data_2B31 # _entry.id 2B31 # _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 2B31 RCSB RCSB034613 WWPDB D_1000034613 # _pdbx_database_PDB_obs_spr.id SPRSDE _pdbx_database_PDB_obs_spr.date 2005-09-27 _pdbx_database_PDB_obs_spr.pdb_id 2B31 _pdbx_database_PDB_obs_spr.replace_pdb_id 1ZU9 _pdbx_database_PDB_obs_spr.details ? # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1qzo 'Crystal Structure Of A Goat Signalling Protein Secreted During Involution' unspecified PDB 1syt ;Crystal Structure Of Signalling Protein From Goat Spg-40 In The Presense Of N, N', N''-Triacetyl-Chitotriose At 2.6 A Resolution ; unspecified PDB 1zbv 'Crystal Structure Of The Goat Signalling Protein (Spg-40) Complexed With A Designed Peptide Trp-Pro-Trp At 3.2A Resolution' unspecified PDB 2B2P 'crystal structure of the complex of signalling protein from sheep (SPS-40) with a pentasaccharide at 2.8 A resolution' unspecified PDB 2B2Z 'Crystal structure of the complex formed between goat signalling protein and the hexasaccharide at 2.28 A resolution' unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2B31 _pdbx_database_status.recvd_initial_deposition_date 2005-09-19 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Ethayathulla, A.S.' 1 'Kumar, J.' 2 'Srivastava, D.B.' 3 'Singh, N.' 4 'Sharma, S.' 5 'Bhushan, A.' 6 'Singh, T.P.' 7 # _citation.id primary _citation.title ;Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 3.1 A resolution reveals large scale conformational changes in the residues of TIM barrel ; _citation.journal_abbrev 'TO BE PUBLISHED' _citation.journal_volume ? _citation.page_first ? _citation.page_last ? _citation.year ? _citation.journal_id_ASTM ? _citation.country ? _citation.journal_id_ISSN ? _citation.journal_id_CSD 0353 _citation.book_publisher ? _citation.pdbx_database_id_PubMed ? _citation.pdbx_database_id_DOI ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Ethayathulla, A.S.' 1 primary 'Kumar, J.' 2 primary 'Srivastava, D.B.' 3 primary 'Singh, N.' 4 primary 'Sharma, S.' 5 primary 'Bhushan, A.' 6 primary 'Singh, T.P.' 7 # _cell.entry_id 2B31 _cell.length_a 62.745 _cell.length_b 66.613 _cell.length_c 107.812 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 2B31 _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'Chitinase-3-like protein 1, SPG-40' 40728.090 1 ? ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 5 ? ? ? ? 3 non-polymer man '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' 221.208 2 ? ? ? ? 4 water nat water 18.015 71 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Mammary gland protein MGP-40, BP40' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;YKLICYYTSWSQYREGDGSCFPDAIDPFLCTHVIYSFANISNNEIDTWEWNDVTLYDTLNTLKNRNPKLKTLLSVGGWNF GPERFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKRHLTALVKEMKAEFAREAQAGTERLLLSAAVSAG KIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFRGNSDASSRFSNADYAVSYMLRLGAPANKLVMGIPTFG RSFTLASSKTDVGAPISGPGIPGRFTKEKGILAYYEICDFLHGATTHRFRDQQVPYATKGNQWVAYDDQESVKNKARYLK NRQLAGAMVWALDLDDFRGTFCGQNLTFPLTSAVKDVLARV ; _entity_poly.pdbx_seq_one_letter_code_can ;YKLICYYTSWSQYREGDGSCFPDAIDPFLCTHVIYSFANISNNEIDTWEWNDVTLYDTLNTLKNRNPKLKTLLSVGGWNF GPERFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKRHLTALVKEMKAEFAREAQAGTERLLLSAAVSAG KIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFRGNSDASSRFSNADYAVSYMLRLGAPANKLVMGIPTFG RSFTLASSKTDVGAPISGPGIPGRFTKEKGILAYYEICDFLHGATTHRFRDQQVPYATKGNQWVAYDDQESVKNKARYLK NRQLAGAMVWALDLDDFRGTFCGQNLTFPLTSAVKDVLARV ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 TYR n 1 2 LYS n 1 3 LEU n 1 4 ILE n 1 5 CYS n 1 6 TYR n 1 7 TYR n 1 8 THR n 1 9 SER n 1 10 TRP n 1 11 SER n 1 12 GLN n 1 13 TYR n 1 14 ARG n 1 15 GLU n 1 16 GLY n 1 17 ASP n 1 18 GLY n 1 19 SER n 1 20 CYS n 1 21 PHE n 1 22 PRO n 1 23 ASP n 1 24 ALA n 1 25 ILE n 1 26 ASP n 1 27 PRO n 1 28 PHE n 1 29 LEU n 1 30 CYS n 1 31 THR n 1 32 HIS n 1 33 VAL n 1 34 ILE n 1 35 TYR n 1 36 SER n 1 37 PHE n 1 38 ALA n 1 39 ASN n 1 40 ILE n 1 41 SER n 1 42 ASN n 1 43 ASN n 1 44 GLU n 1 45 ILE n 1 46 ASP n 1 47 THR n 1 48 TRP n 1 49 GLU n 1 50 TRP n 1 51 ASN n 1 52 ASP n 1 53 VAL n 1 54 THR n 1 55 LEU n 1 56 TYR n 1 57 ASP n 1 58 THR n 1 59 LEU n 1 60 ASN n 1 61 THR n 1 62 LEU n 1 63 LYS n 1 64 ASN n 1 65 ARG n 1 66 ASN n 1 67 PRO n 1 68 LYS n 1 69 LEU n 1 70 LYS n 1 71 THR n 1 72 LEU n 1 73 LEU n 1 74 SER n 1 75 VAL n 1 76 GLY n 1 77 GLY n 1 78 TRP n 1 79 ASN n 1 80 PHE n 1 81 GLY n 1 82 PRO n 1 83 GLU n 1 84 ARG n 1 85 PHE n 1 86 SER n 1 87 LYS n 1 88 ILE n 1 89 ALA n 1 90 SER n 1 91 LYS n 1 92 THR n 1 93 GLN n 1 94 SER n 1 95 ARG n 1 96 ARG n 1 97 THR n 1 98 PHE n 1 99 ILE n 1 100 LYS n 1 101 SER n 1 102 VAL n 1 103 PRO n 1 104 PRO n 1 105 PHE n 1 106 LEU n 1 107 ARG n 1 108 THR n 1 109 HIS n 1 110 GLY n 1 111 PHE n 1 112 ASP n 1 113 GLY n 1 114 LEU n 1 115 ASP n 1 116 LEU n 1 117 ALA n 1 118 TRP n 1 119 LEU n 1 120 TYR n 1 121 PRO n 1 122 GLY n 1 123 ARG n 1 124 ARG n 1 125 ASP n 1 126 LYS n 1 127 ARG n 1 128 HIS n 1 129 LEU n 1 130 THR n 1 131 ALA n 1 132 LEU n 1 133 VAL n 1 134 LYS n 1 135 GLU n 1 136 MET n 1 137 LYS n 1 138 ALA n 1 139 GLU n 1 140 PHE n 1 141 ALA n 1 142 ARG n 1 143 GLU n 1 144 ALA n 1 145 GLN n 1 146 ALA n 1 147 GLY n 1 148 THR n 1 149 GLU n 1 150 ARG n 1 151 LEU n 1 152 LEU n 1 153 LEU n 1 154 SER n 1 155 ALA n 1 156 ALA n 1 157 VAL n 1 158 SER n 1 159 ALA n 1 160 GLY n 1 161 LYS n 1 162 ILE n 1 163 ALA n 1 164 ILE n 1 165 ASP n 1 166 ARG n 1 167 GLY n 1 168 TYR n 1 169 ASP n 1 170 ILE n 1 171 ALA n 1 172 GLN n 1 173 ILE n 1 174 SER n 1 175 ARG n 1 176 HIS n 1 177 LEU n 1 178 ASP n 1 179 PHE n 1 180 ILE n 1 181 SER n 1 182 LEU n 1 183 LEU n 1 184 THR n 1 185 TYR n 1 186 ASP n 1 187 PHE n 1 188 HIS n 1 189 GLY n 1 190 ALA n 1 191 TRP n 1 192 ARG n 1 193 GLN n 1 194 THR n 1 195 VAL n 1 196 GLY n 1 197 HIS n 1 198 HIS n 1 199 SER n 1 200 PRO n 1 201 LEU n 1 202 PHE n 1 203 ARG n 1 204 GLY n 1 205 ASN n 1 206 SER n 1 207 ASP n 1 208 ALA n 1 209 SER n 1 210 SER n 1 211 ARG n 1 212 PHE n 1 213 SER n 1 214 ASN n 1 215 ALA n 1 216 ASP n 1 217 TYR n 1 218 ALA n 1 219 VAL n 1 220 SER n 1 221 TYR n 1 222 MET n 1 223 LEU n 1 224 ARG n 1 225 LEU n 1 226 GLY n 1 227 ALA n 1 228 PRO n 1 229 ALA n 1 230 ASN n 1 231 LYS n 1 232 LEU n 1 233 VAL n 1 234 MET n 1 235 GLY n 1 236 ILE n 1 237 PRO n 1 238 THR n 1 239 PHE n 1 240 GLY n 1 241 ARG n 1 242 SER n 1 243 PHE n 1 244 THR n 1 245 LEU n 1 246 ALA n 1 247 SER n 1 248 SER n 1 249 LYS n 1 250 THR n 1 251 ASP n 1 252 VAL n 1 253 GLY n 1 254 ALA n 1 255 PRO n 1 256 ILE n 1 257 SER n 1 258 GLY n 1 259 PRO n 1 260 GLY n 1 261 ILE n 1 262 PRO n 1 263 GLY n 1 264 ARG n 1 265 PHE n 1 266 THR n 1 267 LYS n 1 268 GLU n 1 269 LYS n 1 270 GLY n 1 271 ILE n 1 272 LEU n 1 273 ALA n 1 274 TYR n 1 275 TYR n 1 276 GLU n 1 277 ILE n 1 278 CYS n 1 279 ASP n 1 280 PHE n 1 281 LEU n 1 282 HIS n 1 283 GLY n 1 284 ALA n 1 285 THR n 1 286 THR n 1 287 HIS n 1 288 ARG n 1 289 PHE n 1 290 ARG n 1 291 ASP n 1 292 GLN n 1 293 GLN n 1 294 VAL n 1 295 PRO n 1 296 TYR n 1 297 ALA n 1 298 THR n 1 299 LYS n 1 300 GLY n 1 301 ASN n 1 302 GLN n 1 303 TRP n 1 304 VAL n 1 305 ALA n 1 306 TYR n 1 307 ASP n 1 308 ASP n 1 309 GLN n 1 310 GLU n 1 311 SER n 1 312 VAL n 1 313 LYS n 1 314 ASN n 1 315 LYS n 1 316 ALA n 1 317 ARG n 1 318 TYR n 1 319 LEU n 1 320 LYS n 1 321 ASN n 1 322 ARG n 1 323 GLN n 1 324 LEU n 1 325 ALA n 1 326 GLY n 1 327 ALA n 1 328 MET n 1 329 VAL n 1 330 TRP n 1 331 ALA n 1 332 LEU n 1 333 ASP n 1 334 LEU n 1 335 ASP n 1 336 ASP n 1 337 PHE n 1 338 ARG n 1 339 GLY n 1 340 THR n 1 341 PHE n 1 342 CYS n 1 343 GLY n 1 344 GLN n 1 345 ASN n 1 346 LEU n 1 347 THR n 1 348 PHE n 1 349 PRO n 1 350 LEU n 1 351 THR n 1 352 SER n 1 353 ALA n 1 354 VAL n 1 355 LYS n 1 356 ASP n 1 357 VAL n 1 358 LEU n 1 359 ALA n 1 360 ARG n 1 361 VAL n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name goat _entity_src_nat.pdbx_organism_scientific 'Capra hircus' _entity_src_nat.pdbx_ncbi_taxonomy_id 9925 _entity_src_nat.genus Capra _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion 'Mammary gland' _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 ? # _struct_ref.id 1 _struct_ref.db_name GB _struct_ref.db_code AAL87007 _struct_ref.pdbx_db_accession 19526603 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;YKLICYYTSWSQYREGDGSCFPDAIDPFLCTHIIYSFANISNNEIDTWEWNDVTLYDTLNTLKNRNPKLKTLLSVGGWNF GPERFSKIASKTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKRHLTGLVKEMKAEFAREAQAGTERLLLSAAVSAG KIAIDRGYDIAQISRHLDFISLLTYDFHGAWRQTVGHHSPLFRGQEDASSDRFSNADYAVSYMLRLGAPANKLVMGIPTF GRSFTLASSKTDVGAPISGPGIPGRFTKEKGILAYYEICDFLHGATTHRFRDQQVPYATKGNQWVAYDDQESVKNKARYL KNRQLAGAMVWALDLDDFRGTFCGQNLTFPLTSAVKDVLAEV ; _struct_ref.pdbx_align_begin 22 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2B31 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 361 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession 19526603 _struct_ref_seq.db_align_beg 22 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 383 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 362 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 2B31 VAL A 33 ? GB 19526603 ILE 54 'SEE REMARK 999' 33 1 1 2B31 ALA A 131 ? GB 19526603 GLY 152 'SEE REMARK 999' 131 2 1 2B31 ASN A 205 ? GB 19526603 GLN 226 'SEE REMARK 999' 205 3 1 2B31 SER A 206 ? GB 19526603 GLU 227 'SEE REMARK 999' 206 4 1 2B31 ? A ? ? GB 19526603 ASP 232 'SEE REMARK 999' ? 5 1 2B31 ARG A 360 ? GB 19526603 GLU 382 'SEE REMARK 999' 361 6 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 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 NDG D-saccharide . '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 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 2B31 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.80 _exptl_crystal.density_percent_sol 56.30 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp 298.0 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.80 _exptl_crystal_grow.pdbx_details '25mM Tris HCl, 50mM NaCl, 19% ethanol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298.0 K, pH 7.80' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 298.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 2005-05-14 _diffrn_detector.details MIRROR # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator GRAPHITE _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'RIGAKU RU300' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength 1.5418 _diffrn_source.pdbx_wavelength_list ? # _reflns.entry_id 2B31 _reflns.observed_criterion_sigma_I 0.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 56.700 _reflns.d_resolution_high 3.100 _reflns.number_obs 8493 _reflns.number_all ? _reflns.percent_possible_obs 98.5 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.11 _reflns.pdbx_netI_over_sigmaI 7.0000 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 3.10 _reflns_shell.d_res_low 3.21 _reflns_shell.percent_possible_all 99.5 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.43 _reflns_shell.meanI_over_sigI_obs 2.400 _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 2B31 _refine.ls_number_reflns_obs 8090 _refine.ls_number_reflns_all 8493 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.000 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 56.70 _refine.ls_d_res_high 3.10 _refine.ls_percent_reflns_obs 98.17 _refine.ls_R_factor_obs 0.17859 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1766 _refine.ls_R_factor_R_free 0.21782 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.700 _refine.ls_number_reflns_R_free 403 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.932 _refine.correlation_coeff_Fo_to_Fc_free 0.886 _refine.B_iso_mean 24.973 _refine.aniso_B[1][1] 0.40000 _refine.aniso_B[2][2] 0.08000 _refine.aniso_B[3][3] -0.48000 _refine.aniso_B[1][2] 0.00000 _refine.aniso_B[1][3] 0.00000 _refine.aniso_B[2][3] 0.00000 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _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' _refine.pdbx_starting_model 'PDB ENTRY 1QZO' _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 ? _refine.pdbx_overall_ESU_R_Free 0.424 _refine.overall_SU_ML 0.464 _refine.overall_SU_B 25.315 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_phase_error ? _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 2876 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 98 _refine_hist.number_atoms_solvent 71 _refine_hist.number_atoms_total 3045 _refine_hist.d_res_high 3.10 _refine_hist.d_res_low 56.70 # 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 0.020 0.021 ? 3057 'X-RAY DIFFRACTION' ? r_bond_other_d 0.003 0.020 ? 2703 'X-RAY DIFFRACTION' ? r_angle_refined_deg 2.440 1.972 ? 4152 'X-RAY DIFFRACTION' ? r_angle_other_deg 2.381 3.000 ? 6234 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 2.243 3.000 ? 359 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 22.793 15.000 ? 497 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_chiral_restr 0.152 0.200 ? 459 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.007 0.020 ? 3334 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.006 0.020 ? 671 'X-RAY DIFFRACTION' ? r_nbd_refined 0.296 0.300 ? 744 'X-RAY DIFFRACTION' ? r_nbd_other 0.268 0.300 ? 2855 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other 0.472 0.500 ? 10 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.233 0.500 ? 165 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other 0.231 0.500 ? 5 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.311 0.300 ? 6 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.409 0.300 ? 19 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.258 0.500 ? 4 '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 1.683 1.500 ? 1791 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 3.163 2.000 ? 2872 'X-RAY DIFFRACTION' ? r_scbond_it 3.417 3.000 ? 1266 'X-RAY DIFFRACTION' ? r_scangle_it 5.634 4.500 ? 1280 '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_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 3.10 _refine_ls_shell.d_res_low 3.18 _refine_ls_shell.number_reflns_R_work 609 _refine_ls_shell.R_factor_R_work 0.243 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.231 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 30 _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_all ? # _struct.entry_id 2B31 _struct.title ;Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 3.1 A resolution reveals large scale conformational changes in the residues of TIM barrel ; _struct.pdbx_descriptor 'Chitinase-3-like protein 1, SPG-40' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2B31 _struct_keywords.pdbx_keywords 'SIGNALING PROTEIN' _struct_keywords.text 'SIGNALLING PROTEIN, COMPLEX PENTASACCHARIDE, SIGNALING PROTEIN' # 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 2 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 3 ? I N N 4 ? # _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 TRP A 10 ? ARG A 14 ? TRP A 10 ARG A 14 5 ? 5 HELX_P HELX_P2 2 GLU A 15 ? SER A 19 ? GLU A 15 SER A 19 5 ? 5 HELX_P HELX_P3 3 PHE A 21 ? ILE A 25 ? PHE A 21 ILE A 25 5 ? 5 HELX_P HELX_P4 4 ASN A 51 ? ASN A 60 ? ASN A 51 ASN A 60 1 ? 10 HELX_P HELX_P5 5 THR A 61 ? ARG A 65 ? THR A 61 ARG A 65 5 ? 5 HELX_P HELX_P6 6 GLY A 81 ? SER A 90 ? GLY A 81 SER A 90 1 ? 10 HELX_P HELX_P7 7 LYS A 91 ? HIS A 109 ? LYS A 91 HIS A 109 1 ? 19 HELX_P HELX_P8 8 GLY A 122 ? ARG A 124 ? GLY A 122 ARG A 124 5 ? 3 HELX_P HELX_P9 9 ASP A 125 ? ALA A 144 ? ASP A 125 ALA A 144 1 ? 20 HELX_P HELX_P10 10 GLN A 145 ? GLY A 147 ? GLN A 145 GLY A 147 5 ? 3 HELX_P HELX_P11 11 GLY A 160 ? TYR A 168 ? GLY A 160 TYR A 168 1 ? 9 HELX_P HELX_P12 12 ASP A 169 ? LEU A 177 ? ASP A 169 LEU A 177 1 ? 9 HELX_P HELX_P13 13 ASN A 214 ? GLY A 226 ? ASN A 215 GLY A 227 1 ? 13 HELX_P HELX_P14 14 PRO A 228 ? ASN A 230 ? PRO A 229 ASN A 231 5 ? 3 HELX_P HELX_P15 15 TYR A 274 ? LEU A 281 ? TYR A 275 LEU A 282 1 ? 8 HELX_P HELX_P16 16 ASP A 308 ? ARG A 322 ? ASP A 309 ARG A 323 1 ? 15 HELX_P HELX_P17 17 PHE A 348 ? ALA A 359 ? PHE A 349 ALA A 360 1 ? 12 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 5 SG ? ? ? 1_555 A CYS 30 SG ? ? A CYS 5 A CYS 30 1_555 ? ? ? ? ? ? ? 1.973 ? disulf2 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 342 SG ? ? A CYS 279 A CYS 343 1_555 ? ? ? ? ? ? ? 1.995 ? covale1 covale ? ? A ASN 39 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 39 A NAG 368 1_555 ? ? ? ? ? ? ? 1.459 ? covale2 covale ? ? B NAG . O4 ? ? ? 1_555 C NDG . C1 ? ? A NAG 363 A NDG 364 1_555 ? ? ? ? ? ? ? 1.487 ? covale3 covale ? ? C NDG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NDG 364 A NAG 365 1_555 ? ? ? ? ? ? ? 1.409 ? covale4 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 365 A NAG 366 1_555 ? ? ? ? ? ? ? 1.552 ? covale5 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 366 A NAG 367 1_555 ? ? ? ? ? ? ? 1.411 ? covale6 covale ? ? G NAG . O4 ? ? ? 1_555 H NDG . C1 ? ? A NAG 368 A NDG 369 1_555 ? ? ? ? ? ? ? 1.483 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 10 ? B ? 3 ? C ? 5 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? parallel A 7 8 ? parallel A 8 9 ? parallel A 9 10 ? parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? 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 A 1 GLU A 44 ? ASP A 46 ? GLU A 44 ASP A 46 A 2 HIS A 32 ? SER A 41 ? HIS A 32 SER A 41 A 3 LYS A 70 ? GLY A 76 ? LYS A 70 GLY A 76 A 4 GLY A 113 ? ALA A 117 ? GLY A 113 ALA A 117 A 5 LEU A 152 ? VAL A 157 ? LEU A 152 VAL A 157 A 6 PHE A 179 ? LEU A 182 ? PHE A 179 LEU A 182 A 7 LEU A 232 ? PRO A 237 ? LEU A 233 PRO A 238 A 8 GLY A 326 ? TRP A 330 ? GLY A 327 TRP A 331 A 9 LYS A 2 ? THR A 8 ? LYS A 2 THR A 8 A 10 HIS A 32 ? SER A 41 ? HIS A 32 SER A 41 B 1 ILE A 256 ? PRO A 259 ? ILE A 257 PRO A 260 B 2 PHE A 239 ? LEU A 245 ? PHE A 240 LEU A 246 B 3 ILE A 271 ? ALA A 273 ? ILE A 272 ALA A 274 C 1 ILE A 256 ? PRO A 259 ? ILE A 257 PRO A 260 C 2 PHE A 239 ? LEU A 245 ? PHE A 240 LEU A 246 C 3 GLN A 302 ? ALA A 305 ? GLN A 303 ALA A 306 C 4 VAL A 294 ? LYS A 299 ? VAL A 295 LYS A 300 C 5 THR A 285 ? PHE A 289 ? THR A 286 PHE A 290 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O ASP A 46 ? O ASP A 46 N ASN A 39 ? N ASN A 39 A 2 3 N ALA A 38 ? N ALA A 38 O SER A 74 ? O SER A 74 A 3 4 N VAL A 75 ? N VAL A 75 O ASP A 115 ? O ASP A 115 A 4 5 N LEU A 116 ? N LEU A 116 O ALA A 156 ? O ALA A 156 A 5 6 N ALA A 155 ? N ALA A 155 O SER A 181 ? O SER A 181 A 6 7 N LEU A 182 ? N LEU A 182 O VAL A 233 ? O VAL A 234 A 7 8 N ILE A 236 ? N ILE A 237 O MET A 328 ? O MET A 329 A 8 9 O VAL A 329 ? O VAL A 330 N ILE A 4 ? N ILE A 4 A 9 10 N CYS A 5 ? N CYS A 5 O HIS A 32 ? O HIS A 32 B 1 2 O SER A 257 ? O SER A 258 N THR A 244 ? N THR A 245 B 2 3 N GLY A 240 ? N GLY A 241 O LEU A 272 ? O LEU A 273 C 1 2 O SER A 257 ? O SER A 258 N THR A 244 ? N THR A 245 C 2 3 N ARG A 241 ? N ARG A 242 O ALA A 305 ? O ALA A 306 C 3 4 O VAL A 304 ? O VAL A 305 N ALA A 297 ? N ALA A 298 C 4 5 O THR A 298 ? O THR A 299 N THR A 285 ? N THR A 286 # 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 ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 363' AC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NDG A 364' AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 365' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 366' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 367' AC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 368' AC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NDG A 369' # 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 8 TRP A 78 ? TRP A 78 . ? 1_555 ? 2 AC1 8 ALA A 117 ? ALA A 117 . ? 1_555 ? 3 AC1 8 LEU A 119 ? LEU A 119 . ? 1_555 ? 4 AC1 8 LEU A 183 ? LEU A 183 . ? 1_555 ? 5 AC1 8 TYR A 185 ? TYR A 185 . ? 1_555 ? 6 AC1 8 PHE A 239 ? PHE A 240 . ? 1_555 ? 7 AC1 8 TRP A 330 ? TRP A 331 . ? 1_555 ? 8 AC1 8 NDG C . ? NDG A 364 . ? 1_555 ? 9 AC2 8 TRP A 10 ? TRP A 10 . ? 1_555 ? 10 AC2 8 TRP A 78 ? TRP A 78 . ? 1_555 ? 11 AC2 8 ASN A 79 ? ASN A 79 . ? 1_555 ? 12 AC2 8 GLU A 268 ? GLU A 269 . ? 1_555 ? 13 AC2 8 ILE A 271 ? ILE A 272 . ? 1_555 ? 14 AC2 8 TRP A 330 ? TRP A 331 . ? 1_555 ? 15 AC2 8 NAG B . ? NAG A 363 . ? 1_555 ? 16 AC2 8 NAG D . ? NAG A 365 . ? 1_555 ? 17 AC3 6 TRP A 10 ? TRP A 10 . ? 1_555 ? 18 AC3 6 TRP A 48 ? TRP A 48 . ? 1_555 ? 19 AC3 6 ASN A 79 ? ASN A 79 . ? 1_555 ? 20 AC3 6 GLU A 268 ? GLU A 269 . ? 1_555 ? 21 AC3 6 NDG C . ? NDG A 364 . ? 1_555 ? 22 AC3 6 NAG E . ? NAG A 366 . ? 1_555 ? 23 AC4 4 TYR A 13 ? TYR A 13 . ? 1_555 ? 24 AC4 4 GLU A 49 ? GLU A 49 . ? 1_555 ? 25 AC4 4 NAG D . ? NAG A 365 . ? 1_555 ? 26 AC4 4 NAG F . ? NAG A 367 . ? 1_555 ? 27 AC5 4 TYR A 13 ? TYR A 13 . ? 1_555 ? 28 AC5 4 TRP A 50 ? TRP A 50 . ? 1_555 ? 29 AC5 4 NAG E . ? NAG A 366 . ? 1_555 ? 30 AC5 4 HOH I . ? HOH A 407 . ? 1_555 ? 31 AC6 7 ASN A 39 ? ASN A 39 . ? 1_555 ? 32 AC6 7 ILE A 40 ? ILE A 40 . ? 1_555 ? 33 AC6 7 SER A 41 ? SER A 41 . ? 1_555 ? 34 AC6 7 ARG A 84 ? ARG A 84 . ? 1_555 ? 35 AC6 7 NDG H . ? NDG A 369 . ? 1_555 ? 36 AC6 7 HOH I . ? HOH A 412 . ? 1_555 ? 37 AC6 7 HOH I . ? HOH A 434 . ? 1_555 ? 38 AC7 1 NAG G . ? NAG A 368 . ? 1_555 ? # _database_PDB_matrix.entry_id 2B31 _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 2B31 _atom_sites.fract_transf_matrix[1][1] 0.015938 _atom_sites.fract_transf_matrix[1][2] 0.000000 _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] 0.015012 _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] 0.009275 _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 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 . TYR A 1 1 ? 15.343 15.654 58.873 1.00 25.88 ? 1 TYR A N 1 ATOM 2 C CA . TYR A 1 1 ? 14.564 14.987 57.812 1.00 24.67 ? 1 TYR A CA 1 ATOM 3 C C . TYR A 1 1 ? 15.348 13.859 57.229 1.00 22.94 ? 1 TYR A C 1 ATOM 4 O O . TYR A 1 1 ? 16.565 13.928 57.168 1.00 23.68 ? 1 TYR A O 1 ATOM 5 C CB . TYR A 1 1 ? 14.217 15.969 56.737 1.00 26.65 ? 1 TYR A CB 1 ATOM 6 C CG . TYR A 1 1 ? 13.101 16.946 57.150 1.00 32.99 ? 1 TYR A CG 1 ATOM 7 C CD1 . TYR A 1 1 ? 11.839 16.478 57.518 1.00 36.03 ? 1 TYR A CD1 1 ATOM 8 C CD2 . TYR A 1 1 ? 13.314 18.333 57.186 1.00 35.11 ? 1 TYR A CD2 1 ATOM 9 C CE1 . TYR A 1 1 ? 10.834 17.352 57.925 1.00 37.66 ? 1 TYR A CE1 1 ATOM 10 C CE2 . TYR A 1 1 ? 12.307 19.209 57.582 1.00 37.53 ? 1 TYR A CE2 1 ATOM 11 C CZ . TYR A 1 1 ? 11.071 18.710 57.965 1.00 38.72 ? 1 TYR A CZ 1 ATOM 12 O OH . TYR A 1 1 ? 10.048 19.561 58.359 1.00 42.88 ? 1 TYR A OH 1 ATOM 13 N N . LYS A 1 2 ? 14.642 12.772 56.893 1.00 20.14 ? 2 LYS A N 1 ATOM 14 C CA . LYS A 1 2 ? 15.199 11.571 56.270 1.00 16.06 ? 2 LYS A CA 1 ATOM 15 C C . LYS A 1 2 ? 14.966 11.488 54.762 1.00 12.98 ? 2 LYS A C 1 ATOM 16 O O . LYS A 1 2 ? 13.944 11.878 54.252 1.00 12.57 ? 2 LYS A O 1 ATOM 17 C CB . LYS A 1 2 ? 14.574 10.356 56.923 1.00 14.40 ? 2 LYS A CB 1 ATOM 18 C CG . LYS A 1 2 ? 14.886 10.214 58.369 1.00 19.71 ? 2 LYS A CG 1 ATOM 19 C CD . LYS A 1 2 ? 13.860 9.346 59.100 1.00 23.75 ? 2 LYS A CD 1 ATOM 20 C CE . LYS A 1 2 ? 14.447 8.680 60.333 1.00 25.47 ? 2 LYS A CE 1 ATOM 21 N NZ . LYS A 1 2 ? 13.381 8.279 61.271 1.00 30.82 ? 2 LYS A NZ 1 ATOM 22 N N . LEU A 1 3 ? 15.914 10.945 54.054 1.00 11.11 ? 3 LEU A N 1 ATOM 23 C CA . LEU A 1 3 ? 15.815 10.775 52.651 1.00 12.22 ? 3 LEU A CA 1 ATOM 24 C C . LEU A 1 3 ? 16.128 9.318 52.373 1.00 13.29 ? 3 LEU A C 1 ATOM 25 O O . LEU A 1 3 ? 17.298 8.944 52.237 1.00 14.04 ? 3 LEU A O 1 ATOM 26 C CB . LEU A 1 3 ? 16.822 11.691 51.920 1.00 11.69 ? 3 LEU A CB 1 ATOM 27 C CG . LEU A 1 3 ? 16.449 12.180 50.506 1.00 12.46 ? 3 LEU A CG 1 ATOM 28 C CD1 . LEU A 1 3 ? 17.728 12.620 49.774 1.00 12.74 ? 3 LEU A CD1 1 ATOM 29 C CD2 . LEU A 1 3 ? 15.759 11.085 49.698 1.00 11.51 ? 3 LEU A CD2 1 ATOM 30 N N . ILE A 1 4 ? 15.076 8.488 52.309 1.00 13.74 ? 4 ILE A N 1 ATOM 31 C CA . ILE A 1 4 ? 15.234 7.066 52.070 1.00 14.43 ? 4 ILE A CA 1 ATOM 32 C C . ILE A 1 4 ? 15.304 6.781 50.552 1.00 14.61 ? 4 ILE A C 1 ATOM 33 O O . ILE A 1 4 ? 14.421 7.121 49.808 1.00 16.29 ? 4 ILE A O 1 ATOM 34 C CB . ILE A 1 4 ? 14.154 6.290 52.727 1.00 14.07 ? 4 ILE A CB 1 ATOM 35 C CG1 . ILE A 1 4 ? 14.195 6.478 54.220 1.00 16.66 ? 4 ILE A CG1 1 ATOM 36 C CG2 . ILE A 1 4 ? 14.331 4.824 52.410 1.00 18.16 ? 4 ILE A CG2 1 ATOM 37 C CD1 . ILE A 1 4 ? 12.987 5.871 54.964 1.00 23.71 ? 4 ILE A CD1 1 ATOM 38 N N . CYS A 1 5 ? 16.364 6.140 50.101 1.00 13.41 ? 5 CYS A N 1 ATOM 39 C CA . CYS A 1 5 ? 16.495 5.884 48.698 1.00 12.05 ? 5 CYS A CA 1 ATOM 40 C C . CYS A 1 5 ? 16.621 4.415 48.395 1.00 12.81 ? 5 CYS A C 1 ATOM 41 O O . CYS A 1 5 ? 17.530 3.772 48.782 1.00 13.95 ? 5 CYS A O 1 ATOM 42 C CB . CYS A 1 5 ? 17.704 6.618 48.164 1.00 12.41 ? 5 CYS A CB 1 ATOM 43 S SG . CYS A 1 5 ? 17.732 8.413 48.522 1.00 12.33 ? 5 CYS A SG 1 ATOM 44 N N . TYR A 1 6 ? 15.672 3.886 47.647 1.00 14.47 ? 6 TYR A N 1 ATOM 45 C CA . TYR A 1 6 ? 15.629 2.481 47.233 1.00 12.53 ? 6 TYR A CA 1 ATOM 46 C C . TYR A 1 6 ? 16.579 2.269 46.058 1.00 11.81 ? 6 TYR A C 1 ATOM 47 O O . TYR A 1 6 ? 16.697 3.085 45.172 1.00 13.42 ? 6 TYR A O 1 ATOM 48 C CB . TYR A 1 6 ? 14.165 2.057 46.860 1.00 10.87 ? 6 TYR A CB 1 ATOM 49 C CG . TYR A 1 6 ? 13.277 1.574 48.029 1.00 12.63 ? 6 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 6 ? 12.381 2.434 48.651 1.00 16.51 ? 6 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 6 ? 13.353 0.277 48.502 1.00 8.03 ? 6 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 6 ? 11.591 1.990 49.710 1.00 18.79 ? 6 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 6 ? 12.610 -0.143 49.528 1.00 11.00 ? 6 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 6 ? 11.716 0.706 50.135 1.00 17.29 ? 6 TYR A CZ 1 ATOM 55 O OH . TYR A 1 6 ? 10.899 0.269 51.169 1.00 21.75 ? 6 TYR A OH 1 ATOM 56 N N . TYR A 1 7 ? 17.294 1.180 46.070 1.00 11.73 ? 7 TYR A N 1 ATOM 57 C CA . TYR A 1 7 ? 18.183 0.817 44.992 1.00 12.02 ? 7 TYR A CA 1 ATOM 58 C C . TYR A 1 7 ? 17.807 -0.603 44.540 1.00 11.31 ? 7 TYR A C 1 ATOM 59 O O . TYR A 1 7 ? 17.660 -1.465 45.324 1.00 9.41 ? 7 TYR A O 1 ATOM 60 C CB . TYR A 1 7 ? 19.632 0.832 45.472 1.00 13.73 ? 7 TYR A CB 1 ATOM 61 C CG . TYR A 1 7 ? 20.543 0.164 44.478 1.00 14.43 ? 7 TYR A CG 1 ATOM 62 C CD1 . TYR A 1 7 ? 21.013 0.827 43.415 1.00 16.71 ? 7 TYR A CD1 1 ATOM 63 C CD2 . TYR A 1 7 ? 20.844 -1.159 44.580 1.00 17.93 ? 7 TYR A CD2 1 ATOM 64 C CE1 . TYR A 1 7 ? 21.778 0.209 42.464 1.00 19.59 ? 7 TYR A CE1 1 ATOM 65 C CE2 . TYR A 1 7 ? 21.609 -1.788 43.647 1.00 19.51 ? 7 TYR A CE2 1 ATOM 66 C CZ . TYR A 1 7 ? 22.068 -1.103 42.579 1.00 20.50 ? 7 TYR A CZ 1 ATOM 67 O OH . TYR A 1 7 ? 22.825 -1.755 41.600 1.00 21.76 ? 7 TYR A OH 1 ATOM 68 N N . THR A 1 8 ? 17.684 -0.854 43.257 1.00 12.69 ? 8 THR A N 1 ATOM 69 C CA . THR A 1 8 ? 17.289 -2.181 42.815 1.00 12.05 ? 8 THR A CA 1 ATOM 70 C C . THR A 1 8 ? 18.350 -3.080 42.255 1.00 14.51 ? 8 THR A C 1 ATOM 71 O O . THR A 1 8 ? 19.171 -2.722 41.431 1.00 12.76 ? 8 THR A O 1 ATOM 72 C CB . THR A 1 8 ? 16.149 -2.125 41.811 1.00 11.01 ? 8 THR A CB 1 ATOM 73 O OG1 . THR A 1 8 ? 16.560 -1.421 40.623 1.00 7.71 ? 8 THR A OG1 1 ATOM 74 C CG2 . THR A 1 8 ? 14.992 -1.416 42.467 1.00 7.95 ? 8 THR A CG2 1 ATOM 75 N N . SER A 1 9 ? 18.231 -4.308 42.723 1.00 18.07 ? 9 SER A N 1 ATOM 76 C CA . SER A 1 9 ? 19.112 -5.449 42.409 1.00 19.96 ? 9 SER A CA 1 ATOM 77 C C . SER A 1 9 ? 19.357 -5.673 40.932 1.00 20.02 ? 9 SER A C 1 ATOM 78 O O . SER A 1 9 ? 20.490 -5.826 40.508 1.00 19.37 ? 9 SER A O 1 ATOM 79 C CB . SER A 1 9 ? 18.475 -6.711 42.991 1.00 21.34 ? 9 SER A CB 1 ATOM 80 O OG . SER A 1 9 ? 19.387 -7.767 43.138 1.00 26.24 ? 9 SER A OG 1 ATOM 81 N N . TRP A 1 10 ? 18.285 -5.671 40.150 1.00 20.44 ? 10 TRP A N 1 ATOM 82 C CA . TRP A 1 10 ? 18.341 -5.927 38.711 1.00 18.81 ? 10 TRP A CA 1 ATOM 83 C C . TRP A 1 10 ? 18.711 -4.784 37.812 1.00 18.74 ? 10 TRP A C 1 ATOM 84 O O . TRP A 1 10 ? 18.646 -4.913 36.625 1.00 20.64 ? 10 TRP A O 1 ATOM 85 C CB . TRP A 1 10 ? 16.988 -6.493 38.246 1.00 18.30 ? 10 TRP A CB 1 ATOM 86 C CG . TRP A 1 10 ? 15.872 -5.522 38.445 1.00 16.22 ? 10 TRP A CG 1 ATOM 87 C CD1 . TRP A 1 10 ? 15.423 -4.628 37.568 1.00 15.98 ? 10 TRP A CD1 1 ATOM 88 C CD2 . TRP A 1 10 ? 15.122 -5.317 39.651 1.00 16.70 ? 10 TRP A CD2 1 ATOM 89 N NE1 . TRP A 1 10 ? 14.423 -3.867 38.129 1.00 17.48 ? 10 TRP A NE1 1 ATOM 90 C CE2 . TRP A 1 10 ? 14.237 -4.263 39.419 1.00 15.38 ? 10 TRP A CE2 1 ATOM 91 C CE3 . TRP A 1 10 ? 15.141 -5.904 40.920 1.00 14.25 ? 10 TRP A CE3 1 ATOM 92 C CZ2 . TRP A 1 10 ? 13.363 -3.796 40.377 1.00 15.26 ? 10 TRP A CZ2 1 ATOM 93 C CZ3 . TRP A 1 10 ? 14.281 -5.432 41.873 1.00 14.42 ? 10 TRP A CZ3 1 ATOM 94 C CH2 . TRP A 1 10 ? 13.395 -4.393 41.603 1.00 14.10 ? 10 TRP A CH2 1 ATOM 95 N N . SER A 1 11 ? 19.132 -3.662 38.330 1.00 19.45 ? 11 SER A N 1 ATOM 96 C CA . SER A 1 11 ? 19.495 -2.552 37.443 1.00 20.23 ? 11 SER A CA 1 ATOM 97 C C . SER A 1 11 ? 20.891 -2.744 36.914 1.00 20.41 ? 11 SER A C 1 ATOM 98 O O . SER A 1 11 ? 21.360 -1.948 36.079 1.00 22.66 ? 11 SER A O 1 ATOM 99 C CB . SER A 1 11 ? 19.367 -1.208 38.167 1.00 20.06 ? 11 SER A CB 1 ATOM 100 O OG . SER A 1 11 ? 20.182 -1.163 39.288 1.00 22.71 ? 11 SER A OG 1 ATOM 101 N N . GLN A 1 12 ? 21.551 -3.810 37.367 1.00 19.63 ? 12 GLN A N 1 ATOM 102 C CA . GLN A 1 12 ? 22.920 -4.105 36.915 1.00 18.90 ? 12 GLN A CA 1 ATOM 103 C C . GLN A 1 12 ? 22.920 -4.690 35.535 1.00 18.90 ? 12 GLN A C 1 ATOM 104 O O . GLN A 1 12 ? 23.844 -4.486 34.792 1.00 17.81 ? 12 GLN A O 1 ATOM 105 C CB . GLN A 1 12 ? 23.605 -5.068 37.839 1.00 17.35 ? 12 GLN A CB 1 ATOM 106 C CG . GLN A 1 12 ? 22.823 -6.366 38.014 1.00 19.61 ? 12 GLN A CG 1 ATOM 107 C CD . GLN A 1 12 ? 23.621 -7.435 38.758 1.00 21.30 ? 12 GLN A CD 1 ATOM 108 O OE1 . GLN A 1 12 ? 24.637 -7.894 38.246 1.00 24.13 ? 12 GLN A OE1 1 ATOM 109 N NE2 . GLN A 1 12 ? 23.195 -7.788 39.985 1.00 19.26 ? 12 GLN A NE2 1 ATOM 110 N N . TYR A 1 13 ? 21.850 -5.404 35.197 1.00 19.83 ? 13 TYR A N 1 ATOM 111 C CA . TYR A 1 13 ? 21.756 -6.101 33.929 1.00 20.85 ? 13 TYR A CA 1 ATOM 112 C C . TYR A 1 13 ? 21.379 -5.259 32.744 1.00 23.56 ? 13 TYR A C 1 ATOM 113 O O . TYR A 1 13 ? 21.294 -5.753 31.649 1.00 25.09 ? 13 TYR A O 1 ATOM 114 C CB . TYR A 1 13 ? 20.756 -7.245 34.054 1.00 20.41 ? 13 TYR A CB 1 ATOM 115 C CG . TYR A 1 13 ? 21.036 -8.241 35.145 1.00 18.54 ? 13 TYR A CG 1 ATOM 116 C CD1 . TYR A 1 13 ? 22.191 -9.003 35.144 1.00 18.65 ? 13 TYR A CD1 1 ATOM 117 C CD2 . TYR A 1 13 ? 20.147 -8.420 36.174 1.00 17.67 ? 13 TYR A CD2 1 ATOM 118 C CE1 . TYR A 1 13 ? 22.453 -9.943 36.131 1.00 21.81 ? 13 TYR A CE1 1 ATOM 119 C CE2 . TYR A 1 13 ? 20.386 -9.349 37.177 1.00 23.17 ? 13 TYR A CE2 1 ATOM 120 C CZ . TYR A 1 13 ? 21.546 -10.128 37.176 1.00 24.30 ? 13 TYR A CZ 1 ATOM 121 O OH . TYR A 1 13 ? 21.745 -11.084 38.227 1.00 21.62 ? 13 TYR A OH 1 ATOM 122 N N . ARG A 1 14 ? 21.122 -3.982 32.933 1.00 26.98 ? 14 ARG A N 1 ATOM 123 C CA . ARG A 1 14 ? 20.741 -3.123 31.803 1.00 28.60 ? 14 ARG A CA 1 ATOM 124 C C . ARG A 1 14 ? 21.927 -2.807 30.916 1.00 30.55 ? 14 ARG A C 1 ATOM 125 O O . ARG A 1 14 ? 23.054 -2.726 31.373 1.00 31.13 ? 14 ARG A O 1 ATOM 126 C CB . ARG A 1 14 ? 20.119 -1.842 32.343 1.00 28.29 ? 14 ARG A CB 1 ATOM 127 C CG . ARG A 1 14 ? 18.797 -2.134 33.074 1.00 26.88 ? 14 ARG A CG 1 ATOM 128 C CD . ARG A 1 14 ? 18.212 -0.971 33.811 1.00 23.87 ? 14 ARG A CD 1 ATOM 129 N NE . ARG A 1 14 ? 17.061 -1.386 34.597 1.00 22.59 ? 14 ARG A NE 1 ATOM 130 C CZ . ARG A 1 14 ? 16.580 -0.705 35.613 1.00 20.21 ? 14 ARG A CZ 1 ATOM 131 N NH1 . ARG A 1 14 ? 17.144 0.457 35.950 1.00 26.09 ? 14 ARG A NH1 1 ATOM 132 N NH2 . ARG A 1 14 ? 15.554 -1.168 36.288 1.00 12.88 ? 14 ARG A NH2 1 ATOM 133 N N . GLU A 1 15 ? 21.682 -2.652 29.634 1.00 33.44 ? 15 GLU A N 1 ATOM 134 C CA . GLU A 1 15 ? 22.772 -2.382 28.694 1.00 36.59 ? 15 GLU A CA 1 ATOM 135 C C . GLU A 1 15 ? 23.234 -0.930 28.631 1.00 35.02 ? 15 GLU A C 1 ATOM 136 O O . GLU A 1 15 ? 22.522 0.013 28.894 1.00 34.53 ? 15 GLU A O 1 ATOM 137 C CB . GLU A 1 15 ? 22.425 -2.863 27.286 1.00 39.37 ? 15 GLU A CB 1 ATOM 138 C CG . GLU A 1 15 ? 21.220 -2.198 26.656 1.00 47.70 ? 15 GLU A CG 1 ATOM 139 C CD . GLU A 1 15 ? 21.035 -2.578 25.185 1.00 56.02 ? 15 GLU A CD 1 ATOM 140 O OE1 . GLU A 1 15 ? 20.958 -3.820 24.867 1.00 56.83 ? 15 GLU A OE1 1 ATOM 141 O OE2 . GLU A 1 15 ? 20.968 -1.586 24.370 1.00 61.31 ? 15 GLU A OE2 1 ATOM 142 N N . GLY A 1 16 ? 24.478 -0.778 28.259 1.00 34.29 ? 16 GLY A N 1 ATOM 143 C CA . GLY A 1 16 ? 25.044 0.543 28.157 1.00 33.31 ? 16 GLY A CA 1 ATOM 144 C C . GLY A 1 16 ? 25.006 1.253 29.476 1.00 32.02 ? 16 GLY A C 1 ATOM 145 O O . GLY A 1 16 ? 25.225 0.642 30.503 1.00 29.34 ? 16 GLY A O 1 ATOM 146 N N . ASP A 1 17 ? 24.711 2.557 29.414 1.00 33.12 ? 17 ASP A N 1 ATOM 147 C CA . ASP A 1 17 ? 24.638 3.430 30.588 1.00 33.09 ? 17 ASP A CA 1 ATOM 148 C C . ASP A 1 17 ? 23.504 3.015 31.501 1.00 30.78 ? 17 ASP A C 1 ATOM 149 O O . ASP A 1 17 ? 23.500 3.309 32.654 1.00 29.87 ? 17 ASP A O 1 ATOM 150 C CB . ASP A 1 17 ? 24.433 4.866 30.156 1.00 34.91 ? 17 ASP A CB 1 ATOM 151 C CG . ASP A 1 17 ? 25.571 5.384 29.263 1.00 40.03 ? 17 ASP A CG 1 ATOM 152 O OD1 . ASP A 1 17 ? 26.760 5.431 29.720 1.00 43.06 ? 17 ASP A OD1 1 ATOM 153 O OD2 . ASP A 1 17 ? 25.311 5.781 28.092 1.00 45.91 ? 17 ASP A OD2 1 ATOM 154 N N . GLY A 1 18 ? 22.536 2.325 30.957 1.00 29.09 ? 18 GLY A N 1 ATOM 155 C CA . GLY A 1 18 ? 21.436 1.871 31.755 1.00 28.41 ? 18 GLY A CA 1 ATOM 156 C C . GLY A 1 18 ? 21.894 1.050 32.922 1.00 28.30 ? 18 GLY A C 1 ATOM 157 O O . GLY A 1 18 ? 21.259 1.071 33.978 1.00 31.09 ? 18 GLY A O 1 ATOM 158 N N . SER A 1 19 ? 22.990 0.321 32.756 1.00 27.61 ? 19 SER A N 1 ATOM 159 C CA . SER A 1 19 ? 23.551 -0.529 33.826 1.00 25.99 ? 19 SER A CA 1 ATOM 160 C C . SER A 1 19 ? 23.874 0.323 35.049 1.00 25.39 ? 19 SER A C 1 ATOM 161 O O . SER A 1 19 ? 24.398 1.433 34.910 1.00 24.25 ? 19 SER A O 1 ATOM 162 C CB . SER A 1 19 ? 24.836 -1.221 33.322 1.00 25.74 ? 19 SER A CB 1 ATOM 163 O OG . SER A 1 19 ? 25.415 -2.065 34.303 1.00 22.21 ? 19 SER A OG 1 ATOM 164 N N . CYS A 1 20 ? 23.576 -0.212 36.233 1.00 23.96 ? 20 CYS A N 1 ATOM 165 C CA . CYS A 1 20 ? 23.845 0.494 37.465 1.00 24.30 ? 20 CYS A CA 1 ATOM 166 C C . CYS A 1 20 ? 24.291 -0.405 38.618 1.00 22.86 ? 20 CYS A C 1 ATOM 167 O O . CYS A 1 20 ? 23.634 -1.371 38.937 1.00 22.91 ? 20 CYS A O 1 ATOM 168 C CB . CYS A 1 20 ? 22.603 1.274 37.878 1.00 25.53 ? 20 CYS A CB 1 ATOM 169 S SG . CYS A 1 20 ? 22.893 2.487 39.228 1.00 32.08 ? 20 CYS A SG 1 ATOM 170 N N . PHE A 1 21 ? 25.402 -0.062 39.241 1.00 22.19 ? 21 PHE A N 1 ATOM 171 C CA . PHE A 1 21 ? 25.922 -0.797 40.390 1.00 23.03 ? 21 PHE A CA 1 ATOM 172 C C . PHE A 1 21 ? 26.033 0.138 41.581 1.00 23.13 ? 21 PHE A C 1 ATOM 173 O O . PHE A 1 21 ? 26.243 1.341 41.384 1.00 25.23 ? 21 PHE A O 1 ATOM 174 C CB . PHE A 1 21 ? 27.302 -1.388 40.095 1.00 23.57 ? 21 PHE A CB 1 ATOM 175 C CG . PHE A 1 21 ? 27.274 -2.547 39.123 1.00 23.72 ? 21 PHE A CG 1 ATOM 176 C CD1 . PHE A 1 21 ? 27.129 -2.337 37.796 1.00 24.60 ? 21 PHE A CD1 1 ATOM 177 C CD2 . PHE A 1 21 ? 27.368 -3.837 39.572 1.00 26.84 ? 21 PHE A CD2 1 ATOM 178 C CE1 . PHE A 1 21 ? 27.092 -3.374 36.919 1.00 25.87 ? 21 PHE A CE1 1 ATOM 179 C CE2 . PHE A 1 21 ? 27.321 -4.884 38.711 1.00 27.95 ? 21 PHE A CE2 1 ATOM 180 C CZ . PHE A 1 21 ? 27.184 -4.652 37.377 1.00 27.56 ? 21 PHE A CZ 1 ATOM 181 N N . PRO A 1 22 ? 25.936 -0.387 42.803 1.00 21.92 ? 22 PRO A N 1 ATOM 182 C CA . PRO A 1 22 ? 26.007 0.389 44.055 1.00 22.24 ? 22 PRO A CA 1 ATOM 183 C C . PRO A 1 22 ? 27.078 1.430 43.959 1.00 22.63 ? 22 PRO A C 1 ATOM 184 O O . PRO A 1 22 ? 27.024 2.466 44.563 1.00 21.55 ? 22 PRO A O 1 ATOM 185 C CB . PRO A 1 22 ? 26.357 -0.666 45.094 1.00 21.88 ? 22 PRO A CB 1 ATOM 186 C CG . PRO A 1 22 ? 25.665 -1.840 44.577 1.00 23.37 ? 22 PRO A CG 1 ATOM 187 C CD . PRO A 1 22 ? 25.846 -1.811 43.065 1.00 21.25 ? 22 PRO A CD 1 ATOM 188 N N . ASP A 1 23 ? 28.085 1.075 43.202 1.00 26.35 ? 23 ASP A N 1 ATOM 189 C CA . ASP A 1 23 ? 29.241 1.914 42.857 1.00 29.53 ? 23 ASP A CA 1 ATOM 190 C C . ASP A 1 23 ? 28.871 3.393 42.515 1.00 29.27 ? 23 ASP A C 1 ATOM 191 O O . ASP A 1 23 ? 29.489 4.326 43.027 1.00 30.00 ? 23 ASP A O 1 ATOM 192 C CB . ASP A 1 23 ? 29.877 1.283 41.621 1.00 32.00 ? 23 ASP A CB 1 ATOM 193 C CG . ASP A 1 23 ? 31.267 1.020 41.798 1.00 36.63 ? 23 ASP A CG 1 ATOM 194 O OD1 . ASP A 1 23 ? 31.655 0.858 42.975 1.00 41.32 ? 23 ASP A OD1 1 ATOM 195 O OD2 . ASP A 1 23 ? 32.024 0.987 40.784 1.00 44.82 ? 23 ASP A OD2 1 ATOM 196 N N . ALA A 1 24 ? 27.867 3.588 41.658 1.00 26.58 ? 24 ALA A N 1 ATOM 197 C CA . ALA A 1 24 ? 27.462 4.912 41.243 1.00 26.40 ? 24 ALA A CA 1 ATOM 198 C C . ALA A 1 24 ? 26.684 5.777 42.246 1.00 25.50 ? 24 ALA A C 1 ATOM 199 O O . ALA A 1 24 ? 26.271 6.880 41.902 1.00 26.53 ? 24 ALA A O 1 ATOM 200 C CB . ALA A 1 24 ? 26.633 4.798 39.956 1.00 27.59 ? 24 ALA A CB 1 ATOM 201 N N . ILE A 1 25 ? 26.475 5.318 43.464 1.00 23.33 ? 25 ILE A N 1 ATOM 202 C CA . ILE A 1 25 ? 25.680 6.064 44.427 1.00 21.14 ? 25 ILE A CA 1 ATOM 203 C C . ILE A 1 25 ? 26.509 7.042 45.210 1.00 19.72 ? 25 ILE A C 1 ATOM 204 O O . ILE A 1 25 ? 27.541 6.697 45.728 1.00 20.52 ? 25 ILE A O 1 ATOM 205 C CB . ILE A 1 25 ? 24.969 5.106 45.382 1.00 21.72 ? 25 ILE A CB 1 ATOM 206 C CG1 . ILE A 1 25 ? 24.020 4.181 44.594 1.00 23.78 ? 25 ILE A CG1 1 ATOM 207 C CG2 . ILE A 1 25 ? 24.201 5.868 46.400 1.00 22.79 ? 25 ILE A CG2 1 ATOM 208 C CD1 . ILE A 1 25 ? 23.401 3.055 45.416 1.00 21.61 ? 25 ILE A CD1 1 ATOM 209 N N . ASP A 1 26 ? 26.040 8.289 45.307 1.00 18.49 ? 26 ASP A N 1 ATOM 210 C CA . ASP A 1 26 ? 26.722 9.295 46.106 1.00 18.51 ? 26 ASP A CA 1 ATOM 211 C C . ASP A 1 26 ? 26.399 8.993 47.540 1.00 17.77 ? 26 ASP A C 1 ATOM 212 O O . ASP A 1 26 ? 25.263 9.144 47.973 1.00 19.61 ? 26 ASP A O 1 ATOM 213 C CB . ASP A 1 26 ? 26.241 10.715 45.752 1.00 20.48 ? 26 ASP A CB 1 ATOM 214 C CG . ASP A 1 26 ? 26.705 11.771 46.766 1.00 21.88 ? 26 ASP A CG 1 ATOM 215 O OD1 . ASP A 1 26 ? 27.762 11.596 47.417 1.00 23.84 ? 26 ASP A OD1 1 ATOM 216 O OD2 . ASP A 1 26 ? 26.042 12.785 46.939 1.00 22.68 ? 26 ASP A OD2 1 ATOM 217 N N . PRO A 1 27 ? 27.379 8.581 48.312 1.00 15.36 ? 27 PRO A N 1 ATOM 218 C CA . PRO A 1 27 ? 27.166 8.257 49.723 1.00 14.07 ? 27 PRO A CA 1 ATOM 219 C C . PRO A 1 27 ? 26.706 9.420 50.559 1.00 13.52 ? 27 PRO A C 1 ATOM 220 O O . PRO A 1 27 ? 25.987 9.206 51.505 1.00 15.24 ? 27 PRO A O 1 ATOM 221 C CB . PRO A 1 27 ? 28.534 7.768 50.176 1.00 13.51 ? 27 PRO A CB 1 ATOM 222 C CG . PRO A 1 27 ? 29.460 8.506 49.332 1.00 14.47 ? 27 PRO A CG 1 ATOM 223 C CD . PRO A 1 27 ? 28.786 8.459 47.962 1.00 15.35 ? 27 PRO A CD 1 ATOM 224 N N . PHE A 1 28 ? 27.056 10.650 50.204 1.00 12.53 ? 28 PHE A N 1 ATOM 225 C CA . PHE A 1 28 ? 26.635 11.764 51.020 1.00 11.88 ? 28 PHE A CA 1 ATOM 226 C C . PHE A 1 28 ? 25.224 12.245 50.642 1.00 10.61 ? 28 PHE A C 1 ATOM 227 O O . PHE A 1 28 ? 24.642 13.078 51.280 1.00 10.89 ? 28 PHE A O 1 ATOM 228 C CB . PHE A 1 28 ? 27.712 12.865 51.013 1.00 11.63 ? 28 PHE A CB 1 ATOM 229 C CG . PHE A 1 28 ? 28.876 12.527 51.831 1.00 12.60 ? 28 PHE A CG 1 ATOM 230 C CD1 . PHE A 1 28 ? 28.785 12.563 53.198 1.00 18.67 ? 28 PHE A CD1 1 ATOM 231 C CD2 . PHE A 1 28 ? 30.048 12.083 51.246 1.00 15.67 ? 28 PHE A CD2 1 ATOM 232 C CE1 . PHE A 1 28 ? 29.878 12.177 53.995 1.00 22.79 ? 28 PHE A CE1 1 ATOM 233 C CE2 . PHE A 1 28 ? 31.119 11.702 52.000 1.00 16.71 ? 28 PHE A CE2 1 ATOM 234 C CZ . PHE A 1 28 ? 31.037 11.733 53.387 1.00 21.66 ? 28 PHE A CZ 1 ATOM 235 N N . LEU A 1 29 ? 24.657 11.647 49.634 1.00 10.02 ? 29 LEU A N 1 ATOM 236 C CA . LEU A 1 29 ? 23.318 12.029 49.181 1.00 10.13 ? 29 LEU A CA 1 ATOM 237 C C . LEU A 1 29 ? 22.165 11.691 50.126 1.00 9.87 ? 29 LEU A C 1 ATOM 238 O O . LEU A 1 29 ? 21.680 12.573 50.803 1.00 12.23 ? 29 LEU A O 1 ATOM 239 C CB . LEU A 1 29 ? 23.039 11.381 47.858 1.00 9.67 ? 29 LEU A CB 1 ATOM 240 C CG . LEU A 1 29 ? 21.685 11.616 47.239 1.00 11.56 ? 29 LEU A CG 1 ATOM 241 C CD1 . LEU A 1 29 ? 21.331 13.065 47.255 1.00 11.73 ? 29 LEU A CD1 1 ATOM 242 C CD2 . LEU A 1 29 ? 21.767 11.099 45.756 1.00 8.16 ? 29 LEU A CD2 1 ATOM 243 N N . CYS A 1 30 ? 21.721 10.442 50.167 1.00 9.76 ? 30 CYS A N 1 ATOM 244 C CA . CYS A 1 30 ? 20.658 10.020 51.063 1.00 10.48 ? 30 CYS A CA 1 ATOM 245 C C . CYS A 1 30 ? 21.120 9.649 52.497 1.00 9.25 ? 30 CYS A C 1 ATOM 246 O O . CYS A 1 30 ? 22.308 9.466 52.729 1.00 9.67 ? 30 CYS A O 1 ATOM 247 C CB . CYS A 1 30 ? 19.939 8.812 50.451 1.00 10.90 ? 30 CYS A CB 1 ATOM 248 S SG . CYS A 1 30 ? 19.647 8.860 48.685 1.00 9.58 ? 30 CYS A SG 1 ATOM 249 N N . THR A 1 31 ? 20.177 9.583 53.437 1.00 8.53 ? 31 THR A N 1 ATOM 250 C CA . THR A 1 31 ? 20.462 9.180 54.819 1.00 10.21 ? 31 THR A CA 1 ATOM 251 C C . THR A 1 31 ? 20.405 7.658 54.920 1.00 9.97 ? 31 THR A C 1 ATOM 252 O O . THR A 1 31 ? 21.157 7.036 55.596 1.00 7.76 ? 31 THR A O 1 ATOM 253 C CB . THR A 1 31 ? 19.456 9.768 55.883 1.00 10.55 ? 31 THR A CB 1 ATOM 254 O OG1 . THR A 1 31 ? 18.126 9.562 55.456 1.00 11.23 ? 31 THR A OG1 1 ATOM 255 C CG2 . THR A 1 31 ? 19.653 11.248 56.072 1.00 13.99 ? 31 THR A CG2 1 ATOM 256 N N . HIS A 1 32 ? 19.403 7.075 54.272 1.00 10.70 ? 32 HIS A N 1 ATOM 257 C CA . HIS A 1 32 ? 19.183 5.639 54.286 1.00 9.65 ? 32 HIS A CA 1 ATOM 258 C C . HIS A 1 32 ? 18.996 5.107 52.879 1.00 9.10 ? 32 HIS A C 1 ATOM 259 O O . HIS A 1 32 ? 18.190 5.620 52.091 1.00 8.67 ? 32 HIS A O 1 ATOM 260 C CB . HIS A 1 32 ? 17.893 5.282 55.058 1.00 10.78 ? 32 HIS A CB 1 ATOM 261 C CG . HIS A 1 32 ? 17.829 5.776 56.464 1.00 7.99 ? 32 HIS A CG 1 ATOM 262 N ND1 . HIS A 1 32 ? 17.638 7.097 56.767 1.00 7.37 ? 32 HIS A ND1 1 ATOM 263 C CD2 . HIS A 1 32 ? 17.840 5.115 57.628 1.00 7.49 ? 32 HIS A CD2 1 ATOM 264 C CE1 . HIS A 1 32 ? 17.524 7.226 58.066 1.00 6.26 ? 32 HIS A CE1 1 ATOM 265 N NE2 . HIS A 1 32 ? 17.667 6.037 58.614 1.00 7.73 ? 32 HIS A NE2 1 ATOM 266 N N . VAL A 1 33 ? 19.726 4.035 52.601 1.00 8.57 ? 33 VAL A N 1 ATOM 267 C CA . VAL A 1 33 ? 19.672 3.355 51.320 1.00 7.39 ? 33 VAL A CA 1 ATOM 268 C C . VAL A 1 33 ? 19.148 1.968 51.548 1.00 7.10 ? 33 VAL A C 1 ATOM 269 O O . VAL A 1 33 ? 19.727 1.256 52.249 1.00 6.65 ? 33 VAL A O 1 ATOM 270 C CB . VAL A 1 33 ? 21.030 3.306 50.627 1.00 3.71 ? 33 VAL A CB 1 ATOM 271 C CG1 . VAL A 1 33 ? 20.892 2.566 49.359 1.00 4.29 ? 33 VAL A CG1 1 ATOM 272 C CG2 . VAL A 1 33 ? 21.442 4.707 50.271 1.00 5.21 ? 33 VAL A CG2 1 ATOM 273 N N . ILE A 1 34 ? 18.017 1.611 50.928 1.00 9.68 ? 34 ILE A N 1 ATOM 274 C CA . ILE A 1 34 ? 17.375 0.303 51.070 1.00 10.61 ? 34 ILE A CA 1 ATOM 275 C C . ILE A 1 34 ? 17.631 -0.529 49.834 1.00 10.12 ? 34 ILE A C 1 ATOM 276 O O . ILE A 1 34 ? 17.112 -0.258 48.801 1.00 11.57 ? 34 ILE A O 1 ATOM 277 C CB . ILE A 1 34 ? 15.882 0.405 51.352 1.00 11.07 ? 34 ILE A CB 1 ATOM 278 C CG1 . ILE A 1 34 ? 15.663 1.169 52.671 1.00 16.42 ? 34 ILE A CG1 1 ATOM 279 C CG2 . ILE A 1 34 ? 15.280 -0.951 51.435 1.00 10.77 ? 34 ILE A CG2 1 ATOM 280 C CD1 . ILE A 1 34 ? 14.190 1.520 52.943 1.00 22.41 ? 34 ILE A CD1 1 ATOM 281 N N . TYR A 1 35 ? 18.452 -1.559 49.976 1.00 11.07 ? 35 TYR A N 1 ATOM 282 C CA . TYR A 1 35 ? 18.803 -2.499 48.911 1.00 10.55 ? 35 TYR A CA 1 ATOM 283 C C . TYR A 1 35 ? 17.590 -3.356 48.514 1.00 10.34 ? 35 TYR A C 1 ATOM 284 O O . TYR A 1 35 ? 16.874 -3.871 49.352 1.00 8.08 ? 35 TYR A O 1 ATOM 285 C CB . TYR A 1 35 ? 19.933 -3.405 49.379 1.00 11.51 ? 35 TYR A CB 1 ATOM 286 C CG . TYR A 1 35 ? 20.415 -4.339 48.299 1.00 11.41 ? 35 TYR A CG 1 ATOM 287 C CD1 . TYR A 1 35 ? 21.463 -3.990 47.497 1.00 10.29 ? 35 TYR A CD1 1 ATOM 288 C CD2 . TYR A 1 35 ? 19.833 -5.566 48.101 1.00 9.58 ? 35 TYR A CD2 1 ATOM 289 C CE1 . TYR A 1 35 ? 21.899 -4.825 46.506 1.00 11.90 ? 35 TYR A CE1 1 ATOM 290 C CE2 . TYR A 1 35 ? 20.286 -6.414 47.128 1.00 4.07 ? 35 TYR A CE2 1 ATOM 291 C CZ . TYR A 1 35 ? 21.309 -6.058 46.323 1.00 9.00 ? 35 TYR A CZ 1 ATOM 292 O OH . TYR A 1 35 ? 21.788 -6.903 45.331 1.00 5.61 ? 35 TYR A OH 1 ATOM 293 N N . SER A 1 36 ? 17.377 -3.540 47.226 1.00 12.19 ? 36 SER A N 1 ATOM 294 C CA . SER A 1 36 ? 16.121 -4.145 46.820 1.00 11.68 ? 36 SER A CA 1 ATOM 295 C C . SER A 1 36 ? 16.009 -5.588 46.389 1.00 12.29 ? 36 SER A C 1 ATOM 296 O O . SER A 1 36 ? 16.507 -6.046 45.419 1.00 10.54 ? 36 SER A O 1 ATOM 297 C CB . SER A 1 36 ? 15.521 -3.310 45.757 1.00 13.17 ? 36 SER A CB 1 ATOM 298 O OG . SER A 1 36 ? 14.376 -2.660 46.257 1.00 18.34 ? 36 SER A OG 1 ATOM 299 N N . PHE A 1 37 ? 15.213 -6.223 47.263 1.00 15.78 ? 37 PHE A N 1 ATOM 300 C CA . PHE A 1 37 ? 14.665 -7.565 47.380 1.00 12.33 ? 37 PHE A CA 1 ATOM 301 C C . PHE A 1 37 ? 15.574 -8.687 47.671 1.00 12.74 ? 37 PHE A C 1 ATOM 302 O O . PHE A 1 37 ? 16.289 -9.204 46.876 1.00 15.30 ? 37 PHE A O 1 ATOM 303 C CB . PHE A 1 37 ? 13.698 -7.778 46.275 1.00 11.30 ? 37 PHE A CB 1 ATOM 304 C CG . PHE A 1 37 ? 12.738 -6.638 46.259 1.00 11.69 ? 37 PHE A CG 1 ATOM 305 C CD1 . PHE A 1 37 ? 12.349 -6.035 47.440 1.00 11.71 ? 37 PHE A CD1 1 ATOM 306 C CD2 . PHE A 1 37 ? 12.249 -6.108 45.082 1.00 12.78 ? 37 PHE A CD2 1 ATOM 307 C CE1 . PHE A 1 37 ? 11.534 -4.895 47.428 1.00 15.87 ? 37 PHE A CE1 1 ATOM 308 C CE2 . PHE A 1 37 ? 11.448 -4.982 45.077 1.00 12.94 ? 37 PHE A CE2 1 ATOM 309 C CZ . PHE A 1 37 ? 11.088 -4.367 46.256 1.00 12.72 ? 37 PHE A CZ 1 ATOM 310 N N . ALA A 1 38 ? 15.477 -9.024 48.916 1.00 15.21 ? 38 ALA A N 1 ATOM 311 C CA . ALA A 1 38 ? 16.038 -10.223 49.418 1.00 16.98 ? 38 ALA A CA 1 ATOM 312 C C . ALA A 1 38 ? 14.917 -11.229 49.141 1.00 16.61 ? 38 ALA A C 1 ATOM 313 O O . ALA A 1 38 ? 13.873 -10.842 48.633 1.00 15.53 ? 38 ALA A O 1 ATOM 314 C CB . ALA A 1 38 ? 16.369 -10.147 50.911 1.00 16.32 ? 38 ALA A CB 1 ATOM 315 N N . ASN A 1 39 ? 15.122 -12.500 49.481 1.00 16.95 ? 39 ASN A N 1 ATOM 316 C CA . ASN A 1 39 ? 14.063 -13.464 49.220 1.00 16.88 ? 39 ASN A CA 1 ATOM 317 C C . ASN A 1 39 ? 13.844 -14.312 50.431 1.00 18.13 ? 39 ASN A C 1 ATOM 318 O O . ASN A 1 39 ? 14.484 -14.113 51.457 1.00 17.79 ? 39 ASN A O 1 ATOM 319 C CB . ASN A 1 39 ? 14.439 -14.288 47.976 1.00 15.83 ? 39 ASN A CB 1 ATOM 320 C CG . ASN A 1 39 ? 13.397 -15.277 47.455 1.00 20.38 ? 39 ASN A CG 1 ATOM 321 O OD1 . ASN A 1 39 ? 12.193 -15.087 47.602 1.00 29.56 ? 39 ASN A OD1 1 ATOM 322 N ND2 . ASN A 1 39 ? 13.890 -16.359 46.811 1.00 23.70 ? 39 ASN A ND2 1 ATOM 323 N N . ILE A 1 40 ? 12.947 -15.270 50.300 1.00 20.41 ? 40 ILE A N 1 ATOM 324 C CA . ILE A 1 40 ? 12.687 -16.226 51.381 1.00 20.65 ? 40 ILE A CA 1 ATOM 325 C C . ILE A 1 40 ? 12.702 -17.629 50.810 1.00 20.10 ? 40 ILE A C 1 ATOM 326 O O . ILE A 1 40 ? 12.141 -17.853 49.745 1.00 18.55 ? 40 ILE A O 1 ATOM 327 C CB . ILE A 1 40 ? 11.337 -15.938 52.050 1.00 21.47 ? 40 ILE A CB 1 ATOM 328 C CG1 . ILE A 1 40 ? 11.372 -14.566 52.691 1.00 24.25 ? 40 ILE A CG1 1 ATOM 329 C CG2 . ILE A 1 40 ? 11.020 -16.988 53.091 1.00 24.71 ? 40 ILE A CG2 1 ATOM 330 C CD1 . ILE A 1 40 ? 10.003 -14.037 53.072 1.00 26.63 ? 40 ILE A CD1 1 ATOM 331 N N . SER A 1 41 ? 13.356 -18.543 51.516 1.00 21.19 ? 41 SER A N 1 ATOM 332 C CA . SER A 1 41 ? 13.418 -19.935 51.097 1.00 22.88 ? 41 SER A CA 1 ATOM 333 C C . SER A 1 41 ? 13.667 -20.827 52.281 1.00 24.57 ? 41 SER A C 1 ATOM 334 O O . SER A 1 41 ? 14.597 -20.627 53.048 1.00 22.86 ? 41 SER A O 1 ATOM 335 C CB . SER A 1 41 ? 14.486 -20.144 50.084 1.00 22.72 ? 41 SER A CB 1 ATOM 336 O OG . SER A 1 41 ? 15.741 -19.915 50.658 1.00 28.04 ? 41 SER A OG 1 ATOM 337 N N . ASN A 1 42 ? 12.808 -21.828 52.417 1.00 27.58 ? 42 ASN A N 1 ATOM 338 C CA . ASN A 1 42 ? 12.870 -22.741 53.540 1.00 30.06 ? 42 ASN A CA 1 ATOM 339 C C . ASN A 1 42 ? 12.607 -21.945 54.773 1.00 28.28 ? 42 ASN A C 1 ATOM 340 O O . ASN A 1 42 ? 13.075 -22.224 55.850 1.00 30.12 ? 42 ASN A O 1 ATOM 341 C CB . ASN A 1 42 ? 14.224 -23.421 53.604 1.00 33.37 ? 42 ASN A CB 1 ATOM 342 C CG . ASN A 1 42 ? 14.274 -24.658 52.730 1.00 40.13 ? 42 ASN A CG 1 ATOM 343 O OD1 . ASN A 1 42 ? 14.964 -24.677 51.700 1.00 46.12 ? 42 ASN A OD1 1 ATOM 344 N ND2 . ASN A 1 42 ? 13.486 -25.693 53.109 1.00 45.90 ? 42 ASN A ND2 1 ATOM 345 N N . ASN A 1 43 ? 11.826 -20.911 54.587 1.00 27.54 ? 43 ASN A N 1 ATOM 346 C CA . ASN A 1 43 ? 11.382 -20.001 55.645 1.00 25.51 ? 43 ASN A CA 1 ATOM 347 C C . ASN A 1 43 ? 12.394 -19.062 56.261 1.00 22.60 ? 43 ASN A C 1 ATOM 348 O O . ASN A 1 43 ? 12.146 -18.469 57.296 1.00 20.82 ? 43 ASN A O 1 ATOM 349 C CB . ASN A 1 43 ? 10.620 -20.786 56.740 1.00 25.50 ? 43 ASN A CB 1 ATOM 350 C CG . ASN A 1 43 ? 9.257 -21.238 56.280 1.00 23.96 ? 43 ASN A CG 1 ATOM 351 O OD1 . ASN A 1 43 ? 8.778 -20.834 55.221 1.00 25.44 ? 43 ASN A OD1 1 ATOM 352 N ND2 . ASN A 1 43 ? 8.628 -22.070 57.072 1.00 25.97 ? 43 ASN A ND2 1 ATOM 353 N N . GLU A 1 44 ? 13.495 -18.890 55.596 1.00 21.88 ? 44 GLU A N 1 ATOM 354 C CA . GLU A 1 44 ? 14.528 -17.996 56.123 1.00 22.84 ? 44 GLU A CA 1 ATOM 355 C C . GLU A 1 44 ? 14.819 -16.935 55.082 1.00 22.30 ? 44 GLU A C 1 ATOM 356 O O . GLU A 1 44 ? 14.545 -17.142 53.901 1.00 22.56 ? 44 GLU A O 1 ATOM 357 C CB . GLU A 1 44 ? 15.823 -18.756 56.454 1.00 22.09 ? 44 GLU A CB 1 ATOM 358 C CG . GLU A 1 44 ? 15.607 -20.056 57.189 1.00 23.79 ? 44 GLU A CG 1 ATOM 359 C CD . GLU A 1 44 ? 16.888 -20.620 57.757 1.00 27.91 ? 44 GLU A CD 1 ATOM 360 O OE1 . GLU A 1 44 ? 17.917 -20.673 57.044 1.00 28.30 ? 44 GLU A OE1 1 ATOM 361 O OE2 . GLU A 1 44 ? 16.867 -21.040 58.938 1.00 33.65 ? 44 GLU A OE2 1 ATOM 362 N N . ILE A 1 45 ? 15.290 -15.776 55.497 1.00 20.31 ? 45 ILE A N 1 ATOM 363 C CA . ILE A 1 45 ? 15.619 -14.772 54.491 1.00 21.12 ? 45 ILE A CA 1 ATOM 364 C C . ILE A 1 45 ? 16.839 -15.309 53.745 1.00 21.14 ? 45 ILE A C 1 ATOM 365 O O . ILE A 1 45 ? 17.601 -16.086 54.270 1.00 22.55 ? 45 ILE A O 1 ATOM 366 C CB . ILE A 1 45 ? 15.833 -13.355 55.074 1.00 22.02 ? 45 ILE A CB 1 ATOM 367 C CG1 . ILE A 1 45 ? 16.454 -12.427 54.055 1.00 22.55 ? 45 ILE A CG1 1 ATOM 368 C CG2 . ILE A 1 45 ? 16.638 -13.408 56.325 1.00 23.63 ? 45 ILE A CG2 1 ATOM 369 C CD1 . ILE A 1 45 ? 16.765 -11.065 54.592 1.00 22.61 ? 45 ILE A CD1 1 ATOM 370 N N . ASP A 1 46 ? 16.995 -14.896 52.522 1.00 21.36 ? 46 ASP A N 1 ATOM 371 C CA . ASP A 1 46 ? 18.046 -15.426 51.691 1.00 20.30 ? 46 ASP A CA 1 ATOM 372 C C . ASP A 1 46 ? 18.280 -14.463 50.521 1.00 19.69 ? 46 ASP A C 1 ATOM 373 O O . ASP A 1 46 ? 17.550 -13.504 50.333 1.00 19.00 ? 46 ASP A O 1 ATOM 374 C CB . ASP A 1 46 ? 17.634 -16.790 51.198 1.00 19.68 ? 46 ASP A CB 1 ATOM 375 C CG . ASP A 1 46 ? 18.760 -17.554 50.641 1.00 22.25 ? 46 ASP A CG 1 ATOM 376 O OD1 . ASP A 1 46 ? 19.885 -17.463 51.200 1.00 21.31 ? 46 ASP A OD1 1 ATOM 377 O OD2 . ASP A 1 46 ? 18.564 -18.267 49.626 1.00 26.16 ? 46 ASP A OD2 1 ATOM 378 N N . THR A 1 47 ? 19.324 -14.719 49.771 1.00 19.50 ? 47 THR A N 1 ATOM 379 C CA . THR A 1 47 ? 19.699 -13.888 48.629 1.00 20.47 ? 47 THR A CA 1 ATOM 380 C C . THR A 1 47 ? 18.803 -14.078 47.456 1.00 19.29 ? 47 THR A C 1 ATOM 381 O O . THR A 1 47 ? 17.953 -14.921 47.518 1.00 20.19 ? 47 THR A O 1 ATOM 382 C CB . THR A 1 47 ? 21.203 -14.167 48.200 1.00 20.70 ? 47 THR A CB 1 ATOM 383 O OG1 . THR A 1 47 ? 21.473 -15.557 48.308 1.00 25.13 ? 47 THR A OG1 1 ATOM 384 C CG2 . THR A 1 47 ? 22.193 -13.493 49.146 1.00 18.57 ? 47 THR A CG2 1 ATOM 385 N N . TRP A 1 48 ? 18.998 -13.289 46.401 1.00 20.80 ? 48 TRP A N 1 ATOM 386 C CA . TRP A 1 48 ? 18.171 -13.350 45.167 1.00 24.13 ? 48 TRP A CA 1 ATOM 387 C C . TRP A 1 48 ? 18.998 -13.478 43.845 1.00 26.16 ? 48 TRP A C 1 ATOM 388 O O . TRP A 1 48 ? 18.817 -14.379 43.059 1.00 27.74 ? 48 TRP A O 1 ATOM 389 C CB . TRP A 1 48 ? 17.241 -12.131 45.082 1.00 23.82 ? 48 TRP A CB 1 ATOM 390 C CG . TRP A 1 48 ? 16.189 -12.217 44.054 1.00 24.80 ? 48 TRP A CG 1 ATOM 391 C CD1 . TRP A 1 48 ? 16.362 -12.231 42.713 1.00 28.95 ? 48 TRP A CD1 1 ATOM 392 C CD2 . TRP A 1 48 ? 14.782 -12.253 44.269 1.00 28.14 ? 48 TRP A CD2 1 ATOM 393 N NE1 . TRP A 1 48 ? 15.136 -12.277 42.070 1.00 30.58 ? 48 TRP A NE1 1 ATOM 394 C CE2 . TRP A 1 48 ? 14.153 -12.299 43.006 1.00 27.46 ? 48 TRP A CE2 1 ATOM 395 C CE3 . TRP A 1 48 ? 13.982 -12.242 45.406 1.00 31.29 ? 48 TRP A CE3 1 ATOM 396 C CZ2 . TRP A 1 48 ? 12.810 -12.341 42.854 1.00 27.72 ? 48 TRP A CZ2 1 ATOM 397 C CZ3 . TRP A 1 48 ? 12.615 -12.297 45.254 1.00 30.04 ? 48 TRP A CZ3 1 ATOM 398 C CH2 . TRP A 1 48 ? 12.049 -12.350 43.991 1.00 30.92 ? 48 TRP A CH2 1 ATOM 399 N N . GLU A 1 49 ? 19.880 -12.548 43.590 1.00 28.39 ? 49 GLU A N 1 ATOM 400 C CA . GLU A 1 49 ? 20.694 -12.620 42.399 1.00 29.35 ? 49 GLU A CA 1 ATOM 401 C C . GLU A 1 49 ? 21.916 -13.430 42.808 1.00 29.61 ? 49 GLU A C 1 ATOM 402 O O . GLU A 1 49 ? 22.274 -13.465 43.944 1.00 27.57 ? 49 GLU A O 1 ATOM 403 C CB . GLU A 1 49 ? 21.140 -11.198 41.928 1.00 29.93 ? 49 GLU A CB 1 ATOM 404 C CG . GLU A 1 49 ? 20.029 -10.171 41.651 1.00 27.86 ? 49 GLU A CG 1 ATOM 405 C CD . GLU A 1 49 ? 19.215 -10.474 40.421 1.00 25.38 ? 49 GLU A CD 1 ATOM 406 O OE1 . GLU A 1 49 ? 19.731 -11.279 39.606 1.00 24.38 ? 49 GLU A OE1 1 ATOM 407 O OE2 . GLU A 1 49 ? 18.091 -9.893 40.277 1.00 21.71 ? 49 GLU A OE2 1 ATOM 408 N N . TRP A 1 50 ? 22.571 -14.062 41.850 1.00 32.21 ? 50 TRP A N 1 ATOM 409 C CA . TRP A 1 50 ? 23.759 -14.862 42.146 1.00 33.46 ? 50 TRP A CA 1 ATOM 410 C C . TRP A 1 50 ? 24.837 -14.063 42.852 1.00 31.86 ? 50 TRP A C 1 ATOM 411 O O . TRP A 1 50 ? 25.470 -14.558 43.783 1.00 33.14 ? 50 TRP A O 1 ATOM 412 C CB . TRP A 1 50 ? 24.320 -15.506 40.865 1.00 35.14 ? 50 TRP A CB 1 ATOM 413 C CG . TRP A 1 50 ? 24.846 -14.578 39.820 1.00 39.91 ? 50 TRP A CG 1 ATOM 414 C CD1 . TRP A 1 50 ? 24.130 -13.837 38.940 1.00 45.38 ? 50 TRP A CD1 1 ATOM 415 C CD2 . TRP A 1 50 ? 26.221 -14.331 39.512 1.00 46.54 ? 50 TRP A CD2 1 ATOM 416 N NE1 . TRP A 1 50 ? 24.962 -13.122 38.099 1.00 46.04 ? 50 TRP A NE1 1 ATOM 417 C CE2 . TRP A 1 50 ? 26.255 -13.407 38.440 1.00 47.04 ? 50 TRP A CE2 1 ATOM 418 C CE3 . TRP A 1 50 ? 27.441 -14.791 40.043 1.00 48.92 ? 50 TRP A CE3 1 ATOM 419 C CZ2 . TRP A 1 50 ? 27.444 -12.935 37.905 1.00 49.60 ? 50 TRP A CZ2 1 ATOM 420 C CZ3 . TRP A 1 50 ? 28.618 -14.328 39.492 1.00 49.72 ? 50 TRP A CZ3 1 ATOM 421 C CH2 . TRP A 1 50 ? 28.614 -13.411 38.437 1.00 49.75 ? 50 TRP A CH2 1 ATOM 422 N N . ASN A 1 51 ? 25.028 -12.818 42.427 1.00 29.07 ? 51 ASN A N 1 ATOM 423 C CA . ASN A 1 51 ? 26.069 -11.961 42.997 1.00 25.97 ? 51 ASN A CA 1 ATOM 424 C C . ASN A 1 51 ? 25.621 -10.959 44.088 1.00 23.99 ? 51 ASN A C 1 ATOM 425 O O . ASN A 1 51 ? 26.198 -9.909 44.242 1.00 22.94 ? 51 ASN A O 1 ATOM 426 C CB . ASN A 1 51 ? 26.731 -11.218 41.866 1.00 24.33 ? 51 ASN A CB 1 ATOM 427 C CG . ASN A 1 51 ? 25.777 -10.302 41.165 1.00 24.42 ? 51 ASN A CG 1 ATOM 428 O OD1 . ASN A 1 51 ? 24.622 -10.626 41.021 1.00 26.24 ? 51 ASN A OD1 1 ATOM 429 N ND2 . ASN A 1 51 ? 26.248 -9.154 40.729 1.00 26.56 ? 51 ASN A ND2 1 ATOM 430 N N . ASP A 1 52 ? 24.620 -11.297 44.872 1.00 22.51 ? 52 ASP A N 1 ATOM 431 C CA . ASP A 1 52 ? 24.159 -10.369 45.920 1.00 21.88 ? 52 ASP A CA 1 ATOM 432 C C . ASP A 1 52 ? 25.195 -10.086 47.024 1.00 21.60 ? 52 ASP A C 1 ATOM 433 O O . ASP A 1 52 ? 25.384 -8.972 47.445 1.00 22.08 ? 52 ASP A O 1 ATOM 434 C CB . ASP A 1 52 ? 22.844 -10.851 46.553 1.00 20.69 ? 52 ASP A CB 1 ATOM 435 C CG . ASP A 1 52 ? 21.672 -10.420 45.799 1.00 20.83 ? 52 ASP A CG 1 ATOM 436 O OD1 . ASP A 1 52 ? 21.795 -9.417 45.089 1.00 23.21 ? 52 ASP A OD1 1 ATOM 437 O OD2 . ASP A 1 52 ? 20.594 -11.012 45.881 1.00 23.02 ? 52 ASP A OD2 1 ATOM 438 N N . VAL A 1 53 ? 25.841 -11.105 47.524 1.00 22.07 ? 53 VAL A N 1 ATOM 439 C CA . VAL A 1 53 ? 26.826 -10.917 48.562 1.00 22.43 ? 53 VAL A CA 1 ATOM 440 C C . VAL A 1 53 ? 27.883 -9.954 48.082 1.00 20.99 ? 53 VAL A C 1 ATOM 441 O O . VAL A 1 53 ? 28.370 -9.145 48.868 1.00 21.96 ? 53 VAL A O 1 ATOM 442 C CB . VAL A 1 53 ? 27.525 -12.250 49.005 1.00 22.39 ? 53 VAL A CB 1 ATOM 443 C CG1 . VAL A 1 53 ? 26.525 -13.166 49.659 1.00 20.79 ? 53 VAL A CG1 1 ATOM 444 C CG2 . VAL A 1 53 ? 28.110 -12.943 47.857 1.00 26.81 ? 53 VAL A CG2 1 ATOM 445 N N . THR A 1 54 ? 28.227 -10.022 46.804 1.00 18.51 ? 54 THR A N 1 ATOM 446 C CA . THR A 1 54 ? 29.234 -9.100 46.314 1.00 18.57 ? 54 THR A CA 1 ATOM 447 C C . THR A 1 54 ? 28.708 -7.674 46.380 1.00 17.56 ? 54 THR A C 1 ATOM 448 O O . THR A 1 54 ? 29.289 -6.801 46.957 1.00 18.30 ? 54 THR A O 1 ATOM 449 C CB . THR A 1 54 ? 29.627 -9.401 44.900 1.00 18.29 ? 54 THR A CB 1 ATOM 450 O OG1 . THR A 1 54 ? 30.439 -10.588 44.876 1.00 19.05 ? 54 THR A OG1 1 ATOM 451 C CG2 . THR A 1 54 ? 30.442 -8.257 44.306 1.00 17.74 ? 54 THR A CG2 1 ATOM 452 N N . LEU A 1 55 ? 27.575 -7.470 45.778 1.00 17.31 ? 55 LEU A N 1 ATOM 453 C CA . LEU A 1 55 ? 26.950 -6.165 45.755 1.00 16.81 ? 55 LEU A CA 1 ATOM 454 C C . LEU A 1 55 ? 26.560 -5.708 47.143 1.00 15.85 ? 55 LEU A C 1 ATOM 455 O O . LEU A 1 55 ? 26.565 -4.537 47.420 1.00 17.00 ? 55 LEU A O 1 ATOM 456 C CB . LEU A 1 55 ? 25.723 -6.176 44.839 1.00 17.22 ? 55 LEU A CB 1 ATOM 457 C CG . LEU A 1 55 ? 25.968 -6.629 43.367 1.00 17.67 ? 55 LEU A CG 1 ATOM 458 C CD1 . LEU A 1 55 ? 24.698 -6.436 42.528 1.00 17.61 ? 55 LEU A CD1 1 ATOM 459 C CD2 . LEU A 1 55 ? 27.093 -5.851 42.760 1.00 19.06 ? 55 LEU A CD2 1 ATOM 460 N N . TYR A 1 56 ? 26.206 -6.630 48.021 1.00 15.09 ? 56 TYR A N 1 ATOM 461 C CA . TYR A 1 56 ? 25.865 -6.269 49.404 1.00 14.31 ? 56 TYR A CA 1 ATOM 462 C C . TYR A 1 56 ? 27.059 -5.479 49.970 1.00 15.29 ? 56 TYR A C 1 ATOM 463 O O . TYR A 1 56 ? 26.928 -4.445 50.582 1.00 12.43 ? 56 TYR A O 1 ATOM 464 C CB . TYR A 1 56 ? 25.658 -7.527 50.254 1.00 12.96 ? 56 TYR A CB 1 ATOM 465 C CG . TYR A 1 56 ? 24.338 -8.207 50.168 1.00 9.83 ? 56 TYR A CG 1 ATOM 466 C CD1 . TYR A 1 56 ? 23.319 -7.692 49.450 1.00 11.40 ? 56 TYR A CD1 1 ATOM 467 C CD2 . TYR A 1 56 ? 24.099 -9.350 50.871 1.00 11.91 ? 56 TYR A CD2 1 ATOM 468 C CE1 . TYR A 1 56 ? 22.086 -8.313 49.399 1.00 13.20 ? 56 TYR A CE1 1 ATOM 469 C CE2 . TYR A 1 56 ? 22.860 -9.988 50.824 1.00 12.87 ? 56 TYR A CE2 1 ATOM 470 C CZ . TYR A 1 56 ? 21.884 -9.471 50.081 1.00 11.72 ? 56 TYR A CZ 1 ATOM 471 O OH . TYR A 1 56 ? 20.707 -10.112 49.978 1.00 16.91 ? 56 TYR A OH 1 ATOM 472 N N . ASP A 1 57 ? 28.229 -6.047 49.708 1.00 17.66 ? 57 ASP A N 1 ATOM 473 C CA . ASP A 1 57 ? 29.518 -5.532 50.132 1.00 19.09 ? 57 ASP A CA 1 ATOM 474 C C . ASP A 1 57 ? 29.848 -4.161 49.542 1.00 18.33 ? 57 ASP A C 1 ATOM 475 O O . ASP A 1 57 ? 30.373 -3.303 50.232 1.00 16.93 ? 57 ASP A O 1 ATOM 476 C CB . ASP A 1 57 ? 30.608 -6.573 49.782 1.00 19.34 ? 57 ASP A CB 1 ATOM 477 C CG . ASP A 1 57 ? 31.903 -6.310 50.469 1.00 22.57 ? 57 ASP A CG 1 ATOM 478 O OD1 . ASP A 1 57 ? 31.905 -5.958 51.669 1.00 23.63 ? 57 ASP A OD1 1 ATOM 479 O OD2 . ASP A 1 57 ? 32.977 -6.450 49.845 1.00 31.58 ? 57 ASP A OD2 1 ATOM 480 N N . THR A 1 58 ? 29.544 -3.981 48.275 1.00 19.36 ? 58 THR A N 1 ATOM 481 C CA . THR A 1 58 ? 29.816 -2.727 47.579 1.00 22.50 ? 58 THR A CA 1 ATOM 482 C C . THR A 1 58 ? 29.014 -1.564 48.144 1.00 23.99 ? 58 THR A C 1 ATOM 483 O O . THR A 1 58 ? 29.559 -0.448 48.372 1.00 23.49 ? 58 THR A O 1 ATOM 484 C CB . THR A 1 58 ? 29.433 -2.841 46.121 1.00 22.81 ? 58 THR A CB 1 ATOM 485 O OG1 . THR A 1 58 ? 30.094 -3.968 45.536 1.00 25.11 ? 58 THR A OG1 1 ATOM 486 C CG2 . THR A 1 58 ? 29.862 -1.598 45.375 1.00 24.61 ? 58 THR A CG2 1 ATOM 487 N N . LEU A 1 59 ? 27.712 -1.836 48.328 1.00 24.22 ? 59 LEU A N 1 ATOM 488 C CA . LEU A 1 59 ? 26.771 -0.902 48.907 1.00 23.56 ? 59 LEU A CA 1 ATOM 489 C C . LEU A 1 59 ? 27.201 -0.563 50.336 1.00 24.00 ? 59 LEU A C 1 ATOM 490 O O . LEU A 1 59 ? 27.276 0.580 50.722 1.00 25.24 ? 59 LEU A O 1 ATOM 491 C CB . LEU A 1 59 ? 25.389 -1.526 48.942 1.00 23.18 ? 59 LEU A CB 1 ATOM 492 C CG . LEU A 1 59 ? 24.249 -0.709 49.561 1.00 21.16 ? 59 LEU A CG 1 ATOM 493 C CD1 . LEU A 1 59 ? 23.927 0.413 48.624 1.00 19.52 ? 59 LEU A CD1 1 ATOM 494 C CD2 . LEU A 1 59 ? 23.018 -1.587 49.800 1.00 18.23 ? 59 LEU A CD2 1 ATOM 495 N N . ASN A 1 60 ? 27.491 -1.575 51.125 1.00 24.28 ? 60 ASN A N 1 ATOM 496 C CA . ASN A 1 60 ? 27.876 -1.380 52.520 1.00 24.25 ? 60 ASN A CA 1 ATOM 497 C C . ASN A 1 60 ? 29.290 -0.802 52.729 1.00 23.76 ? 60 ASN A C 1 ATOM 498 O O . ASN A 1 60 ? 29.780 -0.568 53.850 1.00 25.44 ? 60 ASN A O 1 ATOM 499 C CB . ASN A 1 60 ? 27.668 -2.696 53.295 1.00 23.21 ? 60 ASN A CB 1 ATOM 500 C CG . ASN A 1 60 ? 26.173 -2.980 53.594 1.00 22.95 ? 60 ASN A CG 1 ATOM 501 O OD1 . ASN A 1 60 ? 25.712 -4.126 53.609 1.00 27.89 ? 60 ASN A OD1 1 ATOM 502 N ND2 . ASN A 1 60 ? 25.422 -1.927 53.833 1.00 18.61 ? 60 ASN A ND2 1 ATOM 503 N N . THR A 1 61 ? 29.993 -0.575 51.664 1.00 22.86 ? 61 THR A N 1 ATOM 504 C CA . THR A 1 61 ? 31.306 0.018 51.874 1.00 23.70 ? 61 THR A CA 1 ATOM 505 C C . THR A 1 61 ? 31.201 1.544 51.785 1.00 21.53 ? 61 THR A C 1 ATOM 506 O O . THR A 1 61 ? 32.105 2.257 52.183 1.00 22.06 ? 61 THR A O 1 ATOM 507 C CB . THR A 1 61 ? 32.316 -0.450 50.839 1.00 24.04 ? 61 THR A CB 1 ATOM 508 O OG1 . THR A 1 61 ? 31.729 -0.350 49.541 1.00 26.37 ? 61 THR A OG1 1 ATOM 509 C CG2 . THR A 1 61 ? 32.686 -1.913 51.085 1.00 26.35 ? 61 THR A CG2 1 ATOM 510 N N . LEU A 1 62 ? 30.078 2.023 51.270 1.00 17.93 ? 62 LEU A N 1 ATOM 511 C CA . LEU A 1 62 ? 29.845 3.441 51.142 1.00 14.05 ? 62 LEU A CA 1 ATOM 512 C C . LEU A 1 62 ? 29.844 4.009 52.512 1.00 13.72 ? 62 LEU A C 1 ATOM 513 O O . LEU A 1 62 ? 30.112 5.196 52.703 1.00 13.74 ? 62 LEU A O 1 ATOM 514 C CB . LEU A 1 62 ? 28.496 3.719 50.492 1.00 13.07 ? 62 LEU A CB 1 ATOM 515 C CG . LEU A 1 62 ? 28.247 3.192 49.077 1.00 12.73 ? 62 LEU A CG 1 ATOM 516 C CD1 . LEU A 1 62 ? 27.063 3.876 48.507 1.00 12.14 ? 62 LEU A CD1 1 ATOM 517 C CD2 . LEU A 1 62 ? 29.425 3.378 48.161 1.00 13.22 ? 62 LEU A CD2 1 ATOM 518 N N . LYS A 1 63 ? 29.509 3.169 53.477 1.00 13.34 ? 63 LYS A N 1 ATOM 519 C CA . LYS A 1 63 ? 29.507 3.591 54.863 1.00 13.93 ? 63 LYS A CA 1 ATOM 520 C C . LYS A 1 63 ? 30.919 3.845 55.279 1.00 16.32 ? 63 LYS A C 1 ATOM 521 O O . LYS A 1 63 ? 31.174 4.177 56.416 1.00 16.15 ? 63 LYS A O 1 ATOM 522 C CB . LYS A 1 63 ? 28.897 2.522 55.770 1.00 13.49 ? 63 LYS A CB 1 ATOM 523 C CG . LYS A 1 63 ? 27.343 2.583 55.811 1.00 14.56 ? 63 LYS A CG 1 ATOM 524 C CD . LYS A 1 63 ? 26.656 1.251 56.175 1.00 13.14 ? 63 LYS A CD 1 ATOM 525 C CE . LYS A 1 63 ? 27.030 0.768 57.537 1.00 18.42 ? 63 LYS A CE 1 ATOM 526 N NZ . LYS A 1 63 ? 26.443 -0.621 57.802 1.00 18.34 ? 63 LYS A NZ 1 ATOM 527 N N . ASN A 1 64 ? 31.853 3.657 54.352 1.00 19.42 ? 64 ASN A N 1 ATOM 528 C CA . ASN A 1 64 ? 33.238 3.930 54.666 1.00 22.93 ? 64 ASN A CA 1 ATOM 529 C C . ASN A 1 64 ? 33.621 5.346 54.314 1.00 23.82 ? 64 ASN A C 1 ATOM 530 O O . ASN A 1 64 ? 34.565 5.885 54.878 1.00 25.16 ? 64 ASN A O 1 ATOM 531 C CB . ASN A 1 64 ? 34.182 2.960 53.986 1.00 24.61 ? 64 ASN A CB 1 ATOM 532 C CG . ASN A 1 64 ? 34.421 1.731 54.825 1.00 28.92 ? 64 ASN A CG 1 ATOM 533 O OD1 . ASN A 1 64 ? 34.098 1.723 56.019 1.00 29.62 ? 64 ASN A OD1 1 ATOM 534 N ND2 . ASN A 1 64 ? 34.958 0.673 54.212 1.00 35.80 ? 64 ASN A ND2 1 ATOM 535 N N . ARG A 1 65 ? 32.891 5.950 53.394 1.00 25.13 ? 65 ARG A N 1 ATOM 536 C CA . ARG A 1 65 ? 33.133 7.335 53.033 1.00 26.74 ? 65 ARG A CA 1 ATOM 537 C C . ARG A 1 65 ? 32.179 8.220 53.831 1.00 24.77 ? 65 ARG A C 1 ATOM 538 O O . ARG A 1 65 ? 32.470 9.364 54.128 1.00 23.79 ? 65 ARG A O 1 ATOM 539 C CB . ARG A 1 65 ? 32.931 7.549 51.540 1.00 29.06 ? 65 ARG A CB 1 ATOM 540 C CG . ARG A 1 65 ? 34.164 7.213 50.720 1.00 36.56 ? 65 ARG A CG 1 ATOM 541 C CD . ARG A 1 65 ? 34.000 7.513 49.247 1.00 43.95 ? 65 ARG A CD 1 ATOM 542 N NE . ARG A 1 65 ? 33.024 6.614 48.654 1.00 49.23 ? 65 ARG A NE 1 ATOM 543 C CZ . ARG A 1 65 ? 32.602 6.726 47.409 1.00 54.59 ? 65 ARG A CZ 1 ATOM 544 N NH1 . ARG A 1 65 ? 33.076 7.702 46.637 1.00 56.98 ? 65 ARG A NH1 1 ATOM 545 N NH2 . ARG A 1 65 ? 31.699 5.876 46.928 1.00 56.05 ? 65 ARG A NH2 1 ATOM 546 N N . ASN A 1 66 ? 31.036 7.665 54.176 1.00 23.03 ? 66 ASN A N 1 ATOM 547 C CA . ASN A 1 66 ? 30.054 8.391 54.967 1.00 22.40 ? 66 ASN A CA 1 ATOM 548 C C . ASN A 1 66 ? 29.590 7.486 56.112 1.00 23.67 ? 66 ASN A C 1 ATOM 549 O O . ASN A 1 66 ? 28.752 6.598 55.919 1.00 24.46 ? 66 ASN A O 1 ATOM 550 C CB . ASN A 1 66 ? 28.856 8.764 54.092 1.00 21.27 ? 66 ASN A CB 1 ATOM 551 C CG . ASN A 1 66 ? 27.794 9.550 54.820 1.00 14.83 ? 66 ASN A CG 1 ATOM 552 O OD1 . ASN A 1 66 ? 27.985 10.000 55.945 1.00 14.04 ? 66 ASN A OD1 1 ATOM 553 N ND2 . ASN A 1 66 ? 26.684 9.736 54.164 1.00 9.06 ? 66 ASN A ND2 1 ATOM 554 N N . PRO A 1 67 ? 30.114 7.724 57.318 1.00 24.48 ? 67 PRO A N 1 ATOM 555 C CA . PRO A 1 67 ? 29.786 6.894 58.461 1.00 24.69 ? 67 PRO A CA 1 ATOM 556 C C . PRO A 1 67 ? 28.365 7.104 58.938 1.00 25.55 ? 67 PRO A C 1 ATOM 557 O O . PRO A 1 67 ? 27.802 6.200 59.541 1.00 27.55 ? 67 PRO A O 1 ATOM 558 C CB . PRO A 1 67 ? 30.818 7.339 59.463 1.00 24.73 ? 67 PRO A CB 1 ATOM 559 C CG . PRO A 1 67 ? 30.888 8.790 59.211 1.00 24.62 ? 67 PRO A CG 1 ATOM 560 C CD . PRO A 1 67 ? 30.986 8.836 57.732 1.00 25.02 ? 67 PRO A CD 1 ATOM 561 N N . LYS A 1 68 ? 27.795 8.276 58.669 1.00 26.00 ? 68 LYS A N 1 ATOM 562 C CA . LYS A 1 68 ? 26.417 8.606 59.048 1.00 25.53 ? 68 LYS A CA 1 ATOM 563 C C . LYS A 1 68 ? 25.456 7.685 58.262 1.00 23.16 ? 68 LYS A C 1 ATOM 564 O O . LYS A 1 68 ? 24.383 7.340 58.712 1.00 23.02 ? 68 LYS A O 1 ATOM 565 C CB . LYS A 1 68 ? 26.112 10.055 58.663 1.00 28.39 ? 68 LYS A CB 1 ATOM 566 C CG . LYS A 1 68 ? 26.605 11.102 59.638 1.00 34.18 ? 68 LYS A CG 1 ATOM 567 C CD . LYS A 1 68 ? 25.866 11.033 61.010 1.00 37.76 ? 68 LYS A CD 1 ATOM 568 C CE . LYS A 1 68 ? 26.674 10.287 62.059 1.00 36.93 ? 68 LYS A CE 1 ATOM 569 N NZ . LYS A 1 68 ? 26.532 11.010 63.376 1.00 35.39 ? 68 LYS A NZ 1 ATOM 570 N N . LEU A 1 69 ? 25.868 7.285 57.072 1.00 19.73 ? 69 LEU A N 1 ATOM 571 C CA . LEU A 1 69 ? 25.038 6.471 56.213 1.00 17.79 ? 69 LEU A CA 1 ATOM 572 C C . LEU A 1 69 ? 24.542 5.156 56.810 1.00 18.37 ? 69 LEU A C 1 ATOM 573 O O . LEU A 1 69 ? 25.304 4.392 57.360 1.00 22.13 ? 69 LEU A O 1 ATOM 574 C CB . LEU A 1 69 ? 25.780 6.225 54.927 1.00 15.83 ? 69 LEU A CB 1 ATOM 575 C CG . LEU A 1 69 ? 25.029 5.894 53.663 1.00 12.39 ? 69 LEU A CG 1 ATOM 576 C CD1 . LEU A 1 69 ? 25.081 4.426 53.497 1.00 11.84 ? 69 LEU A CD1 1 ATOM 577 C CD2 . LEU A 1 69 ? 23.656 6.389 53.742 1.00 12.49 ? 69 LEU A CD2 1 ATOM 578 N N . LYS A 1 70 ? 23.250 4.882 56.693 1.00 17.74 ? 70 LYS A N 1 ATOM 579 C CA . LYS A 1 70 ? 22.592 3.672 57.215 1.00 16.67 ? 70 LYS A CA 1 ATOM 580 C C . LYS A 1 70 ? 21.997 2.901 56.029 1.00 15.85 ? 70 LYS A C 1 ATOM 581 O O . LYS A 1 70 ? 21.404 3.500 55.170 1.00 16.78 ? 70 LYS A O 1 ATOM 582 C CB . LYS A 1 70 ? 21.461 4.023 58.169 1.00 16.03 ? 70 LYS A CB 1 ATOM 583 C CG . LYS A 1 70 ? 21.872 4.825 59.350 1.00 25.08 ? 70 LYS A CG 1 ATOM 584 C CD . LYS A 1 70 ? 21.971 4.000 60.584 1.00 33.64 ? 70 LYS A CD 1 ATOM 585 C CE . LYS A 1 70 ? 22.922 4.610 61.613 1.00 41.48 ? 70 LYS A CE 1 ATOM 586 N NZ . LYS A 1 70 ? 23.281 3.526 62.640 1.00 45.33 ? 70 LYS A NZ 1 ATOM 587 N N . THR A 1 71 ? 22.188 1.591 55.958 1.00 13.99 ? 71 THR A N 1 ATOM 588 C CA . THR A 1 71 ? 21.635 0.812 54.862 1.00 12.97 ? 71 THR A CA 1 ATOM 589 C C . THR A 1 71 ? 20.718 -0.273 55.402 1.00 12.06 ? 71 THR A C 1 ATOM 590 O O . THR A 1 71 ? 20.930 -0.778 56.484 1.00 11.40 ? 71 THR A O 1 ATOM 591 C CB . THR A 1 71 ? 22.668 0.159 53.957 1.00 14.15 ? 71 THR A CB 1 ATOM 592 O OG1 . THR A 1 71 ? 23.500 -0.725 54.723 1.00 19.56 ? 71 THR A OG1 1 ATOM 593 C CG2 . THR A 1 71 ? 23.536 1.183 53.322 1.00 14.37 ? 71 THR A CG2 1 ATOM 594 N N . LEU A 1 72 ? 19.637 -0.582 54.666 1.00 11.23 ? 72 LEU A N 1 ATOM 595 C CA . LEU A 1 72 ? 18.701 -1.615 55.067 1.00 11.07 ? 72 LEU A CA 1 ATOM 596 C C . LEU A 1 72 ? 18.504 -2.550 53.904 1.00 10.78 ? 72 LEU A C 1 ATOM 597 O O . LEU A 1 72 ? 18.815 -2.191 52.775 1.00 10.37 ? 72 LEU A O 1 ATOM 598 C CB . LEU A 1 72 ? 17.372 -0.994 55.436 1.00 10.58 ? 72 LEU A CB 1 ATOM 599 C CG . LEU A 1 72 ? 17.233 -0.159 56.694 1.00 14.43 ? 72 LEU A CG 1 ATOM 600 C CD1 . LEU A 1 72 ? 17.747 1.249 56.420 1.00 19.68 ? 72 LEU A CD1 1 ATOM 601 C CD2 . LEU A 1 72 ? 15.769 -0.112 57.139 1.00 14.46 ? 72 LEU A CD2 1 ATOM 602 N N . LEU A 1 73 ? 17.976 -3.738 54.194 1.00 9.65 ? 73 LEU A N 1 ATOM 603 C CA . LEU A 1 73 ? 17.678 -4.715 53.168 1.00 9.72 ? 73 LEU A CA 1 ATOM 604 C C . LEU A 1 73 ? 16.187 -4.898 53.129 1.00 8.91 ? 73 LEU A C 1 ATOM 605 O O . LEU A 1 73 ? 15.580 -4.883 54.183 1.00 12.08 ? 73 LEU A O 1 ATOM 606 C CB . LEU A 1 73 ? 18.322 -6.068 53.511 1.00 11.39 ? 73 LEU A CB 1 ATOM 607 C CG . LEU A 1 73 ? 18.054 -7.219 52.478 1.00 9.27 ? 73 LEU A CG 1 ATOM 608 C CD1 . LEU A 1 73 ? 18.567 -6.865 51.103 1.00 3.58 ? 73 LEU A CD1 1 ATOM 609 C CD2 . LEU A 1 73 ? 18.743 -8.449 52.953 1.00 7.75 ? 73 LEU A CD2 1 ATOM 610 N N . SER A 1 74 ? 15.607 -5.084 51.953 1.00 7.49 ? 74 SER A N 1 ATOM 611 C CA . SER A 1 74 ? 14.156 -5.213 51.833 1.00 8.20 ? 74 SER A CA 1 ATOM 612 C C . SER A 1 74 ? 13.676 -6.568 51.418 1.00 8.16 ? 74 SER A C 1 ATOM 613 O O . SER A 1 74 ? 14.293 -7.201 50.629 1.00 10.38 ? 74 SER A O 1 ATOM 614 C CB . SER A 1 74 ? 13.632 -4.165 50.850 1.00 6.13 ? 74 SER A CB 1 ATOM 615 O OG . SER A 1 74 ? 12.255 -4.086 50.961 1.00 7.99 ? 74 SER A OG 1 ATOM 616 N N . VAL A 1 75 ? 12.574 -7.037 51.974 1.00 8.17 ? 75 VAL A N 1 ATOM 617 C CA . VAL A 1 75 ? 12.045 -8.373 51.645 1.00 9.95 ? 75 VAL A CA 1 ATOM 618 C C . VAL A 1 75 ? 10.665 -8.294 51.057 1.00 11.91 ? 75 VAL A C 1 ATOM 619 O O . VAL A 1 75 ? 9.770 -7.784 51.685 1.00 10.98 ? 75 VAL A O 1 ATOM 620 C CB . VAL A 1 75 ? 11.930 -9.304 52.869 1.00 8.43 ? 75 VAL A CB 1 ATOM 621 C CG1 . VAL A 1 75 ? 11.771 -10.773 52.399 1.00 5.28 ? 75 VAL A CG1 1 ATOM 622 C CG2 . VAL A 1 75 ? 13.146 -9.205 53.738 1.00 13.01 ? 75 VAL A CG2 1 ATOM 623 N N . GLY A 1 76 ? 10.503 -8.824 49.844 1.00 15.92 ? 76 GLY A N 1 ATOM 624 C CA . GLY A 1 76 ? 9.236 -8.801 49.196 1.00 19.12 ? 76 GLY A CA 1 ATOM 625 C C . GLY A 1 76 ? 9.359 -8.168 47.858 1.00 23.73 ? 76 GLY A C 1 ATOM 626 O O . GLY A 1 76 ? 10.299 -8.462 47.132 1.00 24.67 ? 76 GLY A O 1 ATOM 627 N N . GLY A 1 77 ? 8.413 -7.295 47.538 1.00 29.00 ? 77 GLY A N 1 ATOM 628 C CA . GLY A 1 77 ? 8.390 -6.642 46.245 1.00 34.75 ? 77 GLY A CA 1 ATOM 629 C C . GLY A 1 77 ? 7.187 -7.107 45.438 1.00 39.74 ? 77 GLY A C 1 ATOM 630 O O . GLY A 1 77 ? 6.530 -8.084 45.799 1.00 38.85 ? 77 GLY A O 1 ATOM 631 N N . TRP A 1 78 ? 6.916 -6.430 44.325 1.00 45.44 ? 78 TRP A N 1 ATOM 632 C CA . TRP A 1 78 ? 5.767 -6.807 43.535 1.00 50.71 ? 78 TRP A CA 1 ATOM 633 C C . TRP A 1 78 ? 5.871 -8.242 42.994 1.00 51.03 ? 78 TRP A C 1 ATOM 634 O O . TRP A 1 78 ? 4.952 -9.038 43.168 1.00 51.14 ? 78 TRP A O 1 ATOM 635 C CB . TRP A 1 78 ? 5.561 -5.832 42.428 1.00 54.29 ? 78 TRP A CB 1 ATOM 636 C CG . TRP A 1 78 ? 4.211 -6.075 41.821 1.00 63.39 ? 78 TRP A CG 1 ATOM 637 C CD1 . TRP A 1 78 ? 3.960 -6.601 40.576 1.00 68.87 ? 78 TRP A CD1 1 ATOM 638 C CD2 . TRP A 1 78 ? 2.920 -5.838 42.413 1.00 68.24 ? 78 TRP A CD2 1 ATOM 639 N NE1 . TRP A 1 78 ? 2.617 -6.681 40.336 1.00 70.48 ? 78 TRP A NE1 1 ATOM 640 C CE2 . TRP A 1 78 ? 1.947 -6.219 41.447 1.00 69.83 ? 78 TRP A CE2 1 ATOM 641 C CE3 . TRP A 1 78 ? 2.469 -5.341 43.639 1.00 68.10 ? 78 TRP A CE3 1 ATOM 642 C CZ2 . TRP A 1 78 ? 0.571 -6.103 41.683 1.00 68.68 ? 78 TRP A CZ2 1 ATOM 643 C CZ3 . TRP A 1 78 ? 1.106 -5.227 43.859 1.00 68.54 ? 78 TRP A CZ3 1 ATOM 644 C CH2 . TRP A 1 78 ? 0.175 -5.611 42.886 1.00 67.48 ? 78 TRP A CH2 1 ATOM 645 N N . ASN A 1 79 ? 6.993 -8.551 42.347 1.00 51.11 ? 79 ASN A N 1 ATOM 646 C CA . ASN A 1 79 ? 7.259 -9.888 41.756 1.00 51.66 ? 79 ASN A CA 1 ATOM 647 C C . ASN A 1 79 ? 7.565 -10.974 42.835 1.00 48.96 ? 79 ASN A C 1 ATOM 648 O O . ASN A 1 79 ? 8.292 -11.936 42.579 1.00 49.02 ? 79 ASN A O 1 ATOM 649 C CB . ASN A 1 79 ? 8.481 -9.800 40.776 1.00 54.01 ? 79 ASN A CB 1 ATOM 650 C CG . ASN A 1 79 ? 8.193 -9.279 39.336 1.00 58.45 ? 79 ASN A CG 1 ATOM 651 O OD1 . ASN A 1 79 ? 7.715 -8.151 39.149 1.00 59.43 ? 79 ASN A OD1 1 ATOM 652 N ND2 . ASN A 1 79 ? 8.523 -10.111 38.339 1.00 61.85 ? 79 ASN A ND2 1 ATOM 653 N N . PHE A 1 80 ? 7.028 -10.789 44.029 1.00 45.41 ? 80 PHE A N 1 ATOM 654 C CA . PHE A 1 80 ? 7.174 -11.730 45.135 1.00 42.21 ? 80 PHE A CA 1 ATOM 655 C C . PHE A 1 80 ? 5.743 -11.954 45.565 1.00 41.26 ? 80 PHE A C 1 ATOM 656 O O . PHE A 1 80 ? 5.116 -11.060 46.135 1.00 42.45 ? 80 PHE A O 1 ATOM 657 C CB . PHE A 1 80 ? 8.017 -11.133 46.286 1.00 41.30 ? 80 PHE A CB 1 ATOM 658 C CG . PHE A 1 80 ? 8.173 -12.051 47.484 1.00 37.15 ? 80 PHE A CG 1 ATOM 659 C CD1 . PHE A 1 80 ? 7.119 -12.287 48.317 1.00 34.74 ? 80 PHE A CD1 1 ATOM 660 C CD2 . PHE A 1 80 ? 9.373 -12.684 47.751 1.00 35.21 ? 80 PHE A CD2 1 ATOM 661 C CE1 . PHE A 1 80 ? 7.243 -13.144 49.387 1.00 33.33 ? 80 PHE A CE1 1 ATOM 662 C CE2 . PHE A 1 80 ? 9.509 -13.538 48.815 1.00 32.02 ? 80 PHE A CE2 1 ATOM 663 C CZ . PHE A 1 80 ? 8.438 -13.779 49.625 1.00 32.34 ? 80 PHE A CZ 1 ATOM 664 N N . GLY A 1 81 ? 5.152 -13.097 45.269 1.00 38.81 ? 81 GLY A N 1 ATOM 665 C CA . GLY A 1 81 ? 3.743 -13.252 45.565 1.00 37.87 ? 81 GLY A CA 1 ATOM 666 C C . GLY A 1 81 ? 3.452 -12.967 47.041 1.00 36.83 ? 81 GLY A C 1 ATOM 667 O O . GLY A 1 81 ? 4.258 -13.263 47.901 1.00 38.06 ? 81 GLY A O 1 ATOM 668 N N . PRO A 1 82 ? 2.288 -12.368 47.291 1.00 34.21 ? 82 PRO A N 1 ATOM 669 C CA . PRO A 1 82 ? 1.791 -12.174 48.630 1.00 32.93 ? 82 PRO A CA 1 ATOM 670 C C . PRO A 1 82 ? 1.328 -13.474 49.294 1.00 33.02 ? 82 PRO A C 1 ATOM 671 O O . PRO A 1 82 ? 1.466 -13.620 50.522 1.00 32.69 ? 82 PRO A O 1 ATOM 672 C CB . PRO A 1 82 ? 0.663 -11.209 48.409 1.00 32.39 ? 82 PRO A CB 1 ATOM 673 C CG . PRO A 1 82 ? 0.230 -11.498 47.026 1.00 32.57 ? 82 PRO A CG 1 ATOM 674 C CD . PRO A 1 82 ? 1.501 -11.585 46.350 1.00 33.92 ? 82 PRO A CD 1 ATOM 675 N N . GLU A 1 83 ? 0.828 -14.425 48.514 1.00 32.68 ? 83 GLU A N 1 ATOM 676 C CA . GLU A 1 83 ? 0.391 -15.691 49.093 1.00 33.26 ? 83 GLU A CA 1 ATOM 677 C C . GLU A 1 83 ? 1.555 -16.263 49.778 1.00 32.01 ? 83 GLU A C 1 ATOM 678 O O . GLU A 1 83 ? 1.417 -16.991 50.727 1.00 32.41 ? 83 GLU A O 1 ATOM 679 C CB . GLU A 1 83 ? -0.075 -16.698 48.058 1.00 33.95 ? 83 GLU A CB 1 ATOM 680 C CG . GLU A 1 83 ? -0.489 -16.096 46.728 1.00 41.53 ? 83 GLU A CG 1 ATOM 681 C CD . GLU A 1 83 ? 0.677 -15.426 46.003 1.00 45.67 ? 83 GLU A CD 1 ATOM 682 O OE1 . GLU A 1 83 ? 1.805 -16.014 46.058 1.00 46.45 ? 83 GLU A OE1 1 ATOM 683 O OE2 . GLU A 1 83 ? 0.446 -14.324 45.398 1.00 45.44 ? 83 GLU A OE2 1 ATOM 684 N N . ARG A 1 84 ? 2.730 -15.944 49.283 1.00 31.65 ? 84 ARG A N 1 ATOM 685 C CA . ARG A 1 84 ? 3.933 -16.478 49.906 1.00 32.18 ? 84 ARG A CA 1 ATOM 686 C C . ARG A 1 84 ? 4.140 -15.805 51.291 1.00 31.88 ? 84 ARG A C 1 ATOM 687 O O . ARG A 1 84 ? 4.324 -16.474 52.293 1.00 33.70 ? 84 ARG A O 1 ATOM 688 C CB . ARG A 1 84 ? 5.144 -16.278 49.002 1.00 31.81 ? 84 ARG A CB 1 ATOM 689 C CG . ARG A 1 84 ? 5.089 -17.043 47.733 1.00 31.73 ? 84 ARG A CG 1 ATOM 690 C CD . ARG A 1 84 ? 6.389 -16.902 46.965 1.00 32.43 ? 84 ARG A CD 1 ATOM 691 N NE . ARG A 1 84 ? 7.509 -17.438 47.695 1.00 29.42 ? 84 ARG A NE 1 ATOM 692 C CZ . ARG A 1 84 ? 8.750 -17.012 47.537 1.00 31.28 ? 84 ARG A CZ 1 ATOM 693 N NH1 . ARG A 1 84 ? 9.017 -16.044 46.700 1.00 27.69 ? 84 ARG A NH1 1 ATOM 694 N NH2 . ARG A 1 84 ? 9.745 -17.565 48.227 1.00 37.02 ? 84 ARG A NH2 1 ATOM 695 N N . PHE A 1 85 ? 4.107 -14.489 51.349 1.00 29.90 ? 85 PHE A N 1 ATOM 696 C CA . PHE A 1 85 ? 4.266 -13.812 52.604 1.00 28.14 ? 85 PHE A CA 1 ATOM 697 C C . PHE A 1 85 ? 3.196 -14.264 53.522 1.00 27.86 ? 85 PHE A C 1 ATOM 698 O O . PHE A 1 85 ? 3.422 -14.647 54.660 1.00 26.40 ? 85 PHE A O 1 ATOM 699 C CB . PHE A 1 85 ? 4.127 -12.290 52.412 1.00 28.78 ? 85 PHE A CB 1 ATOM 700 C CG . PHE A 1 85 ? 5.374 -11.529 52.743 1.00 24.81 ? 85 PHE A CG 1 ATOM 701 C CD1 . PHE A 1 85 ? 5.904 -11.624 53.989 1.00 18.74 ? 85 PHE A CD1 1 ATOM 702 C CD2 . PHE A 1 85 ? 6.038 -10.814 51.783 1.00 25.90 ? 85 PHE A CD2 1 ATOM 703 C CE1 . PHE A 1 85 ? 7.018 -10.982 54.312 1.00 20.77 ? 85 PHE A CE1 1 ATOM 704 C CE2 . PHE A 1 85 ? 7.199 -10.176 52.086 1.00 27.73 ? 85 PHE A CE2 1 ATOM 705 C CZ . PHE A 1 85 ? 7.690 -10.256 53.375 1.00 26.73 ? 85 PHE A CZ 1 ATOM 706 N N . SER A 1 86 ? 1.981 -14.212 53.014 1.00 29.23 ? 86 SER A N 1 ATOM 707 C CA . SER A 1 86 ? 0.770 -14.582 53.768 1.00 30.01 ? 86 SER A CA 1 ATOM 708 C C . SER A 1 86 ? 0.815 -15.921 54.499 1.00 30.78 ? 86 SER A C 1 ATOM 709 O O . SER A 1 86 ? 0.313 -16.058 55.616 1.00 31.33 ? 86 SER A O 1 ATOM 710 C CB . SER A 1 86 ? -0.396 -14.578 52.831 1.00 28.65 ? 86 SER A CB 1 ATOM 711 O OG . SER A 1 86 ? -1.500 -14.912 53.580 1.00 31.77 ? 86 SER A OG 1 ATOM 712 N N . LYS A 1 87 ? 1.461 -16.896 53.876 1.00 32.02 ? 87 LYS A N 1 ATOM 713 C CA . LYS A 1 87 ? 1.576 -18.240 54.422 1.00 33.21 ? 87 LYS A CA 1 ATOM 714 C C . LYS A 1 87 ? 2.687 -18.433 55.445 1.00 31.72 ? 87 LYS A C 1 ATOM 715 O O . LYS A 1 87 ? 2.641 -19.406 56.209 1.00 33.03 ? 87 LYS A O 1 ATOM 716 C CB . LYS A 1 87 ? 1.683 -19.186 53.238 1.00 35.36 ? 87 LYS A CB 1 ATOM 717 C CG . LYS A 1 87 ? 2.480 -20.433 53.414 1.00 43.77 ? 87 LYS A CG 1 ATOM 718 C CD . LYS A 1 87 ? 2.588 -21.154 52.036 1.00 50.52 ? 87 LYS A CD 1 ATOM 719 C CE . LYS A 1 87 ? 1.225 -21.111 51.290 1.00 54.92 ? 87 LYS A CE 1 ATOM 720 N NZ . LYS A 1 87 ? 0.068 -21.718 52.094 1.00 55.87 ? 87 LYS A NZ 1 ATOM 721 N N . ILE A 1 88 ? 3.679 -17.506 55.464 1.00 29.64 ? 88 ILE A N 1 ATOM 722 C CA . ILE A 1 88 ? 4.802 -17.527 56.437 1.00 26.68 ? 88 ILE A CA 1 ATOM 723 C C . ILE A 1 88 ? 4.306 -16.854 57.702 1.00 25.68 ? 88 ILE A C 1 ATOM 724 O O . ILE A 1 88 ? 4.645 -17.247 58.802 1.00 25.50 ? 88 ILE A O 1 ATOM 725 C CB . ILE A 1 88 ? 5.968 -16.632 56.054 1.00 26.13 ? 88 ILE A CB 1 ATOM 726 C CG1 . ILE A 1 88 ? 6.440 -16.873 54.638 1.00 28.30 ? 88 ILE A CG1 1 ATOM 727 C CG2 . ILE A 1 88 ? 7.109 -16.873 56.985 1.00 27.05 ? 88 ILE A CG2 1 ATOM 728 C CD1 . ILE A 1 88 ? 7.446 -17.982 54.519 1.00 27.10 ? 88 ILE A CD1 1 ATOM 729 N N . ALA A 1 89 ? 3.501 -15.817 57.528 1.00 23.55 ? 89 ALA A N 1 ATOM 730 C CA . ALA A 1 89 ? 3.076 -15.033 58.639 1.00 23.44 ? 89 ALA A CA 1 ATOM 731 C C . ALA A 1 89 ? 1.915 -15.574 59.400 1.00 24.65 ? 89 ALA A C 1 ATOM 732 O O . ALA A 1 89 ? 1.710 -15.190 60.545 1.00 25.41 ? 89 ALA A O 1 ATOM 733 C CB . ALA A 1 89 ? 2.753 -13.672 58.176 1.00 24.97 ? 89 ALA A CB 1 ATOM 734 N N . SER A 1 90 ? 1.130 -16.464 58.810 1.00 26.14 ? 90 SER A N 1 ATOM 735 C CA . SER A 1 90 ? -0.064 -17.017 59.514 1.00 26.51 ? 90 SER A CA 1 ATOM 736 C C . SER A 1 90 ? 0.142 -18.297 60.316 1.00 26.88 ? 90 SER A C 1 ATOM 737 O O . SER A 1 90 ? -0.768 -18.752 60.949 1.00 25.79 ? 90 SER A O 1 ATOM 738 C CB . SER A 1 90 ? -1.178 -17.212 58.538 1.00 25.74 ? 90 SER A CB 1 ATOM 739 O OG . SER A 1 90 ? -0.629 -17.719 57.344 1.00 28.55 ? 90 SER A OG 1 ATOM 740 N N . LYS A 1 91 ? 1.348 -18.856 60.286 1.00 29.17 ? 91 LYS A N 1 ATOM 741 C CA . LYS A 1 91 ? 1.700 -20.061 61.034 1.00 30.73 ? 91 LYS A CA 1 ATOM 742 C C . LYS A 1 91 ? 2.786 -19.625 61.976 1.00 31.46 ? 91 LYS A C 1 ATOM 743 O O . LYS A 1 91 ? 3.944 -19.629 61.608 1.00 34.21 ? 91 LYS A O 1 ATOM 744 C CB . LYS A 1 91 ? 2.298 -21.160 60.123 1.00 30.85 ? 91 LYS A CB 1 ATOM 745 C CG . LYS A 1 91 ? 1.368 -21.757 59.073 1.00 33.17 ? 91 LYS A CG 1 ATOM 746 C CD . LYS A 1 91 ? 2.150 -22.722 58.185 1.00 36.29 ? 91 LYS A CD 1 ATOM 747 C CE . LYS A 1 91 ? 1.268 -23.600 57.275 1.00 36.78 ? 91 LYS A CE 1 ATOM 748 N NZ . LYS A 1 91 ? 0.474 -22.825 56.264 1.00 34.54 ? 91 LYS A NZ 1 ATOM 749 N N . THR A 1 92 ? 2.460 -19.289 63.196 1.00 32.12 ? 92 THR A N 1 ATOM 750 C CA . THR A 1 92 ? 3.496 -18.845 64.142 1.00 33.28 ? 92 THR A CA 1 ATOM 751 C C . THR A 1 92 ? 4.764 -19.660 64.079 1.00 33.40 ? 92 THR A C 1 ATOM 752 O O . THR A 1 92 ? 5.837 -19.151 64.309 1.00 35.45 ? 92 THR A O 1 ATOM 753 C CB . THR A 1 92 ? 3.034 -18.879 65.623 1.00 33.02 ? 92 THR A CB 1 ATOM 754 O OG1 . THR A 1 92 ? 3.220 -20.179 66.156 1.00 29.76 ? 92 THR A OG1 1 ATOM 755 C CG2 . THR A 1 92 ? 1.542 -18.499 65.738 1.00 35.45 ? 92 THR A CG2 1 ATOM 756 N N . GLN A 1 93 ? 4.670 -20.924 63.768 1.00 33.26 ? 93 GLN A N 1 ATOM 757 C CA . GLN A 1 93 ? 5.881 -21.720 63.735 1.00 33.59 ? 93 GLN A CA 1 ATOM 758 C C . GLN A 1 93 ? 6.763 -21.304 62.562 1.00 30.82 ? 93 GLN A C 1 ATOM 759 O O . GLN A 1 93 ? 7.954 -21.118 62.702 1.00 30.83 ? 93 GLN A O 1 ATOM 760 C CB . GLN A 1 93 ? 5.549 -23.219 63.691 1.00 36.69 ? 93 GLN A CB 1 ATOM 761 C CG . GLN A 1 93 ? 5.945 -23.924 62.380 1.00 44.28 ? 93 GLN A CG 1 ATOM 762 C CD . GLN A 1 93 ? 4.728 -24.556 61.589 1.00 51.07 ? 93 GLN A CD 1 ATOM 763 O OE1 . GLN A 1 93 ? 4.185 -25.614 61.993 1.00 54.58 ? 93 GLN A OE1 1 ATOM 764 N NE2 . GLN A 1 93 ? 4.321 -23.909 60.472 1.00 50.74 ? 93 GLN A NE2 1 ATOM 765 N N . SER A 1 94 ? 6.188 -21.137 61.384 1.00 27.99 ? 94 SER A N 1 ATOM 766 C CA . SER A 1 94 ? 6.991 -20.783 60.223 1.00 24.90 ? 94 SER A CA 1 ATOM 767 C C . SER A 1 94 ? 7.377 -19.333 60.322 1.00 23.85 ? 94 SER A C 1 ATOM 768 O O . SER A 1 94 ? 8.384 -18.890 59.751 1.00 24.03 ? 94 SER A O 1 ATOM 769 C CB . SER A 1 94 ? 6.226 -21.058 58.938 1.00 23.88 ? 94 SER A CB 1 ATOM 770 O OG . SER A 1 94 ? 4.952 -20.442 58.965 1.00 24.59 ? 94 SER A OG 1 ATOM 771 N N . ARG A 1 95 ? 6.606 -18.582 61.079 1.00 23.20 ? 95 ARG A N 1 ATOM 772 C CA . ARG A 1 95 ? 6.856 -17.146 61.274 1.00 23.31 ? 95 ARG A CA 1 ATOM 773 C C . ARG A 1 95 ? 8.048 -16.903 62.208 1.00 24.47 ? 95 ARG A C 1 ATOM 774 O O . ARG A 1 95 ? 8.965 -16.143 61.906 1.00 22.74 ? 95 ARG A O 1 ATOM 775 C CB . ARG A 1 95 ? 5.604 -16.451 61.865 1.00 21.34 ? 95 ARG A CB 1 ATOM 776 C CG . ARG A 1 95 ? 5.873 -15.064 62.316 1.00 20.51 ? 95 ARG A CG 1 ATOM 777 C CD . ARG A 1 95 ? 4.658 -14.261 62.601 1.00 23.25 ? 95 ARG A CD 1 ATOM 778 N NE . ARG A 1 95 ? 4.107 -14.518 63.928 1.00 24.51 ? 95 ARG A NE 1 ATOM 779 C CZ . ARG A 1 95 ? 2.948 -15.106 64.155 1.00 23.77 ? 95 ARG A CZ 1 ATOM 780 N NH1 . ARG A 1 95 ? 2.184 -15.560 63.142 1.00 24.10 ? 95 ARG A NH1 1 ATOM 781 N NH2 . ARG A 1 95 ? 2.551 -15.263 65.389 1.00 23.46 ? 95 ARG A NH2 1 ATOM 782 N N . ARG A 1 96 ? 7.999 -17.558 63.357 1.00 26.31 ? 96 ARG A N 1 ATOM 783 C CA . ARG A 1 96 ? 9.027 -17.435 64.353 1.00 28.81 ? 96 ARG A CA 1 ATOM 784 C C . ARG A 1 96 ? 10.386 -17.886 63.767 1.00 26.74 ? 96 ARG A C 1 ATOM 785 O O . ARG A 1 96 ? 11.451 -17.397 64.124 1.00 27.09 ? 96 ARG A O 1 ATOM 786 C CB . ARG A 1 96 ? 8.641 -18.273 65.558 1.00 31.93 ? 96 ARG A CB 1 ATOM 787 C CG . ARG A 1 96 ? 9.369 -17.933 66.851 1.00 43.88 ? 96 ARG A CG 1 ATOM 788 C CD . ARG A 1 96 ? 9.653 -19.173 67.705 1.00 55.56 ? 96 ARG A CD 1 ATOM 789 N NE . ARG A 1 96 ? 10.582 -20.055 66.991 1.00 65.46 ? 96 ARG A NE 1 ATOM 790 C CZ . ARG A 1 96 ? 10.250 -21.220 66.405 1.00 71.92 ? 96 ARG A CZ 1 ATOM 791 N NH1 . ARG A 1 96 ? 8.996 -21.689 66.447 1.00 74.64 ? 96 ARG A NH1 1 ATOM 792 N NH2 . ARG A 1 96 ? 11.186 -21.919 65.765 1.00 74.81 ? 96 ARG A NH2 1 ATOM 793 N N . THR A 1 97 ? 10.340 -18.804 62.831 1.00 24.42 ? 97 THR A N 1 ATOM 794 C CA . THR A 1 97 ? 11.550 -19.299 62.197 1.00 23.04 ? 97 THR A CA 1 ATOM 795 C C . THR A 1 97 ? 12.166 -18.263 61.291 1.00 21.40 ? 97 THR A C 1 ATOM 796 O O . THR A 1 97 ? 13.356 -18.092 61.278 1.00 21.21 ? 97 THR A O 1 ATOM 797 C CB . THR A 1 97 ? 11.221 -20.556 61.368 1.00 23.49 ? 97 THR A CB 1 ATOM 798 O OG1 . THR A 1 97 ? 10.957 -21.647 62.261 1.00 24.55 ? 97 THR A OG1 1 ATOM 799 C CG2 . THR A 1 97 ? 12.380 -20.954 60.481 1.00 22.68 ? 97 THR A CG2 1 ATOM 800 N N . PHE A 1 98 ? 11.348 -17.603 60.483 1.00 20.88 ? 98 PHE A N 1 ATOM 801 C CA . PHE A 1 98 ? 11.821 -16.560 59.574 1.00 20.08 ? 98 PHE A CA 1 ATOM 802 C C . PHE A 1 98 ? 12.458 -15.426 60.369 1.00 19.93 ? 98 PHE A C 1 ATOM 803 O O . PHE A 1 98 ? 13.527 -14.979 60.056 1.00 19.86 ? 98 PHE A O 1 ATOM 804 C CB . PHE A 1 98 ? 10.620 -16.031 58.799 1.00 20.93 ? 98 PHE A CB 1 ATOM 805 C CG . PHE A 1 98 ? 10.875 -14.735 58.031 1.00 17.87 ? 98 PHE A CG 1 ATOM 806 C CD1 . PHE A 1 98 ? 11.733 -14.717 56.949 1.00 16.71 ? 98 PHE A CD1 1 ATOM 807 C CD2 . PHE A 1 98 ? 10.195 -13.599 58.343 1.00 14.23 ? 98 PHE A CD2 1 ATOM 808 C CE1 . PHE A 1 98 ? 11.950 -13.581 56.237 1.00 13.35 ? 98 PHE A CE1 1 ATOM 809 C CE2 . PHE A 1 98 ? 10.419 -12.447 57.642 1.00 14.69 ? 98 PHE A CE2 1 ATOM 810 C CZ . PHE A 1 98 ? 11.317 -12.447 56.583 1.00 13.77 ? 98 PHE A CZ 1 ATOM 811 N N . ILE A 1 99 ? 11.786 -14.991 61.430 1.00 20.14 ? 99 ILE A N 1 ATOM 812 C CA . ILE A 1 99 ? 12.288 -13.929 62.293 1.00 19.16 ? 99 ILE A CA 1 ATOM 813 C C . ILE A 1 99 ? 13.663 -14.250 62.834 1.00 19.06 ? 99 ILE A C 1 ATOM 814 O O . ILE A 1 99 ? 14.562 -13.497 62.683 1.00 19.61 ? 99 ILE A O 1 ATOM 815 C CB . ILE A 1 99 ? 11.336 -13.692 63.435 1.00 19.36 ? 99 ILE A CB 1 ATOM 816 C CG1 . ILE A 1 99 ? 9.971 -13.268 62.908 1.00 19.77 ? 99 ILE A CG1 1 ATOM 817 C CG2 . ILE A 1 99 ? 11.873 -12.637 64.357 1.00 20.58 ? 99 ILE A CG2 1 ATOM 818 C CD1 . ILE A 1 99 ? 8.881 -13.194 64.017 1.00 23.80 ? 99 ILE A CD1 1 ATOM 819 N N . LYS A 1 100 ? 13.836 -15.394 63.447 1.00 20.78 ? 100 LYS A N 1 ATOM 820 C CA . LYS A 1 100 ? 15.128 -15.790 64.030 1.00 22.26 ? 100 LYS A CA 1 ATOM 821 C C . LYS A 1 100 ? 16.228 -15.828 62.983 1.00 21.63 ? 100 LYS A C 1 ATOM 822 O O . LYS A 1 100 ? 17.398 -15.681 63.308 1.00 24.75 ? 100 LYS A O 1 ATOM 823 C CB . LYS A 1 100 ? 15.029 -17.176 64.704 1.00 22.62 ? 100 LYS A CB 1 ATOM 824 C CG . LYS A 1 100 ? 14.096 -17.233 65.906 1.00 29.51 ? 100 LYS A CG 1 ATOM 825 C CD . LYS A 1 100 ? 14.851 -17.223 67.212 1.00 38.79 ? 100 LYS A CD 1 ATOM 826 C CE . LYS A 1 100 ? 15.954 -16.110 67.253 1.00 44.35 ? 100 LYS A CE 1 ATOM 827 N NZ . LYS A 1 100 ? 16.675 -16.028 68.597 1.00 45.44 ? 100 LYS A NZ 1 ATOM 828 N N . SER A 1 101 ? 15.877 -16.006 61.729 1.00 19.20 ? 101 SER A N 1 ATOM 829 C CA . SER A 1 101 ? 16.891 -16.101 60.716 1.00 18.58 ? 101 SER A CA 1 ATOM 830 C C . SER A 1 101 ? 17.380 -14.776 60.268 1.00 17.50 ? 101 SER A C 1 ATOM 831 O O . SER A 1 101 ? 18.430 -14.720 59.654 1.00 18.79 ? 101 SER A O 1 ATOM 832 C CB . SER A 1 101 ? 16.367 -16.864 59.495 1.00 19.84 ? 101 SER A CB 1 ATOM 833 O OG . SER A 1 101 ? 15.554 -16.076 58.640 1.00 20.65 ? 101 SER A OG 1 ATOM 834 N N . VAL A 1 102 ? 16.634 -13.715 60.572 1.00 15.71 ? 102 VAL A N 1 ATOM 835 C CA . VAL A 1 102 ? 16.951 -12.366 60.089 1.00 15.21 ? 102 VAL A CA 1 ATOM 836 C C . VAL A 1 102 ? 18.168 -11.599 60.676 1.00 14.26 ? 102 VAL A C 1 ATOM 837 O O . VAL A 1 102 ? 19.047 -11.172 59.919 1.00 15.13 ? 102 VAL A O 1 ATOM 838 C CB . VAL A 1 102 ? 15.726 -11.469 60.147 1.00 15.47 ? 102 VAL A CB 1 ATOM 839 C CG1 . VAL A 1 102 ? 16.091 -10.041 59.752 1.00 16.25 ? 102 VAL A CG1 1 ATOM 840 C CG2 . VAL A 1 102 ? 14.639 -11.994 59.254 1.00 14.87 ? 102 VAL A CG2 1 ATOM 841 N N . PRO A 1 103 ? 18.236 -11.379 61.985 1.00 12.25 ? 103 PRO A N 1 ATOM 842 C CA . PRO A 1 103 ? 19.367 -10.636 62.560 1.00 12.13 ? 103 PRO A CA 1 ATOM 843 C C . PRO A 1 103 ? 20.785 -11.136 62.126 1.00 13.39 ? 103 PRO A C 1 ATOM 844 O O . PRO A 1 103 ? 21.655 -10.382 61.738 1.00 13.59 ? 103 PRO A O 1 ATOM 845 C CB . PRO A 1 103 ? 19.122 -10.756 64.049 1.00 9.60 ? 103 PRO A CB 1 ATOM 846 C CG . PRO A 1 103 ? 17.675 -10.837 64.139 1.00 9.80 ? 103 PRO A CG 1 ATOM 847 C CD . PRO A 1 103 ? 17.267 -11.749 63.017 1.00 11.04 ? 103 PRO A CD 1 ATOM 848 N N . PRO A 1 104 ? 21.058 -12.425 62.222 1.00 15.15 ? 104 PRO A N 1 ATOM 849 C CA . PRO A 1 104 ? 22.380 -12.866 61.814 1.00 14.89 ? 104 PRO A CA 1 ATOM 850 C C . PRO A 1 104 ? 22.655 -12.578 60.324 1.00 14.38 ? 104 PRO A C 1 ATOM 851 O O . PRO A 1 104 ? 23.779 -12.275 59.971 1.00 13.21 ? 104 PRO A O 1 ATOM 852 C CB . PRO A 1 104 ? 22.355 -14.392 62.173 1.00 13.88 ? 104 PRO A CB 1 ATOM 853 C CG . PRO A 1 104 ? 20.936 -14.778 62.159 1.00 13.00 ? 104 PRO A CG 1 ATOM 854 C CD . PRO A 1 104 ? 20.282 -13.573 62.772 1.00 16.19 ? 104 PRO A CD 1 ATOM 855 N N . PHE A 1 105 ? 21.648 -12.691 59.477 1.00 14.77 ? 105 PHE A N 1 ATOM 856 C CA . PHE A 1 105 ? 21.860 -12.452 58.061 1.00 17.58 ? 105 PHE A CA 1 ATOM 857 C C . PHE A 1 105 ? 22.267 -10.989 57.847 1.00 19.31 ? 105 PHE A C 1 ATOM 858 O O . PHE A 1 105 ? 23.252 -10.675 57.175 1.00 20.42 ? 105 PHE A O 1 ATOM 859 C CB . PHE A 1 105 ? 20.593 -12.742 57.259 1.00 18.15 ? 105 PHE A CB 1 ATOM 860 C CG . PHE A 1 105 ? 20.828 -12.833 55.758 1.00 18.43 ? 105 PHE A CG 1 ATOM 861 C CD1 . PHE A 1 105 ? 21.219 -14.022 55.177 1.00 16.73 ? 105 PHE A CD1 1 ATOM 862 C CD2 . PHE A 1 105 ? 20.626 -11.728 54.948 1.00 20.62 ? 105 PHE A CD2 1 ATOM 863 C CE1 . PHE A 1 105 ? 21.420 -14.100 53.805 1.00 15.88 ? 105 PHE A CE1 1 ATOM 864 C CE2 . PHE A 1 105 ? 20.827 -11.801 53.581 1.00 20.88 ? 105 PHE A CE2 1 ATOM 865 C CZ . PHE A 1 105 ? 21.254 -12.995 53.016 1.00 18.09 ? 105 PHE A CZ 1 ATOM 866 N N . LEU A 1 106 ? 21.474 -10.090 58.414 1.00 19.54 ? 106 LEU A N 1 ATOM 867 C CA . LEU A 1 106 ? 21.750 -8.667 58.362 1.00 18.29 ? 106 LEU A CA 1 ATOM 868 C C . LEU A 1 106 ? 23.160 -8.406 58.903 1.00 16.57 ? 106 LEU A C 1 ATOM 869 O O . LEU A 1 106 ? 23.921 -7.689 58.327 1.00 19.19 ? 106 LEU A O 1 ATOM 870 C CB . LEU A 1 106 ? 20.709 -7.878 59.191 1.00 17.56 ? 106 LEU A CB 1 ATOM 871 C CG . LEU A 1 106 ? 19.556 -7.290 58.413 1.00 20.01 ? 106 LEU A CG 1 ATOM 872 C CD1 . LEU A 1 106 ? 19.081 -8.236 57.315 1.00 21.33 ? 106 LEU A CD1 1 ATOM 873 C CD2 . LEU A 1 106 ? 18.428 -6.923 59.316 1.00 23.62 ? 106 LEU A CD2 1 ATOM 874 N N . ARG A 1 107 ? 23.497 -8.981 60.021 1.00 15.51 ? 107 ARG A N 1 ATOM 875 C CA . ARG A 1 107 ? 24.803 -8.752 60.624 1.00 17.06 ? 107 ARG A CA 1 ATOM 876 C C . ARG A 1 107 ? 25.983 -9.267 59.751 1.00 16.79 ? 107 ARG A C 1 ATOM 877 O O . ARG A 1 107 ? 27.003 -8.627 59.574 1.00 15.52 ? 107 ARG A O 1 ATOM 878 C CB . ARG A 1 107 ? 24.846 -9.415 62.010 1.00 17.23 ? 107 ARG A CB 1 ATOM 879 C CG . ARG A 1 107 ? 24.853 -8.455 63.182 1.00 16.61 ? 107 ARG A CG 1 ATOM 880 C CD . ARG A 1 107 ? 23.549 -7.771 63.466 1.00 15.11 ? 107 ARG A CD 1 ATOM 881 N NE . ARG A 1 107 ? 23.740 -6.362 63.788 1.00 15.11 ? 107 ARG A NE 1 ATOM 882 C CZ . ARG A 1 107 ? 23.206 -5.742 64.821 1.00 15.36 ? 107 ARG A CZ 1 ATOM 883 N NH1 . ARG A 1 107 ? 22.471 -6.376 65.682 1.00 20.48 ? 107 ARG A NH1 1 ATOM 884 N NH2 . ARG A 1 107 ? 23.403 -4.471 65.007 1.00 15.91 ? 107 ARG A NH2 1 ATOM 885 N N . THR A 1 108 ? 25.833 -10.446 59.214 1.00 17.24 ? 108 THR A N 1 ATOM 886 C CA . THR A 1 108 ? 26.872 -11.010 58.379 1.00 16.80 ? 108 THR A CA 1 ATOM 887 C C . THR A 1 108 ? 27.166 -10.056 57.226 1.00 16.79 ? 108 THR A C 1 ATOM 888 O O . THR A 1 108 ? 28.316 -9.772 56.956 1.00 18.33 ? 108 THR A O 1 ATOM 889 C CB . THR A 1 108 ? 26.464 -12.371 57.790 1.00 15.69 ? 108 THR A CB 1 ATOM 890 O OG1 . THR A 1 108 ? 26.118 -13.271 58.843 1.00 15.58 ? 108 THR A OG1 1 ATOM 891 C CG2 . THR A 1 108 ? 27.598 -12.954 57.023 1.00 14.80 ? 108 THR A CG2 1 ATOM 892 N N . HIS A 1 109 ? 26.129 -9.559 56.563 1.00 15.53 ? 109 HIS A N 1 ATOM 893 C CA . HIS A 1 109 ? 26.301 -8.691 55.404 1.00 15.40 ? 109 HIS A CA 1 ATOM 894 C C . HIS A 1 109 ? 26.340 -7.191 55.668 1.00 15.00 ? 109 HIS A C 1 ATOM 895 O O . HIS A 1 109 ? 26.324 -6.387 54.742 1.00 16.82 ? 109 HIS A O 1 ATOM 896 C CB . HIS A 1 109 ? 25.245 -9.038 54.378 1.00 15.72 ? 109 HIS A CB 1 ATOM 897 C CG . HIS A 1 109 ? 25.355 -10.444 53.897 1.00 19.10 ? 109 HIS A CG 1 ATOM 898 N ND1 . HIS A 1 109 ? 26.488 -10.924 53.277 1.00 18.72 ? 109 HIS A ND1 1 ATOM 899 C CD2 . HIS A 1 109 ? 24.511 -11.490 54.014 1.00 21.87 ? 109 HIS A CD2 1 ATOM 900 C CE1 . HIS A 1 109 ? 26.339 -12.207 53.045 1.00 21.20 ? 109 HIS A CE1 1 ATOM 901 N NE2 . HIS A 1 109 ? 25.147 -12.573 53.472 1.00 24.37 ? 109 HIS A NE2 1 ATOM 902 N N . GLY A 1 110 ? 26.369 -6.818 56.937 1.00 13.90 ? 110 GLY A N 1 ATOM 903 C CA . GLY A 1 110 ? 26.490 -5.439 57.330 1.00 12.50 ? 110 GLY A CA 1 ATOM 904 C C . GLY A 1 110 ? 25.351 -4.514 57.149 1.00 13.19 ? 110 GLY A C 1 ATOM 905 O O . GLY A 1 110 ? 25.577 -3.323 56.970 1.00 15.17 ? 110 GLY A O 1 ATOM 906 N N . PHE A 1 111 ? 24.125 -4.996 57.219 1.00 13.29 ? 111 PHE A N 1 ATOM 907 C CA . PHE A 1 111 ? 22.949 -4.100 57.080 1.00 12.44 ? 111 PHE A CA 1 ATOM 908 C C . PHE A 1 111 ? 22.551 -3.544 58.432 1.00 12.70 ? 111 PHE A C 1 ATOM 909 O O . PHE A 1 111 ? 22.726 -4.188 59.443 1.00 14.60 ? 111 PHE A O 1 ATOM 910 C CB . PHE A 1 111 ? 21.790 -4.843 56.447 1.00 10.35 ? 111 PHE A CB 1 ATOM 911 C CG . PHE A 1 111 ? 21.913 -4.965 54.966 1.00 10.68 ? 111 PHE A CG 1 ATOM 912 C CD1 . PHE A 1 111 ? 21.606 -3.897 54.161 1.00 8.52 ? 111 PHE A CD1 1 ATOM 913 C CD2 . PHE A 1 111 ? 22.389 -6.118 54.373 1.00 10.53 ? 111 PHE A CD2 1 ATOM 914 C CE1 . PHE A 1 111 ? 21.711 -3.984 52.779 1.00 4.82 ? 111 PHE A CE1 1 ATOM 915 C CE2 . PHE A 1 111 ? 22.554 -6.179 52.983 1.00 7.47 ? 111 PHE A CE2 1 ATOM 916 C CZ . PHE A 1 111 ? 22.187 -5.110 52.192 1.00 4.54 ? 111 PHE A CZ 1 ATOM 917 N N . ASP A 1 112 ? 22.005 -2.354 58.446 1.00 13.19 ? 112 ASP A N 1 ATOM 918 C CA . ASP A 1 112 ? 21.617 -1.705 59.683 1.00 13.61 ? 112 ASP A CA 1 ATOM 919 C C . ASP A 1 112 ? 20.137 -1.933 59.980 1.00 14.07 ? 112 ASP A C 1 ATOM 920 O O . ASP A 1 112 ? 19.580 -1.366 60.932 1.00 16.34 ? 112 ASP A O 1 ATOM 921 C CB . ASP A 1 112 ? 21.958 -0.217 59.619 1.00 12.56 ? 112 ASP A CB 1 ATOM 922 C CG . ASP A 1 112 ? 23.334 0.026 59.168 1.00 13.25 ? 112 ASP A CG 1 ATOM 923 O OD1 . ASP A 1 112 ? 24.200 0.017 60.043 1.00 18.84 ? 112 ASP A OD1 1 ATOM 924 O OD2 . ASP A 1 112 ? 23.632 0.210 57.948 1.00 14.65 ? 112 ASP A OD2 1 ATOM 925 N N . GLY A 1 113 ? 19.503 -2.781 59.200 1.00 13.49 ? 113 GLY A N 1 ATOM 926 C CA . GLY A 1 113 ? 18.097 -3.035 59.417 1.00 12.97 ? 113 GLY A CA 1 ATOM 927 C C . GLY A 1 113 ? 17.414 -3.710 58.237 1.00 13.99 ? 113 GLY A C 1 ATOM 928 O O . GLY A 1 113 ? 17.948 -3.866 57.114 1.00 12.54 ? 113 GLY A O 1 ATOM 929 N N . LEU A 1 114 ? 16.177 -4.106 58.501 1.00 14.84 ? 114 LEU A N 1 ATOM 930 C CA . LEU A 1 114 ? 15.346 -4.792 57.520 1.00 14.53 ? 114 LEU A CA 1 ATOM 931 C C . LEU A 1 114 ? 14.133 -3.995 57.145 1.00 14.29 ? 114 LEU A C 1 ATOM 932 O O . LEU A 1 114 ? 13.631 -3.235 57.947 1.00 15.09 ? 114 LEU A O 1 ATOM 933 C CB . LEU A 1 114 ? 14.887 -6.129 58.095 1.00 14.51 ? 114 LEU A CB 1 ATOM 934 C CG . LEU A 1 114 ? 13.871 -6.901 57.274 1.00 11.84 ? 114 LEU A CG 1 ATOM 935 C CD1 . LEU A 1 114 ? 14.602 -7.864 56.435 1.00 11.19 ? 114 LEU A CD1 1 ATOM 936 C CD2 . LEU A 1 114 ? 12.941 -7.615 58.193 1.00 9.36 ? 114 LEU A CD2 1 ATOM 937 N N . ASP A 1 115 ? 13.671 -4.178 55.912 1.00 15.02 ? 115 ASP A N 1 ATOM 938 C CA . ASP A 1 115 ? 12.477 -3.498 55.395 1.00 15.41 ? 115 ASP A CA 1 ATOM 939 C C . ASP A 1 115 ? 11.456 -4.501 54.827 1.00 14.49 ? 115 ASP A C 1 ATOM 940 O O . ASP A 1 115 ? 11.792 -5.394 54.047 1.00 13.56 ? 115 ASP A O 1 ATOM 941 C CB . ASP A 1 115 ? 12.882 -2.468 54.320 1.00 14.87 ? 115 ASP A CB 1 ATOM 942 C CG . ASP A 1 115 ? 11.678 -1.745 53.699 1.00 16.68 ? 115 ASP A CG 1 ATOM 943 O OD1 . ASP A 1 115 ? 10.953 -1.043 54.449 1.00 16.30 ? 115 ASP A OD1 1 ATOM 944 O OD2 . ASP A 1 115 ? 11.438 -1.867 52.476 1.00 15.29 ? 115 ASP A OD2 1 ATOM 945 N N . LEU A 1 116 ? 10.204 -4.339 55.215 1.00 14.85 ? 116 LEU A N 1 ATOM 946 C CA . LEU A 1 116 ? 9.141 -5.237 54.752 1.00 15.54 ? 116 LEU A CA 1 ATOM 947 C C . LEU A 1 116 ? 8.334 -4.669 53.592 1.00 17.15 ? 116 LEU A C 1 ATOM 948 O O . LEU A 1 116 ? 7.593 -3.684 53.743 1.00 18.42 ? 116 LEU A O 1 ATOM 949 C CB . LEU A 1 116 ? 8.184 -5.553 55.893 1.00 15.55 ? 116 LEU A CB 1 ATOM 950 C CG . LEU A 1 116 ? 8.836 -6.184 57.106 1.00 16.59 ? 116 LEU A CG 1 ATOM 951 C CD1 . LEU A 1 116 ? 7.881 -6.211 58.235 1.00 17.79 ? 116 LEU A CD1 1 ATOM 952 C CD2 . LEU A 1 116 ? 9.282 -7.583 56.797 1.00 22.50 ? 116 LEU A CD2 1 ATOM 953 N N . ALA A 1 117 ? 8.446 -5.307 52.435 1.00 17.69 ? 117 ALA A N 1 ATOM 954 C CA . ALA A 1 117 ? 7.707 -4.890 51.248 1.00 17.71 ? 117 ALA A CA 1 ATOM 955 C C . ALA A 1 117 ? 6.688 -5.952 50.846 1.00 18.36 ? 117 ALA A C 1 ATOM 956 O O . ALA A 1 117 ? 6.684 -6.423 49.717 1.00 17.98 ? 117 ALA A O 1 ATOM 957 C CB . ALA A 1 117 ? 8.648 -4.652 50.117 1.00 17.98 ? 117 ALA A CB 1 ATOM 958 N N . TRP A 1 118 ? 5.844 -6.337 51.803 1.00 18.96 ? 118 TRP A N 1 ATOM 959 C CA . TRP A 1 118 ? 4.762 -7.283 51.574 1.00 18.71 ? 118 TRP A CA 1 ATOM 960 C C . TRP A 1 118 ? 3.806 -6.507 50.702 1.00 20.62 ? 118 TRP A C 1 ATOM 961 O O . TRP A 1 118 ? 3.016 -5.646 51.184 1.00 19.85 ? 118 TRP A O 1 ATOM 962 C CB . TRP A 1 118 ? 4.033 -7.649 52.868 1.00 18.20 ? 118 TRP A CB 1 ATOM 963 C CG . TRP A 1 118 ? 2.932 -8.631 52.740 1.00 15.83 ? 118 TRP A CG 1 ATOM 964 C CD1 . TRP A 1 118 ? 2.240 -8.931 51.641 1.00 16.40 ? 118 TRP A CD1 1 ATOM 965 C CD2 . TRP A 1 118 ? 2.377 -9.417 53.790 1.00 15.45 ? 118 TRP A CD2 1 ATOM 966 N NE1 . TRP A 1 118 ? 1.274 -9.861 51.933 1.00 18.81 ? 118 TRP A NE1 1 ATOM 967 C CE2 . TRP A 1 118 ? 1.362 -10.169 53.260 1.00 15.89 ? 118 TRP A CE2 1 ATOM 968 C CE3 . TRP A 1 118 ? 2.638 -9.543 55.159 1.00 16.65 ? 118 TRP A CE3 1 ATOM 969 C CZ2 . TRP A 1 118 ? 0.626 -11.039 54.032 1.00 15.00 ? 118 TRP A CZ2 1 ATOM 970 C CZ3 . TRP A 1 118 ? 1.921 -10.433 55.895 1.00 16.10 ? 118 TRP A CZ3 1 ATOM 971 C CH2 . TRP A 1 118 ? 0.928 -11.150 55.351 1.00 11.19 ? 118 TRP A CH2 1 ATOM 972 N N . LEU A 1 119 ? 3.833 -6.801 49.405 1.00 21.36 ? 119 LEU A N 1 ATOM 973 C CA . LEU A 1 119 ? 2.975 -6.024 48.551 1.00 20.41 ? 119 LEU A CA 1 ATOM 974 C C . LEU A 1 119 ? 1.536 -6.466 48.485 1.00 19.91 ? 119 LEU A C 1 ATOM 975 O O . LEU A 1 119 ? 1.119 -7.250 47.672 1.00 17.08 ? 119 LEU A O 1 ATOM 976 C CB . LEU A 1 119 ? 3.642 -5.831 47.222 1.00 20.49 ? 119 LEU A CB 1 ATOM 977 C CG . LEU A 1 119 ? 4.641 -4.680 47.343 1.00 16.84 ? 119 LEU A CG 1 ATOM 978 C CD1 . LEU A 1 119 ? 5.070 -4.212 45.964 1.00 17.81 ? 119 LEU A CD1 1 ATOM 979 C CD2 . LEU A 1 119 ? 4.042 -3.538 48.156 1.00 9.93 ? 119 LEU A CD2 1 ATOM 980 N N . TYR A 1 120 ? 0.828 -5.854 49.425 1.00 21.36 ? 120 TYR A N 1 ATOM 981 C CA . TYR A 1 120 ? -0.592 -5.927 49.652 1.00 20.68 ? 120 TYR A CA 1 ATOM 982 C C . TYR A 1 120 ? -1.119 -7.102 50.422 1.00 20.15 ? 120 TYR A C 1 ATOM 983 O O . TYR A 1 120 ? -1.267 -8.165 49.890 1.00 21.91 ? 120 TYR A O 1 ATOM 984 C CB . TYR A 1 120 ? -1.293 -5.682 48.352 1.00 20.93 ? 120 TYR A CB 1 ATOM 985 C CG . TYR A 1 120 ? -0.717 -4.439 47.699 1.00 23.04 ? 120 TYR A CG 1 ATOM 986 C CD1 . TYR A 1 120 ? -0.176 -3.441 48.465 1.00 24.98 ? 120 TYR A CD1 1 ATOM 987 C CD2 . TYR A 1 120 ? -0.678 -4.288 46.303 1.00 27.11 ? 120 TYR A CD2 1 ATOM 988 C CE1 . TYR A 1 120 ? 0.427 -2.327 47.875 1.00 29.91 ? 120 TYR A CE1 1 ATOM 989 C CE2 . TYR A 1 120 ? -0.099 -3.186 45.704 1.00 28.61 ? 120 TYR A CE2 1 ATOM 990 C CZ . TYR A 1 120 ? 0.455 -2.202 46.489 1.00 31.16 ? 120 TYR A CZ 1 ATOM 991 O OH . TYR A 1 120 ? 1.027 -1.071 45.911 1.00 31.20 ? 120 TYR A OH 1 ATOM 992 N N . PRO A 1 121 ? -1.339 -6.911 51.709 1.00 19.46 ? 121 PRO A N 1 ATOM 993 C CA . PRO A 1 121 ? -1.915 -7.858 52.639 1.00 20.72 ? 121 PRO A CA 1 ATOM 994 C C . PRO A 1 121 ? -3.432 -7.778 52.447 1.00 21.54 ? 121 PRO A C 1 ATOM 995 O O . PRO A 1 121 ? -3.933 -6.727 52.078 1.00 21.91 ? 121 PRO A O 1 ATOM 996 C CB . PRO A 1 121 ? -1.531 -7.291 53.991 1.00 20.92 ? 121 PRO A CB 1 ATOM 997 C CG . PRO A 1 121 ? -0.425 -6.352 53.666 1.00 20.90 ? 121 PRO A CG 1 ATOM 998 C CD . PRO A 1 121 ? -0.846 -5.762 52.422 1.00 20.37 ? 121 PRO A CD 1 ATOM 999 N N . GLY A 1 122 ? -4.146 -8.873 52.646 1.00 21.45 ? 122 GLY A N 1 ATOM 1000 C CA . GLY A 1 122 ? -5.555 -8.822 52.433 1.00 23.07 ? 122 GLY A CA 1 ATOM 1001 C C . GLY A 1 122 ? -6.359 -8.792 53.697 1.00 23.94 ? 122 GLY A C 1 ATOM 1002 O O . GLY A 1 122 ? -5.824 -8.763 54.802 1.00 24.91 ? 122 GLY A O 1 ATOM 1003 N N . ARG A 1 123 ? -7.668 -8.798 53.520 1.00 24.82 ? 123 ARG A N 1 ATOM 1004 C CA . ARG A 1 123 ? -8.595 -8.818 54.627 1.00 25.83 ? 123 ARG A CA 1 ATOM 1005 C C . ARG A 1 123 ? -8.181 -9.869 55.625 1.00 24.84 ? 123 ARG A C 1 ATOM 1006 O O . ARG A 1 123 ? -8.151 -9.597 56.797 1.00 24.24 ? 123 ARG A O 1 ATOM 1007 C CB . ARG A 1 123 ? -9.982 -9.169 54.111 1.00 28.48 ? 123 ARG A CB 1 ATOM 1008 C CG . ARG A 1 123 ? -11.135 -8.495 54.798 1.00 36.14 ? 123 ARG A CG 1 ATOM 1009 C CD . ARG A 1 123 ? -12.429 -9.175 54.387 1.00 43.69 ? 123 ARG A CD 1 ATOM 1010 N NE . ARG A 1 123 ? -12.455 -10.548 54.904 1.00 50.49 ? 123 ARG A NE 1 ATOM 1011 C CZ . ARG A 1 123 ? -13.030 -11.585 54.292 1.00 53.31 ? 123 ARG A CZ 1 ATOM 1012 N NH1 . ARG A 1 123 ? -13.628 -11.425 53.107 1.00 56.90 ? 123 ARG A NH1 1 ATOM 1013 N NH2 . ARG A 1 123 ? -12.991 -12.791 54.852 1.00 52.17 ? 123 ARG A NH2 1 ATOM 1014 N N . ARG A 1 124 ? -7.813 -11.055 55.134 1.00 25.58 ? 124 ARG A N 1 ATOM 1015 C CA . ARG A 1 124 ? -7.392 -12.170 55.985 1.00 25.19 ? 124 ARG A CA 1 ATOM 1016 C C . ARG A 1 124 ? -5.965 -12.091 56.457 1.00 24.75 ? 124 ARG A C 1 ATOM 1017 O O . ARG A 1 124 ? -5.487 -13.040 57.019 1.00 26.08 ? 124 ARG A O 1 ATOM 1018 C CB . ARG A 1 124 ? -7.539 -13.506 55.247 1.00 27.17 ? 124 ARG A CB 1 ATOM 1019 C CG . ARG A 1 124 ? -8.965 -13.888 54.875 1.00 29.80 ? 124 ARG A CG 1 ATOM 1020 C CD . ARG A 1 124 ? -9.039 -15.283 54.237 1.00 27.28 ? 124 ARG A CD 1 ATOM 1021 N NE . ARG A 1 124 ? -10.349 -15.618 53.770 1.00 31.60 ? 124 ARG A NE 1 ATOM 1022 C CZ . ARG A 1 124 ? -10.860 -15.267 52.594 1.00 34.39 ? 124 ARG A CZ 1 ATOM 1023 N NH1 . ARG A 1 124 ? -10.108 -14.578 51.747 1.00 38.74 ? 124 ARG A NH1 1 ATOM 1024 N NH2 . ARG A 1 124 ? -12.119 -15.569 52.261 1.00 32.78 ? 124 ARG A NH2 1 ATOM 1025 N N . ASP A 1 125 ? -5.258 -10.986 56.253 1.00 23.65 ? 125 ASP A N 1 ATOM 1026 C CA . ASP A 1 125 ? -3.877 -10.916 56.682 1.00 20.51 ? 125 ASP A CA 1 ATOM 1027 C C . ASP A 1 125 ? -3.574 -9.860 57.691 1.00 21.59 ? 125 ASP A C 1 ATOM 1028 O O . ASP A 1 125 ? -2.535 -9.922 58.305 1.00 19.76 ? 125 ASP A O 1 ATOM 1029 C CB . ASP A 1 125 ? -3.056 -10.711 55.450 1.00 19.88 ? 125 ASP A CB 1 ATOM 1030 C CG . ASP A 1 125 ? -3.074 -11.907 54.556 1.00 17.83 ? 125 ASP A CG 1 ATOM 1031 O OD1 . ASP A 1 125 ? -2.694 -13.018 55.026 1.00 18.01 ? 125 ASP A OD1 1 ATOM 1032 O OD2 . ASP A 1 125 ? -3.422 -11.766 53.369 1.00 16.52 ? 125 ASP A OD2 1 ATOM 1033 N N . LYS A 1 126 ? -4.490 -8.883 57.853 1.00 23.80 ? 126 LYS A N 1 ATOM 1034 C CA . LYS A 1 126 ? -4.348 -7.736 58.766 1.00 24.49 ? 126 LYS A CA 1 ATOM 1035 C C . LYS A 1 126 ? -3.777 -8.179 60.110 1.00 24.15 ? 126 LYS A C 1 ATOM 1036 O O . LYS A 1 126 ? -2.786 -7.639 60.545 1.00 25.00 ? 126 LYS A O 1 ATOM 1037 C CB . LYS A 1 126 ? -5.680 -6.995 58.929 1.00 25.06 ? 126 LYS A CB 1 ATOM 1038 C CG . LYS A 1 126 ? -5.650 -5.816 59.912 1.00 30.68 ? 126 LYS A CG 1 ATOM 1039 C CD . LYS A 1 126 ? -6.945 -5.036 59.957 1.00 36.27 ? 126 LYS A CD 1 ATOM 1040 C CE . LYS A 1 126 ? -7.310 -4.481 58.587 1.00 41.74 ? 126 LYS A CE 1 ATOM 1041 N NZ . LYS A 1 126 ? -8.324 -3.364 58.665 1.00 44.17 ? 126 LYS A NZ 1 ATOM 1042 N N . ARG A 1 127 ? -4.372 -9.175 60.740 1.00 23.63 ? 127 ARG A N 1 ATOM 1043 C CA . ARG A 1 127 ? -3.948 -9.647 62.045 1.00 23.94 ? 127 ARG A CA 1 ATOM 1044 C C . ARG A 1 127 ? -2.547 -10.222 62.069 1.00 23.52 ? 127 ARG A C 1 ATOM 1045 O O . ARG A 1 127 ? -1.821 -10.047 63.011 1.00 25.03 ? 127 ARG A O 1 ATOM 1046 C CB . ARG A 1 127 ? -4.904 -10.707 62.518 1.00 26.76 ? 127 ARG A CB 1 ATOM 1047 C CG . ARG A 1 127 ? -5.079 -10.781 64.007 1.00 34.35 ? 127 ARG A CG 1 ATOM 1048 C CD . ARG A 1 127 ? -4.966 -12.222 64.519 1.00 43.56 ? 127 ARG A CD 1 ATOM 1049 N NE . ARG A 1 127 ? -5.690 -13.168 63.665 1.00 49.90 ? 127 ARG A NE 1 ATOM 1050 C CZ . ARG A 1 127 ? -5.777 -14.484 63.895 1.00 55.29 ? 127 ARG A CZ 1 ATOM 1051 N NH1 . ARG A 1 127 ? -5.172 -15.036 64.947 1.00 56.57 ? 127 ARG A NH1 1 ATOM 1052 N NH2 . ARG A 1 127 ? -6.486 -15.251 63.072 1.00 58.04 ? 127 ARG A NH2 1 ATOM 1053 N N . HIS A 1 128 ? -2.141 -10.939 61.042 1.00 23.69 ? 128 HIS A N 1 ATOM 1054 C CA . HIS A 1 128 ? -0.809 -11.538 60.998 1.00 22.11 ? 128 HIS A CA 1 ATOM 1055 C C . HIS A 1 128 ? 0.292 -10.530 60.644 1.00 20.32 ? 128 HIS A C 1 ATOM 1056 O O . HIS A 1 128 ? 1.422 -10.668 61.091 1.00 20.57 ? 128 HIS A O 1 ATOM 1057 C CB . HIS A 1 128 ? -0.815 -12.715 60.024 1.00 22.53 ? 128 HIS A CB 1 ATOM 1058 C CG . HIS A 1 128 ? -1.920 -13.670 60.295 1.00 27.36 ? 128 HIS A CG 1 ATOM 1059 N ND1 . HIS A 1 128 ? -2.269 -14.037 61.572 1.00 31.43 ? 128 HIS A ND1 1 ATOM 1060 C CD2 . HIS A 1 128 ? -2.811 -14.278 59.475 1.00 31.93 ? 128 HIS A CD2 1 ATOM 1061 C CE1 . HIS A 1 128 ? -3.306 -14.855 61.530 1.00 30.63 ? 128 HIS A CE1 1 ATOM 1062 N NE2 . HIS A 1 128 ? -3.655 -15.015 60.267 1.00 31.42 ? 128 HIS A NE2 1 ATOM 1063 N N . LEU A 1 129 ? -0.046 -9.518 59.841 1.00 17.42 ? 129 LEU A N 1 ATOM 1064 C CA . LEU A 1 129 ? 0.915 -8.512 59.504 1.00 14.08 ? 129 LEU A CA 1 ATOM 1065 C C . LEU A 1 129 ? 1.289 -7.972 60.864 1.00 12.64 ? 129 LEU A C 1 ATOM 1066 O O . LEU A 1 129 ? 2.441 -7.877 61.189 1.00 14.36 ? 129 LEU A O 1 ATOM 1067 C CB . LEU A 1 129 ? 0.311 -7.419 58.658 1.00 13.44 ? 129 LEU A CB 1 ATOM 1068 C CG . LEU A 1 129 ? 1.253 -6.699 57.670 1.00 11.38 ? 129 LEU A CG 1 ATOM 1069 C CD1 . LEU A 1 129 ? 0.630 -5.407 57.205 1.00 10.54 ? 129 LEU A CD1 1 ATOM 1070 C CD2 . LEU A 1 129 ? 2.552 -6.377 58.277 1.00 9.21 ? 129 LEU A CD2 1 ATOM 1071 N N . THR A 1 130 ? 0.301 -7.680 61.682 1.00 10.54 ? 130 THR A N 1 ATOM 1072 C CA . THR A 1 130 ? 0.532 -7.156 63.005 1.00 9.84 ? 130 THR A CA 1 ATOM 1073 C C . THR A 1 130 ? 1.393 -8.048 63.832 1.00 10.35 ? 130 THR A C 1 ATOM 1074 O O . THR A 1 130 ? 2.322 -7.624 64.475 1.00 12.56 ? 130 THR A O 1 ATOM 1075 C CB . THR A 1 130 ? -0.754 -6.921 63.729 1.00 8.09 ? 130 THR A CB 1 ATOM 1076 O OG1 . THR A 1 130 ? -1.680 -6.157 62.935 1.00 7.99 ? 130 THR A OG1 1 ATOM 1077 C CG2 . THR A 1 130 ? -0.519 -6.074 64.940 1.00 9.47 ? 130 THR A CG2 1 ATOM 1078 N N . ALA A 1 131 ? 1.121 -9.317 63.805 1.00 12.06 ? 131 ALA A N 1 ATOM 1079 C CA . ALA A 1 131 ? 1.920 -10.265 64.608 1.00 13.05 ? 131 ALA A CA 1 ATOM 1080 C C . ALA A 1 131 ? 3.362 -10.231 64.212 1.00 12.07 ? 131 ALA A C 1 ATOM 1081 O O . ALA A 1 131 ? 4.248 -10.146 65.031 1.00 11.16 ? 131 ALA A O 1 ATOM 1082 C CB . ALA A 1 131 ? 1.381 -11.685 64.435 1.00 14.16 ? 131 ALA A CB 1 ATOM 1083 N N . LEU A 1 132 ? 3.566 -10.282 62.914 1.00 12.54 ? 132 LEU A N 1 ATOM 1084 C CA . LEU A 1 132 ? 4.899 -10.273 62.294 1.00 12.63 ? 132 LEU A CA 1 ATOM 1085 C C . LEU A 1 132 ? 5.759 -9.042 62.607 1.00 12.24 ? 132 LEU A C 1 ATOM 1086 O O . LEU A 1 132 ? 6.973 -9.141 62.807 1.00 8.70 ? 132 LEU A O 1 ATOM 1087 C CB . LEU A 1 132 ? 4.751 -10.401 60.784 1.00 12.37 ? 132 LEU A CB 1 ATOM 1088 C CG . LEU A 1 132 ? 6.009 -10.368 59.938 1.00 10.81 ? 132 LEU A CG 1 ATOM 1089 C CD1 . LEU A 1 132 ? 6.942 -11.419 60.381 1.00 9.99 ? 132 LEU A CD1 1 ATOM 1090 C CD2 . LEU A 1 132 ? 5.633 -10.599 58.488 1.00 10.95 ? 132 LEU A CD2 1 ATOM 1091 N N . VAL A 1 133 ? 5.118 -7.879 62.634 1.00 12.80 ? 133 VAL A N 1 ATOM 1092 C CA . VAL A 1 133 ? 5.859 -6.651 62.906 1.00 13.69 ? 133 VAL A CA 1 ATOM 1093 C C . VAL A 1 133 ? 6.250 -6.641 64.374 1.00 14.09 ? 133 VAL A C 1 ATOM 1094 O O . VAL A 1 133 ? 7.421 -6.415 64.765 1.00 11.72 ? 133 VAL A O 1 ATOM 1095 C CB . VAL A 1 133 ? 5.044 -5.402 62.590 1.00 12.78 ? 133 VAL A CB 1 ATOM 1096 C CG1 . VAL A 1 133 ? 5.880 -4.136 62.825 1.00 16.13 ? 133 VAL A CG1 1 ATOM 1097 C CG2 . VAL A 1 133 ? 4.600 -5.407 61.151 1.00 12.29 ? 133 VAL A CG2 1 ATOM 1098 N N . LYS A 1 134 ? 5.228 -6.876 65.176 1.00 15.78 ? 134 LYS A N 1 ATOM 1099 C CA . LYS A 1 134 ? 5.369 -6.898 66.618 1.00 16.88 ? 134 LYS A CA 1 ATOM 1100 C C . LYS A 1 134 ? 6.497 -7.854 66.981 1.00 17.25 ? 134 LYS A C 1 ATOM 1101 O O . LYS A 1 134 ? 7.510 -7.460 67.524 1.00 17.09 ? 134 LYS A O 1 ATOM 1102 C CB . LYS A 1 134 ? 4.048 -7.330 67.242 1.00 16.92 ? 134 LYS A CB 1 ATOM 1103 C CG . LYS A 1 134 ? 3.916 -6.936 68.682 1.00 22.20 ? 134 LYS A CG 1 ATOM 1104 C CD . LYS A 1 134 ? 2.732 -7.607 69.390 1.00 28.81 ? 134 LYS A CD 1 ATOM 1105 C CE . LYS A 1 134 ? 1.422 -6.874 69.184 1.00 34.53 ? 134 LYS A CE 1 ATOM 1106 N NZ . LYS A 1 134 ? 0.245 -7.573 69.852 1.00 35.73 ? 134 LYS A NZ 1 ATOM 1107 N N . GLU A 1 135 ? 6.340 -9.122 66.638 1.00 17.83 ? 135 GLU A N 1 ATOM 1108 C CA . GLU A 1 135 ? 7.333 -10.140 66.982 1.00 17.59 ? 135 GLU A CA 1 ATOM 1109 C C . GLU A 1 135 ? 8.711 -9.884 66.445 1.00 16.64 ? 135 GLU A C 1 ATOM 1110 O O . GLU A 1 135 ? 9.677 -10.150 67.096 1.00 17.12 ? 135 GLU A O 1 ATOM 1111 C CB . GLU A 1 135 ? 6.839 -11.483 66.491 1.00 18.62 ? 135 GLU A CB 1 ATOM 1112 C CG . GLU A 1 135 ? 5.957 -12.209 67.493 1.00 22.11 ? 135 GLU A CG 1 ATOM 1113 C CD . GLU A 1 135 ? 5.176 -13.339 66.857 1.00 26.10 ? 135 GLU A CD 1 ATOM 1114 O OE1 . GLU A 1 135 ? 5.732 -13.955 65.919 1.00 31.71 ? 135 GLU A OE1 1 ATOM 1115 O OE2 . GLU A 1 135 ? 4.025 -13.608 67.289 1.00 26.79 ? 135 GLU A OE2 1 ATOM 1116 N N . MET A 1 136 ? 8.779 -9.391 65.224 1.00 16.43 ? 136 MET A N 1 ATOM 1117 C CA . MET A 1 136 ? 10.058 -9.080 64.555 1.00 14.77 ? 136 MET A CA 1 ATOM 1118 C C . MET A 1 136 ? 10.771 -7.994 65.333 1.00 14.38 ? 136 MET A C 1 ATOM 1119 O O . MET A 1 136 ? 11.949 -8.087 65.588 1.00 14.62 ? 136 MET A O 1 ATOM 1120 C CB . MET A 1 136 ? 9.814 -8.591 63.116 1.00 14.02 ? 136 MET A CB 1 ATOM 1121 C CG . MET A 1 136 ? 11.056 -8.254 62.353 1.00 9.98 ? 136 MET A CG 1 ATOM 1122 S SD . MET A 1 136 ? 11.976 -9.711 61.821 1.00 11.74 ? 136 MET A SD 1 ATOM 1123 C CE . MET A 1 136 ? 11.144 -10.135 60.346 1.00 13.50 ? 136 MET A CE 1 ATOM 1124 N N . LYS A 1 137 ? 10.050 -6.956 65.705 1.00 14.53 ? 137 LYS A N 1 ATOM 1125 C CA . LYS A 1 137 ? 10.653 -5.850 66.464 1.00 15.18 ? 137 LYS A CA 1 ATOM 1126 C C . LYS A 1 137 ? 11.152 -6.353 67.806 1.00 13.22 ? 137 LYS A C 1 ATOM 1127 O O . LYS A 1 137 ? 12.210 -5.995 68.230 1.00 13.07 ? 137 LYS A O 1 ATOM 1128 C CB . LYS A 1 137 ? 9.612 -4.703 66.665 1.00 16.63 ? 137 LYS A CB 1 ATOM 1129 C CG . LYS A 1 137 ? 10.129 -3.450 67.351 1.00 13.41 ? 137 LYS A CG 1 ATOM 1130 C CD . LYS A 1 137 ? 11.387 -2.981 66.625 1.00 15.79 ? 137 LYS A CD 1 ATOM 1131 C CE . LYS A 1 137 ? 11.962 -1.715 67.260 1.00 16.76 ? 137 LYS A CE 1 ATOM 1132 N NZ . LYS A 1 137 ? 11.114 -0.503 67.050 1.00 19.66 ? 137 LYS A NZ 1 ATOM 1133 N N . ALA A 1 138 ? 10.363 -7.206 68.451 1.00 11.46 ? 138 ALA A N 1 ATOM 1134 C CA . ALA A 1 138 ? 10.717 -7.760 69.746 1.00 9.87 ? 138 ALA A CA 1 ATOM 1135 C C . ALA A 1 138 ? 12.056 -8.459 69.654 1.00 9.93 ? 138 ALA A C 1 ATOM 1136 O O . ALA A 1 138 ? 12.893 -8.327 70.519 1.00 6.96 ? 138 ALA A O 1 ATOM 1137 C CB . ALA A 1 138 ? 9.666 -8.713 70.170 1.00 10.09 ? 138 ALA A CB 1 ATOM 1138 N N . GLU A 1 139 ? 12.243 -9.194 68.567 1.00 11.19 ? 139 GLU A N 1 ATOM 1139 C CA . GLU A 1 139 ? 13.457 -9.935 68.288 1.00 12.52 ? 139 GLU A CA 1 ATOM 1140 C C . GLU A 1 139 ? 14.626 -9.013 68.105 1.00 13.57 ? 139 GLU A C 1 ATOM 1141 O O . GLU A 1 139 ? 15.724 -9.366 68.431 1.00 15.26 ? 139 GLU A O 1 ATOM 1142 C CB . GLU A 1 139 ? 13.272 -10.768 67.035 1.00 13.10 ? 139 GLU A CB 1 ATOM 1143 C CG . GLU A 1 139 ? 14.475 -11.553 66.582 1.00 16.09 ? 139 GLU A CG 1 ATOM 1144 C CD . GLU A 1 139 ? 15.009 -12.516 67.631 1.00 19.55 ? 139 GLU A CD 1 ATOM 1145 O OE1 . GLU A 1 139 ? 14.233 -13.230 68.288 1.00 19.03 ? 139 GLU A OE1 1 ATOM 1146 O OE2 . GLU A 1 139 ? 16.250 -12.581 67.766 1.00 23.02 ? 139 GLU A OE2 1 ATOM 1147 N N . PHE A 1 140 ? 14.397 -7.816 67.572 1.00 14.30 ? 140 PHE A N 1 ATOM 1148 C CA . PHE A 1 140 ? 15.492 -6.860 67.360 1.00 13.87 ? 140 PHE A CA 1 ATOM 1149 C C . PHE A 1 140 ? 15.953 -6.227 68.686 1.00 13.57 ? 140 PHE A C 1 ATOM 1150 O O . PHE A 1 140 ? 17.125 -5.978 68.877 1.00 12.96 ? 140 PHE A O 1 ATOM 1151 C CB . PHE A 1 140 ? 15.041 -5.772 66.412 1.00 14.88 ? 140 PHE A CB 1 ATOM 1152 C CG . PHE A 1 140 ? 15.068 -6.146 64.966 1.00 16.50 ? 140 PHE A CG 1 ATOM 1153 C CD1 . PHE A 1 140 ? 15.255 -7.435 64.591 1.00 18.90 ? 140 PHE A CD1 1 ATOM 1154 C CD2 . PHE A 1 140 ? 14.885 -5.178 63.968 1.00 18.37 ? 140 PHE A CD2 1 ATOM 1155 C CE1 . PHE A 1 140 ? 15.269 -7.795 63.249 1.00 18.95 ? 140 PHE A CE1 1 ATOM 1156 C CE2 . PHE A 1 140 ? 14.883 -5.530 62.632 1.00 19.66 ? 140 PHE A CE2 1 ATOM 1157 C CZ . PHE A 1 140 ? 15.105 -6.851 62.272 1.00 18.94 ? 140 PHE A CZ 1 ATOM 1158 N N . ALA A 1 141 ? 15.012 -5.977 69.593 1.00 13.61 ? 141 ALA A N 1 ATOM 1159 C CA . ALA A 1 141 ? 15.289 -5.411 70.910 1.00 13.87 ? 141 ALA A CA 1 ATOM 1160 C C . ALA A 1 141 ? 16.100 -6.383 71.723 1.00 16.27 ? 141 ALA A C 1 ATOM 1161 O O . ALA A 1 141 ? 17.145 -6.070 72.236 1.00 16.78 ? 141 ALA A O 1 ATOM 1162 C CB . ALA A 1 141 ? 13.938 -5.043 71.651 1.00 8.50 ? 141 ALA A CB 1 ATOM 1163 N N . ARG A 1 142 ? 15.630 -7.605 71.777 1.00 21.31 ? 142 ARG A N 1 ATOM 1164 C CA . ARG A 1 142 ? 16.316 -8.680 72.497 1.00 26.13 ? 142 ARG A CA 1 ATOM 1165 C C . ARG A 1 142 ? 17.715 -8.906 71.982 1.00 25.22 ? 142 ARG A C 1 ATOM 1166 O O . ARG A 1 142 ? 18.600 -9.292 72.703 1.00 26.98 ? 142 ARG A O 1 ATOM 1167 C CB . ARG A 1 142 ? 15.527 -10.015 72.361 1.00 29.74 ? 142 ARG A CB 1 ATOM 1168 C CG . ARG A 1 142 ? 15.821 -11.094 73.445 1.00 38.96 ? 142 ARG A CG 1 ATOM 1169 C CD . ARG A 1 142 ? 14.572 -11.840 73.970 1.00 47.66 ? 142 ARG A CD 1 ATOM 1170 N NE . ARG A 1 142 ? 13.798 -12.498 72.893 1.00 59.25 ? 142 ARG A NE 1 ATOM 1171 C CZ . ARG A 1 142 ? 12.820 -11.911 72.144 1.00 64.96 ? 142 ARG A CZ 1 ATOM 1172 N NH1 . ARG A 1 142 ? 12.486 -10.634 72.356 1.00 68.66 ? 142 ARG A NH1 1 ATOM 1173 N NH2 . ARG A 1 142 ? 12.182 -12.593 71.187 1.00 64.55 ? 142 ARG A NH2 1 ATOM 1174 N N . GLU A 1 143 ? 17.929 -8.645 70.727 1.00 24.75 ? 143 GLU A N 1 ATOM 1175 C CA . GLU A 1 143 ? 19.236 -8.882 70.142 1.00 24.33 ? 143 GLU A CA 1 ATOM 1176 C C . GLU A 1 143 ? 20.188 -7.739 70.329 1.00 23.44 ? 143 GLU A C 1 ATOM 1177 O O . GLU A 1 143 ? 21.390 -7.914 70.202 1.00 24.21 ? 143 GLU A O 1 ATOM 1178 C CB . GLU A 1 143 ? 19.095 -9.222 68.651 1.00 24.79 ? 143 GLU A CB 1 ATOM 1179 C CG . GLU A 1 143 ? 20.370 -9.641 67.953 1.00 24.92 ? 143 GLU A CG 1 ATOM 1180 C CD . GLU A 1 143 ? 21.070 -8.509 67.230 1.00 24.60 ? 143 GLU A CD 1 ATOM 1181 O OE1 . GLU A 1 143 ? 20.789 -7.312 67.498 1.00 29.56 ? 143 GLU A OE1 1 ATOM 1182 O OE2 . GLU A 1 143 ? 21.925 -8.815 66.404 1.00 23.76 ? 143 GLU A OE2 1 ATOM 1183 N N . ALA A 1 144 ? 19.678 -6.561 70.610 1.00 22.41 ? 144 ALA A N 1 ATOM 1184 C CA . ALA A 1 144 ? 20.566 -5.425 70.798 1.00 21.99 ? 144 ALA A CA 1 ATOM 1185 C C . ALA A 1 144 ? 21.315 -5.592 72.121 1.00 21.52 ? 144 ALA A C 1 ATOM 1186 O O . ALA A 1 144 ? 22.229 -4.869 72.450 1.00 21.87 ? 144 ALA A O 1 ATOM 1187 C CB . ALA A 1 144 ? 19.774 -4.155 70.808 1.00 21.96 ? 144 ALA A CB 1 ATOM 1188 N N . GLN A 1 145 ? 20.904 -6.567 72.888 1.00 20.55 ? 145 GLN A N 1 ATOM 1189 C CA . GLN A 1 145 ? 21.533 -6.805 74.162 1.00 19.75 ? 145 GLN A CA 1 ATOM 1190 C C . GLN A 1 145 ? 22.958 -7.265 74.045 1.00 19.89 ? 145 GLN A C 1 ATOM 1191 O O . GLN A 1 145 ? 23.743 -7.108 74.966 1.00 18.07 ? 145 GLN A O 1 ATOM 1192 C CB . GLN A 1 145 ? 20.718 -7.845 74.927 1.00 20.21 ? 145 GLN A CB 1 ATOM 1193 C CG . GLN A 1 145 ? 19.307 -7.377 75.307 1.00 19.73 ? 145 GLN A CG 1 ATOM 1194 C CD . GLN A 1 145 ? 18.477 -8.463 75.948 1.00 19.41 ? 145 GLN A CD 1 ATOM 1195 O OE1 . GLN A 1 145 ? 18.982 -9.518 76.274 1.00 20.04 ? 145 GLN A OE1 1 ATOM 1196 N NE2 . GLN A 1 145 ? 17.182 -8.218 76.080 1.00 20.90 ? 145 GLN A NE2 1 ATOM 1197 N N . ALA A 1 146 ? 23.288 -7.866 72.916 1.00 21.91 ? 146 ALA A N 1 ATOM 1198 C CA . ALA A 1 146 ? 24.646 -8.368 72.668 1.00 23.62 ? 146 ALA A CA 1 ATOM 1199 C C . ALA A 1 146 ? 25.613 -7.192 72.519 1.00 24.85 ? 146 ALA A C 1 ATOM 1200 O O . ALA A 1 146 ? 26.726 -7.322 72.055 1.00 23.75 ? 146 ALA A O 1 ATOM 1201 C CB . ALA A 1 146 ? 24.683 -9.232 71.433 1.00 24.11 ? 146 ALA A CB 1 ATOM 1202 N N . GLY A 1 147 ? 25.141 -6.030 72.913 1.00 27.11 ? 147 GLY A N 1 ATOM 1203 C CA . GLY A 1 147 ? 25.950 -4.824 72.883 1.00 29.05 ? 147 GLY A CA 1 ATOM 1204 C C . GLY A 1 147 ? 26.348 -4.374 71.502 1.00 30.11 ? 147 GLY A C 1 ATOM 1205 O O . GLY A 1 147 ? 27.506 -4.130 71.207 1.00 32.49 ? 147 GLY A O 1 ATOM 1206 N N . THR A 1 148 ? 25.375 -4.300 70.641 1.00 30.82 ? 148 THR A N 1 ATOM 1207 C CA . THR A 1 148 ? 25.572 -3.819 69.297 1.00 31.64 ? 148 THR A CA 1 ATOM 1208 C C . THR A 1 148 ? 24.356 -2.939 68.989 1.00 30.12 ? 148 THR A C 1 ATOM 1209 O O . THR A 1 148 ? 23.366 -2.959 69.689 1.00 31.54 ? 148 THR A O 1 ATOM 1210 C CB . THR A 1 148 ? 25.681 -4.982 68.312 1.00 33.29 ? 148 THR A CB 1 ATOM 1211 O OG1 . THR A 1 148 ? 25.924 -4.457 66.994 1.00 37.32 ? 148 THR A OG1 1 ATOM 1212 C CG2 . THR A 1 148 ? 24.360 -5.802 68.269 1.00 33.73 ? 148 THR A CG2 1 ATOM 1213 N N . GLU A 1 149 ? 24.410 -2.139 67.963 1.00 28.70 ? 149 GLU A N 1 ATOM 1214 C CA . GLU A 1 149 ? 23.282 -1.249 67.682 1.00 28.43 ? 149 GLU A CA 1 ATOM 1215 C C . GLU A 1 149 ? 22.000 -1.922 67.173 1.00 26.12 ? 149 GLU A C 1 ATOM 1216 O O . GLU A 1 149 ? 22.033 -2.769 66.282 1.00 27.47 ? 149 GLU A O 1 ATOM 1217 C CB . GLU A 1 149 ? 23.738 -0.164 66.711 1.00 29.70 ? 149 GLU A CB 1 ATOM 1218 C CG . GLU A 1 149 ? 22.920 1.081 66.829 1.00 36.81 ? 149 GLU A CG 1 ATOM 1219 C CD . GLU A 1 149 ? 23.691 2.304 66.468 1.00 43.29 ? 149 GLU A CD 1 ATOM 1220 O OE1 . GLU A 1 149 ? 24.811 2.444 67.028 1.00 47.32 ? 149 GLU A OE1 1 ATOM 1221 O OE2 . GLU A 1 149 ? 23.168 3.114 65.646 1.00 48.59 ? 149 GLU A OE2 1 ATOM 1222 N N . ARG A 1 150 ? 20.871 -1.549 67.769 1.00 22.95 ? 150 ARG A N 1 ATOM 1223 C CA . ARG A 1 150 ? 19.556 -2.105 67.408 1.00 21.25 ? 150 ARG A CA 1 ATOM 1224 C C . ARG A 1 150 ? 19.269 -1.993 65.946 1.00 18.34 ? 150 ARG A C 1 ATOM 1225 O O . ARG A 1 150 ? 19.388 -0.948 65.391 1.00 20.06 ? 150 ARG A O 1 ATOM 1226 C CB . ARG A 1 150 ? 18.446 -1.393 68.133 1.00 22.20 ? 150 ARG A CB 1 ATOM 1227 C CG . ARG A 1 150 ? 17.581 -2.259 69.022 1.00 28.07 ? 150 ARG A CG 1 ATOM 1228 C CD . ARG A 1 150 ? 16.317 -1.591 69.418 1.00 32.19 ? 150 ARG A CD 1 ATOM 1229 N NE . ARG A 1 150 ? 15.686 -1.164 68.187 1.00 46.19 ? 150 ARG A NE 1 ATOM 1230 C CZ . ARG A 1 150 ? 14.608 -0.374 68.100 1.00 54.47 ? 150 ARG A CZ 1 ATOM 1231 N NH1 . ARG A 1 150 ? 14.000 0.073 69.211 1.00 56.43 ? 150 ARG A NH1 1 ATOM 1232 N NH2 . ARG A 1 150 ? 14.140 -0.023 66.885 1.00 56.85 ? 150 ARG A NH2 1 ATOM 1233 N N . LEU A 1 151 ? 18.894 -3.084 65.307 1.00 15.48 ? 151 LEU A N 1 ATOM 1234 C CA . LEU A 1 151 ? 18.608 -3.077 63.881 1.00 12.75 ? 151 LEU A CA 1 ATOM 1235 C C . LEU A 1 151 ? 17.275 -2.327 63.617 1.00 12.85 ? 151 LEU A C 1 ATOM 1236 O O . LEU A 1 151 ? 16.300 -2.498 64.369 1.00 13.55 ? 151 LEU A O 1 ATOM 1237 C CB . LEU A 1 151 ? 18.520 -4.531 63.380 1.00 9.94 ? 151 LEU A CB 1 ATOM 1238 C CG . LEU A 1 151 ? 19.788 -5.353 63.389 1.00 4.71 ? 151 LEU A CG 1 ATOM 1239 C CD1 . LEU A 1 151 ? 19.304 -6.822 63.495 1.00 5.52 ? 151 LEU A CD1 1 ATOM 1240 C CD2 . LEU A 1 151 ? 20.612 -5.083 62.139 1.00 4.34 ? 151 LEU A CD2 1 ATOM 1241 N N . LEU A 1 152 ? 17.222 -1.495 62.573 1.00 10.21 ? 152 LEU A N 1 ATOM 1242 C CA . LEU A 1 152 ? 16.000 -0.766 62.267 1.00 9.01 ? 152 LEU A CA 1 ATOM 1243 C C . LEU A 1 152 ? 14.925 -1.666 61.616 1.00 8.78 ? 152 LEU A C 1 ATOM 1244 O O . LEU A 1 152 ? 15.249 -2.639 60.963 1.00 10.74 ? 152 LEU A O 1 ATOM 1245 C CB . LEU A 1 152 ? 16.311 0.380 61.319 1.00 9.08 ? 152 LEU A CB 1 ATOM 1246 C CG . LEU A 1 152 ? 17.269 1.443 61.730 1.00 7.43 ? 152 LEU A CG 1 ATOM 1247 C CD1 . LEU A 1 152 ? 17.656 2.301 60.504 1.00 9.13 ? 152 LEU A CD1 1 ATOM 1248 C CD2 . LEU A 1 152 ? 16.597 2.260 62.772 1.00 9.45 ? 152 LEU A CD2 1 ATOM 1249 N N . LEU A 1 153 ? 13.654 -1.322 61.764 1.00 6.61 ? 153 LEU A N 1 ATOM 1250 C CA . LEU A 1 153 ? 12.585 -2.071 61.166 1.00 4.12 ? 153 LEU A CA 1 ATOM 1251 C C . LEU A 1 153 ? 11.629 -1.131 60.533 1.00 5.33 ? 153 LEU A C 1 ATOM 1252 O O . LEU A 1 153 ? 11.065 -0.269 61.196 1.00 5.45 ? 153 LEU A O 1 ATOM 1253 C CB . LEU A 1 153 ? 11.850 -2.927 62.157 1.00 4.84 ? 153 LEU A CB 1 ATOM 1254 C CG . LEU A 1 153 ? 10.666 -3.725 61.568 1.00 6.19 ? 153 LEU A CG 1 ATOM 1255 C CD1 . LEU A 1 153 ? 11.147 -4.681 60.576 1.00 9.00 ? 153 LEU A CD1 1 ATOM 1256 C CD2 . LEU A 1 153 ? 9.939 -4.509 62.691 1.00 5.94 ? 153 LEU A CD2 1 ATOM 1257 N N . SER A 1 154 ? 11.413 -1.297 59.230 1.00 7.03 ? 154 SER A N 1 ATOM 1258 C CA . SER A 1 154 ? 10.488 -0.442 58.475 1.00 7.33 ? 154 SER A CA 1 ATOM 1259 C C . SER A 1 154 ? 9.602 -1.211 57.556 1.00 6.98 ? 154 SER A C 1 ATOM 1260 O O . SER A 1 154 ? 9.793 -2.342 57.354 1.00 5.77 ? 154 SER A O 1 ATOM 1261 C CB . SER A 1 154 ? 11.281 0.577 57.637 1.00 7.72 ? 154 SER A CB 1 ATOM 1262 O OG . SER A 1 154 ? 12.069 -0.113 56.688 1.00 5.24 ? 154 SER A OG 1 ATOM 1263 N N . ALA A 1 155 ? 8.642 -0.528 56.983 1.00 7.38 ? 155 ALA A N 1 ATOM 1264 C CA . ALA A 1 155 ? 7.677 -1.138 56.077 1.00 7.96 ? 155 ALA A CA 1 ATOM 1265 C C . ALA A 1 155 ? 7.232 -0.183 54.953 1.00 8.89 ? 155 ALA A C 1 ATOM 1266 O O . ALA A 1 155 ? 7.186 1.033 55.145 1.00 10.11 ? 155 ALA A O 1 ATOM 1267 C CB . ALA A 1 155 ? 6.453 -1.581 56.881 1.00 5.02 ? 155 ALA A CB 1 ATOM 1268 N N . ALA A 1 156 ? 6.993 -0.742 53.766 1.00 9.45 ? 156 ALA A N 1 ATOM 1269 C CA . ALA A 1 156 ? 6.528 0.025 52.624 1.00 10.67 ? 156 ALA A CA 1 ATOM 1270 C C . ALA A 1 156 ? 5.038 -0.275 52.524 1.00 12.80 ? 156 ALA A C 1 ATOM 1271 O O . ALA A 1 156 ? 4.646 -1.391 52.276 1.00 14.34 ? 156 ALA A O 1 ATOM 1272 C CB . ALA A 1 156 ? 7.240 -0.415 51.373 1.00 10.62 ? 156 ALA A CB 1 ATOM 1273 N N . VAL A 1 157 ? 4.202 0.725 52.732 1.00 14.95 ? 157 VAL A N 1 ATOM 1274 C CA . VAL A 1 157 ? 2.755 0.561 52.723 1.00 15.48 ? 157 VAL A CA 1 ATOM 1275 C C . VAL A 1 157 ? 2.045 1.158 51.501 1.00 17.17 ? 157 VAL A C 1 ATOM 1276 O O . VAL A 1 157 ? 2.515 2.080 50.835 1.00 18.22 ? 157 VAL A O 1 ATOM 1277 C CB . VAL A 1 157 ? 2.127 1.188 53.999 1.00 15.68 ? 157 VAL A CB 1 ATOM 1278 C CG1 . VAL A 1 157 ? 0.661 1.108 53.980 1.00 17.60 ? 157 VAL A CG1 1 ATOM 1279 C CG2 . VAL A 1 157 ? 2.632 0.477 55.231 1.00 18.03 ? 157 VAL A CG2 1 ATOM 1280 N N . SER A 1 158 ? 0.860 0.620 51.224 1.00 18.51 ? 158 SER A N 1 ATOM 1281 C CA . SER A 1 158 ? 0.015 1.072 50.117 1.00 18.12 ? 158 SER A CA 1 ATOM 1282 C C . SER A 1 158 ? -0.508 2.428 50.447 1.00 18.00 ? 158 SER A C 1 ATOM 1283 O O . SER A 1 158 ? -0.617 2.772 51.605 1.00 20.80 ? 158 SER A O 1 ATOM 1284 C CB . SER A 1 158 ? -1.169 0.115 49.962 1.00 18.92 ? 158 SER A CB 1 ATOM 1285 O OG . SER A 1 158 ? -2.009 0.409 48.833 1.00 13.94 ? 158 SER A OG 1 ATOM 1286 N N . ALA A 1 159 ? -0.849 3.212 49.445 1.00 16.86 ? 159 ALA A N 1 ATOM 1287 C CA . ALA A 1 159 ? -1.439 4.548 49.679 1.00 14.94 ? 159 ALA A CA 1 ATOM 1288 C C . ALA A 1 159 ? -2.852 4.540 49.210 1.00 14.17 ? 159 ALA A C 1 ATOM 1289 O O . ALA A 1 159 ? -3.465 5.540 49.218 1.00 16.10 ? 159 ALA A O 1 ATOM 1290 C CB . ALA A 1 159 ? -0.658 5.615 48.927 1.00 14.77 ? 159 ALA A CB 1 ATOM 1291 N N . GLY A 1 160 ? -3.371 3.417 48.778 1.00 15.07 ? 160 GLY A N 1 ATOM 1292 C CA . GLY A 1 160 ? -4.736 3.332 48.314 1.00 18.22 ? 160 GLY A CA 1 ATOM 1293 C C . GLY A 1 160 ? -5.716 3.034 49.442 1.00 21.35 ? 160 GLY A C 1 ATOM 1294 O O . GLY A 1 160 ? -5.664 1.976 50.069 1.00 21.54 ? 160 GLY A O 1 ATOM 1295 N N . LYS A 1 161 ? -6.607 4.000 49.694 1.00 23.50 ? 161 LYS A N 1 ATOM 1296 C CA . LYS A 1 161 ? -7.613 3.911 50.763 1.00 23.88 ? 161 LYS A CA 1 ATOM 1297 C C . LYS A 1 161 ? -8.187 2.517 50.957 1.00 23.16 ? 161 LYS A C 1 ATOM 1298 O O . LYS A 1 161 ? -8.216 1.995 52.048 1.00 22.70 ? 161 LYS A O 1 ATOM 1299 C CB . LYS A 1 161 ? -8.757 4.895 50.483 1.00 23.67 ? 161 LYS A CB 1 ATOM 1300 C CG . LYS A 1 161 ? -9.677 5.027 51.649 1.00 26.82 ? 161 LYS A CG 1 ATOM 1301 C CD . LYS A 1 161 ? -10.957 5.745 51.301 1.00 28.57 ? 161 LYS A CD 1 ATOM 1302 C CE . LYS A 1 161 ? -11.713 6.170 52.570 1.00 29.87 ? 161 LYS A CE 1 ATOM 1303 N NZ . LYS A 1 161 ? -11.708 5.078 53.600 1.00 26.14 ? 161 LYS A NZ 1 ATOM 1304 N N . ILE A 1 162 ? -8.657 1.914 49.895 1.00 23.19 ? 162 ILE A N 1 ATOM 1305 C CA . ILE A 1 162 ? -9.249 0.596 50.002 1.00 24.96 ? 162 ILE A CA 1 ATOM 1306 C C . ILE A 1 162 ? -8.235 -0.465 50.448 1.00 23.50 ? 162 ILE A C 1 ATOM 1307 O O . ILE A 1 162 ? -8.568 -1.410 51.129 1.00 24.22 ? 162 ILE A O 1 ATOM 1308 C CB . ILE A 1 162 ? -9.902 0.169 48.685 1.00 27.03 ? 162 ILE A CB 1 ATOM 1309 C CG1 . ILE A 1 162 ? -11.010 1.159 48.302 1.00 27.40 ? 162 ILE A CG1 1 ATOM 1310 C CG2 . ILE A 1 162 ? -10.445 -1.231 48.789 1.00 29.22 ? 162 ILE A CG2 1 ATOM 1311 C CD1 . ILE A 1 162 ? -12.242 0.486 47.677 1.00 25.79 ? 162 ILE A CD1 1 ATOM 1312 N N . ALA A 1 163 ? -6.985 -0.303 50.064 1.00 22.73 ? 163 ALA A N 1 ATOM 1313 C CA . ALA A 1 163 ? -5.942 -1.241 50.470 1.00 22.75 ? 163 ALA A CA 1 ATOM 1314 C C . ALA A 1 163 ? -5.544 -1.109 51.939 1.00 22.26 ? 163 ALA A C 1 ATOM 1315 O O . ALA A 1 163 ? -5.176 -2.066 52.591 1.00 21.51 ? 163 ALA A O 1 ATOM 1316 C CB . ALA A 1 163 ? -4.712 -1.051 49.610 1.00 22.62 ? 163 ALA A CB 1 ATOM 1317 N N . ILE A 1 164 ? -5.618 0.105 52.452 1.00 23.08 ? 164 ILE A N 1 ATOM 1318 C CA . ILE A 1 164 ? -5.235 0.399 53.830 1.00 22.02 ? 164 ILE A CA 1 ATOM 1319 C C . ILE A 1 164 ? -6.307 -0.112 54.783 1.00 23.12 ? 164 ILE A C 1 ATOM 1320 O O . ILE A 1 164 ? -5.993 -0.623 55.856 1.00 22.60 ? 164 ILE A O 1 ATOM 1321 C CB . ILE A 1 164 ? -5.002 1.902 54.038 1.00 20.84 ? 164 ILE A CB 1 ATOM 1322 C CG1 . ILE A 1 164 ? -3.887 2.384 53.142 1.00 20.51 ? 164 ILE A CG1 1 ATOM 1323 C CG2 . ILE A 1 164 ? -4.698 2.170 55.510 1.00 18.76 ? 164 ILE A CG2 1 ATOM 1324 C CD1 . ILE A 1 164 ? -3.699 3.883 53.139 1.00 24.33 ? 164 ILE A CD1 1 ATOM 1325 N N . ASP A 1 165 ? -7.583 0.036 54.386 1.00 24.64 ? 165 ASP A N 1 ATOM 1326 C CA . ASP A 1 165 ? -8.695 -0.403 55.198 1.00 25.45 ? 165 ASP A CA 1 ATOM 1327 C C . ASP A 1 165 ? -8.747 -1.906 55.222 1.00 26.15 ? 165 ASP A C 1 ATOM 1328 O O . ASP A 1 165 ? -9.062 -2.493 56.220 1.00 24.72 ? 165 ASP A O 1 ATOM 1329 C CB . ASP A 1 165 ? -10.021 0.094 54.627 1.00 25.67 ? 165 ASP A CB 1 ATOM 1330 C CG . ASP A 1 165 ? -10.274 1.567 54.894 1.00 26.97 ? 165 ASP A CG 1 ATOM 1331 O OD1 . ASP A 1 165 ? -9.645 2.080 55.877 1.00 27.84 ? 165 ASP A OD1 1 ATOM 1332 O OD2 . ASP A 1 165 ? -11.048 2.241 54.136 1.00 22.70 ? 165 ASP A OD2 1 ATOM 1333 N N . ARG A 1 166 ? -8.391 -2.514 54.103 1.00 29.00 ? 166 ARG A N 1 ATOM 1334 C CA . ARG A 1 166 ? -8.423 -3.959 53.962 1.00 31.85 ? 166 ARG A CA 1 ATOM 1335 C C . ARG A 1 166 ? -7.379 -4.787 54.653 1.00 29.68 ? 166 ARG A C 1 ATOM 1336 O O . ARG A 1 166 ? -7.713 -5.824 55.231 1.00 30.62 ? 166 ARG A O 1 ATOM 1337 C CB . ARG A 1 166 ? -8.408 -4.297 52.491 1.00 35.15 ? 166 ARG A CB 1 ATOM 1338 C CG . ARG A 1 166 ? -8.680 -5.733 52.207 1.00 45.12 ? 166 ARG A CG 1 ATOM 1339 C CD . ARG A 1 166 ? -8.014 -6.137 50.912 1.00 56.10 ? 166 ARG A CD 1 ATOM 1340 N NE . ARG A 1 166 ? -8.347 -5.206 49.816 1.00 63.41 ? 166 ARG A NE 1 ATOM 1341 C CZ . ARG A 1 166 ? -7.659 -5.112 48.675 1.00 68.31 ? 166 ARG A CZ 1 ATOM 1342 N NH1 . ARG A 1 166 ? -6.578 -5.881 48.473 1.00 71.00 ? 166 ARG A NH1 1 ATOM 1343 N NH2 . ARG A 1 166 ? -8.047 -4.257 47.735 1.00 70.10 ? 166 ARG A NH2 1 ATOM 1344 N N . GLY A 1 167 ? -6.132 -4.346 54.601 1.00 27.83 ? 167 GLY A N 1 ATOM 1345 C CA . GLY A 1 167 ? -5.055 -5.148 55.181 1.00 27.51 ? 167 GLY A CA 1 ATOM 1346 C C . GLY A 1 167 ? -4.086 -4.578 56.197 1.00 26.21 ? 167 GLY A C 1 ATOM 1347 O O . GLY A 1 167 ? -3.166 -5.273 56.591 1.00 25.79 ? 167 GLY A O 1 ATOM 1348 N N . TYR A 1 168 ? -4.278 -3.352 56.636 1.00 25.30 ? 168 TYR A N 1 ATOM 1349 C CA . TYR A 1 168 ? -3.343 -2.775 57.590 1.00 24.70 ? 168 TYR A CA 1 ATOM 1350 C C . TYR A 1 168 ? -4.006 -2.251 58.856 1.00 25.84 ? 168 TYR A C 1 ATOM 1351 O O . TYR A 1 168 ? -5.085 -1.713 58.832 1.00 28.18 ? 168 TYR A O 1 ATOM 1352 C CB . TYR A 1 168 ? -2.543 -1.627 56.952 1.00 23.31 ? 168 TYR A CB 1 ATOM 1353 C CG . TYR A 1 168 ? -1.764 -1.954 55.710 1.00 18.41 ? 168 TYR A CG 1 ATOM 1354 C CD1 . TYR A 1 168 ? -0.552 -2.499 55.785 1.00 18.91 ? 168 TYR A CD1 1 ATOM 1355 C CD2 . TYR A 1 168 ? -2.233 -1.608 54.454 1.00 17.82 ? 168 TYR A CD2 1 ATOM 1356 C CE1 . TYR A 1 168 ? 0.163 -2.788 54.624 1.00 21.23 ? 168 TYR A CE1 1 ATOM 1357 C CE2 . TYR A 1 168 ? -1.532 -1.874 53.283 1.00 16.64 ? 168 TYR A CE2 1 ATOM 1358 C CZ . TYR A 1 168 ? -0.334 -2.462 53.369 1.00 18.45 ? 168 TYR A CZ 1 ATOM 1359 O OH . TYR A 1 168 ? 0.425 -2.723 52.252 1.00 17.60 ? 168 TYR A OH 1 ATOM 1360 N N . ASP A 1 169 ? -3.343 -2.433 59.970 1.00 26.33 ? 169 ASP A N 1 ATOM 1361 C CA . ASP A 1 169 ? -3.800 -1.899 61.218 1.00 26.93 ? 169 ASP A CA 1 ATOM 1362 C C . ASP A 1 169 ? -2.754 -0.841 61.553 1.00 24.03 ? 169 ASP A C 1 ATOM 1363 O O . ASP A 1 169 ? -1.923 -1.023 62.409 1.00 22.02 ? 169 ASP A O 1 ATOM 1364 C CB . ASP A 1 169 ? -3.876 -2.992 62.291 1.00 30.29 ? 169 ASP A CB 1 ATOM 1365 C CG . ASP A 1 169 ? -4.570 -2.520 63.594 1.00 34.59 ? 169 ASP A CG 1 ATOM 1366 O OD1 . ASP A 1 169 ? -5.076 -1.367 63.654 1.00 39.75 ? 169 ASP A OD1 1 ATOM 1367 O OD2 . ASP A 1 169 ? -4.644 -3.277 64.590 1.00 37.59 ? 169 ASP A OD2 1 ATOM 1368 N N . ILE A 1 170 ? -2.810 0.259 60.816 1.00 22.76 ? 170 ILE A N 1 ATOM 1369 C CA . ILE A 1 170 ? -1.852 1.370 60.948 1.00 23.13 ? 170 ILE A CA 1 ATOM 1370 C C . ILE A 1 170 ? -1.478 1.731 62.412 1.00 23.31 ? 170 ILE A C 1 ATOM 1371 O O . ILE A 1 170 ? -0.316 1.831 62.773 1.00 21.92 ? 170 ILE A O 1 ATOM 1372 C CB . ILE A 1 170 ? -2.375 2.571 60.232 1.00 22.50 ? 170 ILE A CB 1 ATOM 1373 C CG1 . ILE A 1 170 ? -2.526 2.225 58.757 1.00 25.00 ? 170 ILE A CG1 1 ATOM 1374 C CG2 . ILE A 1 170 ? -1.450 3.726 60.359 1.00 22.89 ? 170 ILE A CG2 1 ATOM 1375 C CD1 . ILE A 1 170 ? -3.309 3.343 57.988 1.00 31.22 ? 170 ILE A CD1 1 ATOM 1376 N N . ALA A 1 171 ? -2.477 1.939 63.262 1.00 24.17 ? 171 ALA A N 1 ATOM 1377 C CA . ALA A 1 171 ? -2.212 2.320 64.636 1.00 24.75 ? 171 ALA A CA 1 ATOM 1378 C C . ALA A 1 171 ? -1.250 1.364 65.347 1.00 25.42 ? 171 ALA A C 1 ATOM 1379 O O . ALA A 1 171 ? -0.341 1.784 66.083 1.00 27.17 ? 171 ALA A O 1 ATOM 1380 C CB . ALA A 1 171 ? -3.522 2.412 65.400 1.00 24.44 ? 171 ALA A CB 1 ATOM 1381 N N . GLN A 1 172 ? -1.441 0.084 65.130 1.00 25.26 ? 172 GLN A N 1 ATOM 1382 C CA . GLN A 1 172 ? -0.625 -0.939 65.763 1.00 25.89 ? 172 GLN A CA 1 ATOM 1383 C C . GLN A 1 172 ? 0.782 -1.026 65.225 1.00 23.78 ? 172 GLN A C 1 ATOM 1384 O O . GLN A 1 172 ? 1.689 -0.911 65.955 1.00 24.48 ? 172 GLN A O 1 ATOM 1385 C CB . GLN A 1 172 ? -1.305 -2.306 65.623 1.00 28.13 ? 172 GLN A CB 1 ATOM 1386 C CG . GLN A 1 172 ? -2.625 -2.368 66.326 1.00 35.91 ? 172 GLN A CG 1 ATOM 1387 C CD . GLN A 1 172 ? -2.551 -3.063 67.674 1.00 42.56 ? 172 GLN A CD 1 ATOM 1388 O OE1 . GLN A 1 172 ? -1.603 -2.869 68.436 1.00 42.14 ? 172 GLN A OE1 1 ATOM 1389 N NE2 . GLN A 1 172 ? -3.589 -3.882 67.977 1.00 46.74 ? 172 GLN A NE2 1 ATOM 1390 N N . ILE A 1 173 ? 0.955 -1.229 63.928 1.00 23.02 ? 173 ILE A N 1 ATOM 1391 C CA . ILE A 1 173 ? 2.291 -1.400 63.384 1.00 22.72 ? 173 ILE A CA 1 ATOM 1392 C C . ILE A 1 173 ? 3.122 -0.122 63.417 1.00 22.73 ? 173 ILE A C 1 ATOM 1393 O O . ILE A 1 173 ? 4.286 -0.176 63.170 1.00 23.78 ? 173 ILE A O 1 ATOM 1394 C CB . ILE A 1 173 ? 2.281 -1.976 61.957 1.00 22.77 ? 173 ILE A CB 1 ATOM 1395 C CG1 . ILE A 1 173 ? 2.100 -0.838 60.938 1.00 22.50 ? 173 ILE A CG1 1 ATOM 1396 C CG2 . ILE A 1 173 ? 1.239 -3.031 61.835 1.00 22.76 ? 173 ILE A CG2 1 ATOM 1397 C CD1 . ILE A 1 173 ? 1.424 -1.231 59.670 1.00 19.86 ? 173 ILE A CD1 1 ATOM 1398 N N . SER A 1 174 ? 2.549 1.023 63.696 1.00 23.97 ? 174 SER A N 1 ATOM 1399 C CA . SER A 1 174 ? 3.311 2.281 63.764 1.00 24.94 ? 174 SER A CA 1 ATOM 1400 C C . SER A 1 174 ? 4.056 2.333 65.070 1.00 25.25 ? 174 SER A C 1 ATOM 1401 O O . SER A 1 174 ? 5.088 2.990 65.180 1.00 23.87 ? 174 SER A O 1 ATOM 1402 C CB . SER A 1 174 ? 2.395 3.495 63.682 1.00 25.13 ? 174 SER A CB 1 ATOM 1403 O OG . SER A 1 174 ? 1.591 3.440 62.512 1.00 29.30 ? 174 SER A OG 1 ATOM 1404 N N . ARG A 1 175 ? 3.507 1.659 66.070 1.00 27.00 ? 175 ARG A N 1 ATOM 1405 C CA . ARG A 1 175 ? 4.128 1.594 67.375 1.00 29.98 ? 175 ARG A CA 1 ATOM 1406 C C . ARG A 1 175 ? 5.472 0.864 67.264 1.00 29.60 ? 175 ARG A C 1 ATOM 1407 O O . ARG A 1 175 ? 6.481 1.293 67.844 1.00 31.12 ? 175 ARG A O 1 ATOM 1408 C CB . ARG A 1 175 ? 3.259 0.825 68.344 1.00 32.84 ? 175 ARG A CB 1 ATOM 1409 C CG . ARG A 1 175 ? 1.994 1.490 68.770 1.00 41.95 ? 175 ARG A CG 1 ATOM 1410 C CD . ARG A 1 175 ? 1.532 0.920 70.126 1.00 52.07 ? 175 ARG A CD 1 ATOM 1411 N NE . ARG A 1 175 ? 2.628 0.962 71.113 1.00 57.70 ? 175 ARG A NE 1 ATOM 1412 C CZ . ARG A 1 175 ? 3.012 -0.053 71.892 1.00 61.94 ? 175 ARG A CZ 1 ATOM 1413 N NH1 . ARG A 1 175 ? 2.387 -1.242 71.844 1.00 63.42 ? 175 ARG A NH1 1 ATOM 1414 N NH2 . ARG A 1 175 ? 4.035 0.126 72.728 1.00 63.58 ? 175 ARG A NH2 1 ATOM 1415 N N . HIS A 1 176 ? 5.491 -0.243 66.514 1.00 27.61 ? 176 HIS A N 1 ATOM 1416 C CA . HIS A 1 176 ? 6.694 -1.048 66.352 1.00 26.26 ? 176 HIS A CA 1 ATOM 1417 C C . HIS A 1 176 ? 7.634 -0.755 65.183 1.00 24.94 ? 176 HIS A C 1 ATOM 1418 O O . HIS A 1 176 ? 8.704 -1.313 65.162 1.00 25.34 ? 176 HIS A O 1 ATOM 1419 C CB . HIS A 1 176 ? 6.291 -2.497 66.286 1.00 26.50 ? 176 HIS A CB 1 ATOM 1420 C CG . HIS A 1 176 ? 5.376 -2.881 67.370 1.00 27.49 ? 176 HIS A CG 1 ATOM 1421 N ND1 . HIS A 1 176 ? 5.723 -2.811 68.696 1.00 26.09 ? 176 HIS A ND1 1 ATOM 1422 C CD2 . HIS A 1 176 ? 4.112 -3.349 67.322 1.00 33.15 ? 176 HIS A CD2 1 ATOM 1423 C CE1 . HIS A 1 176 ? 4.694 -3.200 69.424 1.00 33.07 ? 176 HIS A CE1 1 ATOM 1424 N NE2 . HIS A 1 176 ? 3.700 -3.528 68.614 1.00 35.76 ? 176 HIS A NE2 1 ATOM 1425 N N . LEU A 1 177 ? 7.235 0.080 64.220 1.00 22.45 ? 177 LEU A N 1 ATOM 1426 C CA . LEU A 1 177 ? 8.062 0.380 63.073 1.00 19.32 ? 177 LEU A CA 1 ATOM 1427 C C . LEU A 1 177 ? 8.818 1.625 63.273 1.00 19.61 ? 177 LEU A C 1 ATOM 1428 O O . LEU A 1 177 ? 8.284 2.563 63.823 1.00 20.60 ? 177 LEU A O 1 ATOM 1429 C CB . LEU A 1 177 ? 7.206 0.507 61.828 1.00 18.10 ? 177 LEU A CB 1 ATOM 1430 C CG . LEU A 1 177 ? 6.581 -0.852 61.357 1.00 15.49 ? 177 LEU A CG 1 ATOM 1431 C CD1 . LEU A 1 177 ? 5.736 -0.657 60.122 1.00 7.13 ? 177 LEU A CD1 1 ATOM 1432 C CD2 . LEU A 1 177 ? 7.703 -1.853 61.126 1.00 11.99 ? 177 LEU A CD2 1 ATOM 1433 N N . ASP A 1 178 ? 10.076 1.624 62.831 1.00 20.49 ? 178 ASP A N 1 ATOM 1434 C CA . ASP A 1 178 ? 10.968 2.781 62.941 1.00 21.65 ? 178 ASP A CA 1 ATOM 1435 C C . ASP A 1 178 ? 10.548 3.890 61.945 1.00 20.16 ? 178 ASP A C 1 ATOM 1436 O O . ASP A 1 178 ? 10.808 5.064 62.130 1.00 19.18 ? 178 ASP A O 1 ATOM 1437 C CB . ASP A 1 178 ? 12.425 2.354 62.723 1.00 22.51 ? 178 ASP A CB 1 ATOM 1438 C CG . ASP A 1 178 ? 12.970 1.585 63.914 1.00 28.32 ? 178 ASP A CG 1 ATOM 1439 O OD1 . ASP A 1 178 ? 13.063 2.178 65.007 1.00 32.54 ? 178 ASP A OD1 1 ATOM 1440 O OD2 . ASP A 1 178 ? 13.307 0.380 63.836 1.00 35.71 ? 178 ASP A OD2 1 ATOM 1441 N N . PHE A 1 179 ? 9.898 3.469 60.869 1.00 19.34 ? 179 PHE A N 1 ATOM 1442 C CA . PHE A 1 179 ? 9.352 4.353 59.848 1.00 16.61 ? 179 PHE A CA 1 ATOM 1443 C C . PHE A 1 179 ? 8.500 3.595 58.829 1.00 14.60 ? 179 PHE A C 1 ATOM 1444 O O . PHE A 1 179 ? 8.667 2.427 58.603 1.00 13.68 ? 179 PHE A O 1 ATOM 1445 C CB . PHE A 1 179 ? 10.437 5.218 59.154 1.00 16.99 ? 179 PHE A CB 1 ATOM 1446 C CG . PHE A 1 179 ? 11.490 4.478 58.337 1.00 15.04 ? 179 PHE A CG 1 ATOM 1447 C CD1 . PHE A 1 179 ? 12.706 4.183 58.867 1.00 10.56 ? 179 PHE A CD1 1 ATOM 1448 C CD2 . PHE A 1 179 ? 11.291 4.233 57.017 1.00 14.66 ? 179 PHE A CD2 1 ATOM 1449 C CE1 . PHE A 1 179 ? 13.652 3.620 58.125 1.00 10.30 ? 179 PHE A CE1 1 ATOM 1450 C CE2 . PHE A 1 179 ? 12.243 3.624 56.277 1.00 11.86 ? 179 PHE A CE2 1 ATOM 1451 C CZ . PHE A 1 179 ? 13.420 3.338 56.828 1.00 12.28 ? 179 PHE A CZ 1 ATOM 1452 N N . ILE A 1 180 ? 7.589 4.316 58.238 1.00 14.03 ? 180 ILE A N 1 ATOM 1453 C CA . ILE A 1 180 ? 6.619 3.816 57.316 1.00 14.16 ? 180 ILE A CA 1 ATOM 1454 C C . ILE A 1 180 ? 6.756 4.569 55.982 1.00 14.10 ? 180 ILE A C 1 ATOM 1455 O O . ILE A 1 180 ? 6.752 5.799 55.956 1.00 16.20 ? 180 ILE A O 1 ATOM 1456 C CB . ILE A 1 180 ? 5.261 3.965 57.999 1.00 14.31 ? 180 ILE A CB 1 ATOM 1457 C CG1 . ILE A 1 180 ? 5.168 2.977 59.126 1.00 15.93 ? 180 ILE A CG1 1 ATOM 1458 C CG2 . ILE A 1 180 ? 4.157 3.734 57.048 1.00 17.26 ? 180 ILE A CG2 1 ATOM 1459 C CD1 . ILE A 1 180 ? 3.852 3.001 59.858 1.00 21.74 ? 180 ILE A CD1 1 ATOM 1460 N N . SER A 1 181 ? 6.910 3.850 54.877 1.00 13.40 ? 181 SER A N 1 ATOM 1461 C CA . SER A 1 181 ? 7.094 4.508 53.587 1.00 11.90 ? 181 SER A CA 1 ATOM 1462 C C . SER A 1 181 ? 5.818 4.402 52.821 1.00 9.97 ? 181 SER A C 1 ATOM 1463 O O . SER A 1 181 ? 5.325 3.332 52.644 1.00 7.87 ? 181 SER A O 1 ATOM 1464 C CB . SER A 1 181 ? 8.218 3.840 52.797 1.00 13.37 ? 181 SER A CB 1 ATOM 1465 O OG . SER A 1 181 ? 9.452 3.855 53.509 1.00 16.41 ? 181 SER A OG 1 ATOM 1466 N N . LEU A 1 182 ? 5.290 5.537 52.371 1.00 10.29 ? 182 LEU A N 1 ATOM 1467 C CA . LEU A 1 182 ? 4.043 5.579 51.631 1.00 10.82 ? 182 LEU A CA 1 ATOM 1468 C C . LEU A 1 182 ? 4.208 5.474 50.164 1.00 10.37 ? 182 LEU A C 1 ATOM 1469 O O . LEU A 1 182 ? 4.683 6.389 49.568 1.00 11.29 ? 182 LEU A O 1 ATOM 1470 C CB . LEU A 1 182 ? 3.282 6.860 51.928 1.00 11.62 ? 182 LEU A CB 1 ATOM 1471 C CG . LEU A 1 182 ? 2.080 6.813 52.899 1.00 14.68 ? 182 LEU A CG 1 ATOM 1472 C CD1 . LEU A 1 182 ? 1.232 8.084 52.765 1.00 11.51 ? 182 LEU A CD1 1 ATOM 1473 C CD2 . LEU A 1 182 ? 1.197 5.612 52.570 1.00 18.80 ? 182 LEU A CD2 1 ATOM 1474 N N . LEU A 1 183 ? 3.771 4.357 49.574 1.00 10.88 ? 183 LEU A N 1 ATOM 1475 C CA . LEU A 1 183 ? 3.852 4.136 48.138 1.00 11.26 ? 183 LEU A CA 1 ATOM 1476 C C . LEU A 1 183 ? 2.850 5.065 47.403 1.00 11.66 ? 183 LEU A C 1 ATOM 1477 O O . LEU A 1 183 ? 1.864 4.638 46.816 1.00 12.04 ? 183 LEU A O 1 ATOM 1478 C CB . LEU A 1 183 ? 3.572 2.680 47.819 1.00 11.42 ? 183 LEU A CB 1 ATOM 1479 C CG . LEU A 1 183 ? 4.531 1.675 48.426 1.00 12.82 ? 183 LEU A CG 1 ATOM 1480 C CD1 . LEU A 1 183 ? 4.384 0.339 47.678 1.00 16.54 ? 183 LEU A CD1 1 ATOM 1481 C CD2 . LEU A 1 183 ? 5.967 2.136 48.306 1.00 12.72 ? 183 LEU A CD2 1 ATOM 1482 N N . THR A 1 184 ? 3.104 6.362 47.440 1.00 11.62 ? 184 THR A N 1 ATOM 1483 C CA . THR A 1 184 ? 2.213 7.291 46.801 1.00 12.25 ? 184 THR A CA 1 ATOM 1484 C C . THR A 1 184 ? 2.538 7.544 45.352 1.00 14.59 ? 184 THR A C 1 ATOM 1485 O O . THR A 1 184 ? 2.870 8.641 44.976 1.00 11.89 ? 184 THR A O 1 ATOM 1486 C CB . THR A 1 184 ? 2.204 8.626 47.550 1.00 12.07 ? 184 THR A CB 1 ATOM 1487 O OG1 . THR A 1 184 ? 3.501 8.893 48.099 1.00 12.19 ? 184 THR A OG1 1 ATOM 1488 C CG2 . THR A 1 184 ? 1.265 8.602 48.719 1.00 12.51 ? 184 THR A CG2 1 ATOM 1489 N N . TYR A 1 185 ? 2.415 6.523 44.518 1.00 20.09 ? 185 TYR A N 1 ATOM 1490 C CA . TYR A 1 185 ? 2.688 6.703 43.098 1.00 24.92 ? 185 TYR A CA 1 ATOM 1491 C C . TYR A 1 185 ? 2.059 5.717 42.129 1.00 30.41 ? 185 TYR A C 1 ATOM 1492 O O . TYR A 1 185 ? 2.184 5.885 40.911 1.00 33.54 ? 185 TYR A O 1 ATOM 1493 C CB . TYR A 1 185 ? 4.196 6.791 42.833 1.00 23.69 ? 185 TYR A CB 1 ATOM 1494 C CG . TYR A 1 185 ? 5.069 5.767 43.557 1.00 22.66 ? 185 TYR A CG 1 ATOM 1495 C CD1 . TYR A 1 185 ? 4.925 4.409 43.363 1.00 19.37 ? 185 TYR A CD1 1 ATOM 1496 C CD2 . TYR A 1 185 ? 6.079 6.189 44.426 1.00 21.98 ? 185 TYR A CD2 1 ATOM 1497 C CE1 . TYR A 1 185 ? 5.751 3.509 44.016 1.00 19.48 ? 185 TYR A CE1 1 ATOM 1498 C CE2 . TYR A 1 185 ? 6.896 5.290 45.080 1.00 18.61 ? 185 TYR A CE2 1 ATOM 1499 C CZ . TYR A 1 185 ? 6.727 3.958 44.875 1.00 19.07 ? 185 TYR A CZ 1 ATOM 1500 O OH . TYR A 1 185 ? 7.550 3.041 45.506 1.00 21.22 ? 185 TYR A OH 1 ATOM 1501 N N . ASP A 1 186 ? 1.371 4.701 42.616 1.00 35.83 ? 186 ASP A N 1 ATOM 1502 C CA . ASP A 1 186 ? 0.742 3.748 41.684 1.00 40.93 ? 186 ASP A CA 1 ATOM 1503 C C . ASP A 1 186 ? -0.753 4.007 41.474 1.00 42.80 ? 186 ASP A C 1 ATOM 1504 O O . ASP A 1 186 ? -1.459 3.182 40.940 1.00 43.72 ? 186 ASP A O 1 ATOM 1505 C CB . ASP A 1 186 ? 0.950 2.320 42.182 1.00 42.72 ? 186 ASP A CB 1 ATOM 1506 C CG . ASP A 1 186 ? 2.344 1.757 41.790 1.00 47.32 ? 186 ASP A CG 1 ATOM 1507 O OD1 . ASP A 1 186 ? 2.814 0.771 42.458 1.00 52.70 ? 186 ASP A OD1 1 ATOM 1508 O OD2 . ASP A 1 186 ? 2.995 2.256 40.811 1.00 43.41 ? 186 ASP A OD2 1 ATOM 1509 N N . PHE A 1 187 ? -1.208 5.169 41.896 1.00 45.38 ? 187 PHE A N 1 ATOM 1510 C CA . PHE A 1 187 ? -2.600 5.553 41.830 1.00 47.96 ? 187 PHE A CA 1 ATOM 1511 C C . PHE A 1 187 ? -3.377 5.171 40.570 1.00 52.57 ? 187 PHE A C 1 ATOM 1512 O O . PHE A 1 187 ? -4.382 4.417 40.664 1.00 54.32 ? 187 PHE A O 1 ATOM 1513 C CB . PHE A 1 187 ? -2.722 7.037 42.141 1.00 46.31 ? 187 PHE A CB 1 ATOM 1514 C CG . PHE A 1 187 ? -2.450 7.361 43.589 1.00 42.55 ? 187 PHE A CG 1 ATOM 1515 C CD1 . PHE A 1 187 ? -3.053 6.650 44.596 1.00 39.16 ? 187 PHE A CD1 1 ATOM 1516 C CD2 . PHE A 1 187 ? -1.583 8.374 43.939 1.00 41.34 ? 187 PHE A CD2 1 ATOM 1517 C CE1 . PHE A 1 187 ? -2.808 6.954 45.927 1.00 37.87 ? 187 PHE A CE1 1 ATOM 1518 C CE2 . PHE A 1 187 ? -1.334 8.676 45.279 1.00 40.57 ? 187 PHE A CE2 1 ATOM 1519 C CZ . PHE A 1 187 ? -1.956 7.960 46.264 1.00 38.20 ? 187 PHE A CZ 1 ATOM 1520 N N . HIS A 1 188 ? -2.976 5.680 39.405 1.00 56.89 ? 188 HIS A N 1 ATOM 1521 C CA . HIS A 1 188 ? -3.662 5.290 38.172 1.00 60.21 ? 188 HIS A CA 1 ATOM 1522 C C . HIS A 1 188 ? -3.089 3.913 37.879 1.00 64.90 ? 188 HIS A C 1 ATOM 1523 O O . HIS A 1 188 ? -2.277 3.699 36.946 1.00 64.17 ? 188 HIS A O 1 ATOM 1524 C CB . HIS A 1 188 ? -3.380 6.231 37.038 1.00 59.22 ? 188 HIS A CB 1 ATOM 1525 C CG . HIS A 1 188 ? -4.475 6.287 36.025 1.00 58.12 ? 188 HIS A CG 1 ATOM 1526 N ND1 . HIS A 1 188 ? -4.575 5.398 34.981 1.00 54.50 ? 188 HIS A ND1 1 ATOM 1527 C CD2 . HIS A 1 188 ? -5.521 7.142 35.898 1.00 58.64 ? 188 HIS A CD2 1 ATOM 1528 C CE1 . HIS A 1 188 ? -5.637 5.702 34.260 1.00 56.32 ? 188 HIS A CE1 1 ATOM 1529 N NE2 . HIS A 1 188 ? -6.224 6.761 34.788 1.00 57.08 ? 188 HIS A NE2 1 ATOM 1530 N N . GLY A 1 189 ? -3.569 3.003 38.731 1.00 70.17 ? 189 GLY A N 1 ATOM 1531 C CA . GLY A 1 189 ? -3.222 1.601 38.735 1.00 73.97 ? 189 GLY A CA 1 ATOM 1532 C C . GLY A 1 189 ? -3.773 0.714 37.633 1.00 76.96 ? 189 GLY A C 1 ATOM 1533 O O . GLY A 1 189 ? -4.972 0.683 37.314 1.00 77.59 ? 189 GLY A O 1 ATOM 1534 N N . ALA A 1 190 ? -2.788 -0.025 37.103 1.00 80.08 ? 190 ALA A N 1 ATOM 1535 C CA . ALA A 1 190 ? -2.808 -1.093 36.061 1.00 83.00 ? 190 ALA A CA 1 ATOM 1536 C C . ALA A 1 190 ? -4.058 -1.178 35.200 1.00 84.31 ? 190 ALA A C 1 ATOM 1537 O O . ALA A 1 190 ? -3.978 -1.159 33.977 1.00 84.51 ? 190 ALA A O 1 ATOM 1538 C CB . ALA A 1 190 ? -2.525 -2.448 36.711 1.00 84.04 ? 190 ALA A CB 1 ATOM 1539 N N . TRP A 1 191 ? -5.207 -1.268 35.811 1.00 85.45 ? 191 TRP A N 1 ATOM 1540 C CA . TRP A 1 191 ? -6.426 -1.089 34.908 1.00 86.51 ? 191 TRP A CA 1 ATOM 1541 C C . TRP A 1 191 ? -6.784 -0.076 33.822 1.00 84.90 ? 191 TRP A C 1 ATOM 1542 O O . TRP A 1 191 ? -6.025 0.200 32.898 1.00 84.64 ? 191 TRP A O 1 ATOM 1543 C CB . TRP A 1 191 ? -7.527 -1.162 35.946 1.00 88.51 ? 191 TRP A CB 1 ATOM 1544 C CG . TRP A 1 191 ? -8.062 0.034 36.714 1.00 93.37 ? 191 TRP A CG 1 ATOM 1545 C CD1 . TRP A 1 191 ? -7.710 1.384 36.742 1.00 96.64 ? 191 TRP A CD1 1 ATOM 1546 C CD2 . TRP A 1 191 ? -9.155 -0.117 37.591 1.00 96.99 ? 191 TRP A CD2 1 ATOM 1547 N NE1 . TRP A 1 191 ? -8.556 2.046 37.619 1.00 98.20 ? 191 TRP A NE1 1 ATOM 1548 C CE2 . TRP A 1 191 ? -9.451 1.137 38.160 1.00 97.80 ? 191 TRP A CE2 1 ATOM 1549 C CE3 . TRP A 1 191 ? -9.917 -1.232 37.955 1.00 98.02 ? 191 TRP A CE3 1 ATOM 1550 C CZ2 . TRP A 1 191 ? -10.499 1.296 39.091 1.00 97.28 ? 191 TRP A CZ2 1 ATOM 1551 C CZ3 . TRP A 1 191 ? -10.929 -1.077 38.863 1.00 99.14 ? 191 TRP A CZ3 1 ATOM 1552 C CH2 . TRP A 1 191 ? -11.217 0.172 39.429 1.00 98.02 ? 191 TRP A CH2 1 ATOM 1553 N N . ARG A 1 192 ? -8.005 0.418 33.992 1.00 83.34 ? 192 ARG A N 1 ATOM 1554 C CA . ARG A 1 192 ? -8.738 1.402 33.201 1.00 81.57 ? 192 ARG A CA 1 ATOM 1555 C C . ARG A 1 192 ? -8.009 2.149 32.127 1.00 77.79 ? 192 ARG A C 1 ATOM 1556 O O . ARG A 1 192 ? -6.904 2.640 32.290 1.00 77.93 ? 192 ARG A O 1 ATOM 1557 C CB . ARG A 1 192 ? -9.527 2.320 34.134 1.00 82.88 ? 192 ARG A CB 1 ATOM 1558 C CG . ARG A 1 192 ? -10.941 1.755 34.366 1.00 86.55 ? 192 ARG A CG 1 ATOM 1559 C CD . ARG A 1 192 ? -11.515 1.095 33.088 1.00 90.95 ? 192 ARG A CD 1 ATOM 1560 N NE . ARG A 1 192 ? -10.920 -0.221 32.800 1.00 93.33 ? 192 ARG A NE 1 ATOM 1561 C CZ . ARG A 1 192 ? -11.151 -0.915 31.684 1.00 94.22 ? 192 ARG A CZ 1 ATOM 1562 N NH1 . ARG A 1 192 ? -11.967 -0.422 30.750 1.00 93.85 ? 192 ARG A NH1 1 ATOM 1563 N NH2 . ARG A 1 192 ? -10.573 -2.099 31.506 1.00 94.38 ? 192 ARG A NH2 1 ATOM 1564 N N . GLN A 1 193 ? -8.734 2.182 31.013 1.00 72.71 ? 193 GLN A N 1 ATOM 1565 C CA . GLN A 1 193 ? -8.285 2.721 29.779 1.00 68.57 ? 193 GLN A CA 1 ATOM 1566 C C . GLN A 1 193 ? -8.609 4.192 29.590 1.00 63.38 ? 193 GLN A C 1 ATOM 1567 O O . GLN A 1 193 ? -9.315 4.555 28.671 1.00 61.89 ? 193 GLN A O 1 ATOM 1568 C CB . GLN A 1 193 ? -8.893 1.910 28.631 1.00 69.94 ? 193 GLN A CB 1 ATOM 1569 C CG . GLN A 1 193 ? -10.401 1.664 28.706 1.00 73.47 ? 193 GLN A CG 1 ATOM 1570 C CD . GLN A 1 193 ? -11.108 2.004 27.375 1.00 76.38 ? 193 GLN A CD 1 ATOM 1571 O OE1 . GLN A 1 193 ? -11.832 2.995 27.304 1.00 77.44 ? 193 GLN A OE1 1 ATOM 1572 N NE2 . GLN A 1 193 ? -10.924 1.243 26.291 1.00 76.88 ? 193 GLN A NE2 1 ATOM 1573 N N . THR A 1 194 ? -8.079 5.034 30.457 1.00 57.71 ? 194 THR A N 1 ATOM 1574 C CA . THR A 1 194 ? -8.193 6.469 30.298 1.00 54.04 ? 194 THR A CA 1 ATOM 1575 C C . THR A 1 194 ? -6.847 6.993 30.667 1.00 49.32 ? 194 THR A C 1 ATOM 1576 O O . THR A 1 194 ? -6.207 6.450 31.504 1.00 50.04 ? 194 THR A O 1 ATOM 1577 C CB . THR A 1 194 ? -9.216 7.126 31.263 1.00 54.75 ? 194 THR A CB 1 ATOM 1578 O OG1 . THR A 1 194 ? -9.293 6.392 32.509 1.00 56.30 ? 194 THR A OG1 1 ATOM 1579 C CG2 . THR A 1 194 ? -10.604 7.159 30.633 1.00 55.43 ? 194 THR A CG2 1 ATOM 1580 N N . VAL A 1 195 ? -6.407 8.048 30.034 1.00 44.58 ? 195 VAL A N 1 ATOM 1581 C CA . VAL A 1 195 ? -5.127 8.639 30.336 1.00 39.80 ? 195 VAL A CA 1 ATOM 1582 C C . VAL A 1 195 ? -5.280 9.205 31.733 1.00 36.85 ? 195 VAL A C 1 ATOM 1583 O O . VAL A 1 195 ? -6.373 9.586 32.111 1.00 36.64 ? 195 VAL A O 1 ATOM 1584 C CB . VAL A 1 195 ? -4.804 9.723 29.303 1.00 39.46 ? 195 VAL A CB 1 ATOM 1585 C CG1 . VAL A 1 195 ? -3.978 10.804 29.910 1.00 38.56 ? 195 VAL A CG1 1 ATOM 1586 C CG2 . VAL A 1 195 ? -4.099 9.108 28.116 1.00 38.39 ? 195 VAL A CG2 1 ATOM 1587 N N . GLY A 1 196 ? -4.207 9.222 32.504 1.00 32.83 ? 196 GLY A N 1 ATOM 1588 C CA . GLY A 1 196 ? -4.262 9.742 33.841 1.00 29.78 ? 196 GLY A CA 1 ATOM 1589 C C . GLY A 1 196 ? -2.889 9.733 34.467 1.00 28.21 ? 196 GLY A C 1 ATOM 1590 O O . GLY A 1 196 ? -2.014 8.994 34.017 1.00 27.94 ? 196 GLY A O 1 ATOM 1591 N N . HIS A 1 197 ? -2.686 10.547 35.511 1.00 25.63 ? 197 HIS A N 1 ATOM 1592 C CA . HIS A 1 197 ? -1.380 10.649 36.183 1.00 22.41 ? 197 HIS A CA 1 ATOM 1593 C C . HIS A 1 197 ? -1.328 9.740 37.430 1.00 21.14 ? 197 HIS A C 1 ATOM 1594 O O . HIS A 1 197 ? -2.145 9.806 38.305 1.00 22.04 ? 197 HIS A O 1 ATOM 1595 C CB . HIS A 1 197 ? -1.096 12.090 36.542 1.00 20.60 ? 197 HIS A CB 1 ATOM 1596 C CG . HIS A 1 197 ? 0.334 12.385 36.762 1.00 20.41 ? 197 HIS A CG 1 ATOM 1597 N ND1 . HIS A 1 197 ? 1.076 11.777 37.749 1.00 21.35 ? 197 HIS A ND1 1 ATOM 1598 C CD2 . HIS A 1 197 ? 1.174 13.246 36.138 1.00 22.65 ? 197 HIS A CD2 1 ATOM 1599 C CE1 . HIS A 1 197 ? 2.321 12.231 37.715 1.00 19.66 ? 197 HIS A CE1 1 ATOM 1600 N NE2 . HIS A 1 197 ? 2.408 13.133 36.751 1.00 21.61 ? 197 HIS A NE2 1 ATOM 1601 N N . HIS A 1 198 ? -0.317 8.900 37.501 1.00 19.57 ? 198 HIS A N 1 ATOM 1602 C CA . HIS A 1 198 ? -0.147 7.955 38.561 1.00 17.78 ? 198 HIS A CA 1 ATOM 1603 C C . HIS A 1 198 ? 0.263 8.536 39.849 1.00 17.20 ? 198 HIS A C 1 ATOM 1604 O O . HIS A 1 198 ? 0.033 7.941 40.843 1.00 20.15 ? 198 HIS A O 1 ATOM 1605 C CB . HIS A 1 198 ? 0.872 6.904 38.145 1.00 17.64 ? 198 HIS A CB 1 ATOM 1606 C CG . HIS A 1 198 ? 2.236 7.463 37.951 1.00 17.34 ? 198 HIS A CG 1 ATOM 1607 N ND1 . HIS A 1 198 ? 3.225 7.363 38.904 1.00 16.22 ? 198 HIS A ND1 1 ATOM 1608 C CD2 . HIS A 1 198 ? 2.779 8.151 36.917 1.00 17.31 ? 198 HIS A CD2 1 ATOM 1609 C CE1 . HIS A 1 198 ? 4.313 7.975 38.478 1.00 15.55 ? 198 HIS A CE1 1 ATOM 1610 N NE2 . HIS A 1 198 ? 4.072 8.459 37.274 1.00 18.07 ? 198 HIS A NE2 1 ATOM 1611 N N . SER A 1 199 ? 0.907 9.669 39.899 1.00 17.36 ? 199 SER A N 1 ATOM 1612 C CA . SER A 1 199 ? 1.282 10.217 41.210 1.00 18.12 ? 199 SER A CA 1 ATOM 1613 C C . SER A 1 199 ? 0.919 11.680 41.390 1.00 19.32 ? 199 SER A C 1 ATOM 1614 O O . SER A 1 199 ? 1.781 12.513 41.623 1.00 20.24 ? 199 SER A O 1 ATOM 1615 C CB . SER A 1 199 ? 2.772 10.033 41.467 1.00 17.80 ? 199 SER A CB 1 ATOM 1616 O OG . SER A 1 199 ? 3.529 10.813 40.604 1.00 17.53 ? 199 SER A OG 1 ATOM 1617 N N . PRO A 1 200 ? -0.355 12.018 41.307 1.00 19.99 ? 200 PRO A N 1 ATOM 1618 C CA . PRO A 1 200 ? -0.705 13.419 41.447 1.00 20.40 ? 200 PRO A CA 1 ATOM 1619 C C . PRO A 1 200 ? -0.647 13.798 42.885 1.00 19.40 ? 200 PRO A C 1 ATOM 1620 O O . PRO A 1 200 ? -0.837 12.956 43.725 1.00 18.71 ? 200 PRO A O 1 ATOM 1621 C CB . PRO A 1 200 ? -2.117 13.457 40.908 1.00 22.34 ? 200 PRO A CB 1 ATOM 1622 C CG . PRO A 1 200 ? -2.681 12.151 41.365 1.00 22.99 ? 200 PRO A CG 1 ATOM 1623 C CD . PRO A 1 200 ? -1.545 11.169 41.130 1.00 20.00 ? 200 PRO A CD 1 ATOM 1624 N N . LEU A 1 201 ? -0.373 15.064 43.143 1.00 19.63 ? 201 LEU A N 1 ATOM 1625 C CA . LEU A 1 201 ? -0.252 15.582 44.506 1.00 20.68 ? 201 LEU A CA 1 ATOM 1626 C C . LEU A 1 201 ? -1.572 15.894 45.151 1.00 24.39 ? 201 LEU A C 1 ATOM 1627 O O . LEU A 1 201 ? -1.764 15.509 46.305 1.00 24.32 ? 201 LEU A O 1 ATOM 1628 C CB . LEU A 1 201 ? 0.612 16.846 44.555 1.00 18.42 ? 201 LEU A CB 1 ATOM 1629 C CG . LEU A 1 201 ? 0.842 17.449 45.953 1.00 13.58 ? 201 LEU A CG 1 ATOM 1630 C CD1 . LEU A 1 201 ? 1.410 16.432 46.871 1.00 12.15 ? 201 LEU A CD1 1 ATOM 1631 C CD2 . LEU A 1 201 ? 1.786 18.554 45.906 1.00 12.18 ? 201 LEU A CD2 1 ATOM 1632 N N . PHE A 1 202 ? -2.459 16.588 44.413 1.00 28.66 ? 202 PHE A N 1 ATOM 1633 C CA . PHE A 1 202 ? -3.755 16.965 44.918 1.00 31.76 ? 202 PHE A CA 1 ATOM 1634 C C . PHE A 1 202 ? -4.890 16.308 44.188 1.00 38.17 ? 202 PHE A C 1 ATOM 1635 O O . PHE A 1 202 ? -4.680 15.469 43.341 1.00 38.85 ? 202 PHE A O 1 ATOM 1636 C CB . PHE A 1 202 ? -3.890 18.462 44.878 1.00 30.53 ? 202 PHE A CB 1 ATOM 1637 C CG . PHE A 1 202 ? -3.039 19.167 45.877 1.00 26.72 ? 202 PHE A CG 1 ATOM 1638 C CD1 . PHE A 1 202 ? -3.187 18.947 47.231 1.00 23.19 ? 202 PHE A CD1 1 ATOM 1639 C CD2 . PHE A 1 202 ? -2.074 20.031 45.468 1.00 26.71 ? 202 PHE A CD2 1 ATOM 1640 C CE1 . PHE A 1 202 ? -2.389 19.574 48.150 1.00 20.89 ? 202 PHE A CE1 1 ATOM 1641 C CE2 . PHE A 1 202 ? -1.258 20.673 46.407 1.00 25.70 ? 202 PHE A CE2 1 ATOM 1642 C CZ . PHE A 1 202 ? -1.443 20.450 47.743 1.00 21.73 ? 202 PHE A CZ 1 ATOM 1643 N N . ARG A 1 203 ? -6.109 16.691 44.523 1.00 46.90 ? 203 ARG A N 1 ATOM 1644 C CA . ARG A 1 203 ? -7.292 16.089 43.913 1.00 54.69 ? 203 ARG A CA 1 ATOM 1645 C C . ARG A 1 203 ? -7.510 16.478 42.490 1.00 58.47 ? 203 ARG A C 1 ATOM 1646 O O . ARG A 1 203 ? -8.301 15.857 41.806 1.00 59.45 ? 203 ARG A O 1 ATOM 1647 C CB . ARG A 1 203 ? -8.542 16.450 44.697 1.00 57.80 ? 203 ARG A CB 1 ATOM 1648 C CG . ARG A 1 203 ? -9.842 16.053 44.016 1.00 63.46 ? 203 ARG A CG 1 ATOM 1649 C CD . ARG A 1 203 ? -11.047 16.476 44.854 1.00 70.28 ? 203 ARG A CD 1 ATOM 1650 N NE . ARG A 1 203 ? -10.985 17.904 45.205 1.00 75.58 ? 203 ARG A NE 1 ATOM 1651 C CZ . ARG A 1 203 ? -11.534 18.432 46.296 1.00 79.34 ? 203 ARG A CZ 1 ATOM 1652 N NH1 . ARG A 1 203 ? -12.197 17.658 47.164 1.00 81.53 ? 203 ARG A NH1 1 ATOM 1653 N NH2 . ARG A 1 203 ? -11.436 19.734 46.522 1.00 80.50 ? 203 ARG A NH2 1 ATOM 1654 N N . GLY A 1 204 ? -6.830 17.496 42.012 1.00 63.81 ? 204 GLY A N 1 ATOM 1655 C CA . GLY A 1 204 ? -7.066 17.878 40.629 1.00 69.43 ? 204 GLY A CA 1 ATOM 1656 C C . GLY A 1 204 ? -8.549 18.193 40.508 1.00 73.65 ? 204 GLY A C 1 ATOM 1657 O O . GLY A 1 204 ? -9.239 17.709 39.609 1.00 73.50 ? 204 GLY A O 1 ATOM 1658 N N . ASN A 1 205 ? -9.014 18.998 41.470 1.00 78.83 ? 205 ASN A N 1 ATOM 1659 C CA . ASN A 1 205 ? -10.396 19.475 41.620 1.00 82.76 ? 205 ASN A CA 1 ATOM 1660 C C . ASN A 1 205 ? -11.278 19.612 40.352 1.00 85.43 ? 205 ASN A C 1 ATOM 1661 O O . ASN A 1 205 ? -12.447 20.027 40.438 1.00 86.52 ? 205 ASN A O 1 ATOM 1662 C CB . ASN A 1 205 ? -10.349 20.809 42.385 1.00 82.92 ? 205 ASN A CB 1 ATOM 1663 C CG . ASN A 1 205 ? -11.280 21.853 41.802 1.00 83.56 ? 205 ASN A CG 1 ATOM 1664 O OD1 . ASN A 1 205 ? -12.413 22.026 42.276 1.00 83.69 ? 205 ASN A OD1 1 ATOM 1665 N ND2 . ASN A 1 205 ? -10.816 22.550 40.762 1.00 82.83 ? 205 ASN A ND2 1 ATOM 1666 N N . SER A 1 206 ? -10.730 19.281 39.188 1.00 87.51 ? 206 SER A N 1 ATOM 1667 C CA . SER A 1 206 ? -11.498 19.333 37.957 1.00 89.45 ? 206 SER A CA 1 ATOM 1668 C C . SER A 1 206 ? -11.968 17.907 37.681 1.00 90.97 ? 206 SER A C 1 ATOM 1669 O O . SER A 1 206 ? -12.635 17.633 36.687 1.00 91.63 ? 206 SER A O 1 ATOM 1670 C CB . SER A 1 206 ? -10.630 19.850 36.807 1.00 89.49 ? 206 SER A CB 1 ATOM 1671 O OG . SER A 1 206 ? -11.424 20.190 35.674 1.00 90.47 ? 206 SER A OG 1 ATOM 1672 N N . ASP A 1 207 ? -11.594 17.007 38.586 1.00 92.49 ? 207 ASP A N 1 ATOM 1673 C CA . ASP A 1 207 ? -11.933 15.589 38.526 1.00 93.73 ? 207 ASP A CA 1 ATOM 1674 C C . ASP A 1 207 ? -12.866 15.266 39.698 1.00 94.44 ? 207 ASP A C 1 ATOM 1675 O O . ASP A 1 207 ? -12.538 15.557 40.858 1.00 95.68 ? 207 ASP A O 1 ATOM 1676 C CB . ASP A 1 207 ? -10.659 14.755 38.663 1.00 94.02 ? 207 ASP A CB 1 ATOM 1677 C CG . ASP A 1 207 ? -10.938 13.286 38.748 1.00 95.00 ? 207 ASP A CG 1 ATOM 1678 O OD1 . ASP A 1 207 ? -10.096 12.545 39.324 1.00 94.88 ? 207 ASP A OD1 1 ATOM 1679 O OD2 . ASP A 1 207 ? -11.988 12.826 38.238 1.00 96.25 ? 207 ASP A OD2 1 ATOM 1680 N N . ALA A 1 208 ? -14.012 14.649 39.421 1.00 94.02 ? 208 ALA A N 1 ATOM 1681 C CA . ALA A 1 208 ? -14.982 14.360 40.485 1.00 92.87 ? 208 ALA A CA 1 ATOM 1682 C C . ALA A 1 208 ? -15.024 12.935 41.081 1.00 91.89 ? 208 ALA A C 1 ATOM 1683 O O . ALA A 1 208 ? -15.309 12.778 42.283 1.00 91.82 ? 208 ALA A O 1 ATOM 1684 C CB . ALA A 1 208 ? -16.370 14.749 40.008 1.00 93.26 ? 208 ALA A CB 1 ATOM 1685 N N . SER A 1 209 ? -14.752 11.907 40.265 1.00 90.20 ? 209 SER A N 1 ATOM 1686 C CA . SER A 1 209 ? -14.862 10.494 40.707 1.00 88.14 ? 209 SER A CA 1 ATOM 1687 C C . SER A 1 209 ? -14.010 9.951 41.869 1.00 85.70 ? 209 SER A C 1 ATOM 1688 O O . SER A 1 209 ? -14.573 9.503 42.888 1.00 85.86 ? 209 SER A O 1 ATOM 1689 C CB . SER A 1 209 ? -14.712 9.548 39.515 1.00 88.15 ? 209 SER A CB 1 ATOM 1690 O OG . SER A 1 209 ? -14.950 8.191 39.919 1.00 88.34 ? 209 SER A OG 1 ATOM 1691 N N . SER A 1 210 ? -12.681 9.951 41.717 1.00 81.09 ? 210 SER A N 1 ATOM 1692 C CA . SER A 1 210 ? -11.814 9.385 42.755 1.00 77.13 ? 210 SER A CA 1 ATOM 1693 C C . SER A 1 210 ? -10.895 10.359 43.468 1.00 75.39 ? 210 SER A C 1 ATOM 1694 O O . SER A 1 210 ? -9.781 10.602 43.027 1.00 74.37 ? 210 SER A O 1 ATOM 1695 C CB . SER A 1 210 ? -10.985 8.260 42.161 1.00 75.72 ? 210 SER A CB 1 ATOM 1696 O OG . SER A 1 210 ? -9.678 8.416 42.607 1.00 74.61 ? 210 SER A OG 1 ATOM 1697 N N . ARG A 1 211 ? -11.373 10.855 44.648 1.00 55.89 ? 212 ARG A N 1 ATOM 1698 C CA . ARG A 1 211 ? -10.601 11.772 45.446 1.00 55.75 ? 212 ARG A CA 1 ATOM 1699 C C . ARG A 1 211 ? -9.599 11.050 46.323 1.00 51.29 ? 212 ARG A C 1 ATOM 1700 O O . ARG A 1 211 ? -8.665 11.651 46.840 1.00 52.53 ? 212 ARG A O 1 ATOM 1701 C CB . ARG A 1 211 ? -11.553 12.596 46.312 1.00 58.49 ? 212 ARG A CB 1 ATOM 1702 C CG . ARG A 1 211 ? -10.935 13.184 47.616 1.00 64.07 ? 212 ARG A CG 1 ATOM 1703 C CD . ARG A 1 211 ? -9.746 14.092 47.387 1.00 67.47 ? 212 ARG A CD 1 ATOM 1704 N NE . ARG A 1 211 ? -9.158 14.462 48.662 1.00 70.28 ? 212 ARG A NE 1 ATOM 1705 C CZ . ARG A 1 211 ? -8.041 15.173 48.811 1.00 72.82 ? 212 ARG A CZ 1 ATOM 1706 N NH1 . ARG A 1 211 ? -7.354 15.623 47.764 1.00 72.75 ? 212 ARG A NH1 1 ATOM 1707 N NH2 . ARG A 1 211 ? -7.611 15.443 50.034 1.00 74.95 ? 212 ARG A NH2 1 ATOM 1708 N N . PHE A 1 212 ? -9.780 9.762 46.507 1.00 45.16 ? 213 PHE A N 1 ATOM 1709 C CA . PHE A 1 212 ? -8.866 9.032 47.358 1.00 41.51 ? 213 PHE A CA 1 ATOM 1710 C C . PHE A 1 212 ? -7.473 8.832 46.731 1.00 39.04 ? 213 PHE A C 1 ATOM 1711 O O . PHE A 1 212 ? -6.551 8.419 47.424 1.00 38.12 ? 213 PHE A O 1 ATOM 1712 C CB . PHE A 1 212 ? -9.468 7.693 47.712 1.00 41.69 ? 213 PHE A CB 1 ATOM 1713 C CG . PHE A 1 212 ? -10.849 7.785 48.266 1.00 41.01 ? 213 PHE A CG 1 ATOM 1714 C CD1 . PHE A 1 212 ? -11.129 8.663 49.293 1.00 40.07 ? 213 PHE A CD1 1 ATOM 1715 C CD2 . PHE A 1 212 ? -11.871 6.977 47.779 1.00 39.79 ? 213 PHE A CD2 1 ATOM 1716 C CE1 . PHE A 1 212 ? -12.377 8.733 49.818 1.00 36.69 ? 213 PHE A CE1 1 ATOM 1717 C CE2 . PHE A 1 212 ? -13.105 7.050 48.309 1.00 38.02 ? 213 PHE A CE2 1 ATOM 1718 C CZ . PHE A 1 212 ? -13.354 7.928 49.328 1.00 36.97 ? 213 PHE A CZ 1 ATOM 1719 N N . SER A 1 213 ? -7.322 9.147 45.437 1.00 36.37 ? 214 SER A N 1 ATOM 1720 C CA . SER A 1 213 ? -6.076 8.971 44.708 1.00 33.18 ? 214 SER A CA 1 ATOM 1721 C C . SER A 1 213 ? -5.186 10.213 44.508 1.00 30.95 ? 214 SER A C 1 ATOM 1722 O O . SER A 1 213 ? -5.280 10.915 43.518 1.00 31.57 ? 214 SER A O 1 ATOM 1723 C CB . SER A 1 213 ? -6.389 8.361 43.375 1.00 32.76 ? 214 SER A CB 1 ATOM 1724 O OG . SER A 1 213 ? -7.151 7.210 43.597 1.00 32.61 ? 214 SER A OG 1 ATOM 1725 N N . ASN A 1 214 ? -4.290 10.429 45.465 1.00 27.97 ? 215 ASN A N 1 ATOM 1726 C CA . ASN A 1 214 ? -3.311 11.507 45.480 1.00 23.69 ? 215 ASN A CA 1 ATOM 1727 C C . ASN A 1 214 ? -2.563 11.536 46.819 1.00 21.59 ? 215 ASN A C 1 ATOM 1728 O O . ASN A 1 214 ? -3.058 11.131 47.849 1.00 18.75 ? 215 ASN A O 1 ATOM 1729 C CB . ASN A 1 214 ? -3.968 12.855 45.174 1.00 22.87 ? 215 ASN A CB 1 ATOM 1730 C CG . ASN A 1 214 ? -5.334 13.032 45.805 1.00 21.89 ? 215 ASN A CG 1 ATOM 1731 O OD1 . ASN A 1 214 ? -5.427 13.277 46.994 1.00 26.13 ? 215 ASN A OD1 1 ATOM 1732 N ND2 . ASN A 1 214 ? -6.402 12.953 45.003 1.00 18.93 ? 215 ASN A ND2 1 ATOM 1733 N N . ALA A 1 215 ? -1.340 11.987 46.779 1.00 21.41 ? 216 ALA A N 1 ATOM 1734 C CA . ALA A 1 215 ? -0.530 12.084 47.973 1.00 22.39 ? 216 ALA A CA 1 ATOM 1735 C C . ALA A 1 215 ? -1.333 12.731 49.158 1.00 22.81 ? 216 ALA A C 1 ATOM 1736 O O . ALA A 1 215 ? -1.494 12.140 50.237 1.00 22.66 ? 216 ALA A O 1 ATOM 1737 C CB . ALA A 1 215 ? 0.720 12.886 47.677 1.00 21.94 ? 216 ALA A CB 1 ATOM 1738 N N . ASP A 1 216 ? -1.890 13.909 48.936 1.00 21.80 ? 217 ASP A N 1 ATOM 1739 C CA . ASP A 1 216 ? -2.642 14.584 49.981 1.00 20.85 ? 217 ASP A CA 1 ATOM 1740 C C . ASP A 1 216 ? -3.680 13.768 50.682 1.00 20.39 ? 217 ASP A C 1 ATOM 1741 O O . ASP A 1 216 ? -3.674 13.682 51.881 1.00 20.78 ? 217 ASP A O 1 ATOM 1742 C CB . ASP A 1 216 ? -3.311 15.826 49.435 1.00 20.97 ? 217 ASP A CB 1 ATOM 1743 C CG . ASP A 1 216 ? -3.876 16.642 50.495 1.00 20.55 ? 217 ASP A CG 1 ATOM 1744 O OD1 . ASP A 1 216 ? -5.059 16.647 50.668 1.00 25.38 ? 217 ASP A OD1 1 ATOM 1745 O OD2 . ASP A 1 216 ? -3.177 17.283 51.250 1.00 25.72 ? 217 ASP A OD2 1 ATOM 1746 N N . TYR A 1 217 ? -4.605 13.179 49.954 1.00 20.56 ? 218 TYR A N 1 ATOM 1747 C CA . TYR A 1 217 ? -5.635 12.361 50.609 1.00 19.79 ? 218 TYR A CA 1 ATOM 1748 C C . TYR A 1 217 ? -4.958 11.280 51.444 1.00 19.70 ? 218 TYR A C 1 ATOM 1749 O O . TYR A 1 217 ? -5.165 11.174 52.647 1.00 19.82 ? 218 TYR A O 1 ATOM 1750 C CB . TYR A 1 217 ? -6.566 11.671 49.622 1.00 19.41 ? 218 TYR A CB 1 ATOM 1751 C CG . TYR A 1 217 ? -7.630 10.922 50.378 1.00 22.38 ? 218 TYR A CG 1 ATOM 1752 C CD1 . TYR A 1 217 ? -8.745 11.570 50.861 1.00 24.88 ? 218 TYR A CD1 1 ATOM 1753 C CD2 . TYR A 1 217 ? -7.503 9.595 50.675 1.00 24.71 ? 218 TYR A CD2 1 ATOM 1754 C CE1 . TYR A 1 217 ? -9.682 10.918 51.623 1.00 25.61 ? 218 TYR A CE1 1 ATOM 1755 C CE2 . TYR A 1 217 ? -8.466 8.923 51.428 1.00 25.04 ? 218 TYR A CE2 1 ATOM 1756 C CZ . TYR A 1 217 ? -9.533 9.597 51.903 1.00 26.48 ? 218 TYR A CZ 1 ATOM 1757 O OH . TYR A 1 217 ? -10.495 8.940 52.659 1.00 32.97 ? 218 TYR A OH 1 ATOM 1758 N N . ALA A 1 218 ? -4.113 10.487 50.783 1.00 19.12 ? 219 ALA A N 1 ATOM 1759 C CA . ALA A 1 218 ? -3.386 9.384 51.426 1.00 16.92 ? 219 ALA A CA 1 ATOM 1760 C C . ALA A 1 218 ? -2.759 9.800 52.750 1.00 16.88 ? 219 ALA A C 1 ATOM 1761 O O . ALA A 1 218 ? -2.977 9.145 53.769 1.00 17.22 ? 219 ALA A O 1 ATOM 1762 C CB . ALA A 1 218 ? -2.337 8.838 50.501 1.00 14.74 ? 219 ALA A CB 1 ATOM 1763 N N . VAL A 1 219 ? -2.003 10.898 52.735 1.00 16.25 ? 220 VAL A N 1 ATOM 1764 C CA . VAL A 1 219 ? -1.324 11.365 53.938 1.00 15.96 ? 220 VAL A CA 1 ATOM 1765 C C . VAL A 1 219 ? -2.277 11.710 55.058 1.00 17.24 ? 220 VAL A C 1 ATOM 1766 O O . VAL A 1 219 ? -2.175 11.159 56.157 1.00 16.93 ? 220 VAL A O 1 ATOM 1767 C CB . VAL A 1 219 ? -0.439 12.569 53.669 1.00 15.13 ? 220 VAL A CB 1 ATOM 1768 C CG1 . VAL A 1 219 ? 0.113 13.130 54.934 1.00 11.83 ? 220 VAL A CG1 1 ATOM 1769 C CG2 . VAL A 1 219 ? 0.684 12.180 52.752 1.00 14.94 ? 220 VAL A CG2 1 ATOM 1770 N N . SER A 1 220 ? -3.228 12.614 54.784 1.00 19.12 ? 221 SER A N 1 ATOM 1771 C CA . SER A 1 220 ? -4.237 13.024 55.780 1.00 19.98 ? 221 SER A CA 1 ATOM 1772 C C . SER A 1 220 ? -4.844 11.783 56.404 1.00 19.15 ? 221 SER A C 1 ATOM 1773 O O . SER A 1 220 ? -4.889 11.622 57.606 1.00 18.62 ? 221 SER A O 1 ATOM 1774 C CB . SER A 1 220 ? -5.292 13.897 55.131 1.00 21.19 ? 221 SER A CB 1 ATOM 1775 O OG . SER A 1 220 ? -4.721 15.111 54.637 1.00 27.13 ? 221 SER A OG 1 ATOM 1776 N N . TYR A 1 221 ? -5.260 10.862 55.547 1.00 19.75 ? 222 TYR A N 1 ATOM 1777 C CA . TYR A 1 221 ? -5.901 9.608 55.982 1.00 19.08 ? 222 TYR A CA 1 ATOM 1778 C C . TYR A 1 221 ? -5.048 8.826 56.998 1.00 19.51 ? 222 TYR A C 1 ATOM 1779 O O . TYR A 1 221 ? -5.511 8.510 58.098 1.00 20.29 ? 222 TYR A O 1 ATOM 1780 C CB . TYR A 1 221 ? -6.195 8.717 54.773 1.00 17.12 ? 222 TYR A CB 1 ATOM 1781 C CG . TYR A 1 221 ? -7.177 7.616 55.073 1.00 17.06 ? 222 TYR A CG 1 ATOM 1782 C CD1 . TYR A 1 221 ? -8.283 7.884 55.741 1.00 15.61 ? 222 TYR A CD1 1 ATOM 1783 C CD2 . TYR A 1 221 ? -6.946 6.294 54.711 1.00 23.17 ? 222 TYR A CD2 1 ATOM 1784 C CE1 . TYR A 1 221 ? -9.187 6.884 56.012 1.00 18.91 ? 222 TYR A CE1 1 ATOM 1785 C CE2 . TYR A 1 221 ? -7.857 5.281 54.966 1.00 21.19 ? 222 TYR A CE2 1 ATOM 1786 C CZ . TYR A 1 221 ? -8.950 5.579 55.625 1.00 20.24 ? 222 TYR A CZ 1 ATOM 1787 O OH . TYR A 1 221 ? -9.818 4.558 55.897 1.00 21.09 ? 222 TYR A OH 1 ATOM 1788 N N . MET A 1 222 ? -3.807 8.528 56.625 1.00 18.71 ? 223 MET A N 1 ATOM 1789 C CA . MET A 1 222 ? -2.886 7.816 57.494 1.00 18.42 ? 223 MET A CA 1 ATOM 1790 C C . MET A 1 222 ? -2.756 8.505 58.849 1.00 18.97 ? 223 MET A C 1 ATOM 1791 O O . MET A 1 222 ? -2.625 7.874 59.887 1.00 17.46 ? 223 MET A O 1 ATOM 1792 C CB . MET A 1 222 ? -1.535 7.751 56.849 1.00 18.69 ? 223 MET A CB 1 ATOM 1793 C CG . MET A 1 222 ? -1.508 6.837 55.633 1.00 22.53 ? 223 MET A CG 1 ATOM 1794 S SD . MET A 1 222 ? -1.455 5.110 56.117 1.00 19.82 ? 223 MET A SD 1 ATOM 1795 C CE . MET A 1 222 ? 0.135 5.118 56.965 1.00 23.92 ? 223 MET A CE 1 ATOM 1796 N N . LEU A 1 223 ? -2.786 9.819 58.840 1.00 19.99 ? 224 LEU A N 1 ATOM 1797 C CA . LEU A 1 223 ? -2.680 10.557 60.084 1.00 20.88 ? 224 LEU A CA 1 ATOM 1798 C C . LEU A 1 223 ? -3.950 10.305 60.910 1.00 23.96 ? 224 LEU A C 1 ATOM 1799 O O . LEU A 1 223 ? -3.870 10.116 62.132 1.00 25.14 ? 224 LEU A O 1 ATOM 1800 C CB . LEU A 1 223 ? -2.476 12.046 59.804 1.00 18.39 ? 224 LEU A CB 1 ATOM 1801 C CG . LEU A 1 223 ? -1.126 12.333 59.171 1.00 18.26 ? 224 LEU A CG 1 ATOM 1802 C CD1 . LEU A 1 223 ? -0.969 13.762 58.837 1.00 19.42 ? 224 LEU A CD1 1 ATOM 1803 C CD2 . LEU A 1 223 ? -0.008 11.936 60.136 1.00 20.27 ? 224 LEU A CD2 1 ATOM 1804 N N . ARG A 1 224 ? -5.110 10.295 60.253 1.00 25.14 ? 225 ARG A N 1 ATOM 1805 C CA . ARG A 1 224 ? -6.327 10.065 60.958 1.00 27.53 ? 225 ARG A CA 1 ATOM 1806 C C . ARG A 1 224 ? -6.304 8.659 61.529 1.00 26.21 ? 225 ARG A C 1 ATOM 1807 O O . ARG A 1 224 ? -6.611 8.451 62.681 1.00 25.69 ? 225 ARG A O 1 ATOM 1808 C CB . ARG A 1 224 ? -7.481 10.194 60.014 1.00 32.62 ? 225 ARG A CB 1 ATOM 1809 C CG . ARG A 1 224 ? -8.869 10.329 60.680 1.00 45.70 ? 225 ARG A CG 1 ATOM 1810 C CD . ARG A 1 224 ? -9.211 9.222 61.718 1.00 56.50 ? 225 ARG A CD 1 ATOM 1811 N NE . ARG A 1 224 ? -8.760 9.566 63.083 1.00 66.42 ? 225 ARG A NE 1 ATOM 1812 C CZ . ARG A 1 224 ? -9.477 9.377 64.216 1.00 70.96 ? 225 ARG A CZ 1 ATOM 1813 N NH1 . ARG A 1 224 ? -10.703 8.838 64.164 1.00 72.69 ? 225 ARG A NH1 1 ATOM 1814 N NH2 . ARG A 1 224 ? -8.948 9.701 65.401 1.00 71.90 ? 225 ARG A NH2 1 ATOM 1815 N N . LEU A 1 225 ? -5.946 7.669 60.715 1.00 24.82 ? 226 LEU A N 1 ATOM 1816 C CA . LEU A 1 225 ? -5.908 6.291 61.186 1.00 22.59 ? 226 LEU A CA 1 ATOM 1817 C C . LEU A 1 225 ? -4.995 6.147 62.412 1.00 23.41 ? 226 LEU A C 1 ATOM 1818 O O . LEU A 1 225 ? -5.131 5.187 63.166 1.00 25.71 ? 226 LEU A O 1 ATOM 1819 C CB . LEU A 1 225 ? -5.440 5.356 60.088 1.00 20.84 ? 226 LEU A CB 1 ATOM 1820 C CG . LEU A 1 225 ? -6.422 4.670 59.187 1.00 17.27 ? 226 LEU A CG 1 ATOM 1821 C CD1 . LEU A 1 225 ? -7.849 4.912 59.638 1.00 19.13 ? 226 LEU A CD1 1 ATOM 1822 C CD2 . LEU A 1 225 ? -6.220 5.191 57.804 1.00 19.89 ? 226 LEU A CD2 1 ATOM 1823 N N . GLY A 1 226 ? -4.062 7.072 62.623 1.00 22.44 ? 227 GLY A N 1 ATOM 1824 C CA . GLY A 1 226 ? -3.194 6.972 63.803 1.00 21.53 ? 227 GLY A CA 1 ATOM 1825 C C . GLY A 1 226 ? -1.673 6.921 63.639 1.00 20.21 ? 227 GLY A C 1 ATOM 1826 O O . GLY A 1 226 ? -0.980 6.946 64.604 1.00 19.46 ? 227 GLY A O 1 ATOM 1827 N N . ALA A 1 227 ? -1.158 6.867 62.426 1.00 19.91 ? 228 ALA A N 1 ATOM 1828 C CA . ALA A 1 227 ? 0.263 6.824 62.231 1.00 18.87 ? 228 ALA A CA 1 ATOM 1829 C C . ALA A 1 227 ? 0.788 8.191 62.613 1.00 20.71 ? 228 ALA A C 1 ATOM 1830 O O . ALA A 1 227 ? 0.213 9.214 62.256 1.00 22.72 ? 228 ALA A O 1 ATOM 1831 C CB . ALA A 1 227 ? 0.550 6.514 60.798 1.00 17.44 ? 228 ALA A CB 1 ATOM 1832 N N . PRO A 1 228 ? 1.855 8.272 63.371 1.00 21.49 ? 229 PRO A N 1 ATOM 1833 C CA . PRO A 1 228 ? 2.370 9.594 63.712 1.00 22.17 ? 229 PRO A CA 1 ATOM 1834 C C . PRO A 1 228 ? 3.295 10.229 62.620 1.00 22.88 ? 229 PRO A C 1 ATOM 1835 O O . PRO A 1 228 ? 4.116 9.591 62.000 1.00 24.03 ? 229 PRO A O 1 ATOM 1836 C CB . PRO A 1 228 ? 3.119 9.333 65.005 1.00 21.69 ? 229 PRO A CB 1 ATOM 1837 C CG . PRO A 1 228 ? 3.721 8.036 64.736 1.00 24.01 ? 229 PRO A CG 1 ATOM 1838 C CD . PRO A 1 228 ? 2.591 7.219 64.067 1.00 22.51 ? 229 PRO A CD 1 ATOM 1839 N N . ALA A 1 229 ? 3.157 11.519 62.418 1.00 22.83 ? 230 ALA A N 1 ATOM 1840 C CA . ALA A 1 229 ? 3.918 12.247 61.447 1.00 21.25 ? 230 ALA A CA 1 ATOM 1841 C C . ALA A 1 229 ? 5.386 11.927 61.467 1.00 21.25 ? 230 ALA A C 1 ATOM 1842 O O . ALA A 1 229 ? 5.955 11.718 60.403 1.00 21.43 ? 230 ALA A O 1 ATOM 1843 C CB . ALA A 1 229 ? 3.709 13.713 61.656 1.00 21.54 ? 230 ALA A CB 1 ATOM 1844 N N . ASN A 1 230 ? 6.020 11.878 62.639 1.00 20.84 ? 231 ASN A N 1 ATOM 1845 C CA . ASN A 1 230 ? 7.473 11.640 62.683 1.00 21.11 ? 231 ASN A CA 1 ATOM 1846 C C . ASN A 1 230 ? 7.943 10.229 62.327 1.00 19.60 ? 231 ASN A C 1 ATOM 1847 O O . ASN A 1 230 ? 9.102 9.869 62.547 1.00 19.44 ? 231 ASN A O 1 ATOM 1848 C CB . ASN A 1 230 ? 8.058 12.051 64.037 1.00 22.17 ? 231 ASN A CB 1 ATOM 1849 C CG . ASN A 1 230 ? 7.472 11.289 65.195 1.00 24.34 ? 231 ASN A CG 1 ATOM 1850 O OD1 . ASN A 1 230 ? 7.990 10.267 65.634 1.00 24.87 ? 231 ASN A OD1 1 ATOM 1851 N ND2 . ASN A 1 230 ? 6.386 11.794 65.708 1.00 28.68 ? 231 ASN A ND2 1 ATOM 1852 N N . LYS A 1 231 ? 7.040 9.424 61.786 1.00 17.94 ? 232 LYS A N 1 ATOM 1853 C CA . LYS A 1 231 ? 7.353 8.047 61.351 1.00 15.69 ? 232 LYS A CA 1 ATOM 1854 C C . LYS A 1 231 ? 6.964 7.871 59.873 1.00 13.20 ? 232 LYS A C 1 ATOM 1855 O O . LYS A 1 231 ? 7.413 6.998 59.193 1.00 12.99 ? 232 LYS A O 1 ATOM 1856 C CB . LYS A 1 231 ? 6.622 7.011 62.217 1.00 14.42 ? 232 LYS A CB 1 ATOM 1857 C CG . LYS A 1 231 ? 7.297 6.692 63.572 1.00 13.74 ? 232 LYS A CG 1 ATOM 1858 C CD . LYS A 1 231 ? 6.570 5.537 64.290 1.00 13.58 ? 232 LYS A CD 1 ATOM 1859 C CE . LYS A 1 231 ? 7.028 5.271 65.677 1.00 11.05 ? 232 LYS A CE 1 ATOM 1860 N NZ . LYS A 1 231 ? 8.154 4.401 65.705 1.00 12.45 ? 232 LYS A NZ 1 ATOM 1861 N N . LEU A 1 232 ? 6.109 8.743 59.386 1.00 11.93 ? 233 LEU A N 1 ATOM 1862 C CA . LEU A 1 232 ? 5.657 8.717 57.994 1.00 10.53 ? 233 LEU A CA 1 ATOM 1863 C C . LEU A 1 232 ? 6.705 9.273 57.028 1.00 10.58 ? 233 LEU A C 1 ATOM 1864 O O . LEU A 1 232 ? 7.313 10.324 57.244 1.00 11.15 ? 233 LEU A O 1 ATOM 1865 C CB . LEU A 1 232 ? 4.390 9.570 57.826 1.00 8.88 ? 233 LEU A CB 1 ATOM 1866 C CG . LEU A 1 232 ? 3.055 8.916 57.792 1.00 8.48 ? 233 LEU A CG 1 ATOM 1867 C CD1 . LEU A 1 232 ? 1.966 9.919 57.591 1.00 8.86 ? 233 LEU A CD1 1 ATOM 1868 C CD2 . LEU A 1 232 ? 3.033 7.947 56.651 1.00 17.05 ? 233 LEU A CD2 1 ATOM 1869 N N . VAL A 1 233 ? 6.896 8.566 55.938 1.00 10.27 ? 234 VAL A N 1 ATOM 1870 C CA . VAL A 1 233 ? 7.795 8.970 54.899 1.00 9.53 ? 234 VAL A CA 1 ATOM 1871 C C . VAL A 1 233 ? 7.002 8.908 53.591 1.00 8.99 ? 234 VAL A C 1 ATOM 1872 O O . VAL A 1 233 ? 6.458 7.886 53.234 1.00 8.95 ? 234 VAL A O 1 ATOM 1873 C CB . VAL A 1 233 ? 8.929 8.024 54.842 1.00 10.04 ? 234 VAL A CB 1 ATOM 1874 C CG1 . VAL A 1 233 ? 9.844 8.420 53.727 1.00 13.25 ? 234 VAL A CG1 1 ATOM 1875 C CG2 . VAL A 1 233 ? 9.743 8.091 56.128 1.00 10.11 ? 234 VAL A CG2 1 ATOM 1876 N N . MET A 1 234 ? 6.929 10.023 52.882 1.00 8.29 ? 235 MET A N 1 ATOM 1877 C CA . MET A 1 234 ? 6.174 10.067 51.649 1.00 7.56 ? 235 MET A CA 1 ATOM 1878 C C . MET A 1 234 ? 6.980 9.633 50.413 1.00 5.69 ? 235 MET A C 1 ATOM 1879 O O . MET A 1 234 ? 8.013 10.145 50.103 1.00 5.48 ? 235 MET A O 1 ATOM 1880 C CB . MET A 1 234 ? 5.574 11.452 51.421 1.00 7.88 ? 235 MET A CB 1 ATOM 1881 C CG . MET A 1 234 ? 4.609 11.499 50.247 1.00 8.80 ? 235 MET A CG 1 ATOM 1882 S SD . MET A 1 234 ? 3.944 13.119 49.936 1.00 7.55 ? 235 MET A SD 1 ATOM 1883 C CE . MET A 1 234 ? 5.175 13.711 48.773 1.00 11.24 ? 235 MET A CE 1 ATOM 1884 N N . GLY A 1 235 ? 6.408 8.700 49.671 1.00 5.05 ? 236 GLY A N 1 ATOM 1885 C CA . GLY A 1 235 ? 7.023 8.167 48.466 1.00 6.72 ? 236 GLY A CA 1 ATOM 1886 C C . GLY A 1 235 ? 7.041 9.084 47.250 1.00 5.78 ? 236 GLY A C 1 ATOM 1887 O O . GLY A 1 235 ? 6.043 9.620 46.830 1.00 7.46 ? 236 GLY A O 1 ATOM 1888 N N . ILE A 1 236 ? 8.203 9.274 46.684 1.00 8.27 ? 237 ILE A N 1 ATOM 1889 C CA . ILE A 1 236 ? 8.289 10.053 45.487 1.00 11.44 ? 237 ILE A CA 1 ATOM 1890 C C . ILE A 1 236 ? 8.829 9.127 44.406 1.00 11.80 ? 237 ILE A C 1 ATOM 1891 O O . ILE A 1 236 ? 9.764 8.402 44.654 1.00 11.81 ? 237 ILE A O 1 ATOM 1892 C CB . ILE A 1 236 ? 9.169 11.336 45.727 1.00 11.71 ? 237 ILE A CB 1 ATOM 1893 C CG1 . ILE A 1 236 ? 8.503 12.227 46.784 1.00 10.14 ? 237 ILE A CG1 1 ATOM 1894 C CG2 . ILE A 1 236 ? 9.358 12.094 44.429 1.00 10.62 ? 237 ILE A CG2 1 ATOM 1895 C CD1 . ILE A 1 236 ? 9.323 13.359 47.190 1.00 19.46 ? 237 ILE A CD1 1 ATOM 1896 N N . PRO A 1 237 ? 8.233 9.155 43.206 1.00 13.28 ? 238 PRO A N 1 ATOM 1897 C CA . PRO A 1 237 ? 8.731 8.323 42.111 1.00 12.93 ? 238 PRO A CA 1 ATOM 1898 C C . PRO A 1 237 ? 9.794 9.021 41.276 1.00 12.49 ? 238 PRO A C 1 ATOM 1899 O O . PRO A 1 237 ? 9.883 10.221 41.255 1.00 11.54 ? 238 PRO A O 1 ATOM 1900 C CB . PRO A 1 237 ? 7.477 8.073 41.304 1.00 13.04 ? 238 PRO A CB 1 ATOM 1901 C CG . PRO A 1 237 ? 6.825 9.484 41.334 1.00 13.38 ? 238 PRO A CG 1 ATOM 1902 C CD . PRO A 1 237 ? 6.989 9.863 42.784 1.00 14.26 ? 238 PRO A CD 1 ATOM 1903 N N . THR A 1 238 ? 10.601 8.225 40.592 1.00 12.21 ? 239 THR A N 1 ATOM 1904 C CA . THR A 1 238 ? 11.659 8.717 39.741 1.00 10.03 ? 239 THR A CA 1 ATOM 1905 C C . THR A 1 238 ? 11.479 8.102 38.352 1.00 10.76 ? 239 THR A C 1 ATOM 1906 O O . THR A 1 238 ? 12.338 8.203 37.534 1.00 11.95 ? 239 THR A O 1 ATOM 1907 C CB . THR A 1 238 ? 12.982 8.331 40.343 1.00 10.09 ? 239 THR A CB 1 ATOM 1908 O OG1 . THR A 1 238 ? 13.737 9.521 40.617 1.00 11.73 ? 239 THR A OG1 1 ATOM 1909 C CG2 . THR A 1 238 ? 13.794 7.390 39.412 1.00 5.15 ? 239 THR A CG2 1 ATOM 1910 N N . PHE A 1 239 ? 10.335 7.476 38.103 1.00 10.83 ? 240 PHE A N 1 ATOM 1911 C CA . PHE A 1 239 ? 10.018 6.895 36.836 1.00 10.53 ? 240 PHE A CA 1 ATOM 1912 C C . PHE A 1 239 ? 8.694 7.440 36.318 1.00 13.45 ? 240 PHE A C 1 ATOM 1913 O O . PHE A 1 239 ? 7.961 8.088 37.026 1.00 14.54 ? 240 PHE A O 1 ATOM 1914 C CB . PHE A 1 239 ? 9.889 5.410 36.973 1.00 7.60 ? 240 PHE A CB 1 ATOM 1915 C CG . PHE A 1 239 ? 8.797 4.996 37.883 1.00 7.01 ? 240 PHE A CG 1 ATOM 1916 C CD1 . PHE A 1 239 ? 9.015 4.954 39.246 1.00 7.30 ? 240 PHE A CD1 1 ATOM 1917 C CD2 . PHE A 1 239 ? 7.556 4.671 37.404 1.00 6.17 ? 240 PHE A CD2 1 ATOM 1918 C CE1 . PHE A 1 239 ? 7.994 4.589 40.127 1.00 7.06 ? 240 PHE A CE1 1 ATOM 1919 C CE2 . PHE A 1 239 ? 6.510 4.281 38.270 1.00 2.78 ? 240 PHE A CE2 1 ATOM 1920 C CZ . PHE A 1 239 ? 6.731 4.249 39.628 1.00 7.55 ? 240 PHE A CZ 1 ATOM 1921 N N . GLY A 1 240 ? 8.394 7.164 35.060 1.00 16.09 ? 241 GLY A N 1 ATOM 1922 C CA . GLY A 1 240 ? 7.161 7.629 34.460 1.00 17.23 ? 241 GLY A CA 1 ATOM 1923 C C . GLY A 1 240 ? 6.309 6.488 33.948 1.00 19.17 ? 241 GLY A C 1 ATOM 1924 O O . GLY A 1 240 ? 6.802 5.461 33.515 1.00 20.76 ? 241 GLY A O 1 ATOM 1925 N N . ARG A 1 241 ? 5.018 6.659 33.991 1.00 20.04 ? 242 ARG A N 1 ATOM 1926 C CA . ARG A 1 241 ? 4.114 5.662 33.520 1.00 21.82 ? 242 ARG A CA 1 ATOM 1927 C C . ARG A 1 241 ? 3.677 6.110 32.143 1.00 22.29 ? 242 ARG A C 1 ATOM 1928 O O . ARG A 1 241 ? 3.291 7.259 31.951 1.00 22.31 ? 242 ARG A O 1 ATOM 1929 C CB . ARG A 1 241 ? 2.940 5.613 34.476 1.00 23.72 ? 242 ARG A CB 1 ATOM 1930 C CG . ARG A 1 241 ? 2.431 4.237 34.756 1.00 29.56 ? 242 ARG A CG 1 ATOM 1931 C CD . ARG A 1 241 ? 2.705 3.761 36.130 1.00 29.09 ? 242 ARG A CD 1 ATOM 1932 N NE . ARG A 1 241 ? 3.344 2.452 36.105 1.00 35.34 ? 242 ARG A NE 1 ATOM 1933 C CZ . ARG A 1 241 ? 3.579 1.745 37.201 1.00 40.46 ? 242 ARG A CZ 1 ATOM 1934 N NH1 . ARG A 1 241 ? 3.192 2.217 38.405 1.00 42.90 ? 242 ARG A NH1 1 ATOM 1935 N NH2 . ARG A 1 241 ? 4.222 0.590 37.118 1.00 40.10 ? 242 ARG A NH2 1 ATOM 1936 N N . SER A 1 242 ? 3.753 5.214 31.168 1.00 24.16 ? 243 SER A N 1 ATOM 1937 C CA . SER A 1 242 ? 3.396 5.532 29.760 1.00 25.67 ? 243 SER A CA 1 ATOM 1938 C C . SER A 1 242 ? 2.232 4.762 29.132 1.00 26.34 ? 243 SER A C 1 ATOM 1939 O O . SER A 1 242 ? 1.976 3.632 29.472 1.00 28.79 ? 243 SER A O 1 ATOM 1940 C CB . SER A 1 242 ? 4.606 5.303 28.891 1.00 25.94 ? 243 SER A CB 1 ATOM 1941 O OG . SER A 1 242 ? 4.956 3.918 28.898 1.00 27.58 ? 243 SER A OG 1 ATOM 1942 N N . PHE A 1 243 ? 1.538 5.387 28.207 1.00 27.33 ? 244 PHE A N 1 ATOM 1943 C CA . PHE A 1 243 ? 0.381 4.793 27.520 1.00 28.38 ? 244 PHE A CA 1 ATOM 1944 C C . PHE A 1 243 ? 0.472 4.988 26.013 1.00 27.21 ? 244 PHE A C 1 ATOM 1945 O O . PHE A 1 243 ? 1.072 5.957 25.531 1.00 26.66 ? 244 PHE A O 1 ATOM 1946 C CB . PHE A 1 243 ? -0.932 5.487 27.936 1.00 29.33 ? 244 PHE A CB 1 ATOM 1947 C CG . PHE A 1 243 ? -1.159 5.524 29.392 1.00 32.69 ? 244 PHE A CG 1 ATOM 1948 C CD1 . PHE A 1 243 ? -1.552 4.393 30.067 1.00 35.19 ? 244 PHE A CD1 1 ATOM 1949 C CD2 . PHE A 1 243 ? -0.967 6.704 30.101 1.00 36.12 ? 244 PHE A CD2 1 ATOM 1950 C CE1 . PHE A 1 243 ? -1.767 4.433 31.436 1.00 39.09 ? 244 PHE A CE1 1 ATOM 1951 C CE2 . PHE A 1 243 ? -1.174 6.755 31.469 1.00 37.80 ? 244 PHE A CE2 1 ATOM 1952 C CZ . PHE A 1 243 ? -1.573 5.620 32.143 1.00 39.46 ? 244 PHE A CZ 1 ATOM 1953 N N . THR A 1 244 ? -0.159 4.085 25.273 1.00 25.40 ? 245 THR A N 1 ATOM 1954 C CA . THR A 1 244 ? -0.225 4.214 23.831 1.00 23.84 ? 245 THR A CA 1 ATOM 1955 C C . THR A 1 244 ? -1.658 4.736 23.613 1.00 24.44 ? 245 THR A C 1 ATOM 1956 O O . THR A 1 244 ? -2.636 4.042 23.904 1.00 22.39 ? 245 THR A O 1 ATOM 1957 C CB . THR A 1 244 ? -0.062 2.864 23.115 1.00 22.45 ? 245 THR A CB 1 ATOM 1958 O OG1 . THR A 1 244 ? 1.243 2.328 23.346 1.00 20.25 ? 245 THR A OG1 1 ATOM 1959 C CG2 . THR A 1 244 ? -0.226 3.034 21.629 1.00 19.55 ? 245 THR A CG2 1 ATOM 1960 N N . LEU A 1 245 ? -1.769 5.971 23.129 1.00 25.43 ? 246 LEU A N 1 ATOM 1961 C CA . LEU A 1 245 ? -3.043 6.574 22.903 1.00 26.63 ? 246 LEU A CA 1 ATOM 1962 C C . LEU A 1 245 ? -3.840 5.766 21.913 1.00 30.31 ? 246 LEU A C 1 ATOM 1963 O O . LEU A 1 245 ? -3.300 4.919 21.233 1.00 30.65 ? 246 LEU A O 1 ATOM 1964 C CB . LEU A 1 245 ? -2.871 7.981 22.421 1.00 25.49 ? 246 LEU A CB 1 ATOM 1965 C CG . LEU A 1 245 ? -2.382 8.995 23.431 1.00 25.30 ? 246 LEU A CG 1 ATOM 1966 C CD1 . LEU A 1 245 ? -2.144 10.318 22.721 1.00 27.73 ? 246 LEU A CD1 1 ATOM 1967 C CD2 . LEU A 1 245 ? -3.399 9.198 24.552 1.00 25.48 ? 246 LEU A CD2 1 ATOM 1968 N N . ALA A 1 246 ? -5.148 6.036 21.842 1.00 35.22 ? 247 ALA A N 1 ATOM 1969 C CA . ALA A 1 246 ? -6.059 5.339 20.933 1.00 37.60 ? 247 ALA A CA 1 ATOM 1970 C C . ALA A 1 246 ? -6.892 6.359 20.180 1.00 39.92 ? 247 ALA A C 1 ATOM 1971 O O . ALA A 1 246 ? -7.948 6.047 19.695 1.00 41.02 ? 247 ALA A O 1 ATOM 1972 C CB . ALA A 1 246 ? -6.952 4.383 21.714 1.00 36.97 ? 247 ALA A CB 1 ATOM 1973 N N . SER A 1 247 ? -6.409 7.588 20.095 1.00 43.24 ? 248 SER A N 1 ATOM 1974 C CA . SER A 1 247 ? -7.110 8.661 19.383 1.00 46.44 ? 248 SER A CA 1 ATOM 1975 C C . SER A 1 247 ? -6.269 9.945 19.389 1.00 47.93 ? 248 SER A C 1 ATOM 1976 O O . SER A 1 247 ? -5.246 10.038 20.043 1.00 48.96 ? 248 SER A O 1 ATOM 1977 C CB . SER A 1 247 ? -8.449 8.985 20.058 1.00 47.41 ? 248 SER A CB 1 ATOM 1978 O OG . SER A 1 247 ? -8.300 9.839 21.205 1.00 48.33 ? 248 SER A OG 1 ATOM 1979 N N . SER A 1 248 ? -6.733 10.950 18.687 1.00 48.95 ? 249 SER A N 1 ATOM 1980 C CA . SER A 1 248 ? -6.019 12.185 18.633 1.00 50.79 ? 249 SER A CA 1 ATOM 1981 C C . SER A 1 248 ? -6.122 12.912 19.948 1.00 52.08 ? 249 SER A C 1 ATOM 1982 O O . SER A 1 248 ? -5.343 13.809 20.223 1.00 53.33 ? 249 SER A O 1 ATOM 1983 C CB . SER A 1 248 ? -6.628 13.038 17.536 1.00 51.82 ? 249 SER A CB 1 ATOM 1984 O OG . SER A 1 248 ? -7.017 12.223 16.433 1.00 53.49 ? 249 SER A OG 1 ATOM 1985 N N . LYS A 1 249 ? -7.088 12.528 20.769 1.00 53.28 ? 250 LYS A N 1 ATOM 1986 C CA . LYS A 1 249 ? -7.307 13.195 22.051 1.00 53.60 ? 250 LYS A CA 1 ATOM 1987 C C . LYS A 1 249 ? -6.123 12.980 22.991 1.00 52.80 ? 250 LYS A C 1 ATOM 1988 O O . LYS A 1 249 ? -5.597 11.874 23.096 1.00 52.01 ? 250 LYS A O 1 ATOM 1989 C CB . LYS A 1 249 ? -8.617 12.722 22.711 1.00 54.85 ? 250 LYS A CB 1 ATOM 1990 C CG . LYS A 1 249 ? -9.177 13.736 23.733 1.00 56.94 ? 250 LYS A CG 1 ATOM 1991 C CD . LYS A 1 249 ? -10.686 13.739 23.746 1.00 60.00 ? 250 LYS A CD 1 ATOM 1992 C CE . LYS A 1 249 ? -11.254 14.802 24.687 1.00 62.04 ? 250 LYS A CE 1 ATOM 1993 N NZ . LYS A 1 249 ? -11.048 14.467 26.118 1.00 62.07 ? 250 LYS A NZ 1 ATOM 1994 N N . THR A 1 250 ? -5.724 14.061 23.667 1.00 52.01 ? 251 THR A N 1 ATOM 1995 C CA . THR A 1 250 ? -4.588 14.065 24.563 1.00 50.82 ? 251 THR A CA 1 ATOM 1996 C C . THR A 1 250 ? -4.825 14.596 25.975 1.00 51.99 ? 251 THR A C 1 ATOM 1997 O O . THR A 1 250 ? -3.960 14.450 26.846 1.00 51.36 ? 251 THR A O 1 ATOM 1998 C CB . THR A 1 250 ? -3.482 14.864 23.900 1.00 49.83 ? 251 THR A CB 1 ATOM 1999 O OG1 . THR A 1 250 ? -2.468 13.945 23.552 1.00 48.83 ? 251 THR A OG1 1 ATOM 2000 C CG2 . THR A 1 250 ? -2.844 15.924 24.835 1.00 49.22 ? 251 THR A CG2 1 ATOM 2001 N N . ASP A 1 251 ? -5.980 15.211 26.211 1.00 53.89 ? 252 ASP A N 1 ATOM 2002 C CA . ASP A 1 251 ? -6.285 15.783 27.527 1.00 55.20 ? 252 ASP A CA 1 ATOM 2003 C C . ASP A 1 251 ? -6.931 14.812 28.470 1.00 55.02 ? 252 ASP A C 1 ATOM 2004 O O . ASP A 1 251 ? -7.100 13.670 28.141 1.00 54.73 ? 252 ASP A O 1 ATOM 2005 C CB . ASP A 1 251 ? -7.196 16.993 27.383 1.00 56.45 ? 252 ASP A CB 1 ATOM 2006 C CG . ASP A 1 251 ? -8.437 16.670 26.599 1.00 59.61 ? 252 ASP A CG 1 ATOM 2007 O OD1 . ASP A 1 251 ? -8.326 16.475 25.367 1.00 60.11 ? 252 ASP A OD1 1 ATOM 2008 O OD2 . ASP A 1 251 ? -9.548 16.601 27.164 1.00 63.02 ? 252 ASP A OD2 1 ATOM 2009 N N . VAL A 1 252 ? -7.287 15.295 29.644 1.00 55.71 ? 253 VAL A N 1 ATOM 2010 C CA . VAL A 1 252 ? -7.906 14.472 30.660 1.00 57.63 ? 253 VAL A CA 1 ATOM 2011 C C . VAL A 1 252 ? -9.052 13.623 30.101 1.00 57.18 ? 253 VAL A C 1 ATOM 2012 O O . VAL A 1 252 ? -9.935 14.145 29.389 1.00 56.45 ? 253 VAL A O 1 ATOM 2013 C CB . VAL A 1 252 ? -8.444 15.330 31.837 1.00 59.16 ? 253 VAL A CB 1 ATOM 2014 C CG1 . VAL A 1 252 ? -7.288 15.924 32.612 1.00 61.14 ? 253 VAL A CG1 1 ATOM 2015 C CG2 . VAL A 1 252 ? -9.381 16.440 31.330 1.00 60.86 ? 253 VAL A CG2 1 ATOM 2016 N N . GLY A 1 253 ? -9.010 12.313 30.421 1.00 55.61 ? 254 GLY A N 1 ATOM 2017 C CA . GLY A 1 253 ? -10.037 11.364 29.985 1.00 52.84 ? 254 GLY A CA 1 ATOM 2018 C C . GLY A 1 253 ? -9.790 10.620 28.673 1.00 50.03 ? 254 GLY A C 1 ATOM 2019 O O . GLY A 1 253 ? -10.428 9.598 28.415 1.00 49.62 ? 254 GLY A O 1 ATOM 2020 N N . ALA A 1 254 ? -8.872 11.126 27.857 1.00 46.84 ? 255 ALA A N 1 ATOM 2021 C CA . ALA A 1 254 ? -8.541 10.519 26.577 1.00 44.33 ? 255 ALA A CA 1 ATOM 2022 C C . ALA A 1 254 ? -8.401 8.970 26.673 1.00 42.70 ? 255 ALA A C 1 ATOM 2023 O O . ALA A 1 254 ? -7.865 8.418 27.626 1.00 41.66 ? 255 ALA A O 1 ATOM 2024 C CB . ALA A 1 254 ? -7.258 11.165 26.019 1.00 43.74 ? 255 ALA A CB 1 ATOM 2025 N N . PRO A 1 255 ? -8.908 8.271 25.668 1.00 41.38 ? 256 PRO A N 1 ATOM 2026 C CA . PRO A 1 255 ? -8.861 6.819 25.631 1.00 41.02 ? 256 PRO A CA 1 ATOM 2027 C C . PRO A 1 255 ? -7.504 6.143 25.353 1.00 40.53 ? 256 PRO A C 1 ATOM 2028 O O . PRO A 1 255 ? -6.726 6.602 24.514 1.00 40.97 ? 256 PRO A O 1 ATOM 2029 C CB . PRO A 1 255 ? -9.872 6.495 24.549 1.00 40.39 ? 256 PRO A CB 1 ATOM 2030 C CG . PRO A 1 255 ? -9.675 7.609 23.613 1.00 41.31 ? 256 PRO A CG 1 ATOM 2031 C CD . PRO A 1 255 ? -9.637 8.806 24.510 1.00 40.84 ? 256 PRO A CD 1 ATOM 2032 N N . ILE A 1 256 ? -7.244 5.053 26.067 1.00 38.45 ? 257 ILE A N 1 ATOM 2033 C CA . ILE A 1 256 ? -5.973 4.365 25.930 1.00 37.74 ? 257 ILE A CA 1 ATOM 2034 C C . ILE A 1 256 ? -6.176 3.025 25.295 1.00 38.01 ? 257 ILE A C 1 ATOM 2035 O O . ILE A 1 256 ? -7.179 2.383 25.572 1.00 39.67 ? 257 ILE A O 1 ATOM 2036 C CB . ILE A 1 256 ? -5.318 4.187 27.287 1.00 37.45 ? 257 ILE A CB 1 ATOM 2037 C CG1 . ILE A 1 256 ? -4.986 5.547 27.849 1.00 40.25 ? 257 ILE A CG1 1 ATOM 2038 C CG2 . ILE A 1 256 ? -4.061 3.371 27.157 1.00 40.35 ? 257 ILE A CG2 1 ATOM 2039 C CD1 . ILE A 1 256 ? -4.517 5.511 29.314 1.00 36.26 ? 257 ILE A CD1 1 ATOM 2040 N N . SER A 1 257 ? -5.247 2.589 24.441 1.00 36.86 ? 258 SER A N 1 ATOM 2041 C CA . SER A 1 257 ? -5.323 1.303 23.798 1.00 36.50 ? 258 SER A CA 1 ATOM 2042 C C . SER A 1 257 ? -4.437 0.308 24.503 1.00 35.58 ? 258 SER A C 1 ATOM 2043 O O . SER A 1 257 ? -4.563 -0.914 24.267 1.00 37.40 ? 258 SER A O 1 ATOM 2044 C CB . SER A 1 257 ? -4.867 1.399 22.341 1.00 37.57 ? 258 SER A CB 1 ATOM 2045 O OG . SER A 1 257 ? -3.452 1.250 22.245 1.00 41.20 ? 258 SER A OG 1 ATOM 2046 N N . GLY A 1 258 ? -3.536 0.758 25.365 1.00 33.29 ? 259 GLY A N 1 ATOM 2047 C CA . GLY A 1 258 ? -2.649 -0.168 26.077 1.00 30.97 ? 259 GLY A CA 1 ATOM 2048 C C . GLY A 1 258 ? -1.474 0.625 26.673 1.00 29.28 ? 259 GLY A C 1 ATOM 2049 O O . GLY A 1 258 ? -1.484 1.840 26.661 1.00 27.58 ? 259 GLY A O 1 ATOM 2050 N N . PRO A 1 259 ? -0.463 -0.075 27.212 1.00 27.98 ? 260 PRO A N 1 ATOM 2051 C CA . PRO A 1 259 ? 0.706 0.608 27.783 1.00 27.00 ? 260 PRO A CA 1 ATOM 2052 C C . PRO A 1 259 ? 1.536 1.317 26.696 1.00 27.34 ? 260 PRO A C 1 ATOM 2053 O O . PRO A 1 259 ? 1.177 1.290 25.519 1.00 27.51 ? 260 PRO A O 1 ATOM 2054 C CB . PRO A 1 259 ? 1.480 -0.530 28.451 1.00 25.40 ? 260 PRO A CB 1 ATOM 2055 C CG . PRO A 1 259 ? 0.456 -1.635 28.595 1.00 25.37 ? 260 PRO A CG 1 ATOM 2056 C CD . PRO A 1 259 ? -0.365 -1.554 27.388 1.00 26.74 ? 260 PRO A CD 1 ATOM 2057 N N . GLY A 1 260 ? 2.626 1.953 27.095 1.00 27.90 ? 261 GLY A N 1 ATOM 2058 C CA . GLY A 1 260 ? 3.489 2.636 26.153 1.00 27.17 ? 261 GLY A CA 1 ATOM 2059 C C . GLY A 1 260 ? 4.572 1.663 25.700 1.00 27.18 ? 261 GLY A C 1 ATOM 2060 O O . GLY A 1 260 ? 4.776 0.616 26.304 1.00 25.84 ? 261 GLY A O 1 ATOM 2061 N N . ILE A 1 261 ? 5.275 1.961 24.613 1.00 28.18 ? 262 ILE A N 1 ATOM 2062 C CA . ILE A 1 261 ? 6.320 1.034 24.173 1.00 28.75 ? 262 ILE A CA 1 ATOM 2063 C C . ILE A 1 261 ? 7.508 1.208 25.083 1.00 28.85 ? 262 ILE A C 1 ATOM 2064 O O . ILE A 1 261 ? 7.710 2.239 25.668 1.00 29.53 ? 262 ILE A O 1 ATOM 2065 C CB . ILE A 1 261 ? 6.837 1.220 22.750 1.00 29.47 ? 262 ILE A CB 1 ATOM 2066 C CG1 . ILE A 1 261 ? 7.683 2.487 22.622 1.00 29.17 ? 262 ILE A CG1 1 ATOM 2067 C CG2 . ILE A 1 261 ? 5.728 1.221 21.757 1.00 31.52 ? 262 ILE A CG2 1 ATOM 2068 C CD1 . ILE A 1 261 ? 6.938 3.655 22.202 1.00 24.00 ? 262 ILE A CD1 1 ATOM 2069 N N . PRO A 1 262 ? 8.284 0.160 25.204 1.00 28.43 ? 263 PRO A N 1 ATOM 2070 C CA . PRO A 1 262 ? 9.438 0.082 26.095 1.00 28.56 ? 263 PRO A CA 1 ATOM 2071 C C . PRO A 1 262 ? 10.541 1.096 25.880 1.00 28.07 ? 263 PRO A C 1 ATOM 2072 O O . PRO A 1 262 ? 10.721 1.660 24.811 1.00 28.60 ? 263 PRO A O 1 ATOM 2073 C CB . PRO A 1 262 ? 9.924 -1.318 25.869 1.00 28.35 ? 263 PRO A CB 1 ATOM 2074 C CG . PRO A 1 262 ? 8.659 -2.024 25.587 1.00 28.96 ? 263 PRO A CG 1 ATOM 2075 C CD . PRO A 1 262 ? 7.983 -1.132 24.607 1.00 28.56 ? 263 PRO A CD 1 ATOM 2076 N N . GLY A 1 263 ? 11.274 1.336 26.957 1.00 27.90 ? 264 GLY A N 1 ATOM 2077 C CA . GLY A 1 263 ? 12.378 2.261 26.940 1.00 27.45 ? 264 GLY A CA 1 ATOM 2078 C C . GLY A 1 263 ? 13.575 1.517 26.433 1.00 26.42 ? 264 GLY A C 1 ATOM 2079 O O . GLY A 1 263 ? 13.717 0.372 26.738 1.00 26.34 ? 264 GLY A O 1 ATOM 2080 N N . ARG A 1 264 ? 14.434 2.163 25.668 1.00 26.39 ? 265 ARG A N 1 ATOM 2081 C CA . ARG A 1 264 ? 15.579 1.479 25.093 1.00 28.20 ? 265 ARG A CA 1 ATOM 2082 C C . ARG A 1 264 ? 16.511 0.772 26.109 1.00 26.50 ? 265 ARG A C 1 ATOM 2083 O O . ARG A 1 264 ? 17.198 -0.191 25.756 1.00 26.31 ? 265 ARG A O 1 ATOM 2084 C CB . ARG A 1 264 ? 16.363 2.457 24.252 1.00 30.31 ? 265 ARG A CB 1 ATOM 2085 C CG . ARG A 1 264 ? 16.981 1.842 23.023 1.00 38.99 ? 265 ARG A CG 1 ATOM 2086 C CD . ARG A 1 264 ? 18.426 2.332 22.795 1.00 46.67 ? 265 ARG A CD 1 ATOM 2087 N NE . ARG A 1 264 ? 18.533 3.797 22.831 1.00 53.58 ? 265 ARG A NE 1 ATOM 2088 C CZ . ARG A 1 264 ? 19.691 4.464 22.846 1.00 58.92 ? 265 ARG A CZ 1 ATOM 2089 N NH1 . ARG A 1 264 ? 20.858 3.786 22.838 1.00 62.58 ? 265 ARG A NH1 1 ATOM 2090 N NH2 . ARG A 1 264 ? 19.695 5.802 22.883 1.00 57.27 ? 265 ARG A NH2 1 ATOM 2091 N N . PHE A 1 265 ? 16.528 1.240 27.357 1.00 24.47 ? 266 PHE A N 1 ATOM 2092 C CA . PHE A 1 265 ? 17.366 0.653 28.351 1.00 23.80 ? 266 PHE A CA 1 ATOM 2093 C C . PHE A 1 265 ? 16.502 -0.070 29.383 1.00 23.80 ? 266 PHE A C 1 ATOM 2094 O O . PHE A 1 265 ? 16.837 -1.135 29.897 1.00 24.63 ? 266 PHE A O 1 ATOM 2095 C CB . PHE A 1 265 ? 18.132 1.715 29.095 1.00 24.49 ? 266 PHE A CB 1 ATOM 2096 C CG . PHE A 1 265 ? 19.009 2.569 28.252 1.00 25.42 ? 266 PHE A CG 1 ATOM 2097 C CD1 . PHE A 1 265 ? 18.582 3.808 27.866 1.00 25.58 ? 266 PHE A CD1 1 ATOM 2098 C CD2 . PHE A 1 265 ? 20.306 2.178 27.941 1.00 26.73 ? 266 PHE A CD2 1 ATOM 2099 C CE1 . PHE A 1 265 ? 19.412 4.640 27.140 1.00 25.33 ? 266 PHE A CE1 1 ATOM 2100 C CE2 . PHE A 1 265 ? 21.132 3.000 27.223 1.00 28.74 ? 266 PHE A CE2 1 ATOM 2101 C CZ . PHE A 1 265 ? 20.685 4.238 26.818 1.00 27.33 ? 266 PHE A CZ 1 ATOM 2102 N N . THR A 1 266 ? 15.411 0.548 29.753 1.00 22.78 ? 267 THR A N 1 ATOM 2103 C CA . THR A 1 266 ? 14.548 -0.012 30.749 1.00 22.15 ? 267 THR A CA 1 ATOM 2104 C C . THR A 1 266 ? 13.845 -1.319 30.280 1.00 23.38 ? 267 THR A C 1 ATOM 2105 O O . THR A 1 266 ? 13.486 -2.188 31.082 1.00 23.17 ? 267 THR A O 1 ATOM 2106 C CB . THR A 1 266 ? 13.572 1.092 31.145 1.00 21.33 ? 267 THR A CB 1 ATOM 2107 O OG1 . THR A 1 266 ? 13.684 1.312 32.550 1.00 15.45 ? 267 THR A OG1 1 ATOM 2108 C CG2 . THR A 1 266 ? 12.076 0.696 30.804 1.00 21.66 ? 267 THR A CG2 1 ATOM 2109 N N . LYS A 1 267 ? 13.665 -1.452 28.974 1.00 23.80 ? 268 LYS A N 1 ATOM 2110 C CA . LYS A 1 267 ? 13.008 -2.601 28.386 1.00 25.25 ? 268 LYS A CA 1 ATOM 2111 C C . LYS A 1 267 ? 11.814 -3.129 29.178 1.00 26.62 ? 268 LYS A C 1 ATOM 2112 O O . LYS A 1 267 ? 11.812 -4.215 29.639 1.00 27.97 ? 268 LYS A O 1 ATOM 2113 C CB . LYS A 1 267 ? 14.007 -3.716 28.152 1.00 25.25 ? 268 LYS A CB 1 ATOM 2114 C CG . LYS A 1 267 ? 14.990 -3.495 27.020 1.00 27.65 ? 268 LYS A CG 1 ATOM 2115 C CD . LYS A 1 267 ? 15.945 -4.684 26.863 1.00 32.38 ? 268 LYS A CD 1 ATOM 2116 C CE . LYS A 1 267 ? 16.920 -4.508 25.703 1.00 37.61 ? 268 LYS A CE 1 ATOM 2117 N NZ . LYS A 1 267 ? 17.774 -3.253 25.805 1.00 40.54 ? 268 LYS A NZ 1 ATOM 2118 N N . GLU A 1 268 ? 10.770 -2.352 29.317 1.00 29.78 ? 269 GLU A N 1 ATOM 2119 C CA . GLU A 1 268 ? 9.565 -2.790 30.038 1.00 31.54 ? 269 GLU A CA 1 ATOM 2120 C C . GLU A 1 268 ? 8.366 -1.876 29.702 1.00 31.09 ? 269 GLU A C 1 ATOM 2121 O O . GLU A 1 268 ? 8.438 -0.647 29.803 1.00 30.74 ? 269 GLU A O 1 ATOM 2122 C CB . GLU A 1 268 ? 9.798 -2.812 31.547 1.00 33.11 ? 269 GLU A CB 1 ATOM 2123 C CG . GLU A 1 268 ? 8.734 -3.554 32.325 1.00 37.66 ? 269 GLU A CG 1 ATOM 2124 C CD . GLU A 1 268 ? 8.827 -3.328 33.826 1.00 43.61 ? 269 GLU A CD 1 ATOM 2125 O OE1 . GLU A 1 268 ? 9.961 -3.362 34.388 1.00 46.28 ? 269 GLU A OE1 1 ATOM 2126 O OE2 . GLU A 1 268 ? 7.756 -3.122 34.448 1.00 47.89 ? 269 GLU A OE2 1 ATOM 2127 N N . LYS A 1 269 ? 7.270 -2.490 29.303 1.00 30.63 ? 270 LYS A N 1 ATOM 2128 C CA . LYS A 1 269 ? 6.091 -1.763 28.926 1.00 30.96 ? 270 LYS A CA 1 ATOM 2129 C C . LYS A 1 269 ? 5.496 -0.920 30.012 1.00 30.40 ? 270 LYS A C 1 ATOM 2130 O O . LYS A 1 269 ? 5.562 -1.259 31.179 1.00 31.84 ? 270 LYS A O 1 ATOM 2131 C CB . LYS A 1 269 ? 5.050 -2.739 28.465 1.00 32.46 ? 270 LYS A CB 1 ATOM 2132 C CG . LYS A 1 269 ? 5.390 -3.332 27.105 1.00 37.72 ? 270 LYS A CG 1 ATOM 2133 C CD . LYS A 1 269 ? 4.380 -4.383 26.665 1.00 41.95 ? 270 LYS A CD 1 ATOM 2134 C CE . LYS A 1 269 ? 4.601 -5.678 27.402 1.00 43.78 ? 270 LYS A CE 1 ATOM 2135 N NZ . LYS A 1 269 ? 4.461 -6.861 26.446 1.00 48.09 ? 270 LYS A NZ 1 ATOM 2136 N N . GLY A 1 270 ? 4.921 0.206 29.616 1.00 29.09 ? 271 GLY A N 1 ATOM 2137 C CA . GLY A 1 270 ? 4.268 1.116 30.534 1.00 27.99 ? 271 GLY A CA 1 ATOM 2138 C C . GLY A 1 270 ? 5.134 1.804 31.550 1.00 26.85 ? 271 GLY A C 1 ATOM 2139 O O . GLY A 1 270 ? 4.633 2.519 32.428 1.00 27.65 ? 271 GLY A O 1 ATOM 2140 N N . ILE A 1 271 ? 6.425 1.622 31.402 1.00 25.89 ? 272 ILE A N 1 ATOM 2141 C CA . ILE A 1 271 ? 7.390 2.206 32.328 1.00 25.00 ? 272 ILE A CA 1 ATOM 2142 C C . ILE A 1 271 ? 8.527 2.924 31.583 1.00 22.61 ? 272 ILE A C 1 ATOM 2143 O O . ILE A 1 271 ? 8.879 2.563 30.483 1.00 22.85 ? 272 ILE A O 1 ATOM 2144 C CB . ILE A 1 271 ? 7.990 1.081 33.163 1.00 25.41 ? 272 ILE A CB 1 ATOM 2145 C CG1 . ILE A 1 271 ? 7.051 0.694 34.288 1.00 27.33 ? 272 ILE A CG1 1 ATOM 2146 C CG2 . ILE A 1 271 ? 9.341 1.472 33.714 1.00 25.79 ? 272 ILE A CG2 1 ATOM 2147 C CD1 . ILE A 1 271 ? 7.225 1.450 35.549 1.00 24.35 ? 272 ILE A CD1 1 ATOM 2148 N N . LEU A 1 272 ? 9.099 3.923 32.227 1.00 20.28 ? 273 LEU A N 1 ATOM 2149 C CA . LEU A 1 272 ? 10.210 4.683 31.673 1.00 17.99 ? 273 LEU A CA 1 ATOM 2150 C C . LEU A 1 272 ? 11.095 5.266 32.751 1.00 16.18 ? 273 LEU A C 1 ATOM 2151 O O . LEU A 1 272 ? 10.616 5.967 33.625 1.00 15.68 ? 273 LEU A O 1 ATOM 2152 C CB . LEU A 1 272 ? 9.708 5.858 30.816 1.00 17.49 ? 273 LEU A CB 1 ATOM 2153 C CG . LEU A 1 272 ? 9.264 5.559 29.379 1.00 16.58 ? 273 LEU A CG 1 ATOM 2154 C CD1 . LEU A 1 272 ? 8.925 6.868 28.664 1.00 11.69 ? 273 LEU A CD1 1 ATOM 2155 C CD2 . LEU A 1 272 ? 10.382 4.830 28.622 1.00 17.24 ? 273 LEU A CD2 1 ATOM 2156 N N . ALA A 1 273 ? 12.382 5.001 32.683 1.00 15.54 ? 274 ALA A N 1 ATOM 2157 C CA . ALA A 1 273 ? 13.282 5.593 33.644 1.00 17.05 ? 274 ALA A CA 1 ATOM 2158 C C . ALA A 1 273 ? 13.256 7.096 33.395 1.00 17.55 ? 274 ALA A C 1 ATOM 2159 O O . ALA A 1 273 ? 12.854 7.534 32.335 1.00 19.63 ? 274 ALA A O 1 ATOM 2160 C CB . ALA A 1 273 ? 14.682 5.080 33.464 1.00 17.39 ? 274 ALA A CB 1 ATOM 2161 N N . TYR A 1 274 ? 13.678 7.888 34.359 1.00 17.23 ? 275 TYR A N 1 ATOM 2162 C CA . TYR A 1 274 ? 13.669 9.322 34.175 1.00 17.34 ? 275 TYR A CA 1 ATOM 2163 C C . TYR A 1 274 ? 14.650 9.759 33.112 1.00 17.62 ? 275 TYR A C 1 ATOM 2164 O O . TYR A 1 274 ? 14.320 10.600 32.296 1.00 18.81 ? 275 TYR A O 1 ATOM 2165 C CB . TYR A 1 274 ? 13.985 10.060 35.479 1.00 18.26 ? 275 TYR A CB 1 ATOM 2166 C CG . TYR A 1 274 ? 14.017 11.566 35.333 1.00 14.50 ? 275 TYR A CG 1 ATOM 2167 C CD1 . TYR A 1 274 ? 12.959 12.236 34.866 1.00 15.74 ? 275 TYR A CD1 1 ATOM 2168 C CD2 . TYR A 1 274 ? 15.114 12.273 35.701 1.00 16.99 ? 275 TYR A CD2 1 ATOM 2169 C CE1 . TYR A 1 274 ? 12.968 13.599 34.753 1.00 20.31 ? 275 TYR A CE1 1 ATOM 2170 C CE2 . TYR A 1 274 ? 15.177 13.615 35.598 1.00 19.29 ? 275 TYR A CE2 1 ATOM 2171 C CZ . TYR A 1 274 ? 14.100 14.296 35.118 1.00 21.69 ? 275 TYR A CZ 1 ATOM 2172 O OH . TYR A 1 274 ? 14.169 15.665 34.973 1.00 21.47 ? 275 TYR A OH 1 ATOM 2173 N N . TYR A 1 275 ? 15.853 9.187 33.120 1.00 17.01 ? 276 TYR A N 1 ATOM 2174 C CA . TYR A 1 275 ? 16.886 9.549 32.156 1.00 16.12 ? 276 TYR A CA 1 ATOM 2175 C C . TYR A 1 275 ? 16.398 9.261 30.738 1.00 16.76 ? 276 TYR A C 1 ATOM 2176 O O . TYR A 1 275 ? 16.890 9.853 29.786 1.00 18.21 ? 276 TYR A O 1 ATOM 2177 C CB . TYR A 1 275 ? 18.196 8.813 32.468 1.00 14.62 ? 276 TYR A CB 1 ATOM 2178 C CG . TYR A 1 275 ? 18.141 7.272 32.510 1.00 11.82 ? 276 TYR A CG 1 ATOM 2179 C CD1 . TYR A 1 275 ? 18.018 6.523 31.383 1.00 10.29 ? 276 TYR A CD1 1 ATOM 2180 C CD2 . TYR A 1 275 ? 18.279 6.607 33.666 1.00 10.71 ? 276 TYR A CD2 1 ATOM 2181 C CE1 . TYR A 1 275 ? 18.028 5.147 31.420 1.00 8.71 ? 276 TYR A CE1 1 ATOM 2182 C CE2 . TYR A 1 275 ? 18.297 5.246 33.707 1.00 11.07 ? 276 TYR A CE2 1 ATOM 2183 C CZ . TYR A 1 275 ? 18.180 4.506 32.574 1.00 8.54 ? 276 TYR A CZ 1 ATOM 2184 O OH . TYR A 1 275 ? 18.184 3.096 32.616 1.00 7.21 ? 276 TYR A OH 1 ATOM 2185 N N . GLU A 1 276 ? 15.439 8.342 30.604 1.00 16.28 ? 277 GLU A N 1 ATOM 2186 C CA . GLU A 1 276 ? 14.857 7.965 29.311 1.00 15.50 ? 277 GLU A CA 1 ATOM 2187 C C . GLU A 1 276 ? 13.871 9.044 28.911 1.00 15.92 ? 277 GLU A C 1 ATOM 2188 O O . GLU A 1 276 ? 13.762 9.417 27.777 1.00 14.56 ? 277 GLU A O 1 ATOM 2189 C CB . GLU A 1 276 ? 14.130 6.616 29.428 1.00 14.21 ? 277 GLU A CB 1 ATOM 2190 C CG . GLU A 1 276 ? 15.039 5.428 29.704 1.00 14.01 ? 277 GLU A CG 1 ATOM 2191 C CD . GLU A 1 276 ? 14.326 4.075 29.693 1.00 14.87 ? 277 GLU A CD 1 ATOM 2192 O OE1 . GLU A 1 276 ? 13.492 3.797 30.531 1.00 12.71 ? 277 GLU A OE1 1 ATOM 2193 O OE2 . GLU A 1 276 ? 14.642 3.262 28.834 1.00 21.62 ? 277 GLU A OE2 1 ATOM 2194 N N . ILE A 1 277 ? 13.148 9.519 29.911 1.00 17.84 ? 278 ILE A N 1 ATOM 2195 C CA . ILE A 1 277 ? 12.143 10.565 29.748 1.00 18.04 ? 278 ILE A CA 1 ATOM 2196 C C . ILE A 1 277 ? 12.805 11.858 29.291 1.00 18.33 ? 278 ILE A C 1 ATOM 2197 O O . ILE A 1 277 ? 12.225 12.636 28.554 1.00 17.27 ? 278 ILE A O 1 ATOM 2198 C CB . ILE A 1 277 ? 11.371 10.797 31.047 1.00 17.15 ? 278 ILE A CB 1 ATOM 2199 C CG1 . ILE A 1 277 ? 10.626 9.549 31.422 1.00 18.92 ? 278 ILE A CG1 1 ATOM 2200 C CG2 . ILE A 1 277 ? 10.403 11.909 30.878 1.00 18.05 ? 278 ILE A CG2 1 ATOM 2201 C CD1 . ILE A 1 277 ? 9.970 9.626 32.806 1.00 22.76 ? 278 ILE A CD1 1 ATOM 2202 N N . CYS A 1 278 ? 14.024 12.079 29.755 1.00 20.13 ? 279 CYS A N 1 ATOM 2203 C CA . CYS A 1 278 ? 14.771 13.264 29.386 1.00 22.15 ? 279 CYS A CA 1 ATOM 2204 C C . CYS A 1 278 ? 15.013 13.245 27.886 1.00 23.58 ? 279 CYS A C 1 ATOM 2205 O O . CYS A 1 278 ? 14.837 14.234 27.192 1.00 26.06 ? 279 CYS A O 1 ATOM 2206 C CB . CYS A 1 278 ? 16.091 13.324 30.116 1.00 20.27 ? 279 CYS A CB 1 ATOM 2207 S SG . CYS A 1 278 ? 15.869 13.778 31.792 1.00 25.48 ? 279 CYS A SG 1 ATOM 2208 N N . ASP A 1 279 ? 15.420 12.105 27.375 1.00 23.46 ? 280 ASP A N 1 ATOM 2209 C CA . ASP A 1 279 ? 15.660 11.976 25.954 1.00 23.24 ? 280 ASP A CA 1 ATOM 2210 C C . ASP A 1 279 ? 14.317 12.099 25.243 1.00 21.92 ? 280 ASP A C 1 ATOM 2211 O O . ASP A 1 279 ? 14.179 12.840 24.335 1.00 22.79 ? 280 ASP A O 1 ATOM 2212 C CB . ASP A 1 279 ? 16.296 10.650 25.684 1.00 25.04 ? 280 ASP A CB 1 ATOM 2213 C CG . ASP A 1 279 ? 16.602 10.433 24.245 1.00 29.58 ? 280 ASP A CG 1 ATOM 2214 O OD1 . ASP A 1 279 ? 17.367 11.263 23.691 1.00 37.21 ? 280 ASP A OD1 1 ATOM 2215 O OD2 . ASP A 1 279 ? 16.151 9.435 23.621 1.00 32.22 ? 280 ASP A OD2 1 ATOM 2216 N N . PHE A 1 280 ? 13.305 11.414 25.728 1.00 22.12 ? 281 PHE A N 1 ATOM 2217 C CA . PHE A 1 280 ? 11.956 11.455 25.149 1.00 22.58 ? 281 PHE A CA 1 ATOM 2218 C C . PHE A 1 280 ? 11.372 12.886 24.907 1.00 24.37 ? 281 PHE A C 1 ATOM 2219 O O . PHE A 1 280 ? 10.780 13.167 23.884 1.00 23.75 ? 281 PHE A O 1 ATOM 2220 C CB . PHE A 1 280 ? 11.001 10.692 26.075 1.00 20.89 ? 281 PHE A CB 1 ATOM 2221 C CG . PHE A 1 280 ? 9.563 10.761 25.641 1.00 18.30 ? 281 PHE A CG 1 ATOM 2222 C CD1 . PHE A 1 280 ? 9.017 9.744 24.848 1.00 15.04 ? 281 PHE A CD1 1 ATOM 2223 C CD2 . PHE A 1 280 ? 8.743 11.815 26.029 1.00 13.89 ? 281 PHE A CD2 1 ATOM 2224 C CE1 . PHE A 1 280 ? 7.699 9.801 24.425 1.00 12.35 ? 281 PHE A CE1 1 ATOM 2225 C CE2 . PHE A 1 280 ? 7.416 11.823 25.624 1.00 11.80 ? 281 PHE A CE2 1 ATOM 2226 C CZ . PHE A 1 280 ? 6.911 10.822 24.821 1.00 11.32 ? 281 PHE A CZ 1 ATOM 2227 N N . LEU A 1 281 ? 11.539 13.770 25.881 1.00 26.90 ? 282 LEU A N 1 ATOM 2228 C CA . LEU A 1 281 ? 11.018 15.093 25.797 1.00 27.62 ? 282 LEU A CA 1 ATOM 2229 C C . LEU A 1 281 ? 11.380 15.835 24.549 1.00 29.39 ? 282 LEU A C 1 ATOM 2230 O O . LEU A 1 281 ? 10.677 16.778 24.194 1.00 30.20 ? 282 LEU A O 1 ATOM 2231 C CB . LEU A 1 281 ? 11.512 15.883 26.985 1.00 28.69 ? 282 LEU A CB 1 ATOM 2232 C CG . LEU A 1 281 ? 10.608 16.020 28.219 1.00 27.38 ? 282 LEU A CG 1 ATOM 2233 C CD1 . LEU A 1 281 ? 9.516 14.947 28.265 1.00 27.61 ? 282 LEU A CD1 1 ATOM 2234 C CD2 . LEU A 1 281 ? 11.484 15.998 29.421 1.00 25.23 ? 282 LEU A CD2 1 ATOM 2235 N N . HIS A 1 282 ? 12.487 15.455 23.897 1.00 31.65 ? 283 HIS A N 1 ATOM 2236 C CA . HIS A 1 282 ? 12.938 16.126 22.655 1.00 32.80 ? 283 HIS A CA 1 ATOM 2237 C C . HIS A 1 282 ? 11.935 15.873 21.525 1.00 33.06 ? 283 HIS A C 1 ATOM 2238 O O . HIS A 1 282 ? 11.806 14.754 21.020 1.00 32.34 ? 283 HIS A O 1 ATOM 2239 C CB . HIS A 1 282 ? 14.340 15.666 22.242 1.00 33.17 ? 283 HIS A CB 1 ATOM 2240 C CG . HIS A 1 282 ? 15.430 16.124 23.177 1.00 38.68 ? 283 HIS A CG 1 ATOM 2241 N ND1 . HIS A 1 282 ? 15.593 17.437 23.563 1.00 44.89 ? 283 HIS A ND1 1 ATOM 2242 C CD2 . HIS A 1 282 ? 16.427 15.442 23.792 1.00 43.04 ? 283 HIS A CD2 1 ATOM 2243 C CE1 . HIS A 1 282 ? 16.629 17.545 24.378 1.00 43.61 ? 283 HIS A CE1 1 ATOM 2244 N NE2 . HIS A 1 282 ? 17.155 16.347 24.531 1.00 44.29 ? 283 HIS A NE2 1 ATOM 2245 N N . GLY A 1 283 ? 11.208 16.922 21.161 1.00 32.86 ? 284 GLY A N 1 ATOM 2246 C CA . GLY A 1 283 ? 10.221 16.822 20.116 1.00 33.65 ? 284 GLY A CA 1 ATOM 2247 C C . GLY A 1 283 ? 8.873 16.452 20.702 1.00 34.08 ? 284 GLY A C 1 ATOM 2248 O O . GLY A 1 283 ? 7.886 16.222 19.966 1.00 35.73 ? 284 GLY A O 1 ATOM 2249 N N . ALA A 1 284 ? 8.823 16.394 22.024 1.00 33.40 ? 285 ALA A N 1 ATOM 2250 C CA . ALA A 1 284 ? 7.590 16.054 22.726 1.00 32.71 ? 285 ALA A CA 1 ATOM 2251 C C . ALA A 1 284 ? 6.908 17.340 23.179 1.00 32.78 ? 285 ALA A C 1 ATOM 2252 O O . ALA A 1 284 ? 7.561 18.358 23.363 1.00 32.86 ? 285 ALA A O 1 ATOM 2253 C CB . ALA A 1 284 ? 7.898 15.188 23.919 1.00 31.60 ? 285 ALA A CB 1 ATOM 2254 N N . THR A 1 285 ? 5.606 17.279 23.351 1.00 32.89 ? 286 THR A N 1 ATOM 2255 C CA . THR A 1 285 ? 4.856 18.418 23.802 1.00 34.48 ? 286 THR A CA 1 ATOM 2256 C C . THR A 1 285 ? 4.733 18.196 25.302 1.00 35.86 ? 286 THR A C 1 ATOM 2257 O O . THR A 1 285 ? 4.545 17.060 25.739 1.00 37.86 ? 286 THR A O 1 ATOM 2258 C CB . THR A 1 285 ? 3.423 18.411 23.186 1.00 35.38 ? 286 THR A CB 1 ATOM 2259 O OG1 . THR A 1 285 ? 3.471 18.319 21.752 1.00 37.52 ? 286 THR A OG1 1 ATOM 2260 C CG2 . THR A 1 285 ? 2.710 19.701 23.483 1.00 34.66 ? 286 THR A CG2 1 ATOM 2261 N N . THR A 1 286 ? 4.851 19.242 26.104 1.00 35.57 ? 287 THR A N 1 ATOM 2262 C CA . THR A 1 286 ? 4.746 19.074 27.550 1.00 34.85 ? 287 THR A CA 1 ATOM 2263 C C . THR A 1 286 ? 3.572 19.860 28.077 1.00 36.30 ? 287 THR A C 1 ATOM 2264 O O . THR A 1 286 ? 3.321 20.969 27.683 1.00 36.80 ? 287 THR A O 1 ATOM 2265 C CB . THR A 1 286 ? 5.996 19.548 28.243 1.00 33.58 ? 287 THR A CB 1 ATOM 2266 O OG1 . THR A 1 286 ? 5.962 20.980 28.299 1.00 35.88 ? 287 THR A OG1 1 ATOM 2267 C CG2 . THR A 1 286 ? 7.244 19.157 27.459 1.00 33.60 ? 287 THR A CG2 1 ATOM 2268 N N . HIS A 1 287 ? 2.863 19.269 29.003 1.00 38.74 ? 288 HIS A N 1 ATOM 2269 C CA . HIS A 1 287 ? 1.715 19.883 29.628 1.00 40.67 ? 288 HIS A CA 1 ATOM 2270 C C . HIS A 1 287 ? 1.882 19.720 31.137 1.00 39.65 ? 288 HIS A C 1 ATOM 2271 O O . HIS A 1 287 ? 2.785 18.996 31.582 1.00 38.14 ? 288 HIS A O 1 ATOM 2272 C CB . HIS A 1 287 ? 0.428 19.171 29.169 1.00 43.77 ? 288 HIS A CB 1 ATOM 2273 C CG . HIS A 1 287 ? 0.244 19.138 27.678 1.00 51.32 ? 288 HIS A CG 1 ATOM 2274 N ND1 . HIS A 1 287 ? 0.326 20.278 26.892 1.00 57.96 ? 288 HIS A ND1 1 ATOM 2275 C CD2 . HIS A 1 287 ? -0.051 18.116 26.838 1.00 54.94 ? 288 HIS A CD2 1 ATOM 2276 C CE1 . HIS A 1 287 ? 0.091 19.952 25.632 1.00 59.95 ? 288 HIS A CE1 1 ATOM 2277 N NE2 . HIS A 1 287 ? -0.136 18.646 25.572 1.00 59.63 ? 288 HIS A NE2 1 ATOM 2278 N N . ARG A 1 288 ? 1.019 20.379 31.921 1.00 39.44 ? 289 ARG A N 1 ATOM 2279 C CA . ARG A 1 288 ? 1.117 20.309 33.377 1.00 38.53 ? 289 ARG A CA 1 ATOM 2280 C C . ARG A 1 288 ? -0.165 20.608 34.108 1.00 38.61 ? 289 ARG A C 1 ATOM 2281 O O . ARG A 1 288 ? -0.593 21.737 34.120 1.00 39.14 ? 289 ARG A O 1 ATOM 2282 C CB . ARG A 1 288 ? 2.185 21.269 33.864 1.00 37.11 ? 289 ARG A CB 1 ATOM 2283 C CG . ARG A 1 288 ? 2.327 21.332 35.363 1.00 36.17 ? 289 ARG A CG 1 ATOM 2284 C CD . ARG A 1 288 ? 3.328 22.386 35.807 1.00 35.78 ? 289 ARG A CD 1 ATOM 2285 N NE . ARG A 1 288 ? 4.679 22.007 35.456 1.00 36.33 ? 289 ARG A NE 1 ATOM 2286 C CZ . ARG A 1 288 ? 5.399 21.135 36.123 1.00 36.93 ? 289 ARG A CZ 1 ATOM 2287 N NH1 . ARG A 1 288 ? 4.901 20.569 37.211 1.00 38.06 ? 289 ARG A NH1 1 ATOM 2288 N NH2 . ARG A 1 288 ? 6.622 20.813 35.700 1.00 36.91 ? 289 ARG A NH2 1 ATOM 2289 N N . PHE A 1 289 ? -0.739 19.585 34.737 1.00 38.86 ? 290 PHE A N 1 ATOM 2290 C CA . PHE A 1 289 ? -1.948 19.716 35.505 1.00 39.12 ? 290 PHE A CA 1 ATOM 2291 C C . PHE A 1 289 ? -1.709 20.711 36.596 1.00 40.41 ? 290 PHE A C 1 ATOM 2292 O O . PHE A 1 289 ? -0.999 20.473 37.498 1.00 41.03 ? 290 PHE A O 1 ATOM 2293 C CB . PHE A 1 289 ? -2.335 18.401 36.129 1.00 38.99 ? 290 PHE A CB 1 ATOM 2294 C CG . PHE A 1 289 ? -2.565 17.282 35.138 1.00 41.06 ? 290 PHE A CG 1 ATOM 2295 C CD1 . PHE A 1 289 ? -3.537 17.373 34.198 1.00 44.14 ? 290 PHE A CD1 1 ATOM 2296 C CD2 . PHE A 1 289 ? -1.845 16.106 35.208 1.00 43.03 ? 290 PHE A CD2 1 ATOM 2297 C CE1 . PHE A 1 289 ? -3.768 16.329 33.317 1.00 45.08 ? 290 PHE A CE1 1 ATOM 2298 C CE2 . PHE A 1 289 ? -2.082 15.055 34.344 1.00 42.13 ? 290 PHE A CE2 1 ATOM 2299 C CZ . PHE A 1 289 ? -3.031 15.174 33.402 1.00 43.66 ? 290 PHE A CZ 1 ATOM 2300 N N . ARG A 1 290 ? -2.315 21.859 36.500 1.00 43.54 ? 291 ARG A N 1 ATOM 2301 C CA . ARG A 1 290 ? -2.162 22.881 37.497 1.00 46.58 ? 291 ARG A CA 1 ATOM 2302 C C . ARG A 1 290 ? -2.745 22.378 38.808 1.00 45.42 ? 291 ARG A C 1 ATOM 2303 O O . ARG A 1 290 ? -2.153 22.535 39.849 1.00 46.66 ? 291 ARG A O 1 ATOM 2304 C CB . ARG A 1 290 ? -2.912 24.120 37.033 1.00 50.01 ? 291 ARG A CB 1 ATOM 2305 C CG . ARG A 1 290 ? -4.394 23.901 36.871 1.00 57.23 ? 291 ARG A CG 1 ATOM 2306 C CD . ARG A 1 290 ? -5.183 25.045 37.513 1.00 67.15 ? 291 ARG A CD 1 ATOM 2307 N NE . ARG A 1 290 ? -4.690 25.322 38.874 1.00 74.01 ? 291 ARG A NE 1 ATOM 2308 C CZ . ARG A 1 290 ? -5.108 26.327 39.654 1.00 77.55 ? 291 ARG A CZ 1 ATOM 2309 N NH1 . ARG A 1 290 ? -6.049 27.173 39.229 1.00 78.09 ? 291 ARG A NH1 1 ATOM 2310 N NH2 . ARG A 1 290 ? -4.577 26.479 40.867 1.00 79.29 ? 291 ARG A NH2 1 ATOM 2311 N N . ASP A 1 291 ? -3.922 21.774 38.736 1.00 44.35 ? 292 ASP A N 1 ATOM 2312 C CA . ASP A 1 291 ? -4.639 21.230 39.884 1.00 43.60 ? 292 ASP A CA 1 ATOM 2313 C C . ASP A 1 291 ? -3.743 20.299 40.724 1.00 40.81 ? 292 ASP A C 1 ATOM 2314 O O . ASP A 1 291 ? -3.537 20.511 41.894 1.00 39.33 ? 292 ASP A O 1 ATOM 2315 C CB . ASP A 1 291 ? -5.839 20.339 39.396 1.00 45.79 ? 292 ASP A CB 1 ATOM 2316 C CG . ASP A 1 291 ? -7.215 21.049 39.241 1.00 49.05 ? 292 ASP A CG 1 ATOM 2317 O OD1 . ASP A 1 291 ? -7.389 22.208 39.719 1.00 49.29 ? 292 ASP A OD1 1 ATOM 2318 O OD2 . ASP A 1 291 ? -8.156 20.421 38.656 1.00 50.22 ? 292 ASP A OD2 1 ATOM 2319 N N . GLN A 1 292 ? -3.242 19.245 40.101 1.00 38.74 ? 293 GLN A N 1 ATOM 2320 C CA . GLN A 1 292 ? -2.442 18.227 40.789 1.00 36.84 ? 293 GLN A CA 1 ATOM 2321 C C . GLN A 1 292 ? -0.937 18.521 40.858 1.00 33.19 ? 293 GLN A C 1 ATOM 2322 O O . GLN A 1 292 ? -0.178 17.847 41.530 1.00 31.09 ? 293 GLN A O 1 ATOM 2323 C CB . GLN A 1 292 ? -2.696 16.889 40.110 1.00 37.97 ? 293 GLN A CB 1 ATOM 2324 C CG . GLN A 1 292 ? -4.169 16.597 39.954 1.00 40.72 ? 293 GLN A CG 1 ATOM 2325 C CD . GLN A 1 292 ? -4.478 15.796 38.697 1.00 46.94 ? 293 GLN A CD 1 ATOM 2326 O OE1 . GLN A 1 292 ? -4.463 14.557 38.694 1.00 49.15 ? 293 GLN A OE1 1 ATOM 2327 N NE2 . GLN A 1 292 ? -4.772 16.506 37.615 1.00 51.62 ? 293 GLN A NE2 1 ATOM 2328 N N . GLN A 1 293 ? -0.533 19.551 40.144 1.00 30.52 ? 294 GLN A N 1 ATOM 2329 C CA . GLN A 1 293 ? 0.848 19.999 40.126 1.00 28.49 ? 294 GLN A CA 1 ATOM 2330 C C . GLN A 1 293 ? 1.830 18.884 39.703 1.00 25.50 ? 294 GLN A C 1 ATOM 2331 O O . GLN A 1 293 ? 2.784 18.580 40.438 1.00 26.51 ? 294 GLN A O 1 ATOM 2332 C CB . GLN A 1 293 ? 1.212 20.550 41.510 1.00 29.21 ? 294 GLN A CB 1 ATOM 2333 C CG . GLN A 1 293 ? 0.085 21.203 42.248 1.00 29.46 ? 294 GLN A CG 1 ATOM 2334 C CD . GLN A 1 293 ? 0.554 22.328 43.046 1.00 30.93 ? 294 GLN A CD 1 ATOM 2335 O OE1 . GLN A 1 293 ? 0.906 23.349 42.489 1.00 36.99 ? 294 GLN A OE1 1 ATOM 2336 N NE2 . GLN A 1 293 ? 0.605 22.164 44.351 1.00 31.68 ? 294 GLN A NE2 1 ATOM 2337 N N . VAL A 1 294 ? 1.609 18.314 38.530 1.00 20.56 ? 295 VAL A N 1 ATOM 2338 C CA . VAL A 1 294 ? 2.455 17.279 38.033 1.00 18.71 ? 295 VAL A CA 1 ATOM 2339 C C . VAL A 1 294 ? 2.370 17.379 36.528 1.00 18.11 ? 295 VAL A C 1 ATOM 2340 O O . VAL A 1 294 ? 1.323 17.662 36.016 1.00 18.25 ? 295 VAL A O 1 ATOM 2341 C CB . VAL A 1 294 ? 2.007 15.884 38.530 1.00 18.77 ? 295 VAL A CB 1 ATOM 2342 C CG1 . VAL A 1 294 ? 2.503 15.623 39.922 1.00 16.16 ? 295 VAL A CG1 1 ATOM 2343 C CG2 . VAL A 1 294 ? 0.503 15.755 38.531 1.00 20.18 ? 295 VAL A CG2 1 ATOM 2344 N N . PRO A 1 295 ? 3.483 17.165 35.812 1.00 17.41 ? 296 PRO A N 1 ATOM 2345 C CA . PRO A 1 295 ? 3.555 17.211 34.361 1.00 16.58 ? 296 PRO A CA 1 ATOM 2346 C C . PRO A 1 295 ? 3.326 15.934 33.617 1.00 17.62 ? 296 PRO A C 1 ATOM 2347 O O . PRO A 1 295 ? 3.376 14.859 34.191 1.00 17.95 ? 296 PRO A O 1 ATOM 2348 C CB . PRO A 1 295 ? 4.950 17.597 34.153 1.00 16.07 ? 296 PRO A CB 1 ATOM 2349 C CG . PRO A 1 295 ? 5.620 16.752 35.121 1.00 15.45 ? 296 PRO A CG 1 ATOM 2350 C CD . PRO A 1 295 ? 4.810 16.934 36.375 1.00 16.88 ? 296 PRO A CD 1 ATOM 2351 N N . TYR A 1 296 ? 3.033 16.089 32.316 1.00 19.32 ? 297 TYR A N 1 ATOM 2352 C CA . TYR A 1 296 ? 2.838 14.972 31.387 1.00 20.43 ? 297 TYR A CA 1 ATOM 2353 C C . TYR A 1 296 ? 3.277 15.395 29.993 1.00 19.86 ? 297 TYR A C 1 ATOM 2354 O O . TYR A 1 296 ? 3.332 16.555 29.700 1.00 20.03 ? 297 TYR A O 1 ATOM 2355 C CB . TYR A 1 296 ? 1.408 14.437 31.411 1.00 20.07 ? 297 TYR A CB 1 ATOM 2356 C CG . TYR A 1 296 ? 0.382 15.261 30.744 1.00 26.32 ? 297 TYR A CG 1 ATOM 2357 C CD1 . TYR A 1 296 ? -0.407 16.154 31.468 1.00 33.47 ? 297 TYR A CD1 1 ATOM 2358 C CD2 . TYR A 1 296 ? 0.154 15.145 29.375 1.00 32.39 ? 297 TYR A CD2 1 ATOM 2359 C CE1 . TYR A 1 296 ? -1.406 16.917 30.842 1.00 37.06 ? 297 TYR A CE1 1 ATOM 2360 C CE2 . TYR A 1 296 ? -0.836 15.897 28.734 1.00 35.56 ? 297 TYR A CE2 1 ATOM 2361 C CZ . TYR A 1 296 ? -1.615 16.772 29.477 1.00 37.75 ? 297 TYR A CZ 1 ATOM 2362 O OH . TYR A 1 296 ? -2.591 17.514 28.857 1.00 39.30 ? 297 TYR A OH 1 ATOM 2363 N N . ALA A 1 297 ? 3.672 14.452 29.158 1.00 21.34 ? 298 ALA A N 1 ATOM 2364 C CA . ALA A 1 297 ? 4.121 14.776 27.805 1.00 21.88 ? 298 ALA A CA 1 ATOM 2365 C C . ALA A 1 297 ? 3.570 13.803 26.771 1.00 23.40 ? 298 ALA A C 1 ATOM 2366 O O . ALA A 1 297 ? 3.245 12.646 27.079 1.00 23.87 ? 298 ALA A O 1 ATOM 2367 C CB . ALA A 1 297 ? 5.638 14.786 27.731 1.00 21.60 ? 298 ALA A CB 1 ATOM 2368 N N . THR A 1 298 ? 3.463 14.295 25.540 1.00 24.69 ? 299 THR A N 1 ATOM 2369 C CA . THR A 1 298 ? 2.992 13.493 24.422 1.00 25.41 ? 299 THR A CA 1 ATOM 2370 C C . THR A 1 298 ? 3.867 13.735 23.241 1.00 25.97 ? 299 THR A C 1 ATOM 2371 O O . THR A 1 298 ? 4.392 14.839 23.047 1.00 28.45 ? 299 THR A O 1 ATOM 2372 C CB . THR A 1 298 ? 1.576 13.824 24.032 1.00 25.04 ? 299 THR A CB 1 ATOM 2373 O OG1 . THR A 1 298 ? 1.108 14.909 24.828 1.00 25.90 ? 299 THR A OG1 1 ATOM 2374 C CG2 . THR A 1 298 ? 0.677 12.616 24.302 1.00 26.27 ? 299 THR A CG2 1 ATOM 2375 N N . LYS A 1 299 ? 4.022 12.697 22.444 1.00 24.73 ? 300 LYS A N 1 ATOM 2376 C CA . LYS A 1 299 ? 4.847 12.743 21.258 1.00 23.55 ? 300 LYS A CA 1 ATOM 2377 C C . LYS A 1 299 ? 4.370 11.540 20.446 1.00 23.07 ? 300 LYS A C 1 ATOM 2378 O O . LYS A 1 299 ? 4.464 10.390 20.911 1.00 23.84 ? 300 LYS A O 1 ATOM 2379 C CB . LYS A 1 299 ? 6.317 12.587 21.627 1.00 22.93 ? 300 LYS A CB 1 ATOM 2380 C CG . LYS A 1 299 ? 7.253 12.664 20.470 1.00 23.12 ? 300 LYS A CG 1 ATOM 2381 C CD . LYS A 1 299 ? 8.471 11.759 20.694 1.00 26.40 ? 300 LYS A CD 1 ATOM 2382 C CE . LYS A 1 299 ? 9.681 12.523 21.172 1.00 26.07 ? 300 LYS A CE 1 ATOM 2383 N NZ . LYS A 1 299 ? 10.870 11.592 21.243 1.00 22.49 ? 300 LYS A NZ 1 ATOM 2384 N N . GLY A 1 300 ? 3.818 11.786 19.261 1.00 20.33 ? 301 GLY A N 1 ATOM 2385 C CA . GLY A 1 300 ? 3.306 10.671 18.492 1.00 17.81 ? 301 GLY A CA 1 ATOM 2386 C C . GLY A 1 300 ? 2.058 10.145 19.161 1.00 14.14 ? 301 GLY A C 1 ATOM 2387 O O . GLY A 1 300 ? 1.252 10.921 19.535 1.00 15.71 ? 301 GLY A O 1 ATOM 2388 N N . ASN A 1 301 ? 1.920 8.860 19.316 1.00 12.23 ? 302 ASN A N 1 ATOM 2389 C CA . ASN A 1 301 ? 0.767 8.277 19.959 1.00 12.88 ? 302 ASN A CA 1 ATOM 2390 C C . ASN A 1 301 ? 1.135 7.829 21.344 1.00 15.01 ? 302 ASN A C 1 ATOM 2391 O O . ASN A 1 301 ? 0.514 6.939 21.879 1.00 16.16 ? 302 ASN A O 1 ATOM 2392 C CB . ASN A 1 301 ? 0.256 7.052 19.204 1.00 13.28 ? 302 ASN A CB 1 ATOM 2393 C CG . ASN A 1 301 ? 1.256 5.900 19.192 1.00 12.97 ? 302 ASN A CG 1 ATOM 2394 O OD1 . ASN A 1 301 ? 2.415 6.068 19.538 1.00 15.45 ? 302 ASN A OD1 1 ATOM 2395 N ND2 . ASN A 1 301 ? 0.821 4.750 18.767 1.00 13.93 ? 302 ASN A ND2 1 ATOM 2396 N N . GLN A 1 302 ? 2.168 8.440 21.920 1.00 16.81 ? 303 GLN A N 1 ATOM 2397 C CA . GLN A 1 302 ? 2.611 8.118 23.283 1.00 17.99 ? 303 GLN A CA 1 ATOM 2398 C C . GLN A 1 302 ? 2.338 9.265 24.264 1.00 18.04 ? 303 GLN A C 1 ATOM 2399 O O . GLN A 1 302 ? 2.677 10.398 24.007 1.00 18.37 ? 303 GLN A O 1 ATOM 2400 C CB . GLN A 1 302 ? 4.104 7.792 23.286 1.00 19.58 ? 303 GLN A CB 1 ATOM 2401 C CG . GLN A 1 302 ? 4.495 6.597 22.415 1.00 19.80 ? 303 GLN A CG 1 ATOM 2402 C CD . GLN A 1 302 ? 4.070 5.288 23.023 1.00 22.62 ? 303 GLN A CD 1 ATOM 2403 O OE1 . GLN A 1 302 ? 3.016 4.778 22.753 1.00 23.55 ? 303 GLN A OE1 1 ATOM 2404 N NE2 . GLN A 1 302 ? 4.901 4.756 23.894 1.00 29.02 ? 303 GLN A NE2 1 ATOM 2405 N N . TRP A 1 303 ? 1.716 8.953 25.391 1.00 18.91 ? 304 TRP A N 1 ATOM 2406 C CA . TRP A 1 303 ? 1.387 9.930 26.428 1.00 18.20 ? 304 TRP A CA 1 ATOM 2407 C C . TRP A 1 303 ? 2.153 9.462 27.675 1.00 17.30 ? 304 TRP A C 1 ATOM 2408 O O . TRP A 1 303 ? 2.002 8.335 28.117 1.00 17.23 ? 304 TRP A O 1 ATOM 2409 C CB . TRP A 1 303 ? -0.121 9.870 26.699 1.00 18.39 ? 304 TRP A CB 1 ATOM 2410 C CG . TRP A 1 303 ? -0.648 10.940 27.531 1.00 19.50 ? 304 TRP A CG 1 ATOM 2411 C CD1 . TRP A 1 303 ? -1.120 12.132 27.102 1.00 22.15 ? 304 TRP A CD1 1 ATOM 2412 C CD2 . TRP A 1 303 ? -0.789 10.938 28.943 1.00 18.59 ? 304 TRP A CD2 1 ATOM 2413 N NE1 . TRP A 1 303 ? -1.557 12.888 28.167 1.00 21.28 ? 304 TRP A NE1 1 ATOM 2414 C CE2 . TRP A 1 303 ? -1.363 12.169 29.315 1.00 19.37 ? 304 TRP A CE2 1 ATOM 2415 C CE3 . TRP A 1 303 ? -0.470 10.032 29.935 1.00 18.39 ? 304 TRP A CE3 1 ATOM 2416 C CZ2 . TRP A 1 303 ? -1.608 12.514 30.638 1.00 17.10 ? 304 TRP A CZ2 1 ATOM 2417 C CZ3 . TRP A 1 303 ? -0.768 10.365 31.254 1.00 18.40 ? 304 TRP A CZ3 1 ATOM 2418 C CH2 . TRP A 1 303 ? -1.342 11.587 31.582 1.00 16.24 ? 304 TRP A CH2 1 ATOM 2419 N N . VAL A 1 304 ? 2.968 10.334 28.227 1.00 16.52 ? 305 VAL A N 1 ATOM 2420 C CA . VAL A 1 304 ? 3.737 9.990 29.401 1.00 17.07 ? 305 VAL A CA 1 ATOM 2421 C C . VAL A 1 304 ? 3.421 10.866 30.608 1.00 15.90 ? 305 VAL A C 1 ATOM 2422 O O . VAL A 1 304 ? 3.472 12.074 30.520 1.00 14.95 ? 305 VAL A O 1 ATOM 2423 C CB . VAL A 1 304 ? 5.235 10.103 29.121 1.00 17.57 ? 305 VAL A CB 1 ATOM 2424 C CG1 . VAL A 1 304 ? 6.036 9.877 30.398 1.00 18.61 ? 305 VAL A CG1 1 ATOM 2425 C CG2 . VAL A 1 304 ? 5.652 9.087 28.120 1.00 20.29 ? 305 VAL A CG2 1 ATOM 2426 N N . ALA A 1 305 ? 3.105 10.230 31.725 1.00 14.89 ? 306 ALA A N 1 ATOM 2427 C CA . ALA A 1 305 ? 2.842 10.954 32.961 1.00 15.71 ? 306 ALA A CA 1 ATOM 2428 C C . ALA A 1 305 ? 4.125 10.832 33.771 1.00 15.35 ? 306 ALA A C 1 ATOM 2429 O O . ALA A 1 305 ? 4.584 9.717 33.938 1.00 17.79 ? 306 ALA A O 1 ATOM 2430 C CB . ALA A 1 305 ? 1.692 10.320 33.730 1.00 15.07 ? 306 ALA A CB 1 ATOM 2431 N N . TYR A 1 306 ? 4.703 11.927 34.269 1.00 13.35 ? 307 TYR A N 1 ATOM 2432 C CA . TYR A 1 306 ? 5.935 11.819 35.021 1.00 13.32 ? 307 TYR A CA 1 ATOM 2433 C C . TYR A 1 306 ? 6.158 12.888 36.076 1.00 15.54 ? 307 TYR A C 1 ATOM 2434 O O . TYR A 1 306 ? 5.280 13.704 36.368 1.00 16.81 ? 307 TYR A O 1 ATOM 2435 C CB . TYR A 1 306 ? 7.097 11.850 34.073 1.00 13.06 ? 307 TYR A CB 1 ATOM 2436 C CG . TYR A 1 306 ? 7.255 13.175 33.324 1.00 14.42 ? 307 TYR A CG 1 ATOM 2437 C CD1 . TYR A 1 306 ? 6.362 13.552 32.325 1.00 9.87 ? 307 TYR A CD1 1 ATOM 2438 C CD2 . TYR A 1 306 ? 8.307 14.047 33.620 1.00 14.97 ? 307 TYR A CD2 1 ATOM 2439 C CE1 . TYR A 1 306 ? 6.504 14.756 31.688 1.00 11.49 ? 307 TYR A CE1 1 ATOM 2440 C CE2 . TYR A 1 306 ? 8.440 15.248 32.966 1.00 16.56 ? 307 TYR A CE2 1 ATOM 2441 C CZ . TYR A 1 306 ? 7.538 15.609 32.022 1.00 14.56 ? 307 TYR A CZ 1 ATOM 2442 O OH . TYR A 1 306 ? 7.699 16.831 31.409 1.00 16.60 ? 307 TYR A OH 1 ATOM 2443 N N . ASP A 1 307 ? 7.349 12.871 36.643 1.00 17.12 ? 308 ASP A N 1 ATOM 2444 C CA . ASP A 1 307 ? 7.767 13.822 37.666 1.00 17.98 ? 308 ASP A CA 1 ATOM 2445 C C . ASP A 1 307 ? 9.096 14.449 37.312 1.00 19.59 ? 308 ASP A C 1 ATOM 2446 O O . ASP A 1 307 ? 10.109 13.769 37.057 1.00 19.14 ? 308 ASP A O 1 ATOM 2447 C CB . ASP A 1 307 ? 7.938 13.166 39.016 1.00 17.95 ? 308 ASP A CB 1 ATOM 2448 C CG . ASP A 1 307 ? 6.674 13.125 39.798 1.00 17.17 ? 308 ASP A CG 1 ATOM 2449 O OD1 . ASP A 1 307 ? 5.995 12.069 39.750 1.00 18.85 ? 308 ASP A OD1 1 ATOM 2450 O OD2 . ASP A 1 307 ? 6.342 14.125 40.471 1.00 16.94 ? 308 ASP A OD2 1 ATOM 2451 N N . ASP A 1 308 ? 9.080 15.770 37.316 1.00 21.48 ? 309 ASP A N 1 ATOM 2452 C CA . ASP A 1 308 ? 10.245 16.528 36.988 1.00 22.74 ? 309 ASP A CA 1 ATOM 2453 C C . ASP A 1 308 ? 10.782 17.153 38.248 1.00 23.28 ? 309 ASP A C 1 ATOM 2454 O O . ASP A 1 308 ? 10.203 16.991 39.311 1.00 22.13 ? 309 ASP A O 1 ATOM 2455 C CB . ASP A 1 308 ? 9.904 17.590 35.931 1.00 23.93 ? 309 ASP A CB 1 ATOM 2456 C CG . ASP A 1 308 ? 8.882 18.569 36.389 1.00 25.05 ? 309 ASP A CG 1 ATOM 2457 O OD1 . ASP A 1 308 ? 8.031 18.191 37.195 1.00 28.19 ? 309 ASP A OD1 1 ATOM 2458 O OD2 . ASP A 1 308 ? 8.875 19.743 35.959 1.00 30.51 ? 309 ASP A OD2 1 ATOM 2459 N N . GLN A 1 309 ? 11.892 17.878 38.093 1.00 25.01 ? 310 GLN A N 1 ATOM 2460 C CA . GLN A 1 309 ? 12.586 18.549 39.175 1.00 26.50 ? 310 GLN A CA 1 ATOM 2461 C C . GLN A 1 309 ? 11.680 19.401 40.028 1.00 26.30 ? 310 GLN A C 1 ATOM 2462 O O . GLN A 1 309 ? 11.827 19.511 41.238 1.00 27.00 ? 310 GLN A O 1 ATOM 2463 C CB . GLN A 1 309 ? 13.707 19.418 38.631 1.00 27.62 ? 310 GLN A CB 1 ATOM 2464 C CG . GLN A 1 309 ? 15.091 18.791 38.652 1.00 33.81 ? 310 GLN A CG 1 ATOM 2465 C CD . GLN A 1 309 ? 16.163 19.838 38.649 1.00 39.55 ? 310 GLN A CD 1 ATOM 2466 O OE1 . GLN A 1 309 ? 16.116 20.743 39.471 1.00 44.12 ? 310 GLN A OE1 1 ATOM 2467 N NE2 . GLN A 1 309 ? 17.118 19.739 37.723 1.00 42.75 ? 310 GLN A NE2 1 ATOM 2468 N N . GLU A 1 310 ? 10.693 19.988 39.434 1.00 27.02 ? 311 GLU A N 1 ATOM 2469 C CA . GLU A 1 310 ? 9.879 20.847 40.237 1.00 28.86 ? 311 GLU A CA 1 ATOM 2470 C C . GLU A 1 310 ? 8.581 20.278 40.793 1.00 26.19 ? 311 GLU A C 1 ATOM 2471 O O . GLU A 1 310 ? 8.083 20.745 41.796 1.00 27.05 ? 311 GLU A O 1 ATOM 2472 C CB . GLU A 1 310 ? 9.667 22.141 39.478 1.00 31.97 ? 311 GLU A CB 1 ATOM 2473 C CG . GLU A 1 310 ? 8.300 22.416 38.991 1.00 40.57 ? 311 GLU A CG 1 ATOM 2474 C CD . GLU A 1 310 ? 8.085 23.918 38.835 1.00 49.02 ? 311 GLU A CD 1 ATOM 2475 O OE1 . GLU A 1 310 ? 8.454 24.653 39.805 1.00 51.68 ? 311 GLU A OE1 1 ATOM 2476 O OE2 . GLU A 1 310 ? 7.554 24.342 37.756 1.00 53.19 ? 311 GLU A OE2 1 ATOM 2477 N N . SER A 1 311 ? 8.043 19.257 40.190 1.00 22.98 ? 312 SER A N 1 ATOM 2478 C CA . SER A 1 311 ? 6.873 18.681 40.742 1.00 21.49 ? 312 SER A CA 1 ATOM 2479 C C . SER A 1 311 ? 7.406 17.951 41.954 1.00 20.15 ? 312 SER A C 1 ATOM 2480 O O . SER A 1 311 ? 6.746 17.733 42.939 1.00 21.81 ? 312 SER A O 1 ATOM 2481 C CB . SER A 1 311 ? 6.232 17.701 39.783 1.00 21.45 ? 312 SER A CB 1 ATOM 2482 O OG . SER A 1 311 ? 7.019 16.555 39.681 1.00 20.90 ? 312 SER A OG 1 ATOM 2483 N N . VAL A 1 312 ? 8.648 17.575 41.870 1.00 19.07 ? 313 VAL A N 1 ATOM 2484 C CA . VAL A 1 312 ? 9.323 16.854 42.952 1.00 16.91 ? 313 VAL A CA 1 ATOM 2485 C C . VAL A 1 312 ? 9.726 17.812 44.075 1.00 16.83 ? 313 VAL A C 1 ATOM 2486 O O . VAL A 1 312 ? 9.608 17.515 45.252 1.00 15.60 ? 313 VAL A O 1 ATOM 2487 C CB . VAL A 1 312 ? 10.536 16.146 42.378 1.00 15.10 ? 313 VAL A CB 1 ATOM 2488 C CG1 . VAL A 1 312 ? 11.701 16.217 43.279 1.00 13.94 ? 313 VAL A CG1 1 ATOM 2489 C CG2 . VAL A 1 312 ? 10.171 14.696 42.095 1.00 12.83 ? 313 VAL A CG2 1 ATOM 2490 N N . LYS A 1 313 ? 10.218 18.971 43.692 1.00 17.35 ? 314 LYS A N 1 ATOM 2491 C CA . LYS A 1 313 ? 10.594 19.989 44.681 1.00 18.07 ? 314 LYS A CA 1 ATOM 2492 C C . LYS A 1 313 ? 9.366 20.395 45.477 1.00 15.24 ? 314 LYS A C 1 ATOM 2493 O O . LYS A 1 313 ? 9.450 20.910 46.547 1.00 12.14 ? 314 LYS A O 1 ATOM 2494 C CB . LYS A 1 313 ? 11.130 21.231 43.963 1.00 19.49 ? 314 LYS A CB 1 ATOM 2495 C CG . LYS A 1 313 ? 12.610 21.298 43.731 1.00 26.90 ? 314 LYS A CG 1 ATOM 2496 C CD . LYS A 1 313 ? 12.990 22.754 43.431 1.00 35.78 ? 314 LYS A CD 1 ATOM 2497 C CE . LYS A 1 313 ? 14.488 22.995 43.342 1.00 39.94 ? 314 LYS A CE 1 ATOM 2498 N NZ . LYS A 1 313 ? 15.090 22.185 42.224 1.00 44.91 ? 314 LYS A NZ 1 ATOM 2499 N N . ASN A 1 314 ? 8.214 20.172 44.873 1.00 14.61 ? 315 ASN A N 1 ATOM 2500 C CA . ASN A 1 314 ? 6.933 20.586 45.430 1.00 14.68 ? 315 ASN A CA 1 ATOM 2501 C C . ASN A 1 314 ? 6.314 19.577 46.436 1.00 14.02 ? 315 ASN A C 1 ATOM 2502 O O . ASN A 1 314 ? 5.736 19.929 47.465 1.00 9.43 ? 315 ASN A O 1 ATOM 2503 C CB . ASN A 1 314 ? 5.989 20.786 44.257 1.00 16.04 ? 315 ASN A CB 1 ATOM 2504 C CG . ASN A 1 314 ? 4.979 21.750 44.536 1.00 19.81 ? 315 ASN A CG 1 ATOM 2505 O OD1 . ASN A 1 314 ? 3.802 21.412 44.632 1.00 23.68 ? 315 ASN A OD1 1 ATOM 2506 N ND2 . ASN A 1 314 ? 5.414 23.013 44.702 1.00 27.65 ? 315 ASN A ND2 1 ATOM 2507 N N . LYS A 1 315 ? 6.436 18.293 46.067 1.00 14.01 ? 316 LYS A N 1 ATOM 2508 C CA . LYS A 1 315 ? 5.971 17.200 46.860 1.00 11.48 ? 316 LYS A CA 1 ATOM 2509 C C . LYS A 1 315 ? 6.802 17.305 48.107 1.00 11.96 ? 316 LYS A C 1 ATOM 2510 O O . LYS A 1 315 ? 6.268 17.184 49.188 1.00 13.52 ? 316 LYS A O 1 ATOM 2511 C CB . LYS A 1 315 ? 6.194 15.875 46.115 1.00 9.90 ? 316 LYS A CB 1 ATOM 2512 C CG . LYS A 1 315 ? 5.085 15.562 45.133 1.00 10.36 ? 316 LYS A CG 1 ATOM 2513 C CD . LYS A 1 315 ? 5.439 14.526 44.067 1.00 8.05 ? 316 LYS A CD 1 ATOM 2514 C CE . LYS A 1 315 ? 4.223 14.291 43.188 1.00 8.84 ? 316 LYS A CE 1 ATOM 2515 N NZ . LYS A 1 315 ? 4.455 13.348 42.119 1.00 12.70 ? 316 LYS A NZ 1 ATOM 2516 N N . ALA A 1 316 ? 8.109 17.581 47.944 1.00 11.43 ? 317 ALA A N 1 ATOM 2517 C CA . ALA A 1 316 ? 9.052 17.685 49.055 1.00 11.30 ? 317 ALA A CA 1 ATOM 2518 C C . ALA A 1 316 ? 8.655 18.780 49.989 1.00 13.08 ? 317 ALA A C 1 ATOM 2519 O O . ALA A 1 316 ? 8.705 18.670 51.216 1.00 12.78 ? 317 ALA A O 1 ATOM 2520 C CB . ALA A 1 316 ? 10.399 17.978 48.547 1.00 11.56 ? 317 ALA A CB 1 ATOM 2521 N N . ARG A 1 317 ? 8.226 19.864 49.386 1.00 15.99 ? 318 ARG A N 1 ATOM 2522 C CA . ARG A 1 317 ? 7.812 21.028 50.146 1.00 16.81 ? 318 ARG A CA 1 ATOM 2523 C C . ARG A 1 317 ? 6.530 20.734 50.931 1.00 15.74 ? 318 ARG A C 1 ATOM 2524 O O . ARG A 1 317 ? 6.390 21.204 52.006 1.00 15.77 ? 318 ARG A O 1 ATOM 2525 C CB . ARG A 1 317 ? 7.616 22.168 49.188 1.00 18.42 ? 318 ARG A CB 1 ATOM 2526 C CG . ARG A 1 317 ? 7.755 23.520 49.792 1.00 26.06 ? 318 ARG A CG 1 ATOM 2527 C CD . ARG A 1 317 ? 7.785 24.649 48.709 1.00 33.51 ? 318 ARG A CD 1 ATOM 2528 N NE . ARG A 1 317 ? 9.050 24.714 47.989 1.00 36.68 ? 318 ARG A NE 1 ATOM 2529 C CZ . ARG A 1 317 ? 9.164 24.642 46.661 1.00 40.79 ? 318 ARG A CZ 1 ATOM 2530 N NH1 . ARG A 1 317 ? 8.079 24.456 45.879 1.00 39.57 ? 318 ARG A NH1 1 ATOM 2531 N NH2 . ARG A 1 317 ? 10.380 24.758 46.107 1.00 40.65 ? 318 ARG A NH2 1 ATOM 2532 N N . TYR A 1 318 ? 5.613 19.943 50.382 1.00 15.45 ? 319 TYR A N 1 ATOM 2533 C CA . TYR A 1 318 ? 4.364 19.577 51.055 1.00 15.60 ? 319 TYR A CA 1 ATOM 2534 C C . TYR A 1 318 ? 4.687 18.830 52.315 1.00 15.20 ? 319 TYR A C 1 ATOM 2535 O O . TYR A 1 318 ? 4.267 19.179 53.402 1.00 17.69 ? 319 TYR A O 1 ATOM 2536 C CB . TYR A 1 318 ? 3.559 18.657 50.130 1.00 16.39 ? 319 TYR A CB 1 ATOM 2537 C CG . TYR A 1 318 ? 2.370 17.956 50.716 1.00 14.79 ? 319 TYR A CG 1 ATOM 2538 C CD1 . TYR A 1 318 ? 1.128 18.580 50.822 1.00 17.41 ? 319 TYR A CD1 1 ATOM 2539 C CD2 . TYR A 1 318 ? 2.446 16.654 51.071 1.00 17.02 ? 319 TYR A CD2 1 ATOM 2540 C CE1 . TYR A 1 318 ? -0.016 17.906 51.322 1.00 17.65 ? 319 TYR A CE1 1 ATOM 2541 C CE2 . TYR A 1 318 ? 1.284 15.963 51.590 1.00 21.32 ? 319 TYR A CE2 1 ATOM 2542 C CZ . TYR A 1 318 ? 0.069 16.610 51.697 1.00 16.37 ? 319 TYR A CZ 1 ATOM 2543 O OH . TYR A 1 318 ? -1.033 15.961 52.157 1.00 13.90 ? 319 TYR A OH 1 ATOM 2544 N N . LEU A 1 319 ? 5.418 17.761 52.109 1.00 14.21 ? 320 LEU A N 1 ATOM 2545 C CA . LEU A 1 319 ? 5.886 16.825 53.100 1.00 11.09 ? 320 LEU A CA 1 ATOM 2546 C C . LEU A 1 319 ? 6.343 17.584 54.336 1.00 11.64 ? 320 LEU A C 1 ATOM 2547 O O . LEU A 1 319 ? 6.011 17.224 55.462 1.00 10.73 ? 320 LEU A O 1 ATOM 2548 C CB . LEU A 1 319 ? 6.918 15.919 52.365 1.00 9.76 ? 320 LEU A CB 1 ATOM 2549 C CG . LEU A 1 319 ? 8.116 15.237 53.017 1.00 8.30 ? 320 LEU A CG 1 ATOM 2550 C CD1 . LEU A 1 319 ? 8.987 14.609 51.971 1.00 9.05 ? 320 LEU A CD1 1 ATOM 2551 C CD2 . LEU A 1 319 ? 8.904 16.200 53.867 1.00 8.19 ? 320 LEU A CD2 1 ATOM 2552 N N . LYS A 1 320 ? 7.114 18.648 54.130 1.00 11.97 ? 321 LYS A N 1 ATOM 2553 C CA . LYS A 1 320 ? 7.646 19.460 55.251 1.00 12.24 ? 321 LYS A CA 1 ATOM 2554 C C . LYS A 1 320 ? 6.590 20.218 55.974 1.00 13.13 ? 321 LYS A C 1 ATOM 2555 O O . LYS A 1 320 ? 6.571 20.250 57.192 1.00 15.94 ? 321 LYS A O 1 ATOM 2556 C CB . LYS A 1 320 ? 8.726 20.477 54.782 1.00 12.82 ? 321 LYS A CB 1 ATOM 2557 C CG . LYS A 1 320 ? 10.076 19.921 54.528 1.00 15.81 ? 321 LYS A CG 1 ATOM 2558 C CD . LYS A 1 320 ? 10.911 20.898 53.734 1.00 21.24 ? 321 LYS A CD 1 ATOM 2559 C CE . LYS A 1 320 ? 11.746 21.840 54.607 1.00 24.81 ? 321 LYS A CE 1 ATOM 2560 N NZ . LYS A 1 320 ? 12.382 22.932 53.794 1.00 29.67 ? 321 LYS A NZ 1 ATOM 2561 N N . ASN A 1 321 ? 5.727 20.879 55.226 1.00 14.16 ? 322 ASN A N 1 ATOM 2562 C CA . ASN A 1 321 ? 4.624 21.659 55.815 1.00 14.44 ? 322 ASN A CA 1 ATOM 2563 C C . ASN A 1 321 ? 3.673 20.838 56.626 1.00 15.29 ? 322 ASN A C 1 ATOM 2564 O O . ASN A 1 321 ? 3.069 21.377 57.553 1.00 15.78 ? 322 ASN A O 1 ATOM 2565 C CB . ASN A 1 321 ? 3.832 22.395 54.759 1.00 14.68 ? 322 ASN A CB 1 ATOM 2566 C CG . ASN A 1 321 ? 4.619 23.492 54.129 1.00 16.15 ? 322 ASN A CG 1 ATOM 2567 O OD1 . ASN A 1 321 ? 5.472 24.088 54.754 1.00 14.04 ? 322 ASN A OD1 1 ATOM 2568 N ND2 . ASN A 1 321 ? 4.292 23.800 52.888 1.00 24.50 ? 322 ASN A ND2 1 ATOM 2569 N N . ARG A 1 322 ? 3.524 19.550 56.280 1.00 15.75 ? 323 ARG A N 1 ATOM 2570 C CA . ARG A 1 322 ? 2.656 18.642 57.052 1.00 16.02 ? 323 ARG A CA 1 ATOM 2571 C C . ARG A 1 322 ? 3.497 17.944 58.100 1.00 15.70 ? 323 ARG A C 1 ATOM 2572 O O . ARG A 1 322 ? 3.042 17.078 58.796 1.00 17.09 ? 323 ARG A O 1 ATOM 2573 C CB . ARG A 1 322 ? 1.907 17.651 56.147 1.00 14.25 ? 323 ARG A CB 1 ATOM 2574 C CG . ARG A 1 322 ? 0.554 18.244 55.655 1.00 14.87 ? 323 ARG A CG 1 ATOM 2575 C CD . ARG A 1 322 ? -0.237 17.339 54.706 1.00 19.54 ? 323 ARG A CD 1 ATOM 2576 N NE . ARG A 1 322 ? -1.590 16.900 55.140 1.00 17.04 ? 323 ARG A NE 1 ATOM 2577 C CZ . ARG A 1 322 ? -2.015 16.905 56.380 1.00 15.04 ? 323 ARG A CZ 1 ATOM 2578 N NH1 . ARG A 1 322 ? -1.322 17.369 57.387 1.00 12.32 ? 323 ARG A NH1 1 ATOM 2579 N NH2 . ARG A 1 322 ? -3.193 16.398 56.620 1.00 24.42 ? 323 ARG A NH2 1 ATOM 2580 N N . GLN A 1 323 ? 4.738 18.360 58.200 1.00 15.59 ? 324 GLN A N 1 ATOM 2581 C CA . GLN A 1 323 ? 5.695 17.837 59.172 1.00 16.14 ? 324 GLN A CA 1 ATOM 2582 C C . GLN A 1 323 ? 5.975 16.362 59.217 1.00 13.41 ? 324 GLN A C 1 ATOM 2583 O O . GLN A 1 323 ? 6.061 15.815 60.275 1.00 13.25 ? 324 GLN A O 1 ATOM 2584 C CB . GLN A 1 323 ? 5.300 18.303 60.552 1.00 18.49 ? 324 GLN A CB 1 ATOM 2585 C CG . GLN A 1 323 ? 5.154 19.819 60.602 1.00 26.12 ? 324 GLN A CG 1 ATOM 2586 C CD . GLN A 1 323 ? 5.179 20.340 62.038 1.00 34.74 ? 324 GLN A CD 1 ATOM 2587 O OE1 . GLN A 1 323 ? 4.173 20.164 62.794 1.00 35.73 ? 324 GLN A OE1 1 ATOM 2588 N NE2 . GLN A 1 323 ? 6.326 20.973 62.439 1.00 35.02 ? 324 GLN A NE2 1 ATOM 2589 N N . LEU A 1 324 ? 6.160 15.726 58.082 1.00 11.80 ? 325 LEU A N 1 ATOM 2590 C CA . LEU A 1 324 ? 6.432 14.307 58.067 1.00 10.93 ? 325 LEU A CA 1 ATOM 2591 C C . LEU A 1 324 ? 7.906 14.049 58.308 1.00 12.23 ? 325 LEU A C 1 ATOM 2592 O O . LEU A 1 324 ? 8.706 14.953 58.314 1.00 12.39 ? 325 LEU A O 1 ATOM 2593 C CB . LEU A 1 324 ? 6.029 13.694 56.745 1.00 9.50 ? 325 LEU A CB 1 ATOM 2594 C CG . LEU A 1 324 ? 4.607 14.036 56.335 1.00 6.56 ? 325 LEU A CG 1 ATOM 2595 C CD1 . LEU A 1 324 ? 4.204 13.218 55.101 1.00 7.48 ? 325 LEU A CD1 1 ATOM 2596 C CD2 . LEU A 1 324 ? 3.670 13.773 57.447 1.00 5.68 ? 325 LEU A CD2 1 ATOM 2597 N N . ALA A 1 325 ? 8.249 12.786 58.502 1.00 13.09 ? 326 ALA A N 1 ATOM 2598 C CA . ALA A 1 325 ? 9.610 12.364 58.793 1.00 12.18 ? 326 ALA A CA 1 ATOM 2599 C C . ALA A 1 325 ? 10.594 12.571 57.663 1.00 10.64 ? 326 ALA A C 1 ATOM 2600 O O . ALA A 1 325 ? 11.740 12.863 57.869 1.00 10.66 ? 326 ALA A O 1 ATOM 2601 C CB . ALA A 1 325 ? 9.584 10.922 59.208 1.00 12.80 ? 326 ALA A CB 1 ATOM 2602 N N . GLY A 1 326 ? 10.146 12.420 56.451 1.00 10.97 ? 327 GLY A N 1 ATOM 2603 C CA . GLY A 1 326 ? 11.042 12.606 55.305 1.00 10.46 ? 327 GLY A CA 1 ATOM 2604 C C . GLY A 1 326 ? 10.397 12.101 54.001 1.00 10.18 ? 327 GLY A C 1 ATOM 2605 O O . GLY A 1 326 ? 9.197 11.888 53.863 1.00 9.15 ? 327 GLY A O 1 ATOM 2606 N N . ALA A 1 327 ? 11.239 11.900 53.015 1.00 8.95 ? 328 ALA A N 1 ATOM 2607 C CA . ALA A 1 327 ? 10.747 11.450 51.753 1.00 7.98 ? 328 ALA A CA 1 ATOM 2608 C C . ALA A 1 327 ? 11.436 10.154 51.343 1.00 8.80 ? 328 ALA A C 1 ATOM 2609 O O . ALA A 1 327 ? 12.549 9.890 51.749 1.00 9.83 ? 328 ALA A O 1 ATOM 2610 C CB . ALA A 1 327 ? 10.986 12.506 50.753 1.00 5.68 ? 328 ALA A CB 1 ATOM 2611 N N . MET A 1 328 ? 10.726 9.336 50.574 1.00 8.49 ? 329 MET A N 1 ATOM 2612 C CA . MET A 1 328 ? 11.207 8.098 50.052 1.00 7.27 ? 329 MET A CA 1 ATOM 2613 C C . MET A 1 328 ? 11.237 8.229 48.545 1.00 8.68 ? 329 MET A C 1 ATOM 2614 O O . MET A 1 328 ? 10.291 8.694 47.935 1.00 10.49 ? 329 MET A O 1 ATOM 2615 C CB . MET A 1 328 ? 10.260 6.954 50.435 1.00 6.87 ? 329 MET A CB 1 ATOM 2616 C CG . MET A 1 328 ? 10.670 5.595 49.765 1.00 8.68 ? 329 MET A CG 1 ATOM 2617 S SD . MET A 1 328 ? 9.752 5.310 48.214 1.00 5.87 ? 329 MET A SD 1 ATOM 2618 C CE . MET A 1 328 ? 8.402 4.387 48.787 1.00 4.81 ? 329 MET A CE 1 ATOM 2619 N N . VAL A 1 329 ? 12.326 7.801 47.937 1.00 9.66 ? 330 VAL A N 1 ATOM 2620 C CA . VAL A 1 329 ? 12.495 7.887 46.489 1.00 9.28 ? 330 VAL A CA 1 ATOM 2621 C C . VAL A 1 329 ? 12.641 6.556 45.887 1.00 8.44 ? 330 VAL A C 1 ATOM 2622 O O . VAL A 1 329 ? 13.583 5.860 46.166 1.00 7.94 ? 330 VAL A O 1 ATOM 2623 C CB . VAL A 1 329 ? 13.771 8.718 46.173 1.00 10.16 ? 330 VAL A CB 1 ATOM 2624 C CG1 . VAL A 1 329 ? 14.070 8.720 44.708 1.00 9.66 ? 330 VAL A CG1 1 ATOM 2625 C CG2 . VAL A 1 329 ? 13.565 10.152 46.650 1.00 12.26 ? 330 VAL A CG2 1 ATOM 2626 N N . TRP A 1 330 ? 11.710 6.169 45.054 1.00 9.81 ? 331 TRP A N 1 ATOM 2627 C CA . TRP A 1 330 ? 11.811 4.835 44.435 1.00 11.86 ? 331 TRP A CA 1 ATOM 2628 C C . TRP A 1 330 ? 12.764 4.794 43.241 1.00 12.53 ? 331 TRP A C 1 ATOM 2629 O O . TRP A 1 330 ? 12.494 5.464 42.219 1.00 6.79 ? 331 TRP A O 1 ATOM 2630 C CB . TRP A 1 330 ? 10.481 4.236 44.026 1.00 10.77 ? 331 TRP A CB 1 ATOM 2631 C CG . TRP A 1 330 ? 10.702 2.919 43.318 1.00 15.80 ? 331 TRP A CG 1 ATOM 2632 C CD1 . TRP A 1 330 ? 10.660 2.717 41.987 1.00 23.57 ? 331 TRP A CD1 1 ATOM 2633 C CD2 . TRP A 1 330 ? 11.041 1.651 43.886 1.00 13.96 ? 331 TRP A CD2 1 ATOM 2634 N NE1 . TRP A 1 330 ? 10.954 1.404 41.680 1.00 22.00 ? 331 TRP A NE1 1 ATOM 2635 C CE2 . TRP A 1 330 ? 11.181 0.736 42.835 1.00 16.07 ? 331 TRP A CE2 1 ATOM 2636 C CE3 . TRP A 1 330 ? 11.208 1.193 45.182 1.00 15.98 ? 331 TRP A CE3 1 ATOM 2637 C CZ2 . TRP A 1 330 ? 11.469 -0.595 43.028 1.00 17.30 ? 331 TRP A CZ2 1 ATOM 2638 C CZ3 . TRP A 1 330 ? 11.509 -0.129 45.399 1.00 15.25 ? 331 TRP A CZ3 1 ATOM 2639 C CH2 . TRP A 1 330 ? 11.680 -1.007 44.327 1.00 17.83 ? 331 TRP A CH2 1 ATOM 2640 N N . ALA A 1 331 ? 13.857 3.998 43.462 1.00 14.72 ? 332 ALA A N 1 ATOM 2641 C CA . ALA A 1 331 ? 14.956 3.699 42.559 1.00 13.29 ? 332 ALA A CA 1 ATOM 2642 C C . ALA A 1 331 ? 15.913 4.853 42.172 1.00 12.10 ? 332 ALA A C 1 ATOM 2643 O O . ALA A 1 331 ? 15.608 5.682 41.320 1.00 7.73 ? 332 ALA A O 1 ATOM 2644 C CB . ALA A 1 331 ? 14.390 3.035 41.360 1.00 15.31 ? 332 ALA A CB 1 ATOM 2645 N N . LEU A 1 332 ? 17.093 4.837 42.803 1.00 12.63 ? 333 LEU A N 1 ATOM 2646 C CA . LEU A 1 332 ? 18.168 5.782 42.506 1.00 13.53 ? 333 LEU A CA 1 ATOM 2647 C C . LEU A 1 332 ? 18.647 5.411 41.159 1.00 14.25 ? 333 LEU A C 1 ATOM 2648 O O . LEU A 1 332 ? 19.267 6.237 40.528 1.00 17.12 ? 333 LEU A O 1 ATOM 2649 C CB . LEU A 1 332 ? 19.350 5.651 43.468 1.00 12.45 ? 333 LEU A CB 1 ATOM 2650 C CG . LEU A 1 332 ? 19.151 6.033 44.910 1.00 14.18 ? 333 LEU A CG 1 ATOM 2651 C CD1 . LEU A 1 332 ? 20.116 5.175 45.740 1.00 15.30 ? 333 LEU A CD1 1 ATOM 2652 C CD2 . LEU A 1 332 ? 19.365 7.531 45.156 1.00 11.36 ? 333 LEU A CD2 1 ATOM 2653 N N . ASP A 1 333 ? 18.373 4.162 40.738 1.00 13.75 ? 334 ASP A N 1 ATOM 2654 C CA . ASP A 1 333 ? 18.792 3.623 39.451 1.00 12.44 ? 334 ASP A CA 1 ATOM 2655 C C . ASP A 1 333 ? 17.883 4.035 38.328 1.00 11.58 ? 334 ASP A C 1 ATOM 2656 O O . ASP A 1 333 ? 18.236 3.890 37.160 1.00 9.75 ? 334 ASP A O 1 ATOM 2657 C CB . ASP A 1 333 ? 18.900 2.108 39.504 1.00 13.55 ? 334 ASP A CB 1 ATOM 2658 C CG . ASP A 1 333 ? 17.595 1.442 39.880 1.00 14.77 ? 334 ASP A CG 1 ATOM 2659 O OD1 . ASP A 1 333 ? 16.707 1.331 39.011 1.00 16.85 ? 334 ASP A OD1 1 ATOM 2660 O OD2 . ASP A 1 333 ? 17.427 1.007 41.039 1.00 15.25 ? 334 ASP A OD2 1 ATOM 2661 N N . LEU A 1 334 ? 16.715 4.554 38.677 1.00 12.88 ? 335 LEU A N 1 ATOM 2662 C CA . LEU A 1 334 ? 15.754 5.033 37.639 1.00 13.88 ? 335 LEU A CA 1 ATOM 2663 C C . LEU A 1 334 ? 15.945 6.540 37.412 1.00 13.14 ? 335 LEU A C 1 ATOM 2664 O O . LEU A 1 334 ? 15.442 7.123 36.489 1.00 11.86 ? 335 LEU A O 1 ATOM 2665 C CB . LEU A 1 334 ? 14.309 4.737 38.058 1.00 12.51 ? 335 LEU A CB 1 ATOM 2666 C CG . LEU A 1 334 ? 13.994 3.261 38.173 1.00 10.93 ? 335 LEU A CG 1 ATOM 2667 C CD1 . LEU A 1 334 ? 12.562 3.109 38.663 1.00 13.05 ? 335 LEU A CD1 1 ATOM 2668 C CD2 . LEU A 1 334 ? 14.190 2.574 36.854 1.00 10.02 ? 335 LEU A CD2 1 ATOM 2669 N N . ASP A 1 335 ? 16.707 7.142 38.306 1.00 14.06 ? 336 ASP A N 1 ATOM 2670 C CA . ASP A 1 335 ? 17.023 8.578 38.233 1.00 13.60 ? 336 ASP A CA 1 ATOM 2671 C C . ASP A 1 335 ? 18.172 8.655 37.270 1.00 14.57 ? 336 ASP A C 1 ATOM 2672 O O . ASP A 1 335 ? 18.646 7.640 36.805 1.00 14.95 ? 336 ASP A O 1 ATOM 2673 C CB . ASP A 1 335 ? 17.496 9.109 39.596 1.00 13.13 ? 336 ASP A CB 1 ATOM 2674 C CG . ASP A 1 335 ? 17.478 10.606 39.680 1.00 11.84 ? 336 ASP A CG 1 ATOM 2675 O OD1 . ASP A 1 335 ? 17.643 11.203 38.630 1.00 11.51 ? 336 ASP A OD1 1 ATOM 2676 O OD2 . ASP A 1 335 ? 17.340 11.243 40.759 1.00 12.51 ? 336 ASP A OD2 1 ATOM 2677 N N . ASP A 1 336 ? 18.641 9.849 36.968 1.00 15.97 ? 337 ASP A N 1 ATOM 2678 C CA . ASP A 1 336 ? 19.794 10.019 36.072 1.00 16.95 ? 337 ASP A CA 1 ATOM 2679 C C . ASP A 1 336 ? 21.095 9.915 36.899 1.00 16.98 ? 337 ASP A C 1 ATOM 2680 O O . ASP A 1 336 ? 21.777 10.913 37.196 1.00 15.73 ? 337 ASP A O 1 ATOM 2681 C CB . ASP A 1 336 ? 19.704 11.376 35.343 1.00 17.31 ? 337 ASP A CB 1 ATOM 2682 C CG . ASP A 1 336 ? 20.712 11.502 34.187 1.00 17.98 ? 337 ASP A CG 1 ATOM 2683 O OD1 . ASP A 1 336 ? 21.341 10.509 33.830 1.00 20.00 ? 337 ASP A OD1 1 ATOM 2684 O OD2 . ASP A 1 336 ? 20.916 12.572 33.584 1.00 19.66 ? 337 ASP A OD2 1 ATOM 2685 N N . PHE A 1 337 ? 21.428 8.695 37.285 1.00 16.92 ? 338 PHE A N 1 ATOM 2686 C CA . PHE A 1 337 ? 22.596 8.466 38.130 1.00 16.68 ? 338 PHE A CA 1 ATOM 2687 C C . PHE A 1 337 ? 23.898 8.850 37.475 1.00 18.57 ? 338 PHE A C 1 ATOM 2688 O O . PHE A 1 337 ? 24.854 9.191 38.164 1.00 18.40 ? 338 PHE A O 1 ATOM 2689 C CB . PHE A 1 337 ? 22.647 7.015 38.633 1.00 14.40 ? 338 PHE A CB 1 ATOM 2690 C CG . PHE A 1 337 ? 22.660 5.986 37.545 1.00 12.63 ? 338 PHE A CG 1 ATOM 2691 C CD1 . PHE A 1 337 ? 21.489 5.614 36.902 1.00 10.45 ? 338 PHE A CD1 1 ATOM 2692 C CD2 . PHE A 1 337 ? 23.825 5.357 37.190 1.00 10.53 ? 338 PHE A CD2 1 ATOM 2693 C CE1 . PHE A 1 337 ? 21.489 4.667 35.896 1.00 6.34 ? 338 PHE A CE1 1 ATOM 2694 C CE2 . PHE A 1 337 ? 23.821 4.377 36.213 1.00 7.09 ? 338 PHE A CE2 1 ATOM 2695 C CZ . PHE A 1 337 ? 22.662 4.049 35.561 1.00 6.41 ? 338 PHE A CZ 1 ATOM 2696 N N . ARG A 1 338 ? 23.961 8.796 36.146 1.00 21.34 ? 339 ARG A N 1 ATOM 2697 C CA . ARG A 1 338 ? 25.191 9.197 35.458 1.00 22.27 ? 339 ARG A CA 1 ATOM 2698 C C . ARG A 1 338 ? 25.222 10.693 35.335 1.00 23.22 ? 339 ARG A C 1 ATOM 2699 O O . ARG A 1 338 ? 26.249 11.315 35.490 1.00 22.71 ? 339 ARG A O 1 ATOM 2700 C CB . ARG A 1 338 ? 25.284 8.534 34.110 1.00 21.37 ? 339 ARG A CB 1 ATOM 2701 C CG . ARG A 1 338 ? 25.598 7.035 34.242 1.00 25.53 ? 339 ARG A CG 1 ATOM 2702 C CD . ARG A 1 338 ? 25.823 6.306 32.893 1.00 27.57 ? 339 ARG A CD 1 ATOM 2703 N NE . ARG A 1 338 ? 25.940 4.842 32.976 1.00 25.31 ? 339 ARG A NE 1 ATOM 2704 C CZ . ARG A 1 338 ? 26.989 4.201 33.452 1.00 25.59 ? 339 ARG A CZ 1 ATOM 2705 N NH1 . ARG A 1 338 ? 28.045 4.854 33.905 1.00 25.43 ? 339 ARG A NH1 1 ATOM 2706 N NH2 . ARG A 1 338 ? 26.974 2.891 33.502 1.00 29.17 ? 339 ARG A NH2 1 ATOM 2707 N N . GLY A 1 339 ? 24.055 11.266 35.099 1.00 25.92 ? 340 GLY A N 1 ATOM 2708 C CA . GLY A 1 339 ? 23.902 12.715 34.946 1.00 28.39 ? 340 GLY A CA 1 ATOM 2709 C C . GLY A 1 339 ? 24.242 13.222 33.539 1.00 29.09 ? 340 GLY A C 1 ATOM 2710 O O . GLY A 1 339 ? 24.394 14.410 33.306 1.00 30.54 ? 340 GLY A O 1 ATOM 2711 N N . THR A 1 340 ? 24.332 12.299 32.603 1.00 29.15 ? 341 THR A N 1 ATOM 2712 C CA . THR A 1 340 ? 24.650 12.614 31.245 1.00 28.40 ? 341 THR A CA 1 ATOM 2713 C C . THR A 1 340 ? 23.489 12.462 30.332 1.00 29.35 ? 341 THR A C 1 ATOM 2714 O O . THR A 1 340 ? 23.664 12.386 29.152 1.00 30.79 ? 341 THR A O 1 ATOM 2715 C CB . THR A 1 340 ? 25.715 11.683 30.755 1.00 28.60 ? 341 THR A CB 1 ATOM 2716 O OG1 . THR A 1 340 ? 25.189 10.358 30.612 1.00 26.23 ? 341 THR A OG1 1 ATOM 2717 C CG2 . THR A 1 340 ? 26.889 11.649 31.770 1.00 30.38 ? 341 THR A CG2 1 ATOM 2718 N N . PHE A 1 341 ? 22.290 12.410 30.864 1.00 31.35 ? 342 PHE A N 1 ATOM 2719 C CA . PHE A 1 341 ? 21.091 12.244 30.025 1.00 32.42 ? 342 PHE A CA 1 ATOM 2720 C C . PHE A 1 341 ? 20.137 13.427 30.033 1.00 33.82 ? 342 PHE A C 1 ATOM 2721 O O . PHE A 1 341 ? 19.469 13.623 29.046 1.00 34.71 ? 342 PHE A O 1 ATOM 2722 C CB . PHE A 1 341 ? 20.290 11.013 30.468 1.00 32.08 ? 342 PHE A CB 1 ATOM 2723 C CG . PHE A 1 341 ? 20.784 9.719 29.929 1.00 29.62 ? 342 PHE A CG 1 ATOM 2724 C CD1 . PHE A 1 341 ? 21.716 8.986 30.618 1.00 28.73 ? 342 PHE A CD1 1 ATOM 2725 C CD2 . PHE A 1 341 ? 20.234 9.190 28.762 1.00 28.48 ? 342 PHE A CD2 1 ATOM 2726 C CE1 . PHE A 1 341 ? 22.117 7.750 30.156 1.00 29.85 ? 342 PHE A CE1 1 ATOM 2727 C CE2 . PHE A 1 341 ? 20.625 7.953 28.270 1.00 27.72 ? 342 PHE A CE2 1 ATOM 2728 C CZ . PHE A 1 341 ? 21.567 7.228 28.967 1.00 30.58 ? 342 PHE A CZ 1 ATOM 2729 N N . CYS A 1 342 ? 20.059 14.183 31.134 1.00 35.44 ? 343 CYS A N 1 ATOM 2730 C CA . CYS A 1 342 ? 19.119 15.285 31.238 1.00 37.25 ? 343 CYS A CA 1 ATOM 2731 C C . CYS A 1 342 ? 19.706 16.673 31.169 1.00 41.00 ? 343 CYS A C 1 ATOM 2732 O O . CYS A 1 342 ? 19.922 17.306 32.197 1.00 44.65 ? 343 CYS A O 1 ATOM 2733 C CB . CYS A 1 342 ? 18.362 15.140 32.546 1.00 36.27 ? 343 CYS A CB 1 ATOM 2734 S SG . CYS A 1 342 ? 17.600 13.517 32.749 1.00 28.93 ? 343 CYS A SG 1 ATOM 2735 N N . GLY A 1 343 ? 19.944 17.181 29.980 1.00 43.98 ? 344 GLY A N 1 ATOM 2736 C CA . GLY A 1 343 ? 20.513 18.519 29.861 1.00 46.96 ? 344 GLY A CA 1 ATOM 2737 C C . GLY A 1 343 ? 21.630 18.748 30.867 1.00 48.43 ? 344 GLY A C 1 ATOM 2738 O O . GLY A 1 343 ? 22.705 18.186 30.716 1.00 48.15 ? 344 GLY A O 1 ATOM 2739 N N . GLN A 1 344 ? 21.333 19.534 31.903 1.00 50.53 ? 345 GLN A N 1 ATOM 2740 C CA . GLN A 1 344 ? 22.278 19.884 32.959 1.00 52.82 ? 345 GLN A CA 1 ATOM 2741 C C . GLN A 1 344 ? 23.247 18.806 33.377 1.00 53.14 ? 345 GLN A C 1 ATOM 2742 O O . GLN A 1 344 ? 22.949 17.618 33.254 1.00 53.52 ? 345 GLN A O 1 ATOM 2743 C CB . GLN A 1 344 ? 21.532 20.389 34.188 1.00 54.40 ? 345 GLN A CB 1 ATOM 2744 C CG . GLN A 1 344 ? 20.319 19.577 34.593 1.00 56.85 ? 345 GLN A CG 1 ATOM 2745 C CD . GLN A 1 344 ? 19.515 20.284 35.702 1.00 60.13 ? 345 GLN A CD 1 ATOM 2746 O OE1 . GLN A 1 344 ? 19.933 20.320 36.873 1.00 59.94 ? 345 GLN A OE1 1 ATOM 2747 N NE2 . GLN A 1 344 ? 18.368 20.865 35.328 1.00 62.02 ? 345 GLN A NE2 1 ATOM 2748 N N . ASN A 1 345 ? 24.397 19.266 33.883 1.00 53.32 ? 346 ASN A N 1 ATOM 2749 C CA . ASN A 1 345 ? 25.514 18.441 34.315 1.00 53.25 ? 346 ASN A CA 1 ATOM 2750 C C . ASN A 1 345 ? 25.386 17.819 35.687 1.00 49.63 ? 346 ASN A C 1 ATOM 2751 O O . ASN A 1 345 ? 26.319 17.256 36.214 1.00 49.95 ? 346 ASN A O 1 ATOM 2752 C CB . ASN A 1 345 ? 26.788 19.294 34.289 1.00 56.43 ? 346 ASN A CB 1 ATOM 2753 C CG . ASN A 1 345 ? 27.723 18.922 33.127 1.00 62.17 ? 346 ASN A CG 1 ATOM 2754 O OD1 . ASN A 1 345 ? 27.289 18.880 31.947 1.00 65.98 ? 346 ASN A OD1 1 ATOM 2755 N ND2 . ASN A 1 345 ? 29.019 18.646 33.454 1.00 64.34 ? 346 ASN A ND2 1 ATOM 2756 N N . LEU A 1 346 ? 24.222 17.910 36.277 1.00 46.25 ? 347 LEU A N 1 ATOM 2757 C CA . LEU A 1 346 ? 23.999 17.341 37.612 1.00 42.24 ? 347 LEU A CA 1 ATOM 2758 C C . LEU A 1 346 ? 23.806 15.827 37.598 1.00 37.17 ? 347 LEU A C 1 ATOM 2759 O O . LEU A 1 346 ? 23.317 15.245 36.614 1.00 35.01 ? 347 LEU A O 1 ATOM 2760 C CB . LEU A 1 346 ? 22.761 18.012 38.227 1.00 42.45 ? 347 LEU A CB 1 ATOM 2761 C CG . LEU A 1 346 ? 22.894 18.490 39.669 1.00 43.85 ? 347 LEU A CG 1 ATOM 2762 C CD1 . LEU A 1 346 ? 21.722 19.403 40.000 1.00 44.84 ? 347 LEU A CD1 1 ATOM 2763 C CD2 . LEU A 1 346 ? 22.967 17.293 40.625 1.00 45.56 ? 347 LEU A CD2 1 ATOM 2764 N N . THR A 1 347 ? 24.182 15.206 38.704 1.00 32.40 ? 348 THR A N 1 ATOM 2765 C CA . THR A 1 347 ? 24.030 13.764 38.865 1.00 29.13 ? 348 THR A CA 1 ATOM 2766 C C . THR A 1 347 ? 22.908 13.455 39.843 1.00 25.59 ? 348 THR A C 1 ATOM 2767 O O . THR A 1 347 ? 22.870 14.051 40.903 1.00 25.62 ? 348 THR A O 1 ATOM 2768 C CB . THR A 1 347 ? 25.348 13.175 39.325 1.00 27.91 ? 348 THR A CB 1 ATOM 2769 O OG1 . THR A 1 347 ? 25.492 11.882 38.736 1.00 31.89 ? 348 THR A OG1 1 ATOM 2770 C CG2 . THR A 1 347 ? 25.399 13.048 40.841 1.00 26.23 ? 348 THR A CG2 1 ATOM 2771 N N . PHE A 1 348 ? 21.985 12.562 39.483 1.00 22.49 ? 349 PHE A N 1 ATOM 2772 C CA . PHE A 1 348 ? 20.816 12.272 40.336 1.00 20.81 ? 349 PHE A CA 1 ATOM 2773 C C . PHE A 1 348 ? 19.978 13.572 40.480 1.00 19.54 ? 349 PHE A C 1 ATOM 2774 O O . PHE A 1 348 ? 19.590 13.956 41.557 1.00 21.21 ? 349 PHE A O 1 ATOM 2775 C CB . PHE A 1 348 ? 21.225 11.800 41.762 1.00 20.21 ? 349 PHE A CB 1 ATOM 2776 C CG . PHE A 1 348 ? 21.873 10.436 41.849 1.00 16.19 ? 349 PHE A CG 1 ATOM 2777 C CD1 . PHE A 1 348 ? 21.140 9.304 41.673 1.00 17.07 ? 349 PHE A CD1 1 ATOM 2778 C CD2 . PHE A 1 348 ? 23.210 10.303 42.177 1.00 13.72 ? 349 PHE A CD2 1 ATOM 2779 C CE1 . PHE A 1 348 ? 21.714 8.064 41.780 1.00 16.80 ? 349 PHE A CE1 1 ATOM 2780 C CE2 . PHE A 1 348 ? 23.786 9.086 42.309 1.00 13.19 ? 349 PHE A CE2 1 ATOM 2781 C CZ . PHE A 1 348 ? 23.043 7.961 42.107 1.00 16.55 ? 349 PHE A CZ 1 ATOM 2782 N N . PRO A 1 349 ? 19.657 14.234 39.398 1.00 18.04 ? 350 PRO A N 1 ATOM 2783 C CA . PRO A 1 349 ? 18.896 15.496 39.418 1.00 16.13 ? 350 PRO A CA 1 ATOM 2784 C C . PRO A 1 349 ? 17.626 15.518 40.285 1.00 13.69 ? 350 PRO A C 1 ATOM 2785 O O . PRO A 1 349 ? 17.408 16.426 41.022 1.00 13.57 ? 350 PRO A O 1 ATOM 2786 C CB . PRO A 1 349 ? 18.535 15.693 37.936 1.00 16.81 ? 350 PRO A CB 1 ATOM 2787 C CG . PRO A 1 349 ? 18.530 14.311 37.364 1.00 18.78 ? 350 PRO A CG 1 ATOM 2788 C CD . PRO A 1 349 ? 19.751 13.684 38.036 1.00 19.08 ? 350 PRO A CD 1 ATOM 2789 N N . LEU A 1 350 ? 16.817 14.496 40.198 1.00 12.12 ? 351 LEU A N 1 ATOM 2790 C CA . LEU A 1 350 ? 15.590 14.421 40.924 1.00 11.19 ? 351 LEU A CA 1 ATOM 2791 C C . LEU A 1 350 ? 15.812 14.190 42.389 1.00 10.43 ? 351 LEU A C 1 ATOM 2792 O O . LEU A 1 350 ? 15.245 14.885 43.247 1.00 11.96 ? 351 LEU A O 1 ATOM 2793 C CB . LEU A 1 350 ? 14.712 13.300 40.352 1.00 11.48 ? 351 LEU A CB 1 ATOM 2794 C CG . LEU A 1 350 ? 13.446 13.694 39.603 1.00 11.27 ? 351 LEU A CG 1 ATOM 2795 C CD1 . LEU A 1 350 ? 13.709 14.617 38.481 1.00 11.49 ? 351 LEU A CD1 1 ATOM 2796 C CD2 . LEU A 1 350 ? 12.820 12.463 39.044 1.00 16.07 ? 351 LEU A CD2 1 ATOM 2797 N N . THR A 1 351 ? 16.606 13.210 42.726 1.00 8.99 ? 352 THR A N 1 ATOM 2798 C CA . THR A 1 351 ? 16.798 12.911 44.147 1.00 8.80 ? 352 THR A CA 1 ATOM 2799 C C . THR A 1 351 ? 17.466 14.039 44.898 1.00 10.47 ? 352 THR A C 1 ATOM 2800 O O . THR A 1 351 ? 17.204 14.251 46.054 1.00 12.16 ? 352 THR A O 1 ATOM 2801 C CB . THR A 1 351 ? 17.609 11.643 44.332 1.00 7.51 ? 352 THR A CB 1 ATOM 2802 O OG1 . THR A 1 351 ? 16.947 10.541 43.716 1.00 4.92 ? 352 THR A OG1 1 ATOM 2803 C CG2 . THR A 1 351 ? 17.765 11.292 45.825 1.00 3.35 ? 352 THR A CG2 1 ATOM 2804 N N . SER A 1 352 ? 18.367 14.748 44.240 1.00 11.31 ? 353 SER A N 1 ATOM 2805 C CA . SER A 1 352 ? 19.055 15.851 44.871 1.00 12.78 ? 353 SER A CA 1 ATOM 2806 C C . SER A 1 352 ? 18.108 17.124 44.973 1.00 12.39 ? 353 SER A C 1 ATOM 2807 O O . SER A 1 352 ? 18.265 18.004 45.868 1.00 12.43 ? 353 SER A O 1 ATOM 2808 C CB . SER A 1 352 ? 20.349 16.138 44.105 1.00 13.23 ? 353 SER A CB 1 ATOM 2809 O OG . SER A 1 352 ? 20.083 16.224 42.706 1.00 17.87 ? 353 SER A OG 1 ATOM 2810 N N . ALA A 1 353 ? 17.134 17.186 44.080 1.00 10.02 ? 354 ALA A N 1 ATOM 2811 C CA . ALA A 1 353 ? 16.177 18.266 44.133 1.00 9.45 ? 354 ALA A CA 1 ATOM 2812 C C . ALA A 1 353 ? 15.392 18.103 45.459 1.00 9.59 ? 354 ALA A C 1 ATOM 2813 O O . ALA A 1 353 ? 15.067 19.053 46.143 1.00 10.62 ? 354 ALA A O 1 ATOM 2814 C CB . ALA A 1 353 ? 15.236 18.234 42.944 1.00 7.74 ? 354 ALA A CB 1 ATOM 2815 N N . VAL A 1 354 ? 15.092 16.879 45.802 1.00 8.22 ? 355 VAL A N 1 ATOM 2816 C CA . VAL A 1 354 ? 14.368 16.628 47.021 1.00 9.46 ? 355 VAL A CA 1 ATOM 2817 C C . VAL A 1 354 ? 15.254 16.978 48.215 1.00 10.97 ? 355 VAL A C 1 ATOM 2818 O O . VAL A 1 354 ? 14.827 17.607 49.156 1.00 10.22 ? 355 VAL A O 1 ATOM 2819 C CB . VAL A 1 354 ? 13.925 15.107 47.088 1.00 9.16 ? 355 VAL A CB 1 ATOM 2820 C CG1 . VAL A 1 354 ? 13.465 14.713 48.459 1.00 5.13 ? 355 VAL A CG1 1 ATOM 2821 C CG2 . VAL A 1 354 ? 12.882 14.844 46.130 1.00 8.77 ? 355 VAL A CG2 1 ATOM 2822 N N . LYS A 1 355 ? 16.496 16.558 48.155 1.00 13.32 ? 356 LYS A N 1 ATOM 2823 C CA . LYS A 1 355 ? 17.449 16.813 49.232 1.00 16.23 ? 356 LYS A CA 1 ATOM 2824 C C . LYS A 1 355 ? 17.675 18.313 49.460 1.00 16.35 ? 356 LYS A C 1 ATOM 2825 O O . LYS A 1 355 ? 17.907 18.749 50.592 1.00 14.30 ? 356 LYS A O 1 ATOM 2826 C CB . LYS A 1 355 ? 18.804 16.158 48.955 1.00 16.99 ? 356 LYS A CB 1 ATOM 2827 C CG . LYS A 1 355 ? 19.761 16.277 50.106 1.00 22.34 ? 356 LYS A CG 1 ATOM 2828 C CD . LYS A 1 355 ? 21.158 15.819 49.789 1.00 26.00 ? 356 LYS A CD 1 ATOM 2829 C CE . LYS A 1 355 ? 22.072 15.989 51.012 1.00 30.74 ? 356 LYS A CE 1 ATOM 2830 N NZ . LYS A 1 355 ? 23.571 15.914 50.685 1.00 36.04 ? 356 LYS A NZ 1 ATOM 2831 N N . ASP A 1 356 ? 17.634 19.076 48.377 1.00 16.35 ? 357 ASP A N 1 ATOM 2832 C CA . ASP A 1 356 ? 17.800 20.507 48.496 1.00 16.08 ? 357 ASP A CA 1 ATOM 2833 C C . ASP A 1 356 ? 16.678 21.082 49.332 1.00 13.80 ? 357 ASP A C 1 ATOM 2834 O O . ASP A 1 356 ? 16.939 21.753 50.295 1.00 14.80 ? 357 ASP A O 1 ATOM 2835 C CB . ASP A 1 356 ? 17.823 21.139 47.113 1.00 18.23 ? 357 ASP A CB 1 ATOM 2836 C CG . ASP A 1 356 ? 19.206 21.125 46.482 1.00 21.45 ? 357 ASP A CG 1 ATOM 2837 O OD1 . ASP A 1 356 ? 20.184 20.507 47.054 1.00 20.12 ? 357 ASP A OD1 1 ATOM 2838 O OD2 . ASP A 1 356 ? 19.338 21.744 45.394 1.00 23.65 ? 357 ASP A OD2 1 ATOM 2839 N N . VAL A 1 357 ? 15.445 20.821 48.973 1.00 11.50 ? 358 VAL A N 1 ATOM 2840 C CA . VAL A 1 357 ? 14.315 21.345 49.696 1.00 12.05 ? 358 VAL A CA 1 ATOM 2841 C C . VAL A 1 357 ? 14.317 20.862 51.123 1.00 13.18 ? 358 VAL A C 1 ATOM 2842 O O . VAL A 1 357 ? 13.966 21.575 52.050 1.00 13.04 ? 358 VAL A O 1 ATOM 2843 C CB . VAL A 1 357 ? 12.998 20.920 49.050 1.00 11.60 ? 358 VAL A CB 1 ATOM 2844 C CG1 . VAL A 1 357 ? 11.806 21.487 49.805 1.00 11.36 ? 358 VAL A CG1 1 ATOM 2845 C CG2 . VAL A 1 357 ? 12.951 21.384 47.620 1.00 13.69 ? 358 VAL A CG2 1 ATOM 2846 N N . LEU A 1 358 ? 14.699 19.619 51.310 1.00 15.56 ? 359 LEU A N 1 ATOM 2847 C CA . LEU A 1 358 ? 14.702 19.024 52.661 1.00 17.42 ? 359 LEU A CA 1 ATOM 2848 C C . LEU A 1 358 ? 15.776 19.658 53.540 1.00 21.03 ? 359 LEU A C 1 ATOM 2849 O O . LEU A 1 358 ? 15.627 19.775 54.752 1.00 21.91 ? 359 LEU A O 1 ATOM 2850 C CB . LEU A 1 358 ? 14.924 17.528 52.566 1.00 15.47 ? 359 LEU A CB 1 ATOM 2851 C CG . LEU A 1 358 ? 13.758 16.634 52.899 1.00 12.84 ? 359 LEU A CG 1 ATOM 2852 C CD1 . LEU A 1 358 ? 12.492 17.139 52.268 1.00 12.36 ? 359 LEU A CD1 1 ATOM 2853 C CD2 . LEU A 1 358 ? 14.074 15.216 52.441 1.00 13.79 ? 359 LEU A CD2 1 ATOM 2854 N N . ALA A 1 359 ? 16.851 20.099 52.919 1.00 25.52 ? 360 ALA A N 1 ATOM 2855 C CA . ALA A 1 359 ? 17.919 20.705 53.651 1.00 28.32 ? 360 ALA A CA 1 ATOM 2856 C C . ALA A 1 359 ? 17.750 22.175 53.923 1.00 31.36 ? 360 ALA A C 1 ATOM 2857 O O . ALA A 1 359 ? 18.622 22.774 54.554 1.00 31.46 ? 360 ALA A O 1 ATOM 2858 C CB . ALA A 1 359 ? 19.183 20.494 52.927 1.00 30.80 ? 360 ALA A CB 1 ATOM 2859 N N . ARG A 1 360 ? 16.652 22.778 53.481 1.00 35.67 ? 361 ARG A N 1 ATOM 2860 C CA . ARG A 1 360 ? 16.480 24.200 53.774 1.00 41.00 ? 361 ARG A CA 1 ATOM 2861 C C . ARG A 1 360 ? 15.532 24.509 54.917 1.00 43.46 ? 361 ARG A C 1 ATOM 2862 O O . ARG A 1 360 ? 15.001 25.599 54.962 1.00 44.19 ? 361 ARG A O 1 ATOM 2863 C CB . ARG A 1 360 ? 16.108 24.964 52.528 1.00 42.68 ? 361 ARG A CB 1 ATOM 2864 C CG . ARG A 1 360 ? 14.838 24.504 51.910 1.00 52.01 ? 361 ARG A CG 1 ATOM 2865 C CD . ARG A 1 360 ? 14.156 25.605 51.052 1.00 59.81 ? 361 ARG A CD 1 ATOM 2866 N NE . ARG A 1 360 ? 14.541 25.586 49.650 1.00 64.62 ? 361 ARG A NE 1 ATOM 2867 C CZ . ARG A 1 360 ? 13.664 25.567 48.650 1.00 70.98 ? 361 ARG A CZ 1 ATOM 2868 N NH1 . ARG A 1 360 ? 12.349 25.571 48.909 1.00 70.87 ? 361 ARG A NH1 1 ATOM 2869 N NH2 . ARG A 1 360 ? 14.100 25.532 47.386 1.00 75.19 ? 361 ARG A NH2 1 ATOM 2870 N N . VAL A 1 361 ? 15.357 23.556 55.834 1.00 47.67 ? 362 VAL A N 1 ATOM 2871 C CA . VAL A 1 361 ? 14.503 23.691 57.015 1.00 51.92 ? 362 VAL A CA 1 ATOM 2872 C C . VAL A 1 361 ? 12.995 23.607 56.791 1.00 53.21 ? 362 VAL A C 1 ATOM 2873 C CB . VAL A 1 361 ? 14.795 25.000 57.828 1.00 53.72 ? 362 VAL A CB 1 ATOM 2874 C CG1 . VAL A 1 361 ? 13.985 26.201 57.342 1.00 54.45 ? 362 VAL A CG1 1 ATOM 2875 C CG2 . VAL A 1 361 ? 14.501 24.742 59.324 1.00 56.60 ? 362 VAL A CG2 1 ATOM 2876 O OXT . VAL A 1 361 ? 12.461 24.421 56.038 1.00 54.14 ? 362 VAL A OXT 1 HETATM 2877 C C1 . NAG B 2 . ? 6.680 -0.037 44.576 1.00 39.21 ? 363 NAG A C1 1 HETATM 2878 C C2 . NAG B 2 . ? 7.225 -1.458 44.791 1.00 36.03 ? 363 NAG A C2 1 HETATM 2879 C C3 . NAG B 2 . ? 8.039 -2.160 43.706 1.00 33.58 ? 363 NAG A C3 1 HETATM 2880 C C4 . NAG B 2 . ? 7.406 -1.785 42.427 1.00 35.24 ? 363 NAG A C4 1 HETATM 2881 C C5 . NAG B 2 . ? 7.539 -0.278 42.273 1.00 39.07 ? 363 NAG A C5 1 HETATM 2882 C C6 . NAG B 2 . ? 6.894 0.116 40.893 1.00 40.32 ? 363 NAG A C6 1 HETATM 2883 C C7 . NAG B 2 . ? 8.540 -0.925 47.044 1.00 41.62 ? 363 NAG A C7 1 HETATM 2884 C C8 . NAG B 2 . ? 8.800 0.524 47.485 1.00 39.82 ? 363 NAG A C8 1 HETATM 2885 N N2 . NAG B 2 . ? 8.252 -0.954 45.695 1.00 38.98 ? 363 NAG A N2 1 HETATM 2886 O O3 . NAG B 2 . ? 8.029 -3.602 43.797 1.00 32.29 ? 363 NAG A O3 1 HETATM 2887 O O4 . NAG B 2 . ? 8.151 -2.197 41.273 1.00 38.98 ? 363 NAG A O4 1 HETATM 2888 O O5 . NAG B 2 . ? 6.971 0.537 43.311 1.00 40.56 ? 363 NAG A O5 1 HETATM 2889 O O6 . NAG B 2 . ? 7.043 1.567 40.811 1.00 47.82 ? 363 NAG A O6 1 HETATM 2890 O O7 . NAG B 2 . ? 8.741 -1.921 47.817 1.00 42.20 ? 363 NAG A O7 1 HETATM 2891 C C1 . NDG C 3 . ? 9.180 -3.188 40.860 1.00 33.19 ? 364 NDG A C1 1 HETATM 2892 C C2 . NDG C 3 . ? 9.562 -2.927 39.348 1.00 31.32 ? 364 NDG A C2 1 HETATM 2893 C C3 . NDG C 3 . ? 9.599 -4.123 38.426 1.00 32.63 ? 364 NDG A C3 1 HETATM 2894 C C4 . NDG C 3 . ? 10.303 -5.211 39.238 1.00 33.31 ? 364 NDG A C4 1 HETATM 2895 C C5 . NDG C 3 . ? 9.450 -5.604 40.460 1.00 31.39 ? 364 NDG A C5 1 HETATM 2896 C C6 . NDG C 3 . ? 10.201 -6.709 41.230 1.00 31.68 ? 364 NDG A C6 1 HETATM 2897 C C7 . NDG C 3 . ? 9.779 -0.753 38.482 1.00 30.26 ? 364 NDG A C7 1 HETATM 2898 C C8 . NDG C 3 . ? 9.321 0.389 37.659 1.00 30.34 ? 364 NDG A C8 1 HETATM 2899 O O . NDG C 3 . ? 8.923 -4.543 41.291 1.00 28.93 ? 364 NDG A O 1 HETATM 2900 O O3 . NDG C 3 . ? 10.373 -3.731 37.246 1.00 36.32 ? 364 NDG A O3 1 HETATM 2901 O O4 . NDG C 3 . ? 10.342 -6.411 38.453 1.00 34.19 ? 364 NDG A O4 1 HETATM 2902 O O6 . NDG C 3 . ? 9.422 -6.993 42.395 1.00 37.00 ? 364 NDG A O6 1 HETATM 2903 O O7 . NDG C 3 . ? 10.920 -0.633 38.953 1.00 34.35 ? 364 NDG A O7 1 HETATM 2904 N N2 . NDG C 3 . ? 8.951 -1.821 38.651 1.00 29.19 ? 364 NDG A N2 1 HETATM 2905 C C1 . NAG D 2 . ? 11.643 -6.721 38.009 1.00 36.29 ? 365 NAG A C1 1 HETATM 2906 C C2 . NAG D 2 . ? 12.136 -8.036 38.567 1.00 32.44 ? 365 NAG A C2 1 HETATM 2907 C C3 . NAG D 2 . ? 13.520 -8.346 37.974 1.00 34.36 ? 365 NAG A C3 1 HETATM 2908 C C4 . NAG D 2 . ? 13.460 -8.116 36.397 1.00 33.00 ? 365 NAG A C4 1 HETATM 2909 C C5 . NAG D 2 . ? 12.841 -6.742 36.162 1.00 35.45 ? 365 NAG A C5 1 HETATM 2910 C C6 . NAG D 2 . ? 12.880 -6.045 34.764 1.00 35.04 ? 365 NAG A C6 1 HETATM 2911 C C7 . NAG D 2 . ? 12.198 -8.921 40.812 1.00 39.25 ? 365 NAG A C7 1 HETATM 2912 C C8 . NAG D 2 . ? 12.903 -8.714 42.225 1.00 33.79 ? 365 NAG A C8 1 HETATM 2913 N N2 . NAG D 2 . ? 12.184 -7.895 39.978 1.00 34.30 ? 365 NAG A N2 1 HETATM 2914 O O3 . NAG D 2 . ? 13.926 -9.689 38.406 1.00 33.47 ? 365 NAG A O3 1 HETATM 2915 O O4 . NAG D 2 . ? 14.720 -7.988 35.816 1.00 33.90 ? 365 NAG A O4 1 HETATM 2916 O O5 . NAG D 2 . ? 11.490 -6.971 36.646 1.00 38.24 ? 365 NAG A O5 1 HETATM 2917 O O6 . NAG D 2 . ? 11.831 -6.387 33.823 1.00 32.18 ? 365 NAG A O6 1 HETATM 2918 O O7 . NAG D 2 . ? 11.567 -9.942 40.370 1.00 39.42 ? 365 NAG A O7 1 HETATM 2919 C C1 . NAG E 2 . ? 15.405 -9.366 35.618 1.00 33.73 ? 366 NAG A C1 1 HETATM 2920 C C2 . NAG E 2 . ? 16.425 -8.793 34.619 1.00 33.52 ? 366 NAG A C2 1 HETATM 2921 C C3 . NAG E 2 . ? 17.350 -9.914 34.131 1.00 34.07 ? 366 NAG A C3 1 HETATM 2922 C C4 . NAG E 2 . ? 17.771 -10.806 35.351 1.00 37.42 ? 366 NAG A C4 1 HETATM 2923 C C5 . NAG E 2 . ? 16.693 -11.319 36.330 1.00 36.94 ? 366 NAG A C5 1 HETATM 2924 C C6 . NAG E 2 . ? 17.186 -12.166 37.464 1.00 38.35 ? 366 NAG A C6 1 HETATM 2925 C C7 . NAG E 2 . ? 15.358 -7.918 32.346 1.00 40.41 ? 366 NAG A C7 1 HETATM 2926 C C8 . NAG E 2 . ? 15.802 -8.986 31.339 1.00 38.95 ? 366 NAG A C8 1 HETATM 2927 N N2 . NAG E 2 . ? 15.772 -7.869 33.629 1.00 35.99 ? 366 NAG A N2 1 HETATM 2928 O O3 . NAG E 2 . ? 18.531 -9.406 33.405 1.00 36.38 ? 366 NAG A O3 1 HETATM 2929 O O4 . NAG E 2 . ? 18.161 -12.069 34.798 1.00 38.86 ? 366 NAG A O4 1 HETATM 2930 O O5 . NAG E 2 . ? 15.663 -10.397 36.605 1.00 35.50 ? 366 NAG A O5 1 HETATM 2931 O O6 . NAG E 2 . ? 17.307 -12.392 38.886 1.00 40.52 ? 366 NAG A O6 1 HETATM 2932 O O7 . NAG E 2 . ? 14.599 -6.923 31.970 1.00 43.30 ? 366 NAG A O7 1 HETATM 2933 C C1 . NAG F 2 . ? 19.549 -12.321 34.815 1.00 38.51 ? 367 NAG A C1 1 HETATM 2934 C C2 . NAG F 2 . ? 20.048 -13.563 35.517 1.00 39.36 ? 367 NAG A C2 1 HETATM 2935 C C3 . NAG F 2 . ? 21.604 -13.542 35.655 1.00 39.77 ? 367 NAG A C3 1 HETATM 2936 C C4 . NAG F 2 . ? 22.105 -13.552 34.196 1.00 42.04 ? 367 NAG A C4 1 HETATM 2937 C C5 . NAG F 2 . ? 21.178 -12.550 33.424 1.00 40.56 ? 367 NAG A C5 1 HETATM 2938 C C6 . NAG F 2 . ? 21.289 -12.604 31.898 1.00 43.53 ? 367 NAG A C6 1 HETATM 2939 C C7 . NAG F 2 . ? 18.864 -15.232 36.377 1.00 43.69 ? 367 NAG A C7 1 HETATM 2940 C C8 . NAG F 2 . ? 17.348 -15.231 36.118 1.00 43.70 ? 367 NAG A C8 1 HETATM 2941 N N2 . NAG F 2 . ? 19.269 -13.959 36.682 1.00 41.42 ? 367 NAG A N2 1 HETATM 2942 O O3 . NAG F 2 . ? 22.107 -14.684 36.380 1.00 37.12 ? 367 NAG A O3 1 HETATM 2943 O O4 . NAG F 2 . ? 23.534 -13.255 34.140 1.00 46.64 ? 367 NAG A O4 1 HETATM 2944 O O5 . NAG F 2 . ? 19.810 -12.947 33.611 1.00 36.90 ? 367 NAG A O5 1 HETATM 2945 O O6 . NAG F 2 . ? 20.242 -11.691 31.433 1.00 47.45 ? 367 NAG A O6 1 HETATM 2946 O O7 . NAG F 2 . ? 19.662 -16.257 36.184 1.00 35.11 ? 367 NAG A O7 1 HETATM 2947 C C1 . NAG G 2 . ? 13.275 -17.535 46.205 0.50 19.61 ? 368 NAG A C1 1 HETATM 2948 C C2 . NAG G 2 . ? 13.880 -18.153 44.936 0.50 19.38 ? 368 NAG A C2 1 HETATM 2949 C C3 . NAG G 2 . ? 13.140 -19.374 44.385 0.50 20.93 ? 368 NAG A C3 1 HETATM 2950 C C4 . NAG G 2 . ? 12.626 -20.331 45.449 0.50 20.05 ? 368 NAG A C4 1 HETATM 2951 C C5 . NAG G 2 . ? 11.978 -19.430 46.496 0.50 18.77 ? 368 NAG A C5 1 HETATM 2952 C C6 . NAG G 2 . ? 11.298 -20.235 47.565 0.50 17.09 ? 368 NAG A C6 1 HETATM 2953 C C7 . NAG G 2 . ? 15.135 -17.011 43.334 0.50 22.34 ? 368 NAG A C7 1 HETATM 2954 C C8 . NAG G 2 . ? 15.303 -16.072 42.167 0.50 22.18 ? 368 NAG A C8 1 HETATM 2955 N N2 . NAG G 2 . ? 13.933 -17.186 43.882 0.50 19.89 ? 368 NAG A N2 1 HETATM 2956 O O3 . NAG G 2 . ? 13.971 -20.121 43.554 0.50 21.23 ? 368 NAG A O3 1 HETATM 2957 O O4 . NAG G 2 . ? 11.569 -21.148 44.946 0.50 20.10 ? 368 NAG A O4 1 HETATM 2958 O O5 . NAG G 2 . ? 12.961 -18.606 47.064 0.50 18.01 ? 368 NAG A O5 1 HETATM 2959 O O6 . NAG G 2 . ? 12.368 -20.872 48.192 0.50 17.79 ? 368 NAG A O6 1 HETATM 2960 O O7 . NAG G 2 . ? 16.120 -17.593 43.784 0.50 23.99 ? 368 NAG A O7 1 HETATM 2961 C C1 . NDG H 3 . ? 11.446 -22.408 44.174 0.50 23.22 ? 369 NDG A C1 1 HETATM 2962 C C2 . NDG H 3 . ? 9.951 -22.847 44.175 0.50 23.99 ? 369 NDG A C2 1 HETATM 2963 C C3 . NDG H 3 . ? 9.745 -24.102 43.319 0.50 26.18 ? 369 NDG A C3 1 HETATM 2964 C C4 . NDG H 3 . ? 10.962 -24.720 42.665 0.50 25.27 ? 369 NDG A C4 1 HETATM 2965 C C5 . NDG H 3 . ? 12.194 -24.689 43.528 0.50 26.00 ? 369 NDG A C5 1 HETATM 2966 C C6 . NDG H 3 . ? 13.387 -24.891 42.583 0.50 26.32 ? 369 NDG A C6 1 HETATM 2967 C C7 . NDG H 3 . ? 7.952 -22.073 45.346 0.50 23.90 ? 369 NDG A C7 1 HETATM 2968 C C8 . NDG H 3 . ? 7.728 -20.975 44.330 0.50 26.00 ? 369 NDG A C8 1 HETATM 2969 O O . NDG H 3 . ? 12.300 -23.519 44.385 0.50 27.77 ? 369 NDG A O 1 HETATM 2970 O O3 . NDG H 3 . ? 8.989 -23.650 42.201 0.50 31.01 ? 369 NDG A O3 1 HETATM 2971 O O4 . NDG H 3 . ? 10.733 -26.057 42.357 0.50 25.19 ? 369 NDG A O4 1 HETATM 2972 O O6 . NDG H 3 . ? 13.406 -23.853 41.600 0.50 30.32 ? 369 NDG A O6 1 HETATM 2973 O O7 . NDG H 3 . ? 7.058 -22.256 46.169 0.50 26.89 ? 369 NDG A O7 1 HETATM 2974 N N2 . NDG H 3 . ? 9.089 -22.791 45.350 0.50 22.76 ? 369 NDG A N2 1 HETATM 2975 O O . HOH I 4 . ? 18.234 15.571 54.614 1.00 27.67 ? 370 HOH A O 1 HETATM 2976 O O . HOH I 4 . ? 10.599 1.497 53.646 1.00 32.05 ? 371 HOH A O 1 HETATM 2977 O O . HOH I 4 . ? 21.835 7.355 33.137 1.00 34.81 ? 372 HOH A O 1 HETATM 2978 O O . HOH I 4 . ? 24.331 3.132 26.809 1.00 12.09 ? 373 HOH A O 1 HETATM 2979 O O . HOH I 4 . ? 30.230 1.499 39.119 1.00 48.17 ? 374 HOH A O 1 HETATM 2980 O O . HOH I 4 . ? 29.842 -4.392 42.078 1.00 20.76 ? 375 HOH A O 1 HETATM 2981 O O . HOH I 4 . ? 24.436 15.483 46.907 1.00 32.85 ? 376 HOH A O 1 HETATM 2982 O O . HOH I 4 . ? 23.932 10.841 54.676 1.00 23.30 ? 377 HOH A O 1 HETATM 2983 O O . HOH I 4 . ? 18.382 6.694 61.947 1.00 17.07 ? 378 HOH A O 1 HETATM 2984 O O . HOH I 4 . ? -0.986 -9.755 42.980 1.00 67.08 ? 379 HOH A O 1 HETATM 2985 O O . HOH I 4 . ? 14.003 18.245 35.053 1.00 27.82 ? 380 HOH A O 1 HETATM 2986 O O . HOH I 4 . ? 28.819 -9.797 52.145 1.00 41.11 ? 381 HOH A O 1 HETATM 2987 O O . HOH I 4 . ? 5.053 -8.998 48.515 1.00 27.94 ? 382 HOH A O 1 HETATM 2988 O O . HOH I 4 . ? 1.897 12.567 64.938 1.00 45.56 ? 383 HOH A O 1 HETATM 2989 O O . HOH I 4 . ? 32.377 6.546 56.611 1.00 58.96 ? 384 HOH A O 1 HETATM 2990 O O . HOH I 4 . ? 6.493 -23.920 66.051 1.00 55.00 ? 385 HOH A O 1 HETATM 2991 O O . HOH I 4 . ? 16.447 -13.554 71.469 1.00 37.39 ? 386 HOH A O 1 HETATM 2992 O O . HOH I 4 . ? 0.322 2.552 46.196 1.00 34.61 ? 387 HOH A O 1 HETATM 2993 O O . HOH I 4 . ? 18.963 -5.381 66.968 1.00 9.66 ? 388 HOH A O 1 HETATM 2994 O O . HOH I 4 . ? -14.875 14.004 36.866 1.00 49.51 ? 389 HOH A O 1 HETATM 2995 O O . HOH I 4 . ? 2.530 -4.576 72.808 1.00 42.50 ? 390 HOH A O 1 HETATM 2996 O O . HOH I 4 . ? 14.831 -5.735 76.190 1.00 48.38 ? 391 HOH A O 1 HETATM 2997 O O . HOH I 4 . ? 5.660 9.470 66.835 1.00 27.80 ? 392 HOH A O 1 HETATM 2998 O O . HOH I 4 . ? 4.614 11.131 44.518 1.00 15.74 ? 393 HOH A O 1 HETATM 2999 O O . HOH I 4 . ? 6.292 9.908 38.026 1.00 5.56 ? 394 HOH A O 1 HETATM 3000 O O . HOH I 4 . ? 2.787 22.511 38.574 1.00 25.94 ? 395 HOH A O 1 HETATM 3001 O O . HOH I 4 . ? -3.455 18.189 26.280 1.00 42.89 ? 396 HOH A O 1 HETATM 3002 O O . HOH I 4 . ? 13.706 4.931 25.235 1.00 26.74 ? 397 HOH A O 1 HETATM 3003 O O . HOH I 4 . ? 3.505 22.447 48.285 1.00 41.06 ? 398 HOH A O 1 HETATM 3004 O O . HOH I 4 . ? -0.294 18.223 59.604 1.00 51.39 ? 399 HOH A O 1 HETATM 3005 O O . HOH I 4 . ? 35.993 8.640 48.149 1.00 56.19 ? 400 HOH A O 1 HETATM 3006 O O . HOH I 4 . ? -12.342 4.620 57.606 1.00 36.75 ? 401 HOH A O 1 HETATM 3007 O O . HOH I 4 . ? 0.267 -2.652 70.037 1.00 49.69 ? 402 HOH A O 1 HETATM 3008 O O . HOH I 4 . ? -9.994 22.669 38.256 1.00 50.70 ? 403 HOH A O 1 HETATM 3009 O O . HOH I 4 . ? 11.182 9.071 66.111 1.00 15.24 ? 404 HOH A O 1 HETATM 3010 O O . HOH I 4 . ? -1.330 11.611 63.714 1.00 42.14 ? 405 HOH A O 1 HETATM 3011 O O . HOH I 4 . ? 33.234 0.907 27.900 1.00 57.22 ? 406 HOH A O 1 HETATM 3012 O O . HOH I 4 . ? 20.900 -14.226 38.959 1.00 81.70 ? 407 HOH A O 1 HETATM 3013 O O . HOH I 4 . ? 21.961 20.994 49.811 1.00 61.00 ? 408 HOH A O 1 HETATM 3014 O O . HOH I 4 . ? 30.661 4.665 38.167 1.00 48.57 ? 409 HOH A O 1 HETATM 3015 O O . HOH I 4 . ? 33.345 3.993 41.586 1.00 40.51 ? 410 HOH A O 1 HETATM 3016 O O . HOH I 4 . ? 17.281 9.792 61.108 1.00 49.88 ? 411 HOH A O 1 HETATM 3017 O O . HOH I 4 . ? 11.668 -22.882 50.253 1.00 54.33 ? 412 HOH A O 1 HETATM 3018 O O . HOH I 4 . ? 33.071 -3.558 53.914 1.00 53.36 ? 413 HOH A O 1 HETATM 3019 O O . HOH I 4 . ? 29.883 -4.040 54.017 1.00 41.86 ? 414 HOH A O 1 HETATM 3020 O O . HOH I 4 . ? 1.310 16.818 61.135 1.00 33.65 ? 415 HOH A O 1 HETATM 3021 O O . HOH I 4 . ? 19.314 0.822 20.913 1.00 48.43 ? 416 HOH A O 1 HETATM 3022 O O . HOH I 4 . ? -7.884 -14.703 58.698 1.00 51.29 ? 417 HOH A O 1 HETATM 3023 O O . HOH I 4 . ? 18.579 18.051 27.172 1.00 40.52 ? 418 HOH A O 1 HETATM 3024 O O . HOH I 4 . ? -5.552 -1.612 67.236 1.00 53.84 ? 419 HOH A O 1 HETATM 3025 O O . HOH I 4 . ? 7.582 -5.945 70.102 1.00 29.58 ? 420 HOH A O 1 HETATM 3026 O O . HOH I 4 . ? -4.433 21.819 33.869 1.00 43.31 ? 421 HOH A O 1 HETATM 3027 O O . HOH I 4 . ? 19.570 -0.671 22.582 1.00 78.86 ? 422 HOH A O 1 HETATM 3028 O O . HOH I 4 . ? 12.034 19.812 21.292 1.00 25.02 ? 423 HOH A O 1 HETATM 3029 O O . HOH I 4 . ? 20.184 24.665 48.151 1.00 42.15 ? 424 HOH A O 1 HETATM 3030 O O . HOH I 4 . ? 18.764 25.130 50.479 1.00 58.43 ? 425 HOH A O 1 HETATM 3031 O O . HOH I 4 . ? -3.305 -7.807 71.998 1.00 38.36 ? 426 HOH A O 1 HETATM 3032 O O . HOH I 4 . ? -3.165 2.202 34.548 1.00 48.76 ? 427 HOH A O 1 HETATM 3033 O O . HOH I 4 . ? 30.375 -12.748 43.081 1.00 37.61 ? 428 HOH A O 1 HETATM 3034 O O . HOH I 4 . ? -2.203 -8.689 45.827 1.00 66.48 ? 429 HOH A O 1 HETATM 3035 O O . HOH I 4 . ? 32.989 -1.072 30.577 1.00 26.18 ? 430 HOH A O 1 HETATM 3036 O O . HOH I 4 . ? 15.775 20.710 28.901 1.00 44.77 ? 431 HOH A O 1 HETATM 3037 O O . HOH I 4 . ? 14.720 17.937 30.618 1.00 30.33 ? 432 HOH A O 1 HETATM 3038 O O . HOH I 4 . ? -6.362 -9.147 72.203 1.00 47.24 ? 433 HOH A O 1 HETATM 3039 O O . HOH I 4 . ? 11.393 -16.580 43.073 1.00 52.42 ? 434 HOH A O 1 HETATM 3040 O O . HOH I 4 . ? 23.147 -0.880 62.958 1.00 52.03 ? 435 HOH A O 1 HETATM 3041 O O . HOH I 4 . ? 15.930 13.767 61.636 1.00 67.81 ? 436 HOH A O 1 HETATM 3042 O O . HOH I 4 . ? 15.710 -19.497 60.766 1.00 52.31 ? 437 HOH A O 1 HETATM 3043 O O . HOH I 4 . ? -5.219 6.452 66.280 1.00 52.02 ? 438 HOH A O 1 HETATM 3044 O O . HOH I 4 . ? 6.734 2.063 28.336 1.00 31.18 ? 439 HOH A O 1 HETATM 3045 O O . HOH I 4 . ? 7.409 -5.834 29.782 1.00 66.95 ? 440 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 TYR 1 1 1 TYR TYR A . n A 1 2 LYS 2 2 2 LYS LYS A . n A 1 3 LEU 3 3 3 LEU LEU A . n A 1 4 ILE 4 4 4 ILE ILE A . n A 1 5 CYS 5 5 5 CYS CYS A . n A 1 6 TYR 6 6 6 TYR TYR A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 THR 8 8 8 THR THR A . n A 1 9 SER 9 9 9 SER SER A . n A 1 10 TRP 10 10 10 TRP TRP A . n A 1 11 SER 11 11 11 SER SER A . n A 1 12 GLN 12 12 12 GLN GLN A . n A 1 13 TYR 13 13 13 TYR TYR A . n A 1 14 ARG 14 14 14 ARG ARG A . n A 1 15 GLU 15 15 15 GLU GLU A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 GLY 18 18 18 GLY GLY A . n A 1 19 SER 19 19 19 SER SER A . n A 1 20 CYS 20 20 20 CYS CYS A . n A 1 21 PHE 21 21 21 PHE PHE A . n A 1 22 PRO 22 22 22 PRO PRO A . n A 1 23 ASP 23 23 23 ASP ASP A . n A 1 24 ALA 24 24 24 ALA ALA A . n A 1 25 ILE 25 25 25 ILE ILE A . n A 1 26 ASP 26 26 26 ASP ASP A . n A 1 27 PRO 27 27 27 PRO PRO A . n A 1 28 PHE 28 28 28 PHE PHE A . n A 1 29 LEU 29 29 29 LEU LEU A . n A 1 30 CYS 30 30 30 CYS CYS A . n A 1 31 THR 31 31 31 THR THR A . n A 1 32 HIS 32 32 32 HIS HIS A . n A 1 33 VAL 33 33 33 VAL VAL A . n A 1 34 ILE 34 34 34 ILE ILE A . n A 1 35 TYR 35 35 35 TYR TYR A . n A 1 36 SER 36 36 36 SER SER A . n A 1 37 PHE 37 37 37 PHE PHE A . n A 1 38 ALA 38 38 38 ALA ALA A . n A 1 39 ASN 39 39 39 ASN ASN A . n A 1 40 ILE 40 40 40 ILE ILE A . n A 1 41 SER 41 41 41 SER SER A . n A 1 42 ASN 42 42 42 ASN ASN A . n A 1 43 ASN 43 43 43 ASN ASN A . n A 1 44 GLU 44 44 44 GLU GLU A . n A 1 45 ILE 45 45 45 ILE ILE A . n A 1 46 ASP 46 46 46 ASP ASP A . n A 1 47 THR 47 47 47 THR THR A . n A 1 48 TRP 48 48 48 TRP TRP A . n A 1 49 GLU 49 49 49 GLU GLU A . n A 1 50 TRP 50 50 50 TRP TRP A . n A 1 51 ASN 51 51 51 ASN ASN A . n A 1 52 ASP 52 52 52 ASP ASP A . n A 1 53 VAL 53 53 53 VAL VAL A . n A 1 54 THR 54 54 54 THR THR A . n A 1 55 LEU 55 55 55 LEU LEU A . n A 1 56 TYR 56 56 56 TYR TYR A . n A 1 57 ASP 57 57 57 ASP ASP A . n A 1 58 THR 58 58 58 THR THR A . n A 1 59 LEU 59 59 59 LEU LEU A . n A 1 60 ASN 60 60 60 ASN ASN A . n A 1 61 THR 61 61 61 THR THR A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 LYS 63 63 63 LYS LYS A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 ARG 65 65 65 ARG ARG A . n A 1 66 ASN 66 66 66 ASN ASN A . n A 1 67 PRO 67 67 67 PRO PRO A . n A 1 68 LYS 68 68 68 LYS LYS A . n A 1 69 LEU 69 69 69 LEU LEU A . n A 1 70 LYS 70 70 70 LYS LYS A . n A 1 71 THR 71 71 71 THR THR A . n A 1 72 LEU 72 72 72 LEU LEU A . n A 1 73 LEU 73 73 73 LEU LEU A . n A 1 74 SER 74 74 74 SER SER A . n A 1 75 VAL 75 75 75 VAL VAL A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 GLY 77 77 77 GLY GLY A . n A 1 78 TRP 78 78 78 TRP TRP A . n A 1 79 ASN 79 79 79 ASN ASN A . n A 1 80 PHE 80 80 80 PHE PHE A . n A 1 81 GLY 81 81 81 GLY GLY A . n A 1 82 PRO 82 82 82 PRO PRO A . n A 1 83 GLU 83 83 83 GLU GLU A . n A 1 84 ARG 84 84 84 ARG ARG A . n A 1 85 PHE 85 85 85 PHE PHE A . n A 1 86 SER 86 86 86 SER SER A . n A 1 87 LYS 87 87 87 LYS LYS A . n A 1 88 ILE 88 88 88 ILE ILE A . n A 1 89 ALA 89 89 89 ALA ALA A . n A 1 90 SER 90 90 90 SER SER A . n A 1 91 LYS 91 91 91 LYS LYS A . n A 1 92 THR 92 92 92 THR THR A . n A 1 93 GLN 93 93 93 GLN GLN A . n A 1 94 SER 94 94 94 SER SER A . n A 1 95 ARG 95 95 95 ARG ARG A . n A 1 96 ARG 96 96 96 ARG ARG A . n A 1 97 THR 97 97 97 THR THR A . n A 1 98 PHE 98 98 98 PHE PHE A . n A 1 99 ILE 99 99 99 ILE ILE A . n A 1 100 LYS 100 100 100 LYS LYS A . n A 1 101 SER 101 101 101 SER SER A . n A 1 102 VAL 102 102 102 VAL VAL A . n A 1 103 PRO 103 103 103 PRO PRO A . n A 1 104 PRO 104 104 104 PRO PRO A . n A 1 105 PHE 105 105 105 PHE PHE A . n A 1 106 LEU 106 106 106 LEU LEU A . n A 1 107 ARG 107 107 107 ARG ARG A . n A 1 108 THR 108 108 108 THR THR A . n A 1 109 HIS 109 109 109 HIS HIS A . n A 1 110 GLY 110 110 110 GLY GLY A . n A 1 111 PHE 111 111 111 PHE PHE A . n A 1 112 ASP 112 112 112 ASP ASP A . n A 1 113 GLY 113 113 113 GLY GLY A . n A 1 114 LEU 114 114 114 LEU LEU A . n A 1 115 ASP 115 115 115 ASP ASP A . n A 1 116 LEU 116 116 116 LEU LEU A . n A 1 117 ALA 117 117 117 ALA ALA A . n A 1 118 TRP 118 118 118 TRP TRP A . n A 1 119 LEU 119 119 119 LEU LEU A . n A 1 120 TYR 120 120 120 TYR TYR A . n A 1 121 PRO 121 121 121 PRO PRO A . n A 1 122 GLY 122 122 122 GLY GLY A . n A 1 123 ARG 123 123 123 ARG ARG A . n A 1 124 ARG 124 124 124 ARG ARG A . n A 1 125 ASP 125 125 125 ASP ASP A . n A 1 126 LYS 126 126 126 LYS LYS A . n A 1 127 ARG 127 127 127 ARG ARG A . n A 1 128 HIS 128 128 128 HIS HIS A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 THR 130 130 130 THR THR A . n A 1 131 ALA 131 131 131 ALA ALA A . n A 1 132 LEU 132 132 132 LEU LEU A . n A 1 133 VAL 133 133 133 VAL VAL A . n A 1 134 LYS 134 134 134 LYS LYS A . n A 1 135 GLU 135 135 135 GLU GLU A . n A 1 136 MET 136 136 136 MET MET A . n A 1 137 LYS 137 137 137 LYS LYS A . n A 1 138 ALA 138 138 138 ALA ALA A . n A 1 139 GLU 139 139 139 GLU GLU A . n A 1 140 PHE 140 140 140 PHE PHE A . n A 1 141 ALA 141 141 141 ALA ALA A . n A 1 142 ARG 142 142 142 ARG ARG A . n A 1 143 GLU 143 143 143 GLU GLU A . n A 1 144 ALA 144 144 144 ALA ALA A . n A 1 145 GLN 145 145 145 GLN GLN A . n A 1 146 ALA 146 146 146 ALA ALA A . n A 1 147 GLY 147 147 147 GLY GLY A . n A 1 148 THR 148 148 148 THR THR A . n A 1 149 GLU 149 149 149 GLU GLU A . n A 1 150 ARG 150 150 150 ARG ARG A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 LEU 152 152 152 LEU LEU A . n A 1 153 LEU 153 153 153 LEU LEU A . n A 1 154 SER 154 154 154 SER SER A . n A 1 155 ALA 155 155 155 ALA ALA A . n A 1 156 ALA 156 156 156 ALA ALA A . n A 1 157 VAL 157 157 157 VAL VAL A . n A 1 158 SER 158 158 158 SER SER A . n A 1 159 ALA 159 159 159 ALA ALA A . n A 1 160 GLY 160 160 160 GLY GLY A . n A 1 161 LYS 161 161 161 LYS LYS A . n A 1 162 ILE 162 162 162 ILE ILE A . n A 1 163 ALA 163 163 163 ALA ALA A . n A 1 164 ILE 164 164 164 ILE ILE A . n A 1 165 ASP 165 165 165 ASP ASP A . n A 1 166 ARG 166 166 166 ARG ARG A . n A 1 167 GLY 167 167 167 GLY GLY A . n A 1 168 TYR 168 168 168 TYR TYR A . n A 1 169 ASP 169 169 169 ASP ASP A . n A 1 170 ILE 170 170 170 ILE ILE A . n A 1 171 ALA 171 171 171 ALA ALA A . n A 1 172 GLN 172 172 172 GLN GLN A . n A 1 173 ILE 173 173 173 ILE ILE A . n A 1 174 SER 174 174 174 SER SER A . n A 1 175 ARG 175 175 175 ARG ARG A . n A 1 176 HIS 176 176 176 HIS HIS A . n A 1 177 LEU 177 177 177 LEU LEU A . n A 1 178 ASP 178 178 178 ASP ASP A . n A 1 179 PHE 179 179 179 PHE PHE A . n A 1 180 ILE 180 180 180 ILE ILE A . n A 1 181 SER 181 181 181 SER SER A . n A 1 182 LEU 182 182 182 LEU LEU A . n A 1 183 LEU 183 183 183 LEU LEU A . n A 1 184 THR 184 184 184 THR THR A . n A 1 185 TYR 185 185 185 TYR TYR A . n A 1 186 ASP 186 186 186 ASP ASP A . n A 1 187 PHE 187 187 187 PHE PHE A . n A 1 188 HIS 188 188 188 HIS HIS A . n A 1 189 GLY 189 189 189 GLY GLY A . n A 1 190 ALA 190 190 190 ALA ALA A . n A 1 191 TRP 191 191 191 TRP TRP A . n A 1 192 ARG 192 192 192 ARG ARG A . n A 1 193 GLN 193 193 193 GLN GLN A . n A 1 194 THR 194 194 194 THR THR A . n A 1 195 VAL 195 195 195 VAL VAL A . n A 1 196 GLY 196 196 196 GLY GLY A . n A 1 197 HIS 197 197 197 HIS HIS A . n A 1 198 HIS 198 198 198 HIS HIS A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 PRO 200 200 200 PRO PRO A . n A 1 201 LEU 201 201 201 LEU LEU A . n A 1 202 PHE 202 202 202 PHE PHE A . n A 1 203 ARG 203 203 203 ARG ARG A . n A 1 204 GLY 204 204 204 GLY GLY A . n A 1 205 ASN 205 205 205 ASN ASN A . n A 1 206 SER 206 206 206 SER SER A . n A 1 207 ASP 207 207 207 ASP ASP A . n A 1 208 ALA 208 208 208 ALA ALA A . n A 1 209 SER 209 209 209 SER SER A . n A 1 210 SER 210 210 210 SER SER A . n A 1 211 ARG 211 212 212 ARG ARG A . n A 1 212 PHE 212 213 213 PHE PHE A . n A 1 213 SER 213 214 214 SER SER A . n A 1 214 ASN 214 215 215 ASN ASN A . n A 1 215 ALA 215 216 216 ALA ALA A . n A 1 216 ASP 216 217 217 ASP ASP A . n A 1 217 TYR 217 218 218 TYR TYR A . n A 1 218 ALA 218 219 219 ALA ALA A . n A 1 219 VAL 219 220 220 VAL VAL A . n A 1 220 SER 220 221 221 SER SER A . n A 1 221 TYR 221 222 222 TYR TYR A . n A 1 222 MET 222 223 223 MET MET A . n A 1 223 LEU 223 224 224 LEU LEU A . n A 1 224 ARG 224 225 225 ARG ARG A . n A 1 225 LEU 225 226 226 LEU LEU A . n A 1 226 GLY 226 227 227 GLY GLY A . n A 1 227 ALA 227 228 228 ALA ALA A . n A 1 228 PRO 228 229 229 PRO PRO A . n A 1 229 ALA 229 230 230 ALA ALA A . n A 1 230 ASN 230 231 231 ASN ASN A . n A 1 231 LYS 231 232 232 LYS LYS A . n A 1 232 LEU 232 233 233 LEU LEU A . n A 1 233 VAL 233 234 234 VAL VAL A . n A 1 234 MET 234 235 235 MET MET A . n A 1 235 GLY 235 236 236 GLY GLY A . n A 1 236 ILE 236 237 237 ILE ILE A . n A 1 237 PRO 237 238 238 PRO PRO A . n A 1 238 THR 238 239 239 THR THR A . n A 1 239 PHE 239 240 240 PHE PHE A . n A 1 240 GLY 240 241 241 GLY GLY A . n A 1 241 ARG 241 242 242 ARG ARG A . n A 1 242 SER 242 243 243 SER SER A . n A 1 243 PHE 243 244 244 PHE PHE A . n A 1 244 THR 244 245 245 THR THR A . n A 1 245 LEU 245 246 246 LEU LEU A . n A 1 246 ALA 246 247 247 ALA ALA A . n A 1 247 SER 247 248 248 SER SER A . n A 1 248 SER 248 249 249 SER SER A . n A 1 249 LYS 249 250 250 LYS LYS A . n A 1 250 THR 250 251 251 THR THR A . n A 1 251 ASP 251 252 252 ASP ASP A . n A 1 252 VAL 252 253 253 VAL VAL A . n A 1 253 GLY 253 254 254 GLY GLY A . n A 1 254 ALA 254 255 255 ALA ALA A . n A 1 255 PRO 255 256 256 PRO PRO A . n A 1 256 ILE 256 257 257 ILE ILE A . n A 1 257 SER 257 258 258 SER SER A . n A 1 258 GLY 258 259 259 GLY GLY A . n A 1 259 PRO 259 260 260 PRO PRO A . n A 1 260 GLY 260 261 261 GLY GLY A . n A 1 261 ILE 261 262 262 ILE ILE A . n A 1 262 PRO 262 263 263 PRO PRO A . n A 1 263 GLY 263 264 264 GLY GLY A . n A 1 264 ARG 264 265 265 ARG ARG A . n A 1 265 PHE 265 266 266 PHE PHE A . n A 1 266 THR 266 267 267 THR THR A . n A 1 267 LYS 267 268 268 LYS LYS A . n A 1 268 GLU 268 269 269 GLU GLU A . n A 1 269 LYS 269 270 270 LYS LYS A . n A 1 270 GLY 270 271 271 GLY GLY A . n A 1 271 ILE 271 272 272 ILE ILE A . n A 1 272 LEU 272 273 273 LEU LEU A . n A 1 273 ALA 273 274 274 ALA ALA A . n A 1 274 TYR 274 275 275 TYR TYR A . n A 1 275 TYR 275 276 276 TYR TYR A . n A 1 276 GLU 276 277 277 GLU GLU A . n A 1 277 ILE 277 278 278 ILE ILE A . n A 1 278 CYS 278 279 279 CYS CYS A . n A 1 279 ASP 279 280 280 ASP ASP A . n A 1 280 PHE 280 281 281 PHE PHE A . n A 1 281 LEU 281 282 282 LEU LEU A . n A 1 282 HIS 282 283 283 HIS HIS A . n A 1 283 GLY 283 284 284 GLY GLY A . n A 1 284 ALA 284 285 285 ALA ALA A . n A 1 285 THR 285 286 286 THR THR A . n A 1 286 THR 286 287 287 THR THR A . n A 1 287 HIS 287 288 288 HIS HIS A . n A 1 288 ARG 288 289 289 ARG ARG A . n A 1 289 PHE 289 290 290 PHE PHE A . n A 1 290 ARG 290 291 291 ARG ARG A . n A 1 291 ASP 291 292 292 ASP ASP A . n A 1 292 GLN 292 293 293 GLN GLN A . n A 1 293 GLN 293 294 294 GLN GLN A . n A 1 294 VAL 294 295 295 VAL VAL A . n A 1 295 PRO 295 296 296 PRO PRO A . n A 1 296 TYR 296 297 297 TYR TYR A . n A 1 297 ALA 297 298 298 ALA ALA A . n A 1 298 THR 298 299 299 THR THR A . n A 1 299 LYS 299 300 300 LYS LYS A . n A 1 300 GLY 300 301 301 GLY GLY A . n A 1 301 ASN 301 302 302 ASN ASN A . n A 1 302 GLN 302 303 303 GLN GLN A . n A 1 303 TRP 303 304 304 TRP TRP A . n A 1 304 VAL 304 305 305 VAL VAL A . n A 1 305 ALA 305 306 306 ALA ALA A . n A 1 306 TYR 306 307 307 TYR TYR A . n A 1 307 ASP 307 308 308 ASP ASP A . n A 1 308 ASP 308 309 309 ASP ASP A . n A 1 309 GLN 309 310 310 GLN GLN A . n A 1 310 GLU 310 311 311 GLU GLU A . n A 1 311 SER 311 312 312 SER SER A . n A 1 312 VAL 312 313 313 VAL VAL A . n A 1 313 LYS 313 314 314 LYS LYS A . n A 1 314 ASN 314 315 315 ASN ASN A . n A 1 315 LYS 315 316 316 LYS LYS A . n A 1 316 ALA 316 317 317 ALA ALA A . n A 1 317 ARG 317 318 318 ARG ARG A . n A 1 318 TYR 318 319 319 TYR TYR A . n A 1 319 LEU 319 320 320 LEU LEU A . n A 1 320 LYS 320 321 321 LYS LYS A . n A 1 321 ASN 321 322 322 ASN ASN A . n A 1 322 ARG 322 323 323 ARG ARG A . n A 1 323 GLN 323 324 324 GLN GLN A . n A 1 324 LEU 324 325 325 LEU LEU A . n A 1 325 ALA 325 326 326 ALA ALA A . n A 1 326 GLY 326 327 327 GLY GLY A . n A 1 327 ALA 327 328 328 ALA ALA A . n A 1 328 MET 328 329 329 MET MET A . n A 1 329 VAL 329 330 330 VAL VAL A . n A 1 330 TRP 330 331 331 TRP TRP A . n A 1 331 ALA 331 332 332 ALA ALA A . n A 1 332 LEU 332 333 333 LEU LEU A . n A 1 333 ASP 333 334 334 ASP ASP A . n A 1 334 LEU 334 335 335 LEU LEU A . n A 1 335 ASP 335 336 336 ASP ASP A . n A 1 336 ASP 336 337 337 ASP ASP A . n A 1 337 PHE 337 338 338 PHE PHE A . n A 1 338 ARG 338 339 339 ARG ARG A . n A 1 339 GLY 339 340 340 GLY GLY A . n A 1 340 THR 340 341 341 THR THR A . n A 1 341 PHE 341 342 342 PHE PHE A . n A 1 342 CYS 342 343 343 CYS CYS A . n A 1 343 GLY 343 344 344 GLY GLY A . n A 1 344 GLN 344 345 345 GLN GLN A . n A 1 345 ASN 345 346 346 ASN ASN A . n A 1 346 LEU 346 347 347 LEU LEU A . n A 1 347 THR 347 348 348 THR THR A . n A 1 348 PHE 348 349 349 PHE PHE A . n A 1 349 PRO 349 350 350 PRO PRO A . n A 1 350 LEU 350 351 351 LEU LEU A . n A 1 351 THR 351 352 352 THR THR A . n A 1 352 SER 352 353 353 SER SER A . n A 1 353 ALA 353 354 354 ALA ALA A . n A 1 354 VAL 354 355 355 VAL VAL A . n A 1 355 LYS 355 356 356 LYS LYS A . n A 1 356 ASP 356 357 357 ASP ASP A . n A 1 357 VAL 357 358 358 VAL VAL A . n A 1 358 LEU 358 359 359 LEU LEU A . n A 1 359 ALA 359 360 360 ALA ALA A . n A 1 360 ARG 360 361 361 ARG ARG A . n A 1 361 VAL 361 362 362 VAL VAL A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 363 1 NAG NAG A . C 3 NDG 2 364 2 NDG NAG A . D 2 NAG 3 365 3 NAG NAG A . E 2 NAG 4 366 4 NAG NAG A . F 2 NAG 5 367 5 NAG NAG A . G 2 NAG 1 368 1 NAG NAG A . H 3 NDG 2 369 2 NDG NAG A . I 4 HOH 1 370 1 HOH HOH A . I 4 HOH 2 371 2 HOH HOH A . I 4 HOH 3 372 3 HOH HOH A . I 4 HOH 4 373 4 HOH HOH A . I 4 HOH 5 374 5 HOH HOH A . I 4 HOH 6 375 6 HOH HOH A . I 4 HOH 7 376 7 HOH HOH A . I 4 HOH 8 377 8 HOH HOH A . I 4 HOH 9 378 9 HOH HOH A . I 4 HOH 10 379 10 HOH HOH A . I 4 HOH 11 380 11 HOH HOH A . I 4 HOH 12 381 12 HOH HOH A . I 4 HOH 13 382 13 HOH HOH A . I 4 HOH 14 383 14 HOH HOH A . I 4 HOH 15 384 15 HOH HOH A . I 4 HOH 16 385 16 HOH HOH A . I 4 HOH 17 386 17 HOH HOH A . I 4 HOH 18 387 18 HOH HOH A . I 4 HOH 19 388 19 HOH HOH A . I 4 HOH 20 389 20 HOH HOH A . I 4 HOH 21 390 21 HOH HOH A . I 4 HOH 22 391 22 HOH HOH A . I 4 HOH 23 392 23 HOH HOH A . I 4 HOH 24 393 24 HOH HOH A . I 4 HOH 25 394 25 HOH HOH A . I 4 HOH 26 395 26 HOH HOH A . I 4 HOH 27 396 27 HOH HOH A . I 4 HOH 28 397 28 HOH HOH A . I 4 HOH 29 398 29 HOH HOH A . I 4 HOH 30 399 30 HOH HOH A . I 4 HOH 31 400 31 HOH HOH A . I 4 HOH 32 401 32 HOH HOH A . I 4 HOH 33 402 33 HOH HOH A . I 4 HOH 34 403 34 HOH HOH A . I 4 HOH 35 404 35 HOH HOH A . I 4 HOH 36 405 36 HOH HOH A . I 4 HOH 37 406 37 HOH HOH A . I 4 HOH 38 407 38 HOH HOH A . I 4 HOH 39 408 39 HOH HOH A . I 4 HOH 40 409 40 HOH HOH A . I 4 HOH 41 410 41 HOH HOH A . I 4 HOH 42 411 42 HOH HOH A . I 4 HOH 43 412 43 HOH HOH A . I 4 HOH 44 413 44 HOH HOH A . I 4 HOH 45 414 46 HOH HOH A . I 4 HOH 46 415 47 HOH HOH A . I 4 HOH 47 416 48 HOH HOH A . I 4 HOH 48 417 49 HOH HOH A . I 4 HOH 49 418 50 HOH HOH A . I 4 HOH 50 419 51 HOH HOH A . I 4 HOH 51 420 52 HOH HOH A . I 4 HOH 52 421 53 HOH HOH A . I 4 HOH 53 422 54 HOH HOH A . I 4 HOH 54 423 55 HOH HOH A . I 4 HOH 55 424 56 HOH HOH A . I 4 HOH 56 425 57 HOH HOH A . I 4 HOH 57 426 58 HOH HOH A . I 4 HOH 58 427 59 HOH HOH A . I 4 HOH 59 428 60 HOH HOH A . I 4 HOH 60 429 61 HOH HOH A . I 4 HOH 61 430 62 HOH HOH A . I 4 HOH 62 431 63 HOH HOH A . I 4 HOH 63 432 64 HOH HOH A . I 4 HOH 64 433 65 HOH HOH A . I 4 HOH 65 434 66 HOH HOH A . I 4 HOH 66 435 67 HOH HOH A . I 4 HOH 67 436 68 HOH HOH A . I 4 HOH 68 437 69 HOH HOH A . I 4 HOH 69 438 70 HOH HOH A . I 4 HOH 70 439 71 HOH HOH A . I 4 HOH 71 440 72 HOH HOH A . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 39 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 39 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2005-09-27 2 'Structure model' 1 1 2008-05-01 3 'Structure model' 1 2 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.0 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 AMoRE phasing . ? 4 # _pdbx_database_remark.id 999 _pdbx_database_remark.text ;SEQUENCE The authors state that the aminoacid sequence in the database is incorrect for residues 54, 152, 226, 227 and 382. The authors state that residue 232 should be deleted from the sequence database reference. ; # 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 N A TRP 191 ? ? CA A TRP 191 ? ? CB A TRP 191 ? ? 99.75 110.60 -10.85 1.80 N 2 1 N A TRP 191 ? ? CA A TRP 191 ? ? C A TRP 191 ? ? 133.23 111.00 22.23 2.70 N 3 1 NE A ARG 323 ? ? CZ A ARG 323 ? ? NH1 A ARG 323 ? ? 123.92 120.30 3.62 0.50 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 LEU A 29 ? ? -68.86 -78.23 2 1 PHE A 37 ? ? 68.63 102.64 3 1 TRP A 48 ? ? -128.34 -57.60 4 1 ASN A 51 ? ? -97.86 31.46 5 1 LYS A 63 ? ? -67.95 0.47 6 1 ASN A 79 ? ? -73.15 27.70 7 1 ALA A 117 ? ? -113.87 53.61 8 1 TYR A 120 ? ? 81.99 97.45 9 1 ALA A 146 ? ? -68.83 13.87 10 1 ASP A 169 ? ? -112.47 72.84 11 1 TYR A 185 ? ? -157.54 -4.27 12 1 ALA A 190 ? ? 16.36 -53.43 13 1 TRP A 191 ? ? -46.15 -131.40 14 1 ARG A 192 ? ? -9.44 134.60 15 1 ASN A 205 ? ? -27.85 0.29 16 1 ASN A 215 ? ? 173.20 150.46 17 1 PRO A 260 ? ? -67.43 -179.16 18 1 LYS A 268 ? ? 38.59 64.02 19 1 PHE A 290 ? ? -59.19 109.94 20 1 LYS A 300 ? ? -162.03 117.06 21 1 ALA A 332 ? ? 66.79 102.97 22 1 GLN A 345 ? ? -36.41 153.34 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A VAL 362 ? O ? A VAL 361 O 2 1 N 1 A NAG 363 ? O1 ? B NAG 1 O1 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 '2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE' NDG 4 water HOH #