data_3SAP
# 
_entry.id   3SAP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   3SAP         pdb_00003sap 10.2210/pdb3sap/pdb 
RCSB  RCSB065972   ?            ?                   
WWPDB D_1000065972 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3S9T 'human carbonic anhydrase II with 2-chloro-5-{[(4,6-dimethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'      
unspecified 
PDB 3S8X 'human carbonic anhydrase II with 4-{[(4-methyl-6-oxo-1,6-dihydro-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide' 
unspecified 
PDB 3SAX 'human carbonic anhydrase II with 2-chloro-5-{[(5-ethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'           
unspecified 
PDB 3SBI .                                                                                                                   
unspecified 
PDB 3SBH 'human carbonic anhydrase II with 4-{[(4,6-dimethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'               
unspecified 
# 
_pdbx_database_status.entry_id                        3SAP 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2011-06-03 
_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.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'     1 
'Manakova, E.'     2 
'Tamulaitiene, G.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            51 
_citation.page_first                259 
_citation.page_last                 270 
_citation.year                      2012 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22440859 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2012.02.050 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1 ? 
primary 'Zubriene, A.'      2 ? 
primary 'Baranauskiene, L.' 3 ? 
primary 'Tamulaitiene, G.'  4 ? 
primary 'Manakova, E.'      5 ? 
primary 'Kairys, V.'        6 ? 
primary 'Grazulis, S.'      7 ? 
primary 'Tumkevicius, S.'   8 ? 
primary 'Matulis, D.'       9 ? 
# 
_cell.entry_id           3SAP 
_cell.length_a           42.019 
_cell.length_b           40.956 
_cell.length_c           71.742 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.080 
_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                         3SAP 
_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 BICINE                                                          163.172   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 '4-{[(5-butylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' 365.470   1   ?       ? ? ? 
7 water       nat water                                                           18.015    195 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3SAP 
_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 
BCN non-polymer         . BICINE                                                          ? 'C6 H13 N O4'      163.172 
CYS 'L-peptide linking' y CYSTEINE                                                        ? 'C3 H7 N O2 S'     121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                            ? 'C2 H6 O S'        78.133  
E2I non-polymer         . '4-{[(5-butylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' ? 'C16 H19 N3 O3 S2' 365.470 
GLN 'L-peptide linking' y GLUTAMINE                                                       ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                 ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                                                         ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                                                       ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                                           ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                      ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                                                         ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                                          ? 'C6 H15 N2 O2 1'   147.195 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                          ? 'C6 H13 N O4 S'    195.237 
MET 'L-peptide linking' y METHIONINE                                                      ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                   ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                         ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                          ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                                       ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                      ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                                        ? 'C9 H11 N O3'      181.189 
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          3SAP 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   40.2 
_exptl_crystal.density_Matthews      2.1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '2.3M Na-bicine pH 9, 2.3M Na-malonate pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR555 FLAT PANEL' 
_diffrn_detector.pdbx_collection_date   2010-11-14 
_diffrn_detector.details                'Detector swing-out angle up to 30 degrees' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8174 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X11' 
_diffrn_source.pdbx_wavelength_list        0.8174 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X11 
# 
_reflns.entry_id                     3SAP 
_reflns.d_resolution_high            1.750 
_reflns.d_resolution_low             30.360 
_reflns.number_all                   ? 
_reflns.number_obs                   23825 
_reflns.pdbx_Rmerge_I_obs            0.058 
_reflns.pdbx_netI_over_sigmaI        30.300 
_reflns.pdbx_Rsym_value              0.058 
_reflns.pdbx_redundancy              7.200 
_reflns.percent_possible_obs         99.000 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   ? 
_reflns.B_iso_Wilson_estimate        18.8 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.75 1.84  ? 25158 ? 0.266 2.4  0.266 ? 7.30 ? 3435 98.60 1  1 
1.84 1.96  ? 23917 ? 0.169 3.8  0.169 ? 7.30 ? 3265 98.80 2  1 
1.96 2.09  ? 22438 ? 0.116 5.5  0.116 ? 7.30 ? 3065 98.90 3  1 
2.09 2.26  ? 20965 ? 0.088 7.3  0.088 ? 7.30 ? 2871 99.20 4  1 
2.26 2.47  ? 19366 ? 0.071 9.1  0.071 ? 7.30 ? 2654 99.20 5  1 
2.47 2.77  ? 17491 ? 0.056 11.2 0.056 ? 7.30 ? 2401 99.50 6  1 
2.77 3.20  ? 15506 ? 0.046 12.6 0.046 ? 7.30 ? 2137 99.60 7  1 
3.20 3.91  ? 13014 ? 0.039 15.6 0.039 ? 7.20 ? 1818 99.70 8  1 
3.91 5.53  ? 9418  ? 0.033 17.8 0.033 ? 6.70 ? 1408 99.40 9  1 
5.53 30.36 ? 4437  ? 0.032 19.2 0.032 ? 5.80 ? 771  94.60 10 1 
# 
_refine.entry_id                                 3SAP 
_refine.ls_d_res_high                            1.75 
_refine.ls_d_res_low                             28.89 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_number_reflns_obs                     23812 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_R_Free_selection_details            random 
_refine.details                                  ? 
_refine.ls_R_factor_all                          0.182 
_refine.ls_R_factor_obs                          0.182 
_refine.ls_R_factor_R_work                       0.182 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.229 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  2419 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.632 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          MR 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                51.24 
_refine.B_iso_min                                5.91 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          0 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB entry 3HLJ' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             195 
_refine_hist.number_atoms_total               2292 
_refine_hist.d_res_high                       1.75 
_refine_hist.d_res_low                        28.89 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       0.015  ? ? ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    1.487  ? ? ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 6.658  ? ? ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 34.888 ? ? ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         0.104  ? ? ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.750 
_refine_ls_shell.d_res_low                        1.795 
_refine_ls_shell.number_reflns_obs                1569 
_refine_ls_shell.number_reflns_R_free             173 
_refine_ls_shell.R_factor_R_work                  0.285 
_refine_ls_shell.R_factor_R_free                  0.329 
_refine_ls_shell.R_factor_R_free_error            0.138 
_refine_ls_shell.percent_reflns_obs               98.36 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3SAP 
_struct.title                     
'Crystal structure of human carbonic anhydrase isozyme II with 4-{[(5-butyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3SAP 
_struct_keywords.text            'drug design, sulfonamide, 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 ? 
# 
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  ? TRP A 16  ? GLY A 12  TRP A 16  5 ? 5 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  262 1_555 ? ? ? ? ? ? ? 2.000 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  262 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  262 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F E2I . N48 ? ? A ZN  262 A E2I 266 1_555 ? ? ? ? ? ? ? 2.002 ? ? 
# 
_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 0.63 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 7.40 
# 
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 ILE A 91  ? O ILE A 91  N PHE A 70  ? N PHE A 70  
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  262 ? 4  'BINDING SITE FOR RESIDUE ZN A 262'  
AC2 Software A BCN 263 ? 7  'BINDING SITE FOR RESIDUE BCN A 263' 
AC3 Software A MES 264 ? 5  'BINDING SITE FOR RESIDUE MES A 264' 
AC4 Software A DMS 265 ? 3  'BINDING SITE FOR RESIDUE DMS A 265' 
AC5 Software A E2I 266 ? 16 'BINDING SITE FOR RESIDUE E2I A 266' 
# 
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  E2I F .   ? E2I A 266 . ? 1_555 ? 
5  AC2 7  TYR A 114 ? TYR A 114 . ? 1_555 ? 
6  AC2 7  LYS A 148 ? LYS A 149 . ? 1_555 ? 
7  AC2 7  LYS A 212 ? LYS A 213 . ? 1_555 ? 
8  AC2 7  GLU A 213 ? GLU A 214 . ? 1_555 ? 
9  AC2 7  PRO A 214 ? PRO A 215 . ? 1_555 ? 
10 AC2 7  HOH G .   ? HOH A 330 . ? 1_555 ? 
11 AC2 7  HOH G .   ? HOH A 401 . ? 1_555 ? 
12 AC3 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
13 AC3 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
14 AC3 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
15 AC3 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
16 AC3 5  LEU A 228 ? LEU A 229 . ? 1_555 ? 
17 AC4 3  TYR A 7   ? TYR A 7   . ? 1_555 ? 
18 AC4 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
19 AC4 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
20 AC5 16 GLN A 92  ? GLN A 92  . ? 1_555 ? 
21 AC5 16 HIS A 94  ? HIS A 94  . ? 1_555 ? 
22 AC5 16 HIS A 96  ? HIS A 96  . ? 1_555 ? 
23 AC5 16 HIS A 119 ? HIS A 119 . ? 1_555 ? 
24 AC5 16 VAL A 121 ? VAL A 121 . ? 1_555 ? 
25 AC5 16 PHE A 130 ? PHE A 131 . ? 1_555 ? 
26 AC5 16 GLN A 135 ? GLN A 136 . ? 1_555 ? 
27 AC5 16 VAL A 142 ? VAL A 143 . ? 1_555 ? 
28 AC5 16 LEU A 197 ? LEU A 198 . ? 1_555 ? 
29 AC5 16 THR A 198 ? THR A 199 . ? 1_555 ? 
30 AC5 16 THR A 199 ? THR A 200 . ? 1_555 ? 
31 AC5 16 PRO A 201 ? PRO A 202 . ? 1_555 ? 
32 AC5 16 LEU A 203 ? LEU A 204 . ? 1_555 ? 
33 AC5 16 TRP A 208 ? TRP A 209 . ? 1_555 ? 
34 AC5 16 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
35 AC5 16 HOH G .   ? HOH A 448 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3SAP 
_atom_sites.fract_transf_matrix[1][1]   0.023799 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005969 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024416 
_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]   0.014371 
_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  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 9.276   1.021   7.976   1.00 26.46 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.159  -0.082  8.482   1.00 25.44 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.411   -1.056  9.403   1.00 23.49 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.558   -2.254  9.248   1.00 22.69 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 11.415  0.461   9.179   1.00 27.41 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 12.521  -0.549  9.329   1.00 29.81 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 13.440  -0.811  8.331   1.00 34.34 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 12.856  -1.357  10.365  1.00 33.88 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 14.291  -1.736  8.745   1.00 34.06 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 13.955  -2.090  9.975   1.00 34.47 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.608   -0.556  10.342  1.00 20.94 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.888   -1.466  11.260  1.00 18.20 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.869   -2.271  10.489  1.00 16.51 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.349   -1.828  9.471   1.00 15.36 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.221   -0.729  12.424  1.00 18.02 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 6.027   0.086   12.035  1.00 17.91 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.996   1.411   11.681  1.00 16.25 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.669   -0.373  12.001  1.00 15.57 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.698   1.794   11.411  1.00 17.93 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.869   0.713   11.585  1.00 15.83 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 4.062   -1.611  12.250  1.00 14.99 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.481   0.613   11.459  1.00 15.91 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.693   -1.712  12.093  1.00 15.45 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.921   -0.603  11.710  1.00 16.65 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.594   -3.468  10.980  1.00 15.68 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.592   -4.295  10.339  1.00 15.80 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.220   -5.447  11.236  1.00 15.83 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.239   -5.326  12.453  1.00 15.19 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 4.916   -6.581  10.623  1.00 17.29 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.526   -7.736  11.413  1.00 18.86 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.410   -8.993  11.273  1.00 21.16 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.037   -10.060 11.791  1.00 22.23 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.048   -8.046  11.156  1.00 17.52 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.104   -6.978  11.698  1.00 15.16 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.710   -6.977  13.050  1.00 16.02 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.599   -5.979  10.855  1.00 12.96 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 0.822   -5.980  13.550  1.00 13.17 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.707   -4.985  11.331  1.00 14.09 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.332   -4.992  12.683  1.00 14.22 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.534  -4.010  13.136  1.00 13.79 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.582   -8.877  10.636  1.00 22.86 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.513   -10.040 10.510  1.00 23.59 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.538   -10.327 11.608  1.00 25.01 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.620   -9.624  12.627  1.00 26.20 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.364   -11.358 11.398  1.00 26.11 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.390  -11.761 12.387  1.00 26.04 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.360  -10.636 12.734  1.00 25.49 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.833  -10.523 13.882  1.00 25.33 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.184  -12.962 11.873  1.00 27.01 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.344  -13.393 12.752  1.00 29.50 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 13.105  -14.511 12.076  1.00 33.51 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 14.353  -14.889 12.862  1.00 35.18 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 15.172  -15.879 12.084  1.00 38.45 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 11.628  -9.811  11.725  1.00 23.94 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 12.665  -8.807  11.800  1.00 22.56 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 12.155  -7.408  12.078  1.00 21.02 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 12.923  -6.571  12.545  1.00 20.90 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 13.546  -8.893  10.536  1.00 22.44 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 14.216  -10.233 10.386  1.00 23.04 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 15.269  -10.629 11.182  1.00 25.59 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 13.946  -11.280 9.572   1.00 25.15 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 15.630  -11.855 10.853  1.00 25.75 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 14.836  -12.277 9.884   1.00 24.40 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 10.854  -7.174  11.864  1.00 19.94 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 10.265  -5.850  12.122  1.00 18.79 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 8.901   -5.881  12.851  1.00 18.44 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 8.190   -4.856  12.901  1.00 17.48 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 10.116  -5.087  10.810  1.00 18.39 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 9.039   -5.679  9.880   1.00 19.61 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 8.490   -6.758  10.130  1.00 21.54 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 8.753   -4.973  8.794   1.00 20.25 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 8.563   -7.042  13.408  1.00 17.39 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 7.261   -7.244  14.074  1.00 16.62 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 7.183   -6.611  15.453  1.00 16.15 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 8.090   -5.903  15.887  1.00 16.00 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 6.078   -6.867  16.184  1.00 15.27 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 5.852   -6.238  17.497  1.00 15.32 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 7.009   -6.268  18.497  1.00 15.08 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 7.171   -5.315  19.272  1.00 14.97 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 4.679   -7.058  18.057  1.00 15.35 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 3.933   -7.433  16.859  1.00 14.71 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 4.951   -7.729  15.800  1.00 16.03 ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 7.788   -7.353  18.507  1.00 15.27 ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 8.893   -7.476  19.430  1.00 16.73 ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 10.014  -6.460  19.127  1.00 15.91 ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 10.852  -6.202  19.982  1.00 16.62 ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 9.446   -8.907  19.394  1.00 18.05 ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 10.146  -9.297  18.082  1.00 21.24 ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 9.261   -9.888  16.941  1.00 26.02 ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 8.030   -9.595  16.831  1.00 20.50 ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 9.858   -10.647 16.111  1.00 24.05 ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 10.001  -5.893  17.922  1.00 15.79 ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 11.004  -4.901  17.471  1.00 15.20 ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 10.587  -3.443  17.644  1.00 15.81 ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 11.438  -2.520  17.628  1.00 14.32 ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 11.366  -5.150  15.998  1.00 15.78 ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 12.075  -6.457  15.777  1.00 17.93 ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 13.442  -6.595  15.913  1.00 19.64 ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 11.609  -7.677  15.420  1.00 19.47 ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 13.784  -7.850  15.666  1.00 18.56 ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 12.694  -8.528  15.364  1.00 18.74 ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 9.283   -3.223  17.813  1.00 13.61 ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 8.735   -1.870  17.808  1.00 13.35 ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 9.339   -0.880  18.812  1.00 12.68 ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 9.383   0.325   18.503  1.00 13.78 ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 7.203   -1.906  17.943  1.00 12.06 ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 6.526   -2.586  16.789  1.00 12.96 ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 7.093   -3.031  15.626  1.00 11.32 ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 5.117   -2.858  16.680  1.00 11.83 ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 6.131   -3.605  14.815  1.00 12.43 ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 4.908   -3.489  15.427  1.00 13.53 ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 4.021   -2.629  17.524  1.00 10.50 ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 3.641   -3.914  15.001  1.00 13.75 ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 2.763   -3.076  17.117  1.00 11.12 ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 2.577   -3.685  15.860  1.00 12.62 ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 9.816   -1.369  19.960  1.00 12.79 ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 10.274  -0.484  21.048  1.00 14.58 ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 11.505  0.319   20.639  1.00 14.73 ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 11.760  1.369   21.227  1.00 15.29 ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 10.561  -1.248  22.344  1.00 14.56 ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 11.745  -2.165  22.235  1.00 15.64 ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 13.009  -1.801  22.646  1.00 18.41 ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 11.861  -3.401  21.711  1.00 17.81 ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 13.852  -2.786  22.400  1.00 16.01 ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 13.185  -3.768  21.828  1.00 16.57 ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 18  ? 12.255  -0.212  19.671  1.00 16.48 ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 18  ? 13.497  0.434   19.185  1.00 17.62 ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 18  ? 13.158  1.763   18.518  1.00 18.54 ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 18  ? 13.768  2.782   18.839  1.00 19.59 ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 18  ? 14.258  -0.492  18.231  1.00 18.00 ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 18  ? 14.975  -1.647  18.939  1.00 17.81 ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 18  ? 15.607  -2.618  17.941  1.00 18.57 ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 18  ? 14.627  -3.663  17.407  1.00 17.65 ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 18  ? 15.247  -4.474  16.321  1.00 15.75 ? 18  LYS A NZ  1 
ATOM   135  N  N   . ASP A 1 19  ? 12.147  1.782   17.650  1.00 18.49 ? 19  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 19  ? 11.701  3.061   17.074  1.00 19.80 ? 19  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 19  ? 10.714  3.841   17.930  1.00 19.72 ? 19  ASP A C   1 
ATOM   138  O  O   . ASP A 1 19  ? 10.650  5.081   17.838  1.00 19.79 ? 19  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 19  ? 11.150  2.878   15.666  1.00 20.70 ? 19  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 19  ? 12.240  2.852   14.624  1.00 25.06 ? 19  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 19  ? 13.286  3.484   14.855  1.00 27.92 ? 19  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 19  ? 12.046  2.199   13.577  1.00 31.28 ? 19  ASP A OD2 1 
ATOM   143  N  N   . PHE A 1 20  ? 9.953   3.112   18.757  1.00 18.14 ? 20  PHE A N   1 
ATOM   144  C  CA  . PHE A 1 20  ? 8.847   3.666   19.564  1.00 17.39 ? 20  PHE A CA  1 
ATOM   145  C  C   . PHE A 1 20  ? 8.931   3.170   20.999  1.00 16.89 ? 20  PHE A C   1 
ATOM   146  O  O   . PHE A 1 20  ? 8.250   2.199   21.371  1.00 15.15 ? 20  PHE A O   1 
ATOM   147  C  CB  . PHE A 1 20  ? 7.506   3.261   18.936  1.00 17.88 ? 20  PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 20  ? 7.382   3.682   17.514  1.00 17.30 ? 20  PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 20  ? 6.973   4.976   17.197  1.00 19.20 ? 20  PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 20  ? 7.726   2.802   16.483  1.00 17.57 ? 20  PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 20  ? 6.869   5.365   15.871  1.00 19.31 ? 20  PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 20  ? 7.646   3.186   15.166  1.00 20.47 ? 20  PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 20  ? 7.216   4.481   14.862  1.00 19.54 ? 20  PHE A CZ  1 
ATOM   154  N  N   . PRO A 1 21  ? 9.798   3.811   21.818  1.00 15.65 ? 21  PRO A N   1 
ATOM   155  C  CA  . PRO A 1 21  ? 10.078  3.324   23.163  1.00 15.34 ? 21  PRO A CA  1 
ATOM   156  C  C   . PRO A 1 21  ? 8.851   3.203   24.077  1.00 14.41 ? 21  PRO A C   1 
ATOM   157  O  O   . PRO A 1 21  ? 8.862   2.420   25.026  1.00 14.58 ? 21  PRO A O   1 
ATOM   158  C  CB  . PRO A 1 21  ? 11.099  4.347   23.720  1.00 15.92 ? 21  PRO A CB  1 
ATOM   159  C  CG  . PRO A 1 21  ? 11.686  4.968   22.539  1.00 17.34 ? 21  PRO A CG  1 
ATOM   160  C  CD  . PRO A 1 21  ? 10.605  5.011   21.494  1.00 16.24 ? 21  PRO A CD  1 
ATOM   161  N  N   A ILE A 1 22  ? 7.798   3.977   23.790  0.50 13.78 ? 22  ILE A N   1 
ATOM   162  N  N   B ILE A 1 22  ? 7.811   3.976   23.763  0.50 13.72 ? 22  ILE A N   1 
ATOM   163  C  CA  A ILE A 1 22  ? 6.532   3.844   24.511  0.50 13.30 ? 22  ILE A CA  1 
ATOM   164  C  CA  B ILE A 1 22  ? 6.526   3.873   24.432  0.50 13.05 ? 22  ILE A CA  1 
ATOM   165  C  C   A ILE A 1 22  ? 5.909   2.444   24.355  0.50 12.81 ? 22  ILE A C   1 
ATOM   166  C  C   B ILE A 1 22  ? 5.905   2.466   24.330  0.50 12.70 ? 22  ILE A C   1 
ATOM   167  O  O   A ILE A 1 22  ? 4.990   2.106   25.100  0.50 12.07 ? 22  ILE A O   1 
ATOM   168  O  O   B ILE A 1 22  ? 4.991   2.148   25.089  0.50 11.90 ? 22  ILE A O   1 
ATOM   169  C  CB  A ILE A 1 22  ? 5.484   4.971   24.134  0.50 12.34 ? 22  ILE A CB  1 
ATOM   170  C  CB  B ILE A 1 22  ? 5.526   4.966   23.917  0.50 12.32 ? 22  ILE A CB  1 
ATOM   171  C  CG1 A ILE A 1 22  ? 4.388   5.125   25.202  0.50 13.36 ? 22  ILE A CG1 1 
ATOM   172  C  CG1 B ILE A 1 22  ? 4.496   5.324   24.989  0.50 12.72 ? 22  ILE A CG1 1 
ATOM   173  C  CG2 A ILE A 1 22  ? 4.861   4.704   22.767  0.50 13.37 ? 22  ILE A CG2 1 
ATOM   174  C  CG2 B ILE A 1 22  ? 4.916   4.567   22.556  0.50 12.91 ? 22  ILE A CG2 1 
ATOM   175  C  CD1 A ILE A 1 22  ? 4.817   5.753   26.512  0.50 12.47 ? 22  ILE A CD1 1 
ATOM   176  C  CD1 B ILE A 1 22  ? 3.518   6.420   24.588  0.50 12.53 ? 22  ILE A CD1 1 
ATOM   177  N  N   . ALA A 1 23  ? 6.426   1.628   23.431  1.00 13.48 ? 23  ALA A N   1 
ATOM   178  C  CA  . ALA A 1 23  ? 5.993   0.181   23.343  1.00 14.28 ? 23  ALA A CA  1 
ATOM   179  C  C   . ALA A 1 23  ? 6.072   -0.543  24.688  1.00 15.22 ? 23  ALA A C   1 
ATOM   180  O  O   . ALA A 1 23  ? 5.303   -1.492  24.964  1.00 14.71 ? 23  ALA A O   1 
ATOM   181  C  CB  . ALA A 1 23  ? 6.811   -0.600  22.294  1.00 15.05 ? 23  ALA A CB  1 
ATOM   182  N  N   . LYS A 1 24  ? 7.014   -0.111  25.535  1.00 16.11 ? 24  LYS A N   1 
ATOM   183  C  CA  . LYS A 1 24  ? 7.179   -0.723  26.848  1.00 16.60 ? 24  LYS A CA  1 
ATOM   184  C  C   . LYS A 1 24  ? 6.563   0.166   27.938  1.00 17.09 ? 24  LYS A C   1 
ATOM   185  O  O   . LYS A 1 24  ? 6.942   0.052   29.109  1.00 17.53 ? 24  LYS A O   1 
ATOM   186  C  CB  . LYS A 1 24  ? 8.677   -0.902  27.151  1.00 17.04 ? 24  LYS A CB  1 
ATOM   187  C  CG  . LYS A 1 24  ? 9.420   -1.789  26.189  1.00 19.06 ? 24  LYS A CG  1 
ATOM   188  C  CD  . LYS A 1 24  ? 10.840  -1.998  26.707  1.00 22.15 ? 24  LYS A CD  1 
ATOM   189  C  CE  . LYS A 1 24  ? 11.612  -2.985  25.820  1.00 22.72 ? 24  LYS A CE  1 
ATOM   190  N  NZ  . LYS A 1 24  ? 11.134  -4.392  25.971  1.00 24.27 ? 24  LYS A NZ  1 
ATOM   191  N  N   . GLY A 1 25  ? 5.607   1.031   27.570  1.00 16.45 ? 25  GLY A N   1 
ATOM   192  C  CA  . GLY A 1 25  ? 5.054   1.991   28.540  1.00 15.88 ? 25  GLY A CA  1 
ATOM   193  C  C   . GLY A 1 25  ? 4.030   1.417   29.514  1.00 15.22 ? 25  GLY A C   1 
ATOM   194  O  O   . GLY A 1 25  ? 3.834   0.188   29.615  1.00 16.41 ? 25  GLY A O   1 
ATOM   195  N  N   . GLU A 1 26  ? 3.375   2.321   30.241  1.00 15.17 ? 26  GLU A N   1 
ATOM   196  C  CA  . GLU A 1 26  ? 2.519   1.960   31.378  1.00 15.77 ? 26  GLU A CA  1 
ATOM   197  C  C   . GLU A 1 26  ? 1.083   1.633   31.003  1.00 13.78 ? 26  GLU A C   1 
ATOM   198  O  O   . GLU A 1 26  ? 0.360   1.061   31.806  1.00 13.43 ? 26  GLU A O   1 
ATOM   199  C  CB  . GLU A 1 26  ? 2.504   3.078   32.440  1.00 17.80 ? 26  GLU A CB  1 
ATOM   200  C  CG  . GLU A 1 26  ? 3.844   3.308   33.125  1.00 21.89 ? 26  GLU A CG  1 
ATOM   201  C  CD  . GLU A 1 26  ? 4.437   2.007   33.676  1.00 26.94 ? 26  GLU A CD  1 
ATOM   202  O  OE1 . GLU A 1 26  ? 3.815   1.335   34.546  1.00 30.94 ? 26  GLU A OE1 1 
ATOM   203  O  OE2 . GLU A 1 26  ? 5.531   1.642   33.215  1.00 28.20 ? 26  GLU A OE2 1 
ATOM   204  N  N   . ARG A 1 27  ? 0.656   1.997   29.798  1.00 13.19 ? 27  ARG A N   1 
ATOM   205  C  CA  . ARG A 1 27  ? -0.746  1.743   29.416  1.00 12.92 ? 27  ARG A CA  1 
ATOM   206  C  C   . ARG A 1 27  ? -0.843  1.274   27.932  1.00 11.50 ? 27  ARG A C   1 
ATOM   207  O  O   . ARG A 1 27  ? -1.551  1.849   27.098  1.00 10.77 ? 27  ARG A O   1 
ATOM   208  C  CB  . ARG A 1 27  ? -1.669  2.940   29.776  1.00 13.07 ? 27  ARG A CB  1 
ATOM   209  C  CG  . ARG A 1 27  ? -1.353  4.246   29.052  1.00 15.11 ? 27  ARG A CG  1 
ATOM   210  C  CD  . ARG A 1 27  ? -2.344  5.418   29.294  1.00 17.45 ? 27  ARG A CD  1 
ATOM   211  N  NE  . ARG A 1 27  ? -3.540  5.328   28.425  1.00 17.89 ? 27  ARG A NE  1 
ATOM   212  C  CZ  . ARG A 1 27  ? -4.468  6.274   28.300  1.00 18.23 ? 27  ARG A CZ  1 
ATOM   213  N  NH1 . ARG A 1 27  ? -4.379  7.443   28.952  1.00 15.07 ? 27  ARG A NH1 1 
ATOM   214  N  NH2 . ARG A 1 27  ? -5.466  6.071   27.473  1.00 17.57 ? 27  ARG A NH2 1 
ATOM   215  N  N   . GLN A 1 28  ? -0.119  0.192   27.638  1.00 11.00 ? 28  GLN A N   1 
ATOM   216  C  CA  . GLN A 1 28  ? -0.079  -0.342  26.276  1.00 10.21 ? 28  GLN A CA  1 
ATOM   217  C  C   . GLN A 1 28  ? -1.238  -1.297  25.982  1.00 9.67  ? 28  GLN A C   1 
ATOM   218  O  O   . GLN A 1 28  ? -1.757  -1.970  26.879  1.00 9.73  ? 28  GLN A O   1 
ATOM   219  C  CB  . GLN A 1 28  ? 1.265   -1.029  26.034  1.00 10.89 ? 28  GLN A CB  1 
ATOM   220  C  CG  . GLN A 1 28  ? 2.406   0.008   25.863  1.00 10.43 ? 28  GLN A CG  1 
ATOM   221  C  CD  . GLN A 1 28  ? 2.228   0.835   24.563  1.00 10.02 ? 28  GLN A CD  1 
ATOM   222  O  OE1 . GLN A 1 28  ? 2.416   0.315   23.477  1.00 10.40 ? 28  GLN A OE1 1 
ATOM   223  N  NE2 . GLN A 1 28  ? 1.893   2.130   24.690  1.00 8.83  ? 28  GLN A NE2 1 
ATOM   224  N  N   . SER A 1 29  ? -1.614  -1.339  24.705  1.00 8.88  ? 29  SER A N   1 
ATOM   225  C  CA  . SER A 1 29  ? -2.662  -2.234  24.223  1.00 9.07  ? 29  SER A CA  1 
ATOM   226  C  C   . SER A 1 29  ? -2.138  -3.095  23.084  1.00 8.36  ? 29  SER A C   1 
ATOM   227  O  O   . SER A 1 29  ? -1.227  -2.672  22.379  1.00 9.38  ? 29  SER A O   1 
ATOM   228  C  CB  . SER A 1 29  ? -3.848  -1.421  23.720  1.00 7.46  ? 29  SER A CB  1 
ATOM   229  O  OG  . SER A 1 29  ? -4.417  -0.721  24.844  1.00 8.07  ? 29  SER A OG  1 
ATOM   230  N  N   . PRO A 1 30  ? -2.763  -4.269  22.853  1.00 8.46  ? 30  PRO A N   1 
ATOM   231  C  CA  . PRO A 1 30  ? -3.917  -4.821  23.573  1.00 8.63  ? 30  PRO A CA  1 
ATOM   232  C  C   . PRO A 1 30  ? -3.541  -5.479  24.905  1.00 8.53  ? 30  PRO A C   1 
ATOM   233  O  O   . PRO A 1 30  ? -2.368  -5.471  25.285  1.00 8.51  ? 30  PRO A O   1 
ATOM   234  C  CB  . PRO A 1 30  ? -4.428  -5.888  22.597  1.00 8.25  ? 30  PRO A CB  1 
ATOM   235  C  CG  . PRO A 1 30  ? -3.140  -6.428  21.966  1.00 8.68  ? 30  PRO A CG  1 
ATOM   236  C  CD  . PRO A 1 30  ? -2.286  -5.175  21.787  1.00 8.23  ? 30  PRO A CD  1 
ATOM   237  N  N   . VAL A 1 31  ? -4.533  -6.068  25.577  1.00 9.54  ? 31  VAL A N   1 
ATOM   238  C  CA  . VAL A 1 31  ? -4.348  -6.813  26.805  1.00 10.00 ? 31  VAL A CA  1 
ATOM   239  C  C   . VAL A 1 31  ? -5.277  -8.035  26.806  1.00 9.94  ? 31  VAL A C   1 
ATOM   240  O  O   . VAL A 1 31  ? -6.262  -8.103  26.051  1.00 9.42  ? 31  VAL A O   1 
ATOM   241  C  CB  . VAL A 1 31  ? -4.622  -5.953  28.100  1.00 11.49 ? 31  VAL A CB  1 
ATOM   242  C  CG1 . VAL A 1 31  ? -3.665  -4.748  28.209  1.00 8.11  ? 31  VAL A CG1 1 
ATOM   243  C  CG2 . VAL A 1 31  ? -6.131  -5.515  28.221  1.00 11.63 ? 31  VAL A CG2 1 
ATOM   244  N  N   . ASP A 1 32  ? -4.915  -9.018  27.622  1.00 9.88  ? 32  ASP A N   1 
ATOM   245  C  CA  . ASP A 1 32  ? -5.813  -10.098 27.921  1.00 10.11 ? 32  ASP A CA  1 
ATOM   246  C  C   . ASP A 1 32  ? -6.859  -9.570  28.900  1.00 10.18 ? 32  ASP A C   1 
ATOM   247  O  O   . ASP A 1 32  ? -6.522  -8.903  29.888  1.00 10.32 ? 32  ASP A O   1 
ATOM   248  C  CB  . ASP A 1 32  ? -5.063  -11.266 28.539  1.00 11.24 ? 32  ASP A CB  1 
ATOM   249  C  CG  . ASP A 1 32  ? -5.985  -12.419 28.860  1.00 11.76 ? 32  ASP A CG  1 
ATOM   250  O  OD1 . ASP A 1 32  ? -6.648  -12.889 27.902  1.00 12.03 ? 32  ASP A OD1 1 
ATOM   251  O  OD2 . ASP A 1 32  ? -6.051  -12.840 30.069  1.00 13.00 ? 32  ASP A OD2 1 
ATOM   252  N  N   . ILE A 1 33  ? -8.118  -9.842  28.600  1.00 10.72 ? 33  ILE A N   1 
ATOM   253  C  CA  . ILE A 1 33  ? -9.238  -9.490  29.457  1.00 11.92 ? 33  ILE A CA  1 
ATOM   254  C  C   . ILE A 1 33  ? -9.553  -10.732 30.323  1.00 13.15 ? 33  ILE A C   1 
ATOM   255  O  O   . ILE A 1 33  ? -10.080 -11.757 29.842  1.00 14.11 ? 33  ILE A O   1 
ATOM   256  C  CB  . ILE A 1 33  ? -10.478 -9.071  28.658  1.00 11.27 ? 33  ILE A CB  1 
ATOM   257  C  CG1 . ILE A 1 33  ? -10.176 -7.808  27.824  1.00 10.70 ? 33  ILE A CG1 1 
ATOM   258  C  CG2 . ILE A 1 33  ? -11.645 -8.773  29.614  1.00 9.51  ? 33  ILE A CG2 1 
ATOM   259  C  CD1 . ILE A 1 33  ? -11.241 -7.515  26.714  1.00 12.87 ? 33  ILE A CD1 1 
ATOM   260  N  N   . ASP A 1 34  ? -9.150  -10.639 31.573  1.00 14.50 ? 34  ASP A N   1 
ATOM   261  C  CA  . ASP A 1 34  ? -9.419  -11.691 32.566  1.00 15.86 ? 34  ASP A CA  1 
ATOM   262  C  C   . ASP A 1 34  ? -10.852 -11.417 33.093  1.00 16.48 ? 34  ASP A C   1 
ATOM   263  O  O   . ASP A 1 34  ? -11.072 -10.512 33.918  1.00 16.88 ? 34  ASP A O   1 
ATOM   264  C  CB  . ASP A 1 34  ? -8.316  -11.680 33.639  1.00 16.37 ? 34  ASP A CB  1 
ATOM   265  C  CG  . ASP A 1 34  ? -8.555  -12.697 34.807  1.00 21.15 ? 34  ASP A CG  1 
ATOM   266  O  OD1 . ASP A 1 34  ? -9.689  -13.137 35.063  1.00 23.05 ? 34  ASP A OD1 1 
ATOM   267  O  OD2 . ASP A 1 34  ? -7.576  -13.027 35.508  1.00 26.66 ? 34  ASP A OD2 1 
ATOM   268  N  N   . THR A 1 35  ? -11.814 -12.154 32.554  1.00 16.83 ? 35  THR A N   1 
ATOM   269  C  CA  . THR A 1 35  ? -13.256 -11.889 32.760  1.00 17.90 ? 35  THR A CA  1 
ATOM   270  C  C   . THR A 1 35  ? -13.659 -12.017 34.222  1.00 18.89 ? 35  THR A C   1 
ATOM   271  O  O   . THR A 1 35  ? -14.661 -11.413 34.663  1.00 19.00 ? 35  THR A O   1 
ATOM   272  C  CB  . THR A 1 35  ? -14.147 -12.865 31.967  1.00 18.72 ? 35  THR A CB  1 
ATOM   273  O  OG1 . THR A 1 35  ? -13.896 -14.211 32.394  1.00 18.56 ? 35  THR A OG1 1 
ATOM   274  C  CG2 . THR A 1 35  ? -13.895 -12.748 30.472  1.00 15.96 ? 35  THR A CG2 1 
ATOM   275  N  N   . HIS A 1 36  ? -12.901 -12.828 34.964  1.00 19.66 ? 36  HIS A N   1 
ATOM   276  C  CA  . HIS A 1 36  ? -13.166 -12.985 36.390  1.00 21.05 ? 36  HIS A CA  1 
ATOM   277  C  C   . HIS A 1 36  ? -12.635 -11.842 37.266  1.00 21.64 ? 36  HIS A C   1 
ATOM   278  O  O   . HIS A 1 36  ? -13.286 -11.472 38.247  1.00 23.11 ? 36  HIS A O   1 
ATOM   279  C  CB  . HIS A 1 36  ? -12.772 -14.406 36.856  1.00 21.18 ? 36  HIS A CB  1 
ATOM   280  C  CG  . HIS A 1 36  ? -13.673 -15.459 36.289  1.00 22.33 ? 36  HIS A CG  1 
ATOM   281  N  ND1 . HIS A 1 36  ? -13.275 -16.346 35.310  1.00 23.50 ? 36  HIS A ND1 1 
ATOM   282  C  CD2 . HIS A 1 36  ? -14.991 -15.700 36.503  1.00 22.86 ? 36  HIS A CD2 1 
ATOM   283  C  CE1 . HIS A 1 36  ? -14.296 -17.113 34.974  1.00 23.51 ? 36  HIS A CE1 1 
ATOM   284  N  NE2 . HIS A 1 36  ? -15.348 -16.746 35.684  1.00 26.70 ? 36  HIS A NE2 1 
ATOM   285  N  N   . THR A 1 37  ? -11.532 -11.214 36.873  1.00 21.97 ? 37  THR A N   1 
ATOM   286  C  CA  . THR A 1 37  ? -10.990 -10.101 37.648  1.00 22.31 ? 37  THR A CA  1 
ATOM   287  C  C   . THR A 1 37  ? -11.438 -8.708  37.145  1.00 21.67 ? 37  THR A C   1 
ATOM   288  O  O   . THR A 1 37  ? -11.153 -7.701  37.793  1.00 20.98 ? 37  THR A O   1 
ATOM   289  C  CB  . THR A 1 37  ? -9.446  -10.189 37.845  1.00 23.44 ? 37  THR A CB  1 
ATOM   290  O  OG1 . THR A 1 37  ? -8.782  -10.121 36.587  1.00 26.25 ? 37  THR A OG1 1 
ATOM   291  C  CG2 . THR A 1 37  ? -9.055  -11.486 38.540  1.00 23.76 ? 37  THR A CG2 1 
ATOM   292  N  N   . ALA A 1 38  ? -12.147 -8.664  36.013  1.00 19.90 ? 38  ALA A N   1 
ATOM   293  C  CA  . ALA A 1 38  ? -12.774 -7.416  35.550  1.00 20.05 ? 38  ALA A CA  1 
ATOM   294  C  C   . ALA A 1 38  ? -13.861 -7.019  36.564  1.00 20.77 ? 38  ALA A C   1 
ATOM   295  O  O   . ALA A 1 38  ? -14.636 -7.848  37.030  1.00 21.43 ? 38  ALA A O   1 
ATOM   296  C  CB  . ALA A 1 38  ? -13.358 -7.573  34.148  1.00 19.90 ? 38  ALA A CB  1 
ATOM   297  N  N   . LYS A 1 39  ? -13.868 -5.756  36.954  1.00 21.03 ? 39  LYS A N   1 
ATOM   298  C  CA  . LYS A 1 39  ? -14.802 -5.293  37.970  1.00 21.94 ? 39  LYS A CA  1 
ATOM   299  C  C   . LYS A 1 39  ? -16.115 -4.801  37.321  1.00 21.88 ? 39  LYS A C   1 
ATOM   300  O  O   . LYS A 1 39  ? -16.114 -3.839  36.538  1.00 20.13 ? 39  LYS A O   1 
ATOM   301  C  CB  . LYS A 1 39  ? -14.123 -4.168  38.751  1.00 22.14 ? 39  LYS A CB  1 
ATOM   302  C  CG  . LYS A 1 39  ? -15.022 -3.364  39.684  1.00 23.64 ? 39  LYS A CG  1 
ATOM   303  C  CD  . LYS A 1 39  ? -15.085 -3.948  41.097  1.00 24.78 ? 39  LYS A CD  1 
ATOM   304  C  CE  . LYS A 1 39  ? -16.150 -3.197  41.910  1.00 28.32 ? 39  LYS A CE  1 
ATOM   305  N  NZ  . LYS A 1 39  ? -16.184 -3.539  43.357  1.00 29.31 ? 39  LYS A NZ  1 
ATOM   306  N  N   . TYR A 1 40  ? -17.234 -5.432  37.662  1.00 22.46 ? 40  TYR A N   1 
ATOM   307  C  CA  . TYR A 1 40  ? -18.528 -4.839  37.287  1.00 24.05 ? 40  TYR A CA  1 
ATOM   308  C  C   . TYR A 1 40  ? -18.705 -3.428  37.893  1.00 24.19 ? 40  TYR A C   1 
ATOM   309  O  O   . TYR A 1 40  ? -18.554 -3.229  39.116  1.00 23.51 ? 40  TYR A O   1 
ATOM   310  C  CB  . TYR A 1 40  ? -19.706 -5.752  37.639  1.00 25.21 ? 40  TYR A CB  1 
ATOM   311  C  CG  . TYR A 1 40  ? -21.040 -5.044  37.521  1.00 25.79 ? 40  TYR A CG  1 
ATOM   312  C  CD1 . TYR A 1 40  ? -21.499 -4.572  36.279  1.00 25.25 ? 40  TYR A CD1 1 
ATOM   313  C  CD2 . TYR A 1 40  ? -21.837 -4.826  38.653  1.00 28.28 ? 40  TYR A CD2 1 
ATOM   314  C  CE1 . TYR A 1 40  ? -22.707 -3.918  36.161  1.00 26.04 ? 40  TYR A CE1 1 
ATOM   315  C  CE2 . TYR A 1 40  ? -23.072 -4.161  38.545  1.00 26.84 ? 40  TYR A CE2 1 
ATOM   316  C  CZ  . TYR A 1 40  ? -23.488 -3.706  37.300  1.00 27.59 ? 40  TYR A CZ  1 
ATOM   317  O  OH  . TYR A 1 40  ? -24.685 -3.055  37.185  1.00 28.35 ? 40  TYR A OH  1 
ATOM   318  N  N   . ASP A 1 41  ? -19.027 -2.457  37.033  1.00 24.10 ? 41  ASP A N   1 
ATOM   319  C  CA  . ASP A 1 41  ? -19.148 -1.064  37.473  1.00 25.26 ? 41  ASP A CA  1 
ATOM   320  C  C   . ASP A 1 41  ? -20.546 -0.542  37.166  1.00 26.29 ? 41  ASP A C   1 
ATOM   321  O  O   . ASP A 1 41  ? -20.850 -0.198  36.025  1.00 26.24 ? 41  ASP A O   1 
ATOM   322  C  CB  . ASP A 1 41  ? -18.060 -0.178  36.861  1.00 25.54 ? 41  ASP A CB  1 
ATOM   323  C  CG  . ASP A 1 41  ? -18.136 1.282   37.339  1.00 26.32 ? 41  ASP A CG  1 
ATOM   324  O  OD1 . ASP A 1 41  ? -19.112 1.669   38.007  1.00 26.78 ? 41  ASP A OD1 1 
ATOM   325  O  OD2 . ASP A 1 41  ? -17.216 2.056   37.026  1.00 28.37 ? 41  ASP A OD2 1 
ATOM   326  N  N   . PRO A 1 42  ? -21.408 -0.477  38.198  1.00 27.44 ? 42  PRO A N   1 
ATOM   327  C  CA  . PRO A 1 42  ? -22.807 -0.079  37.983  1.00 27.76 ? 42  PRO A CA  1 
ATOM   328  C  C   . PRO A 1 42  ? -22.940 1.406   37.615  1.00 27.71 ? 42  PRO A C   1 
ATOM   329  O  O   . PRO A 1 42  ? -23.993 1.825   37.114  1.00 28.27 ? 42  PRO A O   1 
ATOM   330  C  CB  . PRO A 1 42  ? -23.489 -0.378  39.337  1.00 27.87 ? 42  PRO A CB  1 
ATOM   331  C  CG  . PRO A 1 42  ? -22.454 -1.112  40.170  1.00 28.43 ? 42  PRO A CG  1 
ATOM   332  C  CD  . PRO A 1 42  ? -21.114 -0.734  39.620  1.00 27.54 ? 42  PRO A CD  1 
ATOM   333  N  N   . SER A 1 43  ? -21.886 2.190   37.838  1.00 27.75 ? 43  SER A N   1 
ATOM   334  C  CA  . SER A 1 43  ? -21.870 3.584   37.377  1.00 27.76 ? 43  SER A CA  1 
ATOM   335  C  C   . SER A 1 43  ? -21.571 3.759   35.879  1.00 27.02 ? 43  SER A C   1 
ATOM   336  O  O   . SER A 1 43  ? -21.660 4.876   35.360  1.00 26.99 ? 43  SER A O   1 
ATOM   337  C  CB  . SER A 1 43  ? -20.899 4.442   38.204  1.00 27.79 ? 43  SER A CB  1 
ATOM   338  O  OG  . SER A 1 43  ? -19.543 4.156   37.880  1.00 29.75 ? 43  SER A OG  1 
ATOM   339  N  N   . LEU A 1 44  ? -21.198 2.683   35.179  1.00 26.13 ? 44  LEU A N   1 
ATOM   340  C  CA  . LEU A 1 44  ? -21.009 2.785   33.727  1.00 25.11 ? 44  LEU A CA  1 
ATOM   341  C  C   . LEU A 1 44  ? -22.343 2.887   33.005  1.00 25.42 ? 44  LEU A C   1 
ATOM   342  O  O   . LEU A 1 44  ? -23.291 2.169   33.328  1.00 25.84 ? 44  LEU A O   1 
ATOM   343  C  CB  . LEU A 1 44  ? -20.219 1.604   33.167  1.00 24.71 ? 44  LEU A CB  1 
ATOM   344  C  CG  . LEU A 1 44  ? -18.738 1.546   33.512  1.00 22.48 ? 44  LEU A CG  1 
ATOM   345  C  CD1 . LEU A 1 44  ? -18.256 0.150   33.197  1.00 24.70 ? 44  LEU A CD1 1 
ATOM   346  C  CD2 . LEU A 1 44  ? -17.928 2.597   32.750  1.00 23.08 ? 44  LEU A CD2 1 
ATOM   347  N  N   . LYS A 1 45  ? -22.397 3.772   32.016  1.00 25.49 ? 45  LYS A N   1 
ATOM   348  C  CA  . LYS A 1 45  ? -23.629 4.006   31.258  1.00 25.39 ? 45  LYS A CA  1 
ATOM   349  C  C   . LYS A 1 45  ? -23.697 3.052   30.086  1.00 24.90 ? 45  LYS A C   1 
ATOM   350  O  O   . LYS A 1 45  ? -22.658 2.496   29.690  1.00 25.12 ? 45  LYS A O   1 
ATOM   351  C  CB  . LYS A 1 45  ? -23.627 5.413   30.708  1.00 25.41 ? 45  LYS A CB  1 
ATOM   352  C  CG  . LYS A 1 45  ? -23.643 6.504   31.753  1.00 28.47 ? 45  LYS A CG  1 
ATOM   353  C  CD  . LYS A 1 45  ? -23.659 7.857   31.053  1.00 33.05 ? 45  LYS A CD  1 
ATOM   354  C  CE  . LYS A 1 45  ? -24.391 8.905   31.865  1.00 35.94 ? 45  LYS A CE  1 
ATOM   355  N  NZ  . LYS A 1 45  ? -25.848 8.978   31.519  1.00 39.03 ? 45  LYS A NZ  1 
ATOM   356  N  N   . PRO A 1 46  ? -24.914 2.860   29.511  1.00 23.93 ? 46  PRO A N   1 
ATOM   357  C  CA  . PRO A 1 46  ? -24.989 2.206   28.202  1.00 23.35 ? 46  PRO A CA  1 
ATOM   358  C  C   . PRO A 1 46  ? -24.132 2.965   27.188  1.00 22.22 ? 46  PRO A C   1 
ATOM   359  O  O   . PRO A 1 46  ? -24.050 4.192   27.248  1.00 21.96 ? 46  PRO A O   1 
ATOM   360  C  CB  . PRO A 1 46  ? -26.479 2.345   27.818  1.00 23.36 ? 46  PRO A CB  1 
ATOM   361  C  CG  . PRO A 1 46  ? -27.195 2.419   29.097  1.00 23.93 ? 46  PRO A CG  1 
ATOM   362  C  CD  . PRO A 1 46  ? -26.260 3.186   30.039  1.00 23.88 ? 46  PRO A CD  1 
ATOM   363  N  N   . LEU A 1 47  ? -23.503 2.228   26.274  1.00 21.94 ? 47  LEU A N   1 
ATOM   364  C  CA  . LEU A 1 47  ? -22.770 2.832   25.190  1.00 20.58 ? 47  LEU A CA  1 
ATOM   365  C  C   . LEU A 1 47  ? -23.778 3.420   24.218  1.00 21.00 ? 47  LEU A C   1 
ATOM   366  O  O   . LEU A 1 47  ? -24.837 2.823   23.994  1.00 20.89 ? 47  LEU A O   1 
ATOM   367  C  CB  . LEU A 1 47  ? -21.914 1.782   24.485  1.00 21.25 ? 47  LEU A CB  1 
ATOM   368  C  CG  . LEU A 1 47  ? -20.870 2.304   23.516  1.00 22.57 ? 47  LEU A CG  1 
ATOM   369  C  CD1 . LEU A 1 47  ? -19.826 3.146   24.282  1.00 23.27 ? 47  LEU A CD1 1 
ATOM   370  C  CD2 . LEU A 1 47  ? -20.229 1.137   22.771  1.00 23.18 ? 47  LEU A CD2 1 
ATOM   371  N  N   . SER A 1 48  ? -23.464 4.592   23.678  1.00 18.69 ? 48  SER A N   1 
ATOM   372  C  CA  . SER A 1 48  ? -24.298 5.232   22.665  1.00 19.50 ? 48  SER A CA  1 
ATOM   373  C  C   . SER A 1 48  ? -23.590 5.270   21.334  1.00 19.45 ? 48  SER A C   1 
ATOM   374  O  O   . SER A 1 48  ? -22.623 6.029   21.135  1.00 18.98 ? 48  SER A O   1 
ATOM   375  C  CB  . SER A 1 48  ? -24.715 6.645   23.082  1.00 19.02 ? 48  SER A CB  1 
ATOM   376  O  OG  . SER A 1 48  ? -25.344 7.334   22.003  1.00 20.38 ? 48  SER A OG  1 
ATOM   377  N  N   . VAL A 1 49  ? -24.111 4.470   20.410  1.00 19.38 ? 49  VAL A N   1 
ATOM   378  C  CA  . VAL A 1 49  ? -23.598 4.415   19.048  1.00 20.65 ? 49  VAL A CA  1 
ATOM   379  C  C   . VAL A 1 49  ? -24.585 5.096   18.087  1.00 21.32 ? 49  VAL A C   1 
ATOM   380  O  O   . VAL A 1 49  ? -25.682 4.585   17.821  1.00 21.78 ? 49  VAL A O   1 
ATOM   381  C  CB  . VAL A 1 49  ? -23.280 2.956   18.625  1.00 20.48 ? 49  VAL A CB  1 
ATOM   382  C  CG1 . VAL A 1 49  ? -22.533 2.914   17.283  1.00 21.84 ? 49  VAL A CG1 1 
ATOM   383  C  CG2 . VAL A 1 49  ? -22.457 2.242   19.707  1.00 21.21 ? 49  VAL A CG2 1 
ATOM   384  N  N   . SER A 1 50  ? -24.218 6.267   17.596  1.00 20.66 ? 50  SER A N   1 
ATOM   385  C  CA  . SER A 1 50  ? -25.069 6.971   16.624  1.00 21.89 ? 50  SER A CA  1 
ATOM   386  C  C   . SER A 1 50  ? -24.427 6.986   15.250  1.00 21.23 ? 50  SER A C   1 
ATOM   387  O  O   . SER A 1 50  ? -23.659 7.879   14.932  1.00 21.17 ? 50  SER A O   1 
ATOM   388  C  CB  . SER A 1 50  ? -25.418 8.375   17.112  1.00 21.87 ? 50  SER A CB  1 
ATOM   389  O  OG  . SER A 1 50  ? -25.904 8.271   18.424  1.00 26.02 ? 50  SER A OG  1 
ATOM   390  N  N   . TYR A 1 51  ? -24.704 5.951   14.456  1.00 20.88 ? 51  TYR A N   1 
ATOM   391  C  CA  . TYR A 1 51  ? -24.097 5.799   13.137  1.00 20.47 ? 51  TYR A CA  1 
ATOM   392  C  C   . TYR A 1 51  ? -25.073 6.013   11.968  1.00 21.36 ? 51  TYR A C   1 
ATOM   393  O  O   . TYR A 1 51  ? -24.685 5.847   10.815  1.00 20.87 ? 51  TYR A O   1 
ATOM   394  C  CB  . TYR A 1 51  ? -23.443 4.417   12.961  1.00 18.88 ? 51  TYR A CB  1 
ATOM   395  C  CG  . TYR A 1 51  ? -22.158 4.123   13.742  1.00 18.51 ? 51  TYR A CG  1 
ATOM   396  C  CD1 . TYR A 1 51  ? -21.423 5.144   14.378  1.00 15.99 ? 51  TYR A CD1 1 
ATOM   397  C  CD2 . TYR A 1 51  ? -21.672 2.822   13.799  1.00 15.45 ? 51  TYR A CD2 1 
ATOM   398  C  CE1 . TYR A 1 51  ? -20.250 4.844   15.104  1.00 14.14 ? 51  TYR A CE1 1 
ATOM   399  C  CE2 . TYR A 1 51  ? -20.496 2.502   14.473  1.00 14.68 ? 51  TYR A CE2 1 
ATOM   400  C  CZ  . TYR A 1 51  ? -19.789 3.523   15.134  1.00 16.46 ? 51  TYR A CZ  1 
ATOM   401  O  OH  . TYR A 1 51  ? -18.630 3.180   15.795  1.00 15.08 ? 51  TYR A OH  1 
ATOM   402  N  N   . ASP A 1 52  ? -26.322 6.380   12.260  1.00 23.18 ? 52  ASP A N   1 
ATOM   403  C  CA  . ASP A 1 52  ? -27.322 6.554   11.178  1.00 25.02 ? 52  ASP A CA  1 
ATOM   404  C  C   . ASP A 1 52  ? -26.885 7.517   10.049  1.00 24.50 ? 52  ASP A C   1 
ATOM   405  O  O   . ASP A 1 52  ? -27.172 7.277   8.868   1.00 25.25 ? 52  ASP A O   1 
ATOM   406  C  CB  . ASP A 1 52  ? -28.719 6.877   11.732  1.00 25.89 ? 52  ASP A CB  1 
ATOM   407  C  CG  . ASP A 1 52  ? -28.910 8.329   12.049  1.00 29.10 ? 52  ASP A CG  1 
ATOM   408  O  OD1 . ASP A 1 52  ? -28.563 8.756   13.177  1.00 31.97 ? 52  ASP A OD1 1 
ATOM   409  O  OD2 . ASP A 1 52  ? -29.465 9.033   11.172  1.00 35.70 ? 52  ASP A OD2 1 
ATOM   410  N  N   . GLN A 1 53  ? -26.155 8.566   10.409  1.00 24.08 ? 53  GLN A N   1 
ATOM   411  C  CA  . GLN A 1 53  ? -25.708 9.571   9.433   1.00 24.09 ? 53  GLN A CA  1 
ATOM   412  C  C   . GLN A 1 53  ? -24.276 9.374   8.930   1.00 22.47 ? 53  GLN A C   1 
ATOM   413  O  O   . GLN A 1 53  ? -23.732 10.265  8.270   1.00 21.94 ? 53  GLN A O   1 
ATOM   414  C  CB  . GLN A 1 53  ? -25.873 10.981  10.030  1.00 24.31 ? 53  GLN A CB  1 
ATOM   415  C  CG  . GLN A 1 53  ? -27.332 11.357  10.301  1.00 27.82 ? 53  GLN A CG  1 
ATOM   416  C  CD  . GLN A 1 53  ? -28.149 11.327  9.022   1.00 31.28 ? 53  GLN A CD  1 
ATOM   417  O  OE1 . GLN A 1 53  ? -27.750 11.912  8.004   1.00 35.85 ? 53  GLN A OE1 1 
ATOM   418  N  NE2 . GLN A 1 53  ? -29.275 10.623  9.050   1.00 33.34 ? 53  GLN A NE2 1 
ATOM   419  N  N   . ALA A 1 54  ? -23.669 8.217   9.222   1.00 21.00 ? 54  ALA A N   1 
ATOM   420  C  CA  . ALA A 1 54  ? -22.285 7.946   8.816   1.00 19.60 ? 54  ALA A CA  1 
ATOM   421  C  C   . ALA A 1 54  ? -22.065 8.148   7.322   1.00 19.64 ? 54  ALA A C   1 
ATOM   422  O  O   . ALA A 1 54  ? -22.916 7.765   6.495   1.00 19.62 ? 54  ALA A O   1 
ATOM   423  C  CB  . ALA A 1 54  ? -21.807 6.518   9.276   1.00 19.99 ? 54  ALA A CB  1 
ATOM   424  N  N   . THR A 1 55  ? -20.944 8.782   6.979   1.00 18.66 ? 55  THR A N   1 
ATOM   425  C  CA  . THR A 1 55  ? -20.545 8.945   5.586   1.00 18.56 ? 55  THR A CA  1 
ATOM   426  C  C   . THR A 1 55  ? -19.206 8.308   5.288   1.00 17.90 ? 55  THR A C   1 
ATOM   427  O  O   . THR A 1 55  ? -18.168 8.925   5.510   1.00 15.67 ? 55  THR A O   1 
ATOM   428  C  CB  . THR A 1 55  ? -20.450 10.452  5.184   1.00 18.39 ? 55  THR A CB  1 
ATOM   429  O  OG1 . THR A 1 55  ? -21.720 11.068  5.367   1.00 20.78 ? 55  THR A OG1 1 
ATOM   430  C  CG2 . THR A 1 55  ? -20.045 10.567  3.696   1.00 20.85 ? 55  THR A CG2 1 
ATOM   431  N  N   . SER A 1 56  ? -19.207 7.086   4.761   1.00 18.10 ? 56  SER A N   1 
ATOM   432  C  CA  . SER A 1 56  ? -17.951 6.502   4.305   1.00 18.97 ? 56  SER A CA  1 
ATOM   433  C  C   . SER A 1 56  ? -17.489 7.182   3.012   1.00 19.63 ? 56  SER A C   1 
ATOM   434  O  O   . SER A 1 56  ? -18.310 7.667   2.212   1.00 21.05 ? 56  SER A O   1 
ATOM   435  C  CB  . SER A 1 56  ? -18.056 4.979   4.101   1.00 19.11 ? 56  SER A CB  1 
ATOM   436  O  OG  . SER A 1 56  ? -19.101 4.660   3.179   1.00 19.06 ? 56  SER A OG  1 
ATOM   437  N  N   . LEU A 1 57  ? -16.181 7.234   2.811   1.00 19.49 ? 57  LEU A N   1 
ATOM   438  C  CA  . LEU A 1 57  ? -15.633 7.891   1.619   1.00 20.17 ? 57  LEU A CA  1 
ATOM   439  C  C   . LEU A 1 57  ? -14.738 6.993   0.780   1.00 20.00 ? 57  LEU A C   1 
ATOM   440  O  O   . LEU A 1 57  ? -14.735 7.055   -0.455  1.00 19.89 ? 57  LEU A O   1 
ATOM   441  C  CB  . LEU A 1 57  ? -14.839 9.126   2.031   1.00 21.16 ? 57  LEU A CB  1 
ATOM   442  C  CG  . LEU A 1 57  ? -15.666 10.197  2.746   1.00 22.19 ? 57  LEU A CG  1 
ATOM   443  C  CD1 . LEU A 1 57  ? -14.727 11.288  3.211   1.00 22.61 ? 57  LEU A CD1 1 
ATOM   444  C  CD2 . LEU A 1 57  ? -16.784 10.733  1.838   1.00 24.79 ? 57  LEU A CD2 1 
ATOM   445  N  N   . ARG A 1 58  ? -13.949 6.173   1.460   1.00 18.40 ? 58  ARG A N   1 
ATOM   446  C  CA  . ARG A 1 58  ? -12.886 5.498   0.796   1.00 18.83 ? 58  ARG A CA  1 
ATOM   447  C  C   . ARG A 1 58  ? -12.395 4.336   1.614   1.00 18.46 ? 58  ARG A C   1 
ATOM   448  O  O   . ARG A 1 58  ? -12.433 4.378   2.843   1.00 17.93 ? 58  ARG A O   1 
ATOM   449  C  CB  . ARG A 1 58  ? -11.725 6.465   0.662   1.00 19.14 ? 58  ARG A CB  1 
ATOM   450  C  CG  . ARG A 1 58  ? -10.835 6.174   -0.474  1.00 22.67 ? 58  ARG A CG  1 
ATOM   451  C  CD  . ARG A 1 58  ? -9.821  7.265   -0.576  1.00 27.15 ? 58  ARG A CD  1 
ATOM   452  N  NE  . ARG A 1 58  ? -9.004  7.239   0.631   1.00 26.06 ? 58  ARG A NE  1 
ATOM   453  C  CZ  . ARG A 1 58  ? -7.697  7.432   0.624   1.00 27.14 ? 58  ARG A CZ  1 
ATOM   454  N  NH1 . ARG A 1 58  ? -7.083  7.677   -0.530  1.00 27.57 ? 58  ARG A NH1 1 
ATOM   455  N  NH2 . ARG A 1 58  ? -7.019  7.404   1.770   1.00 27.58 ? 58  ARG A NH2 1 
ATOM   456  N  N   . ILE A 1 59  ? -11.894 3.343   0.902   1.00 17.69 ? 59  ILE A N   1 
ATOM   457  C  CA  . ILE A 1 59  ? -11.209 2.228   1.528   1.00 17.94 ? 59  ILE A CA  1 
ATOM   458  C  C   . ILE A 1 59  ? -9.765  2.194   1.018   1.00 18.10 ? 59  ILE A C   1 
ATOM   459  O  O   . ILE A 1 59  ? -9.477  2.364   -0.186  1.00 18.31 ? 59  ILE A O   1 
ATOM   460  C  CB  . ILE A 1 59  ? -11.989 0.904   1.307   1.00 17.16 ? 59  ILE A CB  1 
ATOM   461  C  CG1 . ILE A 1 59  ? -11.336 -0.253  2.089   1.00 17.48 ? 59  ILE A CG1 1 
ATOM   462  C  CG2 . ILE A 1 59  ? -12.126 0.578   -0.214  1.00 18.26 ? 59  ILE A CG2 1 
ATOM   463  C  CD1 . ILE A 1 59  ? -12.117 -1.583  1.997   1.00 16.79 ? 59  ILE A CD1 1 
ATOM   464  N  N   . LEU A 1 60  ? -8.835  1.996   1.943   1.00 18.03 ? 60  LEU A N   1 
ATOM   465  C  CA  . LEU A 1 60  ? -7.424  2.066   1.638   1.00 17.63 ? 60  LEU A CA  1 
ATOM   466  C  C   . LEU A 1 60  ? -6.625  0.885   2.185   1.00 17.56 ? 60  LEU A C   1 
ATOM   467  O  O   . LEU A 1 60  ? -6.789  0.524   3.357   1.00 16.40 ? 60  LEU A O   1 
ATOM   468  C  CB  . LEU A 1 60  ? -6.863  3.380   2.242   1.00 18.56 ? 60  LEU A CB  1 
ATOM   469  C  CG  . LEU A 1 60  ? -5.349  3.546   2.316   1.00 19.66 ? 60  LEU A CG  1 
ATOM   470  C  CD1 . LEU A 1 60  ? -4.720  3.760   0.923   1.00 19.98 ? 60  LEU A CD1 1 
ATOM   471  C  CD2 . LEU A 1 60  ? -4.983  4.700   3.278   1.00 18.15 ? 60  LEU A CD2 1 
ATOM   472  N  N   . ASN A 1 61  ? -5.731  0.329   1.360   1.00 16.57 ? 61  ASN A N   1 
ATOM   473  C  CA  . ASN A 1 61  ? -4.711  -0.604  1.832   1.00 17.46 ? 61  ASN A CA  1 
ATOM   474  C  C   . ASN A 1 61  ? -3.461  0.198   2.216   1.00 17.66 ? 61  ASN A C   1 
ATOM   475  O  O   . ASN A 1 61  ? -2.743  0.684   1.336   1.00 17.35 ? 61  ASN A O   1 
ATOM   476  C  CB  . ASN A 1 61  ? -4.388  -1.668  0.766   1.00 17.12 ? 61  ASN A CB  1 
ATOM   477  C  CG  . ASN A 1 61  ? -3.306  -2.670  1.201   1.00 17.29 ? 61  ASN A CG  1 
ATOM   478  O  OD1 . ASN A 1 61  ? -2.468  -2.389  2.060   1.00 17.60 ? 61  ASN A OD1 1 
ATOM   479  N  ND2 . ASN A 1 61  ? -3.315  -3.864  0.587   1.00 19.39 ? 61  ASN A ND2 1 
ATOM   480  N  N   . ASN A 1 62  ? -3.199  0.325   3.519   1.00 17.22 ? 62  ASN A N   1 
ATOM   481  C  CA  . ASN A 1 62  ? -2.056  1.132   3.990   1.00 18.42 ? 62  ASN A CA  1 
ATOM   482  C  C   . ASN A 1 62  ? -0.802  0.316   4.232   1.00 19.05 ? 62  ASN A C   1 
ATOM   483  O  O   . ASN A 1 62  ? 0.166   0.803   4.839   1.00 20.85 ? 62  ASN A O   1 
ATOM   484  C  CB  . ASN A 1 62  ? -2.424  1.962   5.243   1.00 18.46 ? 62  ASN A CB  1 
ATOM   485  C  CG  . ASN A 1 62  ? -2.681  1.092   6.484   1.00 17.99 ? 62  ASN A CG  1 
ATOM   486  O  OD1 . ASN A 1 62  ? -2.413  -0.130  6.495   1.00 15.49 ? 62  ASN A OD1 1 
ATOM   487  N  ND2 . ASN A 1 62  ? -3.172  1.730   7.551   1.00 18.86 ? 62  ASN A ND2 1 
ATOM   488  N  N   . GLY A 1 63  ? -0.803  -0.933  3.756   1.00 17.97 ? 63  GLY A N   1 
ATOM   489  C  CA  . GLY A 1 63  ? 0.303   -1.839  3.963   1.00 16.95 ? 63  GLY A CA  1 
ATOM   490  C  C   . GLY A 1 63  ? 0.358   -2.574  5.301   1.00 16.75 ? 63  GLY A C   1 
ATOM   491  O  O   . GLY A 1 63  ? 1.211   -3.434  5.482   1.00 16.72 ? 63  GLY A O   1 
ATOM   492  N  N   . HIS A 1 64  ? -0.533  -2.235  6.240   1.00 16.91 ? 64  HIS A N   1 
ATOM   493  C  CA  . HIS A 1 64  ? -0.615  -2.969  7.530   1.00 17.40 ? 64  HIS A CA  1 
ATOM   494  C  C   . HIS A 1 64  ? -2.003  -3.571  7.738   1.00 17.02 ? 64  HIS A C   1 
ATOM   495  O  O   . HIS A 1 64  ? -2.154  -4.606  8.422   1.00 17.88 ? 64  HIS A O   1 
ATOM   496  C  CB  . HIS A 1 64  ? -0.296  -2.058  8.714   1.00 18.02 ? 64  HIS A CB  1 
ATOM   497  C  CG  . HIS A 1 64  ? 0.928   -1.219  8.517   1.00 22.09 ? 64  HIS A CG  1 
ATOM   498  N  ND1 . HIS A 1 64  ? 2.208   -1.734  8.590   1.00 25.42 ? 64  HIS A ND1 1 
ATOM   499  C  CD2 . HIS A 1 64  ? 1.067   0.101   8.253   1.00 23.84 ? 64  HIS A CD2 1 
ATOM   500  C  CE1 . HIS A 1 64  ? 3.085   -0.767  8.395   1.00 24.21 ? 64  HIS A CE1 1 
ATOM   501  N  NE2 . HIS A 1 64  ? 2.420   0.353   8.169   1.00 24.87 ? 64  HIS A NE2 1 
ATOM   502  N  N   . ALA A 1 65  ? -3.016  -2.907  7.180   1.00 15.63 ? 65  ALA A N   1 
ATOM   503  C  CA  . ALA A 1 65  ? -4.390  -3.370  7.201   1.00 15.08 ? 65  ALA A CA  1 
ATOM   504  C  C   . ALA A 1 65  ? -5.119  -2.623  6.087   1.00 14.42 ? 65  ALA A C   1 
ATOM   505  O  O   . ALA A 1 65  ? -4.468  -1.984  5.233   1.00 15.05 ? 65  ALA A O   1 
ATOM   506  C  CB  . ALA A 1 65  ? -5.057  -3.109  8.582   1.00 13.54 ? 65  ALA A CB  1 
ATOM   507  N  N   . PHE A 1 66  ? -6.444  -2.707  6.066   1.00 13.29 ? 66  PHE A N   1 
ATOM   508  C  CA  . PHE A 1 66  ? -7.225  -1.772  5.251   1.00 13.98 ? 66  PHE A CA  1 
ATOM   509  C  C   . PHE A 1 66  ? -8.120  -0.914  6.121   1.00 14.27 ? 66  PHE A C   1 
ATOM   510  O  O   . PHE A 1 66  ? -8.742  -1.399  7.084   1.00 13.59 ? 66  PHE A O   1 
ATOM   511  C  CB  . PHE A 1 66  ? -8.027  -2.474  4.134   1.00 13.80 ? 66  PHE A CB  1 
ATOM   512  C  CG  . PHE A 1 66  ? -9.090  -3.419  4.650   1.00 14.17 ? 66  PHE A CG  1 
ATOM   513  C  CD1 . PHE A 1 66  ? -10.383 -2.966  4.959   1.00 14.97 ? 66  PHE A CD1 1 
ATOM   514  C  CD2 . PHE A 1 66  ? -8.783  -4.778  4.827   1.00 15.55 ? 66  PHE A CD2 1 
ATOM   515  C  CE1 . PHE A 1 66  ? -11.345 -3.857  5.446   1.00 15.82 ? 66  PHE A CE1 1 
ATOM   516  C  CE2 . PHE A 1 66  ? -9.735  -5.660  5.328   1.00 14.54 ? 66  PHE A CE2 1 
ATOM   517  C  CZ  . PHE A 1 66  ? -10.999 -5.220  5.629   1.00 14.55 ? 66  PHE A CZ  1 
ATOM   518  N  N   . ASN A 1 67  ? -8.174  0.372   5.790   1.00 14.56 ? 67  ASN A N   1 
ATOM   519  C  CA  . ASN A 1 67  ? -9.014  1.302   6.505   1.00 15.47 ? 67  ASN A CA  1 
ATOM   520  C  C   . ASN A 1 67  ? -10.212 1.691   5.674   1.00 15.89 ? 67  ASN A C   1 
ATOM   521  O  O   . ASN A 1 67  ? -10.052 2.067   4.512   1.00 16.95 ? 67  ASN A O   1 
ATOM   522  C  CB  . ASN A 1 67  ? -8.248  2.598   6.841   1.00 15.87 ? 67  ASN A CB  1 
ATOM   523  C  CG  . ASN A 1 67  ? -7.167  2.392   7.875   1.00 16.95 ? 67  ASN A CG  1 
ATOM   524  O  OD1 . ASN A 1 67  ? -7.016  1.300   8.435   1.00 17.27 ? 67  ASN A OD1 1 
ATOM   525  N  ND2 . ASN A 1 67  ? -6.377  3.451   8.119   1.00 18.21 ? 67  ASN A ND2 1 
ATOM   526  N  N   . VAL A 1 68  ? -11.390 1.609   6.265   1.00 15.25 ? 68  VAL A N   1 
ATOM   527  C  CA  . VAL A 1 68  ? -12.573 2.266   5.705   1.00 16.12 ? 68  VAL A CA  1 
ATOM   528  C  C   . VAL A 1 68  ? -12.720 3.629   6.413   1.00 17.14 ? 68  VAL A C   1 
ATOM   529  O  O   . VAL A 1 68  ? -12.997 3.692   7.629   1.00 15.72 ? 68  VAL A O   1 
ATOM   530  C  CB  . VAL A 1 68  ? -13.834 1.389   5.843   1.00 15.79 ? 68  VAL A CB  1 
ATOM   531  C  CG1 . VAL A 1 68  ? -15.140 2.192   5.479   1.00 16.72 ? 68  VAL A CG1 1 
ATOM   532  C  CG2 . VAL A 1 68  ? -13.707 0.156   4.967   1.00 17.65 ? 68  VAL A CG2 1 
ATOM   533  N  N   . GLU A 1 69  ? -12.508 4.704   5.643   1.00 18.10 ? 69  GLU A N   1 
ATOM   534  C  CA  . GLU A 1 69  ? -12.491 6.083   6.149   1.00 18.46 ? 69  GLU A CA  1 
ATOM   535  C  C   . GLU A 1 69  ? -13.832 6.782   6.003   1.00 18.52 ? 69  GLU A C   1 
ATOM   536  O  O   . GLU A 1 69  ? -14.569 6.574   5.013   1.00 19.50 ? 69  GLU A O   1 
ATOM   537  C  CB  . GLU A 1 69  ? -11.470 6.898   5.386   1.00 19.67 ? 69  GLU A CB  1 
ATOM   538  C  CG  . GLU A 1 69  ? -10.098 6.285   5.352   1.00 20.42 ? 69  GLU A CG  1 
ATOM   539  C  CD  . GLU A 1 69  ? -9.315  6.713   4.136   1.00 24.59 ? 69  GLU A CD  1 
ATOM   540  O  OE1 . GLU A 1 69  ? -9.915  7.394   3.250   1.00 26.89 ? 69  GLU A OE1 1 
ATOM   541  O  OE2 . GLU A 1 69  ? -8.108  6.371   4.071   1.00 25.44 ? 69  GLU A OE2 1 
ATOM   542  N  N   . PHE A 1 70  ? -14.126 7.626   6.985   1.00 16.44 ? 70  PHE A N   1 
ATOM   543  C  CA  . PHE A 1 70  ? -15.399 8.335   7.065   1.00 15.96 ? 70  PHE A CA  1 
ATOM   544  C  C   . PHE A 1 70  ? -15.162 9.823   7.023   1.00 15.70 ? 70  PHE A C   1 
ATOM   545  O  O   . PHE A 1 70  ? -14.092 10.273  7.345   1.00 15.83 ? 70  PHE A O   1 
ATOM   546  C  CB  . PHE A 1 70  ? -16.137 7.957   8.351   1.00 15.30 ? 70  PHE A CB  1 
ATOM   547  C  CG  . PHE A 1 70  ? -16.726 6.590   8.294   1.00 14.55 ? 70  PHE A CG  1 
ATOM   548  C  CD1 . PHE A 1 70  ? -15.908 5.467   8.466   1.00 15.44 ? 70  PHE A CD1 1 
ATOM   549  C  CD2 . PHE A 1 70  ? -18.076 6.404   8.017   1.00 15.13 ? 70  PHE A CD2 1 
ATOM   550  C  CE1 . PHE A 1 70  ? -16.446 4.162   8.387   1.00 17.30 ? 70  PHE A CE1 1 
ATOM   551  C  CE2 . PHE A 1 70  ? -18.634 5.090   7.927   1.00 15.19 ? 70  PHE A CE2 1 
ATOM   552  C  CZ  . PHE A 1 70  ? -17.797 3.975   8.093   1.00 17.08 ? 70  PHE A CZ  1 
ATOM   553  N  N   . ASP A 1 71  ? -16.170 10.569  6.599   1.00 16.93 ? 71  ASP A N   1 
ATOM   554  C  CA  . ASP A 1 71  ? -16.112 12.019  6.693   1.00 17.51 ? 71  ASP A CA  1 
ATOM   555  C  C   . ASP A 1 71  ? -16.376 12.396  8.142   1.00 17.02 ? 71  ASP A C   1 
ATOM   556  O  O   . ASP A 1 71  ? -17.480 12.190  8.658   1.00 18.47 ? 71  ASP A O   1 
ATOM   557  C  CB  . ASP A 1 71  ? -17.175 12.630  5.790   1.00 18.29 ? 71  ASP A CB  1 
ATOM   558  C  CG  . ASP A 1 71  ? -17.437 14.099  6.114   1.00 19.95 ? 71  ASP A CG  1 
ATOM   559  O  OD1 . ASP A 1 71  ? -16.481 14.764  6.567   1.00 20.74 ? 71  ASP A OD1 1 
ATOM   560  O  OD2 . ASP A 1 71  ? -18.592 14.568  5.947   1.00 23.46 ? 71  ASP A OD2 1 
ATOM   561  N  N   . ASP A 1 72  ? -15.363 12.936  8.806   1.00 17.25 ? 72  ASP A N   1 
ATOM   562  C  CA  . ASP A 1 72  ? -15.459 13.264  10.224  1.00 17.76 ? 72  ASP A CA  1 
ATOM   563  C  C   . ASP A 1 72  ? -15.445 14.784  10.408  1.00 18.70 ? 72  ASP A C   1 
ATOM   564  O  O   . ASP A 1 72  ? -15.006 15.279  11.446  1.00 18.35 ? 72  ASP A O   1 
ATOM   565  C  CB  . ASP A 1 72  ? -14.302 12.605  11.013  1.00 18.16 ? 72  ASP A CB  1 
ATOM   566  C  CG  . ASP A 1 72  ? -12.912 13.104  10.587  1.00 19.18 ? 72  ASP A CG  1 
ATOM   567  O  OD1 . ASP A 1 72  ? -12.769 13.837  9.578   1.00 17.71 ? 72  ASP A OD1 1 
ATOM   568  O  OD2 . ASP A 1 72  ? -11.924 12.760  11.270  1.00 19.79 ? 72  ASP A OD2 1 
ATOM   569  N  N   . SER A 1 73  ? -15.913 15.509  9.392   1.00 18.86 ? 73  SER A N   1 
ATOM   570  C  CA  . SER A 1 73  ? -15.898 16.995  9.422   1.00 20.69 ? 73  SER A CA  1 
ATOM   571  C  C   . SER A 1 73  ? -17.193 17.568  10.008  1.00 21.53 ? 73  SER A C   1 
ATOM   572  O  O   . SER A 1 73  ? -17.354 18.790  10.138  1.00 20.98 ? 73  SER A O   1 
ATOM   573  C  CB  . SER A 1 73  ? -15.647 17.569  8.024   1.00 19.86 ? 73  SER A CB  1 
ATOM   574  O  OG  . SER A 1 73  ? -16.760 17.313  7.183   1.00 20.51 ? 73  SER A OG  1 
ATOM   575  N  N   . GLN A 1 74  ? -18.131 16.688  10.351  1.00 22.58 ? 74  GLN A N   1 
ATOM   576  C  CA  . GLN A 1 74  ? -19.314 17.091  11.100  1.00 24.37 ? 74  GLN A CA  1 
ATOM   577  C  C   . GLN A 1 74  ? -19.635 15.968  12.051  1.00 24.62 ? 74  GLN A C   1 
ATOM   578  O  O   . GLN A 1 74  ? -19.108 14.884  11.877  1.00 24.35 ? 74  GLN A O   1 
ATOM   579  C  CB  . GLN A 1 74  ? -20.511 17.256  10.170  1.00 24.38 ? 74  GLN A CB  1 
ATOM   580  C  CG  . GLN A 1 74  ? -20.501 18.462  9.285   1.00 27.31 ? 74  GLN A CG  1 
ATOM   581  C  CD  . GLN A 1 74  ? -21.716 18.471  8.384   1.00 30.21 ? 74  GLN A CD  1 
ATOM   582  O  OE1 . GLN A 1 74  ? -21.680 17.968  7.258   1.00 32.15 ? 74  GLN A OE1 1 
ATOM   583  N  NE2 . GLN A 1 74  ? -22.818 19.013  8.892   1.00 34.74 ? 74  GLN A NE2 1 
ATOM   584  N  N   . ASP A 1 75  ? -20.505 16.235  13.030  1.00 25.61 ? 75  ASP A N   1 
ATOM   585  C  CA  . ASP A 1 75  ? -21.004 15.219  13.960  1.00 26.88 ? 75  ASP A CA  1 
ATOM   586  C  C   . ASP A 1 75  ? -22.050 14.358  13.259  1.00 26.69 ? 75  ASP A C   1 
ATOM   587  O  O   . ASP A 1 75  ? -23.246 14.714  13.252  1.00 27.66 ? 75  ASP A O   1 
ATOM   588  C  CB  . ASP A 1 75  ? -21.629 15.859  15.211  1.00 28.02 ? 75  ASP A CB  1 
ATOM   589  C  CG  . ASP A 1 75  ? -20.616 16.092  16.343  1.00 30.20 ? 75  ASP A CG  1 
ATOM   590  O  OD1 . ASP A 1 75  ? -19.436 15.698  16.204  1.00 32.06 ? 75  ASP A OD1 1 
ATOM   591  O  OD2 . ASP A 1 75  ? -21.015 16.661  17.390  1.00 34.28 ? 75  ASP A OD2 1 
ATOM   592  N  N   . LYS A 1 76  ? -21.602 13.244  12.678  1.00 25.41 ? 76  LYS A N   1 
ATOM   593  C  CA  . LYS A 1 76  ? -22.460 12.355  11.851  1.00 25.34 ? 76  LYS A CA  1 
ATOM   594  C  C   . LYS A 1 76  ? -22.488 10.897  12.340  1.00 24.89 ? 76  LYS A C   1 
ATOM   595  O  O   . LYS A 1 76  ? -23.517 10.193  12.250  1.00 26.25 ? 76  LYS A O   1 
ATOM   596  C  CB  . LYS A 1 76  ? -21.960 12.336  10.404  1.00 24.86 ? 76  LYS A CB  1 
ATOM   597  C  CG  . LYS A 1 76  ? -22.453 13.455  9.495   1.00 26.60 ? 76  LYS A CG  1 
ATOM   598  C  CD  . LYS A 1 76  ? -21.657 13.380  8.195   1.00 29.94 ? 76  LYS A CD  1 
ATOM   599  C  CE  . LYS A 1 76  ? -22.135 14.351  7.126   1.00 29.49 ? 76  LYS A CE  1 
ATOM   600  N  NZ  . LYS A 1 76  ? -21.537 13.978  5.826   1.00 28.20 ? 76  LYS A NZ  1 
ATOM   601  N  N   . ALA A 1 77  ? -21.331 10.416  12.766  1.00 23.00 ? 77  ALA A N   1 
ATOM   602  C  CA  . ALA A 1 77  ? -21.204 9.051   13.289  1.00 20.98 ? 77  ALA A CA  1 
ATOM   603  C  C   . ALA A 1 77  ? -20.424 9.217   14.571  1.00 20.46 ? 77  ALA A C   1 
ATOM   604  O  O   . ALA A 1 77  ? -19.206 9.451   14.522  1.00 19.41 ? 77  ALA A O   1 
ATOM   605  C  CB  . ALA A 1 77  ? -20.430 8.192   12.316  1.00 21.09 ? 77  ALA A CB  1 
ATOM   606  N  N   . VAL A 1 78  ? -21.122 9.135   15.700  1.00 19.03 ? 78  VAL A N   1 
ATOM   607  C  CA  . VAL A 1 78  ? -20.496 9.424   16.999  1.00 19.54 ? 78  VAL A CA  1 
ATOM   608  C  C   . VAL A 1 78  ? -20.759 8.376   18.081  1.00 17.96 ? 78  VAL A C   1 
ATOM   609  O  O   . VAL A 1 78  ? -21.842 7.742   18.163  1.00 17.36 ? 78  VAL A O   1 
ATOM   610  C  CB  . VAL A 1 78  ? -20.844 10.852  17.550  1.00 20.19 ? 78  VAL A CB  1 
ATOM   611  C  CG1 . VAL A 1 78  ? -20.546 11.972  16.502  1.00 21.74 ? 78  VAL A CG1 1 
ATOM   612  C  CG2 . VAL A 1 78  ? -22.274 10.896  18.075  1.00 21.64 ? 78  VAL A CG2 1 
ATOM   613  N  N   . LEU A 1 79  ? -19.715 8.196   18.889  1.00 17.26 ? 79  LEU A N   1 
ATOM   614  C  CA  . LEU A 1 79  ? -19.730 7.386   20.073  1.00 18.16 ? 79  LEU A CA  1 
ATOM   615  C  C   . LEU A 1 79  ? -19.736 8.309   21.300  1.00 18.12 ? 79  LEU A C   1 
ATOM   616  O  O   . LEU A 1 79  ? -19.009 9.312   21.357  1.00 17.70 ? 79  LEU A O   1 
ATOM   617  C  CB  . LEU A 1 79  ? -18.481 6.490   20.069  1.00 17.75 ? 79  LEU A CB  1 
ATOM   618  C  CG  . LEU A 1 79  ? -18.424 5.341   21.058  1.00 18.60 ? 79  LEU A CG  1 
ATOM   619  C  CD1 . LEU A 1 79  ? -19.460 4.286   20.715  1.00 20.67 ? 79  LEU A CD1 1 
ATOM   620  C  CD2 . LEU A 1 79  ? -17.027 4.746   21.030  1.00 14.91 ? 79  LEU A CD2 1 
ATOM   621  N  N   . LYS A 1 80  ? -20.614 8.011   22.241  1.00 18.11 ? 80  LYS A N   1 
ATOM   622  C  CA  . LYS A 1 80  ? -20.624 8.693   23.536  1.00 19.08 ? 80  LYS A CA  1 
ATOM   623  C  C   . LYS A 1 80  ? -21.235 7.770   24.587  1.00 18.64 ? 80  LYS A C   1 
ATOM   624  O  O   . LYS A 1 80  ? -21.582 6.619   24.279  1.00 17.67 ? 80  LYS A O   1 
ATOM   625  C  CB  . LYS A 1 80  ? -21.356 10.034  23.448  1.00 20.38 ? 80  LYS A CB  1 
ATOM   626  C  CG  . LYS A 1 80  ? -22.847 9.879   23.201  1.00 22.77 ? 80  LYS A CG  1 
ATOM   627  C  CD  . LYS A 1 80  ? -23.567 11.221  23.236  1.00 28.17 ? 80  LYS A CD  1 
ATOM   628  C  CE  . LYS A 1 80  ? -23.688 11.792  21.844  1.00 30.69 ? 80  LYS A CE  1 
ATOM   629  N  NZ  . LYS A 1 80  ? -22.387 12.330  21.342  1.00 33.85 ? 80  LYS A NZ  1 
ATOM   630  N  N   . GLY A 1 81  ? -21.346 8.271   25.818  1.00 18.63 ? 81  GLY A N   1 
ATOM   631  C  CA  . GLY A 1 81  ? -21.894 7.495   26.906  1.00 18.95 ? 81  GLY A CA  1 
ATOM   632  C  C   . GLY A 1 81  ? -20.880 6.432   27.221  1.00 18.94 ? 81  GLY A C   1 
ATOM   633  O  O   . GLY A 1 81  ? -19.674 6.657   27.050  1.00 18.57 ? 81  GLY A O   1 
ATOM   634  N  N   . GLY A 1 82  ? -21.353 5.270   27.654  1.00 18.94 ? 82  GLY A N   1 
ATOM   635  C  CA  . GLY A 1 82  ? -20.439 4.225   28.128  1.00 19.26 ? 82  GLY A CA  1 
ATOM   636  C  C   . GLY A 1 82  ? -19.545 4.811   29.214  1.00 18.14 ? 82  GLY A C   1 
ATOM   637  O  O   . GLY A 1 82  ? -20.055 5.459   30.132  1.00 19.60 ? 82  GLY A O   1 
ATOM   638  N  N   . PRO A 1 83  ? -18.200 4.630   29.105  1.00 17.52 ? 83  PRO A N   1 
ATOM   639  C  CA  . PRO A 1 83  ? -17.262 5.236   30.050  1.00 17.15 ? 83  PRO A CA  1 
ATOM   640  C  C   . PRO A 1 83  ? -16.842 6.666   29.661  1.00 18.25 ? 83  PRO A C   1 
ATOM   641  O  O   . PRO A 1 83  ? -16.040 7.309   30.367  1.00 18.54 ? 83  PRO A O   1 
ATOM   642  C  CB  . PRO A 1 83  ? -16.038 4.323   29.931  1.00 18.76 ? 83  PRO A CB  1 
ATOM   643  C  CG  . PRO A 1 83  ? -16.041 3.953   28.475  1.00 16.32 ? 83  PRO A CG  1 
ATOM   644  C  CD  . PRO A 1 83  ? -17.490 3.828   28.069  1.00 15.60 ? 83  PRO A CD  1 
ATOM   645  N  N   . LEU A 1 84  ? -17.366 7.162   28.545  1.00 18.29 ? 84  LEU A N   1 
ATOM   646  C  CA  . LEU A 1 84  ? -16.802 8.357   27.950  1.00 18.92 ? 84  LEU A CA  1 
ATOM   647  C  C   . LEU A 1 84  ? -17.453 9.605   28.509  1.00 20.79 ? 84  LEU A C   1 
ATOM   648  O  O   . LEU A 1 84  ? -18.640 9.597   28.807  1.00 19.98 ? 84  LEU A O   1 
ATOM   649  C  CB  . LEU A 1 84  ? -16.966 8.335   26.437  1.00 19.05 ? 84  LEU A CB  1 
ATOM   650  C  CG  . LEU A 1 84  ? -16.416 7.079   25.756  1.00 17.45 ? 84  LEU A CG  1 
ATOM   651  C  CD1 . LEU A 1 84  ? -16.972 7.001   24.336  1.00 15.95 ? 84  LEU A CD1 1 
ATOM   652  C  CD2 . LEU A 1 84  ? -14.847 7.037   25.791  1.00 16.93 ? 84  LEU A CD2 1 
ATOM   653  N  N   . ASP A 1 85  ? -16.648 10.659  28.632  1.00 21.98 ? 85  ASP A N   1 
ATOM   654  C  CA  . ASP A 1 85  ? -17.156 12.005  28.790  1.00 24.87 ? 85  ASP A CA  1 
ATOM   655  C  C   . ASP A 1 85  ? -17.115 12.638  27.394  1.00 25.40 ? 85  ASP A C   1 
ATOM   656  O  O   . ASP A 1 85  ? -16.134 12.497  26.655  1.00 26.78 ? 85  ASP A O   1 
ATOM   657  C  CB  . ASP A 1 85  ? -16.287 12.789  29.787  1.00 25.44 ? 85  ASP A CB  1 
ATOM   658  C  CG  . ASP A 1 85  ? -16.376 12.248  31.207  1.00 29.82 ? 85  ASP A CG  1 
ATOM   659  O  OD1 . ASP A 1 85  ? -17.468 11.752  31.608  1.00 31.88 ? 85  ASP A OD1 1 
ATOM   660  O  OD2 . ASP A 1 85  ? -15.350 12.347  31.945  1.00 32.03 ? 85  ASP A OD2 1 
ATOM   661  N  N   . GLY A 1 86  ? -18.173 13.330  27.008  1.00 25.78 ? 86  GLY A N   1 
ATOM   662  C  CA  . GLY A 1 86  ? -18.174 13.990  25.721  1.00 24.68 ? 86  GLY A CA  1 
ATOM   663  C  C   . GLY A 1 86  ? -18.409 13.092  24.514  1.00 24.38 ? 86  GLY A C   1 
ATOM   664  O  O   . GLY A 1 86  ? -18.881 11.951  24.648  1.00 24.83 ? 86  GLY A O   1 
ATOM   665  N  N   . THR A 1 87  ? -18.027 13.609  23.346  1.00 22.25 ? 87  THR A N   1 
ATOM   666  C  CA  . THR A 1 87  ? -18.450 13.081  22.055  1.00 20.85 ? 87  THR A CA  1 
ATOM   667  C  C   . THR A 1 87  ? -17.240 12.720  21.218  1.00 19.16 ? 87  THR A C   1 
ATOM   668  O  O   . THR A 1 87  ? -16.317 13.515  21.094  1.00 17.48 ? 87  THR A O   1 
ATOM   669  C  CB  . THR A 1 87  ? -19.254 14.155  21.287  1.00 21.62 ? 87  THR A CB  1 
ATOM   670  O  OG1 . THR A 1 87  ? -20.505 14.363  21.969  1.00 24.19 ? 87  THR A OG1 1 
ATOM   671  C  CG2 . THR A 1 87  ? -19.526 13.723  19.817  1.00 22.59 ? 87  THR A CG2 1 
ATOM   672  N  N   . TYR A 1 88  ? -17.269 11.524  20.637  1.00 17.12 ? 88  TYR A N   1 
ATOM   673  C  CA  . TYR A 1 88  ? -16.136 11.025  19.862  1.00 15.67 ? 88  TYR A CA  1 
ATOM   674  C  C   . TYR A 1 88  ? -16.601 10.712  18.434  1.00 15.62 ? 88  TYR A C   1 
ATOM   675  O  O   . TYR A 1 88  ? -17.595 9.986   18.249  1.00 17.17 ? 88  TYR A O   1 
ATOM   676  C  CB  . TYR A 1 88  ? -15.558 9.774   20.529  1.00 14.34 ? 88  TYR A CB  1 
ATOM   677  C  CG  . TYR A 1 88  ? -14.792 10.002  21.843  1.00 13.58 ? 88  TYR A CG  1 
ATOM   678  C  CD1 . TYR A 1 88  ? -15.460 10.357  23.031  1.00 10.87 ? 88  TYR A CD1 1 
ATOM   679  C  CD2 . TYR A 1 88  ? -13.388 9.832   21.878  1.00 12.58 ? 88  TYR A CD2 1 
ATOM   680  C  CE1 . TYR A 1 88  ? -14.749 10.550  24.232  1.00 11.31 ? 88  TYR A CE1 1 
ATOM   681  C  CE2 . TYR A 1 88  ? -12.659 10.026  23.058  1.00 9.17  ? 88  TYR A CE2 1 
ATOM   682  C  CZ  . TYR A 1 88  ? -13.353 10.362  24.234  1.00 11.40 ? 88  TYR A CZ  1 
ATOM   683  O  OH  . TYR A 1 88  ? -12.681 10.536  25.399  1.00 12.86 ? 88  TYR A OH  1 
ATOM   684  N  N   . ARG A 1 89  ? -15.912 11.277  17.448  1.00 14.14 ? 89  ARG A N   1 
ATOM   685  C  CA  . ARG A 1 89  ? -16.310 11.143  16.044  1.00 13.71 ? 89  ARG A CA  1 
ATOM   686  C  C   . ARG A 1 89  ? -15.620 9.987   15.367  1.00 11.90 ? 89  ARG A C   1 
ATOM   687  O  O   . ARG A 1 89  ? -14.403 9.880   15.435  1.00 11.13 ? 89  ARG A O   1 
ATOM   688  C  CB  . ARG A 1 89  ? -15.961 12.393  15.243  1.00 16.16 ? 89  ARG A CB  1 
ATOM   689  C  CG  . ARG A 1 89  ? -17.002 13.451  15.291  1.00 19.80 ? 89  ARG A CG  1 
ATOM   690  C  CD  . ARG A 1 89  ? -16.717 14.505  14.262  1.00 23.28 ? 89  ARG A CD  1 
ATOM   691  N  NE  . ARG A 1 89  ? -17.393 15.749  14.614  1.00 26.28 ? 89  ARG A NE  1 
ATOM   692  C  CZ  . ARG A 1 89  ? -17.038 16.957  14.186  1.00 28.56 ? 89  ARG A CZ  1 
ATOM   693  N  NH1 . ARG A 1 89  ? -15.987 17.124  13.403  1.00 26.40 ? 89  ARG A NH1 1 
ATOM   694  N  NH2 . ARG A 1 89  ? -17.732 18.018  14.584  1.00 32.14 ? 89  ARG A NH2 1 
ATOM   695  N  N   . LEU A 1 90  ? -16.397 9.162   14.659  1.00 10.87 ? 90  LEU A N   1 
ATOM   696  C  CA  . LEU A 1 90  ? -15.829 8.073   13.841  1.00 10.62 ? 90  LEU A CA  1 
ATOM   697  C  C   . LEU A 1 90  ? -14.979 8.596   12.691  1.00 10.77 ? 90  LEU A C   1 
ATOM   698  O  O   . LEU A 1 90  ? -15.458 9.379   11.829  1.00 11.61 ? 90  LEU A O   1 
ATOM   699  C  CB  . LEU A 1 90  ? -16.963 7.206   13.255  1.00 11.04 ? 90  LEU A CB  1 
ATOM   700  C  CG  . LEU A 1 90  ? -16.506 6.068   12.342  1.00 10.20 ? 90  LEU A CG  1 
ATOM   701  C  CD1 . LEU A 1 90  ? -15.593 5.079   13.092  1.00 13.74 ? 90  LEU A CD1 1 
ATOM   702  C  CD2 . LEU A 1 90  ? -17.707 5.329   11.754  1.00 10.82 ? 90  LEU A CD2 1 
ATOM   703  N  N   . ILE A 1 91  ? -13.711 8.185   12.674  1.00 9.94  ? 91  ILE A N   1 
ATOM   704  C  CA  . ILE A 1 91  ? -12.823 8.525   11.564  1.00 11.17 ? 91  ILE A CA  1 
ATOM   705  C  C   . ILE A 1 91  ? -12.565 7.359   10.594  1.00 11.12 ? 91  ILE A C   1 
ATOM   706  O  O   . ILE A 1 91  ? -12.556 7.552   9.375   1.00 11.29 ? 91  ILE A O   1 
ATOM   707  C  CB  . ILE A 1 91  ? -11.499 9.197   12.051  1.00 10.47 ? 91  ILE A CB  1 
ATOM   708  C  CG1 . ILE A 1 91  ? -10.596 9.540   10.856  1.00 12.33 ? 91  ILE A CG1 1 
ATOM   709  C  CG2 . ILE A 1 91  ? -10.746 8.335   13.106  1.00 10.87 ? 91  ILE A CG2 1 
ATOM   710  C  CD1 . ILE A 1 91  ? -9.417  10.448  11.230  1.00 13.02 ? 91  ILE A CD1 1 
ATOM   711  N  N   . GLN A 1 92  ? -12.343 6.145   11.120  1.00 10.62 ? 92  GLN A N   1 
ATOM   712  C  CA  . GLN A 1 92  ? -12.090 5.001   10.247  1.00 10.13 ? 92  GLN A CA  1 
ATOM   713  C  C   . GLN A 1 92  ? -12.331 3.719   11.046  1.00 10.24 ? 92  GLN A C   1 
ATOM   714  O  O   . GLN A 1 92  ? -12.354 3.747   12.263  1.00 9.18  ? 92  GLN A O   1 
ATOM   715  C  CB  . GLN A 1 92  ? -10.630 4.996   9.729   1.00 10.64 ? 92  GLN A CB  1 
ATOM   716  C  CG  . GLN A 1 92  ? -9.559  5.149   10.847  1.00 11.20 ? 92  GLN A CG  1 
ATOM   717  C  CD  . GLN A 1 92  ? -8.833  3.835   11.193  1.00 12.98 ? 92  GLN A CD  1 
ATOM   718  O  OE1 . GLN A 1 92  ? -9.370  2.751   11.011  1.00 11.06 ? 92  GLN A OE1 1 
ATOM   719  N  NE2 . GLN A 1 92  ? -7.607  3.950   11.688  1.00 14.67 ? 92  GLN A NE2 1 
ATOM   720  N  N   . PHE A 1 93  ? -12.553 2.632   10.321  1.00 9.51  ? 93  PHE A N   1 
ATOM   721  C  CA  . PHE A 1 93  ? -12.402 1.309   10.899  1.00 10.17 ? 93  PHE A CA  1 
ATOM   722  C  C   . PHE A 1 93  ? -11.449 0.405   10.098  1.00 10.73 ? 93  PHE A C   1 
ATOM   723  O  O   . PHE A 1 93  ? -11.198 0.602   8.918   1.00 11.20 ? 93  PHE A O   1 
ATOM   724  C  CB  . PHE A 1 93  ? -13.768 0.654   11.199  1.00 9.47  ? 93  PHE A CB  1 
ATOM   725  C  CG  . PHE A 1 93  ? -14.510 0.194   9.967   1.00 11.03 ? 93  PHE A CG  1 
ATOM   726  C  CD1 . PHE A 1 93  ? -14.131 -0.971  9.282   1.00 12.37 ? 93  PHE A CD1 1 
ATOM   727  C  CD2 . PHE A 1 93  ? -15.602 0.926   9.506   1.00 10.49 ? 93  PHE A CD2 1 
ATOM   728  C  CE1 . PHE A 1 93  ? -14.819 -1.414  8.136   1.00 14.59 ? 93  PHE A CE1 1 
ATOM   729  C  CE2 . PHE A 1 93  ? -16.315 0.479   8.343   1.00 13.75 ? 93  PHE A CE2 1 
ATOM   730  C  CZ  . PHE A 1 93  ? -15.915 -0.668  7.662   1.00 11.92 ? 93  PHE A CZ  1 
ATOM   731  N  N   . HIS A 1 94  ? -10.915 -0.605  10.767  1.00 10.00 ? 94  HIS A N   1 
ATOM   732  C  CA  . HIS A 1 94  ? -10.013 -1.554  10.158  1.00 10.18 ? 94  HIS A CA  1 
ATOM   733  C  C   . HIS A 1 94  ? -10.150 -2.808  11.012  1.00 9.84  ? 94  HIS A C   1 
ATOM   734  O  O   . HIS A 1 94  ? -10.844 -2.800  12.056  1.00 10.09 ? 94  HIS A O   1 
ATOM   735  C  CB  . HIS A 1 94  ? -8.555  -1.047  10.186  1.00 10.96 ? 94  HIS A CB  1 
ATOM   736  C  CG  . HIS A 1 94  ? -8.066  -0.753  11.566  1.00 10.92 ? 94  HIS A CG  1 
ATOM   737  N  ND1 . HIS A 1 94  ? -8.240  0.476   12.176  1.00 11.45 ? 94  HIS A ND1 1 
ATOM   738  C  CD2 . HIS A 1 94  ? -7.489  -1.555  12.488  1.00 9.23  ? 94  HIS A CD2 1 
ATOM   739  C  CE1 . HIS A 1 94  ? -7.760  0.422   13.407  1.00 9.64  ? 94  HIS A CE1 1 
ATOM   740  N  NE2 . HIS A 1 94  ? -7.301  -0.800  13.625  1.00 10.94 ? 94  HIS A NE2 1 
ATOM   741  N  N   . PHE A 1 95  ? -9.461  -3.849  10.580  1.00 9.18  ? 95  PHE A N   1 
ATOM   742  C  CA  . PHE A 1 95  ? -9.483  -5.130  11.261  1.00 9.16  ? 95  PHE A CA  1 
ATOM   743  C  C   . PHE A 1 95  ? -8.024  -5.588  11.470  1.00 8.96  ? 95  PHE A C   1 
ATOM   744  O  O   . PHE A 1 95  ? -7.078  -5.104  10.823  1.00 9.49  ? 95  PHE A O   1 
ATOM   745  C  CB  . PHE A 1 95  ? -10.194 -6.199  10.413  1.00 8.89  ? 95  PHE A CB  1 
ATOM   746  C  CG  . PHE A 1 95  ? -11.646 -5.895  10.070  1.00 8.96  ? 95  PHE A CG  1 
ATOM   747  C  CD1 . PHE A 1 95  ? -11.963 -5.056  8.992   1.00 11.52 ? 95  PHE A CD1 1 
ATOM   748  C  CD2 . PHE A 1 95  ? -12.676 -6.503  10.786  1.00 11.45 ? 95  PHE A CD2 1 
ATOM   749  C  CE1 . PHE A 1 95  ? -13.298 -4.810  8.629   1.00 10.46 ? 95  PHE A CE1 1 
ATOM   750  C  CE2 . PHE A 1 95  ? -14.026 -6.283  10.451  1.00 11.07 ? 95  PHE A CE2 1 
ATOM   751  C  CZ  . PHE A 1 95  ? -14.335 -5.429  9.341   1.00 11.63 ? 95  PHE A CZ  1 
ATOM   752  N  N   . HIS A 1 96  ? -7.875  -6.575  12.344  1.00 8.52  ? 96  HIS A N   1 
ATOM   753  C  CA  . HIS A 1 96  ? -6.615  -7.315  12.557  1.00 8.84  ? 96  HIS A CA  1 
ATOM   754  C  C   . HIS A 1 96  ? -7.018  -8.755  12.436  1.00 8.57  ? 96  HIS A C   1 
ATOM   755  O  O   . HIS A 1 96  ? -8.052  -9.108  12.957  1.00 8.91  ? 96  HIS A O   1 
ATOM   756  C  CB  . HIS A 1 96  ? -6.061  -7.067  13.955  1.00 9.36  ? 96  HIS A CB  1 
ATOM   757  C  CG  . HIS A 1 96  ? -5.749  -5.628  14.222  1.00 8.91  ? 96  HIS A CG  1 
ATOM   758  N  ND1 . HIS A 1 96  ? -4.498  -5.093  14.010  1.00 9.82  ? 96  HIS A ND1 1 
ATOM   759  C  CD2 . HIS A 1 96  ? -6.535  -4.603  14.630  1.00 11.24 ? 96  HIS A CD2 1 
ATOM   760  C  CE1 . HIS A 1 96  ? -4.510  -3.808  14.333  1.00 11.32 ? 96  HIS A CE1 1 
ATOM   761  N  NE2 . HIS A 1 96  ? -5.746  -3.480  14.678  1.00 11.04 ? 96  HIS A NE2 1 
ATOM   762  N  N   . TRP A 1 97  ? -6.249  -9.581  11.732  1.00 8.53  ? 97  TRP A N   1 
ATOM   763  C  CA  . TRP A 1 97  ? -6.674  -10.984 11.573  1.00 9.88  ? 97  TRP A CA  1 
ATOM   764  C  C   . TRP A 1 97  ? -5.512  -11.911 11.427  1.00 9.95  ? 97  TRP A C   1 
ATOM   765  O  O   . TRP A 1 97  ? -4.360  -11.460 11.241  1.00 11.09 ? 97  TRP A O   1 
ATOM   766  C  CB  . TRP A 1 97  ? -7.602  -11.160 10.366  1.00 10.08 ? 97  TRP A CB  1 
ATOM   767  C  CG  . TRP A 1 97  ? -6.973  -10.750 9.056   1.00 10.56 ? 97  TRP A CG  1 
ATOM   768  C  CD1 . TRP A 1 97  ? -6.307  -11.556 8.175   1.00 12.33 ? 97  TRP A CD1 1 
ATOM   769  C  CD2 . TRP A 1 97  ? -6.944  -9.427  8.499   1.00 12.35 ? 97  TRP A CD2 1 
ATOM   770  N  NE1 . TRP A 1 97  ? -5.867  -10.812 7.081   1.00 13.76 ? 97  TRP A NE1 1 
ATOM   771  C  CE2 . TRP A 1 97  ? -6.250  -9.506  7.257   1.00 13.97 ? 97  TRP A CE2 1 
ATOM   772  C  CE3 . TRP A 1 97  ? -7.453  -8.183  8.917   1.00 10.42 ? 97  TRP A CE3 1 
ATOM   773  C  CZ2 . TRP A 1 97  ? -6.044  -8.384  6.440   1.00 13.66 ? 97  TRP A CZ2 1 
ATOM   774  C  CZ3 . TRP A 1 97  ? -7.232  -7.041  8.084   1.00 12.41 ? 97  TRP A CZ3 1 
ATOM   775  C  CH2 . TRP A 1 97  ? -6.537  -7.164  6.874   1.00 11.21 ? 97  TRP A CH2 1 
ATOM   776  N  N   . GLY A 1 98  ? -5.837  -13.207 11.439  1.00 9.46  ? 98  GLY A N   1 
ATOM   777  C  CA  . GLY A 1 98  ? -4.812  -14.253 11.481  1.00 10.57 ? 98  GLY A CA  1 
ATOM   778  C  C   . GLY A 1 98  ? -4.550  -14.933 10.156  1.00 11.16 ? 98  GLY A C   1 
ATOM   779  O  O   . GLY A 1 98  ? -5.216  -14.669 9.149   1.00 11.37 ? 98  GLY A O   1 
ATOM   780  N  N   . SER A 1 99  ? -3.527  -15.776 10.151  1.00 12.44 ? 99  SER A N   1 
ATOM   781  C  CA  . SER A 1 99  ? -3.253  -16.671 9.025   1.00 13.96 ? 99  SER A CA  1 
ATOM   782  C  C   . SER A 1 99  ? -4.142  -17.929 9.121   1.00 14.20 ? 99  SER A C   1 
ATOM   783  O  O   . SER A 1 99  ? -4.271  -18.705 8.154   1.00 16.24 ? 99  SER A O   1 
ATOM   784  C  CB  . SER A 1 99  ? -1.772  -17.056 9.035   1.00 12.98 ? 99  SER A CB  1 
ATOM   785  O  OG  . SER A 1 99  ? -1.388  -17.629 10.280  1.00 13.15 ? 99  SER A OG  1 
ATOM   786  N  N   . LEU A 1 100 ? -4.725  -18.125 10.304  1.00 14.92 ? 100 LEU A N   1 
ATOM   787  C  CA  . LEU A 1 100 ? -5.535  -19.289 10.677  1.00 16.22 ? 100 LEU A CA  1 
ATOM   788  C  C   . LEU A 1 100 ? -6.706  -18.780 11.513  1.00 15.41 ? 100 LEU A C   1 
ATOM   789  O  O   . LEU A 1 100 ? -6.578  -17.751 12.187  1.00 15.06 ? 100 LEU A O   1 
ATOM   790  C  CB  . LEU A 1 100 ? -4.710  -20.247 11.551  1.00 16.99 ? 100 LEU A CB  1 
ATOM   791  C  CG  . LEU A 1 100 ? -3.385  -20.723 10.953  1.00 19.89 ? 100 LEU A CG  1 
ATOM   792  C  CD1 . LEU A 1 100 ? -2.421  -21.173 12.037  1.00 23.87 ? 100 LEU A CD1 1 
ATOM   793  C  CD2 . LEU A 1 100 ? -3.631  -21.834 9.940   1.00 23.64 ? 100 LEU A CD2 1 
ATOM   794  N  N   . ASP A 1 101 ? -7.816  -19.528 11.534  1.00 14.43 ? 101 ASP A N   1 
ATOM   795  C  CA  . ASP A 1 101 ? -8.969  -19.083 12.334  1.00 14.24 ? 101 ASP A CA  1 
ATOM   796  C  C   . ASP A 1 101 ? -8.654  -19.021 13.830  1.00 14.17 ? 101 ASP A C   1 
ATOM   797  O  O   . ASP A 1 101 ? -9.298  -18.288 14.572  1.00 14.57 ? 101 ASP A O   1 
ATOM   798  C  CB  . ASP A 1 101 ? -10.211 -19.954 12.097  1.00 14.48 ? 101 ASP A CB  1 
ATOM   799  C  CG  . ASP A 1 101 ? -10.674 -19.986 10.646  1.00 17.14 ? 101 ASP A CG  1 
ATOM   800  O  OD1 . ASP A 1 101 ? -10.281 -19.151 9.808   1.00 14.59 ? 101 ASP A OD1 1 
ATOM   801  O  OD2 . ASP A 1 101 ? -11.479 -20.900 10.353  1.00 21.89 ? 101 ASP A OD2 1 
ATOM   802  N  N   . GLY A 1 102 ? -7.643  -19.778 14.279  1.00 13.31 ? 102 GLY A N   1 
ATOM   803  C  CA  . GLY A 1 102 ? -7.299  -19.829 15.703  1.00 12.93 ? 102 GLY A CA  1 
ATOM   804  C  C   . GLY A 1 102 ? -6.574  -18.612 16.289  1.00 11.47 ? 102 GLY A C   1 
ATOM   805  O  O   . GLY A 1 102 ? -6.248  -18.589 17.471  1.00 11.84 ? 102 GLY A O   1 
ATOM   806  N  N   . GLN A 1 103 ? -6.301  -17.596 15.476  1.00 11.27 ? 103 GLN A N   1 
ATOM   807  C  CA  . GLN A 1 103 ? -5.604  -16.410 15.975  1.00 11.14 ? 103 GLN A CA  1 
ATOM   808  C  C   . GLN A 1 103 ? -5.944  -15.242 15.072  1.00 10.74 ? 103 GLN A C   1 
ATOM   809  O  O   . GLN A 1 103 ? -6.503  -15.440 14.001  1.00 10.67 ? 103 GLN A O   1 
ATOM   810  C  CB  . GLN A 1 103 ? -4.087  -16.639 16.000  1.00 11.67 ? 103 GLN A CB  1 
ATOM   811  C  CG  . GLN A 1 103 ? -3.471  -16.865 14.606  1.00 12.99 ? 103 GLN A CG  1 
ATOM   812  C  CD  . GLN A 1 103 ? -2.041  -17.330 14.724  1.00 16.69 ? 103 GLN A CD  1 
ATOM   813  O  OE1 . GLN A 1 103 ? -1.687  -18.020 15.689  1.00 21.45 ? 103 GLN A OE1 1 
ATOM   814  N  NE2 . GLN A 1 103 ? -1.212  -16.974 13.745  1.00 12.92 ? 103 GLN A NE2 1 
ATOM   815  N  N   . GLY A 1 104 ? -5.621  -14.029 15.500  1.00 10.89 ? 104 GLY A N   1 
ATOM   816  C  CA  . GLY A 1 104 ? -6.019  -12.847 14.730  1.00 10.06 ? 104 GLY A CA  1 
ATOM   817  C  C   . GLY A 1 104 ? -6.390  -11.653 15.604  1.00 9.64  ? 104 GLY A C   1 
ATOM   818  O  O   . GLY A 1 104 ? -6.077  -10.483 15.270  1.00 9.45  ? 104 GLY A O   1 
ATOM   819  N  N   . SER A 1 105 ? -7.092  -11.926 16.710  1.00 9.52  ? 105 SER A N   1 
ATOM   820  C  CA  . SER A 1 105 ? -7.526  -10.818 17.569  1.00 9.24  ? 105 SER A CA  1 
ATOM   821  C  C   . SER A 1 105 ? -6.327  -10.285 18.350  1.00 8.77  ? 105 SER A C   1 
ATOM   822  O  O   . SER A 1 105 ? -5.310  -10.981 18.560  1.00 9.49  ? 105 SER A O   1 
ATOM   823  C  CB  . SER A 1 105 ? -8.655  -11.217 18.511  1.00 8.44  ? 105 SER A CB  1 
ATOM   824  O  OG  . SER A 1 105 ? -8.189  -12.123 19.502  1.00 9.87  ? 105 SER A OG  1 
ATOM   825  N  N   . GLU A 1 106 ? -6.454  -9.027  18.737  1.00 8.54  ? 106 GLU A N   1 
ATOM   826  C  CA  . GLU A 1 106 ? -5.423  -8.344  19.518  1.00 8.54  ? 106 GLU A CA  1 
ATOM   827  C  C   . GLU A 1 106 ? -5.759  -8.521  20.992  1.00 8.42  ? 106 GLU A C   1 
ATOM   828  O  O   . GLU A 1 106 ? -4.992  -9.129  21.760  1.00 7.26  ? 106 GLU A O   1 
ATOM   829  C  CB  . GLU A 1 106 ? -5.354  -6.855  19.099  1.00 7.06  ? 106 GLU A CB  1 
ATOM   830  C  CG  . GLU A 1 106 ? -4.913  -6.719  17.628  1.00 9.33  ? 106 GLU A CG  1 
ATOM   831  C  CD  . GLU A 1 106 ? -4.273  -5.421  17.332  1.00 10.98 ? 106 GLU A CD  1 
ATOM   832  O  OE1 . GLU A 1 106 ? -4.903  -4.365  17.590  1.00 9.24  ? 106 GLU A OE1 1 
ATOM   833  O  OE2 . GLU A 1 106 ? -3.113  -5.456  16.868  1.00 11.98 ? 106 GLU A OE2 1 
ATOM   834  N  N   . HIS A 1 107 ? -6.939  -8.051  21.408  1.00 8.17  ? 107 HIS A N   1 
ATOM   835  C  CA  . HIS A 1 107 ? -7.401  -8.425  22.720  1.00 8.23  ? 107 HIS A CA  1 
ATOM   836  C  C   . HIS A 1 107 ? -7.704  -9.897  22.766  1.00 9.31  ? 107 HIS A C   1 
ATOM   837  O  O   . HIS A 1 107 ? -8.044  -10.508 21.734  1.00 9.34  ? 107 HIS A O   1 
ATOM   838  C  CB  . HIS A 1 107 ? -8.636  -7.621  23.100  1.00 8.98  ? 107 HIS A CB  1 
ATOM   839  C  CG  . HIS A 1 107 ? -8.333  -6.177  23.264  1.00 7.71  ? 107 HIS A CG  1 
ATOM   840  N  ND1 . HIS A 1 107 ? -8.338  -5.299  22.204  1.00 8.52  ? 107 HIS A ND1 1 
ATOM   841  C  CD2 . HIS A 1 107 ? -7.905  -5.475  24.339  1.00 9.09  ? 107 HIS A CD2 1 
ATOM   842  C  CE1 . HIS A 1 107 ? -7.969  -4.099  22.628  1.00 10.02 ? 107 HIS A CE1 1 
ATOM   843  N  NE2 . HIS A 1 107 ? -7.694  -4.184  23.920  1.00 9.49  ? 107 HIS A NE2 1 
ATOM   844  N  N   . THR A 1 108 ? -7.474  -10.475 23.932  1.00 9.37  ? 108 THR A N   1 
ATOM   845  C  CA  . THR A 1 108 ? -7.899  -11.855 24.197  1.00 9.78  ? 108 THR A CA  1 
ATOM   846  C  C   . THR A 1 108 ? -8.873  -11.895 25.391  1.00 10.47 ? 108 THR A C   1 
ATOM   847  O  O   . THR A 1 108 ? -8.911  -10.975 26.221  1.00 10.51 ? 108 THR A O   1 
ATOM   848  C  CB  . THR A 1 108 ? -6.706  -12.778 24.431  1.00 9.56  ? 108 THR A CB  1 
ATOM   849  O  OG1 . THR A 1 108 ? -5.868  -12.243 25.454  1.00 10.01 ? 108 THR A OG1 1 
ATOM   850  C  CG2 . THR A 1 108 ? -5.854  -12.909 23.123  1.00 8.91  ? 108 THR A CG2 1 
ATOM   851  N  N   . VAL A 1 109 ? -9.657  -12.964 25.491  1.00 10.87 ? 109 VAL A N   1 
ATOM   852  C  CA  . VAL A 1 109 ? -10.638 -13.062 26.602  1.00 11.46 ? 109 VAL A CA  1 
ATOM   853  C  C   . VAL A 1 109 ? -10.342 -14.362 27.359  1.00 12.05 ? 109 VAL A C   1 
ATOM   854  O  O   . VAL A 1 109 ? -10.507 -15.450 26.810  1.00 11.30 ? 109 VAL A O   1 
ATOM   855  C  CB  . VAL A 1 109 ? -12.074 -13.044 26.057  1.00 12.26 ? 109 VAL A CB  1 
ATOM   856  C  CG1 . VAL A 1 109 ? -13.127 -13.200 27.183  1.00 12.47 ? 109 VAL A CG1 1 
ATOM   857  C  CG2 . VAL A 1 109 ? -12.318 -11.739 25.237  1.00 11.82 ? 109 VAL A CG2 1 
ATOM   858  N  N   . ASP A 1 110 ? -9.850  -14.231 28.581  1.00 11.97 ? 110 ASP A N   1 
ATOM   859  C  CA  . ASP A 1 110 ? -9.308  -15.390 29.322  1.00 13.26 ? 110 ASP A CA  1 
ATOM   860  C  C   . ASP A 1 110 ? -8.368  -16.225 28.433  1.00 12.72 ? 110 ASP A C   1 
ATOM   861  O  O   . ASP A 1 110 ? -8.492  -17.471 28.359  1.00 12.33 ? 110 ASP A O   1 
ATOM   862  C  CB  . ASP A 1 110 ? -10.457 -16.237 29.879  1.00 13.74 ? 110 ASP A CB  1 
ATOM   863  C  CG  . ASP A 1 110 ? -11.339 -15.455 30.844  1.00 14.13 ? 110 ASP A CG  1 
ATOM   864  O  OD1 . ASP A 1 110 ? -10.801 -14.585 31.554  1.00 17.14 ? 110 ASP A OD1 1 
ATOM   865  O  OD2 . ASP A 1 110 ? -12.539 -15.741 30.891  1.00 18.53 ? 110 ASP A OD2 1 
ATOM   866  N  N   . LYS A 1 111 ? -7.445  -15.519 27.759  1.00 12.36 ? 111 LYS A N   1 
ATOM   867  C  CA  . LYS A 1 111 ? -6.431  -16.077 26.830  1.00 12.84 ? 111 LYS A CA  1 
ATOM   868  C  C   . LYS A 1 111 ? -6.987  -16.578 25.500  1.00 11.95 ? 111 LYS A C   1 
ATOM   869  O  O   . LYS A 1 111 ? -6.237  -16.989 24.638  1.00 12.41 ? 111 LYS A O   1 
ATOM   870  C  CB  . LYS A 1 111 ? -5.557  -17.121 27.530  1.00 13.76 ? 111 LYS A CB  1 
ATOM   871  C  CG  . LYS A 1 111 ? -4.967  -16.589 28.829  1.00 16.45 ? 111 LYS A CG  1 
ATOM   872  C  CD  . LYS A 1 111 ? -3.868  -15.628 28.533  1.00 20.69 ? 111 LYS A CD  1 
ATOM   873  C  CE  . LYS A 1 111 ? -3.230  -15.147 29.824  1.00 23.27 ? 111 LYS A CE  1 
ATOM   874  N  NZ  . LYS A 1 111 ? -1.781  -15.305 29.705  1.00 24.22 ? 111 LYS A NZ  1 
ATOM   875  N  N   . LYS A 1 112 ? -8.302  -16.492 25.315  1.00 10.79 ? 112 LYS A N   1 
ATOM   876  C  CA  . LYS A 1 112 ? -8.890  -16.889 24.044  1.00 12.26 ? 112 LYS A CA  1 
ATOM   877  C  C   . LYS A 1 112 ? -8.613  -15.833 22.942  1.00 12.05 ? 112 LYS A C   1 
ATOM   878  O  O   . LYS A 1 112 ? -8.886  -14.622 23.120  1.00 11.61 ? 112 LYS A O   1 
ATOM   879  C  CB  . LYS A 1 112 ? -10.389 -17.126 24.185  1.00 12.24 ? 112 LYS A CB  1 
ATOM   880  C  CG  . LYS A 1 112 ? -11.073 -17.449 22.838  1.00 14.42 ? 112 LYS A CG  1 
ATOM   881  C  CD  . LYS A 1 112 ? -12.586 -17.264 22.984  1.00 18.42 ? 112 LYS A CD  1 
ATOM   882  C  CE  . LYS A 1 112 ? -13.261 -17.375 21.614  1.00 22.18 ? 112 LYS A CE  1 
ATOM   883  N  NZ  . LYS A 1 112 ? -13.188 -18.747 21.069  1.00 21.16 ? 112 LYS A NZ  1 
ATOM   884  N  N   . LYS A 1 113 ? -8.065  -16.319 21.825  1.00 11.62 ? 113 LYS A N   1 
ATOM   885  C  CA  . LYS A 1 113 ? -7.860  -15.506 20.605  1.00 11.60 ? 113 LYS A CA  1 
ATOM   886  C  C   . LYS A 1 113 ? -9.001  -15.752 19.633  1.00 11.15 ? 113 LYS A C   1 
ATOM   887  O  O   . LYS A 1 113 ? -9.386  -16.905 19.378  1.00 10.75 ? 113 LYS A O   1 
ATOM   888  C  CB  . LYS A 1 113 ? -6.548  -15.902 19.914  1.00 11.86 ? 113 LYS A CB  1 
ATOM   889  C  CG  . LYS A 1 113 ? -5.295  -15.576 20.702  1.00 12.04 ? 113 LYS A CG  1 
ATOM   890  C  CD  . LYS A 1 113 ? -4.113  -16.215 20.009  1.00 13.91 ? 113 LYS A CD  1 
ATOM   891  C  CE  . LYS A 1 113 ? -2.795  -15.664 20.539  1.00 16.98 ? 113 LYS A CE  1 
ATOM   892  N  NZ  . LYS A 1 113 ? -2.308  -16.434 21.691  1.00 20.75 ? 113 LYS A NZ  1 
ATOM   893  N  N   . TYR A 1 114 ? -9.579  -14.675 19.115  1.00 10.34 ? 114 TYR A N   1 
ATOM   894  C  CA  . TYR A 1 114 ? -10.588 -14.781 18.079  1.00 9.90  ? 114 TYR A CA  1 
ATOM   895  C  C   . TYR A 1 114 ? -9.932  -14.711 16.696  1.00 9.71  ? 114 TYR A C   1 
ATOM   896  O  O   . TYR A 1 114 ? -8.750  -14.367 16.600  1.00 10.33 ? 114 TYR A O   1 
ATOM   897  C  CB  . TYR A 1 114 ? -11.624 -13.666 18.249  1.00 10.11 ? 114 TYR A CB  1 
ATOM   898  C  CG  . TYR A 1 114 ? -12.588 -13.883 19.402  1.00 11.11 ? 114 TYR A CG  1 
ATOM   899  C  CD1 . TYR A 1 114 ? -12.288 -13.451 20.700  1.00 11.47 ? 114 TYR A CD1 1 
ATOM   900  C  CD2 . TYR A 1 114 ? -13.820 -14.515 19.185  1.00 13.44 ? 114 TYR A CD2 1 
ATOM   901  C  CE1 . TYR A 1 114 ? -13.185 -13.660 21.772  1.00 13.62 ? 114 TYR A CE1 1 
ATOM   902  C  CE2 . TYR A 1 114 ? -14.726 -14.684 20.218  1.00 13.52 ? 114 TYR A CE2 1 
ATOM   903  C  CZ  . TYR A 1 114 ? -14.403 -14.275 21.508  1.00 13.95 ? 114 TYR A CZ  1 
ATOM   904  O  OH  . TYR A 1 114 ? -15.322 -14.469 22.527  1.00 16.34 ? 114 TYR A OH  1 
ATOM   905  N  N   . ALA A 1 115 ? -10.689 -15.033 15.633  1.00 9.79  ? 115 ALA A N   1 
ATOM   906  C  CA  . ALA A 1 115 ? -10.149 -15.076 14.265  1.00 10.21 ? 115 ALA A CA  1 
ATOM   907  C  C   . ALA A 1 115 ? -9.745  -13.687 13.763  1.00 9.66  ? 115 ALA A C   1 
ATOM   908  O  O   . ALA A 1 115 ? -8.876  -13.531 12.893  1.00 10.04 ? 115 ALA A O   1 
ATOM   909  C  CB  . ALA A 1 115 ? -11.188 -15.720 13.319  1.00 10.85 ? 115 ALA A CB  1 
ATOM   910  N  N   . ALA A 1 116 ? -10.418 -12.662 14.290  1.00 10.09 ? 116 ALA A N   1 
ATOM   911  C  CA  . ALA A 1 116 ? -10.086 -11.299 13.916  1.00 9.16  ? 116 ALA A CA  1 
ATOM   912  C  C   . ALA A 1 116 ? -10.644 -10.321 14.929  1.00 8.27  ? 116 ALA A C   1 
ATOM   913  O  O   . ALA A 1 116 ? -11.404 -10.703 15.851  1.00 8.22  ? 116 ALA A O   1 
ATOM   914  C  CB  . ALA A 1 116 ? -10.611 -10.971 12.491  1.00 8.59  ? 116 ALA A CB  1 
ATOM   915  N  N   . GLU A 1 117 ? -10.298 -9.050  14.749  1.00 7.56  ? 117 GLU A N   1 
ATOM   916  C  CA  . GLU A 1 117 ? -10.860 -8.008  15.610  1.00 7.92  ? 117 GLU A CA  1 
ATOM   917  C  C   . GLU A 1 117 ? -11.046 -6.737  14.796  1.00 8.48  ? 117 GLU A C   1 
ATOM   918  O  O   . GLU A 1 117 ? -10.143 -6.291  14.124  1.00 9.68  ? 117 GLU A O   1 
ATOM   919  C  CB  . GLU A 1 117 ? -9.943  -7.767  16.827  1.00 7.64  ? 117 GLU A CB  1 
ATOM   920  C  CG  . GLU A 1 117 ? -10.422 -6.734  17.858  1.00 6.65  ? 117 GLU A CG  1 
ATOM   921  C  CD  . GLU A 1 117 ? -9.523  -6.714  19.090  1.00 9.19  ? 117 GLU A CD  1 
ATOM   922  O  OE1 . GLU A 1 117 ? -8.881  -7.769  19.412  1.00 10.88 ? 117 GLU A OE1 1 
ATOM   923  O  OE2 . GLU A 1 117 ? -9.502  -5.649  19.771  1.00 11.20 ? 117 GLU A OE2 1 
ATOM   924  N  N   . LEU A 1 118 ? -12.253 -6.211  14.869  1.00 8.91  ? 118 LEU A N   1 
ATOM   925  C  CA  . LEU A 1 118 ? -12.620 -4.931  14.287  1.00 8.29  ? 118 LEU A CA  1 
ATOM   926  C  C   . LEU A 1 118 ? -12.386 -3.759  15.274  1.00 7.82  ? 118 LEU A C   1 
ATOM   927  O  O   . LEU A 1 118 ? -12.807 -3.799  16.438  1.00 8.37  ? 118 LEU A O   1 
ATOM   928  C  CB  . LEU A 1 118 ? -14.102 -4.980  13.889  1.00 7.66  ? 118 LEU A CB  1 
ATOM   929  C  CG  . LEU A 1 118 ? -14.836 -3.692  13.484  1.00 8.81  ? 118 LEU A CG  1 
ATOM   930  C  CD1 . LEU A 1 118 ? -14.300 -3.161  12.183  1.00 11.02 ? 118 LEU A CD1 1 
ATOM   931  C  CD2 . LEU A 1 118 ? -16.332 -4.041  13.340  1.00 9.22  ? 118 LEU A CD2 1 
ATOM   932  N  N   . HIS A 1 119 ? -11.782 -2.689  14.751  1.00 7.51  ? 119 HIS A N   1 
ATOM   933  C  CA  . HIS A 1 119 ? -11.542 -1.486  15.512  1.00 7.10  ? 119 HIS A CA  1 
ATOM   934  C  C   . HIS A 1 119 ? -12.250 -0.320  14.833  1.00 7.30  ? 119 HIS A C   1 
ATOM   935  O  O   . HIS A 1 119 ? -11.902 0.025   13.705  1.00 8.75  ? 119 HIS A O   1 
ATOM   936  C  CB  . HIS A 1 119 ? -10.028 -1.252  15.625  1.00 7.70  ? 119 HIS A CB  1 
ATOM   937  C  CG  . HIS A 1 119 ? -9.375  -2.208  16.576  1.00 6.55  ? 119 HIS A CG  1 
ATOM   938  N  ND1 . HIS A 1 119 ? -8.028  -2.489  16.555  1.00 8.62  ? 119 HIS A ND1 1 
ATOM   939  C  CD2 . HIS A 1 119 ? -9.907  -2.977  17.555  1.00 6.44  ? 119 HIS A CD2 1 
ATOM   940  C  CE1 . HIS A 1 119 ? -7.751  -3.381  17.491  1.00 6.43  ? 119 HIS A CE1 1 
ATOM   941  N  NE2 . HIS A 1 119 ? -8.875  -3.701  18.107  1.00 7.76  ? 119 HIS A NE2 1 
ATOM   942  N  N   . LEU A 1 120 ? -13.251 0.234   15.498  1.00 7.01  ? 120 LEU A N   1 
ATOM   943  C  CA  . LEU A 1 120 ? -13.924 1.466   15.032  1.00 9.00  ? 120 LEU A CA  1 
ATOM   944  C  C   . LEU A 1 120 ? -13.299 2.625   15.795  1.00 8.98  ? 120 LEU A C   1 
ATOM   945  O  O   . LEU A 1 120 ? -13.456 2.731   17.017  1.00 9.67  ? 120 LEU A O   1 
ATOM   946  C  CB  . LEU A 1 120 ? -15.411 1.391   15.272  1.00 9.69  ? 120 LEU A CB  1 
ATOM   947  C  CG  . LEU A 1 120 ? -16.047 0.322   14.333  1.00 11.51 ? 120 LEU A CG  1 
ATOM   948  C  CD1 . LEU A 1 120 ? -16.814 -0.713  15.095  1.00 14.41 ? 120 LEU A CD1 1 
ATOM   949  C  CD2 . LEU A 1 120 ? -16.886 0.986   13.208  1.00 13.13 ? 120 LEU A CD2 1 
ATOM   950  N  N   . VAL A 1 121 ? -12.547 3.433   15.066  1.00 9.77  ? 121 VAL A N   1 
ATOM   951  C  CA  . VAL A 1 121 ? -11.682 4.450   15.701  1.00 9.75  ? 121 VAL A CA  1 
ATOM   952  C  C   . VAL A 1 121 ? -12.370 5.801   15.751  1.00 9.85  ? 121 VAL A C   1 
ATOM   953  O  O   . VAL A 1 121 ? -12.794 6.323   14.707  1.00 9.38  ? 121 VAL A O   1 
ATOM   954  C  CB  . VAL A 1 121 ? -10.317 4.565   14.959  1.00 10.57 ? 121 VAL A CB  1 
ATOM   955  C  CG1 . VAL A 1 121 ? -9.387  5.602   15.633  1.00 11.28 ? 121 VAL A CG1 1 
ATOM   956  C  CG2 . VAL A 1 121 ? -9.631  3.205   14.809  1.00 9.58  ? 121 VAL A CG2 1 
ATOM   957  N  N   . HIS A 1 122 ? -12.464 6.381   16.959  1.00 9.21  ? 122 HIS A N   1 
ATOM   958  C  CA  . HIS A 1 122 ? -13.187 7.655   17.138  1.00 9.28  ? 122 HIS A CA  1 
ATOM   959  C  C   . HIS A 1 122 ? -12.303 8.658   17.888  1.00 9.78  ? 122 HIS A C   1 
ATOM   960  O  O   . HIS A 1 122 ? -11.510 8.282   18.746  1.00 8.65  ? 122 HIS A O   1 
ATOM   961  C  CB  . HIS A 1 122 ? -14.494 7.516   17.910  1.00 9.31  ? 122 HIS A CB  1 
ATOM   962  C  CG  . HIS A 1 122 ? -15.376 6.376   17.490  1.00 9.75  ? 122 HIS A CG  1 
ATOM   963  N  ND1 . HIS A 1 122 ? -15.072 5.053   17.738  1.00 10.12 ? 122 HIS A ND1 1 
ATOM   964  C  CD2 . HIS A 1 122 ? -16.609 6.377   16.916  1.00 10.81 ? 122 HIS A CD2 1 
ATOM   965  C  CE1 . HIS A 1 122 ? -16.061 4.285   17.298  1.00 12.38 ? 122 HIS A CE1 1 
ATOM   966  N  NE2 . HIS A 1 122 ? -17.009 5.064   16.804  1.00 10.86 ? 122 HIS A NE2 1 
ATOM   967  N  N   . TRP A 1 123 ? -12.432 9.936   17.546  1.00 10.15 ? 123 TRP A N   1 
ATOM   968  C  CA  . TRP A 1 123 ? -11.631 10.973  18.230  1.00 10.68 ? 123 TRP A CA  1 
ATOM   969  C  C   . TRP A 1 123 ? -12.499 12.009  18.958  1.00 11.27 ? 123 TRP A C   1 
ATOM   970  O  O   . TRP A 1 123 ? -13.584 12.370  18.499  1.00 10.95 ? 123 TRP A O   1 
ATOM   971  C  CB  . TRP A 1 123 ? -10.617 11.639  17.296  1.00 11.58 ? 123 TRP A CB  1 
ATOM   972  C  CG  . TRP A 1 123 ? -11.221 12.276  16.078  1.00 12.96 ? 123 TRP A CG  1 
ATOM   973  C  CD1 . TRP A 1 123 ? -11.405 11.689  14.846  1.00 15.80 ? 123 TRP A CD1 1 
ATOM   974  C  CD2 . TRP A 1 123 ? -11.732 13.620  15.965  1.00 15.52 ? 123 TRP A CD2 1 
ATOM   975  N  NE1 . TRP A 1 123 ? -12.019 12.581  13.982  1.00 15.36 ? 123 TRP A NE1 1 
ATOM   976  C  CE2 . TRP A 1 123 ? -12.225 13.771  14.637  1.00 15.38 ? 123 TRP A CE2 1 
ATOM   977  C  CE3 . TRP A 1 123 ? -11.828 14.703  16.853  1.00 15.08 ? 123 TRP A CE3 1 
ATOM   978  C  CZ2 . TRP A 1 123 ? -12.789 14.973  14.169  1.00 15.49 ? 123 TRP A CZ2 1 
ATOM   979  C  CZ3 . TRP A 1 123 ? -12.399 15.908  16.392  1.00 14.71 ? 123 TRP A CZ3 1 
ATOM   980  C  CH2 . TRP A 1 123 ? -12.869 16.030  15.050  1.00 15.09 ? 123 TRP A CH2 1 
ATOM   981  N  N   . ASN A 1 124 ? -11.993 12.455  20.107  1.00 11.58 ? 124 ASN A N   1 
ATOM   982  C  CA  . ASN A 1 124 ? -12.704 13.351  21.005  1.00 11.55 ? 124 ASN A CA  1 
ATOM   983  C  C   . ASN A 1 124 ? -12.898 14.732  20.371  1.00 11.49 ? 124 ASN A C   1 
ATOM   984  O  O   . ASN A 1 124 ? -11.923 15.411  20.063  1.00 10.48 ? 124 ASN A O   1 
ATOM   985  C  CB  . ASN A 1 124 ? -11.943 13.480  22.332  1.00 11.82 ? 124 ASN A CB  1 
ATOM   986  C  CG  . ASN A 1 124 ? -12.817 14.062  23.439  1.00 13.12 ? 124 ASN A CG  1 
ATOM   987  O  OD1 . ASN A 1 124 ? -13.625 14.957  23.184  1.00 13.93 ? 124 ASN A OD1 1 
ATOM   988  N  ND2 . ASN A 1 124 ? -12.669 13.550  24.662  1.00 14.91 ? 124 ASN A ND2 1 
ATOM   989  N  N   . THR A 1 125 ? -14.148 15.133  20.157  1.00 13.55 ? 125 THR A N   1 
ATOM   990  C  CA  . THR A 1 125 ? -14.448 16.413  19.488  1.00 15.53 ? 125 THR A CA  1 
ATOM   991  C  C   . THR A 1 125 ? -13.846 17.632  20.179  1.00 14.68 ? 125 THR A C   1 
ATOM   992  O  O   . THR A 1 125 ? -13.662 18.672  19.549  1.00 16.20 ? 125 THR A O   1 
ATOM   993  C  CB  . THR A 1 125 ? -15.964 16.600  19.213  1.00 14.68 ? 125 THR A CB  1 
ATOM   994  O  OG1 . THR A 1 125 ? -16.684 16.524  20.449  1.00 18.66 ? 125 THR A OG1 1 
ATOM   995  C  CG2 . THR A 1 125 ? -16.483 15.532  18.262  1.00 18.11 ? 125 THR A CG2 1 
ATOM   996  N  N   . LYS A 1 126 ? -13.524 17.502  21.459  1.00 16.54 ? 127 LYS A N   1 
ATOM   997  C  CA  . LYS A 1 126 ? -12.956 18.630  22.182  1.00 16.80 ? 127 LYS A CA  1 
ATOM   998  C  C   . LYS A 1 126 ? -11.527 18.968  21.734  1.00 16.66 ? 127 LYS A C   1 
ATOM   999  O  O   . LYS A 1 126 ? -11.003 20.029  22.065  1.00 17.36 ? 127 LYS A O   1 
ATOM   1000 C  CB  . LYS A 1 126 ? -13.061 18.453  23.708  1.00 17.99 ? 127 LYS A CB  1 
ATOM   1001 C  CG  . LYS A 1 126 ? -12.139 17.421  24.330  1.00 19.25 ? 127 LYS A CG  1 
ATOM   1002 C  CD  . LYS A 1 126 ? -12.450 17.275  25.816  1.00 22.35 ? 127 LYS A CD  1 
ATOM   1003 C  CE  . LYS A 1 126 ? -11.441 16.388  26.531  1.00 24.37 ? 127 LYS A CE  1 
ATOM   1004 N  NZ  . LYS A 1 126 ? -11.504 16.532  28.016  1.00 29.57 ? 127 LYS A NZ  1 
ATOM   1005 N  N   . TYR A 1 127 ? -10.910 18.083  20.949  1.00 14.78 ? 128 TYR A N   1 
ATOM   1006 C  CA  . TYR A 1 127 ? -9.548  18.329  20.472  1.00 13.95 ? 128 TYR A CA  1 
ATOM   1007 C  C   . TYR A 1 127 ? -9.473  18.748  19.025  1.00 14.34 ? 128 TYR A C   1 
ATOM   1008 O  O   . TYR A 1 127 ? -8.387  19.002  18.475  1.00 15.05 ? 128 TYR A O   1 
ATOM   1009 C  CB  . TYR A 1 127 ? -8.631  17.134  20.775  1.00 13.32 ? 128 TYR A CB  1 
ATOM   1010 C  CG  . TYR A 1 127 ? -8.532  16.872  22.251  1.00 12.94 ? 128 TYR A CG  1 
ATOM   1011 C  CD1 . TYR A 1 127 ? -8.131  17.885  23.142  1.00 15.89 ? 128 TYR A CD1 1 
ATOM   1012 C  CD2 . TYR A 1 127 ? -8.805  15.606  22.764  1.00 12.29 ? 128 TYR A CD2 1 
ATOM   1013 C  CE1 . TYR A 1 127 ? -8.057  17.644  24.498  1.00 13.51 ? 128 TYR A CE1 1 
ATOM   1014 C  CE2 . TYR A 1 127 ? -8.737  15.348  24.097  1.00 11.76 ? 128 TYR A CE2 1 
ATOM   1015 C  CZ  . TYR A 1 127 ? -8.333  16.376  24.970  1.00 13.23 ? 128 TYR A CZ  1 
ATOM   1016 O  OH  . TYR A 1 127 ? -8.251  16.117  26.314  1.00 13.69 ? 128 TYR A OH  1 
ATOM   1017 N  N   . GLY A 1 128 ? -10.644 18.840  18.409  1.00 14.55 ? 129 GLY A N   1 
ATOM   1018 C  CA  . GLY A 1 128 ? -10.772 19.494  17.094  1.00 15.76 ? 129 GLY A CA  1 
ATOM   1019 C  C   . GLY A 1 128 ? -10.424 18.632  15.900  1.00 16.55 ? 129 GLY A C   1 
ATOM   1020 O  O   . GLY A 1 128 ? -11.066 18.745  14.836  1.00 16.67 ? 129 GLY A O   1 
ATOM   1021 N  N   . ASP A 1 129 ? -9.485  17.719  16.073  1.00 16.47 ? 130 ASP A N   1 
ATOM   1022 C  CA  . ASP A 1 129 ? -9.216  16.757  15.013  1.00 17.32 ? 130 ASP A CA  1 
ATOM   1023 C  C   . ASP A 1 129 ? -8.399  15.579  15.509  1.00 17.19 ? 130 ASP A C   1 
ATOM   1024 O  O   . ASP A 1 129 ? -7.949  15.568  16.668  1.00 15.61 ? 130 ASP A O   1 
ATOM   1025 C  CB  . ASP A 1 129 ? -8.560  17.425  13.799  1.00 17.90 ? 130 ASP A CB  1 
ATOM   1026 C  CG  . ASP A 1 129 ? -7.139  17.877  14.070  1.00 20.52 ? 130 ASP A CG  1 
ATOM   1027 O  OD1 . ASP A 1 129 ? -6.567  17.467  15.100  1.00 25.09 ? 130 ASP A OD1 1 
ATOM   1028 O  OD2 . ASP A 1 129 ? -6.596  18.645  13.248  1.00 20.89 ? 130 ASP A OD2 1 
ATOM   1029 N  N   . PHE A 1 130 ? -8.226  14.600  14.623  1.00 16.22 ? 131 PHE A N   1 
ATOM   1030 C  CA  . PHE A 1 130 ? -7.543  13.360  14.974  1.00 15.83 ? 131 PHE A CA  1 
ATOM   1031 C  C   . PHE A 1 130 ? -6.097  13.571  15.425  1.00 14.90 ? 131 PHE A C   1 
ATOM   1032 O  O   . PHE A 1 130 ? -5.689  13.002  16.426  1.00 13.46 ? 131 PHE A O   1 
ATOM   1033 C  CB  . PHE A 1 130 ? -7.605  12.336  13.830  1.00 15.55 ? 131 PHE A CB  1 
ATOM   1034 C  CG  . PHE A 1 130 ? -6.963  11.031  14.152  1.00 16.33 ? 131 PHE A CG  1 
ATOM   1035 C  CD1 . PHE A 1 130 ? -7.663  10.060  14.860  1.00 14.31 ? 131 PHE A CD1 1 
ATOM   1036 C  CD2 . PHE A 1 130 ? -5.635  10.756  13.758  1.00 15.97 ? 131 PHE A CD2 1 
ATOM   1037 C  CE1 . PHE A 1 130 ? -7.071  8.831   15.181  1.00 15.85 ? 131 PHE A CE1 1 
ATOM   1038 C  CE2 . PHE A 1 130 ? -5.038  9.538   14.071  1.00 17.04 ? 131 PHE A CE2 1 
ATOM   1039 C  CZ  . PHE A 1 130 ? -5.764  8.569   14.793  1.00 18.32 ? 131 PHE A CZ  1 
ATOM   1040 N  N   . GLY A 1 131 ? -5.330  14.365  14.674  1.00 13.44 ? 132 GLY A N   1 
ATOM   1041 C  CA  . GLY A 1 131 ? -3.906  14.542  14.968  1.00 15.09 ? 132 GLY A CA  1 
ATOM   1042 C  C   . GLY A 1 131 ? -3.645  15.183  16.319  1.00 14.72 ? 132 GLY A C   1 
ATOM   1043 O  O   . GLY A 1 131 ? -2.662  14.866  16.983  1.00 15.46 ? 132 GLY A O   1 
ATOM   1044 N  N   . LYS A 1 132 ? -4.528  16.093  16.725  1.00 14.38 ? 133 LYS A N   1 
ATOM   1045 C  CA  . LYS A 1 132 ? -4.426  16.686  18.067  1.00 13.91 ? 133 LYS A CA  1 
ATOM   1046 C  C   . LYS A 1 132 ? -4.898  15.737  19.169  1.00 13.68 ? 133 LYS A C   1 
ATOM   1047 O  O   . LYS A 1 132 ? -4.307  15.646  20.250  1.00 13.12 ? 133 LYS A O   1 
ATOM   1048 C  CB  . LYS A 1 132 ? -5.192  17.998  18.154  1.00 14.20 ? 133 LYS A CB  1 
ATOM   1049 C  CG  . LYS A 1 132 ? -4.608  19.118  17.286  1.00 18.29 ? 133 LYS A CG  1 
ATOM   1050 C  CD  . LYS A 1 132 ? -3.105  19.201  17.448  1.00 23.16 ? 133 LYS A CD  1 
ATOM   1051 C  CE  . LYS A 1 132 ? -2.680  19.636  18.862  1.00 24.07 ? 133 LYS A CE  1 
ATOM   1052 N  NZ  . LYS A 1 132 ? -3.210  20.989  19.241  1.00 28.29 ? 133 LYS A NZ  1 
ATOM   1053 N  N   . ALA A 1 133 ? -5.979  15.042  18.878  1.00 12.64 ? 134 ALA A N   1 
ATOM   1054 C  CA  . ALA A 1 133 ? -6.540  14.094  19.819  1.00 13.08 ? 134 ALA A CA  1 
ATOM   1055 C  C   . ALA A 1 133 ? -5.535  12.999  20.236  1.00 12.02 ? 134 ALA A C   1 
ATOM   1056 O  O   . ALA A 1 133 ? -5.480  12.625  21.422  1.00 11.96 ? 134 ALA A O   1 
ATOM   1057 C  CB  . ALA A 1 133 ? -7.844  13.482  19.213  1.00 12.95 ? 134 ALA A CB  1 
ATOM   1058 N  N   . VAL A 1 134 ? -4.726  12.493  19.302  1.00 12.10 ? 135 VAL A N   1 
ATOM   1059 C  CA  . VAL A 1 134 ? -3.800  11.376  19.661  1.00 13.63 ? 135 VAL A CA  1 
ATOM   1060 C  C   . VAL A 1 134 ? -2.686  11.789  20.628  1.00 13.88 ? 135 VAL A C   1 
ATOM   1061 O  O   . VAL A 1 134 ? -1.968  10.947  21.177  1.00 13.90 ? 135 VAL A O   1 
ATOM   1062 C  CB  . VAL A 1 134 ? -3.191  10.644  18.425  1.00 13.40 ? 135 VAL A CB  1 
ATOM   1063 C  CG1 . VAL A 1 134 ? -4.283  10.000  17.606  1.00 12.80 ? 135 VAL A CG1 1 
ATOM   1064 C  CG2 . VAL A 1 134 ? -2.297  11.576  17.586  1.00 13.80 ? 135 VAL A CG2 1 
ATOM   1065 N  N   A GLN A 1 135 ? -2.541  13.100  20.818  0.50 13.97 ? 136 GLN A N   1 
ATOM   1066 N  N   B GLN A 1 135 ? -2.567  13.092  20.850  0.50 13.95 ? 136 GLN A N   1 
ATOM   1067 C  CA  A GLN A 1 135 ? -1.551  13.637  21.750  0.50 14.62 ? 136 GLN A CA  1 
ATOM   1068 C  CA  B GLN A 1 135 ? -1.563  13.622  21.764  0.50 14.55 ? 136 GLN A CA  1 
ATOM   1069 C  C   A GLN A 1 135 ? -2.173  13.902  23.129  0.50 14.61 ? 136 GLN A C   1 
ATOM   1070 C  C   B GLN A 1 135 ? -2.112  13.737  23.185  0.50 14.60 ? 136 GLN A C   1 
ATOM   1071 O  O   A GLN A 1 135 ? -1.570  14.579  23.978  0.50 14.60 ? 136 GLN A O   1 
ATOM   1072 O  O   B GLN A 1 135 ? -1.399  14.129  24.116  0.50 14.84 ? 136 GLN A O   1 
ATOM   1073 C  CB  A GLN A 1 135 ? -0.919  14.923  21.172  0.50 15.10 ? 136 GLN A CB  1 
ATOM   1074 C  CB  B GLN A 1 135 ? -1.081  14.979  21.235  0.50 14.93 ? 136 GLN A CB  1 
ATOM   1075 C  CG  A GLN A 1 135 ? -0.167  14.749  19.833  0.50 16.79 ? 136 GLN A CG  1 
ATOM   1076 C  CG  B GLN A 1 135 ? -0.620  14.893  19.788  0.50 16.37 ? 136 GLN A CG  1 
ATOM   1077 C  CD  A GLN A 1 135 ? 1.090   13.895  19.933  0.50 18.82 ? 136 GLN A CD  1 
ATOM   1078 C  CD  B GLN A 1 135 ? 0.004   16.167  19.274  0.50 18.10 ? 136 GLN A CD  1 
ATOM   1079 O  OE1 A GLN A 1 135 ? 1.784   13.905  20.948  0.50 21.54 ? 136 GLN A OE1 1 
ATOM   1080 O  OE1 B GLN A 1 135 ? -0.327  16.630  18.183  0.50 19.62 ? 136 GLN A OE1 1 
ATOM   1081 N  NE2 A GLN A 1 135 ? 1.399   13.159  18.860  0.50 19.66 ? 136 GLN A NE2 1 
ATOM   1082 N  NE2 B GLN A 1 135 ? 0.911   16.743  20.052  0.50 17.55 ? 136 GLN A NE2 1 
ATOM   1083 N  N   . GLN A 1 136 ? -3.383  13.382  23.347  1.00 14.14 ? 137 GLN A N   1 
ATOM   1084 C  CA  . GLN A 1 136 ? -4.093  13.564  24.627  1.00 13.94 ? 137 GLN A CA  1 
ATOM   1085 C  C   . GLN A 1 136 ? -4.475  12.209  25.237  1.00 12.79 ? 137 GLN A C   1 
ATOM   1086 O  O   . GLN A 1 136 ? -4.835  11.269  24.521  1.00 12.01 ? 137 GLN A O   1 
ATOM   1087 C  CB  . GLN A 1 136 ? -5.343  14.416  24.452  1.00 13.74 ? 137 GLN A CB  1 
ATOM   1088 C  CG  . GLN A 1 136 ? -5.132  15.742  23.686  1.00 17.20 ? 137 GLN A CG  1 
ATOM   1089 C  CD  . GLN A 1 136 ? -4.136  16.635  24.387  1.00 20.75 ? 137 GLN A CD  1 
ATOM   1090 O  OE1 . GLN A 1 136 ? -4.056  16.657  25.617  1.00 21.50 ? 137 GLN A OE1 1 
ATOM   1091 N  NE2 . GLN A 1 136 ? -3.331  17.343  23.604  1.00 25.65 ? 137 GLN A NE2 1 
ATOM   1092 N  N   . PRO A 1 137 ? -4.422  12.103  26.574  1.00 13.33 ? 138 PRO A N   1 
ATOM   1093 C  CA  . PRO A 1 137 ? -4.697  10.791  27.199  1.00 13.66 ? 138 PRO A CA  1 
ATOM   1094 C  C   . PRO A 1 137 ? -6.149  10.344  27.029  1.00 13.08 ? 138 PRO A C   1 
ATOM   1095 O  O   . PRO A 1 137 ? -6.436  9.137   27.093  1.00 12.91 ? 138 PRO A O   1 
ATOM   1096 C  CB  . PRO A 1 137 ? -4.346  10.988  28.669  1.00 14.61 ? 138 PRO A CB  1 
ATOM   1097 C  CG  . PRO A 1 137 ? -4.222  12.459  28.870  1.00 15.34 ? 138 PRO A CG  1 
ATOM   1098 C  CD  . PRO A 1 137 ? -4.121  13.166  27.555  1.00 14.13 ? 138 PRO A CD  1 
ATOM   1099 N  N   . ASP A 1 138 ? -7.056  11.287  26.769  1.00 11.17 ? 139 ASP A N   1 
ATOM   1100 C  CA  . ASP A 1 138 ? -8.451  10.915  26.465  1.00 11.49 ? 139 ASP A CA  1 
ATOM   1101 C  C   . ASP A 1 138 ? -8.860  11.298  25.024  1.00 10.74 ? 139 ASP A C   1 
ATOM   1102 O  O   . ASP A 1 138 ? -10.001 11.715  24.781  1.00 11.03 ? 139 ASP A O   1 
ATOM   1103 C  CB  . ASP A 1 138 ? -9.418  11.548  27.464  1.00 11.82 ? 139 ASP A CB  1 
ATOM   1104 C  CG  . ASP A 1 138 ? -9.299  13.045  27.515  1.00 11.17 ? 139 ASP A CG  1 
ATOM   1105 O  OD1 . ASP A 1 138 ? -8.355  13.615  26.908  1.00 16.82 ? 139 ASP A OD1 1 
ATOM   1106 O  OD2 . ASP A 1 138 ? -10.140 13.646  28.200  1.00 16.02 ? 139 ASP A OD2 1 
ATOM   1107 N  N   . GLY A 1 139 ? -7.917  11.192  24.089  1.00 10.16 ? 140 GLY A N   1 
ATOM   1108 C  CA  . GLY A 1 139 ? -8.140  11.705  22.762  1.00 8.75  ? 140 GLY A CA  1 
ATOM   1109 C  C   . GLY A 1 139 ? -8.949  10.767  21.893  1.00 9.15  ? 140 GLY A C   1 
ATOM   1110 O  O   . GLY A 1 139 ? -9.700  11.239  21.052  1.00 8.19  ? 140 GLY A O   1 
ATOM   1111 N  N   . LEU A 1 140 ? -8.788  9.458   22.099  1.00 8.00  ? 141 LEU A N   1 
ATOM   1112 C  CA  . LEU A 1 140 ? -9.469  8.479   21.239  1.00 8.43  ? 141 LEU A CA  1 
ATOM   1113 C  C   . LEU A 1 140 ? -10.384 7.557   22.030  1.00 8.72  ? 141 LEU A C   1 
ATOM   1114 O  O   . LEU A 1 140 ? -10.153 7.271   23.203  1.00 8.78  ? 141 LEU A O   1 
ATOM   1115 C  CB  . LEU A 1 140 ? -8.461  7.633   20.468  1.00 9.26  ? 141 LEU A CB  1 
ATOM   1116 C  CG  . LEU A 1 140 ? -7.506  8.275   19.465  1.00 12.04 ? 141 LEU A CG  1 
ATOM   1117 C  CD1 . LEU A 1 140 ? -6.951  7.181   18.580  1.00 11.05 ? 141 LEU A CD1 1 
ATOM   1118 C  CD2 . LEU A 1 140 ? -8.162  9.355   18.589  1.00 13.40 ? 141 LEU A CD2 1 
ATOM   1119 N  N   . ALA A 1 141 ? -11.442 7.093   21.365  1.00 9.13  ? 142 ALA A N   1 
ATOM   1120 C  CA  . ALA A 1 141 ? -12.219 5.949   21.878  1.00 8.93  ? 142 ALA A CA  1 
ATOM   1121 C  C   . ALA A 1 141 ? -12.244 4.922   20.726  1.00 8.86  ? 142 ALA A C   1 
ATOM   1122 O  O   . ALA A 1 141 ? -12.635 5.246   19.584  1.00 9.03  ? 142 ALA A O   1 
ATOM   1123 C  CB  . ALA A 1 141 ? -13.609 6.380   22.253  1.00 9.57  ? 142 ALA A CB  1 
ATOM   1124 N  N   . VAL A 1 142 ? -11.720 3.732   20.996  1.00 9.66  ? 143 VAL A N   1 
ATOM   1125 C  CA  . VAL A 1 142 ? -11.750 2.689   19.980  1.00 9.04  ? 143 VAL A CA  1 
ATOM   1126 C  C   . VAL A 1 142 ? -12.715 1.623   20.456  1.00 9.22  ? 143 VAL A C   1 
ATOM   1127 O  O   . VAL A 1 142 ? -12.571 1.065   21.566  1.00 8.22  ? 143 VAL A O   1 
ATOM   1128 C  CB  . VAL A 1 142 ? -10.342 2.099   19.621  1.00 9.17  ? 143 VAL A CB  1 
ATOM   1129 C  CG1 . VAL A 1 142 ? -10.442 1.070   18.456  1.00 9.55  ? 143 VAL A CG1 1 
ATOM   1130 C  CG2 . VAL A 1 142 ? -9.390  3.230   19.220  1.00 8.41  ? 143 VAL A CG2 1 
ATOM   1131 N  N   . LEU A 1 143 ? -13.688 1.330   19.605  1.00 7.82  ? 144 LEU A N   1 
ATOM   1132 C  CA  . LEU A 1 143 ? -14.668 0.274   19.897  1.00 9.47  ? 144 LEU A CA  1 
ATOM   1133 C  C   . LEU A 1 143 ? -14.159 -1.002  19.224  1.00 8.90  ? 144 LEU A C   1 
ATOM   1134 O  O   . LEU A 1 143 ? -14.040 -1.062  17.983  1.00 9.74  ? 144 LEU A O   1 
ATOM   1135 C  CB  . LEU A 1 143 ? -16.065 0.691   19.363  1.00 9.75  ? 144 LEU A CB  1 
ATOM   1136 C  CG  . LEU A 1 143 ? -17.206 -0.302  19.469  1.00 9.86  ? 144 LEU A CG  1 
ATOM   1137 C  CD1 . LEU A 1 143 ? -17.416 -0.673  20.933  1.00 12.10 ? 144 LEU A CD1 1 
ATOM   1138 C  CD2 . LEU A 1 143 ? -18.493 0.250   18.774  1.00 11.13 ? 144 LEU A CD2 1 
ATOM   1139 N  N   . GLY A 1 144 ? -13.865 -2.017  20.042  1.00 8.45  ? 145 GLY A N   1 
ATOM   1140 C  CA  . GLY A 1 144 ? -13.296 -3.290  19.566  1.00 6.96  ? 145 GLY A CA  1 
ATOM   1141 C  C   . GLY A 1 144 ? -14.375 -4.364  19.536  1.00 7.06  ? 145 GLY A C   1 
ATOM   1142 O  O   . GLY A 1 144 ? -15.125 -4.537  20.502  1.00 8.31  ? 145 GLY A O   1 
ATOM   1143 N  N   . ILE A 1 145 ? -14.441 -5.096  18.432  1.00 7.54  ? 146 ILE A N   1 
ATOM   1144 C  CA  . ILE A 1 145 ? -15.480 -6.125  18.258  1.00 7.86  ? 146 ILE A CA  1 
ATOM   1145 C  C   . ILE A 1 145 ? -14.790 -7.395  17.728  1.00 8.26  ? 146 ILE A C   1 
ATOM   1146 O  O   . ILE A 1 145 ? -14.109 -7.356  16.720  1.00 9.18  ? 146 ILE A O   1 
ATOM   1147 C  CB  . ILE A 1 145 ? -16.550 -5.636  17.262  1.00 8.42  ? 146 ILE A CB  1 
ATOM   1148 C  CG1 . ILE A 1 145 ? -17.222 -4.349  17.812  1.00 7.42  ? 146 ILE A CG1 1 
ATOM   1149 C  CG2 . ILE A 1 145 ? -17.579 -6.726  17.031  1.00 8.74  ? 146 ILE A CG2 1 
ATOM   1150 C  CD1 . ILE A 1 145 ? -18.361 -3.743  16.917  1.00 8.99  ? 146 ILE A CD1 1 
ATOM   1151 N  N   . PHE A 1 146 ? -14.957 -8.499  18.432  1.00 9.51  ? 147 PHE A N   1 
ATOM   1152 C  CA  . PHE A 1 146 ? -14.340 -9.766  18.035  1.00 8.31  ? 147 PHE A CA  1 
ATOM   1153 C  C   . PHE A 1 146 ? -15.099 -10.398 16.883  1.00 9.17  ? 147 PHE A C   1 
ATOM   1154 O  O   . PHE A 1 146 ? -16.322 -10.285 16.806  1.00 9.67  ? 147 PHE A O   1 
ATOM   1155 C  CB  . PHE A 1 146 ? -14.344 -10.715 19.229  1.00 8.12  ? 147 PHE A CB  1 
ATOM   1156 C  CG  . PHE A 1 146 ? -13.488 -10.255 20.356  1.00 5.91  ? 147 PHE A CG  1 
ATOM   1157 C  CD1 . PHE A 1 146 ? -12.101 -10.087 20.181  1.00 9.98  ? 147 PHE A CD1 1 
ATOM   1158 C  CD2 . PHE A 1 146 ? -14.039 -9.997  21.592  1.00 9.37  ? 147 PHE A CD2 1 
ATOM   1159 C  CE1 . PHE A 1 146 ? -11.271 -9.675  21.256  1.00 9.04  ? 147 PHE A CE1 1 
ATOM   1160 C  CE2 . PHE A 1 146 ? -13.250 -9.607  22.667  1.00 11.29 ? 147 PHE A CE2 1 
ATOM   1161 C  CZ  . PHE A 1 146 ? -11.856 -9.443  22.497  1.00 7.83  ? 147 PHE A CZ  1 
ATOM   1162 N  N   . LEU A 1 147 ? -14.359 -11.036 15.990  1.00 8.80  ? 148 LEU A N   1 
ATOM   1163 C  CA  . LEU A 1 147 ? -14.942 -11.862 14.936  1.00 9.09  ? 148 LEU A CA  1 
ATOM   1164 C  C   . LEU A 1 147 ? -14.611 -13.345 15.166  1.00 10.01 ? 148 LEU A C   1 
ATOM   1165 O  O   . LEU A 1 147 ? -13.426 -13.698 15.356  1.00 9.27  ? 148 LEU A O   1 
ATOM   1166 C  CB  . LEU A 1 147 ? -14.402 -11.437 13.543  1.00 9.39  ? 148 LEU A CB  1 
ATOM   1167 C  CG  . LEU A 1 147 ? -14.985 -10.204 12.837  1.00 9.43  ? 148 LEU A CG  1 
ATOM   1168 C  CD1 . LEU A 1 147 ? -14.907 -8.893  13.679  1.00 11.21 ? 148 LEU A CD1 1 
ATOM   1169 C  CD2 . LEU A 1 147 ? -14.328 -9.981  11.512  1.00 10.60 ? 148 LEU A CD2 1 
ATOM   1170 N  N   . LYS A 1 148 ? -15.648 -14.194 15.146  1.00 11.34 ? 149 LYS A N   1 
ATOM   1171 C  CA  . LYS A 1 148 ? -15.460 -15.631 15.060  1.00 11.34 ? 149 LYS A CA  1 
ATOM   1172 C  C   . LYS A 1 148 ? -15.958 -16.129 13.706  1.00 11.95 ? 149 LYS A C   1 
ATOM   1173 O  O   . LYS A 1 148 ? -16.776 -15.478 13.044  1.00 11.91 ? 149 LYS A O   1 
ATOM   1174 C  CB  . LYS A 1 148 ? -16.175 -16.380 16.184  1.00 12.75 ? 149 LYS A CB  1 
ATOM   1175 C  CG  . LYS A 1 148 ? -17.699 -16.254 16.137  1.00 15.24 ? 149 LYS A CG  1 
ATOM   1176 C  CD  . LYS A 1 148 ? -18.268 -16.893 17.387  1.00 20.75 ? 149 LYS A CD  1 
ATOM   1177 C  CE  . LYS A 1 148 ? -19.758 -16.770 17.404  1.00 23.55 ? 149 LYS A CE  1 
ATOM   1178 N  NZ  . LYS A 1 148 ? -20.316 -17.796 18.327  1.00 28.82 ? 149 LYS A NZ  1 
ATOM   1179 N  N   . VAL A 1 149 ? -15.472 -17.299 13.317  1.00 12.65 ? 150 VAL A N   1 
ATOM   1180 C  CA  . VAL A 1 149 ? -15.816 -17.874 12.024  1.00 13.40 ? 150 VAL A CA  1 
ATOM   1181 C  C   . VAL A 1 149 ? -17.038 -18.791 12.208  1.00 13.89 ? 150 VAL A C   1 
ATOM   1182 O  O   . VAL A 1 149 ? -17.054 -19.705 13.070  1.00 14.01 ? 150 VAL A O   1 
ATOM   1183 C  CB  . VAL A 1 149 ? -14.621 -18.643 11.410  1.00 14.08 ? 150 VAL A CB  1 
ATOM   1184 C  CG1 . VAL A 1 149 ? -15.033 -19.460 10.145  1.00 13.07 ? 150 VAL A CG1 1 
ATOM   1185 C  CG2 . VAL A 1 149 ? -13.492 -17.678 11.063  1.00 14.55 ? 150 VAL A CG2 1 
ATOM   1186 N  N   . GLY A 1 150 ? -18.041 -18.555 11.376  1.00 13.11 ? 151 GLY A N   1 
ATOM   1187 C  CA  . GLY A 1 150 ? -19.271 -19.374 11.370  1.00 14.44 ? 151 GLY A CA  1 
ATOM   1188 C  C   . GLY A 1 150 ? -20.195 -18.884 10.275  1.00 13.72 ? 151 GLY A C   1 
ATOM   1189 O  O   . GLY A 1 150 ? -19.838 -18.942 9.098   1.00 13.34 ? 151 GLY A O   1 
ATOM   1190 N  N   A SER A 1 151 ? -21.389 -18.408 10.643  0.50 14.63 ? 152 SER A N   1 
ATOM   1191 N  N   B SER A 1 151 ? -21.370 -18.383 10.669  0.50 14.44 ? 152 SER A N   1 
ATOM   1192 C  CA  A SER A 1 151 ? -22.286 -17.829 9.623   0.50 15.48 ? 152 SER A CA  1 
ATOM   1193 C  CA  B SER A 1 151 ? -22.292 -17.734 9.720   0.50 15.18 ? 152 SER A CA  1 
ATOM   1194 C  C   A SER A 1 151 ? -21.726 -16.493 9.096   0.50 15.49 ? 152 SER A C   1 
ATOM   1195 C  C   B SER A 1 151 ? -21.659 -16.482 9.083   0.50 15.27 ? 152 SER A C   1 
ATOM   1196 O  O   A SER A 1 151 ? -21.015 -15.775 9.818   0.50 14.94 ? 152 SER A O   1 
ATOM   1197 O  O   B SER A 1 151 ? -20.844 -15.800 9.721   0.50 14.57 ? 152 SER A O   1 
ATOM   1198 C  CB  A SER A 1 151 ? -23.720 -17.678 10.140  0.50 16.03 ? 152 SER A CB  1 
ATOM   1199 C  CB  B SER A 1 151 ? -23.590 -17.356 10.428  0.50 15.55 ? 152 SER A CB  1 
ATOM   1200 O  OG  A SER A 1 151 ? -23.835 -16.641 11.098  0.50 17.35 ? 152 SER A OG  1 
ATOM   1201 O  OG  B SER A 1 151 ? -24.223 -18.504 10.963  0.50 16.37 ? 152 SER A OG  1 
ATOM   1202 N  N   . ALA A 1 152 ? -22.025 -16.181 7.834   1.00 15.17 ? 153 ALA A N   1 
ATOM   1203 C  CA  . ALA A 1 152 ? -21.603 -14.922 7.214   1.00 14.95 ? 153 ALA A CA  1 
ATOM   1204 C  C   . ALA A 1 152 ? -22.243 -13.724 7.917   1.00 15.06 ? 153 ALA A C   1 
ATOM   1205 O  O   . ALA A 1 152 ? -23.328 -13.811 8.471   1.00 15.64 ? 153 ALA A O   1 
ATOM   1206 C  CB  . ALA A 1 152 ? -21.926 -14.872 5.692   1.00 15.28 ? 153 ALA A CB  1 
ATOM   1207 N  N   . LYS A 1 153 ? -21.540 -12.606 7.872   1.00 15.47 ? 154 LYS A N   1 
ATOM   1208 C  CA  . LYS A 1 153 ? -22.077 -11.349 8.313   1.00 15.60 ? 154 LYS A CA  1 
ATOM   1209 C  C   . LYS A 1 153 ? -22.467 -10.578 7.041   1.00 15.28 ? 154 LYS A C   1 
ATOM   1210 O  O   . LYS A 1 153 ? -21.597 -10.087 6.310   1.00 14.65 ? 154 LYS A O   1 
ATOM   1211 C  CB  . LYS A 1 153 ? -21.021 -10.595 9.139   1.00 15.67 ? 154 LYS A CB  1 
ATOM   1212 C  CG  . LYS A 1 153 ? -21.553 -9.400  9.907   1.00 17.82 ? 154 LYS A CG  1 
ATOM   1213 C  CD  . LYS A 1 153 ? -22.377 -9.806  11.119  1.00 20.95 ? 154 LYS A CD  1 
ATOM   1214 C  CE  . LYS A 1 153 ? -22.922 -8.595  11.840  1.00 22.53 ? 154 LYS A CE  1 
ATOM   1215 N  NZ  . LYS A 1 153 ? -23.724 -8.982  13.013  1.00 24.95 ? 154 LYS A NZ  1 
ATOM   1216 N  N   . PRO A 1 154 ? -23.788 -10.480 6.764   1.00 16.58 ? 155 PRO A N   1 
ATOM   1217 C  CA  . PRO A 1 154 ? -24.231 -9.883  5.487   1.00 17.00 ? 155 PRO A CA  1 
ATOM   1218 C  C   . PRO A 1 154 ? -23.695 -8.466  5.309   1.00 16.54 ? 155 PRO A C   1 
ATOM   1219 O  O   . PRO A 1 154 ? -23.229 -8.102  4.225   1.00 16.46 ? 155 PRO A O   1 
ATOM   1220 C  CB  . PRO A 1 154 ? -25.771 -9.881  5.617   1.00 17.69 ? 155 PRO A CB  1 
ATOM   1221 C  CG  . PRO A 1 154 ? -26.069 -10.998 6.587   1.00 17.58 ? 155 PRO A CG  1 
ATOM   1222 C  CD  . PRO A 1 154 ? -24.932 -10.911 7.588   1.00 16.79 ? 155 PRO A CD  1 
ATOM   1223 N  N   . GLY A 1 155 ? -23.680 -7.717  6.402   1.00 17.20 ? 156 GLY A N   1 
ATOM   1224 C  CA  . GLY A 1 155 ? -23.242 -6.330  6.381   1.00 17.59 ? 156 GLY A CA  1 
ATOM   1225 C  C   . GLY A 1 155 ? -21.765 -6.101  6.163   1.00 17.82 ? 156 GLY A C   1 
ATOM   1226 O  O   . GLY A 1 155 ? -21.353 -4.967  5.941   1.00 18.54 ? 156 GLY A O   1 
ATOM   1227 N  N   . LEU A 1 156 ? -20.968 -7.175  6.238   1.00 16.52 ? 157 LEU A N   1 
ATOM   1228 C  CA  . LEU A 1 156 ? -19.563 -7.149  5.875   1.00 15.22 ? 157 LEU A CA  1 
ATOM   1229 C  C   . LEU A 1 156 ? -19.267 -7.370  4.401   1.00 15.09 ? 157 LEU A C   1 
ATOM   1230 O  O   . LEU A 1 156 ? -18.147 -7.118  3.936   1.00 14.11 ? 157 LEU A O   1 
ATOM   1231 C  CB  . LEU A 1 156 ? -18.788 -8.187  6.718   1.00 15.92 ? 157 LEU A CB  1 
ATOM   1232 C  CG  . LEU A 1 156 ? -17.266 -8.270  6.515   1.00 14.14 ? 157 LEU A CG  1 
ATOM   1233 C  CD1 . LEU A 1 156 ? -16.585 -6.939  6.927   1.00 12.14 ? 157 LEU A CD1 1 
ATOM   1234 C  CD2 . LEU A 1 156 ? -16.677 -9.445  7.290   1.00 14.64 ? 157 LEU A CD2 1 
ATOM   1235 N  N   . GLN A 1 157 ? -20.250 -7.861  3.643   1.00 15.65 ? 158 GLN A N   1 
ATOM   1236 C  CA  . GLN A 1 157 ? -19.931 -8.373  2.315   1.00 15.97 ? 158 GLN A CA  1 
ATOM   1237 C  C   . GLN A 1 157 ? -19.481 -7.281  1.361   1.00 15.62 ? 158 GLN A C   1 
ATOM   1238 O  O   . GLN A 1 157 ? -18.611 -7.505  0.546   1.00 15.07 ? 158 GLN A O   1 
ATOM   1239 C  CB  . GLN A 1 157 ? -21.080 -9.212  1.733   1.00 16.49 ? 158 GLN A CB  1 
ATOM   1240 C  CG  . GLN A 1 157 ? -20.673 -10.021 0.483   1.00 16.59 ? 158 GLN A CG  1 
ATOM   1241 C  CD  . GLN A 1 157 ? -19.537 -11.019 0.750   1.00 17.19 ? 158 GLN A CD  1 
ATOM   1242 O  OE1 . GLN A 1 157 ? -19.447 -11.603 1.824   1.00 17.23 ? 158 GLN A OE1 1 
ATOM   1243 N  NE2 . GLN A 1 157 ? -18.683 -11.221 -0.236  1.00 18.05 ? 158 GLN A NE2 1 
ATOM   1244 N  N   . LYS A 1 158 ? -20.066 -6.093  1.479   1.00 16.48 ? 159 LYS A N   1 
ATOM   1245 C  CA  . LYS A 1 158 ? -19.652 -4.969  0.653   1.00 17.63 ? 159 LYS A CA  1 
ATOM   1246 C  C   . LYS A 1 158 ? -18.148 -4.651  0.834   1.00 16.96 ? 159 LYS A C   1 
ATOM   1247 O  O   . LYS A 1 158 ? -17.454 -4.345  -0.120  1.00 16.73 ? 159 LYS A O   1 
ATOM   1248 C  CB  . LYS A 1 158 ? -20.537 -3.750  0.924   1.00 18.58 ? 159 LYS A CB  1 
ATOM   1249 C  CG  . LYS A 1 158 ? -21.973 -3.901  0.382   1.00 21.81 ? 159 LYS A CG  1 
ATOM   1250 C  CD  . LYS A 1 158 ? -22.816 -2.629  0.571   1.00 21.96 ? 159 LYS A CD  1 
ATOM   1251 C  CE  . LYS A 1 158 ? -24.270 -2.860  0.048   1.00 24.67 ? 159 LYS A CE  1 
ATOM   1252 N  NZ  . LYS A 1 158 ? -25.216 -1.682  0.183   1.00 26.97 ? 159 LYS A NZ  1 
ATOM   1253 N  N   . VAL A 1 159 ? -17.663 -4.752  2.074   1.00 16.22 ? 160 VAL A N   1 
ATOM   1254 C  CA  . VAL A 1 159 ? -16.238 -4.579  2.367   1.00 15.24 ? 160 VAL A CA  1 
ATOM   1255 C  C   . VAL A 1 159 ? -15.419 -5.679  1.686   1.00 15.13 ? 160 VAL A C   1 
ATOM   1256 O  O   . VAL A 1 159 ? -14.445 -5.406  0.977   1.00 14.59 ? 160 VAL A O   1 
ATOM   1257 C  CB  . VAL A 1 159 ? -15.997 -4.595  3.881   1.00 14.86 ? 160 VAL A CB  1 
ATOM   1258 C  CG1 . VAL A 1 159 ? -14.488 -4.538  4.197   1.00 13.92 ? 160 VAL A CG1 1 
ATOM   1259 C  CG2 . VAL A 1 159 ? -16.773 -3.444  4.564   1.00 15.57 ? 160 VAL A CG2 1 
ATOM   1260 N  N   . VAL A 1 160 ? -15.818 -6.928  1.902   1.00 15.48 ? 161 VAL A N   1 
ATOM   1261 C  CA  . VAL A 1 160 ? -15.098 -8.074  1.350   1.00 17.89 ? 161 VAL A CA  1 
ATOM   1262 C  C   . VAL A 1 160 ? -15.052 -8.000  -0.183  1.00 17.81 ? 161 VAL A C   1 
ATOM   1263 O  O   . VAL A 1 160 ? -14.031 -8.255  -0.800  1.00 17.37 ? 161 VAL A O   1 
ATOM   1264 C  CB  . VAL A 1 160 ? -15.763 -9.403  1.900   1.00 18.03 ? 161 VAL A CB  1 
ATOM   1265 C  CG1 . VAL A 1 160 ? -15.476 -10.602 1.033   1.00 20.62 ? 161 VAL A CG1 1 
ATOM   1266 C  CG2 . VAL A 1 160 ? -15.308 -9.628  3.322   1.00 19.50 ? 161 VAL A CG2 1 
ATOM   1267 N  N   . ASP A 1 161 ? -16.145 -7.560  -0.789  1.00 19.27 ? 162 ASP A N   1 
ATOM   1268 C  CA  . ASP A 1 161 ? -16.212 -7.537  -2.245  1.00 20.28 ? 162 ASP A CA  1 
ATOM   1269 C  C   . ASP A 1 161 ? -15.281 -6.509  -2.932  1.00 20.83 ? 162 ASP A C   1 
ATOM   1270 O  O   . ASP A 1 161 ? -14.940 -6.673  -4.105  1.00 22.15 ? 162 ASP A O   1 
ATOM   1271 C  CB  . ASP A 1 161 ? -17.656 -7.436  -2.706  1.00 21.34 ? 162 ASP A CB  1 
ATOM   1272 C  CG  . ASP A 1 161 ? -18.364 -8.797  -2.707  1.00 22.40 ? 162 ASP A CG  1 
ATOM   1273 O  OD1 . ASP A 1 161 ? -17.678 -9.837  -2.862  1.00 25.75 ? 162 ASP A OD1 1 
ATOM   1274 O  OD2 . ASP A 1 161 ? -19.604 -8.827  -2.543  1.00 26.67 ? 162 ASP A OD2 1 
ATOM   1275 N  N   . VAL A 1 162 ? -14.846 -5.477  -2.207  1.00 19.52 ? 163 VAL A N   1 
ATOM   1276 C  CA  . VAL A 1 162 ? -13.995 -4.443  -2.803  1.00 19.81 ? 163 VAL A CA  1 
ATOM   1277 C  C   . VAL A 1 162 ? -12.479 -4.723  -2.640  1.00 18.63 ? 163 VAL A C   1 
ATOM   1278 O  O   . VAL A 1 162 ? -11.616 -4.062  -3.245  1.00 17.49 ? 163 VAL A O   1 
ATOM   1279 C  CB  . VAL A 1 162 ? -14.448 -3.032  -2.266  1.00 19.45 ? 163 VAL A CB  1 
ATOM   1280 C  CG1 . VAL A 1 162 ? -13.769 -2.701  -0.941  1.00 20.31 ? 163 VAL A CG1 1 
ATOM   1281 C  CG2 . VAL A 1 162 ? -14.227 -1.924  -3.306  1.00 21.26 ? 163 VAL A CG2 1 
ATOM   1282 N  N   . LEU A 1 163 ? -12.132 -5.710  -1.807  1.00 18.45 ? 164 LEU A N   1 
ATOM   1283 C  CA  . LEU A 1 163 ? -10.721 -5.963  -1.452  1.00 17.87 ? 164 LEU A CA  1 
ATOM   1284 C  C   . LEU A 1 163 ? -9.798  -6.345  -2.623  1.00 18.29 ? 164 LEU A C   1 
ATOM   1285 O  O   . LEU A 1 163 ? -8.609  -6.047  -2.622  1.00 17.94 ? 164 LEU A O   1 
ATOM   1286 C  CB  . LEU A 1 163 ? -10.625 -7.018  -0.339  1.00 17.47 ? 164 LEU A CB  1 
ATOM   1287 C  CG  . LEU A 1 163 ? -11.295 -6.722  1.008   1.00 17.17 ? 164 LEU A CG  1 
ATOM   1288 C  CD1 . LEU A 1 163 ? -11.002 -7.884  1.978   1.00 16.86 ? 164 LEU A CD1 1 
ATOM   1289 C  CD2 . LEU A 1 163 ? -10.816 -5.404  1.594   1.00 16.29 ? 164 LEU A CD2 1 
ATOM   1290 N  N   . ASP A 1 164 ? -10.347 -7.034  -3.614  1.00 20.35 ? 165 ASP A N   1 
ATOM   1291 C  CA  . ASP A 1 164 ? -9.553  -7.376  -4.777  1.00 22.17 ? 165 ASP A CA  1 
ATOM   1292 C  C   . ASP A 1 164 ? -9.055  -6.102  -5.503  1.00 22.08 ? 165 ASP A C   1 
ATOM   1293 O  O   . ASP A 1 164 ? -8.008  -6.136  -6.146  1.00 22.93 ? 165 ASP A O   1 
ATOM   1294 C  CB  . ASP A 1 164 ? -10.345 -8.280  -5.727  1.00 23.16 ? 165 ASP A CB  1 
ATOM   1295 C  CG  . ASP A 1 164 ? -11.251 -7.498  -6.628  1.00 25.68 ? 165 ASP A CG  1 
ATOM   1296 O  OD1 . ASP A 1 164 ? -12.309 -7.022  -6.153  1.00 28.89 ? 165 ASP A OD1 1 
ATOM   1297 O  OD2 . ASP A 1 164 ? -10.887 -7.324  -7.815  1.00 28.84 ? 165 ASP A OD2 1 
ATOM   1298 N  N   . SER A 1 165 ? -9.790  -4.995  -5.348  1.00 21.57 ? 166 SER A N   1 
ATOM   1299 C  CA  . SER A 1 165 ? -9.437  -3.701  -5.959  1.00 21.47 ? 166 SER A CA  1 
ATOM   1300 C  C   . SER A 1 165 ? -8.368  -2.897  -5.186  1.00 21.11 ? 166 SER A C   1 
ATOM   1301 O  O   . SER A 1 165 ? -7.828  -1.901  -5.707  1.00 20.25 ? 166 SER A O   1 
ATOM   1302 C  CB  . SER A 1 165 ? -10.696 -2.860  -6.213  1.00 21.48 ? 166 SER A CB  1 
ATOM   1303 O  OG  . SER A 1 165 ? -11.158 -2.211  -5.039  1.00 23.65 ? 166 SER A OG  1 
ATOM   1304 N  N   . ILE A 1 166 ? -8.072  -3.317  -3.945  1.00 19.39 ? 167 ILE A N   1 
ATOM   1305 C  CA  . ILE A 1 166 ? -7.039  -2.666  -3.123  1.00 19.15 ? 167 ILE A CA  1 
ATOM   1306 C  C   . ILE A 1 166 ? -6.061  -3.725  -2.601  1.00 19.26 ? 167 ILE A C   1 
ATOM   1307 O  O   . ILE A 1 166 ? -5.686  -3.745  -1.421  1.00 18.67 ? 167 ILE A O   1 
ATOM   1308 C  CB  . ILE A 1 166 ? -7.662  -1.849  -1.943  1.00 18.86 ? 167 ILE A CB  1 
ATOM   1309 C  CG1 . ILE A 1 166 ? -8.571  -2.740  -1.095  1.00 18.16 ? 167 ILE A CG1 1 
ATOM   1310 C  CG2 . ILE A 1 166 ? -8.493  -0.655  -2.460  1.00 18.64 ? 167 ILE A CG2 1 
ATOM   1311 C  CD1 . ILE A 1 166 ? -8.781  -2.245  0.314   1.00 20.04 ? 167 ILE A CD1 1 
ATOM   1312 N  N   . LYS A 1 167 ? -5.669  -4.633  -3.490  1.00 19.69 ? 168 LYS A N   1 
ATOM   1313 C  CA  . LYS A 1 167 ? -4.857  -5.772  -3.081  1.00 19.86 ? 168 LYS A CA  1 
ATOM   1314 C  C   . LYS A 1 167 ? -3.550  -5.403  -2.375  1.00 19.49 ? 168 LYS A C   1 
ATOM   1315 O  O   . LYS A 1 167 ? -3.185  -6.048  -1.394  1.00 18.30 ? 168 LYS A O   1 
ATOM   1316 C  CB  . LYS A 1 167 ? -4.539  -6.673  -4.275  1.00 19.62 ? 168 LYS A CB  1 
ATOM   1317 C  CG  . LYS A 1 167 ? -3.684  -7.838  -3.884  1.00 20.77 ? 168 LYS A CG  1 
ATOM   1318 C  CD  . LYS A 1 167 ? -3.398  -8.770  -5.048  1.00 24.28 ? 168 LYS A CD  1 
ATOM   1319 C  CE  . LYS A 1 167 ? -2.873  -10.074 -4.493  1.00 27.94 ? 168 LYS A CE  1 
ATOM   1320 N  NZ  . LYS A 1 167 ? -2.348  -10.987 -5.563  1.00 31.42 ? 168 LYS A NZ  1 
ATOM   1321 N  N   . THR A 1 168 ? -2.866  -4.378  -2.885  1.00 19.06 ? 169 THR A N   1 
ATOM   1322 C  CA  . THR A 1 168 ? -1.506  -4.058  -2.474  1.00 19.74 ? 169 THR A CA  1 
ATOM   1323 C  C   . THR A 1 168 ? -1.407  -2.697  -1.772  1.00 19.68 ? 169 THR A C   1 
ATOM   1324 O  O   . THR A 1 168 ? -2.279  -1.841  -1.917  1.00 20.29 ? 169 THR A O   1 
ATOM   1325 C  CB  . THR A 1 168 ? -0.519  -4.108  -3.681  1.00 20.51 ? 169 THR A CB  1 
ATOM   1326 O  OG1 . THR A 1 168 ? -1.110  -3.422  -4.792  1.00 21.91 ? 169 THR A OG1 1 
ATOM   1327 C  CG2 . THR A 1 168 ? -0.202  -5.565  -4.067  1.00 21.53 ? 169 THR A CG2 1 
ATOM   1328 N  N   . LYS A 1 169 ? -0.337  -2.549  -1.004  1.00 20.97 ? 170 LYS A N   1 
ATOM   1329 C  CA  . LYS A 1 169 ? 0.008   -1.340  -0.262  1.00 22.36 ? 170 LYS A CA  1 
ATOM   1330 C  C   . LYS A 1 169 ? -0.099  -0.090  -1.128  1.00 22.86 ? 170 LYS A C   1 
ATOM   1331 O  O   . LYS A 1 169 ? 0.432   -0.055  -2.249  1.00 24.04 ? 170 LYS A O   1 
ATOM   1332 C  CB  . LYS A 1 169 ? 1.411   -1.490  0.307   1.00 21.76 ? 170 LYS A CB  1 
ATOM   1333 C  CG  . LYS A 1 169 ? 1.898   -0.317  1.174   1.00 22.78 ? 170 LYS A CG  1 
ATOM   1334 C  CD  . LYS A 1 169 ? 3.345   -0.514  1.577   1.00 26.25 ? 170 LYS A CD  1 
ATOM   1335 C  CE  . LYS A 1 169 ? 3.686   0.417   2.724   1.00 29.22 ? 170 LYS A CE  1 
ATOM   1336 N  NZ  . LYS A 1 169 ? 5.090   0.909   2.635   1.00 32.83 ? 170 LYS A NZ  1 
ATOM   1337 N  N   . GLY A 1 170 ? -0.817  0.911   -0.620  1.00 23.96 ? 171 GLY A N   1 
ATOM   1338 C  CA  . GLY A 1 170 ? -1.030  2.170   -1.341  1.00 24.09 ? 171 GLY A CA  1 
ATOM   1339 C  C   . GLY A 1 170 ? -2.280  2.249   -2.195  1.00 24.59 ? 171 GLY A C   1 
ATOM   1340 O  O   . GLY A 1 170 ? -2.713  3.347   -2.570  1.00 25.63 ? 171 GLY A O   1 
ATOM   1341 N  N   . LYS A 1 171 ? -2.898  1.114   -2.523  1.00 23.23 ? 172 LYS A N   1 
ATOM   1342 C  CA  . LYS A 1 171 ? -4.147  1.197   -3.279  1.00 23.26 ? 172 LYS A CA  1 
ATOM   1343 C  C   . LYS A 1 171 ? -5.352  1.659   -2.449  1.00 23.15 ? 172 LYS A C   1 
ATOM   1344 O  O   . LYS A 1 171 ? -5.533  1.244   -1.287  1.00 23.27 ? 172 LYS A O   1 
ATOM   1345 C  CB  . LYS A 1 171 ? -4.457  -0.107  -4.032  1.00 23.13 ? 172 LYS A CB  1 
ATOM   1346 C  CG  . LYS A 1 171 ? -3.378  -0.511  -5.025  1.00 23.65 ? 172 LYS A CG  1 
ATOM   1347 C  CD  . LYS A 1 171 ? -3.833  -1.649  -5.944  1.00 25.47 ? 172 LYS A CD  1 
ATOM   1348 C  CE  . LYS A 1 171 ? -4.768  -1.133  -7.045  1.00 29.95 ? 172 LYS A CE  1 
ATOM   1349 N  NZ  . LYS A 1 171 ? -5.333  -2.241  -7.885  1.00 31.27 ? 172 LYS A NZ  1 
ATOM   1350 N  N   . SER A 1 172 ? -6.175  2.504   -3.068  1.00 22.48 ? 173 SER A N   1 
ATOM   1351 C  CA  . SER A 1 172 ? -7.421  2.977   -2.492  1.00 22.90 ? 173 SER A CA  1 
ATOM   1352 C  C   . SER A 1 172 ? -8.570  2.888   -3.485  1.00 23.68 ? 173 SER A C   1 
ATOM   1353 O  O   . SER A 1 172 ? -8.357  2.778   -4.708  1.00 23.58 ? 173 SER A O   1 
ATOM   1354 C  CB  . SER A 1 172 ? -7.283  4.424   -1.967  1.00 23.50 ? 173 SER A CB  1 
ATOM   1355 O  OG  . SER A 1 172 ? -7.196  5.366   -3.031  1.00 23.71 ? 173 SER A OG  1 
ATOM   1356 N  N   . ALA A 1 173 ? -9.788  2.917   -2.963  1.00 24.15 ? 174 ALA A N   1 
ATOM   1357 C  CA  . ALA A 1 173 ? -10.986 2.897   -3.795  1.00 24.30 ? 174 ALA A CA  1 
ATOM   1358 C  C   . ALA A 1 173 ? -12.106 3.672   -3.122  1.00 24.88 ? 174 ALA A C   1 
ATOM   1359 O  O   . ALA A 1 173 ? -12.243 3.638   -1.898  1.00 24.25 ? 174 ALA A O   1 
ATOM   1360 C  CB  . ALA A 1 173 ? -11.419 1.462   -4.091  1.00 24.17 ? 174 ALA A CB  1 
ATOM   1361 N  N   . ASP A 1 174 ? -12.906 4.372   -3.930  1.00 24.29 ? 175 ASP A N   1 
ATOM   1362 C  CA  . ASP A 1 174 ? -14.166 4.943   -3.444  1.00 24.93 ? 175 ASP A CA  1 
ATOM   1363 C  C   . ASP A 1 174 ? -14.989 3.912   -2.718  1.00 23.88 ? 175 ASP A C   1 
ATOM   1364 O  O   . ASP A 1 174 ? -15.157 2.756   -3.171  1.00 23.14 ? 175 ASP A O   1 
ATOM   1365 C  CB  . ASP A 1 174 ? -15.026 5.492   -4.579  1.00 25.79 ? 175 ASP A CB  1 
ATOM   1366 C  CG  . ASP A 1 174 ? -14.260 6.391   -5.468  1.00 29.39 ? 175 ASP A CG  1 
ATOM   1367 O  OD1 . ASP A 1 174 ? -13.558 7.282   -4.934  1.00 32.97 ? 175 ASP A OD1 1 
ATOM   1368 O  OD2 . ASP A 1 174 ? -14.355 6.195   -6.703  1.00 35.97 ? 175 ASP A OD2 1 
ATOM   1369 N  N   . PHE A 1 175 ? -15.510 4.340   -1.579  1.00 22.28 ? 176 PHE A N   1 
ATOM   1370 C  CA  . PHE A 1 175 ? -16.287 3.449   -0.746  1.00 21.27 ? 176 PHE A CA  1 
ATOM   1371 C  C   . PHE A 1 175 ? -17.309 4.272   -0.031  1.00 21.18 ? 176 PHE A C   1 
ATOM   1372 O  O   . PHE A 1 175 ? -17.155 4.620   1.148   1.00 21.88 ? 176 PHE A O   1 
ATOM   1373 C  CB  . PHE A 1 175 ? -15.388 2.653   0.208   1.00 20.58 ? 176 PHE A CB  1 
ATOM   1374 C  CG  . PHE A 1 175 ? -16.003 1.372   0.673   1.00 20.34 ? 176 PHE A CG  1 
ATOM   1375 C  CD1 . PHE A 1 175 ? -16.269 0.340   -0.226  1.00 20.65 ? 176 PHE A CD1 1 
ATOM   1376 C  CD2 . PHE A 1 175 ? -16.298 1.179   2.016   1.00 20.64 ? 176 PHE A CD2 1 
ATOM   1377 C  CE1 . PHE A 1 175 ? -16.834 -0.873  0.234   1.00 21.45 ? 176 PHE A CE1 1 
ATOM   1378 C  CE2 . PHE A 1 175 ? -16.846 -0.006  2.471   1.00 20.65 ? 176 PHE A CE2 1 
ATOM   1379 C  CZ  . PHE A 1 175 ? -17.124 -1.033  1.581   1.00 20.28 ? 176 PHE A CZ  1 
ATOM   1380 N  N   . THR A 1 176 ? -18.356 4.618   -0.768  1.00 19.45 ? 177 THR A N   1 
ATOM   1381 C  CA  . THR A 1 176 ? -19.428 5.413   -0.223  1.00 19.07 ? 177 THR A CA  1 
ATOM   1382 C  C   . THR A 1 176 ? -20.608 4.550   0.183   1.00 18.49 ? 177 THR A C   1 
ATOM   1383 O  O   . THR A 1 176 ? -20.758 3.399   -0.295  1.00 18.56 ? 177 THR A O   1 
ATOM   1384 C  CB  . THR A 1 176 ? -19.910 6.500   -1.231  1.00 19.59 ? 177 THR A CB  1 
ATOM   1385 O  OG1 . THR A 1 176 ? -20.289 5.868   -2.456  1.00 20.60 ? 177 THR A OG1 1 
ATOM   1386 C  CG2 . THR A 1 176 ? -18.831 7.536   -1.492  1.00 19.83 ? 177 THR A CG2 1 
ATOM   1387 N  N   . ASN A 1 177 ? -21.415 5.127   1.071   1.00 17.27 ? 178 ASN A N   1 
ATOM   1388 C  CA  . ASN A 1 177 ? -22.690 4.596   1.510   1.00 17.10 ? 178 ASN A CA  1 
ATOM   1389 C  C   . ASN A 1 177 ? -22.529 3.260   2.215   1.00 16.87 ? 178 ASN A C   1 
ATOM   1390 O  O   . ASN A 1 177 ? -23.430 2.450   2.194   1.00 17.69 ? 178 ASN A O   1 
ATOM   1391 C  CB  . ASN A 1 177 ? -23.676 4.477   0.342   1.00 17.30 ? 178 ASN A CB  1 
ATOM   1392 C  CG  . ASN A 1 177 ? -23.981 5.829   -0.281  1.00 19.72 ? 178 ASN A CG  1 
ATOM   1393 O  OD1 . ASN A 1 177 ? -24.750 6.604   0.277   1.00 19.75 ? 178 ASN A OD1 1 
ATOM   1394 N  ND2 . ASN A 1 177 ? -23.322 6.137   -1.395  1.00 18.59 ? 178 ASN A ND2 1 
ATOM   1395 N  N   . PHE A 1 178 ? -21.383 3.051   2.844   1.00 16.82 ? 179 PHE A N   1 
ATOM   1396 C  CA  . PHE A 1 178 ? -21.251 1.860   3.668   1.00 16.39 ? 179 PHE A CA  1 
ATOM   1397 C  C   . PHE A 1 178 ? -21.715 2.165   5.075   1.00 15.99 ? 179 PHE A C   1 
ATOM   1398 O  O   . PHE A 1 178 ? -21.237 3.135   5.687   1.00 16.51 ? 179 PHE A O   1 
ATOM   1399 C  CB  . PHE A 1 178 ? -19.846 1.327   3.705   1.00 15.68 ? 179 PHE A CB  1 
ATOM   1400 C  CG  . PHE A 1 178 ? -19.732 0.112   4.557   1.00 15.77 ? 179 PHE A CG  1 
ATOM   1401 C  CD1 . PHE A 1 178 ? -20.207 -1.112  4.094   1.00 16.27 ? 179 PHE A CD1 1 
ATOM   1402 C  CD2 . PHE A 1 178 ? -19.263 0.207   5.861   1.00 15.32 ? 179 PHE A CD2 1 
ATOM   1403 C  CE1 . PHE A 1 178 ? -20.151 -2.247  4.898   1.00 14.71 ? 179 PHE A CE1 1 
ATOM   1404 C  CE2 . PHE A 1 178 ? -19.215 -0.923  6.682   1.00 17.35 ? 179 PHE A CE2 1 
ATOM   1405 C  CZ  . PHE A 1 178 ? -19.659 -2.154  6.201   1.00 16.17 ? 179 PHE A CZ  1 
ATOM   1406 N  N   . ASP A 1 179 ? -22.580 1.294   5.587   1.00 16.29 ? 180 ASP A N   1 
ATOM   1407 C  CA  . ASP A 1 179 ? -23.238 1.472   6.869   1.00 15.89 ? 180 ASP A CA  1 
ATOM   1408 C  C   . ASP A 1 179 ? -22.579 0.612   7.949   1.00 15.43 ? 180 ASP A C   1 
ATOM   1409 O  O   . ASP A 1 179 ? -22.790 -0.620  7.972   1.00 13.99 ? 180 ASP A O   1 
ATOM   1410 C  CB  . ASP A 1 179 ? -24.706 1.082   6.742   1.00 16.96 ? 180 ASP A CB  1 
ATOM   1411 C  CG  . ASP A 1 179 ? -25.544 1.519   7.932   1.00 19.32 ? 180 ASP A CG  1 
ATOM   1412 O  OD1 . ASP A 1 179 ? -25.002 1.805   9.038   1.00 16.92 ? 180 ASP A OD1 1 
ATOM   1413 O  OD2 . ASP A 1 179 ? -26.777 1.598   7.756   1.00 24.51 ? 180 ASP A OD2 1 
ATOM   1414 N  N   . PRO A 1 180 ? -21.805 1.248   8.864   1.00 14.15 ? 181 PRO A N   1 
ATOM   1415 C  CA  . PRO A 1 180 ? -21.093 0.424   9.863   1.00 14.13 ? 181 PRO A CA  1 
ATOM   1416 C  C   . PRO A 1 180 ? -22.019 -0.244  10.888  1.00 13.38 ? 181 PRO A C   1 
ATOM   1417 O  O   . PRO A 1 180 ? -21.579 -1.148  11.614  1.00 11.86 ? 181 PRO A O   1 
ATOM   1418 C  CB  . PRO A 1 180 ? -20.116 1.416   10.508  1.00 14.72 ? 181 PRO A CB  1 
ATOM   1419 C  CG  . PRO A 1 180 ? -20.812 2.749   10.397  1.00 14.93 ? 181 PRO A CG  1 
ATOM   1420 C  CD  . PRO A 1 180 ? -21.527 2.689   9.045   1.00 15.26 ? 181 PRO A CD  1 
ATOM   1421 N  N   . ARG A 1 181 ? -23.297 0.154   10.932  1.00 12.12 ? 182 ARG A N   1 
ATOM   1422 C  CA  . ARG A 1 181 ? -24.250 -0.526  11.845  1.00 13.76 ? 182 ARG A CA  1 
ATOM   1423 C  C   . ARG A 1 181 ? -24.396 -2.022  11.501  1.00 13.94 ? 182 ARG A C   1 
ATOM   1424 O  O   . ARG A 1 181 ? -24.783 -2.820  12.349  1.00 14.15 ? 182 ARG A O   1 
ATOM   1425 C  CB  . ARG A 1 181 ? -25.621 0.183   11.863  1.00 13.11 ? 182 ARG A CB  1 
ATOM   1426 C  CG  . ARG A 1 181 ? -25.539 1.620   12.381  1.00 14.03 ? 182 ARG A CG  1 
ATOM   1427 C  CD  . ARG A 1 181 ? -26.908 2.296   12.308  1.00 15.38 ? 182 ARG A CD  1 
ATOM   1428 N  NE  . ARG A 1 181 ? -27.306 2.438   10.916  1.00 19.06 ? 182 ARG A NE  1 
ATOM   1429 C  CZ  . ARG A 1 181 ? -28.388 3.092   10.511  1.00 21.05 ? 182 ARG A CZ  1 
ATOM   1430 N  NH1 . ARG A 1 181 ? -29.170 3.668   11.403  1.00 20.98 ? 182 ARG A NH1 1 
ATOM   1431 N  NH2 . ARG A 1 181 ? -28.664 3.178   9.219   1.00 21.48 ? 182 ARG A NH2 1 
ATOM   1432 N  N   . GLY A 1 182 ? -24.058 -2.392  10.266  1.00 14.55 ? 183 GLY A N   1 
ATOM   1433 C  CA  . GLY A 1 182 ? -24.124 -3.790  9.844   1.00 15.46 ? 183 GLY A CA  1 
ATOM   1434 C  C   . GLY A 1 182 ? -22.964 -4.640  10.344  1.00 15.58 ? 183 GLY A C   1 
ATOM   1435 O  O   . GLY A 1 182 ? -22.855 -5.821  9.982   1.00 16.95 ? 183 GLY A O   1 
ATOM   1436 N  N   . LEU A 1 183 ? -22.078 -4.035  11.138  1.00 14.50 ? 184 LEU A N   1 
ATOM   1437 C  CA  . LEU A 1 183 ? -20.933 -4.765  11.703  1.00 14.37 ? 184 LEU A CA  1 
ATOM   1438 C  C   . LEU A 1 183 ? -21.088 -4.987  13.205  1.00 14.05 ? 184 LEU A C   1 
ATOM   1439 O  O   . LEU A 1 183 ? -20.188 -5.550  13.848  1.00 15.86 ? 184 LEU A O   1 
ATOM   1440 C  CB  . LEU A 1 183 ? -19.626 -4.007  11.445  1.00 13.40 ? 184 LEU A CB  1 
ATOM   1441 C  CG  . LEU A 1 183 ? -19.325 -3.794  9.951   1.00 15.93 ? 184 LEU A CG  1 
ATOM   1442 C  CD1 . LEU A 1 183 ? -18.091 -2.929  9.766   1.00 17.63 ? 184 LEU A CD1 1 
ATOM   1443 C  CD2 . LEU A 1 183 ? -19.239 -5.109  9.186   1.00 18.12 ? 184 LEU A CD2 1 
ATOM   1444 N  N   . LEU A 1 184 ? -22.200 -4.531  13.775  1.00 13.60 ? 185 LEU A N   1 
ATOM   1445 C  CA  . LEU A 1 184 ? -22.372 -4.551  15.242  1.00 12.88 ? 185 LEU A CA  1 
ATOM   1446 C  C   . LEU A 1 184 ? -23.135 -5.767  15.729  1.00 14.15 ? 185 LEU A C   1 
ATOM   1447 O  O   . LEU A 1 184 ? -24.182 -6.116  15.159  1.00 16.07 ? 185 LEU A O   1 
ATOM   1448 C  CB  . LEU A 1 184 ? -23.107 -3.295  15.753  1.00 12.66 ? 185 LEU A CB  1 
ATOM   1449 C  CG  . LEU A 1 184 ? -22.527 -1.939  15.340  1.00 11.65 ? 185 LEU A CG  1 
ATOM   1450 C  CD1 . LEU A 1 184 ? -23.423 -0.787  15.799  1.00 13.73 ? 185 LEU A CD1 1 
ATOM   1451 C  CD2 . LEU A 1 184 ? -21.044 -1.724  15.787  1.00 14.10 ? 185 LEU A CD2 1 
ATOM   1452 N  N   . PRO A 1 185 ? -22.683 -6.366  16.841  1.00 13.97 ? 186 PRO A N   1 
ATOM   1453 C  CA  . PRO A 1 185 ? -23.453 -7.493  17.332  1.00 13.81 ? 186 PRO A CA  1 
ATOM   1454 C  C   . PRO A 1 185 ? -24.755 -6.972  17.989  1.00 14.37 ? 186 PRO A C   1 
ATOM   1455 O  O   . PRO A 1 185 ? -24.979 -5.755  18.123  1.00 15.09 ? 186 PRO A O   1 
ATOM   1456 C  CB  . PRO A 1 185 ? -22.536 -8.107  18.402  1.00 13.11 ? 186 PRO A CB  1 
ATOM   1457 C  CG  . PRO A 1 185 ? -21.825 -6.918  18.978  1.00 11.85 ? 186 PRO A CG  1 
ATOM   1458 C  CD  . PRO A 1 185 ? -21.572 -6.000  17.749  1.00 12.06 ? 186 PRO A CD  1 
ATOM   1459 N  N   . GLU A 1 186 ? -25.591 -7.882  18.452  1.00 15.31 ? 187 GLU A N   1 
ATOM   1460 C  CA  . GLU A 1 186 ? -26.823 -7.469  19.082  1.00 16.32 ? 187 GLU A CA  1 
ATOM   1461 C  C   . GLU A 1 186 ? -26.628 -6.720  20.434  1.00 15.70 ? 187 GLU A C   1 
ATOM   1462 O  O   . GLU A 1 186 ? -27.247 -5.679  20.668  1.00 16.70 ? 187 GLU A O   1 
ATOM   1463 C  CB  . GLU A 1 186 ? -27.738 -8.702  19.168  1.00 16.80 ? 187 GLU A CB  1 
ATOM   1464 C  CG  . GLU A 1 186 ? -28.482 -8.867  20.428  1.00 19.81 ? 187 GLU A CG  1 
ATOM   1465 C  CD  . GLU A 1 186 ? -29.278 -10.191 20.474  1.00 18.75 ? 187 GLU A CD  1 
ATOM   1466 O  OE1 . GLU A 1 186 ? -29.220 -10.976 19.508  1.00 21.69 ? 187 GLU A OE1 1 
ATOM   1467 O  OE2 . GLU A 1 186 ? -29.996 -10.384 21.475  1.00 28.26 ? 187 GLU A OE2 1 
ATOM   1468 N  N   . SER A 1 187 ? -25.759 -7.221  21.312  1.00 14.11 ? 188 SER A N   1 
ATOM   1469 C  CA  . SER A 1 187 ? -25.566 -6.620  22.622  1.00 14.43 ? 188 SER A CA  1 
ATOM   1470 C  C   . SER A 1 187 ? -24.438 -5.580  22.590  1.00 14.17 ? 188 SER A C   1 
ATOM   1471 O  O   . SER A 1 187 ? -23.434 -5.788  21.919  1.00 15.13 ? 188 SER A O   1 
ATOM   1472 C  CB  . SER A 1 187 ? -25.224 -7.679  23.659  1.00 14.56 ? 188 SER A CB  1 
ATOM   1473 O  OG  . SER A 1 187 ? -24.886 -7.096  24.908  1.00 15.04 ? 188 SER A OG  1 
ATOM   1474 N  N   . LEU A 1 188 ? -24.614 -4.499  23.331  1.00 13.76 ? 189 LEU A N   1 
ATOM   1475 C  CA  . LEU A 1 188 ? -23.518 -3.530  23.551  1.00 14.84 ? 189 LEU A CA  1 
ATOM   1476 C  C   . LEU A 1 188 ? -22.833 -3.650  24.928  1.00 14.61 ? 189 LEU A C   1 
ATOM   1477 O  O   . LEU A 1 188 ? -22.163 -2.708  25.367  1.00 15.58 ? 189 LEU A O   1 
ATOM   1478 C  CB  . LEU A 1 188 ? -23.984 -2.078  23.255  1.00 14.40 ? 189 LEU A CB  1 
ATOM   1479 C  CG  . LEU A 1 188 ? -24.483 -1.730  21.837  1.00 17.02 ? 189 LEU A CG  1 
ATOM   1480 C  CD1 . LEU A 1 188 ? -24.921 -0.244  21.748  1.00 18.90 ? 189 LEU A CD1 1 
ATOM   1481 C  CD2 . LEU A 1 188 ? -23.428 -2.089  20.765  1.00 17.76 ? 189 LEU A CD2 1 
ATOM   1482 N  N   . ASP A 1 189 ? -22.990 -4.788  25.612  1.00 14.47 ? 190 ASP A N   1 
ATOM   1483 C  CA  . ASP A 1 189 ? -22.222 -5.061  26.837  1.00 14.19 ? 190 ASP A CA  1 
ATOM   1484 C  C   . ASP A 1 189 ? -20.722 -4.993  26.489  1.00 13.32 ? 190 ASP A C   1 
ATOM   1485 O  O   . ASP A 1 189 ? -20.293 -5.440  25.400  1.00 12.53 ? 190 ASP A O   1 
ATOM   1486 C  CB  . ASP A 1 189 ? -22.554 -6.419  27.452  1.00 14.17 ? 190 ASP A CB  1 
ATOM   1487 C  CG  . ASP A 1 189 ? -23.971 -6.476  28.074  1.00 17.15 ? 190 ASP A CG  1 
ATOM   1488 O  OD1 . ASP A 1 189 ? -24.635 -5.435  28.197  1.00 20.07 ? 190 ASP A OD1 1 
ATOM   1489 O  OD2 . ASP A 1 189 ? -24.401 -7.589  28.407  1.00 22.31 ? 190 ASP A OD2 1 
ATOM   1490 N  N   . TYR A 1 190 ? -19.957 -4.342  27.368  1.00 12.67 ? 191 TYR A N   1 
ATOM   1491 C  CA  . TYR A 1 190 ? -18.550 -4.062  27.050  1.00 11.90 ? 191 TYR A CA  1 
ATOM   1492 C  C   . TYR A 1 190 ? -17.623 -4.138  28.276  1.00 11.76 ? 191 TYR A C   1 
ATOM   1493 O  O   . TYR A 1 190 ? -18.061 -3.985  29.420  1.00 11.10 ? 191 TYR A O   1 
ATOM   1494 C  CB  . TYR A 1 190 ? -18.431 -2.683  26.390  1.00 12.24 ? 191 TYR A CB  1 
ATOM   1495 C  CG  . TYR A 1 190 ? -18.843 -1.528  27.283  1.00 11.15 ? 191 TYR A CG  1 
ATOM   1496 C  CD1 . TYR A 1 190 ? -17.914 -0.899  28.126  1.00 13.11 ? 191 TYR A CD1 1 
ATOM   1497 C  CD2 . TYR A 1 190 ? -20.164 -1.044  27.271  1.00 12.62 ? 191 TYR A CD2 1 
ATOM   1498 C  CE1 . TYR A 1 190 ? -18.307 0.172   28.968  1.00 13.15 ? 191 TYR A CE1 1 
ATOM   1499 C  CE2 . TYR A 1 190 ? -20.562 0.034   28.089  1.00 15.33 ? 191 TYR A CE2 1 
ATOM   1500 C  CZ  . TYR A 1 190 ? -19.626 0.625   28.943  1.00 14.96 ? 191 TYR A CZ  1 
ATOM   1501 O  OH  . TYR A 1 190 ? -20.005 1.664   29.752  1.00 13.80 ? 191 TYR A OH  1 
ATOM   1502 N  N   . TRP A 1 191 ? -16.344 -4.391  28.016  1.00 10.74 ? 192 TRP A N   1 
ATOM   1503 C  CA  . TRP A 1 191 ? -15.268 -4.111  28.966  1.00 10.25 ? 192 TRP A CA  1 
ATOM   1504 C  C   . TRP A 1 191 ? -14.582 -2.810  28.554  1.00 9.56  ? 192 TRP A C   1 
ATOM   1505 O  O   . TRP A 1 191 ? -14.623 -2.428  27.381  1.00 9.75  ? 192 TRP A O   1 
ATOM   1506 C  CB  . TRP A 1 191 ? -14.218 -5.226  28.956  1.00 10.31 ? 192 TRP A CB  1 
ATOM   1507 C  CG  . TRP A 1 191 ? -14.725 -6.587  29.370  1.00 11.84 ? 192 TRP A CG  1 
ATOM   1508 C  CD1 . TRP A 1 191 ? -14.983 -7.023  30.641  1.00 11.62 ? 192 TRP A CD1 1 
ATOM   1509 C  CD2 . TRP A 1 191 ? -14.984 -7.698  28.499  1.00 11.22 ? 192 TRP A CD2 1 
ATOM   1510 N  NE1 . TRP A 1 191 ? -15.404 -8.350  30.609  1.00 12.04 ? 192 TRP A NE1 1 
ATOM   1511 C  CE2 . TRP A 1 191 ? -15.419 -8.778  29.306  1.00 13.05 ? 192 TRP A CE2 1 
ATOM   1512 C  CE3 . TRP A 1 191 ? -14.889 -7.885  27.117  1.00 10.28 ? 192 TRP A CE3 1 
ATOM   1513 C  CZ2 . TRP A 1 191 ? -15.754 -10.040 28.756  1.00 11.06 ? 192 TRP A CZ2 1 
ATOM   1514 C  CZ3 . TRP A 1 191 ? -15.217 -9.125  26.575  1.00 10.80 ? 192 TRP A CZ3 1 
ATOM   1515 C  CH2 . TRP A 1 191 ? -15.626 -10.191 27.397  1.00 12.36 ? 192 TRP A CH2 1 
ATOM   1516 N  N   . THR A 1 192 ? -13.973 -2.119  29.513  1.00 8.68  ? 193 THR A N   1 
ATOM   1517 C  CA  . THR A 1 192 ? -13.285 -0.851  29.200  1.00 9.98  ? 193 THR A CA  1 
ATOM   1518 C  C   . THR A 1 192 ? -12.060 -0.667  30.087  1.00 9.71  ? 193 THR A C   1 
ATOM   1519 O  O   . THR A 1 192 ? -12.057 -1.072  31.262  1.00 11.27 ? 193 THR A O   1 
ATOM   1520 C  CB  . THR A 1 192 ? -14.238 0.403   29.281  1.00 9.77  ? 193 THR A CB  1 
ATOM   1521 O  OG1 . THR A 1 192 ? -13.558 1.601   28.869  1.00 11.26 ? 193 THR A OG1 1 
ATOM   1522 C  CG2 . THR A 1 192 ? -14.798 0.623   30.724  1.00 10.90 ? 193 THR A CG2 1 
ATOM   1523 N  N   . TYR A 1 193 ? -11.026 -0.065  29.504  1.00 9.88  ? 194 TYR A N   1 
ATOM   1524 C  CA  . TYR A 1 193 ? -9.776  0.173   30.208  1.00 9.89  ? 194 TYR A CA  1 
ATOM   1525 C  C   . TYR A 1 193 ? -8.994  1.217   29.383  1.00 9.86  ? 194 TYR A C   1 
ATOM   1526 O  O   . TYR A 1 193 ? -9.270  1.372   28.177  1.00 8.93  ? 194 TYR A O   1 
ATOM   1527 C  CB  . TYR A 1 193 ? -8.966  -1.137  30.372  1.00 9.88  ? 194 TYR A CB  1 
ATOM   1528 C  CG  . TYR A 1 193 ? -8.251  -1.559  29.100  1.00 11.50 ? 194 TYR A CG  1 
ATOM   1529 C  CD1 . TYR A 1 193 ? -8.910  -2.331  28.123  1.00 8.69  ? 194 TYR A CD1 1 
ATOM   1530 C  CD2 . TYR A 1 193 ? -6.941  -1.161  28.864  1.00 11.00 ? 194 TYR A CD2 1 
ATOM   1531 C  CE1 . TYR A 1 193 ? -8.261  -2.699  26.936  1.00 7.35  ? 194 TYR A CE1 1 
ATOM   1532 C  CE2 . TYR A 1 193 ? -6.272  -1.488  27.667  1.00 11.00 ? 194 TYR A CE2 1 
ATOM   1533 C  CZ  . TYR A 1 193 ? -6.942  -2.267  26.715  1.00 9.69  ? 194 TYR A CZ  1 
ATOM   1534 O  OH  . TYR A 1 193 ? -6.300  -2.589  25.561  1.00 9.90  ? 194 TYR A OH  1 
ATOM   1535 N  N   . PRO A 1 194 ? -8.083  1.950   30.040  1.00 10.20 ? 195 PRO A N   1 
ATOM   1536 C  CA  . PRO A 1 194 ? -7.193  2.936   29.397  1.00 10.06 ? 195 PRO A CA  1 
ATOM   1537 C  C   . PRO A 1 194 ? -6.011  2.268   28.725  1.00 9.91  ? 195 PRO A C   1 
ATOM   1538 O  O   . PRO A 1 194 ? -5.319  1.475   29.359  1.00 9.23  ? 195 PRO A O   1 
ATOM   1539 C  CB  . PRO A 1 194 ? -6.688  3.810   30.584  1.00 11.36 ? 195 PRO A CB  1 
ATOM   1540 C  CG  . PRO A 1 194 ? -6.805  2.944   31.763  1.00 10.68 ? 195 PRO A CG  1 
ATOM   1541 C  CD  . PRO A 1 194 ? -7.871  1.893   31.498  1.00 10.77 ? 195 PRO A CD  1 
ATOM   1542 N  N   . GLY A 1 195 ? -5.809  2.544   27.434  1.00 9.80  ? 196 GLY A N   1 
ATOM   1543 C  CA  . GLY A 1 195 ? -4.703  1.892   26.709  1.00 9.72  ? 196 GLY A CA  1 
ATOM   1544 C  C   . GLY A 1 195 ? -4.125  2.780   25.633  1.00 9.83  ? 196 GLY A C   1 
ATOM   1545 O  O   . GLY A 1 195 ? -4.076  4.021   25.769  1.00 9.12  ? 196 GLY A O   1 
ATOM   1546 N  N   . SER A 1 196 ? -3.707  2.144   24.546  1.00 9.57  ? 197 SER A N   1 
ATOM   1547 C  CA  . SER A 1 196 ? -2.926  2.812   23.514  1.00 9.12  ? 197 SER A CA  1 
ATOM   1548 C  C   . SER A 1 196 ? -3.377  2.416   22.115  1.00 8.85  ? 197 SER A C   1 
ATOM   1549 O  O   . SER A 1 196 ? -4.129  1.457   21.942  1.00 10.00 ? 197 SER A O   1 
ATOM   1550 C  CB  . SER A 1 196 ? -1.457  2.404   23.661  1.00 9.04  ? 197 SER A CB  1 
ATOM   1551 O  OG  . SER A 1 196 ? -1.296  1.041   23.232  1.00 8.09  ? 197 SER A OG  1 
ATOM   1552 N  N   . LEU A 1 197 ? -2.860  3.118   21.106  1.00 8.67  ? 198 LEU A N   1 
ATOM   1553 C  CA  . LEU A 1 197 ? -2.927  2.601   19.738  1.00 9.18  ? 198 LEU A CA  1 
ATOM   1554 C  C   . LEU A 1 197 ? -2.166  1.272   19.746  1.00 9.63  ? 198 LEU A C   1 
ATOM   1555 O  O   . LEU A 1 197 ? -1.157  1.134   20.455  1.00 10.67 ? 198 LEU A O   1 
ATOM   1556 C  CB  . LEU A 1 197 ? -2.284  3.602   18.787  1.00 9.93  ? 198 LEU A CB  1 
ATOM   1557 C  CG  . LEU A 1 197 ? -2.876  5.007   18.633  1.00 12.45 ? 198 LEU A CG  1 
ATOM   1558 C  CD1 . LEU A 1 197 ? -1.943  5.815   17.725  1.00 15.16 ? 198 LEU A CD1 1 
ATOM   1559 C  CD2 . LEU A 1 197 ? -4.283  4.982   18.056  1.00 15.35 ? 198 LEU A CD2 1 
ATOM   1560 N  N   . THR A 1 198 ? -2.620  0.297   18.967  1.00 8.95  ? 199 THR A N   1 
ATOM   1561 C  CA  . THR A 1 198 ? -1.924  -0.998  18.927  1.00 9.41  ? 199 THR A CA  1 
ATOM   1562 C  C   . THR A 1 198 ? -0.906  -1.118  17.790  1.00 9.79  ? 199 THR A C   1 
ATOM   1563 O  O   . THR A 1 198 ? -0.329  -2.201  17.609  1.00 10.40 ? 199 THR A O   1 
ATOM   1564 C  CB  . THR A 1 198 ? -2.915  -2.183  18.786  1.00 9.06  ? 199 THR A CB  1 
ATOM   1565 O  OG1 . THR A 1 198 ? -3.561  -2.114  17.518  1.00 8.75  ? 199 THR A OG1 1 
ATOM   1566 C  CG2 . THR A 1 198 ? -3.912  -2.190  19.937  1.00 9.55  ? 199 THR A CG2 1 
ATOM   1567 N  N   . THR A 1 199 ? -0.749  -0.048  17.001  1.00 11.29 ? 200 THR A N   1 
ATOM   1568 C  CA  . THR A 1 199 ? 0.327   0.033   16.007  1.00 11.80 ? 200 THR A CA  1 
ATOM   1569 C  C   . THR A 1 199 ? 1.133   1.277   16.290  1.00 11.09 ? 200 THR A C   1 
ATOM   1570 O  O   . THR A 1 199 ? 0.610   2.245   16.852  1.00 10.13 ? 200 THR A O   1 
ATOM   1571 C  CB  . THR A 1 199 ? -0.167  0.158   14.537  1.00 12.67 ? 200 THR A CB  1 
ATOM   1572 O  OG1 . THR A 1 199 ? -1.020  1.309   14.371  1.00 15.31 ? 200 THR A OG1 1 
ATOM   1573 C  CG2 . THR A 1 199 ? -0.924  -1.088  14.093  1.00 12.71 ? 200 THR A CG2 1 
ATOM   1574 N  N   . PRO A 1 200 ? 2.386   1.283   15.826  1.00 11.36 ? 201 PRO A N   1 
ATOM   1575 C  CA  . PRO A 1 200 ? 3.109   2.550   15.928  1.00 11.11 ? 201 PRO A CA  1 
ATOM   1576 C  C   . PRO A 1 200 ? 2.260   3.733   15.392  1.00 10.89 ? 201 PRO A C   1 
ATOM   1577 O  O   . PRO A 1 200 ? 1.593   3.620   14.328  1.00 11.53 ? 201 PRO A O   1 
ATOM   1578 C  CB  . PRO A 1 200 ? 4.349   2.301   15.053  1.00 10.34 ? 201 PRO A CB  1 
ATOM   1579 C  CG  . PRO A 1 200 ? 4.593   0.857   15.134  1.00 11.01 ? 201 PRO A CG  1 
ATOM   1580 C  CD  . PRO A 1 200 ? 3.199   0.215   15.214  1.00 11.03 ? 201 PRO A CD  1 
ATOM   1581 N  N   . PRO A 1 201 ? 2.334   4.904   16.048  1.00 11.60 ? 202 PRO A N   1 
ATOM   1582 C  CA  . PRO A 1 201 ? 3.227   5.316   17.154  1.00 11.87 ? 202 PRO A CA  1 
ATOM   1583 C  C   . PRO A 1 201 ? 2.887   4.847   18.581  1.00 10.45 ? 202 PRO A C   1 
ATOM   1584 O  O   . PRO A 1 201 ? 3.551   5.278   19.539  1.00 10.52 ? 202 PRO A O   1 
ATOM   1585 C  CB  . PRO A 1 201 ? 3.197   6.855   17.064  1.00 12.64 ? 202 PRO A CB  1 
ATOM   1586 C  CG  . PRO A 1 201 ? 1.858   7.175   16.527  1.00 12.91 ? 202 PRO A CG  1 
ATOM   1587 C  CD  . PRO A 1 201 ? 1.483   6.028   15.586  1.00 12.38 ? 202 PRO A CD  1 
ATOM   1588 N  N   . LEU A 1 202 ? 1.885   3.958   18.724  1.00 10.35 ? 203 LEU A N   1 
ATOM   1589 C  CA  . LEU A 1 202 ? 1.584   3.322   20.015  1.00 9.08  ? 203 LEU A CA  1 
ATOM   1590 C  C   . LEU A 1 202 ? 1.209   4.329   21.130  1.00 8.52  ? 203 LEU A C   1 
ATOM   1591 O  O   . LEU A 1 202 ? 1.405   4.076   22.321  1.00 8.96  ? 203 LEU A O   1 
ATOM   1592 C  CB  . LEU A 1 202 ? 2.764   2.441   20.471  1.00 10.14 ? 203 LEU A CB  1 
ATOM   1593 C  CG  . LEU A 1 202 ? 3.140   1.291   19.534  1.00 9.97  ? 203 LEU A CG  1 
ATOM   1594 C  CD1 . LEU A 1 202 ? 4.418   0.636   20.085  1.00 8.99  ? 203 LEU A CD1 1 
ATOM   1595 C  CD2 . LEU A 1 202 ? 1.982   0.259   19.417  1.00 9.65  ? 203 LEU A CD2 1 
ATOM   1596 N  N   . LEU A 1 203 ? 0.646   5.457   20.717  1.00 9.74  ? 204 LEU A N   1 
ATOM   1597 C  CA  . LEU A 1 203 ? 0.374   6.567   21.637  1.00 10.85 ? 204 LEU A CA  1 
ATOM   1598 C  C   . LEU A 1 203 ? -0.648  6.150   22.687  1.00 10.72 ? 204 LEU A C   1 
ATOM   1599 O  O   . LEU A 1 203 ? -1.605  5.419   22.382  1.00 10.69 ? 204 LEU A O   1 
ATOM   1600 C  CB  . LEU A 1 203 ? -0.082  7.826   20.868  1.00 9.81  ? 204 LEU A CB  1 
ATOM   1601 C  CG  . LEU A 1 203 ? 1.007   8.407   19.932  1.00 12.71 ? 204 LEU A CG  1 
ATOM   1602 C  CD1 . LEU A 1 203 ? 0.435   9.478   19.042  1.00 16.76 ? 204 LEU A CD1 1 
ATOM   1603 C  CD2 . LEU A 1 203 ? 2.216   8.955   20.767  1.00 15.97 ? 204 LEU A CD2 1 
ATOM   1604 N  N   . GLU A 1 204 ? -0.433  6.606   23.921  1.00 10.28 ? 205 GLU A N   1 
ATOM   1605 C  CA  . GLU A 1 204 ? -1.277  6.208   25.033  1.00 10.44 ? 205 GLU A CA  1 
ATOM   1606 C  C   . GLU A 1 204 ? -2.484  7.148   25.173  1.00 10.33 ? 205 GLU A C   1 
ATOM   1607 O  O   . GLU A 1 204 ? -2.619  7.905   26.156  1.00 9.99  ? 205 GLU A O   1 
ATOM   1608 C  CB  . GLU A 1 204 ? -0.436  6.063   26.314  1.00 11.33 ? 205 GLU A CB  1 
ATOM   1609 C  CG  . GLU A 1 204 ? 0.485   4.824   26.151  1.00 12.16 ? 205 GLU A CG  1 
ATOM   1610 C  CD  . GLU A 1 204 ? 1.428   4.599   27.318  1.00 14.00 ? 205 GLU A CD  1 
ATOM   1611 O  OE1 . GLU A 1 204 ? 1.720   5.567   28.064  1.00 16.98 ? 205 GLU A OE1 1 
ATOM   1612 O  OE2 . GLU A 1 204 ? 1.862   3.456   27.487  1.00 12.91 ? 205 GLU A OE2 1 
ATOM   1613 N  N   . CYS A 1 205 ? -3.350  7.102   24.170  1.00 9.27  ? 206 CYS A N   1 
ATOM   1614 C  CA  . CYS A 1 205 ? -4.428  8.127   24.014  1.00 9.24  ? 206 CYS A CA  1 
ATOM   1615 C  C   . CYS A 1 205 ? -5.810  7.483   23.907  1.00 9.12  ? 206 CYS A C   1 
ATOM   1616 O  O   . CYS A 1 205 ? -6.784  8.144   23.559  1.00 10.15 ? 206 CYS A O   1 
ATOM   1617 C  CB  . CYS A 1 205 ? -4.144  8.950   22.763  1.00 9.93  ? 206 CYS A CB  1 
ATOM   1618 S  SG  . CYS A 1 205 ? -4.098  7.932   21.230  1.00 11.53 ? 206 CYS A SG  1 
ATOM   1619 N  N   . VAL A 1 206 ? -5.880  6.174   24.157  1.00 8.75  ? 207 VAL A N   1 
ATOM   1620 C  CA  . VAL A 1 206 ? -7.113  5.402   23.860  1.00 8.31  ? 207 VAL A CA  1 
ATOM   1621 C  C   . VAL A 1 206 ? -7.932  4.967   25.087  1.00 8.17  ? 207 VAL A C   1 
ATOM   1622 O  O   . VAL A 1 206 ? -7.418  4.320   25.988  1.00 9.61  ? 207 VAL A O   1 
ATOM   1623 C  CB  . VAL A 1 206 ? -6.829  4.134   23.000  1.00 8.74  ? 207 VAL A CB  1 
ATOM   1624 C  CG1 . VAL A 1 206 ? -8.199  3.418   22.696  1.00 8.34  ? 207 VAL A CG1 1 
ATOM   1625 C  CG2 . VAL A 1 206 ? -6.128  4.488   21.680  1.00 11.64 ? 207 VAL A CG2 1 
ATOM   1626 N  N   . THR A 1 207 ? -9.221  5.301   25.097  1.00 8.32  ? 208 THR A N   1 
ATOM   1627 C  CA  . THR A 1 207 ? -10.150 4.596   25.969  1.00 8.23  ? 208 THR A CA  1 
ATOM   1628 C  C   . THR A 1 207 ? -10.663 3.412   25.174  1.00 8.37  ? 208 THR A C   1 
ATOM   1629 O  O   . THR A 1 207 ? -11.370 3.587   24.166  1.00 9.06  ? 208 THR A O   1 
ATOM   1630 C  CB  . THR A 1 207 ? -11.317 5.486   26.461  1.00 8.76  ? 208 THR A CB  1 
ATOM   1631 O  OG1 . THR A 1 207 ? -10.781 6.612   27.203  1.00 9.43  ? 208 THR A OG1 1 
ATOM   1632 C  CG2 . THR A 1 207 ? -12.247 4.656   27.336  1.00 7.87  ? 208 THR A CG2 1 
ATOM   1633 N  N   . TRP A 1 208 ? -10.288 2.217   25.603  1.00 8.51  ? 209 TRP A N   1 
ATOM   1634 C  CA  . TRP A 1 208 ? -10.735 1.007   24.906  1.00 7.94  ? 209 TRP A CA  1 
ATOM   1635 C  C   . TRP A 1 208 ? -12.129 0.573   25.393  1.00 8.52  ? 209 TRP A C   1 
ATOM   1636 O  O   . TRP A 1 208 ? -12.365 0.486   26.590  1.00 8.69  ? 209 TRP A O   1 
ATOM   1637 C  CB  . TRP A 1 208 ? -9.715  -0.129  25.092  1.00 7.95  ? 209 TRP A CB  1 
ATOM   1638 C  CG  . TRP A 1 208 ? -8.632  -0.001  24.103  1.00 7.74  ? 209 TRP A CG  1 
ATOM   1639 C  CD1 . TRP A 1 208 ? -7.382  0.583   24.275  1.00 8.33  ? 209 TRP A CD1 1 
ATOM   1640 C  CD2 . TRP A 1 208 ? -8.706  -0.403  22.730  1.00 9.20  ? 209 TRP A CD2 1 
ATOM   1641 N  NE1 . TRP A 1 208 ? -6.685  0.563   23.087  1.00 8.74  ? 209 TRP A NE1 1 
ATOM   1642 C  CE2 . TRP A 1 208 ? -7.460  -0.052  22.122  1.00 7.61  ? 209 TRP A CE2 1 
ATOM   1643 C  CE3 . TRP A 1 208 ? -9.710  -1.008  21.948  1.00 6.42  ? 209 TRP A CE3 1 
ATOM   1644 C  CZ2 . TRP A 1 208 ? -7.189  -0.301  20.787  1.00 7.19  ? 209 TRP A CZ2 1 
ATOM   1645 C  CZ3 . TRP A 1 208 ? -9.444  -1.281  20.627  1.00 8.58  ? 209 TRP A CZ3 1 
ATOM   1646 C  CH2 . TRP A 1 208 ? -8.175  -0.945  20.051  1.00 7.47  ? 209 TRP A CH2 1 
ATOM   1647 N  N   . ILE A 1 209 ? -13.021 0.328   24.444  1.00 8.80  ? 210 ILE A N   1 
ATOM   1648 C  CA  . ILE A 1 209 ? -14.326 -0.230  24.739  1.00 9.34  ? 210 ILE A CA  1 
ATOM   1649 C  C   . ILE A 1 209 ? -14.436 -1.516  23.904  1.00 9.72  ? 210 ILE A C   1 
ATOM   1650 O  O   . ILE A 1 209 ? -14.558 -1.451  22.699  1.00 10.49 ? 210 ILE A O   1 
ATOM   1651 C  CB  . ILE A 1 209 ? -15.435 0.797   24.395  1.00 9.57  ? 210 ILE A CB  1 
ATOM   1652 C  CG1 . ILE A 1 209 ? -15.195 2.108   25.178  1.00 10.15 ? 210 ILE A CG1 1 
ATOM   1653 C  CG2 . ILE A 1 209 ? -16.833 0.188   24.687  1.00 10.23 ? 210 ILE A CG2 1 
ATOM   1654 C  CD1 . ILE A 1 209 ? -15.912 3.336   24.573  1.00 11.90 ? 210 ILE A CD1 1 
ATOM   1655 N  N   . VAL A 1 210 ? -14.398 -2.673  24.553  1.00 9.85  ? 211 VAL A N   1 
ATOM   1656 C  CA  . VAL A 1 210 ? -14.375 -3.955  23.849  1.00 8.88  ? 211 VAL A CA  1 
ATOM   1657 C  C   . VAL A 1 210 ? -15.687 -4.675  24.128  1.00 8.71  ? 211 VAL A C   1 
ATOM   1658 O  O   . VAL A 1 210 ? -16.019 -4.925  25.283  1.00 9.54  ? 211 VAL A O   1 
ATOM   1659 C  CB  . VAL A 1 210 ? -13.136 -4.821  24.299  1.00 8.39  ? 211 VAL A CB  1 
ATOM   1660 C  CG1 . VAL A 1 210 ? -13.110 -6.168  23.561  1.00 8.06  ? 211 VAL A CG1 1 
ATOM   1661 C  CG2 . VAL A 1 210 ? -11.784 -4.042  24.065  1.00 7.56  ? 211 VAL A CG2 1 
ATOM   1662 N  N   . LEU A 1 211 ? -16.456 -4.913  23.076  1.00 9.48  ? 212 LEU A N   1 
ATOM   1663 C  CA  . LEU A 1 211 ? -17.736 -5.624  23.201  1.00 9.62  ? 212 LEU A CA  1 
ATOM   1664 C  C   . LEU A 1 211 ? -17.548 -7.082  23.597  1.00 9.92  ? 212 LEU A C   1 
ATOM   1665 O  O   . LEU A 1 211 ? -16.656 -7.756  23.084  1.00 9.68  ? 212 LEU A O   1 
ATOM   1666 C  CB  . LEU A 1 211 ? -18.533 -5.528  21.891  1.00 9.68  ? 212 LEU A CB  1 
ATOM   1667 C  CG  . LEU A 1 211 ? -18.941 -4.104  21.453  1.00 10.52 ? 212 LEU A CG  1 
ATOM   1668 C  CD1 . LEU A 1 211 ? -20.002 -4.186  20.306  1.00 10.46 ? 212 LEU A CD1 1 
ATOM   1669 C  CD2 . LEU A 1 211 ? -19.469 -3.215  22.650  1.00 8.88  ? 212 LEU A CD2 1 
ATOM   1670 N  N   . LYS A 1 212 ? -18.401 -7.573  24.510  1.00 11.43 ? 213 LYS A N   1 
ATOM   1671 C  CA  . LYS A 1 212 ? -18.353 -8.973  24.960  1.00 12.69 ? 213 LYS A CA  1 
ATOM   1672 C  C   . LYS A 1 212 ? -18.833 -9.935  23.865  1.00 12.34 ? 213 LYS A C   1 
ATOM   1673 O  O   . LYS A 1 212 ? -18.301 -11.040 23.734  1.00 12.64 ? 213 LYS A O   1 
ATOM   1674 C  CB  . LYS A 1 212 ? -19.145 -9.142  26.288  1.00 14.05 ? 213 LYS A CB  1 
ATOM   1675 C  CG  . LYS A 1 212 ? -19.478 -10.585 26.733  1.00 17.01 ? 213 LYS A CG  1 
ATOM   1676 C  CD  . LYS A 1 212 ? -20.602 -10.611 27.792  1.00 17.58 ? 213 LYS A CD  1 
ATOM   1677 C  CE  . LYS A 1 212 ? -22.065 -10.489 27.203  1.00 22.35 ? 213 LYS A CE  1 
ATOM   1678 N  NZ  . LYS A 1 212 ? -22.347 -9.668  25.928  1.00 25.41 ? 213 LYS A NZ  1 
ATOM   1679 N  N   . GLU A 1 213 ? -19.837 -9.512  23.101  1.00 11.79 ? 214 GLU A N   1 
ATOM   1680 C  CA  . GLU A 1 213 ? -20.430 -10.371 22.067  1.00 11.80 ? 214 GLU A CA  1 
ATOM   1681 C  C   . GLU A 1 213 ? -19.671 -10.260 20.748  1.00 10.75 ? 214 GLU A C   1 
ATOM   1682 O  O   . GLU A 1 213 ? -19.675 -9.189  20.121  1.00 11.10 ? 214 GLU A O   1 
ATOM   1683 C  CB  . GLU A 1 213 ? -21.909 -10.029 21.830  1.00 12.31 ? 214 GLU A CB  1 
ATOM   1684 C  CG  . GLU A 1 213 ? -22.517 -10.886 20.704  1.00 14.38 ? 214 GLU A CG  1 
ATOM   1685 C  CD  . GLU A 1 213 ? -24.044 -10.795 20.607  1.00 15.01 ? 214 GLU A CD  1 
ATOM   1686 O  OE1 . GLU A 1 213 ? -24.653 -10.009 21.338  1.00 14.07 ? 214 GLU A OE1 1 
ATOM   1687 O  OE2 . GLU A 1 213 ? -24.619 -11.558 19.796  1.00 21.88 ? 214 GLU A OE2 1 
ATOM   1688 N  N   . PRO A 1 214 ? -19.065 -11.373 20.286  1.00 11.88 ? 215 PRO A N   1 
ATOM   1689 C  CA  . PRO A 1 214 ? -18.431 -11.355 18.971  1.00 12.37 ? 215 PRO A CA  1 
ATOM   1690 C  C   . PRO A 1 214 ? -19.490 -11.368 17.860  1.00 12.55 ? 215 PRO A C   1 
ATOM   1691 O  O   . PRO A 1 214 ? -20.666 -11.762 18.102  1.00 13.97 ? 215 PRO A O   1 
ATOM   1692 C  CB  . PRO A 1 214 ? -17.602 -12.657 18.934  1.00 12.19 ? 215 PRO A CB  1 
ATOM   1693 C  CG  . PRO A 1 214 ? -18.272 -13.560 19.889  1.00 15.65 ? 215 PRO A CG  1 
ATOM   1694 C  CD  . PRO A 1 214 ? -19.015 -12.703 20.920  1.00 11.92 ? 215 PRO A CD  1 
ATOM   1695 N  N   . ILE A 1 215 ? -19.097 -10.901 16.679  1.00 11.14 ? 216 ILE A N   1 
ATOM   1696 C  CA  . ILE A 1 215 ? -19.877 -11.144 15.471  1.00 11.65 ? 216 ILE A CA  1 
ATOM   1697 C  C   . ILE A 1 215 ? -19.373 -12.389 14.749  1.00 11.84 ? 216 ILE A C   1 
ATOM   1698 O  O   . ILE A 1 215 ? -18.206 -12.756 14.868  1.00 12.07 ? 216 ILE A O   1 
ATOM   1699 C  CB  . ILE A 1 215 ? -19.944 -9.898  14.502  1.00 10.61 ? 216 ILE A CB  1 
ATOM   1700 C  CG1 . ILE A 1 215 ? -18.524 -9.511  13.991  1.00 10.21 ? 216 ILE A CG1 1 
ATOM   1701 C  CG2 . ILE A 1 215 ? -20.686 -8.679  15.224  1.00 13.13 ? 216 ILE A CG2 1 
ATOM   1702 C  CD1 . ILE A 1 215 ? -18.527 -8.526  12.736  1.00 11.31 ? 216 ILE A CD1 1 
ATOM   1703 N  N   . SER A 1 216 ? -20.270 -13.061 14.023  1.00 13.26 ? 217 SER A N   1 
ATOM   1704 C  CA  . SER A 1 216 ? -19.836 -14.184 13.180  1.00 14.43 ? 217 SER A CA  1 
ATOM   1705 C  C   . SER A 1 216 ? -19.635 -13.735 11.744  1.00 13.95 ? 217 SER A C   1 
ATOM   1706 O  O   . SER A 1 216 ? -20.442 -12.977 11.202  1.00 14.43 ? 217 SER A O   1 
ATOM   1707 C  CB  . SER A 1 216 ? -20.829 -15.347 13.207  1.00 15.83 ? 217 SER A CB  1 
ATOM   1708 O  OG  . SER A 1 216 ? -20.936 -15.861 14.524  1.00 20.24 ? 217 SER A OG  1 
ATOM   1709 N  N   . VAL A 1 217 ? -18.540 -14.199 11.162  1.00 13.72 ? 218 VAL A N   1 
ATOM   1710 C  CA  . VAL A 1 217 ? -18.220 -14.004 9.757   1.00 13.42 ? 218 VAL A CA  1 
ATOM   1711 C  C   . VAL A 1 217 ? -17.922 -15.377 9.164   1.00 13.34 ? 218 VAL A C   1 
ATOM   1712 O  O   . VAL A 1 217 ? -17.481 -16.292 9.882   1.00 13.74 ? 218 VAL A O   1 
ATOM   1713 C  CB  . VAL A 1 217 ? -17.017 -13.019 9.528   1.00 13.60 ? 218 VAL A CB  1 
ATOM   1714 C  CG1 . VAL A 1 217 ? -17.348 -11.659 10.139  1.00 12.46 ? 218 VAL A CG1 1 
ATOM   1715 C  CG2 . VAL A 1 217 ? -15.708 -13.598 10.101  1.00 12.65 ? 218 VAL A CG2 1 
ATOM   1716 N  N   . SER A 1 218 ? -18.182 -15.537 7.875   1.00 13.40 ? 219 SER A N   1 
ATOM   1717 C  CA  . SER A 1 218 ? -17.976 -16.835 7.238   1.00 13.08 ? 219 SER A CA  1 
ATOM   1718 C  C   . SER A 1 218 ? -16.492 -17.089 6.970   1.00 13.08 ? 219 SER A C   1 
ATOM   1719 O  O   . SER A 1 218 ? -15.662 -16.149 6.911   1.00 11.17 ? 219 SER A O   1 
ATOM   1720 C  CB  . SER A 1 218 ? -18.785 -16.956 5.936   1.00 12.69 ? 219 SER A CB  1 
ATOM   1721 O  OG  . SER A 1 218 ? -18.218 -16.142 4.928   1.00 14.36 ? 219 SER A OG  1 
ATOM   1722 N  N   A SER A 1 219 ? -16.146 -18.362 6.809   0.50 12.77 ? 220 SER A N   1 
ATOM   1723 N  N   B SER A 1 219 ? -16.149 -18.365 6.797   0.50 13.05 ? 220 SER A N   1 
ATOM   1724 C  CA  A SER A 1 219 ? -14.800 -18.732 6.416   0.50 13.25 ? 220 SER A CA  1 
ATOM   1725 C  CA  B SER A 1 219 ? -14.802 -18.741 6.405   0.50 13.87 ? 220 SER A CA  1 
ATOM   1726 C  C   A SER A 1 219 ? -14.415 -18.026 5.110   0.50 13.73 ? 220 SER A C   1 
ATOM   1727 C  C   B SER A 1 219 ? -14.416 -18.023 5.110   0.50 14.04 ? 220 SER A C   1 
ATOM   1728 O  O   A SER A 1 219 ? -13.294 -17.524 4.989   0.50 13.53 ? 220 SER A O   1 
ATOM   1729 O  O   B SER A 1 219 ? -13.297 -17.515 4.994   0.50 13.84 ? 220 SER A O   1 
ATOM   1730 C  CB  A SER A 1 219 ? -14.689 -20.254 6.289   0.50 13.50 ? 220 SER A CB  1 
ATOM   1731 C  CB  B SER A 1 219 ? -14.687 -20.263 6.249   0.50 14.21 ? 220 SER A CB  1 
ATOM   1732 O  OG  A SER A 1 219 ? -15.684 -20.755 5.427   0.50 12.24 ? 220 SER A OG  1 
ATOM   1733 O  OG  B SER A 1 219 ? -13.322 -20.657 6.223   0.50 15.34 ? 220 SER A OG  1 
ATOM   1734 N  N   . GLU A 1 220 ? -15.360 -17.920 4.168   1.00 13.97 ? 221 GLU A N   1 
ATOM   1735 C  CA  . GLU A 1 220 ? -15.089 -17.279 2.866   1.00 14.33 ? 221 GLU A CA  1 
ATOM   1736 C  C   . GLU A 1 220 ? -14.790 -15.780 3.006   1.00 13.88 ? 221 GLU A C   1 
ATOM   1737 O  O   . GLU A 1 220 ? -13.923 -15.245 2.306   1.00 13.44 ? 221 GLU A O   1 
ATOM   1738 C  CB  . GLU A 1 220 ? -16.233 -17.481 1.884   1.00 15.29 ? 221 GLU A CB  1 
ATOM   1739 C  CG  . GLU A 1 220 ? -16.479 -18.964 1.533   1.00 18.52 ? 221 GLU A CG  1 
ATOM   1740 C  CD  . GLU A 1 220 ? -17.654 -19.589 2.309   1.00 22.53 ? 221 GLU A CD  1 
ATOM   1741 O  OE1 . GLU A 1 220 ? -18.010 -19.150 3.423   1.00 21.70 ? 221 GLU A OE1 1 
ATOM   1742 O  OE2 . GLU A 1 220 ? -18.243 -20.558 1.789   1.00 28.22 ? 221 GLU A OE2 1 
ATOM   1743 N  N   . GLN A 1 221 ? -15.490 -15.134 3.936   1.00 13.38 ? 222 GLN A N   1 
ATOM   1744 C  CA  . GLN A 1 221 ? -15.252 -13.705 4.216   1.00 14.14 ? 222 GLN A CA  1 
ATOM   1745 C  C   . GLN A 1 221 ? -13.830 -13.494 4.742   1.00 14.34 ? 222 GLN A C   1 
ATOM   1746 O  O   . GLN A 1 221 ? -13.093 -12.645 4.233   1.00 13.10 ? 222 GLN A O   1 
ATOM   1747 C  CB  . GLN A 1 221 ? -16.312 -13.175 5.188   1.00 13.80 ? 222 GLN A CB  1 
ATOM   1748 C  CG  . GLN A 1 221 ? -17.665 -12.970 4.456   1.00 14.07 ? 222 GLN A CG  1 
ATOM   1749 C  CD  . GLN A 1 221 ? -18.752 -12.447 5.341   1.00 13.90 ? 222 GLN A CD  1 
ATOM   1750 O  OE1 . GLN A 1 221 ? -18.874 -12.851 6.503   1.00 13.89 ? 222 GLN A OE1 1 
ATOM   1751 N  NE2 . GLN A 1 221 ? -19.590 -11.575 4.788   1.00 12.62 ? 222 GLN A NE2 1 
ATOM   1752 N  N   . VAL A 1 222 ? -13.424 -14.303 5.726   1.00 13.82 ? 223 VAL A N   1 
ATOM   1753 C  CA  . VAL A 1 222 ? -12.107 -14.108 6.335   1.00 14.89 ? 223 VAL A CA  1 
ATOM   1754 C  C   . VAL A 1 222 ? -11.006 -14.551 5.346   1.00 15.17 ? 223 VAL A C   1 
ATOM   1755 O  O   . VAL A 1 222 ? -9.932  -13.959 5.294   1.00 14.36 ? 223 VAL A O   1 
ATOM   1756 C  CB  . VAL A 1 222 ? -11.973 -14.761 7.750   1.00 15.72 ? 223 VAL A CB  1 
ATOM   1757 C  CG1 . VAL A 1 222 ? -12.052 -16.260 7.686   1.00 16.96 ? 223 VAL A CG1 1 
ATOM   1758 C  CG2 . VAL A 1 222 ? -10.629 -14.343 8.391   1.00 15.82 ? 223 VAL A CG2 1 
ATOM   1759 N  N   . LEU A 1 223 ? -11.316 -15.550 4.519   1.00 15.37 ? 224 LEU A N   1 
ATOM   1760 C  CA  . LEU A 1 223 ? -10.362 -15.966 3.491   1.00 16.43 ? 224 LEU A CA  1 
ATOM   1761 C  C   . LEU A 1 223 ? -9.980  -14.830 2.575   1.00 16.03 ? 224 LEU A C   1 
ATOM   1762 O  O   . LEU A 1 223 ? -8.794  -14.688 2.236   1.00 16.56 ? 224 LEU A O   1 
ATOM   1763 C  CB  . LEU A 1 223 ? -10.872 -17.164 2.692   1.00 17.29 ? 224 LEU A CB  1 
ATOM   1764 C  CG  . LEU A 1 223 ? -10.613 -18.467 3.455   1.00 20.65 ? 224 LEU A CG  1 
ATOM   1765 C  CD1 . LEU A 1 223 ? -11.508 -19.615 2.905   1.00 24.36 ? 224 LEU A CD1 1 
ATOM   1766 C  CD2 . LEU A 1 223 ? -9.129  -18.827 3.419   1.00 23.63 ? 224 LEU A CD2 1 
ATOM   1767 N  N   A LYS A 1 224 ? -10.979 -14.039 2.179   0.50 15.15 ? 225 LYS A N   1 
ATOM   1768 N  N   B LYS A 1 224 ? -10.958 -14.006 2.209   0.50 15.27 ? 225 LYS A N   1 
ATOM   1769 C  CA  A LYS A 1 224 ? -10.768 -12.853 1.358   0.50 15.78 ? 225 LYS A CA  1 
ATOM   1770 C  CA  B LYS A 1 224 ? -10.731 -12.856 1.337   0.50 15.86 ? 225 LYS A CA  1 
ATOM   1771 C  C   A LYS A 1 224 ? -9.800  -11.854 2.008   0.50 14.99 ? 225 LYS A C   1 
ATOM   1772 C  C   B LYS A 1 224 ? -9.929  -11.698 1.975   0.50 15.21 ? 225 LYS A C   1 
ATOM   1773 O  O   A LYS A 1 224 ? -8.887  -11.364 1.329   0.50 14.73 ? 225 LYS A O   1 
ATOM   1774 O  O   B LYS A 1 224 ? -9.267  -10.935 1.257   0.50 15.25 ? 225 LYS A O   1 
ATOM   1775 C  CB  A LYS A 1 224 ? -12.097 -12.186 0.968   0.50 15.33 ? 225 LYS A CB  1 
ATOM   1776 C  CB  B LYS A 1 224 ? -12.055 -12.393 0.721   0.50 15.84 ? 225 LYS A CB  1 
ATOM   1777 C  CG  A LYS A 1 224 ? -12.868 -12.931 -0.145  0.50 17.81 ? 225 LYS A CG  1 
ATOM   1778 C  CG  B LYS A 1 224 ? -12.573 -13.370 -0.369  0.50 16.46 ? 225 LYS A CG  1 
ATOM   1779 C  CD  A LYS A 1 224 ? -13.424 -11.954 -1.181  0.50 19.33 ? 225 LYS A CD  1 
ATOM   1780 C  CD  B LYS A 1 224 ? -14.048 -13.146 -0.643  0.50 17.20 ? 225 LYS A CD  1 
ATOM   1781 C  CE  A LYS A 1 224 ? -14.479 -12.601 -2.074  0.50 20.62 ? 225 LYS A CE  1 
ATOM   1782 C  CE  B LYS A 1 224 ? -14.566 -13.950 -1.831  0.50 18.00 ? 225 LYS A CE  1 
ATOM   1783 N  NZ  A LYS A 1 224 ? -14.726 -11.870 -3.357  0.50 20.95 ? 225 LYS A NZ  1 
ATOM   1784 N  NZ  B LYS A 1 224 ? -14.640 -15.398 -1.571  0.50 19.01 ? 225 LYS A NZ  1 
ATOM   1785 N  N   . PHE A 1 225 ? -9.988  -11.568 3.309   1.00 14.90 ? 226 PHE A N   1 
ATOM   1786 C  CA  . PHE A 1 225 ? -9.034  -10.716 4.075   1.00 14.13 ? 226 PHE A CA  1 
ATOM   1787 C  C   . PHE A 1 225 ? -7.605  -11.212 3.854   1.00 14.22 ? 226 PHE A C   1 
ATOM   1788 O  O   . PHE A 1 225 ? -6.677  -10.427 3.682   1.00 13.21 ? 226 PHE A O   1 
ATOM   1789 C  CB  . PHE A 1 225 ? -9.264  -10.811 5.600   1.00 14.62 ? 226 PHE A CB  1 
ATOM   1790 C  CG  . PHE A 1 225 ? -10.423 -9.978  6.156   1.00 13.97 ? 226 PHE A CG  1 
ATOM   1791 C  CD1 . PHE A 1 225 ? -11.477 -9.529  5.370   1.00 15.39 ? 226 PHE A CD1 1 
ATOM   1792 C  CD2 . PHE A 1 225 ? -10.480 -9.761  7.552   1.00 14.40 ? 226 PHE A CD2 1 
ATOM   1793 C  CE1 . PHE A 1 225 ? -12.528 -8.795  5.945   1.00 15.00 ? 226 PHE A CE1 1 
ATOM   1794 C  CE2 . PHE A 1 225 ? -11.516 -9.063  8.138   1.00 17.46 ? 226 PHE A CE2 1 
ATOM   1795 C  CZ  . PHE A 1 225 ? -12.545 -8.553  7.329   1.00 17.03 ? 226 PHE A CZ  1 
ATOM   1796 N  N   . ARG A 1 226 ? -7.426  -12.532 3.895   1.00 14.00 ? 227 ARG A N   1 
ATOM   1797 C  CA  . ARG A 1 226 ? -6.095  -13.163 3.804   1.00 15.40 ? 227 ARG A CA  1 
ATOM   1798 C  C   . ARG A 1 226 ? -5.475  -13.128 2.399   1.00 15.44 ? 227 ARG A C   1 
ATOM   1799 O  O   . ARG A 1 226 ? -4.340  -13.550 2.229   1.00 17.03 ? 227 ARG A O   1 
ATOM   1800 C  CB  . ARG A 1 226 ? -6.137  -14.613 4.319   1.00 15.22 ? 227 ARG A CB  1 
ATOM   1801 C  CG  . ARG A 1 226 ? -6.561  -14.746 5.773   1.00 14.60 ? 227 ARG A CG  1 
ATOM   1802 C  CD  . ARG A 1 226 ? -6.490  -16.197 6.299   1.00 15.27 ? 227 ARG A CD  1 
ATOM   1803 N  NE  . ARG A 1 226 ? -7.077  -16.262 7.648   1.00 16.35 ? 227 ARG A NE  1 
ATOM   1804 C  CZ  . ARG A 1 226 ? -8.012  -17.134 8.032   1.00 17.09 ? 227 ARG A CZ  1 
ATOM   1805 N  NH1 . ARG A 1 226 ? -8.429  -18.098 7.195   1.00 17.88 ? 227 ARG A NH1 1 
ATOM   1806 N  NH2 . ARG A 1 226 ? -8.489  -17.079 9.272   1.00 16.33 ? 227 ARG A NH2 1 
ATOM   1807 N  N   . LYS A 1 227 ? -6.230  -12.649 1.411   1.00 16.36 ? 228 LYS A N   1 
ATOM   1808 C  CA  . LYS A 1 227 ? -5.733  -12.524 0.026   1.00 17.00 ? 228 LYS A CA  1 
ATOM   1809 C  C   . LYS A 1 227 ? -5.048  -11.189 -0.229  1.00 17.21 ? 228 LYS A C   1 
ATOM   1810 O  O   . LYS A 1 227 ? -4.319  -11.003 -1.213  1.00 16.76 ? 228 LYS A O   1 
ATOM   1811 C  CB  . LYS A 1 227 ? -6.887  -12.729 -0.949  1.00 17.32 ? 228 LYS A CB  1 
ATOM   1812 C  CG  . LYS A 1 227 ? -7.339  -14.174 -0.969  1.00 20.20 ? 228 LYS A CG  1 
ATOM   1813 C  CD  . LYS A 1 227 ? -8.409  -14.400 -2.020  1.00 26.20 ? 228 LYS A CD  1 
ATOM   1814 C  CE  . LYS A 1 227 ? -7.790  -14.942 -3.287  1.00 30.63 ? 228 LYS A CE  1 
ATOM   1815 N  NZ  . LYS A 1 227 ? -7.041  -16.199 -2.977  1.00 31.79 ? 228 LYS A NZ  1 
ATOM   1816 N  N   . LEU A 1 228 ? -5.261  -10.260 0.693   1.00 16.48 ? 229 LEU A N   1 
ATOM   1817 C  CA  . LEU A 1 228 ? -4.575  -8.992  0.634   1.00 16.45 ? 229 LEU A CA  1 
ATOM   1818 C  C   . LEU A 1 228 ? -3.069  -9.120  0.781   1.00 16.56 ? 229 LEU A C   1 
ATOM   1819 O  O   . LEU A 1 228 ? -2.549  -10.122 1.268   1.00 16.22 ? 229 LEU A O   1 
ATOM   1820 C  CB  . LEU A 1 228 ? -5.102  -8.083  1.731   1.00 15.12 ? 229 LEU A CB  1 
ATOM   1821 C  CG  . LEU A 1 228 ? -6.485  -7.493  1.491   1.00 15.07 ? 229 LEU A CG  1 
ATOM   1822 C  CD1 . LEU A 1 228 ? -6.994  -6.917  2.769   1.00 15.78 ? 229 LEU A CD1 1 
ATOM   1823 C  CD2 . LEU A 1 228 ? -6.454  -6.409  0.394   1.00 14.68 ? 229 LEU A CD2 1 
ATOM   1824 N  N   . ASN A 1 229 ? -2.369  -8.059  0.395   1.00 17.67 ? 230 ASN A N   1 
ATOM   1825 C  CA  . ASN A 1 229 ? -0.917  -8.032  0.411   1.00 18.19 ? 230 ASN A CA  1 
ATOM   1826 C  C   . ASN A 1 229 ? -0.386  -6.872  1.277   1.00 18.17 ? 230 ASN A C   1 
ATOM   1827 O  O   . ASN A 1 229 ? -0.889  -5.760  1.201   1.00 18.21 ? 230 ASN A O   1 
ATOM   1828 C  CB  . ASN A 1 229 ? -0.397  -7.845  -1.025  1.00 18.38 ? 230 ASN A CB  1 
ATOM   1829 C  CG  . ASN A 1 229 ? -0.538  -9.098  -1.905  1.00 20.01 ? 230 ASN A CG  1 
ATOM   1830 O  OD1 . ASN A 1 229 ? -1.123  -10.132 -1.523  1.00 20.51 ? 230 ASN A OD1 1 
ATOM   1831 N  ND2 . ASN A 1 229 ? 0.022   -9.000  -3.111  1.00 19.25 ? 230 ASN A ND2 1 
ATOM   1832 N  N   . PHE A 1 230 ? 0.630   -7.155  2.082   1.00 18.80 ? 231 PHE A N   1 
ATOM   1833 C  CA  . PHE A 1 230 ? 1.431   -6.148  2.805   1.00 19.51 ? 231 PHE A CA  1 
ATOM   1834 C  C   . PHE A 1 230 ? 2.300   -5.323  1.838   1.00 20.81 ? 231 PHE A C   1 
ATOM   1835 O  O   . PHE A 1 230 ? 2.559   -4.141  2.082   1.00 20.15 ? 231 PHE A O   1 
ATOM   1836 C  CB  . PHE A 1 230 ? 2.437   -6.837  3.718   1.00 19.52 ? 231 PHE A CB  1 
ATOM   1837 C  CG  . PHE A 1 230 ? 1.876   -7.374  5.021   1.00 19.94 ? 231 PHE A CG  1 
ATOM   1838 C  CD1 . PHE A 1 230 ? 1.079   -6.574  5.858   1.00 19.00 ? 231 PHE A CD1 1 
ATOM   1839 C  CD2 . PHE A 1 230 ? 2.231   -8.665  5.445   1.00 18.47 ? 231 PHE A CD2 1 
ATOM   1840 C  CE1 . PHE A 1 230 ? 0.594   -7.074  7.093   1.00 20.81 ? 231 PHE A CE1 1 
ATOM   1841 C  CE2 . PHE A 1 230 ? 1.768   -9.179  6.669   1.00 18.95 ? 231 PHE A CE2 1 
ATOM   1842 C  CZ  . PHE A 1 230 ? 0.951   -8.382  7.494   1.00 17.17 ? 231 PHE A CZ  1 
ATOM   1843 N  N   . ASN A 1 231 ? 2.793   -6.000  0.797   1.00 21.22 ? 232 ASN A N   1 
ATOM   1844 C  CA  . ASN A 1 231 ? 3.652   -5.388  -0.235  1.00 22.04 ? 232 ASN A CA  1 
ATOM   1845 C  C   . ASN A 1 231 ? 2.897   -4.491  -1.196  1.00 22.21 ? 232 ASN A C   1 
ATOM   1846 O  O   . ASN A 1 231 ? 1.678   -4.640  -1.368  1.00 21.12 ? 232 ASN A O   1 
ATOM   1847 C  CB  . ASN A 1 231 ? 4.340   -6.477  -1.056  1.00 22.18 ? 232 ASN A CB  1 
ATOM   1848 C  CG  . ASN A 1 231 ? 3.354   -7.430  -1.703  1.00 23.09 ? 232 ASN A CG  1 
ATOM   1849 O  OD1 . ASN A 1 231 ? 2.925   -8.396  -1.081  1.00 26.38 ? 232 ASN A OD1 1 
ATOM   1850 N  ND2 . ASN A 1 231 ? 3.001   -7.172  -2.962  1.00 23.52 ? 232 ASN A ND2 1 
ATOM   1851 N  N   . GLY A 1 232 ? 3.637   -3.588  -1.849  1.00 22.79 ? 233 GLY A N   1 
ATOM   1852 C  CA  . GLY A 1 232 ? 3.081   -2.759  -2.928  1.00 24.27 ? 233 GLY A CA  1 
ATOM   1853 C  C   . GLY A 1 232 ? 3.050   -3.512  -4.250  1.00 25.55 ? 233 GLY A C   1 
ATOM   1854 O  O   . GLY A 1 232 ? 3.748   -4.511  -4.417  1.00 25.75 ? 233 GLY A O   1 
ATOM   1855 N  N   . GLU A 1 233 ? 2.241   -3.023  -5.185  1.00 26.46 ? 234 GLU A N   1 
ATOM   1856 C  CA  . GLU A 1 233 ? 2.105   -3.635  -6.505  1.00 27.96 ? 234 GLU A CA  1 
ATOM   1857 C  C   . GLU A 1 233 ? 3.459   -3.749  -7.207  1.00 28.20 ? 234 GLU A C   1 
ATOM   1858 O  O   . GLU A 1 233 ? 4.277   -2.835  -7.155  1.00 27.79 ? 234 GLU A O   1 
ATOM   1859 C  CB  . GLU A 1 233 ? 1.132   -2.839  -7.371  1.00 27.50 ? 234 GLU A CB  1 
ATOM   1860 C  CG  . GLU A 1 233 ? 0.810   -3.480  -8.720  1.00 27.88 ? 234 GLU A CG  1 
ATOM   1861 C  CD  . GLU A 1 233 ? -0.048  -2.596  -9.595  1.00 29.31 ? 234 GLU A CD  1 
ATOM   1862 O  OE1 . GLU A 1 233 ? -0.381  -1.451  -9.170  1.00 30.88 ? 234 GLU A OE1 1 
ATOM   1863 O  OE2 . GLU A 1 233 ? -0.373  -3.036  -10.721 1.00 30.75 ? 234 GLU A OE2 1 
ATOM   1864 N  N   . GLY A 1 234 ? 3.691   -4.898  -7.831  1.00 29.15 ? 235 GLY A N   1 
ATOM   1865 C  CA  . GLY A 1 234 ? 4.958   -5.162  -8.485  1.00 30.11 ? 235 GLY A CA  1 
ATOM   1866 C  C   . GLY A 1 234 ? 6.073   -5.493  -7.516  1.00 30.54 ? 235 GLY A C   1 
ATOM   1867 O  O   . GLY A 1 234 ? 7.247   -5.288  -7.820  1.00 30.55 ? 235 GLY A O   1 
ATOM   1868 N  N   . GLU A 1 235 ? 5.705   -6.004  -6.342  1.00 30.86 ? 236 GLU A N   1 
ATOM   1869 C  CA  . GLU A 1 235 ? 6.687   -6.512  -5.381  1.00 30.95 ? 236 GLU A CA  1 
ATOM   1870 C  C   . GLU A 1 235 ? 6.393   -7.978  -5.071  1.00 30.68 ? 236 GLU A C   1 
ATOM   1871 O  O   . GLU A 1 235 ? 5.327   -8.487  -5.453  1.00 31.07 ? 236 GLU A O   1 
ATOM   1872 C  CB  . GLU A 1 235 ? 6.705   -5.661  -4.110  1.00 31.85 ? 236 GLU A CB  1 
ATOM   1873 C  CG  . GLU A 1 235 ? 7.244   -4.260  -4.355  1.00 33.77 ? 236 GLU A CG  1 
ATOM   1874 C  CD  . GLU A 1 235 ? 7.514   -3.489  -3.078  1.00 38.06 ? 236 GLU A CD  1 
ATOM   1875 O  OE1 . GLU A 1 235 ? 8.309   -3.974  -2.235  1.00 41.05 ? 236 GLU A OE1 1 
ATOM   1876 O  OE2 . GLU A 1 235 ? 6.941   -2.384  -2.931  1.00 38.42 ? 236 GLU A OE2 1 
ATOM   1877 N  N   . PRO A 1 236 ? 7.353   -8.684  -4.441  1.00 29.68 ? 237 PRO A N   1 
ATOM   1878 C  CA  . PRO A 1 236 ? 7.112   -10.080 -4.060  1.00 29.14 ? 237 PRO A CA  1 
ATOM   1879 C  C   . PRO A 1 236 ? 5.898   -10.155 -3.136  1.00 27.89 ? 237 PRO A C   1 
ATOM   1880 O  O   . PRO A 1 236 ? 5.706   -9.279  -2.297  1.00 27.15 ? 237 PRO A O   1 
ATOM   1881 C  CB  . PRO A 1 236 ? 8.381   -10.462 -3.305  1.00 29.62 ? 237 PRO A CB  1 
ATOM   1882 C  CG  . PRO A 1 236 ? 9.420   -9.524  -3.799  1.00 29.67 ? 237 PRO A CG  1 
ATOM   1883 C  CD  . PRO A 1 236 ? 8.710   -8.241  -4.073  1.00 30.15 ? 237 PRO A CD  1 
ATOM   1884 N  N   . GLU A 1 237 ? 5.063   -11.166 -3.332  1.00 26.40 ? 238 GLU A N   1 
ATOM   1885 C  CA  . GLU A 1 237 ? 3.851   -11.263 -2.558  1.00 24.65 ? 238 GLU A CA  1 
ATOM   1886 C  C   . GLU A 1 237 ? 4.136   -11.729 -1.126  1.00 23.50 ? 238 GLU A C   1 
ATOM   1887 O  O   . GLU A 1 237 ? 4.719   -12.780 -0.901  1.00 22.41 ? 238 GLU A O   1 
ATOM   1888 C  CB  . GLU A 1 237 ? 2.805   -12.152 -3.241  1.00 24.67 ? 238 GLU A CB  1 
ATOM   1889 C  CG  . GLU A 1 237 ? 1.464   -12.091 -2.534  1.00 23.60 ? 238 GLU A CG  1 
ATOM   1890 C  CD  . GLU A 1 237 ? 0.367   -12.860 -3.234  1.00 25.28 ? 238 GLU A CD  1 
ATOM   1891 O  OE1 . GLU A 1 237 ? 0.634   -13.988 -3.718  1.00 26.77 ? 238 GLU A OE1 1 
ATOM   1892 O  OE2 . GLU A 1 237 ? -0.774  -12.351 -3.291  1.00 20.19 ? 238 GLU A OE2 1 
ATOM   1893 N  N   . GLU A 1 238 ? 3.718   -10.895 -0.177  1.00 22.77 ? 239 GLU A N   1 
ATOM   1894 C  CA  . GLU A 1 238 ? 3.658   -11.244 1.235   1.00 22.84 ? 239 GLU A CA  1 
ATOM   1895 C  C   . GLU A 1 238 ? 2.182   -11.111 1.629   1.00 20.19 ? 239 GLU A C   1 
ATOM   1896 O  O   . GLU A 1 238 ? 1.616   -10.024 1.562   1.00 19.11 ? 239 GLU A O   1 
ATOM   1897 C  CB  . GLU A 1 238 ? 4.555   -10.326 2.093   1.00 22.41 ? 239 GLU A CB  1 
ATOM   1898 C  CG  . GLU A 1 238 ? 4.640   -8.870  1.622   1.00 27.25 ? 239 GLU A CG  1 
ATOM   1899 C  CD  . GLU A 1 238 ? 5.714   -8.016  2.332   1.00 26.57 ? 239 GLU A CD  1 
ATOM   1900 O  OE1 . GLU A 1 238 ? 5.817   -8.033  3.586   1.00 30.14 ? 239 GLU A OE1 1 
ATOM   1901 O  OE2 . GLU A 1 238 ? 6.446   -7.298  1.609   1.00 32.74 ? 239 GLU A OE2 1 
ATOM   1902 N  N   . LEU A 1 239 ? 1.533   -12.228 1.948   1.00 18.35 ? 240 LEU A N   1 
ATOM   1903 C  CA  . LEU A 1 239 ? 0.118   -12.131 2.310   1.00 16.31 ? 240 LEU A CA  1 
ATOM   1904 C  C   . LEU A 1 239 ? -0.053  -11.296 3.591   1.00 14.87 ? 240 LEU A C   1 
ATOM   1905 O  O   . LEU A 1 239 ? 0.722   -11.442 4.546   1.00 15.06 ? 240 LEU A O   1 
ATOM   1906 C  CB  . LEU A 1 239 ? -0.498  -13.511 2.520   1.00 16.45 ? 240 LEU A CB  1 
ATOM   1907 C  CG  . LEU A 1 239 ? -0.605  -14.453 1.310   1.00 16.38 ? 240 LEU A CG  1 
ATOM   1908 C  CD1 . LEU A 1 239 ? -1.338  -15.724 1.772   1.00 20.38 ? 240 LEU A CD1 1 
ATOM   1909 C  CD2 . LEU A 1 239 ? -1.329  -13.779 0.154   1.00 19.19 ? 240 LEU A CD2 1 
ATOM   1910 N  N   . MET A 1 240 ? -1.075  -10.440 3.570   1.00 14.33 ? 241 MET A N   1 
ATOM   1911 C  CA  . MET A 1 240 ? -1.488  -9.650  4.725   1.00 14.27 ? 241 MET A CA  1 
ATOM   1912 C  C   . MET A 1 240 ? -2.271  -10.571 5.649   1.00 12.77 ? 241 MET A C   1 
ATOM   1913 O  O   . MET A 1 240 ? -3.477  -10.737 5.502   1.00 11.83 ? 241 MET A O   1 
ATOM   1914 C  CB  . MET A 1 240 ? -2.308  -8.422  4.313   1.00 14.00 ? 241 MET A CB  1 
ATOM   1915 C  CG  . MET A 1 240 ? -2.652  -7.455  5.496   1.00 14.33 ? 241 MET A CG  1 
ATOM   1916 S  SD  . MET A 1 240 ? -3.644  -6.067  4.942   1.00 17.91 ? 241 MET A SD  1 
ATOM   1917 C  CE  . MET A 1 240 ? -2.324  -4.981  4.353   1.00 16.62 ? 241 MET A CE  1 
ATOM   1918 N  N   . VAL A 1 241 ? -1.524  -11.180 6.570   1.00 12.58 ? 242 VAL A N   1 
ATOM   1919 C  CA  . VAL A 1 241 ? -2.056  -12.089 7.610   1.00 12.11 ? 242 VAL A CA  1 
ATOM   1920 C  C   . VAL A 1 241 ? -1.239  -11.868 8.903   1.00 12.28 ? 242 VAL A C   1 
ATOM   1921 O  O   . VAL A 1 241 ? -0.051  -11.450 8.868   1.00 12.80 ? 242 VAL A O   1 
ATOM   1922 C  CB  . VAL A 1 241 ? -1.998  -13.630 7.211   1.00 11.27 ? 242 VAL A CB  1 
ATOM   1923 C  CG1 . VAL A 1 241 ? -2.902  -13.940 5.957   1.00 12.43 ? 242 VAL A CG1 1 
ATOM   1924 C  CG2 . VAL A 1 241 ? -0.557  -14.083 7.024   1.00 11.37 ? 242 VAL A CG2 1 
ATOM   1925 N  N   . ASP A 1 242 ? -1.847  -12.210 10.037  1.00 11.08 ? 243 ASP A N   1 
ATOM   1926 C  CA  . ASP A 1 242 ? -1.209  -11.999 11.342  1.00 11.29 ? 243 ASP A CA  1 
ATOM   1927 C  C   . ASP A 1 242 ? -0.727  -10.558 11.561  1.00 10.62 ? 243 ASP A C   1 
ATOM   1928 O  O   . ASP A 1 242 ? 0.386   -10.360 12.080  1.00 11.97 ? 243 ASP A O   1 
ATOM   1929 C  CB  . ASP A 1 242 ? -0.089  -13.022 11.627  1.00 10.73 ? 243 ASP A CB  1 
ATOM   1930 C  CG  . ASP A 1 242 ? -0.609  -14.438 11.670  1.00 13.69 ? 243 ASP A CG  1 
ATOM   1931 O  OD1 . ASP A 1 242 ? -1.696  -14.657 12.233  1.00 11.46 ? 243 ASP A OD1 1 
ATOM   1932 O  OD2 . ASP A 1 242 ? 0.040   -15.335 11.096  1.00 14.52 ? 243 ASP A OD2 1 
ATOM   1933 N  N   . ASN A 1 243 ? -1.580  -9.586  11.203  1.00 10.32 ? 244 ASN A N   1 
ATOM   1934 C  CA  . ASN A 1 243 ? -1.301  -8.149  11.439  1.00 9.67  ? 244 ASN A CA  1 
ATOM   1935 C  C   . ASN A 1 243 ? -1.878  -7.736  12.818  1.00 10.75 ? 244 ASN A C   1 
ATOM   1936 O  O   . ASN A 1 243 ? -2.605  -6.733  12.918  1.00 10.26 ? 244 ASN A O   1 
ATOM   1937 C  CB  . ASN A 1 243 ? -1.880  -7.281  10.302  1.00 11.23 ? 244 ASN A CB  1 
ATOM   1938 C  CG  . ASN A 1 243 ? -3.379  -7.478  10.105  1.00 11.80 ? 244 ASN A CG  1 
ATOM   1939 O  OD1 . ASN A 1 243 ? -3.980  -8.408  10.669  1.00 13.50 ? 244 ASN A OD1 1 
ATOM   1940 N  ND2 . ASN A 1 243 ? -4.005  -6.581  9.314   1.00 14.16 ? 244 ASN A ND2 1 
ATOM   1941 N  N   . TRP A 1 244 ? -1.553  -8.510  13.856  1.00 9.93  ? 245 TRP A N   1 
ATOM   1942 C  CA  . TRP A 1 244 ? -2.048  -8.251  15.225  1.00 10.47 ? 245 TRP A CA  1 
ATOM   1943 C  C   . TRP A 1 244 ? -0.871  -8.157  16.160  1.00 11.20 ? 245 TRP A C   1 
ATOM   1944 O  O   . TRP A 1 244 ? 0.160   -8.851  15.976  1.00 10.98 ? 245 TRP A O   1 
ATOM   1945 C  CB  . TRP A 1 244 ? -3.021  -9.355  15.727  1.00 10.29 ? 245 TRP A CB  1 
ATOM   1946 C  CG  . TRP A 1 244 ? -2.529  -10.775 15.560  1.00 9.52  ? 245 TRP A CG  1 
ATOM   1947 C  CD1 . TRP A 1 244 ? -2.623  -11.536 14.435  1.00 11.90 ? 245 TRP A CD1 1 
ATOM   1948 C  CD2 . TRP A 1 244 ? -1.996  -11.632 16.579  1.00 10.53 ? 245 TRP A CD2 1 
ATOM   1949 N  NE1 . TRP A 1 244 ? -2.114  -12.799 14.657  1.00 12.09 ? 245 TRP A NE1 1 
ATOM   1950 C  CE2 . TRP A 1 244 ? -1.718  -12.885 15.966  1.00 12.26 ? 245 TRP A CE2 1 
ATOM   1951 C  CE3 . TRP A 1 244 ? -1.715  -11.465 17.940  1.00 12.18 ? 245 TRP A CE3 1 
ATOM   1952 C  CZ2 . TRP A 1 244 ? -1.143  -13.957 16.663  1.00 10.65 ? 245 TRP A CZ2 1 
ATOM   1953 C  CZ3 . TRP A 1 244 ? -1.136  -12.534 18.649  1.00 12.14 ? 245 TRP A CZ3 1 
ATOM   1954 C  CH2 . TRP A 1 244 ? -0.867  -13.770 18.005  1.00 10.90 ? 245 TRP A CH2 1 
ATOM   1955 N  N   . ARG A 1 245 ? -1.006  -7.268  17.142  1.00 10.13 ? 246 ARG A N   1 
ATOM   1956 C  CA  . ARG A 1 245 ? -0.074  -7.169  18.259  1.00 11.04 ? 246 ARG A CA  1 
ATOM   1957 C  C   . ARG A 1 245 ? -0.561  -8.085  19.387  1.00 11.01 ? 246 ARG A C   1 
ATOM   1958 O  O   . ARG A 1 245 ? -1.755  -8.091  19.709  1.00 11.78 ? 246 ARG A O   1 
ATOM   1959 C  CB  . ARG A 1 245 ? -0.021  -5.713  18.774  1.00 9.92  ? 246 ARG A CB  1 
ATOM   1960 C  CG  . ARG A 1 245 ? 1.121   -5.485  19.742  1.00 10.55 ? 246 ARG A CG  1 
ATOM   1961 C  CD  . ARG A 1 245 ? 1.053   -4.130  20.430  1.00 11.58 ? 246 ARG A CD  1 
ATOM   1962 N  NE  . ARG A 1 245 ? 2.330   -3.813  21.123  1.00 12.19 ? 246 ARG A NE  1 
ATOM   1963 C  CZ  . ARG A 1 245 ? 2.516   -2.775  21.939  1.00 13.74 ? 246 ARG A CZ  1 
ATOM   1964 N  NH1 . ARG A 1 245 ? 1.508   -1.955  22.232  1.00 10.00 ? 246 ARG A NH1 1 
ATOM   1965 N  NH2 . ARG A 1 245 ? 3.722   -2.560  22.472  1.00 13.19 ? 246 ARG A NH2 1 
ATOM   1966 N  N   . PRO A 1 246 ? 0.347   -8.863  20.004  1.00 12.39 ? 247 PRO A N   1 
ATOM   1967 C  CA  . PRO A 1 246 ? -0.041  -9.716  21.111  1.00 12.04 ? 247 PRO A CA  1 
ATOM   1968 C  C   . PRO A 1 246 ? -0.360  -8.907  22.382  1.00 11.71 ? 247 PRO A C   1 
ATOM   1969 O  O   . PRO A 1 246 ? 0.026   -7.727  22.536  1.00 11.93 ? 247 PRO A O   1 
ATOM   1970 C  CB  . PRO A 1 246 ? 1.206   -10.594 21.360  1.00 12.05 ? 247 PRO A CB  1 
ATOM   1971 C  CG  . PRO A 1 246 ? 2.184   -10.232 20.319  1.00 13.62 ? 247 PRO A CG  1 
ATOM   1972 C  CD  . PRO A 1 246 ? 1.799   -8.922  19.752  1.00 12.75 ? 247 PRO A CD  1 
ATOM   1973 N  N   . ALA A 1 247 ? -1.028  -9.583  23.310  1.00 11.81 ? 248 ALA A N   1 
ATOM   1974 C  CA  . ALA A 1 247 ? -1.339  -9.023  24.611  1.00 10.76 ? 248 ALA A CA  1 
ATOM   1975 C  C   . ALA A 1 247 ? -0.113  -8.444  25.313  1.00 11.73 ? 248 ALA A C   1 
ATOM   1976 O  O   . ALA A 1 247 ? 0.975   -9.068  25.335  1.00 10.56 ? 248 ALA A O   1 
ATOM   1977 C  CB  . ALA A 1 247 ? -2.049  -10.089 25.499  1.00 11.48 ? 248 ALA A CB  1 
ATOM   1978 N  N   . GLN A 1 248 ? -0.311  -7.276  25.910  1.00 11.38 ? 249 GLN A N   1 
ATOM   1979 C  CA  . GLN A 1 248 ? 0.742   -6.514  26.592  1.00 12.68 ? 249 GLN A CA  1 
ATOM   1980 C  C   . GLN A 1 248 ? 0.478   -6.488  28.103  1.00 13.39 ? 249 GLN A C   1 
ATOM   1981 O  O   . GLN A 1 248 ? -0.667  -6.710  28.530  1.00 12.16 ? 249 GLN A O   1 
ATOM   1982 C  CB  . GLN A 1 248 ? 0.770   -5.086  26.043  1.00 13.08 ? 249 GLN A CB  1 
ATOM   1983 C  CG  . GLN A 1 248 ? 1.119   -4.979  24.558  1.00 12.24 ? 249 GLN A CG  1 
ATOM   1984 C  CD  . GLN A 1 248 ? 2.463   -5.628  24.232  1.00 14.67 ? 249 GLN A CD  1 
ATOM   1985 O  OE1 . GLN A 1 248 ? 3.512   -5.254  24.796  1.00 16.00 ? 249 GLN A OE1 1 
ATOM   1986 N  NE2 . GLN A 1 248 ? 2.442   -6.601  23.321  1.00 13.05 ? 249 GLN A NE2 1 
ATOM   1987 N  N   . PRO A 1 249 ? 1.529   -6.231  28.931  1.00 14.42 ? 250 PRO A N   1 
ATOM   1988 C  CA  . PRO A 1 249 ? 1.326   -6.213  30.383  1.00 14.82 ? 250 PRO A CA  1 
ATOM   1989 C  C   . PRO A 1 249 ? 0.253   -5.239  30.848  1.00 14.35 ? 250 PRO A C   1 
ATOM   1990 O  O   . PRO A 1 249 ? 0.264   -4.075  30.440  1.00 14.11 ? 250 PRO A O   1 
ATOM   1991 C  CB  . PRO A 1 249 ? 2.688   -5.736  30.914  1.00 14.82 ? 250 PRO A CB  1 
ATOM   1992 C  CG  . PRO A 1 249 ? 3.653   -6.218  29.890  1.00 16.04 ? 250 PRO A CG  1 
ATOM   1993 C  CD  . PRO A 1 249 ? 2.943   -5.989  28.581  1.00 15.01 ? 250 PRO A CD  1 
ATOM   1994 N  N   . LEU A 1 250 ? -0.653  -5.716  31.699  1.00 14.25 ? 251 LEU A N   1 
ATOM   1995 C  CA  . LEU A 1 250 ? -1.724  -4.867  32.229  1.00 14.95 ? 251 LEU A CA  1 
ATOM   1996 C  C   . LEU A 1 250 ? -1.159  -3.786  33.146  1.00 15.11 ? 251 LEU A C   1 
ATOM   1997 O  O   . LEU A 1 250 ? -1.666  -2.662  33.187  1.00 13.03 ? 251 LEU A O   1 
ATOM   1998 C  CB  . LEU A 1 250 ? -2.793  -5.694  32.956  1.00 15.41 ? 251 LEU A CB  1 
ATOM   1999 C  CG  . LEU A 1 250 ? -4.126  -5.026  33.359  1.00 14.54 ? 251 LEU A CG  1 
ATOM   2000 C  CD1 . LEU A 1 250 ? -4.895  -4.425  32.164  1.00 15.15 ? 251 LEU A CD1 1 
ATOM   2001 C  CD2 . LEU A 1 250 ? -5.044  -5.964  34.184  1.00 16.91 ? 251 LEU A CD2 1 
ATOM   2002 N  N   . LYS A 1 251 ? -0.118  -4.150  33.901  1.00 15.87 ? 252 LYS A N   1 
ATOM   2003 C  CA  . LYS A 1 251 ? 0.567   -3.197  34.811  1.00 17.86 ? 252 LYS A CA  1 
ATOM   2004 C  C   . LYS A 1 251 ? -0.457  -2.627  35.786  1.00 18.35 ? 252 LYS A C   1 
ATOM   2005 O  O   . LYS A 1 251 ? -1.268  -3.380  36.326  1.00 18.80 ? 252 LYS A O   1 
ATOM   2006 C  CB  . LYS A 1 251 ? 1.323   -2.108  34.025  1.00 17.39 ? 252 LYS A CB  1 
ATOM   2007 C  CG  . LYS A 1 251 ? 2.527   -2.695  33.266  1.00 19.70 ? 252 LYS A CG  1 
ATOM   2008 C  CD  . LYS A 1 251 ? 3.412   -1.660  32.606  1.00 20.47 ? 252 LYS A CD  1 
ATOM   2009 C  CE  . LYS A 1 251 ? 4.665   -2.325  32.098  1.00 24.90 ? 252 LYS A CE  1 
ATOM   2010 N  NZ  . LYS A 1 251 ? 5.421   -1.402  31.219  1.00 26.30 ? 252 LYS A NZ  1 
ATOM   2011 N  N   . ASN A 1 252 ? -0.440  -1.315  35.978  1.00 19.49 ? 253 ASN A N   1 
ATOM   2012 C  CA  . ASN A 1 252 ? -1.258  -0.673  36.989  1.00 22.01 ? 253 ASN A CA  1 
ATOM   2013 C  C   . ASN A 1 252 ? -2.637  -0.264  36.458  1.00 21.43 ? 253 ASN A C   1 
ATOM   2014 O  O   . ASN A 1 252 ? -2.948  0.950   36.489  1.00 22.47 ? 253 ASN A O   1 
ATOM   2015 C  CB  . ASN A 1 252 ? -0.520  0.572   37.535  1.00 23.73 ? 253 ASN A CB  1 
ATOM   2016 C  CG  . ASN A 1 252 ? -1.239  1.216   38.729  1.00 27.64 ? 253 ASN A CG  1 
ATOM   2017 O  OD1 . ASN A 1 252 ? -1.874  0.527   39.542  1.00 33.01 ? 253 ASN A OD1 1 
ATOM   2018 N  ND2 . ASN A 1 252 ? -1.150  2.546   38.829  1.00 32.36 ? 253 ASN A ND2 1 
ATOM   2019 N  N   . ARG A 1 253 ? -3.421  -1.240  35.939  1.00 18.53 ? 254 ARG A N   1 
ATOM   2020 C  CA  . ARG A 1 253 ? -4.723  -0.937  35.330  1.00 17.27 ? 254 ARG A CA  1 
ATOM   2021 C  C   . ARG A 1 253 ? -5.817  -1.913  35.701  1.00 17.85 ? 254 ARG A C   1 
ATOM   2022 O  O   . ARG A 1 253 ? -5.564  -3.096  35.904  1.00 18.35 ? 254 ARG A O   1 
ATOM   2023 C  CB  . ARG A 1 253 ? -4.640  -0.878  33.802  1.00 16.40 ? 254 ARG A CB  1 
ATOM   2024 C  CG  . ARG A 1 253 ? -3.840  0.293   33.251  1.00 15.31 ? 254 ARG A CG  1 
ATOM   2025 C  CD  . ARG A 1 253 ? -3.789  0.203   31.750  1.00 14.74 ? 254 ARG A CD  1 
ATOM   2026 N  NE  . ARG A 1 253 ? -2.880  -0.878  31.297  1.00 13.77 ? 254 ARG A NE  1 
ATOM   2027 C  CZ  . ARG A 1 253 ? -2.607  -1.131  30.015  1.00 10.70 ? 254 ARG A CZ  1 
ATOM   2028 N  NH1 . ARG A 1 253 ? -3.211  -0.416  29.069  1.00 9.24  ? 254 ARG A NH1 1 
ATOM   2029 N  NH2 . ARG A 1 253 ? -1.773  -2.124  29.684  1.00 9.02  ? 254 ARG A NH2 1 
ATOM   2030 N  N   . GLN A 1 254 ? -7.038  -1.383  35.742  1.00 17.69 ? 255 GLN A N   1 
ATOM   2031 C  CA  . GLN A 1 254 ? -8.217  -2.129  36.075  1.00 18.63 ? 255 GLN A CA  1 
ATOM   2032 C  C   . GLN A 1 254 ? -9.127  -2.137  34.842  1.00 17.83 ? 255 GLN A C   1 
ATOM   2033 O  O   . GLN A 1 254 ? -9.409  -1.070  34.251  1.00 18.86 ? 255 GLN A O   1 
ATOM   2034 C  CB  . GLN A 1 254 ? -8.911  -1.436  37.260  1.00 19.38 ? 255 GLN A CB  1 
ATOM   2035 C  CG  . GLN A 1 254 ? -10.144 -2.147  37.788  1.00 24.84 ? 255 GLN A CG  1 
ATOM   2036 C  CD  . GLN A 1 254 ? -9.892  -3.585  38.222  1.00 31.51 ? 255 GLN A CD  1 
ATOM   2037 O  OE1 . GLN A 1 254 ? -10.614 -4.510  37.806  1.00 34.73 ? 255 GLN A OE1 1 
ATOM   2038 N  NE2 . GLN A 1 254 ? -8.877  -3.788  39.066  1.00 34.77 ? 255 GLN A NE2 1 
ATOM   2039 N  N   . ILE A 1 255 ? -9.544  -3.330  34.429  1.00 16.28 ? 256 ILE A N   1 
ATOM   2040 C  CA  . ILE A 1 255 ? -10.550 -3.470  33.396  1.00 15.45 ? 256 ILE A CA  1 
ATOM   2041 C  C   . ILE A 1 255 ? -11.929 -3.522  34.083  1.00 14.95 ? 256 ILE A C   1 
ATOM   2042 O  O   . ILE A 1 255 ? -12.148 -4.304  35.037  1.00 14.19 ? 256 ILE A O   1 
ATOM   2043 C  CB  . ILE A 1 255 ? -10.326 -4.748  32.510  1.00 15.35 ? 256 ILE A CB  1 
ATOM   2044 C  CG1 . ILE A 1 255 ? -8.947  -4.724  31.834  1.00 15.79 ? 256 ILE A CG1 1 
ATOM   2045 C  CG2 . ILE A 1 255 ? -11.466 -4.915  31.476  1.00 12.79 ? 256 ILE A CG2 1 
ATOM   2046 C  CD1 . ILE A 1 255 ? -8.628  -6.049  31.062  1.00 15.56 ? 256 ILE A CD1 1 
ATOM   2047 N  N   . LYS A 1 256 ? -12.822 -2.643  33.629  1.00 13.99 ? 257 LYS A N   1 
ATOM   2048 C  CA  . LYS A 1 256 ? -14.191 -2.532  34.143  1.00 14.46 ? 257 LYS A CA  1 
ATOM   2049 C  C   . LYS A 1 256 ? -15.173 -3.182  33.186  1.00 14.45 ? 257 LYS A C   1 
ATOM   2050 O  O   . LYS A 1 256 ? -14.980 -3.144  31.960  1.00 14.61 ? 257 LYS A O   1 
ATOM   2051 C  CB  . LYS A 1 256 ? -14.593 -1.057  34.313  1.00 14.15 ? 257 LYS A CB  1 
ATOM   2052 C  CG  . LYS A 1 256 ? -13.568 -0.174  35.010  1.00 19.57 ? 257 LYS A CG  1 
ATOM   2053 C  CD  . LYS A 1 256 ? -13.480 -0.369  36.490  1.00 25.39 ? 257 LYS A CD  1 
ATOM   2054 C  CE  . LYS A 1 256 ? -13.459 1.004   37.221  1.00 29.55 ? 257 LYS A CE  1 
ATOM   2055 N  NZ  . LYS A 1 256 ? -12.741 2.126   36.499  1.00 32.73 ? 257 LYS A NZ  1 
ATOM   2056 N  N   . ALA A 1 257 ? -16.235 -3.755  33.735  1.00 14.20 ? 258 ALA A N   1 
ATOM   2057 C  CA  . ALA A 1 257 ? -17.272 -4.360  32.917  1.00 14.47 ? 258 ALA A CA  1 
ATOM   2058 C  C   . ALA A 1 257 ? -18.582 -3.621  33.091  1.00 14.92 ? 258 ALA A C   1 
ATOM   2059 O  O   . ALA A 1 257 ? -18.935 -3.196  34.214  1.00 15.51 ? 258 ALA A O   1 
ATOM   2060 C  CB  . ALA A 1 257 ? -17.422 -5.865  33.221  1.00 14.82 ? 258 ALA A CB  1 
ATOM   2061 N  N   . SER A 1 258 ? -19.295 -3.473  31.981  1.00 14.66 ? 259 SER A N   1 
ATOM   2062 C  CA  . SER A 1 258 ? -20.576 -2.768  31.972  1.00 16.74 ? 259 SER A CA  1 
ATOM   2063 C  C   . SER A 1 258 ? -21.717 -3.695  32.403  1.00 17.67 ? 259 SER A C   1 
ATOM   2064 O  O   . SER A 1 258 ? -22.867 -3.254  32.495  1.00 18.83 ? 259 SER A O   1 
ATOM   2065 C  CB  . SER A 1 258 ? -20.882 -2.165  30.604  1.00 16.25 ? 259 SER A CB  1 
ATOM   2066 O  OG  . SER A 1 258 ? -21.365 -3.130  29.659  1.00 16.09 ? 259 SER A OG  1 
ATOM   2067 N  N   . PHE A 1 259 ? -21.391 -4.950  32.680  1.00 19.38 ? 260 PHE A N   1 
ATOM   2068 C  CA  . PHE A 1 259 ? -22.401 -6.005  32.849  1.00 21.43 ? 260 PHE A CA  1 
ATOM   2069 C  C   . PHE A 1 259 ? -22.052 -6.989  33.964  1.00 24.32 ? 260 PHE A C   1 
ATOM   2070 O  O   . PHE A 1 259 ? -20.878 -7.165  34.317  1.00 23.56 ? 260 PHE A O   1 
ATOM   2071 C  CB  . PHE A 1 259 ? -22.580 -6.779  31.533  1.00 20.78 ? 260 PHE A CB  1 
ATOM   2072 C  CG  . PHE A 1 259 ? -21.301 -7.476  31.056  1.00 20.88 ? 260 PHE A CG  1 
ATOM   2073 C  CD1 . PHE A 1 259 ? -20.376 -6.787  30.270  1.00 18.81 ? 260 PHE A CD1 1 
ATOM   2074 C  CD2 . PHE A 1 259 ? -21.013 -8.785  31.442  1.00 20.15 ? 260 PHE A CD2 1 
ATOM   2075 C  CE1 . PHE A 1 259 ? -19.190 -7.394  29.842  1.00 19.72 ? 260 PHE A CE1 1 
ATOM   2076 C  CE2 . PHE A 1 259 ? -19.821 -9.414  31.030  1.00 21.21 ? 260 PHE A CE2 1 
ATOM   2077 C  CZ  . PHE A 1 259 ? -18.907 -8.706  30.215  1.00 20.87 ? 260 PHE A CZ  1 
ATOM   2078 N  N   . LYS A 1 260 ? -23.118 -7.611  34.485  1.00 27.70 ? 261 LYS A N   1 
ATOM   2079 C  CA  . LYS A 1 260 ? -23.128 -8.801  35.368  1.00 31.46 ? 261 LYS A CA  1 
ATOM   2080 C  C   . LYS A 1 260 ? -22.441 -8.698  36.730  1.00 32.97 ? 261 LYS A C   1 
ATOM   2081 O  O   . LYS A 1 260 ? -21.387 -9.299  36.996  1.00 35.15 ? 261 LYS A O   1 
ATOM   2082 C  CB  . LYS A 1 260 ? -22.729 -10.091 34.623  1.00 31.14 ? 261 LYS A CB  1 
ATOM   2083 C  CG  . LYS A 1 260 ? -23.674 -10.488 33.477  1.00 31.77 ? 261 LYS A CG  1 
ATOM   2084 C  CD  . LYS A 1 260 ? -23.194 -11.758 32.722  1.00 32.22 ? 261 LYS A CD  1 
ATOM   2085 C  CE  . LYS A 1 260 ? -21.648 -11.942 32.789  1.00 31.76 ? 261 LYS A CE  1 
ATOM   2086 N  NZ  . LYS A 1 260 ? -21.153 -13.287 32.367  1.00 32.46 ? 261 LYS A NZ  1 
ATOM   2087 O  OXT . LYS A 1 260 ? -22.976 -8.010  37.613  1.00 34.86 ? 261 LYS A OXT 1 
HETATM 2088 ZN ZN  . ZN  B 2 .   ? -6.586  -1.701  15.261  1.00 10.15 ? 262 ZN  A ZN  1 
HETATM 2089 N  N1  . BCN C 3 .   ? -20.466 -14.617 23.589  1.00 45.35 ? 263 BCN A N1  1 
HETATM 2090 C  C1  . BCN C 3 .   ? -19.781 -15.875 23.333  1.00 44.17 ? 263 BCN A C1  1 
HETATM 2091 C  C2  . BCN C 3 .   ? -19.086 -16.106 22.025  1.00 44.97 ? 263 BCN A C2  1 
HETATM 2092 O  O21 . BCN C 3 .   ? -17.804 -16.128 21.985  1.00 43.80 ? 263 BCN A O21 1 
HETATM 2093 O  O22 . BCN C 3 .   ? -19.877 -16.284 21.001  1.00 43.89 ? 263 BCN A O22 1 
HETATM 2094 C  C3  . BCN C 3 .   ? -21.714 -14.270 23.029  1.00 44.19 ? 263 BCN A C3  1 
HETATM 2095 C  C4  . BCN C 3 .   ? -22.292 -12.926 23.399  1.00 44.68 ? 263 BCN A C4  1 
HETATM 2096 O  O4  . BCN C 3 .   ? -22.632 -12.756 24.761  1.00 44.15 ? 263 BCN A O4  1 
HETATM 2097 C  C5  . BCN C 3 .   ? -19.764 -13.738 24.506  1.00 42.79 ? 263 BCN A C5  1 
HETATM 2098 C  C6  . BCN C 3 .   ? -20.159 -14.392 25.823  1.00 43.22 ? 263 BCN A C6  1 
HETATM 2099 O  O6  . BCN C 3 .   ? -19.116 -15.149 26.290  1.00 40.28 ? 263 BCN A O6  1 
HETATM 2100 O  O1  . MES D 4 .   ? -7.230  -9.042  -2.661  1.00 33.11 ? 264 MES A O1  1 
HETATM 2101 C  C2  . MES D 4 .   ? -7.343  -9.850  -3.911  1.00 32.20 ? 264 MES A C2  1 
HETATM 2102 C  C3  . MES D 4 .   ? -8.440  -10.977 -3.956  1.00 32.15 ? 264 MES A C3  1 
HETATM 2103 N  N4  . MES D 4 .   ? -9.622  -10.782 -3.077  1.00 31.88 ? 264 MES A N4  1 
HETATM 2104 C  C5  . MES D 4 .   ? -9.402  -9.975  -1.851  1.00 30.11 ? 264 MES A C5  1 
HETATM 2105 C  C6  . MES D 4 .   ? -7.965  -9.623  -1.583  1.00 32.23 ? 264 MES A C6  1 
HETATM 2106 C  C7  . MES D 4 .   ? -10.951 -11.452 -3.306  1.00 32.07 ? 264 MES A C7  1 
HETATM 2107 C  C8  . MES D 4 .   ? -10.909 -12.963 -3.859  1.00 34.20 ? 264 MES A C8  1 
HETATM 2108 S  S   . DMS E 5 .   ? 1.459   -11.610 15.044  1.00 31.88 ? 265 DMS A S   1 
HETATM 2109 O  O   . DMS E 5 .   ? 2.008   -13.249 14.529  1.00 31.09 ? 265 DMS A O   1 
HETATM 2110 C  C1  . DMS E 5 .   ? 1.925   -11.410 16.779  1.00 28.92 ? 265 DMS A C1  1 
HETATM 2111 C  C2  . DMS E 5 .   ? 2.524   -10.381 14.243  1.00 31.44 ? 265 DMS A C2  1 
HETATM 2112 N  N1  . E2I F 6 .   ? -0.503  8.732   14.853  1.00 49.51 ? 266 E2I A N1  1 
HETATM 2113 C  C2  . E2I F 6 .   ? 0.148   9.739   15.369  1.00 50.66 ? 266 E2I A C2  1 
HETATM 2114 C  C3  . E2I F 6 .   ? 0.189   11.014  14.847  1.00 50.07 ? 266 E2I A C3  1 
HETATM 2115 C  C4  . E2I F 6 .   ? -0.515  11.291  13.664  1.00 49.91 ? 266 E2I A C4  1 
HETATM 2116 N  N5  . E2I F 6 .   ? -1.169  10.211  13.171  1.00 49.44 ? 266 E2I A N5  1 
HETATM 2117 C  C6  . E2I F 6 .   ? -1.133  8.976   13.789  1.00 49.06 ? 266 E2I A C6  1 
HETATM 2118 C  C13 . E2I F 6 .   ? 1.015   11.923  15.662  1.00 49.92 ? 266 E2I A C13 1 
HETATM 2119 C  C15 . E2I F 6 .   ? 2.478   11.555  15.291  1.00 50.34 ? 266 E2I A C15 1 
HETATM 2120 C  C17 . E2I F 6 .   ? 3.469   11.818  16.425  1.00 51.24 ? 266 E2I A C17 1 
HETATM 2121 C  C19 . E2I F 6 .   ? 3.898   10.543  17.185  1.00 50.63 ? 266 E2I A C19 1 
HETATM 2122 S  S21 . E2I F 6 .   ? -1.939  7.577   13.177  1.00 48.81 ? 266 E2I A S21 1 
HETATM 2123 C  C23 . E2I F 6 .   ? -2.078  5.872   13.748  1.00 34.66 ? 266 E2I A C23 1 
HETATM 2124 C  C25 . E2I F 6 .   ? -3.540  5.454   13.582  1.00 27.21 ? 266 E2I A C25 1 
HETATM 2125 O  O27 . E2I F 6 .   ? -4.287  6.038   12.790  1.00 27.98 ? 266 E2I A O27 1 
HETATM 2126 C  C29 . E2I F 6 .   ? -4.146  4.325   14.368  1.00 23.55 ? 266 E2I A C29 1 
HETATM 2127 C  C31 . E2I F 6 .   ? -5.522  4.295   14.617  1.00 20.25 ? 266 E2I A C31 1 
HETATM 2128 C  C32 . E2I F 6 .   ? -6.026  3.200   15.359  1.00 19.07 ? 266 E2I A C32 1 
HETATM 2129 C  C33 . E2I F 6 .   ? -5.199  2.201   15.848  1.00 20.17 ? 266 E2I A C33 1 
HETATM 2130 C  C34 . E2I F 6 .   ? -3.846  2.242   15.592  1.00 20.29 ? 266 E2I A C34 1 
HETATM 2131 C  C35 . E2I F 6 .   ? -3.315  3.302   14.847  1.00 22.41 ? 266 E2I A C35 1 
HETATM 2132 S  S42 . E2I F 6 .   ? -5.853  0.804   16.770  1.00 17.25 ? 266 E2I A S42 1 
HETATM 2133 O  O44 . E2I F 6 .   ? -5.305  0.961   18.129  1.00 14.61 ? 266 E2I A O44 1 
HETATM 2134 O  O46 . E2I F 6 .   ? -7.314  0.901   16.626  1.00 13.86 ? 266 E2I A O46 1 
HETATM 2135 N  N48 . E2I F 6 .   ? -5.139  -0.522  15.985  1.00 14.87 ? 266 E2I A N48 1 
HETATM 2136 O  O   . HOH G 7 .   ? -16.491 5.178   -7.905  1.00 27.88 ? 126 HOH A O   1 
HETATM 2137 O  O   . HOH G 7 .   ? -1.179  -4.110  15.683  1.00 9.85  ? 267 HOH A O   1 
HETATM 2138 O  O   . HOH G 7 .   ? -4.474  -13.466 18.088  1.00 10.26 ? 268 HOH A O   1 
HETATM 2139 O  O   . HOH G 7 .   ? -3.732  -15.892 24.391  1.00 14.94 ? 269 HOH A O   1 
HETATM 2140 O  O   . HOH G 7 .   ? -3.498  -11.082 20.867  1.00 12.90 ? 270 HOH A O   1 
HETATM 2141 O  O   . HOH G 7 .   ? -21.517 5.630   4.721   1.00 16.83 ? 271 HOH A O   1 
HETATM 2142 O  O   . HOH G 7 .   ? 4.941   -4.970  20.996  1.00 16.47 ? 272 HOH A O   1 
HETATM 2143 O  O   . HOH G 7 .   ? -16.900 -8.326  20.436  1.00 12.09 ? 273 HOH A O   1 
HETATM 2144 O  O   . HOH G 7 .   ? -2.407  -8.658  29.215  1.00 12.47 ? 274 HOH A O   1 
HETATM 2145 O  O   . HOH G 7 .   ? 3.791   5.043   29.723  1.00 18.34 ? 275 HOH A O   1 
HETATM 2146 O  O   . HOH G 7 .   ? -21.545 -7.158  23.671  1.00 13.29 ? 276 HOH A O   1 
HETATM 2147 O  O   . HOH G 7 .   ? -17.919 -20.439 8.018   1.00 12.55 ? 277 HOH A O   1 
HETATM 2148 O  O   . HOH G 7 .   ? -3.344  -13.241 25.249  1.00 11.90 ? 278 HOH A O   1 
HETATM 2149 O  O   . HOH G 7 .   ? -7.819  -15.401 11.232  1.00 10.22 ? 279 HOH A O   1 
HETATM 2150 O  O   . HOH G 7 .   ? -8.516  -3.851  7.876   1.00 13.78 ? 280 HOH A O   1 
HETATM 2151 O  O   . HOH G 7 .   ? -10.656 8.770   25.537  1.00 13.81 ? 281 HOH A O   1 
HETATM 2152 O  O   . HOH G 7 .   ? 1.358   -1.519  29.383  1.00 13.74 ? 282 HOH A O   1 
HETATM 2153 O  O   . HOH G 7 .   ? -13.757 10.395  27.845  1.00 19.59 ? 283 HOH A O   1 
HETATM 2154 O  O   . HOH G 7 .   ? -16.007 -12.250 24.372  1.00 16.28 ? 284 HOH A O   1 
HETATM 2155 O  O   . HOH G 7 .   ? -7.913  -22.199 10.435  1.00 20.22 ? 285 HOH A O   1 
HETATM 2156 O  O   . HOH G 7 .   ? -9.560  -7.928  34.051  1.00 17.26 ? 286 HOH A O   1 
HETATM 2157 O  O   . HOH G 7 .   ? -14.561 -18.413 18.825  1.00 19.93 ? 287 HOH A O   1 
HETATM 2158 O  O   . HOH G 7 .   ? -19.143 10.096  8.860   1.00 16.11 ? 288 HOH A O   1 
HETATM 2159 O  O   . HOH G 7 .   ? -6.010  -4.625  -6.519  1.00 26.12 ? 289 HOH A O   1 
HETATM 2160 O  O   . HOH G 7 .   ? -16.161 -9.922  32.943  1.00 17.09 ? 290 HOH A O   1 
HETATM 2161 O  O   . HOH G 7 .   ? -14.172 -16.594 28.982  1.00 20.70 ? 291 HOH A O   1 
HETATM 2162 O  O   . HOH G 7 .   ? -23.878 -0.711  26.435  1.00 19.23 ? 292 HOH A O   1 
HETATM 2163 O  O   . HOH G 7 .   ? 5.369   7.144   20.125  1.00 14.63 ? 293 HOH A O   1 
HETATM 2164 O  O   . HOH G 7 .   ? -1.940  -12.315 22.869  1.00 15.52 ? 294 HOH A O   1 
HETATM 2165 O  O   . HOH G 7 .   ? -21.070 -12.765 -1.771  1.00 18.67 ? 295 HOH A O   1 
HETATM 2166 O  O   . HOH G 7 .   ? -10.278 -18.203 17.021  1.00 15.25 ? 296 HOH A O   1 
HETATM 2167 O  O   . HOH G 7 .   ? -17.826 10.410  11.337  1.00 17.67 ? 297 HOH A O   1 
HETATM 2168 O  O   . HOH G 7 .   ? -4.693  1.020   43.315  1.00 21.31 ? 298 HOH A O   1 
HETATM 2169 O  O   . HOH G 7 .   ? 8.633   -3.781  21.178  1.00 19.57 ? 299 HOH A O   1 
HETATM 2170 O  O   . HOH G 7 .   ? -12.864 -16.820 26.499  1.00 15.97 ? 300 HOH A O   1 
HETATM 2171 O  O   . HOH G 7 .   ? -12.738 -17.285 16.841  1.00 17.74 ? 301 HOH A O   1 
HETATM 2172 O  O   . HOH G 7 .   ? -23.228 -2.994  6.767   1.00 17.58 ? 302 HOH A O   1 
HETATM 2173 O  O   . HOH G 7 .   ? -1.790  -17.422 25.547  1.00 23.30 ? 303 HOH A O   1 
HETATM 2174 O  O   . HOH G 7 .   ? -28.483 0.182   24.348  1.00 22.54 ? 304 HOH A O   1 
HETATM 2175 O  O   . HOH G 7 .   ? -24.803 -7.737  8.968   1.00 16.78 ? 305 HOH A O   1 
HETATM 2176 O  O   . HOH G 7 .   ? 7.673   6.152   21.632  1.00 16.72 ? 306 HOH A O   1 
HETATM 2177 O  O   . HOH G 7 .   ? -17.621 -21.216 17.509  1.00 21.45 ? 307 HOH A O   1 
HETATM 2178 O  O   . HOH G 7 .   ? -23.707 -0.856  3.929   1.00 18.09 ? 308 HOH A O   1 
HETATM 2179 O  O   . HOH G 7 .   ? -8.044  -19.259 21.723  1.00 17.56 ? 309 HOH A O   1 
HETATM 2180 O  O   . HOH G 7 .   ? 1.404   8.812   24.431  1.00 17.07 ? 310 HOH A O   1 
HETATM 2181 O  O   . HOH G 7 .   ? -26.688 -2.543  14.329  1.00 19.95 ? 311 HOH A O   1 
HETATM 2182 O  O   . HOH G 7 .   ? -13.399 -18.578 14.673  1.00 21.17 ? 312 HOH A O   1 
HETATM 2183 O  O   . HOH G 7 .   ? -28.899 -5.748  24.642  1.00 28.75 ? 313 HOH A O   1 
HETATM 2184 O  O   . HOH G 7 .   ? -5.058  0.876   9.979   1.00 30.30 ? 314 HOH A O   1 
HETATM 2185 O  O   . HOH G 7 .   ? -22.153 -18.369 13.548  1.00 23.49 ? 315 HOH A O   1 
HETATM 2186 O  O   . HOH G 7 .   ? -11.901 2.873   30.851  1.00 25.68 ? 316 HOH A O   1 
HETATM 2187 O  O   . HOH G 7 .   ? -16.189 -11.351 41.499  1.00 19.16 ? 317 HOH A O   1 
HETATM 2188 O  O   . HOH G 7 .   ? -23.975 8.777   20.141  1.00 22.69 ? 318 HOH A O   1 
HETATM 2189 O  O   . HOH G 7 .   ? 4.454   -3.459  26.409  1.00 21.57 ? 319 HOH A O   1 
HETATM 2190 O  O   . HOH G 7 .   ? -20.329 10.957  26.633  1.00 20.96 ? 320 HOH A O   1 
HETATM 2191 O  O   . HOH G 7 .   ? -7.034  5.960   6.641   1.00 25.28 ? 321 HOH A O   1 
HETATM 2192 O  O   . HOH G 7 .   ? -11.015 -19.569 7.145   1.00 26.81 ? 322 HOH A O   1 
HETATM 2193 O  O   . HOH G 7 .   ? -4.309  3.988   10.135  1.00 28.54 ? 323 HOH A O   1 
HETATM 2194 O  O   . HOH G 7 .   ? 4.465   -6.585  7.895   1.00 19.56 ? 324 HOH A O   1 
HETATM 2195 O  O   . HOH G 7 .   ? -25.583 9.594   13.215  1.00 29.38 ? 325 HOH A O   1 
HETATM 2196 O  O   . HOH G 7 .   ? 1.471   -11.708 25.039  1.00 19.06 ? 326 HOH A O   1 
HETATM 2197 O  O   . HOH G 7 .   ? -22.195 3.654   -3.004  1.00 21.72 ? 327 HOH A O   1 
HETATM 2198 O  O   . HOH G 7 .   ? 8.023   -5.948  -10.601 1.00 24.58 ? 328 HOH A O   1 
HETATM 2199 O  O   . HOH G 7 .   ? -4.581  -11.878 32.151  1.00 19.96 ? 329 HOH A O   1 
HETATM 2200 O  O   . HOH G 7 .   ? -16.752 -13.941 26.470  1.00 20.16 ? 330 HOH A O   1 
HETATM 2201 O  O   . HOH G 7 .   ? -22.786 -5.824  2.715   1.00 21.13 ? 331 HOH A O   1 
HETATM 2202 O  O   . HOH G 7 .   ? -2.261  -3.009  11.400  1.00 24.99 ? 332 HOH A O   1 
HETATM 2203 O  O   . HOH G 7 .   ? -7.148  -8.618  32.665  1.00 17.25 ? 333 HOH A O   1 
HETATM 2204 O  O   . HOH G 7 .   ? -6.672  -20.174 19.534  1.00 18.89 ? 334 HOH A O   1 
HETATM 2205 O  O   . HOH G 7 .   ? 2.647   -11.428 9.352   1.00 26.63 ? 335 HOH A O   1 
HETATM 2206 O  O   . HOH G 7 .   ? -26.685 -3.943  25.066  1.00 20.06 ? 336 HOH A O   1 
HETATM 2207 O  O   . HOH G 7 .   ? -23.038 -0.476  34.451  1.00 24.53 ? 337 HOH A O   1 
HETATM 2208 O  O   . HOH G 7 .   ? -0.381  10.929  23.391  1.00 21.28 ? 338 HOH A O   1 
HETATM 2209 O  O   . HOH G 7 .   ? -1.413  -13.196 27.163  1.00 20.40 ? 339 HOH A O   1 
HETATM 2210 O  O   . HOH G 7 .   ? -0.491  -8.548  32.485  1.00 22.97 ? 340 HOH A O   1 
HETATM 2211 O  O   . HOH G 7 .   ? -6.674  -14.859 31.585  1.00 20.49 ? 341 HOH A O   1 
HETATM 2212 O  O   . HOH G 7 .   ? -11.000 -15.278 34.158  1.00 23.90 ? 342 HOH A O   1 
HETATM 2213 O  O   . HOH G 7 .   ? -17.680 -21.980 5.862   1.00 18.19 ? 343 HOH A O   1 
HETATM 2214 O  O   . HOH G 7 .   ? -0.933  -11.167 28.974  1.00 19.93 ? 344 HOH A O   1 
HETATM 2215 O  O   . HOH G 7 .   ? -16.045 15.828  23.642  1.00 22.86 ? 345 HOH A O   1 
HETATM 2216 O  O   . HOH G 7 .   ? -9.958  14.696  12.171  1.00 22.16 ? 346 HOH A O   1 
HETATM 2217 O  O   . HOH G 7 .   ? 11.272  1.446   25.982  1.00 24.29 ? 347 HOH A O   1 
HETATM 2218 O  O   . HOH G 7 .   ? -8.385  -17.341 34.878  1.00 20.90 ? 348 HOH A O   1 
HETATM 2219 O  O   . HOH G 7 .   ? -24.598 -9.367  2.125   1.00 23.79 ? 349 HOH A O   1 
HETATM 2220 O  O   . HOH G 7 .   ? -22.929 -11.653 14.132  1.00 21.56 ? 350 HOH A O   1 
HETATM 2221 O  O   . HOH G 7 .   ? -23.463 16.508  2.544   1.00 21.40 ? 351 HOH A O   1 
HETATM 2222 O  O   . HOH G 7 .   ? -14.828 -20.999 17.728  1.00 25.68 ? 352 HOH A O   1 
HETATM 2223 O  O   . HOH G 7 .   ? -8.120  0.591   -6.352  1.00 26.62 ? 353 HOH A O   1 
HETATM 2224 O  O   . HOH G 7 .   ? -15.263 -16.562 25.467  1.00 28.00 ? 354 HOH A O   1 
HETATM 2225 O  O   . HOH G 7 .   ? -27.464 2.731   23.510  1.00 28.02 ? 355 HOH A O   1 
HETATM 2226 O  O   . HOH G 7 .   ? 2.837   -4.214  7.644   1.00 26.73 ? 356 HOH A O   1 
HETATM 2227 O  O   . HOH G 7 .   ? -8.489  -19.811 26.650  1.00 21.01 ? 357 HOH A O   1 
HETATM 2228 O  O   . HOH G 7 .   ? -1.783  -12.087 31.378  1.00 33.80 ? 358 HOH A O   1 
HETATM 2229 O  O   . HOH G 7 .   ? -27.121 -6.913  7.794   1.00 33.47 ? 359 HOH A O   1 
HETATM 2230 O  O   . HOH G 7 .   ? -25.761 -6.203  13.095  1.00 26.62 ? 360 HOH A O   1 
HETATM 2231 O  O   . HOH G 7 .   ? -25.570 4.205   4.107   1.00 31.89 ? 361 HOH A O   1 
HETATM 2232 O  O   . HOH G 7 .   ? -5.953  -19.744 23.873  1.00 23.14 ? 362 HOH A O   1 
HETATM 2233 O  O   . HOH G 7 .   ? -13.811 14.183  27.232  1.00 26.63 ? 363 HOH A O   1 
HETATM 2234 O  O   . HOH G 7 .   ? -8.876  -5.816  35.885  1.00 19.25 ? 364 HOH A O   1 
HETATM 2235 O  O   . HOH G 7 .   ? -13.646 -21.085 15.019  1.00 22.41 ? 365 HOH A O   1 
HETATM 2236 O  O   . HOH G 7 .   ? -19.104 14.262  35.231  1.00 22.25 ? 366 HOH A O   1 
HETATM 2237 O  O   . HOH G 7 .   ? -9.643  1.429   39.010  1.00 28.82 ? 367 HOH A O   1 
HETATM 2238 O  O   . HOH G 7 .   ? -0.126  -14.114 22.404  1.00 21.47 ? 368 HOH A O   1 
HETATM 2239 O  O   . HOH G 7 .   ? -30.957 -6.910  22.345  1.00 28.09 ? 369 HOH A O   1 
HETATM 2240 O  O   . HOH G 7 .   ? -12.293 12.554  29.142  1.00 21.50 ? 370 HOH A O   1 
HETATM 2241 O  O   . HOH G 7 .   ? -15.664 8.946   -2.000  1.00 25.55 ? 371 HOH A O   1 
HETATM 2242 O  O   . HOH G 7 .   ? 0.128   -1.054  -4.740  1.00 22.65 ? 372 HOH A O   1 
HETATM 2243 O  O   . HOH G 7 .   ? -1.345  11.333  25.981  1.00 28.77 ? 373 HOH A O   1 
HETATM 2244 O  O   . HOH G 7 .   ? -23.852 -16.826 3.743   1.00 29.93 ? 374 HOH A O   1 
HETATM 2245 O  O   . HOH G 7 .   ? -21.214 -19.606 6.439   1.00 25.53 ? 375 HOH A O   1 
HETATM 2246 O  O   . HOH G 7 .   ? 2.351   -14.111 20.694  1.00 27.20 ? 376 HOH A O   1 
HETATM 2247 O  O   . HOH G 7 .   ? -0.929  -17.580 18.099  1.00 28.37 ? 377 HOH A O   1 
HETATM 2248 O  O   . HOH G 7 .   ? -3.592  -12.980 -2.821  1.00 22.95 ? 378 HOH A O   1 
HETATM 2249 O  O   . HOH G 7 .   ? -5.312  3.500   -5.802  1.00 27.98 ? 379 HOH A O   1 
HETATM 2250 O  O   . HOH G 7 .   ? -28.255 -0.041  6.297   1.00 27.92 ? 380 HOH A O   1 
HETATM 2251 O  O   . HOH G 7 .   ? -17.584 -8.535  -6.231  1.00 25.02 ? 381 HOH A O   1 
HETATM 2252 O  O   . HOH G 7 .   ? -17.657 -19.271 35.131  1.00 27.23 ? 382 HOH A O   1 
HETATM 2253 O  O   . HOH G 7 .   ? 4.655   -2.527  28.987  1.00 22.84 ? 383 HOH A O   1 
HETATM 2254 O  O   . HOH G 7 .   ? -10.973 0.993   33.635  1.00 25.30 ? 384 HOH A O   1 
HETATM 2255 O  O   . HOH G 7 .   ? -23.590 8.282   3.453   1.00 22.75 ? 385 HOH A O   1 
HETATM 2256 O  O   . HOH G 7 .   ? -25.508 -10.618 17.687  1.00 26.21 ? 386 HOH A O   1 
HETATM 2257 O  O   . HOH G 7 .   ? -16.304 -15.211 32.768  1.00 34.34 ? 387 HOH A O   1 
HETATM 2258 O  O   . HOH G 7 .   ? -4.692  -20.818 21.408  1.00 20.89 ? 388 HOH A O   1 
HETATM 2259 O  O   . HOH G 7 .   ? -5.095  2.117   37.210  1.00 30.56 ? 389 HOH A O   1 
HETATM 2260 O  O   . HOH G 7 .   ? -2.726  7.258   -5.182  1.00 22.02 ? 390 HOH A O   1 
HETATM 2261 O  O   . HOH G 7 .   ? -17.028 -23.129 3.876   1.00 29.72 ? 391 HOH A O   1 
HETATM 2262 O  O   . HOH G 7 .   ? -3.747  -15.489 -2.278  1.00 30.15 ? 392 HOH A O   1 
HETATM 2263 O  O   . HOH G 7 .   ? 8.690   -4.722  23.764  1.00 24.82 ? 393 HOH A O   1 
HETATM 2264 O  O   . HOH G 7 .   ? 2.208   8.093   27.738  1.00 26.64 ? 394 HOH A O   1 
HETATM 2265 O  O   . HOH G 7 .   ? -27.851 4.946   25.619  1.00 31.22 ? 395 HOH A O   1 
HETATM 2266 O  O   . HOH G 7 .   ? -23.225 -13.236 11.357  1.00 23.29 ? 396 HOH A O   1 
HETATM 2267 O  O   . HOH G 7 .   ? -8.938  5.250   32.924  1.00 25.13 ? 397 HOH A O   1 
HETATM 2268 O  O   . HOH G 7 .   ? 10.364  -2.582  13.664  1.00 28.82 ? 398 HOH A O   1 
HETATM 2269 O  O   . HOH G 7 .   ? -10.539 -19.455 19.817  1.00 26.20 ? 399 HOH A O   1 
HETATM 2270 O  O   . HOH G 7 .   ? -24.355 -17.560 6.745   1.00 41.27 ? 400 HOH A O   1 
HETATM 2271 O  O   . HOH G 7 .   ? -16.829 -17.987 20.111  1.00 22.94 ? 401 HOH A O   1 
HETATM 2272 O  O   . HOH G 7 .   ? -25.879 6.186   27.012  1.00 21.58 ? 402 HOH A O   1 
HETATM 2273 O  O   . HOH G 7 .   ? -32.507 1.980   11.937  1.00 30.00 ? 403 HOH A O   1 
HETATM 2274 O  O   . HOH G 7 .   ? -4.586  -7.337  37.856  1.00 32.85 ? 404 HOH A O   1 
HETATM 2275 O  O   . HOH G 7 .   ? -28.919 -3.883  13.511  1.00 25.10 ? 405 HOH A O   1 
HETATM 2276 O  O   . HOH G 7 .   ? 3.893   9.675   23.703  1.00 24.14 ? 406 HOH A O   1 
HETATM 2277 O  O   . HOH G 7 .   ? -12.958 -22.022 8.528   1.00 25.96 ? 407 HOH A O   1 
HETATM 2278 O  O   . HOH G 7 .   ? -1.966  -4.619  -6.937  1.00 28.50 ? 408 HOH A O   1 
HETATM 2279 O  O   . HOH G 7 .   ? -23.997 -6.884  0.259   1.00 25.71 ? 409 HOH A O   1 
HETATM 2280 O  O   . HOH G 7 .   ? -19.326 -20.614 5.000   1.00 26.24 ? 410 HOH A O   1 
HETATM 2281 O  O   . HOH G 7 .   ? 1.756   12.397  22.796  1.00 26.01 ? 411 HOH A O   1 
HETATM 2282 O  O   . HOH G 7 .   ? 10.427  -7.059  -8.649  1.00 31.23 ? 412 HOH A O   1 
HETATM 2283 O  O   . HOH G 7 .   ? -13.158 -22.347 12.226  1.00 36.26 ? 413 HOH A O   1 
HETATM 2284 O  O   . HOH G 7 .   ? -16.878 -13.909 37.491  1.00 29.25 ? 414 HOH A O   1 
HETATM 2285 O  O   . HOH G 7 .   ? -31.730 5.655   13.094  1.00 34.16 ? 415 HOH A O   1 
HETATM 2286 O  O   . HOH G 7 .   ? -26.565 -1.261  26.025  1.00 24.96 ? 416 HOH A O   1 
HETATM 2287 O  O   . HOH G 7 .   ? -6.356  -5.221  37.411  1.00 20.96 ? 417 HOH A O   1 
HETATM 2288 O  O   . HOH G 7 .   ? 5.127   -7.343  22.250  1.00 27.10 ? 418 HOH A O   1 
HETATM 2289 O  O   . HOH G 7 .   ? -20.053 13.831  29.301  1.00 43.85 ? 419 HOH A O   1 
HETATM 2290 O  O   . HOH G 7 .   ? -5.839  -11.218 36.353  1.00 26.28 ? 420 HOH A O   1 
HETATM 2291 O  O   . HOH G 7 .   ? 9.805   -4.498  -7.731  1.00 32.20 ? 421 HOH A O   1 
HETATM 2292 O  O   . HOH G 7 .   ? -18.837 -8.952  34.316  1.00 28.82 ? 422 HOH A O   1 
HETATM 2293 O  O   . HOH G 7 .   ? -26.067 3.450   15.364  1.00 31.20 ? 423 HOH A O   1 
HETATM 2294 O  O   . HOH G 7 .   ? -6.103  15.115  11.967  1.00 27.53 ? 424 HOH A O   1 
HETATM 2295 O  O   . HOH G 7 .   ? 14.166  -1.334  28.350  1.00 26.90 ? 425 HOH A O   1 
HETATM 2296 O  O   . HOH G 7 .   ? -12.563 10.992  35.491  1.00 32.16 ? 426 HOH A O   1 
HETATM 2297 O  O   . HOH G 7 .   ? 2.401   2.889   -5.154  1.00 31.05 ? 427 HOH A O   1 
HETATM 2298 O  O   . HOH G 7 .   ? -19.497 -23.656 6.014   1.00 29.90 ? 428 HOH A O   1 
HETATM 2299 O  O   . HOH G 7 .   ? 12.145  -6.577  8.076   1.00 29.35 ? 429 HOH A O   1 
HETATM 2300 O  O   . HOH G 7 .   ? -4.265  -8.496  31.213  1.00 25.45 ? 430 HOH A O   1 
HETATM 2301 O  O   . HOH G 7 .   ? 3.400   1.199   -1.628  1.00 34.58 ? 431 HOH A O   1 
HETATM 2302 O  O   . HOH G 7 .   ? 0.626   0.480   -6.794  1.00 25.95 ? 432 HOH A O   1 
HETATM 2303 O  O   . HOH G 7 .   ? -7.037  -16.944 1.495   1.00 19.44 ? 433 HOH A O   1 
HETATM 2304 O  O   . HOH G 7 .   ? 14.272  -4.447  10.072  1.00 30.99 ? 434 HOH A O   1 
HETATM 2305 O  O   . HOH G 7 .   ? 9.822   -13.328 9.366   1.00 32.48 ? 435 HOH A O   1 
HETATM 2306 O  O   . HOH G 7 .   ? 10.624  -9.012  9.133   1.00 34.70 ? 436 HOH A O   1 
HETATM 2307 O  O   . HOH G 7 .   ? 11.599  -0.526  16.005  1.00 29.68 ? 437 HOH A O   1 
HETATM 2308 O  O   . HOH G 7 .   ? 8.466   3.238   27.696  1.00 27.39 ? 438 HOH A O   1 
HETATM 2309 O  O   . HOH G 7 .   ? -15.128 -10.370 37.107  1.00 31.92 ? 439 HOH A O   1 
HETATM 2310 O  O   . HOH G 7 .   ? -17.078 -7.408  39.678  1.00 27.37 ? 440 HOH A O   1 
HETATM 2311 O  O   . HOH G 7 .   ? -4.745  7.142   5.872   1.00 32.18 ? 441 HOH A O   1 
HETATM 2312 O  O   . HOH G 7 .   ? -20.888 -20.632 1.928   1.00 37.02 ? 442 HOH A O   1 
HETATM 2313 O  O   . HOH G 7 .   ? -13.851 -8.968  -5.032  1.00 33.94 ? 443 HOH A O   1 
HETATM 2314 O  O   . HOH G 7 .   ? -10.312 5.040   30.923  1.00 30.14 ? 444 HOH A O   1 
HETATM 2315 O  O   . HOH G 7 .   ? 4.374   -11.458 23.350  1.00 29.07 ? 445 HOH A O   1 
HETATM 2316 O  O   . HOH G 7 .   ? -23.897 -2.449  28.995  1.00 26.76 ? 446 HOH A O   1 
HETATM 2317 O  O   . HOH G 7 .   ? -6.058  -20.696 26.223  1.00 28.86 ? 447 HOH A O   1 
HETATM 2318 O  O   . HOH G 7 .   ? -3.910  0.435   13.625  1.00 25.33 ? 448 HOH A O   1 
HETATM 2319 O  O   . HOH G 7 .   ? -3.950  -0.996  11.519  1.00 37.01 ? 449 HOH A O   1 
HETATM 2320 O  O   . HOH G 7 .   ? 15.358  3.232   20.648  1.00 38.78 ? 450 HOH A O   1 
HETATM 2321 O  O   . HOH G 7 .   ? 6.638   5.337   28.868  1.00 31.56 ? 451 HOH A O   1 
HETATM 2322 O  O   . HOH G 7 .   ? -27.968 5.792   19.123  1.00 36.41 ? 452 HOH A O   1 
HETATM 2323 O  O   . HOH G 7 .   ? -25.232 11.043  19.415  1.00 41.44 ? 453 HOH A O   1 
HETATM 2324 O  O   . HOH G 7 .   ? -3.420  17.839  21.452  1.00 30.74 ? 454 HOH A O   1 
HETATM 2325 O  O   . HOH G 7 .   ? -6.964  -8.405  -7.209  1.00 44.10 ? 455 HOH A O   1 
HETATM 2326 O  O   . HOH G 7 .   ? -21.868 -13.991 18.604  1.00 33.57 ? 456 HOH A O   1 
HETATM 2327 O  O   . HOH G 7 .   ? -4.560  -15.868 0.727   1.00 31.62 ? 457 HOH A O   1 
HETATM 2328 O  O   . HOH G 7 .   ? -8.452  7.559   8.354   1.00 28.40 ? 458 HOH A O   1 
HETATM 2329 O  O   . HOH G 7 .   ? -12.121 10.575  5.700   1.00 28.93 ? 459 HOH A O   1 
HETATM 2330 O  O   . HOH G 7 .   ? -5.701  8.584   10.661  1.00 38.77 ? 460 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   262 1   ZN  ZN  A . 
C 3 BCN 1   263 1   BCN BCN A . 
D 4 MES 1   264 1   MES MES A . 
E 5 DMS 1   265 1   DMS DMS A . 
F 6 E2I 1   266 1   E2I E2I A . 
G 7 HOH 1   126 126 HOH HOH A . 
G 7 HOH 2   267 1   HOH HOH A . 
G 7 HOH 3   268 2   HOH HOH A . 
G 7 HOH 4   269 3   HOH HOH A . 
G 7 HOH 5   270 4   HOH HOH A . 
G 7 HOH 6   271 5   HOH HOH A . 
G 7 HOH 7   272 6   HOH HOH A . 
G 7 HOH 8   273 7   HOH HOH A . 
G 7 HOH 9   274 8   HOH HOH A . 
G 7 HOH 10  275 9   HOH HOH A . 
G 7 HOH 11  276 10  HOH HOH A . 
G 7 HOH 12  277 11  HOH HOH A . 
G 7 HOH 13  278 12  HOH HOH A . 
G 7 HOH 14  279 13  HOH HOH A . 
G 7 HOH 15  280 14  HOH HOH A . 
G 7 HOH 16  281 15  HOH HOH A . 
G 7 HOH 17  282 16  HOH HOH A . 
G 7 HOH 18  283 17  HOH HOH A . 
G 7 HOH 19  284 18  HOH HOH A . 
G 7 HOH 20  285 19  HOH HOH A . 
G 7 HOH 21  286 20  HOH HOH A . 
G 7 HOH 22  287 21  HOH HOH A . 
G 7 HOH 23  288 22  HOH HOH A . 
G 7 HOH 24  289 23  HOH HOH A . 
G 7 HOH 25  290 24  HOH HOH A . 
G 7 HOH 26  291 25  HOH HOH A . 
G 7 HOH 27  292 26  HOH HOH A . 
G 7 HOH 28  293 27  HOH HOH A . 
G 7 HOH 29  294 28  HOH HOH A . 
G 7 HOH 30  295 29  HOH HOH A . 
G 7 HOH 31  296 30  HOH HOH A . 
G 7 HOH 32  297 31  HOH HOH A . 
G 7 HOH 33  298 32  HOH HOH A . 
G 7 HOH 34  299 33  HOH HOH A . 
G 7 HOH 35  300 34  HOH HOH A . 
G 7 HOH 36  301 35  HOH HOH A . 
G 7 HOH 37  302 36  HOH HOH A . 
G 7 HOH 38  303 37  HOH HOH A . 
G 7 HOH 39  304 38  HOH HOH A . 
G 7 HOH 40  305 39  HOH HOH A . 
G 7 HOH 41  306 40  HOH HOH A . 
G 7 HOH 42  307 41  HOH HOH A . 
G 7 HOH 43  308 42  HOH HOH A . 
G 7 HOH 44  309 43  HOH HOH A . 
G 7 HOH 45  310 44  HOH HOH A . 
G 7 HOH 46  311 45  HOH HOH A . 
G 7 HOH 47  312 46  HOH HOH A . 
G 7 HOH 48  313 47  HOH HOH A . 
G 7 HOH 49  314 48  HOH HOH A . 
G 7 HOH 50  315 49  HOH HOH A . 
G 7 HOH 51  316 50  HOH HOH A . 
G 7 HOH 52  317 51  HOH HOH A . 
G 7 HOH 53  318 52  HOH HOH A . 
G 7 HOH 54  319 53  HOH HOH A . 
G 7 HOH 55  320 54  HOH HOH A . 
G 7 HOH 56  321 55  HOH HOH A . 
G 7 HOH 57  322 56  HOH HOH A . 
G 7 HOH 58  323 57  HOH HOH A . 
G 7 HOH 59  324 58  HOH HOH A . 
G 7 HOH 60  325 59  HOH HOH A . 
G 7 HOH 61  326 60  HOH HOH A . 
G 7 HOH 62  327 61  HOH HOH A . 
G 7 HOH 63  328 62  HOH HOH A . 
G 7 HOH 64  329 63  HOH HOH A . 
G 7 HOH 65  330 64  HOH HOH A . 
G 7 HOH 66  331 65  HOH HOH A . 
G 7 HOH 67  332 66  HOH HOH A . 
G 7 HOH 68  333 67  HOH HOH A . 
G 7 HOH 69  334 68  HOH HOH A . 
G 7 HOH 70  335 69  HOH HOH A . 
G 7 HOH 71  336 70  HOH HOH A . 
G 7 HOH 72  337 71  HOH HOH A . 
G 7 HOH 73  338 72  HOH HOH A . 
G 7 HOH 74  339 73  HOH HOH A . 
G 7 HOH 75  340 74  HOH HOH A . 
G 7 HOH 76  341 75  HOH HOH A . 
G 7 HOH 77  342 76  HOH HOH A . 
G 7 HOH 78  343 77  HOH HOH A . 
G 7 HOH 79  344 78  HOH HOH A . 
G 7 HOH 80  345 79  HOH HOH A . 
G 7 HOH 81  346 80  HOH HOH A . 
G 7 HOH 82  347 81  HOH HOH A . 
G 7 HOH 83  348 82  HOH HOH A . 
G 7 HOH 84  349 83  HOH HOH A . 
G 7 HOH 85  350 84  HOH HOH A . 
G 7 HOH 86  351 85  HOH HOH A . 
G 7 HOH 87  352 86  HOH HOH A . 
G 7 HOH 88  353 87  HOH HOH A . 
G 7 HOH 89  354 88  HOH HOH A . 
G 7 HOH 90  355 89  HOH HOH A . 
G 7 HOH 91  356 90  HOH HOH A . 
G 7 HOH 92  357 91  HOH HOH A . 
G 7 HOH 93  358 92  HOH HOH A . 
G 7 HOH 94  359 93  HOH HOH A . 
G 7 HOH 95  360 94  HOH HOH A . 
G 7 HOH 96  361 95  HOH HOH A . 
G 7 HOH 97  362 96  HOH HOH A . 
G 7 HOH 98  363 97  HOH HOH A . 
G 7 HOH 99  364 98  HOH HOH A . 
G 7 HOH 100 365 99  HOH HOH A . 
G 7 HOH 101 366 100 HOH HOH A . 
G 7 HOH 102 367 101 HOH HOH A . 
G 7 HOH 103 368 102 HOH HOH A . 
G 7 HOH 104 369 103 HOH HOH A . 
G 7 HOH 105 370 104 HOH HOH A . 
G 7 HOH 106 371 105 HOH HOH A . 
G 7 HOH 107 372 106 HOH HOH A . 
G 7 HOH 108 373 107 HOH HOH A . 
G 7 HOH 109 374 108 HOH HOH A . 
G 7 HOH 110 375 109 HOH HOH A . 
G 7 HOH 111 376 110 HOH HOH A . 
G 7 HOH 112 377 111 HOH HOH A . 
G 7 HOH 113 378 112 HOH HOH A . 
G 7 HOH 114 379 113 HOH HOH A . 
G 7 HOH 115 380 114 HOH HOH A . 
G 7 HOH 116 381 115 HOH HOH A . 
G 7 HOH 117 382 116 HOH HOH A . 
G 7 HOH 118 383 117 HOH HOH A . 
G 7 HOH 119 384 118 HOH HOH A . 
G 7 HOH 120 385 119 HOH HOH A . 
G 7 HOH 121 386 120 HOH HOH A . 
G 7 HOH 122 387 121 HOH HOH A . 
G 7 HOH 123 388 122 HOH HOH A . 
G 7 HOH 124 389 123 HOH HOH A . 
G 7 HOH 125 390 124 HOH HOH A . 
G 7 HOH 126 391 125 HOH HOH A . 
G 7 HOH 127 392 127 HOH HOH A . 
G 7 HOH 128 393 128 HOH HOH A . 
G 7 HOH 129 394 129 HOH HOH A . 
G 7 HOH 130 395 130 HOH HOH A . 
G 7 HOH 131 396 131 HOH HOH A . 
G 7 HOH 132 397 132 HOH HOH A . 
G 7 HOH 133 398 133 HOH HOH A . 
G 7 HOH 134 399 134 HOH HOH A . 
G 7 HOH 135 400 135 HOH HOH A . 
G 7 HOH 136 401 136 HOH HOH A . 
G 7 HOH 137 402 137 HOH HOH A . 
G 7 HOH 138 403 138 HOH HOH A . 
G 7 HOH 139 404 139 HOH HOH A . 
G 7 HOH 140 405 140 HOH HOH A . 
G 7 HOH 141 406 141 HOH HOH A . 
G 7 HOH 142 407 142 HOH HOH A . 
G 7 HOH 143 408 143 HOH HOH A . 
G 7 HOH 144 409 144 HOH HOH A . 
G 7 HOH 145 410 145 HOH HOH A . 
G 7 HOH 146 411 146 HOH HOH A . 
G 7 HOH 147 412 147 HOH HOH A . 
G 7 HOH 148 413 148 HOH HOH A . 
G 7 HOH 149 414 149 HOH HOH A . 
G 7 HOH 150 415 150 HOH HOH A . 
G 7 HOH 151 416 151 HOH HOH A . 
G 7 HOH 152 417 152 HOH HOH A . 
G 7 HOH 153 418 153 HOH HOH A . 
G 7 HOH 154 419 154 HOH HOH A . 
G 7 HOH 155 420 155 HOH HOH A . 
G 7 HOH 156 421 156 HOH HOH A . 
G 7 HOH 157 422 157 HOH HOH A . 
G 7 HOH 158 423 158 HOH HOH A . 
G 7 HOH 159 424 159 HOH HOH A . 
G 7 HOH 160 425 160 HOH HOH A . 
G 7 HOH 161 426 161 HOH HOH A . 
G 7 HOH 162 427 162 HOH HOH A . 
G 7 HOH 163 428 163 HOH HOH A . 
G 7 HOH 164 429 164 HOH HOH A . 
G 7 HOH 165 430 165 HOH HOH A . 
G 7 HOH 166 431 166 HOH HOH A . 
G 7 HOH 167 432 167 HOH HOH A . 
G 7 HOH 168 433 168 HOH HOH A . 
G 7 HOH 169 434 169 HOH HOH A . 
G 7 HOH 170 435 170 HOH HOH A . 
G 7 HOH 171 436 171 HOH HOH A . 
G 7 HOH 172 437 172 HOH HOH A . 
G 7 HOH 173 438 173 HOH HOH A . 
G 7 HOH 174 439 174 HOH HOH A . 
G 7 HOH 175 440 175 HOH HOH A . 
G 7 HOH 176 441 176 HOH HOH A . 
G 7 HOH 177 442 177 HOH HOH A . 
G 7 HOH 178 443 178 HOH HOH A . 
G 7 HOH 179 444 179 HOH HOH A . 
G 7 HOH 180 445 180 HOH HOH A . 
G 7 HOH 181 446 181 HOH HOH A . 
G 7 HOH 182 447 182 HOH HOH A . 
G 7 HOH 183 448 183 HOH HOH A . 
G 7 HOH 184 449 184 HOH HOH A . 
G 7 HOH 185 450 185 HOH HOH A . 
G 7 HOH 186 451 186 HOH HOH A . 
G 7 HOH 187 452 187 HOH HOH A . 
G 7 HOH 188 453 188 HOH HOH A . 
G 7 HOH 189 454 189 HOH HOH A . 
G 7 HOH 190 455 190 HOH HOH A . 
G 7 HOH 191 456 191 HOH HOH A . 
G 7 HOH 192 457 192 HOH HOH A . 
G 7 HOH 193 458 193 HOH HOH A . 
G 7 HOH 194 459 194 HOH HOH A . 
G 7 HOH 195 460 195 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 262 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 107.7 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 115.4 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 97.5  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N48 ? F E2I .   ? A E2I 266 ? 1_555 106.8 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N48 ? F E2I .   ? A E2I 266 ? 1_555 108.5 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N48 ? F E2I .   ? A E2I 266 ? 1_555 119.8 ? 
# 
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 2012-04-11 
2 'Structure model' 1 1 2012-05-16 
3 'Structure model' 1 2 2017-09-27 
4 'Structure model' 1 3 2017-11-15 
5 'Structure model' 1 4 2023-09-13 
# 
_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' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Refinement description' 
4 4 'Structure model' 'Database references'    
5 5 'Structure model' 'Data collection'        
6 5 'Structure model' 'Database references'    
7 5 'Structure model' 'Derived calculations'   
8 5 '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  3 'Structure model' diffrn_detector               
2  3 'Structure model' software                      
3  4 'Structure model' pdbx_database_related         
4  5 'Structure model' chem_comp_atom                
5  5 'Structure model' chem_comp_bond                
6  5 'Structure model' database_2                    
7  5 'Structure model' diffrn_source                 
8  5 'Structure model' pdbx_initial_refinement_model 
9  5 'Structure model' pdbx_struct_conn_angle        
10 5 'Structure model' struct_conn                   
11 5 '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  3 'Structure model' '_diffrn_detector.detector'                   
2  4 'Structure model' '_pdbx_database_related.db_name'              
3  5 'Structure model' '_database_2.pdbx_DOI'                        
4  5 'Structure model' '_database_2.pdbx_database_accession'         
5  5 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
6  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
7  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
8  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
9  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
10 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
11 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
12 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
13 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
14 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
15 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
16 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
17 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
18 5 'Structure model' '_pdbx_struct_conn_angle.value'               
19 5 'Structure model' '_struct_conn.pdbx_dist_value'                
20 5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
21 5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
22 5 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
23 5 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
24 5 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
25 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
26 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
27 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
28 5 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
29 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
30 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
31 5 'Structure model' '_struct_site.pdbx_auth_asym_id'              
32 5 'Structure model' '_struct_site.pdbx_auth_comp_id'              
33 5 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.2.19 22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
# 
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  ? ? -140.19 56.42   
2 1 ALA A 65  ? ? -160.85 -168.39 
3 1 LYS A 111 ? ? 71.64   -1.23   
4 1 ASN A 244 ? ? -91.02  50.31   
5 1 LYS A 252 ? ? 57.21   -133.75 
# 
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 264 ? S   ? D MES 1 S   
2 1 N 1 A MES 264 ? O1S ? D MES 1 O1S 
3 1 N 1 A MES 264 ? O2S ? D MES 1 O2S 
4 1 N 1 A MES 264 ? O3S ? D MES 1 O3S 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
E2I N1   N  Y N 122 
E2I C2   C  Y N 123 
E2I C3   C  Y N 124 
E2I C4   C  Y N 125 
E2I N5   N  Y N 126 
E2I C6   C  Y N 127 
E2I C13  C  N N 128 
E2I C15  C  N N 129 
E2I C17  C  N N 130 
E2I C19  C  N N 131 
E2I S21  S  N N 132 
E2I C23  C  N N 133 
E2I C25  C  N N 134 
E2I O27  O  N N 135 
E2I C29  C  Y N 136 
E2I C31  C  Y N 137 
E2I C32  C  Y N 138 
E2I C33  C  Y N 139 
E2I C34  C  Y N 140 
E2I C35  C  Y N 141 
E2I S42  S  N N 142 
E2I O44  O  N N 143 
E2I O46  O  N N 144 
E2I N48  N  N N 145 
E2I H2   H  N N 146 
E2I H4   H  N N 147 
E2I H13  H  N N 148 
E2I H13A H  N N 149 
E2I H15  H  N N 150 
E2I H15A H  N N 151 
E2I H17  H  N N 152 
E2I H17A H  N N 153 
E2I H19  H  N N 154 
E2I H19A H  N N 155 
E2I H19B H  N N 156 
E2I H23  H  N N 157 
E2I H23A H  N N 158 
E2I H31  H  N N 159 
E2I H32  H  N N 160 
E2I H34  H  N N 161 
E2I H35  H  N N 162 
E2I HN48 H  N N 163 
E2I HN4A H  N N 164 
GLN N    N  N N 165 
GLN CA   C  N S 166 
GLN C    C  N N 167 
GLN O    O  N N 168 
GLN CB   C  N N 169 
GLN CG   C  N N 170 
GLN CD   C  N N 171 
GLN OE1  O  N N 172 
GLN NE2  N  N N 173 
GLN OXT  O  N N 174 
GLN H    H  N N 175 
GLN H2   H  N N 176 
GLN HA   H  N N 177 
GLN HB2  H  N N 178 
GLN HB3  H  N N 179 
GLN HG2  H  N N 180 
GLN HG3  H  N N 181 
GLN HE21 H  N N 182 
GLN HE22 H  N N 183 
GLN HXT  H  N N 184 
GLU N    N  N N 185 
GLU CA   C  N S 186 
GLU C    C  N N 187 
GLU O    O  N N 188 
GLU CB   C  N N 189 
GLU CG   C  N N 190 
GLU CD   C  N N 191 
GLU OE1  O  N N 192 
GLU OE2  O  N N 193 
GLU OXT  O  N N 194 
GLU H    H  N N 195 
GLU H2   H  N N 196 
GLU HA   H  N N 197 
GLU HB2  H  N N 198 
GLU HB3  H  N N 199 
GLU HG2  H  N N 200 
GLU HG3  H  N N 201 
GLU HE2  H  N N 202 
GLU HXT  H  N N 203 
GLY N    N  N N 204 
GLY CA   C  N N 205 
GLY C    C  N N 206 
GLY O    O  N N 207 
GLY OXT  O  N N 208 
GLY H    H  N N 209 
GLY H2   H  N N 210 
GLY HA2  H  N N 211 
GLY HA3  H  N N 212 
GLY HXT  H  N N 213 
HIS N    N  N N 214 
HIS CA   C  N S 215 
HIS C    C  N N 216 
HIS O    O  N N 217 
HIS CB   C  N N 218 
HIS CG   C  Y N 219 
HIS ND1  N  Y N 220 
HIS CD2  C  Y N 221 
HIS CE1  C  Y N 222 
HIS NE2  N  Y N 223 
HIS OXT  O  N N 224 
HIS H    H  N N 225 
HIS H2   H  N N 226 
HIS HA   H  N N 227 
HIS HB2  H  N N 228 
HIS HB3  H  N N 229 
HIS HD1  H  N N 230 
HIS HD2  H  N N 231 
HIS HE1  H  N N 232 
HIS HE2  H  N N 233 
HIS HXT  H  N N 234 
HOH O    O  N N 235 
HOH H1   H  N N 236 
HOH H2   H  N N 237 
ILE N    N  N N 238 
ILE CA   C  N S 239 
ILE C    C  N N 240 
ILE O    O  N N 241 
ILE CB   C  N S 242 
ILE CG1  C  N N 243 
ILE CG2  C  N N 244 
ILE CD1  C  N N 245 
ILE OXT  O  N N 246 
ILE H    H  N N 247 
ILE H2   H  N N 248 
ILE HA   H  N N 249 
ILE HB   H  N N 250 
ILE HG12 H  N N 251 
ILE HG13 H  N N 252 
ILE HG21 H  N N 253 
ILE HG22 H  N N 254 
ILE HG23 H  N N 255 
ILE HD11 H  N N 256 
ILE HD12 H  N N 257 
ILE HD13 H  N N 258 
ILE HXT  H  N N 259 
LEU N    N  N N 260 
LEU CA   C  N S 261 
LEU C    C  N N 262 
LEU O    O  N N 263 
LEU CB   C  N N 264 
LEU CG   C  N N 265 
LEU CD1  C  N N 266 
LEU CD2  C  N N 267 
LEU OXT  O  N N 268 
LEU H    H  N N 269 
LEU H2   H  N N 270 
LEU HA   H  N N 271 
LEU HB2  H  N N 272 
LEU HB3  H  N N 273 
LEU HG   H  N N 274 
LEU HD11 H  N N 275 
LEU HD12 H  N N 276 
LEU HD13 H  N N 277 
LEU HD21 H  N N 278 
LEU HD22 H  N N 279 
LEU HD23 H  N N 280 
LEU HXT  H  N N 281 
LYS N    N  N N 282 
LYS CA   C  N S 283 
LYS C    C  N N 284 
LYS O    O  N N 285 
LYS CB   C  N N 286 
LYS CG   C  N N 287 
LYS CD   C  N N 288 
LYS CE   C  N N 289 
LYS NZ   N  N N 290 
LYS OXT  O  N N 291 
LYS H    H  N N 292 
LYS H2   H  N N 293 
LYS HA   H  N N 294 
LYS HB2  H  N N 295 
LYS HB3  H  N N 296 
LYS HG2  H  N N 297 
LYS HG3  H  N N 298 
LYS HD2  H  N N 299 
LYS HD3  H  N N 300 
LYS HE2  H  N N 301 
LYS HE3  H  N N 302 
LYS HZ1  H  N N 303 
LYS HZ2  H  N N 304 
LYS HZ3  H  N N 305 
LYS HXT  H  N N 306 
MES O1   O  N N 307 
MES C2   C  N N 308 
MES C3   C  N N 309 
MES N4   N  N N 310 
MES C5   C  N N 311 
MES C6   C  N N 312 
MES C7   C  N N 313 
MES C8   C  N N 314 
MES S    S  N N 315 
MES O1S  O  N N 316 
MES O2S  O  N N 317 
MES O3S  O  N N 318 
MES H21  H  N N 319 
MES H22  H  N N 320 
MES H31  H  N N 321 
MES H32  H  N N 322 
MES HN4  H  N N 323 
MES H51  H  N N 324 
MES H52  H  N N 325 
MES H61  H  N N 326 
MES H62  H  N N 327 
MES H71  H  N N 328 
MES H72  H  N N 329 
MES H81  H  N N 330 
MES H82  H  N N 331 
MET N    N  N N 332 
MET CA   C  N S 333 
MET C    C  N N 334 
MET O    O  N N 335 
MET CB   C  N N 336 
MET CG   C  N N 337 
MET SD   S  N N 338 
MET CE   C  N N 339 
MET OXT  O  N N 340 
MET H    H  N N 341 
MET H2   H  N N 342 
MET HA   H  N N 343 
MET HB2  H  N N 344 
MET HB3  H  N N 345 
MET HG2  H  N N 346 
MET HG3  H  N N 347 
MET HE1  H  N N 348 
MET HE2  H  N N 349 
MET HE3  H  N N 350 
MET HXT  H  N N 351 
PHE N    N  N N 352 
PHE CA   C  N S 353 
PHE C    C  N N 354 
PHE O    O  N N 355 
PHE CB   C  N N 356 
PHE CG   C  Y N 357 
PHE CD1  C  Y N 358 
PHE CD2  C  Y N 359 
PHE CE1  C  Y N 360 
PHE CE2  C  Y N 361 
PHE CZ   C  Y N 362 
PHE OXT  O  N N 363 
PHE H    H  N N 364 
PHE H2   H  N N 365 
PHE HA   H  N N 366 
PHE HB2  H  N N 367 
PHE HB3  H  N N 368 
PHE HD1  H  N N 369 
PHE HD2  H  N N 370 
PHE HE1  H  N N 371 
PHE HE2  H  N N 372 
PHE HZ   H  N N 373 
PHE HXT  H  N N 374 
PRO N    N  N N 375 
PRO CA   C  N S 376 
PRO C    C  N N 377 
PRO O    O  N N 378 
PRO CB   C  N N 379 
PRO CG   C  N N 380 
PRO CD   C  N N 381 
PRO OXT  O  N N 382 
PRO H    H  N N 383 
PRO HA   H  N N 384 
PRO HB2  H  N N 385 
PRO HB3  H  N N 386 
PRO HG2  H  N N 387 
PRO HG3  H  N N 388 
PRO HD2  H  N N 389 
PRO HD3  H  N N 390 
PRO HXT  H  N N 391 
SER N    N  N N 392 
SER CA   C  N S 393 
SER C    C  N N 394 
SER O    O  N N 395 
SER CB   C  N N 396 
SER OG   O  N N 397 
SER OXT  O  N N 398 
SER H    H  N N 399 
SER H2   H  N N 400 
SER HA   H  N N 401 
SER HB2  H  N N 402 
SER HB3  H  N N 403 
SER HG   H  N N 404 
SER HXT  H  N N 405 
THR N    N  N N 406 
THR CA   C  N S 407 
THR C    C  N N 408 
THR O    O  N N 409 
THR CB   C  N R 410 
THR OG1  O  N N 411 
THR CG2  C  N N 412 
THR OXT  O  N N 413 
THR H    H  N N 414 
THR H2   H  N N 415 
THR HA   H  N N 416 
THR HB   H  N N 417 
THR HG1  H  N N 418 
THR HG21 H  N N 419 
THR HG22 H  N N 420 
THR HG23 H  N N 421 
THR HXT  H  N N 422 
TRP N    N  N N 423 
TRP CA   C  N S 424 
TRP C    C  N N 425 
TRP O    O  N N 426 
TRP CB   C  N N 427 
TRP CG   C  Y N 428 
TRP CD1  C  Y N 429 
TRP CD2  C  Y N 430 
TRP NE1  N  Y N 431 
TRP CE2  C  Y N 432 
TRP CE3  C  Y N 433 
TRP CZ2  C  Y N 434 
TRP CZ3  C  Y N 435 
TRP CH2  C  Y N 436 
TRP OXT  O  N N 437 
TRP H    H  N N 438 
TRP H2   H  N N 439 
TRP HA   H  N N 440 
TRP HB2  H  N N 441 
TRP HB3  H  N N 442 
TRP HD1  H  N N 443 
TRP HE1  H  N N 444 
TRP HE3  H  N N 445 
TRP HZ2  H  N N 446 
TRP HZ3  H  N N 447 
TRP HH2  H  N N 448 
TRP HXT  H  N N 449 
TYR N    N  N N 450 
TYR CA   C  N S 451 
TYR C    C  N N 452 
TYR O    O  N N 453 
TYR CB   C  N N 454 
TYR CG   C  Y N 455 
TYR CD1  C  Y N 456 
TYR CD2  C  Y N 457 
TYR CE1  C  Y N 458 
TYR CE2  C  Y N 459 
TYR CZ   C  Y N 460 
TYR OH   O  N N 461 
TYR OXT  O  N N 462 
TYR H    H  N N 463 
TYR H2   H  N N 464 
TYR HA   H  N N 465 
TYR HB2  H  N N 466 
TYR HB3  H  N N 467 
TYR HD1  H  N N 468 
TYR HD2  H  N N 469 
TYR HE1  H  N N 470 
TYR HE2  H  N N 471 
TYR HH   H  N N 472 
TYR HXT  H  N N 473 
VAL N    N  N N 474 
VAL CA   C  N S 475 
VAL C    C  N N 476 
VAL O    O  N N 477 
VAL CB   C  N N 478 
VAL CG1  C  N N 479 
VAL CG2  C  N N 480 
VAL OXT  O  N N 481 
VAL H    H  N N 482 
VAL H2   H  N N 483 
VAL HA   H  N N 484 
VAL HB   H  N N 485 
VAL HG11 H  N N 486 
VAL HG12 H  N N 487 
VAL HG13 H  N N 488 
VAL HG21 H  N N 489 
VAL HG22 H  N N 490 
VAL HG23 H  N N 491 
VAL HXT  H  N N 492 
ZN  ZN   ZN N N 493 
# 
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  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
E2I C6  N1   doub Y N 115 
E2I N1  C2   sing Y N 116 
E2I C3  C2   doub Y N 117 
E2I C2  H2   sing N N 118 
E2I C4  C3   sing Y N 119 
E2I C3  C13  sing N N 120 
E2I N5  C4   doub Y N 121 
E2I C4  H4   sing N N 122 
E2I N5  C6   sing Y N 123 
E2I S21 C6   sing N N 124 
E2I C15 C13  sing N N 125 
E2I C13 H13  sing N N 126 
E2I C13 H13A sing N N 127 
E2I C15 C17  sing N N 128 
E2I C15 H15  sing N N 129 
E2I C15 H15A sing N N 130 
E2I C17 C19  sing N N 131 
E2I C17 H17  sing N N 132 
E2I C17 H17A sing N N 133 
E2I C19 H19  sing N N 134 
E2I C19 H19A sing N N 135 
E2I C19 H19B sing N N 136 
E2I S21 C23  sing N N 137 
E2I C25 C23  sing N N 138 
E2I C23 H23  sing N N 139 
E2I C23 H23A sing N N 140 
E2I O27 C25  doub N N 141 
E2I C25 C29  sing N N 142 
E2I C29 C31  doub Y N 143 
E2I C29 C35  sing Y N 144 
E2I C31 C32  sing Y N 145 
E2I C31 H31  sing N N 146 
E2I C32 C33  doub Y N 147 
E2I C32 H32  sing N N 148 
E2I C34 C33  sing Y N 149 
E2I C33 S42  sing N N 150 
E2I C35 C34  doub Y N 151 
E2I C34 H34  sing N N 152 
E2I C35 H35  sing N N 153 
E2I N48 S42  sing N N 154 
E2I O46 S42  doub N N 155 
E2I S42 O44  doub N N 156 
E2I N48 HN48 sing N N 157 
E2I N48 HN4A sing N N 158 
GLN N   CA   sing N N 159 
GLN N   H    sing N N 160 
GLN N   H2   sing N N 161 
GLN CA  C    sing N N 162 
GLN CA  CB   sing N N 163 
GLN CA  HA   sing N N 164 
GLN C   O    doub N N 165 
GLN C   OXT  sing N N 166 
GLN CB  CG   sing N N 167 
GLN CB  HB2  sing N N 168 
GLN CB  HB3  sing N N 169 
GLN CG  CD   sing N N 170 
GLN CG  HG2  sing N N 171 
GLN CG  HG3  sing N N 172 
GLN CD  OE1  doub N N 173 
GLN CD  NE2  sing N N 174 
GLN NE2 HE21 sing N N 175 
GLN NE2 HE22 sing N N 176 
GLN OXT HXT  sing N N 177 
GLU N   CA   sing N N 178 
GLU N   H    sing N N 179 
GLU N   H2   sing N N 180 
GLU CA  C    sing N N 181 
GLU CA  CB   sing N N 182 
GLU CA  HA   sing N N 183 
GLU C   O    doub N N 184 
GLU C   OXT  sing N N 185 
GLU CB  CG   sing N N 186 
GLU CB  HB2  sing N N 187 
GLU CB  HB3  sing N N 188 
GLU CG  CD   sing N N 189 
GLU CG  HG2  sing N N 190 
GLU CG  HG3  sing N N 191 
GLU CD  OE1  doub N N 192 
GLU CD  OE2  sing N N 193 
GLU OE2 HE2  sing N N 194 
GLU OXT HXT  sing N N 195 
GLY N   CA   sing N N 196 
GLY N   H    sing N N 197 
GLY N   H2   sing N N 198 
GLY CA  C    sing N N 199 
GLY CA  HA2  sing N N 200 
GLY CA  HA3  sing N N 201 
GLY C   O    doub N N 202 
GLY C   OXT  sing N N 203 
GLY OXT HXT  sing N N 204 
HIS N   CA   sing N N 205 
HIS N   H    sing N N 206 
HIS N   H2   sing N N 207 
HIS CA  C    sing N N 208 
HIS CA  CB   sing N N 209 
HIS CA  HA   sing N N 210 
HIS C   O    doub N N 211 
HIS C   OXT  sing N N 212 
HIS CB  CG   sing N N 213 
HIS CB  HB2  sing N N 214 
HIS CB  HB3  sing N N 215 
HIS CG  ND1  sing Y N 216 
HIS CG  CD2  doub Y N 217 
HIS ND1 CE1  doub Y N 218 
HIS ND1 HD1  sing N N 219 
HIS CD2 NE2  sing Y N 220 
HIS CD2 HD2  sing N N 221 
HIS CE1 NE2  sing Y N 222 
HIS CE1 HE1  sing N N 223 
HIS NE2 HE2  sing N N 224 
HIS OXT HXT  sing N N 225 
HOH O   H1   sing N N 226 
HOH O   H2   sing N N 227 
ILE N   CA   sing N N 228 
ILE N   H    sing N N 229 
ILE N   H2   sing N N 230 
ILE CA  C    sing N N 231 
ILE CA  CB   sing N N 232 
ILE CA  HA   sing N N 233 
ILE C   O    doub N N 234 
ILE C   OXT  sing N N 235 
ILE CB  CG1  sing N N 236 
ILE CB  CG2  sing N N 237 
ILE CB  HB   sing N N 238 
ILE CG1 CD1  sing N N 239 
ILE CG1 HG12 sing N N 240 
ILE CG1 HG13 sing N N 241 
ILE CG2 HG21 sing N N 242 
ILE CG2 HG22 sing N N 243 
ILE CG2 HG23 sing N N 244 
ILE CD1 HD11 sing N N 245 
ILE CD1 HD12 sing N N 246 
ILE CD1 HD13 sing N N 247 
ILE OXT HXT  sing N N 248 
LEU N   CA   sing N N 249 
LEU N   H    sing N N 250 
LEU N   H2   sing N N 251 
LEU CA  C    sing N N 252 
LEU CA  CB   sing N N 253 
LEU CA  HA   sing N N 254 
LEU C   O    doub N N 255 
LEU C   OXT  sing N N 256 
LEU CB  CG   sing N N 257 
LEU CB  HB2  sing N N 258 
LEU CB  HB3  sing N N 259 
LEU CG  CD1  sing N N 260 
LEU CG  CD2  sing N N 261 
LEU CG  HG   sing N N 262 
LEU CD1 HD11 sing N N 263 
LEU CD1 HD12 sing N N 264 
LEU CD1 HD13 sing N N 265 
LEU CD2 HD21 sing N N 266 
LEU CD2 HD22 sing N N 267 
LEU CD2 HD23 sing N N 268 
LEU OXT HXT  sing N N 269 
LYS N   CA   sing N N 270 
LYS N   H    sing N N 271 
LYS N   H2   sing N N 272 
LYS CA  C    sing N N 273 
LYS CA  CB   sing N N 274 
LYS CA  HA   sing N N 275 
LYS C   O    doub N N 276 
LYS C   OXT  sing N N 277 
LYS CB  CG   sing N N 278 
LYS CB  HB2  sing N N 279 
LYS CB  HB3  sing N N 280 
LYS CG  CD   sing N N 281 
LYS CG  HG2  sing N N 282 
LYS CG  HG3  sing N N 283 
LYS CD  CE   sing N N 284 
LYS CD  HD2  sing N N 285 
LYS CD  HD3  sing N N 286 
LYS CE  NZ   sing N N 287 
LYS CE  HE2  sing N N 288 
LYS CE  HE3  sing N N 289 
LYS NZ  HZ1  sing N N 290 
LYS NZ  HZ2  sing N N 291 
LYS NZ  HZ3  sing N N 292 
LYS OXT HXT  sing N N 293 
MES O1  C2   sing N N 294 
MES O1  C6   sing N N 295 
MES C2  C3   sing N N 296 
MES C2  H21  sing N N 297 
MES C2  H22  sing N N 298 
MES C3  N4   sing N N 299 
MES C3  H31  sing N N 300 
MES C3  H32  sing N N 301 
MES N4  C5   sing N N 302 
MES N4  C7   sing N N 303 
MES N4  HN4  sing N N 304 
MES C5  C6   sing N N 305 
MES C5  H51  sing N N 306 
MES C5  H52  sing N N 307 
MES C6  H61  sing N N 308 
MES C6  H62  sing N N 309 
MES C7  C8   sing N N 310 
MES C7  H71  sing N N 311 
MES C7  H72  sing N N 312 
MES C8  S    sing N N 313 
MES C8  H81  sing N N 314 
MES C8  H82  sing N N 315 
MES S   O1S  doub N N 316 
MES S   O2S  doub N N 317 
MES S   O3S  sing N N 318 
MET N   CA   sing N N 319 
MET N   H    sing N N 320 
MET N   H2   sing N N 321 
MET CA  C    sing N N 322 
MET CA  CB   sing N N 323 
MET CA  HA   sing N N 324 
MET C   O    doub N N 325 
MET C   OXT  sing N N 326 
MET CB  CG   sing N N 327 
MET CB  HB2  sing N N 328 
MET CB  HB3  sing N N 329 
MET CG  SD   sing N N 330 
MET CG  HG2  sing N N 331 
MET CG  HG3  sing N N 332 
MET SD  CE   sing N N 333 
MET CE  HE1  sing N N 334 
MET CE  HE2  sing N N 335 
MET CE  HE3  sing N N 336 
MET OXT HXT  sing N N 337 
PHE N   CA   sing N N 338 
PHE N   H    sing N N 339 
PHE N   H2   sing N N 340 
PHE CA  C    sing N N 341 
PHE CA  CB   sing N N 342 
PHE CA  HA   sing N N 343 
PHE C   O    doub N N 344 
PHE C   OXT  sing N N 345 
PHE CB  CG   sing N N 346 
PHE CB  HB2  sing N N 347 
PHE CB  HB3  sing N N 348 
PHE CG  CD1  doub Y N 349 
PHE CG  CD2  sing Y N 350 
PHE CD1 CE1  sing Y N 351 
PHE CD1 HD1  sing N N 352 
PHE CD2 CE2  doub Y N 353 
PHE CD2 HD2  sing N N 354 
PHE CE1 CZ   doub Y N 355 
PHE CE1 HE1  sing N N 356 
PHE CE2 CZ   sing Y N 357 
PHE CE2 HE2  sing N N 358 
PHE CZ  HZ   sing N N 359 
PHE OXT HXT  sing N N 360 
PRO N   CA   sing N N 361 
PRO N   CD   sing N N 362 
PRO N   H    sing N N 363 
PRO CA  C    sing N N 364 
PRO CA  CB   sing N N 365 
PRO CA  HA   sing N N 366 
PRO C   O    doub N N 367 
PRO C   OXT  sing N N 368 
PRO CB  CG   sing N N 369 
PRO CB  HB2  sing N N 370 
PRO CB  HB3  sing N N 371 
PRO CG  CD   sing N N 372 
PRO CG  HG2  sing N N 373 
PRO CG  HG3  sing N N 374 
PRO CD  HD2  sing N N 375 
PRO CD  HD3  sing N N 376 
PRO OXT HXT  sing N N 377 
SER N   CA   sing N N 378 
SER N   H    sing N N 379 
SER N   H2   sing N N 380 
SER CA  C    sing N N 381 
SER CA  CB   sing N N 382 
SER CA  HA   sing N N 383 
SER C   O    doub N N 384 
SER C   OXT  sing N N 385 
SER CB  OG   sing N N 386 
SER CB  HB2  sing N N 387 
SER CB  HB3  sing N N 388 
SER OG  HG   sing N N 389 
SER OXT HXT  sing N N 390 
THR N   CA   sing N N 391 
THR N   H    sing N N 392 
THR N   H2   sing N N 393 
THR CA  C    sing N N 394 
THR CA  CB   sing N N 395 
THR CA  HA   sing N N 396 
THR C   O    doub N N 397 
THR C   OXT  sing N N 398 
THR CB  OG1  sing N N 399 
THR CB  CG2  sing N N 400 
THR CB  HB   sing N N 401 
THR OG1 HG1  sing N N 402 
THR CG2 HG21 sing N N 403 
THR CG2 HG22 sing N N 404 
THR CG2 HG23 sing N N 405 
THR OXT HXT  sing N N 406 
TRP N   CA   sing N N 407 
TRP N   H    sing N N 408 
TRP N   H2   sing N N 409 
TRP CA  C    sing N N 410 
TRP CA  CB   sing N N 411 
TRP CA  HA   sing N N 412 
TRP C   O    doub N N 413 
TRP C   OXT  sing N N 414 
TRP CB  CG   sing N N 415 
TRP CB  HB2  sing N N 416 
TRP CB  HB3  sing N N 417 
TRP CG  CD1  doub Y N 418 
TRP CG  CD2  sing Y N 419 
TRP CD1 NE1  sing Y N 420 
TRP CD1 HD1  sing N N 421 
TRP CD2 CE2  doub Y N 422 
TRP CD2 CE3  sing Y N 423 
TRP NE1 CE2  sing Y N 424 
TRP NE1 HE1  sing N N 425 
TRP CE2 CZ2  sing Y N 426 
TRP CE3 CZ3  doub Y N 427 
TRP CE3 HE3  sing N N 428 
TRP CZ2 CH2  doub Y N 429 
TRP CZ2 HZ2  sing N N 430 
TRP CZ3 CH2  sing Y N 431 
TRP CZ3 HZ3  sing N N 432 
TRP CH2 HH2  sing N N 433 
TRP OXT HXT  sing N N 434 
TYR N   CA   sing N N 435 
TYR N   H    sing N N 436 
TYR N   H2   sing N N 437 
TYR CA  C    sing N N 438 
TYR CA  CB   sing N N 439 
TYR CA  HA   sing N N 440 
TYR C   O    doub N N 441 
TYR C   OXT  sing N N 442 
TYR CB  CG   sing N N 443 
TYR CB  HB2  sing N N 444 
TYR CB  HB3  sing N N 445 
TYR CG  CD1  doub Y N 446 
TYR CG  CD2  sing Y N 447 
TYR CD1 CE1  sing Y N 448 
TYR CD1 HD1  sing N N 449 
TYR CD2 CE2  doub Y N 450 
TYR CD2 HD2  sing N N 451 
TYR CE1 CZ   doub Y N 452 
TYR CE1 HE1  sing N N 453 
TYR CE2 CZ   sing Y N 454 
TYR CE2 HE2  sing N N 455 
TYR CZ  OH   sing N N 456 
TYR OH  HH   sing N N 457 
TYR OXT HXT  sing N N 458 
VAL N   CA   sing N N 459 
VAL N   H    sing N N 460 
VAL N   H2   sing N N 461 
VAL CA  C    sing N N 462 
VAL CA  CB   sing N N 463 
VAL CA  HA   sing N N 464 
VAL C   O    doub N N 465 
VAL C   OXT  sing N N 466 
VAL CB  CG1  sing N N 467 
VAL CB  CG2  sing N N 468 
VAL CB  HB   sing N N 469 
VAL CG1 HG11 sing N N 470 
VAL CG1 HG12 sing N N 471 
VAL CG1 HG13 sing N N 472 
VAL CG2 HG21 sing N N 473 
VAL CG2 HG22 sing N N 474 
VAL CG2 HG23 sing N N 475 
VAL OXT HXT  sing N N 476 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                      ZN  
3 BICINE                                                          BCN 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                          MES 
5 'DIMETHYL SULFOXIDE'                                            DMS 
6 '4-{[(5-butylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' E2I 
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          'PDB entry 3HLJ' 
# 
