data_4PYX
# 
_entry.id   4PYX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4PYX         pdb_00004pyx 10.2210/pdb4pyx/pdb 
RCSB  RCSB085393   ?            ?                   
WWPDB D_1000085393 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4PYY . unspecified 
PDB 4PZH . unspecified 
PDB 4Q06 . unspecified 
PDB 4Q07 . unspecified 
PDB 4Q08 . unspecified 
PDB 4Q09 . unspecified 
PDB 4Q0L . unspecified 
# 
_pdbx_database_status.entry_id                        4PYX 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2014-03-28 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     'Discovery and characterization of novel selective inhibitors of carbonic anhydrase IX.' 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_volume            57 
_citation.page_first                9435 
_citation.page_last                 9446 
_citation.year                      2014 
_citation.journal_id_ASTM           JMCMAR 
_citation.country                   US 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_id_CSD            0151 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25358084 
_citation.pdbx_database_id_DOI      10.1021/jm501003k 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dudutiene, V.'      1  ? 
primary 'Matuliene, J.'      2  ? 
primary 'Smirnov, A.'        3  ? 
primary 'Timm, D.D.'         4  ? 
primary 'Zubriene, A.'       5  ? 
primary 'Baranauskiene, L.'  6  ? 
primary 'Morkunaite, V.'     7  ? 
primary 'Smirnoviene, J.'    8  ? 
primary 'Michailoviene, V.'  9  ? 
primary 'Juozapaitiene, V.'  10 ? 
primary 'Mickeviciute, A.'   11 ? 
primary 'Kazokaite, J.'      12 ? 
primary 'Baksyte, S.'        13 ? 
primary 'Kasiliauskaite, A.' 14 ? 
primary 'Jachno, J.'         15 ? 
primary 'Revuckiene, J.'     16 ? 
primary 'Kisonaite, M.'      17 ? 
primary 'Pilipuityte, V.'    18 ? 
primary 'Ivanauskaite, E.'   19 ? 
primary 'Milinaviciute, G.'  20 ? 
primary 'Smirnovas, V.'      21 ? 
primary 'Petrikaite, V.'     22 ? 
primary 'Kairys, V.'         23 ? 
primary 'Petrauskas, V.'     24 ? 
primary 'Norvaisas, P.'      25 ? 
primary 'Linge, D.'          26 ? 
primary 'Gibieza, P.'        27 ? 
primary 'Capkauskaite, E.'   28 ? 
primary 'Zaksauskas, A.'     29 ? 
primary 'Kazlauskas, E.'     30 ? 
primary 'Manakova, E.'       31 ? 
primary 'Grazulis, S.'       32 ? 
primary 'Ladbury, J.E.'      33 ? 
primary 'Matulis, D.'        34 ? 
# 
_cell.entry_id           4PYX 
_cell.length_a           42.022 
_cell.length_b           41.143 
_cell.length_c           71.519 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.070 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              2 
_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                         4PYX 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_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 2'                                                               29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                           65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                 78.133    1   ?       ? ? ? 
4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                               195.237   1   ?       ? ? ? 
5 non-polymer syn '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 412.491   1   ?       ? ? ? 
6 water       nat water                                                                                18.015    168 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_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   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS 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                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               '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                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_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              4PYX 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
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 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                                 ? 'C2 H6 O S' 
78.133  
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 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                               ? 'C6 H13 N O4 S' 
195.237 
MET 'L-peptide linking' y METHIONINE                                                                           ? 'C5 H11 N O2 S' 
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                        ? 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                              ? 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                               ? 'C3 H7 N O3' 
105.093 
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 
V90 non-polymer         . '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' ? 
'C16 H23 F3 N2 O3 S2' 412.491 
VAL 'L-peptide linking' y VALINE                                                                               ? 'C5 H11 N O2' 
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                           ? 'Zn 2' 65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4PYX 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   38.0 
_exptl_crystal.density_Matthews      2.00 
_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              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate, VAPOR DIFFUSION, SITTING DROP, temperature 291K
;
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS IV++' 
_diffrn_detector.pdbx_collection_date   2012-10-30 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'VARIMAX-HF MIRROR' 
_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   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
# 
_reflns.entry_id                     4PYX 
_reflns.d_resolution_high            1.800 
_reflns.d_resolution_low             25.222 
_reflns.number_all                   ? 
_reflns.number_obs                   21036 
_reflns.pdbx_Rmerge_I_obs            0.127 
_reflns.pdbx_netI_over_sigmaI        9.900 
_reflns.pdbx_Rsym_value              0.127 
_reflns.pdbx_redundancy              3.700 
_reflns.percent_possible_obs         95.100 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        18.529 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.80 1.90  ? 10783 ? 0.422 1.3 0.422 ? 3.70 ? 2943 92.00 1  1 
1.90 2.01  ? 10458 ? 0.333 1.6 0.333 ? 3.70 ? 2832 93.10 2  1 
2.01 2.15  ? 9816  ? 0.269 2.0 0.269 ? 3.70 ? 2663 94.30 3  1 
2.15 2.32  ? 9358  ? 0.215 2.6 0.215 ? 3.70 ? 2528 94.60 4  1 
2.32 2.55  ? 8743  ? 0.173 3.2 0.173 ? 3.70 ? 2367 96.30 5  1 
2.55 2.85  ? 7899  ? 0.130 4.4 0.130 ? 3.70 ? 2128 96.00 6  1 
2.85 3.29  ? 7034  ? 0.102 5.4 0.102 ? 3.70 ? 1907 97.30 7  1 
3.29 4.03  ? 6056  ? 0.082 6.7 0.082 ? 3.70 ? 1656 98.10 8  1 
4.03 5.69  ? 4633  ? 0.075 6.9 0.075 ? 3.60 ? 1282 98.40 9  1 
5.69 25.22 ? 2488  ? 0.084 5.6 0.084 ? 3.40 ? 730  97.40 10 1 
# 
_refine.entry_id                                 4PYX 
_refine.ls_d_res_high                            1.800 
_refine.ls_d_res_low                             25.220 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    94.570 
_refine.ls_number_reflns_obs                     21026 
_refine.ls_number_reflns_all                     21026 
_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      : REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          0.183 
_refine.ls_R_factor_obs                          0.183 
_refine.ls_R_factor_R_work                       0.178 
_refine.ls_wR_factor_R_work                      0.175 
_refine.ls_R_factor_R_free                       0.230 
_refine.ls_wR_factor_R_free                      0.227 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  2095 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.991 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.300 
_refine.aniso_B[2][2]                            -1.200 
_refine.aniso_B[3][3]                            0.810 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.160 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.923 
_refine.overall_SU_R_Cruickshank_DPI             0.163 
_refine.overall_SU_R_free                        0.152 
_refine.pdbx_overall_ESU_R                       0.163 
_refine.pdbx_overall_ESU_R_Free                  0.152 
_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          MR 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.851 
_refine.B_iso_max                                71.52 
_refine.B_iso_min                                7.02 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3HLJ' 
_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        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.number_atoms_solvent             168 
_refine_hist.number_atoms_total               2255 
_refine_hist.d_res_high                       1.800 
_refine_hist.d_res_low                        25.220 
# 
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       2178 0.020  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    2957 2.137  1.967  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 262  7.295  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 99   37.598 24.747 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 359  15.701 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 7    14.848 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         307  0.145  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1667 0.013  0.021  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               90.810 
_refine_ls_shell.number_reflns_R_work             1303 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.334 
_refine_ls_shell.R_factor_R_free                  0.344 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             149 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1452 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4PYX 
_struct.title                     'Crystal structure of human carbonic anhydrase isozyme II with inhibitor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4PYX 
_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 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 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 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.998 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E V90 . N11 ? ? A ZN  301 A V90 304 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
# 
_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 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 0.83  
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 13.25 
# 
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  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
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 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N LYS A 148 ? N LYS A 149 O VAL A 217 ? O VAL 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 DMS 302 ? 5  'BINDING SITE FOR RESIDUE DMS A 302' 
AC3 Software A MES 303 ? 5  'BINDING SITE FOR RESIDUE MES A 303' 
AC4 Software A V90 304 ? 19 'BINDING SITE FOR RESIDUE V90 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 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  V90 E .   ? V90 A 304 . ? 1_555 ? 
5  AC2 5  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 5  PRO A 13  ? PRO A 13  . ? 1_555 ? 
7  AC2 5  ASP A 242 ? ASP A 243 . ? 1_555 ? 
8  AC2 5  TRP A 244 ? TRP A 245 . ? 1_555 ? 
9  AC2 5  HOH F .   ? HOH A 545 . ? 1_555 ? 
10 AC3 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
11 AC3 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
12 AC3 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
13 AC3 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
14 AC3 5  HOH F .   ? HOH A 534 . ? 1_555 ? 
15 AC4 19 TYR A 7   ? TYR A 7   . ? 1_555 ? 
16 AC4 19 ASN A 62  ? ASN A 62  . ? 1_555 ? 
17 AC4 19 HIS A 64  ? HIS A 64  . ? 1_555 ? 
18 AC4 19 ALA A 65  ? ALA A 65  . ? 1_555 ? 
19 AC4 19 ASN A 67  ? ASN A 67  . ? 1_555 ? 
20 AC4 19 GLN A 92  ? GLN A 92  . ? 1_555 ? 
21 AC4 19 HIS A 94  ? HIS A 94  . ? 1_555 ? 
22 AC4 19 HIS A 96  ? HIS A 96  . ? 1_555 ? 
23 AC4 19 HIS A 119 ? HIS A 119 . ? 1_555 ? 
24 AC4 19 VAL A 121 ? VAL A 121 . ? 1_555 ? 
25 AC4 19 PHE A 130 ? PHE A 131 . ? 1_555 ? 
26 AC4 19 LEU A 140 ? LEU A 141 . ? 1_555 ? 
27 AC4 19 VAL A 142 ? VAL A 143 . ? 1_555 ? 
28 AC4 19 LEU A 197 ? LEU A 198 . ? 1_555 ? 
29 AC4 19 THR A 198 ? THR A 199 . ? 1_555 ? 
30 AC4 19 THR A 199 ? THR A 200 . ? 1_555 ? 
31 AC4 19 TRP A 208 ? TRP A 209 . ? 1_555 ? 
32 AC4 19 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
33 AC4 19 HOH F .   ? HOH A 518 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4PYX 
_atom_sites.fract_transf_matrix[1][1]   0.023797 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005965 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024306 
_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]   0.014415 
_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   . HIS A 1 4   ? 9.649   1.394   8.377   1.00  35.89 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.350  0.091   8.591   1.00  35.19 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.515   -0.894  9.392   1.00  31.94 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.569   -2.081  9.094   1.00  34.82 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 11.707  0.298   9.283   1.00  44.46 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 12.694  -0.818  9.036   1.00  47.80 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 13.222  -1.062  7.823   1.00  48.91 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 13.242  -1.764  9.901   1.00  55.10 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 14.065  -2.109  7.903   1.00  56.04 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 14.076  -2.538  9.176   1.00  56.07 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.753   -0.452  10.397  1.00  26.96 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.979   -1.407  11.269  1.00  20.99 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.970   -2.186  10.498  1.00  18.15 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.462   -1.762  9.436   1.00  15.40 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.355   -0.728  12.506  1.00  19.72 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 6.168   0.130   12.163  1.00  18.72 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 6.152   1.507   11.843  1.00  18.58 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.784   -0.323  12.015  1.00  17.10 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.887   1.915   11.509  1.00  17.88 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 4.006   0.860   11.620  1.00  16.91 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 4.129   -1.555  12.181  1.00  16.46 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.658   0.804   11.405  1.00  17.23 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.738   -1.578  11.972  1.00  17.50 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 2.023   -0.416  11.617  1.00  16.66 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.639   -3.372  11.008  1.00  18.22 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.684   -4.185  10.273  1.00  17.05 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.263   -5.302  11.168  1.00  16.96 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.281   -5.174  12.384  1.00  15.81 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 4.889   -6.415  10.547  1.00  18.74 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.456   -7.572  11.340  1.00  19.34 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.311   -8.833  11.186  1.00  23.92 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 4.970   -9.890  11.784  1.00  25.80 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.002   -7.859  11.031  1.00  16.14 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.056   -6.815  11.612  1.00  15.17 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.683   -6.848  12.971  1.00  14.81 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.518   -5.831  10.787  1.00  14.88 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 0.798   -5.895  13.489  1.00  14.50 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.620   -4.901  11.273  1.00  14.66 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.261   -4.956  12.637  1.00  14.37 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.675  -4.031  13.051  1.00  14.77 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.405   -8.761  10.423  1.00  27.76 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.312   -9.950  10.276  1.00  26.33 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.317   -10.297 11.374  1.00  28.38 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.447   -9.598  12.410  1.00  29.37 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.115   -11.353 11.140  1.00  31.98 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.145  -11.774 12.149  1.00  33.93 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.161  -10.682 12.452  1.00  32.91 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.666  -10.555 13.616  1.00  31.85 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 10.887  -13.049 11.730  1.00  42.08 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 11.897  -13.526 12.767  1.00  44.64 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 12.865  -14.568 12.222  1.00  49.51 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 14.087  -14.671 13.142  1.00  55.23 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 15.346  -15.078 12.426  1.00  59.36 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 11.431  -9.861  11.434  1.00  28.16 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 12.481  -8.855  11.573  1.00  24.91 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 12.051  -7.484  11.936  1.00  21.83 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 12.829  -6.730  12.502  1.00  27.13 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 13.378  -8.912  10.339  1.00  23.05 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 14.057  -10.275 10.172  1.00  23.77 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 15.047  -10.701 10.987  1.00  26.60 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 13.799  -11.328 9.292   1.00  26.96 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 15.422  -11.948 10.629  1.00  27.09 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 14.659  -12.330 9.594   1.00  24.03 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 10.807  -7.142  11.635  1.00  23.53 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 10.278  -5.802  11.949  1.00  22.17 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 8.952   -5.822  12.777  1.00  22.18 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 8.312   -4.790  12.925  1.00  22.52 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 10.111  -5.042  10.619  1.00  20.27 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 8.990   -5.616  9.777   1.00  22.04 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 8.423   -6.654  10.121  1.00  22.39 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 8.698   -4.997  8.650   1.00  20.80 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 8.558   -6.996  13.308  1.00  21.52 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 7.207   -7.233  13.888  1.00  17.99 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 7.088   -6.671  15.294  1.00  17.47 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 7.956   -5.938  15.713  1.00  15.85 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 6.034   -7.034  16.061  1.00  17.91 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 5.848   -6.348  17.350  1.00  18.44 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 6.995   -6.331  18.361  1.00  18.15 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 7.163   -5.354  19.101  1.00  17.97 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 4.635   -7.099  17.951  1.00  19.64 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 3.825   -7.459  16.753  1.00  19.08 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 4.767   -7.623  15.599  1.00  19.30 ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 7.814   -7.381  18.407  1.00  17.53 ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 8.849   -7.472  19.397  1.00  17.71 ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 10.029  -6.477  19.116  1.00  16.49 ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 10.855  -6.223  19.973  1.00  18.44 ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 9.313   -8.924  19.399  1.00  21.72 ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 9.970   -9.366  18.048  1.00  24.90 ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 9.080   -9.965  16.909  1.00  29.23 ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 7.860   -9.642  16.789  1.00  24.27 ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 9.653   -10.748 16.072  1.00  25.35 ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 10.060  -5.934  17.916  1.00  14.99 ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 11.001  -4.936  17.505  1.00  15.76 ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 10.550  -3.510  17.679  1.00  18.16 ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 11.371  -2.610  17.597  1.00  16.72 ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 11.300  -5.147  16.038  1.00  17.71 ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 12.028  -6.443  15.785  1.00  21.17 ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 13.361  -6.575  15.945  1.00  19.82 ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 11.552  -7.704  15.385  1.00  20.54 ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 13.718  -7.857  15.654  1.00  20.68 ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 12.620  -8.545  15.355  1.00  19.81 ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 9.267   -3.272  17.914  1.00  15.65 ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 8.791   -1.875  17.794  1.00  16.57 ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 9.397   -0.935  18.795  1.00  16.02 ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 9.514   0.301   18.522  1.00  16.28 ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 7.286   -1.804  17.902  1.00  13.40 ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 6.554   -2.492  16.781  1.00  15.05 ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 7.058   -2.939  15.557  1.00  15.13 ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 5.107   -2.764  16.704  1.00  13.97 ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 6.088   -3.530  14.828  1.00  15.15 ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 4.884   -3.408  15.416  1.00  15.22 ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 4.052   -2.617  17.572  1.00  13.90 ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 3.610   -3.860  15.015  1.00  15.40 ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 2.764   -3.036  17.158  1.00  13.05 ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 2.546   -3.653  15.916  1.00  14.89 ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 9.737   -1.469  19.951  1.00  16.23 ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 10.267  -0.629  21.013  1.00  17.93 ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 11.518  0.166   20.618  1.00  18.26 ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 11.706  1.220   21.162  1.00  16.56 ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 10.527  -1.414  22.287  1.00  17.54 ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 11.741  -2.303  22.164  1.00  19.68 ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 12.959  -1.931  22.623  1.00  22.16 ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 11.906  -3.518  21.539  1.00  18.25 ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 13.851  -2.890  22.352  1.00  20.24 ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 13.218  -3.862  21.672  1.00  17.77 ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 18  ? 12.334  -0.339  19.692  1.00  17.57 ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 18  ? 13.565  0.335   19.237  1.00  21.69 ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 18  ? 13.271  1.671   18.545  1.00  23.27 ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 18  ? 13.880  2.651   18.863  1.00  26.75 ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 18  ? 14.333  -0.598  18.300  1.00  20.82 ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 18  ? 14.938  -1.829  19.010  1.00  21.35 ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 18  ? 15.551  -2.755  18.003  1.00  19.14 ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 18  ? 14.572  -3.751  17.431  1.00  20.80 ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 18  ? 15.261  -4.510  16.334  1.00  18.19 ? 18  LYS A NZ  1 
ATOM   135  N  N   . ASP A 1 19  ? 12.280  1.735   17.666  1.00  22.81 ? 19  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 19  ? 11.843  3.037   17.153  1.00  26.42 ? 19  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 19  ? 10.851  3.769   18.038  1.00  25.65 ? 19  ASP A C   1 
ATOM   138  O  O   . ASP A 1 19  ? 10.698  4.990   17.894  1.00  22.45 ? 19  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 19  ? 11.286  2.901   15.732  1.00  29.04 ? 19  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 19  ? 12.373  2.714   14.729  1.00  36.80 ? 19  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 19  ? 13.303  3.523   14.724  1.00  36.03 ? 19  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 19  ? 12.341  1.720   13.982  1.00  45.42 ? 19  ASP A OD2 1 
ATOM   143  N  N   . PHE A 1 20  ? 10.182  3.034   18.946  1.00  20.44 ? 20  PHE A N   1 
ATOM   144  C  CA  . PHE A 1 20  ? 9.022   3.583   19.661  1.00  21.08 ? 20  PHE A CA  1 
ATOM   145  C  C   . PHE A 1 20  ? 9.043   3.106   21.087  1.00  20.99 ? 20  PHE A C   1 
ATOM   146  O  O   . PHE A 1 20  ? 8.348   2.136   21.449  1.00  18.42 ? 20  PHE A O   1 
ATOM   147  C  CB  . PHE A 1 20  ? 7.720   3.178   18.934  1.00  20.51 ? 20  PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 20  ? 7.641   3.710   17.543  1.00  19.21 ? 20  PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 20  ? 7.202   5.022   17.321  1.00  21.08 ? 20  PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 20  ? 7.988   2.928   16.470  1.00  21.23 ? 20  PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 20  ? 7.132   5.507   16.025  1.00  21.21 ? 20  PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 20  ? 7.969   3.414   15.162  1.00  21.13 ? 20  PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 20  ? 7.528   4.717   14.946  1.00  23.71 ? 20  PHE A CZ  1 
ATOM   154  N  N   . PRO A 1 21  ? 9.865   3.773   21.919  1.00  19.77 ? 21  PRO A N   1 
ATOM   155  C  CA  . PRO A 1 21  ? 10.134  3.301   23.251  1.00  17.81 ? 21  PRO A CA  1 
ATOM   156  C  C   . PRO A 1 21  ? 8.875   3.159   24.129  1.00  16.87 ? 21  PRO A C   1 
ATOM   157  O  O   . PRO A 1 21  ? 8.848   2.374   25.074  1.00  16.13 ? 21  PRO A O   1 
ATOM   158  C  CB  . PRO A 1 21  ? 11.172  4.337   23.796  1.00  20.27 ? 21  PRO A CB  1 
ATOM   159  C  CG  . PRO A 1 21  ? 11.815  4.885   22.575  1.00  21.81 ? 21  PRO A CG  1 
ATOM   160  C  CD  . PRO A 1 21  ? 10.790  4.862   21.501  1.00  21.26 ? 21  PRO A CD  1 
ATOM   161  N  N   A ILE A 1 22  ? 7.824   3.910   23.799  0.50  16.65 ? 22  ILE A N   1 
ATOM   162  N  N   B ILE A 1 22  ? 7.825   3.908   23.787  0.50  16.24 ? 22  ILE A N   1 
ATOM   163  C  CA  A ILE A 1 22  ? 6.553   3.801   24.520  0.50  15.87 ? 22  ILE A CA  1 
ATOM   164  C  CA  B ILE A 1 22  ? 6.541   3.823   24.493  0.50  15.24 ? 22  ILE A CA  1 
ATOM   165  C  C   A ILE A 1 22  ? 5.942   2.381   24.405  0.50  15.10 ? 22  ILE A C   1 
ATOM   166  C  C   B ILE A 1 22  ? 5.907   2.408   24.362  0.50  14.72 ? 22  ILE A C   1 
ATOM   167  O  O   A ILE A 1 22  ? 5.071   1.999   25.210  0.50  14.34 ? 22  ILE A O   1 
ATOM   168  O  O   B ILE A 1 22  ? 4.993   2.052   25.120  0.50  14.15 ? 22  ILE A O   1 
ATOM   169  C  CB  A ILE A 1 22  ? 5.546   4.884   24.063  0.50  15.60 ? 22  ILE A CB  1 
ATOM   170  C  CB  B ILE A 1 22  ? 5.585   4.962   24.028  0.50  14.45 ? 22  ILE A CB  1 
ATOM   171  C  CG1 A ILE A 1 22  ? 4.348   4.902   24.995  0.50  15.95 ? 22  ILE A CG1 1 
ATOM   172  C  CG1 B ILE A 1 22  ? 4.607   5.356   25.123  0.50  14.40 ? 22  ILE A CG1 1 
ATOM   173  C  CG2 A ILE A 1 22  ? 5.091   4.617   22.626  0.50  16.47 ? 22  ILE A CG2 1 
ATOM   174  C  CG2 B ILE A 1 22  ? 4.844   4.567   22.757  0.50  15.27 ? 22  ILE A CG2 1 
ATOM   175  C  CD1 A ILE A 1 22  ? 4.644   5.330   26.413  0.50  15.87 ? 22  ILE A CD1 1 
ATOM   176  C  CD1 B ILE A 1 22  ? 3.642   6.443   24.687  0.50  13.13 ? 22  ILE A CD1 1 
ATOM   177  N  N   . ALA A 1 23  ? 6.463   1.581   23.465  1.00  15.04 ? 23  ALA A N   1 
ATOM   178  C  CA  . ALA A 1 23  ? 6.083   0.130   23.339  1.00  15.75 ? 23  ALA A CA  1 
ATOM   179  C  C   . ALA A 1 23  ? 6.113   -0.611  24.645  1.00  17.54 ? 23  ALA A C   1 
ATOM   180  O  O   . ALA A 1 23  ? 5.422   -1.633  24.789  1.00  16.11 ? 23  ALA A O   1 
ATOM   181  C  CB  . ALA A 1 23  ? 6.941   -0.620  22.306  1.00  16.20 ? 23  ALA A CB  1 
ATOM   182  N  N   . LYS A 1 24  ? 6.975   -0.151  25.566  1.00  17.87 ? 24  LYS A N   1 
ATOM   183  C  CA  . LYS A 1 24  ? 7.179   -0.819  26.846  1.00  18.58 ? 24  LYS A CA  1 
ATOM   184  C  C   . LYS A 1 24  ? 6.548   0.013   27.931  1.00  19.45 ? 24  LYS A C   1 
ATOM   185  O  O   . LYS A 1 24  ? 6.951   -0.122  29.101  1.00  21.94 ? 24  LYS A O   1 
ATOM   186  C  CB  . LYS A 1 24  ? 8.691   -0.966  27.162  1.00  20.35 ? 24  LYS A CB  1 
ATOM   187  C  CG  . LYS A 1 24  ? 9.421   -1.834  26.160  1.00  21.93 ? 24  LYS A CG  1 
ATOM   188  C  CD  . LYS A 1 24  ? 10.882  -2.039  26.521  1.00  24.76 ? 24  LYS A CD  1 
ATOM   189  C  CE  . LYS A 1 24  ? 11.522  -3.056  25.565  1.00  24.22 ? 24  LYS A CE  1 
ATOM   190  N  NZ  . LYS A 1 24  ? 10.876  -4.378  25.814  1.00  25.74 ? 24  LYS A NZ  1 
ATOM   191  N  N   . GLY A 1 25  ? 5.557   0.846   27.561  1.00  18.73 ? 25  GLY A N   1 
ATOM   192  C  CA  . GLY A 1 25  ? 5.046   1.876   28.466  1.00  18.22 ? 25  GLY A CA  1 
ATOM   193  C  C   . GLY A 1 25  ? 4.086   1.344   29.470  1.00  18.09 ? 25  GLY A C   1 
ATOM   194  O  O   . GLY A 1 25  ? 3.878   0.101   29.567  1.00  18.40 ? 25  GLY A O   1 
ATOM   195  N  N   . GLU A 1 26  ? 3.442   2.274   30.166  1.00  16.20 ? 26  GLU A N   1 
ATOM   196  C  CA  . GLU A 1 26  ? 2.574   1.881   31.262  1.00  17.35 ? 26  GLU A CA  1 
ATOM   197  C  C   . GLU A 1 26  ? 1.125   1.610   30.889  1.00  14.79 ? 26  GLU A C   1 
ATOM   198  O  O   . GLU A 1 26  ? 0.441   1.082   31.691  1.00  14.88 ? 26  GLU A O   1 
ATOM   199  C  CB  . GLU A 1 26  ? 2.603   2.884   32.473  1.00  21.28 ? 26  GLU A CB  1 
ATOM   200  C  CG  . GLU A 1 26  ? 3.915   3.033   33.277  1.00  26.37 ? 26  GLU A CG  1 
ATOM   201  C  CD  . GLU A 1 26  ? 4.636   1.701   33.643  1.00  32.89 ? 26  GLU A CD  1 
ATOM   202  O  OE1 . GLU A 1 26  ? 4.114   0.870   34.436  1.00  37.82 ? 26  GLU A OE1 1 
ATOM   203  O  OE2 . GLU A 1 26  ? 5.756   1.467   33.133  1.00  32.71 ? 26  GLU A OE2 1 
ATOM   204  N  N   . ARG A 1 27  ? 0.679   1.897   29.658  1.00  14.42 ? 27  ARG A N   1 
ATOM   205  C  CA  . ARG A 1 27  ? -0.723  1.671   29.295  1.00  12.55 ? 27  ARG A CA  1 
ATOM   206  C  C   . ARG A 1 27  ? -0.780  1.230   27.827  1.00  12.03 ? 27  ARG A C   1 
ATOM   207  O  O   . ARG A 1 27  ? -1.445  1.856   26.994  1.00  11.99 ? 27  ARG A O   1 
ATOM   208  C  CB  . ARG A 1 27  ? -1.589  2.912   29.625  1.00  14.27 ? 27  ARG A CB  1 
ATOM   209  C  CG  . ARG A 1 27  ? -1.343  4.182   28.841  1.00  17.56 ? 27  ARG A CG  1 
ATOM   210  C  CD  . ARG A 1 27  ? -2.344  5.334   29.105  1.00  19.60 ? 27  ARG A CD  1 
ATOM   211  N  NE  . ARG A 1 27  ? -3.609  5.271   28.341  1.00  18.99 ? 27  ARG A NE  1 
ATOM   212  C  CZ  . ARG A 1 27  ? -4.471  6.280   28.190  1.00  20.67 ? 27  ARG A CZ  1 
ATOM   213  N  NH1 . ARG A 1 27  ? -4.256  7.511   28.736  1.00  19.68 ? 27  ARG A NH1 1 
ATOM   214  N  NH2 . ARG A 1 27  ? -5.564  6.062   27.482  1.00  19.97 ? 27  ARG A NH2 1 
ATOM   215  N  N   . GLN A 1 28  ? -0.111  0.108   27.525  1.00  10.37 ? 28  GLN A N   1 
ATOM   216  C  CA  . GLN A 1 28  ? -0.050  -0.393  26.152  1.00  9.61  ? 28  GLN A CA  1 
ATOM   217  C  C   . GLN A 1 28  ? -1.212  -1.363  25.889  1.00  9.67  ? 28  GLN A C   1 
ATOM   218  O  O   . GLN A 1 28  ? -1.735  -2.011  26.799  1.00  9.73  ? 28  GLN A O   1 
ATOM   219  C  CB  . GLN A 1 28  ? 1.276   -1.096  25.933  1.00  10.53 ? 28  GLN A CB  1 
ATOM   220  C  CG  . GLN A 1 28  ? 2.448   -0.090  25.794  1.00  9.72  ? 28  GLN A CG  1 
ATOM   221  C  CD  . GLN A 1 28  ? 2.284   0.769   24.549  1.00  9.75  ? 28  GLN A CD  1 
ATOM   222  O  OE1 . GLN A 1 28  ? 2.520   0.310   23.446  1.00  11.29 ? 28  GLN A OE1 1 
ATOM   223  N  NE2 . GLN A 1 28  ? 1.809   2.014   24.707  1.00  10.32 ? 28  GLN A NE2 1 
ATOM   224  N  N   . SER A 1 29  ? -1.503  -1.518  24.600  1.00  9.45  ? 29  SER A N   1 
ATOM   225  C  CA  . SER A 1 29  ? -2.679  -2.293  24.174  1.00  9.63  ? 29  SER A CA  1 
ATOM   226  C  C   . SER A 1 29  ? -2.158  -3.151  23.055  1.00  8.75  ? 29  SER A C   1 
ATOM   227  O  O   . SER A 1 29  ? -1.204  -2.762  22.379  1.00  9.83  ? 29  SER A O   1 
ATOM   228  C  CB  . SER A 1 29  ? -3.760  -1.397  23.622  1.00  9.48  ? 29  SER A CB  1 
ATOM   229  O  OG  . SER A 1 29  ? -4.453  -0.742  24.699  1.00  10.36 ? 29  SER A OG  1 
ATOM   230  N  N   . PRO A 1 30  ? -2.798  -4.299  22.802  1.00  9.00  ? 30  PRO A N   1 
ATOM   231  C  CA  . PRO A 1 30  ? -3.969  -4.789  23.503  1.00  9.38  ? 30  PRO A CA  1 
ATOM   232  C  C   . PRO A 1 30  ? -3.533  -5.507  24.817  1.00  10.13 ? 30  PRO A C   1 
ATOM   233  O  O   . PRO A 1 30  ? -2.330  -5.582  25.111  1.00  9.85  ? 30  PRO A O   1 
ATOM   234  C  CB  . PRO A 1 30  ? -4.512  -5.855  22.542  1.00  9.02  ? 30  PRO A CB  1 
ATOM   235  C  CG  . PRO A 1 30  ? -3.212  -6.458  22.004  1.00  9.15  ? 30  PRO A CG  1 
ATOM   236  C  CD  . PRO A 1 30  ? -2.327  -5.232  21.751  1.00  9.26  ? 30  PRO A CD  1 
ATOM   237  N  N   . VAL A 1 31  ? -4.539  -6.036  25.533  1.00  10.28 ? 31  VAL A N   1 
ATOM   238  C  CA  . VAL A 1 31  ? -4.338  -6.818  26.708  1.00  10.28 ? 31  VAL A CA  1 
ATOM   239  C  C   . VAL A 1 31  ? -5.166  -8.052  26.684  1.00  10.96 ? 31  VAL A C   1 
ATOM   240  O  O   . VAL A 1 31  ? -6.190  -8.122  25.996  1.00  9.83  ? 31  VAL A O   1 
ATOM   241  C  CB  . VAL A 1 31  ? -4.608  -5.979  27.997  1.00  10.47 ? 31  VAL A CB  1 
ATOM   242  C  CG1 . VAL A 1 31  ? -3.637  -4.781  27.982  1.00  9.00  ? 31  VAL A CG1 1 
ATOM   243  C  CG2 . VAL A 1 31  ? -6.054  -5.494  28.084  1.00  9.75  ? 31  VAL A CG2 1 
ATOM   244  N  N   . ASP A 1 32  ? -4.777  -9.025  27.491  1.00  12.13 ? 32  ASP A N   1 
ATOM   245  C  CA  . ASP A 1 32  ? -5.732  -10.087 27.803  1.00  12.19 ? 32  ASP A CA  1 
ATOM   246  C  C   . ASP A 1 32  ? -6.843  -9.652  28.735  1.00  12.16 ? 32  ASP A C   1 
ATOM   247  O  O   . ASP A 1 32  ? -6.561  -9.039  29.730  1.00  12.70 ? 32  ASP A O   1 
ATOM   248  C  CB  . ASP A 1 32  ? -4.982  -11.247 28.461  1.00  11.98 ? 32  ASP A CB  1 
ATOM   249  C  CG  . ASP A 1 32  ? -5.905  -12.422 28.721  1.00  12.63 ? 32  ASP A CG  1 
ATOM   250  O  OD1 . ASP A 1 32  ? -6.625  -12.852 27.782  1.00  12.29 ? 32  ASP A OD1 1 
ATOM   251  O  OD2 . ASP A 1 32  ? -5.965  -12.919 29.892  1.00  14.46 ? 32  ASP A OD2 1 
ATOM   252  N  N   . ILE A 1 33  ? -8.118  -9.970  28.456  1.00  13.51 ? 33  ILE A N   1 
ATOM   253  C  CA  . ILE A 1 33  ? -9.190  -9.596  29.315  1.00  15.21 ? 33  ILE A CA  1 
ATOM   254  C  C   . ILE A 1 33  ? -9.493  -10.790 30.205  1.00  14.49 ? 33  ILE A C   1 
ATOM   255  O  O   . ILE A 1 33  ? -10.027 -11.828 29.762  1.00  16.35 ? 33  ILE A O   1 
ATOM   256  C  CB  . ILE A 1 33  ? -10.438 -9.079  28.546  1.00  14.93 ? 33  ILE A CB  1 
ATOM   257  C  CG1 . ILE A 1 33  ? -10.076 -7.792  27.743  1.00  14.37 ? 33  ILE A CG1 1 
ATOM   258  C  CG2 . ILE A 1 33  ? -11.532 -8.785  29.546  1.00  14.87 ? 33  ILE A CG2 1 
ATOM   259  C  CD1 . ILE A 1 33  ? -11.030 -7.474  26.578  1.00  14.17 ? 33  ILE A CD1 1 
ATOM   260  N  N   . ASP A 1 34  ? -9.047  -10.678 31.430  1.00  17.34 ? 34  ASP A N   1 
ATOM   261  C  CA  . ASP A 1 34  ? -9.381  -11.711 32.447  1.00  18.92 ? 34  ASP A CA  1 
ATOM   262  C  C   . ASP A 1 34  ? -10.826 -11.474 32.948  1.00  18.71 ? 34  ASP A C   1 
ATOM   263  O  O   . ASP A 1 34  ? -11.128 -10.551 33.784  1.00  19.50 ? 34  ASP A O   1 
ATOM   264  C  CB  . ASP A 1 34  ? -8.415  -11.664 33.611  1.00  23.43 ? 34  ASP A CB  1 
ATOM   265  C  CG  . ASP A 1 34  ? -8.653  -12.844 34.582  1.00  29.98 ? 34  ASP A CG  1 
ATOM   266  O  OD1 . ASP A 1 34  ? -9.748  -12.959 35.171  1.00  30.93 ? 34  ASP A OD1 1 
ATOM   267  O  OD2 . ASP A 1 34  ? -7.783  -13.720 34.646  1.00  35.39 ? 34  ASP A OD2 1 
ATOM   268  N  N   . THR A 1 35  ? -11.748 -12.254 32.424  1.00  18.09 ? 35  THR A N   1 
ATOM   269  C  CA  . THR A 1 35  ? -13.136 -11.968 32.627  1.00  19.17 ? 35  THR A CA  1 
ATOM   270  C  C   . THR A 1 35  ? -13.503 -12.151 34.094  1.00  21.54 ? 35  THR A C   1 
ATOM   271  O  O   . THR A 1 35  ? -14.533 -11.651 34.562  1.00  20.76 ? 35  THR A O   1 
ATOM   272  C  CB  . THR A 1 35  ? -14.073 -12.900 31.828  1.00  21.23 ? 35  THR A CB  1 
ATOM   273  O  OG1 . THR A 1 35  ? -13.862 -14.261 32.250  1.00  18.94 ? 35  THR A OG1 1 
ATOM   274  C  CG2 . THR A 1 35  ? -13.882 -12.762 30.308  1.00  19.83 ? 35  THR A CG2 1 
ATOM   275  N  N   . HIS A 1 36  ? -12.670 -12.881 34.817  1.00  22.77 ? 36  HIS A N   1 
ATOM   276  C  CA  . HIS A 1 36  ? -12.923 -13.056 36.232  1.00  24.23 ? 36  HIS A CA  1 
ATOM   277  C  C   . HIS A 1 36  ? -12.379 -11.964 37.059  1.00  25.07 ? 36  HIS A C   1 
ATOM   278  O  O   . HIS A 1 36  ? -12.911 -11.691 38.090  1.00  31.52 ? 36  HIS A O   1 
ATOM   279  C  CB  . HIS A 1 36  ? -12.475 -14.453 36.680  1.00  24.25 ? 36  HIS A CB  1 
ATOM   280  C  CG  . HIS A 1 36  ? -13.267 -15.557 36.008  1.00  23.56 ? 36  HIS A CG  1 
ATOM   281  N  ND1 . HIS A 1 36  ? -12.717 -16.405 35.104  1.00  26.27 ? 36  HIS A ND1 1 
ATOM   282  C  CD2 . HIS A 1 36  ? -14.621 -15.910 36.109  1.00  24.17 ? 36  HIS A CD2 1 
ATOM   283  C  CE1 . HIS A 1 36  ? -13.646 -17.262 34.664  1.00  26.60 ? 36  HIS A CE1 1 
ATOM   284  N  NE2 . HIS A 1 36  ? -14.820 -16.955 35.255  1.00  27.97 ? 36  HIS A NE2 1 
ATOM   285  N  N   . THR A 1 37  ? -11.350 -11.269 36.618  1.00  23.39 ? 37  THR A N   1 
ATOM   286  C  CA  . THR A 1 37  ? -10.873 -10.191 37.427  1.00  24.46 ? 37  THR A CA  1 
ATOM   287  C  C   . THR A 1 37  ? -11.426 -8.797  36.965  1.00  23.06 ? 37  THR A C   1 
ATOM   288  O  O   . THR A 1 37  ? -11.153 -7.800  37.614  1.00  21.65 ? 37  THR A O   1 
ATOM   289  C  CB  . THR A 1 37  ? -9.335  -10.204 37.590  1.00  27.28 ? 37  THR A CB  1 
ATOM   290  O  OG1 . THR A 1 37  ? -8.703  -9.960  36.333  1.00  34.84 ? 37  THR A OG1 1 
ATOM   291  C  CG2 . THR A 1 37  ? -8.844  -11.569 38.134  1.00  26.13 ? 37  THR A CG2 1 
ATOM   292  N  N   . ALA A 1 38  ? -12.204 -8.759  35.885  1.00  21.33 ? 38  ALA A N   1 
ATOM   293  C  CA  . ALA A 1 38  ? -12.786 -7.488  35.410  1.00  21.89 ? 38  ALA A CA  1 
ATOM   294  C  C   . ALA A 1 38  ? -13.892 -7.167  36.403  1.00  24.14 ? 38  ALA A C   1 
ATOM   295  O  O   . ALA A 1 38  ? -14.671 -8.011  36.749  1.00  26.89 ? 38  ALA A O   1 
ATOM   296  C  CB  . ALA A 1 38  ? -13.364 -7.623  34.024  1.00  21.39 ? 38  ALA A CB  1 
ATOM   297  N  N   . LYS A 1 39  ? -13.957 -5.915  36.807  1.00  24.97 ? 39  LYS A N   1 
ATOM   298  C  CA  . LYS A 1 39  ? -14.811 -5.444  37.871  1.00  23.84 ? 39  LYS A CA  1 
ATOM   299  C  C   . LYS A 1 39  ? -16.100 -4.897  37.241  1.00  23.03 ? 39  LYS A C   1 
ATOM   300  O  O   . LYS A 1 39  ? -16.102 -3.914  36.476  1.00  18.35 ? 39  LYS A O   1 
ATOM   301  C  CB  . LYS A 1 39  ? -13.997 -4.361  38.561  1.00  26.76 ? 39  LYS A CB  1 
ATOM   302  C  CG  . LYS A 1 39  ? -14.751 -3.462  39.531  1.00  28.74 ? 39  LYS A CG  1 
ATOM   303  C  CD  . LYS A 1 39  ? -14.861 -4.009  40.950  1.00  28.62 ? 39  LYS A CD  1 
ATOM   304  C  CE  . LYS A 1 39  ? -16.026 -3.286  41.656  1.00  31.13 ? 39  LYS A CE  1 
ATOM   305  N  NZ  . LYS A 1 39  ? -16.318 -3.687  43.060  1.00  32.07 ? 39  LYS A NZ  1 
ATOM   306  N  N   . TYR A 1 40  ? -17.223 -5.518  37.559  1.00  21.65 ? 40  TYR A N   1 
ATOM   307  C  CA  . TYR A 1 40  ? -18.485 -4.891  37.220  1.00  23.16 ? 40  TYR A CA  1 
ATOM   308  C  C   . TYR A 1 40  ? -18.645 -3.493  37.851  1.00  23.87 ? 40  TYR A C   1 
ATOM   309  O  O   . TYR A 1 40  ? -18.466 -3.301  39.072  1.00  19.17 ? 40  TYR A O   1 
ATOM   310  C  CB  . TYR A 1 40  ? -19.705 -5.791  37.521  1.00  26.26 ? 40  TYR A CB  1 
ATOM   311  C  CG  . TYR A 1 40  ? -21.034 -5.062  37.399  1.00  26.74 ? 40  TYR A CG  1 
ATOM   312  C  CD1 . TYR A 1 40  ? -21.546 -4.688  36.160  1.00  28.68 ? 40  TYR A CD1 1 
ATOM   313  C  CD2 . TYR A 1 40  ? -21.795 -4.743  38.541  1.00  33.45 ? 40  TYR A CD2 1 
ATOM   314  C  CE1 . TYR A 1 40  ? -22.755 -4.023  36.045  1.00  28.67 ? 40  TYR A CE1 1 
ATOM   315  C  CE2 . TYR A 1 40  ? -23.012 -4.069  38.440  1.00  29.68 ? 40  TYR A CE2 1 
ATOM   316  C  CZ  . TYR A 1 40  ? -23.489 -3.706  37.196  1.00  34.32 ? 40  TYR A CZ  1 
ATOM   317  O  OH  . TYR A 1 40  ? -24.692 -3.025  37.088  1.00  35.58 ? 40  TYR A OH  1 
ATOM   318  N  N   . ASP A 1 41  ? -19.028 -2.539  37.001  1.00  22.28 ? 41  ASP A N   1 
ATOM   319  C  CA  . ASP A 1 41  ? -19.144 -1.167  37.455  1.00  26.07 ? 41  ASP A CA  1 
ATOM   320  C  C   . ASP A 1 41  ? -20.532 -0.646  37.119  1.00  28.22 ? 41  ASP A C   1 
ATOM   321  O  O   . ASP A 1 41  ? -20.749 -0.236  35.977  1.00  27.98 ? 41  ASP A O   1 
ATOM   322  C  CB  . ASP A 1 41  ? -18.036 -0.274  36.862  1.00  25.10 ? 41  ASP A CB  1 
ATOM   323  C  CG  . ASP A 1 41  ? -18.137 1.195   37.336  1.00  28.49 ? 41  ASP A CG  1 
ATOM   324  O  OD1 . ASP A 1 41  ? -19.162 1.561   37.958  1.00  28.85 ? 41  ASP A OD1 1 
ATOM   325  O  OD2 . ASP A 1 41  ? -17.195 1.962   37.090  1.00  26.50 ? 41  ASP A OD2 1 
ATOM   326  N  N   . PRO A 1 42  ? -21.478 -0.684  38.096  1.00  31.53 ? 42  PRO A N   1 
ATOM   327  C  CA  . PRO A 1 42  ? -22.833 -0.177  37.868  1.00  34.53 ? 42  PRO A CA  1 
ATOM   328  C  C   . PRO A 1 42  ? -22.905 1.314   37.527  1.00  32.25 ? 42  PRO A C   1 
ATOM   329  O  O   . PRO A 1 42  ? -23.932 1.735   37.011  1.00  34.26 ? 42  PRO A O   1 
ATOM   330  C  CB  . PRO A 1 42  ? -23.538 -0.422  39.222  1.00  37.41 ? 42  PRO A CB  1 
ATOM   331  C  CG  . PRO A 1 42  ? -22.414 -0.520  40.212  1.00  37.47 ? 42  PRO A CG  1 
ATOM   332  C  CD  . PRO A 1 42  ? -21.387 -1.294  39.433  1.00  33.18 ? 42  PRO A CD  1 
ATOM   333  N  N   . SER A 1 43  ? -21.867 2.116   37.788  1.00  30.55 ? 43  SER A N   1 
ATOM   334  C  CA  . SER A 1 43  ? -21.944 3.504   37.310  1.00  32.43 ? 43  SER A CA  1 
ATOM   335  C  C   . SER A 1 43  ? -21.638 3.732   35.814  1.00  33.16 ? 43  SER A C   1 
ATOM   336  O  O   . SER A 1 43  ? -21.723 4.875   35.349  1.00  36.70 ? 43  SER A O   1 
ATOM   337  C  CB  . SER A 1 43  ? -21.047 4.416   38.141  1.00  36.42 ? 43  SER A CB  1 
ATOM   338  O  OG  . SER A 1 43  ? -19.665 4.199   37.863  1.00  36.32 ? 43  SER A OG  1 
ATOM   339  N  N   . LEU A 1 44  ? -21.233 2.684   35.069  1.00  28.73 ? 44  LEU A N   1 
ATOM   340  C  CA  . LEU A 1 44  ? -20.945 2.807   33.603  1.00  24.96 ? 44  LEU A CA  1 
ATOM   341  C  C   . LEU A 1 44  ? -22.256 2.903   32.839  1.00  27.29 ? 44  LEU A C   1 
ATOM   342  O  O   . LEU A 1 44  ? -23.174 2.106   33.073  1.00  28.07 ? 44  LEU A O   1 
ATOM   343  C  CB  . LEU A 1 44  ? -20.134 1.596   33.068  1.00  22.75 ? 44  LEU A CB  1 
ATOM   344  C  CG  . LEU A 1 44  ? -18.668 1.414   33.443  1.00  18.61 ? 44  LEU A CG  1 
ATOM   345  C  CD1 . LEU A 1 44  ? -18.179 0.066   32.967  1.00  19.30 ? 44  LEU A CD1 1 
ATOM   346  C  CD2 . LEU A 1 44  ? -17.806 2.455   32.743  1.00  19.93 ? 44  LEU A CD2 1 
ATOM   347  N  N   . LYS A 1 45  ? -22.352 3.846   31.906  1.00  27.76 ? 45  LYS A N   1 
ATOM   348  C  CA  . LYS A 1 45  ? -23.609 4.018   31.157  1.00  28.26 ? 45  LYS A CA  1 
ATOM   349  C  C   . LYS A 1 45  ? -23.663 3.067   29.980  1.00  28.53 ? 45  LYS A C   1 
ATOM   350  O  O   . LYS A 1 45  ? -22.624 2.456   29.618  1.00  29.14 ? 45  LYS A O   1 
ATOM   351  C  CB  . LYS A 1 45  ? -23.789 5.452   30.732  1.00  30.92 ? 45  LYS A CB  1 
ATOM   352  C  CG  . LYS A 1 45  ? -23.795 6.346   31.964  1.00  34.17 ? 45  LYS A CG  1 
ATOM   353  C  CD  . LYS A 1 45  ? -24.293 7.767   31.767  1.00  41.93 ? 45  LYS A CD  1 
ATOM   354  C  CE  . LYS A 1 45  ? -23.515 8.502   30.686  1.00  44.49 ? 45  LYS A CE  1 
ATOM   355  N  NZ  . LYS A 1 45  ? -24.378 8.537   29.463  1.00  42.92 ? 45  LYS A NZ  1 
ATOM   356  N  N   . PRO A 1 46  ? -24.879 2.878   29.398  1.00  29.89 ? 46  PRO A N   1 
ATOM   357  C  CA  . PRO A 1 46  ? -24.912 2.138   28.117  1.00  28.81 ? 46  PRO A CA  1 
ATOM   358  C  C   . PRO A 1 46  ? -24.054 2.898   27.136  1.00  24.66 ? 46  PRO A C   1 
ATOM   359  O  O   . PRO A 1 46  ? -23.998 4.119   27.222  1.00  24.61 ? 46  PRO A O   1 
ATOM   360  C  CB  . PRO A 1 46  ? -26.388 2.226   27.701  1.00  30.08 ? 46  PRO A CB  1 
ATOM   361  C  CG  . PRO A 1 46  ? -27.137 2.338   28.989  1.00  30.07 ? 46  PRO A CG  1 
ATOM   362  C  CD  . PRO A 1 46  ? -26.238 3.153   29.911  1.00  29.21 ? 46  PRO A CD  1 
ATOM   363  N  N   . LEU A 1 47  ? -23.402 2.175   26.234  1.00  24.50 ? 47  LEU A N   1 
ATOM   364  C  CA  . LEU A 1 47  ? -22.618 2.768   25.170  1.00  21.20 ? 47  LEU A CA  1 
ATOM   365  C  C   . LEU A 1 47  ? -23.657 3.327   24.233  1.00  23.32 ? 47  LEU A C   1 
ATOM   366  O  O   . LEU A 1 47  ? -24.635 2.645   23.953  1.00  22.36 ? 47  LEU A O   1 
ATOM   367  C  CB  . LEU A 1 47  ? -21.853 1.645   24.438  1.00  24.41 ? 47  LEU A CB  1 
ATOM   368  C  CG  . LEU A 1 47  ? -20.843 2.065   23.413  1.00  26.75 ? 47  LEU A CG  1 
ATOM   369  C  CD1 . LEU A 1 47  ? -19.909 2.978   24.214  1.00  26.04 ? 47  LEU A CD1 1 
ATOM   370  C  CD2 . LEU A 1 47  ? -20.106 0.900   22.712  1.00  25.45 ? 47  LEU A CD2 1 
ATOM   371  N  N   . SER A 1 48  ? -23.448 4.542   23.741  1.00  20.47 ? 48  SER A N   1 
ATOM   372  C  CA  . SER A 1 48  ? -24.271 5.113   22.698  1.00  21.73 ? 48  SER A CA  1 
ATOM   373  C  C   . SER A 1 48  ? -23.557 5.227   21.342  1.00  20.61 ? 48  SER A C   1 
ATOM   374  O  O   . SER A 1 48  ? -22.606 6.006   21.165  1.00  18.88 ? 48  SER A O   1 
ATOM   375  C  CB  . SER A 1 48  ? -24.867 6.481   23.147  1.00  22.92 ? 48  SER A CB  1 
ATOM   376  O  OG  . SER A 1 48  ? -25.416 7.147   22.029  1.00  19.71 ? 48  SER A OG  1 
ATOM   377  N  N   . VAL A 1 49  ? -24.084 4.476   20.385  1.00  19.21 ? 49  VAL A N   1 
ATOM   378  C  CA  . VAL A 1 49  ? -23.541 4.329   19.065  1.00  23.82 ? 49  VAL A CA  1 
ATOM   379  C  C   . VAL A 1 49  ? -24.511 4.978   18.092  1.00  26.01 ? 49  VAL A C   1 
ATOM   380  O  O   . VAL A 1 49  ? -25.633 4.490   17.887  1.00  28.76 ? 49  VAL A O   1 
ATOM   381  C  CB  . VAL A 1 49  ? -23.279 2.836   18.710  1.00  25.36 ? 49  VAL A CB  1 
ATOM   382  C  CG1 . VAL A 1 49  ? -22.745 2.702   17.285  1.00  26.20 ? 49  VAL A CG1 1 
ATOM   383  C  CG2 . VAL A 1 49  ? -22.320 2.203   19.704  1.00  23.18 ? 49  VAL A CG2 1 
ATOM   384  N  N   . SER A 1 50  ? -24.120 6.119   17.543  1.00  24.86 ? 50  SER A N   1 
ATOM   385  C  CA  . SER A 1 50  ? -24.999 6.828   16.620  1.00  24.09 ? 50  SER A CA  1 
ATOM   386  C  C   . SER A 1 50  ? -24.383 6.876   15.255  1.00  23.09 ? 50  SER A C   1 
ATOM   387  O  O   . SER A 1 50  ? -23.609 7.771   14.934  1.00  25.30 ? 50  SER A O   1 
ATOM   388  C  CB  . SER A 1 50  ? -25.293 8.248   17.052  1.00  25.90 ? 50  SER A CB  1 
ATOM   389  O  OG  . SER A 1 50  ? -25.859 8.276   18.323  1.00  31.30 ? 50  SER A OG  1 
ATOM   390  N  N   . TYR A 1 51  ? -24.680 5.881   14.454  1.00  21.87 ? 51  TYR A N   1 
ATOM   391  C  CA  . TYR A 1 51  ? -24.050 5.787   13.166  1.00  20.75 ? 51  TYR A CA  1 
ATOM   392  C  C   . TYR A 1 51  ? -25.070 6.049   12.059  1.00  21.70 ? 51  TYR A C   1 
ATOM   393  O  O   . TYR A 1 51  ? -24.766 5.848   10.886  1.00  20.73 ? 51  TYR A O   1 
ATOM   394  C  CB  . TYR A 1 51  ? -23.382 4.414   12.971  1.00  17.62 ? 51  TYR A CB  1 
ATOM   395  C  CG  . TYR A 1 51  ? -22.095 4.123   13.748  1.00  16.88 ? 51  TYR A CG  1 
ATOM   396  C  CD1 . TYR A 1 51  ? -21.365 5.140   14.414  1.00  15.60 ? 51  TYR A CD1 1 
ATOM   397  C  CD2 . TYR A 1 51  ? -21.556 2.814   13.760  1.00  15.72 ? 51  TYR A CD2 1 
ATOM   398  C  CE1 . TYR A 1 51  ? -20.184 4.831   15.129  1.00  13.94 ? 51  TYR A CE1 1 
ATOM   399  C  CE2 . TYR A 1 51  ? -20.389 2.511   14.444  1.00  14.55 ? 51  TYR A CE2 1 
ATOM   400  C  CZ  . TYR A 1 51  ? -19.713 3.532   15.129  1.00  14.72 ? 51  TYR A CZ  1 
ATOM   401  O  OH  . TYR A 1 51  ? -18.537 3.221   15.774  1.00  14.30 ? 51  TYR A OH  1 
ATOM   402  N  N   . ASP A 1 52  ? -26.285 6.486   12.403  1.00  27.23 ? 52  ASP A N   1 
ATOM   403  C  CA  . ASP A 1 52  ? -27.320 6.737   11.352  1.00  31.91 ? 52  ASP A CA  1 
ATOM   404  C  C   . ASP A 1 52  ? -26.834 7.623   10.180  1.00  31.43 ? 52  ASP A C   1 
ATOM   405  O  O   . ASP A 1 52  ? -27.151 7.358   9.025   1.00  31.34 ? 52  ASP A O   1 
ATOM   406  C  CB  . ASP A 1 52  ? -28.655 7.253   11.923  1.00  37.92 ? 52  ASP A CB  1 
ATOM   407  C  CG  . ASP A 1 52  ? -28.475 8.376   12.957  1.00  49.19 ? 52  ASP A CG  1 
ATOM   408  O  OD1 . ASP A 1 52  ? -28.294 8.086   14.184  1.00  53.17 ? 52  ASP A OD1 1 
ATOM   409  O  OD2 . ASP A 1 52  ? -28.534 9.557   12.539  1.00  52.41 ? 52  ASP A OD2 1 
ATOM   410  N  N   . GLN A 1 53  ? -25.992 8.606   10.460  1.00  30.47 ? 53  GLN A N   1 
ATOM   411  C  CA  . GLN A 1 53  ? -25.558 9.522   9.402   1.00  30.92 ? 53  GLN A CA  1 
ATOM   412  C  C   . GLN A 1 53  ? -24.146 9.293   8.875   1.00  28.44 ? 53  GLN A C   1 
ATOM   413  O  O   . GLN A 1 53  ? -23.578 10.184  8.212   1.00  23.95 ? 53  GLN A O   1 
ATOM   414  C  CB  . GLN A 1 53  ? -25.675 10.953  9.928   1.00  36.09 ? 53  GLN A CB  1 
ATOM   415  C  CG  . GLN A 1 53  ? -27.088 11.424  10.212  1.00  41.60 ? 53  GLN A CG  1 
ATOM   416  C  CD  . GLN A 1 53  ? -27.755 11.738  8.904   1.00  53.23 ? 53  GLN A CD  1 
ATOM   417  O  OE1 . GLN A 1 53  ? -27.762 12.900  8.473   1.00  63.40 ? 53  GLN A OE1 1 
ATOM   418  N  NE2 . GLN A 1 53  ? -28.238 10.697  8.208   1.00  51.15 ? 53  GLN A NE2 1 
ATOM   419  N  N   . ALA A 1 54  ? -23.575 8.105   9.109   1.00  24.04 ? 54  ALA A N   1 
ATOM   420  C  CA  . ALA A 1 54  ? -22.188 7.884   8.767   1.00  20.63 ? 54  ALA A CA  1 
ATOM   421  C  C   . ALA A 1 54  ? -22.029 8.038   7.262   1.00  23.27 ? 54  ALA A C   1 
ATOM   422  O  O   . ALA A 1 54  ? -22.903 7.627   6.493   1.00  23.18 ? 54  ALA A O   1 
ATOM   423  C  CB  . ALA A 1 54  ? -21.695 6.517   9.236   1.00  20.39 ? 54  ALA A CB  1 
ATOM   424  N  N   . THR A 1 55  ? -20.964 8.726   6.853   1.00  17.96 ? 55  THR A N   1 
ATOM   425  C  CA  . THR A 1 55  ? -20.575 8.895   5.450   1.00  18.95 ? 55  THR A CA  1 
ATOM   426  C  C   . THR A 1 55  ? -19.236 8.248   5.185   1.00  18.18 ? 55  THR A C   1 
ATOM   427  O  O   . THR A 1 55  ? -18.204 8.885   5.385   1.00  18.17 ? 55  THR A O   1 
ATOM   428  C  CB  . THR A 1 55  ? -20.327 10.418  5.114   1.00  19.61 ? 55  THR A CB  1 
ATOM   429  O  OG1 . THR A 1 55  ? -21.538 11.138  5.313   1.00  26.40 ? 55  THR A OG1 1 
ATOM   430  C  CG2 . THR A 1 55  ? -19.941 10.555  3.651   1.00  20.48 ? 55  THR A CG2 1 
ATOM   431  N  N   . SER A 1 56  ? -19.206 7.024   4.660   1.00  16.76 ? 56  SER A N   1 
ATOM   432  C  CA  . SER A 1 56  ? -17.902 6.458   4.322   1.00  16.98 ? 56  SER A CA  1 
ATOM   433  C  C   . SER A 1 56  ? -17.387 7.098   3.022   1.00  19.21 ? 56  SER A C   1 
ATOM   434  O  O   . SER A 1 56  ? -18.170 7.609   2.225   1.00  21.09 ? 56  SER A O   1 
ATOM   435  C  CB  . SER A 1 56  ? -17.992 4.918   4.193   1.00  18.49 ? 56  SER A CB  1 
ATOM   436  O  OG  . SER A 1 56  ? -18.917 4.596   3.168   1.00  18.54 ? 56  SER A OG  1 
ATOM   437  N  N   . LEU A 1 57  ? -16.081 7.129   2.838   1.00  18.79 ? 57  LEU A N   1 
ATOM   438  C  CA  . LEU A 1 57  ? -15.473 7.826   1.691   1.00  22.07 ? 57  LEU A CA  1 
ATOM   439  C  C   . LEU A 1 57  ? -14.715 6.889   0.780   1.00  20.91 ? 57  LEU A C   1 
ATOM   440  O  O   . LEU A 1 57  ? -14.986 6.854   -0.423  1.00  18.26 ? 57  LEU A O   1 
ATOM   441  C  CB  . LEU A 1 57  ? -14.519 8.942   2.153   1.00  21.01 ? 57  LEU A CB  1 
ATOM   442  C  CG  . LEU A 1 57  ? -15.277 10.026  2.938   1.00  24.93 ? 57  LEU A CG  1 
ATOM   443  C  CD1 . LEU A 1 57  ? -14.274 11.081  3.446   1.00  25.44 ? 57  LEU A CD1 1 
ATOM   444  C  CD2 . LEU A 1 57  ? -16.372 10.636  2.081   1.00  27.36 ? 57  LEU A CD2 1 
ATOM   445  N  N   . ARG A 1 58  ? -13.755 6.160   1.371   1.00  20.90 ? 58  ARG A N   1 
ATOM   446  C  CA  . ARG A 1 58  ? -12.711 5.436   0.637   1.00  20.65 ? 58  ARG A CA  1 
ATOM   447  C  C   . ARG A 1 58  ? -12.255 4.237   1.449   1.00  18.96 ? 58  ARG A C   1 
ATOM   448  O  O   . ARG A 1 58  ? -12.379 4.221   2.678   1.00  16.21 ? 58  ARG A O   1 
ATOM   449  C  CB  . ARG A 1 58  ? -11.473 6.280   0.485   1.00  22.53 ? 58  ARG A CB  1 
ATOM   450  C  CG  . ARG A 1 58  ? -11.380 7.204   -0.717  1.00  31.84 ? 58  ARG A CG  1 
ATOM   451  C  CD  . ARG A 1 58  ? -9.900  7.323   -1.049  1.00  34.88 ? 58  ARG A CD  1 
ATOM   452  N  NE  . ARG A 1 58  ? -9.148  7.210   0.218   1.00  35.74 ? 58  ARG A NE  1 
ATOM   453  C  CZ  . ARG A 1 58  ? -7.823  7.292   0.297   1.00  35.60 ? 58  ARG A CZ  1 
ATOM   454  N  NH1 . ARG A 1 58  ? -7.128  7.476   -0.816  1.00  32.35 ? 58  ARG A NH1 1 
ATOM   455  N  NH2 . ARG A 1 58  ? -7.198  7.214   1.469   1.00  33.04 ? 58  ARG A NH2 1 
ATOM   456  N  N   . ILE A 1 59  ? -11.719 3.267   0.750   1.00  16.94 ? 59  ILE A N   1 
ATOM   457  C  CA  . ILE A 1 59  ? -11.097 2.160   1.410   1.00  15.95 ? 59  ILE A CA  1 
ATOM   458  C  C   . ILE A 1 59  ? -9.684  2.105   0.864   1.00  16.69 ? 59  ILE A C   1 
ATOM   459  O  O   . ILE A 1 59  ? -9.445  2.244   -0.350  1.00  15.75 ? 59  ILE A O   1 
ATOM   460  C  CB  . ILE A 1 59  ? -11.871 0.826   1.238   1.00  15.38 ? 59  ILE A CB  1 
ATOM   461  C  CG1 . ILE A 1 59  ? -11.196 -0.271  2.079   1.00  13.98 ? 59  ILE A CG1 1 
ATOM   462  C  CG2 . ILE A 1 59  ? -11.851 0.365   -0.233  1.00  16.00 ? 59  ILE A CG2 1 
ATOM   463  C  CD1 . ILE A 1 59  ? -11.874 -1.634  2.036   1.00  13.58 ? 59  ILE A CD1 1 
ATOM   464  N  N   . LEU A 1 60  ? -8.743  1.886   1.763   1.00  15.81 ? 60  LEU A N   1 
ATOM   465  C  CA  . LEU A 1 60  ? -7.327  1.940   1.442   1.00  15.08 ? 60  LEU A CA  1 
ATOM   466  C  C   . LEU A 1 60  ? -6.526  0.769   2.001   1.00  16.44 ? 60  LEU A C   1 
ATOM   467  O  O   . LEU A 1 60  ? -6.560  0.496   3.230   1.00  15.89 ? 60  LEU A O   1 
ATOM   468  C  CB  . LEU A 1 60  ? -6.747  3.276   2.030   1.00  15.56 ? 60  LEU A CB  1 
ATOM   469  C  CG  . LEU A 1 60  ? -5.215  3.303   1.979   1.00  16.65 ? 60  LEU A CG  1 
ATOM   470  C  CD1 . LEU A 1 60  ? -4.674  3.565   0.579   1.00  18.29 ? 60  LEU A CD1 1 
ATOM   471  C  CD2 . LEU A 1 60  ? -4.716  4.364   2.954   1.00  16.87 ? 60  LEU A CD2 1 
ATOM   472  N  N   . ASN A 1 61  ? -5.702  0.143   1.166   1.00  16.66 ? 61  ASN A N   1 
ATOM   473  C  CA  . ASN A 1 61  ? -4.679  -0.794  1.640   1.00  17.23 ? 61  ASN A CA  1 
ATOM   474  C  C   . ASN A 1 61  ? -3.388  -0.010  1.911   1.00  18.41 ? 61  ASN A C   1 
ATOM   475  O  O   . ASN A 1 61  ? -2.734  0.471   0.987   1.00  18.41 ? 61  ASN A O   1 
ATOM   476  C  CB  . ASN A 1 61  ? -4.430  -1.940  0.629   1.00  16.75 ? 61  ASN A CB  1 
ATOM   477  C  CG  . ASN A 1 61  ? -3.321  -2.876  1.023   1.00  17.30 ? 61  ASN A CG  1 
ATOM   478  O  OD1 . ASN A 1 61  ? -2.487  -2.582  1.837   1.00  19.66 ? 61  ASN A OD1 1 
ATOM   479  N  ND2 . ASN A 1 61  ? -3.317  -4.081  0.436   1.00  20.06 ? 61  ASN A ND2 1 
ATOM   480  N  N   . ASN A 1 62  ? -3.021  0.110   3.182   1.00  18.18 ? 62  ASN A N   1 
ATOM   481  C  CA  . ASN A 1 62  ? -1.807  0.862   3.539   1.00  21.21 ? 62  ASN A CA  1 
ATOM   482  C  C   . ASN A 1 62  ? -0.598  -0.008  3.703   1.00  20.92 ? 62  ASN A C   1 
ATOM   483  O  O   . ASN A 1 62  ? 0.481   0.404   4.184   1.00  20.53 ? 62  ASN A O   1 
ATOM   484  C  CB  . ASN A 1 62  ? -2.067  1.736   4.779   1.00  23.74 ? 62  ASN A CB  1 
ATOM   485  C  CG  . ASN A 1 62  ? -1.779  1.017   6.091   1.00  25.42 ? 62  ASN A CG  1 
ATOM   486  O  OD1 . ASN A 1 62  ? -2.040  -0.207  6.284   1.00  19.50 ? 62  ASN A OD1 1 
ATOM   487  N  ND2 . ASN A 1 62  ? -1.274  1.808   7.040   1.00  28.78 ? 62  ASN A ND2 1 
ATOM   488  N  N   . GLY A 1 63  ? -0.718  -1.274  3.351   1.00  17.87 ? 63  GLY A N   1 
ATOM   489  C  CA  . GLY A 1 63  ? 0.480   -2.033  3.503   1.00  17.72 ? 63  GLY A CA  1 
ATOM   490  C  C   . GLY A 1 63  ? 0.505   -2.782  4.829   1.00  18.55 ? 63  GLY A C   1 
ATOM   491  O  O   . GLY A 1 63  ? 1.362   -3.635  5.009   1.00  17.19 ? 63  GLY A O   1 
ATOM   492  N  N   . HIS A 1 64  ? -0.393  -2.430  5.758   1.00  16.70 ? 64  HIS A N   1 
ATOM   493  C  CA  . HIS A 1 64  ? -0.404  -3.131  7.084   1.00  17.22 ? 64  HIS A CA  1 
ATOM   494  C  C   . HIS A 1 64  ? -1.757  -3.772  7.322   1.00  16.67 ? 64  HIS A C   1 
ATOM   495  O  O   . HIS A 1 64  ? -1.858  -4.867  7.902   1.00  19.38 ? 64  HIS A O   1 
ATOM   496  C  CB  . HIS A 1 64  ? -0.124  -2.163  8.228   1.00  14.83 ? 64  HIS A CB  1 
ATOM   497  C  CG  . HIS A 1 64  ? 1.266   -1.513  8.179   1.00  17.54 ? 64  HIS A CG  1 
ATOM   498  N  ND1 . HIS A 1 64  ? 2.403   -2.216  8.360   1.00  17.94 ? 64  HIS A ND1 1 
ATOM   499  C  CD2 . HIS A 1 64  ? 1.647   -0.184  8.036   1.00  17.28 ? 64  HIS A CD2 1 
ATOM   500  C  CE1 . HIS A 1 64  ? 3.470   -1.379  8.372   1.00  17.17 ? 64  HIS A CE1 1 
ATOM   501  N  NE2 . HIS A 1 64  ? 3.005   -0.130  8.161   1.00  18.61 ? 64  HIS A NE2 1 
ATOM   502  N  N   . ALA A 1 65  ? -2.793  -3.045  6.952   1.00  15.01 ? 65  ALA A N   1 
ATOM   503  C  CA  . ALA A 1 65  ? -4.195  -3.487  7.016   1.00  14.64 ? 65  ALA A CA  1 
ATOM   504  C  C   . ALA A 1 65  ? -5.007  -2.695  5.996   1.00  14.74 ? 65  ALA A C   1 
ATOM   505  O  O   . ALA A 1 65  ? -4.426  -2.003  5.172   1.00  16.02 ? 65  ALA A O   1 
ATOM   506  C  CB  . ALA A 1 65  ? -4.773  -3.346  8.466   1.00  12.65 ? 65  ALA A CB  1 
ATOM   507  N  N   . PHE A 1 66  ? -6.338  -2.775  6.015   1.00  12.81 ? 66  PHE A N   1 
ATOM   508  C  CA  . PHE A 1 66  ? -7.056  -1.876  5.150   1.00  13.95 ? 66  PHE A CA  1 
ATOM   509  C  C   . PHE A 1 66  ? -7.909  -0.991  5.979   1.00  13.65 ? 66  PHE A C   1 
ATOM   510  O  O   . PHE A 1 66  ? -8.402  -1.426  7.016   1.00  12.99 ? 66  PHE A O   1 
ATOM   511  C  CB  . PHE A 1 66  ? -7.827  -2.626  4.046   1.00  13.19 ? 66  PHE A CB  1 
ATOM   512  C  CG  . PHE A 1 66  ? -8.915  -3.514  4.576   1.00  14.00 ? 66  PHE A CG  1 
ATOM   513  C  CD1 . PHE A 1 66  ? -10.198 -2.985  4.921   1.00  13.47 ? 66  PHE A CD1 1 
ATOM   514  C  CD2 . PHE A 1 66  ? -8.662  -4.892  4.719   1.00  14.51 ? 66  PHE A CD2 1 
ATOM   515  C  CE1 . PHE A 1 66  ? -11.182 -3.816  5.402   1.00  13.01 ? 66  PHE A CE1 1 
ATOM   516  C  CE2 . PHE A 1 66  ? -9.643  -5.719  5.245   1.00  13.34 ? 66  PHE A CE2 1 
ATOM   517  C  CZ  . PHE A 1 66  ? -10.896 -5.178  5.575   1.00  12.74 ? 66  PHE A CZ  1 
ATOM   518  N  N   . ASN A 1 67  ? -8.051  0.280   5.585   1.00  14.70 ? 67  ASN A N   1 
ATOM   519  C  CA  . ASN A 1 67  ? -8.825  1.220   6.346   1.00  15.94 ? 67  ASN A CA  1 
ATOM   520  C  C   . ASN A 1 67  ? -10.031 1.717   5.625   1.00  15.93 ? 67  ASN A C   1 
ATOM   521  O  O   . ASN A 1 67  ? -9.916  2.195   4.490   1.00  17.44 ? 67  ASN A O   1 
ATOM   522  C  CB  . ASN A 1 67  ? -8.012  2.465   6.721   1.00  18.38 ? 67  ASN A CB  1 
ATOM   523  C  CG  . ASN A 1 67  ? -6.765  2.149   7.437   1.00  23.79 ? 67  ASN A CG  1 
ATOM   524  O  OD1 . ASN A 1 67  ? -6.738  1.235   8.270   1.00  22.73 ? 67  ASN A OD1 1 
ATOM   525  N  ND2 . ASN A 1 67  ? -5.709  2.933   7.168   1.00  23.94 ? 67  ASN A ND2 1 
ATOM   526  N  N   . VAL A 1 68  ? -11.184 1.615   6.235   1.00  14.69 ? 68  VAL A N   1 
ATOM   527  C  CA  . VAL A 1 68  ? -12.340 2.259   5.643   1.00  15.37 ? 68  VAL A CA  1 
ATOM   528  C  C   . VAL A 1 68  ? -12.468 3.644   6.329   1.00  17.84 ? 68  VAL A C   1 
ATOM   529  O  O   . VAL A 1 68  ? -12.658 3.704   7.523   1.00  16.07 ? 68  VAL A O   1 
ATOM   530  C  CB  . VAL A 1 68  ? -13.638 1.409   5.782   1.00  15.26 ? 68  VAL A CB  1 
ATOM   531  C  CG1 . VAL A 1 68  ? -14.898 2.226   5.450   1.00  14.84 ? 68  VAL A CG1 1 
ATOM   532  C  CG2 . VAL A 1 68  ? -13.529 0.134   4.920   1.00  13.39 ? 68  VAL A CG2 1 
ATOM   533  N  N   . GLU A 1 69  ? -12.410 4.731   5.563   1.00  20.24 ? 69  GLU A N   1 
ATOM   534  C  CA  . GLU A 1 69  ? -12.416 6.110   6.114   1.00  20.39 ? 69  GLU A CA  1 
ATOM   535  C  C   . GLU A 1 69  ? -13.764 6.802   5.983   1.00  19.70 ? 69  GLU A C   1 
ATOM   536  O  O   . GLU A 1 69  ? -14.573 6.455   5.086   1.00  22.87 ? 69  GLU A O   1 
ATOM   537  C  CB  . GLU A 1 69  ? -11.373 6.948   5.431   1.00  21.59 ? 69  GLU A CB  1 
ATOM   538  C  CG  . GLU A 1 69  ? -10.055 6.213   5.302   1.00  25.50 ? 69  GLU A CG  1 
ATOM   539  C  CD  . GLU A 1 69  ? -9.309  6.582   4.019   1.00  32.10 ? 69  GLU A CD  1 
ATOM   540  O  OE1 . GLU A 1 69  ? -9.956  7.218   3.097   1.00  32.89 ? 69  GLU A OE1 1 
ATOM   541  O  OE2 . GLU A 1 69  ? -8.084  6.238   3.924   1.00  32.78 ? 69  GLU A OE2 1 
ATOM   542  N  N   . PHE A 1 70  ? -14.029 7.714   6.929   1.00  16.40 ? 70  PHE A N   1 
ATOM   543  C  CA  . PHE A 1 70  ? -15.356 8.340   7.051   1.00  16.53 ? 70  PHE A CA  1 
ATOM   544  C  C   . PHE A 1 70  ? -15.102 9.806   6.990   1.00  17.29 ? 70  PHE A C   1 
ATOM   545  O  O   . PHE A 1 70  ? -13.966 10.195  7.213   1.00  16.05 ? 70  PHE A O   1 
ATOM   546  C  CB  . PHE A 1 70  ? -16.032 7.964   8.351   1.00  15.50 ? 70  PHE A CB  1 
ATOM   547  C  CG  . PHE A 1 70  ? -16.611 6.557   8.311   1.00  16.27 ? 70  PHE A CG  1 
ATOM   548  C  CD1 . PHE A 1 70  ? -15.763 5.415   8.365   1.00  17.10 ? 70  PHE A CD1 1 
ATOM   549  C  CD2 . PHE A 1 70  ? -17.958 6.373   8.005   1.00  14.73 ? 70  PHE A CD2 1 
ATOM   550  C  CE1 . PHE A 1 70  ? -16.319 4.111   8.288   1.00  15.74 ? 70  PHE A CE1 1 
ATOM   551  C  CE2 . PHE A 1 70  ? -18.511 5.084   7.902   1.00  15.02 ? 70  PHE A CE2 1 
ATOM   552  C  CZ  . PHE A 1 70  ? -17.688 3.957   8.037   1.00  15.01 ? 70  PHE A CZ  1 
ATOM   553  N  N   . ASP A 1 71  ? -16.123 10.570  6.594   1.00  17.41 ? 71  ASP A N   1 
ATOM   554  C  CA  . ASP A 1 71  ? -16.039 12.011  6.626   1.00  18.33 ? 71  ASP A CA  1 
ATOM   555  C  C   . ASP A 1 71  ? -16.376 12.365  8.056   1.00  17.60 ? 71  ASP A C   1 
ATOM   556  O  O   . ASP A 1 71  ? -17.479 12.052  8.571   1.00  23.98 ? 71  ASP A O   1 
ATOM   557  C  CB  . ASP A 1 71  ? -17.027 12.609  5.651   1.00  19.17 ? 71  ASP A CB  1 
ATOM   558  C  CG  . ASP A 1 71  ? -17.289 14.077  5.924   1.00  23.25 ? 71  ASP A CG  1 
ATOM   559  O  OD1 . ASP A 1 71  ? -16.335 14.754  6.331   1.00  21.89 ? 71  ASP A OD1 1 
ATOM   560  O  OD2 . ASP A 1 71  ? -18.473 14.498  5.843   1.00  24.91 ? 71  ASP A OD2 1 
ATOM   561  N  N   . ASP A 1 72  ? -15.438 12.997  8.721   1.00  15.42 ? 72  ASP A N   1 
ATOM   562  C  CA  . ASP A 1 72  ? -15.579 13.294  10.169  1.00  18.01 ? 72  ASP A CA  1 
ATOM   563  C  C   . ASP A 1 72  ? -15.438 14.830  10.323  1.00  20.00 ? 72  ASP A C   1 
ATOM   564  O  O   . ASP A 1 72  ? -14.927 15.302  11.339  1.00  20.37 ? 72  ASP A O   1 
ATOM   565  C  CB  . ASP A 1 72  ? -14.427 12.603  10.932  1.00  19.93 ? 72  ASP A CB  1 
ATOM   566  C  CG  . ASP A 1 72  ? -13.032 13.174  10.592  1.00  20.37 ? 72  ASP A CG  1 
ATOM   567  O  OD1 . ASP A 1 72  ? -12.789 13.798  9.520   1.00  21.54 ? 72  ASP A OD1 1 
ATOM   568  O  OD2 . ASP A 1 72  ? -12.107 13.066  11.409  1.00  22.69 ? 72  ASP A OD2 1 
ATOM   569  N  N   . SER A 1 73  ? -15.807 15.562  9.280   1.00  21.18 ? 73  SER A N   1 
ATOM   570  C  CA  . SER A 1 73  ? -15.800 17.052  9.331   1.00  22.77 ? 73  SER A CA  1 
ATOM   571  C  C   . SER A 1 73  ? -17.073 17.640  9.936   1.00  26.15 ? 73  SER A C   1 
ATOM   572  O  O   . SER A 1 73  ? -17.216 18.880  10.067  1.00  23.96 ? 73  SER A O   1 
ATOM   573  C  CB  . SER A 1 73  ? -15.524 17.607  7.945   1.00  21.39 ? 73  SER A CB  1 
ATOM   574  O  OG  . SER A 1 73  ? -16.584 17.300  7.078   1.00  21.54 ? 73  SER A OG  1 
ATOM   575  N  N   . GLN A 1 74  ? -18.032 16.777  10.311  1.00  27.31 ? 74  GLN A N   1 
ATOM   576  C  CA  . GLN A 1 74  ? -19.093 17.193  11.234  1.00  28.88 ? 74  GLN A CA  1 
ATOM   577  C  C   . GLN A 1 74  ? -19.555 16.010  12.047  1.00  30.04 ? 74  GLN A C   1 
ATOM   578  O  O   . GLN A 1 74  ? -19.077 14.922  11.819  1.00  27.07 ? 74  GLN A O   1 
ATOM   579  C  CB  . GLN A 1 74  ? -20.289 17.851  10.527  1.00  31.50 ? 74  GLN A CB  1 
ATOM   580  C  CG  . GLN A 1 74  ? -20.434 17.437  9.084   1.00  36.18 ? 74  GLN A CG  1 
ATOM   581  C  CD  . GLN A 1 74  ? -21.505 18.207  8.342   1.00  38.72 ? 74  GLN A CD  1 
ATOM   582  O  OE1 . GLN A 1 74  ? -22.176 19.067  8.918   1.00  47.81 ? 74  GLN A OE1 1 
ATOM   583  N  NE2 . GLN A 1 74  ? -21.693 17.879  7.072   1.00  34.31 ? 74  GLN A NE2 1 
ATOM   584  N  N   . ASP A 1 75  ? -20.473 16.268  12.993  1.00  32.74 ? 75  ASP A N   1 
ATOM   585  C  CA  . ASP A 1 75  ? -20.945 15.295  13.981  1.00  35.98 ? 75  ASP A CA  1 
ATOM   586  C  C   . ASP A 1 75  ? -21.970 14.376  13.357  1.00  32.52 ? 75  ASP A C   1 
ATOM   587  O  O   . ASP A 1 75  ? -23.169 14.576  13.494  1.00  40.99 ? 75  ASP A O   1 
ATOM   588  C  CB  . ASP A 1 75  ? -21.520 15.993  15.233  1.00  37.63 ? 75  ASP A CB  1 
ATOM   589  C  CG  . ASP A 1 75  ? -20.500 16.063  16.385  1.00  37.99 ? 75  ASP A CG  1 
ATOM   590  O  OD1 . ASP A 1 75  ? -19.428 15.403  16.284  1.00  37.55 ? 75  ASP A OD1 1 
ATOM   591  O  OD2 . ASP A 1 75  ? -20.754 16.774  17.384  1.00  40.28 ? 75  ASP A OD2 1 
ATOM   592  N  N   . LYS A 1 76  ? -21.474 13.379  12.659  1.00  28.49 ? 76  LYS A N   1 
ATOM   593  C  CA  . LYS A 1 76  ? -22.305 12.507  11.839  1.00  29.11 ? 76  LYS A CA  1 
ATOM   594  C  C   . LYS A 1 76  ? -22.410 11.092  12.452  1.00  30.47 ? 76  LYS A C   1 
ATOM   595  O  O   . LYS A 1 76  ? -23.502 10.559  12.635  1.00  38.85 ? 76  LYS A O   1 
ATOM   596  C  CB  . LYS A 1 76  ? -21.726 12.450  10.412  1.00  29.91 ? 76  LYS A CB  1 
ATOM   597  C  CG  . LYS A 1 76  ? -22.250 13.542  9.455   1.00  28.51 ? 76  LYS A CG  1 
ATOM   598  C  CD  . LYS A 1 76  ? -21.530 13.397  8.105   1.00  30.74 ? 76  LYS A CD  1 
ATOM   599  C  CE  . LYS A 1 76  ? -21.936 14.453  7.066   1.00  31.54 ? 76  LYS A CE  1 
ATOM   600  N  NZ  . LYS A 1 76  ? -21.589 14.023  5.685   1.00  27.85 ? 76  LYS A NZ  1 
ATOM   601  N  N   . ALA A 1 77  ? -21.275 10.476  12.734  1.00  25.87 ? 77  ALA A N   1 
ATOM   602  C  CA  . ALA A 1 77  ? -21.244 9.133   13.326  1.00  20.96 ? 77  ALA A CA  1 
ATOM   603  C  C   . ALA A 1 77  ? -20.508 9.294   14.648  1.00  20.40 ? 77  ALA A C   1 
ATOM   604  O  O   . ALA A 1 77  ? -19.330 9.542   14.629  1.00  24.66 ? 77  ALA A O   1 
ATOM   605  C  CB  . ALA A 1 77  ? -20.448 8.262   12.406  1.00  20.65 ? 77  ALA A CB  1 
ATOM   606  N  N   . VAL A 1 78  ? -21.179 9.203   15.787  1.00  19.42 ? 78  VAL A N   1 
ATOM   607  C  CA  . VAL A 1 78  ? -20.542 9.454   17.081  1.00  19.31 ? 78  VAL A CA  1 
ATOM   608  C  C   . VAL A 1 78  ? -20.799 8.346   18.116  1.00  18.17 ? 78  VAL A C   1 
ATOM   609  O  O   . VAL A 1 78  ? -21.846 7.674   18.119  1.00  18.31 ? 78  VAL A O   1 
ATOM   610  C  CB  . VAL A 1 78  ? -20.959 10.837  17.666  1.00  20.21 ? 78  VAL A CB  1 
ATOM   611  C  CG1 . VAL A 1 78  ? -20.609 11.954  16.676  1.00  18.47 ? 78  VAL A CG1 1 
ATOM   612  C  CG2 . VAL A 1 78  ? -22.442 10.838  17.968  1.00  21.40 ? 78  VAL A CG2 1 
ATOM   613  N  N   . LEU A 1 79  ? -19.806 8.190   18.955  1.00  16.28 ? 79  LEU A N   1 
ATOM   614  C  CA  . LEU A 1 79  ? -19.825 7.324   20.092  1.00  17.73 ? 79  LEU A CA  1 
ATOM   615  C  C   . LEU A 1 79  ? -19.806 8.253   21.297  1.00  18.86 ? 79  LEU A C   1 
ATOM   616  O  O   . LEU A 1 79  ? -19.017 9.228   21.345  1.00  18.60 ? 79  LEU A O   1 
ATOM   617  C  CB  . LEU A 1 79  ? -18.555 6.479   20.061  1.00  15.75 ? 79  LEU A CB  1 
ATOM   618  C  CG  . LEU A 1 79  ? -18.329 5.411   21.059  1.00  16.52 ? 79  LEU A CG  1 
ATOM   619  C  CD1 . LEU A 1 79  ? -19.504 4.429   20.969  1.00  16.12 ? 79  LEU A CD1 1 
ATOM   620  C  CD2 . LEU A 1 79  ? -16.976 4.742   20.777  1.00  13.34 ? 79  LEU A CD2 1 
ATOM   621  N  N   . LYS A 1 80  ? -20.670 7.951   22.260  1.00  17.71 ? 80  LYS A N   1 
ATOM   622  C  CA  . LYS A 1 80  ? -20.711 8.660   23.541  1.00  20.43 ? 80  LYS A CA  1 
ATOM   623  C  C   . LYS A 1 80  ? -21.279 7.739   24.617  1.00  21.19 ? 80  LYS A C   1 
ATOM   624  O  O   . LYS A 1 80  ? -21.546 6.571   24.316  1.00  20.81 ? 80  LYS A O   1 
ATOM   625  C  CB  . LYS A 1 80  ? -21.432 10.011  23.463  1.00  22.27 ? 80  LYS A CB  1 
ATOM   626  C  CG  . LYS A 1 80  ? -22.934 9.938   23.225  1.00  30.99 ? 80  LYS A CG  1 
ATOM   627  C  CD  . LYS A 1 80  ? -23.449 11.342  22.846  1.00  34.16 ? 80  LYS A CD  1 
ATOM   628  C  CE  . LYS A 1 80  ? -23.558 11.475  21.322  1.00  37.97 ? 80  LYS A CE  1 
ATOM   629  N  NZ  . LYS A 1 80  ? -23.769 12.851  20.736  1.00  39.14 ? 80  LYS A NZ  1 
ATOM   630  N  N   . GLY A 1 81  ? -21.447 8.267   25.831  1.00  20.53 ? 81  GLY A N   1 
ATOM   631  C  CA  . GLY A 1 81  ? -21.825 7.501   27.007  1.00  20.84 ? 81  GLY A CA  1 
ATOM   632  C  C   . GLY A 1 81  ? -20.815 6.403   27.215  1.00  21.41 ? 81  GLY A C   1 
ATOM   633  O  O   . GLY A 1 81  ? -19.617 6.568   26.955  1.00  20.87 ? 81  GLY A O   1 
ATOM   634  N  N   . GLY A 1 82  ? -21.293 5.234   27.599  1.00  22.85 ? 82  GLY A N   1 
ATOM   635  C  CA  . GLY A 1 82  ? -20.355 4.220   28.084  1.00  22.78 ? 82  GLY A CA  1 
ATOM   636  C  C   . GLY A 1 82  ? -19.515 4.783   29.193  1.00  22.04 ? 82  GLY A C   1 
ATOM   637  O  O   . GLY A 1 82  ? -20.059 5.379   30.127  1.00  23.52 ? 82  GLY A O   1 
ATOM   638  N  N   . PRO A 1 83  ? -18.172 4.645   29.099  1.00  20.33 ? 83  PRO A N   1 
ATOM   639  C  CA  . PRO A 1 83  ? -17.234 5.240   30.042  1.00  18.22 ? 83  PRO A CA  1 
ATOM   640  C  C   . PRO A 1 83  ? -16.777 6.658   29.628  1.00  19.03 ? 83  PRO A C   1 
ATOM   641  O  O   . PRO A 1 83  ? -15.909 7.288   30.294  1.00  22.84 ? 83  PRO A O   1 
ATOM   642  C  CB  . PRO A 1 83  ? -16.032 4.290   29.944  1.00  20.13 ? 83  PRO A CB  1 
ATOM   643  C  CG  . PRO A 1 83  ? -16.046 3.864   28.479  1.00  17.05 ? 83  PRO A CG  1 
ATOM   644  C  CD  . PRO A 1 83  ? -17.494 3.782   28.093  1.00  19.13 ? 83  PRO A CD  1 
ATOM   645  N  N   . LEU A 1 84  ? -17.360 7.191   28.562  1.00  17.92 ? 84  LEU A N   1 
ATOM   646  C  CA  . LEU A 1 84  ? -16.764 8.348   27.928  1.00  18.36 ? 84  LEU A CA  1 
ATOM   647  C  C   . LEU A 1 84  ? -17.434 9.614   28.425  1.00  20.13 ? 84  LEU A C   1 
ATOM   648  O  O   . LEU A 1 84  ? -18.568 9.562   28.778  1.00  22.55 ? 84  LEU A O   1 
ATOM   649  C  CB  . LEU A 1 84  ? -16.928 8.293   26.414  1.00  15.84 ? 84  LEU A CB  1 
ATOM   650  C  CG  . LEU A 1 84  ? -16.307 7.003   25.813  1.00  15.83 ? 84  LEU A CG  1 
ATOM   651  C  CD1 . LEU A 1 84  ? -16.868 6.834   24.440  1.00  16.05 ? 84  LEU A CD1 1 
ATOM   652  C  CD2 . LEU A 1 84  ? -14.741 7.002   25.832  1.00  14.75 ? 84  LEU A CD2 1 
ATOM   653  N  N   A ASP A 1 85  ? -16.695 10.716  28.472  0.50  20.65 ? 85  ASP A N   1 
ATOM   654  N  N   B ASP A 1 85  ? -16.692 10.720  28.446  0.50  22.15 ? 85  ASP A N   1 
ATOM   655  C  CA  A ASP A 1 85  ? -17.321 12.009  28.627  0.50  20.19 ? 85  ASP A CA  1 
ATOM   656  C  CA  B ASP A 1 85  ? -17.189 11.958  29.026  0.50  23.16 ? 85  ASP A CA  1 
ATOM   657  C  C   A ASP A 1 85  ? -17.149 12.709  27.289  0.50  19.71 ? 85  ASP A C   1 
ATOM   658  C  C   B ASP A 1 85  ? -17.617 12.918  27.960  0.50  25.05 ? 85  ASP A C   1 
ATOM   659  O  O   A ASP A 1 85  ? -16.152 12.541  26.606  0.50  17.45 ? 85  ASP A O   1 
ATOM   660  O  O   B ASP A 1 85  ? -18.398 13.835  28.221  0.50  26.27 ? 85  ASP A O   1 
ATOM   661  C  CB  A ASP A 1 85  ? -16.811 12.785  29.856  0.50  22.79 ? 85  ASP A CB  1 
ATOM   662  C  CB  B ASP A 1 85  ? -16.169 12.590  29.960  0.50  24.11 ? 85  ASP A CB  1 
ATOM   663  C  CG  A ASP A 1 85  ? -15.328 12.943  29.864  0.50  23.47 ? 85  ASP A CG  1 
ATOM   664  C  CG  B ASP A 1 85  ? -16.338 12.119  31.375  0.50  25.01 ? 85  ASP A CG  1 
ATOM   665  O  OD1 A ASP A 1 85  ? -14.797 12.984  28.742  0.50  27.46 ? 85  ASP A OD1 1 
ATOM   666  O  OD1 B ASP A 1 85  ? -17.478 11.763  31.726  0.50  24.70 ? 85  ASP A OD1 1 
ATOM   667  O  OD2 A ASP A 1 85  ? -14.694 13.024  30.957  0.50  22.28 ? 85  ASP A OD2 1 
ATOM   668  O  OD2 B ASP A 1 85  ? -15.340 12.114  32.134  0.50  25.77 ? 85  ASP A OD2 1 
ATOM   669  N  N   A GLY A 1 86  ? -18.178 13.434  26.873  0.50  18.33 ? 86  GLY A N   1 
ATOM   670  N  N   B GLY A 1 86  ? -17.133 12.694  26.746  0.50  23.78 ? 86  GLY A N   1 
ATOM   671  C  CA  A GLY A 1 86  ? -18.121 14.121  25.618  0.50  19.47 ? 86  GLY A CA  1 
ATOM   672  C  CA  B GLY A 1 86  ? -17.548 13.546  25.659  0.50  22.32 ? 86  GLY A CA  1 
ATOM   673  C  C   A GLY A 1 86  ? -18.569 13.250  24.450  0.50  22.69 ? 86  GLY A C   1 
ATOM   674  C  C   B GLY A 1 86  ? -18.031 12.797  24.423  0.50  22.90 ? 86  GLY A C   1 
ATOM   675  O  O   A GLY A 1 86  ? -19.420 12.343  24.595  0.50  24.53 ? 86  GLY A O   1 
ATOM   676  O  O   B GLY A 1 86  ? -18.490 11.638  24.488  0.50  21.20 ? 86  GLY A O   1 
ATOM   677  N  N   . THR A 1 87  ? -17.955 13.499  23.301  1.00  20.04 ? 87  THR A N   1 
ATOM   678  C  CA  . THR A 1 87  ? -18.449 13.018  22.028  1.00  20.55 ? 87  THR A CA  1 
ATOM   679  C  C   . THR A 1 87  ? -17.249 12.648  21.231  1.00  16.49 ? 87  THR A C   1 
ATOM   680  O  O   . THR A 1 87  ? -16.294 13.429  21.102  1.00  15.22 ? 87  THR A O   1 
ATOM   681  C  CB  . THR A 1 87  ? -19.171 14.168  21.271  1.00  22.73 ? 87  THR A CB  1 
ATOM   682  O  OG1 . THR A 1 87  ? -20.382 14.420  21.938  1.00  30.07 ? 87  THR A OG1 1 
ATOM   683  C  CG2 . THR A 1 87  ? -19.558 13.753  19.805  1.00  21.46 ? 87  THR A CG2 1 
ATOM   684  N  N   . TYR A 1 88  ? -17.288 11.451  20.685  1.00  15.42 ? 88  TYR A N   1 
ATOM   685  C  CA  . TYR A 1 88  ? -16.187 11.010  19.910  1.00  14.49 ? 88  TYR A CA  1 
ATOM   686  C  C   . TYR A 1 88  ? -16.666 10.682  18.486  1.00  14.27 ? 88  TYR A C   1 
ATOM   687  O  O   . TYR A 1 88  ? -17.615 9.922   18.289  1.00  18.00 ? 88  TYR A O   1 
ATOM   688  C  CB  . TYR A 1 88  ? -15.507 9.803   20.559  1.00  12.50 ? 88  TYR A CB  1 
ATOM   689  C  CG  . TYR A 1 88  ? -14.758 10.022  21.857  1.00  12.62 ? 88  TYR A CG  1 
ATOM   690  C  CD1 . TYR A 1 88  ? -15.431 10.318  23.036  1.00  11.21 ? 88  TYR A CD1 1 
ATOM   691  C  CD2 . TYR A 1 88  ? -13.377 9.869   21.911  1.00  10.77 ? 88  TYR A CD2 1 
ATOM   692  C  CE1 . TYR A 1 88  ? -14.742 10.488  24.226  1.00  11.46 ? 88  TYR A CE1 1 
ATOM   693  C  CE2 . TYR A 1 88  ? -12.683 10.040  23.094  1.00  11.08 ? 88  TYR A CE2 1 
ATOM   694  C  CZ  . TYR A 1 88  ? -13.368 10.349  24.247  1.00  10.38 ? 88  TYR A CZ  1 
ATOM   695  O  OH  . TYR A 1 88  ? -12.678 10.519  25.425  1.00  12.82 ? 88  TYR A OH  1 
ATOM   696  N  N   . ARG A 1 89  ? -15.994 11.269  17.516  1.00  14.00 ? 89  ARG A N   1 
ATOM   697  C  CA  . ARG A 1 89  ? -16.289 11.142  16.087  1.00  15.57 ? 89  ARG A CA  1 
ATOM   698  C  C   . ARG A 1 89  ? -15.623 9.993   15.360  1.00  13.67 ? 89  ARG A C   1 
ATOM   699  O  O   . ARG A 1 89  ? -14.397 9.903   15.345  1.00  12.59 ? 89  ARG A O   1 
ATOM   700  C  CB  . ARG A 1 89  ? -15.766 12.381  15.388  1.00  18.71 ? 89  ARG A CB  1 
ATOM   701  C  CG  . ARG A 1 89  ? -16.870 13.116  14.756  1.00  23.16 ? 89  ARG A CG  1 
ATOM   702  C  CD  . ARG A 1 89  ? -16.380 14.353  14.078  1.00  22.37 ? 89  ARG A CD  1 
ATOM   703  N  NE  . ARG A 1 89  ? -17.162 15.398  14.670  1.00  22.55 ? 89  ARG A NE  1 
ATOM   704  C  CZ  . ARG A 1 89  ? -17.021 16.682  14.395  1.00  24.67 ? 89  ARG A CZ  1 
ATOM   705  N  NH1 . ARG A 1 89  ? -16.088 17.081  13.525  1.00  23.67 ? 89  ARG A NH1 1 
ATOM   706  N  NH2 . ARG A 1 89  ? -17.822 17.554  15.017  1.00  24.00 ? 89  ARG A NH2 1 
ATOM   707  N  N   . LEU A 1 90  ? -16.404 9.135   14.689  1.00  13.35 ? 90  LEU A N   1 
ATOM   708  C  CA  . LEU A 1 90  ? -15.750 8.048   13.898  1.00  13.61 ? 90  LEU A CA  1 
ATOM   709  C  C   . LEU A 1 90  ? -14.922 8.546   12.740  1.00  13.43 ? 90  LEU A C   1 
ATOM   710  O  O   . LEU A 1 90  ? -15.374 9.332   11.886  1.00  14.04 ? 90  LEU A O   1 
ATOM   711  C  CB  . LEU A 1 90  ? -16.838 7.094   13.392  1.00  14.69 ? 90  LEU A CB  1 
ATOM   712  C  CG  . LEU A 1 90  ? -16.436 6.011   12.387  1.00  16.14 ? 90  LEU A CG  1 
ATOM   713  C  CD1 . LEU A 1 90  ? -15.535 4.954   12.998  1.00  16.28 ? 90  LEU A CD1 1 
ATOM   714  C  CD2 . LEU A 1 90  ? -17.678 5.295   11.869  1.00  14.49 ? 90  LEU A CD2 1 
ATOM   715  N  N   . ILE A 1 91  ? -13.668 8.120   12.678  1.00  12.48 ? 91  ILE A N   1 
ATOM   716  C  CA  . ILE A 1 91  ? -12.817 8.500   11.580  1.00  11.42 ? 91  ILE A CA  1 
ATOM   717  C  C   . ILE A 1 91  ? -12.569 7.357   10.620  1.00  11.20 ? 91  ILE A C   1 
ATOM   718  O  O   . ILE A 1 91  ? -12.538 7.602   9.436   1.00  9.43  ? 91  ILE A O   1 
ATOM   719  C  CB  . ILE A 1 91  ? -11.493 9.166   12.045  1.00  11.59 ? 91  ILE A CB  1 
ATOM   720  C  CG1 . ILE A 1 91  ? -10.532 9.448   10.852  1.00  11.79 ? 91  ILE A CG1 1 
ATOM   721  C  CG2 . ILE A 1 91  ? -10.776 8.361   13.146  1.00  11.78 ? 91  ILE A CG2 1 
ATOM   722  C  CD1 . ILE A 1 91  ? -9.572  10.563  11.234  1.00  13.31 ? 91  ILE A CD1 1 
ATOM   723  N  N   . GLN A 1 92  ? -12.403 6.113   11.124  1.00  9.75  ? 92  GLN A N   1 
ATOM   724  C  CA  . GLN A 1 92  ? -12.109 4.990   10.240  1.00  10.37 ? 92  GLN A CA  1 
ATOM   725  C  C   . GLN A 1 92  ? -12.396 3.695   10.995  1.00  10.13 ? 92  GLN A C   1 
ATOM   726  O  O   . GLN A 1 92  ? -12.489 3.723   12.224  1.00  9.31  ? 92  GLN A O   1 
ATOM   727  C  CB  . GLN A 1 92  ? -10.634 5.069   9.753   1.00  10.31 ? 92  GLN A CB  1 
ATOM   728  C  CG  . GLN A 1 92  ? -9.604  5.009   10.871  1.00  11.15 ? 92  GLN A CG  1 
ATOM   729  C  CD  . GLN A 1 92  ? -8.915  3.636   10.867  1.00  13.74 ? 92  GLN A CD  1 
ATOM   730  O  OE1 . GLN A 1 92  ? -9.476  2.669   11.324  1.00  14.70 ? 92  GLN A OE1 1 
ATOM   731  N  NE2 . GLN A 1 92  ? -7.670  3.593   10.413  1.00  17.26 ? 92  GLN A NE2 1 
ATOM   732  N  N   . PHE A 1 93  ? -12.515 2.598   10.249  1.00  11.54 ? 93  PHE A N   1 
ATOM   733  C  CA  . PHE A 1 93  ? -12.433 1.295   10.849  1.00  11.22 ? 93  PHE A CA  1 
ATOM   734  C  C   . PHE A 1 93  ? -11.411 0.418   10.107  1.00  11.91 ? 93  PHE A C   1 
ATOM   735  O  O   . PHE A 1 93  ? -11.098 0.624   8.927   1.00  12.38 ? 93  PHE A O   1 
ATOM   736  C  CB  . PHE A 1 93  ? -13.833 0.642   11.113  1.00  11.67 ? 93  PHE A CB  1 
ATOM   737  C  CG  . PHE A 1 93  ? -14.524 0.157   9.906   1.00  13.76 ? 93  PHE A CG  1 
ATOM   738  C  CD1 . PHE A 1 93  ? -14.037 -0.970  9.196   1.00  13.65 ? 93  PHE A CD1 1 
ATOM   739  C  CD2 . PHE A 1 93  ? -15.666 0.838   9.425   1.00  12.86 ? 93  PHE A CD2 1 
ATOM   740  C  CE1 . PHE A 1 93  ? -14.665 -1.404  8.047   1.00  13.91 ? 93  PHE A CE1 1 
ATOM   741  C  CE2 . PHE A 1 93  ? -16.321 0.369   8.274   1.00  12.69 ? 93  PHE A CE2 1 
ATOM   742  C  CZ  . PHE A 1 93  ? -15.822 -0.729  7.597   1.00  14.51 ? 93  PHE A CZ  1 
ATOM   743  N  N   . HIS A 1 94  ? -10.833 -0.549  10.798  1.00  11.92 ? 94  HIS A N   1 
ATOM   744  C  CA  . HIS A 1 94  ? -9.914  -1.498  10.182  1.00  11.17 ? 94  HIS A CA  1 
ATOM   745  C  C   . HIS A 1 94  ? -10.086 -2.757  10.973  1.00  11.03 ? 94  HIS A C   1 
ATOM   746  O  O   . HIS A 1 94  ? -10.833 -2.742  12.004  1.00  9.59  ? 94  HIS A O   1 
ATOM   747  C  CB  . HIS A 1 94  ? -8.460  -0.995  10.176  1.00  11.74 ? 94  HIS A CB  1 
ATOM   748  C  CG  . HIS A 1 94  ? -7.949  -0.732  11.573  1.00  12.88 ? 94  HIS A CG  1 
ATOM   749  N  ND1 . HIS A 1 94  ? -8.302  0.417   12.295  1.00  13.46 ? 94  HIS A ND1 1 
ATOM   750  C  CD2 . HIS A 1 94  ? -7.303  -1.564  12.440  1.00  12.61 ? 94  HIS A CD2 1 
ATOM   751  C  CE1 . HIS A 1 94  ? -7.758  0.317   13.513  1.00  12.92 ? 94  HIS A CE1 1 
ATOM   752  N  NE2 . HIS A 1 94  ? -7.188  -0.919  13.622  1.00  13.46 ? 94  HIS A NE2 1 
ATOM   753  N  N   . PHE A 1 95  ? -9.380  -3.808  10.519  1.00  10.01 ? 95  PHE A N   1 
ATOM   754  C  CA  . PHE A 1 95  ? -9.440  -5.149  11.198  1.00  10.00 ? 95  PHE A CA  1 
ATOM   755  C  C   . PHE A 1 95  ? -8.052  -5.626  11.421  1.00  9.18  ? 95  PHE A C   1 
ATOM   756  O  O   . PHE A 1 95  ? -7.150  -5.161  10.787  1.00  11.42 ? 95  PHE A O   1 
ATOM   757  C  CB  . PHE A 1 95  ? -10.151 -6.188  10.277  1.00  9.49  ? 95  PHE A CB  1 
ATOM   758  C  CG  . PHE A 1 95  ? -11.604 -5.888  9.960   1.00  10.35 ? 95  PHE A CG  1 
ATOM   759  C  CD1 . PHE A 1 95  ? -11.966 -5.037  8.885   1.00  9.72  ? 95  PHE A CD1 1 
ATOM   760  C  CD2 . PHE A 1 95  ? -12.641 -6.579  10.623  1.00  10.23 ? 95  PHE A CD2 1 
ATOM   761  C  CE1 . PHE A 1 95  ? -13.307 -4.832  8.555   1.00  10.78 ? 95  PHE A CE1 1 
ATOM   762  C  CE2 . PHE A 1 95  ? -13.979 -6.357  10.285  1.00  10.22 ? 95  PHE A CE2 1 
ATOM   763  C  CZ  . PHE A 1 95  ? -14.310 -5.528  9.205   1.00  10.62 ? 95  PHE A CZ  1 
ATOM   764  N  N   . HIS A 1 96  ? -7.862  -6.681  12.239  1.00  8.77  ? 96  HIS A N   1 
ATOM   765  C  CA  . HIS A 1 96  ? -6.555  -7.382  12.388  1.00  8.16  ? 96  HIS A CA  1 
ATOM   766  C  C   . HIS A 1 96  ? -6.979  -8.841  12.270  1.00  8.85  ? 96  HIS A C   1 
ATOM   767  O  O   . HIS A 1 96  ? -8.054  -9.184  12.795  1.00  8.80  ? 96  HIS A O   1 
ATOM   768  C  CB  . HIS A 1 96  ? -5.923  -7.164  13.784  1.00  8.04  ? 96  HIS A CB  1 
ATOM   769  C  CG  . HIS A 1 96  ? -5.639  -5.703  14.098  1.00  7.59  ? 96  HIS A CG  1 
ATOM   770  N  ND1 . HIS A 1 96  ? -4.422  -5.198  13.968  1.00  7.96  ? 96  HIS A ND1 1 
ATOM   771  C  CD2 . HIS A 1 96  ? -6.467  -4.655  14.538  1.00  7.67  ? 96  HIS A CD2 1 
ATOM   772  C  CE1 . HIS A 1 96  ? -4.443  -3.863  14.313  1.00  8.45  ? 96  HIS A CE1 1 
ATOM   773  N  NE2 . HIS A 1 96  ? -5.705  -3.551  14.646  1.00  8.85  ? 96  HIS A NE2 1 
ATOM   774  N  N   . TRP A 1 97  ? -6.171  -9.684  11.618  1.00  9.88  ? 97  TRP A N   1 
ATOM   775  C  CA  . TRP A 1 97  ? -6.664  -11.090 11.495  1.00  9.93  ? 97  TRP A CA  1 
ATOM   776  C  C   . TRP A 1 97  ? -5.518  -12.001 11.340  1.00  10.31 ? 97  TRP A C   1 
ATOM   777  O  O   . TRP A 1 97  ? -4.367  -11.530 11.154  1.00  10.81 ? 97  TRP A O   1 
ATOM   778  C  CB  . TRP A 1 97  ? -7.583  -11.269 10.304  1.00  11.32 ? 97  TRP A CB  1 
ATOM   779  C  CG  . TRP A 1 97  ? -7.003  -10.869 8.961   1.00  11.19 ? 97  TRP A CG  1 
ATOM   780  C  CD1 . TRP A 1 97  ? -6.376  -11.696 8.024   1.00  12.24 ? 97  TRP A CD1 1 
ATOM   781  C  CD2 . TRP A 1 97  ? -6.906  -9.496  8.409   1.00  12.00 ? 97  TRP A CD2 1 
ATOM   782  N  NE1 . TRP A 1 97  ? -5.975  -10.960 6.907   1.00  13.64 ? 97  TRP A NE1 1 
ATOM   783  C  CE2 . TRP A 1 97  ? -6.255  -9.620  7.097   1.00  12.62 ? 97  TRP A CE2 1 
ATOM   784  C  CE3 . TRP A 1 97  ? -7.322  -8.219  8.850   1.00  11.64 ? 97  TRP A CE3 1 
ATOM   785  C  CZ2 . TRP A 1 97  ? -5.983  -8.511  6.292   1.00  12.20 ? 97  TRP A CZ2 1 
ATOM   786  C  CZ3 . TRP A 1 97  ? -7.063  -7.079  7.995   1.00  12.74 ? 97  TRP A CZ3 1 
ATOM   787  C  CH2 . TRP A 1 97  ? -6.383  -7.222  6.773   1.00  11.50 ? 97  TRP A CH2 1 
ATOM   788  N  N   . GLY A 1 98  ? -5.841  -13.304 11.341  1.00  9.48  ? 98  GLY A N   1 
ATOM   789  C  CA  . GLY A 1 98  ? -4.830  -14.330 11.372  1.00  10.80 ? 98  GLY A CA  1 
ATOM   790  C  C   . GLY A 1 98  ? -4.594  -15.068 10.039  1.00  10.22 ? 98  GLY A C   1 
ATOM   791  O  O   . GLY A 1 98  ? -5.250  -14.824 9.033   1.00  11.52 ? 98  GLY A O   1 
ATOM   792  N  N   . SER A 1 99  ? -3.544  -15.886 10.025  1.00  11.55 ? 99  SER A N   1 
ATOM   793  C  CA  . SER A 1 99  ? -3.253  -16.804 8.964   1.00  11.92 ? 99  SER A CA  1 
ATOM   794  C  C   . SER A 1 99  ? -4.167  -18.001 9.102   1.00  13.95 ? 99  SER A C   1 
ATOM   795  O  O   . SER A 1 99  ? -4.279  -18.795 8.158   1.00  14.19 ? 99  SER A O   1 
ATOM   796  C  CB  . SER A 1 99  ? -1.792  -17.235 9.119   1.00  11.38 ? 99  SER A CB  1 
ATOM   797  O  OG  . SER A 1 99  ? -1.445  -17.675 10.437  1.00  12.48 ? 99  SER A OG  1 
ATOM   798  N  N   . LEU A 1 100 ? -4.704  -18.208 10.301  1.00  15.49 ? 100 LEU A N   1 
ATOM   799  C  CA  . LEU A 1 100 ? -5.597  -19.371 10.597  1.00  17.18 ? 100 LEU A CA  1 
ATOM   800  C  C   . LEU A 1 100 ? -6.722  -18.890 11.473  1.00  16.97 ? 100 LEU A C   1 
ATOM   801  O  O   . LEU A 1 100 ? -6.559  -17.866 12.176  1.00  15.45 ? 100 LEU A O   1 
ATOM   802  C  CB  . LEU A 1 100 ? -4.845  -20.434 11.421  1.00  18.16 ? 100 LEU A CB  1 
ATOM   803  C  CG  . LEU A 1 100 ? -3.464  -20.833 10.964  1.00  19.85 ? 100 LEU A CG  1 
ATOM   804  C  CD1 . LEU A 1 100 ? -2.647  -21.360 12.101  1.00  23.71 ? 100 LEU A CD1 1 
ATOM   805  C  CD2 . LEU A 1 100 ? -3.687  -21.940 9.948   1.00  24.63 ? 100 LEU A CD2 1 
ATOM   806  N  N   . ASP A 1 101 ? -7.843  -19.637 11.509  1.00  15.41 ? 101 ASP A N   1 
ATOM   807  C  CA  . ASP A 1 101 ? -8.963  -19.143 12.344  1.00  14.78 ? 101 ASP A CA  1 
ATOM   808  C  C   . ASP A 1 101 ? -8.634  -19.115 13.829  1.00  15.42 ? 101 ASP A C   1 
ATOM   809  O  O   . ASP A 1 101 ? -9.299  -18.408 14.560  1.00  16.04 ? 101 ASP A O   1 
ATOM   810  C  CB  . ASP A 1 101 ? -10.330 -19.903 12.131  1.00  16.87 ? 101 ASP A CB  1 
ATOM   811  C  CG  . ASP A 1 101 ? -10.755 -20.055 10.673  1.00  18.30 ? 101 ASP A CG  1 
ATOM   812  O  OD1 . ASP A 1 101 ? -10.430 -19.227 9.776   1.00  15.20 ? 101 ASP A OD1 1 
ATOM   813  O  OD2 . ASP A 1 101 ? -11.507 -21.029 10.464  1.00  20.24 ? 101 ASP A OD2 1 
ATOM   814  N  N   . GLY A 1 102 ? -7.609  -19.867 14.320  1.00  13.49 ? 102 GLY A N   1 
ATOM   815  C  CA  . GLY A 1 102 ? -7.374  -19.840 15.799  1.00  12.60 ? 102 GLY A CA  1 
ATOM   816  C  C   . GLY A 1 102 ? -6.634  -18.627 16.326  1.00  11.85 ? 102 GLY A C   1 
ATOM   817  O  O   . GLY A 1 102 ? -6.307  -18.545 17.487  1.00  12.21 ? 102 GLY A O   1 
ATOM   818  N  N   . GLN A 1 103 ? -6.360  -17.642 15.458  1.00  12.70 ? 103 GLN A N   1 
ATOM   819  C  CA  . GLN A 1 103 ? -5.662  -16.455 15.923  1.00  12.40 ? 103 GLN A CA  1 
ATOM   820  C  C   . GLN A 1 103 ? -5.998  -15.317 15.004  1.00  12.36 ? 103 GLN A C   1 
ATOM   821  O  O   . GLN A 1 103 ? -6.518  -15.528 13.953  1.00  11.90 ? 103 GLN A O   1 
ATOM   822  C  CB  . GLN A 1 103 ? -4.149  -16.718 15.926  1.00  13.24 ? 103 GLN A CB  1 
ATOM   823  C  CG  . GLN A 1 103 ? -3.534  -16.906 14.520  1.00  15.25 ? 103 GLN A CG  1 
ATOM   824  C  CD  . GLN A 1 103 ? -2.127  -17.516 14.589  1.00  18.98 ? 103 GLN A CD  1 
ATOM   825  O  OE1 . GLN A 1 103 ? -1.922  -18.469 15.350  1.00  21.15 ? 103 GLN A OE1 1 
ATOM   826  N  NE2 . GLN A 1 103 ? -1.159  -16.929 13.891  1.00  17.13 ? 103 GLN A NE2 1 
ATOM   827  N  N   . GLY A 1 104 ? -5.725  -14.097 15.428  1.00  11.70 ? 104 GLY A N   1 
ATOM   828  C  CA  . GLY A 1 104 ? -5.971  -12.914 14.568  1.00  11.04 ? 104 GLY A CA  1 
ATOM   829  C  C   . GLY A 1 104 ? -6.389  -11.751 15.493  1.00  10.90 ? 104 GLY A C   1 
ATOM   830  O  O   . GLY A 1 104 ? -6.030  -10.578 15.231  1.00  12.25 ? 104 GLY A O   1 
ATOM   831  N  N   . SER A 1 105 ? -7.189  -12.023 16.540  1.00  10.32 ? 105 SER A N   1 
ATOM   832  C  CA  . SER A 1 105 ? -7.555  -10.859 17.480  1.00  9.59  ? 105 SER A CA  1 
ATOM   833  C  C   . SER A 1 105 ? -6.315  -10.290 18.241  1.00  8.48  ? 105 SER A C   1 
ATOM   834  O  O   . SER A 1 105 ? -5.251  -10.919 18.417  1.00  9.49  ? 105 SER A O   1 
ATOM   835  C  CB  . SER A 1 105 ? -8.642  -11.174 18.490  1.00  8.52  ? 105 SER A CB  1 
ATOM   836  O  OG  . SER A 1 105 ? -8.203  -12.148 19.401  1.00  9.45  ? 105 SER A OG  1 
ATOM   837  N  N   . GLU A 1 106 ? -6.444  -9.033  18.640  1.00  8.49  ? 106 GLU A N   1 
ATOM   838  C  CA  . GLU A 1 106 ? -5.359  -8.362  19.384  1.00  8.65  ? 106 GLU A CA  1 
ATOM   839  C  C   . GLU A 1 106 ? -5.727  -8.560  20.866  1.00  9.07  ? 106 GLU A C   1 
ATOM   840  O  O   . GLU A 1 106 ? -4.923  -9.070  21.648  1.00  9.94  ? 106 GLU A O   1 
ATOM   841  C  CB  . GLU A 1 106 ? -5.364  -6.842  19.028  1.00  8.06  ? 106 GLU A CB  1 
ATOM   842  C  CG  . GLU A 1 106 ? -5.091  -6.657  17.556  1.00  9.11  ? 106 GLU A CG  1 
ATOM   843  C  CD  . GLU A 1 106 ? -4.266  -5.406  17.297  1.00  9.83  ? 106 GLU A CD  1 
ATOM   844  O  OE1 . GLU A 1 106 ? -4.842  -4.312  17.491  1.00  9.59  ? 106 GLU A OE1 1 
ATOM   845  O  OE2 . GLU A 1 106 ? -3.068  -5.508  16.947  1.00  9.59  ? 106 GLU A OE2 1 
ATOM   846  N  N   . HIS A 1 107 ? -6.968  -8.195  21.271  1.00  8.96  ? 107 HIS A N   1 
ATOM   847  C  CA  . HIS A 1 107 ? -7.376  -8.465  22.649  1.00  8.98  ? 107 HIS A CA  1 
ATOM   848  C  C   . HIS A 1 107 ? -7.713  -9.948  22.701  1.00  10.00 ? 107 HIS A C   1 
ATOM   849  O  O   . HIS A 1 107 ? -7.965  -10.546 21.635  1.00  9.63  ? 107 HIS A O   1 
ATOM   850  C  CB  . HIS A 1 107 ? -8.623  -7.679  22.922  1.00  8.94  ? 107 HIS A CB  1 
ATOM   851  C  CG  . HIS A 1 107 ? -8.338  -6.233  23.132  1.00  8.70  ? 107 HIS A CG  1 
ATOM   852  N  ND1 . HIS A 1 107 ? -8.307  -5.382  22.106  1.00  8.43  ? 107 HIS A ND1 1 
ATOM   853  C  CD2 . HIS A 1 107 ? -7.911  -5.542  24.248  1.00  8.75  ? 107 HIS A CD2 1 
ATOM   854  C  CE1 . HIS A 1 107 ? -7.960  -4.158  22.565  1.00  8.41  ? 107 HIS A CE1 1 
ATOM   855  N  NE2 . HIS A 1 107 ? -7.726  -4.256  23.879  1.00  8.24  ? 107 HIS A NE2 1 
ATOM   856  N  N   . THR A 1 108 ? -7.560  -10.534 23.885  1.00  10.40 ? 108 THR A N   1 
ATOM   857  C  CA  . THR A 1 108 ? -7.903  -11.948 24.115  1.00  11.21 ? 108 THR A CA  1 
ATOM   858  C  C   . THR A 1 108 ? -8.822  -11.973 25.342  1.00  12.83 ? 108 THR A C   1 
ATOM   859  O  O   . THR A 1 108 ? -8.815  -11.031 26.150  1.00  13.99 ? 108 THR A O   1 
ATOM   860  C  CB  . THR A 1 108 ? -6.620  -12.852 24.266  1.00  10.50 ? 108 THR A CB  1 
ATOM   861  O  OG1 . THR A 1 108 ? -5.806  -12.375 25.349  1.00  10.33 ? 108 THR A OG1 1 
ATOM   862  C  CG2 . THR A 1 108 ? -5.740  -12.892 22.967  1.00  9.88  ? 108 THR A CG2 1 
ATOM   863  N  N   . VAL A 1 109 ? -9.647  -13.020 25.501  1.00  13.88 ? 109 VAL A N   1 
ATOM   864  C  CA  . VAL A 1 109 ? -10.604 -13.069 26.612  1.00  12.88 ? 109 VAL A CA  1 
ATOM   865  C  C   . VAL A 1 109 ? -10.269 -14.391 27.430  1.00  13.70 ? 109 VAL A C   1 
ATOM   866  O  O   . VAL A 1 109 ? -10.479 -15.482 26.908  1.00  14.11 ? 109 VAL A O   1 
ATOM   867  C  CB  . VAL A 1 109 ? -12.050 -13.104 26.051  1.00  12.92 ? 109 VAL A CB  1 
ATOM   868  C  CG1 . VAL A 1 109 ? -13.098 -13.177 27.151  1.00  12.24 ? 109 VAL A CG1 1 
ATOM   869  C  CG2 . VAL A 1 109 ? -12.327 -11.892 25.118  1.00  12.03 ? 109 VAL A CG2 1 
ATOM   870  N  N   . ASP A 1 110 ? -9.698  -14.265 28.611  1.00  13.56 ? 110 ASP A N   1 
ATOM   871  C  CA  . ASP A 1 110 ? -9.177  -15.437 29.327  1.00  15.06 ? 110 ASP A CA  1 
ATOM   872  C  C   . ASP A 1 110 ? -8.314  -16.260 28.413  1.00  15.48 ? 110 ASP A C   1 
ATOM   873  O  O   . ASP A 1 110 ? -8.537  -17.502 28.299  1.00  14.66 ? 110 ASP A O   1 
ATOM   874  C  CB  . ASP A 1 110 ? -10.348 -16.271 29.886  1.00  15.90 ? 110 ASP A CB  1 
ATOM   875  C  CG  . ASP A 1 110 ? -11.226 -15.460 30.838  1.00  17.62 ? 110 ASP A CG  1 
ATOM   876  O  OD1 . ASP A 1 110 ? -10.671 -14.592 31.546  1.00  18.63 ? 110 ASP A OD1 1 
ATOM   877  O  OD2 . ASP A 1 110 ? -12.420 -15.711 30.825  1.00  17.31 ? 110 ASP A OD2 1 
ATOM   878  N  N   . LYS A 1 111 ? -7.375  -15.579 27.723  1.00  14.22 ? 111 LYS A N   1 
ATOM   879  C  CA  . LYS A 1 111 ? -6.365  -16.120 26.774  1.00  14.09 ? 111 LYS A CA  1 
ATOM   880  C  C   . LYS A 1 111 ? -6.898  -16.593 25.404  1.00  13.33 ? 111 LYS A C   1 
ATOM   881  O  O   . LYS A 1 111 ? -6.130  -17.013 24.569  1.00  12.71 ? 111 LYS A O   1 
ATOM   882  C  CB  . LYS A 1 111 ? -5.474  -17.208 27.459  1.00  15.45 ? 111 LYS A CB  1 
ATOM   883  C  CG  . LYS A 1 111 ? -4.759  -16.796 28.772  1.00  17.05 ? 111 LYS A CG  1 
ATOM   884  C  CD  . LYS A 1 111 ? -3.909  -15.554 28.594  1.00  22.40 ? 111 LYS A CD  1 
ATOM   885  C  CE  . LYS A 1 111 ? -3.309  -15.130 29.934  1.00  27.12 ? 111 LYS A CE  1 
ATOM   886  N  NZ  . LYS A 1 111 ? -1.925  -15.648 29.820  1.00  26.20 ? 111 LYS A NZ  1 
ATOM   887  N  N   . LYS A 1 112 ? -8.226  -16.530 25.172  1.00  12.48 ? 112 LYS A N   1 
ATOM   888  C  CA  . LYS A 1 112 ? -8.823  -17.031 23.959  1.00  13.92 ? 112 LYS A CA  1 
ATOM   889  C  C   . LYS A 1 112 ? -8.567  -16.000 22.819  1.00  14.26 ? 112 LYS A C   1 
ATOM   890  O  O   . LYS A 1 112 ? -8.890  -14.813 22.977  1.00  13.99 ? 112 LYS A O   1 
ATOM   891  C  CB  . LYS A 1 112 ? -10.363 -17.188 24.107  1.00  13.29 ? 112 LYS A CB  1 
ATOM   892  C  CG  . LYS A 1 112 ? -11.070 -17.540 22.805  1.00  15.71 ? 112 LYS A CG  1 
ATOM   893  C  CD  . LYS A 1 112 ? -12.593 -17.300 22.958  1.00  17.25 ? 112 LYS A CD  1 
ATOM   894  C  CE  . LYS A 1 112 ? -13.402 -17.613 21.674  1.00  21.67 ? 112 LYS A CE  1 
ATOM   895  N  NZ  . LYS A 1 112 ? -12.916 -18.788 20.933  1.00  17.85 ? 112 LYS A NZ  1 
ATOM   896  N  N   A LYS A 1 113 ? -7.944  -16.459 21.747  0.50  12.99 ? 113 LYS A N   1 
ATOM   897  N  N   B LYS A 1 113 ? -7.966  -16.467 21.731  0.50  13.11 ? 113 LYS A N   1 
ATOM   898  C  CA  A LYS A 1 113 ? -7.841  -15.674 20.516  0.50  13.16 ? 113 LYS A CA  1 
ATOM   899  C  CA  B LYS A 1 113 ? -7.742  -15.663 20.507  0.50  13.33 ? 113 LYS A CA  1 
ATOM   900  C  C   A LYS A 1 113 ? -9.091  -15.881 19.674  0.50  12.18 ? 113 LYS A C   1 
ATOM   901  C  C   B LYS A 1 113 ? -8.865  -15.890 19.448  0.50  12.48 ? 113 LYS A C   1 
ATOM   902  O  O   A LYS A 1 113 ? -9.616  -17.014 19.586  0.50  11.49 ? 113 LYS A O   1 
ATOM   903  O  O   B LYS A 1 113 ? -9.115  -17.059 19.028  0.50  11.77 ? 113 LYS A O   1 
ATOM   904  C  CB  A LYS A 1 113 ? -6.600  -16.082 19.704  0.50  12.54 ? 113 LYS A CB  1 
ATOM   905  C  CB  B LYS A 1 113 ? -6.332  -15.947 19.924  0.50  12.68 ? 113 LYS A CB  1 
ATOM   906  C  CG  A LYS A 1 113 ? -5.315  -15.769 20.413  0.50  12.72 ? 113 LYS A CG  1 
ATOM   907  C  CG  B LYS A 1 113 ? -5.182  -15.540 20.848  0.50  12.78 ? 113 LYS A CG  1 
ATOM   908  C  CD  A LYS A 1 113 ? -4.171  -16.499 19.740  0.50  12.75 ? 113 LYS A CD  1 
ATOM   909  C  CD  B LYS A 1 113 ? -3.895  -16.288 20.496  0.50  12.72 ? 113 LYS A CD  1 
ATOM   910  C  CE  A LYS A 1 113 ? -2.869  -15.846 20.141  0.50  12.38 ? 113 LYS A CE  1 
ATOM   911  C  CE  B LYS A 1 113 ? -2.608  -15.537 20.819  0.50  13.14 ? 113 LYS A CE  1 
ATOM   912  N  NZ  A LYS A 1 113 ? -2.363  -16.369 21.444  0.50  12.47 ? 113 LYS A NZ  1 
ATOM   913  N  NZ  B LYS A 1 113 ? -1.369  -16.355 20.530  0.50  12.55 ? 113 LYS A NZ  1 
ATOM   914  N  N   . TYR A 1 114 ? -9.538  -14.795 19.038  1.00  11.04 ? 114 TYR A N   1 
ATOM   915  C  CA  . TYR A 1 114 ? -10.573 -14.840 18.028  1.00  10.99 ? 114 TYR A CA  1 
ATOM   916  C  C   . TYR A 1 114 ? -9.941  -14.739 16.634  1.00  11.13 ? 114 TYR A C   1 
ATOM   917  O  O   . TYR A 1 114 ? -8.736  -14.410 16.527  1.00  11.24 ? 114 TYR A O   1 
ATOM   918  C  CB  . TYR A 1 114 ? -11.625 -13.719 18.228  1.00  10.58 ? 114 TYR A CB  1 
ATOM   919  C  CG  . TYR A 1 114 ? -12.583 -13.976 19.374  1.00  12.60 ? 114 TYR A CG  1 
ATOM   920  C  CD1 . TYR A 1 114 ? -12.318 -13.535 20.663  1.00  12.94 ? 114 TYR A CD1 1 
ATOM   921  C  CD2 . TYR A 1 114 ? -13.801 -14.611 19.155  1.00  12.84 ? 114 TYR A CD2 1 
ATOM   922  C  CE1 . TYR A 1 114 ? -13.185 -13.776 21.715  1.00  13.87 ? 114 TYR A CE1 1 
ATOM   923  C  CE2 . TYR A 1 114 ? -14.692 -14.810 20.183  1.00  13.58 ? 114 TYR A CE2 1 
ATOM   924  C  CZ  . TYR A 1 114 ? -14.389 -14.402 21.446  1.00  14.12 ? 114 TYR A CZ  1 
ATOM   925  O  OH  . TYR A 1 114 ? -15.298 -14.545 22.457  1.00  17.43 ? 114 TYR A OH  1 
ATOM   926  N  N   . ALA A 1 115 ? -10.715 -15.075 15.600  1.00  10.95 ? 115 ALA A N   1 
ATOM   927  C  CA  . ALA A 1 115 ? -10.243 -15.099 14.215  1.00  10.18 ? 115 ALA A CA  1 
ATOM   928  C  C   . ALA A 1 115 ? -9.854  -13.734 13.738  1.00  10.43 ? 115 ALA A C   1 
ATOM   929  O  O   . ALA A 1 115 ? -8.936  -13.598 12.951  1.00  11.31 ? 115 ALA A O   1 
ATOM   930  C  CB  . ALA A 1 115 ? -11.283 -15.734 13.293  1.00  10.75 ? 115 ALA A CB  1 
ATOM   931  N  N   . ALA A 1 116 ? -10.523 -12.688 14.266  1.00  9.75  ? 116 ALA A N   1 
ATOM   932  C  CA  . ALA A 1 116 ? -10.136 -11.366 13.875  1.00  9.48  ? 116 ALA A CA  1 
ATOM   933  C  C   . ALA A 1 116 ? -10.646 -10.356 14.865  1.00  8.85  ? 116 ALA A C   1 
ATOM   934  O  O   . ALA A 1 116 ? -11.350 -10.727 15.791  1.00  8.58  ? 116 ALA A O   1 
ATOM   935  C  CB  . ALA A 1 116 ? -10.635 -11.058 12.429  1.00  9.48  ? 116 ALA A CB  1 
ATOM   936  N  N   . GLU A 1 117 ? -10.308 -9.076  14.685  1.00  9.02  ? 117 GLU A N   1 
ATOM   937  C  CA  . GLU A 1 117 ? -10.865 -8.061  15.506  1.00  8.93  ? 117 GLU A CA  1 
ATOM   938  C  C   . GLU A 1 117 ? -11.074 -6.790  14.688  1.00  9.60  ? 117 GLU A C   1 
ATOM   939  O  O   . GLU A 1 117 ? -10.163 -6.338  14.063  1.00  10.40 ? 117 GLU A O   1 
ATOM   940  C  CB  . GLU A 1 117 ? -9.951  -7.830  16.721  1.00  9.84  ? 117 GLU A CB  1 
ATOM   941  C  CG  . GLU A 1 117 ? -10.487 -6.830  17.774  1.00  9.08  ? 117 GLU A CG  1 
ATOM   942  C  CD  . GLU A 1 117 ? -9.594  -6.749  19.006  1.00  9.72  ? 117 GLU A CD  1 
ATOM   943  O  OE1 . GLU A 1 117 ? -8.910  -7.767  19.320  1.00  10.34 ? 117 GLU A OE1 1 
ATOM   944  O  OE2 . GLU A 1 117 ? -9.556  -5.650  19.696  1.00  9.82  ? 117 GLU A OE2 1 
ATOM   945  N  N   . LEU A 1 118 ? -12.265 -6.250  14.771  1.00  8.06  ? 118 LEU A N   1 
ATOM   946  C  CA  . LEU A 1 118 ? -12.620 -4.980  14.091  1.00  8.30  ? 118 LEU A CA  1 
ATOM   947  C  C   . LEU A 1 118 ? -12.345 -3.801  15.070  1.00  8.05  ? 118 LEU A C   1 
ATOM   948  O  O   . LEU A 1 118 ? -12.645 -3.898  16.196  1.00  7.56  ? 118 LEU A O   1 
ATOM   949  C  CB  . LEU A 1 118 ? -14.131 -5.002  13.825  1.00  7.07  ? 118 LEU A CB  1 
ATOM   950  C  CG  . LEU A 1 118 ? -14.833 -3.737  13.361  1.00  7.02  ? 118 LEU A CG  1 
ATOM   951  C  CD1 . LEU A 1 118 ? -14.254 -3.293  12.025  1.00  8.16  ? 118 LEU A CD1 1 
ATOM   952  C  CD2 . LEU A 1 118 ? -16.320 -4.047  13.259  1.00  7.37  ? 118 LEU A CD2 1 
ATOM   953  N  N   . HIS A 1 119 ? -11.793 -2.695  14.584  1.00  7.96  ? 119 HIS A N   1 
ATOM   954  C  CA  . HIS A 1 119 ? -11.598 -1.578  15.467  1.00  8.16  ? 119 HIS A CA  1 
ATOM   955  C  C   . HIS A 1 119 ? -12.219 -0.388  14.795  1.00  8.29  ? 119 HIS A C   1 
ATOM   956  O  O   . HIS A 1 119 ? -11.804 -0.057  13.653  1.00  7.84  ? 119 HIS A O   1 
ATOM   957  C  CB  . HIS A 1 119 ? -10.075 -1.352  15.608  1.00  7.90  ? 119 HIS A CB  1 
ATOM   958  C  CG  . HIS A 1 119 ? -9.389  -2.362  16.543  1.00  7.88  ? 119 HIS A CG  1 
ATOM   959  N  ND1 . HIS A 1 119 ? -8.053  -2.605  16.540  1.00  8.54  ? 119 HIS A ND1 1 
ATOM   960  C  CD2 . HIS A 1 119 ? -9.907  -3.184  17.506  1.00  9.06  ? 119 HIS A CD2 1 
ATOM   961  C  CE1 . HIS A 1 119 ? -7.736  -3.498  17.490  1.00  8.22  ? 119 HIS A CE1 1 
ATOM   962  N  NE2 . HIS A 1 119 ? -8.849  -3.928  18.009  1.00  8.00  ? 119 HIS A NE2 1 
ATOM   963  N  N   . LEU A 1 120 ? -13.191 0.237   15.454  1.00  8.94  ? 120 LEU A N   1 
ATOM   964  C  CA  . LEU A 1 120 ? -13.801 1.467   14.938  1.00  9.89  ? 120 LEU A CA  1 
ATOM   965  C  C   . LEU A 1 120 ? -13.236 2.631   15.771  1.00  9.09  ? 120 LEU A C   1 
ATOM   966  O  O   . LEU A 1 120 ? -13.419 2.653   16.990  1.00  9.69  ? 120 LEU A O   1 
ATOM   967  C  CB  . LEU A 1 120 ? -15.275 1.378   15.100  1.00  10.14 ? 120 LEU A CB  1 
ATOM   968  C  CG  . LEU A 1 120 ? -15.915 0.300   14.212  1.00  11.66 ? 120 LEU A CG  1 
ATOM   969  C  CD1 . LEU A 1 120 ? -16.701 -0.578  15.157  1.00  12.85 ? 120 LEU A CD1 1 
ATOM   970  C  CD2 . LEU A 1 120 ? -16.842 1.043   13.275  1.00  11.87 ? 120 LEU A CD2 1 
ATOM   971  N  N   . VAL A 1 121 ? -12.521 3.513   15.104  1.00  10.78 ? 121 VAL A N   1 
ATOM   972  C  CA  . VAL A 1 121 ? -11.569 4.454   15.762  1.00  9.80  ? 121 VAL A CA  1 
ATOM   973  C  C   . VAL A 1 121 ? -12.289 5.811   15.798  1.00  10.43 ? 121 VAL A C   1 
ATOM   974  O  O   . VAL A 1 121 ? -12.683 6.281   14.727  1.00  9.24  ? 121 VAL A O   1 
ATOM   975  C  CB  . VAL A 1 121 ? -10.248 4.630   14.971  1.00  10.40 ? 121 VAL A CB  1 
ATOM   976  C  CG1 . VAL A 1 121 ? -9.335  5.691   15.617  1.00  10.05 ? 121 VAL A CG1 1 
ATOM   977  C  CG2 . VAL A 1 121 ? -9.449  3.317   14.848  1.00  9.02  ? 121 VAL A CG2 1 
ATOM   978  N  N   . HIS A 1 122 ? -12.424 6.421   16.987  1.00  9.33  ? 122 HIS A N   1 
ATOM   979  C  CA  . HIS A 1 122 ? -13.175 7.699   17.093  1.00  10.71 ? 122 HIS A CA  1 
ATOM   980  C  C   . HIS A 1 122 ? -12.351 8.693   17.856  1.00  11.79 ? 122 HIS A C   1 
ATOM   981  O  O   . HIS A 1 122 ? -11.582 8.309   18.735  1.00  11.56 ? 122 HIS A O   1 
ATOM   982  C  CB  . HIS A 1 122 ? -14.464 7.551   17.843  1.00  11.91 ? 122 HIS A CB  1 
ATOM   983  C  CG  . HIS A 1 122 ? -15.277 6.358   17.474  1.00  11.14 ? 122 HIS A CG  1 
ATOM   984  N  ND1 . HIS A 1 122 ? -14.864 5.054   17.700  1.00  10.79 ? 122 HIS A ND1 1 
ATOM   985  C  CD2 . HIS A 1 122 ? -16.577 6.287   16.947  1.00  11.83 ? 122 HIS A CD2 1 
ATOM   986  C  CE1 . HIS A 1 122 ? -15.861 4.227   17.293  1.00  11.85 ? 122 HIS A CE1 1 
ATOM   987  N  NE2 . HIS A 1 122 ? -16.900 4.967   16.847  1.00  11.53 ? 122 HIS A NE2 1 
ATOM   988  N  N   . TRP A 1 123 ? -12.478 9.996   17.537  1.00  11.50 ? 123 TRP A N   1 
ATOM   989  C  CA  . TRP A 1 123 ? -11.641 10.983  18.275  1.00  10.94 ? 123 TRP A CA  1 
ATOM   990  C  C   . TRP A 1 123 ? -12.480 12.013  18.997  1.00  11.42 ? 123 TRP A C   1 
ATOM   991  O  O   . TRP A 1 123 ? -13.581 12.359  18.520  1.00  10.97 ? 123 TRP A O   1 
ATOM   992  C  CB  . TRP A 1 123 ? -10.651 11.631  17.357  1.00  11.64 ? 123 TRP A CB  1 
ATOM   993  C  CG  . TRP A 1 123 ? -11.262 12.276  16.127  1.00  12.30 ? 123 TRP A CG  1 
ATOM   994  C  CD1 . TRP A 1 123 ? -11.474 11.705  14.843  1.00  12.72 ? 123 TRP A CD1 1 
ATOM   995  C  CD2 . TRP A 1 123 ? -11.708 13.682  16.019  1.00  13.26 ? 123 TRP A CD2 1 
ATOM   996  N  NE1 . TRP A 1 123 ? -12.053 12.647  13.984  1.00  12.98 ? 123 TRP A NE1 1 
ATOM   997  C  CE2 . TRP A 1 123 ? -12.216 13.857  14.647  1.00  12.72 ? 123 TRP A CE2 1 
ATOM   998  C  CE3 . TRP A 1 123 ? -11.742 14.758  16.907  1.00  13.32 ? 123 TRP A CE3 1 
ATOM   999  C  CZ2 . TRP A 1 123 ? -12.696 15.088  14.188  1.00  13.83 ? 123 TRP A CZ2 1 
ATOM   1000 C  CZ3 . TRP A 1 123 ? -12.265 15.980  16.432  1.00  13.45 ? 123 TRP A CZ3 1 
ATOM   1001 C  CH2 . TRP A 1 123 ? -12.688 16.125  15.088  1.00  14.18 ? 123 TRP A CH2 1 
ATOM   1002 N  N   . ASN A 1 124 ? -11.970 12.485  20.139  1.00  11.86 ? 124 ASN A N   1 
ATOM   1003 C  CA  . ASN A 1 124 ? -12.716 13.320  21.075  1.00  12.74 ? 124 ASN A CA  1 
ATOM   1004 C  C   . ASN A 1 124 ? -12.869 14.725  20.419  1.00  13.85 ? 124 ASN A C   1 
ATOM   1005 O  O   . ASN A 1 124 ? -11.870 15.404  20.195  1.00  13.69 ? 124 ASN A O   1 
ATOM   1006 C  CB  . ASN A 1 124 ? -11.898 13.352  22.351  1.00  14.08 ? 124 ASN A CB  1 
ATOM   1007 C  CG  . ASN A 1 124 ? -12.625 13.988  23.512  1.00  13.97 ? 124 ASN A CG  1 
ATOM   1008 O  OD1 . ASN A 1 124 ? -13.344 14.934  23.329  1.00  15.29 ? 124 ASN A OD1 1 
ATOM   1009 N  ND2 . ASN A 1 124 ? -12.476 13.404  24.705  1.00  15.00 ? 124 ASN A ND2 1 
ATOM   1010 N  N   . THR A 1 125 ? -14.103 15.106  20.041  1.00  14.97 ? 125 THR A N   1 
ATOM   1011 C  CA  . THR A 1 125 ? -14.413 16.387  19.337  1.00  15.18 ? 125 THR A CA  1 
ATOM   1012 C  C   . THR A 1 125 ? -13.926 17.562  20.165  1.00  16.27 ? 125 THR A C   1 
ATOM   1013 O  O   . THR A 1 125 ? -13.635 18.629  19.628  1.00  16.72 ? 125 THR A O   1 
ATOM   1014 C  CB  . THR A 1 125 ? -15.922 16.531  19.097  1.00  16.53 ? 125 THR A CB  1 
ATOM   1015 O  OG1 . THR A 1 125 ? -16.593 16.496  20.364  1.00  16.42 ? 125 THR A OG1 1 
ATOM   1016 C  CG2 . THR A 1 125 ? -16.436 15.394  18.247  1.00  18.60 ? 125 THR A CG2 1 
ATOM   1017 N  N   . LYS A 1 126 ? -13.632 17.536  21.549  1.00  14.01 ? 127 LYS A N   1 
ATOM   1018 C  CA  . LYS A 1 126 ? -13.054 18.702  22.186  1.00  17.00 ? 127 LYS A CA  1 
ATOM   1019 C  C   . LYS A 1 126 ? -11.617 19.051  21.750  1.00  18.36 ? 127 LYS A C   1 
ATOM   1020 O  O   . LYS A 1 126 ? -11.168 20.164  22.068  1.00  17.44 ? 127 LYS A O   1 
ATOM   1021 C  CB  . LYS A 1 126 ? -13.148 18.531  23.691  1.00  19.46 ? 127 LYS A CB  1 
ATOM   1022 C  CG  . LYS A 1 126 ? -12.110 17.647  24.326  1.00  19.83 ? 127 LYS A CG  1 
ATOM   1023 C  CD  . LYS A 1 126 ? -12.380 17.617  25.845  1.00  26.05 ? 127 LYS A CD  1 
ATOM   1024 C  CE  . LYS A 1 126 ? -11.633 16.508  26.573  1.00  27.65 ? 127 LYS A CE  1 
ATOM   1025 N  NZ  . LYS A 1 126 ? -11.570 16.717  28.070  1.00  37.37 ? 127 LYS A NZ  1 
ATOM   1026 N  N   . TYR A 1 127 ? -10.909 18.141  21.049  1.00  15.27 ? 128 TYR A N   1 
ATOM   1027 C  CA  . TYR A 1 127 ? -9.557  18.395  20.543  1.00  15.75 ? 128 TYR A CA  1 
ATOM   1028 C  C   . TYR A 1 127 ? -9.477  18.826  19.109  1.00  15.28 ? 128 TYR A C   1 
ATOM   1029 O  O   . TYR A 1 127 ? -8.377  19.023  18.585  1.00  16.10 ? 128 TYR A O   1 
ATOM   1030 C  CB  . TYR A 1 127 ? -8.611  17.191  20.833  1.00  15.02 ? 128 TYR A CB  1 
ATOM   1031 C  CG  . TYR A 1 127 ? -8.547  16.914  22.328  1.00  13.90 ? 128 TYR A CG  1 
ATOM   1032 C  CD1 . TYR A 1 127 ? -8.189  17.928  23.241  1.00  14.40 ? 128 TYR A CD1 1 
ATOM   1033 C  CD2 . TYR A 1 127 ? -8.792  15.656  22.837  1.00  13.42 ? 128 TYR A CD2 1 
ATOM   1034 C  CE1 . TYR A 1 127 ? -8.121  17.682  24.619  1.00  14.65 ? 128 TYR A CE1 1 
ATOM   1035 C  CE2 . TYR A 1 127 ? -8.734  15.412  24.168  1.00  14.84 ? 128 TYR A CE2 1 
ATOM   1036 C  CZ  . TYR A 1 127 ? -8.358  16.430  25.069  1.00  15.06 ? 128 TYR A CZ  1 
ATOM   1037 O  OH  . TYR A 1 127 ? -8.300  16.120  26.428  1.00  16.20 ? 128 TYR A OH  1 
ATOM   1038 N  N   . GLY A 1 128 ? -10.636 18.937  18.457  1.00  15.31 ? 129 GLY A N   1 
ATOM   1039 C  CA  . GLY A 1 128 ? -10.760 19.695  17.203  1.00  17.13 ? 129 GLY A CA  1 
ATOM   1040 C  C   . GLY A 1 128 ? -10.386 18.825  16.016  1.00  17.53 ? 129 GLY A C   1 
ATOM   1041 O  O   . GLY A 1 128 ? -11.013 18.919  14.962  1.00  17.37 ? 129 GLY A O   1 
ATOM   1042 N  N   . ASP A 1 129 ? -9.295  18.069  16.098  1.00  18.19 ? 130 ASP A N   1 
ATOM   1043 C  CA  . ASP A 1 129 ? -9.118  17.062  15.044  1.00  18.37 ? 130 ASP A CA  1 
ATOM   1044 C  C   . ASP A 1 129 ? -8.400  15.843  15.531  1.00  18.03 ? 130 ASP A C   1 
ATOM   1045 O  O   . ASP A 1 129 ? -7.947  15.813  16.664  1.00  16.98 ? 130 ASP A O   1 
ATOM   1046 C  CB  . ASP A 1 129 ? -8.442  17.599  13.797  1.00  21.19 ? 130 ASP A CB  1 
ATOM   1047 C  CG  . ASP A 1 129 ? -7.087  18.094  14.035  1.00  22.50 ? 130 ASP A CG  1 
ATOM   1048 O  OD1 . ASP A 1 129 ? -6.467  17.870  15.080  1.00  24.25 ? 130 ASP A OD1 1 
ATOM   1049 O  OD2 . ASP A 1 129 ? -6.563  18.685  13.096  1.00  24.72 ? 130 ASP A OD2 1 
ATOM   1050 N  N   . PHE A 1 130 ? -8.323  14.836  14.666  1.00  16.79 ? 131 PHE A N   1 
ATOM   1051 C  CA  . PHE A 1 130 ? -7.698  13.598  15.049  1.00  17.33 ? 131 PHE A CA  1 
ATOM   1052 C  C   . PHE A 1 130 ? -6.207  13.799  15.411  1.00  16.25 ? 131 PHE A C   1 
ATOM   1053 O  O   . PHE A 1 130 ? -5.700  13.189  16.347  1.00  13.07 ? 131 PHE A O   1 
ATOM   1054 C  CB  . PHE A 1 130 ? -7.853  12.601  13.887  1.00  17.13 ? 131 PHE A CB  1 
ATOM   1055 C  CG  . PHE A 1 130 ? -7.174  11.325  14.134  1.00  19.10 ? 131 PHE A CG  1 
ATOM   1056 C  CD1 . PHE A 1 130 ? -7.839  10.295  14.820  1.00  20.31 ? 131 PHE A CD1 1 
ATOM   1057 C  CD2 . PHE A 1 130 ? -5.835  11.169  13.807  1.00  21.22 ? 131 PHE A CD2 1 
ATOM   1058 C  CE1 . PHE A 1 130 ? -7.196  9.113   15.116  1.00  21.98 ? 131 PHE A CE1 1 
ATOM   1059 C  CE2 . PHE A 1 130 ? -5.187  9.979   14.097  1.00  22.97 ? 131 PHE A CE2 1 
ATOM   1060 C  CZ  . PHE A 1 130 ? -5.872  8.950   14.744  1.00  23.04 ? 131 PHE A CZ  1 
ATOM   1061 N  N   . GLY A 1 131 ? -5.476  14.609  14.642  1.00  14.89 ? 132 GLY A N   1 
ATOM   1062 C  CA  . GLY A 1 131 ? -4.036  14.748  14.955  1.00  16.02 ? 132 GLY A CA  1 
ATOM   1063 C  C   . GLY A 1 131 ? -3.789  15.328  16.341  1.00  15.76 ? 132 GLY A C   1 
ATOM   1064 O  O   . GLY A 1 131 ? -2.887  14.959  17.035  1.00  17.04 ? 132 GLY A O   1 
ATOM   1065 N  N   . LYS A 1 132 ? -4.603  16.280  16.741  1.00  16.21 ? 133 LYS A N   1 
ATOM   1066 C  CA  . LYS A 1 132 ? -4.443  16.819  18.075  1.00  15.30 ? 133 LYS A CA  1 
ATOM   1067 C  C   . LYS A 1 132 ? -4.952  15.859  19.190  1.00  15.19 ? 133 LYS A C   1 
ATOM   1068 O  O   . LYS A 1 132 ? -4.347  15.768  20.236  1.00  13.69 ? 133 LYS A O   1 
ATOM   1069 C  CB  . LYS A 1 132 ? -5.039  18.232  18.115  1.00  16.41 ? 133 LYS A CB  1 
ATOM   1070 C  CG  . LYS A 1 132 ? -4.209  19.288  17.294  1.00  18.59 ? 133 LYS A CG  1 
ATOM   1071 C  CD  . LYS A 1 132 ? -2.931  19.660  18.034  0.010 17.75 ? 133 LYS A CD  1 
ATOM   1072 C  CE  . LYS A 1 132 ? -1.823  20.057  17.075  0.010 17.87 ? 133 LYS A CE  1 
ATOM   1073 N  NZ  . LYS A 1 132 ? -0.555  20.371  17.790  0.010 17.83 ? 133 LYS A NZ  1 
ATOM   1074 N  N   . ALA A 1 133 ? -6.057  15.157  18.934  1.00  13.91 ? 134 ALA A N   1 
ATOM   1075 C  CA  . ALA A 1 133 ? -6.609  14.185  19.859  1.00  14.03 ? 134 ALA A CA  1 
ATOM   1076 C  C   . ALA A 1 133 ? -5.577  13.080  20.235  1.00  11.84 ? 134 ALA A C   1 
ATOM   1077 O  O   . ALA A 1 133 ? -5.534  12.601  21.420  1.00  11.36 ? 134 ALA A O   1 
ATOM   1078 C  CB  . ALA A 1 133 ? -7.833  13.541  19.236  1.00  11.66 ? 134 ALA A CB  1 
ATOM   1079 N  N   . VAL A 1 134 ? -4.829  12.572  19.259  1.00  12.31 ? 135 VAL A N   1 
ATOM   1080 C  CA  . VAL A 1 134 ? -3.864  11.480  19.600  1.00  14.12 ? 135 VAL A CA  1 
ATOM   1081 C  C   . VAL A 1 134 ? -2.765  11.940  20.556  1.00  15.46 ? 135 VAL A C   1 
ATOM   1082 O  O   . VAL A 1 134 ? -2.051  11.138  21.156  1.00  16.79 ? 135 VAL A O   1 
ATOM   1083 C  CB  . VAL A 1 134 ? -3.179  10.701  18.401  1.00  15.18 ? 135 VAL A CB  1 
ATOM   1084 C  CG1 . VAL A 1 134 ? -4.228  9.979   17.632  1.00  16.15 ? 135 VAL A CG1 1 
ATOM   1085 C  CG2 . VAL A 1 134 ? -2.285  11.568  17.472  1.00  15.85 ? 135 VAL A CG2 1 
ATOM   1086 N  N   . GLN A 1 135 ? -2.634  13.244  20.763  1.00  16.67 ? 136 GLN A N   1 
ATOM   1087 C  CA  . GLN A 1 135 ? -1.624  13.688  21.686  1.00  17.17 ? 136 GLN A CA  1 
ATOM   1088 C  C   . GLN A 1 135 ? -2.179  13.790  23.120  1.00  19.19 ? 136 GLN A C   1 
ATOM   1089 O  O   . GLN A 1 135 ? -1.496  14.279  24.039  1.00  20.07 ? 136 GLN A O   1 
ATOM   1090 C  CB  . GLN A 1 135 ? -1.096  15.041  21.210  1.00  20.64 ? 136 GLN A CB  1 
ATOM   1091 C  CG  . GLN A 1 135 ? -0.302  14.962  19.946  1.00  25.79 ? 136 GLN A CG  1 
ATOM   1092 C  CD  . GLN A 1 135 ? 0.044   16.348  19.459  1.00  35.00 ? 136 GLN A CD  1 
ATOM   1093 O  OE1 . GLN A 1 135 ? 0.641   17.166  20.188  1.00  42.11 ? 136 GLN A OE1 1 
ATOM   1094 N  NE2 . GLN A 1 135 ? -0.360  16.649  18.242  1.00  34.95 ? 136 GLN A NE2 1 
ATOM   1095 N  N   . GLN A 1 136 ? -3.430  13.386  23.329  1.00  15.36 ? 137 GLN A N   1 
ATOM   1096 C  CA  . GLN A 1 136 ? -4.064  13.602  24.623  1.00  15.39 ? 137 GLN A CA  1 
ATOM   1097 C  C   . GLN A 1 136 ? -4.428  12.281  25.239  1.00  14.31 ? 137 GLN A C   1 
ATOM   1098 O  O   . GLN A 1 136 ? -4.702  11.340  24.500  1.00  15.59 ? 137 GLN A O   1 
ATOM   1099 C  CB  . GLN A 1 136 ? -5.346  14.389  24.450  1.00  15.88 ? 137 GLN A CB  1 
ATOM   1100 C  CG  . GLN A 1 136 ? -5.192  15.581  23.529  1.00  17.75 ? 137 GLN A CG  1 
ATOM   1101 C  CD  . GLN A 1 136 ? -4.274  16.635  24.130  1.00  21.30 ? 137 GLN A CD  1 
ATOM   1102 O  OE1 . GLN A 1 136 ? -4.150  16.729  25.345  1.00  19.66 ? 137 GLN A OE1 1 
ATOM   1103 N  NE2 . GLN A 1 136 ? -3.604  17.400  23.268  1.00  22.93 ? 137 GLN A NE2 1 
ATOM   1104 N  N   . PRO A 1 137 ? -4.406  12.180  26.593  1.00  14.06 ? 138 PRO A N   1 
ATOM   1105 C  CA  . PRO A 1 137 ? -4.609  10.870  27.242  1.00  13.81 ? 138 PRO A CA  1 
ATOM   1106 C  C   . PRO A 1 137 ? -6.075  10.395  27.029  1.00  11.99 ? 138 PRO A C   1 
ATOM   1107 O  O   . PRO A 1 137 ? -6.371  9.180   27.128  1.00  12.82 ? 138 PRO A O   1 
ATOM   1108 C  CB  . PRO A 1 137 ? -4.219  11.104  28.714  1.00  14.24 ? 138 PRO A CB  1 
ATOM   1109 C  CG  . PRO A 1 137 ? -4.298  12.601  28.865  1.00  15.57 ? 138 PRO A CG  1 
ATOM   1110 C  CD  . PRO A 1 137 ? -3.977  13.234  27.536  1.00  14.40 ? 138 PRO A CD  1 
ATOM   1111 N  N   . ASP A 1 138 ? -6.996  11.301  26.739  1.00  10.83 ? 139 ASP A N   1 
ATOM   1112 C  CA  . ASP A 1 138 ? -8.379  10.845  26.437  1.00  12.42 ? 139 ASP A CA  1 
ATOM   1113 C  C   . ASP A 1 138 ? -8.790  11.206  25.003  1.00  11.44 ? 139 ASP A C   1 
ATOM   1114 O  O   . ASP A 1 138 ? -9.931  11.615  24.789  1.00  10.95 ? 139 ASP A O   1 
ATOM   1115 C  CB  . ASP A 1 138 ? -9.406  11.481  27.384  1.00  14.15 ? 139 ASP A CB  1 
ATOM   1116 C  CG  . ASP A 1 138 ? -9.287  12.992  27.456  1.00  16.12 ? 139 ASP A CG  1 
ATOM   1117 O  OD1 . ASP A 1 138 ? -8.308  13.596  26.936  1.00  16.10 ? 139 ASP A OD1 1 
ATOM   1118 O  OD2 . ASP A 1 138 ? -10.151 13.585  28.126  1.00  15.63 ? 139 ASP A OD2 1 
ATOM   1119 N  N   . GLY A 1 139 ? -7.842  11.108  24.070  1.00  11.10 ? 140 GLY A N   1 
ATOM   1120 C  CA  . GLY A 1 139 ? -8.007  11.686  22.772  1.00  10.77 ? 140 GLY A CA  1 
ATOM   1121 C  C   . GLY A 1 139 ? -8.863  10.780  21.925  1.00  10.48 ? 140 GLY A C   1 
ATOM   1122 O  O   . GLY A 1 139 ? -9.604  11.263  21.098  1.00  10.01 ? 140 GLY A O   1 
ATOM   1123 N  N   . LEU A 1 140 ? -8.728  9.448   22.112  1.00  9.39  ? 141 LEU A N   1 
ATOM   1124 C  CA  . LEU A 1 140 ? -9.429  8.490   21.221  1.00  9.77  ? 141 LEU A CA  1 
ATOM   1125 C  C   . LEU A 1 140 ? -10.257 7.515   21.991  1.00  9.05  ? 141 LEU A C   1 
ATOM   1126 O  O   . LEU A 1 140 ? -9.962  7.297   23.172  1.00  9.13  ? 141 LEU A O   1 
ATOM   1127 C  CB  . LEU A 1 140 ? -8.396  7.669   20.410  1.00  10.90 ? 141 LEU A CB  1 
ATOM   1128 C  CG  . LEU A 1 140 ? -7.461  8.308   19.407  1.00  13.70 ? 141 LEU A CG  1 
ATOM   1129 C  CD1 . LEU A 1 140 ? -6.817  7.214   18.542  1.00  12.14 ? 141 LEU A CD1 1 
ATOM   1130 C  CD2 . LEU A 1 140 ? -8.036  9.402   18.508  1.00  13.92 ? 141 LEU A CD2 1 
ATOM   1131 N  N   . ALA A 1 141 ? -11.352 7.041   21.373  1.00  9.44  ? 142 ALA A N   1 
ATOM   1132 C  CA  . ALA A 1 141 ? -12.177 5.876   21.900  1.00  8.72  ? 142 ALA A CA  1 
ATOM   1133 C  C   . ALA A 1 141 ? -12.189 4.878   20.718  1.00  9.38  ? 142 ALA A C   1 
ATOM   1134 O  O   . ALA A 1 141 ? -12.575 5.202   19.611  1.00  9.20  ? 142 ALA A O   1 
ATOM   1135 C  CB  . ALA A 1 141 ? -13.583 6.345   22.269  1.00  8.48  ? 142 ALA A CB  1 
ATOM   1136 N  N   . VAL A 1 142 ? -11.673 3.673   20.945  1.00  8.97  ? 143 VAL A N   1 
ATOM   1137 C  CA  . VAL A 1 142 ? -11.709 2.682   19.888  1.00  8.66  ? 143 VAL A CA  1 
ATOM   1138 C  C   . VAL A 1 142 ? -12.652 1.585   20.390  1.00  8.18  ? 143 VAL A C   1 
ATOM   1139 O  O   . VAL A 1 142 ? -12.495 1.095   21.526  1.00  7.64  ? 143 VAL A O   1 
ATOM   1140 C  CB  . VAL A 1 142 ? -10.348 2.066   19.586  1.00  9.23  ? 143 VAL A CB  1 
ATOM   1141 C  CG1 . VAL A 1 142 ? -10.445 1.105   18.379  1.00  9.02  ? 143 VAL A CG1 1 
ATOM   1142 C  CG2 . VAL A 1 142 ? -9.346  3.194   19.177  1.00  9.09  ? 143 VAL A CG2 1 
ATOM   1143 N  N   . LEU A 1 143 ? -13.607 1.242   19.540  1.00  8.07  ? 144 LEU A N   1 
ATOM   1144 C  CA  . LEU A 1 143 ? -14.609 0.196   19.858  1.00  9.13  ? 144 LEU A CA  1 
ATOM   1145 C  C   . LEU A 1 143 ? -14.135 -1.053  19.183  1.00  9.03  ? 144 LEU A C   1 
ATOM   1146 O  O   . LEU A 1 143 ? -13.924 -1.060  17.995  1.00  10.48 ? 144 LEU A O   1 
ATOM   1147 C  CB  . LEU A 1 143 ? -15.985 0.626   19.345  1.00  9.65  ? 144 LEU A CB  1 
ATOM   1148 C  CG  . LEU A 1 143 ? -17.092 -0.399  19.385  1.00  10.64 ? 144 LEU A CG  1 
ATOM   1149 C  CD1 . LEU A 1 143 ? -17.246 -0.732  20.857  1.00  10.34 ? 144 LEU A CD1 1 
ATOM   1150 C  CD2 . LEU A 1 143 ? -18.367 0.161   18.728  1.00  11.15 ? 144 LEU A CD2 1 
ATOM   1151 N  N   . GLY A 1 144 ? -13.853 -2.100  19.949  1.00  9.73  ? 145 GLY A N   1 
ATOM   1152 C  CA  . GLY A 1 144 ? -13.259 -3.307  19.344  1.00  8.23  ? 145 GLY A CA  1 
ATOM   1153 C  C   . GLY A 1 144 ? -14.343 -4.402  19.395  1.00  8.06  ? 145 GLY A C   1 
ATOM   1154 O  O   . GLY A 1 144 ? -15.048 -4.572  20.423  1.00  8.56  ? 145 GLY A O   1 
ATOM   1155 N  N   . ILE A 1 145 ? -14.443 -5.164  18.310  1.00  8.41  ? 146 ILE A N   1 
ATOM   1156 C  CA  . ILE A 1 145 ? -15.485 -6.201  18.148  1.00  8.91  ? 146 ILE A CA  1 
ATOM   1157 C  C   . ILE A 1 145 ? -14.724 -7.442  17.643  1.00  9.07  ? 146 ILE A C   1 
ATOM   1158 O  O   . ILE A 1 145 ? -14.035 -7.418  16.651  1.00  9.56  ? 146 ILE A O   1 
ATOM   1159 C  CB  . ILE A 1 145 ? -16.557 -5.752  17.092  1.00  8.11  ? 146 ILE A CB  1 
ATOM   1160 C  CG1 . ILE A 1 145 ? -17.127 -4.422  17.593  1.00  8.23  ? 146 ILE A CG1 1 
ATOM   1161 C  CG2 . ILE A 1 145 ? -17.664 -6.827  16.917  1.00  8.52  ? 146 ILE A CG2 1 
ATOM   1162 C  CD1 . ILE A 1 145 ? -18.116 -3.741  16.716  1.00  9.33  ? 146 ILE A CD1 1 
ATOM   1163 N  N   . PHE A 1 146 ? -14.861 -8.529  18.348  1.00  10.02 ? 147 PHE A N   1 
ATOM   1164 C  CA  . PHE A 1 146 ? -14.279 -9.816  17.918  1.00  9.15  ? 147 PHE A CA  1 
ATOM   1165 C  C   . PHE A 1 146 ? -15.008 -10.463 16.757  1.00  10.42 ? 147 PHE A C   1 
ATOM   1166 O  O   . PHE A 1 146 ? -16.195 -10.307 16.589  1.00  10.58 ? 147 PHE A O   1 
ATOM   1167 C  CB  . PHE A 1 146 ? -14.362 -10.725 19.171  1.00  8.86  ? 147 PHE A CB  1 
ATOM   1168 C  CG  . PHE A 1 146 ? -13.495 -10.261 20.298  1.00  8.90  ? 147 PHE A CG  1 
ATOM   1169 C  CD1 . PHE A 1 146 ? -12.121 -10.131 20.111  1.00  9.68  ? 147 PHE A CD1 1 
ATOM   1170 C  CD2 . PHE A 1 146 ? -14.016 -10.004 21.576  1.00  10.41 ? 147 PHE A CD2 1 
ATOM   1171 C  CE1 . PHE A 1 146 ? -11.277 -9.744  21.165  1.00  9.45  ? 147 PHE A CE1 1 
ATOM   1172 C  CE2 . PHE A 1 146 ? -13.190 -9.642  22.639  1.00  9.92  ? 147 PHE A CE2 1 
ATOM   1173 C  CZ  . PHE A 1 146 ? -11.825 -9.488  22.418  1.00  9.84  ? 147 PHE A CZ  1 
ATOM   1174 N  N   . LEU A 1 147 ? -14.286 -11.158 15.900  1.00  9.90  ? 148 LEU A N   1 
ATOM   1175 C  CA  . LEU A 1 147 ? -14.914 -11.888 14.852  1.00  10.33 ? 148 LEU A CA  1 
ATOM   1176 C  C   . LEU A 1 147 ? -14.585 -13.357 15.104  1.00  10.40 ? 148 LEU A C   1 
ATOM   1177 O  O   . LEU A 1 147 ? -13.398 -13.672 15.329  1.00  9.61  ? 148 LEU A O   1 
ATOM   1178 C  CB  . LEU A 1 147 ? -14.315 -11.507 13.480  1.00  9.40  ? 148 LEU A CB  1 
ATOM   1179 C  CG  . LEU A 1 147 ? -14.915 -10.231 12.799  1.00  9.85  ? 148 LEU A CG  1 
ATOM   1180 C  CD1 . LEU A 1 147 ? -14.643 -8.975  13.649  1.00  10.18 ? 148 LEU A CD1 1 
ATOM   1181 C  CD2 . LEU A 1 147 ? -14.386 -10.044 11.392  1.00  11.58 ? 148 LEU A CD2 1 
ATOM   1182 N  N   . LYS A 1 148 ? -15.617 -14.202 15.058  1.00  12.06 ? 149 LYS A N   1 
ATOM   1183 C  CA  . LYS A 1 148 ? -15.362 -15.620 14.990  1.00  13.55 ? 149 LYS A CA  1 
ATOM   1184 C  C   . LYS A 1 148 ? -15.898 -16.164 13.673  1.00  13.68 ? 149 LYS A C   1 
ATOM   1185 O  O   . LYS A 1 148 ? -16.798 -15.596 13.029  1.00  13.56 ? 149 LYS A O   1 
ATOM   1186 C  CB  . LYS A 1 148 ? -16.040 -16.347 16.123  1.00  16.42 ? 149 LYS A CB  1 
ATOM   1187 C  CG  . LYS A 1 148 ? -17.561 -16.294 16.097  1.00  18.53 ? 149 LYS A CG  1 
ATOM   1188 C  CD  . LYS A 1 148 ? -18.056 -17.093 17.296  1.00  22.99 ? 149 LYS A CD  1 
ATOM   1189 C  CE  . LYS A 1 148 ? -19.559 -17.140 17.346  1.00  27.29 ? 149 LYS A CE  1 
ATOM   1190 N  NZ  . LYS A 1 148 ? -19.884 -18.263 18.288  1.00  32.89 ? 149 LYS A NZ  1 
ATOM   1191 N  N   . VAL A 1 149 ? -15.387 -17.328 13.286  1.00  14.35 ? 150 VAL A N   1 
ATOM   1192 C  CA  . VAL A 1 149 ? -15.814 -17.889 12.029  1.00  13.42 ? 150 VAL A CA  1 
ATOM   1193 C  C   . VAL A 1 149 ? -17.026 -18.815 12.240  1.00  15.03 ? 150 VAL A C   1 
ATOM   1194 O  O   . VAL A 1 149 ? -17.000 -19.693 13.143  1.00  14.34 ? 150 VAL A O   1 
ATOM   1195 C  CB  . VAL A 1 149 ? -14.666 -18.657 11.432  1.00  13.26 ? 150 VAL A CB  1 
ATOM   1196 C  CG1 . VAL A 1 149 ? -15.111 -19.367 10.138  1.00  12.09 ? 150 VAL A CG1 1 
ATOM   1197 C  CG2 . VAL A 1 149 ? -13.519 -17.691 11.194  1.00  14.33 ? 150 VAL A CG2 1 
ATOM   1198 N  N   . GLY A 1 150 ? -18.039 -18.631 11.421  1.00  14.88 ? 151 GLY A N   1 
ATOM   1199 C  CA  . GLY A 1 150 ? -19.262 -19.456 11.423  1.00  17.00 ? 151 GLY A CA  1 
ATOM   1200 C  C   . GLY A 1 150 ? -20.202 -19.001 10.324  1.00  16.20 ? 151 GLY A C   1 
ATOM   1201 O  O   . GLY A 1 150 ? -19.883 -19.121 9.131   1.00  17.81 ? 151 GLY A O   1 
ATOM   1202 N  N   . SER A 1 151 ? -21.353 -18.449 10.694  1.00  16.50 ? 152 SER A N   1 
ATOM   1203 C  CA  . SER A 1 151 ? -22.201 -17.894 9.606   1.00  19.45 ? 152 SER A CA  1 
ATOM   1204 C  C   . SER A 1 151 ? -21.655 -16.549 9.052   1.00  18.08 ? 152 SER A C   1 
ATOM   1205 O  O   . SER A 1 151 ? -20.853 -15.862 9.737   1.00  16.17 ? 152 SER A O   1 
ATOM   1206 C  CB  . SER A 1 151 ? -23.654 -17.811 10.028  1.00  23.03 ? 152 SER A CB  1 
ATOM   1207 O  OG  . SER A 1 151 ? -23.798 -16.890 11.083  1.00  32.05 ? 152 SER A OG  1 
ATOM   1208 N  N   . ALA A 1 152 ? -22.002 -16.232 7.789   1.00  14.84 ? 153 ALA A N   1 
ATOM   1209 C  CA  . ALA A 1 152 ? -21.549 -15.012 7.183   1.00  14.28 ? 153 ALA A CA  1 
ATOM   1210 C  C   . ALA A 1 152 ? -22.135 -13.812 7.912   1.00  14.95 ? 153 ALA A C   1 
ATOM   1211 O  O   . ALA A 1 152 ? -23.228 -13.859 8.429   1.00  13.67 ? 153 ALA A O   1 
ATOM   1212 C  CB  . ALA A 1 152 ? -21.884 -14.961 5.701   1.00  13.62 ? 153 ALA A CB  1 
ATOM   1213 N  N   . LYS A 1 153 ? -21.415 -12.702 7.872   1.00  14.44 ? 154 LYS A N   1 
ATOM   1214 C  CA  . LYS A 1 153 ? -21.991 -11.450 8.306   1.00  15.26 ? 154 LYS A CA  1 
ATOM   1215 C  C   . LYS A 1 153 ? -22.437 -10.675 7.078   1.00  14.96 ? 154 LYS A C   1 
ATOM   1216 O  O   . LYS A 1 153 ? -21.606 -10.126 6.386   1.00  15.64 ? 154 LYS A O   1 
ATOM   1217 C  CB  . LYS A 1 153 ? -20.886 -10.667 8.999   1.00  15.28 ? 154 LYS A CB  1 
ATOM   1218 C  CG  . LYS A 1 153 ? -21.329 -9.537  9.902   1.00  17.36 ? 154 LYS A CG  1 
ATOM   1219 C  CD  . LYS A 1 153 ? -22.427 -9.943  10.860  1.00  18.70 ? 154 LYS A CD  1 
ATOM   1220 C  CE  . LYS A 1 153 ? -22.577 -8.860  11.892  1.00  19.57 ? 154 LYS A CE  1 
ATOM   1221 N  NZ  . LYS A 1 153 ? -23.635 -9.165  12.882  1.00  20.49 ? 154 LYS A NZ  1 
ATOM   1222 N  N   . PRO A 1 154 ? -23.764 -10.599 6.817   1.00  16.74 ? 155 PRO A N   1 
ATOM   1223 C  CA  . PRO A 1 154 ? -24.210 -9.936  5.572   1.00  18.04 ? 155 PRO A CA  1 
ATOM   1224 C  C   . PRO A 1 154 ? -23.620 -8.532  5.431   1.00  17.58 ? 155 PRO A C   1 
ATOM   1225 O  O   . PRO A 1 154 ? -23.229 -8.143  4.345   1.00  18.93 ? 155 PRO A O   1 
ATOM   1226 C  CB  . PRO A 1 154 ? -25.762 -9.904  5.731   1.00  18.02 ? 155 PRO A CB  1 
ATOM   1227 C  CG  . PRO A 1 154 ? -26.061 -10.969 6.780   1.00  16.16 ? 155 PRO A CG  1 
ATOM   1228 C  CD  . PRO A 1 154 ? -24.899 -10.910 7.703   1.00  17.61 ? 155 PRO A CD  1 
ATOM   1229 N  N   . GLY A 1 155 ? -23.521 -7.792  6.521   1.00  18.38 ? 156 GLY A N   1 
ATOM   1230 C  CA  . GLY A 1 155 ? -23.133 -6.356  6.424   1.00  19.35 ? 156 GLY A CA  1 
ATOM   1231 C  C   . GLY A 1 155 ? -21.660 -6.116  6.231   1.00  19.45 ? 156 GLY A C   1 
ATOM   1232 O  O   . GLY A 1 155 ? -21.216 -4.972  6.041   1.00  21.75 ? 156 GLY A O   1 
ATOM   1233 N  N   . LEU A 1 156 ? -20.896 -7.204  6.303   1.00  16.41 ? 157 LEU A N   1 
ATOM   1234 C  CA  . LEU A 1 156 ? -19.516 -7.195  5.900   1.00  14.93 ? 157 LEU A CA  1 
ATOM   1235 C  C   . LEU A 1 156 ? -19.254 -7.450  4.428   1.00  13.99 ? 157 LEU A C   1 
ATOM   1236 O  O   . LEU A 1 156 ? -18.125 -7.235  3.943   1.00  15.36 ? 157 LEU A O   1 
ATOM   1237 C  CB  . LEU A 1 156 ? -18.760 -8.219  6.732   1.00  14.15 ? 157 LEU A CB  1 
ATOM   1238 C  CG  . LEU A 1 156 ? -17.231 -8.353  6.580   1.00  13.81 ? 157 LEU A CG  1 
ATOM   1239 C  CD1 . LEU A 1 156 ? -16.539 -7.032  6.962   1.00  11.72 ? 157 LEU A CD1 1 
ATOM   1240 C  CD2 . LEU A 1 156 ? -16.673 -9.552  7.354   1.00  11.46 ? 157 LEU A CD2 1 
ATOM   1241 N  N   . GLN A 1 157 ? -20.232 -7.967  3.691   1.00  16.71 ? 158 GLN A N   1 
ATOM   1242 C  CA  . GLN A 1 157 ? -19.900 -8.459  2.338   1.00  16.43 ? 158 GLN A CA  1 
ATOM   1243 C  C   . GLN A 1 157 ? -19.460 -7.355  1.405   1.00  15.84 ? 158 GLN A C   1 
ATOM   1244 O  O   . GLN A 1 157 ? -18.527 -7.538  0.641   1.00  14.65 ? 158 GLN A O   1 
ATOM   1245 C  CB  . GLN A 1 157 ? -21.023 -9.284  1.749   1.00  18.57 ? 158 GLN A CB  1 
ATOM   1246 C  CG  . GLN A 1 157 ? -20.635 -10.041 0.485   1.00  19.00 ? 158 GLN A CG  1 
ATOM   1247 C  CD  . GLN A 1 157 ? -19.556 -11.083 0.774   1.00  20.16 ? 158 GLN A CD  1 
ATOM   1248 O  OE1 . GLN A 1 157 ? -19.468 -11.647 1.889   1.00  19.08 ? 158 GLN A OE1 1 
ATOM   1249 N  NE2 . GLN A 1 157 ? -18.709 -11.315 -0.207  1.00  19.58 ? 158 GLN A NE2 1 
ATOM   1250 N  N   . LYS A 1 158 ? -20.065 -6.183  1.521   1.00  18.41 ? 159 LYS A N   1 
ATOM   1251 C  CA  . LYS A 1 158 ? -19.645 -5.064  0.691   1.00  18.83 ? 159 LYS A CA  1 
ATOM   1252 C  C   . LYS A 1 158 ? -18.179 -4.790  0.872   1.00  18.31 ? 159 LYS A C   1 
ATOM   1253 O  O   . LYS A 1 158 ? -17.478 -4.525  -0.114  1.00  17.65 ? 159 LYS A O   1 
ATOM   1254 C  CB  . LYS A 1 158 ? -20.503 -3.803  0.957   1.00  23.25 ? 159 LYS A CB  1 
ATOM   1255 C  CG  . LYS A 1 158 ? -21.952 -4.003  0.476   1.00  32.09 ? 159 LYS A CG  1 
ATOM   1256 C  CD  . LYS A 1 158 ? -22.902 -2.866  0.862   1.00  39.70 ? 159 LYS A CD  1 
ATOM   1257 C  CE  . LYS A 1 158 ? -24.293 -3.058  0.233   1.00  46.39 ? 159 LYS A CE  1 
ATOM   1258 N  NZ  . LYS A 1 158 ? -25.066 -1.773  0.056   1.00  47.83 ? 159 LYS A NZ  1 
ATOM   1259 N  N   . VAL A 1 159 ? -17.679 -4.879  2.120   1.00  17.23 ? 160 VAL A N   1 
ATOM   1260 C  CA  . VAL A 1 159 ? -16.220 -4.725  2.372   1.00  15.93 ? 160 VAL A CA  1 
ATOM   1261 C  C   . VAL A 1 159 ? -15.441 -5.843  1.670   1.00  16.18 ? 160 VAL A C   1 
ATOM   1262 O  O   . VAL A 1 159 ? -14.486 -5.616  0.956   1.00  16.12 ? 160 VAL A O   1 
ATOM   1263 C  CB  . VAL A 1 159 ? -15.896 -4.711  3.874   1.00  14.45 ? 160 VAL A CB  1 
ATOM   1264 C  CG1 . VAL A 1 159 ? -14.388 -4.883  4.103   1.00  16.08 ? 160 VAL A CG1 1 
ATOM   1265 C  CG2 . VAL A 1 159 ? -16.418 -3.401  4.471   1.00  14.37 ? 160 VAL A CG2 1 
ATOM   1266 N  N   . VAL A 1 160 ? -15.855 -7.064  1.902   1.00  14.31 ? 161 VAL A N   1 
ATOM   1267 C  CA  . VAL A 1 160 ? -15.113 -8.178  1.370   1.00  16.49 ? 161 VAL A CA  1 
ATOM   1268 C  C   . VAL A 1 160 ? -15.046 -8.113  -0.168  1.00  16.54 ? 161 VAL A C   1 
ATOM   1269 O  O   . VAL A 1 160 ? -14.029 -8.335  -0.733  1.00  16.87 ? 161 VAL A O   1 
ATOM   1270 C  CB  . VAL A 1 160 ? -15.773 -9.470  1.843   1.00  16.37 ? 161 VAL A CB  1 
ATOM   1271 C  CG1 . VAL A 1 160 ? -15.369 -10.654 0.973   1.00  19.42 ? 161 VAL A CG1 1 
ATOM   1272 C  CG2 . VAL A 1 160 ? -15.470 -9.676  3.301   1.00  16.75 ? 161 VAL A CG2 1 
ATOM   1273 N  N   . ASP A 1 161 ? -16.146 -7.769  -0.812  1.00  20.53 ? 162 ASP A N   1 
ATOM   1274 C  CA  . ASP A 1 161 ? -16.153 -7.761  -2.290  1.00  24.20 ? 162 ASP A CA  1 
ATOM   1275 C  C   . ASP A 1 161 ? -15.239 -6.739  -2.951  1.00  25.30 ? 162 ASP A C   1 
ATOM   1276 O  O   . ASP A 1 161 ? -14.828 -6.927  -4.091  1.00  28.93 ? 162 ASP A O   1 
ATOM   1277 C  CB  . ASP A 1 161 ? -17.550 -7.639  -2.825  1.00  28.46 ? 162 ASP A CB  1 
ATOM   1278 C  CG  . ASP A 1 161 ? -18.285 -8.967  -2.792  1.00  31.59 ? 162 ASP A CG  1 
ATOM   1279 O  OD1 . ASP A 1 161 ? -17.630 -10.010 -2.988  1.00  32.53 ? 162 ASP A OD1 1 
ATOM   1280 O  OD2 . ASP A 1 161 ? -19.507 -8.960  -2.527  1.00  34.05 ? 162 ASP A OD2 1 
ATOM   1281 N  N   . VAL A 1 162 ? -14.926 -5.661  -2.248  1.00  21.98 ? 163 VAL A N   1 
ATOM   1282 C  CA  . VAL A 1 162 ? -14.135 -4.601  -2.862  1.00  21.80 ? 163 VAL A CA  1 
ATOM   1283 C  C   . VAL A 1 162 ? -12.663 -4.872  -2.664  1.00  18.21 ? 163 VAL A C   1 
ATOM   1284 O  O   . VAL A 1 162 ? -11.825 -4.209  -3.258  1.00  18.42 ? 163 VAL A O   1 
ATOM   1285 C  CB  . VAL A 1 162 ? -14.604 -3.207  -2.304  1.00  22.33 ? 163 VAL A CB  1 
ATOM   1286 C  CG1 . VAL A 1 162 ? -13.947 -2.879  -0.988  1.00  22.27 ? 163 VAL A CG1 1 
ATOM   1287 C  CG2 . VAL A 1 162 ? -14.407 -2.077  -3.307  1.00  23.57 ? 163 VAL A CG2 1 
ATOM   1288 N  N   . LEU A 1 163 ? -12.292 -5.843  -1.805  1.00  18.72 ? 164 LEU A N   1 
ATOM   1289 C  CA  . LEU A 1 163 ? -10.858 -6.101  -1.494  1.00  17.53 ? 164 LEU A CA  1 
ATOM   1290 C  C   . LEU A 1 163 ? -9.948  -6.434  -2.677  1.00  18.92 ? 164 LEU A C   1 
ATOM   1291 O  O   . LEU A 1 163 ? -8.751  -6.098  -2.672  1.00  16.20 ? 164 LEU A O   1 
ATOM   1292 C  CB  . LEU A 1 163 ? -10.672 -7.189  -0.391  1.00  17.13 ? 164 LEU A CB  1 
ATOM   1293 C  CG  . LEU A 1 163 ? -11.265 -6.865  0.999   1.00  16.10 ? 164 LEU A CG  1 
ATOM   1294 C  CD1 . LEU A 1 163 ? -11.008 -8.027  1.974   1.00  14.53 ? 164 LEU A CD1 1 
ATOM   1295 C  CD2 . LEU A 1 163 ? -10.665 -5.565  1.503   1.00  14.14 ? 164 LEU A CD2 1 
ATOM   1296 N  N   . ASP A 1 164 ? -10.514 -7.132  -3.666  1.00  21.87 ? 165 ASP A N   1 
ATOM   1297 C  CA  . ASP A 1 164 ? -9.763  -7.543  -4.843  1.00  26.76 ? 165 ASP A CA  1 
ATOM   1298 C  C   . ASP A 1 164 ? -9.210  -6.293  -5.585  1.00  27.16 ? 165 ASP A C   1 
ATOM   1299 O  O   . ASP A 1 164 ? -8.166  -6.362  -6.242  1.00  24.14 ? 165 ASP A O   1 
ATOM   1300 C  CB  . ASP A 1 164 ? -10.663 -8.373  -5.775  1.00  30.21 ? 165 ASP A CB  1 
ATOM   1301 C  CG  . ASP A 1 164 ? -11.631 -7.503  -6.623  1.00  38.17 ? 165 ASP A CG  1 
ATOM   1302 O  OD1 . ASP A 1 164 ? -12.721 -7.028  -6.145  1.00  39.25 ? 165 ASP A OD1 1 
ATOM   1303 O  OD2 . ASP A 1 164 ? -11.314 -7.307  -7.820  1.00  39.60 ? 165 ASP A OD2 1 
ATOM   1304 N  N   . SER A 1 165 ? -9.928  -5.178  -5.452  1.00  24.28 ? 166 SER A N   1 
ATOM   1305 C  CA  . SER A 1 165 ? -9.548  -3.905  -6.080  1.00  23.13 ? 166 SER A CA  1 
ATOM   1306 C  C   . SER A 1 165 ? -8.483  -3.107  -5.275  1.00  25.41 ? 166 SER A C   1 
ATOM   1307 O  O   . SER A 1 165 ? -7.903  -2.117  -5.788  1.00  21.36 ? 166 SER A O   1 
ATOM   1308 C  CB  . SER A 1 165 ? -10.810 -3.080  -6.276  1.00  26.84 ? 166 SER A CB  1 
ATOM   1309 O  OG  . SER A 1 165 ? -11.227 -2.448  -5.068  1.00  28.21 ? 166 SER A OG  1 
ATOM   1310 N  N   . ILE A 1 166 ? -8.186  -3.522  -4.020  1.00  19.12 ? 167 ILE A N   1 
ATOM   1311 C  CA  . ILE A 1 166 ? -7.100  -2.858  -3.259  1.00  19.75 ? 167 ILE A CA  1 
ATOM   1312 C  C   . ILE A 1 166 ? -6.101  -3.925  -2.765  1.00  19.91 ? 167 ILE A C   1 
ATOM   1313 O  O   . ILE A 1 166 ? -5.761  -4.029  -1.568  1.00  16.34 ? 167 ILE A O   1 
ATOM   1314 C  CB  . ILE A 1 166 ? -7.713  -2.013  -2.100  1.00  18.36 ? 167 ILE A CB  1 
ATOM   1315 C  CG1 . ILE A 1 166 ? -8.594  -2.898  -1.235  1.00  17.23 ? 167 ILE A CG1 1 
ATOM   1316 C  CG2 . ILE A 1 166 ? -8.592  -0.930  -2.662  1.00  15.48 ? 167 ILE A CG2 1 
ATOM   1317 C  CD1 . ILE A 1 166 ? -8.755  -2.449  0.206   1.00  16.94 ? 167 ILE A CD1 1 
ATOM   1318 N  N   . LYS A 1 167 ? -5.707  -4.813  -3.673  1.00  20.27 ? 168 LYS A N   1 
ATOM   1319 C  CA  . LYS A 1 167 ? -4.905  -5.952  -3.216  1.00  21.79 ? 168 LYS A CA  1 
ATOM   1320 C  C   . LYS A 1 167 ? -3.533  -5.625  -2.566  1.00  22.38 ? 168 LYS A C   1 
ATOM   1321 O  O   . LYS A 1 167 ? -3.101  -6.335  -1.638  1.00  18.36 ? 168 LYS A O   1 
ATOM   1322 C  CB  . LYS A 1 167 ? -4.729  -6.977  -4.335  1.00  21.33 ? 168 LYS A CB  1 
ATOM   1323 C  CG  . LYS A 1 167 ? -3.798  -8.150  -4.000  1.00  22.99 ? 168 LYS A CG  1 
ATOM   1324 C  CD  . LYS A 1 167 ? -3.429  -8.926  -5.277  1.00  25.42 ? 168 LYS A CD  1 
ATOM   1325 C  CE  . LYS A 1 167 ? -3.097  -10.369 -4.937  1.00  30.20 ? 168 LYS A CE  1 
ATOM   1326 N  NZ  . LYS A 1 167 ? -2.940  -11.196 -6.195  1.00  37.06 ? 168 LYS A NZ  1 
ATOM   1327 N  N   . THR A 1 168 ? -2.861  -4.565  -3.055  1.00  17.52 ? 169 THR A N   1 
ATOM   1328 C  CA  . THR A 1 168 ? -1.487  -4.337  -2.703  1.00  19.80 ? 169 THR A CA  1 
ATOM   1329 C  C   . THR A 1 168 ? -1.372  -2.957  -2.076  1.00  17.31 ? 169 THR A C   1 
ATOM   1330 O  O   . THR A 1 168 ? -2.242  -2.152  -2.246  1.00  19.28 ? 169 THR A O   1 
ATOM   1331 C  CB  . THR A 1 168 ? -0.542  -4.432  -3.940  1.00  18.51 ? 169 THR A CB  1 
ATOM   1332 O  OG1 . THR A 1 168 ? -1.173  -3.777  -5.011  1.00  19.47 ? 169 THR A OG1 1 
ATOM   1333 C  CG2 . THR A 1 168 ? -0.291  -5.901  -4.337  1.00  20.67 ? 169 THR A CG2 1 
ATOM   1334 N  N   . LYS A 1 169 ? -0.276  -2.749  -1.392  1.00  20.29 ? 170 LYS A N   1 
ATOM   1335 C  CA  . LYS A 1 169 ? 0.011   -1.556  -0.591  1.00  20.42 ? 170 LYS A CA  1 
ATOM   1336 C  C   . LYS A 1 169 ? -0.168  -0.366  -1.448  1.00  23.47 ? 170 LYS A C   1 
ATOM   1337 O  O   . LYS A 1 169 ? 0.222   -0.391  -2.626  1.00  24.44 ? 170 LYS A O   1 
ATOM   1338 C  CB  . LYS A 1 169 ? 1.457   -1.628  -0.134  1.00  21.01 ? 170 LYS A CB  1 
ATOM   1339 C  CG  . LYS A 1 169 ? 2.040   -0.501  0.755   1.00  22.75 ? 170 LYS A CG  1 
ATOM   1340 C  CD  . LYS A 1 169 ? 3.524   -0.803  0.818   1.00  27.71 ? 170 LYS A CD  1 
ATOM   1341 C  CE  . LYS A 1 169 ? 4.145   -0.497  2.161   1.00  33.81 ? 170 LYS A CE  1 
ATOM   1342 N  NZ  . LYS A 1 169 ? 4.790   0.855   2.118   1.00  30.75 ? 170 LYS A NZ  1 
ATOM   1343 N  N   . GLY A 1 170 ? -0.762  0.671   -0.879  1.00  24.79 ? 171 GLY A N   1 
ATOM   1344 C  CA  . GLY A 1 170 ? -0.948  1.932   -1.572  1.00  23.77 ? 171 GLY A CA  1 
ATOM   1345 C  C   . GLY A 1 170 ? -2.148  2.023   -2.478  1.00  26.49 ? 171 GLY A C   1 
ATOM   1346 O  O   . GLY A 1 170 ? -2.442  3.125   -2.936  1.00  27.20 ? 171 GLY A O   1 
ATOM   1347 N  N   . LYS A 1 171 ? -2.856  0.907   -2.766  1.00  21.02 ? 172 LYS A N   1 
ATOM   1348 C  CA  . LYS A 1 171 ? -4.080  0.976   -3.581  1.00  23.85 ? 172 LYS A CA  1 
ATOM   1349 C  C   . LYS A 1 171 ? -5.268  1.418   -2.771  1.00  23.72 ? 172 LYS A C   1 
ATOM   1350 O  O   . LYS A 1 171 ? -5.431  0.996   -1.631  1.00  24.68 ? 172 LYS A O   1 
ATOM   1351 C  CB  . LYS A 1 171 ? -4.407  -0.383  -4.269  1.00  25.47 ? 172 LYS A CB  1 
ATOM   1352 C  CG  . LYS A 1 171 ? -3.339  -0.756  -5.285  1.00  29.76 ? 172 LYS A CG  1 
ATOM   1353 C  CD  . LYS A 1 171 ? -3.536  -2.101  -5.992  1.00  32.63 ? 172 LYS A CD  1 
ATOM   1354 C  CE  . LYS A 1 171 ? -3.868  -1.943  -7.472  1.00  34.37 ? 172 LYS A CE  1 
ATOM   1355 N  NZ  . LYS A 1 171 ? -5.348  -2.115  -7.707  1.00  34.47 ? 172 LYS A NZ  1 
ATOM   1356 N  N   . SER A 1 172 ? -6.134  2.231   -3.356  1.00  22.64 ? 173 SER A N   1 
ATOM   1357 C  CA  . SER A 1 172 ? -7.346  2.657   -2.705  1.00  23.94 ? 173 SER A CA  1 
ATOM   1358 C  C   . SER A 1 172 ? -8.497  2.661   -3.679  1.00  27.12 ? 173 SER A C   1 
ATOM   1359 O  O   . SER A 1 172 ? -8.300  2.611   -4.908  1.00  27.41 ? 173 SER A O   1 
ATOM   1360 C  CB  . SER A 1 172 ? -7.199  4.056   -2.060  1.00  29.37 ? 173 SER A CB  1 
ATOM   1361 O  OG  . SER A 1 172 ? -7.055  5.082   -3.039  1.00  29.54 ? 173 SER A OG  1 
ATOM   1362 N  N   . ALA A 1 173 ? -9.705  2.697   -3.141  1.00  24.69 ? 174 ALA A N   1 
ATOM   1363 C  CA  . ALA A 1 173 ? -10.933 2.705   -3.949  1.00  28.73 ? 174 ALA A CA  1 
ATOM   1364 C  C   . ALA A 1 173 ? -11.986 3.549   -3.270  1.00  32.72 ? 174 ALA A C   1 
ATOM   1365 O  O   . ALA A 1 173 ? -11.974 3.685   -2.029  1.00  28.50 ? 174 ALA A O   1 
ATOM   1366 C  CB  . ALA A 1 173 ? -11.464 1.302   -4.114  1.00  27.13 ? 174 ALA A CB  1 
ATOM   1367 N  N   . ASP A 1 174 ? -12.879 4.121   -4.078  1.00  29.13 ? 175 ASP A N   1 
ATOM   1368 C  CA  . ASP A 1 174 ? -14.096 4.748   -3.582  1.00  30.67 ? 175 ASP A CA  1 
ATOM   1369 C  C   . ASP A 1 174 ? -14.940 3.795   -2.770  1.00  27.11 ? 175 ASP A C   1 
ATOM   1370 O  O   . ASP A 1 174 ? -15.167 2.646   -3.145  1.00  23.45 ? 175 ASP A O   1 
ATOM   1371 C  CB  . ASP A 1 174 ? -14.956 5.276   -4.743  1.00  35.47 ? 175 ASP A CB  1 
ATOM   1372 C  CG  . ASP A 1 174 ? -14.319 6.453   -5.421  1.00  40.71 ? 175 ASP A CG  1 
ATOM   1373 O  OD1 . ASP A 1 174 ? -13.867 7.361   -4.687  1.00  43.81 ? 175 ASP A OD1 1 
ATOM   1374 O  OD2 . ASP A 1 174 ? -14.280 6.469   -6.682  1.00  45.87 ? 175 ASP A OD2 1 
ATOM   1375 N  N   . PHE A 1 175 ? -15.452 4.272   -1.653  1.00  23.93 ? 176 PHE A N   1 
ATOM   1376 C  CA  . PHE A 1 175 ? -16.227 3.344   -0.800  1.00  23.58 ? 176 PHE A CA  1 
ATOM   1377 C  C   . PHE A 1 175 ? -17.264 4.142   -0.050  1.00  21.64 ? 176 PHE A C   1 
ATOM   1378 O  O   . PHE A 1 175 ? -17.088 4.479   1.134   1.00  24.90 ? 176 PHE A O   1 
ATOM   1379 C  CB  . PHE A 1 175 ? -15.276 2.527   0.109   1.00  21.20 ? 176 PHE A CB  1 
ATOM   1380 C  CG  . PHE A 1 175 ? -15.896 1.245   0.653   1.00  20.77 ? 176 PHE A CG  1 
ATOM   1381 C  CD1 . PHE A 1 175 ? -16.224 0.191   -0.188  1.00  22.38 ? 176 PHE A CD1 1 
ATOM   1382 C  CD2 . PHE A 1 175 ? -16.141 1.103   1.998   1.00  20.63 ? 176 PHE A CD2 1 
ATOM   1383 C  CE1 . PHE A 1 175 ? -16.813 -0.985  0.321   1.00  22.69 ? 176 PHE A CE1 1 
ATOM   1384 C  CE2 . PHE A 1 175 ? -16.723 -0.049  2.506   1.00  22.15 ? 176 PHE A CE2 1 
ATOM   1385 C  CZ  . PHE A 1 175 ? -17.054 -1.095  1.674   1.00  21.49 ? 176 PHE A CZ  1 
ATOM   1386 N  N   . THR A 1 176 ? -18.327 4.512   -0.764  1.00  18.37 ? 177 THR A N   1 
ATOM   1387 C  CA  . THR A 1 176 ? -19.386 5.325   -0.210  1.00  17.77 ? 177 THR A CA  1 
ATOM   1388 C  C   . THR A 1 176 ? -20.566 4.529   0.222   1.00  16.14 ? 177 THR A C   1 
ATOM   1389 O  O   . THR A 1 176 ? -20.753 3.405   -0.246  1.00  18.06 ? 177 THR A O   1 
ATOM   1390 C  CB  . THR A 1 176 ? -19.857 6.407   -1.215  1.00  19.09 ? 177 THR A CB  1 
ATOM   1391 O  OG1 . THR A 1 176 ? -20.351 5.754   -2.402  1.00  23.01 ? 177 THR A OG1 1 
ATOM   1392 C  CG2 . THR A 1 176 ? -18.701 7.290   -1.599  1.00  21.93 ? 177 THR A CG2 1 
ATOM   1393 N  N   . ASN A 1 177 ? -21.341 5.108   1.139   1.00  15.89 ? 178 ASN A N   1 
ATOM   1394 C  CA  . ASN A 1 177 ? -22.635 4.589   1.575   1.00  16.75 ? 178 ASN A CA  1 
ATOM   1395 C  C   . ASN A 1 177 ? -22.450 3.213   2.203   1.00  17.35 ? 178 ASN A C   1 
ATOM   1396 O  O   . ASN A 1 177 ? -23.322 2.389   2.067   1.00  16.94 ? 178 ASN A O   1 
ATOM   1397 C  CB  . ASN A 1 177 ? -23.545 4.457   0.381   1.00  19.26 ? 178 ASN A CB  1 
ATOM   1398 C  CG  . ASN A 1 177 ? -23.926 5.821   -0.188  1.00  22.51 ? 178 ASN A CG  1 
ATOM   1399 O  OD1 . ASN A 1 177 ? -24.727 6.536   0.416   1.00  20.92 ? 178 ASN A OD1 1 
ATOM   1400 N  ND2 . ASN A 1 177 ? -23.298 6.199   -1.299  1.00  20.67 ? 178 ASN A ND2 1 
ATOM   1401 N  N   . PHE A 1 178 ? -21.260 2.919   2.734   1.00  18.08 ? 179 PHE A N   1 
ATOM   1402 C  CA  . PHE A 1 178 ? -21.146 1.748   3.646   1.00  17.29 ? 179 PHE A CA  1 
ATOM   1403 C  C   . PHE A 1 178 ? -21.702 2.058   5.048   1.00  17.04 ? 179 PHE A C   1 
ATOM   1404 O  O   . PHE A 1 178 ? -21.301 3.029   5.661   1.00  17.48 ? 179 PHE A O   1 
ATOM   1405 C  CB  . PHE A 1 178 ? -19.718 1.294   3.754   1.00  16.44 ? 179 PHE A CB  1 
ATOM   1406 C  CG  . PHE A 1 178 ? -19.581 0.052   4.577   1.00  16.13 ? 179 PHE A CG  1 
ATOM   1407 C  CD1 . PHE A 1 178 ? -19.968 -1.183  4.053   1.00  15.16 ? 179 PHE A CD1 1 
ATOM   1408 C  CD2 . PHE A 1 178 ? -19.247 0.142   5.914   1.00  15.91 ? 179 PHE A CD2 1 
ATOM   1409 C  CE1 . PHE A 1 178 ? -19.898 -2.323  4.824   1.00  15.86 ? 179 PHE A CE1 1 
ATOM   1410 C  CE2 . PHE A 1 178 ? -19.157 -1.009  6.691   1.00  17.41 ? 179 PHE A CE2 1 
ATOM   1411 C  CZ  . PHE A 1 178 ? -19.503 -2.231  6.165   1.00  16.33 ? 179 PHE A CZ  1 
ATOM   1412 N  N   . ASP A 1 179 ? -22.596 1.225   5.575   1.00  17.45 ? 180 ASP A N   1 
ATOM   1413 C  CA  . ASP A 1 179 ? -23.195 1.461   6.880   1.00  19.07 ? 180 ASP A CA  1 
ATOM   1414 C  C   . ASP A 1 179 ? -22.546 0.586   7.929   1.00  18.00 ? 180 ASP A C   1 
ATOM   1415 O  O   . ASP A 1 179 ? -22.776 -0.630  7.925   1.00  17.49 ? 180 ASP A O   1 
ATOM   1416 C  CB  . ASP A 1 179 ? -24.668 1.094   6.823   1.00  19.09 ? 180 ASP A CB  1 
ATOM   1417 C  CG  . ASP A 1 179 ? -25.409 1.402   8.095   1.00  20.98 ? 180 ASP A CG  1 
ATOM   1418 O  OD1 . ASP A 1 179 ? -24.842 1.755   9.159   1.00  18.80 ? 180 ASP A OD1 1 
ATOM   1419 O  OD2 . ASP A 1 179 ? -26.671 1.358   8.025   1.00  26.57 ? 180 ASP A OD2 1 
ATOM   1420 N  N   . PRO A 1 180 ? -21.778 1.165   8.853   1.00  18.77 ? 181 PRO A N   1 
ATOM   1421 C  CA  . PRO A 1 180 ? -21.023 0.306   9.845   1.00  16.53 ? 181 PRO A CA  1 
ATOM   1422 C  C   . PRO A 1 180 ? -21.931 -0.325  10.909  1.00  16.04 ? 181 PRO A C   1 
ATOM   1423 O  O   . PRO A 1 180 ? -21.473 -1.213  11.663  1.00  14.18 ? 181 PRO A O   1 
ATOM   1424 C  CB  . PRO A 1 180 ? -20.039 1.316   10.434  1.00  18.65 ? 181 PRO A CB  1 
ATOM   1425 C  CG  . PRO A 1 180 ? -20.810 2.603   10.396  1.00  19.36 ? 181 PRO A CG  1 
ATOM   1426 C  CD  . PRO A 1 180 ? -21.460 2.598   9.062   1.00  18.57 ? 181 PRO A CD  1 
ATOM   1427 N  N   . ARG A 1 181 ? -23.215 0.074   10.986  1.00  14.90 ? 182 ARG A N   1 
ATOM   1428 C  CA  . ARG A 1 181 ? -24.142 -0.611  11.912  1.00  16.11 ? 182 ARG A CA  1 
ATOM   1429 C  C   . ARG A 1 181 ? -24.273 -2.077  11.488  1.00  15.81 ? 182 ARG A C   1 
ATOM   1430 O  O   . ARG A 1 181 ? -24.618 -2.906  12.295  1.00  17.04 ? 182 ARG A O   1 
ATOM   1431 C  CB  . ARG A 1 181 ? -25.545 0.051   11.939  1.00  16.34 ? 182 ARG A CB  1 
ATOM   1432 C  CG  . ARG A 1 181 ? -25.459 1.459   12.568  1.00  17.74 ? 182 ARG A CG  1 
ATOM   1433 C  CD  . ARG A 1 181 ? -26.712 2.248   12.398  1.00  18.20 ? 182 ARG A CD  1 
ATOM   1434 N  NE  . ARG A 1 181 ? -27.136 2.317   10.988  1.00  19.12 ? 182 ARG A NE  1 
ATOM   1435 C  CZ  . ARG A 1 181 ? -28.201 3.019   10.630  1.00  21.43 ? 182 ARG A CZ  1 
ATOM   1436 N  NH1 . ARG A 1 181 ? -28.850 3.673   11.576  1.00  21.79 ? 182 ARG A NH1 1 
ATOM   1437 N  NH2 . ARG A 1 181 ? -28.616 3.085   9.361   1.00  21.83 ? 182 ARG A NH2 1 
ATOM   1438 N  N   . GLY A 1 182 ? -24.022 -2.376  10.223  1.00  15.68 ? 183 GLY A N   1 
ATOM   1439 C  CA  . GLY A 1 182 ? -24.023 -3.779  9.753   1.00  16.80 ? 183 GLY A CA  1 
ATOM   1440 C  C   . GLY A 1 182 ? -22.895 -4.638  10.322  1.00  16.08 ? 183 GLY A C   1 
ATOM   1441 O  O   . GLY A 1 182 ? -22.827 -5.831  10.043  1.00  17.29 ? 183 GLY A O   1 
ATOM   1442 N  N   . LEU A 1 183 ? -22.025 -4.060  11.150  1.00  14.91 ? 184 LEU A N   1 
ATOM   1443 C  CA  . LEU A 1 183 ? -20.858 -4.814  11.664  1.00  14.73 ? 184 LEU A CA  1 
ATOM   1444 C  C   . LEU A 1 183 ? -20.997 -5.064  13.180  1.00  14.93 ? 184 LEU A C   1 
ATOM   1445 O  O   . LEU A 1 183 ? -20.082 -5.621  13.831  1.00  17.06 ? 184 LEU A O   1 
ATOM   1446 C  CB  . LEU A 1 183 ? -19.552 -4.054  11.354  1.00  14.29 ? 184 LEU A CB  1 
ATOM   1447 C  CG  . LEU A 1 183 ? -19.250 -3.803  9.863   1.00  15.68 ? 184 LEU A CG  1 
ATOM   1448 C  CD1 . LEU A 1 183 ? -18.052 -2.935  9.817   1.00  18.15 ? 184 LEU A CD1 1 
ATOM   1449 C  CD2 . LEU A 1 183 ? -19.025 -5.083  9.050   1.00  15.58 ? 184 LEU A CD2 1 
ATOM   1450 N  N   . LEU A 1 184 ? -22.092 -4.587  13.783  1.00  13.96 ? 185 LEU A N   1 
ATOM   1451 C  CA  . LEU A 1 184 ? -22.198 -4.628  15.271  1.00  14.24 ? 185 LEU A CA  1 
ATOM   1452 C  C   . LEU A 1 184 ? -22.896 -5.942  15.590  1.00  14.99 ? 185 LEU A C   1 
ATOM   1453 O  O   . LEU A 1 184 ? -23.597 -6.517  14.690  1.00  20.19 ? 185 LEU A O   1 
ATOM   1454 C  CB  . LEU A 1 184 ? -23.053 -3.460  15.790  1.00  13.61 ? 185 LEU A CB  1 
ATOM   1455 C  CG  . LEU A 1 184 ? -22.483 -2.077  15.412  1.00  13.22 ? 185 LEU A CG  1 
ATOM   1456 C  CD1 . LEU A 1 184 ? -23.443 -1.028  15.875  1.00  14.27 ? 185 LEU A CD1 1 
ATOM   1457 C  CD2 . LEU A 1 184 ? -21.056 -1.814  15.904  1.00  11.67 ? 185 LEU A CD2 1 
ATOM   1458 N  N   . PRO A 1 185 ? -22.655 -6.472  16.800  1.00  15.12 ? 186 PRO A N   1 
ATOM   1459 C  CA  . PRO A 1 185 ? -23.457 -7.624  17.314  1.00  14.57 ? 186 PRO A CA  1 
ATOM   1460 C  C   . PRO A 1 185 ? -24.762 -7.086  17.996  1.00  15.97 ? 186 PRO A C   1 
ATOM   1461 O  O   . PRO A 1 185 ? -24.964 -5.870  18.086  1.00  15.25 ? 186 PRO A O   1 
ATOM   1462 C  CB  . PRO A 1 185 ? -22.471 -8.242  18.321  1.00  12.94 ? 186 PRO A CB  1 
ATOM   1463 C  CG  . PRO A 1 185 ? -21.773 -7.032  18.935  1.00  12.91 ? 186 PRO A CG  1 
ATOM   1464 C  CD  . PRO A 1 185 ? -21.639 -6.018  17.783  1.00  12.16 ? 186 PRO A CD  1 
ATOM   1465 N  N   . GLU A 1 186 ? -25.645 -7.935  18.529  1.00  16.79 ? 187 GLU A N   1 
ATOM   1466 C  CA  . GLU A 1 186 ? -26.860 -7.473  19.163  1.00  18.46 ? 187 GLU A CA  1 
ATOM   1467 C  C   . GLU A 1 186 ? -26.601 -6.734  20.429  1.00  19.86 ? 187 GLU A C   1 
ATOM   1468 O  O   . GLU A 1 186 ? -27.294 -5.720  20.742  1.00  21.85 ? 187 GLU A O   1 
ATOM   1469 C  CB  . GLU A 1 186 ? -27.759 -8.658  19.607  1.00  19.89 ? 187 GLU A CB  1 
ATOM   1470 C  CG  . GLU A 1 186 ? -28.359 -9.496  18.498  1.00  27.45 ? 187 GLU A CG  1 
ATOM   1471 C  CD  . GLU A 1 186 ? -28.973 -10.807 19.033  1.00  25.34 ? 187 GLU A CD  1 
ATOM   1472 O  OE1 . GLU A 1 186 ? -29.229 -11.744 18.239  1.00  40.75 ? 187 GLU A OE1 1 
ATOM   1473 O  OE2 . GLU A 1 186 ? -29.190 -10.894 20.236  1.00  23.99 ? 187 GLU A OE2 1 
ATOM   1474 N  N   . SER A 1 187 ? -25.710 -7.304  21.262  1.00  16.73 ? 188 SER A N   1 
ATOM   1475 C  CA  . SER A 1 187 ? -25.507 -6.703  22.566  1.00  17.15 ? 188 SER A CA  1 
ATOM   1476 C  C   . SER A 1 187 ? -24.368 -5.671  22.522  1.00  16.31 ? 188 SER A C   1 
ATOM   1477 O  O   . SER A 1 187 ? -23.392 -5.865  21.874  1.00  13.36 ? 188 SER A O   1 
ATOM   1478 C  CB  . SER A 1 187 ? -25.301 -7.783  23.640  1.00  16.36 ? 188 SER A CB  1 
ATOM   1479 O  OG  . SER A 1 187 ? -24.775 -7.246  24.861  1.00  15.73 ? 188 SER A OG  1 
ATOM   1480 N  N   . LEU A 1 188 ? -24.505 -4.666  23.339  1.00  16.41 ? 189 LEU A N   1 
ATOM   1481 C  CA  . LEU A 1 188 ? -23.456 -3.664  23.488  1.00  16.40 ? 189 LEU A CA  1 
ATOM   1482 C  C   . LEU A 1 188 ? -22.753 -3.718  24.862  1.00  16.70 ? 189 LEU A C   1 
ATOM   1483 O  O   . LEU A 1 188 ? -22.130 -2.752  25.278  1.00  17.47 ? 189 LEU A O   1 
ATOM   1484 C  CB  . LEU A 1 188 ? -24.037 -2.254  23.191  1.00  17.10 ? 189 LEU A CB  1 
ATOM   1485 C  CG  . LEU A 1 188 ? -24.409 -1.760  21.782  1.00  19.46 ? 189 LEU A CG  1 
ATOM   1486 C  CD1 . LEU A 1 188 ? -24.859 -0.266  21.761  1.00  17.85 ? 189 LEU A CD1 1 
ATOM   1487 C  CD2 . LEU A 1 188 ? -23.383 -2.064  20.701  1.00  19.75 ? 189 LEU A CD2 1 
ATOM   1488 N  N   . ASP A 1 189 ? -22.875 -4.842  25.584  1.00  18.21 ? 190 ASP A N   1 
ATOM   1489 C  CA  . ASP A 1 189 ? -22.089 -5.090  26.791  1.00  16.05 ? 190 ASP A CA  1 
ATOM   1490 C  C   . ASP A 1 189 ? -20.580 -5.084  26.426  1.00  14.01 ? 190 ASP A C   1 
ATOM   1491 O  O   . ASP A 1 189 ? -20.182 -5.455  25.322  1.00  12.76 ? 190 ASP A O   1 
ATOM   1492 C  CB  . ASP A 1 189 ? -22.449 -6.447  27.380  1.00  16.52 ? 190 ASP A CB  1 
ATOM   1493 C  CG  . ASP A 1 189 ? -23.829 -6.483  28.082  1.00  23.31 ? 190 ASP A CG  1 
ATOM   1494 O  OD1 . ASP A 1 189 ? -24.557 -5.459  28.198  1.00  25.67 ? 190 ASP A OD1 1 
ATOM   1495 O  OD2 . ASP A 1 189 ? -24.178 -7.597  28.509  1.00  24.26 ? 190 ASP A OD2 1 
ATOM   1496 N  N   . TYR A 1 190 ? -19.800 -4.495  27.308  1.00  13.45 ? 191 TYR A N   1 
ATOM   1497 C  CA  . TYR A 1 190 ? -18.423 -4.158  26.994  1.00  13.35 ? 191 TYR A CA  1 
ATOM   1498 C  C   . TYR A 1 190 ? -17.544 -4.256  28.223  1.00  13.12 ? 191 TYR A C   1 
ATOM   1499 O  O   . TYR A 1 190 ? -18.026 -4.121  29.359  1.00  12.30 ? 191 TYR A O   1 
ATOM   1500 C  CB  . TYR A 1 190 ? -18.364 -2.761  26.319  1.00  12.73 ? 191 TYR A CB  1 
ATOM   1501 C  CG  . TYR A 1 190 ? -18.765 -1.621  27.238  1.00  13.80 ? 191 TYR A CG  1 
ATOM   1502 C  CD1 . TYR A 1 190 ? -17.830 -0.978  28.046  1.00  14.45 ? 191 TYR A CD1 1 
ATOM   1503 C  CD2 . TYR A 1 190 ? -20.054 -1.091  27.166  1.00  13.40 ? 191 TYR A CD2 1 
ATOM   1504 C  CE1 . TYR A 1 190 ? -18.193 0.066   28.890  1.00  14.78 ? 191 TYR A CE1 1 
ATOM   1505 C  CE2 . TYR A 1 190 ? -20.417 -0.029  27.984  1.00  17.03 ? 191 TYR A CE2 1 
ATOM   1506 C  CZ  . TYR A 1 190 ? -19.486 0.534   28.842  1.00  15.91 ? 191 TYR A CZ  1 
ATOM   1507 O  OH  . TYR A 1 190 ? -19.870 1.551   29.661  1.00  16.51 ? 191 TYR A OH  1 
ATOM   1508 N  N   . TRP A 1 191 ? -16.244 -4.436  27.981  1.00  11.38 ? 192 TRP A N   1 
ATOM   1509 C  CA  . TRP A 1 191 ? -15.207 -4.137  28.920  1.00  11.37 ? 192 TRP A CA  1 
ATOM   1510 C  C   . TRP A 1 191 ? -14.535 -2.852  28.496  1.00  10.15 ? 192 TRP A C   1 
ATOM   1511 O  O   . TRP A 1 191 ? -14.544 -2.487  27.303  1.00  9.73  ? 192 TRP A O   1 
ATOM   1512 C  CB  . TRP A 1 191 ? -14.174 -5.184  28.907  1.00  11.25 ? 192 TRP A CB  1 
ATOM   1513 C  CG  . TRP A 1 191 ? -14.687 -6.547  29.279  1.00  12.14 ? 192 TRP A CG  1 
ATOM   1514 C  CD1 . TRP A 1 191 ? -14.978 -7.019  30.556  1.00  11.17 ? 192 TRP A CD1 1 
ATOM   1515 C  CD2 . TRP A 1 191 ? -14.930 -7.685  28.374  1.00  11.55 ? 192 TRP A CD2 1 
ATOM   1516 N  NE1 . TRP A 1 191 ? -15.389 -8.319  30.507  1.00  11.24 ? 192 TRP A NE1 1 
ATOM   1517 C  CE2 . TRP A 1 191 ? -15.386 -8.781  29.230  1.00  12.00 ? 192 TRP A CE2 1 
ATOM   1518 C  CE3 . TRP A 1 191 ? -14.838 -7.889  27.002  1.00  12.08 ? 192 TRP A CE3 1 
ATOM   1519 C  CZ2 . TRP A 1 191 ? -15.715 -10.033 28.706  1.00  11.22 ? 192 TRP A CZ2 1 
ATOM   1520 C  CZ3 . TRP A 1 191 ? -15.177 -9.141  26.490  1.00  11.20 ? 192 TRP A CZ3 1 
ATOM   1521 C  CH2 . TRP A 1 191 ? -15.598 -10.191 27.322  1.00  11.63 ? 192 TRP A CH2 1 
ATOM   1522 N  N   . THR A 1 192 ? -13.968 -2.137  29.436  1.00  10.24 ? 193 THR A N   1 
ATOM   1523 C  CA  . THR A 1 192 ? -13.240 -0.924  29.053  1.00  11.10 ? 193 THR A CA  1 
ATOM   1524 C  C   . THR A 1 192 ? -11.963 -0.726  29.926  1.00  11.47 ? 193 THR A C   1 
ATOM   1525 O  O   . THR A 1 192 ? -11.927 -1.088  31.135  1.00  12.61 ? 193 THR A O   1 
ATOM   1526 C  CB  . THR A 1 192 ? -14.194 0.340   29.181  1.00  10.73 ? 193 THR A CB  1 
ATOM   1527 O  OG1 . THR A 1 192 ? -13.511 1.539   28.741  1.00  11.17 ? 193 THR A OG1 1 
ATOM   1528 C  CG2 . THR A 1 192 ? -14.441 0.592   30.605  1.00  11.17 ? 193 THR A CG2 1 
ATOM   1529 N  N   . TYR A 1 193 ? -10.911 -0.156  29.344  1.00  10.53 ? 194 TYR A N   1 
ATOM   1530 C  CA  . TYR A 1 193 ? -9.708  0.102   30.071  1.00  10.07 ? 194 TYR A CA  1 
ATOM   1531 C  C   . TYR A 1 193 ? -9.029  1.192   29.317  1.00  9.73  ? 194 TYR A C   1 
ATOM   1532 O  O   . TYR A 1 193 ? -9.394  1.380   28.166  1.00  8.62  ? 194 TYR A O   1 
ATOM   1533 C  CB  . TYR A 1 193 ? -8.810  -1.195  30.303  1.00  9.55  ? 194 TYR A CB  1 
ATOM   1534 C  CG  . TYR A 1 193 ? -8.136  -1.653  29.018  1.00  10.50 ? 194 TYR A CG  1 
ATOM   1535 C  CD1 . TYR A 1 193 ? -8.812  -2.415  28.050  1.00  9.59  ? 194 TYR A CD1 1 
ATOM   1536 C  CD2 . TYR A 1 193 ? -6.844  -1.261  28.762  1.00  9.91  ? 194 TYR A CD2 1 
ATOM   1537 C  CE1 . TYR A 1 193 ? -8.177  -2.779  26.844  1.00  9.59  ? 194 TYR A CE1 1 
ATOM   1538 C  CE2 . TYR A 1 193 ? -6.200  -1.577  27.569  1.00  10.03 ? 194 TYR A CE2 1 
ATOM   1539 C  CZ  . TYR A 1 193 ? -6.862  -2.361  26.627  1.00  10.02 ? 194 TYR A CZ  1 
ATOM   1540 O  OH  . TYR A 1 193 ? -6.151  -2.649  25.468  1.00  11.96 ? 194 TYR A OH  1 
ATOM   1541 N  N   . PRO A 1 194 ? -8.057  1.896   29.966  1.00  10.67 ? 195 PRO A N   1 
ATOM   1542 C  CA  . PRO A 1 194 ? -7.231  2.904   29.325  1.00  10.90 ? 195 PRO A CA  1 
ATOM   1543 C  C   . PRO A 1 194 ? -6.052  2.258   28.648  1.00  10.52 ? 195 PRO A C   1 
ATOM   1544 O  O   . PRO A 1 194 ? -5.384  1.447   29.271  1.00  9.81  ? 195 PRO A O   1 
ATOM   1545 C  CB  . PRO A 1 194 ? -6.721  3.784   30.500  1.00  12.09 ? 195 PRO A CB  1 
ATOM   1546 C  CG  . PRO A 1 194 ? -6.699  2.898   31.703  1.00  11.50 ? 195 PRO A CG  1 
ATOM   1547 C  CD  . PRO A 1 194 ? -7.874  1.910   31.444  1.00  10.75 ? 195 PRO A CD  1 
ATOM   1548 N  N   . GLY A 1 195 ? -5.793  2.584   27.373  1.00  9.04  ? 196 GLY A N   1 
ATOM   1549 C  CA  . GLY A 1 195 ? -4.735  1.822   26.663  1.00  9.78  ? 196 GLY A CA  1 
ATOM   1550 C  C   . GLY A 1 195 ? -4.099  2.695   25.573  1.00  10.49 ? 196 GLY A C   1 
ATOM   1551 O  O   . GLY A 1 195 ? -4.055  3.941   25.725  1.00  10.65 ? 196 GLY A O   1 
ATOM   1552 N  N   . SER A 1 196 ? -3.719  2.092   24.469  1.00  9.59  ? 197 SER A N   1 
ATOM   1553 C  CA  . SER A 1 196 ? -2.942  2.807   23.440  1.00  9.41  ? 197 SER A CA  1 
ATOM   1554 C  C   . SER A 1 196 ? -3.287  2.407   22.008  1.00  9.36  ? 197 SER A C   1 
ATOM   1555 O  O   . SER A 1 196 ? -4.027  1.431   21.794  1.00  9.59  ? 197 SER A O   1 
ATOM   1556 C  CB  . SER A 1 196 ? -1.477  2.452   23.665  1.00  10.29 ? 197 SER A CB  1 
ATOM   1557 O  OG  . SER A 1 196 ? -1.283  1.077   23.170  1.00  10.11 ? 197 SER A OG  1 
ATOM   1558 N  N   . LEU A 1 197 ? -2.723  3.106   21.009  1.00  8.58  ? 198 LEU A N   1 
ATOM   1559 C  CA  . LEU A 1 197 ? -2.764  2.571   19.693  1.00  9.41  ? 198 LEU A CA  1 
ATOM   1560 C  C   . LEU A 1 197 ? -2.043  1.246   19.764  1.00  9.30  ? 198 LEU A C   1 
ATOM   1561 O  O   . LEU A 1 197 ? -1.048  1.128   20.483  1.00  9.72  ? 198 LEU A O   1 
ATOM   1562 C  CB  . LEU A 1 197 ? -2.017  3.490   18.736  1.00  9.83  ? 198 LEU A CB  1 
ATOM   1563 C  CG  . LEU A 1 197 ? -2.329  4.988   18.774  1.00  12.36 ? 198 LEU A CG  1 
ATOM   1564 C  CD1 . LEU A 1 197 ? -1.443  5.676   17.720  1.00  14.75 ? 198 LEU A CD1 1 
ATOM   1565 C  CD2 . LEU A 1 197 ? -3.786  5.314   18.542  1.00  11.23 ? 198 LEU A CD2 1 
ATOM   1566 N  N   . THR A 1 198 ? -2.525  0.264   18.974  1.00  9.72  ? 199 THR A N   1 
ATOM   1567 C  CA  . THR A 1 198 ? -1.816  -1.003  18.846  1.00  11.18 ? 199 THR A CA  1 
ATOM   1568 C  C   . THR A 1 198 ? -0.796  -1.091  17.694  1.00  11.84 ? 199 THR A C   1 
ATOM   1569 O  O   . THR A 1 198 ? -0.181  -2.181  17.455  1.00  13.15 ? 199 THR A O   1 
ATOM   1570 C  CB  . THR A 1 198 ? -2.837  -2.180  18.748  1.00  8.50  ? 199 THR A CB  1 
ATOM   1571 O  OG1 . THR A 1 198 ? -3.469  -2.197  17.434  1.00  8.66  ? 199 THR A OG1 1 
ATOM   1572 C  CG2 . THR A 1 198 ? -3.832  -2.156  20.001  1.00  8.66  ? 199 THR A CG2 1 
ATOM   1573 N  N   . THR A 1 199 ? -0.584  0.002   16.960  1.00  13.40 ? 200 THR A N   1 
ATOM   1574 C  CA  . THR A 1 199 ? 0.535   0.070   16.040  1.00  12.88 ? 200 THR A CA  1 
ATOM   1575 C  C   . THR A 1 199 ? 1.322   1.344   16.336  1.00  13.76 ? 200 THR A C   1 
ATOM   1576 O  O   . THR A 1 199 ? 0.739   2.302   16.904  1.00  11.91 ? 200 THR A O   1 
ATOM   1577 C  CB  . THR A 1 199 ? 0.129   0.131   14.551  1.00  13.79 ? 200 THR A CB  1 
ATOM   1578 O  OG1 . THR A 1 199 ? -0.824  1.210   14.352  1.00  14.41 ? 200 THR A OG1 1 
ATOM   1579 C  CG2 . THR A 1 199 ? -0.483  -1.241  14.087  1.00  12.44 ? 200 THR A CG2 1 
ATOM   1580 N  N   . PRO A 1 200 ? 2.644   1.323   15.981  1.00  13.93 ? 201 PRO A N   1 
ATOM   1581 C  CA  . PRO A 1 200 ? 3.397   2.564   16.106  1.00  15.02 ? 201 PRO A CA  1 
ATOM   1582 C  C   . PRO A 1 200 ? 2.596   3.772   15.535  1.00  14.01 ? 201 PRO A C   1 
ATOM   1583 O  O   . PRO A 1 200 ? 2.093   3.685   14.432  1.00  16.44 ? 201 PRO A O   1 
ATOM   1584 C  CB  . PRO A 1 200 ? 4.581   2.295   15.206  1.00  14.11 ? 201 PRO A CB  1 
ATOM   1585 C  CG  . PRO A 1 200 ? 4.863   0.814   15.347  1.00  15.41 ? 201 PRO A CG  1 
ATOM   1586 C  CD  . PRO A 1 200 ? 3.420   0.315   15.206  1.00  15.18 ? 201 PRO A CD  1 
ATOM   1587 N  N   . PRO A 1 201 ? 2.609   4.939   16.168  1.00  13.23 ? 202 PRO A N   1 
ATOM   1588 C  CA  . PRO A 1 201 ? 3.473   5.448   17.256  1.00  12.59 ? 202 PRO A CA  1 
ATOM   1589 C  C   . PRO A 1 201 ? 3.068   4.977   18.654  1.00  11.43 ? 202 PRO A C   1 
ATOM   1590 O  O   . PRO A 1 201 ? 3.732   5.312   19.614  1.00  11.12 ? 202 PRO A O   1 
ATOM   1591 C  CB  . PRO A 1 201 ? 3.305   6.987   17.176  1.00  13.37 ? 202 PRO A CB  1 
ATOM   1592 C  CG  . PRO A 1 201 ? 2.123   7.228   16.290  1.00  13.61 ? 202 PRO A CG  1 
ATOM   1593 C  CD  . PRO A 1 201 ? 1.992   6.028   15.376  1.00  13.49 ? 202 PRO A CD  1 
ATOM   1594 N  N   . LEU A 1 202 ? 2.085   4.078   18.741  1.00  10.68 ? 203 LEU A N   1 
ATOM   1595 C  CA  . LEU A 1 202 ? 1.826   3.386   20.014  1.00  10.61 ? 203 LEU A CA  1 
ATOM   1596 C  C   . LEU A 1 202 ? 1.410   4.377   21.138  1.00  9.89  ? 203 LEU A C   1 
ATOM   1597 O  O   . LEU A 1 202 ? 1.613   4.115   22.339  1.00  10.04 ? 203 LEU A O   1 
ATOM   1598 C  CB  . LEU A 1 202 ? 2.954   2.435   20.444  1.00  11.05 ? 203 LEU A CB  1 
ATOM   1599 C  CG  . LEU A 1 202 ? 3.169   1.231   19.505  1.00  12.06 ? 203 LEU A CG  1 
ATOM   1600 C  CD1 . LEU A 1 202 ? 4.479   0.577   19.898  1.00  13.17 ? 203 LEU A CD1 1 
ATOM   1601 C  CD2 . LEU A 1 202 ? 2.015   0.177   19.549  1.00  10.57 ? 203 LEU A CD2 1 
ATOM   1602 N  N   . LEU A 1 203 ? 0.726   5.458   20.728  1.00  9.64  ? 204 LEU A N   1 
ATOM   1603 C  CA  . LEU A 1 203 ? 0.452   6.571   21.658  1.00  10.60 ? 204 LEU A CA  1 
ATOM   1604 C  C   . LEU A 1 203 ? -0.577  6.143   22.680  1.00  11.19 ? 204 LEU A C   1 
ATOM   1605 O  O   . LEU A 1 203 ? -1.578  5.460   22.361  1.00  10.49 ? 204 LEU A O   1 
ATOM   1606 C  CB  . LEU A 1 203 ? -0.028  7.823   20.904  1.00  10.66 ? 204 LEU A CB  1 
ATOM   1607 C  CG  . LEU A 1 203 ? 0.956   8.262   19.776  1.00  11.20 ? 204 LEU A CG  1 
ATOM   1608 C  CD1 . LEU A 1 203 ? 0.399   9.324   18.822  1.00  13.22 ? 204 LEU A CD1 1 
ATOM   1609 C  CD2 . LEU A 1 203 ? 2.194   8.799   20.516  1.00  14.23 ? 204 LEU A CD2 1 
ATOM   1610 N  N   . GLU A 1 204 ? -0.344  6.563   23.914  1.00  11.48 ? 205 GLU A N   1 
ATOM   1611 C  CA  . GLU A 1 204 ? -1.213  6.185   24.995  1.00  12.99 ? 205 GLU A CA  1 
ATOM   1612 C  C   . GLU A 1 204 ? -2.393  7.140   25.154  1.00  12.05 ? 205 GLU A C   1 
ATOM   1613 O  O   . GLU A 1 204 ? -2.478  7.902   26.118  1.00  11.54 ? 205 GLU A O   1 
ATOM   1614 C  CB  . GLU A 1 204 ? -0.418  6.030   26.250  1.00  13.76 ? 205 GLU A CB  1 
ATOM   1615 C  CG  . GLU A 1 204 ? 0.473   4.823   26.062  1.00  14.54 ? 205 GLU A CG  1 
ATOM   1616 C  CD  . GLU A 1 204 ? 1.373   4.534   27.268  1.00  16.85 ? 205 GLU A CD  1 
ATOM   1617 O  OE1 . GLU A 1 204 ? 1.656   5.463   28.075  1.00  15.88 ? 205 GLU A OE1 1 
ATOM   1618 O  OE2 . GLU A 1 204 ? 1.828   3.385   27.409  1.00  14.46 ? 205 GLU A OE2 1 
ATOM   1619 N  N   . CYS A 1 205 ? -3.326  7.035   24.226  1.00  12.00 ? 206 CYS A N   1 
ATOM   1620 C  CA  . CYS A 1 205 ? -4.397  8.084   24.042  1.00  10.88 ? 206 CYS A CA  1 
ATOM   1621 C  C   . CYS A 1 205 ? -5.770  7.445   23.878  1.00  11.51 ? 206 CYS A C   1 
ATOM   1622 O  O   . CYS A 1 205 ? -6.712  8.083   23.450  1.00  11.15 ? 206 CYS A O   1 
ATOM   1623 C  CB  . CYS A 1 205 ? -4.051  8.905   22.811  1.00  11.22 ? 206 CYS A CB  1 
ATOM   1624 S  SG  . CYS A 1 205 ? -4.092  7.964   21.249  1.00  12.10 ? 206 CYS A SG  1 
ATOM   1625 N  N   . VAL A 1 206 ? -5.870  6.157   24.158  1.00  10.26 ? 207 VAL A N   1 
ATOM   1626 C  CA  . VAL A 1 206 ? -7.108  5.396   23.815  1.00  9.99  ? 207 VAL A CA  1 
ATOM   1627 C  C   . VAL A 1 206 ? -7.879  4.940   25.025  1.00  9.92  ? 207 VAL A C   1 
ATOM   1628 O  O   . VAL A 1 206 ? -7.336  4.350   25.921  1.00  11.59 ? 207 VAL A O   1 
ATOM   1629 C  CB  . VAL A 1 206 ? -6.858  4.126   22.969  1.00  9.81  ? 207 VAL A CB  1 
ATOM   1630 C  CG1 . VAL A 1 206 ? -8.202  3.481   22.645  1.00  8.57  ? 207 VAL A CG1 1 
ATOM   1631 C  CG2 . VAL A 1 206 ? -6.088  4.435   21.650  1.00  10.36 ? 207 VAL A CG2 1 
ATOM   1632 N  N   . THR A 1 207 ? -9.165  5.237   25.053  1.00  10.08 ? 208 THR A N   1 
ATOM   1633 C  CA  . THR A 1 207 ? -10.130 4.536   25.904  1.00  10.47 ? 208 THR A CA  1 
ATOM   1634 C  C   . THR A 1 207 ? -10.626 3.401   25.064  1.00  10.12 ? 208 THR A C   1 
ATOM   1635 O  O   . THR A 1 207 ? -11.198 3.646   24.038  1.00  11.39 ? 208 THR A O   1 
ATOM   1636 C  CB  . THR A 1 207 ? -11.309 5.468   26.308  1.00  10.39 ? 208 THR A CB  1 
ATOM   1637 O  OG1 . THR A 1 207 ? -10.758 6.529   27.141  1.00  9.92  ? 208 THR A OG1 1 
ATOM   1638 C  CG2 . THR A 1 207 ? -12.263 4.705   27.134  1.00  11.37 ? 208 THR A CG2 1 
ATOM   1639 N  N   . TRP A 1 208 ? -10.328 2.179   25.484  1.00  10.60 ? 209 TRP A N   1 
ATOM   1640 C  CA  . TRP A 1 208 ? -10.682 0.959   24.767  1.00  9.89  ? 209 TRP A CA  1 
ATOM   1641 C  C   . TRP A 1 208 ? -12.007 0.454   25.276  1.00  10.41 ? 209 TRP A C   1 
ATOM   1642 O  O   . TRP A 1 208 ? -12.262 0.414   26.478  1.00  10.44 ? 209 TRP A O   1 
ATOM   1643 C  CB  . TRP A 1 208 ? -9.583  -0.159  24.988  1.00  9.57  ? 209 TRP A CB  1 
ATOM   1644 C  CG  . TRP A 1 208 ? -8.505  -0.046  23.998  1.00  9.88  ? 209 TRP A CG  1 
ATOM   1645 C  CD1 . TRP A 1 208 ? -7.240  0.531   24.162  1.00  10.66 ? 209 TRP A CD1 1 
ATOM   1646 C  CD2 . TRP A 1 208 ? -8.569  -0.464  22.589  1.00  10.05 ? 209 TRP A CD2 1 
ATOM   1647 N  NE1 . TRP A 1 208 ? -6.557  0.463   23.020  1.00  11.01 ? 209 TRP A NE1 1 
ATOM   1648 C  CE2 . TRP A 1 208 ? -7.285  -0.130  22.018  1.00  9.98  ? 209 TRP A CE2 1 
ATOM   1649 C  CE3 . TRP A 1 208 ? -9.543  -1.057  21.787  1.00  9.61  ? 209 TRP A CE3 1 
ATOM   1650 C  CZ2 . TRP A 1 208 ? -6.980  -0.383  20.686  1.00  10.12 ? 209 TRP A CZ2 1 
ATOM   1651 C  CZ3 . TRP A 1 208 ? -9.222  -1.319  20.430  1.00  9.49  ? 209 TRP A CZ3 1 
ATOM   1652 C  CH2 . TRP A 1 208 ? -7.959  -0.995  19.906  1.00  9.47  ? 209 TRP A CH2 1 
ATOM   1653 N  N   . ILE A 1 209 ? -12.891 0.188   24.343  1.00  9.91  ? 210 ILE A N   1 
ATOM   1654 C  CA  . ILE A 1 209 ? -14.238 -0.278  24.621  1.00  9.90  ? 210 ILE A CA  1 
ATOM   1655 C  C   . ILE A 1 209 ? -14.353 -1.587  23.849  1.00  9.89  ? 210 ILE A C   1 
ATOM   1656 O  O   . ILE A 1 209 ? -14.352 -1.580  22.672  1.00  10.53 ? 210 ILE A O   1 
ATOM   1657 C  CB  . ILE A 1 209 ? -15.258 0.764   24.215  1.00  10.50 ? 210 ILE A CB  1 
ATOM   1658 C  CG1 . ILE A 1 209 ? -15.061 2.062   25.078  1.00  10.68 ? 210 ILE A CG1 1 
ATOM   1659 C  CG2 . ILE A 1 209 ? -16.697 0.190   24.462  1.00  11.40 ? 210 ILE A CG2 1 
ATOM   1660 C  CD1 . ILE A 1 209 ? -15.952 3.204   24.622  1.00  12.31 ? 210 ILE A CD1 1 
ATOM   1661 N  N   . VAL A 1 210 ? -14.311 -2.747  24.495  1.00  10.40 ? 211 VAL A N   1 
ATOM   1662 C  CA  . VAL A 1 210 ? -14.270 -3.994  23.724  1.00  8.95  ? 211 VAL A CA  1 
ATOM   1663 C  C   . VAL A 1 210 ? -15.594 -4.712  24.017  1.00  9.72  ? 211 VAL A C   1 
ATOM   1664 O  O   . VAL A 1 210 ? -15.862 -5.004  25.203  1.00  9.02  ? 211 VAL A O   1 
ATOM   1665 C  CB  . VAL A 1 210 ? -13.113 -4.900  24.184  1.00  8.85  ? 211 VAL A CB  1 
ATOM   1666 C  CG1 . VAL A 1 210 ? -13.149 -6.257  23.441  1.00  8.75  ? 211 VAL A CG1 1 
ATOM   1667 C  CG2 . VAL A 1 210 ? -11.746 -4.211  23.982  1.00  8.51  ? 211 VAL A CG2 1 
ATOM   1668 N  N   . LEU A 1 211 ? -16.408 -4.948  22.981  1.00  9.64  ? 212 LEU A N   1 
ATOM   1669 C  CA  . LEU A 1 211 ? -17.686 -5.679  23.123  1.00  10.02 ? 212 LEU A CA  1 
ATOM   1670 C  C   . LEU A 1 211 ? -17.466 -7.125  23.505  1.00  10.41 ? 212 LEU A C   1 
ATOM   1671 O  O   . LEU A 1 211 ? -16.601 -7.830  22.964  1.00  10.03 ? 212 LEU A O   1 
ATOM   1672 C  CB  . LEU A 1 211 ? -18.522 -5.597  21.842  1.00  10.42 ? 212 LEU A CB  1 
ATOM   1673 C  CG  . LEU A 1 211 ? -18.878 -4.172  21.292  1.00  11.05 ? 212 LEU A CG  1 
ATOM   1674 C  CD1 . LEU A 1 211 ? -19.951 -4.261  20.149  1.00  11.22 ? 212 LEU A CD1 1 
ATOM   1675 C  CD2 . LEU A 1 211 ? -19.326 -3.279  22.469  1.00  11.48 ? 212 LEU A CD2 1 
ATOM   1676 N  N   . LYS A 1 212 ? -18.288 -7.565  24.439  1.00  12.21 ? 213 LYS A N   1 
ATOM   1677 C  CA  . LYS A 1 212 ? -18.304 -8.949  24.855  1.00  13.17 ? 213 LYS A CA  1 
ATOM   1678 C  C   . LYS A 1 212 ? -18.773 -9.925  23.765  1.00  12.83 ? 213 LYS A C   1 
ATOM   1679 O  O   . LYS A 1 212 ? -18.229 -11.033 23.651  1.00  13.22 ? 213 LYS A O   1 
ATOM   1680 C  CB  . LYS A 1 212 ? -19.213 -9.053  26.101  1.00  15.12 ? 213 LYS A CB  1 
ATOM   1681 C  CG  . LYS A 1 212 ? -19.362 -10.481 26.616  1.00  21.97 ? 213 LYS A CG  1 
ATOM   1682 C  CD  . LYS A 1 212 ? -20.504 -10.691 27.632  1.00  22.55 ? 213 LYS A CD  1 
ATOM   1683 C  CE  . LYS A 1 212 ? -21.860 -10.054 27.240  1.00  28.24 ? 213 LYS A CE  1 
ATOM   1684 N  NZ  . LYS A 1 212 ? -22.285 -9.855  25.785  1.00  27.48 ? 213 LYS A NZ  1 
ATOM   1685 N  N   . GLU A 1 213 ? -19.823 -9.589  23.047  1.00  12.27 ? 214 GLU A N   1 
ATOM   1686 C  CA  . GLU A 1 213 ? -20.403 -10.479 22.030  1.00  13.29 ? 214 GLU A CA  1 
ATOM   1687 C  C   . GLU A 1 213 ? -19.614 -10.375 20.682  1.00  12.82 ? 214 GLU A C   1 
ATOM   1688 O  O   . GLU A 1 213 ? -19.552 -9.269  20.106  1.00  12.13 ? 214 GLU A O   1 
ATOM   1689 C  CB  . GLU A 1 213 ? -21.866 -10.127 21.807  1.00  16.65 ? 214 GLU A CB  1 
ATOM   1690 C  CG  . GLU A 1 213 ? -22.532 -11.078 20.803  1.00  19.07 ? 214 GLU A CG  1 
ATOM   1691 C  CD  . GLU A 1 213 ? -24.033 -10.807 20.633  1.00  21.33 ? 214 GLU A CD  1 
ATOM   1692 O  OE1 . GLU A 1 213 ? -24.580 -9.952  21.319  1.00  21.38 ? 214 GLU A OE1 1 
ATOM   1693 O  OE2 . GLU A 1 213 ? -24.671 -11.541 19.850  1.00  28.33 ? 214 GLU A OE2 1 
ATOM   1694 N  N   . PRO A 1 214 ? -18.965 -11.480 20.213  1.00  12.66 ? 215 PRO A N   1 
ATOM   1695 C  CA  . PRO A 1 214 ? -18.375 -11.414 18.902  1.00  12.92 ? 215 PRO A CA  1 
ATOM   1696 C  C   . PRO A 1 214 ? -19.449 -11.356 17.792  1.00  13.61 ? 215 PRO A C   1 
ATOM   1697 O  O   . PRO A 1 214 ? -20.642 -11.728 18.083  1.00  15.39 ? 215 PRO A O   1 
ATOM   1698 C  CB  . PRO A 1 214 ? -17.562 -12.730 18.789  1.00  15.10 ? 215 PRO A CB  1 
ATOM   1699 C  CG  . PRO A 1 214 ? -18.303 -13.681 19.693  1.00  15.09 ? 215 PRO A CG  1 
ATOM   1700 C  CD  . PRO A 1 214 ? -18.973 -12.857 20.784  1.00  13.59 ? 215 PRO A CD  1 
ATOM   1701 N  N   . ILE A 1 215 ? -19.073 -10.916 16.569  1.00  11.94 ? 216 ILE A N   1 
ATOM   1702 C  CA  . ILE A 1 215 ? -19.954 -11.177 15.408  1.00  12.77 ? 216 ILE A CA  1 
ATOM   1703 C  C   . ILE A 1 215 ? -19.416 -12.422 14.727  1.00  13.04 ? 216 ILE A C   1 
ATOM   1704 O  O   . ILE A 1 215 ? -18.196 -12.736 14.858  1.00  13.94 ? 216 ILE A O   1 
ATOM   1705 C  CB  . ILE A 1 215 ? -20.007 -9.989  14.380  1.00  12.40 ? 216 ILE A CB  1 
ATOM   1706 C  CG1 . ILE A 1 215 ? -18.596 -9.571  13.995  1.00  12.20 ? 216 ILE A CG1 1 
ATOM   1707 C  CG2 . ILE A 1 215 ? -20.696 -8.725  15.009  1.00  15.01 ? 216 ILE A CG2 1 
ATOM   1708 C  CD1 . ILE A 1 215 ? -18.568 -8.534  12.829  1.00  11.85 ? 216 ILE A CD1 1 
ATOM   1709 N  N   . SER A 1 216 ? -20.308 -13.201 14.110  1.00  13.44 ? 217 SER A N   1 
ATOM   1710 C  CA  . SER A 1 216 ? -19.831 -14.285 13.191  1.00  14.58 ? 217 SER A CA  1 
ATOM   1711 C  C   . SER A 1 216 ? -19.602 -13.826 11.760  1.00  13.64 ? 217 SER A C   1 
ATOM   1712 O  O   . SER A 1 216 ? -20.458 -13.127 11.199  1.00  16.96 ? 217 SER A O   1 
ATOM   1713 C  CB  . SER A 1 216 ? -20.817 -15.455 13.135  1.00  15.45 ? 217 SER A CB  1 
ATOM   1714 O  OG  . SER A 1 216 ? -20.847 -15.949 14.442  1.00  25.70 ? 217 SER A OG  1 
ATOM   1715 N  N   . VAL A 1 217 ? -18.525 -14.301 11.152  1.00  12.28 ? 218 VAL A N   1 
ATOM   1716 C  CA  . VAL A 1 217 ? -18.245 -14.078 9.744   1.00  13.37 ? 218 VAL A CA  1 
ATOM   1717 C  C   . VAL A 1 217 ? -17.959 -15.463 9.206   1.00  13.32 ? 218 VAL A C   1 
ATOM   1718 O  O   . VAL A 1 217 ? -17.618 -16.356 9.996   1.00  14.67 ? 218 VAL A O   1 
ATOM   1719 C  CB  . VAL A 1 217 ? -17.040 -13.142 9.458   1.00  12.72 ? 218 VAL A CB  1 
ATOM   1720 C  CG1 . VAL A 1 217 ? -17.287 -11.789 10.093  1.00  12.29 ? 218 VAL A CG1 1 
ATOM   1721 C  CG2 . VAL A 1 217 ? -15.672 -13.771 9.915   1.00  13.43 ? 218 VAL A CG2 1 
ATOM   1722 N  N   . SER A 1 218 ? -18.108 -15.640 7.908   1.00  14.05 ? 219 SER A N   1 
ATOM   1723 C  CA  . SER A 1 218 ? -17.896 -16.969 7.264   1.00  12.60 ? 219 SER A CA  1 
ATOM   1724 C  C   . SER A 1 218 ? -16.448 -17.209 6.950   1.00  12.75 ? 219 SER A C   1 
ATOM   1725 O  O   . SER A 1 218 ? -15.616 -16.284 6.877   1.00  9.87  ? 219 SER A O   1 
ATOM   1726 C  CB  . SER A 1 218 ? -18.721 -17.186 6.009   1.00  12.56 ? 219 SER A CB  1 
ATOM   1727 O  OG  . SER A 1 218 ? -18.301 -16.311 5.015   1.00  14.88 ? 219 SER A OG  1 
ATOM   1728 N  N   . SER A 1 219 ? -16.097 -18.481 6.801   1.00  13.70 ? 220 SER A N   1 
ATOM   1729 C  CA  . SER A 1 219 ? -14.728 -18.795 6.470   1.00  13.86 ? 220 SER A CA  1 
ATOM   1730 C  C   . SER A 1 219 ? -14.465 -18.127 5.136   1.00  16.13 ? 220 SER A C   1 
ATOM   1731 O  O   . SER A 1 219 ? -13.357 -17.611 4.923   1.00  17.27 ? 220 SER A O   1 
ATOM   1732 C  CB  . SER A 1 219 ? -14.509 -20.335 6.351   1.00  17.86 ? 220 SER A CB  1 
ATOM   1733 O  OG  . SER A 1 219 ? -15.625 -20.827 5.570   1.00  23.57 ? 220 SER A OG  1 
ATOM   1734 N  N   . GLU A 1 220 ? -15.460 -18.104 4.221   1.00  16.37 ? 221 GLU A N   1 
ATOM   1735 C  CA  . GLU A 1 220 ? -15.225 -17.472 2.877   1.00  17.01 ? 221 GLU A CA  1 
ATOM   1736 C  C   . GLU A 1 220 ? -14.876 -15.985 3.002   1.00  15.87 ? 221 GLU A C   1 
ATOM   1737 O  O   . GLU A 1 220 ? -14.005 -15.491 2.279   1.00  14.69 ? 221 GLU A O   1 
ATOM   1738 C  CB  . GLU A 1 220 ? -16.404 -17.629 1.971   1.00  19.26 ? 221 GLU A CB  1 
ATOM   1739 C  CG  . GLU A 1 220 ? -16.603 -19.087 1.529   1.00  22.60 ? 221 GLU A CG  1 
ATOM   1740 C  CD  . GLU A 1 220 ? -17.587 -19.829 2.445   1.00  26.70 ? 221 GLU A CD  1 
ATOM   1741 O  OE1 . GLU A 1 220 ? -17.885 -19.400 3.603   1.00  27.14 ? 221 GLU A OE1 1 
ATOM   1742 O  OE2 . GLU A 1 220 ? -18.081 -20.889 2.000   1.00  30.32 ? 221 GLU A OE2 1 
ATOM   1743 N  N   . GLN A 1 221 ? -15.537 -15.315 3.938   1.00  13.84 ? 222 GLN A N   1 
ATOM   1744 C  CA  . GLN A 1 221 ? -15.264 -13.883 4.173   1.00  14.97 ? 222 GLN A CA  1 
ATOM   1745 C  C   . GLN A 1 221 ? -13.823 -13.650 4.669   1.00  15.69 ? 222 GLN A C   1 
ATOM   1746 O  O   . GLN A 1 221 ? -13.064 -12.807 4.129   1.00  15.23 ? 222 GLN A O   1 
ATOM   1747 C  CB  . GLN A 1 221 ? -16.306 -13.385 5.169   1.00  14.00 ? 222 GLN A CB  1 
ATOM   1748 C  CG  . GLN A 1 221 ? -17.645 -13.116 4.454   1.00  13.93 ? 222 GLN A CG  1 
ATOM   1749 C  CD  . GLN A 1 221 ? -18.787 -12.575 5.325   1.00  13.72 ? 222 GLN A CD  1 
ATOM   1750 O  OE1 . GLN A 1 221 ? -18.942 -12.950 6.466   1.00  13.70 ? 222 GLN A OE1 1 
ATOM   1751 N  NE2 . GLN A 1 221 ? -19.579 -11.689 4.760   1.00  12.00 ? 222 GLN A NE2 1 
ATOM   1752 N  N   . VAL A 1 222 ? -13.399 -14.430 5.670   1.00  15.57 ? 223 VAL A N   1 
ATOM   1753 C  CA  . VAL A 1 222 ? -12.098 -14.178 6.306   1.00  16.84 ? 223 VAL A CA  1 
ATOM   1754 C  C   . VAL A 1 222 ? -11.007 -14.632 5.322   1.00  17.73 ? 223 VAL A C   1 
ATOM   1755 O  O   . VAL A 1 222 ? -9.936  -14.024 5.234   1.00  14.87 ? 223 VAL A O   1 
ATOM   1756 C  CB  . VAL A 1 222 ? -11.969 -14.801 7.719   1.00  17.39 ? 223 VAL A CB  1 
ATOM   1757 C  CG1 . VAL A 1 222 ? -11.915 -16.340 7.658   1.00  18.54 ? 223 VAL A CG1 1 
ATOM   1758 C  CG2 . VAL A 1 222 ? -10.763 -14.203 8.472   1.00  17.55 ? 223 VAL A CG2 1 
ATOM   1759 N  N   . LEU A 1 223 ? -11.330 -15.643 4.510   1.00  17.05 ? 224 LEU A N   1 
ATOM   1760 C  CA  . LEU A 1 223 ? -10.389 -16.101 3.530   1.00  18.32 ? 224 LEU A CA  1 
ATOM   1761 C  C   . LEU A 1 223 ? -10.036 -14.986 2.546   1.00  16.78 ? 224 LEU A C   1 
ATOM   1762 O  O   . LEU A 1 223 ? -8.908  -14.876 2.119   1.00  19.12 ? 224 LEU A O   1 
ATOM   1763 C  CB  . LEU A 1 223 ? -10.930 -17.368 2.792   1.00  19.82 ? 224 LEU A CB  1 
ATOM   1764 C  CG  . LEU A 1 223 ? -10.642 -18.639 3.636   1.00  21.74 ? 224 LEU A CG  1 
ATOM   1765 C  CD1 . LEU A 1 223 ? -11.471 -19.876 3.139   1.00  27.13 ? 224 LEU A CD1 1 
ATOM   1766 C  CD2 . LEU A 1 223 ? -9.117  -18.929 3.602   1.00  20.52 ? 224 LEU A CD2 1 
ATOM   1767 N  N   . LYS A 1 224 ? -11.012 -14.167 2.211   1.00  17.06 ? 225 LYS A N   1 
ATOM   1768 C  CA  . LYS A 1 224 ? -10.794 -13.063 1.308   1.00  16.33 ? 225 LYS A CA  1 
ATOM   1769 C  C   . LYS A 1 224 ? -9.905  -11.954 1.901   1.00  16.57 ? 225 LYS A C   1 
ATOM   1770 O  O   . LYS A 1 224 ? -9.113  -11.325 1.154   1.00  15.20 ? 225 LYS A O   1 
ATOM   1771 C  CB  . LYS A 1 224 ? -12.120 -12.556 0.764   1.00  18.57 ? 225 LYS A CB  1 
ATOM   1772 C  CG  . LYS A 1 224 ? -12.726 -13.596 -0.227  1.00  20.87 ? 225 LYS A CG  1 
ATOM   1773 C  CD  . LYS A 1 224 ? -14.008 -13.148 -0.893  1.00  27.09 ? 225 LYS A CD  1 
ATOM   1774 C  CE  . LYS A 1 224 ? -14.523 -14.337 -1.714  1.00  32.54 ? 225 LYS A CE  1 
ATOM   1775 N  NZ  . LYS A 1 224 ? -15.770 -14.010 -2.463  1.00  33.87 ? 225 LYS A NZ  1 
ATOM   1776 N  N   . PHE A 1 225 ? -10.015 -11.717 3.223   1.00  15.88 ? 226 PHE A N   1 
ATOM   1777 C  CA  . PHE A 1 225 ? -9.040  -10.902 3.974   1.00  13.82 ? 226 PHE A CA  1 
ATOM   1778 C  C   . PHE A 1 225 ? -7.607  -11.411 3.749   1.00  14.32 ? 226 PHE A C   1 
ATOM   1779 O  O   . PHE A 1 225 ? -6.675  -10.661 3.526   1.00  13.10 ? 226 PHE A O   1 
ATOM   1780 C  CB  . PHE A 1 225 ? -9.288  -10.977 5.482   1.00  14.83 ? 226 PHE A CB  1 
ATOM   1781 C  CG  . PHE A 1 225 ? -10.404 -10.080 6.006   1.00  16.48 ? 226 PHE A CG  1 
ATOM   1782 C  CD1 . PHE A 1 225 ? -11.428 -9.661  5.225   1.00  15.72 ? 226 PHE A CD1 1 
ATOM   1783 C  CD2 . PHE A 1 225 ? -10.450 -9.772  7.391   1.00  19.24 ? 226 PHE A CD2 1 
ATOM   1784 C  CE1 . PHE A 1 225 ? -12.480 -8.874  5.743   1.00  18.10 ? 226 PHE A CE1 1 
ATOM   1785 C  CE2 . PHE A 1 225 ? -11.497 -9.024  7.920   1.00  20.35 ? 226 PHE A CE2 1 
ATOM   1786 C  CZ  . PHE A 1 225 ? -12.515 -8.549  7.079   1.00  18.78 ? 226 PHE A CZ  1 
ATOM   1787 N  N   . ARG A 1 226 ? -7.425  -12.721 3.865   1.00  14.56 ? 227 ARG A N   1 
ATOM   1788 C  CA  . ARG A 1 226 ? -6.098  -13.344 3.789   1.00  14.91 ? 227 ARG A CA  1 
ATOM   1789 C  C   . ARG A 1 226 ? -5.505  -13.349 2.364   1.00  15.31 ? 227 ARG A C   1 
ATOM   1790 O  O   . ARG A 1 226 ? -4.360  -13.743 2.209   1.00  16.71 ? 227 ARG A O   1 
ATOM   1791 C  CB  . ARG A 1 226 ? -6.277  -14.790 4.254   1.00  14.27 ? 227 ARG A CB  1 
ATOM   1792 C  CG  . ARG A 1 226 ? -6.673  -14.912 5.724   1.00  12.58 ? 227 ARG A CG  1 
ATOM   1793 C  CD  . ARG A 1 226 ? -6.511  -16.374 6.231   1.00  14.84 ? 227 ARG A CD  1 
ATOM   1794 N  NE  . ARG A 1 226 ? -7.084  -16.432 7.595   1.00  16.43 ? 227 ARG A NE  1 
ATOM   1795 C  CZ  . ARG A 1 226 ? -8.025  -17.296 7.958   1.00  16.64 ? 227 ARG A CZ  1 
ATOM   1796 N  NH1 . ARG A 1 226 ? -8.393  -18.258 7.096   1.00  15.74 ? 227 ARG A NH1 1 
ATOM   1797 N  NH2 . ARG A 1 226 ? -8.538  -17.224 9.163   1.00  15.42 ? 227 ARG A NH2 1 
ATOM   1798 N  N   . LYS A 1 227 ? -6.278  -12.923 1.370   1.00  16.36 ? 228 LYS A N   1 
ATOM   1799 C  CA  . LYS A 1 227 ? -5.815  -12.834 -0.005  1.00  18.02 ? 228 LYS A CA  1 
ATOM   1800 C  C   . LYS A 1 227 ? -5.190  -11.461 -0.267  1.00  18.46 ? 228 LYS A C   1 
ATOM   1801 O  O   . LYS A 1 227 ? -4.527  -11.243 -1.266  1.00  17.52 ? 228 LYS A O   1 
ATOM   1802 C  CB  . LYS A 1 227 ? -6.998  -13.058 -0.963  1.00  19.52 ? 228 LYS A CB  1 
ATOM   1803 C  CG  . LYS A 1 227 ? -7.299  -14.546 -1.185  1.00  26.68 ? 228 LYS A CG  1 
ATOM   1804 C  CD  . LYS A 1 227 ? -8.523  -14.778 -2.075  1.00  29.85 ? 228 LYS A CD  1 
ATOM   1805 C  CE  . LYS A 1 227 ? -8.221  -14.596 -3.570  1.00  36.28 ? 228 LYS A CE  1 
ATOM   1806 N  NZ  . LYS A 1 227 ? -8.124  -15.885 -4.298  1.00  47.79 ? 228 LYS A NZ  1 
ATOM   1807 N  N   . LEU A 1 228 ? -5.390  -10.527 0.653   1.00  17.18 ? 229 LEU A N   1 
ATOM   1808 C  CA  . LEU A 1 228 ? -4.727  -9.211  0.510   1.00  15.76 ? 229 LEU A CA  1 
ATOM   1809 C  C   . LEU A 1 228 ? -3.209  -9.352  0.654   1.00  16.21 ? 229 LEU A C   1 
ATOM   1810 O  O   . LEU A 1 228 ? -2.709  -10.356 1.134   1.00  16.59 ? 229 LEU A O   1 
ATOM   1811 C  CB  . LEU A 1 228 ? -5.254  -8.261  1.583   1.00  13.48 ? 229 LEU A CB  1 
ATOM   1812 C  CG  . LEU A 1 228 ? -6.691  -7.736  1.495   1.00  14.44 ? 229 LEU A CG  1 
ATOM   1813 C  CD1 . LEU A 1 228 ? -6.970  -6.921  2.739   1.00  12.88 ? 229 LEU A CD1 1 
ATOM   1814 C  CD2 . LEU A 1 228 ? -6.851  -6.815  0.288   1.00  14.93 ? 229 LEU A CD2 1 
ATOM   1815 N  N   . ASN A 1 229 ? -2.462  -8.341  0.204   1.00  17.32 ? 230 ASN A N   1 
ATOM   1816 C  CA  . ASN A 1 229 ? -1.033  -8.319  0.287   1.00  16.61 ? 230 ASN A CA  1 
ATOM   1817 C  C   . ASN A 1 229 ? -0.474  -7.131  1.121   1.00  17.06 ? 230 ASN A C   1 
ATOM   1818 O  O   . ASN A 1 229 ? -0.961  -5.984  1.060   1.00  16.42 ? 230 ASN A O   1 
ATOM   1819 C  CB  . ASN A 1 229 ? -0.445  -8.117  -1.111  1.00  18.10 ? 230 ASN A CB  1 
ATOM   1820 C  CG  . ASN A 1 229 ? -0.599  -9.308  -2.040  1.00  22.24 ? 230 ASN A CG  1 
ATOM   1821 O  OD1 . ASN A 1 229 ? -0.069  -9.234  -3.159  1.00  21.68 ? 230 ASN A OD1 1 
ATOM   1822 N  ND2 . ASN A 1 229 ? -1.275  -10.415 -1.602  1.00  18.47 ? 230 ASN A ND2 1 
ATOM   1823 N  N   . PHE A 1 230 ? 0.638   -7.411  1.798   1.00  18.61 ? 231 PHE A N   1 
ATOM   1824 C  CA  . PHE A 1 230 ? 1.424   -6.397  2.518   1.00  19.92 ? 231 PHE A CA  1 
ATOM   1825 C  C   . PHE A 1 230 ? 2.315   -5.627  1.482   1.00  23.43 ? 231 PHE A C   1 
ATOM   1826 O  O   . PHE A 1 230 ? 2.547   -4.414  1.631   1.00  20.38 ? 231 PHE A O   1 
ATOM   1827 C  CB  . PHE A 1 230 ? 2.392   -7.070  3.457   1.00  19.45 ? 231 PHE A CB  1 
ATOM   1828 C  CG  . PHE A 1 230 ? 1.824   -7.593  4.772   1.00  19.70 ? 231 PHE A CG  1 
ATOM   1829 C  CD1 . PHE A 1 230 ? 1.075   -6.797  5.624   1.00  19.91 ? 231 PHE A CD1 1 
ATOM   1830 C  CD2 . PHE A 1 230 ? 2.205   -8.858  5.208   1.00  19.38 ? 231 PHE A CD2 1 
ATOM   1831 C  CE1 . PHE A 1 230 ? 0.672   -7.283  6.873   1.00  20.77 ? 231 PHE A CE1 1 
ATOM   1832 C  CE2 . PHE A 1 230 ? 1.818   -9.334  6.455   1.00  18.41 ? 231 PHE A CE2 1 
ATOM   1833 C  CZ  . PHE A 1 230 ? 1.055   -8.555  7.275   1.00  16.78 ? 231 PHE A CZ  1 
ATOM   1834 N  N   . ASN A 1 231 ? 2.877   -6.355  0.494   1.00  22.29 ? 232 ASN A N   1 
ATOM   1835 C  CA  . ASN A 1 231 ? 3.755   -5.723  -0.520  1.00  24.93 ? 232 ASN A CA  1 
ATOM   1836 C  C   . ASN A 1 231 ? 2.990   -4.809  -1.460  1.00  23.53 ? 232 ASN A C   1 
ATOM   1837 O  O   . ASN A 1 231 ? 1.784   -4.894  -1.545  1.00  20.71 ? 232 ASN A O   1 
ATOM   1838 C  CB  . ASN A 1 231 ? 4.411   -6.785  -1.370  1.00  23.13 ? 232 ASN A CB  1 
ATOM   1839 C  CG  . ASN A 1 231 ? 3.412   -7.756  -1.901  1.00  24.83 ? 232 ASN A CG  1 
ATOM   1840 O  OD1 . ASN A 1 231 ? 2.900   -8.607  -1.164  1.00  24.93 ? 232 ASN A OD1 1 
ATOM   1841 N  ND2 . ASN A 1 231 ? 3.089   -7.621  -3.165  1.00  27.06 ? 232 ASN A ND2 1 
ATOM   1842 N  N   . GLY A 1 232 ? 3.705   -3.945  -2.195  1.00  24.25 ? 233 GLY A N   1 
ATOM   1843 C  CA  . GLY A 1 232 ? 3.052   -3.113  -3.211  1.00  24.62 ? 233 GLY A CA  1 
ATOM   1844 C  C   . GLY A 1 232 ? 3.047   -3.828  -4.569  1.00  27.38 ? 233 GLY A C   1 
ATOM   1845 O  O   . GLY A 1 232 ? 3.841   -4.722  -4.764  1.00  26.90 ? 233 GLY A O   1 
ATOM   1846 N  N   . GLU A 1 233 ? 2.146   -3.424  -5.473  1.00  32.29 ? 234 GLU A N   1 
ATOM   1847 C  CA  . GLU A 1 233 ? 2.019   -4.016  -6.843  1.00  33.63 ? 234 GLU A CA  1 
ATOM   1848 C  C   . GLU A 1 233 ? 3.366   -4.103  -7.515  1.00  32.28 ? 234 GLU A C   1 
ATOM   1849 O  O   . GLU A 1 233 ? 4.172   -3.188  -7.429  1.00  27.56 ? 234 GLU A O   1 
ATOM   1850 C  CB  . GLU A 1 233 ? 1.062   -3.227  -7.741  1.00  33.95 ? 234 GLU A CB  1 
ATOM   1851 C  CG  . GLU A 1 233 ? 0.827   -3.871  -9.118  1.00  37.47 ? 234 GLU A CG  1 
ATOM   1852 C  CD  . GLU A 1 233 ? 0.067   -2.967  -10.045 1.00  42.10 ? 234 GLU A CD  1 
ATOM   1853 O  OE1 . GLU A 1 233 ? -0.604  -2.032  -9.567  1.00  50.57 ? 234 GLU A OE1 1 
ATOM   1854 O  OE2 . GLU A 1 233 ? 0.145   -3.160  -11.266 1.00  46.64 ? 234 GLU A OE2 1 
ATOM   1855 N  N   . GLY A 1 234 ? 3.591   -5.231  -8.165  1.00  32.92 ? 235 GLY A N   1 
ATOM   1856 C  CA  . GLY A 1 234 ? 4.912   -5.553  -8.704  1.00  37.54 ? 235 GLY A CA  1 
ATOM   1857 C  C   . GLY A 1 234 ? 6.039   -5.731  -7.708  1.00  35.04 ? 235 GLY A C   1 
ATOM   1858 O  O   . GLY A 1 234 ? 7.200   -5.418  -7.994  1.00  34.31 ? 235 GLY A O   1 
ATOM   1859 N  N   . GLU A 1 235 ? 5.711   -6.230  -6.525  1.00  35.96 ? 236 GLU A N   1 
ATOM   1860 C  CA  . GLU A 1 235 ? 6.732   -6.757  -5.593  1.00  34.35 ? 236 GLU A CA  1 
ATOM   1861 C  C   . GLU A 1 235 ? 6.411   -8.228  -5.232  1.00  34.13 ? 236 GLU A C   1 
ATOM   1862 O  O   . GLU A 1 235 ? 5.318   -8.722  -5.573  1.00  34.21 ? 236 GLU A O   1 
ATOM   1863 C  CB  . GLU A 1 235 ? 6.765   -5.930  -4.329  1.00  43.69 ? 236 GLU A CB  1 
ATOM   1864 C  CG  . GLU A 1 235 ? 6.907   -4.448  -4.572  1.00  46.42 ? 236 GLU A CG  1 
ATOM   1865 C  CD  . GLU A 1 235 ? 7.527   -3.764  -3.391  1.00  49.35 ? 236 GLU A CD  1 
ATOM   1866 O  OE1 . GLU A 1 235 ? 7.120   -2.628  -3.089  1.00  44.95 ? 236 GLU A OE1 1 
ATOM   1867 O  OE2 . GLU A 1 235 ? 8.430   -4.380  -2.782  1.00  55.27 ? 236 GLU A OE2 1 
ATOM   1868 N  N   . PRO A 1 236 ? 7.337   -8.925  -4.565  1.00  30.07 ? 237 PRO A N   1 
ATOM   1869 C  CA  . PRO A 1 236 ? 7.053   -10.341 -4.223  1.00  33.09 ? 237 PRO A CA  1 
ATOM   1870 C  C   . PRO A 1 236 ? 5.839   -10.460 -3.257  1.00  32.28 ? 237 PRO A C   1 
ATOM   1871 O  O   . PRO A 1 236 ? 5.634   -9.606  -2.379  1.00  26.77 ? 237 PRO A O   1 
ATOM   1872 C  CB  . PRO A 1 236 ? 8.323   -10.797 -3.533  1.00  31.86 ? 237 PRO A CB  1 
ATOM   1873 C  CG  . PRO A 1 236 ? 9.369   -9.810  -3.929  1.00  33.70 ? 237 PRO A CG  1 
ATOM   1874 C  CD  . PRO A 1 236 ? 8.661   -8.506  -4.084  1.00  32.47 ? 237 PRO A CD  1 
ATOM   1875 N  N   . GLU A 1 237 ? 5.023   -11.480 -3.457  1.00  28.93 ? 238 GLU A N   1 
ATOM   1876 C  CA  . GLU A 1 237 ? 3.773   -11.568 -2.728  1.00  24.63 ? 238 GLU A CA  1 
ATOM   1877 C  C   . GLU A 1 237 ? 4.043   -11.930 -1.251  1.00  23.55 ? 238 GLU A C   1 
ATOM   1878 O  O   . GLU A 1 237 ? 4.657   -12.935 -0.944  1.00  22.00 ? 238 GLU A O   1 
ATOM   1879 C  CB  . GLU A 1 237 ? 2.800   -12.553 -3.381  1.00  24.88 ? 238 GLU A CB  1 
ATOM   1880 C  CG  . GLU A 1 237 ? 1.435   -12.436 -2.734  1.00  23.22 ? 238 GLU A CG  1 
ATOM   1881 C  CD  . GLU A 1 237 ? 0.308   -13.236 -3.356  1.00  27.83 ? 238 GLU A CD  1 
ATOM   1882 O  OE1 . GLU A 1 237 ? 0.591   -14.364 -3.763  1.00  32.63 ? 238 GLU A OE1 1 
ATOM   1883 O  OE2 . GLU A 1 237 ? -0.885  -12.758 -3.379  1.00  27.57 ? 238 GLU A OE2 1 
ATOM   1884 N  N   . GLU A 1 238 ? 3.591   -11.085 -0.335  1.00  21.26 ? 239 GLU A N   1 
ATOM   1885 C  CA  . GLU A 1 238 ? 3.606   -11.421 1.077   1.00  22.74 ? 239 GLU A CA  1 
ATOM   1886 C  C   . GLU A 1 238 ? 2.144   -11.331 1.504   1.00  19.82 ? 239 GLU A C   1 
ATOM   1887 O  O   . GLU A 1 238 ? 1.569   -10.255 1.439   1.00  17.56 ? 239 GLU A O   1 
ATOM   1888 C  CB  . GLU A 1 238 ? 4.478   -10.415 1.832   1.00  26.92 ? 239 GLU A CB  1 
ATOM   1889 C  CG  . GLU A 1 238 ? 5.940   -10.852 1.740   1.00  37.82 ? 239 GLU A CG  1 
ATOM   1890 C  CD  . GLU A 1 238 ? 6.898   -10.118 2.666   1.00  47.93 ? 239 GLU A CD  1 
ATOM   1891 O  OE1 . GLU A 1 238 ? 7.147   -8.885  2.434   1.00  49.40 ? 239 GLU A OE1 1 
ATOM   1892 O  OE2 . GLU A 1 238 ? 7.394   -10.802 3.607   1.00  42.16 ? 239 GLU A OE2 1 
ATOM   1893 N  N   . LEU A 1 239 ? 1.496   -12.465 1.837   1.00  15.52 ? 240 LEU A N   1 
ATOM   1894 C  CA  . LEU A 1 239 ? 0.083   -12.349 2.168   1.00  14.05 ? 240 LEU A CA  1 
ATOM   1895 C  C   . LEU A 1 239 ? -0.105  -11.506 3.473   1.00  13.45 ? 240 LEU A C   1 
ATOM   1896 O  O   . LEU A 1 239 ? 0.708   -11.667 4.406   1.00  13.66 ? 240 LEU A O   1 
ATOM   1897 C  CB  . LEU A 1 239 ? -0.482  -13.750 2.409   1.00  13.92 ? 240 LEU A CB  1 
ATOM   1898 C  CG  . LEU A 1 239 ? -0.496  -14.597 1.111   1.00  13.72 ? 240 LEU A CG  1 
ATOM   1899 C  CD1 . LEU A 1 239 ? -1.213  -15.867 1.499   1.00  17.51 ? 240 LEU A CD1 1 
ATOM   1900 C  CD2 . LEU A 1 239 ? -1.309  -13.960 0.023   1.00  15.32 ? 240 LEU A CD2 1 
ATOM   1901 N  N   . MET A 1 240 ? -1.105  -10.617 3.462   1.00  11.96 ? 241 MET A N   1 
ATOM   1902 C  CA  . MET A 1 240 ? -1.500  -9.791  4.623   1.00  12.56 ? 241 MET A CA  1 
ATOM   1903 C  C   . MET A 1 240 ? -2.274  -10.735 5.539   1.00  12.11 ? 241 MET A C   1 
ATOM   1904 O  O   . MET A 1 240 ? -3.509  -10.923 5.374   1.00  12.08 ? 241 MET A O   1 
ATOM   1905 C  CB  . MET A 1 240 ? -2.414  -8.643  4.206   1.00  13.59 ? 241 MET A CB  1 
ATOM   1906 C  CG  . MET A 1 240 ? -2.526  -7.495  5.245   1.00  14.69 ? 241 MET A CG  1 
ATOM   1907 S  SD  . MET A 1 240 ? -3.667  -6.224  4.726   1.00  19.24 ? 241 MET A SD  1 
ATOM   1908 C  CE  . MET A 1 240 ? -2.527  -5.017  4.013   1.00  20.40 ? 241 MET A CE  1 
ATOM   1909 N  N   . VAL A 1 241 ? -1.501  -11.349 6.415   1.00  12.32 ? 242 VAL A N   1 
ATOM   1910 C  CA  . VAL A 1 241 ? -2.004  -12.154 7.527   1.00  13.74 ? 242 VAL A CA  1 
ATOM   1911 C  C   . VAL A 1 241 ? -1.247  -11.863 8.817   1.00  13.62 ? 242 VAL A C   1 
ATOM   1912 O  O   . VAL A 1 241 ? -0.074  -11.459 8.782   1.00  14.37 ? 242 VAL A O   1 
ATOM   1913 C  CB  . VAL A 1 241 ? -1.929  -13.695 7.252   1.00  12.61 ? 242 VAL A CB  1 
ATOM   1914 C  CG1 . VAL A 1 241 ? -2.869  -14.055 6.092   1.00  12.85 ? 242 VAL A CG1 1 
ATOM   1915 C  CG2 . VAL A 1 241 ? -0.504  -14.164 7.049   1.00  14.25 ? 242 VAL A CG2 1 
ATOM   1916 N  N   . ASP A 1 242 ? -1.888  -12.193 9.944   1.00  11.91 ? 243 ASP A N   1 
ATOM   1917 C  CA  . ASP A 1 242 ? -1.260  -12.058 11.253  1.00  12.30 ? 243 ASP A CA  1 
ATOM   1918 C  C   . ASP A 1 242 ? -0.761  -10.638 11.476  1.00  11.70 ? 243 ASP A C   1 
ATOM   1919 O  O   . ASP A 1 242 ? 0.350   -10.474 11.937  1.00  12.51 ? 243 ASP A O   1 
ATOM   1920 C  CB  . ASP A 1 242 ? -0.103  -13.067 11.484  1.00  12.58 ? 243 ASP A CB  1 
ATOM   1921 C  CG  . ASP A 1 242 ? -0.635  -14.500 11.582  1.00  12.14 ? 243 ASP A CG  1 
ATOM   1922 O  OD1 . ASP A 1 242 ? -1.685  -14.670 12.187  1.00  13.86 ? 243 ASP A OD1 1 
ATOM   1923 O  OD2 . ASP A 1 242 ? -0.072  -15.438 10.979  1.00  12.39 ? 243 ASP A OD2 1 
ATOM   1924 N  N   . ASN A 1 243 ? -1.639  -9.667  11.178  1.00  11.59 ? 244 ASN A N   1 
ATOM   1925 C  CA  . ASN A 1 243 ? -1.283  -8.262  11.404  1.00  11.33 ? 244 ASN A CA  1 
ATOM   1926 C  C   . ASN A 1 243 ? -1.826  -7.855  12.780  1.00  11.78 ? 244 ASN A C   1 
ATOM   1927 O  O   . ASN A 1 243 ? -2.474  -6.814  12.879  1.00  13.22 ? 244 ASN A O   1 
ATOM   1928 C  CB  . ASN A 1 243 ? -1.841  -7.364  10.305  1.00  12.21 ? 244 ASN A CB  1 
ATOM   1929 C  CG  . ASN A 1 243 ? -3.280  -7.623  9.973   1.00  11.62 ? 244 ASN A CG  1 
ATOM   1930 O  OD1 . ASN A 1 243 ? -3.904  -8.511  10.517  1.00  12.15 ? 244 ASN A OD1 1 
ATOM   1931 N  ND2 . ASN A 1 243 ? -3.860  -6.753  9.107   1.00  11.71 ? 244 ASN A ND2 1 
ATOM   1932 N  N   . TRP A 1 244 ? -1.544  -8.634  13.818  1.00  10.46 ? 245 TRP A N   1 
ATOM   1933 C  CA  . TRP A 1 244 ? -2.005  -8.379  15.215  1.00  11.74 ? 245 TRP A CA  1 
ATOM   1934 C  C   . TRP A 1 244 ? -0.838  -8.224  16.140  1.00  11.70 ? 245 TRP A C   1 
ATOM   1935 O  O   . TRP A 1 244 ? 0.249   -8.862  16.004  1.00  12.17 ? 245 TRP A O   1 
ATOM   1936 C  CB  . TRP A 1 244 ? -3.064  -9.418  15.778  1.00  11.24 ? 245 TRP A CB  1 
ATOM   1937 C  CG  . TRP A 1 244 ? -2.602  -10.822 15.598  1.00  11.75 ? 245 TRP A CG  1 
ATOM   1938 C  CD1 . TRP A 1 244 ? -2.588  -11.548 14.453  1.00  11.73 ? 245 TRP A CD1 1 
ATOM   1939 C  CD2 . TRP A 1 244 ? -1.986  -11.715 16.621  1.00  12.14 ? 245 TRP A CD2 1 
ATOM   1940 N  NE1 . TRP A 1 244 ? -2.075  -12.815 14.677  1.00  10.20 ? 245 TRP A NE1 1 
ATOM   1941 C  CE2 . TRP A 1 244 ? -1.715  -12.958 15.952  1.00  12.64 ? 245 TRP A CE2 1 
ATOM   1942 C  CE3 . TRP A 1 244 ? -1.733  -11.612 17.977  1.00  12.13 ? 245 TRP A CE3 1 
ATOM   1943 C  CZ2 . TRP A 1 244 ? -1.129  -14.032 16.620  1.00  11.86 ? 245 TRP A CZ2 1 
ATOM   1944 C  CZ3 . TRP A 1 244 ? -1.114  -12.691 18.631  1.00  12.98 ? 245 TRP A CZ3 1 
ATOM   1945 C  CH2 . TRP A 1 244 ? -0.849  -13.866 17.947  1.00  13.61 ? 245 TRP A CH2 1 
ATOM   1946 N  N   . ARG A 1 245 ? -0.984  -7.291  17.071  1.00  11.31 ? 246 ARG A N   1 
ATOM   1947 C  CA  . ARG A 1 245 ? -0.018  -7.137  18.146  1.00  12.54 ? 246 ARG A CA  1 
ATOM   1948 C  C   . ARG A 1 245 ? -0.493  -8.051  19.312  1.00  12.31 ? 246 ARG A C   1 
ATOM   1949 O  O   . ARG A 1 245 ? -1.707  -8.062  19.661  1.00  13.80 ? 246 ARG A O   1 
ATOM   1950 C  CB  . ARG A 1 245 ? -0.006  -5.649  18.653  1.00  11.63 ? 246 ARG A CB  1 
ATOM   1951 C  CG  . ARG A 1 245 ? 1.163   -5.477  19.601  1.00  10.89 ? 246 ARG A CG  1 
ATOM   1952 C  CD  . ARG A 1 245 ? 1.061   -4.190  20.435  1.00  10.83 ? 246 ARG A CD  1 
ATOM   1953 N  NE  . ARG A 1 245 ? 2.381   -3.870  21.068  1.00  11.53 ? 246 ARG A NE  1 
ATOM   1954 C  CZ  . ARG A 1 245 ? 2.542   -2.844  21.908  1.00  12.79 ? 246 ARG A CZ  1 
ATOM   1955 N  NH1 . ARG A 1 245 ? 1.486   -2.043  22.247  1.00  10.88 ? 246 ARG A NH1 1 
ATOM   1956 N  NH2 . ARG A 1 245 ? 3.761   -2.610  22.390  1.00  12.71 ? 246 ARG A NH2 1 
ATOM   1957 N  N   . PRO A 1 246 ? 0.425   -8.834  19.916  1.00  11.92 ? 247 PRO A N   1 
ATOM   1958 C  CA  . PRO A 1 246 ? 0.002   -9.704  21.018  1.00  11.97 ? 247 PRO A CA  1 
ATOM   1959 C  C   . PRO A 1 246 ? -0.342  -8.908  22.268  1.00  10.98 ? 247 PRO A C   1 
ATOM   1960 O  O   . PRO A 1 246 ? 0.123   -7.763  22.461  1.00  10.37 ? 247 PRO A O   1 
ATOM   1961 C  CB  . PRO A 1 246 ? 1.290   -10.531 21.292  1.00  12.68 ? 247 PRO A CB  1 
ATOM   1962 C  CG  . PRO A 1 246 ? 2.156   -10.280 20.087  1.00  14.61 ? 247 PRO A CG  1 
ATOM   1963 C  CD  . PRO A 1 246 ? 1.876   -8.862  19.785  1.00  13.44 ? 247 PRO A CD  1 
ATOM   1964 N  N   . ALA A 1 247 ? -1.059  -9.568  23.163  1.00  11.94 ? 248 ALA A N   1 
ATOM   1965 C  CA  . ALA A 1 247 ? -1.313  -8.988  24.488  1.00  11.28 ? 248 ALA A CA  1 
ATOM   1966 C  C   . ALA A 1 247 ? -0.080  -8.433  25.197  1.00  12.47 ? 248 ALA A C   1 
ATOM   1967 O  O   . ALA A 1 247 ? 0.967   -9.076  25.246  1.00  11.20 ? 248 ALA A O   1 
ATOM   1968 C  CB  . ALA A 1 247 ? -2.116  -9.972  25.386  1.00  12.93 ? 248 ALA A CB  1 
ATOM   1969 N  N   . GLN A 1 248 ? -0.241  -7.253  25.805  1.00  11.06 ? 249 GLN A N   1 
ATOM   1970 C  CA  . GLN A 1 248 ? 0.843   -6.554  26.500  1.00  11.96 ? 249 GLN A CA  1 
ATOM   1971 C  C   . GLN A 1 248 ? 0.527   -6.584  28.021  1.00  13.28 ? 249 GLN A C   1 
ATOM   1972 O  O   . GLN A 1 248 ? -0.657  -6.828  28.402  1.00  12.44 ? 249 GLN A O   1 
ATOM   1973 C  CB  . GLN A 1 248 ? 0.882   -5.126  26.026  1.00  12.24 ? 249 GLN A CB  1 
ATOM   1974 C  CG  . GLN A 1 248 ? 1.150   -4.973  24.522  1.00  11.80 ? 249 GLN A CG  1 
ATOM   1975 C  CD  . GLN A 1 248 ? 2.429   -5.679  24.152  1.00  13.12 ? 249 GLN A CD  1 
ATOM   1976 O  OE1 . GLN A 1 248 ? 3.509   -5.370  24.691  1.00  14.84 ? 249 GLN A OE1 1 
ATOM   1977 N  NE2 . GLN A 1 248 ? 2.318   -6.692  23.309  1.00  13.45 ? 249 GLN A NE2 1 
ATOM   1978 N  N   . PRO A 1 249 ? 1.545   -6.311  28.894  1.00  14.46 ? 250 PRO A N   1 
ATOM   1979 C  CA  . PRO A 1 249 ? 1.394   -6.300  30.359  1.00  14.76 ? 250 PRO A CA  1 
ATOM   1980 C  C   . PRO A 1 249 ? 0.327   -5.305  30.793  1.00  15.26 ? 250 PRO A C   1 
ATOM   1981 O  O   . PRO A 1 249 ? 0.381   -4.102  30.417  1.00  15.12 ? 250 PRO A O   1 
ATOM   1982 C  CB  . PRO A 1 249 ? 2.730   -5.729  30.845  1.00  14.50 ? 250 PRO A CB  1 
ATOM   1983 C  CG  . PRO A 1 249 ? 3.693   -6.181  29.807  1.00  16.48 ? 250 PRO A CG  1 
ATOM   1984 C  CD  . PRO A 1 249 ? 2.941   -5.993  28.496  1.00  13.43 ? 250 PRO A CD  1 
ATOM   1985 N  N   . LEU A 1 250 ? -0.597  -5.804  31.596  1.00  15.47 ? 251 LEU A N   1 
ATOM   1986 C  CA  . LEU A 1 250 ? -1.712  -4.971  32.081  1.00  16.08 ? 251 LEU A CA  1 
ATOM   1987 C  C   . LEU A 1 250 ? -1.152  -3.907  33.014  1.00  16.40 ? 251 LEU A C   1 
ATOM   1988 O  O   . LEU A 1 250 ? -1.628  -2.757  33.036  1.00  13.99 ? 251 LEU A O   1 
ATOM   1989 C  CB  . LEU A 1 250 ? -2.731  -5.812  32.853  1.00  16.82 ? 251 LEU A CB  1 
ATOM   1990 C  CG  . LEU A 1 250 ? -4.000  -5.090  33.232  1.00  15.68 ? 251 LEU A CG  1 
ATOM   1991 C  CD1 . LEU A 1 250 ? -4.726  -4.468  32.033  1.00  13.82 ? 251 LEU A CD1 1 
ATOM   1992 C  CD2 . LEU A 1 250 ? -4.905  -6.057  34.032  1.00  17.38 ? 251 LEU A CD2 1 
ATOM   1993 N  N   . LYS A 1 251 ? -0.168  -4.300  33.829  1.00  17.87 ? 252 LYS A N   1 
ATOM   1994 C  CA  . LYS A 1 251 ? 0.441   -3.308  34.772  1.00  20.10 ? 252 LYS A CA  1 
ATOM   1995 C  C   . LYS A 1 251 ? -0.503  -2.691  35.772  1.00  20.58 ? 252 LYS A C   1 
ATOM   1996 O  O   . LYS A 1 251 ? -1.357  -3.347  36.364  1.00  22.16 ? 252 LYS A O   1 
ATOM   1997 C  CB  . LYS A 1 251 ? 1.204   -2.230  33.991  1.00  18.37 ? 252 LYS A CB  1 
ATOM   1998 C  CG  . LYS A 1 251 ? 2.509   -2.839  33.521  1.00  22.42 ? 252 LYS A CG  1 
ATOM   1999 C  CD  . LYS A 1 251 ? 3.211   -2.020  32.473  1.00  24.04 ? 252 LYS A CD  1 
ATOM   2000 C  CE  . LYS A 1 251 ? 4.696   -2.393  32.496  1.00  29.51 ? 252 LYS A CE  1 
ATOM   2001 N  NZ  . LYS A 1 251 ? 5.342   -1.823  31.270  1.00  26.77 ? 252 LYS A NZ  1 
ATOM   2002 N  N   . ASN A 1 252 ? -0.388  -1.393  35.929  1.00  24.38 ? 253 ASN A N   1 
ATOM   2003 C  CA  . ASN A 1 252 ? -1.176  -0.789  36.952  1.00  31.93 ? 253 ASN A CA  1 
ATOM   2004 C  C   . ASN A 1 252 ? -2.575  -0.307  36.442  1.00  28.37 ? 253 ASN A C   1 
ATOM   2005 O  O   . ASN A 1 252 ? -2.878  0.926   36.536  1.00  27.94 ? 253 ASN A O   1 
ATOM   2006 C  CB  . ASN A 1 252 ? -0.361  0.320   37.636  1.00  34.74 ? 253 ASN A CB  1 
ATOM   2007 C  CG  . ASN A 1 252 ? -1.100  0.921   38.810  1.00  44.54 ? 253 ASN A CG  1 
ATOM   2008 O  OD1 . ASN A 1 252 ? -1.664  0.196   39.644  1.00  43.90 ? 253 ASN A OD1 1 
ATOM   2009 N  ND2 . ASN A 1 252 ? -1.161  2.251   38.847  1.00  45.86 ? 253 ASN A ND2 1 
ATOM   2010 N  N   . ARG A 1 253 ? -3.372  -1.255  35.868  1.00  21.66 ? 254 ARG A N   1 
ATOM   2011 C  CA  . ARG A 1 253 ? -4.691  -0.924  35.251  1.00  19.46 ? 254 ARG A CA  1 
ATOM   2012 C  C   . ARG A 1 253 ? -5.781  -1.879  35.654  1.00  19.82 ? 254 ARG A C   1 
ATOM   2013 O  O   . ARG A 1 253 ? -5.512  -3.060  35.846  1.00  22.64 ? 254 ARG A O   1 
ATOM   2014 C  CB  . ARG A 1 253 ? -4.641  -0.833  33.702  1.00  16.98 ? 254 ARG A CB  1 
ATOM   2015 C  CG  . ARG A 1 253 ? -3.691  0.260   33.170  1.00  15.46 ? 254 ARG A CG  1 
ATOM   2016 C  CD  . ARG A 1 253 ? -3.664  0.141   31.662  1.00  13.32 ? 254 ARG A CD  1 
ATOM   2017 N  NE  . ARG A 1 253 ? -2.791  -0.982  31.210  1.00  13.17 ? 254 ARG A NE  1 
ATOM   2018 C  CZ  . ARG A 1 253 ? -2.556  -1.227  29.913  1.00  11.48 ? 254 ARG A CZ  1 
ATOM   2019 N  NH1 . ARG A 1 253 ? -3.206  -0.485  28.996  1.00  10.08 ? 254 ARG A NH1 1 
ATOM   2020 N  NH2 . ARG A 1 253 ? -1.763  -2.241  29.523  1.00  10.19 ? 254 ARG A NH2 1 
ATOM   2021 N  N   . GLN A 1 254 ? -6.999  -1.353  35.702  1.00  18.70 ? 255 GLN A N   1 
ATOM   2022 C  CA  . GLN A 1 254 ? -8.181  -2.098  36.018  1.00  24.07 ? 255 GLN A CA  1 
ATOM   2023 C  C   . GLN A 1 254 ? -9.045  -2.188  34.748  1.00  22.40 ? 255 GLN A C   1 
ATOM   2024 O  O   . GLN A 1 254 ? -9.230  -1.177  34.070  1.00  20.93 ? 255 GLN A O   1 
ATOM   2025 C  CB  . GLN A 1 254 ? -8.969  -1.301  37.059  1.00  27.75 ? 255 GLN A CB  1 
ATOM   2026 C  CG  . GLN A 1 254 ? -8.856  -1.853  38.449  1.00  40.47 ? 255 GLN A CG  1 
ATOM   2027 C  CD  . GLN A 1 254 ? -9.737  -3.080  38.595  1.00  46.44 ? 255 GLN A CD  1 
ATOM   2028 O  OE1 . GLN A 1 254 ? -10.967 -3.011  38.422  1.00  56.59 ? 255 GLN A OE1 1 
ATOM   2029 N  NE2 . GLN A 1 254 ? -9.117  -4.215  38.900  1.00  50.23 ? 255 GLN A NE2 1 
ATOM   2030 N  N   . ILE A 1 255 ? -9.564  -3.372  34.442  1.00  19.70 ? 256 ILE A N   1 
ATOM   2031 C  CA  . ILE A 1 255 ? -10.507 -3.500  33.354  1.00  18.76 ? 256 ILE A CA  1 
ATOM   2032 C  C   . ILE A 1 255 ? -11.901 -3.569  33.999  1.00  18.95 ? 256 ILE A C   1 
ATOM   2033 O  O   . ILE A 1 255 ? -12.180 -4.393  34.873  1.00  17.50 ? 256 ILE A O   1 
ATOM   2034 C  CB  . ILE A 1 255 ? -10.256 -4.772  32.473  1.00  17.74 ? 256 ILE A CB  1 
ATOM   2035 C  CG1 . ILE A 1 255 ? -8.852  -4.740  31.887  1.00  15.60 ? 256 ILE A CG1 1 
ATOM   2036 C  CG2 . ILE A 1 255 ? -11.377 -4.944  31.442  1.00  15.23 ? 256 ILE A CG2 1 
ATOM   2037 C  CD1 . ILE A 1 255 ? -8.511  -5.988  31.046  1.00  16.38 ? 256 ILE A CD1 1 
ATOM   2038 N  N   . LYS A 1 256 ? -12.751 -2.649  33.592  1.00  17.07 ? 257 LYS A N   1 
ATOM   2039 C  CA  . LYS A 1 256 ? -14.110 -2.538  34.115  1.00  18.26 ? 257 LYS A CA  1 
ATOM   2040 C  C   . LYS A 1 256 ? -15.142 -3.190  33.171  1.00  16.69 ? 257 LYS A C   1 
ATOM   2041 O  O   . LYS A 1 256 ? -15.040 -3.037  31.955  1.00  16.79 ? 257 LYS A O   1 
ATOM   2042 C  CB  . LYS A 1 256 ? -14.390 -1.043  34.421  1.00  20.73 ? 257 LYS A CB  1 
ATOM   2043 C  CG  . LYS A 1 256 ? -13.427 -0.554  35.519  1.00  26.43 ? 257 LYS A CG  1 
ATOM   2044 C  CD  . LYS A 1 256 ? -13.838 0.734   36.228  1.00  34.25 ? 257 LYS A CD  1 
ATOM   2045 C  CE  . LYS A 1 256 ? -12.595 1.550   36.622  1.00  38.73 ? 257 LYS A CE  1 
ATOM   2046 N  NZ  . LYS A 1 256 ? -12.877 3.008   36.848  1.00  40.56 ? 257 LYS A NZ  1 
ATOM   2047 N  N   . ALA A 1 257 ? -16.141 -3.899  33.702  1.00  16.13 ? 258 ALA A N   1 
ATOM   2048 C  CA  . ALA A 1 257 ? -17.198 -4.490  32.862  1.00  16.26 ? 258 ALA A CA  1 
ATOM   2049 C  C   . ALA A 1 257 ? -18.493 -3.696  33.004  1.00  15.88 ? 258 ALA A C   1 
ATOM   2050 O  O   . ALA A 1 257 ? -18.874 -3.240  34.124  1.00  14.48 ? 258 ALA A O   1 
ATOM   2051 C  CB  . ALA A 1 257 ? -17.429 -5.977  33.162  1.00  17.19 ? 258 ALA A CB  1 
ATOM   2052 N  N   . SER A 1 258 ? -19.189 -3.542  31.881  1.00  15.60 ? 259 SER A N   1 
ATOM   2053 C  CA  . SER A 1 258 ? -20.560 -2.910  31.907  1.00  16.19 ? 259 SER A CA  1 
ATOM   2054 C  C   . SER A 1 258 ? -21.682 -3.802  32.354  1.00  17.53 ? 259 SER A C   1 
ATOM   2055 O  O   . SER A 1 258 ? -22.787 -3.331  32.439  1.00  19.50 ? 259 SER A O   1 
ATOM   2056 C  CB  . SER A 1 258 ? -20.998 -2.290  30.569  1.00  16.79 ? 259 SER A CB  1 
ATOM   2057 O  OG  . SER A 1 258 ? -21.326 -3.284  29.575  1.00  15.38 ? 259 SER A OG  1 
ATOM   2058 N  N   . PHE A 1 259 ? -21.382 -5.051  32.656  1.00  18.52 ? 260 PHE A N   1 
ATOM   2059 C  CA  . PHE A 1 259 ? -22.397 -6.076  32.782  1.00  22.13 ? 260 PHE A CA  1 
ATOM   2060 C  C   . PHE A 1 259 ? -22.029 -7.070  33.884  1.00  28.26 ? 260 PHE A C   1 
ATOM   2061 O  O   . PHE A 1 259 ? -20.821 -7.274  34.190  1.00  23.91 ? 260 PHE A O   1 
ATOM   2062 C  CB  . PHE A 1 259 ? -22.519 -6.815  31.443  1.00  21.47 ? 260 PHE A CB  1 
ATOM   2063 C  CG  . PHE A 1 259 ? -21.232 -7.512  31.004  1.00  21.17 ? 260 PHE A CG  1 
ATOM   2064 C  CD1 . PHE A 1 259 ? -20.257 -6.826  30.261  1.00  20.42 ? 260 PHE A CD1 1 
ATOM   2065 C  CD2 . PHE A 1 259 ? -20.967 -8.833  31.377  1.00  23.06 ? 260 PHE A CD2 1 
ATOM   2066 C  CE1 . PHE A 1 259 ? -19.078 -7.450  29.888  1.00  19.93 ? 260 PHE A CE1 1 
ATOM   2067 C  CE2 . PHE A 1 259 ? -19.776 -9.459  31.002  1.00  22.88 ? 260 PHE A CE2 1 
ATOM   2068 C  CZ  . PHE A 1 259 ? -18.825 -8.753  30.266  1.00  21.96 ? 260 PHE A CZ  1 
ATOM   2069 N  N   . LYS A 1 260 ? -23.095 -7.652  34.468  1.00  34.67 ? 261 LYS A N   1 
ATOM   2070 C  CA  . LYS A 1 260 ? -23.070 -8.784  35.440  1.00  46.48 ? 261 LYS A CA  1 
ATOM   2071 C  C   . LYS A 1 260 ? -22.101 -8.672  36.619  1.00  58.28 ? 261 LYS A C   1 
ATOM   2072 O  O   . LYS A 1 260 ? -20.878 -8.850  36.468  1.00  71.52 ? 261 LYS A O   1 
ATOM   2073 C  CB  . LYS A 1 260 ? -22.864 -10.133 34.729  1.00  44.56 ? 261 LYS A CB  1 
ATOM   2074 C  CG  . LYS A 1 260 ? -23.852 -10.404 33.605  1.00  44.69 ? 261 LYS A CG  1 
ATOM   2075 C  CD  . LYS A 1 260 ? -23.380 -11.638 32.854  1.00  47.66 ? 261 LYS A CD  1 
ATOM   2076 C  CE  . LYS A 1 260 ? -21.864 -11.775 33.047  1.00  48.20 ? 261 LYS A CE  1 
ATOM   2077 N  NZ  . LYS A 1 260 ? -21.337 -13.088 32.617  1.00  44.85 ? 261 LYS A NZ  1 
ATOM   2078 O  OXT . LYS A 1 260 ? -22.522 -8.404  37.753  1.00  62.37 ? 261 LYS A OXT 1 
HETATM 2079 ZN ZN  . ZN  B 2 .   ? -6.563  -1.844  15.279  1.00  11.59 ? 301 ZN  A ZN  1 
HETATM 2080 S  S   . DMS C 3 .   ? 1.487   -11.563 14.810  1.00  30.22 ? 302 DMS A S   1 
HETATM 2081 O  O   . DMS C 3 .   ? 2.116   -13.214 14.438  1.00  24.91 ? 302 DMS A O   1 
HETATM 2082 C  C1  . DMS C 3 .   ? 1.696   -11.555 16.543  1.00  21.13 ? 302 DMS A C1  1 
HETATM 2083 C  C2  . DMS C 3 .   ? 2.640   -10.211 14.478  1.00  24.97 ? 302 DMS A C2  1 
HETATM 2084 O  O1  . MES D 4 .   ? -7.449  -9.341  -2.945  1.00  33.66 ? 303 MES A O1  1 
HETATM 2085 C  C2  . MES D 4 .   ? -7.487  -10.306 -4.128  1.00  28.58 ? 303 MES A C2  1 
HETATM 2086 C  C3  . MES D 4 .   ? -8.741  -11.275 -4.163  1.00  30.65 ? 303 MES A C3  1 
HETATM 2087 N  N4  . MES D 4 .   ? -9.888  -11.105 -3.253  1.00  29.74 ? 303 MES A N4  1 
HETATM 2088 C  C5  . MES D 4 .   ? -9.610  -10.317 -1.994  1.00  24.88 ? 303 MES A C5  1 
HETATM 2089 C  C6  . MES D 4 .   ? -8.320  -9.732  -1.833  1.00  27.09 ? 303 MES A C6  1 
HETATM 2090 C  C7  . MES D 4 .   ? -11.303 -11.761 -3.429  1.00  25.82 ? 303 MES A C7  1 
HETATM 2091 F  F18 . V90 E 5 .   ? -2.912  3.208   13.242  1.00  13.42 ? 304 V90 A F18 1 
HETATM 2092 C  C5  . V90 E 5 .   ? -3.840  3.286   14.173  1.00  15.86 ? 304 V90 A C5  1 
HETATM 2093 C  C6  . V90 E 5 .   ? -4.351  4.511   14.550  1.00  17.43 ? 304 V90 A C6  1 
HETATM 2094 S  S12 . V90 E 5 .   ? -3.723  6.023   13.820  1.00  21.08 ? 304 V90 A S12 1 
HETATM 2095 C  C13 . V90 E 5 .   ? -4.203  5.818   12.049  1.00  30.12 ? 304 V90 A C13 1 
HETATM 2096 C  C14 . V90 E 5 .   ? -5.662  6.245   11.714  1.00  35.86 ? 304 V90 A C14 1 
HETATM 2097 O  O15 . V90 E 5 .   ? -6.026  5.862   10.390  1.00  43.36 ? 304 V90 A O15 1 
HETATM 2098 C  C1  . V90 E 5 .   ? -5.336  4.563   15.521  1.00  15.88 ? 304 V90 A C1  1 
HETATM 2099 F  F17 . V90 E 5 .   ? -5.892  5.715   15.904  1.00  18.22 ? 304 V90 A F17 1 
HETATM 2100 C  C4  . V90 E 5 .   ? -4.311  2.074   14.732  1.00  13.93 ? 304 V90 A C4  1 
HETATM 2101 C  C3  . V90 E 5 .   ? -5.236  2.166   15.774  1.00  13.49 ? 304 V90 A C3  1 
HETATM 2102 S  S8  . V90 E 5 .   ? -5.850  0.756   16.665  1.00  11.93 ? 304 V90 A S8  1 
HETATM 2103 O  O10 . V90 E 5 .   ? -7.339  0.820   16.566  1.00  10.05 ? 304 V90 A O10 1 
HETATM 2104 N  N11 . V90 E 5 .   ? -5.120  -0.668  16.110  1.00  10.43 ? 304 V90 A N11 1 
HETATM 2105 O  O9  . V90 E 5 .   ? -5.427  0.984   18.057  1.00  10.56 ? 304 V90 A O9  1 
HETATM 2106 C  C2  . V90 E 5 .   ? -5.779  3.394   16.141  1.00  15.45 ? 304 V90 A C2  1 
HETATM 2107 F  F16 . V90 E 5 .   ? -6.679  3.456   17.093  1.00  16.18 ? 304 V90 A F16 1 
HETATM 2108 N  N7  . V90 E 5 .   ? -3.744  0.846   14.302  1.00  14.46 ? 304 V90 A N7  1 
HETATM 2109 C  C19 . V90 E 5 .   ? -3.600  0.536   12.898  1.00  15.35 ? 304 V90 A C19 1 
HETATM 2110 C  C26 . V90 E 5 .   ? -3.816  -1.003  12.833  1.00  16.11 ? 304 V90 A C26 1 
HETATM 2111 C  C25 . V90 E 5 .   ? -3.032  -1.714  11.725  1.00  18.96 ? 304 V90 A C25 1 
HETATM 2112 C  C24 . V90 E 5 .   ? -2.975  -1.209  10.299  1.00  17.47 ? 304 V90 A C24 1 
HETATM 2113 C  C23 . V90 E 5 .   ? -2.492  0.225   9.954   1.00  18.08 ? 304 V90 A C23 1 
HETATM 2114 C  C22 . V90 E 5 .   ? -3.762  0.982   9.662   1.00  16.70 ? 304 V90 A C22 1 
HETATM 2115 C  C21 . V90 E 5 .   ? -4.219  1.930   10.763  1.00  16.88 ? 304 V90 A C21 1 
HETATM 2116 C  C20 . V90 E 5 .   ? -4.710  1.208   12.031  1.00  16.03 ? 304 V90 A C20 1 
HETATM 2117 O  O   . HOH F 6 .   ? -1.268  -4.123  15.614  1.00  9.80  ? 401 HOH A O   1 
HETATM 2118 O  O   . HOH F 6 .   ? -3.745  -15.876 24.323  1.00  13.00 ? 402 HOH A O   1 
HETATM 2119 O  O   . HOH F 6 .   ? -4.448  -13.489 17.881  1.00  8.39  ? 403 HOH A O   1 
HETATM 2120 O  O   . HOH F 6 .   ? -16.846 -8.393  20.357  1.00  11.23 ? 404 HOH A O   1 
HETATM 2121 O  O   . HOH F 6 .   ? -21.505 5.582   4.727   1.00  17.71 ? 405 HOH A O   1 
HETATM 2122 O  O   . HOH F 6 .   ? -7.814  -15.455 11.287  1.00  10.01 ? 406 HOH A O   1 
HETATM 2123 O  O   . HOH F 6 .   ? 3.751   4.892   29.703  1.00  13.00 ? 407 HOH A O   1 
HETATM 2124 O  O   . HOH F 6 .   ? -21.415 -7.272  23.569  1.00  14.44 ? 408 HOH A O   1 
HETATM 2125 O  O   . HOH F 6 .   ? -17.915 -20.581 8.028   1.00  13.81 ? 409 HOH A O   1 
HETATM 2126 O  O   . HOH F 6 .   ? -13.841 10.397  27.801  1.00  17.67 ? 410 HOH A O   1 
HETATM 2127 O  O   . HOH F 6 .   ? -8.410  -3.863  7.765   1.00  12.62 ? 411 HOH A O   1 
HETATM 2128 O  O   . HOH F 6 .   ? 4.945   -4.915  20.851  1.00  14.48 ? 412 HOH A O   1 
HETATM 2129 O  O   . HOH F 6 .   ? -9.500  -8.104  34.037  1.00  23.33 ? 413 HOH A O   1 
HETATM 2130 O  O   . HOH F 6 .   ? -11.672 2.770   30.709  1.00  20.52 ? 414 HOH A O   1 
HETATM 2131 O  O   . HOH F 6 .   ? -7.957  -22.163 10.418  1.00  16.84 ? 415 HOH A O   1 
HETATM 2132 O  O   . HOH F 6 .   ? -10.506 8.607   25.609  1.00  12.15 ? 416 HOH A O   1 
HETATM 2133 O  O   . HOH F 6 .   ? 1.382   -1.668  29.305  1.00  17.77 ? 417 HOH A O   1 
HETATM 2134 O  O   . HOH F 6 .   ? -0.462  10.828  23.379  1.00  21.08 ? 418 HOH A O   1 
HETATM 2135 O  O   . HOH F 6 .   ? -3.487  -11.123 20.784  1.00  12.51 ? 419 HOH A O   1 
HETATM 2136 O  O   . HOH F 6 .   ? -2.439  -8.755  29.034  1.00  15.91 ? 420 HOH A O   1 
HETATM 2137 O  O   . HOH F 6 .   ? -17.640 10.514  11.311  1.00  18.63 ? 421 HOH A O   1 
HETATM 2138 O  O   . HOH F 6 .   ? -13.532 -21.075 15.097  1.00  22.47 ? 422 HOH A O   1 
HETATM 2139 O  O   . HOH F 6 .   ? -16.278 -9.994  32.803  1.00  16.43 ? 423 HOH A O   1 
HETATM 2140 O  O   . HOH F 6 .   ? -16.038 -12.399 24.381  1.00  14.25 ? 424 HOH A O   1 
HETATM 2141 O  O   . HOH F 6 .   ? 1.445   -11.729 24.962  1.00  15.15 ? 425 HOH A O   1 
HETATM 2142 O  O   . HOH F 6 .   ? -20.812 7.760   1.701   1.00  22.32 ? 426 HOH A O   1 
HETATM 2143 O  O   . HOH F 6 .   ? -23.045 -3.059  6.804   1.00  18.59 ? 427 HOH A O   1 
HETATM 2144 O  O   . HOH F 6 .   ? -4.543  -12.015 32.000  1.00  24.59 ? 428 HOH A O   1 
HETATM 2145 O  O   . HOH F 6 .   ? -3.317  -13.293 25.124  1.00  13.61 ? 429 HOH A O   1 
HETATM 2146 O  O   . HOH F 6 .   ? 8.717   -3.978  20.926  1.00  22.54 ? 430 HOH A O   1 
HETATM 2147 O  O   . HOH F 6 .   ? -14.032 14.318  27.093  1.00  21.98 ? 431 HOH A O   1 
HETATM 2148 O  O   . HOH F 6 .   ? -23.017 -11.701 14.322  1.00  24.59 ? 432 HOH A O   1 
HETATM 2149 O  O   . HOH F 6 .   ? -10.812 -19.836 7.081   1.00  20.94 ? 433 HOH A O   1 
HETATM 2150 O  O   . HOH F 6 .   ? -1.830  -12.419 22.790  1.00  13.67 ? 434 HOH A O   1 
HETATM 2151 O  O   . HOH F 6 .   ? -17.654 -21.200 17.532  1.00  23.62 ? 435 HOH A O   1 
HETATM 2152 O  O   . HOH F 6 .   ? -12.953 -16.974 26.394  1.00  18.19 ? 436 HOH A O   1 
HETATM 2153 O  O   . HOH F 6 .   ? -6.303  -4.814  -6.565  1.00  27.92 ? 437 HOH A O   1 
HETATM 2154 O  O   . HOH F 6 .   ? -23.683 -0.810  26.442  1.00  18.68 ? 438 HOH A O   1 
HETATM 2155 O  O   . HOH F 6 .   ? -19.153 10.009  8.864   1.00  25.52 ? 439 HOH A O   1 
HETATM 2156 O  O   . HOH F 6 .   ? 1.400   8.908   24.332  1.00  16.96 ? 440 HOH A O   1 
HETATM 2157 O  O   . HOH F 6 .   ? -12.687 -17.426 16.929  1.00  23.59 ? 441 HOH A O   1 
HETATM 2158 O  O   . HOH F 6 .   ? -6.597  -20.169 19.356  1.00  22.21 ? 442 HOH A O   1 
HETATM 2159 O  O   . HOH F 6 .   ? -10.209 -18.249 17.016  1.00  19.10 ? 443 HOH A O   1 
HETATM 2160 O  O   . HOH F 6 .   ? -13.954 -16.728 29.076  1.00  33.40 ? 444 HOH A O   1 
HETATM 2161 O  O   . HOH F 6 .   ? -24.707 -7.808  9.004   1.00  15.10 ? 445 HOH A O   1 
HETATM 2162 O  O   . HOH F 6 .   ? 2.152   -14.205 20.857  1.00  30.40 ? 446 HOH A O   1 
HETATM 2163 O  O   . HOH F 6 .   ? -8.062  21.839  21.632  1.00  23.92 ? 447 HOH A O   1 
HETATM 2164 O  O   . HOH F 6 .   ? -17.592 -19.453 34.869  1.00  23.88 ? 448 HOH A O   1 
HETATM 2165 O  O   . HOH F 6 .   ? -24.105 -16.613 3.987   1.00  27.99 ? 449 HOH A O   1 
HETATM 2166 O  O   . HOH F 6 .   ? 0.078   -14.144 22.384  1.00  26.85 ? 450 HOH A O   1 
HETATM 2167 O  O   . HOH F 6 .   ? -13.174 -18.661 14.691  1.00  16.73 ? 451 HOH A O   1 
HETATM 2168 O  O   . HOH F 6 .   ? 4.624   -2.485  28.801  1.00  29.64 ? 452 HOH A O   1 
HETATM 2169 O  O   . HOH F 6 .   ? -22.747 -5.797  2.989   1.00  24.65 ? 453 HOH A O   1 
HETATM 2170 O  O   . HOH F 6 .   ? 7.809   6.099   21.587  1.00  19.80 ? 454 HOH A O   1 
HETATM 2171 O  O   . HOH F 6 .   ? -20.126 10.750  26.615  1.00  23.86 ? 455 HOH A O   1 
HETATM 2172 O  O   . HOH F 6 .   ? -3.755  -13.186 -2.838  1.00  17.04 ? 456 HOH A O   1 
HETATM 2173 O  O   . HOH F 6 .   ? -25.446 -5.773  12.981  1.00  22.85 ? 457 HOH A O   1 
HETATM 2174 O  O   . HOH F 6 .   ? -26.631 -2.632  14.465  1.00  20.65 ? 458 HOH A O   1 
HETATM 2175 O  O   . HOH F 6 .   ? -8.904  -5.906  35.675  1.00  20.27 ? 459 HOH A O   1 
HETATM 2176 O  O   . HOH F 6 .   ? -15.436 -21.803 13.301  1.00  26.59 ? 460 HOH A O   1 
HETATM 2177 O  O   . HOH F 6 .   ? -1.600  -17.462 25.445  1.00  22.75 ? 461 HOH A O   1 
HETATM 2178 O  O   . HOH F 6 .   ? 4.847   -7.387  22.157  1.00  29.59 ? 462 HOH A O   1 
HETATM 2179 O  O   . HOH F 6 .   ? -6.737  -14.985 31.502  1.00  16.68 ? 463 HOH A O   1 
HETATM 2180 O  O   . HOH F 6 .   ? -26.807 -4.075  25.155  1.00  22.92 ? 464 HOH A O   1 
HETATM 2181 O  O   . HOH F 6 .   ? -0.846  -17.906 -1.789  1.00  23.29 ? 465 HOH A O   1 
HETATM 2182 O  O   . HOH F 6 .   ? 5.653   7.144   20.172  1.00  15.32 ? 466 HOH A O   1 
HETATM 2183 O  O   . HOH F 6 .   ? -23.937 8.657   20.158  1.00  28.32 ? 467 HOH A O   1 
HETATM 2184 O  O   . HOH F 6 .   ? 4.518   -11.558 23.391  1.00  32.30 ? 468 HOH A O   1 
HETATM 2185 O  O   . HOH F 6 .   ? -1.187  -17.720 17.828  1.00  33.15 ? 469 HOH A O   1 
HETATM 2186 O  O   . HOH F 6 .   ? 2.633   -11.277 9.480   1.00  18.88 ? 470 HOH A O   1 
HETATM 2187 O  O   . HOH F 6 .   ? -16.833 -18.117 20.149  1.00  24.82 ? 471 HOH A O   1 
HETATM 2188 O  O   . HOH F 6 .   ? -21.962 -18.605 13.530  1.00  25.88 ? 472 HOH A O   1 
HETATM 2189 O  O   . HOH F 6 .   ? -1.261  -13.147 26.954  1.00  20.43 ? 473 HOH A O   1 
HETATM 2190 O  O   . HOH F 6 .   ? -0.579  -8.597  32.383  1.00  23.64 ? 474 HOH A O   1 
HETATM 2191 O  O   . HOH F 6 .   ? -18.155 -9.013  34.565  1.00  25.83 ? 475 HOH A O   1 
HETATM 2192 O  O   . HOH F 6 .   ? -28.827 -6.064  24.540  1.00  27.25 ? 476 HOH A O   1 
HETATM 2193 O  O   . HOH F 6 .   ? 0.250   -1.447  -5.107  1.00  21.81 ? 477 HOH A O   1 
HETATM 2194 O  O   . HOH F 6 .   ? 4.519   -3.510  26.289  1.00  23.19 ? 478 HOH A O   1 
HETATM 2195 O  O   . HOH F 6 .   ? -25.038 4.575   8.474   1.00  29.32 ? 479 HOH A O   1 
HETATM 2196 O  O   . HOH F 6 .   ? -6.448  -5.134  37.379  1.00  19.95 ? 480 HOH A O   1 
HETATM 2197 O  O   . HOH F 6 .   ? -14.554 -18.607 18.820  1.00  21.69 ? 481 HOH A O   1 
HETATM 2198 O  O   . HOH F 6 .   ? -23.486 -0.906  3.723   1.00  22.98 ? 482 HOH A O   1 
HETATM 2199 O  O   . HOH F 6 .   ? -22.234 3.629   -3.012  1.00  27.51 ? 483 HOH A O   1 
HETATM 2200 O  O   . HOH F 6 .   ? -16.643 -13.864 26.328  1.00  23.04 ? 484 HOH A O   1 
HETATM 2201 O  O   . HOH F 6 .   ? 4.590   -6.624  7.657   1.00  26.00 ? 485 HOH A O   1 
HETATM 2202 O  O   . HOH F 6 .   ? 11.039  -6.858  22.308  1.00  26.18 ? 486 HOH A O   1 
HETATM 2203 O  O   . HOH F 6 .   ? 8.644   -4.725  23.746  1.00  25.80 ? 487 HOH A O   1 
HETATM 2204 O  O   . HOH F 6 .   ? 13.417  0.313   24.478  1.00  24.07 ? 488 HOH A O   1 
HETATM 2205 O  O   . HOH F 6 .   ? 11.563  1.217   25.751  1.00  28.75 ? 489 HOH A O   1 
HETATM 2206 O  O   . HOH F 6 .   ? 8.247   3.062   27.932  1.00  30.28 ? 490 HOH A O   1 
HETATM 2207 O  O   . HOH F 6 .   ? -1.392  9.232   27.931  1.00  27.54 ? 491 HOH A O   1 
HETATM 2208 O  O   . HOH F 6 .   ? -7.042  -8.830  32.487  1.00  19.08 ? 492 HOH A O   1 
HETATM 2209 O  O   . HOH F 6 .   ? -10.816 -15.378 33.978  1.00  24.28 ? 493 HOH A O   1 
HETATM 2210 O  O   . HOH F 6 .   ? -7.547  -19.278 30.390  1.00  23.83 ? 494 HOH A O   1 
HETATM 2211 O  O   . HOH F 6 .   ? -1.102  -11.189 28.933  1.00  22.69 ? 495 HOH A O   1 
HETATM 2212 O  O   . HOH F 6 .   ? -17.270 -16.311 21.918  1.00  27.15 ? 496 HOH A O   1 
HETATM 2213 O  O   . HOH F 6 .   ? -23.105 -0.461  34.302  1.00  27.28 ? 497 HOH A O   1 
HETATM 2214 O  O   . HOH F 6 .   ? -25.677 6.300   26.905  1.00  23.59 ? 498 HOH A O   1 
HETATM 2215 O  O   . HOH F 6 .   ? -25.618 4.217   4.206   1.00  31.68 ? 499 HOH A O   1 
HETATM 2216 O  O   . HOH F 6 .   ? -6.776  5.648   5.919   1.00  25.09 ? 500 HOH A O   1 
HETATM 2217 O  O   . HOH F 6 .   ? -4.227  6.501   5.871   1.00  36.44 ? 501 HOH A O   1 
HETATM 2218 O  O   . HOH F 6 .   ? -16.394 5.248   -7.973  1.00  26.45 ? 502 HOH A O   1 
HETATM 2219 O  O   . HOH F 6 .   ? -12.214 12.448  29.032  1.00  24.38 ? 503 HOH A O   1 
HETATM 2220 O  O   . HOH F 6 .   ? -12.653 -19.487 26.258  1.00  25.89 ? 504 HOH A O   1 
HETATM 2221 O  O   . HOH F 6 .   ? -10.446 13.143  8.557   1.00  30.87 ? 505 HOH A O   1 
HETATM 2222 O  O   . HOH F 6 .   ? 1.811   12.557  22.798  1.00  26.78 ? 506 HOH A O   1 
HETATM 2223 O  O   . HOH F 6 .   ? -24.055 -17.891 6.576   1.00  30.33 ? 507 HOH A O   1 
HETATM 2224 O  O   . HOH F 6 .   ? -23.391 -13.479 11.401  1.00  21.95 ? 508 HOH A O   1 
HETATM 2225 O  O   . HOH F 6 .   ? -18.113 -3.775  -2.608  1.00  22.33 ? 509 HOH A O   1 
HETATM 2226 O  O   . HOH F 6 .   ? -7.055  -17.121 1.522   1.00  19.56 ? 510 HOH A O   1 
HETATM 2227 O  O   . HOH F 6 .   ? -4.162  -15.626 -2.246  1.00  24.30 ? 511 HOH A O   1 
HETATM 2228 O  O   . HOH F 6 .   ? -4.462  -16.043 0.672   1.00  25.50 ? 512 HOH A O   1 
HETATM 2229 O  O   . HOH F 6 .   ? 0.262   0.354   -6.980  1.00  28.89 ? 513 HOH A O   1 
HETATM 2230 O  O   . HOH F 6 .   ? 7.807   -5.810  -10.903 1.00  25.46 ? 514 HOH A O   1 
HETATM 2231 O  O   . HOH F 6 .   ? 2.701   -13.392 5.036   1.00  25.24 ? 515 HOH A O   1 
HETATM 2232 O  O   . HOH F 6 .   ? 1.301   -6.465  34.352  1.00  22.13 ? 516 HOH A O   1 
HETATM 2233 O  O   . HOH F 6 .   ? -5.075  2.185   37.235  1.00  27.77 ? 517 HOH A O   1 
HETATM 2234 O  O   . HOH F 6 .   ? -0.112  2.998   12.344  1.00  25.05 ? 518 HOH A O   1 
HETATM 2235 O  O   . HOH F 6 .   ? -0.031  2.844   10.056  1.00  31.55 ? 519 HOH A O   1 
HETATM 2236 O  O   . HOH F 6 .   ? -0.721  8.918   14.844  1.00  31.52 ? 520 HOH A O   1 
HETATM 2237 O  O   . HOH F 6 .   ? 14.528  2.549   23.138  1.00  39.01 ? 521 HOH A O   1 
HETATM 2238 O  O   . HOH F 6 .   ? 4.077   9.658   23.776  1.00  27.09 ? 522 HOH A O   1 
HETATM 2239 O  O   . HOH F 6 .   ? -8.220  -17.658 34.825  1.00  24.45 ? 523 HOH A O   1 
HETATM 2240 O  O   . HOH F 6 .   ? -11.378 -2.868  42.014  1.00  38.01 ? 524 HOH A O   1 
HETATM 2241 O  O   . HOH F 6 .   ? -25.573 9.581   13.263  1.00  28.96 ? 525 HOH A O   1 
HETATM 2242 O  O   . HOH F 6 .   ? -24.582 12.092  6.342   1.00  26.07 ? 526 HOH A O   1 
HETATM 2243 O  O   . HOH F 6 .   ? -17.225 11.080  -1.973  1.00  25.98 ? 527 HOH A O   1 
HETATM 2244 O  O   . HOH F 6 .   ? -18.267 19.457  5.901   1.00  26.65 ? 528 HOH A O   1 
HETATM 2245 O  O   . HOH F 6 .   ? -23.509 -6.908  -0.018  1.00  38.67 ? 529 HOH A O   1 
HETATM 2246 O  O   . HOH F 6 .   ? -9.830  14.871  12.148  1.00  17.47 ? 530 HOH A O   1 
HETATM 2247 O  O   . HOH F 6 .   ? -14.796 20.073  17.691  1.00  27.47 ? 531 HOH A O   1 
HETATM 2248 O  O   . HOH F 6 .   ? -5.998  -19.800 23.773  1.00  29.09 ? 532 HOH A O   1 
HETATM 2249 O  O   . HOH F 6 .   ? -21.429 -19.618 6.653   1.00  30.88 ? 533 HOH A O   1 
HETATM 2250 O  O   . HOH F 6 .   ? -12.859 -9.185  -3.152  1.00  27.41 ? 534 HOH A O   1 
HETATM 2251 O  O   . HOH F 6 .   ? -8.397  0.417   -6.572  1.00  26.94 ? 535 HOH A O   1 
HETATM 2252 O  O   . HOH F 6 .   ? -6.906  1.610   35.592  1.00  36.01 ? 536 HOH A O   1 
HETATM 2253 O  O   . HOH F 6 .   ? -19.482 -4.541  41.097  1.00  35.51 ? 537 HOH A O   1 
HETATM 2254 O  O   . HOH F 6 .   ? -8.418  -15.275 36.504  1.00  29.63 ? 538 HOH A O   1 
HETATM 2255 O  O   . HOH F 6 .   ? -14.042 -0.020  43.072  1.00  29.45 ? 539 HOH A O   1 
HETATM 2256 O  O   . HOH F 6 .   ? -2.028  -12.068 31.374  1.00  34.49 ? 540 HOH A O   1 
HETATM 2257 O  O   . HOH F 6 .   ? -5.395  16.026  12.058  1.00  38.59 ? 541 HOH A O   1 
HETATM 2258 O  O   . HOH F 6 .   ? -13.189 -22.180 8.610   1.00  19.49 ? 542 HOH A O   1 
HETATM 2259 O  O   . HOH F 6 .   ? -21.443 -13.759 23.198  1.00  25.31 ? 543 HOH A O   1 
HETATM 2260 O  O   . HOH F 6 .   ? 4.398   4.545   11.322  1.00  37.91 ? 544 HOH A O   1 
HETATM 2261 O  O   . HOH F 6 .   ? 3.652   -13.757 12.242  1.00  36.33 ? 545 HOH A O   1 
HETATM 2262 O  O   . HOH F 6 .   ? 13.195  -3.881  13.361  1.00  34.39 ? 546 HOH A O   1 
HETATM 2263 O  O   . HOH F 6 .   ? 9.678   -8.437  7.883   1.00  36.63 ? 547 HOH A O   1 
HETATM 2264 O  O   . HOH F 6 .   ? 15.844  2.948   20.610  1.00  36.71 ? 548 HOH A O   1 
HETATM 2265 O  O   . HOH F 6 .   ? 14.342  5.613   19.580  1.00  35.81 ? 549 HOH A O   1 
HETATM 2266 O  O   . HOH F 6 .   ? 16.020  3.322   15.518  1.00  36.72 ? 550 HOH A O   1 
HETATM 2267 O  O   . HOH F 6 .   ? 14.390  4.804   24.685  1.00  41.57 ? 551 HOH A O   1 
HETATM 2268 O  O   . HOH F 6 .   ? -4.280  -8.657  31.140  1.00  23.25 ? 552 HOH A O   1 
HETATM 2269 O  O   . HOH F 6 .   ? 1.641   -9.878  30.459  1.00  31.05 ? 553 HOH A O   1 
HETATM 2270 O  O   . HOH F 6 .   ? -4.804  -9.768  33.623  1.00  33.94 ? 554 HOH A O   1 
HETATM 2271 O  O   . HOH F 6 .   ? -2.467  -9.036  34.480  1.00  33.08 ? 555 HOH A O   1 
HETATM 2272 O  O   . HOH F 6 .   ? -15.490 -10.394 37.119  1.00  35.06 ? 556 HOH A O   1 
HETATM 2273 O  O   . HOH F 6 .   ? -17.305 -12.324 31.724  1.00  28.21 ? 557 HOH A O   1 
HETATM 2274 O  O   . HOH F 6 .   ? -16.937 -7.437  39.659  1.00  26.56 ? 558 HOH A O   1 
HETATM 2275 O  O   . HOH F 6 .   ? -23.682 19.681  10.861  1.00  44.68 ? 559 HOH A O   1 
HETATM 2276 O  O   . HOH F 6 .   ? -16.084 15.921  23.684  1.00  31.22 ? 560 HOH A O   1 
HETATM 2277 O  O   . HOH F 6 .   ? -21.127 -6.954  -1.864  1.00  33.77 ? 561 HOH A O   1 
HETATM 2278 O  O   . HOH F 6 .   ? -13.947 -9.315  -5.759  1.00  40.42 ? 562 HOH A O   1 
HETATM 2279 O  O   . HOH F 6 .   ? -15.173 8.813   -2.275  1.00  33.04 ? 563 HOH A O   1 
HETATM 2280 O  O   . HOH F 6 .   ? -10.916 0.929   33.814  1.00  35.76 ? 564 HOH A O   1 
HETATM 2281 O  O   . HOH F 6 .   ? -8.853  5.910   28.938  1.00  29.25 ? 565 HOH A O   1 
HETATM 2282 O  O   . HOH F 6 .   ? 9.672   -5.730  -6.098  1.00  39.18 ? 566 HOH A O   1 
HETATM 2283 O  O   . HOH F 6 .   ? 5.647   -10.767 18.644  1.00  35.84 ? 567 HOH A O   1 
HETATM 2284 O  O   . HOH F 6 .   ? -8.455  7.427   8.023   1.00  32.96 ? 568 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   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS 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 DMS 1   302 1   DMS DMS A . 
D 4 MES 1   303 1   MES MES A . 
E 5 V90 1   304 1   V90 V90 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 . 
# 
_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 
# 
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 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 105.4 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 116.4 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 100.6 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 ? E V90 .   ? A V90 304 ? 1_555 107.0 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 ? E V90 .   ? A V90 304 ? 1_555 108.4 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 ? E V90 .   ? A V90 304 ? 1_555 117.9 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-01-28 
2 'Structure model' 1 1 2023-09-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' pdbx_initial_refinement_model 
5 2 'Structure model' pdbx_struct_conn_angle        
6 2 'Structure model' struct_conn                   
7 2 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_database_2.pdbx_DOI'                        
2  2 'Structure model' '_database_2.pdbx_database_accession'         
3  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
15 2 'Structure model' '_pdbx_struct_conn_angle.value'               
16 2 'Structure model' '_struct_conn.pdbx_dist_value'                
17 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
18 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
19 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
20 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
21 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
22 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
23 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
24 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
25 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
26 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
27 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
28 2 'Structure model' '_struct_site.pdbx_auth_asym_id'              
29 2 'Structure model' '_struct_site.pdbx_auth_comp_id'              
30 2 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.2.19 22/12/2005      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 
HKL-3000    .      ?               ?       ?                    ?                        '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 ARG A 27  ? ? -145.03 59.63   
2 1 LYS A 111 ? ? 72.42   -2.14   
3 1 PHE A 176 ? ? -150.81 76.49   
4 1 ASN A 244 ? ? -94.95  50.54   
5 1 LYS A 252 ? ? 60.35   -135.41 
6 1 ASN A 253 ? ? -90.62  57.15   
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 A MES 303 ? C8  ? D MES 1 C8  
2 1 N 1 A MES 303 ? S   ? D MES 1 S   
3 1 N 1 A MES 303 ? O1S ? D MES 1 O1S 
4 1 N 1 A MES 303 ? O2S ? D MES 1 O2S 
5 1 N 1 A MES 303 ? O3S ? D MES 1 O3S 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
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  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  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 
MES O1   O  N N 240 
MES C2   C  N N 241 
MES C3   C  N N 242 
MES N4   N  N N 243 
MES C5   C  N N 244 
MES C6   C  N N 245 
MES C7   C  N N 246 
MES C8   C  N N 247 
MES S    S  N N 248 
MES O1S  O  N N 249 
MES O2S  O  N N 250 
MES O3S  O  N N 251 
MES H21  H  N N 252 
MES H22  H  N N 253 
MES H31  H  N N 254 
MES H32  H  N N 255 
MES HN4  H  N N 256 
MES H51  H  N N 257 
MES H52  H  N N 258 
MES H61  H  N N 259 
MES H62  H  N N 260 
MES H71  H  N N 261 
MES H72  H  N N 262 
MES H81  H  N N 263 
MES H82  H  N N 264 
MET N    N  N N 265 
MET CA   C  N S 266 
MET C    C  N N 267 
MET O    O  N N 268 
MET CB   C  N N 269 
MET CG   C  N N 270 
MET SD   S  N N 271 
MET CE   C  N N 272 
MET OXT  O  N N 273 
MET H    H  N N 274 
MET H2   H  N N 275 
MET HA   H  N N 276 
MET HB2  H  N N 277 
MET HB3  H  N N 278 
MET HG2  H  N N 279 
MET HG3  H  N N 280 
MET HE1  H  N N 281 
MET HE2  H  N N 282 
MET HE3  H  N N 283 
MET HXT  H  N N 284 
PHE N    N  N N 285 
PHE CA   C  N S 286 
PHE C    C  N N 287 
PHE O    O  N N 288 
PHE CB   C  N N 289 
PHE CG   C  Y N 290 
PHE CD1  C  Y N 291 
PHE CD2  C  Y N 292 
PHE CE1  C  Y N 293 
PHE CE2  C  Y N 294 
PHE CZ   C  Y N 295 
PHE OXT  O  N N 296 
PHE H    H  N N 297 
PHE H2   H  N N 298 
PHE HA   H  N N 299 
PHE HB2  H  N N 300 
PHE HB3  H  N N 301 
PHE HD1  H  N N 302 
PHE HD2  H  N N 303 
PHE HE1  H  N N 304 
PHE HE2  H  N N 305 
PHE HZ   H  N N 306 
PHE HXT  H  N N 307 
PRO N    N  N N 308 
PRO CA   C  N S 309 
PRO C    C  N N 310 
PRO O    O  N N 311 
PRO CB   C  N N 312 
PRO CG   C  N N 313 
PRO CD   C  N N 314 
PRO OXT  O  N N 315 
PRO H    H  N N 316 
PRO HA   H  N N 317 
PRO HB2  H  N N 318 
PRO HB3  H  N N 319 
PRO HG2  H  N N 320 
PRO HG3  H  N N 321 
PRO HD2  H  N N 322 
PRO HD3  H  N N 323 
PRO HXT  H  N N 324 
SER N    N  N N 325 
SER CA   C  N S 326 
SER C    C  N N 327 
SER O    O  N N 328 
SER CB   C  N N 329 
SER OG   O  N N 330 
SER OXT  O  N N 331 
SER H    H  N N 332 
SER H2   H  N N 333 
SER HA   H  N N 334 
SER HB2  H  N N 335 
SER HB3  H  N N 336 
SER HG   H  N N 337 
SER HXT  H  N N 338 
THR N    N  N N 339 
THR CA   C  N S 340 
THR C    C  N N 341 
THR O    O  N N 342 
THR CB   C  N R 343 
THR OG1  O  N N 344 
THR CG2  C  N N 345 
THR OXT  O  N N 346 
THR H    H  N N 347 
THR H2   H  N N 348 
THR HA   H  N N 349 
THR HB   H  N N 350 
THR HG1  H  N N 351 
THR HG21 H  N N 352 
THR HG22 H  N N 353 
THR HG23 H  N N 354 
THR HXT  H  N N 355 
TRP N    N  N N 356 
TRP CA   C  N S 357 
TRP C    C  N N 358 
TRP O    O  N N 359 
TRP CB   C  N N 360 
TRP CG   C  Y N 361 
TRP CD1  C  Y N 362 
TRP CD2  C  Y N 363 
TRP NE1  N  Y N 364 
TRP CE2  C  Y N 365 
TRP CE3  C  Y N 366 
TRP CZ2  C  Y N 367 
TRP CZ3  C  Y N 368 
TRP CH2  C  Y N 369 
TRP OXT  O  N N 370 
TRP H    H  N N 371 
TRP H2   H  N N 372 
TRP HA   H  N N 373 
TRP HB2  H  N N 374 
TRP HB3  H  N N 375 
TRP HD1  H  N N 376 
TRP HE1  H  N N 377 
TRP HE3  H  N N 378 
TRP HZ2  H  N N 379 
TRP HZ3  H  N N 380 
TRP HH2  H  N N 381 
TRP HXT  H  N N 382 
TYR N    N  N N 383 
TYR CA   C  N S 384 
TYR C    C  N N 385 
TYR O    O  N N 386 
TYR CB   C  N N 387 
TYR CG   C  Y N 388 
TYR CD1  C  Y N 389 
TYR CD2  C  Y N 390 
TYR CE1  C  Y N 391 
TYR CE2  C  Y N 392 
TYR CZ   C  Y N 393 
TYR OH   O  N N 394 
TYR OXT  O  N N 395 
TYR H    H  N N 396 
TYR H2   H  N N 397 
TYR HA   H  N N 398 
TYR HB2  H  N N 399 
TYR HB3  H  N N 400 
TYR HD1  H  N N 401 
TYR HD2  H  N N 402 
TYR HE1  H  N N 403 
TYR HE2  H  N N 404 
TYR HH   H  N N 405 
TYR HXT  H  N N 406 
V90 F18  F  N N 407 
V90 C5   C  Y N 408 
V90 C6   C  Y N 409 
V90 S12  S  N N 410 
V90 C13  C  N N 411 
V90 C14  C  N N 412 
V90 O15  O  N N 413 
V90 C1   C  Y N 414 
V90 F17  F  N N 415 
V90 C4   C  Y N 416 
V90 C3   C  Y N 417 
V90 S8   S  N N 418 
V90 O10  O  N N 419 
V90 N11  N  N N 420 
V90 O9   O  N N 421 
V90 C2   C  Y N 422 
V90 F16  F  N N 423 
V90 N7   N  N N 424 
V90 C19  C  N N 425 
V90 C26  C  N N 426 
V90 C25  C  N N 427 
V90 C24  C  N N 428 
V90 C23  C  N N 429 
V90 C22  C  N N 430 
V90 C21  C  N N 431 
V90 C20  C  N N 432 
V90 H1   H  N N 433 
V90 H2   H  N N 434 
V90 H3   H  N N 435 
V90 H4   H  N N 436 
V90 H5   H  N N 437 
V90 H6   H  N N 438 
V90 H7   H  N N 439 
V90 H8   H  N N 440 
V90 H9   H  N N 441 
V90 H10  H  N N 442 
V90 H11  H  N N 443 
V90 H12  H  N N 444 
V90 H13  H  N N 445 
V90 H14  H  N N 446 
V90 H15  H  N N 447 
V90 H16  H  N N 448 
V90 H17  H  N N 449 
V90 H18  H  N N 450 
V90 H19  H  N N 451 
V90 H20  H  N N 452 
V90 H21  H  N N 453 
V90 H22  H  N N 454 
V90 H23  H  N N 455 
VAL N    N  N N 456 
VAL CA   C  N S 457 
VAL C    C  N N 458 
VAL O    O  N N 459 
VAL CB   C  N N 460 
VAL CG1  C  N N 461 
VAL CG2  C  N N 462 
VAL OXT  O  N N 463 
VAL H    H  N N 464 
VAL H2   H  N N 465 
VAL HA   H  N N 466 
VAL HB   H  N N 467 
VAL HG11 H  N N 468 
VAL HG12 H  N N 469 
VAL HG13 H  N N 470 
VAL HG21 H  N N 471 
VAL HG22 H  N N 472 
VAL HG23 H  N N 473 
VAL HXT  H  N N 474 
ZN  ZN   ZN N N 475 
# 
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  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  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 
MES O1  C2   sing N N 227 
MES O1  C6   sing N N 228 
MES C2  C3   sing N N 229 
MES C2  H21  sing N N 230 
MES C2  H22  sing N N 231 
MES C3  N4   sing N N 232 
MES C3  H31  sing N N 233 
MES C3  H32  sing N N 234 
MES N4  C5   sing N N 235 
MES N4  C7   sing N N 236 
MES N4  HN4  sing N N 237 
MES C5  C6   sing N N 238 
MES C5  H51  sing N N 239 
MES C5  H52  sing N N 240 
MES C6  H61  sing N N 241 
MES C6  H62  sing N N 242 
MES C7  C8   sing N N 243 
MES C7  H71  sing N N 244 
MES C7  H72  sing N N 245 
MES C8  S    sing N N 246 
MES C8  H81  sing N N 247 
MES C8  H82  sing N N 248 
MES S   O1S  doub N N 249 
MES S   O2S  doub N N 250 
MES S   O3S  sing N N 251 
MET N   CA   sing N N 252 
MET N   H    sing N N 253 
MET N   H2   sing N N 254 
MET CA  C    sing N N 255 
MET CA  CB   sing N N 256 
MET CA  HA   sing N N 257 
MET C   O    doub N N 258 
MET C   OXT  sing N N 259 
MET CB  CG   sing N N 260 
MET CB  HB2  sing N N 261 
MET CB  HB3  sing N N 262 
MET CG  SD   sing N N 263 
MET CG  HG2  sing N N 264 
MET CG  HG3  sing N N 265 
MET SD  CE   sing N N 266 
MET CE  HE1  sing N N 267 
MET CE  HE2  sing N N 268 
MET CE  HE3  sing N N 269 
MET OXT HXT  sing N N 270 
PHE N   CA   sing N N 271 
PHE N   H    sing N N 272 
PHE N   H2   sing N N 273 
PHE CA  C    sing N N 274 
PHE CA  CB   sing N N 275 
PHE CA  HA   sing N N 276 
PHE C   O    doub N N 277 
PHE C   OXT  sing N N 278 
PHE CB  CG   sing N N 279 
PHE CB  HB2  sing N N 280 
PHE CB  HB3  sing N N 281 
PHE CG  CD1  doub Y N 282 
PHE CG  CD2  sing Y N 283 
PHE CD1 CE1  sing Y N 284 
PHE CD1 HD1  sing N N 285 
PHE CD2 CE2  doub Y N 286 
PHE CD2 HD2  sing N N 287 
PHE CE1 CZ   doub Y N 288 
PHE CE1 HE1  sing N N 289 
PHE CE2 CZ   sing Y N 290 
PHE CE2 HE2  sing N N 291 
PHE CZ  HZ   sing N N 292 
PHE OXT HXT  sing N N 293 
PRO N   CA   sing N N 294 
PRO N   CD   sing N N 295 
PRO N   H    sing N N 296 
PRO CA  C    sing N N 297 
PRO CA  CB   sing N N 298 
PRO CA  HA   sing N N 299 
PRO C   O    doub N N 300 
PRO C   OXT  sing N N 301 
PRO CB  CG   sing N N 302 
PRO CB  HB2  sing N N 303 
PRO CB  HB3  sing N N 304 
PRO CG  CD   sing N N 305 
PRO CG  HG2  sing N N 306 
PRO CG  HG3  sing N N 307 
PRO CD  HD2  sing N N 308 
PRO CD  HD3  sing N N 309 
PRO OXT HXT  sing N N 310 
SER N   CA   sing N N 311 
SER N   H    sing N N 312 
SER N   H2   sing N N 313 
SER CA  C    sing N N 314 
SER CA  CB   sing N N 315 
SER CA  HA   sing N N 316 
SER C   O    doub N N 317 
SER C   OXT  sing N N 318 
SER CB  OG   sing N N 319 
SER CB  HB2  sing N N 320 
SER CB  HB3  sing N N 321 
SER OG  HG   sing N N 322 
SER OXT HXT  sing N N 323 
THR N   CA   sing N N 324 
THR N   H    sing N N 325 
THR N   H2   sing N N 326 
THR CA  C    sing N N 327 
THR CA  CB   sing N N 328 
THR CA  HA   sing N N 329 
THR C   O    doub N N 330 
THR C   OXT  sing N N 331 
THR CB  OG1  sing N N 332 
THR CB  CG2  sing N N 333 
THR CB  HB   sing N N 334 
THR OG1 HG1  sing N N 335 
THR CG2 HG21 sing N N 336 
THR CG2 HG22 sing N N 337 
THR CG2 HG23 sing N N 338 
THR OXT HXT  sing N N 339 
TRP N   CA   sing N N 340 
TRP N   H    sing N N 341 
TRP N   H2   sing N N 342 
TRP CA  C    sing N N 343 
TRP CA  CB   sing N N 344 
TRP CA  HA   sing N N 345 
TRP C   O    doub N N 346 
TRP C   OXT  sing N N 347 
TRP CB  CG   sing N N 348 
TRP CB  HB2  sing N N 349 
TRP CB  HB3  sing N N 350 
TRP CG  CD1  doub Y N 351 
TRP CG  CD2  sing Y N 352 
TRP CD1 NE1  sing Y N 353 
TRP CD1 HD1  sing N N 354 
TRP CD2 CE2  doub Y N 355 
TRP CD2 CE3  sing Y N 356 
TRP NE1 CE2  sing Y N 357 
TRP NE1 HE1  sing N N 358 
TRP CE2 CZ2  sing Y N 359 
TRP CE3 CZ3  doub Y N 360 
TRP CE3 HE3  sing N N 361 
TRP CZ2 CH2  doub Y N 362 
TRP CZ2 HZ2  sing N N 363 
TRP CZ3 CH2  sing Y N 364 
TRP CZ3 HZ3  sing N N 365 
TRP CH2 HH2  sing N N 366 
TRP OXT HXT  sing N N 367 
TYR N   CA   sing N N 368 
TYR N   H    sing N N 369 
TYR N   H2   sing N N 370 
TYR CA  C    sing N N 371 
TYR CA  CB   sing N N 372 
TYR CA  HA   sing N N 373 
TYR C   O    doub N N 374 
TYR C   OXT  sing N N 375 
TYR CB  CG   sing N N 376 
TYR CB  HB2  sing N N 377 
TYR CB  HB3  sing N N 378 
TYR CG  CD1  doub Y N 379 
TYR CG  CD2  sing Y N 380 
TYR CD1 CE1  sing Y N 381 
TYR CD1 HD1  sing N N 382 
TYR CD2 CE2  doub Y N 383 
TYR CD2 HD2  sing N N 384 
TYR CE1 CZ   doub Y N 385 
TYR CE1 HE1  sing N N 386 
TYR CE2 CZ   sing Y N 387 
TYR CE2 HE2  sing N N 388 
TYR CZ  OH   sing N N 389 
TYR OH  HH   sing N N 390 
TYR OXT HXT  sing N N 391 
V90 C22 C23  sing N N 392 
V90 C22 C21  sing N N 393 
V90 C23 C24  sing N N 394 
V90 C24 C25  sing N N 395 
V90 O15 C14  sing N N 396 
V90 C21 C20  sing N N 397 
V90 C14 C13  sing N N 398 
V90 C25 C26  sing N N 399 
V90 C20 C19  sing N N 400 
V90 C13 S12  sing N N 401 
V90 C26 C19  sing N N 402 
V90 C19 N7   sing N N 403 
V90 F18 C5   sing N N 404 
V90 S12 C6   sing N N 405 
V90 C5  C6   doub Y N 406 
V90 C5  C4   sing Y N 407 
V90 N7  C4   sing N N 408 
V90 C6  C1   sing Y N 409 
V90 C4  C3   doub Y N 410 
V90 C1  F17  sing N N 411 
V90 C1  C2   doub Y N 412 
V90 C3  C2   sing Y N 413 
V90 C3  S8   sing N N 414 
V90 N11 S8   sing N N 415 
V90 C2  F16  sing N N 416 
V90 O10 S8   doub N N 417 
V90 S8  O9   doub N N 418 
V90 C13 H1   sing N N 419 
V90 C13 H2   sing N N 420 
V90 C14 H3   sing N N 421 
V90 C14 H4   sing N N 422 
V90 O15 H5   sing N N 423 
V90 N11 H6   sing N N 424 
V90 N11 H7   sing N N 425 
V90 N7  H8   sing N N 426 
V90 C19 H9   sing N N 427 
V90 C26 H10  sing N N 428 
V90 C26 H11  sing N N 429 
V90 C25 H12  sing N N 430 
V90 C25 H13  sing N N 431 
V90 C24 H14  sing N N 432 
V90 C24 H15  sing N N 433 
V90 C23 H16  sing N N 434 
V90 C23 H17  sing N N 435 
V90 C22 H18  sing N N 436 
V90 C22 H19  sing N N 437 
V90 C21 H20  sing N N 438 
V90 C21 H21  sing N N 439 
V90 C20 H22  sing N N 440 
V90 C20 H23  sing N N 441 
VAL N   CA   sing N N 442 
VAL N   H    sing N N 443 
VAL N   H2   sing N N 444 
VAL CA  C    sing N N 445 
VAL CA  CB   sing N N 446 
VAL CA  HA   sing N N 447 
VAL C   O    doub N N 448 
VAL C   OXT  sing N N 449 
VAL CB  CG1  sing N N 450 
VAL CB  CG2  sing N N 451 
VAL CB  HB   sing N N 452 
VAL CG1 HG11 sing N N 453 
VAL CG1 HG12 sing N N 454 
VAL CG1 HG13 sing N N 455 
VAL CG2 HG21 sing N N 456 
VAL CG2 HG22 sing N N 457 
VAL CG2 HG23 sing N N 458 
VAL OXT HXT  sing N N 459 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                           ZN  
3 'DIMETHYL SULFOXIDE'                                                                 DMS 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                               MES 
5 '2-(cyclooctylamino)-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' V90 
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   3HLJ 
_pdbx_initial_refinement_model.details          'PDB ENTRY 3HLJ' 
# 
