data_4QJM
# 
_entry.id   4QJM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.381 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4QJM         pdb_00004qjm 10.2210/pdb4qjm/pdb 
RCSB  RCSB086137   ?            ?                   
WWPDB D_1000086137 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4QIY . unspecified 
PDB 4QIZ . unspecified 
PDB 4QJ0 . unspecified 
PDB 4QJO . unspecified 
PDB 4QJP . unspecified 
PDB 4QJW . unspecified 
PDB 4QJX . unspecified 
PDB 4QTL . unspecified 
# 
_pdbx_database_status.entry_id                        4QJM 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2014-06-04 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Functionalization of Fluorinated Benzenesulfonamides and Their Inhibitory Properties toward Carbonic Anhydrases' 
_citation.journal_abbrev            Chemmedchem 
_citation.journal_volume            10 
_citation.page_first                662 
_citation.page_last                 687 
_citation.year                      2015 
_citation.journal_id_ASTM           ? 
_citation.country                   DE 
_citation.journal_id_ISSN           1860-7179 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25758852 
_citation.pdbx_database_id_DOI      10.1002/cmdc.201402490 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dudutiene, V.'     1  ? 
primary 'Zubriene, A.'      2  ? 
primary 'Smirnov, A.'       3  ? 
primary 'Timm, D.D.'        4  ? 
primary 'Smirnoviene, J.'   5  ? 
primary 'Kazokaite, J.'     6  ? 
primary 'Michailoviene, V.' 7  ? 
primary 'Zaksauskas, A.'    8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Matulis, D.'       11 ? 
# 
_cell.entry_id           4QJM 
_cell.length_a           42.187 
_cell.length_b           41.090 
_cell.length_c           71.981 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.120 
_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                         4QJM 
_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 '3-(benzylamino)-2,5,6-trifluoro-4-[(2-phenylethyl)sulfonyl]benzenesulfonamide' 484.512   1   ?       ? ? ? 
4 non-polymer syn BICINE                                                                          163.172   1   ?       ? ? ? 
5 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                          195.237   1   ?       ? ? ? 
6 non-polymer syn 'DIMETHYL SULFOXIDE'                                                            78.133    1   ?       ? ? ? 
7 water       nat water                                                                           18.015    286 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4QJM 
_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  
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 
V1F non-polymer         . '3-(benzylamino)-2,5,6-trifluoro-4-[(2-phenylethyl)sulfonyl]benzenesulfonamide' ? 'C21 H19 F3 N2 O4 S2' 
484.512 
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          4QJM 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   38.6 
_exptl_crystal.density_Matthews      2.02 
_exptl_crystal.pdbx_mosaicity        0.56 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
'0.1M sodium BICINE pH 9, 0.2M ammonium sulfate, 2M sodium malonate pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS IV++' 
_diffrn_detector.pdbx_collection_date   2012-08-04 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'VARIMAX-HF MIRROR' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
# 
_reflns.entry_id                     4QJM 
_reflns.d_resolution_high            1.750 
_reflns.d_resolution_low             20.618 
_reflns.number_all                   ? 
_reflns.number_obs                   23685 
_reflns.pdbx_netI_over_sigmaI        12.600 
_reflns.pdbx_Rsym_value              0.057 
_reflns.pdbx_redundancy              3.600 
_reflns.percent_possible_obs         97.400 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        16.693 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.75 1.84  ? 12178 ? ? 0.177 3.7  0.177 ? 3.60 ? 5.10  ? 3390 ? ? 0.258 ? 95.40 0.26 0.14 1  1 
1.84 1.96  ? 11399 ? ? 0.122 5.7  0.122 ? 3.60 ? 7.00  ? 3184 ? ? 0.167 ? 96.10 0.17 0.09 2  1 
1.96 2.09  ? 10798 ? ? 0.088 7.1  0.088 ? 3.60 ? 8.90  ? 3022 ? ? 0.115 ? 96.60 0.12 0.06 3  1 
2.09 2.26  ? 10121 ? ? 0.066 8.8  0.066 ? 3.60 ? 11.40 ? 2831 ? ? 0.089 ? 97.30 0.09 0.05 4  1 
2.26 2.47  ? 9478  ? ? 0.059 10.3 0.059 ? 3.60 ? 13.60 ? 2638 ? ? 0.080 ? 98.00 0.08 0.04 5  1 
2.47 2.77  ? 8761  ? ? 0.054 9.4  0.054 ? 3.60 ? 15.50 ? 2419 ? ? 0.074 ? 98.60 0.07 0.04 6  1 
2.77 3.20  ? 7697  ? ? 0.047 11.4 0.047 ? 3.60 ? 17.80 ? 2122 ? ? 0.067 ? 98.90 0.07 0.04 7  1 
3.20 3.91  ? 6622  ? ? 0.046 8.9  0.046 ? 3.60 ? 21.50 ? 1839 ? ? 0.067 ? 99.50 0.07 0.04 8  1 
3.91 5.53  ? 5115  ? ? 0.045 10.2 0.045 ? 3.60 ? 21.40 ? 1430 ? ? 0.062 ? 99.60 0.06 0.03 9  1 
5.53 20.62 ? 2745  ? ? 0.057 5.1  0.057 ? 3.40 ? 22.30 ? 810  ? ? 0.085 ? 98.40 0.09 0.05 10 1 
# 
_refine.entry_id                                 4QJM 
_refine.ls_d_res_high                            1.750 
_refine.ls_d_res_low                             20.550 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    96.980 
_refine.ls_number_reflns_obs                     23673 
_refine.ls_number_reflns_all                     23673 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES' 
_refine.ls_R_factor_all                          0.166 
_refine.ls_R_factor_obs                          0.166 
_refine.ls_R_factor_R_work                       0.161 
_refine.ls_wR_factor_R_work                      0.175 
_refine.ls_R_factor_R_free                       0.212 
_refine.ls_wR_factor_R_free                      0.234 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  2362 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.018 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.170 
_refine.aniso_B[2][2]                            0.060 
_refine.aniso_B[3][3]                            -0.130 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.210 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.938 
_refine.overall_SU_R_Cruickshank_DPI             0.136 
_refine.overall_SU_R_free                        0.132 
_refine.pdbx_overall_ESU_R                       0.136 
_refine.pdbx_overall_ESU_R_Free                  0.132 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.882 
_refine.B_iso_max                                60.14 
_refine.B_iso_min                                5.92 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      3HLJ 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.number_atoms_solvent             286 
_refine_hist.number_atoms_total               2391 
_refine_hist.d_res_high                       1.750 
_refine_hist.d_res_low                        20.550 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       2233 0.019  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3039 2.127  1.973  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 271  6.825  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 102  37.563 24.902 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 361  14.182 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 7    13.307 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         312  0.149  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1740 0.012  0.021  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.750 
_refine_ls_shell.d_res_low                        1.795 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               94.810 
_refine_ls_shell.number_reflns_R_work             1545 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.293 
_refine_ls_shell.R_factor_R_free                  0.316 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             153 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1698 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  4QJM 
_struct.title                     'Crystal structure of human carbonic anhydrase isozyme II with inhibitor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4QJM 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, LYASE-LYASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 12  ? 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  301 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V1F . N10 ? ? A ZN  301 A V1F 302 1_555 ? ? ? ? ? ? ? 1.877 ? ? 
# 
_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 -4.34 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 6.93  
# 
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 LEU A 211 ? O LEU A 212 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 VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A V1F 302 ? 18 'BINDING SITE FOR RESIDUE V1F A 302' 
AC3 Software A BCN 303 ? 8  'BINDING SITE FOR RESIDUE BCN A 303' 
AC4 Software A MES 304 ? 5  'BINDING SITE FOR RESIDUE MES A 304' 
AC5 Software A DMS 305 ? 5  'BINDING SITE FOR RESIDUE DMS A 305' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  V1F C .   ? V1F A 302 . ? 1_555 ? 
5  AC2 18 ASN A 62  ? ASN A 62  . ? 1_555 ? 
6  AC2 18 HIS A 64  ? HIS A 64  . ? 1_555 ? 
7  AC2 18 ASN A 67  ? ASN A 67  . ? 1_555 ? 
8  AC2 18 ILE A 91  ? ILE A 91  . ? 1_555 ? 
9  AC2 18 GLN A 92  ? GLN A 92  . ? 1_555 ? 
10 AC2 18 HIS A 94  ? HIS A 94  . ? 1_555 ? 
11 AC2 18 HIS A 96  ? HIS A 96  . ? 1_555 ? 
12 AC2 18 HIS A 119 ? HIS A 119 . ? 1_555 ? 
13 AC2 18 VAL A 121 ? VAL A 121 . ? 1_555 ? 
14 AC2 18 PHE A 130 ? PHE A 131 . ? 1_555 ? 
15 AC2 18 LEU A 197 ? LEU A 198 . ? 1_555 ? 
16 AC2 18 THR A 198 ? THR A 199 . ? 1_555 ? 
17 AC2 18 THR A 199 ? THR A 200 . ? 1_555 ? 
18 AC2 18 PRO A 200 ? PRO A 201 . ? 1_555 ? 
19 AC2 18 PRO A 201 ? PRO A 202 . ? 1_555 ? 
20 AC2 18 TRP A 208 ? TRP A 209 . ? 1_555 ? 
21 AC2 18 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
22 AC2 18 HOH G .   ? HOH A 597 . ? 1_555 ? 
23 AC3 8  LYS A 148 ? LYS A 149 . ? 1_555 ? 
24 AC3 8  LYS A 212 ? LYS A 213 . ? 1_555 ? 
25 AC3 8  GLU A 213 ? GLU A 214 . ? 1_555 ? 
26 AC3 8  PRO A 214 ? PRO A 215 . ? 1_555 ? 
27 AC3 8  HOH G .   ? HOH A 430 . ? 1_555 ? 
28 AC3 8  HOH G .   ? HOH A 440 . ? 1_555 ? 
29 AC3 8  HOH G .   ? HOH A 613 . ? 1_555 ? 
30 AC3 8  HOH G .   ? HOH A 638 . ? 1_555 ? 
31 AC4 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
32 AC4 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
33 AC4 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
34 AC4 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
35 AC4 5  HOH G .   ? HOH A 604 . ? 1_555 ? 
36 AC5 5  TYR A 7   ? TYR A 7   . ? 1_555 ? 
37 AC5 5  ASP A 242 ? ASP A 243 . ? 1_555 ? 
38 AC5 5  TRP A 244 ? TRP A 245 . ? 1_555 ? 
39 AC5 5  HOH G .   ? HOH A 575 . ? 1_555 ? 
40 AC5 5  HOH G .   ? HOH A 643 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4QJM 
_atom_sites.fract_transf_matrix[1][1]   0.023704 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005964 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024337 
_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]   0.014326 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 30.076  3.049   8.170   1.00 28.14 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 30.915  1.953   8.460   1.00 28.25 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.362  0.908   9.410   1.00 25.54 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.610  -0.280  9.218   1.00 22.64 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 32.226  2.421   9.030   1.00 38.10 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 33.404  1.506   8.892   1.00 43.56 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 33.970  0.986   9.949   1.00 46.31 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 34.212  1.162   7.807   1.00 48.77 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 35.027  0.252   9.584   1.00 50.18 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 35.178  0.378   8.270   1.00 50.32 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.611  1.315   10.428  1.00 20.62 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 28.987  0.334   11.317  1.00 15.86 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 27.981  -0.462  10.551  1.00 14.69 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.468  -0.041  9.491   1.00 15.05 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.332  0.989   12.513  1.00 15.69 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 27.144  1.834   12.130  1.00 16.72 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 27.108  3.181   11.776  1.00 16.23 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.758  1.376   12.073  1.00 15.06 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.822  3.570   11.532  1.00 16.76 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.966  2.521   11.704  1.00 15.07 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 25.133  0.156   12.336  1.00 14.94 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.592  2.447   11.558  1.00 15.60 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.752  0.076   12.168  1.00 13.68 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 23.005  1.196   11.768  1.00 15.85 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.730  -1.647  11.043  1.00 13.45 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.678  -2.480  10.444  1.00 14.13 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.307  -3.607  11.384  1.00 14.01 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.303  -3.455  12.600  1.00 14.03 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 25.994  -4.752  10.791  1.00 15.30 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.626  -5.929  11.561  1.00 15.89 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.561  -7.189  11.456  1.00 22.15 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 26.344  -8.236  12.163  1.00 23.05 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 24.154  -6.202  11.230  1.00 14.27 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.231  -5.152  11.826  1.00 11.68 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.806  -5.250  13.163  1.00 11.70 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.771  -4.081  11.039  1.00 11.39 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.975  -4.234  13.713  1.00 11.54 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.922  -3.089  11.557  1.00 12.56 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.511  -3.202  12.892  1.00 11.47 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.624  -2.217  13.315  1.00 12.20 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.635  -7.085  10.649  1.00 24.93 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.647  -8.203  10.599  1.00 22.71 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.670  -8.467  11.707  1.00 26.16 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.722  -7.790  12.799  1.00 28.02 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.572  -9.436  11.421  1.00 30.91 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.569  -9.925  12.406  1.00 29.21 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.509  -8.830  12.760  1.00 29.21 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.954  -8.732  13.939  1.00 28.45 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 32.380  -11.103 11.874  1.00 33.60 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 32.645  -12.208 12.878  1.00 47.42 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 34.052  -12.113 13.476  1.00 51.55 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 34.308  -13.226 14.502  1.00 55.09 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 33.527  -13.162 15.788  1.00 53.87 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 32.760  -8.000  11.735  1.00 25.78 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 33.751  -6.962  11.787  1.00 24.32 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 33.214  -5.625  12.036  1.00 19.72 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 33.962  -4.790  12.450  1.00 20.51 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 34.615  -7.001  10.515  1.00 26.16 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 35.295  -8.334  10.334  1.00 26.20 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 36.296  -8.740  11.146  1.00 27.28 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 35.035  -9.380  9.461   1.00 29.67 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 36.650  -9.985  10.805  1.00 28.79 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 35.878  -10.374 9.771   1.00 26.05 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 31.902  -5.396  11.841  1.00 18.76 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 31.356  -4.047  12.162  1.00 17.39 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 30.023  -4.041  12.944  1.00 17.19 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 29.347  -2.984  13.003  1.00 15.77 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 31.131  -3.252  10.874  1.00 15.88 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 30.090  -3.887  9.962   1.00 18.67 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 29.521  -4.925  10.265  1.00 19.16 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 29.877  -3.297  8.820   1.00 17.25 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 29.687  -5.198  13.518  1.00 15.86 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 28.370  -5.369  14.177  1.00 14.64 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 28.320  -4.736  15.547  1.00 14.32 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 29.231  -4.073  16.008  1.00 15.34 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 27.233  -4.999  16.276  1.00 13.57 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 26.940  -4.417  17.586  1.00 14.61 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 28.092  -4.431  18.587  1.00 13.60 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 28.252  -3.468  19.352  1.00 14.28 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 25.772  -5.314  18.064  1.00 13.60 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 25.016  -5.546  16.811  1.00 14.77 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 26.150  -5.907  15.845  1.00 14.62 ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 28.902  -5.504  18.602  1.00 14.95 ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 30.033  -5.613  19.532  1.00 16.02 ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 31.197  -4.623  19.263  1.00 14.34 ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 32.096  -4.429  20.087  1.00 14.19 ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 30.483  -7.106  19.525  1.00 22.18 ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 31.178  -7.545  18.214  1.00 23.54 ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 30.215  -8.090  17.174  1.00 27.96 ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 29.010  -7.766  17.235  1.00 20.90 ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 30.669  -8.844  16.288  1.00 20.64 ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 31.177  -4.009  18.091  1.00 13.69 ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 32.191  -3.044  17.640  1.00 13.43 ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 31.751  -1.619  17.768  1.00 14.92 ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 32.575  -0.691  17.712  1.00 11.31 ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 32.476  -3.266  16.164  1.00 16.38 ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 33.253  -4.527  15.886  1.00 18.55 ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 34.603  -4.607  16.036  1.00 19.82 ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 32.827  -5.779  15.491  1.00 18.82 ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 35.005  -5.869  15.755  1.00 19.91 ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 33.925  -6.593  15.463  1.00 19.73 ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 30.448  -1.402  17.951  1.00 12.00 ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 29.922  -0.023  17.878  1.00 11.84 ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 30.484  0.931   18.884  1.00 11.26 ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 30.548  2.140   18.611  1.00 11.76 ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 28.398  -0.058  18.053  1.00 10.24 ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 27.719  -0.727  16.905  1.00 10.53 ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 28.251  -1.163  15.683  1.00 10.37 ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 26.275  -1.058  16.859  1.00 9.55  ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 27.267  -1.749  14.904  1.00 10.49 ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 26.040  -1.679  15.572  1.00 10.51 ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 25.220  -0.869  17.763  1.00 9.73  ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 24.796  -2.110  15.192  1.00 11.11 ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 23.964  -1.272  17.383  1.00 9.44  ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 23.738  -1.896  16.144  1.00 10.72 ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 30.897  0.418   20.035  1.00 11.42 ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 31.346  1.285   21.109  1.00 12.74 ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 32.590  2.093   20.707  1.00 13.19 ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 32.834  3.120   21.302  1.00 13.07 ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 31.627  0.543   22.425  1.00 13.49 ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 32.871  -0.374  22.348  1.00 15.19 ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 34.068  -0.021  22.857  1.00 17.55 ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 33.065  -1.547  21.679  1.00 16.36 ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 34.979  -0.966  22.563  1.00 16.84 ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 34.372  -1.904  21.851  1.00 16.43 ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 18  ? 33.339  1.598   19.720  1.00 14.27 ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 18  ? 34.639  2.247   19.379  1.00 15.76 ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 18  ? 34.330  3.600   18.747  1.00 16.23 ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 18  ? 34.932  4.612   19.115  1.00 19.15 ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 18  ? 35.437  1.348   18.459  1.00 16.48 ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 18  ? 36.157  0.218   19.199  1.00 16.81 ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 18  ? 36.797  -0.758  18.214  1.00 15.47 ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 18  ? 35.839  -1.758  17.624  1.00 15.24 ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 18  ? 36.441  -2.516  16.469  1.00 14.55 ? 18  LYS A NZ  1 
ATOM   135  N  N   A ASP A 1 19  ? 33.340  3.632   17.853  0.50 16.80 ? 19  ASP A N   1 
ATOM   136  N  N   B ASP A 1 19  ? 33.349  3.648   17.847  0.50 16.31 ? 19  ASP A N   1 
ATOM   137  C  CA  A ASP A 1 19  ? 32.870  4.926   17.305  0.50 17.57 ? 19  ASP A CA  1 
ATOM   138  C  CA  B ASP A 1 19  ? 32.888  4.966   17.348  0.50 16.68 ? 19  ASP A CA  1 
ATOM   139  C  C   A ASP A 1 19  ? 31.784  5.646   18.090  0.50 17.16 ? 19  ASP A C   1 
ATOM   140  C  C   B ASP A 1 19  ? 31.899  5.690   18.255  0.50 16.63 ? 19  ASP A C   1 
ATOM   141  O  O   A ASP A 1 19  ? 31.552  6.851   17.845  0.50 14.94 ? 19  ASP A O   1 
ATOM   142  O  O   B ASP A 1 19  ? 31.842  6.930   18.272  0.50 14.64 ? 19  ASP A O   1 
ATOM   143  C  CB  A ASP A 1 19  ? 32.428  4.779   15.857  0.50 19.17 ? 19  ASP A CB  1 
ATOM   144  C  CB  B ASP A 1 19  ? 32.323  4.854   15.938  0.50 17.38 ? 19  ASP A CB  1 
ATOM   145  C  CG  A ASP A 1 19  ? 33.589  4.737   14.923  0.50 23.54 ? 19  ASP A CG  1 
ATOM   146  C  CG  B ASP A 1 19  ? 33.389  4.913   14.911  0.50 20.32 ? 19  ASP A CG  1 
ATOM   147  O  OD1 A ASP A 1 19  ? 34.267  5.792   14.775  0.50 24.96 ? 19  ASP A OD1 1 
ATOM   148  O  OD1 B ASP A 1 19  ? 34.571  4.904   15.336  0.50 20.75 ? 19  ASP A OD1 1 
ATOM   149  O  OD2 A ASP A 1 19  ? 33.824  3.643   14.368  0.50 23.92 ? 19  ASP A OD2 1 
ATOM   150  O  OD2 B ASP A 1 19  ? 33.064  4.975   13.706  0.50 19.48 ? 19  ASP A OD2 1 
ATOM   151  N  N   . PHE A 1 20  ? 31.102  4.909   18.989  1.00 15.12 ? 20  PHE A N   1 
ATOM   152  C  CA  . PHE A 1 20  ? 29.995  5.445   19.787  1.00 14.81 ? 20  PHE A CA  1 
ATOM   153  C  C   . PHE A 1 20  ? 30.096  4.957   21.184  1.00 14.77 ? 20  PHE A C   1 
ATOM   154  O  O   . PHE A 1 20  ? 29.457  3.959   21.507  1.00 13.82 ? 20  PHE A O   1 
ATOM   155  C  CB  . PHE A 1 20  ? 28.653  5.035   19.157  1.00 13.94 ? 20  PHE A CB  1 
ATOM   156  C  CG  . PHE A 1 20  ? 28.544  5.468   17.745  1.00 15.10 ? 20  PHE A CG  1 
ATOM   157  C  CD1 . PHE A 1 20  ? 28.203  6.785   17.460  1.00 16.61 ? 20  PHE A CD1 1 
ATOM   158  C  CD2 . PHE A 1 20  ? 28.799  4.574   16.698  1.00 15.87 ? 20  PHE A CD2 1 
ATOM   159  C  CE1 . PHE A 1 20  ? 28.135  7.190   16.142  1.00 17.05 ? 20  PHE A CE1 1 
ATOM   160  C  CE2 . PHE A 1 20  ? 28.762  4.996   15.365  1.00 16.53 ? 20  PHE A CE2 1 
ATOM   161  C  CZ  . PHE A 1 20  ? 28.429  6.307   15.106  1.00 14.91 ? 20  PHE A CZ  1 
ATOM   162  N  N   . PRO A 1 21  ? 30.866  5.665   22.050  1.00 14.78 ? 21  PRO A N   1 
ATOM   163  C  CA  . PRO A 1 21  ? 31.172  5.138   23.367  1.00 14.36 ? 21  PRO A CA  1 
ATOM   164  C  C   . PRO A 1 21  ? 29.920  4.980   24.262  1.00 13.32 ? 21  PRO A C   1 
ATOM   165  O  O   . PRO A 1 21  ? 29.945  4.241   25.235  1.00 12.25 ? 21  PRO A O   1 
ATOM   166  C  CB  . PRO A 1 21  ? 32.153  6.170   23.984  1.00 17.76 ? 21  PRO A CB  1 
ATOM   167  C  CG  . PRO A 1 21  ? 32.595  7.070   22.868  1.00 18.63 ? 21  PRO A CG  1 
ATOM   168  C  CD  . PRO A 1 21  ? 31.794  6.762   21.630  1.00 16.42 ? 21  PRO A CD  1 
ATOM   169  N  N   . ILE A 1 22  ? 28.857  5.740   23.919  1.00 12.20 ? 22  ILE A N   1 
ATOM   170  C  CA  . ILE A 1 22  ? 27.566  5.674   24.599  1.00 12.10 ? 22  ILE A CA  1 
ATOM   171  C  C   . ILE A 1 22  ? 26.969  4.270   24.455  1.00 11.25 ? 22  ILE A C   1 
ATOM   172  O  O   . ILE A 1 22  ? 26.054  3.929   25.209  1.00 11.37 ? 22  ILE A O   1 
ATOM   173  C  CB  . ILE A 1 22  ? 26.582  6.794   24.112  1.00 10.93 ? 22  ILE A CB  1 
ATOM   174  C  CG1 . ILE A 1 22  ? 25.570  7.155   25.194  1.00 11.63 ? 22  ILE A CG1 1 
ATOM   175  C  CG2 . ILE A 1 22  ? 26.005  6.404   22.727  1.00 12.42 ? 22  ILE A CG2 1 
ATOM   176  C  CD1 . ILE A 1 22  ? 24.477  8.132   24.745  1.00 12.86 ? 22  ILE A CD1 1 
ATOM   177  N  N   . ALA A 1 23  ? 27.510  3.445   23.541  1.00 11.71 ? 23  ALA A N   1 
ATOM   178  C  CA  . ALA A 1 23  ? 27.072  2.026   23.493  1.00 12.73 ? 23  ALA A CA  1 
ATOM   179  C  C   . ALA A 1 23  ? 27.142  1.322   24.837  1.00 13.63 ? 23  ALA A C   1 
ATOM   180  O  O   . ALA A 1 23  ? 26.419  0.332   25.067  1.00 13.19 ? 23  ALA A O   1 
ATOM   181  C  CB  . ALA A 1 23  ? 27.838  1.229   22.458  1.00 13.17 ? 23  ALA A CB  1 
ATOM   182  N  N   . LYS A 1 24  ? 28.030  1.787   25.720  1.00 13.08 ? 24  LYS A N   1 
ATOM   183  C  CA  . LYS A 1 24  ? 28.208  1.081   27.009  1.00 14.17 ? 24  LYS A CA  1 
ATOM   184  C  C   . LYS A 1 24  ? 27.604  1.986   28.081  1.00 15.72 ? 24  LYS A C   1 
ATOM   185  O  O   . LYS A 1 24  ? 27.996  1.903   29.288  1.00 16.10 ? 24  LYS A O   1 
ATOM   186  C  CB  . LYS A 1 24  ? 29.719  0.894   27.321  1.00 15.63 ? 24  LYS A CB  1 
ATOM   187  C  CG  . LYS A 1 24  ? 30.426  -0.107  26.427  1.00 19.76 ? 24  LYS A CG  1 
ATOM   188  C  CD  . LYS A 1 24  ? 31.891  -0.281  26.826  1.00 22.41 ? 24  LYS A CD  1 
ATOM   189  C  CE  . LYS A 1 24  ? 32.599  -1.156  25.788  1.00 23.24 ? 24  LYS A CE  1 
ATOM   190  N  NZ  . LYS A 1 24  ? 32.224  -2.561  25.966  1.00 23.10 ? 24  LYS A NZ  1 
ATOM   191  N  N   . GLY A 1 25  ? 26.618  2.797   27.697  1.00 14.22 ? 25  GLY A N   1 
ATOM   192  C  CA  . GLY A 1 25  ? 26.121  3.776   28.642  1.00 14.35 ? 25  GLY A CA  1 
ATOM   193  C  C   . GLY A 1 25  ? 25.102  3.244   29.622  1.00 13.89 ? 25  GLY A C   1 
ATOM   194  O  O   . GLY A 1 25  ? 24.880  2.012   29.775  1.00 14.93 ? 25  GLY A O   1 
ATOM   195  N  N   . GLU A 1 26  ? 24.455  4.190   30.280  1.00 13.24 ? 26  GLU A N   1 
ATOM   196  C  CA  . GLU A 1 26  ? 23.606  3.831   31.380  1.00 14.72 ? 26  GLU A CA  1 
ATOM   197  C  C   . GLU A 1 26  ? 22.163  3.542   31.017  1.00 12.84 ? 26  GLU A C   1 
ATOM   198  O  O   . GLU A 1 26  ? 21.382  3.042   31.860  1.00 12.16 ? 26  GLU A O   1 
ATOM   199  C  CB  . GLU A 1 26  ? 23.676  4.903   32.493  1.00 20.49 ? 26  GLU A CB  1 
ATOM   200  C  CG  . GLU A 1 26  ? 25.051  5.069   33.076  1.00 22.34 ? 26  GLU A CG  1 
ATOM   201  C  CD  . GLU A 1 26  ? 25.557  3.781   33.735  1.00 27.56 ? 26  GLU A CD  1 
ATOM   202  O  OE1 . GLU A 1 26  ? 24.804  3.105   34.520  1.00 27.78 ? 26  GLU A OE1 1 
ATOM   203  O  OE2 . GLU A 1 26  ? 26.722  3.441   33.451  1.00 29.71 ? 26  GLU A OE2 1 
ATOM   204  N  N   . ARG A 1 27  ? 21.752  3.840   29.784  1.00 11.55 ? 27  ARG A N   1 
ATOM   205  C  CA  . ARG A 1 27  ? 20.343  3.568   29.493  1.00 10.37 ? 27  ARG A CA  1 
ATOM   206  C  C   . ARG A 1 27  ? 20.201  3.113   28.013  1.00 9.70  ? 27  ARG A C   1 
ATOM   207  O  O   . ARG A 1 27  ? 19.479  3.740   27.184  1.00 9.34  ? 27  ARG A O   1 
ATOM   208  C  CB  . ARG A 1 27  ? 19.396  4.777   29.781  1.00 12.29 ? 27  ARG A CB  1 
ATOM   209  C  CG  . ARG A 1 27  ? 19.764  6.060   29.052  1.00 14.56 ? 27  ARG A CG  1 
ATOM   210  C  CD  . ARG A 1 27  ? 18.807  7.220   29.352  1.00 18.11 ? 27  ARG A CD  1 
ATOM   211  N  NE  . ARG A 1 27  ? 17.606  7.191   28.491  1.00 14.81 ? 27  ARG A NE  1 
ATOM   212  C  CZ  . ARG A 1 27  ? 16.671  8.138   28.462  1.00 14.84 ? 27  ARG A CZ  1 
ATOM   213  N  NH1 . ARG A 1 27  ? 16.768  9.228   29.253  1.00 15.84 ? 27  ARG A NH1 1 
ATOM   214  N  NH2 . ARG A 1 27  ? 15.677  8.028   27.618  1.00 15.03 ? 27  ARG A NH2 1 
ATOM   215  N  N   . GLN A 1 28  ? 20.868  2.003   27.719  1.00 8.66  ? 28  GLN A N   1 
ATOM   216  C  CA  . GLN A 1 28  ? 20.917  1.493   26.322  1.00 8.42  ? 28  GLN A CA  1 
ATOM   217  C  C   . GLN A 1 28  ? 19.791  0.535   26.043  1.00 8.25  ? 28  GLN A C   1 
ATOM   218  O  O   . GLN A 1 28  ? 19.283  -0.143  26.960  1.00 8.52  ? 28  GLN A O   1 
ATOM   219  C  CB  . GLN A 1 28  ? 22.257  0.756   26.083  1.00 8.52  ? 28  GLN A CB  1 
ATOM   220  C  CG  . GLN A 1 28  ? 23.439  1.780   25.985  1.00 8.67  ? 28  GLN A CG  1 
ATOM   221  C  CD  . GLN A 1 28  ? 23.331  2.634   24.707  1.00 8.57  ? 28  GLN A CD  1 
ATOM   222  O  OE1 . GLN A 1 28  ? 23.577  2.129   23.627  1.00 8.84  ? 28  GLN A OE1 1 
ATOM   223  N  NE2 . GLN A 1 28  ? 23.000  3.942   24.834  1.00 8.10  ? 28  GLN A NE2 1 
ATOM   224  N  N   . SER A 1 29  ? 19.443  0.442   24.750  1.00 7.38  ? 29  SER A N   1 
ATOM   225  C  CA  . SER A 1 29  ? 18.361  -0.407  24.299  1.00 7.33  ? 29  SER A CA  1 
ATOM   226  C  C   . SER A 1 29  ? 18.903  -1.260  23.180  1.00 6.88  ? 29  SER A C   1 
ATOM   227  O  O   . SER A 1 29  ? 19.863  -0.902  22.538  1.00 7.31  ? 29  SER A O   1 
ATOM   228  C  CB  . SER A 1 29  ? 17.241  0.419   23.723  1.00 6.21  ? 29  SER A CB  1 
ATOM   229  O  OG  . SER A 1 29  ? 16.615  1.116   24.816  1.00 6.62  ? 29  SER A OG  1 
ATOM   230  N  N   . PRO A 1 30  ? 18.246  -2.374  22.924  1.00 6.96  ? 30  PRO A N   1 
ATOM   231  C  CA  . PRO A 1 30  ? 17.115  -2.953  23.618  1.00 7.02  ? 30  PRO A CA  1 
ATOM   232  C  C   . PRO A 1 30  ? 17.489  -3.621  24.922  1.00 6.97  ? 30  PRO A C   1 
ATOM   233  O  O   . PRO A 1 30  ? 18.694  -3.633  25.295  1.00 7.64  ? 30  PRO A O   1 
ATOM   234  C  CB  . PRO A 1 30  ? 16.618  -3.978  22.606  1.00 6.92  ? 30  PRO A CB  1 
ATOM   235  C  CG  . PRO A 1 30  ? 17.936  -4.543  22.079  1.00 6.69  ? 30  PRO A CG  1 
ATOM   236  C  CD  . PRO A 1 30  ? 18.684  -3.244  21.825  1.00 6.96  ? 30  PRO A CD  1 
ATOM   237  N  N   . VAL A 1 31  ? 16.472  -4.168  25.584  1.00 8.11  ? 31  VAL A N   1 
ATOM   238  C  CA  . VAL A 1 31  ? 16.646  -4.910  26.839  1.00 7.85  ? 31  VAL A CA  1 
ATOM   239  C  C   . VAL A 1 31  ? 15.773  -6.137  26.822  1.00 8.14  ? 31  VAL A C   1 
ATOM   240  O  O   . VAL A 1 31  ? 14.758  -6.240  26.083  1.00 8.14  ? 31  VAL A O   1 
ATOM   241  C  CB  . VAL A 1 31  ? 16.335  -4.098  28.121  1.00 8.13  ? 31  VAL A CB  1 
ATOM   242  C  CG1 . VAL A 1 31  ? 17.314  -2.913  28.291  1.00 7.14  ? 31  VAL A CG1 1 
ATOM   243  C  CG2 . VAL A 1 31  ? 14.842  -3.663  28.217  1.00 7.55  ? 31  VAL A CG2 1 
ATOM   244  N  N   . ASP A 1 32  ? 16.143  -7.081  27.672  1.00 8.36  ? 32  ASP A N   1 
ATOM   245  C  CA  . ASP A 1 32  ? 15.236  -8.200  27.967  1.00 8.72  ? 32  ASP A CA  1 
ATOM   246  C  C   . ASP A 1 32  ? 14.181  -7.725  28.917  1.00 9.14  ? 32  ASP A C   1 
ATOM   247  O  O   . ASP A 1 32  ? 14.497  -7.101  29.960  1.00 9.17  ? 32  ASP A O   1 
ATOM   248  C  CB  . ASP A 1 32  ? 15.977  -9.384  28.575  1.00 10.55 ? 32  ASP A CB  1 
ATOM   249  C  CG  . ASP A 1 32  ? 15.010  -10.597 28.866  1.00 11.10 ? 32  ASP A CG  1 
ATOM   250  O  OD1 . ASP A 1 32  ? 14.327  -11.022 27.935  1.00 10.81 ? 32  ASP A OD1 1 
ATOM   251  O  OD2 . ASP A 1 32  ? 14.982  -11.095 30.060  1.00 11.36 ? 32  ASP A OD2 1 
ATOM   252  N  N   . ILE A 1 33  ? 12.929  -8.010  28.610  1.00 9.63  ? 33  ILE A N   1 
ATOM   253  C  CA  . ILE A 1 33  ? 11.851  -7.654  29.507  1.00 10.54 ? 33  ILE A CA  1 
ATOM   254  C  C   . ILE A 1 33  ? 11.526  -8.866  30.347  1.00 11.81 ? 33  ILE A C   1 
ATOM   255  O  O   . ILE A 1 33  ? 10.970  -9.886  29.835  1.00 11.87 ? 33  ILE A O   1 
ATOM   256  C  CB  . ILE A 1 33  ? 10.575  -7.226  28.762  1.00 9.68  ? 33  ILE A CB  1 
ATOM   257  C  CG1 . ILE A 1 33  ? 10.823  -5.881  28.028  1.00 8.72  ? 33  ILE A CG1 1 
ATOM   258  C  CG2 . ILE A 1 33  ? 9.428   -6.975  29.759  1.00 9.80  ? 33  ILE A CG2 1 
ATOM   259  C  CD1 . ILE A 1 33  ? 9.867   -5.565  26.833  1.00 10.29 ? 33  ILE A CD1 1 
ATOM   260  N  N   A ASP A 1 34  ? 11.907  -8.768  31.615  0.50 12.14 ? 34  ASP A N   1 
ATOM   261  N  N   B ASP A 1 34  ? 11.923  -8.789  31.625  0.50 12.14 ? 34  ASP A N   1 
ATOM   262  C  CA  A ASP A 1 34  ? 11.579  -9.820  32.580  0.50 13.04 ? 34  ASP A CA  1 
ATOM   263  C  CA  B ASP A 1 34  ? 11.612  -9.833  32.656  0.50 12.98 ? 34  ASP A CA  1 
ATOM   264  C  C   A ASP A 1 34  ? 10.167  -9.552  33.122  0.50 14.28 ? 34  ASP A C   1 
ATOM   265  C  C   B ASP A 1 34  ? 10.173  -9.568  33.157  0.50 14.22 ? 34  ASP A C   1 
ATOM   266  O  O   A ASP A 1 34  ? 9.937   -8.604  33.889  0.50 15.01 ? 34  ASP A O   1 
ATOM   267  O  O   B ASP A 1 34  ? 9.925   -8.624  33.924  0.50 14.97 ? 34  ASP A O   1 
ATOM   268  C  CB  A ASP A 1 34  ? 12.632  -9.878  33.694  0.50 14.03 ? 34  ASP A CB  1 
ATOM   269  C  CB  B ASP A 1 34  ? 12.686  -9.805  33.799  0.50 13.87 ? 34  ASP A CB  1 
ATOM   270  C  CG  A ASP A 1 34  ? 12.438  -11.090 34.574  0.50 15.19 ? 34  ASP A CG  1 
ATOM   271  C  CG  B ASP A 1 34  ? 12.440  -10.880 34.902  0.50 15.16 ? 34  ASP A CG  1 
ATOM   272  O  OD1 A ASP A 1 34  ? 11.852  -10.934 35.663  0.50 15.89 ? 34  ASP A OD1 1 
ATOM   273  O  OD1 B ASP A 1 34  ? 11.270  -11.323 35.061  0.50 15.37 ? 34  ASP A OD1 1 
ATOM   274  O  OD2 A ASP A 1 34  ? 12.821  -12.187 34.125  0.50 14.38 ? 34  ASP A OD2 1 
ATOM   275  O  OD2 B ASP A 1 34  ? 13.428  -11.281 35.601  0.50 15.08 ? 34  ASP A OD2 1 
ATOM   276  N  N   . THR A 1 35  ? 9.223   -10.366 32.676  1.00 13.76 ? 35  THR A N   1 
ATOM   277  C  CA  . THR A 1 35  ? 7.798   -10.106 32.887  1.00 14.61 ? 35  THR A CA  1 
ATOM   278  C  C   . THR A 1 35  ? 7.442   -10.200 34.336  1.00 16.24 ? 35  THR A C   1 
ATOM   279  O  O   . THR A 1 35  ? 6.448   -9.570  34.787  1.00 15.86 ? 35  THR A O   1 
ATOM   280  C  CB  . THR A 1 35  ? 6.873   -11.073 32.123  1.00 15.56 ? 35  THR A CB  1 
ATOM   281  O  OG1 . THR A 1 35  ? 7.134   -12.439 32.470  1.00 14.87 ? 35  THR A OG1 1 
ATOM   282  C  CG2 . THR A 1 35  ? 7.018   -10.891 30.599  1.00 13.38 ? 35  THR A CG2 1 
ATOM   283  N  N   . HIS A 1 36  ? 8.248   -10.993 35.067  1.00 15.46 ? 36  HIS A N   1 
ATOM   284  C  CA  . HIS A 1 36  ? 8.010   -11.190 36.470  1.00 19.26 ? 36  HIS A CA  1 
ATOM   285  C  C   . HIS A 1 36  ? 8.443   -10.063 37.343  1.00 19.83 ? 36  HIS A C   1 
ATOM   286  O  O   . HIS A 1 36  ? 7.717   -9.755  38.303  1.00 23.72 ? 36  HIS A O   1 
ATOM   287  C  CB  . HIS A 1 36  ? 8.462   -12.606 36.887  1.00 18.15 ? 36  HIS A CB  1 
ATOM   288  C  CG  . HIS A 1 36  ? 7.491   -13.671 36.370  1.00 19.80 ? 36  HIS A CG  1 
ATOM   289  N  ND1 . HIS A 1 36  ? 7.813   -14.603 35.411  1.00 21.19 ? 36  HIS A ND1 1 
ATOM   290  C  CD2 . HIS A 1 36  ? 6.132   -13.836 36.644  1.00 21.48 ? 36  HIS A CD2 1 
ATOM   291  C  CE1 . HIS A 1 36  ? 6.733   -15.339 35.148  1.00 23.50 ? 36  HIS A CE1 1 
ATOM   292  N  NE2 . HIS A 1 36  ? 5.700   -14.870 35.904  1.00 28.20 ? 36  HIS A NE2 1 
ATOM   293  N  N   . THR A 1 37  ? 9.523   -9.374  36.985  1.00 18.66 ? 37  THR A N   1 
ATOM   294  C  CA  . THR A 1 37  ? 9.968   -8.218  37.766  1.00 18.78 ? 37  THR A CA  1 
ATOM   295  C  C   . THR A 1 37  ? 9.510   -6.827  37.258  1.00 18.06 ? 37  THR A C   1 
ATOM   296  O  O   . THR A 1 37  ? 9.732   -5.808  37.951  1.00 17.68 ? 37  THR A O   1 
ATOM   297  C  CB  . THR A 1 37  ? 11.463  -8.308  38.162  1.00 24.39 ? 37  THR A CB  1 
ATOM   298  O  OG1 . THR A 1 37  ? 12.308  -7.832  37.119  1.00 32.34 ? 37  THR A OG1 1 
ATOM   299  C  CG2 . THR A 1 37  ? 11.855  -9.727  38.482  1.00 22.27 ? 37  THR A CG2 1 
ATOM   300  N  N   . ALA A 1 38  ? 8.866   -6.788  36.084  1.00 15.13 ? 38  ALA A N   1 
ATOM   301  C  CA  . ALA A 1 38  ? 8.220   -5.543  35.559  1.00 14.94 ? 38  ALA A CA  1 
ATOM   302  C  C   . ALA A 1 38  ? 7.081   -5.206  36.526  1.00 17.11 ? 38  ALA A C   1 
ATOM   303  O  O   . ALA A 1 38  ? 6.285   -6.055  36.847  1.00 21.09 ? 38  ALA A O   1 
ATOM   304  C  CB  . ALA A 1 38  ? 7.654   -5.770  34.169  1.00 16.74 ? 38  ALA A CB  1 
ATOM   305  N  N   . LYS A 1 39  ? 7.043   -3.985  37.013  1.00 16.90 ? 39  LYS A N   1 
ATOM   306  C  CA  . LYS A 1 39  ? 6.082   -3.638  38.072  1.00 19.73 ? 39  LYS A CA  1 
ATOM   307  C  C   . LYS A 1 39  ? 4.822   -3.078  37.418  1.00 17.46 ? 39  LYS A C   1 
ATOM   308  O  O   . LYS A 1 39  ? 4.897   -2.086  36.654  1.00 16.84 ? 39  LYS A O   1 
ATOM   309  C  CB  . LYS A 1 39  ? 6.819   -2.575  38.905  1.00 21.52 ? 39  LYS A CB  1 
ATOM   310  C  CG  . LYS A 1 39  ? 6.050   -1.713  39.870  1.00 24.98 ? 39  LYS A CG  1 
ATOM   311  C  CD  . LYS A 1 39  ? 5.744   -2.430  41.160  1.00 27.72 ? 39  LYS A CD  1 
ATOM   312  C  CE  . LYS A 1 39  ? 5.022   -1.516  42.136  1.00 28.84 ? 39  LYS A CE  1 
ATOM   313  N  NZ  . LYS A 1 39  ? 4.866   -2.315  43.374  1.00 32.35 ? 39  LYS A NZ  1 
ATOM   314  N  N   . TYR A 1 40  ? 3.654   -3.586  37.794  1.00 17.80 ? 40  TYR A N   1 
ATOM   315  C  CA  . TYR A 1 40  ? 2.430   -2.953  37.312  1.00 19.00 ? 40  TYR A CA  1 
ATOM   316  C  C   . TYR A 1 40  ? 2.318   -1.547  37.916  1.00 19.16 ? 40  TYR A C   1 
ATOM   317  O  O   . TYR A 1 40  ? 2.514   -1.377  39.126  1.00 19.87 ? 40  TYR A O   1 
ATOM   318  C  CB  . TYR A 1 40  ? 1.217   -3.811  37.617  1.00 23.13 ? 40  TYR A CB  1 
ATOM   319  C  CG  . TYR A 1 40  ? -0.064  -3.043  37.528  1.00 26.31 ? 40  TYR A CG  1 
ATOM   320  C  CD1 . TYR A 1 40  ? -0.547  -2.594  36.308  1.00 26.64 ? 40  TYR A CD1 1 
ATOM   321  C  CD2 . TYR A 1 40  ? -0.819  -2.771  38.680  1.00 33.31 ? 40  TYR A CD2 1 
ATOM   322  C  CE1 . TYR A 1 40  ? -1.716  -1.882  36.229  1.00 29.19 ? 40  TYR A CE1 1 
ATOM   323  C  CE2 . TYR A 1 40  ? -2.000  -2.046  38.604  1.00 30.86 ? 40  TYR A CE2 1 
ATOM   324  C  CZ  . TYR A 1 40  ? -2.430  -1.606  37.381  1.00 31.21 ? 40  TYR A CZ  1 
ATOM   325  O  OH  . TYR A 1 40  ? -3.576  -0.902  37.290  1.00 33.36 ? 40  TYR A OH  1 
ATOM   326  N  N   . ASP A 1 41  ? 2.024   -0.551  37.080  1.00 19.08 ? 41  ASP A N   1 
ATOM   327  C  CA  . ASP A 1 41  ? 2.027   0.829   37.527  1.00 21.39 ? 41  ASP A CA  1 
ATOM   328  C  C   . ASP A 1 41  ? 0.665   1.417   37.320  1.00 24.22 ? 41  ASP A C   1 
ATOM   329  O  O   . ASP A 1 41  ? 0.275   1.781   36.185  1.00 22.14 ? 41  ASP A O   1 
ATOM   330  C  CB  . ASP A 1 41  ? 3.030   1.686   36.801  1.00 22.51 ? 41  ASP A CB  1 
ATOM   331  C  CG  . ASP A 1 41  ? 3.077   3.119   37.366  1.00 25.41 ? 41  ASP A CG  1 
ATOM   332  O  OD1 . ASP A 1 41  ? 2.102   3.577   38.015  1.00 23.53 ? 41  ASP A OD1 1 
ATOM   333  O  OD2 . ASP A 1 41  ? 4.103   3.773   37.151  1.00 25.42 ? 41  ASP A OD2 1 
ATOM   334  N  N   . PRO A 1 42  ? -0.084  1.513   38.415  1.00 28.49 ? 42  PRO A N   1 
ATOM   335  C  CA  . PRO A 1 42  ? -1.470  1.844   38.187  1.00 27.71 ? 42  PRO A CA  1 
ATOM   336  C  C   . PRO A 1 42  ? -1.604  3.307   37.804  1.00 25.69 ? 42  PRO A C   1 
ATOM   337  O  O   . PRO A 1 42  ? -2.677  3.684   37.327  1.00 24.76 ? 42  PRO A O   1 
ATOM   338  C  CB  . PRO A 1 42  ? -2.131  1.523   39.545  1.00 29.33 ? 42  PRO A CB  1 
ATOM   339  C  CG  . PRO A 1 42  ? -1.042  1.719   40.549  1.00 28.82 ? 42  PRO A CG  1 
ATOM   340  C  CD  . PRO A 1 42  ? 0.222   1.276   39.845  1.00 28.77 ? 42  PRO A CD  1 
ATOM   341  N  N   . SER A 1 43  ? -0.546  4.119   38.001  1.00 24.44 ? 43  SER A N   1 
ATOM   342  C  CA  . SER A 1 43  ? -0.504  5.525   37.500  1.00 27.69 ? 43  SER A CA  1 
ATOM   343  C  C   . SER A 1 43  ? -0.299  5.730   35.970  1.00 28.63 ? 43  SER A C   1 
ATOM   344  O  O   . SER A 1 43  ? -0.458  6.862   35.462  1.00 28.44 ? 43  SER A O   1 
ATOM   345  C  CB  . SER A 1 43  ? 0.548   6.349   38.246  1.00 26.72 ? 43  SER A CB  1 
ATOM   346  O  OG  . SER A 1 43  ? 1.882   6.057   37.804  1.00 28.76 ? 43  SER A OG  1 
ATOM   347  N  N   . LEU A 1 44  ? 0.081   4.666   35.250  1.00 26.82 ? 44  LEU A N   1 
ATOM   348  C  CA  . LEU A 1 44  ? 0.257   4.740   33.785  1.00 24.04 ? 44  LEU A CA  1 
ATOM   349  C  C   . LEU A 1 44  ? -1.105  4.942   33.156  1.00 27.91 ? 44  LEU A C   1 
ATOM   350  O  O   . LEU A 1 44  ? -2.128  4.488   33.674  1.00 28.02 ? 44  LEU A O   1 
ATOM   351  C  CB  . LEU A 1 44  ? 0.885   3.453   33.223  1.00 21.43 ? 44  LEU A CB  1 
ATOM   352  C  CG  . LEU A 1 44  ? 2.369   3.342   33.526  1.00 19.16 ? 44  LEU A CG  1 
ATOM   353  C  CD1 . LEU A 1 44  ? 2.791   1.965   33.058  1.00 18.03 ? 44  LEU A CD1 1 
ATOM   354  C  CD2 . LEU A 1 44  ? 3.157   4.409   32.789  1.00 18.82 ? 44  LEU A CD2 1 
ATOM   355  N  N   . LYS A 1 45  ? -1.127  5.643   32.035  1.00 28.05 ? 45  LYS A N   1 
ATOM   356  C  CA  . LYS A 1 45  ? -2.394  5.850   31.305  1.00 28.15 ? 45  LYS A CA  1 
ATOM   357  C  C   . LYS A 1 45  ? -2.546  4.833   30.191  1.00 28.16 ? 45  LYS A C   1 
ATOM   358  O  O   . LYS A 1 45  ? -1.577  4.073   29.890  1.00 30.87 ? 45  LYS A O   1 
ATOM   359  C  CB  . LYS A 1 45  ? -2.465  7.255   30.766  1.00 28.80 ? 45  LYS A CB  1 
ATOM   360  C  CG  . LYS A 1 45  ? -2.492  8.295   31.862  1.00 27.82 ? 45  LYS A CG  1 
ATOM   361  C  CD  . LYS A 1 45  ? -3.054  9.611   31.350  1.00 35.98 ? 45  LYS A CD  1 
ATOM   362  C  CE  . LYS A 1 45  ? -3.189  10.602  32.503  1.00 40.99 ? 45  LYS A CE  1 
ATOM   363  N  NZ  . LYS A 1 45  ? -1.830  10.992  32.997  1.00 44.42 ? 45  LYS A NZ  1 
ATOM   364  N  N   . PRO A 1 46  ? -3.767  4.767   29.600  1.00 26.71 ? 46  PRO A N   1 
ATOM   365  C  CA  . PRO A 1 46  ? -3.919  4.022   28.351  1.00 24.76 ? 46  PRO A CA  1 
ATOM   366  C  C   . PRO A 1 46  ? -3.121  4.799   27.322  1.00 19.99 ? 46  PRO A C   1 
ATOM   367  O  O   . PRO A 1 46  ? -3.052  6.021   27.413  1.00 19.40 ? 46  PRO A O   1 
ATOM   368  C  CB  . PRO A 1 46  ? -5.410  4.179   28.040  1.00 24.40 ? 46  PRO A CB  1 
ATOM   369  C  CG  . PRO A 1 46  ? -6.042  4.323   29.387  1.00 28.50 ? 46  PRO A CG  1 
ATOM   370  C  CD  . PRO A 1 46  ? -5.076  5.254   30.087  1.00 28.51 ? 46  PRO A CD  1 
ATOM   371  N  N   . LEU A 1 47  ? -2.509  4.080   26.387  1.00 21.08 ? 47  LEU A N   1 
ATOM   372  C  CA  . LEU A 1 47  ? -1.756  4.717   25.325  1.00 17.32 ? 47  LEU A CA  1 
ATOM   373  C  C   . LEU A 1 47  ? -2.786  5.295   24.387  1.00 20.65 ? 47  LEU A C   1 
ATOM   374  O  O   . LEU A 1 47  ? -3.834  4.662   24.177  1.00 21.34 ? 47  LEU A O   1 
ATOM   375  C  CB  . LEU A 1 47  ? -1.022  3.644   24.570  1.00 20.95 ? 47  LEU A CB  1 
ATOM   376  C  CG  . LEU A 1 47  ? 0.139   4.014   23.750  1.00 21.25 ? 47  LEU A CG  1 
ATOM   377  C  CD1 . LEU A 1 47  ? 1.099   4.869   24.580  1.00 20.92 ? 47  LEU A CD1 1 
ATOM   378  C  CD2 . LEU A 1 47  ? 0.699   2.673   23.283  1.00 23.13 ? 47  LEU A CD2 1 
ATOM   379  N  N   . SER A 1 48  ? -2.476  6.456   23.808  1.00 14.81 ? 48  SER A N   1 
ATOM   380  C  CA  . SER A 1 48  ? -3.275  7.113   22.799  1.00 16.65 ? 48  SER A CA  1 
ATOM   381  C  C   . SER A 1 48  ? -2.522  7.165   21.489  1.00 16.12 ? 48  SER A C   1 
ATOM   382  O  O   . SER A 1 48  ? -1.556  7.930   21.329  1.00 15.78 ? 48  SER A O   1 
ATOM   383  C  CB  . SER A 1 48  ? -3.629  8.523   23.260  1.00 16.43 ? 48  SER A CB  1 
ATOM   384  O  OG  . SER A 1 48  ? -4.356  9.177   22.225  1.00 18.41 ? 48  SER A OG  1 
ATOM   385  N  N   . VAL A 1 49  ? -2.991  6.367   20.543  1.00 15.74 ? 49  VAL A N   1 
ATOM   386  C  CA  . VAL A 1 49  ? -2.411  6.280   19.224  1.00 18.03 ? 49  VAL A CA  1 
ATOM   387  C  C   . VAL A 1 49  ? -3.446  6.864   18.269  1.00 20.01 ? 49  VAL A C   1 
ATOM   388  O  O   . VAL A 1 49  ? -4.502  6.263   18.026  1.00 21.30 ? 49  VAL A O   1 
ATOM   389  C  CB  . VAL A 1 49  ? -2.098  4.818   18.840  1.00 17.98 ? 49  VAL A CB  1 
ATOM   390  C  CG1 . VAL A 1 49  ? -1.308  4.787   17.540  1.00 19.72 ? 49  VAL A CG1 1 
ATOM   391  C  CG2 . VAL A 1 49  ? -1.373  4.101   19.957  1.00 18.03 ? 49  VAL A CG2 1 
ATOM   392  N  N   . SER A 1 50  ? -3.154  8.034   17.726  1.00 18.55 ? 50  SER A N   1 
ATOM   393  C  CA  . SER A 1 50  ? -4.057  8.690   16.767  1.00 20.91 ? 50  SER A CA  1 
ATOM   394  C  C   . SER A 1 50  ? -3.440  8.733   15.393  1.00 19.10 ? 50  SER A C   1 
ATOM   395  O  O   . SER A 1 50  ? -2.760  9.698   15.060  1.00 19.65 ? 50  SER A O   1 
ATOM   396  C  CB  . SER A 1 50  ? -4.361  10.108  17.219  1.00 21.30 ? 50  SER A CB  1 
ATOM   397  O  OG  . SER A 1 50  ? -4.837  10.061  18.526  1.00 31.06 ? 50  SER A OG  1 
ATOM   398  N  N   . TYR A 1 51  ? -3.655  7.688   14.601  1.00 18.87 ? 51  TYR A N   1 
ATOM   399  C  CA  . TYR A 1 51  ? -3.052  7.603   13.277  1.00 16.72 ? 51  TYR A CA  1 
ATOM   400  C  C   . TYR A 1 51  ? -4.054  7.854   12.126  1.00 19.89 ? 51  TYR A C   1 
ATOM   401  O  O   . TYR A 1 51  ? -3.684  7.679   10.965  1.00 18.47 ? 51  TYR A O   1 
ATOM   402  C  CB  . TYR A 1 51  ? -2.357  6.246   13.065  1.00 15.58 ? 51  TYR A CB  1 
ATOM   403  C  CG  . TYR A 1 51  ? -1.094  5.957   13.865  1.00 13.97 ? 51  TYR A CG  1 
ATOM   404  C  CD1 . TYR A 1 51  ? -0.346  6.991   14.462  1.00 12.91 ? 51  TYR A CD1 1 
ATOM   405  C  CD2 . TYR A 1 51  ? -0.605  4.658   13.942  1.00 11.94 ? 51  TYR A CD2 1 
ATOM   406  C  CE1 . TYR A 1 51  ? 0.816   6.710   15.214  1.00 12.87 ? 51  TYR A CE1 1 
ATOM   407  C  CE2 . TYR A 1 51  ? 0.558   4.357   14.635  1.00 12.00 ? 51  TYR A CE2 1 
ATOM   408  C  CZ  . TYR A 1 51  ? 1.267   5.408   15.278  1.00 11.60 ? 51  TYR A CZ  1 
ATOM   409  O  OH  . TYR A 1 51  ? 2.398   5.088   15.960  1.00 11.07 ? 51  TYR A OH  1 
ATOM   410  N  N   . ASP A 1 52  ? -5.285  8.274   12.443  1.00 21.35 ? 52  ASP A N   1 
ATOM   411  C  CA  . ASP A 1 52  ? -6.311  8.474   11.367  1.00 26.24 ? 52  ASP A CA  1 
ATOM   412  C  C   . ASP A 1 52  ? -5.839  9.450   10.267  1.00 24.99 ? 52  ASP A C   1 
ATOM   413  O  O   . ASP A 1 52  ? -6.073  9.208   9.079   1.00 28.89 ? 52  ASP A O   1 
ATOM   414  C  CB  . ASP A 1 52  ? -7.658  8.954   11.923  1.00 29.85 ? 52  ASP A CB  1 
ATOM   415  C  CG  . ASP A 1 52  ? -7.492  10.071  12.928  1.00 33.61 ? 52  ASP A CG  1 
ATOM   416  O  OD1 . ASP A 1 52  ? -7.082  9.798   14.101  1.00 40.17 ? 52  ASP A OD1 1 
ATOM   417  O  OD2 . ASP A 1 52  ? -7.785  11.217  12.545  1.00 40.05 ? 52  ASP A OD2 1 
ATOM   418  N  N   . GLN A 1 53  ? -5.113  10.498  10.640  1.00 24.70 ? 53  GLN A N   1 
ATOM   419  C  CA  . GLN A 1 53  ? -4.633  11.467  9.618   1.00 28.93 ? 53  GLN A CA  1 
ATOM   420  C  C   . GLN A 1 53  ? -3.231  11.246  9.080   1.00 23.76 ? 53  GLN A C   1 
ATOM   421  O  O   . GLN A 1 53  ? -2.727  12.144  8.424   1.00 22.49 ? 53  GLN A O   1 
ATOM   422  C  CB  . GLN A 1 53  ? -4.673  12.909  10.162  1.00 33.18 ? 53  GLN A CB  1 
ATOM   423  C  CG  . GLN A 1 53  ? -6.059  13.482  10.394  1.00 42.42 ? 53  GLN A CG  1 
ATOM   424  C  CD  . GLN A 1 53  ? -6.841  13.479  9.104   1.00 46.60 ? 53  GLN A CD  1 
ATOM   425  O  OE1 . GLN A 1 53  ? -6.562  14.253  8.172   1.00 52.58 ? 53  GLN A OE1 1 
ATOM   426  N  NE2 . GLN A 1 53  ? -7.783  12.568  9.015   1.00 42.95 ? 53  GLN A NE2 1 
ATOM   427  N  N   . ALA A 1 54  ? -2.572  10.129  9.417   1.00 22.00 ? 54  ALA A N   1 
ATOM   428  C  CA  . ALA A 1 54  ? -1.205  9.867   9.000   1.00 18.71 ? 54  ALA A CA  1 
ATOM   429  C  C   . ALA A 1 54  ? -1.018  10.014  7.491   1.00 20.50 ? 54  ALA A C   1 
ATOM   430  O  O   . ALA A 1 54  ? -1.822  9.486   6.703   1.00 20.38 ? 54  ALA A O   1 
ATOM   431  C  CB  . ALA A 1 54  ? -0.736  8.464   9.455   1.00 19.82 ? 54  ALA A CB  1 
ATOM   432  N  N   . THR A 1 55  ? 0.047   10.700  7.078   1.00 17.01 ? 55  THR A N   1 
ATOM   433  C  CA  . THR A 1 55  ? 0.379   10.773  5.657   1.00 18.21 ? 55  THR A CA  1 
ATOM   434  C  C   . THR A 1 55  ? 1.720   10.187  5.299   1.00 16.94 ? 55  THR A C   1 
ATOM   435  O  O   . THR A 1 55  ? 2.747   10.832  5.515   1.00 15.20 ? 55  THR A O   1 
ATOM   436  C  CB  . THR A 1 55  ? 0.503   12.197  5.102   1.00 21.63 ? 55  THR A CB  1 
ATOM   437  O  OG1 . THR A 1 55  ? -0.487  13.002  5.641   1.00 26.39 ? 55  THR A OG1 1 
ATOM   438  C  CG2 . THR A 1 55  ? 0.269   12.122  3.635   1.00 22.09 ? 55  THR A CG2 1 
ATOM   439  N  N   . SER A 1 56  ? 1.743   9.003   4.677   1.00 16.63 ? 56  SER A N   1 
ATOM   440  C  CA  . SER A 1 56  ? 3.026   8.439   4.290   1.00 17.63 ? 56  SER A CA  1 
ATOM   441  C  C   . SER A 1 56  ? 3.606   9.156   3.036   1.00 18.86 ? 56  SER A C   1 
ATOM   442  O  O   . SER A 1 56  ? 2.881   9.702   2.195   1.00 21.05 ? 56  SER A O   1 
ATOM   443  C  CB  . SER A 1 56  ? 2.974   6.885   4.091   1.00 18.04 ? 56  SER A CB  1 
ATOM   444  O  OG  . SER A 1 56  ? 2.026   6.571   3.082   1.00 19.83 ? 56  SER A OG  1 
ATOM   445  N  N   . LEU A 1 57  ? 4.912   9.209   2.946   1.00 18.57 ? 57  LEU A N   1 
ATOM   446  C  CA  . LEU A 1 57  ? 5.519   9.839   1.778   1.00 21.21 ? 57  LEU A CA  1 
ATOM   447  C  C   . LEU A 1 57  ? 6.281   8.875   0.884   1.00 21.98 ? 57  LEU A C   1 
ATOM   448  O  O   . LEU A 1 57  ? 6.055   8.837   -0.341  1.00 21.18 ? 57  LEU A O   1 
ATOM   449  C  CB  . LEU A 1 57  ? 6.441   10.964  2.175   1.00 22.91 ? 57  LEU A CB  1 
ATOM   450  C  CG  . LEU A 1 57  ? 5.650   12.064  2.878   1.00 26.86 ? 57  LEU A CG  1 
ATOM   451  C  CD1 . LEU A 1 57  ? 6.631   13.129  3.301   1.00 27.03 ? 57  LEU A CD1 1 
ATOM   452  C  CD2 . LEU A 1 57  ? 4.477   12.608  2.054   1.00 28.75 ? 57  LEU A CD2 1 
ATOM   453  N  N   . ARG A 1 58  ? 7.195   8.123   1.499   1.00 18.90 ? 58  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 58  ? 8.225   7.414   0.766   1.00 17.89 ? 58  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 58  ? 8.599   6.202   1.571   1.00 17.32 ? 58  ARG A C   1 
ATOM   456  O  O   . ARG A 1 58  ? 8.446   6.194   2.819   1.00 16.21 ? 58  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 58  ? 9.494   8.275   0.650   1.00 19.33 ? 58  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 58  ? 9.585   9.279   -0.509  1.00 26.73 ? 58  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 58  ? 11.046  9.372   -0.876  1.00 29.06 ? 58  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 58  ? 11.824  9.169   0.363   1.00 31.01 ? 58  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 58  ? 13.149  9.293   0.407   1.00 29.95 ? 58  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 58  ? 13.783  9.617   -0.700  1.00 29.80 ? 58  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 58  ? 13.829  9.156   1.537   1.00 28.24 ? 58  ARG A NH2 1 
ATOM   464  N  N   . ILE A 1 59  ? 9.118   5.222   0.858   1.00 16.13 ? 59  ILE A N   1 
ATOM   465  C  CA  . ILE A 1 59  ? 9.770   4.098   1.495   1.00 15.66 ? 59  ILE A CA  1 
ATOM   466  C  C   . ILE A 1 59  ? 11.244  4.062   1.044   1.00 17.12 ? 59  ILE A C   1 
ATOM   467  O  O   . ILE A 1 59  ? 11.565  4.264   -0.138  1.00 16.31 ? 59  ILE A O   1 
ATOM   468  C  CB  . ILE A 1 59  ? 8.968   2.780   1.244   1.00 14.67 ? 59  ILE A CB  1 
ATOM   469  C  CG1 . ILE A 1 59  ? 9.579   1.630   2.050   1.00 13.44 ? 59  ILE A CG1 1 
ATOM   470  C  CG2 . ILE A 1 59  ? 8.984   2.355   -0.227  1.00 14.50 ? 59  ILE A CG2 1 
ATOM   471  C  CD1 . ILE A 1 59  ? 8.809   0.317   1.988   1.00 13.95 ? 59  ILE A CD1 1 
ATOM   472  N  N   . LEU A 1 60  ? 12.169  3.775   1.968   1.00 16.56 ? 60  LEU A N   1 
ATOM   473  C  CA  . LEU A 1 60  ? 13.589  3.908   1.699   1.00 16.06 ? 60  LEU A CA  1 
ATOM   474  C  C   . LEU A 1 60  ? 14.389  2.745   2.277   1.00 16.95 ? 60  LEU A C   1 
ATOM   475  O  O   . LEU A 1 60  ? 14.198  2.337   3.455   1.00 15.25 ? 60  LEU A O   1 
ATOM   476  C  CB  . LEU A 1 60  ? 14.112  5.228   2.339   1.00 16.57 ? 60  LEU A CB  1 
ATOM   477  C  CG  . LEU A 1 60  ? 15.663  5.405   2.359   1.00 18.89 ? 60  LEU A CG  1 
ATOM   478  C  CD1 . LEU A 1 60  ? 16.285  5.614   0.983   1.00 19.73 ? 60  LEU A CD1 1 
ATOM   479  C  CD2 . LEU A 1 60  ? 16.016  6.551   3.317   1.00 18.91 ? 60  LEU A CD2 1 
ATOM   480  N  N   . ASN A 1 61  ? 15.245  2.155   1.445   1.00 14.51 ? 61  ASN A N   1 
ATOM   481  C  CA  . ASN A 1 61  ? 16.267  1.246   1.932   1.00 15.32 ? 61  ASN A CA  1 
ATOM   482  C  C   . ASN A 1 61  ? 17.475  2.100   2.295   1.00 17.33 ? 61  ASN A C   1 
ATOM   483  O  O   . ASN A 1 61  ? 18.091  2.708   1.427   1.00 17.21 ? 61  ASN A O   1 
ATOM   484  C  CB  . ASN A 1 61  ? 16.622  0.199   0.877   1.00 14.66 ? 61  ASN A CB  1 
ATOM   485  C  CG  . ASN A 1 61  ? 17.689  -0.755  1.304   1.00 14.59 ? 61  ASN A CG  1 
ATOM   486  O  OD1 . ASN A 1 61  ? 18.519  -0.468  2.122   1.00 16.17 ? 61  ASN A OD1 1 
ATOM   487  N  ND2 . ASN A 1 61  ? 17.704  -1.943  0.698   1.00 16.97 ? 61  ASN A ND2 1 
ATOM   488  N  N   . ASN A 1 62  ? 17.810  2.152   3.584   1.00 15.73 ? 62  ASN A N   1 
ATOM   489  C  CA  . ASN A 1 62  ? 18.852  3.065   4.005   1.00 15.67 ? 62  ASN A CA  1 
ATOM   490  C  C   . ASN A 1 62  ? 20.125  2.284   4.242   1.00 16.61 ? 62  ASN A C   1 
ATOM   491  O  O   . ASN A 1 62  ? 21.080  2.798   4.848   1.00 17.58 ? 62  ASN A O   1 
ATOM   492  C  CB  . ASN A 1 62  ? 18.371  3.888   5.239   1.00 16.15 ? 62  ASN A CB  1 
ATOM   493  C  CG  . ASN A 1 62  ? 18.242  3.039   6.512   1.00 16.17 ? 62  ASN A CG  1 
ATOM   494  O  OD1 . ASN A 1 62  ? 18.516  1.797   6.511   1.00 14.34 ? 62  ASN A OD1 1 
ATOM   495  N  ND2 . ASN A 1 62  ? 17.888  3.719   7.618   1.00 15.96 ? 62  ASN A ND2 1 
ATOM   496  N  N   . GLY A 1 63  ? 20.147  1.015   3.816   1.00 14.25 ? 63  GLY A N   1 
ATOM   497  C  CA  . GLY A 1 63  ? 21.316  0.188   3.975   1.00 14.50 ? 63  GLY A CA  1 
ATOM   498  C  C   . GLY A 1 63  ? 21.373  -0.628  5.251   1.00 15.96 ? 63  GLY A C   1 
ATOM   499  O  O   . GLY A 1 63  ? 22.211  -1.501  5.375   1.00 14.35 ? 63  GLY A O   1 
ATOM   500  N  N   . HIS A 1 64  ? 20.460  -0.375  6.195   1.00 14.58 ? 64  HIS A N   1 
ATOM   501  C  CA  . HIS A 1 64  ? 20.317  -1.345  7.320   1.00 17.58 ? 64  HIS A CA  1 
ATOM   502  C  C   . HIS A 1 64  ? 18.900  -1.692  7.697   1.00 16.61 ? 64  HIS A C   1 
ATOM   503  O  O   . HIS A 1 64  ? 18.690  -2.559  8.564   1.00 17.75 ? 64  HIS A O   1 
ATOM   504  C  CB  . HIS A 1 64  ? 21.020  -0.933  8.562   1.00 19.96 ? 64  HIS A CB  1 
ATOM   505  C  CG  . HIS A 1 64  ? 20.710  0.456   8.994   1.00 21.20 ? 64  HIS A CG  1 
ATOM   506  N  ND1 . HIS A 1 64  ? 21.409  1.517   8.525   1.00 24.05 ? 64  HIS A ND1 1 
ATOM   507  C  CD2 . HIS A 1 64  ? 19.785  0.965   9.915   1.00 23.41 ? 64  HIS A CD2 1 
ATOM   508  C  CE1 . HIS A 1 64  ? 20.947  2.661   9.088   1.00 23.55 ? 64  HIS A CE1 1 
ATOM   509  N  NE2 . HIS A 1 64  ? 19.977  2.333   9.966   1.00 26.64 ? 64  HIS A NE2 1 
ATOM   510  N  N   . ALA A 1 65  ? 17.925  -1.015  7.120   1.00 13.46 ? 65  ALA A N   1 
ATOM   511  C  CA  . ALA A 1 65  ? 16.535  -1.439  7.302   1.00 14.02 ? 65  ALA A CA  1 
ATOM   512  C  C   . ALA A 1 65  ? 15.823  -0.794  6.152   1.00 14.96 ? 65  ALA A C   1 
ATOM   513  O  O   . ALA A 1 65  ? 16.503  -0.155  5.322   1.00 13.75 ? 65  ALA A O   1 
ATOM   514  C  CB  . ALA A 1 65  ? 15.989  -0.940  8.636   1.00 14.59 ? 65  ALA A CB  1 
ATOM   515  N  N   . PHE A 1 66  ? 14.495  -0.941  6.066   1.00 13.95 ? 66  PHE A N   1 
ATOM   516  C  CA  . PHE A 1 66  ? 13.659  -0.038  5.268   1.00 16.38 ? 66  PHE A CA  1 
ATOM   517  C  C   . PHE A 1 66  ? 12.797  0.842   6.112   1.00 16.90 ? 66  PHE A C   1 
ATOM   518  O  O   . PHE A 1 66  ? 12.244  0.390   7.117   1.00 19.03 ? 66  PHE A O   1 
ATOM   519  C  CB  . PHE A 1 66  ? 12.805  -0.793  4.214   1.00 15.75 ? 66  PHE A CB  1 
ATOM   520  C  CG  . PHE A 1 66  ? 11.775  -1.744  4.811   1.00 15.47 ? 66  PHE A CG  1 
ATOM   521  C  CD1 . PHE A 1 66  ? 10.474  -1.325  5.080   1.00 15.38 ? 66  PHE A CD1 1 
ATOM   522  C  CD2 . PHE A 1 66  ? 12.111  -3.083  5.042   1.00 15.31 ? 66  PHE A CD2 1 
ATOM   523  C  CE1 . PHE A 1 66  ? 9.535   -2.213  5.635   1.00 14.23 ? 66  PHE A CE1 1 
ATOM   524  C  CE2 . PHE A 1 66  ? 11.181  -3.955  5.601   1.00 13.75 ? 66  PHE A CE2 1 
ATOM   525  C  CZ  . PHE A 1 66  ? 9.900   -3.529  5.882   1.00 14.23 ? 66  PHE A CZ  1 
ATOM   526  N  N   . ASN A 1 67  ? 12.734  2.119   5.757   1.00 18.77 ? 67  ASN A N   1 
ATOM   527  C  CA  . ASN A 1 67  ? 11.981  3.045   6.481   1.00 16.56 ? 67  ASN A CA  1 
ATOM   528  C  C   . ASN A 1 67  ? 10.766  3.449   5.710   1.00 15.57 ? 67  ASN A C   1 
ATOM   529  O  O   . ASN A 1 67  ? 10.883  3.782   4.543   1.00 16.14 ? 67  ASN A O   1 
ATOM   530  C  CB  . ASN A 1 67  ? 12.770  4.317   6.691   1.00 18.97 ? 67  ASN A CB  1 
ATOM   531  C  CG  . ASN A 1 67  ? 13.956  4.155   7.601   1.00 21.42 ? 67  ASN A CG  1 
ATOM   532  O  OD1 . ASN A 1 67  ? 14.145  3.113   8.338   1.00 17.51 ? 67  ASN A OD1 1 
ATOM   533  N  ND2 . ASN A 1 67  ? 14.824  5.242   7.583   1.00 25.16 ? 67  ASN A ND2 1 
ATOM   534  N  N   . VAL A 1 68  ? 9.625   3.482   6.353   1.00 13.47 ? 68  VAL A N   1 
ATOM   535  C  CA  . VAL A 1 68  ? 8.462   4.167   5.763   1.00 13.99 ? 68  VAL A CA  1 
ATOM   536  C  C   . VAL A 1 68  ? 8.344   5.543   6.440   1.00 16.77 ? 68  VAL A C   1 
ATOM   537  O  O   . VAL A 1 68  ? 8.178   5.629   7.657   1.00 12.78 ? 68  VAL A O   1 
ATOM   538  C  CB  . VAL A 1 68  ? 7.153   3.368   5.864   1.00 14.30 ? 68  VAL A CB  1 
ATOM   539  C  CG1 . VAL A 1 68  ? 5.976   4.238   5.414   1.00 14.18 ? 68  VAL A CG1 1 
ATOM   540  C  CG2 . VAL A 1 68  ? 7.289   2.099   5.002   1.00 13.87 ? 68  VAL A CG2 1 
ATOM   541  N  N   . GLU A 1 69  ? 8.440   6.616   5.660   1.00 17.09 ? 69  GLU A N   1 
ATOM   542  C  CA  . GLU A 1 69  ? 8.471   7.996   6.212   1.00 17.91 ? 69  GLU A CA  1 
ATOM   543  C  C   . GLU A 1 69  ? 7.148   8.690   6.062   1.00 17.57 ? 69  GLU A C   1 
ATOM   544  O  O   . GLU A 1 69  ? 6.416   8.451   5.063   1.00 16.78 ? 69  GLU A O   1 
ATOM   545  C  CB  . GLU A 1 69  ? 9.377   8.819   5.377   1.00 22.95 ? 69  GLU A CB  1 
ATOM   546  C  CG  . GLU A 1 69  ? 10.791  8.299   5.344   1.00 23.03 ? 69  GLU A CG  1 
ATOM   547  C  CD  . GLU A 1 69  ? 11.505  8.716   4.057   1.00 25.76 ? 69  GLU A CD  1 
ATOM   548  O  OE1 . GLU A 1 69  ? 10.840  9.366   3.190   1.00 26.49 ? 69  GLU A OE1 1 
ATOM   549  O  OE2 . GLU A 1 69  ? 12.698  8.344   3.888   1.00 26.33 ? 69  GLU A OE2 1 
ATOM   550  N  N   . PHE A 1 70  ? 6.873   9.577   7.018   1.00 14.71 ? 70  PHE A N   1 
ATOM   551  C  CA  . PHE A 1 70  ? 5.608   10.292  7.048   1.00 12.85 ? 70  PHE A CA  1 
ATOM   552  C  C   . PHE A 1 70  ? 5.876   11.769  6.966   1.00 13.34 ? 70  PHE A C   1 
ATOM   553  O  O   . PHE A 1 70  ? 6.940   12.204  7.328   1.00 12.29 ? 70  PHE A O   1 
ATOM   554  C  CB  . PHE A 1 70  ? 4.822   9.966   8.314   1.00 12.88 ? 70  PHE A CB  1 
ATOM   555  C  CG  . PHE A 1 70  ? 4.274   8.568   8.281   1.00 12.55 ? 70  PHE A CG  1 
ATOM   556  C  CD1 . PHE A 1 70  ? 5.112   7.473   8.511   1.00 12.95 ? 70  PHE A CD1 1 
ATOM   557  C  CD2 . PHE A 1 70  ? 2.927   8.347   8.013   1.00 12.97 ? 70  PHE A CD2 1 
ATOM   558  C  CE1 . PHE A 1 70  ? 4.581   6.170   8.478   1.00 11.52 ? 70  PHE A CE1 1 
ATOM   559  C  CE2 . PHE A 1 70  ? 2.406   7.051   7.908   1.00 12.39 ? 70  PHE A CE2 1 
ATOM   560  C  CZ  . PHE A 1 70  ? 3.258   5.973   8.121   1.00 11.82 ? 70  PHE A CZ  1 
ATOM   561  N  N   . ASP A 1 71  ? 4.899   12.522  6.473   1.00 14.62 ? 71  ASP A N   1 
ATOM   562  C  CA  . ASP A 1 71  ? 4.952   13.961  6.585   1.00 17.10 ? 71  ASP A CA  1 
ATOM   563  C  C   . ASP A 1 71  ? 4.595   14.382  8.001   1.00 16.12 ? 71  ASP A C   1 
ATOM   564  O  O   . ASP A 1 71  ? 3.459   14.222  8.431   1.00 18.00 ? 71  ASP A O   1 
ATOM   565  C  CB  . ASP A 1 71  ? 4.016   14.594  5.599   1.00 21.82 ? 71  ASP A CB  1 
ATOM   566  C  CG  . ASP A 1 71  ? 3.772   16.062  5.926   1.00 25.41 ? 71  ASP A CG  1 
ATOM   567  O  OD1 . ASP A 1 71  ? 4.749   16.732  6.315   1.00 27.92 ? 71  ASP A OD1 1 
ATOM   568  O  OD2 . ASP A 1 71  ? 2.610   16.502  5.876   1.00 31.12 ? 71  ASP A OD2 1 
ATOM   569  N  N   . ASP A 1 72  ? 5.575   14.849  8.755   1.00 14.64 ? 72  ASP A N   1 
ATOM   570  C  CA  . ASP A 1 72  ? 5.400   15.228  10.139  1.00 15.89 ? 72  ASP A CA  1 
ATOM   571  C  C   . ASP A 1 72  ? 5.392   16.764  10.282  1.00 18.68 ? 72  ASP A C   1 
ATOM   572  O  O   . ASP A 1 72  ? 5.792   17.282  11.313  1.00 20.31 ? 72  ASP A O   1 
ATOM   573  C  CB  . ASP A 1 72  ? 6.535   14.636  11.005  1.00 16.70 ? 72  ASP A CB  1 
ATOM   574  C  CG  . ASP A 1 72  ? 7.940   15.176  10.657  1.00 17.81 ? 72  ASP A CG  1 
ATOM   575  O  OD1 . ASP A 1 72  ? 8.160   15.841  9.608   1.00 16.19 ? 72  ASP A OD1 1 
ATOM   576  O  OD2 . ASP A 1 72  ? 8.860   14.929  11.445  1.00 16.10 ? 72  ASP A OD2 1 
ATOM   577  N  N   . SER A 1 73  ? 4.984   17.473  9.245   1.00 19.13 ? 73  SER A N   1 
ATOM   578  C  CA  . SER A 1 73  ? 5.048   18.968  9.293   1.00 21.36 ? 73  SER A CA  1 
ATOM   579  C  C   . SER A 1 73  ? 3.756   19.558  9.840   1.00 21.22 ? 73  SER A C   1 
ATOM   580  O  O   . SER A 1 73  ? 3.639   20.793  10.047  1.00 20.24 ? 73  SER A O   1 
ATOM   581  C  CB  . SER A 1 73  ? 5.337   19.539  7.917   1.00 20.40 ? 73  SER A CB  1 
ATOM   582  O  OG  . SER A 1 73  ? 4.195   19.341  7.110   1.00 21.10 ? 73  SER A OG  1 
ATOM   583  N  N   . GLN A 1 74  ? 2.752   18.708  10.064  1.00 23.24 ? 74  GLN A N   1 
ATOM   584  C  CA  . GLN A 1 74  ? 1.594   19.165  10.789  1.00 25.58 ? 74  GLN A CA  1 
ATOM   585  C  C   . GLN A 1 74  ? 1.287   18.179  11.836  1.00 29.29 ? 74  GLN A C   1 
ATOM   586  O  O   . GLN A 1 74  ? 1.842   17.059  11.859  1.00 24.33 ? 74  GLN A O   1 
ATOM   587  C  CB  . GLN A 1 74  ? 0.353   19.207  9.911   1.00 27.10 ? 74  GLN A CB  1 
ATOM   588  C  CG  . GLN A 1 74  ? 0.277   20.435  9.044   1.00 32.74 ? 74  GLN A CG  1 
ATOM   589  C  CD  . GLN A 1 74  ? -0.925  20.384  8.155   1.00 34.88 ? 74  GLN A CD  1 
ATOM   590  O  OE1 . GLN A 1 74  ? -1.941  20.979  8.468   1.00 50.14 ? 74  GLN A OE1 1 
ATOM   591  N  NE2 . GLN A 1 74  ? -0.839  19.646  7.070   1.00 35.01 ? 74  GLN A NE2 1 
ATOM   592  N  N   . ASP A 1 75  ? 0.329   18.577  12.666  1.00 29.07 ? 75  ASP A N   1 
ATOM   593  C  CA  . ASP A 1 75  ? -0.040  17.728  13.759  1.00 30.12 ? 75  ASP A CA  1 
ATOM   594  C  C   . ASP A 1 75  ? -1.067  16.698  13.339  1.00 29.57 ? 75  ASP A C   1 
ATOM   595  O  O   . ASP A 1 75  ? -2.272  16.894  13.470  1.00 29.73 ? 75  ASP A O   1 
ATOM   596  C  CB  . ASP A 1 75  ? -0.477  18.544  14.941  1.00 35.83 ? 75  ASP A CB  1 
ATOM   597  C  CG  . ASP A 1 75  ? -0.230  17.800  16.202  1.00 41.10 ? 75  ASP A CG  1 
ATOM   598  O  OD1 . ASP A 1 75  ? 0.979   17.538  16.586  1.00 39.64 ? 75  ASP A OD1 1 
ATOM   599  O  OD2 . ASP A 1 75  ? -1.260  17.377  16.729  1.00 36.55 ? 75  ASP A OD2 1 
ATOM   600  N  N   . LYS A 1 76  ? -0.568  15.584  12.826  1.00 24.80 ? 76  LYS A N   1 
ATOM   601  C  CA  . LYS A 1 76  ? -1.462  14.579  12.255  1.00 28.78 ? 76  LYS A CA  1 
ATOM   602  C  C   . LYS A 1 76  ? -1.478  13.308  13.146  1.00 29.69 ? 76  LYS A C   1 
ATOM   603  O  O   . LYS A 1 76  ? -2.321  13.185  14.059  1.00 33.36 ? 76  LYS A O   1 
ATOM   604  C  CB  . LYS A 1 76  ? -1.084  14.292  10.792  1.00 28.51 ? 76  LYS A CB  1 
ATOM   605  C  CG  . LYS A 1 76  ? -1.675  15.293  9.801   1.00 32.64 ? 76  LYS A CG  1 
ATOM   606  C  CD  . LYS A 1 76  ? -0.746  15.468  8.609   1.00 32.72 ? 76  LYS A CD  1 
ATOM   607  C  CE  . LYS A 1 76  ? -1.456  16.101  7.414   1.00 38.84 ? 76  LYS A CE  1 
ATOM   608  N  NZ  . LYS A 1 76  ? -0.582  16.057  6.218   1.00 34.38 ? 76  LYS A NZ  1 
ATOM   609  N  N   . ALA A 1 77  ? -0.508  12.439  12.907  1.00 24.70 ? 77  ALA A N   1 
ATOM   610  C  CA  . ALA A 1 77  ? -0.393  11.125  13.533  1.00 20.49 ? 77  ALA A CA  1 
ATOM   611  C  C   . ALA A 1 77  ? 0.362   11.338  14.841  1.00 19.96 ? 77  ALA A C   1 
ATOM   612  O  O   . ALA A 1 77  ? 1.527   11.727  14.803  1.00 21.03 ? 77  ALA A O   1 
ATOM   613  C  CB  . ALA A 1 77  ? 0.445   10.247  12.631  1.00 20.11 ? 77  ALA A CB  1 
ATOM   614  N  N   . VAL A 1 78  ? -0.270  11.124  15.974  1.00 15.83 ? 78  VAL A N   1 
ATOM   615  C  CA  . VAL A 1 78  ? 0.413   11.402  17.254  1.00 15.80 ? 78  VAL A CA  1 
ATOM   616  C  C   . VAL A 1 78  ? 0.168   10.291  18.274  1.00 14.07 ? 78  VAL A C   1 
ATOM   617  O  O   . VAL A 1 78  ? -0.926  9.623   18.318  1.00 13.34 ? 78  VAL A O   1 
ATOM   618  C  CB  . VAL A 1 78  ? -0.030  12.734  17.894  1.00 18.94 ? 78  VAL A CB  1 
ATOM   619  C  CG1 . VAL A 1 78  ? 0.330   13.955  17.039  1.00 19.68 ? 78  VAL A CG1 1 
ATOM   620  C  CG2 . VAL A 1 78  ? -1.498  12.689  18.189  1.00 18.98 ? 78  VAL A CG2 1 
ATOM   621  N  N   . LEU A 1 79  ? 1.209   10.141  19.100  1.00 13.19 ? 79  LEU A N   1 
ATOM   622  C  CA  . LEU A 1 79  ? 1.238   9.236   20.204  1.00 13.95 ? 79  LEU A CA  1 
ATOM   623  C  C   . LEU A 1 79  ? 1.313   10.099  21.451  1.00 14.38 ? 79  LEU A C   1 
ATOM   624  O  O   . LEU A 1 79  ? 2.052   11.079  21.489  1.00 14.71 ? 79  LEU A O   1 
ATOM   625  C  CB  . LEU A 1 79  ? 2.478   8.344   20.012  1.00 13.38 ? 79  LEU A CB  1 
ATOM   626  C  CG  . LEU A 1 79  ? 2.609   7.363   21.150  1.00 15.17 ? 79  LEU A CG  1 
ATOM   627  C  CD1 . LEU A 1 79  ? 1.532   6.296   21.102  1.00 17.57 ? 79  LEU A CD1 1 
ATOM   628  C  CD2 . LEU A 1 79  ? 3.988   6.728   21.047  1.00 13.34 ? 79  LEU A CD2 1 
ATOM   629  N  N   . LYS A 1 80  ? 0.475   9.805   22.444  1.00 14.26 ? 80  LYS A N   1 
ATOM   630  C  CA  . LYS A 1 80  ? 0.525   10.499  23.728  1.00 14.81 ? 80  LYS A CA  1 
ATOM   631  C  C   . LYS A 1 80  ? -0.130  9.581   24.766  1.00 15.45 ? 80  LYS A C   1 
ATOM   632  O  O   . LYS A 1 80  ? -0.527  8.449   24.441  1.00 13.04 ? 80  LYS A O   1 
ATOM   633  C  CB  . LYS A 1 80  ? -0.191  11.878  23.649  1.00 18.28 ? 80  LYS A CB  1 
ATOM   634  C  CG  . LYS A 1 80  ? -1.661  11.712  23.308  1.00 21.72 ? 80  LYS A CG  1 
ATOM   635  C  CD  . LYS A 1 80  ? -2.173  13.058  22.771  1.00 27.40 ? 80  LYS A CD  1 
ATOM   636  C  CE  . LYS A 1 80  ? -3.329  13.556  23.615  1.00 36.75 ? 80  LYS A CE  1 
ATOM   637  N  NZ  . LYS A 1 80  ? -4.629  12.953  23.157  1.00 37.16 ? 80  LYS A NZ  1 
ATOM   638  N  N   . GLY A 1 81  ? -0.202  10.045  26.010  1.00 16.05 ? 81  GLY A N   1 
ATOM   639  C  CA  . GLY A 1 81  ? -0.784  9.229   27.070  1.00 15.57 ? 81  GLY A CA  1 
ATOM   640  C  C   . GLY A 1 81  ? 0.195   8.158   27.413  1.00 17.75 ? 81  GLY A C   1 
ATOM   641  O  O   . GLY A 1 81  ? 1.401   8.351   27.220  1.00 15.81 ? 81  GLY A O   1 
ATOM   642  N  N   . GLY A 1 82  ? -0.275  7.015   27.919  1.00 16.94 ? 82  GLY A N   1 
ATOM   643  C  CA  . GLY A 1 82  ? 0.695   5.987   28.301  1.00 17.41 ? 82  GLY A CA  1 
ATOM   644  C  C   . GLY A 1 82  ? 1.589   6.590   29.400  1.00 17.15 ? 82  GLY A C   1 
ATOM   645  O  O   . GLY A 1 82  ? 1.060   7.238   30.334  1.00 19.89 ? 82  GLY A O   1 
ATOM   646  N  N   . PRO A 1 83  ? 2.956   6.468   29.290  1.00 14.60 ? 83  PRO A N   1 
ATOM   647  C  CA  . PRO A 1 83  ? 3.871   7.078   30.220  1.00 14.33 ? 83  PRO A CA  1 
ATOM   648  C  C   . PRO A 1 83  ? 4.255   8.498   29.812  1.00 14.85 ? 83  PRO A C   1 
ATOM   649  O  O   . PRO A 1 83  ? 5.045   9.133   30.476  1.00 17.32 ? 83  PRO A O   1 
ATOM   650  C  CB  . PRO A 1 83  ? 5.140   6.215   30.051  1.00 15.61 ? 83  PRO A CB  1 
ATOM   651  C  CG  . PRO A 1 83  ? 5.145   5.901   28.576  1.00 12.94 ? 83  PRO A CG  1 
ATOM   652  C  CD  . PRO A 1 83  ? 3.693   5.685   28.248  1.00 13.09 ? 83  PRO A CD  1 
ATOM   653  N  N   . LEU A 1 84  ? 3.716   8.991   28.712  1.00 15.30 ? 84  LEU A N   1 
ATOM   654  C  CA  . LEU A 1 84  ? 4.314   10.189  28.070  1.00 13.30 ? 84  LEU A CA  1 
ATOM   655  C  C   . LEU A 1 84  ? 3.654   11.432  28.660  1.00 16.65 ? 84  LEU A C   1 
ATOM   656  O  O   . LEU A 1 84  ? 2.459   11.393  29.003  1.00 15.35 ? 84  LEU A O   1 
ATOM   657  C  CB  . LEU A 1 84  ? 4.083   10.171  26.599  1.00 12.31 ? 84  LEU A CB  1 
ATOM   658  C  CG  . LEU A 1 84  ? 4.637   8.909   25.877  1.00 11.29 ? 84  LEU A CG  1 
ATOM   659  C  CD1 . LEU A 1 84  ? 4.084   8.814   24.468  1.00 12.21 ? 84  LEU A CD1 1 
ATOM   660  C  CD2 . LEU A 1 84  ? 6.194   8.863   25.979  1.00 11.29 ? 84  LEU A CD2 1 
ATOM   661  N  N   A ASP A 1 85  ? 4.441   12.490  28.817  0.50 17.08 ? 85  ASP A N   1 
ATOM   662  N  N   B ASP A 1 85  ? 4.427   12.514  28.656  0.50 15.53 ? 85  ASP A N   1 
ATOM   663  C  CA  A ASP A 1 85  ? 3.946   13.744  29.394  0.50 19.81 ? 85  ASP A CA  1 
ATOM   664  C  CA  B ASP A 1 85  ? 3.921   13.869  28.856  0.50 16.54 ? 85  ASP A CA  1 
ATOM   665  C  C   A ASP A 1 85  ? 3.604   14.703  28.287  0.50 20.33 ? 85  ASP A C   1 
ATOM   666  C  C   B ASP A 1 85  ? 3.980   14.568  27.529  0.50 15.60 ? 85  ASP A C   1 
ATOM   667  O  O   A ASP A 1 85  ? 3.159   15.827  28.538  0.50 21.49 ? 85  ASP A O   1 
ATOM   668  O  O   B ASP A 1 85  ? 4.994   14.503  26.843  0.50 14.22 ? 85  ASP A O   1 
ATOM   669  C  CB  A ASP A 1 85  ? 5.004   14.375  30.285  0.50 22.49 ? 85  ASP A CB  1 
ATOM   670  C  CB  B ASP A 1 85  ? 4.830   14.627  29.805  0.50 19.35 ? 85  ASP A CB  1 
ATOM   671  C  CG  A ASP A 1 85  ? 4.863   13.963  31.739  0.50 25.66 ? 85  ASP A CG  1 
ATOM   672  C  CG  B ASP A 1 85  ? 4.521   14.347  31.245  0.50 23.14 ? 85  ASP A CG  1 
ATOM   673  O  OD1 A ASP A 1 85  ? 3.760   13.518  32.128  0.50 26.95 ? 85  ASP A OD1 1 
ATOM   674  O  OD1 B ASP A 1 85  ? 3.315   14.298  31.606  0.50 24.39 ? 85  ASP A OD1 1 
ATOM   675  O  OD2 A ASP A 1 85  ? 5.853   14.107  32.496  0.50 27.16 ? 85  ASP A OD2 1 
ATOM   676  O  OD2 B ASP A 1 85  ? 5.494   14.230  32.030  0.50 24.52 ? 85  ASP A OD2 1 
ATOM   677  N  N   A GLY A 1 86  ? 3.833   14.295  27.049  0.50 20.00 ? 86  GLY A N   1 
ATOM   678  N  N   B GLY A 1 86  ? 2.913   15.294  27.191  0.50 13.97 ? 86  GLY A N   1 
ATOM   679  C  CA  A GLY A 1 86  ? 3.627   15.225  25.955  0.50 18.87 ? 86  GLY A CA  1 
ATOM   680  C  CA  B GLY A 1 86  ? 2.896   16.111  26.009  0.50 13.84 ? 86  GLY A CA  1 
ATOM   681  C  C   A GLY A 1 86  ? 3.004   14.620  24.711  0.50 18.39 ? 86  GLY A C   1 
ATOM   682  C  C   B GLY A 1 86  ? 2.451   15.227  24.866  0.50 14.64 ? 86  GLY A C   1 
ATOM   683  O  O   A GLY A 1 86  ? 2.362   13.570  24.764  0.50 19.37 ? 86  GLY A O   1 
ATOM   684  O  O   B GLY A 1 86  ? 1.681   14.309  25.077  0.50 15.18 ? 86  GLY A O   1 
ATOM   685  N  N   A THR A 1 87  ? 3.181   15.315  23.601  0.50 16.47 ? 87  THR A N   1 
ATOM   686  N  N   B THR A 1 87  ? 2.989   15.455  23.674  0.50 14.16 ? 87  THR A N   1 
ATOM   687  C  CA  A THR A 1 87  ? 2.599   14.930  22.341  0.50 15.30 ? 87  THR A CA  1 
ATOM   688  C  CA  B THR A 1 87  ? 2.548   14.724  22.496  0.50 14.25 ? 87  THR A CA  1 
ATOM   689  C  C   A THR A 1 87  ? 3.732   14.552  21.428  0.50 14.30 ? 87  THR A C   1 
ATOM   690  C  C   B THR A 1 87  ? 3.722   14.480  21.575  0.50 13.58 ? 87  THR A C   1 
ATOM   691  O  O   A THR A 1 87  ? 4.620   15.345  21.197  0.50 12.76 ? 87  THR A O   1 
ATOM   692  O  O   B THR A 1 87  ? 4.596   15.319  21.437  0.50 12.12 ? 87  THR A O   1 
ATOM   693  C  CB  A THR A 1 87  ? 1.765   16.115  21.777  0.50 16.30 ? 87  THR A CB  1 
ATOM   694  C  CB  B THR A 1 87  ? 1.450   15.554  21.783  0.50 15.99 ? 87  THR A CB  1 
ATOM   695  O  OG1 A THR A 1 87  ? 0.444   16.052  22.345  0.50 16.52 ? 87  THR A OG1 1 
ATOM   696  O  OG1 B THR A 1 87  ? 1.084   14.964  20.531  0.50 19.58 ? 87  THR A OG1 1 
ATOM   697  C  CG2 A THR A 1 87  ? 1.671   16.073  20.252  0.50 16.71 ? 87  THR A CG2 1 
ATOM   698  C  CG2 B THR A 1 87  ? 1.927   16.982  21.572  0.50 14.80 ? 87  THR A CG2 1 
ATOM   699  N  N   . TYR A 1 88  ? 3.728   13.319  20.928  1.00 11.83 ? 88  TYR A N   1 
ATOM   700  C  CA  . TYR A 1 88  ? 4.840   12.915  20.093  1.00 11.36 ? 88  TYR A CA  1 
ATOM   701  C  C   . TYR A 1 88  ? 4.332   12.657  18.691  1.00 12.18 ? 88  TYR A C   1 
ATOM   702  O  O   . TYR A 1 88  ? 3.327   11.942  18.517  1.00 13.88 ? 88  TYR A O   1 
ATOM   703  C  CB  . TYR A 1 88  ? 5.478   11.629  20.655  1.00 9.82  ? 88  TYR A CB  1 
ATOM   704  C  CG  . TYR A 1 88  ? 6.258   11.844  21.975  1.00 10.57 ? 88  TYR A CG  1 
ATOM   705  C  CD1 . TYR A 1 88  ? 5.588   12.141  23.172  1.00 9.90  ? 88  TYR A CD1 1 
ATOM   706  C  CD2 . TYR A 1 88  ? 7.657   11.719  21.996  1.00 9.69  ? 88  TYR A CD2 1 
ATOM   707  C  CE1 . TYR A 1 88  ? 6.316   12.357  24.377  1.00 10.40 ? 88  TYR A CE1 1 
ATOM   708  C  CE2 . TYR A 1 88  ? 8.390   11.912  23.184  1.00 9.56  ? 88  TYR A CE2 1 
ATOM   709  C  CZ  . TYR A 1 88  ? 7.677   12.219  24.364  1.00 9.88  ? 88  TYR A CZ  1 
ATOM   710  O  OH  . TYR A 1 88  ? 8.361   12.351  25.526  1.00 9.30  ? 88  TYR A OH  1 
ATOM   711  N  N   . ARG A 1 89  ? 5.039   13.161  17.693  1.00 11.08 ? 89  ARG A N   1 
ATOM   712  C  CA  . ARG A 1 89  ? 4.568   13.095  16.330  1.00 11.33 ? 89  ARG A CA  1 
ATOM   713  C  C   . ARG A 1 89  ? 5.231   11.964  15.532  1.00 9.81  ? 89  ARG A C   1 
ATOM   714  O  O   . ARG A 1 89  ? 6.453   11.853  15.533  1.00 9.21  ? 89  ARG A O   1 
ATOM   715  C  CB  . ARG A 1 89  ? 4.800   14.457  15.661  1.00 14.61 ? 89  ARG A CB  1 
ATOM   716  C  CG  . ARG A 1 89  ? 4.083   14.563  14.357  1.00 17.94 ? 89  ARG A CG  1 
ATOM   717  C  CD  . ARG A 1 89  ? 4.205   16.004  13.885  1.00 17.49 ? 89  ARG A CD  1 
ATOM   718  N  NE  . ARG A 1 89  ? 3.554   16.985  14.740  1.00 17.17 ? 89  ARG A NE  1 
ATOM   719  C  CZ  . ARG A 1 89  ? 3.686   18.286  14.502  1.00 17.70 ? 89  ARG A CZ  1 
ATOM   720  N  NH1 . ARG A 1 89  ? 4.398   18.675  13.448  1.00 17.21 ? 89  ARG A NH1 1 
ATOM   721  N  NH2 . ARG A 1 89  ? 3.125   19.202  15.293  1.00 18.05 ? 89  ARG A NH2 1 
ATOM   722  N  N   . LEU A 1 90  ? 4.411   11.121  14.851  1.00 9.48  ? 90  LEU A N   1 
ATOM   723  C  CA  . LEU A 1 90  ? 5.014   10.029  14.016  1.00 9.90  ? 90  LEU A CA  1 
ATOM   724  C  C   . LEU A 1 90  ? 5.864   10.550  12.868  1.00 9.46  ? 90  LEU A C   1 
ATOM   725  O  O   . LEU A 1 90  ? 5.396   11.387  12.078  1.00 10.60 ? 90  LEU A O   1 
ATOM   726  C  CB  . LEU A 1 90  ? 3.925   9.178   13.414  1.00 11.01 ? 90  LEU A CB  1 
ATOM   727  C  CG  . LEU A 1 90  ? 4.419   8.028   12.520  1.00 11.33 ? 90  LEU A CG  1 
ATOM   728  C  CD1 . LEU A 1 90  ? 5.167   6.952   13.304  1.00 13.27 ? 90  LEU A CD1 1 
ATOM   729  C  CD2 . LEU A 1 90  ? 3.170   7.403   11.918  1.00 13.73 ? 90  LEU A CD2 1 
ATOM   730  N  N   . ILE A 1 91  ? 7.098   10.088  12.780  1.00 9.95  ? 91  ILE A N   1 
ATOM   731  C  CA  . ILE A 1 91  ? 8.008   10.466  11.687  1.00 10.10 ? 91  ILE A CA  1 
ATOM   732  C  C   . ILE A 1 91  ? 8.253   9.302   10.732  1.00 10.59 ? 91  ILE A C   1 
ATOM   733  O  O   . ILE A 1 91  ? 8.354   9.494   9.493   1.00 11.01 ? 91  ILE A O   1 
ATOM   734  C  CB  . ILE A 1 91  ? 9.324   11.132  12.176  1.00 10.03 ? 91  ILE A CB  1 
ATOM   735  C  CG1 . ILE A 1 91  ? 10.200  11.555  10.975  1.00 11.97 ? 91  ILE A CG1 1 
ATOM   736  C  CG2 . ILE A 1 91  ? 10.045  10.235  13.164  1.00 9.92  ? 91  ILE A CG2 1 
ATOM   737  C  CD1 . ILE A 1 91  ? 11.280  12.564  11.349  1.00 14.15 ? 91  ILE A CD1 1 
ATOM   738  N  N   . GLN A 1 92  ? 8.411   8.073   11.257  1.00 9.64  ? 92  GLN A N   1 
ATOM   739  C  CA  . GLN A 1 92  ? 8.736   6.995   10.366  1.00 9.71  ? 92  GLN A CA  1 
ATOM   740  C  C   . GLN A 1 92  ? 8.502   5.708   11.119  1.00 9.20  ? 92  GLN A C   1 
ATOM   741  O  O   . GLN A 1 92  ? 8.365   5.718   12.335  1.00 8.60  ? 92  GLN A O   1 
ATOM   742  C  CB  . GLN A 1 92  ? 10.183  7.036   9.796   1.00 12.26 ? 92  GLN A CB  1 
ATOM   743  C  CG  . GLN A 1 92  ? 11.288  6.942   10.834  1.00 14.34 ? 92  GLN A CG  1 
ATOM   744  C  CD  . GLN A 1 92  ? 11.953  5.561   10.762  1.00 16.26 ? 92  GLN A CD  1 
ATOM   745  O  OE1 . GLN A 1 92  ? 11.492  4.665   11.345  1.00 13.79 ? 92  GLN A OE1 1 
ATOM   746  N  NE2 . GLN A 1 92  ? 13.007  5.431   9.990   1.00 20.70 ? 92  GLN A NE2 1 
ATOM   747  N  N   . PHE A 1 93  ? 8.430   4.622   10.358  1.00 8.45  ? 93  PHE A N   1 
ATOM   748  C  CA  . PHE A 1 93  ? 8.530   3.307   10.981  1.00 8.20  ? 93  PHE A CA  1 
ATOM   749  C  C   . PHE A 1 93  ? 9.505   2.404   10.234  1.00 8.50  ? 93  PHE A C   1 
ATOM   750  O  O   . PHE A 1 93  ? 9.816   2.595   9.028   1.00 7.63  ? 93  PHE A O   1 
ATOM   751  C  CB  . PHE A 1 93  ? 7.169   2.636   11.249  1.00 8.74  ? 93  PHE A CB  1 
ATOM   752  C  CG  . PHE A 1 93  ? 6.482   2.130   10.015  1.00 9.23  ? 93  PHE A CG  1 
ATOM   753  C  CD1 . PHE A 1 93  ? 6.930   0.992   9.324   1.00 10.29 ? 93  PHE A CD1 1 
ATOM   754  C  CD2 . PHE A 1 93  ? 5.343   2.800   9.561   1.00 9.91  ? 93  PHE A CD2 1 
ATOM   755  C  CE1 . PHE A 1 93  ? 6.277   0.532   8.149   1.00 11.29 ? 93  PHE A CE1 1 
ATOM   756  C  CE2 . PHE A 1 93  ? 4.671   2.349   8.398   1.00 10.79 ? 93  PHE A CE2 1 
ATOM   757  C  CZ  . PHE A 1 93  ? 5.148   1.229   7.700   1.00 12.01 ? 93  PHE A CZ  1 
ATOM   758  N  N   . HIS A 1 94  ? 9.985   1.351   10.899  1.00 7.74  ? 94  HIS A N   1 
ATOM   759  C  CA  . HIS A 1 94  ? 10.914  0.454   10.250  1.00 7.22  ? 94  HIS A CA  1 
ATOM   760  C  C   . HIS A 1 94  ? 10.829  -0.818  11.012  1.00 6.97  ? 94  HIS A C   1 
ATOM   761  O  O   . HIS A 1 94  ? 10.142  -0.847  12.023  1.00 7.17  ? 94  HIS A O   1 
ATOM   762  C  CB  . HIS A 1 94  ? 12.422  0.910   10.235  1.00 7.99  ? 94  HIS A CB  1 
ATOM   763  C  CG  . HIS A 1 94  ? 12.955  1.194   11.603  1.00 7.30  ? 94  HIS A CG  1 
ATOM   764  N  ND1 . HIS A 1 94  ? 12.726  2.413   12.220  1.00 8.05  ? 94  HIS A ND1 1 
ATOM   765  C  CD2 . HIS A 1 94  ? 13.575  0.380   12.534  1.00 7.43  ? 94  HIS A CD2 1 
ATOM   766  C  CE1 . HIS A 1 94  ? 13.260  2.364   13.454  1.00 7.39  ? 94  HIS A CE1 1 
ATOM   767  N  NE2 . HIS A 1 94  ? 13.820  1.126   13.630  1.00 7.26  ? 94  HIS A NE2 1 
ATOM   768  N  N   . PHE A 1 95  ? 11.503  -1.862  10.539  1.00 7.36  ? 95  PHE A N   1 
ATOM   769  C  CA  . PHE A 1 95  ? 11.564  -3.164  11.222  1.00 7.60  ? 95  PHE A CA  1 
ATOM   770  C  C   . PHE A 1 95  ? 13.025  -3.612  11.444  1.00 7.24  ? 95  PHE A C   1 
ATOM   771  O  O   . PHE A 1 95  ? 13.959  -3.141  10.799  1.00 8.17  ? 95  PHE A O   1 
ATOM   772  C  CB  . PHE A 1 95  ? 10.891  -4.260  10.375  1.00 7.88  ? 95  PHE A CB  1 
ATOM   773  C  CG  . PHE A 1 95  ? 9.425   -4.000  10.113  1.00 7.71  ? 95  PHE A CG  1 
ATOM   774  C  CD1 . PHE A 1 95  ? 9.032   -3.133  9.070   1.00 8.47  ? 95  PHE A CD1 1 
ATOM   775  C  CD2 . PHE A 1 95  ? 8.426   -4.684  10.801  1.00 8.68  ? 95  PHE A CD2 1 
ATOM   776  C  CE1 . PHE A 1 95  ? 7.675   -2.939  8.794   1.00 8.59  ? 95  PHE A CE1 1 
ATOM   777  C  CE2 . PHE A 1 95  ? 7.071   -4.467  10.541  1.00 8.73  ? 95  PHE A CE2 1 
ATOM   778  C  CZ  . PHE A 1 95  ? 6.710   -3.598  9.507   1.00 9.30  ? 95  PHE A CZ  1 
ATOM   779  N  N   . HIS A 1 96  ? 13.178  -4.598  12.340  1.00 7.67  ? 96  HIS A N   1 
ATOM   780  C  CA  . HIS A 1 96  ? 14.400  -5.355  12.565  1.00 7.26  ? 96  HIS A CA  1 
ATOM   781  C  C   . HIS A 1 96  ? 14.015  -6.803  12.445  1.00 7.52  ? 96  HIS A C   1 
ATOM   782  O  O   . HIS A 1 96  ? 12.945  -7.165  12.962  1.00 7.15  ? 96  HIS A O   1 
ATOM   783  C  CB  . HIS A 1 96  ? 14.996  -5.110  13.977  1.00 7.79  ? 96  HIS A CB  1 
ATOM   784  C  CG  . HIS A 1 96  ? 15.304  -3.677  14.222  1.00 8.01  ? 96  HIS A CG  1 
ATOM   785  N  ND1 . HIS A 1 96  ? 16.564  -3.149  14.022  1.00 7.96  ? 96  HIS A ND1 1 
ATOM   786  C  CD2 . HIS A 1 96  ? 14.458  -2.625  14.539  1.00 8.62  ? 96  HIS A CD2 1 
ATOM   787  C  CE1 . HIS A 1 96  ? 16.514  -1.843  14.376  1.00 8.60  ? 96  HIS A CE1 1 
ATOM   788  N  NE2 . HIS A 1 96  ? 15.183  -1.528  14.625  1.00 7.95  ? 96  HIS A NE2 1 
ATOM   789  N  N   . TRP A 1 97  ? 14.775  -7.622  11.706  1.00 7.40  ? 97  TRP A N   1 
ATOM   790  C  CA  . TRP A 1 97  ? 14.356  -9.035  11.569  1.00 8.26  ? 97  TRP A CA  1 
ATOM   791  C  C   . TRP A 1 97  ? 15.465  -9.967  11.441  1.00 8.04  ? 97  TRP A C   1 
ATOM   792  O  O   . TRP A 1 97  ? 16.628  -9.568  11.350  1.00 9.38  ? 97  TRP A O   1 
ATOM   793  C  CB  . TRP A 1 97  ? 13.399  -9.203  10.368  1.00 8.68  ? 97  TRP A CB  1 
ATOM   794  C  CG  . TRP A 1 97  ? 14.060  -8.809  9.067   1.00 9.09  ? 97  TRP A CG  1 
ATOM   795  C  CD1 . TRP A 1 97  ? 14.713  -9.639  8.174   1.00 10.39 ? 97  TRP A CD1 1 
ATOM   796  C  CD2 . TRP A 1 97  ? 14.095  -7.493  8.501   1.00 9.84  ? 97  TRP A CD2 1 
ATOM   797  N  NE1 . TRP A 1 97  ? 15.127  -8.942  7.050   1.00 10.79 ? 97  TRP A NE1 1 
ATOM   798  C  CE2 . TRP A 1 97  ? 14.820  -7.605  7.237   1.00 9.80  ? 97  TRP A CE2 1 
ATOM   799  C  CE3 . TRP A 1 97  ? 13.597  -6.230  8.909   1.00 9.04  ? 97  TRP A CE3 1 
ATOM   800  C  CZ2 . TRP A 1 97  ? 15.052  -6.508  6.443   1.00 10.26 ? 97  TRP A CZ2 1 
ATOM   801  C  CZ3 . TRP A 1 97  ? 13.880  -5.099  8.107   1.00 10.04 ? 97  TRP A CZ3 1 
ATOM   802  C  CH2 . TRP A 1 97  ? 14.596  -5.236  6.914   1.00 9.66  ? 97  TRP A CH2 1 
ATOM   803  N  N   . GLY A 1 98  ? 15.127  -11.268 11.431  1.00 8.92  ? 98  GLY A N   1 
ATOM   804  C  CA  . GLY A 1 98  ? 16.166  -12.307 11.510  1.00 8.37  ? 98  GLY A CA  1 
ATOM   805  C  C   . GLY A 1 98  ? 16.438  -13.021 10.173  1.00 8.97  ? 98  GLY A C   1 
ATOM   806  O  O   . GLY A 1 98  ? 15.735  -12.790 9.168   1.00 8.27  ? 98  GLY A O   1 
ATOM   807  N  N   . SER A 1 99  ? 17.445  -13.871 10.196  1.00 9.76  ? 99  SER A N   1 
ATOM   808  C  CA  . SER A 1 99  ? 17.743  -14.770 9.042   1.00 10.94 ? 99  SER A CA  1 
ATOM   809  C  C   . SER A 1 99  ? 16.849  -16.006 9.135   1.00 12.62 ? 99  SER A C   1 
ATOM   810  O  O   . SER A 1 99  ? 16.711  -16.761 8.152   1.00 15.68 ? 99  SER A O   1 
ATOM   811  C  CB  . SER A 1 99  ? 19.229  -15.156 9.069   1.00 10.08 ? 99  SER A CB  1 
ATOM   812  O  OG  . SER A 1 99  ? 19.600  -15.752 10.302  1.00 12.02 ? 99  SER A OG  1 
ATOM   813  N  N   . LEU A 1 100 ? 16.275  -16.239 10.319  1.00 13.47 ? 100 LEU A N   1 
ATOM   814  C  CA  . LEU A 1 100 ? 15.411  -17.365 10.617  1.00 14.54 ? 100 LEU A CA  1 
ATOM   815  C  C   . LEU A 1 100 ? 14.277  -16.904 11.509  1.00 14.47 ? 100 LEU A C   1 
ATOM   816  O  O   . LEU A 1 100 ? 14.420  -15.903 12.231  1.00 13.20 ? 100 LEU A O   1 
ATOM   817  C  CB  . LEU A 1 100 ? 16.155  -18.408 11.472  1.00 16.63 ? 100 LEU A CB  1 
ATOM   818  C  CG  . LEU A 1 100 ? 17.482  -18.855 10.927  1.00 21.14 ? 100 LEU A CG  1 
ATOM   819  C  CD1 . LEU A 1 100 ? 18.260  -19.660 11.971  1.00 22.90 ? 100 LEU A CD1 1 
ATOM   820  C  CD2 . LEU A 1 100 ? 17.033  -19.722 9.739   1.00 22.96 ? 100 LEU A CD2 1 
ATOM   821  N  N   . ASP A 1 101 ? 13.178  -17.658 11.511  1.00 12.87 ? 101 ASP A N   1 
ATOM   822  C  CA  . ASP A 1 101 ? 12.048  -17.239 12.366  1.00 12.55 ? 101 ASP A CA  1 
ATOM   823  C  C   . ASP A 1 101 ? 12.349  -17.163 13.841  1.00 12.52 ? 101 ASP A C   1 
ATOM   824  O  O   . ASP A 1 101 ? 11.717  -16.396 14.565  1.00 11.70 ? 101 ASP A O   1 
ATOM   825  C  CB  . ASP A 1 101 ? 10.810  -18.126 12.142  1.00 12.85 ? 101 ASP A CB  1 
ATOM   826  C  CG  . ASP A 1 101 ? 10.291  -18.127 10.700  1.00 16.36 ? 101 ASP A CG  1 
ATOM   827  O  OD1 . ASP A 1 101 ? 10.703  -17.277 9.866   1.00 14.84 ? 101 ASP A OD1 1 
ATOM   828  O  OD2 . ASP A 1 101 ? 9.462   -19.026 10.390  1.00 18.17 ? 101 ASP A OD2 1 
ATOM   829  N  N   . GLY A 1 102 ? 13.349  -17.946 14.314  1.00 11.73 ? 102 GLY A N   1 
ATOM   830  C  CA  . GLY A 1 102 ? 13.687  -17.999 15.746  1.00 10.27 ? 102 GLY A CA  1 
ATOM   831  C  C   . GLY A 1 102 ? 14.400  -16.784 16.308  1.00 8.94  ? 102 GLY A C   1 
ATOM   832  O  O   . GLY A 1 102 ? 14.729  -16.742 17.493  1.00 10.20 ? 102 GLY A O   1 
ATOM   833  N  N   A GLN A 1 103 ? 14.711  -15.803 15.459  0.50 9.13  ? 103 GLN A N   1 
ATOM   834  N  N   B GLN A 1 103 ? 14.620  -15.756 15.492  0.50 9.21  ? 103 GLN A N   1 
ATOM   835  C  CA  A GLN A 1 103 ? 15.372  -14.593 15.957  0.50 8.45  ? 103 GLN A CA  1 
ATOM   836  C  CA  B GLN A 1 103 ? 15.309  -14.576 16.009  0.50 8.55  ? 103 GLN A CA  1 
ATOM   837  C  C   A GLN A 1 103 ? 14.975  -13.424 15.112  0.50 8.14  ? 103 GLN A C   1 
ATOM   838  C  C   B GLN A 1 103 ? 15.095  -13.436 15.080  0.50 8.18  ? 103 GLN A C   1 
ATOM   839  O  O   A GLN A 1 103 ? 14.301  -13.586 14.104  0.50 7.84  ? 103 GLN A O   1 
ATOM   840  O  O   B GLN A 1 103 ? 14.740  -13.632 13.947  0.50 7.85  ? 103 GLN A O   1 
ATOM   841  C  CB  A GLN A 1 103 ? 16.905  -14.760 16.013  0.50 8.74  ? 103 GLN A CB  1 
ATOM   842  C  CB  B GLN A 1 103 ? 16.802  -14.842 16.090  0.50 9.00  ? 103 GLN A CB  1 
ATOM   843  C  CG  A GLN A 1 103 ? 17.650  -14.792 14.666  0.50 8.96  ? 103 GLN A CG  1 
ATOM   844  C  CG  B GLN A 1 103 ? 17.412  -15.204 14.741  0.50 9.55  ? 103 GLN A CG  1 
ATOM   845  C  CD  A GLN A 1 103 ? 18.973  -15.555 14.729  0.50 9.54  ? 103 GLN A CD  1 
ATOM   846  C  CD  B GLN A 1 103 ? 18.904  -15.413 14.845  0.50 10.20 ? 103 GLN A CD  1 
ATOM   847  O  OE1 A GLN A 1 103 ? 19.006  -16.713 15.169  0.50 9.53  ? 103 GLN A OE1 1 
ATOM   848  O  OE1 B GLN A 1 103 ? 19.422  -15.762 15.940  0.50 10.84 ? 103 GLN A OE1 1 
ATOM   849  N  NE2 A GLN A 1 103 ? 20.084  -14.918 14.266  0.50 9.41  ? 103 GLN A NE2 1 
ATOM   850  N  NE2 B GLN A 1 103 ? 19.629  -15.233 13.697  0.50 10.11 ? 103 GLN A NE2 1 
ATOM   851  N  N   . GLY A 1 104 ? 15.333  -12.234 15.568  1.00 7.96  ? 104 GLY A N   1 
ATOM   852  C  CA  . GLY A 1 104 ? 15.002  -11.036 14.769  1.00 7.61  ? 104 GLY A CA  1 
ATOM   853  C  C   . GLY A 1 104 ? 14.635  -9.851  15.610  1.00 8.22  ? 104 GLY A C   1 
ATOM   854  O  O   . GLY A 1 104 ? 14.878  -8.682  15.194  1.00 8.85  ? 104 GLY A O   1 
ATOM   855  N  N   . SER A 1 105 ? 13.932  -10.107 16.721  1.00 7.84  ? 105 SER A N   1 
ATOM   856  C  CA  . SER A 1 105 ? 13.527  -8.944  17.558  1.00 7.22  ? 105 SER A CA  1 
ATOM   857  C  C   . SER A 1 105 ? 14.719  -8.376  18.349  1.00 6.91  ? 105 SER A C   1 
ATOM   858  O  O   . SER A 1 105 ? 15.757  -9.037  18.512  1.00 7.46  ? 105 SER A O   1 
ATOM   859  C  CB  . SER A 1 105 ? 12.369  -9.303  18.452  1.00 7.15  ? 105 SER A CB  1 
ATOM   860  O  OG  . SER A 1 105 ? 12.789  -10.224 19.458  1.00 7.78  ? 105 SER A OG  1 
ATOM   861  N  N   . GLU A 1 106 ? 14.596  -7.102  18.717  1.00 6.60  ? 106 GLU A N   1 
ATOM   862  C  CA  . GLU A 1 106 ? 15.614  -6.410  19.510  1.00 7.10  ? 106 GLU A CA  1 
ATOM   863  C  C   . GLU A 1 106 ? 15.270  -6.604  21.004  1.00 7.12  ? 106 GLU A C   1 
ATOM   864  O  O   . GLU A 1 106 ? 16.063  -7.203  21.754  1.00 6.39  ? 106 GLU A O   1 
ATOM   865  C  CB  . GLU A 1 106 ? 15.722  -4.917  19.159  1.00 7.37  ? 106 GLU A CB  1 
ATOM   866  C  CG  . GLU A 1 106 ? 16.033  -4.767  17.643  1.00 8.49  ? 106 GLU A CG  1 
ATOM   867  C  CD  . GLU A 1 106 ? 16.770  -3.528  17.387  1.00 9.01  ? 106 GLU A CD  1 
ATOM   868  O  OE1 . GLU A 1 106 ? 16.160  -2.441  17.549  1.00 8.32  ? 106 GLU A OE1 1 
ATOM   869  O  OE2 . GLU A 1 106 ? 17.982  -3.656  17.033  1.00 9.66  ? 106 GLU A OE2 1 
ATOM   870  N  N   . HIS A 1 107 ? 14.033  -6.261  21.401  1.00 6.91  ? 107 HIS A N   1 
ATOM   871  C  CA  . HIS A 1 107 ? 13.626  -6.569  22.750  1.00 6.66  ? 107 HIS A CA  1 
ATOM   872  C  C   . HIS A 1 107 ? 13.325  -8.013  22.783  1.00 6.84  ? 107 HIS A C   1 
ATOM   873  O  O   . HIS A 1 107 ? 13.029  -8.624  21.728  1.00 6.93  ? 107 HIS A O   1 
ATOM   874  C  CB  . HIS A 1 107 ? 12.421  -5.757  23.135  1.00 6.38  ? 107 HIS A CB  1 
ATOM   875  C  CG  . HIS A 1 107 ? 12.760  -4.296  23.277  1.00 6.79  ? 107 HIS A CG  1 
ATOM   876  N  ND1 . HIS A 1 107 ? 12.689  -3.423  22.239  1.00 6.72  ? 107 HIS A ND1 1 
ATOM   877  C  CD2 . HIS A 1 107 ? 13.193  -3.572  24.391  1.00 6.29  ? 107 HIS A CD2 1 
ATOM   878  C  CE1 . HIS A 1 107 ? 13.116  -2.197  22.644  1.00 6.34  ? 107 HIS A CE1 1 
ATOM   879  N  NE2 . HIS A 1 107 ? 13.371  -2.278  23.972  1.00 6.66  ? 107 HIS A NE2 1 
ATOM   880  N  N   . THR A 1 108 ? 13.484  -8.576  23.963  1.00 7.22  ? 108 THR A N   1 
ATOM   881  C  CA  . THR A 1 108 ? 13.122  -9.996  24.220  1.00 7.57  ? 108 THR A CA  1 
ATOM   882  C  C   . THR A 1 108 ? 12.168  -10.014 25.407  1.00 8.52  ? 108 THR A C   1 
ATOM   883  O  O   . THR A 1 108 ? 12.129  -9.032  26.161  1.00 9.50  ? 108 THR A O   1 
ATOM   884  C  CB  . THR A 1 108 ? 14.350  -10.904 24.448  1.00 7.60  ? 108 THR A CB  1 
ATOM   885  O  OG1 . THR A 1 108 ? 15.143  -10.390 25.538  1.00 8.34  ? 108 THR A OG1 1 
ATOM   886  C  CG2 . THR A 1 108 ? 15.203  -10.993 23.098  1.00 7.16  ? 108 THR A CG2 1 
ATOM   887  N  N   . VAL A 1 109 ? 11.399  -11.093 25.557  1.00 8.81  ? 109 VAL A N   1 
ATOM   888  C  CA  . VAL A 1 109 ? 10.376  -11.178 26.683  1.00 8.30  ? 109 VAL A CA  1 
ATOM   889  C  C   . VAL A 1 109 ? 10.690  -12.505 27.424  1.00 8.48  ? 109 VAL A C   1 
ATOM   890  O  O   . VAL A 1 109 ? 10.517  -13.568 26.844  1.00 7.82  ? 109 VAL A O   1 
ATOM   891  C  CB  . VAL A 1 109 ? 8.970   -11.176 26.096  1.00 9.43  ? 109 VAL A CB  1 
ATOM   892  C  CG1 . VAL A 1 109 ? 7.936   -11.282 27.212  1.00 9.00  ? 109 VAL A CG1 1 
ATOM   893  C  CG2 . VAL A 1 109 ? 8.722   -9.881  25.318  1.00 8.76  ? 109 VAL A CG2 1 
ATOM   894  N  N   . ASP A 1 110 ? 11.227  -12.392 28.645  1.00 8.69  ? 110 ASP A N   1 
ATOM   895  C  CA  . ASP A 1 110 ? 11.767  -13.572 29.343  1.00 10.43 ? 110 ASP A CA  1 
ATOM   896  C  C   . ASP A 1 110 ? 12.661  -14.414 28.450  1.00 9.64  ? 110 ASP A C   1 
ATOM   897  O  O   . ASP A 1 110 ? 12.527  -15.682 28.378  1.00 10.10 ? 110 ASP A O   1 
ATOM   898  C  CB  . ASP A 1 110 ? 10.623  -14.398 29.949  1.00 11.85 ? 110 ASP A CB  1 
ATOM   899  C  CG  . ASP A 1 110 ? 9.772   -13.583 30.899  1.00 11.89 ? 110 ASP A CG  1 
ATOM   900  O  OD1 . ASP A 1 110 ? 10.319  -12.747 31.585  1.00 13.15 ? 110 ASP A OD1 1 
ATOM   901  O  OD2 . ASP A 1 110 ? 8.612   -13.872 31.001  1.00 15.04 ? 110 ASP A OD2 1 
ATOM   902  N  N   . LYS A 1 111 ? 13.599  -13.693 27.801  1.00 9.64  ? 111 LYS A N   1 
ATOM   903  C  CA  . LYS A 1 111 ? 14.618  -14.196 26.851  1.00 9.87  ? 111 LYS A CA  1 
ATOM   904  C  C   . LYS A 1 111 ? 14.030  -14.719 25.522  1.00 9.79  ? 111 LYS A C   1 
ATOM   905  O  O   . LYS A 1 111 ? 14.786  -15.116 24.647  1.00 10.17 ? 111 LYS A O   1 
ATOM   906  C  CB  . LYS A 1 111 ? 15.596  -15.217 27.508  1.00 12.13 ? 111 LYS A CB  1 
ATOM   907  C  CG  . LYS A 1 111 ? 16.301  -14.631 28.736  1.00 13.42 ? 111 LYS A CG  1 
ATOM   908  C  CD  . LYS A 1 111 ? 17.272  -13.509 28.303  1.00 16.93 ? 111 LYS A CD  1 
ATOM   909  C  CE  . LYS A 1 111 ? 18.014  -13.019 29.550  1.00 19.22 ? 111 LYS A CE  1 
ATOM   910  N  NZ  . LYS A 1 111 ? 19.164  -13.944 29.781  1.00 21.19 ? 111 LYS A NZ  1 
ATOM   911  N  N   . LYS A 1 112 ? 12.711  -14.656 25.342  1.00 8.52  ? 112 LYS A N   1 
ATOM   912  C  CA  . LYS A 1 112 ? 12.133  -15.080 24.088  1.00 9.46  ? 112 LYS A CA  1 
ATOM   913  C  C   . LYS A 1 112 ? 12.420  -14.014 22.961  1.00 9.63  ? 112 LYS A C   1 
ATOM   914  O  O   . LYS A 1 112 ? 12.205  -12.822 23.148  1.00 8.92  ? 112 LYS A O   1 
ATOM   915  C  CB  . LYS A 1 112 ? 10.598  -15.287 24.225  1.00 10.66 ? 112 LYS A CB  1 
ATOM   916  C  CG  . LYS A 1 112 ? 9.952   -15.551 22.845  1.00 10.39 ? 112 LYS A CG  1 
ATOM   917  C  CD  . LYS A 1 112 ? 8.429   -15.612 23.024  1.00 12.75 ? 112 LYS A CD  1 
ATOM   918  C  CE  . LYS A 1 112 ? 7.732   -15.661 21.647  1.00 12.47 ? 112 LYS A CE  1 
ATOM   919  N  NZ  . LYS A 1 112 ? 7.869   -16.973 21.005  1.00 13.11 ? 112 LYS A NZ  1 
ATOM   920  N  N   . LYS A 1 113 ? 12.956  -14.510 21.830  1.00 9.21  ? 113 LYS A N   1 
ATOM   921  C  CA  . LYS A 1 113 ? 13.173  -13.695 20.616  1.00 9.53  ? 113 LYS A CA  1 
ATOM   922  C  C   . LYS A 1 113 ? 12.028  -13.877 19.643  1.00 8.25  ? 113 LYS A C   1 
ATOM   923  O  O   . LYS A 1 113 ? 11.651  -15.007 19.359  1.00 9.33  ? 113 LYS A O   1 
ATOM   924  C  CB  . LYS A 1 113 ? 14.476  -14.135 19.892  1.00 9.47  ? 113 LYS A CB  1 
ATOM   925  C  CG  . LYS A 1 113 ? 15.689  -13.747 20.650  1.00 10.92 ? 113 LYS A CG  1 
ATOM   926  C  CD  . LYS A 1 113 ? 16.857  -14.499 20.025  1.00 12.14 ? 113 LYS A CD  1 
ATOM   927  C  CE  . LYS A 1 113 ? 18.151  -13.893 20.569  1.00 14.62 ? 113 LYS A CE  1 
ATOM   928  N  NZ  . LYS A 1 113 ? 18.539  -14.622 21.782  1.00 18.10 ? 113 LYS A NZ  1 
ATOM   929  N  N   . TYR A 1 114 ? 11.436  -12.789 19.155  1.00 7.68  ? 114 TYR A N   1 
ATOM   930  C  CA  . TYR A 1 114 ? 10.435  -12.875 18.107  1.00 7.57  ? 114 TYR A CA  1 
ATOM   931  C  C   . TYR A 1 114 ? 11.066  -12.803 16.738  1.00 7.68  ? 114 TYR A C   1 
ATOM   932  O  O   . TYR A 1 114 ? 12.283  -12.535 16.639  1.00 7.66  ? 114 TYR A O   1 
ATOM   933  C  CB  . TYR A 1 114 ? 9.404   -11.744 18.255  1.00 7.39  ? 114 TYR A CB  1 
ATOM   934  C  CG  . TYR A 1 114 ? 8.414   -12.020 19.399  1.00 8.68  ? 114 TYR A CG  1 
ATOM   935  C  CD1 . TYR A 1 114 ? 8.668   -11.585 20.707  1.00 8.67  ? 114 TYR A CD1 1 
ATOM   936  C  CD2 . TYR A 1 114 ? 7.214   -12.652 19.135  1.00 9.31  ? 114 TYR A CD2 1 
ATOM   937  C  CE1 . TYR A 1 114 ? 7.786   -11.818 21.745  1.00 10.29 ? 114 TYR A CE1 1 
ATOM   938  C  CE2 . TYR A 1 114 ? 6.278   -12.846 20.173  1.00 10.95 ? 114 TYR A CE2 1 
ATOM   939  C  CZ  . TYR A 1 114 ? 6.598   -12.444 21.485  1.00 11.32 ? 114 TYR A CZ  1 
ATOM   940  O  OH  . TYR A 1 114 ? 5.733   -12.545 22.570  1.00 13.87 ? 114 TYR A OH  1 
ATOM   941  N  N   . ALA A 1 115 ? 10.306  -13.177 15.703  1.00 7.93  ? 115 ALA A N   1 
ATOM   942  C  CA  . ALA A 1 115 ? 10.841  -13.170 14.302  1.00 8.04  ? 115 ALA A CA  1 
ATOM   943  C  C   . ALA A 1 115 ? 11.223  -11.776 13.817  1.00 7.83  ? 115 ALA A C   1 
ATOM   944  O  O   . ALA A 1 115 ? 12.126  -11.657 12.971  1.00 7.82  ? 115 ALA A O   1 
ATOM   945  C  CB  . ALA A 1 115 ? 9.793   -13.797 13.353  1.00 8.39  ? 115 ALA A CB  1 
ATOM   946  N  N   . ALA A 1 116 ? 10.552  -10.732 14.338  1.00 7.63  ? 116 ALA A N   1 
ATOM   947  C  CA  . ALA A 1 116 ? 10.930  -9.384  13.941  1.00 7.11  ? 116 ALA A CA  1 
ATOM   948  C  C   . ALA A 1 116 ? 10.382  -8.377  14.950  1.00 7.40  ? 116 ALA A C   1 
ATOM   949  O  O   . ALA A 1 116 ? 9.663   -8.771  15.874  1.00 7.78  ? 116 ALA A O   1 
ATOM   950  C  CB  . ALA A 1 116 ? 10.363  -9.100  12.530  1.00 7.34  ? 116 ALA A CB  1 
ATOM   951  N  N   . GLU A 1 117 ? 10.639  -7.086  14.746  1.00 7.17  ? 117 GLU A N   1 
ATOM   952  C  CA  . GLU A 1 117 ? 10.069  -6.072  15.664  1.00 7.09  ? 117 GLU A CA  1 
ATOM   953  C  C   . GLU A 1 117 ? 9.911   -4.824  14.838  1.00 7.21  ? 117 GLU A C   1 
ATOM   954  O  O   . GLU A 1 117 ? 10.833  -4.430  14.119  1.00 7.40  ? 117 GLU A O   1 
ATOM   955  C  CB  . GLU A 1 117 ? 11.045  -5.805  16.815  1.00 7.84  ? 117 GLU A CB  1 
ATOM   956  C  CG  . GLU A 1 117 ? 10.539  -4.833  17.898  1.00 7.65  ? 117 GLU A CG  1 
ATOM   957  C  CD  . GLU A 1 117 ? 11.495  -4.799  19.097  1.00 8.68  ? 117 GLU A CD  1 
ATOM   958  O  OE1 . GLU A 1 117 ? 12.108  -5.845  19.451  1.00 8.33  ? 117 GLU A OE1 1 
ATOM   959  O  OE2 . GLU A 1 117 ? 11.598  -3.732  19.771  1.00 10.48 ? 117 GLU A OE2 1 
ATOM   960  N  N   . LEU A 1 118 ? 8.736   -4.265  14.914  1.00 6.90  ? 118 LEU A N   1 
ATOM   961  C  CA  . LEU A 1 118 ? 8.366   -3.014  14.229  1.00 6.46  ? 118 LEU A CA  1 
ATOM   962  C  C   . LEU A 1 118 ? 8.628   -1.856  15.221  1.00 6.43  ? 118 LEU A C   1 
ATOM   963  O  O   . LEU A 1 118 ? 8.202   -1.941  16.380  1.00 6.37  ? 118 LEU A O   1 
ATOM   964  C  CB  . LEU A 1 118 ? 6.874   -3.062  13.889  1.00 6.83  ? 118 LEU A CB  1 
ATOM   965  C  CG  . LEU A 1 118 ? 6.088   -1.733  13.571  1.00 6.93  ? 118 LEU A CG  1 
ATOM   966  C  CD1 . LEU A 1 118 ? 6.694   -1.177  12.313  1.00 7.95  ? 118 LEU A CD1 1 
ATOM   967  C  CD2 . LEU A 1 118 ? 4.582   -2.153  13.355  1.00 7.21  ? 118 LEU A CD2 1 
ATOM   968  N  N   . HIS A 1 119 ? 9.223   -0.764  14.710  1.00 6.07  ? 119 HIS A N   1 
ATOM   969  C  CA  . HIS A 1 119 ? 9.444   0.420   15.534  1.00 6.43  ? 119 HIS A CA  1 
ATOM   970  C  C   . HIS A 1 119 ? 8.752   1.570   14.877  1.00 6.68  ? 119 HIS A C   1 
ATOM   971  O  O   . HIS A 1 119 ? 9.099   1.911   13.727  1.00 7.57  ? 119 HIS A O   1 
ATOM   972  C  CB  . HIS A 1 119 ? 10.939  0.700   15.616  1.00 6.25  ? 119 HIS A CB  1 
ATOM   973  C  CG  . HIS A 1 119 ? 11.644  -0.278  16.558  1.00 6.20  ? 119 HIS A CG  1 
ATOM   974  N  ND1 . HIS A 1 119 ? 12.956  -0.528  16.514  1.00 6.10  ? 119 HIS A ND1 1 
ATOM   975  C  CD2 . HIS A 1 119 ? 11.121  -1.077  17.545  1.00 6.37  ? 119 HIS A CD2 1 
ATOM   976  C  CE1 . HIS A 1 119 ? 13.276  -1.438  17.479  1.00 6.30  ? 119 HIS A CE1 1 
ATOM   977  N  NE2 . HIS A 1 119 ? 12.146  -1.789  18.093  1.00 6.13  ? 119 HIS A NE2 1 
ATOM   978  N  N   . LEU A 1 120 ? 7.761   2.154   15.564  1.00 7.24  ? 120 LEU A N   1 
ATOM   979  C  CA  . LEU A 1 120 ? 7.083   3.386   15.061  1.00 7.33  ? 120 LEU A CA  1 
ATOM   980  C  C   . LEU A 1 120 ? 7.670   4.540   15.856  1.00 7.62  ? 120 LEU A C   1 
ATOM   981  O  O   . LEU A 1 120 ? 7.534   4.561   17.103  1.00 6.83  ? 120 LEU A O   1 
ATOM   982  C  CB  . LEU A 1 120 ? 5.617   3.312   15.291  1.00 7.96  ? 120 LEU A CB  1 
ATOM   983  C  CG  . LEU A 1 120 ? 4.923   2.228   14.408  1.00 8.32  ? 120 LEU A CG  1 
ATOM   984  C  CD1 . LEU A 1 120 ? 4.073   1.314   15.268  1.00 10.06 ? 120 LEU A CD1 1 
ATOM   985  C  CD2 . LEU A 1 120 ? 4.082   2.854   13.271  1.00 9.44  ? 120 LEU A CD2 1 
ATOM   986  N  N   . VAL A 1 121 ? 8.336   5.444   15.128  1.00 7.49  ? 121 VAL A N   1 
ATOM   987  C  CA  . VAL A 1 121 ? 9.256   6.381   15.826  1.00 7.69  ? 121 VAL A CA  1 
ATOM   988  C  C   . VAL A 1 121 ? 8.566   7.729   15.908  1.00 7.91  ? 121 VAL A C   1 
ATOM   989  O  O   . VAL A 1 121 ? 8.112   8.215   14.882  1.00 7.30  ? 121 VAL A O   1 
ATOM   990  C  CB  . VAL A 1 121 ? 10.577  6.505   15.029  1.00 7.79  ? 121 VAL A CB  1 
ATOM   991  C  CG1 . VAL A 1 121 ? 11.527  7.584   15.630  1.00 7.75  ? 121 VAL A CG1 1 
ATOM   992  C  CG2 . VAL A 1 121 ? 11.268  5.146   14.816  1.00 7.57  ? 121 VAL A CG2 1 
ATOM   993  N  N   . HIS A 1 122 ? 8.489   8.363   17.098  1.00 7.33  ? 122 HIS A N   1 
ATOM   994  C  CA  . HIS A 1 122 ? 7.812   9.643   17.227  1.00 7.73  ? 122 HIS A CA  1 
ATOM   995  C  C   . HIS A 1 122 ? 8.665   10.617  17.977  1.00 7.85  ? 122 HIS A C   1 
ATOM   996  O  O   . HIS A 1 122 ? 9.460   10.209  18.854  1.00 7.42  ? 122 HIS A O   1 
ATOM   997  C  CB  . HIS A 1 122 ? 6.458   9.490   18.018  1.00 8.21  ? 122 HIS A CB  1 
ATOM   998  C  CG  . HIS A 1 122 ? 5.604   8.303   17.612  1.00 8.18  ? 122 HIS A CG  1 
ATOM   999  N  ND1 . HIS A 1 122 ? 5.956   7.027   17.862  1.00 8.46  ? 122 HIS A ND1 1 
ATOM   1000 C  CD2 . HIS A 1 122 ? 4.348   8.251   17.008  1.00 8.65  ? 122 HIS A CD2 1 
ATOM   1001 C  CE1 . HIS A 1 122 ? 4.988   6.199   17.414  1.00 9.11  ? 122 HIS A CE1 1 
ATOM   1002 N  NE2 . HIS A 1 122 ? 4.006   6.951   16.894  1.00 8.28  ? 122 HIS A NE2 1 
ATOM   1003 N  N   . TRP A 1 123 ? 8.553   11.915  17.657  1.00 8.00  ? 123 TRP A N   1 
ATOM   1004 C  CA  . TRP A 1 123 ? 9.389   12.905  18.343  1.00 8.91  ? 123 TRP A CA  1 
ATOM   1005 C  C   . TRP A 1 123 ? 8.541   13.886  19.099  1.00 9.43  ? 123 TRP A C   1 
ATOM   1006 O  O   . TRP A 1 123 ? 7.446   14.247  18.693  1.00 8.99  ? 123 TRP A O   1 
ATOM   1007 C  CB  . TRP A 1 123 ? 10.367  13.620  17.361  1.00 9.49  ? 123 TRP A CB  1 
ATOM   1008 C  CG  . TRP A 1 123 ? 9.687   14.264  16.163  1.00 10.34 ? 123 TRP A CG  1 
ATOM   1009 C  CD1 . TRP A 1 123 ? 9.437   13.692  14.915  1.00 10.29 ? 123 TRP A CD1 1 
ATOM   1010 C  CD2 . TRP A 1 123 ? 9.150   15.639  16.058  1.00 11.08 ? 123 TRP A CD2 1 
ATOM   1011 N  NE1 . TRP A 1 123 ? 8.804   14.580  14.082  1.00 10.45 ? 123 TRP A NE1 1 
ATOM   1012 C  CE2 . TRP A 1 123 ? 8.604   15.764  14.704  1.00 10.40 ? 123 TRP A CE2 1 
ATOM   1013 C  CE3 . TRP A 1 123 ? 9.073   16.725  16.917  1.00 11.09 ? 123 TRP A CE3 1 
ATOM   1014 C  CZ2 . TRP A 1 123 ? 8.010   16.936  14.258  1.00 10.99 ? 123 TRP A CZ2 1 
ATOM   1015 C  CZ3 . TRP A 1 123 ? 8.473   17.901  16.453  1.00 10.71 ? 123 TRP A CZ3 1 
ATOM   1016 C  CH2 . TRP A 1 123 ? 7.955   18.000  15.156  1.00 10.45 ? 123 TRP A CH2 1 
ATOM   1017 N  N   . ASN A 1 124 ? 9.069   14.317  20.229  1.00 10.19 ? 124 ASN A N   1 
ATOM   1018 C  CA  . ASN A 1 124 ? 8.402   15.199  21.175  1.00 10.02 ? 124 ASN A CA  1 
ATOM   1019 C  C   . ASN A 1 124 ? 8.207   16.610  20.583  1.00 11.20 ? 124 ASN A C   1 
ATOM   1020 O  O   . ASN A 1 124 ? 9.179   17.243  20.241  1.00 8.88  ? 124 ASN A O   1 
ATOM   1021 C  CB  . ASN A 1 124 ? 9.217   15.238  22.485  1.00 11.00 ? 124 ASN A CB  1 
ATOM   1022 C  CG  . ASN A 1 124 ? 8.411   15.835  23.629  1.00 11.94 ? 124 ASN A CG  1 
ATOM   1023 O  OD1 . ASN A 1 124 ? 7.600   16.715  23.398  1.00 11.53 ? 124 ASN A OD1 1 
ATOM   1024 N  ND2 . ASN A 1 124 ? 8.582   15.319  24.846  1.00 12.55 ? 124 ASN A ND2 1 
ATOM   1025 N  N   . THR A 1 125 ? 6.941   17.032  20.426  1.00 11.89 ? 125 THR A N   1 
ATOM   1026 C  CA  . THR A 1 125 ? 6.665   18.266  19.625  1.00 13.21 ? 125 THR A CA  1 
ATOM   1027 C  C   . THR A 1 125 ? 7.119   19.459  20.443  1.00 12.71 ? 125 THR A C   1 
ATOM   1028 O  O   . THR A 1 125 ? 7.343   20.530  19.849  1.00 12.12 ? 125 THR A O   1 
ATOM   1029 C  CB  . THR A 1 125 ? 5.157   18.436  19.304  1.00 14.10 ? 125 THR A CB  1 
ATOM   1030 O  OG1 . THR A 1 125 ? 4.410   18.408  20.501  1.00 16.05 ? 125 THR A OG1 1 
ATOM   1031 C  CG2 . THR A 1 125 ? 4.625   17.256  18.402  1.00 13.97 ? 125 THR A CG2 1 
ATOM   1032 N  N   . LYS A 1 126 ? 7.530   19.325  21.766  1.00 12.39 ? 127 LYS A N   1 
ATOM   1033 C  CA  . LYS A 1 126 ? 8.097   20.478  22.457  1.00 12.92 ? 127 LYS A CA  1 
ATOM   1034 C  C   . LYS A 1 126 ? 9.494   20.843  21.980  1.00 11.13 ? 127 LYS A C   1 
ATOM   1035 O  O   . LYS A 1 126 ? 9.963   21.924  22.297  1.00 10.22 ? 127 LYS A O   1 
ATOM   1036 C  CB  . LYS A 1 126 ? 8.047   20.265  23.963  1.00 17.09 ? 127 LYS A CB  1 
ATOM   1037 C  CG  . LYS A 1 126 ? 9.119   19.361  24.478  1.00 19.23 ? 127 LYS A CG  1 
ATOM   1038 C  CD  . LYS A 1 126 ? 8.849   18.928  25.914  1.00 24.57 ? 127 LYS A CD  1 
ATOM   1039 C  CE  . LYS A 1 126 ? 9.718   19.714  26.860  1.00 29.78 ? 127 LYS A CE  1 
ATOM   1040 N  NZ  . LYS A 1 126 ? 9.835   18.952  28.135  1.00 35.82 ? 127 LYS A NZ  1 
ATOM   1041 N  N   . TYR A 1 127 ? 10.152  19.983  21.217  1.00 10.21 ? 128 TYR A N   1 
ATOM   1042 C  CA  . TYR A 1 127 ? 11.487  20.239  20.651  1.00 9.67  ? 128 TYR A CA  1 
ATOM   1043 C  C   . TYR A 1 127 ? 11.501  20.645  19.173  1.00 11.74 ? 128 TYR A C   1 
ATOM   1044 O  O   . TYR A 1 127 ? 12.563  20.882  18.585  1.00 11.46 ? 128 TYR A O   1 
ATOM   1045 C  CB  . TYR A 1 127 ? 12.392  19.032  20.913  1.00 11.06 ? 128 TYR A CB  1 
ATOM   1046 C  CG  . TYR A 1 127 ? 12.493  18.769  22.394  1.00 10.07 ? 128 TYR A CG  1 
ATOM   1047 C  CD1 . TYR A 1 127 ? 12.910  19.774  23.288  1.00 10.93 ? 128 TYR A CD1 1 
ATOM   1048 C  CD2 . TYR A 1 127 ? 12.241  17.519  22.907  1.00 10.19 ? 128 TYR A CD2 1 
ATOM   1049 C  CE1 . TYR A 1 127 ? 13.016  19.508  24.651  1.00 10.09 ? 128 TYR A CE1 1 
ATOM   1050 C  CE2 . TYR A 1 127 ? 12.320  17.249  24.253  1.00 10.26 ? 128 TYR A CE2 1 
ATOM   1051 C  CZ  . TYR A 1 127 ? 12.730  18.269  25.122  1.00 10.69 ? 128 TYR A CZ  1 
ATOM   1052 O  OH  . TYR A 1 127 ? 12.806  17.917  26.461  1.00 11.10 ? 128 TYR A OH  1 
ATOM   1053 N  N   . GLY A 1 128 ? 10.316  20.737  18.566  1.00 10.39 ? 129 GLY A N   1 
ATOM   1054 C  CA  . GLY A 1 128 ? 10.204  21.450  17.299  1.00 12.47 ? 129 GLY A CA  1 
ATOM   1055 C  C   . GLY A 1 128 ? 10.557  20.571  16.087  1.00 13.44 ? 129 GLY A C   1 
ATOM   1056 O  O   . GLY A 1 128 ? 9.909   20.693  15.051  1.00 15.57 ? 129 GLY A O   1 
ATOM   1057 N  N   . ASP A 1 129 ? 11.541  19.686  16.191  1.00 13.01 ? 130 ASP A N   1 
ATOM   1058 C  CA  . ASP A 1 129 ? 11.798  18.770  15.103  1.00 13.22 ? 130 ASP A CA  1 
ATOM   1059 C  C   . ASP A 1 129 ? 12.526  17.556  15.616  1.00 14.06 ? 130 ASP A C   1 
ATOM   1060 O  O   . ASP A 1 129 ? 13.005  17.527  16.749  1.00 12.30 ? 130 ASP A O   1 
ATOM   1061 C  CB  . ASP A 1 129 ? 12.458  19.422  13.870  1.00 15.12 ? 130 ASP A CB  1 
ATOM   1062 C  CG  . ASP A 1 129 ? 13.924  19.806  14.080  1.00 16.89 ? 130 ASP A CG  1 
ATOM   1063 O  OD1 . ASP A 1 129 ? 14.572  19.354  15.051  1.00 21.66 ? 130 ASP A OD1 1 
ATOM   1064 O  OD2 . ASP A 1 129 ? 14.436  20.574  13.237  1.00 18.54 ? 130 ASP A OD2 1 
ATOM   1065 N  N   . PHE A 1 130 ? 12.653  16.562  14.738  1.00 11.85 ? 131 PHE A N   1 
ATOM   1066 C  CA  . PHE A 1 130 ? 13.342  15.344  15.087  1.00 12.82 ? 131 PHE A CA  1 
ATOM   1067 C  C   . PHE A 1 130 ? 14.797  15.563  15.502  1.00 12.49 ? 131 PHE A C   1 
ATOM   1068 O  O   . PHE A 1 130 ? 15.264  14.987  16.477  1.00 11.64 ? 131 PHE A O   1 
ATOM   1069 C  CB  . PHE A 1 130 ? 13.277  14.339  13.898  1.00 11.88 ? 131 PHE A CB  1 
ATOM   1070 C  CG  . PHE A 1 130 ? 13.953  13.034  14.170  1.00 12.02 ? 131 PHE A CG  1 
ATOM   1071 C  CD1 . PHE A 1 130 ? 13.242  12.029  14.863  1.00 11.28 ? 131 PHE A CD1 1 
ATOM   1072 C  CD2 . PHE A 1 130 ? 15.270  12.786  13.791  1.00 12.91 ? 131 PHE A CD2 1 
ATOM   1073 C  CE1 . PHE A 1 130 ? 13.840  10.812  15.188  1.00 12.17 ? 131 PHE A CE1 1 
ATOM   1074 C  CE2 . PHE A 1 130 ? 15.879  11.537  14.050  1.00 13.09 ? 131 PHE A CE2 1 
ATOM   1075 C  CZ  . PHE A 1 130 ? 15.157  10.544  14.763  1.00 13.16 ? 131 PHE A CZ  1 
ATOM   1076 N  N   . GLY A 1 131 ? 15.550  16.335  14.702  1.00 11.24 ? 132 GLY A N   1 
ATOM   1077 C  CA  . GLY A 1 131 ? 16.979  16.485  14.971  1.00 12.11 ? 132 GLY A CA  1 
ATOM   1078 C  C   . GLY A 1 131 ? 17.253  17.117  16.310  1.00 12.72 ? 132 GLY A C   1 
ATOM   1079 O  O   . GLY A 1 131 ? 18.271  16.777  16.923  1.00 13.74 ? 132 GLY A O   1 
ATOM   1080 N  N   . LYS A 1 132 ? 16.412  18.051  16.744  1.00 11.55 ? 133 LYS A N   1 
ATOM   1081 C  CA  . LYS A 1 132 ? 16.589  18.642  18.094  1.00 12.18 ? 133 LYS A CA  1 
ATOM   1082 C  C   . LYS A 1 132 ? 16.099  17.668  19.223  1.00 11.80 ? 133 LYS A C   1 
ATOM   1083 O  O   . LYS A 1 132 ? 16.683  17.603  20.327  1.00 10.63 ? 133 LYS A O   1 
ATOM   1084 C  CB  . LYS A 1 132 ? 15.831  19.962  18.216  1.00 14.11 ? 133 LYS A CB  1 
ATOM   1085 C  CG  . LYS A 1 132 ? 16.318  21.104  17.339  1.00 18.82 ? 133 LYS A CG  1 
ATOM   1086 C  CD  . LYS A 1 132 ? 17.820  21.251  17.264  1.00 23.84 ? 133 LYS A CD  1 
ATOM   1087 C  CE  . LYS A 1 132 ? 18.343  21.775  18.592  1.00 30.45 ? 133 LYS A CE  1 
ATOM   1088 N  NZ  . LYS A 1 132 ? 19.597  22.617  18.459  1.00 40.77 ? 133 LYS A NZ  1 
ATOM   1089 N  N   . ALA A 1 133 ? 15.058  16.909  18.906  1.00 10.85 ? 134 ALA A N   1 
ATOM   1090 C  CA  . ALA A 1 133 ? 14.464  15.977  19.895  1.00 11.43 ? 134 ALA A CA  1 
ATOM   1091 C  C   . ALA A 1 133 ? 15.495  14.909  20.284  1.00 10.64 ? 134 ALA A C   1 
ATOM   1092 O  O   . ALA A 1 133 ? 15.585  14.502  21.473  1.00 9.92  ? 134 ALA A O   1 
ATOM   1093 C  CB  . ALA A 1 133 ? 13.155  15.350  19.305  1.00 10.28 ? 134 ALA A CB  1 
ATOM   1094 N  N   . VAL A 1 134 ? 16.283  14.410  19.314  1.00 10.87 ? 135 VAL A N   1 
ATOM   1095 C  CA  . VAL A 1 134 ? 17.198  13.311  19.679  1.00 11.72 ? 135 VAL A CA  1 
ATOM   1096 C  C   . VAL A 1 134 ? 18.281  13.774  20.627  1.00 11.64 ? 135 VAL A C   1 
ATOM   1097 O  O   . VAL A 1 134 ? 18.990  12.953  21.207  1.00 11.49 ? 135 VAL A O   1 
ATOM   1098 C  CB  . VAL A 1 134 ? 17.819  12.555  18.488  1.00 11.95 ? 135 VAL A CB  1 
ATOM   1099 C  CG1 . VAL A 1 134 ? 16.734  11.927  17.649  1.00 12.25 ? 135 VAL A CG1 1 
ATOM   1100 C  CG2 . VAL A 1 134 ? 18.716  13.500  17.687  1.00 12.06 ? 135 VAL A CG2 1 
ATOM   1101 N  N   . GLN A 1 135 ? 18.427  15.102  20.831  1.00 11.11 ? 136 GLN A N   1 
ATOM   1102 C  CA  . GLN A 1 135 ? 19.447  15.540  21.769  1.00 13.24 ? 136 GLN A CA  1 
ATOM   1103 C  C   . GLN A 1 135 ? 18.871  15.673  23.172  1.00 13.31 ? 136 GLN A C   1 
ATOM   1104 O  O   . GLN A 1 135 ? 19.527  16.198  24.081  1.00 12.97 ? 136 GLN A O   1 
ATOM   1105 C  CB  . GLN A 1 135 ? 20.013  16.886  21.278  1.00 15.25 ? 136 GLN A CB  1 
ATOM   1106 C  CG  . GLN A 1 135 ? 20.604  16.761  19.899  1.00 19.30 ? 136 GLN A CG  1 
ATOM   1107 C  CD  . GLN A 1 135 ? 21.066  18.072  19.296  1.00 24.52 ? 136 GLN A CD  1 
ATOM   1108 O  OE1 . GLN A 1 135 ? 21.769  18.857  19.942  1.00 31.36 ? 136 GLN A OE1 1 
ATOM   1109 N  NE2 . GLN A 1 135 ? 20.663  18.326  18.057  1.00 25.43 ? 136 GLN A NE2 1 
ATOM   1110 N  N   . GLN A 1 136 ? 17.641  15.206  23.358  1.00 11.95 ? 137 GLN A N   1 
ATOM   1111 C  CA  . GLN A 1 136 ? 16.956  15.390  24.655  1.00 11.96 ? 137 GLN A CA  1 
ATOM   1112 C  C   . GLN A 1 136 ? 16.590  14.046  25.260  1.00 10.78 ? 137 GLN A C   1 
ATOM   1113 O  O   . GLN A 1 136 ? 16.262  13.087  24.542  1.00 9.81  ? 137 GLN A O   1 
ATOM   1114 C  CB  . GLN A 1 136 ? 15.675  16.229  24.502  1.00 12.19 ? 137 GLN A CB  1 
ATOM   1115 C  CG  . GLN A 1 136 ? 15.921  17.601  23.835  1.00 15.37 ? 137 GLN A CG  1 
ATOM   1116 C  CD  . GLN A 1 136 ? 16.880  18.517  24.610  1.00 17.52 ? 137 GLN A CD  1 
ATOM   1117 O  OE1 . GLN A 1 136 ? 17.063  18.390  25.803  1.00 21.77 ? 137 GLN A OE1 1 
ATOM   1118 N  NE2 . GLN A 1 136 ? 17.588  19.343  23.884  1.00 21.41 ? 137 GLN A NE2 1 
ATOM   1119 N  N   . PRO A 1 137 ? 16.638  13.947  26.604  1.00 11.37 ? 138 PRO A N   1 
ATOM   1120 C  CA  . PRO A 1 137 ? 16.373  12.631  27.226  1.00 11.74 ? 138 PRO A CA  1 
ATOM   1121 C  C   . PRO A 1 137 ? 14.927  12.159  27.102  1.00 11.39 ? 138 PRO A C   1 
ATOM   1122 O  O   . PRO A 1 137 ? 14.655  10.942  27.246  1.00 11.51 ? 138 PRO A O   1 
ATOM   1123 C  CB  . PRO A 1 137 ? 16.778  12.821  28.686  1.00 13.52 ? 138 PRO A CB  1 
ATOM   1124 C  CG  . PRO A 1 137 ? 16.849  14.295  28.873  1.00 14.87 ? 138 PRO A CG  1 
ATOM   1125 C  CD  . PRO A 1 137 ? 17.045  14.979  27.571  1.00 13.27 ? 138 PRO A CD  1 
ATOM   1126 N  N   . ASP A 1 138 ? 13.997  13.075  26.814  1.00 9.25  ? 139 ASP A N   1 
ATOM   1127 C  CA  . ASP A 1 138 ? 12.612  12.694  26.562  1.00 9.79  ? 139 ASP A CA  1 
ATOM   1128 C  C   . ASP A 1 138 ? 12.219  13.066  25.125  1.00 8.57  ? 139 ASP A C   1 
ATOM   1129 O  O   . ASP A 1 138 ? 11.093  13.482  24.892  1.00 9.16  ? 139 ASP A O   1 
ATOM   1130 C  CB  . ASP A 1 138 ? 11.601  13.365  27.516  1.00 10.74 ? 139 ASP A CB  1 
ATOM   1131 C  CG  . ASP A 1 138 ? 11.764  14.866  27.592  1.00 11.04 ? 139 ASP A CG  1 
ATOM   1132 O  OD1 . ASP A 1 138 ? 12.707  15.446  27.017  1.00 12.04 ? 139 ASP A OD1 1 
ATOM   1133 O  OD2 . ASP A 1 138 ? 10.895  15.463  28.247  1.00 11.85 ? 139 ASP A OD2 1 
ATOM   1134 N  N   . GLY A 1 139 ? 13.169  13.009  24.187  1.00 8.68  ? 140 GLY A N   1 
ATOM   1135 C  CA  . GLY A 1 139 ? 12.929  13.524  22.882  1.00 7.31  ? 140 GLY A CA  1 
ATOM   1136 C  C   . GLY A 1 139 ? 12.157  12.599  21.999  1.00 8.03  ? 140 GLY A C   1 
ATOM   1137 O  O   . GLY A 1 139 ? 11.384  13.089  21.172  1.00 7.83  ? 140 GLY A O   1 
ATOM   1138 N  N   . LEU A 1 140 ? 12.339  11.289  22.173  1.00 7.04  ? 141 LEU A N   1 
ATOM   1139 C  CA  . LEU A 1 140 ? 11.617  10.376  21.295  1.00 7.53  ? 141 LEU A CA  1 
ATOM   1140 C  C   . LEU A 1 140 ? 10.697  9.424   22.055  1.00 7.74  ? 141 LEU A C   1 
ATOM   1141 O  O   . LEU A 1 140 ? 10.940  9.105   23.202  1.00 8.36  ? 141 LEU A O   1 
ATOM   1142 C  CB  . LEU A 1 140 ? 12.581  9.533   20.468  1.00 8.04  ? 141 LEU A CB  1 
ATOM   1143 C  CG  . LEU A 1 140 ? 13.527  10.253  19.493  1.00 9.85  ? 141 LEU A CG  1 
ATOM   1144 C  CD1 . LEU A 1 140 ? 14.157  9.157   18.620  1.00 9.14  ? 141 LEU A CD1 1 
ATOM   1145 C  CD2 . LEU A 1 140 ? 12.845  11.234  18.574  1.00 9.80  ? 141 LEU A CD2 1 
ATOM   1146 N  N   . ALA A 1 141 ? 9.644   8.954   21.395  1.00 7.76  ? 142 ALA A N   1 
ATOM   1147 C  CA  . ALA A 1 141 ? 8.864   7.799   21.968  1.00 7.48  ? 142 ALA A CA  1 
ATOM   1148 C  C   . ALA A 1 141 ? 8.853   6.797   20.830  1.00 7.85  ? 142 ALA A C   1 
ATOM   1149 O  O   . ALA A 1 141 ? 8.416   7.096   19.714  1.00 8.38  ? 142 ALA A O   1 
ATOM   1150 C  CB  . ALA A 1 141 ? 7.441   8.231   22.314  1.00 7.18  ? 142 ALA A CB  1 
ATOM   1151 N  N   . VAL A 1 142 ? 9.314   5.589   21.109  1.00 7.72  ? 143 VAL A N   1 
ATOM   1152 C  CA  . VAL A 1 142 ? 9.290   4.552   20.089  1.00 7.24  ? 143 VAL A CA  1 
ATOM   1153 C  C   . VAL A 1 142 ? 8.349   3.465   20.534  1.00 7.49  ? 143 VAL A C   1 
ATOM   1154 O  O   . VAL A 1 142 ? 8.515   2.932   21.657  1.00 7.21  ? 143 VAL A O   1 
ATOM   1155 C  CB  . VAL A 1 142 ? 10.679  4.025   19.701  1.00 7.68  ? 143 VAL A CB  1 
ATOM   1156 C  CG1 . VAL A 1 142 ? 10.611  2.990   18.536  1.00 7.91  ? 143 VAL A CG1 1 
ATOM   1157 C  CG2 . VAL A 1 142 ? 11.530  5.195   19.199  1.00 8.66  ? 143 VAL A CG2 1 
ATOM   1158 N  N   . LEU A 1 143 ? 7.374   3.158   19.675  1.00 6.61  ? 144 LEU A N   1 
ATOM   1159 C  CA  . LEU A 1 143 ? 6.397   2.095   19.973  1.00 7.75  ? 144 LEU A CA  1 
ATOM   1160 C  C   . LEU A 1 143 ? 6.951   0.841   19.322  1.00 7.97  ? 144 LEU A C   1 
ATOM   1161 O  O   . LEU A 1 143 ? 7.037   0.806   18.040  1.00 8.46  ? 144 LEU A O   1 
ATOM   1162 C  CB  . LEU A 1 143 ? 5.031   2.559   19.392  1.00 8.57  ? 144 LEU A CB  1 
ATOM   1163 C  CG  . LEU A 1 143 ? 3.878   1.600   19.521  1.00 9.02  ? 144 LEU A CG  1 
ATOM   1164 C  CD1 . LEU A 1 143 ? 3.759   1.328   21.032  1.00 9.50  ? 144 LEU A CD1 1 
ATOM   1165 C  CD2 . LEU A 1 143 ? 2.616   2.136   18.840  1.00 9.84  ? 144 LEU A CD2 1 
ATOM   1166 N  N   . GLY A 1 144 ? 7.214   -0.223  20.150  1.00 7.95  ? 145 GLY A N   1 
ATOM   1167 C  CA  . GLY A 1 144 ? 7.762   -1.467  19.600  1.00 7.66  ? 145 GLY A CA  1 
ATOM   1168 C  C   . GLY A 1 144 ? 6.691   -2.522  19.559  1.00 7.17  ? 145 GLY A C   1 
ATOM   1169 O  O   . GLY A 1 144 ? 5.954   -2.664  20.529  1.00 7.34  ? 145 GLY A O   1 
ATOM   1170 N  N   . ILE A 1 145 ? 6.540   -3.212  18.438  1.00 7.24  ? 146 ILE A N   1 
ATOM   1171 C  CA  . ILE A 1 145 ? 5.491   -4.227  18.313  1.00 7.39  ? 146 ILE A CA  1 
ATOM   1172 C  C   . ILE A 1 145 ? 6.206   -5.461  17.791  1.00 7.30  ? 146 ILE A C   1 
ATOM   1173 O  O   . ILE A 1 145 ? 6.872   -5.423  16.762  1.00 7.74  ? 146 ILE A O   1 
ATOM   1174 C  CB  . ILE A 1 145 ? 4.447   -3.756  17.310  1.00 7.20  ? 146 ILE A CB  1 
ATOM   1175 C  CG1 . ILE A 1 145 ? 3.802   -2.468  17.827  1.00 7.79  ? 146 ILE A CG1 1 
ATOM   1176 C  CG2 . ILE A 1 145 ? 3.435   -4.883  17.032  1.00 8.14  ? 146 ILE A CG2 1 
ATOM   1177 C  CD1 . ILE A 1 145 ? 2.775   -1.832  16.882  1.00 7.11  ? 146 ILE A CD1 1 
ATOM   1178 N  N   . PHE A 1 146 ? 5.975   -6.580  18.454  1.00 8.01  ? 147 PHE A N   1 
ATOM   1179 C  CA  . PHE A 1 146 ? 6.662   -7.833  18.023  1.00 7.06  ? 147 PHE A CA  1 
ATOM   1180 C  C   . PHE A 1 146 ? 5.936   -8.498  16.899  1.00 7.54  ? 147 PHE A C   1 
ATOM   1181 O  O   . PHE A 1 146 ? 4.737   -8.354  16.788  1.00 7.23  ? 147 PHE A O   1 
ATOM   1182 C  CB  . PHE A 1 146 ? 6.674   -8.788  19.223  1.00 6.97  ? 147 PHE A CB  1 
ATOM   1183 C  CG  . PHE A 1 146 ? 7.582   -8.307  20.332  1.00 6.48  ? 147 PHE A CG  1 
ATOM   1184 C  CD1 . PHE A 1 146 ? 8.946   -8.163  20.116  1.00 7.36  ? 147 PHE A CD1 1 
ATOM   1185 C  CD2 . PHE A 1 146 ? 7.073   -8.106  21.586  1.00 7.37  ? 147 PHE A CD2 1 
ATOM   1186 C  CE1 . PHE A 1 146 ? 9.784   -7.803  21.143  1.00 6.74  ? 147 PHE A CE1 1 
ATOM   1187 C  CE2 . PHE A 1 146 ? 7.890   -7.757  22.653  1.00 7.20  ? 147 PHE A CE2 1 
ATOM   1188 C  CZ  . PHE A 1 146 ? 9.236   -7.592  22.413  1.00 7.25  ? 147 PHE A CZ  1 
ATOM   1189 N  N   . LEU A 1 147 ? 6.692   -9.143  16.018  1.00 7.32  ? 148 LEU A N   1 
ATOM   1190 C  CA  . LEU A 1 147 ? 6.101   -9.984  14.978  1.00 7.54  ? 148 LEU A CA  1 
ATOM   1191 C  C   . LEU A 1 147 ? 6.417   -11.462 15.222  1.00 7.91  ? 148 LEU A C   1 
ATOM   1192 O  O   . LEU A 1 147 ? 7.618   -11.800 15.369  1.00 7.53  ? 148 LEU A O   1 
ATOM   1193 C  CB  . LEU A 1 147 ? 6.692   -9.593  13.595  1.00 7.91  ? 148 LEU A CB  1 
ATOM   1194 C  CG  . LEU A 1 147 ? 6.035   -8.388  12.912  1.00 7.68  ? 148 LEU A CG  1 
ATOM   1195 C  CD1 . LEU A 1 147 ? 6.311   -7.086  13.735  1.00 8.49  ? 148 LEU A CD1 1 
ATOM   1196 C  CD2 . LEU A 1 147 ? 6.702   -8.163  11.568  1.00 7.29  ? 148 LEU A CD2 1 
ATOM   1197 N  N   . LYS A 1 148 ? 5.370   -12.327 15.177  1.00 8.79  ? 149 LYS A N   1 
ATOM   1198 C  CA  . LYS A 1 148 ? 5.571   -13.763 15.076  1.00 10.05 ? 149 LYS A CA  1 
ATOM   1199 C  C   . LYS A 1 148 ? 5.089   -14.261 13.697  1.00 10.92 ? 149 LYS A C   1 
ATOM   1200 O  O   . LYS A 1 148 ? 4.298   -13.624 13.004  1.00 11.41 ? 149 LYS A O   1 
ATOM   1201 C  CB  . LYS A 1 148 ? 4.841   -14.498 16.189  1.00 11.96 ? 149 LYS A CB  1 
ATOM   1202 C  CG  . LYS A 1 148 ? 3.323   -14.251 16.140  1.00 15.10 ? 149 LYS A CG  1 
ATOM   1203 C  CD  . LYS A 1 148 ? 2.726   -15.116 17.258  1.00 18.98 ? 149 LYS A CD  1 
ATOM   1204 C  CE  . LYS A 1 148 ? 1.225   -15.005 17.289  1.00 24.23 ? 149 LYS A CE  1 
ATOM   1205 N  NZ  . LYS A 1 148 ? 0.747   -15.980 18.329  1.00 31.26 ? 149 LYS A NZ  1 
ATOM   1206 N  N   . VAL A 1 149 ? 5.541   -15.451 13.325  1.00 10.25 ? 150 VAL A N   1 
ATOM   1207 C  CA  . VAL A 1 149 ? 5.174   -15.983 12.004  1.00 11.03 ? 150 VAL A CA  1 
ATOM   1208 C  C   . VAL A 1 149 ? 3.935   -16.863 12.207  1.00 12.61 ? 150 VAL A C   1 
ATOM   1209 O  O   . VAL A 1 149 ? 3.914   -17.750 13.088  1.00 13.58 ? 150 VAL A O   1 
ATOM   1210 C  CB  . VAL A 1 149 ? 6.330   -16.764 11.413  1.00 11.18 ? 150 VAL A CB  1 
ATOM   1211 C  CG1 . VAL A 1 149 ? 5.908   -17.528 10.104  1.00 10.80 ? 150 VAL A CG1 1 
ATOM   1212 C  CG2 . VAL A 1 149 ? 7.480   -15.778 11.143  1.00 11.55 ? 150 VAL A CG2 1 
ATOM   1213 N  N   . GLY A 1 150 ? 2.918   -16.610 11.431  1.00 10.66 ? 151 GLY A N   1 
ATOM   1214 C  CA  . GLY A 1 150 ? 1.638   -17.333 11.571  1.00 13.32 ? 151 GLY A CA  1 
ATOM   1215 C  C   . GLY A 1 150 ? 0.771   -16.910 10.412  1.00 12.73 ? 151 GLY A C   1 
ATOM   1216 O  O   . GLY A 1 150 ? 1.210   -17.044 9.274   1.00 13.01 ? 151 GLY A O   1 
ATOM   1217 N  N   A SER A 1 151 ? -0.450  -16.433 10.695  0.50 13.76 ? 152 SER A N   1 
ATOM   1218 N  N   B SER A 1 151 ? -0.437  -16.422 10.696  0.50 13.35 ? 152 SER A N   1 
ATOM   1219 C  CA  A SER A 1 151 ? -1.357  -15.871 9.653   0.50 14.31 ? 152 SER A CA  1 
ATOM   1220 C  CA  B SER A 1 151 ? -1.311  -15.845 9.652   0.50 13.63 ? 152 SER A CA  1 
ATOM   1221 C  C   A SER A 1 151 ? -0.782  -14.556 9.092   0.50 14.46 ? 152 SER A C   1 
ATOM   1222 C  C   B SER A 1 151 ? -0.684  -14.580 9.056   0.50 14.01 ? 152 SER A C   1 
ATOM   1223 O  O   A SER A 1 151 ? -0.067  -13.843 9.806   0.50 14.15 ? 152 SER A O   1 
ATOM   1224 O  O   B SER A 1 151 ? 0.145   -13.926 9.699   0.50 13.20 ? 152 SER A O   1 
ATOM   1225 C  CB  A SER A 1 151 ? -2.794  -15.675 10.186  0.50 15.90 ? 152 SER A CB  1 
ATOM   1226 C  CB  B SER A 1 151 ? -2.702  -15.548 10.208  0.50 14.63 ? 152 SER A CB  1 
ATOM   1227 O  OG  A SER A 1 151 ? -2.932  -14.481 10.952  0.50 17.36 ? 152 SER A OG  1 
ATOM   1228 O  OG  B SER A 1 151 ? -3.242  -16.709 10.793  0.50 14.57 ? 152 SER A OG  1 
ATOM   1229 N  N   . ALA A 1 152 ? -1.024  -14.272 7.798   1.00 12.66 ? 153 ALA A N   1 
ATOM   1230 C  CA  . ALA A 1 152 ? -0.580  -13.033 7.205   1.00 12.29 ? 153 ALA A CA  1 
ATOM   1231 C  C   . ALA A 1 152 ? -1.205  -11.805 7.921   1.00 12.27 ? 153 ALA A C   1 
ATOM   1232 O  O   . ALA A 1 152 ? -2.319  -11.887 8.448   1.00 13.41 ? 153 ALA A O   1 
ATOM   1233 C  CB  . ALA A 1 152 ? -0.875  -13.024 5.690   1.00 12.23 ? 153 ALA A CB  1 
ATOM   1234 N  N   . LYS A 1 153 ? -0.502  -10.665 7.904   1.00 12.29 ? 154 LYS A N   1 
ATOM   1235 C  CA  . LYS A 1 153 ? -1.052  -9.404  8.324   1.00 13.36 ? 154 LYS A CA  1 
ATOM   1236 C  C   . LYS A 1 153 ? -1.466  -8.628  7.005   1.00 12.49 ? 154 LYS A C   1 
ATOM   1237 O  O   . LYS A 1 153 ? -0.586  -8.133  6.279   1.00 13.49 ? 154 LYS A O   1 
ATOM   1238 C  CB  . LYS A 1 153 ? -0.006  -8.601  9.098   1.00 14.50 ? 154 LYS A CB  1 
ATOM   1239 C  CG  . LYS A 1 153 ? -0.596  -7.420  9.861   1.00 16.83 ? 154 LYS A CG  1 
ATOM   1240 C  CD  . LYS A 1 153 ? -1.406  -7.903  11.039  1.00 16.85 ? 154 LYS A CD  1 
ATOM   1241 C  CE  . LYS A 1 153 ? -1.982  -6.736  11.788  1.00 20.59 ? 154 LYS A CE  1 
ATOM   1242 N  NZ  . LYS A 1 153 ? -2.593  -7.259  13.010  1.00 21.30 ? 154 LYS A NZ  1 
ATOM   1243 N  N   . PRO A 1 154 ? -2.792  -8.572  6.703   1.00 14.72 ? 155 PRO A N   1 
ATOM   1244 C  CA  . PRO A 1 154 ? -3.339  -7.960  5.460   1.00 14.97 ? 155 PRO A CA  1 
ATOM   1245 C  C   . PRO A 1 154 ? -2.773  -6.539  5.333   1.00 16.59 ? 155 PRO A C   1 
ATOM   1246 O  O   . PRO A 1 154 ? -2.245  -6.175  4.250   1.00 17.56 ? 155 PRO A O   1 
ATOM   1247 C  CB  . PRO A 1 154 ? -4.871  -7.957  5.727   1.00 16.72 ? 155 PRO A CB  1 
ATOM   1248 C  CG  . PRO A 1 154 ? -5.024  -9.185  6.578   1.00 15.53 ? 155 PRO A CG  1 
ATOM   1249 C  CD  . PRO A 1 154 ? -3.872  -9.142  7.513   1.00 13.72 ? 155 PRO A CD  1 
ATOM   1250 N  N   . GLY A 1 155 ? -2.734  -5.831  6.464   1.00 15.64 ? 156 GLY A N   1 
ATOM   1251 C  CA  . GLY A 1 155 ? -2.206  -4.454  6.520   1.00 17.07 ? 156 GLY A CA  1 
ATOM   1252 C  C   . GLY A 1 155 ? -0.748  -4.195  6.274   1.00 16.75 ? 156 GLY A C   1 
ATOM   1253 O  O   . GLY A 1 155 ? -0.369  -3.057  6.083   1.00 19.38 ? 156 GLY A O   1 
ATOM   1254 N  N   . LEU A 1 156 ? 0.071   -5.242  6.264   1.00 15.02 ? 157 LEU A N   1 
ATOM   1255 C  CA  . LEU A 1 156 ? 1.458   -5.188  5.900   1.00 14.20 ? 157 LEU A CA  1 
ATOM   1256 C  C   . LEU A 1 156 ? 1.710   -5.489  4.458   1.00 13.56 ? 157 LEU A C   1 
ATOM   1257 O  O   . LEU A 1 156 ? 2.804   -5.263  3.960   1.00 13.59 ? 157 LEU A O   1 
ATOM   1258 C  CB  . LEU A 1 156 ? 2.267   -6.198  6.747   1.00 13.14 ? 157 LEU A CB  1 
ATOM   1259 C  CG  . LEU A 1 156 ? 3.816   -6.349  6.620   1.00 12.35 ? 157 LEU A CG  1 
ATOM   1260 C  CD1 . LEU A 1 156 ? 4.548   -5.045  6.946   1.00 11.94 ? 157 LEU A CD1 1 
ATOM   1261 C  CD2 . LEU A 1 156 ? 4.314   -7.518  7.482   1.00 12.85 ? 157 LEU A CD2 1 
ATOM   1262 N  N   . GLN A 1 157 ? 0.726   -6.050  3.754   1.00 14.56 ? 158 GLN A N   1 
ATOM   1263 C  CA  . GLN A 1 157 ? 1.061   -6.514  2.391   1.00 16.02 ? 158 GLN A CA  1 
ATOM   1264 C  C   . GLN A 1 157 ? 1.495   -5.412  1.440   1.00 15.51 ? 158 GLN A C   1 
ATOM   1265 O  O   . GLN A 1 157 ? 2.405   -5.639  0.634   1.00 16.35 ? 158 GLN A O   1 
ATOM   1266 C  CB  . GLN A 1 157 ? -0.080  -7.346  1.785   1.00 17.64 ? 158 GLN A CB  1 
ATOM   1267 C  CG  . GLN A 1 157 ? 0.370   -8.137  0.534   1.00 16.69 ? 158 GLN A CG  1 
ATOM   1268 C  CD  . GLN A 1 157 ? 1.497   -9.139  0.765   1.00 17.92 ? 158 GLN A CD  1 
ATOM   1269 O  OE1 . GLN A 1 157 ? 1.648   -9.708  1.851   1.00 17.58 ? 158 GLN A OE1 1 
ATOM   1270 N  NE2 . GLN A 1 157 ? 2.292   -9.368  -0.278  1.00 17.64 ? 158 GLN A NE2 1 
ATOM   1271 N  N   . LYS A 1 158 ? 0.894   -4.230  1.525   1.00 16.03 ? 159 LYS A N   1 
ATOM   1272 C  CA  . LYS A 1 158 ? 1.364   -3.135  0.655   1.00 17.25 ? 159 LYS A CA  1 
ATOM   1273 C  C   . LYS A 1 158 ? 2.833   -2.794  0.820   1.00 16.05 ? 159 LYS A C   1 
ATOM   1274 O  O   . LYS A 1 158 ? 3.510   -2.455  -0.143  1.00 16.04 ? 159 LYS A O   1 
ATOM   1275 C  CB  . LYS A 1 158 ? 0.536   -1.872  0.860   1.00 21.95 ? 159 LYS A CB  1 
ATOM   1276 C  CG  . LYS A 1 158 ? -0.865  -2.052  0.355   1.00 27.01 ? 159 LYS A CG  1 
ATOM   1277 C  CD  . LYS A 1 158 ? -1.422  -0.770  -0.252  1.00 35.81 ? 159 LYS A CD  1 
ATOM   1278 C  CE  . LYS A 1 158 ? -2.577  -1.077  -1.226  1.00 41.61 ? 159 LYS A CE  1 
ATOM   1279 N  NZ  . LYS A 1 158 ? -3.928  -1.080  -0.569  1.00 44.92 ? 159 LYS A NZ  1 
ATOM   1280 N  N   . VAL A 1 159 ? 3.327   -2.880  2.069   1.00 15.29 ? 160 VAL A N   1 
ATOM   1281 C  CA  . VAL A 1 159 ? 4.740   -2.696  2.322   1.00 13.00 ? 160 VAL A CA  1 
ATOM   1282 C  C   . VAL A 1 159 ? 5.534   -3.827  1.662   1.00 13.43 ? 160 VAL A C   1 
ATOM   1283 O  O   . VAL A 1 159 ? 6.525   -3.570  0.982   1.00 13.92 ? 160 VAL A O   1 
ATOM   1284 C  CB  . VAL A 1 159 ? 5.027   -2.622  3.839   1.00 13.35 ? 160 VAL A CB  1 
ATOM   1285 C  CG1 . VAL A 1 159 ? 6.529   -2.619  4.115   1.00 13.42 ? 160 VAL A CG1 1 
ATOM   1286 C  CG2 . VAL A 1 159 ? 4.346   -1.395  4.431   1.00 15.93 ? 160 VAL A CG2 1 
ATOM   1287 N  N   . VAL A 1 160 ? 5.136   -5.071  1.887   1.00 12.92 ? 161 VAL A N   1 
ATOM   1288 C  CA  . VAL A 1 160 ? 5.902   -6.202  1.372   1.00 15.63 ? 161 VAL A CA  1 
ATOM   1289 C  C   . VAL A 1 160 ? 5.953   -6.100  -0.146  1.00 15.74 ? 161 VAL A C   1 
ATOM   1290 O  O   . VAL A 1 160 ? 6.985   -6.327  -0.749  1.00 16.23 ? 161 VAL A O   1 
ATOM   1291 C  CB  . VAL A 1 160 ? 5.263   -7.556  1.851   1.00 17.23 ? 161 VAL A CB  1 
ATOM   1292 C  CG1 . VAL A 1 160 ? 5.695   -8.752  1.004   1.00 19.94 ? 161 VAL A CG1 1 
ATOM   1293 C  CG2 . VAL A 1 160 ? 5.595   -7.769  3.321   1.00 17.89 ? 161 VAL A CG2 1 
ATOM   1294 N  N   . ASP A 1 161 ? 4.852   -5.670  -0.748  1.00 18.46 ? 162 ASP A N   1 
ATOM   1295 C  CA  . ASP A 1 161 ? 4.808   -5.751  -2.211  1.00 20.27 ? 162 ASP A CA  1 
ATOM   1296 C  C   . ASP A 1 161 ? 5.717   -4.731  -2.901  1.00 21.67 ? 162 ASP A C   1 
ATOM   1297 O  O   . ASP A 1 161 ? 6.033   -4.907  -4.094  1.00 24.15 ? 162 ASP A O   1 
ATOM   1298 C  CB  . ASP A 1 161 ? 3.377   -5.622  -2.707  1.00 21.31 ? 162 ASP A CB  1 
ATOM   1299 C  CG  . ASP A 1 161 ? 2.669   -6.965  -2.737  1.00 21.37 ? 162 ASP A CG  1 
ATOM   1300 O  OD1 . ASP A 1 161 ? 3.343   -7.965  -2.853  1.00 24.76 ? 162 ASP A OD1 1 
ATOM   1301 O  OD2 . ASP A 1 161 ? 1.454   -7.009  -2.577  1.00 26.16 ? 162 ASP A OD2 1 
ATOM   1302 N  N   . VAL A 1 162 ? 6.089   -3.641  -2.201  1.00 17.91 ? 163 VAL A N   1 
ATOM   1303 C  CA  . VAL A 1 162 ? 6.900   -2.608  -2.806  1.00 20.11 ? 163 VAL A CA  1 
ATOM   1304 C  C   . VAL A 1 162 ? 8.410   -2.898  -2.617  1.00 16.70 ? 163 VAL A C   1 
ATOM   1305 O  O   . VAL A 1 162 ? 9.259   -2.213  -3.168  1.00 16.68 ? 163 VAL A O   1 
ATOM   1306 C  CB  . VAL A 1 162 ? 6.437   -1.216  -2.254  1.00 20.13 ? 163 VAL A CB  1 
ATOM   1307 C  CG1 . VAL A 1 162 ? 7.050   -0.905  -0.909  1.00 19.18 ? 163 VAL A CG1 1 
ATOM   1308 C  CG2 . VAL A 1 162 ? 6.671   -0.097  -3.247  1.00 22.64 ? 163 VAL A CG2 1 
ATOM   1309 N  N   . LEU A 1 163 ? 8.790   -3.899  -1.793  1.00 17.61 ? 164 LEU A N   1 
ATOM   1310 C  CA  . LEU A 1 163 ? 10.215  -4.081  -1.396  1.00 14.57 ? 164 LEU A CA  1 
ATOM   1311 C  C   . LEU A 1 163 ? 11.151  -4.431  -2.550  1.00 14.86 ? 164 LEU A C   1 
ATOM   1312 O  O   . LEU A 1 163 ? 12.337  -4.156  -2.511  1.00 14.21 ? 164 LEU A O   1 
ATOM   1313 C  CB  . LEU A 1 163 ? 10.386  -5.139  -0.289  1.00 13.18 ? 164 LEU A CB  1 
ATOM   1314 C  CG  . LEU A 1 163 ? 9.644   -4.950  1.041   1.00 13.17 ? 164 LEU A CG  1 
ATOM   1315 C  CD1 . LEU A 1 163 ? 9.934   -6.152  1.945   1.00 13.62 ? 164 LEU A CD1 1 
ATOM   1316 C  CD2 . LEU A 1 163 ? 10.112  -3.663  1.701   1.00 13.93 ? 164 LEU A CD2 1 
ATOM   1317 N  N   . ASP A 1 164 ? 10.600  -5.102  -3.553  1.00 18.94 ? 165 ASP A N   1 
ATOM   1318 C  CA  . ASP A 1 164 ? 11.400  -5.495  -4.697  1.00 21.14 ? 165 ASP A CA  1 
ATOM   1319 C  C   . ASP A 1 164 ? 11.937  -4.235  -5.444  1.00 22.02 ? 165 ASP A C   1 
ATOM   1320 O  O   . ASP A 1 164 ? 13.009  -4.275  -6.094  1.00 23.64 ? 165 ASP A O   1 
ATOM   1321 C  CB  . ASP A 1 164 ? 10.549  -6.389  -5.621  1.00 24.85 ? 165 ASP A CB  1 
ATOM   1322 C  CG  . ASP A 1 164 ? 9.639   -5.576  -6.504  1.00 31.25 ? 165 ASP A CG  1 
ATOM   1323 O  OD1 . ASP A 1 164 ? 8.673   -5.001  -5.978  1.00 34.13 ? 165 ASP A OD1 1 
ATOM   1324 O  OD2 . ASP A 1 164 ? 9.931   -5.419  -7.724  1.00 35.08 ? 165 ASP A OD2 1 
ATOM   1325 N  N   . SER A 1 165 ? 11.243  -3.120  -5.244  1.00 19.77 ? 166 SER A N   1 
ATOM   1326 C  CA  . SER A 1 165 ? 11.583  -1.829  -5.865  1.00 19.84 ? 166 SER A CA  1 
ATOM   1327 C  C   . SER A 1 165 ? 12.642  -1.026  -5.122  1.00 19.58 ? 166 SER A C   1 
ATOM   1328 O  O   . SER A 1 165 ? 13.199  -0.040  -5.667  1.00 17.64 ? 166 SER A O   1 
ATOM   1329 C  CB  . SER A 1 165 ? 10.324  -0.984  -6.065  1.00 19.29 ? 166 SER A CB  1 
ATOM   1330 O  OG  . SER A 1 165 ? 9.902   -0.271  -4.921  1.00 22.36 ? 166 SER A OG  1 
ATOM   1331 N  N   . ILE A 1 166 ? 12.945  -1.432  -3.881  1.00 16.56 ? 167 ILE A N   1 
ATOM   1332 C  CA  . ILE A 1 166 ? 14.047  -0.809  -3.111  1.00 16.76 ? 167 ILE A CA  1 
ATOM   1333 C  C   . ILE A 1 166 ? 14.956  -1.876  -2.539  1.00 16.80 ? 167 ILE A C   1 
ATOM   1334 O  O   . ILE A 1 166 ? 15.257  -1.898  -1.326  1.00 15.22 ? 167 ILE A O   1 
ATOM   1335 C  CB  . ILE A 1 166 ? 13.487  0.045   -1.924  1.00 16.72 ? 167 ILE A CB  1 
ATOM   1336 C  CG1 . ILE A 1 166 ? 12.508  -0.798  -1.090  1.00 16.70 ? 167 ILE A CG1 1 
ATOM   1337 C  CG2 . ILE A 1 166 ? 12.709  1.245   -2.443  1.00 19.27 ? 167 ILE A CG2 1 
ATOM   1338 C  CD1 . ILE A 1 166 ? 12.356  -0.301  0.352   1.00 17.36 ? 167 ILE A CD1 1 
ATOM   1339 N  N   . LYS A 1 167 ? 15.341  -2.811  -3.405  1.00 18.11 ? 168 LYS A N   1 
ATOM   1340 C  CA  . LYS A 1 167 ? 16.163  -3.924  -2.992  1.00 18.52 ? 168 LYS A CA  1 
ATOM   1341 C  C   . LYS A 1 167 ? 17.485  -3.533  -2.342  1.00 16.54 ? 168 LYS A C   1 
ATOM   1342 O  O   . LYS A 1 167 ? 17.897  -4.190  -1.389  1.00 14.17 ? 168 LYS A O   1 
ATOM   1343 C  CB  . LYS A 1 167 ? 16.523  -4.796  -4.193  1.00 18.34 ? 168 LYS A CB  1 
ATOM   1344 C  CG  . LYS A 1 167 ? 17.247  -6.048  -3.761  1.00 21.83 ? 168 LYS A CG  1 
ATOM   1345 C  CD  . LYS A 1 167 ? 17.537  -6.964  -4.962  1.00 25.12 ? 168 LYS A CD  1 
ATOM   1346 C  CE  . LYS A 1 167 ? 18.124  -8.263  -4.458  1.00 29.46 ? 168 LYS A CE  1 
ATOM   1347 N  NZ  . LYS A 1 167 ? 18.420  -9.284  -5.523  1.00 33.86 ? 168 LYS A NZ  1 
ATOM   1348 N  N   . THR A 1 168 ? 18.140  -2.457  -2.844  1.00 14.91 ? 169 THR A N   1 
ATOM   1349 C  CA  . THR A 1 168 ? 19.515  -2.181  -2.453  1.00 14.81 ? 169 THR A CA  1 
ATOM   1350 C  C   . THR A 1 168 ? 19.614  -0.829  -1.766  1.00 14.50 ? 169 THR A C   1 
ATOM   1351 O  O   . THR A 1 168 ? 18.759  0.000   -1.939  1.00 15.67 ? 169 THR A O   1 
ATOM   1352 C  CB  . THR A 1 168 ? 20.500  -2.177  -3.639  1.00 15.47 ? 169 THR A CB  1 
ATOM   1353 O  OG1 . THR A 1 168 ? 19.888  -1.461  -4.700  1.00 16.67 ? 169 THR A OG1 1 
ATOM   1354 C  CG2 . THR A 1 168 ? 20.839  -3.669  -4.070  1.00 15.77 ? 169 THR A CG2 1 
ATOM   1355 N  N   . LYS A 1 169 ? 20.673  -0.663  -0.993  1.00 15.73 ? 170 LYS A N   1 
ATOM   1356 C  CA  . LYS A 1 169 ? 20.919  0.552   -0.221  1.00 17.31 ? 170 LYS A CA  1 
ATOM   1357 C  C   . LYS A 1 169 ? 20.718  1.815   -1.025  1.00 18.50 ? 170 LYS A C   1 
ATOM   1358 O  O   . LYS A 1 169 ? 21.224  1.889   -2.132  1.00 20.47 ? 170 LYS A O   1 
ATOM   1359 C  CB  . LYS A 1 169 ? 22.336  0.490   0.328   1.00 17.05 ? 170 LYS A CB  1 
ATOM   1360 C  CG  . LYS A 1 169 ? 22.826  1.762   1.025   1.00 19.99 ? 170 LYS A CG  1 
ATOM   1361 C  CD  . LYS A 1 169 ? 24.047  1.472   1.851   1.00 22.79 ? 170 LYS A CD  1 
ATOM   1362 C  CE  . LYS A 1 169 ? 25.219  0.998   1.000   1.00 28.83 ? 170 LYS A CE  1 
ATOM   1363 N  NZ  . LYS A 1 169 ? 26.458  1.229   1.785   1.00 36.55 ? 170 LYS A NZ  1 
ATOM   1364 N  N   . GLY A 1 170 ? 19.941  2.762   -0.504  1.00 17.23 ? 171 GLY A N   1 
ATOM   1365 C  CA  . GLY A 1 170 ? 19.814  4.097   -1.125  1.00 17.54 ? 171 GLY A CA  1 
ATOM   1366 C  C   . GLY A 1 170 ? 18.709  4.162   -2.143  1.00 20.19 ? 171 GLY A C   1 
ATOM   1367 O  O   . GLY A 1 170 ? 18.362  5.270   -2.629  1.00 22.51 ? 171 GLY A O   1 
ATOM   1368 N  N   . LYS A 1 171 ? 18.092  3.017   -2.455  1.00 16.58 ? 172 LYS A N   1 
ATOM   1369 C  CA  . LYS A 1 171 ? 16.879  3.036   -3.256  1.00 16.66 ? 172 LYS A CA  1 
ATOM   1370 C  C   . LYS A 1 171 ? 15.643  3.487   -2.441  1.00 17.01 ? 172 LYS A C   1 
ATOM   1371 O  O   . LYS A 1 171 ? 15.461  3.078   -1.270  1.00 17.04 ? 172 LYS A O   1 
ATOM   1372 C  CB  . LYS A 1 171 ? 16.599  1.698   -3.960  1.00 16.57 ? 172 LYS A CB  1 
ATOM   1373 C  CG  . LYS A 1 171 ? 17.666  1.394   -5.021  1.00 19.22 ? 172 LYS A CG  1 
ATOM   1374 C  CD  . LYS A 1 171 ? 17.319  0.242   -5.989  1.00 24.71 ? 172 LYS A CD  1 
ATOM   1375 C  CE  . LYS A 1 171 ? 16.289  0.682   -7.039  1.00 25.96 ? 172 LYS A CE  1 
ATOM   1376 N  NZ  . LYS A 1 171 ? 15.660  -0.433  -7.842  1.00 25.17 ? 172 LYS A NZ  1 
ATOM   1377 N  N   . SER A 1 172 ? 14.812  4.298   -3.074  1.00 17.18 ? 173 SER A N   1 
ATOM   1378 C  CA  . SER A 1 172 ? 13.559  4.774   -2.509  1.00 17.86 ? 173 SER A CA  1 
ATOM   1379 C  C   . SER A 1 172 ? 12.390  4.706   -3.489  1.00 19.89 ? 173 SER A C   1 
ATOM   1380 O  O   . SER A 1 172 ? 12.561  4.592   -4.746  1.00 19.08 ? 173 SER A O   1 
ATOM   1381 C  CB  . SER A 1 172 ? 13.702  6.208   -1.955  1.00 21.26 ? 173 SER A CB  1 
ATOM   1382 O  OG  . SER A 1 172 ? 14.048  7.152   -2.953  1.00 20.71 ? 173 SER A OG  1 
ATOM   1383 N  N   . ALA A 1 173 ? 11.196  4.822   -2.963  1.00 20.35 ? 174 ALA A N   1 
ATOM   1384 C  CA  . ALA A 1 173 ? 10.013  4.682   -3.807  1.00 20.44 ? 174 ALA A CA  1 
ATOM   1385 C  C   . ALA A 1 173 ? 8.874   5.437   -3.163  1.00 25.28 ? 174 ALA A C   1 
ATOM   1386 O  O   . ALA A 1 173 ? 8.803   5.531   -1.938  1.00 20.11 ? 174 ALA A O   1 
ATOM   1387 C  CB  . ALA A 1 173 ? 9.672   3.226   -3.982  1.00 18.88 ? 174 ALA A CB  1 
ATOM   1388 N  N   . ASP A 1 174 ? 7.992   5.978   -3.998  1.00 22.54 ? 175 ASP A N   1 
ATOM   1389 C  CA  . ASP A 1 174 ? 6.820   6.670   -3.508  1.00 27.12 ? 175 ASP A CA  1 
ATOM   1390 C  C   . ASP A 1 174 ? 5.953   5.723   -2.756  1.00 23.83 ? 175 ASP A C   1 
ATOM   1391 O  O   . ASP A 1 174 ? 5.776   4.558   -3.147  1.00 21.67 ? 175 ASP A O   1 
ATOM   1392 C  CB  . ASP A 1 174 ? 6.060   7.350   -4.653  1.00 31.63 ? 175 ASP A CB  1 
ATOM   1393 C  CG  . ASP A 1 174 ? 6.940   8.363   -5.375  1.00 35.79 ? 175 ASP A CG  1 
ATOM   1394 O  OD1 . ASP A 1 174 ? 7.659   9.108   -4.676  1.00 40.68 ? 175 ASP A OD1 1 
ATOM   1395 O  OD2 . ASP A 1 174 ? 6.920   8.420   -6.628  1.00 40.86 ? 175 ASP A OD2 1 
ATOM   1396 N  N   . PHE A 1 175 ? 5.460   6.194   -1.618  1.00 20.11 ? 176 PHE A N   1 
ATOM   1397 C  CA  . PHE A 1 175 ? 4.700   5.287   -0.776  1.00 20.54 ? 176 PHE A CA  1 
ATOM   1398 C  C   . PHE A 1 175 ? 3.670   6.106   -0.053  1.00 19.68 ? 176 PHE A C   1 
ATOM   1399 O  O   . PHE A 1 175 ? 3.859   6.498   1.108   1.00 21.76 ? 176 PHE A O   1 
ATOM   1400 C  CB  . PHE A 1 175 ? 5.597   4.485   0.176   1.00 17.17 ? 176 PHE A CB  1 
ATOM   1401 C  CG  . PHE A 1 175 ? 4.935   3.236   0.693   1.00 15.13 ? 176 PHE A CG  1 
ATOM   1402 C  CD1 . PHE A 1 175 ? 4.569   2.206   -0.179  1.00 16.89 ? 176 PHE A CD1 1 
ATOM   1403 C  CD2 . PHE A 1 175 ? 4.652   3.085   2.055   1.00 16.68 ? 176 PHE A CD2 1 
ATOM   1404 C  CE1 . PHE A 1 175 ? 3.949   1.051   0.282   1.00 17.85 ? 176 PHE A CE1 1 
ATOM   1405 C  CE2 . PHE A 1 175 ? 4.036   1.923   2.537   1.00 15.62 ? 176 PHE A CE2 1 
ATOM   1406 C  CZ  . PHE A 1 175 ? 3.681   0.903   1.647   1.00 17.40 ? 176 PHE A CZ  1 
ATOM   1407 N  N   . THR A 1 176 ? 2.594   6.436   -0.755  1.00 17.64 ? 177 THR A N   1 
ATOM   1408 C  CA  . THR A 1 176 ? 1.540   7.261   -0.180  1.00 17.07 ? 177 THR A CA  1 
ATOM   1409 C  C   . THR A 1 176 ? 0.370   6.441   0.251   1.00 16.58 ? 177 THR A C   1 
ATOM   1410 O  O   . THR A 1 176 ? 0.184   5.302   -0.234  1.00 16.70 ? 177 THR A O   1 
ATOM   1411 C  CB  . THR A 1 176 ? 1.021   8.405   -1.154  1.00 19.79 ? 177 THR A CB  1 
ATOM   1412 O  OG1 . THR A 1 176 ? 0.886   7.891   -2.466  1.00 20.70 ? 177 THR A OG1 1 
ATOM   1413 C  CG2 . THR A 1 176 ? 1.976   9.562   -1.183  1.00 20.91 ? 177 THR A CG2 1 
ATOM   1414 N  N   . ASN A 1 177 ? -0.416  7.038   1.130   1.00 15.71 ? 178 ASN A N   1 
ATOM   1415 C  CA  . ASN A 1 177 ? -1.722  6.531   1.573   1.00 14.99 ? 178 ASN A CA  1 
ATOM   1416 C  C   . ASN A 1 177 ? -1.600  5.171   2.271   1.00 14.87 ? 178 ASN A C   1 
ATOM   1417 O  O   . ASN A 1 177 ? -2.510  4.366   2.262   1.00 16.71 ? 178 ASN A O   1 
ATOM   1418 C  CB  . ASN A 1 177 ? -2.690  6.442   0.402   1.00 16.36 ? 178 ASN A CB  1 
ATOM   1419 C  CG  . ASN A 1 177 ? -2.938  7.794   -0.223  1.00 17.41 ? 178 ASN A CG  1 
ATOM   1420 O  OD1 . ASN A 1 177 ? -3.623  8.611   0.360   1.00 18.85 ? 178 ASN A OD1 1 
ATOM   1421 N  ND2 . ASN A 1 177 ? -2.313  8.057   -1.371  1.00 17.89 ? 178 ASN A ND2 1 
ATOM   1422 N  N   . PHE A 1 178 ? -0.464  4.960   2.918   1.00 14.61 ? 179 PHE A N   1 
ATOM   1423 C  CA  . PHE A 1 178 ? -0.309  3.738   3.732   1.00 13.76 ? 179 PHE A CA  1 
ATOM   1424 C  C   . PHE A 1 178 ? -0.807  4.042   5.110   1.00 14.23 ? 179 PHE A C   1 
ATOM   1425 O  O   . PHE A 1 178 ? -0.385  5.054   5.692   1.00 16.60 ? 179 PHE A O   1 
ATOM   1426 C  CB  . PHE A 1 178 ? 1.119   3.270   3.791   1.00 13.08 ? 179 PHE A CB  1 
ATOM   1427 C  CG  . PHE A 1 178 ? 1.271   2.053   4.633   1.00 13.38 ? 179 PHE A CG  1 
ATOM   1428 C  CD1 . PHE A 1 178 ? 0.826   0.822   4.149   1.00 13.04 ? 179 PHE A CD1 1 
ATOM   1429 C  CD2 . PHE A 1 178 ? 1.648   2.179   5.973   1.00 13.36 ? 179 PHE A CD2 1 
ATOM   1430 C  CE1 . PHE A 1 178 ? 0.881   -0.305  4.949   1.00 13.73 ? 179 PHE A CE1 1 
ATOM   1431 C  CE2 . PHE A 1 178 ? 1.701   1.050   6.778   1.00 12.78 ? 179 PHE A CE2 1 
ATOM   1432 C  CZ  . PHE A 1 178 ? 1.314   -0.186  6.289   1.00 12.74 ? 179 PHE A CZ  1 
ATOM   1433 N  N   . ASP A 1 179 ? -1.670  3.171   5.647   1.00 14.88 ? 180 ASP A N   1 
ATOM   1434 C  CA  . ASP A 1 179 ? -2.308  3.399   6.937   1.00 13.99 ? 180 ASP A CA  1 
ATOM   1435 C  C   . ASP A 1 179 ? -1.656  2.549   8.013   1.00 12.78 ? 180 ASP A C   1 
ATOM   1436 O  O   . ASP A 1 179 ? -1.842  1.344   8.042   1.00 11.63 ? 180 ASP A O   1 
ATOM   1437 C  CB  . ASP A 1 179 ? -3.780  3.041   6.837   1.00 15.21 ? 180 ASP A CB  1 
ATOM   1438 C  CG  . ASP A 1 179 ? -4.583  3.469   8.060   1.00 18.05 ? 180 ASP A CG  1 
ATOM   1439 O  OD1 . ASP A 1 179 ? -3.998  3.721   9.144   1.00 15.56 ? 180 ASP A OD1 1 
ATOM   1440 O  OD2 . ASP A 1 179 ? -5.820  3.629   7.901   1.00 20.26 ? 180 ASP A OD2 1 
ATOM   1441 N  N   . PRO A 1 180 ? -0.851  3.165   8.932   1.00 13.08 ? 181 PRO A N   1 
ATOM   1442 C  CA  . PRO A 1 180 ? -0.123  2.303   9.923   1.00 12.14 ? 181 PRO A CA  1 
ATOM   1443 C  C   . PRO A 1 180 ? -1.017  1.668   10.978  1.00 12.77 ? 181 PRO A C   1 
ATOM   1444 O  O   . PRO A 1 180 ? -0.543  0.750   11.740  1.00 10.64 ? 181 PRO A O   1 
ATOM   1445 C  CB  . PRO A 1 180 ? 0.896   3.272   10.529  1.00 14.28 ? 181 PRO A CB  1 
ATOM   1446 C  CG  . PRO A 1 180 ? 0.218   4.617   10.417  1.00 13.09 ? 181 PRO A CG  1 
ATOM   1447 C  CD  . PRO A 1 180 ? -0.527  4.593   9.107   1.00 13.58 ? 181 PRO A CD  1 
ATOM   1448 N  N   . ARG A 1 181 ? -2.287  2.093   11.014  1.00 11.66 ? 182 ARG A N   1 
ATOM   1449 C  CA  . ARG A 1 181 ? -3.265  1.442   11.943  1.00 12.83 ? 182 ARG A CA  1 
ATOM   1450 C  C   . ARG A 1 181 ? -3.417  -0.050  11.592  1.00 11.95 ? 182 ARG A C   1 
ATOM   1451 O  O   . ARG A 1 181 ? -3.730  -0.879  12.458  1.00 12.59 ? 182 ARG A O   1 
ATOM   1452 C  CB  . ARG A 1 181 ? -4.625  2.153   11.948  1.00 14.86 ? 182 ARG A CB  1 
ATOM   1453 C  CG  . ARG A 1 181 ? -4.551  3.578   12.502  1.00 15.15 ? 182 ARG A CG  1 
ATOM   1454 C  CD  . ARG A 1 181 ? -5.879  4.248   12.393  1.00 16.40 ? 182 ARG A CD  1 
ATOM   1455 N  NE  . ARG A 1 181 ? -6.236  4.422   11.001  1.00 17.24 ? 182 ARG A NE  1 
ATOM   1456 C  CZ  . ARG A 1 181 ? -7.364  5.003   10.633  1.00 20.79 ? 182 ARG A CZ  1 
ATOM   1457 N  NH1 . ARG A 1 181 ? -8.191  5.472   11.556  1.00 19.55 ? 182 ARG A NH1 1 
ATOM   1458 N  NH2 . ARG A 1 181 ? -7.662  5.116   9.356   1.00 21.53 ? 182 ARG A NH2 1 
ATOM   1459 N  N   . GLY A 1 182 ? -3.125  -0.387  10.355  1.00 12.38 ? 183 GLY A N   1 
ATOM   1460 C  CA  . GLY A 1 182 ? -3.166  -1.783  9.949   1.00 12.31 ? 183 GLY A CA  1 
ATOM   1461 C  C   . GLY A 1 182 ? -2.022  -2.651  10.454  1.00 13.74 ? 183 GLY A C   1 
ATOM   1462 O  O   . GLY A 1 182 ? -2.021  -3.850  10.161  1.00 15.65 ? 183 GLY A O   1 
ATOM   1463 N  N   . LEU A 1 183 ? -1.062  -2.089  11.206  1.00 13.48 ? 184 LEU A N   1 
ATOM   1464 C  CA  . LEU A 1 183 ? 0.058   -2.867  11.728  1.00 12.40 ? 184 LEU A CA  1 
ATOM   1465 C  C   . LEU A 1 183 ? -0.055  -3.086  13.237  1.00 12.74 ? 184 LEU A C   1 
ATOM   1466 O  O   . LEU A 1 183 ? 0.882   -3.618  13.841  1.00 14.00 ? 184 LEU A O   1 
ATOM   1467 C  CB  . LEU A 1 183 ? 1.385   -2.172  11.432  1.00 13.57 ? 184 LEU A CB  1 
ATOM   1468 C  CG  . LEU A 1 183 ? 1.627   -1.944  9.926   1.00 14.69 ? 184 LEU A CG  1 
ATOM   1469 C  CD1 . LEU A 1 183 ? 2.832   -1.092  9.766   1.00 14.69 ? 184 LEU A CD1 1 
ATOM   1470 C  CD2 . LEU A 1 183 ? 1.739   -3.220  9.099   1.00 15.35 ? 184 LEU A CD2 1 
ATOM   1471 N  N   . LEU A 1 184 ? -1.164  -2.633  13.845  1.00 11.08 ? 185 LEU A N   1 
ATOM   1472 C  CA  . LEU A 1 184 ? -1.308  -2.687  15.323  1.00 10.60 ? 185 LEU A CA  1 
ATOM   1473 C  C   . LEU A 1 184 ? -2.043  -3.942  15.771  1.00 12.75 ? 185 LEU A C   1 
ATOM   1474 O  O   . LEU A 1 184 ? -3.115  -4.319  15.195  1.00 15.94 ? 185 LEU A O   1 
ATOM   1475 C  CB  . LEU A 1 184 ? -2.091  -1.463  15.859  1.00 10.35 ? 185 LEU A CB  1 
ATOM   1476 C  CG  . LEU A 1 184 ? -1.518  -0.109  15.460  1.00 10.12 ? 185 LEU A CG  1 
ATOM   1477 C  CD1 . LEU A 1 184 ? -2.406  1.080   15.827  1.00 10.48 ? 185 LEU A CD1 1 
ATOM   1478 C  CD2 . LEU A 1 184 ? -0.068  0.076   15.961  1.00 11.03 ? 185 LEU A CD2 1 
ATOM   1479 N  N   . PRO A 1 185 ? -1.615  -4.487  16.904  1.00 12.00 ? 186 PRO A N   1 
ATOM   1480 C  CA  . PRO A 1 185 ? -2.445  -5.550  17.422  1.00 11.95 ? 186 PRO A CA  1 
ATOM   1481 C  C   . PRO A 1 185 ? -3.740  -5.063  18.077  1.00 12.56 ? 186 PRO A C   1 
ATOM   1482 O  O   . PRO A 1 185 ? -3.985  -3.860  18.242  1.00 13.19 ? 186 PRO A O   1 
ATOM   1483 C  CB  . PRO A 1 185 ? -1.545  -6.185  18.488  1.00 10.95 ? 186 PRO A CB  1 
ATOM   1484 C  CG  . PRO A 1 185 ? -0.765  -5.022  19.048  1.00 9.71  ? 186 PRO A CG  1 
ATOM   1485 C  CD  . PRO A 1 185 ? -0.575  -4.053  17.852  1.00 10.30 ? 186 PRO A CD  1 
ATOM   1486 N  N   . GLU A 1 186 ? -4.547  -5.999  18.572  1.00 12.84 ? 187 GLU A N   1 
ATOM   1487 C  CA  . GLU A 1 186 ? -5.786  -5.590  19.169  1.00 14.24 ? 187 GLU A CA  1 
ATOM   1488 C  C   . GLU A 1 186 ? -5.571  -4.856  20.532  1.00 14.31 ? 187 GLU A C   1 
ATOM   1489 O  O   . GLU A 1 186 ? -6.149  -3.803  20.787  1.00 15.56 ? 187 GLU A O   1 
ATOM   1490 C  CB  . GLU A 1 186 ? -6.678  -6.863  19.221  1.00 17.23 ? 187 GLU A CB  1 
ATOM   1491 C  CG  . GLU A 1 186 ? -7.451  -6.964  20.469  1.00 20.45 ? 187 GLU A CG  1 
ATOM   1492 C  CD  . GLU A 1 186 ? -8.316  -8.232  20.535  1.00 23.78 ? 187 GLU A CD  1 
ATOM   1493 O  OE1 . GLU A 1 186 ? -8.234  -9.114  19.630  1.00 21.39 ? 187 GLU A OE1 1 
ATOM   1494 O  OE2 . GLU A 1 186 ? -9.111  -8.252  21.528  1.00 28.66 ? 187 GLU A OE2 1 
ATOM   1495 N  N   . SER A 1 187 ? -4.704  -5.369  21.402  1.00 12.03 ? 188 SER A N   1 
ATOM   1496 C  CA  . SER A 1 187 ? -4.502  -4.772  22.733  1.00 12.74 ? 188 SER A CA  1 
ATOM   1497 C  C   . SER A 1 187 ? -3.359  -3.771  22.667  1.00 12.30 ? 188 SER A C   1 
ATOM   1498 O  O   . SER A 1 187 ? -2.325  -4.027  21.992  1.00 14.32 ? 188 SER A O   1 
ATOM   1499 C  CB  . SER A 1 187 ? -4.037  -5.832  23.719  1.00 12.30 ? 188 SER A CB  1 
ATOM   1500 O  OG  . SER A 1 187 ? -3.850  -5.305  25.039  1.00 12.60 ? 188 SER A OG  1 
ATOM   1501 N  N   . LEU A 1 188 ? -3.536  -2.718  23.421  1.00 11.43 ? 189 LEU A N   1 
ATOM   1502 C  CA  . LEU A 1 188 ? -2.456  -1.751  23.640  1.00 12.10 ? 189 LEU A CA  1 
ATOM   1503 C  C   . LEU A 1 188 ? -1.803  -1.887  25.012  1.00 11.85 ? 189 LEU A C   1 
ATOM   1504 O  O   . LEU A 1 188 ? -1.167  -0.946  25.475  1.00 14.50 ? 189 LEU A O   1 
ATOM   1505 C  CB  . LEU A 1 188 ? -2.986  -0.306  23.385  1.00 11.99 ? 189 LEU A CB  1 
ATOM   1506 C  CG  . LEU A 1 188 ? -3.444  -0.005  21.942  1.00 14.30 ? 189 LEU A CG  1 
ATOM   1507 C  CD1 . LEU A 1 188 ? -3.868  1.442   21.898  1.00 15.60 ? 189 LEU A CD1 1 
ATOM   1508 C  CD2 . LEU A 1 188 ? -2.357  -0.250  20.893  1.00 14.92 ? 189 LEU A CD2 1 
ATOM   1509 N  N   . ASP A 1 189 ? -1.945  -3.037  25.705  1.00 12.08 ? 190 ASP A N   1 
ATOM   1510 C  CA  . ASP A 1 189 ? -1.178  -3.274  26.936  1.00 10.94 ? 190 ASP A CA  1 
ATOM   1511 C  C   . ASP A 1 189 ? 0.321   -3.238  26.595  1.00 10.44 ? 190 ASP A C   1 
ATOM   1512 O  O   . ASP A 1 189 ? 0.737   -3.707  25.496  1.00 9.49  ? 190 ASP A O   1 
ATOM   1513 C  CB  . ASP A 1 189 ? -1.527  -4.585  27.573  1.00 11.82 ? 190 ASP A CB  1 
ATOM   1514 C  CG  . ASP A 1 189 ? -2.959  -4.560  28.157  1.00 13.05 ? 190 ASP A CG  1 
ATOM   1515 O  OD1 . ASP A 1 189 ? -3.552  -3.478  28.243  1.00 15.67 ? 190 ASP A OD1 1 
ATOM   1516 O  OD2 . ASP A 1 189 ? -3.444  -5.624  28.464  1.00 16.56 ? 190 ASP A OD2 1 
ATOM   1517 N  N   . TYR A 1 190 ? 1.086   -2.583  27.466  1.00 9.07  ? 191 TYR A N   1 
ATOM   1518 C  CA  . TYR A 1 190 ? 2.496   -2.289  27.108  1.00 8.69  ? 191 TYR A CA  1 
ATOM   1519 C  C   . TYR A 1 190 ? 3.425   -2.355  28.333  1.00 8.64  ? 191 TYR A C   1 
ATOM   1520 O  O   . TYR A 1 190 ? 2.997   -2.294  29.498  1.00 8.33  ? 191 TYR A O   1 
ATOM   1521 C  CB  . TYR A 1 190 ? 2.635   -0.886  26.415  1.00 8.79  ? 191 TYR A CB  1 
ATOM   1522 C  CG  . TYR A 1 190 ? 2.249   0.228   27.333  1.00 9.77  ? 191 TYR A CG  1 
ATOM   1523 C  CD1 . TYR A 1 190 ? 3.206   0.834   28.183  1.00 10.35 ? 191 TYR A CD1 1 
ATOM   1524 C  CD2 . TYR A 1 190 ? 0.943   0.765   27.294  1.00 9.69  ? 191 TYR A CD2 1 
ATOM   1525 C  CE1 . TYR A 1 190 ? 2.821   1.885   29.034  1.00 10.19 ? 191 TYR A CE1 1 
ATOM   1526 C  CE2 . TYR A 1 190 ? 0.570   1.811   28.121  1.00 11.75 ? 191 TYR A CE2 1 
ATOM   1527 C  CZ  . TYR A 1 190 ? 1.509   2.356   28.989  1.00 11.93 ? 191 TYR A CZ  1 
ATOM   1528 O  OH  . TYR A 1 190 ? 1.120   3.377   29.830  1.00 11.12 ? 191 TYR A OH  1 
ATOM   1529 N  N   . TRP A 1 191 ? 4.714   -2.526  28.060  1.00 8.78  ? 192 TRP A N   1 
ATOM   1530 C  CA  . TRP A 1 191 ? 5.805   -2.281  29.041  1.00 8.52  ? 192 TRP A CA  1 
ATOM   1531 C  C   . TRP A 1 191 ? 6.518   -1.009  28.625  1.00 8.23  ? 192 TRP A C   1 
ATOM   1532 O  O   . TRP A 1 191 ? 6.512   -0.628  27.442  1.00 9.15  ? 192 TRP A O   1 
ATOM   1533 C  CB  . TRP A 1 191 ? 6.833   -3.402  28.962  1.00 8.67  ? 192 TRP A CB  1 
ATOM   1534 C  CG  . TRP A 1 191 ? 6.301   -4.712  29.407  1.00 8.60  ? 192 TRP A CG  1 
ATOM   1535 C  CD1 . TRP A 1 191 ? 5.993   -5.135  30.703  1.00 8.69  ? 192 TRP A CD1 1 
ATOM   1536 C  CD2 . TRP A 1 191 ? 6.070   -5.838  28.556  1.00 8.56  ? 192 TRP A CD2 1 
ATOM   1537 N  NE1 . TRP A 1 191 ? 5.552   -6.477  30.666  1.00 9.97  ? 192 TRP A NE1 1 
ATOM   1538 C  CE2 . TRP A 1 191 ? 5.558   -6.920  29.392  1.00 9.81  ? 192 TRP A CE2 1 
ATOM   1539 C  CE3 . TRP A 1 191 ? 6.193   -6.037  27.206  1.00 8.46  ? 192 TRP A CE3 1 
ATOM   1540 C  CZ2 . TRP A 1 191 ? 5.249   -8.145  28.870  1.00 9.19  ? 192 TRP A CZ2 1 
ATOM   1541 C  CZ3 . TRP A 1 191 ? 5.813   -7.243  26.680  1.00 8.76  ? 192 TRP A CZ3 1 
ATOM   1542 C  CH2 . TRP A 1 191 ? 5.404   -8.298  27.491  1.00 9.46  ? 192 TRP A CH2 1 
ATOM   1543 N  N   . THR A 1 192 ? 7.046   -0.264  29.581  1.00 7.66  ? 193 THR A N   1 
ATOM   1544 C  CA  . THR A 1 192 ? 7.745   0.993   29.232  1.00 7.95  ? 193 THR A CA  1 
ATOM   1545 C  C   . THR A 1 192 ? 8.977   1.172   30.093  1.00 8.75  ? 193 THR A C   1 
ATOM   1546 O  O   . THR A 1 192 ? 8.983   0.731   31.248  1.00 8.72  ? 193 THR A O   1 
ATOM   1547 C  CB  . THR A 1 192 ? 6.822   2.211   29.380  1.00 8.50  ? 193 THR A CB  1 
ATOM   1548 O  OG1 . THR A 1 192 ? 7.469   3.399   28.922  1.00 8.08  ? 193 THR A OG1 1 
ATOM   1549 C  CG2 . THR A 1 192 ? 6.428   2.448   30.845  1.00 8.40  ? 193 THR A CG2 1 
ATOM   1550 N  N   . TYR A 1 193 ? 10.068  1.745   29.497  1.00 7.47  ? 194 TYR A N   1 
ATOM   1551 C  CA  . TYR A 1 193 ? 11.277  2.006   30.235  1.00 7.66  ? 194 TYR A CA  1 
ATOM   1552 C  C   . TYR A 1 193 ? 12.066  3.060   29.437  1.00 7.74  ? 194 TYR A C   1 
ATOM   1553 O  O   . TYR A 1 193 ? 11.783  3.255   28.227  1.00 7.32  ? 194 TYR A O   1 
ATOM   1554 C  CB  . TYR A 1 193 ? 12.087  0.680   30.418  1.00 7.83  ? 194 TYR A CB  1 
ATOM   1555 C  CG  . TYR A 1 193 ? 12.824  0.250   29.176  1.00 7.73  ? 194 TYR A CG  1 
ATOM   1556 C  CD1 . TYR A 1 193 ? 12.152  -0.497  28.167  1.00 8.02  ? 194 TYR A CD1 1 
ATOM   1557 C  CD2 . TYR A 1 193 ? 14.131  0.603   28.970  1.00 8.18  ? 194 TYR A CD2 1 
ATOM   1558 C  CE1 . TYR A 1 193 ? 12.796  -0.841  26.981  1.00 7.14  ? 194 TYR A CE1 1 
ATOM   1559 C  CE2 . TYR A 1 193 ? 14.805  0.271   27.781  1.00 8.23  ? 194 TYR A CE2 1 
ATOM   1560 C  CZ  . TYR A 1 193 ? 14.154  -0.442  26.835  1.00 7.68  ? 194 TYR A CZ  1 
ATOM   1561 O  OH  . TYR A 1 193 ? 14.772  -0.741  25.643  1.00 7.68  ? 194 TYR A OH  1 
ATOM   1562 N  N   . PRO A 1 194 ? 13.000  3.746   30.112  1.00 7.73  ? 195 PRO A N   1 
ATOM   1563 C  CA  . PRO A 1 194 ? 13.823  4.786   29.476  1.00 7.81  ? 195 PRO A CA  1 
ATOM   1564 C  C   . PRO A 1 194 ? 15.017  4.139   28.817  1.00 7.57  ? 195 PRO A C   1 
ATOM   1565 O  O   . PRO A 1 194 ? 15.678  3.337   29.439  1.00 7.84  ? 195 PRO A O   1 
ATOM   1566 C  CB  . PRO A 1 194 ? 14.311  5.650   30.680  1.00 8.72  ? 195 PRO A CB  1 
ATOM   1567 C  CG  . PRO A 1 194 ? 14.249  4.710   31.860  1.00 8.60  ? 195 PRO A CG  1 
ATOM   1568 C  CD  . PRO A 1 194 ? 13.061  3.815   31.595  1.00 8.28  ? 195 PRO A CD  1 
ATOM   1569 N  N   . GLY A 1 195 ? 15.288  4.453   27.555  1.00 7.49  ? 196 GLY A N   1 
ATOM   1570 C  CA  . GLY A 1 195 ? 16.385  3.726   26.828  1.00 7.96  ? 196 GLY A CA  1 
ATOM   1571 C  C   . GLY A 1 195 ? 16.904  4.572   25.707  1.00 7.67  ? 196 GLY A C   1 
ATOM   1572 O  O   . GLY A 1 195 ? 16.958  5.837   25.822  1.00 8.23  ? 196 GLY A O   1 
ATOM   1573 N  N   . SER A 1 196 ? 17.312  3.915   24.636  1.00 8.03  ? 197 SER A N   1 
ATOM   1574 C  CA  . SER A 1 196 ? 18.067  4.612   23.598  1.00 7.25  ? 197 SER A CA  1 
ATOM   1575 C  C   . SER A 1 196 ? 17.679  4.255   22.186  1.00 7.32  ? 197 SER A C   1 
ATOM   1576 O  O   . SER A 1 196 ? 16.956  3.282   21.989  1.00 6.83  ? 197 SER A O   1 
ATOM   1577 C  CB  . SER A 1 196 ? 19.588  4.251   23.776  1.00 7.07  ? 197 SER A CB  1 
ATOM   1578 O  OG  . SER A 1 196 ? 19.845  2.888   23.319  1.00 6.68  ? 197 SER A OG  1 
ATOM   1579 N  N   . LEU A 1 197 ? 18.188  5.006   21.194  1.00 7.46  ? 198 LEU A N   1 
ATOM   1580 C  CA  . LEU A 1 197 ? 18.211  4.466   19.819  1.00 8.23  ? 198 LEU A CA  1 
ATOM   1581 C  C   . LEU A 1 197 ? 18.955  3.128   19.877  1.00 7.91  ? 198 LEU A C   1 
ATOM   1582 O  O   . LEU A 1 197 ? 19.979  2.978   20.539  1.00 8.91  ? 198 LEU A O   1 
ATOM   1583 C  CB  . LEU A 1 197 ? 19.011  5.441   18.985  1.00 9.61  ? 198 LEU A CB  1 
ATOM   1584 C  CG  . LEU A 1 197 ? 18.427  6.821   18.919  1.00 10.84 ? 198 LEU A CG  1 
ATOM   1585 C  CD1 . LEU A 1 197 ? 19.329  7.673   18.019  1.00 12.81 ? 198 LEU A CD1 1 
ATOM   1586 C  CD2 . LEU A 1 197 ? 17.006  6.846   18.401  1.00 10.78 ? 198 LEU A CD2 1 
ATOM   1587 N  N   . THR A 1 198 ? 18.477  2.145   19.109  1.00 7.29  ? 199 THR A N   1 
ATOM   1588 C  CA  . THR A 1 198 ? 19.162  0.863   19.115  1.00 7.49  ? 199 THR A CA  1 
ATOM   1589 C  C   . THR A 1 198 ? 20.208  0.724   17.968  1.00 7.90  ? 199 THR A C   1 
ATOM   1590 O  O   . THR A 1 198 ? 20.724  -0.383  17.811  1.00 8.58  ? 199 THR A O   1 
ATOM   1591 C  CB  . THR A 1 198 ? 18.158  -0.281  18.916  1.00 6.88  ? 199 THR A CB  1 
ATOM   1592 O  OG1 . THR A 1 198 ? 17.590  -0.219  17.581  1.00 7.16  ? 199 THR A OG1 1 
ATOM   1593 C  CG2 . THR A 1 198 ? 17.083  -0.238  19.973  1.00 6.64  ? 199 THR A CG2 1 
ATOM   1594 N  N   . THR A 1 199 ? 20.403  1.752   17.134  1.00 8.97  ? 200 THR A N   1 
ATOM   1595 C  CA  . THR A 1 199 ? 21.539  1.733   16.198  1.00 9.26  ? 200 THR A CA  1 
ATOM   1596 C  C   . THR A 1 199 ? 22.345  2.987   16.461  1.00 9.70  ? 200 THR A C   1 
ATOM   1597 O  O   . THR A 1 199 ? 21.845  3.935   17.068  1.00 8.88  ? 200 THR A O   1 
ATOM   1598 C  CB  . THR A 1 199 ? 21.098  1.851   14.706  1.00 10.62 ? 200 THR A CB  1 
ATOM   1599 O  OG1 . THR A 1 199 ? 20.623  3.180   14.451  1.00 15.62 ? 200 THR A OG1 1 
ATOM   1600 C  CG2 . THR A 1 199 ? 20.000  0.876   14.334  1.00 10.97 ? 200 THR A CG2 1 
ATOM   1601 N  N   . PRO A 1 200 ? 23.592  3.014   15.955  1.00 10.02 ? 201 PRO A N   1 
ATOM   1602 C  CA  . PRO A 1 200 ? 24.335  4.245   16.046  1.00 9.96  ? 201 PRO A CA  1 
ATOM   1603 C  C   . PRO A 1 200 ? 23.450  5.386   15.517  1.00 9.67  ? 201 PRO A C   1 
ATOM   1604 O  O   . PRO A 1 200 ? 22.774  5.226   14.448  1.00 11.45 ? 201 PRO A O   1 
ATOM   1605 C  CB  . PRO A 1 200 ? 25.519  3.958   15.112  1.00 9.92  ? 201 PRO A CB  1 
ATOM   1606 C  CG  . PRO A 1 200 ? 25.802  2.494   15.383  1.00 10.60 ? 201 PRO A CG  1 
ATOM   1607 C  CD  . PRO A 1 200 ? 24.397  1.897   15.390  1.00 10.62 ? 201 PRO A CD  1 
ATOM   1608 N  N   . PRO A 1 201 ? 23.491  6.577   16.157  1.00 9.78  ? 202 PRO A N   1 
ATOM   1609 C  CA  . PRO A 1 201 ? 24.378  7.029   17.248  1.00 10.18 ? 202 PRO A CA  1 
ATOM   1610 C  C   . PRO A 1 201 ? 24.035  6.645   18.688  1.00 9.73  ? 202 PRO A C   1 
ATOM   1611 O  O   . PRO A 1 201 ? 24.685  7.159   19.660  1.00 10.21 ? 202 PRO A O   1 
ATOM   1612 C  CB  . PRO A 1 201 ? 24.343  8.566   17.111  1.00 10.00 ? 202 PRO A CB  1 
ATOM   1613 C  CG  . PRO A 1 201 ? 23.023  8.900   16.499  1.00 11.52 ? 202 PRO A CG  1 
ATOM   1614 C  CD  . PRO A 1 201 ? 22.674  7.696   15.605  1.00 10.56 ? 202 PRO A CD  1 
ATOM   1615 N  N   . LEU A 1 202 ? 23.044  5.745   18.853  1.00 9.42  ? 203 LEU A N   1 
ATOM   1616 C  CA  . LEU A 1 202 ? 22.773  5.091   20.150  1.00 8.53  ? 203 LEU A CA  1 
ATOM   1617 C  C   . LEU A 1 202 ? 22.380  6.134   21.252  1.00 8.95  ? 203 LEU A C   1 
ATOM   1618 O  O   . LEU A 1 202 ? 22.541  5.887   22.443  1.00 8.85  ? 203 LEU A O   1 
ATOM   1619 C  CB  . LEU A 1 202 ? 23.942  4.189   20.665  1.00 8.86  ? 203 LEU A CB  1 
ATOM   1620 C  CG  . LEU A 1 202 ? 24.270  3.106   19.613  1.00 8.66  ? 203 LEU A CG  1 
ATOM   1621 C  CD1 . LEU A 1 202 ? 25.496  2.471   20.215  1.00 9.25  ? 203 LEU A CD1 1 
ATOM   1622 C  CD2 . LEU A 1 202 ? 23.185  2.050   19.627  1.00 8.45  ? 203 LEU A CD2 1 
ATOM   1623 N  N   . LEU A 1 203 ? 21.905  7.286   20.802  1.00 8.81  ? 204 LEU A N   1 
ATOM   1624 C  CA  . LEU A 1 203 ? 21.531  8.379   21.708  1.00 9.53  ? 204 LEU A CA  1 
ATOM   1625 C  C   . LEU A 1 203 ? 20.471  7.958   22.728  1.00 9.20  ? 204 LEU A C   1 
ATOM   1626 O  O   . LEU A 1 203 ? 19.465  7.283   22.409  1.00 8.84  ? 204 LEU A O   1 
ATOM   1627 C  CB  . LEU A 1 203 ? 21.059  9.594   20.908  1.00 10.28 ? 204 LEU A CB  1 
ATOM   1628 C  CG  . LEU A 1 203 ? 22.191  10.155  19.981  1.00 11.17 ? 204 LEU A CG  1 
ATOM   1629 C  CD1 . LEU A 1 203 ? 21.481  11.138  19.063  1.00 13.38 ? 204 LEU A CD1 1 
ATOM   1630 C  CD2 . LEU A 1 203 ? 23.343  10.795  20.778  1.00 14.33 ? 204 LEU A CD2 1 
ATOM   1631 N  N   . GLU A 1 204 ? 20.699  8.411   23.951  1.00 9.04  ? 205 GLU A N   1 
ATOM   1632 C  CA  . GLU A 1 204 ? 19.885  8.039   25.075  1.00 9.51  ? 205 GLU A CA  1 
ATOM   1633 C  C   . GLU A 1 204 ? 18.682  8.988   25.190  1.00 9.87  ? 205 GLU A C   1 
ATOM   1634 O  O   . GLU A 1 204 ? 18.546  9.752   26.193  1.00 10.42 ? 205 GLU A O   1 
ATOM   1635 C  CB  . GLU A 1 204 ? 20.751  7.960   26.330  1.00 10.20 ? 205 GLU A CB  1 
ATOM   1636 C  CG  . GLU A 1 204 ? 21.611  6.684   26.217  1.00 11.19 ? 205 GLU A CG  1 
ATOM   1637 C  CD  . GLU A 1 204 ? 22.496  6.412   27.398  1.00 12.43 ? 205 GLU A CD  1 
ATOM   1638 O  OE1 . GLU A 1 204 ? 22.798  7.353   28.161  1.00 12.84 ? 205 GLU A OE1 1 
ATOM   1639 O  OE2 . GLU A 1 204 ? 22.923  5.257   27.546  1.00 10.49 ? 205 GLU A OE2 1 
ATOM   1640 N  N   . CYS A 1 205 ? 17.771  8.886   24.208  1.00 8.33  ? 206 CYS A N   1 
ATOM   1641 C  CA  . CYS A 1 205 ? 16.738  9.924   24.028  1.00 9.13  ? 206 CYS A CA  1 
ATOM   1642 C  C   . CYS A 1 205 ? 15.328  9.332   23.946  1.00 8.25  ? 206 CYS A C   1 
ATOM   1643 O  O   . CYS A 1 205 ? 14.375  10.016  23.513  1.00 9.24  ? 206 CYS A O   1 
ATOM   1644 C  CB  . CYS A 1 205 ? 17.041  10.744  22.780  1.00 9.40  ? 206 CYS A CB  1 
ATOM   1645 S  SG  . CYS A 1 205 ? 17.079  9.780   21.232  1.00 9.24  ? 206 CYS A SG  1 
ATOM   1646 N  N   . VAL A 1 206 ? 15.189  8.026   24.265  1.00 8.23  ? 207 VAL A N   1 
ATOM   1647 C  CA  . VAL A 1 206 ? 13.929  7.284   23.894  1.00 7.76  ? 207 VAL A CA  1 
ATOM   1648 C  C   . VAL A 1 206 ? 13.154  6.824   25.111  1.00 7.55  ? 207 VAL A C   1 
ATOM   1649 O  O   . VAL A 1 206 ? 13.713  6.225   26.003  1.00 9.44  ? 207 VAL A O   1 
ATOM   1650 C  CB  . VAL A 1 206 ? 14.219  5.995   23.030  1.00 7.50  ? 207 VAL A CB  1 
ATOM   1651 C  CG1 . VAL A 1 206 ? 12.840  5.374   22.679  1.00 6.75  ? 207 VAL A CG1 1 
ATOM   1652 C  CG2 . VAL A 1 206 ? 14.983  6.389   21.725  1.00 8.00  ? 207 VAL A CG2 1 
ATOM   1653 N  N   . THR A 1 207 ? 11.851  7.120   25.134  1.00 7.96  ? 208 THR A N   1 
ATOM   1654 C  CA  . THR A 1 207 ? 10.922  6.437   26.030  1.00 7.01  ? 208 THR A CA  1 
ATOM   1655 C  C   . THR A 1 207 ? 10.427  5.274   25.224  1.00 6.94  ? 208 THR A C   1 
ATOM   1656 O  O   . THR A 1 207 ? 9.723   5.475   24.208  1.00 7.07  ? 208 THR A O   1 
ATOM   1657 C  CB  . THR A 1 207 ? 9.783   7.357   26.488  1.00 8.49  ? 208 THR A CB  1 
ATOM   1658 O  OG1 . THR A 1 207 ? 10.350  8.417   27.289  1.00 8.31  ? 208 THR A OG1 1 
ATOM   1659 C  CG2 . THR A 1 207 ? 8.803   6.541   27.368  1.00 7.66  ? 208 THR A CG2 1 
ATOM   1660 N  N   . TRP A 1 208 ? 10.799  4.063   25.643  1.00 6.61  ? 209 TRP A N   1 
ATOM   1661 C  CA  . TRP A 1 208 ? 10.321  2.871   24.925  1.00 6.70  ? 209 TRP A CA  1 
ATOM   1662 C  C   . TRP A 1 208 ? 8.969   2.410   25.379  1.00 6.98  ? 209 TRP A C   1 
ATOM   1663 O  O   . TRP A 1 208 ? 8.739   2.353   26.584  1.00 7.58  ? 209 TRP A O   1 
ATOM   1664 C  CB  . TRP A 1 208 ? 11.314  1.706   25.141  1.00 6.68  ? 209 TRP A CB  1 
ATOM   1665 C  CG  . TRP A 1 208 ? 12.434  1.849   24.152  1.00 6.15  ? 209 TRP A CG  1 
ATOM   1666 C  CD1 . TRP A 1 208 ? 13.690  2.414   24.314  1.00 6.65  ? 209 TRP A CD1 1 
ATOM   1667 C  CD2 . TRP A 1 208 ? 12.384  1.425   22.773  1.00 6.62  ? 209 TRP A CD2 1 
ATOM   1668 N  NE1 . TRP A 1 208 ? 14.389  2.420   23.135  1.00 6.56  ? 209 TRP A NE1 1 
ATOM   1669 C  CE2 . TRP A 1 208 ? 13.648  1.832   22.168  1.00 6.50  ? 209 TRP A CE2 1 
ATOM   1670 C  CE3 . TRP A 1 208 ? 11.383  0.848   21.962  1.00 6.25  ? 209 TRP A CE3 1 
ATOM   1671 C  CZ2 . TRP A 1 208 ? 13.928  1.619   20.833  1.00 6.39  ? 209 TRP A CZ2 1 
ATOM   1672 C  CZ3 . TRP A 1 208 ? 11.670  0.568   20.637  1.00 7.20  ? 209 TRP A CZ3 1 
ATOM   1673 C  CH2 . TRP A 1 208 ? 12.931  0.953   20.057  1.00 6.37  ? 209 TRP A CH2 1 
ATOM   1674 N  N   . ILE A 1 209 ? 8.060   2.166   24.445  1.00 7.09  ? 210 ILE A N   1 
ATOM   1675 C  CA  . ILE A 1 209 ? 6.751   1.599   24.827  1.00 6.84  ? 210 ILE A CA  1 
ATOM   1676 C  C   . ILE A 1 209 ? 6.639   0.336   24.002  1.00 7.05  ? 210 ILE A C   1 
ATOM   1677 O  O   . ILE A 1 209 ? 6.549   0.411   22.792  1.00 7.40  ? 210 ILE A O   1 
ATOM   1678 C  CB  . ILE A 1 209 ? 5.664   2.592   24.477  1.00 7.42  ? 210 ILE A CB  1 
ATOM   1679 C  CG1 . ILE A 1 209 ? 5.931   3.891   25.224  1.00 7.81  ? 210 ILE A CG1 1 
ATOM   1680 C  CG2 . ILE A 1 209 ? 4.230   2.035   24.771  1.00 7.17  ? 210 ILE A CG2 1 
ATOM   1681 C  CD1 . ILE A 1 209 ? 5.024   5.048   24.729  1.00 9.15  ? 210 ILE A CD1 1 
ATOM   1682 N  N   . VAL A 1 210 ? 6.678   -0.830  24.664  1.00 6.76  ? 211 VAL A N   1 
ATOM   1683 C  CA  . VAL A 1 210 ? 6.719   -2.115  23.883  1.00 6.97  ? 211 VAL A CA  1 
ATOM   1684 C  C   . VAL A 1 210 ? 5.396   -2.863  24.134  1.00 7.32  ? 211 VAL A C   1 
ATOM   1685 O  O   . VAL A 1 210 ? 5.051   -3.155  25.300  1.00 6.76  ? 211 VAL A O   1 
ATOM   1686 C  CB  . VAL A 1 210 ? 7.894   -2.998  24.315  1.00 7.12  ? 211 VAL A CB  1 
ATOM   1687 C  CG1 . VAL A 1 210 ? 7.920   -4.381  23.605  1.00 5.92  ? 211 VAL A CG1 1 
ATOM   1688 C  CG2 . VAL A 1 210 ? 9.188   -2.244  23.998  1.00 6.70  ? 211 VAL A CG2 1 
ATOM   1689 N  N   . LEU A 1 211 ? 4.667   -3.118  23.057  1.00 7.35  ? 212 LEU A N   1 
ATOM   1690 C  CA  . LEU A 1 211 ? 3.372   -3.789  23.254  1.00 8.10  ? 212 LEU A CA  1 
ATOM   1691 C  C   . LEU A 1 211 ? 3.557   -5.267  23.578  1.00 8.58  ? 212 LEU A C   1 
ATOM   1692 O  O   . LEU A 1 211 ? 4.388   -5.945  23.018  1.00 9.44  ? 212 LEU A O   1 
ATOM   1693 C  CB  . LEU A 1 211 ? 2.497   -3.666  22.007  1.00 8.17  ? 212 LEU A CB  1 
ATOM   1694 C  CG  . LEU A 1 211 ? 2.155   -2.246  21.559  1.00 8.57  ? 212 LEU A CG  1 
ATOM   1695 C  CD1 . LEU A 1 211 ? 1.108   -2.272  20.426  1.00 8.86  ? 212 LEU A CD1 1 
ATOM   1696 C  CD2 . LEU A 1 211 ? 1.600   -1.417  22.734  1.00 8.87  ? 212 LEU A CD2 1 
ATOM   1697 N  N   . LYS A 1 212 ? 2.732   -5.743  24.486  1.00 9.30  ? 213 LYS A N   1 
ATOM   1698 C  CA  . LYS A 1 212 ? 2.761   -7.111  24.895  1.00 9.62  ? 213 LYS A CA  1 
ATOM   1699 C  C   . LYS A 1 212 ? 2.249   -8.064  23.856  1.00 9.87  ? 213 LYS A C   1 
ATOM   1700 O  O   . LYS A 1 212 ? 2.714   -9.136  23.769  1.00 10.71 ? 213 LYS A O   1 
ATOM   1701 C  CB  . LYS A 1 212 ? 1.975   -7.313  26.178  1.00 11.18 ? 213 LYS A CB  1 
ATOM   1702 C  CG  . LYS A 1 212 ? 1.816   -8.764  26.566  1.00 11.56 ? 213 LYS A CG  1 
ATOM   1703 C  CD  . LYS A 1 212 ? 0.938   -8.904  27.782  1.00 13.16 ? 213 LYS A CD  1 
ATOM   1704 C  CE  . LYS A 1 212 ? 1.071   -10.223 28.493  1.00 13.67 ? 213 LYS A CE  1 
ATOM   1705 N  NZ  . LYS A 1 212 ? -0.154  -10.399 29.337  1.00 17.90 ? 213 LYS A NZ  1 
ATOM   1706 N  N   . GLU A 1 213 ? 1.280   -7.637  23.085  1.00 9.57  ? 214 GLU A N   1 
ATOM   1707 C  CA  . GLU A 1 213 ? 0.642   -8.516  22.080  1.00 10.54 ? 214 GLU A CA  1 
ATOM   1708 C  C   . GLU A 1 213 ? 1.381   -8.424  20.760  1.00 9.81  ? 214 GLU A C   1 
ATOM   1709 O  O   . GLU A 1 213 ? 1.463   -7.324  20.185  1.00 9.78  ? 214 GLU A O   1 
ATOM   1710 C  CB  . GLU A 1 213 ? -0.797  -8.077  21.839  1.00 10.91 ? 214 GLU A CB  1 
ATOM   1711 C  CG  . GLU A 1 213 ? -1.400  -9.020  20.810  1.00 13.52 ? 214 GLU A CG  1 
ATOM   1712 C  CD  . GLU A 1 213 ? -2.906  -8.924  20.677  1.00 16.04 ? 214 GLU A CD  1 
ATOM   1713 O  OE1 . GLU A 1 213 ? -3.579  -8.162  21.353  1.00 13.70 ? 214 GLU A OE1 1 
ATOM   1714 O  OE2 . GLU A 1 213 ? -3.407  -9.783  19.936  1.00 24.39 ? 214 GLU A OE2 1 
ATOM   1715 N  N   . PRO A 1 214 ? 1.937   -9.538  20.254  1.00 10.93 ? 215 PRO A N   1 
ATOM   1716 C  CA  . PRO A 1 214 ? 2.608   -9.466  18.964  1.00 10.40 ? 215 PRO A CA  1 
ATOM   1717 C  C   . PRO A 1 214 ? 1.568   -9.464  17.840  1.00 11.61 ? 215 PRO A C   1 
ATOM   1718 O  O   . PRO A 1 214 ? 0.405   -9.806  18.086  1.00 12.27 ? 215 PRO A O   1 
ATOM   1719 C  CB  . PRO A 1 214 ? 3.398   -10.778 18.874  1.00 10.58 ? 215 PRO A CB  1 
ATOM   1720 C  CG  . PRO A 1 214 ? 2.710   -11.729 19.771  1.00 11.97 ? 215 PRO A CG  1 
ATOM   1721 C  CD  . PRO A 1 214 ? 2.001   -10.907 20.839  1.00 11.25 ? 215 PRO A CD  1 
ATOM   1722 N  N   . ILE A 1 215 ? 1.963   -8.982  16.656  1.00 10.13 ? 216 ILE A N   1 
ATOM   1723 C  CA  . ILE A 1 215 ? 1.139   -9.174  15.466  1.00 10.87 ? 216 ILE A CA  1 
ATOM   1724 C  C   . ILE A 1 215 ? 1.651   -10.429 14.736  1.00 11.17 ? 216 ILE A C   1 
ATOM   1725 O  O   . ILE A 1 215 ? 2.840   -10.811 14.883  1.00 10.36 ? 216 ILE A O   1 
ATOM   1726 C  CB  . ILE A 1 215 ? 1.104   -7.937  14.517  1.00 10.24 ? 216 ILE A CB  1 
ATOM   1727 C  CG1 . ILE A 1 215 ? 2.561   -7.537  14.033  1.00 10.55 ? 216 ILE A CG1 1 
ATOM   1728 C  CG2 . ILE A 1 215 ? 0.362   -6.734  15.203  1.00 11.23 ? 216 ILE A CG2 1 
ATOM   1729 C  CD1 . ILE A 1 215 ? 2.604   -6.593  12.784  1.00 10.60 ? 216 ILE A CD1 1 
ATOM   1730 N  N   A SER A 1 216 ? 0.755   -11.097 13.997  0.50 11.21 ? 217 SER A N   1 
ATOM   1731 N  N   B SER A 1 216 ? 0.750   -11.101 14.001  0.50 11.85 ? 217 SER A N   1 
ATOM   1732 C  CA  A SER A 1 216 ? 1.164   -12.268 13.198  0.50 11.50 ? 217 SER A CA  1 
ATOM   1733 C  CA  B SER A 1 216 ? 1.137   -12.279 13.194  0.50 12.54 ? 217 SER A CA  1 
ATOM   1734 C  C   A SER A 1 216 ? 1.380   -11.833 11.773  0.50 11.50 ? 217 SER A C   1 
ATOM   1735 C  C   B SER A 1 216 ? 1.378   -11.833 11.773  0.50 12.12 ? 217 SER A C   1 
ATOM   1736 O  O   A SER A 1 216 ? 0.564   -11.086 11.224  0.50 12.45 ? 217 SER A O   1 
ATOM   1737 O  O   B SER A 1 216 ? 0.567   -11.083 11.221  0.50 13.08 ? 217 SER A O   1 
ATOM   1738 C  CB  A SER A 1 216 ? 0.101   -13.363 13.241  0.50 11.95 ? 217 SER A CB  1 
ATOM   1739 C  CB  B SER A 1 216 ? 0.028   -13.337 13.187  0.50 13.95 ? 217 SER A CB  1 
ATOM   1740 O  OG  A SER A 1 216 ? 0.056   -13.941 14.531  0.50 12.40 ? 217 SER A OG  1 
ATOM   1741 O  OG  B SER A 1 216 ? 0.411   -14.458 12.403  0.50 17.30 ? 217 SER A OG  1 
ATOM   1742 N  N   . VAL A 1 217 ? 2.501   -12.256 11.204  1.00 10.98 ? 218 VAL A N   1 
ATOM   1743 C  CA  . VAL A 1 217 ? 2.781   -12.049 9.762   1.00 11.78 ? 218 VAL A CA  1 
ATOM   1744 C  C   . VAL A 1 217 ? 3.001   -13.456 9.183   1.00 11.31 ? 218 VAL A C   1 
ATOM   1745 O  O   . VAL A 1 217 ? 3.364   -14.404 9.913   1.00 12.09 ? 218 VAL A O   1 
ATOM   1746 C  CB  . VAL A 1 217 ? 3.992   -11.180 9.487   1.00 11.67 ? 218 VAL A CB  1 
ATOM   1747 C  CG1 . VAL A 1 217 ? 3.742   -9.824  10.122  1.00 11.90 ? 218 VAL A CG1 1 
ATOM   1748 C  CG2 . VAL A 1 217 ? 5.242   -11.825 10.089  1.00 11.50 ? 218 VAL A CG2 1 
ATOM   1749 N  N   . SER A 1 218 ? 2.815   -13.594 7.887   1.00 10.58 ? 219 SER A N   1 
ATOM   1750 C  CA  . SER A 1 218 ? 3.064   -14.918 7.306   1.00 11.75 ? 219 SER A CA  1 
ATOM   1751 C  C   . SER A 1 218 ? 4.552   -15.187 7.018   1.00 12.10 ? 219 SER A C   1 
ATOM   1752 O  O   . SER A 1 218 ? 5.398   -14.290 6.887   1.00 10.00 ? 219 SER A O   1 
ATOM   1753 C  CB  . SER A 1 218 ? 2.222   -15.145 6.032   1.00 11.83 ? 219 SER A CB  1 
ATOM   1754 O  OG  . SER A 1 218 ? 2.712   -14.275 5.051   1.00 12.96 ? 219 SER A OG  1 
ATOM   1755 N  N   A SER A 1 219 ? 4.892   -16.463 6.917   0.50 12.23 ? 220 SER A N   1 
ATOM   1756 N  N   B SER A 1 219 ? 4.883   -16.469 6.912   0.50 12.20 ? 220 SER A N   1 
ATOM   1757 C  CA  A SER A 1 219 ? 6.210   -16.831 6.486   0.50 13.07 ? 220 SER A CA  1 
ATOM   1758 C  CA  B SER A 1 219 ? 6.196   -16.857 6.478   0.50 13.02 ? 220 SER A CA  1 
ATOM   1759 C  C   A SER A 1 219 ? 6.565   -16.131 5.156   0.50 13.69 ? 220 SER A C   1 
ATOM   1760 C  C   B SER A 1 219 ? 6.562   -16.147 5.157   0.50 13.67 ? 220 SER A C   1 
ATOM   1761 O  O   A SER A 1 219 ? 7.665   -15.606 5.023   0.50 13.11 ? 220 SER A O   1 
ATOM   1762 O  O   B SER A 1 219 ? 7.665   -15.624 5.035   0.50 13.12 ? 220 SER A O   1 
ATOM   1763 C  CB  A SER A 1 219 ? 6.318   -18.359 6.411   0.50 14.42 ? 220 SER A CB  1 
ATOM   1764 C  CB  B SER A 1 219 ? 6.309   -18.397 6.408   0.50 14.24 ? 220 SER A CB  1 
ATOM   1765 O  OG  A SER A 1 219 ? 5.321   -18.849 5.545   0.50 14.72 ? 220 SER A OG  1 
ATOM   1766 O  OG  B SER A 1 219 ? 7.651   -18.798 6.182   0.50 14.51 ? 220 SER A OG  1 
ATOM   1767 N  N   . GLU A 1 220 ? 5.632   -16.066 4.192   1.00 14.45 ? 221 GLU A N   1 
ATOM   1768 C  CA  . GLU A 1 220 ? 5.947   -15.424 2.867   1.00 15.80 ? 221 GLU A CA  1 
ATOM   1769 C  C   . GLU A 1 220 ? 6.227   -13.921 3.050   1.00 14.78 ? 221 GLU A C   1 
ATOM   1770 O  O   . GLU A 1 220 ? 7.082   -13.354 2.355   1.00 14.97 ? 221 GLU A O   1 
ATOM   1771 C  CB  . GLU A 1 220 ? 4.849   -15.619 1.820   1.00 20.67 ? 221 GLU A CB  1 
ATOM   1772 C  CG  . GLU A 1 220 ? 4.650   -17.112 1.491   1.00 23.00 ? 221 GLU A CG  1 
ATOM   1773 C  CD  . GLU A 1 220 ? 3.589   -17.750 2.401   1.00 28.87 ? 221 GLU A CD  1 
ATOM   1774 O  OE1 . GLU A 1 220 ? 3.385   -17.305 3.555   1.00 24.75 ? 221 GLU A OE1 1 
ATOM   1775 O  OE2 . GLU A 1 220 ? 2.944   -18.742 1.967   1.00 32.47 ? 221 GLU A OE2 1 
ATOM   1776 N  N   . GLN A 1 221 ? 5.514   -13.307 3.979   1.00 13.78 ? 222 GLN A N   1 
ATOM   1777 C  CA  . GLN A 1 221 ? 5.743   -11.851 4.256   1.00 12.86 ? 222 GLN A CA  1 
ATOM   1778 C  C   . GLN A 1 221 ? 7.182   -11.596 4.786   1.00 13.11 ? 222 GLN A C   1 
ATOM   1779 O  O   . GLN A 1 221 ? 7.947   -10.753 4.251   1.00 11.49 ? 222 GLN A O   1 
ATOM   1780 C  CB  . GLN A 1 221 ? 4.646   -11.360 5.203   1.00 12.97 ? 222 GLN A CB  1 
ATOM   1781 C  CG  . GLN A 1 221 ? 3.373   -11.031 4.430   1.00 12.69 ? 222 GLN A CG  1 
ATOM   1782 C  CD  . GLN A 1 221 ? 2.205   -10.554 5.265   1.00 12.74 ? 222 GLN A CD  1 
ATOM   1783 O  OE1 . GLN A 1 221 ? 2.030   -10.964 6.397   1.00 12.73 ? 222 GLN A OE1 1 
ATOM   1784 N  NE2 . GLN A 1 221 ? 1.414   -9.665  4.697   1.00 12.36 ? 222 GLN A NE2 1 
ATOM   1785 N  N   . VAL A 1 222 ? 7.596   -12.365 5.801   1.00 13.07 ? 223 VAL A N   1 
ATOM   1786 C  CA  . VAL A 1 222 ? 8.917   -12.179 6.401   1.00 13.04 ? 223 VAL A CA  1 
ATOM   1787 C  C   . VAL A 1 222 ? 10.037  -12.651 5.413   1.00 13.48 ? 223 VAL A C   1 
ATOM   1788 O  O   . VAL A 1 222 ? 11.098  -12.085 5.338   1.00 14.07 ? 223 VAL A O   1 
ATOM   1789 C  CB  . VAL A 1 222 ? 8.981   -12.810 7.810   1.00 14.61 ? 223 VAL A CB  1 
ATOM   1790 C  CG1 . VAL A 1 222 ? 9.057   -14.307 7.709   1.00 15.33 ? 223 VAL A CG1 1 
ATOM   1791 C  CG2 . VAL A 1 222 ? 10.172  -12.187 8.588   1.00 15.77 ? 223 VAL A CG2 1 
ATOM   1792 N  N   . LEU A 1 223 ? 9.733   -13.652 4.574   1.00 14.03 ? 224 LEU A N   1 
ATOM   1793 C  CA  . LEU A 1 223 ? 10.702  -14.071 3.581   1.00 15.02 ? 224 LEU A CA  1 
ATOM   1794 C  C   . LEU A 1 223 ? 11.054  -12.963 2.616   1.00 15.71 ? 224 LEU A C   1 
ATOM   1795 O  O   . LEU A 1 223 ? 12.226  -12.824 2.259   1.00 15.49 ? 224 LEU A O   1 
ATOM   1796 C  CB  . LEU A 1 223 ? 10.243  -15.347 2.852   1.00 16.94 ? 224 LEU A CB  1 
ATOM   1797 C  CG  . LEU A 1 223 ? 10.449  -16.611 3.679   1.00 19.20 ? 224 LEU A CG  1 
ATOM   1798 C  CD1 . LEU A 1 223 ? 9.536   -17.778 3.197   1.00 22.80 ? 224 LEU A CD1 1 
ATOM   1799 C  CD2 . LEU A 1 223 ? 11.935  -16.975 3.630   1.00 21.30 ? 224 LEU A CD2 1 
ATOM   1800 N  N   . LYS A 1 224 ? 10.066  -12.165 2.236   1.00 13.19 ? 225 LYS A N   1 
ATOM   1801 C  CA  . LYS A 1 224 ? 10.297  -11.005 1.401   1.00 15.80 ? 225 LYS A CA  1 
ATOM   1802 C  C   . LYS A 1 224 ? 11.191  -9.906  2.078   1.00 14.60 ? 225 LYS A C   1 
ATOM   1803 O  O   . LYS A 1 224 ? 12.044  -9.297  1.409   1.00 15.59 ? 225 LYS A O   1 
ATOM   1804 C  CB  . LYS A 1 224 ? 8.954   -10.523 0.819   1.00 17.88 ? 225 LYS A CB  1 
ATOM   1805 C  CG  . LYS A 1 224 ? 8.347   -11.612 -0.107  1.00 20.38 ? 225 LYS A CG  1 
ATOM   1806 C  CD  . LYS A 1 224 ? 7.058   -11.183 -0.787  1.00 25.76 ? 225 LYS A CD  1 
ATOM   1807 C  CE  . LYS A 1 224 ? 6.554   -12.340 -1.683  1.00 26.79 ? 225 LYS A CE  1 
ATOM   1808 N  NZ  . LYS A 1 224 ? 5.325   -12.035 -2.498  1.00 30.66 ? 225 LYS A NZ  1 
ATOM   1809 N  N   . PHE A 1 225 ? 11.043  -9.678  3.401   1.00 13.45 ? 226 PHE A N   1 
ATOM   1810 C  CA  . PHE A 1 225 ? 11.995  -8.806  4.116   1.00 12.45 ? 226 PHE A CA  1 
ATOM   1811 C  C   . PHE A 1 225 ? 13.417  -9.303  3.920   1.00 11.47 ? 226 PHE A C   1 
ATOM   1812 O  O   . PHE A 1 225 ? 14.352  -8.519  3.731   1.00 12.86 ? 226 PHE A O   1 
ATOM   1813 C  CB  . PHE A 1 225 ? 11.802  -8.888  5.650   1.00 13.09 ? 226 PHE A CB  1 
ATOM   1814 C  CG  . PHE A 1 225 ? 10.590  -8.145  6.193   1.00 14.46 ? 226 PHE A CG  1 
ATOM   1815 C  CD1 . PHE A 1 225 ? 9.508   -7.740  5.401   1.00 14.81 ? 226 PHE A CD1 1 
ATOM   1816 C  CD2 . PHE A 1 225 ? 10.554  -7.917  7.595   1.00 15.38 ? 226 PHE A CD2 1 
ATOM   1817 C  CE1 . PHE A 1 225 ? 8.448   -7.050  5.967   1.00 15.72 ? 226 PHE A CE1 1 
ATOM   1818 C  CE2 . PHE A 1 225 ? 9.490   -7.274  8.177   1.00 16.07 ? 226 PHE A CE2 1 
ATOM   1819 C  CZ  . PHE A 1 225 ? 8.445   -6.811  7.352   1.00 17.23 ? 226 PHE A CZ  1 
ATOM   1820 N  N   . ARG A 1 226 ? 13.622  -10.607 4.027   1.00 10.98 ? 227 ARG A N   1 
ATOM   1821 C  CA  . ARG A 1 226 ? 14.950  -11.242 3.900   1.00 12.81 ? 227 ARG A CA  1 
ATOM   1822 C  C   . ARG A 1 226 ? 15.536  -11.238 2.494   1.00 13.94 ? 227 ARG A C   1 
ATOM   1823 O  O   . ARG A 1 226 ? 16.681  -11.647 2.314   1.00 15.33 ? 227 ARG A O   1 
ATOM   1824 C  CB  . ARG A 1 226 ? 14.859  -12.708 4.383   1.00 11.98 ? 227 ARG A CB  1 
ATOM   1825 C  CG  . ARG A 1 226 ? 14.448  -12.826 5.835   1.00 12.24 ? 227 ARG A CG  1 
ATOM   1826 C  CD  . ARG A 1 226 ? 14.563  -14.276 6.364   1.00 12.63 ? 227 ARG A CD  1 
ATOM   1827 N  NE  . ARG A 1 226 ? 13.998  -14.336 7.729   1.00 12.75 ? 227 ARG A NE  1 
ATOM   1828 C  CZ  . ARG A 1 226 ? 13.008  -15.159 8.062   1.00 13.55 ? 227 ARG A CZ  1 
ATOM   1829 N  NH1 . ARG A 1 226 ? 12.592  -16.114 7.166   1.00 14.60 ? 227 ARG A NH1 1 
ATOM   1830 N  NH2 . ARG A 1 226 ? 12.506  -15.129 9.286   1.00 13.61 ? 227 ARG A NH2 1 
ATOM   1831 N  N   . LYS A 1 227 ? 14.782  -10.764 1.498   1.00 15.69 ? 228 LYS A N   1 
ATOM   1832 C  CA  . LYS A 1 227 ? 15.339  -10.635 0.131   1.00 15.46 ? 228 LYS A CA  1 
ATOM   1833 C  C   . LYS A 1 227 ? 15.951  -9.277  -0.124  1.00 15.21 ? 228 LYS A C   1 
ATOM   1834 O  O   . LYS A 1 227 ? 16.586  -9.066  -1.140  1.00 15.07 ? 228 LYS A O   1 
ATOM   1835 C  CB  . LYS A 1 227 ? 14.260  -10.899 -0.929  1.00 15.52 ? 228 LYS A CB  1 
ATOM   1836 C  CG  . LYS A 1 227 ? 13.927  -12.380 -1.070  1.00 20.46 ? 228 LYS A CG  1 
ATOM   1837 C  CD  . LYS A 1 227 ? 12.672  -12.505 -1.936  1.00 25.67 ? 228 LYS A CD  1 
ATOM   1838 C  CE  . LYS A 1 227 ? 13.105  -12.511 -3.404  1.00 27.55 ? 228 LYS A CE  1 
ATOM   1839 N  NZ  . LYS A 1 227 ? 12.050  -12.853 -4.412  1.00 33.67 ? 228 LYS A NZ  1 
ATOM   1840 N  N   . LEU A 1 228 ? 15.803  -8.360  0.833   1.00 13.88 ? 229 LEU A N   1 
ATOM   1841 C  CA  . LEU A 1 228 ? 16.434  -7.068  0.710   1.00 14.18 ? 229 LEU A CA  1 
ATOM   1842 C  C   . LEU A 1 228 ? 17.946  -7.241  0.864   1.00 13.90 ? 229 LEU A C   1 
ATOM   1843 O  O   . LEU A 1 228 ? 18.459  -8.293  1.310   1.00 12.64 ? 229 LEU A O   1 
ATOM   1844 C  CB  . LEU A 1 228 ? 15.878  -6.139  1.815   1.00 11.46 ? 229 LEU A CB  1 
ATOM   1845 C  CG  . LEU A 1 228 ? 14.473  -5.631  1.594   1.00 11.51 ? 229 LEU A CG  1 
ATOM   1846 C  CD1 . LEU A 1 228 ? 13.960  -4.966  2.856   1.00 12.27 ? 229 LEU A CD1 1 
ATOM   1847 C  CD2 . LEU A 1 228 ? 14.445  -4.581  0.489   1.00 11.74 ? 229 LEU A CD2 1 
ATOM   1848 N  N   . ASN A 1 229 ? 18.672  -6.191  0.497   1.00 14.88 ? 230 ASN A N   1 
ATOM   1849 C  CA  . ASN A 1 229 ? 20.127  -6.228  0.498   1.00 15.36 ? 230 ASN A CA  1 
ATOM   1850 C  C   . ASN A 1 229 ? 20.630  -5.053  1.364   1.00 15.28 ? 230 ASN A C   1 
ATOM   1851 O  O   . ASN A 1 229 ? 20.106  -3.947  1.247   1.00 14.62 ? 230 ASN A O   1 
ATOM   1852 C  CB  . ASN A 1 229 ? 20.634  -5.948  -0.929  1.00 16.96 ? 230 ASN A CB  1 
ATOM   1853 C  CG  . ASN A 1 229 ? 20.584  -7.161  -1.863  1.00 18.61 ? 230 ASN A CG  1 
ATOM   1854 O  OD1 . ASN A 1 229 ? 21.151  -7.077  -2.986  1.00 19.53 ? 230 ASN A OD1 1 
ATOM   1855 N  ND2 . ASN A 1 229 ? 19.912  -8.255  -1.466  1.00 17.70 ? 230 ASN A ND2 1 
ATOM   1856 N  N   . PHE A 1 230 ? 21.699  -5.287  2.131   1.00 15.44 ? 231 PHE A N   1 
ATOM   1857 C  CA  . PHE A 1 230 ? 22.459  -4.236  2.867   1.00 15.47 ? 231 PHE A CA  1 
ATOM   1858 C  C   . PHE A 1 230 ? 23.348  -3.420  1.903   1.00 18.38 ? 231 PHE A C   1 
ATOM   1859 O  O   . PHE A 1 230 ? 23.595  -2.246  2.131   1.00 17.14 ? 231 PHE A O   1 
ATOM   1860 C  CB  . PHE A 1 230 ? 23.464  -4.897  3.737   1.00 15.48 ? 231 PHE A CB  1 
ATOM   1861 C  CG  . PHE A 1 230 ? 22.914  -5.487  5.054   1.00 14.80 ? 231 PHE A CG  1 
ATOM   1862 C  CD1 . PHE A 1 230 ? 22.181  -4.677  5.937   1.00 15.00 ? 231 PHE A CD1 1 
ATOM   1863 C  CD2 . PHE A 1 230 ? 23.207  -6.779  5.414   1.00 15.34 ? 231 PHE A CD2 1 
ATOM   1864 C  CE1 . PHE A 1 230 ? 21.726  -5.174  7.171   1.00 15.68 ? 231 PHE A CE1 1 
ATOM   1865 C  CE2 . PHE A 1 230 ? 22.758  -7.299  6.636   1.00 15.85 ? 231 PHE A CE2 1 
ATOM   1866 C  CZ  . PHE A 1 230 ? 22.015  -6.500  7.514   1.00 13.85 ? 231 PHE A CZ  1 
ATOM   1867 N  N   . ASN A 1 231 ? 23.872  -4.107  0.887   1.00 19.69 ? 232 ASN A N   1 
ATOM   1868 C  CA  . ASN A 1 231 ? 24.742  -3.480  -0.122  1.00 19.92 ? 232 ASN A CA  1 
ATOM   1869 C  C   . ASN A 1 231 ? 23.997  -2.594  -1.097  1.00 20.82 ? 232 ASN A C   1 
ATOM   1870 O  O   . ASN A 1 231 ? 22.814  -2.757  -1.248  1.00 19.88 ? 232 ASN A O   1 
ATOM   1871 C  CB  . ASN A 1 231 ? 25.418  -4.598  -0.906  1.00 18.84 ? 232 ASN A CB  1 
ATOM   1872 C  CG  . ASN A 1 231 ? 24.429  -5.515  -1.561  1.00 18.70 ? 232 ASN A CG  1 
ATOM   1873 O  OD1 . ASN A 1 231 ? 23.902  -6.465  -0.919  1.00 20.14 ? 232 ASN A OD1 1 
ATOM   1874 N  ND2 . ASN A 1 231 ? 24.225  -5.325  -2.887  1.00 20.37 ? 232 ASN A ND2 1 
ATOM   1875 N  N   . GLY A 1 232 ? 24.702  -1.666  -1.767  1.00 21.52 ? 233 GLY A N   1 
ATOM   1876 C  CA  . GLY A 1 232 ? 24.130  -0.907  -2.892  1.00 21.23 ? 233 GLY A CA  1 
ATOM   1877 C  C   . GLY A 1 232 ? 24.177  -1.693  -4.190  1.00 23.59 ? 233 GLY A C   1 
ATOM   1878 O  O   . GLY A 1 232 ? 24.903  -2.698  -4.304  1.00 22.89 ? 233 GLY A O   1 
ATOM   1879 N  N   . GLU A 1 233 ? 23.414  -1.197  -5.168  1.00 23.57 ? 234 GLU A N   1 
ATOM   1880 C  CA  . GLU A 1 233 ? 23.297  -1.795  -6.486  1.00 25.41 ? 234 GLU A CA  1 
ATOM   1881 C  C   . GLU A 1 233 ? 24.672  -1.878  -7.113  1.00 25.26 ? 234 GLU A C   1 
ATOM   1882 O  O   . GLU A 1 233 ? 25.388  -0.893  -7.135  1.00 22.92 ? 234 GLU A O   1 
ATOM   1883 C  CB  . GLU A 1 233 ? 22.392  -0.956  -7.382  1.00 25.65 ? 234 GLU A CB  1 
ATOM   1884 C  CG  . GLU A 1 233 ? 22.133  -1.519  -8.782  1.00 28.23 ? 234 GLU A CG  1 
ATOM   1885 C  CD  . GLU A 1 233 ? 21.269  -0.615  -9.622  1.00 32.09 ? 234 GLU A CD  1 
ATOM   1886 O  OE1 . GLU A 1 233 ? 21.059  0.589   -9.253  1.00 33.20 ? 234 GLU A OE1 1 
ATOM   1887 O  OE2 . GLU A 1 233 ? 20.796  -1.093  -10.671 1.00 33.67 ? 234 GLU A OE2 1 
ATOM   1888 N  N   . GLY A 1 234 ? 24.997  -3.056  -7.625  1.00 28.22 ? 235 GLY A N   1 
ATOM   1889 C  CA  . GLY A 1 234 ? 26.291  -3.304  -8.232  1.00 31.57 ? 235 GLY A CA  1 
ATOM   1890 C  C   . GLY A 1 234 ? 27.388  -3.834  -7.349  1.00 34.63 ? 235 GLY A C   1 
ATOM   1891 O  O   . GLY A 1 234 ? 28.500  -4.081  -7.839  1.00 34.59 ? 235 GLY A O   1 
ATOM   1892 N  N   . GLU A 1 235 ? 27.084  -4.042  -6.061  1.00 28.98 ? 236 GLU A N   1 
ATOM   1893 C  CA  . GLU A 1 235 ? 28.020  -4.637  -5.127  1.00 28.50 ? 236 GLU A CA  1 
ATOM   1894 C  C   . GLU A 1 235 ? 27.607  -6.068  -4.859  1.00 28.37 ? 236 GLU A C   1 
ATOM   1895 O  O   . GLU A 1 235 ? 26.493  -6.468  -5.236  1.00 28.37 ? 236 GLU A O   1 
ATOM   1896 C  CB  . GLU A 1 235 ? 28.092  -3.811  -3.830  1.00 31.75 ? 236 GLU A CB  1 
ATOM   1897 C  CG  . GLU A 1 235 ? 28.466  -2.373  -4.118  1.00 34.26 ? 236 GLU A CG  1 
ATOM   1898 C  CD  . GLU A 1 235 ? 28.144  -1.412  -2.996  1.00 40.80 ? 236 GLU A CD  1 
ATOM   1899 O  OE1 . GLU A 1 235 ? 27.580  -1.828  -1.954  1.00 44.24 ? 236 GLU A OE1 1 
ATOM   1900 O  OE2 . GLU A 1 235 ? 28.455  -0.215  -3.159  1.00 45.49 ? 236 GLU A OE2 1 
ATOM   1901 N  N   . PRO A 1 236 ? 28.525  -6.864  -4.299  1.00 25.78 ? 237 PRO A N   1 
ATOM   1902 C  CA  . PRO A 1 236 ? 28.292  -8.258  -3.935  1.00 27.15 ? 237 PRO A CA  1 
ATOM   1903 C  C   . PRO A 1 236 ? 27.086  -8.302  -2.991  1.00 27.16 ? 237 PRO A C   1 
ATOM   1904 O  O   . PRO A 1 236 ? 26.930  -7.416  -2.132  1.00 25.95 ? 237 PRO A O   1 
ATOM   1905 C  CB  . PRO A 1 236 ? 29.573  -8.657  -3.217  1.00 27.29 ? 237 PRO A CB  1 
ATOM   1906 C  CG  . PRO A 1 236 ? 30.620  -7.740  -3.783  1.00 27.49 ? 237 PRO A CG  1 
ATOM   1907 C  CD  . PRO A 1 236 ? 29.924  -6.448  -4.060  1.00 29.05 ? 237 PRO A CD  1 
ATOM   1908 N  N   . GLU A 1 237 ? 26.204  -9.265  -3.231  1.00 23.46 ? 238 GLU A N   1 
ATOM   1909 C  CA  . GLU A 1 237 ? 24.945  -9.291  -2.525  1.00 21.96 ? 238 GLU A CA  1 
ATOM   1910 C  C   . GLU A 1 237 ? 25.153  -9.768  -1.093  1.00 21.06 ? 238 GLU A C   1 
ATOM   1911 O  O   . GLU A 1 237 ? 25.728  -10.825 -0.859  1.00 20.32 ? 238 GLU A O   1 
ATOM   1912 C  CB  . GLU A 1 237 ? 23.888  -10.131 -3.272  1.00 21.75 ? 238 GLU A CB  1 
ATOM   1913 C  CG  . GLU A 1 237 ? 22.572  -10.192 -2.490  1.00 22.31 ? 238 GLU A CG  1 
ATOM   1914 C  CD  . GLU A 1 237 ? 21.489  -10.982 -3.187  1.00 24.60 ? 238 GLU A CD  1 
ATOM   1915 O  OE1 . GLU A 1 237 ? 21.837  -12.048 -3.755  1.00 31.08 ? 238 GLU A OE1 1 
ATOM   1916 O  OE2 . GLU A 1 237 ? 20.301  -10.569 -3.190  1.00 21.12 ? 238 GLU A OE2 1 
ATOM   1917 N  N   . GLU A 1 238 ? 24.684  -8.964  -0.131  1.00 18.80 ? 239 GLU A N   1 
ATOM   1918 C  CA  . GLU A 1 238 ? 24.734  -9.333  1.292   1.00 21.76 ? 239 GLU A CA  1 
ATOM   1919 C  C   . GLU A 1 238 ? 23.283  -9.219  1.704   1.00 17.09 ? 239 GLU A C   1 
ATOM   1920 O  O   . GLU A 1 238 ? 22.755  -8.136  1.667   1.00 17.17 ? 239 GLU A O   1 
ATOM   1921 C  CB  . GLU A 1 238 ? 25.514  -8.334  2.174   1.00 23.49 ? 239 GLU A CB  1 
ATOM   1922 C  CG  . GLU A 1 238 ? 26.535  -7.446  1.472   1.00 33.97 ? 239 GLU A CG  1 
ATOM   1923 C  CD  . GLU A 1 238 ? 27.516  -6.724  2.427   1.00 40.14 ? 239 GLU A CD  1 
ATOM   1924 O  OE1 . GLU A 1 238 ? 27.093  -6.054  3.427   1.00 39.60 ? 239 GLU A OE1 1 
ATOM   1925 O  OE2 . GLU A 1 238 ? 28.749  -6.855  2.175   1.00 41.31 ? 239 GLU A OE2 1 
ATOM   1926 N  N   . LEU A 1 239 ? 22.610  -10.328 1.983   1.00 14.88 ? 240 LEU A N   1 
ATOM   1927 C  CA  . LEU A 1 239 ? 21.154  -10.236 2.302   1.00 13.80 ? 240 LEU A CA  1 
ATOM   1928 C  C   . LEU A 1 239 ? 20.955  -9.393  3.585   1.00 13.50 ? 240 LEU A C   1 
ATOM   1929 O  O   . LEU A 1 239 ? 21.712  -9.553  4.552   1.00 14.65 ? 240 LEU A O   1 
ATOM   1930 C  CB  . LEU A 1 239 ? 20.566  -11.633 2.561   1.00 14.35 ? 240 LEU A CB  1 
ATOM   1931 C  CG  . LEU A 1 239 ? 20.527  -12.503 1.290   1.00 14.84 ? 240 LEU A CG  1 
ATOM   1932 C  CD1 . LEU A 1 239 ? 20.004  -13.893 1.626   1.00 16.79 ? 240 LEU A CD1 1 
ATOM   1933 C  CD2 . LEU A 1 239 ? 19.772  -11.816 0.185   1.00 16.44 ? 240 LEU A CD2 1 
ATOM   1934 N  N   . MET A 1 240 ? 19.898  -8.576  3.584   1.00 13.23 ? 241 MET A N   1 
ATOM   1935 C  CA  . MET A 1 240 ? 19.514  -7.764  4.780   1.00 12.19 ? 241 MET A CA  1 
ATOM   1936 C  C   . MET A 1 240 ? 18.763  -8.705  5.736   1.00 11.24 ? 241 MET A C   1 
ATOM   1937 O  O   . MET A 1 240 ? 17.561  -8.860  5.637   1.00 11.39 ? 241 MET A O   1 
ATOM   1938 C  CB  . MET A 1 240 ? 18.666  -6.541  4.429   1.00 14.46 ? 241 MET A CB  1 
ATOM   1939 C  CG  . MET A 1 240 ? 18.431  -5.577  5.656   1.00 14.03 ? 241 MET A CG  1 
ATOM   1940 S  SD  . MET A 1 240 ? 17.493  -4.202  5.101   1.00 16.12 ? 241 MET A SD  1 
ATOM   1941 C  CE  . MET A 1 240 ? 18.806  -3.133  4.490   1.00 16.02 ? 241 MET A CE  1 
ATOM   1942 N  N   . VAL A 1 241 ? 19.517  -9.272  6.657   1.00 11.58 ? 242 VAL A N   1 
ATOM   1943 C  CA  . VAL A 1 241 ? 18.960  -10.148 7.703   1.00 11.25 ? 242 VAL A CA  1 
ATOM   1944 C  C   . VAL A 1 241 ? 19.760  -9.898  8.957   1.00 11.54 ? 242 VAL A C   1 
ATOM   1945 O  O   . VAL A 1 241 ? 20.961  -9.586  8.893   1.00 12.08 ? 242 VAL A O   1 
ATOM   1946 C  CB  . VAL A 1 241 ? 19.016  -11.670 7.338   1.00 10.66 ? 242 VAL A CB  1 
ATOM   1947 C  CG1 . VAL A 1 241 ? 18.068  -11.918 6.135   1.00 11.97 ? 242 VAL A CG1 1 
ATOM   1948 C  CG2 . VAL A 1 241 ? 20.452  -12.181 7.146   1.00 11.92 ? 242 VAL A CG2 1 
ATOM   1949 N  N   . ASP A 1 242 ? 19.135  -10.209 10.100  1.00 10.13 ? 243 ASP A N   1 
ATOM   1950 C  CA  . ASP A 1 242 ? 19.807  -10.086 11.399  1.00 10.00 ? 243 ASP A CA  1 
ATOM   1951 C  C   . ASP A 1 242 ? 20.285  -8.657  11.649  1.00 9.89  ? 243 ASP A C   1 
ATOM   1952 O  O   . ASP A 1 242 ? 21.406  -8.478  12.130  1.00 10.16 ? 243 ASP A O   1 
ATOM   1953 C  CB  . ASP A 1 242 ? 20.899  -11.123 11.700  1.00 9.65  ? 243 ASP A CB  1 
ATOM   1954 C  CG  . ASP A 1 242 ? 20.375  -12.544 11.692  1.00 10.23 ? 243 ASP A CG  1 
ATOM   1955 O  OD1 . ASP A 1 242 ? 19.317  -12.777 12.285  1.00 10.47 ? 243 ASP A OD1 1 
ATOM   1956 O  OD2 . ASP A 1 242 ? 20.999  -13.443 11.053  1.00 10.67 ? 243 ASP A OD2 1 
ATOM   1957 N  N   . ASN A 1 243 ? 19.412  -7.694  11.355  1.00 9.68  ? 244 ASN A N   1 
ATOM   1958 C  CA  . ASN A 1 243 ? 19.769  -6.248  11.599  1.00 8.99  ? 244 ASN A CA  1 
ATOM   1959 C  C   . ASN A 1 243 ? 19.146  -5.853  12.964  1.00 9.57  ? 244 ASN A C   1 
ATOM   1960 O  O   . ASN A 1 243 ? 18.504  -4.813  13.075  1.00 9.15  ? 244 ASN A O   1 
ATOM   1961 C  CB  . ASN A 1 243 ? 19.288  -5.342  10.468  1.00 11.18 ? 244 ASN A CB  1 
ATOM   1962 C  CG  . ASN A 1 243 ? 17.807  -5.566  10.165  1.00 11.56 ? 244 ASN A CG  1 
ATOM   1963 O  OD1 . ASN A 1 243 ? 17.174  -6.480  10.764  1.00 12.01 ? 244 ASN A OD1 1 
ATOM   1964 N  ND2 . ASN A 1 243 ? 17.251  -4.796  9.246   1.00 12.53 ? 244 ASN A ND2 1 
ATOM   1965 N  N   . TRP A 1 244 ? 19.441  -6.685  13.968  1.00 9.23  ? 245 TRP A N   1 
ATOM   1966 C  CA  . TRP A 1 244 ? 18.990  -6.445  15.336  1.00 9.08  ? 245 TRP A CA  1 
ATOM   1967 C  C   . TRP A 1 244 ? 20.164  -6.344  16.262  1.00 9.25  ? 245 TRP A C   1 
ATOM   1968 O  O   . TRP A 1 244 ? 21.182  -7.049  16.105  1.00 10.05 ? 245 TRP A O   1 
ATOM   1969 C  CB  . TRP A 1 244 ? 17.994  -7.511  15.816  1.00 8.69  ? 245 TRP A CB  1 
ATOM   1970 C  CG  . TRP A 1 244 ? 18.469  -8.922  15.647  1.00 9.00  ? 245 TRP A CG  1 
ATOM   1971 C  CD1 . TRP A 1 244 ? 18.380  -9.670  14.519  1.00 9.07  ? 245 TRP A CD1 1 
ATOM   1972 C  CD2 . TRP A 1 244 ? 19.081  -9.790  16.662  1.00 8.71  ? 245 TRP A CD2 1 
ATOM   1973 N  NE1 . TRP A 1 244 ? 18.909  -10.936 14.732  1.00 9.21  ? 245 TRP A NE1 1 
ATOM   1974 C  CE2 . TRP A 1 244 ? 19.319  -11.064 16.007  1.00 9.46  ? 245 TRP A CE2 1 
ATOM   1975 C  CE3 . TRP A 1 244 ? 19.388  -9.652  18.000  1.00 9.30  ? 245 TRP A CE3 1 
ATOM   1976 C  CZ2 . TRP A 1 244 ? 19.901  -12.138 16.665  1.00 9.31  ? 245 TRP A CZ2 1 
ATOM   1977 C  CZ3 . TRP A 1 244 ? 20.006  -10.750 18.670  1.00 8.85  ? 245 TRP A CZ3 1 
ATOM   1978 C  CH2 . TRP A 1 244 ? 20.252  -11.950 18.002  1.00 10.13 ? 245 TRP A CH2 1 
ATOM   1979 N  N   . ARG A 1 245 ? 20.061  -5.457  17.265  1.00 8.93  ? 246 ARG A N   1 
ATOM   1980 C  CA  . ARG A 1 245 ? 21.049  -5.370  18.353  1.00 9.58  ? 246 ARG A CA  1 
ATOM   1981 C  C   . ARG A 1 245 ? 20.560  -6.293  19.489  1.00 9.45  ? 246 ARG A C   1 
ATOM   1982 O  O   . ARG A 1 245 ? 19.345  -6.296  19.797  1.00 11.03 ? 246 ARG A O   1 
ATOM   1983 C  CB  . ARG A 1 245 ? 21.139  -3.876  18.836  1.00 8.92  ? 246 ARG A CB  1 
ATOM   1984 C  CG  . ARG A 1 245 ? 22.272  -3.685  19.832  1.00 9.01  ? 246 ARG A CG  1 
ATOM   1985 C  CD  . ARG A 1 245 ? 22.138  -2.325  20.558  1.00 9.13  ? 246 ARG A CD  1 
ATOM   1986 N  NE  . ARG A 1 245 ? 23.446  -2.026  21.224  1.00 9.41  ? 246 ARG A NE  1 
ATOM   1987 C  CZ  . ARG A 1 245 ? 23.667  -1.003  22.029  1.00 10.91 ? 246 ARG A CZ  1 
ATOM   1988 N  NH1 . ARG A 1 245 ? 22.630  -0.227  22.391  1.00 9.52  ? 246 ARG A NH1 1 
ATOM   1989 N  NH2 . ARG A 1 245 ? 24.901  -0.784  22.483  1.00 9.49  ? 246 ARG A NH2 1 
ATOM   1990 N  N   . PRO A 1 246 ? 21.439  -7.106  20.107  1.00 10.99 ? 247 PRO A N   1 
ATOM   1991 C  CA  . PRO A 1 246 ? 21.087  -7.946  21.228  1.00 10.41 ? 247 PRO A CA  1 
ATOM   1992 C  C   . PRO A 1 246 ? 20.766  -7.102  22.451  1.00 10.01 ? 247 PRO A C   1 
ATOM   1993 O  O   . PRO A 1 246 ? 21.115  -5.918  22.566  1.00 10.19 ? 247 PRO A O   1 
ATOM   1994 C  CB  . PRO A 1 246 ? 22.387  -8.796  21.515  1.00 12.26 ? 247 PRO A CB  1 
ATOM   1995 C  CG  . PRO A 1 246 ? 23.222  -8.528  20.303  1.00 14.22 ? 247 PRO A CG  1 
ATOM   1996 C  CD  . PRO A 1 246 ? 22.890  -7.146  19.869  1.00 11.07 ? 247 PRO A CD  1 
ATOM   1997 N  N   . ALA A 1 247 ? 20.049  -7.754  23.352  1.00 9.51  ? 248 ALA A N   1 
ATOM   1998 C  CA  . ALA A 1 247 ? 19.745  -7.168  24.641  1.00 8.75  ? 248 ALA A CA  1 
ATOM   1999 C  C   . ALA A 1 247 ? 20.928  -6.620  25.389  1.00 9.84  ? 248 ALA A C   1 
ATOM   2000 O  O   . ALA A 1 247 ? 21.984  -7.267  25.470  1.00 8.45  ? 248 ALA A O   1 
ATOM   2001 C  CB  . ALA A 1 247 ? 18.950  -8.204  25.495  1.00 10.04 ? 248 ALA A CB  1 
ATOM   2002 N  N   . GLN A 1 248 ? 20.737  -5.435  25.971  1.00 9.01  ? 249 GLN A N   1 
ATOM   2003 C  CA  . GLN A 1 248 ? 21.792  -4.685  26.706  1.00 9.66  ? 249 GLN A CA  1 
ATOM   2004 C  C   . GLN A 1 248 ? 21.510  -4.685  28.210  1.00 10.75 ? 249 GLN A C   1 
ATOM   2005 O  O   . GLN A 1 248 ? 20.341  -4.848  28.642  1.00 10.35 ? 249 GLN A O   1 
ATOM   2006 C  CB  . GLN A 1 248 ? 21.831  -3.265  26.171  1.00 9.62  ? 249 GLN A CB  1 
ATOM   2007 C  CG  . GLN A 1 248 ? 22.185  -3.194  24.663  1.00 9.74  ? 249 GLN A CG  1 
ATOM   2008 C  CD  . GLN A 1 248 ? 23.510  -3.846  24.323  1.00 10.47 ? 249 GLN A CD  1 
ATOM   2009 O  OE1 . GLN A 1 248 ? 24.574  -3.491  24.902  1.00 11.87 ? 249 GLN A OE1 1 
ATOM   2010 N  NE2 . GLN A 1 248 ? 23.465  -4.878  23.456  1.00 11.71 ? 249 GLN A NE2 1 
ATOM   2011 N  N   . PRO A 1 249 ? 22.534  -4.376  29.047  1.00 12.06 ? 250 PRO A N   1 
ATOM   2012 C  CA  . PRO A 1 249 ? 22.319  -4.448  30.485  1.00 12.68 ? 250 PRO A CA  1 
ATOM   2013 C  C   . PRO A 1 249 ? 21.240  -3.438  30.972  1.00 12.41 ? 250 PRO A C   1 
ATOM   2014 O  O   . PRO A 1 249 ? 21.257  -2.269  30.552  1.00 13.73 ? 250 PRO A O   1 
ATOM   2015 C  CB  . PRO A 1 249 ? 23.670  -3.957  31.035  1.00 13.81 ? 250 PRO A CB  1 
ATOM   2016 C  CG  . PRO A 1 249 ? 24.614  -4.508  30.062  1.00 15.35 ? 250 PRO A CG  1 
ATOM   2017 C  CD  . PRO A 1 249 ? 23.953  -4.139  28.740  1.00 13.23 ? 250 PRO A CD  1 
ATOM   2018 N  N   . LEU A 1 250 ? 20.345  -3.918  31.851  1.00 13.03 ? 251 LEU A N   1 
ATOM   2019 C  CA  . LEU A 1 250 ? 19.225  -3.072  32.310  1.00 12.10 ? 251 LEU A CA  1 
ATOM   2020 C  C   . LEU A 1 250 ? 19.836  -1.981  33.214  1.00 12.98 ? 251 LEU A C   1 
ATOM   2021 O  O   . LEU A 1 250 ? 19.365  -0.827  33.233  1.00 10.24 ? 251 LEU A O   1 
ATOM   2022 C  CB  . LEU A 1 250 ? 18.095  -3.882  32.979  1.00 14.05 ? 251 LEU A CB  1 
ATOM   2023 C  CG  . LEU A 1 250 ? 16.865  -3.107  33.452  1.00 12.52 ? 251 LEU A CG  1 
ATOM   2024 C  CD1 . LEU A 1 250 ? 16.109  -2.485  32.271  1.00 13.66 ? 251 LEU A CD1 1 
ATOM   2025 C  CD2 . LEU A 1 250 ? 15.976  -4.102  34.223  1.00 15.53 ? 251 LEU A CD2 1 
ATOM   2026 N  N   . LYS A 1 251 ? 20.924  -2.323  33.934  1.00 13.86 ? 252 LYS A N   1 
ATOM   2027 C  CA  . LYS A 1 251 ? 21.541  -1.296  34.857  1.00 15.78 ? 252 LYS A CA  1 
ATOM   2028 C  C   . LYS A 1 251 ? 20.519  -0.751  35.832  1.00 16.24 ? 252 LYS A C   1 
ATOM   2029 O  O   . LYS A 1 251 ? 19.732  -1.528  36.367  1.00 17.00 ? 252 LYS A O   1 
ATOM   2030 C  CB  . LYS A 1 251 ? 22.294  -0.248  34.086  1.00 18.10 ? 252 LYS A CB  1 
ATOM   2031 C  CG  . LYS A 1 251 ? 23.630  -0.928  33.699  1.00 19.02 ? 252 LYS A CG  1 
ATOM   2032 C  CD  . LYS A 1 251 ? 24.319  -0.144  32.650  1.00 20.59 ? 252 LYS A CD  1 
ATOM   2033 C  CE  . LYS A 1 251 ? 25.747  -0.647  32.476  1.00 24.34 ? 252 LYS A CE  1 
ATOM   2034 N  NZ  . LYS A 1 251 ? 26.250  0.083   31.286  1.00 25.06 ? 252 LYS A NZ  1 
ATOM   2035 N  N   . ASN A 1 252 ? 20.495  0.559   36.049  1.00 17.74 ? 253 ASN A N   1 
ATOM   2036 C  CA  . ASN A 1 252 ? 19.685  1.039   37.127  1.00 24.81 ? 253 ASN A CA  1 
ATOM   2037 C  C   . ASN A 1 252 ? 18.358  1.555   36.550  1.00 23.62 ? 253 ASN A C   1 
ATOM   2038 O  O   . ASN A 1 252 ? 18.156  2.813   36.554  1.00 23.98 ? 253 ASN A O   1 
ATOM   2039 C  CB  . ASN A 1 252 ? 20.445  2.136   37.924  1.00 31.81 ? 253 ASN A CB  1 
ATOM   2040 C  CG  . ASN A 1 252 ? 19.681  2.596   39.153  1.00 34.08 ? 253 ASN A CG  1 
ATOM   2041 O  OD1 . ASN A 1 252 ? 19.005  1.799   39.816  1.00 40.80 ? 253 ASN A OD1 1 
ATOM   2042 N  ND2 . ASN A 1 252 ? 19.751  3.886   39.440  1.00 37.67 ? 253 ASN A ND2 1 
ATOM   2043 N  N   . ARG A 1 253 ? 17.542  0.609   36.001  1.00 15.98 ? 254 ARG A N   1 
ATOM   2044 C  CA  . ARG A 1 253 ? 16.262  0.944   35.370  1.00 15.18 ? 254 ARG A CA  1 
ATOM   2045 C  C   . ARG A 1 253 ? 15.168  -0.025  35.790  1.00 15.48 ? 254 ARG A C   1 
ATOM   2046 O  O   . ARG A 1 253 ? 15.453  -1.188  36.066  1.00 16.98 ? 254 ARG A O   1 
ATOM   2047 C  CB  . ARG A 1 253 ? 16.357  0.990   33.813  1.00 13.69 ? 254 ARG A CB  1 
ATOM   2048 C  CG  . ARG A 1 253 ? 17.263  2.104   33.317  1.00 14.32 ? 254 ARG A CG  1 
ATOM   2049 C  CD  . ARG A 1 253 ? 17.345  2.072   31.799  1.00 12.08 ? 254 ARG A CD  1 
ATOM   2050 N  NE  . ARG A 1 253 ? 18.202  0.951   31.354  1.00 12.47 ? 254 ARG A NE  1 
ATOM   2051 C  CZ  . ARG A 1 253 ? 18.410  0.637   30.084  1.00 10.30 ? 254 ARG A CZ  1 
ATOM   2052 N  NH1 . ARG A 1 253 ? 17.765  1.337   29.124  1.00 9.10  ? 254 ARG A NH1 1 
ATOM   2053 N  NH2 . ARG A 1 253 ? 19.240  -0.374  29.763  1.00 9.99  ? 254 ARG A NH2 1 
ATOM   2054 N  N   . GLN A 1 254 ? 13.940  0.490   35.850  1.00 14.38 ? 255 GLN A N   1 
ATOM   2055 C  CA  . GLN A 1 254 ? 12.756  -0.262  36.208  1.00 16.35 ? 255 GLN A CA  1 
ATOM   2056 C  C   . GLN A 1 254 ? 11.896  -0.360  34.938  1.00 15.70 ? 255 GLN A C   1 
ATOM   2057 O  O   . GLN A 1 254 ? 11.633  0.694   34.314  1.00 15.61 ? 255 GLN A O   1 
ATOM   2058 C  CB  . GLN A 1 254 ? 12.004  0.678   37.160  1.00 20.79 ? 255 GLN A CB  1 
ATOM   2059 C  CG  . GLN A 1 254 ? 10.895  0.016   37.927  1.00 31.71 ? 255 GLN A CG  1 
ATOM   2060 C  CD  . GLN A 1 254 ? 11.414  -0.517  39.247  1.00 41.11 ? 255 GLN A CD  1 
ATOM   2061 O  OE1 . GLN A 1 254 ? 11.876  0.242   40.131  1.00 54.02 ? 255 GLN A OE1 1 
ATOM   2062 N  NE2 . GLN A 1 254 ? 11.358  -1.827  39.391  1.00 46.35 ? 255 GLN A NE2 1 
ATOM   2063 N  N   . ILE A 1 255 ? 11.479  -1.561  34.526  1.00 12.60 ? 256 ILE A N   1 
ATOM   2064 C  CA  . ILE A 1 255 ? 10.539  -1.646  33.447  1.00 10.95 ? 256 ILE A CA  1 
ATOM   2065 C  C   . ILE A 1 255 ? 9.129   -1.685  34.091  1.00 11.00 ? 256 ILE A C   1 
ATOM   2066 O  O   . ILE A 1 255 ? 8.896   -2.424  35.040  1.00 11.26 ? 256 ILE A O   1 
ATOM   2067 C  CB  . ILE A 1 255 ? 10.741  -2.949  32.626  1.00 10.69 ? 256 ILE A CB  1 
ATOM   2068 C  CG1 . ILE A 1 255 ? 12.151  -2.908  31.987  1.00 10.11 ? 256 ILE A CG1 1 
ATOM   2069 C  CG2 . ILE A 1 255 ? 9.639   -3.155  31.556  1.00 9.42  ? 256 ILE A CG2 1 
ATOM   2070 C  CD1 . ILE A 1 255 ? 12.389  -4.144  31.119  1.00 11.48 ? 256 ILE A CD1 1 
ATOM   2071 N  N   . LYS A 1 256 ? 8.259   -0.795  33.615  1.00 10.85 ? 257 LYS A N   1 
ATOM   2072 C  CA  . LYS A 1 256 ? 6.900   -0.690  34.176  1.00 11.13 ? 257 LYS A CA  1 
ATOM   2073 C  C   . LYS A 1 256 ? 5.868   -1.319  33.240  1.00 11.33 ? 257 LYS A C   1 
ATOM   2074 O  O   . LYS A 1 256 ? 5.988   -1.213  32.009  1.00 11.42 ? 257 LYS A O   1 
ATOM   2075 C  CB  . LYS A 1 256 ? 6.548   0.765   34.485  1.00 12.62 ? 257 LYS A CB  1 
ATOM   2076 C  CG  . LYS A 1 256 ? 7.442   1.322   35.593  1.00 17.75 ? 257 LYS A CG  1 
ATOM   2077 C  CD  . LYS A 1 256 ? 7.390   2.821   35.710  1.00 22.10 ? 257 LYS A CD  1 
ATOM   2078 C  CE  . LYS A 1 256 ? 8.418   3.326   36.746  1.00 26.87 ? 257 LYS A CE  1 
ATOM   2079 N  NZ  . LYS A 1 256 ? 8.346   4.815   37.018  1.00 27.35 ? 257 LYS A NZ  1 
ATOM   2080 N  N   . ALA A 1 257 ? 4.835   -1.945  33.793  1.00 11.22 ? 258 ALA A N   1 
ATOM   2081 C  CA  . ALA A 1 257 ? 3.750   -2.539  32.955  1.00 11.03 ? 258 ALA A CA  1 
ATOM   2082 C  C   . ALA A 1 257 ? 2.477   -1.780  33.121  1.00 11.11 ? 258 ALA A C   1 
ATOM   2083 O  O   . ALA A 1 257 ? 2.153   -1.292  34.226  1.00 11.18 ? 258 ALA A O   1 
ATOM   2084 C  CB  . ALA A 1 257 ? 3.517   -4.028  33.305  1.00 11.77 ? 258 ALA A CB  1 
ATOM   2085 N  N   . SER A 1 258 ? 1.725   -1.716  32.043  1.00 10.82 ? 259 SER A N   1 
ATOM   2086 C  CA  . SER A 1 258 ? 0.503   -0.950  32.010  1.00 13.49 ? 259 SER A CA  1 
ATOM   2087 C  C   . SER A 1 258 ? -0.665  -1.814  32.458  1.00 14.21 ? 259 SER A C   1 
ATOM   2088 O  O   . SER A 1 258 ? -1.780  -1.307  32.604  1.00 15.89 ? 259 SER A O   1 
ATOM   2089 C  CB  . SER A 1 258 ? 0.229   -0.431  30.638  1.00 14.12 ? 259 SER A CB  1 
ATOM   2090 O  OG  . SER A 1 258 ? -0.342  -1.429  29.761  1.00 14.62 ? 259 SER A OG  1 
ATOM   2091 N  N   . PHE A 1 259 ? -0.390  -3.085  32.709  1.00 14.31 ? 260 PHE A N   1 
ATOM   2092 C  CA  . PHE A 1 259 ? -1.426  -4.083  32.929  1.00 16.96 ? 260 PHE A CA  1 
ATOM   2093 C  C   . PHE A 1 259 ? -1.067  -5.052  34.066  1.00 22.86 ? 260 PHE A C   1 
ATOM   2094 O  O   . PHE A 1 259 ? 0.122   -5.255  34.397  1.00 21.61 ? 260 PHE A O   1 
ATOM   2095 C  CB  . PHE A 1 259 ? -1.617  -4.900  31.641  1.00 15.77 ? 260 PHE A CB  1 
ATOM   2096 C  CG  . PHE A 1 259 ? -0.339  -5.670  31.227  1.00 15.27 ? 260 PHE A CG  1 
ATOM   2097 C  CD1 . PHE A 1 259 ? 0.674   -5.028  30.480  1.00 14.49 ? 260 PHE A CD1 1 
ATOM   2098 C  CD2 . PHE A 1 259 ? -0.119  -6.978  31.651  1.00 15.98 ? 260 PHE A CD2 1 
ATOM   2099 C  CE1 . PHE A 1 259 ? 1.874   -5.671  30.158  1.00 15.89 ? 260 PHE A CE1 1 
ATOM   2100 C  CE2 . PHE A 1 259 ? 1.076   -7.629  31.333  1.00 17.17 ? 260 PHE A CE2 1 
ATOM   2101 C  CZ  . PHE A 1 259 ? 2.081   -6.979  30.599  1.00 16.08 ? 260 PHE A CZ  1 
ATOM   2102 N  N   . LYS A 1 260 ? -2.154  -5.636  34.613  1.00 29.11 ? 261 LYS A N   1 
ATOM   2103 C  CA  . LYS A 1 260 ? -2.231  -6.839  35.489  1.00 39.32 ? 261 LYS A CA  1 
ATOM   2104 C  C   . LYS A 1 260 ? -1.583  -6.830  36.873  1.00 49.24 ? 261 LYS A C   1 
ATOM   2105 O  O   . LYS A 1 260 ? -0.689  -7.624  37.199  1.00 60.14 ? 261 LYS A O   1 
ATOM   2106 C  CB  . LYS A 1 260 ? -1.923  -8.141  34.724  1.00 39.77 ? 261 LYS A CB  1 
ATOM   2107 C  CG  . LYS A 1 260 ? -2.953  -8.448  33.646  1.00 39.54 ? 261 LYS A CG  1 
ATOM   2108 C  CD  . LYS A 1 260 ? -2.961  -9.923  33.263  1.00 42.73 ? 261 LYS A CD  1 
ATOM   2109 C  CE  . LYS A 1 260 ? -1.894  -10.287 32.236  1.00 44.65 ? 261 LYS A CE  1 
ATOM   2110 N  NZ  . LYS A 1 260 ? -0.506  -10.450 32.779  1.00 41.88 ? 261 LYS A NZ  1 
ATOM   2111 O  OXT . LYS A 1 260 ? -1.993  -6.024  37.717  1.00 56.48 ? 261 LYS A OXT 1 
HETATM 2112 ZN ZN  . ZN  B 2 .   ? 14.478  0.214   15.285  1.00 8.69  ? 301 ZN  A ZN  1 
HETATM 2113 F  F26 . V1F C 3 .   ? 14.216  5.057   14.997  1.00 23.70 ? 302 V1F A F26 1 
HETATM 2114 C  C5  . V1F C 3 .   ? 15.521  5.157   15.048  1.00 19.52 ? 302 V1F A C5  1 
HETATM 2115 C  C4  . V1F C 3 .   ? 16.174  4.161   15.784  1.00 15.90 ? 302 V1F A C4  1 
HETATM 2116 S  S7  . V1F C 3 .   ? 15.357  2.831   16.692  1.00 12.99 ? 302 V1F A S7  1 
HETATM 2117 O  O9  . V1F C 3 .   ? 13.850  2.924   16.584  1.00 12.16 ? 302 V1F A O9  1 
HETATM 2118 N  N10 . V1F C 3 .   ? 15.785  1.279   16.110  1.00 11.59 ? 302 V1F A N10 1 
HETATM 2119 O  O8  . V1F C 3 .   ? 15.847  3.052   18.082  1.00 11.87 ? 302 V1F A O8  1 
HETATM 2120 C  C3  . V1F C 3 .   ? 17.566  4.281   15.897  1.00 18.25 ? 302 V1F A C3  1 
HETATM 2121 F  F12 . V1F C 3 .   ? 18.256  3.353   16.611  1.00 19.30 ? 302 V1F A F12 1 
HETATM 2122 C  C2  . V1F C 3 .   ? 18.271  5.282   15.264  1.00 20.05 ? 302 V1F A C2  1 
HETATM 2123 F  F13 . V1F C 3 .   ? 19.624  5.332   15.431  1.00 20.33 ? 302 V1F A F13 1 
HETATM 2124 C  C6  . V1F C 3 .   ? 16.208  6.173   14.365  1.00 20.41 ? 302 V1F A C6  1 
HETATM 2125 C  C1  . V1F C 3 .   ? 17.615  6.248   14.486  1.00 22.08 ? 302 V1F A C1  1 
HETATM 2126 S  S11 . V1F C 3 .   ? 18.704  7.464   13.700  1.00 25.10 ? 302 V1F A S11 1 
HETATM 2127 O  O22 . V1F C 3 .   ? 19.322  8.528   14.608  1.00 27.52 ? 302 V1F A O22 1 
HETATM 2128 O  O23 . V1F C 3 .   ? 17.903  8.378   12.741  1.00 29.68 ? 302 V1F A O23 1 
HETATM 2129 C  C21 . V1F C 3 .   ? 20.005  6.606   12.727  1.00 27.38 ? 302 V1F A C21 1 
HETATM 2130 C  C24 . V1F C 3 .   ? 19.588  5.777   11.478  1.00 27.82 ? 302 V1F A C24 1 
HETATM 2131 C  C30 . V1F C 3 .   ? 18.436  4.804   11.456  1.00 27.01 ? 302 V1F A C30 1 
HETATM 2132 C  C29 . V1F C 3 .   ? 18.327  3.734   12.363  1.00 28.08 ? 302 V1F A C29 1 
HETATM 2133 C  C28 . V1F C 3 .   ? 17.225  2.853   12.256  1.00 30.26 ? 302 V1F A C28 1 
HETATM 2134 C  C32 . V1F C 3 .   ? 17.416  4.956   10.478  1.00 26.92 ? 302 V1F A C32 1 
HETATM 2135 C  C31 . V1F C 3 .   ? 16.317  4.088   10.393  1.00 27.60 ? 302 V1F A C31 1 
HETATM 2136 C  C27 . V1F C 3 .   ? 16.217  3.003   11.265  1.00 26.52 ? 302 V1F A C27 1 
HETATM 2137 N  N25 . V1F C 3 .   ? 15.546  7.143   13.594  1.00 22.87 ? 302 V1F A N25 1 
HETATM 2138 C  C14 . V1F C 3 .   ? 14.658  6.736   12.534  1.00 22.66 ? 302 V1F A C14 1 
HETATM 2139 C  C15 . V1F C 3 .   ? 14.489  7.889   11.630  1.00 25.85 ? 302 V1F A C15 1 
HETATM 2140 C  C20 . V1F C 3 .   ? 13.800  9.023   12.107  1.00 26.41 ? 302 V1F A C20 1 
HETATM 2141 C  C19 . V1F C 3 .   ? 13.621  10.131  11.254  1.00 26.55 ? 302 V1F A C19 1 
HETATM 2142 C  C18 . V1F C 3 .   ? 14.142  10.090  9.956   1.00 31.19 ? 302 V1F A C18 1 
HETATM 2143 C  C17 . V1F C 3 .   ? 14.815  8.942   9.488   1.00 31.30 ? 302 V1F A C17 1 
HETATM 2144 C  C16 . V1F C 3 .   ? 14.974  7.834   10.311  1.00 26.54 ? 302 V1F A C16 1 
HETATM 2145 N  N1  . BCN D 4 .   ? 0.703   -12.651 23.206  1.00 33.57 ? 303 BCN A N1  1 
HETATM 2146 C  C1  . BCN D 4 .   ? 1.554   -12.306 24.300  1.00 30.67 ? 303 BCN A C1  1 
HETATM 2147 C  C2  . BCN D 4 .   ? 1.351   -13.174 25.487  1.00 35.47 ? 303 BCN A C2  1 
HETATM 2148 O  O21 . BCN D 4 .   ? 0.379   -14.035 25.436  1.00 36.36 ? 303 BCN A O21 1 
HETATM 2149 O  O22 . BCN D 4 .   ? 2.048   -13.098 26.457  1.00 36.00 ? 303 BCN A O22 1 
HETATM 2150 C  C3  . BCN D 4 .   ? 0.668   -13.525 22.202  1.00 29.73 ? 303 BCN A C3  1 
HETATM 2151 C  C4  . BCN D 4 .   ? 1.516   -14.515 21.659  1.00 33.44 ? 303 BCN A C4  1 
HETATM 2152 O  O4  . BCN D 4 .   ? 0.502   -14.684 20.665  1.00 36.25 ? 303 BCN A O4  1 
HETATM 2153 C  C5  . BCN D 4 .   ? -0.538  -11.941 23.139  1.00 30.34 ? 303 BCN A C5  1 
HETATM 2154 C  C6  . BCN D 4 .   ? -1.312  -12.478 21.933  1.00 41.15 ? 303 BCN A C6  1 
HETATM 2155 O  O6  . BCN D 4 .   ? -2.638  -12.693 22.170  1.00 37.31 ? 303 BCN A O6  1 
HETATM 2156 O  O1  . MES E 5 .   ? 13.754  -7.160  -2.493  1.00 29.12 ? 304 MES A O1  1 
HETATM 2157 C  C2  . MES E 5 .   ? 13.769  -7.873  -3.847  1.00 30.01 ? 304 MES A C2  1 
HETATM 2158 C  C3  . MES E 5 .   ? 12.573  -8.879  -4.102  1.00 31.65 ? 304 MES A C3  1 
HETATM 2159 N  N4  . MES E 5 .   ? 11.426  -8.960  -3.182  1.00 31.22 ? 304 MES A N4  1 
HETATM 2160 C  C5  . MES E 5 .   ? 11.524  -8.225  -1.866  1.00 28.72 ? 304 MES A C5  1 
HETATM 2161 C  C6  . MES E 5 .   ? 12.838  -7.774  -1.519  1.00 28.58 ? 304 MES A C6  1 
HETATM 2162 C  C7  . MES E 5 .   ? 10.259  -9.914  -3.441  1.00 35.70 ? 304 MES A C7  1 
HETATM 2163 C  C8  . MES E 5 .   ? 8.687   -9.691  -3.082  1.00 38.21 ? 304 MES A C8  1 
HETATM 2164 S  S   . DMS F 6 .   ? 22.586  -9.665  14.864  1.00 37.55 ? 305 DMS A S   1 
HETATM 2165 O  O   . DMS F 6 .   ? 22.924  -11.155 14.677  1.00 37.28 ? 305 DMS A O   1 
HETATM 2166 C  C1  . DMS F 6 .   ? 22.980  -9.162  16.452  1.00 29.86 ? 305 DMS A C1  1 
HETATM 2167 C  C2  . DMS F 6 .   ? 23.706  -8.922  13.758  1.00 31.54 ? 305 DMS A C2  1 
HETATM 2168 O  O   . HOH G 7 .   ? 19.935  -2.291  15.887  1.00 8.64  ? 401 HOH A O   1 
HETATM 2169 O  O   . HOH G 7 .   ? 17.601  -9.124  20.886  1.00 9.10  ? 402 HOH A O   1 
HETATM 2170 O  O   . HOH G 7 .   ? 16.651  -11.578 18.065  1.00 7.71  ? 403 HOH A O   1 
HETATM 2171 O  O   . HOH G 7 .   ? 10.510  10.521  25.592  1.00 12.00 ? 404 HOH A O   1 
HETATM 2172 O  O   . HOH G 7 .   ? 22.431  0.320   29.470  1.00 13.26 ? 405 HOH A O   1 
HETATM 2173 O  O   . HOH G 7 .   ? 26.136  -3.039  21.033  1.00 11.57 ? 406 HOH A O   1 
HETATM 2174 O  O   . HOH G 7 .   ? 5.034   -10.453 24.400  1.00 10.79 ? 407 HOH A O   1 
HETATM 2175 O  O   . HOH G 7 .   ? 17.731  -11.376 25.184  1.00 10.80 ? 408 HOH A O   1 
HETATM 2176 O  O   . HOH G 7 .   ? 17.325  -14.003 24.409  1.00 10.78 ? 409 HOH A O   1 
HETATM 2177 O  O   . HOH G 7 .   ? 4.106   -6.536  20.475  1.00 9.83  ? 410 HOH A O   1 
HETATM 2178 O  O   . HOH G 7 .   ? 24.796  6.931   29.852  1.00 15.91 ? 411 HOH A O   1 
HETATM 2179 O  O   . HOH G 7 .   ? 8.270   -15.373 16.866  1.00 12.01 ? 412 HOH A O   1 
HETATM 2180 O  O   . HOH G 7 .   ? -0.640  7.506   4.786   1.00 15.15 ? 413 HOH A O   1 
HETATM 2181 O  O   . HOH G 7 .   ? 9.093   4.678   30.957  1.00 15.82 ? 414 HOH A O   1 
HETATM 2182 O  O   . HOH G 7 .   ? 18.551  -6.870  29.175  1.00 10.80 ? 415 HOH A O   1 
HETATM 2183 O  O   . HOH G 7 .   ? -0.456  -5.385  23.731  1.00 11.35 ? 416 HOH A O   1 
HETATM 2184 O  O   . HOH G 7 .   ? -2.656  1.071   3.979   1.00 15.38 ? 417 HOH A O   1 
HETATM 2185 O  O   . HOH G 7 .   ? 19.140  -10.529 22.830  1.00 9.49  ? 418 HOH A O   1 
HETATM 2186 O  O   . HOH G 7 .   ? 14.265  -18.347 19.520  1.00 14.08 ? 419 HOH A O   1 
HETATM 2187 O  O   . HOH G 7 .   ? 6.468   -16.734 18.792  1.00 14.65 ? 420 HOH A O   1 
HETATM 2188 O  O   . HOH G 7 .   ? 3.024   -18.468 7.978   1.00 12.53 ? 421 HOH A O   1 
HETATM 2189 O  O   . HOH G 7 .   ? 13.185  -13.478 11.414  1.00 11.46 ? 422 HOH A O   1 
HETATM 2190 O  O   . HOH G 7 .   ? 6.989   -14.717 29.206  1.00 20.77 ? 423 HOH A O   1 
HETATM 2191 O  O   . HOH G 7 .   ? 11.462  -6.095  34.226  1.00 20.14 ? 424 HOH A O   1 
HETATM 2192 O  O   . HOH G 7 .   ? 7.511   -16.719 14.764  1.00 16.05 ? 425 HOH A O   1 
HETATM 2193 O  O   . HOH G 7 .   ? 2.977   12.588  11.399  1.00 18.47 ? 426 HOH A O   1 
HETATM 2194 O  O   . HOH G 7 .   ? 12.901  -17.486 21.767  1.00 13.76 ? 427 HOH A O   1 
HETATM 2195 O  O   . HOH G 7 .   ? 15.053  -2.704  -6.395  1.00 22.44 ? 428 HOH A O   1 
HETATM 2196 O  O   . HOH G 7 .   ? 10.910  16.635  12.367  1.00 20.06 ? 429 HOH A O   1 
HETATM 2197 O  O   . HOH G 7 .   ? 3.851   -14.271 22.161  1.00 19.38 ? 430 HOH A O   1 
HETATM 2198 O  O   . HOH G 7 .   ? 1.800   11.985  8.864   1.00 16.11 ? 431 HOH A O   1 
HETATM 2199 O  O   . HOH G 7 .   ? 26.487  8.963   20.280  1.00 13.63 ? 432 HOH A O   1 
HETATM 2200 O  O   . HOH G 7 .   ? 10.083  -17.725 7.211   1.00 20.40 ? 433 HOH A O   1 
HETATM 2201 O  O   . HOH G 7 .   ? 21.291  0.575   -4.815  1.00 22.02 ? 434 HOH A O   1 
HETATM 2202 O  O   . HOH G 7 .   ? 4.225   -16.180 20.105  1.00 18.77 ? 435 HOH A O   1 
HETATM 2203 O  O   . HOH G 7 .   ? 10.629  -16.365 17.109  1.00 14.61 ? 436 HOH A O   1 
HETATM 2204 O  O   . HOH G 7 .   ? 29.930  -2.621  23.684  1.00 18.42 ? 437 HOH A O   1 
HETATM 2205 O  O   . HOH G 7 .   ? 8.109   -15.010 26.670  1.00 14.55 ? 438 HOH A O   1 
HETATM 2206 O  O   . HOH G 7 .   ? 20.713  12.681  23.369  1.00 18.06 ? 439 HOH A O   1 
HETATM 2207 O  O   . HOH G 7 .   ? 4.321   -12.122 26.469  1.00 17.76 ? 440 HOH A O   1 
HETATM 2208 O  O   . HOH G 7 .   ? 7.100   16.133  27.253  1.00 22.28 ? 441 HOH A O   1 
HETATM 2209 O  O   . HOH G 7 .   ? 7.336   12.349  27.955  1.00 16.84 ? 442 HOH A O   1 
HETATM 2210 O  O   . HOH G 7 .   ? -3.034  10.377  20.251  1.00 19.61 ? 443 HOH A O   1 
HETATM 2211 O  O   . HOH G 7 .   ? 3.345   -19.342 17.560  1.00 24.95 ? 444 HOH A O   1 
HETATM 2212 O  O   . HOH G 7 .   ? -3.941  -5.867  9.075   1.00 16.29 ? 445 HOH A O   1 
HETATM 2213 O  O   . HOH G 7 .   ? 1.160   -14.814 2.971   1.00 20.76 ? 446 HOH A O   1 
HETATM 2214 O  O   . HOH G 7 .   ? 25.732  -4.871  8.016   1.00 25.36 ? 447 HOH A O   1 
HETATM 2215 O  O   . HOH G 7 .   ? 22.544  10.654  24.400  1.00 16.87 ? 448 HOH A O   1 
HETATM 2216 O  O   . HOH G 7 .   ? 4.853   -8.067  32.986  1.00 15.81 ? 449 HOH A O   1 
HETATM 2217 O  O   . HOH G 7 .   ? 19.960  -9.515  29.076  1.00 18.19 ? 450 HOH A O   1 
HETATM 2218 O  O   . HOH G 7 .   ? 29.948  -1.974  21.267  1.00 18.73 ? 451 HOH A O   1 
HETATM 2219 O  O   . HOH G 7 .   ? 22.370  -9.930  25.081  1.00 19.55 ? 452 HOH A O   1 
HETATM 2220 O  O   . HOH G 7 .   ? 16.274  -10.062 32.247  1.00 18.91 ? 453 HOH A O   1 
HETATM 2221 O  O   . HOH G 7 .   ? -2.776  1.002   26.624  1.00 19.68 ? 454 HOH A O   1 
HETATM 2222 O  O   . HOH G 7 .   ? -1.655  -4.025  2.838   1.00 19.72 ? 455 HOH A O   1 
HETATM 2223 O  O   . HOH G 7 .   ? 10.510  -17.514 20.065  1.00 17.36 ? 456 HOH A O   1 
HETATM 2224 O  O   . HOH G 7 .   ? 0.766   12.561  26.880  1.00 14.36 ? 457 HOH A O   1 
HETATM 2225 O  O   . HOH G 7 .   ? 18.739  -1.242  11.684  1.00 16.45 ? 458 HOH A O   1 
HETATM 2226 O  O   . HOH G 7 .   ? 19.275  -15.611 25.615  1.00 22.59 ? 459 HOH A O   1 
HETATM 2227 O  O   . HOH G 7 .   ? 5.666   -19.901 13.155  1.00 21.24 ? 460 HOH A O   1 
HETATM 2228 O  O   . HOH G 7 .   ? 5.115   17.668  23.931  1.00 18.72 ? 461 HOH A O   1 
HETATM 2229 O  O   . HOH G 7 .   ? 25.277  -1.492  26.605  1.00 19.12 ? 462 HOH A O   1 
HETATM 2230 O  O   . HOH G 7 .   ? 25.644  -0.720  29.009  1.00 23.51 ? 463 HOH A O   1 
HETATM 2231 O  O   . HOH G 7 .   ? 20.910  -12.366 22.307  1.00 19.85 ? 464 HOH A O   1 
HETATM 2232 O  O   . HOH G 7 .   ? 28.745  7.978   21.680  1.00 14.18 ? 465 HOH A O   1 
HETATM 2233 O  O   . HOH G 7 .   ? 23.731  -9.433  9.503   1.00 18.79 ? 466 HOH A O   1 
HETATM 2234 O  O   . HOH G 7 .   ? 12.124  -3.894  36.073  1.00 20.43 ? 467 HOH A O   1 
HETATM 2235 O  O   . HOH G 7 .   ? -5.743  -0.702  14.399  1.00 20.15 ? 468 HOH A O   1 
HETATM 2236 O  O   . HOH G 7 .   ? -2.246  -11.260 11.276  1.00 20.70 ? 469 HOH A O   1 
HETATM 2237 O  O   . HOH G 7 .   ? 10.378  -17.117 34.297  1.00 25.55 ? 470 HOH A O   1 
HETATM 2238 O  O   . HOH G 7 .   ? -4.392  11.492  13.225  1.00 26.98 ? 471 HOH A O   1 
HETATM 2239 O  O   . HOH G 7 .   ? 8.722   14.325  29.257  1.00 20.10 ? 472 HOH A O   1 
HETATM 2240 O  O   . HOH G 7 .   ? 7.280   -19.222 15.191  1.00 16.13 ? 473 HOH A O   1 
HETATM 2241 O  O   . HOH G 7 .   ? 5.329   10.841  -2.088  1.00 25.08 ? 474 HOH A O   1 
HETATM 2242 O  O   . HOH G 7 .   ? 19.704  -11.262 27.137  1.00 21.37 ? 475 HOH A O   1 
HETATM 2243 O  O   . HOH G 7 .   ? 23.240  -12.230 20.790  1.00 27.41 ? 476 HOH A O   1 
HETATM 2244 O  O   . HOH G 7 .   ? 8.328   9.762   28.805  1.00 21.02 ? 477 HOH A O   1 
HETATM 2245 O  O   . HOH G 7 .   ? -2.123  -1.151  6.786   1.00 18.33 ? 478 HOH A O   1 
HETATM 2246 O  O   . HOH G 7 .   ? -1.907  -9.805  14.094  1.00 23.30 ? 479 HOH A O   1 
HETATM 2247 O  O   . HOH G 7 .   ? 29.366  5.038   27.860  1.00 24.58 ? 480 HOH A O   1 
HETATM 2248 O  O   . HOH G 7 .   ? -6.467  4.584   23.671  1.00 31.54 ? 481 HOH A O   1 
HETATM 2249 O  O   . HOH G 7 .   ? -5.023  5.425   15.260  1.00 28.77 ? 482 HOH A O   1 
HETATM 2250 O  O   . HOH G 7 .   ? -1.200  -16.449 13.530  1.00 26.05 ? 483 HOH A O   1 
HETATM 2251 O  O   . HOH G 7 .   ? -3.414  -7.567  1.990   1.00 27.77 ? 484 HOH A O   1 
HETATM 2252 O  O   . HOH G 7 .   ? 3.017   -19.769 5.758   1.00 29.68 ? 485 HOH A O   1 
HETATM 2253 O  O   . HOH G 7 .   ? 8.179   15.049  31.848  1.00 23.19 ? 486 HOH A O   1 
HETATM 2254 O  O   . HOH G 7 .   ? -4.351  -8.589  17.829  1.00 29.72 ? 487 HOH A O   1 
HETATM 2255 O  O   . HOH G 7 .   ? -4.475  6.101   4.074   1.00 32.71 ? 488 HOH A O   1 
HETATM 2256 O  O   . HOH G 7 .   ? 13.491  -3.093  39.942  1.00 34.77 ? 489 HOH A O   1 
HETATM 2257 O  O   . HOH G 7 .   ? 4.155   -19.484 21.512  1.00 35.74 ? 490 HOH A O   1 
HETATM 2258 O  O   . HOH G 7 .   ? 19.753  13.305  25.926  1.00 28.03 ? 491 HOH A O   1 
HETATM 2259 O  O   . HOH G 7 .   ? 15.025  19.626  27.764  1.00 29.44 ? 492 HOH A O   1 
HETATM 2260 O  O   . HOH G 7 .   ? 12.801  2.472   -6.440  1.00 26.78 ? 493 HOH A O   1 
HETATM 2261 O  O   . HOH G 7 .   ? 15.067  -9.503  36.626  1.00 27.09 ? 494 HOH A O   1 
HETATM 2262 O  O   . HOH G 7 .   ? 12.385  -1.985  7.984   1.00 18.69 ? 495 HOH A O   1 
HETATM 2263 O  O   . HOH G 7 .   ? 31.024  -11.313 9.470   1.00 35.84 ? 496 HOH A O   1 
HETATM 2264 O  O   . HOH G 7 .   ? 7.766   1.100   -5.992  1.00 21.41 ? 497 HOH A O   1 
HETATM 2265 O  O   . HOH G 7 .   ? 23.004  -13.728 9.128   1.00 24.96 ? 498 HOH A O   1 
HETATM 2266 O  O   . HOH G 7 .   ? 14.830  -17.804 23.866  1.00 22.23 ? 499 HOH A O   1 
HETATM 2267 O  O   . HOH G 7 .   ? 14.487  -3.391  37.569  1.00 19.86 ? 500 HOH A O   1 
HETATM 2268 O  O   . HOH G 7 .   ? 13.865  -15.095 1.552   1.00 17.41 ? 501 HOH A O   1 
HETATM 2269 O  O   . HOH G 7 .   ? 19.515  4.733   -7.130  1.00 27.54 ? 502 HOH A O   1 
HETATM 2270 O  O   . HOH G 7 .   ? 16.384  -13.958 0.778   1.00 22.98 ? 503 HOH A O   1 
HETATM 2271 O  O   . HOH G 7 .   ? 14.946  17.280  11.870  1.00 26.50 ? 504 HOH A O   1 
HETATM 2272 O  O   . HOH G 7 .   ? 23.947  -2.473  7.723   1.00 34.25 ? 505 HOH A O   1 
HETATM 2273 O  O   . HOH G 7 .   ? 24.220  -11.913 8.135   1.00 25.93 ? 506 HOH A O   1 
HETATM 2274 O  O   . HOH G 7 .   ? 31.674  -7.203  9.034   1.00 34.44 ? 507 HOH A O   1 
HETATM 2275 O  O   . HOH G 7 .   ? -3.053  -5.069  0.369   1.00 31.31 ? 508 HOH A O   1 
HETATM 2276 O  O   . HOH G 7 .   ? -1.933  1.472   34.623  1.00 28.50 ? 509 HOH A O   1 
HETATM 2277 O  O   . HOH G 7 .   ? 16.379  -19.024 21.377  1.00 20.96 ? 510 HOH A O   1 
HETATM 2278 O  O   . HOH G 7 .   ? 12.639  -18.027 26.834  1.00 16.36 ? 511 HOH A O   1 
HETATM 2279 O  O   . HOH G 7 .   ? 9.923   -3.303  38.072  1.00 44.56 ? 512 HOH A O   1 
HETATM 2280 O  O   . HOH G 7 .   ? -2.262  -9.374  16.971  1.00 26.82 ? 513 HOH A O   1 
HETATM 2281 O  O   . HOH G 7 .   ? 20.562  -6.719  32.409  1.00 24.01 ? 514 HOH A O   1 
HETATM 2282 O  O   . HOH G 7 .   ? 26.109  -11.166 -5.688  1.00 29.38 ? 515 HOH A O   1 
HETATM 2283 O  O   . HOH G 7 .   ? 2.507   -19.173 14.839  1.00 26.91 ? 516 HOH A O   1 
HETATM 2284 O  O   . HOH G 7 .   ? -5.187  4.740   20.946  1.00 37.92 ? 517 HOH A O   1 
HETATM 2285 O  O   . HOH G 7 .   ? 32.430  -1.918  7.802   1.00 30.97 ? 518 HOH A O   1 
HETATM 2286 O  O   . HOH G 7 .   ? 28.862  -6.144  -0.595  1.00 36.13 ? 519 HOH A O   1 
HETATM 2287 O  O   . HOH G 7 .   ? 1.643   -2.501  41.377  1.00 30.12 ? 520 HOH A O   1 
HETATM 2288 O  O   . HOH G 7 .   ? 13.225  -17.137 30.689  1.00 30.81 ? 521 HOH A O   1 
HETATM 2289 O  O   . HOH G 7 .   ? 27.620  7.131   28.351  1.00 29.52 ? 522 HOH A O   1 
HETATM 2290 O  O   . HOH G 7 .   ? 19.246  -2.689  -6.900  1.00 23.81 ? 523 HOH A O   1 
HETATM 2291 O  O   . HOH G 7 .   ? 24.466  0.209   8.671   1.00 26.66 ? 524 HOH A O   1 
HETATM 2292 O  O   . HOH G 7 .   ? 5.637   -14.555 25.546  1.00 28.88 ? 525 HOH A O   1 
HETATM 2293 O  O   . HOH G 7 .   ? 7.047   5.499   33.363  1.00 27.66 ? 526 HOH A O   1 
HETATM 2294 O  O   . HOH G 7 .   ? 18.817  -17.252 21.217  1.00 36.03 ? 527 HOH A O   1 
HETATM 2295 O  O   . HOH G 7 .   ? 31.451  -0.590  13.891  1.00 35.27 ? 528 HOH A O   1 
HETATM 2296 O  O   . HOH G 7 .   ? 33.135  -4.769  8.085   1.00 29.27 ? 529 HOH A O   1 
HETATM 2297 O  O   . HOH G 7 .   ? 21.103  2.943   34.538  1.00 25.74 ? 530 HOH A O   1 
HETATM 2298 O  O   . HOH G 7 .   ? 13.887  -6.836  32.712  1.00 16.50 ? 531 HOH A O   1 
HETATM 2299 O  O   . HOH G 7 .   ? 17.469  -11.156 -2.767  1.00 22.47 ? 532 HOH A O   1 
HETATM 2300 O  O   . HOH G 7 .   ? 35.366  -2.191  10.480  1.00 40.78 ? 533 HOH A O   1 
HETATM 2301 O  O   . HOH G 7 .   ? 34.132  -1.845  13.694  1.00 25.57 ? 534 HOH A O   1 
HETATM 2302 O  O   . HOH G 7 .   ? 34.628  1.997   24.651  1.00 20.62 ? 535 HOH A O   1 
HETATM 2303 O  O   . HOH G 7 .   ? 32.363  3.015   25.877  1.00 26.65 ? 536 HOH A O   1 
HETATM 2304 O  O   . HOH G 7 .   ? 34.218  -3.899  24.717  1.00 22.51 ? 537 HOH A O   1 
HETATM 2305 O  O   . HOH G 7 .   ? 31.506  7.570   13.041  1.00 35.27 ? 538 HOH A O   1 
HETATM 2306 O  O   . HOH G 7 .   ? 19.819  11.142  28.067  1.00 23.15 ? 539 HOH A O   1 
HETATM 2307 O  O   . HOH G 7 .   ? 27.536  -3.657  27.425  1.00 27.26 ? 540 HOH A O   1 
HETATM 2308 O  O   . HOH G 7 .   ? 16.881  -6.681  31.198  1.00 24.38 ? 541 HOH A O   1 
HETATM 2309 O  O   . HOH G 7 .   ? 18.273  -13.069 32.862  1.00 25.83 ? 542 HOH A O   1 
HETATM 2310 O  O   . HOH G 7 .   ? 14.390  -13.050 31.658  1.00 25.10 ? 543 HOH A O   1 
HETATM 2311 O  O   . HOH G 7 .   ? 10.210  -13.501 34.235  1.00 27.16 ? 544 HOH A O   1 
HETATM 2312 O  O   . HOH G 7 .   ? 4.733   -13.406 32.948  1.00 25.46 ? 545 HOH A O   1 
HETATM 2313 O  O   . HOH G 7 .   ? 8.617   -16.427 32.211  1.00 31.93 ? 546 HOH A O   1 
HETATM 2314 O  O   . HOH G 7 .   ? 3.224   -10.190 31.563  1.00 26.35 ? 547 HOH A O   1 
HETATM 2315 O  O   . HOH G 7 .   ? 2.731   -6.963  35.042  1.00 28.03 ? 548 HOH A O   1 
HETATM 2316 O  O   . HOH G 7 .   ? 3.833   0.683   40.055  1.00 37.63 ? 549 HOH A O   1 
HETATM 2317 O  O   . HOH G 7 .   ? 3.344   8.115   38.524  1.00 30.80 ? 550 HOH A O   1 
HETATM 2318 O  O   . HOH G 7 .   ? 6.047   11.270  31.445  1.00 32.53 ? 551 HOH A O   1 
HETATM 2319 O  O   . HOH G 7 .   ? 6.442   8.021   32.805  1.00 28.86 ? 552 HOH A O   1 
HETATM 2320 O  O   . HOH G 7 .   ? 12.115  7.708   29.102  1.00 19.73 ? 553 HOH A O   1 
HETATM 2321 O  O   . HOH G 7 .   ? 10.726  6.678   30.878  1.00 25.16 ? 554 HOH A O   1 
HETATM 2322 O  O   . HOH G 7 .   ? -4.750  8.058   27.052  1.00 27.65 ? 555 HOH A O   1 
HETATM 2323 O  O   . HOH G 7 .   ? -5.578  0.660   26.144  1.00 24.84 ? 556 HOH A O   1 
HETATM 2324 O  O   . HOH G 7 .   ? -5.842  -2.180  25.134  1.00 17.87 ? 557 HOH A O   1 
HETATM 2325 O  O   . HOH G 7 .   ? -3.834  6.459   8.457   1.00 28.06 ? 558 HOH A O   1 
HETATM 2326 O  O   . HOH G 7 .   ? -0.128  9.593   1.862   1.00 18.38 ? 559 HOH A O   1 
HETATM 2327 O  O   . HOH G 7 .   ? 2.914   5.811   -3.683  1.00 36.54 ? 560 HOH A O   1 
HETATM 2328 O  O   . HOH G 7 .   ? 4.580   7.172   -7.908  1.00 26.27 ? 561 HOH A O   1 
HETATM 2329 O  O   . HOH G 7 .   ? 22.070  5.197   1.834   1.00 28.88 ? 562 HOH A O   1 
HETATM 2330 O  O   . HOH G 7 .   ? -3.352  15.449  20.217  1.00 36.77 ? 563 HOH A O   1 
HETATM 2331 O  O   . HOH G 7 .   ? 6.201   21.893  17.849  1.00 17.48 ? 564 HOH A O   1 
HETATM 2332 O  O   . HOH G 7 .   ? 13.090  -20.384 10.580  1.00 21.58 ? 565 HOH A O   1 
HETATM 2333 O  O   . HOH G 7 .   ? 23.691  -11.377 5.222   1.00 23.10 ? 566 HOH A O   1 
HETATM 2334 O  O   . HOH G 7 .   ? 8.249   -17.644 26.339  1.00 16.39 ? 567 HOH A O   1 
HETATM 2335 O  O   . HOH G 7 .   ? 2.597   -2.003  -2.514  1.00 25.81 ? 568 HOH A O   1 
HETATM 2336 O  O   . HOH G 7 .   ? 24.097  2.860   -1.787  1.00 35.65 ? 569 HOH A O   1 
HETATM 2337 O  O   . HOH G 7 .   ? 21.856  2.453   -6.767  1.00 30.50 ? 570 HOH A O   1 
HETATM 2338 O  O   . HOH G 7 .   ? 15.322  5.829   -5.721  1.00 32.04 ? 571 HOH A O   1 
HETATM 2339 O  O   . HOH G 7 .   ? -4.812  -4.399  13.185  1.00 30.66 ? 572 HOH A O   1 
HETATM 2340 O  O   . HOH G 7 .   ? 29.159  -3.915  -10.691 1.00 34.46 ? 573 HOH A O   1 
HETATM 2341 O  O   . HOH G 7 .   ? -2.696  1.469   31.759  1.00 29.79 ? 574 HOH A O   1 
HETATM 2342 O  O   . HOH G 7 .   ? 24.561  -11.836 12.324  1.00 28.84 ? 575 HOH A O   1 
HETATM 2343 O  O   . HOH G 7 .   ? 26.402  -5.498  22.494  1.00 26.03 ? 576 HOH A O   1 
HETATM 2344 O  O   . HOH G 7 .   ? 32.283  -5.181  22.412  1.00 27.02 ? 577 HOH A O   1 
HETATM 2345 O  O   . HOH G 7 .   ? 35.368  7.620   19.435  1.00 26.31 ? 578 HOH A O   1 
HETATM 2346 O  O   . HOH G 7 .   ? 19.089  -10.098 31.664  1.00 30.55 ? 579 HOH A O   1 
HETATM 2347 O  O   . HOH G 7 .   ? 22.976  -7.804  30.780  1.00 30.86 ? 580 HOH A O   1 
HETATM 2348 O  O   . HOH G 7 .   ? 16.376  -7.800  33.568  1.00 29.04 ? 581 HOH A O   1 
HETATM 2349 O  O   . HOH G 7 .   ? 12.707  -15.602 34.962  1.00 23.08 ? 582 HOH A O   1 
HETATM 2350 O  O   . HOH G 7 .   ? 12.411  -13.474 36.704  1.00 27.87 ? 583 HOH A O   1 
HETATM 2351 O  O   . HOH G 7 .   ? -6.918  6.897   25.911  1.00 28.54 ? 584 HOH A O   1 
HETATM 2352 O  O   . HOH G 7 .   ? 12.241  10.955  6.625   1.00 36.75 ? 585 HOH A O   1 
HETATM 2353 O  O   . HOH G 7 .   ? 8.165   20.974  8.479   1.00 21.85 ? 586 HOH A O   1 
HETATM 2354 O  O   . HOH G 7 .   ? -0.177  22.598  14.685  1.00 37.91 ? 587 HOH A O   1 
HETATM 2355 O  O   . HOH G 7 .   ? 0.583   15.237  28.740  1.00 36.29 ? 588 HOH A O   1 
HETATM 2356 O  O   . HOH G 7 .   ? 20.275  -15.624 18.097  1.00 25.47 ? 589 HOH A O   1 
HETATM 2357 O  O   . HOH G 7 .   ? 10.577  -18.473 24.932  1.00 18.48 ? 590 HOH A O   1 
HETATM 2358 O  O   . HOH G 7 .   ? 20.684  16.008  16.056  1.00 24.54 ? 591 HOH A O   1 
HETATM 2359 O  O   . HOH G 7 .   ? 17.550  19.720  21.643  1.00 27.62 ? 592 HOH A O   1 
HETATM 2360 O  O   . HOH G 7 .   ? -4.990  -5.794  2.238   1.00 35.10 ? 593 HOH A O   1 
HETATM 2361 O  O   . HOH G 7 .   ? -3.129  1.658   1.318   1.00 27.51 ? 594 HOH A O   1 
HETATM 2362 O  O   . HOH G 7 .   ? 31.189  -3.510  -6.343  1.00 36.81 ? 595 HOH A O   1 
HETATM 2363 O  O   . HOH G 7 .   ? 10.049  2.919   33.650  1.00 19.34 ? 596 HOH A O   1 
HETATM 2364 O  O   . HOH G 7 .   ? 20.323  10.808  14.828  1.00 34.43 ? 597 HOH A O   1 
HETATM 2365 O  O   . HOH G 7 .   ? 17.547  6.650   7.580   1.00 28.35 ? 598 HOH A O   1 
HETATM 2366 O  O   . HOH G 7 .   ? 13.899  7.755   6.142   1.00 24.74 ? 599 HOH A O   1 
HETATM 2367 O  O   . HOH G 7 .   ? 16.625  -2.642  10.972  1.00 29.81 ? 600 HOH A O   1 
HETATM 2368 O  O   . HOH G 7 .   ? -0.990  -12.120 18.665  1.00 28.70 ? 601 HOH A O   1 
HETATM 2369 O  O   . HOH G 7 .   ? 5.895   -18.194 22.970  1.00 24.92 ? 602 HOH A O   1 
HETATM 2370 O  O   . HOH G 7 .   ? 17.014  -13.518 -2.052  1.00 30.65 ? 603 HOH A O   1 
HETATM 2371 O  O   . HOH G 7 .   ? 8.050   -7.034  -3.191  1.00 28.79 ? 604 HOH A O   1 
HETATM 2372 O  O   . HOH G 7 .   ? 0.183   1.410   -2.012  1.00 43.80 ? 605 HOH A O   1 
HETATM 2373 O  O   . HOH G 7 .   ? -1.512  -7.771  25.446  1.00 21.99 ? 606 HOH A O   1 
HETATM 2374 O  O   . HOH G 7 .   ? 4.965   -8.526  37.267  1.00 37.42 ? 607 HOH A O   1 
HETATM 2375 O  O   . HOH G 7 .   ? 10.532  15.349  8.673   1.00 26.38 ? 608 HOH A O   1 
HETATM 2376 O  O   . HOH G 7 .   ? 9.784   19.479  12.433  1.00 24.93 ? 609 HOH A O   1 
HETATM 2377 O  O   . HOH G 7 .   ? -0.155  -4.476  -2.559  1.00 42.57 ? 610 HOH A O   1 
HETATM 2378 O  O   . HOH G 7 .   ? 30.633  3.708   12.202  1.00 36.14 ? 611 HOH A O   1 
HETATM 2379 O  O   . HOH G 7 .   ? 23.502  9.873   27.875  1.00 30.79 ? 612 HOH A O   1 
HETATM 2380 O  O   . HOH G 7 .   ? -1.529  -10.380 24.887  1.00 27.67 ? 613 HOH A O   1 
HETATM 2381 O  O   . HOH G 7 .   ? 17.863  7.698   -1.928  1.00 35.67 ? 614 HOH A O   1 
HETATM 2382 O  O   . HOH G 7 .   ? 22.456  -4.474  34.403  1.00 29.35 ? 615 HOH A O   1 
HETATM 2383 O  O   . HOH G 7 .   ? 20.897  -14.202 27.397  1.00 34.17 ? 616 HOH A O   1 
HETATM 2384 O  O   . HOH G 7 .   ? 8.258   5.451   -6.761  1.00 27.81 ? 617 HOH A O   1 
HETATM 2385 O  O   . HOH G 7 .   ? -6.381  -5.881  26.281  1.00 34.99 ? 618 HOH A O   1 
HETATM 2386 O  O   . HOH G 7 .   ? -2.690  -0.411  28.827  1.00 33.74 ? 619 HOH A O   1 
HETATM 2387 O  O   . HOH G 7 .   ? 26.892  2.737   8.543   1.00 31.83 ? 620 HOH A O   1 
HETATM 2388 O  O   . HOH G 7 .   ? 3.947   -2.714  -5.459  1.00 37.98 ? 621 HOH A O   1 
HETATM 2389 O  O   . HOH G 7 .   ? 13.867  -6.715  -7.047  1.00 37.58 ? 622 HOH A O   1 
HETATM 2390 O  O   . HOH G 7 .   ? 5.176   5.563   35.395  1.00 36.03 ? 623 HOH A O   1 
HETATM 2391 O  O   . HOH G 7 .   ? -3.992  10.815  26.134  1.00 32.74 ? 624 HOH A O   1 
HETATM 2392 O  O   . HOH G 7 .   ? 6.017   13.421  35.138  1.00 38.90 ? 625 HOH A O   1 
HETATM 2393 O  O   . HOH G 7 .   ? 15.514  -10.762 -5.458  1.00 34.41 ? 626 HOH A O   1 
HETATM 2394 O  O   . HOH G 7 .   ? 2.691   -10.405 -3.572  1.00 28.11 ? 627 HOH A O   1 
HETATM 2395 O  O   . HOH G 7 .   ? 4.177   -15.991 24.073  1.00 42.96 ? 628 HOH A O   1 
HETATM 2396 O  O   . HOH G 7 .   ? 0.487   10.059  30.246  1.00 24.01 ? 629 HOH A O   1 
HETATM 2397 O  O   . HOH G 7 .   ? 3.818   -4.701  42.511  1.00 38.35 ? 630 HOH A O   1 
HETATM 2398 O  O   . HOH G 7 .   ? 1.233   18.076  19.170  1.00 32.96 ? 631 HOH A O   1 
HETATM 2399 O  O   . HOH G 7 .   ? 25.045  -1.285  4.617   1.00 41.24 ? 632 HOH A O   1 
HETATM 2400 O  O   . HOH G 7 .   ? 8.850   6.725   35.103  1.00 39.85 ? 633 HOH A O   1 
HETATM 2401 O  O   . HOH G 7 .   ? 4.302   2.228   -4.110  1.00 37.77 ? 634 HOH A O   1 
HETATM 2402 O  O   . HOH G 7 .   ? -3.857  12.867  19.764  1.00 30.05 ? 635 HOH A O   1 
HETATM 2403 O  O   . HOH G 7 .   ? 3.030   4.732   -6.416  1.00 31.76 ? 636 HOH A O   1 
HETATM 2404 O  O   . HOH G 7 .   ? 27.203  -9.294  15.412  1.00 37.38 ? 637 HOH A O   1 
HETATM 2405 O  O   . HOH G 7 .   ? -2.189  -15.759 20.714  1.00 33.19 ? 638 HOH A O   1 
HETATM 2406 O  O   . HOH G 7 .   ? 6.941   -7.073  -5.461  1.00 35.20 ? 639 HOH A O   1 
HETATM 2407 O  O   . HOH G 7 .   ? -0.216  -17.750 6.571   1.00 27.48 ? 640 HOH A O   1 
HETATM 2408 O  O   . HOH G 7 .   ? 18.439  -16.060 31.121  1.00 32.66 ? 641 HOH A O   1 
HETATM 2409 O  O   . HOH G 7 .   ? 21.817  9.961   13.099  1.00 38.04 ? 642 HOH A O   1 
HETATM 2410 O  O   . HOH G 7 .   ? 25.668  -9.171  17.525  1.00 40.69 ? 643 HOH A O   1 
HETATM 2411 O  O   . HOH G 7 .   ? -10.468 6.074   7.889   1.00 33.12 ? 644 HOH A O   1 
HETATM 2412 O  O   . HOH G 7 .   ? 22.970  -2.361  -12.316 1.00 27.18 ? 645 HOH A O   1 
HETATM 2413 O  O   . HOH G 7 .   ? 21.499  -7.645  -5.541  1.00 35.27 ? 646 HOH A O   1 
HETATM 2414 O  O   . HOH G 7 .   ? 21.112  2.824   -10.933 1.00 37.57 ? 647 HOH A O   1 
HETATM 2415 O  O   . HOH G 7 .   ? 33.713  1.662   12.246  1.00 42.61 ? 648 HOH A O   1 
HETATM 2416 O  O   . HOH G 7 .   ? 19.684  19.705  15.137  1.00 33.48 ? 649 HOH A O   1 
HETATM 2417 O  O   . HOH G 7 .   ? 15.529  -7.423  35.672  1.00 33.57 ? 650 HOH A O   1 
HETATM 2418 O  O   . HOH G 7 .   ? 1.584   -0.161  42.842  1.00 47.09 ? 651 HOH A O   1 
HETATM 2419 O  O   . HOH G 7 .   ? -1.891  -13.237 16.189  1.00 32.74 ? 652 HOH A O   1 
HETATM 2420 O  O   . HOH G 7 .   ? 20.570  -18.918 14.576  1.00 35.78 ? 653 HOH A O   1 
HETATM 2421 O  O   . HOH G 7 .   ? 23.145  6.350   11.977  1.00 35.73 ? 654 HOH A O   1 
HETATM 2422 O  O   . HOH G 7 .   ? 8.767   8.601   31.178  1.00 34.37 ? 655 HOH A O   1 
HETATM 2423 O  O   . HOH G 7 .   ? -7.265  12.888  16.041  1.00 34.72 ? 656 HOH A O   1 
HETATM 2424 O  O   . HOH G 7 .   ? 21.372  -5.097  -7.284  1.00 37.43 ? 657 HOH A O   1 
HETATM 2425 O  O   . HOH G 7 .   ? 13.578  -15.623 32.467  1.00 38.15 ? 658 HOH A O   1 
HETATM 2426 O  O   . HOH G 7 .   ? 27.192  -3.601  3.450   1.00 43.46 ? 659 HOH A O   1 
HETATM 2427 O  O   . HOH G 7 .   ? 15.456  -0.596  -11.573 1.00 36.66 ? 660 HOH A O   1 
HETATM 2428 O  O   . HOH G 7 .   ? 9.719   2.744   -7.920  1.00 31.07 ? 661 HOH A O   1 
HETATM 2429 O  O   . HOH G 7 .   ? 2.157   0.652   -2.949  1.00 42.38 ? 662 HOH A O   1 
HETATM 2430 O  O   . HOH G 7 .   ? 24.376  4.644   0.200   1.00 34.46 ? 663 HOH A O   1 
HETATM 2431 O  O   . HOH G 7 .   ? 17.644  -18.421 27.081  1.00 30.96 ? 664 HOH A O   1 
HETATM 2432 O  O   . HOH G 7 .   ? -6.033  -11.172 20.259  1.00 30.97 ? 665 HOH A O   1 
HETATM 2433 O  O   . HOH G 7 .   ? 19.935  9.962   10.758  1.00 44.98 ? 666 HOH A O   1 
HETATM 2434 O  O   . HOH G 7 .   ? 1.583   19.086  6.106   1.00 44.65 ? 667 HOH A O   1 
HETATM 2435 O  O   . HOH G 7 .   ? 25.673  6.340   11.307  1.00 37.48 ? 668 HOH A O   1 
HETATM 2436 O  O   . HOH G 7 .   ? 34.280  8.343   16.636  1.00 46.28 ? 669 HOH A O   1 
HETATM 2437 O  O   . HOH G 7 .   ? 31.513  8.796   15.489  1.00 29.94 ? 670 HOH A O   1 
HETATM 2438 O  O   . HOH G 7 .   ? -6.137  -3.333  27.726  1.00 31.86 ? 671 HOH A O   1 
HETATM 2439 O  O   . HOH G 7 .   ? -5.836  -8.868  22.744  1.00 30.63 ? 672 HOH A O   1 
HETATM 2440 O  O   . HOH G 7 .   ? -3.093  21.675  11.195  1.00 48.75 ? 673 HOH A O   1 
HETATM 2441 O  O   . HOH G 7 .   ? 20.336  20.608  21.400  1.00 34.50 ? 674 HOH A O   1 
HETATM 2442 O  O   . HOH G 7 .   ? -5.005  -5.941  30.370  1.00 27.57 ? 675 HOH A O   1 
HETATM 2443 O  O   . HOH G 7 .   ? -9.939  -10.900 21.583  1.00 45.22 ? 676 HOH A O   1 
HETATM 2444 O  O   . HOH G 7 .   ? 30.298  4.050   30.630  1.00 43.85 ? 677 HOH A O   1 
HETATM 2445 O  O   . HOH G 7 .   ? 26.313  -4.767  33.440  1.00 34.66 ? 678 HOH A O   1 
HETATM 2446 O  O   . HOH G 7 .   ? 26.909  -12.392 8.750   1.00 32.90 ? 679 HOH A O   1 
HETATM 2447 O  O   . HOH G 7 .   ? 15.262  22.138  26.253  1.00 28.32 ? 680 HOH A O   1 
HETATM 2448 O  O   . HOH G 7 .   ? 18.534  -15.957 5.266   0.50 31.64 ? 681 HOH A O   1 
HETATM 2449 O  O   . HOH G 7 .   ? 9.542   12.679  0.657   1.00 36.05 ? 682 HOH A O   1 
HETATM 2450 O  O   . HOH G 7 .   ? 9.061   15.681  2.228   1.00 31.54 ? 683 HOH A O   1 
HETATM 2451 O  O   . HOH G 7 .   ? 31.600  0.181   5.111   1.00 34.12 ? 684 HOH A O   1 
HETATM 2452 O  O   . HOH G 7 .   ? -6.912  0.534   28.374  1.00 32.21 ? 685 HOH A O   1 
HETATM 2453 O  O   . HOH G 7 .   ? 23.005  14.239  22.776  1.00 28.60 ? 686 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 V1F 1   302 1   V1F V1F A . 
D 4 BCN 1   303 1   BCN BCN A . 
E 5 MES 1   304 1   MES MES A . 
F 6 DMS 1   305 1   DMS DMS A . 
G 7 HOH 1   401 1   HOH HOH A . 
G 7 HOH 2   402 2   HOH HOH A . 
G 7 HOH 3   403 3   HOH HOH A . 
G 7 HOH 4   404 4   HOH HOH A . 
G 7 HOH 5   405 5   HOH HOH A . 
G 7 HOH 6   406 6   HOH HOH A . 
G 7 HOH 7   407 7   HOH HOH A . 
G 7 HOH 8   408 8   HOH HOH A . 
G 7 HOH 9   409 9   HOH HOH A . 
G 7 HOH 10  410 10  HOH HOH A . 
G 7 HOH 11  411 11  HOH HOH A . 
G 7 HOH 12  412 12  HOH HOH A . 
G 7 HOH 13  413 13  HOH HOH A . 
G 7 HOH 14  414 14  HOH HOH A . 
G 7 HOH 15  415 15  HOH HOH A . 
G 7 HOH 16  416 16  HOH HOH A . 
G 7 HOH 17  417 17  HOH HOH A . 
G 7 HOH 18  418 18  HOH HOH A . 
G 7 HOH 19  419 19  HOH HOH A . 
G 7 HOH 20  420 20  HOH HOH A . 
G 7 HOH 21  421 21  HOH HOH A . 
G 7 HOH 22  422 22  HOH HOH A . 
G 7 HOH 23  423 23  HOH HOH A . 
G 7 HOH 24  424 24  HOH HOH A . 
G 7 HOH 25  425 25  HOH HOH A . 
G 7 HOH 26  426 26  HOH HOH A . 
G 7 HOH 27  427 27  HOH HOH A . 
G 7 HOH 28  428 28  HOH HOH A . 
G 7 HOH 29  429 29  HOH HOH A . 
G 7 HOH 30  430 30  HOH HOH A . 
G 7 HOH 31  431 31  HOH HOH A . 
G 7 HOH 32  432 32  HOH HOH A . 
G 7 HOH 33  433 33  HOH HOH A . 
G 7 HOH 34  434 34  HOH HOH A . 
G 7 HOH 35  435 35  HOH HOH A . 
G 7 HOH 36  436 36  HOH HOH A . 
G 7 HOH 37  437 37  HOH HOH A . 
G 7 HOH 38  438 38  HOH HOH A . 
G 7 HOH 39  439 39  HOH HOH A . 
G 7 HOH 40  440 40  HOH HOH A . 
G 7 HOH 41  441 41  HOH HOH A . 
G 7 HOH 42  442 42  HOH HOH A . 
G 7 HOH 43  443 43  HOH HOH A . 
G 7 HOH 44  444 44  HOH HOH A . 
G 7 HOH 45  445 45  HOH HOH A . 
G 7 HOH 46  446 46  HOH HOH A . 
G 7 HOH 47  447 47  HOH HOH A . 
G 7 HOH 48  448 48  HOH HOH A . 
G 7 HOH 49  449 49  HOH HOH A . 
G 7 HOH 50  450 50  HOH HOH A . 
G 7 HOH 51  451 51  HOH HOH A . 
G 7 HOH 52  452 52  HOH HOH A . 
G 7 HOH 53  453 53  HOH HOH A . 
G 7 HOH 54  454 54  HOH HOH A . 
G 7 HOH 55  455 55  HOH HOH A . 
G 7 HOH 56  456 56  HOH HOH A . 
G 7 HOH 57  457 57  HOH HOH A . 
G 7 HOH 58  458 58  HOH HOH A . 
G 7 HOH 59  459 59  HOH HOH A . 
G 7 HOH 60  460 60  HOH HOH A . 
G 7 HOH 61  461 61  HOH HOH A . 
G 7 HOH 62  462 62  HOH HOH A . 
G 7 HOH 63  463 63  HOH HOH A . 
G 7 HOH 64  464 64  HOH HOH A . 
G 7 HOH 65  465 65  HOH HOH A . 
G 7 HOH 66  466 66  HOH HOH A . 
G 7 HOH 67  467 67  HOH HOH A . 
G 7 HOH 68  468 68  HOH HOH A . 
G 7 HOH 69  469 69  HOH HOH A . 
G 7 HOH 70  470 70  HOH HOH A . 
G 7 HOH 71  471 71  HOH HOH A . 
G 7 HOH 72  472 72  HOH HOH A . 
G 7 HOH 73  473 73  HOH HOH A . 
G 7 HOH 74  474 74  HOH HOH A . 
G 7 HOH 75  475 75  HOH HOH A . 
G 7 HOH 76  476 76  HOH HOH A . 
G 7 HOH 77  477 77  HOH HOH A . 
G 7 HOH 78  478 78  HOH HOH A . 
G 7 HOH 79  479 79  HOH HOH A . 
G 7 HOH 80  480 80  HOH HOH A . 
G 7 HOH 81  481 81  HOH HOH A . 
G 7 HOH 82  482 82  HOH HOH A . 
G 7 HOH 83  483 83  HOH HOH A . 
G 7 HOH 84  484 84  HOH HOH A . 
G 7 HOH 85  485 85  HOH HOH A . 
G 7 HOH 86  486 86  HOH HOH A . 
G 7 HOH 87  487 87  HOH HOH A . 
G 7 HOH 88  488 88  HOH HOH A . 
G 7 HOH 89  489 89  HOH HOH A . 
G 7 HOH 90  490 90  HOH HOH A . 
G 7 HOH 91  491 91  HOH HOH A . 
G 7 HOH 92  492 92  HOH HOH A . 
G 7 HOH 93  493 93  HOH HOH A . 
G 7 HOH 94  494 94  HOH HOH A . 
G 7 HOH 95  495 95  HOH HOH A . 
G 7 HOH 96  496 96  HOH HOH A . 
G 7 HOH 97  497 97  HOH HOH A . 
G 7 HOH 98  498 98  HOH HOH A . 
G 7 HOH 99  499 99  HOH HOH A . 
G 7 HOH 100 500 100 HOH HOH A . 
G 7 HOH 101 501 101 HOH HOH A . 
G 7 HOH 102 502 102 HOH HOH A . 
G 7 HOH 103 503 103 HOH HOH A . 
G 7 HOH 104 504 104 HOH HOH A . 
G 7 HOH 105 505 105 HOH HOH A . 
G 7 HOH 106 506 106 HOH HOH A . 
G 7 HOH 107 507 107 HOH HOH A . 
G 7 HOH 108 508 108 HOH HOH A . 
G 7 HOH 109 509 109 HOH HOH A . 
G 7 HOH 110 510 110 HOH HOH A . 
G 7 HOH 111 511 111 HOH HOH A . 
G 7 HOH 112 512 112 HOH HOH A . 
G 7 HOH 113 513 113 HOH HOH A . 
G 7 HOH 114 514 114 HOH HOH A . 
G 7 HOH 115 515 115 HOH HOH A . 
G 7 HOH 116 516 116 HOH HOH A . 
G 7 HOH 117 517 117 HOH HOH A . 
G 7 HOH 118 518 118 HOH HOH A . 
G 7 HOH 119 519 119 HOH HOH A . 
G 7 HOH 120 520 120 HOH HOH A . 
G 7 HOH 121 521 121 HOH HOH A . 
G 7 HOH 122 522 122 HOH HOH A . 
G 7 HOH 123 523 123 HOH HOH A . 
G 7 HOH 124 524 124 HOH HOH A . 
G 7 HOH 125 525 125 HOH HOH A . 
G 7 HOH 126 526 126 HOH HOH A . 
G 7 HOH 127 527 127 HOH HOH A . 
G 7 HOH 128 528 128 HOH HOH A . 
G 7 HOH 129 529 129 HOH HOH A . 
G 7 HOH 130 530 130 HOH HOH A . 
G 7 HOH 131 531 131 HOH HOH A . 
G 7 HOH 132 532 132 HOH HOH A . 
G 7 HOH 133 533 133 HOH HOH A . 
G 7 HOH 134 534 134 HOH HOH A . 
G 7 HOH 135 535 135 HOH HOH A . 
G 7 HOH 136 536 136 HOH HOH A . 
G 7 HOH 137 537 137 HOH HOH A . 
G 7 HOH 138 538 138 HOH HOH A . 
G 7 HOH 139 539 139 HOH HOH A . 
G 7 HOH 140 540 140 HOH HOH A . 
G 7 HOH 141 541 141 HOH HOH A . 
G 7 HOH 142 542 142 HOH HOH A . 
G 7 HOH 143 543 143 HOH HOH A . 
G 7 HOH 144 544 144 HOH HOH A . 
G 7 HOH 145 545 145 HOH HOH A . 
G 7 HOH 146 546 146 HOH HOH A . 
G 7 HOH 147 547 147 HOH HOH A . 
G 7 HOH 148 548 148 HOH HOH A . 
G 7 HOH 149 549 149 HOH HOH A . 
G 7 HOH 150 550 150 HOH HOH A . 
G 7 HOH 151 551 151 HOH HOH A . 
G 7 HOH 152 552 152 HOH HOH A . 
G 7 HOH 153 553 153 HOH HOH A . 
G 7 HOH 154 554 154 HOH HOH A . 
G 7 HOH 155 555 155 HOH HOH A . 
G 7 HOH 156 556 156 HOH HOH A . 
G 7 HOH 157 557 157 HOH HOH A . 
G 7 HOH 158 558 158 HOH HOH A . 
G 7 HOH 159 559 159 HOH HOH A . 
G 7 HOH 160 560 160 HOH HOH A . 
G 7 HOH 161 561 161 HOH HOH A . 
G 7 HOH 162 562 162 HOH HOH A . 
G 7 HOH 163 563 163 HOH HOH A . 
G 7 HOH 164 564 164 HOH HOH A . 
G 7 HOH 165 565 165 HOH HOH A . 
G 7 HOH 166 566 166 HOH HOH A . 
G 7 HOH 167 567 167 HOH HOH A . 
G 7 HOH 168 568 168 HOH HOH A . 
G 7 HOH 169 569 169 HOH HOH A . 
G 7 HOH 170 570 170 HOH HOH A . 
G 7 HOH 171 571 171 HOH HOH A . 
G 7 HOH 172 572 172 HOH HOH A . 
G 7 HOH 173 573 173 HOH HOH A . 
G 7 HOH 174 574 174 HOH HOH A . 
G 7 HOH 175 575 175 HOH HOH A . 
G 7 HOH 176 576 176 HOH HOH A . 
G 7 HOH 177 577 177 HOH HOH A . 
G 7 HOH 178 578 178 HOH HOH A . 
G 7 HOH 179 579 179 HOH HOH A . 
G 7 HOH 180 580 180 HOH HOH A . 
G 7 HOH 181 581 181 HOH HOH A . 
G 7 HOH 182 582 182 HOH HOH A . 
G 7 HOH 183 583 183 HOH HOH A . 
G 7 HOH 184 584 184 HOH HOH A . 
G 7 HOH 185 585 185 HOH HOH A . 
G 7 HOH 186 586 186 HOH HOH A . 
G 7 HOH 187 587 187 HOH HOH A . 
G 7 HOH 188 588 188 HOH HOH A . 
G 7 HOH 189 589 189 HOH HOH A . 
G 7 HOH 190 590 190 HOH HOH A . 
G 7 HOH 191 591 191 HOH HOH A . 
G 7 HOH 192 592 192 HOH HOH A . 
G 7 HOH 193 593 193 HOH HOH A . 
G 7 HOH 194 594 194 HOH HOH A . 
G 7 HOH 195 595 195 HOH HOH A . 
G 7 HOH 196 596 196 HOH HOH A . 
G 7 HOH 197 597 197 HOH HOH A . 
G 7 HOH 198 598 198 HOH HOH A . 
G 7 HOH 199 599 199 HOH HOH A . 
G 7 HOH 200 600 200 HOH HOH A . 
G 7 HOH 201 601 201 HOH HOH A . 
G 7 HOH 202 602 202 HOH HOH A . 
G 7 HOH 203 603 203 HOH HOH A . 
G 7 HOH 204 604 204 HOH HOH A . 
G 7 HOH 205 605 205 HOH HOH A . 
G 7 HOH 206 606 206 HOH HOH A . 
G 7 HOH 207 607 207 HOH HOH A . 
G 7 HOH 208 608 208 HOH HOH A . 
G 7 HOH 209 609 209 HOH HOH A . 
G 7 HOH 210 610 210 HOH HOH A . 
G 7 HOH 211 611 211 HOH HOH A . 
G 7 HOH 212 612 212 HOH HOH A . 
G 7 HOH 213 613 213 HOH HOH A . 
G 7 HOH 214 614 214 HOH HOH A . 
G 7 HOH 215 615 215 HOH HOH A . 
G 7 HOH 216 616 216 HOH HOH A . 
G 7 HOH 217 617 217 HOH HOH A . 
G 7 HOH 218 618 218 HOH HOH A . 
G 7 HOH 219 619 219 HOH HOH A . 
G 7 HOH 220 620 220 HOH HOH A . 
G 7 HOH 221 621 221 HOH HOH A . 
G 7 HOH 222 622 223 HOH HOH A . 
G 7 HOH 223 623 224 HOH HOH A . 
G 7 HOH 224 624 225 HOH HOH A . 
G 7 HOH 225 625 226 HOH HOH A . 
G 7 HOH 226 626 227 HOH HOH A . 
G 7 HOH 227 627 228 HOH HOH A . 
G 7 HOH 228 628 229 HOH HOH A . 
G 7 HOH 229 629 230 HOH HOH A . 
G 7 HOH 230 630 231 HOH HOH A . 
G 7 HOH 231 631 232 HOH HOH A . 
G 7 HOH 232 632 233 HOH HOH A . 
G 7 HOH 233 633 234 HOH HOH A . 
G 7 HOH 234 634 235 HOH HOH A . 
G 7 HOH 235 635 236 HOH HOH A . 
G 7 HOH 236 636 238 HOH HOH A . 
G 7 HOH 237 637 239 HOH HOH A . 
G 7 HOH 238 638 240 HOH HOH A . 
G 7 HOH 239 639 241 HOH HOH A . 
G 7 HOH 240 640 242 HOH HOH A . 
G 7 HOH 241 641 243 HOH HOH A . 
G 7 HOH 242 642 244 HOH HOH A . 
G 7 HOH 243 643 245 HOH HOH A . 
G 7 HOH 244 644 246 HOH HOH A . 
G 7 HOH 245 645 247 HOH HOH A . 
G 7 HOH 246 646 248 HOH HOH A . 
G 7 HOH 247 647 249 HOH HOH A . 
G 7 HOH 248 648 250 HOH HOH A . 
G 7 HOH 249 649 251 HOH HOH A . 
G 7 HOH 250 650 252 HOH HOH A . 
G 7 HOH 251 651 253 HOH HOH A . 
G 7 HOH 252 652 254 HOH HOH A . 
G 7 HOH 253 653 255 HOH HOH A . 
G 7 HOH 254 654 256 HOH HOH A . 
G 7 HOH 255 655 257 HOH HOH A . 
G 7 HOH 256 656 258 HOH HOH A . 
G 7 HOH 257 657 259 HOH HOH A . 
G 7 HOH 258 658 260 HOH HOH A . 
G 7 HOH 259 659 261 HOH HOH A . 
G 7 HOH 260 660 262 HOH HOH A . 
G 7 HOH 261 661 263 HOH HOH A . 
G 7 HOH 262 662 264 HOH HOH A . 
G 7 HOH 263 663 265 HOH HOH A . 
G 7 HOH 264 664 266 HOH HOH A . 
G 7 HOH 265 665 267 HOH HOH A . 
G 7 HOH 266 666 268 HOH HOH A . 
G 7 HOH 267 667 269 HOH HOH A . 
G 7 HOH 268 668 270 HOH HOH A . 
G 7 HOH 269 669 271 HOH HOH A . 
G 7 HOH 270 670 272 HOH HOH A . 
G 7 HOH 271 671 273 HOH HOH A . 
G 7 HOH 272 672 274 HOH HOH A . 
G 7 HOH 273 673 275 HOH HOH A . 
G 7 HOH 274 674 276 HOH HOH A . 
G 7 HOH 275 675 277 HOH HOH A . 
G 7 HOH 276 676 278 HOH HOH A . 
G 7 HOH 277 677 279 HOH HOH A . 
G 7 HOH 278 678 280 HOH HOH A . 
G 7 HOH 279 679 281 HOH HOH A . 
G 7 HOH 280 680 282 HOH HOH A . 
G 7 HOH 281 681 284 HOH HOH A . 
G 7 HOH 282 682 285 HOH HOH A . 
G 7 HOH 283 683 286 HOH HOH A . 
G 7 HOH 284 684 287 HOH HOH A . 
G 7 HOH 285 685 288 HOH HOH A . 
G 7 HOH 286 686 289 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.9 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 114.1 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.2  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C V1F .   ? A V1F 302 ? 1_555 109.5 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C V1F .   ? A V1F 302 ? 1_555 113.3 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C V1F .   ? A V1F 302 ? 1_555 116.7 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-04-15 
2 'Structure model' 1 1 2023-11-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' pdbx_initial_refinement_model 
5 2 'Structure model' pdbx_struct_conn_angle        
6 2 'Structure model' struct_conn                   
7 2 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_database_2.pdbx_DOI'                        
2  2 'Structure model' '_database_2.pdbx_database_accession'         
3  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
15 2 'Structure model' '_pdbx_struct_conn_angle.value'               
16 2 'Structure model' '_struct_conn.pdbx_dist_value'                
17 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
18 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
19 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
20 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
21 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
22 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
23 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
24 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
25 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
26 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
27 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
28 2 'Structure model' '_struct_site.pdbx_auth_asym_id'              
29 2 'Structure model' '_struct_site.pdbx_auth_comp_id'              
30 2 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.3.20 2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
HKL-2000    .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 76  ? ? -110.91 -85.04  
2 1 ASN A 244 ? ? -97.42  51.43   
3 1 LYS A 252 ? ? 55.12   -136.01 
# 
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 304 ? S   ? E MES 1 S   
2 1 N 1 A MES 304 ? O1S ? E MES 1 O1S 
3 1 N 1 A MES 304 ? O2S ? E MES 1 O2S 
4 1 N 1 A MES 304 ? O3S ? E 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 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
LEU N    N  N N 217 
LEU CA   C  N S 218 
LEU C    C  N N 219 
LEU O    O  N N 220 
LEU CB   C  N N 221 
LEU CG   C  N N 222 
LEU CD1  C  N N 223 
LEU CD2  C  N N 224 
LEU OXT  O  N N 225 
LEU H    H  N N 226 
LEU H2   H  N N 227 
LEU HA   H  N N 228 
LEU HB2  H  N N 229 
LEU HB3  H  N N 230 
LEU HG   H  N N 231 
LEU HD11 H  N N 232 
LEU HD12 H  N N 233 
LEU HD13 H  N N 234 
LEU HD21 H  N N 235 
LEU HD22 H  N N 236 
LEU HD23 H  N N 237 
LEU HXT  H  N N 238 
LYS N    N  N N 239 
LYS CA   C  N S 240 
LYS C    C  N N 241 
LYS O    O  N N 242 
LYS CB   C  N N 243 
LYS CG   C  N N 244 
LYS CD   C  N N 245 
LYS CE   C  N N 246 
LYS NZ   N  N N 247 
LYS OXT  O  N N 248 
LYS H    H  N N 249 
LYS H2   H  N N 250 
LYS HA   H  N N 251 
LYS HB2  H  N N 252 
LYS HB3  H  N N 253 
LYS HG2  H  N N 254 
LYS HG3  H  N N 255 
LYS HD2  H  N N 256 
LYS HD3  H  N N 257 
LYS HE2  H  N N 258 
LYS HE3  H  N N 259 
LYS HZ1  H  N N 260 
LYS HZ2  H  N N 261 
LYS HZ3  H  N N 262 
LYS HXT  H  N N 263 
MES O1   O  N N 264 
MES C2   C  N N 265 
MES C3   C  N N 266 
MES N4   N  N N 267 
MES C5   C  N N 268 
MES C6   C  N N 269 
MES C7   C  N N 270 
MES C8   C  N N 271 
MES S    S  N N 272 
MES O1S  O  N N 273 
MES O2S  O  N N 274 
MES O3S  O  N N 275 
MES H21  H  N N 276 
MES H22  H  N N 277 
MES H31  H  N N 278 
MES H32  H  N N 279 
MES HN4  H  N N 280 
MES H51  H  N N 281 
MES H52  H  N N 282 
MES H61  H  N N 283 
MES H62  H  N N 284 
MES H71  H  N N 285 
MES H72  H  N N 286 
MES H81  H  N N 287 
MES H82  H  N N 288 
MET N    N  N N 289 
MET CA   C  N S 290 
MET C    C  N N 291 
MET O    O  N N 292 
MET CB   C  N N 293 
MET CG   C  N N 294 
MET SD   S  N N 295 
MET CE   C  N N 296 
MET OXT  O  N N 297 
MET H    H  N N 298 
MET H2   H  N N 299 
MET HA   H  N N 300 
MET HB2  H  N N 301 
MET HB3  H  N N 302 
MET HG2  H  N N 303 
MET HG3  H  N N 304 
MET HE1  H  N N 305 
MET HE2  H  N N 306 
MET HE3  H  N N 307 
MET HXT  H  N N 308 
PHE N    N  N N 309 
PHE CA   C  N S 310 
PHE C    C  N N 311 
PHE O    O  N N 312 
PHE CB   C  N N 313 
PHE CG   C  Y N 314 
PHE CD1  C  Y N 315 
PHE CD2  C  Y N 316 
PHE CE1  C  Y N 317 
PHE CE2  C  Y N 318 
PHE CZ   C  Y N 319 
PHE OXT  O  N N 320 
PHE H    H  N N 321 
PHE H2   H  N N 322 
PHE HA   H  N N 323 
PHE HB2  H  N N 324 
PHE HB3  H  N N 325 
PHE HD1  H  N N 326 
PHE HD2  H  N N 327 
PHE HE1  H  N N 328 
PHE HE2  H  N N 329 
PHE HZ   H  N N 330 
PHE HXT  H  N N 331 
PRO N    N  N N 332 
PRO CA   C  N S 333 
PRO C    C  N N 334 
PRO O    O  N N 335 
PRO CB   C  N N 336 
PRO CG   C  N N 337 
PRO CD   C  N N 338 
PRO OXT  O  N N 339 
PRO H    H  N N 340 
PRO HA   H  N N 341 
PRO HB2  H  N N 342 
PRO HB3  H  N N 343 
PRO HG2  H  N N 344 
PRO HG3  H  N N 345 
PRO HD2  H  N N 346 
PRO HD3  H  N N 347 
PRO HXT  H  N N 348 
SER N    N  N N 349 
SER CA   C  N S 350 
SER C    C  N N 351 
SER O    O  N N 352 
SER CB   C  N N 353 
SER OG   O  N N 354 
SER OXT  O  N N 355 
SER H    H  N N 356 
SER H2   H  N N 357 
SER HA   H  N N 358 
SER HB2  H  N N 359 
SER HB3  H  N N 360 
SER HG   H  N N 361 
SER HXT  H  N N 362 
THR N    N  N N 363 
THR CA   C  N S 364 
THR C    C  N N 365 
THR O    O  N N 366 
THR CB   C  N R 367 
THR OG1  O  N N 368 
THR CG2  C  N N 369 
THR OXT  O  N N 370 
THR H    H  N N 371 
THR H2   H  N N 372 
THR HA   H  N N 373 
THR HB   H  N N 374 
THR HG1  H  N N 375 
THR HG21 H  N N 376 
THR HG22 H  N N 377 
THR HG23 H  N N 378 
THR HXT  H  N N 379 
TRP N    N  N N 380 
TRP CA   C  N S 381 
TRP C    C  N N 382 
TRP O    O  N N 383 
TRP CB   C  N N 384 
TRP CG   C  Y N 385 
TRP CD1  C  Y N 386 
TRP CD2  C  Y N 387 
TRP NE1  N  Y N 388 
TRP CE2  C  Y N 389 
TRP CE3  C  Y N 390 
TRP CZ2  C  Y N 391 
TRP CZ3  C  Y N 392 
TRP CH2  C  Y N 393 
TRP OXT  O  N N 394 
TRP H    H  N N 395 
TRP H2   H  N N 396 
TRP HA   H  N N 397 
TRP HB2  H  N N 398 
TRP HB3  H  N N 399 
TRP HD1  H  N N 400 
TRP HE1  H  N N 401 
TRP HE3  H  N N 402 
TRP HZ2  H  N N 403 
TRP HZ3  H  N N 404 
TRP HH2  H  N N 405 
TRP HXT  H  N N 406 
TYR N    N  N N 407 
TYR CA   C  N S 408 
TYR C    C  N N 409 
TYR O    O  N N 410 
TYR CB   C  N N 411 
TYR CG   C  Y N 412 
TYR CD1  C  Y N 413 
TYR CD2  C  Y N 414 
TYR CE1  C  Y N 415 
TYR CE2  C  Y N 416 
TYR CZ   C  Y N 417 
TYR OH   O  N N 418 
TYR OXT  O  N N 419 
TYR H    H  N N 420 
TYR H2   H  N N 421 
TYR HA   H  N N 422 
TYR HB2  H  N N 423 
TYR HB3  H  N N 424 
TYR HD1  H  N N 425 
TYR HD2  H  N N 426 
TYR HE1  H  N N 427 
TYR HE2  H  N N 428 
TYR HH   H  N N 429 
TYR HXT  H  N N 430 
V1F F26  F  N N 431 
V1F C5   C  Y N 432 
V1F C4   C  Y N 433 
V1F S7   S  N N 434 
V1F O9   O  N N 435 
V1F N10  N  N N 436 
V1F O8   O  N N 437 
V1F C3   C  Y N 438 
V1F F12  F  N N 439 
V1F C2   C  Y N 440 
V1F F13  F  N N 441 
V1F C6   C  Y N 442 
V1F C1   C  Y N 443 
V1F S11  S  N N 444 
V1F O22  O  N N 445 
V1F O23  O  N N 446 
V1F C21  C  N N 447 
V1F C24  C  N N 448 
V1F C30  C  Y N 449 
V1F C29  C  Y N 450 
V1F C28  C  Y N 451 
V1F C32  C  Y N 452 
V1F C31  C  Y N 453 
V1F C27  C  Y N 454 
V1F N25  N  N N 455 
V1F C14  C  N N 456 
V1F C15  C  Y N 457 
V1F C20  C  Y N 458 
V1F C19  C  Y N 459 
V1F C18  C  Y N 460 
V1F C17  C  Y N 461 
V1F C16  C  Y N 462 
V1F H1   H  N N 463 
V1F H2   H  N N 464 
V1F H3   H  N N 465 
V1F H4   H  N N 466 
V1F H5   H  N N 467 
V1F H6   H  N N 468 
V1F H7   H  N N 469 
V1F H8   H  N N 470 
V1F H9   H  N N 471 
V1F H10  H  N N 472 
V1F H11  H  N N 473 
V1F H12  H  N N 474 
V1F H13  H  N N 475 
V1F H14  H  N N 476 
V1F H15  H  N N 477 
V1F H16  H  N N 478 
V1F H17  H  N N 479 
V1F H18  H  N N 480 
V1F H19  H  N N 481 
VAL N    N  N N 482 
VAL CA   C  N S 483 
VAL C    C  N N 484 
VAL O    O  N N 485 
VAL CB   C  N N 486 
VAL CG1  C  N N 487 
VAL CG2  C  N N 488 
VAL OXT  O  N N 489 
VAL H    H  N N 490 
VAL H2   H  N N 491 
VAL HA   H  N N 492 
VAL HB   H  N N 493 
VAL HG11 H  N N 494 
VAL HG12 H  N N 495 
VAL HG13 H  N N 496 
VAL HG21 H  N N 497 
VAL HG22 H  N N 498 
VAL HG23 H  N N 499 
VAL HXT  H  N N 500 
ZN  ZN   ZN N N 501 
# 
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 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
LEU N   CA   sing N N 205 
LEU N   H    sing N N 206 
LEU N   H2   sing N N 207 
LEU CA  C    sing N N 208 
LEU CA  CB   sing N N 209 
LEU CA  HA   sing N N 210 
LEU C   O    doub N N 211 
LEU C   OXT  sing N N 212 
LEU CB  CG   sing N N 213 
LEU CB  HB2  sing N N 214 
LEU CB  HB3  sing N N 215 
LEU CG  CD1  sing N N 216 
LEU CG  CD2  sing N N 217 
LEU CG  HG   sing N N 218 
LEU CD1 HD11 sing N N 219 
LEU CD1 HD12 sing N N 220 
LEU CD1 HD13 sing N N 221 
LEU CD2 HD21 sing N N 222 
LEU CD2 HD22 sing N N 223 
LEU CD2 HD23 sing N N 224 
LEU OXT HXT  sing N N 225 
LYS N   CA   sing N N 226 
LYS N   H    sing N N 227 
LYS N   H2   sing N N 228 
LYS CA  C    sing N N 229 
LYS CA  CB   sing N N 230 
LYS CA  HA   sing N N 231 
LYS C   O    doub N N 232 
LYS C   OXT  sing N N 233 
LYS CB  CG   sing N N 234 
LYS CB  HB2  sing N N 235 
LYS CB  HB3  sing N N 236 
LYS CG  CD   sing N N 237 
LYS CG  HG2  sing N N 238 
LYS CG  HG3  sing N N 239 
LYS CD  CE   sing N N 240 
LYS CD  HD2  sing N N 241 
LYS CD  HD3  sing N N 242 
LYS CE  NZ   sing N N 243 
LYS CE  HE2  sing N N 244 
LYS CE  HE3  sing N N 245 
LYS NZ  HZ1  sing N N 246 
LYS NZ  HZ2  sing N N 247 
LYS NZ  HZ3  sing N N 248 
LYS OXT HXT  sing N N 249 
MES O1  C2   sing N N 250 
MES O1  C6   sing N N 251 
MES C2  C3   sing N N 252 
MES C2  H21  sing N N 253 
MES C2  H22  sing N N 254 
MES C3  N4   sing N N 255 
MES C3  H31  sing N N 256 
MES C3  H32  sing N N 257 
MES N4  C5   sing N N 258 
MES N4  C7   sing N N 259 
MES N4  HN4  sing N N 260 
MES C5  C6   sing N N 261 
MES C5  H51  sing N N 262 
MES C5  H52  sing N N 263 
MES C6  H61  sing N N 264 
MES C6  H62  sing N N 265 
MES C7  C8   sing N N 266 
MES C7  H71  sing N N 267 
MES C7  H72  sing N N 268 
MES C8  S    sing N N 269 
MES C8  H81  sing N N 270 
MES C8  H82  sing N N 271 
MES S   O1S  doub N N 272 
MES S   O2S  doub N N 273 
MES S   O3S  sing N N 274 
MET N   CA   sing N N 275 
MET N   H    sing N N 276 
MET N   H2   sing N N 277 
MET CA  C    sing N N 278 
MET CA  CB   sing N N 279 
MET CA  HA   sing N N 280 
MET C   O    doub N N 281 
MET C   OXT  sing N N 282 
MET CB  CG   sing N N 283 
MET CB  HB2  sing N N 284 
MET CB  HB3  sing N N 285 
MET CG  SD   sing N N 286 
MET CG  HG2  sing N N 287 
MET CG  HG3  sing N N 288 
MET SD  CE   sing N N 289 
MET CE  HE1  sing N N 290 
MET CE  HE2  sing N N 291 
MET CE  HE3  sing N N 292 
MET OXT HXT  sing N N 293 
PHE N   CA   sing N N 294 
PHE N   H    sing N N 295 
PHE N   H2   sing N N 296 
PHE CA  C    sing N N 297 
PHE CA  CB   sing N N 298 
PHE CA  HA   sing N N 299 
PHE C   O    doub N N 300 
PHE C   OXT  sing N N 301 
PHE CB  CG   sing N N 302 
PHE CB  HB2  sing N N 303 
PHE CB  HB3  sing N N 304 
PHE CG  CD1  doub Y N 305 
PHE CG  CD2  sing Y N 306 
PHE CD1 CE1  sing Y N 307 
PHE CD1 HD1  sing N N 308 
PHE CD2 CE2  doub Y N 309 
PHE CD2 HD2  sing N N 310 
PHE CE1 CZ   doub Y N 311 
PHE CE1 HE1  sing N N 312 
PHE CE2 CZ   sing Y N 313 
PHE CE2 HE2  sing N N 314 
PHE CZ  HZ   sing N N 315 
PHE OXT HXT  sing N N 316 
PRO N   CA   sing N N 317 
PRO N   CD   sing N N 318 
PRO N   H    sing N N 319 
PRO CA  C    sing N N 320 
PRO CA  CB   sing N N 321 
PRO CA  HA   sing N N 322 
PRO C   O    doub N N 323 
PRO C   OXT  sing N N 324 
PRO CB  CG   sing N N 325 
PRO CB  HB2  sing N N 326 
PRO CB  HB3  sing N N 327 
PRO CG  CD   sing N N 328 
PRO CG  HG2  sing N N 329 
PRO CG  HG3  sing N N 330 
PRO CD  HD2  sing N N 331 
PRO CD  HD3  sing N N 332 
PRO OXT HXT  sing N N 333 
SER N   CA   sing N N 334 
SER N   H    sing N N 335 
SER N   H2   sing N N 336 
SER CA  C    sing N N 337 
SER CA  CB   sing N N 338 
SER CA  HA   sing N N 339 
SER C   O    doub N N 340 
SER C   OXT  sing N N 341 
SER CB  OG   sing N N 342 
SER CB  HB2  sing N N 343 
SER CB  HB3  sing N N 344 
SER OG  HG   sing N N 345 
SER OXT HXT  sing N N 346 
THR N   CA   sing N N 347 
THR N   H    sing N N 348 
THR N   H2   sing N N 349 
THR CA  C    sing N N 350 
THR CA  CB   sing N N 351 
THR CA  HA   sing N N 352 
THR C   O    doub N N 353 
THR C   OXT  sing N N 354 
THR CB  OG1  sing N N 355 
THR CB  CG2  sing N N 356 
THR CB  HB   sing N N 357 
THR OG1 HG1  sing N N 358 
THR CG2 HG21 sing N N 359 
THR CG2 HG22 sing N N 360 
THR CG2 HG23 sing N N 361 
THR OXT HXT  sing N N 362 
TRP N   CA   sing N N 363 
TRP N   H    sing N N 364 
TRP N   H2   sing N N 365 
TRP CA  C    sing N N 366 
TRP CA  CB   sing N N 367 
TRP CA  HA   sing N N 368 
TRP C   O    doub N N 369 
TRP C   OXT  sing N N 370 
TRP CB  CG   sing N N 371 
TRP CB  HB2  sing N N 372 
TRP CB  HB3  sing N N 373 
TRP CG  CD1  doub Y N 374 
TRP CG  CD2  sing Y N 375 
TRP CD1 NE1  sing Y N 376 
TRP CD1 HD1  sing N N 377 
TRP CD2 CE2  doub Y N 378 
TRP CD2 CE3  sing Y N 379 
TRP NE1 CE2  sing Y N 380 
TRP NE1 HE1  sing N N 381 
TRP CE2 CZ2  sing Y N 382 
TRP CE3 CZ3  doub Y N 383 
TRP CE3 HE3  sing N N 384 
TRP CZ2 CH2  doub Y N 385 
TRP CZ2 HZ2  sing N N 386 
TRP CZ3 CH2  sing Y N 387 
TRP CZ3 HZ3  sing N N 388 
TRP CH2 HH2  sing N N 389 
TRP OXT HXT  sing N N 390 
TYR N   CA   sing N N 391 
TYR N   H    sing N N 392 
TYR N   H2   sing N N 393 
TYR CA  C    sing N N 394 
TYR CA  CB   sing N N 395 
TYR CA  HA   sing N N 396 
TYR C   O    doub N N 397 
TYR C   OXT  sing N N 398 
TYR CB  CG   sing N N 399 
TYR CB  HB2  sing N N 400 
TYR CB  HB3  sing N N 401 
TYR CG  CD1  doub Y N 402 
TYR CG  CD2  sing Y N 403 
TYR CD1 CE1  sing Y N 404 
TYR CD1 HD1  sing N N 405 
TYR CD2 CE2  doub Y N 406 
TYR CD2 HD2  sing N N 407 
TYR CE1 CZ   doub Y N 408 
TYR CE1 HE1  sing N N 409 
TYR CE2 CZ   sing Y N 410 
TYR CE2 HE2  sing N N 411 
TYR CZ  OH   sing N N 412 
TYR OH  HH   sing N N 413 
TYR OXT HXT  sing N N 414 
V1F C17 C18  doub Y N 415 
V1F C17 C16  sing Y N 416 
V1F C18 C19  sing Y N 417 
V1F C16 C15  doub Y N 418 
V1F C31 C32  doub Y N 419 
V1F C31 C27  sing Y N 420 
V1F C32 C30  sing Y N 421 
V1F C19 C20  doub Y N 422 
V1F C27 C28  doub Y N 423 
V1F C30 C24  sing N N 424 
V1F C30 C29  doub Y N 425 
V1F C24 C21  sing N N 426 
V1F C15 C20  sing Y N 427 
V1F C15 C14  sing N N 428 
V1F C28 C29  sing Y N 429 
V1F C14 N25  sing N N 430 
V1F C21 S11  sing N N 431 
V1F O23 S11  doub N N 432 
V1F N25 C6   sing N N 433 
V1F S11 C1   sing N N 434 
V1F S11 O22  doub N N 435 
V1F C6  C1   doub Y N 436 
V1F C6  C5   sing Y N 437 
V1F C1  C2   sing Y N 438 
V1F F26 C5   sing N N 439 
V1F C5  C4   doub Y N 440 
V1F C2  F13  sing N N 441 
V1F C2  C3   doub Y N 442 
V1F C4  C3   sing Y N 443 
V1F C4  S7   sing N N 444 
V1F C3  F12  sing N N 445 
V1F N10 S7   sing N N 446 
V1F O9  S7   doub N N 447 
V1F S7  O8   doub N N 448 
V1F N10 H1   sing N N 449 
V1F N10 H2   sing N N 450 
V1F C21 H3   sing N N 451 
V1F C21 H4   sing N N 452 
V1F C24 H5   sing N N 453 
V1F C24 H6   sing N N 454 
V1F C29 H7   sing N N 455 
V1F C28 H8   sing N N 456 
V1F C32 H9   sing N N 457 
V1F C31 H10  sing N N 458 
V1F C27 H11  sing N N 459 
V1F N25 H12  sing N N 460 
V1F C14 H13  sing N N 461 
V1F C14 H14  sing N N 462 
V1F C20 H15  sing N N 463 
V1F C19 H16  sing N N 464 
V1F C18 H17  sing N N 465 
V1F C17 H18  sing N N 466 
V1F C16 H19  sing N N 467 
VAL N   CA   sing N N 468 
VAL N   H    sing N N 469 
VAL N   H2   sing N N 470 
VAL CA  C    sing N N 471 
VAL CA  CB   sing N N 472 
VAL CA  HA   sing N N 473 
VAL C   O    doub N N 474 
VAL C   OXT  sing N N 475 
VAL CB  CG1  sing N N 476 
VAL CB  CG2  sing N N 477 
VAL CB  HB   sing N N 478 
VAL CG1 HG11 sing N N 479 
VAL CG1 HG12 sing N N 480 
VAL CG1 HG13 sing N N 481 
VAL CG2 HG21 sing N N 482 
VAL CG2 HG22 sing N N 483 
VAL CG2 HG23 sing N N 484 
VAL OXT HXT  sing N N 485 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                      ZN  
3 '3-(benzylamino)-2,5,6-trifluoro-4-[(2-phenylethyl)sulfonyl]benzenesulfonamide' V1F 
4 BICINE                                                                          BCN 
5 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                          MES 
6 'DIMETHYL SULFOXIDE'                                                            DMS 
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          ? 
# 
