data_4BWC # _entry.id 4BWC # _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 4BWC PDBE EBI-56781 WWPDB D_1290056781 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4BWC _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2013-07-01 _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 'Repo, H.' 1 'Kuokkanen, E.' 2 'Oksanen, E.' 3 'Goldman, A.' 4 'Heikinheimo, P.' 5 # _citation.id primary _citation.title 'Is the Bovine Lysosomal Phospholipase B-Like Protein an Amidase?' _citation.journal_abbrev Proteins _citation.journal_volume 82 _citation.page_first 300 _citation.page_last ? _citation.year 2014 _citation.journal_id_ASTM PSFGEY _citation.country US _citation.journal_id_ISSN 0887-3585 _citation.journal_id_CSD 0867 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 23934913 _citation.pdbx_database_id_DOI 10.1002/PROT.24388 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Repo, H.' 1 primary 'Kuokkanen, E.' 2 primary 'Oksanen, E.' 3 primary 'Goldman, A.' 4 primary 'Heikinheimo, P.' 5 # _cell.entry_id 4BWC _cell.length_a 97.370 _cell.length_b 97.370 _cell.length_c 140.945 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4BWC _symmetry.space_group_name_H-M 'P 31 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 152 # 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 nat 'PHOSPHOLIPASE B-LIKE 1' 19522.355 1 3.1.1.- ? 'N-TERMINAL SEGMENT, RESIDUES 36-205' ? 2 polymer nat 'PHOSPHOLIPASE B-LIKE 1' 37160.078 1 3.1.1.- ? 'C-TERMINAL SEGMENT, RESIDUES 225-545' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 8 ? ? ? ? 4 non-polymer syn '1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE' 162.227 1 ? ? ? ? 5 non-polymer syn 'HEXAETHYLENE GLYCOL' 282.331 1 ? ? ? ? 6 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 7 water nat water 18.015 184 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'LAMA-LIKE PROTEIN 1, LAMINA ANCESTOR HOMOLOG 1, PHOSPHOLIPASE B DOMAIN-CONTAINING PROTEIN 1, PHOSPHOLIPASE B-LIKE PROTEIN 1' 2 'LAMA-LIKE PROTEIN 1, LAMINA ANCESTOR HOMOLOG 1, PHOSPHOLIPASE B DOMAIN-CONTAINING PROTEIN 1, PHOSPHOLIPASE B-LIKE PROTEIN 1' # 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 ;GVYYATAYWMPTEKTIQVKNVLDRKGDAYGFYNNSVKTTGWGILEIKAGYGSQSLSNEIIMFAAGFLEGYLTAPHMDDHF TNLYPQLIKKRSMLNKVQDFLTKQDQWTRENIKYYKSDPFWRHADYVMAQMDGLFAGATKRAVLEGKKPMTLFQIQFLNA IGDLLDLIPS ; ;GVYYATAYWMPTEKTIQVKNVLDRKGDAYGFYNNSVKTTGWGILEIKAGYGSQSLSNEIIMFAAGFLEGYLTAPHMDDHF TNLYPQLIKKRSMLNKVQDFLTKQDQWTRENIKYYKSDPFWRHADYVMAQMDGLFAGATKRAVLEGKKPMTLFQIQFLNA IGDLLDLIPS ; A ? 2 'polypeptide(L)' no yes ;(OCS)SALIKVLPGFENIFFAHSSWYTYAAMLRIYKHWDFNIVDKDTSSSRLSFSSYPGFLESLDDFYLLSSGLVLLQTT NSVYNKTLLQHVVPQSLLAWQRVRVASMMANNGKQWAEVFSKYNSGTYNNQYMVLDLKKVNLNHSLDEGTLYIVEQIPTY VEYSEQTAVLRRGYWPSYNIPFHEKVYNWSGYPILVKKLGLDYSYDLASRAKIFRRDQGKVTDMESMKYIMRYNNYKQDP YSKGDPCNTVCCREDLNSHSPSPGGCYDTKVADIYLASKYKAYAISGPTVQGGLPVFHWSRFNKTLHEGMPEAYNFDFIT MKPIL ; ;CSALIKVLPGFENIFFAHSSWYTYAAMLRIYKHWDFNIVDKDTSSSRLSFSSYPGFLESLDDFYLLSSGLVLLQTTNSVY NKTLLQHVVPQSLLAWQRVRVASMMANNGKQWAEVFSKYNSGTYNNQYMVLDLKKVNLNHSLDEGTLYIVEQIPTYVEYS EQTAVLRRGYWPSYNIPFHEKVYNWSGYPILVKKLGLDYSYDLASRAKIFRRDQGKVTDMESMKYIMRYNNYKQDPYSKG DPCNTVCCREDLNSHSPSPGGCYDTKVADIYLASKYKAYAISGPTVQGGLPVFHWSRFNKTLHEGMPEAYNFDFITMKPI L ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLY n 1 2 VAL n 1 3 TYR n 1 4 TYR n 1 5 ALA n 1 6 THR n 1 7 ALA n 1 8 TYR n 1 9 TRP n 1 10 MET n 1 11 PRO n 1 12 THR n 1 13 GLU n 1 14 LYS n 1 15 THR n 1 16 ILE n 1 17 GLN n 1 18 VAL n 1 19 LYS n 1 20 ASN n 1 21 VAL n 1 22 LEU n 1 23 ASP n 1 24 ARG n 1 25 LYS n 1 26 GLY n 1 27 ASP n 1 28 ALA n 1 29 TYR n 1 30 GLY n 1 31 PHE n 1 32 TYR n 1 33 ASN n 1 34 ASN n 1 35 SER n 1 36 VAL n 1 37 LYS n 1 38 THR n 1 39 THR n 1 40 GLY n 1 41 TRP n 1 42 GLY n 1 43 ILE n 1 44 LEU n 1 45 GLU n 1 46 ILE n 1 47 LYS n 1 48 ALA n 1 49 GLY n 1 50 TYR n 1 51 GLY n 1 52 SER n 1 53 GLN n 1 54 SER n 1 55 LEU n 1 56 SER n 1 57 ASN n 1 58 GLU n 1 59 ILE n 1 60 ILE n 1 61 MET n 1 62 PHE n 1 63 ALA n 1 64 ALA n 1 65 GLY n 1 66 PHE n 1 67 LEU n 1 68 GLU n 1 69 GLY n 1 70 TYR n 1 71 LEU n 1 72 THR n 1 73 ALA n 1 74 PRO n 1 75 HIS n 1 76 MET n 1 77 ASP n 1 78 ASP n 1 79 HIS n 1 80 PHE n 1 81 THR n 1 82 ASN n 1 83 LEU n 1 84 TYR n 1 85 PRO n 1 86 GLN n 1 87 LEU n 1 88 ILE n 1 89 LYS n 1 90 LYS n 1 91 ARG n 1 92 SER n 1 93 MET n 1 94 LEU n 1 95 ASN n 1 96 LYS n 1 97 VAL n 1 98 GLN n 1 99 ASP n 1 100 PHE n 1 101 LEU n 1 102 THR n 1 103 LYS n 1 104 GLN n 1 105 ASP n 1 106 GLN n 1 107 TRP n 1 108 THR n 1 109 ARG n 1 110 GLU n 1 111 ASN n 1 112 ILE n 1 113 LYS n 1 114 TYR n 1 115 TYR n 1 116 LYS n 1 117 SER n 1 118 ASP n 1 119 PRO n 1 120 PHE n 1 121 TRP n 1 122 ARG n 1 123 HIS n 1 124 ALA n 1 125 ASP n 1 126 TYR n 1 127 VAL n 1 128 MET n 1 129 ALA n 1 130 GLN n 1 131 MET n 1 132 ASP n 1 133 GLY n 1 134 LEU n 1 135 PHE n 1 136 ALA n 1 137 GLY n 1 138 ALA n 1 139 THR n 1 140 LYS n 1 141 ARG n 1 142 ALA n 1 143 VAL n 1 144 LEU n 1 145 GLU n 1 146 GLY n 1 147 LYS n 1 148 LYS n 1 149 PRO n 1 150 MET n 1 151 THR n 1 152 LEU n 1 153 PHE n 1 154 GLN n 1 155 ILE n 1 156 GLN n 1 157 PHE n 1 158 LEU n 1 159 ASN n 1 160 ALA n 1 161 ILE n 1 162 GLY n 1 163 ASP n 1 164 LEU n 1 165 LEU n 1 166 ASP n 1 167 LEU n 1 168 ILE n 1 169 PRO n 1 170 SER n 2 1 OCS n 2 2 SER n 2 3 ALA n 2 4 LEU n 2 5 ILE n 2 6 LYS n 2 7 VAL n 2 8 LEU n 2 9 PRO n 2 10 GLY n 2 11 PHE n 2 12 GLU n 2 13 ASN n 2 14 ILE n 2 15 PHE n 2 16 PHE n 2 17 ALA n 2 18 HIS n 2 19 SER n 2 20 SER n 2 21 TRP n 2 22 TYR n 2 23 THR n 2 24 TYR n 2 25 ALA n 2 26 ALA n 2 27 MET n 2 28 LEU n 2 29 ARG n 2 30 ILE n 2 31 TYR n 2 32 LYS n 2 33 HIS n 2 34 TRP n 2 35 ASP n 2 36 PHE n 2 37 ASN n 2 38 ILE n 2 39 VAL n 2 40 ASP n 2 41 LYS n 2 42 ASP n 2 43 THR n 2 44 SER n 2 45 SER n 2 46 SER n 2 47 ARG n 2 48 LEU n 2 49 SER n 2 50 PHE n 2 51 SER n 2 52 SER n 2 53 TYR n 2 54 PRO n 2 55 GLY n 2 56 PHE n 2 57 LEU n 2 58 GLU n 2 59 SER n 2 60 LEU n 2 61 ASP n 2 62 ASP n 2 63 PHE n 2 64 TYR n 2 65 LEU n 2 66 LEU n 2 67 SER n 2 68 SER n 2 69 GLY n 2 70 LEU n 2 71 VAL n 2 72 LEU n 2 73 LEU n 2 74 GLN n 2 75 THR n 2 76 THR n 2 77 ASN n 2 78 SER n 2 79 VAL n 2 80 TYR n 2 81 ASN n 2 82 LYS n 2 83 THR n 2 84 LEU n 2 85 LEU n 2 86 GLN n 2 87 HIS n 2 88 VAL n 2 89 VAL n 2 90 PRO n 2 91 GLN n 2 92 SER n 2 93 LEU n 2 94 LEU n 2 95 ALA n 2 96 TRP n 2 97 GLN n 2 98 ARG n 2 99 VAL n 2 100 ARG n 2 101 VAL n 2 102 ALA n 2 103 SER n 2 104 MET n 2 105 MET n 2 106 ALA n 2 107 ASN n 2 108 ASN n 2 109 GLY n 2 110 LYS n 2 111 GLN n 2 112 TRP n 2 113 ALA n 2 114 GLU n 2 115 VAL n 2 116 PHE n 2 117 SER n 2 118 LYS n 2 119 TYR n 2 120 ASN n 2 121 SER n 2 122 GLY n 2 123 THR n 2 124 TYR n 2 125 ASN n 2 126 ASN n 2 127 GLN n 2 128 TYR n 2 129 MET n 2 130 VAL n 2 131 LEU n 2 132 ASP n 2 133 LEU n 2 134 LYS n 2 135 LYS n 2 136 VAL n 2 137 ASN n 2 138 LEU n 2 139 ASN n 2 140 HIS n 2 141 SER n 2 142 LEU n 2 143 ASP n 2 144 GLU n 2 145 GLY n 2 146 THR n 2 147 LEU n 2 148 TYR n 2 149 ILE n 2 150 VAL n 2 151 GLU n 2 152 GLN n 2 153 ILE n 2 154 PRO n 2 155 THR n 2 156 TYR n 2 157 VAL n 2 158 GLU n 2 159 TYR n 2 160 SER n 2 161 GLU n 2 162 GLN n 2 163 THR n 2 164 ALA n 2 165 VAL n 2 166 LEU n 2 167 ARG n 2 168 ARG n 2 169 GLY n 2 170 TYR n 2 171 TRP n 2 172 PRO n 2 173 SER n 2 174 TYR n 2 175 ASN n 2 176 ILE n 2 177 PRO n 2 178 PHE n 2 179 HIS n 2 180 GLU n 2 181 LYS n 2 182 VAL n 2 183 TYR n 2 184 ASN n 2 185 TRP n 2 186 SER n 2 187 GLY n 2 188 TYR n 2 189 PRO n 2 190 ILE n 2 191 LEU n 2 192 VAL n 2 193 LYS n 2 194 LYS n 2 195 LEU n 2 196 GLY n 2 197 LEU n 2 198 ASP n 2 199 TYR n 2 200 SER n 2 201 TYR n 2 202 ASP n 2 203 LEU n 2 204 ALA n 2 205 SER n 2 206 ARG n 2 207 ALA n 2 208 LYS n 2 209 ILE n 2 210 PHE n 2 211 ARG n 2 212 ARG n 2 213 ASP n 2 214 GLN n 2 215 GLY n 2 216 LYS n 2 217 VAL n 2 218 THR n 2 219 ASP n 2 220 MET n 2 221 GLU n 2 222 SER n 2 223 MET n 2 224 LYS n 2 225 TYR n 2 226 ILE n 2 227 MET n 2 228 ARG n 2 229 TYR n 2 230 ASN n 2 231 ASN n 2 232 TYR n 2 233 LYS n 2 234 GLN n 2 235 ASP n 2 236 PRO n 2 237 TYR n 2 238 SER n 2 239 LYS n 2 240 GLY n 2 241 ASP n 2 242 PRO n 2 243 CYS n 2 244 ASN n 2 245 THR n 2 246 VAL n 2 247 CYS n 2 248 CYS n 2 249 ARG n 2 250 GLU n 2 251 ASP n 2 252 LEU n 2 253 ASN n 2 254 SER n 2 255 HIS n 2 256 SER n 2 257 PRO n 2 258 SER n 2 259 PRO n 2 260 GLY n 2 261 GLY n 2 262 CYS n 2 263 TYR n 2 264 ASP n 2 265 THR n 2 266 LYS n 2 267 VAL n 2 268 ALA n 2 269 ASP n 2 270 ILE n 2 271 TYR n 2 272 LEU n 2 273 ALA n 2 274 SER n 2 275 LYS n 2 276 TYR n 2 277 LYS n 2 278 ALA n 2 279 TYR n 2 280 ALA n 2 281 ILE n 2 282 SER n 2 283 GLY n 2 284 PRO n 2 285 THR n 2 286 VAL n 2 287 GLN n 2 288 GLY n 2 289 GLY n 2 290 LEU n 2 291 PRO n 2 292 VAL n 2 293 PHE n 2 294 HIS n 2 295 TRP n 2 296 SER n 2 297 ARG n 2 298 PHE n 2 299 ASN n 2 300 LYS n 2 301 THR n 2 302 LEU n 2 303 HIS n 2 304 GLU n 2 305 GLY n 2 306 MET n 2 307 PRO n 2 308 GLU n 2 309 ALA n 2 310 TYR n 2 311 ASN n 2 312 PHE n 2 313 ASP n 2 314 PHE n 2 315 ILE n 2 316 THR n 2 317 MET n 2 318 LYS n 2 319 PRO n 2 320 ILE n 2 321 LEU n # loop_ _entity_src_nat.entity_id _entity_src_nat.pdbx_src_id _entity_src_nat.pdbx_alt_source_flag _entity_src_nat.pdbx_beg_seq_num _entity_src_nat.pdbx_end_seq_num _entity_src_nat.common_name _entity_src_nat.pdbx_organism_scientific _entity_src_nat.pdbx_ncbi_taxonomy_id _entity_src_nat.genus _entity_src_nat.species _entity_src_nat.strain _entity_src_nat.tissue _entity_src_nat.tissue_fraction _entity_src_nat.pdbx_secretion _entity_src_nat.pdbx_fragment _entity_src_nat.pdbx_variant _entity_src_nat.pdbx_cell_line _entity_src_nat.pdbx_atcc _entity_src_nat.pdbx_cellular_location _entity_src_nat.pdbx_organ _entity_src_nat.pdbx_organelle _entity_src_nat.pdbx_cell _entity_src_nat.pdbx_plasmid_name _entity_src_nat.pdbx_plasmid_details _entity_src_nat.details 1 1 sample ? ? BOVINE 'BOS TAURUS' 9913 ? ? ? ? ? ? ? ? ? ? ? KIDNEY ? ? ? ? ? 2 1 sample ? ? BOVINE 'BOS TAURUS' 9913 ? ? ? ? ? ? ? ? ? ? ? KIDNEY ? ? ? ? ? # 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 PLBL1_BOVIN 1 ? ? Q9GL30 ? 2 UNP PLBL1_BOVIN 2 ? ? Q9GL30 ? # 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 4BWC A 1 ? 170 ? Q9GL30 36 ? 205 ? 36 205 2 2 4BWC B 1 ? 321 ? Q9GL30 225 ? 545 ? 225 545 # 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 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 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 OCS 'L-peptide linking' n 'CYSTEINESULFONIC ACID' ? 'C3 H7 N O5 S' 169.156 P4G non-polymer . '1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE' ? 'C8 H18 O3' 162.227 P6G non-polymer . 'HEXAETHYLENE GLYCOL' 'POLYETHYLENE GLYCOL PEG400' 'C12 H26 O7' 282.331 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4BWC _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.8 _exptl_crystal.density_percent_sol 56 _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 7 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M TRIS-CL PH 7, 40% PEG 300, 5% PEG 1000' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date 2007-05-21 _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 0.931 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-3' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-3 _diffrn_source.pdbx_wavelength 0.931 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4BWC _reflns.observed_criterion_sigma_I 2.91 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 46.98 _reflns.d_resolution_high 1.89 _reflns.number_obs 62608 _reflns.number_all ? _reflns.percent_possible_obs 99.8 _reflns.pdbx_Rmerge_I_obs 0.06 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 18.74 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 5.5 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.89 _reflns_shell.d_res_low 2.00 _reflns_shell.percent_possible_all 99.3 _reflns_shell.Rmerge_I_obs 0.62 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.91 _reflns_shell.pdbx_redundancy 5.5 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4BWC _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 59478 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 46.98 _refine.ls_d_res_high 1.89 _refine.ls_percent_reflns_obs 99.80 _refine.ls_R_factor_obs 0.19019 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.18810 _refine.ls_R_factor_R_free 0.23061 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 3127 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.961 _refine.correlation_coeff_Fo_to_Fc_free 0.938 _refine.B_iso_mean 34.379 _refine.aniso_B[1][1] 0.00 _refine.aniso_B[2][2] 0.00 _refine.aniso_B[3][3] 0.00 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.U VALUES REFINED INDIVIDUALLY' _refine.pdbx_starting_model 'PDB ENTRY 3FBX' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.116 _refine.pdbx_overall_ESU_R_Free 0.120 _refine.overall_SU_ML 0.084 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.871 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3996 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 143 _refine_hist.number_atoms_solvent 184 _refine_hist.number_atoms_total 4323 _refine_hist.d_res_high 1.89 _refine_hist.d_res_low 46.98 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.023 0.020 ? 4272 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 2.181 1.983 ? 5795 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.751 5.000 ? 493 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 37.358 23.969 ? 194 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 14.744 15.000 ? 693 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 21.647 15.000 ? 17 'X-RAY DIFFRACTION' ? r_chiral_restr 0.155 0.200 ? 624 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.013 0.021 ? 3215 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.887 _refine_ls_shell.d_res_low 1.936 _refine_ls_shell.number_reflns_R_work 4095 _refine_ls_shell.R_factor_R_work 0.294 _refine_ls_shell.percent_reflns_obs 99.03 _refine_ls_shell.R_factor_R_free 0.349 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 204 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4BWC _struct.title 'X-ray structure of a phospholiapse B like protein 1 from bovine kidneys' _struct.pdbx_descriptor 'PHOSPHOLIPASE B-LIKE 1 (E.C.3.1.1.-)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4BWC _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, GLYCOSYLATION, LYSOSOMAL STORAGE DISORDERS' # 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 3 ? E N N 4 ? F N N 3 ? G N N 3 ? H N N 3 ? I N N 3 ? J N N 3 ? K N N 3 ? L N N 5 ? M N N 6 ? N N N 7 ? O N N 7 ? # _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 SER A 35 ? GLY A 40 ? SER A 70 GLY A 75 1 ? 6 HELX_P HELX_P2 2 SER A 56 ? ILE A 88 ? SER A 91 ILE A 123 1 ? 33 HELX_P HELX_P3 3 LYS A 90 ? TYR A 115 ? LYS A 125 TYR A 150 1 ? 26 HELX_P HELX_P4 4 ASP A 118 ? GLY A 146 ? ASP A 153 GLY A 181 1 ? 29 HELX_P HELX_P5 5 THR A 151 ? ALA A 160 ? THR A 186 ALA A 195 1 ? 10 HELX_P HELX_P6 6 ALA A 160 ? ILE A 168 ? ALA A 195 ILE A 203 1 ? 9 HELX_P HELX_P7 7 ALA B 25 ? MET B 27 ? ALA B 249 MET B 251 5 ? 3 HELX_P HELX_P8 8 ASN B 81 ? GLN B 86 ? ASN B 305 GLN B 310 1 ? 6 HELX_P HELX_P9 9 LEU B 94 ? ALA B 106 ? LEU B 318 ALA B 330 1 ? 13 HELX_P HELX_P10 10 ASN B 108 ? SER B 117 ? ASN B 332 SER B 341 1 ? 10 HELX_P HELX_P11 11 GLN B 162 ? ARG B 168 ? GLN B 386 ARG B 392 1 ? 7 HELX_P HELX_P12 12 HIS B 179 ? SER B 186 ? HIS B 403 SER B 410 1 ? 8 HELX_P HELX_P13 13 GLY B 187 ? GLY B 196 ? GLY B 411 GLY B 420 1 ? 10 HELX_P HELX_P14 14 LEU B 197 ? SER B 200 ? LEU B 421 SER B 424 5 ? 4 HELX_P HELX_P15 15 ALA B 204 ? GLN B 214 ? ALA B 428 GLN B 438 1 ? 11 HELX_P HELX_P16 16 GLY B 215 ? VAL B 217 ? GLY B 439 VAL B 441 5 ? 3 HELX_P HELX_P17 17 ASP B 219 ? ARG B 228 ? ASP B 443 ARG B 452 1 ? 10 HELX_P HELX_P18 18 ASP B 235 ? LYS B 239 ? ASP B 459 LYS B 463 5 ? 5 HELX_P HELX_P19 19 GLU B 250 ? ASN B 253 ? GLU B 474 ASN B 477 5 ? 4 HELX_P HELX_P20 20 ILE B 270 ? LYS B 275 ? ILE B 494 LYS B 499 1 ? 6 HELX_P HELX_P21 21 SER B 296 ? ASN B 299 ? SER B 520 ASN B 523 5 ? 4 # _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 ? ? B CYS 243 SG ? ? ? 1_555 B CYS 248 SG ? ? B CYS 467 B CYS 472 1_555 ? ? ? ? ? ? ? 2.090 ? disulf2 disulf ? ? B CYS 247 SG ? ? ? 1_555 B CYS 262 SG ? ? B CYS 471 B CYS 486 1_555 ? ? ? ? ? ? ? 2.138 ? covale1 covale ? ? A ASN 33 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 68 A NAG 1048 1_555 ? ? ? ? ? ? ? 1.426 ? covale2 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 1048 A NAG 1049 1_555 ? ? ? ? ? ? ? 1.450 ? covale3 covale ? ? B OCS 1 C ? ? ? 1_555 B SER 2 N ? ? B OCS 225 B SER 226 1_555 ? ? ? ? ? ? ? 1.335 ? covale4 covale ? ? B ASN 81 ND2 ? ? ? 1_555 F NAG . C1 ? ? B ASN 305 B NAG 1285 1_555 ? ? ? ? ? ? ? 1.418 ? covale5 covale ? ? B ASN 139 ND2 ? ? ? 1_555 H NAG . C1 ? ? B ASN 363 B NAG 1343 1_555 ? ? ? ? ? ? ? 1.448 ? covale6 covale ? ? B ASN 184 ND2 ? ? ? 1_555 J NAG . C1 ? ? B ASN 408 B NAG 1388 1_555 ? ? ? ? ? ? ? 1.431 ? covale7 covale ? ? B ASN 299 ND2 ? ? ? 1_555 K NAG . C1 ? ? B ASN 523 B NAG 1503 1_555 ? ? ? ? ? ? ? 1.459 ? covale8 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? B NAG 1285 B NAG 1286 1_555 ? ? ? ? ? ? ? 1.457 ? covale9 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? B NAG 1343 B NAG 1345 1_555 ? ? ? ? ? ? ? 1.446 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id ASP _struct_mon_prot_cis.label_seq_id 61 _struct_mon_prot_cis.label_asym_id B _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id ASP _struct_mon_prot_cis.auth_seq_id 285 _struct_mon_prot_cis.auth_asym_id B _struct_mon_prot_cis.pdbx_label_comp_id_2 ASP _struct_mon_prot_cis.pdbx_label_seq_id_2 62 _struct_mon_prot_cis.pdbx_label_asym_id_2 B _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 ASP _struct_mon_prot_cis.pdbx_auth_seq_id_2 286 _struct_mon_prot_cis.pdbx_auth_asym_id_2 B _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 3.20 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 11 ? BA ? 6 ? BB ? 2 ? BC ? 2 ? BD ? 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 AA 2 3 ? anti-parallel AA 3 4 ? anti-parallel AA 4 5 ? parallel AA 5 6 ? anti-parallel AA 6 7 ? anti-parallel AA 7 8 ? anti-parallel AA 8 9 ? anti-parallel AA 9 10 ? anti-parallel AA 10 11 ? anti-parallel BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 4 5 ? anti-parallel BA 5 6 ? anti-parallel BB 1 2 ? anti-parallel BC 1 2 ? anti-parallel BD 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 THR A 15 ? LYS A 19 ? THR A 50 LYS A 54 AA 2 VAL A 2 ? MET A 10 ? VAL A 37 MET A 45 AA 3 ALA A 28 ? ASN A 33 ? ALA A 63 ASN A 68 AA 4 TRP A 41 ? ALA A 48 ? TRP A 76 ALA A 83 AA 5 ARG B 29 ? PHE B 36 ? ARG B 253 PHE B 260 AA 6 ARG B 47 ? SER B 52 ? ARG B 271 SER B 276 AA 7 PHE B 63 ? LEU B 66 ? PHE B 287 LEU B 290 AA 8 LEU B 70 ? THR B 76 ? LEU B 294 THR B 300 AA 9 ASN B 126 ? ASP B 132 ? ASN B 350 ASP B 356 AA 10 LEU B 147 ? ILE B 153 ? LEU B 371 ILE B 377 AA 11 TYR B 156 ? GLU B 161 ? TYR B 380 GLU B 385 BA 1 TYR B 170 ? SER B 173 ? TYR B 394 SER B 397 BA 2 SER B 2 ? VAL B 7 ? SER B 226 VAL B 231 BA 3 ILE B 14 ? SER B 19 ? ILE B 238 SER B 243 BA 4 ASP B 264 ? ASP B 269 ? ASP B 488 ASP B 493 BA 5 ALA B 278 ? SER B 282 ? ALA B 502 SER B 506 BA 6 ILE B 315 ? MET B 317 ? ILE B 539 MET B 541 BB 1 TRP B 21 ? THR B 23 ? TRP B 245 THR B 247 BB 2 GLY B 260 ? CYS B 262 ? GLY B 484 CYS B 486 BC 1 VAL B 136 ? ASN B 137 ? VAL B 360 ASN B 361 BC 2 SER B 141 ? LEU B 142 ? SER B 365 LEU B 366 BD 1 PHE B 293 ? HIS B 294 ? PHE B 517 HIS B 518 BD 2 ALA B 309 ? TYR B 310 ? ALA B 533 TYR B 534 # 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 LYS A 19 ? N LYS A 54 O THR A 6 ? O THR A 41 AA 2 3 N ALA A 7 ? N ALA A 42 O ALA A 28 ? O ALA A 63 AA 3 4 N ASN A 33 ? N ASN A 68 O ILE A 43 ? O ILE A 78 AA 4 5 N GLY A 42 ? N GLY A 77 O ARG B 29 ? O ARG B 253 AA 5 6 N TRP B 34 ? N TRP B 258 O LEU B 48 ? O LEU B 272 AA 6 7 N SER B 51 ? N SER B 275 O PHE B 63 ? O PHE B 287 AA 7 8 N LEU B 66 ? N LEU B 290 O LEU B 70 ? O LEU B 294 AA 8 9 N THR B 75 ? N THR B 299 O GLN B 127 ? O GLN B 351 AA 9 10 N VAL B 130 ? N VAL B 354 O TYR B 148 ? O TYR B 372 AA 10 11 N ILE B 153 ? N ILE B 377 O TYR B 156 ? O TYR B 380 BA 1 2 N SER B 173 ? N SER B 397 O ALA B 3 ? O ALA B 227 BA 2 3 N LYS B 6 ? N LYS B 230 O PHE B 15 ? O PHE B 239 BA 3 4 N HIS B 18 ? N HIS B 242 O LYS B 266 ? O LYS B 490 BA 4 5 N VAL B 267 ? N VAL B 491 O TYR B 279 ? O TYR B 503 BA 5 6 N ALA B 280 ? N ALA B 504 O ILE B 315 ? O ILE B 539 BB 1 2 N TYR B 22 ? N TYR B 246 O GLY B 261 ? O GLY B 485 BC 1 2 N ASN B 137 ? N ASN B 361 O SER B 141 ? O SER B 365 BD 1 2 N PHE B 293 ? N PHE B 517 O TYR B 310 ? O TYR B 534 # 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 ? ? ? ? 3 'BINDING SITE FOR RESIDUE P4G A 1206' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE P6G B 1546' AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CL B 1547' AC4 Software ? ? ? ? 5 'Binding site for Poly-Saccharide residues NAG A1048 through NAG A1049 bound to ASN A 68' AC5 Software ? ? ? ? 6 'Binding site for Poly-Saccharide residues NAG B1285 through NAG B1286 bound to ASN B 305' AC6 Software ? ? ? ? 2 'Binding site for Poly-Saccharide residues NAG B1343 through NAG B1345 bound to ASN B 363' AC7 Software ? ? ? ? 2 'Binding site for Mono-Saccharide NAG B1388 bound to ASN B 408' AC8 Software ? ? ? ? 4 'Binding site for Mono-Saccharide NAG B1503 bound to ASN B 523' # 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 3 TYR A 8 ? TYR A 43 . ? 1_555 ? 2 AC1 3 GLN A 17 ? GLN A 52 . ? 1_555 ? 3 AC1 3 LYS A 19 ? LYS A 54 . ? 1_555 ? 4 AC2 7 LYS A 96 ? LYS A 131 . ? 2_655 ? 5 AC2 7 SER B 67 ? SER B 291 . ? 1_555 ? 6 AC2 7 GLY B 69 ? GLY B 293 . ? 1_555 ? 7 AC2 7 TYR B 271 ? TYR B 495 . ? 1_555 ? 8 AC2 7 ALA B 273 ? ALA B 497 . ? 1_555 ? 9 AC2 7 SER B 274 ? SER B 498 . ? 1_555 ? 10 AC2 7 TYR B 276 ? TYR B 500 . ? 1_555 ? 11 AC3 4 ARG B 168 ? ARG B 392 . ? 1_555 ? 12 AC3 4 ARG B 168 ? ARG B 392 . ? 6_765 ? 13 AC3 4 TYR B 170 ? TYR B 394 . ? 6_765 ? 14 AC3 4 HOH O . ? HOH B 2070 . ? 6_765 ? 15 AC4 5 PHE A 31 ? PHE A 66 . ? 1_555 ? 16 AC4 5 ASN A 33 ? ASN A 68 . ? 1_555 ? 17 AC4 5 SER A 35 ? SER A 70 . ? 1_555 ? 18 AC4 5 THR A 38 ? THR A 73 . ? 1_555 ? 19 AC4 5 THR A 39 ? THR A 74 . ? 1_555 ? 20 AC5 6 ASN B 81 ? ASN B 305 . ? 1_555 ? 21 AC5 6 THR B 83 ? THR B 307 . ? 1_555 ? 22 AC5 6 LEU B 84 ? LEU B 308 . ? 1_555 ? 23 AC5 6 HIS B 87 ? HIS B 311 . ? 1_555 ? 24 AC5 6 ASN B 184 ? ASN B 408 . ? 1_555 ? 25 AC5 6 TRP B 185 ? TRP B 409 . ? 1_555 ? 26 AC6 2 ASN B 139 ? ASN B 363 . ? 1_555 ? 27 AC6 2 HOH O . ? HOH B 2013 . ? 1_555 ? 28 AC7 2 GLU B 180 ? GLU B 404 . ? 1_555 ? 29 AC7 2 ASN B 184 ? ASN B 408 . ? 1_555 ? 30 AC8 4 LYS A 37 ? LYS A 72 . ? 4_555 ? 31 AC8 4 ASN B 299 ? ASN B 523 . ? 1_555 ? 32 AC8 4 ASN B 311 ? ASN B 535 . ? 4_555 ? 33 AC8 4 PHE B 312 ? PHE B 536 . ? 4_555 ? # _database_PDB_matrix.entry_id 4BWC _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 4BWC _atom_sites.fract_transf_matrix[1][1] 0.010270 _atom_sites.fract_transf_matrix[1][2] 0.005929 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.011859 _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] 0.007095 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CL N O S # 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 . GLY A 1 1 ? 24.253 42.686 13.675 1.00 50.39 ? 36 GLY A N 1 ATOM 2 C CA . GLY A 1 1 ? 23.790 42.129 14.976 1.00 48.01 ? 36 GLY A CA 1 ATOM 3 C C . GLY A 1 1 ? 24.540 40.860 15.329 1.00 53.20 ? 36 GLY A C 1 ATOM 4 O O . GLY A 1 1 ? 25.321 40.335 14.536 1.00 52.17 ? 36 GLY A O 1 ATOM 5 N N . VAL A 1 2 ? 24.268 40.361 16.520 1.00 48.03 ? 37 VAL A N 1 ATOM 6 C CA . VAL A 1 2 ? 24.891 39.182 17.086 1.00 45.88 ? 37 VAL A CA 1 ATOM 7 C C . VAL A 1 2 ? 24.114 37.882 16.807 1.00 50.94 ? 37 VAL A C 1 ATOM 8 O O . VAL A 1 2 ? 22.925 37.804 17.104 1.00 50.44 ? 37 VAL A O 1 ATOM 9 C CB . VAL A 1 2 ? 24.989 39.414 18.613 1.00 42.12 ? 37 VAL A CB 1 ATOM 10 C CG1 . VAL A 1 2 ? 25.882 38.381 19.267 1.00 45.76 ? 37 VAL A CG1 1 ATOM 11 C CG2 . VAL A 1 2 ? 25.482 40.831 18.877 1.00 38.54 ? 37 VAL A CG2 1 ATOM 12 N N . TYR A 1 3 ? 24.783 36.871 16.240 1.00 43.59 ? 38 TYR A N 1 ATOM 13 C CA . TYR A 1 3 ? 24.219 35.534 16.037 1.00 45.18 ? 38 TYR A CA 1 ATOM 14 C C . TYR A 1 3 ? 24.803 34.615 17.066 1.00 52.14 ? 38 TYR A C 1 ATOM 15 O O . TYR A 1 3 ? 26.043 34.480 17.090 1.00 47.94 ? 38 TYR A O 1 ATOM 16 C CB . TYR A 1 3 ? 24.577 34.980 14.619 1.00 45.23 ? 38 TYR A CB 1 ATOM 17 C CG . TYR A 1 3 ? 24.069 35.917 13.587 1.00 58.19 ? 38 TYR A CG 1 ATOM 18 C CD1 . TYR A 1 3 ? 24.798 37.066 13.241 1.00 50.15 ? 38 TYR A CD1 1 ATOM 19 C CD2 . TYR A 1 3 ? 22.774 35.748 13.049 1.00 59.14 ? 38 TYR A CD2 1 ATOM 20 C CE1 . TYR A 1 3 ? 24.300 37.970 12.332 1.00 52.38 ? 38 TYR A CE1 1 ATOM 21 C CE2 . TYR A 1 3 ? 22.259 36.669 12.154 1.00 58.51 ? 38 TYR A CE2 1 ATOM 22 C CZ . TYR A 1 3 ? 23.025 37.760 11.801 1.00 60.16 ? 38 TYR A CZ 1 ATOM 23 O OH . TYR A 1 3 ? 22.511 38.668 10.926 1.00 61.39 ? 38 TYR A OH 1 ATOM 24 N N . TYR A 1 4 ? 23.965 33.973 17.903 1.00 41.56 ? 39 TYR A N 1 ATOM 25 C CA . TYR A 1 4 ? 24.444 32.946 18.834 1.00 41.12 ? 39 TYR A CA 1 ATOM 26 C C . TYR A 1 4 ? 24.261 31.602 18.299 1.00 41.17 ? 39 TYR A C 1 ATOM 27 O O . TYR A 1 4 ? 23.303 31.369 17.578 1.00 47.95 ? 39 TYR A O 1 ATOM 28 C CB . TYR A 1 4 ? 23.681 33.027 20.159 1.00 46.55 ? 39 TYR A CB 1 ATOM 29 C CG . TYR A 1 4 ? 23.874 34.360 20.777 1.00 48.00 ? 39 TYR A CG 1 ATOM 30 C CD1 . TYR A 1 4 ? 23.142 35.438 20.335 1.00 46.29 ? 39 TYR A CD1 1 ATOM 31 C CD2 . TYR A 1 4 ? 24.858 34.553 21.747 1.00 44.21 ? 39 TYR A CD2 1 ATOM 32 C CE1 . TYR A 1 4 ? 23.329 36.679 20.870 1.00 45.56 ? 39 TYR A CE1 1 ATOM 33 C CE2 . TYR A 1 4 ? 25.065 35.806 22.287 1.00 50.01 ? 39 TYR A CE2 1 ATOM 34 C CZ . TYR A 1 4 ? 24.278 36.855 21.849 1.00 48.59 ? 39 TYR A CZ 1 ATOM 35 O OH . TYR A 1 4 ? 24.469 38.127 22.357 1.00 51.48 ? 39 TYR A OH 1 ATOM 36 N N . ALA A 1 5 ? 25.120 30.661 18.688 1.00 39.95 ? 40 ALA A N 1 ATOM 37 C CA . ALA A 1 5 ? 24.923 29.314 18.265 1.00 39.49 ? 40 ALA A CA 1 ATOM 38 C C . ALA A 1 5 ? 25.599 28.324 19.192 1.00 40.61 ? 40 ALA A C 1 ATOM 39 O O . ALA A 1 5 ? 26.535 28.663 19.913 1.00 40.56 ? 40 ALA A O 1 ATOM 40 C CB . ALA A 1 5 ? 25.408 29.135 16.814 1.00 41.83 ? 40 ALA A CB 1 ATOM 41 N N . THR A 1 6 ? 25.187 27.078 19.096 1.00 34.22 ? 41 THR A N 1 ATOM 42 C CA . THR A 1 6 ? 25.685 26.037 19.953 1.00 34.50 ? 41 THR A CA 1 ATOM 43 C C . THR A 1 6 ? 25.773 24.765 19.194 1.00 40.63 ? 41 THR A C 1 ATOM 44 O O . THR A 1 6 ? 24.844 24.375 18.467 1.00 41.41 ? 41 THR A O 1 ATOM 45 C CB . THR A 1 6 ? 24.761 25.875 21.242 1.00 34.57 ? 41 THR A CB 1 ATOM 46 O OG1 . THR A 1 6 ? 24.555 27.144 21.875 1.00 39.70 ? 41 THR A OG1 1 ATOM 47 C CG2 . THR A 1 6 ? 25.320 25.016 22.220 1.00 37.08 ? 41 THR A CG2 1 ATOM 48 N N . ALA A 1 7 ? 26.890 24.079 19.359 1.00 36.97 ? 42 ALA A N 1 ATOM 49 C CA . ALA A 1 7 ? 27.101 22.807 18.742 1.00 41.47 ? 42 ALA A CA 1 ATOM 50 C C . ALA A 1 7 ? 27.004 21.711 19.791 1.00 49.70 ? 42 ALA A C 1 ATOM 51 O O . ALA A 1 7 ? 27.446 21.909 20.920 1.00 50.78 ? 42 ALA A O 1 ATOM 52 C CB . ALA A 1 7 ? 28.499 22.763 18.133 1.00 43.00 ? 42 ALA A CB 1 ATOM 53 N N . TYR A 1 8 ? 26.500 20.546 19.385 1.00 49.47 ? 43 TYR A N 1 ATOM 54 C CA . TYR A 1 8 ? 26.388 19.345 20.242 1.00 48.91 ? 43 TYR A CA 1 ATOM 55 C C . TYR A 1 8 ? 27.013 18.170 19.556 1.00 41.33 ? 43 TYR A C 1 ATOM 56 O O . TYR A 1 8 ? 26.619 17.786 18.455 1.00 48.96 ? 43 TYR A O 1 ATOM 57 C CB . TYR A 1 8 ? 24.908 18.990 20.549 1.00 41.89 ? 43 TYR A CB 1 ATOM 58 C CG . TYR A 1 8 ? 24.142 20.169 21.099 1.00 41.87 ? 43 TYR A CG 1 ATOM 59 C CD1 . TYR A 1 8 ? 23.580 21.095 20.256 1.00 40.30 ? 43 TYR A CD1 1 ATOM 60 C CD2 . TYR A 1 8 ? 24.026 20.364 22.464 1.00 38.61 ? 43 TYR A CD2 1 ATOM 61 C CE1 . TYR A 1 8 ? 22.933 22.185 20.760 1.00 34.94 ? 43 TYR A CE1 1 ATOM 62 C CE2 . TYR A 1 8 ? 23.363 21.443 22.974 1.00 36.62 ? 43 TYR A CE2 1 ATOM 63 C CZ . TYR A 1 8 ? 22.812 22.340 22.136 1.00 37.07 ? 43 TYR A CZ 1 ATOM 64 O OH . TYR A 1 8 ? 22.133 23.446 22.656 1.00 40.33 ? 43 TYR A OH 1 ATOM 65 N N . TRP A 1 9 ? 27.953 17.542 20.221 1.00 38.59 ? 44 TRP A N 1 ATOM 66 C CA . TRP A 1 9 ? 28.470 16.284 19.714 1.00 41.10 ? 44 TRP A CA 1 ATOM 67 C C . TRP A 1 9 ? 27.459 15.200 20.029 1.00 50.24 ? 44 TRP A C 1 ATOM 68 O O . TRP A 1 9 ? 27.018 15.070 21.173 1.00 48.21 ? 44 TRP A O 1 ATOM 69 C CB . TRP A 1 9 ? 29.818 15.992 20.348 1.00 36.92 ? 44 TRP A CB 1 ATOM 70 C CG . TRP A 1 9 ? 30.493 14.709 19.968 1.00 38.02 ? 44 TRP A CG 1 ATOM 71 C CD1 . TRP A 1 9 ? 30.789 13.652 20.820 1.00 39.61 ? 44 TRP A CD1 1 ATOM 72 C CD2 . TRP A 1 9 ? 31.031 14.310 18.666 1.00 42.23 ? 44 TRP A CD2 1 ATOM 73 N NE1 . TRP A 1 9 ? 31.424 12.658 20.154 1.00 43.31 ? 44 TRP A NE1 1 ATOM 74 C CE2 . TRP A 1 9 ? 31.600 12.976 18.858 1.00 40.28 ? 44 TRP A CE2 1 ATOM 75 C CE3 . TRP A 1 9 ? 31.095 14.904 17.388 1.00 41.63 ? 44 TRP A CE3 1 ATOM 76 C CZ2 . TRP A 1 9 ? 32.201 12.270 17.826 1.00 42.49 ? 44 TRP A CZ2 1 ATOM 77 C CZ3 . TRP A 1 9 ? 31.705 14.183 16.359 1.00 41.30 ? 44 TRP A CZ3 1 ATOM 78 C CH2 . TRP A 1 9 ? 32.256 12.916 16.566 1.00 46.72 ? 44 TRP A CH2 1 ATOM 79 N N . MET A 1 10 ? 27.090 14.431 19.005 1.00 57.71 ? 45 MET A N 1 ATOM 80 C CA . MET A 1 10 ? 26.221 13.243 19.148 1.00 58.72 ? 45 MET A CA 1 ATOM 81 C C . MET A 1 10 ? 27.168 12.054 19.040 1.00 52.15 ? 45 MET A C 1 ATOM 82 O O . MET A 1 10 ? 27.509 11.665 17.927 1.00 51.73 ? 45 MET A O 1 ATOM 83 C CB . MET A 1 10 ? 25.168 13.139 18.012 1.00 59.67 ? 45 MET A CB 1 ATOM 84 C CG . MET A 1 10 ? 24.405 14.394 17.568 1.00 66.92 ? 45 MET A CG 1 ATOM 85 S SD . MET A 1 10 ? 23.569 15.256 18.910 1.00 80.48 ? 45 MET A SD 1 ATOM 86 C CE . MET A 1 10 ? 22.084 15.864 18.105 1.00 78.29 ? 45 MET A CE 1 ATOM 87 N N . PRO A 1 11 ? 27.564 11.448 20.186 1.00 55.31 ? 46 PRO A N 1 ATOM 88 C CA . PRO A 1 11 ? 28.693 10.524 20.172 1.00 55.31 ? 46 PRO A CA 1 ATOM 89 C C . PRO A 1 11 ? 28.436 9.328 19.266 1.00 66.31 ? 46 PRO A C 1 ATOM 90 O O . PRO A 1 11 ? 29.383 8.835 18.643 1.00 71.11 ? 46 PRO A O 1 ATOM 91 C CB . PRO A 1 11 ? 28.825 10.081 21.651 1.00 48.60 ? 46 PRO A CB 1 ATOM 92 C CG . PRO A 1 11 ? 28.017 11.056 22.425 1.00 55.33 ? 46 PRO A CG 1 ATOM 93 C CD . PRO A 1 11 ? 26.908 11.471 21.509 1.00 52.96 ? 46 PRO A CD 1 ATOM 94 N N . THR A 1 12 ? 27.172 8.880 19.185 1.00 68.50 ? 47 THR A N 1 ATOM 95 C CA . THR A 1 12 ? 26.834 7.670 18.407 1.00 68.68 ? 47 THR A CA 1 ATOM 96 C C . THR A 1 12 ? 26.891 7.880 16.896 1.00 67.35 ? 47 THR A C 1 ATOM 97 O O . THR A 1 12 ? 27.627 7.161 16.207 1.00 73.02 ? 47 THR A O 1 ATOM 98 C CB . THR A 1 12 ? 25.495 7.054 18.821 1.00 71.23 ? 47 THR A CB 1 ATOM 99 O OG1 . THR A 1 12 ? 25.560 6.727 20.211 1.00 74.76 ? 47 THR A OG1 1 ATOM 100 C CG2 . THR A 1 12 ? 25.183 5.784 17.983 1.00 65.86 ? 47 THR A CG2 1 ATOM 101 N N . GLU A 1 13 ? 26.153 8.869 16.390 1.00 65.71 ? 48 GLU A N 1 ATOM 102 C CA . GLU A 1 13 ? 26.225 9.243 14.974 1.00 70.76 ? 48 GLU A CA 1 ATOM 103 C C . GLU A 1 13 ? 27.602 9.818 14.592 1.00 71.61 ? 48 GLU A C 1 ATOM 104 O O . GLU A 1 13 ? 27.969 9.821 13.415 1.00 73.72 ? 48 GLU A O 1 ATOM 105 C CB . GLU A 1 13 ? 25.101 10.214 14.608 1.00 74.70 ? 48 GLU A CB 1 ATOM 106 C CG . GLU A 1 13 ? 23.752 9.802 15.175 1.00 80.49 ? 48 GLU A CG 1 ATOM 107 C CD . GLU A 1 13 ? 23.609 10.180 16.642 1.00 94.65 ? 48 GLU A CD 1 ATOM 108 O OE1 . GLU A 1 13 ? 24.075 9.424 17.524 1.00 95.44 ? 48 GLU A OE1 1 ATOM 109 O OE2 . GLU A 1 13 ? 23.031 11.252 16.917 1.00 103.77 ? 48 GLU A OE2 1 ATOM 110 N N . LYS A 1 14 ? 28.356 10.273 15.599 1.00 67.83 ? 49 LYS A N 1 ATOM 111 C CA . LYS A 1 14 ? 29.665 10.915 15.423 1.00 60.51 ? 49 LYS A CA 1 ATOM 112 C C . LYS A 1 14 ? 29.501 12.140 14.560 1.00 54.20 ? 49 LYS A C 1 ATOM 113 O O . LYS A 1 14 ? 30.231 12.338 13.618 1.00 52.24 ? 49 LYS A O 1 ATOM 114 C CB . LYS A 1 14 ? 30.687 9.959 14.796 1.00 61.89 ? 49 LYS A CB 1 ATOM 115 C CG . LYS A 1 14 ? 31.294 9.001 15.779 1.00 65.35 ? 49 LYS A CG 1 ATOM 116 C CD . LYS A 1 14 ? 32.232 8.067 15.047 1.00 69.44 ? 49 LYS A CD 1 ATOM 117 C CE . LYS A 1 14 ? 32.622 6.928 15.964 1.00 69.22 ? 49 LYS A CE 1 ATOM 118 N NZ . LYS A 1 14 ? 33.815 6.216 15.443 1.00 78.67 ? 49 LYS A NZ 1 ATOM 119 N N . THR A 1 15 ? 28.503 12.949 14.870 1.00 55.86 ? 50 THR A N 1 ATOM 120 C CA . THR A 1 15 ? 28.217 14.112 14.076 1.00 55.02 ? 50 THR A CA 1 ATOM 121 C C . THR A 1 15 ? 27.924 15.215 15.068 1.00 52.72 ? 50 THR A C 1 ATOM 122 O O . THR A 1 15 ? 27.620 14.952 16.225 1.00 51.18 ? 50 THR A O 1 ATOM 123 C CB . THR A 1 15 ? 26.985 13.878 13.175 1.00 63.28 ? 50 THR A CB 1 ATOM 124 O OG1 . THR A 1 15 ? 25.882 13.440 13.984 1.00 57.98 ? 50 THR A OG1 1 ATOM 125 C CG2 . THR A 1 15 ? 27.287 12.804 12.088 1.00 64.65 ? 50 THR A CG2 1 ATOM 126 N N . ILE A 1 16 ? 28.033 16.451 14.613 1.00 45.64 ? 51 ILE A N 1 ATOM 127 C CA . ILE A 1 16 ? 27.673 17.585 15.404 1.00 46.84 ? 51 ILE A CA 1 ATOM 128 C C . ILE A 1 16 ? 26.315 18.041 14.925 1.00 49.16 ? 51 ILE A C 1 ATOM 129 O O . ILE A 1 16 ? 26.103 18.105 13.722 1.00 51.03 ? 51 ILE A O 1 ATOM 130 C CB . ILE A 1 16 ? 28.652 18.755 15.073 1.00 44.60 ? 51 ILE A CB 1 ATOM 131 C CG1 . ILE A 1 16 ? 30.085 18.489 15.600 1.00 41.84 ? 51 ILE A CG1 1 ATOM 132 C CG2 . ILE A 1 16 ? 28.049 20.087 15.498 1.00 42.18 ? 51 ILE A CG2 1 ATOM 133 C CD1 . ILE A 1 16 ? 30.291 18.742 17.092 1.00 40.55 ? 51 ILE A CD1 1 ATOM 134 N N . GLN A 1 17 ? 25.427 18.453 15.810 1.00 48.52 ? 52 GLN A N 1 ATOM 135 C CA . GLN A 1 17 ? 24.280 19.204 15.353 1.00 52.62 ? 52 GLN A CA 1 ATOM 136 C C . GLN A 1 17 ? 24.399 20.580 15.962 1.00 53.24 ? 52 GLN A C 1 ATOM 137 O O . GLN A 1 17 ? 24.885 20.728 17.102 1.00 53.80 ? 52 GLN A O 1 ATOM 138 C CB . GLN A 1 17 ? 22.948 18.492 15.757 1.00 62.30 ? 52 GLN A CB 1 ATOM 139 C CG . GLN A 1 17 ? 21.690 19.382 15.793 1.00 61.88 ? 52 GLN A CG 1 ATOM 140 C CD . GLN A 1 17 ? 20.515 18.829 16.647 1.00 79.01 ? 52 GLN A CD 1 ATOM 141 O OE1 . GLN A 1 17 ? 20.228 17.622 16.664 1.00 76.16 ? 52 GLN A OE1 1 ATOM 142 N NE2 . GLN A 1 17 ? 19.821 19.732 17.351 1.00 73.40 ? 52 GLN A NE2 1 ATOM 143 N N . VAL A 1 18 ? 23.925 21.592 15.238 1.00 47.22 ? 53 VAL A N 1 ATOM 144 C CA . VAL A 1 18 ? 23.971 22.956 15.711 1.00 43.87 ? 53 VAL A CA 1 ATOM 145 C C . VAL A 1 18 ? 22.602 23.533 15.922 1.00 49.38 ? 53 VAL A C 1 ATOM 146 O O . VAL A 1 18 ? 21.712 23.182 15.178 1.00 58.51 ? 53 VAL A O 1 ATOM 147 C CB . VAL A 1 18 ? 24.699 23.877 14.698 1.00 51.74 ? 53 VAL A CB 1 ATOM 148 C CG1 . VAL A 1 18 ? 24.471 25.337 15.036 1.00 49.62 ? 53 VAL A CG1 1 ATOM 149 C CG2 . VAL A 1 18 ? 26.174 23.637 14.766 1.00 43.53 ? 53 VAL A CG2 1 ATOM 150 N N . LYS A 1 19 ? 22.432 24.432 16.905 1.00 43.91 ? 54 LYS A N 1 ATOM 151 C CA . LYS A 1 19 ? 21.185 25.147 17.117 1.00 48.05 ? 54 LYS A CA 1 ATOM 152 C C . LYS A 1 19 ? 21.552 26.583 17.263 1.00 49.09 ? 54 LYS A C 1 ATOM 153 O O . LYS A 1 19 ? 22.671 26.909 17.728 1.00 48.58 ? 54 LYS A O 1 ATOM 154 C CB . LYS A 1 19 ? 20.434 24.663 18.386 1.00 47.88 ? 54 LYS A CB 1 ATOM 155 C CG . LYS A 1 19 ? 19.931 23.214 18.326 1.00 50.64 ? 54 LYS A CG 1 ATOM 156 C CD . LYS A 1 19 ? 19.194 22.876 19.618 1.00 57.11 ? 54 LYS A CD 1 ATOM 157 C CE . LYS A 1 19 ? 18.077 21.885 19.388 1.00 57.80 ? 54 LYS A CE 1 ATOM 158 N NZ . LYS A 1 19 ? 17.470 21.441 20.660 1.00 63.04 ? 54 LYS A NZ 1 ATOM 159 N N . ASN A 1 20 ? 20.623 27.444 16.877 1.00 42.98 ? 55 ASN A N 1 ATOM 160 C CA . ASN A 1 20 ? 20.842 28.873 16.940 1.00 45.10 ? 55 ASN A CA 1 ATOM 161 C C . ASN A 1 20 ? 20.469 29.557 18.231 1.00 45.72 ? 55 ASN A C 1 ATOM 162 O O . ASN A 1 20 ? 19.919 30.663 18.215 1.00 49.24 ? 55 ASN A O 1 ATOM 163 C CB . ASN A 1 20 ? 20.184 29.608 15.793 1.00 48.04 ? 55 ASN A CB 1 ATOM 164 C CG . ASN A 1 20 ? 20.638 29.087 14.463 1.00 57.53 ? 55 ASN A CG 1 ATOM 165 O OD1 . ASN A 1 20 ? 21.825 29.126 14.127 1.00 59.62 ? 55 ASN A OD1 1 ATOM 166 N ND2 . ASN A 1 20 ? 19.697 28.570 13.695 1.00 55.69 ? 55 ASN A ND2 1 ATOM 167 N N . VAL A 1 21 ? 20.884 28.957 19.336 1.00 46.56 ? 56 VAL A N 1 ATOM 168 C CA . VAL A 1 21 ? 20.780 29.599 20.655 1.00 50.11 ? 56 VAL A CA 1 ATOM 169 C C . VAL A 1 21 ? 22.146 29.559 21.400 1.00 51.33 ? 56 VAL A C 1 ATOM 170 O O . VAL A 1 21 ? 23.041 28.777 21.042 1.00 44.38 ? 56 VAL A O 1 ATOM 171 C CB . VAL A 1 21 ? 19.720 28.894 21.503 1.00 48.42 ? 56 VAL A CB 1 ATOM 172 C CG1 . VAL A 1 21 ? 18.314 29.226 20.949 1.00 48.06 ? 56 VAL A CG1 1 ATOM 173 C CG2 . VAL A 1 21 ? 20.009 27.399 21.513 1.00 52.22 ? 56 VAL A CG2 1 ATOM 174 N N . LEU A 1 22 ? 22.302 30.409 22.405 1.00 49.08 ? 57 LEU A N 1 ATOM 175 C CA . LEU A 1 22 ? 23.417 30.253 23.339 1.00 48.49 ? 57 LEU A CA 1 ATOM 176 C C . LEU A 1 22 ? 23.052 29.313 24.478 1.00 48.10 ? 57 LEU A C 1 ATOM 177 O O . LEU A 1 22 ? 22.360 29.711 25.396 1.00 48.67 ? 57 LEU A O 1 ATOM 178 C CB . LEU A 1 22 ? 23.821 31.625 23.880 1.00 47.27 ? 57 LEU A CB 1 ATOM 179 C CG . LEU A 1 22 ? 25.034 31.629 24.834 1.00 48.26 ? 57 LEU A CG 1 ATOM 180 C CD1 . LEU A 1 22 ? 26.332 31.581 24.051 1.00 41.80 ? 57 LEU A CD1 1 ATOM 181 C CD2 . LEU A 1 22 ? 24.903 32.914 25.629 1.00 48.79 ? 57 LEU A CD2 1 ATOM 182 N N . ASP A 1 23 ? 23.546 28.089 24.438 1.00 44.61 ? 58 ASP A N 1 ATOM 183 C CA . ASP A 1 23 ? 23.297 27.139 25.498 1.00 48.31 ? 58 ASP A CA 1 ATOM 184 C C . ASP A 1 23 ? 24.604 26.597 26.189 1.00 51.79 ? 58 ASP A C 1 ATOM 185 O O . ASP A 1 23 ? 25.317 25.700 25.665 1.00 43.52 ? 58 ASP A O 1 ATOM 186 C CB . ASP A 1 23 ? 22.415 25.998 24.953 1.00 51.11 ? 58 ASP A CB 1 ATOM 187 C CG . ASP A 1 23 ? 22.354 24.796 25.874 1.00 51.34 ? 58 ASP A CG 1 ATOM 188 O OD1 . ASP A 1 23 ? 22.590 24.947 27.088 1.00 56.72 ? 58 ASP A OD1 1 ATOM 189 O OD2 . ASP A 1 23 ? 22.094 23.691 25.380 1.00 51.65 ? 58 ASP A OD2 1 ATOM 190 N N . ARG A 1 24 ? 24.857 27.080 27.408 1.00 49.57 ? 59 ARG A N 1 ATOM 191 C CA . ARG A 1 24 ? 26.070 26.711 28.136 1.00 41.78 ? 59 ARG A CA 1 ATOM 192 C C . ARG A 1 24 ? 26.272 25.230 28.433 1.00 48.22 ? 59 ARG A C 1 ATOM 193 O O . ARG A 1 24 ? 27.382 24.793 28.827 1.00 44.94 ? 59 ARG A O 1 ATOM 194 C CB . ARG A 1 24 ? 26.197 27.582 29.369 1.00 49.54 ? 59 ARG A CB 1 ATOM 195 C CG . ARG A 1 24 ? 25.861 29.040 29.102 1.00 46.98 ? 59 ARG A CG 1 ATOM 196 C CD . ARG A 1 24 ? 26.819 29.881 29.893 1.00 49.12 ? 59 ARG A CD 1 ATOM 197 N NE . ARG A 1 24 ? 26.627 31.305 29.656 1.00 54.41 ? 59 ARG A NE 1 ATOM 198 C CZ . ARG A 1 24 ? 27.636 32.173 29.630 1.00 55.74 ? 59 ARG A CZ 1 ATOM 199 N NH1 . ARG A 1 24 ? 28.887 31.742 29.810 1.00 50.67 ? 59 ARG A NH1 1 ATOM 200 N NH2 . ARG A 1 24 ? 27.402 33.461 29.417 1.00 54.06 ? 59 ARG A NH2 1 ATOM 201 N N . LYS A 1 25 ? 25.266 24.397 28.191 1.00 43.80 ? 60 LYS A N 1 ATOM 202 C CA . LYS A 1 25 ? 25.520 22.941 28.366 1.00 41.15 ? 60 LYS A CA 1 ATOM 203 C C . LYS A 1 25 ? 26.057 22.365 27.105 1.00 38.11 ? 60 LYS A C 1 ATOM 204 O O . LYS A 1 25 ? 26.471 21.178 27.089 1.00 43.34 ? 60 LYS A O 1 ATOM 205 C CB . LYS A 1 25 ? 24.219 22.133 28.787 1.00 48.55 ? 60 LYS A CB 1 ATOM 206 C CG . LYS A 1 25 ? 23.302 22.855 29.762 1.00 52.74 ? 60 LYS A CG 1 ATOM 207 C CD . LYS A 1 25 ? 23.925 22.871 31.147 1.00 61.03 ? 60 LYS A CD 1 ATOM 208 C CE . LYS A 1 25 ? 22.931 23.279 32.223 1.00 65.03 ? 60 LYS A CE 1 ATOM 209 N NZ . LYS A 1 25 ? 23.689 23.746 33.427 1.00 74.18 ? 60 LYS A NZ 1 ATOM 210 N N . GLY A 1 26 ? 26.082 23.192 26.039 1.00 44.96 ? 61 GLY A N 1 ATOM 211 C CA . GLY A 1 26 ? 26.539 22.730 24.714 1.00 46.36 ? 61 GLY A CA 1 ATOM 212 C C . GLY A 1 26 ? 28.036 22.424 24.663 1.00 45.82 ? 61 GLY A C 1 ATOM 213 O O . GLY A 1 26 ? 28.806 22.877 25.537 1.00 41.35 ? 61 GLY A O 1 ATOM 214 N N . ASP A 1 27 ? 28.444 21.676 23.647 1.00 40.91 ? 62 ASP A N 1 ATOM 215 C CA . ASP A 1 27 ? 29.839 21.305 23.455 1.00 40.68 ? 62 ASP A CA 1 ATOM 216 C C . ASP A 1 27 ? 30.798 22.411 22.879 1.00 41.26 ? 62 ASP A C 1 ATOM 217 O O . ASP A 1 27 ? 32.028 22.329 23.047 1.00 45.56 ? 62 ASP A O 1 ATOM 218 C CB . ASP A 1 27 ? 29.905 20.037 22.627 1.00 42.58 ? 62 ASP A CB 1 ATOM 219 C CG . ASP A 1 27 ? 29.363 18.828 23.384 1.00 53.17 ? 62 ASP A CG 1 ATOM 220 O OD1 . ASP A 1 27 ? 29.687 18.712 24.591 1.00 48.89 ? 62 ASP A OD1 1 ATOM 221 O OD2 . ASP A 1 27 ? 28.665 17.964 22.779 1.00 44.71 ? 62 ASP A OD2 1 ATOM 222 N N . ALA A 1 28 ? 30.233 23.414 22.220 1.00 41.18 ? 63 ALA A N 1 ATOM 223 C CA . ALA A 1 28 ? 30.969 24.608 21.784 1.00 39.46 ? 63 ALA A CA 1 ATOM 224 C C . ALA A 1 28 ? 29.868 25.581 21.623 1.00 37.74 ? 63 ALA A C 1 ATOM 225 O O . ALA A 1 28 ? 28.822 25.269 21.014 1.00 40.85 ? 63 ALA A O 1 ATOM 226 C CB . ALA A 1 28 ? 31.681 24.352 20.436 1.00 35.14 ? 63 ALA A CB 1 ATOM 227 N N . TYR A 1 29 ? 29.997 26.739 22.226 1.00 35.91 ? 64 TYR A N 1 ATOM 228 C CA . TYR A 1 29 ? 28.922 27.686 22.109 1.00 34.95 ? 64 TYR A CA 1 ATOM 229 C C . TYR A 1 29 ? 29.527 29.034 22.027 1.00 40.29 ? 64 TYR A C 1 ATOM 230 O O . TYR A 1 29 ? 30.701 29.248 22.450 1.00 38.82 ? 64 TYR A O 1 ATOM 231 C CB . TYR A 1 29 ? 27.956 27.609 23.316 1.00 37.13 ? 64 TYR A CB 1 ATOM 232 C CG . TYR A 1 29 ? 28.602 27.774 24.711 1.00 38.23 ? 64 TYR A CG 1 ATOM 233 C CD1 . TYR A 1 29 ? 28.829 29.034 25.253 1.00 35.63 ? 64 TYR A CD1 1 ATOM 234 C CD2 . TYR A 1 29 ? 28.973 26.650 25.451 1.00 41.63 ? 64 TYR A CD2 1 ATOM 235 C CE1 . TYR A 1 29 ? 29.388 29.165 26.518 1.00 41.42 ? 64 TYR A CE1 1 ATOM 236 C CE2 . TYR A 1 29 ? 29.532 26.766 26.720 1.00 43.63 ? 64 TYR A CE2 1 ATOM 237 C CZ . TYR A 1 29 ? 29.735 28.012 27.238 1.00 44.31 ? 64 TYR A CZ 1 ATOM 238 O OH . TYR A 1 29 ? 30.289 28.081 28.491 1.00 46.14 ? 64 TYR A OH 1 ATOM 239 N N . GLY A 1 30 ? 28.772 29.974 21.499 1.00 35.16 ? 65 GLY A N 1 ATOM 240 C CA . GLY A 1 30 ? 29.303 31.317 21.466 1.00 32.70 ? 65 GLY A CA 1 ATOM 241 C C . GLY A 1 30 ? 28.578 32.098 20.401 1.00 42.59 ? 65 GLY A C 1 ATOM 242 O O . GLY A 1 30 ? 27.456 31.767 20.060 1.00 40.46 ? 65 GLY A O 1 ATOM 243 N N . PHE A 1 31 ? 29.209 33.142 19.884 1.00 33.86 ? 66 PHE A N 1 ATOM 244 C CA . PHE A 1 31 ? 28.554 34.077 18.987 1.00 37.19 ? 66 PHE A CA 1 ATOM 245 C C . PHE A 1 31 ? 29.467 34.609 17.888 1.00 39.14 ? 66 PHE A C 1 ATOM 246 O O . PHE A 1 31 ? 30.723 34.521 17.967 1.00 35.78 ? 66 PHE A O 1 ATOM 247 C CB . PHE A 1 31 ? 27.922 35.291 19.744 1.00 34.22 ? 66 PHE A CB 1 ATOM 248 C CG . PHE A 1 31 ? 28.900 36.114 20.559 1.00 37.46 ? 66 PHE A CG 1 ATOM 249 C CD1 . PHE A 1 31 ? 29.151 35.800 21.904 1.00 40.47 ? 66 PHE A CD1 1 ATOM 250 C CD2 . PHE A 1 31 ? 29.523 37.226 20.017 1.00 35.19 ? 66 PHE A CD2 1 ATOM 251 C CE1 . PHE A 1 31 ? 30.068 36.549 22.663 1.00 41.32 ? 66 PHE A CE1 1 ATOM 252 C CE2 . PHE A 1 31 ? 30.439 37.988 20.765 1.00 39.11 ? 66 PHE A CE2 1 ATOM 253 C CZ . PHE A 1 31 ? 30.690 37.676 22.107 1.00 35.65 ? 66 PHE A CZ 1 ATOM 254 N N . TYR A 1 32 ? 28.807 35.133 16.854 1.00 40.39 ? 67 TYR A N 1 ATOM 255 C CA . TYR A 1 32 ? 29.397 35.991 15.862 1.00 34.48 ? 67 TYR A CA 1 ATOM 256 C C . TYR A 1 32 ? 28.668 37.272 15.811 1.00 39.85 ? 67 TYR A C 1 ATOM 257 O O . TYR A 1 32 ? 27.512 37.354 15.380 1.00 46.80 ? 67 TYR A O 1 ATOM 258 C CB . TYR A 1 32 ? 29.506 35.282 14.495 1.00 34.65 ? 67 TYR A CB 1 ATOM 259 C CG . TYR A 1 32 ? 30.248 36.079 13.441 1.00 39.92 ? 67 TYR A CG 1 ATOM 260 C CD1 . TYR A 1 32 ? 31.453 36.766 13.745 1.00 33.43 ? 67 TYR A CD1 1 ATOM 261 C CD2 . TYR A 1 32 ? 29.808 36.068 12.106 1.00 40.92 ? 67 TYR A CD2 1 ATOM 262 C CE1 . TYR A 1 32 ? 32.133 37.488 12.760 1.00 28.95 ? 67 TYR A CE1 1 ATOM 263 C CE2 . TYR A 1 32 ? 30.486 36.786 11.098 1.00 38.64 ? 67 TYR A CE2 1 ATOM 264 C CZ . TYR A 1 32 ? 31.662 37.469 11.414 1.00 38.58 ? 67 TYR A CZ 1 ATOM 265 O OH . TYR A 1 32 ? 32.308 38.198 10.386 1.00 34.05 ? 67 TYR A OH 1 ATOM 266 N N . ASN A 1 33 ? 29.347 38.283 16.299 1.00 34.18 ? 68 ASN A N 1 ATOM 267 C CA . ASN A 1 33 ? 28.937 39.642 16.184 1.00 37.36 ? 68 ASN A CA 1 ATOM 268 C C . ASN A 1 33 ? 29.306 40.265 14.816 1.00 45.04 ? 68 ASN A C 1 ATOM 269 O O . ASN A 1 33 ? 30.456 40.660 14.518 1.00 40.80 ? 68 ASN A O 1 ATOM 270 C CB . ASN A 1 33 ? 29.423 40.459 17.388 1.00 33.88 ? 68 ASN A CB 1 ATOM 271 C CG . ASN A 1 33 ? 28.818 41.845 17.428 1.00 41.30 ? 68 ASN A CG 1 ATOM 272 O OD1 . ASN A 1 33 ? 28.221 42.305 16.443 1.00 38.88 ? 68 ASN A OD1 1 ATOM 273 N ND2 . ASN A 1 33 ? 28.984 42.526 18.563 1.00 37.12 ? 68 ASN A ND2 1 ATOM 274 N N . ASN A 1 34 ? 28.275 40.396 13.983 1.00 42.23 ? 69 ASN A N 1 ATOM 275 C CA . ASN A 1 34 ? 28.459 40.864 12.626 1.00 37.31 ? 69 ASN A CA 1 ATOM 276 C C . ASN A 1 34 ? 28.573 42.340 12.641 1.00 36.48 ? 69 ASN A C 1 ATOM 277 O O . ASN A 1 34 ? 27.779 43.073 12.029 1.00 39.61 ? 69 ASN A O 1 ATOM 278 C CB . ASN A 1 34 ? 27.284 40.373 11.746 1.00 44.78 ? 69 ASN A CB 1 ATOM 279 C CG . ASN A 1 34 ? 27.448 40.753 10.293 1.00 50.99 ? 69 ASN A CG 1 ATOM 280 O OD1 . ASN A 1 34 ? 28.573 40.928 9.791 1.00 46.92 ? 69 ASN A OD1 1 ATOM 281 N ND2 . ASN A 1 34 ? 26.317 40.906 9.599 1.00 47.74 ? 69 ASN A ND2 1 ATOM 282 N N . SER A 1 35 ? 29.606 42.855 13.301 1.00 35.11 ? 70 SER A N 1 ATOM 283 C CA . SER A 1 35 ? 29.750 44.299 13.360 1.00 32.57 ? 70 SER A CA 1 ATOM 284 C C . SER A 1 35 ? 30.670 44.909 12.361 1.00 34.85 ? 70 SER A C 1 ATOM 285 O O . SER A 1 35 ? 31.109 46.092 12.549 1.00 32.09 ? 70 SER A O 1 ATOM 286 C CB . SER A 1 35 ? 30.199 44.749 14.779 1.00 43.09 ? 70 SER A CB 1 ATOM 287 O OG . SER A 1 35 ? 31.004 43.735 15.415 1.00 38.39 ? 70 SER A OG 1 ATOM 288 N N . VAL A 1 36 ? 31.063 44.139 11.336 1.00 39.35 ? 71 VAL A N 1 ATOM 289 C CA . VAL A 1 36 ? 32.085 44.703 10.445 1.00 40.27 ? 71 VAL A CA 1 ATOM 290 C C . VAL A 1 36 ? 31.745 46.090 9.842 1.00 38.71 ? 71 VAL A C 1 ATOM 291 O O . VAL A 1 36 ? 32.623 46.926 9.687 1.00 38.82 ? 71 VAL A O 1 ATOM 292 C CB . VAL A 1 36 ? 32.614 43.710 9.369 1.00 39.56 ? 71 VAL A CB 1 ATOM 293 C CG1 . VAL A 1 36 ? 31.597 43.518 8.253 1.00 41.47 ? 71 VAL A CG1 1 ATOM 294 C CG2 . VAL A 1 36 ? 33.930 44.250 8.782 1.00 44.69 ? 71 VAL A CG2 1 ATOM 295 N N . LYS A 1 37 ? 30.472 46.355 9.499 1.00 38.96 ? 72 LYS A N 1 ATOM 296 C CA . LYS A 1 37 ? 30.146 47.669 8.874 1.00 37.66 ? 72 LYS A CA 1 ATOM 297 C C . LYS A 1 37 ? 30.043 48.763 9.892 1.00 34.99 ? 72 LYS A C 1 ATOM 298 O O . LYS A 1 37 ? 30.217 49.971 9.587 1.00 35.80 ? 72 LYS A O 1 ATOM 299 C CB . LYS A 1 37 ? 28.901 47.568 7.951 1.00 41.29 ? 72 LYS A CB 1 ATOM 300 C CG . LYS A 1 37 ? 29.116 46.570 6.813 1.00 47.72 ? 72 LYS A CG 1 ATOM 301 C CD . LYS A 1 37 ? 28.100 46.691 5.671 1.00 45.22 ? 72 LYS A CD 1 ATOM 302 C CE . LYS A 1 37 ? 28.392 45.688 4.576 1.00 46.96 ? 72 LYS A CE 1 ATOM 303 N NZ . LYS A 1 37 ? 27.250 45.524 3.617 1.00 58.41 ? 72 LYS A NZ 1 ATOM 304 N N . THR A 1 38 ? 29.829 48.361 11.151 1.00 36.22 ? 73 THR A N 1 ATOM 305 C CA . THR A 1 38 ? 29.674 49.326 12.286 1.00 36.55 ? 73 THR A CA 1 ATOM 306 C C . THR A 1 38 ? 30.987 49.795 12.894 1.00 40.40 ? 73 THR A C 1 ATOM 307 O O . THR A 1 38 ? 31.184 50.999 13.231 1.00 41.94 ? 73 THR A O 1 ATOM 308 C CB . THR A 1 38 ? 28.944 48.611 13.416 1.00 38.59 ? 73 THR A CB 1 ATOM 309 O OG1 . THR A 1 38 ? 27.800 47.982 12.862 1.00 51.69 ? 73 THR A OG1 1 ATOM 310 C CG2 . THR A 1 38 ? 28.460 49.619 14.419 1.00 46.95 ? 73 THR A CG2 1 ATOM 311 N N . THR A 1 39 ? 31.893 48.826 13.065 1.00 38.53 ? 74 THR A N 1 ATOM 312 C CA . THR A 1 39 ? 33.211 49.099 13.694 1.00 38.22 ? 74 THR A CA 1 ATOM 313 C C . THR A 1 39 ? 34.456 48.744 12.849 1.00 37.03 ? 74 THR A C 1 ATOM 314 O O . THR A 1 39 ? 35.569 49.173 13.198 1.00 36.77 ? 74 THR A O 1 ATOM 315 C CB . THR A 1 39 ? 33.350 48.352 15.022 1.00 35.84 ? 74 THR A CB 1 ATOM 316 O OG1 . THR A 1 39 ? 33.266 46.951 14.786 1.00 33.82 ? 74 THR A OG1 1 ATOM 317 C CG2 . THR A 1 39 ? 32.238 48.747 16.024 1.00 40.34 ? 74 THR A CG2 1 ATOM 318 N N . GLY A 1 40 ? 34.287 48.024 11.743 1.00 29.68 ? 75 GLY A N 1 ATOM 319 C CA . GLY A 1 40 ? 35.445 47.600 10.954 1.00 34.21 ? 75 GLY A CA 1 ATOM 320 C C . GLY A 1 40 ? 35.893 46.209 11.428 1.00 32.11 ? 75 GLY A C 1 ATOM 321 O O . GLY A 1 40 ? 36.779 45.589 10.804 1.00 33.55 ? 75 GLY A O 1 ATOM 322 N N . TRP A 1 41 ? 35.244 45.684 12.477 1.00 33.49 ? 76 TRP A N 1 ATOM 323 C CA . TRP A 1 41 ? 35.414 44.320 12.954 1.00 31.25 ? 76 TRP A CA 1 ATOM 324 C C . TRP A 1 41 ? 34.163 43.516 13.137 1.00 34.29 ? 76 TRP A C 1 ATOM 325 O O . TRP A 1 41 ? 33.260 43.928 13.874 1.00 35.31 ? 76 TRP A O 1 ATOM 326 C CB . TRP A 1 41 ? 36.069 44.289 14.351 1.00 28.32 ? 76 TRP A CB 1 ATOM 327 C CG . TRP A 1 41 ? 37.368 45.070 14.406 1.00 28.86 ? 76 TRP A CG 1 ATOM 328 C CD1 . TRP A 1 41 ? 37.549 46.399 14.718 1.00 31.62 ? 76 TRP A CD1 1 ATOM 329 C CD2 . TRP A 1 41 ? 38.732 44.527 14.202 1.00 28.09 ? 76 TRP A CD2 1 ATOM 330 N NE1 . TRP A 1 41 ? 38.919 46.732 14.713 1.00 28.46 ? 76 TRP A NE1 1 ATOM 331 C CE2 . TRP A 1 41 ? 39.647 45.646 14.361 1.00 27.68 ? 76 TRP A CE2 1 ATOM 332 C CE3 . TRP A 1 41 ? 39.253 43.238 13.905 1.00 26.72 ? 76 TRP A CE3 1 ATOM 333 C CZ2 . TRP A 1 41 ? 41.052 45.492 14.203 1.00 29.06 ? 76 TRP A CZ2 1 ATOM 334 C CZ3 . TRP A 1 41 ? 40.652 43.112 13.739 1.00 26.59 ? 76 TRP A CZ3 1 ATOM 335 C CH2 . TRP A 1 41 ? 41.497 44.217 13.873 1.00 24.99 ? 76 TRP A CH2 1 ATOM 336 N N . GLY A 1 42 ? 34.172 42.299 12.599 1.00 26.72 ? 77 GLY A N 1 ATOM 337 C CA . GLY A 1 42 ? 33.447 41.200 13.222 1.00 26.94 ? 77 GLY A CA 1 ATOM 338 C C . GLY A 1 42 ? 34.090 40.743 14.546 1.00 35.81 ? 77 GLY A C 1 ATOM 339 O O . GLY A 1 42 ? 35.337 40.875 14.759 1.00 31.29 ? 77 GLY A O 1 ATOM 340 N N . ILE A 1 43 ? 33.267 40.197 15.424 1.00 32.80 ? 78 ILE A N 1 ATOM 341 C CA . ILE A 1 43 ? 33.724 39.586 16.692 1.00 31.42 ? 78 ILE A CA 1 ATOM 342 C C . ILE A 1 43 ? 33.187 38.182 16.846 1.00 35.33 ? 78 ILE A C 1 ATOM 343 O O . ILE A 1 43 ? 31.965 37.930 16.841 1.00 38.72 ? 78 ILE A O 1 ATOM 344 C CB . ILE A 1 43 ? 33.427 40.469 17.930 1.00 33.32 ? 78 ILE A CB 1 ATOM 345 C CG1 . ILE A 1 43 ? 33.951 41.884 17.701 1.00 33.70 ? 78 ILE A CG1 1 ATOM 346 C CG2 . ILE A 1 43 ? 34.042 39.807 19.179 1.00 32.52 ? 78 ILE A CG2 1 ATOM 347 C CD1 . ILE A 1 43 ? 33.447 42.988 18.612 1.00 43.39 ? 78 ILE A CD1 1 ATOM 348 N N . LEU A 1 44 ? 34.097 37.239 16.909 1.00 28.60 ? 79 LEU A N 1 ATOM 349 C CA . LEU A 1 44 ? 33.753 35.862 17.160 1.00 28.79 ? 79 LEU A CA 1 ATOM 350 C C . LEU A 1 44 ? 34.254 35.403 18.531 1.00 36.55 ? 79 LEU A C 1 ATOM 351 O O . LEU A 1 44 ? 35.432 35.664 18.900 1.00 31.78 ? 79 LEU A O 1 ATOM 352 C CB . LEU A 1 44 ? 34.359 35.031 16.041 1.00 29.09 ? 79 LEU A CB 1 ATOM 353 C CG . LEU A 1 44 ? 34.233 33.499 16.168 1.00 35.24 ? 79 LEU A CG 1 ATOM 354 C CD1 . LEU A 1 44 ? 32.855 32.991 15.662 1.00 35.63 ? 79 LEU A CD1 1 ATOM 355 C CD2 . LEU A 1 44 ? 35.341 32.839 15.395 1.00 31.22 ? 79 LEU A CD2 1 ATOM 356 N N . GLU A 1 45 ? 33.415 34.688 19.296 1.00 32.20 ? 80 GLU A N 1 ATOM 357 C CA . GLU A 1 45 ? 33.865 34.135 20.608 1.00 33.93 ? 80 GLU A CA 1 ATOM 358 C C . GLU A 1 45 ? 33.331 32.758 20.778 1.00 38.34 ? 80 GLU A C 1 ATOM 359 O O . GLU A 1 45 ? 32.137 32.551 20.556 1.00 37.74 ? 80 GLU A O 1 ATOM 360 C CB . GLU A 1 45 ? 33.503 35.052 21.810 1.00 32.83 ? 80 GLU A CB 1 ATOM 361 C CG . GLU A 1 45 ? 33.823 34.388 23.139 1.00 29.54 ? 80 GLU A CG 1 ATOM 362 C CD . GLU A 1 45 ? 33.743 35.318 24.365 1.00 31.67 ? 80 GLU A CD 1 ATOM 363 O OE1 . GLU A 1 45 ? 33.402 36.519 24.279 1.00 32.94 ? 80 GLU A OE1 1 ATOM 364 O OE2 . GLU A 1 45 ? 34.053 34.797 25.456 1.00 33.90 ? 80 GLU A OE2 1 ATOM 365 N N . ILE A 1 46 ? 34.220 31.810 21.082 1.00 31.52 ? 81 ILE A N 1 ATOM 366 C CA . ILE A 1 46 ? 33.876 30.407 21.183 1.00 37.05 ? 81 ILE A CA 1 ATOM 367 C C . ILE A 1 46 ? 34.371 29.885 22.528 1.00 44.45 ? 81 ILE A C 1 ATOM 368 O O . ILE A 1 46 ? 35.536 30.122 22.882 1.00 38.42 ? 81 ILE A O 1 ATOM 369 C CB . ILE A 1 46 ? 34.507 29.640 20.030 1.00 38.50 ? 81 ILE A CB 1 ATOM 370 C CG1 . ILE A 1 46 ? 33.943 30.174 18.697 1.00 40.07 ? 81 ILE A CG1 1 ATOM 371 C CG2 . ILE A 1 46 ? 34.382 28.130 20.193 1.00 34.22 ? 81 ILE A CG2 1 ATOM 372 C CD1 . ILE A 1 46 ? 34.547 29.584 17.449 1.00 41.63 ? 81 ILE A CD1 1 ATOM 373 N N . LYS A 1 47 ? 33.491 29.196 23.273 1.00 37.19 ? 82 LYS A N 1 ATOM 374 C CA . LYS A 1 47 ? 33.830 28.456 24.501 1.00 37.24 ? 82 LYS A CA 1 ATOM 375 C C . LYS A 1 47 ? 33.495 27.017 24.187 1.00 38.31 ? 82 LYS A C 1 ATOM 376 O O . LYS A 1 47 ? 32.328 26.692 23.945 1.00 45.66 ? 82 LYS A O 1 ATOM 377 C CB . LYS A 1 47 ? 32.951 29.029 25.652 1.00 41.10 ? 82 LYS A CB 1 ATOM 378 C CG . LYS A 1 47 ? 33.589 29.145 27.047 1.00 47.88 ? 82 LYS A CG 1 ATOM 379 C CD . LYS A 1 47 ? 33.891 30.599 27.375 1.00 50.61 ? 82 LYS A CD 1 ATOM 380 C CE . LYS A 1 47 ? 34.457 30.734 28.765 1.00 52.80 ? 82 LYS A CE 1 ATOM 381 N NZ . LYS A 1 47 ? 35.820 31.357 28.700 1.00 50.92 ? 82 LYS A NZ 1 ATOM 382 N N . ALA A 1 48 ? 34.469 26.132 24.170 1.00 36.12 ? 83 ALA A N 1 ATOM 383 C CA . ALA A 1 48 ? 34.240 24.759 23.798 1.00 33.29 ? 83 ALA A CA 1 ATOM 384 C C . ALA A 1 48 ? 34.756 23.743 24.816 1.00 41.98 ? 83 ALA A C 1 ATOM 385 O O . ALA A 1 48 ? 35.832 23.935 25.443 1.00 38.30 ? 83 ALA A O 1 ATOM 386 C CB . ALA A 1 48 ? 34.870 24.456 22.418 1.00 34.62 ? 83 ALA A CB 1 ATOM 387 N N . GLY A 1 49 ? 34.032 22.605 24.924 1.00 39.53 ? 84 GLY A N 1 ATOM 388 C CA . GLY A 1 49 ? 34.280 21.602 25.937 1.00 39.21 ? 84 GLY A CA 1 ATOM 389 C C . GLY A 1 49 ? 33.934 21.931 27.400 1.00 33.76 ? 84 GLY A C 1 ATOM 390 O O . GLY A 1 49 ? 34.413 21.225 28.290 1.00 37.64 ? 84 GLY A O 1 ATOM 391 N N . TYR A 1 50 ? 33.180 22.998 27.629 1.00 38.14 ? 85 TYR A N 1 ATOM 392 C CA . TYR A 1 50 ? 32.708 23.455 28.933 1.00 38.48 ? 85 TYR A CA 1 ATOM 393 C C . TYR A 1 50 ? 31.210 23.103 29.205 1.00 43.93 ? 85 TYR A C 1 ATOM 394 O O . TYR A 1 50 ? 30.562 23.771 30.007 1.00 39.05 ? 85 TYR A O 1 ATOM 395 C CB . TYR A 1 50 ? 32.848 24.977 28.992 1.00 41.97 ? 85 TYR A CB 1 ATOM 396 C CG . TYR A 1 50 ? 34.306 25.405 29.069 1.00 44.69 ? 85 TYR A CG 1 ATOM 397 C CD1 . TYR A 1 50 ? 35.064 25.157 30.224 1.00 47.63 ? 85 TYR A CD1 1 ATOM 398 C CD2 . TYR A 1 50 ? 34.942 25.994 27.987 1.00 39.92 ? 85 TYR A CD2 1 ATOM 399 C CE1 . TYR A 1 50 ? 36.420 25.534 30.316 1.00 42.54 ? 85 TYR A CE1 1 ATOM 400 C CE2 . TYR A 1 50 ? 36.293 26.371 28.059 1.00 42.73 ? 85 TYR A CE2 1 ATOM 401 C CZ . TYR A 1 50 ? 37.037 26.145 29.228 1.00 44.38 ? 85 TYR A CZ 1 ATOM 402 O OH . TYR A 1 50 ? 38.390 26.508 29.333 1.00 35.45 ? 85 TYR A OH 1 ATOM 403 N N . GLY A 1 51 ? 30.653 22.114 28.504 1.00 43.00 ? 86 GLY A N 1 ATOM 404 C CA . GLY A 1 51 ? 29.187 21.827 28.646 1.00 47.69 ? 86 GLY A CA 1 ATOM 405 C C . GLY A 1 51 ? 28.989 20.565 29.462 1.00 51.51 ? 86 GLY A C 1 ATOM 406 O O . GLY A 1 51 ? 29.931 20.073 30.114 1.00 48.78 ? 86 GLY A O 1 ATOM 407 N N . SER A 1 52 ? 27.791 19.998 29.405 1.00 48.73 ? 87 SER A N 1 ATOM 408 C CA . SER A 1 52 ? 27.504 18.743 30.086 1.00 51.99 ? 87 SER A CA 1 ATOM 409 C C . SER A 1 52 ? 28.444 17.634 29.731 1.00 48.28 ? 87 SER A C 1 ATOM 410 O O . SER A 1 52 ? 28.940 16.918 30.602 1.00 60.03 ? 87 SER A O 1 ATOM 411 C CB . SER A 1 52 ? 26.065 18.313 29.784 1.00 53.37 ? 87 SER A CB 1 ATOM 412 O OG . SER A 1 52 ? 25.234 19.365 30.243 1.00 54.56 ? 87 SER A OG 1 ATOM 413 N N . GLN A 1 53 ? 28.710 17.464 28.459 1.00 50.87 ? 88 GLN A N 1 ATOM 414 C CA . GLN A 1 53 ? 29.433 16.268 28.025 1.00 57.13 ? 88 GLN A CA 1 ATOM 415 C C . GLN A 1 53 ? 30.923 16.422 28.292 1.00 63.38 ? 88 GLN A C 1 ATOM 416 O O . GLN A 1 53 ? 31.492 17.501 28.158 1.00 55.13 ? 88 GLN A O 1 ATOM 417 C CB . GLN A 1 53 ? 29.160 15.968 26.550 1.00 56.32 ? 88 GLN A CB 1 ATOM 418 C CG . GLN A 1 53 ? 29.634 14.594 26.097 1.00 59.81 ? 88 GLN A CG 1 ATOM 419 C CD . GLN A 1 53 ? 29.057 14.160 24.757 1.00 68.94 ? 88 GLN A CD 1 ATOM 420 O OE1 . GLN A 1 53 ? 29.260 13.005 24.340 1.00 67.57 ? 88 GLN A OE1 1 ATOM 421 N NE2 . GLN A 1 53 ? 28.356 15.085 24.053 1.00 55.55 ? 88 GLN A NE2 1 ATOM 422 N N . SER A 1 54 ? 31.557 15.333 28.673 1.00 59.18 ? 89 SER A N 1 ATOM 423 C CA . SER A 1 54 ? 32.967 15.385 28.906 1.00 68.14 ? 89 SER A CA 1 ATOM 424 C C . SER A 1 54 ? 33.550 14.868 27.600 1.00 71.86 ? 89 SER A C 1 ATOM 425 O O . SER A 1 54 ? 33.169 13.777 27.145 1.00 68.46 ? 89 SER A O 1 ATOM 426 C CB . SER A 1 54 ? 33.334 14.511 30.115 1.00 71.49 ? 89 SER A CB 1 ATOM 427 O OG . SER A 1 54 ? 34.698 14.648 30.443 1.00 70.80 ? 89 SER A OG 1 ATOM 428 N N . LEU A 1 55 ? 34.430 15.650 26.972 1.00 54.83 ? 90 LEU A N 1 ATOM 429 C CA . LEU A 1 55 ? 34.836 15.345 25.591 1.00 49.89 ? 90 LEU A CA 1 ATOM 430 C C . LEU A 1 55 ? 36.321 15.193 25.461 1.00 49.00 ? 90 LEU A C 1 ATOM 431 O O . LEU A 1 55 ? 37.065 15.934 26.119 1.00 46.03 ? 90 LEU A O 1 ATOM 432 C CB . LEU A 1 55 ? 34.411 16.467 24.660 1.00 52.08 ? 90 LEU A CB 1 ATOM 433 C CG . LEU A 1 55 ? 32.953 16.655 24.274 1.00 61.72 ? 90 LEU A CG 1 ATOM 434 C CD1 . LEU A 1 55 ? 32.842 17.978 23.507 1.00 54.90 ? 90 LEU A CD1 1 ATOM 435 C CD2 . LEU A 1 55 ? 32.446 15.448 23.475 1.00 51.23 ? 90 LEU A CD2 1 ATOM 436 N N . SER A 1 56 ? 36.751 14.247 24.627 1.00 38.55 ? 91 SER A N 1 ATOM 437 C CA . SER A 1 56 ? 38.139 14.091 24.237 1.00 38.66 ? 91 SER A CA 1 ATOM 438 C C . SER A 1 56 ? 38.618 15.422 23.623 1.00 38.87 ? 91 SER A C 1 ATOM 439 O O . SER A 1 56 ? 37.793 16.284 23.202 1.00 38.44 ? 91 SER A O 1 ATOM 440 C CB . SER A 1 56 ? 38.278 12.963 23.237 1.00 42.50 ? 91 SER A CB 1 ATOM 441 O OG . SER A 1 56 ? 37.860 13.381 21.947 1.00 46.43 ? 91 SER A OG 1 ATOM 442 N N . ASN A 1 57 ? 39.933 15.644 23.685 1.00 35.77 ? 92 ASN A N 1 ATOM 443 C CA . ASN A 1 57 ? 40.507 16.939 23.249 1.00 39.10 ? 92 ASN A CA 1 ATOM 444 C C . ASN A 1 57 ? 40.251 17.245 21.763 1.00 32.64 ? 92 ASN A C 1 ATOM 445 O O . ASN A 1 57 ? 39.755 18.329 21.397 1.00 33.58 ? 92 ASN A O 1 ATOM 446 C CB . ASN A 1 57 ? 42.002 16.960 23.603 1.00 34.12 ? 92 ASN A CB 1 ATOM 447 C CG . ASN A 1 57 ? 42.231 17.120 25.094 1.00 33.81 ? 92 ASN A CG 1 ATOM 448 O OD1 . ASN A 1 57 ? 41.412 17.731 25.815 1.00 32.78 ? 92 ASN A OD1 1 ATOM 449 N ND2 . ASN A 1 57 ? 43.383 16.661 25.555 1.00 32.54 ? 92 ASN A ND2 1 ATOM 450 N N . GLU A 1 58 ? 40.494 16.243 20.945 1.00 34.50 ? 93 GLU A N 1 ATOM 451 C CA . GLU A 1 58 ? 40.233 16.270 19.490 1.00 41.48 ? 93 GLU A CA 1 ATOM 452 C C . GLU A 1 58 ? 38.793 16.667 19.117 1.00 41.12 ? 93 GLU A C 1 ATOM 453 O O . GLU A 1 58 ? 38.570 17.403 18.128 1.00 38.22 ? 93 GLU A O 1 ATOM 454 C CB . GLU A 1 58 ? 40.689 14.962 18.833 1.00 44.11 ? 93 GLU A CB 1 ATOM 455 C CG . GLU A 1 58 ? 40.402 13.721 19.680 1.00 60.12 ? 93 GLU A CG 1 ATOM 456 C CD . GLU A 1 58 ? 41.381 13.588 20.881 1.00 69.18 ? 93 GLU A CD 1 ATOM 457 O OE1 . GLU A 1 58 ? 42.575 13.246 20.689 1.00 67.96 ? 93 GLU A OE1 1 ATOM 458 O OE2 . GLU A 1 58 ? 40.979 13.846 22.039 1.00 59.33 ? 93 GLU A OE2 1 ATOM 459 N N . ILE A 1 59 ? 37.804 16.230 19.922 1.00 38.13 ? 94 ILE A N 1 ATOM 460 C CA . ILE A 1 59 ? 36.415 16.545 19.629 1.00 35.46 ? 94 ILE A CA 1 ATOM 461 C C . ILE A 1 59 ? 36.087 17.925 20.117 1.00 33.99 ? 94 ILE A C 1 ATOM 462 O O . ILE A 1 59 ? 35.272 18.567 19.508 1.00 35.52 ? 94 ILE A O 1 ATOM 463 C CB . ILE A 1 59 ? 35.432 15.495 20.262 1.00 37.40 ? 94 ILE A CB 1 ATOM 464 C CG1 . ILE A 1 59 ? 35.577 14.127 19.556 1.00 43.96 ? 94 ILE A CG1 1 ATOM 465 C CG2 . ILE A 1 59 ? 34.002 15.969 20.093 1.00 37.20 ? 94 ILE A CG2 1 ATOM 466 C CD1 . ILE A 1 59 ? 35.072 12.912 20.316 1.00 47.31 ? 94 ILE A CD1 1 ATOM 467 N N . ILE A 1 60 ? 36.719 18.392 21.226 1.00 29.12 ? 95 ILE A N 1 ATOM 468 C CA . ILE A 1 60 ? 36.613 19.803 21.599 1.00 35.97 ? 95 ILE A CA 1 ATOM 469 C C . ILE A 1 60 ? 37.111 20.715 20.414 1.00 32.40 ? 95 ILE A C 1 ATOM 470 O O . ILE A 1 60 ? 36.454 21.672 20.056 1.00 35.03 ? 95 ILE A O 1 ATOM 471 C CB . ILE A 1 60 ? 37.415 20.188 22.885 1.00 30.94 ? 95 ILE A CB 1 ATOM 472 C CG1 . ILE A 1 60 ? 36.774 19.457 24.104 1.00 38.58 ? 95 ILE A CG1 1 ATOM 473 C CG2 . ILE A 1 60 ? 37.269 21.683 23.140 1.00 29.97 ? 95 ILE A CG2 1 ATOM 474 C CD1 . ILE A 1 60 ? 37.686 19.206 25.293 1.00 35.69 ? 95 ILE A CD1 1 ATOM 475 N N . MET A 1 61 ? 38.270 20.398 19.879 1.00 32.88 ? 96 MET A N 1 ATOM 476 C CA . MET A 1 61 ? 38.842 21.200 18.755 1.00 34.32 ? 96 MET A CA 1 ATOM 477 C C . MET A 1 61 ? 37.891 21.158 17.486 1.00 30.11 ? 96 MET A C 1 ATOM 478 O O . MET A 1 61 ? 37.568 22.195 16.882 1.00 32.02 ? 96 MET A O 1 ATOM 479 C CB . MET A 1 61 ? 40.224 20.666 18.416 1.00 26.13 ? 96 MET A CB 1 ATOM 480 C CG . MET A 1 61 ? 41.256 20.766 19.561 1.00 25.62 ? 96 MET A CG 1 ATOM 481 S SD . MET A 1 61 ? 41.407 22.452 20.233 1.00 31.27 ? 96 MET A SD 1 ATOM 482 C CE . MET A 1 61 ? 42.182 23.283 18.806 1.00 28.87 ? 96 MET A CE 1 ATOM 483 N N . PHE A 1 62 ? 37.422 19.958 17.162 1.00 33.26 ? 97 PHE A N 1 ATOM 484 C CA . PHE A 1 62 ? 36.510 19.759 16.013 1.00 34.65 ? 97 PHE A CA 1 ATOM 485 C C . PHE A 1 62 ? 35.246 20.596 16.200 1.00 35.01 ? 97 PHE A C 1 ATOM 486 O O . PHE A 1 62 ? 34.855 21.360 15.335 1.00 33.40 ? 97 PHE A O 1 ATOM 487 C CB . PHE A 1 62 ? 36.222 18.257 15.851 1.00 39.57 ? 97 PHE A CB 1 ATOM 488 C CG . PHE A 1 62 ? 35.422 17.934 14.636 1.00 43.26 ? 97 PHE A CG 1 ATOM 489 C CD1 . PHE A 1 62 ? 36.062 17.678 13.425 1.00 42.96 ? 97 PHE A CD1 1 ATOM 490 C CD2 . PHE A 1 62 ? 34.017 17.917 14.687 1.00 45.64 ? 97 PHE A CD2 1 ATOM 491 C CE1 . PHE A 1 62 ? 35.327 17.388 12.262 1.00 41.02 ? 97 PHE A CE1 1 ATOM 492 C CE2 . PHE A 1 62 ? 33.271 17.638 13.535 1.00 47.49 ? 97 PHE A CE2 1 ATOM 493 C CZ . PHE A 1 62 ? 33.930 17.365 12.333 1.00 42.98 ? 97 PHE A CZ 1 ATOM 494 N N . ALA A 1 63 ? 34.653 20.531 17.398 1.00 37.01 ? 98 ALA A N 1 ATOM 495 C CA . ALA A 1 63 ? 33.465 21.294 17.707 1.00 31.10 ? 98 ALA A CA 1 ATOM 496 C C . ALA A 1 63 ? 33.669 22.808 17.660 1.00 33.67 ? 98 ALA A C 1 ATOM 497 O O . ALA A 1 63 ? 32.779 23.560 17.236 1.00 30.84 ? 98 ALA A O 1 ATOM 498 C CB . ALA A 1 63 ? 32.968 20.896 19.112 1.00 36.82 ? 98 ALA A CB 1 ATOM 499 N N . ALA A 1 64 ? 34.813 23.284 18.161 1.00 31.30 ? 99 ALA A N 1 ATOM 500 C CA . ALA A 1 64 ? 35.108 24.715 18.097 1.00 29.15 ? 99 ALA A CA 1 ATOM 501 C C . ALA A 1 64 ? 35.196 25.144 16.609 1.00 26.08 ? 99 ALA A C 1 ATOM 502 O O . ALA A 1 64 ? 34.709 26.211 16.223 1.00 30.19 ? 99 ALA A O 1 ATOM 503 C CB . ALA A 1 64 ? 36.483 24.947 18.773 1.00 30.42 ? 99 ALA A CB 1 ATOM 504 N N . GLY A 1 65 ? 35.887 24.352 15.803 1.00 28.87 ? 100 GLY A N 1 ATOM 505 C CA . GLY A 1 65 ? 36.020 24.754 14.341 1.00 31.34 ? 100 GLY A CA 1 ATOM 506 C C . GLY A 1 65 ? 34.661 24.672 13.650 1.00 28.93 ? 100 GLY A C 1 ATOM 507 O O . GLY A 1 65 ? 34.219 25.637 12.949 1.00 30.11 ? 100 GLY A O 1 ATOM 508 N N . PHE A 1 66 ? 33.936 23.602 13.977 1.00 32.75 ? 101 PHE A N 1 ATOM 509 C CA . PHE A 1 66 ? 32.538 23.426 13.442 1.00 31.65 ? 101 PHE A CA 1 ATOM 510 C C . PHE A 1 66 ? 31.721 24.614 13.727 1.00 30.82 ? 101 PHE A C 1 ATOM 511 O O . PHE A 1 66 ? 31.211 25.200 12.807 1.00 36.62 ? 101 PHE A O 1 ATOM 512 C CB . PHE A 1 66 ? 31.809 22.185 13.986 1.00 38.51 ? 101 PHE A CB 1 ATOM 513 C CG . PHE A 1 66 ? 30.553 21.848 13.198 1.00 36.17 ? 101 PHE A CG 1 ATOM 514 C CD1 . PHE A 1 66 ? 29.451 22.689 13.217 1.00 42.49 ? 101 PHE A CD1 1 ATOM 515 C CD2 . PHE A 1 66 ? 30.513 20.706 12.433 1.00 39.87 ? 101 PHE A CD2 1 ATOM 516 C CE1 . PHE A 1 66 ? 28.306 22.366 12.490 1.00 41.14 ? 101 PHE A CE1 1 ATOM 517 C CE2 . PHE A 1 66 ? 29.391 20.389 11.708 1.00 43.64 ? 101 PHE A CE2 1 ATOM 518 C CZ . PHE A 1 66 ? 28.288 21.223 11.749 1.00 38.79 ? 101 PHE A CZ 1 ATOM 519 N N . LEU A 1 67 ? 31.653 25.036 14.993 1.00 34.73 ? 102 LEU A N 1 ATOM 520 C CA . LEU A 1 67 ? 30.931 26.245 15.340 1.00 33.14 ? 102 LEU A CA 1 ATOM 521 C C . LEU A 1 67 ? 31.394 27.500 14.584 1.00 36.74 ? 102 LEU A C 1 ATOM 522 O O . LEU A 1 67 ? 30.556 28.357 14.125 1.00 35.73 ? 102 LEU A O 1 ATOM 523 C CB . LEU A 1 67 ? 30.922 26.467 16.877 1.00 33.45 ? 102 LEU A CB 1 ATOM 524 C CG . LEU A 1 67 ? 30.076 27.667 17.375 1.00 40.97 ? 102 LEU A CG 1 ATOM 525 C CD1 . LEU A 1 67 ? 28.577 27.442 17.191 1.00 41.28 ? 102 LEU A CD1 1 ATOM 526 C CD2 . LEU A 1 67 ? 30.292 27.995 18.842 1.00 38.86 ? 102 LEU A CD2 1 ATOM 527 N N . GLU A 1 68 ? 32.729 27.694 14.515 1.00 35.25 ? 103 GLU A N 1 ATOM 528 C CA . GLU A 1 68 ? 33.228 28.876 13.804 1.00 34.43 ? 103 GLU A CA 1 ATOM 529 C C . GLU A 1 68 ? 32.826 28.810 12.308 1.00 28.23 ? 103 GLU A C 1 ATOM 530 O O . GLU A 1 68 ? 32.440 29.811 11.733 1.00 30.42 ? 103 GLU A O 1 ATOM 531 C CB . GLU A 1 68 ? 34.779 29.002 13.950 1.00 31.40 ? 103 GLU A CB 1 ATOM 532 C CG . GLU A 1 68 ? 35.403 30.112 13.096 1.00 28.64 ? 103 GLU A CG 1 ATOM 533 C CD . GLU A 1 68 ? 36.860 30.465 13.502 1.00 29.64 ? 103 GLU A CD 1 ATOM 534 O OE1 . GLU A 1 68 ? 37.358 29.996 14.608 1.00 30.37 ? 103 GLU A OE1 1 ATOM 535 O OE2 . GLU A 1 68 ? 37.461 31.259 12.744 1.00 29.67 ? 103 GLU A OE2 1 ATOM 536 N N . GLY A 1 69 ? 32.964 27.652 11.668 1.00 27.84 ? 104 GLY A N 1 ATOM 537 C CA . GLY A 1 69 ? 32.657 27.554 10.189 1.00 31.13 ? 104 GLY A CA 1 ATOM 538 C C . GLY A 1 69 ? 31.162 27.834 9.931 1.00 34.95 ? 104 GLY A C 1 ATOM 539 O O . GLY A 1 69 ? 30.783 28.630 9.040 1.00 32.02 ? 104 GLY A O 1 ATOM 540 N N . TYR A 1 70 ? 30.311 27.232 10.780 1.00 35.86 ? 105 TYR A N 1 ATOM 541 C CA . TYR A 1 70 ? 28.846 27.467 10.758 1.00 37.08 ? 105 TYR A CA 1 ATOM 542 C C . TYR A 1 70 ? 28.468 28.936 10.884 1.00 36.58 ? 105 TYR A C 1 ATOM 543 O O . TYR A 1 70 ? 27.726 29.467 10.053 1.00 37.32 ? 105 TYR A O 1 ATOM 544 C CB . TYR A 1 70 ? 28.179 26.638 11.873 1.00 43.78 ? 105 TYR A CB 1 ATOM 545 C CG . TYR A 1 70 ? 26.689 26.854 11.917 1.00 41.50 ? 105 TYR A CG 1 ATOM 546 C CD1 . TYR A 1 70 ? 26.133 27.896 12.671 1.00 44.64 ? 105 TYR A CD1 1 ATOM 547 C CD2 . TYR A 1 70 ? 25.844 26.058 11.148 1.00 45.76 ? 105 TYR A CD2 1 ATOM 548 C CE1 . TYR A 1 70 ? 24.767 28.113 12.683 1.00 44.96 ? 105 TYR A CE1 1 ATOM 549 C CE2 . TYR A 1 70 ? 24.468 26.259 11.164 1.00 48.06 ? 105 TYR A CE2 1 ATOM 550 C CZ . TYR A 1 70 ? 23.951 27.269 11.929 1.00 47.84 ? 105 TYR A CZ 1 ATOM 551 O OH . TYR A 1 70 ? 22.600 27.440 11.939 1.00 51.67 ? 105 TYR A OH 1 ATOM 552 N N . LEU A 1 71 ? 29.033 29.654 11.850 1.00 36.97 ? 106 LEU A N 1 ATOM 553 C CA . LEU A 1 71 ? 28.768 31.091 11.978 1.00 35.32 ? 106 LEU A CA 1 ATOM 554 C C . LEU A 1 71 ? 29.397 32.010 10.928 1.00 40.27 ? 106 LEU A C 1 ATOM 555 O O . LEU A 1 71 ? 28.861 33.111 10.643 1.00 38.16 ? 106 LEU A O 1 ATOM 556 C CB . LEU A 1 71 ? 29.247 31.595 13.362 1.00 34.97 ? 106 LEU A CB 1 ATOM 557 C CG . LEU A 1 71 ? 28.548 31.103 14.664 1.00 39.07 ? 106 LEU A CG 1 ATOM 558 C CD1 . LEU A 1 71 ? 29.430 31.335 15.887 1.00 32.25 ? 106 LEU A CD1 1 ATOM 559 C CD2 . LEU A 1 71 ? 27.230 31.855 14.794 1.00 40.46 ? 106 LEU A CD2 1 ATOM 560 N N . THR A 1 72 ? 30.585 31.666 10.422 1.00 33.75 ? 107 THR A N 1 ATOM 561 C CA . THR A 1 72 ? 31.248 32.670 9.582 1.00 29.77 ? 107 THR A CA 1 ATOM 562 C C . THR A 1 72 ? 31.293 32.314 8.106 1.00 30.60 ? 107 THR A C 1 ATOM 563 O O . THR A 1 72 ? 31.888 33.083 7.351 1.00 29.95 ? 107 THR A O 1 ATOM 564 C CB . THR A 1 72 ? 32.725 32.993 10.030 1.00 29.36 ? 107 THR A CB 1 ATOM 565 O OG1 . THR A 1 72 ? 33.462 31.757 10.046 1.00 28.77 ? 107 THR A OG1 1 ATOM 566 C CG2 . THR A 1 72 ? 32.719 33.524 11.416 1.00 26.16 ? 107 THR A CG2 1 ATOM 567 N N . ALA A 1 73 ? 30.781 31.144 7.693 1.00 34.27 ? 108 ALA A N 1 ATOM 568 C CA . ALA A 1 73 ? 30.884 30.716 6.253 1.00 40.50 ? 108 ALA A CA 1 ATOM 569 C C . ALA A 1 73 ? 30.622 31.833 5.204 1.00 40.97 ? 108 ALA A C 1 ATOM 570 O O . ALA A 1 73 ? 31.425 31.957 4.266 1.00 38.96 ? 108 ALA A O 1 ATOM 571 C CB . ALA A 1 73 ? 30.054 29.460 5.924 1.00 37.77 ? 108 ALA A CB 1 ATOM 572 N N . PRO A 1 74 ? 29.538 32.654 5.375 1.00 39.04 ? 109 PRO A N 1 ATOM 573 C CA . PRO A 1 74 ? 29.276 33.686 4.358 1.00 42.19 ? 109 PRO A CA 1 ATOM 574 C C . PRO A 1 74 ? 30.511 34.602 4.162 1.00 36.57 ? 109 PRO A C 1 ATOM 575 O O . PRO A 1 74 ? 30.986 34.849 3.049 1.00 31.41 ? 109 PRO A O 1 ATOM 576 C CB . PRO A 1 74 ? 28.091 34.480 4.962 1.00 40.13 ? 109 PRO A CB 1 ATOM 577 C CG . PRO A 1 74 ? 27.338 33.443 5.699 1.00 40.95 ? 109 PRO A CG 1 ATOM 578 C CD . PRO A 1 74 ? 28.387 32.504 6.280 1.00 42.64 ? 109 PRO A CD 1 ATOM 579 N N . HIS A 1 75 ? 31.049 35.043 5.278 1.00 36.25 ? 110 HIS A N 1 ATOM 580 C CA . HIS A 1 75 ? 32.245 35.859 5.292 1.00 33.39 ? 110 HIS A CA 1 ATOM 581 C C . HIS A 1 75 ? 33.520 35.101 4.885 1.00 30.00 ? 110 HIS A C 1 ATOM 582 O O . HIS A 1 75 ? 34.396 35.698 4.272 1.00 31.00 ? 110 HIS A O 1 ATOM 583 C CB . HIS A 1 75 ? 32.328 36.542 6.660 1.00 31.24 ? 110 HIS A CB 1 ATOM 584 C CG . HIS A 1 75 ? 31.492 37.800 6.744 1.00 37.65 ? 110 HIS A CG 1 ATOM 585 N ND1 . HIS A 1 75 ? 31.109 38.351 7.918 1.00 39.16 ? 110 HIS A ND1 1 ATOM 586 C CD2 . HIS A 1 75 ? 31.044 38.665 5.743 1.00 34.56 ? 110 HIS A CD2 1 ATOM 587 C CE1 . HIS A 1 75 ? 30.472 39.521 7.686 1.00 38.64 ? 110 HIS A CE1 1 ATOM 588 N NE2 . HIS A 1 75 ? 30.424 39.708 6.357 1.00 39.06 ? 110 HIS A NE2 1 ATOM 589 N N . MET A 1 76 ? 33.598 33.803 5.147 1.00 28.60 ? 111 MET A N 1 ATOM 590 C CA . MET A 1 76 ? 34.691 32.983 4.628 1.00 28.96 ? 111 MET A CA 1 ATOM 591 C C . MET A 1 76 ? 34.700 33.001 3.101 1.00 34.64 ? 111 MET A C 1 ATOM 592 O O . MET A 1 76 ? 35.735 33.095 2.407 1.00 26.25 ? 111 MET A O 1 ATOM 593 C CB . MET A 1 76 ? 34.584 31.552 5.136 1.00 28.36 ? 111 MET A CB 1 ATOM 594 C CG . MET A 1 76 ? 34.929 31.391 6.645 1.00 27.41 ? 111 MET A CG 1 ATOM 595 S SD . MET A 1 76 ? 34.564 29.783 7.225 1.00 32.36 ? 111 MET A SD 1 ATOM 596 C CE . MET A 1 76 ? 35.687 28.776 6.274 1.00 27.46 ? 111 MET A CE 1 ATOM 597 N N . ASP A 1 77 ? 33.494 32.934 2.553 1.00 33.50 ? 112 ASP A N 1 ATOM 598 C CA . ASP A 1 77 ? 33.409 32.976 1.132 1.00 30.94 ? 112 ASP A CA 1 ATOM 599 C C . ASP A 1 77 ? 33.712 34.344 0.561 1.00 28.95 ? 112 ASP A C 1 ATOM 600 O O . ASP A 1 77 ? 34.356 34.386 -0.454 1.00 32.53 ? 112 ASP A O 1 ATOM 601 C CB . ASP A 1 77 ? 31.992 32.407 0.715 1.00 39.05 ? 112 ASP A CB 1 ATOM 602 C CG . ASP A 1 77 ? 31.796 32.450 -0.792 1.00 44.92 ? 112 ASP A CG 1 ATOM 603 O OD1 . ASP A 1 77 ? 32.307 31.554 -1.486 1.00 43.70 ? 112 ASP A OD1 1 ATOM 604 O OD2 . ASP A 1 77 ? 31.221 33.432 -1.253 1.00 46.72 ? 112 ASP A OD2 1 ATOM 605 N N . ASP A 1 78 ? 33.301 35.467 1.203 1.00 25.33 ? 113 ASP A N 1 ATOM 606 C CA . ASP A 1 78 ? 33.633 36.774 0.722 1.00 25.65 ? 113 ASP A CA 1 ATOM 607 C C . ASP A 1 78 ? 35.179 37.001 0.813 1.00 29.01 ? 113 ASP A C 1 ATOM 608 O O . ASP A 1 78 ? 35.791 37.604 -0.072 1.00 28.80 ? 113 ASP A O 1 ATOM 609 C CB . ASP A 1 78 ? 33.036 37.809 1.639 1.00 27.54 ? 113 ASP A CB 1 ATOM 610 C CG . ASP A 1 78 ? 31.499 37.994 1.434 1.00 34.17 ? 113 ASP A CG 1 ATOM 611 O OD1 . ASP A 1 78 ? 30.988 37.665 0.346 1.00 30.74 ? 113 ASP A OD1 1 ATOM 612 O OD2 . ASP A 1 78 ? 30.855 38.502 2.339 1.00 33.53 ? 113 ASP A OD2 1 ATOM 613 N N . HIS A 1 79 ? 35.769 36.604 1.936 1.00 27.82 ? 114 HIS A N 1 ATOM 614 C CA . HIS A 1 79 ? 37.232 36.811 2.106 1.00 27.38 ? 114 HIS A CA 1 ATOM 615 C C . HIS A 1 79 ? 38.027 36.048 1.038 1.00 25.37 ? 114 HIS A C 1 ATOM 616 O O . HIS A 1 79 ? 39.026 36.541 0.513 1.00 30.48 ? 114 HIS A O 1 ATOM 617 C CB . HIS A 1 79 ? 37.577 36.324 3.527 1.00 26.45 ? 114 HIS A CB 1 ATOM 618 C CG . HIS A 1 79 ? 38.929 36.776 4.011 1.00 28.01 ? 114 HIS A CG 1 ATOM 619 N ND1 . HIS A 1 79 ? 39.326 38.050 3.927 1.00 28.56 ? 114 HIS A ND1 1 ATOM 620 C CD2 . HIS A 1 79 ? 39.953 36.076 4.664 1.00 27.06 ? 114 HIS A CD2 1 ATOM 621 C CE1 . HIS A 1 79 ? 40.579 38.173 4.471 1.00 25.05 ? 114 HIS A CE1 1 ATOM 622 N NE2 . HIS A 1 79 ? 40.958 36.958 4.906 1.00 28.01 ? 114 HIS A NE2 1 ATOM 623 N N . PHE A 1 80 ? 37.615 34.806 0.733 1.00 24.19 ? 115 PHE A N 1 ATOM 624 C CA . PHE A 1 80 ? 38.198 34.065 -0.392 1.00 26.56 ? 115 PHE A CA 1 ATOM 625 C C . PHE A 1 80 ? 38.059 34.785 -1.754 1.00 29.70 ? 115 PHE A C 1 ATOM 626 O O . PHE A 1 80 ? 39.050 35.012 -2.536 1.00 29.73 ? 115 PHE A O 1 ATOM 627 C CB . PHE A 1 80 ? 37.582 32.649 -0.518 1.00 26.20 ? 115 PHE A CB 1 ATOM 628 C CG . PHE A 1 80 ? 38.269 31.829 -1.564 1.00 29.37 ? 115 PHE A CG 1 ATOM 629 C CD1 . PHE A 1 80 ? 39.435 31.080 -1.243 1.00 29.67 ? 115 PHE A CD1 1 ATOM 630 C CD2 . PHE A 1 80 ? 37.838 31.892 -2.891 1.00 32.00 ? 115 PHE A CD2 1 ATOM 631 C CE1 . PHE A 1 80 ? 40.102 30.353 -2.199 1.00 29.84 ? 115 PHE A CE1 1 ATOM 632 C CE2 . PHE A 1 80 ? 38.490 31.144 -3.853 1.00 34.69 ? 115 PHE A CE2 1 ATOM 633 C CZ . PHE A 1 80 ? 39.620 30.395 -3.533 1.00 35.47 ? 115 PHE A CZ 1 ATOM 634 N N . THR A 1 81 ? 36.824 35.191 -2.032 1.00 31.56 ? 116 THR A N 1 ATOM 635 C CA . THR A 1 81 ? 36.564 36.025 -3.224 1.00 27.95 ? 116 THR A CA 1 ATOM 636 C C . THR A 1 81 ? 37.465 37.195 -3.304 1.00 29.09 ? 116 THR A C 1 ATOM 637 O O . THR A 1 81 ? 37.929 37.477 -4.380 1.00 28.73 ? 116 THR A O 1 ATOM 638 C CB . THR A 1 81 ? 35.134 36.539 -3.173 1.00 31.84 ? 116 THR A CB 1 ATOM 639 O OG1 . THR A 1 81 ? 34.300 35.398 -3.304 1.00 30.81 ? 116 THR A OG1 1 ATOM 640 C CG2 . THR A 1 81 ? 34.833 37.649 -4.231 1.00 32.72 ? 116 THR A CG2 1 ATOM 641 N N . ASN A 1 82 ? 37.732 37.882 -2.177 1.00 26.05 ? 117 ASN A N 1 ATOM 642 C CA . ASN A 1 82 ? 38.503 39.095 -2.212 1.00 27.79 ? 117 ASN A CA 1 ATOM 643 C C . ASN A 1 82 ? 40.010 38.859 -2.337 1.00 25.76 ? 117 ASN A C 1 ATOM 644 O O . ASN A 1 82 ? 40.734 39.638 -2.996 1.00 27.27 ? 117 ASN A O 1 ATOM 645 C CB . ASN A 1 82 ? 38.293 39.881 -0.938 1.00 27.77 ? 117 ASN A CB 1 ATOM 646 C CG . ASN A 1 82 ? 36.842 40.306 -0.742 1.00 36.12 ? 117 ASN A CG 1 ATOM 647 O OD1 . ASN A 1 82 ? 36.069 40.468 -1.736 1.00 31.23 ? 117 ASN A OD1 1 ATOM 648 N ND2 . ASN A 1 82 ? 36.464 40.535 0.531 1.00 28.28 ? 117 ASN A ND2 1 ATOM 649 N N . LEU A 1 83 ? 40.493 37.814 -1.655 1.00 27.32 ? 118 LEU A N 1 ATOM 650 C CA . LEU A 1 83 ? 41.950 37.583 -1.640 1.00 27.67 ? 118 LEU A CA 1 ATOM 651 C C . LEU A 1 83 ? 42.453 36.663 -2.759 1.00 26.94 ? 118 LEU A C 1 ATOM 652 O O . LEU A 1 83 ? 43.648 36.773 -3.160 1.00 27.25 ? 118 LEU A O 1 ATOM 653 C CB . LEU A 1 83 ? 42.400 36.980 -0.272 1.00 26.60 ? 118 LEU A CB 1 ATOM 654 C CG . LEU A 1 83 ? 42.310 37.935 0.908 1.00 29.82 ? 118 LEU A CG 1 ATOM 655 C CD1 . LEU A 1 83 ? 42.857 37.310 2.182 1.00 30.84 ? 118 LEU A CD1 1 ATOM 656 C CD2 . LEU A 1 83 ? 43.024 39.221 0.631 1.00 30.83 ? 118 LEU A CD2 1 ATOM 657 N N . TYR A 1 84 ? 41.596 35.760 -3.221 1.00 26.18 ? 119 TYR A N 1 ATOM 658 C CA . TYR A 1 84 ? 42.016 34.840 -4.329 1.00 29.21 ? 119 TYR A CA 1 ATOM 659 C C . TYR A 1 84 ? 42.726 35.615 -5.467 1.00 29.40 ? 119 TYR A C 1 ATOM 660 O O . TYR A 1 84 ? 43.851 35.269 -5.840 1.00 26.40 ? 119 TYR A O 1 ATOM 661 C CB . TYR A 1 84 ? 40.837 34.008 -4.845 1.00 31.04 ? 119 TYR A CB 1 ATOM 662 C CG . TYR A 1 84 ? 41.246 33.033 -5.948 1.00 37.95 ? 119 TYR A CG 1 ATOM 663 C CD1 . TYR A 1 84 ? 41.812 31.813 -5.615 1.00 36.14 ? 119 TYR A CD1 1 ATOM 664 C CD2 . TYR A 1 84 ? 41.067 33.344 -7.315 1.00 38.01 ? 119 TYR A CD2 1 ATOM 665 C CE1 . TYR A 1 84 ? 42.190 30.905 -6.596 1.00 40.20 ? 119 TYR A CE1 1 ATOM 666 C CE2 . TYR A 1 84 ? 41.463 32.465 -8.314 1.00 39.24 ? 119 TYR A CE2 1 ATOM 667 C CZ . TYR A 1 84 ? 42.000 31.233 -7.948 1.00 41.19 ? 119 TYR A CZ 1 ATOM 668 O OH . TYR A 1 84 ? 42.418 30.323 -8.890 1.00 41.20 ? 119 TYR A OH 1 ATOM 669 N N . PRO A 1 85 ? 42.121 36.687 -6.014 1.00 28.53 ? 120 PRO A N 1 ATOM 670 C CA . PRO A 1 85 ? 42.759 37.397 -7.168 1.00 26.14 ? 120 PRO A CA 1 ATOM 671 C C . PRO A 1 85 ? 43.902 38.281 -6.804 1.00 29.54 ? 120 PRO A C 1 ATOM 672 O O . PRO A 1 85 ? 44.645 38.702 -7.689 1.00 29.55 ? 120 PRO A O 1 ATOM 673 C CB . PRO A 1 85 ? 41.594 38.296 -7.714 1.00 31.16 ? 120 PRO A CB 1 ATOM 674 C CG . PRO A 1 85 ? 40.775 38.493 -6.489 1.00 26.55 ? 120 PRO A CG 1 ATOM 675 C CD . PRO A 1 85 ? 40.721 37.137 -5.847 1.00 29.29 ? 120 PRO A CD 1 ATOM 676 N N . GLN A 1 86 ? 44.042 38.601 -5.506 1.00 27.37 ? 121 GLN A N 1 ATOM 677 C CA . GLN A 1 86 ? 45.221 39.274 -5.022 1.00 31.08 ? 121 GLN A CA 1 ATOM 678 C C . GLN A 1 86 ? 46.411 38.327 -5.133 1.00 31.08 ? 121 GLN A C 1 ATOM 679 O O . GLN A 1 86 ? 47.545 38.777 -5.225 1.00 34.55 ? 121 GLN A O 1 ATOM 680 C CB . GLN A 1 86 ? 45.051 39.758 -3.550 1.00 26.96 ? 121 GLN A CB 1 ATOM 681 C CG . GLN A 1 86 ? 43.922 40.811 -3.344 1.00 27.65 ? 121 GLN A CG 1 ATOM 682 C CD . GLN A 1 86 ? 44.227 42.069 -4.111 1.00 29.35 ? 121 GLN A CD 1 ATOM 683 O OE1 . GLN A 1 86 ? 45.406 42.381 -4.340 1.00 30.78 ? 121 GLN A OE1 1 ATOM 684 N NE2 . GLN A 1 86 ? 43.189 42.790 -4.575 1.00 28.43 ? 121 GLN A NE2 1 ATOM 685 N N . LEU A 1 87 ? 46.176 37.037 -5.010 1.00 28.18 ? 122 LEU A N 1 ATOM 686 C CA . LEU A 1 87 ? 47.362 36.154 -5.038 1.00 26.58 ? 122 LEU A CA 1 ATOM 687 C C . LEU A 1 87 ? 47.486 35.386 -6.352 1.00 29.73 ? 122 LEU A C 1 ATOM 688 O O . LEU A 1 87 ? 48.603 35.041 -6.776 1.00 28.16 ? 122 LEU A O 1 ATOM 689 C CB . LEU A 1 87 ? 47.330 35.141 -3.862 1.00 26.98 ? 122 LEU A CB 1 ATOM 690 C CG . LEU A 1 87 ? 47.704 35.679 -2.481 1.00 31.42 ? 122 LEU A CG 1 ATOM 691 C CD1 . LEU A 1 87 ? 46.525 36.317 -1.776 1.00 34.94 ? 122 LEU A CD1 1 ATOM 692 C CD2 . LEU A 1 87 ? 48.033 34.386 -1.748 1.00 35.96 ? 122 LEU A CD2 1 ATOM 693 N N . ILE A 1 88 ? 46.356 35.056 -6.952 1.00 27.51 ? 123 ILE A N 1 ATOM 694 C CA . ILE A 1 88 ? 46.357 34.125 -8.106 1.00 31.39 ? 123 ILE A CA 1 ATOM 695 C C . ILE A 1 88 ? 45.787 34.931 -9.303 1.00 32.84 ? 123 ILE A C 1 ATOM 696 O O . ILE A 1 88 ? 44.583 35.318 -9.305 1.00 32.66 ? 123 ILE A O 1 ATOM 697 C CB . ILE A 1 88 ? 45.422 32.875 -7.914 1.00 35.56 ? 123 ILE A CB 1 ATOM 698 C CG1 . ILE A 1 88 ? 45.761 32.033 -6.652 1.00 34.09 ? 123 ILE A CG1 1 ATOM 699 C CG2 . ILE A 1 88 ? 45.431 32.001 -9.189 1.00 37.68 ? 123 ILE A CG2 1 ATOM 700 C CD1 . ILE A 1 88 ? 47.224 31.654 -6.596 1.00 37.69 ? 123 ILE A CD1 1 ATOM 701 N N . LYS A 1 89 ? 46.626 35.232 -10.279 1.00 30.57 ? 124 LYS A N 1 ATOM 702 C CA . LYS A 1 89 ? 46.063 35.824 -11.515 1.00 40.89 ? 124 LYS A CA 1 ATOM 703 C C . LYS A 1 89 ? 46.162 34.901 -12.732 1.00 39.21 ? 124 LYS A C 1 ATOM 704 O O . LYS A 1 89 ? 45.571 35.220 -13.746 1.00 40.28 ? 124 LYS A O 1 ATOM 705 C CB . LYS A 1 89 ? 46.759 37.126 -11.898 1.00 45.13 ? 124 LYS A CB 1 ATOM 706 C CG . LYS A 1 89 ? 46.517 38.307 -10.943 1.00 49.27 ? 124 LYS A CG 1 ATOM 707 C CD . LYS A 1 89 ? 47.882 38.896 -10.667 1.00 50.12 ? 124 LYS A CD 1 ATOM 708 C CE . LYS A 1 89 ? 48.548 38.276 -9.441 1.00 57.16 ? 124 LYS A CE 1 ATOM 709 N NZ . LYS A 1 89 ? 48.266 39.195 -8.292 1.00 56.79 ? 124 LYS A NZ 1 ATOM 710 N N . LYS A 1 90 ? 46.958 33.828 -12.636 1.00 35.43 ? 125 LYS A N 1 ATOM 711 C CA . LYS A 1 90 ? 47.212 32.930 -13.790 1.00 36.49 ? 125 LYS A CA 1 ATOM 712 C C . LYS A 1 90 ? 46.942 31.471 -13.338 1.00 37.20 ? 125 LYS A C 1 ATOM 713 O O . LYS A 1 90 ? 47.223 31.110 -12.159 1.00 23.52 ? 125 LYS A O 1 ATOM 714 C CB . LYS A 1 90 ? 48.676 33.025 -14.244 1.00 37.89 ? 125 LYS A CB 1 ATOM 715 C CG . LYS A 1 90 ? 49.182 34.409 -14.677 1.00 41.50 ? 125 LYS A CG 1 ATOM 716 C CD . LYS A 1 90 ? 48.347 34.955 -15.814 1.00 43.73 ? 125 LYS A CD 1 ATOM 717 C CE . LYS A 1 90 ? 48.722 36.413 -16.130 1.00 40.87 ? 125 LYS A CE 1 ATOM 718 N NZ . LYS A 1 90 ? 50.125 36.652 -16.546 1.00 34.56 ? 125 LYS A NZ 1 ATOM 719 N N . ARG A 1 91 ? 46.368 30.646 -14.226 1.00 37.52 ? 126 ARG A N 1 ATOM 720 C CA . ARG A 1 91 ? 46.049 29.258 -13.846 1.00 38.32 ? 126 ARG A CA 1 ATOM 721 C C . ARG A 1 91 ? 47.330 28.511 -13.565 1.00 36.40 ? 126 ARG A C 1 ATOM 722 O O . ARG A 1 91 ? 47.364 27.600 -12.728 1.00 31.85 ? 126 ARG A O 1 ATOM 723 C CB . ARG A 1 91 ? 45.176 28.530 -14.898 1.00 45.77 ? 126 ARG A CB 1 ATOM 724 C CG . ARG A 1 91 ? 45.087 27.031 -14.655 1.00 43.80 ? 126 ARG A CG 1 ATOM 725 C CD . ARG A 1 91 ? 43.949 26.496 -15.449 1.00 61.20 ? 126 ARG A CD 1 ATOM 726 N NE . ARG A 1 91 ? 42.695 26.797 -14.824 1.00 63.83 ? 126 ARG A NE 1 ATOM 727 C CZ . ARG A 1 91 ? 41.886 25.860 -14.346 1.00 79.17 ? 126 ARG A CZ 1 ATOM 728 N NH1 . ARG A 1 91 ? 42.234 24.572 -14.438 1.00 82.67 ? 126 ARG A NH1 1 ATOM 729 N NH2 . ARG A 1 91 ? 40.727 26.205 -13.785 1.00 67.87 ? 126 ARG A NH2 1 ATOM 730 N N . SER A 1 92 ? 48.418 28.916 -14.211 1.00 35.27 ? 127 SER A N 1 ATOM 731 C CA . SER A 1 92 ? 49.765 28.412 -13.866 1.00 33.23 ? 127 SER A CA 1 ATOM 732 C C . SER A 1 92 ? 50.133 28.527 -12.419 1.00 39.94 ? 127 SER A C 1 ATOM 733 O O . SER A 1 92 ? 50.752 27.583 -11.838 1.00 40.50 ? 127 SER A O 1 ATOM 734 C CB . SER A 1 92 ? 50.834 29.173 -14.675 1.00 41.52 ? 127 SER A CB 1 ATOM 735 O OG . SER A 1 92 ? 51.392 30.278 -13.936 1.00 45.51 ? 127 SER A OG 1 ATOM 736 N N . MET A 1 93 ? 49.802 29.694 -11.816 1.00 36.09 ? 128 MET A N 1 ATOM 737 C CA . MET A 1 93 ? 50.010 29.865 -10.380 1.00 32.36 ? 128 MET A CA 1 ATOM 738 C C . MET A 1 93 ? 49.073 28.976 -9.600 1.00 30.76 ? 128 MET A C 1 ATOM 739 O O . MET A 1 93 ? 49.489 28.382 -8.589 1.00 32.13 ? 128 MET A O 1 ATOM 740 C CB . MET A 1 93 ? 49.874 31.339 -9.900 1.00 30.49 ? 128 MET A CB 1 ATOM 741 C CG . MET A 1 93 ? 50.910 32.290 -10.540 1.00 35.75 ? 128 MET A CG 1 ATOM 742 S SD . MET A 1 93 ? 50.493 34.035 -10.076 1.00 43.76 ? 128 MET A SD 1 ATOM 743 C CE . MET A 1 93 ? 49.036 34.290 -10.978 1.00 28.89 ? 128 MET A CE 1 ATOM 744 N N . LEU A 1 94 ? 47.816 28.867 -10.059 1.00 26.36 ? 129 LEU A N 1 ATOM 745 C CA . LEU A 1 94 ? 46.860 28.065 -9.318 1.00 28.31 ? 129 LEU A CA 1 ATOM 746 C C . LEU A 1 94 ? 47.455 26.607 -9.308 1.00 26.77 ? 129 LEU A C 1 ATOM 747 O O . LEU A 1 94 ? 47.465 25.931 -8.261 1.00 25.81 ? 129 LEU A O 1 ATOM 748 C CB . LEU A 1 94 ? 45.450 28.138 -9.899 1.00 27.17 ? 129 LEU A CB 1 ATOM 749 C CG . LEU A 1 94 ? 44.444 27.155 -9.235 1.00 28.07 ? 129 LEU A CG 1 ATOM 750 C CD1 . LEU A 1 94 ? 44.267 27.455 -7.736 1.00 27.57 ? 129 LEU A CD1 1 ATOM 751 C CD2 . LEU A 1 94 ? 43.078 27.227 -9.900 1.00 27.27 ? 129 LEU A CD2 1 ATOM 752 N N . ASN A 1 95 ? 47.978 26.150 -10.453 1.00 24.93 ? 130 ASN A N 1 ATOM 753 C CA . ASN A 1 95 ? 48.566 24.784 -10.513 1.00 28.89 ? 130 ASN A CA 1 ATOM 754 C C . ASN A 1 95 ? 49.631 24.595 -9.436 1.00 28.40 ? 130 ASN A C 1 ATOM 755 O O . ASN A 1 95 ? 49.617 23.588 -8.729 1.00 31.69 ? 130 ASN A O 1 ATOM 756 C CB . ASN A 1 95 ? 49.244 24.494 -11.862 1.00 25.15 ? 130 ASN A CB 1 ATOM 757 C CG . ASN A 1 95 ? 48.247 24.277 -12.960 1.00 24.87 ? 130 ASN A CG 1 ATOM 758 O OD1 . ASN A 1 95 ? 47.081 23.931 -12.692 1.00 25.80 ? 130 ASN A OD1 1 ATOM 759 N ND2 . ASN A 1 95 ? 48.647 24.552 -14.207 1.00 26.66 ? 130 ASN A ND2 1 ATOM 760 N N . LYS A 1 96 ? 50.558 25.528 -9.333 1.00 29.04 ? 131 LYS A N 1 ATOM 761 C CA . LYS A 1 96 ? 51.643 25.420 -8.379 1.00 30.68 ? 131 LYS A CA 1 ATOM 762 C C . LYS A 1 96 ? 51.121 25.336 -6.938 1.00 27.41 ? 131 LYS A C 1 ATOM 763 O O . LYS A 1 96 ? 51.599 24.559 -6.117 1.00 26.47 ? 131 LYS A O 1 ATOM 764 C CB . LYS A 1 96 ? 52.560 26.659 -8.495 1.00 41.17 ? 131 LYS A CB 1 ATOM 765 C CG . LYS A 1 96 ? 53.653 26.585 -9.573 1.00 56.50 ? 131 LYS A CG 1 ATOM 766 C CD . LYS A 1 96 ? 54.933 27.304 -9.048 1.00 72.74 ? 131 LYS A CD 1 ATOM 767 C CE . LYS A 1 96 ? 56.021 27.544 -10.118 1.00 71.47 ? 131 LYS A CE 1 ATOM 768 N NZ . LYS A 1 96 ? 57.406 27.828 -9.638 1.00 56.74 ? 131 LYS A NZ 1 ATOM 769 N N . VAL A 1 97 ? 50.150 26.175 -6.646 1.00 24.78 ? 132 VAL A N 1 ATOM 770 C CA . VAL A 1 97 ? 49.574 26.334 -5.305 1.00 30.72 ? 132 VAL A CA 1 ATOM 771 C C . VAL A 1 97 ? 48.763 25.066 -4.926 1.00 32.70 ? 132 VAL A C 1 ATOM 772 O O . VAL A 1 97 ? 48.929 24.506 -3.831 1.00 28.84 ? 132 VAL A O 1 ATOM 773 C CB . VAL A 1 97 ? 48.739 27.643 -5.217 1.00 30.95 ? 132 VAL A CB 1 ATOM 774 C CG1 . VAL A 1 97 ? 47.845 27.681 -4.004 1.00 36.00 ? 132 VAL A CG1 1 ATOM 775 C CG2 . VAL A 1 97 ? 49.689 28.821 -5.168 1.00 34.50 ? 132 VAL A CG2 1 ATOM 776 N N . GLN A 1 98 ? 47.942 24.591 -5.854 1.00 25.30 ? 133 GLN A N 1 ATOM 777 C CA . GLN A 1 98 ? 47.136 23.372 -5.581 1.00 29.25 ? 133 GLN A CA 1 ATOM 778 C C . GLN A 1 98 ? 48.055 22.236 -5.281 1.00 24.88 ? 133 GLN A C 1 ATOM 779 O O . GLN A 1 98 ? 47.848 21.504 -4.335 1.00 30.36 ? 133 GLN A O 1 ATOM 780 C CB . GLN A 1 98 ? 46.254 22.975 -6.787 1.00 30.04 ? 133 GLN A CB 1 ATOM 781 C CG . GLN A 1 98 ? 44.901 23.678 -6.733 1.00 33.86 ? 133 GLN A CG 1 ATOM 782 C CD . GLN A 1 98 ? 44.076 23.535 -8.008 1.00 35.48 ? 133 GLN A CD 1 ATOM 783 O OE1 . GLN A 1 98 ? 44.615 23.452 -9.107 1.00 36.29 ? 133 GLN A OE1 1 ATOM 784 N NE2 . GLN A 1 98 ? 42.772 23.551 -7.860 1.00 40.41 ? 133 GLN A NE2 1 ATOM 785 N N . ASP A 1 99 ? 49.024 22.044 -6.137 1.00 26.13 ? 134 ASP A N 1 ATOM 786 C CA . ASP A 1 99 ? 49.994 20.954 -5.947 1.00 29.09 ? 134 ASP A CA 1 ATOM 787 C C . ASP A 1 99 ? 50.717 21.049 -4.585 1.00 31.48 ? 134 ASP A C 1 ATOM 788 O O . ASP A 1 99 ? 50.857 20.050 -3.860 1.00 28.36 ? 134 ASP A O 1 ATOM 789 C CB . ASP A 1 99 ? 51.021 20.952 -7.094 1.00 31.13 ? 134 ASP A CB 1 ATOM 790 C CG . ASP A 1 99 ? 52.006 19.769 -6.995 1.00 37.65 ? 134 ASP A CG 1 ATOM 791 O OD1 . ASP A 1 99 ? 51.540 18.616 -7.087 1.00 40.15 ? 134 ASP A OD1 1 ATOM 792 O OD2 . ASP A 1 99 ? 53.229 19.981 -6.782 1.00 38.32 ? 134 ASP A OD2 1 ATOM 793 N N . PHE A 1 100 ? 51.297 22.208 -4.286 1.00 28.06 ? 135 PHE A N 1 ATOM 794 C CA . PHE A 1 100 ? 51.951 22.346 -2.958 1.00 27.66 ? 135 PHE A CA 1 ATOM 795 C C . PHE A 1 100 ? 50.975 22.081 -1.802 1.00 26.53 ? 135 PHE A C 1 ATOM 796 O O . PHE A 1 100 ? 51.319 21.340 -0.868 1.00 27.48 ? 135 PHE A O 1 ATOM 797 C CB . PHE A 1 100 ? 52.555 23.765 -2.821 1.00 27.35 ? 135 PHE A CB 1 ATOM 798 C CG . PHE A 1 100 ? 53.505 23.907 -1.666 1.00 29.34 ? 135 PHE A CG 1 ATOM 799 C CD1 . PHE A 1 100 ? 54.851 23.651 -1.842 1.00 29.85 ? 135 PHE A CD1 1 ATOM 800 C CD2 . PHE A 1 100 ? 53.028 24.333 -0.401 1.00 34.68 ? 135 PHE A CD2 1 ATOM 801 C CE1 . PHE A 1 100 ? 55.755 23.796 -0.790 1.00 36.42 ? 135 PHE A CE1 1 ATOM 802 C CE2 . PHE A 1 100 ? 53.932 24.510 0.654 1.00 33.30 ? 135 PHE A CE2 1 ATOM 803 C CZ . PHE A 1 100 ? 55.286 24.224 0.445 1.00 33.21 ? 135 PHE A CZ 1 ATOM 804 N N . LEU A 1 101 ? 49.796 22.719 -1.775 1.00 25.53 ? 136 LEU A N 1 ATOM 805 C CA . LEU A 1 101 ? 48.961 22.534 -0.597 1.00 24.66 ? 136 LEU A CA 1 ATOM 806 C C . LEU A 1 101 ? 48.485 21.098 -0.522 1.00 31.41 ? 136 LEU A C 1 ATOM 807 O O . LEU A 1 101 ? 48.320 20.555 0.586 1.00 31.27 ? 136 LEU A O 1 ATOM 808 C CB . LEU A 1 101 ? 47.736 23.484 -0.539 1.00 25.62 ? 136 LEU A CB 1 ATOM 809 C CG . LEU A 1 101 ? 48.180 24.940 -0.568 1.00 29.09 ? 136 LEU A CG 1 ATOM 810 C CD1 . LEU A 1 101 ? 46.939 25.775 -0.509 1.00 31.21 ? 136 LEU A CD1 1 ATOM 811 C CD2 . LEU A 1 101 ? 48.983 25.226 0.697 1.00 34.63 ? 136 LEU A CD2 1 ATOM 812 N N . THR A 1 102 ? 48.237 20.467 -1.665 1.00 28.84 ? 137 THR A N 1 ATOM 813 C CA . THR A 1 102 ? 47.793 19.043 -1.622 1.00 31.92 ? 137 THR A CA 1 ATOM 814 C C . THR A 1 102 ? 48.896 18.145 -1.037 1.00 27.97 ? 137 THR A C 1 ATOM 815 O O . THR A 1 102 ? 48.617 17.345 -0.145 1.00 34.47 ? 137 THR A O 1 ATOM 816 C CB . THR A 1 102 ? 47.315 18.532 -2.993 1.00 34.44 ? 137 THR A CB 1 ATOM 817 O OG1 . THR A 1 102 ? 46.234 19.364 -3.421 1.00 31.77 ? 137 THR A OG1 1 ATOM 818 C CG2 . THR A 1 102 ? 46.677 17.177 -2.828 1.00 29.26 ? 137 THR A CG2 1 ATOM 819 N N . LYS A 1 103 ? 50.129 18.297 -1.500 1.00 28.37 ? 138 LYS A N 1 ATOM 820 C CA . LYS A 1 103 ? 51.243 17.460 -1.006 1.00 26.41 ? 138 LYS A CA 1 ATOM 821 C C . LYS A 1 103 ? 51.525 17.743 0.494 1.00 31.74 ? 138 LYS A C 1 ATOM 822 O O . LYS A 1 103 ? 51.880 16.843 1.327 1.00 29.39 ? 138 LYS A O 1 ATOM 823 C CB . LYS A 1 103 ? 52.490 17.669 -1.862 1.00 27.88 ? 138 LYS A CB 1 ATOM 824 C CG . LYS A 1 103 ? 52.363 16.950 -3.217 1.00 32.12 ? 138 LYS A CG 1 ATOM 825 C CD . LYS A 1 103 ? 53.493 17.320 -4.122 1.00 33.97 ? 138 LYS A CD 1 ATOM 826 C CE . LYS A 1 103 ? 53.287 16.543 -5.418 1.00 43.23 ? 138 LYS A CE 1 ATOM 827 N NZ . LYS A 1 103 ? 54.074 17.334 -6.390 1.00 45.19 ? 138 LYS A NZ 1 ATOM 828 N N . GLN A 1 104 ? 51.326 19.008 0.858 1.00 28.86 ? 139 GLN A N 1 ATOM 829 C CA . GLN A 1 104 ? 51.642 19.420 2.220 1.00 25.55 ? 139 GLN A CA 1 ATOM 830 C C . GLN A 1 104 ? 50.651 18.896 3.192 1.00 26.15 ? 139 GLN A C 1 ATOM 831 O O . GLN A 1 104 ? 51.049 18.454 4.312 1.00 29.82 ? 139 GLN A O 1 ATOM 832 C CB . GLN A 1 104 ? 51.832 20.975 2.288 1.00 25.51 ? 139 GLN A CB 1 ATOM 833 C CG . GLN A 1 104 ? 52.319 21.512 3.683 1.00 22.95 ? 139 GLN A CG 1 ATOM 834 C CD . GLN A 1 104 ? 51.261 21.465 4.783 1.00 21.50 ? 139 GLN A CD 1 ATOM 835 O OE1 . GLN A 1 104 ? 50.055 21.536 4.505 1.00 27.82 ? 139 GLN A OE1 1 ATOM 836 N NE2 . GLN A 1 104 ? 51.707 21.389 6.094 1.00 22.56 ? 139 GLN A NE2 1 ATOM 837 N N . ASP A 1 105 ? 49.368 18.896 2.795 1.00 27.39 ? 140 ASP A N 1 ATOM 838 C CA . ASP A 1 105 ? 48.298 18.433 3.667 1.00 32.31 ? 140 ASP A CA 1 ATOM 839 C C . ASP A 1 105 ? 48.349 16.894 3.837 1.00 37.81 ? 140 ASP A C 1 ATOM 840 O O . ASP A 1 105 ? 48.217 16.342 4.967 1.00 35.14 ? 140 ASP A O 1 ATOM 841 C CB . ASP A 1 105 ? 46.935 18.837 3.189 1.00 26.64 ? 140 ASP A CB 1 ATOM 842 C CG . ASP A 1 105 ? 45.862 18.586 4.226 1.00 36.66 ? 140 ASP A CG 1 ATOM 843 O OD1 . ASP A 1 105 ? 45.946 19.216 5.335 1.00 33.74 ? 140 ASP A OD1 1 ATOM 844 O OD2 . ASP A 1 105 ? 44.909 17.774 3.951 1.00 34.65 ? 140 ASP A OD2 1 ATOM 845 N N . GLN A 1 106 ? 48.621 16.232 2.733 1.00 33.77 ? 141 GLN A N 1 ATOM 846 C CA . GLN A 1 106 ? 48.818 14.787 2.761 1.00 38.13 ? 141 GLN A CA 1 ATOM 847 C C . GLN A 1 106 ? 49.982 14.389 3.661 1.00 35.45 ? 141 GLN A C 1 ATOM 848 O O . GLN A 1 106 ? 49.860 13.477 4.485 1.00 36.96 ? 141 GLN A O 1 ATOM 849 C CB . GLN A 1 106 ? 48.996 14.289 1.324 1.00 38.79 ? 141 GLN A CB 1 ATOM 850 C CG . GLN A 1 106 ? 48.615 12.833 1.173 1.00 60.54 ? 141 GLN A CG 1 ATOM 851 C CD . GLN A 1 106 ? 49.548 12.123 0.223 1.00 71.42 ? 141 GLN A CD 1 ATOM 852 O OE1 . GLN A 1 106 ? 49.998 12.722 -0.772 1.00 79.82 ? 141 GLN A OE1 1 ATOM 853 N NE2 . GLN A 1 106 ? 49.877 10.851 0.530 1.00 77.83 ? 141 GLN A NE2 1 ATOM 854 N N . TRP A 1 107 ? 51.112 15.032 3.507 1.00 31.06 ? 142 TRP A N 1 ATOM 855 C CA . TRP A 1 107 ? 52.232 14.841 4.390 1.00 34.10 ? 142 TRP A CA 1 ATOM 856 C C . TRP A 1 107 ? 51.921 15.124 5.894 1.00 34.93 ? 142 TRP A C 1 ATOM 857 O O . TRP A 1 107 ? 52.333 14.334 6.780 1.00 33.77 ? 142 TRP A O 1 ATOM 858 C CB . TRP A 1 107 ? 53.380 15.682 3.910 1.00 32.79 ? 142 TRP A CB 1 ATOM 859 C CG . TRP A 1 107 ? 54.587 15.576 4.791 1.00 32.33 ? 142 TRP A CG 1 ATOM 860 C CD1 . TRP A 1 107 ? 55.640 14.696 4.667 1.00 34.77 ? 142 TRP A CD1 1 ATOM 861 C CD2 . TRP A 1 107 ? 54.919 16.408 5.964 1.00 35.30 ? 142 TRP A CD2 1 ATOM 862 N NE1 . TRP A 1 107 ? 56.567 14.914 5.635 1.00 37.27 ? 142 TRP A NE1 1 ATOM 863 C CE2 . TRP A 1 107 ? 56.210 15.934 6.439 1.00 34.76 ? 142 TRP A CE2 1 ATOM 864 C CE3 . TRP A 1 107 ? 54.295 17.467 6.623 1.00 33.77 ? 142 TRP A CE3 1 ATOM 865 C CZ2 . TRP A 1 107 ? 56.850 16.489 7.556 1.00 33.41 ? 142 TRP A CZ2 1 ATOM 866 C CZ3 . TRP A 1 107 ? 54.939 18.028 7.762 1.00 33.20 ? 142 TRP A CZ3 1 ATOM 867 C CH2 . TRP A 1 107 ? 56.189 17.546 8.207 1.00 25.68 ? 142 TRP A CH2 1 ATOM 868 N N . THR A 1 108 ? 51.209 16.214 6.178 1.00 29.96 ? 143 THR A N 1 ATOM 869 C CA . THR A 1 108 ? 50.790 16.564 7.540 1.00 30.31 ? 143 THR A CA 1 ATOM 870 C C . THR A 1 108 ? 49.939 15.428 8.139 1.00 34.43 ? 143 THR A C 1 ATOM 871 O O . THR A 1 108 ? 50.240 14.970 9.240 1.00 33.24 ? 143 THR A O 1 ATOM 872 C CB . THR A 1 108 ? 50.055 17.948 7.630 1.00 29.68 ? 143 THR A CB 1 ATOM 873 O OG1 . THR A 1 108 ? 50.962 18.987 7.175 1.00 26.57 ? 143 THR A OG1 1 ATOM 874 C CG2 . THR A 1 108 ? 49.684 18.288 9.033 1.00 29.14 ? 143 THR A CG2 1 ATOM 875 N N . ARG A 1 109 ? 48.944 14.943 7.403 1.00 31.01 ? 144 ARG A N 1 ATOM 876 C CA . ARG A 1 109 ? 47.999 13.893 7.892 1.00 36.34 ? 144 ARG A CA 1 ATOM 877 C C . ARG A 1 109 ? 48.658 12.562 8.155 1.00 37.10 ? 144 ARG A C 1 ATOM 878 O O . ARG A 1 109 ? 48.321 11.884 9.157 1.00 36.29 ? 144 ARG A O 1 ATOM 879 C CB . ARG A 1 109 ? 46.794 13.765 6.940 1.00 33.12 ? 144 ARG A CB 1 ATOM 880 C CG . ARG A 1 109 ? 45.972 15.063 6.986 1.00 34.83 ? 144 ARG A CG 1 ATOM 881 C CD . ARG A 1 109 ? 44.757 14.956 6.100 1.00 36.40 ? 144 ARG A CD 1 ATOM 882 N NE . ARG A 1 109 ? 44.012 16.211 6.001 1.00 38.29 ? 144 ARG A NE 1 ATOM 883 C CZ . ARG A 1 109 ? 43.077 16.616 6.859 1.00 38.13 ? 144 ARG A CZ 1 ATOM 884 N NH1 . ARG A 1 109 ? 42.778 15.891 7.946 1.00 41.15 ? 144 ARG A NH1 1 ATOM 885 N NH2 . ARG A 1 109 ? 42.455 17.777 6.679 1.00 34.11 ? 144 ARG A NH2 1 ATOM 886 N N . GLU A 1 110 ? 49.589 12.199 7.277 1.00 35.88 ? 145 GLU A N 1 ATOM 887 C CA . GLU A 1 110 ? 50.374 10.976 7.423 1.00 38.79 ? 145 GLU A CA 1 ATOM 888 C C . GLU A 1 110 ? 51.233 11.055 8.670 1.00 45.77 ? 145 GLU A C 1 ATOM 889 O O . GLU A 1 110 ? 51.365 10.039 9.421 1.00 37.09 ? 145 GLU A O 1 ATOM 890 C CB . GLU A 1 110 ? 51.268 10.727 6.226 1.00 35.41 ? 145 GLU A CB 1 ATOM 891 C CG . GLU A 1 110 ? 50.573 10.412 4.902 1.00 50.86 ? 145 GLU A CG 1 ATOM 892 C CD . GLU A 1 110 ? 49.844 9.074 4.919 1.00 61.49 ? 145 GLU A CD 1 ATOM 893 O OE1 . GLU A 1 110 ? 50.512 8.017 5.064 1.00 71.25 ? 145 GLU A OE1 1 ATOM 894 O OE2 . GLU A 1 110 ? 48.596 9.068 4.806 1.00 75.65 ? 145 GLU A OE2 1 ATOM 895 N N . ASN A 1 111 ? 51.870 12.209 8.911 1.00 34.46 ? 146 ASN A N 1 ATOM 896 C CA . ASN A 1 111 ? 52.649 12.295 10.183 1.00 37.31 ? 146 ASN A CA 1 ATOM 897 C C . ASN A 1 111 ? 51.797 12.230 11.412 1.00 35.16 ? 146 ASN A C 1 ATOM 898 O O . ASN A 1 111 ? 52.185 11.645 12.423 1.00 40.47 ? 146 ASN A O 1 ATOM 899 C CB . ASN A 1 111 ? 53.531 13.556 10.276 1.00 36.18 ? 146 ASN A CB 1 ATOM 900 C CG . ASN A 1 111 ? 54.800 13.407 9.528 1.00 37.27 ? 146 ASN A CG 1 ATOM 901 O OD1 . ASN A 1 111 ? 55.797 12.986 10.076 1.00 40.57 ? 146 ASN A OD1 1 ATOM 902 N ND2 . ASN A 1 111 ? 54.774 13.726 8.234 1.00 43.71 ? 146 ASN A ND2 1 ATOM 903 N N . ILE A 1 112 ? 50.637 12.853 11.368 1.00 33.13 ? 147 ILE A N 1 ATOM 904 C CA . ILE A 1 112 ? 49.766 12.815 12.501 1.00 35.74 ? 147 ILE A CA 1 ATOM 905 C C . ILE A 1 112 ? 49.362 11.350 12.816 1.00 43.96 ? 147 ILE A C 1 ATOM 906 O O . ILE A 1 112 ? 49.446 10.902 13.967 1.00 38.75 ? 147 ILE A O 1 ATOM 907 C CB . ILE A 1 112 ? 48.521 13.656 12.248 1.00 36.78 ? 147 ILE A CB 1 ATOM 908 C CG1 . ILE A 1 112 ? 48.875 15.142 12.467 1.00 35.41 ? 147 ILE A CG1 1 ATOM 909 C CG2 . ILE A 1 112 ? 47.376 13.209 13.155 1.00 37.27 ? 147 ILE A CG2 1 ATOM 910 C CD1 . ILE A 1 112 ? 47.822 16.072 11.887 1.00 31.71 ? 147 ILE A CD1 1 ATOM 911 N N . LYS A 1 113 ? 48.924 10.632 11.788 1.00 40.51 ? 148 LYS A N 1 ATOM 912 C CA . LYS A 1 113 ? 48.669 9.171 11.875 1.00 49.19 ? 148 LYS A CA 1 ATOM 913 C C . LYS A 1 113 ? 49.870 8.342 12.428 1.00 40.42 ? 148 LYS A C 1 ATOM 914 O O . LYS A 1 113 ? 49.716 7.602 13.378 1.00 49.56 ? 148 LYS A O 1 ATOM 915 C CB . LYS A 1 113 ? 48.183 8.648 10.511 1.00 55.23 ? 148 LYS A CB 1 ATOM 916 C CG . LYS A 1 113 ? 47.315 7.391 10.553 1.00 65.92 ? 148 LYS A CG 1 ATOM 917 C CD . LYS A 1 113 ? 46.176 7.475 9.528 1.00 78.95 ? 148 LYS A CD 1 ATOM 918 C CE . LYS A 1 113 ? 45.484 6.130 9.289 1.00 80.66 ? 148 LYS A CE 1 ATOM 919 N NZ . LYS A 1 113 ? 46.349 5.268 8.428 1.00 89.91 ? 148 LYS A NZ 1 ATOM 920 N N . TYR A 1 114 ? 51.048 8.496 11.867 1.00 39.55 ? 149 TYR A N 1 ATOM 921 C CA . TYR A 1 114 ? 52.244 7.819 12.319 1.00 43.63 ? 149 TYR A CA 1 ATOM 922 C C . TYR A 1 114 ? 52.655 8.133 13.767 1.00 50.43 ? 149 TYR A C 1 ATOM 923 O O . TYR A 1 114 ? 52.936 7.220 14.530 1.00 45.02 ? 149 TYR A O 1 ATOM 924 C CB . TYR A 1 114 ? 53.387 8.119 11.387 1.00 47.76 ? 149 TYR A CB 1 ATOM 925 C CG . TYR A 1 114 ? 54.627 7.304 11.641 1.00 56.98 ? 149 TYR A CG 1 ATOM 926 C CD1 . TYR A 1 114 ? 54.742 6.002 11.110 1.00 64.78 ? 149 TYR A CD1 1 ATOM 927 C CD2 . TYR A 1 114 ? 55.687 7.811 12.404 1.00 61.11 ? 149 TYR A CD2 1 ATOM 928 C CE1 . TYR A 1 114 ? 55.871 5.235 11.337 1.00 65.02 ? 149 TYR A CE1 1 ATOM 929 C CE2 . TYR A 1 114 ? 56.819 7.052 12.637 1.00 60.38 ? 149 TYR A CE2 1 ATOM 930 C CZ . TYR A 1 114 ? 56.896 5.762 12.099 1.00 64.16 ? 149 TYR A CZ 1 ATOM 931 O OH . TYR A 1 114 ? 57.995 4.995 12.301 1.00 64.51 ? 149 TYR A OH 1 ATOM 932 N N . TYR A 1 115 ? 52.673 9.409 14.164 1.00 46.49 ? 150 TYR A N 1 ATOM 933 C CA . TYR A 1 115 ? 53.271 9.784 15.438 1.00 43.87 ? 150 TYR A CA 1 ATOM 934 C C . TYR A 1 115 ? 52.240 9.940 16.523 1.00 46.50 ? 150 TYR A C 1 ATOM 935 O O . TYR A 1 115 ? 52.178 10.988 17.198 1.00 43.00 ? 150 TYR A O 1 ATOM 936 C CB . TYR A 1 115 ? 54.075 11.070 15.281 1.00 43.56 ? 150 TYR A CB 1 ATOM 937 C CG . TYR A 1 115 ? 55.404 10.915 14.614 1.00 45.30 ? 150 TYR A CG 1 ATOM 938 C CD1 . TYR A 1 115 ? 56.483 10.369 15.291 1.00 51.06 ? 150 TYR A CD1 1 ATOM 939 C CD2 . TYR A 1 115 ? 55.602 11.365 13.317 1.00 49.26 ? 150 TYR A CD2 1 ATOM 940 C CE1 . TYR A 1 115 ? 57.726 10.240 14.684 1.00 52.19 ? 150 TYR A CE1 1 ATOM 941 C CE2 . TYR A 1 115 ? 56.836 11.254 12.695 1.00 48.90 ? 150 TYR A CE2 1 ATOM 942 C CZ . TYR A 1 115 ? 57.892 10.698 13.385 1.00 54.15 ? 150 TYR A CZ 1 ATOM 943 O OH . TYR A 1 115 ? 59.115 10.598 12.767 1.00 51.14 ? 150 TYR A OH 1 ATOM 944 N N . LYS A 1 116 ? 51.452 8.879 16.740 1.00 54.32 ? 151 LYS A N 1 ATOM 945 C CA . LYS A 1 116 ? 50.360 8.960 17.721 1.00 61.96 ? 151 LYS A CA 1 ATOM 946 C C . LYS A 1 116 ? 50.844 9.029 19.187 1.00 55.69 ? 151 LYS A C 1 ATOM 947 O O . LYS A 1 116 ? 50.158 9.546 20.058 1.00 54.73 ? 151 LYS A O 1 ATOM 948 C CB . LYS A 1 116 ? 49.290 7.888 17.466 1.00 70.21 ? 151 LYS A CB 1 ATOM 949 C CG . LYS A 1 116 ? 48.072 8.485 16.751 1.00 82.41 ? 151 LYS A CG 1 ATOM 950 C CD . LYS A 1 116 ? 47.442 7.493 15.797 1.00 91.13 ? 151 LYS A CD 1 ATOM 951 C CE . LYS A 1 116 ? 46.450 8.161 14.863 1.00 97.01 ? 151 LYS A CE 1 ATOM 952 N NZ . LYS A 1 116 ? 46.055 7.148 13.835 1.00 96.56 ? 151 LYS A NZ 1 ATOM 953 N N . SER A 1 117 ? 52.064 8.584 19.435 1.00 54.17 ? 152 SER A N 1 ATOM 954 C CA . SER A 1 117 ? 52.667 8.765 20.766 1.00 57.91 ? 152 SER A CA 1 ATOM 955 C C . SER A 1 117 ? 53.186 10.200 21.064 1.00 56.67 ? 152 SER A C 1 ATOM 956 O O . SER A 1 117 ? 53.318 10.584 22.219 1.00 53.06 ? 152 SER A O 1 ATOM 957 C CB . SER A 1 117 ? 53.838 7.783 20.931 1.00 64.28 ? 152 SER A CB 1 ATOM 958 O OG . SER A 1 117 ? 53.375 6.448 20.935 1.00 67.70 ? 152 SER A OG 1 ATOM 959 N N . ASP A 1 118 ? 53.512 10.975 20.038 1.00 45.49 ? 153 ASP A N 1 ATOM 960 C CA . ASP A 1 118 ? 54.375 12.146 20.244 1.00 44.46 ? 153 ASP A CA 1 ATOM 961 C C . ASP A 1 118 ? 53.546 13.361 20.676 1.00 39.37 ? 153 ASP A C 1 ATOM 962 O O . ASP A 1 118 ? 52.549 13.681 20.026 1.00 41.70 ? 153 ASP A O 1 ATOM 963 C CB . ASP A 1 118 ? 55.118 12.425 18.953 1.00 46.14 ? 153 ASP A CB 1 ATOM 964 C CG . ASP A 1 118 ? 56.000 13.605 19.062 1.00 49.10 ? 153 ASP A CG 1 ATOM 965 O OD1 . ASP A 1 118 ? 56.983 13.488 19.774 1.00 45.75 ? 153 ASP A OD1 1 ATOM 966 O OD2 . ASP A 1 118 ? 55.710 14.652 18.477 1.00 55.25 ? 153 ASP A OD2 1 ATOM 967 N N . PRO A 1 119 ? 53.931 14.038 21.785 1.00 39.28 ? 154 PRO A N 1 ATOM 968 C CA . PRO A 1 119 ? 53.186 15.241 22.215 1.00 36.92 ? 154 PRO A CA 1 ATOM 969 C C . PRO A 1 119 ? 53.072 16.359 21.124 1.00 32.73 ? 154 PRO A C 1 ATOM 970 O O . PRO A 1 119 ? 51.972 16.970 20.965 1.00 35.33 ? 154 PRO A O 1 ATOM 971 C CB . PRO A 1 119 ? 53.995 15.760 23.439 1.00 41.80 ? 154 PRO A CB 1 ATOM 972 C CG . PRO A 1 119 ? 54.848 14.589 23.867 1.00 44.40 ? 154 PRO A CG 1 ATOM 973 C CD . PRO A 1 119 ? 55.131 13.767 22.637 1.00 37.35 ? 154 PRO A CD 1 ATOM 974 N N . PHE A 1 120 ? 54.145 16.580 20.380 1.00 33.18 ? 155 PHE A N 1 ATOM 975 C CA . PHE A 1 120 ? 54.141 17.587 19.288 1.00 28.47 ? 155 PHE A CA 1 ATOM 976 C C . PHE A 1 120 ? 53.139 17.198 18.218 1.00 29.67 ? 155 PHE A C 1 ATOM 977 O O . PHE A 1 120 ? 52.246 17.953 17.885 1.00 26.59 ? 155 PHE A O 1 ATOM 978 C CB . PHE A 1 120 ? 55.513 17.722 18.678 1.00 29.97 ? 155 PHE A CB 1 ATOM 979 C CG . PHE A 1 120 ? 55.555 18.661 17.507 1.00 28.76 ? 155 PHE A CG 1 ATOM 980 C CD1 . PHE A 1 120 ? 55.258 18.225 16.205 1.00 30.44 ? 155 PHE A CD1 1 ATOM 981 C CD2 . PHE A 1 120 ? 55.943 20.022 17.710 1.00 25.14 ? 155 PHE A CD2 1 ATOM 982 C CE1 . PHE A 1 120 ? 55.275 19.119 15.115 1.00 30.04 ? 155 PHE A CE1 1 ATOM 983 C CE2 . PHE A 1 120 ? 55.942 20.926 16.624 1.00 22.48 ? 155 PHE A CE2 1 ATOM 984 C CZ . PHE A 1 120 ? 55.632 20.476 15.328 1.00 28.36 ? 155 PHE A CZ 1 ATOM 985 N N . TRP A 1 121 ? 53.195 15.971 17.736 1.00 29.17 ? 156 TRP A N 1 ATOM 986 C CA . TRP A 1 121 ? 52.236 15.602 16.702 1.00 29.27 ? 156 TRP A CA 1 ATOM 987 C C . TRP A 1 121 ? 50.863 15.473 17.214 1.00 32.15 ? 156 TRP A C 1 ATOM 988 O O . TRP A 1 121 ? 49.892 15.739 16.492 1.00 30.11 ? 156 TRP A O 1 ATOM 989 C CB . TRP A 1 121 ? 52.702 14.371 15.940 1.00 30.39 ? 156 TRP A CB 1 ATOM 990 C CG . TRP A 1 121 ? 53.819 14.702 14.971 1.00 28.46 ? 156 TRP A CG 1 ATOM 991 C CD1 . TRP A 1 121 ? 55.171 14.436 15.084 1.00 28.95 ? 156 TRP A CD1 1 ATOM 992 C CD2 . TRP A 1 121 ? 53.670 15.416 13.709 1.00 26.28 ? 156 TRP A CD2 1 ATOM 993 N NE1 . TRP A 1 121 ? 55.852 14.936 13.998 1.00 31.05 ? 156 TRP A NE1 1 ATOM 994 C CE2 . TRP A 1 121 ? 55.012 15.562 13.162 1.00 28.94 ? 156 TRP A CE2 1 ATOM 995 C CE3 . TRP A 1 121 ? 52.581 15.983 13.028 1.00 32.80 ? 156 TRP A CE3 1 ATOM 996 C CZ2 . TRP A 1 121 ? 55.250 16.207 11.954 1.00 31.99 ? 156 TRP A CZ2 1 ATOM 997 C CZ3 . TRP A 1 121 ? 52.823 16.609 11.797 1.00 27.54 ? 156 TRP A CZ3 1 ATOM 998 C CH2 . TRP A 1 121 ? 54.125 16.740 11.293 1.00 27.19 ? 156 TRP A CH2 1 ATOM 999 N N . ARG A 1 122 ? 50.726 15.140 18.488 1.00 30.56 ? 157 ARG A N 1 ATOM 1000 C CA . ARG A 1 122 ? 49.374 15.119 19.036 1.00 32.34 ? 157 ARG A CA 1 ATOM 1001 C C . ARG A 1 122 ? 48.729 16.499 18.999 1.00 30.24 ? 157 ARG A C 1 ATOM 1002 O O . ARG A 1 122 ? 47.511 16.614 18.902 1.00 28.58 ? 157 ARG A O 1 ATOM 1003 C CB . ARG A 1 122 ? 49.406 14.657 20.516 1.00 33.31 ? 157 ARG A CB 1 ATOM 1004 C CG . ARG A 1 122 ? 48.016 14.475 21.120 1.00 36.21 ? 157 ARG A CG 1 ATOM 1005 C CD . ARG A 1 122 ? 48.131 13.844 22.525 1.00 44.26 ? 157 ARG A CD 1 ATOM 1006 N NE . ARG A 1 122 ? 48.827 14.671 23.552 1.00 40.68 ? 157 ARG A NE 1 ATOM 1007 C CZ . ARG A 1 122 ? 50.013 14.383 24.088 1.00 37.48 ? 157 ARG A CZ 1 ATOM 1008 N NH1 . ARG A 1 122 ? 50.698 13.311 23.664 1.00 41.62 ? 157 ARG A NH1 1 ATOM 1009 N NH2 . ARG A 1 122 ? 50.516 15.140 25.067 1.00 35.92 ? 157 ARG A NH2 1 ATOM 1010 N N . HIS A 1 123 ? 49.526 17.556 19.238 1.00 28.45 ? 158 HIS A N 1 ATOM 1011 C CA . HIS A 1 123 ? 48.999 18.911 19.142 1.00 28.99 ? 158 HIS A CA 1 ATOM 1012 C C . HIS A 1 123 ? 48.812 19.370 17.703 1.00 28.06 ? 158 HIS A C 1 ATOM 1013 O O . HIS A 1 123 ? 47.887 20.126 17.406 1.00 28.12 ? 158 HIS A O 1 ATOM 1014 C CB . HIS A 1 123 ? 49.924 19.902 19.874 1.00 31.86 ? 158 HIS A CB 1 ATOM 1015 C CG . HIS A 1 123 ? 49.774 19.830 21.364 1.00 30.20 ? 158 HIS A CG 1 ATOM 1016 N ND1 . HIS A 1 123 ? 50.322 18.824 22.086 1.00 34.05 ? 158 HIS A ND1 1 ATOM 1017 C CD2 . HIS A 1 123 ? 49.063 20.612 22.236 1.00 32.86 ? 158 HIS A CD2 1 ATOM 1018 C CE1 . HIS A 1 123 ? 50.006 19.001 23.382 1.00 32.07 ? 158 HIS A CE1 1 ATOM 1019 N NE2 . HIS A 1 123 ? 49.211 20.082 23.474 1.00 39.99 ? 158 HIS A NE2 1 ATOM 1020 N N . ALA A 1 124 ? 49.709 18.965 16.802 1.00 28.58 ? 159 ALA A N 1 ATOM 1021 C CA . ALA A 1 124 ? 49.342 19.127 15.342 1.00 30.69 ? 159 ALA A CA 1 ATOM 1022 C C . ALA A 1 124 ? 47.974 18.549 15.016 1.00 34.23 ? 159 ALA A C 1 ATOM 1023 O O . ALA A 1 124 ? 47.124 19.161 14.326 1.00 29.08 ? 159 ALA A O 1 ATOM 1024 C CB . ALA A 1 124 ? 50.388 18.495 14.447 1.00 27.46 ? 159 ALA A CB 1 ATOM 1025 N N . ASP A 1 125 ? 47.715 17.380 15.606 1.00 32.23 ? 160 ASP A N 1 ATOM 1026 C CA . ASP A 1 125 ? 46.383 16.722 15.472 1.00 31.18 ? 160 ASP A CA 1 ATOM 1027 C C . ASP A 1 125 ? 45.234 17.581 16.002 1.00 32.77 ? 160 ASP A C 1 ATOM 1028 O O . ASP A 1 125 ? 44.166 17.710 15.376 1.00 31.86 ? 160 ASP A O 1 ATOM 1029 C CB . ASP A 1 125 ? 46.486 15.372 16.213 1.00 36.24 ? 160 ASP A CB 1 ATOM 1030 C CG . ASP A 1 125 ? 45.397 14.358 15.788 1.00 49.49 ? 160 ASP A CG 1 ATOM 1031 O OD1 . ASP A 1 125 ? 44.572 14.668 14.916 1.00 46.11 ? 160 ASP A OD1 1 ATOM 1032 O OD2 . ASP A 1 125 ? 45.393 13.242 16.350 1.00 54.99 ? 160 ASP A OD2 1 ATOM 1033 N N . TYR A 1 126 ? 45.407 18.205 17.175 1.00 30.62 ? 161 TYR A N 1 ATOM 1034 C CA . TYR A 1 126 ? 44.390 19.133 17.614 1.00 28.28 ? 161 TYR A CA 1 ATOM 1035 C C . TYR A 1 126 ? 44.071 20.277 16.632 1.00 29.15 ? 161 TYR A C 1 ATOM 1036 O O . TYR A 1 126 ? 42.908 20.716 16.536 1.00 32.22 ? 161 TYR A O 1 ATOM 1037 C CB . TYR A 1 126 ? 44.767 19.795 18.939 1.00 33.83 ? 161 TYR A CB 1 ATOM 1038 C CG . TYR A 1 126 ? 44.983 18.841 20.097 1.00 38.34 ? 161 TYR A CG 1 ATOM 1039 C CD1 . TYR A 1 126 ? 44.312 17.624 20.169 1.00 36.91 ? 161 TYR A CD1 1 ATOM 1040 C CD2 . TYR A 1 126 ? 45.858 19.178 21.136 1.00 39.48 ? 161 TYR A CD2 1 ATOM 1041 C CE1 . TYR A 1 126 ? 44.531 16.736 21.220 1.00 42.59 ? 161 TYR A CE1 1 ATOM 1042 C CE2 . TYR A 1 126 ? 46.050 18.328 22.201 1.00 40.13 ? 161 TYR A CE2 1 ATOM 1043 C CZ . TYR A 1 126 ? 45.393 17.091 22.242 1.00 42.49 ? 161 TYR A CZ 1 ATOM 1044 O OH . TYR A 1 126 ? 45.604 16.240 23.311 1.00 39.22 ? 161 TYR A OH 1 ATOM 1045 N N . VAL A 1 127 ? 45.130 20.856 16.038 1.00 30.77 ? 162 VAL A N 1 ATOM 1046 C CA . VAL A 1 127 ? 44.938 21.963 15.087 1.00 28.99 ? 162 VAL A CA 1 ATOM 1047 C C . VAL A 1 127 ? 44.191 21.438 13.830 1.00 29.30 ? 162 VAL A C 1 ATOM 1048 O O . VAL A 1 127 ? 43.205 22.071 13.370 1.00 27.72 ? 162 VAL A O 1 ATOM 1049 C CB . VAL A 1 127 ? 46.284 22.663 14.725 1.00 31.77 ? 162 VAL A CB 1 ATOM 1050 C CG1 . VAL A 1 127 ? 46.018 23.664 13.646 1.00 27.58 ? 162 VAL A CG1 1 ATOM 1051 C CG2 . VAL A 1 127 ? 46.808 23.489 15.942 1.00 25.35 ? 162 VAL A CG2 1 ATOM 1052 N N . MET A 1 128 ? 44.601 20.283 13.354 1.00 29.79 ? 163 MET A N 1 ATOM 1053 C CA . MET A 1 128 ? 43.958 19.641 12.174 1.00 30.17 ? 163 MET A CA 1 ATOM 1054 C C . MET A 1 128 ? 42.481 19.188 12.453 1.00 33.30 ? 163 MET A C 1 ATOM 1055 O O . MET A 1 128 ? 41.666 19.223 11.586 1.00 35.89 ? 163 MET A O 1 ATOM 1056 C CB . MET A 1 128 ? 44.803 18.499 11.651 1.00 30.44 ? 163 MET A CB 1 ATOM 1057 C CG . MET A 1 128 ? 46.158 18.970 11.095 1.00 38.85 ? 163 MET A CG 1 ATOM 1058 S SD . MET A 1 128 ? 45.890 20.285 9.813 1.00 50.22 ? 163 MET A SD 1 ATOM 1059 C CE . MET A 1 128 ? 44.833 19.166 8.771 1.00 30.83 ? 163 MET A CE 1 ATOM 1060 N N . ALA A 1 129 ? 42.167 18.746 13.671 1.00 31.09 ? 164 ALA A N 1 ATOM 1061 C CA . ALA A 1 129 ? 40.742 18.529 14.049 1.00 28.94 ? 164 ALA A CA 1 ATOM 1062 C C . ALA A 1 129 ? 39.969 19.803 13.955 1.00 30.39 ? 164 ALA A C 1 ATOM 1063 O O . ALA A 1 129 ? 38.791 19.797 13.566 1.00 33.63 ? 164 ALA A O 1 ATOM 1064 C CB . ALA A 1 129 ? 40.665 18.023 15.503 1.00 29.79 ? 164 ALA A CB 1 ATOM 1065 N N . GLN A 1 130 ? 40.573 20.938 14.386 1.00 26.70 ? 165 GLN A N 1 ATOM 1066 C CA . GLN A 1 130 ? 39.829 22.165 14.374 1.00 26.95 ? 165 GLN A CA 1 ATOM 1067 C C . GLN A 1 130 ? 39.557 22.529 12.906 1.00 29.58 ? 165 GLN A C 1 ATOM 1068 O O . GLN A 1 130 ? 38.477 23.113 12.566 1.00 30.10 ? 165 GLN A O 1 ATOM 1069 C CB . GLN A 1 130 ? 40.565 23.286 15.114 1.00 27.23 ? 165 GLN A CB 1 ATOM 1070 C CG . GLN A 1 130 ? 39.732 24.534 15.285 1.00 28.58 ? 165 GLN A CG 1 ATOM 1071 C CD . GLN A 1 130 ? 40.604 25.690 15.826 1.00 30.69 ? 165 GLN A CD 1 ATOM 1072 O OE1 . GLN A 1 130 ? 41.842 25.591 15.866 1.00 30.67 ? 165 GLN A OE1 1 ATOM 1073 N NE2 . GLN A 1 130 ? 39.979 26.751 16.229 1.00 28.17 ? 165 GLN A NE2 1 ATOM 1074 N N . MET A 1 131 ? 40.537 22.247 12.066 1.00 27.93 ? 166 MET A N 1 ATOM 1075 C CA . MET A 1 131 ? 40.434 22.592 10.622 1.00 31.32 ? 166 MET A CA 1 ATOM 1076 C C . MET A 1 131 ? 39.337 21.700 9.964 1.00 29.70 ? 166 MET A C 1 ATOM 1077 O O . MET A 1 131 ? 38.522 22.208 9.183 1.00 32.31 ? 166 MET A O 1 ATOM 1078 C CB . MET A 1 131 ? 41.766 22.424 9.902 1.00 26.24 ? 166 MET A CB 1 ATOM 1079 C CG . MET A 1 131 ? 41.777 23.032 8.461 1.00 32.81 ? 166 MET A CG 1 ATOM 1080 S SD . MET A 1 131 ? 43.389 22.779 7.698 1.00 33.18 ? 166 MET A SD 1 ATOM 1081 C CE . MET A 1 131 ? 43.280 24.176 6.559 1.00 27.82 ? 166 MET A CE 1 ATOM 1082 N N . ASP A 1 132 ? 39.325 20.394 10.288 1.00 34.87 ? 167 ASP A N 1 ATOM 1083 C CA . ASP A 1 132 ? 38.216 19.499 9.806 1.00 31.15 ? 167 ASP A CA 1 ATOM 1084 C C . ASP A 1 132 ? 36.874 19.976 10.236 1.00 34.71 ? 167 ASP A C 1 ATOM 1085 O O . ASP A 1 132 ? 35.901 20.005 9.455 1.00 33.57 ? 167 ASP A O 1 ATOM 1086 C CB . ASP A 1 132 ? 38.501 18.080 10.189 1.00 33.36 ? 167 ASP A CB 1 ATOM 1087 C CG . ASP A 1 132 ? 39.666 17.553 9.413 1.00 34.39 ? 167 ASP A CG 1 ATOM 1088 O OD1 . ASP A 1 132 ? 39.967 18.168 8.386 1.00 37.00 ? 167 ASP A OD1 1 ATOM 1089 O OD2 . ASP A 1 132 ? 40.308 16.545 9.765 1.00 39.14 ? 167 ASP A OD2 1 ATOM 1090 N N . GLY A 1 133 ? 36.800 20.402 11.488 1.00 30.44 ? 168 GLY A N 1 ATOM 1091 C CA . GLY A 1 133 ? 35.604 20.994 11.994 1.00 32.45 ? 168 GLY A CA 1 ATOM 1092 C C . GLY A 1 133 ? 35.194 22.236 11.289 1.00 35.06 ? 168 GLY A C 1 ATOM 1093 O O . GLY A 1 133 ? 33.983 22.437 10.984 1.00 31.63 ? 168 GLY A O 1 ATOM 1094 N N . LEU A 1 134 ? 36.165 23.119 11.042 1.00 32.72 ? 169 LEU A N 1 ATOM 1095 C CA . LEU A 1 134 ? 35.858 24.361 10.326 1.00 27.59 ? 169 LEU A CA 1 ATOM 1096 C C . LEU A 1 134 ? 35.277 23.983 8.916 1.00 30.97 ? 169 LEU A C 1 ATOM 1097 O O . LEU A 1 134 ? 34.296 24.566 8.436 1.00 30.54 ? 169 LEU A O 1 ATOM 1098 C CB . LEU A 1 134 ? 37.119 25.192 10.135 1.00 30.26 ? 169 LEU A CB 1 ATOM 1099 C CG . LEU A 1 134 ? 36.938 26.519 9.373 1.00 29.77 ? 169 LEU A CG 1 ATOM 1100 C CD1 . LEU A 1 134 ? 36.274 27.626 10.151 1.00 30.60 ? 169 LEU A CD1 1 ATOM 1101 C CD2 . LEU A 1 134 ? 38.300 26.986 8.850 1.00 30.50 ? 169 LEU A CD2 1 ATOM 1102 N N . PHE A 1 135 ? 35.880 23.002 8.274 1.00 27.91 ? 170 PHE A N 1 ATOM 1103 C CA . PHE A 1 135 ? 35.420 22.561 6.948 1.00 33.68 ? 170 PHE A CA 1 ATOM 1104 C C . PHE A 1 135 ? 33.952 21.991 7.054 1.00 39.34 ? 170 PHE A C 1 ATOM 1105 O O . PHE A 1 135 ? 33.041 22.436 6.293 1.00 33.88 ? 170 PHE A O 1 ATOM 1106 C CB . PHE A 1 135 ? 36.399 21.533 6.358 1.00 31.79 ? 170 PHE A CB 1 ATOM 1107 C CG . PHE A 1 135 ? 35.935 20.934 5.026 1.00 38.96 ? 170 PHE A CG 1 ATOM 1108 C CD1 . PHE A 1 135 ? 35.436 21.754 4.007 1.00 37.14 ? 170 PHE A CD1 1 ATOM 1109 C CD2 . PHE A 1 135 ? 35.999 19.556 4.812 1.00 40.58 ? 170 PHE A CD2 1 ATOM 1110 C CE1 . PHE A 1 135 ? 34.995 21.210 2.790 1.00 43.77 ? 170 PHE A CE1 1 ATOM 1111 C CE2 . PHE A 1 135 ? 35.570 19.010 3.609 1.00 46.60 ? 170 PHE A CE2 1 ATOM 1112 C CZ . PHE A 1 135 ? 35.066 19.838 2.594 1.00 42.57 ? 170 PHE A CZ 1 ATOM 1113 N N . ALA A 1 136 ? 33.759 21.087 8.035 1.00 37.90 ? 171 ALA A N 1 ATOM 1114 C CA . ALA A 1 136 ? 32.434 20.466 8.377 1.00 37.45 ? 171 ALA A CA 1 ATOM 1115 C C . ALA A 1 136 ? 31.340 21.485 8.685 1.00 39.07 ? 171 ALA A C 1 ATOM 1116 O O . ALA A 1 136 ? 30.242 21.416 8.130 1.00 38.96 ? 171 ALA A O 1 ATOM 1117 C CB . ALA A 1 136 ? 32.567 19.474 9.515 1.00 35.57 ? 171 ALA A CB 1 ATOM 1118 N N . GLY A 1 137 ? 31.648 22.445 9.552 1.00 38.15 ? 172 GLY A N 1 ATOM 1119 C CA . GLY A 1 137 ? 30.803 23.594 9.859 1.00 32.47 ? 172 GLY A CA 1 ATOM 1120 C C . GLY A 1 137 ? 30.412 24.507 8.719 1.00 38.17 ? 172 GLY A C 1 ATOM 1121 O O . GLY A 1 137 ? 29.219 24.895 8.598 1.00 34.73 ? 172 GLY A O 1 ATOM 1122 N N . ALA A 1 138 ? 31.390 24.946 7.920 1.00 35.02 ? 173 ALA A N 1 ATOM 1123 C CA . ALA A 1 138 ? 31.091 25.855 6.792 1.00 37.03 ? 173 ALA A CA 1 ATOM 1124 C C . ALA A 1 138 ? 30.160 25.177 5.715 1.00 34.73 ? 173 ALA A C 1 ATOM 1125 O O . ALA A 1 138 ? 29.279 25.855 5.158 1.00 38.05 ? 173 ALA A O 1 ATOM 1126 C CB . ALA A 1 138 ? 32.361 26.264 6.121 1.00 34.30 ? 173 ALA A CB 1 ATOM 1127 N N . THR A 1 139 ? 30.403 23.900 5.466 1.00 37.29 ? 174 THR A N 1 ATOM 1128 C CA . THR A 1 139 ? 29.589 23.043 4.593 1.00 45.93 ? 174 THR A CA 1 ATOM 1129 C C . THR A 1 139 ? 28.165 22.965 5.098 1.00 51.47 ? 174 THR A C 1 ATOM 1130 O O . THR A 1 139 ? 27.233 23.250 4.330 1.00 53.66 ? 174 THR A O 1 ATOM 1131 C CB . THR A 1 139 ? 30.138 21.623 4.588 1.00 40.13 ? 174 THR A CB 1 ATOM 1132 O OG1 . THR A 1 139 ? 31.451 21.672 4.065 1.00 37.26 ? 174 THR A OG1 1 ATOM 1133 C CG2 . THR A 1 139 ? 29.300 20.643 3.653 1.00 43.00 ? 174 THR A CG2 1 ATOM 1134 N N . LYS A 1 140 ? 28.006 22.613 6.388 1.00 48.75 ? 175 LYS A N 1 ATOM 1135 C CA . LYS A 1 140 ? 26.687 22.489 7.021 1.00 45.26 ? 175 LYS A CA 1 ATOM 1136 C C . LYS A 1 140 ? 25.897 23.742 6.767 1.00 47.79 ? 175 LYS A C 1 ATOM 1137 O O . LYS A 1 140 ? 24.708 23.678 6.388 1.00 45.73 ? 175 LYS A O 1 ATOM 1138 C CB . LYS A 1 140 ? 26.764 22.238 8.541 1.00 49.61 ? 175 LYS A CB 1 ATOM 1139 C CG . LYS A 1 140 ? 25.422 22.259 9.298 1.00 53.21 ? 175 LYS A CG 1 ATOM 1140 C CD . LYS A 1 140 ? 24.474 21.153 8.820 1.00 51.90 ? 175 LYS A CD 1 ATOM 1141 C CE . LYS A 1 140 ? 23.328 20.911 9.779 1.00 59.41 ? 175 LYS A CE 1 ATOM 1142 N NZ . LYS A 1 140 ? 22.103 20.443 9.048 1.00 65.16 ? 175 LYS A NZ 1 ATOM 1143 N N . ARG A 1 141 ? 26.554 24.887 6.940 1.00 41.76 ? 176 ARG A N 1 ATOM 1144 C CA . ARG A 1 141 ? 25.899 26.210 6.858 1.00 40.45 ? 176 ARG A CA 1 ATOM 1145 C C . ARG A 1 141 ? 25.472 26.482 5.418 1.00 44.44 ? 176 ARG A C 1 ATOM 1146 O O . ARG A 1 141 ? 24.370 27.003 5.197 1.00 47.54 ? 176 ARG A O 1 ATOM 1147 C CB . ARG A 1 141 ? 26.861 27.336 7.320 1.00 38.98 ? 176 ARG A CB 1 ATOM 1148 C CG . ARG A 1 141 ? 26.405 28.773 7.107 1.00 43.16 ? 176 ARG A CG 1 ATOM 1149 C CD . ARG A 1 141 ? 25.219 29.118 7.975 1.00 37.01 ? 176 ARG A CD 1 ATOM 1150 N NE . ARG A 1 141 ? 24.691 30.435 7.661 1.00 39.05 ? 176 ARG A NE 1 ATOM 1151 C CZ . ARG A 1 141 ? 25.086 31.576 8.242 1.00 45.82 ? 176 ARG A CZ 1 ATOM 1152 N NH1 . ARG A 1 141 ? 26.031 31.590 9.191 1.00 49.82 ? 176 ARG A NH1 1 ATOM 1153 N NH2 . ARG A 1 141 ? 24.537 32.723 7.894 1.00 44.92 ? 176 ARG A NH2 1 ATOM 1154 N N . ALA A 1 142 ? 26.357 26.121 4.473 1.00 42.41 ? 177 ALA A N 1 ATOM 1155 C CA . ALA A 1 142 ? 26.146 26.241 3.023 1.00 45.55 ? 177 ALA A CA 1 ATOM 1156 C C . ALA A 1 142 ? 24.960 25.388 2.554 1.00 47.00 ? 177 ALA A C 1 ATOM 1157 O O . ALA A 1 142 ? 24.036 25.910 1.953 1.00 49.86 ? 177 ALA A O 1 ATOM 1158 C CB . ALA A 1 142 ? 27.411 25.843 2.266 1.00 41.46 ? 177 ALA A CB 1 ATOM 1159 N N . VAL A 1 143 ? 24.998 24.093 2.829 1.00 49.46 ? 178 VAL A N 1 ATOM 1160 C CA . VAL A 1 143 ? 23.877 23.207 2.511 1.00 50.00 ? 178 VAL A CA 1 ATOM 1161 C C . VAL A 1 143 ? 22.541 23.755 3.051 1.00 58.10 ? 178 VAL A C 1 ATOM 1162 O O . VAL A 1 143 ? 21.580 23.913 2.307 1.00 57.77 ? 178 VAL A O 1 ATOM 1163 C CB . VAL A 1 143 ? 24.172 21.788 3.011 1.00 51.86 ? 178 VAL A CB 1 ATOM 1164 C CG1 . VAL A 1 143 ? 22.979 20.843 2.796 1.00 54.37 ? 178 VAL A CG1 1 ATOM 1165 C CG2 . VAL A 1 143 ? 25.421 21.272 2.330 1.00 43.63 ? 178 VAL A CG2 1 ATOM 1166 N N . LEU A 1 144 ? 22.515 24.091 4.332 1.00 52.93 ? 179 LEU A N 1 ATOM 1167 C CA . LEU A 1 144 ? 21.351 24.612 4.984 1.00 59.00 ? 179 LEU A CA 1 ATOM 1168 C C . LEU A 1 144 ? 20.827 25.913 4.338 1.00 59.74 ? 179 LEU A C 1 ATOM 1169 O O . LEU A 1 144 ? 19.637 26.204 4.425 1.00 59.10 ? 179 LEU A O 1 ATOM 1170 C CB . LEU A 1 144 ? 21.656 24.793 6.480 1.00 62.18 ? 179 LEU A CB 1 ATOM 1171 C CG . LEU A 1 144 ? 20.552 24.629 7.526 1.00 71.80 ? 179 LEU A CG 1 ATOM 1172 C CD1 . LEU A 1 144 ? 20.940 23.589 8.583 1.00 74.72 ? 179 LEU A CD1 1 ATOM 1173 C CD2 . LEU A 1 144 ? 20.221 26.001 8.118 1.00 73.84 ? 179 LEU A CD2 1 ATOM 1174 N N . GLU A 1 145 ? 21.712 26.700 3.715 1.00 57.61 ? 180 GLU A N 1 ATOM 1175 C CA . GLU A 1 145 ? 21.343 27.962 3.064 1.00 49.67 ? 180 GLU A CA 1 ATOM 1176 C C . GLU A 1 145 ? 21.122 27.728 1.551 1.00 53.86 ? 180 GLU A C 1 ATOM 1177 O O . GLU A 1 145 ? 20.738 28.646 0.818 1.00 49.19 ? 180 GLU A O 1 ATOM 1178 C CB . GLU A 1 145 ? 22.431 29.036 3.240 1.00 59.70 ? 180 GLU A CB 1 ATOM 1179 C CG . GLU A 1 145 ? 22.762 29.441 4.689 1.00 59.95 ? 180 GLU A CG 1 ATOM 1180 C CD . GLU A 1 145 ? 21.984 30.658 5.127 1.00 62.22 ? 180 GLU A CD 1 ATOM 1181 O OE1 . GLU A 1 145 ? 20.992 31.009 4.451 1.00 67.71 ? 180 GLU A OE1 1 ATOM 1182 O OE2 . GLU A 1 145 ? 22.347 31.271 6.145 1.00 56.51 ? 180 GLU A OE2 1 ATOM 1183 N N . GLY A 1 146 ? 21.400 26.503 1.096 1.00 48.54 ? 181 GLY A N 1 ATOM 1184 C CA . GLY A 1 146 ? 21.336 26.136 -0.319 1.00 55.39 ? 181 GLY A CA 1 ATOM 1185 C C . GLY A 1 146 ? 22.417 26.734 -1.209 1.00 62.10 ? 181 GLY A C 1 ATOM 1186 O O . GLY A 1 146 ? 22.156 27.025 -2.370 1.00 67.35 ? 181 GLY A O 1 ATOM 1187 N N . LYS A 1 147 ? 23.633 26.922 -0.697 1.00 60.93 ? 182 LYS A N 1 ATOM 1188 C CA . LYS A 1 147 ? 24.752 27.384 -1.543 1.00 55.22 ? 182 LYS A CA 1 ATOM 1189 C C . LYS A 1 147 ? 25.700 26.235 -1.829 1.00 45.85 ? 182 LYS A C 1 ATOM 1190 O O . LYS A 1 147 ? 25.703 25.248 -1.112 1.00 56.36 ? 182 LYS A O 1 ATOM 1191 C CB . LYS A 1 147 ? 25.495 28.569 -0.907 1.00 59.90 ? 182 LYS A CB 1 ATOM 1192 C CG . LYS A 1 147 ? 24.613 29.704 -0.399 1.00 61.49 ? 182 LYS A CG 1 ATOM 1193 C CD . LYS A 1 147 ? 24.037 30.538 -1.534 1.00 72.99 ? 182 LYS A CD 1 ATOM 1194 C CE . LYS A 1 147 ? 22.706 31.161 -1.110 1.00 74.89 ? 182 LYS A CE 1 ATOM 1195 N NZ . LYS A 1 147 ? 22.215 32.161 -2.104 1.00 73.13 ? 182 LYS A NZ 1 ATOM 1196 N N . LYS A 1 148 ? 26.484 26.328 -2.896 1.00 50.31 ? 183 LYS A N 1 ATOM 1197 C CA . LYS A 1 148 ? 27.598 25.375 -3.124 1.00 56.92 ? 183 LYS A CA 1 ATOM 1198 C C . LYS A 1 148 ? 28.596 25.543 -1.935 1.00 51.92 ? 183 LYS A C 1 ATOM 1199 O O . LYS A 1 148 ? 29.052 26.649 -1.717 1.00 46.85 ? 183 LYS A O 1 ATOM 1200 C CB . LYS A 1 148 ? 28.290 25.636 -4.494 1.00 57.19 ? 183 LYS A CB 1 ATOM 1201 C CG . LYS A 1 148 ? 29.518 24.770 -4.845 1.00 65.08 ? 183 LYS A CG 1 ATOM 1202 C CD . LYS A 1 148 ? 29.223 23.310 -5.200 1.00 84.15 ? 183 LYS A CD 1 ATOM 1203 C CE . LYS A 1 148 ? 28.467 23.154 -6.524 1.00 90.61 ? 183 LYS A CE 1 ATOM 1204 N NZ . LYS A 1 148 ? 29.170 23.846 -7.652 1.00 97.71 ? 183 LYS A NZ 1 ATOM 1205 N N . PRO A 1 149 ? 28.862 24.474 -1.139 1.00 53.73 ? 184 PRO A N 1 ATOM 1206 C CA . PRO A 1 149 ? 29.829 24.632 -0.015 1.00 47.26 ? 184 PRO A CA 1 ATOM 1207 C C . PRO A 1 149 ? 31.229 24.975 -0.538 1.00 46.36 ? 184 PRO A C 1 ATOM 1208 O O . PRO A 1 149 ? 31.607 24.498 -1.622 1.00 41.05 ? 184 PRO A O 1 ATOM 1209 C CB . PRO A 1 149 ? 29.855 23.239 0.601 1.00 44.07 ? 184 PRO A CB 1 ATOM 1210 C CG . PRO A 1 149 ? 28.505 22.648 0.272 1.00 54.72 ? 184 PRO A CG 1 ATOM 1211 C CD . PRO A 1 149 ? 28.256 23.127 -1.145 1.00 56.19 ? 184 PRO A CD 1 ATOM 1212 N N . MET A 1 150 ? 32.005 25.758 0.223 1.00 44.33 ? 185 MET A N 1 ATOM 1213 C CA . MET A 1 150 ? 33.464 25.918 -0.045 1.00 36.54 ? 185 MET A CA 1 ATOM 1214 C C . MET A 1 150 ? 34.230 24.590 -0.066 1.00 34.46 ? 185 MET A C 1 ATOM 1215 O O . MET A 1 150 ? 33.825 23.652 0.600 1.00 39.18 ? 185 MET A O 1 ATOM 1216 C CB . MET A 1 150 ? 34.050 26.859 1.015 1.00 36.48 ? 185 MET A CB 1 ATOM 1217 C CG . MET A 1 150 ? 33.380 28.226 0.967 1.00 39.35 ? 185 MET A CG 1 ATOM 1218 S SD . MET A 1 150 ? 34.167 29.330 2.173 1.00 44.04 ? 185 MET A SD 1 ATOM 1219 C CE . MET A 1 150 ? 35.806 29.368 1.424 1.00 38.97 ? 185 MET A CE 1 ATOM 1220 N N . THR A 1 151 ? 35.299 24.463 -0.856 1.00 33.66 ? 186 THR A N 1 ATOM 1221 C CA . THR A 1 151 ? 36.007 23.196 -0.882 1.00 34.47 ? 186 THR A CA 1 ATOM 1222 C C . THR A 1 151 ? 37.090 23.230 0.208 1.00 37.47 ? 186 THR A C 1 ATOM 1223 O O . THR A 1 151 ? 37.362 24.345 0.783 1.00 36.51 ? 186 THR A O 1 ATOM 1224 C CB . THR A 1 151 ? 36.734 22.956 -2.204 1.00 38.97 ? 186 THR A CB 1 ATOM 1225 O OG1 . THR A 1 151 ? 37.686 24.015 -2.404 1.00 36.50 ? 186 THR A OG1 1 ATOM 1226 C CG2 . THR A 1 151 ? 35.742 22.833 -3.413 1.00 34.24 ? 186 THR A CG2 1 ATOM 1227 N N . LEU A 1 152 ? 37.710 22.060 0.473 1.00 34.20 ? 187 LEU A N 1 ATOM 1228 C CA . LEU A 1 152 ? 38.715 21.952 1.540 1.00 36.54 ? 187 LEU A CA 1 ATOM 1229 C C . LEU A 1 152 ? 39.915 22.762 1.020 1.00 34.31 ? 187 LEU A C 1 ATOM 1230 O O . LEU A 1 152 ? 40.615 23.443 1.786 1.00 31.45 ? 187 LEU A O 1 ATOM 1231 C CB . LEU A 1 152 ? 39.159 20.495 1.828 1.00 36.48 ? 187 LEU A CB 1 ATOM 1232 C CG . LEU A 1 152 ? 40.216 20.404 2.986 1.00 33.03 ? 187 LEU A CG 1 ATOM 1233 C CD1 . LEU A 1 152 ? 39.751 21.122 4.258 1.00 32.90 ? 187 LEU A CD1 1 ATOM 1234 C CD2 . LEU A 1 152 ? 40.557 18.958 3.303 1.00 39.71 ? 187 LEU A CD2 1 ATOM 1235 N N . PHE A 1 153 ? 40.115 22.715 -0.304 1.00 31.13 ? 188 PHE A N 1 ATOM 1236 C CA . PHE A 1 153 ? 41.211 23.501 -0.900 1.00 32.63 ? 188 PHE A CA 1 ATOM 1237 C C . PHE A 1 153 ? 41.062 24.990 -0.611 1.00 31.48 ? 188 PHE A C 1 ATOM 1238 O O . PHE A 1 153 ? 42.042 25.678 -0.276 1.00 30.53 ? 188 PHE A O 1 ATOM 1239 C CB . PHE A 1 153 ? 41.340 23.299 -2.424 1.00 36.59 ? 188 PHE A CB 1 ATOM 1240 C CG . PHE A 1 153 ? 42.313 24.225 -3.020 1.00 37.68 ? 188 PHE A CG 1 ATOM 1241 C CD1 . PHE A 1 153 ? 43.675 24.009 -2.839 1.00 37.30 ? 188 PHE A CD1 1 ATOM 1242 C CD2 . PHE A 1 153 ? 41.882 25.415 -3.610 1.00 41.24 ? 188 PHE A CD2 1 ATOM 1243 C CE1 . PHE A 1 153 ? 44.580 24.902 -3.338 1.00 40.24 ? 188 PHE A CE1 1 ATOM 1244 C CE2 . PHE A 1 153 ? 42.809 26.318 -4.110 1.00 37.60 ? 188 PHE A CE2 1 ATOM 1245 C CZ . PHE A 1 153 ? 44.148 26.043 -3.971 1.00 35.31 ? 188 PHE A CZ 1 ATOM 1246 N N . GLN A 1 154 ? 39.853 25.489 -0.743 1.00 29.22 ? 189 GLN A N 1 ATOM 1247 C CA . GLN A 1 154 ? 39.626 26.892 -0.458 1.00 30.76 ? 189 GLN A CA 1 ATOM 1248 C C . GLN A 1 154 ? 39.971 27.276 1.016 1.00 34.45 ? 189 GLN A C 1 ATOM 1249 O O . GLN A 1 154 ? 40.449 28.405 1.274 1.00 29.00 ? 189 GLN A O 1 ATOM 1250 C CB . GLN A 1 154 ? 38.192 27.275 -0.724 1.00 30.49 ? 189 GLN A CB 1 ATOM 1251 C CG . GLN A 1 154 ? 37.829 27.462 -2.237 1.00 34.71 ? 189 GLN A CG 1 ATOM 1252 C CD . GLN A 1 154 ? 36.322 27.713 -2.408 1.00 36.70 ? 189 GLN A CD 1 ATOM 1253 O OE1 . GLN A 1 154 ? 35.531 26.807 -2.288 1.00 38.07 ? 189 GLN A OE1 1 ATOM 1254 N NE2 . GLN A 1 154 ? 35.935 28.966 -2.608 1.00 40.21 ? 189 GLN A NE2 1 ATOM 1255 N N . ILE A 1 155 ? 39.685 26.344 1.934 1.00 32.87 ? 190 ILE A N 1 ATOM 1256 C CA . ILE A 1 155 ? 39.946 26.574 3.369 1.00 32.08 ? 190 ILE A CA 1 ATOM 1257 C C . ILE A 1 155 ? 41.480 26.471 3.608 1.00 27.62 ? 190 ILE A C 1 ATOM 1258 O O . ILE A 1 155 ? 42.005 27.226 4.419 1.00 27.64 ? 190 ILE A O 1 ATOM 1259 C CB . ILE A 1 155 ? 39.083 25.676 4.284 1.00 32.48 ? 190 ILE A CB 1 ATOM 1260 C CG1 . ILE A 1 155 ? 37.581 26.100 4.145 1.00 33.11 ? 190 ILE A CG1 1 ATOM 1261 C CG2 . ILE A 1 155 ? 39.605 25.691 5.738 1.00 33.20 ? 190 ILE A CG2 1 ATOM 1262 C CD1 . ILE A 1 155 ? 36.574 25.336 5.000 1.00 38.85 ? 190 ILE A CD1 1 ATOM 1263 N N . GLN A 1 156 ? 42.152 25.549 2.915 1.00 25.60 ? 191 GLN A N 1 ATOM 1264 C CA . GLN A 1 156 ? 43.613 25.403 3.007 1.00 28.35 ? 191 GLN A CA 1 ATOM 1265 C C . GLN A 1 156 ? 44.274 26.699 2.515 1.00 28.73 ? 191 GLN A C 1 ATOM 1266 O O . GLN A 1 156 ? 45.263 27.185 3.071 1.00 26.56 ? 191 GLN A O 1 ATOM 1267 C CB . GLN A 1 156 ? 44.086 24.213 2.165 1.00 28.32 ? 191 GLN A CB 1 ATOM 1268 C CG . GLN A 1 156 ? 43.716 22.877 2.807 1.00 33.35 ? 191 GLN A CG 1 ATOM 1269 C CD . GLN A 1 156 ? 43.875 21.696 1.874 1.00 36.11 ? 191 GLN A CD 1 ATOM 1270 O OE1 . GLN A 1 156 ? 44.138 21.873 0.711 1.00 33.10 ? 191 GLN A OE1 1 ATOM 1271 N NE2 . GLN A 1 156 ? 43.761 20.481 2.407 1.00 38.80 ? 191 GLN A NE2 1 ATOM 1272 N N . PHE A 1 157 ? 43.766 27.200 1.391 1.00 30.58 ? 192 PHE A N 1 ATOM 1273 C CA . PHE A 1 157 ? 44.262 28.417 0.779 1.00 31.76 ? 192 PHE A CA 1 ATOM 1274 C C . PHE A 1 157 ? 44.097 29.621 1.743 1.00 29.54 ? 192 PHE A C 1 ATOM 1275 O O . PHE A 1 157 ? 45.035 30.354 1.896 1.00 24.15 ? 192 PHE A O 1 ATOM 1276 C CB . PHE A 1 157 ? 43.494 28.700 -0.514 1.00 31.48 ? 192 PHE A CB 1 ATOM 1277 C CG . PHE A 1 157 ? 43.952 29.918 -1.227 1.00 31.70 ? 192 PHE A CG 1 ATOM 1278 C CD1 . PHE A 1 157 ? 43.350 31.146 -0.987 1.00 28.92 ? 192 PHE A CD1 1 ATOM 1279 C CD2 . PHE A 1 157 ? 44.891 29.809 -2.250 1.00 33.72 ? 192 PHE A CD2 1 ATOM 1280 C CE1 . PHE A 1 157 ? 43.764 32.291 -1.648 1.00 36.91 ? 192 PHE A CE1 1 ATOM 1281 C CE2 . PHE A 1 157 ? 45.311 30.939 -2.939 1.00 36.29 ? 192 PHE A CE2 1 ATOM 1282 C CZ . PHE A 1 157 ? 44.762 32.191 -2.633 1.00 31.36 ? 192 PHE A CZ 1 ATOM 1283 N N . LEU A 1 158 ? 42.918 29.816 2.357 1.00 26.94 ? 193 LEU A N 1 ATOM 1284 C CA . LEU A 1 158 ? 42.757 30.905 3.330 1.00 27.35 ? 193 LEU A CA 1 ATOM 1285 C C . LEU A 1 158 ? 43.808 30.822 4.479 1.00 28.58 ? 193 LEU A C 1 ATOM 1286 O O . LEU A 1 158 ? 44.441 31.809 4.794 1.00 27.61 ? 193 LEU A O 1 ATOM 1287 C CB . LEU A 1 158 ? 41.374 30.946 3.944 1.00 24.85 ? 193 LEU A CB 1 ATOM 1288 C CG . LEU A 1 158 ? 40.275 31.325 2.917 1.00 29.95 ? 193 LEU A CG 1 ATOM 1289 C CD1 . LEU A 1 158 ? 38.893 31.188 3.579 1.00 29.60 ? 193 LEU A CD1 1 ATOM 1290 C CD2 . LEU A 1 158 ? 40.513 32.717 2.422 1.00 26.64 ? 193 LEU A CD2 1 ATOM 1291 N N . ASN A 1 159 ? 44.019 29.625 5.008 1.00 28.64 ? 194 ASN A N 1 ATOM 1292 C CA . ASN A 1 159 ? 44.871 29.469 6.175 1.00 24.52 ? 194 ASN A CA 1 ATOM 1293 C C . ASN A 1 159 ? 46.343 29.590 5.767 1.00 25.52 ? 194 ASN A C 1 ATOM 1294 O O . ASN A 1 159 ? 47.179 29.964 6.591 1.00 27.40 ? 194 ASN A O 1 ATOM 1295 C CB . ASN A 1 159 ? 44.553 28.114 6.805 1.00 25.95 ? 194 ASN A CB 1 ATOM 1296 C CG . ASN A 1 159 ? 43.388 28.219 7.771 1.00 31.61 ? 194 ASN A CG 1 ATOM 1297 O OD1 . ASN A 1 159 ? 43.612 28.573 8.909 1.00 25.02 ? 194 ASN A OD1 1 ATOM 1298 N ND2 . ASN A 1 159 ? 42.139 28.009 7.306 1.00 28.29 ? 194 ASN A ND2 1 ATOM 1299 N N . ALA A 1 160 ? 46.623 29.341 4.471 1.00 23.35 ? 195 ALA A N 1 ATOM 1300 C CA . ALA A 1 160 ? 47.947 29.382 3.932 1.00 25.10 ? 195 ALA A CA 1 ATOM 1301 C C . ALA A 1 160 ? 48.352 30.745 3.354 1.00 24.43 ? 195 ALA A C 1 ATOM 1302 O O . ALA A 1 160 ? 49.471 30.853 2.781 1.00 23.90 ? 195 ALA A O 1 ATOM 1303 C CB . ALA A 1 160 ? 48.147 28.246 2.854 1.00 23.39 ? 195 ALA A CB 1 ATOM 1304 N N . ILE A 1 161 ? 47.496 31.790 3.432 1.00 23.30 ? 196 ILE A N 1 ATOM 1305 C CA . ILE A 1 161 ? 47.806 33.047 2.728 1.00 25.11 ? 196 ILE A CA 1 ATOM 1306 C C . ILE A 1 161 ? 49.235 33.539 3.007 1.00 26.62 ? 196 ILE A C 1 ATOM 1307 O O . ILE A 1 161 ? 49.969 33.954 2.090 1.00 22.98 ? 196 ILE A O 1 ATOM 1308 C CB . ILE A 1 161 ? 46.793 34.199 3.120 1.00 25.54 ? 196 ILE A CB 1 ATOM 1309 C CG1 . ILE A 1 161 ? 45.382 33.808 2.638 1.00 27.81 ? 196 ILE A CG1 1 ATOM 1310 C CG2 . ILE A 1 161 ? 47.205 35.607 2.639 1.00 28.24 ? 196 ILE A CG2 1 ATOM 1311 C CD1 . ILE A 1 161 ? 45.191 33.921 1.173 1.00 34.48 ? 196 ILE A CD1 1 ATOM 1312 N N . GLY A 1 162 ? 49.592 33.549 4.281 1.00 26.03 ? 197 GLY A N 1 ATOM 1313 C CA . GLY A 1 162 ? 50.983 34.001 4.645 1.00 26.33 ? 197 GLY A CA 1 ATOM 1314 C C . GLY A 1 162 ? 52.074 33.178 4.015 1.00 24.19 ? 197 GLY A C 1 ATOM 1315 O O . GLY A 1 162 ? 53.070 33.695 3.478 1.00 25.17 ? 197 GLY A O 1 ATOM 1316 N N . ASP A 1 163 ? 51.931 31.860 4.058 1.00 25.02 ? 198 ASP A N 1 ATOM 1317 C CA . ASP A 1 163 ? 52.926 30.981 3.440 1.00 25.34 ? 198 ASP A CA 1 ATOM 1318 C C . ASP A 1 163 ? 52.933 31.146 1.936 1.00 29.83 ? 198 ASP A C 1 ATOM 1319 O O . ASP A 1 163 ? 53.988 31.033 1.292 1.00 28.67 ? 198 ASP A O 1 ATOM 1320 C CB . ASP A 1 163 ? 52.489 29.533 3.753 1.00 23.24 ? 198 ASP A CB 1 ATOM 1321 C CG . ASP A 1 163 ? 52.547 29.267 5.218 1.00 23.94 ? 198 ASP A CG 1 ATOM 1322 O OD1 . ASP A 1 163 ? 53.625 28.999 5.712 1.00 23.43 ? 198 ASP A OD1 1 ATOM 1323 O OD2 . ASP A 1 163 ? 51.537 29.345 5.934 1.00 26.44 ? 198 ASP A OD2 1 ATOM 1324 N N . LEU A 1 164 ? 51.749 31.442 1.362 1.00 27.36 ? 199 LEU A N 1 ATOM 1325 C CA . LEU A 1 164 ? 51.683 31.657 -0.100 1.00 31.44 ? 199 LEU A CA 1 ATOM 1326 C C . LEU A 1 164 ? 52.366 32.941 -0.581 1.00 30.66 ? 199 LEU A C 1 ATOM 1327 O O . LEU A 1 164 ? 52.910 32.942 -1.692 1.00 35.17 ? 199 LEU A O 1 ATOM 1328 C CB . LEU A 1 164 ? 50.245 31.521 -0.647 1.00 29.61 ? 199 LEU A CB 1 ATOM 1329 C CG . LEU A 1 164 ? 49.600 30.154 -0.411 1.00 30.28 ? 199 LEU A CG 1 ATOM 1330 C CD1 . LEU A 1 164 ? 48.111 30.137 -0.811 1.00 32.26 ? 199 LEU A CD1 1 ATOM 1331 C CD2 . LEU A 1 164 ? 50.351 29.032 -1.128 1.00 29.28 ? 199 LEU A CD2 1 ATOM 1332 N N . LEU A 1 165 ? 52.358 34.005 0.211 1.00 37.34 ? 200 LEU A N 1 ATOM 1333 C CA . LEU A 1 165 ? 52.911 35.317 -0.247 1.00 43.93 ? 200 LEU A CA 1 ATOM 1334 C C . LEU A 1 165 ? 54.340 35.209 -0.728 1.00 54.25 ? 200 LEU A C 1 ATOM 1335 O O . LEU A 1 165 ? 54.607 35.534 -1.880 1.00 63.41 ? 200 LEU A O 1 ATOM 1336 C CB . LEU A 1 165 ? 52.808 36.395 0.795 1.00 42.32 ? 200 LEU A CB 1 ATOM 1337 C CG . LEU A 1 165 ? 51.320 36.768 0.884 1.00 50.13 ? 200 LEU A CG 1 ATOM 1338 C CD1 . LEU A 1 165 ? 51.087 37.724 2.037 1.00 43.00 ? 200 LEU A CD1 1 ATOM 1339 C CD2 . LEU A 1 165 ? 50.803 37.272 -0.463 1.00 51.95 ? 200 LEU A CD2 1 ATOM 1340 N N . ASP A 1 166 ? 55.249 34.730 0.120 1.00 59.17 ? 201 ASP A N 1 ATOM 1341 C CA . ASP A 1 166 ? 56.631 34.498 -0.344 1.00 68.70 ? 201 ASP A CA 1 ATOM 1342 C C . ASP A 1 166 ? 56.769 33.302 -1.293 1.00 68.60 ? 201 ASP A C 1 ATOM 1343 O O . ASP A 1 166 ? 57.631 33.290 -2.171 1.00 81.11 ? 201 ASP A O 1 ATOM 1344 C CB . ASP A 1 166 ? 57.729 34.513 0.776 1.00 61.19 ? 201 ASP A CB 1 ATOM 1345 C CG . ASP A 1 166 ? 57.367 33.693 2.056 1.00 59.12 ? 201 ASP A CG 1 ATOM 1346 O OD1 . ASP A 1 166 ? 56.777 32.578 1.979 1.00 44.91 ? 201 ASP A OD1 1 ATOM 1347 O OD2 . ASP A 1 166 ? 57.735 34.199 3.175 1.00 49.88 ? 201 ASP A OD2 1 ATOM 1348 N N . LEU A 1 167 ? 55.898 32.320 -1.162 1.00 55.16 ? 202 LEU A N 1 ATOM 1349 C CA . LEU A 1 167 ? 56.018 31.146 -2.031 1.00 49.24 ? 202 LEU A CA 1 ATOM 1350 C C . LEU A 1 167 ? 55.673 31.326 -3.530 1.00 48.96 ? 202 LEU A C 1 ATOM 1351 O O . LEU A 1 167 ? 56.372 30.818 -4.413 1.00 49.44 ? 202 LEU A O 1 ATOM 1352 C CB . LEU A 1 167 ? 55.178 30.023 -1.447 1.00 48.83 ? 202 LEU A CB 1 ATOM 1353 C CG . LEU A 1 167 ? 55.273 28.696 -2.180 1.00 51.27 ? 202 LEU A CG 1 ATOM 1354 C CD1 . LEU A 1 167 ? 56.705 28.161 -2.148 1.00 47.40 ? 202 LEU A CD1 1 ATOM 1355 C CD2 . LEU A 1 167 ? 54.279 27.727 -1.595 1.00 49.37 ? 202 LEU A CD2 1 ATOM 1356 N N . ILE A 1 168 ? 54.583 32.026 -3.830 1.00 48.24 ? 203 ILE A N 1 ATOM 1357 C CA . ILE A 1 168 ? 54.106 32.157 -5.212 1.00 48.41 ? 203 ILE A CA 1 ATOM 1358 C C . ILE A 1 168 ? 55.119 32.770 -6.201 1.00 62.00 ? 203 ILE A C 1 ATOM 1359 O O . ILE A 1 168 ? 55.316 32.188 -7.254 1.00 73.83 ? 203 ILE A O 1 ATOM 1360 C CB . ILE A 1 168 ? 52.732 32.861 -5.308 1.00 48.41 ? 203 ILE A CB 1 ATOM 1361 C CG1 . ILE A 1 168 ? 51.674 31.951 -4.701 1.00 43.88 ? 203 ILE A CG1 1 ATOM 1362 C CG2 . ILE A 1 168 ? 52.410 33.175 -6.758 1.00 48.93 ? 203 ILE A CG2 1 ATOM 1363 C CD1 . ILE A 1 168 ? 50.294 32.563 -4.623 1.00 39.89 ? 203 ILE A CD1 1 ATOM 1364 N N . PRO A 1 169 ? 55.756 33.930 -5.884 1.00 67.12 ? 204 PRO A N 1 ATOM 1365 C CA . PRO A 1 169 ? 56.827 34.336 -6.815 1.00 74.25 ? 204 PRO A CA 1 ATOM 1366 C C . PRO A 1 169 ? 57.983 33.304 -7.082 1.00 84.46 ? 204 PRO A C 1 ATOM 1367 O O . PRO A 1 169 ? 58.589 33.375 -8.152 1.00 88.38 ? 204 PRO A O 1 ATOM 1368 C CB . PRO A 1 169 ? 57.345 35.658 -6.224 1.00 70.52 ? 204 PRO A CB 1 ATOM 1369 C CG . PRO A 1 169 ? 56.574 35.917 -4.966 1.00 63.26 ? 204 PRO A CG 1 ATOM 1370 C CD . PRO A 1 169 ? 55.332 35.075 -5.051 1.00 71.33 ? 204 PRO A CD 1 ATOM 1371 N N . SER A 1 170 ? 58.265 32.362 -6.164 1.00 80.26 ? 205 SER A N 1 ATOM 1372 C CA . SER A 1 170 ? 59.202 31.238 -6.429 1.00 71.51 ? 205 SER A CA 1 ATOM 1373 C C . SER A 1 170 ? 58.823 30.446 -7.665 1.00 70.99 ? 205 SER A C 1 ATOM 1374 O O . SER A 1 170 ? 57.744 29.848 -7.716 1.00 72.22 ? 205 SER A O 1 ATOM 1375 C CB . SER A 1 170 ? 59.255 30.251 -5.257 1.00 77.37 ? 205 SER A CB 1 ATOM 1376 O OG . SER A 1 170 ? 60.051 30.747 -4.203 1.00 81.11 ? 205 SER A OG 1 HETATM 1377 N N . OCS B 2 1 ? 54.377 45.634 7.696 1.00 27.10 ? 225 OCS B N 1 HETATM 1378 C CA . OCS B 2 1 ? 53.841 45.693 9.074 1.00 26.32 ? 225 OCS B CA 1 HETATM 1379 C CB . OCS B 2 1 ? 53.662 44.267 9.608 1.00 34.30 ? 225 OCS B CB 1 HETATM 1380 S SG . OCS B 2 1 ? 53.179 43.206 8.411 1.00 46.22 ? 225 OCS B SG 1 HETATM 1381 C C . OCS B 2 1 ? 54.827 46.282 10.063 1.00 25.97 ? 225 OCS B C 1 HETATM 1382 O O . OCS B 2 1 ? 56.046 46.093 9.923 1.00 22.47 ? 225 OCS B O 1 HETATM 1383 O OD1 . OCS B 2 1 ? 53.127 43.963 7.191 1.00 50.43 ? 225 OCS B OD1 1 HETATM 1384 O OD2 . OCS B 2 1 ? 51.582 42.730 8.552 1.00 43.99 ? 225 OCS B OD2 1 HETATM 1385 O OD3 . OCS B 2 1 ? 54.279 42.226 8.175 1.00 43.54 ? 225 OCS B OD3 1 ATOM 1386 N N . SER B 2 2 ? 54.309 47.020 11.048 1.00 23.42 ? 226 SER B N 1 ATOM 1387 C CA . SER B 2 2 ? 55.083 47.701 12.088 1.00 23.06 ? 226 SER B CA 1 ATOM 1388 C C . SER B 2 2 ? 54.661 47.122 13.426 1.00 23.13 ? 226 SER B C 1 ATOM 1389 O O . SER B 2 2 ? 53.458 46.850 13.658 1.00 23.69 ? 226 SER B O 1 ATOM 1390 C CB . SER B 2 2 ? 54.816 49.227 12.077 1.00 22.95 ? 226 SER B CB 1 ATOM 1391 O OG . SER B 2 2 ? 55.279 49.671 10.819 1.00 21.85 ? 226 SER B OG 1 ATOM 1392 N N . ALA B 2 3 ? 55.667 46.908 14.314 1.00 19.77 ? 227 ALA B N 1 ATOM 1393 C CA . ALA B 2 3 ? 55.383 46.492 15.640 1.00 17.15 ? 227 ALA B CA 1 ATOM 1394 C C . ALA B 2 3 ? 56.326 47.168 16.601 1.00 18.03 ? 227 ALA B C 1 ATOM 1395 O O . ALA B 2 3 ? 57.414 47.600 16.217 1.00 18.12 ? 227 ALA B O 1 ATOM 1396 C CB . ALA B 2 3 ? 55.507 44.940 15.759 1.00 18.16 ? 227 ALA B CB 1 ATOM 1397 N N . LEU B 2 4 ? 55.915 47.251 17.839 1.00 18.75 ? 228 LEU B N 1 ATOM 1398 C CA . LEU B 2 4 ? 56.710 47.977 18.814 1.00 22.18 ? 228 LEU B CA 1 ATOM 1399 C C . LEU B 2 4 ? 56.341 47.480 20.204 1.00 22.45 ? 228 LEU B C 1 ATOM 1400 O O . LEU B 2 4 ? 55.156 47.274 20.522 1.00 20.19 ? 228 LEU B O 1 ATOM 1401 C CB . LEU B 2 4 ? 56.492 49.495 18.738 1.00 20.33 ? 228 LEU B CB 1 ATOM 1402 C CG . LEU B 2 4 ? 57.320 50.306 19.776 1.00 19.97 ? 228 LEU B CG 1 ATOM 1403 C CD1 . LEU B 2 4 ? 58.821 50.451 19.450 1.00 18.82 ? 228 LEU B CD1 1 ATOM 1404 C CD2 . LEU B 2 4 ? 56.673 51.735 19.740 1.00 20.28 ? 228 LEU B CD2 1 ATOM 1405 N N . ILE B 2 5 ? 57.381 47.227 21.014 1.00 20.22 ? 229 ILE B N 1 ATOM 1406 C CA . ILE B 2 5 ? 57.190 46.970 22.430 1.00 21.69 ? 229 ILE B CA 1 ATOM 1407 C C . ILE B 2 5 ? 57.910 48.121 23.080 1.00 24.21 ? 229 ILE B C 1 ATOM 1408 O O . ILE B 2 5 ? 59.031 48.416 22.756 1.00 22.80 ? 229 ILE B O 1 ATOM 1409 C CB . ILE B 2 5 ? 57.835 45.640 22.845 1.00 21.42 ? 229 ILE B CB 1 ATOM 1410 C CG1 . ILE B 2 5 ? 57.151 44.478 22.067 1.00 21.89 ? 229 ILE B CG1 1 ATOM 1411 C CG2 . ILE B 2 5 ? 57.731 45.409 24.396 1.00 18.72 ? 229 ILE B CG2 1 ATOM 1412 C CD1 . ILE B 2 5 ? 57.885 43.147 22.258 1.00 21.11 ? 229 ILE B CD1 1 ATOM 1413 N N . LYS B 2 6 ? 57.239 48.805 24.001 1.00 22.03 ? 230 LYS B N 1 ATOM 1414 C CA . LYS B 2 6 ? 57.860 50.007 24.636 1.00 20.67 ? 230 LYS B CA 1 ATOM 1415 C C . LYS B 2 6 ? 57.623 49.955 26.143 1.00 22.49 ? 230 LYS B C 1 ATOM 1416 O O . LYS B 2 6 ? 56.461 49.864 26.598 1.00 24.57 ? 230 LYS B O 1 ATOM 1417 C CB . LYS B 2 6 ? 57.272 51.328 24.026 1.00 20.83 ? 230 LYS B CB 1 ATOM 1418 C CG . LYS B 2 6 ? 58.133 52.578 24.221 1.00 19.61 ? 230 LYS B CG 1 ATOM 1419 C CD . LYS B 2 6 ? 57.809 53.136 25.668 1.00 21.18 ? 230 LYS B CD 1 ATOM 1420 C CE . LYS B 2 6 ? 58.796 54.266 25.958 1.00 20.21 ? 230 LYS B CE 1 ATOM 1421 N NZ . LYS B 2 6 ? 60.303 53.873 26.137 1.00 24.02 ? 230 LYS B NZ 1 ATOM 1422 N N . VAL B 2 7 ? 58.718 50.036 26.925 1.00 24.04 ? 231 VAL B N 1 ATOM 1423 C CA . VAL B 2 7 ? 58.575 50.023 28.392 1.00 22.94 ? 231 VAL B CA 1 ATOM 1424 C C . VAL B 2 7 ? 58.738 51.430 28.862 1.00 21.75 ? 231 VAL B C 1 ATOM 1425 O O . VAL B 2 7 ? 59.593 52.198 28.355 1.00 22.16 ? 231 VAL B O 1 ATOM 1426 C CB . VAL B 2 7 ? 59.525 48.971 29.073 1.00 22.32 ? 231 VAL B CB 1 ATOM 1427 C CG1 . VAL B 2 7 ? 60.984 49.285 28.767 1.00 20.80 ? 231 VAL B CG1 1 ATOM 1428 C CG2 . VAL B 2 7 ? 59.270 48.783 30.569 1.00 23.97 ? 231 VAL B CG2 1 ATOM 1429 N N . LEU B 2 8 ? 57.914 51.783 29.833 1.00 22.87 ? 232 LEU B N 1 ATOM 1430 C CA . LEU B 2 8 ? 58.017 53.129 30.466 1.00 23.41 ? 232 LEU B CA 1 ATOM 1431 C C . LEU B 2 8 ? 59.342 53.345 31.254 1.00 22.70 ? 232 LEU B C 1 ATOM 1432 O O . LEU B 2 8 ? 60.017 52.374 31.596 1.00 25.04 ? 232 LEU B O 1 ATOM 1433 C CB . LEU B 2 8 ? 56.752 53.354 31.340 1.00 22.99 ? 232 LEU B CB 1 ATOM 1434 C CG . LEU B 2 8 ? 55.446 53.469 30.458 1.00 25.51 ? 232 LEU B CG 1 ATOM 1435 C CD1 . LEU B 2 8 ? 54.377 54.011 31.406 1.00 27.58 ? 232 LEU B CD1 1 ATOM 1436 C CD2 . LEU B 2 8 ? 55.700 54.404 29.279 1.00 20.75 ? 232 LEU B CD2 1 ATOM 1437 N N . PRO B 2 9 ? 59.750 54.619 31.494 1.00 25.55 ? 233 PRO B N 1 ATOM 1438 C CA . PRO B 2 9 ? 61.085 54.821 32.038 1.00 25.26 ? 233 PRO B CA 1 ATOM 1439 C C . PRO B 2 9 ? 61.374 54.251 33.443 1.00 26.92 ? 233 PRO B C 1 ATOM 1440 O O . PRO B 2 9 ? 62.545 53.890 33.695 1.00 25.41 ? 233 PRO B O 1 ATOM 1441 C CB . PRO B 2 9 ? 61.245 56.385 32.016 1.00 22.70 ? 233 PRO B CB 1 ATOM 1442 C CG . PRO B 2 9 ? 60.301 56.826 30.899 1.00 23.03 ? 233 PRO B CG 1 ATOM 1443 C CD . PRO B 2 9 ? 59.120 55.915 31.052 1.00 21.34 ? 233 PRO B CD 1 ATOM 1444 N N . GLY B 2 10 ? 60.326 54.075 34.297 1.00 21.42 ? 234 GLY B N 1 ATOM 1445 C CA . GLY B 2 10 ? 60.467 53.429 35.604 1.00 21.47 ? 234 GLY B CA 1 ATOM 1446 C C . GLY B 2 10 ? 59.826 52.043 35.624 1.00 26.28 ? 234 GLY B C 1 ATOM 1447 O O . GLY B 2 10 ? 59.539 51.499 36.687 1.00 23.36 ? 234 GLY B O 1 ATOM 1448 N N . PHE B 2 11 ? 59.714 51.409 34.434 1.00 24.18 ? 235 PHE B N 1 ATOM 1449 C CA . PHE B 2 11 ? 59.030 50.096 34.266 1.00 23.84 ? 235 PHE B CA 1 ATOM 1450 C C . PHE B 2 11 ? 57.636 50.168 34.848 1.00 23.64 ? 235 PHE B C 1 ATOM 1451 O O . PHE B 2 11 ? 57.122 49.129 35.342 1.00 25.84 ? 235 PHE B O 1 ATOM 1452 C CB . PHE B 2 11 ? 59.814 48.915 34.865 1.00 23.33 ? 235 PHE B CB 1 ATOM 1453 C CG . PHE B 2 11 ? 61.176 48.643 34.194 1.00 24.27 ? 235 PHE B CG 1 ATOM 1454 C CD1 . PHE B 2 11 ? 61.614 49.369 33.087 1.00 22.46 ? 235 PHE B CD1 1 ATOM 1455 C CD2 . PHE B 2 11 ? 61.982 47.653 34.678 1.00 22.99 ? 235 PHE B CD2 1 ATOM 1456 C CE1 . PHE B 2 11 ? 62.837 49.105 32.450 1.00 25.03 ? 235 PHE B CE1 1 ATOM 1457 C CE2 . PHE B 2 11 ? 63.252 47.434 34.132 1.00 24.62 ? 235 PHE B CE2 1 ATOM 1458 C CZ . PHE B 2 11 ? 63.681 48.125 32.980 1.00 22.71 ? 235 PHE B CZ 1 ATOM 1459 N N . GLU B 2 12 ? 57.046 51.352 34.763 1.00 23.99 ? 236 GLU B N 1 ATOM 1460 C CA . GLU B 2 12 ? 55.642 51.543 35.262 1.00 29.58 ? 236 GLU B CA 1 ATOM 1461 C C . GLU B 2 12 ? 54.575 50.828 34.470 1.00 28.46 ? 236 GLU B C 1 ATOM 1462 O O . GLU B 2 12 ? 53.482 50.540 34.996 1.00 25.38 ? 236 GLU B O 1 ATOM 1463 C CB . GLU B 2 12 ? 55.256 53.032 35.392 1.00 26.93 ? 236 GLU B CB 1 ATOM 1464 C CG . GLU B 2 12 ? 56.138 53.769 36.367 1.00 27.33 ? 236 GLU B CG 1 ATOM 1465 C CD . GLU B 2 12 ? 57.302 54.466 35.673 1.00 34.59 ? 236 GLU B CD 1 ATOM 1466 O OE1 . GLU B 2 12 ? 57.643 54.158 34.499 1.00 27.79 ? 236 GLU B OE1 1 ATOM 1467 O OE2 . GLU B 2 12 ? 57.892 55.379 36.303 1.00 30.23 ? 236 GLU B OE2 1 ATOM 1468 N N . ASN B 2 13 ? 54.849 50.566 33.174 1.00 23.84 ? 237 ASN B N 1 ATOM 1469 C CA . ASN B 2 13 ? 53.962 49.792 32.415 1.00 22.84 ? 237 ASN B CA 1 ATOM 1470 C C . ASN B 2 13 ? 54.813 49.284 31.249 1.00 23.10 ? 237 ASN B C 1 ATOM 1471 O O . ASN B 2 13 ? 55.878 49.833 30.962 1.00 24.32 ? 237 ASN B O 1 ATOM 1472 C CB . ASN B 2 13 ? 52.801 50.719 31.832 1.00 23.43 ? 237 ASN B CB 1 ATOM 1473 C CG . ASN B 2 13 ? 51.541 49.927 31.510 1.00 28.66 ? 237 ASN B CG 1 ATOM 1474 O OD1 . ASN B 2 13 ? 51.575 48.661 31.370 1.00 24.25 ? 237 ASN B OD1 1 ATOM 1475 N ND2 . ASN B 2 13 ? 50.411 50.657 31.318 1.00 25.02 ? 237 ASN B ND2 1 ATOM 1476 N N . ILE B 2 14 ? 54.259 48.343 30.486 1.00 21.01 ? 238 ILE B N 1 ATOM 1477 C CA . ILE B 2 14 ? 54.849 48.005 29.155 1.00 22.06 ? 238 ILE B CA 1 ATOM 1478 C C . ILE B 2 14 ? 53.707 47.887 28.100 1.00 22.24 ? 238 ILE B C 1 ATOM 1479 O O . ILE B 2 14 ? 52.683 47.260 28.399 1.00 22.81 ? 238 ILE B O 1 ATOM 1480 C CB . ILE B 2 14 ? 55.633 46.657 29.279 1.00 21.75 ? 238 ILE B CB 1 ATOM 1481 C CG1 . ILE B 2 14 ? 56.245 46.219 27.946 1.00 20.02 ? 238 ILE B CG1 1 ATOM 1482 C CG2 . ILE B 2 14 ? 54.821 45.491 29.868 1.00 22.12 ? 238 ILE B CG2 1 ATOM 1483 C CD1 . ILE B 2 14 ? 57.322 45.104 28.246 1.00 24.89 ? 238 ILE B CD1 1 ATOM 1484 N N . PHE B 2 15 ? 53.902 48.540 26.962 1.00 22.68 ? 239 PHE B N 1 ATOM 1485 C CA . PHE B 2 15 ? 52.973 48.546 25.823 1.00 24.73 ? 239 PHE B CA 1 ATOM 1486 C C . PHE B 2 15 ? 53.474 47.657 24.687 1.00 25.26 ? 239 PHE B C 1 ATOM 1487 O O . PHE B 2 15 ? 54.681 47.536 24.509 1.00 24.86 ? 239 PHE B O 1 ATOM 1488 C CB . PHE B 2 15 ? 52.819 49.958 25.289 1.00 22.99 ? 239 PHE B CB 1 ATOM 1489 C CG . PHE B 2 15 ? 52.215 50.925 26.344 1.00 25.37 ? 239 PHE B CG 1 ATOM 1490 C CD1 . PHE B 2 15 ? 50.829 50.984 26.546 1.00 29.70 ? 239 PHE B CD1 1 ATOM 1491 C CD2 . PHE B 2 15 ? 53.021 51.662 27.158 1.00 24.99 ? 239 PHE B CD2 1 ATOM 1492 C CE1 . PHE B 2 15 ? 50.263 51.843 27.528 1.00 27.08 ? 239 PHE B CE1 1 ATOM 1493 C CE2 . PHE B 2 15 ? 52.498 52.461 28.193 1.00 28.87 ? 239 PHE B CE2 1 ATOM 1494 C CZ . PHE B 2 15 ? 51.097 52.570 28.341 1.00 30.48 ? 239 PHE B CZ 1 ATOM 1495 N N . PHE B 2 16 ? 52.562 46.995 23.974 1.00 22.22 ? 240 PHE B N 1 ATOM 1496 C CA . PHE B 2 16 ? 53.002 46.232 22.798 1.00 21.02 ? 240 PHE B CA 1 ATOM 1497 C C . PHE B 2 16 ? 51.924 46.418 21.770 1.00 22.67 ? 240 PHE B C 1 ATOM 1498 O O . PHE B 2 16 ? 50.739 46.461 22.136 1.00 22.77 ? 240 PHE B O 1 ATOM 1499 C CB . PHE B 2 16 ? 53.109 44.724 23.126 1.00 21.88 ? 240 PHE B CB 1 ATOM 1500 C CG . PHE B 2 16 ? 52.239 44.261 24.294 1.00 26.48 ? 240 PHE B CG 1 ATOM 1501 C CD1 . PHE B 2 16 ? 52.661 44.468 25.627 1.00 26.83 ? 240 PHE B CD1 1 ATOM 1502 C CD2 . PHE B 2 16 ? 51.024 43.580 24.066 1.00 23.59 ? 240 PHE B CD2 1 ATOM 1503 C CE1 . PHE B 2 16 ? 51.884 44.022 26.689 1.00 29.48 ? 240 PHE B CE1 1 ATOM 1504 C CE2 . PHE B 2 16 ? 50.260 43.144 25.146 1.00 25.89 ? 240 PHE B CE2 1 ATOM 1505 C CZ . PHE B 2 16 ? 50.689 43.377 26.430 1.00 25.97 ? 240 PHE B CZ 1 ATOM 1506 N N . ALA B 2 17 ? 52.315 46.518 20.507 1.00 20.25 ? 241 ALA B N 1 ATOM 1507 C CA . ALA B 2 17 ? 51.318 46.877 19.473 1.00 22.50 ? 241 ALA B CA 1 ATOM 1508 C C . ALA B 2 17 ? 51.755 46.390 18.144 1.00 23.85 ? 241 ALA B C 1 ATOM 1509 O O . ALA B 2 17 ? 52.993 46.199 17.909 1.00 22.88 ? 241 ALA B O 1 ATOM 1510 C CB . ALA B 2 17 ? 51.138 48.416 19.437 1.00 18.71 ? 241 ALA B CB 1 ATOM 1511 N N . HIS B 2 18 ? 50.816 46.149 17.234 1.00 19.06 ? 242 HIS B N 1 ATOM 1512 C CA . HIS B 2 18 ? 51.179 45.772 15.856 1.00 19.59 ? 242 HIS B CA 1 ATOM 1513 C C . HIS B 2 18 ? 50.248 46.495 14.902 1.00 19.98 ? 242 HIS B C 1 ATOM 1514 O O . HIS B 2 18 ? 49.010 46.506 15.196 1.00 20.52 ? 242 HIS B O 1 ATOM 1515 C CB . HIS B 2 18 ? 50.955 44.305 15.769 1.00 19.66 ? 242 HIS B CB 1 ATOM 1516 C CG . HIS B 2 18 ? 51.202 43.700 14.392 1.00 21.49 ? 242 HIS B CG 1 ATOM 1517 N ND1 . HIS B 2 18 ? 50.239 43.650 13.421 1.00 22.99 ? 242 HIS B ND1 1 ATOM 1518 C CD2 . HIS B 2 18 ? 52.351 43.049 13.853 1.00 22.97 ? 242 HIS B CD2 1 ATOM 1519 C CE1 . HIS B 2 18 ? 50.735 43.068 12.320 1.00 26.37 ? 242 HIS B CE1 1 ATOM 1520 N NE2 . HIS B 2 18 ? 52.034 42.677 12.582 1.00 24.48 ? 242 HIS B NE2 1 ATOM 1521 N N . SER B 2 19 ? 50.779 47.061 13.835 1.00 21.57 ? 243 SER B N 1 ATOM 1522 C CA . SER B 2 19 ? 49.936 47.614 12.779 1.00 22.41 ? 243 SER B CA 1 ATOM 1523 C C . SER B 2 19 ? 50.200 46.831 11.479 1.00 21.63 ? 243 SER B C 1 ATOM 1524 O O . SER B 2 19 ? 51.310 46.926 10.897 1.00 20.46 ? 243 SER B O 1 ATOM 1525 C CB . SER B 2 19 ? 50.192 49.111 12.566 1.00 21.88 ? 243 SER B CB 1 ATOM 1526 O OG . SER B 2 19 ? 49.891 49.944 13.718 1.00 20.57 ? 243 SER B OG 1 ATOM 1527 N N . SER B 2 20 ? 49.187 46.071 11.037 1.00 21.17 ? 244 SER B N 1 ATOM 1528 C CA . SER B 2 20 ? 49.295 45.238 9.807 1.00 19.90 ? 244 SER B CA 1 ATOM 1529 C C . SER B 2 20 ? 49.385 46.085 8.557 1.00 26.00 ? 244 SER B C 1 ATOM 1530 O O . SER B 2 20 ? 48.747 47.132 8.520 1.00 23.28 ? 244 SER B O 1 ATOM 1531 C CB . SER B 2 20 ? 48.071 44.353 9.592 1.00 19.54 ? 244 SER B CB 1 ATOM 1532 O OG . SER B 2 20 ? 47.851 43.660 10.798 1.00 22.89 ? 244 SER B OG 1 ATOM 1533 N N . TRP B 2 21 ? 50.197 45.677 7.586 1.00 20.36 ? 245 TRP B N 1 ATOM 1534 C CA . TRP B 2 21 ? 50.192 46.266 6.201 1.00 23.51 ? 245 TRP B CA 1 ATOM 1535 C C . TRP B 2 21 ? 49.977 45.133 5.260 1.00 29.26 ? 245 TRP B C 1 ATOM 1536 O O . TRP B 2 21 ? 50.729 44.106 5.287 1.00 23.47 ? 245 TRP B O 1 ATOM 1537 C CB . TRP B 2 21 ? 51.481 46.887 5.727 1.00 25.16 ? 245 TRP B CB 1 ATOM 1538 C CG . TRP B 2 21 ? 52.129 47.972 6.551 1.00 22.87 ? 245 TRP B CG 1 ATOM 1539 C CD1 . TRP B 2 21 ? 51.792 48.450 7.803 1.00 24.69 ? 245 TRP B CD1 1 ATOM 1540 C CD2 . TRP B 2 21 ? 53.280 48.758 6.141 1.00 19.76 ? 245 TRP B CD2 1 ATOM 1541 N NE1 . TRP B 2 21 ? 52.630 49.418 8.176 1.00 22.51 ? 245 TRP B NE1 1 ATOM 1542 C CE2 . TRP B 2 21 ? 53.538 49.670 7.216 1.00 20.72 ? 245 TRP B CE2 1 ATOM 1543 C CE3 . TRP B 2 21 ? 54.113 48.749 5.008 1.00 19.85 ? 245 TRP B CE3 1 ATOM 1544 C CZ2 . TRP B 2 21 ? 54.592 50.571 7.197 1.00 24.09 ? 245 TRP B CZ2 1 ATOM 1545 C CZ3 . TRP B 2 21 ? 55.179 49.694 4.979 1.00 24.74 ? 245 TRP B CZ3 1 ATOM 1546 C CH2 . TRP B 2 21 ? 55.374 50.609 6.046 1.00 21.69 ? 245 TRP B CH2 1 ATOM 1547 N N . TYR B 2 22 ? 49.010 45.288 4.340 1.00 25.53 ? 246 TYR B N 1 ATOM 1548 C CA . TYR B 2 22 ? 48.800 44.316 3.273 1.00 23.80 ? 246 TYR B CA 1 ATOM 1549 C C . TYR B 2 22 ? 47.760 44.915 2.300 1.00 26.96 ? 246 TYR B C 1 ATOM 1550 O O . TYR B 2 22 ? 47.514 46.140 2.356 1.00 24.90 ? 246 TYR B O 1 ATOM 1551 C CB . TYR B 2 22 ? 48.379 42.993 3.895 1.00 21.93 ? 246 TYR B CB 1 ATOM 1552 C CG . TYR B 2 22 ? 48.251 41.832 2.910 1.00 23.97 ? 246 TYR B CG 1 ATOM 1553 C CD1 . TYR B 2 22 ? 49.093 41.676 1.806 1.00 26.79 ? 246 TYR B CD1 1 ATOM 1554 C CD2 . TYR B 2 22 ? 47.215 40.934 3.102 1.00 25.54 ? 246 TYR B CD2 1 ATOM 1555 C CE1 . TYR B 2 22 ? 48.896 40.677 0.896 1.00 31.23 ? 246 TYR B CE1 1 ATOM 1556 C CE2 . TYR B 2 22 ? 47.029 39.879 2.235 1.00 30.93 ? 246 TYR B CE2 1 ATOM 1557 C CZ . TYR B 2 22 ? 47.850 39.771 1.127 1.00 32.77 ? 246 TYR B CZ 1 ATOM 1558 O OH . TYR B 2 22 ? 47.534 38.745 0.274 1.00 32.34 ? 246 TYR B OH 1 ATOM 1559 N N . THR B 2 23 ? 47.194 44.120 1.423 1.00 24.63 ? 247 THR B N 1 ATOM 1560 C CA . THR B 2 23 ? 46.232 44.685 0.481 1.00 25.49 ? 247 THR B CA 1 ATOM 1561 C C . THR B 2 23 ? 44.985 45.088 1.235 1.00 20.30 ? 247 THR B C 1 ATOM 1562 O O . THR B 2 23 ? 44.539 44.411 2.178 1.00 19.92 ? 247 THR B O 1 ATOM 1563 C CB . THR B 2 23 ? 45.893 43.755 -0.691 1.00 27.78 ? 247 THR B CB 1 ATOM 1564 O OG1 . THR B 2 23 ? 44.675 44.296 -1.294 1.00 32.11 ? 247 THR B OG1 1 ATOM 1565 C CG2 . THR B 2 23 ? 45.636 42.338 -0.189 1.00 27.31 ? 247 THR B CG2 1 ATOM 1566 N N . TYR B 2 24 ? 44.434 46.259 0.946 1.00 25.24 ? 248 TYR B N 1 ATOM 1567 C CA . TYR B 2 24 ? 43.120 46.603 1.595 1.00 25.24 ? 248 TYR B CA 1 ATOM 1568 C C . TYR B 2 24 ? 42.017 45.602 1.301 1.00 25.08 ? 248 TYR B C 1 ATOM 1569 O O . TYR B 2 24 ? 40.987 45.557 2.026 1.00 26.77 ? 248 TYR B O 1 ATOM 1570 C CB . TYR B 2 24 ? 42.666 48.036 1.250 1.00 25.81 ? 248 TYR B CB 1 ATOM 1571 C CG . TYR B 2 24 ? 43.614 49.166 1.659 1.00 27.44 ? 248 TYR B CG 1 ATOM 1572 C CD1 . TYR B 2 24 ? 44.539 49.012 2.689 1.00 27.93 ? 248 TYR B CD1 1 ATOM 1573 C CD2 . TYR B 2 24 ? 43.502 50.436 1.071 1.00 31.46 ? 248 TYR B CD2 1 ATOM 1574 C CE1 . TYR B 2 24 ? 45.390 50.066 3.067 1.00 24.74 ? 248 TYR B CE1 1 ATOM 1575 C CE2 . TYR B 2 24 ? 44.296 51.523 1.461 1.00 28.13 ? 248 TYR B CE2 1 ATOM 1576 C CZ . TYR B 2 24 ? 45.260 51.331 2.478 1.00 26.03 ? 248 TYR B CZ 1 ATOM 1577 O OH . TYR B 2 24 ? 46.096 52.392 2.821 1.00 27.53 ? 248 TYR B OH 1 ATOM 1578 N N . ALA B 2 25 ? 42.188 44.773 0.276 1.00 23.98 ? 249 ALA B N 1 ATOM 1579 C CA . ALA B 2 25 ? 41.198 43.660 0.044 1.00 26.04 ? 249 ALA B CA 1 ATOM 1580 C C . ALA B 2 25 ? 41.135 42.636 1.156 1.00 27.28 ? 249 ALA B C 1 ATOM 1581 O O . ALA B 2 25 ? 40.218 41.768 1.219 1.00 29.43 ? 249 ALA B O 1 ATOM 1582 C CB . ALA B 2 25 ? 41.463 42.955 -1.294 1.00 27.46 ? 249 ALA B CB 1 ATOM 1583 N N . ALA B 2 26 ? 42.055 42.761 2.127 1.00 27.88 ? 250 ALA B N 1 ATOM 1584 C CA . ALA B 2 26 ? 42.003 41.835 3.242 1.00 24.86 ? 250 ALA B CA 1 ATOM 1585 C C . ALA B 2 26 ? 41.215 42.408 4.439 1.00 26.62 ? 250 ALA B C 1 ATOM 1586 O O . ALA B 2 26 ? 40.997 41.679 5.415 1.00 26.63 ? 250 ALA B O 1 ATOM 1587 C CB . ALA B 2 26 ? 43.435 41.435 3.670 1.00 27.75 ? 250 ALA B CB 1 ATOM 1588 N N . MET B 2 27 ? 40.680 43.647 4.366 1.00 29.24 ? 251 MET B N 1 ATOM 1589 C CA . MET B 2 27 ? 40.019 44.252 5.542 1.00 32.23 ? 251 MET B CA 1 ATOM 1590 C C . MET B 2 27 ? 38.592 43.792 5.919 1.00 31.69 ? 251 MET B C 1 ATOM 1591 O O . MET B 2 27 ? 37.862 44.552 6.563 1.00 30.93 ? 251 MET B O 1 ATOM 1592 C CB . MET B 2 27 ? 39.999 45.780 5.439 1.00 30.77 ? 251 MET B CB 1 ATOM 1593 C CG . MET B 2 27 ? 41.323 46.392 5.066 1.00 29.68 ? 251 MET B CG 1 ATOM 1594 S SD . MET B 2 27 ? 41.408 48.226 5.134 1.00 32.93 ? 251 MET B SD 1 ATOM 1595 C CE . MET B 2 27 ? 40.260 48.810 3.810 1.00 33.67 ? 251 MET B CE 1 ATOM 1596 N N . LEU B 2 28 ? 38.215 42.575 5.584 1.00 27.78 ? 252 LEU B N 1 ATOM 1597 C CA . LEU B 2 28 ? 37.051 41.932 6.155 1.00 28.17 ? 252 LEU B CA 1 ATOM 1598 C C . LEU B 2 28 ? 37.529 41.188 7.471 1.00 29.75 ? 252 LEU B C 1 ATOM 1599 O O . LEU B 2 28 ? 38.007 40.016 7.441 1.00 31.37 ? 252 LEU B O 1 ATOM 1600 C CB . LEU B 2 28 ? 36.441 40.923 5.163 1.00 26.16 ? 252 LEU B CB 1 ATOM 1601 C CG . LEU B 2 28 ? 35.103 40.228 5.556 1.00 30.04 ? 252 LEU B CG 1 ATOM 1602 C CD1 . LEU B 2 28 ? 34.060 41.341 5.807 1.00 34.33 ? 252 LEU B CD1 1 ATOM 1603 C CD2 . LEU B 2 28 ? 34.652 39.364 4.404 1.00 27.61 ? 252 LEU B CD2 1 ATOM 1604 N N . ARG B 2 29 ? 37.415 41.870 8.615 1.00 25.24 ? 253 ARG B N 1 ATOM 1605 C CA . ARG B 2 29 ? 38.156 41.428 9.812 1.00 24.74 ? 253 ARG B CA 1 ATOM 1606 C C . ARG B 2 29 ? 37.298 40.739 10.760 1.00 31.46 ? 253 ARG B C 1 ATOM 1607 O O . ARG B 2 29 ? 36.089 41.102 10.875 1.00 33.09 ? 253 ARG B O 1 ATOM 1608 C CB . ARG B 2 29 ? 38.710 42.615 10.555 1.00 23.63 ? 253 ARG B CB 1 ATOM 1609 C CG . ARG B 2 29 ? 39.597 43.469 9.736 1.00 23.65 ? 253 ARG B CG 1 ATOM 1610 C CD . ARG B 2 29 ? 40.790 42.751 9.119 1.00 30.06 ? 253 ARG B CD 1 ATOM 1611 N NE . ARG B 2 29 ? 41.568 41.958 10.078 1.00 25.59 ? 253 ARG B NE 1 ATOM 1612 C CZ . ARG B 2 29 ? 42.645 42.374 10.711 1.00 24.55 ? 253 ARG B CZ 1 ATOM 1613 N NH1 . ARG B 2 29 ? 43.032 43.611 10.539 1.00 21.30 ? 253 ARG B NH1 1 ATOM 1614 N NH2 . ARG B 2 29 ? 43.340 41.506 11.543 1.00 23.70 ? 253 ARG B NH2 1 ATOM 1615 N N . ILE B 2 30 ? 37.876 39.754 11.473 1.00 26.54 ? 254 ILE B N 1 ATOM 1616 C CA . ILE B 2 30 ? 37.192 39.183 12.639 1.00 29.63 ? 254 ILE B CA 1 ATOM 1617 C C . ILE B 2 30 ? 38.200 39.150 13.825 1.00 30.36 ? 254 ILE B C 1 ATOM 1618 O O . ILE B 2 30 ? 39.294 38.536 13.683 1.00 25.78 ? 254 ILE B O 1 ATOM 1619 C CB . ILE B 2 30 ? 36.677 37.749 12.390 1.00 27.44 ? 254 ILE B CB 1 ATOM 1620 C CG1 . ILE B 2 30 ? 35.650 37.686 11.205 1.00 28.26 ? 254 ILE B CG1 1 ATOM 1621 C CG2 . ILE B 2 30 ? 35.988 37.197 13.671 1.00 28.39 ? 254 ILE B CG2 1 ATOM 1622 C CD1 . ILE B 2 30 ? 35.130 36.288 10.876 1.00 24.75 ? 254 ILE B CD1 1 ATOM 1623 N N . TYR B 2 31 ? 37.825 39.746 14.951 1.00 26.71 ? 255 TYR B N 1 ATOM 1624 C CA . TYR B 2 31 ? 38.615 39.666 16.191 1.00 28.59 ? 255 TYR B CA 1 ATOM 1625 C C . TYR B 2 31 ? 38.105 38.473 16.929 1.00 29.70 ? 255 TYR B C 1 ATOM 1626 O O . TYR B 2 31 ? 36.905 38.307 17.020 1.00 31.99 ? 255 TYR B O 1 ATOM 1627 C CB . TYR B 2 31 ? 38.615 40.985 16.967 1.00 26.91 ? 255 TYR B CB 1 ATOM 1628 C CG . TYR B 2 31 ? 39.805 41.069 17.959 1.00 24.97 ? 255 TYR B CG 1 ATOM 1629 C CD1 . TYR B 2 31 ? 39.756 40.336 19.146 1.00 22.51 ? 255 TYR B CD1 1 ATOM 1630 C CD2 . TYR B 2 31 ? 40.957 41.906 17.679 1.00 25.19 ? 255 TYR B CD2 1 ATOM 1631 C CE1 . TYR B 2 31 ? 40.837 40.348 20.053 1.00 27.53 ? 255 TYR B CE1 1 ATOM 1632 C CE2 . TYR B 2 31 ? 42.047 41.921 18.578 1.00 27.73 ? 255 TYR B CE2 1 ATOM 1633 C CZ . TYR B 2 31 ? 41.973 41.131 19.747 1.00 27.49 ? 255 TYR B CZ 1 ATOM 1634 O OH . TYR B 2 31 ? 42.943 41.130 20.729 1.00 33.61 ? 255 TYR B OH 1 ATOM 1635 N N . LYS B 2 32 ? 39.003 37.532 17.302 1.00 25.50 ? 256 LYS B N 1 ATOM 1636 C CA . LYS B 2 32 ? 38.622 36.294 17.838 1.00 23.67 ? 256 LYS B CA 1 ATOM 1637 C C . LYS B 2 32 ? 39.039 36.057 19.287 1.00 27.23 ? 256 LYS B C 1 ATOM 1638 O O . LYS B 2 32 ? 40.210 36.384 19.698 1.00 25.46 ? 256 LYS B O 1 ATOM 1639 C CB . LYS B 2 32 ? 39.162 35.117 16.980 1.00 25.82 ? 256 LYS B CB 1 ATOM 1640 C CG . LYS B 2 32 ? 38.841 35.311 15.500 1.00 23.90 ? 256 LYS B CG 1 ATOM 1641 C CD . LYS B 2 32 ? 39.224 34.050 14.696 1.00 21.02 ? 256 LYS B CD 1 ATOM 1642 C CE . LYS B 2 32 ? 38.668 34.374 13.266 1.00 22.77 ? 256 LYS B CE 1 ATOM 1643 N NZ . LYS B 2 32 ? 39.072 33.276 12.295 1.00 23.31 ? 256 LYS B NZ 1 ATOM 1644 N N . HIS B 2 33 ? 38.110 35.466 20.023 1.00 26.50 ? 257 HIS B N 1 ATOM 1645 C CA . HIS B 2 33 ? 38.350 35.010 21.403 1.00 29.27 ? 257 HIS B CA 1 ATOM 1646 C C . HIS B 2 33 ? 38.029 33.541 21.462 1.00 28.10 ? 257 HIS B C 1 ATOM 1647 O O . HIS B 2 33 ? 36.852 33.126 21.325 1.00 31.09 ? 257 HIS B O 1 ATOM 1648 C CB . HIS B 2 33 ? 37.528 35.815 22.416 1.00 31.11 ? 257 HIS B CB 1 ATOM 1649 C CG . HIS B 2 33 ? 37.644 37.327 22.283 1.00 28.80 ? 257 HIS B CG 1 ATOM 1650 N ND1 . HIS B 2 33 ? 38.710 38.034 22.704 1.00 28.06 ? 257 HIS B ND1 1 ATOM 1651 C CD2 . HIS B 2 33 ? 36.721 38.269 21.789 1.00 27.63 ? 257 HIS B CD2 1 ATOM 1652 C CE1 . HIS B 2 33 ? 38.516 39.346 22.451 1.00 25.41 ? 257 HIS B CE1 1 ATOM 1653 N NE2 . HIS B 2 33 ? 37.303 39.490 21.881 1.00 29.81 ? 257 HIS B NE2 1 ATOM 1654 N N . TRP B 2 34 ? 39.026 32.676 21.632 1.00 24.69 ? 258 TRP B N 1 ATOM 1655 C CA . TRP B 2 34 ? 38.784 31.270 21.761 1.00 25.91 ? 258 TRP B CA 1 ATOM 1656 C C . TRP B 2 34 ? 39.141 30.807 23.163 1.00 34.24 ? 258 TRP B C 1 ATOM 1657 O O . TRP B 2 34 ? 40.242 31.137 23.673 1.00 29.33 ? 258 TRP B O 1 ATOM 1658 C CB . TRP B 2 34 ? 39.682 30.452 20.846 1.00 26.15 ? 258 TRP B CB 1 ATOM 1659 C CG . TRP B 2 34 ? 39.441 30.536 19.328 1.00 27.66 ? 258 TRP B CG 1 ATOM 1660 C CD1 . TRP B 2 34 ? 38.327 31.038 18.654 1.00 28.80 ? 258 TRP B CD1 1 ATOM 1661 C CD2 . TRP B 2 34 ? 40.395 30.180 18.288 1.00 26.12 ? 258 TRP B CD2 1 ATOM 1662 N NE1 . TRP B 2 34 ? 38.505 30.926 17.295 1.00 29.34 ? 258 TRP B NE1 1 ATOM 1663 C CE2 . TRP B 2 34 ? 39.713 30.406 17.008 1.00 23.30 ? 258 TRP B CE2 1 ATOM 1664 C CE3 . TRP B 2 34 ? 41.701 29.614 18.284 1.00 27.66 ? 258 TRP B CE3 1 ATOM 1665 C CZ2 . TRP B 2 34 ? 40.313 30.131 15.817 1.00 25.94 ? 258 TRP B CZ2 1 ATOM 1666 C CZ3 . TRP B 2 34 ? 42.318 29.365 17.067 1.00 27.68 ? 258 TRP B CZ3 1 ATOM 1667 C CH2 . TRP B 2 34 ? 41.657 29.596 15.854 1.00 24.84 ? 258 TRP B CH2 1 ATOM 1668 N N . ASP B 2 35 ? 38.326 29.890 23.701 1.00 28.90 ? 259 ASP B N 1 ATOM 1669 C CA . ASP B 2 35 ? 38.632 29.167 24.951 1.00 31.33 ? 259 ASP B CA 1 ATOM 1670 C C . ASP B 2 35 ? 38.159 27.755 24.791 1.00 30.44 ? 259 ASP B C 1 ATOM 1671 O O . ASP B 2 35 ? 36.960 27.469 24.754 1.00 34.26 ? 259 ASP B O 1 ATOM 1672 C CB . ASP B 2 35 ? 37.930 29.848 26.128 1.00 30.02 ? 259 ASP B CB 1 ATOM 1673 C CG . ASP B 2 35 ? 38.276 29.226 27.475 1.00 32.13 ? 259 ASP B CG 1 ATOM 1674 O OD1 . ASP B 2 35 ? 38.996 28.179 27.586 1.00 32.79 ? 259 ASP B OD1 1 ATOM 1675 O OD2 . ASP B 2 35 ? 37.782 29.808 28.448 1.00 34.21 ? 259 ASP B OD2 1 ATOM 1676 N N . PHE B 2 36 ? 39.111 26.866 24.706 1.00 26.96 ? 260 PHE B N 1 ATOM 1677 C CA . PHE B 2 36 ? 38.874 25.480 24.509 1.00 30.03 ? 260 PHE B CA 1 ATOM 1678 C C . PHE B 2 36 ? 39.326 24.714 25.759 1.00 35.85 ? 260 PHE B C 1 ATOM 1679 O O . PHE B 2 36 ? 40.452 24.853 26.251 1.00 33.95 ? 260 PHE B O 1 ATOM 1680 C CB . PHE B 2 36 ? 39.708 25.007 23.341 1.00 31.21 ? 260 PHE B CB 1 ATOM 1681 C CG . PHE B 2 36 ? 39.495 25.817 22.043 1.00 30.96 ? 260 PHE B CG 1 ATOM 1682 C CD1 . PHE B 2 36 ? 38.306 26.534 21.791 1.00 30.28 ? 260 PHE B CD1 1 ATOM 1683 C CD2 . PHE B 2 36 ? 40.534 25.838 21.064 1.00 35.52 ? 260 PHE B CD2 1 ATOM 1684 C CE1 . PHE B 2 36 ? 38.137 27.211 20.564 1.00 33.28 ? 260 PHE B CE1 1 ATOM 1685 C CE2 . PHE B 2 36 ? 40.375 26.539 19.865 1.00 32.85 ? 260 PHE B CE2 1 ATOM 1686 C CZ . PHE B 2 36 ? 39.174 27.225 19.624 1.00 31.70 ? 260 PHE B CZ 1 ATOM 1687 N N . ASN B 2 37 ? 38.457 23.868 26.255 1.00 30.28 ? 261 ASN B N 1 ATOM 1688 C CA . ASN B 2 37 ? 38.719 23.187 27.559 1.00 32.86 ? 261 ASN B CA 1 ATOM 1689 C C . ASN B 2 37 ? 39.660 22.022 27.424 1.00 34.60 ? 261 ASN B C 1 ATOM 1690 O O . ASN B 2 37 ? 39.295 20.866 27.735 1.00 33.39 ? 261 ASN B O 1 ATOM 1691 C CB . ASN B 2 37 ? 37.378 22.704 28.203 1.00 34.28 ? 261 ASN B CB 1 ATOM 1692 C CG . ASN B 2 37 ? 37.539 22.437 29.691 1.00 44.90 ? 261 ASN B CG 1 ATOM 1693 O OD1 . ASN B 2 37 ? 38.546 22.848 30.344 1.00 34.21 ? 261 ASN B OD1 1 ATOM 1694 N ND2 . ASN B 2 37 ? 36.566 21.740 30.242 1.00 40.54 ? 261 ASN B ND2 1 ATOM 1695 N N . ILE B 2 38 ? 40.887 22.270 26.923 1.00 33.27 ? 262 ILE B N 1 ATOM 1696 C CA . ILE B 2 38 ? 41.803 21.143 26.671 1.00 32.07 ? 262 ILE B CA 1 ATOM 1697 C C . ILE B 2 38 ? 42.502 20.713 28.000 1.00 35.58 ? 262 ILE B C 1 ATOM 1698 O O . ILE B 2 38 ? 42.895 21.584 28.813 1.00 34.18 ? 262 ILE B O 1 ATOM 1699 C CB . ILE B 2 38 ? 42.893 21.534 25.622 1.00 30.50 ? 262 ILE B CB 1 ATOM 1700 C CG1 . ILE B 2 38 ? 42.223 22.025 24.313 1.00 34.52 ? 262 ILE B CG1 1 ATOM 1701 C CG2 . ILE B 2 38 ? 43.815 20.383 25.318 1.00 33.63 ? 262 ILE B CG2 1 ATOM 1702 C CD1 . ILE B 2 38 ? 41.391 20.950 23.593 1.00 29.11 ? 262 ILE B CD1 1 ATOM 1703 N N . VAL B 2 39 ? 42.676 19.400 28.164 1.00 36.12 ? 263 VAL B N 1 ATOM 1704 C CA . VAL B 2 39 ? 43.246 18.798 29.339 1.00 37.68 ? 263 VAL B CA 1 ATOM 1705 C C . VAL B 2 39 ? 44.303 17.868 28.862 1.00 35.44 ? 263 VAL B C 1 ATOM 1706 O O . VAL B 2 39 ? 44.061 16.757 28.386 1.00 38.35 ? 263 VAL B O 1 ATOM 1707 C CB . VAL B 2 39 ? 42.129 18.057 30.148 1.00 50.29 ? 263 VAL B CB 1 ATOM 1708 C CG1 . VAL B 2 39 ? 42.713 17.062 31.140 1.00 47.28 ? 263 VAL B CG1 1 ATOM 1709 C CG2 . VAL B 2 39 ? 41.210 19.082 30.829 1.00 38.31 ? 263 VAL B CG2 1 ATOM 1710 N N . ASP B 2 40 ? 45.537 18.335 28.978 1.00 36.67 ? 264 ASP B N 1 ATOM 1711 C CA . ASP B 2 40 ? 46.662 17.680 28.356 1.00 38.44 ? 264 ASP B CA 1 ATOM 1712 C C . ASP B 2 40 ? 47.912 18.227 29.023 1.00 42.88 ? 264 ASP B C 1 ATOM 1713 O O . ASP B 2 40 ? 48.096 19.489 29.168 1.00 32.95 ? 264 ASP B O 1 ATOM 1714 C CB . ASP B 2 40 ? 46.696 17.984 26.847 1.00 39.50 ? 264 ASP B CB 1 ATOM 1715 C CG . ASP B 2 40 ? 47.793 17.242 26.144 1.00 40.49 ? 264 ASP B CG 1 ATOM 1716 O OD1 . ASP B 2 40 ? 48.912 17.239 26.682 1.00 40.57 ? 264 ASP B OD1 1 ATOM 1717 O OD2 . ASP B 2 40 ? 47.590 16.684 25.020 1.00 40.84 ? 264 ASP B OD2 1 ATOM 1718 N N . LYS B 2 41 ? 48.755 17.291 29.461 1.00 41.23 ? 265 LYS B N 1 ATOM 1719 C CA . LYS B 2 41 ? 49.940 17.699 30.277 1.00 47.01 ? 265 LYS B CA 1 ATOM 1720 C C . LYS B 2 41 ? 50.981 18.522 29.506 1.00 47.42 ? 265 LYS B C 1 ATOM 1721 O O . LYS B 2 41 ? 51.708 19.320 30.109 1.00 42.25 ? 265 LYS B O 1 ATOM 1722 C CB . LYS B 2 41 ? 50.565 16.512 31.016 1.00 44.67 ? 265 LYS B CB 1 ATOM 1723 C CG . LYS B 2 41 ? 51.162 15.392 30.190 1.00 56.75 ? 265 LYS B CG 1 ATOM 1724 C CD . LYS B 2 41 ? 51.549 14.257 31.140 1.00 61.29 ? 265 LYS B CD 1 ATOM 1725 C CE . LYS B 2 41 ? 52.662 13.374 30.601 1.00 65.42 ? 265 LYS B CE 1 ATOM 1726 N NZ . LYS B 2 41 ? 52.302 12.833 29.270 1.00 67.45 ? 265 LYS B NZ 1 ATOM 1727 N N . ASP B 2 42 ? 50.988 18.376 28.172 1.00 43.12 ? 266 ASP B N 1 ATOM 1728 C CA . ASP B 2 42 ? 51.912 19.102 27.282 1.00 39.46 ? 266 ASP B CA 1 ATOM 1729 C C . ASP B 2 42 ? 51.252 20.332 26.612 1.00 36.14 ? 266 ASP B C 1 ATOM 1730 O O . ASP B 2 42 ? 51.895 21.011 25.793 1.00 35.81 ? 266 ASP B O 1 ATOM 1731 C CB . ASP B 2 42 ? 52.480 18.132 26.249 1.00 41.04 ? 266 ASP B CB 1 ATOM 1732 C CG . ASP B 2 42 ? 53.200 17.002 26.893 1.00 41.18 ? 266 ASP B CG 1 ATOM 1733 O OD1 . ASP B 2 42 ? 54.094 17.321 27.664 1.00 46.94 ? 266 ASP B OD1 1 ATOM 1734 O OD2 . ASP B 2 42 ? 52.881 15.810 26.687 1.00 48.21 ? 266 ASP B OD2 1 ATOM 1735 N N . THR B 2 43 ? 50.011 20.645 26.986 1.00 33.17 ? 267 THR B N 1 ATOM 1736 C CA . THR B 2 43 ? 49.363 21.900 26.583 1.00 33.84 ? 267 THR B CA 1 ATOM 1737 C C . THR B 2 43 ? 49.665 22.950 27.622 1.00 37.79 ? 267 THR B C 1 ATOM 1738 O O . THR B 2 43 ? 49.363 22.733 28.819 1.00 35.45 ? 267 THR B O 1 ATOM 1739 C CB . THR B 2 43 ? 47.836 21.768 26.483 1.00 33.84 ? 267 THR B CB 1 ATOM 1740 O OG1 . THR B 2 43 ? 47.571 20.824 25.467 1.00 38.26 ? 267 THR B OG1 1 ATOM 1741 C CG2 . THR B 2 43 ? 47.180 23.109 26.080 1.00 31.50 ? 267 THR B CG2 1 ATOM 1742 N N . SER B 2 44 ? 50.243 24.082 27.200 1.00 29.84 ? 268 SER B N 1 ATOM 1743 C CA . SER B 2 44 ? 50.340 25.267 28.097 1.00 29.29 ? 268 SER B CA 1 ATOM 1744 C C . SER B 2 44 ? 49.216 26.260 27.943 1.00 32.41 ? 268 SER B C 1 ATOM 1745 O O . SER B 2 44 ? 48.969 27.008 28.845 1.00 31.82 ? 268 SER B O 1 ATOM 1746 C CB . SER B 2 44 ? 51.709 26.008 27.928 1.00 31.35 ? 268 SER B CB 1 ATOM 1747 O OG . SER B 2 44 ? 52.738 25.086 28.285 1.00 30.19 ? 268 SER B OG 1 ATOM 1748 N N . SER B 2 45 ? 48.542 26.322 26.791 1.00 26.96 ? 269 SER B N 1 ATOM 1749 C CA . SER B 2 45 ? 47.569 27.386 26.579 1.00 27.40 ? 269 SER B CA 1 ATOM 1750 C C . SER B 2 45 ? 46.543 26.851 25.564 1.00 31.20 ? 269 SER B C 1 ATOM 1751 O O . SER B 2 45 ? 46.949 26.328 24.499 1.00 28.47 ? 269 SER B O 1 ATOM 1752 C CB . SER B 2 45 ? 48.227 28.667 26.036 1.00 21.63 ? 269 SER B CB 1 ATOM 1753 O OG . SER B 2 45 ? 47.224 29.603 25.667 1.00 28.94 ? 269 SER B OG 1 ATOM 1754 N N . SER B 2 46 ? 45.254 26.951 25.905 1.00 27.99 ? 270 SER B N 1 ATOM 1755 C CA . SER B 2 46 ? 44.181 26.687 24.951 1.00 26.99 ? 270 SER B CA 1 ATOM 1756 C C . SER B 2 46 ? 43.158 27.773 25.041 1.00 29.24 ? 270 SER B C 1 ATOM 1757 O O . SER B 2 46 ? 41.952 27.587 24.752 1.00 30.63 ? 270 SER B O 1 ATOM 1758 C CB . SER B 2 46 ? 43.597 25.264 25.167 1.00 33.96 ? 270 SER B CB 1 ATOM 1759 O OG . SER B 2 46 ? 43.153 25.103 26.531 1.00 34.90 ? 270 SER B OG 1 ATOM 1760 N N . ARG B 2 47 ? 43.636 28.955 25.413 1.00 27.44 ? 271 ARG B N 1 ATOM 1761 C CA . ARG B 2 47 ? 42.800 30.132 25.423 1.00 26.83 ? 271 ARG B CA 1 ATOM 1762 C C . ARG B 2 47 ? 43.633 31.278 24.910 1.00 27.92 ? 271 ARG B C 1 ATOM 1763 O O . ARG B 2 47 ? 44.788 31.449 25.299 1.00 26.20 ? 271 ARG B O 1 ATOM 1764 C CB . ARG B 2 47 ? 42.289 30.475 26.846 1.00 26.60 ? 271 ARG B CB 1 ATOM 1765 C CG . ARG B 2 47 ? 41.350 31.665 26.926 1.00 28.06 ? 271 ARG B CG 1 ATOM 1766 C CD . ARG B 2 47 ? 40.725 31.824 28.363 1.00 30.33 ? 271 ARG B CD 1 ATOM 1767 N NE . ARG B 2 47 ? 39.598 32.770 28.329 1.00 33.71 ? 271 ARG B NE 1 ATOM 1768 C CZ . ARG B 2 47 ? 38.999 33.319 29.391 1.00 38.24 ? 271 ARG B CZ 1 ATOM 1769 N NH1 . ARG B 2 47 ? 39.446 33.066 30.605 1.00 35.68 ? 271 ARG B NH1 1 ATOM 1770 N NH2 . ARG B 2 47 ? 37.989 34.176 29.231 1.00 33.31 ? 271 ARG B NH2 1 ATOM 1771 N N . LEU B 2 48 ? 43.048 32.066 24.029 1.00 27.11 ? 272 LEU B N 1 ATOM 1772 C CA . LEU B 2 48 ? 43.789 33.088 23.291 1.00 29.01 ? 272 LEU B CA 1 ATOM 1773 C C . LEU B 2 48 ? 42.800 34.011 22.648 1.00 27.37 ? 272 LEU B C 1 ATOM 1774 O O . LEU B 2 48 ? 41.736 33.565 22.187 1.00 29.15 ? 272 LEU B O 1 ATOM 1775 C CB . LEU B 2 48 ? 44.679 32.407 22.227 1.00 25.79 ? 272 LEU B CB 1 ATOM 1776 C CG . LEU B 2 48 ? 44.048 31.474 21.185 1.00 23.38 ? 272 LEU B CG 1 ATOM 1777 C CD1 . LEU B 2 48 ? 45.086 31.380 20.052 1.00 25.00 ? 272 LEU B CD1 1 ATOM 1778 C CD2 . LEU B 2 48 ? 43.712 30.059 21.707 1.00 27.84 ? 272 LEU B CD2 1 ATOM 1779 N N . SER B 2 49 ? 43.190 35.269 22.565 1.00 24.19 ? 273 SER B N 1 ATOM 1780 C CA . SER B 2 49 ? 42.473 36.347 21.880 1.00 27.09 ? 273 SER B CA 1 ATOM 1781 C C . SER B 2 49 ? 43.432 36.958 20.871 1.00 28.28 ? 273 SER B C 1 ATOM 1782 O O . SER B 2 49 ? 44.630 37.190 21.188 1.00 24.41 ? 273 SER B O 1 ATOM 1783 C CB . SER B 2 49 ? 42.036 37.429 22.863 1.00 25.77 ? 273 SER B CB 1 ATOM 1784 O OG . SER B 2 49 ? 40.980 36.910 23.689 1.00 30.41 ? 273 SER B OG 1 ATOM 1785 N N . PHE B 2 50 ? 42.935 37.263 19.669 1.00 26.68 ? 274 PHE B N 1 ATOM 1786 C CA . PHE B 2 50 ? 43.835 37.715 18.636 1.00 24.83 ? 274 PHE B CA 1 ATOM 1787 C C . PHE B 2 50 ? 43.082 38.333 17.439 1.00 26.64 ? 274 PHE B C 1 ATOM 1788 O O . PHE B 2 50 ? 41.898 38.024 17.173 1.00 23.74 ? 274 PHE B O 1 ATOM 1789 C CB . PHE B 2 50 ? 44.671 36.527 18.162 1.00 20.19 ? 274 PHE B CB 1 ATOM 1790 C CG . PHE B 2 50 ? 43.844 35.393 17.647 1.00 23.59 ? 274 PHE B CG 1 ATOM 1791 C CD1 . PHE B 2 50 ? 43.272 34.501 18.534 1.00 24.43 ? 274 PHE B CD1 1 ATOM 1792 C CD2 . PHE B 2 50 ? 43.688 35.188 16.238 1.00 21.89 ? 274 PHE B CD2 1 ATOM 1793 C CE1 . PHE B 2 50 ? 42.508 33.410 18.063 1.00 27.05 ? 274 PHE B CE1 1 ATOM 1794 C CE2 . PHE B 2 50 ? 42.967 34.105 15.749 1.00 21.22 ? 274 PHE B CE2 1 ATOM 1795 C CZ . PHE B 2 50 ? 42.350 33.230 16.661 1.00 23.65 ? 274 PHE B CZ 1 ATOM 1796 N N . SER B 2 51 ? 43.769 39.235 16.743 1.00 23.65 ? 275 SER B N 1 ATOM 1797 C CA . SER B 2 51 ? 43.204 39.812 15.522 1.00 25.36 ? 275 SER B CA 1 ATOM 1798 C C . SER B 2 51 ? 43.256 38.798 14.398 1.00 25.97 ? 275 SER B C 1 ATOM 1799 O O . SER B 2 51 ? 44.220 37.990 14.289 1.00 21.84 ? 275 SER B O 1 ATOM 1800 C CB . SER B 2 51 ? 43.926 41.100 15.134 1.00 22.77 ? 275 SER B CB 1 ATOM 1801 O OG . SER B 2 51 ? 45.349 40.869 14.982 1.00 23.85 ? 275 SER B OG 1 ATOM 1802 N N . SER B 2 52 ? 42.166 38.732 13.599 1.00 21.69 ? 276 SER B N 1 ATOM 1803 C CA . SER B 2 52 ? 42.080 37.728 12.606 1.00 21.86 ? 276 SER B CA 1 ATOM 1804 C C . SER B 2 52 ? 41.092 38.060 11.423 1.00 22.99 ? 276 SER B C 1 ATOM 1805 O O . SER B 2 52 ? 40.851 39.252 11.135 1.00 24.19 ? 276 SER B O 1 ATOM 1806 C CB . SER B 2 52 ? 41.666 36.468 13.342 1.00 22.82 ? 276 SER B CB 1 ATOM 1807 O OG . SER B 2 52 ? 41.682 35.319 12.497 1.00 25.10 ? 276 SER B OG 1 ATOM 1808 N N . TYR B 2 53 ? 40.634 36.989 10.764 1.00 25.76 ? 277 TYR B N 1 ATOM 1809 C CA . TYR B 2 53 ? 39.927 37.098 9.443 1.00 28.11 ? 277 TYR B CA 1 ATOM 1810 C C . TYR B 2 53 ? 39.011 35.942 9.314 1.00 25.44 ? 277 TYR B C 1 ATOM 1811 O O . TYR B 2 53 ? 39.259 34.880 9.882 1.00 26.92 ? 277 TYR B O 1 ATOM 1812 C CB . TYR B 2 53 ? 40.923 36.983 8.244 1.00 24.48 ? 277 TYR B CB 1 ATOM 1813 C CG . TYR B 2 53 ? 41.974 38.073 8.343 1.00 25.78 ? 277 TYR B CG 1 ATOM 1814 C CD1 . TYR B 2 53 ? 43.116 37.900 9.192 1.00 24.70 ? 277 TYR B CD1 1 ATOM 1815 C CD2 . TYR B 2 53 ? 41.829 39.282 7.656 1.00 21.43 ? 277 TYR B CD2 1 ATOM 1816 C CE1 . TYR B 2 53 ? 44.095 38.906 9.272 1.00 19.48 ? 277 TYR B CE1 1 ATOM 1817 C CE2 . TYR B 2 53 ? 42.818 40.297 7.727 1.00 21.46 ? 277 TYR B CE2 1 ATOM 1818 C CZ . TYR B 2 53 ? 43.961 40.079 8.548 1.00 23.54 ? 277 TYR B CZ 1 ATOM 1819 O OH . TYR B 2 53 ? 44.923 41.133 8.682 1.00 20.89 ? 277 TYR B OH 1 ATOM 1820 N N . PRO B 2 54 ? 38.024 36.035 8.383 1.00 27.54 ? 278 PRO B N 1 ATOM 1821 C CA . PRO B 2 54 ? 37.153 34.859 8.191 1.00 24.32 ? 278 PRO B CA 1 ATOM 1822 C C . PRO B 2 54 ? 37.916 33.635 7.693 1.00 25.44 ? 278 PRO B C 1 ATOM 1823 O O . PRO B 2 54 ? 38.655 33.716 6.703 1.00 25.49 ? 278 PRO B O 1 ATOM 1824 C CB . PRO B 2 54 ? 36.128 35.353 7.093 1.00 26.25 ? 278 PRO B CB 1 ATOM 1825 C CG . PRO B 2 54 ? 36.131 36.871 7.280 1.00 22.02 ? 278 PRO B CG 1 ATOM 1826 C CD . PRO B 2 54 ? 37.609 37.208 7.591 1.00 27.55 ? 278 PRO B CD 1 ATOM 1827 N N . GLY B 2 55 ? 37.645 32.484 8.293 1.00 23.49 ? 279 GLY B N 1 ATOM 1828 C CA . GLY B 2 55 ? 38.262 31.194 7.950 1.00 25.50 ? 279 GLY B CA 1 ATOM 1829 C C . GLY B 2 55 ? 39.711 30.969 8.393 1.00 26.71 ? 279 GLY B C 1 ATOM 1830 O O . GLY B 2 55 ? 40.254 29.902 8.208 1.00 25.95 ? 279 GLY B O 1 ATOM 1831 N N . PHE B 2 56 ? 40.335 32.003 8.952 1.00 23.01 ? 280 PHE B N 1 ATOM 1832 C CA . PHE B 2 56 ? 41.725 31.858 9.467 1.00 23.19 ? 280 PHE B CA 1 ATOM 1833 C C . PHE B 2 56 ? 41.789 31.244 10.880 1.00 23.10 ? 280 PHE B C 1 ATOM 1834 O O . PHE B 2 56 ? 41.329 31.862 11.812 1.00 28.51 ? 280 PHE B O 1 ATOM 1835 C CB . PHE B 2 56 ? 42.405 33.238 9.557 1.00 21.49 ? 280 PHE B CB 1 ATOM 1836 C CG . PHE B 2 56 ? 42.800 33.858 8.240 1.00 22.92 ? 280 PHE B CG 1 ATOM 1837 C CD1 . PHE B 2 56 ? 42.175 33.531 7.021 1.00 23.50 ? 280 PHE B CD1 1 ATOM 1838 C CD2 . PHE B 2 56 ? 43.864 34.794 8.233 1.00 24.28 ? 280 PHE B CD2 1 ATOM 1839 C CE1 . PHE B 2 56 ? 42.596 34.158 5.834 1.00 25.53 ? 280 PHE B CE1 1 ATOM 1840 C CE2 . PHE B 2 56 ? 44.266 35.434 7.059 1.00 27.60 ? 280 PHE B CE2 1 ATOM 1841 C CZ . PHE B 2 56 ? 43.625 35.111 5.856 1.00 27.81 ? 280 PHE B CZ 1 ATOM 1842 N N . LEU B 2 57 ? 42.325 30.033 11.014 1.00 23.23 ? 281 LEU B N 1 ATOM 1843 C CA . LEU B 2 57 ? 42.535 29.458 12.353 1.00 22.15 ? 281 LEU B CA 1 ATOM 1844 C C . LEU B 2 57 ? 43.908 29.996 12.928 1.00 20.55 ? 281 LEU B C 1 ATOM 1845 O O . LEU B 2 57 ? 44.651 29.223 13.513 1.00 25.07 ? 281 LEU B O 1 ATOM 1846 C CB . LEU B 2 57 ? 42.568 27.948 12.200 1.00 21.11 ? 281 LEU B CB 1 ATOM 1847 C CG . LEU B 2 57 ? 41.242 27.282 11.719 1.00 23.26 ? 281 LEU B CG 1 ATOM 1848 C CD1 . LEU B 2 57 ? 41.350 25.793 11.741 1.00 25.40 ? 281 LEU B CD1 1 ATOM 1849 C CD2 . LEU B 2 57 ? 40.115 27.803 12.586 1.00 24.39 ? 281 LEU B CD2 1 ATOM 1850 N N . GLU B 2 58 ? 44.182 31.292 12.679 1.00 23.39 ? 282 GLU B N 1 ATOM 1851 C CA . GLU B 2 58 ? 45.432 31.969 13.105 1.00 25.62 ? 282 GLU B CA 1 ATOM 1852 C C . GLU B 2 58 ? 45.160 33.457 12.975 1.00 24.48 ? 282 GLU B C 1 ATOM 1853 O O . GLU B 2 58 ? 44.091 33.913 12.387 1.00 24.45 ? 282 GLU B O 1 ATOM 1854 C CB . GLU B 2 58 ? 46.672 31.473 12.304 1.00 20.93 ? 282 GLU B CB 1 ATOM 1855 C CG . GLU B 2 58 ? 46.642 31.830 10.777 1.00 24.09 ? 282 GLU B CG 1 ATOM 1856 C CD . GLU B 2 58 ? 45.623 30.926 9.978 1.00 26.07 ? 282 GLU B CD 1 ATOM 1857 O OE1 . GLU B 2 58 ? 45.551 29.701 10.216 1.00 24.34 ? 282 GLU B OE1 1 ATOM 1858 O OE2 . GLU B 2 58 ? 44.859 31.466 9.164 1.00 24.78 ? 282 GLU B OE2 1 ATOM 1859 N N . SER B 2 59 ? 46.061 34.243 13.573 1.00 21.29 ? 283 SER B N 1 ATOM 1860 C CA . SER B 2 59 ? 46.014 35.709 13.410 1.00 19.46 ? 283 SER B CA 1 ATOM 1861 C C . SER B 2 59 ? 46.427 36.173 12.005 1.00 22.86 ? 283 SER B C 1 ATOM 1862 O O . SER B 2 59 ? 45.825 37.105 11.424 1.00 20.26 ? 283 SER B O 1 ATOM 1863 C CB . SER B 2 59 ? 46.937 36.427 14.439 1.00 19.70 ? 283 SER B CB 1 ATOM 1864 O OG . SER B 2 59 ? 46.799 37.864 14.329 1.00 22.75 ? 283 SER B OG 1 ATOM 1865 N N . LEU B 2 60 ? 47.445 35.503 11.462 1.00 22.81 ? 284 LEU B N 1 ATOM 1866 C CA . LEU B 2 60 ? 48.223 36.023 10.307 1.00 26.82 ? 284 LEU B CA 1 ATOM 1867 C C . LEU B 2 60 ? 49.027 37.311 10.612 1.00 23.95 ? 284 LEU B C 1 ATOM 1868 O O . LEU B 2 60 ? 50.143 37.502 10.119 1.00 20.45 ? 284 LEU B O 1 ATOM 1869 C CB . LEU B 2 60 ? 47.377 36.225 9.025 1.00 26.85 ? 284 LEU B CB 1 ATOM 1870 C CG . LEU B 2 60 ? 48.151 36.860 7.813 1.00 36.92 ? 284 LEU B CG 1 ATOM 1871 C CD1 . LEU B 2 60 ? 48.830 35.749 7.086 1.00 32.39 ? 284 LEU B CD1 1 ATOM 1872 C CD2 . LEU B 2 60 ? 47.250 37.559 6.788 1.00 38.45 ? 284 LEU B CD2 1 ATOM 1873 N N . ASP B 2 61 ? 48.427 38.270 11.296 1.00 23.71 ? 285 ASP B N 1 ATOM 1874 C CA . ASP B 2 61 ? 49.055 39.583 11.412 1.00 19.36 ? 285 ASP B CA 1 ATOM 1875 C C . ASP B 2 61 ? 50.556 39.719 11.786 1.00 21.04 ? 285 ASP B C 1 ATOM 1876 O O . ASP B 2 61 ? 51.309 40.387 11.036 1.00 20.66 ? 285 ASP B O 1 ATOM 1877 C CB . ASP B 2 61 ? 48.165 40.421 12.423 1.00 20.87 ? 285 ASP B CB 1 ATOM 1878 C CG . ASP B 2 61 ? 46.793 40.841 11.768 1.00 22.09 ? 285 ASP B CG 1 ATOM 1879 O OD1 . ASP B 2 61 ? 46.589 40.479 10.577 1.00 22.49 ? 285 ASP B OD1 1 ATOM 1880 O OD2 . ASP B 2 61 ? 46.011 41.472 12.496 1.00 23.98 ? 285 ASP B OD2 1 ATOM 1881 N N . ASP B 2 62 ? 50.986 39.291 12.977 1.00 18.98 ? 286 ASP B N 1 ATOM 1882 C CA . ASP B 2 62 ? 50.212 38.621 14.011 1.00 19.86 ? 286 ASP B CA 1 ATOM 1883 C C . ASP B 2 62 ? 50.130 39.475 15.271 1.00 20.58 ? 286 ASP B C 1 ATOM 1884 O O . ASP B 2 62 ? 51.080 40.245 15.593 1.00 20.90 ? 286 ASP B O 1 ATOM 1885 C CB . ASP B 2 62 ? 50.956 37.360 14.529 1.00 22.86 ? 286 ASP B CB 1 ATOM 1886 C CG . ASP B 2 62 ? 51.039 36.199 13.510 1.00 23.94 ? 286 ASP B CG 1 ATOM 1887 O OD1 . ASP B 2 62 ? 49.980 35.731 13.043 1.00 23.09 ? 286 ASP B OD1 1 ATOM 1888 O OD2 . ASP B 2 62 ? 52.198 35.639 13.252 1.00 24.96 ? 286 ASP B OD2 1 ATOM 1889 N N . PHE B 2 63 ? 49.057 39.227 16.036 1.00 19.71 ? 287 PHE B N 1 ATOM 1890 C CA . PHE B 2 63 ? 48.866 39.814 17.354 1.00 21.60 ? 287 PHE B CA 1 ATOM 1891 C C . PHE B 2 63 ? 48.033 38.866 18.220 1.00 23.47 ? 287 PHE B C 1 ATOM 1892 O O . PHE B 2 63 ? 46.814 38.588 17.978 1.00 23.48 ? 287 PHE B O 1 ATOM 1893 C CB . PHE B 2 63 ? 48.213 41.199 17.260 1.00 24.33 ? 287 PHE B CB 1 ATOM 1894 C CG . PHE B 2 63 ? 47.939 41.868 18.605 1.00 21.43 ? 287 PHE B CG 1 ATOM 1895 C CD1 . PHE B 2 63 ? 46.717 41.614 19.317 1.00 21.38 ? 287 PHE B CD1 1 ATOM 1896 C CD2 . PHE B 2 63 ? 48.812 42.824 19.080 1.00 18.48 ? 287 PHE B CD2 1 ATOM 1897 C CE1 . PHE B 2 63 ? 46.456 42.285 20.530 1.00 24.90 ? 287 PHE B CE1 1 ATOM 1898 C CE2 . PHE B 2 63 ? 48.549 43.485 20.333 1.00 21.85 ? 287 PHE B CE2 1 ATOM 1899 C CZ . PHE B 2 63 ? 47.351 43.263 21.006 1.00 24.83 ? 287 PHE B CZ 1 ATOM 1900 N N . TYR B 2 64 ? 48.706 38.259 19.194 1.00 21.54 ? 288 TYR B N 1 ATOM 1901 C CA . TYR B 2 64 ? 48.079 37.213 19.987 1.00 22.22 ? 288 TYR B CA 1 ATOM 1902 C C . TYR B 2 64 ? 48.269 37.555 21.471 1.00 24.43 ? 288 TYR B C 1 ATOM 1903 O O . TYR B 2 64 ? 49.423 37.851 21.900 1.00 20.50 ? 288 TYR B O 1 ATOM 1904 C CB . TYR B 2 64 ? 48.801 35.883 19.798 1.00 19.04 ? 288 TYR B CB 1 ATOM 1905 C CG . TYR B 2 64 ? 48.561 35.118 18.501 1.00 21.16 ? 288 TYR B CG 1 ATOM 1906 C CD1 . TYR B 2 64 ? 47.475 34.225 18.385 1.00 22.34 ? 288 TYR B CD1 1 ATOM 1907 C CD2 . TYR B 2 64 ? 49.467 35.194 17.442 1.00 21.93 ? 288 TYR B CD2 1 ATOM 1908 C CE1 . TYR B 2 64 ? 47.294 33.489 17.221 1.00 22.56 ? 288 TYR B CE1 1 ATOM 1909 C CE2 . TYR B 2 64 ? 49.315 34.437 16.299 1.00 20.58 ? 288 TYR B CE2 1 ATOM 1910 C CZ . TYR B 2 64 ? 48.220 33.573 16.221 1.00 21.59 ? 288 TYR B CZ 1 ATOM 1911 O OH . TYR B 2 64 ? 48.118 32.844 15.101 1.00 21.52 ? 288 TYR B OH 1 ATOM 1912 N N . LEU B 2 65 ? 47.218 37.295 22.272 1.00 21.24 ? 289 LEU B N 1 ATOM 1913 C CA . LEU B 2 65 ? 47.324 37.338 23.768 1.00 22.55 ? 289 LEU B CA 1 ATOM 1914 C C . LEU B 2 65 ? 47.037 35.876 24.160 1.00 27.12 ? 289 LEU B C 1 ATOM 1915 O O . LEU B 2 65 ? 45.915 35.397 23.945 1.00 25.20 ? 289 LEU B O 1 ATOM 1916 C CB . LEU B 2 65 ? 46.214 38.275 24.286 1.00 21.88 ? 289 LEU B CB 1 ATOM 1917 C CG . LEU B 2 65 ? 46.285 39.728 23.790 1.00 24.83 ? 289 LEU B CG 1 ATOM 1918 C CD1 . LEU B 2 65 ? 45.188 40.556 24.526 1.00 28.59 ? 289 LEU B CD1 1 ATOM 1919 C CD2 . LEU B 2 65 ? 47.706 40.425 24.022 1.00 23.01 ? 289 LEU B CD2 1 ATOM 1920 N N . LEU B 2 66 ? 48.030 35.161 24.690 1.00 21.49 ? 290 LEU B N 1 ATOM 1921 C CA . LEU B 2 66 ? 47.886 33.765 25.009 1.00 23.03 ? 290 LEU B CA 1 ATOM 1922 C C . LEU B 2 66 ? 47.673 33.618 26.536 1.00 22.62 ? 290 LEU B C 1 ATOM 1923 O O . LEU B 2 66 ? 48.280 34.314 27.335 1.00 22.58 ? 290 LEU B O 1 ATOM 1924 C CB . LEU B 2 66 ? 49.096 32.935 24.577 1.00 21.26 ? 290 LEU B CB 1 ATOM 1925 C CG . LEU B 2 66 ? 49.472 33.207 23.088 1.00 25.85 ? 290 LEU B CG 1 ATOM 1926 C CD1 . LEU B 2 66 ? 50.809 32.590 22.730 1.00 20.22 ? 290 LEU B CD1 1 ATOM 1927 C CD2 . LEU B 2 66 ? 48.340 32.678 22.175 1.00 24.17 ? 290 LEU B CD2 1 ATOM 1928 N N . SER B 2 67 ? 46.925 32.593 26.913 1.00 26.53 ? 291 SER B N 1 ATOM 1929 C CA . SER B 2 67 ? 46.615 32.332 28.354 1.00 26.18 ? 291 SER B CA 1 ATOM 1930 C C . SER B 2 67 ? 47.905 31.851 29.075 1.00 25.33 ? 291 SER B C 1 ATOM 1931 O O . SER B 2 67 ? 47.924 31.837 30.315 1.00 26.22 ? 291 SER B O 1 ATOM 1932 C CB . SER B 2 67 ? 45.593 31.210 28.442 1.00 24.60 ? 291 SER B CB 1 ATOM 1933 O OG . SER B 2 67 ? 46.197 29.984 28.010 1.00 29.07 ? 291 SER B OG 1 ATOM 1934 N N . SER B 2 68 ? 48.961 31.474 28.332 1.00 23.62 ? 292 SER B N 1 ATOM 1935 C CA . SER B 2 68 ? 50.256 31.122 28.988 1.00 22.41 ? 292 SER B CA 1 ATOM 1936 C C . SER B 2 68 ? 50.990 32.383 29.512 1.00 22.33 ? 292 SER B C 1 ATOM 1937 O O . SER B 2 68 ? 52.078 32.303 30.089 1.00 21.18 ? 292 SER B O 1 ATOM 1938 C CB . SER B 2 68 ? 51.187 30.421 28.001 1.00 22.04 ? 292 SER B CB 1 ATOM 1939 O OG . SER B 2 68 ? 51.210 31.194 26.770 1.00 24.44 ? 292 SER B OG 1 ATOM 1940 N N . GLY B 2 69 ? 50.391 33.545 29.280 1.00 21.23 ? 293 GLY B N 1 ATOM 1941 C CA . GLY B 2 69 ? 51.041 34.862 29.626 1.00 26.43 ? 293 GLY B CA 1 ATOM 1942 C C . GLY B 2 69 ? 52.026 35.334 28.525 1.00 23.68 ? 293 GLY B C 1 ATOM 1943 O O . GLY B 2 69 ? 52.645 36.411 28.646 1.00 23.53 ? 293 GLY B O 1 ATOM 1944 N N . LEU B 2 70 ? 52.214 34.570 27.450 1.00 21.98 ? 294 LEU B N 1 ATOM 1945 C CA . LEU B 2 70 ? 52.993 35.096 26.305 1.00 21.51 ? 294 LEU B CA 1 ATOM 1946 C C . LEU B 2 70 ? 52.074 35.977 25.431 1.00 22.73 ? 294 LEU B C 1 ATOM 1947 O O . LEU B 2 70 ? 50.884 35.704 25.285 1.00 25.02 ? 294 LEU B O 1 ATOM 1948 C CB . LEU B 2 70 ? 53.439 33.979 25.422 1.00 22.02 ? 294 LEU B CB 1 ATOM 1949 C CG . LEU B 2 70 ? 54.278 32.834 25.996 1.00 26.22 ? 294 LEU B CG 1 ATOM 1950 C CD1 . LEU B 2 70 ? 54.938 31.954 24.983 1.00 26.64 ? 294 LEU B CD1 1 ATOM 1951 C CD2 . LEU B 2 70 ? 55.307 33.369 26.965 1.00 26.85 ? 294 LEU B CD2 1 ATOM 1952 N N . VAL B 2 71 ? 52.671 36.979 24.860 1.00 21.25 ? 295 VAL B N 1 ATOM 1953 C CA . VAL B 2 71 ? 52.131 37.838 23.791 1.00 23.37 ? 295 VAL B CA 1 ATOM 1954 C C . VAL B 2 71 ? 53.006 37.587 22.579 1.00 23.89 ? 295 VAL B C 1 ATOM 1955 O O . VAL B 2 71 ? 54.261 37.476 22.705 1.00 20.27 ? 295 VAL B O 1 ATOM 1956 C CB . VAL B 2 71 ? 52.223 39.339 24.173 1.00 23.58 ? 295 VAL B CB 1 ATOM 1957 C CG1 . VAL B 2 71 ? 51.830 40.272 22.998 1.00 21.50 ? 295 VAL B CG1 1 ATOM 1958 C CG2 . VAL B 2 71 ? 51.254 39.557 25.319 1.00 24.32 ? 295 VAL B CG2 1 ATOM 1959 N N . LEU B 2 72 ? 52.369 37.444 21.415 1.00 21.66 ? 296 LEU B N 1 ATOM 1960 C CA A LEU B 2 72 ? 53.124 37.225 20.170 0.50 22.00 ? 296 LEU B CA 1 ATOM 1961 C CA B LEU B 2 72 ? 53.120 37.228 20.164 0.50 24.12 ? 296 LEU B CA 1 ATOM 1962 C C . LEU B 2 72 ? 52.843 38.361 19.199 1.00 21.56 ? 296 LEU B C 1 ATOM 1963 O O . LEU B 2 72 ? 51.671 38.605 18.886 1.00 23.65 ? 296 LEU B O 1 ATOM 1964 C CB A LEU B 2 72 ? 52.744 35.872 19.542 0.50 18.05 ? 296 LEU B CB 1 ATOM 1965 C CB B LEU B 2 72 ? 52.720 35.909 19.484 0.50 22.92 ? 296 LEU B CB 1 ATOM 1966 C CG A LEU B 2 72 ? 53.528 35.241 18.388 0.50 16.03 ? 296 LEU B CG 1 ATOM 1967 C CG B LEU B 2 72 ? 53.065 34.533 20.047 0.50 24.16 ? 296 LEU B CG 1 ATOM 1968 C CD1 A LEU B 2 72 ? 54.996 34.977 18.848 0.50 15.84 ? 296 LEU B CD1 1 ATOM 1969 C CD1 B LEU B 2 72 ? 52.458 33.462 19.138 0.50 23.68 ? 296 LEU B CD1 1 ATOM 1970 C CD2 A LEU B 2 72 ? 52.817 33.970 17.922 0.50 15.64 ? 296 LEU B CD2 1 ATOM 1971 C CD2 B LEU B 2 72 ? 54.579 34.365 20.176 0.50 25.66 ? 296 LEU B CD2 1 ATOM 1972 N N . LEU B 2 73 ? 53.907 39.061 18.764 1.00 20.55 ? 297 LEU B N 1 ATOM 1973 C CA . LEU B 2 73 ? 53.834 40.002 17.675 1.00 20.42 ? 297 LEU B CA 1 ATOM 1974 C C . LEU B 2 73 ? 54.687 39.454 16.520 1.00 24.17 ? 297 LEU B C 1 ATOM 1975 O O . LEU B 2 73 ? 55.674 38.714 16.759 1.00 23.24 ? 297 LEU B O 1 ATOM 1976 C CB . LEU B 2 73 ? 54.384 41.382 18.061 1.00 18.69 ? 297 LEU B CB 1 ATOM 1977 C CG . LEU B 2 73 ? 53.920 41.982 19.436 1.00 18.55 ? 297 LEU B CG 1 ATOM 1978 C CD1 . LEU B 2 73 ? 54.617 43.319 19.698 1.00 20.90 ? 297 LEU B CD1 1 ATOM 1979 C CD2 . LEU B 2 73 ? 52.379 42.129 19.292 1.00 19.57 ? 297 LEU B CD2 1 ATOM 1980 N N . GLN B 2 74 ? 54.392 39.837 15.278 1.00 20.36 ? 298 GLN B N 1 ATOM 1981 C CA . GLN B 2 74 ? 55.275 39.396 14.219 1.00 19.58 ? 298 GLN B CA 1 ATOM 1982 C C . GLN B 2 74 ? 55.288 40.381 13.068 1.00 21.94 ? 298 GLN B C 1 ATOM 1983 O O . GLN B 2 74 ? 54.252 40.978 12.763 1.00 20.55 ? 298 GLN B O 1 ATOM 1984 C CB . GLN B 2 74 ? 54.730 38.020 13.732 1.00 19.79 ? 298 GLN B CB 1 ATOM 1985 C CG . GLN B 2 74 ? 55.372 37.523 12.391 1.00 17.59 ? 298 GLN B CG 1 ATOM 1986 C CD . GLN B 2 74 ? 54.487 37.903 11.185 1.00 21.14 ? 298 GLN B CD 1 ATOM 1987 O OE1 . GLN B 2 74 ? 54.868 38.680 10.375 1.00 22.57 ? 298 GLN B OE1 1 ATOM 1988 N NE2 . GLN B 2 74 ? 53.237 37.427 11.176 1.00 20.53 ? 298 GLN B NE2 1 ATOM 1989 N N . THR B 2 75 ? 56.434 40.578 12.410 1.00 20.38 ? 299 THR B N 1 ATOM 1990 C CA . THR B 2 75 ? 56.488 41.313 11.116 1.00 19.66 ? 299 THR B CA 1 ATOM 1991 C C . THR B 2 75 ? 57.302 40.450 10.107 1.00 22.28 ? 299 THR B C 1 ATOM 1992 O O . THR B 2 75 ? 58.195 39.690 10.512 1.00 19.38 ? 299 THR B O 1 ATOM 1993 C CB . THR B 2 75 ? 57.071 42.775 11.182 1.00 19.79 ? 299 THR B CB 1 ATOM 1994 O OG1 . THR B 2 75 ? 58.509 42.759 11.270 1.00 22.02 ? 299 THR B OG1 1 ATOM 1995 C CG2 . THR B 2 75 ? 56.421 43.666 12.284 1.00 17.55 ? 299 THR B CG2 1 ATOM 1996 N N . THR B 2 76 ? 57.003 40.567 8.808 1.00 21.00 ? 300 THR B N 1 ATOM 1997 C CA . THR B 2 76 ? 57.421 39.607 7.786 1.00 22.11 ? 300 THR B CA 1 ATOM 1998 C C . THR B 2 76 ? 58.767 40.076 7.232 1.00 23.67 ? 300 THR B C 1 ATOM 1999 O O . THR B 2 76 ? 58.973 41.263 7.080 1.00 21.88 ? 300 THR B O 1 ATOM 2000 C CB . THR B 2 76 ? 56.333 39.478 6.674 1.00 24.03 ? 300 THR B CB 1 ATOM 2001 O OG1 . THR B 2 76 ? 55.149 38.927 7.268 1.00 27.38 ? 300 THR B OG1 1 ATOM 2002 C CG2 . THR B 2 76 ? 56.744 38.490 5.610 1.00 23.72 ? 300 THR B CG2 1 ATOM 2003 N N . ASN B 2 77 ? 59.728 39.164 7.028 1.00 19.56 ? 301 ASN B N 1 ATOM 2004 C CA . ASN B 2 77 ? 61.001 39.567 6.455 1.00 24.38 ? 301 ASN B CA 1 ATOM 2005 C C . ASN B 2 77 ? 60.882 39.204 4.913 1.00 28.20 ? 301 ASN B C 1 ATOM 2006 O O . ASN B 2 77 ? 59.867 38.698 4.499 1.00 37.86 ? 301 ASN B O 1 ATOM 2007 C CB . ASN B 2 77 ? 62.163 38.867 7.253 1.00 23.53 ? 301 ASN B CB 1 ATOM 2008 C CG . ASN B 2 77 ? 62.337 39.458 8.609 1.00 25.03 ? 301 ASN B CG 1 ATOM 2009 O OD1 . ASN B 2 77 ? 62.142 40.670 8.781 1.00 24.45 ? 301 ASN B OD1 1 ATOM 2010 N ND2 . ASN B 2 77 ? 62.728 38.683 9.569 1.00 22.25 ? 301 ASN B ND2 1 ATOM 2011 N N . SER B 2 78 ? 61.770 39.614 4.053 1.00 30.89 ? 302 SER B N 1 ATOM 2012 C CA . SER B 2 78 ? 61.750 39.011 2.718 1.00 33.30 ? 302 SER B CA 1 ATOM 2013 C C . SER B 2 78 ? 62.928 38.155 2.632 1.00 31.06 ? 302 SER B C 1 ATOM 2014 O O . SER B 2 78 ? 63.878 38.355 3.369 1.00 31.38 ? 302 SER B O 1 ATOM 2015 C CB . SER B 2 78 ? 61.861 40.066 1.658 1.00 41.37 ? 302 SER B CB 1 ATOM 2016 O OG . SER B 2 78 ? 60.822 40.982 1.854 1.00 45.00 ? 302 SER B OG 1 ATOM 2017 N N . VAL B 2 79 ? 62.899 37.155 1.768 1.00 32.53 ? 303 VAL B N 1 ATOM 2018 C CA . VAL B 2 79 ? 64.115 36.403 1.547 1.00 29.42 ? 303 VAL B CA 1 ATOM 2019 C C . VAL B 2 79 ? 64.494 36.681 0.086 1.00 37.37 ? 303 VAL B C 1 ATOM 2020 O O . VAL B 2 79 ? 63.735 36.375 -0.825 1.00 35.62 ? 303 VAL B O 1 ATOM 2021 C CB . VAL B 2 79 ? 63.923 34.894 1.869 1.00 29.87 ? 303 VAL B CB 1 ATOM 2022 C CG1 . VAL B 2 79 ? 65.127 34.086 1.321 1.00 28.77 ? 303 VAL B CG1 1 ATOM 2023 C CG2 . VAL B 2 79 ? 63.771 34.702 3.406 1.00 24.43 ? 303 VAL B CG2 1 ATOM 2024 N N . TYR B 2 80 ? 65.655 37.277 -0.138 1.00 34.23 ? 304 TYR B N 1 ATOM 2025 C CA . TYR B 2 80 ? 66.073 37.595 -1.520 1.00 42.17 ? 304 TYR B CA 1 ATOM 2026 C C . TYR B 2 80 ? 67.134 36.647 -2.052 1.00 40.39 ? 304 TYR B C 1 ATOM 2027 O O . TYR B 2 80 ? 67.872 36.977 -2.929 1.00 54.48 ? 304 TYR B O 1 ATOM 2028 C CB . TYR B 2 80 ? 66.634 38.999 -1.562 1.00 38.90 ? 304 TYR B CB 1 ATOM 2029 C CG . TYR B 2 80 ? 65.630 40.007 -1.196 1.00 41.21 ? 304 TYR B CG 1 ATOM 2030 C CD1 . TYR B 2 80 ? 64.610 40.374 -2.097 1.00 45.02 ? 304 TYR B CD1 1 ATOM 2031 C CD2 . TYR B 2 80 ? 65.660 40.628 0.074 1.00 49.12 ? 304 TYR B CD2 1 ATOM 2032 C CE1 . TYR B 2 80 ? 63.663 41.347 -1.763 1.00 50.28 ? 304 TYR B CE1 1 ATOM 2033 C CE2 . TYR B 2 80 ? 64.726 41.624 0.408 1.00 48.17 ? 304 TYR B CE2 1 ATOM 2034 C CZ . TYR B 2 80 ? 63.736 41.964 -0.507 1.00 51.43 ? 304 TYR B CZ 1 ATOM 2035 O OH . TYR B 2 80 ? 62.830 42.920 -0.180 1.00 51.62 ? 304 TYR B OH 1 ATOM 2036 N N . ASN B 2 81 ? 67.212 35.472 -1.499 1.00 41.78 ? 305 ASN B N 1 ATOM 2037 C CA . ASN B 2 81 ? 68.205 34.534 -1.895 1.00 43.29 ? 305 ASN B CA 1 ATOM 2038 C C . ASN B 2 81 ? 67.414 33.392 -2.566 1.00 42.39 ? 305 ASN B C 1 ATOM 2039 O O . ASN B 2 81 ? 66.633 32.635 -1.946 1.00 37.36 ? 305 ASN B O 1 ATOM 2040 C CB . ASN B 2 81 ? 69.063 34.180 -0.700 1.00 41.88 ? 305 ASN B CB 1 ATOM 2041 C CG . ASN B 2 81 ? 70.072 33.086 -0.989 1.00 43.50 ? 305 ASN B CG 1 ATOM 2042 O OD1 . ASN B 2 81 ? 69.923 32.311 -1.922 1.00 41.77 ? 305 ASN B OD1 1 ATOM 2043 N ND2 . ASN B 2 81 ? 71.086 33.024 -0.176 1.00 37.06 ? 305 ASN B ND2 1 ATOM 2044 N N . LYS B 2 82 ? 67.498 33.388 -3.895 1.00 44.25 ? 306 LYS B N 1 ATOM 2045 C CA . LYS B 2 82 ? 66.741 32.437 -4.718 1.00 44.71 ? 306 LYS B CA 1 ATOM 2046 C C . LYS B 2 82 ? 67.166 30.976 -4.545 1.00 39.39 ? 306 LYS B C 1 ATOM 2047 O O . LYS B 2 82 ? 66.326 30.095 -4.553 1.00 52.02 ? 306 LYS B O 1 ATOM 2048 C CB . LYS B 2 82 ? 66.732 32.893 -6.182 1.00 55.38 ? 306 LYS B CB 1 ATOM 2049 C CG . LYS B 2 82 ? 65.628 33.906 -6.466 1.00 56.38 ? 306 LYS B CG 1 ATOM 2050 C CD . LYS B 2 82 ? 66.138 35.327 -6.227 1.00 72.72 ? 306 LYS B CD 1 ATOM 2051 C CE . LYS B 2 82 ? 65.013 36.274 -5.821 1.00 76.00 ? 306 LYS B CE 1 ATOM 2052 N NZ . LYS B 2 82 ? 65.044 37.483 -6.688 1.00 67.87 ? 306 LYS B NZ 1 ATOM 2053 N N . THR B 2 83 ? 68.442 30.735 -4.348 1.00 36.10 ? 307 THR B N 1 ATOM 2054 C CA . THR B 2 83 ? 68.958 29.409 -4.015 1.00 46.00 ? 307 THR B CA 1 ATOM 2055 C C . THR B 2 83 ? 68.361 28.904 -2.713 1.00 48.34 ? 307 THR B C 1 ATOM 2056 O O . THR B 2 83 ? 67.964 27.727 -2.608 1.00 43.47 ? 307 THR B O 1 ATOM 2057 C CB . THR B 2 83 ? 70.474 29.473 -3.821 1.00 45.39 ? 307 THR B CB 1 ATOM 2058 O OG1 . THR B 2 83 ? 71.040 29.969 -5.020 1.00 55.69 ? 307 THR B OG1 1 ATOM 2059 C CG2 . THR B 2 83 ? 71.109 28.081 -3.521 1.00 45.87 ? 307 THR B CG2 1 ATOM 2060 N N . LEU B 2 84 ? 68.314 29.796 -1.706 1.00 38.21 ? 308 LEU B N 1 ATOM 2061 C CA . LEU B 2 84 ? 67.708 29.408 -0.458 1.00 35.45 ? 308 LEU B CA 1 ATOM 2062 C C . LEU B 2 84 ? 66.237 29.044 -0.644 1.00 31.53 ? 308 LEU B C 1 ATOM 2063 O O . LEU B 2 84 ? 65.790 28.016 -0.121 1.00 36.06 ? 308 LEU B O 1 ATOM 2064 C CB . LEU B 2 84 ? 67.923 30.504 0.633 1.00 37.57 ? 308 LEU B CB 1 ATOM 2065 C CG . LEU B 2 84 ? 67.555 30.065 2.026 1.00 30.81 ? 308 LEU B CG 1 ATOM 2066 C CD1 . LEU B 2 84 ? 68.369 28.810 2.525 1.00 30.59 ? 308 LEU B CD1 1 ATOM 2067 C CD2 . LEU B 2 84 ? 67.765 31.283 2.903 1.00 29.98 ? 308 LEU B CD2 1 ATOM 2068 N N . LEU B 2 85 ? 65.480 29.849 -1.383 1.00 34.08 ? 309 LEU B N 1 ATOM 2069 C CA . LEU B 2 85 ? 64.073 29.576 -1.571 1.00 35.11 ? 309 LEU B CA 1 ATOM 2070 C C . LEU B 2 85 ? 63.839 28.219 -2.296 1.00 40.93 ? 309 LEU B C 1 ATOM 2071 O O . LEU B 2 85 ? 62.796 27.617 -2.123 1.00 35.22 ? 309 LEU B O 1 ATOM 2072 C CB . LEU B 2 85 ? 63.341 30.729 -2.277 1.00 39.02 ? 309 LEU B CB 1 ATOM 2073 C CG . LEU B 2 85 ? 63.303 31.984 -1.392 1.00 35.32 ? 309 LEU B CG 1 ATOM 2074 C CD1 . LEU B 2 85 ? 63.110 33.198 -2.308 1.00 36.21 ? 309 LEU B CD1 1 ATOM 2075 C CD2 . LEU B 2 85 ? 62.189 31.789 -0.348 1.00 32.43 ? 309 LEU B CD2 1 ATOM 2076 N N . GLN B 2 86 ? 64.850 27.720 -3.000 1.00 41.14 ? 310 GLN B N 1 ATOM 2077 C CA . GLN B 2 86 ? 64.765 26.393 -3.664 1.00 46.95 ? 310 GLN B CA 1 ATOM 2078 C C . GLN B 2 86 ? 64.643 25.254 -2.685 1.00 42.68 ? 310 GLN B C 1 ATOM 2079 O O . GLN B 2 86 ? 64.256 24.167 -3.088 1.00 40.08 ? 310 GLN B O 1 ATOM 2080 C CB . GLN B 2 86 ? 65.998 26.116 -4.576 1.00 48.25 ? 310 GLN B CB 1 ATOM 2081 C CG . GLN B 2 86 ? 66.072 26.999 -5.803 1.00 52.37 ? 310 GLN B CG 1 ATOM 2082 C CD . GLN B 2 86 ? 64.681 27.508 -6.185 1.00 61.47 ? 310 GLN B CD 1 ATOM 2083 O OE1 . GLN B 2 86 ? 63.824 26.730 -6.624 1.00 70.06 ? 310 GLN B OE1 1 ATOM 2084 N NE2 . GLN B 2 86 ? 64.431 28.815 -5.966 1.00 64.14 ? 310 GLN B NE2 1 ATOM 2085 N N . HIS B 2 87 ? 65.043 25.478 -1.420 1.00 37.81 ? 311 HIS B N 1 ATOM 2086 C CA . HIS B 2 87 ? 64.927 24.450 -0.429 1.00 35.87 ? 311 HIS B CA 1 ATOM 2087 C C . HIS B 2 87 ? 63.525 24.235 0.118 1.00 31.63 ? 311 HIS B C 1 ATOM 2088 O O . HIS B 2 87 ? 63.292 23.285 0.883 1.00 34.65 ? 311 HIS B O 1 ATOM 2089 C CB . HIS B 2 87 ? 65.899 24.693 0.688 1.00 37.46 ? 311 HIS B CB 1 ATOM 2090 C CG . HIS B 2 87 ? 67.326 24.580 0.271 1.00 45.53 ? 311 HIS B CG 1 ATOM 2091 N ND1 . HIS B 2 87 ? 68.103 23.545 0.642 1.00 54.99 ? 311 HIS B ND1 1 ATOM 2092 C CD2 . HIS B 2 87 ? 68.120 25.410 -0.531 1.00 43.12 ? 311 HIS B CD2 1 ATOM 2093 C CE1 . HIS B 2 87 ? 69.341 23.711 0.117 1.00 52.34 ? 311 HIS B CE1 1 ATOM 2094 N NE2 . HIS B 2 87 ? 69.336 24.849 -0.612 1.00 52.05 ? 311 HIS B NE2 1 ATOM 2095 N N . VAL B 2 88 ? 62.562 25.041 -0.290 1.00 25.79 ? 312 VAL B N 1 ATOM 2096 C CA . VAL B 2 88 ? 61.227 24.896 0.237 1.00 25.10 ? 312 VAL B CA 1 ATOM 2097 C C . VAL B 2 88 ? 60.538 23.683 -0.343 1.00 30.94 ? 312 VAL B C 1 ATOM 2098 O O . VAL B 2 88 ? 60.529 23.578 -1.555 1.00 29.72 ? 312 VAL B O 1 ATOM 2099 C CB . VAL B 2 88 ? 60.386 26.168 -0.089 1.00 26.96 ? 312 VAL B CB 1 ATOM 2100 C CG1 . VAL B 2 88 ? 58.922 25.885 0.195 1.00 24.92 ? 312 VAL B CG1 1 ATOM 2101 C CG2 . VAL B 2 88 ? 60.928 27.378 0.711 1.00 28.29 ? 312 VAL B CG2 1 ATOM 2102 N N . VAL B 2 89 ? 59.908 22.820 0.470 1.00 27.14 ? 313 VAL B N 1 ATOM 2103 C CA . VAL B 2 89 ? 59.289 21.596 -0.037 1.00 29.46 ? 313 VAL B CA 1 ATOM 2104 C C . VAL B 2 89 ? 57.977 21.448 0.708 1.00 29.79 ? 313 VAL B C 1 ATOM 2105 O O . VAL B 2 89 ? 57.833 22.011 1.776 1.00 30.02 ? 313 VAL B O 1 ATOM 2106 C CB . VAL B 2 89 ? 60.179 20.327 0.213 1.00 29.28 ? 313 VAL B CB 1 ATOM 2107 C CG1 . VAL B 2 89 ? 61.412 20.395 -0.653 1.00 29.30 ? 313 VAL B CG1 1 ATOM 2108 C CG2 . VAL B 2 89 ? 60.577 20.200 1.699 1.00 29.59 ? 313 VAL B CG2 1 ATOM 2109 N N . PRO B 2 90 ? 57.023 20.687 0.166 1.00 31.00 ? 314 PRO B N 1 ATOM 2110 C CA . PRO B 2 90 ? 55.735 20.550 0.906 1.00 27.22 ? 314 PRO B CA 1 ATOM 2111 C C . PRO B 2 90 ? 55.817 19.609 2.090 1.00 29.31 ? 314 PRO B C 1 ATOM 2112 O O . PRO B 2 90 ? 54.881 19.551 2.877 1.00 32.80 ? 314 PRO B O 1 ATOM 2113 C CB . PRO B 2 90 ? 54.767 20.003 -0.145 1.00 28.74 ? 314 PRO B CB 1 ATOM 2114 C CG . PRO B 2 90 ? 55.636 19.543 -1.304 1.00 30.14 ? 314 PRO B CG 1 ATOM 2115 C CD . PRO B 2 90 ? 56.939 20.303 -1.269 1.00 31.20 ? 314 PRO B CD 1 ATOM 2116 N N . GLN B 2 91 ? 56.927 18.878 2.222 1.00 27.77 ? 315 GLN B N 1 ATOM 2117 C CA . GLN B 2 91 ? 57.134 17.980 3.374 1.00 30.55 ? 315 GLN B CA 1 ATOM 2118 C C . GLN B 2 91 ? 57.587 18.769 4.624 1.00 27.60 ? 315 GLN B C 1 ATOM 2119 O O . GLN B 2 91 ? 58.707 18.610 5.086 1.00 28.15 ? 315 GLN B O 1 ATOM 2120 C CB . GLN B 2 91 ? 58.160 16.858 3.043 1.00 31.31 ? 315 GLN B CB 1 ATOM 2121 C CG . GLN B 2 91 ? 57.573 15.876 1.984 1.00 35.02 ? 315 GLN B CG 1 ATOM 2122 C CD . GLN B 2 91 ? 57.624 16.468 0.578 1.00 40.30 ? 315 GLN B CD 1 ATOM 2123 O OE1 . GLN B 2 91 ? 58.544 17.218 0.249 1.00 33.85 ? 315 GLN B OE1 1 ATOM 2124 N NE2 . GLN B 2 91 ? 56.575 16.221 -0.218 1.00 49.04 ? 315 GLN B NE2 1 ATOM 2125 N N . SER B 2 92 ? 56.699 19.583 5.163 1.00 27.50 ? 316 SER B N 1 ATOM 2126 C CA . SER B 2 92 ? 57.086 20.475 6.287 1.00 26.53 ? 316 SER B CA 1 ATOM 2127 C C . SER B 2 92 ? 55.729 21.056 6.760 1.00 25.88 ? 316 SER B C 1 ATOM 2128 O O . SER B 2 92 ? 54.716 20.892 6.060 1.00 27.52 ? 316 SER B O 1 ATOM 2129 C CB . SER B 2 92 ? 58.032 21.576 5.761 1.00 27.89 ? 316 SER B CB 1 ATOM 2130 O OG . SER B 2 92 ? 57.449 22.411 4.743 1.00 27.46 ? 316 SER B OG 1 ATOM 2131 N N . LEU B 2 93 ? 55.691 21.685 7.964 1.00 23.32 ? 317 LEU B N 1 ATOM 2132 C CA . LEU B 2 93 ? 54.455 22.217 8.467 1.00 23.82 ? 317 LEU B CA 1 ATOM 2133 C C . LEU B 2 93 ? 54.450 23.720 8.022 1.00 22.70 ? 317 LEU B C 1 ATOM 2134 O O . LEU B 2 93 ? 55.475 24.367 8.084 1.00 22.55 ? 317 LEU B O 1 ATOM 2135 C CB . LEU B 2 93 ? 54.402 22.177 10.010 1.00 23.39 ? 317 LEU B CB 1 ATOM 2136 C CG . LEU B 2 93 ? 54.102 20.802 10.532 1.00 25.14 ? 317 LEU B CG 1 ATOM 2137 C CD1 . LEU B 2 93 ? 54.261 20.729 12.040 1.00 23.71 ? 317 LEU B CD1 1 ATOM 2138 C CD2 . LEU B 2 93 ? 52.718 20.328 10.086 1.00 26.33 ? 317 LEU B CD2 1 ATOM 2139 N N . LEU B 2 94 ? 53.296 24.246 7.617 1.00 24.17 ? 318 LEU B N 1 ATOM 2140 C CA . LEU B 2 94 ? 53.187 25.663 7.238 1.00 23.00 ? 318 LEU B CA 1 ATOM 2141 C C . LEU B 2 94 ? 53.368 26.523 8.510 1.00 24.45 ? 318 LEU B C 1 ATOM 2142 O O . LEU B 2 94 ? 53.161 26.056 9.681 1.00 21.41 ? 318 LEU B O 1 ATOM 2143 C CB . LEU B 2 94 ? 51.731 25.907 6.714 1.00 22.09 ? 318 LEU B CB 1 ATOM 2144 C CG . LEU B 2 94 ? 51.459 25.205 5.338 1.00 20.82 ? 318 LEU B CG 1 ATOM 2145 C CD1 . LEU B 2 94 ? 49.988 25.282 4.918 1.00 25.66 ? 318 LEU B CD1 1 ATOM 2146 C CD2 . LEU B 2 94 ? 52.320 25.798 4.247 1.00 24.31 ? 318 LEU B CD2 1 ATOM 2147 N N . ALA B 2 95 ? 53.754 27.784 8.303 1.00 25.10 ? 319 ALA B N 1 ATOM 2148 C CA . ALA B 2 95 ? 53.895 28.741 9.417 1.00 26.19 ? 319 ALA B CA 1 ATOM 2149 C C . ALA B 2 95 ? 52.684 28.751 10.366 1.00 26.47 ? 319 ALA B C 1 ATOM 2150 O O . ALA B 2 95 ? 52.834 28.715 11.611 1.00 22.48 ? 319 ALA B O 1 ATOM 2151 C CB . ALA B 2 95 ? 54.183 30.169 8.862 1.00 21.11 ? 319 ALA B CB 1 ATOM 2152 N N . TRP B 2 96 ? 51.473 28.784 9.822 1.00 21.10 ? 320 TRP B N 1 ATOM 2153 C CA . TRP B 2 96 ? 50.314 28.984 10.741 1.00 22.73 ? 320 TRP B CA 1 ATOM 2154 C C . TRP B 2 96 ? 50.160 27.791 11.663 1.00 26.02 ? 320 TRP B C 1 ATOM 2155 O O . TRP B 2 96 ? 49.710 27.923 12.784 1.00 23.25 ? 320 TRP B O 1 ATOM 2156 C CB . TRP B 2 96 ? 49.029 29.243 9.959 1.00 24.62 ? 320 TRP B CB 1 ATOM 2157 C CG . TRP B 2 96 ? 48.428 28.016 9.236 1.00 25.03 ? 320 TRP B CG 1 ATOM 2158 C CD1 . TRP B 2 96 ? 48.653 27.564 7.906 1.00 26.08 ? 320 TRP B CD1 1 ATOM 2159 C CD2 . TRP B 2 96 ? 47.399 27.137 9.759 1.00 23.94 ? 320 TRP B CD2 1 ATOM 2160 N NE1 . TRP B 2 96 ? 47.857 26.433 7.603 1.00 24.57 ? 320 TRP B NE1 1 ATOM 2161 C CE2 . TRP B 2 96 ? 47.092 26.125 8.689 1.00 25.10 ? 320 TRP B CE2 1 ATOM 2162 C CE3 . TRP B 2 96 ? 46.725 27.051 10.982 1.00 25.20 ? 320 TRP B CE3 1 ATOM 2163 C CZ2 . TRP B 2 96 ? 46.139 25.119 8.880 1.00 26.16 ? 320 TRP B CZ2 1 ATOM 2164 C CZ3 . TRP B 2 96 ? 45.762 26.018 11.156 1.00 25.53 ? 320 TRP B CZ3 1 ATOM 2165 C CH2 . TRP B 2 96 ? 45.494 25.054 10.130 1.00 23.22 ? 320 TRP B CH2 1 ATOM 2166 N N . GLN B 2 97 ? 50.542 26.610 11.172 1.00 23.74 ? 321 GLN B N 1 ATOM 2167 C CA . GLN B 2 97 ? 50.465 25.370 11.949 1.00 24.88 ? 321 GLN B CA 1 ATOM 2168 C C . GLN B 2 97 ? 51.537 25.345 13.043 1.00 25.26 ? 321 GLN B C 1 ATOM 2169 O O . GLN B 2 97 ? 51.217 25.037 14.210 1.00 24.68 ? 321 GLN B O 1 ATOM 2170 C CB . GLN B 2 97 ? 50.649 24.181 11.030 1.00 23.21 ? 321 GLN B CB 1 ATOM 2171 C CG . GLN B 2 97 ? 49.447 24.083 10.081 1.00 24.56 ? 321 GLN B CG 1 ATOM 2172 C CD . GLN B 2 97 ? 49.637 23.022 8.996 1.00 28.91 ? 321 GLN B CD 1 ATOM 2173 O OE1 . GLN B 2 97 ? 50.737 22.881 8.406 1.00 27.15 ? 321 GLN B OE1 1 ATOM 2174 N NE2 . GLN B 2 97 ? 48.501 22.308 8.670 1.00 24.50 ? 321 GLN B NE2 1 ATOM 2175 N N . ARG B 2 98 ? 52.768 25.705 12.704 1.00 24.34 ? 322 ARG B N 1 ATOM 2176 C CA . ARG B 2 98 ? 53.815 25.844 13.730 1.00 25.37 ? 322 ARG B CA 1 ATOM 2177 C C . ARG B 2 98 ? 53.559 26.943 14.780 1.00 25.33 ? 322 ARG B C 1 ATOM 2178 O O . ARG B 2 98 ? 53.814 26.718 15.946 1.00 22.46 ? 322 ARG B O 1 ATOM 2179 C CB . ARG B 2 98 ? 55.195 25.934 13.114 1.00 23.72 ? 322 ARG B CB 1 ATOM 2180 C CG . ARG B 2 98 ? 55.508 24.679 12.253 1.00 24.61 ? 322 ARG B CG 1 ATOM 2181 C CD . ARG B 2 98 ? 56.882 24.810 11.563 1.00 22.42 ? 322 ARG B CD 1 ATOM 2182 N NE . ARG B 2 98 ? 56.743 25.651 10.352 1.00 24.11 ? 322 ARG B NE 1 ATOM 2183 C CZ . ARG B 2 98 ? 57.301 26.848 10.204 1.00 23.27 ? 322 ARG B CZ 1 ATOM 2184 N NH1 . ARG B 2 98 ? 58.074 27.403 11.214 1.00 19.61 ? 322 ARG B NH1 1 ATOM 2185 N NH2 . ARG B 2 98 ? 57.089 27.473 9.055 1.00 22.63 ? 322 ARG B NH2 1 ATOM 2186 N N . VAL B 2 99 ? 53.039 28.100 14.356 1.00 22.23 ? 323 VAL B N 1 ATOM 2187 C CA . VAL B 2 99 ? 52.610 29.150 15.289 1.00 21.38 ? 323 VAL B CA 1 ATOM 2188 C C . VAL B 2 99 ? 51.537 28.538 16.191 1.00 23.65 ? 323 VAL B C 1 ATOM 2189 O O . VAL B 2 99 ? 51.594 28.721 17.433 1.00 23.90 ? 323 VAL B O 1 ATOM 2190 C CB . VAL B 2 99 ? 52.131 30.447 14.547 1.00 21.20 ? 323 VAL B CB 1 ATOM 2191 C CG1 . VAL B 2 99 ? 51.429 31.486 15.505 1.00 20.60 ? 323 VAL B CG1 1 ATOM 2192 C CG2 . VAL B 2 99 ? 53.309 31.111 13.830 1.00 19.74 ? 323 VAL B CG2 1 ATOM 2193 N N . ARG B 2 100 ? 50.574 27.782 15.630 1.00 21.44 ? 324 ARG B N 1 ATOM 2194 C CA . ARG B 2 100 ? 49.521 27.306 16.521 1.00 23.22 ? 324 ARG B CA 1 ATOM 2195 C C . ARG B 2 100 ? 50.018 26.209 17.483 1.00 22.50 ? 324 ARG B C 1 ATOM 2196 O O . ARG B 2 100 ? 49.629 26.191 18.665 1.00 25.21 ? 324 ARG B O 1 ATOM 2197 C CB . ARG B 2 100 ? 48.306 26.742 15.706 1.00 23.80 ? 324 ARG B CB 1 ATOM 2198 C CG . ARG B 2 100 ? 47.471 27.888 15.059 1.00 23.52 ? 324 ARG B CG 1 ATOM 2199 C CD . ARG B 2 100 ? 46.583 28.692 16.043 1.00 25.53 ? 324 ARG B CD 1 ATOM 2200 N NE . ARG B 2 100 ? 45.878 27.743 16.947 1.00 24.89 ? 324 ARG B NE 1 ATOM 2201 C CZ . ARG B 2 100 ? 44.804 27.013 16.625 1.00 29.74 ? 324 ARG B CZ 1 ATOM 2202 N NH1 . ARG B 2 100 ? 44.241 27.102 15.413 1.00 27.91 ? 324 ARG B NH1 1 ATOM 2203 N NH2 . ARG B 2 100 ? 44.260 26.180 17.536 1.00 29.71 ? 324 ARG B NH2 1 ATOM 2204 N N . VAL B 2 101 ? 50.858 25.317 16.981 1.00 23.73 ? 325 VAL B N 1 ATOM 2205 C CA . VAL B 2 101 ? 51.347 24.250 17.865 1.00 24.12 ? 325 VAL B CA 1 ATOM 2206 C C . VAL B 2 101 ? 52.241 24.865 18.998 1.00 26.89 ? 325 VAL B C 1 ATOM 2207 O O . VAL B 2 101 ? 52.089 24.577 20.210 1.00 26.66 ? 325 VAL B O 1 ATOM 2208 C CB . VAL B 2 101 ? 52.078 23.176 17.079 1.00 23.79 ? 325 VAL B CB 1 ATOM 2209 C CG1 . VAL B 2 101 ? 52.743 22.194 18.088 1.00 19.53 ? 325 VAL B CG1 1 ATOM 2210 C CG2 . VAL B 2 101 ? 51.023 22.392 16.226 1.00 25.04 ? 325 VAL B CG2 1 ATOM 2211 N N . ALA B 2 102 ? 53.174 25.701 18.611 1.00 25.28 ? 326 ALA B N 1 ATOM 2212 C CA . ALA B 2 102 ? 54.000 26.382 19.584 1.00 25.19 ? 326 ALA B CA 1 ATOM 2213 C C . ALA B 2 102 ? 53.183 27.197 20.608 1.00 26.46 ? 326 ALA B C 1 ATOM 2214 O O . ALA B 2 102 ? 53.530 27.195 21.820 1.00 25.04 ? 326 ALA B O 1 ATOM 2215 C CB . ALA B 2 102 ? 55.034 27.280 18.858 1.00 24.22 ? 326 ALA B CB 1 ATOM 2216 N N . SER B 2 103 ? 52.142 27.941 20.167 1.00 24.96 ? 327 SER B N 1 ATOM 2217 C CA . SER B 2 103 ? 51.406 28.821 21.063 1.00 23.60 ? 327 SER B CA 1 ATOM 2218 C C . SER B 2 103 ? 50.524 27.983 22.001 1.00 26.35 ? 327 SER B C 1 ATOM 2219 O O . SER B 2 103 ? 50.107 28.437 23.099 1.00 28.57 ? 327 SER B O 1 ATOM 2220 C CB . SER B 2 103 ? 50.528 29.801 20.269 1.00 24.64 ? 327 SER B CB 1 ATOM 2221 O OG . SER B 2 103 ? 51.334 30.594 19.425 1.00 27.73 ? 327 SER B OG 1 ATOM 2222 N N . MET B 2 104 ? 50.256 26.745 21.583 1.00 23.77 ? 328 MET B N 1 ATOM 2223 C CA . MET B 2 104 ? 49.550 25.787 22.447 1.00 27.05 ? 328 MET B CA 1 ATOM 2224 C C . MET B 2 104 ? 50.434 25.021 23.428 1.00 26.30 ? 328 MET B C 1 ATOM 2225 O O . MET B 2 104 ? 50.015 24.713 24.570 1.00 28.12 ? 328 MET B O 1 ATOM 2226 C CB . MET B 2 104 ? 48.869 24.736 21.556 1.00 27.51 ? 328 MET B CB 1 ATOM 2227 C CG . MET B 2 104 ? 47.758 23.984 22.249 1.00 35.53 ? 328 MET B CG 1 ATOM 2228 S SD . MET B 2 104 ? 46.596 23.262 21.025 1.00 37.70 ? 328 MET B SD 1 ATOM 2229 C CE . MET B 2 104 ? 45.473 22.757 22.350 1.00 33.08 ? 328 MET B CE 1 ATOM 2230 N N . MET B 2 105 ? 51.649 24.680 23.013 1.00 26.88 ? 329 MET B N 1 ATOM 2231 C CA . MET B 2 105 ? 52.517 23.808 23.822 1.00 30.22 ? 329 MET B CA 1 ATOM 2232 C C . MET B 2 105 ? 53.474 24.661 24.725 1.00 32.37 ? 329 MET B C 1 ATOM 2233 O O . MET B 2 105 ? 53.849 24.224 25.797 1.00 27.29 ? 329 MET B O 1 ATOM 2234 C CB . MET B 2 105 ? 53.329 22.909 22.899 1.00 28.44 ? 329 MET B CB 1 ATOM 2235 C CG . MET B 2 105 ? 52.502 21.893 22.085 1.00 29.98 ? 329 MET B CG 1 ATOM 2236 S SD . MET B 2 105 ? 53.635 20.729 21.385 1.00 31.94 ? 329 MET B SD 1 ATOM 2237 C CE . MET B 2 105 ? 53.945 19.681 22.825 1.00 33.59 ? 329 MET B CE 1 ATOM 2238 N N . ALA B 2 106 ? 53.849 25.878 24.317 1.00 25.31 ? 330 ALA B N 1 ATOM 2239 C CA . ALA B 2 106 ? 54.982 26.539 24.989 1.00 28.21 ? 330 ALA B CA 1 ATOM 2240 C C . ALA B 2 106 ? 54.575 27.406 26.192 1.00 27.42 ? 330 ALA B C 1 ATOM 2241 O O . ALA B 2 106 ? 53.543 28.072 26.161 1.00 24.52 ? 330 ALA B O 1 ATOM 2242 C CB . ALA B 2 106 ? 55.824 27.363 23.999 1.00 28.01 ? 330 ALA B CB 1 ATOM 2243 N N . ASN B 2 107 ? 55.428 27.449 27.212 1.00 26.35 ? 331 ASN B N 1 ATOM 2244 C CA . ASN B 2 107 ? 55.130 28.244 28.430 1.00 24.80 ? 331 ASN B CA 1 ATOM 2245 C C . ASN B 2 107 ? 56.127 29.370 28.670 1.00 23.14 ? 331 ASN B C 1 ATOM 2246 O O . ASN B 2 107 ? 56.038 30.113 29.652 1.00 25.31 ? 331 ASN B O 1 ATOM 2247 C CB . ASN B 2 107 ? 55.027 27.311 29.671 1.00 26.23 ? 331 ASN B CB 1 ATOM 2248 C CG . ASN B 2 107 ? 54.272 27.958 30.810 1.00 25.98 ? 331 ASN B CG 1 ATOM 2249 O OD1 . ASN B 2 107 ? 53.240 28.533 30.615 1.00 27.41 ? 331 ASN B OD1 1 ATOM 2250 N ND2 . ASN B 2 107 ? 54.815 27.829 32.056 1.00 25.39 ? 331 ASN B ND2 1 ATOM 2251 N N . ASN B 2 108 ? 57.028 29.560 27.726 1.00 21.48 ? 332 ASN B N 1 ATOM 2252 C CA . ASN B 2 108 ? 58.114 30.609 27.851 1.00 21.85 ? 332 ASN B CA 1 ATOM 2253 C C . ASN B 2 108 ? 58.645 30.796 26.460 1.00 22.55 ? 332 ASN B C 1 ATOM 2254 O O . ASN B 2 108 ? 58.359 29.971 25.575 1.00 20.35 ? 332 ASN B O 1 ATOM 2255 C CB . ASN B 2 108 ? 59.274 30.188 28.875 1.00 21.87 ? 332 ASN B CB 1 ATOM 2256 C CG . ASN B 2 108 ? 59.967 28.934 28.481 1.00 28.27 ? 332 ASN B CG 1 ATOM 2257 O OD1 . ASN B 2 108 ? 60.621 28.883 27.479 1.00 26.67 ? 332 ASN B OD1 1 ATOM 2258 N ND2 . ASN B 2 108 ? 59.741 27.856 29.237 1.00 31.83 ? 332 ASN B ND2 1 ATOM 2259 N N . GLY B 2 109 ? 59.438 31.845 26.221 1.00 21.43 ? 333 GLY B N 1 ATOM 2260 C CA . GLY B 2 109 ? 59.797 32.164 24.861 1.00 18.63 ? 333 GLY B CA 1 ATOM 2261 C C . GLY B 2 109 ? 60.818 31.249 24.236 1.00 20.99 ? 333 GLY B C 1 ATOM 2262 O O . GLY B 2 109 ? 60.789 31.086 23.049 1.00 20.41 ? 333 GLY B O 1 ATOM 2263 N N . LYS B 2 110 ? 61.664 30.556 25.046 1.00 20.14 ? 334 LYS B N 1 ATOM 2264 C CA . LYS B 2 110 ? 62.664 29.664 24.460 1.00 20.64 ? 334 LYS B CA 1 ATOM 2265 C C . LYS B 2 110 ? 61.920 28.413 23.956 1.00 22.25 ? 334 LYS B C 1 ATOM 2266 O O . LYS B 2 110 ? 62.116 27.952 22.835 1.00 23.73 ? 334 LYS B O 1 ATOM 2267 C CB . LYS B 2 110 ? 63.692 29.248 25.534 1.00 20.41 ? 334 LYS B CB 1 ATOM 2268 C CG . LYS B 2 110 ? 64.801 28.302 24.968 1.00 27.62 ? 334 LYS B CG 1 ATOM 2269 C CD . LYS B 2 110 ? 65.964 28.101 25.979 1.00 33.45 ? 334 LYS B CD 1 ATOM 2270 C CE . LYS B 2 110 ? 66.924 27.075 25.334 1.00 42.38 ? 334 LYS B CE 1 ATOM 2271 N NZ . LYS B 2 110 ? 68.087 26.557 26.142 1.00 45.87 ? 334 LYS B NZ 1 ATOM 2272 N N . GLN B 2 111 ? 61.027 27.927 24.789 1.00 21.63 ? 335 GLN B N 1 ATOM 2273 C CA . GLN B 2 111 ? 60.263 26.751 24.394 1.00 22.51 ? 335 GLN B CA 1 ATOM 2274 C C . GLN B 2 111 ? 59.353 27.076 23.158 1.00 23.50 ? 335 GLN B C 1 ATOM 2275 O O . GLN B 2 111 ? 59.163 26.241 22.256 1.00 20.25 ? 335 GLN B O 1 ATOM 2276 C CB . GLN B 2 111 ? 59.436 26.367 25.584 1.00 24.78 ? 335 GLN B CB 1 ATOM 2277 C CG . GLN B 2 111 ? 58.559 25.164 25.286 1.00 33.68 ? 335 GLN B CG 1 ATOM 2278 C CD . GLN B 2 111 ? 57.795 24.668 26.506 1.00 39.83 ? 335 GLN B CD 1 ATOM 2279 O OE1 . GLN B 2 111 ? 57.489 25.429 27.430 1.00 27.70 ? 335 GLN B OE1 1 ATOM 2280 N NE2 . GLN B 2 111 ? 57.435 23.359 26.482 1.00 40.59 ? 335 GLN B NE2 1 ATOM 2281 N N . TRP B 2 112 ? 58.813 28.296 23.112 1.00 19.64 ? 336 TRP B N 1 ATOM 2282 C CA . TRP B 2 112 ? 58.020 28.708 21.921 1.00 21.28 ? 336 TRP B CA 1 ATOM 2283 C C . TRP B 2 112 ? 58.930 28.583 20.685 1.00 20.55 ? 336 TRP B C 1 ATOM 2284 O O . TRP B 2 112 ? 58.547 27.952 19.672 1.00 20.59 ? 336 TRP B O 1 ATOM 2285 C CB . TRP B 2 112 ? 57.531 30.164 22.096 1.00 19.90 ? 336 TRP B CB 1 ATOM 2286 C CG . TRP B 2 112 ? 56.442 30.463 21.065 1.00 22.62 ? 336 TRP B CG 1 ATOM 2287 C CD1 . TRP B 2 112 ? 55.053 30.301 21.226 1.00 19.66 ? 336 TRP B CD1 1 ATOM 2288 C CD2 . TRP B 2 112 ? 56.638 30.841 19.663 1.00 21.32 ? 336 TRP B CD2 1 ATOM 2289 N NE1 . TRP B 2 112 ? 54.400 30.599 20.015 1.00 21.62 ? 336 TRP B NE1 1 ATOM 2290 C CE2 . TRP B 2 112 ? 55.299 30.964 19.071 1.00 21.46 ? 336 TRP B CE2 1 ATOM 2291 C CE3 . TRP B 2 112 ? 57.748 31.158 18.873 1.00 21.29 ? 336 TRP B CE3 1 ATOM 2292 C CZ2 . TRP B 2 112 ? 55.123 31.288 17.734 1.00 21.87 ? 336 TRP B CZ2 1 ATOM 2293 C CZ3 . TRP B 2 112 ? 57.524 31.584 17.543 1.00 21.88 ? 336 TRP B CZ3 1 ATOM 2294 C CH2 . TRP B 2 112 ? 56.238 31.624 16.997 1.00 20.87 ? 336 TRP B CH2 1 ATOM 2295 N N . ALA B 2 113 ? 60.140 29.185 20.729 1.00 18.30 ? 337 ALA B N 1 ATOM 2296 C CA . ALA B 2 113 ? 60.983 29.138 19.550 1.00 19.19 ? 337 ALA B CA 1 ATOM 2297 C C . ALA B 2 113 ? 61.340 27.651 19.176 1.00 21.76 ? 337 ALA B C 1 ATOM 2298 O O . ALA B 2 113 ? 61.412 27.280 18.013 1.00 21.98 ? 337 ALA B O 1 ATOM 2299 C CB . ALA B 2 113 ? 62.259 29.917 19.858 1.00 20.04 ? 337 ALA B CB 1 ATOM 2300 N N . GLU B 2 114 ? 61.617 26.834 20.178 1.00 22.85 ? 338 GLU B N 1 ATOM 2301 C CA . GLU B 2 114 ? 62.084 25.458 19.892 1.00 25.10 ? 338 GLU B CA 1 ATOM 2302 C C . GLU B 2 114 ? 60.947 24.700 19.185 1.00 26.02 ? 338 GLU B C 1 ATOM 2303 O O . GLU B 2 114 ? 61.209 24.018 18.229 1.00 28.47 ? 338 GLU B O 1 ATOM 2304 C CB . GLU B 2 114 ? 62.453 24.760 21.248 1.00 27.65 ? 338 GLU B CB 1 ATOM 2305 C CG . GLU B 2 114 ? 63.798 25.264 21.722 1.00 31.17 ? 338 GLU B CG 1 ATOM 2306 C CD . GLU B 2 114 ? 64.111 24.804 23.147 1.00 44.09 ? 338 GLU B CD 1 ATOM 2307 O OE1 . GLU B 2 114 ? 63.199 24.347 23.913 1.00 42.30 ? 338 GLU B OE1 1 ATOM 2308 O OE2 . GLU B 2 114 ? 65.282 24.931 23.534 1.00 49.30 ? 338 GLU B OE2 1 ATOM 2309 N N . VAL B 2 115 ? 59.726 24.833 19.675 1.00 22.27 ? 339 VAL B N 1 ATOM 2310 C CA . VAL B 2 115 ? 58.557 24.070 19.128 1.00 24.91 ? 339 VAL B CA 1 ATOM 2311 C C . VAL B 2 115 ? 58.236 24.642 17.710 1.00 26.01 ? 339 VAL B C 1 ATOM 2312 O O . VAL B 2 115 ? 58.076 23.920 16.749 1.00 20.94 ? 339 VAL B O 1 ATOM 2313 C CB . VAL B 2 115 ? 57.341 24.175 20.058 1.00 22.38 ? 339 VAL B CB 1 ATOM 2314 C CG1 . VAL B 2 115 ? 56.069 23.638 19.435 1.00 26.06 ? 339 VAL B CG1 1 ATOM 2315 C CG2 . VAL B 2 115 ? 57.588 23.452 21.416 1.00 24.64 ? 339 VAL B CG2 1 ATOM 2316 N N . PHE B 2 116 ? 58.228 25.968 17.583 1.00 21.63 ? 340 PHE B N 1 ATOM 2317 C CA . PHE B 2 116 ? 57.860 26.615 16.295 1.00 22.00 ? 340 PHE B CA 1 ATOM 2318 C C . PHE B 2 116 ? 58.866 26.214 15.198 1.00 24.72 ? 340 PHE B C 1 ATOM 2319 O O . PHE B 2 116 ? 58.527 26.157 14.036 1.00 24.84 ? 340 PHE B O 1 ATOM 2320 C CB . PHE B 2 116 ? 58.018 28.178 16.487 1.00 19.43 ? 340 PHE B CB 1 ATOM 2321 C CG . PHE B 2 116 ? 58.118 28.922 15.219 1.00 20.98 ? 340 PHE B CG 1 ATOM 2322 C CD1 . PHE B 2 116 ? 56.979 29.247 14.528 1.00 20.28 ? 340 PHE B CD1 1 ATOM 2323 C CD2 . PHE B 2 116 ? 59.356 29.327 14.731 1.00 22.61 ? 340 PHE B CD2 1 ATOM 2324 C CE1 . PHE B 2 116 ? 57.096 29.995 13.341 1.00 23.07 ? 340 PHE B CE1 1 ATOM 2325 C CE2 . PHE B 2 116 ? 59.482 30.053 13.557 1.00 22.79 ? 340 PHE B CE2 1 ATOM 2326 C CZ . PHE B 2 116 ? 58.366 30.406 12.853 1.00 20.37 ? 340 PHE B CZ 1 ATOM 2327 N N . SER B 2 117 ? 60.120 26.020 15.575 1.00 21.91 ? 341 SER B N 1 ATOM 2328 C CA . SER B 2 117 ? 61.199 25.639 14.662 1.00 24.38 ? 341 SER B CA 1 ATOM 2329 C C . SER B 2 117 ? 61.042 24.240 14.023 1.00 26.83 ? 341 SER B C 1 ATOM 2330 O O . SER B 2 117 ? 61.632 23.946 12.996 1.00 24.93 ? 341 SER B O 1 ATOM 2331 C CB . SER B 2 117 ? 62.543 25.598 15.414 1.00 25.39 ? 341 SER B CB 1 ATOM 2332 O OG . SER B 2 117 ? 62.884 26.946 15.777 1.00 31.01 ? 341 SER B OG 1 ATOM 2333 N N . LYS B 2 118 ? 60.298 23.383 14.663 1.00 24.82 ? 342 LYS B N 1 ATOM 2334 C CA . LYS B 2 118 ? 60.197 21.946 14.187 1.00 26.77 ? 342 LYS B CA 1 ATOM 2335 C C . LYS B 2 118 ? 59.412 21.808 12.872 1.00 27.54 ? 342 LYS B C 1 ATOM 2336 O O . LYS B 2 118 ? 58.233 22.295 12.773 1.00 22.50 ? 342 LYS B O 1 ATOM 2337 C CB . LYS B 2 118 ? 59.486 21.099 15.272 1.00 24.77 ? 342 LYS B CB 1 ATOM 2338 C CG . LYS B 2 118 ? 60.380 20.926 16.537 1.00 31.56 ? 342 LYS B CG 1 ATOM 2339 C CD . LYS B 2 118 ? 59.731 19.944 17.535 1.00 40.89 ? 342 LYS B CD 1 ATOM 2340 C CE . LYS B 2 118 ? 60.070 20.241 18.996 1.00 57.28 ? 342 LYS B CE 1 ATOM 2341 N NZ . LYS B 2 118 ? 61.276 19.511 19.496 1.00 68.36 ? 342 LYS B NZ 1 ATOM 2342 N N . TYR B 2 119 ? 60.021 21.121 11.911 1.00 24.70 ? 343 TYR B N 1 ATOM 2343 C CA . TYR B 2 119 ? 59.438 20.952 10.534 1.00 25.93 ? 343 TYR B CA 1 ATOM 2344 C C . TYR B 2 119 ? 59.261 22.340 9.877 1.00 24.76 ? 343 TYR B C 1 ATOM 2345 O O . TYR B 2 119 ? 58.327 22.564 9.183 1.00 23.06 ? 343 TYR B O 1 ATOM 2346 C CB . TYR B 2 119 ? 58.076 20.191 10.551 1.00 23.99 ? 343 TYR B CB 1 ATOM 2347 C CG . TYR B 2 119 ? 58.214 18.869 11.285 1.00 31.48 ? 343 TYR B CG 1 ATOM 2348 C CD1 . TYR B 2 119 ? 58.798 17.757 10.637 1.00 32.67 ? 343 TYR B CD1 1 ATOM 2349 C CD2 . TYR B 2 119 ? 57.859 18.750 12.631 1.00 27.46 ? 343 TYR B CD2 1 ATOM 2350 C CE1 . TYR B 2 119 ? 58.973 16.550 11.305 1.00 36.99 ? 343 TYR B CE1 1 ATOM 2351 C CE2 . TYR B 2 119 ? 58.019 17.548 13.305 1.00 33.30 ? 343 TYR B CE2 1 ATOM 2352 C CZ . TYR B 2 119 ? 58.566 16.454 12.629 1.00 35.91 ? 343 TYR B CZ 1 ATOM 2353 O OH . TYR B 2 119 ? 58.689 15.248 13.284 1.00 38.69 ? 343 TYR B OH 1 ATOM 2354 N N . ASN B 2 120 ? 60.200 23.249 10.120 1.00 24.98 ? 344 ASN B N 1 ATOM 2355 C CA . ASN B 2 120 ? 60.175 24.585 9.488 1.00 24.39 ? 344 ASN B CA 1 ATOM 2356 C C . ASN B 2 120 ? 59.946 24.461 7.955 1.00 24.85 ? 344 ASN B C 1 ATOM 2357 O O . ASN B 2 120 ? 60.675 23.775 7.270 1.00 26.90 ? 344 ASN B O 1 ATOM 2358 C CB . ASN B 2 120 ? 61.539 25.236 9.794 1.00 22.76 ? 344 ASN B CB 1 ATOM 2359 C CG . ASN B 2 120 ? 61.768 26.551 9.041 1.00 23.44 ? 344 ASN B CG 1 ATOM 2360 O OD1 . ASN B 2 120 ? 60.803 27.212 8.651 1.00 25.60 ? 344 ASN B OD1 1 ATOM 2361 N ND2 . ASN B 2 120 ? 63.048 26.898 8.770 1.00 22.21 ? 344 ASN B ND2 1 ATOM 2362 N N . SER B 2 121 ? 58.971 25.171 7.396 1.00 22.35 ? 345 SER B N 1 ATOM 2363 C CA . SER B 2 121 ? 58.721 25.150 5.957 1.00 21.82 ? 345 SER B CA 1 ATOM 2364 C C . SER B 2 121 ? 59.533 26.171 5.149 1.00 24.60 ? 345 SER B C 1 ATOM 2365 O O . SER B 2 121 ? 59.612 26.065 3.925 1.00 25.68 ? 345 SER B O 1 ATOM 2366 C CB . SER B 2 121 ? 57.231 25.375 5.721 1.00 24.18 ? 345 SER B CB 1 ATOM 2367 O OG . SER B 2 121 ? 56.929 26.733 6.215 1.00 24.23 ? 345 SER B OG 1 ATOM 2368 N N . GLY B 2 122 ? 60.112 27.206 5.784 1.00 21.91 ? 346 GLY B N 1 ATOM 2369 C CA . GLY B 2 122 ? 60.729 28.261 4.980 1.00 22.21 ? 346 GLY B CA 1 ATOM 2370 C C . GLY B 2 122 ? 59.693 29.080 4.206 1.00 21.65 ? 346 GLY B C 1 ATOM 2371 O O . GLY B 2 122 ? 60.021 29.728 3.223 1.00 20.24 ? 346 GLY B O 1 ATOM 2372 N N . THR B 2 123 ? 58.441 29.030 4.652 1.00 22.09 ? 347 THR B N 1 ATOM 2373 C CA . THR B 2 123 ? 57.338 29.834 4.033 1.00 21.73 ? 347 THR B CA 1 ATOM 2374 C C . THR B 2 123 ? 56.835 30.826 5.091 1.00 22.69 ? 347 THR B C 1 ATOM 2375 O O . THR B 2 123 ? 56.856 30.474 6.303 1.00 22.11 ? 347 THR B O 1 ATOM 2376 C CB . THR B 2 123 ? 56.190 28.931 3.451 1.00 21.71 ? 347 THR B CB 1 ATOM 2377 O OG1 . THR B 2 123 ? 55.599 28.123 4.461 1.00 23.00 ? 347 THR B OG1 1 ATOM 2378 C CG2 . THR B 2 123 ? 56.781 28.006 2.254 1.00 24.14 ? 347 THR B CG2 1 ATOM 2379 N N . TYR B 2 124 ? 56.367 32.024 4.666 1.00 22.85 ? 348 TYR B N 1 ATOM 2380 C CA . TYR B 2 124 ? 55.983 33.097 5.607 1.00 21.88 ? 348 TYR B CA 1 ATOM 2381 C C . TYR B 2 124 ? 57.174 33.407 6.549 1.00 20.69 ? 348 TYR B C 1 ATOM 2382 O O . TYR B 2 124 ? 57.105 33.234 7.790 1.00 22.42 ? 348 TYR B O 1 ATOM 2383 C CB . TYR B 2 124 ? 54.688 32.743 6.389 1.00 20.77 ? 348 TYR B CB 1 ATOM 2384 C CG . TYR B 2 124 ? 53.901 34.007 6.846 1.00 19.40 ? 348 TYR B CG 1 ATOM 2385 C CD1 . TYR B 2 124 ? 54.103 35.239 6.213 1.00 22.55 ? 348 TYR B CD1 1 ATOM 2386 C CD2 . TYR B 2 124 ? 53.007 33.938 7.892 1.00 24.35 ? 348 TYR B CD2 1 ATOM 2387 C CE1 . TYR B 2 124 ? 53.380 36.383 6.608 1.00 24.99 ? 348 TYR B CE1 1 ATOM 2388 C CE2 . TYR B 2 124 ? 52.307 35.094 8.349 1.00 23.78 ? 348 TYR B CE2 1 ATOM 2389 C CZ . TYR B 2 124 ? 52.476 36.292 7.676 1.00 23.70 ? 348 TYR B CZ 1 ATOM 2390 O OH . TYR B 2 124 ? 51.815 37.480 8.099 1.00 20.96 ? 348 TYR B OH 1 ATOM 2391 N N . ASN B 2 125 ? 58.289 33.823 5.933 1.00 20.27 ? 349 ASN B N 1 ATOM 2392 C CA . ASN B 2 125 ? 59.566 34.018 6.660 1.00 23.38 ? 349 ASN B CA 1 ATOM 2393 C C . ASN B 2 125 ? 59.584 35.330 7.464 1.00 23.99 ? 349 ASN B C 1 ATOM 2394 O O . ASN B 2 125 ? 59.663 36.415 6.883 1.00 21.48 ? 349 ASN B O 1 ATOM 2395 C CB . ASN B 2 125 ? 60.725 33.979 5.681 1.00 21.22 ? 349 ASN B CB 1 ATOM 2396 C CG . ASN B 2 125 ? 60.816 32.592 5.034 1.00 23.61 ? 349 ASN B CG 1 ATOM 2397 O OD1 . ASN B 2 125 ? 60.984 31.573 5.738 1.00 23.73 ? 349 ASN B OD1 1 ATOM 2398 N ND2 . ASN B 2 125 ? 60.612 32.547 3.707 1.00 22.07 ? 349 ASN B ND2 1 ATOM 2399 N N . ASN B 2 126 ? 59.524 35.202 8.792 1.00 20.09 ? 350 ASN B N 1 ATOM 2400 C CA . ASN B 2 126 ? 59.080 36.319 9.650 1.00 22.80 ? 350 ASN B CA 1 ATOM 2401 C C . ASN B 2 126 ? 60.004 36.441 10.805 1.00 23.83 ? 350 ASN B C 1 ATOM 2402 O O . ASN B 2 126 ? 60.759 35.495 11.153 1.00 21.53 ? 350 ASN B O 1 ATOM 2403 C CB . ASN B 2 126 ? 57.687 36.007 10.319 1.00 19.91 ? 350 ASN B CB 1 ATOM 2404 C CG . ASN B 2 126 ? 56.522 36.006 9.306 1.00 22.01 ? 350 ASN B CG 1 ATOM 2405 O OD1 . ASN B 2 126 ? 56.606 36.606 8.254 1.00 24.90 ? 350 ASN B OD1 1 ATOM 2406 N ND2 . ASN B 2 126 ? 55.473 35.254 9.603 1.00 19.05 ? 350 ASN B ND2 1 ATOM 2407 N N . GLN B 2 127 ? 59.930 37.613 11.425 1.00 18.05 ? 351 GLN B N 1 ATOM 2408 C CA . GLN B 2 127 ? 60.390 37.776 12.811 1.00 18.97 ? 351 GLN B CA 1 ATOM 2409 C C . GLN B 2 127 ? 59.189 37.734 13.796 1.00 19.75 ? 351 GLN B C 1 ATOM 2410 O O . GLN B 2 127 ? 58.256 38.534 13.620 1.00 20.21 ? 351 GLN B O 1 ATOM 2411 C CB . GLN B 2 127 ? 60.952 39.187 12.946 1.00 16.89 ? 351 GLN B CB 1 ATOM 2412 C CG . GLN B 2 127 ? 61.430 39.486 14.416 1.00 16.99 ? 351 GLN B CG 1 ATOM 2413 C CD . GLN B 2 127 ? 61.883 40.959 14.597 1.00 20.17 ? 351 GLN B CD 1 ATOM 2414 O OE1 . GLN B 2 127 ? 61.175 41.764 15.217 1.00 19.09 ? 351 GLN B OE1 1 ATOM 2415 N NE2 . GLN B 2 127 ? 63.077 41.272 14.173 1.00 16.66 ? 351 GLN B NE2 1 ATOM 2416 N N . TYR B 2 128 ? 59.273 36.937 14.863 1.00 17.35 ? 352 TYR B N 1 ATOM 2417 C CA . TYR B 2 128 ? 58.357 36.919 15.977 1.00 18.67 ? 352 TYR B CA 1 ATOM 2418 C C . TYR B 2 128 ? 59.026 37.549 17.174 1.00 21.62 ? 352 TYR B C 1 ATOM 2419 O O . TYR B 2 128 ? 60.245 37.299 17.434 1.00 20.03 ? 352 TYR B O 1 ATOM 2420 C CB . TYR B 2 128 ? 57.986 35.448 16.354 1.00 17.49 ? 352 TYR B CB 1 ATOM 2421 C CG . TYR B 2 128 ? 57.329 34.785 15.194 1.00 18.26 ? 352 TYR B CG 1 ATOM 2422 C CD1 . TYR B 2 128 ? 58.089 34.184 14.160 1.00 21.78 ? 352 TYR B CD1 1 ATOM 2423 C CD2 . TYR B 2 128 ? 55.906 34.797 15.079 1.00 20.77 ? 352 TYR B CD2 1 ATOM 2424 C CE1 . TYR B 2 128 ? 57.482 33.598 13.056 1.00 21.96 ? 352 TYR B CE1 1 ATOM 2425 C CE2 . TYR B 2 128 ? 55.299 34.215 13.942 1.00 19.84 ? 352 TYR B CE2 1 ATOM 2426 C CZ . TYR B 2 128 ? 56.076 33.612 12.982 1.00 20.79 ? 352 TYR B CZ 1 ATOM 2427 O OH . TYR B 2 128 ? 55.409 33.057 11.873 1.00 22.16 ? 352 TYR B OH 1 ATOM 2428 N N . MET B 2 129 ? 58.241 38.337 17.892 1.00 16.95 ? 353 MET B N 1 ATOM 2429 C CA . MET B 2 129 ? 58.590 38.818 19.226 1.00 18.46 ? 353 MET B CA 1 ATOM 2430 C C . MET B 2 129 ? 57.755 38.029 20.186 1.00 20.15 ? 353 MET B C 1 ATOM 2431 O O . MET B 2 129 ? 56.514 38.114 20.109 1.00 19.44 ? 353 MET B O 1 ATOM 2432 C CB . MET B 2 129 ? 58.326 40.308 19.357 1.00 17.75 ? 353 MET B CB 1 ATOM 2433 C CG . MET B 2 129 ? 59.278 41.167 18.498 1.00 19.26 ? 353 MET B CG 1 ATOM 2434 S SD . MET B 2 129 ? 58.311 42.534 17.593 1.00 20.89 ? 353 MET B SD 1 ATOM 2435 C CE . MET B 2 129 ? 57.647 41.636 16.136 1.00 16.63 ? 353 MET B CE 1 ATOM 2436 N N . VAL B 2 130 ? 58.392 37.205 21.054 1.00 18.57 ? 354 VAL B N 1 ATOM 2437 C CA . VAL B 2 130 ? 57.634 36.409 22.009 1.00 19.13 ? 354 VAL B CA 1 ATOM 2438 C C . VAL B 2 130 ? 57.896 37.173 23.326 1.00 19.41 ? 354 VAL B C 1 ATOM 2439 O O . VAL B 2 130 ? 59.044 37.189 23.849 1.00 20.58 ? 354 VAL B O 1 ATOM 2440 C CB . VAL B 2 130 ? 58.160 34.905 22.099 1.00 17.99 ? 354 VAL B CB 1 ATOM 2441 C CG1 . VAL B 2 130 ? 57.269 34.117 23.052 1.00 19.56 ? 354 VAL B CG1 1 ATOM 2442 C CG2 . VAL B 2 130 ? 58.174 34.361 20.677 1.00 17.89 ? 354 VAL B CG2 1 ATOM 2443 N N . LEU B 2 131 ? 56.865 37.866 23.801 1.00 17.95 ? 355 LEU B N 1 ATOM 2444 C CA . LEU B 2 131 ? 56.966 38.699 25.044 1.00 20.16 ? 355 LEU B CA 1 ATOM 2445 C C . LEU B 2 131 ? 56.324 37.877 26.213 1.00 24.09 ? 355 LEU B C 1 ATOM 2446 O O . LEU B 2 131 ? 55.080 37.670 26.250 1.00 20.05 ? 355 LEU B O 1 ATOM 2447 C CB . LEU B 2 131 ? 56.266 40.042 24.827 1.00 18.44 ? 355 LEU B CB 1 ATOM 2448 C CG . LEU B 2 131 ? 56.236 40.995 26.070 1.00 21.93 ? 355 LEU B CG 1 ATOM 2449 C CD1 . LEU B 2 131 ? 57.661 41.448 26.384 1.00 21.22 ? 355 LEU B CD1 1 ATOM 2450 C CD2 . LEU B 2 131 ? 55.350 42.226 25.760 1.00 23.42 ? 355 LEU B CD2 1 ATOM 2451 N N . ASP B 2 132 ? 57.137 37.464 27.210 1.00 21.51 ? 356 ASP B N 1 ATOM 2452 C CA . ASP B 2 132 ? 56.602 36.565 28.279 1.00 21.83 ? 356 ASP B CA 1 ATOM 2453 C C . ASP B 2 132 ? 56.285 37.512 29.469 1.00 24.25 ? 356 ASP B C 1 ATOM 2454 O O . ASP B 2 132 ? 57.192 37.964 30.239 1.00 23.84 ? 356 ASP B O 1 ATOM 2455 C CB . ASP B 2 132 ? 57.662 35.502 28.705 1.00 20.36 ? 356 ASP B CB 1 ATOM 2456 C CG . ASP B 2 132 ? 57.120 34.478 29.700 1.00 24.20 ? 356 ASP B CG 1 ATOM 2457 O OD1 . ASP B 2 132 ? 55.968 34.636 30.204 1.00 19.37 ? 356 ASP B OD1 1 ATOM 2458 O OD2 . ASP B 2 132 ? 57.846 33.452 29.945 1.00 24.34 ? 356 ASP B OD2 1 ATOM 2459 N N . LEU B 2 133 ? 55.012 37.919 29.581 1.00 19.75 ? 357 LEU B N 1 ATOM 2460 C CA . LEU B 2 133 ? 54.593 38.825 30.607 1.00 22.07 ? 357 LEU B CA 1 ATOM 2461 C C . LEU B 2 133 ? 54.732 38.244 32.006 1.00 20.20 ? 357 LEU B C 1 ATOM 2462 O O . LEU B 2 133 ? 54.741 38.993 32.972 1.00 22.82 ? 357 LEU B O 1 ATOM 2463 C CB . LEU B 2 133 ? 53.112 39.231 30.384 1.00 25.50 ? 357 LEU B CB 1 ATOM 2464 C CG . LEU B 2 133 ? 52.849 39.994 29.054 1.00 27.33 ? 357 LEU B CG 1 ATOM 2465 C CD1 . LEU B 2 133 ? 51.344 40.220 28.833 1.00 26.89 ? 357 LEU B CD1 1 ATOM 2466 C CD2 . LEU B 2 133 ? 53.638 41.252 28.888 1.00 26.32 ? 357 LEU B CD2 1 ATOM 2467 N N . LYS B 2 134 ? 54.909 36.937 32.128 1.00 21.87 ? 358 LYS B N 1 ATOM 2468 C CA . LYS B 2 134 ? 55.142 36.340 33.456 1.00 24.22 ? 358 LYS B CA 1 ATOM 2469 C C . LYS B 2 134 ? 56.474 36.836 33.967 1.00 28.38 ? 358 LYS B C 1 ATOM 2470 O O . LYS B 2 134 ? 56.701 36.759 35.167 1.00 28.15 ? 358 LYS B O 1 ATOM 2471 C CB . LYS B 2 134 ? 55.232 34.814 33.347 1.00 25.25 ? 358 LYS B CB 1 ATOM 2472 C CG . LYS B 2 134 ? 53.813 34.261 32.903 1.00 23.49 ? 358 LYS B CG 1 ATOM 2473 C CD . LYS B 2 134 ? 53.715 32.717 33.045 1.00 25.73 ? 358 LYS B CD 1 ATOM 2474 C CE . LYS B 2 134 ? 54.720 31.928 32.166 1.00 23.40 ? 358 LYS B CE 1 ATOM 2475 N NZ . LYS B 2 134 ? 54.770 32.360 30.708 1.00 24.04 ? 358 LYS B NZ 1 ATOM 2476 N N . LYS B 2 135 ? 57.371 37.292 33.077 1.00 21.81 ? 359 LYS B N 1 ATOM 2477 C CA . LYS B 2 135 ? 58.702 37.770 33.500 1.00 22.88 ? 359 LYS B CA 1 ATOM 2478 C C . LYS B 2 135 ? 58.760 39.268 33.835 1.00 23.70 ? 359 LYS B C 1 ATOM 2479 O O . LYS B 2 135 ? 59.827 39.795 34.203 1.00 25.59 ? 359 LYS B O 1 ATOM 2480 C CB . LYS B 2 135 ? 59.714 37.476 32.400 1.00 26.86 ? 359 LYS B CB 1 ATOM 2481 C CG . LYS B 2 135 ? 59.877 35.990 32.057 1.00 26.17 ? 359 LYS B CG 1 ATOM 2482 C CD . LYS B 2 135 ? 60.411 35.078 33.204 1.00 32.59 ? 359 LYS B CD 1 ATOM 2483 C CE . LYS B 2 135 ? 60.427 33.614 32.697 1.00 30.11 ? 359 LYS B CE 1 ATOM 2484 N NZ . LYS B 2 135 ? 61.101 32.795 33.815 1.00 36.40 ? 359 LYS B NZ 1 ATOM 2485 N N . VAL B 2 136 ? 57.652 39.932 33.646 1.00 22.83 ? 360 VAL B N 1 ATOM 2486 C CA . VAL B 2 136 ? 57.567 41.426 33.808 1.00 25.25 ? 360 VAL B CA 1 ATOM 2487 C C . VAL B 2 136 ? 57.100 41.728 35.237 1.00 25.95 ? 360 VAL B C 1 ATOM 2488 O O . VAL B 2 136 ? 56.021 41.293 35.670 1.00 29.35 ? 360 VAL B O 1 ATOM 2489 C CB . VAL B 2 136 ? 56.614 42.028 32.776 1.00 23.75 ? 360 VAL B CB 1 ATOM 2490 C CG1 . VAL B 2 136 ? 56.422 43.560 32.997 1.00 22.63 ? 360 VAL B CG1 1 ATOM 2491 C CG2 . VAL B 2 136 ? 57.160 41.834 31.343 1.00 23.52 ? 360 VAL B CG2 1 ATOM 2492 N N . ASN B 2 137 ? 57.907 42.444 35.991 1.00 26.37 ? 361 ASN B N 1 ATOM 2493 C CA . ASN B 2 137 ? 57.450 42.894 37.352 1.00 28.28 ? 361 ASN B CA 1 ATOM 2494 C C . ASN B 2 137 ? 57.496 44.410 37.362 1.00 24.56 ? 361 ASN B C 1 ATOM 2495 O O . ASN B 2 137 ? 58.612 45.029 37.491 1.00 24.43 ? 361 ASN B O 1 ATOM 2496 C CB . ASN B 2 137 ? 58.396 42.355 38.418 1.00 32.07 ? 361 ASN B CB 1 ATOM 2497 C CG . ASN B 2 137 ? 58.626 40.878 38.259 1.00 38.59 ? 361 ASN B CG 1 ATOM 2498 O OD1 . ASN B 2 137 ? 57.710 40.045 38.437 1.00 44.42 ? 361 ASN B OD1 1 ATOM 2499 N ND2 . ASN B 2 137 ? 59.852 40.535 37.894 1.00 46.56 ? 361 ASN B ND2 1 ATOM 2500 N N . LEU B 2 138 ? 56.336 45.028 37.222 1.00 23.32 ? 362 LEU B N 1 ATOM 2501 C CA . LEU B 2 138 ? 56.295 46.506 37.051 1.00 25.54 ? 362 LEU B CA 1 ATOM 2502 C C . LEU B 2 138 ? 56.978 47.218 38.235 1.00 27.66 ? 362 LEU B C 1 ATOM 2503 O O . LEU B 2 138 ? 56.884 46.702 39.364 1.00 24.13 ? 362 LEU B O 1 ATOM 2504 C CB . LEU B 2 138 ? 54.835 46.995 36.881 1.00 26.91 ? 362 LEU B CB 1 ATOM 2505 C CG . LEU B 2 138 ? 54.140 46.424 35.604 1.00 27.16 ? 362 LEU B CG 1 ATOM 2506 C CD1 . LEU B 2 138 ? 52.730 46.976 35.593 1.00 30.37 ? 362 LEU B CD1 1 ATOM 2507 C CD2 . LEU B 2 138 ? 54.832 46.849 34.291 1.00 24.14 ? 362 LEU B CD2 1 ATOM 2508 N N . ASN B 2 139 ? 57.650 48.366 37.970 1.00 29.11 ? 363 ASN B N 1 ATOM 2509 C CA . ASN B 2 139 ? 58.395 49.123 38.975 1.00 31.38 ? 363 ASN B CA 1 ATOM 2510 C C . ASN B 2 139 ? 59.514 48.320 39.586 1.00 32.07 ? 363 ASN B C 1 ATOM 2511 O O . ASN B 2 139 ? 60.000 48.666 40.644 1.00 28.59 ? 363 ASN B O 1 ATOM 2512 C CB . ASN B 2 139 ? 57.472 49.634 40.122 1.00 29.07 ? 363 ASN B CB 1 ATOM 2513 C CG . ASN B 2 139 ? 56.491 50.657 39.619 1.00 34.72 ? 363 ASN B CG 1 ATOM 2514 O OD1 . ASN B 2 139 ? 56.549 50.987 38.456 1.00 29.10 ? 363 ASN B OD1 1 ATOM 2515 N ND2 . ASN B 2 139 ? 55.576 51.156 40.469 1.00 35.79 ? 363 ASN B ND2 1 ATOM 2516 N N . HIS B 2 140 ? 59.918 47.232 38.966 1.00 27.88 ? 364 HIS B N 1 ATOM 2517 C CA . HIS B 2 140 ? 60.915 46.362 39.616 1.00 30.04 ? 364 HIS B CA 1 ATOM 2518 C C . HIS B 2 140 ? 61.917 45.799 38.639 1.00 26.98 ? 364 HIS B C 1 ATOM 2519 O O . HIS B 2 140 ? 63.132 45.880 38.867 1.00 22.73 ? 364 HIS B O 1 ATOM 2520 C CB . HIS B 2 140 ? 60.203 45.209 40.391 1.00 29.77 ? 364 HIS B CB 1 ATOM 2521 C CG . HIS B 2 140 ? 61.150 44.278 41.128 1.00 43.49 ? 364 HIS B CG 1 ATOM 2522 N ND1 . HIS B 2 140 ? 61.749 43.201 40.548 1.00 46.64 ? 364 HIS B ND1 1 ATOM 2523 C CD2 . HIS B 2 140 ? 61.579 44.284 42.466 1.00 52.55 ? 364 HIS B CD2 1 ATOM 2524 C CE1 . HIS B 2 140 ? 62.536 42.580 41.447 1.00 48.50 ? 364 HIS B CE1 1 ATOM 2525 N NE2 . HIS B 2 140 ? 62.429 43.245 42.624 1.00 49.67 ? 364 HIS B NE2 1 ATOM 2526 N N . SER B 2 141 ? 61.439 45.128 37.575 1.00 24.73 ? 365 SER B N 1 ATOM 2527 C CA . SER B 2 141 ? 62.403 44.407 36.687 1.00 26.45 ? 365 SER B CA 1 ATOM 2528 C C . SER B 2 141 ? 61.753 43.772 35.478 1.00 25.45 ? 365 SER B C 1 ATOM 2529 O O . SER B 2 141 ? 60.568 43.351 35.532 1.00 24.83 ? 365 SER B O 1 ATOM 2530 C CB . SER B 2 141 ? 63.158 43.250 37.454 1.00 27.07 ? 365 SER B CB 1 ATOM 2531 O OG . SER B 2 141 ? 62.198 42.317 37.936 1.00 33.06 ? 365 SER B OG 1 ATOM 2532 N N . LEU B 2 142 ? 62.552 43.608 34.421 1.00 21.96 ? 366 LEU B N 1 ATOM 2533 C CA . LEU B 2 142 ? 62.161 42.720 33.297 1.00 24.95 ? 366 LEU B CA 1 ATOM 2534 C C . LEU B 2 142 ? 63.075 41.558 33.387 1.00 23.27 ? 366 LEU B C 1 ATOM 2535 O O . LEU B 2 142 ? 64.272 41.702 33.071 1.00 24.73 ? 366 LEU B O 1 ATOM 2536 C CB . LEU B 2 142 ? 62.363 43.433 31.935 1.00 21.04 ? 366 LEU B CB 1 ATOM 2537 C CG . LEU B 2 142 ? 61.641 44.794 31.730 1.00 23.23 ? 366 LEU B CG 1 ATOM 2538 C CD1 . LEU B 2 142 ? 61.877 45.301 30.262 1.00 19.81 ? 366 LEU B CD1 1 ATOM 2539 C CD2 . LEU B 2 142 ? 60.158 44.697 32.079 1.00 22.28 ? 366 LEU B CD2 1 ATOM 2540 N N . ASP B 2 143 ? 62.578 40.430 33.883 1.00 22.71 ? 367 ASP B N 1 ATOM 2541 C CA . ASP B 2 143 ? 63.515 39.322 34.170 1.00 25.93 ? 367 ASP B CA 1 ATOM 2542 C C . ASP B 2 143 ? 63.974 38.612 32.935 1.00 27.16 ? 367 ASP B C 1 ATOM 2543 O O . ASP B 2 143 ? 63.393 38.765 31.830 1.00 24.65 ? 367 ASP B O 1 ATOM 2544 C CB . ASP B 2 143 ? 62.804 38.318 35.038 1.00 26.65 ? 367 ASP B CB 1 ATOM 2545 C CG . ASP B 2 143 ? 62.576 38.841 36.459 1.00 38.69 ? 367 ASP B CG 1 ATOM 2546 O OD1 . ASP B 2 143 ? 63.258 39.819 36.886 1.00 41.89 ? 367 ASP B OD1 1 ATOM 2547 O OD2 . ASP B 2 143 ? 61.730 38.235 37.186 1.00 47.13 ? 367 ASP B OD2 1 ATOM 2548 N N . GLU B 2 144 ? 65.015 37.796 33.085 1.00 24.86 ? 368 GLU B N 1 ATOM 2549 C CA . GLU B 2 144 ? 65.539 37.074 31.986 1.00 25.59 ? 368 GLU B CA 1 ATOM 2550 C C . GLU B 2 144 ? 64.386 36.247 31.380 1.00 24.73 ? 368 GLU B C 1 ATOM 2551 O O . GLU B 2 144 ? 63.554 35.711 32.138 1.00 23.29 ? 368 GLU B O 1 ATOM 2552 C CB . GLU B 2 144 ? 66.569 36.060 32.485 1.00 30.78 ? 368 GLU B CB 1 ATOM 2553 C CG . GLU B 2 144 ? 67.383 35.583 31.280 1.00 37.49 ? 368 GLU B CG 1 ATOM 2554 C CD . GLU B 2 144 ? 68.516 34.687 31.688 1.00 58.92 ? 368 GLU B CD 1 ATOM 2555 O OE1 . GLU B 2 144 ? 69.513 35.203 32.247 1.00 63.40 ? 368 GLU B OE1 1 ATOM 2556 O OE2 . GLU B 2 144 ? 68.387 33.463 31.471 1.00 69.36 ? 368 GLU B OE2 1 ATOM 2557 N N . GLY B 2 145 ? 64.326 36.152 30.049 1.00 24.56 ? 369 GLY B N 1 ATOM 2558 C CA . GLY B 2 145 ? 63.187 35.441 29.433 1.00 23.99 ? 369 GLY B CA 1 ATOM 2559 C C . GLY B 2 145 ? 62.059 36.399 28.981 1.00 21.69 ? 369 GLY B C 1 ATOM 2560 O O . GLY B 2 145 ? 61.124 35.931 28.348 1.00 21.55 ? 369 GLY B O 1 ATOM 2561 N N . THR B 2 146 ? 62.080 37.675 29.362 1.00 20.62 ? 370 THR B N 1 ATOM 2562 C CA . THR B 2 146 ? 60.966 38.562 28.993 1.00 20.14 ? 370 THR B CA 1 ATOM 2563 C C . THR B 2 146 ? 60.765 38.615 27.477 1.00 19.18 ? 370 THR B C 1 ATOM 2564 O O . THR B 2 146 ? 59.644 38.501 26.992 1.00 20.76 ? 370 THR B O 1 ATOM 2565 C CB . THR B 2 146 ? 61.223 40.008 29.483 1.00 20.04 ? 370 THR B CB 1 ATOM 2566 O OG1 . THR B 2 146 ? 61.217 39.998 30.915 1.00 20.16 ? 370 THR B OG1 1 ATOM 2567 C CG2 . THR B 2 146 ? 60.166 41.004 28.949 1.00 18.09 ? 370 THR B CG2 1 ATOM 2568 N N . LEU B 2 147 ? 61.857 38.780 26.719 1.00 18.07 ? 371 LEU B N 1 ATOM 2569 C CA . LEU B 2 147 ? 61.728 38.919 25.271 1.00 18.52 ? 371 LEU B CA 1 ATOM 2570 C C . LEU B 2 147 ? 62.630 37.930 24.522 1.00 21.44 ? 371 LEU B C 1 ATOM 2571 O O . LEU B 2 147 ? 63.868 37.943 24.726 1.00 20.60 ? 371 LEU B O 1 ATOM 2572 C CB . LEU B 2 147 ? 62.079 40.364 24.851 1.00 18.82 ? 371 LEU B CB 1 ATOM 2573 C CG . LEU B 2 147 ? 61.970 40.584 23.304 1.00 18.91 ? 371 LEU B CG 1 ATOM 2574 C CD1 . LEU B 2 147 ? 60.488 40.462 22.867 1.00 16.57 ? 371 LEU B CD1 1 ATOM 2575 C CD2 . LEU B 2 147 ? 62.491 42.047 22.994 1.00 14.87 ? 371 LEU B CD2 1 ATOM 2576 N N . TYR B 2 148 ? 62.024 37.085 23.687 1.00 19.52 ? 372 TYR B N 1 ATOM 2577 C CA . TYR B 2 148 ? 62.758 36.323 22.700 1.00 20.27 ? 372 TYR B CA 1 ATOM 2578 C C . TYR B 2 148 ? 62.399 36.815 21.311 1.00 22.44 ? 372 TYR B C 1 ATOM 2579 O O . TYR B 2 148 ? 61.255 37.084 21.042 1.00 19.66 ? 372 TYR B O 1 ATOM 2580 C CB . TYR B 2 148 ? 62.365 34.855 22.801 1.00 20.10 ? 372 TYR B CB 1 ATOM 2581 C CG . TYR B 2 148 ? 63.248 34.136 23.789 1.00 21.49 ? 372 TYR B CG 1 ATOM 2582 C CD1 . TYR B 2 148 ? 62.925 34.137 25.140 1.00 20.52 ? 372 TYR B CD1 1 ATOM 2583 C CD2 . TYR B 2 148 ? 64.374 33.450 23.364 1.00 26.29 ? 372 TYR B CD2 1 ATOM 2584 C CE1 . TYR B 2 148 ? 63.720 33.446 26.087 1.00 23.46 ? 372 TYR B CE1 1 ATOM 2585 C CE2 . TYR B 2 148 ? 65.206 32.786 24.285 1.00 24.37 ? 372 TYR B CE2 1 ATOM 2586 C CZ . TYR B 2 148 ? 64.874 32.833 25.616 1.00 25.66 ? 372 TYR B CZ 1 ATOM 2587 O OH . TYR B 2 148 ? 65.662 32.193 26.522 1.00 30.51 ? 372 TYR B OH 1 ATOM 2588 N N . ILE B 2 149 ? 63.384 36.908 20.441 1.00 18.15 ? 373 ILE B N 1 ATOM 2589 C CA . ILE B 2 149 ? 63.202 37.270 19.051 1.00 16.82 ? 373 ILE B CA 1 ATOM 2590 C C . ILE B 2 149 ? 63.534 36.023 18.215 1.00 22.83 ? 373 ILE B C 1 ATOM 2591 O O . ILE B 2 149 ? 64.636 35.435 18.346 1.00 20.26 ? 373 ILE B O 1 ATOM 2592 C CB . ILE B 2 149 ? 64.170 38.434 18.662 1.00 14.70 ? 373 ILE B CB 1 ATOM 2593 C CG1 . ILE B 2 149 ? 63.922 39.681 19.553 1.00 17.07 ? 373 ILE B CG1 1 ATOM 2594 C CG2 . ILE B 2 149 ? 63.992 38.834 17.175 1.00 15.88 ? 373 ILE B CG2 1 ATOM 2595 C CD1 . ILE B 2 149 ? 62.449 40.240 19.545 1.00 19.49 ? 373 ILE B CD1 1 ATOM 2596 N N . VAL B 2 150 ? 62.541 35.561 17.432 1.00 20.91 ? 374 VAL B N 1 ATOM 2597 C CA . VAL B 2 150 ? 62.637 34.378 16.613 1.00 20.78 ? 374 VAL B CA 1 ATOM 2598 C C . VAL B 2 150 ? 62.517 34.725 15.113 1.00 22.35 ? 374 VAL B C 1 ATOM 2599 O O . VAL B 2 150 ? 61.560 35.407 14.711 1.00 21.12 ? 374 VAL B O 1 ATOM 2600 C CB . VAL B 2 150 ? 61.513 33.361 17.049 1.00 17.66 ? 374 VAL B CB 1 ATOM 2601 C CG1 . VAL B 2 150 ? 61.631 32.024 16.309 1.00 19.66 ? 374 VAL B CG1 1 ATOM 2602 C CG2 . VAL B 2 150 ? 61.482 33.202 18.580 1.00 17.08 ? 374 VAL B CG2 1 ATOM 2603 N N . GLU B 2 151 ? 63.476 34.277 14.260 1.00 17.92 ? 375 GLU B N 1 ATOM 2604 C CA . GLU B 2 151 ? 63.409 34.622 12.831 1.00 17.40 ? 375 GLU B CA 1 ATOM 2605 C C . GLU B 2 151 ? 63.571 33.414 11.976 1.00 22.43 ? 375 GLU B C 1 ATOM 2606 O O . GLU B 2 151 ? 64.547 32.618 12.208 1.00 21.16 ? 375 GLU B O 1 ATOM 2607 C CB . GLU B 2 151 ? 64.490 35.675 12.466 1.00 20.06 ? 375 GLU B CB 1 ATOM 2608 C CG . GLU B 2 151 ? 64.078 37.071 13.055 1.00 20.10 ? 375 GLU B CG 1 ATOM 2609 C CD . GLU B 2 151 ? 65.109 38.161 12.850 1.00 23.06 ? 375 GLU B CD 1 ATOM 2610 O OE1 . GLU B 2 151 ? 66.348 37.866 12.839 1.00 21.36 ? 375 GLU B OE1 1 ATOM 2611 O OE2 . GLU B 2 151 ? 64.664 39.331 12.667 1.00 20.63 ? 375 GLU B OE2 1 ATOM 2612 N N . GLN B 2 152 ? 62.662 33.257 10.985 1.00 20.86 ? 376 GLN B N 1 ATOM 2613 C CA . GLN B 2 152 ? 62.648 32.014 10.231 1.00 20.38 ? 376 GLN B CA 1 ATOM 2614 C C . GLN B 2 152 ? 63.056 32.317 8.801 1.00 22.67 ? 376 GLN B C 1 ATOM 2615 O O . GLN B 2 152 ? 62.615 33.307 8.241 1.00 25.21 ? 376 GLN B O 1 ATOM 2616 C CB . GLN B 2 152 ? 61.244 31.430 10.252 1.00 19.20 ? 376 GLN B CB 1 ATOM 2617 C CG . GLN B 2 152 ? 61.062 30.237 9.268 1.00 21.63 ? 376 GLN B CG 1 ATOM 2618 C CD . GLN B 2 152 ? 59.629 30.086 8.898 1.00 19.93 ? 376 GLN B CD 1 ATOM 2619 O OE1 . GLN B 2 152 ? 58.746 29.746 9.742 1.00 22.66 ? 376 GLN B OE1 1 ATOM 2620 N NE2 . GLN B 2 152 ? 59.348 30.330 7.608 1.00 20.23 ? 376 GLN B NE2 1 ATOM 2621 N N . ILE B 2 153 ? 63.925 31.495 8.206 1.00 18.96 ? 377 ILE B N 1 ATOM 2622 C CA . ILE B 2 153 ? 64.108 31.472 6.739 1.00 19.16 ? 377 ILE B CA 1 ATOM 2623 C C . ILE B 2 153 ? 64.100 29.943 6.354 1.00 20.92 ? 377 ILE B C 1 ATOM 2624 O O . ILE B 2 153 ? 64.007 29.098 7.238 1.00 23.18 ? 377 ILE B O 1 ATOM 2625 C CB . ILE B 2 153 ? 65.428 32.173 6.318 1.00 20.55 ? 377 ILE B CB 1 ATOM 2626 C CG1 . ILE B 2 153 ? 66.646 31.477 6.975 1.00 21.95 ? 377 ILE B CG1 1 ATOM 2627 C CG2 . ILE B 2 153 ? 65.383 33.717 6.574 1.00 20.62 ? 377 ILE B CG2 1 ATOM 2628 C CD1 . ILE B 2 153 ? 67.921 32.177 6.554 1.00 23.20 ? 377 ILE B CD1 1 ATOM 2629 N N . PRO B 2 154 ? 64.100 29.612 5.053 1.00 22.39 ? 378 PRO B N 1 ATOM 2630 C CA . PRO B 2 154 ? 64.088 28.167 4.694 1.00 25.69 ? 378 PRO B CA 1 ATOM 2631 C C . PRO B 2 154 ? 65.336 27.499 5.311 1.00 24.20 ? 378 PRO B C 1 ATOM 2632 O O . PRO B 2 154 ? 66.405 28.101 5.311 1.00 22.98 ? 378 PRO B O 1 ATOM 2633 C CB . PRO B 2 154 ? 64.151 28.173 3.163 1.00 22.29 ? 378 PRO B CB 1 ATOM 2634 C CG . PRO B 2 154 ? 63.523 29.488 2.771 1.00 22.24 ? 378 PRO B CG 1 ATOM 2635 C CD . PRO B 2 154 ? 63.988 30.470 3.854 1.00 22.70 ? 378 PRO B CD 1 ATOM 2636 N N . THR B 2 155 ? 65.147 26.335 5.906 1.00 24.77 ? 379 THR B N 1 ATOM 2637 C CA . THR B 2 155 ? 66.241 25.511 6.530 1.00 26.93 ? 379 THR B CA 1 ATOM 2638 C C . THR B 2 155 ? 66.780 26.028 7.864 1.00 34.08 ? 379 THR B C 1 ATOM 2639 O O . THR B 2 155 ? 67.576 25.337 8.472 1.00 27.24 ? 379 THR B O 1 ATOM 2640 C CB . THR B 2 155 ? 67.458 25.246 5.589 1.00 29.83 ? 379 THR B CB 1 ATOM 2641 O OG1 . THR B 2 155 ? 68.416 26.346 5.565 1.00 30.25 ? 379 THR B OG1 1 ATOM 2642 C CG2 . THR B 2 155 ? 66.965 24.963 4.185 1.00 31.89 ? 379 THR B CG2 1 ATOM 2643 N N . TYR B 2 156 ? 66.359 27.217 8.352 1.00 28.07 ? 380 TYR B N 1 ATOM 2644 C CA . TYR B 2 156 ? 67.061 27.765 9.496 1.00 28.07 ? 380 TYR B CA 1 ATOM 2645 C C . TYR B 2 156 ? 66.177 28.701 10.335 1.00 27.43 ? 380 TYR B C 1 ATOM 2646 O O . TYR B 2 156 ? 65.637 29.681 9.790 1.00 24.86 ? 380 TYR B O 1 ATOM 2647 C CB . TYR B 2 156 ? 68.280 28.538 8.982 1.00 28.29 ? 380 TYR B CB 1 ATOM 2648 C CG . TYR B 2 156 ? 69.134 29.166 10.079 1.00 35.11 ? 380 TYR B CG 1 ATOM 2649 C CD1 . TYR B 2 156 ? 69.789 28.387 11.065 1.00 34.16 ? 380 TYR B CD1 1 ATOM 2650 C CD2 . TYR B 2 156 ? 69.323 30.552 10.096 1.00 28.90 ? 380 TYR B CD2 1 ATOM 2651 C CE1 . TYR B 2 156 ? 70.599 29.015 12.069 1.00 33.40 ? 380 TYR B CE1 1 ATOM 2652 C CE2 . TYR B 2 156 ? 70.117 31.186 11.067 1.00 32.05 ? 380 TYR B CE2 1 ATOM 2653 C CZ . TYR B 2 156 ? 70.749 30.407 12.042 1.00 34.59 ? 380 TYR B CZ 1 ATOM 2654 O OH . TYR B 2 156 ? 71.491 31.097 12.982 1.00 34.66 ? 380 TYR B OH 1 ATOM 2655 N N . VAL B 2 157 ? 66.052 28.432 11.635 1.00 25.39 ? 381 VAL B N 1 ATOM 2656 C CA . VAL B 2 157 ? 65.404 29.412 12.534 1.00 26.56 ? 381 VAL B CA 1 ATOM 2657 C C . VAL B 2 157 ? 66.444 29.851 13.527 1.00 29.49 ? 381 VAL B C 1 ATOM 2658 O O . VAL B 2 157 ? 67.054 29.025 14.199 1.00 26.90 ? 381 VAL B O 1 ATOM 2659 C CB . VAL B 2 157 ? 64.184 28.755 13.244 1.00 24.50 ? 381 VAL B CB 1 ATOM 2660 C CG1 . VAL B 2 157 ? 63.623 29.627 14.351 1.00 24.01 ? 381 VAL B CG1 1 ATOM 2661 C CG2 . VAL B 2 157 ? 63.120 28.419 12.209 1.00 21.62 ? 381 VAL B CG2 1 ATOM 2662 N N . GLU B 2 158 ? 66.681 31.151 13.658 1.00 22.64 ? 382 GLU B N 1 ATOM 2663 C CA . GLU B 2 158 ? 67.555 31.631 14.716 1.00 21.86 ? 382 GLU B CA 1 ATOM 2664 C C . GLU B 2 158 ? 66.748 32.331 15.789 1.00 24.16 ? 382 GLU B C 1 ATOM 2665 O O . GLU B 2 158 ? 65.703 33.033 15.458 1.00 22.47 ? 382 GLU B O 1 ATOM 2666 C CB . GLU B 2 158 ? 68.661 32.563 14.098 1.00 22.23 ? 382 GLU B CB 1 ATOM 2667 C CG . GLU B 2 158 ? 69.607 33.221 15.166 1.00 25.33 ? 382 GLU B CG 1 ATOM 2668 C CD . GLU B 2 158 ? 70.850 33.817 14.558 1.00 28.61 ? 382 GLU B CD 1 ATOM 2669 O OE1 . GLU B 2 158 ? 71.033 33.719 13.333 1.00 29.93 ? 382 GLU B OE1 1 ATOM 2670 O OE2 . GLU B 2 158 ? 71.615 34.489 15.259 1.00 24.87 ? 382 GLU B OE2 1 ATOM 2671 N N . TYR B 2 159 ? 67.100 32.168 17.047 1.00 20.50 ? 383 TYR B N 1 ATOM 2672 C CA . TYR B 2 159 ? 66.339 32.907 18.096 1.00 23.32 ? 383 TYR B CA 1 ATOM 2673 C C . TYR B 2 159 ? 67.334 33.363 19.167 1.00 28.54 ? 383 TYR B C 1 ATOM 2674 O O . TYR B 2 159 ? 68.409 32.733 19.356 1.00 22.02 ? 383 TYR B O 1 ATOM 2675 C CB . TYR B 2 159 ? 65.178 32.060 18.660 1.00 26.06 ? 383 TYR B CB 1 ATOM 2676 C CG . TYR B 2 159 ? 65.607 30.836 19.429 1.00 31.05 ? 383 TYR B CG 1 ATOM 2677 C CD1 . TYR B 2 159 ? 66.004 30.976 20.748 1.00 35.13 ? 383 TYR B CD1 1 ATOM 2678 C CD2 . TYR B 2 159 ? 65.701 29.565 18.828 1.00 36.91 ? 383 TYR B CD2 1 ATOM 2679 C CE1 . TYR B 2 159 ? 66.416 29.893 21.509 1.00 40.48 ? 383 TYR B CE1 1 ATOM 2680 C CE2 . TYR B 2 159 ? 66.087 28.454 19.608 1.00 38.01 ? 383 TYR B CE2 1 ATOM 2681 C CZ . TYR B 2 159 ? 66.444 28.641 20.944 1.00 37.94 ? 383 TYR B CZ 1 ATOM 2682 O OH . TYR B 2 159 ? 66.883 27.643 21.821 1.00 48.38 ? 383 TYR B OH 1 ATOM 2683 N N . SER B 2 160 ? 67.063 34.475 19.836 1.00 21.24 ? 384 SER B N 1 ATOM 2684 C CA . SER B 2 160 ? 67.904 34.878 20.942 1.00 21.44 ? 384 SER B CA 1 ATOM 2685 C C . SER B 2 160 ? 67.109 35.648 21.971 1.00 23.53 ? 384 SER B C 1 ATOM 2686 O O . SER B 2 160 ? 65.983 36.141 21.678 1.00 19.89 ? 384 SER B O 1 ATOM 2687 C CB . SER B 2 160 ? 69.075 35.745 20.418 1.00 21.85 ? 384 SER B CB 1 ATOM 2688 O OG . SER B 2 160 ? 68.523 36.929 19.793 1.00 22.04 ? 384 SER B OG 1 ATOM 2689 N N . GLU B 2 161 ? 67.664 35.768 23.183 1.00 19.78 ? 385 GLU B N 1 ATOM 2690 C CA . GLU B 2 161 ? 66.977 36.430 24.259 1.00 22.33 ? 385 GLU B CA 1 ATOM 2691 C C . GLU B 2 161 ? 67.360 37.917 24.157 1.00 21.59 ? 385 GLU B C 1 ATOM 2692 O O . GLU B 2 161 ? 68.541 38.227 24.033 1.00 19.98 ? 385 GLU B O 1 ATOM 2693 C CB . GLU B 2 161 ? 67.359 35.749 25.637 1.00 22.49 ? 385 GLU B CB 1 ATOM 2694 C CG . GLU B 2 161 ? 66.327 36.019 26.751 1.00 24.81 ? 385 GLU B CG 1 ATOM 2695 C CD . GLU B 2 161 ? 66.589 37.291 27.511 1.00 25.81 ? 385 GLU B CD 1 ATOM 2696 O OE1 . GLU B 2 161 ? 67.499 38.055 27.124 1.00 27.42 ? 385 GLU B OE1 1 ATOM 2697 O OE2 . GLU B 2 161 ? 65.950 37.577 28.540 1.00 25.35 ? 385 GLU B OE2 1 ATOM 2698 N N . GLN B 2 162 ? 66.359 38.836 24.129 1.00 19.71 ? 386 GLN B N 1 ATOM 2699 C CA . GLN B 2 162 ? 66.683 40.246 23.916 1.00 18.04 ? 386 GLN B CA 1 ATOM 2700 C C . GLN B 2 162 ? 66.134 41.178 24.974 1.00 18.47 ? 386 GLN B C 1 ATOM 2701 O O . GLN B 2 162 ? 65.920 42.347 24.704 1.00 17.68 ? 386 GLN B O 1 ATOM 2702 C CB . GLN B 2 162 ? 66.359 40.744 22.473 1.00 19.60 ? 386 GLN B CB 1 ATOM 2703 C CG . GLN B 2 162 ? 67.114 40.000 21.366 1.00 19.01 ? 386 GLN B CG 1 ATOM 2704 C CD . GLN B 2 162 ? 68.594 40.351 21.307 1.00 19.66 ? 386 GLN B CD 1 ATOM 2705 O OE1 . GLN B 2 162 ? 69.009 41.469 21.729 1.00 22.64 ? 386 GLN B OE1 1 ATOM 2706 N NE2 . GLN B 2 162 ? 69.441 39.362 20.849 1.00 18.34 ? 386 GLN B NE2 1 ATOM 2707 N N . THR B 2 163 ? 66.052 40.676 26.198 1.00 20.18 ? 387 THR B N 1 ATOM 2708 C CA . THR B 2 163 ? 65.516 41.507 27.283 1.00 21.14 ? 387 THR B CA 1 ATOM 2709 C C . THR B 2 163 ? 66.464 42.680 27.602 1.00 20.77 ? 387 THR B C 1 ATOM 2710 O O . THR B 2 163 ? 65.986 43.750 27.895 1.00 20.17 ? 387 THR B O 1 ATOM 2711 C CB . THR B 2 163 ? 65.200 40.669 28.534 1.00 19.69 ? 387 THR B CB 1 ATOM 2712 O OG1 . THR B 2 163 ? 64.361 39.527 28.162 1.00 21.28 ? 387 THR B OG1 1 ATOM 2713 C CG2 . THR B 2 163 ? 64.549 41.526 29.653 1.00 20.19 ? 387 THR B CG2 1 ATOM 2714 N N . ALA B 2 164 ? 67.777 42.480 27.480 1.00 21.22 ? 388 ALA B N 1 ATOM 2715 C CA . ALA B 2 164 ? 68.662 43.592 27.861 1.00 23.31 ? 388 ALA B CA 1 ATOM 2716 C C . ALA B 2 164 ? 68.423 44.853 26.980 1.00 19.63 ? 388 ALA B C 1 ATOM 2717 O O . ALA B 2 164 ? 68.402 46.010 27.457 1.00 21.88 ? 388 ALA B O 1 ATOM 2718 C CB . ALA B 2 164 ? 70.130 43.105 27.838 1.00 20.40 ? 388 ALA B CB 1 ATOM 2719 N N . VAL B 2 165 ? 68.217 44.648 25.675 1.00 19.93 ? 389 VAL B N 1 ATOM 2720 C CA . VAL B 2 165 ? 67.840 45.755 24.738 1.00 24.97 ? 389 VAL B CA 1 ATOM 2721 C C . VAL B 2 165 ? 66.542 46.378 25.174 1.00 21.60 ? 389 VAL B C 1 ATOM 2722 O O . VAL B 2 165 ? 66.425 47.591 25.212 1.00 19.33 ? 389 VAL B O 1 ATOM 2723 C CB . VAL B 2 165 ? 67.606 45.230 23.243 1.00 24.35 ? 389 VAL B CB 1 ATOM 2724 C CG1 . VAL B 2 165 ? 66.992 46.310 22.329 1.00 29.03 ? 389 VAL B CG1 1 ATOM 2725 C CG2 . VAL B 2 165 ? 68.951 44.897 22.723 1.00 33.41 ? 389 VAL B CG2 1 ATOM 2726 N N . LEU B 2 166 ? 65.546 45.529 25.403 1.00 17.91 ? 390 LEU B N 1 ATOM 2727 C CA . LEU B 2 166 ? 64.205 46.043 25.772 1.00 19.52 ? 390 LEU B CA 1 ATOM 2728 C C . LEU B 2 166 ? 64.246 46.883 27.103 1.00 21.95 ? 390 LEU B C 1 ATOM 2729 O O . LEU B 2 166 ? 63.562 47.943 27.232 1.00 21.35 ? 390 LEU B O 1 ATOM 2730 C CB . LEU B 2 166 ? 63.253 44.883 25.980 1.00 18.15 ? 390 LEU B CB 1 ATOM 2731 C CG . LEU B 2 166 ? 61.838 45.351 26.420 1.00 20.37 ? 390 LEU B CG 1 ATOM 2732 C CD1 . LEU B 2 166 ? 61.222 46.314 25.399 1.00 17.41 ? 390 LEU B CD1 1 ATOM 2733 C CD2 . LEU B 2 166 ? 60.950 44.114 26.585 1.00 21.81 ? 390 LEU B CD2 1 ATOM 2734 N N . ARG B 2 167 ? 65.072 46.436 28.073 1.00 20.73 ? 391 ARG B N 1 ATOM 2735 C CA . ARG B 2 167 ? 65.308 47.257 29.293 1.00 23.27 ? 391 ARG B CA 1 ATOM 2736 C C . ARG B 2 167 ? 65.780 48.687 28.999 1.00 19.90 ? 391 ARG B C 1 ATOM 2737 O O . ARG B 2 167 ? 65.482 49.566 29.823 1.00 22.79 ? 391 ARG B O 1 ATOM 2738 C CB . ARG B 2 167 ? 66.302 46.580 30.294 1.00 21.57 ? 391 ARG B CB 1 ATOM 2739 C CG . ARG B 2 167 ? 65.810 45.259 30.901 1.00 22.33 ? 391 ARG B CG 1 ATOM 2740 C CD . ARG B 2 167 ? 66.989 44.643 31.682 1.00 23.97 ? 391 ARG B CD 1 ATOM 2741 N NE . ARG B 2 167 ? 66.601 43.312 32.142 1.00 23.41 ? 391 ARG B NE 1 ATOM 2742 C CZ . ARG B 2 167 ? 67.300 42.214 31.883 1.00 27.72 ? 391 ARG B CZ 1 ATOM 2743 N NH1 . ARG B 2 167 ? 68.450 42.316 31.195 1.00 27.32 ? 391 ARG B NH1 1 ATOM 2744 N NH2 . ARG B 2 167 ? 66.832 41.010 32.281 1.00 23.12 ? 391 ARG B NH2 1 ATOM 2745 N N . ARG B 2 168 ? 66.445 48.931 27.879 1.00 21.12 ? 392 ARG B N 1 ATOM 2746 C CA . ARG B 2 168 ? 66.830 50.358 27.455 1.00 22.03 ? 392 ARG B CA 1 ATOM 2747 C C . ARG B 2 168 ? 65.655 51.213 27.014 1.00 23.95 ? 392 ARG B C 1 ATOM 2748 O O . ARG B 2 168 ? 65.718 52.449 27.042 1.00 23.46 ? 392 ARG B O 1 ATOM 2749 C CB . ARG B 2 168 ? 67.844 50.340 26.380 1.00 21.72 ? 392 ARG B CB 1 ATOM 2750 C CG . ARG B 2 168 ? 69.167 49.655 26.854 1.00 20.57 ? 392 ARG B CG 1 ATOM 2751 C CD . ARG B 2 168 ? 69.957 50.250 28.058 1.00 21.48 ? 392 ARG B CD 1 ATOM 2752 N NE . ARG B 2 168 ? 71.203 49.435 28.250 1.00 20.92 ? 392 ARG B NE 1 ATOM 2753 C CZ . ARG B 2 168 ? 72.100 49.619 29.193 1.00 23.35 ? 392 ARG B CZ 1 ATOM 2754 N NH1 . ARG B 2 168 ? 71.927 50.587 30.112 1.00 23.94 ? 392 ARG B NH1 1 ATOM 2755 N NH2 . ARG B 2 168 ? 73.134 48.780 29.297 1.00 20.22 ? 392 ARG B NH2 1 ATOM 2756 N N . GLY B 2 169 ? 64.543 50.555 26.682 1.00 23.68 ? 393 GLY B N 1 ATOM 2757 C CA . GLY B 2 169 ? 63.318 51.295 26.355 1.00 25.37 ? 393 GLY B CA 1 ATOM 2758 C C . GLY B 2 169 ? 62.382 50.684 25.326 1.00 25.55 ? 393 GLY B C 1 ATOM 2759 O O . GLY B 2 169 ? 61.169 50.882 25.428 1.00 20.98 ? 393 GLY B O 1 ATOM 2760 N N . TYR B 2 170 ? 62.907 49.914 24.356 1.00 20.21 ? 394 TYR B N 1 ATOM 2761 C CA . TYR B 2 170 ? 61.989 49.463 23.328 1.00 19.45 ? 394 TYR B CA 1 ATOM 2762 C C . TYR B 2 170 ? 62.561 48.388 22.431 1.00 19.90 ? 394 TYR B C 1 ATOM 2763 O O . TYR B 2 170 ? 63.760 48.235 22.319 1.00 21.23 ? 394 TYR B O 1 ATOM 2764 C CB . TYR B 2 170 ? 61.548 50.622 22.384 1.00 18.71 ? 394 TYR B CB 1 ATOM 2765 C CG . TYR B 2 170 ? 62.622 51.125 21.400 1.00 20.15 ? 394 TYR B CG 1 ATOM 2766 C CD1 . TYR B 2 170 ? 63.829 51.696 21.873 1.00 21.35 ? 394 TYR B CD1 1 ATOM 2767 C CD2 . TYR B 2 170 ? 62.414 51.036 19.988 1.00 21.68 ? 394 TYR B CD2 1 ATOM 2768 C CE1 . TYR B 2 170 ? 64.800 52.169 21.003 1.00 19.88 ? 394 TYR B CE1 1 ATOM 2769 C CE2 . TYR B 2 170 ? 63.381 51.533 19.068 1.00 18.46 ? 394 TYR B CE2 1 ATOM 2770 C CZ . TYR B 2 170 ? 64.579 52.004 19.589 1.00 18.74 ? 394 TYR B CZ 1 ATOM 2771 O OH . TYR B 2 170 ? 65.501 52.543 18.712 1.00 19.42 ? 394 TYR B OH 1 ATOM 2772 N N . TRP B 2 171 ? 61.644 47.714 21.743 1.00 17.31 ? 395 TRP B N 1 ATOM 2773 C CA . TRP B 2 171 ? 62.029 46.782 20.656 1.00 18.30 ? 395 TRP B CA 1 ATOM 2774 C C . TRP B 2 171 ? 61.143 47.155 19.499 1.00 16.39 ? 395 TRP B C 1 ATOM 2775 O O . TRP B 2 171 ? 59.901 46.829 19.544 1.00 16.87 ? 395 TRP B O 1 ATOM 2776 C CB . TRP B 2 171 ? 61.733 45.289 21.054 1.00 15.02 ? 395 TRP B CB 1 ATOM 2777 C CG . TRP B 2 171 ? 62.111 44.429 19.869 1.00 18.85 ? 395 TRP B CG 1 ATOM 2778 C CD1 . TRP B 2 171 ? 61.370 44.119 18.735 1.00 17.09 ? 395 TRP B CD1 1 ATOM 2779 C CD2 . TRP B 2 171 ? 63.494 43.869 19.628 1.00 16.23 ? 395 TRP B CD2 1 ATOM 2780 N NE1 . TRP B 2 171 ? 62.153 43.393 17.833 1.00 19.00 ? 395 TRP B NE1 1 ATOM 2781 C CE2 . TRP B 2 171 ? 63.462 43.301 18.281 1.00 19.42 ? 395 TRP B CE2 1 ATOM 2782 C CE3 . TRP B 2 171 ? 64.736 43.946 20.345 1.00 17.62 ? 395 TRP B CE3 1 ATOM 2783 C CZ2 . TRP B 2 171 ? 64.627 42.662 17.697 1.00 17.47 ? 395 TRP B CZ2 1 ATOM 2784 C CZ3 . TRP B 2 171 ? 65.864 43.381 19.779 1.00 18.01 ? 395 TRP B CZ3 1 ATOM 2785 C CH2 . TRP B 2 171 ? 65.812 42.710 18.502 1.00 17.49 ? 395 TRP B CH2 1 ATOM 2786 N N . PRO B 2 172 ? 61.718 47.562 18.402 1.00 17.48 ? 396 PRO B N 1 ATOM 2787 C CA . PRO B 2 172 ? 60.967 47.862 17.156 1.00 18.68 ? 396 PRO B CA 1 ATOM 2788 C C . PRO B 2 172 ? 61.009 46.756 16.096 1.00 21.23 ? 396 PRO B C 1 ATOM 2789 O O . PRO B 2 172 ? 61.911 45.920 16.096 1.00 18.62 ? 396 PRO B O 1 ATOM 2790 C CB . PRO B 2 172 ? 61.759 49.033 16.553 1.00 17.93 ? 396 PRO B CB 1 ATOM 2791 C CG . PRO B 2 172 ? 63.199 48.677 16.933 1.00 18.01 ? 396 PRO B CG 1 ATOM 2792 C CD . PRO B 2 172 ? 63.161 47.876 18.262 1.00 14.85 ? 396 PRO B CD 1 ATOM 2793 N N . SER B 2 173 ? 59.996 46.704 15.215 1.00 19.43 ? 397 SER B N 1 ATOM 2794 C CA . SER B 2 173 ? 60.037 45.637 14.158 1.00 17.96 ? 397 SER B CA 1 ATOM 2795 C C . SER B 2 173 ? 59.388 46.201 12.903 1.00 21.60 ? 397 SER B C 1 ATOM 2796 O O . SER B 2 173 ? 58.329 46.813 13.031 1.00 20.50 ? 397 SER B O 1 ATOM 2797 C CB . SER B 2 173 ? 59.222 44.445 14.610 1.00 18.24 ? 397 SER B CB 1 ATOM 2798 O OG . SER B 2 173 ? 59.520 43.311 13.765 1.00 19.42 ? 397 SER B OG 1 ATOM 2799 N N . TYR B 2 174 ? 60.064 46.068 11.749 1.00 18.42 ? 398 TYR B N 1 ATOM 2800 C CA . TYR B 2 174 ? 59.679 46.759 10.512 1.00 19.32 ? 398 TYR B CA 1 ATOM 2801 C C . TYR B 2 174 ? 60.212 46.004 9.297 1.00 19.03 ? 398 TYR B C 1 ATOM 2802 O O . TYR B 2 174 ? 60.723 46.596 8.344 1.00 21.21 ? 398 TYR B O 1 ATOM 2803 C CB . TYR B 2 174 ? 60.239 48.249 10.576 1.00 19.32 ? 398 TYR B CB 1 ATOM 2804 C CG . TYR B 2 174 ? 61.636 48.319 11.195 1.00 18.60 ? 398 TYR B CG 1 ATOM 2805 C CD1 . TYR B 2 174 ? 62.778 48.032 10.414 1.00 20.89 ? 398 TYR B CD1 1 ATOM 2806 C CD2 . TYR B 2 174 ? 61.805 48.661 12.541 1.00 19.37 ? 398 TYR B CD2 1 ATOM 2807 C CE1 . TYR B 2 174 ? 64.056 48.058 10.970 1.00 23.45 ? 398 TYR B CE1 1 ATOM 2808 C CE2 . TYR B 2 174 ? 63.088 48.640 13.134 1.00 20.23 ? 398 TYR B CE2 1 ATOM 2809 C CZ . TYR B 2 174 ? 64.193 48.339 12.334 1.00 21.81 ? 398 TYR B CZ 1 ATOM 2810 O OH . TYR B 2 174 ? 65.465 48.398 12.856 1.00 24.17 ? 398 TYR B OH 1 ATOM 2811 N N . ASN B 2 175 ? 59.979 44.669 9.248 1.00 19.40 ? 399 ASN B N 1 ATOM 2812 C CA . ASN B 2 175 ? 60.159 43.885 8.011 1.00 19.72 ? 399 ASN B CA 1 ATOM 2813 C C . ASN B 2 175 ? 61.636 43.774 7.607 1.00 21.26 ? 399 ASN B C 1 ATOM 2814 O O . ASN B 2 175 ? 61.916 43.501 6.434 1.00 21.94 ? 399 ASN B O 1 ATOM 2815 C CB . ASN B 2 175 ? 59.374 44.490 6.792 1.00 20.50 ? 399 ASN B CB 1 ATOM 2816 C CG . ASN B 2 175 ? 57.934 44.697 7.115 1.00 23.09 ? 399 ASN B CG 1 ATOM 2817 O OD1 . ASN B 2 175 ? 57.390 45.826 7.107 1.00 22.83 ? 399 ASN B OD1 1 ATOM 2818 N ND2 . ASN B 2 175 ? 57.305 43.631 7.463 1.00 20.23 ? 399 ASN B ND2 1 ATOM 2819 N N . ILE B 2 176 ? 62.578 43.978 8.522 1.00 18.88 ? 400 ILE B N 1 ATOM 2820 C CA . ILE B 2 176 ? 64.018 43.716 8.152 1.00 19.81 ? 400 ILE B CA 1 ATOM 2821 C C . ILE B 2 176 ? 64.604 42.824 9.269 1.00 20.31 ? 400 ILE B C 1 ATOM 2822 O O . ILE B 2 176 ? 64.473 43.143 10.430 1.00 19.95 ? 400 ILE B O 1 ATOM 2823 C CB . ILE B 2 176 ? 64.843 45.010 8.042 1.00 22.89 ? 400 ILE B CB 1 ATOM 2824 C CG1 . ILE B 2 176 ? 64.152 45.861 6.983 1.00 25.32 ? 400 ILE B CG1 1 ATOM 2825 C CG2 . ILE B 2 176 ? 66.332 44.791 7.670 1.00 20.50 ? 400 ILE B CG2 1 ATOM 2826 C CD1 . ILE B 2 176 ? 64.755 47.141 6.771 1.00 24.58 ? 400 ILE B CD1 1 ATOM 2827 N N . PRO B 2 177 ? 65.278 41.723 8.903 1.00 17.96 ? 401 PRO B N 1 ATOM 2828 C CA . PRO B 2 177 ? 65.780 40.831 9.953 1.00 19.62 ? 401 PRO B CA 1 ATOM 2829 C C . PRO B 2 177 ? 66.850 41.477 10.832 1.00 17.53 ? 401 PRO B C 1 ATOM 2830 O O . PRO B 2 177 ? 67.740 42.164 10.317 1.00 19.52 ? 401 PRO B O 1 ATOM 2831 C CB . PRO B 2 177 ? 66.456 39.669 9.178 1.00 19.67 ? 401 PRO B CB 1 ATOM 2832 C CG . PRO B 2 177 ? 66.316 39.934 7.765 1.00 20.00 ? 401 PRO B CG 1 ATOM 2833 C CD . PRO B 2 177 ? 65.516 41.238 7.508 1.00 17.13 ? 401 PRO B CD 1 ATOM 2834 N N . PHE B 2 178 ? 66.759 41.182 12.113 1.00 19.49 ? 402 PHE B N 1 ATOM 2835 C CA . PHE B 2 178 ? 67.657 41.625 13.158 1.00 20.29 ? 402 PHE B CA 1 ATOM 2836 C C . PHE B 2 178 ? 68.953 40.727 13.249 1.00 20.21 ? 402 PHE B C 1 ATOM 2837 O O . PHE B 2 178 ? 70.087 41.206 13.341 1.00 20.00 ? 402 PHE B O 1 ATOM 2838 C CB . PHE B 2 178 ? 66.907 41.494 14.489 1.00 17.11 ? 402 PHE B CB 1 ATOM 2839 C CG . PHE B 2 178 ? 67.827 41.488 15.670 1.00 19.30 ? 402 PHE B CG 1 ATOM 2840 C CD1 . PHE B 2 178 ? 68.585 42.613 15.987 1.00 20.42 ? 402 PHE B CD1 1 ATOM 2841 C CD2 . PHE B 2 178 ? 68.002 40.307 16.449 1.00 22.63 ? 402 PHE B CD2 1 ATOM 2842 C CE1 . PHE B 2 178 ? 69.430 42.653 17.100 1.00 21.94 ? 402 PHE B CE1 1 ATOM 2843 C CE2 . PHE B 2 178 ? 68.823 40.349 17.592 1.00 21.63 ? 402 PHE B CE2 1 ATOM 2844 C CZ . PHE B 2 178 ? 69.561 41.488 17.900 1.00 20.86 ? 402 PHE B CZ 1 ATOM 2845 N N . HIS B 2 179 ? 68.773 39.411 13.211 1.00 19.46 ? 403 HIS B N 1 ATOM 2846 C CA . HIS B 2 179 ? 69.987 38.496 13.479 1.00 21.43 ? 403 HIS B CA 1 ATOM 2847 C C . HIS B 2 179 ? 70.868 38.558 12.261 1.00 24.34 ? 403 HIS B C 1 ATOM 2848 O O . HIS B 2 179 ? 70.403 38.441 11.127 1.00 21.35 ? 403 HIS B O 1 ATOM 2849 C CB . HIS B 2 179 ? 69.490 37.069 13.657 1.00 18.84 ? 403 HIS B CB 1 ATOM 2850 C CG . HIS B 2 179 ? 68.826 36.823 14.972 1.00 20.11 ? 403 HIS B CG 1 ATOM 2851 N ND1 . HIS B 2 179 ? 67.498 36.611 15.074 1.00 21.00 ? 403 HIS B ND1 1 ATOM 2852 C CD2 . HIS B 2 179 ? 69.335 36.768 16.279 1.00 20.37 ? 403 HIS B CD2 1 ATOM 2853 C CE1 . HIS B 2 179 ? 67.165 36.436 16.380 1.00 19.40 ? 403 HIS B CE1 1 ATOM 2854 N NE2 . HIS B 2 179 ? 68.269 36.439 17.099 1.00 20.76 ? 403 HIS B NE2 1 ATOM 2855 N N . GLU B 2 180 ? 72.159 38.828 12.482 1.00 24.47 ? 404 GLU B N 1 ATOM 2856 C CA . GLU B 2 180 ? 73.059 39.055 11.352 1.00 28.69 ? 404 GLU B CA 1 ATOM 2857 C C . GLU B 2 180 ? 73.129 37.862 10.376 1.00 26.06 ? 404 GLU B C 1 ATOM 2858 O O . GLU B 2 180 ? 73.142 38.043 9.158 1.00 28.62 ? 404 GLU B O 1 ATOM 2859 C CB . GLU B 2 180 ? 74.455 39.506 11.899 1.00 32.37 ? 404 GLU B CB 1 ATOM 2860 C CG . GLU B 2 180 ? 75.415 39.966 10.794 1.00 44.13 ? 404 GLU B CG 1 ATOM 2861 C CD . GLU B 2 180 ? 76.881 40.001 11.245 1.00 47.75 ? 404 GLU B CD 1 ATOM 2862 O OE1 . GLU B 2 180 ? 77.201 39.658 12.393 1.00 50.76 ? 404 GLU B OE1 1 ATOM 2863 O OE2 . GLU B 2 180 ? 77.734 40.354 10.431 1.00 67.35 ? 404 GLU B OE2 1 ATOM 2864 N N . LYS B 2 181 ? 73.151 36.653 10.905 1.00 27.81 ? 405 LYS B N 1 ATOM 2865 C CA . LYS B 2 181 ? 73.179 35.504 10.012 1.00 28.67 ? 405 LYS B CA 1 ATOM 2866 C C . LYS B 2 181 ? 71.951 35.477 9.135 1.00 29.93 ? 405 LYS B C 1 ATOM 2867 O O . LYS B 2 181 ? 72.062 35.252 7.933 1.00 25.29 ? 405 LYS B O 1 ATOM 2868 C CB . LYS B 2 181 ? 73.285 34.217 10.814 1.00 32.12 ? 405 LYS B CB 1 ATOM 2869 C CG . LYS B 2 181 ? 73.270 32.914 10.000 1.00 39.83 ? 405 LYS B CG 1 ATOM 2870 C CD . LYS B 2 181 ? 74.639 32.682 9.338 1.00 44.03 ? 405 LYS B CD 1 ATOM 2871 C CE . LYS B 2 181 ? 74.929 31.197 9.116 1.00 49.33 ? 405 LYS B CE 1 ATOM 2872 N NZ . LYS B 2 181 ? 76.117 31.066 8.194 1.00 54.16 ? 405 LYS B NZ 1 ATOM 2873 N N . VAL B 2 182 ? 70.771 35.709 9.720 1.00 26.03 ? 406 VAL B N 1 ATOM 2874 C CA . VAL B 2 182 ? 69.538 35.837 8.906 1.00 24.81 ? 406 VAL B CA 1 ATOM 2875 C C . VAL B 2 182 ? 69.552 36.893 7.837 1.00 23.87 ? 406 VAL B C 1 ATOM 2876 O O . VAL B 2 182 ? 69.189 36.639 6.661 1.00 24.41 ? 406 VAL B O 1 ATOM 2877 C CB . VAL B 2 182 ? 68.270 35.964 9.846 1.00 26.00 ? 406 VAL B CB 1 ATOM 2878 C CG1 . VAL B 2 182 ? 66.996 36.127 8.990 1.00 22.59 ? 406 VAL B CG1 1 ATOM 2879 C CG2 . VAL B 2 182 ? 68.201 34.664 10.659 1.00 24.52 ? 406 VAL B CG2 1 ATOM 2880 N N . TYR B 2 183 ? 69.983 38.092 8.237 1.00 23.09 ? 407 TYR B N 1 ATOM 2881 C CA . TYR B 2 183 ? 69.982 39.253 7.367 1.00 22.72 ? 407 TYR B CA 1 ATOM 2882 C C . TYR B 2 183 ? 70.955 38.922 6.158 1.00 26.23 ? 407 TYR B C 1 ATOM 2883 O O . TYR B 2 183 ? 70.646 39.141 4.993 1.00 23.46 ? 407 TYR B O 1 ATOM 2884 C CB . TYR B 2 183 ? 70.592 40.374 8.228 1.00 20.13 ? 407 TYR B CB 1 ATOM 2885 C CG . TYR B 2 183 ? 70.725 41.703 7.527 1.00 22.62 ? 407 TYR B CG 1 ATOM 2886 C CD1 . TYR B 2 183 ? 69.630 42.606 7.494 1.00 22.94 ? 407 TYR B CD1 1 ATOM 2887 C CD2 . TYR B 2 183 ? 71.950 42.074 6.894 1.00 25.00 ? 407 TYR B CD2 1 ATOM 2888 C CE1 . TYR B 2 183 ? 69.757 43.819 6.858 1.00 24.88 ? 407 TYR B CE1 1 ATOM 2889 C CE2 . TYR B 2 183 ? 72.076 43.276 6.218 1.00 27.73 ? 407 TYR B CE2 1 ATOM 2890 C CZ . TYR B 2 183 ? 70.972 44.148 6.228 1.00 31.75 ? 407 TYR B CZ 1 ATOM 2891 O OH . TYR B 2 183 ? 71.089 45.332 5.578 1.00 31.47 ? 407 TYR B OH 1 ATOM 2892 N N . ASN B 2 184 ? 72.121 38.360 6.484 1.00 27.48 ? 408 ASN B N 1 ATOM 2893 C CA . ASN B 2 184 ? 73.119 38.037 5.421 1.00 31.23 ? 408 ASN B CA 1 ATOM 2894 C C . ASN B 2 184 ? 72.632 36.986 4.444 1.00 30.29 ? 408 ASN B C 1 ATOM 2895 O O . ASN B 2 184 ? 72.612 37.195 3.235 1.00 32.98 ? 408 ASN B O 1 ATOM 2896 C CB . ASN B 2 184 ? 74.373 37.477 6.082 1.00 31.61 ? 408 ASN B CB 1 ATOM 2897 C CG . ASN B 2 184 ? 75.253 38.547 6.611 1.00 35.03 ? 408 ASN B CG 1 ATOM 2898 O OD1 . ASN B 2 184 ? 74.897 39.729 6.619 1.00 29.39 ? 408 ASN B OD1 1 ATOM 2899 N ND2 . ASN B 2 184 ? 76.414 38.152 7.067 1.00 39.39 ? 408 ASN B ND2 1 ATOM 2900 N N . TRP B 2 185 ? 72.155 35.882 4.999 1.00 30.80 ? 409 TRP B N 1 ATOM 2901 C CA . TRP B 2 185 ? 71.689 34.719 4.226 1.00 29.75 ? 409 TRP B CA 1 ATOM 2902 C C . TRP B 2 185 ? 70.450 35.046 3.409 1.00 34.77 ? 409 TRP B C 1 ATOM 2903 O O . TRP B 2 185 ? 70.258 34.542 2.270 1.00 30.84 ? 409 TRP B O 1 ATOM 2904 C CB . TRP B 2 185 ? 71.536 33.583 5.228 1.00 38.02 ? 409 TRP B CB 1 ATOM 2905 C CG . TRP B 2 185 ? 71.507 32.136 4.761 1.00 43.21 ? 409 TRP B CG 1 ATOM 2906 C CD1 . TRP B 2 185 ? 71.378 31.623 3.452 1.00 47.15 ? 409 TRP B CD1 1 ATOM 2907 C CD2 . TRP B 2 185 ? 71.504 30.922 5.651 1.00 37.87 ? 409 TRP B CD2 1 ATOM 2908 N NE1 . TRP B 2 185 ? 71.315 30.217 3.477 1.00 43.23 ? 409 TRP B NE1 1 ATOM 2909 C CE2 . TRP B 2 185 ? 71.372 29.745 4.753 1.00 40.68 ? 409 TRP B CE2 1 ATOM 2910 C CE3 . TRP B 2 185 ? 71.491 30.723 7.043 1.00 33.97 ? 409 TRP B CE3 1 ATOM 2911 C CZ2 . TRP B 2 185 ? 71.286 28.431 5.256 1.00 36.66 ? 409 TRP B CZ2 1 ATOM 2912 C CZ3 . TRP B 2 185 ? 71.453 29.392 7.530 1.00 38.99 ? 409 TRP B CZ3 1 ATOM 2913 C CH2 . TRP B 2 185 ? 71.380 28.277 6.640 1.00 39.24 ? 409 TRP B CH2 1 ATOM 2914 N N . SER B 2 186 ? 69.622 35.988 3.875 1.00 29.26 ? 410 SER B N 1 ATOM 2915 C CA . SER B 2 186 ? 68.451 36.399 3.101 1.00 26.48 ? 410 SER B CA 1 ATOM 2916 C C . SER B 2 186 ? 68.787 37.398 2.003 1.00 29.29 ? 410 SER B C 1 ATOM 2917 O O . SER B 2 186 ? 67.903 37.782 1.253 1.00 35.08 ? 410 SER B O 1 ATOM 2918 C CB . SER B 2 186 ? 67.359 37.043 4.003 1.00 24.80 ? 410 SER B CB 1 ATOM 2919 O OG . SER B 2 186 ? 67.148 36.217 5.141 1.00 25.02 ? 410 SER B OG 1 ATOM 2920 N N . GLY B 2 187 ? 70.019 37.856 1.962 1.00 28.02 ? 411 GLY B N 1 ATOM 2921 C CA . GLY B 2 187 ? 70.453 38.671 0.842 1.00 28.92 ? 411 GLY B CA 1 ATOM 2922 C C . GLY B 2 187 ? 70.332 40.175 1.014 1.00 34.28 ? 411 GLY B C 1 ATOM 2923 O O . GLY B 2 187 ? 70.356 40.938 0.016 1.00 33.44 ? 411 GLY B O 1 ATOM 2924 N N . TYR B 2 188 ? 70.147 40.609 2.254 1.00 29.09 ? 412 TYR B N 1 ATOM 2925 C CA . TYR B 2 188 ? 69.928 42.028 2.467 1.00 27.51 ? 412 TYR B CA 1 ATOM 2926 C C . TYR B 2 188 ? 71.211 42.858 2.123 1.00 26.49 ? 412 TYR B C 1 ATOM 2927 O O . TYR B 2 188 ? 71.048 44.024 1.707 1.00 31.75 ? 412 TYR B O 1 ATOM 2928 C CB . TYR B 2 188 ? 69.380 42.399 3.894 1.00 21.68 ? 412 TYR B CB 1 ATOM 2929 C CG . TYR B 2 188 ? 67.860 42.133 4.045 1.00 23.81 ? 412 TYR B CG 1 ATOM 2930 C CD1 . TYR B 2 188 ? 67.400 40.813 4.112 1.00 20.99 ? 412 TYR B CD1 1 ATOM 2931 C CD2 . TYR B 2 188 ? 66.909 43.182 3.974 1.00 25.30 ? 412 TYR B CD2 1 ATOM 2932 C CE1 . TYR B 2 188 ? 66.033 40.511 4.218 1.00 20.67 ? 412 TYR B CE1 1 ATOM 2933 C CE2 . TYR B 2 188 ? 65.552 42.912 4.092 1.00 25.90 ? 412 TYR B CE2 1 ATOM 2934 C CZ . TYR B 2 188 ? 65.123 41.608 4.145 1.00 24.88 ? 412 TYR B CZ 1 ATOM 2935 O OH . TYR B 2 188 ? 63.787 41.419 4.216 1.00 26.65 ? 412 TYR B OH 1 ATOM 2936 N N . PRO B 2 189 ? 72.402 42.338 2.410 1.00 28.53 ? 413 PRO B N 1 ATOM 2937 C CA . PRO B 2 189 ? 73.591 43.168 2.148 1.00 35.17 ? 413 PRO B CA 1 ATOM 2938 C C . PRO B 2 189 ? 73.752 43.589 0.675 1.00 36.82 ? 413 PRO B C 1 ATOM 2939 O O . PRO B 2 189 ? 74.144 44.742 0.410 1.00 31.64 ? 413 PRO B O 1 ATOM 2940 C CB . PRO B 2 189 ? 74.750 42.267 2.601 1.00 34.60 ? 413 PRO B CB 1 ATOM 2941 C CG . PRO B 2 189 ? 74.126 41.461 3.729 1.00 33.59 ? 413 PRO B CG 1 ATOM 2942 C CD . PRO B 2 189 ? 72.800 41.090 3.080 1.00 23.08 ? 413 PRO B CD 1 ATOM 2943 N N . ILE B 2 190 ? 73.428 42.698 -0.253 1.00 36.73 ? 414 ILE B N 1 ATOM 2944 C CA . ILE B 2 190 ? 73.433 43.038 -1.694 1.00 39.86 ? 414 ILE B CA 1 ATOM 2945 C C . ILE B 2 190 ? 72.294 44.003 -2.013 1.00 40.53 ? 414 ILE B C 1 ATOM 2946 O O . ILE B 2 190 ? 72.526 44.947 -2.744 1.00 38.14 ? 414 ILE B O 1 ATOM 2947 C CB . ILE B 2 190 ? 73.424 41.774 -2.601 1.00 43.89 ? 414 ILE B CB 1 ATOM 2948 C CG1 . ILE B 2 190 ? 73.718 42.118 -4.076 1.00 51.92 ? 414 ILE B CG1 1 ATOM 2949 C CG2 . ILE B 2 190 ? 72.114 41.014 -2.494 1.00 42.78 ? 414 ILE B CG2 1 ATOM 2950 C CD1 . ILE B 2 190 ? 74.058 40.891 -4.928 1.00 58.73 ? 414 ILE B CD1 1 ATOM 2951 N N . LEU B 2 191 ? 71.090 43.837 -1.426 1.00 35.88 ? 415 LEU B N 1 ATOM 2952 C CA . LEU B 2 191 ? 70.054 44.868 -1.618 1.00 34.38 ? 415 LEU B CA 1 ATOM 2953 C C . LEU B 2 191 ? 70.443 46.242 -1.140 1.00 35.27 ? 415 LEU B C 1 ATOM 2954 O O . LEU B 2 191 ? 70.006 47.236 -1.734 1.00 42.57 ? 415 LEU B O 1 ATOM 2955 C CB . LEU B 2 191 ? 68.754 44.561 -0.876 1.00 41.15 ? 415 LEU B CB 1 ATOM 2956 C CG . LEU B 2 191 ? 67.808 43.698 -1.653 1.00 57.58 ? 415 LEU B CG 1 ATOM 2957 C CD1 . LEU B 2 191 ? 67.475 42.576 -0.711 1.00 59.69 ? 415 LEU B CD1 1 ATOM 2958 C CD2 . LEU B 2 191 ? 66.578 44.452 -2.101 1.00 59.03 ? 415 LEU B CD2 1 ATOM 2959 N N . VAL B 2 192 ? 71.127 46.323 0.001 1.00 32.59 ? 416 VAL B N 1 ATOM 2960 C CA . VAL B 2 192 ? 71.582 47.635 0.479 1.00 33.67 ? 416 VAL B CA 1 ATOM 2961 C C . VAL B 2 192 ? 72.569 48.244 -0.554 1.00 39.74 ? 416 VAL B C 1 ATOM 2962 O O . VAL B 2 192 ? 72.459 49.434 -0.932 1.00 37.61 ? 416 VAL B O 1 ATOM 2963 C CB . VAL B 2 192 ? 72.239 47.534 1.881 1.00 32.47 ? 416 VAL B CB 1 ATOM 2964 C CG1 . VAL B 2 192 ? 73.049 48.800 2.201 1.00 33.63 ? 416 VAL B CG1 1 ATOM 2965 C CG2 . VAL B 2 192 ? 71.136 47.372 2.931 1.00 27.87 ? 416 VAL B CG2 1 ATOM 2966 N N . LYS B 2 193 ? 73.498 47.422 -1.036 1.00 43.14 ? 417 LYS B N 1 ATOM 2967 C CA . LYS B 2 193 ? 74.462 47.898 -2.092 1.00 49.31 ? 417 LYS B CA 1 ATOM 2968 C C . LYS B 2 193 ? 73.776 48.314 -3.383 1.00 46.41 ? 417 LYS B C 1 ATOM 2969 O O . LYS B 2 193 ? 74.162 49.280 -3.986 1.00 58.07 ? 417 LYS B O 1 ATOM 2970 C CB . LYS B 2 193 ? 75.553 46.883 -2.372 1.00 48.44 ? 417 LYS B CB 1 ATOM 2971 C CG . LYS B 2 193 ? 76.617 46.935 -1.299 1.00 57.28 ? 417 LYS B CG 1 ATOM 2972 C CD . LYS B 2 193 ? 77.734 45.935 -1.559 1.00 71.11 ? 417 LYS B CD 1 ATOM 2973 C CE . LYS B 2 193 ? 78.990 46.326 -0.778 1.00 72.34 ? 417 LYS B CE 1 ATOM 2974 N NZ . LYS B 2 193 ? 79.820 45.138 -0.443 1.00 76.17 ? 417 LYS B NZ 1 ATOM 2975 N N . LYS B 2 194 ? 72.718 47.619 -3.763 1.00 48.02 ? 418 LYS B N 1 ATOM 2976 C CA . LYS B 2 194 ? 72.020 47.879 -4.998 1.00 52.28 ? 418 LYS B CA 1 ATOM 2977 C C . LYS B 2 194 ? 70.983 49.003 -4.842 1.00 52.14 ? 418 LYS B C 1 ATOM 2978 O O . LYS B 2 194 ? 70.792 49.779 -5.760 1.00 46.86 ? 418 LYS B O 1 ATOM 2979 C CB . LYS B 2 194 ? 71.343 46.569 -5.450 1.00 58.89 ? 418 LYS B CB 1 ATOM 2980 C CG . LYS B 2 194 ? 71.084 46.384 -6.944 1.00 68.19 ? 418 LYS B CG 1 ATOM 2981 C CD . LYS B 2 194 ? 69.866 45.491 -7.225 1.00 65.92 ? 418 LYS B CD 1 ATOM 2982 C CE . LYS B 2 194 ? 70.054 44.059 -6.748 1.00 65.78 ? 418 LYS B CE 1 ATOM 2983 N NZ . LYS B 2 194 ? 69.067 43.172 -7.418 1.00 64.52 ? 418 LYS B NZ 1 ATOM 2984 N N . LEU B 2 195 ? 70.307 49.091 -3.695 1.00 42.58 ? 419 LEU B N 1 ATOM 2985 C CA . LEU B 2 195 ? 69.180 50.028 -3.518 1.00 34.80 ? 419 LEU B CA 1 ATOM 2986 C C . LEU B 2 195 ? 69.313 51.002 -2.353 1.00 42.14 ? 419 LEU B C 1 ATOM 2987 O O . LEU B 2 195 ? 68.415 51.823 -2.154 1.00 38.10 ? 419 LEU B O 1 ATOM 2988 C CB . LEU B 2 195 ? 67.855 49.281 -3.320 1.00 41.17 ? 419 LEU B CB 1 ATOM 2989 C CG . LEU B 2 195 ? 67.038 48.716 -4.482 1.00 50.56 ? 419 LEU B CG 1 ATOM 2990 C CD1 . LEU B 2 195 ? 67.667 47.410 -4.824 1.00 44.45 ? 419 LEU B CD1 1 ATOM 2991 C CD2 . LEU B 2 195 ? 65.563 48.527 -4.081 1.00 50.47 ? 419 LEU B CD2 1 ATOM 2992 N N . GLY B 2 196 ? 70.383 50.894 -1.559 1.00 37.11 ? 420 GLY B N 1 ATOM 2993 C CA . GLY B 2 196 ? 70.653 51.910 -0.554 1.00 34.80 ? 420 GLY B CA 1 ATOM 2994 C C . GLY B 2 196 ? 70.091 51.540 0.831 1.00 36.60 ? 420 GLY B C 1 ATOM 2995 O O . GLY B 2 196 ? 69.575 50.442 1.059 1.00 32.54 ? 420 GLY B O 1 ATOM 2996 N N . LEU B 2 197 ? 70.141 52.492 1.746 1.00 34.84 ? 421 LEU B N 1 ATOM 2997 C CA . LEU B 2 197 ? 69.898 52.221 3.171 1.00 39.07 ? 421 LEU B CA 1 ATOM 2998 C C . LEU B 2 197 ? 68.488 51.956 3.653 1.00 38.41 ? 421 LEU B C 1 ATOM 2999 O O . LEU B 2 197 ? 68.326 51.601 4.820 1.00 38.98 ? 421 LEU B O 1 ATOM 3000 C CB . LEU B 2 197 ? 70.554 53.304 4.006 1.00 38.19 ? 421 LEU B CB 1 ATOM 3001 C CG . LEU B 2 197 ? 72.076 53.238 3.853 1.00 38.34 ? 421 LEU B CG 1 ATOM 3002 C CD1 . LEU B 2 197 ? 72.542 54.572 4.348 1.00 39.71 ? 421 LEU B CD1 1 ATOM 3003 C CD2 . LEU B 2 197 ? 72.743 52.076 4.631 1.00 39.14 ? 421 LEU B CD2 1 ATOM 3004 N N . ASP B 2 198 ? 67.468 52.076 2.797 1.00 38.56 ? 422 ASP B N 1 ATOM 3005 C CA . ASP B 2 198 ? 66.089 51.600 3.132 1.00 37.51 ? 422 ASP B CA 1 ATOM 3006 C C . ASP B 2 198 ? 66.086 50.116 3.388 1.00 40.01 ? 422 ASP B C 1 ATOM 3007 O O . ASP B 2 198 ? 65.104 49.527 3.889 1.00 38.89 ? 422 ASP B O 1 ATOM 3008 C CB . ASP B 2 198 ? 65.179 51.688 1.897 1.00 52.28 ? 422 ASP B CB 1 ATOM 3009 C CG . ASP B 2 198 ? 64.693 53.081 1.597 1.00 57.44 ? 422 ASP B CG 1 ATOM 3010 O OD1 . ASP B 2 198 ? 64.687 53.938 2.501 1.00 64.49 ? 422 ASP B OD1 1 ATOM 3011 O OD2 . ASP B 2 198 ? 64.291 53.287 0.427 1.00 60.61 ? 422 ASP B OD2 1 ATOM 3012 N N . TYR B 2 199 ? 67.120 49.453 2.907 1.00 28.52 ? 423 TYR B N 1 ATOM 3013 C CA . TYR B 2 199 ? 67.159 48.007 3.155 1.00 36.37 ? 423 TYR B CA 1 ATOM 3014 C C . TYR B 2 199 ? 68.032 47.688 4.326 1.00 30.65 ? 423 TYR B C 1 ATOM 3015 O O . TYR B 2 199 ? 68.313 46.529 4.591 1.00 34.07 ? 423 TYR B O 1 ATOM 3016 C CB . TYR B 2 199 ? 67.623 47.256 1.874 1.00 37.70 ? 423 TYR B CB 1 ATOM 3017 C CG . TYR B 2 199 ? 66.499 47.355 0.911 1.00 51.69 ? 423 TYR B CG 1 ATOM 3018 C CD1 . TYR B 2 199 ? 66.204 48.591 0.283 1.00 50.65 ? 423 TYR B CD1 1 ATOM 3019 C CD2 . TYR B 2 199 ? 65.631 46.275 0.727 1.00 61.48 ? 423 TYR B CD2 1 ATOM 3020 C CE1 . TYR B 2 199 ? 65.134 48.727 -0.557 1.00 60.34 ? 423 TYR B CE1 1 ATOM 3021 C CE2 . TYR B 2 199 ? 64.546 46.401 -0.127 1.00 71.69 ? 423 TYR B CE2 1 ATOM 3022 C CZ . TYR B 2 199 ? 64.315 47.636 -0.763 1.00 73.08 ? 423 TYR B CZ 1 ATOM 3023 O OH . TYR B 2 199 ? 63.244 47.789 -1.599 1.00 89.89 ? 423 TYR B OH 1 ATOM 3024 N N . SER B 2 200 ? 68.566 48.709 4.995 1.00 25.53 ? 424 SER B N 1 ATOM 3025 C CA . SER B 2 200 ? 69.410 48.325 6.118 1.00 27.19 ? 424 SER B CA 1 ATOM 3026 C C . SER B 2 200 ? 68.585 48.241 7.380 1.00 23.03 ? 424 SER B C 1 ATOM 3027 O O . SER B 2 200 ? 67.627 49.008 7.561 1.00 25.54 ? 424 SER B O 1 ATOM 3028 C CB . SER B 2 200 ? 70.558 49.303 6.348 1.00 26.44 ? 424 SER B CB 1 ATOM 3029 O OG . SER B 2 200 ? 69.954 50.501 6.805 1.00 27.56 ? 424 SER B OG 1 ATOM 3030 N N . TYR B 2 201 ? 69.033 47.386 8.306 1.00 22.96 ? 425 TYR B N 1 ATOM 3031 C CA . TYR B 2 201 ? 68.311 47.205 9.584 1.00 21.78 ? 425 TYR B CA 1 ATOM 3032 C C . TYR B 2 201 ? 68.341 48.477 10.400 1.00 21.32 ? 425 TYR B C 1 ATOM 3033 O O . TYR B 2 201 ? 67.324 48.862 11.018 1.00 24.20 ? 425 TYR B O 1 ATOM 3034 C CB . TYR B 2 201 ? 68.957 46.042 10.409 1.00 19.51 ? 425 TYR B CB 1 ATOM 3035 C CG . TYR B 2 201 ? 68.157 45.765 11.682 1.00 17.36 ? 425 TYR B CG 1 ATOM 3036 C CD1 . TYR B 2 201 ? 66.933 45.058 11.588 1.00 16.77 ? 425 TYR B CD1 1 ATOM 3037 C CD2 . TYR B 2 201 ? 68.624 46.226 12.938 1.00 15.53 ? 425 TYR B CD2 1 ATOM 3038 C CE1 . TYR B 2 201 ? 66.186 44.844 12.726 1.00 17.47 ? 425 TYR B CE1 1 ATOM 3039 C CE2 . TYR B 2 201 ? 67.919 45.998 14.114 1.00 15.92 ? 425 TYR B CE2 1 ATOM 3040 C CZ . TYR B 2 201 ? 66.630 45.340 13.968 1.00 17.21 ? 425 TYR B CZ 1 ATOM 3041 O OH . TYR B 2 201 ? 65.892 45.091 15.091 1.00 17.05 ? 425 TYR B OH 1 ATOM 3042 N N . ASP B 2 202 ? 69.493 49.161 10.412 1.00 21.99 ? 426 ASP B N 1 ATOM 3043 C CA . ASP B 2 202 ? 69.570 50.328 11.282 1.00 22.82 ? 426 ASP B CA 1 ATOM 3044 C C . ASP B 2 202 ? 68.987 51.612 10.733 1.00 23.44 ? 426 ASP B C 1 ATOM 3045 O O . ASP B 2 202 ? 68.526 52.448 11.510 1.00 23.80 ? 426 ASP B O 1 ATOM 3046 C CB . ASP B 2 202 ? 71.035 50.612 11.735 1.00 26.27 ? 426 ASP B CB 1 ATOM 3047 C CG . ASP B 2 202 ? 71.524 49.496 12.596 1.00 27.60 ? 426 ASP B CG 1 ATOM 3048 O OD1 . ASP B 2 202 ? 70.843 49.203 13.598 1.00 27.24 ? 426 ASP B OD1 1 ATOM 3049 O OD2 . ASP B 2 202 ? 72.495 48.873 12.207 1.00 28.86 ? 426 ASP B OD2 1 ATOM 3050 N N . LEU B 2 203 ? 68.977 51.764 9.423 1.00 20.46 ? 427 LEU B N 1 ATOM 3051 C CA . LEU B 2 203 ? 68.615 53.084 8.895 1.00 23.47 ? 427 LEU B CA 1 ATOM 3052 C C . LEU B 2 203 ? 67.427 53.058 7.906 1.00 26.49 ? 427 LEU B C 1 ATOM 3053 O O . LEU B 2 203 ? 67.206 54.004 7.163 1.00 23.08 ? 427 LEU B O 1 ATOM 3054 C CB . LEU B 2 203 ? 69.820 53.807 8.311 1.00 26.16 ? 427 LEU B CB 1 ATOM 3055 C CG . LEU B 2 203 ? 70.928 54.225 9.275 1.00 25.40 ? 427 LEU B CG 1 ATOM 3056 C CD1 . LEU B 2 203 ? 72.063 54.979 8.538 1.00 29.37 ? 427 LEU B CD1 1 ATOM 3057 C CD2 . LEU B 2 203 ? 70.386 55.039 10.467 1.00 25.35 ? 427 LEU B CD2 1 ATOM 3058 N N . ALA B 2 204 ? 66.642 51.986 7.909 1.00 23.43 ? 428 ALA B N 1 ATOM 3059 C CA . ALA B 2 204 ? 65.340 52.035 7.195 1.00 23.99 ? 428 ALA B CA 1 ATOM 3060 C C . ALA B 2 204 ? 64.489 53.125 7.788 1.00 24.76 ? 428 ALA B C 1 ATOM 3061 O O . ALA B 2 204 ? 64.624 53.477 8.971 1.00 23.15 ? 428 ALA B O 1 ATOM 3062 C CB . ALA B 2 204 ? 64.604 50.712 7.348 1.00 21.89 ? 428 ALA B CB 1 ATOM 3063 N N . SER B 2 205 ? 63.587 53.686 7.003 1.00 22.02 ? 429 SER B N 1 ATOM 3064 C CA . SER B 2 205 ? 62.837 54.830 7.543 1.00 22.64 ? 429 SER B CA 1 ATOM 3065 C C . SER B 2 205 ? 62.177 54.518 8.868 1.00 22.54 ? 429 SER B C 1 ATOM 3066 O O . SER B 2 205 ? 62.201 55.371 9.762 1.00 22.72 ? 429 SER B O 1 ATOM 3067 C CB . SER B 2 205 ? 61.745 55.361 6.544 1.00 26.39 ? 429 SER B CB 1 ATOM 3068 O OG . SER B 2 205 ? 60.724 54.391 6.357 1.00 29.88 ? 429 SER B OG 1 ATOM 3069 N N . ARG B 2 206 ? 61.476 53.369 9.014 1.00 21.48 ? 430 ARG B N 1 ATOM 3070 C CA . ARG B 2 206 ? 60.851 53.123 10.289 1.00 19.22 ? 430 ARG B CA 1 ATOM 3071 C C . ARG B 2 206 ? 61.816 52.879 11.451 1.00 22.04 ? 430 ARG B C 1 ATOM 3072 O O . ARG B 2 206 ? 61.449 53.126 12.598 1.00 21.48 ? 430 ARG B O 1 ATOM 3073 C CB . ARG B 2 206 ? 59.820 51.974 10.221 1.00 21.83 ? 430 ARG B CB 1 ATOM 3074 C CG . ARG B 2 206 ? 58.598 52.303 9.375 1.00 20.72 ? 430 ARG B CG 1 ATOM 3075 C CD . ARG B 2 206 ? 57.765 51.036 9.287 1.00 22.10 ? 430 ARG B CD 1 ATOM 3076 N NE . ARG B 2 206 ? 58.285 50.237 8.181 1.00 21.43 ? 430 ARG B NE 1 ATOM 3077 C CZ . ARG B 2 206 ? 57.889 49.009 7.924 1.00 21.87 ? 430 ARG B CZ 1 ATOM 3078 N NH1 . ARG B 2 206 ? 57.002 48.418 8.689 1.00 21.41 ? 430 ARG B NH1 1 ATOM 3079 N NH2 . ARG B 2 206 ? 58.409 48.371 6.882 1.00 22.97 ? 430 ARG B NH2 1 ATOM 3080 N N . ALA B 2 207 ? 63.047 52.391 11.140 1.00 23.27 ? 431 ALA B N 1 ATOM 3081 C CA . ALA B 2 207 ? 64.110 52.248 12.223 1.00 24.59 ? 431 ALA B CA 1 ATOM 3082 C C . ALA B 2 207 ? 64.406 53.649 12.790 1.00 25.56 ? 431 ALA B C 1 ATOM 3083 O O . ALA B 2 207 ? 64.471 53.837 14.020 1.00 21.45 ? 431 ALA B O 1 ATOM 3084 C CB . ALA B 2 207 ? 65.400 51.584 11.653 1.00 20.53 ? 431 ALA B CB 1 ATOM 3085 N N . LYS B 2 208 ? 64.622 54.607 11.878 1.00 22.51 ? 432 LYS B N 1 ATOM 3086 C CA . LYS B 2 208 ? 64.920 55.999 12.248 1.00 23.61 ? 432 LYS B CA 1 ATOM 3087 C C . LYS B 2 208 ? 63.770 56.651 12.966 1.00 23.30 ? 432 LYS B C 1 ATOM 3088 O O . LYS B 2 208 ? 64.001 57.284 13.996 1.00 25.35 ? 432 LYS B O 1 ATOM 3089 C CB . LYS B 2 208 ? 65.352 56.829 10.993 1.00 26.04 ? 432 LYS B CB 1 ATOM 3090 C CG . LYS B 2 208 ? 66.639 56.308 10.353 1.00 23.25 ? 432 LYS B CG 1 ATOM 3091 C CD . LYS B 2 208 ? 67.050 57.109 9.117 1.00 24.89 ? 432 LYS B CD 1 ATOM 3092 C CE . LYS B 2 208 ? 65.916 56.978 8.087 1.00 24.33 ? 432 LYS B CE 1 ATOM 3093 N NZ . LYS B 2 208 ? 66.563 57.417 6.801 1.00 27.89 ? 432 LYS B NZ 1 ATOM 3094 N N . ILE B 2 209 ? 62.525 56.428 12.509 1.00 21.76 ? 433 ILE B N 1 ATOM 3095 C CA . ILE B 2 209 ? 61.397 57.066 13.161 1.00 22.84 ? 433 ILE B CA 1 ATOM 3096 C C . ILE B 2 209 ? 61.218 56.455 14.558 1.00 23.23 ? 433 ILE B C 1 ATOM 3097 O O . ILE B 2 209 ? 60.975 57.146 15.525 1.00 20.91 ? 433 ILE B O 1 ATOM 3098 C CB . ILE B 2 209 ? 60.089 56.927 12.306 1.00 22.32 ? 433 ILE B CB 1 ATOM 3099 C CG1 . ILE B 2 209 ? 60.225 57.821 11.026 1.00 23.70 ? 433 ILE B CG1 1 ATOM 3100 C CG2 . ILE B 2 209 ? 58.830 57.172 13.161 1.00 23.04 ? 433 ILE B CG2 1 ATOM 3101 C CD1 . ILE B 2 209 ? 59.262 57.375 9.939 1.00 24.22 ? 433 ILE B CD1 1 ATOM 3102 N N . PHE B 2 210 ? 61.299 55.126 14.672 1.00 20.76 ? 434 PHE B N 1 ATOM 3103 C CA . PHE B 2 210 ? 61.104 54.569 16.052 1.00 21.09 ? 434 PHE B CA 1 ATOM 3104 C C . PHE B 2 210 ? 62.284 55.009 16.955 1.00 20.61 ? 434 PHE B C 1 ATOM 3105 O O . PHE B 2 210 ? 62.079 55.248 18.153 1.00 18.83 ? 434 PHE B O 1 ATOM 3106 C CB . PHE B 2 210 ? 61.008 53.004 16.013 1.00 21.42 ? 434 PHE B CB 1 ATOM 3107 C CG . PHE B 2 210 ? 59.688 52.455 15.578 1.00 21.22 ? 434 PHE B CG 1 ATOM 3108 C CD1 . PHE B 2 210 ? 58.491 52.826 16.221 1.00 24.74 ? 434 PHE B CD1 1 ATOM 3109 C CD2 . PHE B 2 210 ? 59.663 51.436 14.593 1.00 23.23 ? 434 PHE B CD2 1 ATOM 3110 C CE1 . PHE B 2 210 ? 57.268 52.201 15.862 1.00 21.28 ? 434 PHE B CE1 1 ATOM 3111 C CE2 . PHE B 2 210 ? 58.474 50.823 14.233 1.00 27.37 ? 434 PHE B CE2 1 ATOM 3112 C CZ . PHE B 2 210 ? 57.253 51.252 14.878 1.00 24.77 ? 434 PHE B CZ 1 ATOM 3113 N N . ARG B 2 211 ? 63.481 55.137 16.384 1.00 20.54 ? 435 ARG B N 1 ATOM 3114 C CA . ARG B 2 211 ? 64.678 55.482 17.208 1.00 21.08 ? 435 ARG B CA 1 ATOM 3115 C C . ARG B 2 211 ? 64.392 56.937 17.754 1.00 24.73 ? 435 ARG B C 1 ATOM 3116 O O . ARG B 2 211 ? 64.685 57.259 18.910 1.00 21.61 ? 435 ARG B O 1 ATOM 3117 C CB . ARG B 2 211 ? 65.932 55.514 16.324 1.00 18.99 ? 435 ARG B CB 1 ATOM 3118 C CG . ARG B 2 211 ? 67.156 55.762 17.157 1.00 20.36 ? 435 ARG B CG 1 ATOM 3119 C CD . ARG B 2 211 ? 68.481 55.495 16.402 1.00 21.38 ? 435 ARG B CD 1 ATOM 3120 N NE . ARG B 2 211 ? 68.588 54.050 15.977 1.00 20.97 ? 435 ARG B NE 1 ATOM 3121 C CZ . ARG B 2 211 ? 68.490 53.555 14.724 1.00 19.29 ? 435 ARG B CZ 1 ATOM 3122 N NH1 . ARG B 2 211 ? 68.172 54.301 13.657 1.00 22.64 ? 435 ARG B NH1 1 ATOM 3123 N NH2 . ARG B 2 211 ? 68.719 52.246 14.527 1.00 21.04 ? 435 ARG B NH2 1 ATOM 3124 N N . ARG B 2 212 ? 63.869 57.780 16.854 1.00 27.01 ? 436 ARG B N 1 ATOM 3125 C CA . ARG B 2 212 ? 63.536 59.187 17.177 1.00 24.07 ? 436 ARG B CA 1 ATOM 3126 C C . ARG B 2 212 ? 62.396 59.335 18.136 1.00 22.55 ? 436 ARG B C 1 ATOM 3127 O O . ARG B 2 212 ? 62.464 60.134 19.087 1.00 26.14 ? 436 ARG B O 1 ATOM 3128 C CB . ARG B 2 212 ? 63.266 60.025 15.890 1.00 22.46 ? 436 ARG B CB 1 ATOM 3129 C CG . ARG B 2 212 ? 63.116 61.554 16.202 1.00 22.67 ? 436 ARG B CG 1 ATOM 3130 C CD . ARG B 2 212 ? 62.635 62.319 14.914 1.00 22.80 ? 436 ARG B CD 1 ATOM 3131 N NE . ARG B 2 212 ? 61.251 61.898 14.625 1.00 23.39 ? 436 ARG B NE 1 ATOM 3132 C CZ . ARG B 2 212 ? 60.744 61.696 13.383 1.00 23.46 ? 436 ARG B CZ 1 ATOM 3133 N NH1 . ARG B 2 212 ? 61.409 62.087 12.319 1.00 26.10 ? 436 ARG B NH1 1 ATOM 3134 N NH2 . ARG B 2 212 ? 59.542 61.168 13.231 1.00 30.03 ? 436 ARG B NH2 1 ATOM 3135 N N . ASP B 2 213 ? 61.347 58.566 17.962 1.00 24.12 ? 437 ASP B N 1 ATOM 3136 C CA . ASP B 2 213 ? 60.077 58.767 18.646 1.00 23.98 ? 437 ASP B CA 1 ATOM 3137 C C . ASP B 2 213 ? 59.593 57.793 19.668 1.00 26.15 ? 437 ASP B C 1 ATOM 3138 O O . ASP B 2 213 ? 58.601 58.061 20.378 1.00 22.60 ? 437 ASP B O 1 ATOM 3139 C CB . ASP B 2 213 ? 58.943 58.827 17.559 1.00 26.26 ? 437 ASP B CB 1 ATOM 3140 C CG . ASP B 2 213 ? 59.061 60.044 16.668 1.00 25.72 ? 437 ASP B CG 1 ATOM 3141 O OD1 . ASP B 2 213 ? 59.872 60.940 17.032 1.00 26.44 ? 437 ASP B OD1 1 ATOM 3142 O OD2 . ASP B 2 213 ? 58.399 60.026 15.570 1.00 26.93 ? 437 ASP B OD2 1 ATOM 3143 N N . GLN B 2 214 ? 60.258 56.642 19.853 1.00 22.43 ? 438 GLN B N 1 ATOM 3144 C CA . GLN B 2 214 ? 59.714 55.743 20.858 1.00 20.03 ? 438 GLN B CA 1 ATOM 3145 C C . GLN B 2 214 ? 59.643 56.357 22.276 1.00 21.03 ? 438 GLN B C 1 ATOM 3146 O O . GLN B 2 214 ? 58.703 56.014 23.058 1.00 23.00 ? 438 GLN B O 1 ATOM 3147 C CB . GLN B 2 214 ? 60.534 54.383 20.978 1.00 23.70 ? 438 GLN B CB 1 ATOM 3148 C CG . GLN B 2 214 ? 62.008 54.641 21.344 1.00 19.88 ? 438 GLN B CG 1 ATOM 3149 C CD . GLN B 2 214 ? 62.204 54.624 22.849 1.00 21.32 ? 438 GLN B CD 1 ATOM 3150 O OE1 . GLN B 2 214 ? 61.457 53.960 23.586 1.00 19.93 ? 438 GLN B OE1 1 ATOM 3151 N NE2 . GLN B 2 214 ? 63.229 55.336 23.323 1.00 21.22 ? 438 GLN B NE2 1 ATOM 3152 N N . GLY B 2 215 ? 60.592 57.195 22.577 1.00 24.11 ? 439 GLY B N 1 ATOM 3153 C CA . GLY B 2 215 ? 60.704 57.869 23.893 1.00 25.09 ? 439 GLY B CA 1 ATOM 3154 C C . GLY B 2 215 ? 59.540 58.853 24.080 1.00 28.82 ? 439 GLY B C 1 ATOM 3155 O O . GLY B 2 215 ? 59.275 59.291 25.215 1.00 26.31 ? 439 GLY B O 1 ATOM 3156 N N . LYS B 2 216 ? 58.790 59.120 23.013 1.00 28.87 ? 440 LYS B N 1 ATOM 3157 C CA . LYS B 2 216 ? 57.619 60.011 23.102 1.00 28.26 ? 440 LYS B CA 1 ATOM 3158 C C . LYS B 2 216 ? 56.427 59.222 23.590 1.00 27.38 ? 440 LYS B C 1 ATOM 3159 O O . LYS B 2 216 ? 55.420 59.785 23.937 1.00 25.69 ? 440 LYS B O 1 ATOM 3160 C CB . LYS B 2 216 ? 57.335 60.777 21.766 1.00 26.01 ? 440 LYS B CB 1 ATOM 3161 C CG . LYS B 2 216 ? 58.481 61.668 21.370 1.00 30.20 ? 440 LYS B CG 1 ATOM 3162 C CD . LYS B 2 216 ? 58.295 62.134 19.940 1.00 35.57 ? 440 LYS B CD 1 ATOM 3163 C CE . LYS B 2 216 ? 59.406 63.133 19.643 1.00 31.97 ? 440 LYS B CE 1 ATOM 3164 N NZ . LYS B 2 216 ? 59.656 63.272 18.208 1.00 31.33 ? 440 LYS B NZ 1 ATOM 3165 N N . VAL B 2 217 ? 56.504 57.876 23.657 1.00 23.96 ? 441 VAL B N 1 ATOM 3166 C CA . VAL B 2 217 ? 55.428 57.108 24.297 1.00 23.00 ? 441 VAL B CA 1 ATOM 3167 C C . VAL B 2 217 ? 55.488 57.181 25.851 1.00 26.48 ? 441 VAL B C 1 ATOM 3168 O O . VAL B 2 217 ? 56.507 56.733 26.467 1.00 25.50 ? 441 VAL B O 1 ATOM 3169 C CB . VAL B 2 217 ? 55.458 55.600 23.818 1.00 23.11 ? 441 VAL B CB 1 ATOM 3170 C CG1 . VAL B 2 217 ? 54.376 54.775 24.489 1.00 26.36 ? 441 VAL B CG1 1 ATOM 3171 C CG2 . VAL B 2 217 ? 55.390 55.495 22.254 1.00 20.62 ? 441 VAL B CG2 1 ATOM 3172 N N . THR B 2 218 ? 54.410 57.708 26.501 1.00 22.99 ? 442 THR B N 1 ATOM 3173 C CA . THR B 2 218 ? 54.392 57.977 27.967 1.00 27.29 ? 442 THR B CA 1 ATOM 3174 C C . THR B 2 218 ? 53.193 57.264 28.469 1.00 26.51 ? 442 THR B C 1 ATOM 3175 O O . THR B 2 218 ? 53.039 57.067 29.660 1.00 29.71 ? 442 THR B O 1 ATOM 3176 C CB . THR B 2 218 ? 54.304 59.503 28.282 1.00 29.79 ? 442 THR B CB 1 ATOM 3177 O OG1 . THR B 2 218 ? 53.128 59.995 27.658 1.00 31.42 ? 442 THR B OG1 1 ATOM 3178 C CG2 . THR B 2 218 ? 55.540 60.262 27.692 1.00 30.05 ? 442 THR B CG2 1 ATOM 3179 N N . ASP B 2 219 ? 52.340 56.796 27.544 1.00 25.57 ? 443 ASP B N 1 ATOM 3180 C CA . ASP B 2 219 ? 50.997 56.213 27.955 1.00 28.45 ? 443 ASP B CA 1 ATOM 3181 C C . ASP B 2 219 ? 50.263 55.583 26.806 1.00 25.69 ? 443 ASP B C 1 ATOM 3182 O O . ASP B 2 219 ? 50.761 55.563 25.704 1.00 28.76 ? 443 ASP B O 1 ATOM 3183 C CB . ASP B 2 219 ? 50.060 57.316 28.555 1.00 33.48 ? 443 ASP B CB 1 ATOM 3184 C CG . ASP B 2 219 ? 49.811 58.541 27.617 1.00 34.47 ? 443 ASP B CG 1 ATOM 3185 O OD1 . ASP B 2 219 ? 50.073 58.612 26.386 1.00 30.98 ? 443 ASP B OD1 1 ATOM 3186 O OD2 . ASP B 2 219 ? 49.324 59.562 28.186 1.00 36.71 ? 443 ASP B OD2 1 ATOM 3187 N N . MET B 2 220 ? 49.032 55.128 27.036 1.00 26.86 ? 444 MET B N 1 ATOM 3188 C CA . MET B 2 220 ? 48.317 54.478 25.970 1.00 28.99 ? 444 MET B CA 1 ATOM 3189 C C . MET B 2 220 ? 48.048 55.431 24.796 1.00 32.09 ? 444 MET B C 1 ATOM 3190 O O . MET B 2 220 ? 48.220 55.079 23.634 1.00 29.87 ? 444 MET B O 1 ATOM 3191 C CB . MET B 2 220 ? 47.064 53.808 26.538 1.00 29.39 ? 444 MET B CB 1 ATOM 3192 C CG . MET B 2 220 ? 46.211 53.040 25.507 1.00 32.55 ? 444 MET B CG 1 ATOM 3193 S SD . MET B 2 220 ? 47.151 51.702 24.603 1.00 29.94 ? 444 MET B SD 1 ATOM 3194 C CE . MET B 2 220 ? 46.936 50.439 25.821 1.00 29.26 ? 444 MET B CE 1 ATOM 3195 N N . GLU B 2 221 ? 47.644 56.680 25.072 1.00 30.00 ? 445 GLU B N 1 ATOM 3196 C CA . GLU B 2 221 ? 47.328 57.512 23.965 1.00 29.70 ? 445 GLU B CA 1 ATOM 3197 C C . GLU B 2 221 ? 48.487 57.711 23.034 1.00 24.12 ? 445 GLU B C 1 ATOM 3198 O O . GLU B 2 221 ? 48.289 57.759 21.807 1.00 25.74 ? 445 GLU B O 1 ATOM 3199 C CB . GLU B 2 221 ? 46.838 58.944 24.386 1.00 32.65 ? 445 GLU B CB 1 ATOM 3200 C CG . GLU B 2 221 ? 45.382 58.935 24.859 1.00 50.10 ? 445 GLU B CG 1 ATOM 3201 C CD . GLU B 2 221 ? 44.390 58.210 23.916 1.00 58.70 ? 445 GLU B CD 1 ATOM 3202 O OE1 . GLU B 2 221 ? 44.065 58.770 22.838 1.00 59.57 ? 445 GLU B OE1 1 ATOM 3203 O OE2 . GLU B 2 221 ? 43.929 57.079 24.267 1.00 60.79 ? 445 GLU B OE2 1 ATOM 3204 N N . SER B 2 222 ? 49.665 57.969 23.603 1.00 24.99 ? 446 SER B N 1 ATOM 3205 C CA . SER B 2 222 ? 50.818 58.234 22.757 1.00 26.44 ? 446 SER B CA 1 ATOM 3206 C C . SER B 2 222 ? 51.331 56.845 22.149 1.00 26.39 ? 446 SER B C 1 ATOM 3207 O O . SER B 2 222 ? 51.972 56.866 21.136 1.00 27.84 ? 446 SER B O 1 ATOM 3208 C CB . SER B 2 222 ? 51.923 58.921 23.563 1.00 26.05 ? 446 SER B CB 1 ATOM 3209 O OG . SER B 2 222 ? 52.218 58.261 24.830 1.00 27.20 ? 446 SER B OG 1 ATOM 3210 N N . MET B 2 223 ? 51.048 55.709 22.779 1.00 23.18 ? 447 MET B N 1 ATOM 3211 C CA . MET B 2 223 ? 51.384 54.416 22.057 1.00 24.25 ? 447 MET B CA 1 ATOM 3212 C C . MET B 2 223 ? 50.482 54.280 20.808 1.00 25.94 ? 447 MET B C 1 ATOM 3213 O O . MET B 2 223 ? 50.939 53.941 19.715 1.00 23.49 ? 447 MET B O 1 ATOM 3214 C CB . MET B 2 223 ? 51.177 53.237 23.003 1.00 20.95 ? 447 MET B CB 1 ATOM 3215 C CG . MET B 2 223 ? 51.663 51.882 22.414 1.00 22.61 ? 447 MET B CG 1 ATOM 3216 S SD . MET B 2 223 ? 53.476 51.906 22.250 1.00 23.62 ? 447 MET B SD 1 ATOM 3217 C CE . MET B 2 223 ? 53.574 50.173 21.574 1.00 18.32 ? 447 MET B CE 1 ATOM 3218 N N . LYS B 2 224 ? 49.161 54.487 20.955 1.00 26.25 ? 448 LYS B N 1 ATOM 3219 C CA . LYS B 2 224 ? 48.285 54.555 19.758 1.00 28.72 ? 448 LYS B CA 1 ATOM 3220 C C . LYS B 2 224 ? 48.783 55.461 18.676 1.00 26.41 ? 448 LYS B C 1 ATOM 3221 O O . LYS B 2 224 ? 48.707 55.134 17.496 1.00 28.08 ? 448 LYS B O 1 ATOM 3222 C CB . LYS B 2 224 ? 46.864 55.078 20.173 1.00 26.48 ? 448 LYS B CB 1 ATOM 3223 C CG . LYS B 2 224 ? 46.063 54.013 20.935 1.00 29.83 ? 448 LYS B CG 1 ATOM 3224 C CD . LYS B 2 224 ? 44.844 54.696 21.609 1.00 35.73 ? 448 LYS B CD 1 ATOM 3225 C CE . LYS B 2 224 ? 43.761 53.691 21.998 1.00 45.30 ? 448 LYS B CE 1 ATOM 3226 N NZ . LYS B 2 224 ? 42.658 54.264 22.858 1.00 54.81 ? 448 LYS B NZ 1 ATOM 3227 N N . TYR B 2 225 ? 49.208 56.640 19.081 1.00 27.34 ? 449 TYR B N 1 ATOM 3228 C CA . TYR B 2 225 ? 49.618 57.677 18.172 1.00 27.00 ? 449 TYR B CA 1 ATOM 3229 C C . TYR B 2 225 ? 50.860 57.244 17.363 1.00 26.83 ? 449 TYR B C 1 ATOM 3230 O O . TYR B 2 225 ? 50.913 57.447 16.137 1.00 23.30 ? 449 TYR B O 1 ATOM 3231 C CB . TYR B 2 225 ? 49.984 58.930 18.993 1.00 26.75 ? 449 TYR B CB 1 ATOM 3232 C CG . TYR B 2 225 ? 50.190 60.071 18.041 1.00 32.13 ? 449 TYR B CG 1 ATOM 3233 C CD1 . TYR B 2 225 ? 49.076 60.833 17.634 1.00 37.39 ? 449 TYR B CD1 1 ATOM 3234 C CD2 . TYR B 2 225 ? 51.465 60.418 17.530 1.00 30.95 ? 449 TYR B CD2 1 ATOM 3235 C CE1 . TYR B 2 225 ? 49.227 61.888 16.739 1.00 35.85 ? 449 TYR B CE1 1 ATOM 3236 C CE2 . TYR B 2 225 ? 51.603 61.460 16.568 1.00 36.75 ? 449 TYR B CE2 1 ATOM 3237 C CZ . TYR B 2 225 ? 50.456 62.184 16.229 1.00 35.74 ? 449 TYR B CZ 1 ATOM 3238 O OH . TYR B 2 225 ? 50.446 63.206 15.347 1.00 42.35 ? 449 TYR B OH 1 ATOM 3239 N N . ILE B 2 226 ? 51.869 56.651 18.061 1.00 25.31 ? 450 ILE B N 1 ATOM 3240 C CA . ILE B 2 226 ? 53.075 56.226 17.251 1.00 23.83 ? 450 ILE B CA 1 ATOM 3241 C C . ILE B 2 226 ? 52.720 55.085 16.269 1.00 20.08 ? 450 ILE B C 1 ATOM 3242 O O . ILE B 2 226 ? 53.311 54.992 15.206 1.00 21.89 ? 450 ILE B O 1 ATOM 3243 C CB . ILE B 2 226 ? 54.342 55.855 18.167 1.00 22.85 ? 450 ILE B CB 1 ATOM 3244 C CG1 . ILE B 2 226 ? 55.649 55.919 17.361 1.00 24.88 ? 450 ILE B CG1 1 ATOM 3245 C CG2 . ILE B 2 226 ? 54.095 54.480 18.838 1.00 20.68 ? 450 ILE B CG2 1 ATOM 3246 C CD1 . ILE B 2 226 ? 56.964 55.578 18.143 1.00 21.99 ? 450 ILE B CD1 1 ATOM 3247 N N . MET B 2 227 ? 51.793 54.201 16.644 1.00 21.45 ? 451 MET B N 1 ATOM 3248 C CA . MET B 2 227 ? 51.502 53.024 15.854 1.00 23.20 ? 451 MET B CA 1 ATOM 3249 C C . MET B 2 227 ? 50.552 53.369 14.648 1.00 27.76 ? 451 MET B C 1 ATOM 3250 O O . MET B 2 227 ? 50.455 52.600 13.696 1.00 24.33 ? 451 MET B O 1 ATOM 3251 C CB . MET B 2 227 ? 50.818 51.963 16.742 1.00 23.24 ? 451 MET B CB 1 ATOM 3252 C CG . MET B 2 227 ? 51.689 51.336 17.860 1.00 25.01 ? 451 MET B CG 1 ATOM 3253 S SD . MET B 2 227 ? 53.295 50.833 17.148 1.00 24.62 ? 451 MET B SD 1 ATOM 3254 C CE . MET B 2 227 ? 52.754 49.456 16.113 1.00 18.83 ? 451 MET B CE 1 ATOM 3255 N N . ARG B 2 228 ? 49.826 54.501 14.755 1.00 25.62 ? 452 ARG B N 1 ATOM 3256 C CA . ARG B 2 228 ? 48.971 55.064 13.691 1.00 25.96 ? 452 ARG B CA 1 ATOM 3257 C C . ARG B 2 228 ? 49.735 56.144 12.877 1.00 26.83 ? 452 ARG B C 1 ATOM 3258 O O . ARG B 2 228 ? 49.171 56.705 11.897 1.00 26.93 ? 452 ARG B O 1 ATOM 3259 C CB . ARG B 2 228 ? 47.673 55.745 14.373 1.00 22.24 ? 452 ARG B CB 1 ATOM 3260 C CG . ARG B 2 228 ? 46.609 54.801 14.956 1.00 27.49 ? 452 ARG B CG 1 ATOM 3261 C CD . ARG B 2 228 ? 45.623 54.406 13.895 1.00 28.42 ? 452 ARG B CD 1 ATOM 3262 N NE . ARG B 2 228 ? 46.004 53.210 13.121 1.00 26.47 ? 452 ARG B NE 1 ATOM 3263 C CZ . ARG B 2 228 ? 45.314 52.781 12.058 1.00 30.18 ? 452 ARG B CZ 1 ATOM 3264 N NH1 . ARG B 2 228 ? 44.173 53.452 11.631 1.00 26.51 ? 452 ARG B NH1 1 ATOM 3265 N NH2 . ARG B 2 228 ? 45.694 51.669 11.411 1.00 24.17 ? 452 ARG B NH2 1 ATOM 3266 N N . TYR B 2 229 ? 51.019 56.401 13.202 1.00 24.42 ? 453 TYR B N 1 ATOM 3267 C CA . TYR B 2 229 ? 51.809 57.524 12.682 1.00 26.34 ? 453 TYR B CA 1 ATOM 3268 C C . TYR B 2 229 ? 52.098 57.464 11.184 1.00 29.83 ? 453 TYR B C 1 ATOM 3269 O O . TYR B 2 229 ? 52.478 56.410 10.601 1.00 28.35 ? 453 TYR B O 1 ATOM 3270 C CB . TYR B 2 229 ? 53.141 57.648 13.488 1.00 23.49 ? 453 TYR B CB 1 ATOM 3271 C CG . TYR B 2 229 ? 54.024 58.811 13.070 1.00 26.92 ? 453 TYR B CG 1 ATOM 3272 C CD1 . TYR B 2 229 ? 53.720 60.146 13.458 1.00 25.80 ? 453 TYR B CD1 1 ATOM 3273 C CD2 . TYR B 2 229 ? 55.140 58.586 12.266 1.00 21.06 ? 453 TYR B CD2 1 ATOM 3274 C CE1 . TYR B 2 229 ? 54.530 61.206 13.084 1.00 26.23 ? 453 TYR B CE1 1 ATOM 3275 C CE2 . TYR B 2 229 ? 55.964 59.618 11.884 1.00 26.16 ? 453 TYR B CE2 1 ATOM 3276 C CZ . TYR B 2 229 ? 55.623 60.944 12.285 1.00 27.37 ? 453 TYR B CZ 1 ATOM 3277 O OH . TYR B 2 229 ? 56.488 61.948 11.887 1.00 26.65 ? 453 TYR B OH 1 ATOM 3278 N N . ASN B 2 230 ? 51.828 58.588 10.509 1.00 26.99 ? 454 ASN B N 1 ATOM 3279 C CA . ASN B 2 230 ? 52.225 58.688 9.125 1.00 27.25 ? 454 ASN B CA 1 ATOM 3280 C C . ASN B 2 230 ? 52.968 60.003 8.899 1.00 35.47 ? 454 ASN B C 1 ATOM 3281 O O . ASN B 2 230 ? 54.235 59.988 8.730 1.00 35.62 ? 454 ASN B O 1 ATOM 3282 C CB . ASN B 2 230 ? 51.005 58.400 8.222 1.00 23.10 ? 454 ASN B CB 1 ATOM 3283 C CG . ASN B 2 230 ? 51.332 58.480 6.761 1.00 23.62 ? 454 ASN B CG 1 ATOM 3284 O OD1 . ASN B 2 230 ? 51.905 59.458 6.289 1.00 27.70 ? 454 ASN B OD1 1 ATOM 3285 N ND2 . ASN B 2 230 ? 51.005 57.407 5.997 1.00 25.74 ? 454 ASN B ND2 1 ATOM 3286 N N . ASN B 2 231 ? 52.262 61.158 8.946 1.00 30.22 ? 455 ASN B N 1 ATOM 3287 C CA . ASN B 2 231 ? 53.013 62.445 8.818 1.00 30.25 ? 455 ASN B CA 1 ATOM 3288 C C . ASN B 2 231 ? 53.942 62.590 7.612 1.00 25.26 ? 455 ASN B C 1 ATOM 3289 O O . ASN B 2 231 ? 54.951 63.320 7.674 1.00 32.50 ? 455 ASN B O 1 ATOM 3290 C CB . ASN B 2 231 ? 53.757 62.778 10.149 1.00 32.53 ? 455 ASN B CB 1 ATOM 3291 C CG . ASN B 2 231 ? 54.189 64.264 10.278 1.00 45.80 ? 455 ASN B CG 1 ATOM 3292 O OD1 . ASN B 2 231 ? 53.551 65.168 9.703 1.00 40.28 ? 455 ASN B OD1 1 ATOM 3293 N ND2 . ASN B 2 231 ? 55.320 64.511 11.014 1.00 38.87 ? 455 ASN B ND2 1 ATOM 3294 N N . TYR B 2 232 ? 53.639 61.929 6.492 1.00 26.58 ? 456 TYR B N 1 ATOM 3295 C CA . TYR B 2 232 ? 54.631 61.830 5.445 1.00 27.65 ? 456 TYR B CA 1 ATOM 3296 C C . TYR B 2 232 ? 55.038 63.117 4.735 1.00 32.10 ? 456 TYR B C 1 ATOM 3297 O O . TYR B 2 232 ? 56.112 63.171 4.078 1.00 30.08 ? 456 TYR B O 1 ATOM 3298 C CB . TYR B 2 232 ? 54.273 60.789 4.401 1.00 31.26 ? 456 TYR B CB 1 ATOM 3299 C CG . TYR B 2 232 ? 53.218 61.259 3.396 1.00 33.00 ? 456 TYR B CG 1 ATOM 3300 C CD1 . TYR B 2 232 ? 51.836 61.332 3.759 1.00 32.15 ? 456 TYR B CD1 1 ATOM 3301 C CD2 . TYR B 2 232 ? 53.607 61.677 2.122 1.00 31.46 ? 456 TYR B CD2 1 ATOM 3302 C CE1 . TYR B 2 232 ? 50.867 61.739 2.833 1.00 38.24 ? 456 TYR B CE1 1 ATOM 3303 C CE2 . TYR B 2 232 ? 52.650 62.150 1.191 1.00 35.97 ? 456 TYR B CE2 1 ATOM 3304 C CZ . TYR B 2 232 ? 51.281 62.182 1.584 1.00 35.83 ? 456 TYR B CZ 1 ATOM 3305 O OH . TYR B 2 232 ? 50.337 62.559 0.672 1.00 41.92 ? 456 TYR B OH 1 ATOM 3306 N N . LYS B 2 233 ? 54.158 64.110 4.770 1.00 34.64 ? 457 LYS B N 1 ATOM 3307 C CA . LYS B 2 233 ? 54.468 65.384 4.078 1.00 38.21 ? 457 LYS B CA 1 ATOM 3308 C C . LYS B 2 233 ? 55.474 66.165 4.863 1.00 36.10 ? 457 LYS B C 1 ATOM 3309 O O . LYS B 2 233 ? 56.231 66.932 4.275 1.00 43.90 ? 457 LYS B O 1 ATOM 3310 C CB . LYS B 2 233 ? 53.190 66.208 3.815 1.00 38.16 ? 457 LYS B CB 1 ATOM 3311 C CG . LYS B 2 233 ? 52.197 65.492 2.913 1.00 39.43 ? 457 LYS B CG 1 ATOM 3312 C CD . LYS B 2 233 ? 50.928 66.345 2.705 1.00 44.07 ? 457 LYS B CD 1 ATOM 3313 C CE . LYS B 2 233 ? 49.721 65.438 2.517 1.00 48.28 ? 457 LYS B CE 1 ATOM 3314 N NZ . LYS B 2 233 ? 48.617 66.233 1.894 1.00 65.20 ? 457 LYS B NZ 1 ATOM 3315 N N . GLN B 2 234 ? 55.536 65.975 6.185 1.00 33.11 ? 458 GLN B N 1 ATOM 3316 C CA . GLN B 2 234 ? 56.487 66.776 6.999 1.00 36.01 ? 458 GLN B CA 1 ATOM 3317 C C . GLN B 2 234 ? 57.696 65.972 7.581 1.00 35.15 ? 458 GLN B C 1 ATOM 3318 O O . GLN B 2 234 ? 58.711 66.540 7.942 1.00 30.32 ? 458 GLN B O 1 ATOM 3319 C CB . GLN B 2 234 ? 55.706 67.392 8.194 1.00 47.85 ? 458 GLN B CB 1 ATOM 3320 C CG . GLN B 2 234 ? 54.369 68.032 7.812 1.00 52.74 ? 458 GLN B CG 1 ATOM 3321 C CD . GLN B 2 234 ? 54.327 69.522 8.071 1.00 65.83 ? 458 GLN B CD 1 ATOM 3322 O OE1 . GLN B 2 234 ? 55.366 70.180 8.174 1.00 73.71 ? 458 GLN B OE1 1 ATOM 3323 N NE2 . GLN B 2 234 ? 53.117 70.072 8.169 1.00 66.09 ? 458 GLN B NE2 1 ATOM 3324 N N . ASP B 2 235 ? 57.546 64.653 7.733 1.00 31.23 ? 459 ASP B N 1 ATOM 3325 C CA . ASP B 2 235 ? 58.596 63.905 8.481 1.00 27.43 ? 459 ASP B CA 1 ATOM 3326 C C . ASP B 2 235 ? 59.755 63.832 7.552 1.00 26.34 ? 459 ASP B C 1 ATOM 3327 O O . ASP B 2 235 ? 59.687 63.221 6.443 1.00 30.55 ? 459 ASP B O 1 ATOM 3328 C CB . ASP B 2 235 ? 58.057 62.469 8.777 1.00 26.58 ? 459 ASP B CB 1 ATOM 3329 C CG . ASP B 2 235 ? 58.933 61.747 9.806 1.00 25.81 ? 459 ASP B CG 1 ATOM 3330 O OD1 . ASP B 2 235 ? 60.182 61.856 9.610 1.00 25.50 ? 459 ASP B OD1 1 ATOM 3331 O OD2 . ASP B 2 235 ? 58.347 61.155 10.720 1.00 27.12 ? 459 ASP B OD2 1 ATOM 3332 N N . PRO B 2 236 ? 60.896 64.354 7.951 1.00 28.18 ? 460 PRO B N 1 ATOM 3333 C CA . PRO B 2 236 ? 62.009 64.196 6.998 1.00 30.31 ? 460 PRO B CA 1 ATOM 3334 C C . PRO B 2 236 ? 62.443 62.753 6.651 1.00 34.82 ? 460 PRO B C 1 ATOM 3335 O O . PRO B 2 236 ? 62.975 62.496 5.556 1.00 35.16 ? 460 PRO B O 1 ATOM 3336 C CB . PRO B 2 236 ? 63.174 64.873 7.673 1.00 35.49 ? 460 PRO B CB 1 ATOM 3337 C CG . PRO B 2 236 ? 62.699 65.244 9.005 1.00 31.86 ? 460 PRO B CG 1 ATOM 3338 C CD . PRO B 2 236 ? 61.265 64.946 9.218 1.00 31.12 ? 460 PRO B CD 1 ATOM 3339 N N . TYR B 2 237 ? 62.236 61.810 7.566 1.00 29.09 ? 461 TYR B N 1 ATOM 3340 C CA . TYR B 2 237 ? 62.554 60.415 7.249 1.00 30.69 ? 461 TYR B CA 1 ATOM 3341 C C . TYR B 2 237 ? 61.613 59.767 6.236 1.00 31.47 ? 461 TYR B C 1 ATOM 3342 O O . TYR B 2 237 ? 61.920 58.668 5.701 1.00 31.61 ? 461 TYR B O 1 ATOM 3343 C CB . TYR B 2 237 ? 62.715 59.563 8.527 1.00 28.67 ? 461 TYR B CB 1 ATOM 3344 C CG . TYR B 2 237 ? 63.862 60.077 9.434 1.00 27.34 ? 461 TYR B CG 1 ATOM 3345 C CD1 . TYR B 2 237 ? 65.074 60.440 8.912 1.00 31.75 ? 461 TYR B CD1 1 ATOM 3346 C CD2 . TYR B 2 237 ? 63.679 60.176 10.823 1.00 26.87 ? 461 TYR B CD2 1 ATOM 3347 C CE1 . TYR B 2 237 ? 66.121 60.930 9.738 1.00 30.53 ? 461 TYR B CE1 1 ATOM 3348 C CE2 . TYR B 2 237 ? 64.691 60.654 11.660 1.00 27.59 ? 461 TYR B CE2 1 ATOM 3349 C CZ . TYR B 2 237 ? 65.911 61.027 11.113 1.00 26.55 ? 461 TYR B CZ 1 ATOM 3350 O OH . TYR B 2 237 ? 66.905 61.480 11.950 1.00 26.78 ? 461 TYR B OH 1 ATOM 3351 N N . SER B 2 238 ? 60.474 60.402 5.948 1.00 28.07 ? 462 SER B N 1 ATOM 3352 C CA . SER B 2 238 ? 59.609 59.803 4.938 1.00 28.51 ? 462 SER B CA 1 ATOM 3353 C C . SER B 2 238 ? 60.010 60.121 3.515 1.00 33.24 ? 462 SER B C 1 ATOM 3354 O O . SER B 2 238 ? 59.553 59.439 2.593 1.00 29.86 ? 462 SER B O 1 ATOM 3355 C CB . SER B 2 238 ? 58.163 60.135 5.177 1.00 27.71 ? 462 SER B CB 1 ATOM 3356 O OG . SER B 2 238 ? 57.798 59.715 6.488 1.00 31.55 ? 462 SER B OG 1 ATOM 3357 N N . LYS B 2 239 ? 60.899 61.108 3.331 1.00 30.84 ? 463 LYS B N 1 ATOM 3358 C CA . LYS B 2 239 ? 61.302 61.511 1.975 1.00 32.14 ? 463 LYS B CA 1 ATOM 3359 C C . LYS B 2 239 ? 60.068 61.815 1.076 1.00 36.19 ? 463 LYS B C 1 ATOM 3360 O O . LYS B 2 239 ? 60.085 61.550 -0.126 1.00 36.52 ? 463 LYS B O 1 ATOM 3361 C CB . LYS B 2 239 ? 62.247 60.477 1.360 1.00 39.04 ? 463 LYS B CB 1 ATOM 3362 C CG . LYS B 2 239 ? 63.563 60.461 2.168 1.00 41.30 ? 463 LYS B CG 1 ATOM 3363 C CD . LYS B 2 239 ? 64.590 59.438 1.704 1.00 40.78 ? 463 LYS B CD 1 ATOM 3364 C CE . LYS B 2 239 ? 65.848 59.722 2.508 1.00 46.22 ? 463 LYS B CE 1 ATOM 3365 N NZ . LYS B 2 239 ? 67.119 59.122 2.030 1.00 52.36 ? 463 LYS B NZ 1 ATOM 3366 N N . GLY B 2 240 ? 58.993 62.339 1.657 1.00 33.40 ? 464 GLY B N 1 ATOM 3367 C CA . GLY B 2 240 ? 57.806 62.649 0.859 1.00 37.58 ? 464 GLY B CA 1 ATOM 3368 C C . GLY B 2 240 ? 56.974 61.479 0.392 1.00 39.97 ? 464 GLY B C 1 ATOM 3369 O O . GLY B 2 240 ? 55.989 61.681 -0.323 1.00 36.20 ? 464 GLY B O 1 ATOM 3370 N N . ASP B 2 241 ? 57.281 60.254 0.844 1.00 31.98 ? 465 ASP B N 1 ATOM 3371 C CA . ASP B 2 241 ? 56.593 59.047 0.391 1.00 30.82 ? 465 ASP B CA 1 ATOM 3372 C C . ASP B 2 241 ? 55.567 58.552 1.438 1.00 33.78 ? 465 ASP B C 1 ATOM 3373 O O . ASP B 2 241 ? 55.962 58.226 2.582 1.00 33.15 ? 465 ASP B O 1 ATOM 3374 C CB . ASP B 2 241 ? 57.713 58.012 0.067 1.00 29.04 ? 465 ASP B CB 1 ATOM 3375 C CG . ASP B 2 241 ? 57.192 56.711 -0.464 1.00 34.78 ? 465 ASP B CG 1 ATOM 3376 O OD1 . ASP B 2 241 ? 56.040 56.279 -0.183 1.00 36.40 ? 465 ASP B OD1 1 ATOM 3377 O OD2 . ASP B 2 241 ? 57.995 56.043 -1.108 1.00 38.07 ? 465 ASP B OD2 1 ATOM 3378 N N . PRO B 2 242 ? 54.256 58.518 1.111 1.00 29.86 ? 466 PRO B N 1 ATOM 3379 C CA . PRO B 2 242 ? 53.250 58.190 2.137 1.00 30.27 ? 466 PRO B CA 1 ATOM 3380 C C . PRO B 2 242 ? 53.324 56.745 2.642 1.00 31.32 ? 466 PRO B C 1 ATOM 3381 O O . PRO B 2 242 ? 52.572 56.367 3.551 1.00 31.29 ? 466 PRO B O 1 ATOM 3382 C CB . PRO B 2 242 ? 51.932 58.329 1.379 1.00 31.61 ? 466 PRO B CB 1 ATOM 3383 C CG . PRO B 2 242 ? 52.285 58.044 -0.078 1.00 32.90 ? 466 PRO B CG 1 ATOM 3384 C CD . PRO B 2 242 ? 53.649 58.684 -0.240 1.00 32.31 ? 466 PRO B CD 1 ATOM 3385 N N . CYS B 2 243 ? 54.167 55.928 2.013 1.00 28.90 ? 467 CYS B N 1 ATOM 3386 C CA . CYS B 2 243 ? 54.403 54.570 2.544 1.00 30.51 ? 467 CYS B CA 1 ATOM 3387 C C . CYS B 2 243 ? 55.661 54.473 3.476 1.00 33.02 ? 467 CYS B C 1 ATOM 3388 O O . CYS B 2 243 ? 55.788 53.542 4.273 1.00 37.45 ? 467 CYS B O 1 ATOM 3389 C CB . CYS B 2 243 ? 54.523 53.558 1.395 1.00 32.84 ? 467 CYS B CB 1 ATOM 3390 S SG . CYS B 2 243 ? 54.175 51.857 1.949 1.00 43.32 ? 467 CYS B SG 1 ATOM 3391 N N . ASN B 2 244 ? 56.569 55.447 3.370 1.00 29.59 ? 468 ASN B N 1 ATOM 3392 C CA . ASN B 2 244 ? 57.766 55.552 4.148 1.00 32.60 ? 468 ASN B CA 1 ATOM 3393 C C . ASN B 2 244 ? 57.700 56.003 5.634 1.00 27.11 ? 468 ASN B C 1 ATOM 3394 O O . ASN B 2 244 ? 58.256 57.034 6.051 1.00 29.81 ? 468 ASN B O 1 ATOM 3395 C CB . ASN B 2 244 ? 58.664 56.452 3.360 1.00 37.55 ? 468 ASN B CB 1 ATOM 3396 C CG . ASN B 2 244 ? 60.001 55.868 3.161 1.00 42.97 ? 468 ASN B CG 1 ATOM 3397 O OD1 . ASN B 2 244 ? 60.212 54.700 3.491 1.00 47.14 ? 468 ASN B OD1 1 ATOM 3398 N ND2 . ASN B 2 244 ? 60.953 56.689 2.698 1.00 41.85 ? 468 ASN B ND2 1 ATOM 3399 N N . THR B 2 245 ? 56.934 55.276 6.432 1.00 24.28 ? 469 THR B N 1 ATOM 3400 C CA . THR B 2 245 ? 56.629 55.721 7.778 1.00 25.66 ? 469 THR B CA 1 ATOM 3401 C C . THR B 2 245 ? 56.024 54.524 8.529 1.00 24.77 ? 469 THR B C 1 ATOM 3402 O O . THR B 2 245 ? 55.860 53.483 7.955 1.00 27.14 ? 469 THR B O 1 ATOM 3403 C CB . THR B 2 245 ? 55.587 56.907 7.726 1.00 27.35 ? 469 THR B CB 1 ATOM 3404 O OG1 . THR B 2 245 ? 55.374 57.393 9.041 1.00 27.03 ? 469 THR B OG1 1 ATOM 3405 C CG2 . THR B 2 245 ? 54.181 56.464 7.114 1.00 23.74 ? 469 THR B CG2 1 ATOM 3406 N N . VAL B 2 246 ? 55.565 54.715 9.763 1.00 24.82 ? 470 VAL B N 1 ATOM 3407 C CA . VAL B 2 246 ? 55.028 53.630 10.516 1.00 24.68 ? 470 VAL B CA 1 ATOM 3408 C C . VAL B 2 246 ? 53.748 53.005 9.985 1.00 29.78 ? 470 VAL B C 1 ATOM 3409 O O . VAL B 2 246 ? 53.568 51.752 10.008 1.00 24.52 ? 470 VAL B O 1 ATOM 3410 C CB . VAL B 2 246 ? 54.807 54.031 12.000 1.00 23.48 ? 470 VAL B CB 1 ATOM 3411 C CG1 . VAL B 2 246 ? 54.268 52.866 12.839 1.00 23.18 ? 470 VAL B CG1 1 ATOM 3412 C CG2 . VAL B 2 246 ? 56.098 54.519 12.624 1.00 25.64 ? 470 VAL B CG2 1 ATOM 3413 N N . CYS B 2 247 ? 52.797 53.870 9.580 1.00 25.90 ? 471 CYS B N 1 ATOM 3414 C CA . CYS B 2 247 ? 51.540 53.329 9.159 1.00 22.42 ? 471 CYS B CA 1 ATOM 3415 C C . CYS B 2 247 ? 51.300 53.793 7.715 1.00 27.47 ? 471 CYS B C 1 ATOM 3416 O O . CYS B 2 247 ? 50.706 54.881 7.530 1.00 29.25 ? 471 CYS B O 1 ATOM 3417 C CB . CYS B 2 247 ? 50.388 53.803 10.145 1.00 24.99 ? 471 CYS B CB 1 ATOM 3418 S SG . CYS B 2 247 ? 48.794 52.954 9.913 1.00 30.95 ? 471 CYS B SG 1 ATOM 3419 N N . CYS B 2 248 ? 51.790 52.994 6.746 1.00 25.16 ? 472 CYS B N 1 ATOM 3420 C CA . CYS B 2 248 ? 51.862 53.262 5.288 1.00 27.59 ? 472 CYS B CA 1 ATOM 3421 C C . CYS B 2 248 ? 50.475 53.537 4.643 1.00 27.02 ? 472 CYS B C 1 ATOM 3422 O O . CYS B 2 248 ? 49.493 52.842 4.963 1.00 25.63 ? 472 CYS B O 1 ATOM 3423 C CB . CYS B 2 248 ? 52.407 51.952 4.607 1.00 26.58 ? 472 CYS B CB 1 ATOM 3424 S SG . CYS B 2 248 ? 52.272 51.883 2.813 1.00 32.37 ? 472 CYS B SG 1 ATOM 3425 N N . ARG B 2 249 ? 50.418 54.493 3.709 1.00 26.51 ? 473 ARG B N 1 ATOM 3426 C CA . ARG B 2 249 ? 49.135 54.752 2.921 1.00 28.03 ? 473 ARG B CA 1 ATOM 3427 C C . ARG B 2 249 ? 49.592 54.759 1.492 1.00 27.18 ? 473 ARG B C 1 ATOM 3428 O O . ARG B 2 249 ? 49.825 55.805 0.866 1.00 29.98 ? 473 ARG B O 1 ATOM 3429 C CB . ARG B 2 249 ? 48.580 56.151 3.234 1.00 24.67 ? 473 ARG B CB 1 ATOM 3430 C CG . ARG B 2 249 ? 47.928 56.317 4.596 1.00 25.75 ? 473 ARG B CG 1 ATOM 3431 C CD . ARG B 2 249 ? 46.556 55.679 4.746 1.00 27.76 ? 473 ARG B CD 1 ATOM 3432 N NE . ARG B 2 249 ? 45.630 56.015 3.625 1.00 30.28 ? 473 ARG B NE 1 ATOM 3433 C CZ . ARG B 2 249 ? 44.599 56.906 3.716 1.00 32.90 ? 473 ARG B CZ 1 ATOM 3434 N NH1 . ARG B 2 249 ? 44.423 57.645 4.840 1.00 27.64 ? 473 ARG B NH1 1 ATOM 3435 N NH2 . ARG B 2 249 ? 43.802 57.103 2.633 1.00 28.46 ? 473 ARG B NH2 1 ATOM 3436 N N . GLU B 2 250 ? 49.757 53.582 0.933 1.00 24.87 ? 474 GLU B N 1 ATOM 3437 C CA . GLU B 2 250 ? 50.168 53.491 -0.427 1.00 25.95 ? 474 GLU B CA 1 ATOM 3438 C C . GLU B 2 250 ? 49.026 53.987 -1.367 1.00 25.78 ? 474 GLU B C 1 ATOM 3439 O O . GLU B 2 250 ? 49.289 54.261 -2.569 1.00 27.93 ? 474 GLU B O 1 ATOM 3440 C CB . GLU B 2 250 ? 50.484 52.010 -0.787 1.00 30.63 ? 474 GLU B CB 1 ATOM 3441 C CG . GLU B 2 250 ? 51.110 51.792 -2.151 1.00 36.60 ? 474 GLU B CG 1 ATOM 3442 C CD . GLU B 2 250 ? 52.473 52.424 -2.409 1.00 49.05 ? 474 GLU B CD 1 ATOM 3443 O OE1 . GLU B 2 250 ? 53.148 52.962 -1.475 1.00 51.04 ? 474 GLU B OE1 1 ATOM 3444 O OE2 . GLU B 2 250 ? 52.890 52.335 -3.595 1.00 47.66 ? 474 GLU B OE2 1 ATOM 3445 N N . ASP B 2 251 ? 47.789 54.032 -0.887 1.00 28.88 ? 475 ASP B N 1 ATOM 3446 C CA . ASP B 2 251 ? 46.705 54.548 -1.787 1.00 31.01 ? 475 ASP B CA 1 ATOM 3447 C C . ASP B 2 251 ? 46.955 56.042 -2.081 1.00 35.19 ? 475 ASP B C 1 ATOM 3448 O O . ASP B 2 251 ? 46.354 56.595 -2.978 1.00 32.03 ? 475 ASP B O 1 ATOM 3449 C CB . ASP B 2 251 ? 45.313 54.361 -1.148 1.00 30.55 ? 475 ASP B CB 1 ATOM 3450 C CG . ASP B 2 251 ? 45.229 54.991 0.219 1.00 39.08 ? 475 ASP B CG 1 ATOM 3451 O OD1 . ASP B 2 251 ? 46.063 54.626 1.126 1.00 34.31 ? 475 ASP B OD1 1 ATOM 3452 O OD2 . ASP B 2 251 ? 44.366 55.887 0.426 1.00 30.30 ? 475 ASP B OD2 1 ATOM 3453 N N . LEU B 2 252 ? 47.856 56.691 -1.335 1.00 32.16 ? 476 LEU B N 1 ATOM 3454 C CA . LEU B 2 252 ? 48.045 58.127 -1.464 1.00 31.69 ? 476 LEU B CA 1 ATOM 3455 C C . LEU B 2 252 ? 49.288 58.422 -2.282 1.00 32.79 ? 476 LEU B C 1 ATOM 3456 O O . LEU B 2 252 ? 49.675 59.589 -2.477 1.00 38.62 ? 476 LEU B O 1 ATOM 3457 C CB . LEU B 2 252 ? 48.141 58.779 -0.093 1.00 32.66 ? 476 LEU B CB 1 ATOM 3458 C CG . LEU B 2 252 ? 46.903 58.752 0.773 1.00 29.62 ? 476 LEU B CG 1 ATOM 3459 C CD1 . LEU B 2 252 ? 47.261 59.609 1.963 1.00 27.73 ? 476 LEU B CD1 1 ATOM 3460 C CD2 . LEU B 2 252 ? 45.590 59.304 0.068 1.00 31.21 ? 476 LEU B CD2 1 ATOM 3461 N N . ASN B 2 253 ? 49.907 57.369 -2.812 1.00 33.45 ? 477 ASN B N 1 ATOM 3462 C CA . ASN B 2 253 ? 51.092 57.557 -3.620 1.00 33.01 ? 477 ASN B CA 1 ATOM 3463 C C . ASN B 2 253 ? 50.582 58.308 -4.859 1.00 41.19 ? 477 ASN B C 1 ATOM 3464 O O . ASN B 2 253 ? 49.618 57.872 -5.493 1.00 33.99 ? 477 ASN B O 1 ATOM 3465 C CB . ASN B 2 253 ? 51.665 56.215 -4.095 1.00 35.42 ? 477 ASN B CB 1 ATOM 3466 C CG . ASN B 2 253 ? 52.918 56.379 -4.952 1.00 40.37 ? 477 ASN B CG 1 ATOM 3467 O OD1 . ASN B 2 253 ? 52.882 56.948 -6.055 1.00 40.45 ? 477 ASN B OD1 1 ATOM 3468 N ND2 . ASN B 2 253 ? 54.057 55.925 -4.425 1.00 41.48 ? 477 ASN B ND2 1 ATOM 3469 N N . SER B 2 254 ? 51.288 59.364 -5.249 1.00 38.79 ? 478 SER B N 1 ATOM 3470 C CA . SER B 2 254 ? 50.683 60.355 -6.130 1.00 48.06 ? 478 SER B CA 1 ATOM 3471 C C . SER B 2 254 ? 50.845 59.959 -7.608 1.00 55.37 ? 478 SER B C 1 ATOM 3472 O O . SER B 2 254 ? 50.098 60.416 -8.463 1.00 57.51 ? 478 SER B O 1 ATOM 3473 C CB . SER B 2 254 ? 51.311 61.704 -5.861 1.00 42.98 ? 478 SER B CB 1 ATOM 3474 O OG . SER B 2 254 ? 52.660 61.603 -6.259 1.00 46.94 ? 478 SER B OG 1 ATOM 3475 N N . HIS B 2 255 ? 51.809 59.101 -7.900 1.00 50.16 ? 479 HIS B N 1 ATOM 3476 C CA . HIS B 2 255 ? 51.966 58.624 -9.252 1.00 52.26 ? 479 HIS B CA 1 ATOM 3477 C C . HIS B 2 255 ? 51.546 57.187 -9.470 1.00 46.50 ? 479 HIS B C 1 ATOM 3478 O O . HIS B 2 255 ? 51.240 56.833 -10.580 1.00 49.69 ? 479 HIS B O 1 ATOM 3479 C CB . HIS B 2 255 ? 53.374 58.908 -9.779 1.00 57.00 ? 479 HIS B CB 1 ATOM 3480 C CG . HIS B 2 255 ? 54.463 58.392 -8.901 1.00 64.04 ? 479 HIS B CG 1 ATOM 3481 N ND1 . HIS B 2 255 ? 54.705 57.061 -8.745 1.00 73.46 ? 479 HIS B ND1 1 ATOM 3482 C CD2 . HIS B 2 255 ? 55.412 59.062 -8.125 1.00 71.97 ? 479 HIS B CD2 1 ATOM 3483 C CE1 . HIS B 2 255 ? 55.754 56.889 -7.901 1.00 72.15 ? 479 HIS B CE1 1 ATOM 3484 N NE2 . HIS B 2 255 ? 56.183 58.113 -7.518 1.00 71.06 ? 479 HIS B NE2 1 ATOM 3485 N N . SER B 2 256 ? 51.503 56.341 -8.447 1.00 44.42 ? 480 SER B N 1 ATOM 3486 C CA . SER B 2 256 ? 51.023 54.939 -8.614 1.00 47.46 ? 480 SER B CA 1 ATOM 3487 C C . SER B 2 256 ? 50.173 54.510 -7.436 1.00 40.55 ? 480 SER B C 1 ATOM 3488 O O . SER B 2 256 ? 50.564 53.608 -6.707 1.00 40.35 ? 480 SER B O 1 ATOM 3489 C CB . SER B 2 256 ? 52.189 53.951 -8.713 1.00 51.74 ? 480 SER B CB 1 ATOM 3490 O OG . SER B 2 256 ? 53.355 54.627 -9.135 1.00 59.61 ? 480 SER B OG 1 ATOM 3491 N N . PRO B 2 257 ? 49.040 55.171 -7.218 1.00 40.18 ? 481 PRO B N 1 ATOM 3492 C CA . PRO B 2 257 ? 48.223 54.797 -6.033 1.00 34.30 ? 481 PRO B CA 1 ATOM 3493 C C . PRO B 2 257 ? 47.803 53.325 -6.107 1.00 37.67 ? 481 PRO B C 1 ATOM 3494 O O . PRO B 2 257 ? 47.445 52.849 -7.158 1.00 36.15 ? 481 PRO B O 1 ATOM 3495 C CB . PRO B 2 257 ? 47.005 55.742 -6.108 1.00 38.36 ? 481 PRO B CB 1 ATOM 3496 C CG . PRO B 2 257 ? 47.113 56.513 -7.395 1.00 37.94 ? 481 PRO B CG 1 ATOM 3497 C CD . PRO B 2 257 ? 48.451 56.269 -8.019 1.00 43.05 ? 481 PRO B CD 1 ATOM 3498 N N . SER B 2 258 ? 47.743 52.631 -4.978 1.00 29.45 ? 482 SER B N 1 ATOM 3499 C CA . SER B 2 258 ? 47.307 51.245 -4.938 1.00 31.97 ? 482 SER B CA 1 ATOM 3500 C C . SER B 2 258 ? 46.480 51.050 -3.665 1.00 28.22 ? 482 SER B C 1 ATOM 3501 O O . SER B 2 258 ? 46.765 51.658 -2.646 1.00 33.50 ? 482 SER B O 1 ATOM 3502 C CB . SER B 2 258 ? 48.634 50.408 -4.822 1.00 31.44 ? 482 SER B CB 1 ATOM 3503 O OG . SER B 2 258 ? 48.303 49.100 -4.847 1.00 43.18 ? 482 SER B OG 1 ATOM 3504 N N . PRO B 2 259 ? 45.489 50.183 -3.674 1.00 29.21 ? 483 PRO B N 1 ATOM 3505 C CA . PRO B 2 259 ? 44.715 50.043 -2.410 1.00 29.40 ? 483 PRO B CA 1 ATOM 3506 C C . PRO B 2 259 ? 45.430 49.028 -1.418 1.00 24.29 ? 483 PRO B C 1 ATOM 3507 O O . PRO B 2 259 ? 45.046 47.871 -1.317 1.00 24.03 ? 483 PRO B O 1 ATOM 3508 C CB . PRO B 2 259 ? 43.383 49.491 -2.904 1.00 30.83 ? 483 PRO B CB 1 ATOM 3509 C CG . PRO B 2 259 ? 43.799 48.642 -4.072 1.00 28.02 ? 483 PRO B CG 1 ATOM 3510 C CD . PRO B 2 259 ? 44.927 49.381 -4.768 1.00 31.00 ? 483 PRO B CD 1 ATOM 3511 N N . GLY B 2 260 ? 46.506 49.500 -0.800 1.00 29.80 ? 484 GLY B N 1 ATOM 3512 C CA . GLY B 2 260 ? 47.182 48.711 0.218 1.00 26.25 ? 484 GLY B CA 1 ATOM 3513 C C . GLY B 2 260 ? 48.027 49.562 1.107 1.00 29.57 ? 484 GLY B C 1 ATOM 3514 O O . GLY B 2 260 ? 48.250 50.760 0.854 1.00 27.67 ? 484 GLY B O 1 ATOM 3515 N N . GLY B 2 261 ? 48.478 48.929 2.203 1.00 29.10 ? 485 GLY B N 1 ATOM 3516 C CA . GLY B 2 261 ? 49.333 49.594 3.199 1.00 29.11 ? 485 GLY B CA 1 ATOM 3517 C C . GLY B 2 261 ? 48.808 49.239 4.590 1.00 26.49 ? 485 GLY B C 1 ATOM 3518 O O . GLY B 2 261 ? 48.182 48.182 4.809 1.00 27.16 ? 485 GLY B O 1 ATOM 3519 N N . CYS B 2 262 ? 48.999 50.167 5.521 1.00 26.00 ? 486 CYS B N 1 ATOM 3520 C CA . CYS B 2 262 ? 48.655 49.897 6.897 1.00 26.57 ? 486 CYS B CA 1 ATOM 3521 C C . CYS B 2 262 ? 47.095 49.930 7.062 1.00 28.17 ? 486 CYS B C 1 ATOM 3522 O O . CYS B 2 262 ? 46.437 50.865 6.616 1.00 27.53 ? 486 CYS B O 1 ATOM 3523 C CB . CYS B 2 262 ? 49.337 50.947 7.726 1.00 25.23 ? 486 CYS B CB 1 ATOM 3524 S SG . CYS B 2 262 ? 49.004 50.866 9.505 1.00 29.92 ? 486 CYS B SG 1 ATOM 3525 N N . TYR B 2 263 ? 46.522 48.892 7.649 1.00 23.63 ? 487 TYR B N 1 ATOM 3526 C CA . TYR B 2 263 ? 45.078 48.851 7.757 1.00 23.47 ? 487 TYR B CA 1 ATOM 3527 C C . TYR B 2 263 ? 44.498 48.517 9.112 1.00 24.02 ? 487 TYR B C 1 ATOM 3528 O O . TYR B 2 263 ? 43.287 48.128 9.258 1.00 25.33 ? 487 TYR B O 1 ATOM 3529 C CB . TYR B 2 263 ? 44.507 47.967 6.631 1.00 24.96 ? 487 TYR B CB 1 ATOM 3530 C CG . TYR B 2 263 ? 44.879 46.480 6.593 1.00 22.85 ? 487 TYR B CG 1 ATOM 3531 C CD1 . TYR B 2 263 ? 44.859 45.672 7.739 1.00 23.30 ? 487 TYR B CD1 1 ATOM 3532 C CD2 . TYR B 2 263 ? 45.175 45.878 5.348 1.00 25.86 ? 487 TYR B CD2 1 ATOM 3533 C CE1 . TYR B 2 263 ? 45.100 44.278 7.628 1.00 22.90 ? 487 TYR B CE1 1 ATOM 3534 C CE2 . TYR B 2 263 ? 45.440 44.528 5.237 1.00 29.92 ? 487 TYR B CE2 1 ATOM 3535 C CZ . TYR B 2 263 ? 45.387 43.713 6.406 1.00 24.93 ? 487 TYR B CZ 1 ATOM 3536 O OH . TYR B 2 263 ? 45.684 42.348 6.272 1.00 29.17 ? 487 TYR B OH 1 ATOM 3537 N N . ASP B 2 264 ? 45.372 48.523 10.150 1.00 22.26 ? 488 ASP B N 1 ATOM 3538 C CA . ASP B 2 264 ? 44.870 48.209 11.518 1.00 20.86 ? 488 ASP B CA 1 ATOM 3539 C C . ASP B 2 264 ? 45.919 48.645 12.491 1.00 22.97 ? 488 ASP B C 1 ATOM 3540 O O . ASP B 2 264 ? 47.025 49.038 12.054 1.00 23.32 ? 488 ASP B O 1 ATOM 3541 C CB . ASP B 2 264 ? 44.416 46.743 11.771 1.00 23.40 ? 488 ASP B CB 1 ATOM 3542 C CG . ASP B 2 264 ? 45.619 45.736 11.855 1.00 22.56 ? 488 ASP B CG 1 ATOM 3543 O OD1 . ASP B 2 264 ? 46.641 46.173 12.399 1.00 21.79 ? 488 ASP B OD1 1 ATOM 3544 O OD2 . ASP B 2 264 ? 45.410 44.571 11.464 1.00 22.01 ? 488 ASP B OD2 1 ATOM 3545 N N . THR B 2 265 ? 45.514 48.736 13.752 1.00 23.99 ? 489 THR B N 1 ATOM 3546 C CA . THR B 2 265 ? 46.470 48.828 14.872 1.00 25.87 ? 489 THR B CA 1 ATOM 3547 C C . THR B 2 265 ? 45.835 48.059 16.010 1.00 27.54 ? 489 THR B C 1 ATOM 3548 O O . THR B 2 265 ? 44.618 48.271 16.331 1.00 28.43 ? 489 THR B O 1 ATOM 3549 C CB . THR B 2 265 ? 46.755 50.285 15.355 1.00 27.46 ? 489 THR B CB 1 ATOM 3550 O OG1 . THR B 2 265 ? 47.516 50.982 14.391 1.00 27.25 ? 489 THR B OG1 1 ATOM 3551 C CG2 . THR B 2 265 ? 47.674 50.232 16.618 1.00 24.92 ? 489 THR B CG2 1 ATOM 3552 N N . LYS B 2 266 ? 46.612 47.167 16.675 1.00 23.11 ? 490 LYS B N 1 ATOM 3553 C CA . LYS B 2 266 ? 46.118 46.538 17.889 1.00 21.88 ? 490 LYS B CA 1 ATOM 3554 C C . LYS B 2 266 ? 47.140 46.915 18.952 1.00 27.15 ? 490 LYS B C 1 ATOM 3555 O O . LYS B 2 266 ? 48.356 47.020 18.602 1.00 22.66 ? 490 LYS B O 1 ATOM 3556 C CB . LYS B 2 266 ? 45.974 45.027 17.741 1.00 22.19 ? 490 LYS B CB 1 ATOM 3557 C CG . LYS B 2 266 ? 44.989 44.409 16.723 1.00 21.67 ? 490 LYS B CG 1 ATOM 3558 C CD . LYS B 2 266 ? 45.499 44.531 15.260 1.00 19.72 ? 490 LYS B CD 1 ATOM 3559 C CE . LYS B 2 266 ? 46.948 43.924 15.118 1.00 19.91 ? 490 LYS B CE 1 ATOM 3560 N NZ . LYS B 2 266 ? 47.453 43.976 13.686 1.00 20.69 ? 490 LYS B NZ 1 ATOM 3561 N N . VAL B 2 267 ? 46.697 47.212 20.208 1.00 21.36 ? 491 VAL B N 1 ATOM 3562 C CA . VAL B 2 267 ? 47.635 47.674 21.237 1.00 23.60 ? 491 VAL B CA 1 ATOM 3563 C C . VAL B 2 267 ? 47.129 47.219 22.578 1.00 26.41 ? 491 VAL B C 1 ATOM 3564 O O . VAL B 2 267 ? 45.937 47.251 22.814 1.00 31.59 ? 491 VAL B O 1 ATOM 3565 C CB . VAL B 2 267 ? 47.846 49.201 21.169 1.00 25.68 ? 491 VAL B CB 1 ATOM 3566 C CG1 . VAL B 2 267 ? 46.499 49.993 21.134 1.00 29.81 ? 491 VAL B CG1 1 ATOM 3567 C CG2 . VAL B 2 267 ? 48.671 49.673 22.349 1.00 28.85 ? 491 VAL B CG2 1 ATOM 3568 N N . ALA B 2 268 ? 48.022 46.786 23.475 1.00 24.01 ? 492 ALA B N 1 ATOM 3569 C CA . ALA B 2 268 ? 47.612 46.454 24.817 1.00 20.02 ? 492 ALA B CA 1 ATOM 3570 C C . ALA B 2 268 ? 48.771 46.831 25.735 1.00 23.71 ? 492 ALA B C 1 ATOM 3571 O O . ALA B 2 268 ? 49.877 47.292 25.261 1.00 22.25 ? 492 ALA B O 1 ATOM 3572 C CB . ALA B 2 268 ? 47.178 44.959 24.920 1.00 23.91 ? 492 ALA B CB 1 ATOM 3573 N N . ASP B 2 269 ? 48.545 46.669 27.023 1.00 25.58 ? 493 ASP B N 1 ATOM 3574 C CA . ASP B 2 269 ? 49.630 46.779 28.019 1.00 26.28 ? 493 ASP B CA 1 ATOM 3575 C C . ASP B 2 269 ? 49.505 45.584 28.915 1.00 26.89 ? 493 ASP B C 1 ATOM 3576 O O . ASP B 2 269 ? 48.615 44.701 28.656 1.00 25.54 ? 493 ASP B O 1 ATOM 3577 C CB . ASP B 2 269 ? 49.568 48.154 28.746 1.00 27.10 ? 493 ASP B CB 1 ATOM 3578 C CG . ASP B 2 269 ? 48.278 48.325 29.651 1.00 29.42 ? 493 ASP B CG 1 ATOM 3579 O OD1 . ASP B 2 269 ? 47.585 47.335 29.992 1.00 27.58 ? 493 ASP B OD1 1 ATOM 3580 O OD2 . ASP B 2 269 ? 48.091 49.477 30.082 1.00 31.25 ? 493 ASP B OD2 1 ATOM 3581 N N . ILE B 2 270 ? 50.360 45.439 29.959 1.00 24.48 ? 494 ILE B N 1 ATOM 3582 C CA . ILE B 2 270 ? 50.314 44.184 30.714 1.00 26.17 ? 494 ILE B CA 1 ATOM 3583 C C . ILE B 2 270 ? 48.988 44.065 31.525 1.00 24.06 ? 494 ILE B C 1 ATOM 3584 O O . ILE B 2 270 ? 48.450 42.976 31.687 1.00 27.32 ? 494 ILE B O 1 ATOM 3585 C CB . ILE B 2 270 ? 51.571 44.010 31.656 1.00 28.31 ? 494 ILE B CB 1 ATOM 3586 C CG1 . ILE B 2 270 ? 51.521 42.685 32.402 1.00 30.40 ? 494 ILE B CG1 1 ATOM 3587 C CG2 . ILE B 2 270 ? 51.750 45.323 32.487 1.00 26.57 ? 494 ILE B CG2 1 ATOM 3588 C CD1 . ILE B 2 270 ? 52.841 42.206 33.054 1.00 27.82 ? 494 ILE B CD1 1 ATOM 3589 N N . TYR B 2 271 ? 48.443 45.164 31.971 1.00 25.54 ? 495 TYR B N 1 ATOM 3590 C CA . TYR B 2 271 ? 47.127 45.122 32.715 1.00 29.10 ? 495 TYR B CA 1 ATOM 3591 C C . TYR B 2 271 ? 45.997 44.654 31.772 1.00 30.14 ? 495 TYR B C 1 ATOM 3592 O O . TYR B 2 271 ? 45.226 43.734 32.114 1.00 32.56 ? 495 TYR B O 1 ATOM 3593 C CB . TYR B 2 271 ? 46.721 46.540 33.206 1.00 31.41 ? 495 TYR B CB 1 ATOM 3594 C CG . TYR B 2 271 ? 47.641 47.095 34.279 1.00 35.92 ? 495 TYR B CG 1 ATOM 3595 C CD1 . TYR B 2 271 ? 47.400 46.828 35.656 1.00 37.90 ? 495 TYR B CD1 1 ATOM 3596 C CD2 . TYR B 2 271 ? 48.771 47.897 33.916 1.00 31.63 ? 495 TYR B CD2 1 ATOM 3597 C CE1 . TYR B 2 271 ? 48.254 47.347 36.644 1.00 38.94 ? 495 TYR B CE1 1 ATOM 3598 C CE2 . TYR B 2 271 ? 49.626 48.407 34.912 1.00 36.93 ? 495 TYR B CE2 1 ATOM 3599 C CZ . TYR B 2 271 ? 49.345 48.127 36.276 1.00 40.29 ? 495 TYR B CZ 1 ATOM 3600 O OH . TYR B 2 271 ? 50.206 48.607 37.238 1.00 37.84 ? 495 TYR B OH 1 ATOM 3601 N N . LEU B 2 272 ? 45.865 45.322 30.618 1.00 31.06 ? 496 LEU B N 1 ATOM 3602 C CA . LEU B 2 272 ? 44.828 44.837 29.646 1.00 32.93 ? 496 LEU B CA 1 ATOM 3603 C C . LEU B 2 272 ? 44.995 43.377 29.265 1.00 32.82 ? 496 LEU B C 1 ATOM 3604 O O . LEU B 2 272 ? 44.044 42.613 29.264 1.00 28.31 ? 496 LEU B O 1 ATOM 3605 C CB . LEU B 2 272 ? 44.842 45.698 28.393 1.00 30.06 ? 496 LEU B CB 1 ATOM 3606 C CG . LEU B 2 272 ? 44.484 47.143 28.715 1.00 34.65 ? 496 LEU B CG 1 ATOM 3607 C CD1 . LEU B 2 272 ? 44.936 47.996 27.567 1.00 32.58 ? 496 LEU B CD1 1 ATOM 3608 C CD2 . LEU B 2 272 ? 42.962 47.254 28.840 1.00 33.00 ? 496 LEU B CD2 1 ATOM 3609 N N . ALA B 2 273 ? 46.232 42.946 28.973 1.00 30.95 ? 497 ALA B N 1 ATOM 3610 C CA . ALA B 2 273 ? 46.454 41.568 28.560 1.00 29.00 ? 497 ALA B CA 1 ATOM 3611 C C . ALA B 2 273 ? 46.082 40.513 29.582 1.00 31.61 ? 497 ALA B C 1 ATOM 3612 O O . ALA B 2 273 ? 45.665 39.419 29.166 1.00 29.69 ? 497 ALA B O 1 ATOM 3613 C CB . ALA B 2 273 ? 47.906 41.308 28.076 1.00 31.96 ? 497 ALA B CB 1 ATOM 3614 N N . SER B 2 274 ? 46.224 40.790 30.879 1.00 31.21 ? 498 SER B N 1 ATOM 3615 C CA . SER B 2 274 ? 45.902 39.809 31.889 1.00 34.35 ? 498 SER B CA 1 ATOM 3616 C C . SER B 2 274 ? 44.406 39.552 31.909 1.00 33.06 ? 498 SER B C 1 ATOM 3617 O O . SER B 2 274 ? 44.005 38.554 32.391 1.00 36.97 ? 498 SER B O 1 ATOM 3618 C CB . SER B 2 274 ? 46.429 40.186 33.292 1.00 38.19 ? 498 SER B CB 1 ATOM 3619 O OG . SER B 2 274 ? 45.847 41.406 33.721 1.00 38.23 ? 498 SER B OG 1 ATOM 3620 N N . LYS B 2 275 ? 43.606 40.427 31.308 1.00 34.31 ? 499 LYS B N 1 ATOM 3621 C CA . LYS B 2 275 ? 42.176 40.168 31.140 1.00 36.37 ? 499 LYS B CA 1 ATOM 3622 C C . LYS B 2 275 ? 41.837 39.832 29.649 1.00 36.89 ? 499 LYS B C 1 ATOM 3623 O O . LYS B 2 275 ? 40.682 39.945 29.205 1.00 34.52 ? 499 LYS B O 1 ATOM 3624 C CB . LYS B 2 275 ? 41.444 41.402 31.612 1.00 39.11 ? 499 LYS B CB 1 ATOM 3625 C CG . LYS B 2 275 ? 41.646 41.671 33.120 1.00 41.65 ? 499 LYS B CG 1 ATOM 3626 C CD . LYS B 2 275 ? 41.152 43.082 33.444 1.00 53.55 ? 499 LYS B CD 1 ATOM 3627 C CE . LYS B 2 275 ? 40.728 43.256 34.905 1.00 64.04 ? 499 LYS B CE 1 ATOM 3628 N NZ . LYS B 2 275 ? 39.384 43.925 35.031 1.00 62.73 ? 499 LYS B NZ 1 ATOM 3629 N N . TYR B 2 276 ? 42.855 39.444 28.861 1.00 27.54 ? 500 TYR B N 1 ATOM 3630 C CA . TYR B 2 276 ? 42.652 39.234 27.396 1.00 30.04 ? 500 TYR B CA 1 ATOM 3631 C C . TYR B 2 276 ? 42.010 40.441 26.633 1.00 29.99 ? 500 TYR B C 1 ATOM 3632 O O . TYR B 2 276 ? 41.320 40.266 25.627 1.00 29.24 ? 500 TYR B O 1 ATOM 3633 C CB . TYR B 2 276 ? 41.790 37.984 27.144 1.00 30.23 ? 500 TYR B CB 1 ATOM 3634 C CG . TYR B 2 276 ? 42.318 36.744 27.776 1.00 33.19 ? 500 TYR B CG 1 ATOM 3635 C CD1 . TYR B 2 276 ? 43.307 35.989 27.146 1.00 31.29 ? 500 TYR B CD1 1 ATOM 3636 C CD2 . TYR B 2 276 ? 41.842 36.312 29.032 1.00 31.43 ? 500 TYR B CD2 1 ATOM 3637 C CE1 . TYR B 2 276 ? 43.838 34.861 27.743 1.00 29.59 ? 500 TYR B CE1 1 ATOM 3638 C CE2 . TYR B 2 276 ? 42.333 35.160 29.621 1.00 30.49 ? 500 TYR B CE2 1 ATOM 3639 C CZ . TYR B 2 276 ? 43.324 34.454 28.992 1.00 35.16 ? 500 TYR B CZ 1 ATOM 3640 O OH . TYR B 2 276 ? 43.814 33.321 29.601 1.00 32.24 ? 500 TYR B OH 1 ATOM 3641 N N . LYS B 2 277 ? 42.304 41.632 27.083 1.00 29.79 ? 501 LYS B N 1 ATOM 3642 C CA . LYS B 2 277 ? 41.862 42.862 26.489 1.00 30.48 ? 501 LYS B CA 1 ATOM 3643 C C . LYS B 2 277 ? 42.887 43.524 25.635 1.00 28.31 ? 501 LYS B C 1 ATOM 3644 O O . LYS B 2 277 ? 44.077 43.555 25.994 1.00 28.72 ? 501 LYS B O 1 ATOM 3645 C CB . LYS B 2 277 ? 41.567 43.866 27.607 1.00 33.71 ? 501 LYS B CB 1 ATOM 3646 C CG . LYS B 2 277 ? 40.361 43.492 28.461 1.00 46.52 ? 501 LYS B CG 1 ATOM 3647 C CD . LYS B 2 277 ? 39.987 44.596 29.480 1.00 41.38 ? 501 LYS B CD 1 ATOM 3648 C CE . LYS B 2 277 ? 38.972 44.082 30.511 1.00 56.71 ? 501 LYS B CE 1 ATOM 3649 N NZ . LYS B 2 277 ? 38.916 44.842 31.798 1.00 62.59 ? 501 LYS B NZ 1 ATOM 3650 N N . ALA B 2 278 ? 42.427 44.150 24.554 1.00 26.60 ? 502 ALA B N 1 ATOM 3651 C CA . ALA B 2 278 ? 43.215 45.004 23.708 1.00 25.33 ? 502 ALA B CA 1 ATOM 3652 C C . ALA B 2 278 ? 42.332 46.066 23.095 1.00 28.01 ? 502 ALA B C 1 ATOM 3653 O O . ALA B 2 278 ? 41.114 45.871 23.040 1.00 29.24 ? 502 ALA B O 1 ATOM 3654 C CB . ALA B 2 278 ? 43.959 44.219 22.582 1.00 24.87 ? 502 ALA B CB 1 ATOM 3655 N N . TYR B 2 279 ? 42.947 47.180 22.690 1.00 25.35 ? 503 TYR B N 1 ATOM 3656 C CA . TYR B 2 279 ? 42.309 48.187 21.835 1.00 28.59 ? 503 TYR B CA 1 ATOM 3657 C C . TYR B 2 279 ? 42.671 47.906 20.364 1.00 29.58 ? 503 TYR B C 1 ATOM 3658 O O . TYR B 2 279 ? 43.837 47.648 20.057 1.00 29.07 ? 503 TYR B O 1 ATOM 3659 C CB . TYR B 2 279 ? 42.763 49.611 22.181 1.00 23.61 ? 503 TYR B CB 1 ATOM 3660 C CG . TYR B 2 279 ? 42.481 49.911 23.661 1.00 30.13 ? 503 TYR B CG 1 ATOM 3661 C CD1 . TYR B 2 279 ? 41.233 49.592 24.234 1.00 36.88 ? 503 TYR B CD1 1 ATOM 3662 C CD2 . TYR B 2 279 ? 43.460 50.468 24.470 1.00 32.23 ? 503 TYR B CD2 1 ATOM 3663 C CE1 . TYR B 2 279 ? 40.993 49.831 25.584 1.00 37.03 ? 503 TYR B CE1 1 ATOM 3664 C CE2 . TYR B 2 279 ? 43.245 50.706 25.811 1.00 33.49 ? 503 TYR B CE2 1 ATOM 3665 C CZ . TYR B 2 279 ? 42.016 50.369 26.349 1.00 37.74 ? 503 TYR B CZ 1 ATOM 3666 O OH . TYR B 2 279 ? 41.819 50.636 27.658 1.00 42.45 ? 503 TYR B OH 1 ATOM 3667 N N . ALA B 2 280 ? 41.707 47.931 19.439 1.00 25.29 ? 504 ALA B N 1 ATOM 3668 C CA . ALA B 2 280 ? 41.986 47.534 18.025 1.00 26.35 ? 504 ALA B CA 1 ATOM 3669 C C . ALA B 2 280 ? 41.232 48.495 17.107 1.00 29.68 ? 504 ALA B C 1 ATOM 3670 O O . ALA B 2 280 ? 40.044 48.707 17.350 1.00 28.73 ? 504 ALA B O 1 ATOM 3671 C CB . ALA B 2 280 ? 41.515 46.105 17.758 1.00 23.60 ? 504 ALA B CB 1 ATOM 3672 N N . ILE B 2 281 ? 41.890 49.094 16.123 1.00 26.52 ? 505 ILE B N 1 ATOM 3673 C CA . ILE B 2 281 ? 41.205 49.938 15.104 1.00 26.14 ? 505 ILE B CA 1 ATOM 3674 C C . ILE B 2 281 ? 41.388 49.269 13.745 1.00 30.74 ? 505 ILE B C 1 ATOM 3675 O O . ILE B 2 281 ? 42.493 48.766 13.468 1.00 29.43 ? 505 ILE B O 1 ATOM 3676 C CB . ILE B 2 281 ? 41.739 51.367 15.148 1.00 26.16 ? 505 ILE B CB 1 ATOM 3677 C CG1 . ILE B 2 281 ? 40.945 52.305 14.190 1.00 29.37 ? 505 ILE B CG1 1 ATOM 3678 C CG2 . ILE B 2 281 ? 43.252 51.448 14.703 1.00 20.89 ? 505 ILE B CG2 1 ATOM 3679 C CD1 . ILE B 2 281 ? 41.498 53.698 14.258 1.00 30.62 ? 505 ILE B CD1 1 ATOM 3680 N N . SER B 2 282 ? 40.309 49.171 12.926 1.00 25.59 ? 506 SER B N 1 ATOM 3681 C CA . SER B 2 282 ? 40.363 48.655 11.556 1.00 27.74 ? 506 SER B CA 1 ATOM 3682 C C . SER B 2 282 ? 40.244 49.797 10.559 1.00 35.10 ? 506 SER B C 1 ATOM 3683 O O . SER B 2 282 ? 39.263 50.551 10.591 1.00 31.15 ? 506 SER B O 1 ATOM 3684 C CB . SER B 2 282 ? 39.276 47.613 11.367 1.00 26.84 ? 506 SER B CB 1 ATOM 3685 O OG . SER B 2 282 ? 39.241 47.207 10.025 1.00 24.66 ? 506 SER B OG 1 ATOM 3686 N N . GLY B 2 283 ? 41.293 49.984 9.753 1.00 28.92 ? 507 GLY B N 1 ATOM 3687 C CA . GLY B 2 283 ? 41.273 50.903 8.629 1.00 25.30 ? 507 GLY B CA 1 ATOM 3688 C C . GLY B 2 283 ? 42.542 51.689 8.434 1.00 28.66 ? 507 GLY B C 1 ATOM 3689 O O . GLY B 2 283 ? 43.329 51.846 9.380 1.00 27.60 ? 507 GLY B O 1 ATOM 3690 N N . PRO B 2 284 ? 42.753 52.223 7.221 1.00 25.30 ? 508 PRO B N 1 ATOM 3691 C CA . PRO B 2 284 ? 43.927 53.009 7.013 1.00 24.60 ? 508 PRO B CA 1 ATOM 3692 C C . PRO B 2 284 ? 43.880 54.225 7.900 1.00 29.64 ? 508 PRO B C 1 ATOM 3693 O O . PRO B 2 284 ? 42.761 54.693 8.259 1.00 27.40 ? 508 PRO B O 1 ATOM 3694 C CB . PRO B 2 284 ? 43.915 53.306 5.474 1.00 22.22 ? 508 PRO B CB 1 ATOM 3695 C CG . PRO B 2 284 ? 42.960 52.326 4.889 1.00 22.67 ? 508 PRO B CG 1 ATOM 3696 C CD . PRO B 2 284 ? 41.984 51.971 5.988 1.00 25.11 ? 508 PRO B CD 1 ATOM 3697 N N . THR B 2 285 ? 45.069 54.736 8.251 1.00 28.01 ? 509 THR B N 1 ATOM 3698 C CA . THR B 2 285 ? 45.178 55.782 9.267 1.00 25.54 ? 509 THR B CA 1 ATOM 3699 C C . THR B 2 285 ? 44.684 57.125 8.695 1.00 26.73 ? 509 THR B C 1 ATOM 3700 O O . THR B 2 285 ? 45.059 57.497 7.591 1.00 27.79 ? 509 THR B O 1 ATOM 3701 C CB . THR B 2 285 ? 46.573 55.957 9.872 1.00 25.95 ? 509 THR B CB 1 ATOM 3702 O OG1 . THR B 2 285 ? 46.533 56.980 10.879 1.00 27.74 ? 509 THR B OG1 1 ATOM 3703 C CG2 . THR B 2 285 ? 47.605 56.330 8.832 1.00 21.41 ? 509 THR B CG2 1 ATOM 3704 N N . VAL B 2 286 ? 43.937 57.864 9.536 1.00 28.44 ? 510 VAL B N 1 ATOM 3705 C CA . VAL B 2 286 ? 43.493 59.209 9.165 1.00 33.89 ? 510 VAL B CA 1 ATOM 3706 C C . VAL B 2 286 ? 44.201 60.149 10.073 1.00 39.51 ? 510 VAL B C 1 ATOM 3707 O O . VAL B 2 286 ? 44.052 61.377 9.983 1.00 33.29 ? 510 VAL B O 1 ATOM 3708 C CB . VAL B 2 286 ? 41.909 59.285 9.288 1.00 29.17 ? 510 VAL B CB 1 ATOM 3709 C CG1 . VAL B 2 286 ? 41.305 58.197 8.415 1.00 33.48 ? 510 VAL B CG1 1 ATOM 3710 C CG2 . VAL B 2 286 ? 41.432 59.067 10.751 1.00 30.41 ? 510 VAL B CG2 1 ATOM 3711 N N . GLN B 2 287 ? 45.039 59.597 10.953 1.00 32.51 ? 511 GLN B N 1 ATOM 3712 C CA . GLN B 2 287 ? 45.803 60.473 11.840 1.00 36.75 ? 511 GLN B CA 1 ATOM 3713 C C . GLN B 2 287 ? 46.461 61.698 11.169 1.00 33.69 ? 511 GLN B C 1 ATOM 3714 O O . GLN B 2 287 ? 47.060 61.593 10.148 1.00 36.43 ? 511 GLN B O 1 ATOM 3715 C CB . GLN B 2 287 ? 46.855 59.688 12.609 1.00 40.54 ? 511 GLN B CB 1 ATOM 3716 C CG . GLN B 2 287 ? 47.391 60.446 13.800 1.00 40.30 ? 511 GLN B CG 1 ATOM 3717 C CD . GLN B 2 287 ? 48.012 59.480 14.794 1.00 39.77 ? 511 GLN B CD 1 ATOM 3718 O OE1 . GLN B 2 287 ? 47.307 58.898 15.684 1.00 34.99 ? 511 GLN B OE1 1 ATOM 3719 N NE2 . GLN B 2 287 ? 49.370 59.347 14.682 1.00 32.81 ? 511 GLN B NE2 1 ATOM 3720 N N . GLY B 2 288 ? 46.339 62.867 11.811 1.00 33.92 ? 512 GLY B N 1 ATOM 3721 C CA . GLY B 2 288 ? 47.016 64.057 11.361 1.00 32.28 ? 512 GLY B CA 1 ATOM 3722 C C . GLY B 2 288 ? 46.287 64.675 10.158 1.00 36.97 ? 512 GLY B C 1 ATOM 3723 O O . GLY B 2 288 ? 46.917 65.376 9.387 1.00 43.36 ? 512 GLY B O 1 ATOM 3724 N N . GLY B 2 289 ? 45.005 64.354 9.955 1.00 40.14 ? 513 GLY B N 1 ATOM 3725 C CA . GLY B 2 289 ? 44.200 64.917 8.849 1.00 40.35 ? 513 GLY B CA 1 ATOM 3726 C C . GLY B 2 289 ? 44.348 64.252 7.482 1.00 47.32 ? 513 GLY B C 1 ATOM 3727 O O . GLY B 2 289 ? 44.061 64.869 6.481 1.00 37.47 ? 513 GLY B O 1 ATOM 3728 N N . LEU B 2 290 ? 44.841 63.014 7.416 1.00 35.55 ? 514 LEU B N 1 ATOM 3729 C CA . LEU B 2 290 ? 44.837 62.275 6.168 1.00 34.32 ? 514 LEU B CA 1 ATOM 3730 C C . LEU B 2 290 ? 43.411 61.908 5.764 1.00 29.08 ? 514 LEU B C 1 ATOM 3731 O O . LEU B 2 290 ? 42.586 61.610 6.624 1.00 33.09 ? 514 LEU B O 1 ATOM 3732 C CB . LEU B 2 290 ? 45.595 60.924 6.336 1.00 31.51 ? 514 LEU B CB 1 ATOM 3733 C CG . LEU B 2 290 ? 47.076 61.213 6.525 1.00 34.00 ? 514 LEU B CG 1 ATOM 3734 C CD1 . LEU B 2 290 ? 47.811 59.952 6.979 1.00 32.85 ? 514 LEU B CD1 1 ATOM 3735 C CD2 . LEU B 2 290 ? 47.658 61.789 5.251 1.00 30.79 ? 514 LEU B CD2 1 ATOM 3736 N N . PRO B 2 291 ? 43.162 61.804 4.467 1.00 34.48 ? 515 PRO B N 1 ATOM 3737 C CA . PRO B 2 291 ? 41.790 61.520 3.965 1.00 32.94 ? 515 PRO B CA 1 ATOM 3738 C C . PRO B 2 291 ? 41.293 60.142 4.340 1.00 43.83 ? 515 PRO B C 1 ATOM 3739 O O . PRO B 2 291 ? 42.070 59.139 4.330 1.00 38.56 ? 515 PRO B O 1 ATOM 3740 C CB . PRO B 2 291 ? 41.913 61.664 2.461 1.00 31.64 ? 515 PRO B CB 1 ATOM 3741 C CG . PRO B 2 291 ? 43.404 61.653 2.164 1.00 39.15 ? 515 PRO B CG 1 ATOM 3742 C CD . PRO B 2 291 ? 44.120 62.137 3.397 1.00 29.94 ? 515 PRO B CD 1 ATOM 3743 N N . VAL B 2 292 ? 39.996 60.060 4.655 1.00 31.84 ? 516 VAL B N 1 ATOM 3744 C CA . VAL B 2 292 ? 39.405 58.783 4.937 1.00 31.76 ? 516 VAL B CA 1 ATOM 3745 C C . VAL B 2 292 ? 39.551 57.877 3.722 1.00 32.58 ? 516 VAL B C 1 ATOM 3746 O O . VAL B 2 292 ? 39.283 58.286 2.580 1.00 33.26 ? 516 VAL B O 1 ATOM 3747 C CB . VAL B 2 292 ? 37.900 58.957 5.351 1.00 29.89 ? 516 VAL B CB 1 ATOM 3748 C CG1 . VAL B 2 292 ? 37.148 57.601 5.363 1.00 29.14 ? 516 VAL B CG1 1 ATOM 3749 C CG2 . VAL B 2 292 ? 37.810 59.594 6.711 1.00 29.07 ? 516 VAL B CG2 1 ATOM 3750 N N . PHE B 2 293 ? 39.939 56.608 3.905 1.00 34.00 ? 517 PHE B N 1 ATOM 3751 C CA . PHE B 2 293 ? 39.913 55.711 2.769 1.00 29.97 ? 517 PHE B CA 1 ATOM 3752 C C . PHE B 2 293 ? 38.472 55.283 2.319 1.00 28.45 ? 517 PHE B C 1 ATOM 3753 O O . PHE B 2 293 ? 37.665 54.727 3.091 1.00 28.36 ? 517 PHE B O 1 ATOM 3754 C CB . PHE B 2 293 ? 40.741 54.388 3.030 1.00 30.98 ? 517 PHE B CB 1 ATOM 3755 C CG . PHE B 2 293 ? 40.665 53.437 1.887 1.00 27.95 ? 517 PHE B CG 1 ATOM 3756 C CD1 . PHE B 2 293 ? 41.433 53.668 0.763 1.00 25.62 ? 517 PHE B CD1 1 ATOM 3757 C CD2 . PHE B 2 293 ? 39.833 52.310 1.935 1.00 30.34 ? 517 PHE B CD2 1 ATOM 3758 C CE1 . PHE B 2 293 ? 41.354 52.828 -0.341 1.00 27.29 ? 517 PHE B CE1 1 ATOM 3759 C CE2 . PHE B 2 293 ? 39.758 51.450 0.846 1.00 27.04 ? 517 PHE B CE2 1 ATOM 3760 C CZ . PHE B 2 293 ? 40.484 51.730 -0.304 1.00 26.49 ? 517 PHE B CZ 1 ATOM 3761 N N . HIS B 2 294 ? 38.271 55.365 1.011 1.00 31.21 ? 518 HIS B N 1 ATOM 3762 C CA . HIS B 2 294 ? 36.985 55.057 0.337 1.00 32.62 ? 518 HIS B CA 1 ATOM 3763 C C . HIS B 2 294 ? 37.237 54.115 -0.753 1.00 26.30 ? 518 HIS B C 1 ATOM 3764 O O . HIS B 2 294 ? 38.064 54.374 -1.649 1.00 29.43 ? 518 HIS B O 1 ATOM 3765 C CB . HIS B 2 294 ? 36.358 56.370 -0.259 1.00 31.78 ? 518 HIS B CB 1 ATOM 3766 C CG . HIS B 2 294 ? 35.693 57.247 0.793 1.00 35.57 ? 518 HIS B CG 1 ATOM 3767 N ND1 . HIS B 2 294 ? 34.355 57.093 1.159 1.00 31.55 ? 518 HIS B ND1 1 ATOM 3768 C CD2 . HIS B 2 294 ? 36.187 58.332 1.532 1.00 32.27 ? 518 HIS B CD2 1 ATOM 3769 C CE1 . HIS B 2 294 ? 34.058 58.001 2.128 1.00 35.90 ? 518 HIS B CE1 1 ATOM 3770 N NE2 . HIS B 2 294 ? 35.170 58.760 2.360 1.00 39.21 ? 518 HIS B NE2 1 ATOM 3771 N N . TRP B 2 295 ? 36.520 53.023 -0.728 1.00 27.78 ? 519 TRP B N 1 ATOM 3772 C CA . TRP B 2 295 ? 36.646 52.025 -1.769 1.00 28.09 ? 519 TRP B CA 1 ATOM 3773 C C . TRP B 2 295 ? 36.254 52.566 -3.147 1.00 35.76 ? 519 TRP B C 1 ATOM 3774 O O . TRP B 2 295 ? 36.674 52.039 -4.211 1.00 31.81 ? 519 TRP B O 1 ATOM 3775 C CB . TRP B 2 295 ? 35.778 50.862 -1.398 1.00 29.78 ? 519 TRP B CB 1 ATOM 3776 C CG . TRP B 2 295 ? 36.549 49.771 -0.620 1.00 32.94 ? 519 TRP B CG 1 ATOM 3777 C CD1 . TRP B 2 295 ? 36.283 49.262 0.664 1.00 32.99 ? 519 TRP B CD1 1 ATOM 3778 C CD2 . TRP B 2 295 ? 37.728 49.046 -1.107 1.00 30.04 ? 519 TRP B CD2 1 ATOM 3779 N NE1 . TRP B 2 295 ? 37.242 48.282 1.010 1.00 34.07 ? 519 TRP B NE1 1 ATOM 3780 C CE2 . TRP B 2 295 ? 38.159 48.149 -0.016 1.00 29.50 ? 519 TRP B CE2 1 ATOM 3781 C CE3 . TRP B 2 295 ? 38.484 49.092 -2.279 1.00 28.61 ? 519 TRP B CE3 1 ATOM 3782 C CZ2 . TRP B 2 295 ? 39.272 47.307 -0.159 1.00 30.51 ? 519 TRP B CZ2 1 ATOM 3783 C CZ3 . TRP B 2 295 ? 39.631 48.240 -2.401 1.00 35.48 ? 519 TRP B CZ3 1 ATOM 3784 C CH2 . TRP B 2 295 ? 39.999 47.375 -1.351 1.00 27.47 ? 519 TRP B CH2 1 ATOM 3785 N N . SER B 2 296 ? 35.473 53.665 -3.141 1.00 33.00 ? 520 SER B N 1 ATOM 3786 C CA . SER B 2 296 ? 34.913 54.192 -4.403 1.00 35.63 ? 520 SER B CA 1 ATOM 3787 C C . SER B 2 296 ? 36.077 54.559 -5.285 1.00 36.66 ? 520 SER B C 1 ATOM 3788 O O . SER B 2 296 ? 36.008 54.408 -6.500 1.00 38.55 ? 520 SER B O 1 ATOM 3789 C CB . SER B 2 296 ? 33.998 55.416 -4.091 1.00 29.31 ? 520 SER B CB 1 ATOM 3790 O OG . SER B 2 296 ? 34.741 56.518 -3.612 1.00 31.10 ? 520 SER B OG 1 ATOM 3791 N N . ARG B 2 297 ? 37.184 54.967 -4.678 1.00 33.71 ? 521 ARG B N 1 ATOM 3792 C CA . ARG B 2 297 ? 38.359 55.342 -5.471 1.00 33.93 ? 521 ARG B CA 1 ATOM 3793 C C . ARG B 2 297 ? 39.132 54.147 -6.088 1.00 35.17 ? 521 ARG B C 1 ATOM 3794 O O . ARG B 2 297 ? 39.986 54.349 -6.942 1.00 38.45 ? 521 ARG B O 1 ATOM 3795 C CB . ARG B 2 297 ? 39.272 56.285 -4.668 1.00 38.61 ? 521 ARG B CB 1 ATOM 3796 C CG . ARG B 2 297 ? 40.597 56.577 -5.372 1.00 44.45 ? 521 ARG B CG 1 ATOM 3797 C CD . ARG B 2 297 ? 41.341 57.727 -4.704 1.00 45.24 ? 521 ARG B CD 1 ATOM 3798 N NE . ARG B 2 297 ? 42.522 58.153 -5.474 1.00 51.81 ? 521 ARG B NE 1 ATOM 3799 C CZ . ARG B 2 297 ? 43.775 58.258 -4.998 1.00 52.66 ? 521 ARG B CZ 1 ATOM 3800 N NH1 . ARG B 2 297 ? 44.053 57.983 -3.714 1.00 47.53 ? 521 ARG B NH1 1 ATOM 3801 N NH2 . ARG B 2 297 ? 44.755 58.671 -5.803 1.00 53.89 ? 521 ARG B NH2 1 ATOM 3802 N N . PHE B 2 298 ? 38.803 52.910 -5.697 1.00 31.68 ? 522 PHE B N 1 ATOM 3803 C CA . PHE B 2 298 ? 39.491 51.704 -6.222 1.00 29.80 ? 522 PHE B CA 1 ATOM 3804 C C . PHE B 2 298 ? 38.436 50.697 -6.459 1.00 35.69 ? 522 PHE B C 1 ATOM 3805 O O . PHE B 2 298 ? 38.423 49.570 -5.898 1.00 37.27 ? 522 PHE B O 1 ATOM 3806 C CB . PHE B 2 298 ? 40.490 51.196 -5.128 1.00 29.90 ? 522 PHE B CB 1 ATOM 3807 C CG . PHE B 2 298 ? 41.621 52.138 -4.912 1.00 28.04 ? 522 PHE B CG 1 ATOM 3808 C CD1 . PHE B 2 298 ? 42.713 52.125 -5.765 1.00 30.61 ? 522 PHE B CD1 1 ATOM 3809 C CD2 . PHE B 2 298 ? 41.545 53.066 -3.912 1.00 28.85 ? 522 PHE B CD2 1 ATOM 3810 C CE1 . PHE B 2 298 ? 43.739 53.027 -5.609 1.00 36.17 ? 522 PHE B CE1 1 ATOM 3811 C CE2 . PHE B 2 298 ? 42.564 53.966 -3.735 1.00 27.76 ? 522 PHE B CE2 1 ATOM 3812 C CZ . PHE B 2 298 ? 43.663 53.948 -4.593 1.00 30.66 ? 522 PHE B CZ 1 ATOM 3813 N N . ASN B 2 299 ? 37.487 51.080 -7.308 1.00 35.60 ? 523 ASN B N 1 ATOM 3814 C CA . ASN B 2 299 ? 36.223 50.341 -7.306 1.00 36.31 ? 523 ASN B CA 1 ATOM 3815 C C . ASN B 2 299 ? 36.284 49.091 -8.163 1.00 40.82 ? 523 ASN B C 1 ATOM 3816 O O . ASN B 2 299 ? 35.358 48.282 -8.142 1.00 43.19 ? 523 ASN B O 1 ATOM 3817 C CB . ASN B 2 299 ? 35.037 51.267 -7.660 1.00 42.00 ? 523 ASN B CB 1 ATOM 3818 C CG . ASN B 2 299 ? 35.199 51.956 -9.013 1.00 47.61 ? 523 ASN B CG 1 ATOM 3819 O OD1 . ASN B 2 299 ? 35.834 51.431 -9.921 1.00 37.85 ? 523 ASN B OD1 1 ATOM 3820 N ND2 . ASN B 2 299 ? 34.598 53.163 -9.155 1.00 60.50 ? 523 ASN B ND2 1 ATOM 3821 N N . LYS B 2 300 ? 37.388 48.888 -8.878 1.00 32.67 ? 524 LYS B N 1 ATOM 3822 C CA . LYS B 2 300 ? 37.563 47.567 -9.515 1.00 34.82 ? 524 LYS B CA 1 ATOM 3823 C C . LYS B 2 300 ? 38.186 46.457 -8.656 1.00 37.42 ? 524 LYS B C 1 ATOM 3824 O O . LYS B 2 300 ? 38.366 45.390 -9.145 1.00 40.38 ? 524 LYS B O 1 ATOM 3825 C CB . LYS B 2 300 ? 38.418 47.757 -10.763 1.00 41.30 ? 524 LYS B CB 1 ATOM 3826 C CG . LYS B 2 300 ? 37.727 48.639 -11.834 1.00 45.21 ? 524 LYS B CG 1 ATOM 3827 C CD . LYS B 2 300 ? 38.322 48.271 -13.190 1.00 60.15 ? 524 LYS B CD 1 ATOM 3828 C CE . LYS B 2 300 ? 38.150 49.359 -14.242 1.00 64.41 ? 524 LYS B CE 1 ATOM 3829 N NZ . LYS B 2 300 ? 36.709 49.409 -14.606 1.00 76.37 ? 524 LYS B NZ 1 ATOM 3830 N N . THR B 2 301 ? 38.555 46.717 -7.404 1.00 37.49 ? 525 THR B N 1 ATOM 3831 C CA . THR B 2 301 ? 39.062 45.680 -6.485 1.00 29.91 ? 525 THR B CA 1 ATOM 3832 C C . THR B 2 301 ? 37.907 45.112 -5.711 1.00 33.27 ? 525 THR B C 1 ATOM 3833 O O . THR B 2 301 ? 37.195 45.852 -5.042 1.00 33.89 ? 525 THR B O 1 ATOM 3834 C CB . THR B 2 301 ? 40.079 46.330 -5.529 1.00 35.72 ? 525 THR B CB 1 ATOM 3835 O OG1 . THR B 2 301 ? 41.149 46.826 -6.321 1.00 28.53 ? 525 THR B OG1 1 ATOM 3836 C CG2 . THR B 2 301 ? 40.654 45.339 -4.470 1.00 30.21 ? 525 THR B CG2 1 ATOM 3837 N N . LEU B 2 302 ? 37.724 43.795 -5.800 1.00 29.37 ? 526 LEU B N 1 ATOM 3838 C CA . LEU B 2 302 ? 36.756 43.074 -4.959 1.00 28.55 ? 526 LEU B CA 1 ATOM 3839 C C . LEU B 2 302 ? 37.017 43.238 -3.476 1.00 33.58 ? 526 LEU B C 1 ATOM 3840 O O . LEU B 2 302 ? 38.191 43.123 -3.011 1.00 29.50 ? 526 LEU B O 1 ATOM 3841 C CB . LEU B 2 302 ? 36.793 41.593 -5.330 1.00 31.34 ? 526 LEU B CB 1 ATOM 3842 C CG . LEU B 2 302 ? 36.267 41.326 -6.777 1.00 35.07 ? 526 LEU B CG 1 ATOM 3843 C CD1 . LEU B 2 302 ? 36.572 39.904 -7.150 1.00 29.42 ? 526 LEU B CD1 1 ATOM 3844 C CD2 . LEU B 2 302 ? 34.752 41.496 -6.793 1.00 38.53 ? 526 LEU B CD2 1 ATOM 3845 N N . HIS B 2 303 ? 35.931 43.459 -2.727 1.00 31.59 ? 527 HIS B N 1 ATOM 3846 C CA . HIS B 2 303 ? 35.961 43.847 -1.300 1.00 28.95 ? 527 HIS B CA 1 ATOM 3847 C C . HIS B 2 303 ? 34.591 43.505 -0.754 1.00 31.12 ? 527 HIS B C 1 ATOM 3848 O O . HIS B 2 303 ? 34.047 44.160 0.110 1.00 33.37 ? 527 HIS B O 1 ATOM 3849 C CB . HIS B 2 303 ? 36.410 45.285 -1.111 1.00 33.49 ? 527 HIS B CB 1 ATOM 3850 C CG . HIS B 2 303 ? 35.501 46.321 -1.772 1.00 35.72 ? 527 HIS B CG 1 ATOM 3851 N ND1 . HIS B 2 303 ? 35.697 46.789 -3.040 1.00 34.97 ? 527 HIS B ND1 1 ATOM 3852 C CD2 . HIS B 2 303 ? 34.344 46.952 -1.300 1.00 36.77 ? 527 HIS B CD2 1 ATOM 3853 C CE1 . HIS B 2 303 ? 34.714 47.652 -3.338 1.00 35.50 ? 527 HIS B CE1 1 ATOM 3854 N NE2 . HIS B 2 303 ? 33.942 47.799 -2.245 1.00 32.82 ? 527 HIS B NE2 1 ATOM 3855 N N . GLU B 2 304 ? 34.105 42.390 -1.254 1.00 28.72 ? 528 GLU B N 1 ATOM 3856 C CA . GLU B 2 304 ? 32.917 41.714 -0.799 1.00 34.66 ? 528 GLU B CA 1 ATOM 3857 C C . GLU B 2 304 ? 32.874 41.647 0.731 1.00 40.34 ? 528 GLU B C 1 ATOM 3858 O O . GLU B 2 304 ? 33.900 41.284 1.384 1.00 34.85 ? 528 GLU B O 1 ATOM 3859 C CB . GLU B 2 304 ? 32.828 40.334 -1.411 1.00 36.27 ? 528 GLU B CB 1 ATOM 3860 C CG . GLU B 2 304 ? 32.692 40.335 -2.931 1.00 38.32 ? 528 GLU B CG 1 ATOM 3861 C CD . GLU B 2 304 ? 31.473 41.164 -3.359 1.00 43.64 ? 528 GLU B CD 1 ATOM 3862 O OE1 . GLU B 2 304 ? 30.355 40.748 -3.013 1.00 48.37 ? 528 GLU B OE1 1 ATOM 3863 O OE2 . GLU B 2 304 ? 31.631 42.273 -3.919 1.00 41.58 ? 528 GLU B OE2 1 ATOM 3864 N N . GLY B 2 305 ? 31.709 42.044 1.277 1.00 30.54 ? 529 GLY B N 1 ATOM 3865 C CA . GLY B 2 305 ? 31.414 42.028 2.714 1.00 35.01 ? 529 GLY B CA 1 ATOM 3866 C C . GLY B 2 305 ? 31.844 43.229 3.533 1.00 32.17 ? 529 GLY B C 1 ATOM 3867 O O . GLY B 2 305 ? 31.406 43.352 4.693 1.00 37.09 ? 529 GLY B O 1 ATOM 3868 N N . MET B 2 306 ? 32.676 44.116 2.979 1.00 33.69 ? 530 MET B N 1 ATOM 3869 C CA . MET B 2 306 ? 33.279 45.224 3.729 1.00 37.32 ? 530 MET B CA 1 ATOM 3870 C C . MET B 2 306 ? 32.510 46.534 3.638 1.00 37.91 ? 530 MET B C 1 ATOM 3871 O O . MET B 2 306 ? 31.861 46.792 2.615 1.00 41.57 ? 530 MET B O 1 ATOM 3872 C CB . MET B 2 306 ? 34.690 45.573 3.180 1.00 34.61 ? 530 MET B CB 1 ATOM 3873 C CG . MET B 2 306 ? 35.753 44.566 3.558 1.00 36.10 ? 530 MET B CG 1 ATOM 3874 S SD . MET B 2 306 ? 37.336 45.185 2.874 1.00 30.67 ? 530 MET B SD 1 ATOM 3875 C CE . MET B 2 306 ? 37.671 43.692 1.990 1.00 30.52 ? 530 MET B CE 1 ATOM 3876 N N . PRO B 2 307 ? 32.719 47.444 4.616 1.00 35.91 ? 531 PRO B N 1 ATOM 3877 C CA . PRO B 2 307 ? 32.151 48.779 4.351 1.00 37.28 ? 531 PRO B CA 1 ATOM 3878 C C . PRO B 2 307 ? 32.879 49.482 3.263 1.00 41.00 ? 531 PRO B C 1 ATOM 3879 O O . PRO B 2 307 ? 34.028 49.083 2.910 1.00 34.70 ? 531 PRO B O 1 ATOM 3880 C CB . PRO B 2 307 ? 32.346 49.518 5.675 1.00 35.65 ? 531 PRO B CB 1 ATOM 3881 C CG . PRO B 2 307 ? 33.450 48.789 6.364 1.00 34.63 ? 531 PRO B CG 1 ATOM 3882 C CD . PRO B 2 307 ? 33.385 47.353 5.935 1.00 35.01 ? 531 PRO B CD 1 ATOM 3883 N N . GLU B 2 308 ? 32.278 50.571 2.778 1.00 36.15 ? 532 GLU B N 1 ATOM 3884 C CA A GLU B 2 308 ? 32.779 51.444 1.689 0.50 34.43 ? 532 GLU B CA 1 ATOM 3885 C CA B GLU B 2 308 ? 32.905 51.230 1.676 0.50 35.72 ? 532 GLU B CA 1 ATOM 3886 C C . GLU B 2 308 ? 33.818 52.403 2.139 1.00 32.79 ? 532 GLU B C 1 ATOM 3887 O O . GLU B 2 308 ? 34.685 52.858 1.386 1.00 30.70 ? 532 GLU B O 1 ATOM 3888 C CB A GLU B 2 308 ? 31.643 52.365 1.168 0.50 33.12 ? 532 GLU B CB 1 ATOM 3889 C CB B GLU B 2 308 ? 31.812 51.515 0.609 0.50 39.06 ? 532 GLU B CB 1 ATOM 3890 C CG A GLU B 2 308 ? 31.941 53.049 -0.178 0.50 27.73 ? 532 GLU B CG 1 ATOM 3891 C CG B GLU B 2 308 ? 30.838 50.336 0.407 0.50 34.82 ? 532 GLU B CG 1 ATOM 3892 C CD A GLU B 2 308 ? 32.831 54.255 -0.161 0.50 23.25 ? 532 GLU B CD 1 ATOM 3893 C CD B GLU B 2 308 ? 31.283 49.321 -0.646 0.50 32.14 ? 532 GLU B CD 1 ATOM 3894 O OE1 A GLU B 2 308 ? 32.797 55.166 0.738 0.50 23.85 ? 532 GLU B OE1 1 ATOM 3895 O OE1 B GLU B 2 308 ? 32.112 49.653 -1.504 0.50 28.58 ? 532 GLU B OE1 1 ATOM 3896 O OE2 A GLU B 2 308 ? 33.574 54.322 -1.104 0.50 22.78 ? 532 GLU B OE2 1 ATOM 3897 O OE2 B GLU B 2 308 ? 30.772 48.183 -0.653 0.50 35.15 ? 532 GLU B OE2 1 ATOM 3898 N N . ALA B 2 309 ? 33.679 52.827 3.396 1.00 33.76 ? 533 ALA B N 1 ATOM 3899 C CA . ALA B 2 309 ? 34.527 53.842 3.944 1.00 35.14 ? 533 ALA B CA 1 ATOM 3900 C C . ALA B 2 309 ? 35.019 53.365 5.300 1.00 30.11 ? 533 ALA B C 1 ATOM 3901 O O . ALA B 2 309 ? 34.261 52.790 6.086 1.00 31.40 ? 533 ALA B O 1 ATOM 3902 C CB . ALA B 2 309 ? 33.788 55.194 4.138 1.00 30.40 ? 533 ALA B CB 1 ATOM 3903 N N . TYR B 2 310 ? 36.284 53.701 5.578 1.00 31.74 ? 534 TYR B N 1 ATOM 3904 C CA . TYR B 2 310 ? 36.936 53.328 6.843 1.00 30.61 ? 534 TYR B CA 1 ATOM 3905 C C . TYR B 2 310 ? 37.249 54.531 7.685 1.00 28.39 ? 534 TYR B C 1 ATOM 3906 O O . TYR B 2 310 ? 38.245 55.273 7.452 1.00 32.30 ? 534 TYR B O 1 ATOM 3907 C CB . TYR B 2 310 ? 38.219 52.484 6.531 1.00 28.60 ? 534 TYR B CB 1 ATOM 3908 C CG . TYR B 2 310 ? 37.791 51.081 6.175 1.00 28.35 ? 534 TYR B CG 1 ATOM 3909 C CD1 . TYR B 2 310 ? 37.290 50.746 4.900 1.00 31.29 ? 534 TYR B CD1 1 ATOM 3910 C CD2 . TYR B 2 310 ? 37.902 50.080 7.111 1.00 31.76 ? 534 TYR B CD2 1 ATOM 3911 C CE1 . TYR B 2 310 ? 36.894 49.435 4.596 1.00 29.99 ? 534 TYR B CE1 1 ATOM 3912 C CE2 . TYR B 2 310 ? 37.532 48.796 6.798 1.00 31.11 ? 534 TYR B CE2 1 ATOM 3913 C CZ . TYR B 2 310 ? 37.021 48.496 5.550 1.00 33.65 ? 534 TYR B CZ 1 ATOM 3914 O OH . TYR B 2 310 ? 36.704 47.166 5.337 1.00 40.34 ? 534 TYR B OH 1 ATOM 3915 N N . ASN B 2 311 ? 36.381 54.786 8.648 1.00 30.67 ? 535 ASN B N 1 ATOM 3916 C CA . ASN B 2 311 ? 36.662 55.872 9.573 1.00 40.65 ? 535 ASN B CA 1 ATOM 3917 C C . ASN B 2 311 ? 36.265 55.466 10.966 1.00 41.66 ? 535 ASN B C 1 ATOM 3918 O O . ASN B 2 311 ? 35.651 56.245 11.718 1.00 41.27 ? 535 ASN B O 1 ATOM 3919 C CB . ASN B 2 311 ? 36.019 57.197 9.122 1.00 44.47 ? 535 ASN B CB 1 ATOM 3920 C CG . ASN B 2 311 ? 36.407 58.371 10.018 1.00 54.23 ? 535 ASN B CG 1 ATOM 3921 O OD1 . ASN B 2 311 ? 37.585 58.571 10.368 1.00 47.04 ? 535 ASN B OD1 1 ATOM 3922 N ND2 . ASN B 2 311 ? 35.393 59.148 10.435 1.00 50.27 ? 535 ASN B ND2 1 ATOM 3923 N N . PHE B 2 312 ? 36.642 54.247 11.341 1.00 29.78 ? 536 PHE B N 1 ATOM 3924 C CA . PHE B 2 312 ? 36.285 53.738 12.639 1.00 30.60 ? 536 PHE B CA 1 ATOM 3925 C C . PHE B 2 312 ? 37.163 54.229 13.747 1.00 30.79 ? 536 PHE B C 1 ATOM 3926 O O . PHE B 2 312 ? 38.108 55.011 13.524 1.00 32.89 ? 536 PHE B O 1 ATOM 3927 C CB . PHE B 2 312 ? 36.241 52.212 12.573 1.00 32.15 ? 536 PHE B CB 1 ATOM 3928 C CG . PHE B 2 312 ? 35.366 51.726 11.456 1.00 37.93 ? 536 PHE B CG 1 ATOM 3929 C CD1 . PHE B 2 312 ? 33.948 51.829 11.580 1.00 35.79 ? 536 PHE B CD1 1 ATOM 3930 C CD2 . PHE B 2 312 ? 35.916 51.270 10.248 1.00 31.44 ? 536 PHE B CD2 1 ATOM 3931 C CE1 . PHE B 2 312 ? 33.103 51.402 10.529 1.00 36.94 ? 536 PHE B CE1 1 ATOM 3932 C CE2 . PHE B 2 312 ? 35.069 50.819 9.200 1.00 34.23 ? 536 PHE B CE2 1 ATOM 3933 C CZ . PHE B 2 312 ? 33.659 50.865 9.346 1.00 36.31 ? 536 PHE B CZ 1 ATOM 3934 N N . ASP B 2 313 ? 36.818 53.840 14.955 1.00 32.28 ? 537 ASP B N 1 ATOM 3935 C CA . ASP B 2 313 ? 37.716 54.147 16.066 1.00 34.91 ? 537 ASP B CA 1 ATOM 3936 C C . ASP B 2 313 ? 38.271 52.886 16.666 1.00 27.73 ? 537 ASP B C 1 ATOM 3937 O O . ASP B 2 313 ? 37.802 51.814 16.344 1.00 27.90 ? 537 ASP B O 1 ATOM 3938 C CB . ASP B 2 313 ? 37.049 54.954 17.194 1.00 43.64 ? 537 ASP B CB 1 ATOM 3939 C CG . ASP B 2 313 ? 38.021 56.034 17.780 1.00 52.18 ? 537 ASP B CG 1 ATOM 3940 O OD1 . ASP B 2 313 ? 39.270 55.791 17.953 1.00 45.40 ? 537 ASP B OD1 1 ATOM 3941 O OD2 . ASP B 2 313 ? 37.549 57.158 18.030 1.00 56.47 ? 537 ASP B OD2 1 ATOM 3942 N N . PHE B 2 314 ? 39.229 53.031 17.592 1.00 29.24 ? 538 PHE B N 1 ATOM 3943 C CA . PHE B 2 314 ? 39.672 51.883 18.374 1.00 32.45 ? 538 PHE B CA 1 ATOM 3944 C C . PHE B 2 314 ? 38.485 51.438 19.228 1.00 36.89 ? 538 PHE B C 1 ATOM 3945 O O . PHE B 2 314 ? 37.836 52.282 19.851 1.00 34.87 ? 538 PHE B O 1 ATOM 3946 C CB . PHE B 2 314 ? 40.741 52.387 19.314 1.00 28.30 ? 538 PHE B CB 1 ATOM 3947 C CG . PHE B 2 314 ? 42.098 52.537 18.683 1.00 28.68 ? 538 PHE B CG 1 ATOM 3948 C CD1 . PHE B 2 314 ? 42.983 51.422 18.689 1.00 26.63 ? 538 PHE B CD1 1 ATOM 3949 C CD2 . PHE B 2 314 ? 42.551 53.804 18.207 1.00 29.08 ? 538 PHE B CD2 1 ATOM 3950 C CE1 . PHE B 2 314 ? 44.262 51.522 18.135 1.00 26.39 ? 538 PHE B CE1 1 ATOM 3951 C CE2 . PHE B 2 314 ? 43.854 53.910 17.659 1.00 30.05 ? 538 PHE B CE2 1 ATOM 3952 C CZ . PHE B 2 314 ? 44.716 52.771 17.665 1.00 32.32 ? 538 PHE B CZ 1 ATOM 3953 N N . ILE B 2 315 ? 38.193 50.163 19.272 1.00 28.15 ? 539 ILE B N 1 ATOM 3954 C CA . ILE B 2 315 ? 37.281 49.656 20.238 1.00 35.00 ? 539 ILE B CA 1 ATOM 3955 C C . ILE B 2 315 ? 37.949 48.649 21.148 1.00 36.89 ? 539 ILE B C 1 ATOM 3956 O O . ILE B 2 315 ? 38.995 48.089 20.807 1.00 32.99 ? 539 ILE B O 1 ATOM 3957 C CB . ILE B 2 315 ? 36.148 48.953 19.522 1.00 37.18 ? 539 ILE B CB 1 ATOM 3958 C CG1 . ILE B 2 315 ? 36.726 47.901 18.620 1.00 38.67 ? 539 ILE B CG1 1 ATOM 3959 C CG2 . ILE B 2 315 ? 35.353 49.964 18.658 1.00 37.68 ? 539 ILE B CG2 1 ATOM 3960 C CD1 . ILE B 2 315 ? 35.662 47.120 17.895 1.00 39.56 ? 539 ILE B CD1 1 ATOM 3961 N N . THR B 2 316 ? 37.316 48.385 22.284 1.00 31.21 ? 540 THR B N 1 ATOM 3962 C CA . THR B 2 316 ? 37.795 47.440 23.280 1.00 30.78 ? 540 THR B CA 1 ATOM 3963 C C . THR B 2 316 ? 37.450 46.032 22.935 1.00 33.92 ? 540 THR B C 1 ATOM 3964 O O . THR B 2 316 ? 36.294 45.684 22.909 1.00 32.79 ? 540 THR B O 1 ATOM 3965 C CB . THR B 2 316 ? 37.300 47.853 24.697 1.00 29.38 ? 540 THR B CB 1 ATOM 3966 O OG1 . THR B 2 316 ? 37.708 49.210 24.902 1.00 32.97 ? 540 THR B OG1 1 ATOM 3967 C CG2 . THR B 2 316 ? 37.946 46.986 25.774 1.00 35.88 ? 540 THR B CG2 1 ATOM 3968 N N . MET B 2 317 ? 38.450 45.166 22.739 1.00 27.78 ? 541 MET B N 1 ATOM 3969 C CA . MET B 2 317 ? 38.193 43.731 22.444 1.00 27.82 ? 541 MET B CA 1 ATOM 3970 C C . MET B 2 317 ? 38.475 42.948 23.685 1.00 30.21 ? 541 MET B C 1 ATOM 3971 O O . MET B 2 317 ? 39.581 43.034 24.249 1.00 30.81 ? 541 MET B O 1 ATOM 3972 C CB . MET B 2 317 ? 39.139 43.234 21.320 1.00 28.91 ? 541 MET B CB 1 ATOM 3973 C CG . MET B 2 317 ? 39.096 44.142 20.038 1.00 31.86 ? 541 MET B CG 1 ATOM 3974 S SD . MET B 2 317 ? 37.446 43.803 19.275 1.00 32.50 ? 541 MET B SD 1 ATOM 3975 C CE . MET B 2 317 ? 37.747 44.527 17.660 1.00 31.30 ? 541 MET B CE 1 ATOM 3976 N N . LYS B 2 318 ? 37.526 42.138 24.126 1.00 29.18 ? 542 LYS B N 1 ATOM 3977 C CA . LYS B 2 318 ? 37.755 41.328 25.324 1.00 36.72 ? 542 LYS B CA 1 ATOM 3978 C C . LYS B 2 318 ? 36.813 40.156 25.249 1.00 33.59 ? 542 LYS B C 1 ATOM 3979 O O . LYS B 2 318 ? 35.736 40.314 24.726 1.00 37.12 ? 542 LYS B O 1 ATOM 3980 C CB . LYS B 2 318 ? 37.454 42.154 26.589 1.00 38.89 ? 542 LYS B CB 1 ATOM 3981 C CG . LYS B 2 318 ? 36.046 42.831 26.659 1.00 46.40 ? 542 LYS B CG 1 ATOM 3982 C CD . LYS B 2 318 ? 36.078 44.107 27.529 1.00 54.73 ? 542 LYS B CD 1 ATOM 3983 C CE . LYS B 2 318 ? 34.709 44.748 27.806 1.00 61.62 ? 542 LYS B CE 1 ATOM 3984 N NZ . LYS B 2 318 ? 33.704 44.557 26.716 1.00 56.61 ? 542 LYS B NZ 1 ATOM 3985 N N . PRO B 2 319 ? 37.175 38.975 25.793 1.00 31.63 ? 543 PRO B N 1 ATOM 3986 C CA . PRO B 2 319 ? 36.114 37.997 25.831 1.00 33.68 ? 543 PRO B CA 1 ATOM 3987 C C . PRO B 2 319 ? 35.006 38.336 26.857 1.00 39.14 ? 543 PRO B C 1 ATOM 3988 O O . PRO B 2 319 ? 35.302 38.956 27.876 1.00 35.70 ? 543 PRO B O 1 ATOM 3989 C CB . PRO B 2 319 ? 36.816 36.690 26.317 1.00 34.56 ? 543 PRO B CB 1 ATOM 3990 C CG . PRO B 2 319 ? 38.268 37.052 26.518 1.00 35.12 ? 543 PRO B CG 1 ATOM 3991 C CD . PRO B 2 319 ? 38.378 38.527 26.529 1.00 33.01 ? 543 PRO B CD 1 ATOM 3992 N N . ILE B 2 320 ? 33.768 37.904 26.580 1.00 38.25 ? 544 ILE B N 1 ATOM 3993 C CA . ILE B 2 320 ? 32.650 38.109 27.497 1.00 40.45 ? 544 ILE B CA 1 ATOM 3994 C C . ILE B 2 320 ? 31.924 36.854 27.987 1.00 40.88 ? 544 ILE B C 1 ATOM 3995 O O . ILE B 2 320 ? 31.080 36.953 28.828 1.00 43.20 ? 544 ILE B O 1 ATOM 3996 C CB . ILE B 2 320 ? 31.654 39.127 26.970 1.00 39.26 ? 544 ILE B CB 1 ATOM 3997 C CG1 . ILE B 2 320 ? 30.894 38.524 25.796 1.00 42.32 ? 544 ILE B CG1 1 ATOM 3998 C CG2 . ILE B 2 320 ? 32.320 40.489 26.677 1.00 40.15 ? 544 ILE B CG2 1 ATOM 3999 C CD1 . ILE B 2 320 ? 29.710 39.397 25.360 1.00 45.55 ? 544 ILE B CD1 1 ATOM 4000 N N . LEU B 2 321 ? 32.246 35.662 27.517 1.00 36.94 ? 545 LEU B N 1 ATOM 4001 C CA . LEU B 2 321 ? 31.564 34.516 28.032 1.00 41.04 ? 545 LEU B CA 1 ATOM 4002 C C . LEU B 2 321 ? 32.268 33.954 29.257 1.00 46.25 ? 545 LEU B C 1 ATOM 4003 O O . LEU B 2 321 ? 31.833 32.888 29.724 1.00 54.67 ? 545 LEU B O 1 ATOM 4004 C CB . LEU B 2 321 ? 31.417 33.414 26.959 1.00 39.70 ? 545 LEU B CB 1 ATOM 4005 C CG . LEU B 2 321 ? 30.763 33.797 25.614 1.00 38.61 ? 545 LEU B CG 1 ATOM 4006 C CD1 . LEU B 2 321 ? 30.899 32.653 24.625 1.00 40.58 ? 545 LEU B CD1 1 ATOM 4007 C CD2 . LEU B 2 321 ? 29.300 34.159 25.711 1.00 37.38 ? 545 LEU B CD2 1 HETATM 4008 C C1 . NAG C 3 . ? 28.503 43.831 18.879 1.00 42.80 ? 1048 NAG A C1 1 HETATM 4009 C C2 . NAG C 3 . ? 28.487 44.053 20.407 1.00 50.62 ? 1048 NAG A C2 1 HETATM 4010 C C3 . NAG C 3 . ? 27.815 45.389 20.719 1.00 51.44 ? 1048 NAG A C3 1 HETATM 4011 C C4 . NAG C 3 . ? 28.345 46.533 19.881 1.00 55.34 ? 1048 NAG A C4 1 HETATM 4012 C C5 . NAG C 3 . ? 28.377 46.076 18.399 1.00 52.76 ? 1048 NAG A C5 1 HETATM 4013 C C6 . NAG C 3 . ? 29.031 47.024 17.429 1.00 50.51 ? 1048 NAG A C6 1 HETATM 4014 C C7 . NAG C 3 . ? 28.627 41.718 21.298 1.00 53.34 ? 1048 NAG A C7 1 HETATM 4015 C C8 . NAG C 3 . ? 27.934 40.576 21.984 1.00 52.91 ? 1048 NAG A C8 1 HETATM 4016 N N2 . NAG C 3 . ? 27.929 42.883 21.095 1.00 46.19 ? 1048 NAG A N2 1 HETATM 4017 O O3 . NAG C 3 . ? 28.134 45.768 22.025 1.00 65.79 ? 1048 NAG A O3 1 HETATM 4018 O O4 . NAG C 3 . ? 27.515 47.653 20.146 1.00 57.62 ? 1048 NAG A O4 1 HETATM 4019 O O5 . NAG C 3 . ? 29.140 44.893 18.280 1.00 47.14 ? 1048 NAG A O5 1 HETATM 4020 O O6 . NAG C 3 . ? 30.001 47.824 18.075 1.00 55.62 ? 1048 NAG A O6 1 HETATM 4021 O O7 . NAG C 3 . ? 29.807 41.474 20.928 1.00 50.41 ? 1048 NAG A O7 1 HETATM 4022 C C1 . NAG D 3 . ? 28.163 48.855 20.635 1.00 71.01 ? 1049 NAG A C1 1 HETATM 4023 C C2 . NAG D 3 . ? 27.283 50.104 20.370 1.00 80.95 ? 1049 NAG A C2 1 HETATM 4024 C C3 . NAG D 3 . ? 27.623 51.327 21.256 1.00 89.88 ? 1049 NAG A C3 1 HETATM 4025 C C4 . NAG D 3 . ? 27.848 50.952 22.706 1.00 92.21 ? 1049 NAG A C4 1 HETATM 4026 C C5 . NAG D 3 . ? 29.003 49.959 22.583 1.00 90.51 ? 1049 NAG A C5 1 HETATM 4027 C C6 . NAG D 3 . ? 29.700 49.705 23.909 1.00 91.03 ? 1049 NAG A C6 1 HETATM 4028 C C7 . NAG D 3 . ? 26.705 50.298 17.941 1.00 81.05 ? 1049 NAG A C7 1 HETATM 4029 C C8 . NAG D 3 . ? 26.993 51.146 16.726 1.00 72.80 ? 1049 NAG A C8 1 HETATM 4030 N N2 . NAG D 3 . ? 27.367 50.665 19.032 1.00 81.36 ? 1049 NAG A N2 1 HETATM 4031 O O3 . NAG D 3 . ? 26.672 52.371 21.179 1.00 93.28 ? 1049 NAG A O3 1 HETATM 4032 O O4 . NAG D 3 . ? 28.147 52.122 23.452 1.00 99.62 ? 1049 NAG A O4 1 HETATM 4033 O O5 . NAG D 3 . ? 28.485 48.755 22.014 1.00 78.21 ? 1049 NAG A O5 1 HETATM 4034 O O6 . NAG D 3 . ? 28.795 48.928 24.644 1.00 96.55 ? 1049 NAG A O6 1 HETATM 4035 O O7 . NAG D 3 . ? 25.927 49.340 17.892 1.00 83.49 ? 1049 NAG A O7 1 HETATM 4036 C C8 . P4G E 4 . ? 16.985 18.302 19.593 1.00 73.22 ? 1206 P4G A C8 1 HETATM 4037 C C7 . P4G E 4 . ? 18.204 17.643 20.246 1.00 79.77 ? 1206 P4G A C7 1 HETATM 4038 O O4 . P4G E 4 . ? 19.397 18.466 20.195 1.00 90.96 ? 1206 P4G A O4 1 HETATM 4039 C C6 . P4G E 4 . ? 20.388 18.242 21.214 1.00 65.72 ? 1206 P4G A C6 1 HETATM 4040 C C5 . P4G E 4 . ? 20.268 19.237 22.389 1.00 66.02 ? 1206 P4G A C5 1 HETATM 4041 O O3 . P4G E 4 . ? 19.462 20.426 22.144 1.00 69.66 ? 1206 P4G A O3 1 HETATM 4042 C C4 . P4G E 4 . ? 19.138 21.215 23.307 1.00 57.54 ? 1206 P4G A C4 1 HETATM 4043 C C3 . P4G E 4 . ? 18.826 22.702 23.041 1.00 59.20 ? 1206 P4G A C3 1 HETATM 4044 O O2 . P4G E 4 . ? 17.431 23.049 22.891 1.00 69.70 ? 1206 P4G A O2 1 HETATM 4045 C C2 . P4G E 4 . ? 17.136 24.311 22.251 1.00 61.81 ? 1206 P4G A C2 1 HETATM 4046 C C1 . P4G E 4 . ? 15.982 25.060 22.906 1.00 59.07 ? 1206 P4G A C1 1 HETATM 4047 C C1 . NAG F 3 . ? 72.120 32.057 -0.250 1.00 48.16 ? 1285 NAG B C1 1 HETATM 4048 C C2 . NAG F 3 . ? 73.515 32.377 0.227 1.00 48.15 ? 1285 NAG B C2 1 HETATM 4049 C C3 . NAG F 3 . ? 74.475 31.232 -0.130 1.00 52.48 ? 1285 NAG B C3 1 HETATM 4050 C C4 . NAG F 3 . ? 73.881 29.849 0.138 1.00 54.52 ? 1285 NAG B C4 1 HETATM 4051 C C5 . NAG F 3 . ? 72.416 29.772 -0.333 1.00 51.36 ? 1285 NAG B C5 1 HETATM 4052 C C6 . NAG F 3 . ? 71.691 28.461 -0.013 1.00 45.86 ? 1285 NAG B C6 1 HETATM 4053 C C7 . NAG F 3 . ? 74.122 34.734 0.275 1.00 59.91 ? 1285 NAG B C7 1 HETATM 4054 C C8 . NAG F 3 . ? 74.306 36.037 -0.443 1.00 54.45 ? 1285 NAG B C8 1 HETATM 4055 N N2 . NAG F 3 . ? 73.742 33.658 -0.423 1.00 57.13 ? 1285 NAG B N2 1 HETATM 4056 O O3 . NAG F 3 . ? 75.631 31.249 0.669 1.00 52.82 ? 1285 NAG B O3 1 HETATM 4057 O O4 . NAG F 3 . ? 74.757 28.886 -0.469 1.00 65.31 ? 1285 NAG B O4 1 HETATM 4058 O O5 . NAG F 3 . ? 71.700 30.826 0.283 1.00 47.15 ? 1285 NAG B O5 1 HETATM 4059 O O6 . NAG F 3 . ? 71.744 28.289 1.393 1.00 44.62 ? 1285 NAG B O6 1 HETATM 4060 O O7 . NAG F 3 . ? 74.363 34.681 1.480 1.00 57.58 ? 1285 NAG B O7 1 HETATM 4061 C C1 . NAG G 3 . ? 75.225 27.874 0.469 1.00 73.73 ? 1286 NAG B C1 1 HETATM 4062 C C2 . NAG G 3 . ? 75.513 26.529 -0.248 1.00 79.31 ? 1286 NAG B C2 1 HETATM 4063 C C3 . NAG G 3 . ? 76.584 25.649 0.415 1.00 78.62 ? 1286 NAG B C3 1 HETATM 4064 C C4 . NAG G 3 . ? 77.545 26.326 1.390 1.00 80.65 ? 1286 NAG B C4 1 HETATM 4065 C C5 . NAG G 3 . ? 76.792 27.372 2.203 1.00 81.78 ? 1286 NAG B C5 1 HETATM 4066 C C6 . NAG G 3 . ? 77.669 28.008 3.291 1.00 76.29 ? 1286 NAG B C6 1 HETATM 4067 C C7 . NAG G 3 . ? 73.646 25.512 -1.549 1.00 78.85 ? 1286 NAG B C7 1 HETATM 4068 C C8 . NAG G 3 . ? 72.438 24.612 -1.526 1.00 72.36 ? 1286 NAG B C8 1 HETATM 4069 N N2 . NAG G 3 . ? 74.316 25.695 -0.396 1.00 77.09 ? 1286 NAG B N2 1 HETATM 4070 O O3 . NAG G 3 . ? 77.381 25.174 -0.628 1.00 94.44 ? 1286 NAG B O3 1 HETATM 4071 O O4 . NAG G 3 . ? 78.184 25.362 2.202 1.00 79.47 ? 1286 NAG B O4 1 HETATM 4072 O O5 . NAG G 3 . ? 76.326 28.324 1.252 1.00 81.44 ? 1286 NAG B O5 1 HETATM 4073 O O6 . NAG G 3 . ? 78.472 29.021 2.724 1.00 64.57 ? 1286 NAG B O6 1 HETATM 4074 O O7 . NAG G 3 . ? 73.965 26.052 -2.613 1.00 76.83 ? 1286 NAG B O7 1 HETATM 4075 C C1 . NAG H 3 . ? 54.671 52.137 39.908 1.00 39.52 ? 1343 NAG B C1 1 HETATM 4076 C C2 . NAG H 3 . ? 53.354 51.625 40.528 1.00 46.00 ? 1343 NAG B C2 1 HETATM 4077 C C3 . NAG H 3 . ? 52.205 52.566 40.213 1.00 47.43 ? 1343 NAG B C3 1 HETATM 4078 C C4 . NAG H 3 . ? 52.528 54.014 40.475 1.00 55.91 ? 1343 NAG B C4 1 HETATM 4079 C C5 . NAG H 3 . ? 53.925 54.431 39.997 1.00 56.03 ? 1343 NAG B C5 1 HETATM 4080 C C6 . NAG H 3 . ? 54.211 55.675 40.794 1.00 50.24 ? 1343 NAG B C6 1 HETATM 4081 C C7 . NAG H 3 . ? 53.114 49.204 40.688 1.00 44.09 ? 1343 NAG B C7 1 HETATM 4082 C C8 . NAG H 3 . ? 52.765 47.876 40.098 1.00 40.17 ? 1343 NAG B C8 1 HETATM 4083 N N2 . NAG H 3 . ? 52.973 50.321 39.983 1.00 39.65 ? 1343 NAG B N2 1 HETATM 4084 O O3 . NAG H 3 . ? 51.120 52.182 41.009 1.00 51.29 ? 1343 NAG B O3 1 HETATM 4085 O O4 . NAG H 3 . ? 51.531 54.697 39.763 1.00 75.32 ? 1343 NAG B O4 1 HETATM 4086 O O5 . NAG H 3 . ? 54.984 53.478 40.236 1.00 50.06 ? 1343 NAG B O5 1 HETATM 4087 O O6 . NAG H 3 . ? 55.345 56.158 40.161 1.00 57.08 ? 1343 NAG B O6 1 HETATM 4088 O O7 . NAG H 3 . ? 53.561 49.197 41.833 1.00 47.15 ? 1343 NAG B O7 1 HETATM 4089 C C1 . NAG I 3 . ? 51.171 56.007 40.258 1.00 91.29 ? 1345 NAG B C1 1 HETATM 4090 C C2 . NAG I 3 . ? 49.948 56.411 39.421 1.00 93.15 ? 1345 NAG B C2 1 HETATM 4091 C C3 . NAG I 3 . ? 48.851 57.253 40.118 1.00 103.22 ? 1345 NAG B C3 1 HETATM 4092 C C4 . NAG I 3 . ? 48.956 57.288 41.639 1.00 108.82 ? 1345 NAG B C4 1 HETATM 4093 C C5 . NAG I 3 . ? 50.439 57.413 42.000 1.00 111.06 ? 1345 NAG B C5 1 HETATM 4094 C C6 . NAG I 3 . ? 50.720 57.824 43.448 1.00 103.00 ? 1345 NAG B C6 1 HETATM 4095 C C7 . NAG I 3 . ? 51.410 57.993 38.147 1.00 72.68 ? 1345 NAG B C7 1 HETATM 4096 C C8 . NAG I 3 . ? 51.759 58.497 36.759 1.00 64.46 ? 1345 NAG B C8 1 HETATM 4097 N N2 . NAG I 3 . ? 50.464 57.051 38.206 1.00 81.16 ? 1345 NAG B N2 1 HETATM 4098 O O3 . NAG I 3 . ? 47.566 56.757 39.816 1.00 108.69 ? 1345 NAG B O3 1 HETATM 4099 O O4 . NAG I 3 . ? 48.176 58.371 42.093 1.00 115.03 ? 1345 NAG B O4 1 HETATM 4100 O O5 . NAG I 3 . ? 51.035 56.169 41.668 1.00 103.59 ? 1345 NAG B O5 1 HETATM 4101 O O6 . NAG I 3 . ? 50.927 56.655 44.213 1.00 100.13 ? 1345 NAG B O6 1 HETATM 4102 O O7 . NAG I 3 . ? 51.956 58.439 39.170 1.00 69.49 ? 1345 NAG B O7 1 HETATM 4103 C C1 . NAG J 3 . ? 77.392 39.074 7.559 1.00 47.35 ? 1388 NAG B C1 1 HETATM 4104 C C2 . NAG J 3 . ? 78.480 38.223 8.290 1.00 52.10 ? 1388 NAG B C2 1 HETATM 4105 C C3 . NAG J 3 . ? 79.738 39.097 8.572 1.00 54.43 ? 1388 NAG B C3 1 HETATM 4106 C C4 . NAG J 3 . ? 80.234 39.688 7.254 1.00 58.79 ? 1388 NAG B C4 1 HETATM 4107 C C5 . NAG J 3 . ? 79.051 40.608 6.956 1.00 56.99 ? 1388 NAG B C5 1 HETATM 4108 C C6 . NAG J 3 . ? 79.423 41.755 6.053 1.00 56.26 ? 1388 NAG B C6 1 HETATM 4109 C C7 . NAG J 3 . ? 77.542 36.441 9.773 1.00 45.55 ? 1388 NAG B C7 1 HETATM 4110 C C8 . NAG J 3 . ? 77.056 36.159 11.156 1.00 45.53 ? 1388 NAG B C8 1 HETATM 4111 N N2 . NAG J 3 . ? 77.971 37.695 9.547 1.00 43.00 ? 1388 NAG B N2 1 HETATM 4112 O O3 . NAG J 3 . ? 80.718 38.405 9.309 1.00 60.45 ? 1388 NAG B O3 1 HETATM 4113 O O4 . NAG J 3 . ? 81.455 40.422 7.367 1.00 72.89 ? 1388 NAG B O4 1 HETATM 4114 O O5 . NAG J 3 . ? 77.981 39.800 6.476 1.00 49.91 ? 1388 NAG B O5 1 HETATM 4115 O O6 . NAG J 3 . ? 79.719 41.141 4.838 1.00 60.28 ? 1388 NAG B O6 1 HETATM 4116 O O7 . NAG J 3 . ? 77.511 35.548 8.941 1.00 50.79 ? 1388 NAG B O7 1 HETATM 4117 C C1 . NAG K 3 . ? 34.611 53.918 -10.403 1.00 75.50 ? 1503 NAG B C1 1 HETATM 4118 C C2 . NAG K 3 . ? 33.181 54.469 -10.336 1.00 88.37 ? 1503 NAG B C2 1 HETATM 4119 C C3 . NAG K 3 . ? 32.877 55.136 -11.667 1.00 86.26 ? 1503 NAG B C3 1 HETATM 4120 C C4 . NAG K 3 . ? 33.783 56.372 -11.753 1.00 90.91 ? 1503 NAG B C4 1 HETATM 4121 C C5 . NAG K 3 . ? 35.261 55.994 -11.542 1.00 85.77 ? 1503 NAG B C5 1 HETATM 4122 C C6 . NAG K 3 . ? 36.078 57.242 -11.243 1.00 81.82 ? 1503 NAG B C6 1 HETATM 4123 C C7 . NAG K 3 . ? 31.669 53.597 -8.584 1.00 104.88 ? 1503 NAG B C7 1 HETATM 4124 C C8 . NAG K 3 . ? 32.236 54.579 -7.554 1.00 87.24 ? 1503 NAG B C8 1 HETATM 4125 N N2 . NAG K 3 . ? 32.134 53.561 -9.868 1.00 90.24 ? 1503 NAG B N2 1 HETATM 4126 O O3 . NAG K 3 . ? 31.528 55.500 -11.681 1.00 76.38 ? 1503 NAG B O3 1 HETATM 4127 O O4 . NAG K 3 . ? 33.645 57.018 -13.004 1.00 94.68 ? 1503 NAG B O4 1 HETATM 4128 O O5 . NAG K 3 . ? 35.474 55.054 -10.481 1.00 81.42 ? 1503 NAG B O5 1 HETATM 4129 O O6 . NAG K 3 . ? 37.428 56.844 -11.198 1.00 85.25 ? 1503 NAG B O6 1 HETATM 4130 O O7 . NAG K 3 . ? 30.777 52.821 -8.223 1.00 102.71 ? 1503 NAG B O7 1 HETATM 4131 O O1 . P6G L 5 . ? 50.912 44.298 38.071 1.00 47.29 ? 1546 P6G B O1 1 HETATM 4132 C C2 . P6G L 5 . ? 49.783 44.745 37.314 1.00 51.68 ? 1546 P6G B C2 1 HETATM 4133 C C3 . P6G L 5 . ? 49.659 43.948 36.030 1.00 45.87 ? 1546 P6G B C3 1 HETATM 4134 O O4 . P6G L 5 . ? 49.522 42.584 36.444 1.00 50.28 ? 1546 P6G B O4 1 HETATM 4135 C C5 . P6G L 5 . ? 49.060 41.609 35.479 1.00 48.57 ? 1546 P6G B C5 1 HETATM 4136 C C6 . P6G L 5 . ? 49.463 40.117 35.719 1.00 55.06 ? 1546 P6G B C6 1 HETATM 4137 O O7 . P6G L 5 . ? 50.170 39.475 34.611 1.00 52.41 ? 1546 P6G B O7 1 HETATM 4138 C C8 . P6G L 5 . ? 50.403 38.046 34.774 1.00 56.24 ? 1546 P6G B C8 1 HETATM 4139 C C9 . P6G L 5 . ? 50.699 37.369 33.435 1.00 53.05 ? 1546 P6G B C9 1 HETATM 4140 O O10 . P6G L 5 . ? 50.123 38.265 32.470 1.00 56.36 ? 1546 P6G B O10 1 HETATM 4141 C C11 . P6G L 5 . ? 49.832 37.657 31.223 1.00 55.27 ? 1546 P6G B C11 1 HETATM 4142 C C12 . P6G L 5 . ? 48.425 37.881 30.694 1.00 50.96 ? 1546 P6G B C12 1 HETATM 4143 O O13 . P6G L 5 . ? 47.950 36.570 30.280 1.00 62.91 ? 1546 P6G B O13 1 HETATM 4144 C C14 . P6G L 5 . ? 46.596 36.299 30.599 1.00 55.95 ? 1546 P6G B C14 1 HETATM 4145 C C15 . P6G L 5 . ? 46.551 34.942 31.242 1.00 52.11 ? 1546 P6G B C15 1 HETATM 4146 O O16 . P6G L 5 . ? 45.493 34.947 32.197 1.00 72.15 ? 1546 P6G B O16 1 HETATM 4147 C C17 . P6G L 5 . ? 45.241 33.667 32.810 1.00 75.39 ? 1546 P6G B C17 1 HETATM 4148 C C18 . P6G L 5 . ? 45.972 33.487 34.152 1.00 69.29 ? 1546 P6G B C18 1 HETATM 4149 O O19 . P6G L 5 . ? 46.940 34.534 34.368 1.00 72.21 ? 1546 P6G B O19 1 HETATM 4150 CL CL . CL M 6 . ? 67.681 52.275 23.374 0.50 32.72 ? 1547 CL B CL 1 HETATM 4151 O O . HOH N 7 . ? 23.850 41.444 10.858 1.00 43.51 ? 2001 HOH A O 1 HETATM 4152 O O . HOH N 7 . ? 29.687 25.771 29.872 1.00 38.70 ? 2002 HOH A O 1 HETATM 4153 O O . HOH N 7 . ? 31.343 24.252 25.691 1.00 37.78 ? 2003 HOH A O 1 HETATM 4154 O O . HOH N 7 . ? 31.364 20.126 26.895 1.00 48.07 ? 2004 HOH A O 1 HETATM 4155 O O . HOH N 7 . ? 33.587 40.306 9.725 1.00 42.31 ? 2005 HOH A O 1 HETATM 4156 O O . HOH N 7 . ? 31.073 41.368 10.898 1.00 51.02 ? 2006 HOH A O 1 HETATM 4157 O O . HOH N 7 . ? 28.388 44.698 9.662 1.00 45.29 ? 2007 HOH A O 1 HETATM 4158 O O . HOH N 7 . ? 37.963 49.851 14.447 1.00 26.58 ? 2008 HOH A O 1 HETATM 4159 O O . HOH N 7 . ? 37.203 46.067 8.675 1.00 46.56 ? 2009 HOH A O 1 HETATM 4160 O O . HOH N 7 . ? 38.242 37.285 -9.289 1.00 44.51 ? 2010 HOH A O 1 HETATM 4161 O O . HOH N 7 . ? 33.706 38.579 23.059 1.00 33.74 ? 2011 HOH A O 1 HETATM 4162 O O . HOH N 7 . ? 35.758 32.323 25.236 1.00 42.01 ? 2012 HOH A O 1 HETATM 4163 O O . HOH N 7 . ? 34.920 18.377 27.934 1.00 48.76 ? 2013 HOH A O 1 HETATM 4164 O O . HOH N 7 . ? 46.356 23.108 4.813 1.00 30.68 ? 2014 HOH A O 1 HETATM 4165 O O . HOH N 7 . ? 38.196 29.533 31.092 1.00 48.72 ? 2015 HOH A O 1 HETATM 4166 O O . HOH N 7 . ? 39.400 16.587 27.188 1.00 38.65 ? 2016 HOH A O 1 HETATM 4167 O O . HOH N 7 . ? 41.602 13.609 25.137 1.00 39.71 ? 2017 HOH A O 1 HETATM 4168 O O . HOH N 7 . ? 37.345 27.614 15.888 1.00 31.60 ? 2018 HOH A O 1 HETATM 4169 O O . HOH N 7 . ? 36.142 32.477 10.647 1.00 28.31 ? 2019 HOH A O 1 HETATM 4170 O O . HOH N 7 . ? 49.208 33.038 8.598 1.00 42.62 ? 2020 HOH A O 1 HETATM 4171 O O . HOH N 7 . ? 29.192 42.324 5.502 1.00 41.66 ? 2021 HOH A O 1 HETATM 4172 O O . HOH N 7 . ? 38.503 40.378 2.596 1.00 28.90 ? 2022 HOH A O 1 HETATM 4173 O O . HOH N 7 . ? 37.387 36.350 -6.745 1.00 32.37 ? 2023 HOH A O 1 HETATM 4174 O O . HOH N 7 . ? 40.209 41.843 -4.216 1.00 29.55 ? 2024 HOH A O 1 HETATM 4175 O O . HOH N 7 . ? 48.680 39.247 -2.204 1.00 38.61 ? 2025 HOH A O 1 HETATM 4176 O O . HOH N 7 . ? 45.682 45.752 -3.189 1.00 42.27 ? 2026 HOH A O 1 HETATM 4177 O O . HOH N 7 . ? 48.068 41.926 -3.110 1.00 47.32 ? 2027 HOH A O 1 HETATM 4178 O O . HOH N 7 . ? 43.616 45.548 -5.759 1.00 45.23 ? 2028 HOH A O 1 HETATM 4179 O O . HOH N 7 . ? 51.162 35.158 -18.463 1.00 44.07 ? 2029 HOH A O 1 HETATM 4180 O O . HOH N 7 . ? 45.444 31.784 -16.812 1.00 41.13 ? 2030 HOH A O 1 HETATM 4181 O O . HOH N 7 . ? 49.079 30.318 -16.507 1.00 55.88 ? 2031 HOH A O 1 HETATM 4182 O O . HOH N 7 . ? 44.668 24.440 -11.747 1.00 36.95 ? 2032 HOH A O 1 HETATM 4183 O O . HOH N 7 . ? 49.953 20.862 -10.488 1.00 44.01 ? 2033 HOH A O 1 HETATM 4184 O O . HOH N 7 . ? 52.122 22.169 -10.866 1.00 44.02 ? 2034 HOH A O 1 HETATM 4185 O O . HOH N 7 . ? 46.840 21.446 -10.043 1.00 66.12 ? 2035 HOH A O 1 HETATM 4186 O O . HOH N 7 . ? 54.798 21.322 -4.891 1.00 44.82 ? 2036 HOH A O 1 HETATM 4187 O O . HOH N 7 . ? 48.180 22.418 2.760 1.00 28.25 ? 2037 HOH A O 1 HETATM 4188 O O . HOH N 7 . ? 53.226 14.656 0.442 1.00 42.97 ? 2038 HOH A O 1 HETATM 4189 O O . HOH N 7 . ? 47.850 20.959 6.175 1.00 29.96 ? 2039 HOH A O 1 HETATM 4190 O O . HOH N 7 . ? 43.519 20.236 5.488 1.00 30.21 ? 2040 HOH A O 1 HETATM 4191 O O . HOH N 7 . ? 49.338 12.107 16.535 1.00 47.30 ? 2041 HOH A O 1 HETATM 4192 O O . HOH N 7 . ? 59.825 13.283 11.734 1.00 38.35 ? 2042 HOH A O 1 HETATM 4193 O O . HOH N 7 . ? 58.363 15.686 17.363 1.00 46.42 ? 2043 HOH A O 1 HETATM 4194 O O . HOH N 7 . ? 35.675 17.401 7.855 1.00 37.82 ? 2044 HOH A O 1 HETATM 4195 O O . HOH N 7 . ? 33.175 25.957 -3.701 1.00 50.71 ? 2045 HOH A O 1 HETATM 4196 O O . HOH N 7 . ? 39.220 20.366 -1.944 1.00 42.46 ? 2046 HOH A O 1 HETATM 4197 O O . HOH N 7 . ? 36.651 19.811 -0.713 1.00 50.56 ? 2047 HOH A O 1 HETATM 4198 O O . HOH N 7 . ? 46.480 25.801 5.085 1.00 25.74 ? 2048 HOH A O 1 HETATM 4199 O O . HOH N 7 . ? 46.320 32.937 6.883 1.00 31.18 ? 2049 HOH A O 1 HETATM 4200 O O . HOH N 7 . ? 49.371 31.405 6.341 1.00 37.76 ? 2050 HOH A O 1 HETATM 4201 O O . HOH O 7 . ? 66.519 42.017 36.062 1.00 42.39 ? 2001 HOH B O 1 HETATM 4202 O O . HOH O 7 . ? 71.878 43.613 24.042 0.50 36.01 ? 2002 HOH B O 1 HETATM 4203 O O . HOH O 7 . ? 72.899 41.745 19.503 1.00 30.88 ? 2003 HOH B O 1 HETATM 4204 O O . HOH O 7 . ? 72.619 42.287 30.222 1.00 48.46 ? 2004 HOH B O 1 HETATM 4205 O O . HOH O 7 . ? 72.149 44.414 10.223 1.00 36.16 ? 2005 HOH B O 1 HETATM 4206 O O . HOH O 7 . ? 57.198 58.878 30.758 1.00 29.82 ? 2006 HOH B O 1 HETATM 4207 O O . HOH O 7 . ? 54.531 44.516 5.199 1.00 36.70 ? 2007 HOH B O 1 HETATM 4208 O O . HOH O 7 . ? 53.096 40.151 9.106 1.00 33.31 ? 2008 HOH B O 1 HETATM 4209 O O . HOH O 7 . ? 49.385 41.446 7.901 1.00 47.37 ? 2009 HOH B O 1 HETATM 4210 O O . HOH O 7 . ? 61.420 56.095 27.413 1.00 23.81 ? 2010 HOH B O 1 HETATM 4211 O O . HOH O 7 . ? 59.628 52.659 39.039 1.00 27.46 ? 2011 HOH B O 1 HETATM 4212 O O . HOH O 7 . ? 39.417 40.364 -9.139 1.00 37.74 ? 2012 HOH B O 1 HETATM 4213 O O . HOH O 7 . ? 52.127 50.539 37.259 1.00 41.93 ? 2013 HOH B O 1 HETATM 4214 O O . HOH O 7 . ? 58.179 54.733 39.161 1.00 40.57 ? 2014 HOH B O 1 HETATM 4215 O O . HOH O 7 . ? 50.502 53.499 31.809 1.00 38.31 ? 2015 HOH B O 1 HETATM 4216 O O . HOH O 7 . ? 41.763 46.070 9.081 1.00 27.76 ? 2016 HOH B O 1 HETATM 4217 O O . HOH O 7 . ? 41.491 41.089 23.131 1.00 25.76 ? 2017 HOH B O 1 HETATM 4218 O O . HOH O 7 . ? 35.684 41.753 21.586 1.00 34.96 ? 2018 HOH B O 1 HETATM 4219 O O . HOH O 7 . ? 40.084 34.491 24.625 1.00 35.52 ? 2019 HOH B O 1 HETATM 4220 O O . HOH O 7 . ? 37.973 18.746 28.860 1.00 37.63 ? 2020 HOH B O 1 HETATM 4221 O O . HOH O 7 . ? 45.441 20.967 30.210 1.00 47.69 ? 2021 HOH B O 1 HETATM 4222 O O . HOH O 7 . ? 44.684 24.159 28.454 1.00 46.19 ? 2022 HOH B O 1 HETATM 4223 O O . HOH O 7 . ? 46.357 27.539 21.935 1.00 29.66 ? 2023 HOH B O 1 HETATM 4224 O O . HOH O 7 . ? 47.486 29.559 22.927 1.00 31.47 ? 2024 HOH B O 1 HETATM 4225 O O . HOH O 7 . ? 44.434 27.668 28.889 1.00 18.98 ? 2025 HOH B O 1 HETATM 4226 O O . HOH O 7 . ? 38.190 33.192 26.212 1.00 34.07 ? 2026 HOH B O 1 HETATM 4227 O O . HOH O 7 . ? 42.619 32.033 31.607 1.00 40.42 ? 2027 HOH B O 1 HETATM 4228 O O . HOH O 7 . ? 49.322 33.332 12.960 1.00 26.91 ? 2028 HOH B O 1 HETATM 4229 O O . HOH O 7 . ? 52.722 33.678 11.415 1.00 20.93 ? 2029 HOH B O 1 HETATM 4230 O O . HOH O 7 . ? 49.130 37.181 27.470 1.00 33.85 ? 2030 HOH B O 1 HETATM 4231 O O . HOH O 7 . ? 49.624 31.821 32.481 1.00 24.36 ? 2031 HOH B O 1 HETATM 4232 O O . HOH O 7 . ? 51.935 29.685 24.734 1.00 25.42 ? 2032 HOH B O 1 HETATM 4233 O O . HOH O 7 . ? 61.061 41.973 10.951 1.00 17.47 ? 2033 HOH B O 1 HETATM 4234 O O . HOH O 7 . ? 63.464 36.059 8.699 1.00 24.33 ? 2034 HOH B O 1 HETATM 4235 O O . HOH O 7 . ? 61.087 42.551 3.975 1.00 46.85 ? 2035 HOH B O 1 HETATM 4236 O O . HOH O 7 . ? 64.609 37.067 6.190 1.00 24.08 ? 2036 HOH B O 1 HETATM 4237 O O . HOH O 7 . ? 64.700 20.780 0.884 1.00 47.20 ? 2037 HOH B O 1 HETATM 4238 O O . HOH O 7 . ? 62.434 23.145 3.568 1.00 32.27 ? 2038 HOH B O 1 HETATM 4239 O O . HOH O 7 . ? 59.836 23.577 3.217 1.00 25.05 ? 2039 HOH B O 1 HETATM 4240 O O . HOH O 7 . ? 59.938 19.076 7.627 1.00 32.18 ? 2040 HOH B O 1 HETATM 4241 O O . HOH O 7 . ? 50.714 32.140 10.695 1.00 25.34 ? 2041 HOH B O 1 HETATM 4242 O O . HOH O 7 . ? 47.299 27.676 19.276 1.00 25.32 ? 2042 HOH B O 1 HETATM 4243 O O . HOH O 7 . ? 44.567 26.088 20.320 1.00 28.81 ? 2043 HOH B O 1 HETATM 4244 O O . HOH O 7 . ? 58.128 31.700 31.907 1.00 36.17 ? 2044 HOH B O 1 HETATM 4245 O O . HOH O 7 . ? 58.121 27.571 31.690 1.00 36.08 ? 2045 HOH B O 1 HETATM 4246 O O . HOH O 7 . ? 59.720 35.414 25.834 1.00 20.16 ? 2046 HOH B O 1 HETATM 4247 O O . HOH O 7 . ? 60.094 33.428 28.710 1.00 20.84 ? 2047 HOH B O 1 HETATM 4248 O O . HOH O 7 . ? 62.531 19.797 12.218 1.00 41.73 ? 2048 HOH B O 1 HETATM 4249 O O . HOH O 7 . ? 61.665 21.203 7.591 1.00 32.80 ? 2049 HOH B O 1 HETATM 4250 O O . HOH O 7 . ? 62.765 24.993 5.548 1.00 27.63 ? 2050 HOH B O 1 HETATM 4251 O O . HOH O 7 . ? 65.009 24.919 10.010 1.00 39.84 ? 2051 HOH B O 1 HETATM 4252 O O . HOH O 7 . ? 57.135 31.926 10.059 1.00 20.90 ? 2052 HOH B O 1 HETATM 4253 O O . HOH O 7 . ? 63.456 44.250 14.527 1.00 20.44 ? 2053 HOH B O 1 HETATM 4254 O O . HOH O 7 . ? 53.820 39.471 35.562 1.00 34.05 ? 2054 HOH B O 1 HETATM 4255 O O . HOH O 7 . ? 60.827 30.316 32.292 1.00 41.85 ? 2055 HOH B O 1 HETATM 4256 O O . HOH O 7 . ? 54.035 43.314 37.201 1.00 40.34 ? 2056 HOH B O 1 HETATM 4257 O O . HOH O 7 . ? 65.260 44.176 34.853 1.00 25.22 ? 2057 HOH B O 1 HETATM 4258 O O . HOH O 7 . ? 66.252 37.721 35.520 1.00 43.42 ? 2058 HOH B O 1 HETATM 4259 O O . HOH O 7 . ? 67.131 25.988 12.424 1.00 42.87 ? 2059 HOH B O 1 HETATM 4260 O O . HOH O 7 . ? 73.250 35.919 13.687 1.00 32.34 ? 2060 HOH B O 1 HETATM 4261 O O . HOH O 7 . ? 69.191 30.109 17.543 1.00 29.44 ? 2061 HOH B O 1 HETATM 4262 O O . HOH O 7 . ? 71.193 33.079 18.665 1.00 41.86 ? 2062 HOH B O 1 HETATM 4263 O O . HOH O 7 . ? 70.043 34.401 23.698 1.00 29.81 ? 2063 HOH B O 1 HETATM 4264 O O . HOH O 7 . ? 69.167 40.028 26.877 1.00 34.36 ? 2064 HOH B O 1 HETATM 4265 O O . HOH O 7 . ? 69.669 42.211 24.364 1.00 24.80 ? 2065 HOH B O 1 HETATM 4266 O O . HOH O 7 . ? 72.250 39.344 20.461 1.00 40.13 ? 2066 HOH B O 1 HETATM 4267 O O . HOH O 7 . ? 70.865 43.301 20.750 1.00 19.91 ? 2067 HOH B O 1 HETATM 4268 O O . HOH O 7 . ? 70.023 46.713 29.722 1.00 27.58 ? 2068 HOH B O 1 HETATM 4269 O O . HOH O 7 . ? 71.958 46.740 27.472 1.00 21.07 ? 2069 HOH B O 1 HETATM 4270 O O . HOH O 7 . ? 65.961 49.580 23.405 1.00 19.50 ? 2070 HOH B O 1 HETATM 4271 O O . HOH O 7 . ? 70.364 40.002 30.760 1.00 43.74 ? 2071 HOH B O 1 HETATM 4272 O O . HOH O 7 . ? 70.336 44.692 31.413 1.00 33.52 ? 2072 HOH B O 1 HETATM 4273 O O . HOH O 7 . ? 64.986 51.843 15.846 1.00 24.25 ? 2073 HOH B O 1 HETATM 4274 O O . HOH O 7 . ? 62.460 44.225 11.931 1.00 20.58 ? 2074 HOH B O 1 HETATM 4275 O O . HOH O 7 . ? 61.440 48.721 6.673 1.00 26.52 ? 2075 HOH B O 1 HETATM 4276 O O . HOH O 7 . ? 66.427 49.577 15.265 1.00 21.40 ? 2076 HOH B O 1 HETATM 4277 O O . HOH O 7 . ? 70.415 42.870 10.937 1.00 23.26 ? 2077 HOH B O 1 HETATM 4278 O O . HOH O 7 . ? 73.123 38.636 15.319 1.00 35.26 ? 2078 HOH B O 1 HETATM 4279 O O . HOH O 7 . ? 71.785 46.466 8.416 1.00 27.21 ? 2079 HOH B O 1 HETATM 4280 O O . HOH O 7 . ? 73.368 46.498 5.714 1.00 40.57 ? 2080 HOH B O 1 HETATM 4281 O O . HOH O 7 . ? 75.544 45.993 2.231 1.00 50.16 ? 2081 HOH B O 1 HETATM 4282 O O . HOH O 7 . ? 67.423 53.069 -0.014 1.00 41.17 ? 2082 HOH B O 1 HETATM 4283 O O . HOH O 7 . ? 67.049 55.660 2.778 1.00 56.14 ? 2083 HOH B O 1 HETATM 4284 O O . HOH O 7 . ? 62.610 48.415 4.308 1.00 46.63 ? 2084 HOH B O 1 HETATM 4285 O O . HOH O 7 . ? 63.136 52.900 4.423 1.00 30.20 ? 2085 HOH B O 1 HETATM 4286 O O . HOH O 7 . ? 72.192 48.503 9.449 1.00 29.96 ? 2086 HOH B O 1 HETATM 4287 O O . HOH O 7 . ? 69.299 49.210 15.767 1.00 23.52 ? 2087 HOH B O 1 HETATM 4288 O O . HOH O 7 . ? 72.583 46.401 12.995 1.00 32.86 ? 2088 HOH B O 1 HETATM 4289 O O . HOH O 7 . ? 68.575 55.758 5.519 1.00 46.43 ? 2089 HOH B O 1 HETATM 4290 O O . HOH O 7 . ? 60.865 51.421 6.932 1.00 22.08 ? 2090 HOH B O 1 HETATM 4291 O O . HOH O 7 . ? 64.329 57.428 5.135 1.00 32.98 ? 2091 HOH B O 1 HETATM 4292 O O . HOH O 7 . ? 67.453 60.223 6.567 1.00 32.92 ? 2092 HOH B O 1 HETATM 4293 O O . HOH O 7 . ? 63.456 57.944 21.448 1.00 27.80 ? 2093 HOH B O 1 HETATM 4294 O O . HOH O 7 . ? 66.214 55.969 20.990 1.00 30.35 ? 2094 HOH B O 1 HETATM 4295 O O . HOH O 7 . ? 62.091 59.982 21.789 1.00 31.94 ? 2095 HOH B O 1 HETATM 4296 O O . HOH O 7 . ? 63.764 64.168 12.328 1.00 28.12 ? 2096 HOH B O 1 HETATM 4297 O O . HOH O 7 . ? 56.059 58.809 15.601 1.00 33.43 ? 2097 HOH B O 1 HETATM 4298 O O . HOH O 7 . ? 60.575 58.615 27.336 1.00 29.95 ? 2098 HOH B O 1 HETATM 4299 O O . HOH O 7 . ? 53.143 61.605 25.817 1.00 56.78 ? 2099 HOH B O 1 HETATM 4300 O O . HOH O 7 . ? 62.348 64.586 18.289 1.00 41.18 ? 2100 HOH B O 1 HETATM 4301 O O . HOH O 7 . ? 58.028 57.579 28.550 1.00 28.80 ? 2101 HOH B O 1 HETATM 4302 O O . HOH O 7 . ? 51.345 56.001 31.523 1.00 42.00 ? 2102 HOH B O 1 HETATM 4303 O O . HOH O 7 . ? 54.989 57.879 31.422 1.00 40.90 ? 2103 HOH B O 1 HETATM 4304 O O . HOH O 7 . ? 46.687 57.343 27.613 1.00 30.33 ? 2104 HOH B O 1 HETATM 4305 O O . HOH O 7 . ? 48.347 54.305 29.819 1.00 32.39 ? 2105 HOH B O 1 HETATM 4306 O O . HOH O 7 . ? 46.154 58.665 20.163 1.00 38.14 ? 2106 HOH B O 1 HETATM 4307 O O . HOH O 7 . ? 43.331 55.179 25.043 1.00 42.00 ? 2107 HOH B O 1 HETATM 4308 O O . HOH O 7 . ? 41.160 55.004 10.477 1.00 35.65 ? 2108 HOH B O 1 HETATM 4309 O O . HOH O 7 . ? 43.160 56.112 12.218 1.00 25.69 ? 2109 HOH B O 1 HETATM 4310 O O . HOH O 7 . ? 50.411 60.552 12.296 1.00 29.54 ? 2110 HOH B O 1 HETATM 4311 O O . HOH O 7 . ? 49.690 62.172 9.213 1.00 44.87 ? 2111 HOH B O 1 HETATM 4312 O O . HOH O 7 . ? 58.518 63.815 4.034 1.00 39.62 ? 2112 HOH B O 1 HETATM 4313 O O . HOH O 7 . ? 65.556 63.043 13.868 1.00 33.45 ? 2113 HOH B O 1 HETATM 4314 O O . HOH O 7 . ? 54.169 55.132 -1.643 1.00 44.94 ? 2114 HOH B O 1 HETATM 4315 O O . HOH O 7 . ? 47.160 53.416 6.844 1.00 33.38 ? 2115 HOH B O 1 HETATM 4316 O O . HOH O 7 . ? 42.672 56.798 -1.349 1.00 33.34 ? 2116 HOH B O 1 HETATM 4317 O O . HOH O 7 . ? 49.547 48.274 -2.426 1.00 50.97 ? 2117 HOH B O 1 HETATM 4318 O O . HOH O 7 . ? 45.710 49.499 31.258 1.00 46.97 ? 2118 HOH B O 1 HETATM 4319 O O . HOH O 7 . ? 47.144 51.874 29.266 1.00 39.09 ? 2119 HOH B O 1 HETATM 4320 O O . HOH O 7 . ? 44.281 51.754 29.134 1.00 29.35 ? 2120 HOH B O 1 HETATM 4321 O O . HOH O 7 . ? 38.785 53.228 10.077 1.00 30.34 ? 2121 HOH B O 1 HETATM 4322 O O . HOH O 7 . ? 40.694 55.397 6.314 1.00 29.61 ? 2122 HOH B O 1 HETATM 4323 O O . HOH O 7 . ? 45.143 63.410 14.510 1.00 49.93 ? 2123 HOH B O 1 HETATM 4324 O O . HOH O 7 . ? 38.444 62.502 4.435 1.00 36.51 ? 2124 HOH B O 1 HETATM 4325 O O . HOH O 7 . ? 39.848 56.330 -1.248 1.00 32.45 ? 2125 HOH B O 1 HETATM 4326 O O . HOH O 7 . ? 35.184 61.228 4.172 1.00 36.14 ? 2126 HOH B O 1 HETATM 4327 O O . HOH O 7 . ? 40.998 49.081 -8.059 1.00 35.20 ? 2127 HOH B O 1 HETATM 4328 O O . HOH O 7 . ? 40.009 42.277 -6.970 1.00 31.14 ? 2128 HOH B O 1 HETATM 4329 O O . HOH O 7 . ? 33.390 44.070 -4.045 1.00 36.36 ? 2129 HOH B O 1 HETATM 4330 O O . HOH O 7 . ? 29.615 43.042 -0.242 1.00 45.13 ? 2130 HOH B O 1 HETATM 4331 O O . HOH O 7 . ? 33.691 54.136 8.987 1.00 49.74 ? 2131 HOH B O 1 HETATM 4332 O O . HOH O 7 . ? 39.466 56.547 11.488 1.00 40.10 ? 2132 HOH B O 1 HETATM 4333 O O . HOH O 7 . ? 35.085 53.121 20.195 1.00 50.90 ? 2133 HOH B O 1 HETATM 4334 O O . HOH O 7 . ? 34.982 49.910 22.613 1.00 43.52 ? 2134 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 GLY 1 36 36 GLY GLY A . n A 1 2 VAL 2 37 37 VAL VAL A . n A 1 3 TYR 3 38 38 TYR TYR A . n A 1 4 TYR 4 39 39 TYR TYR A . n A 1 5 ALA 5 40 40 ALA ALA A . n A 1 6 THR 6 41 41 THR THR A . n A 1 7 ALA 7 42 42 ALA ALA A . n A 1 8 TYR 8 43 43 TYR TYR A . n A 1 9 TRP 9 44 44 TRP TRP A . n A 1 10 MET 10 45 45 MET MET A . n A 1 11 PRO 11 46 46 PRO PRO A . n A 1 12 THR 12 47 47 THR THR A . n A 1 13 GLU 13 48 48 GLU GLU A . n A 1 14 LYS 14 49 49 LYS LYS A . n A 1 15 THR 15 50 50 THR THR A . n A 1 16 ILE 16 51 51 ILE ILE A . n A 1 17 GLN 17 52 52 GLN GLN A . n A 1 18 VAL 18 53 53 VAL VAL A . n A 1 19 LYS 19 54 54 LYS LYS A . n A 1 20 ASN 20 55 55 ASN ASN A . n A 1 21 VAL 21 56 56 VAL VAL A . n A 1 22 LEU 22 57 57 LEU LEU A . n A 1 23 ASP 23 58 58 ASP ASP A . n A 1 24 ARG 24 59 59 ARG ARG A . n A 1 25 LYS 25 60 60 LYS LYS A . n A 1 26 GLY 26 61 61 GLY GLY A . n A 1 27 ASP 27 62 62 ASP ASP A . n A 1 28 ALA 28 63 63 ALA ALA A . n A 1 29 TYR 29 64 64 TYR TYR A . n A 1 30 GLY 30 65 65 GLY GLY A . n A 1 31 PHE 31 66 66 PHE PHE A . n A 1 32 TYR 32 67 67 TYR TYR A . n A 1 33 ASN 33 68 68 ASN ASN A . n A 1 34 ASN 34 69 69 ASN ASN A . n A 1 35 SER 35 70 70 SER SER A . n A 1 36 VAL 36 71 71 VAL VAL A . n A 1 37 LYS 37 72 72 LYS LYS A . n A 1 38 THR 38 73 73 THR THR A . n A 1 39 THR 39 74 74 THR THR A . n A 1 40 GLY 40 75 75 GLY GLY A . n A 1 41 TRP 41 76 76 TRP TRP A . n A 1 42 GLY 42 77 77 GLY GLY A . n A 1 43 ILE 43 78 78 ILE ILE A . n A 1 44 LEU 44 79 79 LEU LEU A . n A 1 45 GLU 45 80 80 GLU GLU A . n A 1 46 ILE 46 81 81 ILE ILE A . n A 1 47 LYS 47 82 82 LYS LYS A . n A 1 48 ALA 48 83 83 ALA ALA A . n A 1 49 GLY 49 84 84 GLY GLY A . n A 1 50 TYR 50 85 85 TYR TYR A . n A 1 51 GLY 51 86 86 GLY GLY A . n A 1 52 SER 52 87 87 SER SER A . n A 1 53 GLN 53 88 88 GLN GLN A . n A 1 54 SER 54 89 89 SER SER A . n A 1 55 LEU 55 90 90 LEU LEU A . n A 1 56 SER 56 91 91 SER SER A . n A 1 57 ASN 57 92 92 ASN ASN A . n A 1 58 GLU 58 93 93 GLU GLU A . n A 1 59 ILE 59 94 94 ILE ILE A . n A 1 60 ILE 60 95 95 ILE ILE A . n A 1 61 MET 61 96 96 MET MET A . n A 1 62 PHE 62 97 97 PHE PHE A . n A 1 63 ALA 63 98 98 ALA ALA A . n A 1 64 ALA 64 99 99 ALA ALA A . n A 1 65 GLY 65 100 100 GLY GLY A . n A 1 66 PHE 66 101 101 PHE PHE A . n A 1 67 LEU 67 102 102 LEU LEU A . n A 1 68 GLU 68 103 103 GLU GLU A . n A 1 69 GLY 69 104 104 GLY GLY A . n A 1 70 TYR 70 105 105 TYR TYR A . n A 1 71 LEU 71 106 106 LEU LEU A . n A 1 72 THR 72 107 107 THR THR A . n A 1 73 ALA 73 108 108 ALA ALA A . n A 1 74 PRO 74 109 109 PRO PRO A . n A 1 75 HIS 75 110 110 HIS HIS A . n A 1 76 MET 76 111 111 MET MET A . n A 1 77 ASP 77 112 112 ASP ASP A . n A 1 78 ASP 78 113 113 ASP ASP A . n A 1 79 HIS 79 114 114 HIS HIS A . n A 1 80 PHE 80 115 115 PHE PHE A . n A 1 81 THR 81 116 116 THR THR A . n A 1 82 ASN 82 117 117 ASN ASN A . n A 1 83 LEU 83 118 118 LEU LEU A . n A 1 84 TYR 84 119 119 TYR TYR A . n A 1 85 PRO 85 120 120 PRO PRO A . n A 1 86 GLN 86 121 121 GLN GLN A . n A 1 87 LEU 87 122 122 LEU LEU A . n A 1 88 ILE 88 123 123 ILE ILE A . n A 1 89 LYS 89 124 124 LYS LYS A . n A 1 90 LYS 90 125 125 LYS LYS A . n A 1 91 ARG 91 126 126 ARG ARG A . n A 1 92 SER 92 127 127 SER SER A . n A 1 93 MET 93 128 128 MET MET A . n A 1 94 LEU 94 129 129 LEU LEU A . n A 1 95 ASN 95 130 130 ASN ASN A . n A 1 96 LYS 96 131 131 LYS LYS A . n A 1 97 VAL 97 132 132 VAL VAL A . n A 1 98 GLN 98 133 133 GLN GLN A . n A 1 99 ASP 99 134 134 ASP ASP A . n A 1 100 PHE 100 135 135 PHE PHE A . n A 1 101 LEU 101 136 136 LEU LEU A . n A 1 102 THR 102 137 137 THR THR A . n A 1 103 LYS 103 138 138 LYS LYS A . n A 1 104 GLN 104 139 139 GLN GLN A . n A 1 105 ASP 105 140 140 ASP ASP A . n A 1 106 GLN 106 141 141 GLN GLN A . n A 1 107 TRP 107 142 142 TRP TRP A . n A 1 108 THR 108 143 143 THR THR A . n A 1 109 ARG 109 144 144 ARG ARG A . n A 1 110 GLU 110 145 145 GLU GLU A . n A 1 111 ASN 111 146 146 ASN ASN A . n A 1 112 ILE 112 147 147 ILE ILE A . n A 1 113 LYS 113 148 148 LYS LYS A . n A 1 114 TYR 114 149 149 TYR TYR A . n A 1 115 TYR 115 150 150 TYR TYR A . n A 1 116 LYS 116 151 151 LYS LYS A . n A 1 117 SER 117 152 152 SER SER A . n A 1 118 ASP 118 153 153 ASP ASP A . n A 1 119 PRO 119 154 154 PRO PRO A . n A 1 120 PHE 120 155 155 PHE PHE A . n A 1 121 TRP 121 156 156 TRP TRP A . n A 1 122 ARG 122 157 157 ARG ARG A . n A 1 123 HIS 123 158 158 HIS HIS A . n A 1 124 ALA 124 159 159 ALA ALA A . n A 1 125 ASP 125 160 160 ASP ASP A . n A 1 126 TYR 126 161 161 TYR TYR A . n A 1 127 VAL 127 162 162 VAL VAL A . n A 1 128 MET 128 163 163 MET MET A . n A 1 129 ALA 129 164 164 ALA ALA A . n A 1 130 GLN 130 165 165 GLN GLN A . n A 1 131 MET 131 166 166 MET MET A . n A 1 132 ASP 132 167 167 ASP ASP A . n A 1 133 GLY 133 168 168 GLY GLY A . n A 1 134 LEU 134 169 169 LEU LEU A . n A 1 135 PHE 135 170 170 PHE PHE A . n A 1 136 ALA 136 171 171 ALA ALA A . n A 1 137 GLY 137 172 172 GLY GLY A . n A 1 138 ALA 138 173 173 ALA ALA A . n A 1 139 THR 139 174 174 THR THR A . n A 1 140 LYS 140 175 175 LYS LYS A . n A 1 141 ARG 141 176 176 ARG ARG A . n A 1 142 ALA 142 177 177 ALA ALA A . n A 1 143 VAL 143 178 178 VAL VAL A . n A 1 144 LEU 144 179 179 LEU LEU A . n A 1 145 GLU 145 180 180 GLU GLU A . n A 1 146 GLY 146 181 181 GLY GLY A . n A 1 147 LYS 147 182 182 LYS LYS A . n A 1 148 LYS 148 183 183 LYS LYS A . n A 1 149 PRO 149 184 184 PRO PRO A . n A 1 150 MET 150 185 185 MET MET A . n A 1 151 THR 151 186 186 THR THR A . n A 1 152 LEU 152 187 187 LEU LEU A . n A 1 153 PHE 153 188 188 PHE PHE A . n A 1 154 GLN 154 189 189 GLN GLN A . n A 1 155 ILE 155 190 190 ILE ILE A . n A 1 156 GLN 156 191 191 GLN GLN A . n A 1 157 PHE 157 192 192 PHE PHE A . n A 1 158 LEU 158 193 193 LEU LEU A . n A 1 159 ASN 159 194 194 ASN ASN A . n A 1 160 ALA 160 195 195 ALA ALA A . n A 1 161 ILE 161 196 196 ILE ILE A . n A 1 162 GLY 162 197 197 GLY GLY A . n A 1 163 ASP 163 198 198 ASP ASP A . n A 1 164 LEU 164 199 199 LEU LEU A . n A 1 165 LEU 165 200 200 LEU LEU A . n A 1 166 ASP 166 201 201 ASP ASP A . n A 1 167 LEU 167 202 202 LEU LEU A . n A 1 168 ILE 168 203 203 ILE ILE A . n A 1 169 PRO 169 204 204 PRO PRO A . n A 1 170 SER 170 205 205 SER SER A . n B 2 1 OCS 1 225 225 OCS OCS B . n B 2 2 SER 2 226 226 SER SER B . n B 2 3 ALA 3 227 227 ALA ALA B . n B 2 4 LEU 4 228 228 LEU LEU B . n B 2 5 ILE 5 229 229 ILE ILE B . n B 2 6 LYS 6 230 230 LYS LYS B . n B 2 7 VAL 7 231 231 VAL VAL B . n B 2 8 LEU 8 232 232 LEU LEU B . n B 2 9 PRO 9 233 233 PRO PRO B . n B 2 10 GLY 10 234 234 GLY GLY B . n B 2 11 PHE 11 235 235 PHE PHE B . n B 2 12 GLU 12 236 236 GLU GLU B . n B 2 13 ASN 13 237 237 ASN ASN B . n B 2 14 ILE 14 238 238 ILE ILE B . n B 2 15 PHE 15 239 239 PHE PHE B . n B 2 16 PHE 16 240 240 PHE PHE B . n B 2 17 ALA 17 241 241 ALA ALA B . n B 2 18 HIS 18 242 242 HIS HIS B . n B 2 19 SER 19 243 243 SER SER B . n B 2 20 SER 20 244 244 SER SER B . n B 2 21 TRP 21 245 245 TRP TRP B . n B 2 22 TYR 22 246 246 TYR TYR B . n B 2 23 THR 23 247 247 THR THR B . n B 2 24 TYR 24 248 248 TYR TYR B . n B 2 25 ALA 25 249 249 ALA ALA B . n B 2 26 ALA 26 250 250 ALA ALA B . n B 2 27 MET 27 251 251 MET MET B . n B 2 28 LEU 28 252 252 LEU LEU B . n B 2 29 ARG 29 253 253 ARG ARG B . n B 2 30 ILE 30 254 254 ILE ILE B . n B 2 31 TYR 31 255 255 TYR TYR B . n B 2 32 LYS 32 256 256 LYS LYS B . n B 2 33 HIS 33 257 257 HIS HIS B . n B 2 34 TRP 34 258 258 TRP TRP B . n B 2 35 ASP 35 259 259 ASP ASP B . n B 2 36 PHE 36 260 260 PHE PHE B . n B 2 37 ASN 37 261 261 ASN ASN B . n B 2 38 ILE 38 262 262 ILE ILE B . n B 2 39 VAL 39 263 263 VAL VAL B . n B 2 40 ASP 40 264 264 ASP ASP B . n B 2 41 LYS 41 265 265 LYS LYS B . n B 2 42 ASP 42 266 266 ASP ASP B . n B 2 43 THR 43 267 267 THR THR B . n B 2 44 SER 44 268 268 SER SER B . n B 2 45 SER 45 269 269 SER SER B . n B 2 46 SER 46 270 270 SER SER B . n B 2 47 ARG 47 271 271 ARG ARG B . n B 2 48 LEU 48 272 272 LEU LEU B . n B 2 49 SER 49 273 273 SER SER B . n B 2 50 PHE 50 274 274 PHE PHE B . n B 2 51 SER 51 275 275 SER SER B . n B 2 52 SER 52 276 276 SER SER B . n B 2 53 TYR 53 277 277 TYR TYR B . n B 2 54 PRO 54 278 278 PRO PRO B . n B 2 55 GLY 55 279 279 GLY GLY B . n B 2 56 PHE 56 280 280 PHE PHE B . n B 2 57 LEU 57 281 281 LEU LEU B . n B 2 58 GLU 58 282 282 GLU GLU B . n B 2 59 SER 59 283 283 SER SER B . n B 2 60 LEU 60 284 284 LEU LEU B . n B 2 61 ASP 61 285 285 ASP ASP B . n B 2 62 ASP 62 286 286 ASP ASP B . n B 2 63 PHE 63 287 287 PHE PHE B . n B 2 64 TYR 64 288 288 TYR TYR B . n B 2 65 LEU 65 289 289 LEU LEU B . n B 2 66 LEU 66 290 290 LEU LEU B . n B 2 67 SER 67 291 291 SER SER B . n B 2 68 SER 68 292 292 SER SER B . n B 2 69 GLY 69 293 293 GLY GLY B . n B 2 70 LEU 70 294 294 LEU LEU B . n B 2 71 VAL 71 295 295 VAL VAL B . n B 2 72 LEU 72 296 296 LEU LEU B . n B 2 73 LEU 73 297 297 LEU LEU B . n B 2 74 GLN 74 298 298 GLN GLN B . n B 2 75 THR 75 299 299 THR THR B . n B 2 76 THR 76 300 300 THR THR B . n B 2 77 ASN 77 301 301 ASN ASN B . n B 2 78 SER 78 302 302 SER SER B . n B 2 79 VAL 79 303 303 VAL VAL B . n B 2 80 TYR 80 304 304 TYR TYR B . n B 2 81 ASN 81 305 305 ASN ASN B . n B 2 82 LYS 82 306 306 LYS LYS B . n B 2 83 THR 83 307 307 THR THR B . n B 2 84 LEU 84 308 308 LEU LEU B . n B 2 85 LEU 85 309 309 LEU LEU B . n B 2 86 GLN 86 310 310 GLN GLN B . n B 2 87 HIS 87 311 311 HIS HIS B . n B 2 88 VAL 88 312 312 VAL VAL B . n B 2 89 VAL 89 313 313 VAL VAL B . n B 2 90 PRO 90 314 314 PRO PRO B . n B 2 91 GLN 91 315 315 GLN GLN B . n B 2 92 SER 92 316 316 SER SER B . n B 2 93 LEU 93 317 317 LEU LEU B . n B 2 94 LEU 94 318 318 LEU LEU B . n B 2 95 ALA 95 319 319 ALA ALA B . n B 2 96 TRP 96 320 320 TRP TRP B . n B 2 97 GLN 97 321 321 GLN GLN B . n B 2 98 ARG 98 322 322 ARG ARG B . n B 2 99 VAL 99 323 323 VAL VAL B . n B 2 100 ARG 100 324 324 ARG ARG B . n B 2 101 VAL 101 325 325 VAL VAL B . n B 2 102 ALA 102 326 326 ALA ALA B . n B 2 103 SER 103 327 327 SER SER B . n B 2 104 MET 104 328 328 MET MET B . n B 2 105 MET 105 329 329 MET MET B . n B 2 106 ALA 106 330 330 ALA ALA B . n B 2 107 ASN 107 331 331 ASN ASN B . n B 2 108 ASN 108 332 332 ASN ASN B . n B 2 109 GLY 109 333 333 GLY GLY B . n B 2 110 LYS 110 334 334 LYS LYS B . n B 2 111 GLN 111 335 335 GLN GLN B . n B 2 112 TRP 112 336 336 TRP TRP B . n B 2 113 ALA 113 337 337 ALA ALA B . n B 2 114 GLU 114 338 338 GLU GLU B . n B 2 115 VAL 115 339 339 VAL VAL B . n B 2 116 PHE 116 340 340 PHE PHE B . n B 2 117 SER 117 341 341 SER SER B . n B 2 118 LYS 118 342 342 LYS LYS B . n B 2 119 TYR 119 343 343 TYR TYR B . n B 2 120 ASN 120 344 344 ASN ASN B . n B 2 121 SER 121 345 345 SER SER B . n B 2 122 GLY 122 346 346 GLY GLY B . n B 2 123 THR 123 347 347 THR THR B . n B 2 124 TYR 124 348 348 TYR TYR B . n B 2 125 ASN 125 349 349 ASN ASN B . n B 2 126 ASN 126 350 350 ASN ASN B . n B 2 127 GLN 127 351 351 GLN GLN B . n B 2 128 TYR 128 352 352 TYR TYR B . n B 2 129 MET 129 353 353 MET MET B . n B 2 130 VAL 130 354 354 VAL VAL B . n B 2 131 LEU 131 355 355 LEU LEU B . n B 2 132 ASP 132 356 356 ASP ASP B . n B 2 133 LEU 133 357 357 LEU LEU B . n B 2 134 LYS 134 358 358 LYS LYS B . n B 2 135 LYS 135 359 359 LYS LYS B . n B 2 136 VAL 136 360 360 VAL VAL B . n B 2 137 ASN 137 361 361 ASN ASN B . n B 2 138 LEU 138 362 362 LEU LEU B . n B 2 139 ASN 139 363 363 ASN ASN B . n B 2 140 HIS 140 364 364 HIS HIS B . n B 2 141 SER 141 365 365 SER SER B . n B 2 142 LEU 142 366 366 LEU LEU B . n B 2 143 ASP 143 367 367 ASP ASP B . n B 2 144 GLU 144 368 368 GLU GLU B . n B 2 145 GLY 145 369 369 GLY GLY B . n B 2 146 THR 146 370 370 THR THR B . n B 2 147 LEU 147 371 371 LEU LEU B . n B 2 148 TYR 148 372 372 TYR TYR B . n B 2 149 ILE 149 373 373 ILE ILE B . n B 2 150 VAL 150 374 374 VAL VAL B . n B 2 151 GLU 151 375 375 GLU GLU B . n B 2 152 GLN 152 376 376 GLN GLN B . n B 2 153 ILE 153 377 377 ILE ILE B . n B 2 154 PRO 154 378 378 PRO PRO B . n B 2 155 THR 155 379 379 THR THR B . n B 2 156 TYR 156 380 380 TYR TYR B . n B 2 157 VAL 157 381 381 VAL VAL B . n B 2 158 GLU 158 382 382 GLU GLU B . n B 2 159 TYR 159 383 383 TYR TYR B . n B 2 160 SER 160 384 384 SER SER B . n B 2 161 GLU 161 385 385 GLU GLU B . n B 2 162 GLN 162 386 386 GLN GLN B . n B 2 163 THR 163 387 387 THR THR B . n B 2 164 ALA 164 388 388 ALA ALA B . n B 2 165 VAL 165 389 389 VAL VAL B . n B 2 166 LEU 166 390 390 LEU LEU B . n B 2 167 ARG 167 391 391 ARG ARG B . n B 2 168 ARG 168 392 392 ARG ARG B . n B 2 169 GLY 169 393 393 GLY GLY B . n B 2 170 TYR 170 394 394 TYR TYR B . n B 2 171 TRP 171 395 395 TRP TRP B . n B 2 172 PRO 172 396 396 PRO PRO B . n B 2 173 SER 173 397 397 SER SER B . n B 2 174 TYR 174 398 398 TYR TYR B . n B 2 175 ASN 175 399 399 ASN ASN B . n B 2 176 ILE 176 400 400 ILE ILE B . n B 2 177 PRO 177 401 401 PRO PRO B . n B 2 178 PHE 178 402 402 PHE PHE B . n B 2 179 HIS 179 403 403 HIS HIS B . n B 2 180 GLU 180 404 404 GLU GLU B . n B 2 181 LYS 181 405 405 LYS LYS B . n B 2 182 VAL 182 406 406 VAL VAL B . n B 2 183 TYR 183 407 407 TYR TYR B . n B 2 184 ASN 184 408 408 ASN ASN B . n B 2 185 TRP 185 409 409 TRP TRP B . n B 2 186 SER 186 410 410 SER SER B . n B 2 187 GLY 187 411 411 GLY GLY B . n B 2 188 TYR 188 412 412 TYR TYR B . n B 2 189 PRO 189 413 413 PRO PRO B . n B 2 190 ILE 190 414 414 ILE ILE B . n B 2 191 LEU 191 415 415 LEU LEU B . n B 2 192 VAL 192 416 416 VAL VAL B . n B 2 193 LYS 193 417 417 LYS LYS B . n B 2 194 LYS 194 418 418 LYS LYS B . n B 2 195 LEU 195 419 419 LEU LEU B . n B 2 196 GLY 196 420 420 GLY GLY B . n B 2 197 LEU 197 421 421 LEU LEU B . n B 2 198 ASP 198 422 422 ASP ASP B . n B 2 199 TYR 199 423 423 TYR TYR B . n B 2 200 SER 200 424 424 SER SER B . n B 2 201 TYR 201 425 425 TYR TYR B . n B 2 202 ASP 202 426 426 ASP ASP B . n B 2 203 LEU 203 427 427 LEU LEU B . n B 2 204 ALA 204 428 428 ALA ALA B . n B 2 205 SER 205 429 429 SER SER B . n B 2 206 ARG 206 430 430 ARG ARG B . n B 2 207 ALA 207 431 431 ALA ALA B . n B 2 208 LYS 208 432 432 LYS LYS B . n B 2 209 ILE 209 433 433 ILE ILE B . n B 2 210 PHE 210 434 434 PHE PHE B . n B 2 211 ARG 211 435 435 ARG ARG B . n B 2 212 ARG 212 436 436 ARG ARG B . n B 2 213 ASP 213 437 437 ASP ASP B . n B 2 214 GLN 214 438 438 GLN GLN B . n B 2 215 GLY 215 439 439 GLY GLY B . n B 2 216 LYS 216 440 440 LYS LYS B . n B 2 217 VAL 217 441 441 VAL VAL B . n B 2 218 THR 218 442 442 THR THR B . n B 2 219 ASP 219 443 443 ASP ASP B . n B 2 220 MET 220 444 444 MET MET B . n B 2 221 GLU 221 445 445 GLU GLU B . n B 2 222 SER 222 446 446 SER SER B . n B 2 223 MET 223 447 447 MET MET B . n B 2 224 LYS 224 448 448 LYS LYS B . n B 2 225 TYR 225 449 449 TYR TYR B . n B 2 226 ILE 226 450 450 ILE ILE B . n B 2 227 MET 227 451 451 MET MET B . n B 2 228 ARG 228 452 452 ARG ARG B . n B 2 229 TYR 229 453 453 TYR TYR B . n B 2 230 ASN 230 454 454 ASN ASN B . n B 2 231 ASN 231 455 455 ASN ASN B . n B 2 232 TYR 232 456 456 TYR TYR B . n B 2 233 LYS 233 457 457 LYS LYS B . n B 2 234 GLN 234 458 458 GLN GLN B . n B 2 235 ASP 235 459 459 ASP ASP B . n B 2 236 PRO 236 460 460 PRO PRO B . n B 2 237 TYR 237 461 461 TYR TYR B . n B 2 238 SER 238 462 462 SER SER B . n B 2 239 LYS 239 463 463 LYS LYS B . n B 2 240 GLY 240 464 464 GLY GLY B . n B 2 241 ASP 241 465 465 ASP ASP B . n B 2 242 PRO 242 466 466 PRO PRO B . n B 2 243 CYS 243 467 467 CYS CYS B . n B 2 244 ASN 244 468 468 ASN ASN B . n B 2 245 THR 245 469 469 THR THR B . n B 2 246 VAL 246 470 470 VAL VAL B . n B 2 247 CYS 247 471 471 CYS CYS B . n B 2 248 CYS 248 472 472 CYS CYS B . n B 2 249 ARG 249 473 473 ARG ARG B . n B 2 250 GLU 250 474 474 GLU GLU B . n B 2 251 ASP 251 475 475 ASP ASP B . n B 2 252 LEU 252 476 476 LEU LEU B . n B 2 253 ASN 253 477 477 ASN ASN B . n B 2 254 SER 254 478 478 SER SER B . n B 2 255 HIS 255 479 479 HIS HIS B . n B 2 256 SER 256 480 480 SER SER B . n B 2 257 PRO 257 481 481 PRO PRO B . n B 2 258 SER 258 482 482 SER SER B . n B 2 259 PRO 259 483 483 PRO PRO B . n B 2 260 GLY 260 484 484 GLY GLY B . n B 2 261 GLY 261 485 485 GLY GLY B . n B 2 262 CYS 262 486 486 CYS CYS B . n B 2 263 TYR 263 487 487 TYR TYR B . n B 2 264 ASP 264 488 488 ASP ASP B . n B 2 265 THR 265 489 489 THR THR B . n B 2 266 LYS 266 490 490 LYS LYS B . n B 2 267 VAL 267 491 491 VAL VAL B . n B 2 268 ALA 268 492 492 ALA ALA B . n B 2 269 ASP 269 493 493 ASP ASP B . n B 2 270 ILE 270 494 494 ILE ILE B . n B 2 271 TYR 271 495 495 TYR TYR B . n B 2 272 LEU 272 496 496 LEU LEU B . n B 2 273 ALA 273 497 497 ALA ALA B . n B 2 274 SER 274 498 498 SER SER B . n B 2 275 LYS 275 499 499 LYS LYS B . n B 2 276 TYR 276 500 500 TYR TYR B . n B 2 277 LYS 277 501 501 LYS LYS B . n B 2 278 ALA 278 502 502 ALA ALA B . n B 2 279 TYR 279 503 503 TYR TYR B . n B 2 280 ALA 280 504 504 ALA ALA B . n B 2 281 ILE 281 505 505 ILE ILE B . n B 2 282 SER 282 506 506 SER SER B . n B 2 283 GLY 283 507 507 GLY GLY B . n B 2 284 PRO 284 508 508 PRO PRO B . n B 2 285 THR 285 509 509 THR THR B . n B 2 286 VAL 286 510 510 VAL VAL B . n B 2 287 GLN 287 511 511 GLN GLN B . n B 2 288 GLY 288 512 512 GLY GLY B . n B 2 289 GLY 289 513 513 GLY GLY B . n B 2 290 LEU 290 514 514 LEU LEU B . n B 2 291 PRO 291 515 515 PRO PRO B . n B 2 292 VAL 292 516 516 VAL VAL B . n B 2 293 PHE 293 517 517 PHE PHE B . n B 2 294 HIS 294 518 518 HIS HIS B . n B 2 295 TRP 295 519 519 TRP TRP B . n B 2 296 SER 296 520 520 SER SER B . n B 2 297 ARG 297 521 521 ARG ARG B . n B 2 298 PHE 298 522 522 PHE PHE B . n B 2 299 ASN 299 523 523 ASN ASN B . n B 2 300 LYS 300 524 524 LYS LYS B . n B 2 301 THR 301 525 525 THR THR B . n B 2 302 LEU 302 526 526 LEU LEU B . n B 2 303 HIS 303 527 527 HIS HIS B . n B 2 304 GLU 304 528 528 GLU GLU B . n B 2 305 GLY 305 529 529 GLY GLY B . n B 2 306 MET 306 530 530 MET MET B . n B 2 307 PRO 307 531 531 PRO PRO B . n B 2 308 GLU 308 532 532 GLU GLU B . n B 2 309 ALA 309 533 533 ALA ALA B . n B 2 310 TYR 310 534 534 TYR TYR B . n B 2 311 ASN 311 535 535 ASN ASN B . n B 2 312 PHE 312 536 536 PHE PHE B . n B 2 313 ASP 313 537 537 ASP ASP B . n B 2 314 PHE 314 538 538 PHE PHE B . n B 2 315 ILE 315 539 539 ILE ILE B . n B 2 316 THR 316 540 540 THR THR B . n B 2 317 MET 317 541 541 MET MET B . n B 2 318 LYS 318 542 542 LYS LYS B . n B 2 319 PRO 319 543 543 PRO PRO B . n B 2 320 ILE 320 544 544 ILE ILE B . n B 2 321 LEU 321 545 545 LEU LEU 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 NAG 1 1048 1048 NAG NAG A . D 3 NAG 2 1049 1049 NAG NAG A . E 4 P4G 1 1206 1206 P4G P4G A . F 3 NAG 1 1285 1285 NAG NAG B . G 3 NAG 2 1286 1286 NAG NAG B . H 3 NAG 1 1343 1343 NAG NAG B . I 3 NAG 2 1345 1345 NAG NAG B . J 3 NAG 1 1388 1388 NAG NAG B . K 3 NAG 1 1503 1503 NAG NAG B . L 5 P6G 1 1546 1546 P6G P6G B . M 6 CL 1 1547 1547 CL CL B . N 7 HOH 1 2001 2001 HOH HOH A . N 7 HOH 2 2002 2002 HOH HOH A . N 7 HOH 3 2003 2003 HOH HOH A . N 7 HOH 4 2004 2004 HOH HOH A . N 7 HOH 5 2005 2005 HOH HOH A . N 7 HOH 6 2006 2006 HOH HOH A . N 7 HOH 7 2007 2007 HOH HOH A . N 7 HOH 8 2008 2008 HOH HOH A . N 7 HOH 9 2009 2009 HOH HOH A . N 7 HOH 10 2010 2010 HOH HOH A . N 7 HOH 11 2011 2011 HOH HOH A . N 7 HOH 12 2012 2012 HOH HOH A . N 7 HOH 13 2013 2013 HOH HOH A . N 7 HOH 14 2014 2014 HOH HOH A . N 7 HOH 15 2015 2015 HOH HOH A . N 7 HOH 16 2016 2016 HOH HOH A . N 7 HOH 17 2017 2017 HOH HOH A . N 7 HOH 18 2018 2018 HOH HOH A . N 7 HOH 19 2019 2019 HOH HOH A . N 7 HOH 20 2020 2020 HOH HOH A . N 7 HOH 21 2021 2021 HOH HOH A . N 7 HOH 22 2022 2022 HOH HOH A . N 7 HOH 23 2023 2023 HOH HOH A . N 7 HOH 24 2024 2024 HOH HOH A . N 7 HOH 25 2025 2025 HOH HOH A . N 7 HOH 26 2026 2026 HOH HOH A . N 7 HOH 27 2027 2027 HOH HOH A . N 7 HOH 28 2028 2028 HOH HOH A . N 7 HOH 29 2029 2029 HOH HOH A . N 7 HOH 30 2030 2030 HOH HOH A . N 7 HOH 31 2031 2031 HOH HOH A . N 7 HOH 32 2032 2032 HOH HOH A . N 7 HOH 33 2033 2033 HOH HOH A . N 7 HOH 34 2034 2034 HOH HOH A . N 7 HOH 35 2035 2035 HOH HOH A . N 7 HOH 36 2036 2036 HOH HOH A . N 7 HOH 37 2037 2037 HOH HOH A . N 7 HOH 38 2038 2038 HOH HOH A . N 7 HOH 39 2039 2039 HOH HOH A . N 7 HOH 40 2040 2040 HOH HOH A . N 7 HOH 41 2041 2041 HOH HOH A . N 7 HOH 42 2042 2042 HOH HOH A . N 7 HOH 43 2043 2043 HOH HOH A . N 7 HOH 44 2044 2044 HOH HOH A . N 7 HOH 45 2045 2045 HOH HOH A . N 7 HOH 46 2046 2046 HOH HOH A . N 7 HOH 47 2047 2047 HOH HOH A . N 7 HOH 48 2048 2048 HOH HOH A . N 7 HOH 49 2049 2049 HOH HOH A . N 7 HOH 50 2050 2050 HOH HOH A . O 7 HOH 1 2001 2001 HOH HOH B . O 7 HOH 2 2002 2002 HOH HOH B . O 7 HOH 3 2003 2003 HOH HOH B . O 7 HOH 4 2004 2004 HOH HOH B . O 7 HOH 5 2005 2005 HOH HOH B . O 7 HOH 6 2006 2006 HOH HOH B . O 7 HOH 7 2007 2007 HOH HOH B . O 7 HOH 8 2008 2008 HOH HOH B . O 7 HOH 9 2009 2009 HOH HOH B . O 7 HOH 10 2010 2010 HOH HOH B . O 7 HOH 11 2011 2011 HOH HOH B . O 7 HOH 12 2012 2012 HOH HOH B . O 7 HOH 13 2013 2013 HOH HOH B . O 7 HOH 14 2014 2014 HOH HOH B . O 7 HOH 15 2015 2015 HOH HOH B . O 7 HOH 16 2016 2016 HOH HOH B . O 7 HOH 17 2017 2017 HOH HOH B . O 7 HOH 18 2018 2018 HOH HOH B . O 7 HOH 19 2019 2019 HOH HOH B . O 7 HOH 20 2020 2020 HOH HOH B . O 7 HOH 21 2021 2021 HOH HOH B . O 7 HOH 22 2022 2022 HOH HOH B . O 7 HOH 23 2023 2023 HOH HOH B . O 7 HOH 24 2024 2024 HOH HOH B . O 7 HOH 25 2025 2025 HOH HOH B . O 7 HOH 26 2026 2026 HOH HOH B . O 7 HOH 27 2027 2027 HOH HOH B . O 7 HOH 28 2028 2028 HOH HOH B . O 7 HOH 29 2029 2029 HOH HOH B . O 7 HOH 30 2030 2030 HOH HOH B . O 7 HOH 31 2031 2031 HOH HOH B . O 7 HOH 32 2032 2032 HOH HOH B . O 7 HOH 33 2033 2033 HOH HOH B . O 7 HOH 34 2034 2034 HOH HOH B . O 7 HOH 35 2035 2035 HOH HOH B . O 7 HOH 36 2036 2036 HOH HOH B . O 7 HOH 37 2037 2037 HOH HOH B . O 7 HOH 38 2038 2038 HOH HOH B . O 7 HOH 39 2039 2039 HOH HOH B . O 7 HOH 40 2040 2040 HOH HOH B . O 7 HOH 41 2041 2041 HOH HOH B . O 7 HOH 42 2042 2042 HOH HOH B . O 7 HOH 43 2043 2043 HOH HOH B . O 7 HOH 44 2044 2044 HOH HOH B . O 7 HOH 45 2045 2045 HOH HOH B . O 7 HOH 46 2046 2046 HOH HOH B . O 7 HOH 47 2047 2047 HOH HOH B . O 7 HOH 48 2048 2048 HOH HOH B . O 7 HOH 49 2049 2049 HOH HOH B . O 7 HOH 50 2050 2050 HOH HOH B . O 7 HOH 51 2051 2051 HOH HOH B . O 7 HOH 52 2052 2052 HOH HOH B . O 7 HOH 53 2053 2053 HOH HOH B . O 7 HOH 54 2054 2054 HOH HOH B . O 7 HOH 55 2055 2055 HOH HOH B . O 7 HOH 56 2056 2056 HOH HOH B . O 7 HOH 57 2057 2057 HOH HOH B . O 7 HOH 58 2058 2058 HOH HOH B . O 7 HOH 59 2059 2059 HOH HOH B . O 7 HOH 60 2060 2060 HOH HOH B . O 7 HOH 61 2061 2061 HOH HOH B . O 7 HOH 62 2062 2062 HOH HOH B . O 7 HOH 63 2063 2063 HOH HOH B . O 7 HOH 64 2064 2064 HOH HOH B . O 7 HOH 65 2065 2065 HOH HOH B . O 7 HOH 66 2066 2066 HOH HOH B . O 7 HOH 67 2067 2067 HOH HOH B . O 7 HOH 68 2068 2068 HOH HOH B . O 7 HOH 69 2069 2069 HOH HOH B . O 7 HOH 70 2070 2070 HOH HOH B . O 7 HOH 71 2071 2071 HOH HOH B . O 7 HOH 72 2072 2072 HOH HOH B . O 7 HOH 73 2073 2073 HOH HOH B . O 7 HOH 74 2074 2074 HOH HOH B . O 7 HOH 75 2075 2075 HOH HOH B . O 7 HOH 76 2076 2076 HOH HOH B . O 7 HOH 77 2077 2077 HOH HOH B . O 7 HOH 78 2078 2078 HOH HOH B . O 7 HOH 79 2079 2079 HOH HOH B . O 7 HOH 80 2080 2080 HOH HOH B . O 7 HOH 81 2081 2081 HOH HOH B . O 7 HOH 82 2082 2082 HOH HOH B . O 7 HOH 83 2083 2083 HOH HOH B . O 7 HOH 84 2084 2084 HOH HOH B . O 7 HOH 85 2085 2085 HOH HOH B . O 7 HOH 86 2086 2086 HOH HOH B . O 7 HOH 87 2087 2087 HOH HOH B . O 7 HOH 88 2088 2088 HOH HOH B . O 7 HOH 89 2089 2089 HOH HOH B . O 7 HOH 90 2090 2090 HOH HOH B . O 7 HOH 91 2091 2091 HOH HOH B . O 7 HOH 92 2092 2092 HOH HOH B . O 7 HOH 93 2093 2093 HOH HOH B . O 7 HOH 94 2094 2094 HOH HOH B . O 7 HOH 95 2095 2095 HOH HOH B . O 7 HOH 96 2096 2096 HOH HOH B . O 7 HOH 97 2097 2097 HOH HOH B . O 7 HOH 98 2098 2098 HOH HOH B . O 7 HOH 99 2099 2099 HOH HOH B . O 7 HOH 100 2100 2100 HOH HOH B . O 7 HOH 101 2101 2101 HOH HOH B . O 7 HOH 102 2102 2102 HOH HOH B . O 7 HOH 103 2103 2103 HOH HOH B . O 7 HOH 104 2104 2104 HOH HOH B . O 7 HOH 105 2105 2105 HOH HOH B . O 7 HOH 106 2106 2106 HOH HOH B . O 7 HOH 107 2107 2107 HOH HOH B . O 7 HOH 108 2108 2108 HOH HOH B . O 7 HOH 109 2109 2109 HOH HOH B . O 7 HOH 110 2110 2110 HOH HOH B . O 7 HOH 111 2111 2111 HOH HOH B . O 7 HOH 112 2112 2112 HOH HOH B . O 7 HOH 113 2113 2113 HOH HOH B . O 7 HOH 114 2114 2114 HOH HOH B . O 7 HOH 115 2115 2115 HOH HOH B . O 7 HOH 116 2116 2116 HOH HOH B . O 7 HOH 117 2117 2117 HOH HOH B . O 7 HOH 118 2118 2118 HOH HOH B . O 7 HOH 119 2119 2119 HOH HOH B . O 7 HOH 120 2120 2120 HOH HOH B . O 7 HOH 121 2121 2121 HOH HOH B . O 7 HOH 122 2122 2122 HOH HOH B . O 7 HOH 123 2123 2123 HOH HOH B . O 7 HOH 124 2124 2124 HOH HOH B . O 7 HOH 125 2125 2125 HOH HOH B . O 7 HOH 126 2126 2126 HOH HOH B . O 7 HOH 127 2127 2127 HOH HOH B . O 7 HOH 128 2128 2128 HOH HOH B . O 7 HOH 129 2129 2129 HOH HOH B . O 7 HOH 130 2130 2130 HOH HOH B . O 7 HOH 131 2131 2131 HOH HOH B . O 7 HOH 132 2132 2132 HOH HOH B . O 7 HOH 133 2133 2133 HOH HOH B . O 7 HOH 134 2134 2134 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 33 A ASN 68 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 81 B ASN 305 ? ASN 'GLYCOSYLATION SITE' 3 B ASN 139 B ASN 363 ? ASN 'GLYCOSYLATION SITE' 4 B ASN 184 B ASN 408 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 299 B ASN 523 ? ASN 'GLYCOSYLATION SITE' 6 B OCS 1 B OCS 225 ? CYS 'CYSTEINESULFONIC ACID' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details tetrameric _pdbx_struct_assembly.oligomeric_count 4 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O # 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)' 20580 ? 1 MORE -78.2 ? 1 'SSA (A^2)' 37250 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 6_765 -x+2,-x+y+1,-z+1/3 -0.5000000000 -0.8660254038 0.0000000000 146.0550000000 -0.8660254038 0.5000000000 0.0000000000 84.3248935665 0.0000000000 0.0000000000 -1.0000000000 46.9816666667 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-09-18 2 'Structure model' 1 1 2014-02-05 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.6.0117 ? 1 XDS 'data reduction' . ? 2 MOLREP phasing . ? 3 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OE2 B GLU 445 ? ? O B HOH 2107 ? ? 2.14 2 1 O A TYR 85 ? ? O A HOH 2002 ? ? 2.19 # loop_ _pdbx_validate_rmsd_bond.id _pdbx_validate_rmsd_bond.PDB_model_num _pdbx_validate_rmsd_bond.auth_atom_id_1 _pdbx_validate_rmsd_bond.auth_asym_id_1 _pdbx_validate_rmsd_bond.auth_comp_id_1 _pdbx_validate_rmsd_bond.auth_seq_id_1 _pdbx_validate_rmsd_bond.PDB_ins_code_1 _pdbx_validate_rmsd_bond.label_alt_id_1 _pdbx_validate_rmsd_bond.auth_atom_id_2 _pdbx_validate_rmsd_bond.auth_asym_id_2 _pdbx_validate_rmsd_bond.auth_comp_id_2 _pdbx_validate_rmsd_bond.auth_seq_id_2 _pdbx_validate_rmsd_bond.PDB_ins_code_2 _pdbx_validate_rmsd_bond.label_alt_id_2 _pdbx_validate_rmsd_bond.bond_value _pdbx_validate_rmsd_bond.bond_target_value _pdbx_validate_rmsd_bond.bond_deviation _pdbx_validate_rmsd_bond.bond_standard_deviation _pdbx_validate_rmsd_bond.linker_flag 1 1 CG B HIS 242 ? ? CD2 B HIS 242 ? ? 1.426 1.354 0.072 0.009 N 2 1 CG B HIS 257 ? ? CD2 B HIS 257 ? ? 1.408 1.354 0.054 0.009 N 3 1 CE2 B TRP 320 ? ? CD2 B TRP 320 ? ? 1.504 1.409 0.095 0.012 N 4 1 CE2 B TRP 409 ? ? CD2 B TRP 409 ? ? 1.486 1.409 0.077 0.012 N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE B ARG 322 ? ? CZ B ARG 322 ? ? NH2 B ARG 322 ? ? 117.02 120.30 -3.28 0.50 N 2 1 NE B ARG 435 ? ? CZ B ARG 435 ? ? NH1 B ARG 435 ? ? 123.49 120.30 3.19 0.50 N 3 1 CB B ASP 443 ? ? CG B ASP 443 ? ? OD1 B ASP 443 ? ? 126.67 118.30 8.37 0.90 N # 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 ASN A 55 ? ? -88.84 46.34 2 1 ARG A 59 ? ? -59.73 -9.41 3 1 TYR A 150 ? ? -98.06 55.78 4 1 TYR B 246 ? ? -171.88 -165.53 5 1 MET B 251 ? ? -77.15 27.20 6 1 SER B 276 ? ? -157.88 -157.02 7 1 LEU B 281 ? ? -84.00 39.80 8 1 LEU B 284 ? ? 65.14 -44.12 9 1 HIS B 364 ? ? -141.46 -54.79 10 1 THR B 379 ? ? 74.39 -5.77 11 1 TYR B 398 ? ? -156.12 49.21 12 1 ASP B 443 ? ? -172.55 -175.21 13 1 ASN B 454 ? ? -130.66 -70.47 14 1 HIS B 527 ? ? -160.18 37.70 15 1 ASN B 535 ? ? -140.20 45.34 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 TRP _pdbx_validate_peptide_omega.auth_asym_id_1 A _pdbx_validate_peptide_omega.auth_seq_id_1 76 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 GLY _pdbx_validate_peptide_omega.auth_asym_id_2 A _pdbx_validate_peptide_omega.auth_seq_id_2 77 _pdbx_validate_peptide_omega.PDB_ins_code_2 ? _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega 147.17 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 '1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE' P4G 5 'HEXAETHYLENE GLYCOL' P6G 6 'CHLORIDE ION' CL 7 water HOH #