data_4AZ3 # _entry.id 4AZ3 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4AZ3 PDBE EBI-53025 WWPDB D_1290053025 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 1IVY unspecified 'PHYSIOLOGICAL DIMER HPP PRECURSOR' PDB 4AZ0 unspecified 'CRYSTAL STRUCTURE OF CATHEPSIN A, COMPLEXED WITH 8A.' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4AZ3 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2012-06-22 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Ruf, S.' 1 'Buning, C.' 2 'Schreuder, H.' 3 'Horstick, G.' 4 'Linz, W.' 5 'Olpp, T.' 6 'Pernerstorfer, J.' 7 'Hiss, K.' 8 'Kroll, K.' 9 'Kannt, A.' 10 'Kohlmann, M.' 11 'Linz, D.' 12 'Huebschle, T.' 13 'Ruetten, H.' 14 'Wirth, K.' 15 'Schmidt, T.' 16 'Sadowski, T.' 17 # _citation.id primary _citation.title 'Novel Beta-Amino Acid Derivatives as Inhibitors of Cathepsin A.' _citation.journal_abbrev J.Med.Chem. _citation.journal_volume 55 _citation.page_first 7636 _citation.page_last ? _citation.year 2012 _citation.journal_id_ASTM JMCMAR _citation.country US _citation.journal_id_ISSN 0022-2623 _citation.journal_id_CSD 0151 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 22861813 _citation.pdbx_database_id_DOI 10.1021/JM300663N # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Ruf, S.' 1 primary 'Buning, C.' 2 primary 'Schreuder, H.' 3 primary 'Horstick, G.' 4 primary 'Linz, W.' 5 primary 'Olpp, T.' 6 primary 'Pernerstorfer, J.' 7 primary 'Hiss, K.' 8 primary 'Kroll, K.' 9 primary 'Kannt, A.' 10 primary 'Kohlmann, M.' 11 primary 'Linz, D.' 12 primary 'Hubschle, T.' 13 primary 'Rutten, H.' 14 primary 'Wirth, K.' 15 primary 'Schmidt, T.' 16 primary 'Sadowski, T.' 17 # _cell.entry_id 4AZ3 _cell.length_a 90.590 _cell.length_b 102.800 _cell.length_c 48.390 _cell.angle_alpha 90.00 _cell.angle_beta 101.87 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4AZ3 _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 5 # 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 'LYSOSOMAL PROTECTIVE PROTEIN 32 KDA CHAIN' 33773.734 1 3.4.16.5 ? 'ACTIVATED PROTEASE RESIDUES 29-326' 'ACTIVATED WITH TRYPSIN-SEPHAROSE' 2 polymer man 'LYSOSOMAL PROTECTIVE PROTEIN 20 KDA CHAIN' 18073.738 1 3.4.16.5 ? 'ACTIVATED PROTEASE, RESIDUES 327-480' 'ACTIVATED WITH TRYPSIN-SEPHAROSE' 3 non-polymer syn ;(3S)-3-({[1-(2-fluorophenyl)-5-{[(2R)-2-hydroxy-3,3-dimethylbutyl]oxy}-1H-pyrazol-3-yl]carbonyl}amino)-3-(2-methylphenyl)propanoic acid ; 483.532 1 ? ? ? ? 4 non-polymer syn 'CADMIUM ION' 112.411 4 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 6 water nat water 18.015 422 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 ;LYSOSOMAL PROTECTIVE PROTEIN CARBOXYPEPTIDASE C, CARBOXYPEPTIDASE L, CATHEPSIN A, PROTECTIVE PROTEIN CATHEPSIN A, PPCA, PROTECTIVE PROTEIN FOR BETA-GALACTOSIDASE ; 2 ;LYSOSOMAL PROTECTIVE PROTEIN CARBOXYPEPTIDASE C, CARBOXYPEPTIDASE L, CATHEPSIN A, PROTECTIVE PROTEIN CATHEPSIN A, PPCA, PROTECTIVE PROTEIN FOR BETA-GALACTOSIDASE ; # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;SRAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPD GVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPT LAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARI VGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVR ; ;SRAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPD GVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPT LAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARI VGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVR ; A ? 2 'polypeptide(L)' no no ;MDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFM GDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPYE ; ;MDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFM GDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPYE ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 SER n 1 2 ARG n 1 3 ALA n 1 4 PRO n 1 5 ASP n 1 6 GLN n 1 7 ASP n 1 8 GLU n 1 9 ILE n 1 10 GLN n 1 11 ARG n 1 12 LEU n 1 13 PRO n 1 14 GLY n 1 15 LEU n 1 16 ALA n 1 17 LYS n 1 18 GLN n 1 19 PRO n 1 20 SER n 1 21 PHE n 1 22 ARG n 1 23 GLN n 1 24 TYR n 1 25 SER n 1 26 GLY n 1 27 TYR n 1 28 LEU n 1 29 LYS n 1 30 GLY n 1 31 SER n 1 32 GLY n 1 33 SER n 1 34 LYS n 1 35 HIS n 1 36 LEU n 1 37 HIS n 1 38 TYR n 1 39 TRP n 1 40 PHE n 1 41 VAL n 1 42 GLU n 1 43 SER n 1 44 GLN n 1 45 LYS n 1 46 ASP n 1 47 PRO n 1 48 GLU n 1 49 ASN n 1 50 SER n 1 51 PRO n 1 52 VAL n 1 53 VAL n 1 54 LEU n 1 55 TRP n 1 56 LEU n 1 57 ASN n 1 58 GLY n 1 59 GLY n 1 60 PRO n 1 61 GLY n 1 62 CYS n 1 63 SER n 1 64 SER n 1 65 LEU n 1 66 ASP n 1 67 GLY n 1 68 LEU n 1 69 LEU n 1 70 THR n 1 71 GLU n 1 72 HIS n 1 73 GLY n 1 74 PRO n 1 75 PHE n 1 76 LEU n 1 77 VAL n 1 78 GLN n 1 79 PRO n 1 80 ASP n 1 81 GLY n 1 82 VAL n 1 83 THR n 1 84 LEU n 1 85 GLU n 1 86 TYR n 1 87 ASN n 1 88 PRO n 1 89 TYR n 1 90 SER n 1 91 TRP n 1 92 ASN n 1 93 LEU n 1 94 ILE n 1 95 ALA n 1 96 ASN n 1 97 VAL n 1 98 LEU n 1 99 TYR n 1 100 LEU n 1 101 GLU n 1 102 SER n 1 103 PRO n 1 104 ALA n 1 105 GLY n 1 106 VAL n 1 107 GLY n 1 108 PHE n 1 109 SER n 1 110 TYR n 1 111 SER n 1 112 ASP n 1 113 ASP n 1 114 LYS n 1 115 PHE n 1 116 TYR n 1 117 ALA n 1 118 THR n 1 119 ASN n 1 120 ASP n 1 121 THR n 1 122 GLU n 1 123 VAL n 1 124 ALA n 1 125 GLN n 1 126 SER n 1 127 ASN n 1 128 PHE n 1 129 GLU n 1 130 ALA n 1 131 LEU n 1 132 GLN n 1 133 ASP n 1 134 PHE n 1 135 PHE n 1 136 ARG n 1 137 LEU n 1 138 PHE n 1 139 PRO n 1 140 GLU n 1 141 TYR n 1 142 LYS n 1 143 ASN n 1 144 ASN n 1 145 LYS n 1 146 LEU n 1 147 PHE n 1 148 LEU n 1 149 THR n 1 150 GLY n 1 151 GLU n 1 152 SER n 1 153 TYR n 1 154 ALA n 1 155 GLY n 1 156 ILE n 1 157 TYR n 1 158 ILE n 1 159 PRO n 1 160 THR n 1 161 LEU n 1 162 ALA n 1 163 VAL n 1 164 LEU n 1 165 VAL n 1 166 MET n 1 167 GLN n 1 168 ASP n 1 169 PRO n 1 170 SER n 1 171 MET n 1 172 ASN n 1 173 LEU n 1 174 GLN n 1 175 GLY n 1 176 LEU n 1 177 ALA n 1 178 VAL n 1 179 GLY n 1 180 ASN n 1 181 GLY n 1 182 LEU n 1 183 SER n 1 184 SER n 1 185 TYR n 1 186 GLU n 1 187 GLN n 1 188 ASN n 1 189 ASP n 1 190 ASN n 1 191 SER n 1 192 LEU n 1 193 VAL n 1 194 TYR n 1 195 PHE n 1 196 ALA n 1 197 TYR n 1 198 TYR n 1 199 HIS n 1 200 GLY n 1 201 LEU n 1 202 LEU n 1 203 GLY n 1 204 ASN n 1 205 ARG n 1 206 LEU n 1 207 TRP n 1 208 SER n 1 209 SER n 1 210 LEU n 1 211 GLN n 1 212 THR n 1 213 HIS n 1 214 CYS n 1 215 CYS n 1 216 SER n 1 217 GLN n 1 218 ASN n 1 219 LYS n 1 220 CYS n 1 221 ASN n 1 222 PHE n 1 223 TYR n 1 224 ASP n 1 225 ASN n 1 226 LYS n 1 227 ASP n 1 228 LEU n 1 229 GLU n 1 230 CYS n 1 231 VAL n 1 232 THR n 1 233 ASN n 1 234 LEU n 1 235 GLN n 1 236 GLU n 1 237 VAL n 1 238 ALA n 1 239 ARG n 1 240 ILE n 1 241 VAL n 1 242 GLY n 1 243 ASN n 1 244 SER n 1 245 GLY n 1 246 LEU n 1 247 ASN n 1 248 ILE n 1 249 TYR n 1 250 ASN n 1 251 LEU n 1 252 TYR n 1 253 ALA n 1 254 PRO n 1 255 CYS n 1 256 ALA n 1 257 GLY n 1 258 GLY n 1 259 VAL n 1 260 PRO n 1 261 SER n 1 262 HIS n 1 263 PHE n 1 264 ARG n 1 265 TYR n 1 266 GLU n 1 267 LYS n 1 268 ASP n 1 269 THR n 1 270 VAL n 1 271 VAL n 1 272 VAL n 1 273 GLN n 1 274 ASP n 1 275 LEU n 1 276 GLY n 1 277 ASN n 1 278 ILE n 1 279 PHE n 1 280 THR n 1 281 ARG n 1 282 LEU n 1 283 PRO n 1 284 LEU n 1 285 LYS n 1 286 ARG n 1 287 MET n 1 288 TRP n 1 289 HIS n 1 290 GLN n 1 291 ALA n 1 292 LEU n 1 293 LEU n 1 294 ARG n 1 295 SER n 1 296 GLY n 1 297 ASP n 1 298 LYS n 1 299 VAL n 1 300 ARG n 2 1 MET n 2 2 ASP n 2 3 PRO n 2 4 PRO n 2 5 CYS n 2 6 THR n 2 7 ASN n 2 8 THR n 2 9 THR n 2 10 ALA n 2 11 ALA n 2 12 SER n 2 13 THR n 2 14 TYR n 2 15 LEU n 2 16 ASN n 2 17 ASN n 2 18 PRO n 2 19 TYR n 2 20 VAL n 2 21 ARG n 2 22 LYS n 2 23 ALA n 2 24 LEU n 2 25 ASN n 2 26 ILE n 2 27 PRO n 2 28 GLU n 2 29 GLN n 2 30 LEU n 2 31 PRO n 2 32 GLN n 2 33 TRP n 2 34 ASP n 2 35 MET n 2 36 CYS n 2 37 ASN n 2 38 PHE n 2 39 LEU n 2 40 VAL n 2 41 ASN n 2 42 LEU n 2 43 GLN n 2 44 TYR n 2 45 ARG n 2 46 ARG n 2 47 LEU n 2 48 TYR n 2 49 ARG n 2 50 SER n 2 51 MET n 2 52 ASN n 2 53 SER n 2 54 GLN n 2 55 TYR n 2 56 LEU n 2 57 LYS n 2 58 LEU n 2 59 LEU n 2 60 SER n 2 61 SER n 2 62 GLN n 2 63 LYS n 2 64 TYR n 2 65 GLN n 2 66 ILE n 2 67 LEU n 2 68 LEU n 2 69 TYR n 2 70 ASN n 2 71 GLY n 2 72 ASP n 2 73 VAL n 2 74 ASP n 2 75 MET n 2 76 ALA n 2 77 CYS n 2 78 ASN n 2 79 PHE n 2 80 MET n 2 81 GLY n 2 82 ASP n 2 83 GLU n 2 84 TRP n 2 85 PHE n 2 86 VAL n 2 87 ASP n 2 88 SER n 2 89 LEU n 2 90 ASN n 2 91 GLN n 2 92 LYS n 2 93 MET n 2 94 GLU n 2 95 VAL n 2 96 GLN n 2 97 ARG n 2 98 ARG n 2 99 PRO n 2 100 TRP n 2 101 LEU n 2 102 VAL n 2 103 LYS n 2 104 TYR n 2 105 GLY n 2 106 ASP n 2 107 SER n 2 108 GLY n 2 109 GLU n 2 110 GLN n 2 111 ILE n 2 112 ALA n 2 113 GLY n 2 114 PHE n 2 115 VAL n 2 116 LYS n 2 117 GLU n 2 118 PHE n 2 119 SER n 2 120 HIS n 2 121 ILE n 2 122 ALA n 2 123 PHE n 2 124 LEU n 2 125 THR n 2 126 ILE n 2 127 LYS n 2 128 GLY n 2 129 ALA n 2 130 GLY n 2 131 HIS n 2 132 MET n 2 133 VAL n 2 134 PRO n 2 135 THR n 2 136 ASP n 2 137 LYS n 2 138 PRO n 2 139 LEU n 2 140 ALA n 2 141 ALA n 2 142 PHE n 2 143 THR n 2 144 MET n 2 145 PHE n 2 146 SER n 2 147 ARG n 2 148 PHE n 2 149 LEU n 2 150 ASN n 2 151 LYS n 2 152 GLN n 2 153 PRO n 2 154 TYR n 2 155 GLU n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _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 _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 _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _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 _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _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 _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 _entity_src_gen.pdbx_host_org_vector _entity_src_gen.host_org_details _entity_src_gen.expression_system_id _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 1 sample ? ? ? HUMAN ? ? ? ? ? ? ? ? 'HOMO SAPIENS' 9606 ? ? ? ? ? ? ? 'FALL ARMYWORM' 'SPODOPTERA FRUGIPERDA' 7108 ? ? ? ? ? ? ? ? SF9 ? ? ? ? ? BACULOVIRUS PVL1393 ? ? ? ? ? 2 1 sample ? ? ? HUMAN ? ? ? ? ? ? ? ? 'HOMO SAPIENS' 9606 ? ? ? ? ? ? ? 'FALL ARMYWORM' 'SPODOPTERA FRUGIPERDA' 7108 ? ? ? ? ? ? ? ? SF9 ? ? ? ? ? BACULOVIRUS PVL1393 ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform 1 UNP PPGB_HUMAN 1 ? ? P10619 ? 2 UNP PPGB_HUMAN 2 ? ? P10619 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4AZ3 A 3 ? 300 ? P10619 29 ? 326 ? 1 298 2 2 4AZ3 B 1 ? 154 ? P10619 327 ? 480 ? 299 452 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4AZ3 SER A 1 ? UNP P10619 ? ? 'expression tag' -1 1 1 4AZ3 ARG A 2 ? UNP P10619 ? ? 'expression tag' 0 2 2 4AZ3 GLU B 155 ? UNP P10619 ? ? 'expression tag' 453 3 # 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 CD non-polymer . 'CADMIUM ION' ? 'Cd 2' 112.411 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 S35 non-polymer . ;(3S)-3-({[1-(2-fluorophenyl)-5-{[(2R)-2-hydroxy-3,3-dimethylbutyl]oxy}-1H-pyrazol-3-yl]carbonyl}amino)-3-(2-methylphenyl)propanoic acid ; ? 'C26 H30 F N3 O5' 483.532 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 # _exptl.entry_id 4AZ3 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.4 _exptl_crystal.density_percent_sol 48.7 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.6 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details ;CATA WAS CRYSTALLIZED USING THE HANGING DROP METHOD: 1 UL OF PROTEIN SOLUTION, CONTAINING 6.5 MG/ML CATHEPSIN A, 25 MM TRIS-HCL (PH 8.0) AND 300 MM NACL, WAS MIXED WITH 1 UL RESERVOIR SOLUTION, CONTAINING 100 MM NAACETATE (PH 4.5), 18-20% PEG400 AND 100 MM CDCL2, AND SET TO EQUILIBRATE AT 4 DEG. C. ROD-SHAPED CRYSTALS APPEARED IN ABOUT ONE WEEK. ; # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 315r' _diffrn_detector.pdbx_collection_date 2009-09-17 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9395 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-4' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-4 _diffrn_source.pdbx_wavelength 0.9395 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4AZ3 _reflns.observed_criterion_sigma_I -3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 67.10 _reflns.d_resolution_high 2.04 _reflns.number_obs 27381 _reflns.number_all ? _reflns.percent_possible_obs 99.0 _reflns.pdbx_Rmerge_I_obs 0.06 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 14.90 _reflns.B_iso_Wilson_estimate 27.96 _reflns.pdbx_redundancy 3.7 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.04 _reflns_shell.d_res_low 2.10 _reflns_shell.percent_possible_all 99.1 _reflns_shell.Rmerge_I_obs 0.35 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 4.00 _reflns_shell.pdbx_redundancy 3.7 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4AZ3 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 27378 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 47.36 _refine.ls_d_res_high 2.04 _refine.ls_percent_reflns_obs 99.05 _refine.ls_R_factor_obs ? _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.188 _refine.ls_R_factor_R_free 0.215 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.91 _refine.ls_number_reflns_R_free 1344 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.9447 _refine.correlation_coeff_Fo_to_Fc_free 0.9265 _refine.B_iso_mean 28.88 _refine.aniso_B[1][1] -0.5078 _refine.aniso_B[2][2] -0.5904 _refine.aniso_B[3][3] 1.0981 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] 0.1075 _refine.aniso_B[2][3] 0.0000 _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ;IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=CD. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=3850. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=0. NUMBER TREATED BY BAD NON-BONDED CONTACTS=4. ; _refine.pdbx_starting_model 'MODEL DERIVED FROM PDB ENTRY 1IVY' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI 0.218 _refine.pdbx_overall_SU_R_free_Cruickshank_DPI 0.164 _refine.pdbx_overall_SU_R_Blow_DPI 0.234 _refine.pdbx_overall_SU_R_free_Blow_DPI 0.167 # _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_analyze.entry_id 4AZ3 _refine_analyze.Luzzati_coordinate_error_obs 0.244 _refine_analyze.Luzzati_sigma_a_obs ? _refine_analyze.Luzzati_d_res_low_obs ? _refine_analyze.Luzzati_coordinate_error_free ? _refine_analyze.Luzzati_sigma_a_free ? _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3288 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 95 _refine_hist.number_atoms_solvent 422 _refine_hist.number_atoms_total 3805 _refine_hist.d_res_high 2.04 _refine_hist.d_res_low 47.36 # 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 t_bond_d 0.007 ? 2.00 3533 'X-RAY DIFFRACTION' HARMONIC t_angle_deg 0.96 ? 2.00 4823 'X-RAY DIFFRACTION' HARMONIC t_dihedral_angle_d ? ? 2.00 1183 'X-RAY DIFFRACTION' SINUSOIDAL t_incorr_chiral_ct ? ? ? ? 'X-RAY DIFFRACTION' ? t_pseud_angle ? ? ? ? 'X-RAY DIFFRACTION' ? t_trig_c_planes ? ? 2.00 95 'X-RAY DIFFRACTION' HARMONIC t_gen_planes ? ? 5.00 507 'X-RAY DIFFRACTION' HARMONIC t_it ? ? 20.00 3533 'X-RAY DIFFRACTION' HARMONIC t_nbd ? ? 5.00 0 'X-RAY DIFFRACTION' SEMIHARMONIC t_omega_torsion 2.38 ? ? ? 'X-RAY DIFFRACTION' ? t_other_torsion 16.46 ? ? ? 'X-RAY DIFFRACTION' ? t_improper_torsion ? ? ? ? 'X-RAY DIFFRACTION' ? t_chiral_improper_torsion ? ? 5.00 436 'X-RAY DIFFRACTION' SEMIHARMONIC t_sum_occupancies ? ? 1.00 3 'X-RAY DIFFRACTION' HARMONIC t_utility_distance ? ? ? ? 'X-RAY DIFFRACTION' ? t_utility_angle ? ? ? ? 'X-RAY DIFFRACTION' ? t_utility_torsion ? ? ? ? 'X-RAY DIFFRACTION' ? t_ideal_dist_contact ? ? 4.00 4443 'X-RAY DIFFRACTION' SEMIHARMONIC # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 14 _refine_ls_shell.d_res_high 2.04 _refine_ls_shell.d_res_low 2.12 _refine_ls_shell.number_reflns_R_work 2762 _refine_ls_shell.R_factor_R_work 0.2405 _refine_ls_shell.percent_reflns_obs 99.05 _refine_ls_shell.R_factor_R_free 0.2506 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free 4.50 _refine_ls_shell.number_reflns_R_free 130 _refine_ls_shell.number_reflns_all 2892 _refine_ls_shell.R_factor_all 0.2409 # _struct.entry_id 4AZ3 _struct.title 'crystal structure of cathepsin a, complexed with 15a' _struct.pdbx_descriptor 'LYSOSOMAL PROTECTIVE PROTEIN 32 KDA CHAIN (E.C.3.4.16.5), LYSOSOMAL PROTECTIVE PROTEIN 20 KDA CHAIN (E.C.3.4.16.5)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4AZ3 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, DRUG DISCOVERY, CARBOXYPEPTIDASE, CARDIOVASCULAR' # 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 4 ? F N N 4 ? G N N 5 ? H N N 5 ? I N N 5 ? J N N 5 ? K N N 4 ? L N N 6 ? M N N 6 ? # _struct_biol.id 1 # 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 PRO A 4 ? ASP A 7 ? PRO A 2 ASP A 5 5 ? 4 HELX_P HELX_P2 2 SER A 64 ? THR A 70 ? SER A 62 THR A 68 1 ? 7 HELX_P HELX_P3 3 SER A 90 ? ILE A 94 ? SER A 88 ILE A 92 5 ? 5 HELX_P HELX_P4 4 ASN A 119 ? PHE A 138 ? ASN A 117 PHE A 136 1 ? 20 HELX_P HELX_P5 5 PRO A 139 ? LYS A 142 ? PRO A 137 LYS A 140 5 ? 4 HELX_P HELX_P6 6 TYR A 153 ? MET A 166 ? TYR A 151 MET A 164 1 ? 14 HELX_P HELX_P7 7 SER A 184 ? HIS A 199 ? SER A 182 HIS A 197 1 ? 16 HELX_P HELX_P8 8 GLY A 203 ? CYS A 214 ? GLY A 201 CYS A 212 1 ? 12 HELX_P HELX_P9 9 ASP A 227 ? ASN A 243 ? ASP A 225 ASN A 241 1 ? 17 HELX_P HELX_P10 10 THR B 8 ? ASN B 16 ? THR B 306 ASN B 314 1 ? 9 HELX_P HELX_P11 11 ASN B 17 ? LEU B 24 ? ASN B 315 LEU B 322 1 ? 8 HELX_P HELX_P12 12 ASN B 37 ? TYR B 44 ? ASN B 335 TYR B 342 1 ? 8 HELX_P HELX_P13 13 MET B 51 ? SER B 61 ? MET B 349 SER B 359 1 ? 11 HELX_P HELX_P14 14 ASN B 78 ? LEU B 89 ? ASN B 376 LEU B 387 1 ? 12 HELX_P HELX_P15 15 MET B 132 ? LYS B 137 ? MET B 430 LYS B 435 1 ? 6 HELX_P HELX_P16 16 LYS B 137 ? ASN B 150 ? LYS B 435 ASN B 448 1 ? 14 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 62 SG ? ? ? 1_555 B CYS 36 SG ? ? A CYS 60 B CYS 334 1_555 ? ? ? ? ? ? ? 2.038 ? disulf2 disulf ? ? A CYS 214 SG ? ? ? 1_555 A CYS 230 SG ? ? A CYS 212 A CYS 228 1_555 ? ? ? ? ? ? ? 2.028 ? disulf3 disulf ? ? A CYS 215 SG ? ? ? 1_555 A CYS 220 SG ? ? A CYS 213 A CYS 218 1_555 ? ? ? ? ? ? ? 2.030 ? disulf4 disulf ? ? A CYS 255 SG ? ? ? 1_555 B CYS 5 SG ? ? A CYS 253 B CYS 303 1_555 ? ? ? ? ? ? ? 2.033 ? covale1 covale ? ? A ASN 119 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 117 A NAG 3010 1_555 ? ? ? ? ? ? ? 1.433 ? metalc1 metalc ? ? D CD . CD ? ? ? 1_555 A GLU 186 OE2 ? ? A CD 1260 A GLU 184 1_555 ? ? ? ? ? ? ? 2.773 ? metalc2 metalc ? ? D CD . CD ? ? ? 1_555 A GLU 186 OE1 ? ? A CD 1260 A GLU 184 1_555 ? ? ? ? ? ? ? 3.013 ? metalc3 metalc ? ? E CD . CD ? ? ? 1_555 A ASP 5 OD2 ? ? A CD 1261 A ASP 3 3_455 ? ? ? ? ? ? ? 2.276 ? metalc4 metalc ? ? E CD . CD ? ? ? 1_555 L HOH . O ? ? A CD 1261 A HOH 2220 1_555 ? ? ? ? ? ? ? 2.436 ? metalc5 metalc ? ? E CD . CD ? ? ? 1_555 A ASP 5 OD1 ? ? A CD 1261 A ASP 3 3_455 ? ? ? ? ? ? ? 2.430 ? metalc6 metalc ? ? E CD . CD ? ? ? 1_555 A ASP 227 OD1 ? ? A CD 1261 A ASP 225 1_555 ? ? ? ? ? ? ? 2.702 ? metalc7 metalc ? ? E CD . CD ? ? ? 1_555 A ASP 227 OD2 ? ? A CD 1261 A ASP 225 1_555 ? ? ? ? ? ? ? 2.275 ? metalc8 metalc ? ? E CD . CD ? ? ? 1_555 A HIS 213 ND1 ? ? A CD 1261 A HIS 211 1_555 ? ? ? ? ? ? ? 2.200 ? metalc9 metalc ? ? F CD . CD ? ? ? 1_555 A ASP 224 OD2 ? ? A CD 1262 A ASP 222 1_555 ? ? ? ? ? ? ? 2.760 ? metalc10 metalc ? ? F CD . CD ? ? ? 1_555 B GLU 28 OE2 ? ? A CD 1262 B GLU 326 4_456 ? ? ? ? ? ? ? 2.454 ? metalc11 metalc ? ? F CD . CD ? ? ? 1_555 A ASP 224 OD1 ? ? A CD 1262 A ASP 222 1_555 ? ? ? ? ? ? ? 2.382 ? metalc12 metalc ? ? F CD . CD ? ? ? 1_555 B GLU 28 OE1 ? ? A CD 1262 B GLU 326 4_456 ? ? ? ? ? ? ? 3.044 ? covale2 covale ? ? G NAG . O4 ? ? ? 1_555 H NAG . C1 ? ? A NAG 3010 A NAG 3011 1_555 ? ? ? ? ? ? ? 1.426 ? covale3 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 3020 A NAG 3021 1_555 ? ? ? ? ? ? ? 1.423 ? covale4 covale ? ? B ASN 7 ND2 ? ? ? 1_555 I NAG . C1 ? ? B ASN 305 A NAG 3020 1_555 ? ? ? ? ? ? ? 1.431 ? metalc13 metalc ? ? K CD . CD ? ? ? 1_555 M HOH . O ? ? B CD 1454 B HOH 2091 1_555 ? ? ? ? ? ? ? 2.368 ? metalc14 metalc ? ? K CD . CD ? ? ? 1_555 B CYS 77 SG ? ? B CD 1454 B CYS 375 1_555 ? ? ? ? ? ? ? 1.985 ? metalc15 metalc ? ? K CD . CD ? ? ? 1_555 B ALA 76 O ? ? B CD 1454 B ALA 374 1_555 ? ? ? ? ? ? ? 2.783 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # 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 GLY 59 A . ? GLY 57 A PRO 60 A ? PRO 58 A 1 -3.03 2 SER 102 A . ? SER 100 A PRO 103 A ? PRO 101 A 1 -1.28 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 2 ? AB ? 2 ? BA ? 10 ? BB ? 10 ? AC ? 2 ? AD ? 2 ? # 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 AA 1 2 ? anti-parallel AB 1 2 ? parallel BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? parallel BA 4 5 ? parallel BA 5 6 ? parallel BA 6 7 ? parallel BA 7 8 ? parallel BA 8 9 ? anti-parallel BA 9 10 ? parallel BB 1 2 ? anti-parallel BB 2 3 ? anti-parallel BB 3 4 ? parallel BB 4 5 ? parallel BB 5 6 ? parallel BB 6 7 ? parallel BB 7 8 ? parallel BB 8 9 ? anti-parallel BB 9 10 ? anti-parallel AC 1 2 ? anti-parallel AD 1 2 ? anti-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 AA 1 GLN A 23 ? LYS A 29 ? GLN A 21 LYS A 27 AA 2 LYS A 34 ? VAL A 41 ? LYS A 32 VAL A 39 AB 1 TYR A 110 ? SER A 111 ? TYR A 108 SER A 109 AB 2 LYS A 34 ? VAL A 41 ? LYS A 32 VAL A 39 BA 1 ARG B 98 ? TYR B 104 ? ARG B 396 TYR B 402 BA 2 GLY B 108 ? PHE B 118 ? GLY B 406 PHE B 416 BA 3 ILE B 121 ? ILE B 126 ? ILE B 419 ILE B 424 BA 4 GLN B 65 ? GLY B 71 ? GLN B 363 GLY B 369 BA 5 LEU A 173 ? GLY A 179 ? LEU A 171 GLY A 177 BA 6 LEU A 146 ? GLU A 151 ? LEU A 144 GLU A 149 BA 7 VAL A 52 ? LEU A 56 ? VAL A 50 LEU A 54 BA 8 ASN A 96 ? LEU A 100 ? ASN A 94 LEU A 98 BA 9 LYS A 34 ? VAL A 41 ? LYS A 32 VAL A 39 BA 10 TYR A 110 ? SER A 111 ? TYR A 108 SER A 109 BB 1 ARG B 98 ? TYR B 104 ? ARG B 396 TYR B 402 BB 2 GLY B 108 ? PHE B 118 ? GLY B 406 PHE B 416 BB 3 ILE B 121 ? ILE B 126 ? ILE B 419 ILE B 424 BB 4 GLN B 65 ? GLY B 71 ? GLN B 363 GLY B 369 BB 5 LEU A 173 ? GLY A 179 ? LEU A 171 GLY A 177 BB 6 LEU A 146 ? GLU A 151 ? LEU A 144 GLU A 149 BB 7 VAL A 52 ? LEU A 56 ? VAL A 50 LEU A 54 BB 8 ASN A 96 ? LEU A 100 ? ASN A 94 LEU A 98 BB 9 LYS A 34 ? VAL A 41 ? LYS A 32 VAL A 39 BB 10 GLN A 23 ? LYS A 29 ? GLN A 21 LYS A 27 AC 1 PHE A 75 ? VAL A 77 ? PHE A 73 VAL A 75 AC 2 LEU A 84 ? TYR A 86 ? LEU A 82 TYR A 84 AD 1 CYS A 215 ? SER A 216 ? CYS A 213 SER A 214 AD 2 LYS A 219 ? CYS A 220 ? LYS A 217 CYS 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 AA 1 2 N LEU A 28 ? N LEU A 26 O LEU A 36 ? O LEU A 34 AB 1 2 N TYR A 110 ? N TYR A 108 O HIS A 35 ? O HIS A 33 BA 1 2 N TYR B 104 ? N TYR B 402 O GLY B 108 ? O GLY B 406 BA 2 3 N PHE B 118 ? N PHE B 416 O ILE B 121 ? O ILE B 419 BA 3 4 N ALA B 122 ? N ALA B 420 O ILE B 66 ? O ILE B 364 BA 4 5 N GLN B 65 ? N GLN B 363 O GLN A 174 ? O GLN A 172 BA 5 6 N GLN A 174 ? N GLN A 172 O LEU A 146 ? O LEU A 144 BA 6 7 N PHE A 147 ? N PHE A 145 O VAL A 52 ? O VAL A 50 BA 7 8 N VAL A 53 ? N VAL A 51 O ASN A 96 ? O ASN A 94 BA 8 9 N TYR A 99 ? N TYR A 97 O TRP A 39 ? O TRP A 37 BA 9 10 N HIS A 35 ? N HIS A 33 O TYR A 110 ? O TYR A 108 BB 1 2 N TYR B 104 ? N TYR B 402 O GLY B 108 ? O GLY B 406 BB 2 3 N PHE B 118 ? N PHE B 416 O ILE B 121 ? O ILE B 419 BB 3 4 N ALA B 122 ? N ALA B 420 O ILE B 66 ? O ILE B 364 BB 4 5 N GLN B 65 ? N GLN B 363 O GLN A 174 ? O GLN A 172 BB 5 6 N GLN A 174 ? N GLN A 172 O LEU A 146 ? O LEU A 144 BB 6 7 N PHE A 147 ? N PHE A 145 O VAL A 52 ? O VAL A 50 BB 7 8 N VAL A 53 ? N VAL A 51 O ASN A 96 ? O ASN A 94 BB 8 9 N TYR A 99 ? N TYR A 97 O TRP A 39 ? O TRP A 37 BB 9 10 N PHE A 40 ? N PHE A 38 O TYR A 24 ? O TYR A 22 AC 1 2 N LEU A 76 ? N LEU A 74 O GLU A 85 ? O GLU A 83 AD 1 2 N SER A 216 ? N SER A 214 O LYS A 219 ? O LYS A 217 # 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 ? ? ? ? 5 'BINDING SITE FOR RESIDUE CD B 1454' AC2 Software ? ? ? ? 8 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 117 RESIDUES 3010 TO 3011' # 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 5 LEU A 182 ? LEU A 180 . ? 1_555 ? 2 AC1 5 ASN A 188 ? ASN A 186 . ? 1_555 ? 3 AC1 5 ALA B 76 ? ALA B 374 . ? 1_555 ? 4 AC1 5 CYS B 77 ? CYS B 375 . ? 1_555 ? 5 AC1 5 HOH M . ? HOH B 2091 . ? 1_555 ? 6 AC2 8 ASN A 119 ? ASN A 117 . ? 1_555 ? 7 AC2 8 GLU A 122 ? GLU A 120 . ? 1_555 ? 8 AC2 8 HOH L . ? HOH A 2137 . ? 1_555 ? 9 AC2 8 HOH L . ? HOH A 2259 . ? 1_555 ? 10 AC2 8 HOH L . ? HOH A 2260 . ? 1_555 ? 11 AC2 8 HOH L . ? HOH A 2261 . ? 1_555 ? 12 AC2 8 HOH L . ? HOH A 2262 . ? 1_555 ? 13 AC2 8 ARG B 45 ? ARG B 343 . ? 1_555 ? # _database_PDB_matrix.entry_id 4AZ3 _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4AZ3 _atom_sites.fract_transf_matrix[1][1] 0.011039 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.002320 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.009728 _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] 0.021117 _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 CD F N O S # 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 . ARG A 1 2 ? -1.726 -4.250 15.439 1.00 40.96 ? 0 ARG A N 1 ATOM 2 C CA . ARG A 1 2 ? -2.293 -3.894 14.139 1.00 40.59 ? 0 ARG A CA 1 ATOM 3 C C . ARG A 1 2 ? -3.794 -3.612 14.215 1.00 43.52 ? 0 ARG A C 1 ATOM 4 O O . ARG A 1 2 ? -4.288 -2.754 13.483 1.00 43.38 ? 0 ARG A O 1 ATOM 5 C CB . ARG A 1 2 ? -2.017 -4.996 13.127 1.00 41.37 ? 0 ARG A CB 1 ATOM 6 N N . ALA A 1 3 ? -4.518 -4.354 15.078 1.00 38.95 ? 1 ALA A N 1 ATOM 7 C CA . ALA A 1 3 ? -5.966 -4.248 15.296 1.00 38.09 ? 1 ALA A CA 1 ATOM 8 C C . ALA A 1 3 ? -6.329 -4.830 16.676 1.00 39.14 ? 1 ALA A C 1 ATOM 9 O O . ALA A 1 3 ? -5.631 -5.740 17.130 1.00 38.86 ? 1 ALA A O 1 ATOM 10 C CB . ALA A 1 3 ? -6.714 -5.005 14.203 1.00 38.96 ? 1 ALA A CB 1 ATOM 11 N N . PRO A 1 4 ? -7.390 -4.348 17.375 1.00 33.46 ? 2 PRO A N 1 ATOM 12 C CA . PRO A 1 4 ? -7.718 -4.945 18.676 1.00 32.35 ? 2 PRO A CA 1 ATOM 13 C C . PRO A 1 4 ? -8.477 -6.259 18.503 1.00 33.53 ? 2 PRO A C 1 ATOM 14 O O . PRO A 1 4 ? -9.691 -6.263 18.272 1.00 32.58 ? 2 PRO A O 1 ATOM 15 C CB . PRO A 1 4 ? -8.529 -3.853 19.387 1.00 34.23 ? 2 PRO A CB 1 ATOM 16 C CG . PRO A 1 4 ? -9.070 -2.990 18.302 1.00 38.96 ? 2 PRO A CG 1 ATOM 17 C CD . PRO A 1 4 ? -8.357 -3.292 17.011 1.00 34.70 ? 2 PRO A CD 1 ATOM 18 N N . ASP A 1 5 ? -7.735 -7.383 18.582 1.00 28.17 ? 3 ASP A N 1 ATOM 19 C CA . ASP A 1 5 ? -8.281 -8.737 18.447 1.00 26.81 ? 3 ASP A CA 1 ATOM 20 C C . ASP A 1 5 ? -9.314 -9.060 19.547 1.00 30.01 ? 3 ASP A C 1 ATOM 21 O O . ASP A 1 5 ? -10.214 -9.866 19.317 1.00 29.54 ? 3 ASP A O 1 ATOM 22 C CB . ASP A 1 5 ? -7.149 -9.792 18.362 1.00 27.44 ? 3 ASP A CB 1 ATOM 23 C CG . ASP A 1 5 ? -6.351 -9.782 17.056 1.00 27.49 ? 3 ASP A CG 1 ATOM 24 O OD1 . ASP A 1 5 ? -6.882 -9.281 16.036 1.00 29.15 ? 3 ASP A OD1 1 ATOM 25 O OD2 . ASP A 1 5 ? -5.207 -10.317 17.043 1.00 17.40 ? 3 ASP A OD2 1 ATOM 26 N N . GLN A 1 6 ? -9.211 -8.380 20.709 1.00 26.16 ? 4 GLN A N 1 ATOM 27 C CA . GLN A 1 6 ? -10.111 -8.526 21.863 1.00 25.84 ? 4 GLN A CA 1 ATOM 28 C C . GLN A 1 6 ? -11.510 -7.955 21.578 1.00 28.43 ? 4 GLN A C 1 ATOM 29 O O . GLN A 1 6 ? -12.491 -8.438 22.146 1.00 27.97 ? 4 GLN A O 1 ATOM 30 C CB . GLN A 1 6 ? -9.533 -7.822 23.108 1.00 27.42 ? 4 GLN A CB 1 ATOM 31 C CG . GLN A 1 6 ? -8.076 -8.150 23.429 1.00 46.11 ? 4 GLN A CG 1 ATOM 32 C CD . GLN A 1 6 ? -7.147 -7.034 23.018 1.00 68.15 ? 4 GLN A CD 1 ATOM 33 O OE1 . GLN A 1 6 ? -6.931 -6.772 21.829 1.00 64.64 ? 4 GLN A OE1 1 ATOM 34 N NE2 . GLN A 1 6 ? -6.553 -6.368 23.996 1.00 61.32 ? 4 GLN A NE2 1 ATOM 35 N N . ASP A 1 7 ? -11.590 -6.909 20.734 1.00 24.21 ? 5 ASP A N 1 ATOM 36 C CA . ASP A 1 7 ? -12.838 -6.232 20.366 1.00 23.72 ? 5 ASP A CA 1 ATOM 37 C C . ASP A 1 7 ? -13.596 -6.900 19.213 1.00 27.80 ? 5 ASP A C 1 ATOM 38 O O . ASP A 1 7 ? -14.752 -6.546 18.967 1.00 26.92 ? 5 ASP A O 1 ATOM 39 C CB . ASP A 1 7 ? -12.565 -4.754 20.022 1.00 25.23 ? 5 ASP A CB 1 ATOM 40 C CG . ASP A 1 7 ? -12.216 -3.849 21.193 1.00 30.77 ? 5 ASP A CG 1 ATOM 41 O OD1 . ASP A 1 7 ? -12.326 -4.303 22.355 1.00 30.52 ? 5 ASP A OD1 1 ATOM 42 O OD2 . ASP A 1 7 ? -11.854 -2.679 20.947 1.00 34.52 ? 5 ASP A OD2 1 ATOM 43 N N . GLU A 1 8 ? -12.956 -7.855 18.507 1.00 24.91 ? 6 GLU A N 1 ATOM 44 C CA . GLU A 1 8 ? -13.546 -8.541 17.357 1.00 24.88 ? 6 GLU A CA 1 ATOM 45 C C . GLU A 1 8 ? -14.759 -9.390 17.710 1.00 28.81 ? 6 GLU A C 1 ATOM 46 O O . GLU A 1 8 ? -14.710 -10.177 18.657 1.00 29.24 ? 6 GLU A O 1 ATOM 47 C CB . GLU A 1 8 ? -12.493 -9.364 16.594 1.00 26.22 ? 6 GLU A CB 1 ATOM 48 C CG . GLU A 1 8 ? -12.830 -9.550 15.121 1.00 36.32 ? 6 GLU A CG 1 ATOM 49 C CD . GLU A 1 8 ? -11.864 -10.350 14.263 1.00 52.87 ? 6 GLU A CD 1 ATOM 50 O OE1 . GLU A 1 8 ? -10.736 -10.641 14.722 1.00 42.36 ? 6 GLU A OE1 1 ATOM 51 O OE2 . GLU A 1 8 ? -12.234 -10.664 13.109 1.00 46.60 ? 6 GLU A OE2 1 ATOM 52 N N . ILE A 1 9 ? -15.850 -9.214 16.944 1.00 24.62 ? 7 ILE A N 1 ATOM 53 C CA . ILE A 1 9 ? -17.094 -9.972 17.102 1.00 24.16 ? 7 ILE A CA 1 ATOM 54 C C . ILE A 1 9 ? -16.879 -11.323 16.415 1.00 28.47 ? 7 ILE A C 1 ATOM 55 O O . ILE A 1 9 ? -16.584 -11.365 15.217 1.00 27.51 ? 7 ILE A O 1 ATOM 56 C CB . ILE A 1 9 ? -18.324 -9.202 16.532 1.00 27.03 ? 7 ILE A CB 1 ATOM 57 C CG1 . ILE A 1 9 ? -18.462 -7.802 17.175 1.00 27.38 ? 7 ILE A CG1 1 ATOM 58 C CG2 . ILE A 1 9 ? -19.617 -10.016 16.700 1.00 27.40 ? 7 ILE A CG2 1 ATOM 59 C CD1 . ILE A 1 9 ? -19.053 -6.732 16.254 1.00 31.15 ? 7 ILE A CD1 1 ATOM 60 N N . GLN A 1 10 ? -16.993 -12.416 17.184 1.00 26.28 ? 8 GLN A N 1 ATOM 61 C CA . GLN A 1 10 ? -16.786 -13.773 16.678 1.00 26.77 ? 8 GLN A CA 1 ATOM 62 C C . GLN A 1 10 ? -18.030 -14.314 15.972 1.00 31.86 ? 8 GLN A C 1 ATOM 63 O O . GLN A 1 10 ? -18.008 -14.476 14.750 1.00 32.26 ? 8 GLN A O 1 ATOM 64 C CB . GLN A 1 10 ? -16.305 -14.711 17.798 1.00 28.10 ? 8 GLN A CB 1 ATOM 65 N N . ARG A 1 11 ? -19.109 -14.580 16.734 1.00 28.30 ? 9 ARG A N 1 ATOM 66 C CA . ARG A 1 11 ? -20.375 -15.099 16.220 1.00 28.19 ? 9 ARG A CA 1 ATOM 67 C C . ARG A 1 11 ? -21.535 -14.254 16.740 1.00 32.06 ? 9 ARG A C 1 ATOM 68 O O . ARG A 1 11 ? -21.903 -14.339 17.916 1.00 31.80 ? 9 ARG A O 1 ATOM 69 C CB . ARG A 1 11 ? -20.548 -16.584 16.581 1.00 28.99 ? 9 ARG A CB 1 ATOM 70 N N . LEU A 1 12 ? -22.084 -13.410 15.863 1.00 28.31 ? 10 LEU A N 1 ATOM 71 C CA . LEU A 1 12 ? -23.181 -12.515 16.199 1.00 27.85 ? 10 LEU A CA 1 ATOM 72 C C . LEU A 1 12 ? -24.528 -13.247 16.118 1.00 30.81 ? 10 LEU A C 1 ATOM 73 O O . LEU A 1 12 ? -24.835 -13.833 15.074 1.00 30.18 ? 10 LEU A O 1 ATOM 74 C CB . LEU A 1 12 ? -23.146 -11.276 15.286 1.00 27.91 ? 10 LEU A CB 1 ATOM 75 C CG . LEU A 1 12 ? -23.966 -10.068 15.717 1.00 32.59 ? 10 LEU A CG 1 ATOM 76 C CD1 . LEU A 1 12 ? -23.404 -9.415 16.977 1.00 32.80 ? 10 LEU A CD1 1 ATOM 77 C CD2 . LEU A 1 12 ? -24.018 -9.055 14.621 1.00 35.03 ? 10 LEU A CD2 1 ATOM 78 N N . PRO A 1 13 ? -25.325 -13.259 17.218 1.00 26.72 ? 11 PRO A N 1 ATOM 79 C CA . PRO A 1 13 ? -26.622 -13.961 17.181 1.00 26.39 ? 11 PRO A CA 1 ATOM 80 C C . PRO A 1 13 ? -27.610 -13.316 16.213 1.00 29.93 ? 11 PRO A C 1 ATOM 81 O O . PRO A 1 13 ? -27.589 -12.098 16.031 1.00 29.22 ? 11 PRO A O 1 ATOM 82 C CB . PRO A 1 13 ? -27.120 -13.873 18.631 1.00 28.04 ? 11 PRO A CB 1 ATOM 83 C CG . PRO A 1 13 ? -25.921 -13.488 19.443 1.00 32.41 ? 11 PRO A CG 1 ATOM 84 C CD . PRO A 1 13 ? -25.098 -12.638 18.536 1.00 28.01 ? 11 PRO A CD 1 ATOM 85 N N . GLY A 1 14 ? -28.437 -14.145 15.582 1.00 26.43 ? 12 GLY A N 1 ATOM 86 C CA . GLY A 1 14 ? -29.438 -13.699 14.620 1.00 25.89 ? 12 GLY A CA 1 ATOM 87 C C . GLY A 1 14 ? -29.003 -13.756 13.170 1.00 29.02 ? 12 GLY A C 1 ATOM 88 O O . GLY A 1 14 ? -29.842 -13.621 12.276 1.00 28.28 ? 12 GLY A O 1 ATOM 89 N N . LEU A 1 15 ? -27.690 -13.944 12.922 1.00 25.55 ? 13 LEU A N 1 ATOM 90 C CA . LEU A 1 15 ? -27.140 -14.041 11.569 1.00 25.56 ? 13 LEU A CA 1 ATOM 91 C C . LEU A 1 15 ? -27.077 -15.497 11.112 1.00 29.27 ? 13 LEU A C 1 ATOM 92 O O . LEU A 1 15 ? -26.373 -16.304 11.723 1.00 28.73 ? 13 LEU A O 1 ATOM 93 C CB . LEU A 1 15 ? -25.750 -13.379 11.472 1.00 25.71 ? 13 LEU A CB 1 ATOM 94 C CG . LEU A 1 15 ? -25.706 -11.853 11.415 1.00 30.54 ? 13 LEU A CG 1 ATOM 95 C CD1 . LEU A 1 15 ? -24.289 -11.356 11.581 1.00 30.95 ? 13 LEU A CD1 1 ATOM 96 C CD2 . LEU A 1 15 ? -26.280 -11.324 10.104 1.00 32.76 ? 13 LEU A CD2 1 ATOM 97 N N . ALA A 1 16 ? -27.829 -15.830 10.047 1.00 25.71 ? 14 ALA A N 1 ATOM 98 C CA . ALA A 1 16 ? -27.893 -17.179 9.477 1.00 25.47 ? 14 ALA A CA 1 ATOM 99 C C . ALA A 1 16 ? -26.603 -17.558 8.740 1.00 29.19 ? 14 ALA A C 1 ATOM 100 O O . ALA A 1 16 ? -26.278 -18.741 8.645 1.00 28.97 ? 14 ALA A O 1 ATOM 101 C CB . ALA A 1 16 ? -29.089 -17.299 8.545 1.00 26.13 ? 14 ALA A CB 1 ATOM 102 N N . LYS A 1 17 ? -25.882 -16.553 8.214 1.00 25.10 ? 15 LYS A N 1 ATOM 103 C CA . LYS A 1 17 ? -24.619 -16.727 7.493 1.00 24.59 ? 15 LYS A CA 1 ATOM 104 C C . LYS A 1 17 ? -23.567 -15.831 8.129 1.00 28.59 ? 15 LYS A C 1 ATOM 105 O O . LYS A 1 17 ? -23.876 -14.701 8.517 1.00 27.89 ? 15 LYS A O 1 ATOM 106 C CB . LYS A 1 17 ? -24.773 -16.362 6.006 1.00 26.73 ? 15 LYS A CB 1 ATOM 107 C CG . LYS A 1 17 ? -25.783 -17.209 5.238 1.00 36.82 ? 15 LYS A CG 1 ATOM 108 C CD . LYS A 1 17 ? -25.944 -16.710 3.812 1.00 42.63 ? 15 LYS A CD 1 ATOM 109 C CE . LYS A 1 17 ? -27.171 -17.285 3.150 1.00 50.12 ? 15 LYS A CE 1 ATOM 110 N NZ . LYS A 1 17 ? -27.124 -17.120 1.674 1.00 57.03 ? 15 LYS A NZ 1 ATOM 111 N N . GLN A 1 18 ? -22.327 -16.330 8.240 1.00 24.94 ? 16 GLN A N 1 ATOM 112 C CA . GLN A 1 18 ? -21.232 -15.554 8.819 1.00 24.53 ? 16 GLN A CA 1 ATOM 113 C C . GLN A 1 18 ? -20.775 -14.446 7.861 1.00 27.40 ? 16 GLN A C 1 ATOM 114 O O . GLN A 1 18 ? -20.814 -14.654 6.645 1.00 26.77 ? 16 GLN A O 1 ATOM 115 C CB . GLN A 1 18 ? -20.068 -16.461 9.250 1.00 26.07 ? 16 GLN A CB 1 ATOM 116 C CG . GLN A 1 18 ? -20.354 -17.246 10.531 1.00 46.30 ? 16 GLN A CG 1 ATOM 117 C CD . GLN A 1 18 ? -20.378 -16.376 11.765 1.00 71.40 ? 16 GLN A CD 1 ATOM 118 O OE1 . GLN A 1 18 ? -19.342 -15.905 12.242 1.00 68.51 ? 16 GLN A OE1 1 ATOM 119 N NE2 . GLN A 1 18 ? -21.563 -16.157 12.318 1.00 64.32 ? 16 GLN A NE2 1 ATOM 120 N N . PRO A 1 19 ? -20.385 -13.252 8.373 1.00 23.84 ? 17 PRO A N 1 ATOM 121 C CA . PRO A 1 19 ? -19.981 -12.165 7.464 1.00 23.62 ? 17 PRO A CA 1 ATOM 122 C C . PRO A 1 19 ? -18.682 -12.426 6.713 1.00 27.55 ? 17 PRO A C 1 ATOM 123 O O . PRO A 1 19 ? -17.832 -13.182 7.186 1.00 27.53 ? 17 PRO A O 1 ATOM 124 C CB . PRO A 1 19 ? -19.854 -10.946 8.392 1.00 25.38 ? 17 PRO A CB 1 ATOM 125 C CG . PRO A 1 19 ? -20.504 -11.343 9.683 1.00 29.72 ? 17 PRO A CG 1 ATOM 126 C CD . PRO A 1 19 ? -20.314 -12.818 9.782 1.00 25.26 ? 17 PRO A CD 1 ATOM 127 N N . SER A 1 20 ? -18.539 -11.797 5.537 1.00 24.00 ? 18 SER A N 1 ATOM 128 C CA . SER A 1 20 ? -17.341 -11.889 4.702 1.00 23.81 ? 18 SER A CA 1 ATOM 129 C C . SER A 1 20 ? -16.292 -10.870 5.180 1.00 26.52 ? 18 SER A C 1 ATOM 130 O O . SER A 1 20 ? -15.111 -10.992 4.850 1.00 26.68 ? 18 SER A O 1 ATOM 131 C CB . SER A 1 20 ? -17.695 -11.642 3.238 1.00 28.03 ? 18 SER A CB 1 ATOM 132 O OG . SER A 1 20 ? -18.279 -10.363 3.043 1.00 37.03 ? 18 SER A OG 1 ATOM 133 N N . PHE A 1 21 ? -16.737 -9.882 5.973 1.00 21.22 ? 19 PHE A N 1 ATOM 134 C CA . PHE A 1 21 ? -15.939 -8.789 6.528 1.00 20.14 ? 19 PHE A CA 1 ATOM 135 C C . PHE A 1 21 ? -15.709 -8.956 8.031 1.00 23.54 ? 19 PHE A C 1 ATOM 136 O O . PHE A 1 21 ? -16.543 -9.543 8.728 1.00 23.34 ? 19 PHE A O 1 ATOM 137 C CB . PHE A 1 21 ? -16.646 -7.438 6.258 1.00 21.49 ? 19 PHE A CB 1 ATOM 138 C CG . PHE A 1 21 ? -18.025 -7.334 6.873 1.00 22.51 ? 19 PHE A CG 1 ATOM 139 C CD1 . PHE A 1 21 ? -19.144 -7.813 6.198 1.00 24.32 ? 19 PHE A CD1 1 ATOM 140 C CD2 . PHE A 1 21 ? -18.202 -6.789 8.140 1.00 25.10 ? 19 PHE A CD2 1 ATOM 141 C CE1 . PHE A 1 21 ? -20.412 -7.747 6.780 1.00 26.84 ? 19 PHE A CE1 1 ATOM 142 C CE2 . PHE A 1 21 ? -19.466 -6.740 8.728 1.00 25.81 ? 19 PHE A CE2 1 ATOM 143 C CZ . PHE A 1 21 ? -20.558 -7.233 8.050 1.00 24.73 ? 19 PHE A CZ 1 ATOM 144 N N . ARG A 1 22 ? -14.604 -8.391 8.533 1.00 19.79 ? 20 ARG A N 1 ATOM 145 C CA . ARG A 1 22 ? -14.282 -8.394 9.958 1.00 19.32 ? 20 ARG A CA 1 ATOM 146 C C . ARG A 1 22 ? -15.061 -7.265 10.633 1.00 22.31 ? 20 ARG A C 1 ATOM 147 O O . ARG A 1 22 ? -15.241 -6.199 10.044 1.00 21.19 ? 20 ARG A O 1 ATOM 148 C CB . ARG A 1 22 ? -12.773 -8.201 10.183 1.00 19.72 ? 20 ARG A CB 1 ATOM 149 C CG . ARG A 1 22 ? -11.939 -9.410 9.770 1.00 30.89 ? 20 ARG A CG 1 ATOM 150 C CD . ARG A 1 22 ? -10.439 -9.171 9.868 1.00 40.56 ? 20 ARG A CD 1 ATOM 151 N NE . ARG A 1 22 ? -9.963 -8.074 9.016 1.00 48.38 ? 20 ARG A NE 1 ATOM 152 C CZ . ARG A 1 22 ? -9.703 -8.174 7.713 1.00 61.85 ? 20 ARG A CZ 1 ATOM 153 N NH1 . ARG A 1 22 ? -9.894 -9.322 7.075 1.00 48.38 ? 20 ARG A NH1 1 ATOM 154 N NH2 . ARG A 1 22 ? -9.268 -7.120 7.035 1.00 48.71 ? 20 ARG A NH2 1 ATOM 155 N N . GLN A 1 23 ? -15.538 -7.508 11.855 1.00 19.40 ? 21 GLN A N 1 ATOM 156 C CA . GLN A 1 23 ? -16.284 -6.507 12.616 1.00 19.14 ? 21 GLN A CA 1 ATOM 157 C C . GLN A 1 23 ? -15.857 -6.460 14.069 1.00 23.07 ? 21 GLN A C 1 ATOM 158 O O . GLN A 1 23 ? -15.535 -7.495 14.652 1.00 22.20 ? 21 GLN A O 1 ATOM 159 C CB . GLN A 1 23 ? -17.806 -6.636 12.440 1.00 20.16 ? 21 GLN A CB 1 ATOM 160 C CG . GLN A 1 23 ? -18.391 -8.014 12.753 1.00 25.33 ? 21 GLN A CG 1 ATOM 161 C CD . GLN A 1 23 ? -19.898 -7.989 12.855 1.00 36.09 ? 21 GLN A CD 1 ATOM 162 O OE1 . GLN A 1 23 ? -20.536 -6.930 12.872 1.00 28.62 ? 21 GLN A OE1 1 ATOM 163 N NE2 . GLN A 1 23 ? -20.501 -9.163 12.954 1.00 28.06 ? 21 GLN A NE2 1 ATOM 164 N N . TYR A 1 24 ? -15.819 -5.245 14.637 1.00 20.15 ? 22 TYR A N 1 ATOM 165 C CA . TYR A 1 24 ? -15.345 -5.003 15.997 1.00 19.91 ? 22 TYR A CA 1 ATOM 166 C C . TYR A 1 24 ? -16.347 -4.219 16.826 1.00 23.17 ? 22 TYR A C 1 ATOM 167 O O . TYR A 1 24 ? -17.020 -3.333 16.304 1.00 22.58 ? 22 TYR A O 1 ATOM 168 C CB . TYR A 1 24 ? -13.998 -4.251 15.962 1.00 21.21 ? 22 TYR A CB 1 ATOM 169 C CG . TYR A 1 24 ? -12.905 -4.960 15.190 1.00 23.39 ? 22 TYR A CG 1 ATOM 170 C CD1 . TYR A 1 24 ? -12.817 -4.848 13.804 1.00 25.59 ? 22 TYR A CD1 1 ATOM 171 C CD2 . TYR A 1 24 ? -11.929 -5.701 15.847 1.00 24.19 ? 22 TYR A CD2 1 ATOM 172 C CE1 . TYR A 1 24 ? -11.822 -5.510 13.086 1.00 26.81 ? 22 TYR A CE1 1 ATOM 173 C CE2 . TYR A 1 24 ? -10.919 -6.355 15.141 1.00 25.10 ? 22 TYR A CE2 1 ATOM 174 C CZ . TYR A 1 24 ? -10.871 -6.258 13.761 1.00 33.66 ? 22 TYR A CZ 1 ATOM 175 O OH . TYR A 1 24 ? -9.874 -6.893 13.060 1.00 35.96 ? 22 TYR A OH 1 ATOM 176 N N . SER A 1 25 ? -16.425 -4.540 18.124 1.00 19.17 ? 23 SER A N 1 ATOM 177 C CA . SER A 1 25 ? -17.287 -3.873 19.092 1.00 18.61 ? 23 SER A CA 1 ATOM 178 C C . SER A 1 25 ? -16.536 -3.742 20.409 1.00 22.82 ? 23 SER A C 1 ATOM 179 O O . SER A 1 25 ? -16.122 -4.743 20.996 1.00 22.06 ? 23 SER A O 1 ATOM 180 C CB . SER A 1 25 ? -18.598 -4.629 19.275 1.00 20.82 ? 23 SER A CB 1 ATOM 181 O OG . SER A 1 25 ? -19.482 -3.938 20.143 1.00 25.32 ? 23 SER A OG 1 ATOM 182 N N . GLY A 1 26 ? -16.321 -2.500 20.824 1.00 19.62 ? 24 GLY A N 1 ATOM 183 C CA . GLY A 1 26 ? -15.598 -2.185 22.047 1.00 19.45 ? 24 GLY A CA 1 ATOM 184 C C . GLY A 1 26 ? -15.746 -0.740 22.464 1.00 23.21 ? 24 GLY A C 1 ATOM 185 O O . GLY A 1 26 ? -16.764 -0.106 22.169 1.00 22.84 ? 24 GLY A O 1 ATOM 186 N N . TYR A 1 27 ? -14.714 -0.199 23.123 1.00 19.40 ? 25 TYR A N 1 ATOM 187 C CA . TYR A 1 27 ? -14.756 1.174 23.616 1.00 19.14 ? 25 TYR A CA 1 ATOM 188 C C . TYR A 1 27 ? -13.635 2.071 23.138 1.00 22.83 ? 25 TYR A C 1 ATOM 189 O O . TYR A 1 27 ? -12.491 1.634 23.012 1.00 22.25 ? 25 TYR A O 1 ATOM 190 C CB . TYR A 1 27 ? -14.882 1.199 25.153 1.00 20.23 ? 25 TYR A CB 1 ATOM 191 C CG . TYR A 1 27 ? -16.221 0.678 25.626 1.00 21.71 ? 25 TYR A CG 1 ATOM 192 C CD1 . TYR A 1 27 ? -16.416 -0.680 25.867 1.00 23.76 ? 25 TYR A CD1 1 ATOM 193 C CD2 . TYR A 1 27 ? -17.311 1.530 25.773 1.00 22.25 ? 25 TYR A CD2 1 ATOM 194 C CE1 . TYR A 1 27 ? -17.663 -1.175 26.244 1.00 24.47 ? 25 TYR A CE1 1 ATOM 195 C CE2 . TYR A 1 27 ? -18.558 1.048 26.163 1.00 22.90 ? 25 TYR A CE2 1 ATOM 196 C CZ . TYR A 1 27 ? -18.731 -0.307 26.391 1.00 29.51 ? 25 TYR A CZ 1 ATOM 197 O OH . TYR A 1 27 ? -19.959 -0.791 26.762 1.00 29.07 ? 25 TYR A OH 1 ATOM 198 N N . LEU A 1 28 ? -13.986 3.334 22.858 1.00 19.56 ? 26 LEU A N 1 ATOM 199 C CA . LEU A 1 28 ? -13.057 4.389 22.462 1.00 19.13 ? 26 LEU A CA 1 ATOM 200 C C . LEU A 1 28 ? -13.017 5.392 23.599 1.00 22.76 ? 26 LEU A C 1 ATOM 201 O O . LEU A 1 28 ? -14.070 5.776 24.122 1.00 22.11 ? 26 LEU A O 1 ATOM 202 C CB . LEU A 1 28 ? -13.468 5.087 21.148 1.00 18.99 ? 26 LEU A CB 1 ATOM 203 C CG . LEU A 1 28 ? -13.549 4.236 19.869 1.00 23.46 ? 26 LEU A CG 1 ATOM 204 C CD1 . LEU A 1 28 ? -13.873 5.094 18.671 1.00 23.60 ? 26 LEU A CD1 1 ATOM 205 C CD2 . LEU A 1 28 ? -12.263 3.471 19.606 1.00 25.45 ? 26 LEU A CD2 1 ATOM 206 N N . LYS A 1 29 ? -11.810 5.785 24.013 1.00 19.40 ? 27 LYS A N 1 ATOM 207 C CA . LYS A 1 29 ? -11.654 6.729 25.108 1.00 19.22 ? 27 LYS A CA 1 ATOM 208 C C . LYS A 1 29 ? -11.928 8.163 24.672 1.00 23.21 ? 27 LYS A C 1 ATOM 209 O O . LYS A 1 29 ? -11.275 8.680 23.760 1.00 22.76 ? 27 LYS A O 1 ATOM 210 C CB . LYS A 1 29 ? -10.271 6.595 25.779 1.00 21.44 ? 27 LYS A CB 1 ATOM 211 C CG . LYS A 1 29 ? -10.137 7.357 27.104 1.00 29.62 ? 27 LYS A CG 1 ATOM 212 C CD . LYS A 1 29 ? -10.851 6.652 28.262 1.00 37.09 ? 27 LYS A CD 1 ATOM 213 C CE . LYS A 1 29 ? -11.256 7.591 29.374 1.00 44.84 ? 27 LYS A CE 1 ATOM 214 N NZ . LYS A 1 29 ? -10.087 8.122 30.125 1.00 53.48 ? 27 LYS A NZ 1 ATOM 215 N N . GLY A 1 30 ? -12.901 8.779 25.334 1.00 19.75 ? 28 GLY A N 1 ATOM 216 C CA . GLY A 1 30 ? -13.258 10.176 25.126 1.00 19.55 ? 28 GLY A CA 1 ATOM 217 C C . GLY A 1 30 ? -12.533 11.034 26.144 1.00 23.75 ? 28 GLY A C 1 ATOM 218 O O . GLY A 1 30 ? -11.496 10.624 26.677 1.00 22.73 ? 28 GLY A O 1 ATOM 219 N N . SER A 1 31 ? -13.073 12.222 26.437 1.00 21.50 ? 29 SER A N 1 ATOM 220 C CA . SER A 1 31 ? -12.480 13.121 27.430 1.00 21.51 ? 29 SER A CA 1 ATOM 221 C C . SER A 1 31 ? -12.866 12.662 28.840 1.00 25.57 ? 29 SER A C 1 ATOM 222 O O . SER A 1 31 ? -13.871 11.974 28.997 1.00 24.98 ? 29 SER A O 1 ATOM 223 C CB . SER A 1 31 ? -12.936 14.556 27.191 1.00 24.88 ? 29 SER A CB 1 ATOM 224 O OG . SER A 1 31 ? -14.348 14.677 27.264 1.00 32.43 ? 29 SER A OG 1 ATOM 225 N N . GLY A 1 32 ? -12.062 13.035 29.839 1.00 22.22 ? 30 GLY A N 1 ATOM 226 C CA . GLY A 1 32 ? -12.290 12.679 31.238 1.00 21.76 ? 30 GLY A CA 1 ATOM 227 C C . GLY A 1 32 ? -12.363 11.185 31.481 1.00 24.93 ? 30 GLY A C 1 ATOM 228 O O . GLY A 1 32 ? -11.440 10.453 31.121 1.00 24.41 ? 30 GLY A O 1 ATOM 229 N N . SER A 1 33 ? -13.483 10.723 32.063 1.00 21.29 ? 31 SER A N 1 ATOM 230 C CA . SER A 1 33 ? -13.719 9.307 32.354 1.00 20.72 ? 31 SER A CA 1 ATOM 231 C C . SER A 1 33 ? -14.732 8.668 31.384 1.00 23.32 ? 31 SER A C 1 ATOM 232 O O . SER A 1 33 ? -15.300 7.619 31.699 1.00 22.41 ? 31 SER A O 1 ATOM 233 C CB . SER A 1 33 ? -14.160 9.130 33.807 1.00 24.18 ? 31 SER A CB 1 ATOM 234 O OG . SER A 1 33 ? -15.423 9.729 34.052 1.00 31.74 ? 31 SER A OG 1 ATOM 235 N N . LYS A 1 34 ? -14.926 9.277 30.193 1.00 19.45 ? 32 LYS A N 1 ATOM 236 C CA . LYS A 1 34 ? -15.880 8.800 29.181 1.00 18.99 ? 32 LYS A CA 1 ATOM 237 C C . LYS A 1 34 ? -15.344 7.649 28.327 1.00 23.20 ? 32 LYS A C 1 ATOM 238 O O . LYS A 1 34 ? -14.233 7.728 27.803 1.00 22.77 ? 32 LYS A O 1 ATOM 239 C CB . LYS A 1 34 ? -16.358 9.950 28.274 1.00 20.72 ? 32 LYS A CB 1 ATOM 240 C CG . LYS A 1 34 ? -17.012 11.112 29.013 1.00 26.52 ? 32 LYS A CG 1 ATOM 241 C CD . LYS A 1 34 ? -17.179 12.315 28.091 1.00 30.09 ? 32 LYS A CD 1 ATOM 242 C CE . LYS A 1 34 ? -17.404 13.603 28.848 1.00 30.74 ? 32 LYS A CE 1 ATOM 243 N NZ . LYS A 1 34 ? -16.153 14.112 29.470 1.00 36.11 ? 32 LYS A NZ 1 ATOM 244 N N . HIS A 1 35 ? -16.160 6.594 28.168 1.00 20.22 ? 33 HIS A N 1 ATOM 245 C CA . HIS A 1 35 ? -15.854 5.420 27.349 1.00 20.06 ? 33 HIS A CA 1 ATOM 246 C C . HIS A 1 35 ? -16.994 5.267 26.348 1.00 23.51 ? 33 HIS A C 1 ATOM 247 O O . HIS A 1 35 ? -18.114 4.910 26.729 1.00 23.31 ? 33 HIS A O 1 ATOM 248 C CB . HIS A 1 35 ? -15.687 4.157 28.213 1.00 20.96 ? 33 HIS A CB 1 ATOM 249 C CG . HIS A 1 35 ? -14.708 4.321 29.333 1.00 24.38 ? 33 HIS A CG 1 ATOM 250 N ND1 . HIS A 1 35 ? -13.353 4.127 29.142 1.00 26.12 ? 33 HIS A ND1 1 ATOM 251 C CD2 . HIS A 1 35 ? -14.923 4.663 30.624 1.00 26.12 ? 33 HIS A CD2 1 ATOM 252 C CE1 . HIS A 1 35 ? -12.787 4.357 30.316 1.00 25.56 ? 33 HIS A CE1 1 ATOM 253 N NE2 . HIS A 1 35 ? -13.692 4.685 31.239 1.00 25.92 ? 33 HIS A NE2 1 ATOM 254 N N . LEU A 1 36 ? -16.726 5.610 25.079 1.00 18.94 ? 34 LEU A N 1 ATOM 255 C CA . LEU A 1 36 ? -17.738 5.572 24.027 1.00 18.15 ? 34 LEU A CA 1 ATOM 256 C C . LEU A 1 36 ? -17.757 4.242 23.293 1.00 21.39 ? 34 LEU A C 1 ATOM 257 O O . LEU A 1 36 ? -16.732 3.817 22.759 1.00 20.94 ? 34 LEU A O 1 ATOM 258 C CB . LEU A 1 36 ? -17.589 6.757 23.048 1.00 18.00 ? 34 LEU A CB 1 ATOM 259 C CG . LEU A 1 36 ? -17.451 8.177 23.647 1.00 22.22 ? 34 LEU A CG 1 ATOM 260 C CD1 . LEU A 1 36 ? -17.179 9.197 22.562 1.00 22.23 ? 34 LEU A CD1 1 ATOM 261 C CD2 . LEU A 1 36 ? -18.695 8.590 24.429 1.00 23.71 ? 34 LEU A CD2 1 ATOM 262 N N . HIS A 1 37 ? -18.924 3.572 23.288 1.00 17.81 ? 35 HIS A N 1 ATOM 263 C CA . HIS A 1 37 ? -19.090 2.287 22.615 1.00 17.23 ? 35 HIS A CA 1 ATOM 264 C C . HIS A 1 37 ? -19.121 2.450 21.109 1.00 20.55 ? 35 HIS A C 1 ATOM 265 O O . HIS A 1 37 ? -19.909 3.238 20.580 1.00 20.29 ? 35 HIS A O 1 ATOM 266 C CB . HIS A 1 37 ? -20.330 1.517 23.101 1.00 17.77 ? 35 HIS A CB 1 ATOM 267 C CG . HIS A 1 37 ? -20.614 0.291 22.283 1.00 20.90 ? 35 HIS A CG 1 ATOM 268 N ND1 . HIS A 1 37 ? -21.741 0.200 21.489 1.00 22.44 ? 35 HIS A ND1 1 ATOM 269 C CD2 . HIS A 1 37 ? -19.860 -0.817 22.096 1.00 22.45 ? 35 HIS A CD2 1 ATOM 270 C CE1 . HIS A 1 37 ? -21.662 -0.973 20.884 1.00 21.79 ? 35 HIS A CE1 1 ATOM 271 N NE2 . HIS A 1 37 ? -20.543 -1.616 21.212 1.00 22.18 ? 35 HIS A NE2 1 ATOM 272 N N . TYR A 1 38 ? -18.258 1.693 20.427 1.00 16.95 ? 36 TYR A N 1 ATOM 273 C CA . TYR A 1 38 ? -18.185 1.687 18.977 1.00 16.64 ? 36 TYR A CA 1 ATOM 274 C C . TYR A 1 38 ? -18.514 0.305 18.427 1.00 20.56 ? 36 TYR A C 1 ATOM 275 O O . TYR A 1 38 ? -18.300 -0.708 19.095 1.00 19.68 ? 36 TYR A O 1 ATOM 276 C CB . TYR A 1 38 ? -16.801 2.174 18.479 1.00 17.67 ? 36 TYR A CB 1 ATOM 277 C CG . TYR A 1 38 ? -15.707 1.123 18.493 1.00 19.12 ? 36 TYR A CG 1 ATOM 278 C CD1 . TYR A 1 38 ? -14.911 0.931 19.618 1.00 20.88 ? 36 TYR A CD1 1 ATOM 279 C CD2 . TYR A 1 38 ? -15.449 0.338 17.371 1.00 19.81 ? 36 TYR A CD2 1 ATOM 280 C CE1 . TYR A 1 38 ? -13.891 -0.019 19.631 1.00 21.28 ? 36 TYR A CE1 1 ATOM 281 C CE2 . TYR A 1 38 ? -14.450 -0.634 17.381 1.00 20.74 ? 36 TYR A CE2 1 ATOM 282 C CZ . TYR A 1 38 ? -13.673 -0.809 18.514 1.00 27.58 ? 36 TYR A CZ 1 ATOM 283 O OH . TYR A 1 38 ? -12.675 -1.752 18.525 1.00 28.74 ? 36 TYR A OH 1 ATOM 284 N N . TRP A 1 39 ? -19.021 0.281 17.197 1.00 17.50 ? 37 TRP A N 1 ATOM 285 C CA . TRP A 1 39 ? -19.285 -0.920 16.422 1.00 17.25 ? 37 TRP A CA 1 ATOM 286 C C . TRP A 1 39 ? -18.751 -0.566 15.042 1.00 20.52 ? 37 TRP A C 1 ATOM 287 O O . TRP A 1 39 ? -19.306 0.293 14.348 1.00 20.02 ? 37 TRP A O 1 ATOM 288 C CB . TRP A 1 39 ? -20.777 -1.294 16.409 1.00 16.16 ? 37 TRP A CB 1 ATOM 289 C CG . TRP A 1 39 ? -21.101 -2.644 15.817 1.00 17.09 ? 37 TRP A CG 1 ATOM 290 C CD1 . TRP A 1 39 ? -20.371 -3.344 14.899 1.00 19.93 ? 37 TRP A CD1 1 ATOM 291 C CD2 . TRP A 1 39 ? -22.301 -3.401 16.033 1.00 16.93 ? 37 TRP A CD2 1 ATOM 292 N NE1 . TRP A 1 39 ? -21.031 -4.498 14.547 1.00 19.28 ? 37 TRP A NE1 1 ATOM 293 C CE2 . TRP A 1 39 ? -22.221 -4.557 15.224 1.00 20.77 ? 37 TRP A CE2 1 ATOM 294 C CE3 . TRP A 1 39 ? -23.449 -3.205 16.822 1.00 18.17 ? 37 TRP A CE3 1 ATOM 295 C CZ2 . TRP A 1 39 ? -23.231 -5.524 15.199 1.00 20.04 ? 37 TRP A CZ2 1 ATOM 296 C CZ3 . TRP A 1 39 ? -24.454 -4.159 16.787 1.00 19.74 ? 37 TRP A CZ3 1 ATOM 297 C CH2 . TRP A 1 39 ? -24.338 -5.306 15.988 1.00 20.36 ? 37 TRP A CH2 1 ATOM 298 N N . PHE A 1 40 ? -17.601 -1.152 14.705 1.00 16.43 ? 38 PHE A N 1 ATOM 299 C CA . PHE A 1 40 ? -16.885 -0.903 13.463 1.00 16.01 ? 38 PHE A CA 1 ATOM 300 C C . PHE A 1 40 ? -17.068 -2.061 12.499 1.00 19.71 ? 38 PHE A C 1 ATOM 301 O O . PHE A 1 40 ? -16.782 -3.208 12.845 1.00 18.79 ? 38 PHE A O 1 ATOM 302 C CB . PHE A 1 40 ? -15.398 -0.643 13.769 1.00 17.66 ? 38 PHE A CB 1 ATOM 303 C CG . PHE A 1 40 ? -14.480 -0.423 12.588 1.00 19.03 ? 38 PHE A CG 1 ATOM 304 C CD1 . PHE A 1 40 ? -14.681 0.642 11.718 1.00 21.72 ? 38 PHE A CD1 1 ATOM 305 C CD2 . PHE A 1 40 ? -13.371 -1.238 12.389 1.00 21.04 ? 38 PHE A CD2 1 ATOM 306 C CE1 . PHE A 1 40 ? -13.813 0.862 10.646 1.00 22.68 ? 38 PHE A CE1 1 ATOM 307 C CE2 . PHE A 1 40 ? -12.497 -1.010 11.324 1.00 23.69 ? 38 PHE A CE2 1 ATOM 308 C CZ . PHE A 1 40 ? -12.721 0.041 10.463 1.00 21.76 ? 38 PHE A CZ 1 ATOM 309 N N . VAL A 1 41 ? -17.583 -1.758 11.303 1.00 16.75 ? 39 VAL A N 1 ATOM 310 C CA . VAL A 1 41 ? -17.817 -2.750 10.255 1.00 16.73 ? 39 VAL A CA 1 ATOM 311 C C . VAL A 1 41 ? -16.910 -2.468 9.058 1.00 20.70 ? 39 VAL A C 1 ATOM 312 O O . VAL A 1 41 ? -17.056 -1.439 8.392 1.00 19.81 ? 39 VAL A O 1 ATOM 313 C CB . VAL A 1 41 ? -19.317 -2.961 9.880 1.00 20.52 ? 39 VAL A CB 1 ATOM 314 C CG1 . VAL A 1 41 ? -20.068 -3.681 10.997 1.00 20.22 ? 39 VAL A CG1 1 ATOM 315 C CG2 . VAL A 1 41 ? -20.015 -1.649 9.515 1.00 20.28 ? 39 VAL A CG2 1 ATOM 316 N N . GLU A 1 42 ? -15.930 -3.358 8.825 1.00 17.68 ? 40 GLU A N 1 ATOM 317 C CA . GLU A 1 42 ? -14.978 -3.203 7.723 1.00 17.61 ? 40 GLU A CA 1 ATOM 318 C C . GLU A 1 42 ? -15.655 -3.375 6.369 1.00 21.47 ? 40 GLU A C 1 ATOM 319 O O . GLU A 1 42 ? -16.715 -4.001 6.286 1.00 20.89 ? 40 GLU A O 1 ATOM 320 C CB . GLU A 1 42 ? -13.787 -4.160 7.870 1.00 19.01 ? 40 GLU A CB 1 ATOM 321 C CG . GLU A 1 42 ? -12.885 -3.826 9.046 1.00 27.48 ? 40 GLU A CG 1 ATOM 322 C CD . GLU A 1 42 ? -11.606 -4.630 9.173 1.00 41.13 ? 40 GLU A CD 1 ATOM 323 O OE1 . GLU A 1 42 ? -11.381 -5.546 8.350 1.00 27.73 ? 40 GLU A OE1 1 ATOM 324 O OE2 . GLU A 1 42 ? -10.807 -4.316 10.085 1.00 33.77 ? 40 GLU A OE2 1 ATOM 325 N N . SER A 1 43 ? -15.053 -2.800 5.315 1.00 18.45 ? 41 SER A N 1 ATOM 326 C CA . SER A 1 43 ? -15.583 -2.865 3.959 1.00 18.40 ? 41 SER A CA 1 ATOM 327 C C . SER A 1 43 ? -15.677 -4.285 3.425 1.00 22.65 ? 41 SER A C 1 ATOM 328 O O . SER A 1 43 ? -14.776 -5.095 3.652 1.00 21.64 ? 41 SER A O 1 ATOM 329 C CB . SER A 1 43 ? -14.762 -2.003 3.010 1.00 21.91 ? 41 SER A CB 1 ATOM 330 O OG . SER A 1 43 ? -15.339 -1.968 1.715 1.00 28.29 ? 41 SER A OG 1 ATOM 331 N N . GLN A 1 44 ? -16.777 -4.569 2.710 1.00 19.90 ? 42 GLN A N 1 ATOM 332 C CA . GLN A 1 44 ? -17.051 -5.859 2.079 1.00 20.11 ? 42 GLN A CA 1 ATOM 333 C C . GLN A 1 44 ? -16.164 -6.053 0.841 1.00 25.56 ? 42 GLN A C 1 ATOM 334 O O . GLN A 1 44 ? -15.970 -7.185 0.390 1.00 25.26 ? 42 GLN A O 1 ATOM 335 C CB . GLN A 1 44 ? -18.542 -5.980 1.719 1.00 21.17 ? 42 GLN A CB 1 ATOM 336 C CG . GLN A 1 44 ? -19.453 -6.099 2.942 1.00 27.56 ? 42 GLN A CG 1 ATOM 337 C CD . GLN A 1 44 ? -20.873 -6.499 2.619 1.00 41.29 ? 42 GLN A CD 1 ATOM 338 O OE1 . GLN A 1 44 ? -21.139 -7.324 1.735 1.00 35.59 ? 42 GLN A OE1 1 ATOM 339 N NE2 . GLN A 1 44 ? -21.819 -5.968 3.379 1.00 31.18 ? 42 GLN A NE2 1 ATOM 340 N N . LYS A 1 45 ? -15.626 -4.942 0.304 1.00 23.02 ? 43 LYS A N 1 ATOM 341 C CA . LYS A 1 45 ? -14.732 -4.915 -0.849 1.00 23.39 ? 43 LYS A CA 1 ATOM 342 C C . LYS A 1 45 ? -13.513 -4.048 -0.508 1.00 27.78 ? 43 LYS A C 1 ATOM 343 O O . LYS A 1 45 ? -13.662 -2.850 -0.247 1.00 27.37 ? 43 LYS A O 1 ATOM 344 C CB . LYS A 1 45 ? -15.468 -4.384 -2.096 1.00 26.18 ? 43 LYS A CB 1 ATOM 345 C CG . LYS A 1 45 ? -14.692 -4.552 -3.399 1.00 42.46 ? 43 LYS A CG 1 ATOM 346 C CD . LYS A 1 45 ? -15.413 -3.896 -4.567 1.00 54.47 ? 43 LYS A CD 1 ATOM 347 C CE . LYS A 1 45 ? -14.630 -4.015 -5.852 1.00 67.64 ? 43 LYS A CE 1 ATOM 348 N NZ . LYS A 1 45 ? -15.342 -3.383 -6.993 1.00 77.68 ? 43 LYS A NZ 1 ATOM 349 N N . ASP A 1 46 ? -12.316 -4.675 -0.494 1.00 24.61 ? 44 ASP A N 1 ATOM 350 C CA . ASP A 1 46 ? -11.011 -4.059 -0.213 1.00 24.37 ? 44 ASP A CA 1 ATOM 351 C C . ASP A 1 46 ? -11.000 -3.195 1.085 1.00 27.52 ? 44 ASP A C 1 ATOM 352 O O . ASP A 1 46 ? -10.897 -1.970 0.988 1.00 26.39 ? 44 ASP A O 1 ATOM 353 C CB . ASP A 1 46 ? -10.512 -3.280 -1.457 1.00 26.36 ? 44 ASP A CB 1 ATOM 354 C CG . ASP A 1 46 ? -9.075 -2.782 -1.433 1.00 38.31 ? 44 ASP A CG 1 ATOM 355 O OD1 . ASP A 1 46 ? -8.303 -3.216 -0.546 1.00 39.00 ? 44 ASP A OD1 1 ATOM 356 O OD2 . ASP A 1 46 ? -8.712 -1.985 -2.324 1.00 45.38 ? 44 ASP A OD2 1 ATOM 357 N N . PRO A 1 47 ? -11.105 -3.798 2.302 1.00 24.19 ? 45 PRO A N 1 ATOM 358 C CA . PRO A 1 47 ? -11.117 -2.977 3.531 1.00 24.25 ? 45 PRO A CA 1 ATOM 359 C C . PRO A 1 47 ? -9.857 -2.151 3.785 1.00 28.54 ? 45 PRO A C 1 ATOM 360 O O . PRO A 1 47 ? -9.965 -1.048 4.316 1.00 27.91 ? 45 PRO A O 1 ATOM 361 C CB . PRO A 1 47 ? -11.361 -4.001 4.645 1.00 25.97 ? 45 PRO A CB 1 ATOM 362 C CG . PRO A 1 47 ? -10.914 -5.300 4.077 1.00 30.28 ? 45 PRO A CG 1 ATOM 363 C CD . PRO A 1 47 ? -11.257 -5.233 2.623 1.00 25.75 ? 45 PRO A CD 1 ATOM 364 N N . GLU A 1 48 ? -8.676 -2.666 3.380 1.00 25.58 ? 46 GLU A N 1 ATOM 365 C CA . GLU A 1 48 ? -7.380 -2.000 3.557 1.00 25.60 ? 46 GLU A CA 1 ATOM 366 C C . GLU A 1 48 ? -7.274 -0.646 2.848 1.00 29.67 ? 46 GLU A C 1 ATOM 367 O O . GLU A 1 48 ? -6.634 0.261 3.381 1.00 29.76 ? 46 GLU A O 1 ATOM 368 C CB . GLU A 1 48 ? -6.225 -2.921 3.130 1.00 26.99 ? 46 GLU A CB 1 ATOM 369 N N . ASN A 1 49 ? -7.898 -0.505 1.662 1.00 25.93 ? 47 ASN A N 1 ATOM 370 C CA . ASN A 1 49 ? -7.855 0.739 0.886 1.00 25.73 ? 47 ASN A CA 1 ATOM 371 C C . ASN A 1 49 ? -9.159 1.550 0.892 1.00 28.96 ? 47 ASN A C 1 ATOM 372 O O . ASN A 1 49 ? -9.147 2.717 0.494 1.00 29.15 ? 47 ASN A O 1 ATOM 373 C CB . ASN A 1 49 ? -7.362 0.483 -0.541 1.00 27.19 ? 47 ASN A CB 1 ATOM 374 C CG . ASN A 1 49 ? -5.979 -0.115 -0.604 1.00 50.65 ? 47 ASN A CG 1 ATOM 375 O OD1 . ASN A 1 49 ? -4.976 0.530 -0.278 1.00 46.02 ? 47 ASN A OD1 1 ATOM 376 N ND2 . ASN A 1 49 ? -5.897 -1.369 -1.018 1.00 42.36 ? 47 ASN A ND2 1 ATOM 377 N N . SER A 1 50 ? -10.271 0.945 1.352 1.00 24.22 ? 48 SER A N 1 ATOM 378 C CA . SER A 1 50 ? -11.578 1.606 1.424 1.00 23.15 ? 48 SER A CA 1 ATOM 379 C C . SER A 1 50 ? -11.593 2.747 2.455 1.00 25.01 ? 48 SER A C 1 ATOM 380 O O . SER A 1 50 ? -10.871 2.664 3.453 1.00 24.39 ? 48 SER A O 1 ATOM 381 C CB . SER A 1 50 ? -12.675 0.597 1.743 1.00 26.16 ? 48 SER A CB 1 ATOM 382 O OG . SER A 1 50 ? -12.937 -0.244 0.632 1.00 33.32 ? 48 SER A OG 1 ATOM 383 N N . PRO A 1 51 ? -12.393 3.819 2.238 1.00 20.11 ? 49 PRO A N 1 ATOM 384 C CA . PRO A 1 51 ? -12.408 4.924 3.213 1.00 19.45 ? 49 PRO A CA 1 ATOM 385 C C . PRO A 1 51 ? -12.992 4.550 4.571 1.00 21.89 ? 49 PRO A C 1 ATOM 386 O O . PRO A 1 51 ? -13.786 3.614 4.671 1.00 21.25 ? 49 PRO A O 1 ATOM 387 C CB . PRO A 1 51 ? -13.263 6.003 2.530 1.00 21.26 ? 49 PRO A CB 1 ATOM 388 C CG . PRO A 1 51 ? -13.415 5.566 1.111 1.00 25.96 ? 49 PRO A CG 1 ATOM 389 C CD . PRO A 1 51 ? -13.312 4.086 1.114 1.00 21.54 ? 49 PRO A CD 1 ATOM 390 N N . VAL A 1 52 ? -12.583 5.289 5.614 1.00 17.89 ? 50 VAL A N 1 ATOM 391 C CA . VAL A 1 52 ? -13.080 5.136 6.979 1.00 17.40 ? 50 VAL A CA 1 ATOM 392 C C . VAL A 1 52 ? -14.203 6.167 7.137 1.00 21.63 ? 50 VAL A C 1 ATOM 393 O O . VAL A 1 52 ? -13.974 7.364 6.941 1.00 21.21 ? 50 VAL A O 1 ATOM 394 C CB . VAL A 1 52 ? -11.962 5.273 8.051 1.00 20.89 ? 50 VAL A CB 1 ATOM 395 C CG1 . VAL A 1 52 ? -12.545 5.324 9.463 1.00 20.68 ? 50 VAL A CG1 1 ATOM 396 C CG2 . VAL A 1 52 ? -10.953 4.132 7.934 1.00 20.52 ? 50 VAL A CG2 1 ATOM 397 N N . VAL A 1 53 ? -15.424 5.691 7.435 1.00 18.31 ? 51 VAL A N 1 ATOM 398 C CA . VAL A 1 53 ? -16.604 6.550 7.559 1.00 18.29 ? 51 VAL A CA 1 ATOM 399 C C . VAL A 1 53 ? -17.208 6.501 8.965 1.00 20.84 ? 51 VAL A C 1 ATOM 400 O O . VAL A 1 53 ? -17.699 5.457 9.396 1.00 20.25 ? 51 VAL A O 1 ATOM 401 C CB . VAL A 1 53 ? -17.661 6.264 6.446 1.00 22.37 ? 51 VAL A CB 1 ATOM 402 C CG1 . VAL A 1 53 ? -18.913 7.123 6.627 1.00 22.30 ? 51 VAL A CG1 1 ATOM 403 C CG2 . VAL A 1 53 ? -17.074 6.476 5.052 1.00 22.20 ? 51 VAL A CG2 1 ATOM 404 N N . LEU A 1 54 ? -17.184 7.637 9.671 1.00 16.86 ? 52 LEU A N 1 ATOM 405 C CA . LEU A 1 54 ? -17.793 7.730 10.994 1.00 16.22 ? 52 LEU A CA 1 ATOM 406 C C . LEU A 1 54 ? -19.270 8.073 10.818 1.00 19.14 ? 52 LEU A C 1 ATOM 407 O O . LEU A 1 54 ? -19.599 8.952 10.024 1.00 18.41 ? 52 LEU A O 1 ATOM 408 C CB . LEU A 1 54 ? -17.089 8.790 11.876 1.00 16.22 ? 52 LEU A CB 1 ATOM 409 C CG . LEU A 1 54 ? -17.767 9.123 13.226 1.00 20.61 ? 52 LEU A CG 1 ATOM 410 C CD1 . LEU A 1 54 ? -17.552 8.023 14.255 1.00 20.76 ? 52 LEU A CD1 1 ATOM 411 C CD2 . LEU A 1 54 ? -17.285 10.445 13.769 1.00 23.01 ? 52 LEU A CD2 1 ATOM 412 N N . TRP A 1 55 ? -20.154 7.373 11.546 1.00 15.66 ? 53 TRP A N 1 ATOM 413 C CA . TRP A 1 55 ? -21.587 7.647 11.522 1.00 15.00 ? 53 TRP A CA 1 ATOM 414 C C . TRP A 1 55 ? -22.082 8.009 12.916 1.00 17.80 ? 53 TRP A C 1 ATOM 415 O O . TRP A 1 55 ? -21.863 7.258 13.870 1.00 17.10 ? 53 TRP A O 1 ATOM 416 C CB . TRP A 1 55 ? -22.403 6.485 10.931 1.00 13.65 ? 53 TRP A CB 1 ATOM 417 C CG . TRP A 1 55 ? -23.886 6.731 10.965 1.00 14.47 ? 53 TRP A CG 1 ATOM 418 C CD1 . TRP A 1 55 ? -24.766 6.298 11.912 1.00 17.34 ? 53 TRP A CD1 1 ATOM 419 C CD2 . TRP A 1 55 ? -24.640 7.552 10.061 1.00 14.24 ? 53 TRP A CD2 1 ATOM 420 N NE1 . TRP A 1 55 ? -26.031 6.765 11.634 1.00 16.88 ? 53 TRP A NE1 1 ATOM 421 C CE2 . TRP A 1 55 ? -25.984 7.531 10.498 1.00 18.22 ? 53 TRP A CE2 1 ATOM 422 C CE3 . TRP A 1 55 ? -24.316 8.282 8.904 1.00 15.37 ? 53 TRP A CE3 1 ATOM 423 C CZ2 . TRP A 1 55 ? -27.003 8.210 9.819 1.00 17.42 ? 53 TRP A CZ2 1 ATOM 424 C CZ3 . TRP A 1 55 ? -25.328 8.948 8.228 1.00 16.86 ? 53 TRP A CZ3 1 ATOM 425 C CH2 . TRP A 1 55 ? -26.652 8.909 8.686 1.00 17.50 ? 53 TRP A CH2 1 ATOM 426 N N . LEU A 1 56 ? -22.766 9.154 13.019 1.00 13.61 ? 54 LEU A N 1 ATOM 427 C CA . LEU A 1 56 ? -23.342 9.616 14.277 1.00 13.38 ? 54 LEU A CA 1 ATOM 428 C C . LEU A 1 56 ? -24.825 9.882 14.135 1.00 17.72 ? 54 LEU A C 1 ATOM 429 O O . LEU A 1 56 ? -25.225 10.635 13.251 1.00 17.39 ? 54 LEU A O 1 ATOM 430 C CB . LEU A 1 56 ? -22.654 10.900 14.791 1.00 13.06 ? 54 LEU A CB 1 ATOM 431 C CG . LEU A 1 56 ? -21.181 10.844 15.196 1.00 16.87 ? 54 LEU A CG 1 ATOM 432 C CD1 . LEU A 1 56 ? -20.681 12.233 15.543 1.00 16.68 ? 54 LEU A CD1 1 ATOM 433 C CD2 . LEU A 1 56 ? -20.951 9.908 16.381 1.00 18.84 ? 54 LEU A CD2 1 ATOM 434 N N . ASN A 1 57 ? -25.645 9.298 15.021 1.00 14.90 ? 55 ASN A N 1 ATOM 435 C CA . ASN A 1 57 ? -27.069 9.616 15.043 1.00 14.82 ? 55 ASN A CA 1 ATOM 436 C C . ASN A 1 57 ? -27.242 10.851 15.949 1.00 19.46 ? 55 ASN A C 1 ATOM 437 O O . ASN A 1 57 ? -26.289 11.241 16.633 1.00 18.60 ? 55 ASN A O 1 ATOM 438 C CB . ASN A 1 57 ? -27.923 8.421 15.463 1.00 13.88 ? 55 ASN A CB 1 ATOM 439 C CG . ASN A 1 57 ? -28.303 7.547 14.287 1.00 29.50 ? 55 ASN A CG 1 ATOM 440 O OD1 . ASN A 1 57 ? -27.637 6.560 13.971 1.00 21.09 ? 55 ASN A OD1 1 ATOM 441 N ND2 . ASN A 1 57 ? -29.364 7.910 13.582 1.00 22.48 ? 55 ASN A ND2 1 ATOM 442 N N . GLY A 1 58 ? -28.410 11.485 15.900 1.00 16.50 ? 56 GLY A N 1 ATOM 443 C CA . GLY A 1 58 ? -28.668 12.714 16.644 1.00 16.41 ? 56 GLY A CA 1 ATOM 444 C C . GLY A 1 58 ? -29.279 12.575 18.020 1.00 20.10 ? 56 GLY A C 1 ATOM 445 O O . GLY A 1 58 ? -28.746 11.872 18.884 1.00 19.66 ? 56 GLY A O 1 ATOM 446 N N . GLY A 1 59 ? -30.378 13.296 18.216 1.00 17.08 ? 57 GLY A N 1 ATOM 447 C CA . GLY A 1 59 ? -31.118 13.365 19.469 1.00 17.15 ? 57 GLY A CA 1 ATOM 448 C C . GLY A 1 59 ? -31.239 14.805 19.943 1.00 21.31 ? 57 GLY A C 1 ATOM 449 O O . GLY A 1 59 ? -32.173 15.497 19.532 1.00 20.93 ? 57 GLY A O 1 ATOM 450 N N . PRO A 1 60 ? -30.295 15.335 20.759 1.00 17.90 ? 58 PRO A N 1 ATOM 451 C CA . PRO A 1 60 ? -29.110 14.680 21.353 1.00 17.55 ? 58 PRO A CA 1 ATOM 452 C C . PRO A 1 60 ? -29.506 13.566 22.313 1.00 21.29 ? 58 PRO A C 1 ATOM 453 O O . PRO A 1 60 ? -30.548 13.660 22.957 1.00 20.18 ? 58 PRO A O 1 ATOM 454 C CB . PRO A 1 60 ? -28.426 15.820 22.129 1.00 19.15 ? 58 PRO A CB 1 ATOM 455 C CG . PRO A 1 60 ? -29.002 17.089 21.586 1.00 23.63 ? 58 PRO A CG 1 ATOM 456 C CD . PRO A 1 60 ? -30.403 16.736 21.206 1.00 19.25 ? 58 PRO A CD 1 ATOM 457 N N . GLY A 1 61 ? -28.689 12.518 22.372 1.00 18.47 ? 59 GLY A N 1 ATOM 458 C CA . GLY A 1 61 ? -28.928 11.382 23.253 1.00 18.38 ? 59 GLY A CA 1 ATOM 459 C C . GLY A 1 61 ? -29.320 10.085 22.574 1.00 22.95 ? 59 GLY A C 1 ATOM 460 O O . GLY A 1 61 ? -29.524 9.080 23.258 1.00 22.44 ? 59 GLY A O 1 ATOM 461 N N . CYS A 1 62 ? -29.428 10.084 21.234 1.00 19.95 ? 60 CYS A N 1 ATOM 462 C CA . CYS A 1 62 ? -29.798 8.880 20.490 1.00 19.84 ? 60 CYS A CA 1 ATOM 463 C C . CYS A 1 62 ? -28.594 8.103 19.975 1.00 21.51 ? 60 CYS A C 1 ATOM 464 O O . CYS A 1 62 ? -27.579 8.697 19.609 1.00 20.93 ? 60 CYS A O 1 ATOM 465 C CB . CYS A 1 62 ? -30.792 9.194 19.380 1.00 20.72 ? 60 CYS A CB 1 ATOM 466 S SG . CYS A 1 62 ? -32.366 9.875 19.963 1.00 25.07 ? 60 CYS A SG 1 ATOM 467 N N . SER A 1 63 ? -28.716 6.767 19.966 1.00 17.01 ? 61 SER A N 1 ATOM 468 C CA . SER A 1 63 ? -27.673 5.819 19.583 1.00 16.60 ? 61 SER A CA 1 ATOM 469 C C . SER A 1 63 ? -27.439 5.674 18.090 1.00 20.07 ? 61 SER A C 1 ATOM 470 O O . SER A 1 63 ? -28.393 5.519 17.324 1.00 19.78 ? 61 SER A O 1 ATOM 471 C CB . SER A 1 63 ? -27.946 4.457 20.214 1.00 19.73 ? 61 SER A CB 1 ATOM 472 O OG . SER A 1 63 ? -27.126 3.435 19.672 1.00 24.88 ? 61 SER A OG 1 ATOM 473 N N . SER A 1 64 ? -26.150 5.634 17.697 1.00 16.25 ? 62 SER A N 1 ATOM 474 C CA . SER A 1 64 ? -25.709 5.432 16.315 1.00 15.66 ? 62 SER A CA 1 ATOM 475 C C . SER A 1 64 ? -25.937 3.989 15.837 1.00 19.08 ? 62 SER A C 1 ATOM 476 O O . SER A 1 64 ? -25.815 3.715 14.640 1.00 18.21 ? 62 SER A O 1 ATOM 477 C CB . SER A 1 64 ? -24.249 5.835 16.145 1.00 18.76 ? 62 SER A CB 1 ATOM 478 O OG . SER A 1 64 ? -24.062 7.202 16.471 1.00 26.17 ? 62 SER A OG 1 ATOM 479 N N . LEU A 1 65 ? -26.301 3.074 16.765 1.00 16.05 ? 63 LEU A N 1 ATOM 480 C CA . LEU A 1 65 ? -26.615 1.679 16.439 1.00 16.01 ? 63 LEU A CA 1 ATOM 481 C C . LEU A 1 65 ? -27.961 1.592 15.700 1.00 20.56 ? 63 LEU A C 1 ATOM 482 O O . LEU A 1 65 ? -28.252 0.571 15.073 1.00 20.11 ? 63 LEU A O 1 ATOM 483 C CB . LEU A 1 65 ? -26.571 0.756 17.674 1.00 15.98 ? 63 LEU A CB 1 ATOM 484 C CG . LEU A 1 65 ? -25.237 0.652 18.444 1.00 20.73 ? 63 LEU A CG 1 ATOM 485 C CD1 . LEU A 1 65 ? -25.309 -0.431 19.505 1.00 21.08 ? 63 LEU A CD1 1 ATOM 486 C CD2 . LEU A 1 65 ? -24.051 0.375 17.518 1.00 23.06 ? 63 LEU A CD2 1 ATOM 487 N N . ASP A 1 66 ? -28.756 2.692 15.741 1.00 17.62 ? 64 ASP A N 1 ATOM 488 C CA . ASP A 1 66 ? -30.001 2.854 14.987 1.00 17.73 ? 64 ASP A CA 1 ATOM 489 C C . ASP A 1 66 ? -29.602 2.881 13.515 1.00 21.80 ? 64 ASP A C 1 ATOM 490 O O . ASP A 1 66 ? -30.265 2.254 12.689 1.00 21.49 ? 64 ASP A O 1 ATOM 491 C CB . ASP A 1 66 ? -30.698 4.178 15.348 1.00 19.60 ? 64 ASP A CB 1 ATOM 492 C CG . ASP A 1 66 ? -31.833 4.539 14.408 1.00 29.65 ? 64 ASP A CG 1 ATOM 493 O OD1 . ASP A 1 66 ? -32.939 3.981 14.569 1.00 30.57 ? 64 ASP A OD1 1 ATOM 494 O OD2 . ASP A 1 66 ? -31.603 5.349 13.492 1.00 34.26 ? 64 ASP A OD2 1 ATOM 495 N N . GLY A 1 67 ? -28.514 3.602 13.222 1.00 18.42 ? 65 GLY A N 1 ATOM 496 C CA . GLY A 1 67 ? -27.932 3.714 11.891 1.00 18.41 ? 65 GLY A CA 1 ATOM 497 C C . GLY A 1 67 ? -27.508 2.363 11.350 1.00 21.83 ? 65 GLY A C 1 ATOM 498 O O . GLY A 1 67 ? -27.755 2.058 10.181 1.00 21.86 ? 65 GLY A O 1 ATOM 499 N N . LEU A 1 68 ? -26.901 1.530 12.210 1.00 17.80 ? 66 LEU A N 1 ATOM 500 C CA . LEU A 1 68 ? -26.461 0.192 11.827 1.00 17.23 ? 66 LEU A CA 1 ATOM 501 C C . LEU A 1 68 ? -27.647 -0.758 11.642 1.00 20.51 ? 66 LEU A C 1 ATOM 502 O O . LEU A 1 68 ? -27.866 -1.250 10.539 1.00 19.60 ? 66 LEU A O 1 ATOM 503 C CB . LEU A 1 68 ? -25.459 -0.381 12.856 1.00 17.16 ? 66 LEU A CB 1 ATOM 504 C CG . LEU A 1 68 ? -24.550 -1.533 12.384 1.00 21.66 ? 66 LEU A CG 1 ATOM 505 C CD1 . LEU A 1 68 ? -23.311 -1.602 13.220 1.00 21.91 ? 66 LEU A CD1 1 ATOM 506 C CD2 . LEU A 1 68 ? -25.255 -2.895 12.444 1.00 23.48 ? 66 LEU A CD2 1 ATOM 507 N N . LEU A 1 69 ? -28.395 -1.026 12.721 1.00 17.62 ? 67 LEU A N 1 ATOM 508 C CA . LEU A 1 69 ? -29.487 -1.999 12.713 1.00 17.62 ? 67 LEU A CA 1 ATOM 509 C C . LEU A 1 69 ? -30.780 -1.635 11.976 1.00 21.23 ? 67 LEU A C 1 ATOM 510 O O . LEU A 1 69 ? -31.561 -2.539 11.671 1.00 20.61 ? 67 LEU A O 1 ATOM 511 C CB . LEU A 1 69 ? -29.775 -2.520 14.135 1.00 17.80 ? 67 LEU A CB 1 ATOM 512 C CG . LEU A 1 69 ? -28.625 -3.234 14.865 1.00 22.49 ? 67 LEU A CG 1 ATOM 513 C CD1 . LEU A 1 69 ? -28.976 -3.468 16.299 1.00 22.58 ? 67 LEU A CD1 1 ATOM 514 C CD2 . LEU A 1 69 ? -28.268 -4.567 14.207 1.00 24.85 ? 67 LEU A CD2 1 ATOM 515 N N . THR A 1 70 ? -31.036 -0.339 11.707 1.00 17.68 ? 68 THR A N 1 ATOM 516 C CA . THR A 1 70 ? -32.291 0.054 11.041 1.00 17.36 ? 68 THR A CA 1 ATOM 517 C C . THR A 1 70 ? -32.112 0.899 9.775 1.00 20.58 ? 68 THR A C 1 ATOM 518 O O . THR A 1 70 ? -33.059 1.016 8.991 1.00 20.95 ? 68 THR A O 1 ATOM 519 C CB . THR A 1 70 ? -33.288 0.727 12.029 1.00 24.59 ? 68 THR A CB 1 ATOM 520 O OG1 . THR A 1 70 ? -32.896 2.076 12.284 1.00 25.62 ? 68 THR A OG1 1 ATOM 521 C CG2 . THR A 1 70 ? -33.465 -0.038 13.342 1.00 22.14 ? 68 THR A CG2 1 ATOM 522 N N . GLU A 1 71 ? -30.929 1.504 9.580 1.00 16.05 ? 69 GLU A N 1 ATOM 523 C CA . GLU A 1 71 ? -30.707 2.392 8.437 1.00 15.23 ? 69 GLU A CA 1 ATOM 524 C C . GLU A 1 71 ? -29.827 1.868 7.300 1.00 19.14 ? 69 GLU A C 1 ATOM 525 O O . GLU A 1 71 ? -30.357 1.532 6.240 1.00 18.13 ? 69 GLU A O 1 ATOM 526 C CB . GLU A 1 71 ? -30.250 3.790 8.886 1.00 16.31 ? 69 GLU A CB 1 ATOM 527 C CG . GLU A 1 71 ? -31.135 4.450 9.926 1.00 22.24 ? 69 GLU A CG 1 ATOM 528 C CD . GLU A 1 71 ? -30.785 5.907 10.131 1.00 29.09 ? 69 GLU A CD 1 ATOM 529 O OE1 . GLU A 1 71 ? -31.232 6.736 9.309 1.00 16.53 ? 69 GLU A OE1 1 ATOM 530 O OE2 . GLU A 1 71 ? -30.048 6.221 11.091 1.00 18.21 ? 69 GLU A OE2 1 ATOM 531 N N . HIS A 1 72 ? -28.489 1.855 7.490 1.00 16.32 ? 70 HIS A N 1 ATOM 532 C CA . HIS A 1 72 ? -27.542 1.472 6.439 1.00 16.45 ? 70 HIS A CA 1 ATOM 533 C C . HIS A 1 72 ? -26.422 0.504 6.840 1.00 20.46 ? 70 HIS A C 1 ATOM 534 O O . HIS A 1 72 ? -25.400 0.429 6.147 1.00 20.10 ? 70 HIS A O 1 ATOM 535 C CB . HIS A 1 72 ? -26.967 2.729 5.751 1.00 17.21 ? 70 HIS A CB 1 ATOM 536 C CG . HIS A 1 72 ? -26.398 3.755 6.687 1.00 20.43 ? 70 HIS A CG 1 ATOM 537 N ND1 . HIS A 1 72 ? -25.492 3.417 7.678 1.00 22.10 ? 70 HIS A ND1 1 ATOM 538 C CD2 . HIS A 1 72 ? -26.595 5.092 6.720 1.00 22.05 ? 70 HIS A CD2 1 ATOM 539 C CE1 . HIS A 1 72 ? -25.192 4.549 8.292 1.00 21.43 ? 70 HIS A CE1 1 ATOM 540 N NE2 . HIS A 1 72 ? -25.832 5.582 7.751 1.00 21.78 ? 70 HIS A NE2 1 ATOM 541 N N . GLY A 1 73 ? -26.626 -0.239 7.924 1.00 17.05 ? 71 GLY A N 1 ATOM 542 C CA . GLY A 1 73 ? -25.654 -1.221 8.394 1.00 17.06 ? 71 GLY A CA 1 ATOM 543 C C . GLY A 1 73 ? -25.600 -2.463 7.522 1.00 21.47 ? 71 GLY A C 1 ATOM 544 O O . GLY A 1 73 ? -26.454 -2.629 6.648 1.00 20.82 ? 71 GLY A O 1 ATOM 545 N N . PRO A 1 74 ? -24.609 -3.366 7.739 1.00 18.34 ? 72 PRO A N 1 ATOM 546 C CA . PRO A 1 74 ? -24.510 -4.580 6.897 1.00 18.38 ? 72 PRO A CA 1 ATOM 547 C C . PRO A 1 74 ? -25.668 -5.563 7.014 1.00 22.11 ? 72 PRO A C 1 ATOM 548 O O . PRO A 1 74 ? -25.940 -6.322 6.080 1.00 21.59 ? 72 PRO A O 1 ATOM 549 C CB . PRO A 1 74 ? -23.184 -5.203 7.328 1.00 20.14 ? 72 PRO A CB 1 ATOM 550 C CG . PRO A 1 74 ? -22.951 -4.686 8.703 1.00 24.53 ? 72 PRO A CG 1 ATOM 551 C CD . PRO A 1 74 ? -23.513 -3.306 8.727 1.00 20.00 ? 72 PRO A CD 1 ATOM 552 N N . PHE A 1 75 ? -26.339 -5.546 8.166 1.00 18.44 ? 73 PHE A N 1 ATOM 553 C CA . PHE A 1 75 ? -27.489 -6.378 8.491 1.00 18.16 ? 73 PHE A CA 1 ATOM 554 C C . PHE A 1 75 ? -28.492 -5.539 9.266 1.00 21.61 ? 73 PHE A C 1 ATOM 555 O O . PHE A 1 75 ? -28.098 -4.671 10.055 1.00 20.87 ? 73 PHE A O 1 ATOM 556 C CB . PHE A 1 75 ? -27.080 -7.635 9.290 1.00 19.97 ? 73 PHE A CB 1 ATOM 557 C CG . PHE A 1 75 ? -25.807 -7.486 10.089 1.00 21.51 ? 73 PHE A CG 1 ATOM 558 C CD1 . PHE A 1 75 ? -25.789 -6.751 11.270 1.00 24.53 ? 73 PHE A CD1 1 ATOM 559 C CD2 . PHE A 1 75 ? -24.619 -8.053 9.645 1.00 23.48 ? 73 PHE A CD2 1 ATOM 560 C CE1 . PHE A 1 75 ? -24.604 -6.584 11.988 1.00 25.25 ? 73 PHE A CE1 1 ATOM 561 C CE2 . PHE A 1 75 ? -23.438 -7.900 10.374 1.00 26.26 ? 73 PHE A CE2 1 ATOM 562 C CZ . PHE A 1 75 ? -23.438 -7.162 11.536 1.00 24.26 ? 73 PHE A CZ 1 ATOM 563 N N . LEU A 1 76 ? -29.786 -5.772 9.015 1.00 17.72 ? 74 LEU A N 1 ATOM 564 C CA . LEU A 1 76 ? -30.861 -5.026 9.663 1.00 17.46 ? 74 LEU A CA 1 ATOM 565 C C . LEU A 1 76 ? -31.712 -5.919 10.542 1.00 21.55 ? 74 LEU A C 1 ATOM 566 O O . LEU A 1 76 ? -32.021 -7.051 10.157 1.00 20.99 ? 74 LEU A O 1 ATOM 567 C CB . LEU A 1 76 ? -31.740 -4.288 8.632 1.00 17.30 ? 74 LEU A CB 1 ATOM 568 C CG . LEU A 1 76 ? -31.034 -3.343 7.643 1.00 21.93 ? 74 LEU A CG 1 ATOM 569 C CD1 . LEU A 1 76 ? -31.976 -2.926 6.531 1.00 22.19 ? 74 LEU A CD1 1 ATOM 570 C CD2 . LEU A 1 76 ? -30.457 -2.107 8.340 1.00 23.43 ? 74 LEU A CD2 1 ATOM 571 N N . VAL A 1 77 ? -32.097 -5.402 11.724 1.00 17.97 ? 75 VAL A N 1 ATOM 572 C CA . VAL A 1 77 ? -32.932 -6.122 12.684 1.00 17.91 ? 75 VAL A CA 1 ATOM 573 C C . VAL A 1 77 ? -34.363 -6.283 12.160 1.00 23.02 ? 75 VAL A C 1 ATOM 574 O O . VAL A 1 77 ? -34.940 -5.334 11.622 1.00 22.60 ? 75 VAL A O 1 ATOM 575 C CB . VAL A 1 77 ? -32.836 -5.556 14.134 1.00 21.68 ? 75 VAL A CB 1 ATOM 576 C CG1 . VAL A 1 77 ? -33.445 -4.156 14.256 1.00 21.40 ? 75 VAL A CG1 1 ATOM 577 C CG2 . VAL A 1 77 ? -33.446 -6.514 15.155 1.00 21.50 ? 75 VAL A CG2 1 ATOM 578 N N . GLN A 1 78 ? -34.899 -7.505 12.269 1.00 20.08 ? 76 GLN A N 1 ATOM 579 C CA . GLN A 1 78 ? -36.246 -7.848 11.820 1.00 19.99 ? 76 GLN A CA 1 ATOM 580 C C . GLN A 1 78 ? -37.284 -7.576 12.920 1.00 24.68 ? 76 GLN A C 1 ATOM 581 O O . GLN A 1 78 ? -36.886 -7.473 14.085 1.00 24.21 ? 76 GLN A O 1 ATOM 582 C CB . GLN A 1 78 ? -36.294 -9.312 11.339 1.00 21.13 ? 76 GLN A CB 1 ATOM 583 C CG . GLN A 1 78 ? -35.421 -9.590 10.110 1.00 27.58 ? 76 GLN A CG 1 ATOM 584 C CD . GLN A 1 78 ? -35.686 -8.655 8.948 1.00 37.87 ? 76 GLN A CD 1 ATOM 585 O OE1 . GLN A 1 78 ? -36.717 -8.733 8.278 1.00 30.21 ? 76 GLN A OE1 1 ATOM 586 N NE2 . GLN A 1 78 ? -34.747 -7.759 8.676 1.00 29.69 ? 76 GLN A NE2 1 ATOM 587 N N . PRO A 1 79 ? -38.605 -7.460 12.595 1.00 22.08 ? 77 PRO A N 1 ATOM 588 C CA . PRO A 1 79 ? -39.607 -7.179 13.646 1.00 22.10 ? 77 PRO A CA 1 ATOM 589 C C . PRO A 1 79 ? -39.651 -8.122 14.853 1.00 26.03 ? 77 PRO A C 1 ATOM 590 O O . PRO A 1 79 ? -40.152 -7.717 15.898 1.00 25.57 ? 77 PRO A O 1 ATOM 591 C CB . PRO A 1 79 ? -40.932 -7.162 12.879 1.00 23.89 ? 77 PRO A CB 1 ATOM 592 C CG . PRO A 1 79 ? -40.551 -6.807 11.487 1.00 28.15 ? 77 PRO A CG 1 ATOM 593 C CD . PRO A 1 79 ? -39.248 -7.510 11.264 1.00 23.66 ? 77 PRO A CD 1 ATOM 594 N N . ASP A 1 80 ? -39.111 -9.352 14.736 1.00 22.51 ? 78 ASP A N 1 ATOM 595 C CA . ASP A 1 80 ? -39.076 -10.300 15.857 1.00 22.06 ? 78 ASP A CA 1 ATOM 596 C C . ASP A 1 80 ? -38.064 -9.898 16.947 1.00 26.31 ? 78 ASP A C 1 ATOM 597 O O . ASP A 1 80 ? -38.151 -10.387 18.078 1.00 26.08 ? 78 ASP A O 1 ATOM 598 C CB . ASP A 1 80 ? -38.828 -11.745 15.370 1.00 23.70 ? 78 ASP A CB 1 ATOM 599 C CG . ASP A 1 80 ? -37.568 -11.997 14.549 1.00 31.38 ? 78 ASP A CG 1 ATOM 600 O OD1 . ASP A 1 80 ? -36.757 -11.056 14.387 1.00 31.56 ? 78 ASP A OD1 1 ATOM 601 O OD2 . ASP A 1 80 ? -37.397 -13.133 14.065 1.00 35.96 ? 78 ASP A OD2 1 ATOM 602 N N . GLY A 1 81 ? -37.123 -9.020 16.586 1.00 22.73 ? 79 GLY A N 1 ATOM 603 C CA . GLY A 1 81 ? -36.067 -8.533 17.469 1.00 22.22 ? 79 GLY A CA 1 ATOM 604 C C . GLY A 1 81 ? -35.037 -9.591 17.803 1.00 25.42 ? 79 GLY A C 1 ATOM 605 O O . GLY A 1 81 ? -34.350 -9.488 18.819 1.00 24.78 ? 79 GLY A O 1 ATOM 606 N N . VAL A 1 82 ? -34.943 -10.632 16.954 1.00 22.29 ? 80 VAL A N 1 ATOM 607 C CA . VAL A 1 82 ? -34.030 -11.769 17.105 1.00 22.07 ? 80 VAL A CA 1 ATOM 608 C C . VAL A 1 82 ? -33.215 -11.947 15.808 1.00 25.19 ? 80 VAL A C 1 ATOM 609 O O . VAL A 1 82 ? -31.993 -12.071 15.865 1.00 24.84 ? 80 VAL A O 1 ATOM 610 C CB . VAL A 1 82 ? -34.797 -13.076 17.494 1.00 26.34 ? 80 VAL A CB 1 ATOM 611 C CG1 . VAL A 1 82 ? -33.851 -14.273 17.611 1.00 26.32 ? 80 VAL A CG1 1 ATOM 612 C CG2 . VAL A 1 82 ? -35.594 -12.904 18.787 1.00 26.16 ? 80 VAL A CG2 1 ATOM 613 N N . THR A 1 83 ? -33.900 -11.958 14.653 1.00 21.28 ? 81 THR A N 1 ATOM 614 C CA . THR A 1 83 ? -33.316 -12.177 13.330 1.00 20.85 ? 81 THR A CA 1 ATOM 615 C C . THR A 1 83 ? -32.670 -10.925 12.737 1.00 24.35 ? 81 THR A C 1 ATOM 616 O O . THR A 1 83 ? -33.235 -9.832 12.811 1.00 23.56 ? 81 THR A O 1 ATOM 617 C CB . THR A 1 83 ? -34.377 -12.782 12.379 1.00 27.00 ? 81 THR A CB 1 ATOM 618 O OG1 . THR A 1 83 ? -35.057 -13.851 13.036 1.00 27.26 ? 81 THR A OG1 1 ATOM 619 C CG2 . THR A 1 83 ? -33.788 -13.294 11.067 1.00 24.69 ? 81 THR A CG2 1 ATOM 620 N N . LEU A 1 84 ? -31.488 -11.107 12.129 1.00 20.91 ? 82 LEU A N 1 ATOM 621 C CA . LEU A 1 84 ? -30.763 -10.072 11.401 1.00 20.71 ? 82 LEU A CA 1 ATOM 622 C C . LEU A 1 84 ? -30.690 -10.530 9.953 1.00 24.49 ? 82 LEU A C 1 ATOM 623 O O . LEU A 1 84 ? -30.333 -11.682 9.696 1.00 24.14 ? 82 LEU A O 1 ATOM 624 C CB . LEU A 1 84 ? -29.331 -9.871 11.934 1.00 20.77 ? 82 LEU A CB 1 ATOM 625 C CG . LEU A 1 84 ? -29.118 -9.347 13.356 1.00 25.45 ? 82 LEU A CG 1 ATOM 626 C CD1 . LEU A 1 84 ? -27.649 -9.155 13.607 1.00 25.54 ? 82 LEU A CD1 1 ATOM 627 C CD2 . LEU A 1 84 ? -29.815 -8.012 13.586 1.00 27.96 ? 82 LEU A CD2 1 ATOM 628 N N . GLU A 1 85 ? -31.038 -9.649 9.011 1.00 20.59 ? 83 GLU A N 1 ATOM 629 C CA . GLU A 1 85 ? -30.979 -9.979 7.588 1.00 20.32 ? 83 GLU A CA 1 ATOM 630 C C . GLU A 1 85 ? -29.990 -9.058 6.904 1.00 23.17 ? 83 GLU A C 1 ATOM 631 O O . GLU A 1 85 ? -29.997 -7.856 7.176 1.00 22.68 ? 83 GLU A O 1 ATOM 632 C CB . GLU A 1 85 ? -32.363 -9.874 6.919 1.00 21.84 ? 83 GLU A CB 1 ATOM 633 C CG . GLU A 1 85 ? -33.384 -10.901 7.390 1.00 33.00 ? 83 GLU A CG 1 ATOM 634 C CD . GLU A 1 85 ? -33.200 -12.356 6.998 1.00 58.20 ? 83 GLU A CD 1 ATOM 635 O OE1 . GLU A 1 85 ? -32.464 -12.637 6.024 1.00 53.08 ? 83 GLU A OE1 1 ATOM 636 O OE2 . GLU A 1 85 ? -33.834 -13.219 7.646 1.00 56.01 ? 83 GLU A OE2 1 ATOM 637 N N . TYR A 1 86 ? -29.136 -9.616 6.023 1.00 18.93 ? 84 TYR A N 1 ATOM 638 C CA . TYR A 1 86 ? -28.133 -8.859 5.274 1.00 18.40 ? 84 TYR A CA 1 ATOM 639 C C . TYR A 1 86 ? -28.752 -7.754 4.432 1.00 22.01 ? 84 TYR A C 1 ATOM 640 O O . TYR A 1 86 ? -29.804 -7.950 3.820 1.00 21.67 ? 84 TYR A O 1 ATOM 641 C CB . TYR A 1 86 ? -27.239 -9.784 4.431 1.00 19.52 ? 84 TYR A CB 1 ATOM 642 C CG . TYR A 1 86 ? -26.168 -10.462 5.256 1.00 20.96 ? 84 TYR A CG 1 ATOM 643 C CD1 . TYR A 1 86 ? -24.938 -9.849 5.477 1.00 21.59 ? 84 TYR A CD1 1 ATOM 644 C CD2 . TYR A 1 86 ? -26.402 -11.693 5.862 1.00 22.88 ? 84 TYR A CD2 1 ATOM 645 C CE1 . TYR A 1 86 ? -23.958 -10.455 6.263 1.00 22.34 ? 84 TYR A CE1 1 ATOM 646 C CE2 . TYR A 1 86 ? -25.427 -12.312 6.643 1.00 23.42 ? 84 TYR A CE2 1 ATOM 647 C CZ . TYR A 1 86 ? -24.208 -11.687 6.842 1.00 28.90 ? 84 TYR A CZ 1 ATOM 648 O OH . TYR A 1 86 ? -23.250 -12.286 7.619 1.00 28.38 ? 84 TYR A OH 1 ATOM 649 N N . ASN A 1 87 ? -28.125 -6.577 4.461 1.00 18.14 ? 85 ASN A N 1 ATOM 650 C CA . ASN A 1 87 ? -28.582 -5.395 3.749 1.00 17.76 ? 85 ASN A CA 1 ATOM 651 C C . ASN A 1 87 ? -27.848 -5.254 2.409 1.00 21.19 ? 85 ASN A C 1 ATOM 652 O O . ASN A 1 87 ? -26.643 -4.994 2.401 1.00 20.86 ? 85 ASN A O 1 ATOM 653 C CB . ASN A 1 87 ? -28.415 -4.149 4.638 1.00 16.80 ? 85 ASN A CB 1 ATOM 654 C CG . ASN A 1 87 ? -28.816 -2.823 4.029 1.00 27.01 ? 85 ASN A CG 1 ATOM 655 O OD1 . ASN A 1 87 ? -29.507 -2.742 3.007 1.00 17.06 ? 85 ASN A OD1 1 ATOM 656 N ND2 . ASN A 1 87 ? -28.401 -1.740 4.671 1.00 16.64 ? 85 ASN A ND2 1 ATOM 657 N N . PRO A 1 88 ? -28.559 -5.399 1.264 1.00 17.76 ? 86 PRO A N 1 ATOM 658 C CA . PRO A 1 88 ? -27.881 -5.264 -0.041 1.00 17.77 ? 86 PRO A CA 1 ATOM 659 C C . PRO A 1 88 ? -27.514 -3.824 -0.418 1.00 21.56 ? 86 PRO A C 1 ATOM 660 O O . PRO A 1 88 ? -26.862 -3.613 -1.442 1.00 20.84 ? 86 PRO A O 1 ATOM 661 C CB . PRO A 1 88 ? -28.875 -5.889 -1.026 1.00 19.47 ? 86 PRO A CB 1 ATOM 662 C CG . PRO A 1 88 ? -30.201 -5.706 -0.388 1.00 23.76 ? 86 PRO A CG 1 ATOM 663 C CD . PRO A 1 88 ? -29.993 -5.719 1.100 1.00 19.21 ? 86 PRO A CD 1 ATOM 664 N N . TYR A 1 89 ? -27.925 -2.838 0.405 1.00 18.20 ? 87 TYR A N 1 ATOM 665 C CA . TYR A 1 89 ? -27.638 -1.418 0.176 1.00 18.14 ? 87 TYR A CA 1 ATOM 666 C C . TYR A 1 89 ? -26.790 -0.828 1.309 1.00 21.32 ? 87 TYR A C 1 ATOM 667 O O . TYR A 1 89 ? -26.720 0.395 1.468 1.00 20.90 ? 87 TYR A O 1 ATOM 668 C CB . TYR A 1 89 ? -28.939 -0.623 -0.042 1.00 19.78 ? 87 TYR A CB 1 ATOM 669 C CG . TYR A 1 89 ? -29.884 -1.275 -1.029 1.00 22.02 ? 87 TYR A CG 1 ATOM 670 C CD1 . TYR A 1 89 ? -29.622 -1.250 -2.396 1.00 24.05 ? 87 TYR A CD1 1 ATOM 671 C CD2 . TYR A 1 89 ? -31.033 -1.929 -0.595 1.00 23.02 ? 87 TYR A CD2 1 ATOM 672 C CE1 . TYR A 1 89 ? -30.477 -1.866 -3.307 1.00 25.21 ? 87 TYR A CE1 1 ATOM 673 C CE2 . TYR A 1 89 ? -31.901 -2.539 -1.498 1.00 24.13 ? 87 TYR A CE2 1 ATOM 674 C CZ . TYR A 1 89 ? -31.621 -2.503 -2.854 1.00 32.26 ? 87 TYR A CZ 1 ATOM 675 O OH . TYR A 1 89 ? -32.472 -3.103 -3.750 1.00 35.07 ? 87 TYR A OH 1 ATOM 676 N N . SER A 1 90 ? -26.127 -1.711 2.075 1.00 17.43 ? 88 SER A N 1 ATOM 677 C CA . SER A 1 90 ? -25.254 -1.364 3.195 1.00 17.02 ? 88 SER A CA 1 ATOM 678 C C . SER A 1 90 ? -24.143 -0.416 2.773 1.00 20.63 ? 88 SER A C 1 ATOM 679 O O . SER A 1 90 ? -23.533 -0.600 1.717 1.00 20.35 ? 88 SER A O 1 ATOM 680 C CB . SER A 1 90 ? -24.642 -2.622 3.798 1.00 20.07 ? 88 SER A CB 1 ATOM 681 O OG . SER A 1 90 ? -23.748 -2.288 4.847 1.00 27.10 ? 88 SER A OG 1 ATOM 682 N N . TRP A 1 91 ? -23.870 0.588 3.613 1.00 17.02 ? 89 TRP A N 1 ATOM 683 C CA . TRP A 1 91 ? -22.814 1.561 3.350 1.00 16.54 ? 89 TRP A CA 1 ATOM 684 C C . TRP A 1 91 ? -21.417 0.931 3.513 1.00 20.19 ? 89 TRP A C 1 ATOM 685 O O . TRP A 1 91 ? -20.454 1.439 2.939 1.00 19.44 ? 89 TRP A O 1 ATOM 686 C CB . TRP A 1 91 ? -23.017 2.840 4.187 1.00 15.07 ? 89 TRP A CB 1 ATOM 687 C CG . TRP A 1 91 ? -24.123 3.741 3.689 1.00 15.92 ? 89 TRP A CG 1 ATOM 688 C CD1 . TRP A 1 91 ? -25.112 3.422 2.801 1.00 18.83 ? 89 TRP A CD1 1 ATOM 689 C CD2 . TRP A 1 91 ? -24.346 5.110 4.059 1.00 15.69 ? 89 TRP A CD2 1 ATOM 690 N NE1 . TRP A 1 91 ? -25.941 4.503 2.604 1.00 18.24 ? 89 TRP A NE1 1 ATOM 691 C CE2 . TRP A 1 91 ? -25.490 5.554 3.358 1.00 19.52 ? 89 TRP A CE2 1 ATOM 692 C CE3 . TRP A 1 91 ? -23.700 6.003 4.933 1.00 16.86 ? 89 TRP A CE3 1 ATOM 693 C CZ2 . TRP A 1 91 ? -25.999 6.851 3.499 1.00 18.70 ? 89 TRP A CZ2 1 ATOM 694 C CZ3 . TRP A 1 91 ? -24.194 7.294 5.056 1.00 18.11 ? 89 TRP A CZ3 1 ATOM 695 C CH2 . TRP A 1 91 ? -25.334 7.704 4.351 1.00 18.72 ? 89 TRP A CH2 1 ATOM 696 N N . ASN A 1 92 ? -21.331 -0.226 4.216 1.00 17.05 ? 90 ASN A N 1 ATOM 697 C CA . ASN A 1 92 ? -20.080 -0.971 4.401 1.00 17.02 ? 90 ASN A CA 1 ATOM 698 C C . ASN A 1 92 ? -19.662 -1.816 3.172 1.00 21.78 ? 90 ASN A C 1 ATOM 699 O O . ASN A 1 92 ? -18.636 -2.491 3.219 1.00 21.38 ? 90 ASN A O 1 ATOM 700 C CB . ASN A 1 92 ? -20.066 -1.774 5.721 1.00 15.83 ? 90 ASN A CB 1 ATOM 701 C CG . ASN A 1 92 ? -20.446 -3.235 5.619 1.00 30.89 ? 90 ASN A CG 1 ATOM 702 O OD1 . ASN A 1 92 ? -21.444 -3.609 4.999 1.00 24.45 ? 90 ASN A OD1 1 ATOM 703 N ND2 . ASN A 1 92 ? -19.651 -4.095 6.237 1.00 22.08 ? 90 ASN A ND2 1 ATOM 704 N N . LEU A 1 93 ? -20.448 -1.774 2.077 1.00 18.92 ? 91 LEU A N 1 ATOM 705 C CA . LEU A 1 93 ? -20.118 -2.485 0.837 1.00 18.87 ? 91 LEU A CA 1 ATOM 706 C C . LEU A 1 93 ? -18.899 -1.842 0.170 1.00 22.26 ? 91 LEU A C 1 ATOM 707 O O . LEU A 1 93 ? -18.156 -2.521 -0.539 1.00 21.81 ? 91 LEU A O 1 ATOM 708 C CB . LEU A 1 93 ? -21.299 -2.436 -0.150 1.00 19.06 ? 91 LEU A CB 1 ATOM 709 C CG . LEU A 1 93 ? -22.439 -3.427 0.057 1.00 23.87 ? 91 LEU A CG 1 ATOM 710 C CD1 . LEU A 1 93 ? -23.670 -2.968 -0.678 1.00 24.27 ? 91 LEU A CD1 1 ATOM 711 C CD2 . LEU A 1 93 ? -22.061 -4.822 -0.422 1.00 26.43 ? 91 LEU A CD2 1 ATOM 712 N N . ILE A 1 94 ? -18.713 -0.526 0.389 1.00 18.80 ? 92 ILE A N 1 ATOM 713 C CA . ILE A 1 94 ? -17.646 0.287 -0.209 1.00 18.78 ? 92 ILE A CA 1 ATOM 714 C C . ILE A 1 94 ? -16.857 1.133 0.821 1.00 22.26 ? 92 ILE A C 1 ATOM 715 O O . ILE A 1 94 ? -16.050 1.978 0.422 1.00 21.57 ? 92 ILE A O 1 ATOM 716 C CB . ILE A 1 94 ? -18.235 1.170 -1.354 1.00 22.07 ? 92 ILE A CB 1 ATOM 717 C CG1 . ILE A 1 94 ? -19.427 2.023 -0.848 1.00 22.65 ? 92 ILE A CG1 1 ATOM 718 C CG2 . ILE A 1 94 ? -18.623 0.319 -2.581 1.00 22.75 ? 92 ILE A CG2 1 ATOM 719 C CD1 . ILE A 1 94 ? -19.604 3.335 -1.525 1.00 28.75 ? 92 ILE A CD1 1 ATOM 720 N N . ALA A 1 95 ? -17.091 0.919 2.132 1.00 18.88 ? 93 ALA A N 1 ATOM 721 C CA . ALA A 1 95 ? -16.414 1.687 3.185 1.00 18.79 ? 93 ALA A CA 1 ATOM 722 C C . ALA A 1 95 ? -16.302 0.952 4.518 1.00 22.11 ? 93 ALA A C 1 ATOM 723 O O . ALA A 1 95 ? -17.110 0.075 4.817 1.00 21.75 ? 93 ALA A O 1 ATOM 724 C CB . ALA A 1 95 ? -17.128 3.019 3.397 1.00 19.54 ? 93 ALA A CB 1 ATOM 725 N N . ASN A 1 96 ? -15.297 1.329 5.323 1.00 18.20 ? 94 ASN A N 1 ATOM 726 C CA . ASN A 1 96 ? -15.088 0.814 6.672 1.00 17.61 ? 94 ASN A CA 1 ATOM 727 C C . ASN A 1 96 ? -15.905 1.774 7.548 1.00 21.25 ? 94 ASN A C 1 ATOM 728 O O . ASN A 1 96 ? -15.523 2.937 7.706 1.00 20.79 ? 94 ASN A O 1 ATOM 729 C CB . ASN A 1 96 ? -13.592 0.839 7.031 1.00 16.91 ? 94 ASN A CB 1 ATOM 730 C CG . ASN A 1 96 ? -12.717 0.030 6.103 1.00 28.96 ? 94 ASN A CG 1 ATOM 731 O OD1 . ASN A 1 96 ? -12.758 -1.203 6.082 1.00 20.63 ? 94 ASN A OD1 1 ATOM 732 N ND2 . ASN A 1 96 ? -11.889 0.709 5.327 1.00 19.66 ? 94 ASN A ND2 1 ATOM 733 N N . VAL A 1 97 ? -17.083 1.325 8.015 1.00 17.79 ? 95 VAL A N 1 ATOM 734 C CA . VAL A 1 97 ? -18.017 2.177 8.760 1.00 17.35 ? 95 VAL A CA 1 ATOM 735 C C . VAL A 1 97 ? -17.934 2.054 10.283 1.00 20.52 ? 95 VAL A C 1 ATOM 736 O O . VAL A 1 97 ? -18.169 0.982 10.848 1.00 19.75 ? 95 VAL A O 1 ATOM 737 C CB . VAL A 1 97 ? -19.477 2.134 8.217 1.00 21.13 ? 95 VAL A CB 1 ATOM 738 C CG1 . VAL A 1 97 ? -20.290 3.325 8.726 1.00 20.86 ? 95 VAL A CG1 1 ATOM 739 C CG2 . VAL A 1 97 ? -19.499 2.103 6.690 1.00 20.94 ? 95 VAL A CG2 1 ATOM 740 N N . LEU A 1 98 ? -17.624 3.183 10.932 1.00 16.57 ? 96 LEU A N 1 ATOM 741 C CA . LEU A 1 98 ? -17.497 3.307 12.378 1.00 16.21 ? 96 LEU A CA 1 ATOM 742 C C . LEU A 1 98 ? -18.757 3.946 12.978 1.00 19.16 ? 96 LEU A C 1 ATOM 743 O O . LEU A 1 98 ? -18.983 5.150 12.828 1.00 18.96 ? 96 LEU A O 1 ATOM 744 C CB . LEU A 1 98 ? -16.221 4.113 12.723 1.00 16.21 ? 96 LEU A CB 1 ATOM 745 C CG . LEU A 1 98 ? -15.919 4.404 14.202 1.00 20.76 ? 96 LEU A CG 1 ATOM 746 C CD1 . LEU A 1 98 ? -15.600 3.133 14.972 1.00 20.68 ? 96 LEU A CD1 1 ATOM 747 C CD2 . LEU A 1 98 ? -14.768 5.380 14.330 1.00 23.03 ? 96 LEU A CD2 1 ATOM 748 N N . TYR A 1 99 ? -19.587 3.123 13.634 1.00 15.18 ? 97 TYR A N 1 ATOM 749 C CA . TYR A 1 99 ? -20.805 3.583 14.301 1.00 14.60 ? 97 TYR A CA 1 ATOM 750 C C . TYR A 1 99 ? -20.432 3.850 15.744 1.00 17.89 ? 97 TYR A C 1 ATOM 751 O O . TYR A 1 99 ? -20.003 2.931 16.442 1.00 17.40 ? 97 TYR A O 1 ATOM 752 C CB . TYR A 1 99 ? -21.924 2.536 14.208 1.00 15.28 ? 97 TYR A CB 1 ATOM 753 C CG . TYR A 1 99 ? -22.423 2.298 12.800 1.00 16.14 ? 97 TYR A CG 1 ATOM 754 C CD1 . TYR A 1 99 ? -21.821 1.350 11.977 1.00 17.99 ? 97 TYR A CD1 1 ATOM 755 C CD2 . TYR A 1 99 ? -23.515 2.999 12.299 1.00 16.36 ? 97 TYR A CD2 1 ATOM 756 C CE1 . TYR A 1 99 ? -22.303 1.096 10.694 1.00 18.28 ? 97 TYR A CE1 1 ATOM 757 C CE2 . TYR A 1 99 ? -23.983 2.779 11.006 1.00 17.02 ? 97 TYR A CE2 1 ATOM 758 C CZ . TYR A 1 99 ? -23.373 1.827 10.205 1.00 23.23 ? 97 TYR A CZ 1 ATOM 759 O OH . TYR A 1 99 ? -23.834 1.606 8.930 1.00 21.25 ? 97 TYR A OH 1 ATOM 760 N N . LEU A 1 100 ? -20.537 5.113 16.175 1.00 14.26 ? 98 LEU A N 1 ATOM 761 C CA . LEU A 1 100 ? -20.142 5.510 17.523 1.00 13.70 ? 98 LEU A CA 1 ATOM 762 C C . LEU A 1 100 ? -21.305 6.012 18.367 1.00 18.14 ? 98 LEU A C 1 ATOM 763 O O . LEU A 1 100 ? -21.929 7.018 18.025 1.00 18.05 ? 98 LEU A O 1 ATOM 764 C CB . LEU A 1 100 ? -19.009 6.557 17.452 1.00 13.44 ? 98 LEU A CB 1 ATOM 765 C CG . LEU A 1 100 ? -18.353 6.990 18.768 1.00 17.33 ? 98 LEU A CG 1 ATOM 766 C CD1 . LEU A 1 100 ? -17.491 5.884 19.352 1.00 16.98 ? 98 LEU A CD1 1 ATOM 767 C CD2 . LEU A 1 100 ? -17.524 8.244 18.566 1.00 19.38 ? 98 LEU A CD2 1 ATOM 768 N N . GLU A 1 101 ? -21.578 5.320 19.486 1.00 15.04 ? 99 GLU A N 1 ATOM 769 C CA . GLU A 1 101 ? -22.631 5.709 20.425 1.00 14.70 ? 99 GLU A CA 1 ATOM 770 C C . GLU A 1 101 ? -22.063 6.880 21.212 1.00 19.02 ? 99 GLU A C 1 ATOM 771 O O . GLU A 1 101 ? -21.102 6.715 21.966 1.00 18.71 ? 99 GLU A O 1 ATOM 772 C CB . GLU A 1 101 ? -23.019 4.546 21.346 1.00 15.81 ? 99 GLU A CB 1 ATOM 773 C CG . GLU A 1 101 ? -23.638 3.359 20.630 1.00 23.89 ? 99 GLU A CG 1 ATOM 774 C CD . GLU A 1 101 ? -24.371 2.416 21.561 1.00 31.78 ? 99 GLU A CD 1 ATOM 775 O OE1 . GLU A 1 101 ? -23.705 1.744 22.378 1.00 20.55 ? 99 GLU A OE1 1 ATOM 776 O OE2 . GLU A 1 101 ? -25.618 2.361 21.483 1.00 22.48 ? 99 GLU A OE2 1 ATOM 777 N N . SER A 1 102 ? -22.584 8.084 20.941 1.00 15.74 ? 100 SER A N 1 ATOM 778 C CA . SER A 1 102 ? -22.075 9.323 21.517 1.00 15.23 ? 100 SER A CA 1 ATOM 779 C C . SER A 1 102 ? -23.189 10.355 21.777 1.00 19.46 ? 100 SER A C 1 ATOM 780 O O . SER A 1 102 ? -24.136 10.414 20.989 1.00 18.74 ? 100 SER A O 1 ATOM 781 C CB . SER A 1 102 ? -21.018 9.912 20.587 1.00 17.86 ? 100 SER A CB 1 ATOM 782 O OG . SER A 1 102 ? -20.576 11.193 21.000 1.00 24.26 ? 100 SER A OG 1 ATOM 783 N N . PRO A 1 103 ? -23.102 11.200 22.841 1.00 16.94 ? 101 PRO A N 1 ATOM 784 C CA . PRO A 1 103 ? -22.049 11.280 23.877 1.00 16.89 ? 101 PRO A CA 1 ATOM 785 C C . PRO A 1 103 ? -22.113 10.162 24.926 1.00 21.41 ? 101 PRO A C 1 ATOM 786 O O . PRO A 1 103 ? -22.823 9.178 24.717 1.00 21.05 ? 101 PRO A O 1 ATOM 787 C CB . PRO A 1 103 ? -22.242 12.692 24.442 1.00 18.59 ? 101 PRO A CB 1 ATOM 788 C CG . PRO A 1 103 ? -23.717 12.932 24.327 1.00 23.00 ? 101 PRO A CG 1 ATOM 789 C CD . PRO A 1 103 ? -24.159 12.208 23.074 1.00 18.55 ? 101 PRO A CD 1 ATOM 790 N N . ALA A 1 104 ? -21.349 10.286 26.033 1.00 18.20 ? 102 ALA A N 1 ATOM 791 C CA . ALA A 1 104 ? -21.339 9.288 27.108 1.00 18.18 ? 102 ALA A CA 1 ATOM 792 C C . ALA A 1 104 ? -22.738 9.137 27.714 1.00 21.86 ? 102 ALA A C 1 ATOM 793 O O . ALA A 1 104 ? -23.458 10.127 27.863 1.00 21.41 ? 102 ALA A O 1 ATOM 794 C CB . ALA A 1 104 ? -20.337 9.676 28.182 1.00 18.88 ? 102 ALA A CB 1 ATOM 795 N N . GLY A 1 105 ? -23.117 7.898 28.010 1.00 18.17 ? 103 GLY A N 1 ATOM 796 C CA . GLY A 1 105 ? -24.431 7.578 28.555 1.00 17.94 ? 103 GLY A CA 1 ATOM 797 C C . GLY A 1 105 ? -25.413 7.108 27.499 1.00 21.36 ? 103 GLY A C 1 ATOM 798 O O . GLY A 1 105 ? -26.476 6.587 27.838 1.00 21.02 ? 103 GLY A O 1 ATOM 799 N N . VAL A 1 106 ? -25.063 7.288 26.211 1.00 17.36 ? 104 VAL A N 1 ATOM 800 C CA . VAL A 1 106 ? -25.891 6.890 25.072 1.00 16.97 ? 104 VAL A CA 1 ATOM 801 C C . VAL A 1 106 ? -25.666 5.413 24.755 1.00 20.66 ? 104 VAL A C 1 ATOM 802 O O . VAL A 1 106 ? -24.547 5.011 24.426 1.00 20.02 ? 104 VAL A O 1 ATOM 803 C CB . VAL A 1 106 ? -25.666 7.812 23.844 1.00 20.72 ? 104 VAL A CB 1 ATOM 804 C CG1 . VAL A 1 106 ? -26.369 7.277 22.604 1.00 20.48 ? 104 VAL A CG1 1 ATOM 805 C CG2 . VAL A 1 106 ? -26.122 9.235 24.141 1.00 20.46 ? 104 VAL A CG2 1 ATOM 806 N N . GLY A 1 107 ? -26.740 4.631 24.853 1.00 17.05 ? 105 GLY A N 1 ATOM 807 C CA . GLY A 1 107 ? -26.718 3.197 24.598 1.00 16.73 ? 105 GLY A CA 1 ATOM 808 C C . GLY A 1 107 ? -25.809 2.457 25.556 1.00 20.21 ? 105 GLY A C 1 ATOM 809 O O . GLY A 1 107 ? -26.066 2.439 26.764 1.00 19.46 ? 105 GLY A O 1 ATOM 810 N N . PHE A 1 108 ? -24.716 1.879 25.023 1.00 17.02 ? 106 PHE A N 1 ATOM 811 C CA . PHE A 1 108 ? -23.720 1.163 25.822 1.00 17.02 ? 106 PHE A CA 1 ATOM 812 C C . PHE A 1 108 ? -22.545 2.044 26.267 1.00 21.26 ? 106 PHE A C 1 ATOM 813 O O . PHE A 1 108 ? -21.717 1.596 27.061 1.00 21.08 ? 106 PHE A O 1 ATOM 814 C CB . PHE A 1 108 ? -23.254 -0.132 25.130 1.00 18.84 ? 106 PHE A CB 1 ATOM 815 C CG . PHE A 1 108 ? -24.320 -1.194 24.975 1.00 20.41 ? 106 PHE A CG 1 ATOM 816 C CD1 . PHE A 1 108 ? -25.044 -1.645 26.074 1.00 23.66 ? 106 PHE A CD1 1 ATOM 817 C CD2 . PHE A 1 108 ? -24.576 -1.769 23.737 1.00 22.57 ? 106 PHE A CD2 1 ATOM 818 C CE1 . PHE A 1 108 ? -26.009 -2.646 25.934 1.00 24.59 ? 106 PHE A CE1 1 ATOM 819 C CE2 . PHE A 1 108 ? -25.542 -2.770 23.598 1.00 25.31 ? 106 PHE A CE2 1 ATOM 820 C CZ . PHE A 1 108 ? -26.251 -3.202 24.696 1.00 23.54 ? 106 PHE A CZ 1 ATOM 821 N N . SER A 1 109 ? -22.488 3.306 25.785 1.00 17.85 ? 107 SER A N 1 ATOM 822 C CA . SER A 1 109 ? -21.454 4.263 26.186 1.00 17.51 ? 107 SER A CA 1 ATOM 823 C C . SER A 1 109 ? -21.708 4.697 27.625 1.00 21.95 ? 107 SER A C 1 ATOM 824 O O . SER A 1 109 ? -22.858 4.708 28.071 1.00 21.13 ? 107 SER A O 1 ATOM 825 C CB . SER A 1 109 ? -21.440 5.474 25.263 1.00 20.53 ? 107 SER A CB 1 ATOM 826 O OG . SER A 1 109 ? -21.098 5.082 23.947 1.00 25.69 ? 107 SER A OG 1 ATOM 827 N N . TYR A 1 110 ? -20.634 5.007 28.364 1.00 19.44 ? 108 TYR A N 1 ATOM 828 C CA . TYR A 1 110 ? -20.727 5.376 29.775 1.00 19.53 ? 108 TYR A CA 1 ATOM 829 C C . TYR A 1 110 ? -19.530 6.210 30.226 1.00 23.88 ? 108 TYR A C 1 ATOM 830 O O . TYR A 1 110 ? -18.568 6.391 29.476 1.00 22.94 ? 108 TYR A O 1 ATOM 831 C CB . TYR A 1 110 ? -20.834 4.091 30.645 1.00 20.60 ? 108 TYR A CB 1 ATOM 832 C CG . TYR A 1 110 ? -19.548 3.289 30.733 1.00 22.02 ? 108 TYR A CG 1 ATOM 833 C CD1 . TYR A 1 110 ? -19.174 2.416 29.714 1.00 23.90 ? 108 TYR A CD1 1 ATOM 834 C CD2 . TYR A 1 110 ? -18.709 3.396 31.840 1.00 22.66 ? 108 TYR A CD2 1 ATOM 835 C CE1 . TYR A 1 110 ? -17.986 1.690 29.782 1.00 24.30 ? 108 TYR A CE1 1 ATOM 836 C CE2 . TYR A 1 110 ? -17.519 2.674 31.920 1.00 23.49 ? 108 TYR A CE2 1 ATOM 837 C CZ . TYR A 1 110 ? -17.160 1.823 30.887 1.00 29.99 ? 108 TYR A CZ 1 ATOM 838 O OH . TYR A 1 110 ? -15.992 1.106 30.963 1.00 29.83 ? 108 TYR A OH 1 ATOM 839 N N . SER A 1 111 ? -19.586 6.675 31.479 1.00 21.53 ? 109 SER A N 1 ATOM 840 C CA . SER A 1 111 ? -18.512 7.391 32.155 1.00 22.09 ? 109 SER A CA 1 ATOM 841 C C . SER A 1 111 ? -18.394 6.832 33.576 1.00 27.78 ? 109 SER A C 1 ATOM 842 O O . SER A 1 111 ? -19.400 6.389 34.142 1.00 27.00 ? 109 SER A O 1 ATOM 843 C CB . SER A 1 111 ? -18.744 8.899 32.141 1.00 25.76 ? 109 SER A CB 1 ATOM 844 O OG . SER A 1 111 ? -19.745 9.314 33.053 1.00 36.59 ? 109 SER A OG 1 ATOM 845 N N . ASP A 1 112 ? -17.169 6.802 34.131 1.00 25.94 ? 110 ASP A N 1 ATOM 846 C CA . ASP A 1 112 ? -16.911 6.259 35.470 1.00 26.41 ? 110 ASP A CA 1 ATOM 847 C C . ASP A 1 112 ? -17.633 7.003 36.597 1.00 32.09 ? 110 ASP A C 1 ATOM 848 O O . ASP A 1 112 ? -18.083 6.365 37.549 1.00 31.95 ? 110 ASP A O 1 ATOM 849 C CB . ASP A 1 112 ? -15.405 6.110 35.737 1.00 28.15 ? 110 ASP A CB 1 ATOM 850 C CG . ASP A 1 112 ? -14.709 5.164 34.770 1.00 36.69 ? 110 ASP A CG 1 ATOM 851 O OD1 . ASP A 1 112 ? -15.154 4.000 34.651 1.00 37.02 ? 110 ASP A OD1 1 ATOM 852 O OD2 . ASP A 1 112 ? -13.717 5.585 34.142 1.00 42.07 ? 110 ASP A OD2 1 ATOM 853 N N . ASP A 1 113 ? -17.788 8.334 36.465 1.00 29.87 ? 111 ASP A N 1 ATOM 854 C CA . ASP A 1 113 ? -18.492 9.166 37.447 1.00 30.12 ? 111 ASP A CA 1 ATOM 855 C C . ASP A 1 113 ? -20.016 9.208 37.208 1.00 34.56 ? 111 ASP A C 1 ATOM 856 O O . ASP A 1 113 ? -20.756 9.712 38.057 1.00 34.37 ? 111 ASP A O 1 ATOM 857 C CB . ASP A 1 113 ? -17.890 10.586 37.502 1.00 32.00 ? 111 ASP A CB 1 ATOM 858 C CG . ASP A 1 113 ? -17.791 11.338 36.180 1.00 41.99 ? 111 ASP A CG 1 ATOM 859 O OD1 . ASP A 1 113 ? -18.490 10.951 35.215 1.00 42.49 ? 111 ASP A OD1 1 ATOM 860 O OD2 . ASP A 1 113 ? -17.036 12.330 36.119 1.00 48.05 ? 111 ASP A OD2 1 ATOM 861 N N . LYS A 1 114 ? -20.468 8.682 36.045 1.00 31.18 ? 112 LYS A N 1 ATOM 862 C CA . LYS A 1 114 ? -21.865 8.612 35.586 1.00 31.14 ? 112 LYS A CA 1 ATOM 863 C C . LYS A 1 114 ? -22.548 9.979 35.377 1.00 34.51 ? 112 LYS A C 1 ATOM 864 O O . LYS A 1 114 ? -23.781 10.053 35.350 1.00 34.01 ? 112 LYS A O 1 ATOM 865 C CB . LYS A 1 114 ? -22.720 7.649 36.441 1.00 34.02 ? 112 LYS A CB 1 ATOM 866 C CG . LYS A 1 114 ? -22.299 6.182 36.349 1.00 49.16 ? 112 LYS A CG 1 ATOM 867 C CD . LYS A 1 114 ? -23.466 5.206 36.575 1.00 60.89 ? 112 LYS A CD 1 ATOM 868 C CE . LYS A 1 114 ? -23.936 5.079 38.012 1.00 71.83 ? 112 LYS A CE 1 ATOM 869 N NZ . LYS A 1 114 ? -22.939 4.390 38.873 1.00 81.13 ? 112 LYS A NZ 1 ATOM 870 N N . PHE A 1 115 ? -21.752 11.053 35.196 1.00 30.64 ? 113 PHE A N 1 ATOM 871 C CA . PHE A 1 115 ? -22.286 12.396 34.962 1.00 30.14 ? 113 PHE A CA 1 ATOM 872 C C . PHE A 1 115 ? -22.412 12.642 33.469 1.00 31.52 ? 113 PHE A C 1 ATOM 873 O O . PHE A 1 115 ? -21.407 12.791 32.766 1.00 30.91 ? 113 PHE A O 1 ATOM 874 C CB . PHE A 1 115 ? -21.469 13.478 35.693 1.00 32.41 ? 113 PHE A CB 1 ATOM 875 C CG . PHE A 1 115 ? -21.366 13.272 37.188 1.00 34.69 ? 113 PHE A CG 1 ATOM 876 C CD1 . PHE A 1 115 ? -22.482 12.907 37.938 1.00 38.22 ? 113 PHE A CD1 1 ATOM 877 C CD2 . PHE A 1 115 ? -20.159 13.461 37.851 1.00 37.35 ? 113 PHE A CD2 1 ATOM 878 C CE1 . PHE A 1 115 ? -22.383 12.703 39.316 1.00 39.27 ? 113 PHE A CE1 1 ATOM 879 C CE2 . PHE A 1 115 ? -20.063 13.261 39.232 1.00 40.38 ? 113 PHE A CE2 1 ATOM 880 C CZ . PHE A 1 115 ? -21.176 12.887 39.955 1.00 38.50 ? 113 PHE A CZ 1 ATOM 881 N N . TYR A 1 116 ? -23.658 12.618 32.981 1.00 26.38 ? 114 TYR A N 1 ATOM 882 C CA . TYR A 1 116 ? -23.959 12.738 31.561 1.00 25.54 ? 114 TYR A CA 1 ATOM 883 C C . TYR A 1 116 ? -24.390 14.113 31.046 1.00 29.33 ? 114 TYR A C 1 ATOM 884 O O . TYR A 1 116 ? -24.709 14.245 29.862 1.00 29.09 ? 114 TYR A O 1 ATOM 885 C CB . TYR A 1 116 ? -24.851 11.571 31.088 1.00 26.14 ? 114 TYR A CB 1 ATOM 886 C CG . TYR A 1 116 ? -24.281 10.207 31.431 1.00 26.80 ? 114 TYR A CG 1 ATOM 887 C CD1 . TYR A 1 116 ? -22.976 9.867 31.085 1.00 28.44 ? 114 TYR A CD1 1 ATOM 888 C CD2 . TYR A 1 116 ? -25.041 9.264 32.117 1.00 27.29 ? 114 TYR A CD2 1 ATOM 889 C CE1 . TYR A 1 116 ? -22.443 8.620 31.404 1.00 28.72 ? 114 TYR A CE1 1 ATOM 890 C CE2 . TYR A 1 116 ? -24.519 8.012 32.440 1.00 27.89 ? 114 TYR A CE2 1 ATOM 891 C CZ . TYR A 1 116 ? -23.220 7.693 32.079 1.00 33.51 ? 114 TYR A CZ 1 ATOM 892 O OH . TYR A 1 116 ? -22.696 6.462 32.394 1.00 31.51 ? 114 TYR A OH 1 ATOM 893 N N . ALA A 1 117 ? -24.335 15.148 31.917 1.00 25.52 ? 115 ALA A N 1 ATOM 894 C CA . ALA A 1 117 ? -24.637 16.533 31.546 1.00 24.88 ? 115 ALA A CA 1 ATOM 895 C C . ALA A 1 117 ? -23.492 17.035 30.665 1.00 27.20 ? 115 ALA A C 1 ATOM 896 O O . ALA A 1 117 ? -22.332 16.994 31.083 1.00 26.76 ? 115 ALA A O 1 ATOM 897 C CB . ALA A 1 117 ? -24.766 17.399 32.792 1.00 25.53 ? 115 ALA A CB 1 ATOM 898 N N . THR A 1 118 ? -23.810 17.439 29.424 1.00 22.84 ? 116 THR A N 1 ATOM 899 C CA . THR A 1 118 ? -22.803 17.874 28.449 1.00 22.12 ? 116 THR A CA 1 ATOM 900 C C . THR A 1 118 ? -23.268 19.030 27.549 1.00 25.29 ? 116 THR A C 1 ATOM 901 O O . THR A 1 118 ? -24.375 19.542 27.725 1.00 25.07 ? 116 THR A O 1 ATOM 902 C CB . THR A 1 118 ? -22.234 16.651 27.686 1.00 27.42 ? 116 THR A CB 1 ATOM 903 O OG1 . THR A 1 118 ? -21.085 17.050 26.935 1.00 24.85 ? 116 THR A OG1 1 ATOM 904 C CG2 . THR A 1 118 ? -23.267 15.973 26.783 1.00 25.46 ? 116 THR A CG2 1 ATOM 905 N N . ASN A 1 119 ? -22.405 19.446 26.601 1.00 21.09 ? 117 ASN A N 1 ATOM 906 C CA . ASN A 1 119 ? -22.676 20.530 25.656 1.00 20.57 ? 117 ASN A CA 1 ATOM 907 C C . ASN A 1 119 ? -21.975 20.297 24.307 1.00 23.38 ? 117 ASN A C 1 ATOM 908 O O . ASN A 1 119 ? -21.123 19.413 24.215 1.00 22.98 ? 117 ASN A O 1 ATOM 909 C CB . ASN A 1 119 ? -22.311 21.896 26.271 1.00 21.92 ? 117 ASN A CB 1 ATOM 910 C CG . ASN A 1 119 ? -20.847 22.113 26.586 1.00 43.50 ? 117 ASN A CG 1 ATOM 911 O OD1 . ASN A 1 119 ? -19.966 21.950 25.730 1.00 35.74 ? 117 ASN A OD1 1 ATOM 912 N ND2 . ASN A 1 119 ? -20.573 22.523 27.824 1.00 39.08 ? 117 ASN A ND2 1 ATOM 913 N N . ASP A 1 120 ? -22.315 21.105 23.277 1.00 19.12 ? 118 ASP A N 1 ATOM 914 C CA . ASP A 1 120 ? -21.755 21.014 21.920 1.00 18.50 ? 118 ASP A CA 1 ATOM 915 C C . ASP A 1 120 ? -20.223 20.967 21.860 1.00 21.12 ? 118 ASP A C 1 ATOM 916 O O . ASP A 1 120 ? -19.675 20.134 21.135 1.00 19.83 ? 118 ASP A O 1 ATOM 917 C CB . ASP A 1 120 ? -22.286 22.148 21.027 1.00 20.09 ? 118 ASP A CB 1 ATOM 918 C CG . ASP A 1 120 ? -23.777 22.111 20.749 1.00 25.47 ? 118 ASP A CG 1 ATOM 919 O OD1 . ASP A 1 120 ? -24.335 21.000 20.646 1.00 25.66 ? 118 ASP A OD1 1 ATOM 920 O OD2 . ASP A 1 120 ? -24.375 23.196 20.577 1.00 28.04 ? 118 ASP A OD2 1 ATOM 921 N N . THR A 1 121 ? -19.541 21.852 22.622 1.00 17.44 ? 119 THR A N 1 ATOM 922 C CA . THR A 1 121 ? -18.075 21.933 22.658 1.00 17.25 ? 119 THR A CA 1 ATOM 923 C C . THR A 1 121 ? -17.428 20.704 23.296 1.00 20.51 ? 119 THR A C 1 ATOM 924 O O . THR A 1 121 ? -16.447 20.197 22.753 1.00 20.00 ? 119 THR A O 1 ATOM 925 C CB . THR A 1 121 ? -17.583 23.261 23.271 1.00 25.98 ? 119 THR A CB 1 ATOM 926 O OG1 . THR A 1 121 ? -18.088 23.385 24.598 1.00 28.82 ? 119 THR A OG1 1 ATOM 927 C CG2 . THR A 1 121 ? -17.980 24.479 22.448 1.00 22.50 ? 119 THR A CG2 1 ATOM 928 N N . GLU A 1 122 ? -17.976 20.222 24.436 1.00 17.12 ? 120 GLU A N 1 ATOM 929 C CA . GLU A 1 122 ? -17.467 19.032 25.129 1.00 16.91 ? 120 GLU A CA 1 ATOM 930 C C . GLU A 1 122 ? -17.651 17.770 24.266 1.00 20.41 ? 120 GLU A C 1 ATOM 931 O O . GLU A 1 122 ? -16.734 16.950 24.196 1.00 19.74 ? 120 GLU A O 1 ATOM 932 C CB . GLU A 1 122 ? -18.122 18.860 26.518 1.00 18.28 ? 120 GLU A CB 1 ATOM 933 C CG . GLU A 1 122 ? -17.516 17.721 27.333 1.00 28.42 ? 120 GLU A CG 1 ATOM 934 C CD . GLU A 1 122 ? -18.061 17.453 28.723 1.00 49.32 ? 120 GLU A CD 1 ATOM 935 O OE1 . GLU A 1 122 ? -19.272 17.674 28.955 1.00 40.28 ? 120 GLU A OE1 1 ATOM 936 O OE2 . GLU A 1 122 ? -17.271 16.994 29.579 1.00 44.35 ? 120 GLU A OE2 1 ATOM 937 N N . VAL A 1 123 ? -18.818 17.639 23.596 1.00 16.79 ? 121 VAL A N 1 ATOM 938 C CA . VAL A 1 123 ? -19.152 16.501 22.725 1.00 16.47 ? 121 VAL A CA 1 ATOM 939 C C . VAL A 1 123 ? -18.180 16.396 21.543 1.00 19.72 ? 121 VAL A C 1 ATOM 940 O O . VAL A 1 123 ? -17.692 15.300 21.264 1.00 19.19 ? 121 VAL A O 1 ATOM 941 C CB . VAL A 1 123 ? -20.650 16.493 22.292 1.00 20.26 ? 121 VAL A CB 1 ATOM 942 C CG1 . VAL A 1 123 ? -20.937 15.414 21.248 1.00 19.98 ? 121 VAL A CG1 1 ATOM 943 C CG2 . VAL A 1 123 ? -21.563 16.306 23.495 1.00 20.02 ? 121 VAL A CG2 1 ATOM 944 N N . ALA A 1 124 ? -17.874 17.535 20.885 1.00 16.50 ? 122 ALA A N 1 ATOM 945 C CA . ALA A 1 124 ? -16.950 17.600 19.750 1.00 16.44 ? 122 ALA A CA 1 ATOM 946 C C . ALA A 1 124 ? -15.536 17.179 20.156 1.00 20.45 ? 122 ALA A C 1 ATOM 947 O O . ALA A 1 124 ? -14.906 16.402 19.435 1.00 20.24 ? 122 ALA A O 1 ATOM 948 C CB . ALA A 1 124 ? -16.940 19.000 19.153 1.00 17.13 ? 122 ALA A CB 1 ATOM 949 N N . GLN A 1 125 ? -15.061 17.663 21.325 1.00 16.48 ? 123 GLN A N 1 ATOM 950 C CA . GLN A 1 125 ? -13.739 17.350 21.872 1.00 16.06 ? 123 GLN A CA 1 ATOM 951 C C . GLN A 1 125 ? -13.637 15.877 22.282 1.00 19.67 ? 123 GLN A C 1 ATOM 952 O O . GLN A 1 125 ? -12.615 15.245 22.006 1.00 19.60 ? 123 GLN A O 1 ATOM 953 C CB . GLN A 1 125 ? -13.381 18.305 23.033 1.00 17.19 ? 123 GLN A CB 1 ATOM 954 C CG . GLN A 1 125 ? -11.978 18.117 23.642 1.00 22.33 ? 123 GLN A CG 1 ATOM 955 C CD . GLN A 1 125 ? -10.826 18.271 22.666 1.00 32.94 ? 123 GLN A CD 1 ATOM 956 O OE1 . GLN A 1 125 ? -10.824 19.130 21.779 1.00 25.89 ? 123 GLN A OE1 1 ATOM 957 N NE2 . GLN A 1 125 ? -9.798 17.457 22.838 1.00 24.04 ? 123 GLN A NE2 1 ATOM 958 N N . SER A 1 126 ? -14.704 15.328 22.907 1.00 15.79 ? 124 SER A N 1 ATOM 959 C CA . SER A 1 126 ? -14.772 13.925 23.323 1.00 15.49 ? 124 SER A CA 1 ATOM 960 C C . SER A 1 126 ? -14.789 13.001 22.099 1.00 18.94 ? 124 SER A C 1 ATOM 961 O O . SER A 1 126 ? -14.123 11.967 22.117 1.00 18.09 ? 124 SER A O 1 ATOM 962 C CB . SER A 1 126 ? -15.994 13.676 24.200 1.00 18.95 ? 124 SER A CB 1 ATOM 963 O OG . SER A 1 126 ? -16.040 12.338 24.668 1.00 25.65 ? 124 SER A OG 1 ATOM 964 N N . ASN A 1 127 ? -15.532 13.395 21.034 1.00 15.32 ? 125 ASN A N 1 ATOM 965 C CA . ASN A 1 127 ? -15.611 12.672 19.760 1.00 15.05 ? 125 ASN A CA 1 ATOM 966 C C . ASN A 1 127 ? -14.259 12.697 19.051 1.00 19.18 ? 125 ASN A C 1 ATOM 967 O O . ASN A 1 127 ? -13.882 11.704 18.426 1.00 18.71 ? 125 ASN A O 1 ATOM 968 C CB . ASN A 1 127 ? -16.691 13.272 18.847 1.00 14.79 ? 125 ASN A CB 1 ATOM 969 C CG . ASN A 1 127 ? -18.110 12.853 19.157 1.00 27.06 ? 125 ASN A CG 1 ATOM 970 O OD1 . ASN A 1 127 ? -19.074 13.547 18.814 1.00 22.28 ? 125 ASN A OD1 1 ATOM 971 N ND2 . ASN A 1 127 ? -18.280 11.695 19.775 1.00 13.88 ? 125 ASN A ND2 1 ATOM 972 N N . PHE A 1 128 ? -13.527 13.829 19.161 1.00 16.33 ? 126 PHE A N 1 ATOM 973 C CA . PHE A 1 128 ? -12.198 14.000 18.574 1.00 16.47 ? 126 PHE A CA 1 ATOM 974 C C . PHE A 1 128 ? -11.195 13.066 19.245 1.00 20.23 ? 126 PHE A C 1 ATOM 975 O O . PHE A 1 128 ? -10.444 12.382 18.547 1.00 20.15 ? 126 PHE A O 1 ATOM 976 C CB . PHE A 1 128 ? -11.740 15.471 18.627 1.00 18.31 ? 126 PHE A CB 1 ATOM 977 C CG . PHE A 1 128 ? -10.327 15.695 18.138 1.00 20.01 ? 126 PHE A CG 1 ATOM 978 C CD1 . PHE A 1 128 ? -10.016 15.587 16.786 1.00 23.16 ? 126 PHE A CD1 1 ATOM 979 C CD2 . PHE A 1 128 ? -9.307 16.009 19.029 1.00 22.37 ? 126 PHE A CD2 1 ATOM 980 C CE1 . PHE A 1 128 ? -8.706 15.781 16.336 1.00 24.14 ? 126 PHE A CE1 1 ATOM 981 C CE2 . PHE A 1 128 ? -7.998 16.207 18.577 1.00 25.33 ? 126 PHE A CE2 1 ATOM 982 C CZ . PHE A 1 128 ? -7.708 16.095 17.233 1.00 23.40 ? 126 PHE A CZ 1 ATOM 983 N N . GLU A 1 129 ? -11.221 13.001 20.591 1.00 16.29 ? 127 GLU A N 1 ATOM 984 C CA . GLU A 1 129 ? -10.357 12.114 21.375 1.00 16.07 ? 127 GLU A CA 1 ATOM 985 C C . GLU A 1 129 ? -10.705 10.644 21.112 1.00 19.80 ? 127 GLU A C 1 ATOM 986 O O . GLU A 1 129 ? -9.801 9.808 21.091 1.00 19.27 ? 127 GLU A O 1 ATOM 987 C CB . GLU A 1 129 ? -10.421 12.453 22.871 1.00 17.27 ? 127 GLU A CB 1 ATOM 988 C CG . GLU A 1 129 ? -9.645 13.713 23.226 1.00 25.98 ? 127 GLU A CG 1 ATOM 989 C CD . GLU A 1 129 ? -9.803 14.217 24.648 1.00 40.10 ? 127 GLU A CD 1 ATOM 990 O OE1 . GLU A 1 129 ? -9.611 13.417 25.592 1.00 28.63 ? 127 GLU A OE1 1 ATOM 991 O OE2 . GLU A 1 129 ? -10.063 15.430 24.819 1.00 32.66 ? 127 GLU A OE2 1 ATOM 992 N N . ALA A 1 130 ? -12.003 10.344 20.867 1.00 16.34 ? 128 ALA A N 1 ATOM 993 C CA . ALA A 1 130 ? -12.483 8.997 20.541 1.00 16.47 ? 128 ALA A CA 1 ATOM 994 C C . ALA A 1 130 ? -11.904 8.549 19.193 1.00 20.70 ? 128 ALA A C 1 ATOM 995 O O . ALA A 1 130 ? -11.438 7.415 19.090 1.00 20.22 ? 128 ALA A O 1 ATOM 996 C CB . ALA A 1 130 ? -14.002 8.972 20.497 1.00 17.33 ? 128 ALA A CB 1 ATOM 997 N N . LEU A 1 131 ? -11.895 9.456 18.183 1.00 17.87 ? 129 LEU A N 1 ATOM 998 C CA . LEU A 1 131 ? -11.326 9.214 16.851 1.00 17.81 ? 129 LEU A CA 1 ATOM 999 C C . LEU A 1 131 ? -9.826 8.939 16.951 1.00 20.99 ? 129 LEU A C 1 ATOM 1000 O O . LEU A 1 131 ? -9.335 8.041 16.271 1.00 20.44 ? 129 LEU A O 1 ATOM 1001 C CB . LEU A 1 131 ? -11.581 10.395 15.894 1.00 17.99 ? 129 LEU A CB 1 ATOM 1002 C CG . LEU A 1 131 ? -12.910 10.414 15.126 1.00 23.13 ? 129 LEU A CG 1 ATOM 1003 C CD1 . LEU A 1 131 ? -13.079 11.723 14.388 1.00 23.34 ? 129 LEU A CD1 1 ATOM 1004 C CD2 . LEU A 1 131 ? -13.013 9.253 14.127 1.00 25.54 ? 129 LEU A CD2 1 ATOM 1005 N N . GLN A 1 132 ? -9.111 9.697 17.819 1.00 17.42 ? 130 GLN A N 1 ATOM 1006 C CA . GLN A 1 132 ? -7.675 9.529 18.082 1.00 16.86 ? 130 GLN A CA 1 ATOM 1007 C C . GLN A 1 132 ? -7.418 8.135 18.661 1.00 20.11 ? 130 GLN A C 1 ATOM 1008 O O . GLN A 1 132 ? -6.455 7.479 18.263 1.00 19.47 ? 130 GLN A O 1 ATOM 1009 C CB . GLN A 1 132 ? -7.160 10.601 19.055 1.00 17.94 ? 130 GLN A CB 1 ATOM 1010 C CG . GLN A 1 132 ? -7.036 11.993 18.450 1.00 24.38 ? 130 GLN A CG 1 ATOM 1011 C CD . GLN A 1 132 ? -6.404 12.982 19.398 1.00 34.97 ? 130 GLN A CD 1 ATOM 1012 O OE1 . GLN A 1 132 ? -6.816 13.136 20.553 1.00 26.61 ? 130 GLN A OE1 1 ATOM 1013 N NE2 . GLN A 1 132 ? -5.402 13.699 18.914 1.00 26.04 ? 130 GLN A NE2 1 ATOM 1014 N N . ASP A 1 133 ? -8.301 7.679 19.576 1.00 16.45 ? 131 ASP A N 1 ATOM 1015 C CA . ASP A 1 133 ? -8.220 6.352 20.185 1.00 16.19 ? 131 ASP A CA 1 ATOM 1016 C C . ASP A 1 133 ? -8.470 5.262 19.142 1.00 20.39 ? 131 ASP A C 1 ATOM 1017 O O . ASP A 1 133 ? -7.787 4.238 19.167 1.00 19.73 ? 131 ASP A O 1 ATOM 1018 C CB . ASP A 1 133 ? -9.192 6.220 21.367 1.00 17.93 ? 131 ASP A CB 1 ATOM 1019 C CG . ASP A 1 133 ? -8.793 5.157 22.376 1.00 25.79 ? 131 ASP A CG 1 ATOM 1020 O OD1 . ASP A 1 133 ? -7.598 5.106 22.746 1.00 26.66 ? 131 ASP A OD1 1 ATOM 1021 O OD2 . ASP A 1 133 ? -9.681 4.410 22.830 1.00 29.22 ? 131 ASP A OD2 1 ATOM 1022 N N . PHE A 1 134 ? -9.416 5.501 18.200 1.00 17.67 ? 132 PHE A N 1 ATOM 1023 C CA . PHE A 1 134 ? -9.722 4.570 17.109 1.00 17.36 ? 132 PHE A CA 1 ATOM 1024 C C . PHE A 1 134 ? -8.475 4.332 16.254 1.00 21.15 ? 132 PHE A C 1 ATOM 1025 O O . PHE A 1 134 ? -8.173 3.184 15.934 1.00 20.45 ? 132 PHE A O 1 ATOM 1026 C CB . PHE A 1 134 ? -10.901 5.076 16.246 1.00 18.93 ? 132 PHE A CB 1 ATOM 1027 C CG . PHE A 1 134 ? -11.142 4.279 14.982 1.00 20.12 ? 132 PHE A CG 1 ATOM 1028 C CD1 . PHE A 1 134 ? -11.894 3.111 15.009 1.00 22.96 ? 132 PHE A CD1 1 ATOM 1029 C CD2 . PHE A 1 134 ? -10.597 4.686 13.769 1.00 22.07 ? 132 PHE A CD2 1 ATOM 1030 C CE1 . PHE A 1 134 ? -12.105 2.368 13.843 1.00 23.76 ? 132 PHE A CE1 1 ATOM 1031 C CE2 . PHE A 1 134 ? -10.795 3.934 12.607 1.00 24.77 ? 132 PHE A CE2 1 ATOM 1032 C CZ . PHE A 1 134 ? -11.549 2.782 12.652 1.00 22.72 ? 132 PHE A CZ 1 ATOM 1033 N N . PHE A 1 135 ? -7.752 5.416 15.903 1.00 17.93 ? 133 PHE A N 1 ATOM 1034 C CA . PHE A 1 135 ? -6.527 5.330 15.109 1.00 17.89 ? 133 PHE A CA 1 ATOM 1035 C C . PHE A 1 135 ? -5.360 4.696 15.868 1.00 21.50 ? 133 PHE A C 1 ATOM 1036 O O . PHE A 1 135 ? -4.494 4.094 15.239 1.00 20.87 ? 133 PHE A O 1 ATOM 1037 C CB . PHE A 1 135 ? -6.169 6.670 14.451 1.00 19.72 ? 133 PHE A CB 1 ATOM 1038 C CG . PHE A 1 135 ? -7.166 7.100 13.396 1.00 21.43 ? 133 PHE A CG 1 ATOM 1039 C CD1 . PHE A 1 135 ? -7.444 6.284 12.302 1.00 24.44 ? 133 PHE A CD1 1 ATOM 1040 C CD2 . PHE A 1 135 ? -7.814 8.326 13.485 1.00 23.51 ? 133 PHE A CD2 1 ATOM 1041 C CE1 . PHE A 1 135 ? -8.374 6.676 11.336 1.00 25.39 ? 133 PHE A CE1 1 ATOM 1042 C CE2 . PHE A 1 135 ? -8.738 8.721 12.513 1.00 26.28 ? 133 PHE A CE2 1 ATOM 1043 C CZ . PHE A 1 135 ? -9.014 7.892 11.447 1.00 24.38 ? 133 PHE A CZ 1 ATOM 1044 N N . ARG A 1 136 ? -5.369 4.774 17.213 1.00 18.04 ? 134 ARG A N 1 ATOM 1045 C CA . ARG A 1 136 ? -4.362 4.114 18.048 1.00 18.04 ? 134 ARG A CA 1 ATOM 1046 C C . ARG A 1 136 ? -4.665 2.611 18.078 1.00 22.74 ? 134 ARG A C 1 ATOM 1047 O O . ARG A 1 136 ? -3.742 1.799 18.053 1.00 22.42 ? 134 ARG A O 1 ATOM 1048 C CB . ARG A 1 136 ? -4.366 4.676 19.476 1.00 17.64 ? 134 ARG A CB 1 ATOM 1049 C CG . ARG A 1 136 ? -3.690 6.035 19.613 1.00 25.64 ? 134 ARG A CG 1 ATOM 1050 C CD . ARG A 1 136 ? -3.472 6.416 21.065 1.00 30.55 ? 134 ARG A CD 1 ATOM 1051 N NE . ARG A 1 136 ? -4.728 6.687 21.767 1.00 35.59 ? 134 ARG A NE 1 ATOM 1052 C CZ . ARG A 1 136 ? -5.243 7.898 21.948 1.00 45.39 ? 134 ARG A CZ 1 ATOM 1053 N NH1 . ARG A 1 136 ? -4.612 8.973 21.490 1.00 31.75 ? 134 ARG A NH1 1 ATOM 1054 N NH2 . ARG A 1 136 ? -6.386 8.047 22.602 1.00 29.34 ? 134 ARG A NH2 1 ATOM 1055 N N . LEU A 1 137 ? -5.965 2.247 18.116 1.00 20.18 ? 135 LEU A N 1 ATOM 1056 C CA . LEU A 1 137 ? -6.423 0.855 18.145 1.00 20.61 ? 135 LEU A CA 1 ATOM 1057 C C . LEU A 1 137 ? -6.353 0.194 16.772 1.00 24.12 ? 135 LEU A C 1 ATOM 1058 O O . LEU A 1 137 ? -6.066 -1.002 16.685 1.00 23.91 ? 135 LEU A O 1 ATOM 1059 C CB . LEU A 1 137 ? -7.836 0.741 18.744 1.00 20.95 ? 135 LEU A CB 1 ATOM 1060 C CG . LEU A 1 137 ? -7.966 1.008 20.255 1.00 26.16 ? 135 LEU A CG 1 ATOM 1061 C CD1 . LEU A 1 137 ? -9.405 1.241 20.638 1.00 26.41 ? 135 LEU A CD1 1 ATOM 1062 C CD2 . LEU A 1 137 ? -7.397 -0.139 21.089 1.00 29.08 ? 135 LEU A CD2 1 ATOM 1063 N N . PHE A 1 138 ? -6.582 0.974 15.704 1.00 20.36 ? 136 PHE A N 1 ATOM 1064 C CA . PHE A 1 138 ? -6.529 0.503 14.317 1.00 20.13 ? 136 PHE A CA 1 ATOM 1065 C C . PHE A 1 138 ? -5.464 1.324 13.544 1.00 24.34 ? 136 PHE A C 1 ATOM 1066 O O . PHE A 1 138 ? -5.837 2.168 12.720 1.00 23.73 ? 136 PHE A O 1 ATOM 1067 C CB . PHE A 1 138 ? -7.922 0.616 13.653 1.00 21.78 ? 136 PHE A CB 1 ATOM 1068 C CG . PHE A 1 138 ? -9.027 -0.206 14.278 1.00 23.16 ? 136 PHE A CG 1 ATOM 1069 C CD1 . PHE A 1 138 ? -9.722 0.261 15.390 1.00 26.04 ? 136 PHE A CD1 1 ATOM 1070 C CD2 . PHE A 1 138 ? -9.410 -1.421 13.723 1.00 25.07 ? 136 PHE A CD2 1 ATOM 1071 C CE1 . PHE A 1 138 ? -10.756 -0.491 15.955 1.00 26.86 ? 136 PHE A CE1 1 ATOM 1072 C CE2 . PHE A 1 138 ? -10.448 -2.169 14.285 1.00 27.79 ? 136 PHE A CE2 1 ATOM 1073 C CZ . PHE A 1 138 ? -11.118 -1.696 15.393 1.00 25.87 ? 136 PHE A CZ 1 ATOM 1074 N N . PRO A 1 139 ? -4.139 1.119 13.800 1.00 21.53 ? 137 PRO A N 1 ATOM 1075 C CA . PRO A 1 139 ? -3.122 1.934 13.105 1.00 21.70 ? 137 PRO A CA 1 ATOM 1076 C C . PRO A 1 139 ? -3.035 1.768 11.591 1.00 26.33 ? 137 PRO A C 1 ATOM 1077 O O . PRO A 1 139 ? -2.567 2.689 10.921 1.00 26.42 ? 137 PRO A O 1 ATOM 1078 C CB . PRO A 1 139 ? -1.815 1.555 13.809 1.00 23.40 ? 137 PRO A CB 1 ATOM 1079 C CG . PRO A 1 139 ? -2.060 0.196 14.348 1.00 27.66 ? 137 PRO A CG 1 ATOM 1080 C CD . PRO A 1 139 ? -3.501 0.191 14.759 1.00 23.16 ? 137 PRO A CD 1 ATOM 1081 N N . GLU A 1 140 ? -3.507 0.626 11.048 1.00 23.29 ? 138 GLU A N 1 ATOM 1082 C CA . GLU A 1 140 ? -3.496 0.369 9.605 1.00 23.30 ? 138 GLU A CA 1 ATOM 1083 C C . GLU A 1 140 ? -4.517 1.237 8.830 1.00 27.44 ? 138 GLU A C 1 ATOM 1084 O O . GLU A 1 140 ? -4.475 1.272 7.598 1.00 26.80 ? 138 GLU A O 1 ATOM 1085 C CB . GLU A 1 140 ? -3.633 -1.141 9.295 1.00 24.72 ? 138 GLU A CB 1 ATOM 1086 C CG . GLU A 1 140 ? -5.054 -1.689 9.255 1.00 36.48 ? 138 GLU A CG 1 ATOM 1087 C CD . GLU A 1 140 ? -5.663 -2.118 10.576 1.00 59.57 ? 138 GLU A CD 1 ATOM 1088 O OE1 . GLU A 1 140 ? -5.762 -1.272 11.493 1.00 56.13 ? 138 GLU A OE1 1 ATOM 1089 O OE2 . GLU A 1 140 ? -6.106 -3.285 10.668 1.00 54.17 ? 138 GLU A OE2 1 ATOM 1090 N N . TYR A 1 141 ? -5.411 1.946 9.558 1.00 24.14 ? 139 TYR A N 1 ATOM 1091 C CA . TYR A 1 141 ? -6.442 2.817 8.988 1.00 23.98 ? 139 TYR A CA 1 ATOM 1092 C C . TYR A 1 141 ? -6.137 4.325 9.052 1.00 27.92 ? 139 TYR A C 1 ATOM 1093 O O . TYR A 1 141 ? -6.953 5.130 8.597 1.00 27.32 ? 139 TYR A O 1 ATOM 1094 C CB . TYR A 1 141 ? -7.823 2.490 9.590 1.00 25.13 ? 139 TYR A CB 1 ATOM 1095 C CG . TYR A 1 141 ? -8.382 1.174 9.099 1.00 26.94 ? 139 TYR A CG 1 ATOM 1096 C CD1 . TYR A 1 141 ? -8.801 1.021 7.781 1.00 29.09 ? 139 TYR A CD1 1 ATOM 1097 C CD2 . TYR A 1 141 ? -8.499 0.081 9.952 1.00 27.86 ? 139 TYR A CD2 1 ATOM 1098 C CE1 . TYR A 1 141 ? -9.304 -0.192 7.319 1.00 30.35 ? 139 TYR A CE1 1 ATOM 1099 C CE2 . TYR A 1 141 ? -9.009 -1.137 9.502 1.00 28.86 ? 139 TYR A CE2 1 ATOM 1100 C CZ . TYR A 1 141 ? -9.409 -1.268 8.183 1.00 36.10 ? 139 TYR A CZ 1 ATOM 1101 O OH . TYR A 1 141 ? -9.906 -2.459 7.718 1.00 36.62 ? 139 TYR A OH 1 ATOM 1102 N N . LYS A 1 142 ? -4.954 4.698 9.581 1.00 24.94 ? 140 LYS A N 1 ATOM 1103 C CA . LYS A 1 142 ? -4.504 6.089 9.727 1.00 24.93 ? 140 LYS A CA 1 ATOM 1104 C C . LYS A 1 142 ? -4.408 6.888 8.427 1.00 28.25 ? 140 LYS A C 1 ATOM 1105 O O . LYS A 1 142 ? -4.757 8.068 8.426 1.00 28.05 ? 140 LYS A O 1 ATOM 1106 C CB . LYS A 1 142 ? -3.166 6.153 10.472 1.00 27.88 ? 140 LYS A CB 1 ATOM 1107 C CG . LYS A 1 142 ? -3.322 6.334 11.969 1.00 45.15 ? 140 LYS A CG 1 ATOM 1108 C CD . LYS A 1 142 ? -1.982 6.619 12.640 1.00 57.14 ? 140 LYS A CD 1 ATOM 1109 C CE . LYS A 1 142 ? -1.354 5.389 13.248 1.00 67.76 ? 140 LYS A CE 1 ATOM 1110 N NZ . LYS A 1 142 ? -2.039 4.983 14.502 1.00 75.77 ? 140 LYS A NZ 1 ATOM 1111 N N . ASN A 1 143 ? -3.922 6.265 7.338 1.00 24.28 ? 141 ASN A N 1 ATOM 1112 C CA . ASN A 1 143 ? -3.748 6.932 6.042 1.00 23.81 ? 141 ASN A CA 1 ATOM 1113 C C . ASN A 1 143 ? -4.967 6.856 5.114 1.00 26.55 ? 141 ASN A C 1 ATOM 1114 O O . ASN A 1 143 ? -4.989 7.525 4.076 1.00 25.98 ? 141 ASN A O 1 ATOM 1115 C CB . ASN A 1 143 ? -2.472 6.444 5.336 1.00 25.29 ? 141 ASN A CB 1 ATOM 1116 C CG . ASN A 1 143 ? -1.179 6.734 6.071 1.00 51.13 ? 141 ASN A CG 1 ATOM 1117 O OD1 . ASN A 1 143 ? -0.229 5.947 6.022 1.00 47.47 ? 141 ASN A OD1 1 ATOM 1118 N ND2 . ASN A 1 143 ? -1.091 7.873 6.751 1.00 43.82 ? 141 ASN A ND2 1 ATOM 1119 N N . ASN A 1 144 ? -5.982 6.058 5.498 1.00 22.44 ? 142 ASN A N 1 ATOM 1120 C CA . ASN A 1 144 ? -7.226 5.878 4.746 1.00 22.00 ? 142 ASN A CA 1 ATOM 1121 C C . ASN A 1 144 ? -8.032 7.170 4.715 1.00 24.50 ? 142 ASN A C 1 ATOM 1122 O O . ASN A 1 144 ? -7.973 7.950 5.667 1.00 24.07 ? 142 ASN A O 1 ATOM 1123 C CB . ASN A 1 144 ? -8.066 4.751 5.366 1.00 22.81 ? 142 ASN A CB 1 ATOM 1124 C CG . ASN A 1 144 ? -7.542 3.355 5.112 1.00 38.34 ? 142 ASN A CG 1 ATOM 1125 O OD1 . ASN A 1 144 ? -8.218 2.520 4.511 1.00 31.79 ? 142 ASN A OD1 1 ATOM 1126 N ND2 . ASN A 1 144 ? -6.349 3.046 5.596 1.00 28.73 ? 142 ASN A ND2 1 ATOM 1127 N N . LYS A 1 145 ? -8.769 7.403 3.616 1.00 20.36 ? 143 LYS A N 1 ATOM 1128 C CA . LYS A 1 145 ? -9.613 8.590 3.440 1.00 19.61 ? 143 LYS A CA 1 ATOM 1129 C C . LYS A 1 145 ? -10.674 8.615 4.546 1.00 22.75 ? 143 LYS A C 1 ATOM 1130 O O . LYS A 1 145 ? -11.357 7.615 4.763 1.00 22.45 ? 143 LYS A O 1 ATOM 1131 C CB . LYS A 1 145 ? -10.276 8.592 2.050 1.00 21.76 ? 143 LYS A CB 1 ATOM 1132 C CG . LYS A 1 145 ? -9.323 8.870 0.889 1.00 34.54 ? 143 LYS A CG 1 ATOM 1133 C CD . LYS A 1 145 ? -10.074 8.849 -0.427 1.00 44.27 ? 143 LYS A CD 1 ATOM 1134 C CE . LYS A 1 145 ? -9.327 9.490 -1.574 1.00 56.60 ? 143 LYS A CE 1 ATOM 1135 N NZ . LYS A 1 145 ? -8.276 8.601 -2.135 1.00 66.05 ? 143 LYS A NZ 1 ATOM 1136 N N . LEU A 1 146 ? -10.740 9.717 5.300 1.00 18.72 ? 144 LEU A N 1 ATOM 1137 C CA . LEU A 1 146 ? -11.675 9.850 6.412 1.00 18.25 ? 144 LEU A CA 1 ATOM 1138 C C . LEU A 1 146 ? -12.848 10.751 6.062 1.00 21.56 ? 144 LEU A C 1 ATOM 1139 O O . LEU A 1 146 ? -12.658 11.882 5.605 1.00 21.41 ? 144 LEU A O 1 ATOM 1140 C CB . LEU A 1 146 ? -10.951 10.327 7.692 1.00 18.34 ? 144 LEU A CB 1 ATOM 1141 C CG . LEU A 1 146 ? -11.800 10.556 8.959 1.00 22.77 ? 144 LEU A CG 1 ATOM 1142 C CD1 . LEU A 1 146 ? -12.257 9.235 9.582 1.00 22.74 ? 144 LEU A CD1 1 ATOM 1143 C CD2 . LEU A 1 146 ? -11.026 11.363 9.983 1.00 24.58 ? 144 LEU A CD2 1 ATOM 1144 N N . PHE A 1 147 ? -14.061 10.234 6.283 1.00 17.33 ? 145 PHE A N 1 ATOM 1145 C CA . PHE A 1 147 ? -15.316 10.940 6.054 1.00 16.66 ? 145 PHE A CA 1 ATOM 1146 C C . PHE A 1 147 ? -16.140 10.924 7.343 1.00 19.96 ? 145 PHE A C 1 ATOM 1147 O O . PHE A 1 147 ? -16.278 9.873 7.971 1.00 19.43 ? 145 PHE A O 1 ATOM 1148 C CB . PHE A 1 147 ? -16.096 10.315 4.884 1.00 18.32 ? 145 PHE A CB 1 ATOM 1149 C CG . PHE A 1 147 ? -15.428 10.455 3.534 1.00 19.73 ? 145 PHE A CG 1 ATOM 1150 C CD1 . PHE A 1 147 ? -14.504 9.513 3.094 1.00 22.55 ? 145 PHE A CD1 1 ATOM 1151 C CD2 . PHE A 1 147 ? -15.728 11.524 2.699 1.00 21.57 ? 145 PHE A CD2 1 ATOM 1152 C CE1 . PHE A 1 147 ? -13.896 9.637 1.841 1.00 23.35 ? 145 PHE A CE1 1 ATOM 1153 C CE2 . PHE A 1 147 ? -15.120 11.646 1.445 1.00 24.35 ? 145 PHE A CE2 1 ATOM 1154 C CZ . PHE A 1 147 ? -14.211 10.700 1.023 1.00 22.43 ? 145 PHE A CZ 1 ATOM 1155 N N . LEU A 1 148 ? -16.648 12.097 7.756 1.00 16.03 ? 146 LEU A N 1 ATOM 1156 C CA . LEU A 1 148 ? -17.451 12.238 8.974 1.00 15.37 ? 146 LEU A CA 1 ATOM 1157 C C . LEU A 1 148 ? -18.913 12.428 8.579 1.00 18.06 ? 146 LEU A C 1 ATOM 1158 O O . LEU A 1 148 ? -19.247 13.413 7.925 1.00 17.68 ? 146 LEU A O 1 ATOM 1159 C CB . LEU A 1 148 ? -16.939 13.413 9.836 1.00 15.44 ? 146 LEU A CB 1 ATOM 1160 C CG . LEU A 1 148 ? -15.442 13.402 10.213 1.00 20.05 ? 146 LEU A CG 1 ATOM 1161 C CD1 . LEU A 1 148 ? -15.031 14.719 10.815 1.00 20.26 ? 146 LEU A CD1 1 ATOM 1162 C CD2 . LEU A 1 148 ? -15.105 12.265 11.172 1.00 22.28 ? 146 LEU A CD2 1 ATOM 1163 N N . THR A 1 149 ? -19.772 11.448 8.904 1.00 13.66 ? 147 THR A N 1 ATOM 1164 C CA . THR A 1 149 ? -21.186 11.482 8.513 1.00 13.19 ? 147 THR A CA 1 ATOM 1165 C C . THR A 1 149 ? -22.140 11.424 9.709 1.00 17.36 ? 147 THR A C 1 ATOM 1166 O O . THR A 1 149 ? -21.785 10.888 10.762 1.00 16.56 ? 147 THR A O 1 ATOM 1167 C CB . THR A 1 149 ? -21.497 10.401 7.453 1.00 18.25 ? 147 THR A CB 1 ATOM 1168 O OG1 . THR A 1 149 ? -21.350 9.109 8.035 1.00 17.88 ? 147 THR A OG1 1 ATOM 1169 C CG2 . THR A 1 149 ? -20.616 10.511 6.207 1.00 15.45 ? 147 THR A CG2 1 ATOM 1170 N N . GLY A 1 150 ? -23.343 11.961 9.530 1.00 14.36 ? 148 GLY A N 1 ATOM 1171 C CA . GLY A 1 150 ? -24.337 11.978 10.595 1.00 14.06 ? 148 GLY A CA 1 ATOM 1172 C C . GLY A 1 150 ? -25.755 12.338 10.208 1.00 17.30 ? 148 GLY A C 1 ATOM 1173 O O . GLY A 1 150 ? -26.021 12.722 9.065 1.00 16.71 ? 148 GLY A O 1 ATOM 1174 N N . GLU A 1 151 ? -26.667 12.245 11.196 1.00 13.35 ? 149 GLU A N 1 ATOM 1175 C CA . GLU A 1 151 ? -28.099 12.499 11.057 1.00 12.82 ? 149 GLU A CA 1 ATOM 1176 C C . GLU A 1 151 ? -28.674 13.397 12.164 1.00 17.20 ? 149 GLU A C 1 ATOM 1177 O O . GLU A 1 151 ? -28.281 13.269 13.322 1.00 16.21 ? 149 GLU A O 1 ATOM 1178 C CB . GLU A 1 151 ? -28.833 11.154 11.068 1.00 13.87 ? 149 GLU A CB 1 ATOM 1179 C CG . GLU A 1 151 ? -30.269 11.197 10.581 1.00 20.97 ? 149 GLU A CG 1 ATOM 1180 C CD . GLU A 1 151 ? -30.815 9.809 10.341 1.00 29.75 ? 149 GLU A CD 1 ATOM 1181 O OE1 . GLU A 1 151 ? -30.491 9.224 9.285 1.00 16.37 ? 149 GLU A OE1 1 ATOM 1182 O OE2 . GLU A 1 151 ? -31.499 9.275 11.241 1.00 18.05 ? 149 GLU A OE2 1 ATOM 1183 N N . SER A 1 152 ? -29.665 14.245 11.802 1.00 15.06 ? 150 SER A N 1 ATOM 1184 C CA . SER A 1 152 ? -30.428 15.130 12.696 1.00 15.22 ? 150 SER A CA 1 ATOM 1185 C C . SER A 1 152 ? -29.552 16.087 13.513 1.00 19.44 ? 150 SER A C 1 ATOM 1186 O O . SER A 1 152 ? -28.938 16.969 12.909 1.00 19.15 ? 150 SER A O 1 ATOM 1187 C CB . SER A 1 152 ? -31.380 14.316 13.567 1.00 18.57 ? 150 SER A CB 1 ATOM 1188 O OG . SER A 1 152 ? -32.472 15.093 14.029 1.00 28.49 ? 150 SER A OG 1 ATOM 1189 N N . TYR A 1 153 ? -29.453 15.907 14.863 1.00 16.09 ? 151 TYR A N 1 ATOM 1190 C CA . TYR A 1 153 ? -28.594 16.764 15.693 1.00 15.73 ? 151 TYR A CA 1 ATOM 1191 C C . TYR A 1 153 ? -27.116 16.632 15.316 1.00 19.61 ? 151 TYR A C 1 ATOM 1192 O O . TYR A 1 153 ? -26.338 17.543 15.597 1.00 19.03 ? 151 TYR A O 1 ATOM 1193 C CB . TYR A 1 153 ? -28.825 16.587 17.207 1.00 16.49 ? 151 TYR A CB 1 ATOM 1194 C CG . TYR A 1 153 ? -28.329 17.777 18.006 1.00 17.71 ? 151 TYR A CG 1 ATOM 1195 C CD1 . TYR A 1 153 ? -29.097 18.931 18.124 1.00 19.77 ? 151 TYR A CD1 1 ATOM 1196 C CD2 . TYR A 1 153 ? -27.069 17.768 18.599 1.00 18.04 ? 151 TYR A CD2 1 ATOM 1197 C CE1 . TYR A 1 153 ? -28.633 20.041 18.829 1.00 19.74 ? 151 TYR A CE1 1 ATOM 1198 C CE2 . TYR A 1 153 ? -26.591 18.875 19.300 1.00 18.61 ? 151 TYR A CE2 1 ATOM 1199 C CZ . TYR A 1 153 ? -27.379 20.009 19.414 1.00 23.87 ? 151 TYR A CZ 1 ATOM 1200 O OH . TYR A 1 153 ? -26.925 21.108 20.099 1.00 20.81 ? 151 TYR A OH 1 ATOM 1201 N N . ALA A 1 154 ? -26.744 15.551 14.588 1.00 16.51 ? 152 ALA A N 1 ATOM 1202 C CA . ALA A 1 154 ? -25.379 15.381 14.089 1.00 16.54 ? 152 ALA A CA 1 ATOM 1203 C C . ALA A 1 154 ? -25.025 16.449 13.039 1.00 20.48 ? 152 ALA A C 1 ATOM 1204 O O . ALA A 1 154 ? -23.873 16.546 12.611 1.00 20.30 ? 152 ALA A O 1 ATOM 1205 C CB . ALA A 1 154 ? -25.161 13.980 13.556 1.00 17.24 ? 152 ALA A CB 1 ATOM 1206 N N . GLY A 1 155 ? -26.013 17.285 12.706 1.00 16.76 ? 153 GLY A N 1 ATOM 1207 C CA . GLY A 1 155 ? -25.868 18.457 11.852 1.00 16.43 ? 153 GLY A CA 1 ATOM 1208 C C . GLY A 1 155 ? -25.073 19.525 12.578 1.00 20.00 ? 153 GLY A C 1 ATOM 1209 O O . GLY A 1 155 ? -24.582 20.469 11.957 1.00 19.30 ? 153 GLY A O 1 ATOM 1210 N N . ILE A 1 156 ? -24.959 19.373 13.915 1.00 16.99 ? 154 ILE A N 1 ATOM 1211 C CA . ILE A 1 156 ? -24.175 20.201 14.834 1.00 16.63 ? 154 ILE A CA 1 ATOM 1212 C C . ILE A 1 156 ? -22.913 19.393 15.189 1.00 18.98 ? 154 ILE A C 1 ATOM 1213 O O . ILE A 1 156 ? -21.814 19.938 15.110 1.00 18.10 ? 154 ILE A O 1 ATOM 1214 C CB . ILE A 1 156 ? -24.985 20.605 16.111 1.00 19.83 ? 154 ILE A CB 1 ATOM 1215 C CG1 . ILE A 1 156 ? -26.328 21.335 15.786 1.00 20.48 ? 154 ILE A CG1 1 ATOM 1216 C CG2 . ILE A 1 156 ? -24.122 21.367 17.144 1.00 20.14 ? 154 ILE A CG2 1 ATOM 1217 C CD1 . ILE A 1 156 ? -26.259 22.804 15.225 1.00 28.08 ? 154 ILE A CD1 1 ATOM 1218 N N . TYR A 1 157 ? -23.078 18.090 15.554 1.00 15.58 ? 155 TYR A N 1 ATOM 1219 C CA . TYR A 1 157 ? -21.985 17.177 15.931 1.00 15.31 ? 155 TYR A CA 1 ATOM 1220 C C . TYR A 1 157 ? -20.867 17.126 14.884 1.00 19.28 ? 155 TYR A C 1 ATOM 1221 O O . TYR A 1 157 ? -19.709 17.342 15.234 1.00 18.32 ? 155 TYR A O 1 ATOM 1222 C CB . TYR A 1 157 ? -22.486 15.732 16.157 1.00 16.08 ? 155 TYR A CB 1 ATOM 1223 C CG . TYR A 1 157 ? -23.393 15.455 17.341 1.00 17.40 ? 155 TYR A CG 1 ATOM 1224 C CD1 . TYR A 1 157 ? -23.323 16.228 18.499 1.00 19.34 ? 155 TYR A CD1 1 ATOM 1225 C CD2 . TYR A 1 157 ? -24.235 14.346 17.350 1.00 17.99 ? 155 TYR A CD2 1 ATOM 1226 C CE1 . TYR A 1 157 ? -24.121 15.943 19.608 1.00 19.68 ? 155 TYR A CE1 1 ATOM 1227 C CE2 . TYR A 1 157 ? -25.036 14.052 18.451 1.00 18.74 ? 155 TYR A CE2 1 ATOM 1228 C CZ . TYR A 1 157 ? -24.966 14.845 19.584 1.00 24.81 ? 155 TYR A CZ 1 ATOM 1229 O OH . TYR A 1 157 ? -25.742 14.538 20.673 1.00 23.57 ? 155 TYR A OH 1 ATOM 1230 N N . ILE A 1 158 ? -21.220 16.818 13.614 1.00 16.34 ? 156 ILE A N 1 ATOM 1231 C CA . ILE A 1 158 ? -20.287 16.671 12.490 1.00 16.23 ? 156 ILE A CA 1 ATOM 1232 C C . ILE A 1 158 ? -19.469 17.934 12.132 1.00 20.26 ? 156 ILE A C 1 ATOM 1233 O O . ILE A 1 158 ? -18.244 17.838 12.190 1.00 20.60 ? 156 ILE A O 1 ATOM 1234 C CB . ILE A 1 158 ? -20.903 15.902 11.270 1.00 19.31 ? 156 ILE A CB 1 ATOM 1235 C CG1 . ILE A 1 158 ? -21.253 14.426 11.618 1.00 19.46 ? 156 ILE A CG1 1 ATOM 1236 C CG2 . ILE A 1 158 ? -20.054 16.010 9.991 1.00 20.03 ? 156 ILE A CG2 1 ATOM 1237 C CD1 . ILE A 1 158 ? -20.058 13.469 12.022 1.00 22.47 ? 156 ILE A CD1 1 ATOM 1238 N N . PRO A 1 159 ? -20.074 19.105 11.786 1.00 16.19 ? 157 PRO A N 1 ATOM 1239 C CA . PRO A 1 159 ? -19.253 20.285 11.450 1.00 15.88 ? 157 PRO A CA 1 ATOM 1240 C C . PRO A 1 159 ? -18.330 20.752 12.572 1.00 20.16 ? 157 PRO A C 1 ATOM 1241 O O . PRO A 1 159 ? -17.197 21.129 12.277 1.00 19.81 ? 157 PRO A O 1 ATOM 1242 C CB . PRO A 1 159 ? -20.289 21.349 11.076 1.00 17.59 ? 157 PRO A CB 1 ATOM 1243 C CG . PRO A 1 159 ? -21.506 20.584 10.721 1.00 21.90 ? 157 PRO A CG 1 ATOM 1244 C CD . PRO A 1 159 ? -21.510 19.421 11.650 1.00 17.58 ? 157 PRO A CD 1 ATOM 1245 N N . THR A 1 160 ? -18.792 20.695 13.846 1.00 16.70 ? 158 THR A N 1 ATOM 1246 C CA . THR A 1 160 ? -17.981 21.069 15.013 1.00 16.51 ? 158 THR A CA 1 ATOM 1247 C C . THR A 1 160 ? -16.805 20.102 15.170 1.00 20.27 ? 158 THR A C 1 ATOM 1248 O O . THR A 1 160 ? -15.686 20.546 15.431 1.00 19.87 ? 158 THR A O 1 ATOM 1249 C CB . THR A 1 160 ? -18.825 21.188 16.299 1.00 23.52 ? 158 THR A CB 1 ATOM 1250 O OG1 . THR A 1 160 ? -19.525 19.968 16.541 1.00 23.08 ? 158 THR A OG1 1 ATOM 1251 C CG2 . THR A 1 160 ? -19.791 22.363 16.267 1.00 21.91 ? 158 THR A CG2 1 ATOM 1252 N N . LEU A 1 161 ? -17.049 18.788 14.962 1.00 16.61 ? 159 LEU A N 1 ATOM 1253 C CA . LEU A 1 161 ? -16.007 17.761 15.023 1.00 16.34 ? 159 LEU A CA 1 ATOM 1254 C C . LEU A 1 161 ? -15.014 17.942 13.872 1.00 20.91 ? 159 LEU A C 1 ATOM 1255 O O . LEU A 1 161 ? -13.805 17.873 14.101 1.00 20.72 ? 159 LEU A O 1 ATOM 1256 C CB . LEU A 1 161 ? -16.621 16.344 15.008 1.00 16.29 ? 159 LEU A CB 1 ATOM 1257 C CG . LEU A 1 161 ? -15.665 15.142 14.937 1.00 20.57 ? 159 LEU A CG 1 ATOM 1258 C CD1 . LEU A 1 161 ? -14.748 15.087 16.139 1.00 20.78 ? 159 LEU A CD1 1 ATOM 1259 C CD2 . LEU A 1 161 ? -16.434 13.849 14.837 1.00 21.65 ? 159 LEU A CD2 1 ATOM 1260 N N . ALA A 1 162 ? -15.529 18.206 12.650 1.00 17.75 ? 160 ALA A N 1 ATOM 1261 C CA . ALA A 1 162 ? -14.734 18.421 11.438 1.00 17.92 ? 160 ALA A CA 1 ATOM 1262 C C . ALA A 1 162 ? -13.780 19.614 11.558 1.00 22.27 ? 160 ALA A C 1 ATOM 1263 O O . ALA A 1 162 ? -12.682 19.567 10.995 1.00 21.90 ? 160 ALA A O 1 ATOM 1264 C CB . ALA A 1 162 ? -15.645 18.581 10.234 1.00 18.67 ? 160 ALA A CB 1 ATOM 1265 N N . VAL A 1 163 ? -14.186 20.662 12.316 1.00 18.80 ? 161 VAL A N 1 ATOM 1266 C CA . VAL A 1 163 ? -13.385 21.863 12.596 1.00 18.59 ? 161 VAL A CA 1 ATOM 1267 C C . VAL A 1 163 ? -12.148 21.461 13.428 1.00 22.31 ? 161 VAL A C 1 ATOM 1268 O O . VAL A 1 163 ? -11.047 21.952 13.167 1.00 22.22 ? 161 VAL A O 1 ATOM 1269 C CB . VAL A 1 163 ? -14.249 22.989 13.248 1.00 22.57 ? 161 VAL A CB 1 ATOM 1270 C CG1 . VAL A 1 163 ? -13.400 24.015 14.000 1.00 22.52 ? 161 VAL A CG1 1 ATOM 1271 C CG2 . VAL A 1 163 ? -15.116 23.686 12.203 1.00 22.32 ? 161 VAL A CG2 1 ATOM 1272 N N . LEU A 1 164 ? -12.323 20.524 14.380 1.00 18.50 ? 162 LEU A N 1 ATOM 1273 C CA . LEU A 1 164 ? -11.225 20.012 15.206 1.00 18.27 ? 162 LEU A CA 1 ATOM 1274 C C . LEU A 1 164 ? -10.333 19.060 14.408 1.00 23.18 ? 162 LEU A C 1 ATOM 1275 O O . LEU A 1 164 ? -9.110 19.141 14.525 1.00 23.18 ? 162 LEU A O 1 ATOM 1276 C CB . LEU A 1 164 ? -11.741 19.312 16.477 1.00 18.20 ? 162 LEU A CB 1 ATOM 1277 C CG . LEU A 1 164 ? -12.604 20.131 17.453 1.00 22.67 ? 162 LEU A CG 1 ATOM 1278 C CD1 . LEU A 1 164 ? -13.087 19.261 18.582 1.00 22.64 ? 162 LEU A CD1 1 ATOM 1279 C CD2 . LEU A 1 164 ? -11.842 21.328 18.026 1.00 25.27 ? 162 LEU A CD2 1 ATOM 1280 N N . VAL A 1 165 ? -10.945 18.166 13.596 1.00 20.51 ? 163 VAL A N 1 ATOM 1281 C CA . VAL A 1 165 ? -10.248 17.181 12.757 1.00 20.91 ? 163 VAL A CA 1 ATOM 1282 C C . VAL A 1 165 ? -9.347 17.875 11.716 1.00 26.50 ? 163 VAL A C 1 ATOM 1283 O O . VAL A 1 165 ? -8.208 17.443 11.521 1.00 26.44 ? 163 VAL A O 1 ATOM 1284 C CB . VAL A 1 165 ? -11.223 16.126 12.142 1.00 24.45 ? 163 VAL A CB 1 ATOM 1285 C CG1 . VAL A 1 165 ? -10.529 15.229 11.117 1.00 24.15 ? 163 VAL A CG1 1 ATOM 1286 C CG2 . VAL A 1 165 ? -11.868 15.275 13.232 1.00 24.19 ? 163 VAL A CG2 1 ATOM 1287 N N . MET A 1 166 ? -9.831 18.983 11.109 1.00 24.29 ? 164 MET A N 1 ATOM 1288 C CA . MET A 1 166 ? -9.081 19.762 10.113 1.00 24.74 ? 164 MET A CA 1 ATOM 1289 C C . MET A 1 166 ? -7.767 20.365 10.658 1.00 29.24 ? 164 MET A C 1 ATOM 1290 O O . MET A 1 166 ? -6.847 20.631 9.881 1.00 28.80 ? 164 MET A O 1 ATOM 1291 C CB . MET A 1 166 ? -9.984 20.795 9.397 1.00 27.22 ? 164 MET A CB 1 ATOM 1292 C CG . MET A 1 166 ? -9.978 22.195 9.994 1.00 31.15 ? 164 MET A CG 1 ATOM 1293 S SD . MET A 1 166 ? -11.052 23.361 9.109 1.00 35.66 ? 164 MET A SD 1 ATOM 1294 C CE . MET A 1 166 ? -10.088 23.663 7.645 1.00 32.33 ? 164 MET A CE 1 ATOM 1295 N N . GLN A 1 167 ? -7.685 20.545 11.992 1.00 26.03 ? 165 GLN A N 1 ATOM 1296 C CA . GLN A 1 167 ? -6.513 21.066 12.702 1.00 26.23 ? 165 GLN A CA 1 ATOM 1297 C C . GLN A 1 167 ? -5.486 19.952 12.981 1.00 30.61 ? 165 GLN A C 1 ATOM 1298 O O . GLN A 1 167 ? -4.348 20.255 13.347 1.00 30.58 ? 165 GLN A O 1 ATOM 1299 C CB . GLN A 1 167 ? -6.935 21.742 14.022 1.00 27.53 ? 165 GLN A CB 1 ATOM 1300 C CG . GLN A 1 167 ? -7.761 23.013 13.844 1.00 40.76 ? 165 GLN A CG 1 ATOM 1301 C CD . GLN A 1 167 ? -8.179 23.592 15.173 1.00 63.47 ? 165 GLN A CD 1 ATOM 1302 O OE1 . GLN A 1 167 ? -7.374 24.170 15.911 1.00 60.41 ? 165 GLN A OE1 1 ATOM 1303 N NE2 . GLN A 1 167 ? -9.455 23.459 15.503 1.00 55.79 ? 165 GLN A NE2 1 ATOM 1304 N N . ASP A 1 168 ? -5.891 18.671 12.818 1.00 27.02 ? 166 ASP A N 1 ATOM 1305 C CA . ASP A 1 168 ? -5.040 17.499 13.032 1.00 26.77 ? 166 ASP A CA 1 ATOM 1306 C C . ASP A 1 168 ? -4.526 16.961 11.677 1.00 31.76 ? 166 ASP A C 1 ATOM 1307 O O . ASP A 1 168 ? -5.296 16.337 10.939 1.00 31.38 ? 166 ASP A O 1 ATOM 1308 C CB . ASP A 1 168 ? -5.802 16.413 13.825 1.00 28.25 ? 166 ASP A CB 1 ATOM 1309 C CG . ASP A 1 168 ? -4.969 15.275 14.405 1.00 34.99 ? 166 ASP A CG 1 ATOM 1310 O OD1 . ASP A 1 168 ? -3.790 15.129 14.008 1.00 34.97 ? 166 ASP A OD1 1 ATOM 1311 O OD2 . ASP A 1 168 ? -5.503 14.519 15.242 1.00 39.67 ? 166 ASP A OD2 1 ATOM 1312 N N . PRO A 1 169 ? -3.230 17.189 11.332 1.00 29.02 ? 167 PRO A N 1 ATOM 1313 C CA . PRO A 1 169 ? -2.721 16.711 10.030 1.00 28.77 ? 167 PRO A CA 1 ATOM 1314 C C . PRO A 1 169 ? -2.576 15.194 9.882 1.00 31.83 ? 167 PRO A C 1 ATOM 1315 O O . PRO A 1 169 ? -2.527 14.707 8.751 1.00 31.82 ? 167 PRO A O 1 ATOM 1316 C CB . PRO A 1 169 ? -1.387 17.444 9.874 1.00 30.64 ? 167 PRO A CB 1 ATOM 1317 C CG . PRO A 1 169 ? -0.948 17.726 11.261 1.00 35.17 ? 167 PRO A CG 1 ATOM 1318 C CD . PRO A 1 169 ? -2.191 17.930 12.078 1.00 30.68 ? 167 PRO A CD 1 ATOM 1319 N N . SER A 1 170 ? -2.527 14.448 11.006 1.00 27.42 ? 168 SER A N 1 ATOM 1320 C CA . SER A 1 170 ? -2.415 12.984 11.000 1.00 26.61 ? 168 SER A CA 1 ATOM 1321 C C . SER A 1 170 ? -3.706 12.315 10.498 1.00 28.53 ? 168 SER A C 1 ATOM 1322 O O . SER A 1 170 ? -3.663 11.175 10.028 1.00 28.25 ? 168 SER A O 1 ATOM 1323 C CB . SER A 1 170 ? -2.038 12.461 12.383 1.00 30.40 ? 168 SER A CB 1 ATOM 1324 O OG . SER A 1 170 ? -3.087 12.638 13.319 1.00 40.06 ? 168 SER A OG 1 ATOM 1325 N N . MET A 1 171 ? -4.846 13.030 10.592 1.00 23.26 ? 169 MET A N 1 ATOM 1326 C CA . MET A 1 171 ? -6.147 12.544 10.133 1.00 22.13 ? 169 MET A CA 1 ATOM 1327 C C . MET A 1 171 ? -6.372 12.965 8.689 1.00 24.79 ? 169 MET A C 1 ATOM 1328 O O . MET A 1 171 ? -6.351 14.160 8.378 1.00 24.14 ? 169 MET A O 1 ATOM 1329 C CB . MET A 1 171 ? -7.284 13.034 11.047 1.00 24.10 ? 169 MET A CB 1 ATOM 1330 C CG . MET A 1 171 ? -7.273 12.378 12.404 1.00 27.20 ? 169 MET A CG 1 ATOM 1331 S SD . MET A 1 171 ? -8.719 12.796 13.392 1.00 30.83 ? 169 MET A SD 1 ATOM 1332 C CE . MET A 1 171 ? -8.229 12.142 14.940 1.00 27.39 ? 169 MET A CE 1 ATOM 1333 N N . ASN A 1 172 ? -6.552 11.977 7.800 1.00 20.80 ? 170 ASN A N 1 ATOM 1334 C CA . ASN A 1 172 ? -6.753 12.203 6.373 1.00 20.41 ? 170 ASN A CA 1 ATOM 1335 C C . ASN A 1 172 ? -8.223 12.528 6.065 1.00 23.98 ? 170 ASN A C 1 ATOM 1336 O O . ASN A 1 172 ? -8.916 11.749 5.406 1.00 23.51 ? 170 ASN A O 1 ATOM 1337 C CB . ASN A 1 172 ? -6.212 11.012 5.551 1.00 19.93 ? 170 ASN A CB 1 ATOM 1338 C CG . ASN A 1 172 ? -6.210 11.206 4.048 1.00 34.96 ? 170 ASN A CG 1 ATOM 1339 O OD1 . ASN A 1 172 ? -6.265 12.327 3.526 1.00 26.03 ? 170 ASN A OD1 1 ATOM 1340 N ND2 . ASN A 1 172 ? -6.151 10.104 3.316 1.00 26.18 ? 170 ASN A ND2 1 ATOM 1341 N N . LEU A 1 173 ? -8.693 13.690 6.559 1.00 20.88 ? 171 LEU A N 1 ATOM 1342 C CA . LEU A 1 173 ? -10.063 14.163 6.354 1.00 20.60 ? 171 LEU A CA 1 ATOM 1343 C C . LEU A 1 173 ? -10.269 14.533 4.891 1.00 24.54 ? 171 LEU A C 1 ATOM 1344 O O . LEU A 1 173 ? -9.465 15.270 4.317 1.00 24.66 ? 171 LEU A O 1 ATOM 1345 C CB . LEU A 1 173 ? -10.391 15.347 7.289 1.00 20.58 ? 171 LEU A CB 1 ATOM 1346 C CG . LEU A 1 173 ? -11.830 15.890 7.265 1.00 24.93 ? 171 LEU A CG 1 ATOM 1347 C CD1 . LEU A 1 173 ? -12.834 14.859 7.764 1.00 24.69 ? 171 LEU A CD1 1 ATOM 1348 C CD2 . LEU A 1 173 ? -11.943 17.161 8.080 1.00 27.15 ? 171 LEU A CD2 1 ATOM 1349 N N . GLN A 1 174 ? -11.320 13.975 4.281 1.00 20.75 ? 172 GLN A N 1 ATOM 1350 C CA . GLN A 1 174 ? -11.635 14.195 2.873 1.00 20.12 ? 172 GLN A CA 1 ATOM 1351 C C . GLN A 1 174 ? -13.005 14.822 2.656 1.00 23.63 ? 172 GLN A C 1 ATOM 1352 O O . GLN A 1 174 ? -13.240 15.430 1.613 1.00 23.19 ? 172 GLN A O 1 ATOM 1353 C CB . GLN A 1 174 ? -11.485 12.889 2.072 1.00 21.26 ? 172 GLN A CB 1 ATOM 1354 C CG . GLN A 1 174 ? -10.036 12.411 1.912 1.00 31.53 ? 172 GLN A CG 1 ATOM 1355 C CD . GLN A 1 174 ? -9.146 13.376 1.154 1.00 43.98 ? 172 GLN A CD 1 ATOM 1356 O OE1 . GLN A 1 174 ? -9.523 13.940 0.120 1.00 36.91 ? 172 GLN A OE1 1 ATOM 1357 N NE2 . GLN A 1 174 ? -7.936 13.578 1.655 1.00 33.77 ? 172 GLN A NE2 1 ATOM 1358 N N . GLY A 1 175 ? -13.892 14.683 3.636 1.00 20.03 ? 173 GLY A N 1 ATOM 1359 C CA . GLY A 1 175 ? -15.227 15.253 3.539 1.00 19.53 ? 173 GLY A CA 1 ATOM 1360 C C . GLY A 1 175 ? -16.179 14.944 4.670 1.00 22.50 ? 173 GLY A C 1 ATOM 1361 O O . GLY A 1 175 ? -15.837 14.230 5.616 1.00 21.93 ? 173 GLY A O 1 ATOM 1362 N N . LEU A 1 176 ? -17.392 15.505 4.561 1.00 18.48 ? 174 LEU A N 1 ATOM 1363 C CA . LEU A 1 176 ? -18.472 15.358 5.530 1.00 18.10 ? 174 LEU A CA 1 ATOM 1364 C C . LEU A 1 176 ? -19.846 15.341 4.868 1.00 20.19 ? 174 LEU A C 1 ATOM 1365 O O . LEU A 1 176 ? -20.074 16.068 3.901 1.00 19.56 ? 174 LEU A O 1 ATOM 1366 C CB . LEU A 1 176 ? -18.405 16.424 6.650 1.00 18.34 ? 174 LEU A CB 1 ATOM 1367 C CG . LEU A 1 176 ? -18.178 17.883 6.247 1.00 23.24 ? 174 LEU A CG 1 ATOM 1368 C CD1 . LEU A 1 176 ? -19.007 18.817 7.103 1.00 26.28 ? 174 LEU A CD1 1 ATOM 1369 C CD2 . LEU A 1 176 ? -16.704 18.263 6.374 1.00 23.37 ? 174 LEU A CD2 1 ATOM 1370 N N . ALA A 1 177 ? -20.749 14.490 5.379 1.00 15.84 ? 175 ALA A N 1 ATOM 1371 C CA . ALA A 1 177 ? -22.123 14.364 4.889 1.00 15.01 ? 175 ALA A CA 1 ATOM 1372 C C . ALA A 1 177 ? -23.103 14.411 6.057 1.00 18.00 ? 175 ALA A C 1 ATOM 1373 O O . ALA A 1 177 ? -22.881 13.758 7.075 1.00 16.78 ? 175 ALA A O 1 ATOM 1374 C CB . ALA A 1 177 ? -22.299 13.082 4.092 1.00 15.60 ? 175 ALA A CB 1 ATOM 1375 N N . VAL A 1 178 ? -24.158 15.226 5.931 1.00 14.68 ? 176 VAL A N 1 ATOM 1376 C CA . VAL A 1 178 ? -25.165 15.390 6.982 1.00 14.49 ? 176 VAL A CA 1 ATOM 1377 C C . VAL A 1 178 ? -26.564 15.093 6.420 1.00 18.09 ? 176 VAL A C 1 ATOM 1378 O O . VAL A 1 178 ? -26.993 15.738 5.461 1.00 17.80 ? 176 VAL A O 1 ATOM 1379 C CB . VAL A 1 178 ? -25.059 16.789 7.662 1.00 18.62 ? 176 VAL A CB 1 ATOM 1380 C CG1 . VAL A 1 178 ? -26.254 17.059 8.564 1.00 18.60 ? 176 VAL A CG1 1 ATOM 1381 C CG2 . VAL A 1 178 ? -23.759 16.929 8.454 1.00 18.39 ? 176 VAL A CG2 1 ATOM 1382 N N . GLY A 1 179 ? -27.245 14.119 7.026 1.00 14.41 ? 177 GLY A N 1 ATOM 1383 C CA . GLY A 1 179 ? -28.585 13.696 6.637 1.00 13.81 ? 177 GLY A CA 1 ATOM 1384 C C . GLY A 1 179 ? -29.675 14.307 7.486 1.00 17.29 ? 177 GLY A C 1 ATOM 1385 O O . GLY A 1 179 ? -29.696 14.085 8.698 1.00 16.63 ? 177 GLY A O 1 ATOM 1386 N N . ASN A 1 180 ? -30.596 15.080 6.853 1.00 13.69 ? 178 ASN A N 1 ATOM 1387 C CA . ASN A 1 180 ? -31.709 15.781 7.515 1.00 13.62 ? 178 ASN A CA 1 ATOM 1388 C C . ASN A 1 180 ? -31.206 16.423 8.808 1.00 18.57 ? 178 ASN A C 1 ATOM 1389 O O . ASN A 1 180 ? -31.688 16.113 9.898 1.00 18.07 ? 178 ASN A O 1 ATOM 1390 C CB . ASN A 1 180 ? -32.884 14.828 7.766 1.00 12.96 ? 178 ASN A CB 1 ATOM 1391 C CG . ASN A 1 180 ? -33.620 14.468 6.509 1.00 25.81 ? 178 ASN A CG 1 ATOM 1392 O OD1 . ASN A 1 180 ? -33.229 13.560 5.769 1.00 18.40 ? 178 ASN A OD1 1 ATOM 1393 N ND2 . ASN A 1 180 ? -34.683 15.198 6.222 1.00 13.74 ? 178 ASN A ND2 1 ATOM 1394 N N . GLY A 1 181 ? -30.165 17.232 8.667 1.00 15.92 ? 179 GLY A N 1 ATOM 1395 C CA . GLY A 1 181 ? -29.474 17.832 9.793 1.00 16.56 ? 179 GLY A CA 1 ATOM 1396 C C . GLY A 1 181 ? -29.931 19.197 10.234 1.00 21.59 ? 179 GLY A C 1 ATOM 1397 O O . GLY A 1 181 ? -30.466 19.980 9.448 1.00 21.03 ? 179 GLY A O 1 ATOM 1398 N N . LEU A 1 182 ? -29.696 19.478 11.515 1.00 19.41 ? 180 LEU A N 1 ATOM 1399 C CA . LEU A 1 182 ? -29.988 20.763 12.117 1.00 19.73 ? 180 LEU A CA 1 ATOM 1400 C C . LEU A 1 182 ? -28.756 21.636 11.864 1.00 23.26 ? 180 LEU A C 1 ATOM 1401 O O . LEU A 1 182 ? -27.701 21.413 12.462 1.00 23.00 ? 180 LEU A O 1 ATOM 1402 C CB . LEU A 1 182 ? -30.272 20.576 13.620 1.00 20.09 ? 180 LEU A CB 1 ATOM 1403 C CG . LEU A 1 182 ? -30.617 21.814 14.454 1.00 25.41 ? 180 LEU A CG 1 ATOM 1404 C CD1 . LEU A 1 182 ? -31.933 22.456 14.005 1.00 25.82 ? 180 LEU A CD1 1 ATOM 1405 C CD2 . LEU A 1 182 ? -30.719 21.442 15.911 1.00 28.36 ? 180 LEU A CD2 1 ATOM 1406 N N . SER A 1 183 ? -28.876 22.571 10.912 1.00 19.51 ? 181 SER A N 1 ATOM 1407 C CA . SER A 1 183 ? -27.800 23.485 10.528 1.00 19.32 ? 181 SER A CA 1 ATOM 1408 C C . SER A 1 183 ? -28.042 24.888 11.077 1.00 23.89 ? 181 SER A C 1 ATOM 1409 O O . SER A 1 183 ? -27.087 25.595 11.394 1.00 23.47 ? 181 SER A O 1 ATOM 1410 C CB . SER A 1 183 ? -27.663 23.536 9.010 1.00 22.15 ? 181 SER A CB 1 ATOM 1411 O OG . SER A 1 183 ? -27.285 22.277 8.478 1.00 27.96 ? 181 SER A OG 1 ATOM 1412 N N . SER A 1 184 ? -29.319 25.295 11.161 1.00 20.73 ? 182 SER A N 1 ATOM 1413 C CA . SER A 1 184 ? -29.746 26.601 11.658 1.00 20.63 ? 182 SER A CA 1 ATOM 1414 C C . SER A 1 184 ? -31.165 26.498 12.192 1.00 24.49 ? 182 SER A C 1 ATOM 1415 O O . SER A 1 184 ? -32.058 26.050 11.471 1.00 23.79 ? 182 SER A O 1 ATOM 1416 C CB . SER A 1 184 ? -29.670 27.650 10.548 1.00 23.63 ? 182 SER A CB 1 ATOM 1417 O OG . SER A 1 184 ? -30.317 28.862 10.903 1.00 29.38 ? 182 SER A OG 1 ATOM 1418 N N . TYR A 1 185 ? -31.369 26.912 13.454 1.00 21.35 ? 183 TYR A N 1 ATOM 1419 C CA . TYR A 1 185 ? -32.678 26.912 14.106 1.00 21.34 ? 183 TYR A CA 1 ATOM 1420 C C . TYR A 1 185 ? -33.637 27.865 13.397 1.00 25.19 ? 183 TYR A C 1 ATOM 1421 O O . TYR A 1 185 ? -34.788 27.500 13.177 1.00 24.74 ? 183 TYR A O 1 ATOM 1422 C CB . TYR A 1 185 ? -32.552 27.283 15.590 1.00 22.56 ? 183 TYR A CB 1 ATOM 1423 C CG . TYR A 1 185 ? -31.928 26.198 16.437 1.00 23.93 ? 183 TYR A CG 1 ATOM 1424 C CD1 . TYR A 1 185 ? -30.553 26.149 16.637 1.00 24.55 ? 183 TYR A CD1 1 ATOM 1425 C CD2 . TYR A 1 185 ? -32.715 25.240 17.069 1.00 25.96 ? 183 TYR A CD2 1 ATOM 1426 C CE1 . TYR A 1 185 ? -29.971 25.160 17.428 1.00 25.45 ? 183 TYR A CE1 1 ATOM 1427 C CE2 . TYR A 1 185 ? -32.145 24.245 17.863 1.00 26.58 ? 183 TYR A CE2 1 ATOM 1428 C CZ . TYR A 1 185 ? -30.772 24.214 18.044 1.00 31.70 ? 183 TYR A CZ 1 ATOM 1429 O OH . TYR A 1 185 ? -30.200 23.230 18.813 1.00 32.03 ? 183 TYR A OH 1 ATOM 1430 N N . GLU A 1 186 ? -33.145 29.056 12.993 1.00 21.70 ? 184 GLU A N 1 ATOM 1431 C CA . GLU A 1 186 ? -33.915 30.085 12.287 1.00 21.27 ? 184 GLU A CA 1 ATOM 1432 C C . GLU A 1 186 ? -34.372 29.620 10.905 1.00 24.68 ? 184 GLU A C 1 ATOM 1433 O O . GLU A 1 186 ? -35.542 29.804 10.565 1.00 24.20 ? 184 GLU A O 1 ATOM 1434 C CB . GLU A 1 186 ? -33.117 31.398 12.195 1.00 22.48 ? 184 GLU A CB 1 ATOM 1435 C CG . GLU A 1 186 ? -33.921 32.571 11.656 1.00 31.08 ? 184 GLU A CG 1 ATOM 1436 C CD . GLU A 1 186 ? -33.196 33.899 11.552 1.00 47.02 ? 184 GLU A CD 1 ATOM 1437 O OE1 . GLU A 1 186 ? -32.216 34.114 12.301 1.00 38.46 ? 184 GLU A OE1 1 ATOM 1438 O OE2 . GLU A 1 186 ? -33.633 34.740 10.735 1.00 41.98 ? 184 GLU A OE2 1 ATOM 1439 N N . GLN A 1 187 ? -33.458 29.023 10.117 1.00 20.95 ? 185 GLN A N 1 ATOM 1440 C CA . GLN A 1 187 ? -33.761 28.514 8.779 1.00 20.65 ? 185 GLN A CA 1 ATOM 1441 C C . GLN A 1 187 ? -34.730 27.330 8.862 1.00 23.71 ? 185 GLN A C 1 ATOM 1442 O O . GLN A 1 187 ? -35.639 27.241 8.042 1.00 23.16 ? 185 GLN A O 1 ATOM 1443 C CB . GLN A 1 187 ? -32.479 28.138 8.013 1.00 22.12 ? 185 GLN A CB 1 ATOM 1444 C CG . GLN A 1 187 ? -31.523 29.311 7.763 1.00 38.34 ? 185 GLN A CG 1 ATOM 1445 C CD . GLN A 1 187 ? -31.729 29.994 6.435 1.00 57.77 ? 185 GLN A CD 1 ATOM 1446 O OE1 . GLN A 1 187 ? -32.800 30.534 6.137 1.00 54.53 ? 185 GLN A OE1 1 ATOM 1447 N NE2 . GLN A 1 187 ? -30.681 30.037 5.629 1.00 48.91 ? 185 GLN A NE2 1 ATOM 1448 N N . ASN A 1 188 ? -34.568 26.461 9.884 1.00 20.25 ? 186 ASN A N 1 ATOM 1449 C CA . ASN A 1 188 ? -35.428 25.295 10.116 1.00 20.06 ? 186 ASN A CA 1 ATOM 1450 C C . ASN A 1 188 ? -36.848 25.700 10.534 1.00 23.98 ? 186 ASN A C 1 ATOM 1451 O O . ASN A 1 188 ? -37.809 25.179 9.970 1.00 22.73 ? 186 ASN A O 1 ATOM 1452 C CB . ASN A 1 188 ? -34.806 24.344 11.154 1.00 19.65 ? 186 ASN A CB 1 ATOM 1453 C CG . ASN A 1 188 ? -35.577 23.063 11.393 1.00 36.77 ? 186 ASN A CG 1 ATOM 1454 O OD1 . ASN A 1 188 ? -35.949 22.735 12.523 1.00 32.69 ? 186 ASN A OD1 1 ATOM 1455 N ND2 . ASN A 1 188 ? -35.829 22.302 10.342 1.00 24.33 ? 186 ASN A ND2 1 ATOM 1456 N N . ASP A 1 189 ? -36.973 26.625 11.514 1.00 21.53 ? 187 ASP A N 1 ATOM 1457 C CA . ASP A 1 189 ? -38.259 27.108 12.035 1.00 21.56 ? 187 ASP A CA 1 ATOM 1458 C C . ASP A 1 189 ? -39.079 27.869 11.000 1.00 25.68 ? 187 ASP A C 1 ATOM 1459 O O . ASP A 1 189 ? -40.290 27.657 10.921 1.00 25.89 ? 187 ASP A O 1 ATOM 1460 C CB . ASP A 1 189 ? -38.068 27.951 13.310 1.00 23.37 ? 187 ASP A CB 1 ATOM 1461 C CG . ASP A 1 189 ? -37.544 27.194 14.520 1.00 31.72 ? 187 ASP A CG 1 ATOM 1462 O OD1 . ASP A 1 189 ? -37.294 25.974 14.400 1.00 31.90 ? 187 ASP A OD1 1 ATOM 1463 O OD2 . ASP A 1 189 ? -37.354 27.829 15.578 1.00 38.03 ? 187 ASP A OD2 1 ATOM 1464 N N . ASN A 1 190 ? -38.426 28.742 10.204 1.00 21.70 ? 188 ASN A N 1 ATOM 1465 C CA . ASN A 1 190 ? -39.088 29.529 9.164 1.00 21.26 ? 188 ASN A CA 1 ATOM 1466 C C . ASN A 1 190 ? -39.591 28.656 8.022 1.00 24.88 ? 188 ASN A C 1 ATOM 1467 O O . ASN A 1 190 ? -40.748 28.793 7.624 1.00 24.91 ? 188 ASN A O 1 ATOM 1468 C CB . ASN A 1 190 ? -38.182 30.650 8.646 1.00 21.46 ? 188 ASN A CB 1 ATOM 1469 C CG . ASN A 1 190 ? -38.017 31.812 9.598 1.00 36.94 ? 188 ASN A CG 1 ATOM 1470 O OD1 . ASN A 1 190 ? -38.886 32.116 10.423 1.00 29.59 ? 188 ASN A OD1 1 ATOM 1471 N ND2 . ASN A 1 190 ? -36.909 32.520 9.476 1.00 27.35 ? 188 ASN A ND2 1 ATOM 1472 N N . SER A 1 191 ? -38.742 27.734 7.528 1.00 20.55 ? 189 SER A N 1 ATOM 1473 C CA . SER A 1 191 ? -39.080 26.813 6.439 1.00 19.79 ? 189 SER A CA 1 ATOM 1474 C C . SER A 1 191 ? -40.185 25.818 6.814 1.00 23.06 ? 189 SER A C 1 ATOM 1475 O O . SER A 1 191 ? -40.995 25.482 5.953 1.00 22.57 ? 189 SER A O 1 ATOM 1476 C CB . SER A 1 191 ? -37.841 26.063 5.964 1.00 22.16 ? 189 SER A CB 1 ATOM 1477 O OG . SER A 1 191 ? -37.267 25.311 7.019 1.00 26.85 ? 189 SER A OG 1 ATOM 1478 N N . LEU A 1 192 ? -40.214 25.352 8.085 1.00 19.53 ? 190 LEU A N 1 ATOM 1479 C CA . LEU A 1 192 ? -41.214 24.391 8.582 1.00 19.54 ? 190 LEU A CA 1 ATOM 1480 C C . LEU A 1 192 ? -42.646 24.935 8.530 1.00 23.60 ? 190 LEU A C 1 ATOM 1481 O O . LEU A 1 192 ? -43.558 24.193 8.163 1.00 22.99 ? 190 LEU A O 1 ATOM 1482 C CB . LEU A 1 192 ? -40.855 23.873 9.995 1.00 19.56 ? 190 LEU A CB 1 ATOM 1483 C CG . LEU A 1 192 ? -41.837 22.910 10.701 1.00 24.16 ? 190 LEU A CG 1 ATOM 1484 C CD1 . LEU A 1 192 ? -42.096 21.643 9.878 1.00 24.32 ? 190 LEU A CD1 1 ATOM 1485 C CD2 . LEU A 1 192 ? -41.336 22.538 12.077 1.00 26.14 ? 190 LEU A CD2 1 ATOM 1486 N N . VAL A 1 193 ? -42.841 26.219 8.886 1.00 20.44 ? 191 VAL A N 1 ATOM 1487 C CA . VAL A 1 193 ? -44.159 26.871 8.858 1.00 20.32 ? 191 VAL A CA 1 ATOM 1488 C C . VAL A 1 193 ? -44.662 26.904 7.410 1.00 23.27 ? 191 VAL A C 1 ATOM 1489 O O . VAL A 1 193 ? -45.820 26.560 7.165 1.00 22.98 ? 191 VAL A O 1 ATOM 1490 C CB . VAL A 1 193 ? -44.143 28.265 9.541 1.00 24.39 ? 191 VAL A CB 1 ATOM 1491 C CG1 . VAL A 1 193 ? -45.516 28.937 9.488 1.00 24.33 ? 191 VAL A CG1 1 ATOM 1492 C CG2 . VAL A 1 193 ? -43.667 28.151 10.984 1.00 24.14 ? 191 VAL A CG2 1 ATOM 1493 N N . TYR A 1 194 ? -43.762 27.238 6.456 1.00 19.35 ? 192 TYR A N 1 ATOM 1494 C CA . TYR A 1 194 ? -44.043 27.234 5.020 1.00 19.13 ? 192 TYR A CA 1 ATOM 1495 C C . TYR A 1 194 ? -44.333 25.792 4.574 1.00 22.19 ? 192 TYR A C 1 ATOM 1496 O O . TYR A 1 194 ? -45.288 25.572 3.830 1.00 21.54 ? 192 TYR A O 1 ATOM 1497 C CB . TYR A 1 194 ? -42.851 27.795 4.221 1.00 20.69 ? 192 TYR A CB 1 ATOM 1498 C CG . TYR A 1 194 ? -42.773 29.306 4.163 1.00 23.11 ? 192 TYR A CG 1 ATOM 1499 C CD1 . TYR A 1 194 ? -43.578 30.034 3.292 1.00 24.02 ? 192 TYR A CD1 1 ATOM 1500 C CD2 . TYR A 1 194 ? -41.846 30.005 4.931 1.00 25.32 ? 192 TYR A CD2 1 ATOM 1501 C CE1 . TYR A 1 194 ? -43.492 31.423 3.217 1.00 25.09 ? 192 TYR A CE1 1 ATOM 1502 C CE2 . TYR A 1 194 ? -41.749 31.394 4.863 1.00 26.48 ? 192 TYR A CE2 1 ATOM 1503 C CZ . TYR A 1 194 ? -42.578 32.100 4.007 1.00 32.94 ? 192 TYR A CZ 1 ATOM 1504 O OH . TYR A 1 194 ? -42.484 33.467 3.932 1.00 33.73 ? 192 TYR A OH 1 ATOM 1505 N N . PHE A 1 195 ? -43.525 24.814 5.057 1.00 18.34 ? 193 PHE A N 1 ATOM 1506 C CA . PHE A 1 195 ? -43.680 23.385 4.758 1.00 17.94 ? 193 PHE A CA 1 ATOM 1507 C C . PHE A 1 195 ? -45.062 22.902 5.204 1.00 21.39 ? 193 PHE A C 1 ATOM 1508 O O . PHE A 1 195 ? -45.749 22.255 4.422 1.00 20.72 ? 193 PHE A O 1 ATOM 1509 C CB . PHE A 1 195 ? -42.568 22.551 5.435 1.00 19.62 ? 193 PHE A CB 1 ATOM 1510 C CG . PHE A 1 195 ? -42.495 21.091 5.039 1.00 20.98 ? 193 PHE A CG 1 ATOM 1511 C CD1 . PHE A 1 195 ? -43.374 20.158 5.583 1.00 23.83 ? 193 PHE A CD1 1 ATOM 1512 C CD2 . PHE A 1 195 ? -41.518 20.641 4.160 1.00 22.81 ? 193 PHE A CD2 1 ATOM 1513 C CE1 . PHE A 1 195 ? -43.310 18.812 5.211 1.00 24.61 ? 193 PHE A CE1 1 ATOM 1514 C CE2 . PHE A 1 195 ? -41.441 19.289 3.806 1.00 25.61 ? 193 PHE A CE2 1 ATOM 1515 C CZ . PHE A 1 195 ? -42.339 18.385 4.331 1.00 23.67 ? 193 PHE A CZ 1 ATOM 1516 N N . ALA A 1 196 ? -45.468 23.242 6.446 1.00 17.93 ? 194 ALA A N 1 ATOM 1517 C CA . ALA A 1 196 ? -46.750 22.858 7.043 1.00 17.82 ? 194 ALA A CA 1 ATOM 1518 C C . ALA A 1 196 ? -47.963 23.318 6.229 1.00 21.90 ? 194 ALA A C 1 ATOM 1519 O O . ALA A 1 196 ? -48.836 22.499 5.950 1.00 21.08 ? 194 ALA A O 1 ATOM 1520 C CB . ALA A 1 196 ? -46.841 23.373 8.470 1.00 18.54 ? 194 ALA A CB 1 ATOM 1521 N N . TYR A 1 197 ? -48.009 24.605 5.821 1.00 19.37 ? 195 TYR A N 1 ATOM 1522 C CA . TYR A 1 197 ? -49.128 25.120 5.028 1.00 19.38 ? 195 TYR A CA 1 ATOM 1523 C C . TYR A 1 197 ? -49.198 24.507 3.632 1.00 23.43 ? 195 TYR A C 1 ATOM 1524 O O . TYR A 1 197 ? -50.266 24.052 3.224 1.00 23.57 ? 195 TYR A O 1 ATOM 1525 C CB . TYR A 1 197 ? -49.129 26.659 4.951 1.00 20.74 ? 195 TYR A CB 1 ATOM 1526 C CG . TYR A 1 197 ? -50.174 27.214 4.001 1.00 22.55 ? 195 TYR A CG 1 ATOM 1527 C CD1 . TYR A 1 197 ? -51.535 27.073 4.267 1.00 24.55 ? 195 TYR A CD1 1 ATOM 1528 C CD2 . TYR A 1 197 ? -49.804 27.854 2.822 1.00 23.17 ? 195 TYR A CD2 1 ATOM 1529 C CE1 . TYR A 1 197 ? -52.499 27.559 3.385 1.00 25.54 ? 195 TYR A CE1 1 ATOM 1530 C CE2 . TYR A 1 197 ? -50.759 28.348 1.935 1.00 24.00 ? 195 TYR A CE2 1 ATOM 1531 C CZ . TYR A 1 197 ? -52.107 28.201 2.223 1.00 31.59 ? 195 TYR A CZ 1 ATOM 1532 O OH . TYR A 1 197 ? -53.056 28.689 1.358 1.00 32.88 ? 195 TYR A OH 1 ATOM 1533 N N . TYR A 1 198 ? -48.071 24.492 2.905 1.00 19.87 ? 196 TYR A N 1 ATOM 1534 C CA . TYR A 1 198 ? -48.036 23.964 1.544 1.00 19.53 ? 196 TYR A CA 1 ATOM 1535 C C . TYR A 1 198 ? -48.132 22.440 1.413 1.00 22.88 ? 196 TYR A C 1 ATOM 1536 O O . TYR A 1 198 ? -48.305 21.927 0.306 1.00 22.50 ? 196 TYR A O 1 ATOM 1537 C CB . TYR A 1 198 ? -46.924 24.607 0.711 1.00 20.52 ? 196 TYR A CB 1 ATOM 1538 C CG . TYR A 1 198 ? -47.113 26.099 0.522 1.00 22.12 ? 196 TYR A CG 1 ATOM 1539 C CD1 . TYR A 1 198 ? -47.947 26.595 -0.476 1.00 24.01 ? 196 TYR A CD1 1 ATOM 1540 C CD2 . TYR A 1 198 ? -46.471 27.015 1.351 1.00 22.81 ? 196 TYR A CD2 1 ATOM 1541 C CE1 . TYR A 1 198 ? -48.154 27.965 -0.630 1.00 24.84 ? 196 TYR A CE1 1 ATOM 1542 C CE2 . TYR A 1 198 ? -46.654 28.389 1.193 1.00 23.61 ? 196 TYR A CE2 1 ATOM 1543 C CZ . TYR A 1 198 ? -47.495 28.859 0.197 1.00 30.03 ? 196 TYR A CZ 1 ATOM 1544 O OH . TYR A 1 198 ? -47.684 30.210 0.032 1.00 29.37 ? 196 TYR A OH 1 ATOM 1545 N N . HIS A 1 199 ? -48.078 21.724 2.549 1.00 19.36 ? 197 HIS A N 1 ATOM 1546 C CA . HIS A 1 199 ? -48.286 20.281 2.599 1.00 19.18 ? 197 HIS A CA 1 ATOM 1547 C C . HIS A 1 199 ? -49.708 19.968 3.121 1.00 23.87 ? 197 HIS A C 1 ATOM 1548 O O . HIS A 1 199 ? -50.060 18.808 3.329 1.00 23.71 ? 197 HIS A O 1 ATOM 1549 C CB . HIS A 1 199 ? -47.172 19.569 3.380 1.00 19.61 ? 197 HIS A CB 1 ATOM 1550 C CG . HIS A 1 199 ? -45.905 19.432 2.592 1.00 22.59 ? 197 HIS A CG 1 ATOM 1551 N ND1 . HIS A 1 199 ? -45.027 20.492 2.448 1.00 24.10 ? 197 HIS A ND1 1 ATOM 1552 C CD2 . HIS A 1 199 ? -45.420 18.367 1.913 1.00 24.01 ? 197 HIS A CD2 1 ATOM 1553 C CE1 . HIS A 1 199 ? -44.042 20.041 1.688 1.00 23.41 ? 197 HIS A CE1 1 ATOM 1554 N NE2 . HIS A 1 199 ? -44.232 18.766 1.347 1.00 23.73 ? 197 HIS A NE2 1 ATOM 1555 N N . GLY A 1 200 ? -50.515 21.021 3.277 1.00 20.75 ? 198 GLY A N 1 ATOM 1556 C CA . GLY A 1 200 ? -51.916 20.942 3.679 1.00 20.56 ? 198 GLY A CA 1 ATOM 1557 C C . GLY A 1 200 ? -52.223 20.589 5.115 1.00 24.32 ? 198 GLY A C 1 ATOM 1558 O O . GLY A 1 200 ? -53.230 19.925 5.376 1.00 23.80 ? 198 GLY A O 1 ATOM 1559 N N . LEU A 1 201 ? -51.387 21.055 6.058 1.00 20.65 ? 199 LEU A N 1 ATOM 1560 C CA . LEU A 1 201 ? -51.590 20.796 7.486 1.00 20.67 ? 199 LEU A CA 1 ATOM 1561 C C . LEU A 1 201 ? -52.295 21.966 8.154 1.00 25.28 ? 199 LEU A C 1 ATOM 1562 O O . LEU A 1 201 ? -52.979 21.777 9.158 1.00 24.46 ? 199 LEU A O 1 ATOM 1563 C CB . LEU A 1 201 ? -50.268 20.484 8.214 1.00 20.65 ? 199 LEU A CB 1 ATOM 1564 C CG . LEU A 1 201 ? -49.280 19.512 7.555 1.00 25.26 ? 199 LEU A CG 1 ATOM 1565 C CD1 . LEU A 1 201 ? -48.099 19.284 8.452 1.00 25.27 ? 199 LEU A CD1 1 ATOM 1566 C CD2 . LEU A 1 201 ? -49.931 18.179 7.209 1.00 27.67 ? 199 LEU A CD2 1 ATOM 1567 N N . LEU A 1 202 ? -52.117 23.173 7.595 1.00 23.42 ? 200 LEU A N 1 ATOM 1568 C CA . LEU A 1 202 ? -52.735 24.404 8.083 1.00 24.11 ? 200 LEU A CA 1 ATOM 1569 C C . LEU A 1 202 ? -53.683 24.922 7.006 1.00 29.80 ? 200 LEU A C 1 ATOM 1570 O O . LEU A 1 202 ? -53.427 24.735 5.813 1.00 30.17 ? 200 LEU A O 1 ATOM 1571 C CB . LEU A 1 202 ? -51.678 25.486 8.411 1.00 24.22 ? 200 LEU A CB 1 ATOM 1572 C CG . LEU A 1 202 ? -50.280 25.052 8.892 1.00 28.93 ? 200 LEU A CG 1 ATOM 1573 C CD1 . LEU A 1 202 ? -49.314 26.216 8.842 1.00 29.05 ? 200 LEU A CD1 1 ATOM 1574 C CD2 . LEU A 1 202 ? -50.315 24.461 10.296 1.00 32.05 ? 200 LEU A CD2 1 ATOM 1575 N N . GLY A 1 203 ? -54.762 25.560 7.430 1.00 26.59 ? 201 GLY A N 1 ATOM 1576 C CA . GLY A 1 203 ? -55.746 26.116 6.511 1.00 26.55 ? 201 GLY A CA 1 ATOM 1577 C C . GLY A 1 203 ? -55.428 27.521 6.061 1.00 30.49 ? 201 GLY A C 1 ATOM 1578 O O . GLY A 1 203 ? -54.401 28.087 6.450 1.00 29.77 ? 201 GLY A O 1 ATOM 1579 N N . ASN A 1 204 ? -56.318 28.090 5.235 1.00 27.49 ? 202 ASN A N 1 ATOM 1580 C CA . ASN A 1 204 ? -56.185 29.448 4.718 1.00 27.56 ? 202 ASN A CA 1 ATOM 1581 C C . ASN A 1 204 ? -56.363 30.482 5.823 1.00 31.43 ? 202 ASN A C 1 ATOM 1582 O O . ASN A 1 204 ? -55.701 31.517 5.786 1.00 31.19 ? 202 ASN A O 1 ATOM 1583 C CB . ASN A 1 204 ? -57.155 29.695 3.558 1.00 29.52 ? 202 ASN A CB 1 ATOM 1584 C CG . ASN A 1 204 ? -56.822 28.954 2.277 1.00 56.71 ? 202 ASN A CG 1 ATOM 1585 O OD1 . ASN A 1 204 ? -55.804 28.258 2.156 1.00 52.25 ? 202 ASN A OD1 1 ATOM 1586 N ND2 . ASN A 1 204 ? -57.678 29.101 1.278 1.00 49.42 ? 202 ASN A ND2 1 ATOM 1587 N N . ARG A 1 205 ? -57.224 30.184 6.823 1.00 27.85 ? 203 ARG A N 1 ATOM 1588 C CA . ARG A 1 205 ? -57.494 31.056 7.972 1.00 27.70 ? 203 ARG A CA 1 ATOM 1589 C C . ARG A 1 205 ? -56.263 31.213 8.869 1.00 32.31 ? 203 ARG A C 1 ATOM 1590 O O . ARG A 1 205 ? -55.948 32.334 9.272 1.00 32.13 ? 203 ARG A O 1 ATOM 1591 C CB . ARG A 1 205 ? -58.709 30.557 8.786 1.00 27.02 ? 203 ARG A CB 1 ATOM 1592 C CG . ARG A 1 205 ? -60.055 30.614 8.050 1.00 33.09 ? 203 ARG A CG 1 ATOM 1593 C CD . ARG A 1 205 ? -60.561 32.032 7.833 1.00 36.30 ? 203 ARG A CD 1 ATOM 1594 N NE . ARG A 1 205 ? -61.918 32.053 7.289 1.00 37.55 ? 203 ARG A NE 1 ATOM 1595 C CZ . ARG A 1 205 ? -62.404 33.022 6.519 1.00 48.08 ? 203 ARG A CZ 1 ATOM 1596 N NH1 . ARG A 1 205 ? -61.642 34.054 6.176 1.00 32.13 ? 203 ARG A NH1 1 ATOM 1597 N NH2 . ARG A 1 205 ? -63.651 32.961 6.074 1.00 32.75 ? 203 ARG A NH2 1 ATOM 1598 N N . LEU A 1 206 ? -55.560 30.099 9.165 1.00 28.70 ? 204 LEU A N 1 ATOM 1599 C CA . LEU A 1 206 ? -54.345 30.117 9.983 1.00 28.53 ? 204 LEU A CA 1 ATOM 1600 C C . LEU A 1 206 ? -53.186 30.761 9.216 1.00 32.81 ? 204 LEU A C 1 ATOM 1601 O O . LEU A 1 206 ? -52.434 31.537 9.806 1.00 32.39 ? 204 LEU A O 1 ATOM 1602 C CB . LEU A 1 206 ? -53.982 28.700 10.480 1.00 28.46 ? 204 LEU A CB 1 ATOM 1603 C CG . LEU A 1 206 ? -52.791 28.545 11.454 1.00 32.79 ? 204 LEU A CG 1 ATOM 1604 C CD1 . LEU A 1 206 ? -52.974 29.378 12.722 1.00 32.90 ? 204 LEU A CD1 1 ATOM 1605 C CD2 . LEU A 1 206 ? -52.603 27.097 11.845 1.00 34.70 ? 204 LEU A CD2 1 ATOM 1606 N N . TRP A 1 207 ? -53.076 30.478 7.902 1.00 29.86 ? 205 TRP A N 1 ATOM 1607 C CA . TRP A 1 207 ? -52.031 31.033 7.038 1.00 30.15 ? 205 TRP A CA 1 ATOM 1608 C C . TRP A 1 207 ? -52.176 32.530 6.808 1.00 35.35 ? 205 TRP A C 1 ATOM 1609 O O . TRP A 1 207 ? -51.168 33.235 6.874 1.00 35.13 ? 205 TRP A O 1 ATOM 1610 C CB . TRP A 1 207 ? -51.953 30.289 5.704 1.00 28.79 ? 205 TRP A CB 1 ATOM 1611 C CG . TRP A 1 207 ? -50.812 30.711 4.825 1.00 29.79 ? 205 TRP A CG 1 ATOM 1612 C CD1 . TRP A 1 207 ? -50.899 31.335 3.615 1.00 32.74 ? 205 TRP A CD1 1 ATOM 1613 C CD2 . TRP A 1 207 ? -49.412 30.554 5.097 1.00 29.57 ? 205 TRP A CD2 1 ATOM 1614 N NE1 . TRP A 1 207 ? -49.641 31.538 3.096 1.00 32.20 ? 205 TRP A NE1 1 ATOM 1615 C CE2 . TRP A 1 207 ? -48.709 31.079 3.991 1.00 33.53 ? 205 TRP A CE2 1 ATOM 1616 C CE3 . TRP A 1 207 ? -48.680 30.013 6.170 1.00 30.77 ? 205 TRP A CE3 1 ATOM 1617 C CZ2 . TRP A 1 207 ? -47.311 31.072 3.922 1.00 32.80 ? 205 TRP A CZ2 1 ATOM 1618 C CZ3 . TRP A 1 207 ? -47.297 30.002 6.097 1.00 32.21 ? 205 TRP A CZ3 1 ATOM 1619 C CH2 . TRP A 1 207 ? -46.626 30.532 4.987 1.00 32.83 ? 205 TRP A CH2 1 ATOM 1620 N N . SER A 1 208 ? -53.415 33.016 6.531 1.00 32.72 ? 206 SER A N 1 ATOM 1621 C CA . SER A 1 208 ? -53.701 34.445 6.327 1.00 32.83 ? 206 SER A CA 1 ATOM 1622 C C . SER A 1 208 ? -53.291 35.223 7.570 1.00 36.67 ? 206 SER A C 1 ATOM 1623 O O . SER A 1 208 ? -52.680 36.282 7.449 1.00 36.41 ? 206 SER A O 1 ATOM 1624 C CB . SER A 1 208 ? -55.180 34.677 6.031 1.00 36.67 ? 206 SER A CB 1 ATOM 1625 O OG . SER A 1 208 ? -55.580 34.025 4.837 1.00 46.24 ? 206 SER A OG 1 ATOM 1626 N N . SER A 1 209 ? -53.576 34.656 8.759 1.00 33.27 ? 207 SER A N 1 ATOM 1627 C CA . SER A 1 209 ? -53.220 35.210 10.061 1.00 33.05 ? 207 SER A CA 1 ATOM 1628 C C . SER A 1 209 ? -51.698 35.213 10.241 1.00 37.83 ? 207 SER A C 1 ATOM 1629 O O . SER A 1 209 ? -51.160 36.178 10.780 1.00 37.29 ? 207 SER A O 1 ATOM 1630 C CB . SER A 1 209 ? -53.892 34.416 11.175 1.00 35.81 ? 207 SER A CB 1 ATOM 1631 O OG . SER A 1 209 ? -53.775 35.082 12.421 1.00 43.22 ? 207 SER A OG 1 ATOM 1632 N N . LEU A 1 210 ? -51.004 34.154 9.763 1.00 35.08 ? 208 LEU A N 1 ATOM 1633 C CA . LEU A 1 210 ? -49.540 34.057 9.837 1.00 35.13 ? 208 LEU A CA 1 ATOM 1634 C C . LEU A 1 210 ? -48.873 35.083 8.907 1.00 39.53 ? 208 LEU A C 1 ATOM 1635 O O . LEU A 1 210 ? -47.939 35.761 9.330 1.00 38.89 ? 208 LEU A O 1 ATOM 1636 C CB . LEU A 1 210 ? -49.046 32.629 9.520 1.00 35.15 ? 208 LEU A CB 1 ATOM 1637 C CG . LEU A 1 210 ? -49.171 31.587 10.639 1.00 39.77 ? 208 LEU A CG 1 ATOM 1638 C CD1 . LEU A 1 210 ? -49.330 30.192 10.067 1.00 40.04 ? 208 LEU A CD1 1 ATOM 1639 C CD2 . LEU A 1 210 ? -47.972 31.620 11.571 1.00 42.03 ? 208 LEU A CD2 1 ATOM 1640 N N . GLN A 1 211 ? -49.375 35.217 7.659 1.00 36.89 ? 209 GLN A N 1 ATOM 1641 C CA . GLN A 1 211 ? -48.863 36.154 6.653 1.00 37.19 ? 209 GLN A CA 1 ATOM 1642 C C . GLN A 1 211 ? -49.049 37.620 7.056 1.00 42.24 ? 209 GLN A C 1 ATOM 1643 O O . GLN A 1 211 ? -48.167 38.441 6.801 1.00 41.93 ? 209 GLN A O 1 ATOM 1644 C CB . GLN A 1 211 ? -49.512 35.899 5.280 1.00 38.56 ? 209 GLN A CB 1 ATOM 1645 C CG . GLN A 1 211 ? -48.987 34.668 4.538 1.00 54.34 ? 209 GLN A CG 1 ATOM 1646 C CD . GLN A 1 211 ? -47.542 34.797 4.117 1.00 74.81 ? 209 GLN A CD 1 ATOM 1647 O OE1 . GLN A 1 211 ? -46.647 34.183 4.707 1.00 70.44 ? 209 GLN A OE1 1 ATOM 1648 N NE2 . GLN A 1 211 ? -47.279 35.596 3.091 1.00 67.29 ? 209 GLN A NE2 1 ATOM 1649 N N . THR A 1 212 ? -50.193 37.941 7.684 1.00 39.40 ? 210 THR A N 1 ATOM 1650 C CA . THR A 1 212 ? -50.532 39.297 8.122 1.00 39.31 ? 210 THR A CA 1 ATOM 1651 C C . THR A 1 212 ? -49.727 39.732 9.352 1.00 43.16 ? 210 THR A C 1 ATOM 1652 O O . THR A 1 212 ? -49.208 40.850 9.380 1.00 42.58 ? 210 THR A O 1 ATOM 1653 C CB . THR A 1 212 ? -52.055 39.404 8.365 1.00 47.28 ? 210 THR A CB 1 ATOM 1654 O OG1 . THR A 1 212 ? -52.755 38.987 7.193 1.00 46.93 ? 210 THR A OG1 1 ATOM 1655 C CG2 . THR A 1 212 ? -52.495 40.806 8.754 1.00 45.81 ? 210 THR A CG2 1 ATOM 1656 N N . HIS A 1 213 ? -49.639 38.853 10.365 1.00 39.76 ? 211 HIS A N 1 ATOM 1657 C CA . HIS A 1 213 ? -49.008 39.139 11.652 1.00 39.60 ? 211 HIS A CA 1 ATOM 1658 C C . HIS A 1 213 ? -47.508 38.840 11.800 1.00 43.45 ? 211 HIS A C 1 ATOM 1659 O O . HIS A 1 213 ? -46.789 39.680 12.344 1.00 43.16 ? 211 HIS A O 1 ATOM 1660 C CB . HIS A 1 213 ? -49.831 38.522 12.788 1.00 40.38 ? 211 HIS A CB 1 ATOM 1661 C CG . HIS A 1 213 ? -51.234 39.042 12.851 1.00 43.89 ? 211 HIS A CG 1 ATOM 1662 N ND1 . HIS A 1 213 ? -51.554 40.165 13.593 1.00 45.77 ? 211 HIS A ND1 1 ATOM 1663 C CD2 . HIS A 1 213 ? -52.356 38.583 12.250 1.00 45.61 ? 211 HIS A CD2 1 ATOM 1664 C CE1 . HIS A 1 213 ? -52.855 40.346 13.426 1.00 45.12 ? 211 HIS A CE1 1 ATOM 1665 N NE2 . HIS A 1 213 ? -53.379 39.419 12.625 1.00 45.39 ? 211 HIS A NE2 1 ATOM 1666 N N . CYS A 1 214 ? -47.040 37.658 11.349 1.00 39.88 ? 212 CYS A N 1 ATOM 1667 C CA . CYS A 1 214 ? -45.628 37.252 11.455 1.00 39.58 ? 212 CYS A CA 1 ATOM 1668 C C . CYS A 1 214 ? -44.732 37.903 10.411 1.00 43.54 ? 212 CYS A C 1 ATOM 1669 O O . CYS A 1 214 ? -43.514 37.955 10.606 1.00 43.16 ? 212 CYS A O 1 ATOM 1670 C CB . CYS A 1 214 ? -45.488 35.732 11.393 1.00 39.70 ? 212 CYS A CB 1 ATOM 1671 S SG . CYS A 1 214 ? -46.382 34.834 12.680 1.00 43.48 ? 212 CYS A SG 1 ATOM 1672 N N . CYS A 1 215 ? -45.313 38.321 9.279 1.00 40.09 ? 213 CYS A N 1 ATOM 1673 C CA . CYS A 1 215 ? -44.558 38.824 8.138 1.00 40.15 ? 213 CYS A CA 1 ATOM 1674 C C . CYS A 1 215 ? -44.673 40.316 7.835 1.00 46.61 ? 213 CYS A C 1 ATOM 1675 O O . CYS A 1 215 ? -45.607 40.986 8.280 1.00 46.07 ? 213 CYS A O 1 ATOM 1676 C CB . CYS A 1 215 ? -44.860 37.982 6.901 1.00 39.90 ? 213 CYS A CB 1 ATOM 1677 S SG . CYS A 1 215 ? -45.058 36.210 7.234 1.00 43.42 ? 213 CYS A SG 1 ATOM 1678 N N . SER A 1 216 ? -43.704 40.812 7.041 1.00 45.10 ? 214 SER A N 1 ATOM 1679 C CA . SER A 1 216 ? -43.598 42.173 6.526 1.00 45.70 ? 214 SER A CA 1 ATOM 1680 C C . SER A 1 216 ? -43.329 42.041 5.021 1.00 51.16 ? 214 SER A C 1 ATOM 1681 O O . SER A 1 216 ? -42.245 41.607 4.619 1.00 50.90 ? 214 SER A O 1 ATOM 1682 C CB . SER A 1 216 ? -42.472 42.928 7.225 1.00 49.52 ? 214 SER A CB 1 ATOM 1683 O OG . SER A 1 216 ? -42.419 44.277 6.791 1.00 59.21 ? 214 SER A OG 1 ATOM 1684 N N . GLN A 1 217 ? -44.347 42.377 4.198 1.00 48.65 ? 215 GLN A N 1 ATOM 1685 C CA . GLN A 1 217 ? -44.374 42.282 2.726 1.00 48.87 ? 215 GLN A CA 1 ATOM 1686 C C . GLN A 1 217 ? -44.108 40.849 2.223 1.00 53.14 ? 215 GLN A C 1 ATOM 1687 O O . GLN A 1 217 ? -45.060 40.093 2.014 1.00 53.09 ? 215 GLN A O 1 ATOM 1688 C CB . GLN A 1 217 ? -43.482 43.323 1.996 1.00 50.35 ? 215 GLN A CB 1 ATOM 1689 C CG . GLN A 1 217 ? -43.161 44.622 2.744 1.00 67.96 ? 215 GLN A CG 1 ATOM 1690 C CD . GLN A 1 217 ? -41.760 44.630 3.324 1.00 88.80 ? 215 GLN A CD 1 ATOM 1691 O OE1 . GLN A 1 217 ? -40.896 43.809 2.982 1.00 84.71 ? 215 GLN A OE1 1 ATOM 1692 N NE2 . GLN A 1 217 ? -41.496 45.579 4.208 1.00 80.83 ? 215 GLN A NE2 1 ATOM 1693 N N . ASN A 1 218 ? -42.819 40.475 2.057 1.00 49.34 ? 216 ASN A N 1 ATOM 1694 C CA . ASN A 1 218 ? -42.392 39.155 1.581 1.00 48.90 ? 216 ASN A CA 1 ATOM 1695 C C . ASN A 1 218 ? -41.693 38.331 2.666 1.00 51.21 ? 216 ASN A C 1 ATOM 1696 O O . ASN A 1 218 ? -41.943 37.127 2.769 1.00 51.10 ? 216 ASN A O 1 ATOM 1697 C CB . ASN A 1 218 ? -41.480 39.290 0.354 1.00 51.04 ? 216 ASN A CB 1 ATOM 1698 C CG . ASN A 1 218 ? -42.199 39.651 -0.923 1.00 78.94 ? 216 ASN A CG 1 ATOM 1699 O OD1 . ASN A 1 218 ? -42.731 40.756 -1.081 1.00 74.48 ? 216 ASN A OD1 1 ATOM 1700 N ND2 . ASN A 1 218 ? -42.192 38.735 -1.881 1.00 71.49 ? 216 ASN A ND2 1 ATOM 1701 N N . LYS A 1 219 ? -40.810 38.975 3.459 1.00 45.89 ? 217 LYS A N 1 ATOM 1702 C CA . LYS A 1 219 ? -40.028 38.335 4.522 1.00 44.74 ? 217 LYS A CA 1 ATOM 1703 C C . LYS A 1 219 ? -40.883 37.986 5.740 1.00 45.67 ? 217 LYS A C 1 ATOM 1704 O O . LYS A 1 219 ? -41.610 38.840 6.252 1.00 45.30 ? 217 LYS A O 1 ATOM 1705 C CB . LYS A 1 219 ? -38.816 39.203 4.930 1.00 47.59 ? 217 LYS A CB 1 ATOM 1706 C CG . LYS A 1 219 ? -37.962 39.721 3.766 1.00 65.62 ? 217 LYS A CG 1 ATOM 1707 C CD . LYS A 1 219 ? -36.927 38.707 3.269 1.00 77.88 ? 217 LYS A CD 1 ATOM 1708 C CE . LYS A 1 219 ? -36.249 39.150 1.991 1.00 90.99 ? 217 LYS A CE 1 ATOM 1709 N NZ . LYS A 1 219 ? -35.313 40.288 2.207 1.00 100.87 ? 217 LYS A NZ 1 ATOM 1710 N N . CYS A 1 220 ? -40.782 36.726 6.198 1.00 39.99 ? 218 CYS A N 1 ATOM 1711 C CA . CYS A 1 220 ? -41.515 36.183 7.342 1.00 38.86 ? 218 CYS A CA 1 ATOM 1712 C C . CYS A 1 220 ? -40.589 35.833 8.495 1.00 39.83 ? 218 CYS A C 1 ATOM 1713 O O . CYS A 1 220 ? -39.502 35.301 8.268 1.00 39.30 ? 218 CYS A O 1 ATOM 1714 C CB . CYS A 1 220 ? -42.334 34.967 6.923 1.00 39.32 ? 218 CYS A CB 1 ATOM 1715 S SG . CYS A 1 220 ? -43.782 35.350 5.910 1.00 43.30 ? 218 CYS A SG 1 ATOM 1716 N N . ASN A 1 221 ? -41.046 36.077 9.734 1.00 34.34 ? 219 ASN A N 1 ATOM 1717 C CA . ASN A 1 221 ? -40.301 35.729 10.940 1.00 33.20 ? 219 ASN A CA 1 ATOM 1718 C C . ASN A 1 221 ? -41.147 34.812 11.821 1.00 35.35 ? 219 ASN A C 1 ATOM 1719 O O . ASN A 1 221 ? -42.073 35.266 12.497 1.00 34.64 ? 219 ASN A O 1 ATOM 1720 C CB . ASN A 1 221 ? -39.803 36.973 11.699 1.00 32.44 ? 219 ASN A CB 1 ATOM 1721 C CG . ASN A 1 221 ? -38.970 36.679 12.934 1.00 50.91 ? 219 ASN A CG 1 ATOM 1722 O OD1 . ASN A 1 221 ? -38.391 35.595 13.105 1.00 44.98 ? 219 ASN A OD1 1 ATOM 1723 N ND2 . ASN A 1 221 ? -38.871 37.656 13.821 1.00 41.50 ? 219 ASN A ND2 1 ATOM 1724 N N . PHE A 1 222 ? -40.837 33.509 11.775 1.00 30.62 ? 220 PHE A N 1 ATOM 1725 C CA . PHE A 1 222 ? -41.514 32.465 12.544 1.00 29.68 ? 220 PHE A CA 1 ATOM 1726 C C . PHE A 1 222 ? -40.550 31.860 13.583 1.00 33.13 ? 220 PHE A C 1 ATOM 1727 O O . PHE A 1 222 ? -40.864 30.835 14.195 1.00 32.73 ? 220 PHE A O 1 ATOM 1728 C CB . PHE A 1 222 ? -42.028 31.360 11.600 1.00 31.14 ? 220 PHE A CB 1 ATOM 1729 C CG . PHE A 1 222 ? -42.922 31.760 10.446 1.00 32.21 ? 220 PHE A CG 1 ATOM 1730 C CD1 . PHE A 1 222 ? -44.175 32.320 10.673 1.00 34.85 ? 220 PHE A CD1 1 ATOM 1731 C CD2 . PHE A 1 222 ? -42.554 31.484 9.134 1.00 33.92 ? 220 PHE A CD2 1 ATOM 1732 C CE1 . PHE A 1 222 ? -45.016 32.652 9.605 1.00 35.50 ? 220 PHE A CE1 1 ATOM 1733 C CE2 . PHE A 1 222 ? -43.405 31.795 8.069 1.00 36.50 ? 220 PHE A CE2 1 ATOM 1734 C CZ . PHE A 1 222 ? -44.626 32.386 8.311 1.00 34.60 ? 220 PHE A CZ 1 ATOM 1735 N N . TYR A 1 223 ? -39.382 32.506 13.781 1.00 29.45 ? 221 TYR A N 1 ATOM 1736 C CA . TYR A 1 223 ? -38.323 32.055 14.686 1.00 29.04 ? 221 TYR A CA 1 ATOM 1737 C C . TYR A 1 223 ? -38.322 32.743 16.055 1.00 33.32 ? 221 TYR A C 1 ATOM 1738 O O . TYR A 1 223 ? -38.462 32.059 17.070 1.00 32.62 ? 221 TYR A O 1 ATOM 1739 C CB . TYR A 1 223 ? -36.950 32.156 13.986 1.00 29.89 ? 221 TYR A CB 1 ATOM 1740 C CG . TYR A 1 223 ? -35.749 31.930 14.881 1.00 31.32 ? 221 TYR A CG 1 ATOM 1741 C CD1 . TYR A 1 223 ? -35.496 30.681 15.442 1.00 33.21 ? 221 TYR A CD1 1 ATOM 1742 C CD2 . TYR A 1 223 ? -34.840 32.955 15.131 1.00 31.94 ? 221 TYR A CD2 1 ATOM 1743 C CE1 . TYR A 1 223 ? -34.377 30.461 16.243 1.00 33.90 ? 221 TYR A CE1 1 ATOM 1744 C CE2 . TYR A 1 223 ? -33.714 32.745 15.928 1.00 32.74 ? 221 TYR A CE2 1 ATOM 1745 C CZ . TYR A 1 223 ? -33.488 31.496 16.482 1.00 39.72 ? 221 TYR A CZ 1 ATOM 1746 O OH . TYR A 1 223 ? -32.386 31.280 17.272 1.00 40.65 ? 221 TYR A OH 1 ATOM 1747 N N . ASP A 1 224 ? -38.138 34.078 16.086 1.00 30.62 ? 222 ASP A N 1 ATOM 1748 C CA . ASP A 1 224 ? -38.087 34.854 17.330 1.00 30.71 ? 222 ASP A CA 1 ATOM 1749 C C . ASP A 1 224 ? -39.031 36.073 17.336 1.00 35.96 ? 222 ASP A C 1 ATOM 1750 O O . ASP A 1 224 ? -38.758 37.063 18.023 1.00 35.47 ? 222 ASP A O 1 ATOM 1751 C CB . ASP A 1 224 ? -36.630 35.252 17.659 1.00 32.18 ? 222 ASP A CB 1 ATOM 1752 C CG . ASP A 1 224 ? -35.900 36.088 16.614 1.00 38.86 ? 222 ASP A CG 1 ATOM 1753 O OD1 . ASP A 1 224 ? -36.510 36.411 15.570 1.00 38.46 ? 222 ASP A OD1 1 ATOM 1754 O OD2 . ASP A 1 224 ? -34.712 36.401 16.833 1.00 44.94 ? 222 ASP A OD2 1 ATOM 1755 N N . ASN A 1 225 ? -40.147 35.989 16.580 1.00 33.51 ? 223 ASN A N 1 ATOM 1756 C CA . ASN A 1 225 ? -41.137 37.064 16.485 1.00 33.86 ? 223 ASN A CA 1 ATOM 1757 C C . ASN A 1 225 ? -41.868 37.268 17.806 1.00 39.49 ? 223 ASN A C 1 ATOM 1758 O O . ASN A 1 225 ? -42.134 36.300 18.522 1.00 39.06 ? 223 ASN A O 1 ATOM 1759 C CB . ASN A 1 225 ? -42.137 36.793 15.365 1.00 33.38 ? 223 ASN A CB 1 ATOM 1760 C CG . ASN A 1 225 ? -42.767 38.035 14.778 1.00 47.12 ? 223 ASN A CG 1 ATOM 1761 O OD1 . ASN A 1 225 ? -43.218 38.942 15.487 1.00 38.64 ? 223 ASN A OD1 1 ATOM 1762 N ND2 . ASN A 1 225 ? -42.832 38.092 13.457 1.00 36.86 ? 223 ASN A ND2 1 ATOM 1763 N N . LYS A 1 226 ? -42.175 38.534 18.128 1.00 37.43 ? 224 LYS A N 1 ATOM 1764 C CA . LYS A 1 226 ? -42.864 38.897 19.366 1.00 37.77 ? 224 LYS A CA 1 ATOM 1765 C C . LYS A 1 226 ? -44.283 39.447 19.162 1.00 42.54 ? 224 LYS A C 1 ATOM 1766 O O . LYS A 1 226 ? -44.944 39.793 20.144 1.00 42.36 ? 224 LYS A O 1 ATOM 1767 C CB . LYS A 1 226 ? -41.990 39.803 20.251 1.00 40.44 ? 224 LYS A CB 1 ATOM 1768 C CG . LYS A 1 226 ? -40.883 39.034 20.965 1.00 54.56 ? 224 LYS A CG 1 ATOM 1769 C CD . LYS A 1 226 ? -40.078 39.912 21.908 1.00 64.46 ? 224 LYS A CD 1 ATOM 1770 C CE . LYS A 1 226 ? -38.991 39.144 22.625 1.00 76.18 ? 224 LYS A CE 1 ATOM 1771 N NZ . LYS A 1 226 ? -39.530 38.291 23.718 1.00 86.06 ? 224 LYS A NZ 1 ATOM 1772 N N . ASP A 1 227 ? -44.766 39.485 17.896 1.00 39.63 ? 225 ASP A N 1 ATOM 1773 C CA . ASP A 1 227 ? -46.124 39.923 17.552 1.00 39.71 ? 225 ASP A CA 1 ATOM 1774 C C . ASP A 1 227 ? -47.111 38.964 18.230 1.00 43.81 ? 225 ASP A C 1 ATOM 1775 O O . ASP A 1 227 ? -46.909 37.750 18.190 1.00 43.50 ? 225 ASP A O 1 ATOM 1776 C CB . ASP A 1 227 ? -46.317 39.963 16.025 1.00 41.68 ? 225 ASP A CB 1 ATOM 1777 C CG . ASP A 1 227 ? -47.723 40.298 15.574 1.00 52.82 ? 225 ASP A CG 1 ATOM 1778 O OD1 . ASP A 1 227 ? -48.574 39.386 15.564 1.00 53.64 ? 225 ASP A OD1 1 ATOM 1779 O OD2 . ASP A 1 227 ? -47.965 41.467 15.209 1.00 58.69 ? 225 ASP A OD2 1 ATOM 1780 N N . LEU A 1 228 ? -48.133 39.521 18.896 1.00 40.25 ? 226 LEU A N 1 ATOM 1781 C CA . LEU A 1 228 ? -49.114 38.781 19.693 1.00 40.07 ? 226 LEU A CA 1 ATOM 1782 C C . LEU A 1 228 ? -49.923 37.715 18.968 1.00 43.95 ? 226 LEU A C 1 ATOM 1783 O O . LEU A 1 228 ? -49.940 36.570 19.422 1.00 43.23 ? 226 LEU A O 1 ATOM 1784 C CB . LEU A 1 228 ? -50.000 39.724 20.521 1.00 40.18 ? 226 LEU A CB 1 ATOM 1785 C CG . LEU A 1 228 ? -49.249 40.711 21.422 1.00 44.91 ? 226 LEU A CG 1 ATOM 1786 C CD1 . LEU A 1 228 ? -50.120 41.885 21.782 1.00 45.11 ? 226 LEU A CD1 1 ATOM 1787 C CD2 . LEU A 1 228 ? -48.672 40.025 22.660 1.00 47.49 ? 226 LEU A CD2 1 ATOM 1788 N N . GLU A 1 229 ? -50.568 38.067 17.838 1.00 40.64 ? 227 GLU A N 1 ATOM 1789 C CA . GLU A 1 229 ? -51.339 37.097 17.054 1.00 40.46 ? 227 GLU A CA 1 ATOM 1790 C C . GLU A 1 229 ? -50.403 36.064 16.405 1.00 44.09 ? 227 GLU A C 1 ATOM 1791 O O . GLU A 1 229 ? -50.789 34.906 16.260 1.00 43.66 ? 227 GLU A O 1 ATOM 1792 C CB . GLU A 1 229 ? -52.243 37.801 16.022 1.00 41.85 ? 227 GLU A CB 1 ATOM 1793 C CG . GLU A 1 229 ? -53.287 36.910 15.351 1.00 51.92 ? 227 GLU A CG 1 ATOM 1794 C CD . GLU A 1 229 ? -54.248 36.137 16.241 1.00 69.26 ? 227 GLU A CD 1 ATOM 1795 O OE1 . GLU A 1 229 ? -54.695 36.687 17.274 1.00 64.33 ? 227 GLU A OE1 1 ATOM 1796 O OE2 . GLU A 1 229 ? -54.580 34.984 15.881 1.00 59.62 ? 227 GLU A OE2 1 ATOM 1797 N N . CYS A 1 230 ? -49.155 36.477 16.089 1.00 40.29 ? 228 CYS A N 1 ATOM 1798 C CA . CYS A 1 230 ? -48.111 35.633 15.505 1.00 39.75 ? 228 CYS A CA 1 ATOM 1799 C C . CYS A 1 230 ? -47.721 34.468 16.419 1.00 42.98 ? 228 CYS A C 1 ATOM 1800 O O . CYS A 1 230 ? -47.733 33.322 15.966 1.00 42.47 ? 228 CYS A O 1 ATOM 1801 C CB . CYS A 1 230 ? -46.893 36.466 15.117 1.00 39.88 ? 228 CYS A CB 1 ATOM 1802 S SG . CYS A 1 230 ? -45.541 35.503 14.400 1.00 43.59 ? 228 CYS A SG 1 ATOM 1803 N N . VAL A 1 231 ? -47.375 34.763 17.695 1.00 39.16 ? 229 VAL A N 1 ATOM 1804 C CA . VAL A 1 231 ? -46.981 33.772 18.710 1.00 38.92 ? 229 VAL A CA 1 ATOM 1805 C C . VAL A 1 231 ? -48.129 32.770 18.961 1.00 42.64 ? 229 VAL A C 1 ATOM 1806 O O . VAL A 1 231 ? -47.867 31.575 19.121 1.00 42.53 ? 229 VAL A O 1 ATOM 1807 C CB . VAL A 1 231 ? -46.437 34.441 20.011 1.00 42.91 ? 229 VAL A CB 1 ATOM 1808 C CG1 . VAL A 1 231 ? -46.092 33.410 21.086 1.00 42.64 ? 229 VAL A CG1 1 ATOM 1809 C CG2 . VAL A 1 231 ? -45.219 35.315 19.715 1.00 42.77 ? 229 VAL A CG2 1 ATOM 1810 N N . THR A 1 232 ? -49.391 33.254 18.924 1.00 38.51 ? 230 THR A N 1 ATOM 1811 C CA . THR A 1 232 ? -50.606 32.447 19.087 1.00 37.85 ? 230 THR A CA 1 ATOM 1812 C C . THR A 1 232 ? -50.734 31.448 17.923 1.00 40.61 ? 230 THR A C 1 ATOM 1813 O O . THR A 1 232 ? -50.946 30.258 18.166 1.00 40.24 ? 230 THR A O 1 ATOM 1814 C CB . THR A 1 232 ? -51.842 33.364 19.230 1.00 44.52 ? 230 THR A CB 1 ATOM 1815 O OG1 . THR A 1 232 ? -51.640 34.252 20.330 1.00 43.76 ? 230 THR A OG1 1 ATOM 1816 C CG2 . THR A 1 232 ? -53.143 32.587 19.434 1.00 43.05 ? 230 THR A CG2 1 ATOM 1817 N N . ASN A 1 233 ? -50.589 31.938 16.672 1.00 36.35 ? 231 ASN A N 1 ATOM 1818 C CA . ASN A 1 233 ? -50.669 31.137 15.447 1.00 35.73 ? 231 ASN A CA 1 ATOM 1819 C C . ASN A 1 233 ? -49.566 30.080 15.380 1.00 38.25 ? 231 ASN A C 1 ATOM 1820 O O . ASN A 1 233 ? -49.838 28.954 14.961 1.00 37.69 ? 231 ASN A O 1 ATOM 1821 C CB . ASN A 1 233 ? -50.633 32.029 14.201 1.00 36.66 ? 231 ASN A CB 1 ATOM 1822 C CG . ASN A 1 233 ? -51.769 33.021 14.083 1.00 58.16 ? 231 ASN A CG 1 ATOM 1823 O OD1 . ASN A 1 233 ? -52.932 32.738 14.399 1.00 51.98 ? 231 ASN A OD1 1 ATOM 1824 N ND2 . ASN A 1 233 ? -51.447 34.217 13.620 1.00 49.15 ? 231 ASN A ND2 1 ATOM 1825 N N . LEU A 1 234 ? -48.337 30.434 15.817 1.00 33.71 ? 232 LEU A N 1 ATOM 1826 C CA . LEU A 1 234 ? -47.182 29.530 15.839 1.00 33.00 ? 232 LEU A CA 1 ATOM 1827 C C . LEU A 1 234 ? -47.328 28.404 16.860 1.00 36.23 ? 232 LEU A C 1 ATOM 1828 O O . LEU A 1 234 ? -46.791 27.315 16.646 1.00 35.82 ? 232 LEU A O 1 ATOM 1829 C CB . LEU A 1 234 ? -45.866 30.297 16.049 1.00 32.85 ? 232 LEU A CB 1 ATOM 1830 C CG . LEU A 1 234 ? -45.387 31.146 14.870 1.00 37.28 ? 232 LEU A CG 1 ATOM 1831 C CD1 . LEU A 1 234 ? -44.274 32.068 15.286 1.00 37.36 ? 232 LEU A CD1 1 ATOM 1832 C CD2 . LEU A 1 234 ? -44.941 30.284 13.708 1.00 39.42 ? 232 LEU A CD2 1 ATOM 1833 N N . GLN A 1 235 ? -48.068 28.660 17.957 1.00 32.40 ? 233 GLN A N 1 ATOM 1834 C CA . GLN A 1 235 ? -48.359 27.670 18.998 1.00 32.05 ? 233 GLN A CA 1 ATOM 1835 C C . GLN A 1 235 ? -49.307 26.600 18.441 1.00 35.02 ? 233 GLN A C 1 ATOM 1836 O O . GLN A 1 235 ? -49.197 25.430 18.812 1.00 34.61 ? 233 GLN A O 1 ATOM 1837 C CB . GLN A 1 235 ? -48.971 28.347 20.233 1.00 33.50 ? 233 GLN A CB 1 ATOM 1838 C CG . GLN A 1 235 ? -47.927 28.948 21.173 1.00 50.43 ? 233 GLN A CG 1 ATOM 1839 C CD . GLN A 1 235 ? -48.473 29.999 22.117 1.00 71.36 ? 233 GLN A CD 1 ATOM 1840 O OE1 . GLN A 1 235 ? -49.687 30.180 22.281 1.00 67.04 ? 233 GLN A OE1 1 ATOM 1841 N NE2 . GLN A 1 235 ? -47.575 30.716 22.773 1.00 64.27 ? 233 GLN A NE2 1 ATOM 1842 N N . GLU A 1 236 ? -50.222 27.010 17.536 1.00 30.79 ? 234 GLU A N 1 ATOM 1843 C CA . GLU A 1 236 ? -51.176 26.133 16.858 1.00 30.45 ? 234 GLU A CA 1 ATOM 1844 C C . GLU A 1 236 ? -50.442 25.292 15.803 1.00 33.65 ? 234 GLU A C 1 ATOM 1845 O O . GLU A 1 236 ? -50.740 24.104 15.670 1.00 33.31 ? 234 GLU A O 1 ATOM 1846 C CB . GLU A 1 236 ? -52.317 26.956 16.224 1.00 31.84 ? 234 GLU A CB 1 ATOM 1847 C CG . GLU A 1 236 ? -53.492 26.136 15.704 1.00 42.05 ? 234 GLU A CG 1 ATOM 1848 C CD . GLU A 1 236 ? -54.255 25.293 16.711 1.00 64.44 ? 234 GLU A CD 1 ATOM 1849 O OE1 . GLU A 1 236 ? -54.475 25.763 17.851 1.00 63.11 ? 234 GLU A OE1 1 ATOM 1850 O OE2 . GLU A 1 236 ? -54.663 24.168 16.342 1.00 57.72 ? 234 GLU A OE2 1 ATOM 1851 N N . VAL A 1 237 ? -49.476 25.907 15.073 1.00 29.48 ? 235 VAL A N 1 ATOM 1852 C CA . VAL A 1 237 ? -48.642 25.250 14.052 1.00 28.98 ? 235 VAL A CA 1 ATOM 1853 C C . VAL A 1 237 ? -47.844 24.110 14.712 1.00 32.47 ? 235 VAL A C 1 ATOM 1854 O O . VAL A 1 237 ? -47.862 22.988 14.207 1.00 32.01 ? 235 VAL A O 1 ATOM 1855 C CB . VAL A 1 237 ? -47.730 26.261 13.288 1.00 32.63 ? 235 VAL A CB 1 ATOM 1856 C CG1 . VAL A 1 237 ? -46.706 25.549 12.402 1.00 32.38 ? 235 VAL A CG1 1 ATOM 1857 C CG2 . VAL A 1 237 ? -48.561 27.233 12.455 1.00 32.31 ? 235 VAL A CG2 1 ATOM 1858 N N . ALA A 1 238 ? -47.203 24.394 15.868 1.00 28.95 ? 236 ALA A N 1 ATOM 1859 C CA . ALA A 1 238 ? -46.429 23.428 16.654 1.00 28.70 ? 236 ALA A CA 1 ATOM 1860 C C . ALA A 1 238 ? -47.303 22.257 17.133 1.00 32.35 ? 236 ALA A C 1 ATOM 1861 O O . ALA A 1 238 ? -46.826 21.120 17.180 1.00 31.99 ? 236 ALA A O 1 ATOM 1862 C CB . ALA A 1 238 ? -45.780 24.121 17.841 1.00 29.46 ? 236 ALA A CB 1 ATOM 1863 N N . ARG A 1 239 ? -48.584 22.536 17.455 1.00 28.60 ? 237 ARG A N 1 ATOM 1864 C CA . ARG A 1 239 ? -49.551 21.529 17.897 1.00 28.37 ? 237 ARG A CA 1 ATOM 1865 C C . ARG A 1 239 ? -49.954 20.602 16.737 1.00 31.77 ? 237 ARG A C 1 ATOM 1866 O O . ARG A 1 239 ? -49.977 19.388 16.925 1.00 31.36 ? 237 ARG A O 1 ATOM 1867 C CB . ARG A 1 239 ? -50.784 22.190 18.538 1.00 28.39 ? 237 ARG A CB 1 ATOM 1868 C CG . ARG A 1 239 ? -51.715 21.204 19.249 1.00 37.48 ? 237 ARG A CG 1 ATOM 1869 C CD . ARG A 1 239 ? -53.143 21.717 19.370 1.00 44.38 ? 237 ARG A CD 1 ATOM 1870 N NE . ARG A 1 239 ? -53.767 21.968 18.067 1.00 50.25 ? 237 ARG A NE 1 ATOM 1871 C CZ . ARG A 1 239 ? -54.410 21.055 17.345 1.00 61.84 ? 237 ARG A CZ 1 ATOM 1872 N NH1 . ARG A 1 239 ? -54.524 19.808 17.786 1.00 47.54 ? 237 ARG A NH1 1 ATOM 1873 N NH2 . ARG A 1 239 ? -54.942 21.381 16.175 1.00 48.02 ? 237 ARG A NH2 1 ATOM 1874 N N . ILE A 1 240 ? -50.255 21.168 15.546 1.00 27.87 ? 238 ILE A N 1 ATOM 1875 C CA . ILE A 1 240 ? -50.643 20.395 14.356 1.00 27.49 ? 238 ILE A CA 1 ATOM 1876 C C . ILE A 1 240 ? -49.473 19.520 13.855 1.00 31.62 ? 238 ILE A C 1 ATOM 1877 O O . ILE A 1 240 ? -49.654 18.319 13.653 1.00 31.08 ? 238 ILE A O 1 ATOM 1878 C CB . ILE A 1 240 ? -51.253 21.300 13.234 1.00 30.23 ? 238 ILE A CB 1 ATOM 1879 C CG1 . ILE A 1 240 ? -52.527 22.030 13.727 1.00 30.48 ? 238 ILE A CG1 1 ATOM 1880 C CG2 . ILE A 1 240 ? -51.549 20.496 11.951 1.00 30.55 ? 238 ILE A CG2 1 ATOM 1881 C CD1 . ILE A 1 240 ? -52.849 23.357 13.016 1.00 35.60 ? 238 ILE A CD1 1 ATOM 1882 N N . VAL A 1 241 ? -48.281 20.124 13.691 1.00 28.25 ? 239 VAL A N 1 ATOM 1883 C CA . VAL A 1 241 ? -47.068 19.466 13.193 1.00 28.06 ? 239 VAL A CA 1 ATOM 1884 C C . VAL A 1 241 ? -46.514 18.369 14.129 1.00 32.40 ? 239 VAL A C 1 ATOM 1885 O O . VAL A 1 241 ? -46.258 17.255 13.669 1.00 32.03 ? 239 VAL A O 1 ATOM 1886 C CB . VAL A 1 241 ? -45.984 20.505 12.761 1.00 31.82 ? 239 VAL A CB 1 ATOM 1887 C CG1 . VAL A 1 241 ? -44.664 19.836 12.381 1.00 31.62 ? 239 VAL A CG1 1 ATOM 1888 C CG2 . VAL A 1 241 ? -46.482 21.377 11.612 1.00 31.59 ? 239 VAL A CG2 1 ATOM 1889 N N . GLY A 1 242 ? -46.331 18.695 15.408 1.00 29.27 ? 240 GLY A N 1 ATOM 1890 C CA . GLY A 1 242 ? -45.723 17.786 16.375 1.00 29.23 ? 240 GLY A CA 1 ATOM 1891 C C . GLY A 1 242 ? -46.586 17.034 17.370 1.00 33.41 ? 240 GLY A C 1 ATOM 1892 O O . GLY A 1 242 ? -46.176 15.958 17.814 1.00 33.40 ? 240 GLY A O 1 ATOM 1893 N N . ASN A 1 243 ? -47.752 17.579 17.769 1.00 29.81 ? 241 ASN A N 1 ATOM 1894 C CA . ASN A 1 243 ? -48.577 16.912 18.786 1.00 29.62 ? 241 ASN A CA 1 ATOM 1895 C C . ASN A 1 243 ? -50.060 16.682 18.411 1.00 32.46 ? 241 ASN A C 1 ATOM 1896 O O . ASN A 1 243 ? -50.948 16.869 19.248 1.00 32.42 ? 241 ASN A O 1 ATOM 1897 C CB . ASN A 1 243 ? -48.409 17.615 20.149 1.00 31.70 ? 241 ASN A CB 1 ATOM 1898 C CG . ASN A 1 243 ? -48.705 16.744 21.349 1.00 61.14 ? 241 ASN A CG 1 ATOM 1899 O OD1 . ASN A 1 243 ? -49.701 16.939 22.055 1.00 57.58 ? 241 ASN A OD1 1 ATOM 1900 N ND2 . ASN A 1 243 ? -47.844 15.770 21.617 1.00 54.38 ? 241 ASN A ND2 1 ATOM 1901 N N . SER A 1 244 ? -50.325 16.250 17.163 1.00 27.77 ? 242 SER A N 1 ATOM 1902 C CA . SER A 1 244 ? -51.697 15.994 16.708 1.00 27.14 ? 242 SER A CA 1 ATOM 1903 C C . SER A 1 244 ? -51.932 14.574 16.162 1.00 29.75 ? 242 SER A C 1 ATOM 1904 O O . SER A 1 244 ? -53.079 14.198 15.917 1.00 29.78 ? 242 SER A O 1 ATOM 1905 C CB . SER A 1 244 ? -52.146 17.054 15.702 1.00 30.80 ? 242 SER A CB 1 ATOM 1906 O OG . SER A 1 244 ? -51.713 16.771 14.381 1.00 38.94 ? 242 SER A OG 1 ATOM 1907 N N . GLY A 1 245 ? -50.858 13.807 15.991 1.00 24.76 ? 243 GLY A N 1 ATOM 1908 C CA . GLY A 1 245 ? -50.924 12.446 15.467 1.00 23.85 ? 243 GLY A CA 1 ATOM 1909 C C . GLY A 1 245 ? -50.204 12.258 14.147 1.00 25.68 ? 243 GLY A C 1 ATOM 1910 O O . GLY A 1 245 ? -50.200 11.152 13.598 1.00 25.10 ? 243 GLY A O 1 ATOM 1911 N N . LEU A 1 246 ? -49.610 13.339 13.611 1.00 21.14 ? 244 LEU A N 1 ATOM 1912 C CA . LEU A 1 246 ? -48.837 13.286 12.371 1.00 20.63 ? 244 LEU A CA 1 ATOM 1913 C C . LEU A 1 246 ? -47.421 12.864 12.724 1.00 24.26 ? 244 LEU A C 1 ATOM 1914 O O . LEU A 1 246 ? -46.875 13.332 13.727 1.00 24.35 ? 244 LEU A O 1 ATOM 1915 C CB . LEU A 1 246 ? -48.789 14.658 11.664 1.00 20.52 ? 244 LEU A CB 1 ATOM 1916 C CG . LEU A 1 246 ? -50.094 15.261 11.130 1.00 24.77 ? 244 LEU A CG 1 ATOM 1917 C CD1 . LEU A 1 246 ? -49.883 16.697 10.720 1.00 24.74 ? 244 LEU A CD1 1 ATOM 1918 C CD2 . LEU A 1 246 ? -50.631 14.482 9.943 1.00 26.37 ? 244 LEU A CD2 1 ATOM 1919 N N . ASN A 1 247 ? -46.825 11.979 11.915 1.00 20.23 ? 245 ASN A N 1 ATOM 1920 C CA . ASN A 1 247 ? -45.450 11.549 12.138 1.00 19.42 ? 245 ASN A CA 1 ATOM 1921 C C . ASN A 1 247 ? -44.546 12.674 11.634 1.00 21.90 ? 245 ASN A C 1 ATOM 1922 O O . ASN A 1 247 ? -44.521 12.959 10.435 1.00 20.95 ? 245 ASN A O 1 ATOM 1923 C CB . ASN A 1 247 ? -45.164 10.217 11.427 1.00 19.36 ? 245 ASN A CB 1 ATOM 1924 C CG . ASN A 1 247 ? -43.856 9.542 11.797 1.00 33.87 ? 245 ASN A CG 1 ATOM 1925 O OD1 . ASN A 1 247 ? -42.861 10.175 12.169 1.00 25.94 ? 245 ASN A OD1 1 ATOM 1926 N ND2 . ASN A 1 247 ? -43.817 8.227 11.660 1.00 24.36 ? 245 ASN A ND2 1 ATOM 1927 N N . ILE A 1 248 ? -43.851 13.351 12.568 1.00 18.41 ? 246 ILE A N 1 ATOM 1928 C CA . ILE A 1 248 ? -42.948 14.468 12.267 1.00 18.44 ? 246 ILE A CA 1 ATOM 1929 C C . ILE A 1 248 ? -41.732 14.022 11.431 1.00 21.63 ? 246 ILE A C 1 ATOM 1930 O O . ILE A 1 248 ? -41.178 14.816 10.676 1.00 21.10 ? 246 ILE A O 1 ATOM 1931 C CB . ILE A 1 248 ? -42.568 15.260 13.559 1.00 21.92 ? 246 ILE A CB 1 ATOM 1932 C CG1 . ILE A 1 248 ? -42.105 16.701 13.237 1.00 22.76 ? 246 ILE A CG1 1 ATOM 1933 C CG2 . ILE A 1 248 ? -41.561 14.502 14.451 1.00 22.78 ? 246 ILE A CG2 1 ATOM 1934 C CD1 . ILE A 1 248 ? -42.202 17.714 14.402 1.00 31.50 ? 246 ILE A CD1 1 ATOM 1935 N N . TYR A 1 249 ? -41.349 12.744 11.551 1.00 17.86 ? 247 TYR A N 1 ATOM 1936 C CA . TYR A 1 249 ? -40.205 12.177 10.848 1.00 17.56 ? 247 TYR A CA 1 ATOM 1937 C C . TYR A 1 249 ? -40.508 11.759 9.417 1.00 21.34 ? 247 TYR A C 1 ATOM 1938 O O . TYR A 1 249 ? -39.591 11.662 8.607 1.00 21.05 ? 247 TYR A O 1 ATOM 1939 C CB . TYR A 1 249 ? -39.578 11.050 11.676 1.00 18.56 ? 247 TYR A CB 1 ATOM 1940 C CG . TYR A 1 249 ? -39.184 11.516 13.062 1.00 20.62 ? 247 TYR A CG 1 ATOM 1941 C CD1 . TYR A 1 249 ? -38.116 12.390 13.249 1.00 22.61 ? 247 TYR A CD1 1 ATOM 1942 C CD2 . TYR A 1 249 ? -39.924 11.144 14.179 1.00 21.52 ? 247 TYR A CD2 1 ATOM 1943 C CE1 . TYR A 1 249 ? -37.774 12.855 14.518 1.00 23.50 ? 247 TYR A CE1 1 ATOM 1944 C CE2 . TYR A 1 249 ? -39.578 11.583 15.456 1.00 22.41 ? 247 TYR A CE2 1 ATOM 1945 C CZ . TYR A 1 249 ? -38.511 12.450 15.619 1.00 29.43 ? 247 TYR A CZ 1 ATOM 1946 O OH . TYR A 1 249 ? -38.177 12.893 16.875 1.00 30.30 ? 247 TYR A OH 1 ATOM 1947 N N . ASN A 1 250 ? -41.793 11.542 9.100 1.00 17.84 ? 248 ASN A N 1 ATOM 1948 C CA . ASN A 1 250 ? -42.266 11.169 7.768 1.00 17.34 ? 248 ASN A CA 1 ATOM 1949 C C . ASN A 1 250 ? -43.759 11.455 7.713 1.00 20.93 ? 248 ASN A C 1 ATOM 1950 O O . ASN A 1 250 ? -44.559 10.693 8.263 1.00 20.33 ? 248 ASN A O 1 ATOM 1951 C CB . ASN A 1 250 ? -41.959 9.694 7.454 1.00 17.25 ? 248 ASN A CB 1 ATOM 1952 C CG . ASN A 1 250 ? -42.137 9.309 6.002 1.00 31.25 ? 248 ASN A CG 1 ATOM 1953 O OD1 . ASN A 1 250 ? -43.104 9.692 5.332 1.00 20.60 ? 248 ASN A OD1 1 ATOM 1954 N ND2 . ASN A 1 250 ? -41.238 8.478 5.503 1.00 22.44 ? 248 ASN A ND2 1 ATOM 1955 N N . LEU A 1 251 ? -44.127 12.575 7.066 1.00 17.25 ? 249 LEU A N 1 ATOM 1956 C CA . LEU A 1 251 ? -45.508 13.048 6.945 1.00 16.83 ? 249 LEU A CA 1 ATOM 1957 C C . LEU A 1 251 ? -46.486 12.010 6.381 1.00 20.48 ? 249 LEU A C 1 ATOM 1958 O O . LEU A 1 251 ? -47.610 11.902 6.877 1.00 19.85 ? 249 LEU A O 1 ATOM 1959 C CB . LEU A 1 251 ? -45.558 14.369 6.143 1.00 16.65 ? 249 LEU A CB 1 ATOM 1960 C CG . LEU A 1 251 ? -46.935 15.014 5.915 1.00 20.94 ? 249 LEU A CG 1 ATOM 1961 C CD1 . LEU A 1 251 ? -47.602 15.393 7.232 1.00 21.22 ? 249 LEU A CD1 1 ATOM 1962 C CD2 . LEU A 1 251 ? -46.826 16.216 5.010 1.00 22.22 ? 249 LEU A CD2 1 ATOM 1963 N N . TYR A 1 252 ? -46.049 11.236 5.377 1.00 17.30 ? 250 TYR A N 1 ATOM 1964 C CA . TYR A 1 252 ? -46.886 10.233 4.715 1.00 17.05 ? 250 TYR A CA 1 ATOM 1965 C C . TYR A 1 252 ? -46.853 8.819 5.310 1.00 20.99 ? 250 TYR A C 1 ATOM 1966 O O . TYR A 1 252 ? -47.531 7.920 4.809 1.00 20.30 ? 250 TYR A O 1 ATOM 1967 C CB . TYR A 1 252 ? -46.677 10.279 3.192 1.00 18.01 ? 250 TYR A CB 1 ATOM 1968 C CG . TYR A 1 252 ? -46.796 11.691 2.661 1.00 19.12 ? 250 TYR A CG 1 ATOM 1969 C CD1 . TYR A 1 252 ? -48.010 12.370 2.696 1.00 20.76 ? 250 TYR A CD1 1 ATOM 1970 C CD2 . TYR A 1 252 ? -45.674 12.389 2.228 1.00 19.70 ? 250 TYR A CD2 1 ATOM 1971 C CE1 . TYR A 1 252 ? -48.119 13.682 2.250 1.00 21.17 ? 250 TYR A CE1 1 ATOM 1972 C CE2 . TYR A 1 252 ? -45.768 13.710 1.790 1.00 20.39 ? 250 TYR A CE2 1 ATOM 1973 C CZ . TYR A 1 252 ? -46.994 14.352 1.803 1.00 26.51 ? 250 TYR A CZ 1 ATOM 1974 O OH . TYR A 1 252 ? -47.097 15.649 1.365 1.00 26.05 ? 250 TYR A OH 1 ATOM 1975 N N . ALA A 1 253 ? -46.110 8.640 6.407 1.00 17.97 ? 251 ALA A N 1 ATOM 1976 C CA . ALA A 1 253 ? -46.021 7.367 7.115 1.00 18.32 ? 251 ALA A CA 1 ATOM 1977 C C . ALA A 1 253 ? -46.969 7.385 8.325 1.00 23.34 ? 251 ALA A C 1 ATOM 1978 O O . ALA A 1 253 ? -47.258 8.470 8.841 1.00 22.08 ? 251 ALA A O 1 ATOM 1979 C CB . ALA A 1 253 ? -44.593 7.131 7.578 1.00 19.19 ? 251 ALA A CB 1 ATOM 1980 N N . PRO A 1 254 ? -47.467 6.220 8.811 1.00 21.81 ? 252 PRO A N 1 ATOM 1981 C CA . PRO A 1 254 ? -48.343 6.252 9.994 1.00 22.33 ? 252 PRO A CA 1 ATOM 1982 C C . PRO A 1 254 ? -47.565 6.554 11.276 1.00 27.88 ? 252 PRO A C 1 ATOM 1983 O O . PRO A 1 254 ? -46.338 6.422 11.309 1.00 26.90 ? 252 PRO A O 1 ATOM 1984 C CB . PRO A 1 254 ? -48.949 4.845 10.022 1.00 24.05 ? 252 PRO A CB 1 ATOM 1985 C CG . PRO A 1 254 ? -47.937 3.987 9.367 1.00 28.19 ? 252 PRO A CG 1 ATOM 1986 C CD . PRO A 1 254 ? -47.249 4.833 8.339 1.00 23.48 ? 252 PRO A CD 1 ATOM 1987 N N . CYS A 1 255 ? -48.282 6.978 12.321 1.00 26.40 ? 253 CYS A N 1 ATOM 1988 C CA . CYS A 1 255 ? -47.717 7.261 13.633 1.00 27.26 ? 253 CYS A CA 1 ATOM 1989 C C . CYS A 1 255 ? -47.776 5.959 14.427 1.00 31.96 ? 253 CYS A C 1 ATOM 1990 O O . CYS A 1 255 ? -48.873 5.445 14.667 1.00 31.42 ? 253 CYS A O 1 ATOM 1991 C CB . CYS A 1 255 ? -48.491 8.383 14.321 1.00 28.05 ? 253 CYS A CB 1 ATOM 1992 S SG . CYS A 1 255 ? -47.908 8.785 15.989 1.00 32.16 ? 253 CYS A SG 1 ATOM 1993 N N . ALA A 1 256 ? -46.601 5.394 14.778 1.00 29.44 ? 254 ALA A N 1 ATOM 1994 C CA . ALA A 1 256 ? -46.501 4.141 15.534 1.00 29.71 ? 254 ALA A CA 1 ATOM 1995 C C . ALA A 1 256 ? -47.162 4.292 16.903 1.00 34.63 ? 254 ALA A C 1 ATOM 1996 O O . ALA A 1 256 ? -46.845 5.223 17.648 1.00 34.04 ? 254 ALA A O 1 ATOM 1997 C CB . ALA A 1 256 ? -45.047 3.723 15.683 1.00 30.48 ? 254 ALA A CB 1 ATOM 1998 N N . GLY A 1 257 ? -48.118 3.410 17.180 1.00 32.19 ? 255 GLY A N 1 ATOM 1999 C CA . GLY A 1 257 ? -48.904 3.427 18.407 1.00 32.70 ? 255 GLY A CA 1 ATOM 2000 C C . GLY A 1 257 ? -50.228 4.156 18.257 1.00 38.09 ? 255 GLY A C 1 ATOM 2001 O O . GLY A 1 257 ? -50.992 4.257 19.221 1.00 37.90 ? 255 GLY A O 1 ATOM 2002 N N . GLY A 1 258 ? -50.488 4.668 17.051 1.00 35.25 ? 256 GLY A N 1 ATOM 2003 C CA . GLY A 1 258 ? -51.707 5.399 16.715 1.00 35.29 ? 256 GLY A CA 1 ATOM 2004 C C . GLY A 1 258 ? -51.729 6.838 17.192 1.00 39.76 ? 256 GLY A C 1 ATOM 2005 O O . GLY A 1 258 ? -50.786 7.300 17.840 1.00 39.14 ? 256 GLY A O 1 ATOM 2006 N N . VAL A 1 259 ? -52.819 7.556 16.865 1.00 37.13 ? 257 VAL A N 1 ATOM 2007 C CA . VAL A 1 259 ? -53.029 8.960 17.238 1.00 37.32 ? 257 VAL A CA 1 ATOM 2008 C C . VAL A 1 259 ? -53.420 9.040 18.736 1.00 42.76 ? 257 VAL A C 1 ATOM 2009 O O . VAL A 1 259 ? -54.341 8.329 19.151 1.00 42.26 ? 257 VAL A O 1 ATOM 2010 C CB . VAL A 1 259 ? -54.058 9.660 16.297 1.00 41.13 ? 257 VAL A CB 1 ATOM 2011 C CG1 . VAL A 1 259 ? -54.385 11.080 16.760 1.00 40.86 ? 257 VAL A CG1 1 ATOM 2012 C CG2 . VAL A 1 259 ? -53.562 9.675 14.853 1.00 40.92 ? 257 VAL A CG2 1 ATOM 2013 N N . PRO A 1 260 ? -52.730 9.878 19.559 1.00 40.48 ? 258 PRO A N 1 ATOM 2014 C CA . PRO A 1 260 ? -53.080 9.962 20.992 1.00 44.71 ? 258 PRO A CA 1 ATOM 2015 C C . PRO A 1 260 ? -54.473 10.532 21.266 1.00 81.45 ? 258 PRO A C 1 ATOM 2016 O O . PRO A 1 260 ? -54.951 11.398 20.536 1.00 46.38 ? 258 PRO A O 1 ATOM 2017 C CB . PRO A 1 260 ? -51.984 10.862 21.572 1.00 45.85 ? 258 PRO A CB 1 ATOM 2018 C CG . PRO A 1 260 ? -51.531 11.691 20.420 1.00 48.96 ? 258 PRO A CG 1 ATOM 2019 C CD . PRO A 1 260 ? -51.600 10.775 19.233 1.00 43.49 ? 258 PRO A CD 1 ATOM 2020 N N . MET B 2 1 ? -38.297 7.368 26.562 1.00 51.67 ? 299 MET B N 1 ATOM 2021 C CA . MET B 2 1 ? -37.096 6.878 25.885 1.00 51.41 ? 299 MET B CA 1 ATOM 2022 C C . MET B 2 1 ? -37.220 6.867 24.353 1.00 53.37 ? 299 MET B C 1 ATOM 2023 O O . MET B 2 1 ? -36.201 6.870 23.661 1.00 53.20 ? 299 MET B O 1 ATOM 2024 C CB . MET B 2 1 ? -36.671 5.492 26.418 1.00 54.09 ? 299 MET B CB 1 ATOM 2025 C CG . MET B 2 1 ? -37.675 4.380 26.152 1.00 58.21 ? 299 MET B CG 1 ATOM 2026 S SD . MET B 2 1 ? -36.907 2.745 26.175 1.00 62.88 ? 299 MET B SD 1 ATOM 2027 C CE . MET B 2 1 ? -38.322 1.727 25.837 1.00 59.63 ? 299 MET B CE 1 ATOM 2028 N N . ASP B 2 2 ? -38.459 6.831 23.832 1.00 48.03 ? 300 ASP B N 1 ATOM 2029 C CA . ASP B 2 2 ? -38.724 6.792 22.396 1.00 46.91 ? 300 ASP B CA 1 ATOM 2030 C C . ASP B 2 2 ? -39.290 8.107 21.860 1.00 47.93 ? 300 ASP B C 1 ATOM 2031 O O . ASP B 2 2 ? -40.261 8.619 22.427 1.00 47.59 ? 300 ASP B O 1 ATOM 2032 C CB . ASP B 2 2 ? -39.674 5.628 22.047 1.00 48.92 ? 300 ASP B CB 1 ATOM 2033 C CG . ASP B 2 2 ? -39.032 4.254 21.939 1.00 59.32 ? 300 ASP B CG 1 ATOM 2034 O OD1 . ASP B 2 2 ? -37.858 4.106 22.353 1.00 60.07 ? 300 ASP B OD1 1 ATOM 2035 O OD2 . ASP B 2 2 ? -39.706 3.323 21.447 1.00 64.68 ? 300 ASP B OD2 1 ATOM 2036 N N . PRO B 2 3 ? -38.737 8.641 20.739 1.00 41.94 ? 301 PRO B N 1 ATOM 2037 C CA . PRO B 2 3 ? -39.297 9.874 20.150 1.00 40.77 ? 301 PRO B CA 1 ATOM 2038 C C . PRO B 2 3 ? -40.737 9.658 19.656 1.00 41.85 ? 301 PRO B C 1 ATOM 2039 O O . PRO B 2 3 ? -41.086 8.514 19.353 1.00 41.07 ? 301 PRO B O 1 ATOM 2040 C CB . PRO B 2 3 ? -38.342 10.176 18.986 1.00 42.62 ? 301 PRO B CB 1 ATOM 2041 C CG . PRO B 2 3 ? -37.105 9.392 19.278 1.00 47.36 ? 301 PRO B CG 1 ATOM 2042 C CD . PRO B 2 3 ? -37.591 8.153 19.948 1.00 43.14 ? 301 PRO B CD 1 ATOM 2043 N N . PRO B 2 4 ? -41.603 10.703 19.595 1.00 36.67 ? 302 PRO B N 1 ATOM 2044 C CA . PRO B 2 4 ? -43.000 10.479 19.166 1.00 35.53 ? 302 PRO B CA 1 ATOM 2045 C C . PRO B 2 4 ? -43.161 9.848 17.786 1.00 36.30 ? 302 PRO B C 1 ATOM 2046 O O . PRO B 2 4 ? -42.343 10.091 16.895 1.00 35.71 ? 302 PRO B O 1 ATOM 2047 C CB . PRO B 2 4 ? -43.623 11.877 19.227 1.00 37.48 ? 302 PRO B CB 1 ATOM 2048 C CG . PRO B 2 4 ? -42.769 12.630 20.190 1.00 42.37 ? 302 PRO B CG 1 ATOM 2049 C CD . PRO B 2 4 ? -41.380 12.121 19.946 1.00 38.09 ? 302 PRO B CD 1 ATOM 2050 N N . CYS B 2 5 ? -44.204 9.002 17.637 1.00 30.55 ? 303 CYS B N 1 ATOM 2051 C CA . CYS B 2 5 ? -44.573 8.276 16.412 1.00 29.31 ? 303 CYS B CA 1 ATOM 2052 C C . CYS B 2 5 ? -43.547 7.240 15.918 1.00 32.78 ? 303 CYS B C 1 ATOM 2053 O O . CYS B 2 5 ? -43.694 6.713 14.813 1.00 31.66 ? 303 CYS B O 1 ATOM 2054 C CB . CYS B 2 5 ? -45.001 9.236 15.303 1.00 28.91 ? 303 CYS B CB 1 ATOM 2055 S SG . CYS B 2 5 ? -46.481 10.203 15.697 1.00 32.46 ? 303 CYS B SG 1 ATOM 2056 N N . THR B 2 6 ? -42.535 6.920 16.750 1.00 29.80 ? 304 THR B N 1 ATOM 2057 C CA . THR B 2 6 ? -41.491 5.954 16.403 1.00 29.84 ? 304 THR B CA 1 ATOM 2058 C C . THR B 2 6 ? -41.576 4.703 17.264 1.00 33.90 ? 304 THR B C 1 ATOM 2059 O O . THR B 2 6 ? -41.945 4.779 18.439 1.00 33.49 ? 304 THR B O 1 ATOM 2060 C CB . THR B 2 6 ? -40.089 6.577 16.502 1.00 39.21 ? 304 THR B CB 1 ATOM 2061 O OG1 . THR B 2 6 ? -39.763 6.816 17.869 1.00 40.18 ? 304 THR B OG1 1 ATOM 2062 C CG2 . THR B 2 6 ? -39.937 7.849 15.678 1.00 36.99 ? 304 THR B CG2 1 ATOM 2063 N N . ASN B 2 7 ? -41.205 3.558 16.680 1.00 30.46 ? 305 ASN B N 1 ATOM 2064 C CA . ASN B 2 7 ? -41.185 2.278 17.373 1.00 30.32 ? 305 ASN B CA 1 ATOM 2065 C C . ASN B 2 7 ? -39.806 1.646 17.203 1.00 33.68 ? 305 ASN B C 1 ATOM 2066 O O . ASN B 2 7 ? -39.432 1.240 16.100 1.00 33.09 ? 305 ASN B O 1 ATOM 2067 C CB . ASN B 2 7 ? -42.314 1.361 16.888 1.00 32.02 ? 305 ASN B CB 1 ATOM 2068 C CG . ASN B 2 7 ? -42.425 0.054 17.637 1.00 54.60 ? 305 ASN B CG 1 ATOM 2069 O OD1 . ASN B 2 7 ? -41.765 -0.174 18.664 1.00 46.47 ? 305 ASN B OD1 1 ATOM 2070 N ND2 . ASN B 2 7 ? -43.275 -0.831 17.134 1.00 49.12 ? 305 ASN B ND2 1 ATOM 2071 N N . THR B 2 8 ? -39.042 1.601 18.303 1.00 30.07 ? 306 THR B N 1 ATOM 2072 C CA . THR B 2 8 ? -37.677 1.076 18.316 1.00 29.70 ? 306 THR B CA 1 ATOM 2073 C C . THR B 2 8 ? -37.541 -0.230 19.117 1.00 32.08 ? 306 THR B C 1 ATOM 2074 O O . THR B 2 8 ? -36.435 -0.568 19.548 1.00 31.88 ? 306 THR B O 1 ATOM 2075 C CB . THR B 2 8 ? -36.697 2.169 18.779 1.00 39.89 ? 306 THR B CB 1 ATOM 2076 O OG1 . THR B 2 8 ? -36.947 2.497 20.147 1.00 39.30 ? 306 THR B OG1 1 ATOM 2077 C CG2 . THR B 2 8 ? -36.731 3.424 17.900 1.00 39.91 ? 306 THR B CG2 1 ATOM 2078 N N . THR B 2 9 ? -38.659 -0.968 19.292 1.00 27.33 ? 307 THR B N 1 ATOM 2079 C CA . THR B 2 9 ? -38.730 -2.234 20.035 1.00 26.48 ? 307 THR B CA 1 ATOM 2080 C C . THR B 2 9 ? -37.827 -3.327 19.446 1.00 28.10 ? 307 THR B C 1 ATOM 2081 O O . THR B 2 9 ? -37.148 -4.006 20.212 1.00 27.27 ? 307 THR B O 1 ATOM 2082 C CB . THR B 2 9 ? -40.197 -2.670 20.234 1.00 35.32 ? 307 THR B CB 1 ATOM 2083 O OG1 . THR B 2 9 ? -40.914 -1.602 20.853 1.00 36.09 ? 307 THR B OG1 1 ATOM 2084 C CG2 . THR B 2 9 ? -40.344 -3.932 21.085 1.00 34.81 ? 307 THR B CG2 1 ATOM 2085 N N . ALA B 2 10 ? -37.808 -3.481 18.102 1.00 23.59 ? 308 ALA B N 1 ATOM 2086 C CA . ALA B 2 10 ? -36.999 -4.489 17.398 1.00 22.77 ? 308 ALA B CA 1 ATOM 2087 C C . ALA B 2 10 ? -35.505 -4.397 17.729 1.00 24.92 ? 308 ALA B C 1 ATOM 2088 O O . ALA B 2 10 ? -34.913 -5.406 18.111 1.00 24.33 ? 308 ALA B O 1 ATOM 2089 C CB . ALA B 2 10 ? -37.220 -4.399 15.896 1.00 23.48 ? 308 ALA B CB 1 ATOM 2090 N N . ALA B 2 11 ? -34.910 -3.194 17.613 1.00 21.00 ? 309 ALA B N 1 ATOM 2091 C CA . ALA B 2 11 ? -33.495 -2.968 17.921 1.00 20.59 ? 309 ALA B CA 1 ATOM 2092 C C . ALA B 2 11 ? -33.224 -3.070 19.423 1.00 24.19 ? 309 ALA B C 1 ATOM 2093 O O . ALA B 2 11 ? -32.173 -3.582 19.814 1.00 23.57 ? 309 ALA B O 1 ATOM 2094 C CB . ALA B 2 11 ? -33.048 -1.615 17.394 1.00 21.27 ? 309 ALA B CB 1 ATOM 2095 N N . SER B 2 12 ? -34.182 -2.601 20.258 1.00 20.73 ? 310 SER B N 1 ATOM 2096 C CA . SER B 2 12 ? -34.093 -2.639 21.720 1.00 20.65 ? 310 SER B CA 1 ATOM 2097 C C . SER B 2 12 ? -34.122 -4.076 22.244 1.00 23.69 ? 310 SER B C 1 ATOM 2098 O O . SER B 2 12 ? -33.315 -4.411 23.107 1.00 23.29 ? 310 SER B O 1 ATOM 2099 C CB . SER B 2 12 ? -35.209 -1.812 22.353 1.00 24.64 ? 310 SER B CB 1 ATOM 2100 O OG . SER B 2 12 ? -35.060 -1.724 23.760 1.00 35.49 ? 310 SER B OG 1 ATOM 2101 N N . THR B 2 13 ? -35.030 -4.924 21.706 1.00 19.97 ? 311 THR B N 1 ATOM 2102 C CA . THR B 2 13 ? -35.172 -6.341 22.076 1.00 19.49 ? 311 THR B CA 1 ATOM 2103 C C . THR B 2 13 ? -33.901 -7.106 21.701 1.00 22.99 ? 311 THR B C 1 ATOM 2104 O O . THR B 2 13 ? -33.439 -7.944 22.481 1.00 22.72 ? 311 THR B O 1 ATOM 2105 C CB . THR B 2 13 ? -36.450 -6.949 21.449 1.00 26.87 ? 311 THR B CB 1 ATOM 2106 O OG1 . THR B 2 13 ? -37.576 -6.158 21.830 1.00 26.16 ? 311 THR B OG1 1 ATOM 2107 C CG2 . THR B 2 13 ? -36.695 -8.401 21.866 1.00 25.51 ? 311 THR B CG2 1 ATOM 2108 N N . TYR B 2 14 ? -33.327 -6.793 20.522 1.00 18.99 ? 312 TYR B N 1 ATOM 2109 C CA . TYR B 2 14 ? -32.105 -7.426 20.037 1.00 18.56 ? 312 TYR B CA 1 ATOM 2110 C C . TYR B 2 14 ? -30.878 -7.093 20.891 1.00 22.49 ? 312 TYR B C 1 ATOM 2111 O O . TYR B 2 14 ? -30.210 -8.011 21.362 1.00 21.59 ? 312 TYR B O 1 ATOM 2112 C CB . TYR B 2 14 ? -31.857 -7.117 18.546 1.00 19.59 ? 312 TYR B CB 1 ATOM 2113 C CG . TYR B 2 14 ? -30.592 -7.761 18.025 1.00 21.13 ? 312 TYR B CG 1 ATOM 2114 C CD1 . TYR B 2 14 ? -30.548 -9.122 17.732 1.00 23.08 ? 312 TYR B CD1 1 ATOM 2115 C CD2 . TYR B 2 14 ? -29.417 -7.026 17.890 1.00 21.70 ? 312 TYR B CD2 1 ATOM 2116 C CE1 . TYR B 2 14 ? -29.374 -9.730 17.300 1.00 23.24 ? 312 TYR B CE1 1 ATOM 2117 C CE2 . TYR B 2 14 ? -28.236 -7.624 17.457 1.00 22.48 ? 312 TYR B CE2 1 ATOM 2118 C CZ . TYR B 2 14 ? -28.216 -8.979 17.176 1.00 29.10 ? 312 TYR B CZ 1 ATOM 2119 O OH . TYR B 2 14 ? -27.053 -9.575 16.760 1.00 28.84 ? 312 TYR B OH 1 ATOM 2120 N N . LEU B 2 15 ? -30.584 -5.793 21.080 1.00 19.41 ? 313 LEU B N 1 ATOM 2121 C CA . LEU B 2 15 ? -29.415 -5.331 21.833 1.00 19.32 ? 313 LEU B CA 1 ATOM 2122 C C . LEU B 2 15 ? -29.453 -5.606 23.337 1.00 24.01 ? 313 LEU B C 1 ATOM 2123 O O . LEU B 2 15 ? -28.395 -5.633 23.968 1.00 23.48 ? 313 LEU B O 1 ATOM 2124 C CB . LEU B 2 15 ? -29.082 -3.860 21.520 1.00 19.12 ? 313 LEU B CB 1 ATOM 2125 C CG . LEU B 2 15 ? -28.671 -3.568 20.069 1.00 23.20 ? 313 LEU B CG 1 ATOM 2126 C CD1 . LEU B 2 15 ? -28.728 -2.109 19.777 1.00 23.17 ? 313 LEU B CD1 1 ATOM 2127 C CD2 . LEU B 2 15 ? -27.284 -4.087 19.752 1.00 24.22 ? 313 LEU B CD2 1 ATOM 2128 N N . ASN B 2 16 ? -30.654 -5.848 23.901 1.00 21.54 ? 314 ASN B N 1 ATOM 2129 C CA . ASN B 2 16 ? -30.819 -6.168 25.320 1.00 21.66 ? 314 ASN B CA 1 ATOM 2130 C C . ASN B 2 16 ? -30.732 -7.664 25.622 1.00 26.63 ? 314 ASN B C 1 ATOM 2131 O O . ASN B 2 16 ? -30.787 -8.053 26.790 1.00 26.33 ? 314 ASN B O 1 ATOM 2132 C CB . ASN B 2 16 ? -32.077 -5.531 25.906 1.00 21.58 ? 314 ASN B CB 1 ATOM 2133 C CG . ASN B 2 16 ? -31.895 -4.069 26.218 1.00 37.62 ? 314 ASN B CG 1 ATOM 2134 O OD1 . ASN B 2 16 ? -31.064 -3.686 27.049 1.00 30.61 ? 314 ASN B OD1 1 ATOM 2135 N ND2 . ASN B 2 16 ? -32.669 -3.220 25.562 1.00 26.97 ? 314 ASN B ND2 1 ATOM 2136 N N . ASN B 2 17 ? -30.569 -8.499 24.576 1.00 23.89 ? 315 ASN B N 1 ATOM 2137 C CA . ASN B 2 17 ? -30.402 -9.944 24.730 1.00 24.12 ? 315 ASN B CA 1 ATOM 2138 C C . ASN B 2 17 ? -29.004 -10.179 25.335 1.00 28.11 ? 315 ASN B C 1 ATOM 2139 O O . ASN B 2 17 ? -28.022 -9.676 24.778 1.00 27.47 ? 315 ASN B O 1 ATOM 2140 C CB . ASN B 2 17 ? -30.555 -10.660 23.382 1.00 25.77 ? 315 ASN B CB 1 ATOM 2141 C CG . ASN B 2 17 ? -30.459 -12.162 23.470 1.00 49.92 ? 315 ASN B CG 1 ATOM 2142 O OD1 . ASN B 2 17 ? -29.403 -12.753 23.232 1.00 41.76 ? 315 ASN B OD1 1 ATOM 2143 N ND2 . ASN B 2 17 ? -31.562 -12.811 23.810 1.00 45.03 ? 315 ASN B ND2 1 ATOM 2144 N N . PRO B 2 18 ? -28.903 -10.869 26.501 1.00 24.91 ? 316 PRO B N 1 ATOM 2145 C CA . PRO B 2 18 ? -27.585 -11.064 27.143 1.00 24.79 ? 316 PRO B CA 1 ATOM 2146 C C . PRO B 2 18 ? -26.474 -11.635 26.260 1.00 28.56 ? 316 PRO B C 1 ATOM 2147 O O . PRO B 2 18 ? -25.331 -11.198 26.387 1.00 27.99 ? 316 PRO B O 1 ATOM 2148 C CB . PRO B 2 18 ? -27.895 -11.966 28.345 1.00 26.69 ? 316 PRO B CB 1 ATOM 2149 C CG . PRO B 2 18 ? -29.254 -12.543 28.070 1.00 31.16 ? 316 PRO B CG 1 ATOM 2150 C CD . PRO B 2 18 ? -29.977 -11.489 27.302 1.00 26.51 ? 316 PRO B CD 1 ATOM 2151 N N . TYR B 2 19 ? -26.811 -12.575 25.353 1.00 25.40 ? 317 TYR B N 1 ATOM 2152 C CA . TYR B 2 19 ? -25.859 -13.198 24.429 1.00 25.51 ? 317 TYR B CA 1 ATOM 2153 C C . TYR B 2 19 ? -25.362 -12.223 23.358 1.00 28.28 ? 317 TYR B C 1 ATOM 2154 O O . TYR B 2 19 ? -24.223 -12.346 22.903 1.00 27.63 ? 317 TYR B O 1 ATOM 2155 C CB . TYR B 2 19 ? -26.448 -14.470 23.801 1.00 27.55 ? 317 TYR B CB 1 ATOM 2156 C CG . TYR B 2 19 ? -26.762 -15.548 24.816 1.00 30.50 ? 317 TYR B CG 1 ATOM 2157 C CD1 . TYR B 2 19 ? -25.771 -16.412 25.275 1.00 32.87 ? 317 TYR B CD1 1 ATOM 2158 C CD2 . TYR B 2 19 ? -28.048 -15.700 25.325 1.00 31.45 ? 317 TYR B CD2 1 ATOM 2159 C CE1 . TYR B 2 19 ? -26.052 -17.399 26.220 1.00 34.17 ? 317 TYR B CE1 1 ATOM 2160 C CE2 . TYR B 2 19 ? -28.341 -16.681 26.272 1.00 32.57 ? 317 TYR B CE2 1 ATOM 2161 C CZ . TYR B 2 19 ? -27.340 -17.531 26.713 1.00 40.69 ? 317 TYR B CZ 1 ATOM 2162 O OH . TYR B 2 19 ? -27.627 -18.505 27.638 1.00 42.32 ? 317 TYR B OH 1 ATOM 2163 N N . VAL B 2 20 ? -26.209 -11.251 22.968 1.00 24.33 ? 318 VAL B N 1 ATOM 2164 C CA . VAL B 2 20 ? -25.867 -10.204 22.001 1.00 23.68 ? 318 VAL B CA 1 ATOM 2165 C C . VAL B 2 20 ? -24.862 -9.250 22.669 1.00 26.33 ? 318 VAL B C 1 ATOM 2166 O O . VAL B 2 20 ? -23.853 -8.901 22.055 1.00 25.86 ? 318 VAL B O 1 ATOM 2167 C CB . VAL B 2 20 ? -27.135 -9.483 21.465 1.00 27.56 ? 318 VAL B CB 1 ATOM 2168 C CG1 . VAL B 2 20 ? -26.792 -8.189 20.726 1.00 27.42 ? 318 VAL B CG1 1 ATOM 2169 C CG2 . VAL B 2 20 ? -27.951 -10.413 20.573 1.00 27.29 ? 318 VAL B CG2 1 ATOM 2170 N N . ARG B 2 21 ? -25.122 -8.877 23.942 1.00 22.31 ? 319 ARG B N 1 ATOM 2171 C CA . ARG B 2 21 ? -24.256 -8.017 24.755 1.00 21.82 ? 319 ARG B CA 1 ATOM 2172 C C . ARG B 2 21 ? -22.872 -8.657 24.933 1.00 25.50 ? 319 ARG B C 1 ATOM 2173 O O . ARG B 2 21 ? -21.865 -7.953 24.845 1.00 24.92 ? 319 ARG B O 1 ATOM 2174 C CB . ARG B 2 21 ? -24.897 -7.738 26.120 1.00 21.11 ? 319 ARG B CB 1 ATOM 2175 C CG . ARG B 2 21 ? -25.923 -6.611 26.103 1.00 27.32 ? 319 ARG B CG 1 ATOM 2176 C CD . ARG B 2 21 ? -26.536 -6.369 27.472 1.00 30.71 ? 319 ARG B CD 1 ATOM 2177 N NE . ARG B 2 21 ? -25.553 -5.880 28.444 1.00 33.44 ? 319 ARG B NE 1 ATOM 2178 C CZ . ARG B 2 21 ? -25.749 -4.849 29.260 1.00 44.61 ? 319 ARG B CZ 1 ATOM 2179 N NH1 . ARG B 2 21 ? -26.895 -4.179 29.234 1.00 32.00 ? 319 ARG B NH1 1 ATOM 2180 N NH2 . ARG B 2 21 ? -24.802 -4.481 30.112 1.00 28.63 ? 319 ARG B NH2 1 ATOM 2181 N N . LYS B 2 22 ? -22.829 -9.997 25.138 1.00 22.18 ? 320 LYS B N 1 ATOM 2182 C CA . LYS B 2 22 ? -21.584 -10.761 25.278 1.00 21.94 ? 320 LYS B CA 1 ATOM 2183 C C . LYS B 2 22 ? -20.792 -10.751 23.972 1.00 25.49 ? 320 LYS B C 1 ATOM 2184 O O . LYS B 2 22 ? -19.583 -10.517 23.999 1.00 25.10 ? 320 LYS B O 1 ATOM 2185 C CB . LYS B 2 22 ? -21.851 -12.213 25.733 1.00 24.55 ? 320 LYS B CB 1 ATOM 2186 C CG . LYS B 2 22 ? -22.299 -12.386 27.196 1.00 40.62 ? 320 LYS B CG 1 ATOM 2187 C CD . LYS B 2 22 ? -21.369 -11.758 28.256 1.00 50.68 ? 320 LYS B CD 1 ATOM 2188 C CE . LYS B 2 22 ? -20.014 -12.415 28.391 1.00 61.12 ? 320 LYS B CE 1 ATOM 2189 N NZ . LYS B 2 22 ? -19.167 -11.714 29.391 1.00 70.03 ? 320 LYS B NZ 1 ATOM 2190 N N . ALA B 2 23 ? -21.485 -10.972 22.832 1.00 22.10 ? 321 ALA B N 1 ATOM 2191 C CA . ALA B 2 23 ? -20.908 -10.981 21.483 1.00 21.76 ? 321 ALA B CA 1 ATOM 2192 C C . ALA B 2 23 ? -20.373 -9.603 21.087 1.00 24.60 ? 321 ALA B C 1 ATOM 2193 O O . ALA B 2 23 ? -19.410 -9.519 20.323 1.00 24.24 ? 321 ALA B O 1 ATOM 2194 C CB . ALA B 2 23 ? -21.947 -11.447 20.474 1.00 22.55 ? 321 ALA B CB 1 ATOM 2195 N N . LEU B 2 24 ? -20.990 -8.527 21.620 1.00 20.54 ? 322 LEU B N 1 ATOM 2196 C CA . LEU B 2 24 ? -20.581 -7.147 21.359 1.00 19.95 ? 322 LEU B CA 1 ATOM 2197 C C . LEU B 2 24 ? -19.582 -6.609 22.395 1.00 24.30 ? 322 LEU B C 1 ATOM 2198 O O . LEU B 2 24 ? -19.241 -5.424 22.363 1.00 23.74 ? 322 LEU B O 1 ATOM 2199 C CB . LEU B 2 24 ? -21.798 -6.216 21.223 1.00 19.62 ? 322 LEU B CB 1 ATOM 2200 C CG . LEU B 2 24 ? -22.724 -6.447 20.027 1.00 23.73 ? 322 LEU B CG 1 ATOM 2201 C CD1 . LEU B 2 24 ? -23.934 -5.565 20.124 1.00 23.70 ? 322 LEU B CD1 1 ATOM 2202 C CD2 . LEU B 2 24 ? -22.009 -6.223 18.697 1.00 25.22 ? 322 LEU B CD2 1 ATOM 2203 N N . ASN B 2 25 ? -19.096 -7.494 23.295 1.00 21.55 ? 323 ASN B N 1 ATOM 2204 C CA . ASN B 2 25 ? -18.111 -7.199 24.348 1.00 21.54 ? 323 ASN B CA 1 ATOM 2205 C C . ASN B 2 25 ? -18.574 -6.093 25.307 1.00 26.11 ? 323 ASN B C 1 ATOM 2206 O O . ASN B 2 25 ? -17.793 -5.215 25.689 1.00 25.81 ? 323 ASN B O 1 ATOM 2207 C CB . ASN B 2 25 ? -16.717 -6.919 23.750 1.00 20.29 ? 323 ASN B CB 1 ATOM 2208 C CG . ASN B 2 25 ? -16.293 -7.927 22.711 1.00 34.15 ? 323 ASN B CG 1 ATOM 2209 O OD1 . ASN B 2 25 ? -16.164 -9.122 22.986 1.00 29.89 ? 323 ASN B OD1 1 ATOM 2210 N ND2 . ASN B 2 25 ? -16.085 -7.467 21.488 1.00 23.15 ? 323 ASN B ND2 1 ATOM 2211 N N . ILE B 2 26 ? -19.854 -6.149 25.697 1.00 23.22 ? 324 ILE B N 1 ATOM 2212 C CA . ILE B 2 26 ? -20.454 -5.177 26.607 1.00 23.06 ? 324 ILE B CA 1 ATOM 2213 C C . ILE B 2 26 ? -20.306 -5.652 28.056 1.00 28.28 ? 324 ILE B C 1 ATOM 2214 O O . ILE B 2 26 ? -20.765 -6.755 28.365 1.00 28.01 ? 324 ILE B O 1 ATOM 2215 C CB . ILE B 2 26 ? -21.941 -4.881 26.240 1.00 25.80 ? 324 ILE B CB 1 ATOM 2216 C CG1 . ILE B 2 26 ? -22.142 -4.497 24.742 1.00 25.86 ? 324 ILE B CG1 1 ATOM 2217 C CG2 . ILE B 2 26 ? -22.589 -3.879 27.206 1.00 26.58 ? 324 ILE B CG2 1 ATOM 2218 C CD1 . ILE B 2 26 ? -21.291 -3.314 24.177 1.00 30.97 ? 324 ILE B CD1 1 ATOM 2219 N N . PRO B 2 27 ? -19.713 -4.830 28.963 1.00 25.80 ? 325 PRO B N 1 ATOM 2220 C CA . PRO B 2 27 ? -19.611 -5.245 30.374 1.00 25.93 ? 325 PRO B CA 1 ATOM 2221 C C . PRO B 2 27 ? -20.999 -5.431 30.985 1.00 30.37 ? 325 PRO B C 1 ATOM 2222 O O . PRO B 2 27 ? -21.887 -4.602 30.765 1.00 30.01 ? 325 PRO B O 1 ATOM 2223 C CB . PRO B 2 27 ? -18.835 -4.097 31.035 1.00 27.63 ? 325 PRO B CB 1 ATOM 2224 C CG . PRO B 2 27 ? -18.174 -3.369 29.909 1.00 31.92 ? 325 PRO B CG 1 ATOM 2225 C CD . PRO B 2 27 ? -19.122 -3.493 28.759 1.00 27.38 ? 325 PRO B CD 1 ATOM 2226 N N . GLU B 2 28 ? -21.192 -6.557 31.693 1.00 26.92 ? 326 GLU B N 1 ATOM 2227 C CA . GLU B 2 28 ? -22.454 -6.970 32.315 1.00 26.79 ? 326 GLU B CA 1 ATOM 2228 C C . GLU B 2 28 ? -23.063 -5.983 33.316 1.00 30.58 ? 326 GLU B C 1 ATOM 2229 O O . GLU B 2 28 ? -24.288 -5.928 33.428 1.00 29.64 ? 326 GLU B O 1 ATOM 2230 C CB . GLU B 2 28 ? -22.320 -8.371 32.933 1.00 28.16 ? 326 GLU B CB 1 ATOM 2231 C CG . GLU B 2 28 ? -22.300 -9.490 31.902 1.00 38.49 ? 326 GLU B CG 1 ATOM 2232 C CD . GLU B 2 28 ? -21.826 -10.846 32.395 1.00 59.53 ? 326 GLU B CD 1 ATOM 2233 O OE1 . GLU B 2 28 ? -22.206 -11.249 33.519 1.00 52.20 ? 326 GLU B OE1 1 ATOM 2234 O OE2 . GLU B 2 28 ? -21.099 -11.524 31.634 1.00 54.66 ? 326 GLU B OE2 1 ATOM 2235 N N . GLN B 2 29 ? -22.223 -5.206 34.027 1.00 27.85 ? 327 GLN B N 1 ATOM 2236 C CA . GLN B 2 29 ? -22.669 -4.228 35.031 1.00 28.15 ? 327 GLN B CA 1 ATOM 2237 C C . GLN B 2 29 ? -23.384 -2.994 34.454 1.00 32.28 ? 327 GLN B C 1 ATOM 2238 O O . GLN B 2 29 ? -24.058 -2.281 35.202 1.00 32.42 ? 327 GLN B O 1 ATOM 2239 C CB . GLN B 2 29 ? -21.522 -3.822 35.981 1.00 29.77 ? 327 GLN B CB 1 ATOM 2240 C CG . GLN B 2 29 ? -20.413 -2.989 35.339 1.00 50.18 ? 327 GLN B CG 1 ATOM 2241 C CD . GLN B 2 29 ? -19.580 -2.285 36.378 1.00 75.68 ? 327 GLN B CD 1 ATOM 2242 O OE1 . GLN B 2 29 ? -18.609 -2.832 36.910 1.00 72.34 ? 327 GLN B OE1 1 ATOM 2243 N NE2 . GLN B 2 29 ? -19.941 -1.047 36.686 1.00 69.61 ? 327 GLN B NE2 1 ATOM 2244 N N . LEU B 2 30 ? -23.234 -2.740 33.139 1.00 28.25 ? 328 LEU B N 1 ATOM 2245 C CA . LEU B 2 30 ? -23.849 -1.592 32.468 1.00 27.65 ? 328 LEU B CA 1 ATOM 2246 C C . LEU B 2 30 ? -25.374 -1.683 32.383 1.00 30.55 ? 328 LEU B C 1 ATOM 2247 O O . LEU B 2 30 ? -25.895 -2.778 32.156 1.00 29.99 ? 328 LEU B O 1 ATOM 2248 C CB . LEU B 2 30 ? -23.240 -1.359 31.076 1.00 27.59 ? 328 LEU B CB 1 ATOM 2249 C CG . LEU B 2 30 ? -21.827 -0.780 31.035 1.00 32.15 ? 328 LEU B CG 1 ATOM 2250 C CD1 . LEU B 2 30 ? -21.373 -0.610 29.620 1.00 32.32 ? 328 LEU B CD1 1 ATOM 2251 C CD2 . LEU B 2 30 ? -21.742 0.568 31.749 1.00 34.55 ? 328 LEU B CD2 1 ATOM 2252 N N . PRO B 2 31 ? -26.107 -0.547 32.544 1.00 26.65 ? 329 PRO B N 1 ATOM 2253 C CA . PRO B 2 31 ? -27.581 -0.603 32.480 1.00 26.30 ? 329 PRO B CA 1 ATOM 2254 C C . PRO B 2 31 ? -28.140 -0.993 31.107 1.00 29.80 ? 329 PRO B C 1 ATOM 2255 O O . PRO B 2 31 ? -27.387 -1.077 30.132 1.00 29.43 ? 329 PRO B O 1 ATOM 2256 C CB . PRO B 2 31 ? -28.005 0.812 32.893 1.00 28.03 ? 329 PRO B CB 1 ATOM 2257 C CG . PRO B 2 31 ? -26.845 1.669 32.540 1.00 32.43 ? 329 PRO B CG 1 ATOM 2258 C CD . PRO B 2 31 ? -25.640 0.827 32.826 1.00 28.09 ? 329 PRO B CD 1 ATOM 2259 N N . GLN B 2 32 ? -29.463 -1.244 31.042 1.00 25.86 ? 330 GLN B N 1 ATOM 2260 C CA . GLN B 2 32 ? -30.167 -1.640 29.820 1.00 25.43 ? 330 GLN B CA 1 ATOM 2261 C C . GLN B 2 32 ? -29.972 -0.670 28.651 1.00 27.64 ? 330 GLN B C 1 ATOM 2262 O O . GLN B 2 32 ? -29.779 0.533 28.855 1.00 26.67 ? 330 GLN B O 1 ATOM 2263 C CB . GLN B 2 32 ? -31.660 -1.921 30.080 1.00 26.99 ? 330 GLN B CB 1 ATOM 2264 C CG . GLN B 2 32 ? -32.470 -0.728 30.603 1.00 44.29 ? 330 GLN B CG 1 ATOM 2265 C CD . GLN B 2 32 ? -33.957 -0.879 30.368 1.00 65.88 ? 330 GLN B CD 1 ATOM 2266 O OE1 . GLN B 2 32 ? -34.601 -0.011 29.770 1.00 61.60 ? 330 GLN B OE1 1 ATOM 2267 N NE2 . GLN B 2 32 ? -34.543 -1.973 30.841 1.00 59.62 ? 330 GLN B NE2 1 ATOM 2268 N N . TRP B 2 33 ? -29.999 -1.211 27.430 1.00 23.44 ? 331 TRP B N 1 ATOM 2269 C CA . TRP B 2 33 ? -29.829 -0.422 26.219 1.00 22.74 ? 331 TRP B CA 1 ATOM 2270 C C . TRP B 2 33 ? -31.123 0.285 25.837 1.00 27.04 ? 331 TRP B C 1 ATOM 2271 O O . TRP B 2 33 ? -32.164 -0.357 25.681 1.00 26.55 ? 331 TRP B O 1 ATOM 2272 C CB . TRP B 2 33 ? -29.318 -1.293 25.061 1.00 20.99 ? 331 TRP B CB 1 ATOM 2273 C CG . TRP B 2 33 ? -28.919 -0.496 23.856 1.00 21.61 ? 331 TRP B CG 1 ATOM 2274 C CD1 . TRP B 2 33 ? -27.696 0.049 23.602 1.00 24.43 ? 331 TRP B CD1 1 ATOM 2275 C CD2 . TRP B 2 33 ? -29.763 -0.120 22.761 1.00 21.30 ? 331 TRP B CD2 1 ATOM 2276 N NE1 . TRP B 2 33 ? -27.723 0.741 22.414 1.00 23.63 ? 331 TRP B NE1 1 ATOM 2277 C CE2 . TRP B 2 33 ? -28.982 0.661 21.880 1.00 25.02 ? 331 TRP B CE2 1 ATOM 2278 C CE3 . TRP B 2 33 ? -31.104 -0.378 22.429 1.00 22.52 ? 331 TRP B CE3 1 ATOM 2279 C CZ2 . TRP B 2 33 ? -29.494 1.180 20.686 1.00 24.27 ? 331 TRP B CZ2 1 ATOM 2280 C CZ3 . TRP B 2 33 ? -31.613 0.148 21.253 1.00 23.96 ? 331 TRP B CZ3 1 ATOM 2281 C CH2 . TRP B 2 33 ? -30.803 0.890 20.382 1.00 24.54 ? 331 TRP B CH2 1 ATOM 2282 N N . ASP B 2 34 ? -31.041 1.612 25.682 1.00 23.78 ? 332 ASP B N 1 ATOM 2283 C CA . ASP B 2 34 ? -32.140 2.470 25.251 1.00 23.79 ? 332 ASP B CA 1 ATOM 2284 C C . ASP B 2 34 ? -31.701 3.174 23.972 1.00 27.43 ? 332 ASP B C 1 ATOM 2285 O O . ASP B 2 34 ? -30.545 3.596 23.873 1.00 26.64 ? 332 ASP B O 1 ATOM 2286 C CB . ASP B 2 34 ? -32.495 3.515 26.327 1.00 25.68 ? 332 ASP B CB 1 ATOM 2287 C CG . ASP B 2 34 ? -32.953 2.960 27.664 1.00 36.94 ? 332 ASP B CG 1 ATOM 2288 O OD1 . ASP B 2 34 ? -33.711 1.962 27.670 1.00 37.52 ? 332 ASP B OD1 1 ATOM 2289 O OD2 . ASP B 2 34 ? -32.610 3.563 28.704 1.00 42.79 ? 332 ASP B OD2 1 ATOM 2290 N N . MET B 2 35 ? -32.617 3.293 22.997 1.00 24.17 ? 333 MET B N 1 ATOM 2291 C CA . MET B 2 35 ? -32.371 3.955 21.712 1.00 24.41 ? 333 MET B CA 1 ATOM 2292 C C . MET B 2 35 ? -31.961 5.400 21.888 1.00 26.00 ? 333 MET B C 1 ATOM 2293 O O . MET B 2 35 ? -31.017 5.859 21.246 1.00 24.75 ? 333 MET B O 1 ATOM 2294 C CB . MET B 2 35 ? -33.624 3.903 20.842 1.00 27.37 ? 333 MET B CB 1 ATOM 2295 C CG . MET B 2 35 ? -33.538 2.889 19.781 1.00 32.06 ? 333 MET B CG 1 ATOM 2296 S SD . MET B 2 35 ? -32.546 3.398 18.369 1.00 37.23 ? 333 MET B SD 1 ATOM 2297 C CE . MET B 2 35 ? -32.941 2.072 17.276 1.00 33.96 ? 333 MET B CE 1 ATOM 2298 N N . CYS B 2 36 ? -32.693 6.114 22.747 1.00 21.75 ? 334 CYS B N 1 ATOM 2299 C CA . CYS B 2 36 ? -32.462 7.515 23.048 1.00 21.46 ? 334 CYS B CA 1 ATOM 2300 C C . CYS B 2 36 ? -32.476 7.697 24.560 1.00 25.72 ? 334 CYS B C 1 ATOM 2301 O O . CYS B 2 36 ? -33.411 7.246 25.226 1.00 25.29 ? 334 CYS B O 1 ATOM 2302 C CB . CYS B 2 36 ? -33.506 8.390 22.358 1.00 21.55 ? 334 CYS B CB 1 ATOM 2303 S SG . CYS B 2 36 ? -33.496 8.283 20.548 1.00 25.18 ? 334 CYS B SG 1 ATOM 2304 N N . ASN B 2 37 ? -31.417 8.313 25.105 1.00 22.53 ? 335 ASN B N 1 ATOM 2305 C CA . ASN B 2 37 ? -31.297 8.554 26.540 1.00 22.43 ? 335 ASN B CA 1 ATOM 2306 C C . ASN B 2 37 ? -31.971 9.877 26.892 1.00 26.55 ? 335 ASN B C 1 ATOM 2307 O O . ASN B 2 37 ? -31.495 10.939 26.481 1.00 25.46 ? 335 ASN B O 1 ATOM 2308 C CB . ASN B 2 37 ? -29.827 8.538 26.980 1.00 22.45 ? 335 ASN B CB 1 ATOM 2309 C CG . ASN B 2 37 ? -29.621 8.442 28.476 1.00 40.08 ? 335 ASN B CG 1 ATOM 2310 O OD1 . ASN B 2 37 ? -30.085 9.278 29.257 1.00 32.99 ? 335 ASN B OD1 1 ATOM 2311 N ND2 . ASN B 2 37 ? -28.858 7.454 28.907 1.00 31.97 ? 335 ASN B ND2 1 ATOM 2312 N N . PHE B 2 38 ? -33.082 9.808 27.649 1.00 24.22 ? 336 PHE B N 1 ATOM 2313 C CA . PHE B 2 38 ? -33.841 10.987 28.072 1.00 24.52 ? 336 PHE B CA 1 ATOM 2314 C C . PHE B 2 38 ? -33.024 11.925 28.965 1.00 27.63 ? 336 PHE B C 1 ATOM 2315 O O . PHE B 2 38 ? -33.105 13.142 28.790 1.00 27.11 ? 336 PHE B O 1 ATOM 2316 C CB . PHE B 2 38 ? -35.173 10.591 28.742 1.00 26.85 ? 336 PHE B CB 1 ATOM 2317 C CG . PHE B 2 38 ? -36.020 11.763 29.186 1.00 29.24 ? 336 PHE B CG 1 ATOM 2318 C CD1 . PHE B 2 38 ? -36.679 12.560 28.255 1.00 33.09 ? 336 PHE B CD1 1 ATOM 2319 C CD2 . PHE B 2 38 ? -36.156 12.072 30.534 1.00 32.08 ? 336 PHE B CD2 1 ATOM 2320 C CE1 . PHE B 2 38 ? -37.452 13.651 28.667 1.00 34.36 ? 336 PHE B CE1 1 ATOM 2321 C CE2 . PHE B 2 38 ? -36.930 13.162 30.944 1.00 35.12 ? 336 PHE B CE2 1 ATOM 2322 C CZ . PHE B 2 38 ? -37.573 13.943 30.008 1.00 33.46 ? 336 PHE B CZ 1 ATOM 2323 N N . LEU B 2 39 ? -32.232 11.358 29.898 1.00 24.01 ? 337 LEU B N 1 ATOM 2324 C CA . LEU B 2 39 ? -31.394 12.119 30.831 1.00 23.92 ? 337 LEU B CA 1 ATOM 2325 C C . LEU B 2 39 ? -30.292 12.912 30.133 1.00 26.75 ? 337 LEU B C 1 ATOM 2326 O O . LEU B 2 39 ? -30.031 14.047 30.530 1.00 26.53 ? 337 LEU B O 1 ATOM 2327 C CB . LEU B 2 39 ? -30.820 11.227 31.944 1.00 24.24 ? 337 LEU B CB 1 ATOM 2328 C CG . LEU B 2 39 ? -31.830 10.611 32.923 1.00 29.51 ? 337 LEU B CG 1 ATOM 2329 C CD1 . LEU B 2 39 ? -31.171 9.551 33.782 1.00 30.02 ? 337 LEU B CD1 1 ATOM 2330 C CD2 . LEU B 2 39 ? -32.483 11.672 33.806 1.00 32.56 ? 337 LEU B CD2 1 ATOM 2331 N N . VAL B 2 40 ? -29.672 12.332 29.080 1.00 22.13 ? 338 VAL B N 1 ATOM 2332 C CA . VAL B 2 40 ? -28.634 12.989 28.273 1.00 21.39 ? 338 VAL B CA 1 ATOM 2333 C C . VAL B 2 40 ? -29.261 14.197 27.551 1.00 24.60 ? 338 VAL B C 1 ATOM 2334 O O . VAL B 2 40 ? -28.687 15.285 27.579 1.00 23.72 ? 338 VAL B O 1 ATOM 2335 C CB . VAL B 2 40 ? -27.925 12.000 27.299 1.00 25.03 ? 338 VAL B CB 1 ATOM 2336 C CG1 . VAL B 2 40 ? -27.036 12.731 26.290 1.00 24.73 ? 338 VAL B CG1 1 ATOM 2337 C CG2 . VAL B 2 40 ? -27.108 10.966 28.068 1.00 24.89 ? 338 VAL B CG2 1 ATOM 2338 N N . ASN B 2 41 ? -30.455 14.004 26.953 1.00 21.24 ? 339 ASN B N 1 ATOM 2339 C CA . ASN B 2 41 ? -31.202 15.037 26.234 1.00 21.22 ? 339 ASN B CA 1 ATOM 2340 C C . ASN B 2 41 ? -31.632 16.187 27.147 1.00 25.25 ? 339 ASN B C 1 ATOM 2341 O O . ASN B 2 41 ? -31.450 17.346 26.776 1.00 24.55 ? 339 ASN B O 1 ATOM 2342 C CB . ASN B 2 41 ? -32.418 14.429 25.538 1.00 22.71 ? 339 ASN B CB 1 ATOM 2343 C CG . ASN B 2 41 ? -33.144 15.382 24.625 1.00 44.52 ? 339 ASN B CG 1 ATOM 2344 O OD1 . ASN B 2 41 ? -34.073 16.079 25.032 1.00 40.68 ? 339 ASN B OD1 1 ATOM 2345 N ND2 . ASN B 2 41 ? -32.733 15.439 23.372 1.00 36.06 ? 339 ASN B ND2 1 ATOM 2346 N N . LEU B 2 42 ? -32.197 15.863 28.330 1.00 22.70 ? 340 LEU B N 1 ATOM 2347 C CA . LEU B 2 42 ? -32.668 16.828 29.328 1.00 22.88 ? 340 LEU B CA 1 ATOM 2348 C C . LEU B 2 42 ? -31.534 17.740 29.827 1.00 26.65 ? 340 LEU B C 1 ATOM 2349 O O . LEU B 2 42 ? -31.719 18.954 29.911 1.00 26.39 ? 340 LEU B O 1 ATOM 2350 C CB . LEU B 2 42 ? -33.327 16.081 30.511 1.00 23.05 ? 340 LEU B CB 1 ATOM 2351 C CG . LEU B 2 42 ? -33.915 16.939 31.644 1.00 27.85 ? 340 LEU B CG 1 ATOM 2352 C CD1 . LEU B 2 42 ? -35.368 17.299 31.371 1.00 28.03 ? 340 LEU B CD1 1 ATOM 2353 C CD2 . LEU B 2 42 ? -33.801 16.226 32.972 1.00 30.49 ? 340 LEU B CD2 1 ATOM 2354 N N . GLN B 2 43 ? -30.369 17.147 30.134 1.00 23.08 ? 341 GLN B N 1 ATOM 2355 C CA . GLN B 2 43 ? -29.185 17.833 30.653 1.00 22.83 ? 341 GLN B CA 1 ATOM 2356 C C . GLN B 2 43 ? -28.326 18.490 29.567 1.00 26.45 ? 341 GLN B C 1 ATOM 2357 O O . GLN B 2 43 ? -27.403 19.234 29.907 1.00 26.16 ? 341 GLN B O 1 ATOM 2358 C CB . GLN B 2 43 ? -28.315 16.848 31.445 1.00 24.10 ? 341 GLN B CB 1 ATOM 2359 C CG . GLN B 2 43 ? -28.908 16.372 32.757 1.00 32.27 ? 341 GLN B CG 1 ATOM 2360 C CD . GLN B 2 43 ? -28.021 15.330 33.381 1.00 45.47 ? 341 GLN B CD 1 ATOM 2361 O OE1 . GLN B 2 43 ? -27.998 14.165 32.967 1.00 41.25 ? 341 GLN B OE1 1 ATOM 2362 N NE2 . GLN B 2 43 ? -27.309 15.710 34.426 1.00 34.98 ? 341 GLN B NE2 1 ATOM 2363 N N . TYR B 2 44 ? -28.603 18.204 28.277 1.00 22.40 ? 342 TYR B N 1 ATOM 2364 C CA . TYR B 2 44 ? -27.818 18.744 27.163 1.00 22.04 ? 342 TYR B CA 1 ATOM 2365 C C . TYR B 2 44 ? -27.976 20.249 27.003 1.00 25.92 ? 342 TYR B C 1 ATOM 2366 O O . TYR B 2 44 ? -29.098 20.748 26.879 1.00 25.62 ? 342 TYR B O 1 ATOM 2367 C CB . TYR B 2 44 ? -28.143 18.028 25.841 1.00 22.80 ? 342 TYR B CB 1 ATOM 2368 C CG . TYR B 2 44 ? -27.049 18.148 24.799 1.00 24.07 ? 342 TYR B CG 1 ATOM 2369 C CD1 . TYR B 2 44 ? -26.963 19.265 23.972 1.00 24.58 ? 342 TYR B CD1 1 ATOM 2370 C CD2 . TYR B 2 44 ? -26.104 17.140 24.633 1.00 25.82 ? 342 TYR B CD2 1 ATOM 2371 C CE1 . TYR B 2 44 ? -25.962 19.378 23.009 1.00 25.20 ? 342 TYR B CE1 1 ATOM 2372 C CE2 . TYR B 2 44 ? -25.104 17.238 23.667 1.00 26.14 ? 342 TYR B CE2 1 ATOM 2373 C CZ . TYR B 2 44 ? -25.036 18.361 22.858 1.00 30.66 ? 342 TYR B CZ 1 ATOM 2374 O OH . TYR B 2 44 ? -24.052 18.466 21.905 1.00 29.29 ? 342 TYR B OH 1 ATOM 2375 N N . ARG B 2 45 ? -26.843 20.965 26.988 1.00 22.48 ? 343 ARG B N 1 ATOM 2376 C CA . ARG B 2 45 ? -26.837 22.407 26.789 1.00 22.22 ? 343 ARG B CA 1 ATOM 2377 C C . ARG B 2 45 ? -26.453 22.714 25.340 1.00 25.31 ? 343 ARG B C 1 ATOM 2378 O O . ARG B 2 45 ? -25.306 22.513 24.944 1.00 24.28 ? 343 ARG B O 1 ATOM 2379 C CB . ARG B 2 45 ? -25.912 23.122 27.795 1.00 23.02 ? 343 ARG B CB 1 ATOM 2380 C CG . ARG B 2 45 ? -26.165 24.625 27.860 1.00 35.95 ? 343 ARG B CG 1 ATOM 2381 C CD . ARG B 2 45 ? -25.115 25.375 28.653 1.00 49.25 ? 343 ARG B CD 1 ATOM 2382 N NE . ARG B 2 45 ? -25.324 26.821 28.565 1.00 60.77 ? 343 ARG B NE 1 ATOM 2383 C CZ . ARG B 2 45 ? -24.620 27.730 29.234 1.00 77.16 ? 343 ARG B CZ 1 ATOM 2384 N NH1 . ARG B 2 45 ? -23.651 27.353 30.061 1.00 65.12 ? 343 ARG B NH1 1 ATOM 2385 N NH2 . ARG B 2 45 ? -24.883 29.021 29.087 1.00 64.96 ? 343 ARG B NH2 1 ATOM 2386 N N . ARG B 2 46 ? -27.435 23.163 24.546 1.00 22.25 ? 344 ARG B N 1 ATOM 2387 C CA . ARG B 2 46 ? -27.248 23.547 23.146 1.00 22.12 ? 344 ARG B CA 1 ATOM 2388 C C . ARG B 2 46 ? -26.539 24.901 23.142 1.00 26.55 ? 344 ARG B C 1 ATOM 2389 O O . ARG B 2 46 ? -26.990 25.824 23.824 1.00 26.70 ? 344 ARG B O 1 ATOM 2390 C CB . ARG B 2 46 ? -28.605 23.637 22.423 1.00 21.65 ? 344 ARG B CB 1 ATOM 2391 C CG . ARG B 2 46 ? -29.333 22.299 22.309 1.00 29.73 ? 344 ARG B CG 1 ATOM 2392 C CD . ARG B 2 46 ? -30.817 22.492 22.074 1.00 34.97 ? 344 ARG B CD 1 ATOM 2393 N NE . ARG B 2 46 ? -31.549 21.229 22.163 1.00 40.17 ? 344 ARG B NE 1 ATOM 2394 C CZ . ARG B 2 46 ? -31.972 20.526 21.117 1.00 52.67 ? 344 ARG B CZ 1 ATOM 2395 N NH1 . ARG B 2 46 ? -31.746 20.958 19.881 1.00 35.55 ? 344 ARG B NH1 1 ATOM 2396 N NH2 . ARG B 2 46 ? -32.629 19.388 21.297 1.00 41.01 ? 344 ARG B NH2 1 ATOM 2397 N N . LEU B 2 47 ? -25.409 25.006 22.424 1.00 22.99 ? 345 LEU B N 1 ATOM 2398 C CA . LEU B 2 47 ? -24.615 26.239 22.393 1.00 22.59 ? 345 LEU B CA 1 ATOM 2399 C C . LEU B 2 47 ? -24.700 27.006 21.085 1.00 26.57 ? 345 LEU B C 1 ATOM 2400 O O . LEU B 2 47 ? -24.809 28.233 21.109 1.00 26.20 ? 345 LEU B O 1 ATOM 2401 C CB . LEU B 2 47 ? -23.141 25.969 22.757 1.00 22.57 ? 345 LEU B CB 1 ATOM 2402 C CG . LEU B 2 47 ? -22.846 25.277 24.097 1.00 26.96 ? 345 LEU B CG 1 ATOM 2403 C CD1 . LEU B 2 47 ? -21.364 25.035 24.258 1.00 26.91 ? 345 LEU B CD1 1 ATOM 2404 C CD2 . LEU B 2 47 ? -23.373 26.083 25.281 1.00 28.80 ? 345 LEU B CD2 1 ATOM 2405 N N . TYR B 2 48 ? -24.623 26.296 19.949 1.00 22.82 ? 346 TYR B N 1 ATOM 2406 C CA . TYR B 2 48 ? -24.655 26.915 18.628 1.00 22.54 ? 346 TYR B CA 1 ATOM 2407 C C . TYR B 2 48 ? -26.066 26.997 18.065 1.00 26.22 ? 346 TYR B C 1 ATOM 2408 O O . TYR B 2 48 ? -26.846 26.052 18.205 1.00 26.09 ? 346 TYR B O 1 ATOM 2409 C CB . TYR B 2 48 ? -23.739 26.163 17.650 1.00 23.66 ? 346 TYR B CB 1 ATOM 2410 C CG . TYR B 2 48 ? -22.296 26.043 18.091 1.00 25.66 ? 346 TYR B CG 1 ATOM 2411 C CD1 . TYR B 2 48 ? -21.384 27.068 17.852 1.00 27.77 ? 346 TYR B CD1 1 ATOM 2412 C CD2 . TYR B 2 48 ? -21.827 24.883 18.700 1.00 26.56 ? 346 TYR B CD2 1 ATOM 2413 C CE1 . TYR B 2 48 ? -20.051 26.959 18.248 1.00 28.76 ? 346 TYR B CE1 1 ATOM 2414 C CE2 . TYR B 2 48 ? -20.496 24.760 19.098 1.00 27.57 ? 346 TYR B CE2 1 ATOM 2415 C CZ . TYR B 2 48 ? -19.608 25.797 18.860 1.00 35.61 ? 346 TYR B CZ 1 ATOM 2416 O OH . TYR B 2 48 ? -18.293 25.675 19.244 1.00 36.75 ? 346 TYR B OH 1 ATOM 2417 N N . ARG B 2 49 ? -26.385 28.124 17.413 1.00 22.33 ? 347 ARG B N 1 ATOM 2418 C CA . ARG B 2 49 ? -27.681 28.349 16.776 1.00 21.96 ? 347 ARG B CA 1 ATOM 2419 C C . ARG B 2 49 ? -27.586 28.203 15.257 1.00 25.01 ? 347 ARG B C 1 ATOM 2420 O O . ARG B 2 49 ? -28.602 27.976 14.599 1.00 24.73 ? 347 ARG B O 1 ATOM 2421 C CB . ARG B 2 49 ? -28.293 29.706 17.185 1.00 23.37 ? 347 ARG B CB 1 ATOM 2422 C CG . ARG B 2 49 ? -28.598 29.844 18.684 1.00 36.75 ? 347 ARG B CG 1 ATOM 2423 C CD . ARG B 2 49 ? -29.708 28.924 19.178 1.00 49.85 ? 347 ARG B CD 1 ATOM 2424 N NE . ARG B 2 49 ? -29.393 28.358 20.492 1.00 60.17 ? 347 ARG B NE 1 ATOM 2425 C CZ . ARG B 2 49 ? -30.146 27.470 21.133 1.00 74.64 ? 347 ARG B CZ 1 ATOM 2426 N NH1 . ARG B 2 49 ? -31.277 27.033 20.592 1.00 61.46 ? 347 ARG B NH1 1 ATOM 2427 N NH2 . ARG B 2 49 ? -29.776 27.013 22.322 1.00 63.18 ? 347 ARG B NH2 1 ATOM 2428 N N . SER B 2 50 ? -26.360 28.314 14.708 1.00 21.00 ? 348 SER B N 1 ATOM 2429 C CA . SER B 2 50 ? -26.073 28.181 13.278 1.00 20.22 ? 348 SER B CA 1 ATOM 2430 C C . SER B 2 50 ? -24.695 27.568 13.044 1.00 23.12 ? 348 SER B C 1 ATOM 2431 O O . SER B 2 50 ? -23.755 27.853 13.788 1.00 22.87 ? 348 SER B O 1 ATOM 2432 C CB . SER B 2 50 ? -26.162 29.534 12.580 1.00 23.45 ? 348 SER B CB 1 ATOM 2433 O OG . SER B 2 50 ? -25.944 29.404 11.184 1.00 29.51 ? 348 SER B OG 1 ATOM 2434 N N . MET B 2 51 ? -24.579 26.740 11.993 1.00 18.50 ? 349 MET B N 1 ATOM 2435 C CA . MET B 2 51 ? -23.330 26.086 11.605 1.00 17.58 ? 349 MET B CA 1 ATOM 2436 C C . MET B 2 51 ? -22.622 26.851 10.481 1.00 22.12 ? 349 MET B C 1 ATOM 2437 O O . MET B 2 51 ? -21.621 26.369 9.949 1.00 21.67 ? 349 MET B O 1 ATOM 2438 C CB . MET B 2 51 ? -23.586 24.616 11.209 1.00 19.30 ? 349 MET B CB 1 ATOM 2439 C CG . MET B 2 51 ? -23.897 23.706 12.385 1.00 22.03 ? 349 MET B CG 1 ATOM 2440 S SD . MET B 2 51 ? -22.455 23.292 13.398 1.00 25.19 ? 349 MET B SD 1 ATOM 2441 C CE . MET B 2 51 ? -22.745 24.296 14.784 1.00 21.94 ? 349 MET B CE 1 ATOM 2442 N N . ASN B 2 52 ? -23.139 28.053 10.136 1.00 19.58 ? 350 ASN B N 1 ATOM 2443 C CA . ASN B 2 52 ? -22.617 28.933 9.084 1.00 19.57 ? 350 ASN B CA 1 ATOM 2444 C C . ASN B 2 52 ? -21.098 29.126 9.181 1.00 23.36 ? 350 ASN B C 1 ATOM 2445 O O . ASN B 2 52 ? -20.397 28.857 8.207 1.00 22.80 ? 350 ASN B O 1 ATOM 2446 C CB . ASN B 2 52 ? -23.358 30.276 9.084 1.00 20.59 ? 350 ASN B CB 1 ATOM 2447 C CG . ASN B 2 52 ? -22.910 31.227 8.004 1.00 37.24 ? 350 ASN B CG 1 ATOM 2448 O OD1 . ASN B 2 52 ? -22.069 32.100 8.226 1.00 33.08 ? 350 ASN B OD1 1 ATOM 2449 N ND2 . ASN B 2 52 ? -23.454 31.076 6.808 1.00 26.95 ? 350 ASN B ND2 1 ATOM 2450 N N . SER B 2 53 ? -20.597 29.524 10.367 1.00 20.47 ? 351 SER B N 1 ATOM 2451 C CA . SER B 2 53 ? -19.171 29.737 10.632 1.00 20.61 ? 351 SER B CA 1 ATOM 2452 C C . SER B 2 53 ? -18.341 28.452 10.497 1.00 24.16 ? 351 SER B C 1 ATOM 2453 O O . SER B 2 53 ? -17.243 28.508 9.943 1.00 23.99 ? 351 SER B O 1 ATOM 2454 C CB . SER B 2 53 ? -18.963 30.382 11.998 1.00 24.95 ? 351 SER B CB 1 ATOM 2455 O OG . SER B 2 53 ? -19.529 29.598 13.035 1.00 35.68 ? 351 SER B OG 1 ATOM 2456 N N . GLN B 2 54 ? -18.878 27.300 10.966 1.00 19.85 ? 352 GLN B N 1 ATOM 2457 C CA . GLN B 2 54 ? -18.217 25.989 10.888 1.00 19.04 ? 352 GLN B CA 1 ATOM 2458 C C . GLN B 2 54 ? -18.009 25.559 9.439 1.00 22.89 ? 352 GLN B C 1 ATOM 2459 O O . GLN B 2 54 ? -16.899 25.161 9.081 1.00 22.27 ? 352 GLN B O 1 ATOM 2460 C CB . GLN B 2 54 ? -19.012 24.911 11.647 1.00 20.03 ? 352 GLN B CB 1 ATOM 2461 C CG . GLN B 2 54 ? -18.811 24.924 13.161 1.00 26.95 ? 352 GLN B CG 1 ATOM 2462 C CD . GLN B 2 54 ? -19.598 25.986 13.897 1.00 41.91 ? 352 GLN B CD 1 ATOM 2463 O OE1 . GLN B 2 54 ? -20.398 26.743 13.328 1.00 35.07 ? 352 GLN B OE1 1 ATOM 2464 N NE2 . GLN B 2 54 ? -19.386 26.056 15.198 1.00 34.12 ? 352 GLN B NE2 1 ATOM 2465 N N . TYR B 2 55 ? -19.072 25.655 8.607 1.00 19.27 ? 353 TYR B N 1 ATOM 2466 C CA . TYR B 2 55 ? -19.020 25.298 7.190 1.00 18.96 ? 353 TYR B CA 1 ATOM 2467 C C . TYR B 2 55 ? -18.099 26.220 6.401 1.00 23.25 ? 353 TYR B C 1 ATOM 2468 O O . TYR B 2 55 ? -17.331 25.728 5.576 1.00 22.82 ? 353 TYR B O 1 ATOM 2469 C CB . TYR B 2 55 ? -20.425 25.241 6.571 1.00 19.66 ? 353 TYR B CB 1 ATOM 2470 C CG . TYR B 2 55 ? -21.166 23.956 6.878 1.00 20.70 ? 353 TYR B CG 1 ATOM 2471 C CD1 . TYR B 2 55 ? -20.898 22.787 6.173 1.00 22.55 ? 353 TYR B CD1 1 ATOM 2472 C CD2 . TYR B 2 55 ? -22.145 23.911 7.866 1.00 21.12 ? 353 TYR B CD2 1 ATOM 2473 C CE1 . TYR B 2 55 ? -21.575 21.602 6.453 1.00 23.02 ? 353 TYR B CE1 1 ATOM 2474 C CE2 . TYR B 2 55 ? -22.850 22.738 8.135 1.00 21.77 ? 353 TYR B CE2 1 ATOM 2475 C CZ . TYR B 2 55 ? -22.560 21.584 7.425 1.00 27.77 ? 353 TYR B CZ 1 ATOM 2476 O OH . TYR B 2 55 ? -23.227 20.414 7.686 1.00 26.78 ? 353 TYR B OH 1 ATOM 2477 N N . LEU B 2 56 ? -18.139 27.543 6.681 1.00 20.40 ? 354 LEU B N 1 ATOM 2478 C CA . LEU B 2 56 ? -17.264 28.523 6.021 1.00 20.53 ? 354 LEU B CA 1 ATOM 2479 C C . LEU B 2 56 ? -15.788 28.283 6.373 1.00 25.00 ? 354 LEU B C 1 ATOM 2480 O O . LEU B 2 56 ? -14.922 28.472 5.519 1.00 24.50 ? 354 LEU B O 1 ATOM 2481 C CB . LEU B 2 56 ? -17.684 29.975 6.320 1.00 20.52 ? 354 LEU B CB 1 ATOM 2482 C CG . LEU B 2 56 ? -18.975 30.482 5.648 1.00 25.06 ? 354 LEU B CG 1 ATOM 2483 C CD1 . LEU B 2 56 ? -19.374 31.843 6.198 1.00 25.10 ? 354 LEU B CD1 1 ATOM 2484 C CD2 . LEU B 2 56 ? -18.831 30.569 4.132 1.00 26.75 ? 354 LEU B CD2 1 ATOM 2485 N N . LYS B 2 57 ? -15.517 27.812 7.611 1.00 22.40 ? 355 LYS B N 1 ATOM 2486 C CA . LYS B 2 57 ? -14.172 27.462 8.079 1.00 22.38 ? 355 LYS B CA 1 ATOM 2487 C C . LYS B 2 57 ? -13.686 26.208 7.338 1.00 25.91 ? 355 LYS B C 1 ATOM 2488 O O . LYS B 2 57 ? -12.526 26.151 6.930 1.00 25.68 ? 355 LYS B O 1 ATOM 2489 C CB . LYS B 2 57 ? -14.170 27.225 9.598 1.00 25.15 ? 355 LYS B CB 1 ATOM 2490 C CG . LYS B 2 57 ? -12.778 27.254 10.231 1.00 42.37 ? 355 LYS B CG 1 ATOM 2491 C CD . LYS B 2 57 ? -12.821 27.108 11.752 1.00 53.98 ? 355 LYS B CD 1 ATOM 2492 C CE . LYS B 2 57 ? -12.998 28.425 12.474 1.00 65.66 ? 355 LYS B CE 1 ATOM 2493 N NZ . LYS B 2 57 ? -13.052 28.241 13.948 1.00 75.97 ? 355 LYS B NZ 1 ATOM 2494 N N . LEU B 2 58 ? -14.585 25.220 7.146 1.00 21.77 ? 356 LEU B N 1 ATOM 2495 C CA . LEU B 2 58 ? -14.279 23.973 6.444 1.00 21.31 ? 356 LEU B CA 1 ATOM 2496 C C . LEU B 2 58 ? -14.094 24.178 4.940 1.00 25.51 ? 356 LEU B C 1 ATOM 2497 O O . LEU B 2 58 ? -13.253 23.510 4.336 1.00 25.08 ? 356 LEU B O 1 ATOM 2498 C CB . LEU B 2 58 ? -15.353 22.909 6.717 1.00 21.16 ? 356 LEU B CB 1 ATOM 2499 C CG . LEU B 2 58 ? -15.373 22.336 8.134 1.00 25.26 ? 356 LEU B CG 1 ATOM 2500 C CD1 . LEU B 2 58 ? -16.723 21.735 8.461 1.00 25.12 ? 356 LEU B CD1 1 ATOM 2501 C CD2 . LEU B 2 58 ? -14.232 21.351 8.352 1.00 27.32 ? 356 LEU B CD2 1 ATOM 2502 N N . LEU B 2 59 ? -14.877 25.097 4.341 1.00 21.87 ? 357 LEU B N 1 ATOM 2503 C CA . LEU B 2 59 ? -14.807 25.403 2.912 1.00 22.00 ? 357 LEU B CA 1 ATOM 2504 C C . LEU B 2 59 ? -13.607 26.282 2.532 1.00 26.79 ? 357 LEU B C 1 ATOM 2505 O O . LEU B 2 59 ? -13.172 26.230 1.383 1.00 26.15 ? 357 LEU B O 1 ATOM 2506 C CB . LEU B 2 59 ? -16.125 26.020 2.405 1.00 21.93 ? 357 LEU B CB 1 ATOM 2507 C CG . LEU B 2 59 ? -17.320 25.062 2.285 1.00 26.23 ? 357 LEU B CG 1 ATOM 2508 C CD1 . LEU B 2 59 ? -18.633 25.806 2.408 1.00 26.28 ? 357 LEU B CD1 1 ATOM 2509 C CD2 . LEU B 2 59 ? -17.270 24.264 0.995 1.00 27.95 ? 357 LEU B CD2 1 ATOM 2510 N N . SER B 2 60 ? -13.069 27.072 3.491 1.00 24.51 ? 358 SER B N 1 ATOM 2511 C CA . SER B 2 60 ? -11.924 27.973 3.280 1.00 24.72 ? 358 SER B CA 1 ATOM 2512 C C . SER B 2 60 ? -10.670 27.251 2.775 1.00 29.41 ? 358 SER B C 1 ATOM 2513 O O . SER B 2 60 ? -9.992 27.757 1.879 1.00 29.17 ? 358 SER B O 1 ATOM 2514 C CB . SER B 2 60 ? -11.609 28.758 4.550 1.00 28.24 ? 358 SER B CB 1 ATOM 2515 O OG . SER B 2 60 ? -11.060 27.925 5.559 1.00 37.04 ? 358 SER B OG 1 ATOM 2516 N N . SER B 2 61 ? -10.380 26.062 3.334 1.00 26.41 ? 359 SER B N 1 ATOM 2517 C CA . SER B 2 61 ? -9.221 25.246 2.966 1.00 26.17 ? 359 SER B CA 1 ATOM 2518 C C . SER B 2 61 ? -9.330 24.647 1.560 1.00 29.42 ? 359 SER B C 1 ATOM 2519 O O . SER B 2 61 ? -8.299 24.348 0.955 1.00 29.17 ? 359 SER B O 1 ATOM 2520 C CB . SER B 2 61 ? -9.005 24.136 3.990 1.00 29.83 ? 359 SER B CB 1 ATOM 2521 O OG . SER B 2 61 ? -10.116 23.256 4.027 1.00 38.23 ? 359 SER B OG 1 ATOM 2522 N N . GLN B 2 62 ? -10.579 24.453 1.054 1.00 25.18 ? 360 GLN B N 1 ATOM 2523 C CA . GLN B 2 62 ? -10.905 23.865 -0.259 1.00 24.46 ? 360 GLN B CA 1 ATOM 2524 C C . GLN B 2 62 ? -10.363 22.419 -0.408 1.00 27.48 ? 360 GLN B C 1 ATOM 2525 O O . GLN B 2 62 ? -10.164 21.933 -1.526 1.00 26.76 ? 360 GLN B O 1 ATOM 2526 C CB . GLN B 2 62 ? -10.455 24.783 -1.426 1.00 25.64 ? 360 GLN B CB 1 ATOM 2527 C CG . GLN B 2 62 ? -11.177 26.130 -1.496 1.00 35.92 ? 360 GLN B CG 1 ATOM 2528 C CD . GLN B 2 62 ? -12.538 26.017 -2.135 1.00 47.21 ? 360 GLN B CD 1 ATOM 2529 O OE1 . GLN B 2 62 ? -12.672 25.986 -3.361 1.00 38.98 ? 360 GLN B OE1 1 ATOM 2530 N NE2 . GLN B 2 62 ? -13.579 25.953 -1.317 1.00 37.95 ? 360 GLN B NE2 1 ATOM 2531 N N . LYS B 2 63 ? -10.144 21.740 0.734 1.00 23.96 ? 361 LYS B N 1 ATOM 2532 C CA . LYS B 2 63 ? -9.603 20.380 0.820 1.00 23.69 ? 361 LYS B CA 1 ATOM 2533 C C . LYS B 2 63 ? -10.694 19.324 1.017 1.00 26.97 ? 361 LYS B C 1 ATOM 2534 O O . LYS B 2 63 ? -10.423 18.134 0.837 1.00 26.54 ? 361 LYS B O 1 ATOM 2535 C CB . LYS B 2 63 ? -8.612 20.277 1.997 1.00 26.23 ? 361 LYS B CB 1 ATOM 2536 C CG . LYS B 2 63 ? -7.371 21.158 1.895 1.00 41.35 ? 361 LYS B CG 1 ATOM 2537 C CD . LYS B 2 63 ? -6.569 21.092 3.188 1.00 51.77 ? 361 LYS B CD 1 ATOM 2538 C CE . LYS B 2 63 ? -5.395 22.038 3.196 1.00 63.37 ? 361 LYS B CE 1 ATOM 2539 N NZ . LYS B 2 63 ? -4.667 21.993 4.492 1.00 72.70 ? 361 LYS B NZ 1 ATOM 2540 N N . TYR B 2 64 ? -11.905 19.745 1.431 1.00 22.76 ? 362 TYR B N 1 ATOM 2541 C CA . TYR B 2 64 ? -12.992 18.815 1.745 1.00 22.33 ? 362 TYR B CA 1 ATOM 2542 C C . TYR B 2 64 ? -14.261 18.998 0.931 1.00 25.89 ? 362 TYR B C 1 ATOM 2543 O O . TYR B 2 64 ? -14.653 20.125 0.619 1.00 25.57 ? 362 TYR B O 1 ATOM 2544 C CB . TYR B 2 64 ? -13.319 18.841 3.253 1.00 23.42 ? 362 TYR B CB 1 ATOM 2545 C CG . TYR B 2 64 ? -12.121 19.102 4.142 1.00 25.05 ? 362 TYR B CG 1 ATOM 2546 C CD1 . TYR B 2 64 ? -11.138 18.133 4.324 1.00 26.95 ? 362 TYR B CD1 1 ATOM 2547 C CD2 . TYR B 2 64 ? -11.959 20.325 4.785 1.00 25.72 ? 362 TYR B CD2 1 ATOM 2548 C CE1 . TYR B 2 64 ? -10.022 18.377 5.122 1.00 27.86 ? 362 TYR B CE1 1 ATOM 2549 C CE2 . TYR B 2 64 ? -10.853 20.575 5.596 1.00 26.54 ? 362 TYR B CE2 1 ATOM 2550 C CZ . TYR B 2 64 ? -9.886 19.598 5.760 1.00 33.93 ? 362 TYR B CZ 1 ATOM 2551 O OH . TYR B 2 64 ? -8.785 19.845 6.543 1.00 35.05 ? 362 TYR B OH 1 ATOM 2552 N N . GLN B 2 65 ? -14.917 17.873 0.617 1.00 21.66 ? 363 GLN B N 1 ATOM 2553 C CA . GLN B 2 65 ? -16.183 17.844 -0.107 1.00 20.88 ? 363 GLN B CA 1 ATOM 2554 C C . GLN B 2 65 ? -17.308 17.715 0.908 1.00 22.87 ? 363 GLN B C 1 ATOM 2555 O O . GLN B 2 65 ? -17.278 16.824 1.758 1.00 22.15 ? 363 GLN B O 1 ATOM 2556 C CB . GLN B 2 65 ? -16.214 16.695 -1.125 1.00 22.37 ? 363 GLN B CB 1 ATOM 2557 C CG . GLN B 2 65 ? -15.162 16.821 -2.231 1.00 37.20 ? 363 GLN B CG 1 ATOM 2558 C CD . GLN B 2 65 ? -15.338 18.016 -3.145 1.00 55.22 ? 363 GLN B CD 1 ATOM 2559 O OE1 . GLN B 2 65 ? -16.452 18.407 -3.509 1.00 50.64 ? 363 GLN B OE1 1 ATOM 2560 N NE2 . GLN B 2 65 ? -14.227 18.600 -3.565 1.00 47.81 ? 363 GLN B NE2 1 ATOM 2561 N N . ILE B 2 66 ? -18.275 18.634 0.857 1.00 18.68 ? 364 ILE B N 1 ATOM 2562 C CA . ILE B 2 66 ? -19.382 18.650 1.811 1.00 17.64 ? 364 ILE B CA 1 ATOM 2563 C C . ILE B 2 66 ? -20.713 18.299 1.148 1.00 19.98 ? 364 ILE B C 1 ATOM 2564 O O . ILE B 2 66 ? -20.990 18.740 0.033 1.00 18.98 ? 364 ILE B O 1 ATOM 2565 C CB . ILE B 2 66 ? -19.421 19.979 2.622 1.00 20.70 ? 364 ILE B CB 1 ATOM 2566 C CG1 . ILE B 2 66 ? -18.044 20.269 3.289 1.00 21.15 ? 364 ILE B CG1 1 ATOM 2567 C CG2 . ILE B 2 66 ? -20.541 19.945 3.670 1.00 21.18 ? 364 ILE B CG2 1 ATOM 2568 C CD1 . ILE B 2 66 ? -17.842 21.676 3.864 1.00 28.66 ? 364 ILE B CD1 1 ATOM 2569 N N . LEU B 2 67 ? -21.527 17.492 1.842 1.00 16.02 ? 365 LEU B N 1 ATOM 2570 C CA . LEU B 2 67 ? -22.844 17.089 1.370 1.00 15.61 ? 365 LEU B CA 1 ATOM 2571 C C . LEU B 2 67 ? -23.902 17.256 2.457 1.00 19.48 ? 365 LEU B C 1 ATOM 2572 O O . LEU B 2 67 ? -23.715 16.794 3.581 1.00 19.31 ? 365 LEU B O 1 ATOM 2573 C CB . LEU B 2 67 ? -22.812 15.630 0.852 1.00 15.40 ? 365 LEU B CB 1 ATOM 2574 C CG . LEU B 2 67 ? -24.158 14.931 0.584 1.00 19.65 ? 365 LEU B CG 1 ATOM 2575 C CD1 . LEU B 2 67 ? -24.858 15.515 -0.621 1.00 19.76 ? 365 LEU B CD1 1 ATOM 2576 C CD2 . LEU B 2 67 ? -23.972 13.443 0.402 1.00 21.21 ? 365 LEU B CD2 1 ATOM 2577 N N . LEU B 2 68 ? -25.014 17.911 2.108 1.00 15.66 ? 366 LEU B N 1 ATOM 2578 C CA . LEU B 2 68 ? -26.176 18.052 2.979 1.00 15.58 ? 366 LEU B CA 1 ATOM 2579 C C . LEU B 2 68 ? -27.330 17.405 2.234 1.00 19.23 ? 366 LEU B C 1 ATOM 2580 O O . LEU B 2 68 ? -27.715 17.878 1.164 1.00 18.88 ? 366 LEU B O 1 ATOM 2581 C CB . LEU B 2 68 ? -26.480 19.520 3.328 1.00 15.68 ? 366 LEU B CB 1 ATOM 2582 C CG . LEU B 2 68 ? -25.832 20.040 4.613 1.00 20.40 ? 366 LEU B CG 1 ATOM 2583 C CD1 . LEU B 2 68 ? -24.402 20.498 4.363 1.00 20.80 ? 366 LEU B CD1 1 ATOM 2584 C CD2 . LEU B 2 68 ? -26.636 21.186 5.195 1.00 21.77 ? 366 LEU B CD2 1 ATOM 2585 N N . TYR B 2 69 ? -27.807 16.263 2.742 1.00 15.26 ? 367 TYR B N 1 ATOM 2586 C CA . TYR B 2 69 ? -28.894 15.530 2.109 1.00 14.92 ? 367 TYR B CA 1 ATOM 2587 C C . TYR B 2 69 ? -30.123 15.444 2.997 1.00 18.45 ? 367 TYR B C 1 ATOM 2588 O O . TYR B 2 69 ? -29.999 15.174 4.187 1.00 17.80 ? 367 TYR B O 1 ATOM 2589 C CB . TYR B 2 69 ? -28.428 14.153 1.606 1.00 15.99 ? 367 TYR B CB 1 ATOM 2590 C CG . TYR B 2 69 ? -28.076 13.145 2.680 1.00 17.21 ? 367 TYR B CG 1 ATOM 2591 C CD1 . TYR B 2 69 ? -26.794 13.088 3.219 1.00 18.88 ? 367 TYR B CD1 1 ATOM 2592 C CD2 . TYR B 2 69 ? -28.999 12.187 3.092 1.00 17.87 ? 367 TYR B CD2 1 ATOM 2593 C CE1 . TYR B 2 69 ? -26.454 12.138 4.180 1.00 19.38 ? 367 TYR B CE1 1 ATOM 2594 C CE2 . TYR B 2 69 ? -28.672 11.234 4.055 1.00 18.66 ? 367 TYR B CE2 1 ATOM 2595 C CZ . TYR B 2 69 ? -27.399 11.214 4.598 1.00 24.31 ? 367 TYR B CZ 1 ATOM 2596 O OH . TYR B 2 69 ? -27.078 10.279 5.552 1.00 22.76 ? 367 TYR B OH 1 ATOM 2597 N N . ASN B 2 70 ? -31.306 15.714 2.431 1.00 15.29 ? 368 ASN B N 1 ATOM 2598 C CA . ASN B 2 70 ? -32.543 15.691 3.200 1.00 15.01 ? 368 ASN B CA 1 ATOM 2599 C C . ASN B 2 70 ? -33.667 14.963 2.506 1.00 19.32 ? 368 ASN B C 1 ATOM 2600 O O . ASN B 2 70 ? -33.949 15.218 1.332 1.00 18.85 ? 368 ASN B O 1 ATOM 2601 C CB . ASN B 2 70 ? -33.019 17.112 3.498 1.00 14.23 ? 368 ASN B CB 1 ATOM 2602 C CG . ASN B 2 70 ? -32.187 17.902 4.467 1.00 24.81 ? 368 ASN B CG 1 ATOM 2603 O OD1 . ASN B 2 70 ? -31.028 18.228 4.208 1.00 15.30 ? 368 ASN B OD1 1 ATOM 2604 N ND2 . ASN B 2 70 ? -32.813 18.336 5.551 1.00 13.84 ? 368 ASN B ND2 1 ATOM 2605 N N . GLY B 2 71 ? -34.355 14.121 3.268 1.00 16.15 ? 369 GLY B N 1 ATOM 2606 C CA . GLY B 2 71 ? -35.569 13.467 2.812 1.00 15.87 ? 369 GLY B CA 1 ATOM 2607 C C . GLY B 2 71 ? -36.627 14.552 2.777 1.00 18.90 ? 369 GLY B C 1 ATOM 2608 O O . GLY B 2 71 ? -36.812 15.254 3.775 1.00 18.23 ? 369 GLY B O 1 ATOM 2609 N N . ASP B 2 72 ? -37.264 14.757 1.612 1.00 14.97 ? 370 ASP B N 1 ATOM 2610 C CA . ASP B 2 72 ? -38.237 15.837 1.421 1.00 14.46 ? 370 ASP B CA 1 ATOM 2611 C C . ASP B 2 72 ? -39.608 15.715 2.111 1.00 17.98 ? 370 ASP B C 1 ATOM 2612 O O . ASP B 2 72 ? -40.391 16.669 2.062 1.00 17.60 ? 370 ASP B O 1 ATOM 2613 C CB . ASP B 2 72 ? -38.351 16.246 -0.058 1.00 16.10 ? 370 ASP B CB 1 ATOM 2614 C CG . ASP B 2 72 ? -38.904 15.192 -0.996 1.00 21.32 ? 370 ASP B CG 1 ATOM 2615 O OD1 . ASP B 2 72 ? -39.418 14.161 -0.503 1.00 20.91 ? 370 ASP B OD1 1 ATOM 2616 O OD2 . ASP B 2 72 ? -38.855 15.411 -2.222 1.00 25.66 ? 370 ASP B OD2 1 ATOM 2617 N N . VAL B 2 73 ? -39.900 14.568 2.753 1.00 13.82 ? 371 VAL B N 1 ATOM 2618 C CA . VAL B 2 73 ? -41.173 14.395 3.464 1.00 13.51 ? 371 VAL B CA 1 ATOM 2619 C C . VAL B 2 73 ? -41.026 14.464 4.998 1.00 17.64 ? 371 VAL B C 1 ATOM 2620 O O . VAL B 2 73 ? -41.995 14.266 5.736 1.00 17.22 ? 371 VAL B O 1 ATOM 2621 C CB . VAL B 2 73 ? -42.084 13.246 2.932 1.00 17.13 ? 371 VAL B CB 1 ATOM 2622 C CG1 . VAL B 2 73 ? -42.252 13.337 1.419 1.00 16.69 ? 371 VAL B CG1 1 ATOM 2623 C CG2 . VAL B 2 73 ? -41.561 11.872 3.333 1.00 16.85 ? 371 VAL B CG2 1 ATOM 2624 N N . ASP B 2 74 ? -39.806 14.793 5.459 1.00 14.77 ? 372 ASP B N 1 ATOM 2625 C CA . ASP B 2 74 ? -39.465 14.975 6.867 1.00 14.48 ? 372 ASP B CA 1 ATOM 2626 C C . ASP B 2 74 ? -39.884 16.374 7.325 1.00 18.02 ? 372 ASP B C 1 ATOM 2627 O O . ASP B 2 74 ? -39.726 17.340 6.577 1.00 17.22 ? 372 ASP B O 1 ATOM 2628 C CB . ASP B 2 74 ? -37.950 14.798 7.071 1.00 16.00 ? 372 ASP B CB 1 ATOM 2629 C CG . ASP B 2 74 ? -37.444 15.099 8.471 1.00 21.13 ? 372 ASP B CG 1 ATOM 2630 O OD1 . ASP B 2 74 ? -38.138 14.736 9.449 1.00 20.91 ? 372 ASP B OD1 1 ATOM 2631 O OD2 . ASP B 2 74 ? -36.339 15.664 8.592 1.00 24.29 ? 372 ASP B OD2 1 ATOM 2632 N N . MET B 2 75 ? -40.390 16.478 8.563 1.00 15.14 ? 373 MET B N 1 ATOM 2633 C CA . MET B 2 75 ? -40.802 17.754 9.156 1.00 15.31 ? 373 MET B CA 1 ATOM 2634 C C . MET B 2 75 ? -39.908 18.159 10.336 1.00 20.93 ? 373 MET B C 1 ATOM 2635 O O . MET B 2 75 ? -39.971 19.312 10.759 1.00 21.16 ? 373 MET B O 1 ATOM 2636 C CB . MET B 2 75 ? -42.280 17.730 9.583 1.00 17.36 ? 373 MET B CB 1 ATOM 2637 C CG . MET B 2 75 ? -43.229 17.290 8.490 1.00 20.52 ? 373 MET B CG 1 ATOM 2638 S SD . MET B 2 75 ? -44.933 17.789 8.792 1.00 24.00 ? 373 MET B SD 1 ATOM 2639 C CE . MET B 2 75 ? -45.390 16.660 10.131 1.00 20.65 ? 373 MET B CE 1 ATOM 2640 N N . ALA B 2 76 ? -39.082 17.224 10.867 1.00 18.37 ? 374 ALA B N 1 ATOM 2641 C CA . ALA B 2 76 ? -38.175 17.492 11.996 1.00 18.62 ? 374 ALA B CA 1 ATOM 2642 C C . ALA B 2 76 ? -37.040 18.433 11.577 1.00 23.10 ? 374 ALA B C 1 ATOM 2643 O O . ALA B 2 76 ? -36.787 19.427 12.258 1.00 22.86 ? 374 ALA B O 1 ATOM 2644 C CB . ALA B 2 76 ? -37.618 16.188 12.553 1.00 19.31 ? 374 ALA B CB 1 ATOM 2645 N N . CYS B 2 77 ? -36.377 18.124 10.446 1.00 19.45 ? 375 CYS B N 1 ATOM 2646 C CA . CYS B 2 77 ? -35.323 18.925 9.830 1.00 19.10 ? 375 CYS B CA 1 ATOM 2647 C C . CYS B 2 77 ? -35.630 18.915 8.335 1.00 20.50 ? 375 CYS B C 1 ATOM 2648 O O . CYS B 2 77 ? -35.017 18.167 7.566 1.00 19.00 ? 375 CYS B O 1 ATOM 2649 C CB . CYS B 2 77 ? -33.938 18.357 10.132 1.00 20.02 ? 375 CYS B CB 1 ATOM 2650 S SG . CYS B 2 77 ? -33.472 18.404 11.883 1.00 24.30 ? 375 CYS B SG 1 ATOM 2651 N N . ASN B 2 78 ? -36.650 19.703 7.941 1.00 16.17 ? 376 ASN B N 1 ATOM 2652 C CA . ASN B 2 78 ? -37.136 19.772 6.567 1.00 15.53 ? 376 ASN B CA 1 ATOM 2653 C C . ASN B 2 78 ? -36.068 20.171 5.547 1.00 18.96 ? 376 ASN B C 1 ATOM 2654 O O . ASN B 2 78 ? -35.121 20.889 5.885 1.00 18.45 ? 376 ASN B O 1 ATOM 2655 C CB . ASN B 2 78 ? -38.410 20.616 6.460 1.00 15.13 ? 376 ASN B CB 1 ATOM 2656 C CG . ASN B 2 78 ? -38.173 22.101 6.443 1.00 26.85 ? 376 ASN B CG 1 ATOM 2657 O OD1 . ASN B 2 78 ? -37.974 22.695 5.385 1.00 20.85 ? 376 ASN B OD1 1 ATOM 2658 N ND2 . ASN B 2 78 ? -38.213 22.731 7.608 1.00 14.44 ? 376 ASN B ND2 1 ATOM 2659 N N . PHE B 2 79 ? -36.224 19.679 4.308 1.00 15.26 ? 377 PHE B N 1 ATOM 2660 C CA . PHE B 2 79 ? -35.307 19.908 3.193 1.00 15.25 ? 377 PHE B CA 1 ATOM 2661 C C . PHE B 2 79 ? -35.069 21.392 2.881 1.00 19.88 ? 377 PHE B C 1 ATOM 2662 O O . PHE B 2 79 ? -33.945 21.759 2.540 1.00 19.63 ? 377 PHE B O 1 ATOM 2663 C CB . PHE B 2 79 ? -35.786 19.146 1.932 1.00 16.89 ? 377 PHE B CB 1 ATOM 2664 C CG . PHE B 2 79 ? -36.947 19.797 1.215 1.00 18.22 ? 377 PHE B CG 1 ATOM 2665 C CD1 . PHE B 2 79 ? -38.255 19.564 1.621 1.00 20.92 ? 377 PHE B CD1 1 ATOM 2666 C CD2 . PHE B 2 79 ? -36.728 20.692 0.172 1.00 20.44 ? 377 PHE B CD2 1 ATOM 2667 C CE1 . PHE B 2 79 ? -39.324 20.199 0.985 1.00 22.01 ? 377 PHE B CE1 1 ATOM 2668 C CE2 . PHE B 2 79 ? -37.795 21.351 -0.439 1.00 23.13 ? 377 PHE B CE2 1 ATOM 2669 C CZ . PHE B 2 79 ? -39.087 21.087 -0.041 1.00 21.01 ? 377 PHE B CZ 1 ATOM 2670 N N . MET B 2 80 ? -36.128 22.230 2.970 1.00 17.01 ? 378 MET B N 1 ATOM 2671 C CA . MET B 2 80 ? -36.062 23.653 2.634 1.00 17.12 ? 378 MET B CA 1 ATOM 2672 C C . MET B 2 80 ? -35.107 24.454 3.510 1.00 20.83 ? 378 MET B C 1 ATOM 2673 O O . MET B 2 80 ? -34.362 25.277 2.983 1.00 20.48 ? 378 MET B O 1 ATOM 2674 C CB . MET B 2 80 ? -37.458 24.289 2.549 1.00 19.63 ? 378 MET B CB 1 ATOM 2675 C CG . MET B 2 80 ? -37.453 25.635 1.860 1.00 23.57 ? 378 MET B CG 1 ATOM 2676 S SD . MET B 2 80 ? -39.063 26.205 1.293 1.00 28.04 ? 378 MET B SD 1 ATOM 2677 C CE . MET B 2 80 ? -39.235 25.222 -0.187 1.00 24.52 ? 378 MET B CE 1 ATOM 2678 N N . GLY B 2 81 ? -35.117 24.184 4.817 1.00 17.48 ? 379 GLY B N 1 ATOM 2679 C CA . GLY B 2 81 ? -34.231 24.825 5.785 1.00 17.32 ? 379 GLY B CA 1 ATOM 2680 C C . GLY B 2 81 ? -32.765 24.604 5.461 1.00 21.22 ? 379 GLY B C 1 ATOM 2681 O O . GLY B 2 81 ? -31.971 25.546 5.515 1.00 19.91 ? 379 GLY B O 1 ATOM 2682 N N . ASP B 2 82 ? -32.405 23.361 5.086 1.00 18.37 ? 380 ASP B N 1 ATOM 2683 C CA . ASP B 2 82 ? -31.036 23.022 4.708 1.00 18.20 ? 380 ASP B CA 1 ATOM 2684 C C . ASP B 2 82 ? -30.668 23.542 3.316 1.00 22.20 ? 380 ASP B C 1 ATOM 2685 O O . ASP B 2 82 ? -29.510 23.902 3.106 1.00 21.24 ? 380 ASP B O 1 ATOM 2686 C CB . ASP B 2 82 ? -30.761 21.524 4.857 1.00 19.99 ? 380 ASP B CB 1 ATOM 2687 C CG . ASP B 2 82 ? -30.529 21.093 6.291 1.00 29.67 ? 380 ASP B CG 1 ATOM 2688 O OD1 . ASP B 2 82 ? -29.732 21.758 6.992 1.00 30.53 ? 380 ASP B OD1 1 ATOM 2689 O OD2 . ASP B 2 82 ? -31.114 20.072 6.704 1.00 33.38 ? 380 ASP B OD2 1 ATOM 2690 N N . GLU B 2 83 ? -31.649 23.613 2.380 1.00 19.26 ? 381 GLU B N 1 ATOM 2691 C CA . GLU B 2 83 ? -31.437 24.167 1.035 1.00 19.05 ? 381 GLU B CA 1 ATOM 2692 C C . GLU B 2 83 ? -31.139 25.663 1.168 1.00 23.97 ? 381 GLU B C 1 ATOM 2693 O O . GLU B 2 83 ? -30.209 26.160 0.527 1.00 23.23 ? 381 GLU B O 1 ATOM 2694 C CB . GLU B 2 83 ? -32.655 23.935 0.120 1.00 20.16 ? 381 GLU B CB 1 ATOM 2695 C CG . GLU B 2 83 ? -32.473 24.501 -1.286 1.00 26.98 ? 381 GLU B CG 1 ATOM 2696 C CD . GLU B 2 83 ? -32.958 23.679 -2.464 1.00 36.21 ? 381 GLU B CD 1 ATOM 2697 O OE1 . GLU B 2 83 ? -33.894 22.864 -2.295 1.00 24.69 ? 381 GLU B OE1 1 ATOM 2698 O OE2 . GLU B 2 83 ? -32.425 23.887 -3.578 1.00 26.06 ? 381 GLU B OE2 1 ATOM 2699 N N . TRP B 2 84 ? -31.922 26.364 2.023 1.00 21.56 ? 382 TRP B N 1 ATOM 2700 C CA . TRP B 2 84 ? -31.763 27.788 2.331 1.00 21.79 ? 382 TRP B CA 1 ATOM 2701 C C . TRP B 2 84 ? -30.377 28.015 2.929 1.00 24.73 ? 382 TRP B C 1 ATOM 2702 O O . TRP B 2 84 ? -29.676 28.933 2.505 1.00 24.31 ? 382 TRP B O 1 ATOM 2703 C CB . TRP B 2 84 ? -32.831 28.250 3.344 1.00 20.96 ? 382 TRP B CB 1 ATOM 2704 C CG . TRP B 2 84 ? -34.215 28.468 2.797 1.00 22.41 ? 382 TRP B CG 1 ATOM 2705 C CD1 . TRP B 2 84 ? -34.640 28.278 1.513 1.00 25.45 ? 382 TRP B CD1 1 ATOM 2706 C CD2 . TRP B 2 84 ? -35.360 28.921 3.536 1.00 22.40 ? 382 TRP B CD2 1 ATOM 2707 N NE1 . TRP B 2 84 ? -35.974 28.602 1.403 1.00 25.17 ? 382 TRP B NE1 1 ATOM 2708 C CE2 . TRP B 2 84 ? -36.443 28.989 2.632 1.00 26.48 ? 382 TRP B CE2 1 ATOM 2709 C CE3 . TRP B 2 84 ? -35.575 29.282 4.878 1.00 23.75 ? 382 TRP B CE3 1 ATOM 2710 C CZ2 . TRP B 2 84 ? -37.724 29.394 3.027 1.00 25.80 ? 382 TRP B CZ2 1 ATOM 2711 C CZ3 . TRP B 2 84 ? -36.842 29.689 5.267 1.00 25.24 ? 382 TRP B CZ3 1 ATOM 2712 C CH2 . TRP B 2 84 ? -37.899 29.746 4.348 1.00 25.89 ? 382 TRP B CH2 1 ATOM 2713 N N . PHE B 2 85 ? -29.981 27.145 3.887 1.00 20.34 ? 383 PHE B N 1 ATOM 2714 C CA . PHE B 2 85 ? -28.693 27.179 4.579 1.00 19.51 ? 383 PHE B CA 1 ATOM 2715 C C . PHE B 2 85 ? -27.495 27.062 3.629 1.00 22.49 ? 383 PHE B C 1 ATOM 2716 O O . PHE B 2 85 ? -26.563 27.860 3.745 1.00 22.49 ? 383 PHE B O 1 ATOM 2717 C CB . PHE B 2 85 ? -28.634 26.105 5.681 1.00 20.97 ? 383 PHE B CB 1 ATOM 2718 C CG . PHE B 2 85 ? -27.371 26.146 6.505 1.00 22.20 ? 383 PHE B CG 1 ATOM 2719 C CD1 . PHE B 2 85 ? -27.258 27.003 7.593 1.00 24.88 ? 383 PHE B CD1 1 ATOM 2720 C CD2 . PHE B 2 85 ? -26.287 25.339 6.183 1.00 24.11 ? 383 PHE B CD2 1 ATOM 2721 C CE1 . PHE B 2 85 ? -26.084 27.048 8.347 1.00 25.62 ? 383 PHE B CE1 1 ATOM 2722 C CE2 . PHE B 2 85 ? -25.113 25.390 6.933 1.00 26.80 ? 383 PHE B CE2 1 ATOM 2723 C CZ . PHE B 2 85 ? -25.019 26.244 8.009 1.00 24.71 ? 383 PHE B CZ 1 ATOM 2724 N N . VAL B 2 86 ? -27.503 26.059 2.721 1.00 18.13 ? 384 VAL B N 1 ATOM 2725 C CA . VAL B 2 86 ? -26.420 25.829 1.750 1.00 17.70 ? 384 VAL B CA 1 ATOM 2726 C C . VAL B 2 86 ? -26.301 27.030 0.798 1.00 21.82 ? 384 VAL B C 1 ATOM 2727 O O . VAL B 2 86 ? -25.192 27.523 0.578 1.00 21.47 ? 384 VAL B O 1 ATOM 2728 C CB . VAL B 2 86 ? -26.543 24.464 1.013 1.00 21.32 ? 384 VAL B CB 1 ATOM 2729 C CG1 . VAL B 2 86 ? -25.501 24.323 -0.096 1.00 21.04 ? 384 VAL B CG1 1 ATOM 2730 C CG2 . VAL B 2 86 ? -26.428 23.300 1.993 1.00 21.23 ? 384 VAL B CG2 1 ATOM 2731 N N . ASP B 2 87 ? -27.446 27.525 0.283 1.00 18.57 ? 385 ASP B N 1 ATOM 2732 C CA . ASP B 2 87 ? -27.502 28.697 -0.600 1.00 18.27 ? 385 ASP B CA 1 ATOM 2733 C C . ASP B 2 87 ? -26.966 29.968 0.080 1.00 22.48 ? 385 ASP B C 1 ATOM 2734 O O . ASP B 2 87 ? -26.273 30.751 -0.578 1.00 21.68 ? 385 ASP B O 1 ATOM 2735 C CB . ASP B 2 87 ? -28.933 28.932 -1.121 1.00 19.58 ? 385 ASP B CB 1 ATOM 2736 C CG . ASP B 2 87 ? -29.441 27.925 -2.141 1.00 26.16 ? 385 ASP B CG 1 ATOM 2737 O OD1 . ASP B 2 87 ? -28.622 27.129 -2.658 1.00 25.89 ? 385 ASP B OD1 1 ATOM 2738 O OD2 . ASP B 2 87 ? -30.649 27.957 -2.449 1.00 30.37 ? 385 ASP B OD2 1 ATOM 2739 N N A SER B 2 88 ? -27.274 30.158 1.384 0.40 19.44 ? 386 SER B N 1 ATOM 2740 N N B SER B 2 88 ? -27.270 30.152 1.383 0.60 19.53 ? 386 SER B N 1 ATOM 2741 C CA A SER B 2 88 ? -26.840 31.316 2.177 0.40 19.39 ? 386 SER B CA 1 ATOM 2742 C CA B SER B 2 88 ? -26.842 31.302 2.189 0.60 19.47 ? 386 SER B CA 1 ATOM 2743 C C A SER B 2 88 ? -25.327 31.354 2.439 0.40 23.36 ? 386 SER B C 1 ATOM 2744 C C B SER B 2 88 ? -25.330 31.348 2.447 0.60 23.47 ? 386 SER B C 1 ATOM 2745 O O A SER B 2 88 ? -24.803 32.413 2.795 0.40 22.98 ? 386 SER B O 1 ATOM 2746 O O B SER B 2 88 ? -24.810 32.408 2.808 0.60 23.16 ? 386 SER B O 1 ATOM 2747 C CB A SER B 2 88 ? -27.624 31.409 3.484 0.40 22.95 ? 386 SER B CB 1 ATOM 2748 C CB B SER B 2 88 ? -27.616 31.357 3.503 0.60 22.91 ? 386 SER B CB 1 ATOM 2749 O OG A SER B 2 88 ? -27.319 30.339 4.363 0.40 31.86 ? 386 SER B OG 1 ATOM 2750 O OG B SER B 2 88 ? -29.000 31.551 3.262 0.60 31.34 ? 386 SER B OG 1 ATOM 2751 N N . LEU B 2 89 ? -24.623 30.215 2.238 1.00 19.86 ? 387 LEU B N 1 ATOM 2752 C CA . LEU B 2 89 ? -23.162 30.115 2.405 1.00 19.74 ? 387 LEU B CA 1 ATOM 2753 C C . LEU B 2 89 ? -22.444 30.883 1.281 1.00 23.43 ? 387 LEU B C 1 ATOM 2754 O O . LEU B 2 89 ? -21.265 31.209 1.418 1.00 22.95 ? 387 LEU B O 1 ATOM 2755 C CB . LEU B 2 89 ? -22.680 28.649 2.461 1.00 19.72 ? 387 LEU B CB 1 ATOM 2756 C CG . LEU B 2 89 ? -23.069 27.825 3.698 1.00 24.40 ? 387 LEU B CG 1 ATOM 2757 C CD1 . LEU B 2 89 ? -22.727 26.371 3.499 1.00 24.42 ? 387 LEU B CD1 1 ATOM 2758 C CD2 . LEU B 2 89 ? -22.374 28.331 4.960 1.00 26.56 ? 387 LEU B CD2 1 ATOM 2759 N N . ASN B 2 90 ? -23.183 31.179 0.183 1.00 20.20 ? 388 ASN B N 1 ATOM 2760 C CA . ASN B 2 90 ? -22.780 31.972 -0.979 1.00 19.95 ? 388 ASN B CA 1 ATOM 2761 C C . ASN B 2 90 ? -21.430 31.537 -1.567 1.00 23.64 ? 388 ASN B C 1 ATOM 2762 O O . ASN B 2 90 ? -20.509 32.344 -1.705 1.00 23.12 ? 388 ASN B O 1 ATOM 2763 C CB . ASN B 2 90 ? -22.823 33.474 -0.623 1.00 20.22 ? 388 ASN B CB 1 ATOM 2764 C CG . ASN B 2 90 ? -22.788 34.427 -1.793 1.00 36.43 ? 388 ASN B CG 1 ATOM 2765 O OD1 . ASN B 2 90 ? -23.323 34.163 -2.874 1.00 29.73 ? 388 ASN B OD1 1 ATOM 2766 N ND2 . ASN B 2 90 ? -22.172 35.578 -1.585 1.00 27.30 ? 388 ASN B ND2 1 ATOM 2767 N N . GLN B 2 91 ? -21.313 30.242 -1.883 1.00 19.98 ? 389 GLN B N 1 ATOM 2768 C CA . GLN B 2 91 ? -20.083 29.676 -2.437 1.00 19.63 ? 389 GLN B CA 1 ATOM 2769 C C . GLN B 2 91 ? -19.977 29.869 -3.945 1.00 24.08 ? 389 GLN B C 1 ATOM 2770 O O . GLN B 2 91 ? -20.995 30.038 -4.622 1.00 23.98 ? 389 GLN B O 1 ATOM 2771 C CB . GLN B 2 91 ? -19.924 28.194 -2.042 1.00 20.54 ? 389 GLN B CB 1 ATOM 2772 C CG . GLN B 2 91 ? -19.756 27.962 -0.537 1.00 26.35 ? 389 GLN B CG 1 ATOM 2773 C CD . GLN B 2 91 ? -18.525 28.625 0.034 1.00 36.78 ? 389 GLN B CD 1 ATOM 2774 O OE1 . GLN B 2 91 ? -17.393 28.184 -0.179 1.00 29.16 ? 389 GLN B OE1 1 ATOM 2775 N NE2 . GLN B 2 91 ? -18.722 29.710 0.764 1.00 26.42 ? 389 GLN B NE2 1 ATOM 2776 N N . LYS B 2 92 ? -18.735 29.844 -4.468 1.00 20.55 ? 390 LYS B N 1 ATOM 2777 C CA . LYS B 2 92 ? -18.430 30.000 -5.893 1.00 20.36 ? 390 LYS B CA 1 ATOM 2778 C C . LYS B 2 92 ? -18.821 28.739 -6.679 1.00 25.47 ? 390 LYS B C 1 ATOM 2779 O O . LYS B 2 92 ? -19.223 27.740 -6.075 1.00 24.96 ? 390 LYS B O 1 ATOM 2780 C CB . LYS B 2 92 ? -16.934 30.312 -6.093 1.00 22.33 ? 390 LYS B CB 1 ATOM 2781 C CG . LYS B 2 92 ? -16.494 31.673 -5.569 1.00 30.14 ? 390 LYS B CG 1 ATOM 2782 C CD . LYS B 2 92 ? -14.986 31.829 -5.660 1.00 36.71 ? 390 LYS B CD 1 ATOM 2783 C CE . LYS B 2 92 ? -14.509 33.143 -5.098 1.00 42.86 ? 390 LYS B CE 1 ATOM 2784 N NZ . LYS B 2 92 ? -13.028 33.250 -5.141 1.00 48.40 ? 390 LYS B NZ 1 ATOM 2785 N N . MET B 2 93 ? -18.692 28.793 -8.025 1.00 22.97 ? 391 MET B N 1 ATOM 2786 C CA . MET B 2 93 ? -18.997 27.703 -8.961 1.00 23.40 ? 391 MET B CA 1 ATOM 2787 C C . MET B 2 93 ? -20.426 27.153 -8.802 1.00 26.66 ? 391 MET B C 1 ATOM 2788 O O . MET B 2 93 ? -20.627 25.935 -8.783 1.00 26.03 ? 391 MET B O 1 ATOM 2789 C CB . MET B 2 93 ? -17.931 26.590 -8.899 1.00 26.16 ? 391 MET B CB 1 ATOM 2790 C CG . MET B 2 93 ? -16.620 26.971 -9.533 1.00 30.52 ? 391 MET B CG 1 ATOM 2791 S SD . MET B 2 93 ? -15.359 25.715 -9.234 1.00 35.37 ? 391 MET B SD 1 ATOM 2792 C CE . MET B 2 93 ? -13.979 26.454 -10.074 1.00 32.20 ? 391 MET B CE 1 ATOM 2793 N N . GLU B 2 94 ? -21.413 28.064 -8.673 1.00 23.04 ? 392 GLU B N 1 ATOM 2794 C CA . GLU B 2 94 ? -22.825 27.709 -8.528 1.00 22.82 ? 392 GLU B CA 1 ATOM 2795 C C . GLU B 2 94 ? -23.320 27.055 -9.816 1.00 26.79 ? 392 GLU B C 1 ATOM 2796 O O . GLU B 2 94 ? -23.149 27.611 -10.904 1.00 26.57 ? 392 GLU B O 1 ATOM 2797 C CB . GLU B 2 94 ? -23.678 28.938 -8.156 1.00 24.12 ? 392 GLU B CB 1 ATOM 2798 C CG . GLU B 2 94 ? -25.174 28.662 -8.054 1.00 33.65 ? 392 GLU B CG 1 ATOM 2799 C CD . GLU B 2 94 ? -26.058 29.797 -7.572 1.00 45.74 ? 392 GLU B CD 1 ATOM 2800 O OE1 . GLU B 2 94 ? -25.529 30.885 -7.249 1.00 37.80 ? 392 GLU B OE1 1 ATOM 2801 O OE2 . GLU B 2 94 ? -27.292 29.594 -7.513 1.00 34.23 ? 392 GLU B OE2 1 ATOM 2802 N N . VAL B 2 95 ? -23.899 25.857 -9.677 1.00 22.98 ? 393 VAL B N 1 ATOM 2803 C CA . VAL B 2 95 ? -24.438 25.059 -10.778 1.00 22.75 ? 393 VAL B CA 1 ATOM 2804 C C . VAL B 2 95 ? -25.965 25.190 -10.752 1.00 26.36 ? 393 VAL B C 1 ATOM 2805 O O . VAL B 2 95 ? -26.549 25.413 -9.686 1.00 25.47 ? 393 VAL B O 1 ATOM 2806 C CB . VAL B 2 95 ? -23.990 23.566 -10.676 1.00 26.80 ? 393 VAL B CB 1 ATOM 2807 C CG1 . VAL B 2 95 ? -24.310 22.793 -11.954 1.00 26.69 ? 393 VAL B CG1 1 ATOM 2808 C CG2 . VAL B 2 95 ? -22.505 23.444 -10.346 1.00 26.69 ? 393 VAL B CG2 1 ATOM 2809 N N . GLN B 2 96 ? -26.601 25.054 -11.930 1.00 23.05 ? 394 GLN B N 1 ATOM 2810 C CA . GLN B 2 96 ? -28.052 25.076 -12.103 1.00 22.91 ? 394 GLN B CA 1 ATOM 2811 C C . GLN B 2 96 ? -28.633 23.863 -11.364 1.00 25.55 ? 394 GLN B C 1 ATOM 2812 O O . GLN B 2 96 ? -28.053 22.775 -11.432 1.00 24.51 ? 394 GLN B O 1 ATOM 2813 C CB . GLN B 2 96 ? -28.388 24.988 -13.603 1.00 24.60 ? 394 GLN B CB 1 ATOM 2814 C CG . GLN B 2 96 ? -29.835 25.311 -13.956 1.00 44.01 ? 394 GLN B CG 1 ATOM 2815 C CD . GLN B 2 96 ? -30.122 25.026 -15.410 1.00 67.75 ? 394 GLN B CD 1 ATOM 2816 O OE1 . GLN B 2 96 ? -30.667 23.976 -15.767 1.00 64.79 ? 394 GLN B OE1 1 ATOM 2817 N NE2 . GLN B 2 96 ? -29.755 25.953 -16.286 1.00 60.16 ? 394 GLN B NE2 1 ATOM 2818 N N . ARG B 2 97 ? -29.747 24.062 -10.632 1.00 21.77 ? 395 ARG B N 1 ATOM 2819 C CA . ARG B 2 97 ? -30.419 22.991 -9.890 1.00 21.06 ? 395 ARG B CA 1 ATOM 2820 C C . ARG B 2 97 ? -30.918 21.953 -10.893 1.00 24.77 ? 395 ARG B C 1 ATOM 2821 O O . ARG B 2 97 ? -31.537 22.311 -11.900 1.00 24.88 ? 395 ARG B O 1 ATOM 2822 C CB . ARG B 2 97 ? -31.570 23.552 -9.046 1.00 19.77 ? 395 ARG B CB 1 ATOM 2823 C CG . ARG B 2 97 ? -31.935 22.689 -7.848 1.00 22.28 ? 395 ARG B CG 1 ATOM 2824 C CD . ARG B 2 97 ? -33.047 23.359 -7.078 1.00 23.28 ? 395 ARG B CD 1 ATOM 2825 N NE . ARG B 2 97 ? -33.436 22.638 -5.867 1.00 25.39 ? 395 ARG B NE 1 ATOM 2826 C CZ . ARG B 2 97 ? -34.454 21.786 -5.795 1.00 34.31 ? 395 ARG B CZ 1 ATOM 2827 N NH1 . ARG B 2 97 ? -35.185 21.522 -6.871 1.00 17.11 ? 395 ARG B NH1 1 ATOM 2828 N NH2 . ARG B 2 97 ? -34.744 21.186 -4.648 1.00 22.87 ? 395 ARG B NH2 1 ATOM 2829 N N . ARG B 2 98 ? -30.577 20.682 -10.654 1.00 20.36 ? 396 ARG B N 1 ATOM 2830 C CA . ARG B 2 98 ? -30.891 19.585 -11.562 1.00 19.93 ? 396 ARG B CA 1 ATOM 2831 C C . ARG B 2 98 ? -31.426 18.350 -10.836 1.00 23.30 ? 396 ARG B C 1 ATOM 2832 O O . ARG B 2 98 ? -31.055 18.124 -9.682 1.00 22.55 ? 396 ARG B O 1 ATOM 2833 C CB . ARG B 2 98 ? -29.612 19.179 -12.318 1.00 20.43 ? 396 ARG B CB 1 ATOM 2834 C CG . ARG B 2 98 ? -29.239 20.082 -13.484 1.00 30.24 ? 396 ARG B CG 1 ATOM 2835 C CD . ARG B 2 98 ? -27.922 19.646 -14.095 1.00 40.53 ? 396 ARG B CD 1 ATOM 2836 N NE . ARG B 2 98 ? -27.786 20.099 -15.480 1.00 50.29 ? 396 ARG B NE 1 ATOM 2837 C CZ . ARG B 2 98 ? -27.171 21.217 -15.852 1.00 65.13 ? 396 ARG B CZ 1 ATOM 2838 N NH1 . ARG B 2 98 ? -26.622 22.016 -14.944 1.00 54.32 ? 396 ARG B NH1 1 ATOM 2839 N NH2 . ARG B 2 98 ? -27.100 21.546 -17.134 1.00 50.55 ? 396 ARG B NH2 1 ATOM 2840 N N . PRO B 2 99 ? -32.238 17.491 -11.495 1.00 19.59 ? 397 PRO B N 1 ATOM 2841 C CA . PRO B 2 99 ? -32.640 16.246 -10.827 1.00 19.30 ? 397 PRO B CA 1 ATOM 2842 C C . PRO B 2 99 ? -31.498 15.224 -10.856 1.00 22.50 ? 397 PRO B C 1 ATOM 2843 O O . PRO B 2 99 ? -30.634 15.282 -11.737 1.00 21.45 ? 397 PRO B O 1 ATOM 2844 C CB . PRO B 2 99 ? -33.843 15.776 -11.647 1.00 21.11 ? 397 PRO B CB 1 ATOM 2845 C CG . PRO B 2 99 ? -33.613 16.322 -13.010 1.00 25.54 ? 397 PRO B CG 1 ATOM 2846 C CD . PRO B 2 99 ? -32.766 17.561 -12.877 1.00 21.13 ? 397 PRO B CD 1 ATOM 2847 N N . TRP B 2 100 ? -31.467 14.316 -9.877 1.00 18.91 ? 398 TRP B N 1 ATOM 2848 C CA . TRP B 2 100 ? -30.473 13.248 -9.856 1.00 18.54 ? 398 TRP B CA 1 ATOM 2849 C C . TRP B 2 100 ? -31.180 11.907 -10.005 1.00 23.67 ? 398 TRP B C 1 ATOM 2850 O O . TRP B 2 100 ? -32.263 11.718 -9.445 1.00 22.68 ? 398 TRP B O 1 ATOM 2851 C CB . TRP B 2 100 ? -29.505 13.337 -8.662 1.00 16.89 ? 398 TRP B CB 1 ATOM 2852 C CG . TRP B 2 100 ? -30.105 13.126 -7.306 1.00 17.38 ? 398 TRP B CG 1 ATOM 2853 C CD1 . TRP B 2 100 ? -30.736 14.057 -6.540 1.00 20.14 ? 398 TRP B CD1 1 ATOM 2854 C CD2 . TRP B 2 100 ? -29.984 11.951 -6.492 1.00 17.10 ? 398 TRP B CD2 1 ATOM 2855 N NE1 . TRP B 2 100 ? -31.092 13.512 -5.329 1.00 19.51 ? 398 TRP B NE1 1 ATOM 2856 C CE2 . TRP B 2 100 ? -30.643 12.218 -5.272 1.00 20.78 ? 398 TRP B CE2 1 ATOM 2857 C CE3 . TRP B 2 100 ? -29.412 10.682 -6.689 1.00 18.18 ? 398 TRP B CE3 1 ATOM 2858 C CZ2 . TRP B 2 100 ? -30.735 11.270 -4.246 1.00 19.99 ? 398 TRP B CZ2 1 ATOM 2859 C CZ3 . TRP B 2 100 ? -29.501 9.744 -5.670 1.00 19.58 ? 398 TRP B CZ3 1 ATOM 2860 C CH2 . TRP B 2 100 ? -30.163 10.038 -4.469 1.00 20.17 ? 398 TRP B CH2 1 ATOM 2861 N N . LEU B 2 101 ? -30.616 11.014 -10.836 1.00 21.72 ? 399 LEU B N 1 ATOM 2862 C CA . LEU B 2 101 ? -31.234 9.733 -11.175 1.00 22.31 ? 399 LEU B CA 1 ATOM 2863 C C . LEU B 2 101 ? -30.670 8.499 -10.482 1.00 27.10 ? 399 LEU B C 1 ATOM 2864 O O . LEU B 2 101 ? -29.489 8.453 -10.130 1.00 26.33 ? 399 LEU B O 1 ATOM 2865 C CB . LEU B 2 101 ? -31.230 9.524 -12.705 1.00 22.68 ? 399 LEU B CB 1 ATOM 2866 C CG . LEU B 2 101 ? -31.944 10.573 -13.566 1.00 27.94 ? 399 LEU B CG 1 ATOM 2867 C CD1 . LEU B 2 101 ? -31.427 10.539 -14.991 1.00 28.40 ? 399 LEU B CD1 1 ATOM 2868 C CD2 . LEU B 2 101 ? -33.453 10.377 -13.555 1.00 30.72 ? 399 LEU B CD2 1 ATOM 2869 N N . VAL B 2 102 ? -31.542 7.487 -10.313 1.00 24.40 ? 400 VAL B N 1 ATOM 2870 C CA . VAL B 2 102 ? -31.259 6.168 -9.746 1.00 24.67 ? 400 VAL B CA 1 ATOM 2871 C C . VAL B 2 102 ? -31.980 5.131 -10.625 1.00 30.14 ? 400 VAL B C 1 ATOM 2872 O O . VAL B 2 102 ? -33.170 5.294 -10.915 1.00 29.27 ? 400 VAL B O 1 ATOM 2873 C CB . VAL B 2 102 ? -31.665 6.060 -8.243 1.00 28.39 ? 400 VAL B CB 1 ATOM 2874 C CG1 . VAL B 2 102 ? -31.762 4.607 -7.782 1.00 28.16 ? 400 VAL B CG1 1 ATOM 2875 C CG2 . VAL B 2 102 ? -30.689 6.819 -7.355 1.00 28.15 ? 400 VAL B CG2 1 ATOM 2876 N N . LYS B 2 103 ? -31.259 4.080 -11.053 1.00 28.12 ? 401 LYS B N 1 ATOM 2877 C CA . LYS B 2 103 ? -31.835 3.013 -11.863 1.00 28.69 ? 401 LYS B CA 1 ATOM 2878 C C . LYS B 2 103 ? -32.464 1.958 -10.945 1.00 33.96 ? 401 LYS B C 1 ATOM 2879 O O . LYS B 2 103 ? -31.765 1.358 -10.123 1.00 33.42 ? 401 LYS B O 1 ATOM 2880 C CB . LYS B 2 103 ? -30.774 2.388 -12.789 1.00 31.40 ? 401 LYS B CB 1 ATOM 2881 C CG . LYS B 2 103 ? -31.364 1.466 -13.854 1.00 45.60 ? 401 LYS B CG 1 ATOM 2882 C CD . LYS B 2 103 ? -30.295 0.663 -14.573 1.00 55.33 ? 401 LYS B CD 1 ATOM 2883 C CE . LYS B 2 103 ? -30.909 -0.302 -15.558 1.00 66.55 ? 401 LYS B CE 1 ATOM 2884 N NZ . LYS B 2 103 ? -29.885 -1.180 -16.181 1.00 76.16 ? 401 LYS B NZ 1 ATOM 2885 N N . TYR B 2 104 ? -33.783 1.750 -11.077 1.00 31.99 ? 402 TYR B N 1 ATOM 2886 C CA . TYR B 2 104 ? -34.532 0.766 -10.294 1.00 32.62 ? 402 TYR B CA 1 ATOM 2887 C C . TYR B 2 104 ? -34.824 -0.464 -11.157 1.00 38.44 ? 402 TYR B C 1 ATOM 2888 O O . TYR B 2 104 ? -35.645 -0.382 -12.070 1.00 38.13 ? 402 TYR B O 1 ATOM 2889 C CB . TYR B 2 104 ? -35.842 1.377 -9.755 1.00 33.81 ? 402 TYR B CB 1 ATOM 2890 C CG . TYR B 2 104 ? -35.652 2.334 -8.599 1.00 35.64 ? 402 TYR B CG 1 ATOM 2891 C CD1 . TYR B 2 104 ? -35.614 1.873 -7.286 1.00 37.59 ? 402 TYR B CD1 1 ATOM 2892 C CD2 . TYR B 2 104 ? -35.560 3.706 -8.812 1.00 36.46 ? 402 TYR B CD2 1 ATOM 2893 C CE1 . TYR B 2 104 ? -35.447 2.751 -6.215 1.00 38.19 ? 402 TYR B CE1 1 ATOM 2894 C CE2 . TYR B 2 104 ? -35.400 4.595 -7.749 1.00 37.31 ? 402 TYR B CE2 1 ATOM 2895 C CZ . TYR B 2 104 ? -35.342 4.111 -6.452 1.00 44.37 ? 402 TYR B CZ 1 ATOM 2896 O OH . TYR B 2 104 ? -35.188 4.979 -5.397 1.00 44.81 ? 402 TYR B OH 1 ATOM 2897 N N . GLY B 2 105 ? -34.122 -1.565 -10.875 1.00 36.59 ? 403 GLY B N 1 ATOM 2898 C CA . GLY B 2 105 ? -34.228 -2.857 -11.559 1.00 37.19 ? 403 GLY B CA 1 ATOM 2899 C C . GLY B 2 105 ? -34.686 -2.809 -13.004 1.00 42.62 ? 403 GLY B C 1 ATOM 2900 O O . GLY B 2 105 ? -33.957 -2.325 -13.877 1.00 42.43 ? 403 GLY B O 1 ATOM 2901 N N . ASP B 2 106 ? -35.922 -3.280 -13.250 1.00 39.85 ? 404 ASP B N 1 ATOM 2902 C CA . ASP B 2 106 ? -36.563 -3.280 -14.569 1.00 39.82 ? 404 ASP B CA 1 ATOM 2903 C C . ASP B 2 106 ? -37.518 -2.080 -14.718 1.00 42.86 ? 404 ASP B C 1 ATOM 2904 O O . ASP B 2 106 ? -38.008 -1.816 -15.818 1.00 42.95 ? 404 ASP B O 1 ATOM 2905 C CB . ASP B 2 106 ? -37.299 -4.610 -14.824 1.00 42.00 ? 404 ASP B CB 1 ATOM 2906 C CG . ASP B 2 106 ? -36.412 -5.844 -14.785 1.00 54.40 ? 404 ASP B CG 1 ATOM 2907 O OD1 . ASP B 2 106 ? -35.393 -5.869 -15.513 1.00 55.28 ? 404 ASP B OD1 1 ATOM 2908 O OD2 . ASP B 2 106 ? -36.756 -6.797 -14.054 1.00 60.77 ? 404 ASP B OD2 1 ATOM 2909 N N . SER B 2 107 ? -37.750 -1.337 -13.610 1.00 37.87 ? 405 SER B N 1 ATOM 2910 C CA . SER B 2 107 ? -38.604 -0.144 -13.551 1.00 36.70 ? 405 SER B CA 1 ATOM 2911 C C . SER B 2 107 ? -37.924 1.094 -14.179 1.00 37.44 ? 405 SER B C 1 ATOM 2912 O O . SER B 2 107 ? -38.541 2.158 -14.274 1.00 36.62 ? 405 SER B O 1 ATOM 2913 C CB . SER B 2 107 ? -39.019 0.138 -12.110 1.00 40.45 ? 405 SER B CB 1 ATOM 2914 O OG . SER B 2 107 ? -39.749 -0.952 -11.571 1.00 50.31 ? 405 SER B OG 1 ATOM 2915 N N . GLY B 2 108 ? -36.673 0.924 -14.608 1.00 31.88 ? 406 GLY B N 1 ATOM 2916 C CA . GLY B 2 108 ? -35.871 1.945 -15.272 1.00 30.70 ? 406 GLY B CA 1 ATOM 2917 C C . GLY B 2 108 ? -35.370 3.066 -14.387 1.00 31.94 ? 406 GLY B C 1 ATOM 2918 O O . GLY B 2 108 ? -35.482 3.004 -13.158 1.00 31.43 ? 406 GLY B O 1 ATOM 2919 N N . GLU B 2 109 ? -34.801 4.098 -15.028 1.00 26.73 ? 407 GLU B N 1 ATOM 2920 C CA . GLU B 2 109 ? -34.263 5.294 -14.380 1.00 25.60 ? 407 GLU B CA 1 ATOM 2921 C C . GLU B 2 109 ? -35.401 6.135 -13.804 1.00 26.90 ? 407 GLU B C 1 ATOM 2922 O O . GLU B 2 109 ? -36.423 6.335 -14.468 1.00 26.29 ? 407 GLU B O 1 ATOM 2923 C CB . GLU B 2 109 ? -33.439 6.130 -15.377 1.00 27.01 ? 407 GLU B CB 1 ATOM 2924 C CG . GLU B 2 109 ? -32.120 5.495 -15.800 1.00 37.60 ? 407 GLU B CG 1 ATOM 2925 C CD . GLU B 2 109 ? -30.953 5.575 -14.829 1.00 56.97 ? 407 GLU B CD 1 ATOM 2926 O OE1 . GLU B 2 109 ? -31.047 6.306 -13.816 1.00 48.38 ? 407 GLU B OE1 1 ATOM 2927 O OE2 . GLU B 2 109 ? -29.927 4.909 -15.097 1.00 54.28 ? 407 GLU B OE2 1 ATOM 2928 N N . GLN B 2 110 ? -35.234 6.596 -12.557 1.00 21.41 ? 408 GLN B N 1 ATOM 2929 C CA . GLN B 2 110 ? -36.225 7.416 -11.859 1.00 20.12 ? 408 GLN B CA 1 ATOM 2930 C C . GLN B 2 110 ? -35.554 8.596 -11.179 1.00 22.56 ? 408 GLN B C 1 ATOM 2931 O O . GLN B 2 110 ? -34.393 8.489 -10.780 1.00 21.75 ? 408 GLN B O 1 ATOM 2932 C CB . GLN B 2 110 ? -37.002 6.586 -10.810 1.00 21.10 ? 408 GLN B CB 1 ATOM 2933 C CG . GLN B 2 110 ? -37.854 5.431 -11.365 1.00 28.02 ? 408 GLN B CG 1 ATOM 2934 C CD . GLN B 2 110 ? -39.004 5.858 -12.255 1.00 37.14 ? 408 GLN B CD 1 ATOM 2935 O OE1 . GLN B 2 110 ? -39.580 6.942 -12.112 1.00 31.12 ? 408 GLN B OE1 1 ATOM 2936 N NE2 . GLN B 2 110 ? -39.396 4.983 -13.167 1.00 23.73 ? 408 GLN B NE2 1 ATOM 2937 N N . ILE B 2 111 ? -36.286 9.718 -11.032 1.00 18.95 ? 409 ILE B N 1 ATOM 2938 C CA . ILE B 2 111 ? -35.783 10.901 -10.332 1.00 18.63 ? 409 ILE B CA 1 ATOM 2939 C C . ILE B 2 111 ? -35.777 10.566 -8.839 1.00 21.89 ? 409 ILE B C 1 ATOM 2940 O O . ILE B 2 111 ? -36.831 10.303 -8.260 1.00 21.53 ? 409 ILE B O 1 ATOM 2941 C CB . ILE B 2 111 ? -36.588 12.196 -10.665 1.00 21.80 ? 409 ILE B CB 1 ATOM 2942 C CG1 . ILE B 2 111 ? -36.399 12.596 -12.148 1.00 22.44 ? 409 ILE B CG1 1 ATOM 2943 C CG2 . ILE B 2 111 ? -36.192 13.354 -9.721 1.00 22.29 ? 409 ILE B CG2 1 ATOM 2944 C CD1 . ILE B 2 111 ? -37.367 13.646 -12.664 1.00 30.21 ? 409 ILE B CD1 1 ATOM 2945 N N . ALA B 2 112 ? -34.582 10.515 -8.240 1.00 18.53 ? 410 ALA B N 1 ATOM 2946 C CA . ALA B 2 112 ? -34.418 10.191 -6.822 1.00 17.96 ? 410 ALA B CA 1 ATOM 2947 C C . ALA B 2 112 ? -34.533 11.438 -5.952 1.00 20.84 ? 410 ALA B C 1 ATOM 2948 O O . ALA B 2 112 ? -34.740 11.337 -4.742 1.00 20.26 ? 410 ALA B O 1 ATOM 2949 C CB . ALA B 2 112 ? -33.081 9.513 -6.599 1.00 18.68 ? 410 ALA B CB 1 ATOM 2950 N N . GLY B 2 113 ? -34.414 12.597 -6.589 1.00 17.06 ? 411 GLY B N 1 ATOM 2951 C CA . GLY B 2 113 ? -34.494 13.907 -5.957 1.00 16.53 ? 411 GLY B CA 1 ATOM 2952 C C . GLY B 2 113 ? -33.819 14.967 -6.799 1.00 19.23 ? 411 GLY B C 1 ATOM 2953 O O . GLY B 2 113 ? -33.604 14.760 -7.995 1.00 18.02 ? 411 GLY B O 1 ATOM 2954 N N . PHE B 2 114 ? -33.439 16.090 -6.170 1.00 15.92 ? 412 PHE B N 1 ATOM 2955 C CA . PHE B 2 114 ? -32.791 17.214 -6.848 1.00 15.59 ? 412 PHE B CA 1 ATOM 2956 C C . PHE B 2 114 ? -31.475 17.610 -6.190 1.00 19.78 ? 412 PHE B C 1 ATOM 2957 O O . PHE B 2 114 ? -31.353 17.537 -4.968 1.00 19.16 ? 412 PHE B O 1 ATOM 2958 C CB . PHE B 2 114 ? -33.748 18.415 -6.941 1.00 17.29 ? 412 PHE B CB 1 ATOM 2959 C CG . PHE B 2 114 ? -34.955 18.174 -7.822 1.00 18.62 ? 412 PHE B CG 1 ATOM 2960 C CD1 . PHE B 2 114 ? -36.100 17.569 -7.313 1.00 21.52 ? 412 PHE B CD1 1 ATOM 2961 C CD2 . PHE B 2 114 ? -34.949 18.557 -9.157 1.00 20.57 ? 412 PHE B CD2 1 ATOM 2962 C CE1 . PHE B 2 114 ? -37.208 17.331 -8.132 1.00 22.39 ? 412 PHE B CE1 1 ATOM 2963 C CE2 . PHE B 2 114 ? -36.058 18.321 -9.975 1.00 23.34 ? 412 PHE B CE2 1 ATOM 2964 C CZ . PHE B 2 114 ? -37.182 17.714 -9.455 1.00 21.56 ? 412 PHE B CZ 1 ATOM 2965 N N . VAL B 2 115 ? -30.490 18.023 -7.011 1.00 16.79 ? 413 VAL B N 1 ATOM 2966 C CA . VAL B 2 115 ? -29.150 18.427 -6.573 1.00 16.44 ? 413 VAL B CA 1 ATOM 2967 C C . VAL B 2 115 ? -28.847 19.900 -6.872 1.00 19.58 ? 413 VAL B C 1 ATOM 2968 O O . VAL B 2 115 ? -29.006 20.348 -8.009 1.00 18.90 ? 413 VAL B O 1 ATOM 2969 C CB . VAL B 2 115 ? -28.025 17.452 -7.068 1.00 20.41 ? 413 VAL B CB 1 ATOM 2970 C CG1 . VAL B 2 115 ? -28.156 17.124 -8.554 1.00 20.24 ? 413 VAL B CG1 1 ATOM 2971 C CG2 . VAL B 2 115 ? -26.623 17.977 -6.754 1.00 20.21 ? 413 VAL B CG2 1 ATOM 2972 N N . LYS B 2 116 ? -28.410 20.640 -5.837 1.00 15.86 ? 414 LYS B N 1 ATOM 2973 C CA . LYS B 2 116 ? -27.982 22.034 -5.938 1.00 15.37 ? 414 LYS B CA 1 ATOM 2974 C C . LYS B 2 116 ? -26.507 22.064 -5.543 1.00 20.62 ? 414 LYS B C 1 ATOM 2975 O O . LYS B 2 116 ? -26.171 21.908 -4.367 1.00 20.23 ? 414 LYS B O 1 ATOM 2976 C CB . LYS B 2 116 ? -28.851 22.973 -5.074 1.00 16.68 ? 414 LYS B CB 1 ATOM 2977 C CG . LYS B 2 116 ? -28.458 24.457 -5.152 1.00 19.57 ? 414 LYS B CG 1 ATOM 2978 C CD . LYS B 2 116 ? -28.659 25.066 -6.544 1.00 22.05 ? 414 LYS B CD 1 ATOM 2979 C CE . LYS B 2 116 ? -28.125 26.470 -6.624 1.00 25.10 ? 414 LYS B CE 1 ATOM 2980 N NZ . LYS B 2 116 ? -28.373 27.075 -7.960 1.00 28.03 ? 414 LYS B NZ 1 ATOM 2981 N N . GLU B 2 117 ? -25.631 22.203 -6.546 1.00 18.78 ? 415 GLU B N 1 ATOM 2982 C CA . GLU B 2 117 ? -24.182 22.153 -6.379 1.00 19.10 ? 415 GLU B CA 1 ATOM 2983 C C . GLU B 2 117 ? -23.484 23.510 -6.444 1.00 23.07 ? 415 GLU B C 1 ATOM 2984 O O . GLU B 2 117 ? -23.865 24.382 -7.223 1.00 22.48 ? 415 GLU B O 1 ATOM 2985 C CB . GLU B 2 117 ? -23.583 21.201 -7.427 1.00 20.68 ? 415 GLU B CB 1 ATOM 2986 C CG . GLU B 2 117 ? -22.231 20.600 -7.070 1.00 33.12 ? 415 GLU B CG 1 ATOM 2987 C CD . GLU B 2 117 ? -21.582 19.727 -8.131 1.00 56.31 ? 415 GLU B CD 1 ATOM 2988 O OE1 . GLU B 2 117 ? -22.243 19.413 -9.147 1.00 51.73 ? 415 GLU B OE1 1 ATOM 2989 O OE2 . GLU B 2 117 ? -20.403 19.354 -7.940 1.00 53.48 ? 415 GLU B OE2 1 ATOM 2990 N N . PHE B 2 118 ? -22.434 23.648 -5.625 1.00 20.13 ? 416 PHE B N 1 ATOM 2991 C CA . PHE B 2 118 ? -21.519 24.785 -5.529 1.00 20.36 ? 416 PHE B CA 1 ATOM 2992 C C . PHE B 2 118 ? -20.115 24.171 -5.425 1.00 24.92 ? 416 PHE B C 1 ATOM 2993 O O . PHE B 2 118 ? -19.998 22.941 -5.385 1.00 24.70 ? 416 PHE B O 1 ATOM 2994 C CB . PHE B 2 118 ? -21.817 25.624 -4.270 1.00 22.22 ? 416 PHE B CB 1 ATOM 2995 C CG . PHE B 2 118 ? -23.166 26.300 -4.221 1.00 23.84 ? 416 PHE B CG 1 ATOM 2996 C CD1 . PHE B 2 118 ? -24.273 25.643 -3.692 1.00 26.93 ? 416 PHE B CD1 1 ATOM 2997 C CD2 . PHE B 2 118 ? -23.320 27.613 -4.649 1.00 26.06 ? 416 PHE B CD2 1 ATOM 2998 C CE1 . PHE B 2 118 ? -25.518 26.276 -3.628 1.00 27.91 ? 416 PHE B CE1 1 ATOM 2999 C CE2 . PHE B 2 118 ? -24.562 28.250 -4.570 1.00 28.96 ? 416 PHE B CE2 1 ATOM 3000 C CZ . PHE B 2 118 ? -25.654 27.575 -4.067 1.00 27.03 ? 416 PHE B CZ 1 ATOM 3001 N N . SER B 2 119 ? -19.055 25.005 -5.383 1.00 21.63 ? 417 SER B N 1 ATOM 3002 C CA . SER B 2 119 ? -17.683 24.515 -5.230 1.00 21.36 ? 417 SER B CA 1 ATOM 3003 C C . SER B 2 119 ? -17.546 23.849 -3.854 1.00 24.67 ? 417 SER B C 1 ATOM 3004 O O . SER B 2 119 ? -17.915 24.455 -2.845 1.00 23.84 ? 417 SER B O 1 ATOM 3005 C CB . SER B 2 119 ? -16.681 25.660 -5.370 1.00 24.51 ? 417 SER B CB 1 ATOM 3006 O OG . SER B 2 119 ? -15.358 25.250 -5.065 1.00 31.94 ? 417 SER B OG 1 ATOM 3007 N N . HIS B 2 120 ? -17.091 22.574 -3.834 1.00 21.22 ? 418 HIS B N 1 ATOM 3008 C CA . HIS B 2 120 ? -16.859 21.750 -2.633 1.00 21.11 ? 418 HIS B CA 1 ATOM 3009 C C . HIS B 2 120 ? -18.085 21.474 -1.736 1.00 24.12 ? 418 HIS B C 1 ATOM 3010 O O . HIS B 2 120 ? -17.928 20.878 -0.666 1.00 23.82 ? 418 HIS B O 1 ATOM 3011 C CB . HIS B 2 120 ? -15.672 22.295 -1.809 1.00 22.00 ? 418 HIS B CB 1 ATOM 3012 C CG . HIS B 2 120 ? -14.367 22.265 -2.543 1.00 25.57 ? 418 HIS B CG 1 ATOM 3013 N ND1 . HIS B 2 120 ? -14.121 23.109 -3.612 1.00 27.33 ? 418 HIS B ND1 1 ATOM 3014 C CD2 . HIS B 2 120 ? -13.275 21.496 -2.332 1.00 27.37 ? 418 HIS B CD2 1 ATOM 3015 C CE1 . HIS B 2 120 ? -12.899 22.817 -4.023 1.00 26.78 ? 418 HIS B CE1 1 ATOM 3016 N NE2 . HIS B 2 120 ? -12.350 21.854 -3.283 1.00 27.16 ? 418 HIS B NE2 1 ATOM 3017 N N . ILE B 2 121 ? -19.294 21.890 -2.166 1.00 19.86 ? 419 ILE B N 1 ATOM 3018 C CA . ILE B 2 121 ? -20.531 21.692 -1.407 1.00 19.29 ? 419 ILE B CA 1 ATOM 3019 C C . ILE B 2 121 ? -21.761 21.464 -2.299 1.00 22.31 ? 419 ILE B C 1 ATOM 3020 O O . ILE B 2 121 ? -21.962 22.178 -3.282 1.00 21.82 ? 419 ILE B O 1 ATOM 3021 C CB . ILE B 2 121 ? -20.741 22.769 -0.294 1.00 22.29 ? 419 ILE B CB 1 ATOM 3022 C CG1 . ILE B 2 121 ? -21.873 22.371 0.690 1.00 22.68 ? 419 ILE B CG1 1 ATOM 3023 C CG2 . ILE B 2 121 ? -20.918 24.190 -0.872 1.00 22.69 ? 419 ILE B CG2 1 ATOM 3024 C CD1 . ILE B 2 121 ? -21.839 23.049 2.051 1.00 28.35 ? 419 ILE B CD1 1 ATOM 3025 N N . ALA B 2 122 ? -22.576 20.461 -1.945 1.00 18.26 ? 420 ALA B N 1 ATOM 3026 C CA . ALA B 2 122 ? -23.799 20.143 -2.672 1.00 17.86 ? 420 ALA B CA 1 ATOM 3027 C C . ALA B 2 122 ? -24.953 19.874 -1.717 1.00 21.49 ? 420 ALA B C 1 ATOM 3028 O O . ALA B 2 122 ? -24.758 19.253 -0.669 1.00 21.36 ? 420 ALA B O 1 ATOM 3029 C CB . ALA B 2 122 ? -23.578 18.936 -3.568 1.00 18.47 ? 420 ALA B CB 1 ATOM 3030 N N . PHE B 2 123 ? -26.151 20.354 -2.078 1.00 17.47 ? 421 PHE B N 1 ATOM 3031 C CA . PHE B 2 123 ? -27.371 20.091 -1.326 1.00 17.22 ? 421 PHE B CA 1 ATOM 3032 C C . PHE B 2 123 ? -28.221 19.117 -2.145 1.00 21.20 ? 421 PHE B C 1 ATOM 3033 O O . PHE B 2 123 ? -28.422 19.339 -3.340 1.00 20.33 ? 421 PHE B O 1 ATOM 3034 C CB . PHE B 2 123 ? -28.166 21.371 -0.989 1.00 18.74 ? 421 PHE B CB 1 ATOM 3035 C CG . PHE B 2 123 ? -29.542 21.040 -0.455 1.00 20.05 ? 421 PHE B CG 1 ATOM 3036 C CD1 . PHE B 2 123 ? -29.715 20.630 0.863 1.00 22.99 ? 421 PHE B CD1 1 ATOM 3037 C CD2 . PHE B 2 123 ? -30.651 21.047 -1.294 1.00 21.96 ? 421 PHE B CD2 1 ATOM 3038 C CE1 . PHE B 2 123 ? -30.975 20.259 1.337 1.00 23.96 ? 421 PHE B CE1 1 ATOM 3039 C CE2 . PHE B 2 123 ? -31.905 20.660 -0.823 1.00 24.82 ? 421 PHE B CE2 1 ATOM 3040 C CZ . PHE B 2 123 ? -32.061 20.276 0.490 1.00 22.92 ? 421 PHE B CZ 1 ATOM 3041 N N . LEU B 2 124 ? -28.734 18.058 -1.497 1.00 18.28 ? 422 LEU B N 1 ATOM 3042 C CA . LEU B 2 124 ? -29.551 17.049 -2.168 1.00 18.33 ? 422 LEU B CA 1 ATOM 3043 C C . LEU B 2 124 ? -30.857 16.757 -1.462 1.00 21.15 ? 422 LEU B C 1 ATOM 3044 O O . LEU B 2 124 ? -30.897 16.680 -0.234 1.00 20.57 ? 422 LEU B O 1 ATOM 3045 C CB . LEU B 2 124 ? -28.769 15.731 -2.301 1.00 18.54 ? 422 LEU B CB 1 ATOM 3046 C CG . LEU B 2 124 ? -28.067 15.468 -3.621 1.00 23.42 ? 422 LEU B CG 1 ATOM 3047 C CD1 . LEU B 2 124 ? -26.734 16.164 -3.667 1.00 24.04 ? 422 LEU B CD1 1 ATOM 3048 C CD2 . LEU B 2 124 ? -27.834 13.989 -3.810 1.00 25.81 ? 422 LEU B CD2 1 ATOM 3049 N N . THR B 2 125 ? -31.919 16.551 -2.252 1.00 17.09 ? 423 THR B N 1 ATOM 3050 C CA . THR B 2 125 ? -33.208 16.114 -1.731 1.00 16.78 ? 423 THR B CA 1 ATOM 3051 C C . THR B 2 125 ? -33.330 14.633 -2.078 1.00 19.84 ? 423 THR B C 1 ATOM 3052 O O . THR B 2 125 ? -32.770 14.187 -3.084 1.00 18.39 ? 423 THR B O 1 ATOM 3053 C CB . THR B 2 125 ? -34.405 16.894 -2.319 1.00 24.56 ? 423 THR B CB 1 ATOM 3054 O OG1 . THR B 2 125 ? -34.497 16.685 -3.728 1.00 23.02 ? 423 THR B OG1 1 ATOM 3055 C CG2 . THR B 2 125 ? -34.388 18.373 -1.979 1.00 24.28 ? 423 THR B CG2 1 ATOM 3056 N N . ILE B 2 126 ? -34.033 13.872 -1.239 1.00 16.73 ? 424 ILE B N 1 ATOM 3057 C CA . ILE B 2 126 ? -34.319 12.468 -1.503 1.00 16.73 ? 424 ILE B CA 1 ATOM 3058 C C . ILE B 2 126 ? -35.837 12.398 -1.513 1.00 20.21 ? 424 ILE B C 1 ATOM 3059 O O . ILE B 2 126 ? -36.475 12.512 -0.465 1.00 19.74 ? 424 ILE B O 1 ATOM 3060 C CB . ILE B 2 126 ? -33.604 11.450 -0.563 1.00 20.03 ? 424 ILE B CB 1 ATOM 3061 C CG1 . ILE B 2 126 ? -32.068 11.566 -0.679 1.00 20.56 ? 424 ILE B CG1 1 ATOM 3062 C CG2 . ILE B 2 126 ? -34.023 10.013 -0.899 1.00 20.85 ? 424 ILE B CG2 1 ATOM 3063 C CD1 . ILE B 2 126 ? -31.422 12.469 0.326 1.00 28.44 ? 424 ILE B CD1 1 ATOM 3064 N N . LYS B 2 127 ? -36.401 12.346 -2.729 1.00 16.26 ? 425 LYS B N 1 ATOM 3065 C CA . LYS B 2 127 ? -37.837 12.352 -2.993 1.00 15.61 ? 425 LYS B CA 1 ATOM 3066 C C . LYS B 2 127 ? -38.580 11.175 -2.372 1.00 19.50 ? 425 LYS B C 1 ATOM 3067 O O . LYS B 2 127 ? -38.272 10.020 -2.663 1.00 19.18 ? 425 LYS B O 1 ATOM 3068 C CB . LYS B 2 127 ? -38.103 12.473 -4.501 1.00 17.44 ? 425 LYS B CB 1 ATOM 3069 C CG . LYS B 2 127 ? -39.548 12.822 -4.852 1.00 21.54 ? 425 LYS B CG 1 ATOM 3070 C CD . LYS B 2 127 ? -39.742 13.111 -6.345 1.00 26.02 ? 425 LYS B CD 1 ATOM 3071 C CE . LYS B 2 127 ? -39.521 11.922 -7.255 1.00 27.48 ? 425 LYS B CE 1 ATOM 3072 N NZ . LYS B 2 127 ? -40.443 10.788 -6.973 1.00 30.14 ? 425 LYS B NZ 1 ATOM 3073 N N . GLY B 2 128 ? -39.539 11.496 -1.504 1.00 16.24 ? 426 GLY B N 1 ATOM 3074 C CA . GLY B 2 128 ? -40.372 10.515 -0.817 1.00 16.18 ? 426 GLY B CA 1 ATOM 3075 C C . GLY B 2 128 ? -39.788 9.926 0.449 1.00 19.92 ? 426 GLY B C 1 ATOM 3076 O O . GLY B 2 128 ? -40.424 9.077 1.077 1.00 19.45 ? 426 GLY B O 1 ATOM 3077 N N . ALA B 2 129 ? -38.578 10.364 0.834 1.00 16.33 ? 427 ALA B N 1 ATOM 3078 C CA . ALA B 2 129 ? -37.915 9.883 2.043 1.00 15.76 ? 427 ALA B CA 1 ATOM 3079 C C . ALA B 2 129 ? -38.163 10.832 3.204 1.00 19.32 ? 427 ALA B C 1 ATOM 3080 O O . ALA B 2 129 ? -38.324 12.033 2.999 1.00 18.94 ? 427 ALA B O 1 ATOM 3081 C CB . ALA B 2 129 ? -36.425 9.741 1.801 1.00 16.31 ? 427 ALA B CB 1 ATOM 3082 N N . GLY B 2 130 ? -38.212 10.283 4.408 1.00 15.63 ? 428 GLY B N 1 ATOM 3083 C CA . GLY B 2 130 ? -38.403 11.062 5.621 1.00 15.07 ? 428 GLY B CA 1 ATOM 3084 C C . GLY B 2 130 ? -37.080 11.394 6.276 1.00 18.32 ? 428 GLY B C 1 ATOM 3085 O O . GLY B 2 130 ? -36.057 11.527 5.598 1.00 17.89 ? 428 GLY B O 1 ATOM 3086 N N . HIS B 2 131 ? -37.098 11.504 7.610 1.00 14.49 ? 429 HIS B N 1 ATOM 3087 C CA . HIS B 2 131 ? -35.956 11.824 8.471 1.00 14.29 ? 429 HIS B CA 1 ATOM 3088 C C . HIS B 2 131 ? -34.827 10.801 8.372 1.00 18.21 ? 429 HIS B C 1 ATOM 3089 O O . HIS B 2 131 ? -33.660 11.165 8.534 1.00 17.60 ? 429 HIS B O 1 ATOM 3090 C CB . HIS B 2 131 ? -36.439 11.930 9.920 1.00 15.10 ? 429 HIS B CB 1 ATOM 3091 C CG . HIS B 2 131 ? -35.534 12.706 10.819 1.00 18.36 ? 429 HIS B CG 1 ATOM 3092 N ND1 . HIS B 2 131 ? -35.317 14.059 10.635 1.00 20.00 ? 429 HIS B ND1 1 ATOM 3093 C CD2 . HIS B 2 131 ? -34.870 12.301 11.923 1.00 19.82 ? 429 HIS B CD2 1 ATOM 3094 C CE1 . HIS B 2 131 ? -34.501 14.424 11.610 1.00 19.33 ? 429 HIS B CE1 1 ATOM 3095 N NE2 . HIS B 2 131 ? -34.212 13.399 12.413 1.00 19.65 ? 429 HIS B NE2 1 ATOM 3096 N N A MET B 2 132 ? -35.169 9.531 8.112 0.60 14.96 ? 430 MET B N 1 ATOM 3097 N N B MET B 2 132 ? -35.181 9.531 8.104 0.40 14.81 ? 430 MET B N 1 ATOM 3098 C CA A MET B 2 132 ? -34.196 8.452 7.987 0.60 14.67 ? 430 MET B CA 1 ATOM 3099 C CA B MET B 2 132 ? -34.246 8.419 7.966 0.40 14.51 ? 430 MET B CA 1 ATOM 3100 C C A MET B 2 132 ? -34.102 7.959 6.547 0.60 17.71 ? 430 MET B C 1 ATOM 3101 C C B MET B 2 132 ? -34.161 7.979 6.508 0.40 17.81 ? 430 MET B C 1 ATOM 3102 O O A MET B 2 132 ? -34.641 6.905 6.202 0.60 17.11 ? 430 MET B O 1 ATOM 3103 O O B MET B 2 132 ? -34.774 6.981 6.114 0.40 17.42 ? 430 MET B O 1 ATOM 3104 C CB A MET B 2 132 ? -34.490 7.332 8.991 0.60 17.11 ? 430 MET B CB 1 ATOM 3105 C CB B MET B 2 132 ? -34.634 7.257 8.896 0.40 16.87 ? 430 MET B CB 1 ATOM 3106 C CG A MET B 2 132 ? -34.230 7.754 10.413 0.60 20.84 ? 430 MET B CG 1 ATOM 3107 C CG B MET B 2 132 ? -34.527 7.612 10.346 0.40 20.51 ? 430 MET B CG 1 ATOM 3108 S SD A MET B 2 132 ? -33.969 6.371 11.535 0.60 25.06 ? 430 MET B SD 1 ATOM 3109 S SD B MET B 2 132 ? -34.706 6.203 11.446 0.40 24.63 ? 430 MET B SD 1 ATOM 3110 C CE A MET B 2 132 ? -35.632 5.907 11.835 0.60 21.74 ? 430 MET B CE 1 ATOM 3111 C CE B MET B 2 132 ? -34.350 6.982 12.945 0.40 21.21 ? 430 MET B CE 1 ATOM 3112 N N . VAL B 2 133 ? -33.408 8.754 5.705 1.00 13.99 ? 431 VAL B N 1 ATOM 3113 C CA . VAL B 2 133 ? -33.170 8.518 4.268 1.00 13.77 ? 431 VAL B CA 1 ATOM 3114 C C . VAL B 2 133 ? -32.780 7.057 3.918 1.00 17.42 ? 431 VAL B C 1 ATOM 3115 O O . VAL B 2 133 ? -33.472 6.473 3.077 1.00 16.92 ? 431 VAL B O 1 ATOM 3116 C CB . VAL B 2 133 ? -32.205 9.587 3.671 1.00 17.47 ? 431 VAL B CB 1 ATOM 3117 C CG1 . VAL B 2 133 ? -31.650 9.174 2.309 1.00 17.23 ? 431 VAL B CG1 1 ATOM 3118 C CG2 . VAL B 2 133 ? -32.883 10.948 3.587 1.00 17.23 ? 431 VAL B CG2 1 ATOM 3119 N N . PRO B 2 134 ? -31.777 6.417 4.587 1.00 14.02 ? 432 PRO B N 1 ATOM 3120 C CA . PRO B 2 134 ? -31.440 5.025 4.237 1.00 14.06 ? 432 PRO B CA 1 ATOM 3121 C C . PRO B 2 134 ? -32.501 3.982 4.582 1.00 18.45 ? 432 PRO B C 1 ATOM 3122 O O . PRO B 2 134 ? -32.501 2.920 3.971 1.00 18.13 ? 432 PRO B O 1 ATOM 3123 C CB . PRO B 2 134 ? -30.116 4.781 4.974 1.00 15.67 ? 432 PRO B CB 1 ATOM 3124 C CG . PRO B 2 134 ? -29.602 6.150 5.312 1.00 19.73 ? 432 PRO B CG 1 ATOM 3125 C CD . PRO B 2 134 ? -30.838 6.920 5.611 1.00 15.37 ? 432 PRO B CD 1 ATOM 3126 N N . THR B 2 135 ? -33.401 4.274 5.543 1.00 15.46 ? 433 THR B N 1 ATOM 3127 C CA . THR B 2 135 ? -34.493 3.363 5.915 1.00 15.59 ? 433 THR B CA 1 ATOM 3128 C C . THR B 2 135 ? -35.605 3.435 4.851 1.00 20.03 ? 433 THR B C 1 ATOM 3129 O O . THR B 2 135 ? -36.096 2.397 4.403 1.00 19.94 ? 433 THR B O 1 ATOM 3130 C CB . THR B 2 135 ? -35.025 3.704 7.328 1.00 22.43 ? 433 THR B CB 1 ATOM 3131 O OG1 . THR B 2 135 ? -33.943 3.694 8.259 1.00 21.68 ? 433 THR B OG1 1 ATOM 3132 C CG2 . THR B 2 135 ? -36.122 2.746 7.803 1.00 20.63 ? 433 THR B CG2 1 ATOM 3133 N N . ASP B 2 136 ? -35.990 4.663 4.454 1.00 16.37 ? 434 ASP B N 1 ATOM 3134 C CA . ASP B 2 136 ? -37.069 4.915 3.497 1.00 15.78 ? 434 ASP B CA 1 ATOM 3135 C C . ASP B 2 136 ? -36.708 4.655 2.041 1.00 18.98 ? 434 ASP B C 1 ATOM 3136 O O . ASP B 2 136 ? -37.514 4.079 1.311 1.00 18.29 ? 434 ASP B O 1 ATOM 3137 C CB . ASP B 2 136 ? -37.638 6.330 3.691 1.00 17.34 ? 434 ASP B CB 1 ATOM 3138 C CG . ASP B 2 136 ? -38.156 6.594 5.095 1.00 24.17 ? 434 ASP B CG 1 ATOM 3139 O OD1 . ASP B 2 136 ? -38.516 5.616 5.792 1.00 24.59 ? 434 ASP B OD1 1 ATOM 3140 O OD2 . ASP B 2 136 ? -38.191 7.771 5.501 1.00 25.77 ? 434 ASP B OD2 1 ATOM 3141 N N . LYS B 2 137 ? -35.515 5.097 1.617 1.00 15.85 ? 435 LYS B N 1 ATOM 3142 C CA . LYS B 2 137 ? -35.018 4.931 0.249 1.00 15.34 ? 435 LYS B CA 1 ATOM 3143 C C . LYS B 2 137 ? -33.592 4.343 0.298 1.00 19.52 ? 435 LYS B C 1 ATOM 3144 O O . LYS B 2 137 ? -32.626 5.081 0.075 1.00 19.16 ? 435 LYS B O 1 ATOM 3145 C CB . LYS B 2 137 ? -35.058 6.278 -0.516 1.00 17.19 ? 435 LYS B CB 1 ATOM 3146 C CG . LYS B 2 137 ? -36.455 6.882 -0.707 1.00 23.07 ? 435 LYS B CG 1 ATOM 3147 C CD . LYS B 2 137 ? -37.194 6.308 -1.909 1.00 26.21 ? 435 LYS B CD 1 ATOM 3148 C CE . LYS B 2 137 ? -38.643 6.708 -1.901 1.00 29.57 ? 435 LYS B CE 1 ATOM 3149 N NZ . LYS B 2 137 ? -39.361 6.194 -3.097 1.00 35.60 ? 435 LYS B NZ 1 ATOM 3150 N N . PRO B 2 138 ? -33.430 3.029 0.614 1.00 16.69 ? 436 PRO B N 1 ATOM 3151 C CA . PRO B 2 138 ? -32.069 2.460 0.718 1.00 16.70 ? 436 PRO B CA 1 ATOM 3152 C C . PRO B 2 138 ? -31.214 2.488 -0.548 1.00 20.71 ? 436 PRO B C 1 ATOM 3153 O O . PRO B 2 138 ? -30.015 2.747 -0.439 1.00 19.79 ? 436 PRO B O 1 ATOM 3154 C CB . PRO B 2 138 ? -32.304 1.036 1.229 1.00 18.31 ? 436 PRO B CB 1 ATOM 3155 C CG . PRO B 2 138 ? -33.708 0.723 0.880 1.00 22.64 ? 436 PRO B CG 1 ATOM 3156 C CD . PRO B 2 138 ? -34.458 2.017 0.939 1.00 18.12 ? 436 PRO B CD 1 ATOM 3157 N N . LEU B 2 139 ? -31.809 2.227 -1.734 1.00 17.54 ? 437 LEU B N 1 ATOM 3158 C CA . LEU B 2 139 ? -31.068 2.245 -3.003 1.00 17.58 ? 437 LEU B CA 1 ATOM 3159 C C . LEU B 2 139 ? -30.618 3.661 -3.369 1.00 21.44 ? 437 LEU B C 1 ATOM 3160 O O . LEU B 2 139 ? -29.462 3.841 -3.759 1.00 21.31 ? 437 LEU B O 1 ATOM 3161 C CB . LEU B 2 139 ? -31.851 1.571 -4.154 1.00 17.71 ? 437 LEU B CB 1 ATOM 3162 C CG . LEU B 2 139 ? -31.214 1.593 -5.567 1.00 22.53 ? 437 LEU B CG 1 ATOM 3163 C CD1 . LEU B 2 139 ? -29.830 0.933 -5.597 1.00 22.76 ? 437 LEU B CD1 1 ATOM 3164 C CD2 . LEU B 2 139 ? -32.124 0.942 -6.587 1.00 24.95 ? 437 LEU B CD2 1 ATOM 3165 N N . ALA B 2 140 ? -31.512 4.660 -3.216 1.00 17.73 ? 438 ALA B N 1 ATOM 3166 C CA . ALA B 2 140 ? -31.194 6.068 -3.483 1.00 17.31 ? 438 ALA B CA 1 ATOM 3167 C C . ALA B 2 140 ? -30.090 6.553 -2.535 1.00 20.32 ? 438 ALA B C 1 ATOM 3168 O O . ALA B 2 140 ? -29.172 7.242 -2.981 1.00 20.11 ? 438 ALA B O 1 ATOM 3169 C CB . ALA B 2 140 ? -32.438 6.930 -3.333 1.00 17.99 ? 438 ALA B CB 1 ATOM 3170 N N . ALA B 2 141 ? -30.160 6.154 -1.242 1.00 16.28 ? 439 ALA B N 1 ATOM 3171 C CA . ALA B 2 141 ? -29.172 6.510 -0.216 1.00 15.97 ? 439 ALA B CA 1 ATOM 3172 C C . ALA B 2 141 ? -27.797 5.924 -0.515 1.00 19.38 ? 439 ALA B C 1 ATOM 3173 O O . ALA B 2 141 ? -26.807 6.631 -0.346 1.00 18.39 ? 439 ALA B O 1 ATOM 3174 C CB . ALA B 2 141 ? -29.641 6.065 1.157 1.00 16.67 ? 439 ALA B CB 1 ATOM 3175 N N . PHE B 2 142 ? -27.731 4.645 -0.967 1.00 16.62 ? 440 PHE B N 1 ATOM 3176 C CA . PHE B 2 142 ? -26.458 4.003 -1.314 1.00 16.51 ? 440 PHE B CA 1 ATOM 3177 C C . PHE B 2 142 ? -25.828 4.673 -2.537 1.00 19.99 ? 440 PHE B C 1 ATOM 3178 O O . PHE B 2 142 ? -24.618 4.900 -2.542 1.00 19.37 ? 440 PHE B O 1 ATOM 3179 C CB . PHE B 2 142 ? -26.608 2.481 -1.547 1.00 18.39 ? 440 PHE B CB 1 ATOM 3180 C CG . PHE B 2 142 ? -25.309 1.826 -1.971 1.00 19.98 ? 440 PHE B CG 1 ATOM 3181 C CD1 . PHE B 2 142 ? -24.369 1.432 -1.026 1.00 23.15 ? 440 PHE B CD1 1 ATOM 3182 C CD2 . PHE B 2 142 ? -24.997 1.668 -3.319 1.00 22.35 ? 440 PHE B CD2 1 ATOM 3183 C CE1 . PHE B 2 142 ? -23.147 0.875 -1.420 1.00 24.09 ? 440 PHE B CE1 1 ATOM 3184 C CE2 . PHE B 2 142 ? -23.774 1.114 -3.711 1.00 25.33 ? 440 PHE B CE2 1 ATOM 3185 C CZ . PHE B 2 142 ? -22.860 0.714 -2.759 1.00 23.33 ? 440 PHE B CZ 1 ATOM 3186 N N . THR B 2 143 ? -26.646 4.955 -3.578 1.00 16.52 ? 441 THR B N 1 ATOM 3187 C CA . THR B 2 143 ? -26.211 5.593 -4.827 1.00 16.46 ? 441 THR B CA 1 ATOM 3188 C C . THR B 2 143 ? -25.584 6.959 -4.536 1.00 19.95 ? 441 THR B C 1 ATOM 3189 O O . THR B 2 143 ? -24.512 7.261 -5.061 1.00 19.45 ? 441 THR B O 1 ATOM 3190 C CB . THR B 2 143 ? -27.372 5.669 -5.835 1.00 23.13 ? 441 THR B CB 1 ATOM 3191 O OG1 . THR B 2 143 ? -27.970 4.380 -5.963 1.00 21.82 ? 441 THR B OG1 1 ATOM 3192 C CG2 . THR B 2 143 ? -26.927 6.148 -7.207 1.00 22.29 ? 441 THR B CG2 1 ATOM 3193 N N . MET B 2 144 ? -26.245 7.757 -3.675 1.00 16.44 ? 442 MET B N 1 ATOM 3194 C CA . MET B 2 144 ? -25.791 9.077 -3.239 1.00 16.12 ? 442 MET B CA 1 ATOM 3195 C C . MET B 2 144 ? -24.496 8.948 -2.420 1.00 20.50 ? 442 MET B C 1 ATOM 3196 O O . MET B 2 144 ? -23.558 9.714 -2.653 1.00 20.30 ? 442 MET B O 1 ATOM 3197 C CB . MET B 2 144 ? -26.905 9.765 -2.431 1.00 18.21 ? 442 MET B CB 1 ATOM 3198 C CG . MET B 2 144 ? -26.485 11.055 -1.757 1.00 21.35 ? 442 MET B CG 1 ATOM 3199 S SD . MET B 2 144 ? -27.457 11.371 -0.270 1.00 24.97 ? 442 MET B SD 1 ATOM 3200 C CE . MET B 2 144 ? -26.696 10.230 0.876 1.00 21.70 ? 442 MET B CE 1 ATOM 3201 N N . PHE B 2 145 ? -24.444 7.970 -1.486 1.00 17.45 ? 443 PHE B N 1 ATOM 3202 C CA . PHE B 2 145 ? -23.272 7.718 -0.637 1.00 17.49 ? 443 PHE B CA 1 ATOM 3203 C C . PHE B 2 145 ? -22.039 7.337 -1.461 1.00 21.86 ? 443 PHE B C 1 ATOM 3204 O O . PHE B 2 145 ? -20.945 7.826 -1.178 1.00 21.51 ? 443 PHE B O 1 ATOM 3205 C CB . PHE B 2 145 ? -23.576 6.659 0.438 1.00 19.03 ? 443 PHE B CB 1 ATOM 3206 C CG . PHE B 2 145 ? -22.416 6.309 1.342 1.00 20.33 ? 443 PHE B CG 1 ATOM 3207 C CD1 . PHE B 2 145 ? -21.903 7.241 2.238 1.00 23.00 ? 443 PHE B CD1 1 ATOM 3208 C CD2 . PHE B 2 145 ? -21.844 5.042 1.305 1.00 22.20 ? 443 PHE B CD2 1 ATOM 3209 C CE1 . PHE B 2 145 ? -20.834 6.914 3.076 1.00 23.76 ? 443 PHE B CE1 1 ATOM 3210 C CE2 . PHE B 2 145 ? -20.776 4.716 2.146 1.00 24.71 ? 443 PHE B CE2 1 ATOM 3211 C CZ . PHE B 2 145 ? -20.287 5.649 3.035 1.00 22.69 ? 443 PHE B CZ 1 ATOM 3212 N N . SER B 2 146 ? -22.231 6.489 -2.489 1.00 18.68 ? 444 SER B N 1 ATOM 3213 C CA . SER B 2 146 ? -21.176 6.038 -3.398 1.00 18.53 ? 444 SER B CA 1 ATOM 3214 C C . SER B 2 146 ? -20.610 7.199 -4.219 1.00 22.27 ? 444 SER B C 1 ATOM 3215 O O . SER B 2 146 ? -19.392 7.307 -4.358 1.00 22.10 ? 444 SER B O 1 ATOM 3216 C CB . SER B 2 146 ? -21.693 4.932 -4.313 1.00 22.11 ? 444 SER B CB 1 ATOM 3217 O OG . SER B 2 146 ? -20.653 4.403 -5.118 1.00 32.15 ? 444 SER B OG 1 ATOM 3218 N N . ARG B 2 147 ? -21.493 8.076 -4.735 1.00 18.54 ? 445 ARG B N 1 ATOM 3219 C CA . ARG B 2 147 ? -21.109 9.254 -5.517 1.00 18.27 ? 445 ARG B CA 1 ATOM 3220 C C . ARG B 2 147 ? -20.338 10.259 -4.649 1.00 22.51 ? 445 ARG B C 1 ATOM 3221 O O . ARG B 2 147 ? -19.364 10.850 -5.120 1.00 22.20 ? 445 ARG B O 1 ATOM 3222 C CB . ARG B 2 147 ? -22.341 9.887 -6.183 1.00 18.19 ? 445 ARG B CB 1 ATOM 3223 C CG . ARG B 2 147 ? -22.763 9.125 -7.435 1.00 27.05 ? 445 ARG B CG 1 ATOM 3224 C CD . ARG B 2 147 ? -24.189 9.385 -7.868 1.00 36.48 ? 445 ARG B CD 1 ATOM 3225 N NE . ARG B 2 147 ? -24.538 8.549 -9.021 1.00 45.72 ? 445 ARG B NE 1 ATOM 3226 C CZ . ARG B 2 147 ? -25.748 8.476 -9.567 1.00 59.94 ? 445 ARG B CZ 1 ATOM 3227 N NH1 . ARG B 2 147 ? -26.756 9.178 -9.064 1.00 45.35 ? 445 ARG B NH1 1 ATOM 3228 N NH2 . ARG B 2 147 ? -25.965 7.680 -10.605 1.00 48.74 ? 445 ARG B NH2 1 ATOM 3229 N N . PHE B 2 148 ? -20.739 10.391 -3.366 1.00 18.87 ? 446 PHE B N 1 ATOM 3230 C CA . PHE B 2 148 ? -20.104 11.260 -2.372 1.00 18.65 ? 446 PHE B CA 1 ATOM 3231 C C . PHE B 2 148 ? -18.668 10.806 -2.058 1.00 23.54 ? 446 PHE B C 1 ATOM 3232 O O . PHE B 2 148 ? -17.753 11.628 -2.128 1.00 23.17 ? 446 PHE B O 1 ATOM 3233 C CB . PHE B 2 148 ? -20.969 11.348 -1.095 1.00 20.11 ? 446 PHE B CB 1 ATOM 3234 C CG . PHE B 2 148 ? -20.280 11.886 0.138 1.00 21.09 ? 446 PHE B CG 1 ATOM 3235 C CD1 . PHE B 2 148 ? -20.015 13.245 0.272 1.00 23.74 ? 446 PHE B CD1 1 ATOM 3236 C CD2 . PHE B 2 148 ? -19.914 11.038 1.175 1.00 22.85 ? 446 PHE B CD2 1 ATOM 3237 C CE1 . PHE B 2 148 ? -19.379 13.742 1.413 1.00 24.34 ? 446 PHE B CE1 1 ATOM 3238 C CE2 . PHE B 2 148 ? -19.282 11.536 2.318 1.00 25.39 ? 446 PHE B CE2 1 ATOM 3239 C CZ . PHE B 2 148 ? -19.020 12.885 2.429 1.00 23.26 ? 446 PHE B CZ 1 ATOM 3240 N N . LEU B 2 149 ? -18.476 9.506 -1.722 1.00 21.15 ? 447 LEU B N 1 ATOM 3241 C CA . LEU B 2 149 ? -17.166 8.923 -1.402 1.00 21.53 ? 447 LEU B CA 1 ATOM 3242 C C . LEU B 2 149 ? -16.184 9.021 -2.566 1.00 25.84 ? 447 LEU B C 1 ATOM 3243 O O . LEU B 2 149 ? -15.017 9.354 -2.357 1.00 25.42 ? 447 LEU B O 1 ATOM 3244 C CB . LEU B 2 149 ? -17.288 7.439 -0.997 1.00 21.74 ? 447 LEU B CB 1 ATOM 3245 C CG . LEU B 2 149 ? -17.848 7.061 0.376 1.00 26.77 ? 447 LEU B CG 1 ATOM 3246 C CD1 . LEU B 2 149 ? -17.539 5.611 0.671 1.00 27.11 ? 447 LEU B CD1 1 ATOM 3247 C CD2 . LEU B 2 149 ? -17.255 7.904 1.493 1.00 29.06 ? 447 LEU B CD2 1 ATOM 3248 N N . ASN B 2 150 ? -16.658 8.708 -3.785 1.00 22.64 ? 448 ASN B N 1 ATOM 3249 C CA . ASN B 2 150 ? -15.859 8.709 -5.009 1.00 22.87 ? 448 ASN B CA 1 ATOM 3250 C C . ASN B 2 150 ? -15.718 10.086 -5.667 1.00 27.38 ? 448 ASN B C 1 ATOM 3251 O O . ASN B 2 150 ? -15.083 10.186 -6.721 1.00 27.29 ? 448 ASN B O 1 ATOM 3252 C CB . ASN B 2 150 ? -16.396 7.663 -5.993 1.00 23.54 ? 448 ASN B CB 1 ATOM 3253 C CG . ASN B 2 150 ? -16.184 6.247 -5.527 1.00 42.48 ? 448 ASN B CG 1 ATOM 3254 O OD1 . ASN B 2 150 ? -15.073 5.711 -5.580 1.00 37.65 ? 448 ASN B OD1 1 ATOM 3255 N ND2 . ASN B 2 150 ? -17.243 5.614 -5.048 1.00 31.91 ? 448 ASN B ND2 1 ATOM 3256 N N . LYS B 2 151 ? -16.287 11.148 -5.036 1.00 24.24 ? 449 LYS B N 1 ATOM 3257 C CA . LYS B 2 151 ? -16.251 12.549 -5.490 1.00 24.43 ? 449 LYS B CA 1 ATOM 3258 C C . LYS B 2 151 ? -16.827 12.718 -6.916 1.00 28.72 ? 449 LYS B C 1 ATOM 3259 O O . LYS B 2 151 ? -16.370 13.565 -7.690 1.00 28.32 ? 449 LYS B O 1 ATOM 3260 C CB . LYS B 2 151 ? -14.822 13.117 -5.370 1.00 27.30 ? 449 LYS B CB 1 ATOM 3261 C CG . LYS B 2 151 ? -14.755 14.603 -5.043 1.00 43.46 ? 449 LYS B CG 1 ATOM 3262 C CD . LYS B 2 151 ? -13.326 15.191 -5.128 1.00 54.07 ? 449 LYS B CD 1 ATOM 3263 C CE . LYS B 2 151 ? -12.274 14.546 -4.238 1.00 65.80 ? 449 LYS B CE 1 ATOM 3264 N NZ . LYS B 2 151 ? -12.695 14.456 -2.814 1.00 74.62 ? 449 LYS B NZ 1 ATOM 3265 N N . GLN B 2 152 ? -17.836 11.896 -7.249 1.00 25.40 ? 450 GLN B N 1 ATOM 3266 C CA . GLN B 2 152 ? -18.507 11.882 -8.550 1.00 25.31 ? 450 GLN B CA 1 ATOM 3267 C C . GLN B 2 152 ? -19.731 12.814 -8.532 1.00 29.25 ? 450 GLN B C 1 ATOM 3268 O O . GLN B 2 152 ? -20.264 13.060 -7.445 1.00 29.43 ? 450 GLN B O 1 ATOM 3269 C CB . GLN B 2 152 ? -18.959 10.443 -8.897 1.00 26.70 ? 450 GLN B CB 1 ATOM 3270 C CG . GLN B 2 152 ? -17.837 9.409 -9.022 1.00 43.74 ? 450 GLN B CG 1 ATOM 3271 C CD . GLN B 2 152 ? -16.965 9.618 -10.236 1.00 63.96 ? 450 GLN B CD 1 ATOM 3272 O OE1 . GLN B 2 152 ? -17.361 9.347 -11.375 1.00 59.59 ? 450 GLN B OE1 1 ATOM 3273 N NE2 . GLN B 2 152 ? -15.745 10.083 -10.011 1.00 55.70 ? 450 GLN B NE2 1 ATOM 3274 N N . PRO B 2 153 ? -20.237 13.308 -9.696 1.00 24.99 ? 451 PRO B N 1 ATOM 3275 C CA . PRO B 2 153 ? -21.461 14.135 -9.666 1.00 24.23 ? 451 PRO B CA 1 ATOM 3276 C C . PRO B 2 153 ? -22.655 13.314 -9.181 1.00 25.70 ? 451 PRO B C 1 ATOM 3277 O O . PRO B 2 153 ? -22.684 12.098 -9.381 1.00 24.69 ? 451 PRO B O 1 ATOM 3278 C CB . PRO B 2 153 ? -21.653 14.557 -11.127 1.00 26.14 ? 451 PRO B CB 1 ATOM 3279 C CG . PRO B 2 153 ? -20.367 14.281 -11.788 1.00 30.76 ? 451 PRO B CG 1 ATOM 3280 C CD . PRO B 2 153 ? -19.762 13.123 -11.081 1.00 26.44 ? 451 PRO B CD 1 ATOM 3281 N N . TYR B 2 154 ? -23.615 13.967 -8.520 1.00 21.34 ? 452 TYR B N 1 ATOM 3282 C CA . TYR B 2 154 ? -24.783 13.282 -7.972 1.00 20.63 ? 452 TYR B CA 1 ATOM 3283 C C . TYR B 2 154 ? -25.827 12.876 -9.006 1.00 23.97 ? 452 TYR B C 1 ATOM 3284 O O . TYR B 2 154 ? -26.555 11.914 -8.765 1.00 23.33 ? 452 TYR B O 1 ATOM 3285 C CB . TYR B 2 154 ? -25.388 14.061 -6.795 1.00 21.51 ? 452 TYR B CB 1 ATOM 3286 C CG . TYR B 2 154 ? -24.441 14.165 -5.618 1.00 22.69 ? 452 TYR B CG 1 ATOM 3287 C CD1 . TYR B 2 154 ? -24.282 13.105 -4.730 1.00 24.49 ? 452 TYR B CD1 1 ATOM 3288 C CD2 . TYR B 2 154 ? -23.686 15.315 -5.404 1.00 23.49 ? 452 TYR B CD2 1 ATOM 3289 C CE1 . TYR B 2 154 ? -23.395 13.186 -3.657 1.00 25.09 ? 452 TYR B CE1 1 ATOM 3290 C CE2 . TYR B 2 154 ? -22.807 15.413 -4.326 1.00 24.31 ? 452 TYR B CE2 1 ATOM 3291 C CZ . TYR B 2 154 ? -22.664 14.345 -3.455 1.00 30.83 ? 452 TYR B CZ 1 ATOM 3292 O OH . TYR B 2 154 ? -21.797 14.434 -2.394 1.00 31.56 ? 452 TYR B OH 1 ATOM 3293 N N . GLU B 2 155 ? -25.868 13.574 -10.169 1.00 19.94 ? 453 GLU B N 1 ATOM 3294 C CA . GLU B 2 155 ? -26.803 13.334 -11.280 1.00 20.45 ? 453 GLU B CA 1 ATOM 3295 C C . GLU B 2 155 ? -26.804 11.884 -11.779 1.00 24.03 ? 453 GLU B C 1 ATOM 3296 O O . GLU B 2 155 ? -25.710 11.318 -11.987 1.00 26.15 ? 453 GLU B O 1 ATOM 3297 C CB . GLU B 2 155 ? -26.534 14.303 -12.445 1.00 21.66 ? 453 GLU B CB 1 ATOM 3298 C CG . GLU B 2 155 ? -26.995 15.731 -12.193 1.00 27.80 ? 453 GLU B CG 1 ATOM 3299 C CD . GLU B 2 155 ? -26.044 16.670 -11.470 1.00 39.01 ? 453 GLU B CD 1 ATOM 3300 O OE1 . GLU B 2 155 ? -24.991 16.213 -10.967 1.00 25.93 ? 453 GLU B OE1 1 ATOM 3301 O OE2 . GLU B 2 155 ? -26.368 17.877 -11.398 1.00 30.20 ? 453 GLU B OE2 1 ATOM 3302 O OXT . GLU B 2 155 ? -27.903 11.311 -11.935 1.00 36.75 ? 453 GLU B OXT 1 HETATM 3303 C C35 A S35 C 3 . ? -36.257 9.586 15.402 0.51 16.51 ? 1259 S35 A C35 1 HETATM 3304 C C35 B S35 C 3 . ? -36.352 9.560 15.609 0.49 32.49 ? 1259 S35 A C35 1 HETATM 3305 C C30 A S35 C 3 . ? -35.048 8.739 15.827 0.51 16.53 ? 1259 S35 A C30 1 HETATM 3306 C C30 B S35 C 3 . ? -35.129 8.736 16.046 0.49 32.61 ? 1259 S35 A C30 1 HETATM 3307 C C31 A S35 C 3 . ? -35.246 7.358 15.948 0.51 16.31 ? 1259 S35 A C31 1 HETATM 3308 C C31 B S35 C 3 . ? -35.334 7.367 16.267 0.49 32.57 ? 1259 S35 A C31 1 HETATM 3309 C C32 A S35 C 3 . ? -34.198 6.516 16.331 0.51 16.49 ? 1259 S35 A C32 1 HETATM 3310 C C32 B S35 C 3 . ? -34.273 6.537 16.641 0.49 32.61 ? 1259 S35 A C32 1 HETATM 3311 C C33 A S35 C 3 . ? -32.939 7.060 16.596 0.51 16.90 ? 1259 S35 A C33 1 HETATM 3312 C C33 B S35 C 3 . ? -33.000 7.082 16.820 0.49 32.79 ? 1259 S35 A C33 1 HETATM 3313 C C34 A S35 C 3 . ? -32.735 8.437 16.473 0.51 16.78 ? 1259 S35 A C34 1 HETATM 3314 C C34 B S35 C 3 . ? -32.793 8.447 16.608 0.49 32.78 ? 1259 S35 A C34 1 HETATM 3315 C C29 A S35 C 3 . ? -33.774 9.299 16.079 0.51 16.51 ? 1259 S35 A C29 1 HETATM 3316 C C29 B S35 C 3 . ? -33.837 9.293 16.196 0.49 32.66 ? 1259 S35 A C29 1 HETATM 3317 C C24 A S35 C 3 . ? -33.529 10.834 15.966 0.51 16.45 ? 1259 S35 A C24 1 HETATM 3318 C C24 B S35 C 3 . ? -33.590 10.822 16.029 0.49 32.64 ? 1259 S35 A C24 1 HETATM 3319 C C25 A S35 C 3 . ? -32.061 11.220 15.683 0.51 14.84 ? 1259 S35 A C25 1 HETATM 3320 C C25 B S35 C 3 . ? -32.118 11.210 15.762 0.49 32.10 ? 1259 S35 A C25 1 HETATM 3321 C C26 A S35 C 3 . ? -31.558 10.824 14.286 0.51 13.11 ? 1259 S35 A C26 1 HETATM 3322 C C26 B S35 C 3 . ? -31.612 10.824 14.362 0.49 31.55 ? 1259 S35 A C26 1 HETATM 3323 O O28 A S35 C 3 . ? -32.335 10.985 13.322 0.51 12.76 ? 1259 S35 A O28 1 HETATM 3324 O O28 B S35 C 3 . ? -32.361 11.050 13.388 0.49 31.43 ? 1259 S35 A O28 1 HETATM 3325 O O27 A S35 C 3 . ? -30.380 10.417 14.210 0.51 11.92 ? 1259 S35 A O27 1 HETATM 3326 O O27 B S35 C 3 . ? -30.457 10.355 14.295 0.49 31.08 ? 1259 S35 A O27 1 HETATM 3327 N N23 A S35 C 3 . ? -33.940 11.491 17.219 0.51 18.18 ? 1259 S35 A N23 1 HETATM 3328 N N23 B S35 C 3 . ? -34.032 11.447 17.289 0.49 33.20 ? 1259 S35 A N23 1 HETATM 3329 C C21 A S35 C 3 . ? -34.587 12.659 17.307 0.51 19.57 ? 1259 S35 A C21 1 HETATM 3330 C C21 B S35 C 3 . ? -34.635 12.633 17.421 0.49 33.67 ? 1259 S35 A C21 1 HETATM 3331 O O22 A S35 C 3 . ? -34.946 13.354 16.353 0.51 19.36 ? 1259 S35 A O22 1 HETATM 3332 O O22 B S35 C 3 . ? -34.868 13.426 16.505 0.49 33.64 ? 1259 S35 A O22 1 HETATM 3333 C C10 A S35 C 3 . ? -34.841 13.104 18.753 0.51 21.17 ? 1259 S35 A C10 1 HETATM 3334 C C10 B S35 C 3 . ? -35.045 12.945 18.868 0.49 34.11 ? 1259 S35 A C10 1 HETATM 3335 N N9 A S35 C 3 . ? -34.792 12.273 19.791 0.51 21.43 ? 1259 S35 A N9 1 HETATM 3336 N N9 B S35 C 3 . ? -34.848 12.106 19.883 0.49 34.29 ? 1259 S35 A N9 1 HETATM 3337 C C11 A S35 C 3 . ? -35.091 14.343 19.173 0.51 22.35 ? 1259 S35 A C11 1 HETATM 3338 C C11 B S35 C 3 . ? -35.688 14.030 19.296 0.49 34.39 ? 1259 S35 A C11 1 HETATM 3339 C C12 A S35 C 3 . ? -35.233 14.208 20.494 0.51 23.61 ? 1259 S35 A C12 1 HETATM 3340 C C12 B S35 C 3 . ? -35.852 13.808 20.600 0.49 34.93 ? 1259 S35 A C12 1 HETATM 3341 O O13 A S35 C 3 . ? -35.453 15.200 21.417 0.51 25.11 ? 1259 S35 A O13 1 HETATM 3342 O O13 B S35 C 3 . ? -36.446 14.671 21.483 0.49 35.22 ? 1259 S35 A O13 1 HETATM 3343 C C14 A S35 C 3 . ? -36.421 16.236 21.098 0.51 25.81 ? 1259 S35 A C14 1 HETATM 3344 C C14 B S35 C 3 . ? -37.861 14.390 21.630 0.49 35.56 ? 1259 S35 A C14 1 HETATM 3345 C C15 A S35 C 3 . ? -35.753 17.635 21.132 0.51 26.21 ? 1259 S35 A C15 1 HETATM 3346 C C15 B S35 C 3 . ? -38.637 15.314 22.592 0.49 35.75 ? 1259 S35 A C15 1 HETATM 3347 C C17 A S35 C 3 . ? -36.687 18.868 21.374 0.51 26.86 ? 1259 S35 A C17 1 HETATM 3348 C C17 B S35 C 3 . ? -38.210 15.366 24.095 0.49 35.69 ? 1259 S35 A C17 1 HETATM 3349 C C19 A S35 C 3 . ? -35.990 20.121 20.834 0.51 26.90 ? 1259 S35 A C19 1 HETATM 3350 C C19 B S35 C 3 . ? -39.478 15.549 24.933 0.49 35.67 ? 1259 S35 A C19 1 HETATM 3351 C C20 A S35 C 3 . ? -38.030 18.743 20.635 0.51 26.78 ? 1259 S35 A C20 1 HETATM 3352 C C20 B S35 C 3 . ? -37.519 14.083 24.592 0.49 35.38 ? 1259 S35 A C20 1 HETATM 3353 C C18 A S35 C 3 . ? -36.972 19.088 22.870 0.51 26.99 ? 1259 S35 A C18 1 HETATM 3354 C C18 B S35 C 3 . ? -37.280 16.554 24.369 0.49 36.14 ? 1259 S35 A C18 1 HETATM 3355 O O16 A S35 C 3 . ? -34.631 17.628 22.033 0.51 25.50 ? 1259 S35 A O16 1 HETATM 3356 O O16 B S35 C 3 . ? -38.798 16.616 22.006 0.49 36.03 ? 1259 S35 A O16 1 HETATM 3357 N N8 A S35 C 3 . ? -34.987 12.934 20.808 0.51 22.72 ? 1259 S35 A N8 1 HETATM 3358 N N8 B S35 C 3 . ? -35.298 12.629 20.899 0.49 34.89 ? 1259 S35 A N8 1 HETATM 3359 C C6 A S35 C 3 . ? -35.046 12.389 22.023 0.51 23.32 ? 1259 S35 A C6 1 HETATM 3360 C C6 B S35 C 3 . ? -35.255 12.040 22.098 0.49 35.08 ? 1259 S35 A C6 1 HETATM 3361 C C5 A S35 C 3 . ? -33.876 12.184 22.763 0.51 23.19 ? 1259 S35 A C5 1 HETATM 3362 C C5 B S35 C 3 . ? -36.326 11.243 22.524 0.49 34.99 ? 1259 S35 A C5 1 HETATM 3363 C C4 A S35 C 3 . ? -33.945 11.577 24.022 0.51 23.26 ? 1259 S35 A C4 1 HETATM 3364 C C4 B S35 C 3 . ? -36.280 10.614 23.772 0.49 35.07 ? 1259 S35 A C4 1 HETATM 3365 C C3 A S35 C 3 . ? -35.177 11.161 24.537 0.51 23.34 ? 1259 S35 A C3 1 HETATM 3366 C C3 B S35 C 3 . ? -35.152 10.753 24.586 0.49 34.87 ? 1259 S35 A C3 1 HETATM 3367 C C2 A S35 C 3 . ? -36.345 11.354 23.792 0.51 23.70 ? 1259 S35 A C2 1 HETATM 3368 C C2 B S35 C 3 . ? -34.069 11.523 24.149 0.49 35.04 ? 1259 S35 A C2 1 HETATM 3369 C C1 A S35 C 3 . ? -36.277 11.957 22.530 0.51 23.84 ? 1259 S35 A C1 1 HETATM 3370 C C1 B S35 C 3 . ? -34.117 12.161 22.903 0.49 35.21 ? 1259 S35 A C1 1 HETATM 3371 F F7 A S35 C 3 . ? -37.402 12.136 21.808 0.51 24.64 ? 1259 S35 A F7 1 HETATM 3372 F F7 B S35 C 3 . ? -33.070 12.900 22.487 0.49 35.68 ? 1259 S35 A F7 1 HETATM 3373 CD CD . CD D 4 . ? -33.177 36.970 12.319 0.62 58.80 2 1260 CD A CD 1 HETATM 3374 CD CD . CD E 4 . ? -50.204 41.405 14.810 0.64 28.22 2 1261 CD A CD 1 HETATM 3375 CD CD . CD F 4 . ? -34.965 37.894 14.526 0.45 38.58 2 1262 CD A CD 1 HETATM 3376 C C1 . NAG G 5 . ? -19.241 22.801 28.274 1.00 39.51 ? 3010 NAG A C1 1 HETATM 3377 C C2 . NAG G 5 . ? -19.202 24.066 29.131 1.00 40.37 ? 3010 NAG A C2 1 HETATM 3378 C C3 . NAG G 5 . ? -17.774 24.270 29.634 1.00 41.46 ? 3010 NAG A C3 1 HETATM 3379 C C4 . NAG G 5 . ? -17.281 23.033 30.381 1.00 42.60 ? 3010 NAG A C4 1 HETATM 3380 C C5 . NAG G 5 . ? -17.428 21.794 29.497 1.00 41.43 ? 3010 NAG A C5 1 HETATM 3381 C C6 . NAG G 5 . ? -17.097 20.495 30.198 1.00 41.56 ? 3010 NAG A C6 1 HETATM 3382 C C7 . NAG G 5 . ? -20.738 25.936 28.654 1.00 39.54 ? 3010 NAG A C7 1 HETATM 3383 C C8 . NAG G 5 . ? -20.919 27.201 27.871 1.00 39.00 ? 3010 NAG A C8 1 HETATM 3384 N N2 . NAG G 5 . ? -19.640 25.222 28.365 1.00 39.89 ? 3010 NAG A N2 1 HETATM 3385 O O3 . NAG G 5 . ? -17.725 25.408 30.488 1.00 41.87 ? 3010 NAG A O3 1 HETATM 3386 O O4 . NAG G 5 . ? -15.916 23.230 30.746 1.00 44.72 ? 3010 NAG A O4 1 HETATM 3387 O O5 . NAG G 5 . ? -18.786 21.681 29.035 1.00 40.28 ? 3010 NAG A O5 1 HETATM 3388 O O6 . NAG G 5 . ? -18.015 20.203 31.246 1.00 41.84 ? 3010 NAG A O6 1 HETATM 3389 O O7 . NAG G 5 . ? -21.540 25.584 29.516 1.00 39.36 ? 3010 NAG A O7 1 HETATM 3390 C C1 . NAG H 5 . ? -15.501 22.966 32.085 1.00 46.65 ? 3011 NAG A C1 1 HETATM 3391 C C2 . NAG H 5 . ? -13.996 23.222 32.185 1.00 47.56 ? 3011 NAG A C2 1 HETATM 3392 C C3 . NAG H 5 . ? -13.548 22.907 33.613 1.00 48.15 ? 3011 NAG A C3 1 HETATM 3393 C C4 . NAG H 5 . ? -14.366 23.707 34.624 1.00 48.81 ? 3011 NAG A C4 1 HETATM 3394 C C5 . NAG H 5 . ? -15.860 23.466 34.407 1.00 48.21 ? 3011 NAG A C5 1 HETATM 3395 C C6 . NAG H 5 . ? -16.753 24.314 35.285 1.00 48.20 ? 3011 NAG A C6 1 HETATM 3396 C C7 . NAG H 5 . ? -12.771 22.852 30.073 1.00 47.81 ? 3011 NAG A C7 1 HETATM 3397 C C8 . NAG H 5 . ? -12.126 21.827 29.190 1.00 47.97 ? 3011 NAG A C8 1 HETATM 3398 N N2 . NAG H 5 . ? -13.278 22.393 31.229 1.00 47.58 ? 3011 NAG A N2 1 HETATM 3399 O O3 . NAG H 5 . ? -12.165 23.211 33.758 1.00 47.83 ? 3011 NAG A O3 1 HETATM 3400 O O4 . NAG H 5 . ? -14.003 23.319 35.945 1.00 49.87 ? 3011 NAG A O4 1 HETATM 3401 O O5 . NAG H 5 . ? -16.208 23.761 33.043 1.00 47.43 ? 3011 NAG A O5 1 HETATM 3402 O O6 . NAG H 5 . ? -16.719 25.689 34.921 1.00 48.28 ? 3011 NAG A O6 1 HETATM 3403 O O7 . NAG H 5 . ? -12.835 24.037 29.753 1.00 47.89 ? 3011 NAG A O7 1 HETATM 3404 C C1 . NAG I 5 . ? -43.474 -2.124 17.714 1.00 49.37 ? 3020 NAG A C1 1 HETATM 3405 C C2 . NAG I 5 . ? -44.869 -2.667 17.399 1.00 50.11 ? 3020 NAG A C2 1 HETATM 3406 C C3 . NAG I 5 . ? -44.963 -4.136 17.816 1.00 50.78 ? 3020 NAG A C3 1 HETATM 3407 C C4 . NAG I 5 . ? -43.812 -4.945 17.222 1.00 51.65 ? 3020 NAG A C4 1 HETATM 3408 C C5 . NAG I 5 . ? -42.479 -4.320 17.632 1.00 50.29 ? 3020 NAG A C5 1 HETATM 3409 C C6 . NAG I 5 . ? -41.262 -4.995 17.041 1.00 50.03 ? 3020 NAG A C6 1 HETATM 3410 C C7 . NAG I 5 . ? -46.523 -0.837 17.574 1.00 50.08 ? 3020 NAG A C7 1 HETATM 3411 C C8 . NAG I 5 . ? -47.499 -0.148 18.480 1.00 50.10 ? 3020 NAG A C8 1 HETATM 3412 N N2 . NAG I 5 . ? -45.858 -1.874 18.113 1.00 50.15 ? 3020 NAG A N2 1 HETATM 3413 O O3 . NAG I 5 . ? -46.210 -4.676 17.394 1.00 50.68 ? 3020 NAG A O3 1 HETATM 3414 O O4 . NAG I 5 . ? -43.897 -6.295 17.672 1.00 53.99 ? 3020 NAG A O4 1 HETATM 3415 O O5 . NAG I 5 . ? -42.437 -2.955 17.190 1.00 49.56 ? 3020 NAG A O5 1 HETATM 3416 O O6 . NAG I 5 . ? -41.218 -4.879 15.624 1.00 49.86 ? 3020 NAG A O6 1 HETATM 3417 O O7 . NAG I 5 . ? -46.343 -0.472 16.415 1.00 49.58 ? 3020 NAG A O7 1 HETATM 3418 C C1 . NAG J 5 . ? -43.866 -7.339 16.705 1.00 56.36 ? 3021 NAG A C1 1 HETATM 3419 C C2 . NAG J 5 . ? -43.297 -8.596 17.364 1.00 57.24 ? 3021 NAG A C2 1 HETATM 3420 C C3 . NAG J 5 . ? -43.223 -9.681 16.290 1.00 57.97 ? 3021 NAG A C3 1 HETATM 3421 C C4 . NAG J 5 . ? -44.600 -9.923 15.676 1.00 58.30 ? 3021 NAG A C4 1 HETATM 3422 C C5 . NAG J 5 . ? -45.183 -8.614 15.142 1.00 58.21 ? 3021 NAG A C5 1 HETATM 3423 C C6 . NAG J 5 . ? -46.615 -8.735 14.670 1.00 58.47 ? 3021 NAG A C6 1 HETATM 3424 C C7 . NAG J 5 . ? -41.751 -8.140 19.235 1.00 57.14 ? 3021 NAG A C7 1 HETATM 3425 C C8 . NAG J 5 . ? -40.321 -7.905 19.618 1.00 56.85 ? 3021 NAG A C8 1 HETATM 3426 N N2 . NAG J 5 . ? -41.980 -8.342 17.927 1.00 57.24 ? 3021 NAG A N2 1 HETATM 3427 O O3 . NAG J 5 . ? -42.727 -10.886 16.863 1.00 58.25 ? 3021 NAG A O3 1 HETATM 3428 O O4 . NAG J 5 . ? -44.493 -10.868 14.617 1.00 58.48 ? 3021 NAG A O4 1 HETATM 3429 O O5 . NAG J 5 . ? -45.167 -7.612 16.174 1.00 57.53 ? 3021 NAG A O5 1 HETATM 3430 O O6 . NAG J 5 . ? -47.513 -9.012 15.739 1.00 58.58 ? 3021 NAG A O6 1 HETATM 3431 O O7 . NAG J 5 . ? -42.654 -8.145 20.067 1.00 57.40 ? 3021 NAG A O7 1 HETATM 3432 CD CD . CD K 4 . ? -34.175 19.749 13.163 0.22 33.41 2 1454 CD B CD 1 HETATM 3433 O O . HOH L 6 . ? -4.984 -2.951 21.570 1.00 48.12 ? 2001 HOH A O 1 HETATM 3434 O O . HOH L 6 . ? -15.271 29.097 31.200 1.00 44.95 ? 2002 HOH A O 1 HETATM 3435 O O . HOH L 6 . ? -10.757 26.982 37.418 1.00 66.86 ? 2003 HOH A O 1 HETATM 3436 O O . HOH L 6 . ? -44.178 -13.624 21.036 1.00 64.15 ? 2004 HOH A O 1 HETATM 3437 O O . HOH L 6 . ? 1.587 -1.658 14.981 1.00 51.22 ? 2005 HOH A O 1 HETATM 3438 O O . HOH L 6 . ? -4.883 -2.689 18.881 1.00 31.97 ? 2006 HOH A O 1 HETATM 3439 O O . HOH L 6 . ? -11.509 -1.190 26.072 1.00 43.83 ? 2007 HOH A O 1 HETATM 3440 O O . HOH L 6 . ? -14.369 -14.313 11.150 1.00 59.49 ? 2008 HOH A O 1 HETATM 3441 O O . HOH L 6 . ? -3.111 -8.930 18.472 1.00 41.20 ? 2009 HOH A O 1 HETATM 3442 O O . HOH L 6 . ? -19.176 -14.016 22.338 1.00 45.88 ? 2010 HOH A O 1 HETATM 3443 O O . HOH L 6 . ? -13.241 -6.022 24.253 1.00 45.29 ? 2011 HOH A O 1 HETATM 3444 O O . HOH L 6 . ? -26.164 -21.313 12.270 1.00 37.00 ? 2012 HOH A O 1 HETATM 3445 O O . HOH L 6 . ? -29.971 -20.649 11.113 1.00 43.29 ? 2013 HOH A O 1 HETATM 3446 O O . HOH L 6 . ? -13.124 -2.500 24.316 1.00 32.67 ? 2014 HOH A O 1 HETATM 3447 O O . HOH L 6 . ? -11.202 -0.766 22.754 1.00 40.06 ? 2015 HOH A O 1 HETATM 3448 O O . HOH L 6 . ? -15.190 -10.247 12.801 1.00 22.00 ? 2016 HOH A O 1 HETATM 3449 O O . HOH L 6 . ? -14.169 -13.309 13.674 1.00 50.83 ? 2017 HOH A O 1 HETATM 3450 O O . HOH L 6 . ? -18.571 -11.394 13.052 1.00 28.25 ? 2018 HOH A O 1 HETATM 3451 O O . HOH L 6 . ? -17.941 -11.788 19.916 1.00 41.34 ? 2019 HOH A O 1 HETATM 3452 O O . HOH L 6 . ? -9.554 3.480 27.203 1.00 44.24 ? 2020 HOH A O 1 HETATM 3453 O O . HOH L 6 . ? -19.495 -13.948 19.418 1.00 30.62 ? 2021 HOH A O 1 HETATM 3454 O O . HOH L 6 . ? -21.143 -13.173 13.255 1.00 27.17 ? 2022 HOH A O 1 HETATM 3455 O O . HOH L 6 . ? -25.154 -16.838 14.948 1.00 51.04 ? 2023 HOH A O 1 HETATM 3456 O O . HOH L 6 . ? -28.601 -16.961 16.885 1.00 40.74 ? 2024 HOH A O 1 HETATM 3457 O O . HOH L 6 . ? -12.579 0.450 28.207 1.00 34.81 ? 2025 HOH A O 1 HETATM 3458 O O . HOH L 6 . ? -11.781 1.063 32.453 1.00 48.45 ? 2026 HOH A O 1 HETATM 3459 O O . HOH L 6 . ? -29.516 -13.933 8.619 1.00 32.42 ? 2027 HOH A O 1 HETATM 3460 O O . HOH L 6 . ? -27.506 -20.706 9.956 1.00 30.85 ? 2028 HOH A O 1 HETATM 3461 O O . HOH L 6 . ? -24.142 -20.319 8.433 1.00 28.44 ? 2029 HOH A O 1 HETATM 3462 O O . HOH L 6 . ? -28.255 -14.947 5.986 1.00 17.70 ? 2030 HOH A O 1 HETATM 3463 O O . HOH L 6 . ? -29.167 -19.430 1.300 1.00 34.72 ? 2031 HOH A O 1 HETATM 3464 O O . HOH L 6 . ? -21.865 -13.729 4.294 1.00 40.92 ? 2032 HOH A O 1 HETATM 3465 O O . HOH L 6 . ? -25.159 -11.817 1.016 1.00 61.85 ? 2033 HOH A O 1 HETATM 3466 O O . HOH L 6 . ? -16.054 -13.622 9.127 1.00 52.76 ? 2034 HOH A O 1 HETATM 3467 O O . HOH L 6 . ? -20.905 -10.355 4.129 1.00 26.71 ? 2035 HOH A O 1 HETATM 3468 O O . HOH L 6 . ? -13.815 -12.344 7.906 1.00 46.03 ? 2036 HOH A O 1 HETATM 3469 O O . HOH L 6 . ? -15.674 -8.985 2.455 1.00 40.18 ? 2037 HOH A O 1 HETATM 3470 O O . HOH L 6 . ? -16.733 -11.282 10.876 1.00 26.86 ? 2038 HOH A O 1 HETATM 3471 O O . HOH L 6 . ? -12.702 -7.330 6.618 1.00 20.24 ? 2039 HOH A O 1 HETATM 3472 O O . HOH L 6 . ? -8.690 -5.946 10.636 1.00 35.87 ? 2040 HOH A O 1 HETATM 3473 O O . HOH L 6 . ? -35.904 -3.889 6.921 1.00 43.71 ? 2041 HOH A O 1 HETATM 3474 O O . HOH L 6 . ? -10.734 2.115 24.935 1.00 63.53 ? 2042 HOH A O 1 HETATM 3475 O O . HOH L 6 . ? -8.618 9.319 23.492 1.00 30.06 ? 2043 HOH A O 1 HETATM 3476 O O . HOH L 6 . ? -7.706 7.363 31.385 1.00 41.35 ? 2044 HOH A O 1 HETATM 3477 O O . HOH L 6 . ? -11.520 6.640 32.954 1.00 43.61 ? 2045 HOH A O 1 HETATM 3478 O O . HOH L 6 . ? -9.440 10.507 28.777 1.00 46.53 ? 2046 HOH A O 1 HETATM 3479 O O . HOH L 6 . ? -9.946 8.823 32.992 1.00 55.83 ? 2047 HOH A O 1 HETATM 3480 O O . HOH L 6 . ? -37.882 -12.380 10.243 1.00 39.36 ? 2048 HOH A O 1 HETATM 3481 O O . HOH L 6 . ? -14.629 16.993 25.871 1.00 29.42 ? 2049 HOH A O 1 HETATM 3482 O O . HOH L 6 . ? -30.962 -15.397 19.213 1.00 51.44 ? 2050 HOH A O 1 HETATM 3483 O O . HOH L 6 . ? -30.075 -17.820 12.347 1.00 57.39 ? 2051 HOH A O 1 HETATM 3484 O O . HOH L 6 . ? -15.820 12.656 32.174 1.00 24.40 ? 2052 HOH A O 1 HETATM 3485 O O . HOH L 6 . ? -11.331 11.751 34.631 1.00 40.53 ? 2053 HOH A O 1 HETATM 3486 O O . HOH L 6 . ? -33.961 -2.821 1.505 1.00 43.74 ? 2054 HOH A O 1 HETATM 3487 O O . HOH L 6 . ? -23.411 -5.465 -4.300 1.00 56.06 ? 2055 HOH A O 1 HETATM 3488 O O . HOH L 6 . ? -31.912 -4.917 -9.523 1.00 57.12 ? 2056 HOH A O 1 HETATM 3489 O O . HOH L 6 . ? -28.668 -1.323 -7.950 1.00 48.60 ? 2057 HOH A O 1 HETATM 3490 O O . HOH L 6 . ? -12.245 3.285 26.802 1.00 26.78 ? 2058 HOH A O 1 HETATM 3491 O O . HOH L 6 . ? -14.310 1.888 33.047 1.00 37.41 ? 2059 HOH A O 1 HETATM 3492 O O . HOH L 6 . ? -12.186 1.779 -2.573 1.00 49.11 ? 2060 HOH A O 1 HETATM 3493 O O . HOH L 6 . ? -20.741 13.440 28.428 1.00 33.80 ? 2061 HOH A O 1 HETATM 3494 O O . HOH L 6 . ? -13.900 -7.598 4.010 1.00 26.39 ? 2062 HOH A O 1 HETATM 3495 O O . HOH L 6 . ? -20.161 -7.954 -0.803 1.00 52.15 ? 2063 HOH A O 1 HETATM 3496 O O . HOH L 6 . ? -23.080 -9.256 2.492 1.00 53.70 ? 2064 HOH A O 1 HETATM 3497 O O . HOH L 6 . ? -24.636 -6.321 3.697 1.00 20.31 ? 2065 HOH A O 1 HETATM 3498 O O . HOH L 6 . ? -10.290 23.190 20.646 1.00 38.83 ? 2066 HOH A O 1 HETATM 3499 O O . HOH L 6 . ? -12.357 21.808 24.563 1.00 34.19 ? 2067 HOH A O 1 HETATM 3500 O O . HOH L 6 . ? -6.253 15.078 24.635 1.00 46.70 ? 2068 HOH A O 1 HETATM 3501 O O . HOH L 6 . ? -18.818 -4.736 -7.011 1.00 57.40 ? 2069 HOH A O 1 HETATM 3502 O O . HOH L 6 . ? -12.041 -7.601 -0.064 1.00 32.98 ? 2070 HOH A O 1 HETATM 3503 O O . HOH L 6 . ? -8.093 -5.220 1.476 1.00 30.25 ? 2071 HOH A O 1 HETATM 3504 O O . HOH L 6 . ? -8.700 -6.729 -1.328 1.00 62.74 ? 2072 HOH A O 1 HETATM 3505 O O . HOH L 6 . ? -10.930 18.291 27.773 1.00 50.18 ? 2073 HOH A O 1 HETATM 3506 O O . HOH L 6 . ? -8.511 19.530 26.359 1.00 54.85 ? 2074 HOH A O 1 HETATM 3507 O O . HOH L 6 . ? -8.999 5.346 1.695 1.00 27.88 ? 2075 HOH A O 1 HETATM 3508 O O . HOH L 6 . ? 0.616 0.545 17.296 1.00 31.32 ? 2076 HOH A O 1 HETATM 3509 O O . HOH L 6 . ? -4.343 -0.953 -4.506 1.00 65.01 ? 2077 HOH A O 1 HETATM 3510 O O . HOH L 6 . ? -23.981 10.127 17.932 1.00 18.91 ? 2078 HOH A O 1 HETATM 3511 O O . HOH L 6 . ? -26.532 11.699 20.479 1.00 19.35 ? 2079 HOH A O 1 HETATM 3512 O O . HOH L 6 . ? -13.371 24.523 17.730 1.00 32.72 ? 2080 HOH A O 1 HETATM 3513 O O . HOH L 6 . ? -31.786 14.998 16.647 1.00 14.07 ? 2081 HOH A O 1 HETATM 3514 O O . HOH L 6 . ? -24.972 7.916 19.158 1.00 15.79 ? 2082 HOH A O 1 HETATM 3515 O O . HOH L 6 . ? -6.347 16.901 2.048 1.00 42.95 ? 2083 HOH A O 1 HETATM 3516 O O . HOH L 6 . ? -34.349 -2.723 11.106 1.00 26.02 ? 2084 HOH A O 1 HETATM 3517 O O . HOH L 6 . ? -32.338 35.165 0.249 1.00 51.41 ? 2085 HOH A O 1 HETATM 3518 O O . HOH L 6 . ? -35.138 -0.956 8.890 1.00 34.28 ? 2086 HOH A O 1 HETATM 3519 O O . HOH L 6 . ? -36.025 22.445 16.820 1.00 54.48 ? 2087 HOH A O 1 HETATM 3520 O O . HOH L 6 . ? -43.493 24.741 14.354 1.00 46.81 ? 2088 HOH A O 1 HETATM 3521 O O . HOH L 6 . ? -32.581 0.488 5.117 1.00 17.56 ? 2089 HOH A O 1 HETATM 3522 O O . HOH L 6 . ? -29.483 0.663 3.758 1.00 19.04 ? 2090 HOH A O 1 HETATM 3523 O O . HOH L 6 . ? -38.721 35.480 2.180 1.00 39.30 ? 2091 HOH A O 1 HETATM 3524 O O . HOH L 6 . ? -22.800 -0.223 6.861 1.00 17.58 ? 2092 HOH A O 1 HETATM 3525 O O . HOH L 6 . ? -56.255 32.212 -0.177 1.00 56.67 ? 2093 HOH A O 1 HETATM 3526 O O . HOH L 6 . ? -37.537 -4.545 11.809 1.00 34.04 ? 2094 HOH A O 1 HETATM 3527 O O . HOH L 6 . ? -38.837 -10.388 8.720 1.00 38.22 ? 2095 HOH A O 1 HETATM 3528 O O . HOH L 6 . ? -34.457 -6.112 6.290 1.00 38.86 ? 2096 HOH A O 1 HETATM 3529 O O . HOH L 6 . ? -39.436 -10.789 12.165 1.00 39.63 ? 2097 HOH A O 1 HETATM 3530 O O . HOH L 6 . ? -39.124 -13.941 12.067 1.00 88.31 ? 2098 HOH A O 1 HETATM 3531 O O . HOH L 6 . ? -33.260 -10.913 21.008 1.00 36.23 ? 2099 HOH A O 1 HETATM 3532 O O . HOH L 6 . ? -30.653 -12.885 18.251 1.00 29.69 ? 2100 HOH A O 1 HETATM 3533 O O . HOH L 6 . ? -36.048 -16.091 11.838 1.00 52.95 ? 2101 HOH A O 1 HETATM 3534 O O . HOH L 6 . ? -33.012 -15.880 13.289 1.00 46.80 ? 2102 HOH A O 1 HETATM 3535 O O . HOH L 6 . ? -46.887 36.540 22.890 1.00 41.26 ? 2103 HOH A O 1 HETATM 3536 O O . HOH L 6 . ? -32.069 -6.221 4.904 1.00 38.05 ? 2104 HOH A O 1 HETATM 3537 O O . HOH L 6 . ? -33.847 -14.640 4.782 1.00 43.94 ? 2105 HOH A O 1 HETATM 3538 O O . HOH L 6 . ? -31.884 -15.313 6.809 1.00 43.59 ? 2106 HOH A O 1 HETATM 3539 O O . HOH L 6 . ? -30.107 -11.964 4.960 1.00 25.36 ? 2107 HOH A O 1 HETATM 3540 O O . HOH L 6 . ? -30.006 -14.408 4.133 1.00 34.39 ? 2108 HOH A O 1 HETATM 3541 O O . HOH L 6 . ? -56.658 31.339 13.131 1.00 47.61 ? 2109 HOH A O 1 HETATM 3542 O O . HOH L 6 . ? -31.007 -10.195 2.783 1.00 42.18 ? 2110 HOH A O 1 HETATM 3543 O O . HOH L 6 . ? -28.916 -9.973 1.024 1.00 50.65 ? 2111 HOH A O 1 HETATM 3544 O O . HOH L 6 . ? -32.061 -1.789 3.102 1.00 24.66 ? 2112 HOH A O 1 HETATM 3545 O O . HOH L 6 . ? -25.384 -5.669 -2.423 1.00 35.34 ? 2113 HOH A O 1 HETATM 3546 O O . HOH L 6 . ? -26.405 -1.424 -4.932 1.00 40.34 ? 2114 HOH A O 1 HETATM 3547 O O . HOH L 6 . ? -28.429 2.613 1.848 1.00 18.37 ? 2115 HOH A O 1 HETATM 3548 O O . HOH L 6 . ? -31.142 -3.282 -6.692 1.00 50.85 ? 2116 HOH A O 1 HETATM 3549 O O . HOH L 6 . ? -43.688 16.516 21.480 1.00 64.69 ? 2117 HOH A O 1 HETATM 3550 O O . HOH L 6 . ? -51.159 6.858 7.952 1.00 34.59 ? 2118 HOH A O 1 HETATM 3551 O O . HOH L 6 . ? -18.856 -3.859 -2.807 1.00 38.93 ? 2119 HOH A O 1 HETATM 3552 O O . HOH L 6 . ? -14.930 2.577 -1.915 1.00 25.57 ? 2120 HOH A O 1 HETATM 3553 O O . HOH L 6 . ? -22.012 12.766 19.142 1.00 19.85 ? 2121 HOH A O 1 HETATM 3554 O O . HOH L 6 . ? -18.814 12.943 22.405 1.00 23.63 ? 2122 HOH A O 1 HETATM 3555 O O . HOH L 6 . ? -18.902 12.232 25.048 1.00 19.51 ? 2123 HOH A O 1 HETATM 3556 O O . HOH L 6 . ? -23.250 12.811 28.039 1.00 22.08 ? 2124 HOH A O 1 HETATM 3557 O O . HOH L 6 . ? -26.674 5.129 30.210 1.00 33.30 ? 2125 HOH A O 1 HETATM 3558 O O . HOH L 6 . ? -28.764 2.812 27.290 1.00 23.50 ? 2126 HOH A O 1 HETATM 3559 O O . HOH L 6 . ? -29.429 5.807 24.995 1.00 36.63 ? 2127 HOH A O 1 HETATM 3560 O O . HOH L 6 . ? -25.666 0.750 29.077 1.00 19.85 ? 2128 HOH A O 1 HETATM 3561 O O . HOH L 6 . ? -24.459 3.170 29.942 1.00 21.31 ? 2129 HOH A O 1 HETATM 3562 O O . HOH L 6 . ? -14.748 -0.853 29.178 1.00 34.67 ? 2130 HOH A O 1 HETATM 3563 O O . HOH L 6 . ? -20.472 3.644 35.016 1.00 37.61 ? 2131 HOH A O 1 HETATM 3564 O O . HOH L 6 . ? -18.467 12.275 32.603 1.00 38.25 ? 2132 HOH A O 1 HETATM 3565 O O . HOH L 6 . ? -26.115 12.125 34.370 1.00 29.87 ? 2133 HOH A O 1 HETATM 3566 O O . HOH L 6 . ? -20.510 14.825 30.836 1.00 34.27 ? 2134 HOH A O 1 HETATM 3567 O O . HOH L 6 . ? -26.257 15.970 28.510 1.00 18.40 ? 2135 HOH A O 1 HETATM 3568 O O . HOH L 6 . ? -26.320 5.080 34.701 1.00 49.59 ? 2136 HOH A O 1 HETATM 3569 O O . HOH L 6 . ? -20.316 18.781 31.565 1.00 40.06 ? 2137 HOH A O 1 HETATM 3570 O O . HOH L 6 . ? -19.569 14.618 26.305 1.00 18.27 ? 2138 HOH A O 1 HETATM 3571 O O . HOH L 6 . ? -22.359 21.794 30.086 1.00 34.72 ? 2139 HOH A O 1 HETATM 3572 O O . HOH L 6 . ? -20.708 18.851 19.006 1.00 20.43 ? 2140 HOH A O 1 HETATM 3573 O O . HOH L 6 . ? -27.578 23.687 19.191 1.00 26.15 ? 2141 HOH A O 1 HETATM 3574 O O . HOH L 6 . ? -14.897 21.579 21.057 1.00 23.57 ? 2142 HOH A O 1 HETATM 3575 O O . HOH L 6 . ? -17.829 25.831 25.737 1.00 30.92 ? 2143 HOH A O 1 HETATM 3576 O O . HOH L 6 . ? -14.443 20.753 25.951 1.00 47.95 ? 2144 HOH A O 1 HETATM 3577 O O . HOH L 6 . ? -14.568 18.097 29.567 1.00 43.44 ? 2145 HOH A O 1 HETATM 3578 O O . HOH L 6 . ? -19.264 16.181 17.784 1.00 17.59 ? 2146 HOH A O 1 HETATM 3579 O O . HOH L 6 . ? -8.251 21.374 20.892 1.00 59.30 ? 2147 HOH A O 1 HETATM 3580 O O . HOH L 6 . ? -12.287 21.390 21.871 1.00 31.97 ? 2148 HOH A O 1 HETATM 3581 O O . HOH L 6 . ? -6.956 16.496 21.835 1.00 49.02 ? 2149 HOH A O 1 HETATM 3582 O O . HOH L 6 . ? -6.468 18.823 24.705 1.00 64.09 ? 2150 HOH A O 1 HETATM 3583 O O . HOH L 6 . ? -6.833 11.158 22.519 1.00 25.56 ? 2151 HOH A O 1 HETATM 3584 O O . HOH L 6 . ? -7.088 12.032 25.824 1.00 66.50 ? 2152 HOH A O 1 HETATM 3585 O O . HOH L 6 . ? -9.419 15.938 27.431 1.00 42.95 ? 2153 HOH A O 1 HETATM 3586 O O . HOH L 6 . ? -4.384 8.596 17.004 1.00 25.23 ? 2154 HOH A O 1 HETATM 3587 O O . HOH L 6 . ? -4.022 12.539 16.320 1.00 31.10 ? 2155 HOH A O 1 HETATM 3588 O O . HOH L 6 . ? -4.146 17.360 17.307 1.00 36.51 ? 2156 HOH A O 1 HETATM 3589 O O . HOH L 6 . ? -8.272 3.164 24.887 1.00 55.28 ? 2157 HOH A O 1 HETATM 3590 O O . HOH L 6 . ? -6.254 2.763 23.224 1.00 56.38 ? 2158 HOH A O 1 HETATM 3591 O O . HOH L 6 . ? -1.205 2.398 17.819 1.00 32.05 ? 2159 HOH A O 1 HETATM 3592 O O . HOH L 6 . ? -2.979 9.575 19.289 1.00 35.86 ? 2160 HOH A O 1 HETATM 3593 O O . HOH L 6 . ? -3.691 3.481 6.353 1.00 31.53 ? 2161 HOH A O 1 HETATM 3594 O O . HOH L 6 . ? -0.070 -0.772 11.740 1.00 56.68 ? 2162 HOH A O 1 HETATM 3595 O O . HOH L 6 . ? -8.656 7.273 8.139 1.00 27.55 ? 2163 HOH A O 1 HETATM 3596 O O . HOH L 6 . ? -7.101 9.426 8.808 1.00 27.45 ? 2164 HOH A O 1 HETATM 3597 O O . HOH L 6 . ? -0.508 4.710 16.709 1.00 33.70 ? 2165 HOH A O 1 HETATM 3598 O O . HOH L 6 . ? -31.722 11.562 6.773 1.00 15.50 ? 2166 HOH A O 1 HETATM 3599 O O . HOH L 6 . ? -29.538 9.969 6.961 1.00 18.47 ? 2167 HOH A O 1 HETATM 3600 O O . HOH L 6 . ? -25.236 20.719 9.381 1.00 18.36 ? 2168 HOH A O 1 HETATM 3601 O O . HOH L 6 . ? -15.262 22.854 16.679 1.00 19.02 ? 2169 HOH A O 1 HETATM 3602 O O . HOH L 6 . ? -7.301 19.569 17.078 1.00 43.88 ? 2170 HOH A O 1 HETATM 3603 O O . HOH L 6 . ? -7.453 16.505 9.110 1.00 22.51 ? 2171 HOH A O 1 HETATM 3604 O O . HOH L 6 . ? -6.910 22.654 6.837 1.00 43.36 ? 2172 HOH A O 1 HETATM 3605 O O . HOH L 6 . ? -4.812 19.149 8.859 1.00 40.95 ? 2173 HOH A O 1 HETATM 3606 O O . HOH L 6 . ? -7.358 25.132 11.196 1.00 64.89 ? 2174 HOH A O 1 HETATM 3607 O O . HOH L 6 . ? -1.442 13.383 16.105 1.00 64.73 ? 2175 HOH A O 1 HETATM 3608 O O . HOH L 6 . ? 1.354 13.888 8.220 1.00 60.07 ? 2176 HOH A O 1 HETATM 3609 O O . HOH L 6 . ? -1.601 9.419 10.313 1.00 42.36 ? 2177 HOH A O 1 HETATM 3610 O O . HOH L 6 . ? -5.051 9.297 11.905 1.00 44.52 ? 2178 HOH A O 1 HETATM 3611 O O . HOH L 6 . ? -5.218 10.396 15.132 1.00 35.91 ? 2179 HOH A O 1 HETATM 3612 O O . HOH L 6 . ? -4.729 14.412 4.452 1.00 53.95 ? 2180 HOH A O 1 HETATM 3613 O O . HOH L 6 . ? -5.763 10.354 0.450 1.00 44.04 ? 2181 HOH A O 1 HETATM 3614 O O . HOH L 6 . ? -6.887 16.083 4.610 1.00 28.70 ? 2182 HOH A O 1 HETATM 3615 O O . HOH L 6 . ? -11.811 15.821 -0.638 1.00 28.01 ? 2183 HOH A O 1 HETATM 3616 O O . HOH L 6 . ? -9.395 12.743 -2.746 1.00 51.94 ? 2184 HOH A O 1 HETATM 3617 O O . HOH L 6 . ? -8.007 15.095 -2.368 1.00 58.17 ? 2185 HOH A O 1 HETATM 3618 O O . HOH L 6 . ? -8.395 16.847 -0.314 1.00 34.23 ? 2186 HOH A O 1 HETATM 3619 O O . HOH L 6 . ? -29.061 17.919 6.066 1.00 18.38 ? 2187 HOH A O 1 HETATM 3620 O O . HOH L 6 . ? -31.823 22.899 9.805 1.00 39.94 ? 2188 HOH A O 1 HETATM 3621 O O . HOH L 6 . ? -31.259 25.001 8.296 1.00 49.10 ? 2189 HOH A O 1 HETATM 3622 O O . HOH L 6 . ? -29.278 31.360 11.089 1.00 37.94 ? 2190 HOH A O 1 HETATM 3623 O O . HOH L 6 . ? -30.422 29.964 14.149 1.00 37.44 ? 2191 HOH A O 1 HETATM 3624 O O . HOH L 6 . ? -29.737 32.512 13.513 1.00 50.06 ? 2192 HOH A O 1 HETATM 3625 O O . HOH L 6 . ? -32.692 33.921 7.774 1.00 41.89 ? 2193 HOH A O 1 HETATM 3626 O O . HOH L 6 . ? -36.487 34.942 11.151 1.00 25.83 ? 2194 HOH A O 1 HETATM 3627 O O . HOH L 6 . ? -34.820 32.027 7.701 1.00 24.27 ? 2195 HOH A O 1 HETATM 3628 O O . HOH L 6 . ? -32.782 32.664 4.294 1.00 54.79 ? 2196 HOH A O 1 HETATM 3629 O O . HOH L 6 . ? -35.070 24.101 14.695 1.00 35.72 ? 2197 HOH A O 1 HETATM 3630 O O . HOH L 6 . ? -38.162 21.018 9.901 1.00 14.70 ? 2198 HOH A O 1 HETATM 3631 O O . HOH L 6 . ? -34.289 22.250 8.091 1.00 28.36 ? 2199 HOH A O 1 HETATM 3632 O O . HOH L 6 . ? -41.458 26.269 13.059 1.00 44.35 ? 2200 HOH A O 1 HETATM 3633 O O . HOH L 6 . ? -39.350 23.185 15.175 1.00 70.25 ? 2201 HOH A O 1 HETATM 3634 O O . HOH L 6 . ? -39.862 34.732 4.516 1.00 40.52 ? 2202 HOH A O 1 HETATM 3635 O O . HOH L 6 . ? -52.958 24.130 3.252 1.00 31.95 ? 2203 HOH A O 1 HETATM 3636 O O . HOH L 6 . ? -48.789 23.266 -1.932 1.00 35.06 ? 2204 HOH A O 1 HETATM 3637 O O . HOH L 6 . ? -50.101 31.307 -0.913 1.00 42.37 ? 2205 HOH A O 1 HETATM 3638 O O . HOH L 6 . ? -48.889 33.592 0.459 1.00 40.26 ? 2206 HOH A O 1 HETATM 3639 O O . HOH L 6 . ? -45.301 31.567 0.039 0.50 59.60 ? 2207 HOH A O 1 HETATM 3640 O O . HOH L 6 . ? -49.301 16.576 2.616 1.00 27.40 ? 2208 HOH A O 1 HETATM 3641 O O . HOH L 6 . ? -42.007 17.710 0.077 1.00 28.50 ? 2209 HOH A O 1 HETATM 3642 O O . HOH L 6 . ? -55.602 22.036 9.674 1.00 19.16 ? 2210 HOH A O 1 HETATM 3643 O O . HOH L 6 . ? -55.572 24.995 10.244 1.00 23.50 ? 2211 HOH A O 1 HETATM 3644 O O . HOH L 6 . ? -56.932 27.318 9.467 1.00 33.00 ? 2212 HOH A O 1 HETATM 3645 O O . HOH L 6 . ? -54.714 32.115 3.081 1.00 50.58 ? 2213 HOH A O 1 HETATM 3646 O O . HOH L 6 . ? -57.532 34.533 9.409 1.00 38.04 ? 2214 HOH A O 1 HETATM 3647 O O . HOH L 6 . ? -63.088 36.117 4.989 1.00 38.32 ? 2215 HOH A O 1 HETATM 3648 O O . HOH L 6 . ? -60.587 31.524 3.805 1.00 42.04 ? 2216 HOH A O 1 HETATM 3649 O O . HOH L 6 . ? -63.117 31.991 10.229 1.00 56.64 ? 2217 HOH A O 1 HETATM 3650 O O . HOH L 6 . ? -55.901 37.017 8.945 1.00 43.27 ? 2218 HOH A O 1 HETATM 3651 O O . HOH L 6 . ? -55.880 36.669 13.113 1.00 38.70 ? 2219 HOH A O 1 HETATM 3652 O O . HOH L 6 . ? -50.065 43.293 13.277 1.00 28.78 ? 2220 HOH A O 1 HETATM 3653 O O . HOH L 6 . ? -55.937 39.073 11.634 1.00 34.97 ? 2221 HOH A O 1 HETATM 3654 O O . HOH L 6 . ? -37.011 36.173 8.781 1.00 39.99 ? 2222 HOH A O 1 HETATM 3655 O O . HOH L 6 . ? -39.037 33.183 6.549 1.00 30.29 ? 2223 HOH A O 1 HETATM 3656 O O . HOH L 6 . ? -39.633 40.314 13.573 1.00 36.09 ? 2224 HOH A O 1 HETATM 3657 O O . HOH L 6 . ? -41.707 33.451 16.962 1.00 34.12 ? 2225 HOH A O 1 HETATM 3658 O O . HOH L 6 . ? -38.685 33.210 20.414 1.00 58.32 ? 2226 HOH A O 1 HETATM 3659 O O . HOH L 6 . ? -30.331 34.078 16.118 1.00 40.46 ? 2227 HOH A O 1 HETATM 3660 O O . HOH L 6 . ? -35.879 36.344 21.482 1.00 50.09 ? 2228 HOH A O 1 HETATM 3661 O O . HOH L 6 . ? -40.683 40.747 17.237 1.00 44.39 ? 2229 HOH A O 1 HETATM 3662 O O . HOH L 6 . ? -45.230 42.311 21.105 1.00 50.27 ? 2230 HOH A O 1 HETATM 3663 O O . HOH L 6 . ? -44.705 38.082 22.147 1.00 28.43 ? 2231 HOH A O 1 HETATM 3664 O O . HOH L 6 . ? -46.783 43.839 15.313 1.00 47.17 ? 2232 HOH A O 1 HETATM 3665 O O . HOH L 6 . ? -49.141 35.683 21.694 1.00 37.40 ? 2233 HOH A O 1 HETATM 3666 O O . HOH L 6 . ? -57.125 33.914 13.874 1.00 55.91 ? 2234 HOH A O 1 HETATM 3667 O O . HOH L 6 . ? -54.482 34.544 22.322 1.00 41.33 ? 2235 HOH A O 1 HETATM 3668 O O . HOH L 6 . ? -54.164 30.704 16.159 1.00 38.37 ? 2236 HOH A O 1 HETATM 3669 O O . HOH L 6 . ? -44.671 27.885 19.557 1.00 40.72 ? 2237 HOH A O 1 HETATM 3670 O O . HOH L 6 . ? -52.617 25.704 20.065 1.00 41.66 ? 2238 HOH A O 1 HETATM 3671 O O . HOH L 6 . ? -42.974 21.209 16.316 1.00 50.33 ? 2239 HOH A O 1 HETATM 3672 O O . HOH L 6 . ? -55.117 19.282 14.090 1.00 47.28 ? 2240 HOH A O 1 HETATM 3673 O O . HOH L 6 . ? -48.780 15.982 14.803 1.00 35.82 ? 2241 HOH A O 1 HETATM 3674 O O . HOH L 6 . ? -47.992 13.045 17.159 1.00 45.42 ? 2242 HOH A O 1 HETATM 3675 O O . HOH L 6 . ? -42.319 16.282 19.044 1.00 66.23 ? 2243 HOH A O 1 HETATM 3676 O O . HOH L 6 . ? -45.460 15.386 24.235 1.00 66.59 ? 2244 HOH A O 1 HETATM 3677 O O . HOH L 6 . ? -44.193 12.539 15.311 1.00 31.20 ? 2245 HOH A O 1 HETATM 3678 O O . HOH L 6 . ? -48.260 11.139 9.403 1.00 22.68 ? 2246 HOH A O 1 HETATM 3679 O O . HOH L 6 . ? -41.281 7.009 11.786 1.00 45.72 ? 2247 HOH A O 1 HETATM 3680 O O . HOH L 6 . ? -37.963 8.461 8.382 1.00 27.17 ? 2248 HOH A O 1 HETATM 3681 O O . HOH L 6 . ? -37.444 16.215 16.852 1.00 53.29 ? 2249 HOH A O 1 HETATM 3682 O O . HOH L 6 . ? -43.738 8.083 3.252 1.00 34.86 ? 2250 HOH A O 1 HETATM 3683 O O . HOH L 6 . ? -40.897 7.120 2.842 1.00 26.98 ? 2251 HOH A O 1 HETATM 3684 O O . HOH L 6 . ? -40.085 6.565 7.814 1.00 54.32 ? 2252 HOH A O 1 HETATM 3685 O O . HOH L 6 . ? -48.882 7.835 2.472 1.00 31.50 ? 2253 HOH A O 1 HETATM 3686 O O . HOH L 6 . ? -49.477 6.168 5.910 1.00 37.32 ? 2254 HOH A O 1 HETATM 3687 O O . HOH L 6 . ? -44.321 4.396 10.988 1.00 33.35 ? 2255 HOH A O 1 HETATM 3688 O O . HOH L 6 . ? -48.118 7.257 18.937 1.00 43.68 ? 2256 HOH A O 1 HETATM 3689 O O . HOH L 6 . ? -55.893 12.396 23.517 1.00 49.08 ? 2257 HOH A O 1 HETATM 3690 O O . HOH L 6 . ? -57.372 12.355 17.877 1.00 53.88 ? 2258 HOH A O 1 HETATM 3691 O O . HOH L 6 . ? -18.935 28.106 30.682 1.00 45.63 ? 2259 HOH A O 1 HETATM 3692 O O . HOH L 6 . ? -15.873 27.111 29.447 1.00 53.83 ? 2260 HOH A O 1 HETATM 3693 O O . HOH L 6 . ? -13.953 19.761 31.982 1.00 50.64 ? 2261 HOH A O 1 HETATM 3694 O O . HOH L 6 . ? -12.575 24.410 37.971 1.00 69.71 ? 2262 HOH A O 1 HETATM 3695 O O . HOH L 6 . ? -9.440 25.766 31.509 1.00 43.17 ? 2263 HOH A O 1 HETATM 3696 O O . HOH L 6 . ? -44.004 -0.191 13.971 1.00 47.21 ? 2264 HOH A O 1 HETATM 3697 O O . HOH L 6 . ? -39.351 -3.314 13.408 1.00 50.02 ? 2265 HOH A O 1 HETATM 3698 O O . HOH L 6 . ? -50.002 -3.432 18.402 1.00 50.15 ? 2266 HOH A O 1 HETATM 3699 O O . HOH L 6 . ? -45.005 -13.125 18.477 1.00 57.06 ? 2267 HOH A O 1 HETATM 3700 O O . HOH L 6 . ? -45.487 -12.422 12.630 1.00 61.25 ? 2268 HOH A O 1 HETATM 3701 O O . HOH L 6 . ? -46.003 -13.404 15.854 1.00 68.16 ? 2269 HOH A O 1 HETATM 3702 O O . HOH M 6 . ? -42.448 5.651 26.145 1.00 67.64 ? 2001 HOH B O 1 HETATM 3703 O O . HOH M 6 . ? -38.000 5.580 14.153 1.00 47.46 ? 2002 HOH B O 1 HETATM 3704 O O . HOH M 6 . ? -30.778 -5.002 31.539 1.00 48.01 ? 2003 HOH B O 1 HETATM 3705 O O . HOH M 6 . ? -33.927 -15.259 21.444 1.00 51.24 ? 2004 HOH B O 1 HETATM 3706 O O . HOH M 6 . ? -25.061 -12.651 31.367 1.00 47.36 ? 2005 HOH B O 1 HETATM 3707 O O . HOH M 6 . ? -17.228 -1.675 33.512 1.00 47.69 ? 2006 HOH B O 1 HETATM 3708 O O . HOH M 6 . ? -15.519 -6.075 31.409 1.00 56.42 ? 2007 HOH B O 1 HETATM 3709 O O . HOH M 6 . ? -34.247 7.737 32.910 1.00 46.46 ? 2008 HOH B O 1 HETATM 3710 O O . HOH M 6 . ? -25.723 33.414 10.239 1.00 47.11 ? 2009 HOH B O 1 HETATM 3711 O O . HOH M 6 . ? -14.492 25.839 21.331 1.00 51.81 ? 2010 HOH B O 1 HETATM 3712 O O . HOH M 6 . ? -21.365 30.874 19.478 1.00 66.49 ? 2011 HOH B O 1 HETATM 3713 O O . HOH M 6 . ? -27.572 34.023 6.810 1.00 47.42 ? 2012 HOH B O 1 HETATM 3714 O O . HOH M 6 . ? -20.794 34.228 3.505 1.00 56.70 ? 2013 HOH B O 1 HETATM 3715 O O . HOH M 6 . ? -17.592 33.240 10.169 1.00 49.59 ? 2014 HOH B O 1 HETATM 3716 O O . HOH M 6 . ? -7.969 29.958 -2.140 1.00 46.32 ? 2015 HOH B O 1 HETATM 3717 O O . HOH M 6 . ? -26.951 38.597 1.187 1.00 58.52 ? 2016 HOH B O 1 HETATM 3718 O O . HOH M 6 . ? -29.583 28.786 -11.884 1.00 47.30 ? 2017 HOH B O 1 HETATM 3719 O O . HOH M 6 . ? -30.777 17.419 -16.201 1.00 41.12 ? 2018 HOH B O 1 HETATM 3720 O O . HOH M 6 . ? -27.311 1.208 -11.918 1.00 51.74 ? 2019 HOH B O 1 HETATM 3721 O O . HOH M 6 . ? -35.183 -1.984 -6.454 1.00 45.10 ? 2020 HOH B O 1 HETATM 3722 O O . HOH M 6 . ? -35.435 -4.642 -8.666 1.00 54.50 ? 2021 HOH B O 1 HETATM 3723 O O . HOH M 6 . ? -32.385 2.438 -17.288 1.00 51.28 ? 2022 HOH B O 1 HETATM 3724 O O . HOH M 6 . ? -38.684 -0.446 6.405 1.00 57.38 ? 2023 HOH B O 1 HETATM 3725 O O . HOH M 6 . ? -41.959 4.591 -0.305 1.00 49.77 ? 2024 HOH B O 1 HETATM 3726 O O . HOH M 6 . ? -45.055 4.638 4.733 1.00 49.24 ? 2025 HOH B O 1 HETATM 3727 O O . HOH M 6 . ? -40.043 1.955 5.878 1.00 67.51 ? 2026 HOH B O 1 HETATM 3728 O O . HOH M 6 . ? -40.268 0.842 2.674 1.00 53.06 ? 2027 HOH B O 1 HETATM 3729 O O . HOH M 6 . ? -23.497 3.348 -7.280 1.00 46.52 ? 2028 HOH B O 1 HETATM 3730 O O . HOH M 6 . ? -17.635 5.478 -9.274 1.00 57.14 ? 2029 HOH B O 1 HETATM 3731 O O . HOH M 6 . ? -40.899 8.231 27.639 1.00 56.63 ? 2030 HOH B O 1 HETATM 3732 O O . HOH M 6 . ? -35.239 0.202 25.698 1.00 41.40 ? 2031 HOH B O 1 HETATM 3733 O O . HOH M 6 . ? -35.311 1.839 22.915 1.00 32.63 ? 2032 HOH B O 1 HETATM 3734 O O . HOH M 6 . ? -42.551 4.890 12.990 1.00 51.20 ? 2033 HOH B O 1 HETATM 3735 O O . HOH M 6 . ? -44.153 2.334 19.826 1.00 55.04 ? 2034 HOH B O 1 HETATM 3736 O O . HOH M 6 . ? -40.439 3.449 13.932 1.00 48.79 ? 2035 HOH B O 1 HETATM 3737 O O . HOH M 6 . ? -39.137 -1.592 16.040 1.00 32.14 ? 2036 HOH B O 1 HETATM 3738 O O . HOH M 6 . ? -38.741 -0.681 23.122 1.00 60.48 ? 2037 HOH B O 1 HETATM 3739 O O . HOH M 6 . ? -36.149 -1.125 15.745 1.00 28.53 ? 2038 HOH B O 1 HETATM 3740 O O . HOH M 6 . ? -34.184 -8.446 25.041 1.00 29.43 ? 2039 HOH B O 1 HETATM 3741 O O . HOH M 6 . ? -33.521 -8.968 28.885 1.00 47.21 ? 2040 HOH B O 1 HETATM 3742 O O . HOH M 6 . ? -29.595 -8.260 29.168 1.00 31.55 ? 2041 HOH B O 1 HETATM 3743 O O . HOH M 6 . ? -29.505 -5.312 28.855 1.00 37.31 ? 2042 HOH B O 1 HETATM 3744 O O . HOH M 6 . ? -34.810 -12.098 22.922 1.00 49.36 ? 2043 HOH B O 1 HETATM 3745 O O . HOH M 6 . ? -29.042 -16.144 21.681 1.00 53.42 ? 2044 HOH B O 1 HETATM 3746 O O . HOH M 6 . ? -24.493 -10.133 28.827 1.00 35.49 ? 2045 HOH B O 1 HETATM 3747 O O . HOH M 6 . ? -23.086 -14.757 22.373 1.00 30.05 ? 2046 HOH B O 1 HETATM 3748 O O . HOH M 6 . ? -23.347 -7.585 29.097 1.00 23.18 ? 2047 HOH B O 1 HETATM 3749 O O . HOH M 6 . ? -19.422 -9.015 28.514 1.00 44.01 ? 2048 HOH B O 1 HETATM 3750 O O . HOH M 6 . ? -18.071 -9.955 26.428 1.00 59.54 ? 2049 HOH B O 1 HETATM 3751 O O . HOH M 6 . ? -15.290 -4.161 25.487 1.00 30.47 ? 2050 HOH B O 1 HETATM 3752 O O . HOH M 6 . ? -13.957 -8.327 25.550 1.00 34.12 ? 2051 HOH B O 1 HETATM 3753 O O . HOH M 6 . ? -18.908 -5.794 34.228 1.00 46.01 ? 2052 HOH B O 1 HETATM 3754 O O . HOH M 6 . ? -18.392 -8.345 31.937 1.00 39.06 ? 2053 HOH B O 1 HETATM 3755 O O . HOH M 6 . ? -25.139 -3.497 37.355 1.00 61.44 ? 2054 HOH B O 1 HETATM 3756 O O . HOH M 6 . ? -19.254 0.038 34.172 1.00 48.70 ? 2055 HOH B O 1 HETATM 3757 O O . HOH M 6 . ? -27.854 -4.367 33.179 1.00 38.31 ? 2056 HOH B O 1 HETATM 3758 O O . HOH M 6 . ? -29.893 5.238 27.631 1.00 33.86 ? 2057 HOH B O 1 HETATM 3759 O O . HOH M 6 . ? -34.213 6.954 28.207 1.00 30.80 ? 2058 HOH B O 1 HETATM 3760 O O . HOH M 6 . ? -32.597 8.050 30.536 1.00 43.40 ? 2059 HOH B O 1 HETATM 3761 O O . HOH M 6 . ? -32.599 20.945 32.354 1.00 41.74 ? 2060 HOH B O 1 HETATM 3762 O O . HOH M 6 . ? -27.528 20.550 32.276 1.00 46.79 ? 2061 HOH B O 1 HETATM 3763 O O . HOH M 6 . ? -29.533 22.785 30.103 1.00 62.66 ? 2062 HOH B O 1 HETATM 3764 O O . HOH M 6 . ? -29.733 24.097 25.827 1.00 42.29 ? 2063 HOH B O 1 HETATM 3765 O O . HOH M 6 . ? -22.085 30.031 31.017 1.00 44.07 ? 2064 HOH B O 1 HETATM 3766 O O . HOH M 6 . ? -20.448 28.866 21.074 1.00 56.80 ? 2065 HOH B O 1 HETATM 3767 O O . HOH M 6 . ? -16.652 22.767 19.353 1.00 37.70 ? 2066 HOH B O 1 HETATM 3768 O O . HOH M 6 . ? -24.079 30.133 16.777 1.00 22.53 ? 2067 HOH B O 1 HETATM 3769 O O . HOH M 6 . ? -28.191 30.466 22.622 1.00 53.19 ? 2068 HOH B O 1 HETATM 3770 O O . HOH M 6 . ? -21.237 28.734 14.971 1.00 40.29 ? 2069 HOH B O 1 HETATM 3771 O O . HOH M 6 . ? -22.324 30.155 12.655 1.00 36.64 ? 2070 HOH B O 1 HETATM 3772 O O . HOH M 6 . ? -27.201 30.976 9.394 1.00 40.22 ? 2071 HOH B O 1 HETATM 3773 O O . HOH M 6 . ? -22.889 32.929 4.765 1.00 34.61 ? 2072 HOH B O 1 HETATM 3774 O O . HOH M 6 . ? -21.258 33.096 10.680 1.00 45.88 ? 2073 HOH B O 1 HETATM 3775 O O . HOH M 6 . ? -15.726 31.094 9.657 1.00 38.00 ? 2074 HOH B O 1 HETATM 3776 O O . HOH M 6 . ? -16.844 24.888 15.971 1.00 37.55 ? 2075 HOH B O 1 HETATM 3777 O O . HOH M 6 . ? -14.972 30.022 3.327 1.00 31.87 ? 2076 HOH B O 1 HETATM 3778 O O . HOH M 6 . ? -13.846 30.892 7.698 1.00 47.69 ? 2077 HOH B O 1 HETATM 3779 O O . HOH M 6 . ? -13.323 22.425 1.700 1.00 28.06 ? 2078 HOH B O 1 HETATM 3780 O O . HOH M 6 . ? -15.085 29.112 0.814 1.00 32.10 ? 2079 HOH B O 1 HETATM 3781 O O . HOH M 6 . ? -11.967 29.679 -0.266 1.00 57.19 ? 2080 HOH B O 1 HETATM 3782 O O . HOH M 6 . ? -7.520 28.495 0.107 1.00 52.48 ? 2081 HOH B O 1 HETATM 3783 O O . HOH M 6 . ? -8.078 27.892 5.608 1.00 45.73 ? 2082 HOH B O 1 HETATM 3784 O O . HOH M 6 . ? -14.155 28.035 -4.375 1.00 37.15 ? 2083 HOH B O 1 HETATM 3785 O O . HOH M 6 . ? -11.035 25.955 -5.526 1.00 60.35 ? 2084 HOH B O 1 HETATM 3786 O O . HOH M 6 . ? -16.412 26.394 -1.862 1.00 18.79 ? 2085 HOH B O 1 HETATM 3787 O O . HOH M 6 . ? -7.022 17.818 6.640 1.00 33.33 ? 2086 HOH B O 1 HETATM 3788 O O . HOH M 6 . ? -16.398 20.875 -6.037 1.00 32.35 ? 2087 HOH B O 1 HETATM 3789 O O . HOH M 6 . ? -20.605 16.933 -2.198 1.00 30.78 ? 2088 HOH B O 1 HETATM 3790 O O . HOH M 6 . ? -38.229 17.520 4.333 1.00 14.59 ? 2089 HOH B O 1 HETATM 3791 O O . HOH M 6 . ? -37.419 16.924 -3.953 1.00 19.20 ? 2090 HOH B O 1 HETATM 3792 O O . HOH M 6 . ? -35.373 19.817 15.205 1.00 56.58 ? 2091 HOH B O 1 HETATM 3793 O O . HOH M 6 . ? -31.901 26.508 -4.326 1.00 22.04 ? 2092 HOH B O 1 HETATM 3794 O O . HOH M 6 . ? -30.804 31.310 1.217 1.00 38.55 ? 2093 HOH B O 1 HETATM 3795 O O . HOH M 6 . ? -23.473 28.174 -1.426 1.00 20.48 ? 2094 HOH B O 1 HETATM 3796 O O . HOH M 6 . ? -25.787 31.193 -3.209 1.00 28.38 ? 2095 HOH B O 1 HETATM 3797 O O . HOH M 6 . ? -27.264 33.364 -2.485 1.00 53.63 ? 2096 HOH B O 1 HETATM 3798 O O . HOH M 6 . ? -28.188 29.836 -4.933 1.00 33.84 ? 2097 HOH B O 1 HETATM 3799 O O . HOH M 6 . ? -25.563 34.962 2.196 1.00 45.68 ? 2098 HOH B O 1 HETATM 3800 O O . HOH M 6 . ? -25.156 34.753 -4.740 1.00 31.13 ? 2099 HOH B O 1 HETATM 3801 O O . HOH M 6 . ? -23.286 31.855 -4.471 1.00 24.23 ? 2100 HOH B O 1 HETATM 3802 O O . HOH M 6 . ? -20.972 38.009 -3.056 1.00 34.46 ? 2101 HOH B O 1 HETATM 3803 O O . HOH M 6 . ? -16.415 29.233 -2.893 1.00 40.21 ? 2102 HOH B O 1 HETATM 3804 O O . HOH M 6 . ? -16.716 31.884 1.715 1.00 31.13 ? 2103 HOH B O 1 HETATM 3805 O O . HOH M 6 . ? -12.550 32.003 -2.506 1.00 50.16 ? 2104 HOH B O 1 HETATM 3806 O O . HOH M 6 . ? -12.481 33.344 -7.914 1.00 46.39 ? 2105 HOH B O 1 HETATM 3807 O O . HOH M 6 . ? -19.517 23.379 -8.756 1.00 33.20 ? 2106 HOH B O 1 HETATM 3808 O O . HOH M 6 . ? -14.516 28.011 -7.046 1.00 54.26 ? 2107 HOH B O 1 HETATM 3809 O O . HOH M 6 . ? -23.323 32.341 -7.360 1.00 19.23 ? 2108 HOH B O 1 HETATM 3810 O O . HOH M 6 . ? -25.067 24.995 -14.535 1.00 41.59 ? 2109 HOH B O 1 HETATM 3811 O O . HOH M 6 . ? -26.825 21.427 -9.186 1.00 21.84 ? 2110 HOH B O 1 HETATM 3812 O O . HOH M 6 . ? -30.694 26.746 -10.467 1.00 34.50 ? 2111 HOH B O 1 HETATM 3813 O O . HOH M 6 . ? -34.273 20.685 -12.037 1.00 32.23 ? 2112 HOH B O 1 HETATM 3814 O O . HOH M 6 . ? -29.639 15.272 -14.280 1.00 42.97 ? 2113 HOH B O 1 HETATM 3815 O O . HOH M 6 . ? -28.427 4.249 -10.279 1.00 37.23 ? 2114 HOH B O 1 HETATM 3816 O O . HOH M 6 . ? -30.933 -1.577 -9.560 1.00 55.95 ? 2115 HOH B O 1 HETATM 3817 O O . HOH M 6 . ? -29.163 0.871 -9.512 1.00 50.75 ? 2116 HOH B O 1 HETATM 3818 O O . HOH M 6 . ? -29.889 -3.683 -18.846 1.00 52.32 ? 2117 HOH B O 1 HETATM 3819 O O . HOH M 6 . ? -37.265 7.187 -5.360 1.00 41.44 ? 2118 HOH B O 1 HETATM 3820 O O . HOH M 6 . ? -34.525 3.704 -2.909 1.00 11.82 ? 2119 HOH B O 1 HETATM 3821 O O . HOH M 6 . ? -31.036 -1.962 -12.473 1.00 58.23 ? 2120 HOH B O 1 HETATM 3822 O O . HOH M 6 . ? -33.231 -2.336 -8.288 1.00 51.41 ? 2121 HOH B O 1 HETATM 3823 O O . HOH M 6 . ? -37.183 0.702 -18.190 1.00 56.64 ? 2122 HOH B O 1 HETATM 3824 O O . HOH M 6 . ? -39.139 1.887 -7.975 1.00 52.17 ? 2123 HOH B O 1 HETATM 3825 O O . HOH M 6 . ? -35.446 4.107 -18.218 1.00 44.55 ? 2124 HOH B O 1 HETATM 3826 O O . HOH M 6 . ? -28.120 5.611 -12.625 1.00 63.06 ? 2125 HOH B O 1 HETATM 3827 O O . HOH M 6 . ? -39.062 9.601 -11.759 1.00 17.76 ? 2126 HOH B O 1 HETATM 3828 O O . HOH M 6 . ? -39.650 9.252 -9.187 1.00 35.89 ? 2127 HOH B O 1 HETATM 3829 O O . HOH M 6 . ? -36.019 9.042 -3.813 1.00 19.74 ? 2128 HOH B O 1 HETATM 3830 O O . HOH M 6 . ? -31.467 27.222 -7.266 1.00 7.58 ? 2129 HOH B O 1 HETATM 3831 O O . HOH M 6 . ? -24.966 19.625 -10.033 1.00 24.12 ? 2130 HOH B O 1 HETATM 3832 O O . HOH M 6 . ? -23.447 16.828 -8.820 1.00 29.18 ? 2131 HOH B O 1 HETATM 3833 O O . HOH M 6 . ? -21.230 18.149 -11.674 1.00 49.61 ? 2132 HOH B O 1 HETATM 3834 O O . HOH M 6 . ? -18.828 17.068 -9.098 1.00 55.73 ? 2133 HOH B O 1 HETATM 3835 O O . HOH M 6 . ? -39.955 9.300 -4.685 1.00 30.16 ? 2134 HOH B O 1 HETATM 3836 O O . HOH M 6 . ? -43.892 9.353 0.381 1.00 42.68 ? 2135 HOH B O 1 HETATM 3837 O O . HOH M 6 . ? -37.016 9.252 12.153 1.00 49.12 ? 2136 HOH B O 1 HETATM 3838 O O . HOH M 6 . ? -35.154 -0.357 4.907 1.00 48.88 ? 2137 HOH B O 1 HETATM 3839 O O . HOH M 6 . ? -40.278 4.646 1.831 1.00 43.30 ? 2138 HOH B O 1 HETATM 3840 O O . HOH M 6 . ? -41.476 3.927 4.693 1.00 64.79 ? 2139 HOH B O 1 HETATM 3841 O O . HOH M 6 . ? -39.852 3.053 -2.313 1.00 48.16 ? 2140 HOH B O 1 HETATM 3842 O O . HOH M 6 . ? -25.866 1.984 -7.395 1.00 66.96 ? 2141 HOH B O 1 HETATM 3843 O O . HOH M 6 . ? -20.210 5.952 -7.645 1.00 37.18 ? 2142 HOH B O 1 HETATM 3844 O O . HOH M 6 . ? -19.078 2.200 -5.429 1.00 52.27 ? 2143 HOH B O 1 HETATM 3845 O O . HOH M 6 . ? -27.273 8.413 -13.404 1.00 58.11 ? 2144 HOH B O 1 HETATM 3846 O O . HOH M 6 . ? -18.215 14.363 -2.518 1.00 54.51 ? 2145 HOH B O 1 HETATM 3847 O O . HOH M 6 . ? -13.155 7.996 -1.093 1.00 50.25 ? 2146 HOH B O 1 HETATM 3848 O O . HOH M 6 . ? -12.682 10.619 -2.937 1.00 47.65 ? 2147 HOH B O 1 HETATM 3849 O O . HOH M 6 . ? -16.517 2.896 -4.093 1.00 27.68 ? 2148 HOH B O 1 HETATM 3850 O O . HOH M 6 . ? -13.964 5.342 -2.518 1.00 41.97 ? 2149 HOH B O 1 HETATM 3851 O O . HOH M 6 . ? -19.659 15.850 -6.820 1.00 52.14 ? 2150 HOH B O 1 HETATM 3852 O O . HOH M 6 . ? -38.028 -7.890 -2.367 1.00 44.11 ? 2151 HOH B O 1 HETATM 3853 O O . HOH M 6 . ? -20.682 33.562 19.245 1.00 49.92 ? 2152 HOH B O 1 HETATM 3854 O O . HOH M 6 . ? -30.459 -8.784 -18.904 1.00 50.16 ? 2153 HOH B 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 SER 1 -1 ? ? ? A . n A 1 2 ARG 2 0 0 ARG ARG A . n A 1 3 ALA 3 1 1 ALA ALA A . n A 1 4 PRO 4 2 2 PRO PRO A . n A 1 5 ASP 5 3 3 ASP ASP A . n A 1 6 GLN 6 4 4 GLN GLN A . n A 1 7 ASP 7 5 5 ASP ASP A . n A 1 8 GLU 8 6 6 GLU GLU A . n A 1 9 ILE 9 7 7 ILE ILE A . n A 1 10 GLN 10 8 8 GLN GLN A . n A 1 11 ARG 11 9 9 ARG ARG A . n A 1 12 LEU 12 10 10 LEU LEU A . n A 1 13 PRO 13 11 11 PRO PRO A . n A 1 14 GLY 14 12 12 GLY GLY A . n A 1 15 LEU 15 13 13 LEU LEU A . n A 1 16 ALA 16 14 14 ALA ALA A . n A 1 17 LYS 17 15 15 LYS LYS A . n A 1 18 GLN 18 16 16 GLN GLN A . n A 1 19 PRO 19 17 17 PRO PRO A . n A 1 20 SER 20 18 18 SER SER A . n A 1 21 PHE 21 19 19 PHE PHE A . n A 1 22 ARG 22 20 20 ARG ARG A . n A 1 23 GLN 23 21 21 GLN GLN A . n A 1 24 TYR 24 22 22 TYR TYR A . n A 1 25 SER 25 23 23 SER SER A . n A 1 26 GLY 26 24 24 GLY GLY A . n A 1 27 TYR 27 25 25 TYR TYR A . n A 1 28 LEU 28 26 26 LEU LEU A . n A 1 29 LYS 29 27 27 LYS LYS A . n A 1 30 GLY 30 28 28 GLY GLY A . n A 1 31 SER 31 29 29 SER SER A . n A 1 32 GLY 32 30 30 GLY GLY A . n A 1 33 SER 33 31 31 SER SER A . n A 1 34 LYS 34 32 32 LYS LYS A . n A 1 35 HIS 35 33 33 HIS HIS A . n A 1 36 LEU 36 34 34 LEU LEU A . n A 1 37 HIS 37 35 35 HIS HIS A . n A 1 38 TYR 38 36 36 TYR TYR A . n A 1 39 TRP 39 37 37 TRP TRP A . n A 1 40 PHE 40 38 38 PHE PHE A . n A 1 41 VAL 41 39 39 VAL VAL A . n A 1 42 GLU 42 40 40 GLU GLU A . n A 1 43 SER 43 41 41 SER SER A . n A 1 44 GLN 44 42 42 GLN GLN A . n A 1 45 LYS 45 43 43 LYS LYS A . n A 1 46 ASP 46 44 44 ASP ASP A . n A 1 47 PRO 47 45 45 PRO PRO A . n A 1 48 GLU 48 46 46 GLU GLU A . n A 1 49 ASN 49 47 47 ASN ASN A . n A 1 50 SER 50 48 48 SER SER A . n A 1 51 PRO 51 49 49 PRO PRO A . n A 1 52 VAL 52 50 50 VAL VAL A . n A 1 53 VAL 53 51 51 VAL VAL A . n A 1 54 LEU 54 52 52 LEU LEU A . n A 1 55 TRP 55 53 53 TRP TRP A . n A 1 56 LEU 56 54 54 LEU LEU A . n A 1 57 ASN 57 55 55 ASN ASN A . n A 1 58 GLY 58 56 56 GLY GLY A . n A 1 59 GLY 59 57 57 GLY GLY A . n A 1 60 PRO 60 58 58 PRO PRO A . n A 1 61 GLY 61 59 59 GLY GLY A . n A 1 62 CYS 62 60 60 CYS CYS A . n A 1 63 SER 63 61 61 SER SER A . n A 1 64 SER 64 62 62 SER SER A . n A 1 65 LEU 65 63 63 LEU LEU A . n A 1 66 ASP 66 64 64 ASP ASP A . n A 1 67 GLY 67 65 65 GLY GLY A . n A 1 68 LEU 68 66 66 LEU LEU A . n A 1 69 LEU 69 67 67 LEU LEU A . n A 1 70 THR 70 68 68 THR THR A . n A 1 71 GLU 71 69 69 GLU GLU A . n A 1 72 HIS 72 70 70 HIS HIS A . n A 1 73 GLY 73 71 71 GLY GLY A . n A 1 74 PRO 74 72 72 PRO PRO A . n A 1 75 PHE 75 73 73 PHE PHE A . n A 1 76 LEU 76 74 74 LEU LEU A . n A 1 77 VAL 77 75 75 VAL VAL A . n A 1 78 GLN 78 76 76 GLN GLN A . n A 1 79 PRO 79 77 77 PRO PRO A . n A 1 80 ASP 80 78 78 ASP ASP A . n A 1 81 GLY 81 79 79 GLY GLY A . n A 1 82 VAL 82 80 80 VAL VAL A . n A 1 83 THR 83 81 81 THR THR A . n A 1 84 LEU 84 82 82 LEU LEU A . n A 1 85 GLU 85 83 83 GLU GLU A . n A 1 86 TYR 86 84 84 TYR TYR A . n A 1 87 ASN 87 85 85 ASN ASN A . n A 1 88 PRO 88 86 86 PRO PRO A . n A 1 89 TYR 89 87 87 TYR TYR A . n A 1 90 SER 90 88 88 SER SER A . n A 1 91 TRP 91 89 89 TRP TRP A . n A 1 92 ASN 92 90 90 ASN ASN A . n A 1 93 LEU 93 91 91 LEU LEU A . n A 1 94 ILE 94 92 92 ILE ILE A . n A 1 95 ALA 95 93 93 ALA ALA A . n A 1 96 ASN 96 94 94 ASN ASN A . n A 1 97 VAL 97 95 95 VAL VAL A . n A 1 98 LEU 98 96 96 LEU LEU A . n A 1 99 TYR 99 97 97 TYR TYR A . n A 1 100 LEU 100 98 98 LEU LEU A . n A 1 101 GLU 101 99 99 GLU GLU A . n A 1 102 SER 102 100 100 SER SER A . n A 1 103 PRO 103 101 101 PRO PRO A . n A 1 104 ALA 104 102 102 ALA ALA A . n A 1 105 GLY 105 103 103 GLY GLY A . n A 1 106 VAL 106 104 104 VAL VAL A . n A 1 107 GLY 107 105 105 GLY GLY A . n A 1 108 PHE 108 106 106 PHE PHE A . n A 1 109 SER 109 107 107 SER SER A . n A 1 110 TYR 110 108 108 TYR TYR A . n A 1 111 SER 111 109 109 SER SER A . n A 1 112 ASP 112 110 110 ASP ASP A . n A 1 113 ASP 113 111 111 ASP ASP A . n A 1 114 LYS 114 112 112 LYS LYS A . n A 1 115 PHE 115 113 113 PHE PHE A . n A 1 116 TYR 116 114 114 TYR TYR A . n A 1 117 ALA 117 115 115 ALA ALA A . n A 1 118 THR 118 116 116 THR THR A . n A 1 119 ASN 119 117 117 ASN ASN A . n A 1 120 ASP 120 118 118 ASP ASP A . n A 1 121 THR 121 119 119 THR THR A . n A 1 122 GLU 122 120 120 GLU GLU A . n A 1 123 VAL 123 121 121 VAL VAL A . n A 1 124 ALA 124 122 122 ALA ALA A . n A 1 125 GLN 125 123 123 GLN GLN A . n A 1 126 SER 126 124 124 SER SER A . n A 1 127 ASN 127 125 125 ASN ASN A . n A 1 128 PHE 128 126 126 PHE PHE A . n A 1 129 GLU 129 127 127 GLU GLU A . n A 1 130 ALA 130 128 128 ALA ALA A . n A 1 131 LEU 131 129 129 LEU LEU A . n A 1 132 GLN 132 130 130 GLN GLN A . n A 1 133 ASP 133 131 131 ASP ASP A . n A 1 134 PHE 134 132 132 PHE PHE A . n A 1 135 PHE 135 133 133 PHE PHE A . n A 1 136 ARG 136 134 134 ARG ARG A . n A 1 137 LEU 137 135 135 LEU LEU A . n A 1 138 PHE 138 136 136 PHE PHE A . n A 1 139 PRO 139 137 137 PRO PRO A . n A 1 140 GLU 140 138 138 GLU GLU A . n A 1 141 TYR 141 139 139 TYR TYR A . n A 1 142 LYS 142 140 140 LYS LYS A . n A 1 143 ASN 143 141 141 ASN ASN A . n A 1 144 ASN 144 142 142 ASN ASN A . n A 1 145 LYS 145 143 143 LYS LYS A . n A 1 146 LEU 146 144 144 LEU LEU A . n A 1 147 PHE 147 145 145 PHE PHE A . n A 1 148 LEU 148 146 146 LEU LEU A . n A 1 149 THR 149 147 147 THR THR A . n A 1 150 GLY 150 148 148 GLY GLY A . n A 1 151 GLU 151 149 149 GLU GLU A . n A 1 152 SER 152 150 150 SER SER A . n A 1 153 TYR 153 151 151 TYR TYR A . n A 1 154 ALA 154 152 152 ALA ALA A . n A 1 155 GLY 155 153 153 GLY GLY A . n A 1 156 ILE 156 154 154 ILE ILE A . n A 1 157 TYR 157 155 155 TYR TYR A . n A 1 158 ILE 158 156 156 ILE ILE A . n A 1 159 PRO 159 157 157 PRO PRO A . n A 1 160 THR 160 158 158 THR THR A . n A 1 161 LEU 161 159 159 LEU LEU A . n A 1 162 ALA 162 160 160 ALA ALA A . n A 1 163 VAL 163 161 161 VAL VAL A . n A 1 164 LEU 164 162 162 LEU LEU A . n A 1 165 VAL 165 163 163 VAL VAL A . n A 1 166 MET 166 164 164 MET MET A . n A 1 167 GLN 167 165 165 GLN GLN A . n A 1 168 ASP 168 166 166 ASP ASP A . n A 1 169 PRO 169 167 167 PRO PRO A . n A 1 170 SER 170 168 168 SER SER A . n A 1 171 MET 171 169 169 MET MET A . n A 1 172 ASN 172 170 170 ASN ASN A . n A 1 173 LEU 173 171 171 LEU LEU A . n A 1 174 GLN 174 172 172 GLN GLN A . n A 1 175 GLY 175 173 173 GLY GLY A . n A 1 176 LEU 176 174 174 LEU LEU A . n A 1 177 ALA 177 175 175 ALA ALA A . n A 1 178 VAL 178 176 176 VAL VAL A . n A 1 179 GLY 179 177 177 GLY GLY A . n A 1 180 ASN 180 178 178 ASN ASN A . n A 1 181 GLY 181 179 179 GLY GLY A . n A 1 182 LEU 182 180 180 LEU LEU A . n A 1 183 SER 183 181 181 SER SER A . n A 1 184 SER 184 182 182 SER SER A . n A 1 185 TYR 185 183 183 TYR TYR A . n A 1 186 GLU 186 184 184 GLU GLU A . n A 1 187 GLN 187 185 185 GLN GLN A . n A 1 188 ASN 188 186 186 ASN ASN A . n A 1 189 ASP 189 187 187 ASP ASP A . n A 1 190 ASN 190 188 188 ASN ASN A . n A 1 191 SER 191 189 189 SER SER A . n A 1 192 LEU 192 190 190 LEU LEU A . n A 1 193 VAL 193 191 191 VAL VAL A . n A 1 194 TYR 194 192 192 TYR TYR A . n A 1 195 PHE 195 193 193 PHE PHE A . n A 1 196 ALA 196 194 194 ALA ALA A . n A 1 197 TYR 197 195 195 TYR TYR A . n A 1 198 TYR 198 196 196 TYR TYR A . n A 1 199 HIS 199 197 197 HIS HIS A . n A 1 200 GLY 200 198 198 GLY GLY A . n A 1 201 LEU 201 199 199 LEU LEU A . n A 1 202 LEU 202 200 200 LEU LEU A . n A 1 203 GLY 203 201 201 GLY GLY A . n A 1 204 ASN 204 202 202 ASN ASN A . n A 1 205 ARG 205 203 203 ARG ARG A . n A 1 206 LEU 206 204 204 LEU LEU A . n A 1 207 TRP 207 205 205 TRP TRP A . n A 1 208 SER 208 206 206 SER SER A . n A 1 209 SER 209 207 207 SER SER A . n A 1 210 LEU 210 208 208 LEU LEU A . n A 1 211 GLN 211 209 209 GLN GLN A . n A 1 212 THR 212 210 210 THR THR A . n A 1 213 HIS 213 211 211 HIS HIS A . n A 1 214 CYS 214 212 212 CYS CYS A . n A 1 215 CYS 215 213 213 CYS CYS A . n A 1 216 SER 216 214 214 SER SER A . n A 1 217 GLN 217 215 215 GLN GLN A . n A 1 218 ASN 218 216 216 ASN ASN A . n A 1 219 LYS 219 217 217 LYS LYS A . n A 1 220 CYS 220 218 218 CYS CYS A . n A 1 221 ASN 221 219 219 ASN ASN A . n A 1 222 PHE 222 220 220 PHE PHE A . n A 1 223 TYR 223 221 221 TYR TYR A . n A 1 224 ASP 224 222 222 ASP ASP A . n A 1 225 ASN 225 223 223 ASN ASN A . n A 1 226 LYS 226 224 224 LYS LYS A . n A 1 227 ASP 227 225 225 ASP ASP A . n A 1 228 LEU 228 226 226 LEU LEU A . n A 1 229 GLU 229 227 227 GLU GLU A . n A 1 230 CYS 230 228 228 CYS CYS A . n A 1 231 VAL 231 229 229 VAL VAL A . n A 1 232 THR 232 230 230 THR THR A . n A 1 233 ASN 233 231 231 ASN ASN A . n A 1 234 LEU 234 232 232 LEU LEU A . n A 1 235 GLN 235 233 233 GLN GLN A . n A 1 236 GLU 236 234 234 GLU GLU A . n A 1 237 VAL 237 235 235 VAL VAL A . n A 1 238 ALA 238 236 236 ALA ALA A . n A 1 239 ARG 239 237 237 ARG ARG A . n A 1 240 ILE 240 238 238 ILE ILE A . n A 1 241 VAL 241 239 239 VAL VAL A . n A 1 242 GLY 242 240 240 GLY GLY A . n A 1 243 ASN 243 241 241 ASN ASN A . n A 1 244 SER 244 242 242 SER SER A . n A 1 245 GLY 245 243 243 GLY GLY A . n A 1 246 LEU 246 244 244 LEU LEU A . n A 1 247 ASN 247 245 245 ASN ASN A . n A 1 248 ILE 248 246 246 ILE ILE A . n A 1 249 TYR 249 247 247 TYR TYR A . n A 1 250 ASN 250 248 248 ASN ASN A . n A 1 251 LEU 251 249 249 LEU LEU A . n A 1 252 TYR 252 250 250 TYR TYR A . n A 1 253 ALA 253 251 251 ALA ALA A . n A 1 254 PRO 254 252 252 PRO PRO A . n A 1 255 CYS 255 253 253 CYS CYS A . n A 1 256 ALA 256 254 254 ALA ALA A . n A 1 257 GLY 257 255 255 GLY GLY A . n A 1 258 GLY 258 256 256 GLY GLY A . n A 1 259 VAL 259 257 257 VAL VAL A . n A 1 260 PRO 260 258 258 PRO PRO A . n A 1 261 SER 261 259 ? ? ? A . n A 1 262 HIS 262 260 ? ? ? A . n A 1 263 PHE 263 261 ? ? ? A . n A 1 264 ARG 264 262 ? ? ? A . n A 1 265 TYR 265 263 ? ? ? A . n A 1 266 GLU 266 264 ? ? ? A . n A 1 267 LYS 267 265 ? ? ? A . n A 1 268 ASP 268 266 ? ? ? A . n A 1 269 THR 269 267 ? ? ? A . n A 1 270 VAL 270 268 ? ? ? A . n A 1 271 VAL 271 269 ? ? ? A . n A 1 272 VAL 272 270 ? ? ? A . n A 1 273 GLN 273 271 ? ? ? A . n A 1 274 ASP 274 272 ? ? ? A . n A 1 275 LEU 275 273 ? ? ? A . n A 1 276 GLY 276 274 ? ? ? A . n A 1 277 ASN 277 275 ? ? ? A . n A 1 278 ILE 278 276 ? ? ? A . n A 1 279 PHE 279 277 ? ? ? A . n A 1 280 THR 280 278 ? ? ? A . n A 1 281 ARG 281 279 ? ? ? A . n A 1 282 LEU 282 280 ? ? ? A . n A 1 283 PRO 283 281 ? ? ? A . n A 1 284 LEU 284 282 ? ? ? A . n A 1 285 LYS 285 283 ? ? ? A . n A 1 286 ARG 286 284 ? ? ? A . n A 1 287 MET 287 285 ? ? ? A . n A 1 288 TRP 288 286 ? ? ? A . n A 1 289 HIS 289 287 ? ? ? A . n A 1 290 GLN 290 288 ? ? ? A . n A 1 291 ALA 291 289 ? ? ? A . n A 1 292 LEU 292 290 ? ? ? A . n A 1 293 LEU 293 291 ? ? ? A . n A 1 294 ARG 294 292 ? ? ? A . n A 1 295 SER 295 293 ? ? ? A . n A 1 296 GLY 296 294 ? ? ? A . n A 1 297 ASP 297 295 ? ? ? A . n A 1 298 LYS 298 296 ? ? ? A . n A 1 299 VAL 299 297 ? ? ? A . n A 1 300 ARG 300 298 ? ? ? A . n B 2 1 MET 1 299 299 MET MET B . n B 2 2 ASP 2 300 300 ASP ASP B . n B 2 3 PRO 3 301 301 PRO PRO B . n B 2 4 PRO 4 302 302 PRO PRO B . n B 2 5 CYS 5 303 303 CYS CYS B . n B 2 6 THR 6 304 304 THR THR B . n B 2 7 ASN 7 305 305 ASN ASN B . n B 2 8 THR 8 306 306 THR THR B . n B 2 9 THR 9 307 307 THR THR B . n B 2 10 ALA 10 308 308 ALA ALA B . n B 2 11 ALA 11 309 309 ALA ALA B . n B 2 12 SER 12 310 310 SER SER B . n B 2 13 THR 13 311 311 THR THR B . n B 2 14 TYR 14 312 312 TYR TYR B . n B 2 15 LEU 15 313 313 LEU LEU B . n B 2 16 ASN 16 314 314 ASN ASN B . n B 2 17 ASN 17 315 315 ASN ASN B . n B 2 18 PRO 18 316 316 PRO PRO B . n B 2 19 TYR 19 317 317 TYR TYR B . n B 2 20 VAL 20 318 318 VAL VAL B . n B 2 21 ARG 21 319 319 ARG ARG B . n B 2 22 LYS 22 320 320 LYS LYS B . n B 2 23 ALA 23 321 321 ALA ALA B . n B 2 24 LEU 24 322 322 LEU LEU B . n B 2 25 ASN 25 323 323 ASN ASN B . n B 2 26 ILE 26 324 324 ILE ILE B . n B 2 27 PRO 27 325 325 PRO PRO B . n B 2 28 GLU 28 326 326 GLU GLU B . n B 2 29 GLN 29 327 327 GLN GLN B . n B 2 30 LEU 30 328 328 LEU LEU B . n B 2 31 PRO 31 329 329 PRO PRO B . n B 2 32 GLN 32 330 330 GLN GLN B . n B 2 33 TRP 33 331 331 TRP TRP B . n B 2 34 ASP 34 332 332 ASP ASP B . n B 2 35 MET 35 333 333 MET MET B . n B 2 36 CYS 36 334 334 CYS CYS B . n B 2 37 ASN 37 335 335 ASN ASN B . n B 2 38 PHE 38 336 336 PHE PHE B . n B 2 39 LEU 39 337 337 LEU LEU B . n B 2 40 VAL 40 338 338 VAL VAL B . n B 2 41 ASN 41 339 339 ASN ASN B . n B 2 42 LEU 42 340 340 LEU LEU B . n B 2 43 GLN 43 341 341 GLN GLN B . n B 2 44 TYR 44 342 342 TYR TYR B . n B 2 45 ARG 45 343 343 ARG ARG B . n B 2 46 ARG 46 344 344 ARG ARG B . n B 2 47 LEU 47 345 345 LEU LEU B . n B 2 48 TYR 48 346 346 TYR TYR B . n B 2 49 ARG 49 347 347 ARG ARG B . n B 2 50 SER 50 348 348 SER SER B . n B 2 51 MET 51 349 349 MET MET B . n B 2 52 ASN 52 350 350 ASN ASN B . n B 2 53 SER 53 351 351 SER SER B . n B 2 54 GLN 54 352 352 GLN GLN B . n B 2 55 TYR 55 353 353 TYR TYR B . n B 2 56 LEU 56 354 354 LEU LEU B . n B 2 57 LYS 57 355 355 LYS LYS B . n B 2 58 LEU 58 356 356 LEU LEU B . n B 2 59 LEU 59 357 357 LEU LEU B . n B 2 60 SER 60 358 358 SER SER B . n B 2 61 SER 61 359 359 SER SER B . n B 2 62 GLN 62 360 360 GLN GLN B . n B 2 63 LYS 63 361 361 LYS LYS B . n B 2 64 TYR 64 362 362 TYR TYR B . n B 2 65 GLN 65 363 363 GLN GLN B . n B 2 66 ILE 66 364 364 ILE ILE B . n B 2 67 LEU 67 365 365 LEU LEU B . n B 2 68 LEU 68 366 366 LEU LEU B . n B 2 69 TYR 69 367 367 TYR TYR B . n B 2 70 ASN 70 368 368 ASN ASN B . n B 2 71 GLY 71 369 369 GLY GLY B . n B 2 72 ASP 72 370 370 ASP ASP B . n B 2 73 VAL 73 371 371 VAL VAL B . n B 2 74 ASP 74 372 372 ASP ASP B . n B 2 75 MET 75 373 373 MET MET B . n B 2 76 ALA 76 374 374 ALA ALA B . n B 2 77 CYS 77 375 375 CYS CYS B . n B 2 78 ASN 78 376 376 ASN ASN B . n B 2 79 PHE 79 377 377 PHE PHE B . n B 2 80 MET 80 378 378 MET MET B . n B 2 81 GLY 81 379 379 GLY GLY B . n B 2 82 ASP 82 380 380 ASP ASP B . n B 2 83 GLU 83 381 381 GLU GLU B . n B 2 84 TRP 84 382 382 TRP TRP B . n B 2 85 PHE 85 383 383 PHE PHE B . n B 2 86 VAL 86 384 384 VAL VAL B . n B 2 87 ASP 87 385 385 ASP ASP B . n B 2 88 SER 88 386 386 SER SER B . n B 2 89 LEU 89 387 387 LEU LEU B . n B 2 90 ASN 90 388 388 ASN ASN B . n B 2 91 GLN 91 389 389 GLN GLN B . n B 2 92 LYS 92 390 390 LYS LYS B . n B 2 93 MET 93 391 391 MET MET B . n B 2 94 GLU 94 392 392 GLU GLU B . n B 2 95 VAL 95 393 393 VAL VAL B . n B 2 96 GLN 96 394 394 GLN GLN B . n B 2 97 ARG 97 395 395 ARG ARG B . n B 2 98 ARG 98 396 396 ARG ARG B . n B 2 99 PRO 99 397 397 PRO PRO B . n B 2 100 TRP 100 398 398 TRP TRP B . n B 2 101 LEU 101 399 399 LEU LEU B . n B 2 102 VAL 102 400 400 VAL VAL B . n B 2 103 LYS 103 401 401 LYS LYS B . n B 2 104 TYR 104 402 402 TYR TYR B . n B 2 105 GLY 105 403 403 GLY GLY B . n B 2 106 ASP 106 404 404 ASP ASP B . n B 2 107 SER 107 405 405 SER SER B . n B 2 108 GLY 108 406 406 GLY GLY B . n B 2 109 GLU 109 407 407 GLU GLU B . n B 2 110 GLN 110 408 408 GLN GLN B . n B 2 111 ILE 111 409 409 ILE ILE B . n B 2 112 ALA 112 410 410 ALA ALA B . n B 2 113 GLY 113 411 411 GLY GLY B . n B 2 114 PHE 114 412 412 PHE PHE B . n B 2 115 VAL 115 413 413 VAL VAL B . n B 2 116 LYS 116 414 414 LYS LYS B . n B 2 117 GLU 117 415 415 GLU GLU B . n B 2 118 PHE 118 416 416 PHE PHE B . n B 2 119 SER 119 417 417 SER SER B . n B 2 120 HIS 120 418 418 HIS HIS B . n B 2 121 ILE 121 419 419 ILE ILE B . n B 2 122 ALA 122 420 420 ALA ALA B . n B 2 123 PHE 123 421 421 PHE PHE B . n B 2 124 LEU 124 422 422 LEU LEU B . n B 2 125 THR 125 423 423 THR THR B . n B 2 126 ILE 126 424 424 ILE ILE B . n B 2 127 LYS 127 425 425 LYS LYS B . n B 2 128 GLY 128 426 426 GLY GLY B . n B 2 129 ALA 129 427 427 ALA ALA B . n B 2 130 GLY 130 428 428 GLY GLY B . n B 2 131 HIS 131 429 429 HIS HIS B . n B 2 132 MET 132 430 430 MET MET B . n B 2 133 VAL 133 431 431 VAL VAL B . n B 2 134 PRO 134 432 432 PRO PRO B . n B 2 135 THR 135 433 433 THR THR B . n B 2 136 ASP 136 434 434 ASP ASP B . n B 2 137 LYS 137 435 435 LYS LYS B . n B 2 138 PRO 138 436 436 PRO PRO B . n B 2 139 LEU 139 437 437 LEU LEU B . n B 2 140 ALA 140 438 438 ALA ALA B . n B 2 141 ALA 141 439 439 ALA ALA B . n B 2 142 PHE 142 440 440 PHE PHE B . n B 2 143 THR 143 441 441 THR THR B . n B 2 144 MET 144 442 442 MET MET B . n B 2 145 PHE 145 443 443 PHE PHE B . n B 2 146 SER 146 444 444 SER SER B . n B 2 147 ARG 147 445 445 ARG ARG B . n B 2 148 PHE 148 446 446 PHE PHE B . n B 2 149 LEU 149 447 447 LEU LEU B . n B 2 150 ASN 150 448 448 ASN ASN B . n B 2 151 LYS 151 449 449 LYS LYS B . n B 2 152 GLN 152 450 450 GLN GLN B . n B 2 153 PRO 153 451 451 PRO PRO B . n B 2 154 TYR 154 452 452 TYR TYR B . n B 2 155 GLU 155 453 453 GLU GLU B . 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 C 3 S35 1 1259 1259 S35 S35 A . D 4 CD 1 1260 1260 CD CD A . E 4 CD 1 1261 1261 CD CD A . F 4 CD 1 1262 1262 CD CD A . G 5 NAG 1 3010 3010 NAG NAG A . H 5 NAG 2 3011 3011 NAG NAG A . I 5 NAG 1 3020 3020 NAG NAG A . J 5 NAG 2 3021 3021 NAG NAG A . K 4 CD 1 1454 1454 CD CD B . L 6 HOH 1 2001 2001 HOH HOH A . L 6 HOH 2 2002 2002 HOH HOH A . L 6 HOH 3 2003 2003 HOH HOH A . L 6 HOH 4 2004 2004 HOH HOH A . L 6 HOH 5 2005 2005 HOH HOH A . L 6 HOH 6 2006 2006 HOH HOH A . L 6 HOH 7 2007 2007 HOH HOH A . L 6 HOH 8 2008 2008 HOH HOH A . L 6 HOH 9 2009 2009 HOH HOH A . L 6 HOH 10 2010 2010 HOH HOH A . L 6 HOH 11 2011 2011 HOH HOH A . L 6 HOH 12 2012 2012 HOH HOH A . L 6 HOH 13 2013 2013 HOH HOH A . L 6 HOH 14 2014 2014 HOH HOH A . L 6 HOH 15 2015 2015 HOH HOH A . L 6 HOH 16 2016 2016 HOH HOH A . L 6 HOH 17 2017 2017 HOH HOH A . L 6 HOH 18 2018 2018 HOH HOH A . L 6 HOH 19 2019 2019 HOH HOH A . L 6 HOH 20 2020 2020 HOH HOH A . L 6 HOH 21 2021 2021 HOH HOH A . L 6 HOH 22 2022 2022 HOH HOH A . L 6 HOH 23 2023 2023 HOH HOH A . L 6 HOH 24 2024 2024 HOH HOH A . L 6 HOH 25 2025 2025 HOH HOH A . L 6 HOH 26 2026 2026 HOH HOH A . L 6 HOH 27 2027 2027 HOH HOH A . L 6 HOH 28 2028 2028 HOH HOH A . L 6 HOH 29 2029 2029 HOH HOH A . L 6 HOH 30 2030 2030 HOH HOH A . L 6 HOH 31 2031 2031 HOH HOH A . L 6 HOH 32 2032 2032 HOH HOH A . L 6 HOH 33 2033 2033 HOH HOH A . L 6 HOH 34 2034 2034 HOH HOH A . L 6 HOH 35 2035 2035 HOH HOH A . L 6 HOH 36 2036 2036 HOH HOH A . L 6 HOH 37 2037 2037 HOH HOH A . L 6 HOH 38 2038 2038 HOH HOH A . L 6 HOH 39 2039 2039 HOH HOH A . L 6 HOH 40 2040 2040 HOH HOH A . L 6 HOH 41 2041 2041 HOH HOH A . L 6 HOH 42 2042 2042 HOH HOH A . L 6 HOH 43 2043 2043 HOH HOH A . L 6 HOH 44 2044 2044 HOH HOH A . L 6 HOH 45 2045 2045 HOH HOH A . L 6 HOH 46 2046 2046 HOH HOH A . L 6 HOH 47 2047 2047 HOH HOH A . L 6 HOH 48 2048 2048 HOH HOH A . L 6 HOH 49 2049 2049 HOH HOH A . L 6 HOH 50 2050 2050 HOH HOH A . L 6 HOH 51 2051 2051 HOH HOH A . L 6 HOH 52 2052 2052 HOH HOH A . L 6 HOH 53 2053 2053 HOH HOH A . L 6 HOH 54 2054 2054 HOH HOH A . L 6 HOH 55 2055 2055 HOH HOH A . L 6 HOH 56 2056 2056 HOH HOH A . L 6 HOH 57 2057 2057 HOH HOH A . L 6 HOH 58 2058 2058 HOH HOH A . L 6 HOH 59 2059 2059 HOH HOH A . L 6 HOH 60 2060 2060 HOH HOH A . L 6 HOH 61 2061 2061 HOH HOH A . L 6 HOH 62 2062 2062 HOH HOH A . L 6 HOH 63 2063 2063 HOH HOH A . L 6 HOH 64 2064 2064 HOH HOH A . L 6 HOH 65 2065 2065 HOH HOH A . L 6 HOH 66 2066 2066 HOH HOH A . L 6 HOH 67 2067 2067 HOH HOH A . L 6 HOH 68 2068 2068 HOH HOH A . L 6 HOH 69 2069 2069 HOH HOH A . L 6 HOH 70 2070 2070 HOH HOH A . L 6 HOH 71 2071 2071 HOH HOH A . L 6 HOH 72 2072 2072 HOH HOH A . L 6 HOH 73 2073 2073 HOH HOH A . L 6 HOH 74 2074 2074 HOH HOH A . L 6 HOH 75 2075 2075 HOH HOH A . L 6 HOH 76 2076 2076 HOH HOH A . L 6 HOH 77 2077 2077 HOH HOH A . L 6 HOH 78 2078 2078 HOH HOH A . L 6 HOH 79 2079 2079 HOH HOH A . L 6 HOH 80 2080 2080 HOH HOH A . L 6 HOH 81 2081 2081 HOH HOH A . L 6 HOH 82 2082 2082 HOH HOH A . L 6 HOH 83 2083 2083 HOH HOH A . L 6 HOH 84 2084 2084 HOH HOH A . L 6 HOH 85 2085 2085 HOH HOH A . L 6 HOH 86 2086 2086 HOH HOH A . L 6 HOH 87 2087 2087 HOH HOH A . L 6 HOH 88 2088 2088 HOH HOH A . L 6 HOH 89 2089 2089 HOH HOH A . L 6 HOH 90 2090 2090 HOH HOH A . L 6 HOH 91 2091 2091 HOH HOH A . L 6 HOH 92 2092 2092 HOH HOH A . L 6 HOH 93 2093 2093 HOH HOH A . L 6 HOH 94 2094 2094 HOH HOH A . L 6 HOH 95 2095 2095 HOH HOH A . L 6 HOH 96 2096 2096 HOH HOH A . L 6 HOH 97 2097 2097 HOH HOH A . L 6 HOH 98 2098 2098 HOH HOH A . L 6 HOH 99 2099 2099 HOH HOH A . L 6 HOH 100 2100 2100 HOH HOH A . L 6 HOH 101 2101 2101 HOH HOH A . L 6 HOH 102 2102 2102 HOH HOH A . L 6 HOH 103 2103 2103 HOH HOH A . L 6 HOH 104 2104 2104 HOH HOH A . L 6 HOH 105 2105 2105 HOH HOH A . L 6 HOH 106 2106 2106 HOH HOH A . L 6 HOH 107 2107 2107 HOH HOH A . L 6 HOH 108 2108 2108 HOH HOH A . L 6 HOH 109 2109 2109 HOH HOH A . L 6 HOH 110 2110 2110 HOH HOH A . L 6 HOH 111 2111 2111 HOH HOH A . L 6 HOH 112 2112 2112 HOH HOH A . L 6 HOH 113 2113 2113 HOH HOH A . L 6 HOH 114 2114 2114 HOH HOH A . L 6 HOH 115 2115 2115 HOH HOH A . L 6 HOH 116 2116 2116 HOH HOH A . L 6 HOH 117 2117 2117 HOH HOH A . L 6 HOH 118 2118 2118 HOH HOH A . L 6 HOH 119 2119 2119 HOH HOH A . L 6 HOH 120 2120 2120 HOH HOH A . L 6 HOH 121 2121 2121 HOH HOH A . L 6 HOH 122 2122 2122 HOH HOH A . L 6 HOH 123 2123 2123 HOH HOH A . L 6 HOH 124 2124 2124 HOH HOH A . L 6 HOH 125 2125 2125 HOH HOH A . L 6 HOH 126 2126 2126 HOH HOH A . L 6 HOH 127 2127 2127 HOH HOH A . L 6 HOH 128 2128 2128 HOH HOH A . L 6 HOH 129 2129 2129 HOH HOH A . L 6 HOH 130 2130 2130 HOH HOH A . L 6 HOH 131 2131 2131 HOH HOH A . L 6 HOH 132 2132 2132 HOH HOH A . L 6 HOH 133 2133 2133 HOH HOH A . L 6 HOH 134 2134 2134 HOH HOH A . L 6 HOH 135 2135 2135 HOH HOH A . L 6 HOH 136 2136 2136 HOH HOH A . L 6 HOH 137 2137 2137 HOH HOH A . L 6 HOH 138 2138 2138 HOH HOH A . L 6 HOH 139 2139 2139 HOH HOH A . L 6 HOH 140 2140 2140 HOH HOH A . L 6 HOH 141 2141 2141 HOH HOH A . L 6 HOH 142 2142 2142 HOH HOH A . L 6 HOH 143 2143 2143 HOH HOH A . L 6 HOH 144 2144 2144 HOH HOH A . L 6 HOH 145 2145 2145 HOH HOH A . L 6 HOH 146 2146 2146 HOH HOH A . L 6 HOH 147 2147 2147 HOH HOH A . L 6 HOH 148 2148 2148 HOH HOH A . L 6 HOH 149 2149 2149 HOH HOH A . L 6 HOH 150 2150 2150 HOH HOH A . L 6 HOH 151 2151 2151 HOH HOH A . L 6 HOH 152 2152 2152 HOH HOH A . L 6 HOH 153 2153 2153 HOH HOH A . L 6 HOH 154 2154 2154 HOH HOH A . L 6 HOH 155 2155 2155 HOH HOH A . L 6 HOH 156 2156 2156 HOH HOH A . L 6 HOH 157 2157 2157 HOH HOH A . L 6 HOH 158 2158 2158 HOH HOH A . L 6 HOH 159 2159 2159 HOH HOH A . L 6 HOH 160 2160 2160 HOH HOH A . L 6 HOH 161 2161 2161 HOH HOH A . L 6 HOH 162 2162 2162 HOH HOH A . L 6 HOH 163 2163 2163 HOH HOH A . L 6 HOH 164 2164 2164 HOH HOH A . L 6 HOH 165 2165 2165 HOH HOH A . L 6 HOH 166 2166 2166 HOH HOH A . L 6 HOH 167 2167 2167 HOH HOH A . L 6 HOH 168 2168 2168 HOH HOH A . L 6 HOH 169 2169 2169 HOH HOH A . L 6 HOH 170 2170 2170 HOH HOH A . L 6 HOH 171 2171 2171 HOH HOH A . L 6 HOH 172 2172 2172 HOH HOH A . L 6 HOH 173 2173 2173 HOH HOH A . L 6 HOH 174 2174 2174 HOH HOH A . L 6 HOH 175 2175 2175 HOH HOH A . L 6 HOH 176 2176 2176 HOH HOH A . L 6 HOH 177 2177 2177 HOH HOH A . L 6 HOH 178 2178 2178 HOH HOH A . L 6 HOH 179 2179 2179 HOH HOH A . L 6 HOH 180 2180 2180 HOH HOH A . L 6 HOH 181 2181 2181 HOH HOH A . L 6 HOH 182 2182 2182 HOH HOH A . L 6 HOH 183 2183 2183 HOH HOH A . L 6 HOH 184 2184 2184 HOH HOH A . L 6 HOH 185 2185 2185 HOH HOH A . L 6 HOH 186 2186 2186 HOH HOH A . L 6 HOH 187 2187 2187 HOH HOH A . L 6 HOH 188 2188 2188 HOH HOH A . L 6 HOH 189 2189 2189 HOH HOH A . L 6 HOH 190 2190 2190 HOH HOH A . L 6 HOH 191 2191 2191 HOH HOH A . L 6 HOH 192 2192 2192 HOH HOH A . L 6 HOH 193 2193 2193 HOH HOH A . L 6 HOH 194 2194 2194 HOH HOH A . L 6 HOH 195 2195 2195 HOH HOH A . L 6 HOH 196 2196 2196 HOH HOH A . L 6 HOH 197 2197 2197 HOH HOH A . L 6 HOH 198 2198 2198 HOH HOH A . L 6 HOH 199 2199 2199 HOH HOH A . L 6 HOH 200 2200 2200 HOH HOH A . L 6 HOH 201 2201 2201 HOH HOH A . L 6 HOH 202 2202 2202 HOH HOH A . L 6 HOH 203 2203 2203 HOH HOH A . L 6 HOH 204 2204 2204 HOH HOH A . L 6 HOH 205 2205 2205 HOH HOH A . L 6 HOH 206 2206 2206 HOH HOH A . L 6 HOH 207 2207 2207 HOH HOH A . L 6 HOH 208 2208 2208 HOH HOH A . L 6 HOH 209 2209 2209 HOH HOH A . L 6 HOH 210 2210 2210 HOH HOH A . L 6 HOH 211 2211 2211 HOH HOH A . L 6 HOH 212 2212 2212 HOH HOH A . L 6 HOH 213 2213 2213 HOH HOH A . L 6 HOH 214 2214 2214 HOH HOH A . L 6 HOH 215 2215 2215 HOH HOH A . L 6 HOH 216 2216 2216 HOH HOH A . L 6 HOH 217 2217 2217 HOH HOH A . L 6 HOH 218 2218 2218 HOH HOH A . L 6 HOH 219 2219 2219 HOH HOH A . L 6 HOH 220 2220 2220 HOH HOH A . L 6 HOH 221 2221 2221 HOH HOH A . L 6 HOH 222 2222 2222 HOH HOH A . L 6 HOH 223 2223 2223 HOH HOH A . L 6 HOH 224 2224 2224 HOH HOH A . L 6 HOH 225 2225 2225 HOH HOH A . L 6 HOH 226 2226 2226 HOH HOH A . L 6 HOH 227 2227 2227 HOH HOH A . L 6 HOH 228 2228 2228 HOH HOH A . L 6 HOH 229 2229 2229 HOH HOH A . L 6 HOH 230 2230 2230 HOH HOH A . L 6 HOH 231 2231 2231 HOH HOH A . L 6 HOH 232 2232 2232 HOH HOH A . L 6 HOH 233 2233 2233 HOH HOH A . L 6 HOH 234 2234 2234 HOH HOH A . L 6 HOH 235 2235 2235 HOH HOH A . L 6 HOH 236 2236 2236 HOH HOH A . L 6 HOH 237 2237 2237 HOH HOH A . L 6 HOH 238 2238 2238 HOH HOH A . L 6 HOH 239 2239 2239 HOH HOH A . L 6 HOH 240 2240 2240 HOH HOH A . L 6 HOH 241 2241 2241 HOH HOH A . L 6 HOH 242 2242 2242 HOH HOH A . L 6 HOH 243 2243 2243 HOH HOH A . L 6 HOH 244 2244 2244 HOH HOH A . L 6 HOH 245 2245 2245 HOH HOH A . L 6 HOH 246 2246 2246 HOH HOH A . L 6 HOH 247 2247 2247 HOH HOH A . L 6 HOH 248 2248 2248 HOH HOH A . L 6 HOH 249 2249 2249 HOH HOH A . L 6 HOH 250 2250 2250 HOH HOH A . L 6 HOH 251 2251 2251 HOH HOH A . L 6 HOH 252 2252 2252 HOH HOH A . L 6 HOH 253 2253 2253 HOH HOH A . L 6 HOH 254 2254 2254 HOH HOH A . L 6 HOH 255 2255 2255 HOH HOH A . L 6 HOH 256 2256 2256 HOH HOH A . L 6 HOH 257 2257 2257 HOH HOH A . L 6 HOH 258 2258 2258 HOH HOH A . L 6 HOH 259 2259 2259 HOH HOH A . L 6 HOH 260 2260 2260 HOH HOH A . L 6 HOH 261 2261 2261 HOH HOH A . L 6 HOH 262 2262 2262 HOH HOH A . L 6 HOH 263 2263 2263 HOH HOH A . L 6 HOH 264 2264 2264 HOH HOH A . L 6 HOH 265 2265 2265 HOH HOH A . L 6 HOH 266 2266 2266 HOH HOH A . L 6 HOH 267 2267 2267 HOH HOH A . L 6 HOH 268 2268 2268 HOH HOH A . L 6 HOH 269 2269 2269 HOH HOH A . M 6 HOH 1 2001 2001 HOH HOH B . M 6 HOH 2 2002 2002 HOH HOH B . M 6 HOH 3 2003 2003 HOH HOH B . M 6 HOH 4 2004 2004 HOH HOH B . M 6 HOH 5 2005 2005 HOH HOH B . M 6 HOH 6 2006 2006 HOH HOH B . M 6 HOH 7 2007 2007 HOH HOH B . M 6 HOH 8 2008 2008 HOH HOH B . M 6 HOH 9 2009 2009 HOH HOH B . M 6 HOH 10 2010 2010 HOH HOH B . M 6 HOH 11 2011 2011 HOH HOH B . M 6 HOH 12 2012 2012 HOH HOH B . M 6 HOH 13 2013 2013 HOH HOH B . M 6 HOH 14 2014 2014 HOH HOH B . M 6 HOH 15 2015 2015 HOH HOH B . M 6 HOH 16 2016 2016 HOH HOH B . M 6 HOH 17 2017 2017 HOH HOH B . M 6 HOH 18 2018 2018 HOH HOH B . M 6 HOH 19 2019 2019 HOH HOH B . M 6 HOH 20 2020 2020 HOH HOH B . M 6 HOH 21 2021 2021 HOH HOH B . M 6 HOH 22 2022 2022 HOH HOH B . M 6 HOH 23 2023 2023 HOH HOH B . M 6 HOH 24 2024 2024 HOH HOH B . M 6 HOH 25 2025 2025 HOH HOH B . M 6 HOH 26 2026 2026 HOH HOH B . M 6 HOH 27 2027 2027 HOH HOH B . M 6 HOH 28 2028 2028 HOH HOH B . M 6 HOH 29 2029 2029 HOH HOH B . M 6 HOH 30 2030 2030 HOH HOH B . M 6 HOH 31 2031 2031 HOH HOH B . M 6 HOH 32 2032 2032 HOH HOH B . M 6 HOH 33 2033 2033 HOH HOH B . M 6 HOH 34 2034 2034 HOH HOH B . M 6 HOH 35 2035 2035 HOH HOH B . M 6 HOH 36 2036 2036 HOH HOH B . M 6 HOH 37 2037 2037 HOH HOH B . M 6 HOH 38 2038 2038 HOH HOH B . M 6 HOH 39 2039 2039 HOH HOH B . M 6 HOH 40 2040 2040 HOH HOH B . M 6 HOH 41 2041 2041 HOH HOH B . M 6 HOH 42 2042 2042 HOH HOH B . M 6 HOH 43 2043 2043 HOH HOH B . M 6 HOH 44 2044 2044 HOH HOH B . M 6 HOH 45 2045 2045 HOH HOH B . M 6 HOH 46 2046 2046 HOH HOH B . M 6 HOH 47 2047 2047 HOH HOH B . M 6 HOH 48 2048 2048 HOH HOH B . M 6 HOH 49 2049 2049 HOH HOH B . M 6 HOH 50 2050 2050 HOH HOH B . M 6 HOH 51 2051 2051 HOH HOH B . M 6 HOH 52 2052 2052 HOH HOH B . M 6 HOH 53 2053 2053 HOH HOH B . M 6 HOH 54 2054 2054 HOH HOH B . M 6 HOH 55 2055 2055 HOH HOH B . M 6 HOH 56 2056 2056 HOH HOH B . M 6 HOH 57 2057 2057 HOH HOH B . M 6 HOH 58 2058 2058 HOH HOH B . M 6 HOH 59 2059 2059 HOH HOH B . M 6 HOH 60 2060 2060 HOH HOH B . M 6 HOH 61 2061 2061 HOH HOH B . M 6 HOH 62 2062 2062 HOH HOH B . M 6 HOH 63 2063 2063 HOH HOH B . M 6 HOH 64 2064 2064 HOH HOH B . M 6 HOH 65 2065 2065 HOH HOH B . M 6 HOH 66 2066 2066 HOH HOH B . M 6 HOH 67 2067 2067 HOH HOH B . M 6 HOH 68 2068 2068 HOH HOH B . M 6 HOH 69 2069 2069 HOH HOH B . M 6 HOH 70 2070 2070 HOH HOH B . M 6 HOH 71 2071 2071 HOH HOH B . M 6 HOH 72 2072 2072 HOH HOH B . M 6 HOH 73 2073 2073 HOH HOH B . M 6 HOH 74 2074 2074 HOH HOH B . M 6 HOH 75 2075 2075 HOH HOH B . M 6 HOH 76 2076 2076 HOH HOH B . M 6 HOH 77 2077 2077 HOH HOH B . M 6 HOH 78 2078 2078 HOH HOH B . M 6 HOH 79 2079 2079 HOH HOH B . M 6 HOH 80 2080 2080 HOH HOH B . M 6 HOH 81 2081 2081 HOH HOH B . M 6 HOH 82 2082 2082 HOH HOH B . M 6 HOH 83 2083 2083 HOH HOH B . M 6 HOH 84 2084 2084 HOH HOH B . M 6 HOH 85 2085 2085 HOH HOH B . M 6 HOH 86 2086 2086 HOH HOH B . M 6 HOH 87 2087 2087 HOH HOH B . M 6 HOH 88 2088 2088 HOH HOH B . M 6 HOH 89 2089 2089 HOH HOH B . M 6 HOH 90 2090 2090 HOH HOH B . M 6 HOH 91 2091 2091 HOH HOH B . M 6 HOH 92 2092 2092 HOH HOH B . M 6 HOH 93 2093 2093 HOH HOH B . M 6 HOH 94 2094 2094 HOH HOH B . M 6 HOH 95 2095 2095 HOH HOH B . M 6 HOH 96 2096 2096 HOH HOH B . M 6 HOH 97 2097 2097 HOH HOH B . M 6 HOH 98 2098 2098 HOH HOH B . M 6 HOH 99 2099 2099 HOH HOH B . M 6 HOH 100 2100 2100 HOH HOH B . M 6 HOH 101 2101 2101 HOH HOH B . M 6 HOH 102 2102 2102 HOH HOH B . M 6 HOH 103 2103 2103 HOH HOH B . M 6 HOH 104 2104 2104 HOH HOH B . M 6 HOH 105 2105 2105 HOH HOH B . M 6 HOH 106 2106 2106 HOH HOH B . M 6 HOH 107 2107 2107 HOH HOH B . M 6 HOH 108 2108 2108 HOH HOH B . M 6 HOH 109 2109 2109 HOH HOH B . M 6 HOH 110 2110 2110 HOH HOH B . M 6 HOH 111 2111 2111 HOH HOH B . M 6 HOH 112 2112 2112 HOH HOH B . M 6 HOH 113 2113 2113 HOH HOH B . M 6 HOH 114 2114 2114 HOH HOH B . M 6 HOH 115 2115 2115 HOH HOH B . M 6 HOH 116 2116 2116 HOH HOH B . M 6 HOH 117 2117 2117 HOH HOH B . M 6 HOH 118 2118 2118 HOH HOH B . M 6 HOH 119 2119 2119 HOH HOH B . M 6 HOH 120 2120 2120 HOH HOH B . M 6 HOH 121 2121 2121 HOH HOH B . M 6 HOH 122 2122 2122 HOH HOH B . M 6 HOH 123 2123 2123 HOH HOH B . M 6 HOH 124 2124 2124 HOH HOH B . M 6 HOH 125 2125 2125 HOH HOH B . M 6 HOH 126 2126 2126 HOH HOH B . M 6 HOH 127 2127 2127 HOH HOH B . M 6 HOH 128 2128 2128 HOH HOH B . M 6 HOH 129 2129 2129 HOH HOH B . M 6 HOH 130 2130 2130 HOH HOH B . M 6 HOH 131 2131 2131 HOH HOH B . M 6 HOH 132 2132 2132 HOH HOH B . M 6 HOH 133 2133 2133 HOH HOH B . M 6 HOH 134 2134 2134 HOH HOH B . M 6 HOH 135 2135 2135 HOH HOH B . M 6 HOH 136 2136 2136 HOH HOH B . M 6 HOH 137 2137 2137 HOH HOH B . M 6 HOH 138 2138 2138 HOH HOH B . M 6 HOH 139 2139 2139 HOH HOH B . M 6 HOH 140 2140 2140 HOH HOH B . M 6 HOH 141 2141 2141 HOH HOH B . M 6 HOH 142 2142 2142 HOH HOH B . M 6 HOH 143 2143 2143 HOH HOH B . M 6 HOH 144 2144 2144 HOH HOH B . M 6 HOH 145 2145 2145 HOH HOH B . M 6 HOH 146 2146 2146 HOH HOH B . M 6 HOH 147 2147 2147 HOH HOH B . M 6 HOH 148 2148 2148 HOH HOH B . M 6 HOH 149 2149 2149 HOH HOH B . M 6 HOH 150 2150 2150 HOH HOH B . M 6 HOH 151 2151 2151 HOH HOH B . M 6 HOH 152 2152 2152 HOH HOH B . M 6 HOH 153 2153 2153 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 119 A ASN 117 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 7 B ASN 305 ? ASN 'GLYCOSYLATION SITE' # _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 dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 9920 ? 1 MORE -83.5 ? 1 'SSA (A^2)' 17930 ? # _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 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id A _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 2207 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id L _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 OE2 ? A GLU 186 ? A GLU 184 ? 1_555 CD ? D CD . ? A CD 1260 ? 1_555 OE1 ? A GLU 186 ? A GLU 184 ? 1_555 44.5 ? 2 OD2 ? A ASP 5 ? A ASP 3 ? 3_455 CD ? E CD . ? A CD 1261 ? 1_555 O ? L HOH . ? A HOH 2220 ? 1_555 137.3 ? 3 OD2 ? A ASP 5 ? A ASP 3 ? 3_455 CD ? E CD . ? A CD 1261 ? 1_555 OD1 ? A ASP 5 ? A ASP 3 ? 3_455 56.0 ? 4 O ? L HOH . ? A HOH 2220 ? 1_555 CD ? E CD . ? A CD 1261 ? 1_555 OD1 ? A ASP 5 ? A ASP 3 ? 3_455 97.8 ? 5 OD2 ? A ASP 5 ? A ASP 3 ? 3_455 CD ? E CD . ? A CD 1261 ? 1_555 OD1 ? A ASP 227 ? A ASP 225 ? 1_555 72.5 ? 6 O ? L HOH . ? A HOH 2220 ? 1_555 CD ? E CD . ? A CD 1261 ? 1_555 OD1 ? A ASP 227 ? A ASP 225 ? 1_555 136.1 ? 7 OD1 ? A ASP 5 ? A ASP 3 ? 3_455 CD ? E CD . ? A CD 1261 ? 1_555 OD1 ? A ASP 227 ? A ASP 225 ? 1_555 124.6 ? 8 OD2 ? A ASP 5 ? A ASP 3 ? 3_455 CD ? E CD . ? A CD 1261 ? 1_555 OD2 ? A ASP 227 ? A ASP 225 ? 1_555 87.7 ? 9 O ? L HOH . ? A HOH 2220 ? 1_555 CD ? E CD . ? A CD 1261 ? 1_555 OD2 ? A ASP 227 ? A ASP 225 ? 1_555 91.9 ? 10 OD1 ? A ASP 5 ? A ASP 3 ? 3_455 CD ? E CD . ? A CD 1261 ? 1_555 OD2 ? A ASP 227 ? A ASP 225 ? 1_555 134.6 ? 11 OD1 ? A ASP 227 ? A ASP 225 ? 1_555 CD ? E CD . ? A CD 1261 ? 1_555 OD2 ? A ASP 227 ? A ASP 225 ? 1_555 51.5 ? 12 OD2 ? A ASP 5 ? A ASP 3 ? 3_455 CD ? E CD . ? A CD 1261 ? 1_555 ND1 ? A HIS 213 ? A HIS 211 ? 1_555 112.5 ? 13 O ? L HOH . ? A HOH 2220 ? 1_555 CD ? E CD . ? A CD 1261 ? 1_555 ND1 ? A HIS 213 ? A HIS 211 ? 1_555 97.1 ? 14 OD1 ? A ASP 5 ? A ASP 3 ? 3_455 CD ? E CD . ? A CD 1261 ? 1_555 ND1 ? A HIS 213 ? A HIS 211 ? 1_555 86.9 ? 15 OD1 ? A ASP 227 ? A ASP 225 ? 1_555 CD ? E CD . ? A CD 1261 ? 1_555 ND1 ? A HIS 213 ? A HIS 211 ? 1_555 95.9 ? 16 OD2 ? A ASP 227 ? A ASP 225 ? 1_555 CD ? E CD . ? A CD 1261 ? 1_555 ND1 ? A HIS 213 ? A HIS 211 ? 1_555 135.7 ? 17 OD2 ? A ASP 224 ? A ASP 222 ? 1_555 CD ? F CD . ? A CD 1262 ? 1_555 OE2 ? B GLU 28 ? B GLU 326 ? 4_456 90.0 ? 18 OD2 ? A ASP 224 ? A ASP 222 ? 1_555 CD ? F CD . ? A CD 1262 ? 1_555 OD1 ? A ASP 224 ? A ASP 222 ? 1_555 49.9 ? 19 OE2 ? B GLU 28 ? B GLU 326 ? 4_456 CD ? F CD . ? A CD 1262 ? 1_555 OD1 ? A ASP 224 ? A ASP 222 ? 1_555 120.3 ? 20 OD2 ? A ASP 224 ? A ASP 222 ? 1_555 CD ? F CD . ? A CD 1262 ? 1_555 OE1 ? B GLU 28 ? B GLU 326 ? 4_456 122.2 ? 21 OE2 ? B GLU 28 ? B GLU 326 ? 4_456 CD ? F CD . ? A CD 1262 ? 1_555 OE1 ? B GLU 28 ? B GLU 326 ? 4_456 45.7 ? 22 OD1 ? A ASP 224 ? A ASP 222 ? 1_555 CD ? F CD . ? A CD 1262 ? 1_555 OE1 ? B GLU 28 ? B GLU 326 ? 4_456 166.0 ? 23 O ? M HOH . ? B HOH 2091 ? 1_555 CD ? K CD . ? B CD 1454 ? 1_555 SG ? B CYS 77 ? B CYS 375 ? 1_555 139.0 ? 24 O ? M HOH . ? B HOH 2091 ? 1_555 CD ? K CD . ? B CD 1454 ? 1_555 O ? B ALA 76 ? B ALA 374 ? 1_555 79.0 ? 25 SG ? B CYS 77 ? B CYS 375 ? 1_555 CD ? K CD . ? B CD 1454 ? 1_555 O ? B ALA 76 ? B ALA 374 ? 1_555 92.5 ? # _pdbx_audit_revision_history.ordinal 1 _pdbx_audit_revision_history.data_content_type 'Structure model' _pdbx_audit_revision_history.major_revision 1 _pdbx_audit_revision_history.minor_revision 0 _pdbx_audit_revision_history.revision_date 2012-09-26 # _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 ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal BUSTER refinement 2.11.2 ? 1 XDS 'data reduction' . ? 2 XSCALE 'data scaling' . ? 3 # _pdbx_entry_details.entry_id 4AZ3 _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details 'EXTRA C-TERMINAL GLU AS LEFTOVER FROM MYC-TAG' # 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 GLU A 69 ? ? -106.95 -76.70 2 1 PRO A 101 ? ? -75.57 -168.47 3 1 SER A 150 ? ? 56.24 -111.10 4 1 GLN A 215 ? ? 57.64 -86.25 5 1 TYR A 221 ? ? -98.51 -61.45 6 1 ASN A 248 ? ? -162.04 102.19 7 1 MET B 430 ? A -110.70 76.63 8 1 MET B 430 ? B -109.00 78.08 # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? B HOH 2016 ? 6.30 . 2 1 O ? B HOH 2151 ? 7.46 . 3 1 O ? B HOH 2152 ? 6.99 . 4 1 O ? B HOH 2153 ? 6.66 . # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A ARG 0 ? CG ? A ARG 2 CG 2 1 Y 1 A ARG 0 ? CD ? A ARG 2 CD 3 1 Y 1 A ARG 0 ? NE ? A ARG 2 NE 4 1 Y 1 A ARG 0 ? CZ ? A ARG 2 CZ 5 1 Y 1 A ARG 0 ? NH1 ? A ARG 2 NH1 6 1 Y 1 A ARG 0 ? NH2 ? A ARG 2 NH2 7 1 Y 1 A GLN 8 ? CG ? A GLN 10 CG 8 1 Y 1 A GLN 8 ? CD ? A GLN 10 CD 9 1 Y 1 A GLN 8 ? OE1 ? A GLN 10 OE1 10 1 Y 1 A GLN 8 ? NE2 ? A GLN 10 NE2 11 1 Y 1 A ARG 9 ? CG ? A ARG 11 CG 12 1 Y 1 A ARG 9 ? CD ? A ARG 11 CD 13 1 Y 1 A ARG 9 ? NE ? A ARG 11 NE 14 1 Y 1 A ARG 9 ? CZ ? A ARG 11 CZ 15 1 Y 1 A ARG 9 ? NH1 ? A ARG 11 NH1 16 1 Y 1 A ARG 9 ? NH2 ? A ARG 11 NH2 17 1 Y 1 A GLU 46 ? CG ? A GLU 48 CG 18 1 Y 1 A GLU 46 ? CD ? A GLU 48 CD 19 1 Y 1 A GLU 46 ? OE1 ? A GLU 48 OE1 20 1 Y 1 A GLU 46 ? OE2 ? A GLU 48 OE2 # 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 SER -1 ? A SER 1 2 1 Y 1 A SER 259 ? A SER 261 3 1 Y 1 A HIS 260 ? A HIS 262 4 1 Y 1 A PHE 261 ? A PHE 263 5 1 Y 1 A ARG 262 ? A ARG 264 6 1 Y 1 A TYR 263 ? A TYR 265 7 1 Y 1 A GLU 264 ? A GLU 266 8 1 Y 1 A LYS 265 ? A LYS 267 9 1 Y 1 A ASP 266 ? A ASP 268 10 1 Y 1 A THR 267 ? A THR 269 11 1 Y 1 A VAL 268 ? A VAL 270 12 1 Y 1 A VAL 269 ? A VAL 271 13 1 Y 1 A VAL 270 ? A VAL 272 14 1 Y 1 A GLN 271 ? A GLN 273 15 1 Y 1 A ASP 272 ? A ASP 274 16 1 Y 1 A LEU 273 ? A LEU 275 17 1 Y 1 A GLY 274 ? A GLY 276 18 1 Y 1 A ASN 275 ? A ASN 277 19 1 Y 1 A ILE 276 ? A ILE 278 20 1 Y 1 A PHE 277 ? A PHE 279 21 1 Y 1 A THR 278 ? A THR 280 22 1 Y 1 A ARG 279 ? A ARG 281 23 1 Y 1 A LEU 280 ? A LEU 282 24 1 Y 1 A PRO 281 ? A PRO 283 25 1 Y 1 A LEU 282 ? A LEU 284 26 1 Y 1 A LYS 283 ? A LYS 285 27 1 Y 1 A ARG 284 ? A ARG 286 28 1 Y 1 A MET 285 ? A MET 287 29 1 Y 1 A TRP 286 ? A TRP 288 30 1 Y 1 A HIS 287 ? A HIS 289 31 1 Y 1 A GLN 288 ? A GLN 290 32 1 Y 1 A ALA 289 ? A ALA 291 33 1 Y 1 A LEU 290 ? A LEU 292 34 1 Y 1 A LEU 291 ? A LEU 293 35 1 Y 1 A ARG 292 ? A ARG 294 36 1 Y 1 A SER 293 ? A SER 295 37 1 Y 1 A GLY 294 ? A GLY 296 38 1 Y 1 A ASP 295 ? A ASP 297 39 1 Y 1 A LYS 296 ? A LYS 298 40 1 Y 1 A VAL 297 ? A VAL 299 41 1 Y 1 A ARG 298 ? A ARG 300 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 ;(3S)-3-({[1-(2-fluorophenyl)-5-{[(2R)-2-hydroxy-3,3-dimethylbutyl]oxy}-1H-pyrazol-3-yl]carbonyl}amino)-3-(2-methylphenyl)propanoic acid ; S35 4 'CADMIUM ION' CD 5 N-ACETYL-D-GLUCOSAMINE NAG 6 water HOH #