data_3M5E
# 
_entry.id   3M5E 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.380 
_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   3M5E         pdb_00003m5e 10.2210/pdb3m5e/pdb 
RCSB  RCSB058129   ?            ?                   
WWPDB D_1000058129 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3M2N 'The same protein with other ligand' unspecified 
PDB 3M3X 'The same protein with other ligand' unspecified 
PDB 3M40 'The same protein with other ligand' unspecified 
PDB 3MHI 'The same protein with other ligand' unspecified 
PDB 3MHL 'The same protein with other ligand' unspecified 
PDB 3MHM 'The same protein with other ligand' unspecified 
PDB 3MHO 'The same protein with other ligand' unspecified 
# 
_pdbx_database_status.entry_id                        3M5E 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2010-03-12 
_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.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'  1 
'Manakova, E.'  2 
'Golovenko, D.' 3 
# 
_citation.id                        primary 
_citation.title                     
'4-[N-(Substituted 4-pyrimidinyl)amino]benzenesulfonamides as inhibitors of carbonic anhydrase isozymes I, II, VII, and XIII' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            18 
_citation.page_first                7413 
_citation.page_last                 7421 
_citation.year                      2010 
_citation.journal_id_ASTM           BMECEP 
_citation.country                   UK 
_citation.journal_id_ISSN           0968-0896 
_citation.journal_id_CSD            1200 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20889345 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2010.09.011 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sudzius, J.'       1  ? 
primary 'Baranauskiene, L.' 2  ? 
primary 'Golovenko, D.'     3  ? 
primary 'Matuliene, J.'     4  ? 
primary 'Michailoviene, V.' 5  ? 
primary 'Torresan, J.'      6  ? 
primary 'Jachno, J.'        7  ? 
primary 'Sukackaite, R.'    8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Tumkevicius, S.'   11 ? 
primary 'Matulis, D.'       12 ? 
# 
_cell.entry_id           3M5E 
_cell.length_a           42.423 
_cell.length_b           41.486 
_cell.length_c           72.434 
_cell.angle_alpha        90.00 
_cell.angle_beta         104.49 
_cell.angle_gamma        90.00 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
_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                         3M5E 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                                    29289.062 1   4.2.1.1 
? ? ? 
2 non-polymer syn 'ZINC ION'                                                                                65.409    1   ?       
? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                      78.133    1   ?       
? ? ? 
4 non-polymer syn '4-({[6-chloro-5-formyl-2-(methylsulfanyl)pyrimidin-4-yl]amino}methyl)benzenesulfonamide' 372.850   1   ?       
? ? ? 
5 water       nat water                                                                                     18.015    330 ?       
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonic anhydrase II, CA-II, Carbonate dehydratase II, Carbonic anhydrase C, CAC' 
# 
_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                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3M5E 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                                   ? 'C3 H7 N O2' 
89.093  
ARG 'L-peptide linking' y ARGININE                                                                                  ? 
'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                                ? 
'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                                           ? 'C4 H7 N O4' 
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                                  ? 
'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                                      ? 'C2 H6 O S' 
78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                                                 ? 
'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                           ? 'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                                                   ? 'C2 H5 N O2' 
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                 ? 
'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                                                     ? 'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                ? 
'C6 H13 N O2'         131.173 
JDR non-polymer         . '4-({[6-chloro-5-formyl-2-(methylsulfanyl)pyrimidin-4-yl]amino}methyl)benzenesulfonamide' 
'4-{[N-(6-chloro-5-formyl-2-methylthiopyrimidin-4-yl)amino]methyl}benzenesulfonamide' 'C13 H13 Cl N4 O3 S2' 372.850 
LEU 'L-peptide linking' y LEUCINE                                                                                   ? 
'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                                    ? 
'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                                ? 
'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                             ? 
'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                                                   ? 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                                    ? 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                                                 ? 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                ? 
'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                  ? 
'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                                                                    ? 
'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                                                                ? 'Zn 2' 
65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3M5E 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   41.2 
_exptl_crystal.density_Matthews      2.1 
_exptl_crystal.pdbx_mosaicity        ? 
_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              8 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.pdbx_details    
'0.1M Na-bicine pH 9.0, 2M Na-malonate pH 7.55, VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2009-12-20 
_diffrn_detector.details                'Bent, vertically focussing mirror' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8120 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.pdbx_wavelength_list        0.8120 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
# 
_reflns.entry_id                     3M5E 
_reflns.d_resolution_high            1.7 
_reflns.d_resolution_low             41.487 
_reflns.number_all                   27116 
_reflns.number_obs                   27116 
_reflns.pdbx_Rmerge_I_obs            0.054 
_reflns.pdbx_netI_over_sigmaI        32.800 
_reflns.pdbx_Rsym_value              0.054 
_reflns.pdbx_redundancy              11.600 
_reflns.percent_possible_obs         100.000 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        13.3 
_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_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.70 
_reflns_shell.d_res_low              1.79 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    30571 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.117 
_reflns_shell.meanI_over_sigI_obs    13 
_reflns_shell.pdbx_Rsym_value        0.117 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_redundancy        7.80 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      3922 
_reflns_shell.percent_possible_all   100.00 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3M5E 
_refine.ls_d_res_high                            1.700 
_refine.ls_d_res_low                             40.100 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.950 
_refine.ls_number_reflns_obs                     27090 
_refine.ls_number_reflns_all                     0 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_obs                          0.16752 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.16366 
_refine.ls_R_factor_R_free                       0.20202 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  2727 
_refine.ls_number_reflns_R_work                  24363 
_refine.ls_R_factor_R_free_error                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_Fo_to_Fc               0.952 
_refine.correlation_coeff_Fo_to_Fc_free          0.937 
_refine.B_iso_mean                               12.678 
_refine.aniso_B[1][1]                            0.04 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[3][3]                            -0.08 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.09 
_refine.aniso_B[2][3]                            0.00 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       0.120 
_refine.pdbx_overall_ESU_R_Free                  0.114 
_refine.overall_SU_ML                            0.062 
_refine.overall_SU_B                             1.822 
_refine.solvent_model_details                    'BABINET MODEL WITH 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.pdbx_ls_sigma_I                          0 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3HLJ' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_phase_error                 ? 
_refine.B_iso_max                                58.63 
_refine.B_iso_min                                2.22 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2059 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.number_atoms_solvent             330 
_refine_hist.number_atoms_total               2417 
_refine_hist.d_res_high                       1.700 
_refine_hist.d_res_low                        40.100 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.011  0.021  ? 2227 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.304  1.959  ? 3038 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.156  5.000  ? 275  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.981 24.904 ? 104  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.803 15.000 ? 366  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       21.165 15.000 ? 7    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.092  0.200  ? 313  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.005  0.020  ? 1747 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.194  0.200  ? 1023 'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.309  0.200  ? 1483 'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.132  0.200  ? 260  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          0.049  0.200  ? 2    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.176  0.200  ? 70   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.147  0.200  ? 45   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.773  1.500  ? 1387 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.255  2.000  ? 2176 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.971  3.000  ? 994  'X-RAY DIFFRACTION' ? 
r_scangle_it                 2.923  4.500  ? 862  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.700 
_refine_ls_shell.d_res_low                        1.744 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               100.000 
_refine_ls_shell.number_reflns_R_work             1763 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.211 
_refine_ls_shell.R_factor_R_free                  0.279 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             202 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1965 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3M5E 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 4-{[N-(6-chloro-5-formyl-2-methylthiopyrimidin-4-yl)amino]methyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3M5E 
_struct_keywords.text            'DRUG DESIGN, CARBONIC ANHYDRASE, SULFONAMIDE, METAL-BINDING, LYASE-LYASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 0.35 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 5.69 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N ARG A 58  ? N ARG A 58  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  262 ? 4  'BINDING SITE FOR RESIDUE ZN A 262'  
AC2 Software A DMS 263 ? 5  'BINDING SITE FOR RESIDUE DMS A 263' 
AC3 Software A JDR 264 ? 12 'BINDING SITE FOR RESIDUE JDR A 264' 
# 
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  JDR D .   ? JDR A 264 . ? 1_555 ? 
5  AC2 5  ASP A 242 ? ASP A 243 . ? 1_555 ? 
6  AC2 5  TRP A 244 ? TRP A 245 . ? 1_555 ? 
7  AC2 5  HOH E .   ? HOH A 317 . ? 1_555 ? 
8  AC2 5  HOH E .   ? HOH A 541 . ? 1_555 ? 
9  AC2 5  HOH E .   ? HOH A 587 . ? 1_555 ? 
10 AC3 12 GLN A 92  ? GLN A 92  . ? 1_555 ? 
11 AC3 12 HIS A 94  ? HIS A 94  . ? 1_555 ? 
12 AC3 12 HIS A 96  ? HIS A 96  . ? 1_555 ? 
13 AC3 12 HIS A 119 ? HIS A 119 . ? 1_555 ? 
14 AC3 12 PHE A 130 ? PHE A 131 . ? 1_555 ? 
15 AC3 12 LEU A 197 ? LEU A 198 . ? 1_555 ? 
16 AC3 12 THR A 198 ? THR A 199 . ? 1_555 ? 
17 AC3 12 THR A 199 ? THR A 200 . ? 1_555 ? 
18 AC3 12 TRP A 208 ? TRP A 209 . ? 1_555 ? 
19 AC3 12 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
20 AC3 12 HOH E .   ? HOH A 310 . ? 1_555 ? 
21 AC3 12 HOH E .   ? HOH A 370 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3M5E 
_atom_sites.fract_transf_matrix[1][1]   0.023572 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006092 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024105 
_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]   0.014259 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . HIS A 1 3   ? 13.681  -0.148  6.586   1.00 22.31 ? 3   HIS A N    1 
ATOM   2    C  CA   . HIS A 1 3   ? 13.360  -1.172  7.630   1.00 22.38 ? 3   HIS A CA   1 
ATOM   3    C  C    . HIS A 1 3   ? 12.292  -0.650  8.614   1.00 21.99 ? 3   HIS A C    1 
ATOM   4    O  O    . HIS A 1 3   ? 12.548  -0.447  9.810   1.00 22.14 ? 3   HIS A O    1 
ATOM   5    C  CB   . HIS A 1 3   ? 14.632  -1.617  8.361   1.00 23.20 ? 3   HIS A CB   1 
ATOM   6    C  CG   . HIS A 1 3   ? 14.506  -2.949  9.035   1.00 24.60 ? 3   HIS A CG   1 
ATOM   7    N  ND1  . HIS A 1 3   ? 14.180  -3.083  10.369  1.00 26.68 ? 3   HIS A ND1  1 
ATOM   8    C  CD2  . HIS A 1 3   ? 14.670  -4.207  8.559   1.00 24.98 ? 3   HIS A CD2  1 
ATOM   9    C  CE1  . HIS A 1 3   ? 14.153  -4.366  10.688  1.00 26.04 ? 3   HIS A CE1  1 
ATOM   10   N  NE2  . HIS A 1 3   ? 14.444  -5.069  9.607   1.00 28.10 ? 3   HIS A NE2  1 
ATOM   11   N  N    . HIS A 1 4   ? 11.095  -0.454  8.066   1.00 19.93 ? 4   HIS A N    1 
ATOM   12   C  CA   . HIS A 1 4   ? 9.927   0.133   8.722   1.00 18.14 ? 4   HIS A CA   1 
ATOM   13   C  C    . HIS A 1 4   ? 9.209   -0.952  9.540   1.00 15.96 ? 4   HIS A C    1 
ATOM   14   O  O    . HIS A 1 4   ? 9.372   -2.138  9.277   1.00 14.91 ? 4   HIS A O    1 
ATOM   15   C  CB   . HIS A 1 4   ? 9.033   0.670   7.588   1.00 19.04 ? 4   HIS A CB   1 
ATOM   16   C  CG   . HIS A 1 4   ? 7.677   1.152   8.005   1.00 21.61 ? 4   HIS A CG   1 
ATOM   17   N  ND1  . HIS A 1 4   ? 7.426   2.457   8.376   1.00 24.45 ? 4   HIS A ND1  1 
ATOM   18   C  CD2  . HIS A 1 4   ? 6.476   0.521   8.023   1.00 23.01 ? 4   HIS A CD2  1 
ATOM   19   C  CE1  . HIS A 1 4   ? 6.138   2.594   8.649   1.00 24.13 ? 4   HIS A CE1  1 
ATOM   20   N  NE2  . HIS A 1 4   ? 5.541   1.431   8.445   1.00 22.97 ? 4   HIS A NE2  1 
ATOM   21   N  N    . TRP A 1 5   ? 8.407   -0.545  10.517  1.00 13.88 ? 5   TRP A N    1 
ATOM   22   C  CA   . TRP A 1 5   ? 7.699   -1.515  11.357  1.00 12.05 ? 5   TRP A CA   1 
ATOM   23   C  C    . TRP A 1 5   ? 6.680   -2.322  10.561  1.00 11.44 ? 5   TRP A C    1 
ATOM   24   O  O    . TRP A 1 5   ? 6.140   -1.846  9.555   1.00 11.08 ? 5   TRP A O    1 
ATOM   25   C  CB   . TRP A 1 5   ? 7.011   -0.828  12.539  1.00 11.22 ? 5   TRP A CB   1 
ATOM   26   C  CG   . TRP A 1 5   ? 5.826   0.019   12.172  1.00 11.51 ? 5   TRP A CG   1 
ATOM   27   C  CD1  . TRP A 1 5   ? 5.820   1.357   11.882  1.00 10.98 ? 5   TRP A CD1  1 
ATOM   28   C  CD2  . TRP A 1 5   ? 4.474   -0.417  12.077  1.00 9.65  ? 5   TRP A CD2  1 
ATOM   29   N  NE1  . TRP A 1 5   ? 4.548   1.777   11.605  1.00 11.07 ? 5   TRP A NE1  1 
ATOM   30   C  CE2  . TRP A 1 5   ? 3.698   0.706   11.711  1.00 10.37 ? 5   TRP A CE2  1 
ATOM   31   C  CE3  . TRP A 1 5   ? 3.840   -1.654  12.262  1.00 10.13 ? 5   TRP A CE3  1 
ATOM   32   C  CZ2  . TRP A 1 5   ? 2.315   0.633   11.534  1.00 11.16 ? 5   TRP A CZ2  1 
ATOM   33   C  CZ3  . TRP A 1 5   ? 2.472   -1.729  12.072  1.00 9.80  ? 5   TRP A CZ3  1 
ATOM   34   C  CH2  . TRP A 1 5   ? 1.723   -0.588  11.722  1.00 10.81 ? 5   TRP A CH2  1 
ATOM   35   N  N    . GLY A 1 6   ? 6.407   -3.537  11.030  1.00 10.13 ? 6   GLY A N    1 
ATOM   36   C  CA   . GLY A 1 6   ? 5.415   -4.386  10.380  1.00 10.34 ? 6   GLY A CA   1 
ATOM   37   C  C    . GLY A 1 6   ? 4.987   -5.537  11.267  1.00 10.21 ? 6   GLY A C    1 
ATOM   38   O  O    . GLY A 1 6   ? 4.984   -5.418  12.499  1.00 10.22 ? 6   GLY A O    1 
ATOM   39   N  N    . TYR A 1 7   ? 4.610   -6.642  10.626  1.00 11.43 ? 7   TYR A N    1 
ATOM   40   C  CA   . TYR A 1 7   ? 4.270   -7.882  11.310  1.00 12.76 ? 7   TYR A CA   1 
ATOM   41   C  C    . TYR A 1 7   ? 5.018   -9.043  10.661  1.00 14.76 ? 7   TYR A C    1 
ATOM   42   O  O    . TYR A 1 7   ? 4.558   -10.204 10.689  1.00 15.91 ? 7   TYR A O    1 
ATOM   43   C  CB   . TYR A 1 7   ? 2.772   -8.151  11.212  1.00 11.53 ? 7   TYR A CB   1 
ATOM   44   C  CG   . TYR A 1 7   ? 1.883   -7.071  11.788  1.00 8.71  ? 7   TYR A CG   1 
ATOM   45   C  CD1  . TYR A 1 7   ? 1.490   -7.099  13.132  1.00 6.46  ? 7   TYR A CD1  1 
ATOM   46   C  CD2  . TYR A 1 7   ? 1.393   -6.055  10.976  1.00 6.65  ? 7   TYR A CD2  1 
ATOM   47   C  CE1  . TYR A 1 7   ? 0.665   -6.099  13.649  1.00 6.24  ? 7   TYR A CE1  1 
ATOM   48   C  CE2  . TYR A 1 7   ? 0.555   -5.064  11.480  1.00 6.67  ? 7   TYR A CE2  1 
ATOM   49   C  CZ   . TYR A 1 7   ? 0.190   -5.100  12.815  1.00 7.06  ? 7   TYR A CZ   1 
ATOM   50   O  OH   . TYR A 1 7   ? -0.653  -4.113  13.283  1.00 7.69  ? 7   TYR A OH   1 
ATOM   51   N  N    . GLY A 1 8   ? 6.158   -8.739  10.054  1.00 15.38 ? 8   GLY A N    1 
ATOM   52   C  CA   . GLY A 1 8   ? 6.919   -9.769  9.350   1.00 17.22 ? 8   GLY A CA   1 
ATOM   53   C  C    . GLY A 1 8   ? 7.835   -10.525 10.289  1.00 18.42 ? 8   GLY A C    1 
ATOM   54   O  O    . GLY A 1 8   ? 7.771   -10.371 11.510  1.00 18.70 ? 8   GLY A O    1 
ATOM   55   N  N    . LYS A 1 9   ? 8.730   -11.325 9.710   1.00 18.85 ? 9   LYS A N    1 
ATOM   56   C  CA   . LYS A 1 9   ? 9.637   -12.118 10.528  1.00 19.53 ? 9   LYS A CA   1 
ATOM   57   C  C    . LYS A 1 9   ? 10.675  -11.314 11.324  1.00 18.80 ? 9   LYS A C    1 
ATOM   58   O  O    . LYS A 1 9   ? 11.211  -11.843 12.299  1.00 19.66 ? 9   LYS A O    1 
ATOM   59   C  CB   . LYS A 1 9   ? 10.334  -13.178 9.674   1.00 20.14 ? 9   LYS A CB   1 
ATOM   60   C  CG   . LYS A 1 9   ? 9.480   -14.407 9.394   1.00 22.06 ? 9   LYS A CG   1 
ATOM   61   C  CD   . LYS A 1 9   ? 10.357  -15.536 8.907   1.00 24.89 ? 9   LYS A CD   1 
ATOM   62   C  CE   . LYS A 1 9   ? 10.467  -15.566 7.390   1.00 26.33 ? 9   LYS A CE   1 
ATOM   63   N  NZ   . LYS A 1 9   ? 9.614   -16.643 6.819   1.00 26.31 ? 9   LYS A NZ   1 
ATOM   64   N  N    . HIS A 1 10  ? 10.940  -10.059 10.922  1.00 17.37 ? 10  HIS A N    1 
ATOM   65   C  CA   . HIS A 1 10  ? 12.076  -9.263  11.443  1.00 15.80 ? 10  HIS A CA   1 
ATOM   66   C  C    . HIS A 1 10  ? 11.743  -7.828  11.928  1.00 14.32 ? 10  HIS A C    1 
ATOM   67   O  O    . HIS A 1 10  ? 12.612  -7.095  12.422  1.00 13.78 ? 10  HIS A O    1 
ATOM   68   C  CB   . HIS A 1 10  ? 13.179  -9.178  10.365  1.00 15.95 ? 10  HIS A CB   1 
ATOM   69   C  CG   . HIS A 1 10  ? 13.662  -10.512 9.882   1.00 17.12 ? 10  HIS A CG   1 
ATOM   70   N  ND1  . HIS A 1 10  ? 14.652  -11.223 10.528  1.00 18.48 ? 10  HIS A ND1  1 
ATOM   71   C  CD2  . HIS A 1 10  ? 13.304  -11.257 8.806   1.00 18.02 ? 10  HIS A CD2  1 
ATOM   72   C  CE1  . HIS A 1 10  ? 14.867  -12.357 9.886   1.00 16.98 ? 10  HIS A CE1  1 
ATOM   73   N  NE2  . HIS A 1 10  ? 14.064  -12.402 8.836   1.00 18.33 ? 10  HIS A NE2  1 
ATOM   74   N  N    . ASN A 1 11  ? 10.482  -7.418  11.782  1.00 13.24 ? 11  ASN A N    1 
ATOM   75   C  CA   . ASN A 1 11  ? 10.073  -6.062  12.128  1.00 12.23 ? 11  ASN A CA   1 
ATOM   76   C  C    . ASN A 1 11  ? 8.760   -6.032  12.930  1.00 11.80 ? 11  ASN A C    1 
ATOM   77   O  O    . ASN A 1 11  ? 8.096   -4.989  13.015  1.00 11.73 ? 11  ASN A O    1 
ATOM   78   C  CB   . ASN A 1 11  ? 9.912   -5.222  10.846  1.00 11.97 ? 11  ASN A CB   1 
ATOM   79   C  CG   . ASN A 1 11  ? 8.828   -5.763  9.924   1.00 12.72 ? 11  ASN A CG   1 
ATOM   80   O  OD1  . ASN A 1 11  ? 8.248   -6.823  10.179  1.00 13.20 ? 11  ASN A OD1  1 
ATOM   81   N  ND2  . ASN A 1 11  ? 8.584   -5.059  8.816   1.00 13.94 ? 11  ASN A ND2  1 
ATOM   82   N  N    . GLY A 1 12  ? 8.428   -7.174  13.530  1.00 11.06 ? 12  GLY A N    1 
ATOM   83   C  CA   . GLY A 1 12  ? 7.130   -7.362  14.190  1.00 11.10 ? 12  GLY A CA   1 
ATOM   84   C  C    . GLY A 1 12  ? 7.046   -6.744  15.570  1.00 10.33 ? 12  GLY A C    1 
ATOM   85   O  O    . GLY A 1 12  ? 7.952   -6.034  16.004  1.00 10.62 ? 12  GLY A O    1 
ATOM   86   N  N    . PRO A 1 13  ? 5.937   -7.009  16.286  1.00 9.60  ? 13  PRO A N    1 
ATOM   87   C  CA   . PRO A 1 13  ? 5.680   -6.358  17.569  1.00 9.17  ? 13  PRO A CA   1 
ATOM   88   C  C    . PRO A 1 13  ? 6.820   -6.359  18.593  1.00 8.81  ? 13  PRO A C    1 
ATOM   89   O  O    . PRO A 1 13  ? 6.947   -5.401  19.355  1.00 8.75  ? 13  PRO A O    1 
ATOM   90   C  CB   . PRO A 1 13  ? 4.466   -7.128  18.102  1.00 8.76  ? 13  PRO A CB   1 
ATOM   91   C  CG   . PRO A 1 13  ? 3.716   -7.480  16.871  1.00 8.58  ? 13  PRO A CG   1 
ATOM   92   C  CD   . PRO A 1 13  ? 4.820   -7.888  15.891  1.00 9.89  ? 13  PRO A CD   1 
ATOM   93   N  N    A GLU A 1 14  ? 7.622   -7.425  18.592  0.50 8.42  ? 14  GLU A N    1 
ATOM   94   N  N    B GLU A 1 14  ? 7.629   -7.417  18.638  0.50 8.86  ? 14  GLU A N    1 
ATOM   95   C  CA   A GLU A 1 14  ? 8.722   -7.583  19.542  0.50 8.73  ? 14  GLU A CA   1 
ATOM   96   C  CA   B GLU A 1 14  ? 8.701   -7.484  19.641  0.50 9.45  ? 14  GLU A CA   1 
ATOM   97   C  C    A GLU A 1 14  ? 9.854   -6.580  19.267  0.50 8.63  ? 14  GLU A C    1 
ATOM   98   C  C    B GLU A 1 14  ? 9.845   -6.519  19.299  0.50 9.08  ? 14  GLU A C    1 
ATOM   99   O  O    A GLU A 1 14  ? 10.728  -6.354  20.113  0.50 9.09  ? 14  GLU A O    1 
ATOM   100  O  O    B GLU A 1 14  ? 10.732  -6.268  20.126  0.50 9.41  ? 14  GLU A O    1 
ATOM   101  C  CB   A GLU A 1 14  ? 9.232   -9.034  19.518  0.50 8.72  ? 14  GLU A CB   1 
ATOM   102  C  CB   B GLU A 1 14  ? 9.226   -8.915  19.803  0.50 10.06 ? 14  GLU A CB   1 
ATOM   103  C  CG   A GLU A 1 14  ? 9.995   -9.459  18.278  0.50 8.18  ? 14  GLU A CG   1 
ATOM   104  C  CG   B GLU A 1 14  ? 8.171   -9.976  20.200  0.50 10.99 ? 14  GLU A CG   1 
ATOM   105  C  CD   A GLU A 1 14  ? 9.140   -10.071 17.157  0.50 9.29  ? 14  GLU A CD   1 
ATOM   106  C  CD   B GLU A 1 14  ? 7.333   -9.621  21.434  0.50 14.79 ? 14  GLU A CD   1 
ATOM   107  O  OE1  A GLU A 1 14  ? 7.927   -9.749  17.037  0.50 7.60  ? 14  GLU A OE1  1 
ATOM   108  O  OE1  B GLU A 1 14  ? 7.920   -9.339  22.502  0.50 16.32 ? 14  GLU A OE1  1 
ATOM   109  O  OE2  A GLU A 1 14  ? 9.729   -10.848 16.351  0.50 7.30  ? 14  GLU A OE2  1 
ATOM   110  O  OE2  B GLU A 1 14  ? 6.074   -9.649  21.340  0.50 14.91 ? 14  GLU A OE2  1 
ATOM   111  N  N    . HIS A 1 15  ? 9.810   -5.967  18.087  1.00 8.75  ? 15  HIS A N    1 
ATOM   112  C  CA   . HIS A 1 15  ? 10.838  -5.014  17.642  1.00 8.82  ? 15  HIS A CA   1 
ATOM   113  C  C    . HIS A 1 15  ? 10.424  -3.554  17.778  1.00 9.11  ? 15  HIS A C    1 
ATOM   114  O  O    . HIS A 1 15  ? 11.275  -2.660  17.719  1.00 8.83  ? 15  HIS A O    1 
ATOM   115  C  CB   . HIS A 1 15  ? 11.226  -5.274  16.174  1.00 9.06  ? 15  HIS A CB   1 
ATOM   116  C  CG   . HIS A 1 15  ? 11.868  -6.609  15.943  1.00 10.01 ? 15  HIS A CG   1 
ATOM   117  N  ND1  . HIS A 1 15  ? 13.212  -6.832  16.158  1.00 13.29 ? 15  HIS A ND1  1 
ATOM   118  C  CD2  . HIS A 1 15  ? 11.360  -7.783  15.497  1.00 12.26 ? 15  HIS A CD2  1 
ATOM   119  C  CE1  . HIS A 1 15  ? 13.499  -8.091  15.872  1.00 12.74 ? 15  HIS A CE1  1 
ATOM   120  N  NE2  . HIS A 1 15  ? 12.395  -8.691  15.470  1.00 13.66 ? 15  HIS A NE2  1 
ATOM   121  N  N    . TRP A 1 16  ? 9.125   -3.304  17.967  1.00 8.19  ? 16  TRP A N    1 
ATOM   122  C  CA   . TRP A 1 16  ? 8.622   -1.936  17.888  1.00 7.79  ? 16  TRP A CA   1 
ATOM   123  C  C    . TRP A 1 16  ? 9.215   -0.958  18.906  1.00 7.53  ? 16  TRP A C    1 
ATOM   124  O  O    . TRP A 1 16  ? 9.324   0.235   18.629  1.00 7.87  ? 16  TRP A O    1 
ATOM   125  C  CB   . TRP A 1 16  ? 7.091   -1.929  17.996  1.00 6.58  ? 16  TRP A CB   1 
ATOM   126  C  CG   . TRP A 1 16  ? 6.382   -2.630  16.860  1.00 6.24  ? 16  TRP A CG   1 
ATOM   127  C  CD1  . TRP A 1 16  ? 6.929   -3.079  15.679  1.00 5.84  ? 16  TRP A CD1  1 
ATOM   128  C  CD2  . TRP A 1 16  ? 4.976   -2.910  16.777  1.00 5.38  ? 16  TRP A CD2  1 
ATOM   129  N  NE1  . TRP A 1 16  ? 5.956   -3.654  14.896  1.00 7.12  ? 16  TRP A NE1  1 
ATOM   130  C  CE2  . TRP A 1 16  ? 4.747   -3.550  15.535  1.00 6.02  ? 16  TRP A CE2  1 
ATOM   131  C  CE3  . TRP A 1 16  ? 3.892   -2.694  17.645  1.00 7.09  ? 16  TRP A CE3  1 
ATOM   132  C  CZ2  . TRP A 1 16  ? 3.471   -3.981  15.133  1.00 7.93  ? 16  TRP A CZ2  1 
ATOM   133  C  CZ3  . TRP A 1 16  ? 2.642   -3.112  17.258  1.00 5.77  ? 16  TRP A CZ3  1 
ATOM   134  C  CH2  . TRP A 1 16  ? 2.428   -3.739  16.005  1.00 6.09  ? 16  TRP A CH2  1 
ATOM   135  N  N    . HIS A 1 17  ? 9.601   -1.470  20.066  1.00 8.36  ? 17  HIS A N    1 
ATOM   136  C  CA   . HIS A 1 17  ? 10.082  -0.625  21.154  1.00 9.10  ? 17  HIS A CA   1 
ATOM   137  C  C    . HIS A 1 17  ? 11.331  0.175   20.774  1.00 9.47  ? 17  HIS A C    1 
ATOM   138  O  O    . HIS A 1 17  ? 11.572  1.232   21.340  1.00 9.43  ? 17  HIS A O    1 
ATOM   139  C  CB   . HIS A 1 17  ? 10.335  -1.447  22.408  1.00 8.86  ? 17  HIS A CB   1 
ATOM   140  C  CG   . HIS A 1 17  ? 11.515  -2.360  22.290  1.00 9.76  ? 17  HIS A CG   1 
ATOM   141  N  ND1  . HIS A 1 17  ? 12.753  -2.033  22.796  1.00 12.01 ? 17  HIS A ND1  1 
ATOM   142  C  CD2  . HIS A 1 17  ? 11.664  -3.551  21.666  1.00 11.04 ? 17  HIS A CD2  1 
ATOM   143  C  CE1  . HIS A 1 17  ? 13.609  -2.999  22.519  1.00 10.39 ? 17  HIS A CE1  1 
ATOM   144  N  NE2  . HIS A 1 17  ? 12.973  -3.937  21.841  1.00 12.92 ? 17  HIS A NE2  1 
ATOM   145  N  N    . LYS A 1 18  ? 12.098  -0.332  19.809  1.00 10.88 ? 18  LYS A N    1 
ATOM   146  C  CA   . LYS A 1 18  ? 13.334  0.335   19.371  1.00 11.92 ? 18  LYS A CA   1 
ATOM   147  C  C    . LYS A 1 18  ? 13.072  1.689   18.723  1.00 12.76 ? 18  LYS A C    1 
ATOM   148  O  O    . LYS A 1 18  ? 13.746  2.665   19.048  1.00 14.20 ? 18  LYS A O    1 
ATOM   149  C  CB   . LYS A 1 18  ? 14.135  -0.576  18.445  1.00 11.75 ? 18  LYS A CB   1 
ATOM   150  C  CG   . LYS A 1 18  ? 14.783  -1.746  19.172  1.00 10.83 ? 18  LYS A CG   1 
ATOM   151  C  CD   . LYS A 1 18  ? 15.479  -2.708  18.207  1.00 11.38 ? 18  LYS A CD   1 
ATOM   152  C  CE   . LYS A 1 18  ? 14.523  -3.736  17.601  1.00 11.06 ? 18  LYS A CE   1 
ATOM   153  N  NZ   . LYS A 1 18  ? 15.230  -4.531  16.532  1.00 11.17 ? 18  LYS A NZ   1 
ATOM   154  N  N    . ASP A 1 19  ? 12.057  1.768   17.856  1.00 13.03 ? 19  ASP A N    1 
ATOM   155  C  CA   . ASP A 1 19  ? 11.641  3.072   17.320  1.00 13.19 ? 19  ASP A CA   1 
ATOM   156  C  C    . ASP A 1 19  ? 10.596  3.795   18.174  1.00 12.43 ? 19  ASP A C    1 
ATOM   157  O  O    . ASP A 1 19  ? 10.485  5.021   18.101  1.00 12.18 ? 19  ASP A O    1 
ATOM   158  C  CB   . ASP A 1 19  ? 11.120  2.940   15.887  1.00 14.80 ? 19  ASP A CB   1 
ATOM   159  C  CG   . ASP A 1 19  ? 12.234  2.944   14.854  1.00 18.37 ? 19  ASP A CG   1 
ATOM   160  O  OD1  . ASP A 1 19  ? 13.345  3.433   15.152  1.00 23.27 ? 19  ASP A OD1  1 
ATOM   161  O  OD2  . ASP A 1 19  ? 11.990  2.448   13.745  1.00 23.90 ? 19  ASP A OD2  1 
ATOM   162  N  N    . PHE A 1 20  ? 9.826   3.032   18.953  1.00 10.98 ? 20  PHE A N    1 
ATOM   163  C  CA   . PHE A 1 20  ? 8.717   3.555   19.750  1.00 10.04 ? 20  PHE A CA   1 
ATOM   164  C  C    . PHE A 1 20  ? 8.795   3.073   21.192  1.00 9.61  ? 20  PHE A C    1 
ATOM   165  O  O    . PHE A 1 20  ? 8.100   2.134   21.570  1.00 8.97  ? 20  PHE A O    1 
ATOM   166  C  CB   . PHE A 1 20  ? 7.376   3.169   19.099  1.00 9.71  ? 20  PHE A CB   1 
ATOM   167  C  CG   . PHE A 1 20  ? 7.273   3.617   17.670  1.00 9.53  ? 20  PHE A CG   1 
ATOM   168  C  CD1  . PHE A 1 20  ? 6.865   4.905   17.356  1.00 11.55 ? 20  PHE A CD1  1 
ATOM   169  C  CD2  . PHE A 1 20  ? 7.628   2.744   16.632  1.00 11.18 ? 20  PHE A CD2  1 
ATOM   170  C  CE1  . PHE A 1 20  ? 6.795   5.309   16.020  1.00 12.41 ? 20  PHE A CE1  1 
ATOM   171  C  CE2  . PHE A 1 20  ? 7.573   3.145   15.307  1.00 12.67 ? 20  PHE A CE2  1 
ATOM   172  C  CZ   . PHE A 1 20  ? 7.158   4.423   14.999  1.00 11.57 ? 20  PHE A CZ   1 
ATOM   173  N  N    . PRO A 1 21  ? 9.674   3.694   21.999  1.00 9.50  ? 21  PRO A N    1 
ATOM   174  C  CA   . PRO A 1 21  ? 9.914   3.250   23.376  1.00 8.85  ? 21  PRO A CA   1 
ATOM   175  C  C    . PRO A 1 21  ? 8.651   3.121   24.239  1.00 8.50  ? 21  PRO A C    1 
ATOM   176  O  O    . PRO A 1 21  ? 8.649   2.331   25.177  1.00 8.84  ? 21  PRO A O    1 
ATOM   177  C  CB   . PRO A 1 21  ? 10.853  4.324   23.952  1.00 9.92  ? 21  PRO A CB   1 
ATOM   178  C  CG   . PRO A 1 21  ? 10.924  5.413   22.917  1.00 10.62 ? 21  PRO A CG   1 
ATOM   179  C  CD   . PRO A 1 21  ? 10.565  4.804   21.609  1.00 9.81  ? 21  PRO A CD   1 
ATOM   180  N  N    A ILE A 1 22  ? 7.603   3.889   23.921  0.50 7.62  ? 22  ILE A N    1 
ATOM   181  N  N    B ILE A 1 22  ? 7.609   3.889   23.911  0.50 7.53  ? 22  ILE A N    1 
ATOM   182  C  CA   A ILE A 1 22  ? 6.337   3.820   24.668  0.50 7.41  ? 22  ILE A CA   1 
ATOM   183  C  CA   B ILE A 1 22  ? 6.333   3.833   24.632  0.50 7.20  ? 22  ILE A CA   1 
ATOM   184  C  C    A ILE A 1 22  ? 5.701   2.425   24.545  0.50 7.11  ? 22  ILE A C    1 
ATOM   185  C  C    B ILE A 1 22  ? 5.709   2.430   24.544  0.50 7.01  ? 22  ILE A C    1 
ATOM   186  O  O    A ILE A 1 22  ? 4.748   2.110   25.256  0.50 6.64  ? 22  ILE A O    1 
ATOM   187  O  O    B ILE A 1 22  ? 4.771   2.115   25.276  0.50 6.54  ? 22  ILE A O    1 
ATOM   188  C  CB   A ILE A 1 22  ? 5.338   4.944   24.232  0.50 6.98  ? 22  ILE A CB   1 
ATOM   189  C  CB   B ILE A 1 22  ? 5.346   4.911   24.105  0.50 6.85  ? 22  ILE A CB   1 
ATOM   190  C  CG1  A ILE A 1 22  ? 4.281   5.223   25.315  0.50 6.71  ? 22  ILE A CG1  1 
ATOM   191  C  CG1  B ILE A 1 22  ? 4.258   5.217   25.144  0.50 6.45  ? 22  ILE A CG1  1 
ATOM   192  C  CG2  A ILE A 1 22  ? 4.677   4.602   22.891  0.50 8.24  ? 22  ILE A CG2  1 
ATOM   193  C  CG2  B ILE A 1 22  ? 4.773   4.499   22.731  0.50 7.79  ? 22  ILE A CG2  1 
ATOM   194  C  CD1  A ILE A 1 22  ? 4.827   5.823   26.612  0.50 6.99  ? 22  ILE A CD1  1 
ATOM   195  C  CD1  B ILE A 1 22  ? 3.398   6.407   24.813  0.50 6.68  ? 22  ILE A CD1  1 
ATOM   196  N  N    . ALA A 1 23  ? 6.250   1.588   23.662  1.00 7.02  ? 23  ALA A N    1 
ATOM   197  C  CA   . ALA A 1 23  ? 5.791   0.182   23.525  1.00 7.74  ? 23  ALA A CA   1 
ATOM   198  C  C    . ALA A 1 23  ? 5.866   -0.590  24.841  1.00 8.41  ? 23  ALA A C    1 
ATOM   199  O  O    . ALA A 1 23  ? 5.130   -1.571  25.035  1.00 8.33  ? 23  ALA A O    1 
ATOM   200  C  CB   . ALA A 1 23  ? 6.599   -0.544  22.475  1.00 8.07  ? 23  ALA A CB   1 
ATOM   201  N  N    . LYS A 1 24  ? 6.795   -0.175  25.705  1.00 9.50  ? 24  LYS A N    1 
ATOM   202  C  CA   . LYS A 1 24  ? 7.004   -0.795  27.030  1.00 10.98 ? 24  LYS A CA   1 
ATOM   203  C  C    . LYS A 1 24  ? 6.402   0.083   28.141  1.00 10.94 ? 24  LYS A C    1 
ATOM   204  O  O    . LYS A 1 24  ? 6.819   0.000   29.325  1.00 11.47 ? 24  LYS A O    1 
ATOM   205  C  CB   . LYS A 1 24  ? 8.508   -0.987  27.278  1.00 10.61 ? 24  LYS A CB   1 
ATOM   206  C  CG   . LYS A 1 24  ? 9.165   -2.051  26.431  1.00 12.35 ? 24  LYS A CG   1 
ATOM   207  C  CD   . LYS A 1 24  ? 10.641  -2.214  26.851  1.00 13.02 ? 24  LYS A CD   1 
ATOM   208  C  CE   . LYS A 1 24  ? 11.400  -3.086  25.852  1.00 16.96 ? 24  LYS A CE   1 
ATOM   209  N  NZ   . LYS A 1 24  ? 11.004  -4.509  25.944  1.00 18.72 ? 24  LYS A NZ   1 
ATOM   210  N  N    . GLY A 1 25  ? 5.425   0.913   27.764  1.00 10.26 ? 25  GLY A N    1 
ATOM   211  C  CA   . GLY A 1 25  ? 4.823   1.909   28.655  1.00 10.15 ? 25  GLY A CA   1 
ATOM   212  C  C    . GLY A 1 25  ? 3.834   1.335   29.659  1.00 9.60  ? 25  GLY A C    1 
ATOM   213  O  O    . GLY A 1 25  ? 3.655   0.119   29.744  1.00 10.35 ? 25  GLY A O    1 
ATOM   214  N  N    . GLU A 1 26  ? 3.163   2.225   30.383  1.00 9.84  ? 26  GLU A N    1 
ATOM   215  C  CA   . GLU A 1 26  ? 2.298   1.844   31.510  1.00 9.84  ? 26  GLU A CA   1 
ATOM   216  C  C    . GLU A 1 26  ? 0.832   1.606   31.135  1.00 9.49  ? 26  GLU A C    1 
ATOM   217  O  O    . GLU A 1 26  ? 0.058   1.079   31.952  1.00 9.45  ? 26  GLU A O    1 
ATOM   218  C  CB   . GLU A 1 26  ? 2.342   2.920   32.595  1.00 11.38 ? 26  GLU A CB   1 
ATOM   219  C  CG   . GLU A 1 26  ? 3.707   3.134   33.226  1.00 14.85 ? 26  GLU A CG   1 
ATOM   220  C  CD   . GLU A 1 26  ? 4.242   1.889   33.909  1.00 18.83 ? 26  GLU A CD   1 
ATOM   221  O  OE1  . GLU A 1 26  ? 3.535   1.294   34.748  1.00 22.56 ? 26  GLU A OE1  1 
ATOM   222  O  OE2  . GLU A 1 26  ? 5.382   1.504   33.601  1.00 22.86 ? 26  GLU A OE2  1 
ATOM   223  N  N    . ARG A 1 27  ? 0.440   1.992   29.925  1.00 8.52  ? 27  ARG A N    1 
ATOM   224  C  CA   . ARG A 1 27  ? -0.964  1.787   29.526  1.00 8.68  ? 27  ARG A CA   1 
ATOM   225  C  C    . ARG A 1 27  ? -1.095  1.307   28.072  1.00 7.58  ? 27  ARG A C    1 
ATOM   226  O  O    . ARG A 1 27  ? -1.864  1.863   27.266  1.00 7.16  ? 27  ARG A O    1 
ATOM   227  C  CB   . ARG A 1 27  ? -1.857  3.007   29.855  1.00 9.49  ? 27  ARG A CB   1 
ATOM   228  C  CG   . ARG A 1 27  ? -1.535  4.274   29.114  1.00 10.69 ? 27  ARG A CG   1 
ATOM   229  C  CD   . ARG A 1 27  ? -2.555  5.390   29.400  1.00 11.37 ? 27  ARG A CD   1 
ATOM   230  N  NE   . ARG A 1 27  ? -3.733  5.348   28.513  1.00 11.70 ? 27  ARG A NE   1 
ATOM   231  C  CZ   . ARG A 1 27  ? -4.690  6.269   28.516  1.00 12.17 ? 27  ARG A CZ   1 
ATOM   232  N  NH1  . ARG A 1 27  ? -4.626  7.318   29.347  1.00 11.90 ? 27  ARG A NH1  1 
ATOM   233  N  NH2  . ARG A 1 27  ? -5.709  6.164   27.686  1.00 14.41 ? 27  ARG A NH2  1 
ATOM   234  N  N    . GLN A 1 28  ? -0.370  0.233   27.763  1.00 6.31  ? 28  GLN A N    1 
ATOM   235  C  CA   . GLN A 1 28  ? -0.358  -0.306  26.394  1.00 5.15  ? 28  GLN A CA   1 
ATOM   236  C  C    . GLN A 1 28  ? -1.498  -1.279  26.124  1.00 5.07  ? 28  GLN A C    1 
ATOM   237  O  O    . GLN A 1 28  ? -1.990  -1.955  27.044  1.00 4.79  ? 28  GLN A O    1 
ATOM   238  C  CB   . GLN A 1 28  ? 0.993   -0.992  26.136  1.00 5.68  ? 28  GLN A CB   1 
ATOM   239  C  CG   . GLN A 1 28  ? 2.147   0.026   26.009  1.00 4.56  ? 28  GLN A CG   1 
ATOM   240  C  CD   . GLN A 1 28  ? 2.036   0.865   24.725  1.00 3.70  ? 28  GLN A CD   1 
ATOM   241  O  OE1  . GLN A 1 28  ? 2.226   0.346   23.636  1.00 5.24  ? 28  GLN A OE1  1 
ATOM   242  N  NE2  . GLN A 1 28  ? 1.746   2.162   24.865  1.00 4.38  ? 28  GLN A NE2  1 
ATOM   243  N  N    . SER A 1 29  ? -1.878  -1.353  24.849  1.00 3.98  ? 29  SER A N    1 
ATOM   244  C  CA   . SER A 1 29  ? -2.933  -2.227  24.348  1.00 3.80  ? 29  SER A CA   1 
ATOM   245  C  C    . SER A 1 29  ? -2.400  -3.115  23.217  1.00 4.15  ? 29  SER A C    1 
ATOM   246  O  O    . SER A 1 29  ? -1.453  -2.728  22.520  1.00 4.56  ? 29  SER A O    1 
ATOM   247  C  CB   . SER A 1 29  ? -4.086  -1.384  23.812  1.00 3.47  ? 29  SER A CB   1 
ATOM   248  O  OG   . SER A 1 29  ? -4.737  -0.681  24.880  1.00 3.58  ? 29  SER A OG   1 
ATOM   249  N  N    . PRO A 1 30  ? -3.032  -4.283  22.983  1.00 4.20  ? 30  PRO A N    1 
ATOM   250  C  CA   . PRO A 1 30  ? -4.200  -4.825  23.686  1.00 4.31  ? 30  PRO A CA   1 
ATOM   251  C  C    . PRO A 1 30  ? -3.820  -5.507  24.996  1.00 4.34  ? 30  PRO A C    1 
ATOM   252  O  O    . PRO A 1 30  ? -2.636  -5.506  25.398  1.00 5.07  ? 30  PRO A O    1 
ATOM   253  C  CB   . PRO A 1 30  ? -4.750  -5.837  22.682  1.00 4.00  ? 30  PRO A CB   1 
ATOM   254  C  CG   . PRO A 1 30  ? -3.451  -6.427  22.065  1.00 5.09  ? 30  PRO A CG   1 
ATOM   255  C  CD   . PRO A 1 30  ? -2.554  -5.199  21.925  1.00 4.03  ? 30  PRO A CD   1 
ATOM   256  N  N    . VAL A 1 31  ? -4.824  -6.068  25.664  1.00 4.69  ? 31  VAL A N    1 
ATOM   257  C  CA   . VAL A 1 31  ? -4.636  -6.785  26.925  1.00 4.93  ? 31  VAL A CA   1 
ATOM   258  C  C    . VAL A 1 31  ? -5.547  -7.996  26.944  1.00 5.54  ? 31  VAL A C    1 
ATOM   259  O  O    . VAL A 1 31  ? -6.538  -8.080  26.181  1.00 5.30  ? 31  VAL A O    1 
ATOM   260  C  CB   . VAL A 1 31  ? -4.909  -5.920  28.199  1.00 5.04  ? 31  VAL A CB   1 
ATOM   261  C  CG1  . VAL A 1 31  ? -4.010  -4.684  28.240  1.00 4.94  ? 31  VAL A CG1  1 
ATOM   262  C  CG2  . VAL A 1 31  ? -6.418  -5.527  28.334  1.00 5.86  ? 31  VAL A CG2  1 
ATOM   263  N  N    . ASP A 1 32  ? -5.190  -8.952  27.797  1.00 5.65  ? 32  ASP A N    1 
ATOM   264  C  CA   . ASP A 1 32  ? -6.096  -10.060 28.105  1.00 5.91  ? 32  ASP A CA   1 
ATOM   265  C  C    . ASP A 1 32  ? -7.159  -9.542  29.065  1.00 6.30  ? 32  ASP A C    1 
ATOM   266  O  O    . ASP A 1 32  ? -6.844  -8.873  30.053  1.00 6.79  ? 32  ASP A O    1 
ATOM   267  C  CB   . ASP A 1 32  ? -5.345  -11.233 28.747  1.00 6.69  ? 32  ASP A CB   1 
ATOM   268  C  CG   . ASP A 1 32  ? -6.264  -12.429 29.042  1.00 8.91  ? 32  ASP A CG   1 
ATOM   269  O  OD1  . ASP A 1 32  ? -6.949  -12.895 28.091  1.00 7.01  ? 32  ASP A OD1  1 
ATOM   270  O  OD2  . ASP A 1 32  ? -6.290  -12.905 30.221  1.00 9.00  ? 32  ASP A OD2  1 
ATOM   271  N  N    . ILE A 1 33  ? -8.409  -9.857  28.756  1.00 6.03  ? 33  ILE A N    1 
ATOM   272  C  CA   . ILE A 1 33  ? -9.536  -9.553  29.632  1.00 6.17  ? 33  ILE A CA   1 
ATOM   273  C  C    . ILE A 1 33  ? -9.826  -10.779 30.499  1.00 7.15  ? 33  ILE A C    1 
ATOM   274  O  O    . ILE A 1 33  ? -10.328 -11.792 30.037  1.00 7.88  ? 33  ILE A O    1 
ATOM   275  C  CB   . ILE A 1 33  ? -10.785 -9.104  28.835  1.00 5.69  ? 33  ILE A CB   1 
ATOM   276  C  CG1  . ILE A 1 33  ? -10.474 -7.832  28.037  1.00 6.48  ? 33  ILE A CG1  1 
ATOM   277  C  CG2  . ILE A 1 33  ? -11.973 -8.862  29.799  1.00 5.23  ? 33  ILE A CG2  1 
ATOM   278  C  CD1  . ILE A 1 33  ? -11.456 -7.581  26.827  1.00 6.35  ? 33  ILE A CD1  1 
ATOM   279  N  N    . ASP A 1 34  ? -9.441  -10.692 31.760  1.00 8.62  ? 34  ASP A N    1 
ATOM   280  C  CA   . ASP A 1 34  ? -9.753  -11.763 32.710  1.00 10.13 ? 34  ASP A CA   1 
ATOM   281  C  C    . ASP A 1 34  ? -11.170 -11.527 33.247  1.00 11.28 ? 34  ASP A C    1 
ATOM   282  O  O    . ASP A 1 34  ? -11.389 -10.608 34.054  1.00 12.42 ? 34  ASP A O    1 
ATOM   283  C  CB   . ASP A 1 34  ? -8.730  -11.759 33.848  1.00 10.43 ? 34  ASP A CB   1 
ATOM   284  C  CG   . ASP A 1 34  ? -8.804  -13.017 34.686  1.00 15.57 ? 34  ASP A CG   1 
ATOM   285  O  OD1  . ASP A 1 34  ? -9.586  -13.043 35.657  1.00 18.60 ? 34  ASP A OD1  1 
ATOM   286  O  OD2  . ASP A 1 34  ? -8.114  -14.001 34.331  1.00 19.68 ? 34  ASP A OD2  1 
ATOM   287  N  N    . THR A 1 35  ? -12.122 -12.336 32.791  1.00 11.68 ? 35  THR A N    1 
ATOM   288  C  CA   . THR A 1 35  ? -13.558 -12.075 32.992  1.00 13.09 ? 35  THR A CA   1 
ATOM   289  C  C    . THR A 1 35  ? -13.961 -12.198 34.454  1.00 14.13 ? 35  THR A C    1 
ATOM   290  O  O    . THR A 1 35  ? -14.945 -11.598 34.891  1.00 14.65 ? 35  THR A O    1 
ATOM   291  C  CB   . THR A 1 35  ? -14.436 -13.045 32.191  1.00 13.98 ? 35  THR A CB   1 
ATOM   292  O  OG1  . THR A 1 35  ? -14.235 -14.385 32.656  1.00 13.80 ? 35  THR A OG1  1 
ATOM   293  C  CG2  . THR A 1 35  ? -14.124 -12.963 30.709  1.00 11.64 ? 35  THR A CG2  1 
ATOM   294  N  N    . HIS A 1 36  ? -13.204 -12.991 35.208  1.00 14.93 ? 36  HIS A N    1 
ATOM   295  C  CA   . HIS A 1 36  ? -13.518 -13.165 36.622  1.00 16.53 ? 36  HIS A CA   1 
ATOM   296  C  C    . HIS A 1 36  ? -13.028 -12.012 37.490  1.00 17.43 ? 36  HIS A C    1 
ATOM   297  O  O    . HIS A 1 36  ? -13.600 -11.753 38.569  1.00 19.21 ? 36  HIS A O    1 
ATOM   298  C  CB   . HIS A 1 36  ? -13.039 -14.534 37.107  1.00 15.92 ? 36  HIS A CB   1 
ATOM   299  C  CG   . HIS A 1 36  ? -13.836 -15.663 36.534  1.00 18.08 ? 36  HIS A CG   1 
ATOM   300  N  ND1  . HIS A 1 36  ? -13.337 -16.514 35.572  1.00 19.44 ? 36  HIS A ND1  1 
ATOM   301  C  CD2  . HIS A 1 36  ? -15.121 -16.039 36.739  1.00 18.62 ? 36  HIS A CD2  1 
ATOM   302  C  CE1  . HIS A 1 36  ? -14.269 -17.382 35.229  1.00 20.22 ? 36  HIS A CE1  1 
ATOM   303  N  NE2  . HIS A 1 36  ? -15.362 -17.114 35.918  1.00 21.29 ? 36  HIS A NE2  1 
ATOM   304  N  N    . THR A 1 37  ? -12.033 -11.278 36.992  1.00 17.47 ? 37  THR A N    1 
ATOM   305  C  CA   . THR A 1 37  ? -11.408 -10.177 37.726  1.00 17.97 ? 37  THR A CA   1 
ATOM   306  C  C    . THR A 1 37  ? -11.961 -8.802  37.317  1.00 17.19 ? 37  THR A C    1 
ATOM   307  O  O    . THR A 1 37  ? -11.840 -7.836  38.068  1.00 17.52 ? 37  THR A O    1 
ATOM   308  C  CB   . THR A 1 37  ? -9.873  -10.231 37.596  1.00 18.39 ? 37  THR A CB   1 
ATOM   309  O  OG1  . THR A 1 37  ? -9.407  -11.456 38.180  1.00 21.58 ? 37  THR A OG1  1 
ATOM   310  C  CG2  . THR A 1 37  ? -9.197  -9.051  38.311  1.00 20.19 ? 37  THR A CG2  1 
ATOM   311  N  N    . ALA A 1 38  ? -12.557 -8.715  36.134  1.00 16.38 ? 38  ALA A N    1 
ATOM   312  C  CA   . ALA A 1 38  ? -13.199 -7.461  35.712  1.00 16.45 ? 38  ALA A CA   1 
ATOM   313  C  C    . ALA A 1 38  ? -14.386 -7.193  36.633  1.00 16.88 ? 38  ALA A C    1 
ATOM   314  O  O    . ALA A 1 38  ? -15.240 -8.052  36.825  1.00 18.02 ? 38  ALA A O    1 
ATOM   315  C  CB   . ALA A 1 38  ? -13.633 -7.518  34.260  1.00 16.15 ? 38  ALA A CB   1 
ATOM   316  N  N    . LYS A 1 39  ? -14.430 -6.008  37.220  1.00 17.09 ? 39  LYS A N    1 
ATOM   317  C  CA   . LYS A 1 39  ? -15.476 -5.735  38.195  1.00 17.33 ? 39  LYS A CA   1 
ATOM   318  C  C    . LYS A 1 39  ? -16.653 -5.016  37.540  1.00 16.61 ? 39  LYS A C    1 
ATOM   319  O  O    . LYS A 1 39  ? -16.475 -4.029  36.821  1.00 15.50 ? 39  LYS A O    1 
ATOM   320  C  CB   . LYS A 1 39  ? -14.909 -4.914  39.340  1.00 17.90 ? 39  LYS A CB   1 
ATOM   321  C  CG   . LYS A 1 39  ? -15.758 -4.916  40.599  1.00 20.11 ? 39  LYS A CG   1 
ATOM   322  C  CD   . LYS A 1 39  ? -15.360 -3.745  41.476  1.00 22.73 ? 39  LYS A CD   1 
ATOM   323  C  CE   . LYS A 1 39  ? -16.452 -3.390  42.470  1.00 24.91 ? 39  LYS A CE   1 
ATOM   324  N  NZ   . LYS A 1 39  ? -16.646 -4.472  43.461  1.00 27.33 ? 39  LYS A NZ   1 
ATOM   325  N  N    . TYR A 1 40  ? -17.859 -5.510  37.798  1.00 16.81 ? 40  TYR A N    1 
ATOM   326  C  CA   . TYR A 1 40  ? -19.057 -4.800  37.384  1.00 17.27 ? 40  TYR A CA   1 
ATOM   327  C  C    . TYR A 1 40  ? -19.074 -3.408  38.011  1.00 16.78 ? 40  TYR A C    1 
ATOM   328  O  O    . TYR A 1 40  ? -18.885 -3.263  39.226  1.00 16.42 ? 40  TYR A O    1 
ATOM   329  C  CB   . TYR A 1 40  ? -20.306 -5.584  37.796  1.00 18.47 ? 40  TYR A CB   1 
ATOM   330  C  CG   . TYR A 1 40  ? -21.592 -4.812  37.653  1.00 20.08 ? 40  TYR A CG   1 
ATOM   331  C  CD1  . TYR A 1 40  ? -21.976 -4.286  36.425  1.00 19.50 ? 40  TYR A CD1  1 
ATOM   332  C  CD2  . TYR A 1 40  ? -22.438 -4.620  38.750  1.00 22.39 ? 40  TYR A CD2  1 
ATOM   333  C  CE1  . TYR A 1 40  ? -23.151 -3.579  36.281  1.00 21.70 ? 40  TYR A CE1  1 
ATOM   334  C  CE2  . TYR A 1 40  ? -23.627 -3.910  38.620  1.00 22.17 ? 40  TYR A CE2  1 
ATOM   335  C  CZ   . TYR A 1 40  ? -23.973 -3.391  37.381  1.00 21.92 ? 40  TYR A CZ   1 
ATOM   336  O  OH   . TYR A 1 40  ? -25.136 -2.683  37.222  1.00 22.51 ? 40  TYR A OH   1 
ATOM   337  N  N    . ASP A 1 41  ? -19.311 -2.394  37.187  1.00 16.36 ? 41  ASP A N    1 
ATOM   338  C  CA   . ASP A 1 41  ? -19.344 -1.007  37.656  1.00 16.68 ? 41  ASP A CA   1 
ATOM   339  C  C    . ASP A 1 41  ? -20.725 -0.402  37.401  1.00 17.49 ? 41  ASP A C    1 
ATOM   340  O  O    . ASP A 1 41  ? -21.021 0.013   36.281  1.00 16.28 ? 41  ASP A O    1 
ATOM   341  C  CB   . ASP A 1 41  ? -18.270 -0.177  36.958  1.00 16.94 ? 41  ASP A CB   1 
ATOM   342  C  CG   . ASP A 1 41  ? -18.167 1.227   37.516  1.00 17.63 ? 41  ASP A CG   1 
ATOM   343  O  OD1  . ASP A 1 41  ? -19.035 1.622   38.319  1.00 17.74 ? 41  ASP A OD1  1 
ATOM   344  O  OD2  . ASP A 1 41  ? -17.210 1.932   37.157  1.00 18.09 ? 41  ASP A OD2  1 
ATOM   345  N  N    . PRO A 1 42  ? -21.574 -0.339  38.447  1.00 18.24 ? 42  PRO A N    1 
ATOM   346  C  CA   . PRO A 1 42  ? -22.951 0.111   38.214  1.00 19.06 ? 42  PRO A CA   1 
ATOM   347  C  C    . PRO A 1 42  ? -23.049 1.594   37.856  1.00 19.42 ? 42  PRO A C    1 
ATOM   348  O  O    . PRO A 1 42  ? -24.119 2.041   37.427  1.00 19.73 ? 42  PRO A O    1 
ATOM   349  C  CB   . PRO A 1 42  ? -23.639 -0.176  39.557  1.00 19.26 ? 42  PRO A CB   1 
ATOM   350  C  CG   . PRO A 1 42  ? -22.547 -0.027  40.562  1.00 18.68 ? 42  PRO A CG   1 
ATOM   351  C  CD   . PRO A 1 42  ? -21.341 -0.662  39.870  1.00 18.75 ? 42  PRO A CD   1 
ATOM   352  N  N    . SER A 1 43  ? -21.953 2.336   38.028  1.00 19.64 ? 43  SER A N    1 
ATOM   353  C  CA   . SER A 1 43  ? -21.870 3.733   37.599  1.00 20.43 ? 43  SER A CA   1 
ATOM   354  C  C    . SER A 1 43  ? -21.688 3.889   36.086  1.00 20.26 ? 43  SER A C    1 
ATOM   355  O  O    . SER A 1 43  ? -21.853 4.989   35.551  1.00 20.64 ? 43  SER A O    1 
ATOM   356  C  CB   . SER A 1 43  ? -20.750 4.476   38.337  1.00 20.58 ? 43  SER A CB   1 
ATOM   357  O  OG   . SER A 1 43  ? -19.465 4.201   37.790  1.00 21.53 ? 43  SER A OG   1 
ATOM   358  N  N    . LEU A 1 44  ? -21.331 2.804   35.398  1.00 20.03 ? 44  LEU A N    1 
ATOM   359  C  CA   . LEU A 1 44  ? -21.216 2.856   33.934  1.00 19.77 ? 44  LEU A CA   1 
ATOM   360  C  C    . LEU A 1 44  ? -22.575 2.997   33.250  1.00 20.60 ? 44  LEU A C    1 
ATOM   361  O  O    . LEU A 1 44  ? -23.580 2.462   33.717  1.00 21.44 ? 44  LEU A O    1 
ATOM   362  C  CB   . LEU A 1 44  ? -20.485 1.637   33.380  1.00 19.05 ? 44  LEU A CB   1 
ATOM   363  C  CG   . LEU A 1 44  ? -18.979 1.549   33.598  1.00 17.18 ? 44  LEU A CG   1 
ATOM   364  C  CD1  . LEU A 1 44  ? -18.492 0.153   33.194  1.00 15.57 ? 44  LEU A CD1  1 
ATOM   365  C  CD2  . LEU A 1 44  ? -18.226 2.638   32.838  1.00 15.28 ? 44  LEU A CD2  1 
ATOM   366  N  N    . LYS A 1 45  ? -22.584 3.719   32.138  1.00 20.60 ? 45  LYS A N    1 
ATOM   367  C  CA   . LYS A 1 45  ? -23.810 3.946   31.372  1.00 20.62 ? 45  LYS A CA   1 
ATOM   368  C  C    . LYS A 1 45  ? -23.896 3.026   30.168  1.00 20.06 ? 45  LYS A C    1 
ATOM   369  O  O    . LYS A 1 45  ? -22.877 2.472   29.731  1.00 20.34 ? 45  LYS A O    1 
ATOM   370  C  CB   . LYS A 1 45  ? -23.882 5.397   30.932  1.00 20.77 ? 45  LYS A CB   1 
ATOM   371  C  CG   . LYS A 1 45  ? -23.829 6.351   32.099  1.00 22.52 ? 45  LYS A CG   1 
ATOM   372  C  CD   . LYS A 1 45  ? -23.741 7.786   31.651  1.00 26.06 ? 45  LYS A CD   1 
ATOM   373  C  CE   . LYS A 1 45  ? -23.187 8.673   32.775  1.00 28.81 ? 45  LYS A CE   1 
ATOM   374  N  NZ   . LYS A 1 45  ? -24.146 8.796   33.925  1.00 30.80 ? 45  LYS A NZ   1 
ATOM   375  N  N    . PRO A 1 46  ? -25.129 2.803   29.664  1.00 19.18 ? 46  PRO A N    1 
ATOM   376  C  CA   . PRO A 1 46  ? -25.275 2.151   28.376  1.00 18.55 ? 46  PRO A CA   1 
ATOM   377  C  C    . PRO A 1 46  ? -24.488 2.933   27.335  1.00 17.07 ? 46  PRO A C    1 
ATOM   378  O  O    . PRO A 1 46  ? -24.419 4.167   27.387  1.00 16.95 ? 46  PRO A O    1 
ATOM   379  C  CB   . PRO A 1 46  ? -26.780 2.277   28.095  1.00 18.46 ? 46  PRO A CB   1 
ATOM   380  C  CG   . PRO A 1 46  ? -27.405 2.303   29.431  1.00 19.34 ? 46  PRO A CG   1 
ATOM   381  C  CD   . PRO A 1 46  ? -26.444 3.095   30.282  1.00 19.39 ? 46  PRO A CD   1 
ATOM   382  N  N    . LEU A 1 47  ? -23.881 2.208   26.411  1.00 16.94 ? 47  LEU A N    1 
ATOM   383  C  CA   . LEU A 1 47  ? -23.150 2.843   25.335  1.00 15.58 ? 47  LEU A CA   1 
ATOM   384  C  C    . LEU A 1 47  ? -24.169 3.471   24.381  1.00 15.32 ? 47  LEU A C    1 
ATOM   385  O  O    . LEU A 1 47  ? -25.264 2.910   24.194  1.00 15.69 ? 47  LEU A O    1 
ATOM   386  C  CB   . LEU A 1 47  ? -22.329 1.784   24.613  1.00 16.44 ? 47  LEU A CB   1 
ATOM   387  C  CG   . LEU A 1 47  ? -21.156 2.211   23.762  1.00 17.31 ? 47  LEU A CG   1 
ATOM   388  C  CD1  . LEU A 1 47  ? -20.157 3.047   24.584  1.00 17.14 ? 47  LEU A CD1  1 
ATOM   389  C  CD2  . LEU A 1 47  ? -20.515 0.953   23.202  1.00 18.70 ? 47  LEU A CD2  1 
ATOM   390  N  N    . SER A 1 48  ? -23.830 4.621   23.799  1.00 13.00 ? 48  SER A N    1 
ATOM   391  C  CA   . SER A 1 48  ? -24.670 5.248   22.768  1.00 12.30 ? 48  SER A CA   1 
ATOM   392  C  C    . SER A 1 48  ? -23.930 5.306   21.449  1.00 12.02 ? 48  SER A C    1 
ATOM   393  O  O    . SER A 1 48  ? -22.970 6.059   21.295  1.00 11.83 ? 48  SER A O    1 
ATOM   394  C  CB   . SER A 1 48  ? -25.110 6.651   23.202  1.00 12.76 ? 48  SER A CB   1 
ATOM   395  O  OG   . SER A 1 48  ? -25.671 7.389   22.132  1.00 12.63 ? 48  SER A OG   1 
ATOM   396  N  N    . VAL A 1 49  ? -24.385 4.491   20.504  1.00 11.98 ? 49  VAL A N    1 
ATOM   397  C  CA   . VAL A 1 49  ? -23.777 4.402   19.183  1.00 13.44 ? 49  VAL A CA   1 
ATOM   398  C  C    . VAL A 1 49  ? -24.775 4.999   18.203  1.00 13.91 ? 49  VAL A C    1 
ATOM   399  O  O    . VAL A 1 49  ? -25.836 4.432   17.988  1.00 14.04 ? 49  VAL A O    1 
ATOM   400  C  CB   . VAL A 1 49  ? -23.489 2.922   18.807  1.00 14.01 ? 49  VAL A CB   1 
ATOM   401  C  CG1  . VAL A 1 49  ? -22.768 2.828   17.473  1.00 14.73 ? 49  VAL A CG1  1 
ATOM   402  C  CG2  . VAL A 1 49  ? -22.690 2.221   19.900  1.00 13.76 ? 49  VAL A CG2  1 
ATOM   403  N  N    . SER A 1 50  ? -24.456 6.156   17.633  1.00 14.04 ? 50  SER A N    1 
ATOM   404  C  CA   . SER A 1 50  ? -25.382 6.809   16.700  1.00 14.85 ? 50  SER A CA   1 
ATOM   405  C  C    . SER A 1 50  ? -24.754 6.867   15.318  1.00 14.18 ? 50  SER A C    1 
ATOM   406  O  O    . SER A 1 50  ? -24.064 7.823   14.988  1.00 14.23 ? 50  SER A O    1 
ATOM   407  C  CB   . SER A 1 50  ? -25.775 8.201   17.209  1.00 15.93 ? 50  SER A CB   1 
ATOM   408  O  OG   . SER A 1 50  ? -26.403 8.100   18.481  1.00 20.14 ? 50  SER A OG   1 
ATOM   409  N  N    . TYR A 1 51  ? -24.976 5.816   14.534  1.00 13.51 ? 51  TYR A N    1 
ATOM   410  C  CA   . TYR A 1 51  ? -24.385 5.683   13.204  1.00 12.91 ? 51  TYR A CA   1 
ATOM   411  C  C    . TYR A 1 51  ? -25.369 5.887   12.037  1.00 13.99 ? 51  TYR A C    1 
ATOM   412  O  O    . TYR A 1 51  ? -24.985 5.687   10.887  1.00 13.70 ? 51  TYR A O    1 
ATOM   413  C  CB   . TYR A 1 51  ? -23.734 4.312   13.030  1.00 11.72 ? 51  TYR A CB   1 
ATOM   414  C  CG   . TYR A 1 51  ? -22.462 4.038   13.822  1.00 9.80  ? 51  TYR A CG   1 
ATOM   415  C  CD1  . TYR A 1 51  ? -21.736 5.081   14.441  1.00 9.63  ? 51  TYR A CD1  1 
ATOM   416  C  CD2  . TYR A 1 51  ? -21.961 2.745   13.904  1.00 8.74  ? 51  TYR A CD2  1 
ATOM   417  C  CE1  . TYR A 1 51  ? -20.554 4.815   15.172  1.00 6.81  ? 51  TYR A CE1  1 
ATOM   418  C  CE2  . TYR A 1 51  ? -20.784 2.465   14.610  1.00 8.43  ? 51  TYR A CE2  1 
ATOM   419  C  CZ   . TYR A 1 51  ? -20.090 3.495   15.243  1.00 9.34  ? 51  TYR A CZ   1 
ATOM   420  O  OH   . TYR A 1 51  ? -18.930 3.170   15.936  1.00 7.74  ? 51  TYR A OH   1 
ATOM   421  N  N    . ASP A 1 52  ? -26.622 6.250   12.332  1.00 15.49 ? 52  ASP A N    1 
ATOM   422  C  CA   . ASP A 1 52  ? -27.644 6.469   11.281  1.00 17.15 ? 52  ASP A CA   1 
ATOM   423  C  C    . ASP A 1 52  ? -27.215 7.451   10.172  1.00 17.34 ? 52  ASP A C    1 
ATOM   424  O  O    . ASP A 1 52  ? -27.537 7.233   8.996   1.00 17.64 ? 52  ASP A O    1 
ATOM   425  C  CB   . ASP A 1 52  ? -28.994 6.883   11.890  1.00 18.03 ? 52  ASP A CB   1 
ATOM   426  C  CG   . ASP A 1 52  ? -28.895 8.122   12.748  1.00 21.30 ? 52  ASP A CG   1 
ATOM   427  O  OD1  . ASP A 1 52  ? -28.418 8.027   13.903  1.00 26.22 ? 52  ASP A OD1  1 
ATOM   428  O  OD2  . ASP A 1 52  ? -29.313 9.198   12.279  1.00 27.28 ? 52  ASP A OD2  1 
ATOM   429  N  N    . GLN A 1 53  ? -26.475 8.496   10.545  1.00 16.60 ? 53  GLN A N    1 
ATOM   430  C  CA   . GLN A 1 53  ? -25.973 9.503   9.599   1.00 17.27 ? 53  GLN A CA   1 
ATOM   431  C  C    . GLN A 1 53  ? -24.527 9.283   9.096   1.00 15.77 ? 53  GLN A C    1 
ATOM   432  O  O    . GLN A 1 53  ? -23.971 10.158  8.431   1.00 15.26 ? 53  GLN A O    1 
ATOM   433  C  CB   . GLN A 1 53  ? -26.080 10.913  10.218  1.00 17.79 ? 53  GLN A CB   1 
ATOM   434  C  CG   . GLN A 1 53  ? -27.509 11.374  10.521  1.00 21.66 ? 53  GLN A CG   1 
ATOM   435  C  CD   . GLN A 1 53  ? -28.324 11.531  9.255   1.00 25.07 ? 53  GLN A CD   1 
ATOM   436  O  OE1  . GLN A 1 53  ? -29.223 10.739  8.980   1.00 28.13 ? 53  GLN A OE1  1 
ATOM   437  N  NE2  . GLN A 1 53  ? -27.985 12.540  8.453   1.00 27.64 ? 53  GLN A NE2  1 
ATOM   438  N  N    . ALA A 1 54  ? -23.925 8.132   9.396   1.00 15.24 ? 54  ALA A N    1 
ATOM   439  C  CA   . ALA A 1 54  ? -22.545 7.862   8.976   1.00 14.19 ? 54  ALA A CA   1 
ATOM   440  C  C    . ALA A 1 54  ? -22.382 7.984   7.467   1.00 14.43 ? 54  ALA A C    1 
ATOM   441  O  O    . ALA A 1 54  ? -23.243 7.517   6.714   1.00 15.60 ? 54  ALA A O    1 
ATOM   442  C  CB   . ALA A 1 54  ? -22.088 6.465   9.450   1.00 14.44 ? 54  ALA A CB   1 
ATOM   443  N  N    . THR A 1 55  ? -21.298 8.629   7.032   1.00 14.07 ? 55  THR A N    1 
ATOM   444  C  CA   . THR A 1 55  ? -20.987 8.784   5.610   1.00 14.41 ? 55  THR A CA   1 
ATOM   445  C  C    . THR A 1 55  ? -19.618 8.193   5.286   1.00 12.86 ? 55  THR A C    1 
ATOM   446  O  O    . THR A 1 55  ? -18.599 8.830   5.541   1.00 12.51 ? 55  THR A O    1 
ATOM   447  C  CB   . THR A 1 55  ? -20.941 10.274  5.173   1.00 15.08 ? 55  THR A CB   1 
ATOM   448  O  OG1  . THR A 1 55  ? -22.156 10.939  5.528   1.00 19.25 ? 55  THR A OG1  1 
ATOM   449  C  CG2  . THR A 1 55  ? -20.775 10.353  3.682   1.00 16.27 ? 55  THR A CG2  1 
ATOM   450  N  N    . SER A 1 56  ? -19.592 6.983   4.743   1.00 12.11 ? 56  SER A N    1 
ATOM   451  C  CA   . SER A 1 56  ? -18.322 6.381   4.343   1.00 12.58 ? 56  SER A CA   1 
ATOM   452  C  C    . SER A 1 56  ? -17.874 7.020   3.032   1.00 12.72 ? 56  SER A C    1 
ATOM   453  O  O    . SER A 1 56  ? -18.713 7.470   2.247   1.00 13.08 ? 56  SER A O    1 
ATOM   454  C  CB   . SER A 1 56  ? -18.424 4.848   4.223   1.00 12.45 ? 56  SER A CB   1 
ATOM   455  O  OG   . SER A 1 56  ? -19.255 4.437   3.141   1.00 13.43 ? 56  SER A OG   1 
ATOM   456  N  N    . LEU A 1 57  ? -16.566 7.071   2.797   1.00 12.45 ? 57  LEU A N    1 
ATOM   457  C  CA   . LEU A 1 57  ? -16.047 7.699   1.581   1.00 12.57 ? 57  LEU A CA   1 
ATOM   458  C  C    . LEU A 1 57  ? -15.150 6.799   0.752   1.00 11.80 ? 57  LEU A C    1 
ATOM   459  O  O    . LEU A 1 57  ? -15.220 6.805   -0.481  1.00 11.68 ? 57  LEU A O    1 
ATOM   460  C  CB   . LEU A 1 57  ? -15.279 8.978   1.927   1.00 13.55 ? 57  LEU A CB   1 
ATOM   461  C  CG   . LEU A 1 57  ? -16.045 10.132  2.582   1.00 16.33 ? 57  LEU A CG   1 
ATOM   462  C  CD1  . LEU A 1 57  ? -15.056 11.156  3.116   1.00 18.43 ? 57  LEU A CD1  1 
ATOM   463  C  CD2  . LEU A 1 57  ? -17.033 10.782  1.609   1.00 18.51 ? 57  LEU A CD2  1 
ATOM   464  N  N    . ARG A 1 58  ? -14.267 6.061   1.420   1.00 10.55 ? 58  ARG A N    1 
ATOM   465  C  CA   . ARG A 1 58  ? -13.169 5.401   0.722   1.00 10.32 ? 58  ARG A CA   1 
ATOM   466  C  C    . ARG A 1 58  ? -12.660 4.235   1.535   1.00 9.28  ? 58  ARG A C    1 
ATOM   467  O  O    . ARG A 1 58  ? -12.792 4.224   2.765   1.00 9.17  ? 58  ARG A O    1 
ATOM   468  C  CB   . ARG A 1 58  ? -12.019 6.393   0.525   1.00 10.36 ? 58  ARG A CB   1 
ATOM   469  C  CG   . ARG A 1 58  ? -10.989 5.974   -0.520  1.00 10.86 ? 58  ARG A CG   1 
ATOM   470  C  CD   . ARG A 1 58  ? -9.900  7.038   -0.650  1.00 12.21 ? 58  ARG A CD   1 
ATOM   471  N  NE   . ARG A 1 58  ? -9.088  7.086   0.562   1.00 12.56 ? 58  ARG A NE   1 
ATOM   472  C  CZ   . ARG A 1 58  ? -7.775  7.305   0.574   1.00 12.99 ? 58  ARG A CZ   1 
ATOM   473  N  NH1  . ARG A 1 58  ? -7.126  7.512   -0.561  1.00 13.87 ? 58  ARG A NH1  1 
ATOM   474  N  NH2  . ARG A 1 58  ? -7.110  7.324   1.724   1.00 14.27 ? 58  ARG A NH2  1 
ATOM   475  N  N    . ILE A 1 59  ? -12.059 3.272   0.844   1.00 8.92  ? 59  ILE A N    1 
ATOM   476  C  CA   . ILE A 1 59  ? -11.391 2.160   1.518   1.00 8.15  ? 59  ILE A CA   1 
ATOM   477  C  C    . ILE A 1 59  ? -9.939  2.103   1.034   1.00 8.39  ? 59  ILE A C    1 
ATOM   478  O  O    . ILE A 1 59  ? -9.667  2.225   -0.167  1.00 7.96  ? 59  ILE A O    1 
ATOM   479  C  CB   . ILE A 1 59  ? -12.167 0.820   1.315   1.00 7.86  ? 59  ILE A CB   1 
ATOM   480  C  CG1  . ILE A 1 59  ? -11.573 -0.314  2.172   1.00 7.05  ? 59  ILE A CG1  1 
ATOM   481  C  CG2  . ILE A 1 59  ? -12.251 0.437   -0.183  1.00 8.06  ? 59  ILE A CG2  1 
ATOM   482  C  CD1  . ILE A 1 59  ? -12.411 -1.618  2.120   1.00 8.89  ? 59  ILE A CD1  1 
ATOM   483  N  N    . LEU A 1 60  ? -9.015  1.926   1.979   1.00 7.99  ? 60  LEU A N    1 
ATOM   484  C  CA   . LEU A 1 60  ? -7.594  2.047   1.716   1.00 7.63  ? 60  LEU A CA   1 
ATOM   485  C  C    . LEU A 1 60  ? -6.803  0.867   2.275   1.00 7.64  ? 60  LEU A C    1 
ATOM   486  O  O    . LEU A 1 60  ? -6.951  0.514   3.446   1.00 7.44  ? 60  LEU A O    1 
ATOM   487  C  CB   . LEU A 1 60  ? -7.061  3.360   2.342   1.00 8.08  ? 60  LEU A CB   1 
ATOM   488  C  CG   . LEU A 1 60  ? -5.521  3.495   2.358   1.00 8.57  ? 60  LEU A CG   1 
ATOM   489  C  CD1  . LEU A 1 60  ? -4.971  3.616   0.940   1.00 10.24 ? 60  LEU A CD1  1 
ATOM   490  C  CD2  . LEU A 1 60  ? -5.025  4.645   3.248   1.00 8.26  ? 60  LEU A CD2  1 
ATOM   491  N  N    . ASN A 1 61  ? -5.975  0.256   1.432   1.00 7.15  ? 61  ASN A N    1 
ATOM   492  C  CA   . ASN A 1 61  ? -4.954  -0.683  1.913   1.00 7.87  ? 61  ASN A CA   1 
ATOM   493  C  C    . ASN A 1 61  ? -3.689  0.105   2.278   1.00 8.78  ? 61  ASN A C    1 
ATOM   494  O  O    . ASN A 1 61  ? -3.015  0.629   1.401   1.00 8.68  ? 61  ASN A O    1 
ATOM   495  C  CB   . ASN A 1 61  ? -4.655  -1.739  0.832   1.00 7.63  ? 61  ASN A CB   1 
ATOM   496  C  CG   . ASN A 1 61  ? -3.588  -2.740  1.260   1.00 8.54  ? 61  ASN A CG   1 
ATOM   497  O  OD1  . ASN A 1 61  ? -2.771  -2.469  2.144   1.00 9.88  ? 61  ASN A OD1  1 
ATOM   498  N  ND2  . ASN A 1 61  ? -3.613  -3.924  0.653   1.00 8.99  ? 61  ASN A ND2  1 
ATOM   499  N  N    . ASN A 1 62  ? -3.381  0.198   3.571   1.00 8.74  ? 62  ASN A N    1 
ATOM   500  C  CA   . ASN A 1 62  ? -2.278  1.042   4.029   1.00 8.91  ? 62  ASN A CA   1 
ATOM   501  C  C    . ASN A 1 62  ? -0.997  0.261   4.295   1.00 8.91  ? 62  ASN A C    1 
ATOM   502  O  O    . ASN A 1 62  ? -0.035  0.803   4.862   1.00 9.63  ? 62  ASN A O    1 
ATOM   503  C  CB   . ASN A 1 62  ? -2.693  1.873   5.257   1.00 9.34  ? 62  ASN A CB   1 
ATOM   504  C  CG   . ASN A 1 62  ? -2.961  1.024   6.479   1.00 9.87  ? 62  ASN A CG   1 
ATOM   505  O  OD1  . ASN A 1 62  ? -2.658  -0.175  6.505   1.00 9.74  ? 62  ASN A OD1  1 
ATOM   506  N  ND2  . ASN A 1 62  ? -3.542  1.642   7.506   1.00 13.29 ? 62  ASN A ND2  1 
ATOM   507  N  N    . GLY A 1 63  ? -0.980  -1.008  3.882   1.00 8.26  ? 63  GLY A N    1 
ATOM   508  C  CA   . GLY A 1 63  ? 0.179   -1.869  4.056   1.00 8.66  ? 63  GLY A CA   1 
ATOM   509  C  C    . GLY A 1 63  ? 0.198   -2.652  5.358   1.00 9.13  ? 63  GLY A C    1 
ATOM   510  O  O    . GLY A 1 63  ? 1.051   -3.527  5.540   1.00 9.62  ? 63  GLY A O    1 
ATOM   511  N  N    . HIS A 1 64  ? -0.747  -2.344  6.247   1.00 8.92  ? 64  HIS A N    1 
ATOM   512  C  CA   . HIS A 1 64  ? -0.864  -3.010  7.562   1.00 10.13 ? 64  HIS A CA   1 
ATOM   513  C  C    . HIS A 1 64  ? -2.269  -3.606  7.747   1.00 9.82  ? 64  HIS A C    1 
ATOM   514  O  O    . HIS A 1 64  ? -2.425  -4.666  8.352   1.00 11.13 ? 64  HIS A O    1 
ATOM   515  C  CB   . HIS A 1 64  ? -0.563  -2.026  8.708   1.00 10.58 ? 64  HIS A CB   1 
ATOM   516  C  CG   . HIS A 1 64  ? 0.732   -1.281  8.546   1.00 15.01 ? 64  HIS A CG   1 
ATOM   517  N  ND1  . HIS A 1 64  ? 1.963   -1.900  8.631   1.00 17.16 ? 64  HIS A ND1  1 
ATOM   518  C  CD2  . HIS A 1 64  ? 0.986   0.034   8.343   1.00 17.49 ? 64  HIS A CD2  1 
ATOM   519  C  CE1  . HIS A 1 64  ? 2.921   -1.004  8.465   1.00 18.37 ? 64  HIS A CE1  1 
ATOM   520  N  NE2  . HIS A 1 64  ? 2.356   0.177   8.276   1.00 17.41 ? 64  HIS A NE2  1 
ATOM   521  N  N    . ALA A 1 65  ? -3.287  -2.916  7.240   1.00 8.25  ? 65  ALA A N    1 
ATOM   522  C  CA   . ALA A 1 65  ? -4.663  -3.393  7.290   1.00 7.84  ? 65  ALA A CA   1 
ATOM   523  C  C    . ALA A 1 65  ? -5.398  -2.674  6.165   1.00 7.09  ? 65  ALA A C    1 
ATOM   524  O  O    . ALA A 1 65  ? -4.738  -2.069  5.297   1.00 8.08  ? 65  ALA A O    1 
ATOM   525  C  CB   . ALA A 1 65  ? -5.302  -3.105  8.658   1.00 7.75  ? 65  ALA A CB   1 
ATOM   526  N  N    . PHE A 1 66  ? -6.724  -2.745  6.138   1.00 6.27  ? 66  PHE A N    1 
ATOM   527  C  CA   . PHE A 1 66  ? -7.499  -1.831  5.274   1.00 6.15  ? 66  PHE A CA   1 
ATOM   528  C  C    . PHE A 1 66  ? -8.385  -0.957  6.154   1.00 6.41  ? 66  PHE A C    1 
ATOM   529  O  O    . PHE A 1 66  ? -8.980  -1.444  7.125   1.00 6.33  ? 66  PHE A O    1 
ATOM   530  C  CB   . PHE A 1 66  ? -8.318  -2.560  4.191   1.00 7.00  ? 66  PHE A CB   1 
ATOM   531  C  CG   . PHE A 1 66  ? -9.343  -3.519  4.745   1.00 7.62  ? 66  PHE A CG   1 
ATOM   532  C  CD1  . PHE A 1 66  ? -10.631 -3.080  5.059   1.00 7.92  ? 66  PHE A CD1  1 
ATOM   533  C  CD2  . PHE A 1 66  ? -9.034  -4.872  4.904   1.00 8.51  ? 66  PHE A CD2  1 
ATOM   534  C  CE1  . PHE A 1 66  ? -11.591 -3.950  5.565   1.00 8.14  ? 66  PHE A CE1  1 
ATOM   535  C  CE2  . PHE A 1 66  ? -9.990  -5.769  5.434   1.00 8.47  ? 66  PHE A CE2  1 
ATOM   536  C  CZ   . PHE A 1 66  ? -11.270 -5.314  5.753   1.00 7.25  ? 66  PHE A CZ   1 
ATOM   537  N  N    . ASN A 1 67  ? -8.454  0.332   5.827   1.00 6.56  ? 67  ASN A N    1 
ATOM   538  C  CA   . ASN A 1 67  ? -9.291  1.266   6.568   1.00 6.49  ? 67  ASN A CA   1 
ATOM   539  C  C    . ASN A 1 67  ? -10.489 1.668   5.740   1.00 7.36  ? 67  ASN A C    1 
ATOM   540  O  O    . ASN A 1 67  ? -10.329 2.091   4.577   1.00 6.55  ? 67  ASN A O    1 
ATOM   541  C  CB   . ASN A 1 67  ? -8.509  2.550   6.897   1.00 7.31  ? 67  ASN A CB   1 
ATOM   542  C  CG   . ASN A 1 67  ? -7.401  2.335   7.906   1.00 9.20  ? 67  ASN A CG   1 
ATOM   543  O  OD1  . ASN A 1 67  ? -7.293  1.276   8.523   1.00 9.57  ? 67  ASN A OD1  1 
ATOM   544  N  ND2  . ASN A 1 67  ? -6.545  3.351   8.065   1.00 12.72 ? 67  ASN A ND2  1 
ATOM   545  N  N    . VAL A 1 68  ? -11.675 1.572   6.339   1.00 6.26  ? 68  VAL A N    1 
ATOM   546  C  CA   . VAL A 1 68  ? -12.864 2.152   5.729   1.00 7.28  ? 68  VAL A CA   1 
ATOM   547  C  C    . VAL A 1 68  ? -13.012 3.521   6.372   1.00 7.84  ? 68  VAL A C    1 
ATOM   548  O  O    . VAL A 1 68  ? -13.190 3.633   7.601   1.00 7.13  ? 68  VAL A O    1 
ATOM   549  C  CB   . VAL A 1 68  ? -14.112 1.280   5.903   1.00 7.20  ? 68  VAL A CB   1 
ATOM   550  C  CG1  . VAL A 1 68  ? -15.371 2.038   5.425   1.00 8.00  ? 68  VAL A CG1  1 
ATOM   551  C  CG2  . VAL A 1 68  ? -13.957 -0.019  5.131   1.00 6.99  ? 68  VAL A CG2  1 
ATOM   552  N  N    . GLU A 1 69  ? -12.897 4.557   5.538   1.00 7.98  ? 69  GLU A N    1 
ATOM   553  C  CA   . GLU A 1 69  ? -12.807 5.935   6.004   1.00 8.51  ? 69  GLU A CA   1 
ATOM   554  C  C    . GLU A 1 69  ? -14.153 6.653   5.913   1.00 9.19  ? 69  GLU A C    1 
ATOM   555  O  O    . GLU A 1 69  ? -14.917 6.444   4.963   1.00 9.37  ? 69  GLU A O    1 
ATOM   556  C  CB   . GLU A 1 69  ? -11.801 6.690   5.143   1.00 9.29  ? 69  GLU A CB   1 
ATOM   557  C  CG   . GLU A 1 69  ? -10.377 6.164   5.233   1.00 9.60  ? 69  GLU A CG   1 
ATOM   558  C  CD   . GLU A 1 69  ? -9.522  6.633   4.068   1.00 11.31 ? 69  GLU A CD   1 
ATOM   559  O  OE1  . GLU A 1 69  ? -10.072 7.297   3.163   1.00 13.91 ? 69  GLU A OE1  1 
ATOM   560  O  OE2  . GLU A 1 69  ? -8.320  6.324   4.046   1.00 12.05 ? 69  GLU A OE2  1 
ATOM   561  N  N    . PHE A 1 70  ? -14.412 7.503   6.902   1.00 9.12  ? 70  PHE A N    1 
ATOM   562  C  CA   . PHE A 1 70  ? -15.671 8.257   6.997   1.00 9.69  ? 70  PHE A CA   1 
ATOM   563  C  C    . PHE A 1 70  ? -15.469 9.766   6.928   1.00 10.75 ? 70  PHE A C    1 
ATOM   564  O  O    . PHE A 1 70  ? -14.406 10.276  7.288   1.00 10.35 ? 70  PHE A O    1 
ATOM   565  C  CB   . PHE A 1 70  ? -16.405 7.892   8.299   1.00 9.32  ? 70  PHE A CB   1 
ATOM   566  C  CG   . PHE A 1 70  ? -16.983 6.508   8.287   1.00 8.12  ? 70  PHE A CG   1 
ATOM   567  C  CD1  . PHE A 1 70  ? -16.181 5.396   8.546   1.00 9.39  ? 70  PHE A CD1  1 
ATOM   568  C  CD2  . PHE A 1 70  ? -18.333 6.305   7.997   1.00 7.88  ? 70  PHE A CD2  1 
ATOM   569  C  CE1  . PHE A 1 70  ? -16.711 4.107   8.517   1.00 7.51  ? 70  PHE A CE1  1 
ATOM   570  C  CE2  . PHE A 1 70  ? -18.869 5.035   7.940   1.00 7.41  ? 70  PHE A CE2  1 
ATOM   571  C  CZ   . PHE A 1 70  ? -18.057 3.919   8.202   1.00 8.82  ? 70  PHE A CZ   1 
ATOM   572  N  N    A ASP A 1 71  ? -16.493 10.467  6.433   0.50 11.59 ? 71  ASP A N    1 
ATOM   573  N  N    B ASP A 1 71  ? -16.500 10.472  6.470   0.50 11.85 ? 71  ASP A N    1 
ATOM   574  C  CA   A ASP A 1 71  ? -16.534 11.925  6.535   0.50 12.42 ? 71  ASP A CA   1 
ATOM   575  C  CA   B ASP A 1 71  ? -16.502 11.933  6.465   0.50 12.94 ? 71  ASP A CA   1 
ATOM   576  C  C    A ASP A 1 71  ? -16.744 12.287  7.987   0.50 13.25 ? 71  ASP A C    1 
ATOM   577  C  C    B ASP A 1 71  ? -16.778 12.434  7.883   0.50 13.50 ? 71  ASP A C    1 
ATOM   578  O  O    A ASP A 1 71  ? -17.793 12.000  8.574   0.50 13.58 ? 71  ASP A O    1 
ATOM   579  O  O    B ASP A 1 71  ? -17.921 12.369  8.346   0.50 13.89 ? 71  ASP A O    1 
ATOM   580  C  CB   A ASP A 1 71  ? -17.657 12.530  5.684   0.50 12.80 ? 71  ASP A CB   1 
ATOM   581  C  CB   B ASP A 1 71  ? -17.577 12.428  5.490   0.50 13.46 ? 71  ASP A CB   1 
ATOM   582  C  CG   A ASP A 1 71  ? -17.764 14.058  5.837   0.50 11.98 ? 71  ASP A CG   1 
ATOM   583  C  CG   B ASP A 1 71  ? -17.353 13.862  5.028   0.50 14.29 ? 71  ASP A CG   1 
ATOM   584  O  OD1  A ASP A 1 71  ? -16.953 14.667  6.569   0.50 11.95 ? 71  ASP A OD1  1 
ATOM   585  O  OD1  B ASP A 1 71  ? -16.702 14.646  5.755   0.50 14.85 ? 71  ASP A OD1  1 
ATOM   586  O  OD2  A ASP A 1 71  ? -18.658 14.654  5.206   0.50 13.15 ? 71  ASP A OD2  1 
ATOM   587  O  OD2  B ASP A 1 71  ? -17.860 14.205  3.931   0.50 15.06 ? 71  ASP A OD2  1 
ATOM   588  N  N    . ASP A 1 72  ? -15.736 12.914  8.570   1.00 13.57 ? 72  ASP A N    1 
ATOM   589  C  CA   . ASP A 1 72  ? -15.844 13.384  9.952   1.00 15.00 ? 72  ASP A CA   1 
ATOM   590  C  C    . ASP A 1 72  ? -15.754 14.915  10.045  1.00 16.46 ? 72  ASP A C    1 
ATOM   591  O  O    . ASP A 1 72  ? -15.261 15.446  11.045  1.00 16.70 ? 72  ASP A O    1 
ATOM   592  C  CB   . ASP A 1 72  ? -14.777 12.714  10.832  1.00 15.56 ? 72  ASP A CB   1 
ATOM   593  C  CG   . ASP A 1 72  ? -13.350 13.089  10.438  1.00 16.94 ? 72  ASP A CG   1 
ATOM   594  O  OD1  . ASP A 1 72  ? -13.118 13.545  9.291   1.00 18.13 ? 72  ASP A OD1  1 
ATOM   595  O  OD2  . ASP A 1 72  ? -12.447 12.910  11.278  1.00 16.52 ? 72  ASP A OD2  1 
ATOM   596  N  N    . SER A 1 73  ? -16.197 15.601  8.992   1.00 18.04 ? 73  SER A N    1 
ATOM   597  C  CA   . SER A 1 73  ? -16.179 17.080  8.958   1.00 19.86 ? 73  SER A CA   1 
ATOM   598  C  C    . SER A 1 73  ? -17.391 17.724  9.644   1.00 20.95 ? 73  SER A C    1 
ATOM   599  O  O    . SER A 1 73  ? -17.457 18.945  9.817   1.00 20.88 ? 73  SER A O    1 
ATOM   600  C  CB   . SER A 1 73  ? -15.995 17.619  7.534   1.00 19.71 ? 73  SER A CB   1 
ATOM   601  O  OG   . SER A 1 73  ? -17.113 17.352  6.705   1.00 18.97 ? 73  SER A OG   1 
ATOM   602  N  N    . GLN A 1 74  ? -18.354 16.902  10.032  1.00 22.01 ? 74  GLN A N    1 
ATOM   603  C  CA   . GLN A 1 74  ? -19.417 17.365  10.915  1.00 23.66 ? 74  GLN A CA   1 
ATOM   604  C  C    . GLN A 1 74  ? -19.874 16.255  11.833  1.00 23.47 ? 74  GLN A C    1 
ATOM   605  O  O    . GLN A 1 74  ? -19.477 15.110  11.648  1.00 23.02 ? 74  GLN A O    1 
ATOM   606  C  CB   . GLN A 1 74  ? -20.587 17.970  10.135  1.00 23.74 ? 74  GLN A CB   1 
ATOM   607  C  CG   . GLN A 1 74  ? -20.843 17.387  8.764   1.00 25.55 ? 74  GLN A CG   1 
ATOM   608  C  CD   . GLN A 1 74  ? -21.945 18.115  8.030   1.00 25.58 ? 74  GLN A CD   1 
ATOM   609  O  OE1  . GLN A 1 74  ? -22.080 17.994  6.812   1.00 28.39 ? 74  GLN A OE1  1 
ATOM   610  N  NE2  . GLN A 1 74  ? -22.751 18.878  8.771   1.00 29.46 ? 74  GLN A NE2  1 
ATOM   611  N  N    A ASP A 1 75  ? -20.672 16.623  12.832  0.50 23.81 ? 75  ASP A N    1 
ATOM   612  N  N    B ASP A 1 75  ? -20.699 16.593  12.827  0.50 23.62 ? 75  ASP A N    1 
ATOM   613  C  CA   A ASP A 1 75  ? -21.213 15.667  13.772  0.50 24.04 ? 75  ASP A CA   1 
ATOM   614  C  CA   B ASP A 1 75  ? -21.165 15.639  13.844  0.50 23.72 ? 75  ASP A CA   1 
ATOM   615  C  C    A ASP A 1 75  ? -22.247 14.845  13.033  0.50 24.11 ? 75  ASP A C    1 
ATOM   616  C  C    B ASP A 1 75  ? -22.268 14.731  13.310  0.50 23.92 ? 75  ASP A C    1 
ATOM   617  O  O    A ASP A 1 75  ? -23.355 15.315  12.751  0.50 24.32 ? 75  ASP A O    1 
ATOM   618  O  O    B ASP A 1 75  ? -23.462 15.030  13.455  0.50 24.18 ? 75  ASP A O    1 
ATOM   619  C  CB   A ASP A 1 75  ? -21.839 16.365  14.986  0.50 24.59 ? 75  ASP A CB   1 
ATOM   620  C  CB   B ASP A 1 75  ? -21.664 16.373  15.099  0.50 24.02 ? 75  ASP A CB   1 
ATOM   621  C  CG   A ASP A 1 75  ? -22.415 15.382  15.996  0.50 24.71 ? 75  ASP A CG   1 
ATOM   622  C  CG   B ASP A 1 75  ? -20.789 16.133  16.327  0.50 23.62 ? 75  ASP A CG   1 
ATOM   623  O  OD1  A ASP A 1 75  ? -22.353 15.662  17.211  0.50 26.26 ? 75  ASP A OD1  1 
ATOM   624  O  OD1  B ASP A 1 75  ? -19.928 15.223  16.319  0.50 22.81 ? 75  ASP A OD1  1 
ATOM   625  O  OD2  A ASP A 1 75  ? -22.925 14.318  15.581  0.50 26.82 ? 75  ASP A OD2  1 
ATOM   626  O  OD2  B ASP A 1 75  ? -20.988 16.861  17.322  0.50 24.17 ? 75  ASP A OD2  1 
ATOM   627  N  N    . LYS A 1 76  ? -21.860 13.624  12.697  1.00 23.67 ? 76  LYS A N    1 
ATOM   628  C  CA   . LYS A 1 76  ? -22.787 12.670  12.112  1.00 23.82 ? 76  LYS A CA   1 
ATOM   629  C  C    . LYS A 1 76  ? -22.766 11.415  12.982  1.00 22.77 ? 76  LYS A C    1 
ATOM   630  O  O    . LYS A 1 76  ? -23.621 11.252  13.867  1.00 24.06 ? 76  LYS A O    1 
ATOM   631  C  CB   . LYS A 1 76  ? -22.423 12.377  10.648  1.00 23.98 ? 76  LYS A CB   1 
ATOM   632  C  CG   . LYS A 1 76  ? -22.707 13.539  9.672   1.00 24.77 ? 76  LYS A CG   1 
ATOM   633  C  CD   . LYS A 1 76  ? -22.156 13.236  8.274   1.00 25.37 ? 76  LYS A CD   1 
ATOM   634  C  CE   . LYS A 1 76  ? -22.330 14.417  7.304   1.00 26.58 ? 76  LYS A CE   1 
ATOM   635  N  NZ   . LYS A 1 76  ? -21.707 14.167  5.966   1.00 27.60 ? 76  LYS A NZ   1 
ATOM   636  N  N    . ALA A 1 77  ? -21.764 10.572  12.762  1.00 20.82 ? 77  ALA A N    1 
ATOM   637  C  CA   . ALA A 1 77  ? -21.643 9.268   13.422  1.00 18.58 ? 77  ALA A CA   1 
ATOM   638  C  C    . ALA A 1 77  ? -20.858 9.404   14.725  1.00 17.53 ? 77  ALA A C    1 
ATOM   639  O  O    . ALA A 1 77  ? -19.643 9.615   14.694  1.00 17.51 ? 77  ALA A O    1 
ATOM   640  C  CB   . ALA A 1 77  ? -20.949 8.304   12.491  1.00 18.67 ? 77  ALA A CB   1 
ATOM   641  N  N    . VAL A 1 78  ? -21.545 9.307   15.859  1.00 15.48 ? 78  VAL A N    1 
ATOM   642  C  CA   . VAL A 1 78  ? -20.881 9.534   17.152  1.00 14.18 ? 78  VAL A CA   1 
ATOM   643  C  C    . VAL A 1 78  ? -21.082 8.426   18.175  1.00 12.82 ? 78  VAL A C    1 
ATOM   644  O  O    . VAL A 1 78  ? -22.110 7.731   18.200  1.00 12.41 ? 78  VAL A O    1 
ATOM   645  C  CB   . VAL A 1 78  ? -21.297 10.865  17.798  1.00 15.23 ? 78  VAL A CB   1 
ATOM   646  C  CG1  . VAL A 1 78  ? -20.889 12.041  16.914  1.00 16.38 ? 78  VAL A CG1  1 
ATOM   647  C  CG2  . VAL A 1 78  ? -22.778 10.878  18.072  1.00 16.30 ? 78  VAL A CG2  1 
ATOM   648  N  N    . LEU A 1 79  ? -20.061 8.284   19.012  1.00 10.88 ? 79  LEU A N    1 
ATOM   649  C  CA   . LEU A 1 79  ? -20.073 7.384   20.133  1.00 10.16 ? 79  LEU A CA   1 
ATOM   650  C  C    . LEU A 1 79  ? -20.047 8.243   21.386  1.00 10.31 ? 79  LEU A C    1 
ATOM   651  O  O    . LEU A 1 79  ? -19.233 9.168   21.491  1.00 10.07 ? 79  LEU A O    1 
ATOM   652  C  CB   . LEU A 1 79  ? -18.835 6.474   20.060  1.00 9.82  ? 79  LEU A CB   1 
ATOM   653  C  CG   . LEU A 1 79  ? -18.674 5.436   21.152  1.00 9.71  ? 79  LEU A CG   1 
ATOM   654  C  CD1  . LEU A 1 79  ? -19.785 4.387   21.063  1.00 10.79 ? 79  LEU A CD1  1 
ATOM   655  C  CD2  . LEU A 1 79  ? -17.308 4.780   21.053  1.00 9.23  ? 79  LEU A CD2  1 
ATOM   656  N  N    . LYS A 1 80  ? -20.957 7.966   22.317  1.00 10.04 ? 80  LYS A N    1 
ATOM   657  C  CA   . LYS A 1 80  ? -20.955 8.642   23.617  1.00 11.17 ? 80  LYS A CA   1 
ATOM   658  C  C    . LYS A 1 80  ? -21.529 7.738   24.693  1.00 10.77 ? 80  LYS A C    1 
ATOM   659  O  O    . LYS A 1 80  ? -21.861 6.593   24.417  1.00 9.73  ? 80  LYS A O    1 
ATOM   660  C  CB   . LYS A 1 80  ? -21.704 9.971   23.557  1.00 12.83 ? 80  LYS A CB   1 
ATOM   661  C  CG   . LYS A 1 80  ? -23.218 9.860   23.392  1.00 15.24 ? 80  LYS A CG   1 
ATOM   662  C  CD   . LYS A 1 80  ? -23.830 11.253  23.281  1.00 20.08 ? 80  LYS A CD   1 
ATOM   663  C  CE   . LYS A 1 80  ? -23.586 11.851  21.911  1.00 23.88 ? 80  LYS A CE   1 
ATOM   664  N  NZ   . LYS A 1 80  ? -22.235 11.573  21.336  1.00 27.86 ? 80  LYS A NZ   1 
ATOM   665  N  N    . GLY A 1 81  ? -21.613 8.239   25.925  1.00 11.13 ? 81  GLY A N    1 
ATOM   666  C  CA   . GLY A 1 81  ? -22.122 7.432   27.018  1.00 11.95 ? 81  GLY A CA   1 
ATOM   667  C  C    . GLY A 1 81  ? -21.106 6.376   27.369  1.00 12.56 ? 81  GLY A C    1 
ATOM   668  O  O    . GLY A 1 81  ? -19.907 6.557   27.121  1.00 12.05 ? 81  GLY A O    1 
ATOM   669  N  N    . GLY A 1 82  ? -21.573 5.265   27.936  1.00 13.40 ? 82  GLY A N    1 
ATOM   670  C  CA   . GLY A 1 82  ? -20.644 4.260   28.454  1.00 13.73 ? 82  GLY A CA   1 
ATOM   671  C  C    . GLY A 1 82  ? -19.715 4.904   29.474  1.00 13.69 ? 82  GLY A C    1 
ATOM   672  O  O    . GLY A 1 82  ? -20.183 5.615   30.362  1.00 14.91 ? 82  GLY A O    1 
ATOM   673  N  N    . PRO A 1 83  ? -18.384 4.699   29.333  1.00 12.74 ? 83  PRO A N    1 
ATOM   674  C  CA   . PRO A 1 83  ? -17.433 5.313   30.254  1.00 12.87 ? 83  PRO A CA   1 
ATOM   675  C  C    . PRO A 1 83  ? -17.029 6.731   29.839  1.00 13.08 ? 83  PRO A C    1 
ATOM   676  O  O    . PRO A 1 83  ? -16.242 7.385   30.537  1.00 13.95 ? 83  PRO A O    1 
ATOM   677  C  CB   . PRO A 1 83  ? -16.211 4.397   30.127  1.00 12.87 ? 83  PRO A CB   1 
ATOM   678  C  CG   . PRO A 1 83  ? -16.248 3.964   28.694  1.00 12.10 ? 83  PRO A CG   1 
ATOM   679  C  CD   . PRO A 1 83  ? -17.702 3.867   28.313  1.00 12.25 ? 83  PRO A CD   1 
ATOM   680  N  N    . LEU A 1 84  ? -17.565 7.200   28.712  1.00 12.85 ? 84  LEU A N    1 
ATOM   681  C  CA   . LEU A 1 84  ? -17.080 8.426   28.086  1.00 12.83 ? 84  LEU A CA   1 
ATOM   682  C  C    . LEU A 1 84  ? -17.737 9.691   28.617  1.00 14.27 ? 84  LEU A C    1 
ATOM   683  O  O    . LEU A 1 84  ? -18.933 9.708   28.933  1.00 14.42 ? 84  LEU A O    1 
ATOM   684  C  CB   . LEU A 1 84  ? -17.258 8.369   26.579  1.00 12.30 ? 84  LEU A CB   1 
ATOM   685  C  CG   . LEU A 1 84  ? -16.713 7.140   25.836  1.00 10.01 ? 84  LEU A CG   1 
ATOM   686  C  CD1  . LEU A 1 84  ? -17.219 7.115   24.392  1.00 8.96  ? 84  LEU A CD1  1 
ATOM   687  C  CD2  . LEU A 1 84  ? -15.179 7.128   25.903  1.00 9.91  ? 84  LEU A CD2  1 
ATOM   688  N  N    . ASP A 1 85  ? -16.924 10.737  28.705  1.00 15.26 ? 85  ASP A N    1 
ATOM   689  C  CA   . ASP A 1 85  ? -17.397 12.099  28.902  1.00 17.35 ? 85  ASP A CA   1 
ATOM   690  C  C    . ASP A 1 85  ? -17.342 12.797  27.550  1.00 17.29 ? 85  ASP A C    1 
ATOM   691  O  O    . ASP A 1 85  ? -16.324 12.750  26.853  1.00 18.34 ? 85  ASP A O    1 
ATOM   692  C  CB   . ASP A 1 85  ? -16.500 12.823  29.915  1.00 18.31 ? 85  ASP A CB   1 
ATOM   693  C  CG   . ASP A 1 85  ? -16.645 12.269  31.319  1.00 21.70 ? 85  ASP A CG   1 
ATOM   694  O  OD1  . ASP A 1 85  ? -17.775 11.870  31.686  1.00 25.72 ? 85  ASP A OD1  1 
ATOM   695  O  OD2  . ASP A 1 85  ? -15.635 12.235  32.065  1.00 26.52 ? 85  ASP A OD2  1 
ATOM   696  N  N    . GLY A 1 86  ? -18.439 13.422  27.145  1.00 17.26 ? 86  GLY A N    1 
ATOM   697  C  CA   . GLY A 1 86  ? -18.437 14.138  25.872  1.00 16.06 ? 86  GLY A CA   1 
ATOM   698  C  C    . GLY A 1 86  ? -18.719 13.259  24.655  1.00 15.20 ? 86  GLY A C    1 
ATOM   699  O  O    . GLY A 1 86  ? -19.280 12.167  24.778  1.00 16.09 ? 86  GLY A O    1 
ATOM   700  N  N    A THR A 1 87  ? -18.318 13.738  23.483  0.50 14.39 ? 87  THR A N    1 
ATOM   701  N  N    B THR A 1 87  ? -18.301 13.725  23.484  0.50 14.38 ? 87  THR A N    1 
ATOM   702  C  CA   A THR A 1 87  ? -18.728 13.132  22.218  0.50 13.45 ? 87  THR A CA   1 
ATOM   703  C  CA   B THR A 1 87  ? -18.746 13.131  22.223  0.50 13.42 ? 87  THR A CA   1 
ATOM   704  C  C    A THR A 1 87  ? -17.524 12.767  21.355  0.50 12.41 ? 87  THR A C    1 
ATOM   705  C  C    B THR A 1 87  ? -17.572 12.794  21.297  0.50 12.40 ? 87  THR A C    1 
ATOM   706  O  O    A THR A 1 87  ? -16.585 13.555  21.212  0.50 11.42 ? 87  THR A O    1 
ATOM   707  O  O    B THR A 1 87  ? -16.695 13.628  21.056  0.50 11.49 ? 87  THR A O    1 
ATOM   708  C  CB   A THR A 1 87  ? -19.701 14.069  21.453  0.50 14.18 ? 87  THR A CB   1 
ATOM   709  C  CB   B THR A 1 87  ? -19.754 14.062  21.500  0.50 14.17 ? 87  THR A CB   1 
ATOM   710  O  OG1  A THR A 1 87  ? -20.996 13.997  22.065  0.50 15.54 ? 87  THR A OG1  1 
ATOM   711  O  OG1  B THR A 1 87  ? -19.114 15.291  21.158  0.50 14.53 ? 87  THR A OG1  1 
ATOM   712  C  CG2  A THR A 1 87  ? -19.826 13.676  19.985  0.50 13.92 ? 87  THR A CG2  1 
ATOM   713  C  CG2  B THR A 1 87  ? -20.944 14.381  22.406  0.50 14.68 ? 87  THR A CG2  1 
ATOM   714  N  N    . TYR A 1 88  ? -17.559 11.560  20.792  1.00 10.90 ? 88  TYR A N    1 
ATOM   715  C  CA   . TYR A 1 88  ? -16.466 11.077  19.951  1.00 9.95  ? 88  TYR A CA   1 
ATOM   716  C  C    . TYR A 1 88  ? -16.964 10.761  18.547  1.00 9.11  ? 88  TYR A C    1 
ATOM   717  O  O    . TYR A 1 88  ? -17.953 10.040  18.388  1.00 10.15 ? 88  TYR A O    1 
ATOM   718  C  CB   . TYR A 1 88  ? -15.831 9.828   20.562  1.00 8.56  ? 88  TYR A CB   1 
ATOM   719  C  CG   . TYR A 1 88  ? -15.077 10.048  21.870  1.00 8.46  ? 88  TYR A CG   1 
ATOM   720  C  CD1  . TYR A 1 88  ? -15.754 10.361  23.057  1.00 7.29  ? 88  TYR A CD1  1 
ATOM   721  C  CD2  . TYR A 1 88  ? -13.692 9.913   21.920  1.00 7.28  ? 88  TYR A CD2  1 
ATOM   722  C  CE1  . TYR A 1 88  ? -15.054 10.552  24.258  1.00 7.67  ? 88  TYR A CE1  1 
ATOM   723  C  CE2  . TYR A 1 88  ? -12.984 10.085  23.113  1.00 7.28  ? 88  TYR A CE2  1 
ATOM   724  C  CZ   . TYR A 1 88  ? -13.666 10.397  24.273  1.00 8.05  ? 88  TYR A CZ   1 
ATOM   725  O  OH   . TYR A 1 88  ? -12.959 10.563  25.440  1.00 7.46  ? 88  TYR A OH   1 
ATOM   726  N  N    . ARG A 1 89  ? -16.263 11.270  17.540  1.00 8.22  ? 89  ARG A N    1 
ATOM   727  C  CA   . ARG A 1 89  ? -16.692 11.176  16.145  1.00 8.21  ? 89  ARG A CA   1 
ATOM   728  C  C    . ARG A 1 89  ? -15.997 10.030  15.412  1.00 7.64  ? 89  ARG A C    1 
ATOM   729  O  O    . ARG A 1 89  ? -14.774 9.903   15.494  1.00 6.46  ? 89  ARG A O    1 
ATOM   730  C  CB   . ARG A 1 89  ? -16.372 12.503  15.442  1.00 9.54  ? 89  ARG A CB   1 
ATOM   731  C  CG   . ARG A 1 89  ? -17.136 12.752  14.192  1.00 12.88 ? 89  ARG A CG   1 
ATOM   732  C  CD   . ARG A 1 89  ? -16.912 14.193  13.716  1.00 13.32 ? 89  ARG A CD   1 
ATOM   733  N  NE   . ARG A 1 89  ? -17.603 15.184  14.541  1.00 15.78 ? 89  ARG A NE   1 
ATOM   734  C  CZ   . ARG A 1 89  ? -17.560 16.495  14.325  1.00 17.53 ? 89  ARG A CZ   1 
ATOM   735  N  NH1  . ARG A 1 89  ? -16.867 16.979  13.302  1.00 17.18 ? 89  ARG A NH1  1 
ATOM   736  N  NH2  . ARG A 1 89  ? -18.214 17.325  15.129  1.00 17.44 ? 89  ARG A NH2  1 
ATOM   737  N  N    . LEU A 1 90  ? -16.767 9.205   14.695  1.00 6.60  ? 90  LEU A N    1 
ATOM   738  C  CA   . LEU A 1 90  ? -16.195 8.104   13.921  1.00 6.40  ? 90  LEU A CA   1 
ATOM   739  C  C    . LEU A 1 90  ? -15.360 8.625   12.750  1.00 6.59  ? 90  LEU A C    1 
ATOM   740  O  O    . LEU A 1 90  ? -15.856 9.423   11.930  1.00 7.24  ? 90  LEU A O    1 
ATOM   741  C  CB   . LEU A 1 90  ? -17.313 7.200   13.396  1.00 6.76  ? 90  LEU A CB   1 
ATOM   742  C  CG   . LEU A 1 90  ? -16.909 6.037   12.481  1.00 7.17  ? 90  LEU A CG   1 
ATOM   743  C  CD1  . LEU A 1 90  ? -16.057 5.009   13.249  1.00 7.93  ? 90  LEU A CD1  1 
ATOM   744  C  CD2  . LEU A 1 90  ? -18.156 5.371   11.902  1.00 7.46  ? 90  LEU A CD2  1 
ATOM   745  N  N    . ILE A 1 91  ? -14.121 8.147   12.649  1.00 5.88  ? 91  ILE A N    1 
ATOM   746  C  CA   . ILE A 1 91  ? -13.221 8.531   11.531  1.00 6.60  ? 91  ILE A CA   1 
ATOM   747  C  C    . ILE A 1 91  ? -12.891 7.368   10.584  1.00 6.13  ? 91  ILE A C    1 
ATOM   748  O  O    . ILE A 1 91  ? -12.770 7.561   9.371   1.00 6.68  ? 91  ILE A O    1 
ATOM   749  C  CB   . ILE A 1 91  ? -11.934 9.256   12.035  1.00 6.64  ? 91  ILE A CB   1 
ATOM   750  C  CG1  . ILE A 1 91  ? -10.996 9.598   10.860  1.00 7.51  ? 91  ILE A CG1  1 
ATOM   751  C  CG2  . ILE A 1 91  ? -11.208 8.420   13.095  1.00 6.96  ? 91  ILE A CG2  1 
ATOM   752  C  CD1  . ILE A 1 91  ? -9.855  10.538  11.241  1.00 8.88  ? 91  ILE A CD1  1 
ATOM   753  N  N    . GLN A 1 92  ? -12.745 6.157   11.133  1.00 5.47  ? 92  GLN A N    1 
ATOM   754  C  CA   . GLN A 1 92  ? -12.446 4.996   10.288  1.00 5.27  ? 92  GLN A CA   1 
ATOM   755  C  C    . GLN A 1 92  ? -12.716 3.740   11.083  1.00 5.11  ? 92  GLN A C    1 
ATOM   756  O  O    . GLN A 1 92  ? -12.744 3.781   12.311  1.00 5.15  ? 92  GLN A O    1 
ATOM   757  C  CB   . GLN A 1 92  ? -10.975 5.001   9.795   1.00 5.61  ? 92  GLN A CB   1 
ATOM   758  C  CG   . GLN A 1 92  ? -9.905  5.130   10.912  1.00 6.97  ? 92  GLN A CG   1 
ATOM   759  C  CD   . GLN A 1 92  ? -9.175  3.821   11.223  1.00 9.00  ? 92  GLN A CD   1 
ATOM   760  O  OE1  . GLN A 1 92  ? -9.742  2.745   11.117  1.00 6.92  ? 92  GLN A OE1  1 
ATOM   761  N  NE2  . GLN A 1 92  ? -7.902  3.927   11.599  1.00 10.06 ? 92  GLN A NE2  1 
ATOM   762  N  N    . PHE A 1 93  ? -12.922 2.641   10.374  1.00 4.71  ? 93  PHE A N    1 
ATOM   763  C  CA   . PHE A 1 93  ? -12.761 1.314   10.976  1.00 4.72  ? 93  PHE A CA   1 
ATOM   764  C  C    . PHE A 1 93  ? -11.808 0.417   10.191  1.00 5.00  ? 93  PHE A C    1 
ATOM   765  O  O    . PHE A 1 93  ? -11.546 0.625   9.002   1.00 4.37  ? 93  PHE A O    1 
ATOM   766  C  CB   . PHE A 1 93  ? -14.099 0.612   11.248  1.00 4.57  ? 93  PHE A CB   1 
ATOM   767  C  CG   . PHE A 1 93  ? -14.826 0.115   10.008  1.00 5.46  ? 93  PHE A CG   1 
ATOM   768  C  CD1  . PHE A 1 93  ? -14.413 -1.036  9.341   1.00 6.66  ? 93  PHE A CD1  1 
ATOM   769  C  CD2  . PHE A 1 93  ? -15.976 0.772   9.565   1.00 5.99  ? 93  PHE A CD2  1 
ATOM   770  C  CE1  . PHE A 1 93  ? -15.101 -1.513  8.217   1.00 7.16  ? 93  PHE A CE1  1 
ATOM   771  C  CE2  . PHE A 1 93  ? -16.684 0.303   8.436   1.00 6.40  ? 93  PHE A CE2  1 
ATOM   772  C  CZ   . PHE A 1 93  ? -16.245 -0.843  7.771   1.00 7.38  ? 93  PHE A CZ   1 
ATOM   773  N  N    . HIS A 1 94  ? -11.268 -0.579  10.886  1.00 4.06  ? 94  HIS A N    1 
ATOM   774  C  CA   . HIS A 1 94  ? -10.401 -1.562  10.276  1.00 3.79  ? 94  HIS A CA   1 
ATOM   775  C  C    . HIS A 1 94  ? -10.474 -2.839  11.108  1.00 3.87  ? 94  HIS A C    1 
ATOM   776  O  O    . HIS A 1 94  ? -11.107 -2.868  12.174  1.00 4.36  ? 94  HIS A O    1 
ATOM   777  C  CB   . HIS A 1 94  ? -8.951  -1.071  10.268  1.00 3.84  ? 94  HIS A CB   1 
ATOM   778  C  CG   . HIS A 1 94  ? -8.438  -0.774  11.639  1.00 4.19  ? 94  HIS A CG   1 
ATOM   779  N  ND1  . HIS A 1 94  ? -8.627  0.448   12.245  1.00 4.44  ? 94  HIS A ND1  1 
ATOM   780  C  CD2  . HIS A 1 94  ? -7.786  -1.548  12.537  1.00 3.90  ? 94  HIS A CD2  1 
ATOM   781  C  CE1  . HIS A 1 94  ? -8.098  0.418   13.458  1.00 4.13  ? 94  HIS A CE1  1 
ATOM   782  N  NE2  . HIS A 1 94  ? -7.605  -0.790  13.668  1.00 4.49  ? 94  HIS A NE2  1 
ATOM   783  N  N    . PHE A 1 95  ? -9.785  -3.873  10.635  1.00 3.66  ? 95  PHE A N    1 
ATOM   784  C  CA   . PHE A 1 95  ? -9.729  -5.164  11.340  1.00 4.37  ? 95  PHE A CA   1 
ATOM   785  C  C    . PHE A 1 95  ? -8.279  -5.609  11.559  1.00 4.17  ? 95  PHE A C    1 
ATOM   786  O  O    . PHE A 1 95  ? -7.349  -5.131  10.904  1.00 4.40  ? 95  PHE A O    1 
ATOM   787  C  CB   . PHE A 1 95  ? -10.417 -6.271  10.518  1.00 4.36  ? 95  PHE A CB   1 
ATOM   788  C  CG   . PHE A 1 95  ? -11.853 -5.999  10.195  1.00 3.98  ? 95  PHE A CG   1 
ATOM   789  C  CD1  . PHE A 1 95  ? -12.193 -5.144  9.142   1.00 5.65  ? 95  PHE A CD1  1 
ATOM   790  C  CD2  . PHE A 1 95  ? -12.879 -6.645  10.903  1.00 6.35  ? 95  PHE A CD2  1 
ATOM   791  C  CE1  . PHE A 1 95  ? -13.542 -4.904  8.816   1.00 4.72  ? 95  PHE A CE1  1 
ATOM   792  C  CE2  . PHE A 1 95  ? -14.225 -6.418  10.580  1.00 5.83  ? 95  PHE A CE2  1 
ATOM   793  C  CZ   . PHE A 1 95  ? -14.547 -5.553  9.528   1.00 5.27  ? 95  PHE A CZ   1 
ATOM   794  N  N    . HIS A 1 96  ? -8.127  -6.568  12.471  1.00 4.61  ? 96  HIS A N    1 
ATOM   795  C  CA   . HIS A 1 96  ? -6.899  -7.346  12.660  1.00 4.05  ? 96  HIS A CA   1 
ATOM   796  C  C    . HIS A 1 96  ? -7.319  -8.800  12.555  1.00 4.35  ? 96  HIS A C    1 
ATOM   797  O  O    . HIS A 1 96  ? -8.376  -9.181  13.084  1.00 4.79  ? 96  HIS A O    1 
ATOM   798  C  CB   . HIS A 1 96  ? -6.296  -7.082  14.032  1.00 4.74  ? 96  HIS A CB   1 
ATOM   799  C  CG   . HIS A 1 96  ? -6.011  -5.636  14.288  1.00 4.76  ? 96  HIS A CG   1 
ATOM   800  N  ND1  . HIS A 1 96  ? -4.757  -5.089  14.118  1.00 4.61  ? 96  HIS A ND1  1 
ATOM   801  C  CD2  . HIS A 1 96  ? -6.823  -4.622  14.682  1.00 4.46  ? 96  HIS A CD2  1 
ATOM   802  C  CE1  . HIS A 1 96  ? -4.804  -3.798  14.427  1.00 5.29  ? 96  HIS A CE1  1 
ATOM   803  N  NE2  . HIS A 1 96  ? -6.047  -3.488  14.750  1.00 3.63  ? 96  HIS A NE2  1 
ATOM   804  N  N    . TRP A 1 97  ? -6.539  -9.610  11.846  1.00 4.43  ? 97  TRP A N    1 
ATOM   805  C  CA   . TRP A 1 97  ? -6.937  -11.016 11.674  1.00 5.34  ? 97  TRP A CA   1 
ATOM   806  C  C    . TRP A 1 97  ? -5.759  -11.957 11.556  1.00 5.06  ? 97  TRP A C    1 
ATOM   807  O  O    . TRP A 1 97  ? -4.596  -11.522 11.477  1.00 5.39  ? 97  TRP A O    1 
ATOM   808  C  CB   . TRP A 1 97  ? -7.865  -11.169 10.467  1.00 5.11  ? 97  TRP A CB   1 
ATOM   809  C  CG   . TRP A 1 97  ? -7.243  -10.765 9.160   1.00 5.00  ? 97  TRP A CG   1 
ATOM   810  C  CD1  . TRP A 1 97  ? -6.612  -11.595 8.282   1.00 5.07  ? 97  TRP A CD1  1 
ATOM   811  C  CD2  . TRP A 1 97  ? -7.190  -9.445  8.585   1.00 5.30  ? 97  TRP A CD2  1 
ATOM   812  N  NE1  . TRP A 1 97  ? -6.179  -10.881 7.183   1.00 5.77  ? 97  TRP A NE1  1 
ATOM   813  C  CE2  . TRP A 1 97  ? -6.518  -9.564  7.342   1.00 5.23  ? 97  TRP A CE2  1 
ATOM   814  C  CE3  . TRP A 1 97  ? -7.647  -8.178  8.997   1.00 4.79  ? 97  TRP A CE3  1 
ATOM   815  C  CZ2  . TRP A 1 97  ? -6.285  -8.469  6.503   1.00 6.57  ? 97  TRP A CZ2  1 
ATOM   816  C  CZ3  . TRP A 1 97  ? -7.406  -7.071  8.156   1.00 5.73  ? 97  TRP A CZ3  1 
ATOM   817  C  CH2  . TRP A 1 97  ? -6.734  -7.237  6.920   1.00 4.67  ? 97  TRP A CH2  1 
ATOM   818  N  N    . GLY A 1 98  ? -6.069  -13.253 11.549  1.00 4.97  ? 98  GLY A N    1 
ATOM   819  C  CA   . GLY A 1 98  ? -5.018  -14.269 11.590  1.00 5.26  ? 98  GLY A CA   1 
ATOM   820  C  C    . GLY A 1 98  ? -4.792  -14.997 10.283  1.00 6.07  ? 98  GLY A C    1 
ATOM   821  O  O    . GLY A 1 98  ? -5.520  -14.794 9.305   1.00 6.55  ? 98  GLY A O    1 
ATOM   822  N  N    . SER A 1 99  ? -3.767  -15.843 10.278  1.00 6.25  ? 99  SER A N    1 
ATOM   823  C  CA   . SER A 1 99  ? -3.520  -16.772 9.161   1.00 7.54  ? 99  SER A CA   1 
ATOM   824  C  C    . SER A 1 99  ? -4.420  -18.006 9.251   1.00 8.33  ? 99  SER A C    1 
ATOM   825  O  O    . SER A 1 99  ? -4.570  -18.747 8.269   1.00 9.01  ? 99  SER A O    1 
ATOM   826  C  CB   . SER A 1 99  ? -2.049  -17.214 9.153   1.00 7.65  ? 99  SER A CB   1 
ATOM   827  O  OG   . SER A 1 99  ? -1.642  -17.716 10.418  1.00 8.33  ? 99  SER A OG   1 
ATOM   828  N  N    . LEU A 1 100 ? -5.007  -18.216 10.432  1.00 8.28  ? 100 LEU A N    1 
ATOM   829  C  CA   . LEU A 1 100 ? -5.831  -19.378 10.749  1.00 9.31  ? 100 LEU A CA   1 
ATOM   830  C  C    . LEU A 1 100 ? -6.963  -18.899 11.647  1.00 9.10  ? 100 LEU A C    1 
ATOM   831  O  O    . LEU A 1 100 ? -6.810  -17.898 12.337  1.00 8.81  ? 100 LEU A O    1 
ATOM   832  C  CB   . LEU A 1 100 ? -5.006  -20.419 11.520  1.00 10.19 ? 100 LEU A CB   1 
ATOM   833  C  CG   . LEU A 1 100 ? -3.681  -20.839 10.882  1.00 13.44 ? 100 LEU A CG   1 
ATOM   834  C  CD1  . LEU A 1 100 ? -2.682  -21.283 11.923  1.00 16.70 ? 100 LEU A CD1  1 
ATOM   835  C  CD2  . LEU A 1 100 ? -4.000  -21.956 9.917   1.00 14.62 ? 100 LEU A CD2  1 
ATOM   836  N  N    . ASP A 1 101 ? -8.064  -19.646 11.707  1.00 8.74  ? 101 ASP A N    1 
ATOM   837  C  CA   . ASP A 1 101 ? -9.203  -19.210 12.534  1.00 9.60  ? 101 ASP A CA   1 
ATOM   838  C  C    . ASP A 1 101 ? -8.877  -19.115 14.026  1.00 9.31  ? 101 ASP A C    1 
ATOM   839  O  O    . ASP A 1 101 ? -9.521  -18.352 14.747  1.00 9.32  ? 101 ASP A O    1 
ATOM   840  C  CB   . ASP A 1 101 ? -10.416 -20.126 12.355  1.00 9.80  ? 101 ASP A CB   1 
ATOM   841  C  CG   . ASP A 1 101 ? -11.013 -20.091 10.942  1.00 12.60 ? 101 ASP A CG   1 
ATOM   842  O  OD1  . ASP A 1 101 ? -10.585 -19.302 10.068  1.00 13.35 ? 101 ASP A OD1  1 
ATOM   843  O  OD2  . ASP A 1 101 ? -11.951 -20.887 10.710  1.00 16.17 ? 101 ASP A OD2  1 
ATOM   844  N  N    . GLY A 1 102 ? -7.882  -19.884 14.489  1.00 9.32  ? 102 GLY A N    1 
ATOM   845  C  CA   . GLY A 1 102 ? -7.518  -19.912 15.923  1.00 8.15  ? 102 GLY A CA   1 
ATOM   846  C  C    . GLY A 1 102 ? -6.740  -18.723 16.478  1.00 8.12  ? 102 GLY A C    1 
ATOM   847  O  O    . GLY A 1 102 ? -6.341  -18.710 17.653  1.00 7.93  ? 102 GLY A O    1 
ATOM   848  N  N    . GLN A 1 103 ? -6.509  -17.716 15.638  1.00 6.98  ? 103 GLN A N    1 
ATOM   849  C  CA   . GLN A 1 103 ? -5.828  -16.510 16.104  1.00 7.35  ? 103 GLN A CA   1 
ATOM   850  C  C    . GLN A 1 103 ? -6.188  -15.339 15.216  1.00 6.49  ? 103 GLN A C    1 
ATOM   851  O  O    . GLN A 1 103 ? -6.759  -15.523 14.146  1.00 5.97  ? 103 GLN A O    1 
ATOM   852  C  CB   . GLN A 1 103 ? -4.314  -16.704 16.151  1.00 7.41  ? 103 GLN A CB   1 
ATOM   853  C  CG   . GLN A 1 103 ? -3.648  -16.936 14.793  1.00 8.96  ? 103 GLN A CG   1 
ATOM   854  C  CD   . GLN A 1 103 ? -2.187  -17.346 14.948  1.00 10.65 ? 103 GLN A CD   1 
ATOM   855  O  OE1  . GLN A 1 103 ? -1.799  -17.934 15.968  1.00 17.29 ? 103 GLN A OE1  1 
ATOM   856  N  NE2  . GLN A 1 103 ? -1.363  -17.016 13.958  1.00 11.27 ? 103 GLN A NE2  1 
ATOM   857  N  N    . GLY A 1 104 ? -5.884  -14.138 15.693  1.00 5.50  ? 104 GLY A N    1 
ATOM   858  C  CA   . GLY A 1 104 ? -6.194  -12.956 14.910  1.00 5.42  ? 104 GLY A CA   1 
ATOM   859  C  C    . GLY A 1 104 ? -6.647  -11.779 15.731  1.00 5.73  ? 104 GLY A C    1 
ATOM   860  O  O    . GLY A 1 104 ? -6.393  -10.640 15.353  1.00 5.96  ? 104 GLY A O    1 
ATOM   861  N  N    . SER A 1 105 ? -7.345  -12.025 16.833  1.00 5.17  ? 105 SER A N    1 
ATOM   862  C  CA   . SER A 1 105 ? -7.752  -10.891 17.673  1.00 5.17  ? 105 SER A CA   1 
ATOM   863  C  C    . SER A 1 105 ? -6.554  -10.343 18.449  1.00 4.19  ? 105 SER A C    1 
ATOM   864  O  O    . SER A 1 105 ? -5.533  -11.029 18.622  1.00 4.63  ? 105 SER A O    1 
ATOM   865  C  CB   . SER A 1 105 ? -8.894  -11.240 18.622  1.00 4.19  ? 105 SER A CB   1 
ATOM   866  O  OG   . SER A 1 105 ? -8.515  -12.189 19.614  1.00 4.43  ? 105 SER A OG   1 
ATOM   867  N  N    . GLU A 1 106 ? -6.690  -9.084  18.852  1.00 4.73  ? 106 GLU A N    1 
ATOM   868  C  CA   . GLU A 1 106 ? -5.682  -8.386  19.647  1.00 4.08  ? 106 GLU A CA   1 
ATOM   869  C  C    . GLU A 1 106 ? -6.024  -8.557  21.133  1.00 4.14  ? 106 GLU A C    1 
ATOM   870  O  O    . GLU A 1 106 ? -5.246  -9.104  21.897  1.00 3.76  ? 106 GLU A O    1 
ATOM   871  C  CB   . GLU A 1 106 ? -5.609  -6.894  19.252  1.00 3.90  ? 106 GLU A CB   1 
ATOM   872  C  CG   . GLU A 1 106 ? -5.211  -6.731  17.780  1.00 4.94  ? 106 GLU A CG   1 
ATOM   873  C  CD   . GLU A 1 106 ? -4.502  -5.450  17.479  1.00 6.23  ? 106 GLU A CD   1 
ATOM   874  O  OE1  . GLU A 1 106 ? -5.074  -4.361  17.697  1.00 5.56  ? 106 GLU A OE1  1 
ATOM   875  O  OE2  . GLU A 1 106 ? -3.365  -5.543  17.012  1.00 6.76  ? 106 GLU A OE2  1 
ATOM   876  N  N    . HIS A 1 107 ? -7.214  -8.118  21.541  1.00 4.28  ? 107 HIS A N    1 
ATOM   877  C  CA   . HIS A 1 107 ? -7.681  -8.456  22.868  1.00 3.74  ? 107 HIS A CA   1 
ATOM   878  C  C    . HIS A 1 107 ? -7.962  -9.942  22.924  1.00 4.43  ? 107 HIS A C    1 
ATOM   879  O  O    . HIS A 1 107 ? -8.267  -10.555 21.901  1.00 5.11  ? 107 HIS A O    1 
ATOM   880  C  CB   . HIS A 1 107 ? -8.929  -7.638  23.218  1.00 4.10  ? 107 HIS A CB   1 
ATOM   881  C  CG   . HIS A 1 107 ? -8.615  -6.184  23.392  1.00 3.17  ? 107 HIS A CG   1 
ATOM   882  N  ND1  . HIS A 1 107 ? -8.683  -5.286  22.348  1.00 4.04  ? 107 HIS A ND1  1 
ATOM   883  C  CD2  . HIS A 1 107 ? -8.118  -5.498  24.450  1.00 4.64  ? 107 HIS A CD2  1 
ATOM   884  C  CE1  . HIS A 1 107 ? -8.284  -4.096  22.771  1.00 4.43  ? 107 HIS A CE1  1 
ATOM   885  N  NE2  . HIS A 1 107 ? -7.946  -4.194  24.046  1.00 3.84  ? 107 HIS A NE2  1 
ATOM   886  N  N    . THR A 1 108 ? -7.805  -10.512 24.105  1.00 4.77  ? 108 THR A N    1 
ATOM   887  C  CA   . THR A 1 108 ? -8.180  -11.909 24.331  1.00 4.64  ? 108 THR A CA   1 
ATOM   888  C  C    . THR A 1 108 ? -9.117  -11.931 25.529  1.00 5.35  ? 108 THR A C    1 
ATOM   889  O  O    . THR A 1 108 ? -9.166  -10.957 26.291  1.00 5.38  ? 108 THR A O    1 
ATOM   890  C  CB   . THR A 1 108 ? -6.955  -12.802 24.552  1.00 4.18  ? 108 THR A CB   1 
ATOM   891  O  OG1  . THR A 1 108 ? -6.125  -12.278 25.607  1.00 5.94  ? 108 THR A OG1  1 
ATOM   892  C  CG2  . THR A 1 108 ? -6.122  -12.896 23.269  1.00 5.15  ? 108 THR A CG2  1 
ATOM   893  N  N    . VAL A 1 109 ? -9.861  -13.026 25.693  1.00 4.94  ? 109 VAL A N    1 
ATOM   894  C  CA   . VAL A 1 109 ? -10.857 -13.120 26.782  1.00 5.63  ? 109 VAL A CA   1 
ATOM   895  C  C    . VAL A 1 109 ? -10.555 -14.418 27.519  1.00 6.27  ? 109 VAL A C    1 
ATOM   896  O  O    . VAL A 1 109 ? -10.742 -15.489 26.957  1.00 5.65  ? 109 VAL A O    1 
ATOM   897  C  CB   . VAL A 1 109 ? -12.301 -13.160 26.218  1.00 6.78  ? 109 VAL A CB   1 
ATOM   898  C  CG1  . VAL A 1 109 ? -13.332 -13.329 27.318  1.00 7.01  ? 109 VAL A CG1  1 
ATOM   899  C  CG2  . VAL A 1 109 ? -12.622 -11.879 25.462  1.00 7.84  ? 109 VAL A CG2  1 
ATOM   900  N  N    . ASP A 1 110 ? -10.073 -14.314 28.753  1.00 6.12  ? 110 ASP A N    1 
ATOM   901  C  CA   . ASP A 1 110 ? -9.563  -15.488 29.470  1.00 7.26  ? 110 ASP A CA   1 
ATOM   902  C  C    . ASP A 1 110 ? -8.611  -16.307 28.584  1.00 6.86  ? 110 ASP A C    1 
ATOM   903  O  O    . ASP A 1 110 ? -8.690  -17.560 28.529  1.00 7.26  ? 110 ASP A O    1 
ATOM   904  C  CB   . ASP A 1 110 ? -10.730 -16.339 29.954  1.00 7.56  ? 110 ASP A CB   1 
ATOM   905  C  CG   . ASP A 1 110 ? -11.557 -15.629 31.017  1.00 8.66  ? 110 ASP A CG   1 
ATOM   906  O  OD1  . ASP A 1 110 ? -11.006 -14.727 31.691  1.00 10.83 ? 110 ASP A OD1  1 
ATOM   907  O  OD2  . ASP A 1 110 ? -12.739 -15.997 31.180  1.00 12.48 ? 110 ASP A OD2  1 
ATOM   908  N  N    . LYS A 1 111 ? -7.722  -15.577 27.902  1.00 6.35  ? 111 LYS A N    1 
ATOM   909  C  CA   . LYS A 1 111 ? -6.680  -16.098 26.977  1.00 6.64  ? 111 LYS A CA   1 
ATOM   910  C  C    . LYS A 1 111 ? -7.213  -16.625 25.624  1.00 6.63  ? 111 LYS A C    1 
ATOM   911  O  O    . LYS A 1 111 ? -6.426  -17.004 24.733  1.00 7.52  ? 111 LYS A O    1 
ATOM   912  C  CB   . LYS A 1 111 ? -5.742  -17.107 27.678  1.00 7.80  ? 111 LYS A CB   1 
ATOM   913  C  CG   . LYS A 1 111 ? -4.977  -16.525 28.885  1.00 8.65  ? 111 LYS A CG   1 
ATOM   914  C  CD   . LYS A 1 111 ? -4.106  -15.323 28.509  1.00 12.30 ? 111 LYS A CD   1 
ATOM   915  C  CE   . LYS A 1 111 ? -3.374  -14.778 29.730  1.00 13.10 ? 111 LYS A CE   1 
ATOM   916  N  NZ   . LYS A 1 111 ? -2.206  -15.625 30.094  1.00 15.76 ? 111 LYS A NZ   1 
ATOM   917  N  N    . LYS A 1 112 ? -8.535  -16.640 25.455  1.00 5.42  ? 112 LYS A N    1 
ATOM   918  C  CA   . LYS A 1 112 ? -9.125  -17.026 24.171  1.00 6.79  ? 112 LYS A CA   1 
ATOM   919  C  C    . LYS A 1 112 ? -8.814  -15.994 23.083  1.00 6.82  ? 112 LYS A C    1 
ATOM   920  O  O    . LYS A 1 112 ? -9.072  -14.794 23.270  1.00 6.54  ? 112 LYS A O    1 
ATOM   921  C  CB   . LYS A 1 112 ? -10.644 -17.172 24.294  1.00 6.69  ? 112 LYS A CB   1 
ATOM   922  C  CG   . LYS A 1 112 ? -11.337 -17.477 22.961  1.00 7.94  ? 112 LYS A CG   1 
ATOM   923  C  CD   . LYS A 1 112 ? -12.858 -17.423 23.108  1.00 8.67  ? 112 LYS A CD   1 
ATOM   924  C  CE   . LYS A 1 112 ? -13.531 -17.659 21.756  1.00 11.50 ? 112 LYS A CE   1 
ATOM   925  N  NZ   . LYS A 1 112 ? -13.350 -19.054 21.244  1.00 10.23 ? 112 LYS A NZ   1 
ATOM   926  N  N    . LYS A 1 113 ? -8.290  -16.470 21.948  1.00 6.97  ? 113 LYS A N    1 
ATOM   927  C  CA   . LYS A 1 113 ? -8.117  -15.624 20.753  1.00 7.30  ? 113 LYS A CA   1 
ATOM   928  C  C    . LYS A 1 113 ? -9.270  -15.844 19.763  1.00 7.23  ? 113 LYS A C    1 
ATOM   929  O  O    . LYS A 1 113 ? -9.645  -16.991 19.467  1.00 7.45  ? 113 LYS A O    1 
ATOM   930  C  CB   . LYS A 1 113 ? -6.791  -15.931 20.045  1.00 7.05  ? 113 LYS A CB   1 
ATOM   931  C  CG   . LYS A 1 113 ? -5.548  -15.740 20.886  1.00 8.18  ? 113 LYS A CG   1 
ATOM   932  C  CD   . LYS A 1 113 ? -4.340  -16.228 20.086  1.00 10.08 ? 113 LYS A CD   1 
ATOM   933  C  CE   . LYS A 1 113 ? -3.057  -15.700 20.670  1.00 11.76 ? 113 LYS A CE   1 
ATOM   934  N  NZ   . LYS A 1 113 ? -2.643  -16.545 21.819  1.00 16.02 ? 113 LYS A NZ   1 
ATOM   935  N  N    . TYR A 1 114 ? -9.860  -14.757 19.278  1.00 6.02  ? 114 TYR A N    1 
ATOM   936  C  CA   . TYR A 1 114 ? -10.861 -14.849 18.215  1.00 6.03  ? 114 TYR A CA   1 
ATOM   937  C  C    . TYR A 1 114 ? -10.200 -14.791 16.833  1.00 5.42  ? 114 TYR A C    1 
ATOM   938  O  O    . TYR A 1 114 ? -9.018  -14.463 16.731  1.00 5.13  ? 114 TYR A O    1 
ATOM   939  C  CB   . TYR A 1 114 ? -11.903 -13.722 18.349  1.00 6.13  ? 114 TYR A CB   1 
ATOM   940  C  CG   . TYR A 1 114 ? -12.868 -13.940 19.507  1.00 6.62  ? 114 TYR A CG   1 
ATOM   941  C  CD1  . TYR A 1 114 ? -12.550 -13.513 20.795  1.00 7.82  ? 114 TYR A CD1  1 
ATOM   942  C  CD2  . TYR A 1 114 ? -14.088 -14.597 19.313  1.00 7.01  ? 114 TYR A CD2  1 
ATOM   943  C  CE1  . TYR A 1 114 ? -13.439 -13.704 21.873  1.00 8.24  ? 114 TYR A CE1  1 
ATOM   944  C  CE2  . TYR A 1 114 ? -14.984 -14.793 20.375  1.00 8.38  ? 114 TYR A CE2  1 
ATOM   945  C  CZ   . TYR A 1 114 ? -14.650 -14.343 21.651  1.00 9.23  ? 114 TYR A CZ   1 
ATOM   946  O  OH   . TYR A 1 114 ? -15.533 -14.539 22.704  1.00 11.15 ? 114 TYR A OH   1 
ATOM   947  N  N    . ALA A 1 115 ? -10.965 -15.089 15.780  1.00 5.58  ? 115 ALA A N    1 
ATOM   948  C  CA   . ALA A 1 115 ? -10.422 -15.121 14.409  1.00 5.67  ? 115 ALA A CA   1 
ATOM   949  C  C    . ALA A 1 115 ? -10.019 -13.736 13.909  1.00 5.15  ? 115 ALA A C    1 
ATOM   950  O  O    . ALA A 1 115 ? -9.162  -13.589 13.025  1.00 5.45  ? 115 ALA A O    1 
ATOM   951  C  CB   . ALA A 1 115 ? -11.439 -15.754 13.442  1.00 6.28  ? 115 ALA A CB   1 
ATOM   952  N  N    . ALA A 1 116 ? -10.667 -12.722 14.461  1.00 4.99  ? 116 ALA A N    1 
ATOM   953  C  CA   . ALA A 1 116 ? -10.406 -11.348 14.034  1.00 4.26  ? 116 ALA A CA   1 
ATOM   954  C  C    . ALA A 1 116 ? -10.991 -10.374 15.034  1.00 4.10  ? 116 ALA A C    1 
ATOM   955  O  O    . ALA A 1 116 ? -11.729 -10.766 15.963  1.00 4.10  ? 116 ALA A O    1 
ATOM   956  C  CB   . ALA A 1 116 ? -10.964 -11.085 12.616  1.00 4.77  ? 116 ALA A CB   1 
ATOM   957  N  N    . GLU A 1 117 ? -10.617 -9.111  14.885  1.00 4.29  ? 117 GLU A N    1 
ATOM   958  C  CA   . GLU A 1 117 ? -11.167 -8.062  15.750  1.00 4.34  ? 117 GLU A CA   1 
ATOM   959  C  C    . GLU A 1 117 ? -11.367 -6.781  14.951  1.00 4.85  ? 117 GLU A C    1 
ATOM   960  O  O    . GLU A 1 117 ? -10.482 -6.359  14.231  1.00 5.85  ? 117 GLU A O    1 
ATOM   961  C  CB   . GLU A 1 117 ? -10.226 -7.811  16.927  1.00 4.33  ? 117 GLU A CB   1 
ATOM   962  C  CG   . GLU A 1 117 ? -10.736 -6.801  17.976  1.00 3.33  ? 117 GLU A CG   1 
ATOM   963  C  CD   . GLU A 1 117 ? -9.811  -6.726  19.181  1.00 4.44  ? 117 GLU A CD   1 
ATOM   964  O  OE1  . GLU A 1 117 ? -9.174  -7.757  19.517  1.00 6.19  ? 117 GLU A OE1  1 
ATOM   965  O  OE2  . GLU A 1 117 ? -9.770  -5.660  19.834  1.00 5.92  ? 117 GLU A OE2  1 
ATOM   966  N  N    . LEU A 1 118 ? -12.562 -6.209  15.057  1.00 4.35  ? 118 LEU A N    1 
ATOM   967  C  CA   . LEU A 1 118 ? -12.936 -4.963  14.376  1.00 3.31  ? 118 LEU A CA   1 
ATOM   968  C  C    . LEU A 1 118 ? -12.704 -3.782  15.322  1.00 3.37  ? 118 LEU A C    1 
ATOM   969  O  O    . LEU A 1 118 ? -13.057 -3.862  16.485  1.00 2.48  ? 118 LEU A O    1 
ATOM   970  C  CB   . LEU A 1 118 ? -14.433 -5.033  14.001  1.00 3.20  ? 118 LEU A CB   1 
ATOM   971  C  CG   . LEU A 1 118 ? -15.221 -3.766  13.621  1.00 3.57  ? 118 LEU A CG   1 
ATOM   972  C  CD1  . LEU A 1 118 ? -14.652 -3.167  12.317  1.00 5.05  ? 118 LEU A CD1  1 
ATOM   973  C  CD2  . LEU A 1 118 ? -16.699 -4.126  13.420  1.00 4.47  ? 118 LEU A CD2  1 
ATOM   974  N  N    . HIS A 1 119 ? -12.109 -2.707  14.803  1.00 2.79  ? 119 HIS A N    1 
ATOM   975  C  CA   . HIS A 1 119 ? -11.853 -1.504  15.570  1.00 3.07  ? 119 HIS A CA   1 
ATOM   976  C  C    . HIS A 1 119 ? -12.548 -0.329  14.912  1.00 3.33  ? 119 HIS A C    1 
ATOM   977  O  O    . HIS A 1 119 ? -12.180 0.032   13.797  1.00 3.68  ? 119 HIS A O    1 
ATOM   978  C  CB   . HIS A 1 119 ? -10.333 -1.268  15.659  1.00 2.43  ? 119 HIS A CB   1 
ATOM   979  C  CG   . HIS A 1 119 ? -9.650  -2.228  16.586  1.00 2.56  ? 119 HIS A CG   1 
ATOM   980  N  ND1  . HIS A 1 119 ? -8.286  -2.437  16.592  1.00 3.85  ? 119 HIS A ND1  1 
ATOM   981  C  CD2  . HIS A 1 119 ? -10.160 -3.032  17.550  1.00 2.22  ? 119 HIS A CD2  1 
ATOM   982  C  CE1  . HIS A 1 119 ? -7.984  -3.330  17.519  1.00 2.30  ? 119 HIS A CE1  1 
ATOM   983  N  NE2  . HIS A 1 119 ? -9.102  -3.711  18.114  1.00 3.30  ? 119 HIS A NE2  1 
ATOM   984  N  N    . LEU A 1 120 ? -13.562 0.231   15.587  1.00 3.34  ? 120 LEU A N    1 
ATOM   985  C  CA   . LEU A 1 120 ? -14.238 1.470   15.133  1.00 3.99  ? 120 LEU A CA   1 
ATOM   986  C  C    . LEU A 1 120 ? -13.611 2.615   15.900  1.00 3.97  ? 120 LEU A C    1 
ATOM   987  O  O    . LEU A 1 120 ? -13.742 2.708   17.128  1.00 3.83  ? 120 LEU A O    1 
ATOM   988  C  CB   . LEU A 1 120 ? -15.745 1.419   15.365  1.00 4.47  ? 120 LEU A CB   1 
ATOM   989  C  CG   . LEU A 1 120 ? -16.397 0.337   14.488  1.00 5.83  ? 120 LEU A CG   1 
ATOM   990  C  CD1  . LEU A 1 120 ? -17.268 -0.588  15.293  1.00 7.74  ? 120 LEU A CD1  1 
ATOM   991  C  CD2  . LEU A 1 120 ? -17.179 0.971   13.326  1.00 5.95  ? 120 LEU A CD2  1 
ATOM   992  N  N    . VAL A 1 121 ? -12.909 3.461   15.161  1.00 3.68  ? 121 VAL A N    1 
ATOM   993  C  CA   . VAL A 1 121 ? -12.053 4.484   15.771  1.00 4.69  ? 121 VAL A CA   1 
ATOM   994  C  C    . VAL A 1 121 ? -12.761 5.843   15.815  1.00 5.33  ? 121 VAL A C    1 
ATOM   995  O  O    . VAL A 1 121 ? -13.201 6.330   14.771  1.00 5.23  ? 121 VAL A O    1 
ATOM   996  C  CB   . VAL A 1 121 ? -10.746 4.618   14.951  1.00 4.73  ? 121 VAL A CB   1 
ATOM   997  C  CG1  . VAL A 1 121 ? -9.776  5.617   15.605  1.00 3.86  ? 121 VAL A CG1  1 
ATOM   998  C  CG2  . VAL A 1 121 ? -10.081 3.245   14.747  1.00 5.66  ? 121 VAL A CG2  1 
ATOM   999  N  N    . HIS A 1 122 ? -12.799 6.464   17.002  1.00 5.41  ? 122 HIS A N    1 
ATOM   1000 C  CA   . HIS A 1 122 ? -13.489 7.758   17.196  1.00 5.48  ? 122 HIS A CA   1 
ATOM   1001 C  C    . HIS A 1 122 ? -12.588 8.757   17.926  1.00 5.73  ? 122 HIS A C    1 
ATOM   1002 O  O    . HIS A 1 122 ? -11.811 8.364   18.804  1.00 4.96  ? 122 HIS A O    1 
ATOM   1003 C  CB   . HIS A 1 122 ? -14.786 7.592   18.015  1.00 5.72  ? 122 HIS A CB   1 
ATOM   1004 C  CG   . HIS A 1 122 ? -15.666 6.449   17.595  1.00 5.93  ? 122 HIS A CG   1 
ATOM   1005 N  ND1  . HIS A 1 122 ? -15.351 5.130   17.850  1.00 4.98  ? 122 HIS A ND1  1 
ATOM   1006 C  CD2  . HIS A 1 122 ? -16.889 6.435   17.002  1.00 5.67  ? 122 HIS A CD2  1 
ATOM   1007 C  CE1  . HIS A 1 122 ? -16.325 4.351   17.397  1.00 6.96  ? 122 HIS A CE1  1 
ATOM   1008 N  NE2  . HIS A 1 122 ? -17.269 5.118   16.872  1.00 5.34  ? 122 HIS A NE2  1 
ATOM   1009 N  N    . TRP A 1 123 ? -12.677 10.044  17.565  1.00 5.72  ? 123 TRP A N    1 
ATOM   1010 C  CA   . TRP A 1 123 ? -11.887 11.073  18.273  1.00 6.29  ? 123 TRP A CA   1 
ATOM   1011 C  C    . TRP A 1 123 ? -12.763 12.074  19.009  1.00 6.52  ? 123 TRP A C    1 
ATOM   1012 O  O    . TRP A 1 123 ? -13.864 12.400  18.555  1.00 6.29  ? 123 TRP A O    1 
ATOM   1013 C  CB   . TRP A 1 123 ? -10.914 11.784  17.313  1.00 7.60  ? 123 TRP A CB   1 
ATOM   1014 C  CG   . TRP A 1 123 ? -11.559 12.418  16.115  1.00 8.20  ? 123 TRP A CG   1 
ATOM   1015 C  CD1  . TRP A 1 123 ? -11.854 11.816  14.924  1.00 9.00  ? 123 TRP A CD1  1 
ATOM   1016 C  CD2  . TRP A 1 123 ? -11.990 13.781  15.996  1.00 9.43  ? 123 TRP A CD2  1 
ATOM   1017 N  NE1  . TRP A 1 123 ? -12.436 12.723  14.064  1.00 10.87 ? 123 TRP A NE1  1 
ATOM   1018 C  CE2  . TRP A 1 123 ? -12.530 13.938  14.701  1.00 9.91  ? 123 TRP A CE2  1 
ATOM   1019 C  CE3  . TRP A 1 123 ? -11.966 14.889  16.863  1.00 10.48 ? 123 TRP A CE3  1 
ATOM   1020 C  CZ2  . TRP A 1 123 ? -13.054 15.155  14.245  1.00 10.02 ? 123 TRP A CZ2  1 
ATOM   1021 C  CZ3  . TRP A 1 123 ? -12.493 16.107  16.406  1.00 10.46 ? 123 TRP A CZ3  1 
ATOM   1022 C  CH2  . TRP A 1 123 ? -13.025 16.226  15.105  1.00 10.21 ? 123 TRP A CH2  1 
ATOM   1023 N  N    . ASN A 1 124 ? -12.257 12.530  20.151  1.00 6.26  ? 124 ASN A N    1 
ATOM   1024 C  CA   . ASN A 1 124 ? -12.942 13.452  21.044  1.00 7.71  ? 124 ASN A CA   1 
ATOM   1025 C  C    . ASN A 1 124 ? -13.063 14.834  20.424  1.00 7.84  ? 124 ASN A C    1 
ATOM   1026 O  O    . ASN A 1 124 ? -12.063 15.493  20.194  1.00 7.24  ? 124 ASN A O    1 
ATOM   1027 C  CB   . ASN A 1 124 ? -12.172 13.547  22.368  1.00 7.43  ? 124 ASN A CB   1 
ATOM   1028 C  CG   . ASN A 1 124 ? -13.012 14.133  23.477  1.00 9.39  ? 124 ASN A CG   1 
ATOM   1029 O  OD1  . ASN A 1 124 ? -13.882 14.960  23.223  1.00 8.63  ? 124 ASN A OD1  1 
ATOM   1030 N  ND2  . ASN A 1 124 ? -12.773 13.698  24.708  1.00 10.71 ? 124 ASN A ND2  1 
ATOM   1031 N  N    . THR A 1 125 ? -14.301 15.270  20.192  1.00 9.03  ? 125 THR A N    1 
ATOM   1032 C  CA   . THR A 1 125 ? -14.542 16.513  19.469  1.00 10.51 ? 125 THR A CA   1 
ATOM   1033 C  C    . THR A 1 125 ? -14.045 17.736  20.255  1.00 10.70 ? 125 THR A C    1 
ATOM   1034 O  O    . THR A 1 125 ? -13.837 18.793  19.660  1.00 10.13 ? 125 THR A O    1 
ATOM   1035 C  CB   . THR A 1 125 ? -16.024 16.658  19.050  1.00 10.46 ? 125 THR A CB   1 
ATOM   1036 O  OG1  . THR A 1 125 ? -16.864 16.624  20.210  1.00 14.09 ? 125 THR A OG1  1 
ATOM   1037 C  CG2  . THR A 1 125 ? -16.417 15.505  18.099  1.00 12.16 ? 125 THR A CG2  1 
ATOM   1038 N  N    . LYS A 1 126 ? -13.808 17.584  21.564  1.00 10.67 ? 127 LYS A N    1 
ATOM   1039 C  CA   . LYS A 1 126 ? -13.271 18.705  22.360  1.00 11.21 ? 127 LYS A CA   1 
ATOM   1040 C  C    . LYS A 1 126 ? -11.867 19.136  21.911  1.00 10.32 ? 127 LYS A C    1 
ATOM   1041 O  O    . LYS A 1 126 ? -11.433 20.241  22.230  1.00 10.64 ? 127 LYS A O    1 
ATOM   1042 C  CB   . LYS A 1 126 ? -13.319 18.428  23.868  1.00 11.87 ? 127 LYS A CB   1 
ATOM   1043 C  CG   . LYS A 1 126 ? -12.242 17.519  24.406  1.00 12.78 ? 127 LYS A CG   1 
ATOM   1044 C  CD   . LYS A 1 126 ? -12.459 17.159  25.908  1.00 13.96 ? 127 LYS A CD   1 
ATOM   1045 C  CE   . LYS A 1 126 ? -12.038 18.278  26.869  1.00 18.04 ? 127 LYS A CE   1 
ATOM   1046 N  NZ   . LYS A 1 126 ? -12.481 18.008  28.294  1.00 17.87 ? 127 LYS A NZ   1 
ATOM   1047 N  N    . TYR A 1 127 ? -11.179 18.267  21.171  1.00 9.29  ? 128 TYR A N    1 
ATOM   1048 C  CA   . TYR A 1 127 ? -9.822  18.543  20.681  1.00 8.97  ? 128 TYR A CA   1 
ATOM   1049 C  C    . TYR A 1 127 ? -9.755  18.985  19.218  1.00 9.61  ? 128 TYR A C    1 
ATOM   1050 O  O    . TYR A 1 127 ? -8.665  19.267  18.693  1.00 9.24  ? 128 TYR A O    1 
ATOM   1051 C  CB   . TYR A 1 127 ? -8.874  17.364  20.974  1.00 9.13  ? 128 TYR A CB   1 
ATOM   1052 C  CG   . TYR A 1 127 ? -8.812  17.057  22.451  1.00 8.50  ? 128 TYR A CG   1 
ATOM   1053 C  CD1  . TYR A 1 127 ? -8.425  18.035  23.375  1.00 10.83 ? 128 TYR A CD1  1 
ATOM   1054 C  CD2  . TYR A 1 127 ? -9.131  15.792  22.930  1.00 7.81  ? 128 TYR A CD2  1 
ATOM   1055 C  CE1  . TYR A 1 127 ? -8.389  17.754  24.747  1.00 8.32  ? 128 TYR A CE1  1 
ATOM   1056 C  CE2  . TYR A 1 127 ? -9.083  15.499  24.280  1.00 8.62  ? 128 TYR A CE2  1 
ATOM   1057 C  CZ   . TYR A 1 127 ? -8.721  16.481  25.187  1.00 10.14 ? 128 TYR A CZ   1 
ATOM   1058 O  OH   . TYR A 1 127 ? -8.697  16.156  26.524  1.00 10.78 ? 128 TYR A OH   1 
ATOM   1059 N  N    . GLY A 1 128 ? -10.917 19.087  18.571  1.00 9.26  ? 129 GLY A N    1 
ATOM   1060 C  CA   . GLY A 1 128 ? -10.985 19.763  17.262  1.00 10.23 ? 129 GLY A CA   1 
ATOM   1061 C  C    . GLY A 1 128 ? -10.592 18.928  16.059  1.00 10.73 ? 129 GLY A C    1 
ATOM   1062 O  O    . GLY A 1 128 ? -11.237 19.017  15.000  1.00 11.25 ? 129 GLY A O    1 
ATOM   1063 N  N    . ASP A 1 129 ? -9.523  18.138  16.186  1.00 10.76 ? 130 ASP A N    1 
ATOM   1064 C  CA   . ASP A 1 129 ? -9.188  17.168  15.137  1.00 11.46 ? 130 ASP A CA   1 
ATOM   1065 C  C    . ASP A 1 129 ? -8.453  15.949  15.667  1.00 11.02 ? 130 ASP A C    1 
ATOM   1066 O  O    . ASP A 1 129 ? -8.009  15.925  16.826  1.00 10.00 ? 130 ASP A O    1 
ATOM   1067 C  CB   . ASP A 1 129 ? -8.458  17.815  13.931  1.00 12.01 ? 130 ASP A CB   1 
ATOM   1068 C  CG   . ASP A 1 129 ? -7.036  18.280  14.238  1.00 15.90 ? 130 ASP A CG   1 
ATOM   1069 O  OD1  . ASP A 1 129 ? -6.322  17.714  15.091  1.00 18.85 ? 130 ASP A OD1  1 
ATOM   1070 O  OD2  . ASP A 1 129 ? -6.590  19.228  13.565  1.00 20.59 ? 130 ASP A OD2  1 
ATOM   1071 N  N    . PHE A 1 130 ? -8.319  14.942  14.807  1.00 9.87  ? 131 PHE A N    1 
ATOM   1072 C  CA   . PHE A 1 130 ? -7.670  13.699  15.197  1.00 9.81  ? 131 PHE A CA   1 
ATOM   1073 C  C    . PHE A 1 130 ? -6.219  13.877  15.661  1.00 9.33  ? 131 PHE A C    1 
ATOM   1074 O  O    . PHE A 1 130 ? -5.812  13.283  16.668  1.00 8.86  ? 131 PHE A O    1 
ATOM   1075 C  CB   . PHE A 1 130 ? -7.738  12.677  14.059  1.00 9.20  ? 131 PHE A CB   1 
ATOM   1076 C  CG   . PHE A 1 130 ? -7.283  11.313  14.453  1.00 10.56 ? 131 PHE A CG   1 
ATOM   1077 C  CD1  . PHE A 1 130 ? -5.936  10.995  14.484  1.00 11.79 ? 131 PHE A CD1  1 
ATOM   1078 C  CD2  . PHE A 1 130 ? -8.205  10.353  14.843  1.00 10.34 ? 131 PHE A CD2  1 
ATOM   1079 C  CE1  . PHE A 1 130 ? -5.517  9.740   14.873  1.00 13.33 ? 131 PHE A CE1  1 
ATOM   1080 C  CE2  . PHE A 1 130 ? -7.795  9.093   15.230  1.00 9.95  ? 131 PHE A CE2  1 
ATOM   1081 C  CZ   . PHE A 1 130 ? -6.446  8.786   15.246  1.00 11.09 ? 131 PHE A CZ   1 
ATOM   1082 N  N    . GLY A 1 131 ? -5.437  14.660  14.907  1.00 9.17  ? 132 GLY A N    1 
ATOM   1083 C  CA   . GLY A 1 131 ? -4.034  14.873  15.221  1.00 9.50  ? 132 GLY A CA   1 
ATOM   1084 C  C    . GLY A 1 131 ? -3.821  15.490  16.598  1.00 9.42  ? 132 GLY A C    1 
ATOM   1085 O  O    . GLY A 1 131 ? -2.840  15.191  17.262  1.00 9.89  ? 132 GLY A O    1 
ATOM   1086 N  N    . LYS A 1 132 ? -4.740  16.355  17.017  1.00 9.07  ? 133 LYS A N    1 
ATOM   1087 C  CA   . LYS A 1 132 ? -4.651  16.953  18.349  1.00 8.73  ? 133 LYS A CA   1 
ATOM   1088 C  C    . LYS A 1 132 ? -5.135  15.964  19.421  1.00 8.79  ? 133 LYS A C    1 
ATOM   1089 O  O    . LYS A 1 132 ? -4.566  15.867  20.507  1.00 8.56  ? 133 LYS A O    1 
ATOM   1090 C  CB   . LYS A 1 132 ? -5.468  18.230  18.410  1.00 9.47  ? 133 LYS A CB   1 
ATOM   1091 C  CG   . LYS A 1 132 ? -4.783  19.432  17.744  1.00 10.44 ? 133 LYS A CG   1 
ATOM   1092 C  CD   . LYS A 1 132 ? -3.455  19.805  18.429  1.00 14.99 ? 133 LYS A CD   1 
ATOM   1093 C  CE   . LYS A 1 132 ? -2.929  21.157  17.914  1.00 16.20 ? 133 LYS A CE   1 
ATOM   1094 N  NZ   . LYS A 1 132 ? -1.961  21.733  18.894  1.00 21.71 ? 133 LYS A NZ   1 
ATOM   1095 N  N    . ALA A 1 133 ? -6.194  15.246  19.082  1.00 7.83  ? 134 ALA A N    1 
ATOM   1096 C  CA   . ALA A 1 133 ? -6.791  14.257  20.004  1.00 8.41  ? 134 ALA A CA   1 
ATOM   1097 C  C    . ALA A 1 133 ? -5.798  13.182  20.435  1.00 7.79  ? 134 ALA A C    1 
ATOM   1098 O  O    . ALA A 1 133 ? -5.755  12.819  21.615  1.00 7.76  ? 134 ALA A O    1 
ATOM   1099 C  CB   . ALA A 1 133 ? -8.018  13.608  19.358  1.00 7.78  ? 134 ALA A CB   1 
ATOM   1100 N  N    . VAL A 1 134 ? -5.009  12.649  19.495  1.00 8.18  ? 135 VAL A N    1 
ATOM   1101 C  CA   . VAL A 1 134 ? -4.059  11.562  19.857  1.00 8.96  ? 135 VAL A CA   1 
ATOM   1102 C  C    . VAL A 1 134 ? -2.963  11.993  20.835  1.00 8.89  ? 135 VAL A C    1 
ATOM   1103 O  O    . VAL A 1 134 ? -2.234  11.152  21.370  1.00 9.16  ? 135 VAL A O    1 
ATOM   1104 C  CB   . VAL A 1 134 ? -3.377  10.858  18.642  1.00 9.14  ? 135 VAL A CB   1 
ATOM   1105 C  CG1  . VAL A 1 134 ? -4.393  10.184  17.784  1.00 10.95 ? 135 VAL A CG1  1 
ATOM   1106 C  CG2  . VAL A 1 134 ? -2.485  11.831  17.839  1.00 9.83  ? 135 VAL A CG2  1 
ATOM   1107 N  N    . GLN A 1 135 ? -2.859  13.299  21.073  1.00 9.16  ? 136 GLN A N    1 
ATOM   1108 C  CA   . GLN A 1 135 ? -1.872  13.831  22.020  1.00 9.82  ? 136 GLN A CA   1 
ATOM   1109 C  C    . GLN A 1 135 ? -2.433  13.939  23.444  1.00 9.65  ? 136 GLN A C    1 
ATOM   1110 O  O    . GLN A 1 135 ? -1.773  14.466  24.357  1.00 10.64 ? 136 GLN A O    1 
ATOM   1111 C  CB   . GLN A 1 135 ? -1.397  15.205  21.533  1.00 10.09 ? 136 GLN A CB   1 
ATOM   1112 C  CG   . GLN A 1 135 ? -0.799  15.163  20.139  1.00 12.70 ? 136 GLN A CG   1 
ATOM   1113 C  CD   . GLN A 1 135 ? -0.245  16.498  19.705  1.00 17.71 ? 136 GLN A CD   1 
ATOM   1114 O  OE1  . GLN A 1 135 ? 0.635   17.066  20.360  1.00 21.53 ? 136 GLN A OE1  1 
ATOM   1115 N  NE2  . GLN A 1 135 ? -0.766  17.020  18.603  1.00 17.87 ? 136 GLN A NE2  1 
ATOM   1116 N  N    . GLN A 1 136 ? -3.651  13.443  23.639  1.00 9.37  ? 137 GLN A N    1 
ATOM   1117 C  CA   . GLN A 1 136 ? -4.358  13.606  24.922  1.00 8.83  ? 137 GLN A CA   1 
ATOM   1118 C  C    . GLN A 1 136 ? -4.772  12.242  25.490  1.00 8.09  ? 137 GLN A C    1 
ATOM   1119 O  O    . GLN A 1 136 ? -5.143  11.360  24.722  1.00 6.76  ? 137 GLN A O    1 
ATOM   1120 C  CB   . GLN A 1 136 ? -5.607  14.457  24.708  1.00 9.12  ? 137 GLN A CB   1 
ATOM   1121 C  CG   . GLN A 1 136 ? -5.310  15.818  24.023  1.00 11.38 ? 137 GLN A CG   1 
ATOM   1122 C  CD   . GLN A 1 136 ? -4.575  16.769  24.962  1.00 13.35 ? 137 GLN A CD   1 
ATOM   1123 O  OE1  . GLN A 1 136 ? -4.465  16.508  26.151  1.00 18.17 ? 137 GLN A OE1  1 
ATOM   1124 N  NE2  . GLN A 1 136 ? -4.084  17.866  24.430  1.00 18.72 ? 137 GLN A NE2  1 
ATOM   1125 N  N    . PRO A 1 137 ? -4.723  12.068  26.829  1.00 8.63  ? 138 PRO A N    1 
ATOM   1126 C  CA   . PRO A 1 137 ? -5.058  10.769  27.427  1.00 8.41  ? 138 PRO A CA   1 
ATOM   1127 C  C    . PRO A 1 137 ? -6.493  10.344  27.199  1.00 8.22  ? 138 PRO A C    1 
ATOM   1128 O  O    . PRO A 1 137 ? -6.770  9.139   27.254  1.00 7.72  ? 138 PRO A O    1 
ATOM   1129 C  CB   . PRO A 1 137 ? -4.808  10.970  28.940  1.00 8.55  ? 138 PRO A CB   1 
ATOM   1130 C  CG   . PRO A 1 137 ? -4.725  12.395  29.139  1.00 11.23 ? 138 PRO A CG   1 
ATOM   1131 C  CD   . PRO A 1 137 ? -4.306  13.042  27.854  1.00 9.04  ? 138 PRO A CD   1 
ATOM   1132 N  N    . ASP A 1 138 ? -7.390  11.301  26.957  1.00 6.84  ? 139 ASP A N    1 
ATOM   1133 C  CA   . ASP A 1 138 ? -8.782  10.962  26.644  1.00 6.76  ? 139 ASP A CA   1 
ATOM   1134 C  C    . ASP A 1 138 ? -9.151  11.357  25.203  1.00 6.11  ? 139 ASP A C    1 
ATOM   1135 O  O    . ASP A 1 138 ? -10.292 11.741  24.919  1.00 6.46  ? 139 ASP A O    1 
ATOM   1136 C  CB   . ASP A 1 138 ? -9.749  11.583  27.664  1.00 6.94  ? 139 ASP A CB   1 
ATOM   1137 C  CG   . ASP A 1 138 ? -9.672  13.098  27.721  1.00 7.46  ? 139 ASP A CG   1 
ATOM   1138 O  OD1  . ASP A 1 138 ? -8.763  13.694  27.108  1.00 8.86  ? 139 ASP A OD1  1 
ATOM   1139 O  OD2  . ASP A 1 138 ? -10.555 13.697  28.397  1.00 11.12 ? 139 ASP A OD2  1 
ATOM   1140 N  N    . GLY A 1 139 ? -8.185  11.243  24.290  1.00 5.64  ? 140 GLY A N    1 
ATOM   1141 C  CA   . GLY A 1 139 ? -8.376  11.745  22.933  1.00 5.11  ? 140 GLY A CA   1 
ATOM   1142 C  C    . GLY A 1 139 ? -9.199  10.846  22.015  1.00 5.05  ? 140 GLY A C    1 
ATOM   1143 O  O    . GLY A 1 139 ? -9.931  11.343  21.144  1.00 4.78  ? 140 GLY A O    1 
ATOM   1144 N  N    . LEU A 1 140 ? -9.081  9.526   22.210  1.00 5.22  ? 141 LEU A N    1 
ATOM   1145 C  CA   . LEU A 1 140 ? -9.754  8.574   21.321  1.00 5.03  ? 141 LEU A CA   1 
ATOM   1146 C  C    . LEU A 1 140 ? -10.640 7.607   22.099  1.00 4.70  ? 141 LEU A C    1 
ATOM   1147 O  O    . LEU A 1 140 ? -10.391 7.320   23.279  1.00 4.82  ? 141 LEU A O    1 
ATOM   1148 C  CB   . LEU A 1 140 ? -8.733  7.762   20.513  1.00 5.22  ? 141 LEU A CB   1 
ATOM   1149 C  CG   . LEU A 1 140 ? -7.741  8.446   19.553  1.00 8.04  ? 141 LEU A CG   1 
ATOM   1150 C  CD1  . LEU A 1 140 ? -7.094  7.381   18.671  1.00 6.41  ? 141 LEU A CD1  1 
ATOM   1151 C  CD2  . LEU A 1 140 ? -8.363  9.519   18.698  1.00 9.40  ? 141 LEU A CD2  1 
ATOM   1152 N  N    . ALA A 1 141 ? -11.671 7.110   21.420  1.00 4.58  ? 142 ALA A N    1 
ATOM   1153 C  CA   . ALA A 1 141 ? -12.449 5.978   21.921  1.00 4.42  ? 142 ALA A CA   1 
ATOM   1154 C  C    . ALA A 1 141 ? -12.483 4.960   20.797  1.00 4.32  ? 142 ALA A C    1 
ATOM   1155 O  O    . ALA A 1 141 ? -12.902 5.285   19.682  1.00 4.47  ? 142 ALA A O    1 
ATOM   1156 C  CB   . ALA A 1 141 ? -13.872 6.424   22.317  1.00 5.07  ? 142 ALA A CB   1 
ATOM   1157 N  N    . VAL A 1 142 ? -11.984 3.748   21.060  1.00 4.25  ? 143 VAL A N    1 
ATOM   1158 C  CA   . VAL A 1 142 ? -12.046 2.682   20.054  1.00 4.62  ? 143 VAL A CA   1 
ATOM   1159 C  C    . VAL A 1 142 ? -12.983 1.593   20.552  1.00 4.85  ? 143 VAL A C    1 
ATOM   1160 O  O    . VAL A 1 142 ? -12.851 1.101   21.681  1.00 4.69  ? 143 VAL A O    1 
ATOM   1161 C  CB   . VAL A 1 142 ? -10.663 2.111   19.701  1.00 4.25  ? 143 VAL A CB   1 
ATOM   1162 C  CG1  . VAL A 1 142 ? -10.765 1.109   18.539  1.00 5.18  ? 143 VAL A CG1  1 
ATOM   1163 C  CG2  . VAL A 1 142 ? -9.733  3.230   19.275  1.00 3.94  ? 143 VAL A CG2  1 
ATOM   1164 N  N    . LEU A 1 143 ? -13.968 1.283   19.711  1.00 4.31  ? 144 LEU A N    1 
ATOM   1165 C  CA   . LEU A 1 143 ? -14.952 0.262   19.984  1.00 4.20  ? 144 LEU A CA   1 
ATOM   1166 C  C    . LEU A 1 143 ? -14.452 -1.021  19.312  1.00 4.12  ? 144 LEU A C    1 
ATOM   1167 O  O    . LEU A 1 143 ? -14.319 -1.065  18.076  1.00 4.33  ? 144 LEU A O    1 
ATOM   1168 C  CB   . LEU A 1 143 ? -16.333 0.705   19.427  1.00 5.42  ? 144 LEU A CB   1 
ATOM   1169 C  CG   . LEU A 1 143 ? -17.517 -0.250  19.587  1.00 5.52  ? 144 LEU A CG   1 
ATOM   1170 C  CD1  . LEU A 1 143 ? -17.722 -0.574  21.056  1.00 9.26  ? 144 LEU A CD1  1 
ATOM   1171 C  CD2  . LEU A 1 143 ? -18.810 0.321   18.984  1.00 5.26  ? 144 LEU A CD2  1 
ATOM   1172 N  N    . GLY A 1 144 ? -14.178 -2.043  20.133  1.00 3.48  ? 145 GLY A N    1 
ATOM   1173 C  CA   . GLY A 1 144 ? -13.594 -3.306  19.673  1.00 3.43  ? 145 GLY A CA   1 
ATOM   1174 C  C    . GLY A 1 144 ? -14.657 -4.390  19.650  1.00 3.93  ? 145 GLY A C    1 
ATOM   1175 O  O    . GLY A 1 144 ? -15.434 -4.490  20.582  1.00 4.00  ? 145 GLY A O    1 
ATOM   1176 N  N    . ILE A 1 145 ? -14.711 -5.164  18.564  1.00 3.99  ? 146 ILE A N    1 
ATOM   1177 C  CA   . ILE A 1 145 ? -15.758 -6.180  18.379  1.00 3.92  ? 146 ILE A CA   1 
ATOM   1178 C  C    . ILE A 1 145 ? -15.075 -7.438  17.843  1.00 4.28  ? 146 ILE A C    1 
ATOM   1179 O  O    . ILE A 1 145 ? -14.369 -7.396  16.834  1.00 5.18  ? 146 ILE A O    1 
ATOM   1180 C  CB   . ILE A 1 145 ? -16.833 -5.676  17.375  1.00 4.21  ? 146 ILE A CB   1 
ATOM   1181 C  CG1  . ILE A 1 145 ? -17.523 -4.407  17.935  1.00 3.74  ? 146 ILE A CG1  1 
ATOM   1182 C  CG2  . ILE A 1 145 ? -17.849 -6.785  17.057  1.00 4.97  ? 146 ILE A CG2  1 
ATOM   1183 C  CD1  . ILE A 1 145 ? -18.562 -3.781  16.976  1.00 4.25  ? 146 ILE A CD1  1 
ATOM   1184 N  N    . PHE A 1 146 ? -15.253 -8.543  18.543  1.00 4.97  ? 147 PHE A N    1 
ATOM   1185 C  CA   . PHE A 1 146 ? -14.613 -9.796  18.149  1.00 4.05  ? 147 PHE A CA   1 
ATOM   1186 C  C    . PHE A 1 146 ? -15.375 -10.437 17.000  1.00 5.07  ? 147 PHE A C    1 
ATOM   1187 O  O    . PHE A 1 146 ? -16.604 -10.326 16.936  1.00 4.57  ? 147 PHE A O    1 
ATOM   1188 C  CB   . PHE A 1 146 ? -14.612 -10.752 19.333  1.00 4.37  ? 147 PHE A CB   1 
ATOM   1189 C  CG   . PHE A 1 146 ? -13.751 -10.298 20.476  1.00 2.84  ? 147 PHE A CG   1 
ATOM   1190 C  CD1  . PHE A 1 146 ? -12.378 -10.115 20.312  1.00 4.53  ? 147 PHE A CD1  1 
ATOM   1191 C  CD2  . PHE A 1 146 ? -14.321 -10.071 21.733  1.00 3.91  ? 147 PHE A CD2  1 
ATOM   1192 C  CE1  . PHE A 1 146 ? -11.576 -9.720  21.386  1.00 5.10  ? 147 PHE A CE1  1 
ATOM   1193 C  CE2  . PHE A 1 146 ? -13.540 -9.668  22.826  1.00 3.97  ? 147 PHE A CE2  1 
ATOM   1194 C  CZ   . PHE A 1 146 ? -12.159 -9.483  22.645  1.00 4.16  ? 147 PHE A CZ   1 
ATOM   1195 N  N    . LEU A 1 147 ? -14.638 -11.125 16.124  1.00 4.71  ? 148 LEU A N    1 
ATOM   1196 C  CA   . LEU A 1 147 ? -15.228 -11.953 15.061  1.00 5.43  ? 148 LEU A CA   1 
ATOM   1197 C  C    . LEU A 1 147 ? -14.875 -13.428 15.267  1.00 6.50  ? 148 LEU A C    1 
ATOM   1198 O  O    . LEU A 1 147 ? -13.704 -13.771 15.495  1.00 5.74  ? 148 LEU A O    1 
ATOM   1199 C  CB   . LEU A 1 147 ? -14.702 -11.525 13.678  1.00 5.88  ? 148 LEU A CB   1 
ATOM   1200 C  CG   . LEU A 1 147 ? -15.238 -10.283 12.955  1.00 5.68  ? 148 LEU A CG   1 
ATOM   1201 C  CD1  . LEU A 1 147 ? -15.012 -9.003  13.803  1.00 7.41  ? 148 LEU A CD1  1 
ATOM   1202 C  CD2  . LEU A 1 147 ? -14.586 -10.143 11.579  1.00 5.58  ? 148 LEU A CD2  1 
ATOM   1203 N  N    . LYS A 1 148 ? -15.898 -14.282 15.194  1.00 7.02  ? 149 LYS A N    1 
ATOM   1204 C  CA   . LYS A 1 148 ? -15.729 -15.733 15.157  1.00 8.21  ? 149 LYS A CA   1 
ATOM   1205 C  C    . LYS A 1 148 ? -16.234 -16.249 13.814  1.00 8.52  ? 149 LYS A C    1 
ATOM   1206 O  O    . LYS A 1 148 ? -17.044 -15.593 13.142  1.00 8.18  ? 149 LYS A O    1 
ATOM   1207 C  CB   . LYS A 1 148 ? -16.484 -16.425 16.300  1.00 7.90  ? 149 LYS A CB   1 
ATOM   1208 C  CG   . LYS A 1 148 ? -17.988 -16.183 16.315  1.00 10.38 ? 149 LYS A CG   1 
ATOM   1209 C  CD   . LYS A 1 148 ? -18.638 -16.899 17.490  1.00 11.80 ? 149 LYS A CD   1 
ATOM   1210 C  CE   . LYS A 1 148 ? -20.117 -17.018 17.255  1.00 16.02 ? 149 LYS A CE   1 
ATOM   1211 N  NZ   . LYS A 1 148 ? -20.837 -17.749 18.346  1.00 20.41 ? 149 LYS A NZ   1 
ATOM   1212 N  N    . VAL A 1 149 ? -15.771 -17.441 13.444  1.00 8.42  ? 150 VAL A N    1 
ATOM   1213 C  CA   . VAL A 1 149 ? -16.117 -18.016 12.148  1.00 9.57  ? 150 VAL A CA   1 
ATOM   1214 C  C    . VAL A 1 149 ? -17.328 -18.938 12.312  1.00 9.72  ? 150 VAL A C    1 
ATOM   1215 O  O    . VAL A 1 149 ? -17.320 -19.848 13.138  1.00 11.02 ? 150 VAL A O    1 
ATOM   1216 C  CB   . VAL A 1 149 ? -14.899 -18.752 11.537  1.00 9.69  ? 150 VAL A CB   1 
ATOM   1217 C  CG1  . VAL A 1 149 ? -15.281 -19.512 10.248  1.00 10.55 ? 150 VAL A CG1  1 
ATOM   1218 C  CG2  . VAL A 1 149 ? -13.799 -17.740 11.246  1.00 11.00 ? 150 VAL A CG2  1 
ATOM   1219 N  N    . GLY A 1 150 ? -18.367 -18.692 11.527  1.00 9.23  ? 151 GLY A N    1 
ATOM   1220 C  CA   . GLY A 1 150 ? -19.573 -19.519 11.573  1.00 10.58 ? 151 GLY A CA   1 
ATOM   1221 C  C    . GLY A 1 150 ? -20.477 -19.066 10.458  1.00 9.70  ? 151 GLY A C    1 
ATOM   1222 O  O    . GLY A 1 150 ? -20.115 -19.185 9.289   1.00 10.14 ? 151 GLY A O    1 
ATOM   1223 N  N    A SER A 1 151 ? -21.648 -18.543 10.810  0.50 10.41 ? 152 SER A N    1 
ATOM   1224 N  N    B SER A 1 151 ? -21.642 -18.535 10.819  0.50 10.20 ? 152 SER A N    1 
ATOM   1225 C  CA   A SER A 1 151 ? -22.580 -18.015 9.806   0.50 10.96 ? 152 SER A CA   1 
ATOM   1226 C  CA   B SER A 1 151 ? -22.576 -17.970 9.836   0.50 10.54 ? 152 SER A CA   1 
ATOM   1227 C  C    A SER A 1 151 ? -22.068 -16.692 9.237   0.50 10.91 ? 152 SER A C    1 
ATOM   1228 C  C    B SER A 1 151 ? -21.994 -16.708 9.213   0.50 10.67 ? 152 SER A C    1 
ATOM   1229 O  O    A SER A 1 151 ? -21.409 -15.925 9.947   0.50 10.82 ? 152 SER A O    1 
ATOM   1230 O  O    B SER A 1 151 ? -21.225 -15.992 9.864   0.50 10.49 ? 152 SER A O    1 
ATOM   1231 C  CB   A SER A 1 151 ? -23.975 -17.830 10.406  0.50 11.44 ? 152 SER A CB   1 
ATOM   1232 C  CB   B SER A 1 151 ? -23.906 -17.618 10.498  0.50 10.92 ? 152 SER A CB   1 
ATOM   1233 O  OG   A SER A 1 151 ? -23.986 -16.806 11.388  0.50 12.68 ? 152 SER A OG   1 
ATOM   1234 O  OG   B SER A 1 151 ? -24.419 -18.705 11.241  0.50 10.86 ? 152 SER A OG   1 
ATOM   1235 N  N    . ALA A 1 152 ? -22.359 -16.431 7.959   1.00 10.70 ? 153 ALA A N    1 
ATOM   1236 C  CA   . ALA A 1 152 ? -21.952 -15.175 7.313   1.00 10.45 ? 153 ALA A CA   1 
ATOM   1237 C  C    . ALA A 1 152 ? -22.589 -13.937 7.969   1.00 10.58 ? 153 ALA A C    1 
ATOM   1238 O  O    . ALA A 1 152 ? -23.698 -14.005 8.496   1.00 10.40 ? 153 ALA A O    1 
ATOM   1239 C  CB   . ALA A 1 152 ? -22.268 -15.196 5.793   1.00 11.24 ? 153 ALA A CB   1 
ATOM   1240 N  N    . LYS A 1 153 ? -21.870 -12.816 7.922   1.00 10.67 ? 154 LYS A N    1 
ATOM   1241 C  CA   . LYS A 1 153 ? -22.418 -11.513 8.300   1.00 11.49 ? 154 LYS A CA   1 
ATOM   1242 C  C    . LYS A 1 153 ? -22.818 -10.770 7.019   1.00 11.24 ? 154 LYS A C    1 
ATOM   1243 O  O    . LYS A 1 153 ? -21.957 -10.247 6.304   1.00 10.31 ? 154 LYS A O    1 
ATOM   1244 C  CB   . LYS A 1 153 ? -21.378 -10.704 9.091   1.00 11.99 ? 154 LYS A CB   1 
ATOM   1245 C  CG   . LYS A 1 153 ? -21.942 -9.502  9.864   1.00 13.61 ? 154 LYS A CG   1 
ATOM   1246 C  CD   . LYS A 1 153 ? -22.574 -9.965  11.186  1.00 15.72 ? 154 LYS A CD   1 
ATOM   1247 C  CE   . LYS A 1 153 ? -23.041 -8.796  12.027  1.00 19.50 ? 154 LYS A CE   1 
ATOM   1248 N  NZ   . LYS A 1 153 ? -23.886 -9.284  13.148  1.00 21.08 ? 154 LYS A NZ   1 
ATOM   1249 N  N    . PRO A 1 154 ? -24.130 -10.735 6.696   1.00 11.97 ? 155 PRO A N    1 
ATOM   1250 C  CA   . PRO A 1 154 ? -24.525 -10.060 5.447   1.00 11.99 ? 155 PRO A CA   1 
ATOM   1251 C  C    . PRO A 1 154 ? -24.022 -8.614  5.377   1.00 11.57 ? 155 PRO A C    1 
ATOM   1252 O  O    . PRO A 1 154 ? -23.669 -8.134  4.294   1.00 12.11 ? 155 PRO A O    1 
ATOM   1253 C  CB   . PRO A 1 154 ? -26.061 -10.095 5.503   1.00 12.67 ? 155 PRO A CB   1 
ATOM   1254 C  CG   . PRO A 1 154 ? -26.356 -11.292 6.362   1.00 13.38 ? 155 PRO A CG   1 
ATOM   1255 C  CD   . PRO A 1 154 ? -25.300 -11.255 7.425   1.00 12.80 ? 155 PRO A CD   1 
ATOM   1256 N  N    . GLY A 1 155 ? -23.954 -7.945  6.524   1.00 11.56 ? 156 GLY A N    1 
ATOM   1257 C  CA   . GLY A 1 155 ? -23.535 -6.545  6.574   1.00 11.23 ? 156 GLY A CA   1 
ATOM   1258 C  C    . GLY A 1 155 ? -22.071 -6.293  6.247   1.00 11.41 ? 156 GLY A C    1 
ATOM   1259 O  O    . GLY A 1 155 ? -21.685 -5.143  6.019   1.00 11.71 ? 156 GLY A O    1 
ATOM   1260 N  N    . LEU A 1 156 ? -21.268 -7.357  6.241   1.00 9.78  ? 157 LEU A N    1 
ATOM   1261 C  CA   . LEU A 1 156 ? -19.829 -7.295  5.927   1.00 9.11  ? 157 LEU A CA   1 
ATOM   1262 C  C    . LEU A 1 156 ? -19.531 -7.538  4.454   1.00 9.39  ? 157 LEU A C    1 
ATOM   1263 O  O    . LEU A 1 156 ? -18.445 -7.214  3.961   1.00 9.45  ? 157 LEU A O    1 
ATOM   1264 C  CB   . LEU A 1 156 ? -19.058 -8.311  6.788   1.00 9.01  ? 157 LEU A CB   1 
ATOM   1265 C  CG   . LEU A 1 156 ? -17.534 -8.413  6.633   1.00 9.43  ? 157 LEU A CG   1 
ATOM   1266 C  CD1  . LEU A 1 156 ? -16.881 -7.076  7.002   1.00 10.54 ? 157 LEU A CD1  1 
ATOM   1267 C  CD2  . LEU A 1 156 ? -16.973 -9.543  7.472   1.00 8.38  ? 157 LEU A CD2  1 
ATOM   1268 N  N    . GLN A 1 157 ? -20.490 -8.112  3.728   1.00 9.71  ? 158 GLN A N    1 
ATOM   1269 C  CA   . GLN A 1 157 ? -20.167 -8.561  2.376   1.00 10.57 ? 158 GLN A CA   1 
ATOM   1270 C  C    . GLN A 1 157 ? -19.748 -7.449  1.423   1.00 10.30 ? 158 GLN A C    1 
ATOM   1271 O  O    . GLN A 1 157 ? -18.882 -7.665  0.589   1.00 11.29 ? 158 GLN A O    1 
ATOM   1272 C  CB   . GLN A 1 157 ? -21.280 -9.415  1.763   1.00 10.66 ? 158 GLN A CB   1 
ATOM   1273 C  CG   . GLN A 1 157 ? -20.796 -10.184 0.508   1.00 11.54 ? 158 GLN A CG   1 
ATOM   1274 C  CD   . GLN A 1 157 ? -19.719 -11.223 0.804   1.00 12.74 ? 158 GLN A CD   1 
ATOM   1275 O  OE1  . GLN A 1 157 ? -19.687 -11.829 1.893   1.00 11.99 ? 158 GLN A OE1  1 
ATOM   1276 N  NE2  . GLN A 1 157 ? -18.838 -11.454 -0.174  1.00 11.99 ? 158 GLN A NE2  1 
ATOM   1277 N  N    . LYS A 1 158 ? -20.326 -6.256  1.558   1.00 11.72 ? 159 LYS A N    1 
ATOM   1278 C  CA   . LYS A 1 158 ? -19.928 -5.147  0.700   1.00 12.53 ? 159 LYS A CA   1 
ATOM   1279 C  C    . LYS A 1 158 ? -18.439 -4.841  0.879   1.00 11.87 ? 159 LYS A C    1 
ATOM   1280 O  O    . LYS A 1 158 ? -17.754 -4.483  -0.076  1.00 11.91 ? 159 LYS A O    1 
ATOM   1281 C  CB   . LYS A 1 158 ? -20.751 -3.894  0.989   1.00 13.01 ? 159 LYS A CB   1 
ATOM   1282 C  CG   . LYS A 1 158 ? -22.047 -3.758  0.205   1.00 15.98 ? 159 LYS A CG   1 
ATOM   1283 C  CD   . LYS A 1 158 ? -22.559 -2.284  0.264   1.00 16.29 ? 159 LYS A CD   1 
ATOM   1284 C  CE   . LYS A 1 158 ? -21.425 -1.249  0.419   1.00 20.61 ? 159 LYS A CE   1 
ATOM   1285 N  NZ   . LYS A 1 158 ? -21.855 0.201   0.427   1.00 21.50 ? 159 LYS A NZ   1 
ATOM   1286 N  N    . VAL A 1 159 ? -17.948 -4.986  2.114   1.00 10.91 ? 160 VAL A N    1 
ATOM   1287 C  CA   . VAL A 1 159 ? -16.519 -4.785  2.393   1.00 10.40 ? 160 VAL A CA   1 
ATOM   1288 C  C    . VAL A 1 159 ? -15.701 -5.900  1.727   1.00 10.38 ? 160 VAL A C    1 
ATOM   1289 O  O    . VAL A 1 159 ? -14.715 -5.631  1.041   1.00 10.24 ? 160 VAL A O    1 
ATOM   1290 C  CB   . VAL A 1 159 ? -16.238 -4.764  3.918   1.00 10.12 ? 160 VAL A CB   1 
ATOM   1291 C  CG1  . VAL A 1 159 ? -14.718 -4.708  4.205   1.00 10.16 ? 160 VAL A CG1  1 
ATOM   1292 C  CG2  . VAL A 1 159 ? -16.985 -3.612  4.594   1.00 11.16 ? 160 VAL A CG2  1 
ATOM   1293 N  N    . VAL A 1 160 ? -16.130 -7.146  1.905   1.00 10.94 ? 161 VAL A N    1 
ATOM   1294 C  CA   . VAL A 1 160 ? -15.389 -8.306  1.395   1.00 12.36 ? 161 VAL A CA   1 
ATOM   1295 C  C    . VAL A 1 160 ? -15.234 -8.183  -0.119  1.00 12.43 ? 161 VAL A C    1 
ATOM   1296 O  O    . VAL A 1 160 ? -14.166 -8.431  -0.674  1.00 11.74 ? 161 VAL A O    1 
ATOM   1297 C  CB   . VAL A 1 160 ? -16.092 -9.655  1.779   1.00 12.67 ? 161 VAL A CB   1 
ATOM   1298 C  CG1  . VAL A 1 160 ? -15.484 -10.840 1.034   1.00 15.10 ? 161 VAL A CG1  1 
ATOM   1299 C  CG2  . VAL A 1 160 ? -15.987 -9.889  3.281   1.00 13.57 ? 161 VAL A CG2  1 
ATOM   1300 N  N    . ASP A 1 161 ? -16.294 -7.741  -0.774  1.00 13.04 ? 162 ASP A N    1 
ATOM   1301 C  CA   . ASP A 1 161 ? -16.315 -7.764  -2.232  1.00 13.83 ? 162 ASP A CA   1 
ATOM   1302 C  C    . ASP A 1 161 ? -15.442 -6.716  -2.895  1.00 13.70 ? 162 ASP A C    1 
ATOM   1303 O  O    . ASP A 1 161 ? -15.033 -6.895  -4.042  1.00 15.05 ? 162 ASP A O    1 
ATOM   1304 C  CB   . ASP A 1 161 ? -17.747 -7.674  -2.743  1.00 14.36 ? 162 ASP A CB   1 
ATOM   1305 C  CG   . ASP A 1 161 ? -18.478 -9.004  -2.649  1.00 16.37 ? 162 ASP A CG   1 
ATOM   1306 O  OD1  . ASP A 1 161 ? -17.823 -10.076 -2.691  1.00 20.17 ? 162 ASP A OD1  1 
ATOM   1307 O  OD2  . ASP A 1 161 ? -19.712 -8.974  -2.543  1.00 20.20 ? 162 ASP A OD2  1 
ATOM   1308 N  N    . VAL A 1 162 ? -15.152 -5.630  -2.183  1.00 12.61 ? 163 VAL A N    1 
ATOM   1309 C  CA   . VAL A 1 162 ? -14.312 -4.575  -2.717  1.00 12.69 ? 163 VAL A CA   1 
ATOM   1310 C  C    . VAL A 1 162 ? -12.807 -4.866  -2.509  1.00 12.00 ? 163 VAL A C    1 
ATOM   1311 O  O    . VAL A 1 162 ? -11.969 -4.186  -3.088  1.00 11.49 ? 163 VAL A O    1 
ATOM   1312 C  CB   . VAL A 1 162 ? -14.731 -3.197  -2.129  1.00 12.78 ? 163 VAL A CB   1 
ATOM   1313 C  CG1  . VAL A 1 162 ? -14.171 -2.989  -0.722  1.00 13.81 ? 163 VAL A CG1  1 
ATOM   1314 C  CG2  . VAL A 1 162 ? -14.332 -2.046  -3.056  1.00 13.51 ? 163 VAL A CG2  1 
ATOM   1315 N  N    . LEU A 1 163 ? -12.468 -5.867  -1.685  1.00 11.93 ? 164 LEU A N    1 
ATOM   1316 C  CA   . LEU A 1 163 ? -11.059 -6.133  -1.348  1.00 11.65 ? 164 LEU A CA   1 
ATOM   1317 C  C    . LEU A 1 163 ? -10.161 -6.488  -2.536  1.00 12.67 ? 164 LEU A C    1 
ATOM   1318 O  O    . LEU A 1 163 ? -8.970  -6.166  -2.538  1.00 12.23 ? 164 LEU A O    1 
ATOM   1319 C  CB   . LEU A 1 163 ? -10.925 -7.204  -0.261  1.00 11.61 ? 164 LEU A CB   1 
ATOM   1320 C  CG   . LEU A 1 163 ? -11.572 -6.929  1.098   1.00 10.96 ? 164 LEU A CG   1 
ATOM   1321 C  CD1  . LEU A 1 163 ? -11.253 -8.095  2.042   1.00 10.84 ? 164 LEU A CD1  1 
ATOM   1322 C  CD2  . LEU A 1 163 ? -11.094 -5.618  1.679   1.00 8.72  ? 164 LEU A CD2  1 
ATOM   1323 N  N    . ASP A 1 164 ? -10.731 -7.140  -3.545  1.00 14.22 ? 165 ASP A N    1 
ATOM   1324 C  CA   . ASP A 1 164 ? -9.943  -7.507  -4.713  1.00 15.93 ? 165 ASP A CA   1 
ATOM   1325 C  C    . ASP A 1 164 ? -9.426  -6.254  -5.436  1.00 15.29 ? 165 ASP A C    1 
ATOM   1326 O  O    . ASP A 1 164 ? -8.422  -6.325  -6.137  1.00 16.69 ? 165 ASP A O    1 
ATOM   1327 C  CB   . ASP A 1 164 ? -10.768 -8.374  -5.672  1.00 16.84 ? 165 ASP A CB   1 
ATOM   1328 C  CG   . ASP A 1 164 ? -11.702 -7.553  -6.522  1.00 20.86 ? 165 ASP A CG   1 
ATOM   1329 O  OD1  . ASP A 1 164 ? -12.654 -6.968  -5.957  1.00 25.53 ? 165 ASP A OD1  1 
ATOM   1330 O  OD2  . ASP A 1 164 ? -11.475 -7.471  -7.753  1.00 26.23 ? 165 ASP A OD2  1 
ATOM   1331 N  N    . SER A 1 165 ? -10.100 -5.121  -5.246  1.00 14.30 ? 166 SER A N    1 
ATOM   1332 C  CA   . SER A 1 165 ? -9.721  -3.870  -5.919  1.00 13.55 ? 166 SER A CA   1 
ATOM   1333 C  C    . SER A 1 165 ? -8.660  -3.066  -5.163  1.00 12.81 ? 166 SER A C    1 
ATOM   1334 O  O    . SER A 1 165 ? -8.137  -2.061  -5.683  1.00 12.41 ? 166 SER A O    1 
ATOM   1335 C  CB   . SER A 1 165 ? -10.952 -3.011  -6.193  1.00 13.93 ? 166 SER A CB   1 
ATOM   1336 O  OG   . SER A 1 165 ? -11.325 -2.253  -5.048  1.00 15.80 ? 166 SER A OG   1 
ATOM   1337 N  N    . ILE A 1 166 ? -8.356  -3.489  -3.933  1.00 11.20 ? 167 ILE A N    1 
ATOM   1338 C  CA   . ILE A 1 166 ? -7.310  -2.850  -3.123  1.00 10.58 ? 167 ILE A CA   1 
ATOM   1339 C  C    . ILE A 1 166 ? -6.308  -3.884  -2.585  1.00 10.90 ? 167 ILE A C    1 
ATOM   1340 O  O    . ILE A 1 166 ? -5.888  -3.849  -1.425  1.00 11.23 ? 167 ILE A O    1 
ATOM   1341 C  CB   . ILE A 1 166 ? -7.915  -1.990  -1.966  1.00 10.24 ? 167 ILE A CB   1 
ATOM   1342 C  CG1  . ILE A 1 166 ? -8.794  -2.843  -1.057  1.00 9.46  ? 167 ILE A CG1  1 
ATOM   1343 C  CG2  . ILE A 1 166 ? -8.717  -0.823  -2.532  1.00 9.61  ? 167 ILE A CG2  1 
ATOM   1344 C  CD1  . ILE A 1 166 ? -8.932  -2.284  0.374   1.00 10.31 ? 167 ILE A CD1  1 
ATOM   1345 N  N    . LYS A 1 167 ? -5.895  -4.797  -3.454  1.00 10.84 ? 168 LYS A N    1 
ATOM   1346 C  CA   . LYS A 1 167 ? -5.078  -5.922  -3.011  1.00 11.36 ? 168 LYS A CA   1 
ATOM   1347 C  C    . LYS A 1 167 ? -3.762  -5.523  -2.325  1.00 10.67 ? 168 LYS A C    1 
ATOM   1348 O  O    . LYS A 1 167 ? -3.369  -6.146  -1.342  1.00 9.66  ? 168 LYS A O    1 
ATOM   1349 C  CB   . LYS A 1 167 ? -4.796  -6.854  -4.193  1.00 10.80 ? 168 LYS A CB   1 
ATOM   1350 C  CG   . LYS A 1 167 ? -3.981  -8.083  -3.830  1.00 13.31 ? 168 LYS A CG   1 
ATOM   1351 C  CD   . LYS A 1 167 ? -3.966  -9.110  -4.967  1.00 14.13 ? 168 LYS A CD   1 
ATOM   1352 C  CE   . LYS A 1 167 ? -3.253  -10.385 -4.537  1.00 20.09 ? 168 LYS A CE   1 
ATOM   1353 N  NZ   . LYS A 1 167 ? -3.214  -11.419 -5.630  1.00 23.36 ? 168 LYS A NZ   1 
ATOM   1354 N  N    . THR A 1 168 ? -3.097  -4.495  -2.860  1.00 9.82  ? 169 THR A N    1 
ATOM   1355 C  CA   . THR A 1 168 ? -1.731  -4.151  -2.469  1.00 9.43  ? 169 THR A CA   1 
ATOM   1356 C  C    . THR A 1 168 ? -1.631  -2.797  -1.779  1.00 10.24 ? 169 THR A C    1 
ATOM   1357 O  O    . THR A 1 168 ? -2.506  -1.946  -1.941  1.00 9.51  ? 169 THR A O    1 
ATOM   1358 C  CB   . THR A 1 168 ? -0.788  -4.177  -3.692  1.00 10.31 ? 169 THR A CB   1 
ATOM   1359 O  OG1  . THR A 1 168 ? -1.384  -3.455  -4.778  1.00 10.17 ? 169 THR A OG1  1 
ATOM   1360 C  CG2  . THR A 1 168 ? -0.564  -5.608  -4.133  1.00 9.32  ? 169 THR A CG2  1 
ATOM   1361 N  N    . LYS A 1 169 ? -0.567  -2.630  -0.998  1.00 10.42 ? 170 LYS A N    1 
ATOM   1362 C  CA   . LYS A 1 169 ? -0.309  -1.407  -0.247  1.00 12.36 ? 170 LYS A CA   1 
ATOM   1363 C  C    . LYS A 1 169 ? -0.429  -0.179  -1.121  1.00 12.31 ? 170 LYS A C    1 
ATOM   1364 O  O    . LYS A 1 169 ? 0.147   -0.139  -2.210  1.00 12.56 ? 170 LYS A O    1 
ATOM   1365 C  CB   . LYS A 1 169 ? 1.082   -1.432  0.377   1.00 11.76 ? 170 LYS A CB   1 
ATOM   1366 C  CG   . LYS A 1 169 ? 1.338   -0.200  1.255   1.00 13.67 ? 170 LYS A CG   1 
ATOM   1367 C  CD   . LYS A 1 169 ? 2.772   0.055   1.682   1.00 15.90 ? 170 LYS A CD   1 
ATOM   1368 C  CE   . LYS A 1 169 ? 3.583   -1.179  1.820   1.00 21.09 ? 170 LYS A CE   1 
ATOM   1369 N  NZ   . LYS A 1 169 ? 4.390   -1.373  0.600   1.00 22.91 ? 170 LYS A NZ   1 
ATOM   1370 N  N    . GLY A 1 170 ? -1.185  0.806   -0.642  1.00 12.12 ? 171 GLY A N    1 
ATOM   1371 C  CA   . GLY A 1 170 ? -1.312  2.091   -1.335  1.00 11.95 ? 171 GLY A CA   1 
ATOM   1372 C  C    . GLY A 1 170 ? -2.482  2.207   -2.292  1.00 12.34 ? 171 GLY A C    1 
ATOM   1373 O  O    . GLY A 1 170 ? -2.751  3.305   -2.814  1.00 12.71 ? 171 GLY A O    1 
ATOM   1374 N  N    . LYS A 1 171 ? -3.178  1.095   -2.534  1.00 11.47 ? 172 LYS A N    1 
ATOM   1375 C  CA   . LYS A 1 171 ? -4.383  1.101   -3.360  1.00 12.14 ? 172 LYS A CA   1 
ATOM   1376 C  C    . LYS A 1 171 ? -5.594  1.542   -2.550  1.00 11.55 ? 172 LYS A C    1 
ATOM   1377 O  O    . LYS A 1 171 ? -5.755  1.168   -1.381  1.00 11.33 ? 172 LYS A O    1 
ATOM   1378 C  CB   . LYS A 1 171 ? -4.657  -0.274  -3.986  1.00 11.87 ? 172 LYS A CB   1 
ATOM   1379 C  CG   . LYS A 1 171 ? -3.640  -0.684  -5.047  1.00 13.18 ? 172 LYS A CG   1 
ATOM   1380 C  CD   . LYS A 1 171 ? -4.159  -1.808  -5.960  1.00 14.65 ? 172 LYS A CD   1 
ATOM   1381 C  CE   . LYS A 1 171 ? -5.193  -1.292  -6.971  1.00 18.15 ? 172 LYS A CE   1 
ATOM   1382 N  NZ   . LYS A 1 171 ? -5.689  -2.387  -7.882  1.00 19.55 ? 172 LYS A NZ   1 
ATOM   1383 N  N    . SER A 1 172 ? -6.448  2.338   -3.182  1.00 11.69 ? 173 SER A N    1 
ATOM   1384 C  CA   . SER A 1 172 ? -7.678  2.774   -2.549  1.00 11.31 ? 173 SER A CA   1 
ATOM   1385 C  C    . SER A 1 172 ? -8.830  2.646   -3.541  1.00 11.99 ? 173 SER A C    1 
ATOM   1386 O  O    . SER A 1 172 ? -8.601  2.555   -4.771  1.00 11.19 ? 173 SER A O    1 
ATOM   1387 C  CB   . SER A 1 172 ? -7.534  4.212   -2.039  1.00 11.69 ? 173 SER A CB   1 
ATOM   1388 O  OG   . SER A 1 172 ? -7.499  5.136   -3.111  1.00 12.58 ? 173 SER A OG   1 
ATOM   1389 N  N    . ALA A 1 173 ? -10.060 2.622   -3.021  1.00 11.96 ? 174 ALA A N    1 
ATOM   1390 C  CA   . ALA A 1 173 ? -11.248 2.574   -3.864  1.00 11.74 ? 174 ALA A CA   1 
ATOM   1391 C  C    . ALA A 1 173 ? -12.397 3.351   -3.242  1.00 12.28 ? 174 ALA A C    1 
ATOM   1392 O  O    . ALA A 1 173 ? -12.545 3.397   -2.011  1.00 10.68 ? 174 ALA A O    1 
ATOM   1393 C  CB   . ALA A 1 173 ? -11.665 1.119   -4.142  1.00 11.86 ? 174 ALA A CB   1 
ATOM   1394 N  N    . ASP A 1 174 ? -13.210 3.981   -4.090  1.00 12.38 ? 175 ASP A N    1 
ATOM   1395 C  CA   . ASP A 1 174 ? -14.413 4.643   -3.613  1.00 13.44 ? 175 ASP A CA   1 
ATOM   1396 C  C    . ASP A 1 174 ? -15.281 3.664   -2.815  1.00 13.16 ? 175 ASP A C    1 
ATOM   1397 O  O    . ASP A 1 174 ? -15.461 2.511   -3.212  1.00 13.53 ? 175 ASP A O    1 
ATOM   1398 C  CB   . ASP A 1 174 ? -15.202 5.242   -4.792  1.00 14.12 ? 175 ASP A CB   1 
ATOM   1399 C  CG   . ASP A 1 174 ? -14.384 6.260   -5.566  1.00 17.71 ? 175 ASP A CG   1 
ATOM   1400 O  OD1  . ASP A 1 174 ? -13.572 6.979   -4.937  1.00 21.11 ? 175 ASP A OD1  1 
ATOM   1401 O  OD2  . ASP A 1 174 ? -14.547 6.347   -6.800  1.00 20.88 ? 175 ASP A OD2  1 
ATOM   1402 N  N    . PHE A 1 175 ? -15.778 4.111   -1.664  1.00 13.05 ? 176 PHE A N    1 
ATOM   1403 C  CA   . PHE A 1 175 ? -16.565 3.224   -0.807  1.00 13.08 ? 176 PHE A CA   1 
ATOM   1404 C  C    . PHE A 1 175 ? -17.620 4.034   -0.081  1.00 13.41 ? 176 PHE A C    1 
ATOM   1405 O  O    . PHE A 1 175 ? -17.522 4.303   1.125   1.00 14.18 ? 176 PHE A O    1 
ATOM   1406 C  CB   . PHE A 1 175 ? -15.664 2.437   0.162   1.00 13.17 ? 176 PHE A CB   1 
ATOM   1407 C  CG   . PHE A 1 175 ? -16.298 1.171   0.683   1.00 12.43 ? 176 PHE A CG   1 
ATOM   1408 C  CD1  . PHE A 1 175 ? -16.584 0.115   -0.180  1.00 14.04 ? 176 PHE A CD1  1 
ATOM   1409 C  CD2  . PHE A 1 175 ? -16.630 1.041   2.028   1.00 12.93 ? 176 PHE A CD2  1 
ATOM   1410 C  CE1  . PHE A 1 175 ? -17.196 -1.049  0.297   1.00 14.22 ? 176 PHE A CE1  1 
ATOM   1411 C  CE2  . PHE A 1 175 ? -17.228 -0.120  2.514   1.00 12.32 ? 176 PHE A CE2  1 
ATOM   1412 C  CZ   . PHE A 1 175 ? -17.518 -1.162  1.640   1.00 13.18 ? 176 PHE A CZ   1 
ATOM   1413 N  N    . THR A 1 176 ? -18.645 4.430   -0.833  1.00 12.34 ? 177 THR A N    1 
ATOM   1414 C  CA   . THR A 1 176 ? -19.678 5.292   -0.293  1.00 12.73 ? 177 THR A CA   1 
ATOM   1415 C  C    . THR A 1 176 ? -20.887 4.487   0.170   1.00 11.74 ? 177 THR A C    1 
ATOM   1416 O  O    . THR A 1 176 ? -21.103 3.353   -0.277  1.00 12.06 ? 177 THR A O    1 
ATOM   1417 C  CB   . THR A 1 176 ? -20.129 6.351   -1.341  1.00 12.49 ? 177 THR A CB   1 
ATOM   1418 O  OG1  . THR A 1 176 ? -20.713 5.696   -2.467  1.00 15.76 ? 177 THR A OG1  1 
ATOM   1419 C  CG2  . THR A 1 176 ? -18.963 7.175   -1.807  1.00 15.81 ? 177 THR A CG2  1 
ATOM   1420 N  N    . ASN A 1 177 ? -21.657 5.101   1.069   1.00 11.05 ? 178 ASN A N    1 
ATOM   1421 C  CA   . ASN A 1 177 ? -22.947 4.587   1.522   1.00 10.95 ? 178 ASN A CA   1 
ATOM   1422 C  C    . ASN A 1 177 ? -22.888 3.260   2.276   1.00 10.99 ? 178 ASN A C    1 
ATOM   1423 O  O    . ASN A 1 177 ? -23.886 2.538   2.350   1.00 11.68 ? 178 ASN A O    1 
ATOM   1424 C  CB   . ASN A 1 177 ? -23.928 4.524   0.355   1.00 11.34 ? 178 ASN A CB   1 
ATOM   1425 C  CG   . ASN A 1 177 ? -24.162 5.893   -0.267  1.00 12.72 ? 178 ASN A CG   1 
ATOM   1426 O  OD1  . ASN A 1 177 ? -24.858 6.734   0.301   1.00 14.08 ? 178 ASN A OD1  1 
ATOM   1427 N  ND2  . ASN A 1 177 ? -23.552 6.130   -1.425  1.00 13.08 ? 178 ASN A ND2  1 
ATOM   1428 N  N    . PHE A 1 178 ? -21.739 2.966   2.878   1.00 9.84  ? 179 PHE A N    1 
ATOM   1429 C  CA   . PHE A 1 178 ? -21.648 1.752   3.691   1.00 9.57  ? 179 PHE A CA   1 
ATOM   1430 C  C    . PHE A 1 178 ? -22.130 2.049   5.103   1.00 9.35  ? 179 PHE A C    1 
ATOM   1431 O  O    . PHE A 1 178 ? -21.661 2.987   5.726   1.00 10.34 ? 179 PHE A O    1 
ATOM   1432 C  CB   . PHE A 1 178 ? -20.238 1.183   3.731   1.00 9.85  ? 179 PHE A CB   1 
ATOM   1433 C  CG   . PHE A 1 178 ? -20.122 -0.027  4.614   1.00 7.77  ? 179 PHE A CG   1 
ATOM   1434 C  CD1  . PHE A 1 178 ? -20.487 -1.273  4.134   1.00 8.75  ? 179 PHE A CD1  1 
ATOM   1435 C  CD2  . PHE A 1 178 ? -19.717 0.097   5.944   1.00 8.36  ? 179 PHE A CD2  1 
ATOM   1436 C  CE1  . PHE A 1 178 ? -20.413 -2.405  4.940   1.00 9.12  ? 179 PHE A CE1  1 
ATOM   1437 C  CE2  . PHE A 1 178 ? -19.655 -1.033  6.766   1.00 8.51  ? 179 PHE A CE2  1 
ATOM   1438 C  CZ   . PHE A 1 178 ? -19.999 -2.281  6.267   1.00 9.77  ? 179 PHE A CZ   1 
ATOM   1439 N  N    . ASP A 1 179 ? -23.032 1.214   5.615   1.00 9.62  ? 180 ASP A N    1 
ATOM   1440 C  CA   . ASP A 1 179 ? -23.649 1.425   6.922   1.00 9.37  ? 180 ASP A CA   1 
ATOM   1441 C  C    . ASP A 1 179 ? -23.001 0.549   7.993   1.00 8.56  ? 180 ASP A C    1 
ATOM   1442 O  O    . ASP A 1 179 ? -23.225 -0.665  8.016   1.00 8.46  ? 180 ASP A O    1 
ATOM   1443 C  CB   . ASP A 1 179 ? -25.142 1.092   6.831   1.00 10.51 ? 180 ASP A CB   1 
ATOM   1444 C  CG   . ASP A 1 179 ? -25.905 1.473   8.086   1.00 11.77 ? 180 ASP A CG   1 
ATOM   1445 O  OD1  . ASP A 1 179 ? -25.268 1.709   9.138   1.00 10.52 ? 180 ASP A OD1  1 
ATOM   1446 O  OD2  . ASP A 1 179 ? -27.148 1.553   8.002   1.00 16.04 ? 180 ASP A OD2  1 
ATOM   1447 N  N    . PRO A 1 180 ? -22.190 1.147   8.891   1.00 8.44  ? 181 PRO A N    1 
ATOM   1448 C  CA   . PRO A 1 180 ? -21.483 0.274   9.848   1.00 8.38  ? 181 PRO A CA   1 
ATOM   1449 C  C    . PRO A 1 180 ? -22.396 -0.317  10.939  1.00 8.55  ? 181 PRO A C    1 
ATOM   1450 O  O    . PRO A 1 180 ? -21.942 -1.165  11.718  1.00 8.10  ? 181 PRO A O    1 
ATOM   1451 C  CB   . PRO A 1 180 ? -20.425 1.202   10.445  1.00 8.90  ? 181 PRO A CB   1 
ATOM   1452 C  CG   . PRO A 1 180 ? -21.044 2.561   10.377  1.00 8.60  ? 181 PRO A CG   1 
ATOM   1453 C  CD   . PRO A 1 180 ? -21.844 2.566   9.080   1.00 8.41  ? 181 PRO A CD   1 
ATOM   1454 N  N    . ARG A 1 181 ? -23.668 0.090   10.985  1.00 7.93  ? 182 ARG A N    1 
ATOM   1455 C  CA   . ARG A 1 181 ? -24.605 -0.548  11.939  1.00 8.97  ? 182 ARG A CA   1 
ATOM   1456 C  C    . ARG A 1 181 ? -24.743 -2.048  11.658  1.00 8.99  ? 182 ARG A C    1 
ATOM   1457 O  O    . ARG A 1 181 ? -25.083 -2.839  12.552  1.00 9.94  ? 182 ARG A O    1 
ATOM   1458 C  CB   . ARG A 1 181 ? -25.979 0.122   11.904  1.00 8.73  ? 182 ARG A CB   1 
ATOM   1459 C  CG   . ARG A 1 181 ? -25.943 1.570   12.426  1.00 9.86  ? 182 ARG A CG   1 
ATOM   1460 C  CD   . ARG A 1 181 ? -27.327 2.226   12.334  1.00 10.36 ? 182 ARG A CD   1 
ATOM   1461 N  NE   . ARG A 1 181 ? -27.719 2.413   10.937  1.00 14.47 ? 182 ARG A NE   1 
ATOM   1462 C  CZ   . ARG A 1 181 ? -28.815 3.058   10.547  1.00 17.18 ? 182 ARG A CZ   1 
ATOM   1463 N  NH1  . ARG A 1 181 ? -29.627 3.600   11.448  1.00 18.08 ? 182 ARG A NH1  1 
ATOM   1464 N  NH2  . ARG A 1 181 ? -29.093 3.174   9.253   1.00 18.10 ? 182 ARG A NH2  1 
ATOM   1465 N  N    . GLY A 1 182 ? -24.465 -2.425  10.417  1.00 8.83  ? 183 GLY A N    1 
ATOM   1466 C  CA   . GLY A 1 182 ? -24.525 -3.813  9.979   1.00 8.89  ? 183 GLY A CA   1 
ATOM   1467 C  C    . GLY A 1 182 ? -23.415 -4.687  10.523  1.00 9.41  ? 183 GLY A C    1 
ATOM   1468 O  O    . GLY A 1 182 ? -23.412 -5.899  10.275  1.00 10.64 ? 183 GLY A O    1 
ATOM   1469 N  N    . LEU A 1 183 ? -22.473 -4.085  11.258  1.00 8.20  ? 184 LEU A N    1 
ATOM   1470 C  CA   . LEU A 1 183 ? -21.330 -4.819  11.835  1.00 8.19  ? 184 LEU A CA   1 
ATOM   1471 C  C    . LEU A 1 183 ? -21.457 -4.989  13.350  1.00 8.70  ? 184 LEU A C    1 
ATOM   1472 O  O    . LEU A 1 183 ? -20.537 -5.520  13.997  1.00 10.15 ? 184 LEU A O    1 
ATOM   1473 C  CB   . LEU A 1 183 ? -20.006 -4.096  11.526  1.00 7.99  ? 184 LEU A CB   1 
ATOM   1474 C  CG   . LEU A 1 183 ? -19.696 -4.037  10.016  1.00 8.50  ? 184 LEU A CG   1 
ATOM   1475 C  CD1  . LEU A 1 183 ? -18.409 -3.284  9.777   1.00 9.21  ? 184 LEU A CD1  1 
ATOM   1476 C  CD2  . LEU A 1 183 ? -19.655 -5.422  9.367   1.00 11.02 ? 184 LEU A CD2  1 
ATOM   1477 N  N    . LEU A 1 184 ? -22.560 -4.505  13.929  1.00 8.84  ? 185 LEU A N    1 
ATOM   1478 C  CA   . LEU A 1 184 ? -22.740 -4.540  15.396  1.00 8.23  ? 185 LEU A CA   1 
ATOM   1479 C  C    . LEU A 1 184 ? -23.441 -5.813  15.879  1.00 9.80  ? 185 LEU A C    1 
ATOM   1480 O  O    . LEU A 1 184 ? -24.398 -6.282  15.249  1.00 11.41 ? 185 LEU A O    1 
ATOM   1481 C  CB   . LEU A 1 184 ? -23.535 -3.314  15.893  1.00 8.29  ? 185 LEU A CB   1 
ATOM   1482 C  CG   . LEU A 1 184 ? -22.951 -1.936  15.544  1.00 7.32  ? 185 LEU A CG   1 
ATOM   1483 C  CD1  . LEU A 1 184 ? -23.867 -0.776  15.941  1.00 9.20  ? 185 LEU A CD1  1 
ATOM   1484 C  CD2  . LEU A 1 184 ? -21.565 -1.764  16.178  1.00 9.41  ? 185 LEU A CD2  1 
ATOM   1485 N  N    . PRO A 1 185 ? -23.010 -6.344  17.025  1.00 9.03  ? 186 PRO A N    1 
ATOM   1486 C  CA   . PRO A 1 185 ? -23.765 -7.480  17.561  1.00 9.46  ? 186 PRO A CA   1 
ATOM   1487 C  C    . PRO A 1 185 ? -25.089 -7.012  18.174  1.00 9.41  ? 186 PRO A C    1 
ATOM   1488 O  O    . PRO A 1 185 ? -25.350 -5.802  18.268  1.00 9.60  ? 186 PRO A O    1 
ATOM   1489 C  CB   . PRO A 1 185 ? -22.833 -8.032  18.646  1.00 9.72  ? 186 PRO A CB   1 
ATOM   1490 C  CG   . PRO A 1 185 ? -22.080 -6.841  19.132  1.00 7.71  ? 186 PRO A CG   1 
ATOM   1491 C  CD   . PRO A 1 185 ? -21.870 -5.961  17.882  1.00 8.99  ? 186 PRO A CD   1 
ATOM   1492 N  N    . GLU A 1 186 ? -25.901 -7.958  18.641  1.00 9.88  ? 187 GLU A N    1 
ATOM   1493 C  CA   . GLU A 1 186 ? -27.174 -7.601  19.254  1.00 10.66 ? 187 GLU A CA   1 
ATOM   1494 C  C    . GLU A 1 186 ? -26.995 -6.835  20.576  1.00 9.91  ? 187 GLU A C    1 
ATOM   1495 O  O    . GLU A 1 186 ? -27.654 -5.812  20.807  1.00 10.50 ? 187 GLU A O    1 
ATOM   1496 C  CB   . GLU A 1 186 ? -28.007 -8.873  19.445  1.00 10.63 ? 187 GLU A CB   1 
ATOM   1497 C  CG   . GLU A 1 186 ? -29.110 -8.758  20.461  1.00 13.80 ? 187 GLU A CG   1 
ATOM   1498 C  CD   . GLU A 1 186 ? -29.799 -10.093 20.749  1.00 12.84 ? 187 GLU A CD   1 
ATOM   1499 O  OE1  . GLU A 1 186 ? -29.621 -11.043 19.956  1.00 13.88 ? 187 GLU A OE1  1 
ATOM   1500 O  OE2  . GLU A 1 186 ? -30.524 -10.167 21.775  1.00 18.19 ? 187 GLU A OE2  1 
ATOM   1501 N  N    . SER A 1 187 ? -26.104 -7.323  21.440  1.00 8.96  ? 188 SER A N    1 
ATOM   1502 C  CA   . SER A 1 187 ? -25.872 -6.712  22.757  1.00 8.81  ? 188 SER A CA   1 
ATOM   1503 C  C    . SER A 1 187 ? -24.730 -5.710  22.729  1.00 8.73  ? 188 SER A C    1 
ATOM   1504 O  O    . SER A 1 187 ? -23.721 -5.960  22.072  1.00 8.78  ? 188 SER A O    1 
ATOM   1505 C  CB   . SER A 1 187 ? -25.532 -7.794  23.786  1.00 9.65  ? 188 SER A CB   1 
ATOM   1506 O  OG   . SER A 1 187 ? -25.328 -7.209  25.062  1.00 8.60  ? 188 SER A OG   1 
ATOM   1507 N  N    . LEU A 1 188 ? -24.885 -4.613  23.465  1.00 8.03  ? 189 LEU A N    1 
ATOM   1508 C  CA   . LEU A 1 188 ? -23.801 -3.628  23.665  1.00 8.93  ? 189 LEU A CA   1 
ATOM   1509 C  C    . LEU A 1 188 ? -23.138 -3.719  25.058  1.00 8.08  ? 189 LEU A C    1 
ATOM   1510 O  O    . LEU A 1 188 ? -22.463 -2.769  25.496  1.00 8.91  ? 189 LEU A O    1 
ATOM   1511 C  CB   . LEU A 1 188 ? -24.331 -2.207  23.414  1.00 9.07  ? 189 LEU A CB   1 
ATOM   1512 C  CG   . LEU A 1 188 ? -24.814 -1.836  22.006  1.00 10.92 ? 189 LEU A CG   1 
ATOM   1513 C  CD1  . LEU A 1 188 ? -25.254 -0.367  21.988  1.00 12.70 ? 189 LEU A CD1  1 
ATOM   1514 C  CD2  . LEU A 1 188 ? -23.745 -2.090  20.933  1.00 13.44 ? 189 LEU A CD2  1 
ATOM   1515 N  N    . ASP A 1 189 ? -23.318 -4.847  25.754  1.00 8.39  ? 190 ASP A N    1 
ATOM   1516 C  CA   . ASP A 1 189 ? -22.567 -5.104  26.986  1.00 7.34  ? 190 ASP A CA   1 
ATOM   1517 C  C    . ASP A 1 189 ? -21.068 -5.019  26.641  1.00 6.72  ? 190 ASP A C    1 
ATOM   1518 O  O    . ASP A 1 189 ? -20.632 -5.513  25.584  1.00 5.47  ? 190 ASP A O    1 
ATOM   1519 C  CB   . ASP A 1 189 ? -22.878 -6.496  27.561  1.00 8.56  ? 190 ASP A CB   1 
ATOM   1520 C  CG   . ASP A 1 189 ? -24.288 -6.610  28.158  1.00 11.07 ? 190 ASP A CG   1 
ATOM   1521 O  OD1  . ASP A 1 189 ? -24.952 -5.585  28.381  1.00 14.43 ? 190 ASP A OD1  1 
ATOM   1522 O  OD2  . ASP A 1 189 ? -24.724 -7.757  28.405  1.00 16.89 ? 190 ASP A OD2  1 
ATOM   1523 N  N    . TYR A 1 190 ? -20.279 -4.418  27.532  1.00 6.02  ? 191 TYR A N    1 
ATOM   1524 C  CA   . TYR A 1 190 ? -18.865 -4.170  27.234  1.00 5.39  ? 191 TYR A CA   1 
ATOM   1525 C  C    . TYR A 1 190 ? -17.938 -4.205  28.452  1.00 5.60  ? 191 TYR A C    1 
ATOM   1526 O  O    . TYR A 1 190 ? -18.370 -4.075  29.610  1.00 6.25  ? 191 TYR A O    1 
ATOM   1527 C  CB   . TYR A 1 190 ? -18.692 -2.809  26.535  1.00 6.07  ? 191 TYR A CB   1 
ATOM   1528 C  CG   . TYR A 1 190 ? -19.092 -1.635  27.408  1.00 6.50  ? 191 TYR A CG   1 
ATOM   1529 C  CD1  . TYR A 1 190 ? -18.162 -1.008  28.261  1.00 6.96  ? 191 TYR A CD1  1 
ATOM   1530 C  CD2  . TYR A 1 190 ? -20.391 -1.139  27.378  1.00 5.63  ? 191 TYR A CD2  1 
ATOM   1531 C  CE1  . TYR A 1 190 ? -18.541 0.063   29.074  1.00 7.22  ? 191 TYR A CE1  1 
ATOM   1532 C  CE2  . TYR A 1 190 ? -20.775 -0.060  28.175  1.00 7.87  ? 191 TYR A CE2  1 
ATOM   1533 C  CZ   . TYR A 1 190 ? -19.851 0.537   29.016  1.00 8.21  ? 191 TYR A CZ   1 
ATOM   1534 O  OH   . TYR A 1 190 ? -20.252 1.584   29.808  1.00 8.68  ? 191 TYR A OH   1 
ATOM   1535 N  N    . TRP A 1 191 ? -16.657 -4.373  28.159  1.00 5.50  ? 192 TRP A N    1 
ATOM   1536 C  CA   . TRP A 1 191 ? -15.578 -4.128  29.125  1.00 4.92  ? 192 TRP A CA   1 
ATOM   1537 C  C    . TRP A 1 191 ? -14.881 -2.831  28.716  1.00 5.00  ? 192 TRP A C    1 
ATOM   1538 O  O    . TRP A 1 191 ? -14.868 -2.481  27.541  1.00 5.61  ? 192 TRP A O    1 
ATOM   1539 C  CB   . TRP A 1 191 ? -14.550 -5.246  29.081  1.00 5.94  ? 192 TRP A CB   1 
ATOM   1540 C  CG   . TRP A 1 191 ? -15.049 -6.584  29.531  1.00 5.26  ? 192 TRP A CG   1 
ATOM   1541 C  CD1  . TRP A 1 191 ? -15.337 -6.984  30.817  1.00 5.19  ? 192 TRP A CD1  1 
ATOM   1542 C  CD2  . TRP A 1 191 ? -15.309 -7.712  28.688  1.00 6.72  ? 192 TRP A CD2  1 
ATOM   1543 N  NE1  . TRP A 1 191 ? -15.741 -8.313  30.812  1.00 7.49  ? 192 TRP A NE1  1 
ATOM   1544 C  CE2  . TRP A 1 191 ? -15.746 -8.771  29.520  1.00 7.18  ? 192 TRP A CE2  1 
ATOM   1545 C  CE3  . TRP A 1 191 ? -15.221 -7.928  27.308  1.00 5.92  ? 192 TRP A CE3  1 
ATOM   1546 C  CZ2  . TRP A 1 191 ? -16.077 -10.034 29.011  1.00 7.94  ? 192 TRP A CZ2  1 
ATOM   1547 C  CZ3  . TRP A 1 191 ? -15.536 -9.196  26.809  1.00 6.07  ? 192 TRP A CZ3  1 
ATOM   1548 C  CH2  . TRP A 1 191 ? -15.968 -10.221 27.666  1.00 6.85  ? 192 TRP A CH2  1 
ATOM   1549 N  N    . THR A 1 192 ? -14.321 -2.109  29.678  1.00 4.99  ? 193 THR A N    1 
ATOM   1550 C  CA   . THR A 1 192 ? -13.598 -0.879  29.358  1.00 5.08  ? 193 THR A CA   1 
ATOM   1551 C  C    . THR A 1 192 ? -12.343 -0.675  30.226  1.00 5.14  ? 193 THR A C    1 
ATOM   1552 O  O    . THR A 1 192 ? -12.317 -1.068  31.390  1.00 5.87  ? 193 THR A O    1 
ATOM   1553 C  CB   . THR A 1 192 ? -14.527 0.371   29.419  1.00 5.37  ? 193 THR A CB   1 
ATOM   1554 O  OG1  . THR A 1 192 ? -13.801 1.541   29.015  1.00 5.60  ? 193 THR A OG1  1 
ATOM   1555 C  CG2  . THR A 1 192 ? -15.140 0.583   30.841  1.00 4.87  ? 193 THR A CG2  1 
ATOM   1556 N  N    . TYR A 1 193 ? -11.303 -0.083  29.637  1.00 5.29  ? 194 TYR A N    1 
ATOM   1557 C  CA   . TYR A 1 193 ? -10.061 0.187   30.353  1.00 4.64  ? 194 TYR A CA   1 
ATOM   1558 C  C    . TYR A 1 193 ? -9.276  1.227   29.551  1.00 4.71  ? 194 TYR A C    1 
ATOM   1559 O  O    . TYR A 1 193 ? -9.530  1.395   28.347  1.00 3.32  ? 194 TYR A O    1 
ATOM   1560 C  CB   . TYR A 1 193 ? -9.239  -1.103  30.516  1.00 4.89  ? 194 TYR A CB   1 
ATOM   1561 C  CG   . TYR A 1 193 ? -8.541  -1.516  29.246  1.00 4.46  ? 194 TYR A CG   1 
ATOM   1562 C  CD1  . TYR A 1 193 ? -9.222  -2.246  28.242  1.00 3.93  ? 194 TYR A CD1  1 
ATOM   1563 C  CD2  . TYR A 1 193 ? -7.206  -1.164  29.026  1.00 3.12  ? 194 TYR A CD2  1 
ATOM   1564 C  CE1  . TYR A 1 193 ? -8.565  -2.629  27.059  1.00 4.38  ? 194 TYR A CE1  1 
ATOM   1565 C  CE2  . TYR A 1 193 ? -6.552  -1.522  27.831  1.00 4.48  ? 194 TYR A CE2  1 
ATOM   1566 C  CZ   . TYR A 1 193 ? -7.224  -2.243  26.875  1.00 4.28  ? 194 TYR A CZ   1 
ATOM   1567 O  OH   . TYR A 1 193 ? -6.565  -2.568  25.712  1.00 4.64  ? 194 TYR A OH   1 
ATOM   1568 N  N    . PRO A 1 194 ? -8.364  1.956   30.217  1.00 4.73  ? 195 PRO A N    1 
ATOM   1569 C  CA   . PRO A 1 194 ? -7.520  2.933   29.524  1.00 4.75  ? 195 PRO A CA   1 
ATOM   1570 C  C    . PRO A 1 194 ? -6.323  2.275   28.847  1.00 5.05  ? 195 PRO A C    1 
ATOM   1571 O  O    . PRO A 1 194 ? -5.623  1.497   29.492  1.00 5.08  ? 195 PRO A O    1 
ATOM   1572 C  CB   . PRO A 1 194 ? -7.038  3.848   30.659  1.00 5.29  ? 195 PRO A CB   1 
ATOM   1573 C  CG   . PRO A 1 194 ? -7.031  2.970   31.875  1.00 4.49  ? 195 PRO A CG   1 
ATOM   1574 C  CD   . PRO A 1 194 ? -8.147  1.963   31.680  1.00 5.13  ? 195 PRO A CD   1 
ATOM   1575 N  N    . GLY A 1 195 ? -6.092  2.611   27.576  1.00 4.08  ? 196 GLY A N    1 
ATOM   1576 C  CA   . GLY A 1 195 ? -5.008  1.971   26.829  1.00 4.41  ? 196 GLY A CA   1 
ATOM   1577 C  C    . GLY A 1 195 ? -4.412  2.839   25.750  1.00 4.32  ? 196 GLY A C    1 
ATOM   1578 O  O    . GLY A 1 195 ? -4.332  4.070   25.881  1.00 4.28  ? 196 GLY A O    1 
ATOM   1579 N  N    . SER A 1 196 ? -3.989  2.183   24.679  1.00 4.32  ? 197 SER A N    1 
ATOM   1580 C  CA   . SER A 1 196 ? -3.189  2.846   23.640  1.00 4.14  ? 197 SER A CA   1 
ATOM   1581 C  C    . SER A 1 196 ? -3.611  2.432   22.245  1.00 3.78  ? 197 SER A C    1 
ATOM   1582 O  O    . SER A 1 196 ? -4.374  1.482   22.072  1.00 4.06  ? 197 SER A O    1 
ATOM   1583 C  CB   . SER A 1 196 ? -1.714  2.437   23.789  1.00 4.26  ? 197 SER A CB   1 
ATOM   1584 O  OG   . SER A 1 196 ? -1.550  1.077   23.371  1.00 3.76  ? 197 SER A OG   1 
ATOM   1585 N  N    . LEU A 1 197 ? -3.066  3.120   21.242  1.00 3.69  ? 198 LEU A N    1 
ATOM   1586 C  CA   . LEU A 1 197 ? -3.077  2.586   19.871  1.00 4.07  ? 198 LEU A CA   1 
ATOM   1587 C  C    . LEU A 1 197 ? -2.343  1.253   19.888  1.00 3.93  ? 198 LEU A C    1 
ATOM   1588 O  O    . LEU A 1 197 ? -1.332  1.103   20.608  1.00 4.14  ? 198 LEU A O    1 
ATOM   1589 C  CB   . LEU A 1 197 ? -2.355  3.548   18.935  1.00 4.68  ? 198 LEU A CB   1 
ATOM   1590 C  CG   . LEU A 1 197 ? -2.871  4.981   18.828  1.00 4.82  ? 198 LEU A CG   1 
ATOM   1591 C  CD1  . LEU A 1 197 ? -2.017  5.737   17.807  1.00 7.16  ? 198 LEU A CD1  1 
ATOM   1592 C  CD2  . LEU A 1 197 ? -4.341  5.045   18.426  1.00 6.03  ? 198 LEU A CD2  1 
ATOM   1593 N  N    . THR A 1 198 ? -2.809  0.290   19.092  1.00 3.51  ? 199 THR A N    1 
ATOM   1594 C  CA   . THR A 1 198 ? -2.128  -1.028  19.034  1.00 3.54  ? 199 THR A CA   1 
ATOM   1595 C  C    . THR A 1 198 ? -1.117  -1.141  17.884  1.00 4.27  ? 199 THR A C    1 
ATOM   1596 O  O    . THR A 1 198 ? -0.531  -2.207  17.692  1.00 4.64  ? 199 THR A O    1 
ATOM   1597 C  CB   . THR A 1 198 ? -3.144  -2.200  18.924  1.00 4.04  ? 199 THR A CB   1 
ATOM   1598 O  OG1  . THR A 1 198 ? -3.786  -2.150  17.647  1.00 3.56  ? 199 THR A OG1  1 
ATOM   1599 C  CG2  . THR A 1 198 ? -4.164  -2.144  20.044  1.00 4.05  ? 199 THR A CG2  1 
ATOM   1600 N  N    . THR A 1 199 ? -0.965  -0.074  17.091  1.00 4.49  ? 200 THR A N    1 
ATOM   1601 C  CA   . THR A 1 199 ? 0.127   0.010   16.119  1.00 5.43  ? 200 THR A CA   1 
ATOM   1602 C  C    . THR A 1 199 ? 0.949   1.254   16.417  1.00 5.73  ? 200 THR A C    1 
ATOM   1603 O  O    . THR A 1 199 ? 0.453   2.204   17.048  1.00 5.47  ? 200 THR A O    1 
ATOM   1604 C  CB   . THR A 1 199 ? -0.385  0.086   14.666  1.00 5.71  ? 200 THR A CB   1 
ATOM   1605 O  OG1  . THR A 1 199 ? -1.256  1.214   14.499  1.00 8.43  ? 200 THR A OG1  1 
ATOM   1606 C  CG2  . THR A 1 199 ? -1.126  -1.147  14.291  1.00 5.93  ? 200 THR A CG2  1 
ATOM   1607 N  N    . PRO A 1 200 ? 2.210   1.270   15.950  1.00 6.52  ? 201 PRO A N    1 
ATOM   1608 C  CA   . PRO A 1 200 ? 2.961   2.524   16.034  1.00 6.74  ? 201 PRO A CA   1 
ATOM   1609 C  C    . PRO A 1 200 ? 2.129   3.699   15.500  1.00 7.18  ? 201 PRO A C    1 
ATOM   1610 O  O    . PRO A 1 200 ? 1.438   3.566   14.467  1.00 8.19  ? 201 PRO A O    1 
ATOM   1611 C  CB   . PRO A 1 200 ? 4.179   2.232   15.145  1.00 6.56  ? 201 PRO A CB   1 
ATOM   1612 C  CG   . PRO A 1 200 ? 4.436   0.766   15.415  1.00 6.05  ? 201 PRO A CG   1 
ATOM   1613 C  CD   . PRO A 1 200 ? 3.023   0.175   15.393  1.00 6.35  ? 201 PRO A CD   1 
ATOM   1614 N  N    . PRO A 1 201 ? 2.214   4.874   16.153  1.00 7.58  ? 202 PRO A N    1 
ATOM   1615 C  CA   . PRO A 1 201 ? 3.091   5.253   17.271  1.00 7.09  ? 202 PRO A CA   1 
ATOM   1616 C  C    . PRO A 1 201 ? 2.717   4.828   18.703  1.00 6.48  ? 202 PRO A C    1 
ATOM   1617 O  O    . PRO A 1 201 ? 3.362   5.283   19.656  1.00 5.98  ? 202 PRO A O    1 
ATOM   1618 C  CB   . PRO A 1 201 ? 3.123   6.791   17.170  1.00 7.40  ? 202 PRO A CB   1 
ATOM   1619 C  CG   . PRO A 1 201 ? 1.820   7.146   16.583  1.00 8.56  ? 202 PRO A CG   1 
ATOM   1620 C  CD   . PRO A 1 201 ? 1.450   6.032   15.640  1.00 7.73  ? 202 PRO A CD   1 
ATOM   1621 N  N    . LEU A 1 202 ? 1.720   3.945   18.853  1.00 5.85  ? 203 LEU A N    1 
ATOM   1622 C  CA   . LEU A 1 202 ? 1.408   3.323   20.151  1.00 4.94  ? 203 LEU A CA   1 
ATOM   1623 C  C    . LEU A 1 202 ? 1.051   4.320   21.250  1.00 5.20  ? 203 LEU A C    1 
ATOM   1624 O  O    . LEU A 1 202 ? 1.278   4.069   22.437  1.00 5.63  ? 203 LEU A O    1 
ATOM   1625 C  CB   . LEU A 1 202 ? 2.549   2.396   20.627  1.00 4.92  ? 203 LEU A CB   1 
ATOM   1626 C  CG   . LEU A 1 202 ? 2.931   1.276   19.653  1.00 4.16  ? 203 LEU A CG   1 
ATOM   1627 C  CD1  . LEU A 1 202 ? 4.243   0.642   20.092  1.00 5.21  ? 203 LEU A CD1  1 
ATOM   1628 C  CD2  . LEU A 1 202 ? 1.841   0.223   19.589  1.00 6.56  ? 203 LEU A CD2  1 
ATOM   1629 N  N    . LEU A 1 203 ? 0.468   5.436   20.843  1.00 5.23  ? 204 LEU A N    1 
ATOM   1630 C  CA   . LEU A 1 203 ? 0.191   6.539   21.757  1.00 5.58  ? 204 LEU A CA   1 
ATOM   1631 C  C    . LEU A 1 203 ? -0.845  6.172   22.797  1.00 5.66  ? 204 LEU A C    1 
ATOM   1632 O  O    . LEU A 1 203 ? -1.823  5.484   22.502  1.00 6.08  ? 204 LEU A O    1 
ATOM   1633 C  CB   . LEU A 1 203 ? -0.250  7.792   20.988  1.00 5.97  ? 204 LEU A CB   1 
ATOM   1634 C  CG   . LEU A 1 203 ? 0.836   8.357   20.051  1.00 7.00  ? 204 LEU A CG   1 
ATOM   1635 C  CD1  . LEU A 1 203 ? 0.227   9.431   19.133  1.00 9.18  ? 204 LEU A CD1  1 
ATOM   1636 C  CD2  . LEU A 1 203 ? 2.041   8.888   20.844  1.00 8.91  ? 204 LEU A CD2  1 
ATOM   1637 N  N    . GLU A 1 204 ? -0.630  6.668   24.009  1.00 5.55  ? 205 GLU A N    1 
ATOM   1638 C  CA   . GLU A 1 204 ? -1.468  6.297   25.148  1.00 5.28  ? 205 GLU A CA   1 
ATOM   1639 C  C    . GLU A 1 204 ? -2.657  7.234   25.305  1.00 5.67  ? 205 GLU A C    1 
ATOM   1640 O  O    . GLU A 1 204 ? -2.750  8.041   26.261  1.00 6.29  ? 205 GLU A O    1 
ATOM   1641 C  CB   . GLU A 1 204 ? -0.606  6.154   26.403  1.00 5.93  ? 205 GLU A CB   1 
ATOM   1642 C  CG   . GLU A 1 204 ? 0.273   4.892   26.249  1.00 6.00  ? 205 GLU A CG   1 
ATOM   1643 C  CD   . GLU A 1 204 ? 1.191   4.625   27.429  1.00 8.13  ? 205 GLU A CD   1 
ATOM   1644 O  OE1  . GLU A 1 204 ? 1.492   5.567   28.209  1.00 8.86  ? 205 GLU A OE1  1 
ATOM   1645 O  OE2  . GLU A 1 204 ? 1.594   3.454   27.574  1.00 8.41  ? 205 GLU A OE2  1 
ATOM   1646 N  N    . CYS A 1 205 ? -3.576  7.116   24.348  1.00 4.59  ? 206 CYS A N    1 
ATOM   1647 C  CA   . CYS A 1 205 ? -4.634  8.116   24.185  1.00 4.63  ? 206 CYS A CA   1 
ATOM   1648 C  C    . CYS A 1 205 ? -6.018  7.502   24.008  1.00 4.35  ? 206 CYS A C    1 
ATOM   1649 O  O    . CYS A 1 205 ? -6.939  8.205   23.581  1.00 4.53  ? 206 CYS A O    1 
ATOM   1650 C  CB   . CYS A 1 205 ? -4.334  8.993   22.963  1.00 4.78  ? 206 CYS A CB   1 
ATOM   1651 S  SG   . CYS A 1 205 ? -4.292  8.051   21.390  1.00 7.22  ? 206 CYS A SG   1 
ATOM   1652 N  N    . VAL A 1 206 ? -6.175  6.212   24.316  1.00 3.84  ? 207 VAL A N    1 
ATOM   1653 C  CA   . VAL A 1 206 ? -7.426  5.505   23.963  1.00 3.79  ? 207 VAL A CA   1 
ATOM   1654 C  C    . VAL A 1 206 ? -8.215  5.042   25.168  1.00 3.59  ? 207 VAL A C    1 
ATOM   1655 O  O    . VAL A 1 206 ? -7.647  4.419   26.073  1.00 4.88  ? 207 VAL A O    1 
ATOM   1656 C  CB   . VAL A 1 206 ? -7.156  4.253   23.057  1.00 3.98  ? 207 VAL A CB   1 
ATOM   1657 C  CG1  . VAL A 1 206 ? -8.491  3.569   22.652  1.00 4.08  ? 207 VAL A CG1  1 
ATOM   1658 C  CG2  . VAL A 1 206 ? -6.343  4.671   21.799  1.00 4.74  ? 207 VAL A CG2  1 
ATOM   1659 N  N    . THR A 1 207 ? -9.518  5.351   25.190  1.00 3.45  ? 208 THR A N    1 
ATOM   1660 C  CA   . THR A 1 207 ? -10.440 4.654   26.078  1.00 3.32  ? 208 THR A CA   1 
ATOM   1661 C  C    . THR A 1 207 ? -10.957 3.472   25.284  1.00 3.79  ? 208 THR A C    1 
ATOM   1662 O  O    . THR A 1 207 ? -11.660 3.659   24.272  1.00 3.21  ? 208 THR A O    1 
ATOM   1663 C  CB   . THR A 1 207 ? -11.621 5.529   26.548  1.00 4.07  ? 208 THR A CB   1 
ATOM   1664 O  OG1  . THR A 1 207 ? -11.113 6.638   27.293  1.00 3.88  ? 208 THR A OG1  1 
ATOM   1665 C  CG2  . THR A 1 207 ? -12.527 4.725   27.455  1.00 3.58  ? 208 THR A CG2  1 
ATOM   1666 N  N    . TRP A 1 208 ? -10.589 2.268   25.717  1.00 4.11  ? 209 TRP A N    1 
ATOM   1667 C  CA   . TRP A 1 208 ? -11.010 1.055   25.008  1.00 3.70  ? 209 TRP A CA   1 
ATOM   1668 C  C    . TRP A 1 208 ? -12.367 0.596   25.500  1.00 4.04  ? 209 TRP A C    1 
ATOM   1669 O  O    . TRP A 1 208 ? -12.601 0.532   26.703  1.00 4.21  ? 209 TRP A O    1 
ATOM   1670 C  CB   . TRP A 1 208 ? -9.982  -0.070  25.192  1.00 4.60  ? 209 TRP A CB   1 
ATOM   1671 C  CG   . TRP A 1 208 ? -8.900  0.044   24.190  1.00 3.57  ? 209 TRP A CG   1 
ATOM   1672 C  CD1  . TRP A 1 208 ? -7.676  0.639   24.363  1.00 4.12  ? 209 TRP A CD1  1 
ATOM   1673 C  CD2  . TRP A 1 208 ? -8.971  -0.354  22.818  1.00 4.13  ? 209 TRP A CD2  1 
ATOM   1674 N  NE1  . TRP A 1 208 ? -6.966  0.600   23.178  1.00 3.86  ? 209 TRP A NE1  1 
ATOM   1675 C  CE2  . TRP A 1 208 ? -7.732  -0.018  22.221  1.00 3.25  ? 209 TRP A CE2  1 
ATOM   1676 C  CE3  . TRP A 1 208 ? -9.943  -1.010  22.047  1.00 4.04  ? 209 TRP A CE3  1 
ATOM   1677 C  CZ2  . TRP A 1 208 ? -7.442  -0.297  20.881  1.00 4.78  ? 209 TRP A CZ2  1 
ATOM   1678 C  CZ3  . TRP A 1 208 ? -9.656  -1.300  20.706  1.00 3.99  ? 209 TRP A CZ3  1 
ATOM   1679 C  CH2  . TRP A 1 208 ? -8.415  -0.940  20.136  1.00 3.84  ? 209 TRP A CH2  1 
ATOM   1680 N  N    . ILE A 1 209 ? -13.245 0.279   24.553  1.00 4.01  ? 210 ILE A N    1 
ATOM   1681 C  CA   . ILE A 1 209 ? -14.569 -0.255  24.864  1.00 4.57  ? 210 ILE A CA   1 
ATOM   1682 C  C    . ILE A 1 209 ? -14.718 -1.526  24.028  1.00 4.52  ? 210 ILE A C    1 
ATOM   1683 O  O    . ILE A 1 209 ? -14.844 -1.440  22.803  1.00 4.54  ? 210 ILE A O    1 
ATOM   1684 C  CB   . ILE A 1 209 ? -15.646 0.771   24.500  1.00 4.95  ? 210 ILE A CB   1 
ATOM   1685 C  CG1  . ILE A 1 209 ? -15.423 2.080   25.271  1.00 5.19  ? 210 ILE A CG1  1 
ATOM   1686 C  CG2  . ILE A 1 209 ? -17.065 0.186   24.711  1.00 5.15  ? 210 ILE A CG2  1 
ATOM   1687 C  CD1  . ILE A 1 209 ? -16.331 3.248   24.761  1.00 5.60  ? 210 ILE A CD1  1 
ATOM   1688 N  N    . VAL A 1 210 ? -14.654 -2.690  24.681  1.00 4.34  ? 211 VAL A N    1 
ATOM   1689 C  CA   . VAL A 1 210 ? -14.648 -3.976  23.972  1.00 3.81  ? 211 VAL A CA   1 
ATOM   1690 C  C    . VAL A 1 210 ? -15.956 -4.694  24.239  1.00 4.20  ? 211 VAL A C    1 
ATOM   1691 O  O    . VAL A 1 210 ? -16.294 -4.972  25.392  1.00 3.48  ? 211 VAL A O    1 
ATOM   1692 C  CB   . VAL A 1 210 ? -13.433 -4.875  24.400  1.00 4.32  ? 211 VAL A CB   1 
ATOM   1693 C  CG1  . VAL A 1 210 ? -13.464 -6.235  23.686  1.00 3.97  ? 211 VAL A CG1  1 
ATOM   1694 C  CG2  . VAL A 1 210 ? -12.109 -4.147  24.116  1.00 3.53  ? 211 VAL A CG2  1 
ATOM   1695 N  N    . LEU A 1 211 ? -16.702 -4.961  23.172  1.00 4.28  ? 212 LEU A N    1 
ATOM   1696 C  CA   . LEU A 1 211 ? -17.984 -5.640  23.308  1.00 4.74  ? 212 LEU A CA   1 
ATOM   1697 C  C    . LEU A 1 211 ? -17.798 -7.102  23.670  1.00 5.13  ? 212 LEU A C    1 
ATOM   1698 O  O    . LEU A 1 211 ? -16.904 -7.769  23.147  1.00 6.06  ? 212 LEU A O    1 
ATOM   1699 C  CB   . LEU A 1 211 ? -18.790 -5.537  22.010  1.00 4.88  ? 212 LEU A CB   1 
ATOM   1700 C  CG   . LEU A 1 211 ? -19.182 -4.131  21.578  1.00 5.52  ? 212 LEU A CG   1 
ATOM   1701 C  CD1  . LEU A 1 211 ? -20.212 -4.197  20.420  1.00 7.55  ? 212 LEU A CD1  1 
ATOM   1702 C  CD2  . LEU A 1 211 ? -19.727 -3.267  22.739  1.00 5.41  ? 212 LEU A CD2  1 
ATOM   1703 N  N    . LYS A 1 212 ? -18.662 -7.592  24.560  1.00 5.57  ? 213 LYS A N    1 
ATOM   1704 C  CA   . LYS A 1 212 ? -18.615 -8.991  24.998  1.00 6.81  ? 213 LYS A CA   1 
ATOM   1705 C  C    . LYS A 1 212 ? -19.110 -9.967  23.935  1.00 6.82  ? 213 LYS A C    1 
ATOM   1706 O  O    . LYS A 1 212 ? -18.560 -11.062 23.795  1.00 7.71  ? 213 LYS A O    1 
ATOM   1707 C  CB   . LYS A 1 212 ? -19.389 -9.187  26.315  1.00 7.92  ? 213 LYS A CB   1 
ATOM   1708 C  CG   . LYS A 1 212 ? -19.457 -10.658 26.765  1.00 8.63  ? 213 LYS A CG   1 
ATOM   1709 C  CD   . LYS A 1 212 ? -20.243 -10.866 28.052  1.00 10.85 ? 213 LYS A CD   1 
ATOM   1710 C  CE   . LYS A 1 212 ? -20.369 -12.340 28.347  1.00 15.49 ? 213 LYS A CE   1 
ATOM   1711 N  NZ   . LYS A 1 212 ? -20.718 -12.605 29.771  1.00 20.92 ? 213 LYS A NZ   1 
ATOM   1712 N  N    . GLU A 1 213 ? -20.148 -9.582  23.204  1.00 5.98  ? 214 GLU A N    1 
ATOM   1713 C  CA   . GLU A 1 213 ? -20.738 -10.454 22.177  1.00 7.14  ? 214 GLU A CA   1 
ATOM   1714 C  C    . GLU A 1 213 ? -19.988 -10.360 20.848  1.00 6.16  ? 214 GLU A C    1 
ATOM   1715 O  O    . GLU A 1 213 ? -19.930 -9.283  20.253  1.00 6.16  ? 214 GLU A O    1 
ATOM   1716 C  CB   . GLU A 1 213 ? -22.222 -10.124 21.958  1.00 6.98  ? 214 GLU A CB   1 
ATOM   1717 C  CG   . GLU A 1 213 ? -22.848 -11.054 20.934  1.00 10.04 ? 214 GLU A CG   1 
ATOM   1718 C  CD   . GLU A 1 213 ? -24.347 -10.878 20.750  1.00 10.70 ? 214 GLU A CD   1 
ATOM   1719 O  OE1  . GLU A 1 213 ? -24.964 -9.994  21.378  1.00 11.70 ? 214 GLU A OE1  1 
ATOM   1720 O  OE2  . GLU A 1 213 ? -24.910 -11.695 19.984  1.00 19.01 ? 214 GLU A OE2  1 
ATOM   1721 N  N    . PRO A 1 214 ? -19.403 -11.479 20.381  1.00 7.26  ? 215 PRO A N    1 
ATOM   1722 C  CA   . PRO A 1 214 ? -18.766 -11.428 19.069  1.00 7.60  ? 215 PRO A CA   1 
ATOM   1723 C  C    . PRO A 1 214 ? -19.791 -11.448 17.960  1.00 8.42  ? 215 PRO A C    1 
ATOM   1724 O  O    . PRO A 1 214 ? -20.947 -11.883 18.184  1.00 8.98  ? 215 PRO A O    1 
ATOM   1725 C  CB   . PRO A 1 214 ? -17.944 -12.716 19.016  1.00 7.54  ? 215 PRO A CB   1 
ATOM   1726 C  CG   . PRO A 1 214 ? -18.622 -13.653 19.943  1.00 9.94  ? 215 PRO A CG   1 
ATOM   1727 C  CD   . PRO A 1 214 ? -19.290 -12.812 21.010  1.00 7.26  ? 215 PRO A CD   1 
ATOM   1728 N  N    . ILE A 1 215 ? -19.398 -10.967 16.778  1.00 7.93  ? 216 ILE A N    1 
ATOM   1729 C  CA   . ILE A 1 215 ? -20.213 -11.198 15.585  1.00 7.72  ? 216 ILE A CA   1 
ATOM   1730 C  C    . ILE A 1 215 ? -19.706 -12.443 14.858  1.00 7.74  ? 216 ILE A C    1 
ATOM   1731 O  O    . ILE A 1 215 ? -18.539 -12.798 14.981  1.00 7.84  ? 216 ILE A O    1 
ATOM   1732 C  CB   . ILE A 1 215 ? -20.224 -9.984  14.606  1.00 7.43  ? 216 ILE A CB   1 
ATOM   1733 C  CG1  . ILE A 1 215 ? -18.809 -9.651  14.095  1.00 7.17  ? 216 ILE A CG1  1 
ATOM   1734 C  CG2  . ILE A 1 215 ? -20.896 -8.759  15.280  1.00 9.02  ? 216 ILE A CG2  1 
ATOM   1735 C  CD1  . ILE A 1 215 ? -18.796 -8.637  12.887  1.00 7.75  ? 216 ILE A CD1  1 
ATOM   1736 N  N    . SER A 1 216 ? -20.597 -13.101 14.116  1.00 8.33  ? 217 SER A N    1 
ATOM   1737 C  CA   . SER A 1 216 ? -20.217 -14.267 13.319  1.00 9.30  ? 217 SER A CA   1 
ATOM   1738 C  C    . SER A 1 216 ? -19.998 -13.843 11.879  1.00 8.60  ? 217 SER A C    1 
ATOM   1739 O  O    . SER A 1 216 ? -20.826 -13.123 11.336  1.00 9.00  ? 217 SER A O    1 
ATOM   1740 C  CB   . SER A 1 216 ? -21.334 -15.313 13.373  1.00 10.07 ? 217 SER A CB   1 
ATOM   1741 O  OG   . SER A 1 216 ? -21.278 -16.022 14.591  1.00 14.87 ? 217 SER A OG   1 
ATOM   1742 N  N    . VAL A 1 217 ? -18.876 -14.265 11.290  1.00 8.09  ? 218 VAL A N    1 
ATOM   1743 C  CA   . VAL A 1 217 ? -18.600 -14.095 9.860   1.00 8.23  ? 218 VAL A CA   1 
ATOM   1744 C  C    . VAL A 1 217 ? -18.313 -15.475 9.272   1.00 8.33  ? 218 VAL A C    1 
ATOM   1745 O  O    . VAL A 1 217 ? -17.990 -16.404 10.004  1.00 8.67  ? 218 VAL A O    1 
ATOM   1746 C  CB   . VAL A 1 217 ? -17.416 -13.139 9.595   1.00 7.55  ? 218 VAL A CB   1 
ATOM   1747 C  CG1  . VAL A 1 217 ? -17.672 -11.801 10.300  1.00 7.19  ? 218 VAL A CG1  1 
ATOM   1748 C  CG2  . VAL A 1 217 ? -16.082 -13.745 10.037  1.00 9.23  ? 218 VAL A CG2  1 
ATOM   1749 N  N    . SER A 1 218 ? -18.431 -15.632 7.959   1.00 8.78  ? 219 SER A N    1 
ATOM   1750 C  CA   . SER A 1 218 ? -18.218 -16.970 7.400   1.00 8.86  ? 219 SER A CA   1 
ATOM   1751 C  C    . SER A 1 218 ? -16.750 -17.237 7.098   1.00 9.32  ? 219 SER A C    1 
ATOM   1752 O  O    . SER A 1 218 ? -15.936 -16.314 6.996   1.00 8.41  ? 219 SER A O    1 
ATOM   1753 C  CB   . SER A 1 218 ? -19.063 -17.190 6.150   1.00 8.66  ? 219 SER A CB   1 
ATOM   1754 O  OG   . SER A 1 218 ? -18.595 -16.362 5.109   1.00 9.70  ? 219 SER A OG   1 
ATOM   1755 N  N    A SER A 1 219 ? -16.413 -18.517 6.969   0.50 9.46  ? 220 SER A N    1 
ATOM   1756 N  N    B SER A 1 219 ? -16.418 -18.515 6.958   0.50 9.48  ? 220 SER A N    1 
ATOM   1757 C  CA   A SER A 1 219 ? -15.074 -18.919 6.558   0.50 10.16 ? 220 SER A CA   1 
ATOM   1758 C  CA   B SER A 1 219 ? -15.079 -18.909 6.564   0.50 10.19 ? 220 SER A CA   1 
ATOM   1759 C  C    A SER A 1 219 ? -14.671 -18.215 5.259   0.50 10.21 ? 220 SER A C    1 
ATOM   1760 C  C    B SER A 1 219 ? -14.671 -18.217 5.259   0.50 10.23 ? 220 SER A C    1 
ATOM   1761 O  O    A SER A 1 219 ? -13.568 -17.667 5.163   0.50 10.35 ? 220 SER A O    1 
ATOM   1762 O  O    B SER A 1 219 ? -13.564 -17.678 5.160   0.50 10.37 ? 220 SER A O    1 
ATOM   1763 C  CB   A SER A 1 219 ? -14.991 -20.438 6.405   0.50 10.02 ? 220 SER A CB   1 
ATOM   1764 C  CB   B SER A 1 219 ? -14.983 -20.426 6.436   0.50 10.05 ? 220 SER A CB   1 
ATOM   1765 O  OG   A SER A 1 219 ? -15.944 -20.904 5.468   0.50 10.58 ? 220 SER A OG   1 
ATOM   1766 O  OG   B SER A 1 219 ? -13.631 -20.831 6.435   0.50 10.76 ? 220 SER A OG   1 
ATOM   1767 N  N    . GLU A 1 220 ? -15.576 -18.196 4.280   1.00 10.65 ? 221 GLU A N    1 
ATOM   1768 C  CA   . GLU A 1 220 ? -15.318 -17.531 2.996   1.00 11.07 ? 221 GLU A CA   1 
ATOM   1769 C  C    . GLU A 1 220 ? -15.032 -16.027 3.150   1.00 10.78 ? 221 GLU A C    1 
ATOM   1770 O  O    . GLU A 1 220 ? -14.165 -15.480 2.453   1.00 11.24 ? 221 GLU A O    1 
ATOM   1771 C  CB   . GLU A 1 220 ? -16.473 -17.754 2.026   1.00 12.08 ? 221 GLU A CB   1 
ATOM   1772 C  CG   . GLU A 1 220 ? -16.676 -19.234 1.621   1.00 14.45 ? 221 GLU A CG   1 
ATOM   1773 C  CD   . GLU A 1 220 ? -17.545 -20.025 2.586   1.00 18.75 ? 221 GLU A CD   1 
ATOM   1774 O  OE1  . GLU A 1 220 ? -17.997 -19.486 3.621   1.00 19.15 ? 221 GLU A OE1  1 
ATOM   1775 O  OE2  . GLU A 1 220 ? -17.782 -21.215 2.306   1.00 21.02 ? 221 GLU A OE2  1 
ATOM   1776 N  N    . GLN A 1 221 ? -15.740 -15.367 4.067   1.00 9.10  ? 222 GLN A N    1 
ATOM   1777 C  CA   . GLN A 1 221 ? -15.518 -13.928 4.285   1.00 9.01  ? 222 GLN A CA   1 
ATOM   1778 C  C    . GLN A 1 221 ? -14.108 -13.654 4.821   1.00 8.96  ? 222 GLN A C    1 
ATOM   1779 O  O    . GLN A 1 221 ? -13.370 -12.826 4.269   1.00 8.88  ? 222 GLN A O    1 
ATOM   1780 C  CB   . GLN A 1 221 ? -16.600 -13.344 5.205   1.00 9.01  ? 222 GLN A CB   1 
ATOM   1781 C  CG   . GLN A 1 221 ? -17.933 -13.157 4.466   1.00 8.85  ? 222 GLN A CG   1 
ATOM   1782 C  CD   . GLN A 1 221 ? -19.068 -12.648 5.341   1.00 8.56  ? 222 GLN A CD   1 
ATOM   1783 O  OE1  . GLN A 1 221 ? -19.190 -13.024 6.502   1.00 7.97  ? 222 GLN A OE1  1 
ATOM   1784 N  NE2  . GLN A 1 221 ? -19.920 -11.794 4.771   1.00 8.61  ? 222 GLN A NE2  1 
ATOM   1785 N  N    . VAL A 1 222 ? -13.705 -14.376 5.866   1.00 9.32  ? 223 VAL A N    1 
ATOM   1786 C  CA   . VAL A 1 222 ? -12.365 -14.166 6.432   1.00 9.82  ? 223 VAL A CA   1 
ATOM   1787 C  C    . VAL A 1 222 ? -11.251 -14.657 5.481   1.00 10.63 ? 223 VAL A C    1 
ATOM   1788 O  O    . VAL A 1 222 ? -10.178 -14.060 5.434   1.00 10.21 ? 223 VAL A O    1 
ATOM   1789 C  CB   . VAL A 1 222 ? -12.234 -14.706 7.895   1.00 10.37 ? 223 VAL A CB   1 
ATOM   1790 C  CG1  . VAL A 1 222 ? -12.311 -16.229 7.935   1.00 11.94 ? 223 VAL A CG1  1 
ATOM   1791 C  CG2  . VAL A 1 222 ? -10.949 -14.208 8.552   1.00 11.64 ? 223 VAL A CG2  1 
ATOM   1792 N  N    . LEU A 1 223 ? -11.527 -15.692 4.684   1.00 11.05 ? 224 LEU A N    1 
ATOM   1793 C  CA   . LEU A 1 223 ? -10.543 -16.156 3.702   1.00 11.79 ? 224 LEU A CA   1 
ATOM   1794 C  C    . LEU A 1 223 ? -10.179 -15.048 2.727   1.00 11.68 ? 224 LEU A C    1 
ATOM   1795 O  O    . LEU A 1 223 ? -9.018  -14.928 2.326   1.00 11.80 ? 224 LEU A O    1 
ATOM   1796 C  CB   . LEU A 1 223 ? -11.028 -17.398 2.950   1.00 12.52 ? 224 LEU A CB   1 
ATOM   1797 C  CG   . LEU A 1 223 ? -10.842 -18.690 3.750   1.00 14.47 ? 224 LEU A CG   1 
ATOM   1798 C  CD1  . LEU A 1 223 ? -11.744 -19.810 3.223   1.00 17.43 ? 224 LEU A CD1  1 
ATOM   1799 C  CD2  . LEU A 1 223 ? -9.375  -19.126 3.788   1.00 15.72 ? 224 LEU A CD2  1 
ATOM   1800 N  N    . LYS A 1 224 ? -11.165 -14.232 2.369   1.00 11.77 ? 225 LYS A N    1 
ATOM   1801 C  CA   . LYS A 1 224 ? -10.934 -13.092 1.487   1.00 11.94 ? 225 LYS A CA   1 
ATOM   1802 C  C    . LYS A 1 224 ? -10.099 -11.979 2.136   1.00 10.47 ? 225 LYS A C    1 
ATOM   1803 O  O    . LYS A 1 224 ? -9.316  -11.330 1.447   1.00 10.40 ? 225 LYS A O    1 
ATOM   1804 C  CB   . LYS A 1 224 ? -12.250 -12.606 0.862   1.00 12.47 ? 225 LYS A CB   1 
ATOM   1805 C  CG   . LYS A 1 224 ? -12.808 -13.660 -0.160  1.00 13.52 ? 225 LYS A CG   1 
ATOM   1806 C  CD   . LYS A 1 224 ? -14.151 -13.289 -0.772  1.00 14.52 ? 225 LYS A CD   1 
ATOM   1807 C  CE   . LYS A 1 224 ? -14.641 -14.399 -1.707  1.00 16.11 ? 225 LYS A CE   1 
ATOM   1808 N  NZ   . LYS A 1 224 ? -15.904 -14.091 -2.431  1.00 17.62 ? 225 LYS A NZ   1 
ATOM   1809 N  N    . PHE A 1 225 ? -10.228 -11.771 3.451   1.00 9.43  ? 226 PHE A N    1 
ATOM   1810 C  CA   . PHE A 1 225 ? -9.303  -10.868 4.160   1.00 8.44  ? 226 PHE A CA   1 
ATOM   1811 C  C    . PHE A 1 225 ? -7.879  -11.340 3.917   1.00 7.83  ? 226 PHE A C    1 
ATOM   1812 O  O    . PHE A 1 225 ? -6.976  -10.542 3.673   1.00 7.88  ? 226 PHE A O    1 
ATOM   1813 C  CB   . PHE A 1 225 ? -9.517  -10.926 5.675   1.00 8.27  ? 226 PHE A CB   1 
ATOM   1814 C  CG   . PHE A 1 225 ? -10.686 -10.119 6.186   1.00 8.13  ? 226 PHE A CG   1 
ATOM   1815 C  CD1  . PHE A 1 225 ? -11.720 -9.694  5.350   1.00 10.35 ? 226 PHE A CD1  1 
ATOM   1816 C  CD2  . PHE A 1 225 ? -10.777 -9.862  7.556   1.00 10.01 ? 226 PHE A CD2  1 
ATOM   1817 C  CE1  . PHE A 1 225 ? -12.819 -8.966  5.873   1.00 10.50 ? 226 PHE A CE1  1 
ATOM   1818 C  CE2  . PHE A 1 225 ? -11.859 -9.150  8.088   1.00 11.55 ? 226 PHE A CE2  1 
ATOM   1819 C  CZ   . PHE A 1 225 ? -12.880 -8.697  7.239   1.00 10.65 ? 226 PHE A CZ   1 
ATOM   1820 N  N    . ARG A 1 226 ? -7.688  -12.654 4.008   1.00 7.77  ? 227 ARG A N    1 
ATOM   1821 C  CA   . ARG A 1 226 ? -6.366  -13.278 3.926   1.00 8.97  ? 227 ARG A CA   1 
ATOM   1822 C  C    . ARG A 1 226 ? -5.757  -13.288 2.524   1.00 8.89  ? 227 ARG A C    1 
ATOM   1823 O  O    . ARG A 1 226 ? -4.620  -13.742 2.349   1.00 9.34  ? 227 ARG A O    1 
ATOM   1824 C  CB   . ARG A 1 226 ? -6.419  -14.720 4.466   1.00 8.92  ? 227 ARG A CB   1 
ATOM   1825 C  CG   . ARG A 1 226 ? -6.791  -14.824 5.950   1.00 8.72  ? 227 ARG A CG   1 
ATOM   1826 C  CD   . ARG A 1 226 ? -6.745  -16.289 6.489   1.00 9.44  ? 227 ARG A CD   1 
ATOM   1827 N  NE   . ARG A 1 226 ? -7.381  -16.370 7.815   1.00 8.41  ? 227 ARG A NE   1 
ATOM   1828 C  CZ   . ARG A 1 226 ? -8.337  -17.233 8.168   1.00 10.39 ? 227 ARG A CZ   1 
ATOM   1829 N  NH1  . ARG A 1 226 ? -8.739  -18.192 7.330   1.00 11.87 ? 227 ARG A NH1  1 
ATOM   1830 N  NH2  . ARG A 1 226 ? -8.849  -17.180 9.392   1.00 9.98  ? 227 ARG A NH2  1 
ATOM   1831 N  N    . LYS A 1 227 ? -6.496  -12.795 1.534   1.00 9.00  ? 228 LYS A N    1 
ATOM   1832 C  CA   . LYS A 1 227 ? -5.966  -12.712 0.165   1.00 9.79  ? 228 LYS A CA   1 
ATOM   1833 C  C    . LYS A 1 227 ? -5.343  -11.359 -0.114  1.00 9.40  ? 228 LYS A C    1 
ATOM   1834 O  O    . LYS A 1 227 ? -4.685  -11.169 -1.144  1.00 9.42  ? 228 LYS A O    1 
ATOM   1835 C  CB   . LYS A 1 227 ? -7.059  -12.973 -0.864  1.00 10.25 ? 228 LYS A CB   1 
ATOM   1836 C  CG   . LYS A 1 227 ? -7.479  -14.425 -0.942  1.00 13.93 ? 228 LYS A CG   1 
ATOM   1837 C  CD   . LYS A 1 227 ? -8.540  -14.608 -2.020  1.00 19.06 ? 228 LYS A CD   1 
ATOM   1838 C  CE   . LYS A 1 227 ? -7.899  -14.745 -3.395  1.00 22.78 ? 228 LYS A CE   1 
ATOM   1839 N  NZ   . LYS A 1 227 ? -8.927  -14.796 -4.470  1.00 25.42 ? 228 LYS A NZ   1 
ATOM   1840 N  N    . LEU A 1 228 ? -5.555  -10.418 0.800   1.00 8.54  ? 229 LEU A N    1 
ATOM   1841 C  CA   . LEU A 1 228 ? -4.879  -9.122  0.732   1.00 8.22  ? 229 LEU A CA   1 
ATOM   1842 C  C    . LEU A 1 228 ? -3.362  -9.251  0.876   1.00 8.52  ? 229 LEU A C    1 
ATOM   1843 O  O    . LEU A 1 228 ? -2.845  -10.279 1.334   1.00 8.56  ? 229 LEU A O    1 
ATOM   1844 C  CB   . LEU A 1 228 ? -5.426  -8.167  1.802   1.00 7.38  ? 229 LEU A CB   1 
ATOM   1845 C  CG   . LEU A 1 228 ? -6.861  -7.684  1.576   1.00 8.58  ? 229 LEU A CG   1 
ATOM   1846 C  CD1  . LEU A 1 228 ? -7.397  -7.114  2.862   1.00 8.42  ? 229 LEU A CD1  1 
ATOM   1847 C  CD2  . LEU A 1 228 ? -6.923  -6.630  0.449   1.00 9.93  ? 229 LEU A CD2  1 
ATOM   1848 N  N    . ASN A 1 229 ? -2.653  -8.203  0.461   1.00 8.96  ? 230 ASN A N    1 
ATOM   1849 C  CA   . ASN A 1 229 ? -1.189  -8.185  0.454   1.00 9.20  ? 230 ASN A CA   1 
ATOM   1850 C  C    . ASN A 1 229 ? -0.623  -7.049  1.339   1.00 9.04  ? 230 ASN A C    1 
ATOM   1851 O  O    . ASN A 1 229 ? -1.135  -5.931  1.283   1.00 8.66  ? 230 ASN A O    1 
ATOM   1852 C  CB   . ASN A 1 229 ? -0.686  -7.915  -0.975  1.00 9.69  ? 230 ASN A CB   1 
ATOM   1853 C  CG   . ASN A 1 229 ? -0.692  -9.143  -1.901  1.00 11.67 ? 230 ASN A CG   1 
ATOM   1854 O  OD1  . ASN A 1 229 ? -0.197  -9.039  -3.043  1.00 12.77 ? 230 ASN A OD1  1 
ATOM   1855 N  ND2  . ASN A 1 229 ? -1.258  -10.279 -1.456  1.00 9.77  ? 230 ASN A ND2  1 
ATOM   1856 N  N    . PHE A 1 230 ? 0.434   -7.324  2.120   1.00 8.58  ? 231 PHE A N    1 
ATOM   1857 C  CA   . PHE A 1 230 ? 1.233   -6.280  2.799   1.00 8.95  ? 231 PHE A CA   1 
ATOM   1858 C  C    . PHE A 1 230 ? 2.094   -5.486  1.826   1.00 9.85  ? 231 PHE A C    1 
ATOM   1859 O  O    . PHE A 1 230 ? 2.417   -4.323  2.070   1.00 9.78  ? 231 PHE A O    1 
ATOM   1860 C  CB   . PHE A 1 230 ? 2.227   -6.883  3.790   1.00 9.63  ? 231 PHE A CB   1 
ATOM   1861 C  CG   . PHE A 1 230 ? 1.618   -7.423  5.068   1.00 9.20  ? 231 PHE A CG   1 
ATOM   1862 C  CD1  . PHE A 1 230 ? 0.800   -6.628  5.884   1.00 8.32  ? 231 PHE A CD1  1 
ATOM   1863 C  CD2  . PHE A 1 230 ? 1.936   -8.714  5.493   1.00 8.40  ? 231 PHE A CD2  1 
ATOM   1864 C  CE1  . PHE A 1 230 ? 0.269   -7.142  7.100   1.00 8.57  ? 231 PHE A CE1  1 
ATOM   1865 C  CE2  . PHE A 1 230 ? 1.428   -9.227  6.695   1.00 8.74  ? 231 PHE A CE2  1 
ATOM   1866 C  CZ   . PHE A 1 230 ? 0.590   -8.447  7.495   1.00 8.81  ? 231 PHE A CZ   1 
ATOM   1867 N  N    . ASN A 1 231 ? 2.510   -6.143  0.753   1.00 10.32 ? 232 ASN A N    1 
ATOM   1868 C  CA   . ASN A 1 231 ? 3.425   -5.523  -0.206  1.00 11.09 ? 232 ASN A CA   1 
ATOM   1869 C  C    . ASN A 1 231 ? 2.691   -4.610  -1.190  1.00 11.55 ? 232 ASN A C    1 
ATOM   1870 O  O    . ASN A 1 231 ? 1.461   -4.689  -1.336  1.00 11.09 ? 232 ASN A O    1 
ATOM   1871 C  CB   . ASN A 1 231 ? 4.124   -6.635  -0.975  1.00 10.81 ? 232 ASN A CB   1 
ATOM   1872 C  CG   . ASN A 1 231 ? 3.135   -7.575  -1.602  1.00 12.01 ? 232 ASN A CG   1 
ATOM   1873 O  OD1  . ASN A 1 231 ? 2.570   -8.434  -0.923  1.00 13.39 ? 232 ASN A OD1  1 
ATOM   1874 N  ND2  . ASN A 1 231 ? 2.877   -7.396  -2.896  1.00 13.84 ? 232 ASN A ND2  1 
ATOM   1875 N  N    . GLY A 1 232 ? 3.452   -3.743  -1.864  1.00 12.03 ? 233 GLY A N    1 
ATOM   1876 C  CA   . GLY A 1 232 ? 2.911   -2.928  -2.957  1.00 13.35 ? 233 GLY A CA   1 
ATOM   1877 C  C    . GLY A 1 232 ? 2.848   -3.695  -4.267  1.00 13.88 ? 233 GLY A C    1 
ATOM   1878 O  O    . GLY A 1 232 ? 3.431   -4.773  -4.396  1.00 14.26 ? 233 GLY A O    1 
ATOM   1879 N  N    . GLU A 1 233 ? 2.139   -3.134  -5.242  1.00 14.40 ? 234 GLU A N    1 
ATOM   1880 C  CA   . GLU A 1 233 ? 2.031   -3.716  -6.581  1.00 15.20 ? 234 GLU A CA   1 
ATOM   1881 C  C    . GLU A 1 233 ? 3.398   -3.967  -7.204  1.00 15.28 ? 234 GLU A C    1 
ATOM   1882 O  O    . GLU A 1 233 ? 4.287   -3.133  -7.100  1.00 15.08 ? 234 GLU A O    1 
ATOM   1883 C  CB   . GLU A 1 233 ? 1.231   -2.782  -7.485  1.00 14.73 ? 234 GLU A CB   1 
ATOM   1884 C  CG   . GLU A 1 233 ? 0.880   -3.364  -8.845  1.00 15.34 ? 234 GLU A CG   1 
ATOM   1885 C  CD   . GLU A 1 233 ? 0.124   -2.384  -9.713  1.00 16.95 ? 234 GLU A CD   1 
ATOM   1886 O  OE1  . GLU A 1 233 ? -0.125  -1.233  -9.257  1.00 17.55 ? 234 GLU A OE1  1 
ATOM   1887 O  OE2  . GLU A 1 233 ? -0.214  -2.760  -10.860 1.00 18.11 ? 234 GLU A OE2  1 
ATOM   1888 N  N    . GLY A 1 234 ? 3.543   -5.118  -7.852  1.00 16.52 ? 235 GLY A N    1 
ATOM   1889 C  CA   . GLY A 1 234 ? 4.791   -5.492  -8.505  1.00 18.41 ? 235 GLY A CA   1 
ATOM   1890 C  C    . GLY A 1 234 ? 5.914   -5.911  -7.566  1.00 19.17 ? 235 GLY A C    1 
ATOM   1891 O  O    . GLY A 1 234 ? 7.077   -6.002  -7.992  1.00 20.25 ? 235 GLY A O    1 
ATOM   1892 N  N    . GLU A 1 235 ? 5.584   -6.150  -6.294  1.00 18.69 ? 236 GLU A N    1 
ATOM   1893 C  CA   . GLU A 1 235 ? 6.542   -6.683  -5.314  1.00 18.69 ? 236 GLU A CA   1 
ATOM   1894 C  C    . GLU A 1 235 ? 6.221   -8.148  -5.013  1.00 18.14 ? 236 GLU A C    1 
ATOM   1895 O  O    . GLU A 1 235 ? 5.111   -8.606  -5.306  1.00 17.83 ? 236 GLU A O    1 
ATOM   1896 C  CB   . GLU A 1 235 ? 6.524   -5.850  -4.027  1.00 18.61 ? 236 GLU A CB   1 
ATOM   1897 C  CG   . GLU A 1 235 ? 6.820   -4.376  -4.277  1.00 19.12 ? 236 GLU A CG   1 
ATOM   1898 C  CD   . GLU A 1 235 ? 6.932   -3.550  -3.009  1.00 20.53 ? 236 GLU A CD   1 
ATOM   1899 O  OE1  . GLU A 1 235 ? 6.334   -3.917  -1.970  1.00 20.23 ? 236 GLU A OE1  1 
ATOM   1900 O  OE2  . GLU A 1 235 ? 7.616   -2.508  -3.058  1.00 23.85 ? 236 GLU A OE2  1 
ATOM   1901 N  N    . PRO A 1 236 ? 7.203   -8.905  -4.475  1.00 17.87 ? 237 PRO A N    1 
ATOM   1902 C  CA   . PRO A 1 236 ? 6.927   -10.294 -4.111  1.00 17.52 ? 237 PRO A CA   1 
ATOM   1903 C  C    . PRO A 1 236 ? 5.778   -10.349 -3.111  1.00 16.56 ? 237 PRO A C    1 
ATOM   1904 O  O    . PRO A 1 236 ? 5.687   -9.496  -2.225  1.00 15.99 ? 237 PRO A O    1 
ATOM   1905 C  CB   . PRO A 1 236 ? 8.229   -10.748 -3.452  1.00 18.11 ? 237 PRO A CB   1 
ATOM   1906 C  CG   . PRO A 1 236 ? 9.278   -9.885  -4.092  1.00 18.03 ? 237 PRO A CG   1 
ATOM   1907 C  CD   . PRO A 1 236 ? 8.605   -8.544  -4.193  1.00 18.42 ? 237 PRO A CD   1 
ATOM   1908 N  N    . GLU A 1 237 ? 4.903   -11.328 -3.285  1.00 15.88 ? 238 GLU A N    1 
ATOM   1909 C  CA   . GLU A 1 237 ? 3.678   -11.370 -2.517  1.00 14.87 ? 238 GLU A CA   1 
ATOM   1910 C  C    . GLU A 1 237 ? 3.912   -11.774 -1.065  1.00 13.98 ? 238 GLU A C    1 
ATOM   1911 O  O    . GLU A 1 237 ? 4.521   -12.821 -0.777  1.00 13.81 ? 238 GLU A O    1 
ATOM   1912 C  CB   . GLU A 1 237 ? 2.622   -12.268 -3.182  1.00 15.33 ? 238 GLU A CB   1 
ATOM   1913 C  CG   . GLU A 1 237 ? 1.234   -12.102 -2.547  1.00 15.81 ? 238 GLU A CG   1 
ATOM   1914 C  CD   . GLU A 1 237 ? 0.183   -13.035 -3.115  1.00 16.41 ? 238 GLU A CD   1 
ATOM   1915 O  OE1  . GLU A 1 237 ? 0.533   -14.194 -3.446  1.00 21.15 ? 238 GLU A OE1  1 
ATOM   1916 O  OE2  . GLU A 1 237 ? -0.996  -12.620 -3.212  1.00 15.11 ? 238 GLU A OE2  1 
ATOM   1917 N  N    A GLU A 1 238 ? 3.430   -10.922 -0.162  0.50 13.09 ? 239 GLU A N    1 
ATOM   1918 N  N    B GLU A 1 238 ? 3.411   -10.931 -0.163  0.50 13.01 ? 239 GLU A N    1 
ATOM   1919 C  CA   A GLU A 1 238 ? 3.397   -11.192 1.271   0.50 12.91 ? 239 GLU A CA   1 
ATOM   1920 C  CA   B GLU A 1 238 ? 3.401   -11.180 1.275   0.50 12.76 ? 239 GLU A CA   1 
ATOM   1921 C  C    A GLU A 1 238 ? 1.936   -11.107 1.665   0.50 11.80 ? 239 GLU A C    1 
ATOM   1922 C  C    B GLU A 1 238 ? 1.947   -11.099 1.708   0.50 11.71 ? 239 GLU A C    1 
ATOM   1923 O  O    A GLU A 1 238 ? 1.359   -10.024 1.650   0.50 11.94 ? 239 GLU A O    1 
ATOM   1924 O  O    B GLU A 1 238 ? 1.385   -10.009 1.762   0.50 11.87 ? 239 GLU A O    1 
ATOM   1925 C  CB   A GLU A 1 238 ? 4.162   -10.131 2.067   0.50 12.53 ? 239 GLU A CB   1 
ATOM   1926 C  CB   B GLU A 1 238 ? 4.193   -10.106 2.027   0.50 12.39 ? 239 GLU A CB   1 
ATOM   1927 C  CG   A GLU A 1 238 ? 5.498   -9.686  1.505   0.50 13.82 ? 239 GLU A CG   1 
ATOM   1928 C  CG   B GLU A 1 238 ? 5.668   -9.999  1.675   0.50 13.77 ? 239 GLU A CG   1 
ATOM   1929 C  CD   A GLU A 1 238 ? 6.014   -8.424  2.183   0.50 14.19 ? 239 GLU A CD   1 
ATOM   1930 C  CD   B GLU A 1 238 ? 6.347   -8.780  2.297   0.50 13.66 ? 239 GLU A CD   1 
ATOM   1931 O  OE1  A GLU A 1 238 ? 6.033   -8.369  3.439   0.50 15.15 ? 239 GLU A OE1  1 
ATOM   1932 O  OE1  B GLU A 1 238 ? 5.650   -7.872  2.820   0.50 15.26 ? 239 GLU A OE1  1 
ATOM   1933 O  OE2  A GLU A 1 238 ? 6.397   -7.483  1.456   0.50 15.65 ? 239 GLU A OE2  1 
ATOM   1934 O  OE2  B GLU A 1 238 ? 7.592   -8.725  2.253   0.50 13.87 ? 239 GLU A OE2  1 
ATOM   1935 N  N    . LEU A 1 239 ? 1.322   -12.240 1.987   1.00 10.77 ? 240 LEU A N    1 
ATOM   1936 C  CA   . LEU A 1 239 ? -0.096  -12.235 2.353   1.00 9.48  ? 240 LEU A CA   1 
ATOM   1937 C  C    . LEU A 1 239 ? -0.311  -11.414 3.623   1.00 8.76  ? 240 LEU A C    1 
ATOM   1938 O  O    . LEU A 1 239 ? 0.484   -11.508 4.580   1.00 8.29  ? 240 LEU A O    1 
ATOM   1939 C  CB   . LEU A 1 239 ? -0.644  -13.657 2.536   1.00 9.56  ? 240 LEU A CB   1 
ATOM   1940 C  CG   . LEU A 1 239 ? -0.667  -14.532 1.271   1.00 9.82  ? 240 LEU A CG   1 
ATOM   1941 C  CD1  . LEU A 1 239 ? -1.104  -15.957 1.640   1.00 12.44 ? 240 LEU A CD1  1 
ATOM   1942 C  CD2  . LEU A 1 239 ? -1.572  -13.952 0.197   1.00 11.03 ? 240 LEU A CD2  1 
ATOM   1943 N  N    . MET A 1 240 ? -1.375  -10.608 3.611   1.00 8.34  ? 241 MET A N    1 
ATOM   1944 C  CA   . MET A 1 240 ? -1.749  -9.794  4.775   1.00 8.06  ? 241 MET A CA   1 
ATOM   1945 C  C    . MET A 1 240 ? -2.486  -10.714 5.732   1.00 7.60  ? 241 MET A C    1 
ATOM   1946 O  O    . MET A 1 240 ? -3.707  -10.874 5.637   1.00 7.39  ? 241 MET A O    1 
ATOM   1947 C  CB   . MET A 1 240 ? -2.619  -8.586  4.376   1.00 8.25  ? 241 MET A CB   1 
ATOM   1948 C  CG   . MET A 1 240 ? -2.874  -7.575  5.529   1.00 8.40  ? 241 MET A CG   1 
ATOM   1949 S  SD   . MET A 1 240 ? -3.880  -6.193  4.991   1.00 9.11  ? 241 MET A SD   1 
ATOM   1950 C  CE   . MET A 1 240 ? -2.627  -5.097  4.329   1.00 9.32  ? 241 MET A CE   1 
ATOM   1951 N  N    . VAL A 1 241 ? -1.714  -11.315 6.640   1.00 7.02  ? 242 VAL A N    1 
ATOM   1952 C  CA   . VAL A 1 241 ? -2.259  -12.169 7.710   1.00 6.86  ? 242 VAL A CA   1 
ATOM   1953 C  C    . VAL A 1 241 ? -1.465  -11.900 8.998   1.00 7.11  ? 242 VAL A C    1 
ATOM   1954 O  O    . VAL A 1 241 ? -0.316  -11.443 8.950   1.00 7.23  ? 242 VAL A O    1 
ATOM   1955 C  CB   . VAL A 1 241 ? -2.196  -13.682 7.364   1.00 6.67  ? 242 VAL A CB   1 
ATOM   1956 C  CG1  . VAL A 1 241 ? -3.057  -14.008 6.109   1.00 7.75  ? 242 VAL A CG1  1 
ATOM   1957 C  CG2  . VAL A 1 241 ? -0.755  -14.148 7.183   1.00 7.29  ? 242 VAL A CG2  1 
ATOM   1958 N  N    . ASP A 1 242 ? -2.071  -12.221 10.140  1.00 5.74  ? 243 ASP A N    1 
ATOM   1959 C  CA   . ASP A 1 242 ? -1.419  -12.070 11.430  1.00 5.90  ? 243 ASP A CA   1 
ATOM   1960 C  C    . ASP A 1 242 ? -0.946  -10.635 11.675  1.00 5.38  ? 243 ASP A C    1 
ATOM   1961 O  O    . ASP A 1 242 ? 0.159   -10.400 12.171  1.00 6.01  ? 243 ASP A O    1 
ATOM   1962 C  CB   . ASP A 1 242 ? -0.311  -13.114 11.646  1.00 5.24  ? 243 ASP A CB   1 
ATOM   1963 C  CG   . ASP A 1 242 ? -0.860  -14.539 11.730  1.00 8.25  ? 243 ASP A CG   1 
ATOM   1964 O  OD1  . ASP A 1 242 ? -1.892  -14.716 12.396  1.00 6.90  ? 243 ASP A OD1  1 
ATOM   1965 O  OD2  . ASP A 1 242 ? -0.262  -15.476 11.120  1.00 8.34  ? 243 ASP A OD2  1 
ATOM   1966 N  N    . ASN A 1 243 ? -1.828  -9.687  11.355  1.00 5.17  ? 244 ASN A N    1 
ATOM   1967 C  CA   . ASN A 1 243 ? -1.555  -8.264  11.599  1.00 4.96  ? 244 ASN A CA   1 
ATOM   1968 C  C    . ASN A 1 243 ? -2.147  -7.814  12.948  1.00 5.10  ? 244 ASN A C    1 
ATOM   1969 O  O    . ASN A 1 243 ? -2.831  -6.774  13.036  1.00 5.42  ? 244 ASN A O    1 
ATOM   1970 C  CB   . ASN A 1 243 ? -2.078  -7.413  10.436  1.00 4.72  ? 244 ASN A CB   1 
ATOM   1971 C  CG   . ASN A 1 243 ? -3.570  -7.571  10.221  1.00 6.04  ? 244 ASN A CG   1 
ATOM   1972 O  OD1  . ASN A 1 243 ? -4.213  -8.421  10.837  1.00 5.61  ? 244 ASN A OD1  1 
ATOM   1973 N  ND2  . ASN A 1 243 ? -4.136  -6.728  9.355   1.00 8.38  ? 244 ASN A ND2  1 
ATOM   1974 N  N    . TRP A 1 244 ? -1.865  -8.605  13.986  1.00 5.21  ? 245 TRP A N    1 
ATOM   1975 C  CA   . TRP A 1 244 ? -2.307  -8.335  15.345  1.00 5.02  ? 245 TRP A CA   1 
ATOM   1976 C  C    . TRP A 1 244 ? -1.123  -8.213  16.297  1.00 5.23  ? 245 TRP A C    1 
ATOM   1977 O  O    . TRP A 1 244 ? -0.104  -8.893  16.129  1.00 6.07  ? 245 TRP A O    1 
ATOM   1978 C  CB   . TRP A 1 244 ? -3.268  -9.434  15.835  1.00 5.07  ? 245 TRP A CB   1 
ATOM   1979 C  CG   . TRP A 1 244 ? -2.787  -10.859 15.651  1.00 5.19  ? 245 TRP A CG   1 
ATOM   1980 C  CD1  . TRP A 1 244 ? -2.850  -11.605 14.511  1.00 6.11  ? 245 TRP A CD1  1 
ATOM   1981 C  CD2  . TRP A 1 244 ? -2.201  -11.703 16.654  1.00 6.64  ? 245 TRP A CD2  1 
ATOM   1982 N  NE1  . TRP A 1 244 ? -2.333  -12.868 14.741  1.00 5.50  ? 245 TRP A NE1  1 
ATOM   1983 C  CE2  . TRP A 1 244 ? -1.931  -12.948 16.049  1.00 5.67  ? 245 TRP A CE2  1 
ATOM   1984 C  CE3  . TRP A 1 244 ? -1.903  -11.531 18.013  1.00 5.96  ? 245 TRP A CE3  1 
ATOM   1985 C  CZ2  . TRP A 1 244 ? -1.346  -14.018 16.750  1.00 6.75  ? 245 TRP A CZ2  1 
ATOM   1986 C  CZ3  . TRP A 1 244 ? -1.312  -12.597 18.716  1.00 6.24  ? 245 TRP A CZ3  1 
ATOM   1987 C  CH2  . TRP A 1 244 ? -1.047  -13.818 18.079  1.00 6.57  ? 245 TRP A CH2  1 
ATOM   1988 N  N    . ARG A 1 245 ? -1.263  -7.335  17.290  1.00 4.65  ? 246 ARG A N    1 
ATOM   1989 C  CA   . ARG A 1 245 ? -0.294  -7.223  18.385  1.00 4.92  ? 246 ARG A CA   1 
ATOM   1990 C  C    . ARG A 1 245 ? -0.771  -8.135  19.530  1.00 5.15  ? 246 ARG A C    1 
ATOM   1991 O  O    . ARG A 1 245 ? -1.959  -8.162  19.837  1.00 6.35  ? 246 ARG A O    1 
ATOM   1992 C  CB   . ARG A 1 245 ? -0.218  -5.764  18.872  1.00 5.36  ? 246 ARG A CB   1 
ATOM   1993 C  CG   . ARG A 1 245 ? 0.885   -5.571  19.915  1.00 3.11  ? 246 ARG A CG   1 
ATOM   1994 C  CD   . ARG A 1 245 ? 0.869   -4.149  20.526  1.00 5.35  ? 246 ARG A CD   1 
ATOM   1995 N  NE   . ARG A 1 245 ? 2.153   -3.842  21.193  1.00 6.35  ? 246 ARG A NE   1 
ATOM   1996 C  CZ   . ARG A 1 245 ? 2.334   -2.836  22.053  1.00 7.51  ? 246 ARG A CZ   1 
ATOM   1997 N  NH1  . ARG A 1 245 ? 1.309   -2.044  22.388  1.00 5.28  ? 246 ARG A NH1  1 
ATOM   1998 N  NH2  . ARG A 1 245 ? 3.545   -2.617  22.588  1.00 6.50  ? 246 ARG A NH2  1 
ATOM   1999 N  N    . PRO A 1 246 ? 0.139   -8.888  20.159  1.00 6.13  ? 247 PRO A N    1 
ATOM   2000 C  CA   . PRO A 1 246 ? -0.244  -9.751  21.282  1.00 6.41  ? 247 PRO A CA   1 
ATOM   2001 C  C    . PRO A 1 246 ? -0.578  -8.947  22.520  1.00 6.41  ? 247 PRO A C    1 
ATOM   2002 O  O    . PRO A 1 246 ? -0.218  -7.767  22.619  1.00 6.69  ? 247 PRO A O    1 
ATOM   2003 C  CB   . PRO A 1 246 ? 1.018   -10.579 21.559  1.00 6.95  ? 247 PRO A CB   1 
ATOM   2004 C  CG   . PRO A 1 246 ? 1.994   -10.208 20.533  1.00 7.45  ? 247 PRO A CG   1 
ATOM   2005 C  CD   . PRO A 1 246 ? 1.570   -8.991  19.827  1.00 6.43  ? 247 PRO A CD   1 
ATOM   2006 N  N    . ALA A 1 247 ? -1.250  -9.599  23.462  1.00 6.54  ? 248 ALA A N    1 
ATOM   2007 C  CA   . ALA A 1 247 ? -1.573  -8.969  24.749  1.00 5.75  ? 248 ALA A CA   1 
ATOM   2008 C  C    . ALA A 1 247 ? -0.347  -8.426  25.470  1.00 6.50  ? 248 ALA A C    1 
ATOM   2009 O  O    . ALA A 1 247 ? 0.730   -9.060  25.488  1.00 6.76  ? 248 ALA A O    1 
ATOM   2010 C  CB   . ALA A 1 247 ? -2.344  -9.962  25.658  1.00 7.62  ? 248 ALA A CB   1 
ATOM   2011 N  N    . GLN A 1 248 ? -0.542  -7.254  26.076  1.00 5.61  ? 249 GLN A N    1 
ATOM   2012 C  CA   . GLN A 1 248 ? 0.492   -6.507  26.793  1.00 6.53  ? 249 GLN A CA   1 
ATOM   2013 C  C    . GLN A 1 248 ? 0.218   -6.482  28.297  1.00 7.00  ? 249 GLN A C    1 
ATOM   2014 O  O    . GLN A 1 248 ? -0.920  -6.680  28.718  1.00 6.61  ? 249 GLN A O    1 
ATOM   2015 C  CB   . GLN A 1 248 ? 0.522   -5.080  26.245  1.00 6.97  ? 249 GLN A CB   1 
ATOM   2016 C  CG   . GLN A 1 248 ? 0.900   -4.999  24.753  1.00 6.71  ? 249 GLN A CG   1 
ATOM   2017 C  CD   . GLN A 1 248 ? 2.255   -5.637  24.455  1.00 9.40  ? 249 GLN A CD   1 
ATOM   2018 O  OE1  . GLN A 1 248 ? 3.284   -5.295  25.072  1.00 9.62  ? 249 GLN A OE1  1 
ATOM   2019 N  NE2  . GLN A 1 248 ? 2.263   -6.575  23.521  1.00 9.22  ? 249 GLN A NE2  1 
ATOM   2020 N  N    . PRO A 1 249 ? 1.258   -6.244  29.122  1.00 7.93  ? 250 PRO A N    1 
ATOM   2021 C  CA   . PRO A 1 249 ? 1.054   -6.182  30.579  1.00 8.66  ? 250 PRO A CA   1 
ATOM   2022 C  C    . PRO A 1 249 ? -0.025  -5.197  31.025  1.00 8.48  ? 250 PRO A C    1 
ATOM   2023 O  O    . PRO A 1 249 ? -0.009  -4.034  30.621  1.00 8.73  ? 250 PRO A O    1 
ATOM   2024 C  CB   . PRO A 1 249 ? 2.421   -5.716  31.104  1.00 8.87  ? 250 PRO A CB   1 
ATOM   2025 C  CG   . PRO A 1 249 ? 3.394   -6.205  30.085  1.00 9.72  ? 250 PRO A CG   1 
ATOM   2026 C  CD   . PRO A 1 249 ? 2.679   -6.062  28.759  1.00 8.38  ? 250 PRO A CD   1 
ATOM   2027 N  N    . LEU A 1 250 ? -0.931  -5.667  31.886  1.00 9.30  ? 251 LEU A N    1 
ATOM   2028 C  CA   . LEU A 1 250 ? -2.036  -4.839  32.366  1.00 9.61  ? 251 LEU A CA   1 
ATOM   2029 C  C    . LEU A 1 250 ? -1.513  -3.770  33.318  1.00 10.14 ? 251 LEU A C    1 
ATOM   2030 O  O    . LEU A 1 250 ? -2.079  -2.682  33.408  1.00 9.60  ? 251 LEU A O    1 
ATOM   2031 C  CB   . LEU A 1 250 ? -3.102  -5.695  33.076  1.00 9.88  ? 251 LEU A CB   1 
ATOM   2032 C  CG   . LEU A 1 250 ? -4.401  -4.975  33.475  1.00 10.04 ? 251 LEU A CG   1 
ATOM   2033 C  CD1  . LEU A 1 250 ? -5.078  -4.350  32.240  1.00 9.68  ? 251 LEU A CD1  1 
ATOM   2034 C  CD2  . LEU A 1 250 ? -5.383  -5.884  34.233  1.00 11.32 ? 251 LEU A CD2  1 
ATOM   2035 N  N    . LYS A 1 251 ? -0.444  -4.099  34.042  1.00 10.83 ? 252 LYS A N    1 
ATOM   2036 C  CA   . LYS A 1 251 ? 0.182   -3.148  34.982  1.00 12.30 ? 252 LYS A CA   1 
ATOM   2037 C  C    . LYS A 1 251 ? -0.840  -2.580  35.968  1.00 12.82 ? 252 LYS A C    1 
ATOM   2038 O  O    . LYS A 1 251 ? -1.653  -3.345  36.493  1.00 13.10 ? 252 LYS A O    1 
ATOM   2039 C  CB   . LYS A 1 251 ? 0.998   -2.093  34.236  1.00 12.49 ? 252 LYS A CB   1 
ATOM   2040 C  CG   . LYS A 1 251 ? 2.224   -2.742  33.585  1.00 14.76 ? 252 LYS A CG   1 
ATOM   2041 C  CD   . LYS A 1 251 ? 3.131   -1.755  32.919  1.00 18.49 ? 252 LYS A CD   1 
ATOM   2042 C  CE   . LYS A 1 251 ? 4.395   -2.461  32.449  1.00 20.42 ? 252 LYS A CE   1 
ATOM   2043 N  NZ   . LYS A 1 251 ? 4.987   -1.758  31.280  1.00 22.62 ? 252 LYS A NZ   1 
ATOM   2044 N  N    . ASN A 1 252 ? -0.814  -1.273  36.209  1.00 13.58 ? 253 ASN A N    1 
ATOM   2045 C  CA   . ASN A 1 252 ? -1.667  -0.676  37.220  1.00 15.39 ? 253 ASN A CA   1 
ATOM   2046 C  C    . ASN A 1 252 ? -2.994  -0.215  36.640  1.00 14.79 ? 253 ASN A C    1 
ATOM   2047 O  O    . ASN A 1 252 ? -3.313  0.991   36.708  1.00 16.47 ? 253 ASN A O    1 
ATOM   2048 C  CB   . ASN A 1 252 ? -0.952  0.501   37.898  1.00 16.56 ? 253 ASN A CB   1 
ATOM   2049 C  CG   . ASN A 1 252 ? -1.727  1.047   39.085  1.00 19.06 ? 253 ASN A CG   1 
ATOM   2050 O  OD1  . ASN A 1 252 ? -2.362  0.294   39.827  1.00 22.99 ? 253 ASN A OD1  1 
ATOM   2051 N  ND2  . ASN A 1 252 ? -1.695  2.363   39.260  1.00 23.32 ? 253 ASN A ND2  1 
ATOM   2052 N  N    . ARG A 1 253 ? -3.747  -1.151  36.050  1.00 12.80 ? 254 ARG A N    1 
ATOM   2053 C  CA   . ARG A 1 253 ? -5.057  -0.822  35.453  1.00 11.16 ? 254 ARG A CA   1 
ATOM   2054 C  C    . ARG A 1 253 ? -6.167  -1.785  35.870  1.00 11.18 ? 254 ARG A C    1 
ATOM   2055 O  O    . ARG A 1 253 ? -5.909  -2.964  36.113  1.00 11.52 ? 254 ARG A O    1 
ATOM   2056 C  CB   . ARG A 1 253 ? -4.966  -0.805  33.923  1.00 10.24 ? 254 ARG A CB   1 
ATOM   2057 C  CG   . ARG A 1 253 ? -4.108  0.334   33.376  1.00 9.31  ? 254 ARG A CG   1 
ATOM   2058 C  CD   . ARG A 1 253 ? -4.021  0.233   31.880  1.00 8.15  ? 254 ARG A CD   1 
ATOM   2059 N  NE   . ARG A 1 253 ? -3.125  -0.856  31.450  1.00 7.02  ? 254 ARG A NE   1 
ATOM   2060 C  CZ   . ARG A 1 253 ? -2.875  -1.154  30.173  1.00 6.33  ? 254 ARG A CZ   1 
ATOM   2061 N  NH1  . ARG A 1 253 ? -3.468  -0.465  29.185  1.00 5.98  ? 254 ARG A NH1  1 
ATOM   2062 N  NH2  . ARG A 1 253 ? -2.048  -2.151  29.872  1.00 5.69  ? 254 ARG A NH2  1 
ATOM   2063 N  N    A GLN A 1 254 ? -7.407  -1.283  35.961  0.50 10.87 ? 255 GLN A N    1 
ATOM   2064 N  N    B GLN A 1 254 ? -7.388  -1.263  35.938  0.50 10.70 ? 255 GLN A N    1 
ATOM   2065 C  CA   A GLN A 1 254 ? -8.581  -2.135  36.237  0.50 11.15 ? 255 GLN A CA   1 
ATOM   2066 C  CA   B GLN A 1 254 ? -8.556  -2.087  36.182  0.50 10.87 ? 255 GLN A CA   1 
ATOM   2067 C  C    A GLN A 1 254 ? -9.509  -2.132  35.029  0.50 10.60 ? 255 GLN A C    1 
ATOM   2068 C  C    B GLN A 1 254 ? -9.389  -2.141  34.906  0.50 10.34 ? 255 GLN A C    1 
ATOM   2069 O  O    A GLN A 1 254 ? -9.851  -1.066  34.503  0.50 10.90 ? 255 GLN A O    1 
ATOM   2070 O  O    B GLN A 1 254 ? -9.532  -1.132  34.203  0.50 10.44 ? 255 GLN A O    1 
ATOM   2071 C  CB   A GLN A 1 254 ? -9.359  -1.672  37.488  0.50 11.40 ? 255 GLN A CB   1 
ATOM   2072 C  CB   B GLN A 1 254 ? -9.380  -1.539  37.357  0.50 10.94 ? 255 GLN A CB   1 
ATOM   2073 C  CG   A GLN A 1 254 ? -9.875  -2.823  38.412  0.50 13.36 ? 255 GLN A CG   1 
ATOM   2074 C  CG   B GLN A 1 254 ? -8.736  -1.763  38.745  0.50 12.65 ? 255 GLN A CG   1 
ATOM   2075 C  CD   A GLN A 1 254 ? -11.392 -3.088  38.347  0.50 16.57 ? 255 GLN A CD   1 
ATOM   2076 C  CD   B GLN A 1 254 ? -9.754  -1.802  39.880  0.50 14.62 ? 255 GLN A CD   1 
ATOM   2077 O  OE1  A GLN A 1 254 ? -11.845 -4.096  37.788  0.50 15.59 ? 255 GLN A OE1  1 
ATOM   2078 O  OE1  B GLN A 1 254 ? -10.722 -1.037  39.889  0.50 16.75 ? 255 GLN A OE1  1 
ATOM   2079 N  NE2  A GLN A 1 254 ? -12.175 -2.204  38.960  0.50 17.32 ? 255 GLN A NE2  1 
ATOM   2080 N  NE2  B GLN A 1 254 ? -9.538  -2.699  40.848  0.50 15.52 ? 255 GLN A NE2  1 
ATOM   2081 N  N    . ILE A 1 255 ? -9.903  -3.327  34.596  1.00 9.84  ? 256 ILE A N    1 
ATOM   2082 C  CA   . ILE A 1 255 ? -10.868 -3.478  33.516  1.00 9.48  ? 256 ILE A CA   1 
ATOM   2083 C  C    . ILE A 1 255 ? -12.256 -3.515  34.163  1.00 8.92  ? 256 ILE A C    1 
ATOM   2084 O  O    . ILE A 1 255 ? -12.482 -4.266  35.124  1.00 8.40  ? 256 ILE A O    1 
ATOM   2085 C  CB   . ILE A 1 255 ? -10.619 -4.767  32.705  1.00 9.01  ? 256 ILE A CB   1 
ATOM   2086 C  CG1  . ILE A 1 255 ? -9.192  -4.758  32.139  1.00 10.46 ? 256 ILE A CG1  1 
ATOM   2087 C  CG2  . ILE A 1 255 ? -11.641 -4.881  31.568  1.00 9.64  ? 256 ILE A CG2  1 
ATOM   2088 C  CD1  . ILE A 1 255 ? -8.800  -6.049  31.434  1.00 10.55 ? 256 ILE A CD1  1 
ATOM   2089 N  N    . LYS A 1 256 ? -13.156 -2.658  33.683  1.00 8.35  ? 257 LYS A N    1 
ATOM   2090 C  CA   . LYS A 1 256 ? -14.493 -2.570  34.279  1.00 8.25  ? 257 LYS A CA   1 
ATOM   2091 C  C    . LYS A 1 256 ? -15.519 -3.180  33.335  1.00 8.50  ? 257 LYS A C    1 
ATOM   2092 O  O    . LYS A 1 256 ? -15.374 -3.054  32.116  1.00 8.44  ? 257 LYS A O    1 
ATOM   2093 C  CB   . LYS A 1 256 ? -14.819 -1.111  34.590  1.00 8.73  ? 257 LYS A CB   1 
ATOM   2094 C  CG   . LYS A 1 256 ? -13.869 -0.564  35.658  1.00 12.11 ? 257 LYS A CG   1 
ATOM   2095 C  CD   . LYS A 1 256 ? -14.055 0.904   35.916  1.00 18.86 ? 257 LYS A CD   1 
ATOM   2096 C  CE   . LYS A 1 256 ? -12.987 1.394   36.904  1.00 22.15 ? 257 LYS A CE   1 
ATOM   2097 N  NZ   . LYS A 1 256 ? -13.080 2.876   37.108  1.00 23.62 ? 257 LYS A NZ   1 
ATOM   2098 N  N    . ALA A 1 257 ? -16.539 -3.840  33.896  1.00 8.22  ? 258 ALA A N    1 
ATOM   2099 C  CA   . ALA A 1 257 ? -17.634 -4.429  33.105  1.00 8.98  ? 258 ALA A CA   1 
ATOM   2100 C  C    . ALA A 1 257 ? -18.900 -3.614  33.242  1.00 9.46  ? 258 ALA A C    1 
ATOM   2101 O  O    . ALA A 1 257 ? -19.233 -3.134  34.345  1.00 9.15  ? 258 ALA A O    1 
ATOM   2102 C  CB   . ALA A 1 257 ? -17.900 -5.873  33.520  1.00 9.53  ? 258 ALA A CB   1 
ATOM   2103 N  N    . SER A 1 258 ? -19.623 -3.485  32.129  1.00 9.10  ? 259 SER A N    1 
ATOM   2104 C  CA   . SER A 1 258 ? -20.869 -2.726  32.110  1.00 10.43 ? 259 SER A CA   1 
ATOM   2105 C  C    . SER A 1 258 ? -22.061 -3.571  32.544  1.00 11.51 ? 259 SER A C    1 
ATOM   2106 O  O    . SER A 1 258 ? -23.167 -3.041  32.700  1.00 12.27 ? 259 SER A O    1 
ATOM   2107 C  CB   . SER A 1 258 ? -21.131 -2.200  30.706  1.00 10.25 ? 259 SER A CB   1 
ATOM   2108 O  OG   . SER A 1 258 ? -21.623 -3.218  29.841  1.00 9.87  ? 259 SER A OG   1 
ATOM   2109 N  N    . PHE A 1 259 ? -21.824 -4.861  32.748  1.00 13.11 ? 260 PHE A N    1 
ATOM   2110 C  CA   . PHE A 1 259 ? -22.898 -5.835  32.932  1.00 15.81 ? 260 PHE A CA   1 
ATOM   2111 C  C    . PHE A 1 259 ? -22.702 -6.738  34.140  1.00 18.21 ? 260 PHE A C    1 
ATOM   2112 O  O    . PHE A 1 259 ? -21.560 -7.027  34.544  1.00 18.06 ? 260 PHE A O    1 
ATOM   2113 C  CB   . PHE A 1 259 ? -23.010 -6.715  31.686  1.00 14.89 ? 260 PHE A CB   1 
ATOM   2114 C  CG   . PHE A 1 259 ? -21.730 -7.442  31.350  1.00 14.46 ? 260 PHE A CG   1 
ATOM   2115 C  CD1  . PHE A 1 259 ? -20.765 -6.837  30.545  1.00 11.51 ? 260 PHE A CD1  1 
ATOM   2116 C  CD2  . PHE A 1 259 ? -21.475 -8.710  31.860  1.00 14.40 ? 260 PHE A CD2  1 
ATOM   2117 C  CE1  . PHE A 1 259 ? -19.568 -7.495  30.236  1.00 13.38 ? 260 PHE A CE1  1 
ATOM   2118 C  CE2  . PHE A 1 259 ? -20.285 -9.369  31.551  1.00 15.41 ? 260 PHE A CE2  1 
ATOM   2119 C  CZ   . PHE A 1 259 ? -19.328 -8.754  30.744  1.00 14.58 ? 260 PHE A CZ   1 
ATOM   2120 N  N    . LYS A 1 260 ? -23.851 -7.174  34.670  1.00 21.35 ? 261 LYS A N    1 
ATOM   2121 C  CA   . LYS A 1 260 ? -24.016 -8.257  35.657  1.00 24.66 ? 261 LYS A CA   1 
ATOM   2122 C  C    . LYS A 1 260 ? -23.453 -7.977  37.042  1.00 26.04 ? 261 LYS A C    1 
ATOM   2123 O  O    . LYS A 1 260 ? -22.242 -7.882  37.221  1.00 27.27 ? 261 LYS A O    1 
ATOM   2124 C  CB   . LYS A 1 260 ? -23.535 -9.614  35.110  1.00 24.75 ? 261 LYS A CB   1 
ATOM   2125 C  CG   . LYS A 1 260 ? -24.432 -10.194 34.000  1.00 25.75 ? 261 LYS A CG   1 
ATOM   2126 C  CD   . LYS A 1 260 ? -24.068 -11.641 33.645  1.00 26.56 ? 261 LYS A CD   1 
ATOM   2127 C  CE   . LYS A 1 260 ? -22.855 -11.719 32.728  1.00 28.23 ? 261 LYS A CE   1 
ATOM   2128 N  NZ   . LYS A 1 260 ? -22.484 -13.116 32.363  1.00 29.86 ? 261 LYS A NZ   1 
ATOM   2129 O  OXT  . LYS A 1 260 ? -24.204 -7.816  38.017  1.00 27.09 ? 261 LYS A OXT  1 
HETATM 2130 ZN ZN   . ZN  B 2 .   ? -6.837  -1.668  15.344  1.00 4.75  ? 262 ZN  A ZN   1 
HETATM 2131 S  S    . DMS C 3 .   ? 1.316   -11.722 14.939  1.00 30.27 ? 263 DMS A S    1 
HETATM 2132 O  O    . DMS C 3 .   ? 2.524   -11.013 13.800  1.00 28.89 ? 263 DMS A O    1 
HETATM 2133 C  C1   . DMS C 3 .   ? 1.749   -13.475 15.118  1.00 29.01 ? 263 DMS A C1   1 
HETATM 2134 C  C2   . DMS C 3 .   ? 1.565   -11.188 16.651  1.00 27.74 ? 263 DMS A C2   1 
HETATM 2135 N  N1   . JDR D 4 .   ? -3.992  10.307  12.091  1.00 27.65 ? 264 JDR A N1   1 
HETATM 2136 C  C2   . JDR D 4 .   ? -3.170  9.642   12.892  1.00 27.91 ? 264 JDR A C2   1 
HETATM 2137 N  N3   . JDR D 4 .   ? -3.325  8.348   13.161  1.00 27.38 ? 264 JDR A N3   1 
HETATM 2138 C  C4   . JDR D 4 .   ? -4.341  7.676   12.617  1.00 26.76 ? 264 JDR A C4   1 
HETATM 2139 C  C5   . JDR D 4 .   ? -5.230  8.334   11.769  1.00 27.58 ? 264 JDR A C5   1 
HETATM 2140 C  C6   . JDR D 4 .   ? -5.016  9.686   11.523  1.00 29.03 ? 264 JDR A C6   1 
HETATM 2141 N  N7   . JDR D 4 .   ? -4.523  6.279   12.908  1.00 23.48 ? 264 JDR A N7   1 
HETATM 2142 C  C8   . JDR D 4 .   ? -4.393  4.464   14.585  1.00 9.18  ? 264 JDR A C8   1 
HETATM 2143 C  C9   . JDR D 4 .   ? -5.758  4.446   14.879  1.00 7.64  ? 264 JDR A C9   1 
HETATM 2144 C  C10  . JDR D 4 .   ? -6.299  3.353   15.567  1.00 7.58  ? 264 JDR A C10  1 
HETATM 2145 C  C11  . JDR D 4 .   ? -5.455  2.300   15.946  1.00 6.56  ? 264 JDR A C11  1 
HETATM 2146 C  C12  . JDR D 4 .   ? -4.102  2.332   15.644  1.00 5.69  ? 264 JDR A C12  1 
HETATM 2147 C  C13  . JDR D 4 .   ? -3.571  3.419   14.965  1.00 8.26  ? 264 JDR A C13  1 
HETATM 2148 S  S14  . JDR D 4 .   ? -6.050  0.910   16.802  1.00 5.72  ? 264 JDR A S14  1 
HETATM 2149 O  O15  . JDR D 4 .   ? -5.529  0.982   18.215  1.00 5.14  ? 264 JDR A O15  1 
HETATM 2150 O  O16  . JDR D 4 .   ? -7.563  0.898   16.634  1.00 4.59  ? 264 JDR A O16  1 
HETATM 2151 N  N17  . JDR D 4 .   ? -5.395  -0.492  16.058  1.00 4.60  ? 264 JDR A N17  1 
HETATM 2152 C  C18  . JDR D 4 .   ? -6.372  7.633   11.140  1.00 28.22 ? 264 JDR A C18  1 
HETATM 2153 O  O19  . JDR D 4 .   ? -6.810  6.592   11.635  1.00 28.67 ? 264 JDR A O19  1 
HETATM 2154 CL CL20 . JDR D 4 .   ? -6.067  10.593  10.499  1.00 31.97 ? 264 JDR A CL20 1 
HETATM 2155 S  S21  . JDR D 4 .   ? -1.824  10.471  13.659  1.00 29.25 ? 264 JDR A S21  1 
HETATM 2156 C  C22  . JDR D 4 .   ? -1.103  9.460   14.994  1.00 26.58 ? 264 JDR A C22  1 
HETATM 2157 C  C23  . JDR D 4 .   ? -3.694  5.565   13.858  1.00 12.33 ? 264 JDR A C23  1 
HETATM 2158 O  O    . HOH E 5 .   ? -24.798 12.012  6.491   1.00 27.38 ? 126 HOH A O    1 
HETATM 2159 O  O    . HOH E 5 .   ? -32.343 0.166   14.229  1.00 29.23 ? 265 HOH A O    1 
HETATM 2160 O  O    . HOH E 5 .   ? -25.024 13.777  19.570  1.00 49.46 ? 266 HOH A O    1 
HETATM 2161 O  O    . HOH E 5 .   ? -25.899 -1.116  35.265  1.00 28.56 ? 267 HOH A O    1 
HETATM 2162 O  O    . HOH E 5 .   ? 8.520   -11.764 7.057   1.00 26.80 ? 268 HOH A O    1 
HETATM 2163 O  O    . HOH E 5 .   ? 3.030   -5.846  -11.606 1.00 32.54 ? 269 HOH A O    1 
HETATM 2164 O  O    . HOH E 5 .   ? 2.445   12.970  20.052  1.00 28.76 ? 270 HOH A O    1 
HETATM 2165 O  O    . HOH E 5 .   ? 1.211   -9.838  31.897  1.00 27.23 ? 271 HOH A O    1 
HETATM 2166 O  O    . HOH E 5 .   ? -16.038 3.607   35.491  1.00 32.00 ? 272 HOH A O    1 
HETATM 2167 O  O    . HOH E 5 .   ? -19.756 -15.311 26.104  1.00 30.18 ? 273 HOH A O    1 
HETATM 2168 O  O    . HOH E 5 .   ? -11.943 8.852   -5.850  1.00 25.87 ? 274 HOH A O    1 
HETATM 2169 O  O    . HOH E 5 .   ? -12.546 7.512   35.484  1.00 33.72 ? 275 HOH A O    1 
HETATM 2170 O  O    . HOH E 5 .   ? 6.671   -3.725  30.299  1.00 30.47 ? 276 HOH A O    1 
HETATM 2171 O  O    . HOH E 5 .   ? -15.915 -10.170 38.090  1.00 34.76 ? 277 HOH A O    1 
HETATM 2172 O  O    . HOH E 5 .   ? -28.314 -0.722  14.824  1.00 32.49 ? 278 HOH A O    1 
HETATM 2173 O  O    . HOH E 5 .   ? -15.280 -20.138 23.303  1.00 27.25 ? 279 HOH A O    1 
HETATM 2174 O  O    . HOH E 5 .   ? 4.936   11.314  20.322  1.00 35.20 ? 280 HOH A O    1 
HETATM 2175 O  O    . HOH E 5 .   ? -19.966 -13.683 24.514  1.00 34.93 ? 281 HOH A O    1 
HETATM 2176 O  O    . HOH E 5 .   ? -26.119 11.818  17.047  1.00 26.74 ? 282 HOH A O    1 
HETATM 2177 O  O    . HOH E 5 .   ? -0.490  -15.816 27.588  1.00 35.35 ? 283 HOH A O    1 
HETATM 2178 O  O    . HOH E 5 .   ? 4.566   -3.538  3.363   1.00 26.72 ? 284 HOH A O    1 
HETATM 2179 O  O    . HOH E 5 .   ? 6.598   -5.585  32.201  1.00 37.23 ? 285 HOH A O    1 
HETATM 2180 O  O    . HOH E 5 .   ? -25.838 -2.488  33.114  1.00 30.18 ? 286 HOH A O    1 
HETATM 2181 O  O    . HOH E 5 .   ? -25.399 8.822   26.206  1.00 28.46 ? 287 HOH A O    1 
HETATM 2182 O  O    . HOH E 5 .   ? -10.543 -5.995  38.679  1.00 38.86 ? 288 HOH A O    1 
HETATM 2183 O  O    . HOH E 5 .   ? -6.594  -19.522 5.742   1.00 33.04 ? 289 HOH A O    1 
HETATM 2184 O  O    . HOH E 5 .   ? 4.515   -11.033 6.925   1.00 36.50 ? 290 HOH A O    1 
HETATM 2185 O  O    . HOH E 5 .   ? -0.114  -7.218  -7.415  1.00 33.78 ? 291 HOH A O    1 
HETATM 2186 O  O    . HOH E 5 .   ? 6.434   -5.470  27.532  1.00 32.93 ? 292 HOH A O    1 
HETATM 2187 O  O    . HOH E 5 .   ? -6.022  -9.108  35.842  1.00 37.35 ? 293 HOH A O    1 
HETATM 2188 O  O    . HOH E 5 .   ? -17.323 -4.406  -5.231  1.00 27.64 ? 294 HOH A O    1 
HETATM 2189 O  O    . HOH E 5 .   ? -12.400 13.288  4.886   1.00 30.72 ? 295 HOH A O    1 
HETATM 2190 O  O    . HOH E 5 .   ? -19.628 -18.632 33.985  1.00 30.54 ? 296 HOH A O    1 
HETATM 2191 O  O    . HOH E 5 .   ? -21.839 -21.716 17.740  1.00 40.44 ? 297 HOH A O    1 
HETATM 2192 O  O    . HOH E 5 .   ? -1.502  -13.287 33.439  1.00 22.71 ? 298 HOH A O    1 
HETATM 2193 O  O    . HOH E 5 .   ? 1.392   13.015  17.547  1.00 31.73 ? 299 HOH A O    1 
HETATM 2194 O  O    . HOH E 5 .   ? -29.645 -4.866  4.279   1.00 47.06 ? 300 HOH A O    1 
HETATM 2195 O  O    . HOH E 5 .   ? -5.596  -12.807 -5.009  1.00 35.62 ? 301 HOH A O    1 
HETATM 2196 O  O    . HOH E 5 .   ? -28.673 5.446   26.114  1.00 36.59 ? 302 HOH A O    1 
HETATM 2197 O  O    . HOH E 5 .   ? -14.261 -5.115  -6.278  1.00 35.36 ? 303 HOH A O    1 
HETATM 2198 O  O    . HOH E 5 .   ? 2.082   -14.809 -1.014  1.00 34.45 ? 304 HOH A O    1 
HETATM 2199 O  O    . HOH E 5 .   ? -29.500 -4.074  13.584  1.00 29.04 ? 305 HOH A O    1 
HETATM 2200 O  O    . HOH E 5 .   ? -17.932 6.231   38.589  1.00 24.92 ? 306 HOH A O    1 
HETATM 2201 O  O    . HOH E 5 .   ? -25.936 -3.677  6.208   1.00 33.38 ? 307 HOH A O    1 
HETATM 2202 O  O    . HOH E 5 .   ? -2.664  -8.987  35.042  1.00 37.07 ? 308 HOH A O    1 
HETATM 2203 O  O    . HOH E 5 .   ? -16.360 -12.883 -5.978  1.00 31.97 ? 309 HOH A O    1 
HETATM 2204 O  O    . HOH E 5 .   ? -0.078  7.581   12.782  1.00 41.20 ? 310 HOH A O    1 
HETATM 2205 O  O    . HOH E 5 .   ? -24.641 -7.173  0.596   1.00 28.85 ? 311 HOH A O    1 
HETATM 2206 O  O    . HOH E 5 .   ? 5.463   -12.804 11.290  1.00 33.52 ? 312 HOH A O    1 
HETATM 2207 O  O    . HOH E 5 .   ? -1.323  -6.001  36.754  1.00 30.25 ? 313 HOH A O    1 
HETATM 2208 O  O    . HOH E 5 .   ? -19.167 -21.139 5.626   1.00 33.65 ? 314 HOH A O    1 
HETATM 2209 O  O    . HOH E 5 .   ? -15.616 0.447   -5.067  1.00 33.95 ? 315 HOH A O    1 
HETATM 2210 O  O    . HOH E 5 .   ? -4.721  -9.852  33.673  1.00 36.98 ? 316 HOH A O    1 
HETATM 2211 O  O    . HOH E 5 .   ? 4.460   -11.052 17.062  1.00 55.97 ? 317 HOH A O    1 
HETATM 2212 O  O    . HOH E 5 .   ? 5.690   9.224   26.183  1.00 34.14 ? 318 HOH A O    1 
HETATM 2213 O  O    . HOH E 5 .   ? -0.693  6.442   32.297  1.00 31.64 ? 319 HOH A O    1 
HETATM 2214 O  O    . HOH E 5 .   ? 1.777   -14.071 29.345  1.00 43.01 ? 320 HOH A O    1 
HETATM 2215 O  O    . HOH E 5 .   ? 0.852   -18.586 28.983  1.00 32.09 ? 321 HOH A O    1 
HETATM 2216 O  O    . HOH E 5 .   ? 2.323   -14.952 -5.271  1.00 39.51 ? 322 HOH A O    1 
HETATM 2217 O  O    . HOH E 5 .   ? 7.768   -1.249  -5.753  1.00 27.79 ? 323 HOH A O    1 
HETATM 2218 O  O    . HOH E 5 .   ? 3.929   -13.353 21.664  1.00 35.61 ? 324 HOH A O    1 
HETATM 2219 O  O    . HOH E 5 .   ? -17.326 18.069  22.305  1.00 33.38 ? 325 HOH A O    1 
HETATM 2220 O  O    . HOH E 5 .   ? -26.043 -5.770  13.212  1.00 30.39 ? 326 HOH A O    1 
HETATM 2221 O  O    . HOH E 5 .   ? -28.517 0.134   0.065   1.00 49.54 ? 327 HOH A O    1 
HETATM 2222 O  O    . HOH E 5 .   ? -21.957 15.786  3.747   1.00 38.99 ? 328 HOH A O    1 
HETATM 2223 O  O    . HOH E 5 .   ? -24.338 -0.040  1.261   1.00 26.81 ? 329 HOH A O    1 
HETATM 2224 O  O    . HOH E 5 .   ? -25.652 -1.633  -0.058  1.00 32.74 ? 330 HOH A O    1 
HETATM 2225 O  O    . HOH E 5 .   ? -5.516  3.299   -5.759  1.00 22.35 ? 331 HOH A O    1 
HETATM 2226 O  O    . HOH E 5 .   ? -1.395  -4.191  15.862  1.00 4.21  ? 332 HOH A O    1 
HETATM 2227 O  O    . HOH E 5 .   ? -3.657  -11.123 21.012  1.00 8.01  ? 333 HOH A O    1 
HETATM 2228 O  O    . HOH E 5 .   ? 4.763   -4.961  21.059  1.00 8.59  ? 334 HOH A O    1 
HETATM 2229 O  O    . HOH E 5 .   ? -17.239 -8.459  20.534  1.00 6.66  ? 335 HOH A O    1 
HETATM 2230 O  O    . HOH E 5 .   ? -8.845  -3.946  7.964   1.00 6.75  ? 336 HOH A O    1 
HETATM 2231 O  O    . HOH E 5 .   ? -4.669  -13.532 18.229  1.00 5.36  ? 337 HOH A O    1 
HETATM 2232 O  O    . HOH E 5 .   ? -8.102  -15.480 11.477  1.00 7.87  ? 338 HOH A O    1 
HETATM 2233 O  O    . HOH E 5 .   ? -21.808 -7.321  23.780  1.00 9.66  ? 339 HOH A O    1 
HETATM 2234 O  O    . HOH E 5 .   ? 1.128   -1.481  29.514  1.00 8.22  ? 340 HOH A O    1 
HETATM 2235 O  O    . HOH E 5 .   ? 3.445   5.076   30.004  1.00 13.33 ? 341 HOH A O    1 
HETATM 2236 O  O    . HOH E 5 .   ? -13.055 -17.291 17.013  1.00 11.26 ? 342 HOH A O    1 
HETATM 2237 O  O    . HOH E 5 .   ? -2.233  -12.336 22.941  1.00 8.50  ? 343 HOH A O    1 
HETATM 2238 O  O    . HOH E 5 .   ? -3.556  -13.307 25.355  1.00 7.94  ? 344 HOH A O    1 
HETATM 2239 O  O    . HOH E 5 .   ? -10.872 8.769   25.578  1.00 6.67  ? 345 HOH A O    1 
HETATM 2240 O  O    . HOH E 5 .   ? -22.004 5.503   4.799   1.00 12.25 ? 346 HOH A O    1 
HETATM 2241 O  O    . HOH E 5 .   ? -6.271  -4.787  -6.404  1.00 18.93 ? 347 HOH A O    1 
HETATM 2242 O  O    . HOH E 5 .   ? -10.461 -18.404 17.235  1.00 11.05 ? 348 HOH A O    1 
HETATM 2243 O  O    . HOH E 5 .   ? -18.193 -20.603 7.990   1.00 11.41 ? 349 HOH A O    1 
HETATM 2244 O  O    . HOH E 5 .   ? 8.484   -3.884  21.203  1.00 13.32 ? 350 HOH A O    1 
HETATM 2245 O  O    . HOH E 5 .   ? -14.786 -18.756 18.863  1.00 10.40 ? 351 HOH A O    1 
HETATM 2246 O  O    . HOH E 5 .   ? 4.316   -6.560  7.858   1.00 15.08 ? 352 HOH A O    1 
HETATM 2247 O  O    . HOH E 5 .   ? -12.211 2.792   31.049  1.00 12.40 ? 353 HOH A O    1 
HETATM 2248 O  O    . HOH E 5 .   ? -9.813  -7.964  34.280  1.00 17.63 ? 354 HOH A O    1 
HETATM 2249 O  O    . HOH E 5 .   ? -2.621  -8.717  29.336  1.00 8.16  ? 355 HOH A O    1 
HETATM 2250 O  O    . HOH E 5 .   ? 0.100   -1.103  -4.808  1.00 12.73 ? 356 HOH A O    1 
HETATM 2251 O  O    . HOH E 5 .   ? -18.124 10.516  11.280  1.00 17.03 ? 357 HOH A O    1 
HETATM 2252 O  O    . HOH E 5 .   ? -20.014 -17.147 2.965   1.00 16.32 ? 358 HOH A O    1 
HETATM 2253 O  O    . HOH E 5 .   ? 5.289   7.147   20.311  1.00 10.46 ? 359 HOH A O    1 
HETATM 2254 O  O    . HOH E 5 .   ? -14.066 10.379  28.019  1.00 13.84 ? 360 HOH A O    1 
HETATM 2255 O  O    . HOH E 5 .   ? 7.613   6.037   21.804  1.00 9.80  ? 361 HOH A O    1 
HETATM 2256 O  O    . HOH E 5 .   ? -23.212 -11.870 14.262  1.00 17.43 ? 362 HOH A O    1 
HETATM 2257 O  O    . HOH E 5 .   ? -3.892  -15.958 24.532  1.00 9.30  ? 363 HOH A O    1 
HETATM 2258 O  O    . HOH E 5 .   ? -15.026 -21.237 17.717  1.00 13.94 ? 364 HOH A O    1 
HETATM 2259 O  O    . HOH E 5 .   ? -19.574 10.032  8.843   1.00 9.72  ? 365 HOH A O    1 
HETATM 2260 O  O    . HOH E 5 .   ? -16.374 -9.956  33.230  1.00 15.16 ? 366 HOH A O    1 
HETATM 2261 O  O    . HOH E 5 .   ? -13.134 -16.954 26.791  1.00 10.10 ? 367 HOH A O    1 
HETATM 2262 O  O    . HOH E 5 .   ? -16.319 -12.307 24.544  1.00 10.12 ? 368 HOH A O    1 
HETATM 2263 O  O    . HOH E 5 .   ? -14.395 -16.785 29.198  1.00 16.27 ? 369 HOH A O    1 
HETATM 2264 O  O    . HOH E 5 .   ? -4.118  0.176   13.466  1.00 10.59 ? 370 HOH A O    1 
HETATM 2265 O  O    . HOH E 5 .   ? -6.888  -20.300 19.672  1.00 12.39 ? 371 HOH A O    1 
HETATM 2266 O  O    . HOH E 5 .   ? 11.127  1.051   25.788  1.00 20.07 ? 372 HOH A O    1 
HETATM 2267 O  O    . HOH E 5 .   ? -10.709 -19.607 20.095  1.00 14.89 ? 373 HOH A O    1 
HETATM 2268 O  O    . HOH E 5 .   ? -17.863 -21.481 17.508  1.00 19.12 ? 374 HOH A O    1 
HETATM 2269 O  O    . HOH E 5 .   ? -9.539  3.258   34.974  1.00 16.45 ? 375 HOH A O    1 
HETATM 2270 O  O    . HOH E 5 .   ? 2.710   -4.407  7.634   1.00 16.15 ? 376 HOH A O    1 
HETATM 2271 O  O    . HOH E 5 .   ? -20.964 -12.945 -1.893  1.00 15.47 ? 377 HOH A O    1 
HETATM 2272 O  O    . HOH E 5 .   ? -13.029 -19.707 26.247  1.00 18.52 ? 378 HOH A O    1 
HETATM 2273 O  O    . HOH E 5 .   ? -13.673 -18.645 14.763  1.00 14.77 ? 379 HOH A O    1 
HETATM 2274 O  O    . HOH E 5 .   ? 1.143   8.830   24.565  1.00 11.71 ? 380 HOH A O    1 
HETATM 2275 O  O    . HOH E 5 .   ? -27.181 -2.882  14.378  1.00 18.09 ? 381 HOH A O    1 
HETATM 2276 O  O    . HOH E 5 .   ? -16.380 16.034  23.719  1.00 16.64 ? 382 HOH A O    1 
HETATM 2277 O  O    . HOH E 5 .   ? -3.818  -13.197 -2.747  1.00 17.17 ? 383 HOH A O    1 
HETATM 2278 O  O    . HOH E 5 .   ? -7.520  -8.640  32.837  1.00 15.67 ? 384 HOH A O    1 
HETATM 2279 O  O    . HOH E 5 .   ? -24.115 -0.948  4.023   1.00 14.19 ? 385 HOH A O    1 
HETATM 2280 O  O    . HOH E 5 .   ? -8.438  -19.497 21.914  1.00 14.36 ? 386 HOH A O    1 
HETATM 2281 O  O    . HOH E 5 .   ? -6.997  5.769   6.281   1.00 14.90 ? 387 HOH A O    1 
HETATM 2282 O  O    . HOH E 5 .   ? -1.505  -13.058 27.202  1.00 18.36 ? 388 HOH A O    1 
HETATM 2283 O  O    . HOH E 5 .   ? 4.405   -2.669  29.173  1.00 18.87 ? 389 HOH A O    1 
HETATM 2284 O  O    . HOH E 5 .   ? -1.358  -11.174 29.261  1.00 12.68 ? 390 HOH A O    1 
HETATM 2285 O  O    . HOH E 5 .   ? -17.452 -16.377 22.118  1.00 16.61 ? 391 HOH A O    1 
HETATM 2286 O  O    . HOH E 5 .   ? -26.382 3.508   15.499  1.00 17.92 ? 392 HOH A O    1 
HETATM 2287 O  O    . HOH E 5 .   ? -2.701  -3.699  11.441  1.00 16.15 ? 393 HOH A O    1 
HETATM 2288 O  O    . HOH E 5 .   ? -31.251 -7.196  22.592  1.00 18.98 ? 394 HOH A O    1 
HETATM 2289 O  O    . HOH E 5 .   ? 4.149   -3.434  26.735  1.00 16.45 ? 395 HOH A O    1 
HETATM 2290 O  O    . HOH E 5 .   ? -13.726 -21.288 15.058  1.00 16.83 ? 396 HOH A O    1 
HETATM 2291 O  O    . HOH E 5 .   ? -9.413  5.890   29.183  1.00 17.35 ? 397 HOH A O    1 
HETATM 2292 O  O    . HOH E 5 .   ? -23.024 -5.931  2.827   1.00 16.63 ? 398 HOH A O    1 
HETATM 2293 O  O    . HOH E 5 .   ? 2.479   -11.540 9.513   1.00 15.55 ? 399 HOH A O    1 
HETATM 2294 O  O    . HOH E 5 .   ? -11.289 1.087   33.620  1.00 15.95 ? 400 HOH A O    1 
HETATM 2295 O  O    . HOH E 5 .   ? -9.266  -5.743  36.223  1.00 17.34 ? 401 HOH A O    1 
HETATM 2296 O  O    . HOH E 5 .   ? -26.657 2.837   20.979  1.00 18.30 ? 402 HOH A O    1 
HETATM 2297 O  O    . HOH E 5 .   ? -20.142 -15.655 22.752  1.00 23.45 ? 403 HOH A O    1 
HETATM 2298 O  O    . HOH E 5 .   ? -12.930 7.971   28.998  1.00 20.56 ? 404 HOH A O    1 
HETATM 2299 O  O    . HOH E 5 .   ? -9.388  -10.202 -1.102  1.00 16.29 ? 405 HOH A O    1 
HETATM 2300 O  O    . HOH E 5 .   ? -17.117 -18.173 20.357  1.00 17.77 ? 406 HOH A O    1 
HETATM 2301 O  O    . HOH E 5 .   ? -10.740 4.983   31.175  1.00 18.19 ? 407 HOH A O    1 
HETATM 2302 O  O    . HOH E 5 .   ? -11.241 -19.697 7.400   1.00 18.07 ? 408 HOH A O    1 
HETATM 2303 O  O    . HOH E 5 .   ? 1.212   -11.832 25.328  1.00 18.16 ? 409 HOH A O    1 
HETATM 2304 O  O    . HOH E 5 .   ? -20.555 10.836  26.747  1.00 15.43 ? 410 HOH A O    1 
HETATM 2305 O  O    . HOH E 5 .   ? -27.229 -4.022  25.130  1.00 15.25 ? 411 HOH A O    1 
HETATM 2306 O  O    . HOH E 5 .   ? -5.095  -11.887 32.298  1.00 18.65 ? 412 HOH A O    1 
HETATM 2307 O  O    . HOH E 5 .   ? -2.116  -17.481 25.816  1.00 22.99 ? 413 HOH A O    1 
HETATM 2308 O  O    . HOH E 5 .   ? -15.569 -21.987 13.082  1.00 19.24 ? 414 HOH A O    1 
HETATM 2309 O  O    . HOH E 5 .   ? -5.174  0.554   9.825   1.00 17.31 ? 415 HOH A O    1 
HETATM 2310 O  O    . HOH E 5 .   ? -16.956 -13.979 26.468  1.00 17.12 ? 416 HOH A O    1 
HETATM 2311 O  O    . HOH E 5 .   ? 1.385   -6.220  34.626  1.00 17.55 ? 417 HOH A O    1 
HETATM 2312 O  O    . HOH E 5 .   ? 1.599   12.491  22.880  1.00 19.63 ? 418 HOH A O    1 
HETATM 2313 O  O    . HOH E 5 .   ? -0.313  -14.264 22.317  1.00 16.51 ? 419 HOH A O    1 
HETATM 2314 O  O    . HOH E 5 .   ? -0.635  10.830  23.486  1.00 13.25 ? 420 HOH A O    1 
HETATM 2315 O  O    . HOH E 5 .   ? -7.316  1.718   35.282  1.00 21.51 ? 421 HOH A O    1 
HETATM 2316 O  O    . HOH E 5 .   ? -7.333  -17.048 1.648   1.00 17.28 ? 422 HOH A O    1 
HETATM 2317 O  O    . HOH E 5 .   ? -8.916  0.464   -6.625  1.00 20.11 ? 423 HOH A O    1 
HETATM 2318 O  O    . HOH E 5 .   ? -24.392 8.669   20.186  1.00 18.49 ? 424 HOH A O    1 
HETATM 2319 O  O    . HOH E 5 .   ? -4.474  -8.447  31.251  1.00 16.69 ? 425 HOH A O    1 
HETATM 2320 O  O    . HOH E 5 .   ? -18.197 -12.131 31.873  1.00 22.30 ? 426 HOH A O    1 
HETATM 2321 O  O    . HOH E 5 .   ? -0.294  -20.225 6.871   1.00 19.91 ? 427 HOH A O    1 
HETATM 2322 O  O    . HOH E 5 .   ? 10.106  -2.535  13.912  1.00 27.91 ? 428 HOH A O    1 
HETATM 2323 O  O    . HOH E 5 .   ? -22.372 -18.470 13.721  1.00 18.71 ? 429 HOH A O    1 
HETATM 2324 O  O    . HOH E 5 .   ? 2.661   1.291   -2.207  1.00 25.14 ? 430 HOH A O    1 
HETATM 2325 O  O    . HOH E 5 .   ? -2.820  -17.962 31.270  1.00 23.09 ? 431 HOH A O    1 
HETATM 2326 O  O    . HOH E 5 .   ? -15.621 8.671   -2.420  1.00 30.87 ? 432 HOH A O    1 
HETATM 2327 O  O    . HOH E 5 .   ? -25.123 -7.935  9.105   1.00 15.82 ? 433 HOH A O    1 
HETATM 2328 O  O    . HOH E 5 .   ? -24.191 -0.920  26.705  1.00 16.94 ? 434 HOH A O    1 
HETATM 2329 O  O    . HOH E 5 .   ? -7.567  -8.852  -2.323  1.00 22.64 ? 435 HOH A O    1 
HETATM 2330 O  O    . HOH E 5 .   ? -1.474  9.289   28.187  1.00 21.66 ? 436 HOH A O    1 
HETATM 2331 O  O    . HOH E 5 .   ? -23.395 -3.239  6.859   1.00 17.53 ? 437 HOH A O    1 
HETATM 2332 O  O    . HOH E 5 .   ? -6.982  -14.965 31.728  1.00 19.48 ? 438 HOH A O    1 
HETATM 2333 O  O    . HOH E 5 .   ? -23.349 -17.539 3.535   1.00 27.95 ? 439 HOH A O    1 
HETATM 2334 O  O    . HOH E 5 .   ? -10.408 1.679   39.209  1.00 28.51 ? 440 HOH A O    1 
HETATM 2335 O  O    . HOH E 5 .   ? 2.542   -13.143 5.326   1.00 19.89 ? 441 HOH A O    1 
HETATM 2336 O  O    . HOH E 5 .   ? -1.774  11.265  26.002  1.00 26.62 ? 442 HOH A O    1 
HETATM 2337 O  O    . HOH E 5 .   ? -29.418 -5.940  24.540  1.00 18.58 ? 443 HOH A O    1 
HETATM 2338 O  O    . HOH E 5 .   ? -18.881 -21.250 14.879  1.00 19.03 ? 444 HOH A O    1 
HETATM 2339 O  O    . HOH E 5 .   ? -9.164  5.357   33.215  1.00 20.04 ? 445 HOH A O    1 
HETATM 2340 O  O    . HOH E 5 .   ? 4.969   -7.306  22.443  1.00 20.45 ? 446 HOH A O    1 
HETATM 2341 O  O    . HOH E 5 .   ? 10.286  -8.737  8.601   1.00 21.95 ? 447 HOH A O    1 
HETATM 2342 O  O    . HOH E 5 .   ? -1.380  4.259   -4.963  1.00 24.59 ? 448 HOH A O    1 
HETATM 2343 O  O    . HOH E 5 .   ? -20.008 -4.227  41.587  1.00 23.47 ? 449 HOH A O    1 
HETATM 2344 O  O    . HOH E 5 .   ? -18.487 -3.904  -2.618  1.00 21.37 ? 450 HOH A O    1 
HETATM 2345 O  O    . HOH E 5 .   ? -23.620 -13.480 11.325  1.00 15.93 ? 451 HOH A O    1 
HETATM 2346 O  O    . HOH E 5 .   ? -11.000 8.685   7.635   1.00 25.23 ? 452 HOH A O    1 
HETATM 2347 O  O    . HOH E 5 .   ? -14.002 14.155  27.325  1.00 19.51 ? 453 HOH A O    1 
HETATM 2348 O  O    . HOH E 5 .   ? 0.002   -19.700 10.829  1.00 26.71 ? 454 HOH A O    1 
HETATM 2349 O  O    . HOH E 5 .   ? -5.055  -20.931 21.730  1.00 19.21 ? 455 HOH A O    1 
HETATM 2350 O  O    . HOH E 5 .   ? -16.630 -16.553 -4.102  1.00 26.99 ? 456 HOH A O    1 
HETATM 2351 O  O    . HOH E 5 .   ? -0.611  14.253  16.232  1.00 19.72 ? 457 HOH A O    1 
HETATM 2352 O  O    . HOH E 5 .   ? -13.259 -22.310 8.849   1.00 18.45 ? 458 HOH A O    1 
HETATM 2353 O  O    . HOH E 5 .   ? 1.810   -14.293 20.722  1.00 22.44 ? 459 HOH A O    1 
HETATM 2354 O  O    . HOH E 5 .   ? -5.467  2.076   11.970  1.00 15.95 ? 460 HOH A O    1 
HETATM 2355 O  O    . HOH E 5 .   ? 2.948   -13.747 8.176   1.00 21.10 ? 461 HOH A O    1 
HETATM 2356 O  O    . HOH E 5 .   ? -5.472  2.301   37.504  1.00 29.66 ? 462 HOH A O    1 
HETATM 2357 O  O    . HOH E 5 .   ? -8.391  7.754   8.257   1.00 21.07 ? 463 HOH A O    1 
HETATM 2358 O  O    . HOH E 5 .   ? -0.861  -8.549  32.791  1.00 20.98 ? 464 HOH A O    1 
HETATM 2359 O  O    . HOH E 5 .   ? -25.018 4.653   8.260   1.00 23.93 ? 465 HOH A O    1 
HETATM 2360 O  O    . HOH E 5 .   ? 8.622   -4.677  23.765  1.00 20.36 ? 466 HOH A O    1 
HETATM 2361 O  O    . HOH E 5 .   ? -30.797 -0.532  16.199  1.00 26.76 ? 467 HOH A O    1 
HETATM 2362 O  O    . HOH E 5 .   ? -6.926  5.473   35.817  1.00 20.84 ? 468 HOH A O    1 
HETATM 2363 O  O    . HOH E 5 .   ? -1.992  -4.807  -7.060  1.00 22.27 ? 469 HOH A O    1 
HETATM 2364 O  O    . HOH E 5 .   ? -12.036 9.272   2.881   1.00 24.20 ? 470 HOH A O    1 
HETATM 2365 O  O    . HOH E 5 .   ? 9.229   -10.036 13.742  1.00 19.23 ? 471 HOH A O    1 
HETATM 2366 O  O    . HOH E 5 .   ? -12.846 3.148   -6.884  1.00 21.56 ? 472 HOH A O    1 
HETATM 2367 O  O    . HOH E 5 .   ? -4.369  4.023   10.639  1.00 38.13 ? 473 HOH A O    1 
HETATM 2368 O  O    . HOH E 5 .   ? -10.801 -20.624 24.997  1.00 16.12 ? 474 HOH A O    1 
HETATM 2369 O  O    . HOH E 5 .   ? -6.455  -19.795 23.944  1.00 21.29 ? 475 HOH A O    1 
HETATM 2370 O  O    . HOH E 5 .   ? -24.811 -9.516  2.034   1.00 29.20 ? 476 HOH A O    1 
HETATM 2371 O  O    . HOH E 5 .   ? -8.414  -22.321 10.505  1.00 22.27 ? 477 HOH A O    1 
HETATM 2372 O  O    . HOH E 5 .   ? -15.474 -16.254 25.640  1.00 30.28 ? 478 HOH A O    1 
HETATM 2373 O  O    . HOH E 5 .   ? -3.347  -18.013 0.108   1.00 22.80 ? 479 HOH A O    1 
HETATM 2374 O  O    . HOH E 5 .   ? -23.372 -0.329  34.777  1.00 22.11 ? 480 HOH A O    1 
HETATM 2375 O  O    . HOH E 5 .   ? -21.445 -19.977 6.576   1.00 27.14 ? 481 HOH A O    1 
HETATM 2376 O  O    . HOH E 5 .   ? 11.125  -3.807  7.573   1.00 22.96 ? 482 HOH A O    1 
HETATM 2377 O  O    . HOH E 5 .   ? -22.662 -12.406 25.050  1.00 26.07 ? 483 HOH A O    1 
HETATM 2378 O  O    . HOH E 5 .   ? -24.376 -3.440  29.521  1.00 23.57 ? 484 HOH A O    1 
HETATM 2379 O  O    . HOH E 5 .   ? 5.291   8.941   22.193  1.00 23.29 ? 485 HOH A O    1 
HETATM 2380 O  O    . HOH E 5 .   ? -4.797  -16.075 0.949   1.00 26.92 ? 486 HOH A O    1 
HETATM 2381 O  O    . HOH E 5 .   ? 1.800   -15.789 9.379   1.00 21.77 ? 487 HOH A O    1 
HETATM 2382 O  O    . HOH E 5 .   ? -18.631 -12.513 -3.404  1.00 24.84 ? 488 HOH A O    1 
HETATM 2383 O  O    . HOH E 5 .   ? -29.121 0.080   24.580  1.00 17.56 ? 489 HOH A O    1 
HETATM 2384 O  O    . HOH E 5 .   ? -3.695  -23.306 21.877  1.00 22.86 ? 490 HOH A O    1 
HETATM 2385 O  O    . HOH E 5 .   ? -25.545 9.520   13.070  1.00 23.48 ? 491 HOH A O    1 
HETATM 2386 O  O    . HOH E 5 .   ? 3.584   9.829   23.940  1.00 20.16 ? 492 HOH A O    1 
HETATM 2387 O  O    . HOH E 5 .   ? 1.459   3.183   -4.984  1.00 29.21 ? 493 HOH A O    1 
HETATM 2388 O  O    . HOH E 5 .   ? -20.482 -16.813 20.760  1.00 39.67 ? 494 HOH A O    1 
HETATM 2389 O  O    . HOH E 5 .   ? -12.274 10.438  5.698   1.00 25.38 ? 495 HOH A O    1 
HETATM 2390 O  O    . HOH E 5 .   ? -6.833  -5.142  37.752  1.00 20.54 ? 496 HOH A O    1 
HETATM 2391 O  O    . HOH E 5 .   ? -1.202  -17.491 -1.700  1.00 24.03 ? 497 HOH A O    1 
HETATM 2392 O  O    . HOH E 5 .   ? -9.924  15.079  12.311  1.00 19.98 ? 498 HOH A O    1 
HETATM 2393 O  O    . HOH E 5 .   ? 12.106  -6.628  7.885   1.00 23.48 ? 499 HOH A O    1 
HETATM 2394 O  O    . HOH E 5 .   ? -28.312 5.624   19.065  1.00 21.24 ? 500 HOH A O    1 
HETATM 2395 O  O    . HOH E 5 .   ? 8.421   -8.739  -7.867  1.00 25.11 ? 501 HOH A O    1 
HETATM 2396 O  O    . HOH E 5 .   ? -31.910 5.420   13.111  1.00 30.62 ? 502 HOH A O    1 
HETATM 2397 O  O    . HOH E 5 .   ? -20.693 13.799  28.730  1.00 31.15 ? 503 HOH A O    1 
HETATM 2398 O  O    . HOH E 5 .   ? -24.089 -0.191  32.120  1.00 28.59 ? 504 HOH A O    1 
HETATM 2399 O  O    . HOH E 5 .   ? -10.565 5.844   -4.208  1.00 26.12 ? 505 HOH A O    1 
HETATM 2400 O  O    . HOH E 5 .   ? -16.568 -15.707 32.976  1.00 23.96 ? 506 HOH A O    1 
HETATM 2401 O  O    . HOH E 5 .   ? -25.910 -10.772 17.821  1.00 20.04 ? 507 HOH A O    1 
HETATM 2402 O  O    . HOH E 5 .   ? -30.221 4.013   27.788  1.00 35.44 ? 508 HOH A O    1 
HETATM 2403 O  O    . HOH E 5 .   ? 1.888   8.007   28.099  1.00 25.57 ? 509 HOH A O    1 
HETATM 2404 O  O    . HOH E 5 .   ? -14.164 3.688   33.323  1.00 24.28 ? 510 HOH A O    1 
HETATM 2405 O  O    . HOH E 5 .   ? -11.676 10.581  0.634   1.00 25.97 ? 511 HOH A O    1 
HETATM 2406 O  O    . HOH E 5 .   ? -12.651 11.204  -5.156  1.00 24.13 ? 512 HOH A O    1 
HETATM 2407 O  O    . HOH E 5 .   ? -23.435 -11.065 17.264  1.00 26.71 ? 513 HOH A O    1 
HETATM 2408 O  O    . HOH E 5 .   ? -20.891 8.240   30.249  1.00 25.01 ? 514 HOH A O    1 
HETATM 2409 O  O    . HOH E 5 .   ? -22.822 -9.688  25.534  1.00 17.05 ? 515 HOH A O    1 
HETATM 2410 O  O    . HOH E 5 .   ? -33.020 1.738   12.050  1.00 25.53 ? 516 HOH A O    1 
HETATM 2411 O  O    . HOH E 5 .   ? 10.185  -1.383  5.052   1.00 31.29 ? 517 HOH A O    1 
HETATM 2412 O  O    . HOH E 5 .   ? -25.756 11.006  19.530  1.00 28.92 ? 518 HOH A O    1 
HETATM 2413 O  O    . HOH E 5 .   ? -4.029  -15.699 -2.227  1.00 26.09 ? 519 HOH A O    1 
HETATM 2414 O  O    . HOH E 5 .   ? -2.312  -11.796 31.793  1.00 24.07 ? 520 HOH A O    1 
HETATM 2415 O  O    . HOH E 5 .   ? -27.175 -0.312  4.208   1.00 58.63 ? 521 HOH A O    1 
HETATM 2416 O  O    . HOH E 5 .   ? -11.635 9.307   33.426  1.00 24.31 ? 522 HOH A O    1 
HETATM 2417 O  O    . HOH E 5 .   ? 8.445   3.141   27.996  1.00 27.30 ? 523 HOH A O    1 
HETATM 2418 O  O    . HOH E 5 .   ? -28.154 6.264   21.830  1.00 22.98 ? 524 HOH A O    1 
HETATM 2419 O  O    . HOH E 5 .   ? -13.071 -9.215  -3.047  1.00 20.95 ? 525 HOH A O    1 
HETATM 2420 O  O    . HOH E 5 .   ? -8.757  -19.931 26.789  1.00 20.95 ? 526 HOH A O    1 
HETATM 2421 O  O    . HOH E 5 .   ? 6.371   -11.486 15.501  1.00 28.31 ? 527 HOH A O    1 
HETATM 2422 O  O    . HOH E 5 .   ? -12.683 6.822   31.371  1.00 28.35 ? 528 HOH A O    1 
HETATM 2423 O  O    . HOH E 5 .   ? -6.043  -18.449 3.525   1.00 23.74 ? 529 HOH A O    1 
HETATM 2424 O  O    . HOH E 5 .   ? -13.546 -0.851  -6.232  1.00 28.73 ? 530 HOH A O    1 
HETATM 2425 O  O    . HOH E 5 .   ? -17.831 -19.496 35.501  1.00 25.91 ? 531 HOH A O    1 
HETATM 2426 O  O    . HOH E 5 .   ? -6.337  -21.166 1.486   1.00 34.11 ? 532 HOH A O    1 
HETATM 2427 O  O    . HOH E 5 .   ? -20.141 -2.236  43.357  1.00 36.39 ? 533 HOH A O    1 
HETATM 2428 O  O    . HOH E 5 .   ? -28.648 2.082   22.792  1.00 27.38 ? 534 HOH A O    1 
HETATM 2429 O  O    . HOH E 5 .   ? -15.060 6.091   32.775  1.00 25.66 ? 535 HOH A O    1 
HETATM 2430 O  O    . HOH E 5 .   ? -21.825 -13.948 23.150  1.00 23.38 ? 536 HOH A O    1 
HETATM 2431 O  O    . HOH E 5 .   ? -11.213 -23.741 12.325  1.00 22.93 ? 537 HOH A O    1 
HETATM 2432 O  O    . HOH E 5 .   ? 5.868   -14.325 9.059   1.00 26.53 ? 538 HOH A O    1 
HETATM 2433 O  O    . HOH E 5 .   ? -24.034 -3.631  4.004   1.00 34.60 ? 539 HOH A O    1 
HETATM 2434 O  O    . HOH E 5 .   ? -12.615 12.571  29.398  1.00 23.02 ? 540 HOH A O    1 
HETATM 2435 O  O    . HOH E 5 .   ? 5.186   -10.542 13.291  1.00 32.82 ? 541 HOH A O    1 
HETATM 2436 O  O    . HOH E 5 .   ? 1.412   -16.834 -1.806  1.00 41.67 ? 542 HOH A O    1 
HETATM 2437 O  O    . HOH E 5 .   ? -21.929 -14.371 18.843  1.00 26.14 ? 543 HOH A O    1 
HETATM 2438 O  O    . HOH E 5 .   ? -2.191  -0.150  10.112  1.00 23.39 ? 544 HOH A O    1 
HETATM 2439 O  O    . HOH E 5 .   ? 6.487   -5.734  6.715   1.00 23.76 ? 545 HOH A O    1 
HETATM 2440 O  O    . HOH E 5 .   ? -1.309  2.891   -7.119  1.00 31.59 ? 546 HOH A O    1 
HETATM 2441 O  O    . HOH E 5 .   ? -0.318  -2.361  39.713  1.00 29.77 ? 547 HOH A O    1 
HETATM 2442 O  O    . HOH E 5 .   ? -19.174 -23.684 18.369  1.00 33.60 ? 548 HOH A O    1 
HETATM 2443 O  O    . HOH E 5 .   ? -28.054 4.464   23.747  1.00 22.72 ? 549 HOH A O    1 
HETATM 2444 O  O    . HOH E 5 .   ? -2.893  6.089   -1.238  1.00 25.54 ? 550 HOH A O    1 
HETATM 2445 O  O    . HOH E 5 .   ? -17.209 -1.090  40.296  1.00 28.27 ? 551 HOH A O    1 
HETATM 2446 O  O    . HOH E 5 .   ? -7.866  -4.860  40.262  1.00 36.21 ? 553 HOH A O    1 
HETATM 2447 O  O    . HOH E 5 .   ? -2.840  -19.550 6.366   1.00 27.37 ? 554 HOH A O    1 
HETATM 2448 O  O    . HOH E 5 .   ? -0.841  -17.490 18.296  1.00 27.91 ? 555 HOH A O    1 
HETATM 2449 O  O    . HOH E 5 .   ? -27.792 11.981  5.726   1.00 41.72 ? 556 HOH A O    1 
HETATM 2450 O  O    . HOH E 5 .   ? -21.022 -6.937  -2.034  1.00 35.15 ? 557 HOH A O    1 
HETATM 2451 O  O    . HOH E 5 .   ? 7.568   -8.203  -0.888  1.00 29.56 ? 558 HOH A O    1 
HETATM 2452 O  O    . HOH E 5 .   ? 5.318   -10.949 19.313  1.00 26.65 ? 559 HOH A O    1 
HETATM 2453 O  O    . HOH E 5 .   ? 7.266   -3.963  -10.653 1.00 28.93 ? 560 HOH A O    1 
HETATM 2454 O  O    . HOH E 5 .   ? -4.775  6.369   -2.946  1.00 47.00 ? 561 HOH A O    1 
HETATM 2455 O  O    . HOH E 5 .   ? -26.574 -7.578  30.496  1.00 27.37 ? 562 HOH A O    1 
HETATM 2456 O  O    . HOH E 5 .   ? -18.491 -8.846  35.153  1.00 34.10 ? 563 HOH A O    1 
HETATM 2457 O  O    . HOH E 5 .   ? 1.437   -4.164  -12.576 1.00 25.77 ? 564 HOH A O    1 
HETATM 2458 O  O    . HOH E 5 .   ? 4.870   -13.307 -5.633  1.00 21.43 ? 565 HOH A O    1 
HETATM 2459 O  O    . HOH E 5 .   ? 4.355   -11.368 23.402  1.00 37.84 ? 566 HOH A O    1 
HETATM 2460 O  O    . HOH E 5 .   ? -11.296 12.356  7.216   1.00 33.41 ? 567 HOH A O    1 
HETATM 2461 O  O    . HOH E 5 .   ? 6.172   -5.615  4.052   1.00 33.28 ? 568 HOH A O    1 
HETATM 2462 O  O    . HOH E 5 .   ? -3.698  -20.141 27.308  1.00 29.19 ? 569 HOH A O    1 
HETATM 2463 O  O    . HOH E 5 .   ? 5.686   9.104   18.568  1.00 34.16 ? 570 HOH A O    1 
HETATM 2464 O  O    . HOH E 5 .   ? -2.715  -19.084 21.496  1.00 29.02 ? 571 HOH A O    1 
HETATM 2465 O  O    . HOH E 5 .   ? -28.556 -1.071  28.372  1.00 40.53 ? 572 HOH A O    1 
HETATM 2466 O  O    . HOH E 5 .   ? -5.580  15.425  12.133  1.00 26.52 ? 573 HOH A O    1 
HETATM 2467 O  O    . HOH E 5 .   ? 3.193   -2.793  -14.289 1.00 30.13 ? 574 HOH A O    1 
HETATM 2468 O  O    . HOH E 5 .   ? -3.979  -1.198  11.508  1.00 22.32 ? 575 HOH A O    1 
HETATM 2469 O  O    . HOH E 5 .   ? -16.640 -14.990 28.875  1.00 34.65 ? 576 HOH A O    1 
HETATM 2470 O  O    . HOH E 5 .   ? 6.082   5.418   29.482  1.00 23.48 ? 577 HOH A O    1 
HETATM 2471 O  O    . HOH E 5 .   ? -3.439  4.464   7.154   1.00 29.48 ? 578 HOH A O    1 
HETATM 2472 O  O    . HOH E 5 .   ? -16.354 5.271   -8.343  1.00 24.91 ? 579 HOH A O    1 
HETATM 2473 O  O    . HOH E 5 .   ? 0.448   -9.916  -5.365  1.00 27.90 ? 580 HOH A O    1 
HETATM 2474 O  O    . HOH E 5 .   ? -7.221  -8.564  -6.934  1.00 28.45 ? 581 HOH A O    1 
HETATM 2475 O  O    . HOH E 5 .   ? -27.434 -5.485  27.698  1.00 21.43 ? 582 HOH A O    1 
HETATM 2476 O  O    . HOH E 5 .   ? -11.594 0.800   -7.816  1.00 31.69 ? 583 HOH A O    1 
HETATM 2477 O  O    . HOH E 5 .   ? -26.364 6.381   26.976  1.00 26.50 ? 584 HOH A O    1 
HETATM 2478 O  O    . HOH E 5 .   ? -7.341  -10.188 -4.566  1.00 28.29 ? 585 HOH A O    1 
HETATM 2479 O  O    . HOH E 5 .   ? -6.054  -20.918 26.272  1.00 30.55 ? 586 HOH A O    1 
HETATM 2480 O  O    . HOH E 5 .   ? 3.442   -13.846 12.660  1.00 23.01 ? 587 HOH A O    1 
HETATM 2481 O  O    . HOH E 5 .   ? -19.455 14.214  9.005   1.00 29.92 ? 588 HOH A O    1 
HETATM 2482 O  O    . HOH E 5 .   ? 3.025   6.507   32.359  1.00 28.01 ? 589 HOH A O    1 
HETATM 2483 O  O    . HOH E 5 .   ? 4.542   -5.641  34.397  1.00 33.19 ? 590 HOH A O    1 
HETATM 2484 O  O    . HOH E 5 .   ? 2.100   -2.589  37.681  1.00 37.68 ? 591 HOH A O    1 
HETATM 2485 O  O    . HOH E 5 .   ? -27.034 -1.432  26.267  1.00 22.42 ? 592 HOH A O    1 
HETATM 2486 O  O    . HOH E 5 .   ? -4.908  -7.326  38.140  1.00 32.98 ? 593 HOH A O    1 
HETATM 2487 O  O    . HOH E 5 .   ? -13.561 -17.016 0.035   1.00 26.50 ? 594 HOH A O    1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   262 262 ZN  ZN  A . 
C 3 DMS 1   263 263 DMS DMS A . 
D 4 JDR 1   264 264 JDR JDR A . 
E 5 HOH 1   126 126 HOH HOH A . 
E 5 HOH 2   265 265 HOH HOH A . 
E 5 HOH 3   266 266 HOH HOH A . 
E 5 HOH 4   267 267 HOH HOH A . 
E 5 HOH 5   268 268 HOH HOH A . 
E 5 HOH 6   269 269 HOH HOH A . 
E 5 HOH 7   270 270 HOH HOH A . 
E 5 HOH 8   271 271 HOH HOH A . 
E 5 HOH 9   272 272 HOH HOH A . 
E 5 HOH 10  273 273 HOH HOH A . 
E 5 HOH 11  274 274 HOH HOH A . 
E 5 HOH 12  275 275 HOH HOH A . 
E 5 HOH 13  276 276 HOH HOH A . 
E 5 HOH 14  277 277 HOH HOH A . 
E 5 HOH 15  278 278 HOH HOH A . 
E 5 HOH 16  279 279 HOH HOH A . 
E 5 HOH 17  280 280 HOH HOH A . 
E 5 HOH 18  281 281 HOH HOH A . 
E 5 HOH 19  282 282 HOH HOH A . 
E 5 HOH 20  283 283 HOH HOH A . 
E 5 HOH 21  284 284 HOH HOH A . 
E 5 HOH 22  285 285 HOH HOH A . 
E 5 HOH 23  286 286 HOH HOH A . 
E 5 HOH 24  287 287 HOH HOH A . 
E 5 HOH 25  288 288 HOH HOH A . 
E 5 HOH 26  289 289 HOH HOH A . 
E 5 HOH 27  290 290 HOH HOH A . 
E 5 HOH 28  291 291 HOH HOH A . 
E 5 HOH 29  292 292 HOH HOH A . 
E 5 HOH 30  293 293 HOH HOH A . 
E 5 HOH 31  294 294 HOH HOH A . 
E 5 HOH 32  295 295 HOH HOH A . 
E 5 HOH 33  296 296 HOH HOH A . 
E 5 HOH 34  297 297 HOH HOH A . 
E 5 HOH 35  298 298 HOH HOH A . 
E 5 HOH 36  299 299 HOH HOH A . 
E 5 HOH 37  300 300 HOH HOH A . 
E 5 HOH 38  301 301 HOH HOH A . 
E 5 HOH 39  302 302 HOH HOH A . 
E 5 HOH 40  303 303 HOH HOH A . 
E 5 HOH 41  304 304 HOH HOH A . 
E 5 HOH 42  305 305 HOH HOH A . 
E 5 HOH 43  306 306 HOH HOH A . 
E 5 HOH 44  307 307 HOH HOH A . 
E 5 HOH 45  308 308 HOH HOH A . 
E 5 HOH 46  309 309 HOH HOH A . 
E 5 HOH 47  310 310 HOH HOH A . 
E 5 HOH 48  311 311 HOH HOH A . 
E 5 HOH 49  312 312 HOH HOH A . 
E 5 HOH 50  313 313 HOH HOH A . 
E 5 HOH 51  314 314 HOH HOH A . 
E 5 HOH 52  315 315 HOH HOH A . 
E 5 HOH 53  316 316 HOH HOH A . 
E 5 HOH 54  317 317 HOH HOH A . 
E 5 HOH 55  318 318 HOH HOH A . 
E 5 HOH 56  319 319 HOH HOH A . 
E 5 HOH 57  320 320 HOH HOH A . 
E 5 HOH 58  321 321 HOH HOH A . 
E 5 HOH 59  322 322 HOH HOH A . 
E 5 HOH 60  323 323 HOH HOH A . 
E 5 HOH 61  324 324 HOH HOH A . 
E 5 HOH 62  325 325 HOH HOH A . 
E 5 HOH 63  326 326 HOH HOH A . 
E 5 HOH 64  327 327 HOH HOH A . 
E 5 HOH 65  328 328 HOH HOH A . 
E 5 HOH 66  329 329 HOH HOH A . 
E 5 HOH 67  330 330 HOH HOH A . 
E 5 HOH 68  331 331 HOH HOH A . 
E 5 HOH 69  332 332 HOH HOH A . 
E 5 HOH 70  333 333 HOH HOH A . 
E 5 HOH 71  334 334 HOH HOH A . 
E 5 HOH 72  335 335 HOH HOH A . 
E 5 HOH 73  336 336 HOH HOH A . 
E 5 HOH 74  337 337 HOH HOH A . 
E 5 HOH 75  338 338 HOH HOH A . 
E 5 HOH 76  339 339 HOH HOH A . 
E 5 HOH 77  340 340 HOH HOH A . 
E 5 HOH 78  341 341 HOH HOH A . 
E 5 HOH 79  342 342 HOH HOH A . 
E 5 HOH 80  343 343 HOH HOH A . 
E 5 HOH 81  344 344 HOH HOH A . 
E 5 HOH 82  345 345 HOH HOH A . 
E 5 HOH 83  346 346 HOH HOH A . 
E 5 HOH 84  347 347 HOH HOH A . 
E 5 HOH 85  348 348 HOH HOH A . 
E 5 HOH 86  349 349 HOH HOH A . 
E 5 HOH 87  350 350 HOH HOH A . 
E 5 HOH 88  351 351 HOH HOH A . 
E 5 HOH 89  352 352 HOH HOH A . 
E 5 HOH 90  353 353 HOH HOH A . 
E 5 HOH 91  354 354 HOH HOH A . 
E 5 HOH 92  355 355 HOH HOH A . 
E 5 HOH 93  356 356 HOH HOH A . 
E 5 HOH 94  357 357 HOH HOH A . 
E 5 HOH 95  358 358 HOH HOH A . 
E 5 HOH 96  359 359 HOH HOH A . 
E 5 HOH 97  360 360 HOH HOH A . 
E 5 HOH 98  361 361 HOH HOH A . 
E 5 HOH 99  362 362 HOH HOH A . 
E 5 HOH 100 363 363 HOH HOH A . 
E 5 HOH 101 364 364 HOH HOH A . 
E 5 HOH 102 365 365 HOH HOH A . 
E 5 HOH 103 366 366 HOH HOH A . 
E 5 HOH 104 367 367 HOH HOH A . 
E 5 HOH 105 368 368 HOH HOH A . 
E 5 HOH 106 369 369 HOH HOH A . 
E 5 HOH 107 370 370 HOH HOH A . 
E 5 HOH 108 371 371 HOH HOH A . 
E 5 HOH 109 372 372 HOH HOH A . 
E 5 HOH 110 373 373 HOH HOH A . 
E 5 HOH 111 374 374 HOH HOH A . 
E 5 HOH 112 375 375 HOH HOH A . 
E 5 HOH 113 376 376 HOH HOH A . 
E 5 HOH 114 377 377 HOH HOH A . 
E 5 HOH 115 378 378 HOH HOH A . 
E 5 HOH 116 379 379 HOH HOH A . 
E 5 HOH 117 380 380 HOH HOH A . 
E 5 HOH 118 381 381 HOH HOH A . 
E 5 HOH 119 382 382 HOH HOH A . 
E 5 HOH 120 383 383 HOH HOH A . 
E 5 HOH 121 384 384 HOH HOH A . 
E 5 HOH 122 385 385 HOH HOH A . 
E 5 HOH 123 386 386 HOH HOH A . 
E 5 HOH 124 387 387 HOH HOH A . 
E 5 HOH 125 388 388 HOH HOH A . 
E 5 HOH 126 389 389 HOH HOH A . 
E 5 HOH 127 390 390 HOH HOH A . 
E 5 HOH 128 391 391 HOH HOH A . 
E 5 HOH 129 392 392 HOH HOH A . 
E 5 HOH 130 393 393 HOH HOH A . 
E 5 HOH 131 394 394 HOH HOH A . 
E 5 HOH 132 395 395 HOH HOH A . 
E 5 HOH 133 396 396 HOH HOH A . 
E 5 HOH 134 397 397 HOH HOH A . 
E 5 HOH 135 398 398 HOH HOH A . 
E 5 HOH 136 399 399 HOH HOH A . 
E 5 HOH 137 400 400 HOH HOH A . 
E 5 HOH 138 401 401 HOH HOH A . 
E 5 HOH 139 402 402 HOH HOH A . 
E 5 HOH 140 403 403 HOH HOH A . 
E 5 HOH 141 404 404 HOH HOH A . 
E 5 HOH 142 405 405 HOH HOH A . 
E 5 HOH 143 406 406 HOH HOH A . 
E 5 HOH 144 407 407 HOH HOH A . 
E 5 HOH 145 408 408 HOH HOH A . 
E 5 HOH 146 409 409 HOH HOH A . 
E 5 HOH 147 410 410 HOH HOH A . 
E 5 HOH 148 411 411 HOH HOH A . 
E 5 HOH 149 412 412 HOH HOH A . 
E 5 HOH 150 413 413 HOH HOH A . 
E 5 HOH 151 414 414 HOH HOH A . 
E 5 HOH 152 415 415 HOH HOH A . 
E 5 HOH 153 416 416 HOH HOH A . 
E 5 HOH 154 417 417 HOH HOH A . 
E 5 HOH 155 418 418 HOH HOH A . 
E 5 HOH 156 419 419 HOH HOH A . 
E 5 HOH 157 420 420 HOH HOH A . 
E 5 HOH 158 421 421 HOH HOH A . 
E 5 HOH 159 422 422 HOH HOH A . 
E 5 HOH 160 423 423 HOH HOH A . 
E 5 HOH 161 424 424 HOH HOH A . 
E 5 HOH 162 425 425 HOH HOH A . 
E 5 HOH 163 426 426 HOH HOH A . 
E 5 HOH 164 427 427 HOH HOH A . 
E 5 HOH 165 428 428 HOH HOH A . 
E 5 HOH 166 429 429 HOH HOH A . 
E 5 HOH 167 430 430 HOH HOH A . 
E 5 HOH 168 431 431 HOH HOH A . 
E 5 HOH 169 432 432 HOH HOH A . 
E 5 HOH 170 433 433 HOH HOH A . 
E 5 HOH 171 434 434 HOH HOH A . 
E 5 HOH 172 435 435 HOH HOH A . 
E 5 HOH 173 436 436 HOH HOH A . 
E 5 HOH 174 437 437 HOH HOH A . 
E 5 HOH 175 438 438 HOH HOH A . 
E 5 HOH 176 439 439 HOH HOH A . 
E 5 HOH 177 440 440 HOH HOH A . 
E 5 HOH 178 441 441 HOH HOH A . 
E 5 HOH 179 442 442 HOH HOH A . 
E 5 HOH 180 443 443 HOH HOH A . 
E 5 HOH 181 444 444 HOH HOH A . 
E 5 HOH 182 445 445 HOH HOH A . 
E 5 HOH 183 446 446 HOH HOH A . 
E 5 HOH 184 447 447 HOH HOH A . 
E 5 HOH 185 448 448 HOH HOH A . 
E 5 HOH 186 449 449 HOH HOH A . 
E 5 HOH 187 450 450 HOH HOH A . 
E 5 HOH 188 451 451 HOH HOH A . 
E 5 HOH 189 452 452 HOH HOH A . 
E 5 HOH 190 453 453 HOH HOH A . 
E 5 HOH 191 454 454 HOH HOH A . 
E 5 HOH 192 455 455 HOH HOH A . 
E 5 HOH 193 456 456 HOH HOH A . 
E 5 HOH 194 457 457 HOH HOH A . 
E 5 HOH 195 458 458 HOH HOH A . 
E 5 HOH 196 459 459 HOH HOH A . 
E 5 HOH 197 460 460 HOH HOH A . 
E 5 HOH 198 461 461 HOH HOH A . 
E 5 HOH 199 462 462 HOH HOH A . 
E 5 HOH 200 463 463 HOH HOH A . 
E 5 HOH 201 464 464 HOH HOH A . 
E 5 HOH 202 465 465 HOH HOH A . 
E 5 HOH 203 466 466 HOH HOH A . 
E 5 HOH 204 467 467 HOH HOH A . 
E 5 HOH 205 468 468 HOH HOH A . 
E 5 HOH 206 469 469 HOH HOH A . 
E 5 HOH 207 470 470 HOH HOH A . 
E 5 HOH 208 471 471 HOH HOH A . 
E 5 HOH 209 472 472 HOH HOH A . 
E 5 HOH 210 473 473 HOH HOH A . 
E 5 HOH 211 474 474 HOH HOH A . 
E 5 HOH 212 475 475 HOH HOH A . 
E 5 HOH 213 476 476 HOH HOH A . 
E 5 HOH 214 477 477 HOH HOH A . 
E 5 HOH 215 478 478 HOH HOH A . 
E 5 HOH 216 479 479 HOH HOH A . 
E 5 HOH 217 480 480 HOH HOH A . 
E 5 HOH 218 481 481 HOH HOH A . 
E 5 HOH 219 482 482 HOH HOH A . 
E 5 HOH 220 483 483 HOH HOH A . 
E 5 HOH 221 484 484 HOH HOH A . 
E 5 HOH 222 485 485 HOH HOH A . 
E 5 HOH 223 486 486 HOH HOH A . 
E 5 HOH 224 487 487 HOH HOH A . 
E 5 HOH 225 488 488 HOH HOH A . 
E 5 HOH 226 489 489 HOH HOH A . 
E 5 HOH 227 490 490 HOH HOH A . 
E 5 HOH 228 491 491 HOH HOH A . 
E 5 HOH 229 492 492 HOH HOH A . 
E 5 HOH 230 493 493 HOH HOH A . 
E 5 HOH 231 494 494 HOH HOH A . 
E 5 HOH 232 495 495 HOH HOH A . 
E 5 HOH 233 496 496 HOH HOH A . 
E 5 HOH 234 497 497 HOH HOH A . 
E 5 HOH 235 498 498 HOH HOH A . 
E 5 HOH 236 499 499 HOH HOH A . 
E 5 HOH 237 500 500 HOH HOH A . 
E 5 HOH 238 501 501 HOH HOH A . 
E 5 HOH 239 502 502 HOH HOH A . 
E 5 HOH 240 503 503 HOH HOH A . 
E 5 HOH 241 504 504 HOH HOH A . 
E 5 HOH 242 505 505 HOH HOH A . 
E 5 HOH 243 506 506 HOH HOH A . 
E 5 HOH 244 507 507 HOH HOH A . 
E 5 HOH 245 508 508 HOH HOH A . 
E 5 HOH 246 509 509 HOH HOH A . 
E 5 HOH 247 510 510 HOH HOH A . 
E 5 HOH 248 511 511 HOH HOH A . 
E 5 HOH 249 512 512 HOH HOH A . 
E 5 HOH 250 513 513 HOH HOH A . 
E 5 HOH 251 514 514 HOH HOH A . 
E 5 HOH 252 515 515 HOH HOH A . 
E 5 HOH 253 516 516 HOH HOH A . 
E 5 HOH 254 517 517 HOH HOH A . 
E 5 HOH 255 518 518 HOH HOH A . 
E 5 HOH 256 519 519 HOH HOH A . 
E 5 HOH 257 520 520 HOH HOH A . 
E 5 HOH 258 521 521 HOH HOH A . 
E 5 HOH 259 522 522 HOH HOH A . 
E 5 HOH 260 523 523 HOH HOH A . 
E 5 HOH 261 524 524 HOH HOH A . 
E 5 HOH 262 525 525 HOH HOH A . 
E 5 HOH 263 526 526 HOH HOH A . 
E 5 HOH 264 527 527 HOH HOH A . 
E 5 HOH 265 528 528 HOH HOH A . 
E 5 HOH 266 529 529 HOH HOH A . 
E 5 HOH 267 530 530 HOH HOH A . 
E 5 HOH 268 531 531 HOH HOH A . 
E 5 HOH 269 532 532 HOH HOH A . 
E 5 HOH 270 533 533 HOH HOH A . 
E 5 HOH 271 534 534 HOH HOH A . 
E 5 HOH 272 535 535 HOH HOH A . 
E 5 HOH 273 536 536 HOH HOH A . 
E 5 HOH 274 537 537 HOH HOH A . 
E 5 HOH 275 538 538 HOH HOH A . 
E 5 HOH 276 539 539 HOH HOH A . 
E 5 HOH 277 540 540 HOH HOH A . 
E 5 HOH 278 541 541 HOH HOH A . 
E 5 HOH 279 542 542 HOH HOH A . 
E 5 HOH 280 543 543 HOH HOH A . 
E 5 HOH 281 544 544 HOH HOH A . 
E 5 HOH 282 545 545 HOH HOH A . 
E 5 HOH 283 546 546 HOH HOH A . 
E 5 HOH 284 547 547 HOH HOH A . 
E 5 HOH 285 548 548 HOH HOH A . 
E 5 HOH 286 549 549 HOH HOH A . 
E 5 HOH 287 550 550 HOH HOH A . 
E 5 HOH 288 551 551 HOH HOH A . 
E 5 HOH 289 553 553 HOH HOH A . 
E 5 HOH 290 554 554 HOH HOH A . 
E 5 HOH 291 555 555 HOH HOH A . 
E 5 HOH 292 556 556 HOH HOH A . 
E 5 HOH 293 557 557 HOH HOH A . 
E 5 HOH 294 558 558 HOH HOH A . 
E 5 HOH 295 559 559 HOH HOH A . 
E 5 HOH 296 560 560 HOH HOH A . 
E 5 HOH 297 561 561 HOH HOH A . 
E 5 HOH 298 562 562 HOH HOH A . 
E 5 HOH 299 563 563 HOH HOH A . 
E 5 HOH 300 564 564 HOH HOH A . 
E 5 HOH 301 565 565 HOH HOH A . 
E 5 HOH 302 566 566 HOH HOH A . 
E 5 HOH 303 567 567 HOH HOH A . 
E 5 HOH 304 568 568 HOH HOH A . 
E 5 HOH 305 569 569 HOH HOH A . 
E 5 HOH 306 570 570 HOH HOH A . 
E 5 HOH 307 571 571 HOH HOH A . 
E 5 HOH 308 572 572 HOH HOH A . 
E 5 HOH 309 573 573 HOH HOH A . 
E 5 HOH 310 574 574 HOH HOH A . 
E 5 HOH 311 575 575 HOH HOH A . 
E 5 HOH 312 576 576 HOH HOH A . 
E 5 HOH 313 577 577 HOH HOH A . 
E 5 HOH 314 578 578 HOH HOH A . 
E 5 HOH 315 579 579 HOH HOH A . 
E 5 HOH 316 580 580 HOH HOH A . 
E 5 HOH 317 581 581 HOH HOH A . 
E 5 HOH 318 582 582 HOH HOH A . 
E 5 HOH 319 583 583 HOH HOH A . 
E 5 HOH 320 584 584 HOH HOH A . 
E 5 HOH 321 585 585 HOH HOH A . 
E 5 HOH 322 586 586 HOH HOH A . 
E 5 HOH 323 587 587 HOH HOH A . 
E 5 HOH 324 588 588 HOH HOH A . 
E 5 HOH 325 589 589 HOH HOH A . 
E 5 HOH 326 590 590 HOH HOH A . 
E 5 HOH 327 591 591 HOH HOH A . 
E 5 HOH 328 592 592 HOH HOH A . 
E 5 HOH 329 593 593 HOH HOH A . 
E 5 HOH 330 594 594 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 
# 
_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_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 2010-10-20 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-08 
4 'Structure model' 1 3 2023-11-01 
# 
_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' 'Version format compliance' 
2 3 'Structure model' 'Refinement description'    
3 4 'Structure model' 'Data collection'           
4 4 'Structure model' 'Database references'       
5 4 'Structure model' 'Derived calculations'      
6 4 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' software                      
2 4 'Structure model' chem_comp_atom                
3 4 'Structure model' chem_comp_bond                
4 4 'Structure model' database_2                    
5 4 'Structure model' diffrn_source                 
6 4 'Structure model' pdbx_initial_refinement_model 
7 4 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_software.name'                       
2 4 'Structure model' '_database_2.pdbx_DOI'                 
3 4 'Structure model' '_database_2.pdbx_database_accession'  
4 4 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
5 4 'Structure model' '_struct_site.pdbx_auth_asym_id'       
6 4 'Structure model' '_struct_site.pdbx_auth_comp_id'       
7 4 'Structure model' '_struct_site.pdbx_auth_seq_id'        
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .                            ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .                            ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.2.19                       22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006                        'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345      'v. 0.9.7 on RedHat Linux 8' ?               ?       ?                    ?                        'data collection' ? 
?          ? 5 
O           .                            ?               ?       ?                    ?                        'model building'  ? 
?          ? 6 
# 
_pdbx_entry_details.entry_id                 3M5E 
_pdbx_entry_details.nonpolymer_details       'METAL ION NATURALLY OCCURS IN CARBONIC ANHYDRASES.' 
_pdbx_entry_details.sequence_details         '126 IS SKIPPED IN THE NUMBERING.' 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   ? 
# 
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  ? ? -124.43 -81.29  
2 1 LYS A 76  ? ? -109.16 -81.29  
3 1 LYS A 111 ? ? 72.60   -4.09   
4 1 ASN A 244 ? ? -94.62  48.69   
5 1 LYS A 252 ? ? 53.48   -135.41 
6 1 ASN A 253 ? ? -91.35  58.76   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
JDR N1   N  Y N 193 
JDR C2   C  Y N 194 
JDR N3   N  Y N 195 
JDR C4   C  Y N 196 
JDR C5   C  Y N 197 
JDR C6   C  Y N 198 
JDR N7   N  N N 199 
JDR C8   C  Y N 200 
JDR C9   C  Y N 201 
JDR C10  C  Y N 202 
JDR C11  C  Y N 203 
JDR C12  C  Y N 204 
JDR C13  C  Y N 205 
JDR S14  S  N N 206 
JDR O15  O  N N 207 
JDR O16  O  N N 208 
JDR N17  N  N N 209 
JDR C18  C  N N 210 
JDR O19  O  N N 211 
JDR CL20 CL N N 212 
JDR S21  S  N N 213 
JDR C22  C  N N 214 
JDR C23  C  N N 215 
JDR HN7  H  N N 216 
JDR H9   H  N N 217 
JDR H10  H  N N 218 
JDR H12  H  N N 219 
JDR H13  H  N N 220 
JDR HN17 H  N N 221 
JDR HN1A H  N N 222 
JDR H18  H  N N 223 
JDR H22  H  N N 224 
JDR H22A H  N N 225 
JDR H22B H  N N 226 
JDR H23  H  N N 227 
JDR H23A H  N N 228 
LEU N    N  N N 229 
LEU CA   C  N S 230 
LEU C    C  N N 231 
LEU O    O  N N 232 
LEU CB   C  N N 233 
LEU CG   C  N N 234 
LEU CD1  C  N N 235 
LEU CD2  C  N N 236 
LEU OXT  O  N N 237 
LEU H    H  N N 238 
LEU H2   H  N N 239 
LEU HA   H  N N 240 
LEU HB2  H  N N 241 
LEU HB3  H  N N 242 
LEU HG   H  N N 243 
LEU HD11 H  N N 244 
LEU HD12 H  N N 245 
LEU HD13 H  N N 246 
LEU HD21 H  N N 247 
LEU HD22 H  N N 248 
LEU HD23 H  N N 249 
LEU HXT  H  N N 250 
LYS N    N  N N 251 
LYS CA   C  N S 252 
LYS C    C  N N 253 
LYS O    O  N N 254 
LYS CB   C  N N 255 
LYS CG   C  N N 256 
LYS CD   C  N N 257 
LYS CE   C  N N 258 
LYS NZ   N  N N 259 
LYS OXT  O  N N 260 
LYS H    H  N N 261 
LYS H2   H  N N 262 
LYS HA   H  N N 263 
LYS HB2  H  N N 264 
LYS HB3  H  N N 265 
LYS HG2  H  N N 266 
LYS HG3  H  N N 267 
LYS HD2  H  N N 268 
LYS HD3  H  N N 269 
LYS HE2  H  N N 270 
LYS HE3  H  N N 271 
LYS HZ1  H  N N 272 
LYS HZ2  H  N N 273 
LYS HZ3  H  N N 274 
LYS HXT  H  N N 275 
MET N    N  N N 276 
MET CA   C  N S 277 
MET C    C  N N 278 
MET O    O  N N 279 
MET CB   C  N N 280 
MET CG   C  N N 281 
MET SD   S  N N 282 
MET CE   C  N N 283 
MET OXT  O  N N 284 
MET H    H  N N 285 
MET H2   H  N N 286 
MET HA   H  N N 287 
MET HB2  H  N N 288 
MET HB3  H  N N 289 
MET HG2  H  N N 290 
MET HG3  H  N N 291 
MET HE1  H  N N 292 
MET HE2  H  N N 293 
MET HE3  H  N N 294 
MET HXT  H  N N 295 
PHE N    N  N N 296 
PHE CA   C  N S 297 
PHE C    C  N N 298 
PHE O    O  N N 299 
PHE CB   C  N N 300 
PHE CG   C  Y N 301 
PHE CD1  C  Y N 302 
PHE CD2  C  Y N 303 
PHE CE1  C  Y N 304 
PHE CE2  C  Y N 305 
PHE CZ   C  Y N 306 
PHE OXT  O  N N 307 
PHE H    H  N N 308 
PHE H2   H  N N 309 
PHE HA   H  N N 310 
PHE HB2  H  N N 311 
PHE HB3  H  N N 312 
PHE HD1  H  N N 313 
PHE HD2  H  N N 314 
PHE HE1  H  N N 315 
PHE HE2  H  N N 316 
PHE HZ   H  N N 317 
PHE HXT  H  N N 318 
PRO N    N  N N 319 
PRO CA   C  N S 320 
PRO C    C  N N 321 
PRO O    O  N N 322 
PRO CB   C  N N 323 
PRO CG   C  N N 324 
PRO CD   C  N N 325 
PRO OXT  O  N N 326 
PRO H    H  N N 327 
PRO HA   H  N N 328 
PRO HB2  H  N N 329 
PRO HB3  H  N N 330 
PRO HG2  H  N N 331 
PRO HG3  H  N N 332 
PRO HD2  H  N N 333 
PRO HD3  H  N N 334 
PRO HXT  H  N N 335 
SER N    N  N N 336 
SER CA   C  N S 337 
SER C    C  N N 338 
SER O    O  N N 339 
SER CB   C  N N 340 
SER OG   O  N N 341 
SER OXT  O  N N 342 
SER H    H  N N 343 
SER H2   H  N N 344 
SER HA   H  N N 345 
SER HB2  H  N N 346 
SER HB3  H  N N 347 
SER HG   H  N N 348 
SER HXT  H  N N 349 
THR N    N  N N 350 
THR CA   C  N S 351 
THR C    C  N N 352 
THR O    O  N N 353 
THR CB   C  N R 354 
THR OG1  O  N N 355 
THR CG2  C  N N 356 
THR OXT  O  N N 357 
THR H    H  N N 358 
THR H2   H  N N 359 
THR HA   H  N N 360 
THR HB   H  N N 361 
THR HG1  H  N N 362 
THR HG21 H  N N 363 
THR HG22 H  N N 364 
THR HG23 H  N N 365 
THR HXT  H  N N 366 
TRP N    N  N N 367 
TRP CA   C  N S 368 
TRP C    C  N N 369 
TRP O    O  N N 370 
TRP CB   C  N N 371 
TRP CG   C  Y N 372 
TRP CD1  C  Y N 373 
TRP CD2  C  Y N 374 
TRP NE1  N  Y N 375 
TRP CE2  C  Y N 376 
TRP CE3  C  Y N 377 
TRP CZ2  C  Y N 378 
TRP CZ3  C  Y N 379 
TRP CH2  C  Y N 380 
TRP OXT  O  N N 381 
TRP H    H  N N 382 
TRP H2   H  N N 383 
TRP HA   H  N N 384 
TRP HB2  H  N N 385 
TRP HB3  H  N N 386 
TRP HD1  H  N N 387 
TRP HE1  H  N N 388 
TRP HE3  H  N N 389 
TRP HZ2  H  N N 390 
TRP HZ3  H  N N 391 
TRP HH2  H  N N 392 
TRP HXT  H  N N 393 
TYR N    N  N N 394 
TYR CA   C  N S 395 
TYR C    C  N N 396 
TYR O    O  N N 397 
TYR CB   C  N N 398 
TYR CG   C  Y N 399 
TYR CD1  C  Y N 400 
TYR CD2  C  Y N 401 
TYR CE1  C  Y N 402 
TYR CE2  C  Y N 403 
TYR CZ   C  Y N 404 
TYR OH   O  N N 405 
TYR OXT  O  N N 406 
TYR H    H  N N 407 
TYR H2   H  N N 408 
TYR HA   H  N N 409 
TYR HB2  H  N N 410 
TYR HB3  H  N N 411 
TYR HD1  H  N N 412 
TYR HD2  H  N N 413 
TYR HE1  H  N N 414 
TYR HE2  H  N N 415 
TYR HH   H  N N 416 
TYR HXT  H  N N 417 
VAL N    N  N N 418 
VAL CA   C  N S 419 
VAL C    C  N N 420 
VAL O    O  N N 421 
VAL CB   C  N N 422 
VAL CG1  C  N N 423 
VAL CG2  C  N N 424 
VAL OXT  O  N N 425 
VAL H    H  N N 426 
VAL H2   H  N N 427 
VAL HA   H  N N 428 
VAL HB   H  N N 429 
VAL HG11 H  N N 430 
VAL HG12 H  N N 431 
VAL HG13 H  N N 432 
VAL HG21 H  N N 433 
VAL HG22 H  N N 434 
VAL HG23 H  N N 435 
VAL HXT  H  N N 436 
ZN  ZN   ZN N N 437 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
JDR N1  C2   doub Y N 182 
JDR N1  C6   sing Y N 183 
JDR C2  N3   sing Y N 184 
JDR C2  S21  sing N N 185 
JDR N3  C4   doub Y N 186 
JDR C4  C5   sing Y N 187 
JDR C4  N7   sing N N 188 
JDR C5  C6   doub Y N 189 
JDR C5  C18  sing N N 190 
JDR C6  CL20 sing N N 191 
JDR N7  C23  sing N N 192 
JDR C8  C9   doub Y N 193 
JDR C8  C13  sing Y N 194 
JDR C8  C23  sing N N 195 
JDR C9  C10  sing Y N 196 
JDR C10 C11  doub Y N 197 
JDR C11 C12  sing Y N 198 
JDR C11 S14  sing N N 199 
JDR C12 C13  doub Y N 200 
JDR S14 O15  doub N N 201 
JDR S14 O16  doub N N 202 
JDR S14 N17  sing N N 203 
JDR C18 O19  doub N N 204 
JDR S21 C22  sing N N 205 
JDR N7  HN7  sing N N 206 
JDR C9  H9   sing N N 207 
JDR C10 H10  sing N N 208 
JDR C12 H12  sing N N 209 
JDR C13 H13  sing N N 210 
JDR N17 HN17 sing N N 211 
JDR N17 HN1A sing N N 212 
JDR C18 H18  sing N N 213 
JDR C22 H22  sing N N 214 
JDR C22 H22A sing N N 215 
JDR C22 H22B sing N N 216 
JDR C23 H23  sing N N 217 
JDR C23 H23A sing N N 218 
LEU N   CA   sing N N 219 
LEU N   H    sing N N 220 
LEU N   H2   sing N N 221 
LEU CA  C    sing N N 222 
LEU CA  CB   sing N N 223 
LEU CA  HA   sing N N 224 
LEU C   O    doub N N 225 
LEU C   OXT  sing N N 226 
LEU CB  CG   sing N N 227 
LEU CB  HB2  sing N N 228 
LEU CB  HB3  sing N N 229 
LEU CG  CD1  sing N N 230 
LEU CG  CD2  sing N N 231 
LEU CG  HG   sing N N 232 
LEU CD1 HD11 sing N N 233 
LEU CD1 HD12 sing N N 234 
LEU CD1 HD13 sing N N 235 
LEU CD2 HD21 sing N N 236 
LEU CD2 HD22 sing N N 237 
LEU CD2 HD23 sing N N 238 
LEU OXT HXT  sing N N 239 
LYS N   CA   sing N N 240 
LYS N   H    sing N N 241 
LYS N   H2   sing N N 242 
LYS CA  C    sing N N 243 
LYS CA  CB   sing N N 244 
LYS CA  HA   sing N N 245 
LYS C   O    doub N N 246 
LYS C   OXT  sing N N 247 
LYS CB  CG   sing N N 248 
LYS CB  HB2  sing N N 249 
LYS CB  HB3  sing N N 250 
LYS CG  CD   sing N N 251 
LYS CG  HG2  sing N N 252 
LYS CG  HG3  sing N N 253 
LYS CD  CE   sing N N 254 
LYS CD  HD2  sing N N 255 
LYS CD  HD3  sing N N 256 
LYS CE  NZ   sing N N 257 
LYS CE  HE2  sing N N 258 
LYS CE  HE3  sing N N 259 
LYS NZ  HZ1  sing N N 260 
LYS NZ  HZ2  sing N N 261 
LYS NZ  HZ3  sing N N 262 
LYS OXT HXT  sing N N 263 
MET N   CA   sing N N 264 
MET N   H    sing N N 265 
MET N   H2   sing N N 266 
MET CA  C    sing N N 267 
MET CA  CB   sing N N 268 
MET CA  HA   sing N N 269 
MET C   O    doub N N 270 
MET C   OXT  sing N N 271 
MET CB  CG   sing N N 272 
MET CB  HB2  sing N N 273 
MET CB  HB3  sing N N 274 
MET CG  SD   sing N N 275 
MET CG  HG2  sing N N 276 
MET CG  HG3  sing N N 277 
MET SD  CE   sing N N 278 
MET CE  HE1  sing N N 279 
MET CE  HE2  sing N N 280 
MET CE  HE3  sing N N 281 
MET OXT HXT  sing N N 282 
PHE N   CA   sing N N 283 
PHE N   H    sing N N 284 
PHE N   H2   sing N N 285 
PHE CA  C    sing N N 286 
PHE CA  CB   sing N N 287 
PHE CA  HA   sing N N 288 
PHE C   O    doub N N 289 
PHE C   OXT  sing N N 290 
PHE CB  CG   sing N N 291 
PHE CB  HB2  sing N N 292 
PHE CB  HB3  sing N N 293 
PHE CG  CD1  doub Y N 294 
PHE CG  CD2  sing Y N 295 
PHE CD1 CE1  sing Y N 296 
PHE CD1 HD1  sing N N 297 
PHE CD2 CE2  doub Y N 298 
PHE CD2 HD2  sing N N 299 
PHE CE1 CZ   doub Y N 300 
PHE CE1 HE1  sing N N 301 
PHE CE2 CZ   sing Y N 302 
PHE CE2 HE2  sing N N 303 
PHE CZ  HZ   sing N N 304 
PHE OXT HXT  sing N N 305 
PRO N   CA   sing N N 306 
PRO N   CD   sing N N 307 
PRO N   H    sing N N 308 
PRO CA  C    sing N N 309 
PRO CA  CB   sing N N 310 
PRO CA  HA   sing N N 311 
PRO C   O    doub N N 312 
PRO C   OXT  sing N N 313 
PRO CB  CG   sing N N 314 
PRO CB  HB2  sing N N 315 
PRO CB  HB3  sing N N 316 
PRO CG  CD   sing N N 317 
PRO CG  HG2  sing N N 318 
PRO CG  HG3  sing N N 319 
PRO CD  HD2  sing N N 320 
PRO CD  HD3  sing N N 321 
PRO OXT HXT  sing N N 322 
SER N   CA   sing N N 323 
SER N   H    sing N N 324 
SER N   H2   sing N N 325 
SER CA  C    sing N N 326 
SER CA  CB   sing N N 327 
SER CA  HA   sing N N 328 
SER C   O    doub N N 329 
SER C   OXT  sing N N 330 
SER CB  OG   sing N N 331 
SER CB  HB2  sing N N 332 
SER CB  HB3  sing N N 333 
SER OG  HG   sing N N 334 
SER OXT HXT  sing N N 335 
THR N   CA   sing N N 336 
THR N   H    sing N N 337 
THR N   H2   sing N N 338 
THR CA  C    sing N N 339 
THR CA  CB   sing N N 340 
THR CA  HA   sing N N 341 
THR C   O    doub N N 342 
THR C   OXT  sing N N 343 
THR CB  OG1  sing N N 344 
THR CB  CG2  sing N N 345 
THR CB  HB   sing N N 346 
THR OG1 HG1  sing N N 347 
THR CG2 HG21 sing N N 348 
THR CG2 HG22 sing N N 349 
THR CG2 HG23 sing N N 350 
THR OXT HXT  sing N N 351 
TRP N   CA   sing N N 352 
TRP N   H    sing N N 353 
TRP N   H2   sing N N 354 
TRP CA  C    sing N N 355 
TRP CA  CB   sing N N 356 
TRP CA  HA   sing N N 357 
TRP C   O    doub N N 358 
TRP C   OXT  sing N N 359 
TRP CB  CG   sing N N 360 
TRP CB  HB2  sing N N 361 
TRP CB  HB3  sing N N 362 
TRP CG  CD1  doub Y N 363 
TRP CG  CD2  sing Y N 364 
TRP CD1 NE1  sing Y N 365 
TRP CD1 HD1  sing N N 366 
TRP CD2 CE2  doub Y N 367 
TRP CD2 CE3  sing Y N 368 
TRP NE1 CE2  sing Y N 369 
TRP NE1 HE1  sing N N 370 
TRP CE2 CZ2  sing Y N 371 
TRP CE3 CZ3  doub Y N 372 
TRP CE3 HE3  sing N N 373 
TRP CZ2 CH2  doub Y N 374 
TRP CZ2 HZ2  sing N N 375 
TRP CZ3 CH2  sing Y N 376 
TRP CZ3 HZ3  sing N N 377 
TRP CH2 HH2  sing N N 378 
TRP OXT HXT  sing N N 379 
TYR N   CA   sing N N 380 
TYR N   H    sing N N 381 
TYR N   H2   sing N N 382 
TYR CA  C    sing N N 383 
TYR CA  CB   sing N N 384 
TYR CA  HA   sing N N 385 
TYR C   O    doub N N 386 
TYR C   OXT  sing N N 387 
TYR CB  CG   sing N N 388 
TYR CB  HB2  sing N N 389 
TYR CB  HB3  sing N N 390 
TYR CG  CD1  doub Y N 391 
TYR CG  CD2  sing Y N 392 
TYR CD1 CE1  sing Y N 393 
TYR CD1 HD1  sing N N 394 
TYR CD2 CE2  doub Y N 395 
TYR CD2 HD2  sing N N 396 
TYR CE1 CZ   doub Y N 397 
TYR CE1 HE1  sing N N 398 
TYR CE2 CZ   sing Y N 399 
TYR CE2 HE2  sing N N 400 
TYR CZ  OH   sing N N 401 
TYR OH  HH   sing N N 402 
TYR OXT HXT  sing N N 403 
VAL N   CA   sing N N 404 
VAL N   H    sing N N 405 
VAL N   H2   sing N N 406 
VAL CA  C    sing N N 407 
VAL CA  CB   sing N N 408 
VAL CA  HA   sing N N 409 
VAL C   O    doub N N 410 
VAL C   OXT  sing N N 411 
VAL CB  CG1  sing N N 412 
VAL CB  CG2  sing N N 413 
VAL CB  HB   sing N N 414 
VAL CG1 HG11 sing N N 415 
VAL CG1 HG12 sing N N 416 
VAL CG1 HG13 sing N N 417 
VAL CG2 HG21 sing N N 418 
VAL CG2 HG22 sing N N 419 
VAL CG2 HG23 sing N N 420 
VAL OXT HXT  sing N N 421 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                ZN  
3 'DIMETHYL SULFOXIDE'                                                                      DMS 
4 '4-({[6-chloro-5-formyl-2-(methylsulfanyl)pyrimidin-4-yl]amino}methyl)benzenesulfonamide' JDR 
5 water                                                                                     HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HLJ 
_pdbx_initial_refinement_model.details          'PDB ENTRY 3HLJ' 
# 
