.47 ? 237 GLY A N   1 
ATOM   1900 C  CA  . GLY A 1 237 ? 27.079 18.590  15.035  1.00  46.57 ? 237 GLY A CA  1 
ATOM   1901 C  C   . GLY A 1 237 ? 25.563 18.463  14.810  1.00  48.18 ? 237 GLY A C   1 
ATOM   1902 O  O   . GLY A 1 237 ? 24.875 19.449  14.523  1.00  47.69 ? 237 GLY A O   1 
ATOM   1903 N  N   . GLU A 1 238 ? 25.050 17.238  14.895  1.00  50.10 ? 238 GLU A N   1 
ATOM   1904 C  CA  . GLU A 1 238 ? 23.624 16.976  15.099  1.00  45.40 ? 238 GLU A CA  1 
ATOM   1905 C  C   . GLU A 1 238 ? 23.518 16.603  16.588  1.00  40.72 ? 238 GLU A C   1 
ATOM   1906 O  O   . GLU A 1 238 ? 24.539 16.329  17.231  1.00  38.87 ? 238 GLU A O   1 
ATOM   1907 C  CB  . GLU A 1 238 ? 23.174 15.786  14.244  1.00  51.14 ? 238 GLU A CB  1 
ATOM   1908 C  CG  . GLU A 1 238 ? 22.531 16.051  12.891  1.00  51.38 ? 238 GLU A CG  1 
ATOM   1909 C  CD  . GLU A 1 238 ? 21.720 14.822  12.427  1.00  59.80 ? 238 GLU A CD  1 
ATOM   1910 O  OE1 . GLU A 1 238 ? 22.330 13.854  11.900  1.00  49.14 ? 238 GLU A OE1 1 
ATOM   1911 O  OE2 . GLU A 1 238 ? 20.467 14.802  12.607  1.00  58.38 ? 238 GLU A OE2 1 
ATOM   1912 N  N   . ALA A 1 239 ? 22.318 16.606  17.164  1.00  37.11 ? 239 ALA A N   1 
ATOM   1913 C  CA  . ALA A 1 239 ? 22.185 16.106  18.546  1.00  33.45 ? 239 ALA A CA  1 
ATOM   1914 C  C   . ALA A 1 239 ? 22.335 14.586  18.452  1.00  27.84 ? 239 ALA A C   1 
ATOM   1915 O  O   . ALA A 1 239 ? 21.641 13.949  17.662  1.00  30.60 ? 239 ALA A O   1 
ATOM   1916 C  CB  . ALA A 1 239 ? 20.844 16.464  19.150  1.00  30.97 ? 239 ALA A CB  1 
ATOM   1917 N  N   . ALA A 1 240 ? 23.212 14.052  19.273  1.00  24.44 ? 240 ALA A N   1 
ATOM   1918 C  CA  . ALA A 1 240 ? 23.662 12.680  19.158  1.00  26.55 ? 240 ALA A CA  1 
ATOM   1919 C  C   . ALA A 1 240 ? 22.544 11.713  19.496  1.00  26.15 ? 240 ALA A C   1 
ATOM   1920 O  O   . ALA A 1 240 ? 21.880 11.876  20.537  1.00  21.10 ? 240 ALA A O   1 
ATOM   1921 C  CB  . ALA A 1 240 ? 24.853 12.469  20.062  1.00  27.59 ? 240 ALA A CB  1 
ATOM   1922 N  N   . ALA A 1 241 ? 22.348 10.713  18.627  1.00  22.38 ? 241 ALA A N   1 
ATOM   1923 C  CA  . ALA A 1 241 ? 21.552 9.528   18.982  1.00  20.41 ? 241 ALA A CA  1 
ATOM   1924 C  C   . ALA A 1 241 ? 22.390 8.272   18.676  1.00  20.52 ? 241 ALA A C   1 
ATOM   1925 O  O   . ALA A 1 241 ? 23.124 8.265   17.678  1.00  19.73 ? 241 ALA A O   1 
ATOM   1926 C  CB  . ALA A 1 241 ? 20.287 9.512   18.179  1.00  19.22 ? 241 ALA A CB  1 
ATOM   1927 N  N   . PHE A 1 242 ? 22.320 7.250   19.534  1.00  18.12 ? 242 PHE A N   1 
ATOM   1928 C  CA  . PHE A 1 242 ? 23.147 6.050   19.390  1.00  19.00 ? 242 PHE A CA  1 
ATOM   1929 C  C   . PHE A 1 242 ? 22.423 4.956   18.604  1.00  18.74 ? 242 PHE A C   1 
ATOM   1930 O  O   . PHE A 1 242 ? 21.210 4.714   18.763  1.00  16.36 ? 242 PHE A O   1 
ATOM   1931 C  CB  . PHE A 1 242 ? 23.613 5.471   20.742  1.00  19.43 ? 242 PHE A CB  1 
ATOM   1932 C  CG  . PHE A 1 242 ? 24.502 6.404   21.512  1.00  19.63 ? 242 PHE A CG  1 
ATOM   1933 C  CD1 . PHE A 1 242 ? 23.931 7.366   22.349  1.00  20.13 ? 242 PHE A CD1 1 
ATOM   1934 C  CD2 . PHE A 1 242 ? 25.888 6.380   21.332  1.00  21.05 ? 242 PHE A CD2 1 
ATOM   1935 C  CE1 . PHE A 1 242 ? 24.699 8.262   23.030  1.00  20.65 ? 242 PHE A CE1 1 
ATOM   1936 C  CE2 . PHE A 1 242 ? 26.687 7.277   22.045  1.00  20.13 ? 242 PHE A CE2 1 
ATOM   1937 C  CZ  . PHE A 1 242 ? 26.085 8.204   22.879  1.00  20.97 ? 242 PHE A CZ  1 
ATOM   1938 N  N   . LEU A 1 243 ? 23.188 4.300   17.759  1.00  15.45 ? 243 LEU A N   1 
ATOM   1939 C  CA  . LEU A 1 243 ? 22.712 3.092   17.060  1.00  15.19 ? 243 LEU A CA  1 
ATOM   1940 C  C   . LEU A 1 243 ? 22.762 1.856   17.973  1.00  13.61 ? 243 LEU A C   1 
ATOM   1941 O  O   . LEU A 1 243 ? 23.595 0.919   17.786  1.00  13.93 ? 243 LEU A O   1 
ATOM   1942 C  CB  . LEU A 1 243 ? 23.587 2.905   15.813  1.00  13.70 ? 243 LEU A CB  1 
ATOM   1943 C  CG  . LEU A 1 243 ? 23.114 1.993   14.666  1.00  15.00 ? 243 LEU A CG  1 
ATOM   1944 C  CD1 . LEU A 1 243 ? 21.734 2.412   14.144  1.00  14.69 ? 243 LEU A CD1 1 
ATOM   1945 C  CD2 . LEU A 1 243 ? 24.159 1.979   13.530  1.00  14.32 ? 243 LEU A CD2 1 
ATOM   1946 N  N   . VAL A 1 244 ? 21.896 1.817   18.984  1.00  13.77 ? 244 VAL A N   1 
ATOM   1947 C  CA  . VAL A 1 244 ? 21.965 0.694   19.984  1.00  13.88 ? 244 VAL A CA  1 
ATOM   1948 C  C   . VAL A 1 244 ? 21.343 -0.607  19.451  1.00  13.90 ? 244 VAL A C   1 
ATOM   1949 O  O   . VAL A 1 244 ? 21.659 -1.697  19.944  1.00  13.56 ? 244 VAL A O   1 
ATOM   1950 C  CB  . VAL A 1 244 ? 21.339 1.072   21.379  1.00  13.69 ? 244 VAL A CB  1 
ATOM   1951 C  CG1 . VAL A 1 244 ? 21.977 2.349   21.916  1.00  15.15 ? 244 VAL A CG1 1 
ATOM   1952 C  CG2 . VAL A 1 244 ? 19.837 1.256   21.216  1.00  14.59 ? 244 VAL A CG2 1 
ATOM   1953 N  N   . SER A 1 245 ? 20.471 -0.468  18.437  1.00  13.38 ? 245 SER A N   1 
ATOM   1954 C  CA  . SER A 1 245 ? 19.796 -1.606  17.806  1.00  12.73 ? 245 SER A CA  1 
ATOM   1955 C  C   . SER A 1 245 ? 19.503 -1.233  16.353  1.00  11.96 ? 245 SER A C   1 
ATOM   1956 O  O   . SER A 1 245 ? 19.105 -0.080  16.080  1.00  11.58 ? 245 SER A O   1 
ATOM   1957 C  CB  . SER A 1 245 ? 18.409 -1.771  18.431  1.00  14.01 ? 245 SER A CB  1 
ATOM   1958 O  OG  . SER A 1 245 ? 17.874 -3.014  18.062  1.00  15.28 ? 245 SER A OG  1 
ATOM   1959 N  N   . ASN A 1 246 ? 19.667 -2.193  15.443  1.00  12.60 ? 246 ASN A N   1 
ATOM   1960 C  CA  . ASN A 1 246 ? 19.502 -1.955  13.990  1.00  11.82 ? 246 ASN A CA  1 
ATOM   1961 C  C   . ASN A 1 246 ? 19.016 -3.234  13.274  1.00  13.52 ? 246 ASN A C   1 
ATOM   1962 O  O   . ASN A 1 246 ? 19.370 -3.531  12.100  1.00  12.89 ? 246 ASN A O   1 
ATOM   1963 C  CB  . ASN A 1 246 ? 20.780 -1.329  13.378  1.00  12.94 ? 246 ASN A CB  1 
ATOM   1964 C  CG  . ASN A 1 246 ? 21.952 -2.277  13.430  1.00  13.31 ? 246 ASN A CG  1 
ATOM   1965 O  OD1 . ASN A 1 246 ? 21.884 -3.312  14.108  1.00  13.72 ? 246 ASN A OD1 1 
ATOM   1966 N  ND2 . ASN A 1 246 ? 22.979 -1.994  12.677  1.00  13.43 ? 246 ASN A ND2 1 
ATOM   1967 N  N   . HIS A 1 247 ? 18.167 -4.010  13.960  1.00  12.09 ? 247 HIS A N   1 
ATOM   1968 C  CA  . HIS A 1 247 ? 17.604 -5.171  13.295  1.00  13.32 ? 247 HIS A CA  1 
ATOM   1969 C  C   . HIS A 1 247 ? 16.132 -4.984  12.983  1.00  14.00 ? 247 HIS A C   1 
ATOM   1970 O  O   . HIS A 1 247 ? 15.371 -4.477  13.802  1.00  14.12 ? 247 HIS A O   1 
ATOM   1971 C  CB  . HIS A 1 247 ? 17.898 -6.464  14.074  1.00  12.42 ? 247 HIS A CB  1 
ATOM   1972 C  CG  . HIS A 1 247 ? 17.347 -6.454  15.479  1.00  15.78 ? 247 HIS A CG  1 
ATOM   1973 N  ND1 . HIS A 1 247 ? 16.267 -7.188  15.847  1.00  17.75 ? 247 HIS A ND1 1 
ATOM   1974 C  CD2 . HIS A 1 247 ? 17.737 -5.745  16.594  1.00  13.73 ? 247 HIS A CD2 1 
ATOM   1975 C  CE1 . HIS A 1 247 ? 15.955 -6.947  17.130  1.00  16.97 ? 247 HIS A CE1 1 
ATOM   1976 N  NE2 . HIS A 1 247 ? 16.870 -6.092  17.616  1.00  18.51 ? 247 HIS A NE2 1 
ATOM   1977 N  N   . ARG A 1 248 ? 15.708 -5.438  11.799  1.00  12.69 ? 248 ARG A N   1 
ATOM   1978 C  CA  . ARG A 1 248 ? 14.294 -5.451  11.426  1.00  12.59 ? 248 ARG A CA  1 
ATOM   1979 C  C   . ARG A 1 248 ? 13.631 -6.705  11.961  1.00  11.97 ? 248 ARG A C   1 
ATOM   1980 O  O   . ARG A 1 248 ? 14.249 -7.753  11.910  1.00  11.87 ? 248 ARG A O   1 
ATOM   1981 C  CB  . ARG A 1 248 ? 14.183 -5.446  9.887   1.00  12.08 ? 248 ARG A CB  1 
ATOM   1982 C  CG  . ARG A 1 248 ? 12.739 -5.253  9.410   1.00  13.39 ? 248 ARG A CG  1 
ATOM   1983 C  CD  . ARG A 1 248 ? 12.651 -5.343  7.901   1.00  13.88 ? 248 ARG A CD  1 
ATOM   1984 N  NE  . ARG A 1 248 ? 11.360 -4.821  7.481   1.00  14.43 ? 248 ARG A NE  1 
ATOM   1985 C  CZ  . ARG A 1 248 ? 10.776 -5.120  6.333   1.00  15.28 ? 248 ARG A CZ  1 
ATOM   1986 N  NH1 . ARG A 1 248 ? 11.395 -5.923  5.446   1.00  13.31 ? 248 ARG A NH1 1 
ATOM   1987 N  NH2 . ARG A 1 248 ? 9.610  -4.501  6.021   1.00  15.24 ? 248 ARG A NH2 1 
ATOM   1988 N  N   . PRO A 1 249 ? 12.372 -6.653  12.412  1.00  12.85 ? 249 PRO A N   1 
ATOM   1989 C  CA  . PRO A 1 249 ? 11.692 -7.873  12.856  1.00  12.75 ? 249 PRO A CA  1 
ATOM   1990 C  C   . PRO A 1 249 ? 11.467 -8.846  11.686  1.00  13.22 ? 249 PRO A C   1 
ATOM   1991 O  O   . PRO A 1 249 ? 11.459 -8.394  10.540  1.00  11.88 ? 249 PRO A O   1 
ATOM   1992 C  CB  . PRO A 1 249 ? 10.325 -7.370  13.369  1.00  13.32 ? 249 PRO A CB  1 
ATOM   1993 C  CG  . PRO A 1 249 ? 10.497 -5.915  13.655  1.00  14.88 ? 249 PRO A CG  1 
ATOM   1994 C  CD  . PRO A 1 249 ? 11.569 -5.421  12.685  1.00  14.05 ? 249 PRO A CD  1 
ATOM   1995 N  N   . PRO A 1 250 ? 11.239 -10.149 11.964  1.00  13.78 ? 250 PRO A N   1 
ATOM   1996 C  CA  . PRO A 1 250 ? 10.929 -11.154 10.960  1.00  13.51 ? 250 PRO A CA  1 
ATOM   1997 C  C   . PRO A 1 250 ? 9.645  -10.737 10.261  1.00  14.03 ? 250 PRO A C   1 
ATOM   1998 O  O   . PRO A 1 250 ? 8.799  -10.086 10.889  1.00  14.10 ? 250 PRO A O   1 
ATOM   1999 C  CB  . PRO A 1 250 ? 10.718 -12.405 11.807  1.00  13.41 ? 250 PRO A CB  1 
ATOM   2000 C  CG  . PRO A 1 250 ? 11.773 -12.226 12.897  1.00  16.18 ? 250 PRO A CG  1 
ATOM   2001 C  CD  . PRO A 1 250 ? 11.418 -10.804 13.280  1.00  16.46 ? 250 PRO A CD  1 
ATOM   2002 N  N   . GLN A 1 251 ? 9.519  -11.025 8.974   1.00  12.83 ? 251 GLN A N   1 
ATOM   2003 C  CA  . GLN A 1 251 ? 8.409  -10.535 8.159   1.00  13.07 ? 251 GLN A CA  1 
ATOM   2004 C  C   . GLN A 1 251 ? 7.603  -11.742 7.694   1.00  13.85 ? 251 GLN A C   1 
ATOM   2005 O  O   . GLN A 1 251 ? 8.123  -12.838 7.739   1.00  14.29 ? 251 GLN A O   1 
ATOM   2006 C  CB  . GLN A 1 251 ? 8.979  -9.779  6.946   1.00  12.32 ? 251 GLN A CB  1 
ATOM   2007 C  CG  . GLN A 1 251 ? 9.756  -8.512  7.389   1.00  12.54 ? 251 GLN A CG  1 
ATOM   2008 C  CD  . GLN A 1 251 ? 8.880  -7.536  8.109   1.00  13.40 ? 251 GLN A CD  1 
ATOM   2009 O  OE1 . GLN A 1 251 ? 7.832  -7.166  7.588   1.00  14.66 ? 251 GLN A OE1 1 
ATOM   2010 N  NE2 . GLN A 1 251 ? 9.326  -7.051  9.288   1.00  13.58 ? 251 GLN A NE2 1 
ATOM   2011 N  N   . PRO A 1 252 ? 6.347  -11.543 7.236   1.00  14.98 ? 252 PRO A N   1 
ATOM   2012 C  CA  . PRO A 1 252 ? 5.528  -12.712 6.902   1.00  14.19 ? 252 PRO A CA  1 
ATOM   2013 C  C   . PRO A 1 252 ? 6.176  -13.539 5.767   1.00  13.86 ? 252 PRO A C   1 
ATOM   2014 O  O   . PRO A 1 252 ? 6.720  -13.000 4.808   1.00  14.17 ? 252 PRO A O   1 
ATOM   2015 C  CB  . PRO A 1 252 ? 4.172  -12.097 6.496   1.00  15.21 ? 252 PRO A CB  1 
ATOM   2016 C  CG  . PRO A 1 252 ? 4.147  -10.673 7.011   1.00  14.86 ? 252 PRO A CG  1 
ATOM   2017 C  CD  . PRO A 1 252 ? 5.608  -10.266 7.073   1.00  14.44 ? 252 PRO A CD  1 
ATOM   2018 N  N   . LEU A 1 253 ? 6.141  -14.840 5.916   1.00  14.10 ? 253 LEU A N   1 
ATOM   2019 C  CA  . LEU A 1 253 ? 6.739  -15.723 4.974   1.00  13.72 ? 253 LEU A CA  1 
ATOM   2020 C  C   . LEU A 1 253 ? 5.969  -15.730 3.670   1.00  14.81 ? 253 LEU A C   1 
ATOM   2021 O  O   . LEU A 1 253 ? 6.588  -15.895 2.584   1.00  14.32 ? 253 LEU A O   1 
ATOM   2022 C  CB  . LEU A 1 253 ? 6.754  -17.119 5.554   1.00  14.03 ? 253 LEU A CB  1 
ATOM   2023 C  CG  . LEU A 1 253 ? 7.605  -18.164 4.817   1.00  15.41 ? 253 LEU A CG  1 
ATOM   2024 C  CD1 . LEU A 1 253 ? 9.069  -17.694 4.667   1.00  16.77 ? 253 LEU A CD1 1 
ATOM   2025 C  CD2 . LEU A 1 253 ? 7.535  -19.541 5.571   1.00  16.60 ? 253 LEU A CD2 1 
ATOM   2026 N  N   A LYS A 1 254 ? 4.649  -15.539 3.756   0.50  15.18 ? 254 LYS A N   1 
ATOM   2027 N  N   B LYS A 1 254 ? 4.648  -15.521 3.777   0.50  14.90 ? 254 LYS A N   1 
ATOM   2028 C  CA  A LYS A 1 254 ? 3.798  -15.503 2.567   0.50  16.26 ? 254 LYS A CA  1 
ATOM   2029 C  CA  B LYS A 1 254 ? 3.726  -15.542 2.636   0.50  15.79 ? 254 LYS A CA  1 
ATOM   2030 C  C   A LYS A 1 254 ? 4.027  -16.717 1.642   0.50  16.13 ? 254 LYS A C   1 
ATOM   2031 C  C   B LYS A 1 254 ? 3.999  -16.712 1.666   0.50  15.87 ? 254 LYS A C   1 
ATOM   2032 O  O   A LYS A 1 254 ? 4.017  -16.592 0.394   0.50  16.13 ? 254 LYS A O   1 
ATOM   2033 O  O   B LYS A 1 254 ? 4.004  -16.550 0.421   0.50  15.96 ? 254 LYS A O   1 
ATOM   2034 C  CB  A LYS A 1 254 ? 3.949  -14.165 1.831   0.50  15.77 ? 254 LYS A CB  1 
ATOM   2035 C  CB  B LYS A 1 254 ? 3.667  -14.178 1.932   0.50  14.98 ? 254 LYS A CB  1 
ATOM   2036 C  CG  A LYS A 1 254 ? 3.468  -12.974 2.674   0.50  16.29 ? 254 LYS A CG  1 
ATOM   2037 C  CG  B LYS A 1 254 ? 2.863  -13.115 2.716   0.50  14.44 ? 254 LYS A CG  1 
ATOM   2038 C  CD  A LYS A 1 254 ? 3.317  -11.723 1.829   0.50  16.25 ? 254 LYS A CD  1 
ATOM   2039 C  CD  B LYS A 1 254 ? 3.046  -11.760 2.054   0.50  14.39 ? 254 LYS A CD  1 
ATOM   2040 C  CE  A LYS A 1 254 ? 2.907  -10.522 2.664   0.50  16.96 ? 254 LYS A CE  1 
ATOM   2041 C  CE  B LYS A 1 254 ? 2.593  -10.612 2.939   0.50  14.75 ? 254 LYS A CE  1 
ATOM   2042 N  NZ  A LYS A 1 254 ? 1.528  -10.668 3.220   0.50  17.14 ? 254 LYS A NZ  1 
ATOM   2043 N  NZ  B LYS A 1 254 ? 2.647  -9.315  2.207   0.50  13.73 ? 254 LYS A NZ  1 
ATOM   2044 N  N   . GLY A 1 255 ? 4.227  -17.875 2.271   1.00  15.61 ? 255 GLY A N   1 
ATOM   2045 C  CA  . GLY A 1 255 ? 4.277  -19.154 1.558   1.00  17.04 ? 255 GLY A CA  1 
ATOM   2046 C  C   . GLY A 1 255 ? 5.570  -19.456 0.829   1.00  15.80 ? 255 GLY A C   1 
ATOM   2047 O  O   . GLY A 1 255 ? 5.684  -20.440 0.063   1.00  17.95 ? 255 GLY A O   1 
ATOM   2048 N  N   . ARG A 1 256 ? 6.535  -18.593 0.978   1.00  16.65 ? 256 ARG A N   1 
ATOM   2049 C  CA  . ARG A 1 256 ? 7.841  -18.814 0.333   1.00  15.70 ? 256 ARG A CA  1 
ATOM   2050 C  C   . ARG A 1 256 ? 8.464  -20.107 0.842   1.00  18.32 ? 256 ARG A C   1 
ATOM   2051 O  O   . ARG A 1 256 ? 8.199  -20.505 1.966   1.00  16.37 ? 256 ARG A O   1 
ATOM   2052 C  CB  . ARG A 1 256 ? 8.743  -17.671 0.683   1.00  15.03 ? 256 ARG A CB  1 
ATOM   2053 C  CG  . ARG A 1 256 ? 8.480  -16.455 -0.206  1.00  13.86 ? 256 ARG A CG  1 
ATOM   2054 C  CD  . ARG A 1 256 ? 9.386  -15.339 0.241   1.00  13.00 ? 256 ARG A CD  1 
ATOM   2055 N  NE  . ARG A 1 256 ? 8.948  -14.802 1.523   1.00  11.72 ? 256 ARG A NE  1 
ATOM   2056 C  CZ  . ARG A 1 256 ? 9.546  -13.806 2.151   1.00  11.18 ? 256 ARG A CZ  1 
ATOM   2057 N  NH1 . ARG A 1 256 ? 10.653 -13.301 1.645   1.00  9.76  ? 256 ARG A NH1 1 
ATOM   2058 N  NH2 . ARG A 1 256 ? 9.031  -13.337 3.315   1.00  10.60 ? 256 ARG A NH2 1 
ATOM   2059 N  N   . LYS A 1 257 ? 9.252  -20.792 0.005   1.00  18.29 ? 257 LYS A N   1 
ATOM   2060 C  CA  . LYS A 1 257 ? 9.898  -22.051 0.433   1.00  19.54 ? 257 LYS A CA  1 
ATOM   2061 C  C   . LYS A 1 257 ? 11.351 -21.794 0.872   1.00  18.41 ? 257 LYS A C   1 
ATOM   2062 O  O   . LYS A 1 257 ? 12.151 -21.266 0.078   1.00  19.85 ? 257 LYS A O   1 
ATOM   2063 C  CB  . LYS A 1 257 ? 9.924  -23.028 -0.756  1.00  22.35 ? 257 LYS A CB  1 
ATOM   2064 C  CG  . LYS A 1 257 ? 10.491 -24.400 -0.361  1.00  26.96 ? 257 LYS A CG  1 
ATOM   2065 C  CD  . LYS A 1 257 ? 11.022 -25.213 -1.530  1.00  32.43 ? 257 LYS A CD  1 
ATOM   2066 C  CE  . LYS A 1 257 ? 10.011 -25.557 -2.601  1.00  34.79 ? 257 LYS A CE  1 
ATOM   2067 N  NZ  . LYS A 1 257 ? 10.692 -25.513 -3.939  1.00  39.90 ? 257 LYS A NZ  1 
ATOM   2068 N  N   . VAL A 1 258 ? 11.690 -22.161 2.096   1.00  16.26 ? 258 VAL A N   1 
ATOM   2069 C  CA  . VAL A 1 258 ? 13.060 -22.088 2.579   1.00  16.54 ? 258 VAL A CA  1 
ATOM   2070 C  C   . VAL A 1 258 ? 13.628 -23.509 2.380   1.00  15.83 ? 258 VAL A C   1 
ATOM   2071 O  O   . VAL A 1 258 ? 13.042 -24.502 2.899   1.00  15.69 ? 258 VAL A O   1 
ATOM   2072 C  CB  . VAL A 1 258 ? 13.137 -21.751 4.089   1.00  15.33 ? 258 VAL A CB  1 
ATOM   2073 C  CG1 . VAL A 1 258 ? 14.575 -21.720 4.565   1.00  15.53 ? 258 VAL A CG1 1 
ATOM   2074 C  CG2 . VAL A 1 258 ? 12.376 -20.449 4.425   1.00  15.80 ? 258 VAL A CG2 1 
ATOM   2075 N  N   . ARG A 1 259 ? 14.742 -23.589 1.664   1.00  14.89 ? 259 ARG A N   1 
ATOM   2076 C  CA  . ARG A 1 259 ? 15.385 -24.885 1.346   1.00  16.87 ? 259 ARG A CA  1 
ATOM   2077 C  C   . ARG A 1 259 ? 16.625 -25.007 2.181   1.00  19.00 ? 259 ARG A C   1 
ATOM   2078 O  O   . ARG A 1 259 ? 17.236 -23.980 2.534   1.00  18.01 ? 259 ARG A O   1 
ATOM   2079 C  CB  . ARG A 1 259 ? 15.743 -24.937 -0.151  1.00  15.69 ? 259 ARG A CB  1 
ATOM   2080 C  CG  . ARG A 1 259 ? 14.500 -25.028 -1.018  1.00  17.73 ? 259 ARG A CG  1 
ATOM   2081 C  CD  . ARG A 1 259 ? 14.776 -24.999 -2.503  1.00  16.70 ? 259 ARG A CD  1 
ATOM   2082 N  NE  . ARG A 1 259 ? 15.368 -23.730 -2.880  1.00  16.86 ? 259 ARG A NE  1 
ATOM   2083 C  CZ  . ARG A 1 259 ? 16.132 -23.532 -3.952  1.00  19.00 ? 259 ARG A CZ  1 
ATOM   2084 N  NH1 . ARG A 1 259 ? 16.478 -24.553 -4.696  1.00  22.08 ? 259 ARG A NH1 1 
ATOM   2085 N  NH2 . ARG A 1 259 ? 16.649 -22.337 -4.212  1.00  18.65 ? 259 ARG A NH2 1 
ATOM   2086 N  N   . ALA A 1 260 ? 17.002 -26.249 2.500   1.00  18.58 ? 260 ALA A N   1 
ATOM   2087 C  CA  . ALA A 1 260 ? 18.282 -26.502 3.121   1.00  19.54 ? 260 ALA A CA  1 
ATOM   2088 C  C   . ALA A 1 260 ? 19.251 -27.230 2.181   1.00  18.79 ? 260 ALA A C   1 
ATOM   2089 O  O   . ALA A 1 260 ? 18.830 -28.044 1.326   1.00  17.66 ? 260 ALA A O   1 
ATOM   2090 C  CB  . ALA A 1 260 ? 18.117 -27.281 4.437   1.00  21.44 ? 260 ALA A CB  1 
ATOM   2091 N  N   . SER A 1 261 ? 20.537 -26.912 2.356   1.00  17.75 ? 261 SER A N   1 
ATOM   2092 C  CA  . SER A 1 261 ? 21.638 -27.616 1.645   1.00  21.53 ? 261 SER A CA  1 
ATOM   2093 C  C   . SER A 1 261 ? 21.983 -28.971 2.323   1.00  21.07 ? 261 SER A C   1 
ATOM   2094 O  O   . SER A 1 261 ? 22.810 -29.687 1.855   1.00  21.55 ? 261 SER A O   1 
ATOM   2095 C  CB  . SER A 1 261 ? 22.917 -26.749 1.628   1.00  18.70 ? 261 SER A CB  1 
ATOM   2096 O  OG  . SER A 1 261 ? 23.525 -26.633 2.960   1.00  18.54 ? 261 SER A OG  1 
ATOM   2097 N  N   . PHE A 1 262 ? 21.364 -29.272 3.455   1.00  25.89 ? 262 PHE A N   1 
ATOM   2098 C  CA  . PHE A 1 262 ? 21.883 -30.310 4.352   1.00  27.00 ? 262 PHE A CA  1 
ATOM   2099 C  C   . PHE A 1 262 ? 20.674 -30.984 4.954   1.00  30.27 ? 262 PHE A C   1 
ATOM   2100 O  O   . PHE A 1 262 ? 19.602 -30.403 5.013   1.00  25.83 ? 262 PHE A O   1 
ATOM   2101 C  CB  . PHE A 1 262 ? 22.741 -29.680 5.451   1.00  22.84 ? 262 PHE A CB  1 
ATOM   2102 C  CG  . PHE A 1 262 ? 21.977 -28.708 6.327   1.00  24.70 ? 262 PHE A CG  1 
ATOM   2103 C  CD1 . PHE A 1 262 ? 21.446 -29.126 7.558   1.00  24.61 ? 262 PHE A CD1 1 
ATOM   2104 C  CD2 . PHE A 1 262 ? 21.776 -27.382 5.926   1.00  23.28 ? 262 PHE A CD2 1 
ATOM   2105 C  CE1 . PHE A 1 262 ? 20.730 -28.252 8.376   1.00  25.45 ? 262 PHE A CE1 1 
ATOM   2106 C  CE2 . PHE A 1 262 ? 21.071 -26.486 6.759   1.00  23.09 ? 262 PHE A CE2 1 
ATOM   2107 C  CZ  . PHE A 1 262 ? 20.534 -26.927 7.964   1.00  23.06 ? 262 PHE A CZ  1 
ATOM   2108 N  N   . HIS A 1 263 ? 20.866 -32.237 5.362   1.00  36.06 ? 263 HIS A N   1 
ATOM   2109 C  CA  . HIS A 1 263 ? 19.893 -33.050 6.089   1.00  41.26 ? 263 HIS A CA  1 
ATOM   2110 C  C   . HIS A 1 263 ? 20.657 -34.204 6.659   1.00  45.87 ? 263 HIS A C   1 
ATOM   2111 O  O   . HIS A 1 263 ? 21.885 -34.132 6.845   1.00  50.79 ? 263 HIS A O   1 
ATOM   2112 C  CB  . HIS A 1 263 ? 18.731 -33.533 5.195   1.00  45.02 ? 263 HIS A CB  1 
ATOM   2113 C  CG  . HIS A 1 263 ? 19.100 -34.603 4.178   1.00  46.31 ? 263 HIS A CG  1 
ATOM   2114 N  ND1 . HIS A 1 263 ? 20.325 -34.710 3.631   1.00  47.67 ? 263 HIS A ND1 1 
ATOM   2115 C  CD2 . HIS A 1 263 ? 18.313 -35.571 3.559   1.00  48.30 ? 263 HIS A CD2 1 
ATOM   2116 C  CE1 . HIS A 1 263 ? 20.328 -35.708 2.728   1.00  52.14 ? 263 HIS A CE1 1 
ATOM   2117 N  NE2 . HIS A 1 263 ? 19.098 -36.235 2.687   1.00  48.68 ? 263 HIS A NE2 1 
ATOM   2118 O  OXT . HIS A 1 263 ? 20.095 -35.242 6.954   1.00  55.12 ? 263 HIS A OXT 1 
HETATM 2119 ZN ZN  . ZN  B 2 .   ? 21.903 -6.306  6.438   1.00  12.92 ? 301 ZN  A ZN  1 
HETATM 2120 C  C1  . PEG C 3 .   ? 26.407 -26.127 13.419  1.00  47.81 ? 302 PEG A C1  1 
HETATM 2121 O  O1  . PEG C 3 .   ? 26.182 -25.321 14.621  1.00  38.89 ? 302 PEG A O1  1 
HETATM 2122 C  C2  . PEG C 3 .   ? 26.847 -27.592 13.631  1.00  52.58 ? 302 PEG A C2  1 
HETATM 2123 O  O2  . PEG C 3 .   ? 28.252 -27.714 13.956  1.00  53.88 ? 302 PEG A O2  1 
HETATM 2124 C  C3  . PEG C 3 .   ? 29.058 -28.224 12.877  1.00  45.51 ? 302 PEG A C3  1 
HETATM 2125 C  C4  . PEG C 3 .   ? 30.521 -27.900 13.179  1.00  49.31 ? 302 PEG A C4  1 
HETATM 2126 O  O4  . PEG C 3 .   ? 31.156 -27.175 12.097  1.00  31.96 ? 302 PEG A O4  1 
HETATM 2127 C  C1  . EDO D 4 .   ? 43.433 -0.981  9.403   1.00  37.82 ? 303 EDO A C1  1 
HETATM 2128 O  O1  . EDO D 4 .   ? 42.691 -2.112  9.938   1.00  30.69 ? 303 EDO A O1  1 
HETATM 2129 C  C2  . EDO D 4 .   ? 42.803 -0.571  8.077   1.00  32.79 ? 303 EDO A C2  1 
HETATM 2130 O  O2  . EDO D 4 .   ? 43.225 -1.392  6.952   1.00  28.56 ? 303 EDO A O2  1 
HETATM 2131 F  F27 . WWO E 5 .   ? 21.321 -3.380  1.582   1.00  22.38 ? 304 WWO A F27 1 
HETATM 2132 C  C5  . WWO E 5 .   ? 21.628 -2.781  2.731   1.00  22.67 ? 304 WWO A C5  1 
HETATM 2133 C  C4  . WWO E 5 .   ? 21.436 -3.530  3.928   1.00  22.53 ? 304 WWO A C4  1 
HETATM 2134 S  S7  . WWO E 5 .   ? 20.767 -5.244  3.885   1.00  23.34 ? 304 WWO A S7  1 
HETATM 2135 O  O9  . WWO E 5 .   ? 21.644 -6.322  3.268   1.00  23.15 ? 304 WWO A O9  1 
HETATM 2136 N  N10 . WWO E 5 .   ? 20.524 -5.702  5.596   1.00  17.85 ? 304 WWO A N10 1 
HETATM 2137 O  O8  . WWO E 5 .   ? 19.433 -5.405  3.194   1.00  23.19 ? 304 WWO A O8  1 
HETATM 2138 C  C3  . WWO E 5 .   ? 21.766 -2.879  5.140   1.00  24.44 ? 304 WWO A C3  1 
HETATM 2139 F  F12 . WWO E 5 .   ? 21.663 -3.412  6.370   1.00  25.46 ? 304 WWO A F12 1 
HETATM 2140 C  C2  . WWO E 5 .   ? 22.267 -1.572  5.141   1.00  26.34 ? 304 WWO A C2  1 
HETATM 2141 F  F13 . WWO E 5 .   ? 22.558 -1.031  6.349   1.00  24.99 ? 304 WWO A F13 1 
HETATM 2142 C  C6  . WWO E 5 .   ? 22.123 -1.454  2.706   1.00  25.13 ? 304 WWO A C6  1 
HETATM 2143 C  C1  . WWO E 5 .   ? 22.461 -0.860  3.932   1.00  27.15 ? 304 WWO A C1  1 
HETATM 2144 S  S11 . WWO E 5 .   ? 23.016 0.865   3.994   1.00  29.94 ? 304 WWO A S11 1 
HETATM 2145 O  O22 . WWO E 5 .   ? 22.191 1.491   5.141   1.00  32.80 ? 304 WWO A O22 1 
HETATM 2146 O  O23 . WWO E 5 .   ? 22.220 1.533   2.822   1.00  37.56 ? 304 WWO A O23 1 
HETATM 2147 C  C21 . WWO E 5 .   ? 24.728 1.415   3.901   1.00  33.41 ? 304 WWO A C21 1 
HETATM 2148 C  C24 . WWO E 5 .   ? 24.764 2.707   3.068   1.00  38.08 ? 304 WWO A C24 1 
HETATM 2149 O  O25 . WWO E 5 .   ? 26.038 2.884   2.520   1.00  44.27 ? 304 WWO A O25 1 
HETATM 2150 N  N26 . WWO E 5 .   ? 22.245 -0.737  1.445   1.00  27.15 ? 304 WWO A N26 1 
HETATM 2151 C  C14 . WWO E 5 .   ? 20.955 -0.513  0.824   1.00  27.13 ? 304 WWO A C14 1 
HETATM 2152 C  C15 . WWO E 5 .   ? 20.872 -0.378  -0.658  1.00  29.76 ? 304 WWO A C15 1 
HETATM 2153 C  C20 . WWO E 5 .   ? 21.233 -1.430  -1.514  1.00  31.18 ? 304 WWO A C20 1 
HETATM 2154 C  C19 . WWO E 5 .   ? 21.107 -1.287  -2.916  1.00  30.82 ? 304 WWO A C19 1 
HETATM 2155 C  C18 . WWO E 5 .   ? 20.617 -0.078  -3.431  1.00  32.27 ? 304 WWO A C18 1 
HETATM 2156 C  C17 . WWO E 5 .   ? 20.261 0.983   -2.578  1.00  32.70 ? 304 WWO A C17 1 
HETATM 2157 C  C16 . WWO E 5 .   ? 20.395 0.836   -1.195  1.00  30.02 ? 304 WWO A C16 1 
HETATM 2158 O  O   . HOH F 6 .   ? 22.676 -7.599  20.216  1.00  12.14 ? 401 HOH A O   1 
HETATM 2159 O  O   . HOH F 6 .   ? 6.247  -7.103  5.546   1.00  13.93 ? 402 HOH A O   1 
HETATM 2160 O  O   . HOH F 6 .   ? 15.736 -18.226 -4.588  1.00  17.66 ? 403 HOH A O   1 
HETATM 2161 O  O   . HOH F 6 .   ? 9.425  -3.086  8.713   1.00  15.83 ? 404 HOH A O   1 
HETATM 2162 O  O   . HOH F 6 .   ? 16.384 -10.871 17.063  1.00  13.88 ? 405 HOH A O   1 
HETATM 2163 O  O   . HOH F 6 .   ? 26.700 -23.550 8.557   1.00  15.13 ? 406 HOH A O   1 
HETATM 2164 O  O   . HOH F 6 .   ? 17.304 -3.839  9.071   1.00  12.16 ? 407 HOH A O   1 
HETATM 2165 O  O   . HOH F 6 .   ? 21.306 -21.690 13.470  1.00  16.53 ? 408 HOH A O   1 
HETATM 2166 O  O   . HOH F 6 .   ? 17.761 -6.591  22.030  1.00  18.27 ? 409 HOH A O   1 
HETATM 2167 O  O   . HOH F 6 .   ? 16.732 -4.227  20.440  1.00  21.85 ? 410 HOH A O   1 
HETATM 2168 O  O   . HOH F 6 .   ? 30.942 -5.299  -14.158 1.00  20.41 ? 411 HOH A O   1 
HETATM 2169 O  O   . HOH F 6 .   ? 16.402 -19.837 -2.643  1.00  14.11 ? 412 HOH A O   1 
HETATM 2170 O  O   . HOH F 6 .   ? 2.534  -0.976  1.980   1.00  17.09 ? 413 HOH A O   1 
HETATM 2171 O  O   . HOH F 6 .   ? 16.043 -15.445 -4.884  1.00  15.24 ? 414 HOH A O   1 
HETATM 2172 O  O   . HOH F 6 .   ? 31.035 -12.010 -10.073 1.00  19.60 ? 415 HOH A O   1 
HETATM 2173 O  O   . HOH F 6 .   ? 26.658 -19.988 -9.369  1.00  15.44 ? 416 HOH A O   1 
HETATM 2174 O  O   . HOH F 6 .   ? 25.530 -18.436 10.817  1.00  13.91 ? 417 HOH A O   1 
HETATM 2175 O  O   . HOH F 6 .   ? 6.959  -10.739 2.859   1.00  13.56 ? 418 HOH A O   1 
HETATM 2176 O  O   . HOH F 6 .   ? 20.910 -16.790 -9.306  1.00  16.54 ? 419 HOH A O   1 
HETATM 2177 O  O   . HOH F 6 .   ? 14.121 -21.329 -1.665  1.00  14.76 ? 420 HOH A O   1 
HETATM 2178 O  O   . HOH F 6 .   ? 5.942  -7.929  -3.496  1.00  17.37 ? 421 HOH A O   1 
HETATM 2179 O  O   . HOH F 6 .   ? 22.414 -15.358 -13.528 1.00  26.38 ? 422 HOH A O   1 
HETATM 2180 O  O   . HOH F 6 .   ? 30.926 -11.406 -13.842 1.00  17.02 ? 423 HOH A O   1 
HETATM 2181 O  O   . HOH F 6 .   ? 1.714  2.115   -2.590  1.00  15.79 ? 424 HOH A O   1 
HETATM 2182 O  O   . HOH F 6 .   ? 18.849 2.119   17.516  1.00  14.81 ? 425 HOH A O   1 
HETATM 2183 O  O   . HOH F 6 .   ? 19.698 4.231   11.613  1.00  14.47 ? 426 HOH A O   1 
HETATM 2184 O  O   . HOH F 6 .   ? 30.516 -2.656  -14.350 1.00  25.31 ? 427 HOH A O   1 
HETATM 2185 O  O   . HOH F 6 .   ? 37.294 10.051  2.175   1.00  20.76 ? 428 HOH A O   1 
HETATM 2186 O  O   . HOH F 6 .   ? 16.194 -2.705  15.820  1.00  18.93 ? 429 HOH A O   1 
HETATM 2187 O  O   . HOH F 6 .   ? 18.745 -12.807 -6.354  1.00  18.01 ? 430 HOH A O   1 
HETATM 2188 O  O   . HOH F 6 .   ? 34.416 -7.466  -5.017  1.00  16.05 ? 431 HOH A O   1 
HETATM 2189 O  O   . HOH F 6 .   ? 5.429  -14.757 -1.394  1.00  24.67 ? 432 HOH A O   1 
HETATM 2190 O  O   . HOH F 6 .   ? 39.459 4.027   15.881  1.00  23.48 ? 433 HOH A O   1 
HETATM 2191 O  O   . HOH F 6 .   ? 20.403 -24.070 14.276  1.00  18.29 ? 434 HOH A O   1 
HETATM 2192 O  O   . HOH F 6 .   ? 23.395 -16.126 20.310  1.00  21.61 ? 435 HOH A O   1 
HETATM 2193 O  O   . HOH F 6 .   ? 6.920  -0.830  7.771   1.00  14.60 ? 436 HOH A O   1 
HETATM 2194 O  O   . HOH F 6 .   ? 26.508 -11.042 27.196  1.00  19.29 ? 437 HOH A O   1 
HETATM 2195 O  O   . HOH F 6 .   ? 8.599  -9.963  -5.254  1.00  21.35 ? 438 HOH A O   1 
HETATM 2196 O  O   . HOH F 6 .   ? 34.045 -16.324 26.345  1.00  27.88 ? 439 HOH A O   1 
HETATM 2197 O  O   . HOH F 6 .   ? 18.285 4.855   13.858  1.00  18.82 ? 440 HOH A O   1 
HETATM 2198 O  O   . HOH F 6 .   ? 35.988 -8.682  -6.852  1.00  15.69 ? 441 HOH A O   1 
HETATM 2199 O  O   . HOH F 6 .   ? 12.916 -12.015 -3.947  1.00  18.99 ? 442 HOH A O   1 
HETATM 2200 O  O   . HOH F 6 .   ? 19.276 -17.166 -6.886  1.00  20.47 ? 443 HOH A O   1 
HETATM 2201 O  O   . HOH F 6 .   ? 13.774 -9.943  16.185  1.00  21.25 ? 444 HOH A O   1 
HETATM 2202 O  O   . HOH F 6 .   ? 3.658  -18.839 4.589   1.00  20.88 ? 445 HOH A O   1 
HETATM 2203 O  O   . HOH F 6 .   ? 36.097 12.230  3.674   1.00  21.17 ? 446 HOH A O   1 
HETATM 2204 O  O   . HOH F 6 .   ? 18.555 -25.273 -6.548  1.00  32.36 ? 447 HOH A O   1 
HETATM 2205 O  O   . HOH F 6 .   ? 26.063 -21.094 -12.795 1.00  25.61 ? 448 HOH A O   1 
HETATM 2206 O  O   . HOH F 6 .   ? 35.658 10.426  7.143   1.00  23.62 ? 449 HOH A O   1 
HETATM 2207 O  O   . HOH F 6 .   ? 17.405 -19.112 -6.670  1.00  21.75 ? 450 HOH A O   1 
HETATM 2208 O  O   . HOH F 6 .   ? 37.683 1.867   18.167  1.00  22.65 ? 451 HOH A O   1 
HETATM 2209 O  O   . HOH F 6 .   ? 13.084 1.694   -6.682  1.00  32.14 ? 452 HOH A O   1 
HETATM 2210 O  O   . HOH F 6 .   ? 21.042 7.570   9.928   1.00  22.99 ? 453 HOH A O   1 
HETATM 2211 O  O   . HOH F 6 .   ? 24.333 -23.095 -8.021  1.00  22.28 ? 454 HOH A O   1 
HETATM 2212 O  O   . HOH F 6 .   ? 37.775 13.357  5.548   1.00  20.63 ? 455 HOH A O   1 
HETATM 2213 O  O   . HOH F 6 .   ? 14.640 -13.337 -5.741  1.00  17.69 ? 456 HOH A O   1 
HETATM 2214 O  O   . HOH F 6 .   ? 19.245 4.419   16.360  1.00  20.00 ? 457 HOH A O   1 
HETATM 2215 O  O   . HOH F 6 .   ? 11.193 0.593   -2.476  1.00  18.73 ? 458 HOH A O   1 
HETATM 2216 O  O   . HOH F 6 .   ? 17.056 -27.262 8.336   1.00  28.81 ? 459 HOH A O   1 
HETATM 2217 O  O   . HOH F 6 .   ? 4.979  -8.676  3.911   1.00  24.16 ? 460 HOH A O   1 
HETATM 2218 O  O   . HOH F 6 .   ? 39.980 -16.557 23.275  1.00  21.05 ? 461 HOH A O   1 
HETATM 2219 O  O   . HOH F 6 .   ? 9.059  -6.297  -5.663  1.00  22.38 ? 462 HOH A O   1 
HETATM 2220 O  O   . HOH F 6 .   ? 43.374 -3.455  14.404  1.00  22.97 ? 463 HOH A O   1 
HETATM 2221 O  O   . HOH F 6 .   ? 11.099 -10.357 -6.513  1.00  20.82 ? 464 HOH A O   1 
HETATM 2222 O  O   . HOH F 6 .   ? 2.422  0.155   -3.833  1.00  26.79 ? 465 HOH A O   1 
HETATM 2223 O  O   . HOH F 6 .   ? 17.545 7.597   13.005  1.00  24.88 ? 466 HOH A O   1 
HETATM 2224 O  O   . HOH F 6 .   ? 27.471 -6.189  24.694  1.00  30.49 ? 467 HOH A O   1 
HETATM 2225 O  O   . HOH F 6 .   ? 43.634 -5.175  18.299  1.00  20.27 ? 468 HOH A O   1 
HETATM 2226 O  O   . HOH F 6 .   ? 18.928 -16.907 -11.264 1.00  19.91 ? 469 HOH A O   1 
HETATM 2227 O  O   . HOH F 6 .   ? 7.508  2.364   -3.900  1.00  18.82 ? 470 HOH A O   1 
HETATM 2228 O  O   . HOH F 6 .   ? 24.480 -11.678 -19.726 1.00  24.73 ? 471 HOH A O   1 
HETATM 2229 O  O   . HOH F 6 .   ? 25.361 -30.699 -5.650  1.00  29.26 ? 472 HOH A O   1 
HETATM 2230 O  O   . HOH F 6 .   ? 33.708 -15.394 -11.419 1.00  30.43 ? 473 HOH A O   1 
HETATM 2231 O  O   . HOH F 6 .   ? 28.819 -1.569  -9.006  1.00  20.51 ? 474 HOH A O   1 
HETATM 2232 O  O   . HOH F 6 .   ? 4.970  -16.058 8.247   1.00  22.66 ? 475 HOH A O   1 
HETATM 2233 O  O   . HOH F 6 .   ? 23.445 -22.604 17.002  1.00  24.48 ? 476 HOH A O   1 
HETATM 2234 O  O   . HOH F 6 .   ? 6.706  -4.220  -6.467  1.00  38.69 ? 477 HOH A O   1 
HETATM 2235 O  O   . HOH F 6 .   ? 29.685 -22.306 16.357  1.00  21.51 ? 478 HOH A O   1 
HETATM 2236 O  O   . HOH F 6 .   ? 0.525  -10.332 -3.431  1.00  32.49 ? 479 HOH A O   1 
HETATM 2237 O  O   . HOH F 6 .   ? 13.577 -14.743 19.112  1.00  26.41 ? 480 HOH A O   1 
HETATM 2238 O  O   . HOH F 6 .   ? 43.060 -4.781  20.999  1.00  18.71 ? 481 HOH A O   1 
HETATM 2239 O  O   . HOH F 6 .   ? 6.542  -14.909 -6.000  1.00  24.30 ? 482 HOH A O   1 
HETATM 2240 O  O   . HOH F 6 .   ? 19.484 -19.974 -9.718  1.00  22.47 ? 483 HOH A O   1 
HETATM 2241 O  O   . HOH F 6 .   ? 3.131  2.497   10.191  1.00  34.51 ? 484 HOH A O   1 
HETATM 2242 O  O   . HOH F 6 .   ? 1.690  -7.770  4.591   1.00  21.25 ? 485 HOH A O   1 
HETATM 2243 O  O   . HOH F 6 .   ? 32.930 -26.201 14.611  1.00  32.35 ? 486 HOH A O   1 
HETATM 2244 O  O   . HOH F 6 .   ? 31.755 -26.944 5.607   1.00  25.16 ? 487 HOH A O   1 
HETATM 2245 O  O   . HOH F 6 .   ? 10.775 -9.954  -13.198 1.00  47.57 ? 488 HOH A O   1 
HETATM 2246 O  O   . HOH F 6 .   ? 41.675 2.872   8.894   1.00  31.74 ? 489 HOH A O   1 
HETATM 2247 O  O   . HOH F 6 .   ? 15.074 2.367   -5.305  1.00  29.43 ? 490 HOH A O   1 
HETATM 2248 O  O   . HOH F 6 .   ? 33.355 -22.894 15.422  1.00  34.45 ? 491 HOH A O   1 
HETATM 2249 O  O   . HOH F 6 .   ? 10.241 5.924   8.272   1.00  23.92 ? 492 HOH A O   1 
HETATM 2250 O  O   . HOH F 6 .   ? 16.275 -15.918 -9.061  1.00  37.34 ? 493 HOH A O   1 
HETATM 2251 O  O   . HOH F 6 .   ? 26.179 -26.143 10.112  1.00  22.34 ? 494 HOH A O   1 
HETATM 2252 O  O   . HOH F 6 .   ? 40.126 -15.336 20.986  1.00  22.85 ? 495 HOH A O   1 
HETATM 2253 O  O   . HOH F 6 .   ? 5.260  -2.864  7.287   1.00  29.27 ? 496 HOH A O   1 
HETATM 2254 O  O   . HOH F 6 .   ? 32.213 -20.880 14.163  1.00  20.39 ? 497 HOH A O   1 
HETATM 2255 O  O   . HOH F 6 .   ? 18.139 10.283  14.157  1.00  32.79 ? 498 HOH A O   1 
HETATM 2256 O  O   . HOH F 6 .   ? 34.351 -19.084 13.991  1.00  30.02 ? 499 HOH A O   1 
HETATM 2257 O  O   . HOH F 6 .   ? 20.732 -7.909  -18.270 1.00  20.33 ? 500 HOH A O   1 
HETATM 2258 O  O   . HOH F 6 .   ? 25.913 -16.275 -15.691 1.00  30.03 ? 501 HOH A O   1 
HETATM 2259 O  O   . HOH F 6 .   ? 3.697  11.336  2.880   1.00  31.83 ? 502 HOH A O   1 
HETATM 2260 O  O   . HOH F 6 .   ? 23.934 -24.108 14.777  1.00  37.04 ? 503 HOH A O   1 
HETATM 2261 O  O   . HOH F 6 .   ? 37.627 8.635   10.174  1.00  27.44 ? 504 HOH A O   1 
HETATM 2262 O  O   . HOH F 6 .   ? 23.737 -18.943 20.232  1.00  24.67 ? 505 HOH A O   1 
HETATM 2263 O  O   . HOH F 6 .   ? 30.294 -19.244 -12.319 1.00  35.75 ? 506 HOH A O   1 
HETATM 2264 O  O   . HOH F 6 .   ? 17.981 -21.778 -6.780  1.00  28.36 ? 507 HOH A O   1 
HETATM 2265 O  O   . HOH F 6 .   ? 20.949 -22.181 18.078  1.00  40.45 ? 508 HOH A O   1 
HETATM 2266 O  O   . HOH F 6 .   ? 8.240  -15.054 13.883  1.00  29.17 ? 509 HOH A O   1 
HETATM 2267 O  O   . HOH F 6 .   ? 22.121 -17.614 -17.435 1.00  40.85 ? 510 HOH A O   1 
HETATM 2268 O  O   . HOH F 6 .   ? 34.575 -16.512 15.178  1.00  35.45 ? 511 HOH A O   1 
HETATM 2269 O  O   . HOH F 6 .   ? 28.537 -23.662 -9.865  1.00  34.55 ? 512 HOH A O   1 
HETATM 2270 O  O   . HOH F 6 .   ? 18.548 -27.541 11.259  1.00  23.93 ? 513 HOH A O   1 
HETATM 2271 O  O   . HOH F 6 .   ? 4.123  -1.448  9.556   1.00  24.69 ? 514 HOH A O   1 
HETATM 2272 O  O   . HOH F 6 .   ? 25.041 -29.019 -1.003  1.00  31.63 ? 515 HOH A O   1 
HETATM 2273 O  O   . HOH F 6 .   ? 43.990 -9.233  8.448   1.00  33.99 ? 516 HOH A O   1 
HETATM 2274 O  O   . HOH F 6 .   ? 13.606 -6.660  -13.396 1.00  41.29 ? 517 HOH A O   1 
HETATM 2275 O  O   . HOH F 6 .   ? 6.385  -5.194  8.779   1.00  22.35 ? 518 HOH A O   1 
HETATM 2276 O  O   . HOH F 6 .   ? 2.290  -9.892  -0.589  1.00  25.35 ? 519 HOH A O   1 
HETATM 2277 O  O   . HOH F 6 .   ? 9.461  0.221   14.458  1.00  26.41 ? 520 HOH A O   1 
HETATM 2278 O  O   . HOH F 6 .   ? 11.999 1.717   17.360  1.00  36.16 ? 521 HOH A O   1 
HETATM 2279 O  O   . HOH F 6 .   ? 5.756  5.541   16.714  1.00  38.46 ? 522 HOH A O   1 
HETATM 2280 O  O   . HOH F 6 .   ? 4.749  9.162   1.906   1.00  23.17 ? 523 HOH A O   1 
HETATM 2281 O  O   . HOH F 6 .   ? 8.265  8.225   -0.014  0.50  32.20 ? 524 HOH A O   1 
HETATM 2282 O  O   . HOH F 6 .   ? 3.677  9.117   7.742   1.00  25.50 ? 525 HOH A O   1 
HETATM 2283 O  O   . HOH F 6 .   ? 3.686  -6.677  6.096   1.00  27.82 ? 526 HOH A O   1 
HETATM 2284 O  O   . HOH F 6 .   ? 10.409 11.343  5.602   1.00  37.02 ? 527 HOH A O   1 
HETATM 2285 O  O   . HOH F 6 .   ? 12.423 7.928   4.764   1.00  39.56 ? 528 HOH A O   1 
HETATM 2286 O  O   . HOH F 6 .   ? 5.404  -8.234  -6.485  1.00  28.72 ? 529 HOH A O   1 
HETATM 2287 O  O   . HOH F 6 .   ? 6.667  -11.811 -6.100  1.00  46.22 ? 530 HOH A O   1 
HETATM 2288 O  O   . HOH F 6 .   ? 7.175  -15.558 -3.416  1.00  29.05 ? 531 HOH A O   1 
HETATM 2289 O  O   . HOH F 6 .   ? 2.717  -15.357 5.769   1.00  21.99 ? 532 HOH A O   1 
HETATM 2290 O  O   . HOH F 6 .   ? 9.743  -23.601 3.660   1.00  27.58 ? 533 HOH A O   1 
HETATM 2291 O  O   . HOH F 6 .   ? 10.909 -21.115 7.530   1.00  29.46 ? 534 HOH A O   1 
HETATM 2292 O  O   . HOH F 6 .   ? 17.843 -29.701 7.080   1.00  28.58 ? 535 HOH A O   1 
HETATM 2293 O  O   . HOH F 6 .   ? 15.298 -33.625 -2.568  1.00  38.08 ? 536 HOH A O   1 
HETATM 2294 O  O   . HOH F 6 .   ? 10.367 -25.724 13.090  1.00  29.44 ? 537 HOH A O   1 
HETATM 2295 O  O   . HOH F 6 .   ? 8.668  -17.750 8.557   1.00  30.37 ? 538 HOH A O   1 
HETATM 2296 O  O   . HOH F 6 .   ? 1.735  -22.235 11.929  1.00  38.46 ? 539 HOH A O   1 
HETATM 2297 O  O   . HOH F 6 .   ? 4.598  -26.058 15.237  1.00  25.85 ? 540 HOH A O   1 
HETATM 2298 O  O   . HOH F 6 .   ? 3.342  -25.654 12.736  1.00  43.64 ? 541 HOH A O   1 
HETATM 2299 O  O   . HOH F 6 .   ? 31.753 -13.731 -0.054  1.00  25.28 ? 542 HOH A O   1 
HETATM 2300 O  O   . HOH F 6 .   ? 37.299 -21.030 -11.176 1.00  32.50 ? 543 HOH A O   1 
HETATM 2301 O  O   . HOH F 6 .   ? 46.900 -10.174 0.538   0.50  24.73 ? 544 HOH A O   1 
HETATM 2302 O  O   . HOH F 6 .   ? 33.383 2.948   -1.455  1.00  41.67 ? 545 HOH A O   1 
HETATM 2303 O  O   . HOH F 6 .   ? 21.177 -1.332  9.030   1.00  23.09 ? 546 HOH A O   1 
HETATM 2304 O  O   . HOH F 6 .   ? 37.412 -5.831  -8.094  1.00  27.93 ? 547 HOH A O   1 
HETATM 2305 O  O   . HOH F 6 .   ? 13.447 -4.925  15.771  1.00  28.88 ? 548 HOH A O   1 
HETATM 2306 O  O   . HOH F 6 .   ? 14.634 -9.580  13.788  1.00  24.85 ? 549 HOH A O   1 
HETATM 2307 O  O   . HOH F 6 .   ? 16.633 -22.968 16.958  1.00  31.43 ? 550 HOH A O   1 
HETATM 2308 O  O   . HOH F 6 .   ? 46.322 -4.441  18.545  1.00  29.34 ? 551 HOH A O   1 
HETATM 2309 O  O   . HOH F 6 .   ? 12.947 -14.547 -7.260  1.00  30.89 ? 552 HOH A O   1 
HETATM 2310 O  O   . HOH F 6 .   ? 23.715 -13.906 24.202  1.00  30.52 ? 553 HOH A O   1 
HETATM 2311 O  O   . HOH F 6 .   ? 36.167 -16.450 17.505  1.00  24.67 ? 554 HOH A O   1 
HETATM 2312 O  O   . HOH F 6 .   ? 32.273 4.971   18.130  1.00  31.77 ? 555 HOH A O   1 
HETATM 2313 O  O   . HOH F 6 .   ? 34.915 9.839   15.160  1.00  34.23 ? 556 HOH A O   1 
HETATM 2314 O  O   . HOH F 6 .   ? 25.648 13.375  16.354  1.00  22.09 ? 557 HOH A O   1 
HETATM 2315 O  O   . HOH F 6 .   ? 38.051 -2.263  19.718  1.00  25.63 ? 558 HOH A O   1 
HETATM 2316 O  O   . HOH F 6 .   ? 29.446 13.516  10.478  1.00  31.86 ? 559 HOH A O   1 
HETATM 2317 O  O   . HOH F 6 .   ? 34.226 -13.005 -1.447  1.00  28.63 ? 560 HOH A O   1 
HETATM 2318 O  O   . HOH F 6 .   ? 27.929 -24.897 1.187   1.00  16.22 ? 561 HOH A O   1 
HETATM 2319 O  O   . HOH F 6 .   ? 29.783 -30.413 -1.153  1.00  32.80 ? 562 HOH A O   1 
HETATM 2320 O  O   . HOH F 6 .   ? 25.913 -22.447 18.729  1.00  31.53 ? 563 HOH A O   1 
HETATM 2321 O  O   . HOH F 6 .   ? 35.732 -28.085 10.865  1.00  31.71 ? 564 HOH A O   1 
HETATM 2322 O  O   . HOH F 6 .   ? 36.594 -17.778 26.205  1.00  29.07 ? 565 HOH A O   1 
HETATM 2323 O  O   . HOH F 6 .   ? 34.115 -16.134 29.027  1.00  35.93 ? 566 HOH A O   1 
HETATM 2324 O  O   . HOH F 6 .   ? 37.287 -13.534 30.585  1.00  13.83 ? 567 HOH A O   1 
HETATM 2325 O  O   . HOH F 6 .   ? 35.863 -13.875 28.570  1.00  29.53 ? 568 HOH A O   1 
HETATM 2326 O  O   . HOH F 6 .   ? 44.047 -6.943  17.005  1.00  27.29 ? 569 HOH A O   1 
HETATM 2327 O  O   . HOH F 6 .   ? 14.278 -18.273 22.335  1.00  29.16 ? 570 HOH A O   1 
HETATM 2328 O  O   . HOH F 6 .   ? 18.465 -25.865 13.446  1.00  32.86 ? 571 HOH A O   1 
HETATM 2329 O  O   . HOH F 6 .   ? 19.310 2.574   1.925   1.00  32.36 ? 572 HOH A O   1 
HETATM 2330 O  O   . HOH F 6 .   ? 13.391 -7.127  -8.073  1.00  22.42 ? 573 HOH A O   1 
HETATM 2331 O  O   . HOH F 6 .   ? 13.041 -4.527  -7.017  1.00  24.20 ? 574 HOH A O   1 
HETATM 2332 O  O   . HOH F 6 .   ? 11.218 -4.653  -5.118  1.00  17.81 ? 575 HOH A O   1 
HETATM 2333 O  O   . HOH F 6 .   ? 32.105 0.203   24.095  1.00  37.02 ? 576 HOH A O   1 
HETATM 2334 O  O   . HOH F 6 .   ? 14.378 -0.601  16.140  1.00  35.55 ? 577 HOH A O   1 
HETATM 2335 O  O   . HOH F 6 .   ? 29.670 -17.088 -14.188 1.00  28.60 ? 578 HOH A O   1 
HETATM 2336 O  O   . HOH F 6 .   ? 30.028 -19.301 22.925  1.00  34.36 ? 579 HOH A O   1 
HETATM 2337 O  O   . HOH F 6 .   ? 18.244 7.542   10.536  1.00  30.96 ? 580 HOH A O   1 
HETATM 2338 O  O   . HOH F 6 .   ? 20.665 11.252  11.667  1.00  38.08 ? 581 HOH A O   1 
HETATM 2339 O  O   . HOH F 6 .   ? 8.109  -4.828  10.787  1.00  29.96 ? 582 HOH A O   1 
HETATM 2340 O  O   . HOH F 6 .   ? -1.029 -12.762 2.659   1.00  34.47 ? 583 HOH A O   1 
HETATM 2341 O  O   . HOH F 6 .   ? 22.936 1.657   -15.792 1.00  29.07 ? 584 HOH A O   1 
HETATM 2342 O  O   . HOH F 6 .   ? 32.212 -12.216 25.993  1.00  26.06 ? 585 HOH A O   1 
HETATM 2343 O  O   . HOH F 6 .   ? 34.187 -13.894 25.013  1.00  25.71 ? 586 HOH A O   1 
HETATM 2344 O  O   . HOH F 6 .   ? 25.130 -15.609 22.479  1.00  20.60 ? 587 HOH A O   1 
HETATM 2345 O  O   . HOH F 6 .   ? 16.507 -16.329 21.546  1.00  27.07 ? 588 HOH A O   1 
HETATM 2346 O  O   . HOH F 6 .   ? 12.828 -1.951  -8.518  1.00  26.03 ? 589 HOH A O   1 
HETATM 2347 O  O   . HOH F 6 .   ? 10.088 -1.933  -4.653  1.00  27.01 ? 590 HOH A O   1 
HETATM 2348 O  O   . HOH F 6 .   ? 4.718  -1.742  -3.161  1.00  33.75 ? 591 HOH A O   1 
HETATM 2349 O  O   . HOH F 6 .   ? 8.520  0.853   -1.684  1.00  14.11 ? 592 HOH A O   1 
HETATM 2350 O  O   . HOH F 6 .   ? 41.746 -2.027  12.644  1.00  17.98 ? 593 HOH A O   1 
HETATM 2351 O  O   . HOH F 6 .   ? 25.922 0.396   6.849   1.00  25.85 ? 594 HOH A O   1 
HETATM 2352 O  O   . HOH F 6 .   ? 37.802 -6.329  22.079  1.00  31.70 ? 595 HOH A O   1 
HETATM 2353 O  O   . HOH F 6 .   ? 20.074 -15.490 -13.142 1.00  26.34 ? 596 HOH A O   1 
HETATM 2354 O  O   . HOH F 6 .   ? 42.278 -2.358  20.964  1.00  31.15 ? 597 HOH A O   1 
HETATM 2355 O  O   . HOH F 6 .   ? 27.627 -23.999 16.773  1.00  28.98 ? 598 HOH A O   1 
HETATM 2356 O  O   . HOH F 6 .   ? 28.365 4.325   4.424   1.00  32.96 ? 599 HOH A O   1 
HETATM 2357 O  O   . HOH F 6 .   ? 26.379 0.610   -8.170  1.00  21.14 ? 600 HOH A O   1 
HETATM 2358 O  O   . HOH F 6 .   ? 32.404 2.133   3.425   1.00  29.31 ? 601 HOH A O   1 
HETATM 2359 O  O   . HOH F 6 .   ? 29.092 1.653   -7.574  1.00  27.87 ? 602 HOH A O   1 
HETATM 2360 O  O   . HOH F 6 .   ? 32.730 6.406   0.481   1.00  42.57 ? 603 HOH A O   1 
HETATM 2361 O  O   . HOH F 6 .   ? 45.211 -10.579 5.129   1.00  50.05 ? 604 HOH A O   1 
HETATM 2362 O  O   . HOH F 6 .   ? 28.826 -6.381  -15.120 1.00  15.28 ? 605 HOH A O   1 
HETATM 2363 O  O   . HOH F 6 .   ? 11.354 -16.532 -6.185  1.00  37.18 ? 606 HOH A O   1 
HETATM 2364 O  O   . HOH F 6 .   ? 38.274 9.418   5.961   1.00  31.22 ? 607 HOH A O   1 
HETATM 2365 O  O   . HOH F 6 .   ? 38.449 8.073   3.683   1.00  32.39 ? 608 HOH A O   1 
HETATM 2366 O  O   . HOH F 6 .   ? 10.298 -8.107  -7.692  1.00  39.80 ? 609 HOH A O   1 
HETATM 2367 O  O   . HOH F 6 .   ? 13.475 7.096   19.893  1.00  40.10 ? 610 HOH A O   1 
HETATM 2368 O  O   . HOH F 6 .   ? 16.361 2.042   18.677  1.00  20.85 ? 611 HOH A O   1 
HETATM 2369 O  O   . HOH F 6 .   ? 12.186 2.724   19.843  1.00  31.48 ? 612 HOH A O   1 
HETATM 2370 O  O   . HOH F 6 .   ? 27.881 -12.422 -18.713 1.00  36.87 ? 613 HOH A O   1 
HETATM 2371 O  O   . HOH F 6 .   ? 42.294 0.412   13.362  1.00  33.02 ? 614 HOH A O   1 
HETATM 2372 O  O   . HOH F 6 .   ? 13.991 9.105   3.164   1.00  47.20 ? 615 HOH A O   1 
HETATM 2373 O  O   . HOH F 6 .   ? -1.083 0.400   5.086   1.00  39.57 ? 616 HOH A O   1 
HETATM 2374 O  O   . HOH F 6 .   ? 0.159  -1.342  0.916   1.00  32.70 ? 617 HOH A O   1 
HETATM 2375 O  O   . HOH F 6 .   ? 6.116  -19.410 8.465   1.00  41.66 ? 618 HOH A O   1 
HETATM 2376 O  O   . HOH F 6 .   ? 3.818  -18.633 7.605   1.00  32.04 ? 619 HOH A O   1 
HETATM 2377 O  O   . HOH F 6 .   ? 26.472 -17.647 23.778  1.00  31.58 ? 620 HOH A O   1 
HETATM 2378 O  O   . HOH F 6 .   ? 37.804 -3.753  22.302  1.00  37.97 ? 621 HOH A O   1 
HETATM 2379 O  O   . HOH F 6 .   ? 37.597 -15.708 25.100  1.00  26.07 ? 622 HOH A O   1 
HETATM 2380 O  O   . HOH F 6 .   ? 20.043 5.058   2.981   1.00  47.42 ? 623 HOH A O   1 
HETATM 2381 O  O   . HOH F 6 .   ? 19.000 2.687   -5.842  1.00  38.54 ? 624 HOH A O   1 
HETATM 2382 O  O   . HOH F 6 .   ? 40.291 -14.113 -9.772  1.00  42.38 ? 625 HOH A O   1 
HETATM 2383 O  O   . HOH F 6 .   ? 41.509 -5.091  -5.425  1.00  52.79 ? 626 HOH A O   1 
HETATM 2384 O  O   . HOH F 6 .   ? 35.356 -0.634  -7.218  1.00  32.10 ? 627 HOH A O   1 
HETATM 2385 O  O   . HOH F 6 .   ? 16.310 -25.427 15.279  1.00  27.97 ? 628 HOH A O   1 
HETATM 2386 O  O   . HOH F 6 .   ? 28.896 -11.962 28.415  1.00  37.09 ? 629 HOH A O   1 
HETATM 2387 O  O   . HOH F 6 .   ? 33.719 -19.213 21.677  1.00  37.83 ? 630 HOH A O   1 
HETATM 2388 O  O   . HOH F 6 .   ? 40.966 -20.962 23.374  1.00  35.06 ? 631 HOH A O   1 
HETATM 2389 O  O   . HOH F 6 .   ? 40.194 -11.053 18.387  1.00  31.62 ? 632 HOH A O   1 
HETATM 2390 O  O   . HOH F 6 .   ? 39.631 -14.078 4.143   1.00  30.75 ? 633 HOH A O   1 
HETATM 2391 O  O   . HOH F 6 .   ? 38.492 -18.873 11.521  1.00  35.87 ? 634 HOH A O   1 
HETATM 2392 O  O   . HOH F 6 .   ? 18.959 -23.496 16.907  1.00  34.59 ? 635 HOH A O   1 
HETATM 2393 O  O   . HOH F 6 .   ? 33.554 -9.490  26.734  1.00  32.44 ? 636 HOH A O   1 
HETATM 2394 O  O   . HOH F 6 .   ? 29.456 0.937   24.079  1.00  37.67 ? 637 HOH A O   1 
HETATM 2395 O  O   . HOH F 6 .   ? 7.026  -7.656  14.596  1.00  32.20 ? 638 HOH A O   1 
HETATM 2396 O  O   . HOH F 6 .   ? 0.593  -12.687 5.595   1.00  36.20 ? 639 HOH A O   1 
HETATM 2397 O  O   . HOH F 6 .   ? 18.037 7.476   6.827   1.00  29.64 ? 640 HOH A O   1 
HETATM 2398 O  O   . HOH F 6 .   ? 20.437 6.781   4.942   1.00  39.23 ? 641 HOH A O   1 
HETATM 2399 O  O   . HOH F 6 .   ? 21.779 12.780  9.429   1.00  46.49 ? 642 HOH A O   1 
HETATM 2400 O  O   . HOH F 6 .   ? 31.568 7.523   4.398   1.00  34.19 ? 643 HOH A O   1 
HETATM 2401 O  O   . HOH F 6 .   ? 3.424  -3.802  -0.877  1.00  32.83 ? 644 HOH A O   1 
HETATM 2402 O  O   . HOH F 6 .   ? 22.189 -30.051 -1.644  1.00  32.89 ? 645 HOH A O   1 
HETATM 2403 O  O   . HOH F 6 .   ? 25.585 -28.252 3.330   1.00  32.41 ? 646 HOH A O   1 
HETATM 2404 O  O   . HOH F 6 .   ? 45.071 -3.716  -0.127  1.00  33.45 ? 647 HOH A O   1 
HETATM 2405 O  O   . HOH F 6 .   ? 14.749 -6.467  20.007  1.00  36.72 ? 648 HOH A O   1 
HETATM 2406 O  O   . HOH F 6 .   ? 17.477 -9.607  27.229  1.00  32.27 ? 649 HOH A O   1 
HETATM 2407 O  O   . HOH F 6 .   ? 23.675 1.795   -12.954 1.00  43.45 ? 650 HOH A O   1 
HETATM 2408 O  O   . HOH F 6 .   ? 28.019 13.953  17.370  1.00  38.36 ? 651 HOH A O   1 
HETATM 2409 O  O   . HOH F 6 .   ? 42.734 -13.471 10.037  1.00  41.80 ? 652 HOH A O   1 
HETATM 2410 O  O   . HOH F 6 .   ? 8.306  -15.308 -7.717  1.00  30.23 ? 653 HOH A 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   MET 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   ARG 4   4   ?   ?   ?   A . n 
A 1 5   LEU 5   5   ?   ?   ?   A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   TRP 7   7   7   TRP TRP A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  TRP 18  18  18  TRP TRP A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  SER 64  64  64  SER SER 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  PHE 68  68  68  PHE PHE A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  TRP 99  99  99  TRP TRP A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 HIS 109 109 109 HIS HIS A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 HIS 124 124 124 HIS HIS A . n 
A 1 125 TRP 125 125 125 TRP TRP A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 PRO 140 140 140 PRO PRO A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 GLN 160 160 160 GLN GLN A . n 
A 1 161 LYS 161 161 161 LYS LYS A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 PRO 189 189 189 PRO PRO A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 TRP 191 191 191 TRP TRP A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 TRP 194 194 194 TRP TRP A . n 
A 1 195 THR 195 195 195 THR THR A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 PRO 203 203 203 PRO PRO A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 TRP 211 211 211 TRP TRP A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 PRO 217 217 217 PRO PRO A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 GLN 223 223 223 GLN GLN A . n 
A 1 224 GLN 224 224 224 GLN GLN A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 PHE 228 228 228 PHE PHE A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 CYS 233 233 233 CYS CYS A . n 
A 1 234 THR 234 234 234 THR THR A . n 
A 1 235 ALA 235 235 235 ALA ALA A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 SER 245 245 245 SER SER A . n 
A 1 246 ASN 246 246 246 ASN ASN A . n 
A 1 247 HIS 247 247 247 HIS HIS A . n 
A 1 248 ARG 248 248 248 ARG ARG A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 PRO 250 250 250 PRO PRO A . n 
A 1 251 GLN 251 251 251 GLN GLN A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 LYS 257 257 257 LYS LYS A . n 
A 1 258 VAL 258 258 258 VAL VAL A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 HIS 263 263 263 HIS HIS A . 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 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 PEG 1   302 1   PEG PEG A . 
D 4 EDO 1   303 2   EDO EDO A . 
E 5 WWO 1   304 1   WWO WWO A . 
F 6 HOH 1   401 1   HOH HOH A . 
F 6 HOH 2   402 2   HOH HOH A . 
F 6 HOH 3   403 3   HOH HOH A . 
F 6 HOH 4   404 4   HOH HOH A . 
F 6 HOH 5   405 5   HOH HOH A . 
F 6 HOH 6   406 6   HOH HOH A . 
F 6 HOH 7   407 7   HOH HOH A . 
F 6 HOH 8   408 8   HOH HOH A . 
F 6 HOH 9   409 9   HOH HOH A . 
F 6 HOH 10  410 10  HOH HOH A . 
F 6 HOH 11  411 11  HOH HOH A . 
F 6 HOH 12  412 12  HOH HOH A . 
F 6 HOH 13  413 13  HOH HOH A . 
F 6 HOH 14  414 14  HOH HOH A . 
F 6 HOH 15  415 15  HOH HOH A . 
F 6 HOH 16  416 16  HOH HOH A . 
F 6 HOH 17  417 17  HOH HOH A . 
F 6 HOH 18  418 18  HOH HOH A . 
F 6 HOH 19  419 19  HOH HOH A . 
F 6 HOH 20  420 20  HOH HOH A . 
F 6 HOH 21  421 21  HOH HOH A . 
F 6 HOH 22  422 22  HOH HOH A . 
F 6 HOH 23  423 23  HOH HOH A . 
F 6 HOH 24  424 24  HOH HOH A . 
F 6 HOH 25  425 25  HOH HOH A . 
F 6 HOH 26  426 26  HOH HOH A . 
F 6 HOH 27  427 27  HOH HOH A . 
F 6 HOH 28  428 28  HOH HOH A . 
F 6 HOH 29  429 29  HOH HOH A . 
F 6 HOH 30  430 30  HOH HOH A . 
F 6 HOH 31  431 31  HOH HOH A . 
F 6 HOH 32  432 32  HOH HOH A . 
F 6 HOH 33  433 33  HOH HOH A . 
F 6 HOH 34  434 34  HOH HOH A . 
F 6 HOH 35  435 35  HOH HOH A . 
F 6 HOH 36  436 36  HOH HOH A . 
F 6 HOH 37  437 37  HOH HOH A . 
F 6 HOH 38  438 38  HOH HOH A . 
F 6 HOH 39  439 39  HOH HOH A . 
F 6 HOH 40  440 40  HOH HOH A . 
F 6 HOH 41  441 41  HOH HOH A . 
F 6 HOH 42  442 42  HOH HOH A . 
F 6 HOH 43  443 43  HOH HOH A . 
F 6 HOH 44  444 44  HOH HOH A . 
F 6 HOH 45  445 45  HOH HOH A . 
F 6 HOH 46  446 46  HOH HOH A . 
F 6 HOH 47  447 47  HOH HOH A . 
F 6 HOH 48  448 48  HOH HOH A . 
F 6 HOH 49  449 49  HOH HOH A . 
F 6 HOH 50  450 50  HOH HOH A . 
F 6 HOH 51  451 51  HOH HOH A . 
F 6 HOH 52  452 52  HOH HOH A . 
F 6 HOH 53  453 53  HOH HOH A . 
F 6 HOH 54  454 54  HOH HOH A . 
F 6 HOH 55  455 55  HOH HOH A . 
F 6 HOH 56  456 56  HOH HOH A . 
F 6 HOH 57  457 57  HOH HOH A . 
F 6 HOH 58  458 58  HOH HOH A . 
F 6 HOH 59  459 59  HOH HOH A . 
F 6 HOH 60  460 60  HOH HOH A . 
F 6 HOH 61  461 61  HOH HOH A . 
F 6 HOH 62  462 62  HOH HOH A . 
F 6 HOH 63  463 63  HOH HOH A . 
F 6 HOH 64  464 64  HOH HOH A . 
F 6 HOH 65  465 65  HOH HOH A . 
F 6 HOH 66  466 66  HOH HOH A . 
F 6 HOH 67  467 67  HOH HOH A . 
F 6 HOH 68  468 68  HOH HOH A . 
F 6 HOH 69  469 69  HOH HOH A . 
F 6 HOH 70  470 70  HOH HOH A . 
F 6 HOH 71  471 71  HOH HOH A . 
F 6 HOH 72  472 72  HOH HOH A . 
F 6 HOH 73  473 73  HOH HOH A . 
F 6 HOH 74  474 74  HOH HOH A . 
F 6 HOH 75  475 75  HOH HOH A . 
F 6 HOH 76  476 76  HOH HOH A . 
F 6 HOH 77  477 77  HOH HOH A . 
F 6 HOH 78  478 78  HOH HOH A . 
F 6 HOH 79  479 79  HOH HOH A . 
F 6 HOH 80  480 80  HOH HOH A . 
F 6 HOH 81  481 81  HOH HOH A . 
F 6 HOH 82  482 82  HOH HOH A . 
F 6 HOH 83  483 83  HOH HOH A . 
F 6 HOH 84  484 84  HOH HOH A . 
F 6 HOH 85  485 85  HOH HOH A . 
F 6 HOH 86  486 86  HOH HOH A . 
F 6 HOH 87  487 87  HOH HOH A . 
F 6 HOH 88  488 88  HOH HOH A . 
F 6 HOH 89  489 89  HOH HOH A . 
F 6 HOH 90  490 90  HOH HOH A . 
F 6 HOH 91  491 91  HOH HOH A . 
F 6 HOH 92  492 92  HOH HOH A . 
F 6 HOH 93  493 93  HOH HOH A . 
F 6 HOH 94  494 94  HOH HOH A . 
F 6 HOH 95  495 95  HOH HOH A . 
F 6 HOH 96  496 96  HOH HOH A . 
F 6 HOH 97  497 97  HOH HOH A . 
F 6 HOH 98  498 98  HOH HOH A . 
F 6 HOH 99  499 99  HOH HOH A . 
F 6 HOH 100 500 100 HOH HOH A . 
F 6 HOH 101 501 101 HOH HOH A . 
F 6 HOH 102 502 102 HOH HOH A . 
F 6 HOH 103 503 103 HOH HOH A . 
F 6 HOH 104 504 104 HOH HOH A . 
F 6 HOH 105 505 105 HOH HOH A . 
F 6 HOH 106 506 106 HOH HOH A . 
F 6 HOH 107 507 107 HOH HOH A . 
F 6 HOH 108 508 108 HOH HOH A . 
F 6 HOH 109 509 109 HOH HOH A . 
F 6 HOH 110 510 110 HOH HOH A . 
F 6 HOH 111 511 111 HOH HOH A . 
F 6 HOH 112 512 112 HOH HOH A . 
F 6 HOH 113 513 113 HOH HOH A . 
F 6 HOH 114 514 114 HOH HOH A . 
F 6 HOH 115 515 115 HOH HOH A . 
F 6 HOH 116 516 116 HOH HOH A . 
F 6 HOH 117 517 117 HOH HOH A . 
F 6 HOH 118 518 118 HOH HOH A . 
F 6 HOH 119 519 119 HOH HOH A . 
F 6 HOH 120 520 120 HOH HOH A . 
F 6 HOH 121 521 121 HOH HOH A . 
F 6 HOH 122 522 122 HOH HOH A . 
F 6 HOH 123 523 123 HOH HOH A . 
F 6 HOH 124 524 124 HOH HOH A . 
F 6 HOH 125 525 125 HOH HOH A . 
F 6 HOH 126 526 126 HOH HOH A . 
F 6 HOH 127 527 127 HOH HOH A . 
F 6 HOH 128 528 128 HOH HOH A . 
F 6 HOH 129 529 129 HOH HOH A . 
F 6 HOH 130 530 130 HOH HOH A . 
F 6 HOH 131 531 131 HOH HOH A . 
F 6 HOH 132 532 132 HOH HOH A . 
F 6 HOH 133 533 133 HOH HOH A . 
F 6 HOH 134 534 134 HOH HOH A . 
F 6 HOH 135 535 135 HOH HOH A . 
F 6 HOH 136 536 136 HOH HOH A . 
F 6 HOH 137 537 137 HOH HOH A . 
F 6 HOH 138 538 138 HOH HOH A . 
F 6 HOH 139 539 139 HOH HOH A . 
F 6 HOH 140 540 140 HOH HOH A . 
F 6 HOH 141 541 141 HOH HOH A . 
F 6 HOH 142 542 142 HOH HOH A . 
F 6 HOH 143 543 143 HOH HOH A . 
F 6 HOH 144 544 144 HOH HOH A . 
F 6 HOH 145 545 145 HOH HOH A . 
F 6 HOH 146 546 146 HOH HOH A . 
F 6 HOH 147 547 147 HOH HOH A . 
F 6 HOH 148 548 148 HOH HOH A . 
F 6 HOH 149 549 149 HOH HOH A . 
F 6 HOH 150 550 150 HOH HOH A . 
F 6 HOH 151 551 151 HOH HOH A . 
F 6 HOH 152 552 152 HOH HOH A . 
F 6 HOH 153 553 153 HOH HOH A . 
F 6 HOH 154 554 154 HOH HOH A . 
F 6 HOH 155 555 155 HOH HOH A . 
F 6 HOH 156 556 156 HOH HOH A . 
F 6 HOH 157 557 157 HOH HOH A . 
F 6 HOH 158 558 158 HOH HOH A . 
F 6 HOH 159 559 159 HOH HOH A . 
F 6 HOH 160 560 160 HOH HOH A . 
F 6 HOH 161 561 161 HOH HOH A . 
F 6 HOH 162 562 162 HOH HOH A . 
F 6 HOH 163 563 163 HOH HOH A . 
F 6 HOH 164 564 164 HOH HOH A . 
F 6 HOH 165 565 165 HOH HOH A . 
F 6 HOH 166 566 166 HOH HOH A . 
F 6 HOH 167 567 167 HOH HOH A . 
F 6 HOH 168 568 168 HOH HOH A . 
F 6 HOH 169 569 169 HOH HOH A . 
F 6 HOH 170 570 170 HOH HOH A . 
F 6 HOH 171 571 171 HOH HOH A . 
F 6 HOH 172 572 172 HOH HOH A . 
F 6 HOH 173 573 173 HOH HOH A . 
F 6 HOH 174 574 174 HOH HOH A . 
F 6 HOH 175 575 175 HOH HOH A . 
F 6 HOH 176 576 176 HOH HOH A . 
F 6 HOH 177 577 177 HOH HOH A . 
F 6 HOH 178 578 178 HOH HOH A . 
F 6 HOH 179 579 179 HOH HOH A . 
F 6 HOH 180 580 180 HOH HOH A . 
F 6 HOH 181 581 181 HOH HOH A . 
F 6 HOH 182 582 182 HOH HOH A . 
F 6 HOH 183 583 183 HOH HOH A . 
F 6 HOH 184 584 184 HOH HOH A . 
F 6 HOH 185 585 185 HOH HOH A . 
F 6 HOH 186 586 186 HOH HOH A . 
F 6 HOH 187 587 187 HOH HOH A . 
F 6 HOH 188 588 188 HOH HOH A . 
F 6 HOH 189 589 189 HOH HOH A . 
F 6 HOH 190 590 190 HOH HOH A . 
F 6 HOH 191 591 191 HOH HOH A . 
F 6 HOH 192 592 192 HOH HOH A . 
F 6 HOH 193 593 193 HOH HOH A . 
F 6 HOH 194 594 194 HOH HOH A . 
F 6 HOH 195 595 195 HOH HOH A . 
F 6 HOH 196 596 196 HOH HOH A . 
F 6 HOH 197 597 197 HOH HOH A . 
F 6 HOH 198 598 198 HOH HOH A . 
F 6 HOH 199 599 199 HOH HOH A . 
F 6 HOH 200 600 200 HOH HOH A . 
F 6 HOH 201 601 201 HOH HOH A . 
F 6 HOH 202 602 202 HOH HOH A . 
F 6 HOH 203 603 203 HOH HOH A . 
F 6 HOH 204 604 204 HOH HOH A . 
F 6 HOH 205 605 205 HOH HOH A . 
F 6 HOH 206 606 206 HOH HOH A . 
F 6 HOH 207 607 207 HOH HOH A . 
F 6 HOH 208 608 208 HOH HOH A . 
F 6 HOH 209 609 209 HOH HOH A . 
F 6 HOH 210 610 210 HOH HOH A . 
F 6 HOH 211 611 211 HOH HOH A . 
F 6 HOH 212 612 212 HOH HOH A . 
F 6 HOH 213 613 213 HOH HOH A . 
F 6 HOH 214 614 214 HOH HOH A . 
F 6 HOH 215 615 215 HOH HOH A . 
F 6 HOH 216 616 216 HOH HOH A . 
F 6 HOH 217 617 217 HOH HOH A . 
F 6 HOH 218 618 218 HOH HOH A . 
F 6 HOH 219 619 219 HOH HOH A . 
F 6 HOH 220 620 220 HOH HOH A . 
F 6 HOH 221 621 221 HOH HOH A . 
F 6 HOH 222 622 222 HOH HOH A . 
F 6 HOH 223 623 223 HOH HOH A . 
F 6 HOH 224 624 224 HOH HOH A . 
F 6 HOH 225 625 225 HOH HOH A . 
F 6 HOH 226 626 226 HOH HOH A . 
F 6 HOH 227 627 227 HOH HOH A . 
F 6 HOH 228 628 228 HOH HOH A . 
F 6 HOH 229 629 229 HOH HOH A . 
F 6 HOH 230 630 230 HOH HOH A . 
F 6 HOH 231 631 231 HOH HOH A . 
F 6 HOH 232 632 232 HOH HOH A . 
F 6 HOH 233 633 233 HOH HOH A . 
F 6 HOH 234 634 234 HOH HOH A . 
F 6 HOH 235 635 235 HOH HOH A . 
F 6 HOH 236 636 236 HOH HOH A . 
F 6 HOH 237 637 237 HOH HOH A . 
F 6 HOH 238 638 238 HOH HOH A . 
F 6 HOH 239 639 239 HOH HOH A . 
F 6 HOH 240 640 240 HOH HOH A . 
F 6 HOH 241 641 241 HOH HOH A . 
F 6 HOH 242 642 242 HOH HOH A . 
F 6 HOH 243 643 243 HOH HOH A . 
F 6 HOH 244 644 244 HOH HOH A . 
F 6 HOH 245 645 245 HOH HOH A . 
F 6 HOH 246 646 246 HOH HOH A . 
F 6 HOH 247 647 247 HOH HOH A . 
F 6 HOH 248 648 248 HOH HOH A . 
F 6 HOH 249 649 249 HOH HOH A . 
F 6 HOH 250 650 250 HOH HOH A . 
F 6 HOH 251 651 251 HOH HOH A . 
F 6 HOH 252 652 252 HOH HOH A . 
F 6 HOH 253 653 253 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     524 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 98  ? A HIS 98  ? 1_555 105.5 ? 
2  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 121 ? A HIS 121 ? 1_555 116.6 ? 
3  NE2 ? A HIS 98  ? A HIS 98  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 121 ? A HIS 121 ? 1_555 99.0  ? 
4  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? E WWO .   ? A WWO 304 ? 1_555 112.7 ? 
5  NE2 ? A HIS 98  ? A HIS 98  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? E WWO .   ? A WWO 304 ? 1_555 103.7 ? 
6  ND1 ? A HIS 121 ? A HIS 121 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? E WWO .   ? A WWO 304 ? 1_555 116.6 ? 
7  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  ? E WWO .   ? A WWO 304 ? 1_555 86.1  ? 
8  NE2 ? A HIS 98  ? A HIS 98  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  ? E WWO .   ? A WWO 304 ? 1_555 130.7 ? 
9  ND1 ? A HIS 121 ? A HIS 121 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  ? E WWO .   ? A WWO 304 ? 1_555 118.6 ? 
10 N10 ? E WWO .   ? A WWO 304 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S7  ? E WWO .   ? A WWO 304 ? 1_555 32.3  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-04-15 
2 'Structure model' 1 1 2017-10-04 
3 'Structure model' 1 2 2023-11-08 
# 
_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' 'Refinement description' 
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Database references'    
5 3 'Structure model' 'Derived calculations'   
6 3 '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' diffrn_detector               
2  2 'Structure model' software                      
3  3 'Structure model' chem_comp_atom                
4  3 'Structure model' chem_comp_bond                
5  3 'Structure model' database_2                    
6  3 'Structure model' diffrn_source                 
7  3 'Structure model' pdbx_initial_refinement_model 
8  3 'Structure model' pdbx_struct_conn_angle        
9  3 'Structure model' struct_conn                   
10 3 'Structure model' struct_ref_seq_dif            
11 3 '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' '_diffrn_detector.detector'                   
2  2 'Structure model' '_software.version'                           
3  3 'Structure model' '_database_2.pdbx_DOI'                        
4  3 'Structure model' '_database_2.pdbx_database_accession'         
5  3 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
17 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
18 3 'Structure model' '_pdbx_struct_conn_angle.value'               
19 3 'Structure model' '_struct_conn.pdbx_dist_value'                
20 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
21 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
22 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
23 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
24 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
25 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
26 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
27 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
28 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
29 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
30 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
31 3 'Structure model' '_struct_ref_seq_dif.details'                 
32 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
33 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
34 3 '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      5.6.0117 ?               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       3.3.20   2011/05/18      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 
MAR345dtb   .        ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .        ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 67  ? ? -174.10 -179.57 
2 1 ASN A 77  ? ? -94.88  41.92   
3 1 HIS A 105 ? ? -151.56 68.06   
4 1 ASN A 246 ? ? -150.12 35.48   
# 
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 MET 2 ? A MET 2 
3 1 Y 1 A SER 3 ? A SER 3 
4 1 Y 1 A ARG 4 ? A ARG 4 
5 1 Y 1 A LEU 5 ? A LEU 5 
# 
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 
VAL N    N  N N 399 
VAL CA   C  N S 400 
VAL C    C  N N 401 
VAL O    O  N N 402 
VAL CB   C  N N 403 
VAL CG1  C  N N 404 
VAL CG2  C  N N 405 
VAL OXT  O  N N 406 
VAL H    H  N N 407 
VAL H2   H  N N 408 
VAL HA   H  N N 409 
VAL HB   H  N N 410 
VAL HG11 H  N N 411 
VAL HG12 H  N N 412 
VAL HG13 H  N N 413 
VAL HG21 H  N N 414 
VAL HG22 H  N N 415 
VAL HG23 H  N N 416 
VAL HXT  H  N N 417 
WWO F27  F  N N 418 
WWO C5   C  Y N 419 
WWO C4   C  Y N 420 
WWO S7   S  N N 421 
WWO O9   O  N N 422 
WWO N10  N  N N 423 
WWO O8   O  N N 424 
WWO C3   C  Y N 425 
WWO F12  F  N N 426 
WWO C2   C  Y N 427 
WWO F13  F  N N 428 
WWO C6   C  Y N 429 
WWO C1   C  Y N 430 
WWO S11  S  N N 431 
WWO O22  O  N N 432 
WWO O23  O  N N 433 
WWO C21  C  N N 434 
WWO C24  C  N N 435 
WWO O25  O  N N 436 
WWO N26  N  N N 437 
WWO C14  C  N N 438 
WWO C15  C  Y N 439 
WWO C20  C  Y N 440 
WWO C19  C  Y N 441 
WWO C18  C  Y N 442 
WWO C17  C  Y N 443 
WWO C16  C  Y N 444 
WWO H1   H  N N 445 
WWO H2   H  N N 446 
WWO H3   H  N N 447 
WWO H4   H  N N 448 
WWO H5   H  N N 449 
WWO H6   H  N N 450 
WWO H7   H  N N 451 
WWO H8   H  N N 452 
WWO H9   H  N N 453 
WWO H10  H  N N 454 
WWO H11  H  N N 455 
WWO H12  H  N N 456 
WWO H13  H  N N 457 
WWO H14  H  N N 458 
WWO H15  H  N N 459 
ZN  ZN   ZN N N 460 
# 
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 
VAL N   CA   sing N N 383 
VAL N   H    sing N N 384 
VAL N   H2   sing N N 385 
VAL CA  C    sing N N 386 
VAL CA  CB   sing N N 387 
VAL CA  HA   sing N N 388 
VAL C   O    doub N N 389 
VAL C   OXT  sing N N 390 
VAL CB  CG1  sing N N 391 
VAL CB  CG2  sing N N 392 
VAL CB  HB   sing N N 393 
VAL CG1 HG11 sing N N 394 
VAL CG1 HG12 sing N N 395 
VAL CG1 HG13 sing N N 396 
VAL CG2 HG21 sing N N 397 
VAL CG2 HG22 sing N N 398 
VAL CG2 HG23 sing N N 399 
VAL OXT HXT  sing N N 400 
WWO O9  S7   doub N N 401 
WWO S7  N10  sing N N 402 
WWO S7  C4   sing N N 403 
WWO S7  O8   doub N N 404 
WWO C16 C17  doub Y N 405 
WWO C16 C15  sing Y N 406 
WWO F27 C5   sing N N 407 
WWO C17 C18  sing Y N 408 
WWO C14 C15  sing N N 409 
WWO C14 N26  sing N N 410 
WWO C4  C5   doub Y N 411 
WWO C4  C3   sing Y N 412 
WWO C5  C6   sing Y N 413 
WWO C15 C20  doub Y N 414 
WWO C3  F12  sing N N 415 
WWO C3  C2   doub Y N 416 
WWO C6  N26  sing N N 417 
WWO C6  C1   doub Y N 418 
WWO O23 S11  doub N N 419 
WWO C18 C19  doub Y N 420 
WWO C2  C1   sing Y N 421 
WWO C2  F13  sing N N 422 
WWO C1  S11  sing N N 423 
WWO O22 S11  doub N N 424 
WWO C20 C19  sing Y N 425 
WWO S11 C21  sing N N 426 
WWO C21 C24  sing N N 427 
WWO O25 C24  sing N N 428 
WWO N10 H1   sing N N 429 
WWO N10 H2   sing N N 430 
WWO C21 H3   sing N N 431 
WWO C21 H4   sing N N 432 
WWO C24 H5   sing N N 433 
WWO C24 H6   sing N N 434 
WWO O25 H7   sing N N 435 
WWO N26 H8   sing N N 436 
WWO C14 H9   sing N N 437 
WWO C14 H10  sing N N 438 
WWO C20 H11  sing N N 439 
WWO C19 H12  sing N N 440 
WWO C18 H13  sing N N 441 
WWO C17 H14  sing N N 442 
WWO C16 H15  sing N N 443 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                       ZN  
3 'DI(HYDROXYETHYL)ETHER'                                                          PEG 
4 1,2-ETHANEDIOL                                                                   EDO 
5 '3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' WWO 
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   2NNO 
_pdbx_initial_refinement_model.details          ? 
# 
