data_4QSA
# 
_entry.id   4QSA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.381 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4QSA         pdb_00004qsa 10.2210/pdb4qsa/pdb 
RCSB  RCSB086449   ?            ?                   
WWPDB D_1000086449 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4QSB . unspecified 
PDB 4QSI . unspecified 
PDB 4QSJ . unspecified 
# 
_pdbx_database_status.entry_id                        4QSA 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2014-07-03 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
;Intrinsic Thermodynamics and Structure Correlation of Benzenesulfonamides with a Pyrimidine Moiety Binding to Carbonic Anhydrases I, II, VII, XII, and XIII
;
_citation.journal_abbrev            'Plos One' 
_citation.journal_volume            9 
_citation.page_first                e114106 
_citation.page_last                 e114106 
_citation.year                      2014 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25493428 
_citation.pdbx_database_id_DOI      10.1371/journal.pone.0114106 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kisonaite, M.'     1  ? 
primary 'Zubriene, A.'      2  ? 
primary 'Capkauskaite, E.'  3  ? 
primary 'Smirnov, A.'       4  ? 
primary 'Smirnoviene, J.'   5  ? 
primary 'Kairys, V.'        6  ? 
primary 'Michailoviene, V.' 7  ? 
primary 'Manakova, E.'      8  ? 
primary 'Grazulis, S.'      9  ? 
primary 'Matulis, D.'       10 ? 
# 
_cell.entry_id           4QSA 
_cell.length_a           42.121 
_cell.length_b           40.988 
_cell.length_c           71.645 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.060 
_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                         4QSA 
_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 '2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' 373.835   1   ? ? ? 
? 
4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                                      195.237   1   ? ? ? 
? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                        78.133    1   ? ? ? 
? 
6 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                                     106.120   1   ? ? ? 
? 
7 water       nat water                                                                                       18.015    270 ? ? ? 
? 
# 
_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     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    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              4QSA 
_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  
EWW non-polymer         . '2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' ? 
'C13 H12 Cl N3 O4 S2' 373.835 
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                                     ? 
'C4 H10 O3'           106.120 
PHE 'L-peptide linking' y PHENYLALANINE                                                                               ? 
'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                                                     ? 
'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                                                      ? 
'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                                                                   ? 
'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                  ? 
'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                    ? 
'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                                                                      ? 
'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                                                                  ? 'Zn 2' 
65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4QSA 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   38.0 
_exptl_crystal.density_Matthews      2.00 
_exptl_crystal.pdbx_mosaicity        1.02 
_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    '2M sodium malonate pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2011-11-19 
_diffrn_detector.details                'Mirror Bent, vertically focussing' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8123 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.pdbx_wavelength_list        0.8123 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
# 
_reflns.entry_id                     4QSA 
_reflns.d_resolution_high            1.501 
_reflns.d_resolution_low             23.166 
_reflns.number_all                   ? 
_reflns.number_obs                   38075 
_reflns.pdbx_netI_over_sigmaI        17.300 
_reflns.pdbx_Rsym_value              0.065 
_reflns.pdbx_redundancy              7.000 
_reflns.percent_possible_obs         99.200 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        12.960 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.50 1.58  ? 27366 ? ? 0.119 5.5  0.119 ? 5.50  ? 8.50  ? 5018 ? ? 0.142 ? 94.70  0.14 0.06 1  1 
1.58 1.68  ? 29207 ? ? 0.106 6.1  0.106 ? 5.50  ? 10.10 ? 5316 ? ? 0.126 ? 100.00 0.13 0.05 2  1 
1.68 1.79  ? 27588 ? ? 0.092 7.0  0.092 ? 5.50  ? 11.80 ? 4972 ? ? 0.109 ? 100.00 0.11 0.05 3  1 
1.79 1.94  ? 26097 ? ? 0.081 7.6  0.081 ? 5.60  ? 14.20 ? 4655 ? ? 0.096 ? 100.00 0.10 0.04 4  1 
1.94 2.12  ? 24241 ? ? 0.074 8.0  0.074 ? 5.60  ? 16.70 ? 4311 ? ? 0.087 ? 100.00 0.09 0.04 5  1 
2.12 2.37  ? 21881 ? ? 0.070 8.6  0.070 ? 5.70  ? 18.00 ? 3872 ? ? 0.081 ? 100.00 0.08 0.03 6  1 
2.37 2.74  ? 33608 ? ? 0.084 7.5  0.084 ? 9.80  ? 22.80 ? 3444 ? ? 0.092 ? 100.00 0.09 0.03 7  1 
2.74 3.35  ? 36907 ? ? 0.070 9.0  0.070 ? 12.70 ? 31.80 ? 2913 ? ? 0.075 ? 100.00 0.08 0.02 8  1 
3.35 4.74  ? 25500 ? ? 0.052 11.5 0.052 ? 11.10 ? 36.50 ? 2287 ? ? 0.057 ? 100.00 0.06 0.02 9  1 
4.74 23.17 ? 12411 ? ? 0.044 12.8 0.044 ? 9.60  ? 32.60 ? 1287 ? ? 0.050 ? 99.10  0.05 0.02 10 1 
# 
_refine.entry_id                                 4QSA 
_refine.ls_d_res_high                            1.501 
_refine.ls_d_res_low                             22.650 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.690 
_refine.ls_number_reflns_obs                     38052 
_refine.ls_number_reflns_all                     38052 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES' 
_refine.ls_R_factor_all                          0.170 
_refine.ls_R_factor_obs                          0.170 
_refine.ls_R_factor_R_work                       0.166 
_refine.ls_wR_factor_R_work                      0.182 
_refine.ls_R_factor_R_free                       0.205 
_refine.ls_wR_factor_R_free                      0.227 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  3842 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               15.163 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.180 
_refine.aniso_B[2][2]                            -0.380 
_refine.aniso_B[3][3]                            0.200 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.010 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_refine.overall_SU_R_Cruickshank_DPI             0.082 
_refine.overall_SU_R_free                        0.086 
_refine.pdbx_overall_ESU_R                       0.082 
_refine.pdbx_overall_ESU_R_Free                  0.086 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.876 
_refine.B_iso_max                                66.11 
_refine.B_iso_min                                3.62 
_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                      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        2059 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.number_atoms_solvent             270 
_refine_hist.number_atoms_total               2372 
_refine_hist.d_res_high                       1.501 
_refine_hist.d_res_low                        22.650 
# 
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       2274 0.024  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3096 2.289  1.976  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 276  7.288  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 105  34.289 24.952 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 368  14.252 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 7    26.133 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         313  0.162  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1781 0.014  0.021  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.501 
_refine_ls_shell.d_res_low                        1.540 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               97.140 
_refine_ls_shell.number_reflns_R_work             2409 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.220 
_refine_ls_shell.R_factor_R_free                  0.285 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             279 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                2688 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  4QSA 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)thio]acetyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4QSA 
_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 ? 
G N N 7 ? 
# 
_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  ? GLU A 14  ? GLY A 12  GLU A 14  5 ? 3 
HELX_P HELX_P2  2  HIS A 15  ? PHE A 20  ? HIS A 15  PHE A 20  1 ? 6 
HELX_P HELX_P3  3  PRO A 21  ? GLY A 25  ? PRO A 21  GLY A 25  5 ? 5 
HELX_P HELX_P4  4  LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P5  5  ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P6  6  LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P7  7  LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P8  8  ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P9  9  ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P10 10 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 ? ? ? ? ? ? ? 1.999 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.008 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C EWW . N11 B ? A ZN  301 A EWW 302 1_555 ? ? ? ? ? ? ? 1.784 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C EWW . N11 A ? A ZN  301 A EWW 302 1_555 ? ? ? ? ? ? ? 1.873 ? ? 
metalc6 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C EWW . O8  B ? A ZN  301 A EWW 302 1_555 ? ? ? ? ? ? ? 2.614 ? ? 
# 
_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 0.21 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 8.07 
# 
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 PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
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 EWW 302 ? 18 'BINDING SITE FOR RESIDUE EWW A 302' 
AC3 Software A MES 303 ? 5  'BINDING SITE FOR RESIDUE MES A 303' 
AC4 Software A DMS 304 ? 3  'BINDING SITE FOR RESIDUE DMS A 304' 
AC5 Software A PEG 305 ? 7  'BINDING SITE FOR RESIDUE PEG A 305' 
# 
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  EWW C .   ? EWW A 302 . ? 1_555 ? 
5  AC2 18 GLN A 92  ? GLN A 92  . ? 1_555 ? 
6  AC2 18 HIS A 94  ? HIS A 94  . ? 1_555 ? 
7  AC2 18 HIS A 96  ? HIS A 96  . ? 1_555 ? 
8  AC2 18 HIS A 119 ? HIS A 119 . ? 1_555 ? 
9  AC2 18 VAL A 121 ? VAL A 121 . ? 1_555 ? 
10 AC2 18 PHE A 130 ? PHE A 131 . ? 1_555 ? 
11 AC2 18 VAL A 134 ? VAL A 135 . ? 1_555 ? 
12 AC2 18 VAL A 142 ? VAL A 143 . ? 1_555 ? 
13 AC2 18 LEU A 197 ? LEU A 198 . ? 1_555 ? 
14 AC2 18 THR A 198 ? THR A 199 . ? 1_555 ? 
15 AC2 18 THR A 199 ? THR A 200 . ? 1_555 ? 
16 AC2 18 PRO A 201 ? PRO A 202 . ? 1_555 ? 
17 AC2 18 LEU A 203 ? LEU A 204 . ? 1_555 ? 
18 AC2 18 TRP A 208 ? TRP A 209 . ? 1_555 ? 
19 AC2 18 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
20 AC2 18 HOH G .   ? HOH A 559 . ? 1_555 ? 
21 AC2 18 HOH G .   ? HOH A 616 . ? 1_555 ? 
22 AC2 18 HOH G .   ? HOH A 652 . ? 1_555 ? 
23 AC3 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
24 AC3 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
25 AC3 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
26 AC3 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
27 AC3 5  HOH G .   ? HOH A 626 . ? 1_555 ? 
28 AC4 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
29 AC4 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
30 AC4 3  HOH G .   ? HOH A 609 . ? 1_555 ? 
31 AC5 7  ALA A 247 ? ALA A 248 . ? 1_555 ? 
32 AC5 7  GLN A 248 ? GLN A 249 . ? 1_555 ? 
33 AC5 7  PRO A 249 ? PRO A 250 . ? 1_555 ? 
34 AC5 7  HOH G .   ? HOH A 405 . ? 1_555 ? 
35 AC5 7  HOH G .   ? HOH A 487 . ? 1_555 ? 
36 AC5 7  HOH G .   ? HOH A 498 . ? 1_555 ? 
37 AC5 7  HOH G .   ? HOH A 578 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4QSA 
_atom_sites.fract_transf_matrix[1][1]   0.023741 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005945 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024397 
_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]   0.014389 
_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  
CL 
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 3   ? 13.766  -0.104  6.502   1.00  22.23 ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 3   ? 13.459  -1.112  7.557   1.00  27.50 ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 3   ? 12.420  -0.617  8.573   1.00  31.55 ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 3   ? 12.649  -0.561  9.825   1.00  31.38 ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 3   ? 14.717  -1.517  8.288   1.00  27.78 ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 3   ? 14.535  -2.762  9.067   1.00  30.34 ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 3   ? 14.118  -2.762  10.364  1.00  29.43 ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 3   ? 14.628  -4.100  8.666   1.00  30.89 ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 3   ? 14.015  -4.044  10.782  1.00  30.39 ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 3   ? 14.327  -4.861  9.745   1.00  37.22 ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 4   ? 11.238  -0.264  8.046   1.00  26.33 ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 4   ? 10.198  0.218   8.940   1.00  27.30 ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 4   ? 9.397   -0.890  9.551   1.00  20.59 ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 4   ? 9.551   -2.078  9.251   1.00  18.40 ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 4   ? 9.324   1.287   8.259   1.00  34.50 ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 4   ? 8.878   0.910   6.858   1.00  50.58 ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 4   ? 8.672   1.830   5.892   1.00  62.27 ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 4   ? 8.583   -0.326  6.286   1.00  55.68 ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 4   ? 8.277   1.210   4.762   1.00  62.45 ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 4   ? 8.224   -0.105  5.000   1.00  66.11 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.533   -0.498  10.443  1.00  16.68 ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 7.841   -1.519  11.251  1.00  12.72 ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 6.841   -2.262  10.427  1.00  12.39 ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.272   -1.754  9.465   1.00  13.43 ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.183   -0.816  12.463  1.00  11.87 ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 5.985   0.061   12.087  1.00  13.13 ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 5.940   1.448   11.759  1.00  12.20 ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.585   -0.405  12.014  1.00  10.93 ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.620   1.832   11.494  1.00  13.62 ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.778   0.749   11.620  1.00  12.28 ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 3.954   -1.634  12.278  1.00  10.26 ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.407   0.677   11.470  1.00  11.29 ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.535   -1.693  12.065  1.00  10.02 ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 1.797   -0.529  11.736  1.00  10.86 ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.563   -3.467  10.927  1.00  11.70 ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.506   -4.271  10.313  1.00  11.95 ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.222   -5.431  11.216  1.00  11.70 ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.232   -5.323  12.416  1.00  11.13 ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 4.893   -6.541  10.590  1.00  13.81 ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 4.486   -7.697  11.353  1.00  14.80 ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 5.347   -8.966  11.147  1.00  22.96 ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 4.946   -10.052 11.575  1.00  26.73 ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 3.036   -7.991  11.071  1.00  12.62 ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 2.111   -6.916  11.672  1.00  10.92 ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 1.730   -6.971  13.015  1.00  10.23 ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 1.609   -5.906  10.878  1.00  9.50  ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 0.856   -5.947  13.536  1.00  9.06  ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 0.726   -4.932  11.353  1.00  8.85  ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 0.372   -4.976  12.695  1.00  8.67  ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? -0.456  -4.014  13.146  1.00  8.88  ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 6.531   -8.808  10.558  1.00  22.93 ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 7.467   -9.992  10.391  1.00  20.97 ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 8.453   -10.306 11.512  1.00  20.64 ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 8.539   -9.680  12.615  1.00  23.73 ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 9.358   -11.285 11.249  1.00  25.46 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 10.368  -11.720 12.264  1.00  25.82 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 11.341  -10.616 12.591  1.00  23.01 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 11.854  -10.551 13.752  1.00  26.67 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 11.165  -12.921 11.754  1.00  28.78 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 12.250  -13.412 12.708  1.00  31.40 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 12.962  -14.655 12.117  1.00  35.60 ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 14.284  -14.935 12.849  1.00  39.88 ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 14.215  -14.705 14.329  1.00  40.44 ? 9   LYS A NZ  1 
ATOM   64   N  N   . HIS A 1 10  ? 11.600  -9.791  11.570  1.00  22.92 ? 10  HIS A N   1 
ATOM   65   C  CA  . HIS A 1 10  ? 12.586  -8.784  11.727  1.00  22.27 ? 10  HIS A CA  1 
ATOM   66   C  C   . HIS A 1 10  ? 12.070  -7.410  11.978  1.00  16.95 ? 10  HIS A C   1 
ATOM   67   O  O   . HIS A 1 10  ? 12.821  -6.594  12.471  1.00  18.62 ? 10  HIS A O   1 
ATOM   68   C  CB  . HIS A 1 10  ? 13.659  -8.849  10.605  1.00  20.31 ? 10  HIS A CB  1 
ATOM   69   C  CG  . HIS A 1 10  ? 14.416  -10.195 10.580  1.00  19.62 ? 10  HIS A CG  1 
ATOM   70   N  ND1 . HIS A 1 10  ? 15.438  -10.522 11.458  1.00  24.46 ? 10  HIS A ND1 1 
ATOM   71   C  CD2 . HIS A 1 10  ? 14.245  -11.279 9.745   1.00  22.54 ? 10  HIS A CD2 1 
ATOM   72   C  CE1 . HIS A 1 10  ? 15.886  -11.749 11.164  1.00  21.27 ? 10  HIS A CE1 1 
ATOM   73   N  NE2 . HIS A 1 10  ? 15.111  -12.234 10.133  1.00  19.72 ? 10  HIS A NE2 1 
ATOM   74   N  N   . ASN A 1 11  ? 10.731  -7.186  11.801  1.00  16.26 ? 11  ASN A N   1 
ATOM   75   C  CA  . ASN A 1 11  ? 10.218  -5.810  12.051  1.00  13.82 ? 11  ASN A CA  1 
ATOM   76   C  C   . ASN A 1 11  ? 8.871   -5.846  12.801  1.00  14.23 ? 11  ASN A C   1 
ATOM   77   O  O   . ASN A 1 11  ? 8.215   -4.834  12.865  1.00  13.76 ? 11  ASN A O   1 
ATOM   78   C  CB  . ASN A 1 11  ? 10.006  -5.050  10.786  1.00  13.34 ? 11  ASN A CB  1 
ATOM   79   C  CG  . ASN A 1 11  ? 8.972   -5.662  9.879   1.00  13.47 ? 11  ASN A CG  1 
ATOM   80   O  OD1 . ASN A 1 11  ? 8.458   -6.757  10.196  1.00  16.12 ? 11  ASN A OD1 1 
ATOM   81   N  ND2 . ASN A 1 11  ? 8.652   -5.041  8.777   1.00  15.92 ? 11  ASN A ND2 1 
ATOM   82   N  N   . GLY A 1 12  ? 8.564   -7.002  13.368  1.00  13.98 ? 12  GLY A N   1 
ATOM   83   C  CA  . GLY A 1 12  ? 7.223   -7.222  14.017  1.00  13.08 ? 12  GLY A CA  1 
ATOM   84   C  C   . GLY A 1 12  ? 7.209   -6.631  15.421  1.00  12.29 ? 12  GLY A C   1 
ATOM   85   O  O   . GLY A 1 12  ? 8.094   -5.882  15.878  1.00  12.08 ? 12  GLY A O   1 
ATOM   86   N  N   . PRO A 1 13  ? 6.109   -6.920  16.163  1.00  11.36 ? 13  PRO A N   1 
ATOM   87   C  CA  . PRO A 1 13  ? 5.866   -6.284  17.411  1.00  12.37 ? 13  PRO A CA  1 
ATOM   88   C  C   . PRO A 1 13  ? 6.978   -6.301  18.417  1.00  10.57 ? 13  PRO A C   1 
ATOM   89   O  O   . PRO A 1 13  ? 7.180   -5.314  19.179  1.00  12.11 ? 13  PRO A O   1 
ATOM   90   C  CB  . PRO A 1 13  ? 4.624   -7.052  17.942  1.00  12.43 ? 13  PRO A CB  1 
ATOM   91   C  CG  . PRO A 1 13  ? 3.901   -7.482  16.738  1.00  12.11 ? 13  PRO A CG  1 
ATOM   92   C  CD  . PRO A 1 13  ? 4.955   -7.707  15.658  1.00  10.93 ? 13  PRO A CD  1 
ATOM   93   N  N   . GLU A 1 14  ? 7.776   -7.384  18.470  1.00  12.16 ? 14  GLU A N   1 
ATOM   94   C  CA  . GLU A 1 14  ? 8.874   -7.450  19.449  1.00  13.70 ? 14  GLU A CA  1 
ATOM   95   C  C   . GLU A 1 14  ? 10.062  -6.461  19.132  1.00  12.30 ? 14  GLU A C   1 
ATOM   96   O  O   . GLU A 1 14  ? 10.936  -6.230  19.968  1.00  13.62 ? 14  GLU A O   1 
ATOM   97   C  CB  . GLU A 1 14  ? 9.422   -8.910  19.471  1.00  17.77 ? 14  GLU A CB  1 
ATOM   98   C  CG  . GLU A 1 14  ? 10.078  -9.421  18.151  1.00  21.61 ? 14  GLU A CG  1 
ATOM   99   C  CD  . GLU A 1 14  ? 9.211   -9.929  16.942  1.00  28.65 ? 14  GLU A CD  1 
ATOM   100  O  OE1 . GLU A 1 14  ? 7.974   -9.596  16.793  1.00  20.16 ? 14  GLU A OE1 1 
ATOM   101  O  OE2 . GLU A 1 14  ? 9.873   -10.648 16.067  1.00  27.42 ? 14  GLU A OE2 1 
ATOM   102  N  N   . HIS A 1 15  ? 9.992   -5.854  17.954  1.00  12.94 ? 15  HIS A N   1 
ATOM   103  C  CA  . HIS A 1 15  ? 10.971  -4.848  17.520  1.00  12.24 ? 15  HIS A CA  1 
ATOM   104  C  C   . HIS A 1 15  ? 10.582  -3.425  17.699  1.00  11.99 ? 15  HIS A C   1 
ATOM   105  O  O   . HIS A 1 15  ? 11.408  -2.521  17.617  1.00  12.90 ? 15  HIS A O   1 
ATOM   106  C  CB  . HIS A 1 15  ? 11.365  -5.057  16.044  1.00  12.74 ? 15  HIS A CB  1 
ATOM   107  C  CG  . HIS A 1 15  ? 12.072  -6.352  15.810  1.00  14.41 ? 15  HIS A CG  1 
ATOM   108  N  ND1 . HIS A 1 15  ? 13.443  -6.480  16.001  1.00  16.83 ? 15  HIS A ND1 1 
ATOM   109  C  CD2 . HIS A 1 15  ? 11.596  -7.570  15.363  1.00  16.62 ? 15  HIS A CD2 1 
ATOM   110  C  CE1 . HIS A 1 15  ? 13.768  -7.792  15.751  1.00  17.28 ? 15  HIS A CE1 1 
ATOM   111  N  NE2 . HIS A 1 15  ? 12.707  -8.427  15.304  1.00  18.06 ? 15  HIS A NE2 1 
ATOM   112  N  N   . TRP A 1 16  ? 9.277   -3.182  17.900  1.00  10.08 ? 16  TRP A N   1 
ATOM   113  C  CA  . TRP A 1 16  ? 8.816   -1.839  17.780  1.00  9.79  ? 16  TRP A CA  1 
ATOM   114  C  C   . TRP A 1 16  ? 9.355   -0.917  18.798  1.00  8.91  ? 16  TRP A C   1 
ATOM   115  O  O   . TRP A 1 16  ? 9.417   0.299   18.494  1.00  10.11 ? 16  TRP A O   1 
ATOM   116  C  CB  . TRP A 1 16  ? 7.248   -1.862  17.901  1.00  8.23  ? 16  TRP A CB  1 
ATOM   117  C  CG  . TRP A 1 16  ? 6.606   -2.548  16.759  1.00  9.31  ? 16  TRP A CG  1 
ATOM   118  C  CD1 . TRP A 1 16  ? 7.119   -2.998  15.534  1.00  7.91  ? 16  TRP A CD1 1 
ATOM   119  C  CD2 . TRP A 1 16  ? 5.169   -2.890  16.724  1.00  8.92  ? 16  TRP A CD2 1 
ATOM   120  N  NE1 . TRP A 1 16  ? 6.116   -3.582  14.756  1.00  9.00  ? 16  TRP A NE1 1 
ATOM   121  C  CE2 . TRP A 1 16  ? 4.915   -3.506  15.453  1.00  8.30  ? 16  TRP A CE2 1 
ATOM   122  C  CE3 . TRP A 1 16  ? 4.101   -2.649  17.582  1.00  8.62  ? 16  TRP A CE3 1 
ATOM   123  C  CZ2 . TRP A 1 16  ? 3.624   -3.960  15.072  1.00  9.00  ? 16  TRP A CZ2 1 
ATOM   124  C  CZ3 . TRP A 1 16  ? 2.843   -3.099  17.220  1.00  8.47  ? 16  TRP A CZ3 1 
ATOM   125  C  CH2 . TRP A 1 16  ? 2.568   -3.677  15.993  1.00  9.16  ? 16  TRP A CH2 1 
ATOM   126  N  N   . HIS A 1 17  ? 9.794   -1.402  19.948  1.00  10.63 ? 17  HIS A N   1 
ATOM   127  C  CA  . HIS A 1 17  ? 10.230  -0.531  20.982  1.00  10.34 ? 17  HIS A CA  1 
ATOM   128  C  C   . HIS A 1 17  ? 11.513  0.252   20.591  1.00  11.34 ? 17  HIS A C   1 
ATOM   129  O  O   . HIS A 1 17  ? 11.722  1.299   21.203  1.00  11.49 ? 17  HIS A O   1 
ATOM   130  C  CB  . HIS A 1 17  ? 10.496  -1.260  22.285  1.00  10.55 ? 17  HIS A CB  1 
ATOM   131  C  CG  . HIS A 1 17  ? 11.713  -2.172  22.208  1.00  11.56 ? 17  HIS A CG  1 
ATOM   132  N  ND1 . HIS A 1 17  ? 12.924  -1.778  22.737  1.00  15.59 ? 17  HIS A ND1 1 
ATOM   133  C  CD2 . HIS A 1 17  ? 11.910  -3.359  21.606  1.00  12.82 ? 17  HIS A CD2 1 
ATOM   134  C  CE1 . HIS A 1 17  ? 13.833  -2.716  22.476  1.00  14.49 ? 17  HIS A CE1 1 
ATOM   135  N  NE2 . HIS A 1 17  ? 13.274  -3.673  21.787  1.00  14.33 ? 17  HIS A NE2 1 
ATOM   136  N  N   . LYS A 1 18  ? 12.250  -0.260  19.602  1.00  13.22 ? 18  LYS A N   1 
ATOM   137  C  CA  . LYS A 1 18  ? 13.533  0.417   19.224  1.00  13.58 ? 18  LYS A CA  1 
ATOM   138  C  C   . LYS A 1 18  ? 13.179  1.736   18.549  1.00  15.41 ? 18  LYS A C   1 
ATOM   139  O  O   . LYS A 1 18  ? 13.789  2.761   18.901  1.00  19.16 ? 18  LYS A O   1 
ATOM   140  C  CB  . LYS A 1 18  ? 14.318  -0.494  18.289  1.00  15.97 ? 18  LYS A CB  1 
ATOM   141  C  CG  . LYS A 1 18  ? 14.942  -1.657  19.023  1.00  15.58 ? 18  LYS A CG  1 
ATOM   142  C  CD  . LYS A 1 18  ? 15.650  -2.621  18.109  1.00  15.63 ? 18  LYS A CD  1 
ATOM   143  C  CE  . LYS A 1 18  ? 14.666  -3.590  17.460  1.00  15.73 ? 18  LYS A CE  1 
ATOM   144  N  NZ  . LYS A 1 18  ? 15.244  -4.454  16.367  1.00  14.90 ? 18  LYS A NZ  1 
ATOM   145  N  N   . ASP A 1 19  ? 12.143  1.800   17.688  1.00  13.51 ? 19  ASP A N   1 
ATOM   146  C  CA  . ASP A 1 19  ? 11.734  3.099   17.089  1.00  15.14 ? 19  ASP A CA  1 
ATOM   147  C  C   . ASP A 1 19  ? 10.698  3.840   17.936  1.00  13.89 ? 19  ASP A C   1 
ATOM   148  O  O   . ASP A 1 19  ? 10.559  5.057   17.805  1.00  14.90 ? 19  ASP A O   1 
ATOM   149  C  CB  . ASP A 1 19  ? 11.153  2.888   15.719  1.00  19.52 ? 19  ASP A CB  1 
ATOM   150  C  CG  . ASP A 1 19  ? 12.201  2.933   14.638  1.00  25.69 ? 19  ASP A CG  1 
ATOM   151  O  OD1 . ASP A 1 19  ? 13.202  3.619   14.857  1.00  29.94 ? 19  ASP A OD1 1 
ATOM   152  O  OD2 . ASP A 1 19  ? 12.017  2.286   13.584  1.00  35.16 ? 19  ASP A OD2 1 
ATOM   153  N  N   . PHE A 1 20  ? 9.980   3.069   18.782  1.00  12.59 ? 20  PHE A N   1 
ATOM   154  C  CA  . PHE A 1 20  ? 8.821   3.677   19.513  1.00  11.32 ? 20  PHE A CA  1 
ATOM   155  C  C   . PHE A 1 20  ? 8.913   3.181   20.942  1.00  10.91 ? 20  PHE A C   1 
ATOM   156  O  O   . PHE A 1 20  ? 8.307   2.188   21.338  1.00  11.46 ? 20  PHE A O   1 
ATOM   157  C  CB  . PHE A 1 20  ? 7.469   3.251   18.877  1.00  11.21 ? 20  PHE A CB  1 
ATOM   158  C  CG  . PHE A 1 20  ? 7.353   3.651   17.482  1.00  11.64 ? 20  PHE A CG  1 
ATOM   159  C  CD1 . PHE A 1 20  ? 7.042   4.970   17.124  1.00  12.25 ? 20  PHE A CD1 1 
ATOM   160  C  CD2 . PHE A 1 20  ? 7.671   2.730   16.497  1.00  11.41 ? 20  PHE A CD2 1 
ATOM   161  C  CE1 . PHE A 1 20  ? 7.020   5.277   15.766  1.00  12.27 ? 20  PHE A CE1 1 
ATOM   162  C  CE2 . PHE A 1 20  ? 7.695   3.026   15.154  1.00  12.71 ? 20  PHE A CE2 1 
ATOM   163  C  CZ  . PHE A 1 20  ? 7.354   4.319   14.778  1.00  12.29 ? 20  PHE A CZ  1 
ATOM   164  N  N   . PRO A 1 21  ? 9.782   3.803   21.760  1.00  12.09 ? 21  PRO A N   1 
ATOM   165  C  CA  . PRO A 1 21  ? 10.028  3.314   23.095  1.00  11.48 ? 21  PRO A CA  1 
ATOM   166  C  C   . PRO A 1 21  ? 8.814   3.176   24.032  1.00  12.21 ? 21  PRO A C   1 
ATOM   167  O  O   . PRO A 1 21  ? 8.844   2.407   24.973  1.00  11.56 ? 21  PRO A O   1 
ATOM   168  C  CB  . PRO A 1 21  ? 11.139  4.288   23.670  1.00  12.38 ? 21  PRO A CB  1 
ATOM   169  C  CG  . PRO A 1 21  ? 11.427  5.224   22.518  1.00  15.11 ? 21  PRO A CG  1 
ATOM   170  C  CD  . PRO A 1 21  ? 10.767  4.794   21.261  1.00  13.54 ? 21  PRO A CD  1 
ATOM   171  N  N   . ILE A 1 22  ? 7.740   3.942   23.700  1.00  10.71 ? 22  ILE A N   1 
ATOM   172  C  CA  . ILE A 1 22  ? 6.516   3.851   24.462  1.00  10.73 ? 22  ILE A CA  1 
ATOM   173  C  C   . ILE A 1 22  ? 5.920   2.456   24.322  1.00  9.45  ? 22  ILE A C   1 
ATOM   174  O  O   . ILE A 1 22  ? 5.020   2.125   25.081  1.00  8.50  ? 22  ILE A O   1 
ATOM   175  C  CB  . ILE A 1 22  ? 5.546   4.966   23.980  1.00  9.57  ? 22  ILE A CB  1 
ATOM   176  C  CG1 . ILE A 1 22  ? 4.509   5.258   25.018  1.00  12.20 ? 22  ILE A CG1 1 
ATOM   177  C  CG2 . ILE A 1 22  ? 4.868   4.539   22.672  1.00  10.21 ? 22  ILE A CG2 1 
ATOM   178  C  CD1 . ILE A 1 22  ? 3.546   6.322   24.507  1.00  14.89 ? 22  ILE A CD1 1 
ATOM   179  N  N   . ALA A 1 23  ? 6.458   1.649   23.417  1.00  9.53  ? 23  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 23  ? 5.992   0.232   23.327  1.00  9.21  ? 23  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 23  ? 6.073   -0.469  24.668  1.00  9.82  ? 23  ALA A C   1 
ATOM   182  O  O   . ALA A 1 23  ? 5.395   -1.499  24.867  1.00  9.72  ? 23  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 23  ? 6.844   -0.593  22.280  1.00  9.59  ? 23  ALA A CB  1 
ATOM   184  N  N   . LYS A 1 24  ? 6.967   -0.046  25.586  1.00  11.20 ? 24  LYS A N   1 
ATOM   185  C  CA  . LYS A 1 24  ? 7.132   -0.734  26.872  1.00  11.78 ? 24  LYS A CA  1 
ATOM   186  C  C   . LYS A 1 24  ? 6.581   0.171   27.929  1.00  13.67 ? 24  LYS A C   1 
ATOM   187  O  O   . LYS A 1 24  ? 6.946   0.090   29.103  1.00  14.80 ? 24  LYS A O   1 
ATOM   188  C  CB  . LYS A 1 24  ? 8.655   -1.000  27.164  1.00  12.50 ? 24  LYS A CB  1 
ATOM   189  C  CG  . LYS A 1 24  ? 9.267   -1.976  26.202  1.00  15.45 ? 24  LYS A CG  1 
ATOM   190  C  CD  . LYS A 1 24  ? 10.778  -2.029  26.534  1.00  17.84 ? 24  LYS A CD  1 
ATOM   191  C  CE  . LYS A 1 24  ? 11.458  -3.007  25.580  1.00  19.74 ? 24  LYS A CE  1 
ATOM   192  N  NZ  . LYS A 1 24  ? 11.195  -4.408  26.051  1.00  23.51 ? 24  LYS A NZ  1 
ATOM   193  N  N   . GLY A 1 25  ? 5.557   0.980   27.570  1.00  11.98 ? 25  GLY A N   1 
ATOM   194  C  CA  . GLY A 1 25  ? 4.983   1.962   28.489  1.00  12.70 ? 25  GLY A CA  1 
ATOM   195  C  C   . GLY A 1 25  ? 4.023   1.398   29.511  1.00  10.49 ? 25  GLY A C   1 
ATOM   196  O  O   . GLY A 1 25  ? 3.805   0.177   29.630  1.00  14.12 ? 25  GLY A O   1 
ATOM   197  N  N   . GLU A 1 26  ? 3.372   2.299   30.271  1.00  12.01 ? 26  GLU A N   1 
ATOM   198  C  CA  . GLU A 1 26  ? 2.490   1.908   31.316  1.00  13.42 ? 26  GLU A CA  1 
ATOM   199  C  C   . GLU A 1 26  ? 1.055   1.633   30.951  1.00  10.77 ? 26  GLU A C   1 
ATOM   200  O  O   . GLU A 1 26  ? 0.313   1.112   31.808  1.00  11.01 ? 26  GLU A O   1 
ATOM   201  C  CB  . GLU A 1 26  ? 2.471   3.033   32.395  1.00  16.46 ? 26  GLU A CB  1 
ATOM   202  C  CG  . GLU A 1 26  ? 3.849   3.351   33.018  1.00  21.07 ? 26  GLU A CG  1 
ATOM   203  C  CD  . GLU A 1 26  ? 4.495   2.074   33.617  1.00  26.61 ? 26  GLU A CD  1 
ATOM   204  O  OE1 . GLU A 1 26  ? 3.869   1.360   34.472  1.00  30.62 ? 26  GLU A OE1 1 
ATOM   205  O  OE2 . GLU A 1 26  ? 5.633   1.739   33.186  1.00  30.02 ? 26  GLU A OE2 1 
ATOM   206  N  N   . ARG A 1 27  ? 0.622   1.972   29.712  1.00  9.84  ? 27  ARG A N   1 
ATOM   207  C  CA  . ARG A 1 27  ? -0.815  1.701   29.389  1.00  8.48  ? 27  ARG A CA  1 
ATOM   208  C  C   . ARG A 1 27  ? -0.892  1.242   27.900  1.00  7.59  ? 27  ARG A C   1 
ATOM   209  O  O   . ARG A 1 27  ? -1.603  1.852   27.075  1.00  6.46  ? 27  ARG A O   1 
ATOM   210  C  CB  . ARG A 1 27  ? -1.721  2.940   29.700  1.00  10.12 ? 27  ARG A CB  1 
ATOM   211  C  CG  . ARG A 1 27  ? -1.387  4.221   29.018  1.00  11.56 ? 27  ARG A CG  1 
ATOM   212  C  CD  . ARG A 1 27  ? -2.402  5.386   29.299  1.00  15.51 ? 27  ARG A CD  1 
ATOM   213  N  NE  . ARG A 1 27  ? -3.569  5.290   28.417  1.00  15.24 ? 27  ARG A NE  1 
ATOM   214  C  CZ  . ARG A 1 27  ? -4.470  6.254   28.249  1.00  12.81 ? 27  ARG A CZ  1 
ATOM   215  N  NH1 . ARG A 1 27  ? -4.359  7.397   28.901  1.00  11.81 ? 27  ARG A NH1 1 
ATOM   216  N  NH2 . ARG A 1 27  ? -5.492  6.065   27.421  1.00  12.49 ? 27  ARG A NH2 1 
ATOM   217  N  N   . GLN A 1 28  ? -0.146  0.173   27.578  1.00  7.34  ? 28  GLN A N   1 
ATOM   218  C  CA  . GLN A 1 28  ? -0.109  -0.340  26.214  1.00  6.88  ? 28  GLN A CA  1 
ATOM   219  C  C   . GLN A 1 28  ? -1.261  -1.341  25.964  1.00  6.41  ? 28  GLN A C   1 
ATOM   220  O  O   . GLN A 1 28  ? -1.782  -2.003  26.890  1.00  6.68  ? 28  GLN A O   1 
ATOM   221  C  CB  . GLN A 1 28  ? 1.236   -1.027  25.998  1.00  7.35  ? 28  GLN A CB  1 
ATOM   222  C  CG  . GLN A 1 28  ? 2.353   0.025   25.917  1.00  6.28  ? 28  GLN A CG  1 
ATOM   223  C  CD  . GLN A 1 28  ? 2.209   0.837   24.576  1.00  6.42  ? 28  GLN A CD  1 
ATOM   224  O  OE1 . GLN A 1 28  ? 2.450   0.315   23.502  1.00  6.41  ? 28  GLN A OE1 1 
ATOM   225  N  NE2 . GLN A 1 28  ? 1.880   2.146   24.677  1.00  5.64  ? 28  GLN A NE2 1 
ATOM   226  N  N   . SER A 1 29  ? -1.653  -1.408  24.692  1.00  5.46  ? 29  SER A N   1 
ATOM   227  C  CA  . SER A 1 29  ? -2.745  -2.300  24.257  1.00  5.31  ? 29  SER A CA  1 
ATOM   228  C  C   . SER A 1 29  ? -2.228  -3.149  23.123  1.00  5.19  ? 29  SER A C   1 
ATOM   229  O  O   . SER A 1 29  ? -1.247  -2.769  22.457  1.00  5.42  ? 29  SER A O   1 
ATOM   230  C  CB  . SER A 1 29  ? -3.836  -1.433  23.661  1.00  4.88  ? 29  SER A CB  1 
ATOM   231  O  OG  . SER A 1 29  ? -4.497  -0.763  24.780  1.00  4.93  ? 29  SER A OG  1 
ATOM   232  N  N   . PRO A 1 30  ? -2.824  -4.289  22.852  1.00  5.02  ? 30  PRO A N   1 
ATOM   233  C  CA  . PRO A 1 30  ? -3.997  -4.818  23.589  1.00  5.54  ? 30  PRO A CA  1 
ATOM   234  C  C   . PRO A 1 30  ? -3.588  -5.479  24.870  1.00  5.75  ? 30  PRO A C   1 
ATOM   235  O  O   . PRO A 1 30  ? -2.367  -5.524  25.192  1.00  6.67  ? 30  PRO A O   1 
ATOM   236  C  CB  . PRO A 1 30  ? -4.525  -5.874  22.592  1.00  5.35  ? 30  PRO A CB  1 
ATOM   237  C  CG  . PRO A 1 30  ? -3.221  -6.464  21.986  1.00  5.79  ? 30  PRO A CG  1 
ATOM   238  C  CD  . PRO A 1 30  ? -2.351  -5.224  21.799  1.00  6.16  ? 30  PRO A CD  1 
ATOM   239  N  N   . VAL A 1 31  ? -4.562  -6.070  25.552  1.00  5.91  ? 31  VAL A N   1 
ATOM   240  C  CA  . VAL A 1 31  ? -4.379  -6.842  26.777  1.00  5.98  ? 31  VAL A CA  1 
ATOM   241  C  C   . VAL A 1 31  ? -5.258  -8.062  26.740  1.00  6.29  ? 31  VAL A C   1 
ATOM   242  O  O   . VAL A 1 31  ? -6.242  -8.142  25.992  1.00  6.15  ? 31  VAL A O   1 
ATOM   243  C  CB  . VAL A 1 31  ? -4.696  -6.000  28.072  1.00  6.44  ? 31  VAL A CB  1 
ATOM   244  C  CG1 . VAL A 1 31  ? -3.782  -4.772  28.160  1.00  7.01  ? 31  VAL A CG1 1 
ATOM   245  C  CG2 . VAL A 1 31  ? -6.172  -5.583  28.095  1.00  7.79  ? 31  VAL A CG2 1 
ATOM   246  N  N   . ASP A 1 32  ? -4.939  -9.049  27.595  1.00  6.51  ? 32  ASP A N   1 
ATOM   247  C  CA  . ASP A 1 32  ? -5.843  -10.125 27.872  1.00  7.04  ? 32  ASP A CA  1 
ATOM   248  C  C   . ASP A 1 32  ? -6.915  -9.628  28.839  1.00  7.20  ? 32  ASP A C   1 
ATOM   249  O  O   . ASP A 1 32  ? -6.575  -8.996  29.841  1.00  8.52  ? 32  ASP A O   1 
ATOM   250  C  CB  . ASP A 1 32  ? -5.076  -11.308 28.468  1.00  8.58  ? 32  ASP A CB  1 
ATOM   251  C  CG  . ASP A 1 32  ? -5.996  -12.482 28.785  1.00  10.32 ? 32  ASP A CG  1 
ATOM   252  O  OD1 . ASP A 1 32  ? -6.757  -12.922 27.903  1.00  9.07  ? 32  ASP A OD1 1 
ATOM   253  O  OD2 . ASP A 1 32  ? -6.086  -12.906 29.987  1.00  12.36 ? 32  ASP A OD2 1 
ATOM   254  N  N   . ILE A 1 33  ? -8.163  -9.938  28.555  1.00  7.72  ? 33  ILE A N   1 
ATOM   255  C  CA  . ILE A 1 33  ? -9.274  -9.535  29.419  1.00  7.93  ? 33  ILE A CA  1 
ATOM   256  C  C   . ILE A 1 33  ? -9.605  -10.779 30.226  1.00  9.07  ? 33  ILE A C   1 
ATOM   257  O  O   . ILE A 1 33  ? -10.127 -11.801 29.705  1.00  9.87  ? 33  ILE A O   1 
ATOM   258  C  CB  . ILE A 1 33  ? -10.471 -9.069  28.596  1.00  7.81  ? 33  ILE A CB  1 
ATOM   259  C  CG1 . ILE A 1 33  ? -10.094 -7.825  27.771  1.00  7.04  ? 33  ILE A CG1 1 
ATOM   260  C  CG2 . ILE A 1 33  ? -11.678 -8.825  29.552  1.00  9.78  ? 33  ILE A CG2 1 
ATOM   261  C  CD1 . ILE A 1 33  ? -11.190 -7.560  26.707  1.00  7.65  ? 33  ILE A CD1 1 
ATOM   262  N  N   A ASP A 1 34  ? -9.208  -10.700 31.509  0.50  10.88 ? 34  ASP A N   1 
ATOM   263  N  N   B ASP A 1 34  ? -9.244  -10.714 31.500  0.50  11.00 ? 34  ASP A N   1 
ATOM   264  C  CA  A ASP A 1 34  ? -9.522  -11.772 32.484  0.50  11.15 ? 34  ASP A CA  1 
ATOM   265  C  CA  B ASP A 1 34  ? -9.512  -11.870 32.339  0.50  11.17 ? 34  ASP A CA  1 
ATOM   266  C  C   A ASP A 1 34  ? -10.959 -11.490 32.949  0.50  11.16 ? 34  ASP A C   1 
ATOM   267  C  C   B ASP A 1 34  ? -10.871 -11.605 32.988  0.50  11.37 ? 34  ASP A C   1 
ATOM   268  O  O   A ASP A 1 34  ? -11.220 -10.501 33.621  0.50  11.29 ? 34  ASP A O   1 
ATOM   269  O  O   B ASP A 1 34  ? -10.965 -10.769 33.873  0.50  12.08 ? 34  ASP A O   1 
ATOM   270  C  CB  A ASP A 1 34  ? -8.513  -11.702 33.630  0.50  12.33 ? 34  ASP A CB  1 
ATOM   271  C  CB  B ASP A 1 34  ? -8.407  -11.970 33.359  0.50  12.17 ? 34  ASP A CB  1 
ATOM   272  C  CG  A ASP A 1 34  ? -8.673  -12.861 34.646  0.50  13.31 ? 34  ASP A CG  1 
ATOM   273  C  CG  B ASP A 1 34  ? -8.605  -13.141 34.279  0.50  13.84 ? 34  ASP A CG  1 
ATOM   274  O  OD1 A ASP A 1 34  ? -9.819  -13.300 34.879  0.50  12.65 ? 34  ASP A OD1 1 
ATOM   275  O  OD1 B ASP A 1 34  ? -8.191  -14.269 33.900  0.50  14.97 ? 34  ASP A OD1 1 
ATOM   276  O  OD2 A ASP A 1 34  ? -7.622  -13.337 35.195  0.50  15.27 ? 34  ASP A OD2 1 
ATOM   277  O  OD2 B ASP A 1 34  ? -9.149  -12.896 35.379  0.50  13.99 ? 34  ASP A OD2 1 
ATOM   278  N  N   . THR A 1 35  ? -11.886 -12.294 32.510  1.00  12.41 ? 35  THR A N   1 
ATOM   279  C  CA  . THR A 1 35  ? -13.294 -11.961 32.711  1.00  12.60 ? 35  THR A CA  1 
ATOM   280  C  C   . THR A 1 35  ? -13.682 -12.111 34.144  1.00  13.50 ? 35  THR A C   1 
ATOM   281  O  O   . THR A 1 35  ? -14.611 -11.423 34.593  1.00  15.76 ? 35  THR A O   1 
ATOM   282  C  CB  . THR A 1 35  ? -14.224 -12.870 31.926  1.00  14.81 ? 35  THR A CB  1 
ATOM   283  O  OG1 . THR A 1 35  ? -14.057 -14.209 32.415  1.00  15.55 ? 35  THR A OG1 1 
ATOM   284  C  CG2 . THR A 1 35  ? -13.992 -12.894 30.377  1.00  13.37 ? 35  THR A CG2 1 
ATOM   285  N  N   . HIS A 1 36  ? -12.949 -12.959 34.863  1.00  14.52 ? 36  HIS A N   1 
ATOM   286  C  CA  . HIS A 1 36  ? -13.275 -13.164 36.281  1.00  16.18 ? 36  HIS A CA  1 
ATOM   287  C  C   . HIS A 1 36  ? -12.806 -12.041 37.124  1.00  17.47 ? 36  HIS A C   1 
ATOM   288  O  O   . HIS A 1 36  ? -13.491 -11.754 38.139  1.00  20.25 ? 36  HIS A O   1 
ATOM   289  C  CB  . HIS A 1 36  ? -12.751 -14.569 36.668  1.00  17.84 ? 36  HIS A CB  1 
ATOM   290  C  CG  . HIS A 1 36  ? -13.718 -15.619 36.230  1.00  17.91 ? 36  HIS A CG  1 
ATOM   291  N  ND1 . HIS A 1 36  ? -13.470 -16.555 35.267  1.00  18.48 ? 36  HIS A ND1 1 
ATOM   292  C  CD2 . HIS A 1 36  ? -15.060 -15.737 36.560  1.00  18.46 ? 36  HIS A CD2 1 
ATOM   293  C  CE1 . HIS A 1 36  ? -14.603 -17.233 35.034  1.00  18.49 ? 36  HIS A CE1 1 
ATOM   294  N  NE2 . HIS A 1 36  ? -15.564 -16.752 35.832  1.00  25.38 ? 36  HIS A NE2 1 
ATOM   295  N  N   . THR A 1 37  ? -11.688 -11.364 36.772  1.00  17.44 ? 37  THR A N   1 
ATOM   296  C  CA  . THR A 1 37  ? -11.193 -10.245 37.523  1.00  18.55 ? 37  THR A CA  1 
ATOM   297  C  C   . THR A 1 37  ? -11.587 -8.828  37.026  1.00  15.58 ? 37  THR A C   1 
ATOM   298  O  O   . THR A 1 37  ? -11.232 -7.817  37.675  1.00  19.05 ? 37  THR A O   1 
ATOM   299  C  CB  . THR A 1 37  ? -9.694  -10.294 37.781  1.00  21.00 ? 37  THR A CB  1 
ATOM   300  O  OG1 . THR A 1 37  ? -8.978  -10.304 36.558  1.00  25.65 ? 37  THR A OG1 1 
ATOM   301  C  CG2 . THR A 1 37  ? -9.291  -11.570 38.443  1.00  22.87 ? 37  THR A CG2 1 
ATOM   302  N  N   . ALA A 1 38  ? -12.308 -8.779  35.899  1.00  14.97 ? 38  ALA A N   1 
ATOM   303  C  CA  . ALA A 1 38  ? -12.902 -7.528  35.428  1.00  13.62 ? 38  ALA A CA  1 
ATOM   304  C  C   . ALA A 1 38  ? -13.909 -7.096  36.500  1.00  14.80 ? 38  ALA A C   1 
ATOM   305  O  O   . ALA A 1 38  ? -14.671 -7.940  37.041  1.00  18.98 ? 38  ALA A O   1 
ATOM   306  C  CB  . ALA A 1 38  ? -13.592 -7.704  34.080  1.00  15.31 ? 38  ALA A CB  1 
ATOM   307  N  N   . LYS A 1 39  ? -13.871 -5.834  36.836  1.00  14.28 ? 39  LYS A N   1 
ATOM   308  C  CA  . LYS A 1 39  ? -14.766 -5.288  37.900  1.00  15.43 ? 39  LYS A CA  1 
ATOM   309  C  C   . LYS A 1 39  ? -16.099 -4.818  37.237  1.00  14.90 ? 39  LYS A C   1 
ATOM   310  O  O   . LYS A 1 39  ? -16.111 -3.853  36.471  1.00  12.16 ? 39  LYS A O   1 
ATOM   311  C  CB  . LYS A 1 39  ? -14.024 -4.114  38.553  1.00  18.35 ? 39  LYS A CB  1 
ATOM   312  C  CG  . LYS A 1 39  ? -14.840 -3.221  39.522  1.00  21.14 ? 39  LYS A CG  1 
ATOM   313  C  CD  . LYS A 1 39  ? -14.887 -3.859  40.902  1.00  18.99 ? 39  LYS A CD  1 
ATOM   314  C  CE  . LYS A 1 39  ? -15.673 -2.953  41.840  1.00  22.40 ? 39  LYS A CE  1 
ATOM   315  N  NZ  . LYS A 1 39  ? -16.195 -3.821  42.924  1.00  26.87 ? 39  LYS A NZ  1 
ATOM   316  N  N   . TYR A 1 40  ? -17.226 -5.388  37.636  1.00  15.79 ? 40  TYR A N   1 
ATOM   317  C  CA  . TYR A 1 40  ? -18.506 -4.775  37.264  1.00  15.47 ? 40  TYR A CA  1 
ATOM   318  C  C   . TYR A 1 40  ? -18.648 -3.367  37.845  1.00  15.20 ? 40  TYR A C   1 
ATOM   319  O  O   . TYR A 1 40  ? -18.456 -3.155  39.083  1.00  16.20 ? 40  TYR A O   1 
ATOM   320  C  CB  . TYR A 1 40  ? -19.667 -5.721  37.637  1.00  18.72 ? 40  TYR A CB  1 
ATOM   321  C  CG  . TYR A 1 40  ? -21.018 -5.073  37.479  1.00  21.87 ? 40  TYR A CG  1 
ATOM   322  C  CD1 . TYR A 1 40  ? -21.503 -4.705  36.226  1.00  21.55 ? 40  TYR A CD1 1 
ATOM   323  C  CD2 . TYR A 1 40  ? -21.823 -4.812  38.601  1.00  27.66 ? 40  TYR A CD2 1 
ATOM   324  C  CE1 . TYR A 1 40  ? -22.726 -4.104  36.050  1.00  23.14 ? 40  TYR A CE1 1 
ATOM   325  C  CE2 . TYR A 1 40  ? -23.062 -4.169  38.439  1.00  27.07 ? 40  TYR A CE2 1 
ATOM   326  C  CZ  . TYR A 1 40  ? -23.501 -3.834  37.165  1.00  26.78 ? 40  TYR A CZ  1 
ATOM   327  O  OH  . TYR A 1 40  ? -24.708 -3.225  36.974  1.00  30.61 ? 40  TYR A OH  1 
ATOM   328  N  N   . ASP A 1 41  ? -18.991 -2.390  36.999  1.00  14.41 ? 41  ASP A N   1 
ATOM   329  C  CA  . ASP A 1 41  ? -19.139 -1.006  37.483  1.00  17.14 ? 41  ASP A CA  1 
ATOM   330  C  C   . ASP A 1 41  ? -20.581 -0.605  37.207  1.00  22.05 ? 41  ASP A C   1 
ATOM   331  O  O   . ASP A 1 41  ? -20.948 -0.299  36.073  1.00  18.19 ? 41  ASP A O   1 
ATOM   332  C  CB  . ASP A 1 41  ? -18.136 -0.064  36.867  1.00  20.76 ? 41  ASP A CB  1 
ATOM   333  C  CG  . ASP A 1 41  ? -18.302 1.364   37.394  1.00  26.49 ? 41  ASP A CG  1 
ATOM   334  O  OD1 . ASP A 1 41  ? -19.274 1.614   38.133  1.00  26.86 ? 41  ASP A OD1 1 
ATOM   335  O  OD2 . ASP A 1 41  ? -17.466 2.196   37.053  1.00  28.06 ? 41  ASP A OD2 1 
ATOM   336  N  N   . PRO A 1 42  ? -21.441 -0.672  38.245  1.00  24.48 ? 42  PRO A N   1 
ATOM   337  C  CA  . PRO A 1 42  ? -22.865 -0.445  38.004  1.00  24.05 ? 42  PRO A CA  1 
ATOM   338  C  C   . PRO A 1 42  ? -23.140 0.991   37.581  1.00  25.24 ? 42  PRO A C   1 
ATOM   339  O  O   . PRO A 1 42  ? -24.222 1.252   37.037  1.00  29.97 ? 42  PRO A O   1 
ATOM   340  C  CB  . PRO A 1 42  ? -23.489 -0.754  39.402  1.00  25.45 ? 42  PRO A CB  1 
ATOM   341  C  CG  . PRO A 1 42  ? -22.395 -0.329  40.352  1.00  27.13 ? 42  PRO A CG  1 
ATOM   342  C  CD  . PRO A 1 42  ? -21.163 -0.926  39.682  1.00  26.54 ? 42  PRO A CD  1 
ATOM   343  N  N   . SER A 1 43  ? -22.178 1.898   37.759  1.00  24.41 ? 43  SER A N   1 
ATOM   344  C  CA  . SER A 1 43  ? -22.361 3.272   37.271  1.00  27.45 ? 43  SER A CA  1 
ATOM   345  C  C   . SER A 1 43  ? -21.844 3.545   35.810  1.00  27.05 ? 43  SER A C   1 
ATOM   346  O  O   . SER A 1 43  ? -21.940 4.694   35.293  1.00  29.82 ? 43  SER A O   1 
ATOM   347  C  CB  . SER A 1 43  ? -21.718 4.266   38.230  1.00  31.21 ? 43  SER A CB  1 
ATOM   348  O  OG  . SER A 1 43  ? -20.353 4.449   37.893  1.00  30.55 ? 43  SER A OG  1 
ATOM   349  N  N   . LEU A 1 44  ? -21.288 2.521   35.134  1.00  24.71 ? 44  LEU A N   1 
ATOM   350  C  CA  . LEU A 1 44  ? -21.036 2.699   33.695  1.00  20.72 ? 44  LEU A CA  1 
ATOM   351  C  C   . LEU A 1 44  ? -22.374 2.787   32.967  1.00  21.91 ? 44  LEU A C   1 
ATOM   352  O  O   . LEU A 1 44  ? -23.295 2.033   33.243  1.00  23.77 ? 44  LEU A O   1 
ATOM   353  C  CB  . LEU A 1 44  ? -20.281 1.487   33.147  1.00  17.70 ? 44  LEU A CB  1 
ATOM   354  C  CG  . LEU A 1 44  ? -18.812 1.449   33.480  1.00  16.13 ? 44  LEU A CG  1 
ATOM   355  C  CD1 . LEU A 1 44  ? -18.291 0.054   33.087  1.00  14.70 ? 44  LEU A CD1 1 
ATOM   356  C  CD2 . LEU A 1 44  ? -18.079 2.603   32.788  1.00  16.60 ? 44  LEU A CD2 1 
ATOM   357  N  N   . LYS A 1 45  ? -22.463 3.697   32.006  1.00  19.93 ? 45  LYS A N   1 
ATOM   358  C  CA  . LYS A 1 45  ? -23.729 3.880   31.235  1.00  19.66 ? 45  LYS A CA  1 
ATOM   359  C  C   . LYS A 1 45  ? -23.765 2.996   30.016  1.00  19.23 ? 45  LYS A C   1 
ATOM   360  O  O   . LYS A 1 45  ? -22.683 2.492   29.578  1.00  18.82 ? 45  LYS A O   1 
ATOM   361  C  CB  . LYS A 1 45  ? -23.739 5.271   30.669  1.00  21.32 ? 45  LYS A CB  1 
ATOM   362  C  CG  . LYS A 1 45  ? -23.397 6.361   31.660  1.00  26.37 ? 45  LYS A CG  1 
ATOM   363  C  CD  . LYS A 1 45  ? -24.687 7.005   32.127  1.00  34.35 ? 45  LYS A CD  1 
ATOM   364  C  CE  . LYS A 1 45  ? -24.501 8.518   32.207  1.00  37.98 ? 45  LYS A CE  1 
ATOM   365  N  NZ  . LYS A 1 45  ? -23.550 8.899   33.295  1.00  36.88 ? 45  LYS A NZ  1 
ATOM   366  N  N   . PRO A 1 46  ? -24.966 2.793   29.416  1.00  16.54 ? 46  PRO A N   1 
ATOM   367  C  CA  . PRO A 1 46  ? -25.047 2.112   28.131  1.00  15.93 ? 46  PRO A CA  1 
ATOM   368  C  C   . PRO A 1 46  ? -24.202 2.919   27.128  1.00  12.79 ? 46  PRO A C   1 
ATOM   369  O  O   . PRO A 1 46  ? -24.160 4.156   27.185  1.00  12.66 ? 46  PRO A O   1 
ATOM   370  C  CB  . PRO A 1 46  ? -26.549 2.177   27.771  1.00  15.22 ? 46  PRO A CB  1 
ATOM   371  C  CG  . PRO A 1 46  ? -27.242 2.344   29.086  1.00  18.35 ? 46  PRO A CG  1 
ATOM   372  C  CD  . PRO A 1 46  ? -26.307 3.133   29.975  1.00  17.52 ? 46  PRO A CD  1 
ATOM   373  N  N   . LEU A 1 47  ? -23.550 2.198   26.181  1.00  14.12 ? 47  LEU A N   1 
ATOM   374  C  CA  . LEU A 1 47  ? -22.806 2.836   25.145  1.00  14.21 ? 47  LEU A CA  1 
ATOM   375  C  C   . LEU A 1 47  ? -23.824 3.405   24.162  1.00  17.45 ? 47  LEU A C   1 
ATOM   376  O  O   . LEU A 1 47  ? -24.864 2.753   23.891  1.00  18.86 ? 47  LEU A O   1 
ATOM   377  C  CB  . LEU A 1 47  ? -21.942 1.775   24.488  1.00  16.05 ? 47  LEU A CB  1 
ATOM   378  C  CG  . LEU A 1 47  ? -21.001 2.223   23.436  1.00  16.13 ? 47  LEU A CG  1 
ATOM   379  C  CD1 . LEU A 1 47  ? -19.937 3.128   24.097  1.00  16.25 ? 47  LEU A CD1 1 
ATOM   380  C  CD2 . LEU A 1 47  ? -20.392 0.908   22.937  1.00  17.33 ? 47  LEU A CD2 1 
ATOM   381  N  N   . SER A 1 48  ? -23.576 4.597   23.663  1.00  13.83 ? 48  SER A N   1 
ATOM   382  C  CA  . SER A 1 48  ? -24.413 5.211   22.652  1.00  13.88 ? 48  SER A CA  1 
ATOM   383  C  C   . SER A 1 48  ? -23.649 5.262   21.339  1.00  14.02 ? 48  SER A C   1 
ATOM   384  O  O   . SER A 1 48  ? -22.645 5.984   21.167  1.00  13.50 ? 48  SER A O   1 
ATOM   385  C  CB  . SER A 1 48  ? -24.788 6.643   23.092  1.00  14.50 ? 48  SER A CB  1 
ATOM   386  O  OG  . SER A 1 48  ? -25.422 7.400   22.059  1.00  19.24 ? 48  SER A OG  1 
ATOM   387  N  N   . VAL A 1 49  ? -24.140 4.522   20.406  1.00  15.18 ? 49  VAL A N   1 
ATOM   388  C  CA  . VAL A 1 49  ? -23.585 4.382   19.082  1.00  16.49 ? 49  VAL A CA  1 
ATOM   389  C  C   . VAL A 1 49  ? -24.558 5.029   18.117  1.00  20.41 ? 49  VAL A C   1 
ATOM   390  O  O   . VAL A 1 49  ? -25.610 4.462   17.797  1.00  20.56 ? 49  VAL A O   1 
ATOM   391  C  CB  . VAL A 1 49  ? -23.408 2.895   18.732  1.00  19.51 ? 49  VAL A CB  1 
ATOM   392  C  CG1 . VAL A 1 49  ? -22.833 2.759   17.320  1.00  24.80 ? 49  VAL A CG1 1 
ATOM   393  C  CG2 . VAL A 1 49  ? -22.504 2.204   19.769  1.00  19.09 ? 49  VAL A CG2 1 
ATOM   394  N  N   . SER A 1 50  ? -24.234 6.193   17.608  1.00  16.94 ? 50  SER A N   1 
ATOM   395  C  CA  . SER A 1 50  ? -25.105 6.877   16.692  1.00  17.27 ? 50  SER A CA  1 
ATOM   396  C  C   . SER A 1 50  ? -24.497 6.988   15.353  1.00  16.94 ? 50  SER A C   1 
ATOM   397  O  O   . SER A 1 50  ? -23.836 7.947   15.012  1.00  16.85 ? 50  SER A O   1 
ATOM   398  C  CB  . SER A 1 50  ? -25.530 8.257   17.213  1.00  18.38 ? 50  SER A CB  1 
ATOM   399  O  OG  . SER A 1 50  ? -26.136 8.194   18.457  1.00  26.57 ? 50  SER A OG  1 
ATOM   400  N  N   . TYR A 1 51  ? -24.773 5.982   14.542  1.00  15.71 ? 51  TYR A N   1 
ATOM   401  C  CA  . TYR A 1 51  ? -24.215 5.817   13.215  1.00  14.71 ? 51  TYR A CA  1 
ATOM   402  C  C   . TYR A 1 51  ? -25.216 6.031   12.050  1.00  16.18 ? 51  TYR A C   1 
ATOM   403  O  O   . TYR A 1 51  ? -24.805 5.870   10.894  1.00  15.72 ? 51  TYR A O   1 
ATOM   404  C  CB  . TYR A 1 51  ? -23.590 4.426   13.094  1.00  14.71 ? 51  TYR A CB  1 
ATOM   405  C  CG  . TYR A 1 51  ? -22.260 4.157   13.844  1.00  12.74 ? 51  TYR A CG  1 
ATOM   406  C  CD1 . TYR A 1 51  ? -21.521 5.185   14.490  1.00  13.48 ? 51  TYR A CD1 1 
ATOM   407  C  CD2 . TYR A 1 51  ? -21.761 2.886   13.861  1.00  12.57 ? 51  TYR A CD2 1 
ATOM   408  C  CE1 . TYR A 1 51  ? -20.317 4.850   15.160  1.00  11.61 ? 51  TYR A CE1 1 
ATOM   409  C  CE2 . TYR A 1 51  ? -20.593 2.539   14.501  1.00  12.37 ? 51  TYR A CE2 1 
ATOM   410  C  CZ  . TYR A 1 51  ? -19.855 3.574   15.142  1.00  11.63 ? 51  TYR A CZ  1 
ATOM   411  O  OH  . TYR A 1 51  ? -18.709 3.206   15.797  1.00  10.56 ? 51  TYR A OH  1 
ATOM   412  N  N   . ASP A 1 52  ? -26.448 6.472   12.373  1.00  19.74 ? 52  ASP A N   1 
ATOM   413  C  CA  . ASP A 1 52  ? -27.442 6.726   11.281  1.00  23.70 ? 52  ASP A CA  1 
ATOM   414  C  C   . ASP A 1 52  ? -26.963 7.649   10.150  1.00  22.43 ? 52  ASP A C   1 
ATOM   415  O  O   . ASP A 1 52  ? -27.201 7.386   8.961   1.00  23.69 ? 52  ASP A O   1 
ATOM   416  C  CB  . ASP A 1 52  ? -28.786 7.210   11.824  1.00  28.15 ? 52  ASP A CB  1 
ATOM   417  C  CG  . ASP A 1 52  ? -28.639 8.237   12.935  1.00  35.83 ? 52  ASP A CG  1 
ATOM   418  O  OD1 . ASP A 1 52  ? -28.109 7.896   14.048  1.00  47.34 ? 52  ASP A OD1 1 
ATOM   419  O  OD2 . ASP A 1 52  ? -29.061 9.400   12.706  1.00  45.25 ? 52  ASP A OD2 1 
ATOM   420  N  N   . GLN A 1 53  ? -26.180 8.653   10.500  1.00  22.11 ? 53  GLN A N   1 
ATOM   421  C  CA  . GLN A 1 53  ? -25.789 9.628   9.467   1.00  24.19 ? 53  GLN A CA  1 
ATOM   422  C  C   . GLN A 1 53  ? -24.379 9.439   8.926   1.00  21.43 ? 53  GLN A C   1 
ATOM   423  O  O   . GLN A 1 53  ? -23.826 10.336  8.323   1.00  20.98 ? 53  GLN A O   1 
ATOM   424  C  CB  . GLN A 1 53  ? -26.019 11.064  9.973   1.00  30.27 ? 53  GLN A CB  1 
ATOM   425  C  CG  . GLN A 1 53  ? -27.517 11.389  10.114  1.00  36.69 ? 53  GLN A CG  1 
ATOM   426  C  CD  . GLN A 1 53  ? -28.263 11.113  8.804   1.00  44.85 ? 53  GLN A CD  1 
ATOM   427  O  OE1 . GLN A 1 53  ? -27.797 11.499  7.704   1.00  52.01 ? 53  GLN A OE1 1 
ATOM   428  N  NE2 . GLN A 1 53  ? -29.401 10.417  8.898   1.00  47.23 ? 53  GLN A NE2 1 
ATOM   429  N  N   . ALA A 1 54  ? -23.809 8.240   9.108   1.00  18.01 ? 54  ALA A N   1 
ATOM   430  C  CA  . ALA A 1 54  ? -22.426 8.018   8.776   1.00  14.89 ? 54  ALA A CA  1 
ATOM   431  C  C   . ALA A 1 54  ? -22.212 8.196   7.292   1.00  16.90 ? 54  ALA A C   1 
ATOM   432  O  O   . ALA A 1 54  ? -23.068 7.777   6.477   1.00  18.10 ? 54  ALA A O   1 
ATOM   433  C  CB  . ALA A 1 54  ? -21.946 6.603   9.200   1.00  16.16 ? 54  ALA A CB  1 
ATOM   434  N  N   . THR A 1 55  ? -21.111 8.815   6.944   1.00  13.68 ? 55  THR A N   1 
ATOM   435  C  CA  . THR A 1 55  ? -20.649 8.984   5.568   1.00  13.43 ? 55  THR A CA  1 
ATOM   436  C  C   . THR A 1 55  ? -19.313 8.368   5.274   1.00  12.74 ? 55  THR A C   1 
ATOM   437  O  O   . THR A 1 55  ? -18.268 8.925   5.593   1.00  11.59 ? 55  THR A O   1 
ATOM   438  C  CB  . THR A 1 55  ? -20.546 10.530  5.210   1.00  13.73 ? 55  THR A CB  1 
ATOM   439  O  OG1 . THR A 1 55  ? -21.849 11.069  5.233   1.00  19.04 ? 55  THR A OG1 1 
ATOM   440  C  CG2 . THR A 1 55  ? -19.990 10.648  3.737   1.00  15.48 ? 55  THR A CG2 1 
ATOM   441  N  N   . SER A 1 56  ? -19.293 7.108   4.763   1.00  12.13 ? 56  SER A N   1 
ATOM   442  C  CA  . SER A 1 56  ? -18.075 6.507   4.384   1.00  14.26 ? 56  SER A CA  1 
ATOM   443  C  C   . SER A 1 56  ? -17.576 7.183   3.106   1.00  14.68 ? 56  SER A C   1 
ATOM   444  O  O   . SER A 1 56  ? -18.444 7.659   2.306   1.00  15.75 ? 56  SER A O   1 
ATOM   445  C  CB  . SER A 1 56  ? -18.163 4.956   4.178   1.00  13.95 ? 56  SER A CB  1 
ATOM   446  O  OG  . SER A 1 56  ? -19.138 4.635   3.130   1.00  14.40 ? 56  SER A OG  1 
ATOM   447  N  N   . LEU A 1 57  ? -16.280 7.194   2.879   1.00  14.27 ? 57  LEU A N   1 
ATOM   448  C  CA  . LEU A 1 57  ? -15.737 7.826   1.711   1.00  15.98 ? 57  LEU A CA  1 
ATOM   449  C  C   . LEU A 1 57  ? -14.909 6.903   0.897   1.00  16.50 ? 57  LEU A C   1 
ATOM   450  O  O   . LEU A 1 57  ? -14.957 6.957   -0.367  1.00  15.40 ? 57  LEU A O   1 
ATOM   451  C  CB  . LEU A 1 57  ? -14.882 9.009   2.127   1.00  19.03 ? 57  LEU A CB  1 
ATOM   452  C  CG  . LEU A 1 57  ? -15.637 10.195  2.727   1.00  21.67 ? 57  LEU A CG  1 
ATOM   453  C  CD1 . LEU A 1 57  ? -14.589 11.203  3.126   1.00  21.04 ? 57  LEU A CD1 1 
ATOM   454  C  CD2 . LEU A 1 57  ? -16.699 10.795  1.756   1.00  22.92 ? 57  LEU A CD2 1 
ATOM   455  N  N   . ARG A 1 58  ? -13.973 6.188   1.536   1.00  14.35 ? 58  ARG A N   1 
ATOM   456  C  CA  . ARG A 1 58  ? -12.941 5.526   0.802   1.00  13.77 ? 58  ARG A CA  1 
ATOM   457  C  C   . ARG A 1 58  ? -12.538 4.317   1.620   1.00  14.28 ? 58  ARG A C   1 
ATOM   458  O  O   . ARG A 1 58  ? -12.767 4.310   2.838   1.00  12.37 ? 58  ARG A O   1 
ATOM   459  C  CB  . ARG A 1 58  ? -11.747 6.474   0.652   1.00  16.33 ? 58  ARG A CB  1 
ATOM   460  C  CG  . ARG A 1 58  ? -10.788 6.204   -0.440  1.00  19.97 ? 58  ARG A CG  1 
ATOM   461  C  CD  . ARG A 1 58  ? -9.932  7.473   -0.543  1.00  20.58 ? 58  ARG A CD  1 
ATOM   462  N  NE  . ARG A 1 58  ? -9.127  7.412   0.671   1.00  18.94 ? 58  ARG A NE  1 
ATOM   463  C  CZ  . ARG A 1 58  ? -7.805  7.505   0.668   1.00  19.58 ? 58  ARG A CZ  1 
ATOM   464  N  NH1 . ARG A 1 58  ? -7.186  7.775   -0.463  1.00  19.79 ? 58  ARG A NH1 1 
ATOM   465  N  NH2 . ARG A 1 58  ? -7.154  7.460   1.843   1.00  20.33 ? 58  ARG A NH2 1 
ATOM   466  N  N   . ILE A 1 59  ? -11.905 3.389   0.937   1.00  12.61 ? 59  ILE A N   1 
ATOM   467  C  CA  . ILE A 1 59  ? -11.261 2.240   1.550   1.00  13.50 ? 59  ILE A CA  1 
ATOM   468  C  C   . ILE A 1 59  ? -9.850  2.223   1.065   1.00  13.29 ? 59  ILE A C   1 
ATOM   469  O  O   . ILE A 1 59  ? -9.533  2.378   -0.152  1.00  14.30 ? 59  ILE A O   1 
ATOM   470  C  CB  . ILE A 1 59  ? -12.004 0.924   1.258   1.00  11.71 ? 59  ILE A CB  1 
ATOM   471  C  CG1 . ILE A 1 59  ? -11.386 -0.207  2.126   1.00  13.21 ? 59  ILE A CG1 1 
ATOM   472  C  CG2 . ILE A 1 59  ? -11.892 0.517   -0.256  1.00  12.93 ? 59  ILE A CG2 1 
ATOM   473  C  CD1 . ILE A 1 59  ? -12.257 -1.498  2.002   1.00  13.10 ? 59  ILE A CD1 1 
ATOM   474  N  N   . LEU A 1 60  ? -8.885  2.000   1.967   1.00  13.28 ? 60  LEU A N   1 
ATOM   475  C  CA  . LEU A 1 60  ? -7.497  2.116   1.699   1.00  12.34 ? 60  LEU A CA  1 
ATOM   476  C  C   . LEU A 1 60  ? -6.652  0.971   2.228   1.00  12.20 ? 60  LEU A C   1 
ATOM   477  O  O   . LEU A 1 60  ? -6.925  0.597   3.389   1.00  12.92 ? 60  LEU A O   1 
ATOM   478  C  CB  . LEU A 1 60  ? -6.977  3.438   2.462   1.00  14.35 ? 60  LEU A CB  1 
ATOM   479  C  CG  . LEU A 1 60  ? -5.499  3.666   2.357   1.00  14.28 ? 60  LEU A CG  1 
ATOM   480  C  CD1 . LEU A 1 60  ? -5.042  3.851   0.892   1.00  17.16 ? 60  LEU A CD1 1 
ATOM   481  C  CD2 . LEU A 1 60  ? -4.971  4.806   3.271   1.00  15.18 ? 60  LEU A CD2 1 
ATOM   482  N  N   . ASN A 1 61  ? -5.761  0.365   1.442   1.00  10.62 ? 61  ASN A N   1 
ATOM   483  C  CA  . ASN A 1 61  ? -4.760  -0.555  1.938   1.00  12.07 ? 61  ASN A CA  1 
ATOM   484  C  C   . ASN A 1 61  ? -3.557  0.286   2.321   1.00  14.84 ? 61  ASN A C   1 
ATOM   485  O  O   . ASN A 1 61  ? -2.859  0.844   1.454   1.00  16.06 ? 61  ASN A O   1 
ATOM   486  C  CB  . ASN A 1 61  ? -4.344  -1.623  0.878   1.00  11.80 ? 61  ASN A CB  1 
ATOM   487  C  CG  . ASN A 1 61  ? -3.325  -2.578  1.347   1.00  12.78 ? 61  ASN A CG  1 
ATOM   488  O  OD1 . ASN A 1 61  ? -2.453  -2.302  2.203   1.00  13.74 ? 61  ASN A OD1 1 
ATOM   489  N  ND2 . ASN A 1 61  ? -3.296  -3.770  0.692   1.00  13.34 ? 61  ASN A ND2 1 
ATOM   490  N  N   . ASN A 1 62  ? -3.251  0.359   3.611   1.00  13.35 ? 62  ASN A N   1 
ATOM   491  C  CA  . ASN A 1 62  ? -2.165  1.225   4.115   1.00  13.34 ? 62  ASN A CA  1 
ATOM   492  C  C   . ASN A 1 62  ? -0.881  0.419   4.316   1.00  14.25 ? 62  ASN A C   1 
ATOM   493  O  O   . ASN A 1 62  ? 0.127   0.925   4.921   1.00  18.41 ? 62  ASN A O   1 
ATOM   494  C  CB  . ASN A 1 62  ? -2.577  2.013   5.387   1.00  14.90 ? 62  ASN A CB  1 
ATOM   495  C  CG  . ASN A 1 62  ? -2.710  1.095   6.605   1.00  15.78 ? 62  ASN A CG  1 
ATOM   496  O  OD1 . ASN A 1 62  ? -2.486  -0.130  6.492   1.00  13.74 ? 62  ASN A OD1 1 
ATOM   497  N  ND2 . ASN A 1 62  ? -2.946  1.692   7.776   1.00  19.29 ? 62  ASN A ND2 1 
ATOM   498  N  N   . GLY A 1 63  ? -0.830  -0.833  3.821   1.00  13.60 ? 63  GLY A N   1 
ATOM   499  C  CA  . GLY A 1 63  ? 0.274   -1.681  4.050   1.00  12.35 ? 63  GLY A CA  1 
ATOM   500  C  C   . GLY A 1 63  ? 0.369   -2.480  5.368   1.00  11.92 ? 63  GLY A C   1 
ATOM   501  O  O   . GLY A 1 63  ? 1.258   -3.281  5.558   1.00  13.92 ? 63  GLY A O   1 
ATOM   502  N  N   . HIS A 1 64  ? -0.566  -2.176  6.252   1.00  11.74 ? 64  HIS A N   1 
ATOM   503  C  CA  . HIS A 1 64  ? -0.651  -2.891  7.569   1.00  12.79 ? 64  HIS A CA  1 
ATOM   504  C  C   . HIS A 1 64  ? -2.022  -3.485  7.723   1.00  13.66 ? 64  HIS A C   1 
ATOM   505  O  O   . HIS A 1 64  ? -2.159  -4.510  8.382   1.00  16.22 ? 64  HIS A O   1 
ATOM   506  C  CB  . HIS A 1 64  ? -0.381  -1.938  8.737   1.00  14.47 ? 64  HIS A CB  1 
ATOM   507  C  CG  . HIS A 1 64  ? 0.883   -1.157  8.555   1.00  17.15 ? 64  HIS A CG  1 
ATOM   508  N  ND1 . HIS A 1 64  ? 2.102   -1.752  8.664   1.00  17.94 ? 64  HIS A ND1 1 
ATOM   509  C  CD2 . HIS A 1 64  ? 1.108   0.186   8.263   1.00  19.77 ? 64  HIS A CD2 1 
ATOM   510  C  CE1 . HIS A 1 64  ? 3.075   -0.820  8.510   1.00  17.84 ? 64  HIS A CE1 1 
ATOM   511  N  NE2 . HIS A 1 64  ? 2.504   0.338   8.221   1.00  18.32 ? 64  HIS A NE2 1 
ATOM   512  N  N   . ALA A 1 65  ? -3.037  -2.869  7.164   1.00  11.88 ? 65  ALA A N   1 
ATOM   513  C  CA  . ALA A 1 65  ? -4.439  -3.341  7.251   1.00  10.02 ? 65  ALA A CA  1 
ATOM   514  C  C   . ALA A 1 65  ? -5.204  -2.630  6.127   1.00  10.08 ? 65  ALA A C   1 
ATOM   515  O  O   . ALA A 1 65  ? -4.549  -1.979  5.258   1.00  11.24 ? 65  ALA A O   1 
ATOM   516  C  CB  . ALA A 1 65  ? -5.020  -3.047  8.685   1.00  9.87  ? 65  ALA A CB  1 
ATOM   517  N  N   . PHE A 1 66  ? -6.501  -2.762  6.067   1.00  8.93  ? 66  PHE A N   1 
ATOM   518  C  CA  . PHE A 1 66  ? -7.323  -1.807  5.261   1.00  9.39  ? 66  PHE A CA  1 
ATOM   519  C  C   . PHE A 1 66  ? -8.143  -0.933  6.142   1.00  10.43 ? 66  PHE A C   1 
ATOM   520  O  O   . PHE A 1 66  ? -8.743  -1.391  7.128   1.00  9.74  ? 66  PHE A O   1 
ATOM   521  C  CB  . PHE A 1 66  ? -8.114  -2.525  4.109   1.00  9.66  ? 66  PHE A CB  1 
ATOM   522  C  CG  . PHE A 1 66  ? -9.160  -3.493  4.636   1.00  9.67  ? 66  PHE A CG  1 
ATOM   523  C  CD1 . PHE A 1 66  ? -10.410 -2.996  4.974   1.00  9.45  ? 66  PHE A CD1 1 
ATOM   524  C  CD2 . PHE A 1 66  ? -8.877  -4.877  4.844   1.00  10.47 ? 66  PHE A CD2 1 
ATOM   525  C  CE1 . PHE A 1 66  ? -11.390 -3.815  5.520   1.00  11.34 ? 66  PHE A CE1 1 
ATOM   526  C  CE2 . PHE A 1 66  ? -9.849  -5.673  5.423   1.00  10.24 ? 66  PHE A CE2 1 
ATOM   527  C  CZ  . PHE A 1 66  ? -11.097 -5.174  5.704   1.00  10.46 ? 66  PHE A CZ  1 
ATOM   528  N  N   . ASN A 1 67  ? -8.256  0.359   5.775   1.00  11.35 ? 67  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 67  ? -9.076  1.275   6.509   1.00  11.25 ? 67  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 67  ? -10.286 1.687   5.717   1.00  11.31 ? 67  ASN A C   1 
ATOM   531  O  O   . ASN A 1 67  ? -10.129 2.153   4.570   1.00  12.32 ? 67  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 67  ? -8.310  2.578   6.823   1.00  11.57 ? 67  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 67  ? -7.251  2.424   7.851   1.00  14.34 ? 67  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 67  ? -7.057  1.353   8.478   1.00  12.66 ? 67  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 67  ? -6.462  3.506   7.999   1.00  16.42 ? 67  ASN A ND2 1 
ATOM   536  N  N   . VAL A 1 68  ? -11.455 1.660   6.295   1.00  9.56  ? 68  VAL A N   1 
ATOM   537  C  CA  . VAL A 1 68  ? -12.683 2.265   5.733   1.00  9.87  ? 68  VAL A CA  1 
ATOM   538  C  C   . VAL A 1 68  ? -12.839 3.627   6.418   1.00  12.65 ? 68  VAL A C   1 
ATOM   539  O  O   . VAL A 1 68  ? -12.978 3.707   7.651   1.00  11.60 ? 68  VAL A O   1 
ATOM   540  C  CB  . VAL A 1 68  ? -13.924 1.420   5.914   1.00  11.53 ? 68  VAL A CB  1 
ATOM   541  C  CG1 . VAL A 1 68  ? -15.180 2.185   5.408   1.00  11.34 ? 68  VAL A CG1 1 
ATOM   542  C  CG2 . VAL A 1 68  ? -13.804 0.115   5.141   1.00  11.07 ? 68  VAL A CG2 1 
ATOM   543  N  N   . GLU A 1 69  ? -12.834 4.725   5.649   1.00  12.92 ? 69  GLU A N   1 
ATOM   544  C  CA  . GLU A 1 69  ? -12.632 6.100   6.173   1.00  13.97 ? 69  GLU A CA  1 
ATOM   545  C  C   . GLU A 1 69  ? -13.941 6.784   6.063   1.00  15.31 ? 69  GLU A C   1 
ATOM   546  O  O   . GLU A 1 69  ? -14.732 6.536   5.098   1.00  15.65 ? 69  GLU A O   1 
ATOM   547  C  CB  . GLU A 1 69  ? -11.704 6.832   5.287   1.00  14.82 ? 69  GLU A CB  1 
ATOM   548  C  CG  . GLU A 1 69  ? -10.305 6.401   5.430   1.00  16.71 ? 69  GLU A CG  1 
ATOM   549  C  CD  . GLU A 1 69  ? -9.531  6.800   4.218   1.00  22.79 ? 69  GLU A CD  1 
ATOM   550  O  OE1 . GLU A 1 69  ? -10.184 7.404   3.285   1.00  22.23 ? 69  GLU A OE1 1 
ATOM   551  O  OE2 . GLU A 1 69  ? -8.318  6.482   4.201   1.00  23.24 ? 69  GLU A OE2 1 
ATOM   552  N  N   . PHE A 1 70  ? -14.184 7.689   6.992   1.00  12.39 ? 70  PHE A N   1 
ATOM   553  C  CA  . PHE A 1 70  ? -15.434 8.387   7.098   1.00  12.93 ? 70  PHE A CA  1 
ATOM   554  C  C   . PHE A 1 70  ? -15.234 9.868   7.082   1.00  12.53 ? 70  PHE A C   1 
ATOM   555  O  O   . PHE A 1 70  ? -14.149 10.343  7.409   1.00  13.13 ? 70  PHE A O   1 
ATOM   556  C  CB  . PHE A 1 70  ? -16.158 7.988   8.356   1.00  11.33 ? 70  PHE A CB  1 
ATOM   557  C  CG  . PHE A 1 70  ? -16.715 6.584   8.262   1.00  11.93 ? 70  PHE A CG  1 
ATOM   558  C  CD1 . PHE A 1 70  ? -15.880 5.481   8.476   1.00  11.04 ? 70  PHE A CD1 1 
ATOM   559  C  CD2 . PHE A 1 70  ? -18.040 6.362   7.955   1.00  9.71  ? 70  PHE A CD2 1 
ATOM   560  C  CE1 . PHE A 1 70  ? -16.389 4.171   8.357   1.00  11.50 ? 70  PHE A CE1 1 
ATOM   561  C  CE2 . PHE A 1 70  ? -18.563 5.075   7.831   1.00  9.93  ? 70  PHE A CE2 1 
ATOM   562  C  CZ  . PHE A 1 70  ? -17.719 3.971   8.037   1.00  11.72 ? 70  PHE A CZ  1 
ATOM   563  N  N   A ASP A 1 71  ? -16.289 10.585  6.695   0.50  12.37 ? 71  ASP A N   1 
ATOM   564  N  N   B ASP A 1 71  ? -16.241 10.598  6.643   0.50  14.07 ? 71  ASP A N   1 
ATOM   565  C  CA  A ASP A 1 71  ? -16.259 12.046  6.806   0.50  12.63 ? 71  ASP A CA  1 
ATOM   566  C  CA  B ASP A 1 71  ? -16.068 12.032  6.726   0.50  14.98 ? 71  ASP A CA  1 
ATOM   567  C  C   A ASP A 1 71  ? -16.430 12.388  8.262   0.50  12.89 ? 71  ASP A C   1 
ATOM   568  C  C   B ASP A 1 71  ? -16.392 12.417  8.174   0.50  14.33 ? 71  ASP A C   1 
ATOM   569  O  O   A ASP A 1 71  ? -17.507 12.160  8.828   0.50  15.15 ? 71  ASP A O   1 
ATOM   570  O  O   B ASP A 1 71  ? -17.513 12.207  8.648   0.50  16.43 ? 71  ASP A O   1 
ATOM   571  C  CB  A ASP A 1 71  ? -17.455 12.573  6.039   0.50  11.16 ? 71  ASP A CB  1 
ATOM   572  C  CB  B ASP A 1 71  ? -16.982 12.691  5.707   0.50  16.75 ? 71  ASP A CB  1 
ATOM   573  C  CG  A ASP A 1 71  ? -17.601 14.105  6.184   0.50  12.02 ? 71  ASP A CG  1 
ATOM   574  C  CG  B ASP A 1 71  ? -17.124 14.145  5.979   0.50  19.63 ? 71  ASP A CG  1 
ATOM   575  O  OD1 A ASP A 1 71  ? -16.697 14.790  6.766   0.50  9.22  ? 71  ASP A OD1 1 
ATOM   576  O  OD1 B ASP A 1 71  ? -16.053 14.777  6.127   0.50  21.52 ? 71  ASP A OD1 1 
ATOM   577  O  OD2 A ASP A 1 71  ? -18.635 14.600  5.722   0.50  14.84 ? 71  ASP A OD2 1 
ATOM   578  O  OD2 B ASP A 1 71  ? -18.290 14.600  6.181   0.50  22.59 ? 71  ASP A OD2 1 
ATOM   579  N  N   . ASP A 1 72  ? -15.372 12.892  8.900   1.00  11.58 ? 72  ASP A N   1 
ATOM   580  C  CA  . ASP A 1 72  ? -15.464 13.270  10.276  1.00  12.27 ? 72  ASP A CA  1 
ATOM   581  C  C   . ASP A 1 72  ? -15.450 14.803  10.445  1.00  14.07 ? 72  ASP A C   1 
ATOM   582  O  O   . ASP A 1 72  ? -14.972 15.294  11.465  1.00  14.20 ? 72  ASP A O   1 
ATOM   583  C  CB  . ASP A 1 72  ? -14.305 12.659  11.073  1.00  12.55 ? 72  ASP A CB  1 
ATOM   584  C  CG  . ASP A 1 72  ? -12.937 13.138  10.602  1.00  14.28 ? 72  ASP A CG  1 
ATOM   585  O  OD1 . ASP A 1 72  ? -12.855 13.816  9.550   1.00  14.83 ? 72  ASP A OD1 1 
ATOM   586  O  OD2 . ASP A 1 72  ? -11.940 12.833  11.285  1.00  14.84 ? 72  ASP A OD2 1 
ATOM   587  N  N   . SER A 1 73  ? -15.995 15.505  9.440   1.00  12.97 ? 73  SER A N   1 
ATOM   588  C  CA  . SER A 1 73  ? -15.882 17.034  9.494   1.00  13.52 ? 73  SER A CA  1 
ATOM   589  C  C   . SER A 1 73  ? -17.187 17.554  10.104  1.00  14.48 ? 73  SER A C   1 
ATOM   590  O  O   . SER A 1 73  ? -17.356 18.778  10.264  1.00  15.22 ? 73  SER A O   1 
ATOM   591  C  CB  . SER A 1 73  ? -15.579 17.603  8.113   1.00  15.85 ? 73  SER A CB  1 
ATOM   592  O  OG  . SER A 1 73  ? -16.728 17.397  7.303   1.00  14.73 ? 73  SER A OG  1 
ATOM   593  N  N   . GLN A 1 74  ? -18.118 16.677  10.499  1.00  17.03 ? 74  GLN A N   1 
ATOM   594  C  CA  . GLN A 1 74  ? -19.290 17.046  11.261  1.00  17.08 ? 74  GLN A CA  1 
ATOM   595  C  C   . GLN A 1 74  ? -19.652 15.903  12.171  1.00  15.88 ? 74  GLN A C   1 
ATOM   596  O  O   . GLN A 1 74  ? -19.103 14.822  11.956  1.00  16.44 ? 74  GLN A O   1 
ATOM   597  C  CB  . GLN A 1 74  ? -20.531 17.301  10.367  1.00  21.14 ? 74  GLN A CB  1 
ATOM   598  C  CG  . GLN A 1 74  ? -20.419 18.394  9.332   1.00  22.51 ? 74  GLN A CG  1 
ATOM   599  C  CD  . GLN A 1 74  ? -21.739 18.440  8.579   1.00  23.77 ? 74  GLN A CD  1 
ATOM   600  O  OE1 . GLN A 1 74  ? -22.754 18.810  9.163   1.00  33.91 ? 74  GLN A OE1 1 
ATOM   601  N  NE2 . GLN A 1 74  ? -21.745 17.975  7.344   1.00  23.56 ? 74  GLN A NE2 1 
ATOM   602  N  N   . ASP A 1 75  ? -20.559 16.140  13.134  1.00  18.38 ? 75  ASP A N   1 
ATOM   603  C  CA  . ASP A 1 75  ? -21.038 15.134  14.076  1.00  22.90 ? 75  ASP A CA  1 
ATOM   604  C  C   . ASP A 1 75  ? -22.029 14.379  13.281  1.00  25.14 ? 75  ASP A C   1 
ATOM   605  O  O   . ASP A 1 75  ? -23.202 14.809  13.151  1.00  32.41 ? 75  ASP A O   1 
ATOM   606  C  CB  . ASP A 1 75  ? -21.744 15.695  15.353  1.00  28.05 ? 75  ASP A CB  1 
ATOM   607  C  CG  . ASP A 1 75  ? -20.750 16.123  16.437  1.00  29.95 ? 75  ASP A CG  1 
ATOM   608  O  OD1 . ASP A 1 75  ? -19.544 15.871  16.299  1.00  32.55 ? 75  ASP A OD1 1 
ATOM   609  O  OD2 . ASP A 1 75  ? -21.195 16.722  17.449  1.00  36.90 ? 75  ASP A OD2 1 
ATOM   610  N  N   . LYS A 1 76  ? -21.568 13.315  12.681  1.00  20.59 ? 76  LYS A N   1 
ATOM   611  C  CA  . LYS A 1 76  ? -22.483 12.451  11.992  1.00  22.56 ? 76  LYS A CA  1 
ATOM   612  C  C   . LYS A 1 76  ? -22.444 11.200  12.886  1.00  25.69 ? 76  LYS A C   1 
ATOM   613  O  O   . LYS A 1 76  ? -23.258 11.085  13.897  1.00  26.63 ? 76  LYS A O   1 
ATOM   614  C  CB  . LYS A 1 76  ? -22.011 12.239  10.563  1.00  21.47 ? 76  LYS A CB  1 
ATOM   615  C  CG  . LYS A 1 76  ? -22.266 13.458  9.665   1.00  23.71 ? 76  LYS A CG  1 
ATOM   616  C  CD  . LYS A 1 76  ? -21.459 13.294  8.381   1.00  21.68 ? 76  LYS A CD  1 
ATOM   617  C  CE  . LYS A 1 76  ? -21.924 14.321  7.346   1.00  26.14 ? 76  LYS A CE  1 
ATOM   618  N  NZ  . LYS A 1 76  ? -21.538 13.963  5.969   1.00  23.19 ? 76  LYS A NZ  1 
ATOM   619  N  N   . ALA A 1 77  ? -21.421 10.386  12.650  1.00  16.88 ? 77  ALA A N   1 
ATOM   620  C  CA  . ALA A 1 77  ? -21.271 9.040   13.255  1.00  16.61 ? 77  ALA A CA  1 
ATOM   621  C  C   . ALA A 1 77  ? -20.493 9.230   14.550  1.00  14.60 ? 77  ALA A C   1 
ATOM   622  O  O   . ALA A 1 77  ? -19.284 9.452   14.496  1.00  16.15 ? 77  ALA A O   1 
ATOM   623  C  CB  . ALA A 1 77  ? -20.454 8.228   12.303  1.00  15.84 ? 77  ALA A CB  1 
ATOM   624  N  N   . VAL A 1 78  ? -21.175 9.147   15.662  1.00  12.58 ? 78  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 78  ? -20.533 9.425   16.972  1.00  13.33 ? 78  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 78  ? -20.759 8.356   18.015  1.00  12.88 ? 78  VAL A C   1 
ATOM   627  O  O   . VAL A 1 78  ? -21.787 7.668   18.067  1.00  13.29 ? 78  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 78  ? -20.863 10.824  17.563  1.00  16.81 ? 78  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 78  ? -20.626 11.983  16.572  1.00  18.55 ? 78  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 78  ? -22.248 10.770  18.126  1.00  18.39 ? 78  VAL A CG2 1 
ATOM   631  N  N   . LEU A 1 79  ? -19.744 8.190   18.873  1.00  11.37 ? 79  LEU A N   1 
ATOM   632  C  CA  . LEU A 1 79  ? -19.826 7.372   20.009  1.00  12.30 ? 79  LEU A CA  1 
ATOM   633  C  C   . LEU A 1 79  ? -19.823 8.279   21.213  1.00  12.60 ? 79  LEU A C   1 
ATOM   634  O  O   . LEU A 1 79  ? -19.083 9.272   21.300  1.00  11.99 ? 79  LEU A O   1 
ATOM   635  C  CB  . LEU A 1 79  ? -18.583 6.445   20.000  1.00  12.95 ? 79  LEU A CB  1 
ATOM   636  C  CG  . LEU A 1 79  ? -18.453 5.392   21.059  1.00  13.25 ? 79  LEU A CG  1 
ATOM   637  C  CD1 . LEU A 1 79  ? -19.527 4.309   20.843  1.00  16.28 ? 79  LEU A CD1 1 
ATOM   638  C  CD2 . LEU A 1 79  ? -17.061 4.758   20.993  1.00  12.78 ? 79  LEU A CD2 1 
ATOM   639  N  N   . LYS A 1 80  ? -20.663 7.972   22.167  1.00  13.04 ? 80  LYS A N   1 
ATOM   640  C  CA  . LYS A 1 80  ? -20.733 8.653   23.465  1.00  13.95 ? 80  LYS A CA  1 
ATOM   641  C  C   . LYS A 1 80  ? -21.337 7.745   24.520  1.00  13.40 ? 80  LYS A C   1 
ATOM   642  O  O   . LYS A 1 80  ? -21.570 6.581   24.262  1.00  11.91 ? 80  LYS A O   1 
ATOM   643  C  CB  . LYS A 1 80  ? -21.378 10.028  23.416  1.00  19.22 ? 80  LYS A CB  1 
ATOM   644  C  CG  . LYS A 1 80  ? -22.804 9.944   22.942  1.00  20.63 ? 80  LYS A CG  1 
ATOM   645  C  CD  . LYS A 1 80  ? -23.397 11.300  22.464  1.00  21.92 ? 80  LYS A CD  1 
ATOM   646  C  CE  . LYS A 1 80  ? -22.639 11.904  21.295  0.010 21.35 ? 80  LYS A CE  1 
ATOM   647  N  NZ  . LYS A 1 80  ? -23.282 13.155  20.803  0.010 21.36 ? 80  LYS A NZ  1 
ATOM   648  N  N   . GLY A 1 81  ? -21.511 8.261   25.740  1.00  14.05 ? 81  GLY A N   1 
ATOM   649  C  CA  . GLY A 1 81  ? -21.998 7.414   26.821  1.00  14.58 ? 81  GLY A CA  1 
ATOM   650  C  C   . GLY A 1 81  ? -20.972 6.356   27.156  1.00  15.24 ? 81  GLY A C   1 
ATOM   651  O  O   . GLY A 1 81  ? -19.761 6.578   26.974  1.00  13.67 ? 81  GLY A O   1 
ATOM   652  N  N   . GLY A 1 82  ? -21.434 5.228   27.654  1.00  15.49 ? 82  GLY A N   1 
ATOM   653  C  CA  . GLY A 1 82  ? -20.498 4.179   28.001  1.00  15.08 ? 82  GLY A CA  1 
ATOM   654  C  C   . GLY A 1 82  ? -19.607 4.778   29.118  1.00  14.59 ? 82  GLY A C   1 
ATOM   655  O  O   . GLY A 1 82  ? -20.113 5.493   30.051  1.00  17.93 ? 82  GLY A O   1 
ATOM   656  N  N   . PRO A 1 83  ? -18.259 4.605   29.051  1.00  15.10 ? 83  PRO A N   1 
ATOM   657  C  CA  . PRO A 1 83  ? -17.367 5.217   30.002  1.00  13.05 ? 83  PRO A CA  1 
ATOM   658  C  C   . PRO A 1 83  ? -16.949 6.637   29.633  1.00  15.60 ? 83  PRO A C   1 
ATOM   659  O  O   . PRO A 1 83  ? -16.129 7.250   30.339  1.00  17.71 ? 83  PRO A O   1 
ATOM   660  C  CB  . PRO A 1 83  ? -16.071 4.320   29.907  1.00  15.20 ? 83  PRO A CB  1 
ATOM   661  C  CG  . PRO A 1 83  ? -16.073 3.891   28.462  1.00  12.13 ? 83  PRO A CG  1 
ATOM   662  C  CD  . PRO A 1 83  ? -17.538 3.732   28.079  1.00  13.18 ? 83  PRO A CD  1 
ATOM   663  N  N   . LEU A 1 84  ? -17.477 7.149   28.539  1.00  14.21 ? 84  LEU A N   1 
ATOM   664  C  CA  . LEU A 1 84  ? -16.917 8.382   27.960  1.00  14.16 ? 84  LEU A CA  1 
ATOM   665  C  C   . LEU A 1 84  ? -17.588 9.619   28.493  1.00  17.59 ? 84  LEU A C   1 
ATOM   666  O  O   . LEU A 1 84  ? -18.788 9.583   28.792  1.00  16.82 ? 84  LEU A O   1 
ATOM   667  C  CB  . LEU A 1 84  ? -17.037 8.381   26.431  1.00  11.23 ? 84  LEU A CB  1 
ATOM   668  C  CG  . LEU A 1 84  ? -16.453 7.057   25.807  1.00  9.87  ? 84  LEU A CG  1 
ATOM   669  C  CD1 . LEU A 1 84  ? -16.978 6.913   24.396  1.00  10.63 ? 84  LEU A CD1 1 
ATOM   670  C  CD2 . LEU A 1 84  ? -14.863 7.083   25.885  1.00  9.55  ? 84  LEU A CD2 1 
ATOM   671  N  N   A ASP A 1 85  ? -16.841 10.697  28.659  0.50  19.04 ? 85  ASP A N   1 
ATOM   672  N  N   B ASP A 1 85  ? -16.816 10.709  28.358  0.50  19.61 ? 85  ASP A N   1 
ATOM   673  C  CA  A ASP A 1 85  ? -17.451 11.931  29.152  0.50  21.02 ? 85  ASP A CA  1 
ATOM   674  C  CA  B ASP A 1 85  ? -17.286 12.094  28.425  0.50  21.58 ? 85  ASP A CA  1 
ATOM   675  C  C   A ASP A 1 85  ? -17.645 12.910  28.011  0.50  20.46 ? 85  ASP A C   1 
ATOM   676  C  C   B ASP A 1 85  ? -17.328 12.778  27.078  0.50  20.65 ? 85  ASP A C   1 
ATOM   677  O  O   A ASP A 1 85  ? -18.052 14.050  28.207  0.50  23.23 ? 85  ASP A O   1 
ATOM   678  O  O   B ASP A 1 85  ? -16.351 12.764  26.319  0.50  21.64 ? 85  ASP A O   1 
ATOM   679  C  CB  A ASP A 1 85  ? -16.531 12.559  30.182  0.50  22.45 ? 85  ASP A CB  1 
ATOM   680  C  CB  B ASP A 1 85  ? -16.339 12.921  29.271  0.50  25.90 ? 85  ASP A CB  1 
ATOM   681  C  CG  A ASP A 1 85  ? -16.667 11.927  31.572  0.50  27.72 ? 85  ASP A CG  1 
ATOM   682  C  CG  B ASP A 1 85  ? -16.393 12.565  30.705  0.50  29.68 ? 85  ASP A CG  1 
ATOM   683  O  OD1 A ASP A 1 85  ? -17.714 11.303  31.838  0.50  29.31 ? 85  ASP A OD1 1 
ATOM   684  O  OD1 B ASP A 1 85  ? -17.515 12.282  31.220  0.50  30.18 ? 85  ASP A OD1 1 
ATOM   685  O  OD2 A ASP A 1 85  ? -15.716 12.093  32.391  0.50  31.06 ? 85  ASP A OD2 1 
ATOM   686  O  OD2 B ASP A 1 85  ? -15.298 12.608  31.331  0.50  31.46 ? 85  ASP A OD2 1 
ATOM   687  N  N   A GLY A 1 86  ? -17.278 12.498  26.814  0.50  19.09 ? 86  GLY A N   1 
ATOM   688  N  N   B GLY A 1 86  ? -18.405 13.501  26.853  0.50  19.12 ? 86  GLY A N   1 
ATOM   689  C  CA  A GLY A 1 86  ? -17.296 13.390  25.686  0.50  17.56 ? 86  GLY A CA  1 
ATOM   690  C  CA  B GLY A 1 86  ? -18.590 14.150  25.597  0.50  19.08 ? 86  GLY A CA  1 
ATOM   691  C  C   A GLY A 1 86  ? -17.891 12.704  24.476  0.50  16.43 ? 86  GLY A C   1 
ATOM   692  C  C   B GLY A 1 86  ? -18.665 13.142  24.462  0.50  19.01 ? 86  GLY A C   1 
ATOM   693  O  O   A GLY A 1 86  ? -18.306 11.526  24.585  0.50  15.97 ? 86  GLY A O   1 
ATOM   694  O  O   B GLY A 1 86  ? -19.265 12.082  24.580  0.50  20.22 ? 86  GLY A O   1 
ATOM   695  N  N   . THR A 1 87  ? -18.002 13.456  23.368  1.00  15.76 ? 87  THR A N   1 
ATOM   696  C  CA  . THR A 1 87  ? -18.488 12.965  22.099  1.00  16.38 ? 87  THR A CA  1 
ATOM   697  C  C   . THR A 1 87  ? -17.318 12.676  21.230  1.00  13.95 ? 87  THR A C   1 
ATOM   698  O  O   . THR A 1 87  ? -16.426 13.510  21.123  1.00  13.16 ? 87  THR A O   1 
ATOM   699  C  CB  . THR A 1 87  ? -19.301 14.066  21.378  1.00  21.58 ? 87  THR A CB  1 
ATOM   700  O  OG1 . THR A 1 87  ? -20.449 14.377  22.192  1.00  24.82 ? 87  THR A OG1 1 
ATOM   701  C  CG2 . THR A 1 87  ? -19.726 13.638  19.963  1.00  22.07 ? 87  THR A CG2 1 
ATOM   702  N  N   . TYR A 1 88  ? -17.323 11.490  20.617  1.00  10.89 ? 88  TYR A N   1 
ATOM   703  C  CA  . TYR A 1 88  ? -16.181 11.040  19.825  1.00  10.48 ? 88  TYR A CA  1 
ATOM   704  C  C   . TYR A 1 88  ? -16.672 10.709  18.430  1.00  10.54 ? 88  TYR A C   1 
ATOM   705  O  O   . TYR A 1 88  ? -17.668 9.974   18.267  1.00  13.11 ? 88  TYR A O   1 
ATOM   706  C  CB  . TYR A 1 88  ? -15.556 9.793   20.425  1.00  9.57  ? 88  TYR A CB  1 
ATOM   707  C  CG  . TYR A 1 88  ? -14.806 9.997   21.721  1.00  8.34  ? 88  TYR A CG  1 
ATOM   708  C  CD1 . TYR A 1 88  ? -15.490 10.312  22.895  1.00  8.84  ? 88  TYR A CD1 1 
ATOM   709  C  CD2 . TYR A 1 88  ? -13.397 9.848   21.788  1.00  8.17  ? 88  TYR A CD2 1 
ATOM   710  C  CE1 . TYR A 1 88  ? -14.819 10.508  24.149  1.00  8.56  ? 88  TYR A CE1 1 
ATOM   711  C  CE2 . TYR A 1 88  ? -12.703 10.018  23.004  1.00  7.90  ? 88  TYR A CE2 1 
ATOM   712  C  CZ  . TYR A 1 88  ? -13.406 10.343  24.161  1.00  8.23  ? 88  TYR A CZ  1 
ATOM   713  O  OH  . TYR A 1 88  ? -12.740 10.439  25.330  1.00  9.22  ? 88  TYR A OH  1 
ATOM   714  N  N   . ARG A 1 89  ? -16.032 11.248  17.446  1.00  8.83  ? 89  ARG A N   1 
ATOM   715  C  CA  . ARG A 1 89  ? -16.420 11.059  16.045  1.00  10.37 ? 89  ARG A CA  1 
ATOM   716  C  C   . ARG A 1 89  ? -15.728 9.954   15.392  1.00  7.98  ? 89  ARG A C   1 
ATOM   717  O  O   . ARG A 1 89  ? -14.484 9.776   15.497  1.00  7.15  ? 89  ARG A O   1 
ATOM   718  C  CB  . ARG A 1 89  ? -16.063 12.309  15.254  1.00  12.45 ? 89  ARG A CB  1 
ATOM   719  C  CG  . ARG A 1 89  ? -16.972 13.417  15.504  1.00  16.55 ? 89  ARG A CG  1 
ATOM   720  C  CD  . ARG A 1 89  ? -16.804 14.338  14.338  1.00  16.90 ? 89  ARG A CD  1 
ATOM   721  N  NE  . ARG A 1 89  ? -17.529 15.543  14.743  1.00  19.37 ? 89  ARG A NE  1 
ATOM   722  C  CZ  . ARG A 1 89  ? -17.212 16.790  14.417  1.00  18.07 ? 89  ARG A CZ  1 
ATOM   723  N  NH1 . ARG A 1 89  ? -16.179 17.035  13.627  1.00  17.53 ? 89  ARG A NH1 1 
ATOM   724  N  NH2 . ARG A 1 89  ? -17.948 17.793  14.876  1.00  23.73 ? 89  ARG A NH2 1 
ATOM   725  N  N   . LEU A 1 90  ? -16.464 9.128   14.638  1.00  7.37  ? 90  LEU A N   1 
ATOM   726  C  CA  . LEU A 1 90  ? -15.836 8.044   13.882  1.00  7.55  ? 90  LEU A CA  1 
ATOM   727  C  C   . LEU A 1 90  ? -15.009 8.572   12.752  1.00  7.93  ? 90  LEU A C   1 
ATOM   728  O  O   . LEU A 1 90  ? -15.519 9.356   11.881  1.00  10.26 ? 90  LEU A O   1 
ATOM   729  C  CB  . LEU A 1 90  ? -16.954 7.149   13.282  1.00  7.81  ? 90  LEU A CB  1 
ATOM   730  C  CG  . LEU A 1 90  ? -16.517 5.936   12.455  1.00  7.55  ? 90  LEU A CG  1 
ATOM   731  C  CD1 . LEU A 1 90  ? -15.725 4.879   13.227  1.00  9.06  ? 90  LEU A CD1 1 
ATOM   732  C  CD2 . LEU A 1 90  ? -17.778 5.262   11.850  1.00  8.60  ? 90  LEU A CD2 1 
ATOM   733  N  N   . ILE A 1 91  ? -13.764 8.164   12.691  1.00  7.15  ? 91  ILE A N   1 
ATOM   734  C  CA  . ILE A 1 91  ? -12.862 8.543   11.596  1.00  7.36  ? 91  ILE A CA  1 
ATOM   735  C  C   . ILE A 1 91  ? -12.595 7.375   10.622  1.00  8.81  ? 91  ILE A C   1 
ATOM   736  O  O   . ILE A 1 91  ? -12.548 7.546   9.413   1.00  8.14  ? 91  ILE A O   1 
ATOM   737  C  CB  . ILE A 1 91  ? -11.533 9.228   12.077  1.00  7.98  ? 91  ILE A CB  1 
ATOM   738  C  CG1 . ILE A 1 91  ? -10.645 9.540   10.844  1.00  9.75  ? 91  ILE A CG1 1 
ATOM   739  C  CG2 . ILE A 1 91  ? -10.757 8.394   13.052  1.00  8.95  ? 91  ILE A CG2 1 
ATOM   740  C  CD1 . ILE A 1 91  ? -9.440  10.417  11.238  1.00  11.49 ? 91  ILE A CD1 1 
ATOM   741  N  N   . GLN A 1 92  ? -12.425 6.149   11.148  1.00  7.88  ? 92  GLN A N   1 
ATOM   742  C  CA  . GLN A 1 92  ? -12.162 4.997   10.305  1.00  7.66  ? 92  GLN A CA  1 
ATOM   743  C  C   . GLN A 1 92  ? -12.377 3.737   11.051  1.00  6.84  ? 92  GLN A C   1 
ATOM   744  O  O   . GLN A 1 92  ? -12.414 3.799   12.262  1.00  6.58  ? 92  GLN A O   1 
ATOM   745  C  CB  . GLN A 1 92  ? -10.746 4.949   9.710   1.00  9.84  ? 92  GLN A CB  1 
ATOM   746  C  CG  . GLN A 1 92  ? -9.596  5.057   10.728  1.00  9.22  ? 92  GLN A CG  1 
ATOM   747  C  CD  . GLN A 1 92  ? -8.903  3.755   11.100  1.00  10.84 ? 92  GLN A CD  1 
ATOM   748  O  OE1 . GLN A 1 92  ? -9.478  2.705   11.121  1.00  8.45  ? 92  GLN A OE1 1 
ATOM   749  N  NE2 . GLN A 1 92  ? -7.705  3.884   11.602  1.00  15.47 ? 92  GLN A NE2 1 
ATOM   750  N  N   . PHE A 1 93  ? -12.597 2.629   10.329  1.00  6.75  ? 93  PHE A N   1 
ATOM   751  C  CA  . PHE A 1 93  ? -12.404 1.327   10.958  1.00  6.62  ? 93  PHE A CA  1 
ATOM   752  C  C   . PHE A 1 93  ? -11.506 0.445   10.162  1.00  6.15  ? 93  PHE A C   1 
ATOM   753  O  O   . PHE A 1 93  ? -11.252 0.664   8.981   1.00  7.29  ? 93  PHE A O   1 
ATOM   754  C  CB  . PHE A 1 93  ? -13.756 0.643   11.197  1.00  7.62  ? 93  PHE A CB  1 
ATOM   755  C  CG  . PHE A 1 93  ? -14.539 0.164   9.955   1.00  8.32  ? 93  PHE A CG  1 
ATOM   756  C  CD1 . PHE A 1 93  ? -14.147 -0.978  9.253   1.00  8.38  ? 93  PHE A CD1 1 
ATOM   757  C  CD2 . PHE A 1 93  ? -15.705 0.881   9.549   1.00  8.83  ? 93  PHE A CD2 1 
ATOM   758  C  CE1 . PHE A 1 93  ? -14.888 -1.453  8.157   1.00  9.47  ? 93  PHE A CE1 1 
ATOM   759  C  CE2 . PHE A 1 93  ? -16.478 0.368   8.462   1.00  9.47  ? 93  PHE A CE2 1 
ATOM   760  C  CZ  . PHE A 1 93  ? -16.020 -0.766  7.769   1.00  9.70  ? 93  PHE A CZ  1 
ATOM   761  N  N   . HIS A 1 94  ? -10.984 -0.588  10.839  1.00  5.85  ? 94  HIS A N   1 
ATOM   762  C  CA  . HIS A 1 94  ? -10.110 -1.540  10.237  1.00  5.31  ? 94  HIS A CA  1 
ATOM   763  C  C   . HIS A 1 94  ? -10.125 -2.784  11.067  1.00  5.65  ? 94  HIS A C   1 
ATOM   764  O  O   . HIS A 1 94  ? -10.790 -2.814  12.068  1.00  5.74  ? 94  HIS A O   1 
ATOM   765  C  CB  . HIS A 1 94  ? -8.636  -1.030  10.159  1.00  5.54  ? 94  HIS A CB  1 
ATOM   766  C  CG  . HIS A 1 94  ? -8.050  -0.738  11.521  1.00  5.17  ? 94  HIS A CG  1 
ATOM   767  N  ND1 . HIS A 1 94  ? -8.253  0.486   12.174  1.00  5.97  ? 94  HIS A ND1 1 
ATOM   768  C  CD2 . HIS A 1 94  ? -7.453  -1.597  12.404  1.00  5.23  ? 94  HIS A CD2 1 
ATOM   769  C  CE1 . HIS A 1 94  ? -7.712  0.344   13.419  1.00  4.70  ? 94  HIS A CE1 1 
ATOM   770  N  NE2 . HIS A 1 94  ? -7.236  -0.888  13.570  1.00  4.59  ? 94  HIS A NE2 1 
ATOM   771  N  N   . PHE A 1 95  ? -9.470  -3.820  10.559  1.00  6.02  ? 95  PHE A N   1 
ATOM   772  C  CA  . PHE A 1 95  ? -9.440  -5.119  11.240  1.00  6.23  ? 95  PHE A CA  1 
ATOM   773  C  C   . PHE A 1 95  ? -8.000  -5.564  11.418  1.00  5.75  ? 95  PHE A C   1 
ATOM   774  O  O   . PHE A 1 95  ? -7.065  -5.107  10.761  1.00  6.58  ? 95  PHE A O   1 
ATOM   775  C  CB  . PHE A 1 95  ? -10.132 -6.220  10.357  1.00  6.41  ? 95  PHE A CB  1 
ATOM   776  C  CG  . PHE A 1 95  ? -11.612 -5.929  10.051  1.00  6.07  ? 95  PHE A CG  1 
ATOM   777  C  CD1 . PHE A 1 95  ? -11.963 -5.065  9.007   1.00  6.51  ? 95  PHE A CD1 1 
ATOM   778  C  CD2 . PHE A 1 95  ? -12.619 -6.588  10.747  1.00  6.16  ? 95  PHE A CD2 1 
ATOM   779  C  CE1 . PHE A 1 95  ? -13.289 -4.848  8.667   1.00  6.31  ? 95  PHE A CE1 1 
ATOM   780  C  CE2 . PHE A 1 95  ? -13.969 -6.333  10.481  1.00  6.32  ? 95  PHE A CE2 1 
ATOM   781  C  CZ  . PHE A 1 95  ? -14.264 -5.472  9.379   1.00  6.14  ? 95  PHE A CZ  1 
ATOM   782  N  N   . HIS A 1 96  ? -7.899  -6.508  12.341  1.00  6.75  ? 96  HIS A N   1 
ATOM   783  C  CA  . HIS A 1 96  ? -6.713  -7.335  12.522  1.00  5.85  ? 96  HIS A CA  1 
ATOM   784  C  C   . HIS A 1 96  ? -7.095  -8.765  12.386  1.00  6.21  ? 96  HIS A C   1 
ATOM   785  O  O   . HIS A 1 96  ? -8.143  -9.149  12.936  1.00  6.52  ? 96  HIS A O   1 
ATOM   786  C  CB  . HIS A 1 96  ? -6.001  -7.122  13.895  1.00  6.18  ? 96  HIS A CB  1 
ATOM   787  C  CG  . HIS A 1 96  ? -5.739  -5.695  14.177  1.00  5.97  ? 96  HIS A CG  1 
ATOM   788  N  ND1 . HIS A 1 96  ? -4.487  -5.141  14.002  1.00  6.04  ? 96  HIS A ND1 1 
ATOM   789  C  CD2 . HIS A 1 96  ? -6.589  -4.686  14.523  1.00  5.52  ? 96  HIS A CD2 1 
ATOM   790  C  CE1 . HIS A 1 96  ? -4.568  -3.791  14.353  1.00  6.05  ? 96  HIS A CE1 1 
ATOM   791  N  NE2 . HIS A 1 96  ? -5.868  -3.514  14.642  1.00  6.01  ? 96  HIS A NE2 1 
ATOM   792  N  N   . TRP A 1 97  ? -6.296  -9.584  11.691  1.00  5.68  ? 97  TRP A N   1 
ATOM   793  C  CA  . TRP A 1 97  ? -6.668  -11.005 11.491  1.00  5.48  ? 97  TRP A CA  1 
ATOM   794  C  C   . TRP A 1 97  ? -5.495  -11.922 11.388  1.00  6.13  ? 97  TRP A C   1 
ATOM   795  O  O   . TRP A 1 97  ? -4.325  -11.498 11.290  1.00  6.42  ? 97  TRP A O   1 
ATOM   796  C  CB  . TRP A 1 97  ? -7.601  -11.174 10.268  1.00  6.29  ? 97  TRP A CB  1 
ATOM   797  C  CG  . TRP A 1 97  ? -6.951  -10.768 8.985   1.00  6.71  ? 97  TRP A CG  1 
ATOM   798  C  CD1 . TRP A 1 97  ? -6.217  -11.562 8.146   1.00  6.98  ? 97  TRP A CD1 1 
ATOM   799  C  CD2 . TRP A 1 97  ? -6.880  -9.404  8.426   1.00  6.71  ? 97  TRP A CD2 1 
ATOM   800  N  NE1 . TRP A 1 97  ? -5.814  -10.807 7.044   1.00  8.33  ? 97  TRP A NE1 1 
ATOM   801  C  CE2 . TRP A 1 97  ? -6.141  -9.494  7.209   1.00  7.69  ? 97  TRP A CE2 1 
ATOM   802  C  CE3 . TRP A 1 97  ? -7.382  -8.161  8.840   1.00  6.95  ? 97  TRP A CE3 1 
ATOM   803  C  CZ2 . TRP A 1 97  ? -5.952  -8.403  6.402   1.00  8.11  ? 97  TRP A CZ2 1 
ATOM   804  C  CZ3 . TRP A 1 97  ? -7.157  -7.023  8.038   1.00  7.96  ? 97  TRP A CZ3 1 
ATOM   805  C  CH2 . TRP A 1 97  ? -6.436  -7.165  6.857   1.00  6.94  ? 97  TRP A CH2 1 
ATOM   806  N  N   . GLY A 1 98  ? -5.812  -13.207 11.394  1.00  6.18  ? 98  GLY A N   1 
ATOM   807  C  CA  . GLY A 1 98  ? -4.772  -14.242 11.427  1.00  7.60  ? 98  GLY A CA  1 
ATOM   808  C  C   . GLY A 1 98  ? -4.524  -14.949 10.072  1.00  7.08  ? 98  GLY A C   1 
ATOM   809  O  O   . GLY A 1 98  ? -5.275  -14.741 9.136   1.00  8.47  ? 98  GLY A O   1 
ATOM   810  N  N   . SER A 1 99  ? -3.508  -15.811 10.119  1.00  8.37  ? 99  SER A N   1 
ATOM   811  C  CA  . SER A 1 99  ? -3.230  -16.702 9.004   1.00  9.28  ? 99  SER A CA  1 
ATOM   812  C  C   . SER A 1 99  ? -4.125  -17.935 9.108   1.00  10.72 ? 99  SER A C   1 
ATOM   813  O  O   . SER A 1 99  ? -4.185  -18.699 8.099   1.00  13.46 ? 99  SER A O   1 
ATOM   814  C  CB  . SER A 1 99  ? -1.736  -17.054 9.087   1.00  8.58  ? 99  SER A CB  1 
ATOM   815  O  OG  . SER A 1 99  ? -1.369  -17.658 10.249  1.00  11.14 ? 99  SER A OG  1 
ATOM   816  N  N   . LEU A 1 100 ? -4.776  -18.173 10.264  1.00  10.25 ? 100 LEU A N   1 
ATOM   817  C  CA  . LEU A 1 100 ? -5.550  -19.349 10.560  1.00  11.83 ? 100 LEU A CA  1 
ATOM   818  C  C   . LEU A 1 100 ? -6.686  -18.877 11.425  1.00  11.22 ? 100 LEU A C   1 
ATOM   819  O  O   . LEU A 1 100 ? -6.562  -17.866 12.123  1.00  10.45 ? 100 LEU A O   1 
ATOM   820  C  CB  . LEU A 1 100 ? -4.714  -20.329 11.463  1.00  17.54 ? 100 LEU A CB  1 
ATOM   821  C  CG  . LEU A 1 100 ? -3.354  -20.678 10.963  1.00  20.95 ? 100 LEU A CG  1 
ATOM   822  C  CD1 . LEU A 1 100 ? -2.450  -20.780 12.165  1.00  25.03 ? 100 LEU A CD1 1 
ATOM   823  C  CD2 . LEU A 1 100 ? -3.483  -22.003 10.225  1.00  23.98 ? 100 LEU A CD2 1 
ATOM   824  N  N   . ASP A 1 101 ? -7.819  -19.577 11.415  1.00  9.54  ? 101 ASP A N   1 
ATOM   825  C  CA  . ASP A 1 101 ? -8.952  -19.125 12.270  1.00  10.24 ? 101 ASP A CA  1 
ATOM   826  C  C   . ASP A 1 101 ? -8.681  -19.053 13.747  1.00  10.54 ? 101 ASP A C   1 
ATOM   827  O  O   . ASP A 1 101 ? -9.356  -18.319 14.445  1.00  11.77 ? 101 ASP A O   1 
ATOM   828  C  CB  . ASP A 1 101 ? -10.172 -20.023 12.038  1.00  10.72 ? 101 ASP A CB  1 
ATOM   829  C  CG  . ASP A 1 101 ? -10.677 -19.966 10.614  1.00  13.59 ? 101 ASP A CG  1 
ATOM   830  O  OD1 . ASP A 1 101 ? -10.219 -19.087 9.851   1.00  12.73 ? 101 ASP A OD1 1 
ATOM   831  O  OD2 . ASP A 1 101 ? -11.537 -20.800 10.252  1.00  17.26 ? 101 ASP A OD2 1 
ATOM   832  N  N   . GLY A 1 102 ? -7.669  -19.827 14.263  1.00  10.20 ? 102 GLY A N   1 
ATOM   833  C  CA  . GLY A 1 102 ? -7.340  -19.849 15.668  1.00  10.05 ? 102 GLY A CA  1 
ATOM   834  C  C   . GLY A 1 102 ? -6.606  -18.662 16.235  1.00  8.71  ? 102 GLY A C   1 
ATOM   835  O  O   . GLY A 1 102 ? -6.313  -18.660 17.426  1.00  10.85 ? 102 GLY A O   1 
ATOM   836  N  N   . GLN A 1 103 ? -6.354  -17.660 15.411  1.00  8.65  ? 103 GLN A N   1 
ATOM   837  C  CA  . GLN A 1 103 ? -5.642  -16.458 15.931  1.00  7.78  ? 103 GLN A CA  1 
ATOM   838  C  C   . GLN A 1 103 ? -5.943  -15.308 15.040  1.00  6.79  ? 103 GLN A C   1 
ATOM   839  O  O   . GLN A 1 103 ? -6.540  -15.494 13.968  1.00  7.73  ? 103 GLN A O   1 
ATOM   840  C  CB  . GLN A 1 103 ? -4.118  -16.694 15.942  1.00  9.96  ? 103 GLN A CB  1 
ATOM   841  C  CG  . GLN A 1 103 ? -3.526  -16.896 14.530  1.00  11.46 ? 103 GLN A CG  1 
ATOM   842  C  CD  . GLN A 1 103 ? -2.077  -17.385 14.623  1.00  14.78 ? 103 GLN A CD  1 
ATOM   843  O  OE1 . GLN A 1 103 ? -1.760  -18.219 15.475  1.00  21.10 ? 103 GLN A OE1 1 
ATOM   844  N  NE2 . GLN A 1 103 ? -1.227  -16.938 13.739  1.00  14.79 ? 103 GLN A NE2 1 
ATOM   845  N  N   . GLY A 1 104 ? -5.646  -14.091 15.503  1.00  6.35  ? 104 GLY A N   1 
ATOM   846  C  CA  . GLY A 1 104 ? -5.959  -12.897 14.695  1.00  5.61  ? 104 GLY A CA  1 
ATOM   847  C  C   . GLY A 1 104 ? -6.354  -11.719 15.561  1.00  5.28  ? 104 GLY A C   1 
ATOM   848  O  O   . GLY A 1 104 ? -6.119  -10.555 15.211  1.00  5.53  ? 104 GLY A O   1 
ATOM   849  N  N   . SER A 1 105 ? -7.090  -12.009 16.650  1.00  4.78  ? 105 SER A N   1 
ATOM   850  C  CA  . SER A 1 105 ? -7.516  -10.875 17.514  1.00  5.05  ? 105 SER A CA  1 
ATOM   851  C  C   . SER A 1 105 ? -6.304  -10.343 18.260  1.00  5.00  ? 105 SER A C   1 
ATOM   852  O  O   . SER A 1 105 ? -5.267  -11.024 18.440  1.00  5.55  ? 105 SER A O   1 
ATOM   853  C  CB  . SER A 1 105 ? -8.635  -11.240 18.452  1.00  5.29  ? 105 SER A CB  1 
ATOM   854  O  OG  . SER A 1 105 ? -8.217  -12.177 19.410  1.00  6.03  ? 105 SER A OG  1 
ATOM   855  N  N   . GLU A 1 106 ? -6.434  -9.104  18.634  1.00  4.63  ? 106 GLU A N   1 
ATOM   856  C  CA  . GLU A 1 106 ? -5.376  -8.380  19.501  1.00  4.93  ? 106 GLU A CA  1 
ATOM   857  C  C   . GLU A 1 106 ? -5.744  -8.542  20.982  1.00  4.99  ? 106 GLU A C   1 
ATOM   858  O  O   . GLU A 1 106 ? -4.969  -9.147  21.772  1.00  5.31  ? 106 GLU A O   1 
ATOM   859  C  CB  . GLU A 1 106 ? -5.349  -6.902  19.070  1.00  5.29  ? 106 GLU A CB  1 
ATOM   860  C  CG  . GLU A 1 106 ? -4.816  -6.831  17.667  1.00  6.29  ? 106 GLU A CG  1 
ATOM   861  C  CD  . GLU A 1 106 ? -4.244  -5.505  17.341  1.00  6.49  ? 106 GLU A CD  1 
ATOM   862  O  OE1 . GLU A 1 106 ? -4.819  -4.419  17.565  1.00  6.29  ? 106 GLU A OE1 1 
ATOM   863  O  OE2 . GLU A 1 106 ? -3.077  -5.501  16.827  1.00  7.13  ? 106 GLU A OE2 1 
ATOM   864  N  N   . HIS A 1 107 ? -6.956  -8.090  21.386  1.00  4.59  ? 107 HIS A N   1 
ATOM   865  C  CA  . HIS A 1 107 ? -7.398  -8.471  22.708  1.00  4.16  ? 107 HIS A CA  1 
ATOM   866  C  C   . HIS A 1 107 ? -7.712  -9.954  22.727  1.00  4.66  ? 107 HIS A C   1 
ATOM   867  O  O   . HIS A 1 107 ? -8.065  -10.569 21.666  1.00  5.04  ? 107 HIS A O   1 
ATOM   868  C  CB  . HIS A 1 107 ? -8.634  -7.652  23.117  1.00  3.98  ? 107 HIS A CB  1 
ATOM   869  C  CG  . HIS A 1 107 ? -8.322  -6.208  23.255  1.00  3.76  ? 107 HIS A CG  1 
ATOM   870  N  ND1 . HIS A 1 107 ? -8.412  -5.313  22.194  1.00  4.09  ? 107 HIS A ND1 1 
ATOM   871  C  CD2 . HIS A 1 107 ? -7.874  -5.488  24.334  1.00  3.68  ? 107 HIS A CD2 1 
ATOM   872  C  CE1 . HIS A 1 107 ? -7.978  -4.104  22.595  1.00  4.16  ? 107 HIS A CE1 1 
ATOM   873  N  NE2 . HIS A 1 107 ? -7.669  -4.195  23.922  1.00  3.62  ? 107 HIS A NE2 1 
ATOM   874  N  N   . THR A 1 108 ? -7.595  -10.511 23.910  1.00  5.57  ? 108 THR A N   1 
ATOM   875  C  CA  . THR A 1 108 ? -7.909  -11.891 24.106  1.00  5.03  ? 108 THR A CA  1 
ATOM   876  C  C   . THR A 1 108 ? -8.921  -11.930 25.297  1.00  5.18  ? 108 THR A C   1 
ATOM   877  O  O   . THR A 1 108 ? -8.959  -10.999 26.114  1.00  6.20  ? 108 THR A O   1 
ATOM   878  C  CB  . THR A 1 108 ? -6.720  -12.840 24.304  1.00  5.81  ? 108 THR A CB  1 
ATOM   879  O  OG1 . THR A 1 108 ? -5.927  -12.343 25.400  1.00  6.72  ? 108 THR A OG1 1 
ATOM   880  C  CG2 . THR A 1 108 ? -5.899  -12.956 23.070  1.00  5.58  ? 108 THR A CG2 1 
ATOM   881  N  N   . VAL A 1 109 ? -9.679  -13.032 25.435  1.00  6.30  ? 109 VAL A N   1 
ATOM   882  C  CA  . VAL A 1 109 ? -10.683 -13.122 26.565  1.00  6.97  ? 109 VAL A CA  1 
ATOM   883  C  C   . VAL A 1 109 ? -10.326 -14.417 27.281  1.00  8.10  ? 109 VAL A C   1 
ATOM   884  O  O   . VAL A 1 109 ? -10.476 -15.483 26.699  1.00  8.37  ? 109 VAL A O   1 
ATOM   885  C  CB  . VAL A 1 109 ? -12.111 -13.163 25.954  1.00  8.27  ? 109 VAL A CB  1 
ATOM   886  C  CG1 . VAL A 1 109 ? -13.183 -13.166 27.061  1.00  9.08  ? 109 VAL A CG1 1 
ATOM   887  C  CG2 . VAL A 1 109 ? -12.406 -11.857 25.169  1.00  8.30  ? 109 VAL A CG2 1 
ATOM   888  N  N   . ASP A 1 110 ? -9.897  -14.297 28.511  1.00  8.54  ? 110 ASP A N   1 
ATOM   889  C  CA  . ASP A 1 110 ? -9.388  -15.512 29.251  1.00  8.81  ? 110 ASP A CA  1 
ATOM   890  C  C   . ASP A 1 110 ? -8.455  -16.331 28.326  1.00  8.58  ? 110 ASP A C   1 
ATOM   891  O  O   . ASP A 1 110 ? -8.489  -17.580 28.263  1.00  9.94  ? 110 ASP A O   1 
ATOM   892  C  CB  . ASP A 1 110 ? -10.550 -16.358 29.738  1.00  9.80  ? 110 ASP A CB  1 
ATOM   893  C  CG  . ASP A 1 110 ? -11.453 -15.572 30.733  1.00  10.79 ? 110 ASP A CG  1 
ATOM   894  O  OD1 . ASP A 1 110 ? -10.914 -14.753 31.424  1.00  13.17 ? 110 ASP A OD1 1 
ATOM   895  O  OD2 . ASP A 1 110 ? -12.655 -15.821 30.795  1.00  15.21 ? 110 ASP A OD2 1 
ATOM   896  N  N   . LYS A 1 111 ? -7.579  -15.588 27.633  1.00  8.15  ? 111 LYS A N   1 
ATOM   897  C  CA  . LYS A 1 111 ? -6.464  -16.071 26.757  1.00  9.11  ? 111 LYS A CA  1 
ATOM   898  C  C   . LYS A 1 111 ? -6.996  -16.642 25.464  1.00  8.51  ? 111 LYS A C   1 
ATOM   899  O  O   . LYS A 1 111 ? -6.208  -16.994 24.568  1.00  9.15  ? 111 LYS A O   1 
ATOM   900  C  CB  . LYS A 1 111 ? -5.558  -17.135 27.464  1.00  11.76 ? 111 LYS A CB  1 
ATOM   901  C  CG  . LYS A 1 111 ? -4.907  -16.673 28.753  1.00  14.08 ? 111 LYS A CG  1 
ATOM   902  C  CD  . LYS A 1 111 ? -4.016  -15.526 28.506  1.00  16.77 ? 111 LYS A CD  1 
ATOM   903  C  CE  . LYS A 1 111 ? -3.410  -15.038 29.818  1.00  19.99 ? 111 LYS A CE  1 
ATOM   904  N  NZ  . LYS A 1 111 ? -2.041  -15.527 29.654  1.00  23.89 ? 111 LYS A NZ  1 
ATOM   905  N  N   . LYS A 1 112 ? -8.306  -16.576 25.218  1.00  7.76  ? 112 LYS A N   1 
ATOM   906  C  CA  . LYS A 1 112 ? -8.883  -17.036 23.972  1.00  8.70  ? 112 LYS A CA  1 
ATOM   907  C  C   . LYS A 1 112 ? -8.619  -15.953 22.892  1.00  8.16  ? 112 LYS A C   1 
ATOM   908  O  O   . LYS A 1 112 ? -8.922  -14.715 23.066  1.00  8.49  ? 112 LYS A O   1 
ATOM   909  C  CB  . LYS A 1 112 ? -10.425 -17.192 24.092  1.00  11.02 ? 112 LYS A CB  1 
ATOM   910  C  CG  . LYS A 1 112 ? -11.159 -17.393 22.754  1.00  12.98 ? 112 LYS A CG  1 
ATOM   911  C  CD  . LYS A 1 112 ? -12.682 -17.453 22.974  1.00  15.59 ? 112 LYS A CD  1 
ATOM   912  C  CE  . LYS A 1 112 ? -13.308 -17.479 21.578  1.00  18.51 ? 112 LYS A CE  1 
ATOM   913  N  NZ  . LYS A 1 112 ? -13.153 -18.802 21.022  1.00  20.25 ? 112 LYS A NZ  1 
ATOM   914  N  N   A LYS A 1 113 ? -8.069  -16.429 21.797  0.50  7.67  ? 113 LYS A N   1 
ATOM   915  N  N   B LYS A 1 113 ? -8.077  -16.417 21.784  0.50  7.75  ? 113 LYS A N   1 
ATOM   916  C  CA  A LYS A 1 113 ? -7.928  -15.637 20.559  0.50  7.42  ? 113 LYS A CA  1 
ATOM   917  C  CA  B LYS A 1 113 ? -7.868  -15.595 20.557  0.50  7.52  ? 113 LYS A CA  1 
ATOM   918  C  C   A LYS A 1 113 ? -9.130  -15.845 19.668  0.50  7.14  ? 113 LYS A C   1 
ATOM   919  C  C   B LYS A 1 113 ? -8.959  -15.826 19.545  0.50  7.26  ? 113 LYS A C   1 
ATOM   920  O  O   A LYS A 1 113 ? -9.620  -16.981 19.494  0.50  7.19  ? 113 LYS A O   1 
ATOM   921  O  O   B LYS A 1 113 ? -9.161  -16.978 19.134  0.50  7.41  ? 113 LYS A O   1 
ATOM   922  C  CB  A LYS A 1 113 ? -6.661  -16.044 19.824  0.50  7.16  ? 113 LYS A CB  1 
ATOM   923  C  CB  B LYS A 1 113 ? -6.545  -15.980 19.912  0.50  7.40  ? 113 LYS A CB  1 
ATOM   924  C  CG  A LYS A 1 113 ? -5.383  -15.669 20.564  0.50  7.66  ? 113 LYS A CG  1 
ATOM   925  C  CG  B LYS A 1 113 ? -5.358  -15.531 20.757  0.50  7.75  ? 113 LYS A CG  1 
ATOM   926  C  CD  A LYS A 1 113 ? -4.225  -16.345 19.849  0.50  8.41  ? 113 LYS A CD  1 
ATOM   927  C  CD  B LYS A 1 113 ? -4.053  -16.127 20.265  0.50  8.65  ? 113 LYS A CD  1 
ATOM   928  C  CE  A LYS A 1 113 ? -2.890  -15.840 20.378  0.50  9.15  ? 113 LYS A CE  1 
ATOM   929  C  CE  B LYS A 1 113 ? -2.843  -15.519 20.968  0.50  9.20  ? 113 LYS A CE  1 
ATOM   930  N  NZ  A LYS A 1 113 ? -2.446  -16.453 21.671  0.50  10.01 ? 113 LYS A NZ  1 
ATOM   931  N  NZ  B LYS A 1 113 ? -1.695  -16.377 20.529  0.50  11.96 ? 113 LYS A NZ  1 
ATOM   932  N  N   . TYR A 1 114 ? -9.623  -14.751 19.094  1.00  7.38  ? 114 TYR A N   1 
ATOM   933  C  CA  . TYR A 1 114 ? -10.594 -14.825 18.021  1.00  6.72  ? 114 TYR A CA  1 
ATOM   934  C  C   . TYR A 1 114 ? -9.996  -14.768 16.636  1.00  6.35  ? 114 TYR A C   1 
ATOM   935  O  O   . TYR A 1 114 ? -8.810  -14.479 16.530  1.00  6.40  ? 114 TYR A O   1 
ATOM   936  C  CB  . TYR A 1 114 ? -11.710 -13.726 18.176  1.00  6.95  ? 114 TYR A CB  1 
ATOM   937  C  CG  . TYR A 1 114 ? -12.636 -13.927 19.354  1.00  8.19  ? 114 TYR A CG  1 
ATOM   938  C  CD1 . TYR A 1 114 ? -12.317 -13.510 20.646  1.00  8.67  ? 114 TYR A CD1 1 
ATOM   939  C  CD2 . TYR A 1 114 ? -13.828 -14.582 19.123  1.00  9.44  ? 114 TYR A CD2 1 
ATOM   940  C  CE1 . TYR A 1 114 ? -13.182 -13.743 21.678  1.00  10.44 ? 114 TYR A CE1 1 
ATOM   941  C  CE2 . TYR A 1 114 ? -14.742 -14.748 20.154  1.00  10.30 ? 114 TYR A CE2 1 
ATOM   942  C  CZ  . TYR A 1 114 ? -14.372 -14.353 21.415  1.00  11.28 ? 114 TYR A CZ  1 
ATOM   943  O  OH  . TYR A 1 114 ? -15.252 -14.484 22.530  1.00  15.07 ? 114 TYR A OH  1 
ATOM   944  N  N   . ALA A 1 115 ? -10.741 -15.081 15.581  1.00  6.17  ? 115 ALA A N   1 
ATOM   945  C  CA  . ALA A 1 115 ? -10.155 -15.063 14.252  1.00  6.48  ? 115 ALA A CA  1 
ATOM   946  C  C   . ALA A 1 115 ? -9.748  -13.674 13.754  1.00  6.32  ? 115 ALA A C   1 
ATOM   947  O  O   . ALA A 1 115 ? -8.871  -13.502 12.844  1.00  6.65  ? 115 ALA A O   1 
ATOM   948  C  CB  . ALA A 1 115 ? -11.180 -15.698 13.295  1.00  7.41  ? 115 ALA A CB  1 
ATOM   949  N  N   . ALA A 1 116 ? -10.445 -12.666 14.301  1.00  6.05  ? 116 ALA A N   1 
ATOM   950  C  CA  . ALA A 1 116 ? -10.104 -11.312 13.860  1.00  6.20  ? 116 ALA A CA  1 
ATOM   951  C  C   . ALA A 1 116 ? -10.702 -10.326 14.911  1.00  5.75  ? 116 ALA A C   1 
ATOM   952  O  O   . ALA A 1 116 ? -11.465 -10.697 15.798  1.00  5.65  ? 116 ALA A O   1 
ATOM   953  C  CB  . ALA A 1 116 ? -10.661 -11.001 12.437  1.00  6.68  ? 116 ALA A CB  1 
ATOM   954  N  N   . GLU A 1 117 ? -10.383 -9.050  14.731  1.00  5.83  ? 117 GLU A N   1 
ATOM   955  C  CA  . GLU A 1 117 ? -10.919 -8.007  15.622  1.00  5.41  ? 117 GLU A CA  1 
ATOM   956  C  C   . GLU A 1 117 ? -11.097 -6.742  14.794  1.00  5.53  ? 117 GLU A C   1 
ATOM   957  O  O   . GLU A 1 117 ? -10.169 -6.358  14.058  1.00  6.12  ? 117 GLU A O   1 
ATOM   958  C  CB  . GLU A 1 117 ? -9.939  -7.760  16.771  1.00  5.21  ? 117 GLU A CB  1 
ATOM   959  C  CG  . GLU A 1 117 ? -10.475 -6.794  17.880  1.00  5.46  ? 117 GLU A CG  1 
ATOM   960  C  CD  . GLU A 1 117 ? -9.506  -6.746  19.074  1.00  5.67  ? 117 GLU A CD  1 
ATOM   961  O  OE1 . GLU A 1 117 ? -8.881  -7.794  19.339  1.00  6.09  ? 117 GLU A OE1 1 
ATOM   962  O  OE2 . GLU A 1 117 ? -9.490  -5.673  19.726  1.00  6.20  ? 117 GLU A OE2 1 
ATOM   963  N  N   . LEU A 1 118 ? -12.274 -6.178  14.913  1.00  5.51  ? 118 LEU A N   1 
ATOM   964  C  CA  . LEU A 1 118 ? -12.639 -4.918  14.274  1.00  4.81  ? 118 LEU A CA  1 
ATOM   965  C  C   . LEU A 1 118 ? -12.403 -3.791  15.260  1.00  4.82  ? 118 LEU A C   1 
ATOM   966  O  O   . LEU A 1 118 ? -12.844 -3.852  16.387  1.00  5.58  ? 118 LEU A O   1 
ATOM   967  C  CB  . LEU A 1 118 ? -14.134 -5.036  13.894  1.00  5.30  ? 118 LEU A CB  1 
ATOM   968  C  CG  . LEU A 1 118 ? -14.946 -3.710  13.570  1.00  6.02  ? 118 LEU A CG  1 
ATOM   969  C  CD1 . LEU A 1 118 ? -14.386 -3.081  12.345  1.00  6.49  ? 118 LEU A CD1 1 
ATOM   970  C  CD2 . LEU A 1 118 ? -16.416 -4.086  13.249  1.00  6.18  ? 118 LEU A CD2 1 
ATOM   971  N  N   . HIS A 1 119 ? -11.804 -2.721  14.710  1.00  4.06  ? 119 HIS A N   1 
ATOM   972  C  CA  . HIS A 1 119 ? -11.583 -1.486  15.493  1.00  4.42  ? 119 HIS A CA  1 
ATOM   973  C  C   . HIS A 1 119 ? -12.268 -0.341  14.814  1.00  4.59  ? 119 HIS A C   1 
ATOM   974  O  O   . HIS A 1 119 ? -11.867 0.024   13.713  1.00  5.26  ? 119 HIS A O   1 
ATOM   975  C  CB  . HIS A 1 119 ? -10.070 -1.220  15.577  1.00  4.35  ? 119 HIS A CB  1 
ATOM   976  C  CG  . HIS A 1 119 ? -9.379  -2.203  16.500  1.00  4.50  ? 119 HIS A CG  1 
ATOM   977  N  ND1 . HIS A 1 119 ? -8.013  -2.415  16.488  1.00  4.44  ? 119 HIS A ND1 1 
ATOM   978  C  CD2 . HIS A 1 119 ? -9.907  -3.002  17.473  1.00  4.50  ? 119 HIS A CD2 1 
ATOM   979  C  CE1 . HIS A 1 119 ? -7.703  -3.345  17.400  1.00  4.70  ? 119 HIS A CE1 1 
ATOM   980  N  NE2 . HIS A 1 119 ? -8.867  -3.733  18.028  1.00  4.73  ? 119 HIS A NE2 1 
ATOM   981  N  N   . LEU A 1 120 ? -13.259 0.252   15.499  1.00  4.74  ? 120 LEU A N   1 
ATOM   982  C  CA  . LEU A 1 120 ? -13.889 1.523   15.055  1.00  5.03  ? 120 LEU A CA  1 
ATOM   983  C  C   . LEU A 1 120 ? -13.273 2.655   15.820  1.00  4.64  ? 120 LEU A C   1 
ATOM   984  O  O   . LEU A 1 120 ? -13.412 2.698   17.046  1.00  4.61  ? 120 LEU A O   1 
ATOM   985  C  CB  . LEU A 1 120 ? -15.413 1.429   15.226  1.00  5.53  ? 120 LEU A CB  1 
ATOM   986  C  CG  . LEU A 1 120 ? -16.088 0.295   14.392  1.00  5.94  ? 120 LEU A CG  1 
ATOM   987  C  CD1 . LEU A 1 120 ? -16.934 -0.578  15.264  1.00  7.61  ? 120 LEU A CD1 1 
ATOM   988  C  CD2 . LEU A 1 120 ? -16.950 1.005   13.327  1.00  7.15  ? 120 LEU A CD2 1 
ATOM   989  N  N   . VAL A 1 121 ? -12.487 3.443   15.077  1.00  4.47  ? 121 VAL A N   1 
ATOM   990  C  CA  . VAL A 1 121 ? -11.648 4.486   15.737  1.00  5.26  ? 121 VAL A CA  1 
ATOM   991  C  C   . VAL A 1 121 ? -12.380 5.814   15.775  1.00  5.70  ? 121 VAL A C   1 
ATOM   992  O  O   . VAL A 1 121 ? -12.786 6.318   14.701  1.00  6.01  ? 121 VAL A O   1 
ATOM   993  C  CB  . VAL A 1 121 ? -10.303 4.562   15.013  1.00  5.03  ? 121 VAL A CB  1 
ATOM   994  C  CG1 . VAL A 1 121 ? -9.465  5.659   15.662  1.00  5.45  ? 121 VAL A CG1 1 
ATOM   995  C  CG2 . VAL A 1 121 ? -9.584  3.213   14.911  1.00  5.59  ? 121 VAL A CG2 1 
ATOM   996  N  N   . HIS A 1 122 ? -12.531 6.386   17.011  1.00  5.58  ? 122 HIS A N   1 
ATOM   997  C  CA  . HIS A 1 122 ? -13.188 7.665   17.137  1.00  5.74  ? 122 HIS A CA  1 
ATOM   998  C  C   . HIS A 1 122 ? -12.294 8.658   17.871  1.00  6.35  ? 122 HIS A C   1 
ATOM   999  O  O   . HIS A 1 122 ? -11.477 8.283   18.709  1.00  6.59  ? 122 HIS A O   1 
ATOM   1000 C  CB  . HIS A 1 122 ? -14.495 7.544   17.948  1.00  5.97  ? 122 HIS A CB  1 
ATOM   1001 C  CG  . HIS A 1 122 ? -15.370 6.383   17.545  1.00  5.96  ? 122 HIS A CG  1 
ATOM   1002 N  ND1 . HIS A 1 122 ? -15.042 5.104   17.802  1.00  6.47  ? 122 HIS A ND1 1 
ATOM   1003 C  CD2 . HIS A 1 122 ? -16.608 6.350   16.904  1.00  6.84  ? 122 HIS A CD2 1 
ATOM   1004 C  CE1 . HIS A 1 122 ? -16.011 4.292   17.341  1.00  7.39  ? 122 HIS A CE1 1 
ATOM   1005 N  NE2 . HIS A 1 122 ? -16.969 5.056   16.792  1.00  7.31  ? 122 HIS A NE2 1 
ATOM   1006 N  N   . TRP A 1 123 ? -12.453 9.939   17.554  1.00  6.36  ? 123 TRP A N   1 
ATOM   1007 C  CA  . TRP A 1 123 ? -11.643 11.000  18.255  1.00  6.69  ? 123 TRP A CA  1 
ATOM   1008 C  C   . TRP A 1 123 ? -12.511 11.964  18.995  1.00  6.98  ? 123 TRP A C   1 
ATOM   1009 O  O   . TRP A 1 123 ? -13.630 12.349  18.510  1.00  7.78  ? 123 TRP A O   1 
ATOM   1010 C  CB  . TRP A 1 123 ? -10.635 11.672  17.340  1.00  7.45  ? 123 TRP A CB  1 
ATOM   1011 C  CG  . TRP A 1 123 ? -11.303 12.289  16.150  1.00  8.56  ? 123 TRP A CG  1 
ATOM   1012 C  CD1 . TRP A 1 123 ? -11.425 11.726  14.918  1.00  8.78  ? 123 TRP A CD1 1 
ATOM   1013 C  CD2 . TRP A 1 123 ? -11.743 13.674  16.016  1.00  9.55  ? 123 TRP A CD2 1 
ATOM   1014 N  NE1 . TRP A 1 123 ? -12.080 12.578  14.067  1.00  9.53  ? 123 TRP A NE1 1 
ATOM   1015 C  CE2 . TRP A 1 123 ? -12.244 13.809  14.671  1.00  10.00 ? 123 TRP A CE2 1 
ATOM   1016 C  CE3 . TRP A 1 123 ? -11.824 14.770  16.888  1.00  9.87  ? 123 TRP A CE3 1 
ATOM   1017 C  CZ2 . TRP A 1 123 ? -12.764 14.992  14.213  1.00  11.40 ? 123 TRP A CZ2 1 
ATOM   1018 C  CZ3 . TRP A 1 123 ? -12.398 15.938  16.402  1.00  10.69 ? 123 TRP A CZ3 1 
ATOM   1019 C  CH2 . TRP A 1 123 ? -12.879 16.032  15.091  1.00  10.96 ? 123 TRP A CH2 1 
ATOM   1020 N  N   . ASN A 1 124 ? -11.987 12.465  20.128  1.00  7.71  ? 124 ASN A N   1 
ATOM   1021 C  CA  . ASN A 1 124 ? -12.760 13.352  21.001  1.00  7.93  ? 124 ASN A CA  1 
ATOM   1022 C  C   . ASN A 1 124 ? -12.913 14.736  20.396  1.00  8.63  ? 124 ASN A C   1 
ATOM   1023 O  O   . ASN A 1 124 ? -11.898 15.409  20.091  1.00  8.17  ? 124 ASN A O   1 
ATOM   1024 C  CB  . ASN A 1 124 ? -11.958 13.409  22.318  1.00  8.05  ? 124 ASN A CB  1 
ATOM   1025 C  CG  . ASN A 1 124 ? -12.767 13.989  23.452  1.00  9.22  ? 124 ASN A CG  1 
ATOM   1026 O  OD1 . ASN A 1 124 ? -13.584 14.872  23.208  1.00  10.07 ? 124 ASN A OD1 1 
ATOM   1027 N  ND2 . ASN A 1 124 ? -12.516 13.503  24.679  1.00  11.41 ? 124 ASN A ND2 1 
ATOM   1028 N  N   . THR A 1 125 ? -14.181 15.142  20.228  1.00  9.65  ? 125 THR A N   1 
ATOM   1029 C  CA  . THR A 1 125 ? -14.397 16.454  19.550  1.00  10.88 ? 125 THR A CA  1 
ATOM   1030 C  C   . THR A 1 125 ? -13.845 17.704  20.301  1.00  11.50 ? 125 THR A C   1 
ATOM   1031 O  O   . THR A 1 125 ? -13.637 18.721  19.608  1.00  13.30 ? 125 THR A O   1 
ATOM   1032 C  CB  . THR A 1 125 ? -15.863 16.614  19.191  1.00  12.92 ? 125 THR A CB  1 
ATOM   1033 O  OG1 . THR A 1 125 ? -16.603 16.600  20.391  1.00  15.13 ? 125 THR A OG1 1 
ATOM   1034 C  CG2 . THR A 1 125 ? -16.332 15.486  18.224  1.00  14.81 ? 125 THR A CG2 1 
ATOM   1035 N  N   . LYS A 1 126 ? -13.538 17.408  21.676  1.00  11.18 ? 127 LYS A N   1 
ATOM   1036 C  CA  . LYS A 1 126 ? -12.969 18.601  22.320  1.00  13.68 ? 127 LYS A CA  1 
ATOM   1037 C  C   . LYS A 1 126 ? -11.598 18.955  21.774  1.00  14.98 ? 127 LYS A C   1 
ATOM   1038 O  O   . LYS A 1 126 ? -11.114 20.093  21.980  1.00  16.52 ? 127 LYS A O   1 
ATOM   1039 C  CB  . LYS A 1 126 ? -12.977 18.400  23.838  1.00  16.18 ? 127 LYS A CB  1 
ATOM   1040 C  CG  . LYS A 1 126 ? -12.012 17.455  24.444  1.00  18.64 ? 127 LYS A CG  1 
ATOM   1041 C  CD  . LYS A 1 126 ? -12.444 17.250  25.912  1.00  21.80 ? 127 LYS A CD  1 
ATOM   1042 C  CE  . LYS A 1 126 ? -11.581 16.302  26.697  1.00  25.59 ? 127 LYS A CE  1 
ATOM   1043 N  NZ  . LYS A 1 126 ? -10.705 16.930  27.775  1.00  32.86 ? 127 LYS A NZ  1 
ATOM   1044 N  N   . TYR A 1 127 ? -10.951 18.066  21.005  1.00  11.16 ? 128 TYR A N   1 
ATOM   1045 C  CA  . TYR A 1 127 ? -9.602  18.367  20.503  1.00  11.26 ? 128 TYR A CA  1 
ATOM   1046 C  C   . TYR A 1 127 ? -9.547  18.760  19.052  1.00  11.38 ? 128 TYR A C   1 
ATOM   1047 O  O   . TYR A 1 127 ? -8.472  18.963  18.447  1.00  12.64 ? 128 TYR A O   1 
ATOM   1048 C  CB  . TYR A 1 127 ? -8.664  17.186  20.734  1.00  10.98 ? 128 TYR A CB  1 
ATOM   1049 C  CG  . TYR A 1 127 ? -8.549  16.917  22.173  1.00  9.94  ? 128 TYR A CG  1 
ATOM   1050 C  CD1 . TYR A 1 127 ? -8.144  17.965  23.062  1.00  11.22 ? 128 TYR A CD1 1 
ATOM   1051 C  CD2 . TYR A 1 127 ? -8.829  15.676  22.751  1.00  9.14  ? 128 TYR A CD2 1 
ATOM   1052 C  CE1 . TYR A 1 127 ? -8.058  17.693  24.421  1.00  11.31 ? 128 TYR A CE1 1 
ATOM   1053 C  CE2 . TYR A 1 127 ? -8.728  15.404  24.106  1.00  10.33 ? 128 TYR A CE2 1 
ATOM   1054 C  CZ  . TYR A 1 127 ? -8.299  16.475  24.935  1.00  10.99 ? 128 TYR A CZ  1 
ATOM   1055 O  OH  . TYR A 1 127 ? -8.294  16.201  26.215  1.00  12.71 ? 128 TYR A OH  1 
ATOM   1056 N  N   . GLY A 1 128 ? -10.731 18.809  18.442  1.00  11.60 ? 129 GLY A N   1 
ATOM   1057 C  CA  . GLY A 1 128 ? -10.872 19.444  17.096  1.00  12.47 ? 129 GLY A CA  1 
ATOM   1058 C  C   . GLY A 1 128 ? -10.482 18.608  15.890  1.00  12.81 ? 129 GLY A C   1 
ATOM   1059 O  O   . GLY A 1 128 ? -11.090 18.749  14.783  1.00  14.93 ? 129 GLY A O   1 
ATOM   1060 N  N   . ASP A 1 129 ? -9.431  17.773  16.006  1.00  11.76 ? 130 ASP A N   1 
ATOM   1061 C  CA  . ASP A 1 129 ? -9.201  16.777  14.947  1.00  13.25 ? 130 ASP A CA  1 
ATOM   1062 C  C   . ASP A 1 129 ? -8.382  15.610  15.487  1.00  13.28 ? 130 ASP A C   1 
ATOM   1063 O  O   . ASP A 1 129 ? -7.955  15.619  16.641  1.00  13.71 ? 130 ASP A O   1 
ATOM   1064 C  CB  . ASP A 1 129 ? -8.580  17.402  13.703  1.00  15.72 ? 130 ASP A CB  1 
ATOM   1065 C  CG  . ASP A 1 129 ? -7.207  17.871  13.926  1.00  16.65 ? 130 ASP A CG  1 
ATOM   1066 O  OD1 . ASP A 1 129 ? -6.575  17.643  14.985  1.00  20.74 ? 130 ASP A OD1 1 
ATOM   1067 O  OD2 . ASP A 1 129 ? -6.657  18.514  13.023  1.00  20.49 ? 130 ASP A OD2 1 
ATOM   1068 N  N   . PHE A 1 130 ? -8.262  14.578  14.657  1.00  12.60 ? 131 PHE A N   1 
ATOM   1069 C  CA  . PHE A 1 130 ? -7.599  13.364  15.053  1.00  12.02 ? 131 PHE A CA  1 
ATOM   1070 C  C   . PHE A 1 130 ? -6.154  13.613  15.434  1.00  11.33 ? 131 PHE A C   1 
ATOM   1071 O  O   . PHE A 1 130 ? -5.677  13.053  16.426  1.00  9.02  ? 131 PHE A O   1 
ATOM   1072 C  CB  . PHE A 1 130 ? -7.679  12.338  13.867  1.00  9.74  ? 131 PHE A CB  1 
ATOM   1073 C  CG  . PHE A 1 130 ? -6.998  11.010  14.113  1.00  10.48 ? 131 PHE A CG  1 
ATOM   1074 C  CD1 . PHE A 1 130 ? -7.632  9.994   14.846  1.00  9.68  ? 131 PHE A CD1 1 
ATOM   1075 C  CD2 . PHE A 1 130 ? -5.672  10.816  13.697  1.00  11.64 ? 131 PHE A CD2 1 
ATOM   1076 C  CE1 . PHE A 1 130 ? -6.947  8.831   15.067  1.00  10.36 ? 131 PHE A CE1 1 
ATOM   1077 C  CE2 . PHE A 1 130 ? -5.017  9.634   13.884  1.00  11.88 ? 131 PHE A CE2 1 
ATOM   1078 C  CZ  . PHE A 1 130 ? -5.648  8.670   14.641  1.00  10.96 ? 131 PHE A CZ  1 
ATOM   1079 N  N   . GLY A 1 131 ? -5.411  14.414  14.644  1.00  11.17 ? 132 GLY A N   1 
ATOM   1080 C  CA  . GLY A 1 131 ? -3.989  14.521  14.948  1.00  10.99 ? 132 GLY A CA  1 
ATOM   1081 C  C   . GLY A 1 131 ? -3.709  15.223  16.275  1.00  10.73 ? 132 GLY A C   1 
ATOM   1082 O  O   . GLY A 1 131 ? -2.710  14.902  16.932  1.00  13.04 ? 132 GLY A O   1 
ATOM   1083 N  N   . LYS A 1 132 ? -4.583  16.158  16.648  1.00  11.35 ? 133 LYS A N   1 
ATOM   1084 C  CA  . LYS A 1 132 ? -4.413  16.711  17.987  1.00  11.76 ? 133 LYS A CA  1 
ATOM   1085 C  C   . LYS A 1 132 ? -4.929  15.775  19.104  1.00  10.63 ? 133 LYS A C   1 
ATOM   1086 O  O   . LYS A 1 132 ? -4.336  15.702  20.191  1.00  10.60 ? 133 LYS A O   1 
ATOM   1087 C  CB  . LYS A 1 132 ? -5.147  18.021  18.089  1.00  13.45 ? 133 LYS A CB  1 
ATOM   1088 C  CG  . LYS A 1 132 ? -4.486  19.150  17.291  1.00  19.70 ? 133 LYS A CG  1 
ATOM   1089 C  CD  . LYS A 1 132 ? -3.073  19.455  17.805  1.00  25.75 ? 133 LYS A CD  1 
ATOM   1090 C  CE  . LYS A 1 132 ? -3.051  20.466  18.964  1.00  31.66 ? 133 LYS A CE  1 
ATOM   1091 N  NZ  . LYS A 1 132 ? -1.696  21.082  19.019  1.00  36.53 ? 133 LYS A NZ  1 
ATOM   1092 N  N   . ALA A 1 133 ? -6.028  15.044  18.819  1.00  10.29 ? 134 ALA A N   1 
ATOM   1093 C  CA  . ALA A 1 133 ? -6.574  14.159  19.799  1.00  9.22  ? 134 ALA A CA  1 
ATOM   1094 C  C   . ALA A 1 133 ? -5.568  13.068  20.199  1.00  9.05  ? 134 ALA A C   1 
ATOM   1095 O  O   . ALA A 1 133 ? -5.515  12.696  21.362  1.00  8.77  ? 134 ALA A O   1 
ATOM   1096 C  CB  . ALA A 1 133 ? -7.835  13.464  19.207  1.00  8.16  ? 134 ALA A CB  1 
ATOM   1097 N  N   . VAL A 1 134 ? -4.771  12.555  19.288  1.00  8.81  ? 135 VAL A N   1 
ATOM   1098 C  CA  . VAL A 1 134 ? -3.887  11.431  19.687  1.00  9.28  ? 135 VAL A CA  1 
ATOM   1099 C  C   . VAL A 1 134 ? -2.742  11.878  20.640  1.00  9.14  ? 135 VAL A C   1 
ATOM   1100 O  O   . VAL A 1 134 ? -2.064  11.056  21.173  1.00  8.65  ? 135 VAL A O   1 
ATOM   1101 C  CB  . VAL A 1 134 ? -3.216  10.678  18.498  1.00  10.21 ? 135 VAL A CB  1 
ATOM   1102 C  CG1 . VAL A 1 134 ? -4.316  10.006  17.685  1.00  10.71 ? 135 VAL A CG1 1 
ATOM   1103 C  CG2 . VAL A 1 134 ? -2.309  11.540  17.628  1.00  10.26 ? 135 VAL A CG2 1 
ATOM   1104 N  N   A GLN A 1 135 ? -2.569  13.180  20.810  0.50  10.05 ? 136 GLN A N   1 
ATOM   1105 N  N   B GLN A 1 135 ? -2.607  13.177  20.845  0.50  9.93  ? 136 GLN A N   1 
ATOM   1106 C  CA  A GLN A 1 135 ? -1.573  13.701  21.747  0.50  10.96 ? 136 GLN A CA  1 
ATOM   1107 C  CA  B GLN A 1 135 ? -1.617  13.715  21.780  0.50  10.72 ? 136 GLN A CA  1 
ATOM   1108 C  C   A GLN A 1 135 ? -2.184  13.968  23.115  0.50  10.66 ? 136 GLN A C   1 
ATOM   1109 C  C   B GLN A 1 135 ? -2.119  13.762  23.192  0.50  10.83 ? 136 GLN A C   1 
ATOM   1110 O  O   A GLN A 1 135 ? -1.579  14.664  23.973  0.50  10.02 ? 136 GLN A O   1 
ATOM   1111 O  O   B GLN A 1 135 ? -1.396  14.102  24.138  0.50  10.94 ? 136 GLN A O   1 
ATOM   1112 C  CB  A GLN A 1 135 ? -0.956  15.000  21.132  0.50  12.16 ? 136 GLN A CB  1 
ATOM   1113 C  CB  B GLN A 1 135 ? -1.243  15.130  21.266  0.50  11.52 ? 136 GLN A CB  1 
ATOM   1114 C  CG  A GLN A 1 135 ? -0.185  14.794  19.822  0.50  14.31 ? 136 GLN A CG  1 
ATOM   1115 C  CG  B GLN A 1 135 ? -0.550  15.029  19.922  0.50  12.96 ? 136 GLN A CG  1 
ATOM   1116 C  CD  A GLN A 1 135 ? 1.089   13.947  19.991  0.50  15.75 ? 136 GLN A CD  1 
ATOM   1117 C  CD  B GLN A 1 135 ? -0.045  16.359  19.435  0.50  15.35 ? 136 GLN A CD  1 
ATOM   1118 O  OE1 A GLN A 1 135 ? 1.730   13.982  21.042  0.50  19.59 ? 136 GLN A OE1 1 
ATOM   1119 O  OE1 B GLN A 1 135 ? 0.741   17.031  20.115  0.50  18.29 ? 136 GLN A OE1 1 
ATOM   1120 N  NE2 A GLN A 1 135 ? 1.472   13.187  18.931  0.50  17.81 ? 136 GLN A NE2 1 
ATOM   1121 N  NE2 B GLN A 1 135 ? -0.516  16.762  18.280  0.50  15.32 ? 136 GLN A NE2 1 
ATOM   1122 N  N   . GLN A 1 136 ? -3.376  13.397  23.363  1.00  9.46  ? 137 GLN A N   1 
ATOM   1123 C  CA  . GLN A 1 136 ? -4.067  13.601  24.649  1.00  9.51  ? 137 GLN A CA  1 
ATOM   1124 C  C   . GLN A 1 136 ? -4.454  12.300  25.266  1.00  9.91  ? 137 GLN A C   1 
ATOM   1125 O  O   . GLN A 1 136 ? -4.800  11.292  24.561  1.00  8.28  ? 137 GLN A O   1 
ATOM   1126 C  CB  . GLN A 1 136 ? -5.321  14.471  24.522  1.00  10.38 ? 137 GLN A CB  1 
ATOM   1127 C  CG  . GLN A 1 136 ? -5.101  15.748  23.680  1.00  14.86 ? 137 GLN A CG  1 
ATOM   1128 C  CD  . GLN A 1 136 ? -4.161  16.706  24.378  1.00  17.41 ? 137 GLN A CD  1 
ATOM   1129 O  OE1 . GLN A 1 136 ? -4.001  16.638  25.563  1.00  17.43 ? 137 GLN A OE1 1 
ATOM   1130 N  NE2 . GLN A 1 136 ? -3.398  17.475  23.590  1.00  27.97 ? 137 GLN A NE2 1 
ATOM   1131 N  N   . PRO A 1 137 ? -4.486  12.210  26.608  1.00  8.68  ? 138 PRO A N   1 
ATOM   1132 C  CA  . PRO A 1 137 ? -4.739  10.913  27.245  1.00  9.91  ? 138 PRO A CA  1 
ATOM   1133 C  C   . PRO A 1 137 ? -6.164  10.427  27.083  1.00  9.26  ? 138 PRO A C   1 
ATOM   1134 O  O   . PRO A 1 137 ? -6.347  9.212   27.226  1.00  10.86 ? 138 PRO A O   1 
ATOM   1135 C  CB  . PRO A 1 137 ? -4.442  11.117  28.748  1.00  10.10 ? 138 PRO A CB  1 
ATOM   1136 C  CG  . PRO A 1 137 ? -4.202  12.561  28.842  1.00  12.78 ? 138 PRO A CG  1 
ATOM   1137 C  CD  . PRO A 1 137 ? -4.065  13.285  27.530  1.00  9.78  ? 138 PRO A CD  1 
ATOM   1138 N  N   . ASP A 1 138 ? -7.085  11.315  26.763  1.00  7.80  ? 139 ASP A N   1 
ATOM   1139 C  CA  . ASP A 1 138 ? -8.468  10.919  26.518  1.00  8.61  ? 139 ASP A CA  1 
ATOM   1140 C  C   . ASP A 1 138 ? -8.844  11.288  25.074  1.00  8.04  ? 139 ASP A C   1 
ATOM   1141 O  O   . ASP A 1 138 ? -9.982  11.682  24.792  1.00  8.34  ? 139 ASP A O   1 
ATOM   1142 C  CB  . ASP A 1 138 ? -9.421  11.607  27.497  1.00  9.47  ? 139 ASP A CB  1 
ATOM   1143 C  CG  . ASP A 1 138 ? -9.305  13.123  27.466  1.00  11.43 ? 139 ASP A CG  1 
ATOM   1144 O  OD1 . ASP A 1 138 ? -8.380  13.646  26.807  1.00  12.54 ? 139 ASP A OD1 1 
ATOM   1145 O  OD2 . ASP A 1 138 ? -10.146 13.790  28.108  1.00  15.97 ? 139 ASP A OD2 1 
ATOM   1146 N  N   . GLY A 1 139 ? -7.888  11.219  24.128  1.00  6.77  ? 140 GLY A N   1 
ATOM   1147 C  CA  . GLY A 1 139 ? -8.139  11.672  22.779  1.00  6.38  ? 140 GLY A CA  1 
ATOM   1148 C  C   . GLY A 1 139 ? -8.957  10.731  21.897  1.00  6.50  ? 140 GLY A C   1 
ATOM   1149 O  O   . GLY A 1 139 ? -9.684  11.204  21.019  1.00  6.10  ? 140 GLY A O   1 
ATOM   1150 N  N   . LEU A 1 140 ? -8.832  9.438   22.108  1.00  5.47  ? 141 LEU A N   1 
ATOM   1151 C  CA  . LEU A 1 140 ? -9.512  8.482   21.242  1.00  5.70  ? 141 LEU A CA  1 
ATOM   1152 C  C   . LEU A 1 140 ? -10.377 7.546   22.042  1.00  5.90  ? 141 LEU A C   1 
ATOM   1153 O  O   . LEU A 1 140 ? -10.127 7.283   23.188  1.00  6.37  ? 141 LEU A O   1 
ATOM   1154 C  CB  . LEU A 1 140 ? -8.525  7.595   20.484  1.00  5.93  ? 141 LEU A CB  1 
ATOM   1155 C  CG  . LEU A 1 140 ? -7.570  8.310   19.520  1.00  6.39  ? 141 LEU A CG  1 
ATOM   1156 C  CD1 . LEU A 1 140 ? -6.822  7.285   18.675  1.00  7.83  ? 141 LEU A CD1 1 
ATOM   1157 C  CD2 . LEU A 1 140 ? -8.198  9.279   18.516  1.00  7.35  ? 141 LEU A CD2 1 
ATOM   1158 N  N   . ALA A 1 141 ? -11.398 7.049   21.354  1.00  5.30  ? 142 ALA A N   1 
ATOM   1159 C  CA  . ALA A 1 141 ? -12.208 5.924   21.875  1.00  4.95  ? 142 ALA A CA  1 
ATOM   1160 C  C   . ALA A 1 141 ? -12.278 4.928   20.755  1.00  5.01  ? 142 ALA A C   1 
ATOM   1161 O  O   . ALA A 1 141 ? -12.654 5.273   19.655  1.00  6.06  ? 142 ALA A O   1 
ATOM   1162 C  CB  . ALA A 1 141 ? -13.610 6.342   22.322  1.00  5.63  ? 142 ALA A CB  1 
ATOM   1163 N  N   . VAL A 1 142 ? -11.786 3.694   21.055  1.00  5.18  ? 143 VAL A N   1 
ATOM   1164 C  CA  . VAL A 1 142 ? -11.788 2.652   20.021  1.00  5.25  ? 143 VAL A CA  1 
ATOM   1165 C  C   . VAL A 1 142 ? -12.770 1.590   20.479  1.00  5.33  ? 143 VAL A C   1 
ATOM   1166 O  O   . VAL A 1 142 ? -12.659 1.039   21.572  1.00  5.32  ? 143 VAL A O   1 
ATOM   1167 C  CB  . VAL A 1 142 ? -10.383 2.042   19.678  1.00  5.37  ? 143 VAL A CB  1 
ATOM   1168 C  CG1 . VAL A 1 142 ? -10.580 1.048   18.497  1.00  5.38  ? 143 VAL A CG1 1 
ATOM   1169 C  CG2 . VAL A 1 142 ? -9.456  3.176   19.207  1.00  6.26  ? 143 VAL A CG2 1 
ATOM   1170 N  N   . LEU A 1 143 ? -13.759 1.297   19.582  1.00  4.94  ? 144 LEU A N   1 
ATOM   1171 C  CA  . LEU A 1 143 ? -14.726 0.238   19.856  1.00  5.60  ? 144 LEU A CA  1 
ATOM   1172 C  C   . LEU A 1 143 ? -14.182 -0.997  19.165  1.00  6.08  ? 144 LEU A C   1 
ATOM   1173 O  O   . LEU A 1 143 ? -14.024 -1.045  17.946  1.00  6.47  ? 144 LEU A O   1 
ATOM   1174 C  CB  . LEU A 1 143 ? -16.105 0.684   19.303  1.00  6.00  ? 144 LEU A CB  1 
ATOM   1175 C  CG  . LEU A 1 143 ? -17.254 -0.318  19.447  1.00  6.90  ? 144 LEU A CG  1 
ATOM   1176 C  CD1 . LEU A 1 143 ? -17.500 -0.680  20.888  1.00  7.65  ? 144 LEU A CD1 1 
ATOM   1177 C  CD2 . LEU A 1 143 ? -18.533 0.259   18.824  1.00  7.98  ? 144 LEU A CD2 1 
ATOM   1178 N  N   . GLY A 1 144 ? -13.910 -2.012  20.010  1.00  5.35  ? 145 GLY A N   1 
ATOM   1179 C  CA  . GLY A 1 144 ? -13.347 -3.258  19.505  1.00  4.68  ? 145 GLY A CA  1 
ATOM   1180 C  C   . GLY A 1 144 ? -14.394 -4.363  19.511  1.00  4.72  ? 145 GLY A C   1 
ATOM   1181 O  O   . GLY A 1 144 ? -15.134 -4.523  20.508  1.00  5.47  ? 145 GLY A O   1 
ATOM   1182 N  N   . ILE A 1 145 ? -14.438 -5.121  18.385  1.00  4.69  ? 146 ILE A N   1 
ATOM   1183 C  CA  . ILE A 1 145 ? -15.499 -6.165  18.285  1.00  4.83  ? 146 ILE A CA  1 
ATOM   1184 C  C   . ILE A 1 145 ? -14.766 -7.396  17.753  1.00  4.79  ? 146 ILE A C   1 
ATOM   1185 O  O   . ILE A 1 145 ? -14.092 -7.361  16.731  1.00  5.09  ? 146 ILE A O   1 
ATOM   1186 C  CB  . ILE A 1 145 ? -16.607 -5.684  17.272  1.00  5.54  ? 146 ILE A CB  1 
ATOM   1187 C  CG1 . ILE A 1 145 ? -17.204 -4.388  17.757  1.00  6.49  ? 146 ILE A CG1 1 
ATOM   1188 C  CG2 . ILE A 1 145 ? -17.676 -6.769  17.118  1.00  6.65  ? 146 ILE A CG2 1 
ATOM   1189 C  CD1 . ILE A 1 145 ? -18.308 -3.755  16.845  1.00  6.05  ? 146 ILE A CD1 1 
ATOM   1190 N  N   . PHE A 1 146 ? -14.962 -8.503  18.460  1.00  5.11  ? 147 PHE A N   1 
ATOM   1191 C  CA  . PHE A 1 146 ? -14.332 -9.777  17.997  1.00  5.62  ? 147 PHE A CA  1 
ATOM   1192 C  C   . PHE A 1 146 ? -15.071 -10.417 16.855  1.00  6.23  ? 147 PHE A C   1 
ATOM   1193 O  O   . PHE A 1 146 ? -16.308 -10.295 16.754  1.00  7.09  ? 147 PHE A O   1 
ATOM   1194 C  CB  . PHE A 1 146 ? -14.327 -10.746 19.175  1.00  5.11  ? 147 PHE A CB  1 
ATOM   1195 C  CG  . PHE A 1 146 ? -13.488 -10.260 20.303  1.00  4.49  ? 147 PHE A CG  1 
ATOM   1196 C  CD1 . PHE A 1 146 ? -12.104 -10.122 20.103  1.00  5.22  ? 147 PHE A CD1 1 
ATOM   1197 C  CD2 . PHE A 1 146 ? -14.018 -10.025 21.558  1.00  5.09  ? 147 PHE A CD2 1 
ATOM   1198 C  CE1 . PHE A 1 146 ? -11.290 -9.739  21.174  1.00  4.92  ? 147 PHE A CE1 1 
ATOM   1199 C  CE2 . PHE A 1 146 ? -13.227 -9.596  22.606  1.00  5.27  ? 147 PHE A CE2 1 
ATOM   1200 C  CZ  . PHE A 1 146 ? -11.850 -9.523  22.414  1.00  5.57  ? 147 PHE A CZ  1 
ATOM   1201 N  N   . LEU A 1 147 ? -14.333 -11.063 15.983  1.00  6.21  ? 148 LEU A N   1 
ATOM   1202 C  CA  . LEU A 1 147 ? -14.992 -11.892 14.896  1.00  6.05  ? 148 LEU A CA  1 
ATOM   1203 C  C   . LEU A 1 147 ? -14.614 -13.347 15.115  1.00  7.22  ? 148 LEU A C   1 
ATOM   1204 O  O   . LEU A 1 147 ? -13.439 -13.711 15.296  1.00  7.12  ? 148 LEU A O   1 
ATOM   1205 C  CB  . LEU A 1 147 ? -14.377 -11.490 13.514  1.00  7.37  ? 148 LEU A CB  1 
ATOM   1206 C  CG  . LEU A 1 147 ? -14.953 -10.215 12.864  1.00  6.81  ? 148 LEU A CG  1 
ATOM   1207 C  CD1 . LEU A 1 147 ? -14.645 -8.929  13.691  1.00  8.05  ? 148 LEU A CD1 1 
ATOM   1208 C  CD2 . LEU A 1 147 ? -14.350 -10.044 11.499  1.00  7.37  ? 148 LEU A CD2 1 
ATOM   1209 N  N   . LYS A 1 148 ? -15.660 -14.178 15.099  1.00  7.42  ? 149 LYS A N   1 
ATOM   1210 C  CA  . LYS A 1 148 ? -15.477 -15.625 15.040  1.00  7.82  ? 149 LYS A CA  1 
ATOM   1211 C  C   . LYS A 1 148 ? -15.972 -16.144 13.685  1.00  9.35  ? 149 LYS A C   1 
ATOM   1212 O  O   . LYS A 1 148 ? -16.801 -15.522 13.030  1.00  8.69  ? 149 LYS A O   1 
ATOM   1213 C  CB  . LYS A 1 148 ? -16.223 -16.348 16.183  1.00  9.43  ? 149 LYS A CB  1 
ATOM   1214 C  CG  . LYS A 1 148 ? -17.752 -16.216 16.085  1.00  12.02 ? 149 LYS A CG  1 
ATOM   1215 C  CD  . LYS A 1 148 ? -18.330 -16.967 17.286  1.00  18.94 ? 149 LYS A CD  1 
ATOM   1216 C  CE  . LYS A 1 148 ? -19.829 -16.764 17.290  1.00  22.34 ? 149 LYS A CE  1 
ATOM   1217 N  NZ  . LYS A 1 148 ? -20.460 -17.719 18.275  1.00  31.15 ? 149 LYS A NZ  1 
ATOM   1218 N  N   . VAL A 1 149 ? -15.479 -17.286 13.286  1.00  9.67  ? 150 VAL A N   1 
ATOM   1219 C  CA  . VAL A 1 149 ? -15.874 -17.839 12.010  1.00  9.85  ? 150 VAL A CA  1 
ATOM   1220 C  C   . VAL A 1 149 ? -17.082 -18.795 12.211  1.00  9.96  ? 150 VAL A C   1 
ATOM   1221 O  O   . VAL A 1 149 ? -17.027 -19.774 12.997  1.00  11.83 ? 150 VAL A O   1 
ATOM   1222 C  CB  . VAL A 1 149 ? -14.687 -18.616 11.379  1.00  9.92  ? 150 VAL A CB  1 
ATOM   1223 C  CG1 . VAL A 1 149 ? -15.178 -19.351 10.112  1.00  12.51 ? 150 VAL A CG1 1 
ATOM   1224 C  CG2 . VAL A 1 149 ? -13.568 -17.652 11.007  1.00  11.83 ? 150 VAL A CG2 1 
ATOM   1225 N  N   . GLY A 1 150 ? -18.078 -18.568 11.401  1.00  9.16  ? 151 GLY A N   1 
ATOM   1226 C  CA  . GLY A 1 150 ? -19.350 -19.343 11.516  1.00  9.75  ? 151 GLY A CA  1 
ATOM   1227 C  C   . GLY A 1 150 ? -20.214 -18.917 10.342  1.00  8.75  ? 151 GLY A C   1 
ATOM   1228 O  O   . GLY A 1 150 ? -19.811 -19.016 9.194   1.00  9.88  ? 151 GLY A O   1 
ATOM   1229 N  N   A SER A 1 151 ? -21.442 -18.450 10.668  0.50  10.84 ? 152 SER A N   1 
ATOM   1230 N  N   B SER A 1 151 ? -21.392 -18.385 10.724  0.50  10.47 ? 152 SER A N   1 
ATOM   1231 C  CA  A SER A 1 151 ? -22.390 -17.915 9.619   0.50  11.24 ? 152 SER A CA  1 
ATOM   1232 C  CA  B SER A 1 151 ? -22.305 -17.717 9.759   0.50  10.76 ? 152 SER A CA  1 
ATOM   1233 C  C   A SER A 1 151 ? -21.865 -16.573 9.142   0.50  11.03 ? 152 SER A C   1 
ATOM   1234 C  C   B SER A 1 151 ? -21.645 -16.495 9.064   0.50  10.91 ? 152 SER A C   1 
ATOM   1235 O  O   A SER A 1 151 ? -21.239 -15.913 9.979   0.50  9.57  ? 152 SER A O   1 
ATOM   1236 O  O   B SER A 1 151 ? -20.759 -15.804 9.599   0.50  9.35  ? 152 SER A O   1 
ATOM   1237 C  CB  A SER A 1 151 ? -23.777 -17.736 10.173  0.50  14.34 ? 152 SER A CB  1 
ATOM   1238 C  CB  B SER A 1 151 ? -23.594 -17.339 10.443  0.50  12.78 ? 152 SER A CB  1 
ATOM   1239 O  OG  A SER A 1 151 ? -23.728 -16.761 11.201  0.50  15.52 ? 152 SER A OG  1 
ATOM   1240 O  OG  B SER A 1 151 ? -24.168 -18.510 11.027  0.50  15.64 ? 152 SER A OG  1 
ATOM   1241 N  N   . ALA A 1 152 ? -22.049 -16.220 7.842   1.00  10.51 ? 153 ALA A N   1 
ATOM   1242 C  CA  . ALA A 1 152 ? -21.635 -14.965 7.235   1.00  10.30 ? 153 ALA A CA  1 
ATOM   1243 C  C   . ALA A 1 152 ? -22.270 -13.768 7.936   1.00  10.30 ? 153 ALA A C   1 
ATOM   1244 O  O   . ALA A 1 152 ? -23.342 -13.858 8.525   1.00  12.31 ? 153 ALA A O   1 
ATOM   1245 C  CB  . ALA A 1 152 ? -22.047 -14.940 5.717   1.00  12.66 ? 153 ALA A CB  1 
ATOM   1246 N  N   . LYS A 1 153 ? -21.532 -12.634 7.886   1.00  11.40 ? 154 LYS A N   1 
ATOM   1247 C  CA  . LYS A 1 153 ? -22.066 -11.357 8.304   1.00  11.12 ? 154 LYS A CA  1 
ATOM   1248 C  C   . LYS A 1 153 ? -22.464 -10.569 7.073   1.00  10.89 ? 154 LYS A C   1 
ATOM   1249 O  O   . LYS A 1 153 ? -21.654 -10.162 6.304   1.00  10.62 ? 154 LYS A O   1 
ATOM   1250 C  CB  . LYS A 1 153 ? -21.016 -10.579 9.165   1.00  12.21 ? 154 LYS A CB  1 
ATOM   1251 C  CG  . LYS A 1 153 ? -21.572 -9.377  9.911   1.00  13.08 ? 154 LYS A CG  1 
ATOM   1252 C  CD  . LYS A 1 153 ? -22.435 -9.804  11.047  1.00  13.99 ? 154 LYS A CD  1 
ATOM   1253 C  CE  . LYS A 1 153 ? -22.738 -8.614  11.949  1.00  16.39 ? 154 LYS A CE  1 
ATOM   1254 N  NZ  . LYS A 1 153 ? -23.593 -9.031  13.026  1.00  21.04 ? 154 LYS A NZ  1 
ATOM   1255 N  N   . PRO A 1 154 ? -23.785 -10.505 6.828   1.00  11.83 ? 155 PRO A N   1 
ATOM   1256 C  CA  . PRO A 1 154 ? -24.162 -9.908  5.505   1.00  13.25 ? 155 PRO A CA  1 
ATOM   1257 C  C   . PRO A 1 154 ? -23.729 -8.461  5.349   1.00  11.85 ? 155 PRO A C   1 
ATOM   1258 O  O   . PRO A 1 154 ? -23.254 -8.073  4.293   1.00  13.97 ? 155 PRO A O   1 
ATOM   1259 C  CB  . PRO A 1 154 ? -25.705 -10.025 5.512   1.00  13.92 ? 155 PRO A CB  1 
ATOM   1260 C  CG  . PRO A 1 154 ? -25.980 -11.113 6.467   1.00  15.06 ? 155 PRO A CG  1 
ATOM   1261 C  CD  . PRO A 1 154 ? -24.953 -11.000 7.572   1.00  13.57 ? 155 PRO A CD  1 
ATOM   1262 N  N   . GLY A 1 155 ? -23.644 -7.776  6.481   1.00  10.87 ? 156 GLY A N   1 
ATOM   1263 C  CA  . GLY A 1 155 ? -23.282 -6.356  6.474   1.00  11.33 ? 156 GLY A CA  1 
ATOM   1264 C  C   . GLY A 1 155 ? -21.813 -6.130  6.236   1.00  12.72 ? 156 GLY A C   1 
ATOM   1265 O  O   . GLY A 1 155 ? -21.348 -4.977  6.021   1.00  16.15 ? 156 GLY A O   1 
ATOM   1266 N  N   . LEU A 1 156 ? -21.047 -7.203  6.356   1.00  10.67 ? 157 LEU A N   1 
ATOM   1267 C  CA  . LEU A 1 156 ? -19.632 -7.220  5.932   1.00  10.23 ? 157 LEU A CA  1 
ATOM   1268 C  C   . LEU A 1 156 ? -19.289 -7.412  4.475   1.00  10.17 ? 157 LEU A C   1 
ATOM   1269 O  O   . LEU A 1 156 ? -18.156 -7.130  3.956   1.00  9.63  ? 157 LEU A O   1 
ATOM   1270 C  CB  . LEU A 1 156 ? -18.797 -8.222  6.806   1.00  10.85 ? 157 LEU A CB  1 
ATOM   1271 C  CG  . LEU A 1 156 ? -17.298 -8.341  6.628   1.00  10.27 ? 157 LEU A CG  1 
ATOM   1272 C  CD1 . LEU A 1 156 ? -16.544 -7.027  6.985   1.00  9.73  ? 157 LEU A CD1 1 
ATOM   1273 C  CD2 . LEU A 1 156 ? -16.704 -9.479  7.475   1.00  11.01 ? 157 LEU A CD2 1 
ATOM   1274 N  N   . GLN A 1 157 ? -20.287 -7.959  3.710   1.00  10.90 ? 158 GLN A N   1 
ATOM   1275 C  CA  . GLN A 1 157 ? -19.947 -8.388  2.411   1.00  12.15 ? 158 GLN A CA  1 
ATOM   1276 C  C   . GLN A 1 157 ? -19.551 -7.280  1.428   1.00  10.19 ? 158 GLN A C   1 
ATOM   1277 O  O   . GLN A 1 157 ? -18.650 -7.512  0.649   1.00  11.77 ? 158 GLN A O   1 
ATOM   1278 C  CB  . GLN A 1 157 ? -21.066 -9.240  1.832   1.00  12.43 ? 158 GLN A CB  1 
ATOM   1279 C  CG  . GLN A 1 157 ? -20.639 -9.903  0.515   1.00  13.93 ? 158 GLN A CG  1 
ATOM   1280 C  CD  . GLN A 1 157 ? -19.530 -10.961 0.715   1.00  12.71 ? 158 GLN A CD  1 
ATOM   1281 O  OE1 . GLN A 1 157 ? -19.426 -11.542 1.846   1.00  15.18 ? 158 GLN A OE1 1 
ATOM   1282 N  NE2 . GLN A 1 157 ? -18.675 -11.201 -0.293  1.00  15.36 ? 158 GLN A NE2 1 
ATOM   1283 N  N   . LYS A 1 158 ? -20.137 -6.073  1.563   1.00  12.56 ? 159 LYS A N   1 
ATOM   1284 C  CA  . LYS A 1 158 ? -19.684 -4.991  0.712   1.00  13.10 ? 159 LYS A CA  1 
ATOM   1285 C  C   . LYS A 1 158 ? -18.165 -4.669  0.873   1.00  12.53 ? 159 LYS A C   1 
ATOM   1286 O  O   . LYS A 1 158 ? -17.537 -4.307  -0.057  1.00  14.45 ? 159 LYS A O   1 
ATOM   1287 C  CB  . LYS A 1 158 ? -20.609 -3.767  0.933   1.00  17.52 ? 159 LYS A CB  1 
ATOM   1288 C  CG  . LYS A 1 158 ? -20.208 -2.419  0.267   1.00  25.19 ? 159 LYS A CG  1 
ATOM   1289 C  CD  . LYS A 1 158 ? -20.138 -2.418  -1.287  1.00  31.92 ? 159 LYS A CD  1 
ATOM   1290 C  CE  . LYS A 1 158 ? -19.848 -1.043  -1.953  1.00  29.14 ? 159 LYS A CE  1 
ATOM   1291 N  NZ  . LYS A 1 158 ? -21.004 -0.084  -1.805  1.00  30.44 ? 159 LYS A NZ  1 
ATOM   1292 N  N   . VAL A 1 159 ? -17.623 -4.766  2.114   1.00  12.66 ? 160 VAL A N   1 
ATOM   1293 C  CA  . VAL A 1 159 ? -16.212 -4.568  2.337   1.00  11.65 ? 160 VAL A CA  1 
ATOM   1294 C  C   . VAL A 1 159 ? -15.420 -5.693  1.667   1.00  11.24 ? 160 VAL A C   1 
ATOM   1295 O  O   . VAL A 1 159 ? -14.470 -5.470  0.921   1.00  12.20 ? 160 VAL A O   1 
ATOM   1296 C  CB  . VAL A 1 159 ? -15.933 -4.602  3.839   1.00  12.20 ? 160 VAL A CB  1 
ATOM   1297 C  CG1 . VAL A 1 159 ? -14.447 -4.644  4.151   1.00  12.65 ? 160 VAL A CG1 1 
ATOM   1298 C  CG2 . VAL A 1 159 ? -16.621 -3.428  4.508   1.00  13.82 ? 160 VAL A CG2 1 
ATOM   1299 N  N   . VAL A 1 160 ? -15.824 -6.968  1.925   1.00  11.61 ? 161 VAL A N   1 
ATOM   1300 C  CA  . VAL A 1 160 ? -15.064 -8.086  1.367   1.00  13.45 ? 161 VAL A CA  1 
ATOM   1301 C  C   . VAL A 1 160 ? -15.030 -8.036  -0.162  1.00  12.24 ? 161 VAL A C   1 
ATOM   1302 O  O   . VAL A 1 160 ? -13.992 -8.291  -0.739  1.00  13.37 ? 161 VAL A O   1 
ATOM   1303 C  CB  . VAL A 1 160 ? -15.720 -9.453  1.836   1.00  16.16 ? 161 VAL A CB  1 
ATOM   1304 C  CG1 . VAL A 1 160 ? -15.305 -10.647 0.936   1.00  18.15 ? 161 VAL A CG1 1 
ATOM   1305 C  CG2 . VAL A 1 160 ? -15.389 -9.639  3.321   1.00  15.88 ? 161 VAL A CG2 1 
ATOM   1306 N  N   . ASP A 1 161 ? -16.142 -7.589  -0.753  1.00  13.87 ? 162 ASP A N   1 
ATOM   1307 C  CA  . ASP A 1 161 ? -16.193 -7.616  -2.248  1.00  17.43 ? 162 ASP A CA  1 
ATOM   1308 C  C   . ASP A 1 161 ? -15.325 -6.571  -2.942  1.00  18.55 ? 162 ASP A C   1 
ATOM   1309 O  O   . ASP A 1 161 ? -14.942 -6.773  -4.098  1.00  20.87 ? 162 ASP A O   1 
ATOM   1310 C  CB  . ASP A 1 161 ? -17.601 -7.517  -2.695  1.00  17.85 ? 162 ASP A CB  1 
ATOM   1311 C  CG  . ASP A 1 161 ? -18.302 -8.873  -2.699  1.00  19.01 ? 162 ASP A CG  1 
ATOM   1312 O  OD1 . ASP A 1 161 ? -17.625 -9.916  -2.774  1.00  21.33 ? 162 ASP A OD1 1 
ATOM   1313 O  OD2 . ASP A 1 161 ? -19.526 -8.833  -2.603  1.00  21.15 ? 162 ASP A OD2 1 
ATOM   1314 N  N   . VAL A 1 162 ? -14.938 -5.492  -2.234  1.00  15.66 ? 163 VAL A N   1 
ATOM   1315 C  CA  . VAL A 1 162 ? -14.061 -4.439  -2.815  1.00  16.59 ? 163 VAL A CA  1 
ATOM   1316 C  C   . VAL A 1 162 ? -12.534 -4.716  -2.640  1.00  14.63 ? 163 VAL A C   1 
ATOM   1317 O  O   . VAL A 1 162 ? -11.638 -4.069  -3.185  1.00  15.10 ? 163 VAL A O   1 
ATOM   1318 C  CB  . VAL A 1 162 ? -14.506 -3.086  -2.208  1.00  18.37 ? 163 VAL A CB  1 
ATOM   1319 C  CG1 . VAL A 1 162 ? -13.834 -2.807  -0.893  1.00  16.55 ? 163 VAL A CG1 1 
ATOM   1320 C  CG2 . VAL A 1 162 ? -14.311 -1.865  -3.124  1.00  19.60 ? 163 VAL A CG2 1 
ATOM   1321 N  N   . LEU A 1 163 ? -12.161 -5.707  -1.820  1.00  14.10 ? 164 LEU A N   1 
ATOM   1322 C  CA  . LEU A 1 163 ? -10.769 -5.937  -1.406  1.00  12.92 ? 164 LEU A CA  1 
ATOM   1323 C  C   . LEU A 1 163 ? -9.839  -6.279  -2.577  1.00  14.26 ? 164 LEU A C   1 
ATOM   1324 O  O   . LEU A 1 163 ? -8.705  -5.940  -2.563  1.00  15.57 ? 164 LEU A O   1 
ATOM   1325 C  CB  . LEU A 1 163 ? -10.598 -6.997  -0.273  1.00  13.53 ? 164 LEU A CB  1 
ATOM   1326 C  CG  . LEU A 1 163 ? -11.374 -6.656  1.019   1.00  12.11 ? 164 LEU A CG  1 
ATOM   1327 C  CD1 . LEU A 1 163 ? -11.190 -7.840  1.995   1.00  12.18 ? 164 LEU A CD1 1 
ATOM   1328 C  CD2 . LEU A 1 163 ? -10.793 -5.367  1.605   1.00  10.56 ? 164 LEU A CD2 1 
ATOM   1329 N  N   . ASP A 1 164 ? -10.398 -6.998  -3.554  1.00  18.81 ? 165 ASP A N   1 
ATOM   1330 C  CA  . ASP A 1 164 ? -9.603  -7.261  -4.722  1.00  20.23 ? 165 ASP A CA  1 
ATOM   1331 C  C   . ASP A 1 164 ? -9.182  -5.968  -5.476  1.00  20.08 ? 165 ASP A C   1 
ATOM   1332 O  O   . ASP A 1 164 ? -8.182  -6.010  -6.190  1.00  23.14 ? 165 ASP A O   1 
ATOM   1333 C  CB  . ASP A 1 164 ? -10.423 -8.194  -5.647  1.00  20.29 ? 165 ASP A CB  1 
ATOM   1334 C  CG  . ASP A 1 164 ? -11.330 -7.460  -6.473  1.00  23.11 ? 165 ASP A CG  1 
ATOM   1335 O  OD1 . ASP A 1 164 ? -12.349 -6.952  -5.948  1.00  23.87 ? 165 ASP A OD1 1 
ATOM   1336 O  OD2 . ASP A 1 164 ? -10.994 -7.296  -7.685  1.00  29.84 ? 165 ASP A OD2 1 
ATOM   1337 N  N   . SER A 1 165 ? -9.875  -4.844  -5.277  1.00  18.05 ? 166 SER A N   1 
ATOM   1338 C  CA  . SER A 1 165 ? -9.458  -3.570  -5.921  1.00  18.83 ? 166 SER A CA  1 
ATOM   1339 C  C   . SER A 1 165 ? -8.374  -2.847  -5.127  1.00  21.12 ? 166 SER A C   1 
ATOM   1340 O  O   . SER A 1 165 ? -7.743  -1.902  -5.637  1.00  20.03 ? 166 SER A O   1 
ATOM   1341 C  CB  . SER A 1 165 ? -10.652 -2.652  -6.118  1.00  21.95 ? 166 SER A CB  1 
ATOM   1342 O  OG  . SER A 1 165 ? -11.140 -2.123  -4.916  1.00  24.45 ? 166 SER A OG  1 
ATOM   1343 N  N   . ILE A 1 166 ? -8.144  -3.266  -3.865  1.00  15.52 ? 167 ILE A N   1 
ATOM   1344 C  CA  . ILE A 1 166 ? -7.076  -2.659  -3.059  1.00  13.93 ? 167 ILE A CA  1 
ATOM   1345 C  C   . ILE A 1 166 ? -6.083  -3.695  -2.526  1.00  13.68 ? 167 ILE A C   1 
ATOM   1346 O  O   . ILE A 1 166 ? -5.667  -3.714  -1.350  1.00  13.03 ? 167 ILE A O   1 
ATOM   1347 C  CB  . ILE A 1 166 ? -7.686  -1.786  -1.893  1.00  13.28 ? 167 ILE A CB  1 
ATOM   1348 C  CG1 . ILE A 1 166 ? -8.588  -2.634  -1.017  1.00  14.02 ? 167 ILE A CG1 1 
ATOM   1349 C  CG2 . ILE A 1 166 ? -8.485  -0.617  -2.461  1.00  15.29 ? 167 ILE A CG2 1 
ATOM   1350 C  CD1 . ILE A 1 166 ? -8.485  -2.139  0.419   1.00  15.84 ? 167 ILE A CD1 1 
ATOM   1351 N  N   . LYS A 1 167 ? -5.684  -4.617  -3.394  1.00  13.60 ? 168 LYS A N   1 
ATOM   1352 C  CA  . LYS A 1 167 ? -4.840  -5.666  -3.004  1.00  13.46 ? 168 LYS A CA  1 
ATOM   1353 C  C   . LYS A 1 167 ? -3.533  -5.295  -2.376  1.00  15.05 ? 168 LYS A C   1 
ATOM   1354 O  O   . LYS A 1 167 ? -3.144  -5.951  -1.407  1.00  13.24 ? 168 LYS A O   1 
ATOM   1355 C  CB  . LYS A 1 167 ? -4.575  -6.566  -4.230  1.00  14.91 ? 168 LYS A CB  1 
ATOM   1356 C  CG  . LYS A 1 167 ? -3.834  -7.823  -3.848  1.00  15.97 ? 168 LYS A CG  1 
ATOM   1357 C  CD  . LYS A 1 167 ? -3.335  -8.582  -5.123  1.00  22.59 ? 168 LYS A CD  1 
ATOM   1358 C  CE  . LYS A 1 167 ? -2.721  -9.921  -4.771  1.00  28.87 ? 168 LYS A CE  1 
ATOM   1359 N  NZ  . LYS A 1 167 ? -2.642  -10.842 -5.970  1.00  33.49 ? 168 LYS A NZ  1 
ATOM   1360 N  N   . THR A 1 168 ? -2.853  -4.233  -2.870  1.00  13.23 ? 169 THR A N   1 
ATOM   1361 C  CA  . THR A 1 168 ? -1.486  -3.959  -2.465  1.00  14.11 ? 169 THR A CA  1 
ATOM   1362 C  C   . THR A 1 168 ? -1.417  -2.571  -1.782  1.00  11.42 ? 169 THR A C   1 
ATOM   1363 O  O   . THR A 1 168 ? -2.306  -1.752  -1.906  1.00  16.23 ? 169 THR A O   1 
ATOM   1364 C  CB  . THR A 1 168 ? -0.568  -3.948  -3.737  1.00  15.30 ? 169 THR A CB  1 
ATOM   1365 O  OG1 . THR A 1 168 ? -1.322  -3.210  -4.718  1.00  18.92 ? 169 THR A OG1 1 
ATOM   1366 C  CG2 . THR A 1 168 ? -0.288  -5.408  -4.091  1.00  16.27 ? 169 THR A CG2 1 
ATOM   1367 N  N   . LYS A 1 169 ? -0.367  -2.401  -1.003  1.00  15.38 ? 170 LYS A N   1 
ATOM   1368 C  CA  . LYS A 1 169 ? -0.096  -1.199  -0.246  1.00  15.30 ? 170 LYS A CA  1 
ATOM   1369 C  C   . LYS A 1 169 ? -0.270  0.118   -1.002  1.00  16.01 ? 170 LYS A C   1 
ATOM   1370 O  O   . LYS A 1 169 ? 0.227   0.218   -2.147  1.00  20.51 ? 170 LYS A O   1 
ATOM   1371 C  CB  . LYS A 1 169 ? 1.299   -1.378  0.305   1.00  15.19 ? 170 LYS A CB  1 
ATOM   1372 C  CG  . LYS A 1 169 ? 1.792   -0.187  1.146   1.00  18.39 ? 170 LYS A CG  1 
ATOM   1373 C  CD  . LYS A 1 169 ? 3.126   -0.554  1.754   1.00  22.24 ? 170 LYS A CD  1 
ATOM   1374 C  CE  . LYS A 1 169 ? 3.826   0.582   2.456   1.00  31.51 ? 170 LYS A CE  1 
ATOM   1375 N  NZ  . LYS A 1 169 ? 5.239   0.541   1.966   1.00  39.64 ? 170 LYS A NZ  1 
ATOM   1376 N  N   . GLY A 1 170 ? -0.989  1.062   -0.453  1.00  18.70 ? 171 GLY A N   1 
ATOM   1377 C  CA  . GLY A 1 170 ? -1.234  2.332   -1.154  1.00  18.52 ? 171 GLY A CA  1 
ATOM   1378 C  C   . GLY A 1 170 ? -2.378  2.353   -2.126  1.00  20.74 ? 171 GLY A C   1 
ATOM   1379 O  O   . GLY A 1 170 ? -2.820  3.454   -2.572  1.00  22.69 ? 171 GLY A O   1 
ATOM   1380 N  N   . LYS A 1 171 ? -2.947  1.194   -2.473  1.00  16.69 ? 172 LYS A N   1 
ATOM   1381 C  CA  . LYS A 1 171 ? -4.208  1.272   -3.170  1.00  16.29 ? 172 LYS A CA  1 
ATOM   1382 C  C   . LYS A 1 171 ? -5.416  1.771   -2.418  1.00  16.79 ? 172 LYS A C   1 
ATOM   1383 O  O   . LYS A 1 171 ? -5.669  1.339   -1.280  1.00  17.07 ? 172 LYS A O   1 
ATOM   1384 C  CB  . LYS A 1 171 ? -4.546  -0.040  -3.869  1.00  18.05 ? 172 LYS A CB  1 
ATOM   1385 C  CG  . LYS A 1 171 ? -3.429  -0.522  -4.805  1.00  20.44 ? 172 LYS A CG  1 
ATOM   1386 C  CD  . LYS A 1 171 ? -3.783  -1.705  -5.703  1.00  27.15 ? 172 LYS A CD  1 
ATOM   1387 C  CE  . LYS A 1 171 ? -4.019  -1.328  -7.157  1.00  32.17 ? 172 LYS A CE  1 
ATOM   1388 N  NZ  . LYS A 1 171 ? -5.188  -2.097  -7.725  1.00  34.55 ? 172 LYS A NZ  1 
ATOM   1389 N  N   . SER A 1 172 ? -6.257  2.561   -3.023  1.00  14.78 ? 173 SER A N   1 
ATOM   1390 C  CA  . SER A 1 172 ? -7.543  2.927   -2.497  1.00  16.01 ? 173 SER A CA  1 
ATOM   1391 C  C   . SER A 1 172 ? -8.687  2.864   -3.508  1.00  16.87 ? 173 SER A C   1 
ATOM   1392 O  O   . SER A 1 172 ? -8.500  2.842   -4.767  1.00  18.30 ? 173 SER A O   1 
ATOM   1393 C  CB  . SER A 1 172 ? -7.544  4.353   -1.896  1.00  19.29 ? 173 SER A CB  1 
ATOM   1394 O  OG  . SER A 1 172 ? -7.291  5.310   -2.951  1.00  21.55 ? 173 SER A OG  1 
ATOM   1395 N  N   . ALA A 1 173 ? -9.881  2.870   -3.000  1.00  17.40 ? 174 ALA A N   1 
ATOM   1396 C  CA  . ALA A 1 173 ? -11.079 2.866   -3.794  1.00  18.07 ? 174 ALA A CA  1 
ATOM   1397 C  C   . ALA A 1 173 ? -12.205 3.671   -3.166  1.00  21.33 ? 174 ALA A C   1 
ATOM   1398 O  O   . ALA A 1 173 ? -12.463 3.658   -1.930  1.00  15.61 ? 174 ALA A O   1 
ATOM   1399 C  CB  . ALA A 1 173 ? -11.517 1.451   -4.081  1.00  19.30 ? 174 ALA A CB  1 
ATOM   1400 N  N   . ASP A 1 174 ? -12.952 4.386   -3.983  1.00  21.32 ? 175 ASP A N   1 
ATOM   1401 C  CA  . ASP A 1 174 ? -14.205 4.933   -3.519  1.00  23.80 ? 175 ASP A CA  1 
ATOM   1402 C  C   . ASP A 1 174 ? -15.049 3.912   -2.732  1.00  22.33 ? 175 ASP A C   1 
ATOM   1403 O  O   . ASP A 1 174 ? -15.252 2.728   -3.107  1.00  21.04 ? 175 ASP A O   1 
ATOM   1404 C  CB  . ASP A 1 174 ? -15.051 5.538   -4.677  1.00  27.79 ? 175 ASP A CB  1 
ATOM   1405 C  CG  . ASP A 1 174 ? -14.281 6.567   -5.467  1.00  38.67 ? 175 ASP A CG  1 
ATOM   1406 O  OD1 . ASP A 1 174 ? -13.523 7.378   -4.872  1.00  37.25 ? 175 ASP A OD1 1 
ATOM   1407 O  OD2 . ASP A 1 174 ? -14.427 6.567   -6.719  1.00  43.88 ? 175 ASP A OD2 1 
ATOM   1408 N  N   . PHE A 1 175 ? -15.587 4.384   -1.612  1.00  17.65 ? 176 PHE A N   1 
ATOM   1409 C  CA  . PHE A 1 175 ? -16.361 3.457   -0.783  1.00  14.68 ? 176 PHE A CA  1 
ATOM   1410 C  C   . PHE A 1 175 ? -17.416 4.202   -0.058  1.00  16.94 ? 176 PHE A C   1 
ATOM   1411 O  O   . PHE A 1 175 ? -17.284 4.490   1.137   1.00  17.38 ? 176 PHE A O   1 
ATOM   1412 C  CB  . PHE A 1 175 ? -15.411 2.641   0.150   1.00  15.24 ? 176 PHE A CB  1 
ATOM   1413 C  CG  . PHE A 1 175 ? -16.010 1.369   0.664   1.00  16.42 ? 176 PHE A CG  1 
ATOM   1414 C  CD1 . PHE A 1 175 ? -16.365 0.325   -0.179  1.00  14.67 ? 176 PHE A CD1 1 
ATOM   1415 C  CD2 . PHE A 1 175 ? -16.272 1.217   1.984   1.00  15.65 ? 176 PHE A CD2 1 
ATOM   1416 C  CE1 . PHE A 1 175 ? -16.922 -0.836  0.333   1.00  16.41 ? 176 PHE A CE1 1 
ATOM   1417 C  CE2 . PHE A 1 175 ? -16.864 0.084   2.514   1.00  16.24 ? 176 PHE A CE2 1 
ATOM   1418 C  CZ  . PHE A 1 175 ? -17.171 -0.974  1.681   1.00  14.95 ? 176 PHE A CZ  1 
ATOM   1419 N  N   . THR A 1 176 ? -18.436 4.627   -0.765  1.00  13.86 ? 177 THR A N   1 
ATOM   1420 C  CA  . THR A 1 176 ? -19.504 5.421   -0.242  1.00  14.59 ? 177 THR A CA  1 
ATOM   1421 C  C   . THR A 1 176 ? -20.710 4.630   0.220   1.00  11.45 ? 177 THR A C   1 
ATOM   1422 O  O   . THR A 1 176 ? -20.837 3.428   -0.234  1.00  13.04 ? 177 THR A O   1 
ATOM   1423 C  CB  . THR A 1 176 ? -19.938 6.481   -1.268  1.00  15.87 ? 177 THR A CB  1 
ATOM   1424 O  OG1 . THR A 1 176 ? -20.343 5.794   -2.467  1.00  20.94 ? 177 THR A OG1 1 
ATOM   1425 C  CG2 . THR A 1 176 ? -18.761 7.469   -1.508  1.00  18.80 ? 177 THR A CG2 1 
ATOM   1426 N  N   . ASN A 1 177 ? -21.521 5.148   1.122   1.00  12.34 ? 178 ASN A N   1 
ATOM   1427 C  CA  . ASN A 1 177 ? -22.789 4.605   1.511   1.00  12.54 ? 178 ASN A CA  1 
ATOM   1428 C  C   . ASN A 1 177 ? -22.641 3.253   2.251   1.00  14.18 ? 178 ASN A C   1 
ATOM   1429 O  O   . ASN A 1 177 ? -23.563 2.459   2.230   1.00  16.54 ? 178 ASN A O   1 
ATOM   1430 C  CB  . ASN A 1 177 ? -23.707 4.444   0.275   1.00  13.64 ? 178 ASN A CB  1 
ATOM   1431 C  CG  . ASN A 1 177 ? -24.024 5.814   -0.367  1.00  15.23 ? 178 ASN A CG  1 
ATOM   1432 O  OD1 . ASN A 1 177 ? -24.718 6.636   0.244   1.00  16.39 ? 178 ASN A OD1 1 
ATOM   1433 N  ND2 . ASN A 1 177 ? -23.366 6.089   -1.503  1.00  14.22 ? 178 ASN A ND2 1 
ATOM   1434 N  N   . PHE A 1 178 ? -21.468 3.051   2.866   1.00  12.54 ? 179 PHE A N   1 
ATOM   1435 C  CA  . PHE A 1 178 ? -21.316 1.819   3.726   1.00  13.10 ? 179 PHE A CA  1 
ATOM   1436 C  C   . PHE A 1 178 ? -21.816 2.115   5.080   1.00  12.12 ? 179 PHE A C   1 
ATOM   1437 O  O   . PHE A 1 178 ? -21.401 3.118   5.723   1.00  13.72 ? 179 PHE A O   1 
ATOM   1438 C  CB  . PHE A 1 178 ? -19.915 1.391   3.808   1.00  12.48 ? 179 PHE A CB  1 
ATOM   1439 C  CG  . PHE A 1 178 ? -19.772 0.151   4.650   1.00  12.41 ? 179 PHE A CG  1 
ATOM   1440 C  CD1 . PHE A 1 178 ? -20.251 -1.089  4.168   1.00  13.78 ? 179 PHE A CD1 1 
ATOM   1441 C  CD2 . PHE A 1 178 ? -19.287 0.247   5.938   1.00  11.48 ? 179 PHE A CD2 1 
ATOM   1442 C  CE1 . PHE A 1 178 ? -20.176 -2.203  4.945   1.00  13.26 ? 179 PHE A CE1 1 
ATOM   1443 C  CE2 . PHE A 1 178 ? -19.265 -0.918  6.725   1.00  11.42 ? 179 PHE A CE2 1 
ATOM   1444 C  CZ  . PHE A 1 178 ? -19.659 -2.108  6.234   1.00  12.19 ? 179 PHE A CZ  1 
ATOM   1445 N  N   . ASP A 1 179 ? -22.710 1.275   5.558   1.00  12.53 ? 180 ASP A N   1 
ATOM   1446 C  CA  . ASP A 1 179 ? -23.291 1.437   6.863   1.00  11.49 ? 180 ASP A CA  1 
ATOM   1447 C  C   . ASP A 1 179 ? -22.657 0.620   7.934   1.00  10.73 ? 180 ASP A C   1 
ATOM   1448 O  O   . ASP A 1 179 ? -22.810 -0.612  7.944   1.00  11.48 ? 180 ASP A O   1 
ATOM   1449 C  CB  . ASP A 1 179 ? -24.779 1.072   6.772   1.00  14.41 ? 180 ASP A CB  1 
ATOM   1450 C  CG  . ASP A 1 179 ? -25.572 1.521   7.981   1.00  17.90 ? 180 ASP A CG  1 
ATOM   1451 O  OD1 . ASP A 1 179 ? -24.968 1.737   9.051   1.00  13.34 ? 180 ASP A OD1 1 
ATOM   1452 O  OD2 . ASP A 1 179 ? -26.809 1.650   7.858   1.00  20.74 ? 180 ASP A OD2 1 
ATOM   1453 N  N   . PRO A 1 180 ? -21.914 1.252   8.865   1.00  8.68  ? 181 PRO A N   1 
ATOM   1454 C  CA  . PRO A 1 180 ? -21.164 0.422   9.853   1.00  9.32  ? 181 PRO A CA  1 
ATOM   1455 C  C   . PRO A 1 180 ? -22.068 -0.169  10.894  1.00  9.60  ? 181 PRO A C   1 
ATOM   1456 O  O   . PRO A 1 180 ? -21.615 -1.126  11.622  1.00  8.43  ? 181 PRO A O   1 
ATOM   1457 C  CB  . PRO A 1 180 ? -20.162 1.449   10.391  1.00  10.27 ? 181 PRO A CB  1 
ATOM   1458 C  CG  . PRO A 1 180 ? -20.905 2.712   10.415  1.00  9.80  ? 181 PRO A CG  1 
ATOM   1459 C  CD  . PRO A 1 180 ? -21.603 2.701   9.038   1.00  9.17  ? 181 PRO A CD  1 
ATOM   1460 N  N   . ARG A 1 181 ? -23.364 0.199   10.948  1.00  9.38  ? 182 ARG A N   1 
ATOM   1461 C  CA  . ARG A 1 181 ? -24.297 -0.505  11.897  1.00  9.43  ? 182 ARG A CA  1 
ATOM   1462 C  C   . ARG A 1 181 ? -24.401 -2.021  11.551  1.00  10.13 ? 182 ARG A C   1 
ATOM   1463 O  O   . ARG A 1 181 ? -24.776 -2.808  12.390  1.00  12.41 ? 182 ARG A O   1 
ATOM   1464 C  CB  . ARG A 1 181 ? -25.700 0.124   11.851  1.00  11.34 ? 182 ARG A CB  1 
ATOM   1465 C  CG  . ARG A 1 181 ? -25.639 1.570   12.381  1.00  13.77 ? 182 ARG A CG  1 
ATOM   1466 C  CD  . ARG A 1 181 ? -26.982 2.274   12.231  1.00  16.99 ? 182 ARG A CD  1 
ATOM   1467 N  NE  . ARG A 1 181 ? -27.367 2.440   10.850  1.00  16.32 ? 182 ARG A NE  1 
ATOM   1468 C  CZ  . ARG A 1 181 ? -28.476 3.092   10.481  1.00  20.86 ? 182 ARG A CZ  1 
ATOM   1469 N  NH1 . ARG A 1 181 ? -29.271 3.574   11.424  1.00  21.87 ? 182 ARG A NH1 1 
ATOM   1470 N  NH2 . ARG A 1 181 ? -28.769 3.192   9.189   1.00  20.36 ? 182 ARG A NH2 1 
ATOM   1471 N  N   . GLY A 1 182 ? -24.220 -2.373  10.280  1.00  10.64 ? 183 GLY A N   1 
ATOM   1472 C  CA  . GLY A 1 182 ? -24.248 -3.784  9.850   1.00  11.54 ? 183 GLY A CA  1 
ATOM   1473 C  C   . GLY A 1 182 ? -23.114 -4.644  10.381  1.00  13.73 ? 183 GLY A C   1 
ATOM   1474 O  O   . GLY A 1 182 ? -23.072 -5.863  10.089  1.00  13.22 ? 183 GLY A O   1 
ATOM   1475 N  N   . LEU A 1 183 ? -22.169 -4.042  11.108  1.00  10.79 ? 184 LEU A N   1 
ATOM   1476 C  CA  . LEU A 1 183 ? -21.023 -4.826  11.695  1.00  10.56 ? 184 LEU A CA  1 
ATOM   1477 C  C   . LEU A 1 183 ? -21.168 -4.986  13.155  1.00  10.07 ? 184 LEU A C   1 
ATOM   1478 O  O   . LEU A 1 183 ? -20.244 -5.542  13.793  1.00  11.50 ? 184 LEU A O   1 
ATOM   1479 C  CB  . LEU A 1 183 ? -19.705 -4.079  11.423  1.00  10.23 ? 184 LEU A CB  1 
ATOM   1480 C  CG  . LEU A 1 183 ? -19.365 -3.858  9.940   1.00  11.08 ? 184 LEU A CG  1 
ATOM   1481 C  CD1 . LEU A 1 183 ? -18.070 -3.111  9.707   1.00  11.34 ? 184 LEU A CD1 1 
ATOM   1482 C  CD2 . LEU A 1 183 ? -19.264 -5.208  9.244   1.00  13.34 ? 184 LEU A CD2 1 
ATOM   1483 N  N   . LEU A 1 184 ? -22.270 -4.570  13.772  1.00  9.90  ? 185 LEU A N   1 
ATOM   1484 C  CA  . LEU A 1 184 ? -22.379 -4.567  15.258  1.00  9.65  ? 185 LEU A CA  1 
ATOM   1485 C  C   . LEU A 1 184 ? -23.172 -5.788  15.754  1.00  12.31 ? 185 LEU A C   1 
ATOM   1486 O  O   . LEU A 1 184 ? -24.288 -6.072  15.221  1.00  14.64 ? 185 LEU A O   1 
ATOM   1487 C  CB  . LEU A 1 184 ? -23.179 -3.317  15.765  1.00  9.61  ? 185 LEU A CB  1 
ATOM   1488 C  CG  . LEU A 1 184 ? -22.635 -1.966  15.336  1.00  9.68  ? 185 LEU A CG  1 
ATOM   1489 C  CD1 . LEU A 1 184 ? -23.545 -0.848  15.800  1.00  12.04 ? 185 LEU A CD1 1 
ATOM   1490 C  CD2 . LEU A 1 184 ? -21.196 -1.787  15.863  1.00  10.87 ? 185 LEU A CD2 1 
ATOM   1491 N  N   . PRO A 1 185 ? -22.773 -6.411  16.826  1.00  9.72  ? 186 PRO A N   1 
ATOM   1492 C  CA  . PRO A 1 185 ? -23.546 -7.480  17.396  1.00  10.08 ? 186 PRO A CA  1 
ATOM   1493 C  C   . PRO A 1 185 ? -24.823 -6.952  18.043  1.00  11.88 ? 186 PRO A C   1 
ATOM   1494 O  O   . PRO A 1 185 ? -24.990 -5.755  18.197  1.00  10.45 ? 186 PRO A O   1 
ATOM   1495 C  CB  . PRO A 1 185 ? -22.570 -8.089  18.442  1.00  9.34  ? 186 PRO A CB  1 
ATOM   1496 C  CG  . PRO A 1 185 ? -21.798 -6.869  18.898  1.00  8.17  ? 186 PRO A CG  1 
ATOM   1497 C  CD  . PRO A 1 185 ? -21.624 -5.985  17.690  1.00  8.41  ? 186 PRO A CD  1 
ATOM   1498 N  N   A GLU A 1 186 ? -25.667 -7.862  18.516  0.50  11.71 ? 187 GLU A N   1 
ATOM   1499 N  N   B GLU A 1 186 ? -25.675 -7.870  18.507  0.50  12.68 ? 187 GLU A N   1 
ATOM   1500 C  CA  A GLU A 1 186 ? -26.923 -7.494  19.113  0.50  12.09 ? 187 GLU A CA  1 
ATOM   1501 C  CA  B GLU A 1 186 ? -26.942 -7.496  19.101  0.50  13.72 ? 187 GLU A CA  1 
ATOM   1502 C  C   A GLU A 1 186 ? -26.702 -6.715  20.399  0.50  12.42 ? 187 GLU A C   1 
ATOM   1503 C  C   B GLU A 1 186 ? -26.701 -6.720  20.381  0.50  13.35 ? 187 GLU A C   1 
ATOM   1504 O  O   A GLU A 1 186 ? -27.320 -5.690  20.653  0.50  13.86 ? 187 GLU A O   1 
ATOM   1505 O  O   B GLU A 1 186 ? -27.277 -5.664  20.575  0.50  14.80 ? 187 GLU A O   1 
ATOM   1506 C  CB  A GLU A 1 186 ? -27.672 -8.799  19.379  0.50  13.65 ? 187 GLU A CB  1 
ATOM   1507 C  CB  B GLU A 1 186 ? -27.807 -8.764  19.288  0.50  17.34 ? 187 GLU A CB  1 
ATOM   1508 C  CG  A GLU A 1 186 ? -28.653 -8.660  20.508  0.50  14.09 ? 187 GLU A CG  1 
ATOM   1509 C  CG  B GLU A 1 186 ? -28.233 -9.361  17.947  0.50  20.55 ? 187 GLU A CG  1 
ATOM   1510 C  CD  A GLU A 1 186 ? -29.433 -9.950  20.788  0.50  15.14 ? 187 GLU A CD  1 
ATOM   1511 C  CD  B GLU A 1 186 ? -29.083 -10.632 18.034  0.50  24.19 ? 187 GLU A CD  1 
ATOM   1512 O  OE1 A GLU A 1 186 ? -29.294 -10.889 20.044  0.50  13.63 ? 187 GLU A OE1 1 
ATOM   1513 O  OE1 B GLU A 1 186 ? -29.384 -11.014 19.160  0.50  21.72 ? 187 GLU A OE1 1 
ATOM   1514 O  OE2 A GLU A 1 186 ? -30.146 -9.989  21.808  0.50  16.78 ? 187 GLU A OE2 1 
ATOM   1515 O  OE2 B GLU A 1 186 ? -29.427 -11.241 16.977  0.50  24.62 ? 187 GLU A OE2 1 
ATOM   1516 N  N   . SER A 1 187 ? -25.806 -7.214  21.250  1.00  11.25 ? 188 SER A N   1 
ATOM   1517 C  CA  . SER A 1 187 ? -25.604 -6.637  22.555  1.00  11.51 ? 188 SER A CA  1 
ATOM   1518 C  C   . SER A 1 187 ? -24.445 -5.592  22.532  1.00  10.56 ? 188 SER A C   1 
ATOM   1519 O  O   . SER A 1 187 ? -23.453 -5.838  21.903  1.00  12.74 ? 188 SER A O   1 
ATOM   1520 C  CB  . SER A 1 187 ? -25.177 -7.729  23.583  1.00  12.37 ? 188 SER A CB  1 
ATOM   1521 O  OG  . SER A 1 187 ? -24.954 -7.137  24.854  1.00  13.24 ? 188 SER A OG  1 
ATOM   1522 N  N   . LEU A 1 188 ? -24.589 -4.507  23.252  1.00  9.86  ? 189 LEU A N   1 
ATOM   1523 C  CA  . LEU A 1 188 ? -23.526 -3.498  23.452  1.00  10.92 ? 189 LEU A CA  1 
ATOM   1524 C  C   . LEU A 1 188 ? -22.905 -3.630  24.857  1.00  10.01 ? 189 LEU A C   1 
ATOM   1525 O  O   . LEU A 1 188 ? -22.250 -2.671  25.348  1.00  11.84 ? 189 LEU A O   1 
ATOM   1526 C  CB  . LEU A 1 188 ? -24.074 -2.074  23.136  1.00  10.31 ? 189 LEU A CB  1 
ATOM   1527 C  CG  . LEU A 1 188 ? -24.516 -1.799  21.702  1.00  12.95 ? 189 LEU A CG  1 
ATOM   1528 C  CD1 . LEU A 1 188 ? -25.017 -0.364  21.581  1.00  14.93 ? 189 LEU A CD1 1 
ATOM   1529 C  CD2 . LEU A 1 188 ? -23.428 -2.111  20.683  1.00  13.08 ? 189 LEU A CD2 1 
ATOM   1530 N  N   . ASP A 1 189 ? -23.037 -4.778  25.530  1.00  11.43 ? 190 ASP A N   1 
ATOM   1531 C  CA  . ASP A 1 189 ? -22.299 -5.015  26.765  1.00  10.57 ? 190 ASP A CA  1 
ATOM   1532 C  C   . ASP A 1 189 ? -20.779 -4.949  26.474  1.00  9.26  ? 190 ASP A C   1 
ATOM   1533 O  O   . ASP A 1 189 ? -20.327 -5.461  25.416  1.00  9.28  ? 190 ASP A O   1 
ATOM   1534 C  CB  . ASP A 1 189 ? -22.652 -6.363  27.428  1.00  12.31 ? 190 ASP A CB  1 
ATOM   1535 C  CG  . ASP A 1 189 ? -24.083 -6.393  28.110  1.00  15.85 ? 190 ASP A CG  1 
ATOM   1536 O  OD1 . ASP A 1 189 ? -24.593 -5.324  28.413  1.00  19.56 ? 190 ASP A OD1 1 
ATOM   1537 O  OD2 . ASP A 1 189 ? -24.543 -7.530  28.240  1.00  20.93 ? 190 ASP A OD2 1 
ATOM   1538 N  N   . TYR A 1 190 ? -20.020 -4.312  27.364  1.00  8.12  ? 191 TYR A N   1 
ATOM   1539 C  CA  . TYR A 1 190 ? -18.579 -4.094  27.016  1.00  7.74  ? 191 TYR A CA  1 
ATOM   1540 C  C   . TYR A 1 190 ? -17.690 -4.205  28.236  1.00  8.05  ? 191 TYR A C   1 
ATOM   1541 O  O   . TYR A 1 190 ? -18.117 -4.048  29.408  1.00  8.30  ? 191 TYR A O   1 
ATOM   1542 C  CB  . TYR A 1 190 ? -18.401 -2.698  26.406  1.00  8.75  ? 191 TYR A CB  1 
ATOM   1543 C  CG  . TYR A 1 190 ? -18.848 -1.585  27.284  1.00  7.84  ? 191 TYR A CG  1 
ATOM   1544 C  CD1 . TYR A 1 190 ? -17.930 -0.937  28.162  1.00  8.05  ? 191 TYR A CD1 1 
ATOM   1545 C  CD2 . TYR A 1 190 ? -20.149 -1.080  27.191  1.00  8.08  ? 191 TYR A CD2 1 
ATOM   1546 C  CE1 . TYR A 1 190 ? -18.368 0.073   29.036  1.00  8.69  ? 191 TYR A CE1 1 
ATOM   1547 C  CE2 . TYR A 1 190 ? -20.549 0.005   28.013  1.00  9.21  ? 191 TYR A CE2 1 
ATOM   1548 C  CZ  . TYR A 1 190 ? -19.640 0.575   28.920  1.00  9.67  ? 191 TYR A CZ  1 
ATOM   1549 O  OH  . TYR A 1 190 ? -20.048 1.598   29.770  1.00  10.73 ? 191 TYR A OH  1 
ATOM   1550 N  N   . TRP A 1 191 ? -16.382 -4.349  27.969  1.00  6.54  ? 192 TRP A N   1 
ATOM   1551 C  CA  . TRP A 1 191 ? -15.307 -4.097  28.941  1.00  6.36  ? 192 TRP A CA  1 
ATOM   1552 C  C   . TRP A 1 191 ? -14.637 -2.826  28.506  1.00  6.34  ? 192 TRP A C   1 
ATOM   1553 O  O   . TRP A 1 191 ? -14.663 -2.434  27.350  1.00  6.65  ? 192 TRP A O   1 
ATOM   1554 C  CB  . TRP A 1 191 ? -14.303 -5.205  28.880  1.00  6.62  ? 192 TRP A CB  1 
ATOM   1555 C  CG  . TRP A 1 191 ? -14.799 -6.535  29.288  1.00  6.67  ? 192 TRP A CG  1 
ATOM   1556 C  CD1 . TRP A 1 191 ? -14.990 -7.018  30.582  1.00  7.25  ? 192 TRP A CD1 1 
ATOM   1557 C  CD2 . TRP A 1 191 ? -15.063 -7.652  28.412  1.00  6.66  ? 192 TRP A CD2 1 
ATOM   1558 N  NE1 . TRP A 1 191 ? -15.332 -8.323  30.536  1.00  8.08  ? 192 TRP A NE1 1 
ATOM   1559 C  CE2 . TRP A 1 191 ? -15.444 -8.770  29.263  1.00  7.50  ? 192 TRP A CE2 1 
ATOM   1560 C  CE3 . TRP A 1 191 ? -14.956 -7.843  27.025  1.00  7.23  ? 192 TRP A CE3 1 
ATOM   1561 C  CZ2 . TRP A 1 191 ? -15.756 -10.048 28.720  1.00  7.89  ? 192 TRP A CZ2 1 
ATOM   1562 C  CZ3 . TRP A 1 191 ? -15.279 -9.106  26.517  1.00  7.61  ? 192 TRP A CZ3 1 
ATOM   1563 C  CH2 . TRP A 1 191 ? -15.618 -10.193 27.353  1.00  7.93  ? 192 TRP A CH2 1 
ATOM   1564 N  N   . THR A 1 192 ? -14.023 -2.126  29.450  1.00  5.69  ? 193 THR A N   1 
ATOM   1565 C  CA  . THR A 1 192 ? -13.343 -0.867  29.110  1.00  5.99  ? 193 THR A CA  1 
ATOM   1566 C  C   . THR A 1 192 ? -12.113 -0.671  29.982  1.00  6.03  ? 193 THR A C   1 
ATOM   1567 O  O   . THR A 1 192 ? -12.043 -1.109  31.164  1.00  7.35  ? 193 THR A O   1 
ATOM   1568 C  CB  . THR A 1 192 ? -14.298 0.344   29.215  1.00  6.48  ? 193 THR A CB  1 
ATOM   1569 O  OG1 . THR A 1 192 ? -13.596 1.530   28.814  1.00  7.04  ? 193 THR A OG1 1 
ATOM   1570 C  CG2 . THR A 1 192 ? -14.778 0.594   30.675  1.00  7.91  ? 193 THR A CG2 1 
ATOM   1571 N  N   . TYR A 1 193 ? -11.052 -0.099  29.389  1.00  5.71  ? 194 TYR A N   1 
ATOM   1572 C  CA  . TYR A 1 193 ? -9.820  0.154   30.163  1.00  5.86  ? 194 TYR A CA  1 
ATOM   1573 C  C   . TYR A 1 193 ? -9.033  1.193   29.384  1.00  6.32  ? 194 TYR A C   1 
ATOM   1574 O  O   . TYR A 1 193 ? -9.282  1.385   28.174  1.00  6.37  ? 194 TYR A O   1 
ATOM   1575 C  CB  . TYR A 1 193 ? -8.945  -1.113  30.354  1.00  5.88  ? 194 TYR A CB  1 
ATOM   1576 C  CG  . TYR A 1 193 ? -8.252  -1.575  29.113  1.00  5.10  ? 194 TYR A CG  1 
ATOM   1577 C  CD1 . TYR A 1 193 ? -8.948  -2.316  28.113  1.00  5.19  ? 194 TYR A CD1 1 
ATOM   1578 C  CD2 . TYR A 1 193 ? -6.920  -1.249  28.865  1.00  5.16  ? 194 TYR A CD2 1 
ATOM   1579 C  CE1 . TYR A 1 193 ? -8.322  -2.679  26.939  1.00  4.76  ? 194 TYR A CE1 1 
ATOM   1580 C  CE2 . TYR A 1 193 ? -6.282  -1.588  27.659  1.00  4.87  ? 194 TYR A CE2 1 
ATOM   1581 C  CZ  . TYR A 1 193 ? -6.966  -2.302  26.699  1.00  5.05  ? 194 TYR A CZ  1 
ATOM   1582 O  OH  . TYR A 1 193 ? -6.338  -2.601  25.560  1.00  5.15  ? 194 TYR A OH  1 
ATOM   1583 N  N   . PRO A 1 194 ? -8.081  1.923   30.033  1.00  5.22  ? 195 PRO A N   1 
ATOM   1584 C  CA  . PRO A 1 194 ? -7.280  2.906   29.340  1.00  5.73  ? 195 PRO A CA  1 
ATOM   1585 C  C   . PRO A 1 194 ? -6.048  2.250   28.682  1.00  5.39  ? 195 PRO A C   1 
ATOM   1586 O  O   . PRO A 1 194 ? -5.318  1.509   29.365  1.00  6.44  ? 195 PRO A O   1 
ATOM   1587 C  CB  . PRO A 1 194 ? -6.751  3.828   30.498  1.00  5.85  ? 195 PRO A CB  1 
ATOM   1588 C  CG  . PRO A 1 194 ? -6.773  2.923   31.720  1.00  6.29  ? 195 PRO A CG  1 
ATOM   1589 C  CD  . PRO A 1 194 ? -7.855  1.884   31.511  1.00  6.12  ? 195 PRO A CD  1 
ATOM   1590 N  N   . GLY A 1 195 ? -5.813  2.580   27.415  1.00  5.14  ? 196 GLY A N   1 
ATOM   1591 C  CA  . GLY A 1 195 ? -4.698  1.891   26.676  1.00  5.69  ? 196 GLY A CA  1 
ATOM   1592 C  C   . GLY A 1 195 ? -4.166  2.773   25.612  1.00  5.43  ? 196 GLY A C   1 
ATOM   1593 O  O   . GLY A 1 195 ? -4.070  4.000   25.729  1.00  5.64  ? 196 GLY A O   1 
ATOM   1594 N  N   . SER A 1 196 ? -3.766  2.096   24.557  1.00  5.26  ? 197 SER A N   1 
ATOM   1595 C  CA  . SER A 1 196 ? -2.977  2.787   23.502  1.00  5.38  ? 197 SER A CA  1 
ATOM   1596 C  C   . SER A 1 196 ? -3.413  2.419   22.100  1.00  5.07  ? 197 SER A C   1 
ATOM   1597 O  O   . SER A 1 196 ? -4.155  1.428   21.928  1.00  5.24  ? 197 SER A O   1 
ATOM   1598 C  CB  . SER A 1 196 ? -1.449  2.370   23.626  1.00  5.68  ? 197 SER A CB  1 
ATOM   1599 O  OG  . SER A 1 196 ? -1.222  0.994   23.270  1.00  5.29  ? 197 SER A OG  1 
ATOM   1600 N  N   . LEU A 1 197 ? -2.841  3.075   21.094  1.00  6.29  ? 198 LEU A N   1 
ATOM   1601 C  CA  . LEU A 1 197 ? -2.869  2.505   19.740  1.00  6.21  ? 198 LEU A CA  1 
ATOM   1602 C  C   . LEU A 1 197 ? -2.176  1.174   19.802  1.00  5.61  ? 198 LEU A C   1 
ATOM   1603 O  O   . LEU A 1 197 ? -1.152  1.025   20.538  1.00  5.48  ? 198 LEU A O   1 
ATOM   1604 C  CB  . LEU A 1 197 ? -2.095  3.416   18.829  1.00  8.71  ? 198 LEU A CB  1 
ATOM   1605 C  CG  . LEU A 1 197 ? -2.716  4.561   18.141  1.00  14.12 ? 198 LEU A CG  1 
ATOM   1606 C  CD1 . LEU A 1 197 ? -3.662  5.401   18.908  1.00  12.68 ? 198 LEU A CD1 1 
ATOM   1607 C  CD2 . LEU A 1 197 ? -1.699  5.509   17.506  1.00  16.45 ? 198 LEU A CD2 1 
ATOM   1608 N  N   . THR A 1 198 ? -2.608  0.199   19.007  1.00  5.15  ? 199 THR A N   1 
ATOM   1609 C  CA  . THR A 1 198 ? -1.904  -1.087  18.959  1.00  6.35  ? 199 THR A CA  1 
ATOM   1610 C  C   . THR A 1 198 ? -0.924  -1.141  17.831  1.00  6.41  ? 199 THR A C   1 
ATOM   1611 O  O   . THR A 1 198 ? -0.319  -2.197  17.649  1.00  6.86  ? 199 THR A O   1 
ATOM   1612 C  CB  . THR A 1 198 ? -2.922  -2.216  18.817  1.00  5.52  ? 199 THR A CB  1 
ATOM   1613 O  OG1 . THR A 1 198 ? -3.542  -2.176  17.531  1.00  5.19  ? 199 THR A OG1 1 
ATOM   1614 C  CG2 . THR A 1 198 ? -3.935  -2.257  19.978  1.00  6.05  ? 199 THR A CG2 1 
ATOM   1615 N  N   . THR A 1 199 ? -0.818  -0.078  17.031  1.00  6.85  ? 200 THR A N   1 
ATOM   1616 C  CA  . THR A 1 199 ? 0.301   0.010   15.997  1.00  7.79  ? 200 THR A CA  1 
ATOM   1617 C  C   . THR A 1 199 ? 1.126   1.232   16.343  1.00  7.64  ? 200 THR A C   1 
ATOM   1618 O  O   . THR A 1 199 ? 0.689   2.153   16.973  1.00  7.58  ? 200 THR A O   1 
ATOM   1619 C  CB  . THR A 1 199 ? -0.226  0.177   14.571  1.00  9.53  ? 200 THR A CB  1 
ATOM   1620 O  OG1 . THR A 1 199 ? -0.865  1.430   14.418  1.00  12.60 ? 200 THR A OG1 1 
ATOM   1621 C  CG2 . THR A 1 199 ? -1.257  -0.881  14.232  1.00  9.89  ? 200 THR A CG2 1 
ATOM   1622 N  N   . PRO A 1 200 ? 2.389   1.245   15.915  1.00  7.95  ? 201 PRO A N   1 
ATOM   1623 C  CA  . PRO A 1 200 ? 3.099   2.486   16.028  1.00  8.18  ? 201 PRO A CA  1 
ATOM   1624 C  C   . PRO A 1 200 ? 2.240   3.636   15.457  1.00  7.54  ? 201 PRO A C   1 
ATOM   1625 O  O   . PRO A 1 200 ? 1.530   3.508   14.411  1.00  9.40  ? 201 PRO A O   1 
ATOM   1626 C  CB  . PRO A 1 200 ? 4.321   2.196   15.070  1.00  7.59  ? 201 PRO A CB  1 
ATOM   1627 C  CG  . PRO A 1 200 ? 4.551   0.761   15.274  1.00  8.48  ? 201 PRO A CG  1 
ATOM   1628 C  CD  . PRO A 1 200 ? 3.132   0.156   15.277  1.00  8.06  ? 201 PRO A CD  1 
ATOM   1629 N  N   . PRO A 1 201 ? 2.287   4.839   16.052  1.00  7.68  ? 202 PRO A N   1 
ATOM   1630 C  CA  . PRO A 1 201 ? 3.223   5.239   17.129  1.00  8.67  ? 202 PRO A CA  1 
ATOM   1631 C  C   . PRO A 1 201 ? 2.897   4.827   18.564  1.00  7.81  ? 202 PRO A C   1 
ATOM   1632 O  O   . PRO A 1 201 ? 3.549   5.194   19.504  1.00  9.00  ? 202 PRO A O   1 
ATOM   1633 C  CB  . PRO A 1 201 ? 3.213   6.756   17.018  1.00  8.37  ? 202 PRO A CB  1 
ATOM   1634 C  CG  . PRO A 1 201 ? 1.855   7.074   16.490  1.00  9.73  ? 202 PRO A CG  1 
ATOM   1635 C  CD  . PRO A 1 201 ? 1.563   5.993   15.489  1.00  8.39  ? 202 PRO A CD  1 
ATOM   1636 N  N   . LEU A 1 202 ? 1.898   3.922   18.745  1.00  6.89  ? 203 LEU A N   1 
ATOM   1637 C  CA  . LEU A 1 202 ? 1.645   3.295   20.055  1.00  7.03  ? 203 LEU A CA  1 
ATOM   1638 C  C   . LEU A 1 202 ? 1.251   4.329   21.135  1.00  6.25  ? 203 LEU A C   1 
ATOM   1639 O  O   . LEU A 1 202 ? 1.432   4.086   22.274  1.00  6.41  ? 203 LEU A O   1 
ATOM   1640 C  CB  . LEU A 1 202 ? 2.826   2.398   20.495  1.00  6.93  ? 203 LEU A CB  1 
ATOM   1641 C  CG  . LEU A 1 202 ? 3.075   1.240   19.510  1.00  6.67  ? 203 LEU A CG  1 
ATOM   1642 C  CD1 . LEU A 1 202 ? 4.387   0.649   19.980  1.00  8.69  ? 203 LEU A CD1 1 
ATOM   1643 C  CD2 . LEU A 1 202 ? 2.050   0.126   19.427  1.00  7.92  ? 203 LEU A CD2 1 
ATOM   1644 N  N   . LEU A 1 203 ? 0.676   5.448   20.688  1.00  6.53  ? 204 LEU A N   1 
ATOM   1645 C  CA  . LEU A 1 203 ? 0.398   6.529   21.625  1.00  6.89  ? 204 LEU A CA  1 
ATOM   1646 C  C   . LEU A 1 203 ? -0.648  6.126   22.655  1.00  7.17  ? 204 LEU A C   1 
ATOM   1647 O  O   . LEU A 1 203 ? -1.623  5.413   22.380  1.00  6.71  ? 204 LEU A O   1 
ATOM   1648 C  CB  . LEU A 1 203 ? -0.046  7.799   20.882  1.00  7.41  ? 204 LEU A CB  1 
ATOM   1649 C  CG  . LEU A 1 203 ? 1.048   8.352   19.951  1.00  8.27  ? 204 LEU A CG  1 
ATOM   1650 C  CD1 . LEU A 1 203 ? 0.457   9.468   19.103  1.00  10.29 ? 204 LEU A CD1 1 
ATOM   1651 C  CD2 . LEU A 1 203 ? 2.232   8.941   20.739  1.00  11.93 ? 204 LEU A CD2 1 
ATOM   1652 N  N   . GLU A 1 204 ? -0.449  6.584   23.878  1.00  7.13  ? 205 GLU A N   1 
ATOM   1653 C  CA  . GLU A 1 204 ? -1.264  6.225   25.026  1.00  6.93  ? 205 GLU A CA  1 
ATOM   1654 C  C   . GLU A 1 204 ? -2.459  7.173   25.165  1.00  7.50  ? 205 GLU A C   1 
ATOM   1655 O  O   . GLU A 1 204 ? -2.560  7.969   26.109  1.00  9.38  ? 205 GLU A O   1 
ATOM   1656 C  CB  . GLU A 1 204 ? -0.394  6.063   26.314  1.00  7.57  ? 205 GLU A CB  1 
ATOM   1657 C  CG  . GLU A 1 204 ? 0.482   4.831   26.199  1.00  9.38  ? 205 GLU A CG  1 
ATOM   1658 C  CD  . GLU A 1 204 ? 1.437   4.580   27.332  1.00  10.44 ? 205 GLU A CD  1 
ATOM   1659 O  OE1 . GLU A 1 204 ? 1.749   5.536   28.070  1.00  12.51 ? 205 GLU A OE1 1 
ATOM   1660 O  OE2 . GLU A 1 204 ? 1.810   3.414   27.441  1.00  9.33  ? 205 GLU A OE2 1 
ATOM   1661 N  N   . CYS A 1 205 ? -3.363  7.097   24.192  1.00  6.88  ? 206 CYS A N   1 
ATOM   1662 C  CA  . CYS A 1 205 ? -4.426  8.114   24.028  1.00  6.68  ? 206 CYS A CA  1 
ATOM   1663 C  C   . CYS A 1 205 ? -5.771  7.447   23.899  1.00  6.66  ? 206 CYS A C   1 
ATOM   1664 O  O   . CYS A 1 205 ? -6.735  8.153   23.574  1.00  7.38  ? 206 CYS A O   1 
ATOM   1665 C  CB  . CYS A 1 205 ? -4.157  8.956   22.813  1.00  7.24  ? 206 CYS A CB  1 
ATOM   1666 S  SG  . CYS A 1 205 ? -4.097  7.987   21.262  1.00  8.36  ? 206 CYS A SG  1 
ATOM   1667 N  N   . VAL A 1 206 ? -5.889  6.175   24.200  1.00  5.71  ? 207 VAL A N   1 
ATOM   1668 C  CA  . VAL A 1 206 ? -7.136  5.444   23.809  1.00  5.17  ? 207 VAL A CA  1 
ATOM   1669 C  C   . VAL A 1 206 ? -7.957  4.995   25.032  1.00  5.35  ? 207 VAL A C   1 
ATOM   1670 O  O   . VAL A 1 206 ? -7.404  4.351   25.916  1.00  6.44  ? 207 VAL A O   1 
ATOM   1671 C  CB  . VAL A 1 206 ? -6.836  4.163   23.043  1.00  5.14  ? 207 VAL A CB  1 
ATOM   1672 C  CG1 . VAL A 1 206 ? -8.194  3.451   22.665  1.00  4.91  ? 207 VAL A CG1 1 
ATOM   1673 C  CG2 . VAL A 1 206 ? -6.097  4.518   21.727  1.00  5.98  ? 207 VAL A CG2 1 
ATOM   1674 N  N   . THR A 1 207 ? -9.285  5.293   25.082  1.00  5.73  ? 208 THR A N   1 
ATOM   1675 C  CA  . THR A 1 207 ? -10.167 4.590   25.945  1.00  5.69  ? 208 THR A CA  1 
ATOM   1676 C  C   . THR A 1 207 ? -10.693 3.422   25.166  1.00  5.24  ? 208 THR A C   1 
ATOM   1677 O  O   . THR A 1 207 ? -11.376 3.647   24.151  1.00  5.42  ? 208 THR A O   1 
ATOM   1678 C  CB  . THR A 1 207 ? -11.349 5.483   26.376  1.00  6.44  ? 208 THR A CB  1 
ATOM   1679 O  OG1 . THR A 1 207 ? -10.820 6.570   27.168  1.00  6.77  ? 208 THR A OG1 1 
ATOM   1680 C  CG2 . THR A 1 207 ? -12.303 4.757   27.262  1.00  6.64  ? 208 THR A CG2 1 
ATOM   1681 N  N   . TRP A 1 208 ? -10.318 2.209   25.545  1.00  5.55  ? 209 TRP A N   1 
ATOM   1682 C  CA  . TRP A 1 208 ? -10.785 1.008   24.834  1.00  5.38  ? 209 TRP A CA  1 
ATOM   1683 C  C   . TRP A 1 208 ? -12.144 0.603   25.331  1.00  5.36  ? 209 TRP A C   1 
ATOM   1684 O  O   . TRP A 1 208 ? -12.345 0.528   26.524  1.00  5.69  ? 209 TRP A O   1 
ATOM   1685 C  CB  . TRP A 1 208 ? -9.783  -0.192  25.062  1.00  5.40  ? 209 TRP A CB  1 
ATOM   1686 C  CG  . TRP A 1 208 ? -8.630  -0.064  24.093  1.00  4.90  ? 209 TRP A CG  1 
ATOM   1687 C  CD1 . TRP A 1 208 ? -7.361  0.535   24.256  1.00  4.85  ? 209 TRP A CD1 1 
ATOM   1688 C  CD2 . TRP A 1 208 ? -8.712  -0.456  22.710  1.00  4.78  ? 209 TRP A CD2 1 
ATOM   1689 N  NE1 . TRP A 1 208 ? -6.708  0.525   23.070  1.00  5.07  ? 209 TRP A NE1 1 
ATOM   1690 C  CE2 . TRP A 1 208 ? -7.451  -0.086  22.087  1.00  4.52  ? 209 TRP A CE2 1 
ATOM   1691 C  CE3 . TRP A 1 208 ? -9.703  -1.107  21.905  1.00  4.49  ? 209 TRP A CE3 1 
ATOM   1692 C  CZ2 . TRP A 1 208 ? -7.173  -0.306  20.759  1.00  4.74  ? 209 TRP A CZ2 1 
ATOM   1693 C  CZ3 . TRP A 1 208 ? -9.419  -1.369  20.582  1.00  4.79  ? 209 TRP A CZ3 1 
ATOM   1694 C  CH2 . TRP A 1 208 ? -8.164  -0.953  19.999  1.00  4.53  ? 209 TRP A CH2 1 
ATOM   1695 N  N   . ILE A 1 209 ? -13.008 0.247   24.378  1.00  4.87  ? 210 ILE A N   1 
ATOM   1696 C  CA  . ILE A 1 209 ? -14.354 -0.294  24.722  1.00  5.34  ? 210 ILE A CA  1 
ATOM   1697 C  C   . ILE A 1 209 ? -14.467 -1.564  23.877  1.00  5.66  ? 210 ILE A C   1 
ATOM   1698 O  O   . ILE A 1 209 ? -14.552 -1.459  22.664  1.00  5.09  ? 210 ILE A O   1 
ATOM   1699 C  CB  . ILE A 1 209 ? -15.420 0.764   24.335  1.00  6.34  ? 210 ILE A CB  1 
ATOM   1700 C  CG1 . ILE A 1 209 ? -15.193 2.018   25.162  1.00  7.13  ? 210 ILE A CG1 1 
ATOM   1701 C  CG2 . ILE A 1 209 ? -16.854 0.173   24.590  1.00  6.87  ? 210 ILE A CG2 1 
ATOM   1702 C  CD1 . ILE A 1 209 ? -15.971 3.268   24.714  1.00  9.90  ? 210 ILE A CD1 1 
ATOM   1703 N  N   . VAL A 1 210 ? -14.444 -2.721  24.506  1.00  5.69  ? 211 VAL A N   1 
ATOM   1704 C  CA  . VAL A 1 210 ? -14.404 -4.023  23.800  1.00  5.74  ? 211 VAL A CA  1 
ATOM   1705 C  C   . VAL A 1 210 ? -15.729 -4.718  24.084  1.00  5.98  ? 211 VAL A C   1 
ATOM   1706 O  O   . VAL A 1 210 ? -16.026 -4.942  25.226  1.00  6.62  ? 211 VAL A O   1 
ATOM   1707 C  CB  . VAL A 1 210 ? -13.199 -4.840  24.257  1.00  5.97  ? 211 VAL A CB  1 
ATOM   1708 C  CG1 . VAL A 1 210 ? -13.202 -6.209  23.551  1.00  6.50  ? 211 VAL A CG1 1 
ATOM   1709 C  CG2 . VAL A 1 210 ? -11.896 -4.087  23.944  1.00  6.22  ? 211 VAL A CG2 1 
ATOM   1710 N  N   . LEU A 1 211 ? -16.495 -4.989  23.025  1.00  5.82  ? 212 LEU A N   1 
ATOM   1711 C  CA  . LEU A 1 211 ? -17.813 -5.648  23.187  1.00  6.23  ? 212 LEU A CA  1 
ATOM   1712 C  C   . LEU A 1 211 ? -17.588 -7.088  23.562  1.00  6.49  ? 212 LEU A C   1 
ATOM   1713 O  O   . LEU A 1 211 ? -16.735 -7.827  23.018  1.00  6.72  ? 212 LEU A O   1 
ATOM   1714 C  CB  . LEU A 1 211 ? -18.565 -5.537  21.878  1.00  6.70  ? 212 LEU A CB  1 
ATOM   1715 C  CG  . LEU A 1 211 ? -18.963 -4.096  21.461  1.00  7.62  ? 212 LEU A CG  1 
ATOM   1716 C  CD1 . LEU A 1 211 ? -20.057 -4.130  20.324  1.00  8.55  ? 212 LEU A CD1 1 
ATOM   1717 C  CD2 . LEU A 1 211 ? -19.436 -3.261  22.682  1.00  8.63  ? 212 LEU A CD2 1 
ATOM   1718 N  N   . LYS A 1 212 ? -18.459 -7.563  24.519  1.00  7.53  ? 213 LYS A N   1 
ATOM   1719 C  CA  . LYS A 1 212 ? -18.372 -8.976  24.914  1.00  9.11  ? 213 LYS A CA  1 
ATOM   1720 C  C   . LYS A 1 212 ? -18.874 -9.921  23.846  1.00  7.96  ? 213 LYS A C   1 
ATOM   1721 O  O   . LYS A 1 212 ? -18.381 -11.027 23.720  1.00  9.07  ? 213 LYS A O   1 
ATOM   1722 C  CB  . LYS A 1 212 ? -19.235 -9.151  26.171  1.00  12.15 ? 213 LYS A CB  1 
ATOM   1723 C  CG  . LYS A 1 212 ? -19.653 -10.585 26.578  1.00  17.65 ? 213 LYS A CG  1 
ATOM   1724 C  CD  . LYS A 1 212 ? -20.847 -10.457 27.563  1.00  24.05 ? 213 LYS A CD  1 
ATOM   1725 C  CE  . LYS A 1 212 ? -22.283 -10.409 26.944  1.00  26.64 ? 213 LYS A CE  1 
ATOM   1726 N  NZ  . LYS A 1 212 ? -22.653 -9.680  25.631  1.00  26.27 ? 213 LYS A NZ  1 
ATOM   1727 N  N   . GLU A 1 213 ? -19.852 -9.504  23.027  1.00  7.52  ? 214 GLU A N   1 
ATOM   1728 C  CA  . GLU A 1 213 ? -20.428 -10.400 22.044  1.00  8.83  ? 214 GLU A CA  1 
ATOM   1729 C  C   . GLU A 1 213 ? -19.689 -10.296 20.723  1.00  7.24  ? 214 GLU A C   1 
ATOM   1730 O  O   . GLU A 1 213 ? -19.630 -9.220  20.133  1.00  6.69  ? 214 GLU A O   1 
ATOM   1731 C  CB  . GLU A 1 213 ? -21.911 -10.052 21.835  1.00  9.19  ? 214 GLU A CB  1 
ATOM   1732 C  CG  . GLU A 1 213 ? -22.582 -11.052 20.880  1.00  12.10 ? 214 GLU A CG  1 
ATOM   1733 C  CD  . GLU A 1 213 ? -24.073 -10.825 20.632  1.00  15.57 ? 214 GLU A CD  1 
ATOM   1734 O  OE1 . GLU A 1 213 ? -24.648 -9.958  21.236  1.00  13.77 ? 214 GLU A OE1 1 
ATOM   1735 O  OE2 . GLU A 1 213 ? -24.610 -11.694 19.882  1.00  23.18 ? 214 GLU A OE2 1 
ATOM   1736 N  N   . PRO A 1 214 ? -19.133 -11.406 20.240  1.00  7.21  ? 215 PRO A N   1 
ATOM   1737 C  CA  . PRO A 1 214 ? -18.476 -11.365 18.932  1.00  8.02  ? 215 PRO A CA  1 
ATOM   1738 C  C   . PRO A 1 214 ? -19.487 -11.364 17.838  1.00  8.25  ? 215 PRO A C   1 
ATOM   1739 O  O   . PRO A 1 214 ? -20.696 -11.727 18.044  1.00  10.25 ? 215 PRO A O   1 
ATOM   1740 C  CB  . PRO A 1 214 ? -17.667 -12.697 18.853  1.00  8.20  ? 215 PRO A CB  1 
ATOM   1741 C  CG  . PRO A 1 214 ? -18.453 -13.609 19.758  1.00  11.49 ? 215 PRO A CG  1 
ATOM   1742 C  CD  . PRO A 1 214 ? -19.107 -12.770 20.835  1.00  8.37  ? 215 PRO A CD  1 
ATOM   1743 N  N   . ILE A 1 215 ? -19.066 -10.927 16.658  1.00  6.97  ? 216 ILE A N   1 
ATOM   1744 C  CA  . ILE A 1 215 ? -19.946 -11.148 15.447  1.00  8.44  ? 216 ILE A CA  1 
ATOM   1745 C  C   . ILE A 1 215 ? -19.399 -12.392 14.771  1.00  8.56  ? 216 ILE A C   1 
ATOM   1746 O  O   . ILE A 1 215 ? -18.230 -12.773 14.971  1.00  8.38  ? 216 ILE A O   1 
ATOM   1747 C  CB  . ILE A 1 215 ? -19.935 -9.951  14.467  1.00  8.71  ? 216 ILE A CB  1 
ATOM   1748 C  CG1 . ILE A 1 215 ? -18.498 -9.571  14.044  1.00  8.72  ? 216 ILE A CG1 1 
ATOM   1749 C  CG2 . ILE A 1 215 ? -20.642 -8.730  15.127  1.00  9.36  ? 216 ILE A CG2 1 
ATOM   1750 C  CD1 . ILE A 1 215 ? -18.517 -8.580  12.816  1.00  8.95  ? 216 ILE A CD1 1 
ATOM   1751 N  N   A SER A 1 216 ? -20.259 -13.057 13.980  0.50  9.02  ? 217 SER A N   1 
ATOM   1752 N  N   B SER A 1 216 ? -20.232 -13.109 14.018  0.50  9.18  ? 217 SER A N   1 
ATOM   1753 C  CA  A SER A 1 216 ? -19.849 -14.171 13.134  0.50  9.11  ? 217 SER A CA  1 
ATOM   1754 C  CA  B SER A 1 216 ? -19.701 -14.210 13.246  0.50  9.56  ? 217 SER A CA  1 
ATOM   1755 C  C   A SER A 1 216 ? -19.650 -13.739 11.728  0.50  9.49  ? 217 SER A C   1 
ATOM   1756 C  C   B SER A 1 216 ? -19.648 -13.802 11.842  0.50  9.41  ? 217 SER A C   1 
ATOM   1757 O  O   A SER A 1 216 ? -20.441 -12.986 11.125  0.50  10.23 ? 217 SER A O   1 
ATOM   1758 O  O   B SER A 1 216 ? -20.572 -13.126 11.378  0.50  9.97  ? 217 SER A O   1 
ATOM   1759 C  CB  A SER A 1 216 ? -20.829 -15.331 13.172  0.50  10.67 ? 217 SER A CB  1 
ATOM   1760 C  CB  B SER A 1 216 ? -20.519 -15.445 13.375  0.50  11.18 ? 217 SER A CB  1 
ATOM   1761 O  OG  A SER A 1 216 ? -21.040 -15.774 14.513  0.50  11.24 ? 217 SER A OG  1 
ATOM   1762 O  OG  B SER A 1 216 ? -21.829 -15.213 12.891  0.50  12.79 ? 217 SER A OG  1 
ATOM   1763 N  N   . VAL A 1 217 ? -18.561 -14.205 11.190  1.00  8.93  ? 218 VAL A N   1 
ATOM   1764 C  CA  . VAL A 1 217 ? -18.296 -14.025 9.791   1.00  9.13  ? 218 VAL A CA  1 
ATOM   1765 C  C   . VAL A 1 217 ? -18.054 -15.385 9.170   1.00  8.68  ? 218 VAL A C   1 
ATOM   1766 O  O   . VAL A 1 217 ? -17.668 -16.367 9.862   1.00  8.90  ? 218 VAL A O   1 
ATOM   1767 C  CB  . VAL A 1 217 ? -17.098 -13.046 9.539   1.00  9.10  ? 218 VAL A CB  1 
ATOM   1768 C  CG1 . VAL A 1 217 ? -17.405 -11.697 10.180  1.00  10.22 ? 218 VAL A CG1 1 
ATOM   1769 C  CG2 . VAL A 1 217 ? -15.793 -13.670 10.035  1.00  10.23 ? 218 VAL A CG2 1 
ATOM   1770 N  N   . SER A 1 218 ? -18.227 -15.527 7.869   1.00  7.86  ? 219 SER A N   1 
ATOM   1771 C  CA  . SER A 1 218 ? -17.937 -16.855 7.286   1.00  9.07  ? 219 SER A CA  1 
ATOM   1772 C  C   . SER A 1 218 ? -16.482 -17.109 6.977   1.00  9.82  ? 219 SER A C   1 
ATOM   1773 O  O   . SER A 1 218 ? -15.626 -16.159 6.878   1.00  8.24  ? 219 SER A O   1 
ATOM   1774 C  CB  . SER A 1 218 ? -18.776 -17.029 6.006   1.00  9.81  ? 219 SER A CB  1 
ATOM   1775 O  OG  . SER A 1 218 ? -18.249 -16.161 4.985   1.00  10.81 ? 219 SER A OG  1 
ATOM   1776 N  N   . SER A 1 219 ? -16.125 -18.399 6.824   1.00  10.17 ? 220 SER A N   1 
ATOM   1777 C  CA  . SER A 1 219 ? -14.794 -18.738 6.433   1.00  11.83 ? 220 SER A CA  1 
ATOM   1778 C  C   . SER A 1 219 ? -14.448 -18.046 5.136   1.00  12.64 ? 220 SER A C   1 
ATOM   1779 O  O   . SER A 1 219 ? -13.324 -17.573 4.972   1.00  12.66 ? 220 SER A O   1 
ATOM   1780 C  CB  . SER A 1 219 ? -14.625 -20.282 6.377   1.00  13.22 ? 220 SER A CB  1 
ATOM   1781 O  OG  . SER A 1 219 ? -15.656 -20.768 5.516   1.00  18.72 ? 220 SER A OG  1 
ATOM   1782 N  N   . GLU A 1 220 ? -15.405 -17.907 4.203   1.00  12.62 ? 221 GLU A N   1 
ATOM   1783 C  CA  . GLU A 1 220 ? -15.035 -17.292 2.927   1.00  13.34 ? 221 GLU A CA  1 
ATOM   1784 C  C   . GLU A 1 220 ? -14.785 -15.781 3.100   1.00  12.10 ? 221 GLU A C   1 
ATOM   1785 O  O   . GLU A 1 220 ? -13.930 -15.254 2.404   1.00  12.17 ? 221 GLU A O   1 
ATOM   1786 C  CB  . GLU A 1 220 ? -16.106 -17.463 1.883   1.00  15.87 ? 221 GLU A CB  1 
ATOM   1787 C  CG  . GLU A 1 220 ? -16.331 -18.962 1.549   1.00  20.15 ? 221 GLU A CG  1 
ATOM   1788 C  CD  . GLU A 1 220 ? -17.527 -19.559 2.301   1.00  22.76 ? 221 GLU A CD  1 
ATOM   1789 O  OE1 . GLU A 1 220 ? -17.945 -19.153 3.406   1.00  20.03 ? 221 GLU A OE1 1 
ATOM   1790 O  OE2 . GLU A 1 220 ? -18.106 -20.548 1.793   1.00  28.01 ? 221 GLU A OE2 1 
ATOM   1791 N  N   . GLN A 1 221 ? -15.504 -15.130 4.018   1.00  9.63  ? 222 GLN A N   1 
ATOM   1792 C  CA  . GLN A 1 221 ? -15.256 -13.695 4.234   1.00  9.36  ? 222 GLN A CA  1 
ATOM   1793 C  C   . GLN A 1 221 ? -13.809 -13.516 4.757   1.00  10.32 ? 222 GLN A C   1 
ATOM   1794 O  O   . GLN A 1 221 ? -13.042 -12.659 4.262   1.00  9.75  ? 222 GLN A O   1 
ATOM   1795 C  CB  . GLN A 1 221 ? -16.271 -13.177 5.223   1.00  8.44  ? 222 GLN A CB  1 
ATOM   1796 C  CG  . GLN A 1 221 ? -17.605 -13.059 4.492   1.00  8.04  ? 222 GLN A CG  1 
ATOM   1797 C  CD  . GLN A 1 221 ? -18.730 -12.496 5.356   1.00  8.17  ? 222 GLN A CD  1 
ATOM   1798 O  OE1 . GLN A 1 221 ? -18.880 -12.879 6.511   1.00  9.16  ? 222 GLN A OE1 1 
ATOM   1799 N  NE2 . GLN A 1 221 ? -19.546 -11.572 4.800   1.00  9.16  ? 222 GLN A NE2 1 
ATOM   1800 N  N   . VAL A 1 222 ? -13.409 -14.283 5.766   1.00  10.45 ? 223 VAL A N   1 
ATOM   1801 C  CA  . VAL A 1 222 ? -12.078 -14.072 6.321   1.00  10.89 ? 223 VAL A CA  1 
ATOM   1802 C  C   . VAL A 1 222 ? -10.941 -14.534 5.335   1.00  11.92 ? 223 VAL A C   1 
ATOM   1803 O  O   . VAL A 1 222 ? -9.858  -13.978 5.270   1.00  12.00 ? 223 VAL A O   1 
ATOM   1804 C  CB  . VAL A 1 222 ? -11.935 -14.641 7.758   1.00  13.55 ? 223 VAL A CB  1 
ATOM   1805 C  CG1 . VAL A 1 222 ? -11.966 -16.146 7.724   1.00  15.55 ? 223 VAL A CG1 1 
ATOM   1806 C  CG2 . VAL A 1 222 ? -10.624 -14.111 8.404   1.00  14.34 ? 223 VAL A CG2 1 
ATOM   1807 N  N   . LEU A 1 223 ? -11.260 -15.521 4.515   1.00  12.75 ? 224 LEU A N   1 
ATOM   1808 C  CA  . LEU A 1 223 ? -10.317 -15.955 3.501   1.00  13.69 ? 224 LEU A CA  1 
ATOM   1809 C  C   . LEU A 1 223 ? -10.016 -14.840 2.578   1.00  13.65 ? 224 LEU A C   1 
ATOM   1810 O  O   . LEU A 1 223 ? -8.855  -14.755 2.146   1.00  14.58 ? 224 LEU A O   1 
ATOM   1811 C  CB  . LEU A 1 223 ? -10.868 -17.201 2.760   1.00  16.52 ? 224 LEU A CB  1 
ATOM   1812 C  CG  . LEU A 1 223 ? -10.668 -18.494 3.564   1.00  19.56 ? 224 LEU A CG  1 
ATOM   1813 C  CD1 . LEU A 1 223 ? -11.533 -19.656 3.011   1.00  25.13 ? 224 LEU A CD1 1 
ATOM   1814 C  CD2 . LEU A 1 223 ? -9.184  -18.868 3.631   1.00  21.91 ? 224 LEU A CD2 1 
ATOM   1815 N  N   . LYS A 1 224 ? -11.011 -14.009 2.287   1.00  12.62 ? 225 LYS A N   1 
ATOM   1816 C  CA  . LYS A 1 224 ? -10.777 -12.872 1.390   1.00  13.16 ? 225 LYS A CA  1 
ATOM   1817 C  C   . LYS A 1 224 ? -9.878  -11.808 2.047   1.00  12.95 ? 225 LYS A C   1 
ATOM   1818 O  O   . LYS A 1 224 ? -9.026  -11.241 1.387   1.00  12.45 ? 225 LYS A O   1 
ATOM   1819 C  CB  . LYS A 1 224 ? -12.072 -12.311 0.753   1.00  14.86 ? 225 LYS A CB  1 
ATOM   1820 C  CG  . LYS A 1 224 ? -12.683 -13.355 -0.290  1.00  19.75 ? 225 LYS A CG  1 
ATOM   1821 C  CD  . LYS A 1 224 ? -13.870 -12.841 -1.095  1.00  26.91 ? 225 LYS A CD  1 
ATOM   1822 C  CE  . LYS A 1 224 ? -14.692 -14.050 -1.634  1.00  29.77 ? 225 LYS A CE  1 
ATOM   1823 N  NZ  . LYS A 1 224 ? -15.855 -13.740 -2.559  1.00  36.47 ? 225 LYS A NZ  1 
ATOM   1824 N  N   . PHE A 1 225 ? -9.991  -11.580 3.371   1.00  10.55 ? 226 PHE A N   1 
ATOM   1825 C  CA  . PHE A 1 225 ? -9.039  -10.707 4.033   1.00  9.70  ? 226 PHE A CA  1 
ATOM   1826 C  C   . PHE A 1 225 ? -7.594  -11.208 3.836   1.00  10.71 ? 226 PHE A C   1 
ATOM   1827 O  O   . PHE A 1 225 ? -6.667  -10.397 3.633   1.00  10.54 ? 226 PHE A O   1 
ATOM   1828 C  CB  . PHE A 1 225 ? -9.209  -10.738 5.599   1.00  10.32 ? 226 PHE A CB  1 
ATOM   1829 C  CG  . PHE A 1 225 ? -10.411 -9.998  6.157   1.00  10.37 ? 226 PHE A CG  1 
ATOM   1830 C  CD1 . PHE A 1 225 ? -11.452 -9.526  5.370   1.00  11.83 ? 226 PHE A CD1 1 
ATOM   1831 C  CD2 . PHE A 1 225 ? -10.479 -9.791  7.528   1.00  11.62 ? 226 PHE A CD2 1 
ATOM   1832 C  CE1 . PHE A 1 225 ? -12.528 -8.861  5.953   1.00  13.87 ? 226 PHE A CE1 1 
ATOM   1833 C  CE2 . PHE A 1 225 ? -11.544 -9.132  8.112   1.00  12.84 ? 226 PHE A CE2 1 
ATOM   1834 C  CZ  . PHE A 1 225 ? -12.573 -8.666  7.324   1.00  12.47 ? 226 PHE A CZ  1 
ATOM   1835 N  N   . ARG A 1 226 ? -7.394  -12.532 3.899   1.00  10.55 ? 227 ARG A N   1 
ATOM   1836 C  CA  . ARG A 1 226 ? -6.058  -13.117 3.766   1.00  10.34 ? 227 ARG A CA  1 
ATOM   1837 C  C   . ARG A 1 226 ? -5.514  -13.142 2.336   1.00  10.57 ? 227 ARG A C   1 
ATOM   1838 O  O   . ARG A 1 226 ? -4.359  -13.500 2.213   1.00  12.83 ? 227 ARG A O   1 
ATOM   1839 C  CB  . ARG A 1 226 ? -6.054  -14.556 4.273   1.00  10.68 ? 227 ARG A CB  1 
ATOM   1840 C  CG  . ARG A 1 226 ? -6.521  -14.718 5.741   1.00  11.20 ? 227 ARG A CG  1 
ATOM   1841 C  CD  . ARG A 1 226 ? -6.532  -16.208 6.162   1.00  11.61 ? 227 ARG A CD  1 
ATOM   1842 N  NE  . ARG A 1 226 ? -7.058  -16.324 7.539   1.00  11.37 ? 227 ARG A NE  1 
ATOM   1843 C  CZ  . ARG A 1 226 ? -7.993  -17.176 7.962   1.00  10.59 ? 227 ARG A CZ  1 
ATOM   1844 N  NH1 . ARG A 1 226 ? -8.437  -18.160 7.131   1.00  13.23 ? 227 ARG A NH1 1 
ATOM   1845 N  NH2 . ARG A 1 226 ? -8.417  -17.160 9.184   1.00  10.65 ? 227 ARG A NH2 1 
ATOM   1846 N  N   . LYS A 1 227 ? -6.279  -12.643 1.393   1.00  11.66 ? 228 LYS A N   1 
ATOM   1847 C  CA  . LYS A 1 227 ? -5.726  -12.504 0.023   1.00  13.70 ? 228 LYS A CA  1 
ATOM   1848 C  C   . LYS A 1 227 ? -5.113  -11.171 -0.197  1.00  13.64 ? 228 LYS A C   1 
ATOM   1849 O  O   . LYS A 1 227 ? -4.451  -10.933 -1.224  1.00  15.47 ? 228 LYS A O   1 
ATOM   1850 C  CB  . LYS A 1 227 ? -6.815  -12.810 -1.026  1.00  13.44 ? 228 LYS A CB  1 
ATOM   1851 C  CG  . LYS A 1 227 ? -7.254  -14.274 -1.074  1.00  16.56 ? 228 LYS A CG  1 
ATOM   1852 C  CD  . LYS A 1 227 ? -8.454  -14.410 -2.010  1.00  22.08 ? 228 LYS A CD  1 
ATOM   1853 C  CE  . LYS A 1 227 ? -8.145  -15.197 -3.289  1.00  31.35 ? 228 LYS A CE  1 
ATOM   1854 N  NZ  . LYS A 1 227 ? -8.835  -16.545 -3.271  1.00  35.52 ? 228 LYS A NZ  1 
ATOM   1855 N  N   . LEU A 1 228 ? -5.323  -10.219 0.740   1.00  11.36 ? 229 LEU A N   1 
ATOM   1856 C  CA  . LEU A 1 228 ? -4.613  -8.954  0.625   1.00  11.47 ? 229 LEU A CA  1 
ATOM   1857 C  C   . LEU A 1 228 ? -3.100  -9.113  0.797   1.00  11.81 ? 229 LEU A C   1 
ATOM   1858 O  O   . LEU A 1 228 ? -2.592  -10.101 1.208   1.00  12.08 ? 229 LEU A O   1 
ATOM   1859 C  CB  . LEU A 1 228 ? -5.149  -7.975  1.689   1.00  10.69 ? 229 LEU A CB  1 
ATOM   1860 C  CG  . LEU A 1 228 ? -6.585  -7.577  1.492   1.00  9.96  ? 229 LEU A CG  1 
ATOM   1861 C  CD1 . LEU A 1 228 ? -7.006  -7.038  2.857   1.00  12.26 ? 229 LEU A CD1 1 
ATOM   1862 C  CD2 . LEU A 1 228 ? -6.705  -6.493  0.444   1.00  10.28 ? 229 LEU A CD2 1 
ATOM   1863 N  N   . ASN A 1 229 ? -2.386  -8.023  0.478   1.00  14.87 ? 230 ASN A N   1 
ATOM   1864 C  CA  . ASN A 1 229 ? -0.992  -7.993  0.429   1.00  13.53 ? 230 ASN A CA  1 
ATOM   1865 C  C   . ASN A 1 229 ? -0.426  -6.851  1.281   1.00  13.02 ? 230 ASN A C   1 
ATOM   1866 O  O   . ASN A 1 229 ? -0.935  -5.737  1.195   1.00  13.82 ? 230 ASN A O   1 
ATOM   1867 C  CB  . ASN A 1 229 ? -0.579  -7.727  -1.050  1.00  15.90 ? 230 ASN A CB  1 
ATOM   1868 C  CG  . ASN A 1 229 ? -0.459  -8.990  -1.927  1.00  18.98 ? 230 ASN A CG  1 
ATOM   1869 O  OD1 . ASN A 1 229 ? 0.226   -8.887  -2.985  1.00  20.94 ? 230 ASN A OD1 1 
ATOM   1870 N  ND2 . ASN A 1 229 ? -1.070  -10.135 -1.550  1.00  15.78 ? 230 ASN A ND2 1 
ATOM   1871 N  N   . PHE A 1 230 ? 0.655   -7.161  1.984   1.00  13.78 ? 231 PHE A N   1 
ATOM   1872 C  CA  . PHE A 1 230 ? 1.374   -6.094  2.708   1.00  15.07 ? 231 PHE A CA  1 
ATOM   1873 C  C   . PHE A 1 230 ? 2.238   -5.265  1.763   1.00  17.38 ? 231 PHE A C   1 
ATOM   1874 O  O   . PHE A 1 230 ? 2.515   -4.082  2.041   1.00  15.44 ? 231 PHE A O   1 
ATOM   1875 C  CB  . PHE A 1 230 ? 2.357   -6.643  3.695   1.00  13.29 ? 231 PHE A CB  1 
ATOM   1876 C  CG  . PHE A 1 230 ? 1.761   -7.261  4.990   1.00  13.34 ? 231 PHE A CG  1 
ATOM   1877 C  CD1 . PHE A 1 230 ? 0.965   -6.485  5.873   1.00  12.54 ? 231 PHE A CD1 1 
ATOM   1878 C  CD2 . PHE A 1 230 ? 2.154   -8.545  5.340   1.00  13.29 ? 231 PHE A CD2 1 
ATOM   1879 C  CE1 . PHE A 1 230 ? 0.500   -7.062  7.101   1.00  13.14 ? 231 PHE A CE1 1 
ATOM   1880 C  CE2 . PHE A 1 230 ? 1.697   -9.135  6.561   1.00  12.86 ? 231 PHE A CE2 1 
ATOM   1881 C  CZ  . PHE A 1 230 ? 0.933   -8.365  7.434   1.00  12.18 ? 231 PHE A CZ  1 
ATOM   1882 N  N   . ASN A 1 231 ? 2.695   -5.928  0.707   1.00  16.54 ? 232 ASN A N   1 
ATOM   1883 C  CA  . ASN A 1 231 ? 3.568   -5.269  -0.276  1.00  18.53 ? 232 ASN A CA  1 
ATOM   1884 C  C   . ASN A 1 231 ? 2.818   -4.365  -1.231  1.00  17.19 ? 232 ASN A C   1 
ATOM   1885 O  O   . ASN A 1 231 ? 1.601   -4.452  -1.376  1.00  15.48 ? 232 ASN A O   1 
ATOM   1886 C  CB  . ASN A 1 231 ? 4.232   -6.370  -1.040  1.00  17.63 ? 232 ASN A CB  1 
ATOM   1887 C  CG  . ASN A 1 231 ? 3.238   -7.280  -1.667  1.00  17.03 ? 232 ASN A CG  1 
ATOM   1888 O  OD1 . ASN A 1 231 ? 2.752   -8.200  -1.021  1.00  19.78 ? 232 ASN A OD1 1 
ATOM   1889 N  ND2 . ASN A 1 231 ? 2.909   -7.064  -2.981  1.00  18.48 ? 232 ASN A ND2 1 
ATOM   1890 N  N   . GLY A 1 232 ? 3.575   -3.463  -1.906  1.00  17.20 ? 233 GLY A N   1 
ATOM   1891 C  CA  . GLY A 1 232 ? 3.003   -2.618  -2.966  1.00  20.65 ? 233 GLY A CA  1 
ATOM   1892 C  C   . GLY A 1 232 ? 3.011   -3.395  -4.278  1.00  19.75 ? 233 GLY A C   1 
ATOM   1893 O  O   . GLY A 1 232 ? 3.675   -4.416  -4.365  1.00  20.08 ? 233 GLY A O   1 
ATOM   1894 N  N   A GLU A 1 233 ? 2.223   -2.919  -5.255  0.50  18.83 ? 234 GLU A N   1 
ATOM   1895 N  N   B GLU A 1 233 ? 2.264   -2.908  -5.279  0.50  22.56 ? 234 GLU A N   1 
ATOM   1896 C  CA  A GLU A 1 233 ? 2.132   -3.530  -6.575  0.50  18.38 ? 234 GLU A CA  1 
ATOM   1897 C  CA  B GLU A 1 233 ? 2.063   -3.597  -6.569  0.50  24.24 ? 234 GLU A CA  1 
ATOM   1898 C  C   A GLU A 1 233 ? 3.509   -3.523  -7.222  0.50  16.10 ? 234 GLU A C   1 
ATOM   1899 C  C   B GLU A 1 233 ? 3.371   -4.006  -7.256  0.50  25.10 ? 234 GLU A C   1 
ATOM   1900 O  O   A GLU A 1 233 ? 4.224   -2.542  -7.127  0.50  16.07 ? 234 GLU A O   1 
ATOM   1901 O  O   B GLU A 1 233 ? 3.462   -5.068  -7.910  0.50  22.75 ? 234 GLU A O   1 
ATOM   1902 C  CB  A GLU A 1 233 ? 1.129   -2.746  -7.431  0.50  18.25 ? 234 GLU A CB  1 
ATOM   1903 C  CB  B GLU A 1 233 ? 1.223   -2.699  -7.492  0.50  25.47 ? 234 GLU A CB  1 
ATOM   1904 C  CG  A GLU A 1 233 ? 0.844   -3.359  -8.796  0.50  20.02 ? 234 GLU A CG  1 
ATOM   1905 C  CG  B GLU A 1 233 ? 0.816   -3.334  -8.817  0.50  27.86 ? 234 GLU A CG  1 
ATOM   1906 C  CD  A GLU A 1 233 ? -0.024  -2.471  -9.671  0.50  25.52 ? 234 GLU A CD  1 
ATOM   1907 C  CD  B GLU A 1 233 ? -0.065  -2.420  -9.662  0.50  34.88 ? 234 GLU A CD  1 
ATOM   1908 O  OE1 A GLU A 1 233 ? -0.372  -1.323  -9.242  0.50  26.57 ? 234 GLU A OE1 1 
ATOM   1909 O  OE1 B GLU A 1 233 ? -0.350  -1.265  -9.232  0.50  35.93 ? 234 GLU A OE1 1 
ATOM   1910 O  OE2 A GLU A 1 233 ? -0.357  -2.929  -10.804 0.50  27.40 ? 234 GLU A OE2 1 
ATOM   1911 O  OE2 B GLU A 1 233 ? -0.480  -2.860  -10.768 0.50  36.87 ? 234 GLU A OE2 1 
ATOM   1912 N  N   A GLY A 1 234 ? 3.883   -4.694  -7.748  0.50  17.91 ? 235 GLY A N   1 
ATOM   1913 N  N   B GLY A 1 234 ? 4.402   -3.212  -7.046  0.50  24.12 ? 235 GLY A N   1 
ATOM   1914 C  CA  A GLY A 1 234 ? 5.124   -4.880  -8.475  0.50  21.37 ? 235 GLY A CA  1 
ATOM   1915 C  CA  B GLY A 1 234 ? 5.649   -3.506  -7.685  0.50  27.45 ? 235 GLY A CA  1 
ATOM   1916 C  C   A GLY A 1 234 ? 6.145   -5.536  -7.586  0.50  26.00 ? 235 GLY A C   1 
ATOM   1917 C  C   B GLY A 1 234 ? 6.410   -4.738  -7.234  0.50  26.00 ? 235 GLY A C   1 
ATOM   1918 O  O   A GLY A 1 234 ? 7.166   -6.023  -8.053  0.50  27.37 ? 235 GLY A O   1 
ATOM   1919 O  O   B GLY A 1 234 ? 7.474   -4.972  -7.793  0.50  24.47 ? 235 GLY A O   1 
ATOM   1920 N  N   . GLU A 1 235 ? 5.884   -5.544  -6.287  1.00  28.44 ? 236 GLU A N   1 
ATOM   1921 C  CA  . GLU A 1 235 ? 6.746   -6.285  -5.344  1.00  27.57 ? 236 GLU A CA  1 
ATOM   1922 C  C   . GLU A 1 235 ? 6.335   -7.718  -5.068  1.00  29.53 ? 236 GLU A C   1 
ATOM   1923 O  O   . GLU A 1 235 ? 5.213   -8.156  -5.411  1.00  29.36 ? 236 GLU A O   1 
ATOM   1924 C  CB  . GLU A 1 235 ? 6.837   -5.516  -4.018  1.00  33.94 ? 236 GLU A CB  1 
ATOM   1925 C  CG  . GLU A 1 235 ? 7.711   -4.286  -4.119  1.00  40.14 ? 236 GLU A CG  1 
ATOM   1926 C  CD  . GLU A 1 235 ? 7.228   -3.136  -3.269  1.00  48.19 ? 236 GLU A CD  1 
ATOM   1927 O  OE1 . GLU A 1 235 ? 6.144   -3.233  -2.636  1.00  55.47 ? 236 GLU A OE1 1 
ATOM   1928 O  OE2 . GLU A 1 235 ? 7.948   -2.126  -3.228  1.00  56.09 ? 236 GLU A OE2 1 
ATOM   1929 N  N   . PRO A 1 236 ? 7.262   -8.474  -4.467  1.00  25.91 ? 237 PRO A N   1 
ATOM   1930 C  CA  . PRO A 1 236 ? 7.114   -9.886  -4.148  1.00  28.61 ? 237 PRO A CA  1 
ATOM   1931 C  C   . PRO A 1 236 ? 5.911   -9.990  -3.181  1.00  26.67 ? 237 PRO A C   1 
ATOM   1932 O  O   . PRO A 1 236 ? 5.791   -9.146  -2.277  1.00  24.71 ? 237 PRO A O   1 
ATOM   1933 C  CB  . PRO A 1 236 ? 8.419   -10.225 -3.406  1.00  31.40 ? 237 PRO A CB  1 
ATOM   1934 C  CG  . PRO A 1 236 ? 9.381   -9.121  -3.728  1.00  30.61 ? 237 PRO A CG  1 
ATOM   1935 C  CD  . PRO A 1 236 ? 8.553   -7.908  -4.019  1.00  31.67 ? 237 PRO A CD  1 
ATOM   1936 N  N   . GLU A 1 237 ? 5.078   -11.008 -3.384  1.00  25.91 ? 238 GLU A N   1 
ATOM   1937 C  CA  . GLU A 1 237 ? 3.819   -11.077 -2.659  1.00  23.43 ? 238 GLU A CA  1 
ATOM   1938 C  C   . GLU A 1 237 ? 4.088   -11.518 -1.199  1.00  22.82 ? 238 GLU A C   1 
ATOM   1939 O  O   . GLU A 1 237 ? 4.608   -12.571 -0.952  1.00  19.53 ? 238 GLU A O   1 
ATOM   1940 C  CB  . GLU A 1 237 ? 2.844   -12.046 -3.335  1.00  23.34 ? 238 GLU A CB  1 
ATOM   1941 C  CG  . GLU A 1 237 ? 1.554   -12.176 -2.538  1.00  22.67 ? 238 GLU A CG  1 
ATOM   1942 C  CD  . GLU A 1 237 ? 0.440   -12.845 -3.304  1.00  23.23 ? 238 GLU A CD  1 
ATOM   1943 O  OE1 . GLU A 1 237 ? 0.730   -13.900 -3.942  1.00  28.35 ? 238 GLU A OE1 1 
ATOM   1944 O  OE2 . GLU A 1 237 ? -0.710  -12.335 -3.291  1.00  20.73 ? 238 GLU A OE2 1 
ATOM   1945 N  N   . GLU A 1 238 ? 3.628   -10.708 -0.248  1.00  19.93 ? 239 GLU A N   1 
ATOM   1946 C  CA  . GLU A 1 238 ? 3.635   -11.099 1.172   1.00  21.04 ? 239 GLU A CA  1 
ATOM   1947 C  C   . GLU A 1 238 ? 2.185   -10.967 1.632   1.00  14.01 ? 239 GLU A C   1 
ATOM   1948 O  O   . GLU A 1 238 ? 1.585   -9.854  1.616   1.00  15.17 ? 239 GLU A O   1 
ATOM   1949 C  CB  . GLU A 1 238 ? 4.471   -10.122 2.016   1.00  21.84 ? 239 GLU A CB  1 
ATOM   1950 C  CG  . GLU A 1 238 ? 5.852   -9.748  1.492   1.00  32.90 ? 239 GLU A CG  1 
ATOM   1951 C  CD  . GLU A 1 238 ? 6.393   -8.437  2.131   1.00  43.52 ? 239 GLU A CD  1 
ATOM   1952 O  OE1 . GLU A 1 238 ? 6.060   -8.119  3.318   1.00  46.97 ? 239 GLU A OE1 1 
ATOM   1953 O  OE2 . GLU A 1 238 ? 7.128   -7.701  1.428   1.00  46.91 ? 239 GLU A OE2 1 
ATOM   1954 N  N   . LEU A 1 239 ? 1.575   -12.123 1.942   1.00  14.33 ? 240 LEU A N   1 
ATOM   1955 C  CA  . LEU A 1 239 ? 0.094   -12.025 2.215   1.00  12.53 ? 240 LEU A CA  1 
ATOM   1956 C  C   . LEU A 1 239 ? -0.109  -11.241 3.542   1.00  12.06 ? 240 LEU A C   1 
ATOM   1957 O  O   . LEU A 1 239 ? 0.677   -11.405 4.500   1.00  13.15 ? 240 LEU A O   1 
ATOM   1958 C  CB  . LEU A 1 239 ? -0.472  -13.437 2.440   1.00  13.40 ? 240 LEU A CB  1 
ATOM   1959 C  CG  . LEU A 1 239 ? -0.541  -14.358 1.226   1.00  13.85 ? 240 LEU A CG  1 
ATOM   1960 C  CD1 . LEU A 1 239 ? -1.286  -15.619 1.655   1.00  17.19 ? 240 LEU A CD1 1 
ATOM   1961 C  CD2 . LEU A 1 239 ? -1.308  -13.665 0.124   1.00  13.21 ? 240 LEU A CD2 1 
ATOM   1962 N  N   . MET A 1 240 ? -1.165  -10.443 3.529   1.00  11.03 ? 241 MET A N   1 
ATOM   1963 C  CA  . MET A 1 240 ? -1.518  -9.598  4.722   1.00  10.52 ? 241 MET A CA  1 
ATOM   1964 C  C   . MET A 1 240 ? -2.277  -10.546 5.653   1.00  10.32 ? 241 MET A C   1 
ATOM   1965 O  O   . MET A 1 240 ? -3.478  -10.710 5.528   1.00  10.58 ? 241 MET A O   1 
ATOM   1966 C  CB  . MET A 1 240 ? -2.320  -8.414  4.284   1.00  12.53 ? 241 MET A CB  1 
ATOM   1967 C  CG  . MET A 1 240 ? -2.660  -7.474  5.493   1.00  11.34 ? 241 MET A CG  1 
ATOM   1968 S  SD  . MET A 1 240 ? -3.589  -6.073  4.986   1.00  13.05 ? 241 MET A SD  1 
ATOM   1969 C  CE  . MET A 1 240 ? -2.266  -4.977  4.395   1.00  12.03 ? 241 MET A CE  1 
ATOM   1970 N  N   . VAL A 1 241 ? -1.468  -11.196 6.497   1.00  9.77  ? 242 VAL A N   1 
ATOM   1971 C  CA  . VAL A 1 241 ? -2.046  -12.094 7.568   1.00  9.43  ? 242 VAL A CA  1 
ATOM   1972 C  C   . VAL A 1 241 ? -1.226  -11.868 8.856   1.00  9.88  ? 242 VAL A C   1 
ATOM   1973 O  O   . VAL A 1 241 ? -0.058  -11.397 8.830   1.00  9.86  ? 242 VAL A O   1 
ATOM   1974 C  CB  . VAL A 1 241 ? -1.971  -13.596 7.221   1.00  9.88  ? 242 VAL A CB  1 
ATOM   1975 C  CG1 . VAL A 1 241 ? -2.898  -13.884 6.003   1.00  9.39  ? 242 VAL A CG1 1 
ATOM   1976 C  CG2 . VAL A 1 241 ? -0.527  -14.069 7.013   1.00  11.46 ? 242 VAL A CG2 1 
ATOM   1977 N  N   . ASP A 1 242 ? -1.854  -12.117 10.003  1.00  7.91  ? 243 ASP A N   1 
ATOM   1978 C  CA  . ASP A 1 242 ? -1.150  -11.985 11.252  1.00  7.95  ? 243 ASP A CA  1 
ATOM   1979 C  C   . ASP A 1 242 ? -0.665  -10.571 11.490  1.00  7.74  ? 243 ASP A C   1 
ATOM   1980 O  O   . ASP A 1 242 ? 0.420   -10.359 12.041  1.00  8.81  ? 243 ASP A O   1 
ATOM   1981 C  CB  . ASP A 1 242 ? -0.069  -13.062 11.519  1.00  7.97  ? 243 ASP A CB  1 
ATOM   1982 C  CG  . ASP A 1 242 ? -0.654  -14.433 11.624  1.00  9.37  ? 243 ASP A CG  1 
ATOM   1983 O  OD1 . ASP A 1 242 ? -1.714  -14.633 12.238  1.00  8.53  ? 243 ASP A OD1 1 
ATOM   1984 O  OD2 . ASP A 1 242 ? -0.014  -15.365 11.031  1.00  9.90  ? 243 ASP A OD2 1 
ATOM   1985 N  N   . ASN A 1 243 ? -1.569  -9.621  11.218  1.00  6.99  ? 244 ASN A N   1 
ATOM   1986 C  CA  . ASN A 1 243 ? -1.280  -8.186  11.468  1.00  7.48  ? 244 ASN A CA  1 
ATOM   1987 C  C   . ASN A 1 243 ? -1.873  -7.782  12.836  1.00  7.44  ? 244 ASN A C   1 
ATOM   1988 O  O   . ASN A 1 243 ? -2.552  -6.748  12.931  1.00  7.52  ? 244 ASN A O   1 
ATOM   1989 C  CB  . ASN A 1 243 ? -1.856  -7.324  10.332  1.00  8.69  ? 244 ASN A CB  1 
ATOM   1990 C  CG  . ASN A 1 243 ? -3.335  -7.564  10.076  1.00  9.46  ? 244 ASN A CG  1 
ATOM   1991 O  OD1 . ASN A 1 243 ? -4.009  -8.413  10.689  1.00  8.59  ? 244 ASN A OD1 1 
ATOM   1992 N  ND2 . ASN A 1 243 ? -3.915  -6.702  9.224   1.00  13.04 ? 244 ASN A ND2 1 
ATOM   1993 N  N   . TRP A 1 244 ? -1.572  -8.558  13.842  1.00  6.33  ? 245 TRP A N   1 
ATOM   1994 C  CA  . TRP A 1 244 ? -2.026  -8.295  15.211  1.00  6.22  ? 245 TRP A CA  1 
ATOM   1995 C  C   . TRP A 1 244 ? -0.860  -8.190  16.144  1.00  7.08  ? 245 TRP A C   1 
ATOM   1996 O  O   . TRP A 1 244 ? 0.159   -8.903  15.995  1.00  7.42  ? 245 TRP A O   1 
ATOM   1997 C  CB  . TRP A 1 244 ? -3.020  -9.406  15.686  1.00  7.02  ? 245 TRP A CB  1 
ATOM   1998 C  CG  . TRP A 1 244 ? -2.524  -10.831 15.507  1.00  6.02  ? 245 TRP A CG  1 
ATOM   1999 C  CD1 . TRP A 1 244 ? -2.664  -11.589 14.376  1.00  7.09  ? 245 TRP A CD1 1 
ATOM   2000 C  CD2 . TRP A 1 244 ? -1.943  -11.696 16.530  1.00  6.80  ? 245 TRP A CD2 1 
ATOM   2001 N  NE1 . TRP A 1 244 ? -2.137  -12.860 14.618  1.00  6.77  ? 245 TRP A NE1 1 
ATOM   2002 C  CE2 . TRP A 1 244 ? -1.685  -12.955 15.887  1.00  6.60  ? 245 TRP A CE2 1 
ATOM   2003 C  CE3 . TRP A 1 244 ? -1.633  -11.546 17.881  1.00  7.79  ? 245 TRP A CE3 1 
ATOM   2004 C  CZ2 . TRP A 1 244 ? -1.099  -14.021 16.570  1.00  7.31  ? 245 TRP A CZ2 1 
ATOM   2005 C  CZ3 . TRP A 1 244 ? -1.038  -12.614 18.565  1.00  7.87  ? 245 TRP A CZ3 1 
ATOM   2006 C  CH2 . TRP A 1 244 ? -0.841  -13.856 17.915  1.00  8.06  ? 245 TRP A CH2 1 
ATOM   2007 N  N   . ARG A 1 245 ? -0.986  -7.300  17.130  1.00  6.41  ? 246 ARG A N   1 
ATOM   2008 C  CA  . ARG A 1 245 ? -0.004  -7.175  18.217  1.00  6.50  ? 246 ARG A CA  1 
ATOM   2009 C  C   . ARG A 1 245 ? -0.469  -8.104  19.361  1.00  6.26  ? 246 ARG A C   1 
ATOM   2010 O  O   . ARG A 1 245 ? -1.648  -8.093  19.651  1.00  6.61  ? 246 ARG A O   1 
ATOM   2011 C  CB  . ARG A 1 245 ? 0.013   -5.734  18.759  1.00  6.05  ? 246 ARG A CB  1 
ATOM   2012 C  CG  . ARG A 1 245 ? 1.122   -5.526  19.769  1.00  6.32  ? 246 ARG A CG  1 
ATOM   2013 C  CD  . ARG A 1 245 ? 1.035   -4.109  20.323  1.00  6.32  ? 246 ARG A CD  1 
ATOM   2014 N  NE  . ARG A 1 245 ? 2.295   -3.791  21.010  1.00  7.97  ? 246 ARG A NE  1 
ATOM   2015 C  CZ  . ARG A 1 245 ? 2.488   -2.815  21.897  1.00  7.98  ? 246 ARG A CZ  1 
ATOM   2016 N  NH1 . ARG A 1 245 ? 1.507   -1.993  22.246  1.00  8.24  ? 246 ARG A NH1 1 
ATOM   2017 N  NH2 . ARG A 1 245 ? 3.689   -2.663  22.441  1.00  8.48  ? 246 ARG A NH2 1 
ATOM   2018 N  N   . PRO A 1 246 ? 0.361   -8.947  20.008  1.00  7.61  ? 247 PRO A N   1 
ATOM   2019 C  CA  . PRO A 1 246 ? -0.075  -9.785  21.093  1.00  7.02  ? 247 PRO A CA  1 
ATOM   2020 C  C   . PRO A 1 246 ? -0.367  -8.961  22.357  1.00  6.52  ? 247 PRO A C   1 
ATOM   2021 O  O   . PRO A 1 246 ? -0.024  -7.762  22.482  1.00  6.69  ? 247 PRO A O   1 
ATOM   2022 C  CB  . PRO A 1 246 ? 1.176   -10.649 21.399  1.00  10.18 ? 247 PRO A CB  1 
ATOM   2023 C  CG  . PRO A 1 246 ? 2.113   -10.362 20.258  1.00  11.99 ? 247 PRO A CG  1 
ATOM   2024 C  CD  . PRO A 1 246 ? 1.787   -9.050  19.662  1.00  8.31  ? 247 PRO A CD  1 
ATOM   2025 N  N   . ALA A 1 247 ? -1.023  -9.606  23.298  1.00  7.53  ? 248 ALA A N   1 
ATOM   2026 C  CA  . ALA A 1 247 ? -1.332  -8.961  24.577  1.00  6.86  ? 248 ALA A CA  1 
ATOM   2027 C  C   . ALA A 1 247 ? -0.094  -8.453  25.287  1.00  7.41  ? 248 ALA A C   1 
ATOM   2028 O  O   . ALA A 1 247 ? 0.972   -9.125  25.259  1.00  8.94  ? 248 ALA A O   1 
ATOM   2029 C  CB  . ALA A 1 247 ? -2.079  -10.005 25.429  1.00  8.25  ? 248 ALA A CB  1 
ATOM   2030 N  N   . GLN A 1 248 ? -0.275  -7.289  25.872  1.00  7.14  ? 249 GLN A N   1 
ATOM   2031 C  CA  . GLN A 1 248 ? 0.763   -6.530  26.584  1.00  8.33  ? 249 GLN A CA  1 
ATOM   2032 C  C   . GLN A 1 248 ? 0.468   -6.542  28.078  1.00  9.10  ? 249 GLN A C   1 
ATOM   2033 O  O   . GLN A 1 248 ? -0.676  -6.759  28.516  1.00  8.39  ? 249 GLN A O   1 
ATOM   2034 C  CB  . GLN A 1 248 ? 0.821   -5.133  26.064  1.00  8.37  ? 249 GLN A CB  1 
ATOM   2035 C  CG  . GLN A 1 248 ? 1.136   -5.042  24.566  1.00  8.68  ? 249 GLN A CG  1 
ATOM   2036 C  CD  . GLN A 1 248 ? 2.474   -5.701  24.226  1.00  9.49  ? 249 GLN A CD  1 
ATOM   2037 O  OE1 . GLN A 1 248 ? 3.523   -5.367  24.832  1.00  12.65 ? 249 GLN A OE1 1 
ATOM   2038 N  NE2 . GLN A 1 248 ? 2.464   -6.632  23.285  1.00  9.22  ? 249 GLN A NE2 1 
ATOM   2039 N  N   . PRO A 1 249 ? 1.514   -6.317  28.929  1.00  11.05 ? 250 PRO A N   1 
ATOM   2040 C  CA  . PRO A 1 249 ? 1.277   -6.339  30.355  1.00  11.39 ? 250 PRO A CA  1 
ATOM   2041 C  C   . PRO A 1 249 ? 0.206   -5.336  30.825  1.00  9.73  ? 250 PRO A C   1 
ATOM   2042 O  O   . PRO A 1 249 ? 0.214   -4.178  30.400  1.00  11.42 ? 250 PRO A O   1 
ATOM   2043 C  CB  . PRO A 1 249 ? 2.688   -5.972  30.910  1.00  11.43 ? 250 PRO A CB  1 
ATOM   2044 C  CG  . PRO A 1 249 ? 3.580   -6.481  29.909  1.00  13.53 ? 250 PRO A CG  1 
ATOM   2045 C  CD  . PRO A 1 249 ? 2.919   -6.071  28.589  1.00  11.89 ? 250 PRO A CD  1 
ATOM   2046 N  N   . LEU A 1 250 ? -0.697  -5.782  31.676  1.00  10.21 ? 251 LEU A N   1 
ATOM   2047 C  CA  . LEU A 1 250 ? -1.756  -4.907  32.174  1.00  9.62  ? 251 LEU A CA  1 
ATOM   2048 C  C   . LEU A 1 250 ? -1.227  -3.813  33.097  1.00  11.39 ? 251 LEU A C   1 
ATOM   2049 O  O   . LEU A 1 250 ? -1.738  -2.695  33.157  1.00  9.30  ? 251 LEU A O   1 
ATOM   2050 C  CB  . LEU A 1 250 ? -2.815  -5.743  32.924  1.00  11.96 ? 251 LEU A CB  1 
ATOM   2051 C  CG  . LEU A 1 250 ? -4.098  -5.067  33.341  1.00  12.51 ? 251 LEU A CG  1 
ATOM   2052 C  CD1 . LEU A 1 250 ? -4.849  -4.544  32.112  1.00  11.22 ? 251 LEU A CD1 1 
ATOM   2053 C  CD2 . LEU A 1 250 ? -4.935  -6.079  34.095  1.00  16.02 ? 251 LEU A CD2 1 
ATOM   2054 N  N   . LYS A 1 251 ? -0.185  -4.165  33.859  1.00  12.02 ? 252 LYS A N   1 
ATOM   2055 C  CA  . LYS A 1 251 ? 0.523   -3.165  34.724  1.00  11.71 ? 252 LYS A CA  1 
ATOM   2056 C  C   . LYS A 1 251 ? -0.480  -2.646  35.736  1.00  12.92 ? 252 LYS A C   1 
ATOM   2057 O  O   . LYS A 1 251 ? -1.301  -3.427  36.240  1.00  14.18 ? 252 LYS A O   1 
ATOM   2058 C  CB  . LYS A 1 251 ? 1.264   -2.103  33.944  1.00  13.08 ? 252 LYS A CB  1 
ATOM   2059 C  CG  . LYS A 1 251 ? 2.391   -2.801  33.163  1.00  14.23 ? 252 LYS A CG  1 
ATOM   2060 C  CD  . LYS A 1 251 ? 3.333   -1.782  32.577  1.00  16.05 ? 252 LYS A CD  1 
ATOM   2061 C  CE  . LYS A 1 251 ? 4.539   -2.458  31.988  1.00  19.66 ? 252 LYS A CE  1 
ATOM   2062 N  NZ  . LYS A 1 251 ? 5.445   -1.530  31.293  1.00  21.11 ? 252 LYS A NZ  1 
ATOM   2063 N  N   . ASN A 1 252 ? -0.468  -1.341  35.924  1.00  12.80 ? 253 ASN A N   1 
ATOM   2064 C  CA  . ASN A 1 252 ? -1.304  -0.823  36.957  1.00  20.51 ? 253 ASN A CA  1 
ATOM   2065 C  C   . ASN A 1 252 ? -2.670  -0.406  36.433  1.00  18.71 ? 253 ASN A C   1 
ATOM   2066 O  O   . ASN A 1 252 ? -2.900  0.893   36.442  1.00  21.58 ? 253 ASN A O   1 
ATOM   2067 C  CB  . ASN A 1 252 ? -0.605  0.411   37.534  1.00  24.55 ? 253 ASN A CB  1 
ATOM   2068 C  CG  . ASN A 1 252 ? -1.279  0.931   38.777  1.00  30.36 ? 253 ASN A CG  1 
ATOM   2069 O  OD1 . ASN A 1 252 ? -1.838  0.160   39.589  1.00  34.28 ? 253 ASN A OD1 1 
ATOM   2070 N  ND2 . ASN A 1 252 ? -1.265  2.246   38.928  1.00  33.70 ? 253 ASN A ND2 1 
ATOM   2071 N  N   . ARG A 1 253 ? -3.444  -1.403  35.864  1.00  13.37 ? 254 ARG A N   1 
ATOM   2072 C  CA  . ARG A 1 253 ? -4.768  -1.087  35.313  1.00  12.01 ? 254 ARG A CA  1 
ATOM   2073 C  C   . ARG A 1 253 ? -5.839  -2.046  35.683  1.00  13.85 ? 254 ARG A C   1 
ATOM   2074 O  O   . ARG A 1 253 ? -5.559  -3.198  35.858  1.00  16.82 ? 254 ARG A O   1 
ATOM   2075 C  CB  . ARG A 1 253 ? -4.758  -0.921  33.728  1.00  11.19 ? 254 ARG A CB  1 
ATOM   2076 C  CG  . ARG A 1 253 ? -3.892  0.212   33.218  1.00  9.78  ? 254 ARG A CG  1 
ATOM   2077 C  CD  . ARG A 1 253 ? -3.783  0.154   31.704  1.00  10.08 ? 254 ARG A CD  1 
ATOM   2078 N  NE  . ARG A 1 253 ? -2.893  -0.961  31.292  1.00  8.61  ? 254 ARG A NE  1 
ATOM   2079 C  CZ  . ARG A 1 253 ? -2.647  -1.207  30.014  1.00  7.48  ? 254 ARG A CZ  1 
ATOM   2080 N  NH1 . ARG A 1 253 ? -3.287  -0.497  29.034  1.00  7.39  ? 254 ARG A NH1 1 
ATOM   2081 N  NH2 . ARG A 1 253 ? -1.827  -2.202  29.669  1.00  8.02  ? 254 ARG A NH2 1 
ATOM   2082 N  N   . GLN A 1 254 ? -7.085  -1.534  35.814  1.00  13.81 ? 255 GLN A N   1 
ATOM   2083 C  CA  . GLN A 1 254 ? -8.261  -2.396  36.089  1.00  15.30 ? 255 GLN A CA  1 
ATOM   2084 C  C   . GLN A 1 254 ? -9.197  -2.340  34.884  1.00  14.25 ? 255 GLN A C   1 
ATOM   2085 O  O   . GLN A 1 254 ? -9.426  -1.252  34.317  1.00  18.05 ? 255 GLN A O   1 
ATOM   2086 C  CB  . GLN A 1 254 ? -9.046  -1.990  37.367  1.00  20.29 ? 255 GLN A CB  1 
ATOM   2087 C  CG  . GLN A 1 254 ? -9.683  -3.269  37.946  1.00  28.44 ? 255 GLN A CG  1 
ATOM   2088 C  CD  . GLN A 1 254 ? -10.565 -3.115  39.175  1.00  31.91 ? 255 GLN A CD  1 
ATOM   2089 O  OE1 . GLN A 1 254 ? -11.333 -2.161  39.273  1.00  39.16 ? 255 GLN A OE1 1 
ATOM   2090 N  NE2 . GLN A 1 254 ? -10.526 -4.132  40.083  1.00  33.03 ? 255 GLN A NE2 1 
ATOM   2091 N  N   . ILE A 1 255 ? -9.560  -3.533  34.404  1.00  11.47 ? 256 ILE A N   1 
ATOM   2092 C  CA  . ILE A 1 255 ? -10.568 -3.601  33.347  1.00  9.92  ? 256 ILE A CA  1 
ATOM   2093 C  C   . ILE A 1 255 ? -11.977 -3.618  34.021  1.00  9.64  ? 256 ILE A C   1 
ATOM   2094 O  O   . ILE A 1 255 ? -12.177 -4.295  35.041  1.00  10.99 ? 256 ILE A O   1 
ATOM   2095 C  CB  . ILE A 1 255 ? -10.344 -4.801  32.476  1.00  9.87  ? 256 ILE A CB  1 
ATOM   2096 C  CG1 . ILE A 1 255 ? -8.900  -4.755  31.849  1.00  11.63 ? 256 ILE A CG1 1 
ATOM   2097 C  CG2 . ILE A 1 255 ? -11.454 -4.976  31.413  1.00  9.96  ? 256 ILE A CG2 1 
ATOM   2098 C  CD1 . ILE A 1 255 ? -8.672  -6.072  31.111  1.00  11.80 ? 256 ILE A CD1 1 
ATOM   2099 N  N   . LYS A 1 256 ? -12.838 -2.695  33.554  1.00  9.44  ? 257 LYS A N   1 
ATOM   2100 C  CA  . LYS A 1 256 ? -14.215 -2.578  34.097  1.00  10.20 ? 257 LYS A CA  1 
ATOM   2101 C  C   . LYS A 1 256 ? -15.157 -3.214  33.142  1.00  8.54  ? 257 LYS A C   1 
ATOM   2102 O  O   . LYS A 1 256 ? -14.962 -3.168  31.927  1.00  9.81  ? 257 LYS A O   1 
ATOM   2103 C  CB  . LYS A 1 256 ? -14.503 -1.081  34.325  1.00  11.53 ? 257 LYS A CB  1 
ATOM   2104 C  CG  . LYS A 1 256 ? -13.668 -0.509  35.500  1.00  19.71 ? 257 LYS A CG  1 
ATOM   2105 C  CD  . LYS A 1 256 ? -13.703 1.013   35.552  1.00  30.52 ? 257 LYS A CD  1 
ATOM   2106 C  CE  . LYS A 1 256 ? -14.863 1.546   36.392  1.00  34.77 ? 257 LYS A CE  1 
ATOM   2107 N  NZ  . LYS A 1 256 ? -14.458 2.131   37.713  1.00  41.37 ? 257 LYS A NZ  1 
ATOM   2108 N  N   . ALA A 1 257 ? -16.195 -3.857  33.639  1.00  9.68  ? 258 ALA A N   1 
ATOM   2109 C  CA  . ALA A 1 257 ? -17.321 -4.430  32.845  1.00  9.22  ? 258 ALA A CA  1 
ATOM   2110 C  C   . ALA A 1 257 ? -18.599 -3.683  33.017  1.00  10.25 ? 258 ALA A C   1 
ATOM   2111 O  O   . ALA A 1 257 ? -18.951 -3.225  34.163  1.00  11.24 ? 258 ALA A O   1 
ATOM   2112 C  CB  . ALA A 1 257 ? -17.500 -5.920  33.188  1.00  10.34 ? 258 ALA A CB  1 
ATOM   2113 N  N   . SER A 1 258 ? -19.349 -3.564  31.960  1.00  10.27 ? 259 SER A N   1 
ATOM   2114 C  CA  . SER A 1 258 ? -20.661 -2.901  32.034  1.00  10.75 ? 259 SER A CA  1 
ATOM   2115 C  C   . SER A 1 258 ? -21.749 -3.878  32.388  1.00  12.34 ? 259 SER A C   1 
ATOM   2116 O  O   . SER A 1 258 ? -22.906 -3.417  32.514  1.00  16.58 ? 259 SER A O   1 
ATOM   2117 C  CB  . SER A 1 258 ? -21.012 -2.258  30.720  1.00  11.24 ? 259 SER A CB  1 
ATOM   2118 O  OG  . SER A 1 258 ? -21.424 -3.223  29.726  1.00  11.15 ? 259 SER A OG  1 
ATOM   2119 N  N   . PHE A 1 259 ? -21.425 -5.127  32.623  1.00  13.63 ? 260 PHE A N   1 
ATOM   2120 C  CA  . PHE A 1 259 ? -22.433 -6.127  32.845  1.00  15.85 ? 260 PHE A CA  1 
ATOM   2121 C  C   . PHE A 1 259 ? -21.938 -7.095  33.867  1.00  20.22 ? 260 PHE A C   1 
ATOM   2122 O  O   . PHE A 1 259 ? -20.724 -7.157  34.167  1.00  17.41 ? 260 PHE A O   1 
ATOM   2123 C  CB  . PHE A 1 259 ? -22.690 -6.873  31.547  1.00  15.82 ? 260 PHE A CB  1 
ATOM   2124 C  CG  . PHE A 1 259 ? -21.408 -7.563  30.972  1.00  15.41 ? 260 PHE A CG  1 
ATOM   2125 C  CD1 . PHE A 1 259 ? -20.460 -6.808  30.287  1.00  15.91 ? 260 PHE A CD1 1 
ATOM   2126 C  CD2 . PHE A 1 259 ? -21.107 -8.881  31.309  1.00  15.82 ? 260 PHE A CD2 1 
ATOM   2127 C  CE1 . PHE A 1 259 ? -19.281 -7.414  29.825  1.00  16.61 ? 260 PHE A CE1 1 
ATOM   2128 C  CE2 . PHE A 1 259 ? -19.904 -9.470  30.926  1.00  17.38 ? 260 PHE A CE2 1 
ATOM   2129 C  CZ  . PHE A 1 259 ? -18.970 -8.732  30.152  1.00  16.81 ? 260 PHE A CZ  1 
ATOM   2130 N  N   . LYS A 1 260 ? -22.954 -7.829  34.363  1.00  27.25 ? 261 LYS A N   1 
ATOM   2131 C  CA  . LYS A 1 260 ? -22.962 -9.057  35.186  1.00  40.95 ? 261 LYS A CA  1 
ATOM   2132 C  C   . LYS A 1 260 ? -22.320 -9.037  36.566  1.00  49.76 ? 261 LYS A C   1 
ATOM   2133 O  O   . LYS A 1 260 ? -21.225 -9.585  36.761  1.00  63.32 ? 261 LYS A O   1 
ATOM   2134 C  CB  . LYS A 1 260 ? -22.688 -10.346 34.364  1.00  38.71 ? 261 LYS A CB  1 
ATOM   2135 C  CG  . LYS A 1 260 ? -23.794 -10.575 33.326  1.00  44.15 ? 261 LYS A CG  1 
ATOM   2136 C  CD  . LYS A 1 260 ? -24.150 -12.042 33.047  1.00  52.52 ? 261 LYS A CD  1 
ATOM   2137 C  CE  . LYS A 1 260 ? -23.323 -12.679 31.926  1.00  55.65 ? 261 LYS A CE  1 
ATOM   2138 N  NZ  . LYS A 1 260 ? -21.873 -12.790 32.278  1.00  52.35 ? 261 LYS A NZ  1 
ATOM   2139 O  OXT . LYS A 1 260 ? -22.928 -8.448  37.493  1.00  54.69 ? 261 LYS A OXT 1 
HETATM 2140 ZN ZN  . ZN  B 2 .   ? -6.562  -1.731  15.253  1.00  5.18  ? 301 ZN  A ZN  1 
HETATM 2141 CL CL  A EWW C 3 .   ? -6.577  3.867   17.209  0.60  7.51  ? 302 EWW A CL  1 
HETATM 2142 CL CL  B EWW C 3 .   ? -3.871  0.227   14.210  0.40  24.19 ? 302 EWW A CL  1 
HETATM 2143 C  C3  A EWW C 3 .   ? -5.567  3.430   15.863  0.60  8.94  ? 302 EWW A C3  1 
HETATM 2144 C  C3  B EWW C 3 .   ? -4.197  1.877   14.717  0.40  22.78 ? 302 EWW A C3  1 
HETATM 2145 C  C4  A EWW C 3 .   ? -5.203  2.069   15.677  0.60  8.41  ? 302 EWW A C4  1 
HETATM 2146 C  C4  B EWW C 3 .   ? -5.054  2.160   15.797  0.40  20.60 ? 302 EWW A C4  1 
HETATM 2147 S  S6  A EWW C 3 .   ? -5.828  0.767   16.758  0.60  8.73  ? 302 EWW A S6  1 
HETATM 2148 S  S6  B EWW C 3 .   ? -5.871  0.834   16.725  0.40  20.77 ? 302 EWW A S6  1 
HETATM 2149 O  O8  A EWW C 3 .   ? -7.340  0.833   16.586  0.60  6.67  ? 302 EWW A O8  1 
HETATM 2150 O  O8  B EWW C 3 .   ? -7.336  0.554   16.259  0.40  17.56 ? 302 EWW A O8  1 
HETATM 2151 N  N11 A EWW C 3 .   ? -5.276  -0.659  16.092  0.60  6.61  ? 302 EWW A N11 1 
HETATM 2152 N  N11 B EWW C 3 .   ? -5.358  -0.809  16.192  0.40  15.90 ? 302 EWW A N11 1 
HETATM 2153 O  O7  A EWW C 3 .   ? -5.272  0.982   18.154  0.60  6.77  ? 302 EWW A O7  1 
HETATM 2154 O  O7  B EWW C 3 .   ? -5.693  1.089   18.423  0.40  17.36 ? 302 EWW A O7  1 
HETATM 2155 C  C5  A EWW C 3 .   ? -4.327  1.698   14.635  0.60  11.24 ? 302 EWW A C5  1 
HETATM 2156 C  C5  B EWW C 3 .   ? -5.284  3.491   16.165  0.40  22.56 ? 302 EWW A C5  1 
HETATM 2157 C  C2  A EWW C 3 .   ? -5.112  4.446   15.075  0.60  11.07 ? 302 EWW A C2  1 
HETATM 2158 C  C2  B EWW C 3 .   ? -3.584  2.925   14.025  0.40  22.71 ? 302 EWW A C2  1 
HETATM 2159 C  C22 A EWW C 3 .   ? -4.228  4.096   14.025  0.60  14.19 ? 302 EWW A C22 1 
HETATM 2160 C  C22 B EWW C 3 .   ? -3.814  4.258   14.393  0.40  21.74 ? 302 EWW A C22 1 
HETATM 2161 C  C1  A EWW C 3 .   ? -3.861  2.737   13.804  0.60  13.36 ? 302 EWW A C1  1 
HETATM 2162 C  C1  B EWW C 3 .   ? -4.669  4.533   15.470  0.40  21.99 ? 302 EWW A C1  1 
HETATM 2163 C  C9  A EWW C 3 .   ? -3.724  5.188   13.178  0.60  17.97 ? 302 EWW A C9  1 
HETATM 2164 C  C9  B EWW C 3 .   ? -3.154  5.356   13.646  0.40  22.54 ? 302 EWW A C9  1 
HETATM 2165 O  O12 A EWW C 3 .   ? -4.383  6.172   12.940  0.60  18.31 ? 302 EWW A O12 1 
HETATM 2166 O  O12 B EWW C 3 .   ? -3.200  6.497   14.078  0.40  22.71 ? 302 EWW A O12 1 
HETATM 2167 C  C10 A EWW C 3 .   ? -2.332  5.074   12.670  0.60  19.58 ? 302 EWW A C10 1 
HETATM 2168 C  C10 B EWW C 3 .   ? -2.424  5.106   12.361  0.40  24.40 ? 302 EWW A C10 1 
HETATM 2169 S  S13 A EWW C 3 .   ? -2.034  6.393   11.457  0.60  24.59 ? 302 EWW A S13 1 
HETATM 2170 S  S13 B EWW C 3 .   ? -2.194  6.666   11.453  0.40  26.56 ? 302 EWW A S13 1 
HETATM 2171 C  C14 A EWW C 3 .   ? -1.684  7.785   12.532  0.60  24.00 ? 302 EWW A C14 1 
HETATM 2172 C  C14 B EWW C 3 .   ? -3.949  6.996   11.379  0.40  25.19 ? 302 EWW A C14 1 
HETATM 2173 N  N17 A EWW C 3 .   ? -1.574  9.028   11.965  0.60  24.56 ? 302 EWW A N17 1 
HETATM 2174 N  N17 B EWW C 3 .   ? -4.415  8.019   10.614  0.40  24.63 ? 302 EWW A N17 1 
HETATM 2175 C  C18 A EWW C 3 .   ? -1.314  10.126  12.773  0.60  27.21 ? 302 EWW A C18 1 
HETATM 2176 C  C18 B EWW C 3 .   ? -5.757  8.284   10.547  0.40  23.43 ? 302 EWW A C18 1 
HETATM 2177 O  O21 A EWW C 3 .   ? -1.203  11.252  12.301  0.60  28.88 ? 302 EWW A O21 1 
HETATM 2178 O  O21 B EWW C 3 .   ? -6.163  9.203   9.858   0.40  25.34 ? 302 EWW A O21 1 
HETATM 2179 C  C19 A EWW C 3 .   ? -1.155  9.953   14.139  0.60  25.05 ? 302 EWW A C19 1 
HETATM 2180 C  C19 B EWW C 3 .   ? -6.656  7.502   11.267  0.40  21.64 ? 302 EWW A C19 1 
HETATM 2181 C  C16 A EWW C 3 .   ? -1.280  8.667   14.667  0.60  22.70 ? 302 EWW A C16 1 
HETATM 2182 C  C16 B EWW C 3 .   ? -6.153  6.459   12.045  0.40  22.94 ? 302 EWW A C16 1 
HETATM 2183 N  N15 A EWW C 3 .   ? -1.556  7.594   13.881  0.60  23.72 ? 302 EWW A N15 1 
HETATM 2184 N  N15 B EWW C 3 .   ? -4.816  6.225   12.087  0.40  26.07 ? 302 EWW A N15 1 
HETATM 2185 C  C20 A EWW C 3 .   ? -1.134  8.474   16.102  0.60  23.38 ? 302 EWW A C20 1 
HETATM 2186 C  C20 B EWW C 3 .   ? -7.084  5.604   12.827  0.40  22.05 ? 302 EWW A C20 1 
HETATM 2187 O  O1  . MES D 4 .   ? -7.414  -9.223  -2.555  1.00  28.30 ? 303 MES A O1  1 
HETATM 2188 C  C2  . MES D 4 .   ? -7.234  -9.993  -3.822  1.00  25.87 ? 303 MES A C2  1 
HETATM 2189 C  C3  . MES D 4 .   ? -8.463  -10.730 -4.311  1.00  27.25 ? 303 MES A C3  1 
HETATM 2190 N  N4  . MES D 4 .   ? -9.344  -11.225 -3.225  1.00  29.20 ? 303 MES A N4  1 
HETATM 2191 C  C5  . MES D 4 .   ? -9.756  -10.135 -2.291  1.00  28.11 ? 303 MES A C5  1 
HETATM 2192 C  C6  . MES D 4 .   ? -8.496  -9.584  -1.621  1.00  24.64 ? 303 MES A C6  1 
HETATM 2193 C  C7  . MES D 4 .   ? -10.498 -11.977 -3.765  1.00  31.29 ? 303 MES A C7  1 
HETATM 2194 C  C8  . MES D 4 .   ? -11.728 -11.381 -3.110  1.00  25.04 ? 303 MES A C8  1 
HETATM 2195 S  S   . DMS E 5 .   ? 1.446   -11.740 14.922  1.00  22.10 ? 304 DMS A S   1 
HETATM 2196 O  O   . DMS E 5 .   ? 2.059   -13.061 14.444  1.00  24.44 ? 304 DMS A O   1 
HETATM 2197 C  C1  . DMS E 5 .   ? 1.808   -11.636 16.580  1.00  18.13 ? 304 DMS A C1  1 
HETATM 2198 C  C2  . DMS E 5 .   ? 2.486   -10.433 14.461  1.00  19.16 ? 304 DMS A C2  1 
HETATM 2199 C  C1  . PEG F 6 .   ? 2.750   -9.734  30.418  1.00  35.04 ? 305 PEG A C1  1 
HETATM 2200 O  O1  . PEG F 6 .   ? 1.606   -9.925  31.212  1.00  38.16 ? 305 PEG A O1  1 
HETATM 2201 C  C2  . PEG F 6 .   ? 2.474   -9.649  28.928  1.00  35.01 ? 305 PEG A C2  1 
HETATM 2202 O  O2  . PEG F 6 .   ? 1.071   -9.853  28.706  1.00  33.41 ? 305 PEG A O2  1 
HETATM 2203 C  C3  . PEG F 6 .   ? 1.062   -11.127 28.100  1.00  33.27 ? 305 PEG A C3  1 
HETATM 2204 C  C4  . PEG F 6 .   ? 0.169   -11.978 28.951  1.00  32.38 ? 305 PEG A C4  1 
HETATM 2205 O  O4  . PEG F 6 .   ? -1.007  -11.207 28.935  1.00  20.06 ? 305 PEG A O4  1 
HETATM 2206 O  O   . HOH G 7 .   ? -4.445  -13.540 17.990  1.00  6.92  ? 401 HOH A O   1 
HETATM 2207 O  O   . HOH G 7 .   ? -16.950 -8.397  20.416  1.00  6.83  ? 402 HOH A O   1 
HETATM 2208 O  O   . HOH G 7 .   ? -1.152  -4.072  15.676  1.00  6.54  ? 403 HOH A O   1 
HETATM 2209 O  O   . HOH G 7 .   ? -21.525 -7.093  23.504  1.00  9.95  ? 404 HOH A O   1 
HETATM 2210 O  O   . HOH G 7 .   ? -2.344  -8.796  29.082  1.00  11.24 ? 405 HOH A O   1 
HETATM 2211 O  O   . HOH G 7 .   ? -10.560 8.690   25.557  1.00  8.67  ? 406 HOH A O   1 
HETATM 2212 O  O   . HOH G 7 .   ? -7.883  -15.450 11.309  1.00  8.99  ? 407 HOH A O   1 
HETATM 2213 O  O   . HOH G 7 .   ? -3.449  -11.156 20.869  1.00  9.07  ? 408 HOH A O   1 
HETATM 2214 O  O   . HOH G 7 .   ? -3.352  -13.297 25.159  1.00  10.17 ? 409 HOH A O   1 
HETATM 2215 O  O   . HOH G 7 .   ? 4.933   -4.935  20.921  1.00  11.47 ? 410 HOH A O   1 
HETATM 2216 O  O   . HOH G 7 .   ? -17.913 -20.518 7.993   1.00  10.59 ? 411 HOH A O   1 
HETATM 2217 O  O   . HOH G 7 .   ? 8.651   -3.815  21.080  1.00  12.43 ? 412 HOH A O   1 
HETATM 2218 O  O   . HOH G 7 .   ? -21.674 5.645   4.716   1.00  15.35 ? 413 HOH A O   1 
HETATM 2219 O  O   . HOH G 7 .   ? -3.690  -15.911 24.311  1.00  10.96 ? 414 HOH A O   1 
HETATM 2220 O  O   . HOH G 7 .   ? 1.299   -1.656  29.410  1.00  12.23 ? 415 HOH A O   1 
HETATM 2221 O  O   . HOH G 7 .   ? -8.599  -3.871  7.846   1.00  8.98  ? 416 HOH A O   1 
HETATM 2222 O  O   . HOH G 7 .   ? -1.974  -12.353 22.857  1.00  9.20  ? 417 HOH A O   1 
HETATM 2223 O  O   . HOH G 7 .   ? -21.152 7.810   1.869   1.00  15.09 ? 418 HOH A O   1 
HETATM 2224 O  O   . HOH G 7 .   ? 3.851   5.124   29.590  1.00  17.43 ? 419 HOH A O   1 
HETATM 2225 O  O   . HOH G 7 .   ? -16.240 -9.945  32.827  1.00  14.90 ? 420 HOH A O   1 
HETATM 2226 O  O   . HOH G 7 .   ? -24.924 -7.775  9.074   1.00  15.07 ? 421 HOH A O   1 
HETATM 2227 O  O   . HOH G 7 .   ? -12.741 -17.261 16.766  1.00  15.32 ? 422 HOH A O   1 
HETATM 2228 O  O   . HOH G 7 .   ? -10.292 -18.275 16.997  1.00  12.46 ? 423 HOH A O   1 
HETATM 2229 O  O   . HOH G 7 .   ? 7.692   6.122   21.659  1.00  15.09 ? 424 HOH A O   1 
HETATM 2230 O  O   . HOH G 7 .   ? -17.819 -21.988 6.019   1.00  11.02 ? 425 HOH A O   1 
HETATM 2231 O  O   . HOH G 7 .   ? -22.959 -11.690 14.006  1.00  16.78 ? 426 HOH A O   1 
HETATM 2232 O  O   . HOH G 7 .   ? -23.984 -0.775  26.452  1.00  16.26 ? 427 HOH A O   1 
HETATM 2233 O  O   . HOH G 7 .   ? -19.321 10.015  8.910   1.00  13.30 ? 428 HOH A O   1 
HETATM 2234 O  O   . HOH G 7 .   ? -9.966  14.668  12.114  1.00  16.98 ? 429 HOH A O   1 
HETATM 2235 O  O   . HOH G 7 .   ? 5.527   7.176   20.116  1.00  16.52 ? 430 HOH A O   1 
HETATM 2236 O  O   . HOH G 7 .   ? -16.048 -12.331 24.329  1.00  14.63 ? 431 HOH A O   1 
HETATM 2237 O  O   . HOH G 7 .   ? -26.732 -2.539  14.342  1.00  15.28 ? 432 HOH A O   1 
HETATM 2238 O  O   . HOH G 7 .   ? -14.017 10.474  27.745  1.00  18.39 ? 433 HOH A O   1 
HETATM 2239 O  O   . HOH G 7 .   ? -23.163 -3.023  6.587   1.00  17.18 ? 434 HOH A O   1 
HETATM 2240 O  O   . HOH G 7 .   ? -20.353 10.835  26.560  1.00  15.46 ? 435 HOH A O   1 
HETATM 2241 O  O   . HOH G 7 .   ? -5.276  1.288   10.522  1.00  23.00 ? 436 HOH A O   1 
HETATM 2242 O  O   . HOH G 7 .   ? -24.041 8.586   20.115  1.00  23.13 ? 437 HOH A O   1 
HETATM 2243 O  O   . HOH G 7 .   ? -8.040  -19.389 21.647  1.00  16.29 ? 438 HOH A O   1 
HETATM 2244 O  O   . HOH G 7 .   ? 1.321   8.883   24.325  1.00  15.41 ? 439 HOH A O   1 
HETATM 2245 O  O   . HOH G 7 .   ? -23.844 -0.854  3.932   1.00  19.52 ? 440 HOH A O   1 
HETATM 2246 O  O   . HOH G 7 .   ? -22.719 -5.884  2.780   1.00  20.34 ? 441 HOH A O   1 
HETATM 2247 O  O   . HOH G 7 .   ? -14.480 -18.525 18.784  1.00  18.89 ? 442 HOH A O   1 
HETATM 2248 O  O   . HOH G 7 .   ? -28.687 0.217   24.386  1.00  18.21 ? 443 HOH A O   1 
HETATM 2249 O  O   . HOH G 7 .   ? -17.798 10.457  11.291  1.00  15.88 ? 444 HOH A O   1 
HETATM 2250 O  O   . HOH G 7 .   ? -14.232 -16.489 28.977  1.00  23.84 ? 445 HOH A O   1 
HETATM 2251 O  O   . HOH G 7 .   ? 4.521   -3.508  26.396  1.00  17.94 ? 446 HOH A O   1 
HETATM 2252 O  O   . HOH G 7 .   ? -11.971 2.957   30.748  1.00  22.05 ? 447 HOH A O   1 
HETATM 2253 O  O   . HOH G 7 .   ? -9.505  -8.074  33.976  1.00  19.37 ? 448 HOH A O   1 
HETATM 2254 O  O   . HOH G 7 .   ? -13.410 -18.706 14.676  1.00  20.26 ? 449 HOH A O   1 
HETATM 2255 O  O   . HOH G 7 .   ? -8.875  -5.952  35.809  1.00  15.19 ? 450 HOH A O   1 
HETATM 2256 O  O   . HOH G 7 .   ? -0.417  10.903  23.433  1.00  14.74 ? 451 HOH A O   1 
HETATM 2257 O  O   . HOH G 7 .   ? 1.452   -11.796 25.066  1.00  18.84 ? 452 HOH A O   1 
HETATM 2258 O  O   . HOH G 7 .   ? -25.889 6.154   26.927  1.00  22.76 ? 453 HOH A O   1 
HETATM 2259 O  O   . HOH G 7 .   ? -28.996 -5.862  24.553  1.00  22.82 ? 454 HOH A O   1 
HETATM 2260 O  O   . HOH G 7 .   ? 2.694   -11.320 9.544   1.00  20.88 ? 455 HOH A O   1 
HETATM 2261 O  O   . HOH G 7 .   ? -22.208 3.671   -3.003  1.00  23.43 ? 456 HOH A O   1 
HETATM 2262 O  O   . HOH G 7 .   ? -17.709 -19.380 34.999  1.00  19.91 ? 457 HOH A O   1 
HETATM 2263 O  O   . HOH G 7 .   ? -26.819 -3.955  25.088  1.00  19.03 ? 458 HOH A O   1 
HETATM 2264 O  O   . HOH G 7 .   ? -7.969  14.590  10.491  1.00  20.73 ? 459 HOH A O   1 
HETATM 2265 O  O   . HOH G 7 .   ? -6.808  -14.914 31.589  1.00  18.29 ? 460 HOH A O   1 
HETATM 2266 O  O   . HOH G 7 .   ? -1.371  11.454  25.929  1.00  22.66 ? 461 HOH A O   1 
HETATM 2267 O  O   . HOH G 7 .   ? 0.110   -0.972  -4.755  1.00  19.76 ? 462 HOH A O   1 
HETATM 2268 O  O   . HOH G 7 .   ? -7.268  -8.785  32.572  1.00  18.39 ? 463 HOH A O   1 
HETATM 2269 O  O   . HOH G 7 .   ? -6.147  -19.798 23.863  1.00  21.34 ? 464 HOH A O   1 
HETATM 2270 O  O   . HOH G 7 .   ? -4.548  -11.912 32.003  1.00  18.42 ? 465 HOH A O   1 
HETATM 2271 O  O   . HOH G 7 .   ? -16.077 15.882  23.596  1.00  17.80 ? 466 HOH A O   1 
HETATM 2272 O  O   . HOH G 7 .   ? -22.122 -18.393 13.581  1.00  21.48 ? 467 HOH A O   1 
HETATM 2273 O  O   . HOH G 7 .   ? 4.363   -2.438  28.770  1.00  23.12 ? 468 HOH A O   1 
HETATM 2274 O  O   . HOH G 7 .   ? -12.977 -16.869 26.562  1.00  17.64 ? 469 HOH A O   1 
HETATM 2275 O  O   . HOH G 7 .   ? -7.171  6.044   6.624   1.00  25.52 ? 470 HOH A O   1 
HETATM 2276 O  O   . HOH G 7 .   ? -6.612  -20.214 19.456  1.00  14.63 ? 471 HOH A O   1 
HETATM 2277 O  O   . HOH G 7 .   ? -11.134 -19.285 7.010   1.00  25.38 ? 472 HOH A O   1 
HETATM 2278 O  O   . HOH G 7 .   ? -19.489 -23.703 6.087   1.00  21.36 ? 473 HOH A O   1 
HETATM 2279 O  O   . HOH G 7 .   ? -10.982 -15.282 34.011  1.00  23.76 ? 474 HOH A O   1 
HETATM 2280 O  O   . HOH G 7 .   ? -27.470 2.627   23.542  1.00  27.11 ? 475 HOH A O   1 
HETATM 2281 O  O   . HOH G 7 .   ? -1.939  -17.434 25.435  1.00  27.16 ? 476 HOH A O   1 
HETATM 2282 O  O   . HOH G 7 .   ? -29.051 -3.782  13.498  1.00  20.57 ? 477 HOH A O   1 
HETATM 2283 O  O   . HOH G 7 .   ? 2.797   -4.297  7.822   1.00  18.93 ? 478 HOH A O   1 
HETATM 2284 O  O   . HOH G 7 .   ? -13.729 -21.128 15.007  1.00  22.87 ? 479 HOH A O   1 
HETATM 2285 O  O   . HOH G 7 .   ? -17.749 -21.225 17.606  1.00  26.97 ? 480 HOH A O   1 
HETATM 2286 O  O   . HOH G 7 .   ? -26.028 -6.544  12.991  1.00  28.88 ? 481 HOH A O   1 
HETATM 2287 O  O   . HOH G 7 .   ? -8.255  -15.173 36.786  1.00  24.43 ? 482 HOH A O   1 
HETATM 2288 O  O   . HOH G 7 .   ? -14.867 -21.082 17.505  1.00  23.50 ? 483 HOH A O   1 
HETATM 2289 O  O   . HOH G 7 .   ? -5.947  -4.471  -6.394  1.00  22.22 ? 484 HOH A O   1 
HETATM 2290 O  O   . HOH G 7 .   ? -23.441 -13.305 11.354  1.00  22.78 ? 485 HOH A O   1 
HETATM 2291 O  O   . HOH G 7 .   ? -17.393 -23.145 4.150   1.00  27.20 ? 486 HOH A O   1 
HETATM 2292 O  O   . HOH G 7 .   ? -1.595  -13.266 27.389  1.00  23.74 ? 487 HOH A O   1 
HETATM 2293 O  O   . HOH G 7 .   ? -27.938 4.964   25.313  1.00  26.84 ? 488 HOH A O   1 
HETATM 2294 O  O   . HOH G 7 .   ? -7.099  -16.850 1.485   1.00  20.80 ? 489 HOH A O   1 
HETATM 2295 O  O   . HOH G 7 .   ? -23.849 -16.721 3.729   1.00  29.73 ? 490 HOH A O   1 
HETATM 2296 O  O   . HOH G 7 .   ? -4.627  -15.917 0.750   1.00  22.08 ? 491 HOH A O   1 
HETATM 2297 O  O   . HOH G 7 .   ? -25.559 -15.322 7.833   1.00  24.35 ? 492 HOH A O   1 
HETATM 2298 O  O   . HOH G 7 .   ? -1.116  -17.731 18.037  1.00  26.95 ? 493 HOH A O   1 
HETATM 2299 O  O   . HOH G 7 .   ? 3.867   9.895   23.669  1.00  23.48 ? 494 HOH A O   1 
HETATM 2300 O  O   . HOH G 7 .   ? 2.060   -15.690 9.306   1.00  22.14 ? 495 HOH A O   1 
HETATM 2301 O  O   . HOH G 7 .   ? 6.431   5.364   28.618  1.00  26.08 ? 496 HOH A O   1 
HETATM 2302 O  O   . HOH G 7 .   ? -4.143  -8.676  31.095  1.00  20.16 ? 497 HOH A O   1 
HETATM 2303 O  O   . HOH G 7 .   ? -1.835  -12.107 31.342  1.00  29.95 ? 498 HOH A O   1 
HETATM 2304 O  O   . HOH G 7 .   ? -3.610  -12.929 -2.896  1.00  26.37 ? 499 HOH A O   1 
HETATM 2305 O  O   . HOH G 7 .   ? -0.080  -14.303 22.189  1.00  21.40 ? 500 HOH A O   1 
HETATM 2306 O  O   . HOH G 7 .   ? 2.708   -13.192 5.246   1.00  24.01 ? 501 HOH A O   1 
HETATM 2307 O  O   . HOH G 7 .   ? -5.401  3.759   -5.732  1.00  28.99 ? 502 HOH A O   1 
HETATM 2308 O  O   . HOH G 7 .   ? -12.464 12.666  29.174  1.00  25.05 ? 503 HOH A O   1 
HETATM 2309 O  O   . HOH G 7 .   ? -23.925 -2.449  29.020  1.00  26.84 ? 504 HOH A O   1 
HETATM 2310 O  O   . HOH G 7 .   ? -17.353 -16.126 21.885  1.00  25.86 ? 505 HOH A O   1 
HETATM 2311 O  O   . HOH G 7 .   ? 1.826   12.421  22.728  1.00  27.93 ? 506 HOH A O   1 
HETATM 2312 O  O   . HOH G 7 .   ? -23.137 -0.731  34.265  1.00  23.21 ? 507 HOH A O   1 
HETATM 2313 O  O   . HOH G 7 .   ? -30.543 -0.440  15.994  1.00  23.86 ? 508 HOH A O   1 
HETATM 2314 O  O   . HOH G 7 .   ? -27.525 -0.013  14.939  1.00  27.75 ? 509 HOH A O   1 
HETATM 2315 O  O   . HOH G 7 .   ? -23.553 8.373   3.417   1.00  23.47 ? 510 HOH A O   1 
HETATM 2316 O  O   . HOH G 7 .   ? -14.164 14.340  26.952  1.00  26.20 ? 511 HOH A O   1 
HETATM 2317 O  O   . HOH G 7 .   ? -7.869  7.186   27.640  1.00  28.05 ? 512 HOH A O   1 
HETATM 2318 O  O   . HOH G 7 .   ? -18.509 -9.056  34.340  1.00  22.82 ? 513 HOH A O   1 
HETATM 2319 O  O   . HOH G 7 .   ? -23.833 -7.150  0.153   1.00  26.99 ? 514 HOH A O   1 
HETATM 2320 O  O   . HOH G 7 .   ? -26.274 3.698   15.270  1.00  27.57 ? 515 HOH A O   1 
HETATM 2321 O  O   . HOH G 7 .   ? -25.612 9.727   13.321  1.00  27.80 ? 516 HOH A O   1 
HETATM 2322 O  O   . HOH G 7 .   ? -13.266 -22.318 11.588  1.00  30.32 ? 517 HOH A O   1 
HETATM 2323 O  O   . HOH G 7 .   ? -16.852 -13.945 26.399  1.00  24.11 ? 518 HOH A O   1 
HETATM 2324 O  O   . HOH G 7 .   ? 3.832   4.885   2.216   1.00  27.56 ? 519 HOH A O   1 
HETATM 2325 O  O   . HOH G 7 .   ? -20.828 -6.801  -2.115  1.00  27.41 ? 520 HOH A O   1 
HETATM 2326 O  O   . HOH G 7 .   ? -25.019 4.601   8.116   1.00  29.31 ? 521 HOH A O   1 
HETATM 2327 O  O   . HOH G 7 .   ? -15.267 -21.704 13.184  1.00  25.72 ? 522 HOH A O   1 
HETATM 2328 O  O   . HOH G 7 .   ? -11.606 10.651  0.912   1.00  30.61 ? 523 HOH A O   1 
HETATM 2329 O  O   . HOH G 7 .   ? -14.583 9.293   31.641  1.00  37.04 ? 524 HOH A O   1 
HETATM 2330 O  O   . HOH G 7 .   ? -4.786  2.129   37.326  1.00  29.72 ? 525 HOH A O   1 
HETATM 2331 O  O   . HOH G 7 .   ? -6.040  17.496  27.314  1.00  31.50 ? 526 HOH A O   1 
HETATM 2332 O  O   . HOH G 7 .   ? -8.424  0.672   -6.532  1.00  23.82 ? 527 HOH A O   1 
HETATM 2333 O  O   . HOH G 7 .   ? -6.420  -5.291  37.347  1.00  26.14 ? 528 HOH A O   1 
HETATM 2334 O  O   . HOH G 7 .   ? -0.421  13.975  16.022  1.00  23.87 ? 529 HOH A O   1 
HETATM 2335 O  O   . HOH G 7 .   ? -15.350 -16.541 25.556  1.00  31.11 ? 530 HOH A O   1 
HETATM 2336 O  O   . HOH G 7 .   ? -21.090 -19.614 6.474   1.00  23.84 ? 531 HOH A O   1 
HETATM 2337 O  O   . HOH G 7 .   ? -10.317 4.848   30.854  1.00  29.85 ? 532 HOH A O   1 
HETATM 2338 O  O   . HOH G 7 .   ? -9.006  3.180   34.734  1.00  24.86 ? 533 HOH A O   1 
HETATM 2339 O  O   . HOH G 7 .   ? -16.324 -12.609 -6.031  1.00  30.89 ? 534 HOH A O   1 
HETATM 2340 O  O   . HOH G 7 .   ? 10.238  -7.015  -8.720  1.00  27.41 ? 535 HOH A O   1 
HETATM 2341 O  O   . HOH G 7 .   ? 5.982   0.985   8.287   1.00  33.04 ? 536 HOH A O   1 
HETATM 2342 O  O   . HOH G 7 .   ? 3.405   1.088   -1.783  1.00  36.80 ? 537 HOH A O   1 
HETATM 2343 O  O   . HOH G 7 .   ? -27.977 -1.434  28.364  1.00  28.09 ? 538 HOH A O   1 
HETATM 2344 O  O   . HOH G 7 .   ? -26.720 -1.342  25.930  1.00  22.42 ? 539 HOH A O   1 
HETATM 2345 O  O   . HOH G 7 .   ? -21.105 -22.160 13.892  1.00  34.44 ? 540 HOH A O   1 
HETATM 2346 O  O   . HOH G 7 .   ? -18.651 -20.850 14.705  1.00  30.76 ? 541 HOH A O   1 
HETATM 2347 O  O   . HOH G 7 .   ? -17.238 0.031   -3.936  1.00  30.78 ? 542 HOH A O   1 
HETATM 2348 O  O   . HOH G 7 .   ? 4.314   -11.483 23.512  1.00  34.36 ? 543 HOH A O   1 
HETATM 2349 O  O   . HOH G 7 .   ? 4.623   -6.580  7.875   1.00  25.44 ? 544 HOH A O   1 
HETATM 2350 O  O   . HOH G 7 .   ? 10.280  -2.485  13.698  1.00  27.72 ? 545 HOH A O   1 
HETATM 2351 O  O   . HOH G 7 .   ? -5.921  -11.503 36.315  1.00  29.94 ? 546 HOH A O   1 
HETATM 2352 O  O   . HOH G 7 .   ? -20.816 8.273   30.012  1.00  28.68 ? 547 HOH A O   1 
HETATM 2353 O  O   . HOH G 7 .   ? -24.699 12.052  6.315   1.00  28.11 ? 548 HOH A O   1 
HETATM 2354 O  O   . HOH G 7 .   ? -12.798 7.980   28.913  1.00  29.25 ? 549 HOH A O   1 
HETATM 2355 O  O   . HOH G 7 .   ? -2.568  -17.685 5.268   1.00  29.81 ? 550 HOH A O   1 
HETATM 2356 O  O   . HOH G 7 .   ? -3.293  18.048  21.436  1.00  25.49 ? 551 HOH A O   1 
HETATM 2357 O  O   . HOH G 7 .   ? -4.730  20.229  21.487  1.00  20.90 ? 552 HOH A O   1 
HETATM 2358 O  O   . HOH G 7 .   ? 5.632   9.034   21.834  1.00  26.42 ? 553 HOH A O   1 
HETATM 2359 O  O   . HOH G 7 .   ? -18.491 -3.860  -2.670  1.00  25.24 ? 554 HOH A O   1 
HETATM 2360 O  O   . HOH G 7 .   ? 0.871   3.088   2.076   1.00  33.26 ? 555 HOH A O   1 
HETATM 2361 O  O   . HOH G 7 .   ? 3.763   4.559   10.707  1.00  36.13 ? 556 HOH A O   1 
HETATM 2362 O  O   . HOH G 7 .   ? -2.428  -3.003  11.415  1.00  16.48 ? 557 HOH A O   1 
HETATM 2363 O  O   . HOH G 7 .   ? -1.394  1.863   11.469  1.00  21.39 ? 558 HOH A O   1 
HETATM 2364 O  O   . HOH G 7 .   ? -4.306  4.107   10.183  1.00  24.72 ? 559 HOH A O   1 
HETATM 2365 O  O   . HOH G 7 .   ? 0.142   3.454   9.979   1.00  33.57 ? 560 HOH A O   1 
HETATM 2366 O  O   . HOH G 7 .   ? -12.082 10.684  5.881   1.00  27.14 ? 561 HOH A O   1 
HETATM 2367 O  O   . HOH G 7 .   ? 6.200   -2.800  6.834   1.00  36.05 ? 562 HOH A O   1 
HETATM 2368 O  O   . HOH G 7 .   ? 12.375  4.361   27.227  1.00  30.69 ? 563 HOH A O   1 
HETATM 2369 O  O   . HOH G 7 .   ? -17.773 -12.201 31.537  1.00  27.98 ? 564 HOH A O   1 
HETATM 2370 O  O   . HOH G 7 .   ? -15.997 16.941  26.456  1.00  38.08 ? 565 HOH A O   1 
HETATM 2371 O  O   . HOH G 7 .   ? 1.630   -17.438 7.047   1.00  30.03 ? 566 HOH A O   1 
HETATM 2372 O  O   . HOH G 7 .   ? -10.460 -19.284 19.913  1.00  25.39 ? 567 HOH A O   1 
HETATM 2373 O  O   . HOH G 7 .   ? -20.994 0.645   0.342   1.00  41.16 ? 568 HOH A O   1 
HETATM 2374 O  O   . HOH G 7 .   ? -26.250 -7.803  30.282  1.00  28.82 ? 569 HOH A O   1 
HETATM 2375 O  O   . HOH G 7 .   ? -6.393  -19.427 5.257   1.00  27.16 ? 570 HOH A O   1 
HETATM 2376 O  O   . HOH G 7 .   ? 0.235   0.778   -6.569  1.00  30.95 ? 571 HOH A O   1 
HETATM 2377 O  O   . HOH G 7 .   ? 2.917   -14.351 0.690   1.00  30.17 ? 572 HOH A O   1 
HETATM 2378 O  O   . HOH G 7 .   ? -19.405 -20.682 4.951   1.00  20.41 ? 573 HOH A O   1 
HETATM 2379 O  O   . HOH G 7 .   ? -7.964  -22.308 10.374  1.00  19.16 ? 574 HOH A O   1 
HETATM 2380 O  O   . HOH G 7 .   ? -12.800 -22.065 8.418   1.00  32.52 ? 575 HOH A O   1 
HETATM 2381 O  O   . HOH G 7 .   ? -15.755 9.054   -2.007  1.00  21.68 ? 576 HOH A O   1 
HETATM 2382 O  O   . HOH G 7 .   ? 1.552   -6.289  34.420  1.00  22.22 ? 577 HOH A O   1 
HETATM 2383 O  O   . HOH G 7 .   ? -0.450  -8.659  32.349  1.00  22.61 ? 578 HOH A O   1 
HETATM 2384 O  O   . HOH G 7 .   ? 3.612   -8.901  25.917  1.00  30.62 ? 579 HOH A O   1 
HETATM 2385 O  O   . HOH G 7 .   ? -24.606 -9.489  1.981   1.00  22.82 ? 580 HOH A O   1 
HETATM 2386 O  O   . HOH G 7 .   ? -1.020  9.340   27.818  1.00  23.21 ? 581 HOH A O   1 
HETATM 2387 O  O   . HOH G 7 .   ? 11.413  1.530   26.040  1.00  20.53 ? 582 HOH A O   1 
HETATM 2388 O  O   . HOH G 7 .   ? 8.375   3.185   27.622  1.00  22.97 ? 583 HOH A O   1 
HETATM 2389 O  O   . HOH G 7 .   ? 11.848  0.753   28.679  1.00  34.45 ? 584 HOH A O   1 
HETATM 2390 O  O   . HOH G 7 .   ? 11.177  -6.885  22.407  1.00  27.16 ? 585 HOH A O   1 
HETATM 2391 O  O   . HOH G 7 .   ? 8.624   -4.879  23.740  1.00  25.06 ? 586 HOH A O   1 
HETATM 2392 O  O   . HOH G 7 .   ? 9.492   1.974   12.060  1.00  30.10 ? 587 HOH A O   1 
HETATM 2393 O  O   . HOH G 7 .   ? 9.759   -4.458  -7.884  1.00  26.58 ? 588 HOH A O   1 
HETATM 2394 O  O   . HOH G 7 .   ? -17.144 -7.453  39.581  1.00  28.69 ? 589 HOH A O   1 
HETATM 2395 O  O   . HOH G 7 .   ? -19.398 -4.234  41.329  1.00  31.64 ? 590 HOH A O   1 
HETATM 2396 O  O   . HOH G 7 .   ? -7.832  -19.078 30.548  1.00  27.24 ? 591 HOH A O   1 
HETATM 2397 O  O   . HOH G 7 .   ? -8.426  -19.882 26.611  1.00  22.44 ? 592 HOH A O   1 
HETATM 2398 O  O   . HOH G 7 .   ? -12.734 -19.442 26.361  1.00  26.50 ? 593 HOH A O   1 
HETATM 2399 O  O   . HOH G 7 .   ? -9.007  19.151  28.461  1.00  28.47 ? 594 HOH A O   1 
HETATM 2400 O  O   . HOH G 7 .   ? -5.661  15.496  11.943  1.00  24.17 ? 595 HOH A O   1 
HETATM 2401 O  O   . HOH G 7 .   ? -16.452 -15.243 32.771  1.00  30.43 ? 596 HOH A O   1 
HETATM 2402 O  O   . HOH G 7 .   ? -17.020 -14.043 37.268  1.00  27.82 ? 597 HOH A O   1 
HETATM 2403 O  O   . HOH G 7 .   ? -12.931 3.501   -6.813  1.00  30.89 ? 598 HOH A O   1 
HETATM 2404 O  O   . HOH G 7 .   ? -11.597 0.946   -7.569  1.00  32.44 ? 599 HOH A O   1 
HETATM 2405 O  O   . HOH G 7 .   ? -13.976 -4.933  -6.437  1.00  32.30 ? 600 HOH A O   1 
HETATM 2406 O  O   . HOH G 7 .   ? -25.574 -10.552 17.751  1.00  20.98 ? 601 HOH A O   1 
HETATM 2407 O  O   . HOH G 7 .   ? -24.243 -17.699 6.568   1.00  33.36 ? 602 HOH A O   1 
HETATM 2408 O  O   . HOH G 7 .   ? -24.278 -0.275  1.197   1.00  34.86 ? 603 HOH A O   1 
HETATM 2409 O  O   . HOH G 7 .   ? 1.176   14.833  24.270  1.00  26.81 ? 604 HOH A O   1 
HETATM 2410 O  O   . HOH G 7 .   ? -16.809 -18.002 20.087  1.00  27.01 ? 605 HOH A O   1 
HETATM 2411 O  O   . HOH G 7 .   ? 10.800  -9.000  9.189   1.00  33.44 ? 606 HOH A O   1 
HETATM 2412 O  O   . HOH G 7 .   ? 14.936  -6.664  7.874   1.00  38.40 ? 607 HOH A O   1 
HETATM 2413 O  O   . HOH G 7 .   ? 3.076   -13.407 8.329   1.00  33.34 ? 608 HOH A O   1 
HETATM 2414 O  O   . HOH G 7 .   ? 3.506   -13.691 11.983  1.00  31.32 ? 609 HOH A O   1 
HETATM 2415 O  O   . HOH G 7 .   ? 5.647   -12.459 11.656  1.00  36.59 ? 610 HOH A O   1 
HETATM 2416 O  O   . HOH G 7 .   ? 6.465   -10.906 15.160  1.00  31.70 ? 611 HOH A O   1 
HETATM 2417 O  O   . HOH G 7 .   ? 14.997  3.653   20.903  1.00  29.62 ? 612 HOH A O   1 
HETATM 2418 O  O   . HOH G 7 .   ? 14.135  5.684   19.147  1.00  33.17 ? 613 HOH A O   1 
HETATM 2419 O  O   . HOH G 7 .   ? 2.240   8.063   27.765  1.00  29.08 ? 614 HOH A O   1 
HETATM 2420 O  O   . HOH G 7 .   ? -15.352 -10.279 37.117  1.00  31.04 ? 615 HOH A O   1 
HETATM 2421 O  O   . HOH G 7 .   ? -8.370  7.713   8.479   1.00  32.79 ? 616 HOH A O   1 
HETATM 2422 O  O   . HOH G 7 .   ? -2.486  4.437   8.173   1.00  29.38 ? 617 HOH A O   1 
HETATM 2423 O  O   . HOH G 7 .   ? -2.678  6.120   5.866   1.00  33.78 ? 618 HOH A O   1 
HETATM 2424 O  O   . HOH G 7 .   ? -4.855  7.428   5.835   1.00  27.96 ? 619 HOH A O   1 
HETATM 2425 O  O   . HOH G 7 .   ? -3.099  -0.182  10.548  1.00  23.26 ? 620 HOH A O   1 
HETATM 2426 O  O   . HOH G 7 .   ? -18.744 12.097  13.017  1.00  24.54 ? 621 HOH A O   1 
HETATM 2427 O  O   . HOH G 7 .   ? -0.271  -17.052 29.238  1.00  37.02 ? 622 HOH A O   1 
HETATM 2428 O  O   . HOH G 7 .   ? -10.946 17.367  12.061  1.00  31.90 ? 623 HOH A O   1 
HETATM 2429 O  O   . HOH G 7 .   ? 0.427   17.494  24.474  1.00  34.05 ? 624 HOH A O   1 
HETATM 2430 O  O   . HOH G 7 .   ? -13.767 -8.815  -5.273  1.00  23.20 ? 625 HOH A O   1 
HETATM 2431 O  O   . HOH G 7 .   ? -12.746 -8.922  -3.178  1.00  22.36 ? 626 HOH A O   1 
HETATM 2432 O  O   . HOH G 7 .   ? -19.972 -15.505 22.586  1.00  28.90 ? 627 HOH A O   1 
HETATM 2433 O  O   . HOH G 7 .   ? -21.285 -19.974 15.118  1.00  41.86 ? 628 HOH A O   1 
HETATM 2434 O  O   . HOH G 7 .   ? 6.355   -5.397  3.561   1.00  34.27 ? 629 HOH A O   1 
HETATM 2435 O  O   . HOH G 7 .   ? 6.578   -0.739  -1.160  1.00  36.61 ? 630 HOH A O   1 
HETATM 2436 O  O   . HOH G 7 .   ? 5.149   -7.225  22.256  1.00  26.79 ? 631 HOH A O   1 
HETATM 2437 O  O   . HOH G 7 .   ? -4.638  9.500   7.005   1.00  37.21 ? 632 HOH A O   1 
HETATM 2438 O  O   . HOH G 7 .   ? -10.878 9.089   7.536   1.00  26.78 ? 633 HOH A O   1 
HETATM 2439 O  O   . HOH G 7 .   ? 10.367  5.758   13.098  1.00  33.66 ? 634 HOH A O   1 
HETATM 2440 O  O   . HOH G 7 .   ? 15.394  -10.375 14.531  1.00  32.85 ? 635 HOH A O   1 
HETATM 2441 O  O   . HOH G 7 .   ? -17.135 -6.481  42.338  1.00  30.44 ? 636 HOH A O   1 
HETATM 2442 O  O   . HOH G 7 .   ? -25.305 -3.159  31.654  1.00  29.11 ? 637 HOH A O   1 
HETATM 2443 O  O   . HOH G 7 .   ? -27.818 6.294   21.570  1.00  28.14 ? 638 HOH A O   1 
HETATM 2444 O  O   . HOH G 7 .   ? -4.230  -4.838  11.098  1.00  27.21 ? 639 HOH A O   1 
HETATM 2445 O  O   . HOH G 7 .   ? 0.338   -19.345 10.839  1.00  28.18 ? 640 HOH A O   1 
HETATM 2446 O  O   . HOH G 7 .   ? -10.498 20.544  24.956  1.00  27.93 ? 641 HOH A O   1 
HETATM 2447 O  O   . HOH G 7 .   ? -1.803  -4.820  -6.821  1.00  31.69 ? 642 HOH A O   1 
HETATM 2448 O  O   . HOH G 7 .   ? -9.489  6.553   -3.857  1.00  36.64 ? 643 HOH A O   1 
HETATM 2449 O  O   . HOH G 7 .   ? -7.155  1.474   35.111  1.00  30.07 ? 644 HOH A O   1 
HETATM 2450 O  O   . HOH G 7 .   ? -22.292 -12.469 24.735  1.00  30.60 ? 645 HOH A O   1 
HETATM 2451 O  O   . HOH G 7 .   ? -21.756 -13.858 23.003  1.00  28.46 ? 646 HOH A O   1 
HETATM 2452 O  O   . HOH G 7 .   ? -8.715  -17.957 -0.863  1.00  38.37 ? 647 HOH A O   1 
HETATM 2453 O  O   . HOH G 7 .   ? -5.721  -12.768 -5.321  1.00  37.74 ? 648 HOH A O   1 
HETATM 2454 O  O   . HOH G 7 .   ? 7.641   -7.439  -0.880  1.00  34.39 ? 649 HOH A O   1 
HETATM 2455 O  O   . HOH G 7 .   ? 1.457   -15.843 -1.863  1.00  39.26 ? 650 HOH A O   1 
HETATM 2456 O  O   . HOH G 7 .   ? -14.500 0.644   39.530  1.00  31.09 ? 651 HOH A O   1 
HETATM 2457 O  O   . HOH G 7 .   ? -6.280  12.139  10.058  1.00  37.12 ? 652 HOH A O   1 
HETATM 2458 O  O   . HOH G 7 .   ? 6.478   -5.927  6.552   1.00  37.91 ? 653 HOH A O   1 
HETATM 2459 O  O   . HOH G 7 .   ? 12.088  -6.602  7.965   1.00  34.32 ? 654 HOH A O   1 
HETATM 2460 O  O   . HOH G 7 .   ? 13.174  6.377   15.877  1.00  45.18 ? 655 HOH A O   1 
HETATM 2461 O  O   . HOH G 7 .   ? 1.558   9.850   26.626  1.00  27.10 ? 656 HOH A O   1 
HETATM 2462 O  O   . HOH G 7 .   ? 0.752   7.161   29.770  1.00  30.26 ? 657 HOH A O   1 
HETATM 2463 O  O   . HOH G 7 .   ? 6.947   -3.620  30.067  1.00  31.81 ? 658 HOH A O   1 
HETATM 2464 O  O   . HOH G 7 .   ? 8.880   2.017   30.113  1.00  39.50 ? 659 HOH A O   1 
HETATM 2465 O  O   . HOH G 7 .   ? -10.337 -5.852  38.118  1.00  36.48 ? 660 HOH A O   1 
HETATM 2466 O  O   . HOH G 7 .   ? -25.125 8.788   25.891  1.00  38.11 ? 661 HOH A O   1 
HETATM 2467 O  O   . HOH G 7 .   ? 3.182   2.895   0.436   1.00  32.99 ? 662 HOH A O   1 
HETATM 2468 O  O   . HOH G 7 .   ? -18.748 14.302  2.761   1.00  45.01 ? 663 HOH A O   1 
HETATM 2469 O  O   . HOH G 7 .   ? -26.811 -6.318  4.977   1.00  39.27 ? 664 HOH A O   1 
HETATM 2470 O  O   . HOH G 7 .   ? -27.254 -7.544  26.172  1.00  38.15 ? 665 HOH A O   1 
HETATM 2471 O  O   . HOH G 7 .   ? -10.908 0.971   33.497  1.00  32.60 ? 666 HOH A O   1 
HETATM 2472 O  O   . HOH G 7 .   ? -9.173  5.782   29.068  1.00  29.85 ? 667 HOH A O   1 
HETATM 2473 O  O   . HOH G 7 .   ? -20.119 -23.041 3.765   1.00  41.18 ? 668 HOH A O   1 
HETATM 2474 O  O   . HOH G 7 .   ? 7.588   -4.371  -0.618  1.00  40.27 ? 669 HOH A O   1 
HETATM 2475 O  O   . HOH G 7 .   ? -3.161  -9.607  33.657  1.00  39.75 ? 670 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   3   HIS HIS 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 EWW 1   302 1   EWW EWW A . 
D 4 MES 1   303 2   MES MES A . 
E 5 DMS 1   304 1   DMS DMS A . 
F 6 PEG 1   305 3   PEG PEG A . 
G 7 HOH 1   401 1   HOH HOH A . 
G 7 HOH 2   402 2   HOH HOH A . 
G 7 HOH 3   403 3   HOH HOH A . 
G 7 HOH 4   404 4   HOH HOH A . 
G 7 HOH 5   405 5   HOH HOH A . 
G 7 HOH 6   406 6   HOH HOH A . 
G 7 HOH 7   407 7   HOH HOH A . 
G 7 HOH 8   408 8   HOH HOH A . 
G 7 HOH 9   409 9   HOH HOH A . 
G 7 HOH 10  410 10  HOH HOH A . 
G 7 HOH 11  411 11  HOH HOH A . 
G 7 HOH 12  412 12  HOH HOH A . 
G 7 HOH 13  413 13  HOH HOH A . 
G 7 HOH 14  414 14  HOH HOH A . 
G 7 HOH 15  415 15  HOH HOH A . 
G 7 HOH 16  416 16  HOH HOH A . 
G 7 HOH 17  417 17  HOH HOH A . 
G 7 HOH 18  418 18  HOH HOH A . 
G 7 HOH 19  419 19  HOH HOH A . 
G 7 HOH 20  420 20  HOH HOH A . 
G 7 HOH 21  421 21  HOH HOH A . 
G 7 HOH 22  422 22  HOH HOH A . 
G 7 HOH 23  423 23  HOH HOH A . 
G 7 HOH 24  424 24  HOH HOH A . 
G 7 HOH 25  425 25  HOH HOH A . 
G 7 HOH 26  426 26  HOH HOH A . 
G 7 HOH 27  427 27  HOH HOH A . 
G 7 HOH 28  428 28  HOH HOH A . 
G 7 HOH 29  429 29  HOH HOH A . 
G 7 HOH 30  430 30  HOH HOH A . 
G 7 HOH 31  431 31  HOH HOH A . 
G 7 HOH 32  432 32  HOH HOH A . 
G 7 HOH 33  433 33  HOH HOH A . 
G 7 HOH 34  434 34  HOH HOH A . 
G 7 HOH 35  435 35  HOH HOH A . 
G 7 HOH 36  436 36  HOH HOH A . 
G 7 HOH 37  437 37  HOH HOH A . 
G 7 HOH 38  438 38  HOH HOH A . 
G 7 HOH 39  439 39  HOH HOH A . 
G 7 HOH 40  440 40  HOH HOH A . 
G 7 HOH 41  441 41  HOH HOH A . 
G 7 HOH 42  442 42  HOH HOH A . 
G 7 HOH 43  443 43  HOH HOH A . 
G 7 HOH 44  444 44  HOH HOH A . 
G 7 HOH 45  445 45  HOH HOH A . 
G 7 HOH 46  446 46  HOH HOH A . 
G 7 HOH 47  447 47  HOH HOH A . 
G 7 HOH 48  448 48  HOH HOH A . 
G 7 HOH 49  449 49  HOH HOH A . 
G 7 HOH 50  450 50  HOH HOH A . 
G 7 HOH 51  451 51  HOH HOH A . 
G 7 HOH 52  452 52  HOH HOH A . 
G 7 HOH 53  453 53  HOH HOH A . 
G 7 HOH 54  454 54  HOH HOH A . 
G 7 HOH 55  455 55  HOH HOH A . 
G 7 HOH 56  456 56  HOH HOH A . 
G 7 HOH 57  457 57  HOH HOH A . 
G 7 HOH 58  458 58  HOH HOH A . 
G 7 HOH 59  459 59  HOH HOH A . 
G 7 HOH 60  460 60  HOH HOH A . 
G 7 HOH 61  461 61  HOH HOH A . 
G 7 HOH 62  462 62  HOH HOH A . 
G 7 HOH 63  463 63  HOH HOH A . 
G 7 HOH 64  464 64  HOH HOH A . 
G 7 HOH 65  465 65  HOH HOH A . 
G 7 HOH 66  466 66  HOH HOH A . 
G 7 HOH 67  467 67  HOH HOH A . 
G 7 HOH 68  468 68  HOH HOH A . 
G 7 HOH 69  469 69  HOH HOH A . 
G 7 HOH 70  470 70  HOH HOH A . 
G 7 HOH 71  471 71  HOH HOH A . 
G 7 HOH 72  472 72  HOH HOH A . 
G 7 HOH 73  473 73  HOH HOH A . 
G 7 HOH 74  474 74  HOH HOH A . 
G 7 HOH 75  475 75  HOH HOH A . 
G 7 HOH 76  476 76  HOH HOH A . 
G 7 HOH 77  477 77  HOH HOH A . 
G 7 HOH 78  478 78  HOH HOH A . 
G 7 HOH 79  479 79  HOH HOH A . 
G 7 HOH 80  480 80  HOH HOH A . 
G 7 HOH 81  481 81  HOH HOH A . 
G 7 HOH 82  482 82  HOH HOH A . 
G 7 HOH 83  483 83  HOH HOH A . 
G 7 HOH 84  484 84  HOH HOH A . 
G 7 HOH 85  485 85  HOH HOH A . 
G 7 HOH 86  486 86  HOH HOH A . 
G 7 HOH 87  487 87  HOH HOH A . 
G 7 HOH 88  488 88  HOH HOH A . 
G 7 HOH 89  489 89  HOH HOH A . 
G 7 HOH 90  490 90  HOH HOH A . 
G 7 HOH 91  491 91  HOH HOH A . 
G 7 HOH 92  492 92  HOH HOH A . 
G 7 HOH 93  493 93  HOH HOH A . 
G 7 HOH 94  494 94  HOH HOH A . 
G 7 HOH 95  495 95  HOH HOH A . 
G 7 HOH 96  496 96  HOH HOH A . 
G 7 HOH 97  497 97  HOH HOH A . 
G 7 HOH 98  498 98  HOH HOH A . 
G 7 HOH 99  499 99  HOH HOH A . 
G 7 HOH 100 500 100 HOH HOH A . 
G 7 HOH 101 501 101 HOH HOH A . 
G 7 HOH 102 502 102 HOH HOH A . 
G 7 HOH 103 503 103 HOH HOH A . 
G 7 HOH 104 504 104 HOH HOH A . 
G 7 HOH 105 505 105 HOH HOH A . 
G 7 HOH 106 506 106 HOH HOH A . 
G 7 HOH 107 507 107 HOH HOH A . 
G 7 HOH 108 508 108 HOH HOH A . 
G 7 HOH 109 509 109 HOH HOH A . 
G 7 HOH 110 510 110 HOH HOH A . 
G 7 HOH 111 511 111 HOH HOH A . 
G 7 HOH 112 512 112 HOH HOH A . 
G 7 HOH 113 513 113 HOH HOH A . 
G 7 HOH 114 514 114 HOH HOH A . 
G 7 HOH 115 515 115 HOH HOH A . 
G 7 HOH 116 516 116 HOH HOH A . 
G 7 HOH 117 517 117 HOH HOH A . 
G 7 HOH 118 518 118 HOH HOH A . 
G 7 HOH 119 519 119 HOH HOH A . 
G 7 HOH 120 520 120 HOH HOH A . 
G 7 HOH 121 521 121 HOH HOH A . 
G 7 HOH 122 522 122 HOH HOH A . 
G 7 HOH 123 523 123 HOH HOH A . 
G 7 HOH 124 524 124 HOH HOH A . 
G 7 HOH 125 525 125 HOH HOH A . 
G 7 HOH 126 526 126 HOH HOH A . 
G 7 HOH 127 527 127 HOH HOH A . 
G 7 HOH 128 528 128 HOH HOH A . 
G 7 HOH 129 529 129 HOH HOH A . 
G 7 HOH 130 530 130 HOH HOH A . 
G 7 HOH 131 531 131 HOH HOH A . 
G 7 HOH 132 532 132 HOH HOH A . 
G 7 HOH 133 533 133 HOH HOH A . 
G 7 HOH 134 534 134 HOH HOH A . 
G 7 HOH 135 535 135 HOH HOH A . 
G 7 HOH 136 536 136 HOH HOH A . 
G 7 HOH 137 537 137 HOH HOH A . 
G 7 HOH 138 538 138 HOH HOH A . 
G 7 HOH 139 539 139 HOH HOH A . 
G 7 HOH 140 540 140 HOH HOH A . 
G 7 HOH 141 541 141 HOH HOH A . 
G 7 HOH 142 542 142 HOH HOH A . 
G 7 HOH 143 543 143 HOH HOH A . 
G 7 HOH 144 544 144 HOH HOH A . 
G 7 HOH 145 545 145 HOH HOH A . 
G 7 HOH 146 546 146 HOH HOH A . 
G 7 HOH 147 547 147 HOH HOH A . 
G 7 HOH 148 548 148 HOH HOH A . 
G 7 HOH 149 549 149 HOH HOH A . 
G 7 HOH 150 550 150 HOH HOH A . 
G 7 HOH 151 551 151 HOH HOH A . 
G 7 HOH 152 552 152 HOH HOH A . 
G 7 HOH 153 553 153 HOH HOH A . 
G 7 HOH 154 554 154 HOH HOH A . 
G 7 HOH 155 555 155 HOH HOH A . 
G 7 HOH 156 556 156 HOH HOH A . 
G 7 HOH 157 557 157 HOH HOH A . 
G 7 HOH 158 558 158 HOH HOH A . 
G 7 HOH 159 559 159 HOH HOH A . 
G 7 HOH 160 560 160 HOH HOH A . 
G 7 HOH 161 561 161 HOH HOH A . 
G 7 HOH 162 562 162 HOH HOH A . 
G 7 HOH 163 563 163 HOH HOH A . 
G 7 HOH 164 564 164 HOH HOH A . 
G 7 HOH 165 565 165 HOH HOH A . 
G 7 HOH 166 566 166 HOH HOH A . 
G 7 HOH 167 567 167 HOH HOH A . 
G 7 HOH 168 568 168 HOH HOH A . 
G 7 HOH 169 569 169 HOH HOH A . 
G 7 HOH 170 570 170 HOH HOH A . 
G 7 HOH 171 571 171 HOH HOH A . 
G 7 HOH 172 572 172 HOH HOH A . 
G 7 HOH 173 573 173 HOH HOH A . 
G 7 HOH 174 574 174 HOH HOH A . 
G 7 HOH 175 575 175 HOH HOH A . 
G 7 HOH 176 576 176 HOH HOH A . 
G 7 HOH 177 577 177 HOH HOH A . 
G 7 HOH 178 578 178 HOH HOH A . 
G 7 HOH 179 579 179 HOH HOH A . 
G 7 HOH 180 580 180 HOH HOH A . 
G 7 HOH 181 581 181 HOH HOH A . 
G 7 HOH 182 582 182 HOH HOH A . 
G 7 HOH 183 583 183 HOH HOH A . 
G 7 HOH 184 584 184 HOH HOH A . 
G 7 HOH 185 585 185 HOH HOH A . 
G 7 HOH 186 586 186 HOH HOH A . 
G 7 HOH 187 587 187 HOH HOH A . 
G 7 HOH 188 588 188 HOH HOH A . 
G 7 HOH 189 589 189 HOH HOH A . 
G 7 HOH 190 590 190 HOH HOH A . 
G 7 HOH 191 591 191 HOH HOH A . 
G 7 HOH 192 592 192 HOH HOH A . 
G 7 HOH 193 593 193 HOH HOH A . 
G 7 HOH 194 594 194 HOH HOH A . 
G 7 HOH 195 595 195 HOH HOH A . 
G 7 HOH 196 596 196 HOH HOH A . 
G 7 HOH 197 597 197 HOH HOH A . 
G 7 HOH 198 598 198 HOH HOH A . 
G 7 HOH 199 599 199 HOH HOH A . 
G 7 HOH 200 600 200 HOH HOH A . 
G 7 HOH 201 601 201 HOH HOH A . 
G 7 HOH 202 602 202 HOH HOH A . 
G 7 HOH 203 603 203 HOH HOH A . 
G 7 HOH 204 604 204 HOH HOH A . 
G 7 HOH 205 605 205 HOH HOH A . 
G 7 HOH 206 606 206 HOH HOH A . 
G 7 HOH 207 607 207 HOH HOH A . 
G 7 HOH 208 608 208 HOH HOH A . 
G 7 HOH 209 609 209 HOH HOH A . 
G 7 HOH 210 610 210 HOH HOH A . 
G 7 HOH 211 611 211 HOH HOH A . 
G 7 HOH 212 612 212 HOH HOH A . 
G 7 HOH 213 613 213 HOH HOH A . 
G 7 HOH 214 614 214 HOH HOH A . 
G 7 HOH 215 615 215 HOH HOH A . 
G 7 HOH 216 616 216 HOH HOH A . 
G 7 HOH 217 617 217 HOH HOH A . 
G 7 HOH 218 618 218 HOH HOH A . 
G 7 HOH 219 619 219 HOH HOH A . 
G 7 HOH 220 620 220 HOH HOH A . 
G 7 HOH 221 621 221 HOH HOH A . 
G 7 HOH 222 622 222 HOH HOH A . 
G 7 HOH 223 623 223 HOH HOH A . 
G 7 HOH 224 624 224 HOH HOH A . 
G 7 HOH 225 625 225 HOH HOH A . 
G 7 HOH 226 626 226 HOH HOH A . 
G 7 HOH 227 627 227 HOH HOH A . 
G 7 HOH 228 628 228 HOH HOH A . 
G 7 HOH 229 629 229 HOH HOH A . 
G 7 HOH 230 630 230 HOH HOH A . 
G 7 HOH 231 631 231 HOH HOH A . 
G 7 HOH 232 632 232 HOH HOH A . 
G 7 HOH 233 633 233 HOH HOH A . 
G 7 HOH 234 634 234 HOH HOH A . 
G 7 HOH 235 635 235 HOH HOH A . 
G 7 HOH 236 636 236 HOH HOH A . 
G 7 HOH 237 637 237 HOH HOH A . 
G 7 HOH 238 638 238 HOH HOH A . 
G 7 HOH 239 639 239 HOH HOH A . 
G 7 HOH 240 640 240 HOH HOH A . 
G 7 HOH 241 641 241 HOH HOH A . 
G 7 HOH 242 642 242 HOH HOH A . 
G 7 HOH 243 643 243 HOH HOH A . 
G 7 HOH 244 644 244 HOH HOH A . 
G 7 HOH 245 645 245 HOH HOH A . 
G 7 HOH 246 646 246 HOH HOH A . 
G 7 HOH 247 647 247 HOH HOH A . 
G 7 HOH 248 648 248 HOH HOH A . 
G 7 HOH 249 649 249 HOH HOH A . 
G 7 HOH 250 650 250 HOH HOH A . 
G 7 HOH 251 651 251 HOH HOH A . 
G 7 HOH 252 652 252 HOH HOH A . 
G 7 HOH 253 653 253 HOH HOH A . 
G 7 HOH 254 654 254 HOH HOH A . 
G 7 HOH 255 655 255 HOH HOH A . 
G 7 HOH 256 656 256 HOH HOH A . 
G 7 HOH 257 657 257 HOH HOH A . 
G 7 HOH 258 658 258 HOH HOH A . 
G 7 HOH 259 659 259 HOH HOH A . 
G 7 HOH 260 660 260 HOH HOH A . 
G 7 HOH 261 661 261 HOH HOH A . 
G 7 HOH 262 662 262 HOH HOH A . 
G 7 HOH 263 663 263 HOH HOH A . 
G 7 HOH 264 664 264 HOH HOH A . 
G 7 HOH 265 665 265 HOH HOH A . 
G 7 HOH 266 666 266 HOH HOH A . 
G 7 HOH 267 667 267 HOH HOH A . 
G 7 HOH 268 668 268 HOH HOH A . 
G 7 HOH 269 669 269 HOH HOH A . 
G 7 HOH 270 670 270 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,G 
# 
_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_555 103.6 ? 
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_555 114.5 ? 
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 97.7  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 B C EWW .   ? A EWW 302 ? 1_555 116.9 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 B C EWW .   ? A EWW 302 ? 1_555 112.7 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 B C EWW .   ? A EWW 302 ? 1_555 109.7 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 A C EWW .   ? A EWW 302 ? 1_555 111.5 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 A C EWW .   ? A EWW 302 ? 1_555 114.0 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 A C EWW .   ? A EWW 302 ? 1_555 114.3 ? 
10 N11 B C EWW .   ? A EWW 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N11 A C EWW .   ? A EWW 302 ? 1_555 5.5   ? 
11 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O8  B C EWW .   ? A EWW 302 ? 1_555 81.7  ? 
12 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O8  B C EWW .   ? A EWW 302 ? 1_555 174.5 ? 
13 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O8  B C EWW .   ? A EWW 302 ? 1_555 81.3  ? 
14 N11 B C EWW .   ? A EWW 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O8  B C EWW .   ? A EWW 302 ? 1_555 63.0  ? 
15 N11 A C EWW .   ? A EWW 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O8  B C EWW .   ? A EWW 302 ? 1_555 62.0  ? 
# 
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 2015-01-21 
2 'Structure model' 1 1 2023-11-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' diffrn_source                 
5 2 'Structure model' pdbx_initial_refinement_model 
6 2 'Structure model' pdbx_struct_conn_angle        
7 2 'Structure model' struct_conn                   
8 2 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_database_2.pdbx_DOI'                        
2  2 'Structure model' '_database_2.pdbx_database_accession'         
3  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_alt_id'  
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_alt_id'  
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
15 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
16 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
17 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
18 2 'Structure model' '_pdbx_struct_conn_angle.value'               
19 2 'Structure model' '_struct_conn.pdbx_dist_value'                
20 2 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
21 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
22 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
23 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
24 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
25 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
26 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
27 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
28 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
29 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
30 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
31 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
32 2 'Structure model' '_struct_site.pdbx_auth_asym_id'              
33 2 'Structure model' '_struct_site.pdbx_auth_comp_id'              
34 2 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.3.16 2010/01/06      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345dtb   .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -142.83 56.66   
2 1 LYS A 76  ? ? -111.21 -82.44  
3 1 PHE A 176 ? ? -150.18 72.61   
4 1 ASN A 244 ? ? -96.74  50.25   
5 1 LYS A 252 ? ? 62.04   -135.78 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    235 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   B 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLU 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    236 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -148.46 
# 
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 ? S   ? D MES 1 S   
2 1 N 1 A MES 303 ? O1S ? D MES 1 O1S 
3 1 N 1 A MES 303 ? O2S ? D MES 1 O2S 
4 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 
# 
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  
EWW CL   CL N N 98  
EWW C3   C  Y N 99  
EWW C4   C  Y N 100 
EWW S6   S  N N 101 
EWW O8   O  N N 102 
EWW N11  N  N N 103 
EWW O7   O  N N 104 
EWW C5   C  Y N 105 
EWW C2   C  Y N 106 
EWW C22  C  Y N 107 
EWW C1   C  Y N 108 
EWW C9   C  N N 109 
EWW O12  O  N N 110 
EWW C10  C  N N 111 
EWW S13  S  N N 112 
EWW C14  C  N N 113 
EWW N17  N  N N 114 
EWW C18  C  N N 115 
EWW O21  O  N N 116 
EWW C19  C  N N 117 
EWW C16  C  N N 118 
EWW N15  N  N N 119 
EWW C20  C  N N 120 
EWW H1   H  N N 121 
EWW H2   H  N N 122 
EWW H3   H  N N 123 
EWW H4   H  N N 124 
EWW H5   H  N N 125 
EWW H6   H  N N 126 
EWW H7   H  N N 127 
EWW H8   H  N N 128 
EWW H10  H  N N 129 
EWW H11  H  N N 130 
EWW H12  H  N N 131 
EWW H13  H  N N 132 
GLN N    N  N N 133 
GLN CA   C  N S 134 
GLN C    C  N N 135 
GLN O    O  N N 136 
GLN CB   C  N N 137 
GLN CG   C  N N 138 
GLN CD   C  N N 139 
GLN OE1  O  N N 140 
GLN NE2  N  N N 141 
GLN OXT  O  N N 142 
GLN H    H  N N 143 
GLN H2   H  N N 144 
GLN HA   H  N N 145 
GLN HB2  H  N N 146 
GLN HB3  H  N N 147 
GLN HG2  H  N N 148 
GLN HG3  H  N N 149 
GLN HE21 H  N N 150 
GLN HE22 H  N N 151 
GLN HXT  H  N N 152 
GLU N    N  N N 153 
GLU CA   C  N S 154 
GLU C    C  N N 155 
GLU O    O  N N 156 
GLU CB   C  N N 157 
GLU CG   C  N N 158 
GLU CD   C  N N 159 
GLU OE1  O  N N 160 
GLU OE2  O  N N 161 
GLU OXT  O  N N 162 
GLU H    H  N N 163 
GLU H2   H  N N 164 
GLU HA   H  N N 165 
GLU HB2  H  N N 166 
GLU HB3  H  N N 167 
GLU HG2  H  N N 168 
GLU HG3  H  N N 169 
GLU HE2  H  N N 170 
GLU HXT  H  N N 171 
GLY N    N  N N 172 
GLY CA   C  N N 173 
GLY C    C  N N 174 
GLY O    O  N N 175 
GLY OXT  O  N N 176 
GLY H    H  N N 177 
GLY H2   H  N N 178 
GLY HA2  H  N N 179 
GLY HA3  H  N N 180 
GLY HXT  H  N N 181 
HIS N    N  N N 182 
HIS CA   C  N S 183 
HIS C    C  N N 184 
HIS O    O  N N 185 
HIS CB   C  N N 186 
HIS CG   C  Y N 187 
HIS ND1  N  Y N 188 
HIS CD2  C  Y N 189 
HIS CE1  C  Y N 190 
HIS NE2  N  Y N 191 
HIS OXT  O  N N 192 
HIS H    H  N N 193 
HIS H2   H  N N 194 
HIS HA   H  N N 195 
HIS HB2  H  N N 196 
HIS HB3  H  N N 197 
HIS HD1  H  N N 198 
HIS HD2  H  N N 199 
HIS HE1  H  N N 200 
HIS HE2  H  N N 201 
HIS HXT  H  N N 202 
HOH O    O  N N 203 
HOH H1   H  N N 204 
HOH H2   H  N N 205 
ILE N    N  N N 206 
ILE CA   C  N S 207 
ILE C    C  N N 208 
ILE O    O  N N 209 
ILE CB   C  N S 210 
ILE CG1  C  N N 211 
ILE CG2  C  N N 212 
ILE CD1  C  N N 213 
ILE OXT  O  N N 214 
ILE H    H  N N 215 
ILE H2   H  N N 216 
ILE HA   H  N N 217 
ILE HB   H  N N 218 
ILE HG12 H  N N 219 
ILE HG13 H  N N 220 
ILE HG21 H  N N 221 
ILE HG22 H  N N 222 
ILE HG23 H  N N 223 
ILE HD11 H  N N 224 
ILE HD12 H  N N 225 
ILE HD13 H  N N 226 
ILE HXT  H  N N 227 
LEU N    N  N N 228 
LEU CA   C  N S 229 
LEU C    C  N N 230 
LEU O    O  N N 231 
LEU CB   C  N N 232 
LEU CG   C  N N 233 
LEU CD1  C  N N 234 
LEU CD2  C  N N 235 
LEU OXT  O  N N 236 
LEU H    H  N N 237 
LEU H2   H  N N 238 
LEU HA   H  N N 239 
LEU HB2  H  N N 240 
LEU HB3  H  N N 241 
LEU HG   H  N N 242 
LEU HD11 H  N N 243 
LEU HD12 H  N N 244 
LEU HD13 H  N N 245 
LEU HD21 H  N N 246 
LEU HD22 H  N N 247 
LEU HD23 H  N N 248 
LEU HXT  H  N N 249 
LYS N    N  N N 250 
LYS CA   C  N S 251 
LYS C    C  N N 252 
LYS O    O  N N 253 
LYS CB   C  N N 254 
LYS CG   C  N N 255 
LYS CD   C  N N 256 
LYS CE   C  N N 257 
LYS NZ   N  N N 258 
LYS OXT  O  N N 259 
LYS H    H  N N 260 
LYS H2   H  N N 261 
LYS HA   H  N N 262 
LYS HB2  H  N N 263 
LYS HB3  H  N N 264 
LYS HG2  H  N N 265 
LYS HG3  H  N N 266 
LYS HD2  H  N N 267 
LYS HD3  H  N N 268 
LYS HE2  H  N N 269 
LYS HE3  H  N N 270 
LYS HZ1  H  N N 271 
LYS HZ2  H  N N 272 
LYS HZ3  H  N N 273 
LYS HXT  H  N N 274 
MES O1   O  N N 275 
MES C2   C  N N 276 
MES C3   C  N N 277 
MES N4   N  N N 278 
MES C5   C  N N 279 
MES C6   C  N N 280 
MES C7   C  N N 281 
MES C8   C  N N 282 
MES S    S  N N 283 
MES O1S  O  N N 284 
MES O2S  O  N N 285 
MES O3S  O  N N 286 
MES H21  H  N N 287 
MES H22  H  N N 288 
MES H31  H  N N 289 
MES H32  H  N N 290 
MES HN4  H  N N 291 
MES H51  H  N N 292 
MES H52  H  N N 293 
MES H61  H  N N 294 
MES H62  H  N N 295 
MES H71  H  N N 296 
MES H72  H  N N 297 
MES H81  H  N N 298 
MES H82  H  N N 299 
MET N    N  N N 300 
MET CA   C  N S 301 
MET C    C  N N 302 
MET O    O  N N 303 
MET CB   C  N N 304 
MET CG   C  N N 305 
MET SD   S  N N 306 
MET CE   C  N N 307 
MET OXT  O  N N 308 
MET H    H  N N 309 
MET H2   H  N N 310 
MET HA   H  N N 311 
MET HB2  H  N N 312 
MET HB3  H  N N 313 
MET HG2  H  N N 314 
MET HG3  H  N N 315 
MET HE1  H  N N 316 
MET HE2  H  N N 317 
MET HE3  H  N N 318 
MET HXT  H  N N 319 
PEG C1   C  N N 320 
PEG O1   O  N N 321 
PEG C2   C  N N 322 
PEG O2   O  N N 323 
PEG C3   C  N N 324 
PEG C4   C  N N 325 
PEG O4   O  N N 326 
PEG H11  H  N N 327 
PEG H12  H  N N 328 
PEG HO1  H  N N 329 
PEG H21  H  N N 330 
PEG H22  H  N N 331 
PEG H31  H  N N 332 
PEG H32  H  N N 333 
PEG H41  H  N N 334 
PEG H42  H  N N 335 
PEG HO4  H  N N 336 
PHE N    N  N N 337 
PHE CA   C  N S 338 
PHE C    C  N N 339 
PHE O    O  N N 340 
PHE CB   C  N N 341 
PHE CG   C  Y N 342 
PHE CD1  C  Y N 343 
PHE CD2  C  Y N 344 
PHE CE1  C  Y N 345 
PHE CE2  C  Y N 346 
PHE CZ   C  Y N 347 
PHE OXT  O  N N 348 
PHE H    H  N N 349 
PHE H2   H  N N 350 
PHE HA   H  N N 351 
PHE HB2  H  N N 352 
PHE HB3  H  N N 353 
PHE HD1  H  N N 354 
PHE HD2  H  N N 355 
PHE HE1  H  N N 356 
PHE HE2  H  N N 357 
PHE HZ   H  N N 358 
PHE HXT  H  N N 359 
PRO N    N  N N 360 
PRO CA   C  N S 361 
PRO C    C  N N 362 
PRO O    O  N N 363 
PRO CB   C  N N 364 
PRO CG   C  N N 365 
PRO CD   C  N N 366 
PRO OXT  O  N N 367 
PRO H    H  N N 368 
PRO HA   H  N N 369 
PRO HB2  H  N N 370 
PRO HB3  H  N N 371 
PRO HG2  H  N N 372 
PRO HG3  H  N N 373 
PRO HD2  H  N N 374 
PRO HD3  H  N N 375 
PRO HXT  H  N N 376 
SER N    N  N N 377 
SER CA   C  N S 378 
SER C    C  N N 379 
SER O    O  N N 380 
SER CB   C  N N 381 
SER OG   O  N N 382 
SER OXT  O  N N 383 
SER H    H  N N 384 
SER H2   H  N N 385 
SER HA   H  N N 386 
SER HB2  H  N N 387 
SER HB3  H  N N 388 
SER HG   H  N N 389 
SER HXT  H  N N 390 
THR N    N  N N 391 
THR CA   C  N S 392 
THR C    C  N N 393 
THR O    O  N N 394 
THR CB   C  N R 395 
THR OG1  O  N N 396 
THR CG2  C  N N 397 
THR OXT  O  N N 398 
THR H    H  N N 399 
THR H2   H  N N 400 
THR HA   H  N N 401 
THR HB   H  N N 402 
THR HG1  H  N N 403 
THR HG21 H  N N 404 
THR HG22 H  N N 405 
THR HG23 H  N N 406 
THR HXT  H  N N 407 
TRP N    N  N N 408 
TRP CA   C  N S 409 
TRP C    C  N N 410 
TRP O    O  N N 411 
TRP CB   C  N N 412 
TRP CG   C  Y N 413 
TRP CD1  C  Y N 414 
TRP CD2  C  Y N 415 
TRP NE1  N  Y N 416 
TRP CE2  C  Y N 417 
TRP CE3  C  Y N 418 
TRP CZ2  C  Y N 419 
TRP CZ3  C  Y N 420 
TRP CH2  C  Y N 421 
TRP OXT  O  N N 422 
TRP H    H  N N 423 
TRP H2   H  N N 424 
TRP HA   H  N N 425 
TRP HB2  H  N N 426 
TRP HB3  H  N N 427 
TRP HD1  H  N N 428 
TRP HE1  H  N N 429 
TRP HE3  H  N N 430 
TRP HZ2  H  N N 431 
TRP HZ3  H  N N 432 
TRP HH2  H  N N 433 
TRP HXT  H  N N 434 
TYR N    N  N N 435 
TYR CA   C  N S 436 
TYR C    C  N N 437 
TYR O    O  N N 438 
TYR CB   C  N N 439 
TYR CG   C  Y N 440 
TYR CD1  C  Y N 441 
TYR CD2  C  Y N 442 
TYR CE1  C  Y N 443 
TYR CE2  C  Y N 444 
TYR CZ   C  Y N 445 
TYR OH   O  N N 446 
TYR OXT  O  N N 447 
TYR H    H  N N 448 
TYR H2   H  N N 449 
TYR HA   H  N N 450 
TYR HB2  H  N N 451 
TYR HB3  H  N N 452 
TYR HD1  H  N N 453 
TYR HD2  H  N N 454 
TYR HE1  H  N N 455 
TYR HE2  H  N N 456 
TYR HH   H  N N 457 
TYR HXT  H  N N 458 
VAL N    N  N N 459 
VAL CA   C  N S 460 
VAL C    C  N N 461 
VAL O    O  N N 462 
VAL CB   C  N N 463 
VAL CG1  C  N N 464 
VAL CG2  C  N N 465 
VAL OXT  O  N N 466 
VAL H    H  N N 467 
VAL H2   H  N N 468 
VAL HA   H  N N 469 
VAL HB   H  N N 470 
VAL HG11 H  N N 471 
VAL HG12 H  N N 472 
VAL HG13 H  N N 473 
VAL HG21 H  N N 474 
VAL HG22 H  N N 475 
VAL HG23 H  N N 476 
VAL HXT  H  N N 477 
ZN  ZN   ZN N N 478 
# 
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  
EWW S13 C14  sing N N 92  
EWW S13 C10  sing N N 93  
EWW N17 C14  sing N N 94  
EWW N17 C18  sing N N 95  
EWW O21 C18  doub N N 96  
EWW C14 N15  doub N N 97  
EWW C10 C9   sing N N 98  
EWW C18 C19  sing N N 99  
EWW O12 C9   doub N N 100 
EWW C9  C22  sing N N 101 
EWW C1  C22  doub Y N 102 
EWW C1  C5   sing Y N 103 
EWW N15 C16  sing N N 104 
EWW C22 C2   sing Y N 105 
EWW C19 C16  doub N N 106 
EWW C5  C4   doub Y N 107 
EWW C16 C20  sing N N 108 
EWW C2  C3   doub Y N 109 
EWW C4  C3   sing Y N 110 
EWW C4  S6   sing N N 111 
EWW C3  CL   sing N N 112 
EWW N11 S6   sing N N 113 
EWW O8  S6   doub N N 114 
EWW S6  O7   doub N N 115 
EWW N11 H1   sing N N 116 
EWW N11 H2   sing N N 117 
EWW C5  H3   sing N N 118 
EWW C2  H4   sing N N 119 
EWW C1  H5   sing N N 120 
EWW C10 H6   sing N N 121 
EWW C10 H7   sing N N 122 
EWW C19 H8   sing N N 123 
EWW C20 H10  sing N N 124 
EWW C20 H11  sing N N 125 
EWW C20 H12  sing N N 126 
EWW N17 H13  sing N N 127 
GLN N   CA   sing N N 128 
GLN N   H    sing N N 129 
GLN N   H2   sing N N 130 
GLN CA  C    sing N N 131 
GLN CA  CB   sing N N 132 
GLN CA  HA   sing N N 133 
GLN C   O    doub N N 134 
GLN C   OXT  sing N N 135 
GLN CB  CG   sing N N 136 
GLN CB  HB2  sing N N 137 
GLN CB  HB3  sing N N 138 
GLN CG  CD   sing N N 139 
GLN CG  HG2  sing N N 140 
GLN CG  HG3  sing N N 141 
GLN CD  OE1  doub N N 142 
GLN CD  NE2  sing N N 143 
GLN NE2 HE21 sing N N 144 
GLN NE2 HE22 sing N N 145 
GLN OXT HXT  sing N N 146 
GLU N   CA   sing N N 147 
GLU N   H    sing N N 148 
GLU N   H2   sing N N 149 
GLU CA  C    sing N N 150 
GLU CA  CB   sing N N 151 
GLU CA  HA   sing N N 152 
GLU C   O    doub N N 153 
GLU C   OXT  sing N N 154 
GLU CB  CG   sing N N 155 
GLU CB  HB2  sing N N 156 
GLU CB  HB3  sing N N 157 
GLU CG  CD   sing N N 158 
GLU CG  HG2  sing N N 159 
GLU CG  HG3  sing N N 160 
GLU CD  OE1  doub N N 161 
GLU CD  OE2  sing N N 162 
GLU OE2 HE2  sing N N 163 
GLU OXT HXT  sing N N 164 
GLY N   CA   sing N N 165 
GLY N   H    sing N N 166 
GLY N   H2   sing N N 167 
GLY CA  C    sing N N 168 
GLY CA  HA2  sing N N 169 
GLY CA  HA3  sing N N 170 
GLY C   O    doub N N 171 
GLY C   OXT  sing N N 172 
GLY OXT HXT  sing N N 173 
HIS N   CA   sing N N 174 
HIS N   H    sing N N 175 
HIS N   H2   sing N N 176 
HIS CA  C    sing N N 177 
HIS CA  CB   sing N N 178 
HIS CA  HA   sing N N 179 
HIS C   O    doub N N 180 
HIS C   OXT  sing N N 181 
HIS CB  CG   sing N N 182 
HIS CB  HB2  sing N N 183 
HIS CB  HB3  sing N N 184 
HIS CG  ND1  sing Y N 185 
HIS CG  CD2  doub Y N 186 
HIS ND1 CE1  doub Y N 187 
HIS ND1 HD1  sing N N 188 
HIS CD2 NE2  sing Y N 189 
HIS CD2 HD2  sing N N 190 
HIS CE1 NE2  sing Y N 191 
HIS CE1 HE1  sing N N 192 
HIS NE2 HE2  sing N N 193 
HIS OXT HXT  sing N N 194 
HOH O   H1   sing N N 195 
HOH O   H2   sing N N 196 
ILE N   CA   sing N N 197 
ILE N   H    sing N N 198 
ILE N   H2   sing N N 199 
ILE CA  C    sing N N 200 
ILE CA  CB   sing N N 201 
ILE CA  HA   sing N N 202 
ILE C   O    doub N N 203 
ILE C   OXT  sing N N 204 
ILE CB  CG1  sing N N 205 
ILE CB  CG2  sing N N 206 
ILE CB  HB   sing N N 207 
ILE CG1 CD1  sing N N 208 
ILE CG1 HG12 sing N N 209 
ILE CG1 HG13 sing N N 210 
ILE CG2 HG21 sing N N 211 
ILE CG2 HG22 sing N N 212 
ILE CG2 HG23 sing N N 213 
ILE CD1 HD11 sing N N 214 
ILE CD1 HD12 sing N N 215 
ILE CD1 HD13 sing N N 216 
ILE OXT HXT  sing N N 217 
LEU N   CA   sing N N 218 
LEU N   H    sing N N 219 
LEU N   H2   sing N N 220 
LEU CA  C    sing N N 221 
LEU CA  CB   sing N N 222 
LEU CA  HA   sing N N 223 
LEU C   O    doub N N 224 
LEU C   OXT  sing N N 225 
LEU CB  CG   sing N N 226 
LEU CB  HB2  sing N N 227 
LEU CB  HB3  sing N N 228 
LEU CG  CD1  sing N N 229 
LEU CG  CD2  sing N N 230 
LEU CG  HG   sing N N 231 
LEU CD1 HD11 sing N N 232 
LEU CD1 HD12 sing N N 233 
LEU CD1 HD13 sing N N 234 
LEU CD2 HD21 sing N N 235 
LEU CD2 HD22 sing N N 236 
LEU CD2 HD23 sing N N 237 
LEU OXT HXT  sing N N 238 
LYS N   CA   sing N N 239 
LYS N   H    sing N N 240 
LYS N   H2   sing N N 241 
LYS CA  C    sing N N 242 
LYS CA  CB   sing N N 243 
LYS CA  HA   sing N N 244 
LYS C   O    doub N N 245 
LYS C   OXT  sing N N 246 
LYS CB  CG   sing N N 247 
LYS CB  HB2  sing N N 248 
LYS CB  HB3  sing N N 249 
LYS CG  CD   sing N N 250 
LYS CG  HG2  sing N N 251 
LYS CG  HG3  sing N N 252 
LYS CD  CE   sing N N 253 
LYS CD  HD2  sing N N 254 
LYS CD  HD3  sing N N 255 
LYS CE  NZ   sing N N 256 
LYS CE  HE2  sing N N 257 
LYS CE  HE3  sing N N 258 
LYS NZ  HZ1  sing N N 259 
LYS NZ  HZ2  sing N N 260 
LYS NZ  HZ3  sing N N 261 
LYS OXT HXT  sing N N 262 
MES O1  C2   sing N N 263 
MES O1  C6   sing N N 264 
MES C2  C3   sing N N 265 
MES C2  H21  sing N N 266 
MES C2  H22  sing N N 267 
MES C3  N4   sing N N 268 
MES C3  H31  sing N N 269 
MES C3  H32  sing N N 270 
MES N4  C5   sing N N 271 
MES N4  C7   sing N N 272 
MES N4  HN4  sing N N 273 
MES C5  C6   sing N N 274 
MES C5  H51  sing N N 275 
MES C5  H52  sing N N 276 
MES C6  H61  sing N N 277 
MES C6  H62  sing N N 278 
MES C7  C8   sing N N 279 
MES C7  H71  sing N N 280 
MES C7  H72  sing N N 281 
MES C8  S    sing N N 282 
MES C8  H81  sing N N 283 
MES C8  H82  sing N N 284 
MES S   O1S  doub N N 285 
MES S   O2S  doub N N 286 
MES S   O3S  sing N N 287 
MET N   CA   sing N N 288 
MET N   H    sing N N 289 
MET N   H2   sing N N 290 
MET CA  C    sing N N 291 
MET CA  CB   sing N N 292 
MET CA  HA   sing N N 293 
MET C   O    doub N N 294 
MET C   OXT  sing N N 295 
MET CB  CG   sing N N 296 
MET CB  HB2  sing N N 297 
MET CB  HB3  sing N N 298 
MET CG  SD   sing N N 299 
MET CG  HG2  sing N N 300 
MET CG  HG3  sing N N 301 
MET SD  CE   sing N N 302 
MET CE  HE1  sing N N 303 
MET CE  HE2  sing N N 304 
MET CE  HE3  sing N N 305 
MET OXT HXT  sing N N 306 
PEG C1  O1   sing N N 307 
PEG C1  C2   sing N N 308 
PEG C1  H11  sing N N 309 
PEG C1  H12  sing N N 310 
PEG O1  HO1  sing N N 311 
PEG C2  O2   sing N N 312 
PEG C2  H21  sing N N 313 
PEG C2  H22  sing N N 314 
PEG O2  C3   sing N N 315 
PEG C3  C4   sing N N 316 
PEG C3  H31  sing N N 317 
PEG C3  H32  sing N N 318 
PEG C4  O4   sing N N 319 
PEG C4  H41  sing N N 320 
PEG C4  H42  sing N N 321 
PEG O4  HO4  sing N N 322 
PHE N   CA   sing N N 323 
PHE N   H    sing N N 324 
PHE N   H2   sing N N 325 
PHE CA  C    sing N N 326 
PHE CA  CB   sing N N 327 
PHE CA  HA   sing N N 328 
PHE C   O    doub N N 329 
PHE C   OXT  sing N N 330 
PHE CB  CG   sing N N 331 
PHE CB  HB2  sing N N 332 
PHE CB  HB3  sing N N 333 
PHE CG  CD1  doub Y N 334 
PHE CG  CD2  sing Y N 335 
PHE CD1 CE1  sing Y N 336 
PHE CD1 HD1  sing N N 337 
PHE CD2 CE2  doub Y N 338 
PHE CD2 HD2  sing N N 339 
PHE CE1 CZ   doub Y N 340 
PHE CE1 HE1  sing N N 341 
PHE CE2 CZ   sing Y N 342 
PHE CE2 HE2  sing N N 343 
PHE CZ  HZ   sing N N 344 
PHE OXT HXT  sing N N 345 
PRO N   CA   sing N N 346 
PRO N   CD   sing N N 347 
PRO N   H    sing N N 348 
PRO CA  C    sing N N 349 
PRO CA  CB   sing N N 350 
PRO CA  HA   sing N N 351 
PRO C   O    doub N N 352 
PRO C   OXT  sing N N 353 
PRO CB  CG   sing N N 354 
PRO CB  HB2  sing N N 355 
PRO CB  HB3  sing N N 356 
PRO CG  CD   sing N N 357 
PRO CG  HG2  sing N N 358 
PRO CG  HG3  sing N N 359 
PRO CD  HD2  sing N N 360 
PRO CD  HD3  sing N N 361 
PRO OXT HXT  sing N N 362 
SER N   CA   sing N N 363 
SER N   H    sing N N 364 
SER N   H2   sing N N 365 
SER CA  C    sing N N 366 
SER CA  CB   sing N N 367 
SER CA  HA   sing N N 368 
SER C   O    doub N N 369 
SER C   OXT  sing N N 370 
SER CB  OG   sing N N 371 
SER CB  HB2  sing N N 372 
SER CB  HB3  sing N N 373 
SER OG  HG   sing N N 374 
SER OXT HXT  sing N N 375 
THR N   CA   sing N N 376 
THR N   H    sing N N 377 
THR N   H2   sing N N 378 
THR CA  C    sing N N 379 
THR CA  CB   sing N N 380 
THR CA  HA   sing N N 381 
THR C   O    doub N N 382 
THR C   OXT  sing N N 383 
THR CB  OG1  sing N N 384 
THR CB  CG2  sing N N 385 
THR CB  HB   sing N N 386 
THR OG1 HG1  sing N N 387 
THR CG2 HG21 sing N N 388 
THR CG2 HG22 sing N N 389 
THR CG2 HG23 sing N N 390 
THR OXT HXT  sing N N 391 
TRP N   CA   sing N N 392 
TRP N   H    sing N N 393 
TRP N   H2   sing N N 394 
TRP CA  C    sing N N 395 
TRP CA  CB   sing N N 396 
TRP CA  HA   sing N N 397 
TRP C   O    doub N N 398 
TRP C   OXT  sing N N 399 
TRP CB  CG   sing N N 400 
TRP CB  HB2  sing N N 401 
TRP CB  HB3  sing N N 402 
TRP CG  CD1  doub Y N 403 
TRP CG  CD2  sing Y N 404 
TRP CD1 NE1  sing Y N 405 
TRP CD1 HD1  sing N N 406 
TRP CD2 CE2  doub Y N 407 
TRP CD2 CE3  sing Y N 408 
TRP NE1 CE2  sing Y N 409 
TRP NE1 HE1  sing N N 410 
TRP CE2 CZ2  sing Y N 411 
TRP CE3 CZ3  doub Y N 412 
TRP CE3 HE3  sing N N 413 
TRP CZ2 CH2  doub Y N 414 
TRP CZ2 HZ2  sing N N 415 
TRP CZ3 CH2  sing Y N 416 
TRP CZ3 HZ3  sing N N 417 
TRP CH2 HH2  sing N N 418 
TRP OXT HXT  sing N N 419 
TYR N   CA   sing N N 420 
TYR N   H    sing N N 421 
TYR N   H2   sing N N 422 
TYR CA  C    sing N N 423 
TYR CA  CB   sing N N 424 
TYR CA  HA   sing N N 425 
TYR C   O    doub N N 426 
TYR C   OXT  sing N N 427 
TYR CB  CG   sing N N 428 
TYR CB  HB2  sing N N 429 
TYR CB  HB3  sing N N 430 
TYR CG  CD1  doub Y N 431 
TYR CG  CD2  sing Y N 432 
TYR CD1 CE1  sing Y N 433 
TYR CD1 HD1  sing N N 434 
TYR CD2 CE2  doub Y N 435 
TYR CD2 HD2  sing N N 436 
TYR CE1 CZ   doub Y N 437 
TYR CE1 HE1  sing N N 438 
TYR CE2 CZ   sing Y N 439 
TYR CE2 HE2  sing N N 440 
TYR CZ  OH   sing N N 441 
TYR OH  HH   sing N N 442 
TYR OXT HXT  sing N N 443 
VAL N   CA   sing N N 444 
VAL N   H    sing N N 445 
VAL N   H2   sing N N 446 
VAL CA  C    sing N N 447 
VAL CA  CB   sing N N 448 
VAL CA  HA   sing N N 449 
VAL C   O    doub N N 450 
VAL C   OXT  sing N N 451 
VAL CB  CG1  sing N N 452 
VAL CB  CG2  sing N N 453 
VAL CB  HB   sing N N 454 
VAL CG1 HG11 sing N N 455 
VAL CG1 HG12 sing N N 456 
VAL CG1 HG13 sing N N 457 
VAL CG2 HG21 sing N N 458 
VAL CG2 HG22 sing N N 459 
VAL CG2 HG23 sing N N 460 
VAL OXT HXT  sing N N 461 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                  ZN  
3 '2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' EWW 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                                      MES 
5 'DIMETHYL SULFOXIDE'                                                                        DMS 
6 'DI(HYDROXYETHYL)ETHER'                                                                     PEG 
7 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          ? 
# 
