data_2DT1 # _entry.id 2DT1 # _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 2DT1 RCSB RCSB025810 WWPDB D_1000025810 # _pdbx_database_PDB_obs_spr.id SPRSDE _pdbx_database_PDB_obs_spr.date 2006-08-01 _pdbx_database_PDB_obs_spr.pdb_id 2DT1 _pdbx_database_PDB_obs_spr.replace_pdb_id 2B41 _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 2dpe . unspecified PDB 2esc . unspecified PDB 2dsz . unspecified PDB 2dt0 . unspecified PDB 2dt2 . unspecified PDB 2dt3 . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2DT1 _pdbx_database_status.recvd_initial_deposition_date 2006-07-09 _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Kumar, J.' 1 'Ethayathulla, A.S.' 2 'Srivastava, D.B.' 3 'Singh, N.' 4 'Sharma, S.' 5 'Bhushan, A.' 6 'Kaur, P.' 7 'Singh, T.P.' 8 # _citation.id primary _citation.title ;Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides ; _citation.journal_abbrev 'ACTA CRYSTALLOGR.,SECT.D' _citation.journal_volume 63 _citation.page_first 437 _citation.page_last 446 _citation.year 2007 _citation.journal_id_ASTM ABCRE6 _citation.country DK _citation.journal_id_ISSN 0907-4449 _citation.journal_id_CSD 0766 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 17372347 _citation.pdbx_database_id_DOI 10.1107/S0907444907001631 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Kumar, J.' 1 primary 'Ethayathulla, A.S.' 2 primary 'Srivastava, D.B.' 3 primary 'Singh, N.' 4 primary 'Sharma, S.' 5 primary 'Kaur, P.' 6 primary 'Srinivasan, A.' 7 primary 'Singh, T.P.' 8 # _cell.entry_id 2DT1 _cell.length_a 62.720 _cell.length_b 66.520 _cell.length_c 107.643 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 2DT1 _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' 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 1 ? ? ? ? 4 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 5 water nat water 18.015 211 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'SPG-40, 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 'MILK 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 UNP _struct_ref.db_code CH3L1_CAPHI _struct_ref.pdbx_db_accession Q8SPQ0 _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 2DT1 _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 Q8SPQ0 _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 2DT1 VAL A 33 ? UNP Q8SPQ0 ILE 54 'SEE REMARK 999' 33 1 1 2DT1 ALA A 131 ? UNP Q8SPQ0 GLY 152 'SEE REMARK 999' 131 2 1 2DT1 ASN A 205 ? UNP Q8SPQ0 GLN 226 'SEE REMARK 999' 205 3 1 2DT1 SER A 206 ? UNP Q8SPQ0 GLU 227 'SEE REMARK 999' 206 4 1 2DT1 ? A ? ? UNP Q8SPQ0 ASP 232 'SEE REMARK 999' ? 5 1 2DT1 ARG A 360 ? UNP Q8SPQ0 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 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 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 2DT1 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.76 _exptl_crystal.density_percent_sol 55.36 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 298.0 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.8 _exptl_crystal_grow.pdbx_details '25MM TRIS HCL, 50MM NACL, 19% Ethanol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K' _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 2005-05-16 _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 ? _diffrn_source.pdbx_wavelength_list 1.5418 # _reflns.entry_id 2DT1 _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F 0.0 _reflns.d_resolution_low 56.0 _reflns.d_resolution_high 2.09 _reflns.number_obs 27743 _reflns.number_all ? _reflns.percent_possible_obs 99.4 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.06 _reflns.pdbx_netI_over_sigmaI 17.0 _reflns.B_iso_Wilson_estimate 16.3 _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 2.09 _reflns_shell.d_res_low 2.13 _reflns_shell.percent_possible_all 99.4 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.497 _reflns_shell.meanI_over_sigI_obs 3.0 _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 2DT1 _refine.ls_number_reflns_obs 27200 _refine.ls_number_reflns_all 27743 _refine.pdbx_ls_sigma_I 0.0 _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF 1740040.63 _refine.pdbx_data_cutoff_low_absF 0.000000 _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 56.0 _refine.ls_d_res_high 2.09 _refine.ls_percent_reflns_obs 99.3 _refine.ls_R_factor_obs 0.201 _refine.ls_R_factor_all 0.202 _refine.ls_R_factor_R_work 0.201 _refine.ls_R_factor_R_free 0.231 _refine.ls_R_factor_R_free_error 0.010 _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 2.0 _refine.ls_number_reflns_R_free 543 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 36.0 _refine.aniso_B[1][1] -0.46 _refine.aniso_B[2][2] -0.43 _refine.aniso_B[3][3] 0.89 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'FLAT MODEL' _refine.solvent_model_param_ksol 0.358848 _refine.solvent_model_param_bsol 72.4268 _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 1LJY _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model RESTRAINED _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _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_analyze.entry_id 2DT1 _refine_analyze.Luzzati_coordinate_error_obs 0.23 _refine_analyze.Luzzati_sigma_a_obs 0.17 _refine_analyze.Luzzati_d_res_low_obs 5.00 _refine_analyze.Luzzati_coordinate_error_free 0.26 _refine_analyze.Luzzati_sigma_a_free 0.20 _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? _refine_analyze.pdbx_Luzzati_d_res_high_obs ? _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2877 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 96 _refine_hist.number_atoms_solvent 211 _refine_hist.number_atoms_total 3184 _refine_hist.d_res_high 2.09 _refine_hist.d_res_low 56.0 # 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 c_bond_d 0.007 ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_bond_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg 1.4 ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_angle_deg_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d 24.4 ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_dihedral_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d 0.79 ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_na ? ? ? ? 'X-RAY DIFFRACTION' ? c_improper_angle_d_prot ? ? ? ? 'X-RAY DIFFRACTION' ? c_mcbond_it 1.81 1.50 ? ? 'X-RAY DIFFRACTION' ? c_mcangle_it 2.88 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scbond_it 2.55 2.00 ? ? 'X-RAY DIFFRACTION' ? c_scangle_it 3.88 2.50 ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 6 _refine_ls_shell.d_res_high 2.09 _refine_ls_shell.d_res_low 2.22 _refine_ls_shell.number_reflns_R_work 4385 _refine_ls_shell.R_factor_R_work 0.231 _refine_ls_shell.percent_reflns_obs 99.6 _refine_ls_shell.R_factor_R_free 0.269 _refine_ls_shell.R_factor_R_free_error 0.028 _refine_ls_shell.percent_reflns_R_free 2.1 _refine_ls_shell.number_reflns_R_free 95 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # loop_ _pdbx_xplor_file.serial_no _pdbx_xplor_file.param_file _pdbx_xplor_file.topol_file _pdbx_xplor_file.pdbx_refine_id 1 protein_rep.param protein.top 'X-RAY DIFFRACTION' 2 water.param water.top 'X-RAY DIFFRACTION' 3 carbohydrate.param carbohydrate.top 'X-RAY DIFFRACTION' 4 cis_peptide.param cis_peptide.top 'X-RAY DIFFRACTION' # _struct.entry_id 2DT1 _struct.title 'Crystal Structure Of The Complex Of Goat Signalling Protein With Tetrasaccharide At 2.09 A Resolution' _struct.pdbx_descriptor 'Chitinase-3-like protein 1' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2DT1 _struct_keywords.pdbx_keywords 'SIGNALING PROTEIN' _struct_keywords.text 'SPG-40, TETRASACCHARIDE, 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 4 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 5 ? # _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 ? THR A 61 ? ASN A 51 THR A 61 1 ? 11 HELX_P HELX_P5 5 LEU A 62 ? ARG A 65 ? LEU A 62 ARG A 65 5 ? 4 HELX_P HELX_P6 6 GLY A 81 ? LYS A 91 ? GLY A 81 LYS A 91 1 ? 11 HELX_P HELX_P7 7 LYS A 91 ? GLY A 110 ? LYS A 91 GLY A 110 1 ? 20 HELX_P HELX_P8 8 ASP A 125 ? ALA A 144 ? ASP A 125 ALA A 144 1 ? 20 HELX_P HELX_P9 9 GLN A 145 ? GLY A 147 ? GLN A 145 GLY A 147 5 ? 3 HELX_P HELX_P10 10 GLY A 160 ? TYR A 168 ? GLY A 160 TYR A 168 1 ? 9 HELX_P HELX_P11 11 ASP A 169 ? ARG A 175 ? ASP A 169 ARG A 175 1 ? 7 HELX_P HELX_P12 12 ASN A 214 ? GLY A 226 ? ASN A 215 GLY A 227 1 ? 13 HELX_P HELX_P13 13 PRO A 228 ? ASN A 230 ? PRO A 229 ASN A 231 5 ? 3 HELX_P HELX_P14 14 TYR A 274 ? LEU A 281 ? TYR A 275 LEU A 282 1 ? 8 HELX_P HELX_P15 15 ASP A 308 ? ARG A 322 ? ASP A 309 ARG A 323 1 ? 15 HELX_P HELX_P16 16 ALA A 331 ? ASP A 335 ? ALA A 332 ASP A 336 5 ? 5 HELX_P HELX_P17 17 PHE A 348 ? ARG A 360 ? PHE A 349 ARG A 361 1 ? 13 # _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 ? ? ? ? ? ? ? 2.031 ? disulf2 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 342 SG ? ? A CYS 279 A CYS 343 1_555 ? ? ? ? ? ? ? 2.024 ? covale1 covale ? ? A ASN 39 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 39 A NAG 363 1_555 ? ? ? ? ? ? ? 1.452 ? covale2 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 366 A NAG 367 1_555 ? ? ? ? ? ? ? 1.377 ? covale3 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 367 A NAG 368 1_555 ? ? ? ? ? ? ? 1.391 ? covale4 covale ? ? G NAG . O4 ? ? ? 1_555 H NAG . C1 ? ? A NAG 368 A NAG 369 1_555 ? ? ? ? ? ? ? 1.389 ? covale5 covale ? ? B NAG . O4 ? ? ? 1_555 C NDG . C1 ? ? A NAG 363 A NDG 364 1_555 ? ? ? ? ? ? ? 1.388 ? covale6 covale ? ? C NDG . O4 ? ? ? 1_555 D BMA . C1 ? ? A NDG 364 A BMA 365 1_555 ? ? ? ? ? ? ? 1.467 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 SER 36 A . ? SER 36 A PHE 37 A ? PHE 37 A 1 0.07 2 LEU 119 A . ? LEU 119 A TYR 120 A ? TYR 120 A 1 0.42 3 TRP 330 A . ? TRP 331 A ALA 331 A ? ALA 332 A 1 0.01 # 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 GLU A 44 ? O GLU A 44 N SER A 41 ? N SER A 41 A 2 3 N ALA A 38 ? N ALA A 38 O SER A 74 ? O SER A 74 A 3 4 N LEU A 73 ? N LEU A 73 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 VAL A 157 ? N VAL A 157 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 GLY A 258 ? O GLY A 259 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 GLY A 258 ? O GLY A 259 N THR A 244 ? N THR A 245 C 2 3 N PHE A 243 ? N PHE A 244 O TRP A 303 ? O TRP A 304 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 ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 363' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NDG A 364' AC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE BMA A 365' AC4 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 366' AC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 367' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 368' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG 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 6 ASN A 39 ? ASN A 39 . ? 1_555 ? 2 AC1 6 ILE A 40 ? ILE A 40 . ? 1_555 ? 3 AC1 6 SER A 41 ? SER A 41 . ? 1_555 ? 4 AC1 6 ARG A 84 ? ARG A 84 . ? 1_555 ? 5 AC1 6 NDG C . ? NDG A 364 . ? 1_555 ? 6 AC1 6 HOH I . ? HOH A 459 . ? 1_555 ? 7 AC2 2 NAG B . ? NAG A 363 . ? 1_555 ? 8 AC2 2 BMA D . ? BMA A 365 . ? 1_555 ? 9 AC3 1 NDG C . ? NDG A 364 . ? 1_555 ? 10 AC4 9 TRP A 10 ? TRP A 10 . ? 1_555 ? 11 AC4 9 PHE A 37 ? PHE A 37 . ? 1_555 ? 12 AC4 9 GLY A 77 ? GLY A 77 . ? 1_555 ? 13 AC4 9 TRP A 78 ? TRP A 78 . ? 1_555 ? 14 AC4 9 ASN A 79 ? ASN A 79 . ? 1_555 ? 15 AC4 9 GLU A 268 ? GLU A 269 . ? 1_555 ? 16 AC4 9 TRP A 330 ? TRP A 331 . ? 1_555 ? 17 AC4 9 NAG F . ? NAG A 367 . ? 1_555 ? 18 AC4 9 HOH I . ? HOH A 434 . ? 1_555 ? 19 AC5 8 TRP A 10 ? TRP A 10 . ? 1_555 ? 20 AC5 8 TRP A 48 ? TRP A 48 . ? 1_555 ? 21 AC5 8 ASN A 79 ? ASN A 79 . ? 1_555 ? 22 AC5 8 GLU A 268 ? GLU A 269 . ? 1_555 ? 23 AC5 8 NAG E . ? NAG A 366 . ? 1_555 ? 24 AC5 8 NAG G . ? NAG A 368 . ? 1_555 ? 25 AC5 8 HOH I . ? HOH A 372 . ? 1_555 ? 26 AC5 8 HOH I . ? HOH A 550 . ? 1_555 ? 27 AC6 5 TRP A 10 ? TRP A 10 . ? 1_555 ? 28 AC6 5 TYR A 13 ? TYR A 13 . ? 1_555 ? 29 AC6 5 GLU A 49 ? GLU A 49 . ? 1_555 ? 30 AC6 5 NAG F . ? NAG A 367 . ? 1_555 ? 31 AC6 5 NAG H . ? NAG A 369 . ? 1_555 ? 32 AC7 4 GLU A 49 ? GLU A 49 . ? 1_555 ? 33 AC7 4 TRP A 50 ? TRP A 50 . ? 1_555 ? 34 AC7 4 NAG G . ? NAG A 368 . ? 1_555 ? 35 AC7 4 HOH I . ? HOH A 558 . ? 1_555 ? # _database_PDB_matrix.entry_id 2DT1 _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 2DT1 _atom_sites.fract_transf_matrix[1][1] 0.015944 _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] 0.015033 _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] 0.009290 _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 ? 15.627 15.720 58.560 1.00 32.97 ? 1 TYR A N 1 ATOM 2 C CA . TYR A 1 1 ? 14.706 14.903 57.716 1.00 32.36 ? 1 TYR A CA 1 ATOM 3 C C . TYR A 1 1 ? 15.406 13.659 57.177 1.00 31.20 ? 1 TYR A C 1 ATOM 4 O O . TYR A 1 1 ? 16.630 13.632 57.065 1.00 31.70 ? 1 TYR A O 1 ATOM 5 C CB . TYR A 1 1 ? 14.198 15.738 56.542 1.00 34.68 ? 1 TYR A CB 1 ATOM 6 C CG . TYR A 1 1 ? 13.245 16.838 56.944 1.00 35.18 ? 1 TYR A CG 1 ATOM 7 C CD1 . TYR A 1 1 ? 11.916 16.553 57.257 1.00 37.24 ? 1 TYR A CD1 1 ATOM 8 C CD2 . TYR A 1 1 ? 13.677 18.162 57.043 1.00 36.40 ? 1 TYR A CD2 1 ATOM 9 C CE1 . TYR A 1 1 ? 11.039 17.554 57.659 1.00 37.87 ? 1 TYR A CE1 1 ATOM 10 C CE2 . TYR A 1 1 ? 12.809 19.174 57.448 1.00 36.31 ? 1 TYR A CE2 1 ATOM 11 C CZ . TYR A 1 1 ? 11.491 18.863 57.755 1.00 39.33 ? 1 TYR A CZ 1 ATOM 12 O OH . TYR A 1 1 ? 10.620 19.852 58.163 1.00 40.95 ? 1 TYR A OH 1 ATOM 13 N N . LYS A 1 2 ? 14.634 12.627 56.849 1.00 26.15 ? 2 LYS A N 1 ATOM 14 C CA . LYS A 1 2 ? 15.217 11.406 56.309 1.00 25.45 ? 2 LYS A CA 1 ATOM 15 C C . LYS A 1 2 ? 15.024 11.409 54.799 1.00 21.38 ? 2 LYS A C 1 ATOM 16 O O . LYS A 1 2 ? 14.041 11.945 54.297 1.00 20.13 ? 2 LYS A O 1 ATOM 17 C CB . LYS A 1 2 ? 14.539 10.162 56.904 1.00 26.58 ? 2 LYS A CB 1 ATOM 18 C CG . LYS A 1 2 ? 14.751 9.943 58.402 1.00 30.69 ? 2 LYS A CG 1 ATOM 19 C CD . LYS A 1 2 ? 14.096 8.624 58.829 1.00 34.70 ? 2 LYS A CD 1 ATOM 20 C CE . LYS A 1 2 ? 14.376 8.291 60.289 1.00 35.85 ? 2 LYS A CE 1 ATOM 21 N NZ . LYS A 1 2 ? 13.710 9.227 61.242 1.00 37.35 ? 2 LYS A NZ 1 ATOM 22 N N . LEU A 1 3 ? 15.978 10.842 54.078 1.00 20.24 ? 3 LEU A N 1 ATOM 23 C CA . LEU A 1 3 ? 15.873 10.739 52.630 1.00 20.28 ? 3 LEU A CA 1 ATOM 24 C C . LEU A 1 3 ? 16.172 9.267 52.383 1.00 18.93 ? 3 LEU A C 1 ATOM 25 O O . LEU A 1 3 ? 17.334 8.856 52.359 1.00 16.44 ? 3 LEU A O 1 ATOM 26 C CB . LEU A 1 3 ? 16.904 11.620 51.918 1.00 20.93 ? 3 LEU A CB 1 ATOM 27 C CG . LEU A 1 3 ? 16.424 12.208 50.584 1.00 26.87 ? 3 LEU A CG 1 ATOM 28 C CD1 . LEU A 1 3 ? 17.607 12.778 49.822 1.00 25.12 ? 3 LEU A CD1 1 ATOM 29 C CD2 . LEU A 1 3 ? 15.721 11.164 49.747 1.00 22.11 ? 3 LEU A CD2 1 ATOM 30 N N . ILE A 1 4 ? 15.109 8.479 52.234 1.00 16.63 ? 4 ILE A N 1 ATOM 31 C CA . ILE A 1 4 ? 15.211 7.038 52.028 1.00 17.73 ? 4 ILE A CA 1 ATOM 32 C C . ILE A 1 4 ? 15.277 6.709 50.541 1.00 17.54 ? 4 ILE A C 1 ATOM 33 O O . ILE A 1 4 ? 14.355 7.027 49.793 1.00 17.30 ? 4 ILE A O 1 ATOM 34 C CB . ILE A 1 4 ? 13.992 6.326 52.640 1.00 17.61 ? 4 ILE A CB 1 ATOM 35 C CG1 . ILE A 1 4 ? 13.719 6.873 54.052 1.00 21.02 ? 4 ILE A CG1 1 ATOM 36 C CG2 . ILE A 1 4 ? 14.236 4.819 52.678 1.00 18.90 ? 4 ILE A CG2 1 ATOM 37 C CD1 . ILE A 1 4 ? 14.793 6.535 55.083 1.00 21.80 ? 4 ILE A CD1 1 ATOM 38 N N . CYS A 1 5 ? 16.356 6.064 50.107 1.00 15.46 ? 5 CYS A N 1 ATOM 39 C CA . CYS A 1 5 ? 16.493 5.742 48.689 1.00 17.68 ? 5 CYS A CA 1 ATOM 40 C C . CYS A 1 5 ? 16.650 4.256 48.379 1.00 18.46 ? 5 CYS A C 1 ATOM 41 O O . CYS A 1 5 ? 17.490 3.576 48.959 1.00 17.74 ? 5 CYS A O 1 ATOM 42 C CB . CYS A 1 5 ? 17.685 6.498 48.103 1.00 18.43 ? 5 CYS A CB 1 ATOM 43 S SG . CYS A 1 5 ? 17.680 8.276 48.489 1.00 18.89 ? 5 CYS A SG 1 ATOM 44 N N . TYR A 1 6 ? 15.839 3.760 47.453 1.00 15.81 ? 6 TYR A N 1 ATOM 45 C CA . TYR A 1 6 ? 15.916 2.364 47.061 1.00 17.24 ? 6 TYR A CA 1 ATOM 46 C C . TYR A 1 6 ? 16.864 2.177 45.889 1.00 18.61 ? 6 TYR A C 1 ATOM 47 O O . TYR A 1 6 ? 16.975 3.041 45.017 1.00 15.69 ? 6 TYR A O 1 ATOM 48 C CB . TYR A 1 6 ? 14.551 1.827 46.636 1.00 14.59 ? 6 TYR A CB 1 ATOM 49 C CG . TYR A 1 6 ? 13.635 1.435 47.775 1.00 19.00 ? 6 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 6 ? 12.784 2.365 48.375 1.00 19.08 ? 6 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 6 ? 13.591 0.115 48.224 1.00 18.32 ? 6 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 6 ? 11.898 1.979 49.389 1.00 21.60 ? 6 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 6 ? 12.724 -0.277 49.238 1.00 19.08 ? 6 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 6 ? 11.873 0.659 49.813 1.00 20.47 ? 6 TYR A CZ 1 ATOM 55 O OH . TYR A 1 6 ? 10.984 0.260 50.788 1.00 23.76 ? 6 TYR A OH 1 ATOM 56 N N . TYR A 1 7 ? 17.545 1.039 45.889 1.00 18.72 ? 7 TYR A N 1 ATOM 57 C CA . TYR A 1 7 ? 18.447 0.660 44.810 1.00 20.78 ? 7 TYR A CA 1 ATOM 58 C C . TYR A 1 7 ? 17.969 -0.739 44.452 1.00 21.38 ? 7 TYR A C 1 ATOM 59 O O . TYR A 1 7 ? 17.820 -1.584 45.339 1.00 20.02 ? 7 TYR A O 1 ATOM 60 C CB . TYR A 1 7 ? 19.899 0.580 45.279 1.00 20.00 ? 7 TYR A CB 1 ATOM 61 C CG . TYR A 1 7 ? 20.761 -0.160 44.277 1.00 20.54 ? 7 TYR A CG 1 ATOM 62 C CD1 . TYR A 1 7 ? 21.096 0.418 43.052 1.00 21.85 ? 7 TYR A CD1 1 ATOM 63 C CD2 . TYR A 1 7 ? 21.159 -1.475 44.516 1.00 23.75 ? 7 TYR A CD2 1 ATOM 64 C CE1 . TYR A 1 7 ? 21.800 -0.299 42.080 1.00 24.32 ? 7 TYR A CE1 1 ATOM 65 C CE2 . TYR A 1 7 ? 21.860 -2.204 43.561 1.00 24.50 ? 7 TYR A CE2 1 ATOM 66 C CZ . TYR A 1 7 ? 22.177 -1.609 42.342 1.00 26.77 ? 7 TYR A CZ 1 ATOM 67 O OH . TYR A 1 7 ? 22.856 -2.328 41.384 1.00 27.73 ? 7 TYR A OH 1 ATOM 68 N N . THR A 1 8 ? 17.719 -0.997 43.173 1.00 19.79 ? 8 THR A N 1 ATOM 69 C CA . THR A 1 8 ? 17.234 -2.316 42.783 1.00 22.99 ? 8 THR A CA 1 ATOM 70 C C . THR A 1 8 ? 18.311 -3.203 42.159 1.00 24.91 ? 8 THR A C 1 ATOM 71 O O . THR A 1 8 ? 19.089 -2.766 41.308 1.00 24.34 ? 8 THR A O 1 ATOM 72 C CB . THR A 1 8 ? 16.037 -2.215 41.818 1.00 23.16 ? 8 THR A CB 1 ATOM 73 O OG1 . THR A 1 8 ? 16.475 -1.723 40.543 1.00 22.43 ? 8 THR A OG1 1 ATOM 74 C CG2 . THR A 1 8 ? 14.981 -1.272 42.399 1.00 23.72 ? 8 THR A CG2 1 ATOM 75 N N . SER A 1 9 ? 18.329 -4.455 42.603 1.00 24.13 ? 9 SER A N 1 ATOM 76 C CA . SER A 1 9 ? 19.288 -5.472 42.164 1.00 29.09 ? 9 SER A CA 1 ATOM 77 C C . SER A 1 9 ? 19.372 -5.746 40.669 1.00 29.20 ? 9 SER A C 1 ATOM 78 O O . SER A 1 9 ? 20.456 -5.964 40.125 1.00 31.05 ? 9 SER A O 1 ATOM 79 C CB . SER A 1 9 ? 18.975 -6.801 42.848 1.00 28.74 ? 9 SER A CB 1 ATOM 80 O OG . SER A 1 9 ? 19.850 -7.010 43.930 1.00 40.46 ? 9 SER A OG 1 ATOM 81 N N . TRP A 1 10 ? 18.221 -5.767 40.016 1.00 27.33 ? 10 TRP A N 1 ATOM 82 C CA . TRP A 1 10 ? 18.175 -6.065 38.595 1.00 29.22 ? 10 TRP A CA 1 ATOM 83 C C . TRP A 1 10 ? 18.647 -4.937 37.670 1.00 29.11 ? 10 TRP A C 1 ATOM 84 O O . TRP A 1 10 ? 18.783 -5.142 36.466 1.00 29.29 ? 10 TRP A O 1 ATOM 85 C CB . TRP A 1 10 ? 16.756 -6.527 38.227 1.00 27.31 ? 10 TRP A CB 1 ATOM 86 C CG . TRP A 1 10 ? 15.680 -5.490 38.411 1.00 29.35 ? 10 TRP A CG 1 ATOM 87 C CD1 . TRP A 1 10 ? 15.228 -4.609 37.471 1.00 31.84 ? 10 TRP A CD1 1 ATOM 88 C CD2 . TRP A 1 10 ? 14.923 -5.229 39.606 1.00 28.89 ? 10 TRP A CD2 1 ATOM 89 N NE1 . TRP A 1 10 ? 14.232 -3.819 38.002 1.00 31.71 ? 10 TRP A NE1 1 ATOM 90 C CE2 . TRP A 1 10 ? 14.025 -4.177 39.308 1.00 31.14 ? 10 TRP A CE2 1 ATOM 91 C CE3 . TRP A 1 10 ? 14.912 -5.784 40.897 1.00 29.18 ? 10 TRP A CE3 1 ATOM 92 C CZ2 . TRP A 1 10 ? 13.128 -3.660 40.258 1.00 30.05 ? 10 TRP A CZ2 1 ATOM 93 C CZ3 . TRP A 1 10 ? 14.018 -5.270 41.842 1.00 28.41 ? 10 TRP A CZ3 1 ATOM 94 C CH2 . TRP A 1 10 ? 13.137 -4.220 41.513 1.00 30.75 ? 10 TRP A CH2 1 ATOM 95 N N . SER A 1 11 ? 18.932 -3.758 38.220 1.00 27.28 ? 11 SER A N 1 ATOM 96 C CA . SER A 1 11 ? 19.378 -2.650 37.379 1.00 26.58 ? 11 SER A CA 1 ATOM 97 C C . SER A 1 11 ? 20.785 -2.878 36.833 1.00 27.69 ? 11 SER A C 1 ATOM 98 O O . SER A 1 11 ? 21.195 -2.231 35.864 1.00 26.65 ? 11 SER A O 1 ATOM 99 C CB . SER A 1 11 ? 19.336 -1.316 38.140 1.00 25.23 ? 11 SER A CB 1 ATOM 100 O OG . SER A 1 11 ? 20.248 -1.285 39.217 1.00 23.28 ? 11 SER A OG 1 ATOM 101 N N . GLN A 1 12 ? 21.523 -3.792 37.453 1.00 26.72 ? 12 GLN A N 1 ATOM 102 C CA . GLN A 1 12 ? 22.880 -4.093 37.010 1.00 29.39 ? 12 GLN A CA 1 ATOM 103 C C . GLN A 1 12 ? 22.903 -4.685 35.602 1.00 30.58 ? 12 GLN A C 1 ATOM 104 O O . GLN A 1 12 ? 23.896 -4.559 34.888 1.00 31.87 ? 12 GLN A O 1 ATOM 105 C CB . GLN A 1 12 ? 23.549 -5.085 37.971 1.00 28.61 ? 12 GLN A CB 1 ATOM 106 C CG . GLN A 1 12 ? 22.847 -6.441 38.063 1.00 27.68 ? 12 GLN A CG 1 ATOM 107 C CD . GLN A 1 12 ? 23.655 -7.470 38.846 1.00 31.01 ? 12 GLN A CD 1 ATOM 108 O OE1 . GLN A 1 12 ? 24.792 -7.783 38.490 1.00 32.37 ? 12 GLN A OE1 1 ATOM 109 N NE2 . GLN A 1 12 ? 23.072 -7.993 39.919 1.00 28.46 ? 12 GLN A NE2 1 ATOM 110 N N . TYR A 1 13 ? 21.805 -5.324 35.208 1.00 32.58 ? 13 TYR A N 1 ATOM 111 C CA . TYR A 1 13 ? 21.720 -5.983 33.901 1.00 35.47 ? 13 TYR A CA 1 ATOM 112 C C . TYR A 1 13 ? 21.318 -5.129 32.694 1.00 36.88 ? 13 TYR A C 1 ATOM 113 O O . TYR A 1 13 ? 21.329 -5.614 31.561 1.00 37.68 ? 13 TYR A O 1 ATOM 114 C CB . TYR A 1 13 ? 20.762 -7.174 33.979 1.00 35.36 ? 13 TYR A CB 1 ATOM 115 C CG . TYR A 1 13 ? 21.051 -8.150 35.101 1.00 37.97 ? 13 TYR A CG 1 ATOM 116 C CD1 . TYR A 1 13 ? 22.274 -8.817 35.181 1.00 38.21 ? 13 TYR A CD1 1 ATOM 117 C CD2 . TYR A 1 13 ? 20.087 -8.419 36.078 1.00 36.35 ? 13 TYR A CD2 1 ATOM 118 C CE1 . TYR A 1 13 ? 22.530 -9.728 36.207 1.00 38.60 ? 13 TYR A CE1 1 ATOM 119 C CE2 . TYR A 1 13 ? 20.331 -9.327 37.102 1.00 37.03 ? 13 TYR A CE2 1 ATOM 120 C CZ . TYR A 1 13 ? 21.553 -9.979 37.162 1.00 38.25 ? 13 TYR A CZ 1 ATOM 121 O OH . TYR A 1 13 ? 21.791 -10.889 38.169 1.00 39.28 ? 13 TYR A OH 1 ATOM 122 N N . ARG A 1 14 ? 20.957 -3.872 32.919 1.00 36.44 ? 14 ARG A N 1 ATOM 123 C CA . ARG A 1 14 ? 20.560 -3.012 31.810 1.00 36.72 ? 14 ARG A CA 1 ATOM 124 C C . ARG A 1 14 ? 21.755 -2.735 30.908 1.00 37.54 ? 14 ARG A C 1 ATOM 125 O O . ARG A 1 14 ? 22.875 -2.564 31.385 1.00 36.44 ? 14 ARG A O 1 ATOM 126 C CB . ARG A 1 14 ? 19.955 -1.717 32.355 1.00 34.42 ? 14 ARG A CB 1 ATOM 127 C CG . ARG A 1 14 ? 18.614 -1.974 33.016 1.00 30.98 ? 14 ARG A CG 1 ATOM 128 C CD . ARG A 1 14 ? 18.065 -0.782 33.763 1.00 29.31 ? 14 ARG A CD 1 ATOM 129 N NE . ARG A 1 14 ? 16.836 -1.160 34.453 1.00 27.51 ? 14 ARG A NE 1 ATOM 130 C CZ . ARG A 1 14 ? 16.427 -0.642 35.605 1.00 26.45 ? 14 ARG A CZ 1 ATOM 131 N NH1 . ARG A 1 14 ? 17.149 0.293 36.210 1.00 24.37 ? 14 ARG A NH1 1 ATOM 132 N NH2 . ARG A 1 14 ? 15.310 -1.090 36.162 1.00 23.50 ? 14 ARG A NH2 1 ATOM 133 N N . GLU A 1 15 ? 21.524 -2.699 29.601 1.00 40.02 ? 15 GLU A N 1 ATOM 134 C CA . GLU A 1 15 ? 22.630 -2.479 28.679 1.00 42.45 ? 15 GLU A CA 1 ATOM 135 C C . GLU A 1 15 ? 23.203 -1.071 28.651 1.00 41.52 ? 15 GLU A C 1 ATOM 136 O O . GLU A 1 15 ? 22.506 -0.087 28.901 1.00 40.59 ? 15 GLU A O 1 ATOM 137 C CB . GLU A 1 15 ? 22.252 -2.916 27.255 1.00 46.81 ? 15 GLU A CB 1 ATOM 138 C CG . GLU A 1 15 ? 20.917 -2.410 26.735 1.00 53.28 ? 15 GLU A CG 1 ATOM 139 C CD . GLU A 1 15 ? 20.712 -2.744 25.261 1.00 57.88 ? 15 GLU A CD 1 ATOM 140 O OE1 . GLU A 1 15 ? 20.754 -3.943 24.905 1.00 59.35 ? 15 GLU A OE1 1 ATOM 141 O OE2 . GLU A 1 15 ? 20.510 -1.806 24.458 1.00 60.67 ? 15 GLU A OE2 1 ATOM 142 N N . GLY A 1 16 ? 24.498 -1.001 28.359 1.00 41.33 ? 16 GLY A N 1 ATOM 143 C CA . GLY A 1 16 ? 25.196 0.268 28.277 1.00 40.69 ? 16 GLY A CA 1 ATOM 144 C C . GLY A 1 16 ? 25.139 1.147 29.511 1.00 40.04 ? 16 GLY A C 1 ATOM 145 O O . GLY A 1 16 ? 25.317 0.681 30.641 1.00 38.78 ? 16 GLY A O 1 ATOM 146 N N . ASP A 1 17 ? 24.894 2.433 29.276 1.00 40.27 ? 17 ASP A N 1 ATOM 147 C CA . ASP A 1 17 ? 24.815 3.428 30.339 1.00 40.93 ? 17 ASP A CA 1 ATOM 148 C C . ASP A 1 17 ? 23.718 3.133 31.359 1.00 39.11 ? 17 ASP A C 1 ATOM 149 O O . ASP A 1 17 ? 23.787 3.593 32.495 1.00 39.68 ? 17 ASP A O 1 ATOM 150 C CB . ASP A 1 17 ? 24.596 4.825 29.745 1.00 43.50 ? 17 ASP A CB 1 ATOM 151 C CG . ASP A 1 17 ? 25.823 5.354 29.030 1.00 47.29 ? 17 ASP A CG 1 ATOM 152 O OD1 . ASP A 1 17 ? 26.922 5.325 29.633 1.00 49.36 ? 17 ASP A OD1 1 ATOM 153 O OD2 . ASP A 1 17 ? 25.685 5.806 27.871 1.00 49.26 ? 17 ASP A OD2 1 ATOM 154 N N . GLY A 1 18 ? 22.713 2.364 30.955 1.00 35.72 ? 18 GLY A N 1 ATOM 155 C CA . GLY A 1 18 ? 21.628 2.037 31.863 1.00 35.72 ? 18 GLY A CA 1 ATOM 156 C C . GLY A 1 18 ? 22.069 1.165 33.024 1.00 35.42 ? 18 GLY A C 1 ATOM 157 O O . GLY A 1 18 ? 21.445 1.168 34.087 1.00 33.81 ? 18 GLY A O 1 ATOM 158 N N . SER A 1 19 ? 23.150 0.415 32.821 1.00 32.78 ? 19 SER A N 1 ATOM 159 C CA . SER A 1 19 ? 23.671 -0.469 33.857 1.00 32.06 ? 19 SER A CA 1 ATOM 160 C C . SER A 1 19 ? 24.045 0.344 35.090 1.00 28.80 ? 19 SER A C 1 ATOM 161 O O . SER A 1 19 ? 24.784 1.320 34.997 1.00 28.97 ? 19 SER A O 1 ATOM 162 C CB . SER A 1 19 ? 24.903 -1.222 33.337 1.00 32.09 ? 19 SER A CB 1 ATOM 163 O OG . SER A 1 19 ? 25.342 -2.194 34.268 1.00 37.23 ? 19 SER A OG 1 ATOM 164 N N . CYS A 1 20 ? 23.533 -0.064 36.246 1.00 28.53 ? 20 CYS A N 1 ATOM 165 C CA . CYS A 1 20 ? 23.816 0.643 37.495 1.00 26.68 ? 20 CYS A CA 1 ATOM 166 C C . CYS A 1 20 ? 24.251 -0.300 38.615 1.00 26.60 ? 20 CYS A C 1 ATOM 167 O O . CYS A 1 20 ? 23.552 -1.266 38.928 1.00 24.10 ? 20 CYS A O 1 ATOM 168 C CB . CYS A 1 20 ? 22.568 1.430 37.943 1.00 27.13 ? 20 CYS A CB 1 ATOM 169 S SG . CYS A 1 20 ? 22.766 2.468 39.441 1.00 27.77 ? 20 CYS A SG 1 ATOM 170 N N . PHE A 1 21 ? 25.411 -0.022 39.206 1.00 26.04 ? 21 PHE A N 1 ATOM 171 C CA . PHE A 1 21 ? 25.914 -0.816 40.323 1.00 28.28 ? 21 PHE A CA 1 ATOM 172 C C . PHE A 1 21 ? 25.963 0.089 41.553 1.00 28.60 ? 21 PHE A C 1 ATOM 173 O O . PHE A 1 21 ? 25.979 1.313 41.428 1.00 27.52 ? 21 PHE A O 1 ATOM 174 C CB . PHE A 1 21 ? 27.305 -1.392 40.017 1.00 30.14 ? 21 PHE A CB 1 ATOM 175 C CG . PHE A 1 21 ? 27.284 -2.531 39.026 1.00 32.94 ? 21 PHE A CG 1 ATOM 176 C CD1 . PHE A 1 21 ? 27.147 -2.281 37.664 1.00 35.01 ? 21 PHE A CD1 1 ATOM 177 C CD2 . PHE A 1 21 ? 27.366 -3.855 39.464 1.00 35.40 ? 21 PHE A CD2 1 ATOM 178 C CE1 . PHE A 1 21 ? 27.087 -3.330 36.745 1.00 37.13 ? 21 PHE A CE1 1 ATOM 179 C CE2 . PHE A 1 21 ? 27.308 -4.916 38.558 1.00 36.14 ? 21 PHE A CE2 1 ATOM 180 C CZ . PHE A 1 21 ? 27.167 -4.651 37.192 1.00 36.15 ? 21 PHE A CZ 1 ATOM 181 N N . PRO A 1 22 ? 25.990 -0.502 42.759 1.00 28.48 ? 22 PRO A N 1 ATOM 182 C CA . PRO A 1 22 ? 26.027 0.272 44.004 1.00 29.07 ? 22 PRO A CA 1 ATOM 183 C C . PRO A 1 22 ? 27.085 1.373 44.098 1.00 28.70 ? 22 PRO A C 1 ATOM 184 O O . PRO A 1 22 ? 26.862 2.394 44.757 1.00 27.05 ? 22 PRO A O 1 ATOM 185 C CB . PRO A 1 22 ? 26.231 -0.802 45.070 1.00 28.35 ? 22 PRO A CB 1 ATOM 186 C CG . PRO A 1 22 ? 25.547 -2.002 44.473 1.00 29.22 ? 22 PRO A CG 1 ATOM 187 C CD . PRO A 1 22 ? 26.032 -1.948 43.045 1.00 29.35 ? 22 PRO A CD 1 ATOM 188 N N . ASP A 1 23 ? 28.232 1.182 43.452 1.00 28.62 ? 23 ASP A N 1 ATOM 189 C CA . ASP A 1 23 ? 29.280 2.193 43.537 1.00 29.69 ? 23 ASP A CA 1 ATOM 190 C C . ASP A 1 23 ? 28.986 3.479 42.763 1.00 28.92 ? 23 ASP A C 1 ATOM 191 O O . ASP A 1 23 ? 29.760 4.430 42.827 1.00 29.66 ? 23 ASP A O 1 ATOM 192 C CB . ASP A 1 23 ? 30.638 1.620 43.105 1.00 34.76 ? 23 ASP A CB 1 ATOM 193 C CG . ASP A 1 23 ? 30.643 1.125 41.678 1.00 39.04 ? 23 ASP A CG 1 ATOM 194 O OD1 . ASP A 1 23 ? 31.749 1.034 41.102 1.00 44.79 ? 23 ASP A OD1 1 ATOM 195 O OD2 . ASP A 1 23 ? 29.556 0.820 41.142 1.00 42.70 ? 23 ASP A OD2 1 ATOM 196 N N . ALA A 1 24 ? 27.872 3.516 42.037 1.00 26.48 ? 24 ALA A N 1 ATOM 197 C CA . ALA A 1 24 ? 27.506 4.715 41.290 1.00 25.85 ? 24 ALA A CA 1 ATOM 198 C C . ALA A 1 24 ? 26.754 5.661 42.223 1.00 26.68 ? 24 ALA A C 1 ATOM 199 O O . ALA A 1 24 ? 26.519 6.827 41.893 1.00 26.10 ? 24 ALA A O 1 ATOM 200 C CB . ALA A 1 24 ? 26.622 4.358 40.107 1.00 24.61 ? 24 ALA A CB 1 ATOM 201 N N . ILE A 1 25 ? 26.386 5.145 43.392 1.00 23.88 ? 25 ILE A N 1 ATOM 202 C CA . ILE A 1 25 ? 25.637 5.907 44.387 1.00 23.57 ? 25 ILE A CA 1 ATOM 203 C C . ILE A 1 25 ? 26.477 6.894 45.194 1.00 22.82 ? 25 ILE A C 1 ATOM 204 O O . ILE A 1 25 ? 27.479 6.513 45.794 1.00 23.05 ? 25 ILE A O 1 ATOM 205 C CB . ILE A 1 25 ? 24.941 4.950 45.390 1.00 23.46 ? 25 ILE A CB 1 ATOM 206 C CG1 . ILE A 1 25 ? 23.943 4.061 44.646 1.00 23.63 ? 25 ILE A CG1 1 ATOM 207 C CG2 . ILE A 1 25 ? 24.233 5.750 46.486 1.00 22.87 ? 25 ILE A CG2 1 ATOM 208 C CD1 . ILE A 1 25 ? 23.341 2.968 45.517 1.00 23.36 ? 25 ILE A CD1 1 ATOM 209 N N . ASP A 1 26 ? 26.055 8.157 45.218 1.00 22.61 ? 26 ASP A N 1 ATOM 210 C CA . ASP A 1 26 ? 26.748 9.195 45.985 1.00 23.85 ? 26 ASP A CA 1 ATOM 211 C C . ASP A 1 26 ? 26.499 8.895 47.463 1.00 23.09 ? 26 ASP A C 1 ATOM 212 O O . ASP A 1 26 ? 25.361 8.906 47.912 1.00 23.36 ? 26 ASP A O 1 ATOM 213 C CB . ASP A 1 26 ? 26.187 10.576 45.631 1.00 24.88 ? 26 ASP A CB 1 ATOM 214 C CG . ASP A 1 26 ? 26.716 11.676 46.539 1.00 29.47 ? 26 ASP A CG 1 ATOM 215 O OD1 . ASP A 1 26 ? 27.574 11.393 47.408 1.00 28.01 ? 26 ASP A OD1 1 ATOM 216 O OD2 . ASP A 1 26 ? 26.262 12.828 46.379 1.00 32.17 ? 26 ASP A OD2 1 ATOM 217 N N . PRO A 1 27 ? 27.565 8.635 48.239 1.00 23.53 ? 27 PRO A N 1 ATOM 218 C CA . PRO A 1 27 ? 27.472 8.320 49.672 1.00 25.14 ? 27 PRO A CA 1 ATOM 219 C C . PRO A 1 27 ? 26.745 9.355 50.530 1.00 23.82 ? 27 PRO A C 1 ATOM 220 O O . PRO A 1 27 ? 26.147 9.015 51.558 1.00 21.71 ? 27 PRO A O 1 ATOM 221 C CB . PRO A 1 27 ? 28.943 8.191 50.097 1.00 25.16 ? 27 PRO A CB 1 ATOM 222 C CG . PRO A 1 27 ? 29.659 7.860 48.824 1.00 24.79 ? 27 PRO A CG 1 ATOM 223 C CD . PRO A 1 27 ? 28.975 8.747 47.827 1.00 23.74 ? 27 PRO A CD 1 ATOM 224 N N . PHE A 1 28 ? 26.807 10.618 50.115 1.00 22.35 ? 28 PHE A N 1 ATOM 225 C CA . PHE A 1 28 ? 26.196 11.708 50.878 1.00 23.65 ? 28 PHE A CA 1 ATOM 226 C C . PHE A 1 28 ? 24.824 12.163 50.386 1.00 23.88 ? 28 PHE A C 1 ATOM 227 O O . PHE A 1 28 ? 24.231 13.077 50.954 1.00 24.17 ? 28 PHE A O 1 ATOM 228 C CB . PHE A 1 28 ? 27.162 12.899 50.890 1.00 25.05 ? 28 PHE A CB 1 ATOM 229 C CG . PHE A 1 28 ? 28.519 12.555 51.437 1.00 25.66 ? 28 PHE A CG 1 ATOM 230 C CD1 . PHE A 1 28 ? 28.734 12.514 52.813 1.00 27.32 ? 28 PHE A CD1 1 ATOM 231 C CD2 . PHE A 1 28 ? 29.563 12.219 50.580 1.00 26.01 ? 28 PHE A CD2 1 ATOM 232 C CE1 . PHE A 1 28 ? 29.968 12.127 53.333 1.00 30.65 ? 28 PHE A CE1 1 ATOM 233 C CE2 . PHE A 1 28 ? 30.805 11.829 51.085 1.00 28.22 ? 28 PHE A CE2 1 ATOM 234 C CZ . PHE A 1 28 ? 31.008 11.788 52.467 1.00 26.76 ? 28 PHE A CZ 1 ATOM 235 N N . LEU A 1 29 ? 24.314 11.528 49.337 1.00 22.41 ? 29 LEU A N 1 ATOM 236 C CA . LEU A 1 29 ? 23.015 11.911 48.789 1.00 22.69 ? 29 LEU A CA 1 ATOM 237 C C . LEU A 1 29 ? 21.836 11.599 49.721 1.00 23.37 ? 29 LEU A C 1 ATOM 238 O O . LEU A 1 29 ? 21.072 12.494 50.096 1.00 21.98 ? 29 LEU A O 1 ATOM 239 C CB . LEU A 1 29 ? 22.800 11.221 47.434 1.00 23.95 ? 29 LEU A CB 1 ATOM 240 C CG . LEU A 1 29 ? 21.516 11.516 46.637 1.00 27.08 ? 29 LEU A CG 1 ATOM 241 C CD1 . LEU A 1 29 ? 21.412 13.014 46.350 1.00 26.88 ? 29 LEU A CD1 1 ATOM 242 C CD2 . LEU A 1 29 ? 21.523 10.728 45.322 1.00 25.60 ? 29 LEU A CD2 1 ATOM 243 N N . CYS A 1 30 ? 21.690 10.327 50.088 1.00 21.42 ? 30 CYS A N 1 ATOM 244 C CA . CYS A 1 30 ? 20.595 9.875 50.953 1.00 21.43 ? 30 CYS A CA 1 ATOM 245 C C . CYS A 1 30 ? 21.038 9.605 52.386 1.00 21.50 ? 30 CYS A C 1 ATOM 246 O O . CYS A 1 30 ? 22.233 9.479 52.651 1.00 21.87 ? 30 CYS A O 1 ATOM 247 C CB . CYS A 1 30 ? 20.019 8.587 50.376 1.00 18.01 ? 30 CYS A CB 1 ATOM 248 S SG . CYS A 1 30 ? 19.652 8.748 48.607 1.00 19.71 ? 30 CYS A SG 1 ATOM 249 N N . THR A 1 31 ? 20.076 9.515 53.306 1.00 19.51 ? 31 THR A N 1 ATOM 250 C CA . THR A 1 31 ? 20.400 9.208 54.699 1.00 20.17 ? 31 THR A CA 1 ATOM 251 C C . THR A 1 31 ? 20.321 7.691 54.871 1.00 20.71 ? 31 THR A C 1 ATOM 252 O O . THR A 1 31 ? 21.048 7.115 55.680 1.00 19.43 ? 31 THR A O 1 ATOM 253 C CB . THR A 1 31 ? 19.419 9.859 55.716 1.00 20.96 ? 31 THR A CB 1 ATOM 254 O OG1 . THR A 1 31 ? 18.074 9.436 55.441 1.00 17.36 ? 31 THR A OG1 1 ATOM 255 C CG2 . THR A 1 31 ? 19.511 11.382 55.663 1.00 22.59 ? 31 THR A CG2 1 ATOM 256 N N . HIS A 1 32 ? 19.448 7.055 54.089 1.00 18.86 ? 32 HIS A N 1 ATOM 257 C CA . HIS A 1 32 ? 19.257 5.603 54.138 1.00 18.67 ? 32 HIS A CA 1 ATOM 258 C C . HIS A 1 32 ? 19.153 5.030 52.734 1.00 19.15 ? 32 HIS A C 1 ATOM 259 O O . HIS A 1 32 ? 18.436 5.578 51.894 1.00 17.82 ? 32 HIS A O 1 ATOM 260 C CB . HIS A 1 32 ? 17.958 5.241 54.869 1.00 19.81 ? 32 HIS A CB 1 ATOM 261 C CG . HIS A 1 32 ? 17.887 5.721 56.288 1.00 19.16 ? 32 HIS A CG 1 ATOM 262 N ND1 . HIS A 1 32 ? 17.828 7.056 56.626 1.00 18.59 ? 32 HIS A ND1 1 ATOM 263 C CD2 . HIS A 1 32 ? 17.857 5.035 57.456 1.00 20.87 ? 32 HIS A CD2 1 ATOM 264 C CE1 . HIS A 1 32 ? 17.766 7.173 57.942 1.00 20.48 ? 32 HIS A CE1 1 ATOM 265 N NE2 . HIS A 1 32 ? 17.782 5.962 58.469 1.00 20.14 ? 32 HIS A NE2 1 ATOM 266 N N . VAL A 1 33 ? 19.864 3.936 52.466 1.00 17.63 ? 33 VAL A N 1 ATOM 267 C CA . VAL A 1 33 ? 19.764 3.300 51.151 1.00 18.09 ? 33 VAL A CA 1 ATOM 268 C C . VAL A 1 33 ? 19.258 1.879 51.367 1.00 17.52 ? 33 VAL A C 1 ATOM 269 O O . VAL A 1 33 ? 19.794 1.132 52.184 1.00 16.36 ? 33 VAL A O 1 ATOM 270 C CB . VAL A 1 33 ? 21.116 3.265 50.414 1.00 18.88 ? 33 VAL A CB 1 ATOM 271 C CG1 . VAL A 1 33 ? 20.965 2.514 49.087 1.00 20.07 ? 33 VAL A CG1 1 ATOM 272 C CG2 . VAL A 1 33 ? 21.590 4.691 50.145 1.00 20.85 ? 33 VAL A CG2 1 ATOM 273 N N . ILE A 1 34 ? 18.213 1.513 50.642 1.00 15.46 ? 34 ILE A N 1 ATOM 274 C CA . ILE A 1 34 ? 17.618 0.195 50.782 1.00 17.01 ? 34 ILE A CA 1 ATOM 275 C C . ILE A 1 34 ? 17.850 -0.654 49.537 1.00 17.92 ? 34 ILE A C 1 ATOM 276 O O . ILE A 1 34 ? 17.540 -0.245 48.411 1.00 17.36 ? 34 ILE A O 1 ATOM 277 C CB . ILE A 1 34 ? 16.101 0.319 51.056 1.00 16.97 ? 34 ILE A CB 1 ATOM 278 C CG1 . ILE A 1 34 ? 15.889 1.197 52.294 1.00 18.34 ? 34 ILE A CG1 1 ATOM 279 C CG2 . ILE A 1 34 ? 15.479 -1.075 51.259 1.00 14.51 ? 34 ILE A CG2 1 ATOM 280 C CD1 . ILE A 1 34 ? 14.415 1.428 52.665 1.00 20.02 ? 34 ILE A CD1 1 ATOM 281 N N . TYR A 1 35 ? 18.406 -1.838 49.754 1.00 19.61 ? 35 TYR A N 1 ATOM 282 C CA . TYR A 1 35 ? 18.695 -2.777 48.675 1.00 19.47 ? 35 TYR A CA 1 ATOM 283 C C . TYR A 1 35 ? 17.455 -3.650 48.468 1.00 18.73 ? 35 TYR A C 1 ATOM 284 O O . TYR A 1 35 ? 16.951 -4.233 49.426 1.00 19.02 ? 35 TYR A O 1 ATOM 285 C CB . TYR A 1 35 ? 19.887 -3.641 49.085 1.00 21.40 ? 35 TYR A CB 1 ATOM 286 C CG . TYR A 1 35 ? 20.461 -4.489 47.980 1.00 22.50 ? 35 TYR A CG 1 ATOM 287 C CD1 . TYR A 1 35 ? 21.579 -4.062 47.268 1.00 22.39 ? 35 TYR A CD1 1 ATOM 288 C CD2 . TYR A 1 35 ? 19.895 -5.724 47.651 1.00 20.43 ? 35 TYR A CD2 1 ATOM 289 C CE1 . TYR A 1 35 ? 22.128 -4.842 46.258 1.00 23.56 ? 35 TYR A CE1 1 ATOM 290 C CE2 . TYR A 1 35 ? 20.435 -6.510 46.640 1.00 23.08 ? 35 TYR A CE2 1 ATOM 291 C CZ . TYR A 1 35 ? 21.553 -6.063 45.947 1.00 22.57 ? 35 TYR A CZ 1 ATOM 292 O OH . TYR A 1 35 ? 22.090 -6.831 44.931 1.00 25.72 ? 35 TYR A OH 1 ATOM 293 N N . SER A 1 36 ? 16.967 -3.728 47.228 1.00 19.98 ? 36 SER A N 1 ATOM 294 C CA . SER A 1 36 ? 15.778 -4.521 46.878 1.00 22.79 ? 36 SER A CA 1 ATOM 295 C C . SER A 1 36 ? 16.158 -5.567 45.835 1.00 21.99 ? 36 SER A C 1 ATOM 296 O O . SER A 1 36 ? 16.783 -5.215 44.842 1.00 21.66 ? 36 SER A O 1 ATOM 297 C CB . SER A 1 36 ? 14.704 -3.627 46.256 1.00 24.08 ? 36 SER A CB 1 ATOM 298 O OG . SER A 1 36 ? 14.541 -2.437 46.996 1.00 32.28 ? 36 SER A OG 1 ATOM 299 N N . PHE A 1 37 ? 15.772 -6.832 46.015 1.00 21.65 ? 37 PHE A N 1 ATOM 300 C CA . PHE A 1 37 ? 14.995 -7.328 47.149 1.00 22.25 ? 37 PHE A CA 1 ATOM 301 C C . PHE A 1 37 ? 15.634 -8.634 47.612 1.00 23.57 ? 37 PHE A C 1 ATOM 302 O O . PHE A 1 37 ? 16.349 -9.291 46.853 1.00 23.46 ? 37 PHE A O 1 ATOM 303 C CB . PHE A 1 37 ? 13.547 -7.650 46.726 1.00 22.21 ? 37 PHE A CB 1 ATOM 304 C CG . PHE A 1 37 ? 12.691 -6.441 46.451 1.00 23.37 ? 37 PHE A CG 1 ATOM 305 C CD1 . PHE A 1 37 ? 12.187 -5.669 47.499 1.00 21.07 ? 37 PHE A CD1 1 ATOM 306 C CD2 . PHE A 1 37 ? 12.373 -6.083 45.139 1.00 21.98 ? 37 PHE A CD2 1 ATOM 307 C CE1 . PHE A 1 37 ? 11.375 -4.554 47.239 1.00 21.47 ? 37 PHE A CE1 1 ATOM 308 C CE2 . PHE A 1 37 ? 11.565 -4.974 44.868 1.00 22.47 ? 37 PHE A CE2 1 ATOM 309 C CZ . PHE A 1 37 ? 11.067 -4.210 45.917 1.00 22.16 ? 37 PHE A CZ 1 ATOM 310 N N . ALA A 1 38 ? 15.365 -9.013 48.854 1.00 23.03 ? 38 ALA A N 1 ATOM 311 C CA . ALA A 1 38 ? 15.869 -10.268 49.387 1.00 23.07 ? 38 ALA A CA 1 ATOM 312 C C . ALA A 1 38 ? 14.725 -11.253 49.178 1.00 22.90 ? 38 ALA A C 1 ATOM 313 O O . ALA A 1 38 ? 13.571 -10.849 49.004 1.00 20.85 ? 38 ALA A O 1 ATOM 314 C CB . ALA A 1 38 ? 16.194 -10.139 50.871 1.00 20.38 ? 38 ALA A CB 1 ATOM 315 N N . ASN A 1 39 ? 15.042 -12.540 49.199 1.00 22.95 ? 39 ASN A N 1 ATOM 316 C CA . ASN A 1 39 ? 14.045 -13.576 48.989 1.00 23.87 ? 39 ASN A CA 1 ATOM 317 C C . ASN A 1 39 ? 13.898 -14.354 50.293 1.00 25.75 ? 39 ASN A C 1 ATOM 318 O O . ASN A 1 39 ? 14.569 -14.053 51.285 1.00 23.45 ? 39 ASN A O 1 ATOM 319 C CB . ASN A 1 39 ? 14.542 -14.471 47.844 1.00 28.20 ? 39 ASN A CB 1 ATOM 320 C CG . ASN A 1 39 ? 13.552 -15.562 47.442 1.00 28.76 ? 39 ASN A CG 1 ATOM 321 O OD1 . ASN A 1 39 ? 12.340 -15.437 47.610 1.00 29.64 ? 39 ASN A OD1 1 ATOM 322 N ND2 . ASN A 1 39 ? 14.098 -16.633 46.871 1.00 32.99 ? 39 ASN A ND2 1 ATOM 323 N N . ILE A 1 40 ? 12.994 -15.326 50.302 1.00 26.66 ? 40 ILE A N 1 ATOM 324 C CA . ILE A 1 40 ? 12.796 -16.174 51.471 1.00 28.51 ? 40 ILE A CA 1 ATOM 325 C C . ILE A 1 40 ? 12.785 -17.607 50.954 1.00 30.29 ? 40 ILE A C 1 ATOM 326 O O . ILE A 1 40 ? 11.984 -17.952 50.088 1.00 29.63 ? 40 ILE A O 1 ATOM 327 C CB . ILE A 1 40 ? 11.459 -15.877 52.189 1.00 28.16 ? 40 ILE A CB 1 ATOM 328 C CG1 . ILE A 1 40 ? 11.474 -14.453 52.752 1.00 27.97 ? 40 ILE A CG1 1 ATOM 329 C CG2 . ILE A 1 40 ? 11.237 -16.878 53.328 1.00 29.10 ? 40 ILE A CG2 1 ATOM 330 C CD1 . ILE A 1 40 ? 10.201 -14.064 53.470 1.00 26.61 ? 40 ILE A CD1 1 ATOM 331 N N . SER A 1 41 ? 13.706 -18.418 51.462 1.00 32.24 ? 41 SER A N 1 ATOM 332 C CA . SER A 1 41 ? 13.814 -19.819 51.067 1.00 34.99 ? 41 SER A CA 1 ATOM 333 C C . SER A 1 41 ? 13.843 -20.647 52.343 1.00 35.85 ? 41 SER A C 1 ATOM 334 O O . SER A 1 41 ? 14.568 -20.318 53.283 1.00 32.65 ? 41 SER A O 1 ATOM 335 C CB . SER A 1 41 ? 15.099 -20.054 50.271 1.00 35.97 ? 41 SER A CB 1 ATOM 336 O OG . SER A 1 41 ? 15.184 -19.155 49.182 1.00 44.70 ? 41 SER A OG 1 ATOM 337 N N . ASN A 1 42 ? 13.059 -21.720 52.368 1.00 37.20 ? 42 ASN A N 1 ATOM 338 C CA . ASN A 1 42 ? 12.967 -22.583 53.541 1.00 39.13 ? 42 ASN A CA 1 ATOM 339 C C . ASN A 1 42 ? 12.664 -21.739 54.770 1.00 37.20 ? 42 ASN A C 1 ATOM 340 O O . ASN A 1 42 ? 13.216 -21.965 55.845 1.00 36.63 ? 42 ASN A O 1 ATOM 341 C CB . ASN A 1 42 ? 14.263 -23.374 53.758 1.00 42.71 ? 42 ASN A CB 1 ATOM 342 C CG . ASN A 1 42 ? 14.608 -24.267 52.578 1.00 46.92 ? 42 ASN A CG 1 ATOM 343 O OD1 . ASN A 1 42 ? 15.457 -23.928 51.751 1.00 50.65 ? 42 ASN A OD1 1 ATOM 344 N ND2 . ASN A 1 42 ? 13.938 -25.411 52.487 1.00 49.72 ? 42 ASN A ND2 1 ATOM 345 N N . ASN A 1 43 ? 11.780 -20.761 54.590 1.00 36.71 ? 43 ASN A N 1 ATOM 346 C CA . ASN A 1 43 ? 11.356 -19.858 55.659 1.00 35.64 ? 43 ASN A CA 1 ATOM 347 C C . ASN A 1 43 ? 12.479 -19.031 56.278 1.00 32.89 ? 43 ASN A C 1 ATOM 348 O O . ASN A 1 43 ? 12.394 -18.611 57.430 1.00 32.20 ? 43 ASN A O 1 ATOM 349 C CB . ASN A 1 43 ? 10.630 -20.640 56.758 1.00 37.14 ? 43 ASN A CB 1 ATOM 350 C CG . ASN A 1 43 ? 9.347 -21.277 56.263 1.00 39.80 ? 43 ASN A CG 1 ATOM 351 O OD1 . ASN A 1 43 ? 8.791 -20.860 55.246 1.00 44.33 ? 43 ASN A OD1 1 ATOM 352 N ND2 . ASN A 1 43 ? 8.862 -22.282 56.983 1.00 41.25 ? 43 ASN A ND2 1 ATOM 353 N N . GLU A 1 44 ? 13.533 -18.801 55.509 1.00 30.58 ? 44 GLU A N 1 ATOM 354 C CA . GLU A 1 44 ? 14.649 -18.000 55.983 1.00 31.76 ? 44 GLU A CA 1 ATOM 355 C C . GLU A 1 44 ? 14.990 -16.948 54.946 1.00 30.29 ? 44 GLU A C 1 ATOM 356 O O . GLU A 1 44 ? 14.872 -17.195 53.744 1.00 27.27 ? 44 GLU A O 1 ATOM 357 C CB . GLU A 1 44 ? 15.871 -18.881 56.249 1.00 33.80 ? 44 GLU A CB 1 ATOM 358 C CG . GLU A 1 44 ? 15.792 -19.623 57.570 1.00 38.24 ? 44 GLU A CG 1 ATOM 359 C CD . GLU A 1 44 ? 16.941 -20.586 57.781 1.00 38.98 ? 44 GLU A CD 1 ATOM 360 O OE1 . GLU A 1 44 ? 17.950 -20.492 57.054 1.00 41.28 ? 44 GLU A OE1 1 ATOM 361 O OE2 . GLU A 1 44 ? 16.834 -21.435 58.687 1.00 45.61 ? 44 GLU A OE2 1 ATOM 362 N N . ILE A 1 45 ? 15.397 -15.768 55.408 1.00 28.52 ? 45 ILE A N 1 ATOM 363 C CA . ILE A 1 45 ? 15.758 -14.706 54.483 1.00 27.53 ? 45 ILE A CA 1 ATOM 364 C C . ILE A 1 45 ? 16.941 -15.233 53.686 1.00 26.74 ? 45 ILE A C 1 ATOM 365 O O . ILE A 1 45 ? 17.754 -16.000 54.197 1.00 25.69 ? 45 ILE A O 1 ATOM 366 C CB . ILE A 1 45 ? 16.144 -13.405 55.230 1.00 27.61 ? 45 ILE A CB 1 ATOM 367 C CG1 . ILE A 1 45 ? 16.323 -12.264 54.223 1.00 27.48 ? 45 ILE A CG1 1 ATOM 368 C CG2 . ILE A 1 45 ? 17.428 -13.614 56.034 1.00 26.11 ? 45 ILE A CG2 1 ATOM 369 C CD1 . ILE A 1 45 ? 16.301 -10.878 54.863 1.00 25.16 ? 45 ILE A CD1 1 ATOM 370 N N . ASP A 1 46 ? 17.045 -14.831 52.431 1.00 26.91 ? 46 ASP A N 1 ATOM 371 C CA . ASP A 1 46 ? 18.125 -15.338 51.608 1.00 27.76 ? 46 ASP A CA 1 ATOM 372 C C . ASP A 1 46 ? 18.389 -14.398 50.441 1.00 27.23 ? 46 ASP A C 1 ATOM 373 O O . ASP A 1 46 ? 17.607 -13.481 50.182 1.00 24.35 ? 46 ASP A O 1 ATOM 374 C CB . ASP A 1 46 ? 17.727 -16.737 51.119 1.00 29.45 ? 46 ASP A CB 1 ATOM 375 C CG . ASP A 1 46 ? 18.888 -17.523 50.562 1.00 33.77 ? 46 ASP A CG 1 ATOM 376 O OD1 . ASP A 1 46 ? 20.038 -17.279 50.985 1.00 35.81 ? 46 ASP A OD1 1 ATOM 377 O OD2 . ASP A 1 46 ? 18.637 -18.397 49.707 1.00 39.08 ? 46 ASP A OD2 1 ATOM 378 N N . THR A 1 47 ? 19.499 -14.619 49.747 1.00 26.66 ? 47 THR A N 1 ATOM 379 C CA . THR A 1 47 ? 19.856 -13.786 48.606 1.00 28.16 ? 47 THR A CA 1 ATOM 380 C C . THR A 1 47 ? 18.916 -14.049 47.436 1.00 29.11 ? 47 THR A C 1 ATOM 381 O O . THR A 1 47 ? 18.173 -15.027 47.431 1.00 29.21 ? 47 THR A O 1 ATOM 382 C CB . THR A 1 47 ? 21.299 -14.062 48.140 1.00 29.15 ? 47 THR A CB 1 ATOM 383 O OG1 . THR A 1 47 ? 21.448 -15.460 47.860 1.00 29.20 ? 47 THR A OG1 1 ATOM 384 C CG2 . THR A 1 47 ? 22.297 -13.645 49.211 1.00 27.07 ? 47 THR A CG2 1 ATOM 385 N N . TRP A 1 48 ? 18.960 -13.168 46.444 1.00 30.80 ? 48 TRP A N 1 ATOM 386 C CA . TRP A 1 48 ? 18.116 -13.294 45.263 1.00 31.79 ? 48 TRP A CA 1 ATOM 387 C C . TRP A 1 48 ? 18.997 -13.456 44.025 1.00 33.28 ? 48 TRP A C 1 ATOM 388 O O . TRP A 1 48 ? 18.939 -14.480 43.346 1.00 34.66 ? 48 TRP A O 1 ATOM 389 C CB . TRP A 1 48 ? 17.228 -12.052 45.123 1.00 30.72 ? 48 TRP A CB 1 ATOM 390 C CG . TRP A 1 48 ? 16.183 -12.147 44.049 1.00 32.82 ? 48 TRP A CG 1 ATOM 391 C CD1 . TRP A 1 48 ? 16.390 -12.221 42.698 1.00 33.96 ? 48 TRP A CD1 1 ATOM 392 C CD2 . TRP A 1 48 ? 14.763 -12.173 44.239 1.00 34.40 ? 48 TRP A CD2 1 ATOM 393 N NE1 . TRP A 1 48 ? 15.183 -12.292 42.038 1.00 34.29 ? 48 TRP A NE1 1 ATOM 394 C CE2 . TRP A 1 48 ? 14.170 -12.268 42.960 1.00 35.07 ? 48 TRP A CE2 1 ATOM 395 C CE3 . TRP A 1 48 ? 13.934 -12.127 45.371 1.00 36.56 ? 48 TRP A CE3 1 ATOM 396 C CZ2 . TRP A 1 48 ? 12.777 -12.315 42.779 1.00 37.30 ? 48 TRP A CZ2 1 ATOM 397 C CZ3 . TRP A 1 48 ? 12.545 -12.170 45.191 1.00 36.86 ? 48 TRP A CZ3 1 ATOM 398 C CH2 . TRP A 1 48 ? 11.985 -12.268 43.904 1.00 38.59 ? 48 TRP A CH2 1 ATOM 399 N N . GLU A 1 49 ? 19.812 -12.444 43.735 1.00 33.63 ? 49 GLU A N 1 ATOM 400 C CA . GLU A 1 49 ? 20.705 -12.494 42.581 1.00 35.94 ? 49 GLU A CA 1 ATOM 401 C C . GLU A 1 49 ? 21.949 -13.313 42.920 1.00 35.99 ? 49 GLU A C 1 ATOM 402 O O . GLU A 1 49 ? 22.371 -13.374 44.077 1.00 32.35 ? 49 GLU A O 1 ATOM 403 C CB . GLU A 1 49 ? 21.129 -11.080 42.158 1.00 37.26 ? 49 GLU A CB 1 ATOM 404 C CG . GLU A 1 49 ? 19.994 -10.165 41.712 1.00 38.47 ? 49 GLU A CG 1 ATOM 405 C CD . GLU A 1 49 ? 19.265 -10.662 40.474 1.00 40.64 ? 49 GLU A CD 1 ATOM 406 O OE1 . GLU A 1 49 ? 19.802 -11.537 39.758 1.00 40.31 ? 49 GLU A OE1 1 ATOM 407 O OE2 . GLU A 1 49 ? 18.148 -10.164 40.213 1.00 43.71 ? 49 GLU A OE2 1 ATOM 408 N N . TRP A 1 50 ? 22.538 -13.931 41.901 1.00 36.89 ? 50 TRP A N 1 ATOM 409 C CA . TRP A 1 50 ? 23.732 -14.756 42.084 1.00 38.35 ? 50 TRP A CA 1 ATOM 410 C C . TRP A 1 50 ? 24.905 -13.992 42.692 1.00 38.11 ? 50 TRP A C 1 ATOM 411 O O . TRP A 1 50 ? 25.715 -14.567 43.422 1.00 39.79 ? 50 TRP A O 1 ATOM 412 C CB . TRP A 1 50 ? 24.173 -15.358 40.742 1.00 40.29 ? 50 TRP A CB 1 ATOM 413 C CG . TRP A 1 50 ? 24.530 -14.327 39.717 1.00 43.57 ? 50 TRP A CG 1 ATOM 414 C CD1 . TRP A 1 50 ? 23.664 -13.550 38.998 1.00 45.71 ? 50 TRP A CD1 1 ATOM 415 C CD2 . TRP A 1 50 ? 25.850 -13.911 39.342 1.00 45.66 ? 50 TRP A CD2 1 ATOM 416 N NE1 . TRP A 1 50 ? 24.364 -12.677 38.197 1.00 47.47 ? 50 TRP A NE1 1 ATOM 417 C CE2 . TRP A 1 50 ? 25.707 -12.879 38.385 1.00 47.13 ? 50 TRP A CE2 1 ATOM 418 C CE3 . TRP A 1 50 ? 27.141 -14.316 39.713 1.00 45.88 ? 50 TRP A CE3 1 ATOM 419 C CZ2 . TRP A 1 50 ? 26.809 -12.233 37.804 1.00 47.18 ? 50 TRP A CZ2 1 ATOM 420 C CZ3 . TRP A 1 50 ? 28.238 -13.674 39.134 1.00 47.07 ? 50 TRP A CZ3 1 ATOM 421 C CH2 . TRP A 1 50 ? 28.062 -12.648 38.186 1.00 46.92 ? 50 TRP A CH2 1 ATOM 422 N N . ASN A 1 51 ? 25.004 -12.702 42.389 1.00 35.08 ? 51 ASN A N 1 ATOM 423 C CA . ASN A 1 51 ? 26.106 -11.903 42.909 1.00 34.15 ? 51 ASN A CA 1 ATOM 424 C C . ASN A 1 51 ? 25.728 -10.948 44.047 1.00 32.15 ? 51 ASN A C 1 ATOM 425 O O . ASN A 1 51 ? 26.478 -10.022 44.350 1.00 32.17 ? 51 ASN A O 1 ATOM 426 C CB . ASN A 1 51 ? 26.767 -11.128 41.760 1.00 31.99 ? 51 ASN A CB 1 ATOM 427 C CG . ASN A 1 51 ? 25.811 -10.182 41.064 1.00 32.50 ? 51 ASN A CG 1 ATOM 428 O OD1 . ASN A 1 51 ? 24.598 -10.271 41.236 1.00 31.92 ? 51 ASN A OD1 1 ATOM 429 N ND2 . ASN A 1 51 ? 26.356 -9.275 40.259 1.00 31.24 ? 51 ASN A ND2 1 ATOM 430 N N . ASP A 1 52 ? 24.585 -11.186 44.689 1.00 31.14 ? 52 ASP A N 1 ATOM 431 C CA . ASP A 1 52 ? 24.131 -10.333 45.795 1.00 29.33 ? 52 ASP A CA 1 ATOM 432 C C . ASP A 1 52 ? 25.174 -10.112 46.898 1.00 27.66 ? 52 ASP A C 1 ATOM 433 O O . ASP A 1 52 ? 25.386 -8.984 47.340 1.00 23.00 ? 52 ASP A O 1 ATOM 434 C CB . ASP A 1 52 ? 22.852 -10.892 46.442 1.00 27.11 ? 52 ASP A CB 1 ATOM 435 C CG . ASP A 1 52 ? 21.581 -10.432 45.748 1.00 29.15 ? 52 ASP A CG 1 ATOM 436 O OD1 . ASP A 1 52 ? 21.630 -9.474 44.939 1.00 28.76 ? 52 ASP A OD1 1 ATOM 437 O OD2 . ASP A 1 52 ? 20.515 -11.022 46.038 1.00 25.69 ? 52 ASP A OD2 1 ATOM 438 N N . VAL A 1 53 ? 25.823 -11.178 47.356 1.00 27.56 ? 53 VAL A N 1 ATOM 439 C CA . VAL A 1 53 ? 26.812 -11.022 48.419 1.00 28.38 ? 53 VAL A CA 1 ATOM 440 C C . VAL A 1 53 ? 27.898 -10.021 48.022 1.00 28.26 ? 53 VAL A C 1 ATOM 441 O O . VAL A 1 53 ? 28.408 -9.277 48.864 1.00 27.36 ? 53 VAL A O 1 ATOM 442 C CB . VAL A 1 53 ? 27.464 -12.386 48.818 1.00 29.83 ? 53 VAL A CB 1 ATOM 443 C CG1 . VAL A 1 53 ? 26.391 -13.341 49.343 1.00 27.92 ? 53 VAL A CG1 1 ATOM 444 C CG2 . VAL A 1 53 ? 28.188 -12.998 47.632 1.00 34.21 ? 53 VAL A CG2 1 ATOM 445 N N . THR A 1 54 ? 28.237 -9.988 46.738 1.00 27.51 ? 54 THR A N 1 ATOM 446 C CA . THR A 1 54 ? 29.246 -9.052 46.255 1.00 29.56 ? 54 THR A CA 1 ATOM 447 C C . THR A 1 54 ? 28.679 -7.630 46.204 1.00 28.43 ? 54 THR A C 1 ATOM 448 O O . THR A 1 54 ? 29.342 -6.673 46.605 1.00 29.35 ? 54 THR A O 1 ATOM 449 C CB . THR A 1 54 ? 29.759 -9.457 44.852 1.00 31.66 ? 54 THR A CB 1 ATOM 450 O OG1 . THR A 1 54 ? 30.572 -10.637 44.963 1.00 34.67 ? 54 THR A OG1 1 ATOM 451 C CG2 . THR A 1 54 ? 30.570 -8.318 44.232 1.00 30.45 ? 54 THR A CG2 1 ATOM 452 N N . LEU A 1 55 ? 27.448 -7.491 45.726 1.00 27.40 ? 55 LEU A N 1 ATOM 453 C CA . LEU A 1 55 ? 26.828 -6.169 45.655 1.00 27.12 ? 55 LEU A CA 1 ATOM 454 C C . LEU A 1 55 ? 26.509 -5.644 47.059 1.00 24.95 ? 55 LEU A C 1 ATOM 455 O O . LEU A 1 55 ? 26.589 -4.436 47.303 1.00 25.28 ? 55 LEU A O 1 ATOM 456 C CB . LEU A 1 55 ? 25.571 -6.218 44.780 1.00 28.03 ? 55 LEU A CB 1 ATOM 457 C CG . LEU A 1 55 ? 25.848 -6.595 43.315 1.00 30.77 ? 55 LEU A CG 1 ATOM 458 C CD1 . LEU A 1 55 ? 24.557 -6.533 42.520 1.00 33.43 ? 55 LEU A CD1 1 ATOM 459 C CD2 . LEU A 1 55 ? 26.879 -5.648 42.708 1.00 33.49 ? 55 LEU A CD2 1 ATOM 460 N N . TYR A 1 56 ? 26.164 -6.543 47.981 1.00 23.28 ? 56 TYR A N 1 ATOM 461 C CA . TYR A 1 56 ? 25.895 -6.144 49.366 1.00 23.53 ? 56 TYR A CA 1 ATOM 462 C C . TYR A 1 56 ? 27.160 -5.463 49.866 1.00 25.65 ? 56 TYR A C 1 ATOM 463 O O . TYR A 1 56 ? 27.122 -4.394 50.484 1.00 26.47 ? 56 TYR A O 1 ATOM 464 C CB . TYR A 1 56 ? 25.675 -7.351 50.280 1.00 21.82 ? 56 TYR A CB 1 ATOM 465 C CG . TYR A 1 56 ? 24.361 -8.097 50.187 1.00 21.99 ? 56 TYR A CG 1 ATOM 466 C CD1 . TYR A 1 56 ? 23.303 -7.641 49.395 1.00 18.93 ? 56 TYR A CD1 1 ATOM 467 C CD2 . TYR A 1 56 ? 24.185 -9.280 50.907 1.00 21.49 ? 56 TYR A CD2 1 ATOM 468 C CE1 . TYR A 1 56 ? 22.097 -8.359 49.324 1.00 20.57 ? 56 TYR A CE1 1 ATOM 469 C CE2 . TYR A 1 56 ? 22.996 -10.001 50.846 1.00 20.45 ? 56 TYR A CE2 1 ATOM 470 C CZ . TYR A 1 56 ? 21.956 -9.541 50.056 1.00 22.00 ? 56 TYR A CZ 1 ATOM 471 O OH . TYR A 1 56 ? 20.790 -10.271 50.000 1.00 22.13 ? 56 TYR A OH 1 ATOM 472 N N . ASP A 1 57 ? 28.285 -6.127 49.612 1.00 25.67 ? 57 ASP A N 1 ATOM 473 C CA . ASP A 1 57 ? 29.599 -5.644 50.024 1.00 28.96 ? 57 ASP A CA 1 ATOM 474 C C . ASP A 1 57 ? 29.912 -4.279 49.407 1.00 26.77 ? 57 ASP A C 1 ATOM 475 O O . ASP A 1 57 ? 30.385 -3.380 50.093 1.00 27.81 ? 57 ASP A O 1 ATOM 476 C CB . ASP A 1 57 ? 30.664 -6.686 49.635 1.00 34.39 ? 57 ASP A CB 1 ATOM 477 C CG . ASP A 1 57 ? 32.049 -6.347 50.163 1.00 40.89 ? 57 ASP A CG 1 ATOM 478 O OD1 . ASP A 1 57 ? 32.169 -5.990 51.355 1.00 43.55 ? 57 ASP A OD1 1 ATOM 479 O OD2 . ASP A 1 57 ? 33.021 -6.453 49.386 1.00 46.48 ? 57 ASP A OD2 1 ATOM 480 N N . THR A 1 58 ? 29.629 -4.125 48.118 1.00 25.72 ? 58 THR A N 1 ATOM 481 C CA . THR A 1 58 ? 29.886 -2.871 47.417 1.00 26.47 ? 58 THR A CA 1 ATOM 482 C C . THR A 1 58 ? 29.059 -1.723 48.007 1.00 27.61 ? 58 THR A C 1 ATOM 483 O O . THR A 1 58 ? 29.575 -0.621 48.224 1.00 25.54 ? 58 THR A O 1 ATOM 484 C CB . THR A 1 58 ? 29.565 -3.009 45.911 1.00 28.93 ? 58 THR A CB 1 ATOM 485 O OG1 . THR A 1 58 ? 30.282 -4.126 45.367 1.00 31.44 ? 58 THR A OG1 1 ATOM 486 C CG2 . THR A 1 58 ? 29.958 -1.739 45.154 1.00 28.19 ? 58 THR A CG2 1 ATOM 487 N N . LEU A 1 59 ? 27.779 -1.992 48.270 1.00 25.62 ? 59 LEU A N 1 ATOM 488 C CA . LEU A 1 59 ? 26.869 -0.997 48.841 1.00 26.23 ? 59 LEU A CA 1 ATOM 489 C C . LEU A 1 59 ? 27.316 -0.541 50.222 1.00 25.86 ? 59 LEU A C 1 ATOM 490 O O . LEU A 1 59 ? 27.426 0.656 50.504 1.00 22.94 ? 59 LEU A O 1 ATOM 491 C CB . LEU A 1 59 ? 25.454 -1.576 48.967 1.00 26.93 ? 59 LEU A CB 1 ATOM 492 C CG . LEU A 1 59 ? 24.408 -0.686 49.658 1.00 28.84 ? 59 LEU A CG 1 ATOM 493 C CD1 . LEU A 1 59 ? 24.031 0.460 48.730 1.00 29.11 ? 59 LEU A CD1 1 ATOM 494 C CD2 . LEU A 1 59 ? 23.162 -1.500 50.014 1.00 29.78 ? 59 LEU A CD2 1 ATOM 495 N N . ASN A 1 60 ? 27.568 -1.509 51.089 1.00 25.66 ? 60 ASN A N 1 ATOM 496 C CA . ASN A 1 60 ? 27.965 -1.205 52.447 1.00 28.11 ? 60 ASN A CA 1 ATOM 497 C C . ASN A 1 60 ? 29.348 -0.560 52.574 1.00 30.14 ? 60 ASN A C 1 ATOM 498 O O . ASN A 1 60 ? 29.689 -0.041 53.633 1.00 29.62 ? 60 ASN A O 1 ATOM 499 C CB . ASN A 1 60 ? 27.838 -2.474 53.294 1.00 28.29 ? 60 ASN A CB 1 ATOM 500 C CG . ASN A 1 60 ? 26.381 -2.867 53.521 1.00 31.90 ? 60 ASN A CG 1 ATOM 501 O OD1 . ASN A 1 60 ? 26.031 -4.052 53.542 1.00 32.27 ? 60 ASN A OD1 1 ATOM 502 N ND2 . ASN A 1 60 ? 25.523 -1.865 53.698 1.00 28.91 ? 60 ASN A ND2 1 ATOM 503 N N . THR A 1 61 ? 30.143 -0.568 51.507 1.00 30.72 ? 61 THR A N 1 ATOM 504 C CA . THR A 1 61 ? 31.450 0.077 51.584 1.00 33.64 ? 61 THR A CA 1 ATOM 505 C C . THR A 1 61 ? 31.289 1.595 51.518 1.00 33.56 ? 61 THR A C 1 ATOM 506 O O . THR A 1 61 ? 32.202 2.330 51.889 1.00 34.32 ? 61 THR A O 1 ATOM 507 C CB . THR A 1 61 ? 32.405 -0.354 50.446 1.00 35.41 ? 61 THR A CB 1 ATOM 508 O OG1 . THR A 1 61 ? 31.852 0.023 49.179 1.00 40.62 ? 61 THR A OG1 1 ATOM 509 C CG2 . THR A 1 61 ? 32.640 -1.854 50.485 1.00 36.81 ? 61 THR A CG2 1 ATOM 510 N N . LEU A 1 62 ? 30.130 2.059 51.044 1.00 30.47 ? 62 LEU A N 1 ATOM 511 C CA . LEU A 1 62 ? 29.851 3.491 50.954 1.00 27.46 ? 62 LEU A CA 1 ATOM 512 C C . LEU A 1 62 ? 29.893 4.099 52.344 1.00 27.24 ? 62 LEU A C 1 ATOM 513 O O . LEU A 1 62 ? 30.110 5.305 52.507 1.00 25.16 ? 62 LEU A O 1 ATOM 514 C CB . LEU A 1 62 ? 28.461 3.743 50.366 1.00 25.68 ? 62 LEU A CB 1 ATOM 515 C CG . LEU A 1 62 ? 28.155 3.157 48.991 1.00 28.51 ? 62 LEU A CG 1 ATOM 516 C CD1 . LEU A 1 62 ? 26.702 3.442 48.634 1.00 26.60 ? 62 LEU A CD1 1 ATOM 517 C CD2 . LEU A 1 62 ? 29.093 3.757 47.964 1.00 28.15 ? 62 LEU A CD2 1 ATOM 518 N N . LYS A 1 63 ? 29.668 3.258 53.346 1.00 25.57 ? 63 LYS A N 1 ATOM 519 C CA . LYS A 1 63 ? 29.676 3.704 54.728 1.00 27.96 ? 63 LYS A CA 1 ATOM 520 C C . LYS A 1 63 ? 31.075 4.046 55.214 1.00 29.05 ? 63 LYS A C 1 ATOM 521 O O . LYS A 1 63 ? 31.233 4.649 56.268 1.00 29.30 ? 63 LYS A O 1 ATOM 522 C CB . LYS A 1 63 ? 29.021 2.643 55.616 1.00 27.57 ? 63 LYS A CB 1 ATOM 523 C CG . LYS A 1 63 ? 27.516 2.579 55.400 1.00 30.57 ? 63 LYS A CG 1 ATOM 524 C CD . LYS A 1 63 ? 26.971 1.171 55.570 1.00 33.21 ? 63 LYS A CD 1 ATOM 525 C CE . LYS A 1 63 ? 26.475 0.922 56.965 1.00 31.76 ? 63 LYS A CE 1 ATOM 526 N NZ . LYS A 1 63 ? 26.070 -0.498 57.126 1.00 27.84 ? 63 LYS A NZ 1 ATOM 527 N N . ASN A 1 64 ? 32.093 3.670 54.448 1.00 30.61 ? 64 ASN A N 1 ATOM 528 C CA . ASN A 1 64 ? 33.455 4.009 54.838 1.00 33.16 ? 64 ASN A CA 1 ATOM 529 C C . ASN A 1 64 ? 33.735 5.439 54.370 1.00 33.61 ? 64 ASN A C 1 ATOM 530 O O . ASN A 1 64 ? 34.712 6.061 54.781 1.00 32.54 ? 64 ASN A O 1 ATOM 531 C CB . ASN A 1 64 ? 34.466 3.039 54.220 1.00 36.57 ? 64 ASN A CB 1 ATOM 532 C CG . ASN A 1 64 ? 34.416 1.658 54.857 1.00 39.84 ? 64 ASN A CG 1 ATOM 533 O OD1 . ASN A 1 64 ? 34.150 1.522 56.053 1.00 42.13 ? 64 ASN A OD1 1 ATOM 534 N ND2 . ASN A 1 64 ? 34.683 0.627 54.061 1.00 43.05 ? 64 ASN A ND2 1 ATOM 535 N N . ARG A 1 65 ? 32.867 5.949 53.498 1.00 32.53 ? 65 ARG A N 1 ATOM 536 C CA . ARG A 1 65 ? 32.996 7.310 53.003 1.00 31.42 ? 65 ARG A CA 1 ATOM 537 C C . ARG A 1 65 ? 32.069 8.204 53.824 1.00 32.36 ? 65 ARG A C 1 ATOM 538 O O . ARG A 1 65 ? 32.452 9.306 54.226 1.00 29.11 ? 65 ARG A O 1 ATOM 539 C CB . ARG A 1 65 ? 32.654 7.377 51.508 1.00 35.76 ? 65 ARG A CB 1 ATOM 540 C CG . ARG A 1 65 ? 33.673 6.660 50.631 1.00 41.03 ? 65 ARG A CG 1 ATOM 541 C CD . ARG A 1 65 ? 34.266 7.601 49.602 1.00 47.59 ? 65 ARG A CD 1 ATOM 542 N NE . ARG A 1 65 ? 33.459 7.664 48.387 1.00 52.60 ? 65 ARG A NE 1 ATOM 543 C CZ . ARG A 1 65 ? 33.100 8.791 47.779 1.00 55.97 ? 65 ARG A CZ 1 ATOM 544 N NH1 . ARG A 1 65 ? 33.471 9.966 48.275 1.00 56.70 ? 65 ARG A NH1 1 ATOM 545 N NH2 . ARG A 1 65 ? 32.376 8.746 46.668 1.00 56.26 ? 65 ARG A NH2 1 ATOM 546 N N . ASN A 1 66 ? 30.855 7.717 54.089 1.00 29.40 ? 66 ASN A N 1 ATOM 547 C CA . ASN A 1 66 ? 29.893 8.462 54.890 1.00 28.67 ? 66 ASN A CA 1 ATOM 548 C C . ASN A 1 66 ? 29.462 7.582 56.060 1.00 30.64 ? 66 ASN A C 1 ATOM 549 O O . ASN A 1 66 ? 28.565 6.750 55.934 1.00 30.17 ? 66 ASN A O 1 ATOM 550 C CB . ASN A 1 66 ? 28.672 8.867 54.054 1.00 26.97 ? 66 ASN A CB 1 ATOM 551 C CG . ASN A 1 66 ? 27.632 9.617 54.876 1.00 27.39 ? 66 ASN A CG 1 ATOM 552 O OD1 . ASN A 1 66 ? 27.853 9.907 56.055 1.00 26.11 ? 66 ASN A OD1 1 ATOM 553 N ND2 . ASN A 1 66 ? 26.499 9.935 54.264 1.00 22.16 ? 66 ASN A ND2 1 ATOM 554 N N . PRO A 1 67 ? 30.104 7.763 57.222 1.00 31.91 ? 67 PRO A N 1 ATOM 555 C CA . PRO A 1 67 ? 29.840 7.014 58.455 1.00 32.20 ? 67 PRO A CA 1 ATOM 556 C C . PRO A 1 67 ? 28.408 7.103 58.989 1.00 30.53 ? 67 PRO A C 1 ATOM 557 O O . PRO A 1 67 ? 27.957 6.216 59.710 1.00 31.94 ? 67 PRO A O 1 ATOM 558 C CB . PRO A 1 67 ? 30.852 7.611 59.441 1.00 34.14 ? 67 PRO A CB 1 ATOM 559 C CG . PRO A 1 67 ? 31.962 8.087 58.549 1.00 33.64 ? 67 PRO A CG 1 ATOM 560 C CD . PRO A 1 67 ? 31.192 8.734 57.435 1.00 32.69 ? 67 PRO A CD 1 ATOM 561 N N . LYS A 1 68 ? 27.701 8.176 58.651 1.00 28.96 ? 68 LYS A N 1 ATOM 562 C CA . LYS A 1 68 ? 26.331 8.350 59.117 1.00 29.86 ? 68 LYS A CA 1 ATOM 563 C C . LYS A 1 68 ? 25.309 7.608 58.254 1.00 27.09 ? 68 LYS A C 1 ATOM 564 O O . LYS A 1 68 ? 24.161 7.445 58.650 1.00 26.47 ? 68 LYS A O 1 ATOM 565 C CB . LYS A 1 68 ? 25.982 9.845 59.175 1.00 32.42 ? 68 LYS A CB 1 ATOM 566 C CG . LYS A 1 68 ? 26.758 10.614 60.238 1.00 36.70 ? 68 LYS A CG 1 ATOM 567 C CD . LYS A 1 68 ? 26.089 10.518 61.601 1.00 41.01 ? 68 LYS A CD 1 ATOM 568 C CE . LYS A 1 68 ? 27.083 10.805 62.718 1.00 42.61 ? 68 LYS A CE 1 ATOM 569 N NZ . LYS A 1 68 ? 26.466 11.561 63.843 1.00 44.50 ? 68 LYS A NZ 1 ATOM 570 N N . LEU A 1 69 ? 25.735 7.149 57.083 1.00 24.20 ? 69 LEU A N 1 ATOM 571 C CA . LEU A 1 69 ? 24.849 6.440 56.158 1.00 24.73 ? 69 LEU A CA 1 ATOM 572 C C . LEU A 1 69 ? 24.352 5.094 56.717 1.00 25.72 ? 69 LEU A C 1 ATOM 573 O O . LEU A 1 69 ? 25.132 4.325 57.272 1.00 25.09 ? 69 LEU A O 1 ATOM 574 C CB . LEU A 1 69 ? 25.592 6.226 54.831 1.00 24.90 ? 69 LEU A CB 1 ATOM 575 C CG . LEU A 1 69 ? 24.903 5.779 53.531 1.00 27.20 ? 69 LEU A CG 1 ATOM 576 C CD1 . LEU A 1 69 ? 24.882 4.277 53.450 1.00 31.64 ? 69 LEU A CD1 1 ATOM 577 C CD2 . LEU A 1 69 ? 23.497 6.364 53.437 1.00 24.72 ? 69 LEU A CD2 1 ATOM 578 N N . LYS A 1 70 ? 23.052 4.826 56.584 1.00 22.19 ? 70 LYS A N 1 ATOM 579 C CA . LYS A 1 70 ? 22.460 3.568 57.053 1.00 22.69 ? 70 LYS A CA 1 ATOM 580 C C . LYS A 1 70 ? 21.944 2.779 55.858 1.00 22.50 ? 70 LYS A C 1 ATOM 581 O O . LYS A 1 70 ? 21.446 3.362 54.895 1.00 19.58 ? 70 LYS A O 1 ATOM 582 C CB . LYS A 1 70 ? 21.275 3.827 58.000 1.00 24.69 ? 70 LYS A CB 1 ATOM 583 C CG . LYS A 1 70 ? 21.611 4.568 59.282 1.00 29.26 ? 70 LYS A CG 1 ATOM 584 C CD . LYS A 1 70 ? 22.593 3.778 60.120 1.00 34.43 ? 70 LYS A CD 1 ATOM 585 C CE . LYS A 1 70 ? 22.892 4.485 61.431 1.00 37.95 ? 70 LYS A CE 1 ATOM 586 N NZ . LYS A 1 70 ? 23.958 3.774 62.197 1.00 42.07 ? 70 LYS A NZ 1 ATOM 587 N N . THR A 1 71 ? 22.056 1.455 55.918 1.00 19.95 ? 71 THR A N 1 ATOM 588 C CA . THR A 1 71 ? 21.570 0.617 54.827 1.00 19.23 ? 71 THR A CA 1 ATOM 589 C C . THR A 1 71 ? 20.585 -0.409 55.352 1.00 18.53 ? 71 THR A C 1 ATOM 590 O O . THR A 1 71 ? 20.703 -0.880 56.483 1.00 17.52 ? 71 THR A O 1 ATOM 591 C CB . THR A 1 71 ? 22.717 -0.147 54.105 1.00 20.99 ? 71 THR A CB 1 ATOM 592 O OG1 . THR A 1 71 ? 23.440 -0.945 55.050 1.00 20.38 ? 71 THR A OG1 1 ATOM 593 C CG2 . THR A 1 71 ? 23.652 0.822 53.417 1.00 16.86 ? 71 THR A CG2 1 ATOM 594 N N . LEU A 1 72 ? 19.593 -0.734 54.536 1.00 17.87 ? 72 LEU A N 1 ATOM 595 C CA . LEU A 1 72 ? 18.610 -1.735 54.915 1.00 17.03 ? 72 LEU A CA 1 ATOM 596 C C . LEU A 1 72 ? 18.451 -2.681 53.751 1.00 18.06 ? 72 LEU A C 1 ATOM 597 O O . LEU A 1 72 ? 18.798 -2.348 52.620 1.00 17.66 ? 72 LEU A O 1 ATOM 598 C CB . LEU A 1 72 ? 17.253 -1.104 55.245 1.00 15.57 ? 72 LEU A CB 1 ATOM 599 C CG . LEU A 1 72 ? 17.171 -0.253 56.518 1.00 19.02 ? 72 LEU A CG 1 ATOM 600 C CD1 . LEU A 1 72 ? 17.647 1.173 56.221 1.00 18.19 ? 72 LEU A CD1 1 ATOM 601 C CD2 . LEU A 1 72 ? 15.739 -0.234 57.026 1.00 17.47 ? 72 LEU A CD2 1 ATOM 602 N N . LEU A 1 73 ? 17.929 -3.865 54.036 1.00 18.18 ? 73 LEU A N 1 ATOM 603 C CA . LEU A 1 73 ? 17.701 -4.865 53.009 1.00 15.85 ? 73 LEU A CA 1 ATOM 604 C C . LEU A 1 73 ? 16.192 -5.053 52.990 1.00 15.94 ? 73 LEU A C 1 ATOM 605 O O . LEU A 1 73 ? 15.588 -5.293 54.030 1.00 15.43 ? 73 LEU A O 1 ATOM 606 C CB . LEU A 1 73 ? 18.387 -6.171 53.399 1.00 16.61 ? 73 LEU A CB 1 ATOM 607 C CG . LEU A 1 73 ? 18.172 -7.382 52.479 1.00 17.40 ? 73 LEU A CG 1 ATOM 608 C CD1 . LEU A 1 73 ? 18.619 -7.075 51.041 1.00 19.13 ? 73 LEU A CD1 1 ATOM 609 C CD2 . LEU A 1 73 ? 18.956 -8.564 53.058 1.00 18.96 ? 73 LEU A CD2 1 ATOM 610 N N . SER A 1 74 ? 15.579 -4.932 51.820 1.00 14.12 ? 74 SER A N 1 ATOM 611 C CA . SER A 1 74 ? 14.127 -5.082 51.724 1.00 17.39 ? 74 SER A CA 1 ATOM 612 C C . SER A 1 74 ? 13.747 -6.512 51.312 1.00 18.35 ? 74 SER A C 1 ATOM 613 O O . SER A 1 74 ? 14.349 -7.060 50.389 1.00 16.42 ? 74 SER A O 1 ATOM 614 C CB . SER A 1 74 ? 13.580 -4.066 50.707 1.00 13.99 ? 74 SER A CB 1 ATOM 615 O OG . SER A 1 74 ? 12.164 -4.114 50.633 1.00 15.69 ? 74 SER A OG 1 ATOM 616 N N . VAL A 1 75 ? 12.777 -7.113 52.009 1.00 19.40 ? 75 VAL A N 1 ATOM 617 C CA . VAL A 1 75 ? 12.298 -8.469 51.685 1.00 23.08 ? 75 VAL A CA 1 ATOM 618 C C . VAL A 1 75 ? 10.958 -8.342 50.990 1.00 23.49 ? 75 VAL A C 1 ATOM 619 O O . VAL A 1 75 ? 10.099 -7.589 51.445 1.00 21.89 ? 75 VAL A O 1 ATOM 620 C CB . VAL A 1 75 ? 11.979 -9.363 52.924 1.00 24.19 ? 75 VAL A CB 1 ATOM 621 C CG1 . VAL A 1 75 ? 12.696 -10.693 52.798 1.00 27.34 ? 75 VAL A CG1 1 ATOM 622 C CG2 . VAL A 1 75 ? 12.294 -8.657 54.211 1.00 27.23 ? 75 VAL A CG2 1 ATOM 623 N N . GLY A 1 76 ? 10.768 -9.100 49.918 1.00 25.75 ? 76 GLY A N 1 ATOM 624 C CA . GLY A 1 76 ? 9.503 -9.047 49.210 1.00 27.20 ? 76 GLY A CA 1 ATOM 625 C C . GLY A 1 76 ? 9.629 -8.475 47.817 1.00 27.42 ? 76 GLY A C 1 ATOM 626 O O . GLY A 1 76 ? 10.432 -8.949 47.017 1.00 28.34 ? 76 GLY A O 1 ATOM 627 N N . GLY A 1 77 ? 8.836 -7.449 47.531 1.00 28.81 ? 77 GLY A N 1 ATOM 628 C CA . GLY A 1 77 ? 8.872 -6.833 46.217 1.00 33.21 ? 77 GLY A CA 1 ATOM 629 C C . GLY A 1 77 ? 7.704 -7.313 45.376 1.00 36.63 ? 77 GLY A C 1 ATOM 630 O O . GLY A 1 77 ? 6.953 -8.197 45.801 1.00 35.03 ? 77 GLY A O 1 ATOM 631 N N . TRP A 1 78 ? 7.539 -6.754 44.183 1.00 40.77 ? 78 TRP A N 1 ATOM 632 C CA . TRP A 1 78 ? 6.424 -7.160 43.330 1.00 47.07 ? 78 TRP A CA 1 ATOM 633 C C . TRP A 1 78 ? 6.601 -8.492 42.623 1.00 46.99 ? 78 TRP A C 1 ATOM 634 O O . TRP A 1 78 ? 5.636 -9.030 42.092 1.00 48.93 ? 78 TRP A O 1 ATOM 635 C CB . TRP A 1 78 ? 6.128 -6.099 42.282 1.00 50.77 ? 78 TRP A CB 1 ATOM 636 C CG . TRP A 1 78 ? 5.708 -4.792 42.848 1.00 56.69 ? 78 TRP A CG 1 ATOM 637 C CD1 . TRP A 1 78 ? 4.431 -4.330 43.009 1.00 59.55 ? 78 TRP A CD1 1 ATOM 638 C CD2 . TRP A 1 78 ? 6.575 -3.721 43.230 1.00 59.10 ? 78 TRP A CD2 1 ATOM 639 N NE1 . TRP A 1 78 ? 4.456 -3.026 43.454 1.00 61.22 ? 78 TRP A NE1 1 ATOM 640 C CE2 . TRP A 1 78 ? 5.762 -2.631 43.597 1.00 60.97 ? 78 TRP A CE2 1 ATOM 641 C CE3 . TRP A 1 78 ? 7.964 -3.580 43.299 1.00 59.19 ? 78 TRP A CE3 1 ATOM 642 C CZ2 . TRP A 1 78 ? 6.300 -1.404 44.015 1.00 61.11 ? 78 TRP A CZ2 1 ATOM 643 C CZ3 . TRP A 1 78 ? 8.498 -2.369 43.712 1.00 60.00 ? 78 TRP A CZ3 1 ATOM 644 C CH2 . TRP A 1 78 ? 7.669 -1.298 44.064 1.00 61.32 ? 78 TRP A CH2 1 ATOM 645 N N . ASN A 1 79 ? 7.817 -9.024 42.588 1.00 46.99 ? 79 ASN A N 1 ATOM 646 C CA . ASN A 1 79 ? 8.013 -10.315 41.940 1.00 47.73 ? 79 ASN A CA 1 ATOM 647 C C . ASN A 1 79 ? 8.024 -11.393 42.995 1.00 46.48 ? 79 ASN A C 1 ATOM 648 O O . ASN A 1 79 ? 8.426 -12.527 42.752 1.00 47.27 ? 79 ASN A O 1 ATOM 649 C CB . ASN A 1 79 ? 9.309 -10.350 41.130 1.00 49.43 ? 79 ASN A CB 1 ATOM 650 C CG . ASN A 1 79 ? 9.175 -9.639 39.796 1.00 51.72 ? 79 ASN A CG 1 ATOM 651 O OD1 . ASN A 1 79 ? 9.478 -8.459 39.675 1.00 54.15 ? 79 ASN A OD1 1 ATOM 652 N ND2 . ASN A 1 79 ? 8.700 -10.359 38.789 1.00 55.03 ? 79 ASN A ND2 1 ATOM 653 N N . PHE A 1 80 ? 7.573 -11.010 44.181 1.00 45.21 ? 80 PHE A N 1 ATOM 654 C CA . PHE A 1 80 ? 7.492 -11.914 45.309 1.00 44.36 ? 80 PHE A CA 1 ATOM 655 C C . PHE A 1 80 ? 6.002 -12.116 45.543 1.00 44.38 ? 80 PHE A C 1 ATOM 656 O O . PHE A 1 80 ? 5.290 -11.182 45.919 1.00 44.74 ? 80 PHE A O 1 ATOM 657 C CB . PHE A 1 80 ? 8.153 -11.276 46.534 1.00 42.79 ? 80 PHE A CB 1 ATOM 658 C CG . PHE A 1 80 ? 8.303 -12.207 47.702 1.00 43.36 ? 80 PHE A CG 1 ATOM 659 C CD1 . PHE A 1 80 ? 7.217 -12.500 48.523 1.00 42.46 ? 80 PHE A CD1 1 ATOM 660 C CD2 . PHE A 1 80 ? 9.539 -12.791 47.984 1.00 44.82 ? 80 PHE A CD2 1 ATOM 661 C CE1 . PHE A 1 80 ? 7.355 -13.362 49.612 1.00 43.71 ? 80 PHE A CE1 1 ATOM 662 C CE2 . PHE A 1 80 ? 9.692 -13.656 49.071 1.00 45.13 ? 80 PHE A CE2 1 ATOM 663 C CZ . PHE A 1 80 ? 8.596 -13.942 49.889 1.00 44.82 ? 80 PHE A CZ 1 ATOM 664 N N . GLY A 1 81 ? 5.524 -13.329 45.296 1.00 43.02 ? 81 GLY A N 1 ATOM 665 C CA . GLY A 1 81 ? 4.112 -13.599 45.481 1.00 43.25 ? 81 GLY A CA 1 ATOM 666 C C . GLY A 1 81 ? 3.647 -13.252 46.880 1.00 42.41 ? 81 GLY A C 1 ATOM 667 O O . GLY A 1 81 ? 4.198 -13.763 47.858 1.00 43.16 ? 81 GLY A O 1 ATOM 668 N N . PRO A 1 82 ? 2.647 -12.367 47.016 1.00 41.98 ? 82 PRO A N 1 ATOM 669 C CA . PRO A 1 82 ? 2.175 -12.021 48.359 1.00 40.79 ? 82 PRO A CA 1 ATOM 670 C C . PRO A 1 82 ? 1.633 -13.252 49.084 1.00 40.30 ? 82 PRO A C 1 ATOM 671 O O . PRO A 1 82 ? 1.647 -13.311 50.315 1.00 38.56 ? 82 PRO A O 1 ATOM 672 C CB . PRO A 1 82 ? 1.105 -10.960 48.093 1.00 40.83 ? 82 PRO A CB 1 ATOM 673 C CG . PRO A 1 82 ? 0.623 -11.285 46.702 1.00 40.81 ? 82 PRO A CG 1 ATOM 674 C CD . PRO A 1 82 ? 1.908 -11.617 45.985 1.00 41.24 ? 82 PRO A CD 1 ATOM 675 N N . GLU A 1 83 ? 1.168 -14.237 48.314 1.00 39.54 ? 83 GLU A N 1 ATOM 676 C CA . GLU A 1 83 ? 0.643 -15.469 48.895 1.00 39.24 ? 83 GLU A CA 1 ATOM 677 C C . GLU A 1 83 ? 1.737 -16.109 49.738 1.00 37.71 ? 83 GLU A C 1 ATOM 678 O O . GLU A 1 83 ? 1.467 -16.705 50.779 1.00 36.46 ? 83 GLU A O 1 ATOM 679 C CB . GLU A 1 83 ? 0.224 -16.470 47.811 1.00 41.28 ? 83 GLU A CB 1 ATOM 680 C CG . GLU A 1 83 ? -0.149 -15.868 46.470 1.00 47.44 ? 83 GLU A CG 1 ATOM 681 C CD . GLU A 1 83 ? 1.066 -15.591 45.601 1.00 49.68 ? 83 GLU A CD 1 ATOM 682 O OE1 . GLU A 1 83 ? 1.864 -16.529 45.377 1.00 51.69 ? 83 GLU A OE1 1 ATOM 683 O OE2 . GLU A 1 83 ? 1.219 -14.444 45.135 1.00 50.48 ? 83 GLU A OE2 1 ATOM 684 N N . ARG A 1 84 ? 2.976 -15.989 49.270 1.00 36.50 ? 84 ARG A N 1 ATOM 685 C CA . ARG A 1 84 ? 4.117 -16.550 49.981 1.00 37.19 ? 84 ARG A CA 1 ATOM 686 C C . ARG A 1 84 ? 4.305 -15.857 51.328 1.00 36.36 ? 84 ARG A C 1 ATOM 687 O O . ARG A 1 84 ? 4.660 -16.498 52.319 1.00 35.96 ? 84 ARG A O 1 ATOM 688 C CB . ARG A 1 84 ? 5.378 -16.411 49.128 1.00 39.26 ? 84 ARG A CB 1 ATOM 689 C CG . ARG A 1 84 ? 5.291 -17.146 47.799 1.00 41.55 ? 84 ARG A CG 1 ATOM 690 C CD . ARG A 1 84 ? 6.523 -16.894 46.954 1.00 44.23 ? 84 ARG A CD 1 ATOM 691 N NE . ARG A 1 84 ? 7.740 -17.327 47.634 1.00 45.82 ? 84 ARG A NE 1 ATOM 692 C CZ . ARG A 1 84 ? 8.967 -16.980 47.258 1.00 46.10 ? 84 ARG A CZ 1 ATOM 693 N NH1 . ARG A 1 84 ? 9.140 -16.194 46.204 1.00 47.75 ? 84 ARG A NH1 1 ATOM 694 N NH2 . ARG A 1 84 ? 10.019 -17.411 47.939 1.00 46.17 ? 84 ARG A NH2 1 ATOM 695 N N . PHE A 1 85 ? 4.065 -14.550 51.369 1.00 33.69 ? 85 PHE A N 1 ATOM 696 C CA . PHE A 1 85 ? 4.198 -13.814 52.620 1.00 32.98 ? 85 PHE A CA 1 ATOM 697 C C . PHE A 1 85 ? 3.083 -14.278 53.533 1.00 31.76 ? 85 PHE A C 1 ATOM 698 O O . PHE A 1 85 ? 3.291 -14.564 54.711 1.00 30.45 ? 85 PHE A O 1 ATOM 699 C CB . PHE A 1 85 ? 4.063 -12.305 52.379 1.00 34.34 ? 85 PHE A CB 1 ATOM 700 C CG . PHE A 1 85 ? 5.335 -11.545 52.604 1.00 33.69 ? 85 PHE A CG 1 ATOM 701 C CD1 . PHE A 1 85 ? 5.963 -11.572 53.847 1.00 33.82 ? 85 PHE A CD1 1 ATOM 702 C CD2 . PHE A 1 85 ? 5.923 -10.832 51.567 1.00 34.03 ? 85 PHE A CD2 1 ATOM 703 C CE1 . PHE A 1 85 ? 7.168 -10.903 54.056 1.00 34.82 ? 85 PHE A CE1 1 ATOM 704 C CE2 . PHE A 1 85 ? 7.128 -10.157 51.759 1.00 30.57 ? 85 PHE A CE2 1 ATOM 705 C CZ . PHE A 1 85 ? 7.751 -10.194 53.006 1.00 33.54 ? 85 PHE A CZ 1 ATOM 706 N N . SER A 1 86 ? 1.889 -14.357 52.965 1.00 31.80 ? 86 SER A N 1 ATOM 707 C CA . SER A 1 86 ? 0.715 -14.778 53.709 1.00 33.99 ? 86 SER A CA 1 ATOM 708 C C . SER A 1 86 ? 0.952 -16.118 54.401 1.00 34.11 ? 86 SER A C 1 ATOM 709 O O . SER A 1 86 ? 0.650 -16.283 55.581 1.00 32.95 ? 86 SER A O 1 ATOM 710 C CB . SER A 1 86 ? -0.480 -14.879 52.759 1.00 33.53 ? 86 SER A CB 1 ATOM 711 O OG . SER A 1 86 ? -1.675 -15.107 53.473 1.00 37.53 ? 86 SER A OG 1 ATOM 712 N N . LYS A 1 87 ? 1.510 -17.067 53.660 1.00 34.43 ? 87 LYS A N 1 ATOM 713 C CA . LYS A 1 87 ? 1.780 -18.400 54.186 1.00 37.41 ? 87 LYS A CA 1 ATOM 714 C C . LYS A 1 87 ? 2.790 -18.399 55.332 1.00 36.29 ? 87 LYS A C 1 ATOM 715 O O . LYS A 1 87 ? 2.611 -19.106 56.326 1.00 34.41 ? 87 LYS A O 1 ATOM 716 C CB . LYS A 1 87 ? 2.274 -19.302 53.054 1.00 40.38 ? 87 LYS A CB 1 ATOM 717 C CG . LYS A 1 87 ? 2.519 -20.741 53.463 1.00 47.33 ? 87 LYS A CG 1 ATOM 718 C CD . LYS A 1 87 ? 2.679 -21.633 52.240 1.00 51.36 ? 87 LYS A CD 1 ATOM 719 C CE . LYS A 1 87 ? 1.394 -21.676 51.423 1.00 53.95 ? 87 LYS A CE 1 ATOM 720 N NZ . LYS A 1 87 ? 0.256 -22.239 52.204 1.00 55.45 ? 87 LYS A NZ 1 ATOM 721 N N . ILE A 1 88 ? 3.851 -17.608 55.198 1.00 35.11 ? 88 ILE A N 1 ATOM 722 C CA . ILE A 1 88 ? 4.872 -17.537 56.236 1.00 33.09 ? 88 ILE A CA 1 ATOM 723 C C . ILE A 1 88 ? 4.356 -16.884 57.515 1.00 32.93 ? 88 ILE A C 1 ATOM 724 O O . ILE A 1 88 ? 4.599 -17.376 58.616 1.00 31.66 ? 88 ILE A O 1 ATOM 725 C CB . ILE A 1 88 ? 6.108 -16.749 55.737 1.00 35.47 ? 88 ILE A CB 1 ATOM 726 C CG1 . ILE A 1 88 ? 6.795 -17.524 54.612 1.00 35.45 ? 88 ILE A CG1 1 ATOM 727 C CG2 . ILE A 1 88 ? 7.090 -16.508 56.880 1.00 36.14 ? 88 ILE A CG2 1 ATOM 728 C CD1 . ILE A 1 88 ? 7.886 -16.746 53.895 1.00 39.39 ? 88 ILE A CD1 1 ATOM 729 N N . ALA A 1 89 ? 3.626 -15.783 57.368 1.00 32.96 ? 89 ALA A N 1 ATOM 730 C CA . ALA A 1 89 ? 3.108 -15.054 58.521 1.00 32.67 ? 89 ALA A CA 1 ATOM 731 C C . ALA A 1 89 ? 1.919 -15.693 59.252 1.00 33.38 ? 89 ALA A C 1 ATOM 732 O O . ALA A 1 89 ? 1.699 -15.426 60.437 1.00 32.71 ? 89 ALA A O 1 ATOM 733 C CB . ALA A 1 89 ? 2.747 -13.624 58.097 1.00 30.95 ? 89 ALA A CB 1 ATOM 734 N N . SER A 1 90 ? 1.159 -16.531 58.550 1.00 35.52 ? 90 SER A N 1 ATOM 735 C CA . SER A 1 90 ? -0.022 -17.183 59.124 1.00 37.87 ? 90 SER A CA 1 ATOM 736 C C . SER A 1 90 ? 0.258 -18.233 60.193 1.00 38.92 ? 90 SER A C 1 ATOM 737 O O . SER A 1 90 ? -0.569 -18.458 61.076 1.00 39.32 ? 90 SER A O 1 ATOM 738 C CB . SER A 1 90 ? -0.844 -17.853 58.022 1.00 38.00 ? 90 SER A CB 1 ATOM 739 O OG . SER A 1 90 ? -1.206 -16.933 57.014 1.00 44.20 ? 90 SER A OG 1 ATOM 740 N N . LYS A 1 91 ? 1.408 -18.889 60.096 1.00 40.37 ? 91 LYS A N 1 ATOM 741 C CA . LYS A 1 91 ? 1.774 -19.940 61.042 1.00 42.26 ? 91 LYS A CA 1 ATOM 742 C C . LYS A 1 91 ? 2.846 -19.469 62.005 1.00 41.53 ? 91 LYS A C 1 ATOM 743 O O . LYS A 1 91 ? 3.953 -19.129 61.592 1.00 40.69 ? 91 LYS A O 1 ATOM 744 C CB . LYS A 1 91 ? 2.289 -21.161 60.281 1.00 44.27 ? 91 LYS A CB 1 ATOM 745 C CG . LYS A 1 91 ? 1.341 -21.671 59.210 1.00 48.32 ? 91 LYS A CG 1 ATOM 746 C CD . LYS A 1 91 ? 2.094 -22.478 58.159 1.00 51.52 ? 91 LYS A CD 1 ATOM 747 C CE . LYS A 1 91 ? 1.149 -23.083 57.126 1.00 53.53 ? 91 LYS A CE 1 ATOM 748 N NZ . LYS A 1 91 ? 0.306 -22.064 56.432 1.00 54.44 ? 91 LYS A NZ 1 ATOM 749 N N . THR A 1 92 ? 2.525 -19.471 63.292 1.00 42.03 ? 92 THR A N 1 ATOM 750 C CA . THR A 1 92 ? 3.481 -19.032 64.299 1.00 43.56 ? 92 THR A CA 1 ATOM 751 C C . THR A 1 92 ? 4.836 -19.726 64.156 1.00 42.69 ? 92 THR A C 1 ATOM 752 O O . THR A 1 92 ? 5.873 -19.128 64.447 1.00 42.94 ? 92 THR A O 1 ATOM 753 C CB . THR A 1 92 ? 2.949 -19.275 65.727 1.00 43.54 ? 92 THR A CB 1 ATOM 754 O OG1 . THR A 1 92 ? 2.942 -20.679 66.005 1.00 48.49 ? 92 THR A OG1 1 ATOM 755 C CG2 . THR A 1 92 ? 1.534 -18.715 65.867 1.00 44.48 ? 92 THR A CG2 1 ATOM 756 N N . GLN A 1 93 ? 4.829 -20.974 63.691 1.00 41.62 ? 93 GLN A N 1 ATOM 757 C CA . GLN A 1 93 ? 6.069 -21.734 63.539 1.00 42.03 ? 93 GLN A CA 1 ATOM 758 C C . GLN A 1 93 ? 6.947 -21.239 62.386 1.00 39.53 ? 93 GLN A C 1 ATOM 759 O O . GLN A 1 93 ? 8.151 -21.063 62.553 1.00 37.83 ? 93 GLN A O 1 ATOM 760 C CB . GLN A 1 93 ? 5.756 -23.234 63.373 1.00 46.20 ? 93 GLN A CB 1 ATOM 761 C CG . GLN A 1 93 ? 5.625 -23.731 61.933 1.00 52.83 ? 93 GLN A CG 1 ATOM 762 C CD . GLN A 1 93 ? 4.433 -24.658 61.725 1.00 56.64 ? 93 GLN A CD 1 ATOM 763 O OE1 . GLN A 1 93 ? 4.174 -25.560 62.528 1.00 58.07 ? 93 GLN A OE1 1 ATOM 764 N NE2 . GLN A 1 93 ? 3.709 -24.446 60.630 1.00 59.15 ? 93 GLN A NE2 1 ATOM 765 N N . SER A 1 94 ? 6.359 -21.016 61.217 1.00 36.46 ? 94 SER A N 1 ATOM 766 C CA . SER A 1 94 ? 7.140 -20.538 60.085 1.00 35.51 ? 94 SER A CA 1 ATOM 767 C C . SER A 1 94 ? 7.518 -19.074 60.313 1.00 35.01 ? 94 SER A C 1 ATOM 768 O O . SER A 1 94 ? 8.595 -18.624 59.922 1.00 33.18 ? 94 SER A O 1 ATOM 769 C CB . SER A 1 94 ? 6.344 -20.693 58.786 1.00 35.00 ? 94 SER A CB 1 ATOM 770 O OG . SER A 1 94 ? 4.998 -20.296 58.967 1.00 39.69 ? 94 SER A OG 1 ATOM 771 N N . ARG A 1 95 ? 6.628 -18.336 60.964 1.00 34.17 ? 95 ARG A N 1 ATOM 772 C CA . ARG A 1 95 ? 6.881 -16.930 61.244 1.00 33.89 ? 95 ARG A CA 1 ATOM 773 C C . ARG A 1 95 ? 8.108 -16.753 62.145 1.00 33.88 ? 95 ARG A C 1 ATOM 774 O O . ARG A 1 95 ? 8.958 -15.899 61.885 1.00 30.75 ? 95 ARG A O 1 ATOM 775 C CB . ARG A 1 95 ? 5.656 -16.297 61.904 1.00 32.76 ? 95 ARG A CB 1 ATOM 776 C CG . ARG A 1 95 ? 5.751 -14.788 62.067 1.00 33.12 ? 95 ARG A CG 1 ATOM 777 C CD . ARG A 1 95 ? 4.411 -14.182 62.458 1.00 33.65 ? 95 ARG A CD 1 ATOM 778 N NE . ARG A 1 95 ? 4.043 -14.468 63.841 1.00 35.77 ? 95 ARG A NE 1 ATOM 779 C CZ . ARG A 1 95 ? 2.900 -15.042 64.208 1.00 37.65 ? 95 ARG A CZ 1 ATOM 780 N NH1 . ARG A 1 95 ? 2.008 -15.399 63.292 1.00 36.96 ? 95 ARG A NH1 1 ATOM 781 N NH2 . ARG A 1 95 ? 2.642 -15.246 65.493 1.00 37.97 ? 95 ARG A NH2 1 ATOM 782 N N . ARG A 1 96 ? 8.195 -17.564 63.198 1.00 33.82 ? 96 ARG A N 1 ATOM 783 C CA . ARG A 1 96 ? 9.308 -17.507 64.144 1.00 34.73 ? 96 ARG A CA 1 ATOM 784 C C . ARG A 1 96 ? 10.635 -17.906 63.505 1.00 33.42 ? 96 ARG A C 1 ATOM 785 O O . ARG A 1 96 ? 11.686 -17.349 63.835 1.00 31.28 ? 96 ARG A O 1 ATOM 786 C CB . ARG A 1 96 ? 9.045 -18.429 65.337 1.00 39.53 ? 96 ARG A CB 1 ATOM 787 C CG . ARG A 1 96 ? 10.075 -18.299 66.455 1.00 47.62 ? 96 ARG A CG 1 ATOM 788 C CD . ARG A 1 96 ? 10.435 -19.651 67.060 1.00 54.23 ? 96 ARG A CD 1 ATOM 789 N NE . ARG A 1 96 ? 11.075 -20.523 66.076 1.00 60.99 ? 96 ARG A NE 1 ATOM 790 C CZ . ARG A 1 96 ? 10.529 -21.635 65.592 1.00 63.16 ? 96 ARG A CZ 1 ATOM 791 N NH1 . ARG A 1 96 ? 9.327 -22.021 66.003 1.00 64.50 ? 96 ARG A NH1 1 ATOM 792 N NH2 . ARG A 1 96 ? 11.180 -22.353 64.686 1.00 63.70 ? 96 ARG A NH2 1 ATOM 793 N N . THR A 1 97 ? 10.589 -18.890 62.612 1.00 31.38 ? 97 THR A N 1 ATOM 794 C CA . THR A 1 97 ? 11.792 -19.352 61.934 1.00 30.90 ? 97 THR A CA 1 ATOM 795 C C . THR A 1 97 ? 12.354 -18.216 61.078 1.00 29.49 ? 97 THR A C 1 ATOM 796 O O . THR A 1 97 ? 13.554 -17.938 61.106 1.00 26.59 ? 97 THR A O 1 ATOM 797 C CB . THR A 1 97 ? 11.478 -20.578 61.044 1.00 31.72 ? 97 THR A CB 1 ATOM 798 O OG1 . THR A 1 97 ? 11.045 -21.668 61.872 1.00 35.37 ? 97 THR A OG1 1 ATOM 799 C CG2 . THR A 1 97 ? 12.704 -20.995 60.246 1.00 31.97 ? 97 THR A CG2 1 ATOM 800 N N . PHE A 1 98 ? 11.477 -17.552 60.333 1.00 26.72 ? 98 PHE A N 1 ATOM 801 C CA . PHE A 1 98 ? 11.896 -16.446 59.485 1.00 27.19 ? 98 PHE A CA 1 ATOM 802 C C . PHE A 1 98 ? 12.489 -15.312 60.327 1.00 25.70 ? 98 PHE A C 1 ATOM 803 O O . PHE A 1 98 ? 13.576 -14.816 60.043 1.00 27.40 ? 98 PHE A O 1 ATOM 804 C CB . PHE A 1 98 ? 10.704 -15.939 58.671 1.00 26.83 ? 98 PHE A CB 1 ATOM 805 C CG . PHE A 1 98 ? 10.981 -14.670 57.916 1.00 27.72 ? 98 PHE A CG 1 ATOM 806 C CD1 . PHE A 1 98 ? 12.011 -14.610 56.979 1.00 26.30 ? 98 PHE A CD1 1 ATOM 807 C CD2 . PHE A 1 98 ? 10.233 -13.523 58.172 1.00 26.87 ? 98 PHE A CD2 1 ATOM 808 C CE1 . PHE A 1 98 ? 12.297 -13.420 56.312 1.00 27.17 ? 98 PHE A CE1 1 ATOM 809 C CE2 . PHE A 1 98 ? 10.507 -12.326 57.512 1.00 26.66 ? 98 PHE A CE2 1 ATOM 810 C CZ . PHE A 1 98 ? 11.541 -12.272 56.581 1.00 26.69 ? 98 PHE A CZ 1 ATOM 811 N N . ILE A 1 99 ? 11.778 -14.918 61.375 1.00 26.14 ? 99 ILE A N 1 ATOM 812 C CA . ILE A 1 99 ? 12.240 -13.844 62.245 1.00 25.93 ? 99 ILE A CA 1 ATOM 813 C C . ILE A 1 99 ? 13.629 -14.121 62.814 1.00 28.15 ? 99 ILE A C 1 ATOM 814 O O . ILE A 1 99 ? 14.492 -13.240 62.828 1.00 26.59 ? 99 ILE A O 1 ATOM 815 C CB . ILE A 1 99 ? 11.239 -13.610 63.405 1.00 26.25 ? 99 ILE A CB 1 ATOM 816 C CG1 . ILE A 1 99 ? 9.950 -12.992 62.849 1.00 23.89 ? 99 ILE A CG1 1 ATOM 817 C CG2 . ILE A 1 99 ? 11.847 -12.700 64.467 1.00 24.02 ? 99 ILE A CG2 1 ATOM 818 C CD1 . ILE A 1 99 ? 8.836 -12.863 63.872 1.00 25.11 ? 99 ILE A CD1 1 ATOM 819 N N . LYS A 1 100 ? 13.839 -15.347 63.278 1.00 27.57 ? 100 LYS A N 1 ATOM 820 C CA . LYS A 1 100 ? 15.116 -15.752 63.850 1.00 28.56 ? 100 LYS A CA 1 ATOM 821 C C . LYS A 1 100 ? 16.287 -15.708 62.869 1.00 25.98 ? 100 LYS A C 1 ATOM 822 O O . LYS A 1 100 ? 17.427 -15.480 63.271 1.00 25.93 ? 100 LYS A O 1 ATOM 823 C CB . LYS A 1 100 ? 15.000 -17.170 64.425 1.00 31.03 ? 100 LYS A CB 1 ATOM 824 C CG . LYS A 1 100 ? 14.397 -17.233 65.814 1.00 37.48 ? 100 LYS A CG 1 ATOM 825 C CD . LYS A 1 100 ? 15.350 -16.611 66.817 1.00 42.70 ? 100 LYS A CD 1 ATOM 826 C CE . LYS A 1 100 ? 14.810 -16.681 68.234 1.00 45.36 ? 100 LYS A CE 1 ATOM 827 N NZ . LYS A 1 100 ? 15.796 -16.093 69.181 1.00 46.53 ? 100 LYS A NZ 1 ATOM 828 N N . SER A 1 101 ? 16.009 -15.923 61.588 1.00 24.20 ? 101 SER A N 1 ATOM 829 C CA . SER A 1 101 ? 17.060 -15.937 60.569 1.00 23.53 ? 101 SER A CA 1 ATOM 830 C C . SER A 1 101 ? 17.540 -14.558 60.150 1.00 23.17 ? 101 SER A C 1 ATOM 831 O O . SER A 1 101 ? 18.646 -14.412 59.632 1.00 21.22 ? 101 SER A O 1 ATOM 832 C CB . SER A 1 101 ? 16.568 -16.650 59.313 1.00 24.28 ? 101 SER A CB 1 ATOM 833 O OG . SER A 1 101 ? 15.636 -15.827 58.625 1.00 23.14 ? 101 SER A OG 1 ATOM 834 N N . VAL A 1 102 ? 16.720 -13.541 60.379 1.00 21.86 ? 102 VAL A N 1 ATOM 835 C CA . VAL A 1 102 ? 17.073 -12.197 59.942 1.00 23.82 ? 102 VAL A CA 1 ATOM 836 C C . VAL A 1 102 ? 18.290 -11.500 60.558 1.00 22.70 ? 102 VAL A C 1 ATOM 837 O O . VAL A 1 102 ? 19.207 -11.109 59.837 1.00 25.36 ? 102 VAL A O 1 ATOM 838 C CB . VAL A 1 102 ? 15.836 -11.270 60.035 1.00 23.87 ? 102 VAL A CB 1 ATOM 839 C CG1 . VAL A 1 102 ? 16.231 -9.816 59.753 1.00 23.49 ? 102 VAL A CG1 1 ATOM 840 C CG2 . VAL A 1 102 ? 14.791 -11.742 59.026 1.00 21.31 ? 102 VAL A CG2 1 ATOM 841 N N . PRO A 1 103 ? 18.322 -11.332 61.890 1.00 23.24 ? 103 PRO A N 1 ATOM 842 C CA . PRO A 1 103 ? 19.470 -10.660 62.517 1.00 23.93 ? 103 PRO A CA 1 ATOM 843 C C . PRO A 1 103 ? 20.868 -11.145 62.102 1.00 24.48 ? 103 PRO A C 1 ATOM 844 O O . PRO A 1 103 ? 21.735 -10.336 61.752 1.00 23.43 ? 103 PRO A O 1 ATOM 845 C CB . PRO A 1 103 ? 19.203 -10.851 64.005 1.00 23.13 ? 103 PRO A CB 1 ATOM 846 C CG . PRO A 1 103 ? 17.696 -10.772 64.065 1.00 24.24 ? 103 PRO A CG 1 ATOM 847 C CD . PRO A 1 103 ? 17.284 -11.644 62.890 1.00 22.05 ? 103 PRO A CD 1 ATOM 848 N N . PRO A 1 104 ? 21.109 -12.468 62.141 1.00 25.21 ? 104 PRO A N 1 ATOM 849 C CA . PRO A 1 104 ? 22.431 -12.984 61.756 1.00 24.60 ? 104 PRO A CA 1 ATOM 850 C C . PRO A 1 104 ? 22.786 -12.665 60.300 1.00 22.90 ? 104 PRO A C 1 ATOM 851 O O . PRO A 1 104 ? 23.938 -12.373 59.976 1.00 21.42 ? 104 PRO A O 1 ATOM 852 C CB . PRO A 1 104 ? 22.298 -14.497 61.989 1.00 25.55 ? 104 PRO A CB 1 ATOM 853 C CG . PRO A 1 104 ? 21.255 -14.596 63.077 1.00 28.48 ? 104 PRO A CG 1 ATOM 854 C CD . PRO A 1 104 ? 20.243 -13.552 62.641 1.00 24.67 ? 104 PRO A CD 1 ATOM 855 N N . PHE A 1 105 ? 21.791 -12.739 59.426 1.00 19.36 ? 105 PHE A N 1 ATOM 856 C CA . PHE A 1 105 ? 21.992 -12.468 58.003 1.00 21.18 ? 105 PHE A CA 1 ATOM 857 C C . PHE A 1 105 ? 22.389 -11.005 57.785 1.00 21.90 ? 105 PHE A C 1 ATOM 858 O O . PHE A 1 105 ? 23.349 -10.707 57.071 1.00 21.67 ? 105 PHE A O 1 ATOM 859 C CB . PHE A 1 105 ? 20.700 -12.767 57.240 1.00 20.84 ? 105 PHE A CB 1 ATOM 860 C CG . PHE A 1 105 ? 20.876 -12.831 55.750 1.00 24.04 ? 105 PHE A CG 1 ATOM 861 C CD1 . PHE A 1 105 ? 21.444 -13.959 55.154 1.00 27.03 ? 105 PHE A CD1 1 ATOM 862 C CD2 . PHE A 1 105 ? 20.483 -11.764 54.941 1.00 22.87 ? 105 PHE A CD2 1 ATOM 863 C CE1 . PHE A 1 105 ? 21.622 -14.030 53.766 1.00 28.64 ? 105 PHE A CE1 1 ATOM 864 C CE2 . PHE A 1 105 ? 20.652 -11.815 53.552 1.00 25.84 ? 105 PHE A CE2 1 ATOM 865 C CZ . PHE A 1 105 ? 21.225 -12.954 52.960 1.00 28.24 ? 105 PHE A CZ 1 ATOM 866 N N . LEU A 1 106 ? 21.636 -10.098 58.401 1.00 21.52 ? 106 LEU A N 1 ATOM 867 C CA . LEU A 1 106 ? 21.896 -8.660 58.299 1.00 22.46 ? 106 LEU A CA 1 ATOM 868 C C . LEU A 1 106 ? 23.283 -8.320 58.837 1.00 22.26 ? 106 LEU A C 1 ATOM 869 O O . LEU A 1 106 ? 24.042 -7.580 58.219 1.00 19.44 ? 106 LEU A O 1 ATOM 870 C CB . LEU A 1 106 ? 20.823 -7.888 59.083 1.00 20.63 ? 106 LEU A CB 1 ATOM 871 C CG . LEU A 1 106 ? 19.577 -7.427 58.304 1.00 25.90 ? 106 LEU A CG 1 ATOM 872 C CD1 . LEU A 1 106 ? 19.227 -8.405 57.197 1.00 24.77 ? 106 LEU A CD1 1 ATOM 873 C CD2 . LEU A 1 106 ? 18.408 -7.239 59.265 1.00 21.90 ? 106 LEU A CD2 1 ATOM 874 N N . ARG A 1 107 ? 23.594 -8.872 60.004 1.00 22.53 ? 107 ARG A N 1 ATOM 875 C CA . ARG A 1 107 ? 24.877 -8.656 60.660 1.00 26.48 ? 107 ARG A CA 1 ATOM 876 C C . ARG A 1 107 ? 26.041 -9.153 59.787 1.00 27.06 ? 107 ARG A C 1 ATOM 877 O O . ARG A 1 107 ? 27.061 -8.478 59.639 1.00 27.07 ? 107 ARG A O 1 ATOM 878 C CB . ARG A 1 107 ? 24.885 -9.386 62.010 1.00 27.05 ? 107 ARG A CB 1 ATOM 879 C CG . ARG A 1 107 ? 24.968 -8.501 63.255 1.00 32.32 ? 107 ARG A CG 1 ATOM 880 C CD . ARG A 1 107 ? 23.672 -7.786 63.628 1.00 33.12 ? 107 ARG A CD 1 ATOM 881 N NE . ARG A 1 107 ? 23.832 -6.343 63.504 1.00 36.39 ? 107 ARG A NE 1 ATOM 882 C CZ . ARG A 1 107 ? 23.313 -5.434 64.324 1.00 33.82 ? 107 ARG A CZ 1 ATOM 883 N NH1 . ARG A 1 107 ? 22.580 -5.793 65.365 1.00 33.88 ? 107 ARG A NH1 1 ATOM 884 N NH2 . ARG A 1 107 ? 23.544 -4.150 64.095 1.00 33.28 ? 107 ARG A NH2 1 ATOM 885 N N . THR A 1 108 ? 25.881 -10.338 59.210 1.00 25.49 ? 108 THR A N 1 ATOM 886 C CA . THR A 1 108 ? 26.915 -10.922 58.366 1.00 28.19 ? 108 THR A CA 1 ATOM 887 C C . THR A 1 108 ? 27.198 -10.089 57.121 1.00 27.99 ? 108 THR A C 1 ATOM 888 O O . THR A 1 108 ? 28.347 -9.962 56.696 1.00 26.77 ? 108 THR A O 1 ATOM 889 C CB . THR A 1 108 ? 26.524 -12.345 57.909 1.00 29.00 ? 108 THR A CB 1 ATOM 890 O OG1 . THR A 1 108 ? 26.346 -13.182 59.059 1.00 30.02 ? 108 THR A OG1 1 ATOM 891 C CG2 . THR A 1 108 ? 27.605 -12.933 57.009 1.00 30.60 ? 108 THR A CG2 1 ATOM 892 N N . HIS A 1 109 ? 26.159 -9.505 56.536 1.00 24.81 ? 109 HIS A N 1 ATOM 893 C CA . HIS A 1 109 ? 26.363 -8.726 55.325 1.00 25.34 ? 109 HIS A CA 1 ATOM 894 C C . HIS A 1 109 ? 26.464 -7.218 55.518 1.00 25.57 ? 109 HIS A C 1 ATOM 895 O O . HIS A 1 109 ? 26.548 -6.461 54.546 1.00 24.78 ? 109 HIS A O 1 ATOM 896 C CB . HIS A 1 109 ? 25.286 -9.096 54.312 1.00 24.38 ? 109 HIS A CB 1 ATOM 897 C CG . HIS A 1 109 ? 25.368 -10.528 53.872 1.00 29.40 ? 109 HIS A CG 1 ATOM 898 N ND1 . HIS A 1 109 ? 26.399 -11.008 53.091 1.00 30.89 ? 109 HIS A ND1 1 ATOM 899 C CD2 . HIS A 1 109 ? 24.578 -11.593 54.147 1.00 26.10 ? 109 HIS A CD2 1 ATOM 900 C CE1 . HIS A 1 109 ? 26.239 -12.306 52.903 1.00 29.65 ? 109 HIS A CE1 1 ATOM 901 N NE2 . HIS A 1 109 ? 25.141 -12.685 53.533 1.00 29.61 ? 109 HIS A NE2 1 ATOM 902 N N . GLY A 1 110 ? 26.450 -6.789 56.777 1.00 23.79 ? 110 GLY A N 1 ATOM 903 C CA . GLY A 1 110 ? 26.616 -5.379 57.094 1.00 24.74 ? 110 GLY A CA 1 ATOM 904 C C . GLY A 1 110 ? 25.451 -4.414 56.995 1.00 24.38 ? 110 GLY A C 1 ATOM 905 O O . GLY A 1 110 ? 25.673 -3.204 56.928 1.00 22.93 ? 110 GLY A O 1 ATOM 906 N N . PHE A 1 111 ? 24.221 -4.922 57.012 1.00 21.28 ? 111 PHE A N 1 ATOM 907 C CA . PHE A 1 111 ? 23.047 -4.060 56.937 1.00 21.69 ? 111 PHE A CA 1 ATOM 908 C C . PHE A 1 111 ? 22.653 -3.538 58.311 1.00 22.13 ? 111 PHE A C 1 ATOM 909 O O . PHE A 1 111 ? 22.929 -4.180 59.321 1.00 22.19 ? 111 PHE A O 1 ATOM 910 C CB . PHE A 1 111 ? 21.874 -4.821 56.311 1.00 21.01 ? 111 PHE A CB 1 ATOM 911 C CG . PHE A 1 111 ? 22.010 -5.018 54.827 1.00 19.32 ? 111 PHE A CG 1 ATOM 912 C CD1 . PHE A 1 111 ? 21.771 -3.962 53.955 1.00 19.64 ? 111 PHE A CD1 1 ATOM 913 C CD2 . PHE A 1 111 ? 22.390 -6.249 54.300 1.00 21.41 ? 111 PHE A CD2 1 ATOM 914 C CE1 . PHE A 1 111 ? 21.905 -4.119 52.578 1.00 20.40 ? 111 PHE A CE1 1 ATOM 915 C CE2 . PHE A 1 111 ? 22.530 -6.422 52.908 1.00 22.04 ? 111 PHE A CE2 1 ATOM 916 C CZ . PHE A 1 111 ? 22.286 -5.351 52.047 1.00 19.96 ? 111 PHE A CZ 1 ATOM 917 N N . ASP A 1 112 ? 21.993 -2.382 58.341 1.00 19.63 ? 112 ASP A N 1 ATOM 918 C CA . ASP A 1 112 ? 21.567 -1.771 59.595 1.00 19.22 ? 112 ASP A CA 1 ATOM 919 C C . ASP A 1 112 ? 20.097 -2.018 59.900 1.00 20.60 ? 112 ASP A C 1 ATOM 920 O O . ASP A 1 112 ? 19.583 -1.587 60.939 1.00 19.10 ? 112 ASP A O 1 ATOM 921 C CB . ASP A 1 112 ? 21.821 -0.265 59.554 1.00 22.08 ? 112 ASP A CB 1 ATOM 922 C CG . ASP A 1 112 ? 23.270 0.068 59.302 1.00 22.62 ? 112 ASP A CG 1 ATOM 923 O OD1 . ASP A 1 112 ? 24.095 -0.182 60.207 1.00 25.57 ? 112 ASP A OD1 1 ATOM 924 O OD2 . ASP A 1 112 ? 23.578 0.568 58.197 1.00 20.66 ? 112 ASP A OD2 1 ATOM 925 N N . GLY A 1 113 ? 19.410 -2.705 58.998 1.00 17.42 ? 113 GLY A N 1 ATOM 926 C CA . GLY A 1 113 ? 18.007 -2.962 59.244 1.00 18.26 ? 113 GLY A CA 1 ATOM 927 C C . GLY A 1 113 ? 17.311 -3.735 58.148 1.00 18.74 ? 113 GLY A C 1 ATOM 928 O O . GLY A 1 113 ? 17.896 -4.060 57.111 1.00 16.87 ? 113 GLY A O 1 ATOM 929 N N . LEU A 1 114 ? 16.039 -4.014 58.385 1.00 18.44 ? 114 LEU A N 1 ATOM 930 C CA . LEU A 1 114 ? 15.226 -4.771 57.448 1.00 18.12 ? 114 LEU A CA 1 ATOM 931 C C . LEU A 1 114 ? 14.031 -3.959 57.001 1.00 16.01 ? 114 LEU A C 1 ATOM 932 O O . LEU A 1 114 ? 13.374 -3.331 57.826 1.00 15.82 ? 114 LEU A O 1 ATOM 933 C CB . LEU A 1 114 ? 14.709 -6.034 58.128 1.00 17.63 ? 114 LEU A CB 1 ATOM 934 C CG . LEU A 1 114 ? 13.804 -6.911 57.266 1.00 18.53 ? 114 LEU A CG 1 ATOM 935 C CD1 . LEU A 1 114 ? 14.692 -7.732 56.337 1.00 20.25 ? 114 LEU A CD1 1 ATOM 936 C CD2 . LEU A 1 114 ? 12.959 -7.827 58.143 1.00 21.32 ? 114 LEU A CD2 1 ATOM 937 N N . ASP A 1 115 ? 13.747 -3.977 55.701 1.00 15.02 ? 115 ASP A N 1 ATOM 938 C CA . ASP A 1 115 ? 12.580 -3.275 55.167 1.00 17.08 ? 115 ASP A CA 1 ATOM 939 C C . ASP A 1 115 ? 11.599 -4.345 54.692 1.00 17.51 ? 115 ASP A C 1 ATOM 940 O O . ASP A 1 115 ? 11.984 -5.271 53.986 1.00 18.71 ? 115 ASP A O 1 ATOM 941 C CB . ASP A 1 115 ? 12.968 -2.373 53.995 1.00 15.58 ? 115 ASP A CB 1 ATOM 942 C CG . ASP A 1 115 ? 11.775 -1.658 53.391 1.00 19.46 ? 115 ASP A CG 1 ATOM 943 O OD1 . ASP A 1 115 ? 11.028 -1.003 54.152 1.00 15.88 ? 115 ASP A OD1 1 ATOM 944 O OD2 . ASP A 1 115 ? 11.586 -1.754 52.155 1.00 17.17 ? 115 ASP A OD2 1 ATOM 945 N N . LEU A 1 116 ? 10.337 -4.220 55.098 1.00 18.78 ? 116 LEU A N 1 ATOM 946 C CA . LEU A 1 116 ? 9.298 -5.179 54.717 1.00 20.06 ? 116 LEU A CA 1 ATOM 947 C C . LEU A 1 116 ? 8.488 -4.657 53.549 1.00 21.02 ? 116 LEU A C 1 ATOM 948 O O . LEU A 1 116 ? 7.868 -3.599 53.648 1.00 19.27 ? 116 LEU A O 1 ATOM 949 C CB . LEU A 1 116 ? 8.353 -5.435 55.894 1.00 22.61 ? 116 LEU A CB 1 ATOM 950 C CG . LEU A 1 116 ? 8.991 -6.138 57.090 1.00 25.15 ? 116 LEU A CG 1 ATOM 951 C CD1 . LEU A 1 116 ? 8.052 -6.097 58.278 1.00 28.51 ? 116 LEU A CD1 1 ATOM 952 C CD2 . LEU A 1 116 ? 9.331 -7.581 56.705 1.00 26.57 ? 116 LEU A CD2 1 ATOM 953 N N . ALA A 1 117 ? 8.499 -5.401 52.446 1.00 19.48 ? 117 ALA A N 1 ATOM 954 C CA . ALA A 1 117 ? 7.756 -5.011 51.254 1.00 22.84 ? 117 ALA A CA 1 ATOM 955 C C . ALA A 1 117 ? 6.740 -6.081 50.843 1.00 22.54 ? 117 ALA A C 1 ATOM 956 O O . ALA A 1 117 ? 6.857 -6.680 49.777 1.00 22.87 ? 117 ALA A O 1 ATOM 957 C CB . ALA A 1 117 ? 8.721 -4.730 50.095 1.00 20.42 ? 117 ALA A CB 1 ATOM 958 N N . TRP A 1 118 ? 5.750 -6.315 51.700 1.00 23.05 ? 118 TRP A N 1 ATOM 959 C CA . TRP A 1 118 ? 4.692 -7.290 51.434 1.00 23.12 ? 118 TRP A CA 1 ATOM 960 C C . TRP A 1 118 ? 3.665 -6.523 50.609 1.00 25.17 ? 118 TRP A C 1 ATOM 961 O O . TRP A 1 118 ? 3.005 -5.619 51.120 1.00 26.68 ? 118 TRP A O 1 ATOM 962 C CB . TRP A 1 118 ? 4.078 -7.757 52.765 1.00 24.29 ? 118 TRP A CB 1 ATOM 963 C CG . TRP A 1 118 ? 2.968 -8.805 52.678 1.00 25.49 ? 118 TRP A CG 1 ATOM 964 C CD1 . TRP A 1 118 ? 2.250 -9.163 51.570 1.00 25.30 ? 118 TRP A CD1 1 ATOM 965 C CD2 . TRP A 1 118 ? 2.420 -9.562 53.768 1.00 25.55 ? 118 TRP A CD2 1 ATOM 966 N NE1 . TRP A 1 118 ? 1.288 -10.092 51.904 1.00 26.91 ? 118 TRP A NE1 1 ATOM 967 C CE2 . TRP A 1 118 ? 1.372 -10.353 53.246 1.00 27.72 ? 118 TRP A CE2 1 ATOM 968 C CE3 . TRP A 1 118 ? 2.713 -9.648 55.137 1.00 25.89 ? 118 TRP A CE3 1 ATOM 969 C CZ2 . TRP A 1 118 ? 0.617 -11.217 54.044 1.00 27.58 ? 118 TRP A CZ2 1 ATOM 970 C CZ3 . TRP A 1 118 ? 1.960 -10.506 55.927 1.00 27.33 ? 118 TRP A CZ3 1 ATOM 971 C CH2 . TRP A 1 118 ? 0.924 -11.279 55.376 1.00 26.46 ? 118 TRP A CH2 1 ATOM 972 N N . LEU A 1 119 ? 3.529 -6.877 49.336 1.00 26.60 ? 119 LEU A N 1 ATOM 973 C CA . LEU A 1 119 ? 2.587 -6.183 48.456 1.00 31.23 ? 119 LEU A CA 1 ATOM 974 C C . LEU A 1 119 ? 1.619 -7.151 47.761 1.00 32.17 ? 119 LEU A C 1 ATOM 975 O O . LEU A 1 119 ? 1.978 -7.722 46.731 1.00 33.33 ? 119 LEU A O 1 ATOM 976 C CB . LEU A 1 119 ? 3.376 -5.424 47.387 1.00 30.91 ? 119 LEU A CB 1 ATOM 977 C CG . LEU A 1 119 ? 4.691 -4.751 47.817 1.00 31.73 ? 119 LEU A CG 1 ATOM 978 C CD1 . LEU A 1 119 ? 5.513 -4.411 46.582 1.00 31.10 ? 119 LEU A CD1 1 ATOM 979 C CD2 . LEU A 1 119 ? 4.416 -3.500 48.645 1.00 28.24 ? 119 LEU A CD2 1 ATOM 980 N N . TYR A 1 120 ? 0.400 -7.329 48.281 1.00 33.08 ? 120 TYR A N 1 ATOM 981 C CA . TYR A 1 120 ? -0.101 -6.656 49.479 1.00 33.67 ? 120 TYR A CA 1 ATOM 982 C C . TYR A 1 120 ? -0.862 -7.594 50.394 1.00 33.26 ? 120 TYR A C 1 ATOM 983 O O . TYR A 1 120 ? -1.311 -8.661 49.980 1.00 33.98 ? 120 TYR A O 1 ATOM 984 C CB . TYR A 1 120 ? -1.067 -5.535 49.113 1.00 34.77 ? 120 TYR A CB 1 ATOM 985 C CG . TYR A 1 120 ? -0.456 -4.490 48.243 1.00 36.58 ? 120 TYR A CG 1 ATOM 986 C CD1 . TYR A 1 120 ? -0.565 -4.558 46.855 1.00 37.20 ? 120 TYR A CD1 1 ATOM 987 C CD2 . TYR A 1 120 ? 0.263 -3.441 48.806 1.00 38.34 ? 120 TYR A CD2 1 ATOM 988 C CE1 . TYR A 1 120 ? 0.032 -3.599 46.048 1.00 38.38 ? 120 TYR A CE1 1 ATOM 989 C CE2 . TYR A 1 120 ? 0.864 -2.479 48.014 1.00 39.04 ? 120 TYR A CE2 1 ATOM 990 C CZ . TYR A 1 120 ? 0.746 -2.564 46.638 1.00 39.74 ? 120 TYR A CZ 1 ATOM 991 O OH . TYR A 1 120 ? 1.363 -1.616 45.863 1.00 43.33 ? 120 TYR A OH 1 ATOM 992 N N . PRO A 1 121 ? -1.021 -7.191 51.661 1.00 33.81 ? 121 PRO A N 1 ATOM 993 C CA . PRO A 1 121 ? -1.737 -7.968 52.676 1.00 33.88 ? 121 PRO A CA 1 ATOM 994 C C . PRO A 1 121 ? -3.222 -7.870 52.356 1.00 33.85 ? 121 PRO A C 1 ATOM 995 O O . PRO A 1 121 ? -3.714 -6.784 52.055 1.00 34.87 ? 121 PRO A O 1 ATOM 996 C CB . PRO A 1 121 ? -1.401 -7.239 53.979 1.00 34.02 ? 121 PRO A CB 1 ATOM 997 C CG . PRO A 1 121 ? -0.135 -6.473 53.658 1.00 36.41 ? 121 PRO A CG 1 ATOM 998 C CD . PRO A 1 121 ? -0.387 -6.004 52.263 1.00 33.41 ? 121 PRO A CD 1 ATOM 999 N N . GLY A 1 122 ? -3.928 -8.993 52.409 1.00 33.72 ? 122 GLY A N 1 ATOM 1000 C CA . GLY A 1 122 ? -5.351 -8.973 52.131 1.00 32.37 ? 122 GLY A CA 1 ATOM 1001 C C . GLY A 1 122 ? -6.099 -8.854 53.437 1.00 31.11 ? 122 GLY A C 1 ATOM 1002 O O . GLY A 1 122 ? -5.487 -8.669 54.488 1.00 29.51 ? 122 GLY A O 1 ATOM 1003 N N . ARG A 1 123 ? -7.421 -8.965 53.374 1.00 32.93 ? 123 ARG A N 1 ATOM 1004 C CA . ARG A 1 123 ? -8.258 -8.873 54.559 1.00 33.09 ? 123 ARG A CA 1 ATOM 1005 C C . ARG A 1 123 ? -7.877 -9.955 55.566 1.00 32.37 ? 123 ARG A C 1 ATOM 1006 O O . ARG A 1 123 ? -7.849 -9.713 56.769 1.00 31.39 ? 123 ARG A O 1 ATOM 1007 C CB . ARG A 1 123 ? -9.731 -9.032 54.170 1.00 38.27 ? 123 ARG A CB 1 ATOM 1008 C CG . ARG A 1 123 ? -10.709 -8.599 55.246 1.00 42.90 ? 123 ARG A CG 1 ATOM 1009 C CD . ARG A 1 123 ? -12.154 -8.884 54.855 1.00 47.28 ? 123 ARG A CD 1 ATOM 1010 N NE . ARG A 1 123 ? -12.473 -10.308 54.939 1.00 51.51 ? 123 ARG A NE 1 ATOM 1011 C CZ . ARG A 1 123 ? -12.300 -11.184 53.954 1.00 52.88 ? 123 ARG A CZ 1 ATOM 1012 N NH1 . ARG A 1 123 ? -11.810 -10.788 52.786 1.00 55.83 ? 123 ARG A NH1 1 ATOM 1013 N NH2 . ARG A 1 123 ? -12.619 -12.459 54.140 1.00 53.11 ? 123 ARG A NH2 1 ATOM 1014 N N . ARG A 1 124 ? -7.571 -11.149 55.069 1.00 32.55 ? 124 ARG A N 1 ATOM 1015 C CA . ARG A 1 124 ? -7.217 -12.261 55.944 1.00 33.69 ? 124 ARG A CA 1 ATOM 1016 C C . ARG A 1 124 ? -5.792 -12.182 56.488 1.00 34.05 ? 124 ARG A C 1 ATOM 1017 O O . ARG A 1 124 ? -5.422 -12.957 57.370 1.00 35.80 ? 124 ARG A O 1 ATOM 1018 C CB . ARG A 1 124 ? -7.407 -13.596 55.211 1.00 35.16 ? 124 ARG A CB 1 ATOM 1019 C CG . ARG A 1 124 ? -8.824 -13.865 54.704 1.00 35.46 ? 124 ARG A CG 1 ATOM 1020 C CD . ARG A 1 124 ? -9.058 -15.365 54.519 1.00 37.94 ? 124 ARG A CD 1 ATOM 1021 N NE . ARG A 1 124 ? -10.333 -15.662 53.867 1.00 38.47 ? 124 ARG A NE 1 ATOM 1022 C CZ . ARG A 1 124 ? -10.552 -15.514 52.564 1.00 40.16 ? 124 ARG A CZ 1 ATOM 1023 N NH1 . ARG A 1 124 ? -9.578 -15.071 51.777 1.00 40.01 ? 124 ARG A NH1 1 ATOM 1024 N NH2 . ARG A 1 124 ? -11.737 -15.814 52.046 1.00 39.64 ? 124 ARG A NH2 1 ATOM 1025 N N . ASP A 1 125 ? -5.005 -11.239 55.975 1.00 33.04 ? 125 ASP A N 1 ATOM 1026 C CA . ASP A 1 125 ? -3.613 -11.080 56.401 1.00 33.03 ? 125 ASP A CA 1 ATOM 1027 C C . ASP A 1 125 ? -3.363 -10.026 57.475 1.00 32.95 ? 125 ASP A C 1 ATOM 1028 O O . ASP A 1 125 ? -2.354 -10.090 58.177 1.00 32.34 ? 125 ASP A O 1 ATOM 1029 C CB . ASP A 1 125 ? -2.718 -10.743 55.202 1.00 32.47 ? 125 ASP A CB 1 ATOM 1030 C CG . ASP A 1 125 ? -2.795 -11.777 54.108 1.00 32.72 ? 125 ASP A CG 1 ATOM 1031 O OD1 . ASP A 1 125 ? -2.643 -12.976 54.417 1.00 31.29 ? 125 ASP A OD1 1 ATOM 1032 O OD2 . ASP A 1 125 ? -2.993 -11.386 52.937 1.00 30.76 ? 125 ASP A OD2 1 ATOM 1033 N N . LYS A 1 126 ? -4.268 -9.059 57.599 1.00 33.95 ? 126 LYS A N 1 ATOM 1034 C CA . LYS A 1 126 ? -4.097 -7.977 58.569 1.00 34.73 ? 126 LYS A CA 1 ATOM 1035 C C . LYS A 1 126 ? -3.589 -8.442 59.933 1.00 35.39 ? 126 LYS A C 1 ATOM 1036 O O . LYS A 1 126 ? -2.580 -7.935 60.428 1.00 32.65 ? 126 LYS A O 1 ATOM 1037 C CB . LYS A 1 126 ? -5.404 -7.195 58.741 1.00 35.38 ? 126 LYS A CB 1 ATOM 1038 C CG . LYS A 1 126 ? -5.273 -5.993 59.675 1.00 37.86 ? 126 LYS A CG 1 ATOM 1039 C CD . LYS A 1 126 ? -6.558 -5.179 59.770 1.00 39.69 ? 126 LYS A CD 1 ATOM 1040 C CE . LYS A 1 126 ? -6.852 -4.455 58.470 1.00 42.73 ? 126 LYS A CE 1 ATOM 1041 N NZ . LYS A 1 126 ? -8.068 -3.598 58.584 1.00 44.54 ? 126 LYS A NZ 1 ATOM 1042 N N . ARG A 1 127 ? -4.291 -9.409 60.521 1.00 34.07 ? 127 ARG A N 1 ATOM 1043 C CA . ARG A 1 127 ? -3.951 -9.984 61.823 1.00 36.06 ? 127 ARG A CA 1 ATOM 1044 C C . ARG A 1 127 ? -2.488 -10.429 61.890 1.00 32.83 ? 127 ARG A C 1 ATOM 1045 O O . ARG A 1 127 ? -1.756 -10.085 62.815 1.00 31.74 ? 127 ARG A O 1 ATOM 1046 C CB . ARG A 1 127 ? -4.843 -11.213 62.081 1.00 40.35 ? 127 ARG A CB 1 ATOM 1047 C CG . ARG A 1 127 ? -4.919 -11.670 63.535 1.00 48.08 ? 127 ARG A CG 1 ATOM 1048 C CD . ARG A 1 127 ? -4.775 -13.198 63.720 1.00 54.03 ? 127 ARG A CD 1 ATOM 1049 N NE . ARG A 1 127 ? -5.828 -13.998 63.090 1.00 58.26 ? 127 ARG A NE 1 ATOM 1050 C CZ . ARG A 1 127 ? -6.053 -15.283 63.367 1.00 60.02 ? 127 ARG A CZ 1 ATOM 1051 N NH1 . ARG A 1 127 ? -5.306 -15.914 64.265 1.00 60.83 ? 127 ARG A NH1 1 ATOM 1052 N NH2 . ARG A 1 127 ? -7.018 -15.945 62.740 1.00 62.15 ? 127 ARG A NH2 1 ATOM 1053 N N . HIS A 1 128 ? -2.083 -11.211 60.897 1.00 30.21 ? 128 HIS A N 1 ATOM 1054 C CA . HIS A 1 128 ? -0.741 -11.767 60.826 1.00 30.29 ? 128 HIS A CA 1 ATOM 1055 C C . HIS A 1 128 ? 0.365 -10.754 60.534 1.00 29.23 ? 128 HIS A C 1 ATOM 1056 O O . HIS A 1 128 ? 1.508 -10.943 60.953 1.00 27.58 ? 128 HIS A O 1 ATOM 1057 C CB . HIS A 1 128 ? -0.745 -12.886 59.790 1.00 32.07 ? 128 HIS A CB 1 ATOM 1058 C CG . HIS A 1 128 ? -1.876 -13.848 59.975 1.00 37.21 ? 128 HIS A CG 1 ATOM 1059 N ND1 . HIS A 1 128 ? -2.033 -14.593 61.125 1.00 39.04 ? 128 HIS A ND1 1 ATOM 1060 C CD2 . HIS A 1 128 ? -2.942 -14.137 59.192 1.00 38.60 ? 128 HIS A CD2 1 ATOM 1061 C CE1 . HIS A 1 128 ? -3.149 -15.296 61.043 1.00 40.08 ? 128 HIS A CE1 1 ATOM 1062 N NE2 . HIS A 1 128 ? -3.720 -15.036 59.881 1.00 41.13 ? 128 HIS A NE2 1 ATOM 1063 N N . LEU A 1 129 ? 0.028 -9.682 59.820 1.00 29.14 ? 129 LEU A N 1 ATOM 1064 C CA . LEU A 1 129 ? 1.011 -8.649 59.511 1.00 27.65 ? 129 LEU A CA 1 ATOM 1065 C C . LEU A 1 129 ? 1.408 -8.009 60.839 1.00 25.92 ? 129 LEU A C 1 ATOM 1066 O O . LEU A 1 129 ? 2.585 -7.817 61.123 1.00 24.80 ? 129 LEU A O 1 ATOM 1067 C CB . LEU A 1 129 ? 0.407 -7.584 58.591 1.00 28.33 ? 129 LEU A CB 1 ATOM 1068 C CG . LEU A 1 129 ? 1.326 -6.723 57.707 1.00 30.89 ? 129 LEU A CG 1 ATOM 1069 C CD1 . LEU A 1 129 ? 0.737 -5.327 57.630 1.00 31.57 ? 129 LEU A CD1 1 ATOM 1070 C CD2 . LEU A 1 129 ? 2.739 -6.644 58.256 1.00 31.15 ? 129 LEU A CD2 1 ATOM 1071 N N . THR A 1 130 ? 0.413 -7.683 61.653 1.00 25.03 ? 130 THR A N 1 ATOM 1072 C CA . THR A 1 130 ? 0.677 -7.070 62.946 1.00 27.89 ? 130 THR A CA 1 ATOM 1073 C C . THR A 1 130 ? 1.590 -7.959 63.792 1.00 27.16 ? 130 THR A C 1 ATOM 1074 O O . THR A 1 130 ? 2.564 -7.480 64.370 1.00 26.28 ? 130 THR A O 1 ATOM 1075 C CB . THR A 1 130 ? -0.637 -6.803 63.713 1.00 28.65 ? 130 THR A CB 1 ATOM 1076 O OG1 . THR A 1 130 ? -1.427 -5.850 62.988 1.00 29.25 ? 130 THR A OG1 1 ATOM 1077 C CG2 . THR A 1 130 ? -0.339 -6.271 65.112 1.00 28.50 ? 130 THR A CG2 1 ATOM 1078 N N . ALA A 1 131 ? 1.283 -9.253 63.845 1.00 26.70 ? 131 ALA A N 1 ATOM 1079 C CA . ALA A 1 131 ? 2.083 -10.199 64.620 1.00 27.60 ? 131 ALA A CA 1 ATOM 1080 C C . ALA A 1 131 ? 3.513 -10.242 64.089 1.00 26.15 ? 131 ALA A C 1 ATOM 1081 O O . ALA A 1 131 ? 4.474 -10.229 64.856 1.00 26.04 ? 131 ALA A O 1 ATOM 1082 C CB . ALA A 1 131 ? 1.454 -11.598 64.559 1.00 27.89 ? 131 ALA A CB 1 ATOM 1083 N N . LEU A 1 132 ? 3.645 -10.296 62.769 1.00 24.91 ? 132 LEU A N 1 ATOM 1084 C CA . LEU A 1 132 ? 4.955 -10.326 62.130 1.00 24.62 ? 132 LEU A CA 1 ATOM 1085 C C . LEU A 1 132 ? 5.820 -9.123 62.525 1.00 23.15 ? 132 LEU A C 1 ATOM 1086 O O . LEU A 1 132 ? 6.981 -9.280 62.899 1.00 23.33 ? 132 LEU A O 1 ATOM 1087 C CB . LEU A 1 132 ? 4.786 -10.367 60.611 1.00 25.25 ? 132 LEU A CB 1 ATOM 1088 C CG . LEU A 1 132 ? 6.046 -10.229 59.754 1.00 26.54 ? 132 LEU A CG 1 ATOM 1089 C CD1 . LEU A 1 132 ? 7.071 -11.281 60.154 1.00 24.46 ? 132 LEU A CD1 1 ATOM 1090 C CD2 . LEU A 1 132 ? 5.669 -10.368 58.280 1.00 28.46 ? 132 LEU A CD2 1 ATOM 1091 N N . VAL A 1 133 ? 5.244 -7.928 62.442 1.00 22.06 ? 133 VAL A N 1 ATOM 1092 C CA . VAL A 1 133 ? 5.947 -6.689 62.784 1.00 23.11 ? 133 VAL A CA 1 ATOM 1093 C C . VAL A 1 133 ? 6.308 -6.636 64.264 1.00 25.41 ? 133 VAL A C 1 ATOM 1094 O O . VAL A 1 133 ? 7.446 -6.320 64.639 1.00 24.24 ? 133 VAL A O 1 ATOM 1095 C CB . VAL A 1 133 ? 5.069 -5.458 62.431 1.00 23.45 ? 133 VAL A CB 1 ATOM 1096 C CG1 . VAL A 1 133 ? 5.664 -4.184 63.011 1.00 23.11 ? 133 VAL A CG1 1 ATOM 1097 C CG2 . VAL A 1 133 ? 4.945 -5.339 60.917 1.00 23.86 ? 133 VAL A CG2 1 ATOM 1098 N N . LYS A 1 134 ? 5.327 -6.949 65.100 1.00 25.47 ? 134 LYS A N 1 ATOM 1099 C CA . LYS A 1 134 ? 5.500 -6.940 66.541 1.00 27.77 ? 134 LYS A CA 1 ATOM 1100 C C . LYS A 1 134 ? 6.631 -7.890 66.951 1.00 27.59 ? 134 LYS A C 1 ATOM 1101 O O . LYS A 1 134 ? 7.577 -7.498 67.637 1.00 25.95 ? 134 LYS A O 1 ATOM 1102 C CB . LYS A 1 134 ? 4.178 -7.358 67.200 1.00 30.45 ? 134 LYS A CB 1 ATOM 1103 C CG . LYS A 1 134 ? 4.025 -6.955 68.656 1.00 39.09 ? 134 LYS A CG 1 ATOM 1104 C CD . LYS A 1 134 ? 2.645 -7.341 69.221 1.00 41.59 ? 134 LYS A CD 1 ATOM 1105 C CE . LYS A 1 134 ? 1.502 -6.578 68.544 1.00 45.29 ? 134 LYS A CE 1 ATOM 1106 N NZ . LYS A 1 134 ? 0.177 -6.829 69.200 1.00 47.64 ? 134 LYS A NZ 1 ATOM 1107 N N . GLU A 1 135 ? 6.531 -9.139 66.519 1.00 25.00 ? 135 GLU A N 1 ATOM 1108 C CA . GLU A 1 135 ? 7.533 -10.144 66.847 1.00 27.26 ? 135 GLU A CA 1 ATOM 1109 C C . GLU A 1 135 ? 8.912 -9.862 66.259 1.00 26.21 ? 135 GLU A C 1 ATOM 1110 O O . GLU A 1 135 ? 9.923 -10.150 66.894 1.00 24.56 ? 135 GLU A O 1 ATOM 1111 C CB . GLU A 1 135 ? 7.035 -11.521 66.408 1.00 28.10 ? 135 GLU A CB 1 ATOM 1112 C CG . GLU A 1 135 ? 6.023 -12.109 67.388 1.00 31.90 ? 135 GLU A CG 1 ATOM 1113 C CD . GLU A 1 135 ? 5.196 -13.235 66.800 1.00 33.51 ? 135 GLU A CD 1 ATOM 1114 O OE1 . GLU A 1 135 ? 5.752 -14.046 66.029 1.00 36.72 ? 135 GLU A OE1 1 ATOM 1115 O OE2 . GLU A 1 135 ? 3.992 -13.311 67.119 1.00 37.53 ? 135 GLU A OE2 1 ATOM 1116 N N . MET A 1 136 ? 8.960 -9.301 65.054 1.00 24.91 ? 136 MET A N 1 ATOM 1117 C CA . MET A 1 136 ? 10.244 -8.991 64.433 1.00 25.75 ? 136 MET A CA 1 ATOM 1118 C C . MET A 1 136 ? 10.962 -7.944 65.268 1.00 24.73 ? 136 MET A C 1 ATOM 1119 O O . MET A 1 136 ? 12.153 -8.061 65.535 1.00 23.90 ? 136 MET A O 1 ATOM 1120 C CB . MET A 1 136 ? 10.052 -8.454 63.008 1.00 24.66 ? 136 MET A CB 1 ATOM 1121 C CG . MET A 1 136 ? 11.368 -8.213 62.247 1.00 24.89 ? 136 MET A CG 1 ATOM 1122 S SD . MET A 1 136 ? 12.205 -9.742 61.750 1.00 26.67 ? 136 MET A SD 1 ATOM 1123 C CE . MET A 1 136 ? 11.191 -10.241 60.368 1.00 26.41 ? 136 MET A CE 1 ATOM 1124 N N . LYS A 1 137 ? 10.225 -6.919 65.678 1.00 26.51 ? 137 LYS A N 1 ATOM 1125 C CA . LYS A 1 137 ? 10.790 -5.838 66.480 1.00 27.19 ? 137 LYS A CA 1 ATOM 1126 C C . LYS A 1 137 ? 11.258 -6.356 67.840 1.00 27.43 ? 137 LYS A C 1 ATOM 1127 O O . LYS A 1 137 ? 12.306 -5.943 68.334 1.00 26.85 ? 137 LYS A O 1 ATOM 1128 C CB . LYS A 1 137 ? 9.745 -4.727 66.669 1.00 28.59 ? 137 LYS A CB 1 ATOM 1129 C CG . LYS A 1 137 ? 10.279 -3.432 67.288 1.00 29.59 ? 137 LYS A CG 1 ATOM 1130 C CD . LYS A 1 137 ? 11.480 -2.910 66.502 1.00 34.48 ? 137 LYS A CD 1 ATOM 1131 C CE . LYS A 1 137 ? 11.881 -1.500 66.915 1.00 38.18 ? 137 LYS A CE 1 ATOM 1132 N NZ . LYS A 1 137 ? 10.985 -0.434 66.368 1.00 39.56 ? 137 LYS A NZ 1 ATOM 1133 N N . ALA A 1 138 ? 10.487 -7.258 68.444 1.00 25.49 ? 138 ALA A N 1 ATOM 1134 C CA . ALA A 1 138 ? 10.870 -7.812 69.743 1.00 26.97 ? 138 ALA A CA 1 ATOM 1135 C C . ALA A 1 138 ? 12.204 -8.547 69.617 1.00 26.27 ? 138 ALA A C 1 ATOM 1136 O O . ALA A 1 138 ? 13.039 -8.503 70.523 1.00 26.42 ? 138 ALA A O 1 ATOM 1137 C CB . ALA A 1 138 ? 9.785 -8.764 70.257 1.00 27.75 ? 138 ALA A CB 1 ATOM 1138 N N . GLU A 1 139 ? 12.399 -9.222 68.489 1.00 24.33 ? 139 GLU A N 1 ATOM 1139 C CA . GLU A 1 139 ? 13.635 -9.953 68.237 1.00 25.90 ? 139 GLU A CA 1 ATOM 1140 C C . GLU A 1 139 ? 14.802 -8.975 68.088 1.00 26.40 ? 139 GLU A C 1 ATOM 1141 O O . GLU A 1 139 ? 15.904 -9.219 68.590 1.00 26.49 ? 139 GLU A O 1 ATOM 1142 C CB . GLU A 1 139 ? 13.501 -10.797 66.964 1.00 26.72 ? 139 GLU A CB 1 ATOM 1143 C CG . GLU A 1 139 ? 14.740 -11.610 66.587 1.00 30.12 ? 139 GLU A CG 1 ATOM 1144 C CD . GLU A 1 139 ? 15.043 -12.742 67.564 1.00 35.39 ? 139 GLU A CD 1 ATOM 1145 O OE1 . GLU A 1 139 ? 14.191 -13.041 68.431 1.00 34.85 ? 139 GLU A OE1 1 ATOM 1146 O OE2 . GLU A 1 139 ? 16.138 -13.335 67.451 1.00 36.19 ? 139 GLU A OE2 1 ATOM 1147 N N . PHE A 1 140 ? 14.560 -7.863 67.399 1.00 24.25 ? 140 PHE A N 1 ATOM 1148 C CA . PHE A 1 140 ? 15.607 -6.860 67.205 1.00 23.81 ? 140 PHE A CA 1 ATOM 1149 C C . PHE A 1 140 ? 16.009 -6.232 68.543 1.00 24.82 ? 140 PHE A C 1 ATOM 1150 O O . PHE A 1 140 ? 17.186 -5.963 68.787 1.00 22.78 ? 140 PHE A O 1 ATOM 1151 C CB . PHE A 1 140 ? 15.130 -5.759 66.246 1.00 22.88 ? 140 PHE A CB 1 ATOM 1152 C CG . PHE A 1 140 ? 15.102 -6.169 64.791 1.00 21.04 ? 140 PHE A CG 1 ATOM 1153 C CD1 . PHE A 1 140 ? 15.318 -7.497 64.406 1.00 16.96 ? 140 PHE A CD1 1 ATOM 1154 C CD2 . PHE A 1 140 ? 14.842 -5.217 63.804 1.00 18.85 ? 140 PHE A CD2 1 ATOM 1155 C CE1 . PHE A 1 140 ? 15.272 -7.869 63.054 1.00 20.60 ? 140 PHE A CE1 1 ATOM 1156 C CE2 . PHE A 1 140 ? 14.792 -5.575 62.452 1.00 17.31 ? 140 PHE A CE2 1 ATOM 1157 C CZ . PHE A 1 140 ? 15.007 -6.897 62.075 1.00 17.35 ? 140 PHE A CZ 1 ATOM 1158 N N . ALA A 1 141 ? 15.028 -5.991 69.405 1.00 23.87 ? 141 ALA A N 1 ATOM 1159 C CA . ALA A 1 141 ? 15.306 -5.396 70.707 1.00 28.48 ? 141 ALA A CA 1 ATOM 1160 C C . ALA A 1 141 ? 16.159 -6.356 71.528 1.00 29.80 ? 141 ALA A C 1 ATOM 1161 O O . ALA A 1 141 ? 17.092 -5.952 72.222 1.00 30.19 ? 141 ALA A O 1 ATOM 1162 C CB . ALA A 1 141 ? 13.988 -5.082 71.441 1.00 26.96 ? 141 ALA A CB 1 ATOM 1163 N N . ARG A 1 142 ? 15.832 -7.638 71.430 1.00 31.89 ? 142 ARG A N 1 ATOM 1164 C CA . ARG A 1 142 ? 16.539 -8.686 72.152 1.00 33.95 ? 142 ARG A CA 1 ATOM 1165 C C . ARG A 1 142 ? 17.969 -8.851 71.637 1.00 32.58 ? 142 ARG A C 1 ATOM 1166 O O . ARG A 1 142 ? 18.902 -9.034 72.419 1.00 30.37 ? 142 ARG A O 1 ATOM 1167 C CB . ARG A 1 142 ? 15.765 -9.999 71.994 1.00 37.09 ? 142 ARG A CB 1 ATOM 1168 C CG . ARG A 1 142 ? 16.176 -11.120 72.917 1.00 45.60 ? 142 ARG A CG 1 ATOM 1169 C CD . ARG A 1 142 ? 14.956 -11.968 73.274 1.00 51.03 ? 142 ARG A CD 1 ATOM 1170 N NE . ARG A 1 142 ? 14.143 -12.269 72.097 1.00 55.95 ? 142 ARG A NE 1 ATOM 1171 C CZ . ARG A 1 142 ? 12.910 -11.810 71.899 1.00 57.50 ? 142 ARG A CZ 1 ATOM 1172 N NH1 . ARG A 1 142 ? 12.335 -11.028 72.805 1.00 59.20 ? 142 ARG A NH1 1 ATOM 1173 N NH2 . ARG A 1 142 ? 12.256 -12.127 70.790 1.00 57.15 ? 142 ARG A NH2 1 ATOM 1174 N N . GLU A 1 143 ? 18.136 -8.775 70.320 1.00 29.87 ? 143 GLU A N 1 ATOM 1175 C CA . GLU A 1 143 ? 19.452 -8.933 69.700 1.00 29.52 ? 143 GLU A CA 1 ATOM 1176 C C . GLU A 1 143 ? 20.418 -7.804 70.075 1.00 29.15 ? 143 GLU A C 1 ATOM 1177 O O . GLU A 1 143 ? 21.628 -8.008 70.147 1.00 31.36 ? 143 GLU A O 1 ATOM 1178 C CB . GLU A 1 143 ? 19.294 -9.020 68.172 1.00 28.23 ? 143 GLU A CB 1 ATOM 1179 C CG . GLU A 1 143 ? 20.532 -9.492 67.423 1.00 27.96 ? 143 GLU A CG 1 ATOM 1180 C CD . GLU A 1 143 ? 21.398 -8.352 66.915 1.00 30.64 ? 143 GLU A CD 1 ATOM 1181 O OE1 . GLU A 1 143 ? 21.070 -7.172 67.175 1.00 29.24 ? 143 GLU A OE1 1 ATOM 1182 O OE2 . GLU A 1 143 ? 22.417 -8.641 66.250 1.00 30.73 ? 143 GLU A OE2 1 ATOM 1183 N N . ALA A 1 144 ? 19.881 -6.617 70.324 1.00 27.76 ? 144 ALA A N 1 ATOM 1184 C CA . ALA A 1 144 ? 20.713 -5.475 70.688 1.00 28.94 ? 144 ALA A CA 1 ATOM 1185 C C . ALA A 1 144 ? 21.341 -5.632 72.077 1.00 29.62 ? 144 ALA A C 1 ATOM 1186 O O . ALA A 1 144 ? 22.267 -4.902 72.429 1.00 28.42 ? 144 ALA A O 1 ATOM 1187 C CB . ALA A 1 144 ? 19.888 -4.187 70.631 1.00 28.04 ? 144 ALA A CB 1 ATOM 1188 N N . GLN A 1 145 ? 20.830 -6.571 72.868 1.00 28.10 ? 145 GLN A N 1 ATOM 1189 C CA . GLN A 1 145 ? 21.371 -6.810 74.203 1.00 31.00 ? 145 GLN A CA 1 ATOM 1190 C C . GLN A 1 145 ? 22.829 -7.239 74.100 1.00 31.74 ? 145 GLN A C 1 ATOM 1191 O O . GLN A 1 145 ? 23.594 -7.113 75.056 1.00 33.20 ? 145 GLN A O 1 ATOM 1192 C CB . GLN A 1 145 ? 20.579 -7.913 74.910 1.00 29.69 ? 145 GLN A CB 1 ATOM 1193 C CG . GLN A 1 145 ? 19.253 -7.461 75.496 1.00 31.39 ? 145 GLN A CG 1 ATOM 1194 C CD . GLN A 1 145 ? 18.394 -8.629 75.937 1.00 33.65 ? 145 GLN A CD 1 ATOM 1195 O OE1 . GLN A 1 145 ? 18.890 -9.740 76.127 1.00 36.05 ? 145 GLN A OE1 1 ATOM 1196 N NE2 . GLN A 1 145 ? 17.100 -8.382 76.109 1.00 33.16 ? 145 GLN A NE2 1 ATOM 1197 N N . ALA A 1 146 ? 23.201 -7.749 72.930 1.00 31.84 ? 146 ALA A N 1 ATOM 1198 C CA . ALA A 1 146 ? 24.557 -8.216 72.685 1.00 31.13 ? 146 ALA A CA 1 ATOM 1199 C C . ALA A 1 146 ? 25.571 -7.081 72.559 1.00 31.51 ? 146 ALA A C 1 ATOM 1200 O O . ALA A 1 146 ? 26.746 -7.317 72.298 1.00 32.05 ? 146 ALA A O 1 ATOM 1201 C CB . ALA A 1 146 ? 24.585 -9.095 71.434 1.00 32.10 ? 146 ALA A CB 1 ATOM 1202 N N . GLY A 1 147 ? 25.117 -5.845 72.731 1.00 33.11 ? 147 GLY A N 1 ATOM 1203 C CA . GLY A 1 147 ? 26.036 -4.723 72.663 1.00 34.97 ? 147 GLY A CA 1 ATOM 1204 C C . GLY A 1 147 ? 26.205 -4.023 71.327 1.00 37.92 ? 147 GLY A C 1 ATOM 1205 O O . GLY A 1 147 ? 27.025 -3.113 71.204 1.00 38.90 ? 147 GLY A O 1 ATOM 1206 N N . THR A 1 148 ? 25.445 -4.431 70.320 1.00 38.53 ? 148 THR A N 1 ATOM 1207 C CA . THR A 1 148 ? 25.553 -3.787 69.022 1.00 39.96 ? 148 THR A CA 1 ATOM 1208 C C . THR A 1 148 ? 24.296 -2.977 68.742 1.00 38.17 ? 148 THR A C 1 ATOM 1209 O O . THR A 1 148 ? 23.212 -3.311 69.212 1.00 39.57 ? 148 THR A O 1 ATOM 1210 C CB . THR A 1 148 ? 25.781 -4.822 67.905 1.00 41.84 ? 148 THR A CB 1 ATOM 1211 O OG1 . THR A 1 148 ? 25.820 -4.157 66.633 1.00 47.26 ? 148 THR A OG1 1 ATOM 1212 C CG2 . THR A 1 148 ? 24.680 -5.874 67.922 1.00 42.92 ? 148 THR A CG2 1 ATOM 1213 N N . GLU A 1 149 ? 24.458 -1.898 67.989 1.00 36.62 ? 149 GLU A N 1 ATOM 1214 C CA . GLU A 1 149 ? 23.353 -1.010 67.640 1.00 35.94 ? 149 GLU A CA 1 ATOM 1215 C C . GLU A 1 149 ? 22.105 -1.739 67.149 1.00 32.63 ? 149 GLU A C 1 ATOM 1216 O O . GLU A 1 149 ? 22.163 -2.547 66.223 1.00 31.01 ? 149 GLU A O 1 ATOM 1217 C CB . GLU A 1 149 ? 23.812 -0.026 66.573 1.00 38.98 ? 149 GLU A CB 1 ATOM 1218 C CG . GLU A 1 149 ? 22.772 0.988 66.178 1.00 44.83 ? 149 GLU A CG 1 ATOM 1219 C CD . GLU A 1 149 ? 23.329 2.386 66.232 1.00 49.49 ? 149 GLU A CD 1 ATOM 1220 O OE1 . GLU A 1 149 ? 23.648 2.848 67.349 1.00 53.82 ? 149 GLU A OE1 1 ATOM 1221 O OE2 . GLU A 1 149 ? 23.460 3.014 65.163 1.00 52.90 ? 149 GLU A OE2 1 ATOM 1222 N N . ARG A 1 150 ? 20.972 -1.424 67.770 1.00 29.35 ? 150 ARG A N 1 ATOM 1223 C CA . ARG A 1 150 ? 19.702 -2.044 67.417 1.00 28.03 ? 150 ARG A CA 1 ATOM 1224 C C . ARG A 1 150 ? 19.333 -1.888 65.947 1.00 24.76 ? 150 ARG A C 1 ATOM 1225 O O . ARG A 1 150 ? 19.386 -0.790 65.382 1.00 21.73 ? 150 ARG A O 1 ATOM 1226 C CB . ARG A 1 150 ? 18.564 -1.482 68.272 1.00 27.95 ? 150 ARG A CB 1 ATOM 1227 C CG . ARG A 1 150 ? 17.308 -2.329 68.200 1.00 34.60 ? 150 ARG A CG 1 ATOM 1228 C CD . ARG A 1 150 ? 16.246 -1.869 69.180 1.00 39.94 ? 150 ARG A CD 1 ATOM 1229 N NE . ARG A 1 150 ? 15.436 -0.794 68.630 1.00 47.24 ? 150 ARG A NE 1 ATOM 1230 C CZ . ARG A 1 150 ? 14.137 -0.653 68.862 1.00 53.28 ? 150 ARG A CZ 1 ATOM 1231 N NH1 . ARG A 1 150 ? 13.499 -1.526 69.636 1.00 57.63 ? 150 ARG A NH1 1 ATOM 1232 N NH2 . ARG A 1 150 ? 13.473 0.361 68.321 1.00 57.09 ? 150 ARG A NH2 1 ATOM 1233 N N . LEU A 1 151 ? 18.947 -3.002 65.336 1.00 23.01 ? 151 LEU A N 1 ATOM 1234 C CA . LEU A 1 151 ? 18.556 -3.014 63.932 1.00 22.39 ? 151 LEU A CA 1 ATOM 1235 C C . LEU A 1 151 ? 17.262 -2.230 63.730 1.00 23.27 ? 151 LEU A C 1 ATOM 1236 O O . LEU A 1 151 ? 16.389 -2.213 64.603 1.00 19.87 ? 151 LEU A O 1 ATOM 1237 C CB . LEU A 1 151 ? 18.362 -4.455 63.452 1.00 20.05 ? 151 LEU A CB 1 ATOM 1238 C CG . LEU A 1 151 ? 19.639 -5.307 63.393 1.00 22.54 ? 151 LEU A CG 1 ATOM 1239 C CD1 . LEU A 1 151 ? 19.283 -6.789 63.430 1.00 19.19 ? 151 LEU A CD1 1 ATOM 1240 C CD2 . LEU A 1 151 ? 20.431 -4.964 62.123 1.00 17.24 ? 151 LEU A CD2 1 ATOM 1241 N N . LEU A 1 152 ? 17.151 -1.579 62.575 1.00 22.04 ? 152 LEU A N 1 ATOM 1242 C CA . LEU A 1 152 ? 15.972 -0.794 62.231 1.00 21.03 ? 152 LEU A CA 1 ATOM 1243 C C . LEU A 1 152 ? 14.965 -1.685 61.520 1.00 21.73 ? 152 LEU A C 1 ATOM 1244 O O . LEU A 1 152 ? 15.346 -2.664 60.877 1.00 18.79 ? 152 LEU A O 1 ATOM 1245 C CB . LEU A 1 152 ? 16.367 0.360 61.302 1.00 22.02 ? 152 LEU A CB 1 ATOM 1246 C CG . LEU A 1 152 ? 17.380 1.376 61.851 1.00 24.27 ? 152 LEU A CG 1 ATOM 1247 C CD1 . LEU A 1 152 ? 17.935 2.223 60.713 1.00 24.64 ? 152 LEU A CD1 1 ATOM 1248 C CD2 . LEU A 1 152 ? 16.703 2.244 62.904 1.00 24.92 ? 152 LEU A CD2 1 ATOM 1249 N N . LEU A 1 153 ? 13.683 -1.352 61.650 1.00 20.03 ? 153 LEU A N 1 ATOM 1250 C CA . LEU A 1 153 ? 12.621 -2.100 60.990 1.00 20.63 ? 153 LEU A CA 1 ATOM 1251 C C . LEU A 1 153 ? 11.706 -1.093 60.297 1.00 21.00 ? 153 LEU A C 1 ATOM 1252 O O . LEU A 1 153 ? 11.168 -0.193 60.933 1.00 17.51 ? 153 LEU A O 1 ATOM 1253 C CB . LEU A 1 153 ? 11.806 -2.926 61.996 1.00 20.54 ? 153 LEU A CB 1 ATOM 1254 C CG . LEU A 1 153 ? 10.657 -3.745 61.378 1.00 23.27 ? 153 LEU A CG 1 ATOM 1255 C CD1 . LEU A 1 153 ? 11.225 -4.757 60.377 1.00 22.08 ? 153 LEU A CD1 1 ATOM 1256 C CD2 . LEU A 1 153 ? 9.865 -4.461 62.476 1.00 24.43 ? 153 LEU A CD2 1 ATOM 1257 N N . SER A 1 154 ? 11.552 -1.231 58.985 1.00 20.69 ? 154 SER A N 1 ATOM 1258 C CA . SER A 1 154 ? 10.685 -0.329 58.238 1.00 21.60 ? 154 SER A CA 1 ATOM 1259 C C . SER A 1 154 ? 9.745 -1.153 57.375 1.00 20.59 ? 154 SER A C 1 ATOM 1260 O O . SER A 1 154 ? 9.890 -2.373 57.273 1.00 18.73 ? 154 SER A O 1 ATOM 1261 C CB . SER A 1 154 ? 11.519 0.596 57.348 1.00 20.82 ? 154 SER A CB 1 ATOM 1262 O OG . SER A 1 154 ? 12.213 -0.144 56.359 1.00 20.33 ? 154 SER A OG 1 ATOM 1263 N N . ALA A 1 155 ? 8.774 -0.485 56.764 1.00 19.63 ? 155 ALA A N 1 ATOM 1264 C CA . ALA A 1 155 ? 7.829 -1.158 55.886 1.00 19.67 ? 155 ALA A CA 1 ATOM 1265 C C . ALA A 1 155 ? 7.327 -0.199 54.816 1.00 20.38 ? 155 ALA A C 1 ATOM 1266 O O . ALA A 1 155 ? 7.145 0.995 55.071 1.00 19.50 ? 155 ALA A O 1 ATOM 1267 C CB . ALA A 1 155 ? 6.653 -1.698 56.690 1.00 16.85 ? 155 ALA A CB 1 ATOM 1268 N N . ALA A 1 156 ? 7.134 -0.728 53.613 1.00 20.47 ? 156 ALA A N 1 ATOM 1269 C CA . ALA A 1 156 ? 6.612 0.056 52.499 1.00 21.38 ? 156 ALA A CA 1 ATOM 1270 C C . ALA A 1 156 ? 5.136 -0.298 52.535 1.00 22.88 ? 156 ALA A C 1 ATOM 1271 O O . ALA A 1 156 ? 4.780 -1.483 52.532 1.00 22.03 ? 156 ALA A O 1 ATOM 1272 C CB . ALA A 1 156 ? 7.249 -0.387 51.181 1.00 20.65 ? 156 ALA A CB 1 ATOM 1273 N N . VAL A 1 157 ? 4.283 0.721 52.580 1.00 21.57 ? 157 VAL A N 1 ATOM 1274 C CA . VAL A 1 157 ? 2.839 0.513 52.685 1.00 21.98 ? 157 VAL A CA 1 ATOM 1275 C C . VAL A 1 157 ? 2.027 1.157 51.561 1.00 21.68 ? 157 VAL A C 1 ATOM 1276 O O . VAL A 1 157 ? 2.346 2.249 51.098 1.00 18.90 ? 157 VAL A O 1 ATOM 1277 C CB . VAL A 1 157 ? 2.347 1.063 54.061 1.00 22.72 ? 157 VAL A CB 1 ATOM 1278 C CG1 . VAL A 1 157 ? 0.822 1.108 54.133 1.00 25.17 ? 157 VAL A CG1 1 ATOM 1279 C CG2 . VAL A 1 157 ? 2.915 0.192 55.182 1.00 21.20 ? 157 VAL A CG2 1 ATOM 1280 N N . SER A 1 158 ? 0.967 0.482 51.129 1.00 23.79 ? 158 SER A N 1 ATOM 1281 C CA . SER A 1 158 ? 0.111 1.014 50.067 1.00 24.09 ? 158 SER A CA 1 ATOM 1282 C C . SER A 1 158 ? -0.445 2.383 50.452 1.00 23.31 ? 158 SER A C 1 ATOM 1283 O O . SER A 1 158 ? -0.671 2.657 51.636 1.00 23.67 ? 158 SER A O 1 ATOM 1284 C CB . SER A 1 158 ? -1.062 0.064 49.806 1.00 26.05 ? 158 SER A CB 1 ATOM 1285 O OG . SER A 1 158 ? -1.982 0.640 48.891 1.00 28.88 ? 158 SER A OG 1 ATOM 1286 N N . ALA A 1 159 ? -0.651 3.240 49.455 1.00 20.85 ? 159 ALA A N 1 ATOM 1287 C CA . ALA A 1 159 ? -1.221 4.565 49.683 1.00 22.45 ? 159 ALA A CA 1 ATOM 1288 C C . ALA A 1 159 ? -2.680 4.559 49.226 1.00 23.87 ? 159 ALA A C 1 ATOM 1289 O O . ALA A 1 159 ? -3.346 5.589 49.247 1.00 23.48 ? 159 ALA A O 1 ATOM 1290 C CB . ALA A 1 159 ? -0.432 5.630 48.910 1.00 21.54 ? 159 ALA A CB 1 ATOM 1291 N N . GLY A 1 160 ? -3.162 3.393 48.799 1.00 23.12 ? 160 GLY A N 1 ATOM 1292 C CA . GLY A 1 160 ? -4.542 3.272 48.357 1.00 26.38 ? 160 GLY A CA 1 ATOM 1293 C C . GLY A 1 160 ? -5.460 3.070 49.553 1.00 27.32 ? 160 GLY A C 1 ATOM 1294 O O . GLY A 1 160 ? -5.266 2.138 50.337 1.00 26.27 ? 160 GLY A O 1 ATOM 1295 N N . LYS A 1 161 ? -6.458 3.936 49.700 1.00 28.43 ? 161 LYS A N 1 ATOM 1296 C CA . LYS A 1 161 ? -7.388 3.857 50.829 1.00 28.97 ? 161 LYS A CA 1 ATOM 1297 C C . LYS A 1 161 ? -7.993 2.474 51.031 1.00 29.47 ? 161 LYS A C 1 ATOM 1298 O O . LYS A 1 161 ? -8.010 1.955 52.146 1.00 28.71 ? 161 LYS A O 1 ATOM 1299 C CB . LYS A 1 161 ? -8.524 4.868 50.659 1.00 30.65 ? 161 LYS A CB 1 ATOM 1300 C CG . LYS A 1 161 ? -9.494 4.903 51.839 1.00 32.48 ? 161 LYS A CG 1 ATOM 1301 C CD . LYS A 1 161 ? -10.717 5.765 51.544 1.00 33.74 ? 161 LYS A CD 1 ATOM 1302 C CE . LYS A 1 161 ? -11.579 5.964 52.792 1.00 36.43 ? 161 LYS A CE 1 ATOM 1303 N NZ . LYS A 1 161 ? -12.068 4.676 53.375 1.00 36.41 ? 161 LYS A NZ 1 ATOM 1304 N N . ILE A 1 162 ? -8.504 1.881 49.960 1.00 29.15 ? 162 ILE A N 1 ATOM 1305 C CA . ILE A 1 162 ? -9.115 0.564 50.068 1.00 31.82 ? 162 ILE A CA 1 ATOM 1306 C C . ILE A 1 162 ? -8.100 -0.505 50.462 1.00 30.79 ? 162 ILE A C 1 ATOM 1307 O O . ILE A 1 162 ? -8.406 -1.405 51.245 1.00 30.27 ? 162 ILE A O 1 ATOM 1308 C CB . ILE A 1 162 ? -9.823 0.174 48.748 1.00 35.51 ? 162 ILE A CB 1 ATOM 1309 C CG1 . ILE A 1 162 ? -11.001 1.128 48.515 1.00 37.43 ? 162 ILE A CG1 1 ATOM 1310 C CG2 . ILE A 1 162 ? -10.315 -1.268 48.809 1.00 36.86 ? 162 ILE A CG2 1 ATOM 1311 C CD1 . ILE A 1 162 ? -11.987 0.670 47.451 1.00 40.02 ? 162 ILE A CD1 1 ATOM 1312 N N . ALA A 1 163 ? -6.887 -0.404 49.926 1.00 29.33 ? 163 ALA A N 1 ATOM 1313 C CA . ALA A 1 163 ? -5.844 -1.361 50.269 1.00 28.19 ? 163 ALA A CA 1 ATOM 1314 C C . ALA A 1 163 ? -5.479 -1.176 51.744 1.00 26.01 ? 163 ALA A C 1 ATOM 1315 O O . ALA A 1 163 ? -5.290 -2.151 52.473 1.00 23.15 ? 163 ALA A O 1 ATOM 1316 C CB . ALA A 1 163 ? -4.618 -1.147 49.384 1.00 28.46 ? 163 ALA A CB 1 ATOM 1317 N N . ILE A 1 164 ? -5.391 0.077 52.186 1.00 25.47 ? 164 ILE A N 1 ATOM 1318 C CA . ILE A 1 164 ? -5.056 0.364 53.582 1.00 26.08 ? 164 ILE A CA 1 ATOM 1319 C C . ILE A 1 164 ? -6.112 -0.190 54.545 1.00 28.64 ? 164 ILE A C 1 ATOM 1320 O O . ILE A 1 164 ? -5.778 -0.867 55.528 1.00 26.73 ? 164 ILE A O 1 ATOM 1321 C CB . ILE A 1 164 ? -4.929 1.884 53.837 1.00 25.74 ? 164 ILE A CB 1 ATOM 1322 C CG1 . ILE A 1 164 ? -3.709 2.447 53.101 1.00 25.18 ? 164 ILE A CG1 1 ATOM 1323 C CG2 . ILE A 1 164 ? -4.814 2.149 55.333 1.00 25.49 ? 164 ILE A CG2 1 ATOM 1324 C CD1 . ILE A 1 164 ? -3.618 3.975 53.136 1.00 21.95 ? 164 ILE A CD1 1 ATOM 1325 N N . ASP A 1 165 ? -7.382 0.096 54.262 1.00 28.20 ? 165 ASP A N 1 ATOM 1326 C CA . ASP A 1 165 ? -8.474 -0.365 55.122 1.00 31.61 ? 165 ASP A CA 1 ATOM 1327 C C . ASP A 1 165 ? -8.522 -1.880 55.167 1.00 32.72 ? 165 ASP A C 1 ATOM 1328 O O . ASP A 1 165 ? -8.809 -2.476 56.205 1.00 32.25 ? 165 ASP A O 1 ATOM 1329 C CB . ASP A 1 165 ? -9.833 0.158 54.628 1.00 31.10 ? 165 ASP A CB 1 ATOM 1330 C CG . ASP A 1 165 ? -10.025 1.636 54.894 1.00 34.56 ? 165 ASP A CG 1 ATOM 1331 O OD1 . ASP A 1 165 ? -9.423 2.148 55.865 1.00 35.67 ? 165 ASP A OD1 1 ATOM 1332 O OD2 . ASP A 1 165 ? -10.789 2.278 54.138 1.00 36.36 ? 165 ASP A OD2 1 ATOM 1333 N N . ARG A 1 166 ? -8.207 -2.491 54.033 1.00 32.63 ? 166 ARG A N 1 ATOM 1334 C CA . ARG A 1 166 ? -8.241 -3.936 53.884 1.00 36.13 ? 166 ARG A CA 1 ATOM 1335 C C . ARG A 1 166 ? -7.151 -4.736 54.592 1.00 34.47 ? 166 ARG A C 1 ATOM 1336 O O . ARG A 1 166 ? -7.451 -5.658 55.344 1.00 34.26 ? 166 ARG A O 1 ATOM 1337 C CB . ARG A 1 166 ? -8.215 -4.282 52.397 1.00 38.25 ? 166 ARG A CB 1 ATOM 1338 C CG . ARG A 1 166 ? -8.186 -5.767 52.087 1.00 46.79 ? 166 ARG A CG 1 ATOM 1339 C CD . ARG A 1 166 ? -7.564 -5.998 50.722 1.00 51.42 ? 166 ARG A CD 1 ATOM 1340 N NE . ARG A 1 166 ? -8.235 -5.232 49.677 1.00 56.52 ? 166 ARG A NE 1 ATOM 1341 C CZ . ARG A 1 166 ? -7.641 -4.813 48.564 1.00 58.93 ? 166 ARG A CZ 1 ATOM 1342 N NH1 . ARG A 1 166 ? -6.359 -5.082 48.354 1.00 60.56 ? 166 ARG A NH1 1 ATOM 1343 N NH2 . ARG A 1 166 ? -8.332 -4.132 47.660 1.00 60.41 ? 166 ARG A NH2 1 ATOM 1344 N N . GLY A 1 167 ? -5.887 -4.394 54.371 1.00 33.08 ? 167 GLY A N 1 ATOM 1345 C CA . GLY A 1 167 ? -4.841 -5.199 54.980 1.00 31.20 ? 167 GLY A CA 1 ATOM 1346 C C . GLY A 1 167 ? -3.931 -4.704 56.087 1.00 29.80 ? 167 GLY A C 1 ATOM 1347 O O . GLY A 1 167 ? -3.060 -5.462 56.528 1.00 29.41 ? 167 GLY A O 1 ATOM 1348 N N . TYR A 1 168 ? -4.121 -3.478 56.565 1.00 27.82 ? 168 TYR A N 1 ATOM 1349 C CA . TYR A 1 168 ? -3.239 -2.944 57.605 1.00 28.17 ? 168 TYR A CA 1 ATOM 1350 C C . TYR A 1 168 ? -3.899 -2.406 58.873 1.00 29.16 ? 168 TYR A C 1 ATOM 1351 O O . TYR A 1 168 ? -4.933 -1.750 58.819 1.00 30.55 ? 168 TYR A O 1 ATOM 1352 C CB . TYR A 1 168 ? -2.394 -1.796 57.044 1.00 26.23 ? 168 TYR A CB 1 ATOM 1353 C CG . TYR A 1 168 ? -1.664 -2.073 55.753 1.00 25.61 ? 168 TYR A CG 1 ATOM 1354 C CD1 . TYR A 1 168 ? -0.319 -2.432 55.758 1.00 24.48 ? 168 TYR A CD1 1 ATOM 1355 C CD2 . TYR A 1 168 ? -2.304 -1.920 54.521 1.00 25.17 ? 168 TYR A CD2 1 ATOM 1356 C CE1 . TYR A 1 168 ? 0.384 -2.628 54.564 1.00 25.04 ? 168 TYR A CE1 1 ATOM 1357 C CE2 . TYR A 1 168 ? -1.615 -2.114 53.319 1.00 24.98 ? 168 TYR A CE2 1 ATOM 1358 C CZ . TYR A 1 168 ? -0.271 -2.466 53.348 1.00 24.36 ? 168 TYR A CZ 1 ATOM 1359 O OH . TYR A 1 168 ? 0.405 -2.653 52.164 1.00 25.02 ? 168 TYR A OH 1 ATOM 1360 N N . ASP A 1 169 ? -3.273 -2.670 60.014 1.00 29.19 ? 169 ASP A N 1 ATOM 1361 C CA . ASP A 1 169 ? -3.738 -2.133 61.290 1.00 29.51 ? 169 ASP A CA 1 ATOM 1362 C C . ASP A 1 169 ? -2.682 -1.052 61.548 1.00 27.57 ? 169 ASP A C 1 ATOM 1363 O O . ASP A 1 169 ? -1.731 -1.253 62.307 1.00 27.48 ? 169 ASP A O 1 ATOM 1364 C CB . ASP A 1 169 ? -3.686 -3.192 62.396 1.00 31.57 ? 169 ASP A CB 1 ATOM 1365 C CG . ASP A 1 169 ? -4.287 -2.702 63.699 1.00 35.55 ? 169 ASP A CG 1 ATOM 1366 O OD1 . ASP A 1 169 ? -4.277 -1.471 63.938 1.00 37.31 ? 169 ASP A OD1 1 ATOM 1367 O OD2 . ASP A 1 169 ? -4.749 -3.550 64.492 1.00 35.65 ? 169 ASP A OD2 1 ATOM 1368 N N . ILE A 1 170 ? -2.846 0.086 60.883 1.00 27.42 ? 170 ILE A N 1 ATOM 1369 C CA . ILE A 1 170 ? -1.894 1.189 60.980 1.00 28.25 ? 170 ILE A CA 1 ATOM 1370 C C . ILE A 1 170 ? -1.512 1.626 62.396 1.00 29.05 ? 170 ILE A C 1 ATOM 1371 O O . ILE A 1 170 ? -0.328 1.758 62.709 1.00 26.06 ? 170 ILE A O 1 ATOM 1372 C CB . ILE A 1 170 ? -2.411 2.418 60.196 1.00 28.62 ? 170 ILE A CB 1 ATOM 1373 C CG1 . ILE A 1 170 ? -2.666 2.030 58.732 1.00 29.91 ? 170 ILE A CG1 1 ATOM 1374 C CG2 . ILE A 1 170 ? -1.397 3.559 60.278 1.00 27.89 ? 170 ILE A CG2 1 ATOM 1375 C CD1 . ILE A 1 170 ? -1.420 1.556 57.976 1.00 30.75 ? 170 ILE A CD1 1 ATOM 1376 N N . ALA A 1 171 ? -2.506 1.858 63.246 1.00 28.13 ? 171 ALA A N 1 ATOM 1377 C CA . ALA A 1 171 ? -2.247 2.284 64.614 1.00 31.52 ? 171 ALA A CA 1 ATOM 1378 C C . ALA A 1 171 ? -1.333 1.306 65.352 1.00 32.18 ? 171 ALA A C 1 ATOM 1379 O O . ALA A 1 171 ? -0.468 1.716 66.130 1.00 35.96 ? 171 ALA A O 1 ATOM 1380 C CB . ALA A 1 171 ? -3.564 2.448 65.365 1.00 32.27 ? 171 ALA A CB 1 ATOM 1381 N N . GLN A 1 172 ? -1.515 0.013 65.099 1.00 32.82 ? 172 GLN A N 1 ATOM 1382 C CA . GLN A 1 172 ? -0.699 -1.011 65.747 1.00 33.68 ? 172 GLN A CA 1 ATOM 1383 C C . GLN A 1 172 ? 0.723 -1.151 65.202 1.00 32.20 ? 172 GLN A C 1 ATOM 1384 O O . GLN A 1 172 ? 1.676 -1.186 65.973 1.00 34.59 ? 172 GLN A O 1 ATOM 1385 C CB . GLN A 1 172 ? -1.389 -2.375 65.664 1.00 36.55 ? 172 GLN A CB 1 ATOM 1386 C CG . GLN A 1 172 ? -2.574 -2.564 66.606 1.00 42.61 ? 172 GLN A CG 1 ATOM 1387 C CD . GLN A 1 172 ? -2.151 -2.938 68.013 1.00 47.40 ? 172 GLN A CD 1 ATOM 1388 O OE1 . GLN A 1 172 ? -1.542 -2.139 68.729 1.00 48.38 ? 172 GLN A OE1 1 ATOM 1389 N NE2 . GLN A 1 172 ? -2.467 -4.168 68.416 1.00 49.23 ? 172 GLN A NE2 1 ATOM 1390 N N . ILE A 1 173 ? 0.889 -1.241 63.886 1.00 30.05 ? 173 ILE A N 1 ATOM 1391 C CA . ILE A 1 173 ? 2.241 -1.410 63.357 1.00 29.61 ? 173 ILE A CA 1 ATOM 1392 C C . ILE A 1 173 ? 3.104 -0.160 63.454 1.00 30.03 ? 173 ILE A C 1 ATOM 1393 O O . ILE A 1 173 ? 4.329 -0.253 63.479 1.00 30.40 ? 173 ILE A O 1 ATOM 1394 C CB . ILE A 1 173 ? 2.240 -1.916 61.889 1.00 29.01 ? 173 ILE A CB 1 ATOM 1395 C CG1 . ILE A 1 173 ? 1.589 -0.885 60.961 1.00 26.31 ? 173 ILE A CG1 1 ATOM 1396 C CG2 . ILE A 1 173 ? 1.544 -3.276 61.822 1.00 27.81 ? 173 ILE A CG2 1 ATOM 1397 C CD1 . ILE A 1 173 ? 1.650 -1.275 59.479 1.00 28.71 ? 173 ILE A CD1 1 ATOM 1398 N N . SER A 1 174 ? 2.467 1.004 63.515 1.00 29.67 ? 174 SER A N 1 ATOM 1399 C CA . SER A 1 174 ? 3.186 2.269 63.626 1.00 32.23 ? 174 SER A CA 1 ATOM 1400 C C . SER A 1 174 ? 4.064 2.337 64.871 1.00 31.96 ? 174 SER A C 1 ATOM 1401 O O . SER A 1 174 ? 5.151 2.909 64.847 1.00 31.65 ? 174 SER A O 1 ATOM 1402 C CB . SER A 1 174 ? 2.197 3.439 63.668 1.00 31.15 ? 174 SER A CB 1 ATOM 1403 O OG . SER A 1 174 ? 1.558 3.616 62.422 1.00 37.70 ? 174 SER A OG 1 ATOM 1404 N N . ARG A 1 175 ? 3.593 1.754 65.965 1.00 34.18 ? 175 ARG A N 1 ATOM 1405 C CA . ARG A 1 175 ? 4.355 1.800 67.206 1.00 36.28 ? 175 ARG A CA 1 ATOM 1406 C C . ARG A 1 175 ? 5.609 0.926 67.195 1.00 34.63 ? 175 ARG A C 1 ATOM 1407 O O . ARG A 1 175 ? 6.537 1.167 67.969 1.00 35.71 ? 175 ARG A O 1 ATOM 1408 C CB . ARG A 1 175 ? 3.450 1.418 68.383 1.00 40.40 ? 175 ARG A CB 1 ATOM 1409 C CG . ARG A 1 175 ? 2.981 -0.025 68.396 1.00 49.00 ? 175 ARG A CG 1 ATOM 1410 C CD . ARG A 1 175 ? 1.804 -0.216 69.351 1.00 56.90 ? 175 ARG A CD 1 ATOM 1411 N NE . ARG A 1 175 ? 2.022 0.447 70.635 1.00 62.72 ? 175 ARG A NE 1 ATOM 1412 C CZ . ARG A 1 175 ? 1.840 -0.135 71.817 1.00 66.37 ? 175 ARG A CZ 1 ATOM 1413 N NH1 . ARG A 1 175 ? 1.439 -1.399 71.881 1.00 67.63 ? 175 ARG A NH1 1 ATOM 1414 N NH2 . ARG A 1 175 ? 2.045 0.549 72.936 1.00 68.29 ? 175 ARG A NH2 1 ATOM 1415 N N . HIS A 1 176 ? 5.657 -0.063 66.303 1.00 31.51 ? 176 HIS A N 1 ATOM 1416 C CA . HIS A 1 176 ? 6.814 -0.963 66.234 1.00 31.89 ? 176 HIS A CA 1 ATOM 1417 C C . HIS A 1 176 ? 7.779 -0.703 65.081 1.00 30.10 ? 176 HIS A C 1 ATOM 1418 O O . HIS A 1 176 ? 8.901 -1.206 65.088 1.00 31.22 ? 176 HIS A O 1 ATOM 1419 C CB . HIS A 1 176 ? 6.344 -2.414 66.163 1.00 32.93 ? 176 HIS A CB 1 ATOM 1420 C CG . HIS A 1 176 ? 5.447 -2.808 67.291 1.00 36.49 ? 176 HIS A CG 1 ATOM 1421 N ND1 . HIS A 1 176 ? 5.869 -2.828 68.603 1.00 36.99 ? 176 HIS A ND1 1 ATOM 1422 C CD2 . HIS A 1 176 ? 4.140 -3.160 67.309 1.00 37.99 ? 176 HIS A CD2 1 ATOM 1423 C CE1 . HIS A 1 176 ? 4.859 -3.173 69.381 1.00 40.47 ? 176 HIS A CE1 1 ATOM 1424 N NE2 . HIS A 1 176 ? 3.798 -3.380 68.621 1.00 39.90 ? 176 HIS A NE2 1 ATOM 1425 N N . LEU A 1 177 ? 7.345 0.067 64.090 1.00 28.22 ? 177 LEU A N 1 ATOM 1426 C CA . LEU A 1 177 ? 8.191 0.379 62.942 1.00 25.81 ? 177 LEU A CA 1 ATOM 1427 C C . LEU A 1 177 ? 8.964 1.665 63.178 1.00 24.54 ? 177 LEU A C 1 ATOM 1428 O O . LEU A 1 177 ? 8.447 2.593 63.791 1.00 26.10 ? 177 LEU A O 1 ATOM 1429 C CB . LEU A 1 177 ? 7.331 0.521 61.683 1.00 24.24 ? 177 LEU A CB 1 ATOM 1430 C CG . LEU A 1 177 ? 6.654 -0.757 61.178 1.00 23.50 ? 177 LEU A CG 1 ATOM 1431 C CD1 . LEU A 1 177 ? 5.655 -0.420 60.089 1.00 21.77 ? 177 LEU A CD1 1 ATOM 1432 C CD2 . LEU A 1 177 ? 7.707 -1.713 60.660 1.00 20.25 ? 177 LEU A CD2 1 ATOM 1433 N N . ASP A 1 178 ? 10.201 1.720 62.691 1.00 22.48 ? 178 ASP A N 1 ATOM 1434 C CA . ASP A 1 178 ? 11.033 2.912 62.847 1.00 21.64 ? 178 ASP A CA 1 ATOM 1435 C C . ASP A 1 178 ? 10.572 3.993 61.863 1.00 23.46 ? 178 ASP A C 1 ATOM 1436 O O . ASP A 1 178 ? 10.689 5.193 62.124 1.00 22.38 ? 178 ASP A O 1 ATOM 1437 C CB . ASP A 1 178 ? 12.497 2.535 62.653 1.00 21.73 ? 178 ASP A CB 1 ATOM 1438 C CG . ASP A 1 178 ? 13.003 1.672 63.786 1.00 23.88 ? 178 ASP A CG 1 ATOM 1439 O OD1 . ASP A 1 178 ? 12.925 2.131 64.942 1.00 25.33 ? 178 ASP A OD1 1 ATOM 1440 O OD2 . ASP A 1 178 ? 13.448 0.536 63.533 1.00 24.09 ? 178 ASP A OD2 1 ATOM 1441 N N . PHE A 1 179 ? 10.065 3.549 60.719 1.00 19.90 ? 179 PHE A N 1 ATOM 1442 C CA . PHE A 1 179 ? 9.481 4.447 59.744 1.00 21.43 ? 179 PHE A CA 1 ATOM 1443 C C . PHE A 1 179 ? 8.650 3.664 58.756 1.00 21.29 ? 179 PHE A C 1 ATOM 1444 O O . PHE A 1 179 ? 8.847 2.460 58.570 1.00 18.53 ? 179 PHE A O 1 ATOM 1445 C CB . PHE A 1 179 ? 10.507 5.348 59.031 1.00 19.72 ? 179 PHE A CB 1 ATOM 1446 C CG . PHE A 1 179 ? 11.547 4.620 58.226 1.00 22.14 ? 179 PHE A CG 1 ATOM 1447 C CD1 . PHE A 1 179 ? 12.770 4.280 58.795 1.00 21.20 ? 179 PHE A CD1 1 ATOM 1448 C CD2 . PHE A 1 179 ? 11.338 4.357 56.871 1.00 21.50 ? 179 PHE A CD2 1 ATOM 1449 C CE1 . PHE A 1 179 ? 13.784 3.686 58.022 1.00 22.38 ? 179 PHE A CE1 1 ATOM 1450 C CE2 . PHE A 1 179 ? 12.335 3.766 56.090 1.00 21.23 ? 179 PHE A CE2 1 ATOM 1451 C CZ . PHE A 1 179 ? 13.565 3.433 56.667 1.00 22.06 ? 179 PHE A CZ 1 ATOM 1452 N N . ILE A 1 180 ? 7.692 4.359 58.156 1.00 19.36 ? 180 ILE A N 1 ATOM 1453 C CA . ILE A 1 180 ? 6.769 3.772 57.196 1.00 21.00 ? 180 ILE A CA 1 ATOM 1454 C C . ILE A 1 180 ? 6.855 4.563 55.904 1.00 21.67 ? 180 ILE A C 1 ATOM 1455 O O . ILE A 1 180 ? 6.651 5.776 55.922 1.00 20.89 ? 180 ILE A O 1 ATOM 1456 C CB . ILE A 1 180 ? 5.308 3.883 57.700 1.00 23.42 ? 180 ILE A CB 1 ATOM 1457 C CG1 . ILE A 1 180 ? 5.173 3.235 59.080 1.00 26.06 ? 180 ILE A CG1 1 ATOM 1458 C CG2 . ILE A 1 180 ? 4.358 3.253 56.685 1.00 24.26 ? 180 ILE A CG2 1 ATOM 1459 C CD1 . ILE A 1 180 ? 3.786 3.386 59.693 1.00 29.68 ? 180 ILE A CD1 1 ATOM 1460 N N . SER A 1 181 ? 7.154 3.890 54.794 1.00 19.31 ? 181 SER A N 1 ATOM 1461 C CA . SER A 1 181 ? 7.232 4.563 53.505 1.00 19.04 ? 181 SER A CA 1 ATOM 1462 C C . SER A 1 181 ? 5.890 4.421 52.800 1.00 18.94 ? 181 SER A C 1 ATOM 1463 O O . SER A 1 181 ? 5.398 3.305 52.621 1.00 19.72 ? 181 SER A O 1 ATOM 1464 C CB . SER A 1 181 ? 8.333 3.943 52.634 1.00 18.22 ? 181 SER A CB 1 ATOM 1465 O OG . SER A 1 181 ? 9.612 4.180 53.183 1.00 20.62 ? 181 SER A OG 1 ATOM 1466 N N . LEU A 1 182 ? 5.298 5.549 52.413 1.00 18.64 ? 182 LEU A N 1 ATOM 1467 C CA . LEU A 1 182 ? 4.016 5.554 51.708 1.00 19.75 ? 182 LEU A CA 1 ATOM 1468 C C . LEU A 1 182 ? 4.262 5.459 50.212 1.00 20.54 ? 182 LEU A C 1 ATOM 1469 O O . LEU A 1 182 ? 4.973 6.286 49.645 1.00 19.41 ? 182 LEU A O 1 ATOM 1470 C CB . LEU A 1 182 ? 3.244 6.846 51.983 1.00 22.97 ? 182 LEU A CB 1 ATOM 1471 C CG . LEU A 1 182 ? 2.111 6.892 53.000 1.00 27.60 ? 182 LEU A CG 1 ATOM 1472 C CD1 . LEU A 1 182 ? 1.418 8.255 52.890 1.00 26.08 ? 182 LEU A CD1 1 ATOM 1473 C CD2 . LEU A 1 182 ? 1.112 5.769 52.720 1.00 27.90 ? 182 LEU A CD2 1 ATOM 1474 N N . LEU A 1 183 ? 3.665 4.459 49.573 1.00 20.62 ? 183 LEU A N 1 ATOM 1475 C CA . LEU A 1 183 ? 3.840 4.274 48.138 1.00 22.15 ? 183 LEU A CA 1 ATOM 1476 C C . LEU A 1 183 ? 2.914 5.195 47.358 1.00 21.38 ? 183 LEU A C 1 ATOM 1477 O O . LEU A 1 183 ? 2.027 4.736 46.629 1.00 20.18 ? 183 LEU A O 1 ATOM 1478 C CB . LEU A 1 183 ? 3.567 2.818 47.770 1.00 22.20 ? 183 LEU A CB 1 ATOM 1479 C CG . LEU A 1 183 ? 4.478 1.849 48.522 1.00 25.80 ? 183 LEU A CG 1 ATOM 1480 C CD1 . LEU A 1 183 ? 4.120 0.410 48.165 1.00 25.84 ? 183 LEU A CD1 1 ATOM 1481 C CD2 . LEU A 1 183 ? 5.926 2.150 48.171 1.00 26.27 ? 183 LEU A CD2 1 ATOM 1482 N N . THR A 1 184 ? 3.137 6.497 47.509 1.00 20.47 ? 184 THR A N 1 ATOM 1483 C CA . THR A 1 184 ? 2.314 7.504 46.855 1.00 20.73 ? 184 THR A CA 1 ATOM 1484 C C . THR A 1 184 ? 2.632 7.745 45.372 1.00 23.14 ? 184 THR A C 1 ATOM 1485 O O . THR A 1 184 ? 2.804 8.885 44.934 1.00 23.67 ? 184 THR A O 1 ATOM 1486 C CB . THR A 1 184 ? 2.399 8.841 47.635 1.00 20.93 ? 184 THR A CB 1 ATOM 1487 O OG1 . THR A 1 184 ? 3.755 9.075 48.047 1.00 19.20 ? 184 THR A OG1 1 ATOM 1488 C CG2 . THR A 1 184 ? 1.503 8.786 48.884 1.00 19.75 ? 184 THR A CG2 1 ATOM 1489 N N . TYR A 1 185 ? 2.708 6.674 44.592 1.00 23.61 ? 185 TYR A N 1 ATOM 1490 C CA . TYR A 1 185 ? 2.973 6.822 43.162 1.00 28.30 ? 185 TYR A CA 1 ATOM 1491 C C . TYR A 1 185 ? 2.360 5.750 42.274 1.00 33.19 ? 185 TYR A C 1 ATOM 1492 O O . TYR A 1 185 ? 2.760 5.579 41.121 1.00 34.10 ? 185 TYR A O 1 ATOM 1493 C CB . TYR A 1 185 ? 4.472 6.912 42.894 1.00 23.10 ? 185 TYR A CB 1 ATOM 1494 C CG . TYR A 1 185 ? 5.313 5.868 43.592 1.00 22.80 ? 185 TYR A CG 1 ATOM 1495 C CD1 . TYR A 1 185 ? 5.321 4.538 43.168 1.00 22.48 ? 185 TYR A CD1 1 ATOM 1496 C CD2 . TYR A 1 185 ? 6.128 6.225 44.663 1.00 21.02 ? 185 TYR A CD2 1 ATOM 1497 C CE1 . TYR A 1 185 ? 6.133 3.585 43.804 1.00 21.95 ? 185 TYR A CE1 1 ATOM 1498 C CE2 . TYR A 1 185 ? 6.935 5.298 45.296 1.00 22.27 ? 185 TYR A CE2 1 ATOM 1499 C CZ . TYR A 1 185 ? 6.938 3.984 44.868 1.00 20.84 ? 185 TYR A CZ 1 ATOM 1500 O OH . TYR A 1 185 ? 7.764 3.108 45.533 1.00 21.78 ? 185 TYR A OH 1 ATOM 1501 N N . ASP A 1 186 ? 1.387 5.026 42.806 1.00 37.27 ? 186 ASP A N 1 ATOM 1502 C CA . ASP A 1 186 ? 0.715 4.001 42.017 1.00 43.50 ? 186 ASP A CA 1 ATOM 1503 C C . ASP A 1 186 ? -0.769 4.301 42.079 1.00 44.17 ? 186 ASP A C 1 ATOM 1504 O O . ASP A 1 186 ? -1.578 3.432 42.397 1.00 45.21 ? 186 ASP A O 1 ATOM 1505 C CB . ASP A 1 186 ? 0.975 2.610 42.592 1.00 46.63 ? 186 ASP A CB 1 ATOM 1506 C CG . ASP A 1 186 ? 0.247 1.526 41.825 1.00 50.86 ? 186 ASP A CG 1 ATOM 1507 O OD1 . ASP A 1 186 ? -0.165 0.521 42.453 1.00 52.90 ? 186 ASP A OD1 1 ATOM 1508 O OD2 . ASP A 1 186 ? 0.085 1.693 40.593 1.00 52.89 ? 186 ASP A OD2 1 ATOM 1509 N N . PHE A 1 187 ? -1.128 5.539 41.770 1.00 44.99 ? 187 PHE A N 1 ATOM 1510 C CA . PHE A 1 187 ? -2.521 5.933 41.844 1.00 48.26 ? 187 PHE A CA 1 ATOM 1511 C C . PHE A 1 187 ? -3.412 5.677 40.643 1.00 53.15 ? 187 PHE A C 1 ATOM 1512 O O . PHE A 1 187 ? -4.618 5.502 40.811 1.00 55.78 ? 187 PHE A O 1 ATOM 1513 C CB . PHE A 1 187 ? -2.619 7.389 42.278 1.00 43.42 ? 187 PHE A CB 1 ATOM 1514 C CG . PHE A 1 187 ? -2.331 7.588 43.736 1.00 39.79 ? 187 PHE A CG 1 ATOM 1515 C CD1 . PHE A 1 187 ? -3.072 6.900 44.696 1.00 38.47 ? 187 PHE A CD1 1 ATOM 1516 C CD2 . PHE A 1 187 ? -1.334 8.463 44.158 1.00 34.81 ? 187 PHE A CD2 1 ATOM 1517 C CE1 . PHE A 1 187 ? -2.830 7.082 46.059 1.00 36.07 ? 187 PHE A CE1 1 ATOM 1518 C CE2 . PHE A 1 187 ? -1.080 8.654 45.524 1.00 32.22 ? 187 PHE A CE2 1 ATOM 1519 C CZ . PHE A 1 187 ? -1.833 7.962 46.475 1.00 32.85 ? 187 PHE A CZ 1 ATOM 1520 N N . HIS A 1 188 ? -2.862 5.654 39.436 1.00 57.81 ? 188 HIS A N 1 ATOM 1521 C CA . HIS A 1 188 ? -3.729 5.370 38.309 1.00 62.11 ? 188 HIS A CA 1 ATOM 1522 C C . HIS A 1 188 ? -3.800 3.857 38.219 1.00 65.93 ? 188 HIS A C 1 ATOM 1523 O O . HIS A 1 188 ? -2.774 3.184 38.141 1.00 67.67 ? 188 HIS A O 1 ATOM 1524 C CB . HIS A 1 188 ? -3.193 5.957 37.010 1.00 61.17 ? 188 HIS A CB 1 ATOM 1525 C CG . HIS A 1 188 ? -4.266 6.226 36.002 1.00 62.09 ? 188 HIS A CG 1 ATOM 1526 N ND1 . HIS A 1 188 ? -4.253 5.690 34.733 1.00 61.55 ? 188 HIS A ND1 1 ATOM 1527 C CD2 . HIS A 1 188 ? -5.409 6.948 36.095 1.00 61.84 ? 188 HIS A CD2 1 ATOM 1528 C CE1 . HIS A 1 188 ? -5.342 6.068 34.088 1.00 61.20 ? 188 HIS A CE1 1 ATOM 1529 N NE2 . HIS A 1 188 ? -6.061 6.831 34.892 1.00 61.64 ? 188 HIS A NE2 1 ATOM 1530 N N . GLY A 1 189 ? -5.016 3.327 38.259 1.00 69.75 ? 189 GLY A N 1 ATOM 1531 C CA . GLY A 1 189 ? -5.200 1.888 38.207 1.00 73.67 ? 189 GLY A CA 1 ATOM 1532 C C . GLY A 1 189 ? -4.865 1.237 36.881 1.00 76.52 ? 189 GLY A C 1 ATOM 1533 O O . GLY A 1 189 ? -5.424 1.593 35.840 1.00 77.01 ? 189 GLY A O 1 ATOM 1534 N N . ALA A 1 190 ? -3.957 0.268 36.920 1.00 78.85 ? 190 ALA A N 1 ATOM 1535 C CA . ALA A 1 190 ? -3.563 -0.443 35.716 1.00 81.25 ? 190 ALA A CA 1 ATOM 1536 C C . ALA A 1 190 ? -4.795 -1.091 35.092 1.00 82.84 ? 190 ALA A C 1 ATOM 1537 O O . ALA A 1 190 ? -4.722 -1.633 33.989 1.00 82.54 ? 190 ALA A O 1 ATOM 1538 C CB . ALA A 1 190 ? -2.521 -1.509 36.048 1.00 81.27 ? 190 ALA A CB 1 ATOM 1539 N N . TRP A 1 191 ? -5.930 -1.027 35.788 1.00 84.74 ? 191 TRP A N 1 ATOM 1540 C CA . TRP A 1 191 ? -7.138 -1.640 35.253 1.00 86.26 ? 191 TRP A CA 1 ATOM 1541 C C . TRP A 1 191 ? -7.834 -0.943 34.090 1.00 85.73 ? 191 TRP A C 1 ATOM 1542 O O . TRP A 1 191 ? -8.258 -1.616 33.151 1.00 86.48 ? 191 TRP A O 1 ATOM 1543 C CB . TRP A 1 191 ? -8.184 -1.950 36.355 1.00 88.67 ? 191 TRP A CB 1 ATOM 1544 C CG . TRP A 1 191 ? -8.420 -0.943 37.484 1.00 91.64 ? 191 TRP A CG 1 ATOM 1545 C CD1 . TRP A 1 191 ? -7.764 -0.890 38.687 1.00 92.83 ? 191 TRP A CD1 1 ATOM 1546 C CD2 . TRP A 1 191 ? -9.462 0.047 37.559 1.00 92.95 ? 191 TRP A CD2 1 ATOM 1547 N NE1 . TRP A 1 191 ? -8.342 0.055 39.505 1.00 93.28 ? 191 TRP A NE1 1 ATOM 1548 C CE2 . TRP A 1 191 ? -9.385 0.644 38.841 1.00 93.42 ? 191 TRP A CE2 1 ATOM 1549 C CE3 . TRP A 1 191 ? -10.460 0.477 36.675 1.00 93.64 ? 191 TRP A CE3 1 ATOM 1550 C CZ2 . TRP A 1 191 ? -10.262 1.658 39.252 1.00 93.86 ? 191 TRP A CZ2 1 ATOM 1551 C CZ3 . TRP A 1 191 ? -11.333 1.486 37.085 1.00 94.11 ? 191 TRP A CZ3 1 ATOM 1552 C CH2 . TRP A 1 191 ? -11.229 2.060 38.365 1.00 94.05 ? 191 TRP A CH2 1 ATOM 1553 N N . ARG A 1 192 ? -7.950 0.382 34.111 1.00 84.67 ? 192 ARG A N 1 ATOM 1554 C CA . ARG A 1 192 ? -8.647 1.037 33.008 1.00 82.87 ? 192 ARG A CA 1 ATOM 1555 C C . ARG A 1 192 ? -7.890 1.636 31.828 1.00 80.02 ? 192 ARG A C 1 ATOM 1556 O O . ARG A 1 192 ? -6.676 1.858 31.866 1.00 79.81 ? 192 ARG A O 1 ATOM 1557 C CB . ARG A 1 192 ? -9.640 2.071 33.540 1.00 84.77 ? 192 ARG A CB 1 ATOM 1558 C CG . ARG A 1 192 ? -11.048 1.505 33.707 1.00 88.20 ? 192 ARG A CG 1 ATOM 1559 C CD . ARG A 1 192 ? -11.622 0.981 32.380 1.00 91.17 ? 192 ARG A CD 1 ATOM 1560 N NE . ARG A 1 192 ? -10.744 0.011 31.723 1.00 93.59 ? 192 ARG A NE 1 ATOM 1561 C CZ . ARG A 1 192 ? -11.020 -0.608 30.577 1.00 94.88 ? 192 ARG A CZ 1 ATOM 1562 N NH1 . ARG A 1 192 ? -12.163 -0.369 29.948 1.00 95.11 ? 192 ARG A NH1 1 ATOM 1563 N NH2 . ARG A 1 192 ? -10.144 -1.456 30.051 1.00 95.27 ? 192 ARG A NH2 1 ATOM 1564 N N . GLN A 1 193 ? -8.663 1.890 30.775 1.00 76.25 ? 193 GLN A N 1 ATOM 1565 C CA . GLN A 1 193 ? -8.174 2.432 29.514 1.00 72.02 ? 193 GLN A CA 1 ATOM 1566 C C . GLN A 1 193 ? -8.309 3.941 29.358 1.00 67.91 ? 193 GLN A C 1 ATOM 1567 O O . GLN A 1 193 ? -8.817 4.421 28.344 1.00 66.33 ? 193 GLN A O 1 ATOM 1568 C CB . GLN A 1 193 ? -8.910 1.767 28.352 1.00 74.39 ? 193 GLN A CB 1 ATOM 1569 C CG . GLN A 1 193 ? -10.428 1.853 28.465 1.00 76.53 ? 193 GLN A CG 1 ATOM 1570 C CD . GLN A 1 193 ? -11.103 2.143 27.138 1.00 77.91 ? 193 GLN A CD 1 ATOM 1571 O OE1 . GLN A 1 193 ? -11.348 3.301 26.788 1.00 77.97 ? 193 GLN A OE1 1 ATOM 1572 N NE2 . GLN A 1 193 ? -11.397 1.090 26.386 1.00 78.25 ? 193 GLN A NE2 1 ATOM 1573 N N . THR A 1 194 ? -7.855 4.689 30.351 1.00 63.39 ? 194 THR A N 1 ATOM 1574 C CA . THR A 1 194 ? -7.911 6.139 30.276 1.00 59.79 ? 194 THR A CA 1 ATOM 1575 C C . THR A 1 194 ? -6.563 6.704 30.659 1.00 55.92 ? 194 THR A C 1 ATOM 1576 O O . THR A 1 194 ? -5.791 6.061 31.362 1.00 55.67 ? 194 THR A O 1 ATOM 1577 C CB . THR A 1 194 ? -8.978 6.731 31.217 1.00 61.16 ? 194 THR A CB 1 ATOM 1578 O OG1 . THR A 1 194 ? -9.226 5.824 32.300 1.00 63.58 ? 194 THR A OG1 1 ATOM 1579 C CG2 . THR A 1 194 ? -10.262 7.013 30.452 1.00 61.54 ? 194 THR A CG2 1 ATOM 1580 N N . VAL A 1 195 ? -6.279 7.903 30.173 1.00 51.53 ? 195 VAL A N 1 ATOM 1581 C CA . VAL A 1 195 ? -5.027 8.566 30.484 1.00 48.46 ? 195 VAL A CA 1 ATOM 1582 C C . VAL A 1 195 ? -5.176 9.165 31.883 1.00 45.42 ? 195 VAL A C 1 ATOM 1583 O O . VAL A 1 195 ? -6.253 9.639 32.245 1.00 43.64 ? 195 VAL A O 1 ATOM 1584 C CB . VAL A 1 195 ? -4.726 9.675 29.444 1.00 48.12 ? 195 VAL A CB 1 ATOM 1585 C CG1 . VAL A 1 195 ? -4.317 10.955 30.134 1.00 49.40 ? 195 VAL A CG1 1 ATOM 1586 C CG2 . VAL A 1 195 ? -3.626 9.213 28.504 1.00 49.71 ? 195 VAL A CG2 1 ATOM 1587 N N . GLY A 1 196 ? -4.101 9.131 32.667 1.00 41.95 ? 196 GLY A N 1 ATOM 1588 C CA . GLY A 1 196 ? -4.149 9.670 34.016 1.00 36.76 ? 196 GLY A CA 1 ATOM 1589 C C . GLY A 1 196 ? -2.783 9.664 34.675 1.00 35.09 ? 196 GLY A C 1 ATOM 1590 O O . GLY A 1 196 ? -1.903 8.899 34.281 1.00 34.44 ? 196 GLY A O 1 ATOM 1591 N N . HIS A 1 197 ? -2.595 10.513 35.679 1.00 31.70 ? 197 HIS A N 1 ATOM 1592 C CA . HIS A 1 197 ? -1.310 10.581 36.361 1.00 29.22 ? 197 HIS A CA 1 ATOM 1593 C C . HIS A 1 197 ? -1.264 9.650 37.561 1.00 28.94 ? 197 HIS A C 1 ATOM 1594 O O . HIS A 1 197 ? -2.185 9.619 38.376 1.00 29.05 ? 197 HIS A O 1 ATOM 1595 C CB . HIS A 1 197 ? -1.009 12.015 36.796 1.00 25.30 ? 197 HIS A CB 1 ATOM 1596 C CG . HIS A 1 197 ? 0.454 12.305 36.904 1.00 26.61 ? 197 HIS A CG 1 ATOM 1597 N ND1 . HIS A 1 197 ? 1.252 11.746 37.877 1.00 24.84 ? 197 HIS A ND1 1 ATOM 1598 C CD2 . HIS A 1 197 ? 1.278 13.042 36.120 1.00 24.59 ? 197 HIS A CD2 1 ATOM 1599 C CE1 . HIS A 1 197 ? 2.504 12.123 37.687 1.00 24.18 ? 197 HIS A CE1 1 ATOM 1600 N NE2 . HIS A 1 197 ? 2.546 12.908 36.627 1.00 22.51 ? 197 HIS A NE2 1 ATOM 1601 N N . HIS A 1 198 ? -0.169 8.904 37.664 1.00 27.51 ? 198 HIS A N 1 ATOM 1602 C CA . HIS A 1 198 ? 0.030 7.941 38.736 1.00 27.32 ? 198 HIS A CA 1 ATOM 1603 C C . HIS A 1 198 ? 0.488 8.516 40.073 1.00 26.05 ? 198 HIS A C 1 ATOM 1604 O O . HIS A 1 198 ? 0.393 7.836 41.095 1.00 23.62 ? 198 HIS A O 1 ATOM 1605 C CB . HIS A 1 198 ? 1.042 6.887 38.290 1.00 28.14 ? 198 HIS A CB 1 ATOM 1606 C CG . HIS A 1 198 ? 2.407 7.442 38.036 1.00 28.70 ? 198 HIS A CG 1 ATOM 1607 N ND1 . HIS A 1 198 ? 3.497 7.131 38.821 1.00 31.92 ? 198 HIS A ND1 1 ATOM 1608 C CD2 . HIS A 1 198 ? 2.852 8.320 37.106 1.00 27.60 ? 198 HIS A CD2 1 ATOM 1609 C CE1 . HIS A 1 198 ? 4.553 7.795 38.387 1.00 31.11 ? 198 HIS A CE1 1 ATOM 1610 N NE2 . HIS A 1 198 ? 4.188 8.524 37.348 1.00 30.03 ? 198 HIS A NE2 1 ATOM 1611 N N . SER A 1 199 ? 0.994 9.748 40.078 1.00 24.79 ? 199 SER A N 1 ATOM 1612 C CA . SER A 1 199 ? 1.473 10.343 41.325 1.00 25.21 ? 199 SER A CA 1 ATOM 1613 C C . SER A 1 199 ? 1.061 11.795 41.534 1.00 24.64 ? 199 SER A C 1 ATOM 1614 O O . SER A 1 199 ? 1.901 12.652 41.804 1.00 23.72 ? 199 SER A O 1 ATOM 1615 C CB . SER A 1 199 ? 3.002 10.255 41.397 1.00 27.54 ? 199 SER A CB 1 ATOM 1616 O OG . SER A 1 199 ? 3.605 11.084 40.408 1.00 30.58 ? 199 SER A OG 1 ATOM 1617 N N . PRO A 1 200 ? -0.241 12.090 41.429 1.00 22.39 ? 200 PRO A N 1 ATOM 1618 C CA . PRO A 1 200 ? -0.638 13.484 41.632 1.00 22.73 ? 200 PRO A CA 1 ATOM 1619 C C . PRO A 1 200 ? -0.507 13.865 43.110 1.00 23.83 ? 200 PRO A C 1 ATOM 1620 O O . PRO A 1 200 ? -0.677 13.022 43.994 1.00 23.41 ? 200 PRO A O 1 ATOM 1621 C CB . PRO A 1 200 ? -2.085 13.497 41.153 1.00 22.88 ? 200 PRO A CB 1 ATOM 1622 C CG . PRO A 1 200 ? -2.575 12.127 41.563 1.00 23.95 ? 200 PRO A CG 1 ATOM 1623 C CD . PRO A 1 200 ? -1.412 11.218 41.207 1.00 20.41 ? 200 PRO A CD 1 ATOM 1624 N N . LEU A 1 201 ? -0.196 15.127 43.380 1.00 23.55 ? 201 LEU A N 1 ATOM 1625 C CA . LEU A 1 201 ? -0.056 15.571 44.757 1.00 26.72 ? 201 LEU A CA 1 ATOM 1626 C C . LEU A 1 201 ? -1.434 15.884 45.319 1.00 29.65 ? 201 LEU A C 1 ATOM 1627 O O . LEU A 1 201 ? -1.779 15.456 46.419 1.00 27.43 ? 201 LEU A O 1 ATOM 1628 C CB . LEU A 1 201 ? 0.837 16.812 44.838 1.00 26.62 ? 201 LEU A CB 1 ATOM 1629 C CG . LEU A 1 201 ? 1.031 17.387 46.247 1.00 27.51 ? 201 LEU A CG 1 ATOM 1630 C CD1 . LEU A 1 201 ? 1.528 16.296 47.177 1.00 27.91 ? 201 LEU A CD1 1 ATOM 1631 C CD2 . LEU A 1 201 ? 2.016 18.541 46.206 1.00 27.64 ? 201 LEU A CD2 1 ATOM 1632 N N . PHE A 1 202 ? -2.224 16.621 44.546 1.00 30.49 ? 202 PHE A N 1 ATOM 1633 C CA . PHE A 1 202 ? -3.560 16.993 44.973 1.00 34.67 ? 202 PHE A CA 1 ATOM 1634 C C . PHE A 1 202 ? -4.679 16.386 44.155 1.00 37.94 ? 202 PHE A C 1 ATOM 1635 O O . PHE A 1 202 ? -4.470 15.874 43.053 1.00 37.12 ? 202 PHE A O 1 ATOM 1636 C CB . PHE A 1 202 ? -3.709 18.513 44.973 1.00 30.90 ? 202 PHE A CB 1 ATOM 1637 C CG . PHE A 1 202 ? -2.864 19.195 46.001 1.00 29.67 ? 202 PHE A CG 1 ATOM 1638 C CD1 . PHE A 1 202 ? -3.116 19.003 47.359 1.00 28.74 ? 202 PHE A CD1 1 ATOM 1639 C CD2 . PHE A 1 202 ? -1.797 20.007 45.620 1.00 29.47 ? 202 PHE A CD2 1 ATOM 1640 C CE1 . PHE A 1 202 ? -2.316 19.615 48.331 1.00 27.21 ? 202 PHE A CE1 1 ATOM 1641 C CE2 . PHE A 1 202 ? -0.990 20.626 46.580 1.00 28.96 ? 202 PHE A CE2 1 ATOM 1642 C CZ . PHE A 1 202 ? -1.250 20.426 47.941 1.00 29.08 ? 202 PHE A CZ 1 ATOM 1643 N N . ARG A 1 203 ? -5.873 16.474 44.728 1.00 44.76 ? 203 ARG A N 1 ATOM 1644 C CA . ARG A 1 203 ? -7.117 15.974 44.158 1.00 51.95 ? 203 ARG A CA 1 ATOM 1645 C C . ARG A 1 203 ? -7.409 16.520 42.764 1.00 55.04 ? 203 ARG A C 1 ATOM 1646 O O . ARG A 1 203 ? -7.618 15.758 41.821 1.00 54.88 ? 203 ARG A O 1 ATOM 1647 C CB . ARG A 1 203 ? -8.254 16.336 45.115 1.00 55.68 ? 203 ARG A CB 1 ATOM 1648 C CG . ARG A 1 203 ? -8.032 17.699 45.770 1.00 61.32 ? 203 ARG A CG 1 ATOM 1649 C CD . ARG A 1 203 ? -8.912 17.930 46.992 1.00 66.13 ? 203 ARG A CD 1 ATOM 1650 N NE . ARG A 1 203 ? -8.536 19.158 47.696 1.00 70.37 ? 203 ARG A NE 1 ATOM 1651 C CZ . ARG A 1 203 ? -9.064 19.563 48.850 1.00 72.63 ? 203 ARG A CZ 1 ATOM 1652 N NH1 . ARG A 1 203 ? -10.003 18.841 49.448 1.00 72.37 ? 203 ARG A NH1 1 ATOM 1653 N NH2 . ARG A 1 203 ? -8.650 20.694 49.410 1.00 74.15 ? 203 ARG A NH2 1 ATOM 1654 N N . GLY A 1 204 ? -7.420 17.840 42.636 1.00 58.88 ? 204 GLY A N 1 ATOM 1655 C CA . GLY A 1 204 ? -7.708 18.440 41.348 1.00 66.73 ? 204 GLY A CA 1 ATOM 1656 C C . GLY A 1 204 ? -9.189 18.730 41.189 1.00 70.89 ? 204 GLY A C 1 ATOM 1657 O O . GLY A 1 204 ? -10.000 17.819 41.015 1.00 70.97 ? 204 GLY A O 1 ATOM 1658 N N . ASN A 1 205 ? -9.536 20.012 41.251 1.00 75.87 ? 205 ASN A N 1 ATOM 1659 C CA . ASN A 1 205 ? -10.919 20.469 41.130 1.00 81.02 ? 205 ASN A CA 1 ATOM 1660 C C . ASN A 1 205 ? -11.693 19.879 39.953 1.00 83.91 ? 205 ASN A C 1 ATOM 1661 O O . ASN A 1 205 ? -12.921 19.970 39.911 1.00 84.95 ? 205 ASN A O 1 ATOM 1662 C CB . ASN A 1 205 ? -10.949 21.996 41.014 1.00 81.81 ? 205 ASN A CB 1 ATOM 1663 C CG . ASN A 1 205 ? -10.561 22.688 42.304 1.00 83.48 ? 205 ASN A CG 1 ATOM 1664 O OD1 . ASN A 1 205 ? -9.686 22.219 43.031 1.00 84.32 ? 205 ASN A OD1 1 ATOM 1665 N ND2 . ASN A 1 205 ? -11.201 23.819 42.587 1.00 83.73 ? 205 ASN A ND2 1 ATOM 1666 N N . SER A 1 206 ? -10.988 19.274 39.001 1.00 86.71 ? 206 SER A N 1 ATOM 1667 C CA . SER A 1 206 ? -11.648 18.716 37.825 1.00 89.52 ? 206 SER A CA 1 ATOM 1668 C C . SER A 1 206 ? -12.055 17.243 37.841 1.00 91.41 ? 206 SER A C 1 ATOM 1669 O O . SER A 1 206 ? -11.867 16.545 36.842 1.00 91.76 ? 206 SER A O 1 ATOM 1670 C CB . SER A 1 206 ? -10.800 18.981 36.578 1.00 89.90 ? 206 SER A CB 1 ATOM 1671 O OG . SER A 1 206 ? -10.973 20.312 36.117 1.00 90.80 ? 206 SER A OG 1 ATOM 1672 N N . ASP A 1 207 ? -12.619 16.769 38.950 1.00 93.41 ? 207 ASP A N 1 ATOM 1673 C CA . ASP A 1 207 ? -13.076 15.380 39.029 1.00 95.60 ? 207 ASP A CA 1 ATOM 1674 C C . ASP A 1 207 ? -13.554 14.972 40.423 1.00 96.76 ? 207 ASP A C 1 ATOM 1675 O O . ASP A 1 207 ? -12.802 15.024 41.398 1.00 97.29 ? 207 ASP A O 1 ATOM 1676 C CB . ASP A 1 207 ? -11.983 14.424 38.545 1.00 95.84 ? 207 ASP A CB 1 ATOM 1677 C CG . ASP A 1 207 ? -12.551 13.220 37.822 1.00 96.24 ? 207 ASP A CG 1 ATOM 1678 O OD1 . ASP A 1 207 ? -12.656 12.137 38.441 1.00 96.54 ? 207 ASP A OD1 1 ATOM 1679 O OD2 . ASP A 1 207 ? -12.904 13.372 36.632 1.00 96.39 ? 207 ASP A OD2 1 ATOM 1680 N N . ALA A 1 208 ? -14.813 14.547 40.491 1.00 97.33 ? 208 ALA A N 1 ATOM 1681 C CA . ALA A 1 208 ? -15.453 14.144 41.739 1.00 97.49 ? 208 ALA A CA 1 ATOM 1682 C C . ALA A 1 208 ? -14.984 12.824 42.353 1.00 97.25 ? 208 ALA A C 1 ATOM 1683 O O . ALA A 1 208 ? -14.546 12.797 43.503 1.00 98.19 ? 208 ALA A O 1 ATOM 1684 C CB . ALA A 1 208 ? -16.965 14.108 41.545 1.00 97.72 ? 208 ALA A CB 1 ATOM 1685 N N . SER A 1 209 ? -15.087 11.731 41.601 1.00 95.95 ? 209 SER A N 1 ATOM 1686 C CA . SER A 1 209 ? -14.687 10.425 42.117 1.00 94.11 ? 209 SER A CA 1 ATOM 1687 C C . SER A 1 209 ? -13.180 10.280 42.283 1.00 91.52 ? 209 SER A C 1 ATOM 1688 O O . SER A 1 209 ? -12.400 11.061 41.736 1.00 91.72 ? 209 SER A O 1 ATOM 1689 C CB . SER A 1 209 ? -15.210 9.311 41.208 1.00 95.40 ? 209 SER A CB 1 ATOM 1690 O OG . SER A 1 209 ? -14.917 8.036 41.753 1.00 96.83 ? 209 SER A OG 1 ATOM 1691 N N . SER A 1 210 ? -12.789 9.263 43.043 1.00 87.15 ? 210 SER A N 1 ATOM 1692 C CA . SER A 1 210 ? -11.389 8.976 43.320 1.00 80.76 ? 210 SER A CA 1 ATOM 1693 C C . SER A 1 210 ? -10.653 10.180 43.904 1.00 74.81 ? 210 SER A C 1 ATOM 1694 O O . SER A 1 210 ? -9.574 10.538 43.440 1.00 75.34 ? 210 SER A O 1 ATOM 1695 C CB . SER A 1 210 ? -10.674 8.496 42.051 1.00 82.68 ? 210 SER A CB 1 ATOM 1696 O OG . SER A 1 210 ? -10.537 9.539 41.102 1.00 84.82 ? 210 SER A OG 1 ATOM 1697 N N . ARG A 1 211 ? -11.248 10.812 44.912 1.00 66.61 ? 212 ARG A N 1 ATOM 1698 C CA . ARG A 1 211 ? -10.612 11.939 45.584 1.00 60.44 ? 212 ARG A CA 1 ATOM 1699 C C . ARG A 1 211 ? -9.555 11.290 46.462 1.00 54.43 ? 212 ARG A C 1 ATOM 1700 O O . ARG A 1 211 ? -8.713 11.957 47.056 1.00 56.90 ? 212 ARG A O 1 ATOM 1701 C CB . ARG A 1 211 ? -11.631 12.698 46.452 1.00 61.26 ? 212 ARG A CB 1 ATOM 1702 C CG . ARG A 1 211 ? -11.088 13.282 47.780 1.00 63.51 ? 212 ARG A CG 1 ATOM 1703 C CD . ARG A 1 211 ? -9.885 14.233 47.618 1.00 62.12 ? 212 ARG A CD 1 ATOM 1704 N NE . ARG A 1 211 ? -9.377 14.700 48.911 1.00 62.46 ? 212 ARG A NE 1 ATOM 1705 C CZ . ARG A 1 211 ? -8.175 15.241 49.106 1.00 64.89 ? 212 ARG A CZ 1 ATOM 1706 N NH1 . ARG A 1 211 ? -7.330 15.390 48.092 1.00 64.90 ? 212 ARG A NH1 1 ATOM 1707 N NH2 . ARG A 1 211 ? -7.818 15.639 50.322 1.00 65.29 ? 212 ARG A NH2 1 ATOM 1708 N N . PHE A 1 212 ? -9.607 9.966 46.522 1.00 48.37 ? 213 PHE A N 1 ATOM 1709 C CA . PHE A 1 212 ? -8.675 9.195 47.333 1.00 42.98 ? 213 PHE A CA 1 ATOM 1710 C C . PHE A 1 212 ? -7.334 8.940 46.661 1.00 38.28 ? 213 PHE A C 1 ATOM 1711 O O . PHE A 1 212 ? -6.344 8.657 47.334 1.00 37.66 ? 213 PHE A O 1 ATOM 1712 C CB . PHE A 1 212 ? -9.290 7.842 47.695 1.00 42.83 ? 213 PHE A CB 1 ATOM 1713 C CG . PHE A 1 212 ? -10.642 7.940 48.330 1.00 44.20 ? 213 PHE A CG 1 ATOM 1714 C CD1 . PHE A 1 212 ? -10.915 8.944 49.253 1.00 44.74 ? 213 PHE A CD1 1 ATOM 1715 C CD2 . PHE A 1 212 ? -11.626 6.995 48.050 1.00 45.05 ? 213 PHE A CD2 1 ATOM 1716 C CE1 . PHE A 1 212 ? -12.143 9.013 49.894 1.00 44.26 ? 213 PHE A CE1 1 ATOM 1717 C CE2 . PHE A 1 212 ? -12.865 7.050 48.687 1.00 46.44 ? 213 PHE A CE2 1 ATOM 1718 C CZ . PHE A 1 212 ? -13.121 8.064 49.615 1.00 44.77 ? 213 PHE A CZ 1 ATOM 1719 N N . SER A 1 213 ? -7.302 9.046 45.337 1.00 34.25 ? 214 SER A N 1 ATOM 1720 C CA . SER A 1 213 ? -6.085 8.759 44.586 1.00 32.28 ? 214 SER A CA 1 ATOM 1721 C C . SER A 1 213 ? -5.087 9.893 44.343 1.00 30.64 ? 214 SER A C 1 ATOM 1722 O O . SER A 1 213 ? -4.773 10.236 43.199 1.00 30.69 ? 214 SER A O 1 ATOM 1723 C CB . SER A 1 213 ? -6.468 8.106 43.258 1.00 32.39 ? 214 SER A CB 1 ATOM 1724 O OG . SER A 1 213 ? -7.188 6.906 43.500 1.00 35.12 ? 214 SER A OG 1 ATOM 1725 N N . ASN A 1 214 ? -4.567 10.449 45.430 1.00 25.89 ? 215 ASN A N 1 ATOM 1726 C CA . ASN A 1 214 ? -3.580 11.517 45.364 1.00 25.43 ? 215 ASN A CA 1 ATOM 1727 C C . ASN A 1 214 ? -2.781 11.462 46.658 1.00 24.52 ? 215 ASN A C 1 ATOM 1728 O O . ASN A 1 214 ? -3.259 10.927 47.658 1.00 24.87 ? 215 ASN A O 1 ATOM 1729 C CB . ASN A 1 214 ? -4.275 12.879 45.169 1.00 25.30 ? 215 ASN A CB 1 ATOM 1730 C CG . ASN A 1 214 ? -5.352 13.146 46.203 1.00 28.45 ? 215 ASN A CG 1 ATOM 1731 O OD1 . ASN A 1 214 ? -5.079 13.676 47.283 1.00 27.85 ? 215 ASN A OD1 1 ATOM 1732 N ND2 . ASN A 1 214 ? -6.588 12.768 45.881 1.00 25.92 ? 215 ASN A ND2 1 ATOM 1733 N N . ALA A 1 215 ? -1.564 11.996 46.638 1.00 24.25 ? 216 ALA A N 1 ATOM 1734 C CA . ALA A 1 215 ? -0.694 11.973 47.814 1.00 24.92 ? 216 ALA A CA 1 ATOM 1735 C C . ALA A 1 215 ? -1.295 12.651 49.046 1.00 25.44 ? 216 ALA A C 1 ATOM 1736 O O . ALA A 1 215 ? -1.222 12.116 50.154 1.00 25.40 ? 216 ALA A O 1 ATOM 1737 C CB . ALA A 1 215 ? 0.656 12.616 47.480 1.00 23.22 ? 216 ALA A CB 1 ATOM 1738 N N . ASP A 1 216 ? -1.880 13.828 48.854 1.00 24.22 ? 217 ASP A N 1 ATOM 1739 C CA . ASP A 1 216 ? -2.459 14.564 49.969 1.00 25.74 ? 217 ASP A CA 1 ATOM 1740 C C . ASP A 1 216 ? -3.511 13.759 50.726 1.00 25.13 ? 217 ASP A C 1 ATOM 1741 O O . ASP A 1 216 ? -3.532 13.759 51.954 1.00 24.14 ? 217 ASP A O 1 ATOM 1742 C CB . ASP A 1 216 ? -3.045 15.892 49.474 1.00 26.25 ? 217 ASP A CB 1 ATOM 1743 C CG . ASP A 1 216 ? -3.840 16.615 50.545 1.00 27.95 ? 217 ASP A CG 1 ATOM 1744 O OD1 . ASP A 1 216 ? -5.086 16.646 50.443 1.00 31.57 ? 217 ASP A OD1 1 ATOM 1745 O OD2 . ASP A 1 216 ? -3.216 17.149 51.486 1.00 27.36 ? 217 ASP A OD2 1 ATOM 1746 N N . TYR A 1 217 ? -4.386 13.067 50.008 1.00 25.06 ? 218 TYR A N 1 ATOM 1747 C CA . TYR A 1 217 ? -5.403 12.281 50.690 1.00 25.61 ? 218 TYR A CA 1 ATOM 1748 C C . TYR A 1 217 ? -4.774 11.150 51.504 1.00 24.65 ? 218 TYR A C 1 ATOM 1749 O O . TYR A 1 217 ? -5.098 10.969 52.678 1.00 22.91 ? 218 TYR A O 1 ATOM 1750 C CB . TYR A 1 217 ? -6.391 11.668 49.702 1.00 24.99 ? 218 TYR A CB 1 ATOM 1751 C CG . TYR A 1 217 ? -7.536 10.992 50.422 1.00 27.33 ? 218 TYR A CG 1 ATOM 1752 C CD1 . TYR A 1 217 ? -8.654 11.725 50.823 1.00 28.84 ? 218 TYR A CD1 1 ATOM 1753 C CD2 . TYR A 1 217 ? -7.452 9.651 50.806 1.00 26.61 ? 218 TYR A CD2 1 ATOM 1754 C CE1 . TYR A 1 217 ? -9.660 11.141 51.598 1.00 28.73 ? 218 TYR A CE1 1 ATOM 1755 C CE2 . TYR A 1 217 ? -8.450 9.056 51.584 1.00 28.12 ? 218 TYR A CE2 1 ATOM 1756 C CZ . TYR A 1 217 ? -9.551 9.810 51.976 1.00 30.01 ? 218 TYR A CZ 1 ATOM 1757 O OH . TYR A 1 217 ? -10.542 9.228 52.735 1.00 31.15 ? 218 TYR A OH 1 ATOM 1758 N N . ALA A 1 218 ? -3.889 10.384 50.868 1.00 24.01 ? 219 ALA A N 1 ATOM 1759 C CA . ALA A 1 218 ? -3.217 9.257 51.522 1.00 21.79 ? 219 ALA A CA 1 ATOM 1760 C C . ALA A 1 218 ? -2.486 9.684 52.792 1.00 21.30 ? 219 ALA A C 1 ATOM 1761 O O . ALA A 1 218 ? -2.536 8.992 53.813 1.00 19.30 ? 219 ALA A O 1 ATOM 1762 C CB . ALA A 1 218 ? -2.235 8.600 50.550 1.00 22.68 ? 219 ALA A CB 1 ATOM 1763 N N . VAL A 1 219 ? -1.805 10.823 52.733 1.00 20.20 ? 220 VAL A N 1 ATOM 1764 C CA . VAL A 1 219 ? -1.084 11.317 53.900 1.00 19.99 ? 220 VAL A CA 1 ATOM 1765 C C . VAL A 1 219 ? -2.056 11.664 55.031 1.00 22.00 ? 220 VAL A C 1 ATOM 1766 O O . VAL A 1 219 ? -1.878 11.222 56.171 1.00 19.16 ? 220 VAL A O 1 ATOM 1767 C CB . VAL A 1 219 ? -0.238 12.571 53.557 1.00 22.92 ? 220 VAL A CB 1 ATOM 1768 C CG1 . VAL A 1 219 ? 0.283 13.213 54.839 1.00 20.55 ? 220 VAL A CG1 1 ATOM 1769 C CG2 . VAL A 1 219 ? 0.941 12.181 52.649 1.00 20.60 ? 220 VAL A CG2 1 ATOM 1770 N N . SER A 1 220 ? -3.079 12.456 54.714 1.00 21.16 ? 221 SER A N 1 ATOM 1771 C CA . SER A 1 220 ? -4.085 12.859 55.707 1.00 22.65 ? 221 SER A CA 1 ATOM 1772 C C . SER A 1 220 ? -4.741 11.644 56.340 1.00 22.36 ? 221 SER A C 1 ATOM 1773 O O . SER A 1 220 ? -4.945 11.595 57.546 1.00 24.40 ? 221 SER A O 1 ATOM 1774 C CB . SER A 1 220 ? -5.182 13.703 55.053 1.00 20.07 ? 221 SER A CB 1 ATOM 1775 O OG . SER A 1 220 ? -4.666 14.898 54.494 1.00 21.91 ? 221 SER A OG 1 ATOM 1776 N N . TYR A 1 221 ? -5.083 10.666 55.512 1.00 23.22 ? 222 TYR A N 1 ATOM 1777 C CA . TYR A 1 221 ? -5.727 9.451 55.998 1.00 26.06 ? 222 TYR A CA 1 ATOM 1778 C C . TYR A 1 221 ? -4.826 8.689 56.971 1.00 27.98 ? 222 TYR A C 1 ATOM 1779 O O . TYR A 1 221 ? -5.278 8.243 58.029 1.00 27.90 ? 222 TYR A O 1 ATOM 1780 C CB . TYR A 1 221 ? -6.097 8.548 54.824 1.00 27.39 ? 222 TYR A CB 1 ATOM 1781 C CG . TYR A 1 221 ? -7.111 7.478 55.172 1.00 31.33 ? 222 TYR A CG 1 ATOM 1782 C CD1 . TYR A 1 221 ? -8.364 7.818 55.690 1.00 30.46 ? 222 TYR A CD1 1 ATOM 1783 C CD2 . TYR A 1 221 ? -6.824 6.127 54.970 1.00 29.79 ? 222 TYR A CD2 1 ATOM 1784 C CE1 . TYR A 1 221 ? -9.306 6.836 55.996 1.00 33.92 ? 222 TYR A CE1 1 ATOM 1785 C CE2 . TYR A 1 221 ? -7.761 5.139 55.271 1.00 31.12 ? 222 TYR A CE2 1 ATOM 1786 C CZ . TYR A 1 221 ? -9.000 5.503 55.783 1.00 32.62 ? 222 TYR A CZ 1 ATOM 1787 O OH . TYR A 1 221 ? -9.941 4.546 56.072 1.00 33.64 ? 222 TYR A OH 1 ATOM 1788 N N . MET A 1 222 ? -3.553 8.537 56.616 1.00 25.47 ? 223 MET A N 1 ATOM 1789 C CA . MET A 1 222 ? -2.615 7.834 57.482 1.00 24.53 ? 223 MET A CA 1 ATOM 1790 C C . MET A 1 222 ? -2.510 8.533 58.830 1.00 24.57 ? 223 MET A C 1 ATOM 1791 O O . MET A 1 222 ? -2.493 7.883 59.878 1.00 22.25 ? 223 MET A O 1 ATOM 1792 C CB . MET A 1 222 ? -1.225 7.761 56.832 1.00 24.01 ? 223 MET A CB 1 ATOM 1793 C CG . MET A 1 222 ? -1.105 6.760 55.690 1.00 26.42 ? 223 MET A CG 1 ATOM 1794 S SD . MET A 1 222 ? -1.353 5.048 56.230 1.00 28.20 ? 223 MET A SD 1 ATOM 1795 C CE . MET A 1 222 ? 0.183 4.750 57.054 1.00 29.92 ? 223 MET A CE 1 ATOM 1796 N N . LEU A 1 223 ? -2.428 9.858 58.808 1.00 24.14 ? 224 LEU A N 1 ATOM 1797 C CA . LEU A 1 223 ? -2.331 10.604 60.056 1.00 28.79 ? 224 LEU A CA 1 ATOM 1798 C C . LEU A 1 223 ? -3.591 10.410 60.904 1.00 31.41 ? 224 LEU A C 1 ATOM 1799 O O . LEU A 1 223 ? -3.509 10.342 62.129 1.00 32.10 ? 224 LEU A O 1 ATOM 1800 C CB . LEU A 1 223 ? -2.104 12.094 59.780 1.00 26.86 ? 224 LEU A CB 1 ATOM 1801 C CG . LEU A 1 223 ? -0.759 12.480 59.149 1.00 27.25 ? 224 LEU A CG 1 ATOM 1802 C CD1 . LEU A 1 223 ? -0.769 13.955 58.784 1.00 27.46 ? 224 LEU A CD1 1 ATOM 1803 C CD2 . LEU A 1 223 ? 0.386 12.175 60.116 1.00 25.74 ? 224 LEU A CD2 1 ATOM 1804 N N . ARG A 1 224 ? -4.753 10.311 60.260 1.00 33.46 ? 225 ARG A N 1 ATOM 1805 C CA . ARG A 1 224 ? -5.998 10.129 61.004 1.00 36.69 ? 225 ARG A CA 1 ATOM 1806 C C . ARG A 1 224 ? -6.094 8.722 61.581 1.00 36.19 ? 225 ARG A C 1 ATOM 1807 O O . ARG A 1 224 ? -6.636 8.531 62.666 1.00 34.87 ? 225 ARG A O 1 ATOM 1808 C CB . ARG A 1 224 ? -7.209 10.399 60.110 1.00 40.63 ? 225 ARG A CB 1 ATOM 1809 C CG . ARG A 1 224 ? -8.310 11.236 60.775 1.00 49.68 ? 225 ARG A CG 1 ATOM 1810 C CD . ARG A 1 224 ? -9.229 10.445 61.717 1.00 56.03 ? 225 ARG A CD 1 ATOM 1811 N NE . ARG A 1 224 ? -8.612 10.069 62.988 1.00 61.74 ? 225 ARG A NE 1 ATOM 1812 C CZ . ARG A 1 224 ? -9.291 9.633 64.048 1.00 63.02 ? 225 ARG A CZ 1 ATOM 1813 N NH1 . ARG A 1 224 ? -10.614 9.523 63.994 1.00 62.77 ? 225 ARG A NH1 1 ATOM 1814 N NH2 . ARG A 1 224 ? -8.647 9.296 65.161 1.00 64.82 ? 225 ARG A NH2 1 ATOM 1815 N N . LEU A 1 225 ? -5.561 7.737 60.861 1.00 34.56 ? 226 LEU A N 1 ATOM 1816 C CA . LEU A 1 225 ? -5.601 6.357 61.333 1.00 34.26 ? 226 LEU A CA 1 ATOM 1817 C C . LEU A 1 225 ? -4.672 6.119 62.517 1.00 33.68 ? 226 LEU A C 1 ATOM 1818 O O . LEU A 1 225 ? -4.722 5.059 63.136 1.00 35.06 ? 226 LEU A O 1 ATOM 1819 C CB . LEU A 1 225 ? -5.262 5.380 60.202 1.00 35.00 ? 226 LEU A CB 1 ATOM 1820 C CG . LEU A 1 225 ? -6.386 5.030 59.219 1.00 36.54 ? 226 LEU A CG 1 ATOM 1821 C CD1 . LEU A 1 225 ? -7.453 4.183 59.904 1.00 38.34 ? 226 LEU A CD1 1 ATOM 1822 C CD2 . LEU A 1 225 ? -7.006 6.299 58.692 1.00 40.92 ? 226 LEU A CD2 1 ATOM 1823 N N . GLY A 1 226 ? -3.819 7.090 62.831 1.00 32.30 ? 227 GLY A N 1 ATOM 1824 C CA . GLY A 1 226 ? -2.937 6.921 63.974 1.00 32.33 ? 227 GLY A CA 1 ATOM 1825 C C . GLY A 1 226 ? -1.440 6.854 63.734 1.00 32.90 ? 227 GLY A C 1 ATOM 1826 O O . GLY A 1 226 ? -0.677 6.678 64.686 1.00 33.11 ? 227 GLY A O 1 ATOM 1827 N N . ALA A 1 227 ? -1.000 6.989 62.489 1.00 31.15 ? 228 ALA A N 1 ATOM 1828 C CA . ALA A 1 227 ? 0.428 6.946 62.212 1.00 30.57 ? 228 ALA A CA 1 ATOM 1829 C C . ALA A 1 227 ? 1.041 8.291 62.585 1.00 31.35 ? 228 ALA A C 1 ATOM 1830 O O . ALA A 1 227 ? 0.553 9.342 62.161 1.00 30.76 ? 228 ALA A O 1 ATOM 1831 C CB . ALA A 1 227 ? 0.670 6.645 60.740 1.00 30.95 ? 228 ALA A CB 1 ATOM 1832 N N . PRO A 1 228 ? 2.104 8.276 63.403 1.00 31.00 ? 229 PRO A N 1 ATOM 1833 C CA . PRO A 1 228 ? 2.751 9.529 63.807 1.00 30.92 ? 229 PRO A CA 1 ATOM 1834 C C . PRO A 1 228 ? 3.443 10.173 62.615 1.00 29.95 ? 229 PRO A C 1 ATOM 1835 O O . PRO A 1 228 ? 4.064 9.480 61.810 1.00 25.83 ? 229 PRO A O 1 ATOM 1836 C CB . PRO A 1 228 ? 3.752 9.086 64.878 1.00 31.57 ? 229 PRO A CB 1 ATOM 1837 C CG . PRO A 1 228 ? 3.180 7.783 65.393 1.00 34.01 ? 229 PRO A CG 1 ATOM 1838 C CD . PRO A 1 228 ? 2.683 7.128 64.126 1.00 33.87 ? 229 PRO A CD 1 ATOM 1839 N N . ALA A 1 229 ? 3.336 11.494 62.504 1.00 27.97 ? 230 ALA A N 1 ATOM 1840 C CA . ALA A 1 229 ? 3.964 12.202 61.402 1.00 27.54 ? 230 ALA A CA 1 ATOM 1841 C C . ALA A 1 229 ? 5.469 11.945 61.378 1.00 27.10 ? 230 ALA A C 1 ATOM 1842 O O . ALA A 1 229 ? 6.064 11.806 60.307 1.00 26.90 ? 230 ALA A O 1 ATOM 1843 C CB . ALA A 1 229 ? 3.689 13.704 61.513 1.00 27.15 ? 230 ALA A CB 1 ATOM 1844 N N . ASN A 1 230 ? 6.087 11.868 62.552 1.00 25.35 ? 231 ASN A N 1 ATOM 1845 C CA . ASN A 1 230 ? 7.525 11.650 62.610 1.00 26.81 ? 231 ASN A CA 1 ATOM 1846 C C . ASN A 1 230 ? 7.993 10.253 62.192 1.00 25.87 ? 231 ASN A C 1 ATOM 1847 O O . ASN A 1 230 ? 9.180 9.951 62.275 1.00 23.82 ? 231 ASN A O 1 ATOM 1848 C CB . ASN A 1 230 ? 8.083 12.001 64.004 1.00 30.73 ? 231 ASN A CB 1 ATOM 1849 C CG . ASN A 1 230 ? 7.469 11.175 65.128 1.00 33.12 ? 231 ASN A CG 1 ATOM 1850 O OD1 . ASN A 1 230 ? 6.872 10.126 64.902 1.00 37.82 ? 231 ASN A OD1 1 ATOM 1851 N ND2 . ASN A 1 230 ? 7.638 11.647 66.356 1.00 36.43 ? 231 ASN A ND2 1 ATOM 1852 N N . LYS A 1 231 ? 7.064 9.406 61.756 1.00 24.57 ? 232 LYS A N 1 ATOM 1853 C CA . LYS A 1 231 ? 7.419 8.074 61.283 1.00 25.70 ? 232 LYS A CA 1 ATOM 1854 C C . LYS A 1 231 ? 6.979 7.872 59.833 1.00 25.26 ? 232 LYS A C 1 ATOM 1855 O O . LYS A 1 231 ? 7.337 6.878 59.210 1.00 25.43 ? 232 LYS A O 1 ATOM 1856 C CB . LYS A 1 231 ? 6.806 6.984 62.170 1.00 25.16 ? 232 LYS A CB 1 ATOM 1857 C CG . LYS A 1 231 ? 7.595 6.721 63.451 1.00 25.67 ? 232 LYS A CG 1 ATOM 1858 C CD . LYS A 1 231 ? 7.020 5.550 64.213 1.00 24.99 ? 232 LYS A CD 1 ATOM 1859 C CE . LYS A 1 231 ? 7.875 5.197 65.416 1.00 22.82 ? 232 LYS A CE 1 ATOM 1860 N NZ . LYS A 1 231 ? 7.325 3.985 66.088 1.00 21.84 ? 232 LYS A NZ 1 ATOM 1861 N N . LEU A 1 232 ? 6.211 8.821 59.304 1.00 23.41 ? 233 LEU A N 1 ATOM 1862 C CA . LEU A 1 232 ? 5.728 8.751 57.923 1.00 24.35 ? 233 LEU A CA 1 ATOM 1863 C C . LEU A 1 232 ? 6.709 9.339 56.916 1.00 22.39 ? 233 LEU A C 1 ATOM 1864 O O . LEU A 1 232 ? 7.215 10.444 57.094 1.00 21.46 ? 233 LEU A O 1 ATOM 1865 C CB . LEU A 1 232 ? 4.395 9.491 57.769 1.00 27.19 ? 233 LEU A CB 1 ATOM 1866 C CG . LEU A 1 232 ? 3.087 8.714 57.858 1.00 32.83 ? 233 LEU A CG 1 ATOM 1867 C CD1 . LEU A 1 232 ? 1.936 9.644 57.487 1.00 32.56 ? 233 LEU A CD1 1 ATOM 1868 C CD2 . LEU A 1 232 ? 3.124 7.524 56.899 1.00 35.06 ? 233 LEU A CD2 1 ATOM 1869 N N . VAL A 1 233 ? 6.963 8.596 55.845 1.00 21.63 ? 234 VAL A N 1 ATOM 1870 C CA . VAL A 1 233 ? 7.870 9.046 54.793 1.00 20.70 ? 234 VAL A CA 1 ATOM 1871 C C . VAL A 1 233 ? 7.083 8.980 53.484 1.00 20.85 ? 234 VAL A C 1 ATOM 1872 O O . VAL A 1 233 ? 6.463 7.962 53.176 1.00 18.04 ? 234 VAL A O 1 ATOM 1873 C CB . VAL A 1 233 ? 9.136 8.146 54.734 1.00 23.77 ? 234 VAL A CB 1 ATOM 1874 C CG1 . VAL A 1 233 ? 9.963 8.479 53.514 1.00 21.43 ? 234 VAL A CG1 1 ATOM 1875 C CG2 . VAL A 1 233 ? 9.974 8.365 55.997 1.00 22.13 ? 234 VAL A CG2 1 ATOM 1876 N N . MET A 1 234 ? 7.097 10.065 52.715 1.00 17.75 ? 235 MET A N 1 ATOM 1877 C CA . MET A 1 234 ? 6.333 10.103 51.471 1.00 19.07 ? 235 MET A CA 1 ATOM 1878 C C . MET A 1 234 ? 7.112 9.653 50.239 1.00 17.89 ? 235 MET A C 1 ATOM 1879 O O . MET A 1 234 ? 8.167 10.198 49.921 1.00 17.26 ? 235 MET A O 1 ATOM 1880 C CB . MET A 1 234 ? 5.787 11.515 51.246 1.00 18.30 ? 235 MET A CB 1 ATOM 1881 C CG . MET A 1 234 ? 4.669 11.571 50.224 1.00 25.60 ? 235 MET A CG 1 ATOM 1882 S SD . MET A 1 234 ? 3.977 13.221 50.094 1.00 29.13 ? 235 MET A SD 1 ATOM 1883 C CE . MET A 1 234 ? 5.020 13.890 48.844 1.00 25.30 ? 235 MET A CE 1 ATOM 1884 N N . GLY A 1 235 ? 6.573 8.657 49.543 1.00 17.58 ? 236 GLY A N 1 ATOM 1885 C CA . GLY A 1 235 ? 7.227 8.140 48.357 1.00 19.37 ? 236 GLY A CA 1 ATOM 1886 C C . GLY A 1 235 ? 7.186 9.090 47.178 1.00 19.65 ? 236 GLY A C 1 ATOM 1887 O O . GLY A 1 235 ? 6.153 9.684 46.874 1.00 18.20 ? 236 GLY A O 1 ATOM 1888 N N . ILE A 1 236 ? 8.328 9.239 46.518 1.00 20.36 ? 237 ILE A N 1 ATOM 1889 C CA . ILE A 1 236 ? 8.445 10.107 45.352 1.00 19.83 ? 237 ILE A CA 1 ATOM 1890 C C . ILE A 1 236 ? 9.052 9.241 44.257 1.00 20.81 ? 237 ILE A C 1 ATOM 1891 O O . ILE A 1 236 ? 10.102 8.628 44.453 1.00 17.87 ? 237 ILE A O 1 ATOM 1892 C CB . ILE A 1 236 ? 9.352 11.320 45.652 1.00 20.62 ? 237 ILE A CB 1 ATOM 1893 C CG1 . ILE A 1 236 ? 8.640 12.249 46.645 1.00 21.97 ? 237 ILE A CG1 1 ATOM 1894 C CG2 . ILE A 1 236 ? 9.698 12.060 44.352 1.00 22.37 ? 237 ILE A CG2 1 ATOM 1895 C CD1 . ILE A 1 236 ? 9.472 13.421 47.124 1.00 24.72 ? 237 ILE A CD1 1 ATOM 1896 N N . PRO A 1 237 ? 8.394 9.177 43.089 1.00 19.92 ? 238 PRO A N 1 ATOM 1897 C CA . PRO A 1 237 ? 8.903 8.355 41.994 1.00 20.40 ? 238 PRO A CA 1 ATOM 1898 C C . PRO A 1 237 ? 9.937 9.038 41.129 1.00 22.24 ? 238 PRO A C 1 ATOM 1899 O O . PRO A 1 237 ? 9.909 10.253 40.923 1.00 20.70 ? 238 PRO A O 1 ATOM 1900 C CB . PRO A 1 237 ? 7.641 8.015 41.214 1.00 20.14 ? 238 PRO A CB 1 ATOM 1901 C CG . PRO A 1 237 ? 6.890 9.321 41.277 1.00 19.91 ? 238 PRO A CG 1 ATOM 1902 C CD . PRO A 1 237 ? 7.088 9.773 42.733 1.00 18.93 ? 238 PRO A CD 1 ATOM 1903 N N . THR A 1 238 ? 10.842 8.224 40.610 1.00 21.06 ? 239 THR A N 1 ATOM 1904 C CA . THR A 1 238 ? 11.902 8.700 39.764 1.00 25.02 ? 239 THR A CA 1 ATOM 1905 C C . THR A 1 238 ? 11.678 8.130 38.354 1.00 25.19 ? 239 THR A C 1 ATOM 1906 O O . THR A 1 238 ? 12.506 8.276 37.457 1.00 29.69 ? 239 THR A O 1 ATOM 1907 C CB . THR A 1 238 ? 13.242 8.340 40.404 1.00 25.32 ? 239 THR A CB 1 ATOM 1908 O OG1 . THR A 1 238 ? 14.102 9.476 40.376 1.00 33.07 ? 239 THR A OG1 1 ATOM 1909 C CG2 . THR A 1 238 ? 13.885 7.185 39.652 1.00 22.40 ? 239 THR A CG2 1 ATOM 1910 N N . PHE A 1 239 ? 10.527 7.497 38.173 1.00 24.23 ? 240 PHE A N 1 ATOM 1911 C CA . PHE A 1 239 ? 10.150 6.912 36.891 1.00 25.76 ? 240 PHE A CA 1 ATOM 1912 C C . PHE A 1 239 ? 8.830 7.521 36.438 1.00 24.82 ? 240 PHE A C 1 ATOM 1913 O O . PHE A 1 239 ? 8.173 8.236 37.194 1.00 26.64 ? 240 PHE A O 1 ATOM 1914 C CB . PHE A 1 239 ? 9.959 5.404 37.024 1.00 22.95 ? 240 PHE A CB 1 ATOM 1915 C CG . PHE A 1 239 ? 8.866 5.020 37.982 1.00 22.96 ? 240 PHE A CG 1 ATOM 1916 C CD1 . PHE A 1 239 ? 9.129 4.910 39.343 1.00 23.67 ? 240 PHE A CD1 1 ATOM 1917 C CD2 . PHE A 1 239 ? 7.567 4.799 37.530 1.00 21.39 ? 240 PHE A CD2 1 ATOM 1918 C CE1 . PHE A 1 239 ? 8.113 4.583 40.240 1.00 25.70 ? 240 PHE A CE1 1 ATOM 1919 C CE2 . PHE A 1 239 ? 6.538 4.471 38.422 1.00 26.26 ? 240 PHE A CE2 1 ATOM 1920 C CZ . PHE A 1 239 ? 6.814 4.362 39.781 1.00 24.32 ? 240 PHE A CZ 1 ATOM 1921 N N . GLY A 1 240 ? 8.445 7.211 35.205 1.00 25.28 ? 241 GLY A N 1 ATOM 1922 C CA . GLY A 1 240 ? 7.196 7.707 34.662 1.00 25.27 ? 241 GLY A CA 1 ATOM 1923 C C . GLY A 1 240 ? 6.375 6.540 34.155 1.00 24.56 ? 241 GLY A C 1 ATOM 1924 O O . GLY A 1 240 ? 6.919 5.462 33.922 1.00 25.00 ? 241 GLY A O 1 ATOM 1925 N N . ARG A 1 241 ? 5.065 6.725 34.021 1.00 24.97 ? 242 ARG A N 1 ATOM 1926 C CA . ARG A 1 241 ? 4.213 5.655 33.508 1.00 27.39 ? 242 ARG A CA 1 ATOM 1927 C C . ARG A 1 241 ? 3.766 6.086 32.097 1.00 28.01 ? 242 ARG A C 1 ATOM 1928 O O . ARG A 1 241 ? 3.341 7.223 31.888 1.00 24.93 ? 242 ARG A O 1 ATOM 1929 C CB . ARG A 1 241 ? 3.015 5.404 34.454 1.00 31.79 ? 242 ARG A CB 1 ATOM 1930 C CG . ARG A 1 241 ? 3.427 5.199 35.911 1.00 40.44 ? 242 ARG A CG 1 ATOM 1931 C CD . ARG A 1 241 ? 2.487 4.278 36.655 1.00 50.02 ? 242 ARG A CD 1 ATOM 1932 N NE . ARG A 1 241 ? 3.041 2.925 36.744 1.00 55.29 ? 242 ARG A NE 1 ATOM 1933 C CZ . ARG A 1 241 ? 3.381 2.301 37.873 1.00 58.44 ? 242 ARG A CZ 1 ATOM 1934 N NH1 . ARG A 1 241 ? 3.238 2.894 39.052 1.00 52.94 ? 242 ARG A NH1 1 ATOM 1935 N NH2 . ARG A 1 241 ? 3.839 1.057 37.816 1.00 57.71 ? 242 ARG A NH2 1 ATOM 1936 N N . SER A 1 242 ? 3.894 5.182 31.128 1.00 27.33 ? 243 SER A N 1 ATOM 1937 C CA . SER A 1 242 ? 3.544 5.477 29.740 1.00 27.78 ? 243 SER A CA 1 ATOM 1938 C C . SER A 1 242 ? 2.319 4.728 29.214 1.00 27.54 ? 243 SER A C 1 ATOM 1939 O O . SER A 1 242 ? 1.981 3.636 29.678 1.00 27.03 ? 243 SER A O 1 ATOM 1940 C CB . SER A 1 242 ? 4.737 5.163 28.841 1.00 28.36 ? 243 SER A CB 1 ATOM 1941 O OG . SER A 1 242 ? 5.004 3.772 28.903 1.00 28.82 ? 243 SER A OG 1 ATOM 1942 N N . PHE A 1 243 ? 1.672 5.337 28.224 1.00 29.06 ? 244 PHE A N 1 ATOM 1943 C CA . PHE A 1 243 ? 0.482 4.775 27.588 1.00 31.41 ? 244 PHE A CA 1 ATOM 1944 C C . PHE A 1 243 ? 0.512 4.973 26.075 1.00 31.40 ? 244 PHE A C 1 ATOM 1945 O O . PHE A 1 243 ? 1.100 5.928 25.564 1.00 29.72 ? 244 PHE A O 1 ATOM 1946 C CB . PHE A 1 243 ? -0.788 5.464 28.091 1.00 33.54 ? 244 PHE A CB 1 ATOM 1947 C CG . PHE A 1 243 ? -0.998 5.370 29.572 1.00 36.65 ? 244 PHE A CG 1 ATOM 1948 C CD1 . PHE A 1 243 ? -1.501 4.204 30.149 1.00 37.61 ? 244 PHE A CD1 1 ATOM 1949 C CD2 . PHE A 1 243 ? -0.713 6.460 30.390 1.00 37.53 ? 244 PHE A CD2 1 ATOM 1950 C CE1 . PHE A 1 243 ? -1.719 4.124 31.525 1.00 38.60 ? 244 PHE A CE1 1 ATOM 1951 C CE2 . PHE A 1 243 ? -0.925 6.394 31.764 1.00 39.05 ? 244 PHE A CE2 1 ATOM 1952 C CZ . PHE A 1 243 ? -1.432 5.222 32.334 1.00 38.22 ? 244 PHE A CZ 1 ATOM 1953 N N . THR A 1 244 ? -0.145 4.069 25.364 1.00 31.63 ? 245 THR A N 1 ATOM 1954 C CA . THR A 1 244 ? -0.255 4.184 23.918 1.00 33.43 ? 245 THR A CA 1 ATOM 1955 C C . THR A 1 244 ? -1.679 4.681 23.702 1.00 33.57 ? 245 THR A C 1 ATOM 1956 O O . THR A 1 244 ? -2.641 4.006 24.066 1.00 33.28 ? 245 THR A O 1 ATOM 1957 C CB . THR A 1 244 ? -0.073 2.826 23.221 1.00 33.53 ? 245 THR A CB 1 ATOM 1958 O OG1 . THR A 1 244 ? 1.256 2.340 23.456 1.00 30.31 ? 245 THR A OG1 1 ATOM 1959 C CG2 . THR A 1 244 ? -0.321 2.963 21.718 1.00 33.29 ? 245 THR A CG2 1 ATOM 1960 N N . LEU A 1 245 ? -1.804 5.877 23.139 1.00 36.30 ? 246 LEU A N 1 ATOM 1961 C CA . LEU A 1 245 ? -3.105 6.483 22.894 1.00 39.41 ? 246 LEU A CA 1 ATOM 1962 C C . LEU A 1 245 ? -3.915 5.710 21.858 1.00 42.26 ? 246 LEU A C 1 ATOM 1963 O O . LEU A 1 245 ? -3.361 5.129 20.927 1.00 41.46 ? 246 LEU A O 1 ATOM 1964 C CB . LEU A 1 245 ? -2.924 7.928 22.435 1.00 37.40 ? 246 LEU A CB 1 ATOM 1965 C CG . LEU A 1 245 ? -2.246 8.858 23.441 1.00 36.99 ? 246 LEU A CG 1 ATOM 1966 C CD1 . LEU A 1 245 ? -1.826 10.144 22.754 1.00 36.79 ? 246 LEU A CD1 1 ATOM 1967 C CD2 . LEU A 1 245 ? -3.196 9.144 24.599 1.00 39.02 ? 246 LEU A CD2 1 ATOM 1968 N N . ALA A 1 246 ? -5.232 5.706 22.033 1.00 45.37 ? 247 ALA A N 1 ATOM 1969 C CA . ALA A 1 246 ? -6.121 5.010 21.114 1.00 48.27 ? 247 ALA A CA 1 ATOM 1970 C C . ALA A 1 246 ? -6.709 6.003 20.117 1.00 50.71 ? 247 ALA A C 1 ATOM 1971 O O . ALA A 1 246 ? -7.284 5.609 19.103 1.00 51.59 ? 247 ALA A O 1 ATOM 1972 C CB . ALA A 1 246 ? -7.238 4.316 21.887 1.00 47.34 ? 247 ALA A CB 1 ATOM 1973 N N . SER A 1 247 ? -6.563 7.292 20.409 1.00 52.27 ? 248 SER A N 1 ATOM 1974 C CA . SER A 1 247 ? -7.078 8.329 19.527 1.00 54.30 ? 248 SER A CA 1 ATOM 1975 C C . SER A 1 247 ? -6.152 9.535 19.531 1.00 55.80 ? 248 SER A C 1 ATOM 1976 O O . SER A 1 247 ? -5.156 9.572 20.254 1.00 56.76 ? 248 SER A O 1 ATOM 1977 C CB . SER A 1 247 ? -8.474 8.770 19.970 1.00 55.26 ? 248 SER A CB 1 ATOM 1978 O OG . SER A 1 247 ? -8.397 9.712 21.028 1.00 55.80 ? 248 SER A OG 1 ATOM 1979 N N . SER A 1 248 ? -6.491 10.526 18.716 1.00 56.63 ? 249 SER A N 1 ATOM 1980 C CA . SER A 1 248 ? -5.698 11.739 18.620 1.00 58.36 ? 249 SER A CA 1 ATOM 1981 C C . SER A 1 248 ? -5.915 12.659 19.820 1.00 59.26 ? 249 SER A C 1 ATOM 1982 O O . SER A 1 248 ? -5.281 13.710 19.926 1.00 59.09 ? 249 SER A O 1 ATOM 1983 C CB . SER A 1 248 ? -6.034 12.472 17.321 1.00 58.85 ? 249 SER A CB 1 ATOM 1984 O OG . SER A 1 248 ? -7.424 12.404 17.047 1.00 60.25 ? 249 SER A OG 1 ATOM 1985 N N . LYS A 1 249 ? -6.809 12.262 20.722 1.00 60.28 ? 250 LYS A N 1 ATOM 1986 C CA . LYS A 1 249 ? -7.084 13.057 21.913 1.00 62.42 ? 250 LYS A CA 1 ATOM 1987 C C . LYS A 1 249 ? -5.920 12.878 22.884 1.00 62.78 ? 250 LYS A C 1 ATOM 1988 O O . LYS A 1 249 ? -5.487 11.755 23.141 1.00 61.54 ? 250 LYS A O 1 ATOM 1989 C CB . LYS A 1 249 ? -8.396 12.608 22.563 1.00 64.23 ? 250 LYS A CB 1 ATOM 1990 C CG . LYS A 1 249 ? -8.951 13.588 23.588 1.00 66.82 ? 250 LYS A CG 1 ATOM 1991 C CD . LYS A 1 249 ? -10.410 13.281 23.883 1.00 70.39 ? 250 LYS A CD 1 ATOM 1992 C CE . LYS A 1 249 ? -11.046 14.334 24.777 1.00 72.19 ? 250 LYS A CE 1 ATOM 1993 N NZ . LYS A 1 249 ? -10.509 14.298 26.162 1.00 73.99 ? 250 LYS A NZ 1 ATOM 1994 N N . THR A 1 250 ? -5.418 13.986 23.419 1.00 63.96 ? 251 THR A N 1 ATOM 1995 C CA . THR A 1 250 ? -4.281 13.941 24.333 1.00 65.90 ? 251 THR A CA 1 ATOM 1996 C C . THR A 1 250 ? -4.572 14.463 25.737 1.00 67.00 ? 251 THR A C 1 ATOM 1997 O O . THR A 1 250 ? -3.786 14.241 26.657 1.00 67.00 ? 251 THR A O 1 ATOM 1998 C CB . THR A 1 250 ? -3.097 14.745 23.762 1.00 65.66 ? 251 THR A CB 1 ATOM 1999 O OG1 . THR A 1 250 ? -1.936 14.539 24.576 1.00 67.73 ? 251 THR A OG1 1 ATOM 2000 C CG2 . THR A 1 250 ? -3.439 16.232 23.725 1.00 66.38 ? 251 THR A CG2 1 ATOM 2001 N N . ASP A 1 251 ? -5.693 15.158 25.905 1.00 67.99 ? 252 ASP A N 1 ATOM 2002 C CA . ASP A 1 251 ? -6.052 15.707 27.208 1.00 68.50 ? 252 ASP A CA 1 ATOM 2003 C C . ASP A 1 251 ? -6.639 14.687 28.178 1.00 67.95 ? 252 ASP A C 1 ATOM 2004 O O . ASP A 1 251 ? -6.827 13.520 27.836 1.00 67.56 ? 252 ASP A O 1 ATOM 2005 C CB . ASP A 1 251 ? -7.029 16.871 27.040 1.00 70.21 ? 252 ASP A CB 1 ATOM 2006 C CG . ASP A 1 251 ? -8.169 16.549 26.100 1.00 72.13 ? 252 ASP A CG 1 ATOM 2007 O OD1 . ASP A 1 251 ? -7.921 16.393 24.881 1.00 73.30 ? 252 ASP A OD1 1 ATOM 2008 O OD2 . ASP A 1 251 ? -9.315 16.456 26.588 1.00 74.42 ? 252 ASP A OD2 1 ATOM 2009 N N . VAL A 1 252 ? -6.921 15.149 29.394 1.00 67.59 ? 253 VAL A N 1 ATOM 2010 C CA . VAL A 1 252 ? -7.483 14.307 30.447 1.00 67.43 ? 253 VAL A CA 1 ATOM 2011 C C . VAL A 1 252 ? -8.703 13.528 29.961 1.00 66.28 ? 253 VAL A C 1 ATOM 2012 O O . VAL A 1 252 ? -9.603 14.090 29.333 1.00 66.22 ? 253 VAL A O 1 ATOM 2013 C CB . VAL A 1 252 ? -7.908 15.151 31.666 1.00 68.16 ? 253 VAL A CB 1 ATOM 2014 C CG1 . VAL A 1 252 ? -8.148 14.245 32.867 1.00 68.56 ? 253 VAL A CG1 1 ATOM 2015 C CG2 . VAL A 1 252 ? -6.848 16.195 31.972 1.00 68.65 ? 253 VAL A CG2 1 ATOM 2016 N N . GLY A 1 253 ? -8.726 12.233 30.255 1.00 64.69 ? 254 GLY A N 1 ATOM 2017 C CA . GLY A 1 253 ? -9.841 11.402 29.841 1.00 62.87 ? 254 GLY A CA 1 ATOM 2018 C C . GLY A 1 253 ? -9.569 10.624 28.566 1.00 61.55 ? 254 GLY A C 1 ATOM 2019 O O . GLY A 1 253 ? -10.183 9.583 28.325 1.00 62.02 ? 254 GLY A O 1 ATOM 2020 N N . ALA A 1 254 ? -8.641 11.129 27.757 1.00 59.50 ? 255 ALA A N 1 ATOM 2021 C CA . ALA A 1 254 ? -8.274 10.495 26.491 1.00 56.74 ? 255 ALA A CA 1 ATOM 2022 C C . ALA A 1 254 ? -8.195 8.976 26.605 1.00 54.63 ? 255 ALA A C 1 ATOM 2023 O O . ALA A 1 254 ? -7.584 8.444 27.529 1.00 54.06 ? 255 ALA A O 1 ATOM 2024 C CB . ALA A 1 254 ? -6.941 11.054 25.995 1.00 56.25 ? 255 ALA A CB 1 ATOM 2025 N N . PRO A 1 255 ? -8.810 8.259 25.650 1.00 52.92 ? 256 PRO A N 1 ATOM 2026 C CA . PRO A 1 255 ? -8.822 6.794 25.628 1.00 52.01 ? 256 PRO A CA 1 ATOM 2027 C C . PRO A 1 255 ? -7.430 6.182 25.467 1.00 51.42 ? 256 PRO A C 1 ATOM 2028 O O . PRO A 1 255 ? -6.543 6.760 24.833 1.00 50.39 ? 256 PRO A O 1 ATOM 2029 C CB . PRO A 1 255 ? -9.733 6.480 24.444 1.00 52.41 ? 256 PRO A CB 1 ATOM 2030 C CG . PRO A 1 255 ? -9.437 7.614 23.505 1.00 52.07 ? 256 PRO A CG 1 ATOM 2031 C CD . PRO A 1 255 ? -9.455 8.803 24.442 1.00 53.08 ? 256 PRO A CD 1 ATOM 2032 N N . ILE A 1 256 ? -7.258 5.001 26.046 1.00 51.09 ? 257 ILE A N 1 ATOM 2033 C CA . ILE A 1 256 ? -5.995 4.284 25.991 1.00 51.36 ? 257 ILE A CA 1 ATOM 2034 C C . ILE A 1 256 ? -6.188 2.931 25.322 1.00 51.50 ? 257 ILE A C 1 ATOM 2035 O O . ILE A 1 256 ? -7.245 2.318 25.445 1.00 53.09 ? 257 ILE A O 1 ATOM 2036 C CB . ILE A 1 256 ? -5.419 4.086 27.423 1.00 52.07 ? 257 ILE A CB 1 ATOM 2037 C CG1 . ILE A 1 256 ? -4.198 4.981 27.607 1.00 51.44 ? 257 ILE A CG1 1 ATOM 2038 C CG2 . ILE A 1 256 ? -5.062 2.623 27.671 1.00 51.54 ? 257 ILE A CG2 1 ATOM 2039 C CD1 . ILE A 1 256 ? -4.460 6.420 27.251 1.00 51.17 ? 257 ILE A CD1 1 ATOM 2040 N N . SER A 1 257 ? -5.168 2.466 24.609 1.00 50.50 ? 258 SER A N 1 ATOM 2041 C CA . SER A 1 257 ? -5.258 1.170 23.947 1.00 49.65 ? 258 SER A CA 1 ATOM 2042 C C . SER A 1 257 ? -4.410 0.170 24.725 1.00 48.25 ? 258 SER A C 1 ATOM 2043 O O . SER A 1 257 ? -4.627 -1.042 24.662 1.00 48.20 ? 258 SER A O 1 ATOM 2044 C CB . SER A 1 257 ? -4.750 1.261 22.505 1.00 51.00 ? 258 SER A CB 1 ATOM 2045 O OG . SER A 1 257 ? -3.337 1.176 22.449 1.00 53.71 ? 258 SER A OG 1 ATOM 2046 N N . GLY A 1 258 ? -3.440 0.698 25.464 1.00 45.69 ? 259 GLY A N 1 ATOM 2047 C CA . GLY A 1 258 ? -2.557 -0.140 26.254 1.00 41.89 ? 259 GLY A CA 1 ATOM 2048 C C . GLY A 1 258 ? -1.388 0.666 26.793 1.00 39.57 ? 259 GLY A C 1 ATOM 2049 O O . GLY A 1 258 ? -1.374 1.886 26.662 1.00 38.28 ? 259 GLY A O 1 ATOM 2050 N N . PRO A 1 259 ? -0.392 0.019 27.411 1.00 38.05 ? 260 PRO A N 1 ATOM 2051 C CA . PRO A 1 259 ? 0.764 0.744 27.949 1.00 37.64 ? 260 PRO A CA 1 ATOM 2052 C C . PRO A 1 259 ? 1.672 1.236 26.825 1.00 36.96 ? 260 PRO A C 1 ATOM 2053 O O . PRO A 1 259 ? 1.563 0.783 25.685 1.00 36.94 ? 260 PRO A O 1 ATOM 2054 C CB . PRO A 1 259 ? 1.445 -0.303 28.822 1.00 37.52 ? 260 PRO A CB 1 ATOM 2055 C CG . PRO A 1 259 ? 1.190 -1.567 28.050 1.00 39.03 ? 260 PRO A CG 1 ATOM 2056 C CD . PRO A 1 259 ? -0.271 -1.428 27.666 1.00 38.76 ? 260 PRO A CD 1 ATOM 2057 N N . GLY A 1 260 ? 2.565 2.166 27.146 1.00 35.43 ? 261 GLY A N 1 ATOM 2058 C CA . GLY A 1 260 ? 3.471 2.691 26.143 1.00 34.48 ? 261 GLY A CA 1 ATOM 2059 C C . GLY A 1 260 ? 4.521 1.669 25.752 1.00 34.88 ? 261 GLY A C 1 ATOM 2060 O O . GLY A 1 260 ? 4.688 0.647 26.428 1.00 32.67 ? 261 GLY A O 1 ATOM 2061 N N . ILE A 1 261 ? 5.234 1.930 24.659 1.00 34.34 ? 262 ILE A N 1 ATOM 2062 C CA . ILE A 1 261 ? 6.264 0.998 24.225 1.00 35.41 ? 262 ILE A CA 1 ATOM 2063 C C . ILE A 1 261 ? 7.467 1.115 25.154 1.00 34.71 ? 262 ILE A C 1 ATOM 2064 O O . ILE A 1 261 ? 7.726 2.179 25.721 1.00 33.12 ? 262 ILE A O 1 ATOM 2065 C CB . ILE A 1 261 ? 6.706 1.245 22.751 1.00 37.99 ? 262 ILE A CB 1 ATOM 2066 C CG1 . ILE A 1 261 ? 7.630 2.464 22.653 1.00 37.94 ? 262 ILE A CG1 1 ATOM 2067 C CG2 . ILE A 1 261 ? 5.471 1.430 21.863 1.00 36.79 ? 262 ILE A CG2 1 ATOM 2068 C CD1 . ILE A 1 261 ? 6.925 3.796 22.782 1.00 41.51 ? 262 ILE A CD1 1 ATOM 2069 N N . PRO A 1 262 ? 8.214 0.012 25.324 1.00 35.67 ? 263 PRO A N 1 ATOM 2070 C CA . PRO A 1 262 ? 9.397 -0.048 26.189 1.00 35.88 ? 263 PRO A CA 1 ATOM 2071 C C . PRO A 1 262 ? 10.454 1.007 25.914 1.00 35.38 ? 263 PRO A C 1 ATOM 2072 O O . PRO A 1 262 ? 10.579 1.507 24.795 1.00 34.37 ? 263 PRO A O 1 ATOM 2073 C CB . PRO A 1 262 ? 9.938 -1.455 25.943 1.00 35.62 ? 263 PRO A CB 1 ATOM 2074 C CG . PRO A 1 262 ? 8.704 -2.238 25.603 1.00 37.63 ? 263 PRO A CG 1 ATOM 2075 C CD . PRO A 1 262 ? 7.978 -1.291 24.677 1.00 35.91 ? 263 PRO A CD 1 ATOM 2076 N N . GLY A 1 263 ? 11.211 1.337 26.956 1.00 34.82 ? 264 GLY A N 1 ATOM 2077 C CA . GLY A 1 263 ? 12.285 2.296 26.823 1.00 33.69 ? 264 GLY A CA 1 ATOM 2078 C C . GLY A 1 263 ? 13.468 1.485 26.347 1.00 33.51 ? 264 GLY A C 1 ATOM 2079 O O . GLY A 1 263 ? 13.499 0.270 26.554 1.00 32.60 ? 264 GLY A O 1 ATOM 2080 N N . ARG A 1 264 ? 14.436 2.143 25.720 1.00 34.48 ? 265 ARG A N 1 ATOM 2081 C CA . ARG A 1 264 ? 15.618 1.466 25.190 1.00 36.78 ? 265 ARG A CA 1 ATOM 2082 C C . ARG A 1 264 ? 16.433 0.719 26.246 1.00 36.21 ? 265 ARG A C 1 ATOM 2083 O O . ARG A 1 264 ? 16.923 -0.387 25.999 1.00 36.14 ? 265 ARG A O 1 ATOM 2084 C CB . ARG A 1 264 ? 16.533 2.477 24.491 1.00 40.04 ? 265 ARG A CB 1 ATOM 2085 C CG . ARG A 1 264 ? 17.366 1.866 23.373 1.00 50.18 ? 265 ARG A CG 1 ATOM 2086 C CD . ARG A 1 264 ? 18.822 2.314 23.418 1.00 55.22 ? 265 ARG A CD 1 ATOM 2087 N NE . ARG A 1 264 ? 18.984 3.762 23.320 1.00 60.17 ? 265 ARG A NE 1 ATOM 2088 C CZ . ARG A 1 264 ? 20.153 4.367 23.122 1.00 63.28 ? 265 ARG A CZ 1 ATOM 2089 N NH1 . ARG A 1 264 ? 21.263 3.649 22.997 1.00 64.94 ? 265 ARG A NH1 1 ATOM 2090 N NH2 . ARG A 1 264 ? 20.217 5.690 23.056 1.00 64.27 ? 265 ARG A NH2 1 ATOM 2091 N N . PHE A 1 265 ? 16.574 1.325 27.421 1.00 32.78 ? 266 PHE A N 1 ATOM 2092 C CA . PHE A 1 265 ? 17.368 0.734 28.491 1.00 31.51 ? 266 PHE A CA 1 ATOM 2093 C C . PHE A 1 265 ? 16.595 -0.062 29.529 1.00 32.39 ? 266 PHE A C 1 ATOM 2094 O O . PHE A 1 265 ? 17.075 -1.085 30.018 1.00 30.63 ? 266 PHE A O 1 ATOM 2095 C CB . PHE A 1 265 ? 18.160 1.826 29.220 1.00 31.80 ? 266 PHE A CB 1 ATOM 2096 C CG . PHE A 1 265 ? 19.047 2.643 28.326 1.00 33.34 ? 266 PHE A CG 1 ATOM 2097 C CD1 . PHE A 1 265 ? 18.589 3.827 27.753 1.00 34.83 ? 266 PHE A CD1 1 ATOM 2098 C CD2 . PHE A 1 265 ? 20.349 2.231 28.064 1.00 33.81 ? 266 PHE A CD2 1 ATOM 2099 C CE1 . PHE A 1 265 ? 19.424 4.591 26.931 1.00 36.34 ? 266 PHE A CE1 1 ATOM 2100 C CE2 . PHE A 1 265 ? 21.190 2.981 27.246 1.00 35.70 ? 266 PHE A CE2 1 ATOM 2101 C CZ . PHE A 1 265 ? 20.733 4.163 26.678 1.00 35.85 ? 266 PHE A CZ 1 ATOM 2102 N N . THR A 1 266 ? 15.401 0.408 29.871 1.00 32.15 ? 267 THR A N 1 ATOM 2103 C CA . THR A 1 266 ? 14.607 -0.252 30.892 1.00 34.93 ? 267 THR A CA 1 ATOM 2104 C C . THR A 1 266 ? 13.774 -1.428 30.360 1.00 34.06 ? 267 THR A C 1 ATOM 2105 O O . THR A 1 266 ? 13.426 -2.336 31.110 1.00 32.64 ? 267 THR A O 1 ATOM 2106 C CB . THR A 1 266 ? 13.743 0.809 31.644 1.00 34.62 ? 267 THR A CB 1 ATOM 2107 O OG1 . THR A 1 266 ? 13.178 0.230 32.825 1.00 44.54 ? 267 THR A OG1 1 ATOM 2108 C CG2 . THR A 1 266 ? 12.664 1.351 30.761 1.00 30.77 ? 267 THR A CG2 1 ATOM 2109 N N . LYS A 1 267 ? 13.470 -1.405 29.066 1.00 35.42 ? 268 LYS A N 1 ATOM 2110 C CA . LYS A 1 267 ? 12.736 -2.479 28.394 1.00 37.14 ? 268 LYS A CA 1 ATOM 2111 C C . LYS A 1 267 ? 11.543 -3.079 29.125 1.00 37.95 ? 268 LYS A C 1 ATOM 2112 O O . LYS A 1 267 ? 11.408 -4.298 29.217 1.00 36.97 ? 268 LYS A O 1 ATOM 2113 C CB . LYS A 1 267 ? 13.721 -3.590 28.030 1.00 39.04 ? 268 LYS A CB 1 ATOM 2114 C CG . LYS A 1 267 ? 15.039 -3.018 27.547 1.00 42.90 ? 268 LYS A CG 1 ATOM 2115 C CD . LYS A 1 267 ? 15.613 -3.746 26.348 1.00 48.86 ? 268 LYS A CD 1 ATOM 2116 C CE . LYS A 1 267 ? 16.583 -4.831 26.776 1.00 51.36 ? 268 LYS A CE 1 ATOM 2117 N NZ . LYS A 1 267 ? 17.466 -4.318 27.863 1.00 56.09 ? 268 LYS A NZ 1 ATOM 2118 N N . GLU A 1 268 ? 10.669 -2.222 29.630 1.00 38.86 ? 269 GLU A N 1 ATOM 2119 C CA . GLU A 1 268 ? 9.486 -2.679 30.336 1.00 39.24 ? 269 GLU A CA 1 ATOM 2120 C C . GLU A 1 268 ? 8.318 -1.812 29.889 1.00 38.35 ? 269 GLU A C 1 ATOM 2121 O O . GLU A 1 268 ? 8.298 -0.612 30.155 1.00 37.78 ? 269 GLU A O 1 ATOM 2122 C CB . GLU A 1 268 ? 9.691 -2.548 31.844 1.00 41.55 ? 269 GLU A CB 1 ATOM 2123 C CG . GLU A 1 268 ? 8.649 -3.286 32.664 1.00 47.45 ? 269 GLU A CG 1 ATOM 2124 C CD . GLU A 1 268 ? 8.836 -3.089 34.156 1.00 50.78 ? 269 GLU A CD 1 ATOM 2125 O OE1 . GLU A 1 268 ? 9.979 -3.239 34.636 1.00 52.78 ? 269 GLU A OE1 1 ATOM 2126 O OE2 . GLU A 1 268 ? 7.843 -2.788 34.853 1.00 53.51 ? 269 GLU A OE2 1 ATOM 2127 N N . LYS A 1 269 ? 7.362 -2.413 29.188 1.00 36.47 ? 270 LYS A N 1 ATOM 2128 C CA . LYS A 1 269 ? 6.199 -1.681 28.714 1.00 37.23 ? 270 LYS A CA 1 ATOM 2129 C C . LYS A 1 269 ? 5.519 -1.032 29.910 1.00 35.17 ? 270 LYS A C 1 ATOM 2130 O O . LYS A 1 269 ? 5.417 -1.642 30.974 1.00 33.22 ? 270 LYS A O 1 ATOM 2131 C CB . LYS A 1 269 ? 5.217 -2.637 28.038 1.00 41.10 ? 270 LYS A CB 1 ATOM 2132 C CG . LYS A 1 269 ? 5.768 -3.335 26.805 1.00 46.79 ? 270 LYS A CG 1 ATOM 2133 C CD . LYS A 1 269 ? 4.889 -4.515 26.406 1.00 51.31 ? 270 LYS A CD 1 ATOM 2134 C CE . LYS A 1 269 ? 4.838 -5.555 27.521 1.00 53.67 ? 270 LYS A CE 1 ATOM 2135 N NZ . LYS A 1 269 ? 4.123 -6.795 27.107 1.00 56.38 ? 270 LYS A NZ 1 ATOM 2136 N N . GLY A 1 270 ? 5.076 0.209 29.747 1.00 33.19 ? 271 GLY A N 1 ATOM 2137 C CA . GLY A 1 270 ? 4.386 0.873 30.836 1.00 33.59 ? 271 GLY A CA 1 ATOM 2138 C C . GLY A 1 270 ? 5.191 1.844 31.673 1.00 32.37 ? 271 GLY A C 1 ATOM 2139 O O . GLY A 1 270 ? 4.612 2.742 32.282 1.00 31.80 ? 271 GLY A O 1 ATOM 2140 N N . ILE A 1 271 ? 6.509 1.678 31.733 1.00 30.25 ? 272 ILE A N 1 ATOM 2141 C CA . ILE A 1 271 ? 7.313 2.604 32.516 1.00 31.26 ? 272 ILE A CA 1 ATOM 2142 C C . ILE A 1 271 ? 8.578 3.033 31.789 1.00 29.70 ? 272 ILE A C 1 ATOM 2143 O O . ILE A 1 271 ? 9.064 2.343 30.889 1.00 28.18 ? 272 ILE A O 1 ATOM 2144 C CB . ILE A 1 271 ? 7.719 2.012 33.903 1.00 34.79 ? 272 ILE A CB 1 ATOM 2145 C CG1 . ILE A 1 271 ? 8.828 0.975 33.739 1.00 35.21 ? 272 ILE A CG1 1 ATOM 2146 C CG2 . ILE A 1 271 ? 6.507 1.400 34.601 1.00 35.92 ? 272 ILE A CG2 1 ATOM 2147 C CD1 . ILE A 1 271 ? 10.218 1.568 33.790 1.00 39.59 ? 272 ILE A CD1 1 ATOM 2148 N N . LEU A 1 272 ? 9.098 4.185 32.199 1.00 25.80 ? 273 LEU A N 1 ATOM 2149 C CA . LEU A 1 272 ? 10.321 4.746 31.637 1.00 24.99 ? 273 LEU A CA 1 ATOM 2150 C C . LEU A 1 272 ? 11.117 5.346 32.786 1.00 24.53 ? 273 LEU A C 1 ATOM 2151 O O . LEU A 1 272 ? 10.533 5.911 33.711 1.00 24.26 ? 273 LEU A O 1 ATOM 2152 C CB . LEU A 1 272 ? 9.997 5.860 30.632 1.00 22.95 ? 273 LEU A CB 1 ATOM 2153 C CG . LEU A 1 272 ? 9.335 5.505 29.292 1.00 22.50 ? 273 LEU A CG 1 ATOM 2154 C CD1 . LEU A 1 272 ? 9.062 6.779 28.488 1.00 21.60 ? 273 LEU A CD1 1 ATOM 2155 C CD2 . LEU A 1 272 ? 10.266 4.574 28.503 1.00 20.30 ? 273 LEU A CD2 1 ATOM 2156 N N . ALA A 1 273 ? 12.438 5.224 32.733 1.00 22.50 ? 274 ALA A N 1 ATOM 2157 C CA . ALA A 1 273 ? 13.290 5.792 33.771 1.00 22.86 ? 274 ALA A CA 1 ATOM 2158 C C . ALA A 1 273 ? 13.300 7.285 33.502 1.00 23.30 ? 274 ALA A C 1 ATOM 2159 O O . ALA A 1 273 ? 12.995 7.710 32.385 1.00 24.81 ? 274 ALA A O 1 ATOM 2160 C CB . ALA A 1 273 ? 14.707 5.229 33.660 1.00 22.47 ? 274 ALA A CB 1 ATOM 2161 N N . TYR A 1 274 ? 13.633 8.090 34.503 1.00 21.44 ? 275 TYR A N 1 ATOM 2162 C CA . TYR A 1 274 ? 13.671 9.528 34.285 1.00 23.81 ? 275 TYR A CA 1 ATOM 2163 C C . TYR A 1 274 ? 14.692 9.884 33.201 1.00 25.17 ? 275 TYR A C 1 ATOM 2164 O O . TYR A 1 274 ? 14.461 10.795 32.404 1.00 24.18 ? 275 TYR A O 1 ATOM 2165 C CB . TYR A 1 274 ? 14.029 10.272 35.572 1.00 24.12 ? 275 TYR A CB 1 ATOM 2166 C CG . TYR A 1 274 ? 14.013 11.772 35.390 1.00 25.52 ? 275 TYR A CG 1 ATOM 2167 C CD1 . TYR A 1 274 ? 12.855 12.419 34.966 1.00 27.52 ? 275 TYR A CD1 1 ATOM 2168 C CD2 . TYR A 1 274 ? 15.160 12.538 35.597 1.00 27.42 ? 275 TYR A CD2 1 ATOM 2169 C CE1 . TYR A 1 274 ? 12.831 13.790 34.747 1.00 30.20 ? 275 TYR A CE1 1 ATOM 2170 C CE2 . TYR A 1 274 ? 15.151 13.919 35.383 1.00 29.48 ? 275 TYR A CE2 1 ATOM 2171 C CZ . TYR A 1 274 ? 13.979 14.535 34.958 1.00 31.25 ? 275 TYR A CZ 1 ATOM 2172 O OH . TYR A 1 274 ? 13.939 15.897 34.766 1.00 34.58 ? 275 TYR A OH 1 ATOM 2173 N N . TYR A 1 275 ? 15.819 9.173 33.166 1.00 25.16 ? 276 TYR A N 1 ATOM 2174 C CA . TYR A 1 275 ? 16.825 9.477 32.157 1.00 26.10 ? 276 TYR A CA 1 ATOM 2175 C C . TYR A 1 275 ? 16.318 9.155 30.747 1.00 25.57 ? 276 TYR A C 1 ATOM 2176 O O . TYR A 1 275 ? 16.752 9.776 29.778 1.00 26.55 ? 276 TYR A O 1 ATOM 2177 C CB . TYR A 1 275 ? 18.167 8.777 32.467 1.00 24.82 ? 276 TYR A CB 1 ATOM 2178 C CG . TYR A 1 275 ? 18.165 7.258 32.526 1.00 26.47 ? 276 TYR A CG 1 ATOM 2179 C CD1 . TYR A 1 275 ? 18.169 6.494 31.356 1.00 27.04 ? 276 TYR A CD1 1 ATOM 2180 C CD2 . TYR A 1 275 ? 18.198 6.582 33.755 1.00 24.80 ? 276 TYR A CD2 1 ATOM 2181 C CE1 . TYR A 1 275 ? 18.210 5.101 31.403 1.00 25.05 ? 276 TYR A CE1 1 ATOM 2182 C CE2 . TYR A 1 275 ? 18.233 5.184 33.811 1.00 22.81 ? 276 TYR A CE2 1 ATOM 2183 C CZ . TYR A 1 275 ? 18.241 4.453 32.631 1.00 25.85 ? 276 TYR A CZ 1 ATOM 2184 O OH . TYR A 1 275 ? 18.278 3.073 32.672 1.00 27.28 ? 276 TYR A OH 1 ATOM 2185 N N . GLU A 1 276 ? 15.389 8.209 30.631 1.00 23.44 ? 277 GLU A N 1 ATOM 2186 C CA . GLU A 1 276 ? 14.818 7.881 29.324 1.00 24.14 ? 277 GLU A CA 1 ATOM 2187 C C . GLU A 1 276 ? 13.786 8.945 28.960 1.00 24.98 ? 277 GLU A C 1 ATOM 2188 O O . GLU A 1 276 ? 13.595 9.270 27.787 1.00 25.35 ? 277 GLU A O 1 ATOM 2189 C CB . GLU A 1 276 ? 14.156 6.501 29.339 1.00 23.45 ? 277 GLU A CB 1 ATOM 2190 C CG . GLU A 1 276 ? 15.154 5.351 29.392 1.00 24.23 ? 277 GLU A CG 1 ATOM 2191 C CD . GLU A 1 276 ? 14.481 4.018 29.615 1.00 28.58 ? 277 GLU A CD 1 ATOM 2192 O OE1 . GLU A 1 276 ? 13.591 3.956 30.488 1.00 26.49 ? 277 GLU A OE1 1 ATOM 2193 O OE2 . GLU A 1 276 ? 14.846 3.038 28.933 1.00 30.05 ? 277 GLU A OE2 1 ATOM 2194 N N . ILE A 1 277 ? 13.126 9.496 29.972 1.00 24.64 ? 278 ILE A N 1 ATOM 2195 C CA . ILE A 1 277 ? 12.131 10.540 29.751 1.00 25.79 ? 278 ILE A CA 1 ATOM 2196 C C . ILE A 1 277 ? 12.819 11.812 29.257 1.00 25.17 ? 278 ILE A C 1 ATOM 2197 O O . ILE A 1 277 ? 12.279 12.517 28.413 1.00 23.69 ? 278 ILE A O 1 ATOM 2198 C CB . ILE A 1 277 ? 11.346 10.834 31.054 1.00 26.24 ? 278 ILE A CB 1 ATOM 2199 C CG1 . ILE A 1 277 ? 10.406 9.660 31.354 1.00 25.73 ? 278 ILE A CG1 1 ATOM 2200 C CG2 . ILE A 1 277 ? 10.580 12.157 30.944 1.00 25.06 ? 278 ILE A CG2 1 ATOM 2201 C CD1 . ILE A 1 277 ? 9.740 9.726 32.720 1.00 25.76 ? 278 ILE A CD1 1 ATOM 2202 N N . CYS A 1 278 ? 14.009 12.100 29.781 1.00 26.44 ? 279 CYS A N 1 ATOM 2203 C CA . CYS A 1 278 ? 14.757 13.285 29.356 1.00 30.05 ? 279 CYS A CA 1 ATOM 2204 C C . CYS A 1 278 ? 15.061 13.235 27.861 1.00 32.23 ? 279 CYS A C 1 ATOM 2205 O O . CYS A 1 278 ? 15.148 14.271 27.202 1.00 32.62 ? 279 CYS A O 1 ATOM 2206 C CB . CYS A 1 278 ? 16.071 13.426 30.135 1.00 30.17 ? 279 CYS A CB 1 ATOM 2207 S SG . CYS A 1 278 ? 15.820 13.879 31.877 1.00 31.31 ? 279 CYS A SG 1 ATOM 2208 N N . ASP A 1 279 ? 15.227 12.024 27.333 1.00 32.65 ? 280 ASP A N 1 ATOM 2209 C CA . ASP A 1 279 ? 15.506 11.834 25.911 1.00 32.16 ? 280 ASP A CA 1 ATOM 2210 C C . ASP A 1 279 ? 14.196 11.962 25.130 1.00 31.66 ? 280 ASP A C 1 ATOM 2211 O O . ASP A 1 279 ? 14.145 12.589 24.074 1.00 32.54 ? 280 ASP A O 1 ATOM 2212 C CB . ASP A 1 279 ? 16.138 10.452 25.691 1.00 34.28 ? 280 ASP A CB 1 ATOM 2213 C CG . ASP A 1 279 ? 16.541 10.208 24.247 1.00 39.71 ? 280 ASP A CG 1 ATOM 2214 O OD1 . ASP A 1 279 ? 17.080 11.141 23.610 1.00 41.19 ? 280 ASP A OD1 1 ATOM 2215 O OD2 . ASP A 1 279 ? 16.327 9.074 23.764 1.00 42.13 ? 280 ASP A OD2 1 ATOM 2216 N N . PHE A 1 280 ? 13.138 11.377 25.681 1.00 30.82 ? 281 PHE A N 1 ATOM 2217 C CA . PHE A 1 280 ? 11.802 11.391 25.092 1.00 29.83 ? 281 PHE A CA 1 ATOM 2218 C C . PHE A 1 280 ? 11.264 12.804 24.890 1.00 31.69 ? 281 PHE A C 1 ATOM 2219 O O . PHE A 1 280 ? 10.593 13.088 23.895 1.00 30.31 ? 281 PHE A O 1 ATOM 2220 C CB . PHE A 1 280 ? 10.847 10.626 26.004 1.00 30.00 ? 281 PHE A CB 1 ATOM 2221 C CG . PHE A 1 280 ? 9.419 10.613 25.528 1.00 29.50 ? 281 PHE A CG 1 ATOM 2222 C CD1 . PHE A 1 280 ? 8.971 9.620 24.664 1.00 29.48 ? 281 PHE A CD1 1 ATOM 2223 C CD2 . PHE A 1 280 ? 8.515 11.572 25.979 1.00 29.89 ? 281 PHE A CD2 1 ATOM 2224 C CE1 . PHE A 1 280 ? 7.636 9.576 24.260 1.00 30.15 ? 281 PHE A CE1 1 ATOM 2225 C CE2 . PHE A 1 280 ? 7.178 11.545 25.584 1.00 30.17 ? 281 PHE A CE2 1 ATOM 2226 C CZ . PHE A 1 280 ? 6.734 10.543 24.723 1.00 30.96 ? 281 PHE A CZ 1 ATOM 2227 N N . LEU A 1 281 ? 11.538 13.678 25.855 1.00 32.08 ? 282 LEU A N 1 ATOM 2228 C CA . LEU A 1 281 ? 11.069 15.060 25.804 1.00 35.48 ? 282 LEU A CA 1 ATOM 2229 C C . LEU A 1 281 ? 11.444 15.807 24.527 1.00 36.92 ? 282 LEU A C 1 ATOM 2230 O O . LEU A 1 281 ? 10.682 16.650 24.055 1.00 36.97 ? 282 LEU A O 1 ATOM 2231 C CB . LEU A 1 281 ? 11.581 15.835 27.025 1.00 35.50 ? 282 LEU A CB 1 ATOM 2232 C CG . LEU A 1 281 ? 10.660 15.899 28.253 1.00 36.79 ? 282 LEU A CG 1 ATOM 2233 C CD1 . LEU A 1 281 ? 9.792 14.654 28.363 1.00 38.69 ? 282 LEU A CD1 1 ATOM 2234 C CD2 . LEU A 1 281 ? 11.517 16.079 29.497 1.00 37.53 ? 282 LEU A CD2 1 ATOM 2235 N N . HIS A 1 282 ? 12.616 15.506 23.977 1.00 38.30 ? 283 HIS A N 1 ATOM 2236 C CA . HIS A 1 282 ? 13.057 16.166 22.755 1.00 40.83 ? 283 HIS A CA 1 ATOM 2237 C C . HIS A 1 282 ? 12.073 15.819 21.644 1.00 39.08 ? 283 HIS A C 1 ATOM 2238 O O . HIS A 1 282 ? 11.977 14.667 21.226 1.00 39.19 ? 283 HIS A O 1 ATOM 2239 C CB . HIS A 1 282 ? 14.475 15.710 22.386 1.00 42.94 ? 283 HIS A CB 1 ATOM 2240 C CG . HIS A 1 282 ? 15.510 16.079 23.406 1.00 47.80 ? 283 HIS A CG 1 ATOM 2241 N ND1 . HIS A 1 282 ? 15.856 17.386 23.676 1.00 49.42 ? 283 HIS A ND1 1 ATOM 2242 C CD2 . HIS A 1 282 ? 16.245 15.315 24.251 1.00 49.09 ? 283 HIS A CD2 1 ATOM 2243 C CE1 . HIS A 1 282 ? 16.756 17.412 24.643 1.00 50.67 ? 283 HIS A CE1 1 ATOM 2244 N NE2 . HIS A 1 282 ? 17.009 16.168 25.010 1.00 50.90 ? 283 HIS A NE2 1 ATOM 2245 N N . GLY A 1 283 ? 11.325 16.821 21.192 1.00 39.99 ? 284 GLY A N 1 ATOM 2246 C CA . GLY A 1 283 ? 10.348 16.607 20.140 1.00 39.73 ? 284 GLY A CA 1 ATOM 2247 C C . GLY A 1 283 ? 8.974 16.328 20.715 1.00 40.23 ? 284 GLY A C 1 ATOM 2248 O O . GLY A 1 283 ? 8.013 16.126 19.976 1.00 39.83 ? 284 GLY A O 1 ATOM 2249 N N . ALA A 1 284 ? 8.877 16.316 22.040 1.00 39.07 ? 285 ALA A N 1 ATOM 2250 C CA . ALA A 1 284 ? 7.603 16.053 22.697 1.00 39.08 ? 285 ALA A CA 1 ATOM 2251 C C . ALA A 1 284 ? 6.864 17.329 23.082 1.00 39.36 ? 285 ALA A C 1 ATOM 2252 O O . ALA A 1 284 ? 7.424 18.426 23.081 1.00 40.19 ? 285 ALA A O 1 ATOM 2253 C CB . ALA A 1 284 ? 7.818 15.192 23.932 1.00 37.09 ? 285 ALA A CB 1 ATOM 2254 N N . THR A 1 285 ? 5.594 17.159 23.416 1.00 39.51 ? 286 THR A N 1 ATOM 2255 C CA . THR A 1 285 ? 4.730 18.254 23.819 1.00 42.39 ? 286 THR A CA 1 ATOM 2256 C C . THR A 1 285 ? 4.534 18.124 25.339 1.00 41.27 ? 286 THR A C 1 ATOM 2257 O O . THR A 1 285 ? 4.007 17.117 25.815 1.00 41.63 ? 286 THR A O 1 ATOM 2258 C CB . THR A 1 285 ? 3.371 18.140 23.084 1.00 42.69 ? 286 THR A CB 1 ATOM 2259 O OG1 . THR A 1 285 ? 3.598 18.057 21.667 1.00 44.56 ? 286 THR A OG1 1 ATOM 2260 C CG2 . THR A 1 285 ? 2.491 19.334 23.397 1.00 43.00 ? 286 THR A CG2 1 ATOM 2261 N N . THR A 1 286 ? 4.980 19.124 26.095 1.00 40.54 ? 287 THR A N 1 ATOM 2262 C CA . THR A 1 286 ? 4.849 19.087 27.554 1.00 42.18 ? 287 THR A CA 1 ATOM 2263 C C . THR A 1 286 ? 3.626 19.815 28.103 1.00 42.54 ? 287 THR A C 1 ATOM 2264 O O . THR A 1 286 ? 3.243 20.871 27.603 1.00 44.12 ? 287 THR A O 1 ATOM 2265 C CB . THR A 1 286 ? 6.089 19.677 28.250 1.00 42.38 ? 287 THR A CB 1 ATOM 2266 O OG1 . THR A 1 286 ? 6.276 21.035 27.830 1.00 44.30 ? 287 THR A OG1 1 ATOM 2267 C CG2 . THR A 1 286 ? 7.325 18.853 27.924 1.00 42.88 ? 287 THR A CG2 1 ATOM 2268 N N . HIS A 1 287 ? 3.027 19.242 29.144 1.00 42.23 ? 288 HIS A N 1 ATOM 2269 C CA . HIS A 1 287 ? 1.847 19.810 29.792 1.00 43.06 ? 288 HIS A CA 1 ATOM 2270 C C . HIS A 1 287 ? 1.993 19.635 31.301 1.00 42.40 ? 288 HIS A C 1 ATOM 2271 O O . HIS A 1 287 ? 2.887 18.926 31.767 1.00 40.86 ? 288 HIS A O 1 ATOM 2272 C CB . HIS A 1 287 ? 0.585 19.074 29.345 1.00 45.83 ? 288 HIS A CB 1 ATOM 2273 C CG . HIS A 1 287 ? 0.469 18.905 27.863 1.00 49.97 ? 288 HIS A CG 1 ATOM 2274 N ND1 . HIS A 1 287 ? 0.097 19.931 27.022 1.00 52.95 ? 288 HIS A ND1 1 ATOM 2275 C CD2 . HIS A 1 287 ? 0.665 17.822 27.073 1.00 52.26 ? 288 HIS A CD2 1 ATOM 2276 C CE1 . HIS A 1 287 ? 0.064 19.487 25.778 1.00 53.92 ? 288 HIS A CE1 1 ATOM 2277 N NE2 . HIS A 1 287 ? 0.404 18.210 25.782 1.00 53.56 ? 288 HIS A NE2 1 ATOM 2278 N N . ARG A 1 288 ? 1.107 20.271 32.059 1.00 41.84 ? 289 ARG A N 1 ATOM 2279 C CA . ARG A 1 288 ? 1.142 20.158 33.511 1.00 42.89 ? 289 ARG A CA 1 ATOM 2280 C C . ARG A 1 288 ? -0.239 20.363 34.116 1.00 43.13 ? 289 ARG A C 1 ATOM 2281 O O . ARG A 1 288 ? -0.892 21.379 33.865 1.00 43.95 ? 289 ARG A O 1 ATOM 2282 C CB . ARG A 1 288 ? 2.124 21.176 34.105 1.00 42.15 ? 289 ARG A CB 1 ATOM 2283 C CG . ARG A 1 288 ? 2.420 20.960 35.586 1.00 46.02 ? 289 ARG A CG 1 ATOM 2284 C CD . ARG A 1 288 ? 3.440 21.971 36.108 1.00 48.41 ? 289 ARG A CD 1 ATOM 2285 N NE . ARG A 1 288 ? 4.740 21.823 35.460 1.00 48.15 ? 289 ARG A NE 1 ATOM 2286 C CZ . ARG A 1 288 ? 5.715 21.027 35.894 1.00 47.39 ? 289 ARG A CZ 1 ATOM 2287 N NH1 . ARG A 1 288 ? 5.553 20.301 36.992 1.00 44.85 ? 289 ARG A NH1 1 ATOM 2288 N NH2 . ARG A 1 288 ? 6.850 20.945 35.213 1.00 46.61 ? 289 ARG A NH2 1 ATOM 2289 N N . PHE A 1 289 ? -0.693 19.386 34.895 1.00 42.01 ? 290 PHE A N 1 ATOM 2290 C CA . PHE A 1 289 ? -1.986 19.492 35.559 1.00 42.25 ? 290 PHE A CA 1 ATOM 2291 C C . PHE A 1 289 ? -1.793 20.540 36.641 1.00 42.42 ? 290 PHE A C 1 ATOM 2292 O O . PHE A 1 289 ? -1.027 20.324 37.580 1.00 41.47 ? 290 PHE A O 1 ATOM 2293 C CB . PHE A 1 289 ? -2.370 18.169 36.214 1.00 41.56 ? 290 PHE A CB 1 ATOM 2294 C CG . PHE A 1 289 ? -2.589 17.049 35.244 1.00 43.32 ? 290 PHE A CG 1 ATOM 2295 C CD1 . PHE A 1 289 ? -3.586 17.136 34.274 1.00 45.35 ? 290 PHE A CD1 1 ATOM 2296 C CD2 . PHE A 1 289 ? -1.808 15.898 35.307 1.00 42.63 ? 290 PHE A CD2 1 ATOM 2297 C CE1 . PHE A 1 289 ? -3.807 16.090 33.382 1.00 44.99 ? 290 PHE A CE1 1 ATOM 2298 C CE2 . PHE A 1 289 ? -2.017 14.845 34.423 1.00 43.14 ? 290 PHE A CE2 1 ATOM 2299 C CZ . PHE A 1 289 ? -3.018 14.939 33.455 1.00 44.45 ? 290 PHE A CZ 1 ATOM 2300 N N . ARG A 1 290 ? -2.475 21.672 36.518 1.00 42.98 ? 291 ARG A N 1 ATOM 2301 C CA . ARG A 1 290 ? -2.323 22.725 37.508 1.00 45.24 ? 291 ARG A CA 1 ATOM 2302 C C . ARG A 1 290 ? -2.897 22.289 38.852 1.00 44.02 ? 291 ARG A C 1 ATOM 2303 O O . ARG A 1 290 ? -2.322 22.572 39.900 1.00 43.78 ? 291 ARG A O 1 ATOM 2304 C CB . ARG A 1 290 ? -2.999 24.016 37.033 1.00 47.58 ? 291 ARG A CB 1 ATOM 2305 C CG . ARG A 1 290 ? -4.481 24.132 37.356 1.00 53.20 ? 291 ARG A CG 1 ATOM 2306 C CD . ARG A 1 290 ? -4.985 25.536 37.049 1.00 59.05 ? 291 ARG A CD 1 ATOM 2307 N NE . ARG A 1 290 ? -3.998 26.548 37.425 1.00 64.12 ? 291 ARG A NE 1 ATOM 2308 C CZ . ARG A 1 290 ? -4.275 27.833 37.627 1.00 67.03 ? 291 ARG A CZ 1 ATOM 2309 N NH1 . ARG A 1 290 ? -5.520 28.277 37.496 1.00 67.73 ? 291 ARG A NH1 1 ATOM 2310 N NH2 . ARG A 1 290 ? -3.304 28.676 37.957 1.00 68.68 ? 291 ARG A NH2 1 ATOM 2311 N N . ASP A 1 291 ? -4.029 21.594 38.820 1.00 43.16 ? 292 ASP A N 1 ATOM 2312 C CA . ASP A 1 291 ? -4.652 21.128 40.053 1.00 42.94 ? 292 ASP A CA 1 ATOM 2313 C C . ASP A 1 291 ? -3.790 20.086 40.782 1.00 41.53 ? 292 ASP A C 1 ATOM 2314 O O . ASP A 1 291 ? -3.492 20.236 41.968 1.00 40.37 ? 292 ASP A O 1 ATOM 2315 C CB . ASP A 1 291 ? -6.034 20.528 39.766 1.00 46.22 ? 292 ASP A CB 1 ATOM 2316 C CG . ASP A 1 291 ? -7.120 21.581 39.643 1.00 49.54 ? 292 ASP A CG 1 ATOM 2317 O OD1 . ASP A 1 291 ? -6.889 22.730 40.083 1.00 49.81 ? 292 ASP A OD1 1 ATOM 2318 O OD2 . ASP A 1 291 ? -8.213 21.252 39.123 1.00 52.14 ? 292 ASP A OD2 1 ATOM 2319 N N . GLN A 1 292 ? -3.386 19.040 40.066 1.00 39.12 ? 293 GLN A N 1 ATOM 2320 C CA . GLN A 1 292 ? -2.587 17.963 40.648 1.00 38.34 ? 293 GLN A CA 1 ATOM 2321 C C . GLN A 1 292 ? -1.103 18.285 40.850 1.00 35.73 ? 293 GLN A C 1 ATOM 2322 O O . GLN A 1 292 ? -0.421 17.628 41.641 1.00 35.45 ? 293 GLN A O 1 ATOM 2323 C CB . GLN A 1 292 ? -2.755 16.703 39.799 1.00 39.51 ? 293 GLN A CB 1 ATOM 2324 C CG . GLN A 1 292 ? -4.181 16.177 39.832 1.00 45.41 ? 293 GLN A CG 1 ATOM 2325 C CD . GLN A 1 292 ? -4.515 15.280 38.657 1.00 50.01 ? 293 GLN A CD 1 ATOM 2326 O OE1 . GLN A 1 292 ? -4.070 14.133 38.576 1.00 53.17 ? 293 GLN A OE1 1 ATOM 2327 N NE2 . GLN A 1 292 ? -5.305 15.807 37.729 1.00 53.54 ? 293 GLN A NE2 1 ATOM 2328 N N . GLN A 1 293 ? -0.620 19.296 40.133 1.00 32.51 ? 294 GLN A N 1 ATOM 2329 C CA . GLN A 1 293 ? 0.766 19.759 40.216 1.00 31.90 ? 294 GLN A CA 1 ATOM 2330 C C . GLN A 1 293 ? 1.833 18.769 39.750 1.00 29.89 ? 294 GLN A C 1 ATOM 2331 O O . GLN A 1 293 ? 2.900 18.647 40.358 1.00 28.37 ? 294 GLN A O 1 ATOM 2332 C CB . GLN A 1 293 ? 1.074 20.229 41.640 1.00 32.96 ? 294 GLN A CB 1 ATOM 2333 C CG . GLN A 1 293 ? 0.030 21.200 42.177 1.00 38.64 ? 294 GLN A CG 1 ATOM 2334 C CD . GLN A 1 293 ? 0.586 22.142 43.220 1.00 40.01 ? 294 GLN A CD 1 ATOM 2335 O OE1 . GLN A 1 293 ? 0.700 23.342 42.986 1.00 47.91 ? 294 GLN A OE1 1 ATOM 2336 N NE2 . GLN A 1 293 ? 0.944 21.603 44.375 1.00 41.84 ? 294 GLN A NE2 1 ATOM 2337 N N . VAL A 1 294 ? 1.541 18.077 38.657 1.00 27.44 ? 295 VAL A N 1 ATOM 2338 C CA . VAL A 1 294 ? 2.466 17.119 38.080 1.00 25.06 ? 295 VAL A CA 1 ATOM 2339 C C . VAL A 1 294 ? 2.384 17.229 36.559 1.00 26.46 ? 295 VAL A C 1 ATOM 2340 O O . VAL A 1 294 ? 1.322 17.533 36.005 1.00 25.32 ? 295 VAL A O 1 ATOM 2341 C CB . VAL A 1 294 ? 2.134 15.689 38.527 1.00 24.67 ? 295 VAL A CB 1 ATOM 2342 C CG1 . VAL A 1 294 ? 2.591 15.472 39.973 1.00 21.89 ? 295 VAL A CG1 1 ATOM 2343 C CG2 . VAL A 1 294 ? 0.638 15.441 38.408 1.00 22.21 ? 295 VAL A CG2 1 ATOM 2344 N N . PRO A 1 295 ? 3.503 16.979 35.863 1.00 24.94 ? 296 PRO A N 1 ATOM 2345 C CA . PRO A 1 295 ? 3.503 17.076 34.403 1.00 25.36 ? 296 PRO A CA 1 ATOM 2346 C C . PRO A 1 295 ? 3.271 15.780 33.647 1.00 25.61 ? 296 PRO A C 1 ATOM 2347 O O . PRO A 1 295 ? 3.248 14.692 34.222 1.00 22.18 ? 296 PRO A O 1 ATOM 2348 C CB . PRO A 1 295 ? 4.885 17.628 34.116 1.00 24.08 ? 296 PRO A CB 1 ATOM 2349 C CG . PRO A 1 295 ? 5.729 16.826 35.099 1.00 25.96 ? 296 PRO A CG 1 ATOM 2350 C CD . PRO A 1 295 ? 4.882 16.842 36.379 1.00 24.71 ? 296 PRO A CD 1 ATOM 2351 N N . TYR A 1 296 ? 3.083 15.920 32.340 1.00 27.05 ? 297 TYR A N 1 ATOM 2352 C CA . TYR A 1 296 ? 2.928 14.778 31.451 1.00 29.30 ? 297 TYR A CA 1 ATOM 2353 C C . TYR A 1 296 ? 3.370 15.256 30.073 1.00 28.45 ? 297 TYR A C 1 ATOM 2354 O O . TYR A 1 296 ? 3.431 16.459 29.817 1.00 26.77 ? 297 TYR A O 1 ATOM 2355 C CB . TYR A 1 296 ? 1.489 14.245 31.429 1.00 31.70 ? 297 TYR A CB 1 ATOM 2356 C CG . TYR A 1 296 ? 0.450 15.152 30.825 1.00 36.71 ? 297 TYR A CG 1 ATOM 2357 C CD1 . TYR A 1 296 ? -0.207 16.112 31.597 1.00 38.72 ? 297 TYR A CD1 1 ATOM 2358 C CD2 . TYR A 1 296 ? 0.072 15.004 29.494 1.00 39.05 ? 297 TYR A CD2 1 ATOM 2359 C CE1 . TYR A 1 296 ? -1.222 16.894 31.056 1.00 41.69 ? 297 TYR A CE1 1 ATOM 2360 C CE2 . TYR A 1 296 ? -0.938 15.775 28.942 1.00 41.90 ? 297 TYR A CE2 1 ATOM 2361 C CZ . TYR A 1 296 ? -1.581 16.717 29.726 1.00 43.16 ? 297 TYR A CZ 1 ATOM 2362 O OH . TYR A 1 296 ? -2.583 17.485 29.184 1.00 47.43 ? 297 TYR A OH 1 ATOM 2363 N N . ALA A 1 297 ? 3.720 14.322 29.201 1.00 27.70 ? 298 ALA A N 1 ATOM 2364 C CA . ALA A 1 297 ? 4.182 14.692 27.875 1.00 29.61 ? 298 ALA A CA 1 ATOM 2365 C C . ALA A 1 297 ? 3.640 13.740 26.830 1.00 30.27 ? 298 ALA A C 1 ATOM 2366 O O . ALA A 1 297 ? 3.253 12.612 27.139 1.00 30.05 ? 298 ALA A O 1 ATOM 2367 C CB . ALA A 1 297 ? 5.711 14.703 27.841 1.00 28.27 ? 298 ALA A CB 1 ATOM 2368 N N . THR A 1 298 ? 3.613 14.207 25.586 1.00 31.99 ? 299 THR A N 1 ATOM 2369 C CA . THR A 1 298 ? 3.114 13.397 24.488 1.00 33.24 ? 299 THR A CA 1 ATOM 2370 C C . THR A 1 298 ? 3.953 13.605 23.233 1.00 31.54 ? 299 THR A C 1 ATOM 2371 O O . THR A 1 298 ? 4.437 14.699 22.959 1.00 29.36 ? 299 THR A O 1 ATOM 2372 C CB . THR A 1 298 ? 1.652 13.739 24.160 1.00 34.11 ? 299 THR A CB 1 ATOM 2373 O OG1 . THR A 1 298 ? 0.976 14.144 25.357 1.00 40.58 ? 299 THR A OG1 1 ATOM 2374 C CG2 . THR A 1 298 ? 0.946 12.518 23.583 1.00 33.05 ? 299 THR A CG2 1 ATOM 2375 N N . LYS A 1 299 ? 4.117 12.525 22.485 1.00 32.93 ? 300 LYS A N 1 ATOM 2376 C CA . LYS A 1 299 ? 4.886 12.518 21.248 1.00 34.16 ? 300 LYS A CA 1 ATOM 2377 C C . LYS A 1 299 ? 4.251 11.398 20.441 1.00 32.92 ? 300 LYS A C 1 ATOM 2378 O O . LYS A 1 299 ? 4.172 10.265 20.918 1.00 31.14 ? 300 LYS A O 1 ATOM 2379 C CB . LYS A 1 299 ? 6.355 12.191 21.551 1.00 34.36 ? 300 LYS A CB 1 ATOM 2380 C CG . LYS A 1 299 ? 7.231 12.021 20.333 1.00 36.74 ? 300 LYS A CG 1 ATOM 2381 C CD . LYS A 1 299 ? 8.570 11.378 20.687 1.00 38.92 ? 300 LYS A CD 1 ATOM 2382 C CE . LYS A 1 299 ? 9.540 12.368 21.298 1.00 38.57 ? 300 LYS A CE 1 ATOM 2383 N NZ . LYS A 1 299 ? 10.880 11.740 21.500 1.00 34.72 ? 300 LYS A NZ 1 ATOM 2384 N N . GLY A 1 300 ? 3.784 11.709 19.233 1.00 33.09 ? 301 GLY A N 1 ATOM 2385 C CA . GLY A 1 300 ? 3.141 10.693 18.418 1.00 32.33 ? 301 GLY A CA 1 ATOM 2386 C C . GLY A 1 300 ? 1.930 10.156 19.156 1.00 32.75 ? 301 GLY A C 1 ATOM 2387 O O . GLY A 1 300 ? 1.059 10.927 19.562 1.00 34.27 ? 301 GLY A O 1 ATOM 2388 N N . ASN A 1 301 ? 1.873 8.842 19.349 1.00 33.13 ? 302 ASN A N 1 ATOM 2389 C CA . ASN A 1 301 ? 0.751 8.236 20.057 1.00 34.26 ? 302 ASN A CA 1 ATOM 2390 C C . ASN A 1 301 ? 1.177 7.750 21.442 1.00 33.82 ? 302 ASN A C 1 ATOM 2391 O O . ASN A 1 301 ? 0.535 6.883 22.030 1.00 34.60 ? 302 ASN A O 1 ATOM 2392 C CB . ASN A 1 301 ? 0.183 7.064 19.253 1.00 34.28 ? 302 ASN A CB 1 ATOM 2393 C CG . ASN A 1 301 ? 1.132 5.893 19.189 1.00 36.55 ? 302 ASN A CG 1 ATOM 2394 O OD1 . ASN A 1 301 ? 2.267 5.982 19.645 1.00 38.77 ? 302 ASN A OD1 1 ATOM 2395 N ND2 . ASN A 1 301 ? 0.674 4.783 18.619 1.00 39.21 ? 302 ASN A ND2 1 ATOM 2396 N N . GLN A 1 302 ? 2.273 8.306 21.951 1.00 32.91 ? 303 GLN A N 1 ATOM 2397 C CA . GLN A 1 302 ? 2.780 7.931 23.268 1.00 32.31 ? 303 GLN A CA 1 ATOM 2398 C C . GLN A 1 302 ? 2.495 9.037 24.279 1.00 31.25 ? 303 GLN A C 1 ATOM 2399 O O . GLN A 1 302 ? 2.813 10.206 24.043 1.00 30.63 ? 303 GLN A O 1 ATOM 2400 C CB . GLN A 1 302 ? 4.291 7.669 23.211 1.00 30.63 ? 303 GLN A CB 1 ATOM 2401 C CG . GLN A 1 302 ? 4.695 6.489 22.344 1.00 33.05 ? 303 GLN A CG 1 ATOM 2402 C CD . GLN A 1 302 ? 4.081 5.183 22.809 1.00 34.67 ? 303 GLN A CD 1 ATOM 2403 O OE1 . GLN A 1 302 ? 3.230 4.604 22.129 1.00 36.42 ? 303 GLN A OE1 1 ATOM 2404 N NE2 . GLN A 1 302 ? 4.508 4.712 23.977 1.00 30.29 ? 303 GLN A NE2 1 ATOM 2405 N N . TRP A 1 303 ? 1.904 8.655 25.408 1.00 29.59 ? 304 TRP A N 1 ATOM 2406 C CA . TRP A 1 303 ? 1.552 9.600 26.465 1.00 30.47 ? 304 TRP A CA 1 ATOM 2407 C C . TRP A 1 303 ? 2.315 9.197 27.730 1.00 28.59 ? 304 TRP A C 1 ATOM 2408 O O . TRP A 1 303 ? 2.254 8.046 28.158 1.00 29.01 ? 304 TRP A O 1 ATOM 2409 C CB . TRP A 1 303 ? 0.043 9.544 26.722 1.00 30.54 ? 304 TRP A CB 1 ATOM 2410 C CG . TRP A 1 303 ? -0.510 10.710 27.500 1.00 33.59 ? 304 TRP A CG 1 ATOM 2411 C CD1 . TRP A 1 303 ? -1.006 11.884 26.991 1.00 34.73 ? 304 TRP A CD1 1 ATOM 2412 C CD2 . TRP A 1 303 ? -0.656 10.797 28.923 1.00 33.86 ? 304 TRP A CD2 1 ATOM 2413 N NE1 . TRP A 1 303 ? -1.458 12.690 28.015 1.00 34.45 ? 304 TRP A NE1 1 ATOM 2414 C CE2 . TRP A 1 303 ? -1.254 12.048 29.210 1.00 34.83 ? 304 TRP A CE2 1 ATOM 2415 C CE3 . TRP A 1 303 ? -0.340 9.941 29.986 1.00 35.81 ? 304 TRP A CE3 1 ATOM 2416 C CZ2 . TRP A 1 303 ? -1.544 12.458 30.523 1.00 34.22 ? 304 TRP A CZ2 1 ATOM 2417 C CZ3 . TRP A 1 303 ? -0.629 10.349 31.288 1.00 35.39 ? 304 TRP A CZ3 1 ATOM 2418 C CH2 . TRP A 1 303 ? -1.224 11.596 31.543 1.00 33.63 ? 304 TRP A CH2 1 ATOM 2419 N N . VAL A 1 304 ? 3.025 10.146 28.331 1.00 26.79 ? 305 VAL A N 1 ATOM 2420 C CA . VAL A 1 304 ? 3.816 9.845 29.518 1.00 27.04 ? 305 VAL A CA 1 ATOM 2421 C C . VAL A 1 304 ? 3.534 10.748 30.720 1.00 26.73 ? 305 VAL A C 1 ATOM 2422 O O . VAL A 1 304 ? 3.570 11.973 30.607 1.00 24.96 ? 305 VAL A O 1 ATOM 2423 C CB . VAL A 1 304 ? 5.331 9.928 29.195 1.00 27.91 ? 305 VAL A CB 1 ATOM 2424 C CG1 . VAL A 1 304 ? 6.155 9.630 30.442 1.00 29.11 ? 305 VAL A CG1 1 ATOM 2425 C CG2 . VAL A 1 304 ? 5.681 8.941 28.083 1.00 27.26 ? 305 VAL A CG2 1 ATOM 2426 N N . ALA A 1 305 ? 3.259 10.128 31.867 1.00 23.86 ? 306 ALA A N 1 ATOM 2427 C CA . ALA A 1 305 ? 3.015 10.853 33.117 1.00 25.43 ? 306 ALA A CA 1 ATOM 2428 C C . ALA A 1 305 ? 4.300 10.696 33.919 1.00 23.79 ? 306 ALA A C 1 ATOM 2429 O O . ALA A 1 305 ? 4.747 9.575 34.161 1.00 21.96 ? 306 ALA A O 1 ATOM 2430 C CB . ALA A 1 305 ? 1.844 10.231 33.880 1.00 22.14 ? 306 ALA A CB 1 ATOM 2431 N N . TYR A 1 306 ? 4.902 11.809 34.317 1.00 22.43 ? 307 TYR A N 1 ATOM 2432 C CA . TYR A 1 306 ? 6.151 11.747 35.069 1.00 23.36 ? 307 TYR A CA 1 ATOM 2433 C C . TYR A 1 306 ? 6.287 12.856 36.107 1.00 23.21 ? 307 TYR A C 1 ATOM 2434 O O . TYR A 1 306 ? 5.370 13.648 36.318 1.00 21.08 ? 307 TYR A O 1 ATOM 2435 C CB . TYR A 1 306 ? 7.344 11.828 34.106 1.00 21.70 ? 307 TYR A CB 1 ATOM 2436 C CG . TYR A 1 306 ? 7.470 13.167 33.396 1.00 22.49 ? 307 TYR A CG 1 ATOM 2437 C CD1 . TYR A 1 306 ? 6.541 13.563 32.428 1.00 23.45 ? 307 TYR A CD1 1 ATOM 2438 C CD2 . TYR A 1 306 ? 8.504 14.049 33.713 1.00 22.71 ? 307 TYR A CD2 1 ATOM 2439 C CE1 . TYR A 1 306 ? 6.641 14.808 31.792 1.00 20.37 ? 307 TYR A CE1 1 ATOM 2440 C CE2 . TYR A 1 306 ? 8.612 15.293 33.089 1.00 22.04 ? 307 TYR A CE2 1 ATOM 2441 C CZ . TYR A 1 306 ? 7.677 15.665 32.130 1.00 24.11 ? 307 TYR A CZ 1 ATOM 2442 O OH . TYR A 1 306 ? 7.783 16.898 31.524 1.00 25.97 ? 307 TYR A OH 1 ATOM 2443 N N . ASP A 1 307 ? 7.448 12.889 36.754 1.00 23.24 ? 308 ASP A N 1 ATOM 2444 C CA . ASP A 1 307 ? 7.770 13.897 37.755 1.00 23.64 ? 308 ASP A CA 1 ATOM 2445 C C . ASP A 1 307 ? 9.080 14.558 37.335 1.00 25.40 ? 308 ASP A C 1 ATOM 2446 O O . ASP A 1 307 ? 10.011 13.877 36.898 1.00 22.24 ? 308 ASP A O 1 ATOM 2447 C CB . ASP A 1 307 ? 7.971 13.266 39.143 1.00 21.14 ? 308 ASP A CB 1 ATOM 2448 C CG . ASP A 1 307 ? 6.679 13.112 39.911 1.00 24.36 ? 308 ASP A CG 1 ATOM 2449 O OD1 . ASP A 1 307 ? 6.046 12.037 39.821 1.00 22.70 ? 308 ASP A OD1 1 ATOM 2450 O OD2 . ASP A 1 307 ? 6.297 14.085 40.600 1.00 25.40 ? 308 ASP A OD2 1 ATOM 2451 N N . ASP A 1 308 ? 9.155 15.878 37.454 1.00 24.22 ? 309 ASP A N 1 ATOM 2452 C CA . ASP A 1 308 ? 10.389 16.572 37.109 1.00 25.60 ? 309 ASP A CA 1 ATOM 2453 C C . ASP A 1 308 ? 10.912 17.290 38.348 1.00 24.91 ? 309 ASP A C 1 ATOM 2454 O O . ASP A 1 308 ? 10.315 17.184 39.419 1.00 21.02 ? 309 ASP A O 1 ATOM 2455 C CB . ASP A 1 308 ? 10.169 17.556 35.946 1.00 26.56 ? 309 ASP A CB 1 ATOM 2456 C CG . ASP A 1 308 ? 9.020 18.512 36.184 1.00 29.42 ? 309 ASP A CG 1 ATOM 2457 O OD1 . ASP A 1 308 ? 8.589 18.680 37.352 1.00 27.20 ? 309 ASP A OD1 1 ATOM 2458 O OD2 . ASP A 1 308 ? 8.555 19.106 35.186 1.00 30.05 ? 309 ASP A OD2 1 ATOM 2459 N N . GLN A 1 309 ? 12.022 18.010 38.216 1.00 24.32 ? 310 GLN A N 1 ATOM 2460 C CA . GLN A 1 309 ? 12.598 18.704 39.367 1.00 28.25 ? 310 GLN A CA 1 ATOM 2461 C C . GLN A 1 309 ? 11.574 19.562 40.089 1.00 27.48 ? 310 GLN A C 1 ATOM 2462 O O . GLN A 1 309 ? 11.529 19.613 41.320 1.00 24.58 ? 310 GLN A O 1 ATOM 2463 C CB . GLN A 1 309 ? 13.761 19.604 38.945 1.00 29.74 ? 310 GLN A CB 1 ATOM 2464 C CG . GLN A 1 309 ? 15.003 18.881 38.488 1.00 39.57 ? 310 GLN A CG 1 ATOM 2465 C CD . GLN A 1 309 ? 16.248 19.710 38.741 1.00 46.82 ? 310 GLN A CD 1 ATOM 2466 O OE1 . GLN A 1 309 ? 16.253 20.924 38.523 1.00 51.87 ? 310 GLN A OE1 1 ATOM 2467 N NE2 . GLN A 1 309 ? 17.311 19.061 39.208 1.00 48.91 ? 310 GLN A NE2 1 ATOM 2468 N N . GLU A 1 310 ? 10.760 20.250 39.304 1.00 26.74 ? 311 GLU A N 1 ATOM 2469 C CA . GLU A 1 310 ? 9.733 21.127 39.837 1.00 29.39 ? 311 GLU A CA 1 ATOM 2470 C C . GLU A 1 310 ? 8.674 20.418 40.682 1.00 26.76 ? 311 GLU A C 1 ATOM 2471 O O . GLU A 1 310 ? 8.403 20.826 41.810 1.00 26.26 ? 311 GLU A O 1 ATOM 2472 C CB . GLU A 1 310 ? 9.057 21.852 38.681 1.00 32.81 ? 311 GLU A CB 1 ATOM 2473 C CG . GLU A 1 310 ? 7.738 22.460 39.044 1.00 40.86 ? 311 GLU A CG 1 ATOM 2474 C CD . GLU A 1 310 ? 7.830 23.948 39.227 1.00 48.80 ? 311 GLU A CD 1 ATOM 2475 O OE1 . GLU A 1 310 ? 8.735 24.407 39.961 1.00 52.26 ? 311 GLU A OE1 1 ATOM 2476 O OE2 . GLU A 1 310 ? 6.994 24.661 38.631 1.00 52.64 ? 311 GLU A OE2 1 ATOM 2477 N N . SER A 1 311 ? 8.066 19.368 40.140 1.00 23.06 ? 312 SER A N 1 ATOM 2478 C CA . SER A 1 311 ? 7.026 18.666 40.875 1.00 24.14 ? 312 SER A CA 1 ATOM 2479 C C . SER A 1 311 ? 7.592 17.959 42.099 1.00 24.58 ? 312 SER A C 1 ATOM 2480 O O . SER A 1 311 ? 6.945 17.872 43.142 1.00 24.39 ? 312 SER A O 1 ATOM 2481 C CB . SER A 1 311 ? 6.302 17.664 39.971 1.00 23.34 ? 312 SER A CB 1 ATOM 2482 O OG . SER A 1 311 ? 7.150 16.619 39.554 1.00 23.87 ? 312 SER A OG 1 ATOM 2483 N N . VAL A 1 312 ? 8.810 17.455 41.966 1.00 22.59 ? 313 VAL A N 1 ATOM 2484 C CA . VAL A 1 312 ? 9.474 16.772 43.064 1.00 23.13 ? 313 VAL A CA 1 ATOM 2485 C C . VAL A 1 312 ? 9.776 17.758 44.205 1.00 22.62 ? 313 VAL A C 1 ATOM 2486 O O . VAL A 1 312 ? 9.608 17.434 45.383 1.00 20.98 ? 313 VAL A O 1 ATOM 2487 C CB . VAL A 1 312 ? 10.764 16.094 42.536 1.00 25.91 ? 313 VAL A CB 1 ATOM 2488 C CG1 . VAL A 1 312 ? 11.818 16.069 43.592 1.00 28.40 ? 313 VAL A CG1 1 ATOM 2489 C CG2 . VAL A 1 312 ? 10.436 14.678 42.050 1.00 21.61 ? 313 VAL A CG2 1 ATOM 2490 N N . LYS A 1 313 ? 10.214 18.967 43.862 1.00 21.83 ? 314 LYS A N 1 ATOM 2491 C CA . LYS A 1 313 ? 10.500 19.966 44.888 1.00 24.63 ? 314 LYS A CA 1 ATOM 2492 C C . LYS A 1 313 ? 9.194 20.365 45.555 1.00 24.37 ? 314 LYS A C 1 ATOM 2493 O O . LYS A 1 313 ? 9.142 20.698 46.738 1.00 22.40 ? 314 LYS A O 1 ATOM 2494 C CB . LYS A 1 313 ? 11.137 21.205 44.266 1.00 26.65 ? 314 LYS A CB 1 ATOM 2495 C CG . LYS A 1 313 ? 12.598 21.058 43.877 1.00 30.07 ? 314 LYS A CG 1 ATOM 2496 C CD . LYS A 1 313 ? 13.131 22.413 43.425 1.00 35.32 ? 314 LYS A CD 1 ATOM 2497 C CE . LYS A 1 313 ? 14.588 22.597 43.798 1.00 40.85 ? 314 LYS A CE 1 ATOM 2498 N NZ . LYS A 1 313 ? 14.968 24.041 43.761 1.00 46.67 ? 314 LYS A NZ 1 ATOM 2499 N N . ASN A 1 314 ? 8.131 20.316 44.770 1.00 24.39 ? 315 ASN A N 1 ATOM 2500 C CA . ASN A 1 314 ? 6.807 20.677 45.244 1.00 25.52 ? 315 ASN A CA 1 ATOM 2501 C C . ASN A 1 314 ? 6.312 19.678 46.288 1.00 22.23 ? 315 ASN A C 1 ATOM 2502 O O . ASN A 1 314 ? 5.736 20.057 47.304 1.00 21.27 ? 315 ASN A O 1 ATOM 2503 C CB . ASN A 1 314 ? 5.852 20.714 44.056 1.00 27.09 ? 315 ASN A CB 1 ATOM 2504 C CG . ASN A 1 314 ? 4.649 21.565 44.314 1.00 33.37 ? 315 ASN A CG 1 ATOM 2505 O OD1 . ASN A 1 314 ? 3.532 21.064 44.439 1.00 39.83 ? 315 ASN A OD1 1 ATOM 2506 N ND2 . ASN A 1 314 ? 4.866 22.871 44.403 1.00 36.74 ? 315 ASN A ND2 1 ATOM 2507 N N . LYS A 1 315 ? 6.532 18.397 46.023 1.00 21.10 ? 316 LYS A N 1 ATOM 2508 C CA . LYS A 1 315 ? 6.121 17.354 46.949 1.00 20.51 ? 316 LYS A CA 1 ATOM 2509 C C . LYS A 1 315 ? 6.951 17.425 48.227 1.00 19.74 ? 316 LYS A C 1 ATOM 2510 O O . LYS A 1 315 ? 6.434 17.203 49.327 1.00 19.96 ? 316 LYS A O 1 ATOM 2511 C CB . LYS A 1 315 ? 6.269 15.987 46.279 1.00 20.66 ? 316 LYS A CB 1 ATOM 2512 C CG . LYS A 1 315 ? 5.293 15.806 45.126 1.00 20.74 ? 316 LYS A CG 1 ATOM 2513 C CD . LYS A 1 315 ? 5.507 14.523 44.350 1.00 21.19 ? 316 LYS A CD 1 ATOM 2514 C CE . LYS A 1 315 ? 4.371 14.325 43.342 1.00 22.95 ? 316 LYS A CE 1 ATOM 2515 N NZ . LYS A 1 315 ? 4.556 13.097 42.529 1.00 19.94 ? 316 LYS A NZ 1 ATOM 2516 N N . ALA A 1 316 ? 8.233 17.746 48.080 1.00 18.49 ? 317 ALA A N 1 ATOM 2517 C CA . ALA A 1 316 ? 9.130 17.856 49.230 1.00 20.23 ? 317 ALA A CA 1 ATOM 2518 C C . ALA A 1 316 ? 8.706 18.985 50.183 1.00 21.35 ? 317 ALA A C 1 ATOM 2519 O O . ALA A 1 316 ? 8.849 18.860 51.399 1.00 21.42 ? 317 ALA A O 1 ATOM 2520 C CB . ALA A 1 316 ? 10.573 18.077 48.756 1.00 17.71 ? 317 ALA A CB 1 ATOM 2521 N N . ARG A 1 317 ? 8.201 20.089 49.637 1.00 21.91 ? 318 ARG A N 1 ATOM 2522 C CA . ARG A 1 317 ? 7.754 21.200 50.479 1.00 24.26 ? 318 ARG A CA 1 ATOM 2523 C C . ARG A 1 317 ? 6.464 20.815 51.192 1.00 22.79 ? 318 ARG A C 1 ATOM 2524 O O . ARG A 1 317 ? 6.251 21.156 52.355 1.00 21.05 ? 318 ARG A O 1 ATOM 2525 C CB . ARG A 1 317 ? 7.503 22.459 49.647 1.00 25.65 ? 318 ARG A CB 1 ATOM 2526 C CG . ARG A 1 317 ? 8.738 23.044 49.006 1.00 33.57 ? 318 ARG A CG 1 ATOM 2527 C CD . ARG A 1 317 ? 8.431 24.393 48.384 1.00 39.46 ? 318 ARG A CD 1 ATOM 2528 N NE . ARG A 1 317 ? 9.226 24.613 47.182 1.00 44.84 ? 318 ARG A NE 1 ATOM 2529 C CZ . ARG A 1 317 ? 8.738 24.544 45.948 1.00 46.88 ? 318 ARG A CZ 1 ATOM 2530 N NH1 . ARG A 1 317 ? 7.454 24.267 45.748 1.00 47.57 ? 318 ARG A NH1 1 ATOM 2531 N NH2 . ARG A 1 317 ? 9.539 24.744 44.911 1.00 48.99 ? 318 ARG A NH2 1 ATOM 2532 N N . TYR A 1 318 ? 5.595 20.105 50.484 1.00 22.49 ? 319 TYR A N 1 ATOM 2533 C CA . TYR A 1 318 ? 4.333 19.664 51.064 1.00 20.72 ? 319 TYR A CA 1 ATOM 2534 C C . TYR A 1 318 ? 4.630 18.797 52.287 1.00 21.80 ? 319 TYR A C 1 ATOM 2535 O O . TYR A 1 318 ? 4.071 18.979 53.370 1.00 18.79 ? 319 TYR A O 1 ATOM 2536 C CB . TYR A 1 318 ? 3.555 18.851 50.029 1.00 21.04 ? 319 TYR A CB 1 ATOM 2537 C CG . TYR A 1 318 ? 2.353 18.144 50.598 1.00 24.35 ? 319 TYR A CG 1 ATOM 2538 C CD1 . TYR A 1 318 ? 1.129 18.799 50.731 1.00 25.73 ? 319 TYR A CD1 1 ATOM 2539 C CD2 . TYR A 1 318 ? 2.452 16.826 51.054 1.00 22.70 ? 319 TYR A CD2 1 ATOM 2540 C CE1 . TYR A 1 318 ? 0.027 18.154 51.311 1.00 25.05 ? 319 TYR A CE1 1 ATOM 2541 C CE2 . TYR A 1 318 ? 1.368 16.178 51.631 1.00 24.91 ? 319 TYR A CE2 1 ATOM 2542 C CZ . TYR A 1 318 ? 0.159 16.845 51.759 1.00 25.27 ? 319 TYR A CZ 1 ATOM 2543 O OH . TYR A 1 318 ? -0.896 16.185 52.346 1.00 25.83 ? 319 TYR A OH 1 ATOM 2544 N N . LEU A 1 319 ? 5.522 17.839 52.090 1.00 21.80 ? 320 LEU A N 1 ATOM 2545 C CA . LEU A 1 319 ? 5.929 16.913 53.132 1.00 21.91 ? 320 LEU A CA 1 ATOM 2546 C C . LEU A 1 319 ? 6.464 17.655 54.364 1.00 21.39 ? 320 LEU A C 1 ATOM 2547 O O . LEU A 1 319 ? 6.123 17.320 55.501 1.00 18.94 ? 320 LEU A O 1 ATOM 2548 C CB . LEU A 1 319 ? 6.958 15.967 52.508 1.00 23.41 ? 320 LEU A CB 1 ATOM 2549 C CG . LEU A 1 319 ? 8.206 15.318 53.089 1.00 27.00 ? 320 LEU A CG 1 ATOM 2550 C CD1 . LEU A 1 319 ? 8.897 14.694 51.877 1.00 26.48 ? 320 LEU A CD1 1 ATOM 2551 C CD2 . LEU A 1 319 ? 9.141 16.289 53.777 1.00 26.99 ? 320 LEU A CD2 1 ATOM 2552 N N . LYS A 1 320 ? 7.291 18.672 54.140 1.00 22.52 ? 321 LYS A N 1 ATOM 2553 C CA . LYS A 1 320 ? 7.833 19.458 55.245 1.00 24.65 ? 321 LYS A CA 1 ATOM 2554 C C . LYS A 1 320 ? 6.721 20.245 55.935 1.00 23.51 ? 321 LYS A C 1 ATOM 2555 O O . LYS A 1 320 ? 6.696 20.352 57.164 1.00 21.60 ? 321 LYS A O 1 ATOM 2556 C CB . LYS A 1 320 ? 8.901 20.429 54.738 1.00 25.30 ? 321 LYS A CB 1 ATOM 2557 C CG . LYS A 1 320 ? 10.170 19.747 54.254 1.00 28.83 ? 321 LYS A CG 1 ATOM 2558 C CD . LYS A 1 320 ? 11.099 20.729 53.555 1.00 32.12 ? 321 LYS A CD 1 ATOM 2559 C CE . LYS A 1 320 ? 11.655 21.766 54.511 1.00 33.21 ? 321 LYS A CE 1 ATOM 2560 N NZ . LYS A 1 320 ? 12.444 22.804 53.783 1.00 34.18 ? 321 LYS A NZ 1 ATOM 2561 N N . ASN A 1 321 ? 5.796 20.789 55.150 1.00 21.43 ? 322 ASN A N 1 ATOM 2562 C CA . ASN A 1 321 ? 4.703 21.563 55.726 1.00 24.01 ? 322 ASN A CA 1 ATOM 2563 C C . ASN A 1 321 ? 3.779 20.714 56.590 1.00 25.96 ? 322 ASN A C 1 ATOM 2564 O O . ASN A 1 321 ? 3.070 21.237 57.457 1.00 25.62 ? 322 ASN A O 1 ATOM 2565 C CB . ASN A 1 321 ? 3.910 22.272 54.625 1.00 24.92 ? 322 ASN A CB 1 ATOM 2566 C CG . ASN A 1 321 ? 4.641 23.482 54.085 1.00 27.70 ? 322 ASN A CG 1 ATOM 2567 O OD1 . ASN A 1 321 ? 5.357 24.146 54.824 1.00 31.19 ? 322 ASN A OD1 1 ATOM 2568 N ND2 . ASN A 1 321 ? 4.462 23.780 52.803 1.00 26.95 ? 322 ASN A ND2 1 ATOM 2569 N N . ARG A 1 322 ? 3.797 19.403 56.357 1.00 25.35 ? 323 ARG A N 1 ATOM 2570 C CA . ARG A 1 322 ? 2.988 18.464 57.127 1.00 25.50 ? 323 ARG A CA 1 ATOM 2571 C C . ARG A 1 322 ? 3.838 17.867 58.239 1.00 27.19 ? 323 ARG A C 1 ATOM 2572 O O . ARG A 1 322 ? 3.378 17.015 59.008 1.00 26.40 ? 323 ARG A O 1 ATOM 2573 C CB . ARG A 1 322 ? 2.486 17.341 56.225 1.00 27.87 ? 323 ARG A CB 1 ATOM 2574 C CG . ARG A 1 322 ? 1.375 17.757 55.292 1.00 29.78 ? 323 ARG A CG 1 ATOM 2575 C CD . ARG A 1 322 ? 0.084 17.889 56.066 1.00 31.45 ? 323 ARG A CD 1 ATOM 2576 N NE . ARG A 1 322 ? -1.001 17.334 55.276 1.00 35.70 ? 323 ARG A NE 1 ATOM 2577 C CZ . ARG A 1 322 ? -2.166 16.933 55.763 1.00 36.30 ? 323 ARG A CZ 1 ATOM 2578 N NH1 . ARG A 1 322 ? -2.420 17.021 57.060 1.00 33.15 ? 323 ARG A NH1 1 ATOM 2579 N NH2 . ARG A 1 322 ? -3.074 16.430 54.944 1.00 41.46 ? 323 ARG A NH2 1 ATOM 2580 N N . GLN A 1 323 ? 5.090 18.309 58.303 1.00 25.27 ? 324 GLN A N 1 ATOM 2581 C CA . GLN A 1 323 ? 6.034 17.831 59.306 1.00 27.02 ? 324 GLN A CA 1 ATOM 2582 C C . GLN A 1 323 ? 6.218 16.314 59.308 1.00 25.25 ? 324 GLN A C 1 ATOM 2583 O O . GLN A 1 323 ? 6.224 15.679 60.369 1.00 22.97 ? 324 GLN A O 1 ATOM 2584 C CB . GLN A 1 323 ? 5.604 18.299 60.697 1.00 31.89 ? 324 GLN A CB 1 ATOM 2585 C CG . GLN A 1 323 ? 5.460 19.807 60.796 1.00 38.63 ? 324 GLN A CG 1 ATOM 2586 C CD . GLN A 1 323 ? 5.633 20.308 62.211 1.00 44.40 ? 324 GLN A CD 1 ATOM 2587 O OE1 . GLN A 1 323 ? 4.836 19.995 63.097 1.00 45.95 ? 324 GLN A OE1 1 ATOM 2588 N NE2 . GLN A 1 323 ? 6.689 21.087 62.436 1.00 47.16 ? 324 GLN A NE2 1 ATOM 2589 N N . LEU A 1 324 ? 6.360 15.729 58.121 1.00 22.03 ? 325 LEU A N 1 ATOM 2590 C CA . LEU A 1 324 ? 6.567 14.289 58.034 1.00 21.68 ? 325 LEU A CA 1 ATOM 2591 C C . LEU A 1 324 ? 8.047 14.027 58.300 1.00 20.97 ? 325 LEU A C 1 ATOM 2592 O O . LEU A 1 324 ? 8.855 14.963 58.312 1.00 17.28 ? 325 LEU A O 1 ATOM 2593 C CB . LEU A 1 324 ? 6.175 13.760 56.649 1.00 20.87 ? 325 LEU A CB 1 ATOM 2594 C CG . LEU A 1 324 ? 4.727 13.992 56.204 1.00 24.00 ? 325 LEU A CG 1 ATOM 2595 C CD1 . LEU A 1 324 ? 4.437 13.172 54.943 1.00 21.81 ? 325 LEU A CD1 1 ATOM 2596 C CD2 . LEU A 1 324 ? 3.778 13.593 57.326 1.00 24.16 ? 325 LEU A CD2 1 ATOM 2597 N N . ALA A 1 325 ? 8.399 12.762 58.515 1.00 21.06 ? 326 ALA A N 1 ATOM 2598 C CA . ALA A 1 325 ? 9.783 12.374 58.794 1.00 21.02 ? 326 ALA A CA 1 ATOM 2599 C C . ALA A 1 325 ? 10.714 12.617 57.605 1.00 21.02 ? 326 ALA A C 1 ATOM 2600 O O . ALA A 1 325 ? 11.903 12.887 57.780 1.00 19.54 ? 326 ALA A O 1 ATOM 2601 C CB . ALA A 1 325 ? 9.839 10.900 59.211 1.00 20.86 ? 326 ALA A CB 1 ATOM 2602 N N . GLY A 1 326 ? 10.180 12.521 56.394 1.00 20.13 ? 327 GLY A N 1 ATOM 2603 C CA . GLY A 1 326 ? 11.015 12.754 55.228 1.00 20.72 ? 327 GLY A CA 1 ATOM 2604 C C . GLY A 1 326 ? 10.447 12.181 53.948 1.00 20.58 ? 327 GLY A C 1 ATOM 2605 O O . GLY A 1 326 ? 9.244 11.948 53.844 1.00 18.35 ? 327 GLY A O 1 ATOM 2606 N N . ALA A 1 327 ? 11.324 11.942 52.979 1.00 18.36 ? 328 ALA A N 1 ATOM 2607 C CA . ALA A 1 327 ? 10.931 11.407 51.688 1.00 18.45 ? 328 ALA A CA 1 ATOM 2608 C C . ALA A 1 327 ? 11.610 10.085 51.375 1.00 17.46 ? 328 ALA A C 1 ATOM 2609 O O . ALA A 1 327 ? 12.701 9.797 51.876 1.00 17.87 ? 328 ALA A O 1 ATOM 2610 C CB . ALA A 1 327 ? 11.264 12.419 50.590 1.00 16.24 ? 328 ALA A CB 1 ATOM 2611 N N . MET A 1 328 ? 10.940 9.286 50.548 1.00 16.56 ? 329 MET A N 1 ATOM 2612 C CA . MET A 1 328 ? 11.458 8.008 50.084 1.00 18.52 ? 329 MET A CA 1 ATOM 2613 C C . MET A 1 328 ? 11.485 8.123 48.568 1.00 18.10 ? 329 MET A C 1 ATOM 2614 O O . MET A 1 328 ? 10.552 8.652 47.957 1.00 19.89 ? 329 MET A O 1 ATOM 2615 C CB . MET A 1 328 ? 10.549 6.850 50.510 1.00 16.57 ? 329 MET A CB 1 ATOM 2616 C CG . MET A 1 328 ? 10.903 5.513 49.851 1.00 18.19 ? 329 MET A CG 1 ATOM 2617 S SD . MET A 1 328 ? 10.177 5.266 48.198 1.00 21.26 ? 329 MET A SD 1 ATOM 2618 C CE . MET A 1 328 ? 8.659 4.483 48.594 1.00 20.96 ? 329 MET A CE 1 ATOM 2619 N N . VAL A 1 329 ? 12.560 7.641 47.963 1.00 18.64 ? 330 VAL A N 1 ATOM 2620 C CA . VAL A 1 329 ? 12.709 7.712 46.518 1.00 20.38 ? 330 VAL A CA 1 ATOM 2621 C C . VAL A 1 329 ? 12.831 6.342 45.859 1.00 19.29 ? 330 VAL A C 1 ATOM 2622 O O . VAL A 1 329 ? 13.658 5.520 46.255 1.00 19.22 ? 330 VAL A O 1 ATOM 2623 C CB . VAL A 1 329 ? 13.967 8.537 46.130 1.00 21.39 ? 330 VAL A CB 1 ATOM 2624 C CG1 . VAL A 1 329 ? 14.227 8.412 44.629 1.00 21.93 ? 330 VAL A CG1 1 ATOM 2625 C CG2 . VAL A 1 329 ? 13.778 10.001 46.523 1.00 18.14 ? 330 VAL A CG2 1 ATOM 2626 N N . TRP A 1 330 ? 11.990 6.102 44.863 1.00 18.04 ? 331 TRP A N 1 ATOM 2627 C CA . TRP A 1 330 ? 12.042 4.859 44.105 1.00 19.89 ? 331 TRP A CA 1 ATOM 2628 C C . TRP A 1 330 ? 12.250 5.301 42.657 1.00 20.42 ? 331 TRP A C 1 ATOM 2629 O O . TRP A 1 330 ? 11.346 5.875 42.054 1.00 20.72 ? 331 TRP A O 1 ATOM 2630 C CB . TRP A 1 330 ? 10.727 4.066 44.230 1.00 20.45 ? 331 TRP A CB 1 ATOM 2631 C CG . TRP A 1 330 ? 10.768 2.771 43.446 1.00 21.85 ? 331 TRP A CG 1 ATOM 2632 C CD1 . TRP A 1 330 ? 10.597 2.620 42.093 1.00 23.40 ? 331 TRP A CD1 1 ATOM 2633 C CD2 . TRP A 1 330 ? 11.141 1.480 43.945 1.00 22.89 ? 331 TRP A CD2 1 ATOM 2634 N NE1 . TRP A 1 330 ? 10.851 1.319 41.724 1.00 22.70 ? 331 TRP A NE1 1 ATOM 2635 C CE2 . TRP A 1 330 ? 11.187 0.598 42.841 1.00 25.22 ? 331 TRP A CE2 1 ATOM 2636 C CE3 . TRP A 1 330 ? 11.444 0.983 45.218 1.00 20.86 ? 331 TRP A CE3 1 ATOM 2637 C CZ2 . TRP A 1 330 ? 11.532 -0.753 42.974 1.00 24.42 ? 331 TRP A CZ2 1 ATOM 2638 C CZ3 . TRP A 1 330 ? 11.786 -0.359 45.349 1.00 25.40 ? 331 TRP A CZ3 1 ATOM 2639 C CH2 . TRP A 1 330 ? 11.827 -1.211 44.232 1.00 24.95 ? 331 TRP A CH2 1 ATOM 2640 N N . ALA A 1 331 ? 13.436 5.079 42.097 1.00 21.31 ? 332 ALA A N 1 ATOM 2641 C CA . ALA A 1 331 ? 14.567 4.441 42.759 1.00 19.68 ? 332 ALA A CA 1 ATOM 2642 C C . ALA A 1 331 ? 15.824 5.096 42.187 1.00 18.84 ? 332 ALA A C 1 ATOM 2643 O O . ALA A 1 331 ? 15.795 5.658 41.092 1.00 16.48 ? 332 ALA A O 1 ATOM 2644 C CB . ALA A 1 331 ? 14.573 2.938 42.461 1.00 19.00 ? 332 ALA A CB 1 ATOM 2645 N N . LEU A 1 332 ? 16.931 5.007 42.914 1.00 16.86 ? 333 LEU A N 1 ATOM 2646 C CA . LEU A 1 332 ? 18.181 5.624 42.468 1.00 20.09 ? 333 LEU A CA 1 ATOM 2647 C C . LEU A 1 332 ? 18.623 5.272 41.050 1.00 20.64 ? 333 LEU A C 1 ATOM 2648 O O . LEU A 1 332 ? 19.115 6.140 40.325 1.00 20.57 ? 333 LEU A O 1 ATOM 2649 C CB . LEU A 1 332 ? 19.314 5.293 43.445 1.00 20.50 ? 333 LEU A CB 1 ATOM 2650 C CG . LEU A 1 332 ? 19.123 5.899 44.842 1.00 20.44 ? 333 LEU A CG 1 ATOM 2651 C CD1 . LEU A 1 332 ? 20.227 5.438 45.772 1.00 23.46 ? 333 LEU A CD1 1 ATOM 2652 C CD2 . LEU A 1 332 ? 19.089 7.422 44.743 1.00 23.68 ? 333 LEU A CD2 1 ATOM 2653 N N . ASP A 1 333 ? 18.439 4.013 40.654 1.00 17.55 ? 334 ASP A N 1 ATOM 2654 C CA . ASP A 1 333 ? 18.843 3.553 39.326 1.00 21.51 ? 334 ASP A CA 1 ATOM 2655 C C . ASP A 1 333 ? 17.928 4.013 38.187 1.00 21.92 ? 334 ASP A C 1 ATOM 2656 O O . ASP A 1 333 ? 18.199 3.738 37.017 1.00 22.31 ? 334 ASP A O 1 ATOM 2657 C CB . ASP A 1 333 ? 18.947 2.022 39.323 1.00 21.40 ? 334 ASP A CB 1 ATOM 2658 C CG . ASP A 1 333 ? 17.662 1.351 39.773 1.00 22.72 ? 334 ASP A CG 1 ATOM 2659 O OD1 . ASP A 1 333 ? 16.790 1.097 38.917 1.00 20.73 ? 334 ASP A OD1 1 ATOM 2660 O OD2 . ASP A 1 333 ? 17.527 1.094 40.990 1.00 23.49 ? 334 ASP A OD2 1 ATOM 2661 N N . LEU A 1 334 ? 16.851 4.713 38.519 1.00 21.33 ? 335 LEU A N 1 ATOM 2662 C CA . LEU A 1 334 ? 15.936 5.194 37.498 1.00 21.11 ? 335 LEU A CA 1 ATOM 2663 C C . LEU A 1 334 ? 16.097 6.710 37.323 1.00 21.81 ? 335 LEU A C 1 ATOM 2664 O O . LEU A 1 334 ? 15.566 7.298 36.383 1.00 22.15 ? 335 LEU A O 1 ATOM 2665 C CB . LEU A 1 334 ? 14.500 4.817 37.875 1.00 18.26 ? 335 LEU A CB 1 ATOM 2666 C CG . LEU A 1 334 ? 14.203 3.316 37.903 1.00 22.10 ? 335 LEU A CG 1 ATOM 2667 C CD1 . LEU A 1 334 ? 12.806 3.062 38.463 1.00 21.19 ? 335 LEU A CD1 1 ATOM 2668 C CD2 . LEU A 1 334 ? 14.324 2.756 36.485 1.00 20.03 ? 335 LEU A CD2 1 ATOM 2669 N N . ASP A 1 335 ? 16.837 7.334 38.235 1.00 22.47 ? 336 ASP A N 1 ATOM 2670 C CA . ASP A 1 335 ? 17.120 8.769 38.172 1.00 23.29 ? 336 ASP A CA 1 ATOM 2671 C C . ASP A 1 335 ? 18.300 8.854 37.198 1.00 22.83 ? 336 ASP A C 1 ATOM 2672 O O . ASP A 1 335 ? 18.861 7.819 36.843 1.00 22.99 ? 336 ASP A O 1 ATOM 2673 C CB . ASP A 1 335 ? 17.540 9.265 39.560 1.00 22.53 ? 336 ASP A CB 1 ATOM 2674 C CG . ASP A 1 335 ? 17.505 10.774 39.687 1.00 21.60 ? 336 ASP A CG 1 ATOM 2675 O OD1 . ASP A 1 335 ? 17.296 11.474 38.670 1.00 20.54 ? 336 ASP A OD1 1 ATOM 2676 O OD2 . ASP A 1 335 ? 17.696 11.268 40.815 1.00 22.95 ? 336 ASP A OD2 1 ATOM 2677 N N . ASP A 1 336 ? 18.678 10.053 36.758 1.00 23.88 ? 337 ASP A N 1 ATOM 2678 C CA . ASP A 1 336 ? 19.816 10.186 35.839 1.00 25.27 ? 337 ASP A CA 1 ATOM 2679 C C . ASP A 1 336 ? 21.069 10.046 36.712 1.00 25.56 ? 337 ASP A C 1 ATOM 2680 O O . ASP A 1 336 ? 21.718 11.041 37.049 1.00 24.46 ? 337 ASP A O 1 ATOM 2681 C CB . ASP A 1 336 ? 19.779 11.560 35.132 1.00 26.16 ? 337 ASP A CB 1 ATOM 2682 C CG . ASP A 1 336 ? 20.827 11.693 34.013 1.00 29.88 ? 337 ASP A CG 1 ATOM 2683 O OD1 . ASP A 1 336 ? 21.406 10.666 33.602 1.00 29.81 ? 337 ASP A OD1 1 ATOM 2684 O OD2 . ASP A 1 336 ? 21.051 12.830 33.539 1.00 27.75 ? 337 ASP A OD2 1 ATOM 2685 N N . PHE A 1 337 ? 21.395 8.807 37.091 1.00 24.35 ? 338 PHE A N 1 ATOM 2686 C CA . PHE A 1 337 ? 22.544 8.569 37.961 1.00 26.50 ? 338 PHE A CA 1 ATOM 2687 C C . PHE A 1 337 ? 23.905 8.909 37.363 1.00 28.83 ? 338 PHE A C 1 ATOM 2688 O O . PHE A 1 337 ? 24.823 9.257 38.101 1.00 29.17 ? 338 PHE A O 1 ATOM 2689 C CB . PHE A 1 337 ? 22.556 7.125 38.514 1.00 24.90 ? 338 PHE A CB 1 ATOM 2690 C CG . PHE A 1 337 ? 22.624 6.045 37.462 1.00 25.38 ? 338 PHE A CG 1 ATOM 2691 C CD1 . PHE A 1 337 ? 21.471 5.589 36.823 1.00 24.95 ? 338 PHE A CD1 1 ATOM 2692 C CD2 . PHE A 1 337 ? 23.848 5.470 37.124 1.00 25.47 ? 338 PHE A CD2 1 ATOM 2693 C CE1 . PHE A 1 337 ? 21.537 4.575 35.859 1.00 26.05 ? 338 PHE A CE1 1 ATOM 2694 C CE2 . PHE A 1 337 ? 23.927 4.463 36.169 1.00 25.49 ? 338 PHE A CE2 1 ATOM 2695 C CZ . PHE A 1 337 ? 22.773 4.011 35.533 1.00 27.07 ? 338 PHE A CZ 1 ATOM 2696 N N . ARG A 1 338 ? 24.051 8.809 36.045 1.00 31.27 ? 339 ARG A N 1 ATOM 2697 C CA . ARG A 1 338 ? 25.328 9.156 35.420 1.00 34.86 ? 339 ARG A CA 1 ATOM 2698 C C . ARG A 1 338 ? 25.373 10.670 35.207 1.00 36.10 ? 339 ARG A C 1 ATOM 2699 O O . ARG A 1 338 ? 26.444 11.275 35.191 1.00 37.22 ? 339 ARG A O 1 ATOM 2700 C CB . ARG A 1 338 ? 25.498 8.417 34.088 1.00 33.63 ? 339 ARG A CB 1 ATOM 2701 C CG . ARG A 1 338 ? 25.672 6.911 34.246 1.00 36.52 ? 339 ARG A CG 1 ATOM 2702 C CD . ARG A 1 338 ? 25.922 6.216 32.914 1.00 38.26 ? 339 ARG A CD 1 ATOM 2703 N NE . ARG A 1 338 ? 25.903 4.759 33.045 1.00 39.79 ? 339 ARG A NE 1 ATOM 2704 C CZ . ARG A 1 338 ? 26.880 4.028 33.575 1.00 40.91 ? 339 ARG A CZ 1 ATOM 2705 N NH1 . ARG A 1 338 ? 27.979 4.613 34.030 1.00 42.35 ? 339 ARG A NH1 1 ATOM 2706 N NH2 . ARG A 1 338 ? 26.752 2.708 33.656 1.00 38.96 ? 339 ARG A NH2 1 ATOM 2707 N N . GLY A 1 339 ? 24.196 11.275 35.069 1.00 36.91 ? 340 GLY A N 1 ATOM 2708 C CA . GLY A 1 339 ? 24.103 12.711 34.873 1.00 38.37 ? 340 GLY A CA 1 ATOM 2709 C C . GLY A 1 339 ? 24.418 13.161 33.455 1.00 39.81 ? 340 GLY A C 1 ATOM 2710 O O . GLY A 1 339 ? 24.772 14.318 33.230 1.00 39.90 ? 340 GLY A O 1 ATOM 2711 N N . THR A 1 340 ? 24.271 12.255 32.494 1.00 40.44 ? 341 THR A N 1 ATOM 2712 C CA . THR A 1 340 ? 24.568 12.566 31.102 1.00 41.78 ? 341 THR A CA 1 ATOM 2713 C C . THR A 1 340 ? 23.371 12.594 30.149 1.00 43.10 ? 341 THR A C 1 ATOM 2714 O O . THR A 1 340 ? 23.541 12.853 28.956 1.00 44.07 ? 341 THR A O 1 ATOM 2715 C CB . THR A 1 340 ? 25.587 11.571 30.536 1.00 42.89 ? 341 THR A CB 1 ATOM 2716 O OG1 . THR A 1 340 ? 25.071 10.238 30.661 1.00 44.35 ? 341 THR A OG1 1 ATOM 2717 C CG2 . THR A 1 340 ? 26.915 11.688 31.284 1.00 44.05 ? 341 THR A CG2 1 ATOM 2718 N N . PHE A 1 341 ? 22.168 12.336 30.658 1.00 42.11 ? 342 PHE A N 1 ATOM 2719 C CA . PHE A 1 341 ? 20.977 12.336 29.806 1.00 41.18 ? 342 PHE A CA 1 ATOM 2720 C C . PHE A 1 341 ? 20.111 13.582 29.930 1.00 42.16 ? 342 PHE A C 1 ATOM 2721 O O . PHE A 1 341 ? 19.532 14.051 28.949 1.00 42.02 ? 342 PHE A O 1 ATOM 2722 C CB . PHE A 1 341 ? 20.071 11.141 30.120 1.00 42.45 ? 342 PHE A CB 1 ATOM 2723 C CG . PHE A 1 341 ? 20.673 9.807 29.804 1.00 42.65 ? 342 PHE A CG 1 ATOM 2724 C CD1 . PHE A 1 341 ? 21.559 9.197 30.688 1.00 42.31 ? 342 PHE A CD1 1 ATOM 2725 C CD2 . PHE A 1 341 ? 20.313 9.136 28.638 1.00 44.19 ? 342 PHE A CD2 1 ATOM 2726 C CE1 . PHE A 1 341 ? 22.081 7.931 30.418 1.00 43.18 ? 342 PHE A CE1 1 ATOM 2727 C CE2 . PHE A 1 341 ? 20.828 7.871 28.354 1.00 44.46 ? 342 PHE A CE2 1 ATOM 2728 C CZ . PHE A 1 341 ? 21.712 7.264 29.247 1.00 42.88 ? 342 PHE A CZ 1 ATOM 2729 N N . CYS A 1 342 ? 20.027 14.115 31.141 1.00 41.65 ? 343 CYS A N 1 ATOM 2730 C CA . CYS A 1 342 ? 19.168 15.258 31.417 1.00 43.56 ? 343 CYS A CA 1 ATOM 2731 C C . CYS A 1 342 ? 19.734 16.675 31.417 1.00 47.67 ? 343 CYS A C 1 ATOM 2732 O O . CYS A 1 342 ? 19.341 17.500 32.245 1.00 50.63 ? 343 CYS A O 1 ATOM 2733 C CB . CYS A 1 342 ? 18.471 15.012 32.745 1.00 39.42 ? 343 CYS A CB 1 ATOM 2734 S SG . CYS A 1 342 ? 17.571 13.432 32.789 1.00 30.79 ? 343 CYS A SG 1 ATOM 2735 N N . GLY A 1 343 ? 20.631 16.976 30.488 1.00 51.05 ? 344 GLY A N 1 ATOM 2736 C CA . GLY A 1 343 ? 21.187 18.314 30.436 1.00 55.19 ? 344 GLY A CA 1 ATOM 2737 C C . GLY A 1 343 ? 22.088 18.643 31.611 1.00 57.89 ? 344 GLY A C 1 ATOM 2738 O O . GLY A 1 343 ? 23.247 18.230 31.631 1.00 59.79 ? 344 GLY A O 1 ATOM 2739 N N . GLN A 1 344 ? 21.564 19.381 32.587 1.00 59.90 ? 345 GLN A N 1 ATOM 2740 C CA . GLN A 1 344 ? 22.347 19.770 33.757 1.00 62.60 ? 345 GLN A CA 1 ATOM 2741 C C . GLN A 1 344 ? 23.441 18.767 34.096 1.00 62.47 ? 345 GLN A C 1 ATOM 2742 O O . GLN A 1 344 ? 23.166 17.591 34.336 1.00 64.10 ? 345 GLN A O 1 ATOM 2743 C CB . GLN A 1 344 ? 21.435 19.977 34.976 1.00 65.33 ? 345 GLN A CB 1 ATOM 2744 C CG . GLN A 1 344 ? 20.409 18.876 35.219 1.00 68.53 ? 345 GLN A CG 1 ATOM 2745 C CD . GLN A 1 344 ? 19.434 19.221 36.338 1.00 71.69 ? 345 GLN A CD 1 ATOM 2746 O OE1 . GLN A 1 344 ? 18.291 18.758 36.344 1.00 74.31 ? 345 GLN A OE1 1 ATOM 2747 N NE2 . GLN A 1 344 ? 19.884 20.030 37.294 1.00 72.42 ? 345 GLN A NE2 1 ATOM 2748 N N . ASN A 1 345 ? 24.686 19.234 34.080 1.00 61.39 ? 346 ASN A N 1 ATOM 2749 C CA . ASN A 1 345 ? 25.828 18.391 34.407 1.00 59.86 ? 346 ASN A CA 1 ATOM 2750 C C . ASN A 1 345 ? 25.668 18.128 35.894 1.00 57.54 ? 346 ASN A C 1 ATOM 2751 O O . ASN A 1 345 ? 26.438 18.616 36.725 1.00 58.21 ? 346 ASN A O 1 ATOM 2752 C CB . ASN A 1 345 ? 27.132 19.142 34.126 1.00 61.90 ? 346 ASN A CB 1 ATOM 2753 C CG . ASN A 1 345 ? 27.243 19.588 32.679 1.00 64.08 ? 346 ASN A CG 1 ATOM 2754 O OD1 . ASN A 1 345 ? 26.334 20.226 32.141 1.00 65.25 ? 346 ASN A OD1 1 ATOM 2755 N ND2 . ASN A 1 345 ? 28.361 19.258 32.041 1.00 65.64 ? 346 ASN A ND2 1 ATOM 2756 N N . LEU A 1 346 ? 24.637 17.357 36.216 1.00 53.04 ? 347 LEU A N 1 ATOM 2757 C CA . LEU A 1 346 ? 24.310 17.047 37.595 1.00 48.48 ? 347 LEU A CA 1 ATOM 2758 C C . LEU A 1 346 ? 23.882 15.590 37.715 1.00 43.38 ? 347 LEU A C 1 ATOM 2759 O O . LEU A 1 346 ? 23.026 15.119 36.967 1.00 40.96 ? 347 LEU A O 1 ATOM 2760 C CB . LEU A 1 346 ? 23.170 17.968 38.045 1.00 50.97 ? 347 LEU A CB 1 ATOM 2761 C CG . LEU A 1 346 ? 22.966 18.336 39.515 1.00 52.96 ? 347 LEU A CG 1 ATOM 2762 C CD1 . LEU A 1 346 ? 21.765 19.266 39.625 1.00 53.60 ? 347 LEU A CD1 1 ATOM 2763 C CD2 . LEU A 1 346 ? 22.746 17.098 40.352 1.00 53.59 ? 347 LEU A CD2 1 ATOM 2764 N N . THR A 1 347 ? 24.478 14.880 38.664 1.00 38.35 ? 348 THR A N 1 ATOM 2765 C CA . THR A 1 347 ? 24.142 13.480 38.879 1.00 34.95 ? 348 THR A CA 1 ATOM 2766 C C . THR A 1 347 ? 22.912 13.428 39.809 1.00 31.58 ? 348 THR A C 1 ATOM 2767 O O . THR A 1 347 ? 22.779 14.247 40.718 1.00 28.85 ? 348 THR A O 1 ATOM 2768 C CB . THR A 1 347 ? 25.344 12.734 39.511 1.00 36.14 ? 348 THR A CB 1 ATOM 2769 O OG1 . THR A 1 347 ? 25.169 11.319 39.371 1.00 44.36 ? 348 THR A OG1 1 ATOM 2770 C CG2 . THR A 1 347 ? 25.489 13.098 40.980 1.00 34.34 ? 348 THR A CG2 1 ATOM 2771 N N . PHE A 1 348 ? 22.008 12.485 39.561 1.00 27.17 ? 349 PHE A N 1 ATOM 2772 C CA . PHE A 1 348 ? 20.792 12.342 40.372 1.00 24.92 ? 349 PHE A CA 1 ATOM 2773 C C . PHE A 1 348 ? 20.033 13.659 40.483 1.00 22.54 ? 349 PHE A C 1 ATOM 2774 O O . PHE A 1 348 ? 19.811 14.163 41.583 1.00 21.90 ? 349 PHE A O 1 ATOM 2775 C CB . PHE A 1 348 ? 21.142 11.869 41.781 1.00 23.14 ? 349 PHE A CB 1 ATOM 2776 C CG . PHE A 1 348 ? 21.791 10.525 41.827 1.00 22.29 ? 349 PHE A CG 1 ATOM 2777 C CD1 . PHE A 1 348 ? 21.034 9.367 41.702 1.00 21.43 ? 349 PHE A CD1 1 ATOM 2778 C CD2 . PHE A 1 348 ? 23.166 10.416 42.000 1.00 21.52 ? 349 PHE A CD2 1 ATOM 2779 C CE1 . PHE A 1 348 ? 21.639 8.108 41.758 1.00 22.30 ? 349 PHE A CE1 1 ATOM 2780 C CE2 . PHE A 1 348 ? 23.782 9.165 42.057 1.00 22.00 ? 349 PHE A CE2 1 ATOM 2781 C CZ . PHE A 1 348 ? 23.016 8.012 41.935 1.00 21.48 ? 349 PHE A CZ 1 ATOM 2782 N N . PRO A 1 349 ? 19.601 14.219 39.346 1.00 22.89 ? 350 PRO A N 1 ATOM 2783 C CA . PRO A 1 349 ? 18.872 15.489 39.386 1.00 21.06 ? 350 PRO A CA 1 ATOM 2784 C C . PRO A 1 349 ? 17.581 15.491 40.202 1.00 21.04 ? 350 PRO A C 1 ATOM 2785 O O . PRO A 1 349 ? 17.305 16.449 40.922 1.00 21.24 ? 350 PRO A O 1 ATOM 2786 C CB . PRO A 1 349 ? 18.638 15.799 37.909 1.00 21.83 ? 350 PRO A CB 1 ATOM 2787 C CG . PRO A 1 349 ? 18.577 14.438 37.269 1.00 24.48 ? 350 PRO A CG 1 ATOM 2788 C CD . PRO A 1 349 ? 19.702 13.703 37.968 1.00 22.12 ? 350 PRO A CD 1 ATOM 2789 N N . LEU A 1 350 ? 16.793 14.427 40.096 1.00 18.74 ? 351 LEU A N 1 ATOM 2790 C CA . LEU A 1 350 ? 15.539 14.347 40.834 1.00 20.80 ? 351 LEU A CA 1 ATOM 2791 C C . LEU A 1 350 ? 15.774 14.184 42.334 1.00 20.22 ? 351 LEU A C 1 ATOM 2792 O O . LEU A 1 350 ? 15.235 14.943 43.139 1.00 18.98 ? 351 LEU A O 1 ATOM 2793 C CB . LEU A 1 350 ? 14.685 13.189 40.299 1.00 21.63 ? 351 LEU A CB 1 ATOM 2794 C CG . LEU A 1 350 ? 13.397 13.536 39.540 1.00 25.98 ? 351 LEU A CG 1 ATOM 2795 C CD1 . LEU A 1 350 ? 13.584 14.794 38.699 1.00 26.75 ? 351 LEU A CD1 1 ATOM 2796 C CD2 . LEU A 1 350 ? 12.999 12.351 38.667 1.00 25.40 ? 351 LEU A CD2 1 ATOM 2797 N N . THR A 1 351 ? 16.587 13.204 42.712 1.00 21.14 ? 352 THR A N 1 ATOM 2798 C CA . THR A 1 351 ? 16.868 12.967 44.125 1.00 19.81 ? 352 THR A CA 1 ATOM 2799 C C . THR A 1 351 ? 17.570 14.166 44.778 1.00 22.41 ? 352 THR A C 1 ATOM 2800 O O . THR A 1 351 ? 17.316 14.487 45.947 1.00 20.88 ? 352 THR A O 1 ATOM 2801 C CB . THR A 1 351 ? 17.721 11.692 44.298 1.00 20.84 ? 352 THR A CB 1 ATOM 2802 O OG1 . THR A 1 351 ? 17.080 10.602 43.618 1.00 17.91 ? 352 THR A OG1 1 ATOM 2803 C CG2 . THR A 1 351 ? 17.868 11.342 45.775 1.00 18.28 ? 352 THR A CG2 1 ATOM 2804 N N . SER A 1 352 ? 18.449 14.826 44.026 1.00 20.10 ? 353 SER A N 1 ATOM 2805 C CA . SER A 1 352 ? 19.166 15.995 44.529 1.00 23.22 ? 353 SER A CA 1 ATOM 2806 C C . SER A 1 352 ? 18.202 17.157 44.784 1.00 22.16 ? 353 SER A C 1 ATOM 2807 O O . SER A 1 352 ? 18.342 17.894 45.762 1.00 24.06 ? 353 SER A O 1 ATOM 2808 C CB . SER A 1 352 ? 20.243 16.430 43.524 1.00 24.28 ? 353 SER A CB 1 ATOM 2809 O OG . SER A 1 352 ? 21.211 15.408 43.358 1.00 32.54 ? 353 SER A OG 1 ATOM 2810 N N . ALA A 1 353 ? 17.230 17.319 43.892 1.00 21.07 ? 354 ALA A N 1 ATOM 2811 C CA . ALA A 1 353 ? 16.234 18.375 44.036 1.00 22.25 ? 354 ALA A CA 1 ATOM 2812 C C . ALA A 1 353 ? 15.476 18.162 45.350 1.00 22.74 ? 354 ALA A C 1 ATOM 2813 O O . ALA A 1 353 ? 15.185 19.120 46.066 1.00 23.43 ? 354 ALA A O 1 ATOM 2814 C CB . ALA A 1 353 ? 15.263 18.352 42.852 1.00 20.25 ? 354 ALA A CB 1 ATOM 2815 N N . VAL A 1 354 ? 15.158 16.909 45.666 1.00 20.20 ? 355 VAL A N 1 ATOM 2816 C CA . VAL A 1 354 ? 14.455 16.598 46.908 1.00 19.65 ? 355 VAL A CA 1 ATOM 2817 C C . VAL A 1 354 ? 15.339 16.929 48.105 1.00 20.47 ? 355 VAL A C 1 ATOM 2818 O O . VAL A 1 354 ? 14.885 17.546 49.070 1.00 18.32 ? 355 VAL A O 1 ATOM 2819 C CB . VAL A 1 354 ? 14.082 15.098 46.997 1.00 20.56 ? 355 VAL A CB 1 ATOM 2820 C CG1 . VAL A 1 354 ? 13.492 14.787 48.376 1.00 19.69 ? 355 VAL A CG1 1 ATOM 2821 C CG2 . VAL A 1 354 ? 13.091 14.742 45.916 1.00 18.46 ? 355 VAL A CG2 1 ATOM 2822 N N . LYS A 1 355 ? 16.601 16.508 48.040 1.00 20.54 ? 356 LYS A N 1 ATOM 2823 C CA . LYS A 1 355 ? 17.549 16.755 49.126 1.00 22.97 ? 356 LYS A CA 1 ATOM 2824 C C . LYS A 1 355 ? 17.716 18.249 49.400 1.00 23.65 ? 356 LYS A C 1 ATOM 2825 O O . LYS A 1 355 ? 17.778 18.669 50.556 1.00 22.23 ? 356 LYS A O 1 ATOM 2826 C CB . LYS A 1 355 ? 18.910 16.150 48.789 1.00 26.50 ? 356 LYS A CB 1 ATOM 2827 C CG . LYS A 1 355 ? 19.951 16.309 49.889 1.00 28.11 ? 356 LYS A CG 1 ATOM 2828 C CD . LYS A 1 355 ? 21.314 15.812 49.435 1.00 33.73 ? 356 LYS A CD 1 ATOM 2829 C CE . LYS A 1 355 ? 22.360 15.956 50.540 1.00 35.32 ? 356 LYS A CE 1 ATOM 2830 N NZ . LYS A 1 355 ? 21.965 15.179 51.745 1.00 39.54 ? 356 LYS A NZ 1 ATOM 2831 N N . ASP A 1 356 ? 17.796 19.045 48.337 1.00 24.47 ? 357 ASP A N 1 ATOM 2832 C CA . ASP A 1 356 ? 17.950 20.493 48.479 1.00 27.08 ? 357 ASP A CA 1 ATOM 2833 C C . ASP A 1 356 ? 16.816 21.117 49.286 1.00 27.47 ? 357 ASP A C 1 ATOM 2834 O O . ASP A 1 356 ? 17.053 21.940 50.175 1.00 27.12 ? 357 ASP A O 1 ATOM 2835 C CB . ASP A 1 356 ? 18.005 21.181 47.111 1.00 29.61 ? 357 ASP A CB 1 ATOM 2836 C CG . ASP A 1 356 ? 19.313 20.943 46.387 1.00 32.81 ? 357 ASP A CG 1 ATOM 2837 O OD1 . ASP A 1 356 ? 20.328 20.685 47.067 1.00 33.85 ? 357 ASP A OD1 1 ATOM 2838 O OD2 . ASP A 1 356 ? 19.329 21.027 45.139 1.00 36.75 ? 357 ASP A OD2 1 ATOM 2839 N N . VAL A 1 357 ? 15.581 20.741 48.965 1.00 25.96 ? 358 VAL A N 1 ATOM 2840 C CA . VAL A 1 357 ? 14.425 21.275 49.677 1.00 25.34 ? 358 VAL A CA 1 ATOM 2841 C C . VAL A 1 357 ? 14.444 20.837 51.137 1.00 25.41 ? 358 VAL A C 1 ATOM 2842 O O . VAL A 1 357 ? 14.184 21.640 52.038 1.00 24.29 ? 358 VAL A O 1 ATOM 2843 C CB . VAL A 1 357 ? 13.096 20.815 49.017 1.00 24.21 ? 358 VAL A CB 1 ATOM 2844 C CG1 . VAL A 1 357 ? 11.913 21.187 49.896 1.00 23.52 ? 358 VAL A CG1 1 ATOM 2845 C CG2 . VAL A 1 357 ? 12.946 21.464 47.647 1.00 25.27 ? 358 VAL A CG2 1 ATOM 2846 N N . LEU A 1 358 ? 14.754 19.565 51.373 1.00 23.27 ? 359 LEU A N 1 ATOM 2847 C CA . LEU A 1 358 ? 14.798 19.036 52.736 1.00 26.00 ? 359 LEU A CA 1 ATOM 2848 C C . LEU A 1 358 ? 15.893 19.691 53.581 1.00 28.42 ? 359 LEU A C 1 ATOM 2849 O O . LEU A 1 358 ? 15.763 19.803 54.801 1.00 27.35 ? 359 LEU A O 1 ATOM 2850 C CB . LEU A 1 358 ? 15.003 17.519 52.704 1.00 24.10 ? 359 LEU A CB 1 ATOM 2851 C CG . LEU A 1 358 ? 13.764 16.615 52.766 1.00 27.63 ? 359 LEU A CG 1 ATOM 2852 C CD1 . LEU A 1 358 ? 12.609 17.185 51.958 1.00 27.57 ? 359 LEU A CD1 1 ATOM 2853 C CD2 . LEU A 1 358 ? 14.149 15.220 52.271 1.00 26.98 ? 359 LEU A CD2 1 ATOM 2854 N N . ALA A 1 359 ? 16.965 20.133 52.932 1.00 31.04 ? 360 ALA A N 1 ATOM 2855 C CA . ALA A 1 359 ? 18.068 20.774 53.643 1.00 35.49 ? 360 ALA A CA 1 ATOM 2856 C C . ALA A 1 359 ? 17.775 22.228 54.026 1.00 38.25 ? 360 ALA A C 1 ATOM 2857 O O . ALA A 1 359 ? 18.506 22.820 54.817 1.00 40.39 ? 360 ALA A O 1 ATOM 2858 C CB . ALA A 1 359 ? 19.350 20.700 52.801 1.00 34.56 ? 360 ALA A CB 1 ATOM 2859 N N . ARG A 1 360 ? 16.705 22.798 53.475 1.00 42.76 ? 361 ARG A N 1 ATOM 2860 C CA . ARG A 1 360 ? 16.335 24.186 53.765 1.00 47.27 ? 361 ARG A CA 1 ATOM 2861 C C . ARG A 1 360 ? 15.727 24.430 55.147 1.00 49.37 ? 361 ARG A C 1 ATOM 2862 O O . ARG A 1 360 ? 15.743 25.563 55.616 1.00 50.66 ? 361 ARG A O 1 ATOM 2863 C CB . ARG A 1 360 ? 15.318 24.711 52.756 1.00 48.99 ? 361 ARG A CB 1 ATOM 2864 C CG . ARG A 1 360 ? 15.739 24.829 51.312 1.00 52.84 ? 361 ARG A CG 1 ATOM 2865 C CD . ARG A 1 360 ? 14.532 25.379 50.564 1.00 57.01 ? 361 ARG A CD 1 ATOM 2866 N NE . ARG A 1 360 ? 14.651 25.346 49.115 1.00 60.96 ? 361 ARG A NE 1 ATOM 2867 C CZ . ARG A 1 360 ? 13.632 25.577 48.293 1.00 64.41 ? 361 ARG A CZ 1 ATOM 2868 N NH1 . ARG A 1 360 ? 12.430 25.854 48.788 1.00 65.26 ? 361 ARG A NH1 1 ATOM 2869 N NH2 . ARG A 1 360 ? 13.809 25.532 46.979 1.00 65.24 ? 361 ARG A NH2 1 ATOM 2870 N N . VAL A 1 361 ? 15.170 23.388 55.765 1.00 52.45 ? 362 VAL A N 1 ATOM 2871 C CA . VAL A 1 361 ? 14.510 23.459 57.082 1.00 56.12 ? 362 VAL A CA 1 ATOM 2872 C C . VAL A 1 361 ? 12.996 23.465 56.892 1.00 57.33 ? 362 VAL A C 1 ATOM 2873 O O . VAL A 1 361 ? 12.301 22.804 57.698 1.00 59.12 ? 362 VAL A O 1 ATOM 2874 C CB . VAL A 1 361 ? 14.886 24.734 57.912 1.00 57.35 ? 362 VAL A CB 1 ATOM 2875 C CG1 . VAL A 1 361 ? 13.973 25.915 57.550 1.00 57.19 ? 362 VAL A CG1 1 ATOM 2876 C CG2 . VAL A 1 361 ? 14.774 24.434 59.400 1.00 58.20 ? 362 VAL A CG2 1 ATOM 2877 O OXT . VAL A 1 361 ? 12.530 24.148 55.947 1.00 58.37 ? 362 VAL A OXT 1 HETATM 2878 C C1 . NAG B 2 . ? 13.265 -17.634 46.228 0.50 32.50 ? 363 NAG A C1 1 HETATM 2879 C C2 . NAG B 2 . ? 13.978 -18.247 45.014 0.50 33.00 ? 363 NAG A C2 1 HETATM 2880 C C3 . NAG B 2 . ? 13.156 -19.417 44.411 0.50 35.60 ? 363 NAG A C3 1 HETATM 2881 C C4 . NAG B 2 . ? 12.656 -20.398 45.504 0.50 37.80 ? 363 NAG A C4 1 HETATM 2882 C C5 . NAG B 2 . ? 11.964 -19.578 46.596 0.50 35.79 ? 363 NAG A C5 1 HETATM 2883 C C6 . NAG B 2 . ? 11.383 -20.370 47.754 0.50 34.42 ? 363 NAG A C6 1 HETATM 2884 C C7 . NAG B 2 . ? 15.377 -16.969 43.502 0.50 31.81 ? 363 NAG A C7 1 HETATM 2885 C C8 . NAG B 2 . ? 15.444 -16.240 42.166 0.50 31.52 ? 363 NAG A C8 1 HETATM 2886 N N2 . NAG B 2 . ? 14.171 -17.214 44.009 0.50 32.04 ? 363 NAG A N2 1 HETATM 2887 O O3 . NAG B 2 . ? 13.963 -20.113 43.474 0.50 35.25 ? 363 NAG A O3 1 HETATM 2888 O O4 . NAG B 2 . ? 11.679 -21.303 44.953 0.50 44.88 ? 363 NAG A O4 1 HETATM 2889 O O5 . NAG B 2 . ? 12.898 -18.650 47.157 0.50 32.12 ? 363 NAG A O5 1 HETATM 2890 O O6 . NAG B 2 . ? 12.317 -21.328 48.217 0.50 36.39 ? 363 NAG A O6 1 HETATM 2891 O O7 . NAG B 2 . ? 16.418 -17.302 44.065 0.50 34.08 ? 363 NAG A O7 1 HETATM 2892 C C1 . NDG C 3 . ? 12.041 -22.551 44.466 0.50 50.04 ? 364 NDG A C1 1 HETATM 2893 C C2 . NDG C 3 . ? 10.771 -23.256 43.952 0.50 52.96 ? 364 NDG A C2 1 HETATM 2894 C C3 . NDG C 3 . ? 10.977 -24.732 43.854 0.50 54.82 ? 364 NDG A C3 1 HETATM 2895 C C4 . NDG C 3 . ? 12.393 -25.082 43.791 0.50 56.47 ? 364 NDG A C4 1 HETATM 2896 C C5 . NDG C 3 . ? 13.200 -24.584 45.029 0.50 55.61 ? 364 NDG A C5 1 HETATM 2897 C C6 . NDG C 3 . ? 14.638 -24.282 44.637 0.50 56.53 ? 364 NDG A C6 1 HETATM 2898 C C7 . NDG C 3 . ? 8.432 -22.848 44.355 0.50 55.83 ? 364 NDG A C7 1 HETATM 2899 C C8 . NDG C 3 . ? 8.279 -22.216 42.969 0.50 57.03 ? 364 NDG A C8 1 HETATM 2900 O O . NDG C 3 . ? 12.664 -23.333 45.520 0.50 52.63 ? 364 NDG A O 1 HETATM 2901 O O3 . NDG C 3 . ? 10.412 -25.272 42.665 0.50 54.22 ? 364 NDG A O3 1 HETATM 2902 O O4 . NDG C 3 . ? 12.427 -26.544 43.681 0.50 60.64 ? 364 NDG A O4 1 HETATM 2903 O O6 . NDG C 3 . ? 14.744 -23.933 43.260 0.50 57.78 ? 364 NDG A O6 1 HETATM 2904 O O7 . NDG C 3 . ? 7.424 -23.129 44.998 0.50 57.81 ? 364 NDG A O7 1 HETATM 2905 N N2 . NDG C 3 . ? 9.654 -23.039 44.846 0.50 53.89 ? 364 NDG A N2 1 HETATM 2906 C C1 . BMA D 4 . ? 13.035 -27.412 44.695 0.50 62.29 ? 365 BMA A C1 1 HETATM 2907 C C2 . BMA D 4 . ? 12.351 -28.816 44.509 0.50 63.01 ? 365 BMA A C2 1 HETATM 2908 C C3 . BMA D 4 . ? 13.103 -30.003 45.001 0.50 63.46 ? 365 BMA A C3 1 HETATM 2909 C C4 . BMA D 4 . ? 14.469 -29.982 44.404 0.50 63.75 ? 365 BMA A C4 1 HETATM 2910 C C5 . BMA D 4 . ? 15.209 -28.715 44.810 0.50 63.81 ? 365 BMA A C5 1 HETATM 2911 C C6 . BMA D 4 . ? 16.503 -28.710 44.012 0.50 64.09 ? 365 BMA A C6 1 HETATM 2912 O O2 . BMA D 4 . ? 12.069 -28.979 43.122 0.50 62.07 ? 365 BMA A O2 1 HETATM 2913 O O3 . BMA D 4 . ? 12.416 -31.176 44.616 0.50 64.10 ? 365 BMA A O3 1 HETATM 2914 O O4 . BMA D 4 . ? 15.221 -31.118 44.855 0.50 64.01 ? 365 BMA A O4 1 HETATM 2915 O O5 . BMA D 4 . ? 14.506 -27.485 44.431 0.50 64.18 ? 365 BMA A O5 1 HETATM 2916 O O6 . BMA D 4 . ? 17.589 -28.281 44.819 0.50 64.18 ? 365 BMA A O6 1 HETATM 2917 C C1 . NAG E 2 . ? 9.263 -3.102 40.683 1.00 59.06 ? 366 NAG A C1 1 HETATM 2918 C C2 . NAG E 2 . ? 9.839 -2.935 39.270 1.00 58.15 ? 366 NAG A C2 1 HETATM 2919 C C3 . NAG E 2 . ? 9.613 -4.158 38.420 1.00 58.71 ? 366 NAG A C3 1 HETATM 2920 C C4 . NAG E 2 . ? 10.272 -5.272 39.180 1.00 58.23 ? 366 NAG A C4 1 HETATM 2921 C C5 . NAG E 2 . ? 9.508 -5.546 40.460 1.00 57.59 ? 366 NAG A C5 1 HETATM 2922 C C6 . NAG E 2 . ? 10.233 -6.638 41.233 1.00 56.09 ? 366 NAG A C6 1 HETATM 2923 C C7 . NAG E 2 . ? 9.927 -0.662 38.454 1.00 57.32 ? 366 NAG A C7 1 HETATM 2924 C C8 . NAG E 2 . ? 9.288 0.417 37.589 1.00 56.54 ? 366 NAG A C8 1 HETATM 2925 N N2 . NAG E 2 . ? 9.228 -1.782 38.637 1.00 57.37 ? 366 NAG A N2 1 HETATM 2926 O O1 . NAG E 2 . ? 9.885 -2.145 41.466 1.00 58.83 ? 366 NAG A O1 1 HETATM 2927 O O3 . NAG E 2 . ? 10.240 -3.974 37.156 1.00 58.28 ? 366 NAG A O3 1 HETATM 2928 O O4 . NAG E 2 . ? 10.392 -6.448 38.377 1.00 59.67 ? 366 NAG A O4 1 HETATM 2929 O O5 . NAG E 2 . ? 9.568 -4.383 41.311 1.00 59.36 ? 366 NAG A O5 1 HETATM 2930 O O6 . NAG E 2 . ? 9.579 -6.936 42.458 1.00 56.46 ? 366 NAG A O6 1 HETATM 2931 O O7 . NAG E 2 . ? 11.045 -0.472 38.948 1.00 54.63 ? 366 NAG A O7 1 HETATM 2932 C C1 . NAG F 2 . ? 11.688 -6.610 37.940 1.00 59.49 ? 367 NAG A C1 1 HETATM 2933 C C2 . NAG F 2 . ? 12.285 -7.938 38.428 1.00 59.50 ? 367 NAG A C2 1 HETATM 2934 C C3 . NAG F 2 . ? 13.675 -8.176 37.787 1.00 59.28 ? 367 NAG A C3 1 HETATM 2935 C C4 . NAG F 2 . ? 13.692 -7.859 36.268 1.00 59.23 ? 367 NAG A C4 1 HETATM 2936 C C5 . NAG F 2 . ? 13.059 -6.478 36.063 1.00 59.62 ? 367 NAG A C5 1 HETATM 2937 C C6 . NAG F 2 . ? 13.043 -5.895 34.671 1.00 59.12 ? 367 NAG A C6 1 HETATM 2938 C C7 . NAG F 2 . ? 12.382 -8.938 40.637 1.00 61.76 ? 367 NAG A C7 1 HETATM 2939 C C8 . NAG F 2 . ? 12.942 -8.813 42.051 1.00 59.23 ? 367 NAG A C8 1 HETATM 2940 N N2 . NAG F 2 . ? 12.426 -7.851 39.872 1.00 60.70 ? 367 NAG A N2 1 HETATM 2941 O O3 . NAG F 2 . ? 14.073 -9.523 37.996 1.00 60.80 ? 367 NAG A O3 1 HETATM 2942 O O4 . NAG F 2 . ? 15.050 -7.863 35.762 1.00 59.46 ? 367 NAG A O4 1 HETATM 2943 O O5 . NAG F 2 . ? 11.709 -6.517 36.525 1.00 60.13 ? 367 NAG A O5 1 HETATM 2944 O O6 . NAG F 2 . ? 11.755 -6.016 34.082 1.00 59.18 ? 367 NAG A O6 1 HETATM 2945 O O7 . NAG F 2 . ? 11.919 -10.011 40.253 1.00 61.91 ? 367 NAG A O7 1 HETATM 2946 C C1 . NAG G 2 . ? 15.578 -9.090 35.374 1.00 58.49 ? 368 NAG A C1 1 HETATM 2947 C C2 . NAG G 2 . ? 16.439 -8.923 34.111 1.00 58.44 ? 368 NAG A C2 1 HETATM 2948 C C3 . NAG G 2 . ? 17.209 -10.229 33.797 1.00 58.32 ? 368 NAG A C3 1 HETATM 2949 C C4 . NAG G 2 . ? 17.905 -10.830 35.032 1.00 58.10 ? 368 NAG A C4 1 HETATM 2950 C C5 . NAG G 2 . ? 16.924 -10.883 36.205 1.00 58.14 ? 368 NAG A C5 1 HETATM 2951 C C6 . NAG G 2 . ? 17.603 -11.344 37.490 1.00 59.00 ? 368 NAG A C6 1 HETATM 2952 C C7 . NAG G 2 . ? 15.396 -7.361 32.572 1.00 61.72 ? 368 NAG A C7 1 HETATM 2953 C C8 . NAG G 2 . ? 13.952 -6.947 32.337 1.00 60.06 ? 368 NAG A C8 1 HETATM 2954 N N2 . NAG G 2 . ? 15.588 -8.614 32.977 1.00 60.30 ? 368 NAG A N2 1 HETATM 2955 O O3 . NAG G 2 . ? 18.178 -9.989 32.782 1.00 60.05 ? 368 NAG A O3 1 HETATM 2956 O O4 . NAG G 2 . ? 18.365 -12.172 34.734 1.00 59.32 ? 368 NAG A O4 1 HETATM 2957 O O5 . NAG G 2 . ? 16.390 -9.567 36.451 1.00 57.84 ? 368 NAG A O5 1 HETATM 2958 O O6 . NAG G 2 . ? 16.662 -11.663 38.514 1.00 60.62 ? 368 NAG A O6 1 HETATM 2959 O O7 . NAG G 2 . ? 16.314 -6.562 32.360 1.00 61.85 ? 368 NAG A O7 1 HETATM 2960 C C1 . NAG H 2 . ? 19.740 -12.360 34.671 1.00 58.43 ? 369 NAG A C1 1 HETATM 2961 C C2 . NAG H 2 . ? 20.139 -13.649 35.377 1.00 59.02 ? 369 NAG A C2 1 HETATM 2962 C C3 . NAG H 2 . ? 21.656 -13.737 35.347 1.00 58.85 ? 369 NAG A C3 1 HETATM 2963 C C4 . NAG H 2 . ? 22.177 -13.691 33.901 1.00 59.33 ? 369 NAG A C4 1 HETATM 2964 C C5 . NAG H 2 . ? 21.555 -12.521 33.105 1.00 59.11 ? 369 NAG A C5 1 HETATM 2965 C C6 . NAG H 2 . ? 21.785 -12.710 31.616 1.00 60.05 ? 369 NAG A C6 1 HETATM 2966 C C7 . NAG H 2 . ? 19.144 -14.797 37.241 1.00 60.14 ? 369 NAG A C7 1 HETATM 2967 C C8 . NAG H 2 . ? 17.678 -14.793 37.654 1.00 58.58 ? 369 NAG A C8 1 HETATM 2968 N N2 . NAG H 2 . ? 19.654 -13.672 36.745 1.00 59.65 ? 369 NAG A N2 1 HETATM 2969 O O3 . NAG H 2 . ? 22.078 -14.935 35.980 1.00 59.07 ? 369 NAG A O3 1 HETATM 2970 O O4 . NAG H 2 . ? 23.597 -13.552 33.913 1.00 60.51 ? 369 NAG A O4 1 HETATM 2971 O O5 . NAG H 2 . ? 20.118 -12.453 33.294 1.00 59.08 ? 369 NAG A O5 1 HETATM 2972 O O6 . NAG H 2 . ? 20.919 -11.885 30.845 1.00 62.25 ? 369 NAG A O6 1 HETATM 2973 O O7 . NAG H 2 . ? 19.808 -15.827 37.363 1.00 60.95 ? 369 NAG A O7 1 HETATM 2974 O O . HOH I 5 . ? 18.487 15.448 54.973 1.00 57.05 ? 370 HOH A O 1 HETATM 2975 O O . HOH I 5 . ? 14.496 -0.346 38.786 1.00 29.09 ? 371 HOH A O 1 HETATM 2976 O O . HOH I 5 . ? 15.483 -8.738 43.795 1.00 24.12 ? 372 HOH A O 1 HETATM 2977 O O . HOH I 5 . ? 19.201 2.087 35.188 1.00 22.40 ? 373 HOH A O 1 HETATM 2978 O O . HOH I 5 . ? 24.845 3.151 26.241 1.00 44.23 ? 374 HOH A O 1 HETATM 2979 O O . HOH I 5 . ? 10.707 0.422 29.428 1.00 25.90 ? 375 HOH A O 1 HETATM 2980 O O . HOH I 5 . ? 29.365 7.977 36.042 1.00 70.41 ? 376 HOH A O 1 HETATM 2981 O O . HOH I 5 . ? 29.936 3.160 38.283 1.00 79.98 ? 377 HOH A O 1 HETATM 2982 O O . HOH I 5 . ? 32.391 6.099 46.815 1.00 48.70 ? 378 HOH A O 1 HETATM 2983 O O . HOH I 5 . ? 24.841 14.944 47.633 1.00 40.88 ? 379 HOH A O 1 HETATM 2984 O O . HOH I 5 . ? 26.803 8.335 39.753 1.00 37.93 ? 380 HOH A O 1 HETATM 2985 O O . HOH I 5 . ? 23.535 8.159 49.903 1.00 18.86 ? 381 HOH A O 1 HETATM 2986 O O . HOH I 5 . ? 23.812 11.059 54.564 1.00 48.52 ? 382 HOH A O 1 HETATM 2987 O O . HOH I 5 . ? 17.530 5.910 61.282 1.00 33.53 ? 383 HOH A O 1 HETATM 2988 O O . HOH I 5 . ? 25.022 16.312 53.111 1.00 49.66 ? 384 HOH A O 1 HETATM 2989 O O . HOH I 5 . ? 19.107 -9.727 48.004 1.00 27.71 ? 385 HOH A O 1 HETATM 2990 O O . HOH I 5 . ? 7.785 -23.231 53.060 1.00 60.86 ? 386 HOH A O 1 HETATM 2991 O O . HOH I 5 . ? 13.198 18.917 35.447 1.00 41.36 ? 387 HOH A O 1 HETATM 2992 O O . HOH I 5 . ? 28.473 -9.441 51.514 1.00 46.53 ? 388 HOH A O 1 HETATM 2993 O O . HOH I 5 . ? 26.128 4.290 59.989 1.00 48.03 ? 389 HOH A O 1 HETATM 2994 O O . HOH I 5 . ? 5.213 -8.935 48.213 1.00 27.99 ? 390 HOH A O 1 HETATM 2995 O O . HOH I 5 . ? 20.116 -16.429 58.721 1.00 32.06 ? 391 HOH A O 1 HETATM 2996 O O . HOH I 5 . ? 1.540 12.833 64.264 1.00 43.89 ? 392 HOH A O 1 HETATM 2997 O O . HOH I 5 . ? -13.405 15.989 43.545 1.00 85.19 ? 393 HOH A O 1 HETATM 2998 O O . HOH I 5 . ? -1.218 -11.428 51.005 1.00 33.50 ? 394 HOH A O 1 HETATM 2999 O O . HOH I 5 . ? 15.761 -19.676 61.761 1.00 35.84 ? 395 HOH A O 1 HETATM 3000 O O . HOH I 5 . ? 24.920 -4.638 60.989 1.00 27.02 ? 396 HOH A O 1 HETATM 3001 O O . HOH I 5 . ? 5.271 -4.505 53.834 1.00 30.11 ? 397 HOH A O 1 HETATM 3002 O O . HOH I 5 . ? 2.967 -3.383 52.526 1.00 30.30 ? 398 HOH A O 1 HETATM 3003 O O . HOH I 5 . ? 0.326 2.831 46.547 1.00 30.40 ? 399 HOH A O 1 HETATM 3004 O O . HOH I 5 . ? -1.577 -5.087 60.262 1.00 24.14 ? 400 HOH A O 1 HETATM 3005 O O . HOH I 5 . ? -3.891 -5.990 63.956 1.00 36.13 ? 401 HOH A O 1 HETATM 3006 O O . HOH I 5 . ? -6.669 -10.389 59.513 1.00 44.15 ? 402 HOH A O 1 HETATM 3007 O O . HOH I 5 . ? 18.989 -5.548 66.827 1.00 25.70 ? 403 HOH A O 1 HETATM 3008 O O . HOH I 5 . ? 22.856 -2.229 71.929 1.00 38.24 ? 404 HOH A O 1 HETATM 3009 O O . HOH I 5 . ? 16.547 24.523 45.592 1.00 69.17 ? 405 HOH A O 1 HETATM 3010 O O . HOH I 5 . ? 23.165 -1.512 63.045 1.00 48.21 ? 406 HOH A O 1 HETATM 3011 O O . HOH I 5 . ? -8.271 2.835 46.714 1.00 30.11 ? 407 HOH A O 1 HETATM 3012 O O . HOH I 5 . ? -5.491 -1.199 66.513 1.00 66.75 ? 408 HOH A O 1 HETATM 3013 O O . HOH I 5 . ? -6.753 0.870 47.210 1.00 42.11 ? 409 HOH A O 1 HETATM 3014 O O . HOH I 5 . ? -5.820 0.604 60.556 1.00 47.53 ? 410 HOH A O 1 HETATM 3015 O O . HOH I 5 . ? 8.318 4.254 68.593 1.00 56.02 ? 411 HOH A O 1 HETATM 3016 O O . HOH I 5 . ? 8.530 -5.339 71.924 1.00 68.59 ? 412 HOH A O 1 HETATM 3017 O O . HOH I 5 . ? 6.583 8.438 66.941 1.00 47.93 ? 413 HOH A O 1 HETATM 3018 O O . HOH I 5 . ? 4.777 11.343 44.903 1.00 25.31 ? 414 HOH A O 1 HETATM 3019 O O . HOH I 5 . ? 9.893 11.090 36.625 1.00 27.81 ? 415 HOH A O 1 HETATM 3020 O O . HOH I 5 . ? 6.400 10.010 37.991 1.00 22.69 ? 416 HOH A O 1 HETATM 3021 O O . HOH I 5 . ? 4.979 20.696 39.669 1.00 38.14 ? 417 HOH A O 1 HETATM 3022 O O . HOH I 5 . ? 6.747 5.054 25.546 1.00 29.78 ? 418 HOH A O 1 HETATM 3023 O O . HOH I 5 . ? 7.246 2.375 28.512 1.00 26.23 ? 419 HOH A O 1 HETATM 3024 O O . HOH I 5 . ? -7.592 14.857 19.164 1.00 53.93 ? 420 HOH A O 1 HETATM 3025 O O . HOH I 5 . ? -3.458 16.611 19.519 1.00 62.05 ? 421 HOH A O 1 HETATM 3026 O O . HOH I 5 . ? -7.875 19.455 27.457 1.00 75.01 ? 422 HOH A O 1 HETATM 3027 O O . HOH I 5 . ? -4.927 23.812 24.618 1.00 70.05 ? 423 HOH A O 1 HETATM 3028 O O . HOH I 5 . ? 2.188 15.711 19.287 1.00 93.08 ? 424 HOH A O 1 HETATM 3029 O O . HOH I 5 . ? 7.444 -5.845 29.258 1.00 71.49 ? 425 HOH A O 1 HETATM 3030 O O . HOH I 5 . ? 4.026 17.947 42.740 1.00 31.58 ? 426 HOH A O 1 HETATM 3031 O O . HOH I 5 . ? 23.034 19.192 46.017 1.00 82.96 ? 427 HOH A O 1 HETATM 3032 O O . HOH I 5 . ? 9.556 18.582 32.441 1.00 34.04 ? 428 HOH A O 1 HETATM 3033 O O . HOH I 5 . ? 3.667 22.046 48.057 1.00 42.03 ? 429 HOH A O 1 HETATM 3034 O O . HOH I 5 . ? -0.425 18.081 59.072 1.00 41.23 ? 430 HOH A O 1 HETATM 3035 O O . HOH I 5 . ? 15.613 14.209 60.687 1.00 61.50 ? 431 HOH A O 1 HETATM 3036 O O . HOH I 5 . ? 6.524 -14.712 40.529 1.00 66.13 ? 432 HOH A O 1 HETATM 3037 O O . HOH I 5 . ? 27.168 1.702 37.547 1.00 35.46 ? 433 HOH A O 1 HETATM 3038 O O . HOH I 5 . ? 10.301 -8.875 44.244 1.00 35.25 ? 434 HOH A O 1 HETATM 3039 O O . HOH I 5 . ? 18.840 -9.495 44.534 1.00 49.72 ? 435 HOH A O 1 HETATM 3040 O O . HOH I 5 . ? 18.175 -14.283 65.863 1.00 39.32 ? 436 HOH A O 1 HETATM 3041 O O . HOH I 5 . ? -7.517 -1.527 62.015 1.00 53.51 ? 437 HOH A O 1 HETATM 3042 O O . HOH I 5 . ? -12.953 0.741 52.983 1.00 48.68 ? 438 HOH A O 1 HETATM 3043 O O . HOH I 5 . ? 2.720 -3.802 72.058 1.00 71.81 ? 439 HOH A O 1 HETATM 3044 O O . HOH I 5 . ? -0.295 3.380 38.366 1.00 55.33 ? 440 HOH A O 1 HETATM 3045 O O . HOH I 5 . ? -0.175 7.098 35.043 1.00 36.40 ? 441 HOH A O 1 HETATM 3046 O O . HOH I 5 . ? -7.558 11.960 43.226 1.00 40.42 ? 442 HOH A O 1 HETATM 3047 O O . HOH I 5 . ? -4.006 -1.369 39.267 1.00 75.74 ? 443 HOH A O 1 HETATM 3048 O O . HOH I 5 . ? -6.005 25.026 39.904 1.00 77.84 ? 444 HOH A O 1 HETATM 3049 O O . HOH I 5 . ? 10.958 8.734 65.275 1.00 51.38 ? 445 HOH A O 1 HETATM 3050 O O . HOH I 5 . ? -1.063 10.705 63.567 1.00 38.25 ? 446 HOH A O 1 HETATM 3051 O O . HOH I 5 . ? 7.443 24.393 27.294 1.00 64.81 ? 447 HOH A O 1 HETATM 3052 O O . HOH I 5 . ? 4.055 14.300 17.835 1.00 51.37 ? 448 HOH A O 1 HETATM 3053 O O . HOH I 5 . ? 23.714 6.521 25.852 1.00 56.41 ? 449 HOH A O 1 HETATM 3054 O O . HOH I 5 . ? 18.769 -2.743 29.129 1.00 45.54 ? 450 HOH A O 1 HETATM 3055 O O . HOH I 5 . ? 8.569 -6.082 32.886 1.00 79.44 ? 451 HOH A O 1 HETATM 3056 O O . HOH I 5 . ? 30.134 5.914 38.609 1.00 72.93 ? 452 HOH A O 1 HETATM 3057 O O . HOH I 5 . ? 30.155 8.527 40.188 1.00 88.43 ? 453 HOH A O 1 HETATM 3058 O O . HOH I 5 . ? 29.707 -3.897 42.247 1.00 53.63 ? 454 HOH A O 1 HETATM 3059 O O . HOH I 5 . ? 26.083 16.585 49.935 1.00 46.46 ? 455 HOH A O 1 HETATM 3060 O O . HOH I 5 . ? 21.565 8.223 58.205 1.00 38.58 ? 456 HOH A O 1 HETATM 3061 O O . HOH I 5 . ? 14.941 -0.314 65.805 1.00 31.17 ? 457 HOH A O 1 HETATM 3062 O O . HOH I 5 . ? 16.828 20.831 57.880 1.00 71.83 ? 458 HOH A O 1 HETATM 3063 O O . HOH I 5 . ? 11.487 -23.061 50.398 1.00 61.13 ? 459 HOH A O 1 HETATM 3064 O O . HOH I 5 . ? 28.566 -6.717 52.988 1.00 42.00 ? 460 HOH A O 1 HETATM 3065 O O . HOH I 5 . ? 9.329 -15.032 41.569 1.00 73.27 ? 461 HOH A O 1 HETATM 3066 O O . HOH I 5 . ? 25.305 -2.218 61.137 1.00 54.95 ? 462 HOH A O 1 HETATM 3067 O O . HOH I 5 . ? 19.452 -18.037 63.494 1.00 58.39 ? 463 HOH A O 1 HETATM 3068 O O . HOH I 5 . ? 1.261 16.895 60.856 1.00 39.13 ? 464 HOH A O 1 HETATM 3069 O O . HOH I 5 . ? -4.883 -13.065 51.706 1.00 67.07 ? 465 HOH A O 1 HETATM 3070 O O . HOH I 5 . ? -8.334 -9.068 50.443 1.00 53.62 ? 466 HOH A O 1 HETATM 3071 O O . HOH I 5 . ? 21.095 0.308 70.060 1.00 46.86 ? 467 HOH A O 1 HETATM 3072 O O . HOH I 5 . ? -0.603 -0.840 40.342 1.00 66.48 ? 468 HOH A O 1 HETATM 3073 O O . HOH I 5 . ? -7.414 -14.154 59.526 1.00 63.99 ? 469 HOH A O 1 HETATM 3074 O O . HOH I 5 . ? 8.943 6.052 23.799 1.00 33.28 ? 470 HOH A O 1 HETATM 3075 O O . HOH I 5 . ? 11.787 19.343 25.734 1.00 67.50 ? 471 HOH A O 1 HETATM 3076 O O . HOH I 5 . ? -5.895 6.468 48.637 1.00 40.04 ? 472 HOH A O 1 HETATM 3077 O O . HOH I 5 . ? 7.679 -5.561 69.458 1.00 38.68 ? 473 HOH A O 1 HETATM 3078 O O . HOH I 5 . ? -2.383 22.304 23.640 1.00 53.38 ? 474 HOH A O 1 HETATM 3079 O O . HOH I 5 . ? 11.273 21.046 36.373 1.00 47.51 ? 475 HOH A O 1 HETATM 3080 O O . HOH I 5 . ? 8.795 23.575 42.762 1.00 47.45 ? 476 HOH A O 1 HETATM 3081 O O . HOH I 5 . ? -3.237 26.996 34.389 1.00 77.41 ? 477 HOH A O 1 HETATM 3082 O O . HOH I 5 . ? 15.071 5.338 22.395 1.00 37.03 ? 478 HOH A O 1 HETATM 3083 O O . HOH I 5 . ? 6.014 23.627 32.037 1.00 78.62 ? 479 HOH A O 1 HETATM 3084 O O . HOH I 5 . ? 5.923 21.048 32.086 1.00 57.80 ? 480 HOH A O 1 HETATM 3085 O O . HOH I 5 . ? 26.055 -3.851 31.101 1.00 70.42 ? 481 HOH A O 1 HETATM 3086 O O . HOH I 5 . ? 7.985 23.569 56.618 1.00 64.61 ? 482 HOH A O 1 HETATM 3087 O O . HOH I 5 . ? 26.352 -8.030 36.024 1.00 45.63 ? 483 HOH A O 1 HETATM 3088 O O . HOH I 5 . ? -4.302 -1.704 29.090 1.00 65.32 ? 484 HOH A O 1 HETATM 3089 O O . HOH I 5 . ? 10.372 -10.730 36.114 1.00 72.57 ? 485 HOH A O 1 HETATM 3090 O O . HOH I 5 . ? 12.994 12.299 60.202 1.00 36.60 ? 486 HOH A O 1 HETATM 3091 O O . HOH I 5 . ? -3.406 -7.537 66.173 1.00 47.53 ? 487 HOH A O 1 HETATM 3092 O O . HOH I 5 . ? -11.441 -0.582 40.758 1.00 84.53 ? 488 HOH A O 1 HETATM 3093 O O . HOH I 5 . ? -2.248 2.536 35.908 1.00 69.55 ? 489 HOH A O 1 HETATM 3094 O O . HOH I 5 . ? -2.845 3.894 18.632 1.00 51.03 ? 490 HOH A O 1 HETATM 3095 O O . HOH I 5 . ? -13.014 7.871 27.300 1.00 68.94 ? 491 HOH A O 1 HETATM 3096 O O . HOH I 5 . ? 1.398 13.938 16.540 1.00 75.01 ? 492 HOH A O 1 HETATM 3097 O O . HOH I 5 . ? 24.113 15.349 42.900 1.00 54.23 ? 493 HOH A O 1 HETATM 3098 O O . HOH I 5 . ? 17.069 -17.347 47.259 1.00 42.76 ? 494 HOH A O 1 HETATM 3099 O O . HOH I 5 . ? 14.797 -21.329 63.749 1.00 70.98 ? 495 HOH A O 1 HETATM 3100 O O . HOH I 5 . ? 32.334 -6.424 46.654 1.00 50.80 ? 496 HOH A O 1 HETATM 3101 O O . HOH I 5 . ? 26.562 12.724 56.787 1.00 54.71 ? 497 HOH A O 1 HETATM 3102 O O . HOH I 5 . ? 19.871 -18.648 60.844 1.00 53.92 ? 498 HOH A O 1 HETATM 3103 O O . HOH I 5 . ? -7.561 -12.562 52.015 1.00 62.40 ? 499 HOH A O 1 HETATM 3104 O O . HOH I 5 . ? -7.867 9.422 36.011 1.00 81.65 ? 500 HOH A O 1 HETATM 3105 O O . HOH I 5 . ? 29.845 5.524 62.568 1.00 59.96 ? 501 HOH A O 1 HETATM 3106 O O . HOH I 5 . ? 25.108 -15.473 64.492 1.00 64.81 ? 502 HOH A O 1 HETATM 3107 O O . HOH I 5 . ? 22.784 -11.414 65.345 1.00 41.92 ? 503 HOH A O 1 HETATM 3108 O O . HOH I 5 . ? 14.882 13.464 64.020 1.00 70.19 ? 504 HOH A O 1 HETATM 3109 O O . HOH I 5 . ? 25.078 -12.569 64.399 1.00 50.35 ? 505 HOH A O 1 HETATM 3110 O O . HOH I 5 . ? 10.128 -12.244 68.709 1.00 33.61 ? 506 HOH A O 1 HETATM 3111 O O . HOH I 5 . ? 25.218 13.388 44.169 1.00 61.72 ? 507 HOH A O 1 HETATM 3112 O O . HOH I 5 . ? 28.015 14.568 43.976 1.00 65.01 ? 508 HOH A O 1 HETATM 3113 O O . HOH I 5 . ? 28.502 15.143 47.446 1.00 88.22 ? 509 HOH A O 1 HETATM 3114 O O . HOH I 5 . ? 15.190 16.663 27.964 1.00 55.44 ? 510 HOH A O 1 HETATM 3115 O O . HOH I 5 . ? -0.548 4.986 44.837 1.00 51.55 ? 511 HOH A O 1 HETATM 3116 O O . HOH I 5 . ? 12.449 17.296 32.749 1.00 42.98 ? 512 HOH A O 1 HETATM 3117 O O . HOH I 5 . ? -3.229 7.089 17.656 1.00 61.80 ? 513 HOH A O 1 HETATM 3118 O O . HOH I 5 . ? -2.319 10.209 16.746 1.00 66.99 ? 514 HOH A O 1 HETATM 3119 O O . HOH I 5 . ? 33.434 5.924 43.410 1.00 70.22 ? 515 HOH A O 1 HETATM 3120 O O . HOH I 5 . ? -6.473 -16.781 59.775 1.00 56.20 ? 516 HOH A O 1 HETATM 3121 O O . HOH I 5 . ? -7.978 11.874 54.106 1.00 42.31 ? 517 HOH A O 1 HETATM 3122 O O . HOH I 5 . ? -4.757 10.473 64.982 1.00 49.86 ? 518 HOH A O 1 HETATM 3123 O O . HOH I 5 . ? 28.179 -7.889 69.614 1.00 49.73 ? 519 HOH A O 1 HETATM 3124 O O . HOH I 5 . ? 23.317 8.031 61.243 1.00 59.31 ? 520 HOH A O 1 HETATM 3125 O O . HOH I 5 . ? 21.689 10.626 62.201 1.00 67.26 ? 521 HOH A O 1 HETATM 3126 O O . HOH I 5 . ? -8.583 14.303 53.312 1.00 64.76 ? 522 HOH A O 1 HETATM 3127 O O . HOH I 5 . ? -7.236 -1.654 27.813 1.00 76.43 ? 523 HOH A O 1 HETATM 3128 O O . HOH I 5 . ? 34.751 2.837 40.593 1.00 71.33 ? 524 HOH A O 1 HETATM 3129 O O . HOH I 5 . ? 12.177 -8.548 73.010 1.00 43.72 ? 525 HOH A O 1 HETATM 3130 O O . HOH I 5 . ? 35.439 4.438 42.570 1.00 87.60 ? 526 HOH A O 1 HETATM 3131 O O . HOH I 5 . ? 2.058 -11.620 68.296 1.00 52.08 ? 527 HOH A O 1 HETATM 3132 O O . HOH I 5 . ? 8.879 -0.883 47.594 1.00 58.17 ? 528 HOH A O 1 HETATM 3133 O O . HOH I 5 . ? 10.670 1.670 53.343 1.00 27.52 ? 529 HOH A O 1 HETATM 3134 O O . HOH I 5 . ? 22.071 8.219 34.108 1.00 40.03 ? 530 HOH A O 1 HETATM 3135 O O . HOH I 5 . ? 29.132 21.447 29.020 1.00 69.46 ? 531 HOH A O 1 HETATM 3136 O O . HOH I 5 . ? 2.617 -23.040 63.780 1.00 48.74 ? 532 HOH A O 1 HETATM 3137 O O . HOH I 5 . ? 16.490 -22.043 53.283 1.00 60.94 ? 533 HOH A O 1 HETATM 3138 O O . HOH I 5 . ? 0.850 -21.685 43.992 1.00 74.48 ? 534 HOH A O 1 HETATM 3139 O O . HOH I 5 . ? 6.363 -23.729 66.232 1.00 65.95 ? 535 HOH A O 1 HETATM 3140 O O . HOH I 5 . ? 4.948 13.119 64.865 1.00 51.26 ? 536 HOH A O 1 HETATM 3141 O O . HOH I 5 . ? -0.071 -20.959 64.432 1.00 46.46 ? 537 HOH A O 1 HETATM 3142 O O . HOH I 5 . ? 20.862 -0.191 63.027 1.00 31.47 ? 538 HOH A O 1 HETATM 3143 O O . HOH I 5 . ? 3.781 -8.995 44.875 1.00 57.95 ? 539 HOH A O 1 HETATM 3144 O O . HOH I 5 . ? 16.722 1.765 66.471 1.00 76.59 ? 540 HOH A O 1 HETATM 3145 O O . HOH I 5 . ? -4.119 -4.516 50.883 1.00 53.64 ? 541 HOH A O 1 HETATM 3146 O O . HOH I 5 . ? 1.212 0.757 45.534 1.00 57.47 ? 542 HOH A O 1 HETATM 3147 O O . HOH I 5 . ? 19.123 23.928 49.811 1.00 53.09 ? 543 HOH A O 1 HETATM 3148 O O . HOH I 5 . ? 21.422 15.603 34.511 1.00 44.22 ? 544 HOH A O 1 HETATM 3149 O O . HOH I 5 . ? -5.572 16.384 21.469 1.00 64.03 ? 545 HOH A O 1 HETATM 3150 O O . HOH I 5 . ? 13.677 4.976 24.920 1.00 34.05 ? 546 HOH A O 1 HETATM 3151 O O . HOH I 5 . ? 7.420 15.488 62.973 1.00 60.99 ? 547 HOH A O 1 HETATM 3152 O O . HOH I 5 . ? 11.003 8.007 61.518 1.00 36.80 ? 548 HOH A O 1 HETATM 3153 O O . HOH I 5 . ? -0.141 8.818 66.847 1.00 57.49 ? 549 HOH A O 1 HETATM 3154 O O . HOH I 5 . ? 14.509 -3.416 33.821 1.00 57.37 ? 550 HOH A O 1 HETATM 3155 O O . HOH I 5 . ? -2.551 17.913 26.022 1.00 66.57 ? 551 HOH A O 1 HETATM 3156 O O . HOH I 5 . ? 13.276 -1.718 24.265 1.00 53.35 ? 552 HOH A O 1 HETATM 3157 O O . HOH I 5 . ? 31.503 22.288 29.022 1.00 67.89 ? 553 HOH A O 1 HETATM 3158 O O . HOH I 5 . ? -14.380 10.445 25.856 1.00 74.32 ? 554 HOH A O 1 HETATM 3159 O O . HOH I 5 . ? 2.851 22.752 51.080 1.00 52.81 ? 555 HOH A O 1 HETATM 3160 O O . HOH I 5 . ? 13.342 7.459 63.478 1.00 60.87 ? 556 HOH A O 1 HETATM 3161 O O . HOH I 5 . ? 10.409 -20.264 52.294 1.00 39.03 ? 557 HOH A O 1 HETATM 3162 O O . HOH I 5 . ? 20.854 -14.135 39.217 1.00 55.75 ? 558 HOH A O 1 HETATM 3163 O O . HOH I 5 . ? 21.913 5.075 67.459 1.00 69.95 ? 559 HOH A O 1 HETATM 3164 O O . HOH I 5 . ? 12.545 0.769 70.578 1.00 53.49 ? 560 HOH A O 1 HETATM 3165 O O . HOH I 5 . ? -8.588 -15.994 57.533 1.00 76.98 ? 561 HOH A O 1 HETATM 3166 O O . HOH I 5 . ? 10.866 4.391 23.863 1.00 38.56 ? 562 HOH A O 1 HETATM 3167 O O . HOH I 5 . ? 4.412 23.494 27.846 1.00 73.61 ? 563 HOH A O 1 HETATM 3168 O O . HOH I 5 . ? 17.266 -1.698 23.469 1.00 51.29 ? 564 HOH A O 1 HETATM 3169 O O . HOH I 5 . ? 5.918 26.032 51.362 1.00 53.28 ? 565 HOH A O 1 HETATM 3170 O O . HOH I 5 . ? 3.291 0.698 34.849 1.00 67.08 ? 566 HOH A O 1 HETATM 3171 O O . HOH I 5 . ? 26.054 -12.815 62.003 1.00 45.66 ? 567 HOH A O 1 HETATM 3172 O O . HOH I 5 . ? 28.502 -11.075 61.856 1.00 58.33 ? 568 HOH A O 1 HETATM 3173 O O . HOH I 5 . ? 19.181 1.707 66.201 1.00 42.14 ? 569 HOH A O 1 HETATM 3174 O O . HOH I 5 . ? 11.320 5.254 69.190 1.00 76.76 ? 570 HOH A O 1 HETATM 3175 O O . HOH I 5 . ? -6.315 8.900 22.752 1.00 49.53 ? 571 HOH A O 1 HETATM 3176 O O . HOH I 5 . ? 3.312 -20.003 43.550 1.00 74.19 ? 572 HOH A O 1 HETATM 3177 O O . HOH I 5 . ? -9.734 -5.932 46.048 1.00 83.46 ? 573 HOH A O 1 HETATM 3178 O O . HOH I 5 . ? 4.110 -13.063 69.641 1.00 69.19 ? 574 HOH A O 1 HETATM 3179 O O . HOH I 5 . ? -5.473 18.369 19.109 1.00 72.71 ? 575 HOH A O 1 HETATM 3180 O O . HOH I 5 . ? -8.522 1.200 43.695 1.00 63.94 ? 576 HOH A O 1 HETATM 3181 O O . HOH I 5 . ? 32.401 -5.578 53.760 1.00 72.63 ? 577 HOH A O 1 HETATM 3182 O O . HOH I 5 . ? -11.141 -4.767 44.274 1.00 76.31 ? 578 HOH A O 1 HETATM 3183 O O . HOH I 5 . ? -9.264 -2.739 44.618 1.00 74.20 ? 579 HOH A O 1 HETATM 3184 O O . HOH I 5 . ? 8.191 0.450 45.752 1.00 56.55 ? 580 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 4 BMA 3 365 3 BMA MAN A . E 2 NAG 1 366 1 NAG NAG A . F 2 NAG 2 367 2 NAG NAG A . G 2 NAG 3 368 3 NAG NAG A . H 2 NAG 4 369 4 NAG NAG A . I 5 HOH 1 370 1 HOH HOH A . I 5 HOH 2 371 2 HOH HOH A . I 5 HOH 3 372 3 HOH HOH A . I 5 HOH 4 373 4 HOH HOH A . I 5 HOH 5 374 5 HOH HOH A . I 5 HOH 6 375 6 HOH HOH A . I 5 HOH 7 376 7 HOH HOH A . I 5 HOH 8 377 8 HOH HOH A . I 5 HOH 9 378 9 HOH HOH A . I 5 HOH 10 379 10 HOH HOH A . I 5 HOH 11 380 11 HOH HOH A . I 5 HOH 12 381 12 HOH HOH A . I 5 HOH 13 382 13 HOH HOH A . I 5 HOH 14 383 14 HOH HOH A . I 5 HOH 15 384 15 HOH HOH A . I 5 HOH 16 385 16 HOH HOH A . I 5 HOH 17 386 17 HOH HOH A . I 5 HOH 18 387 18 HOH HOH A . I 5 HOH 19 388 19 HOH HOH A . I 5 HOH 20 389 20 HOH HOH A . I 5 HOH 21 390 21 HOH HOH A . I 5 HOH 22 391 22 HOH HOH A . I 5 HOH 23 392 23 HOH HOH A . I 5 HOH 24 393 24 HOH HOH A . I 5 HOH 25 394 25 HOH HOH A . I 5 HOH 26 395 26 HOH HOH A . I 5 HOH 27 396 27 HOH HOH A . I 5 HOH 28 397 28 HOH HOH A . I 5 HOH 29 398 29 HOH HOH A . I 5 HOH 30 399 30 HOH HOH A . I 5 HOH 31 400 31 HOH HOH A . I 5 HOH 32 401 32 HOH HOH A . I 5 HOH 33 402 33 HOH HOH A . I 5 HOH 34 403 34 HOH HOH A . I 5 HOH 35 404 35 HOH HOH A . I 5 HOH 36 405 36 HOH HOH A . I 5 HOH 37 406 37 HOH HOH A . I 5 HOH 38 407 38 HOH HOH A . I 5 HOH 39 408 39 HOH HOH A . I 5 HOH 40 409 40 HOH HOH A . I 5 HOH 41 410 41 HOH HOH A . I 5 HOH 42 411 42 HOH HOH A . I 5 HOH 43 412 43 HOH HOH A . I 5 HOH 44 413 44 HOH HOH A . I 5 HOH 45 414 45 HOH HOH A . I 5 HOH 46 415 46 HOH HOH A . I 5 HOH 47 416 47 HOH HOH A . I 5 HOH 48 417 48 HOH HOH A . I 5 HOH 49 418 49 HOH HOH A . I 5 HOH 50 419 50 HOH HOH A . I 5 HOH 51 420 51 HOH HOH A . I 5 HOH 52 421 52 HOH HOH A . I 5 HOH 53 422 53 HOH HOH A . I 5 HOH 54 423 54 HOH HOH A . I 5 HOH 55 424 55 HOH HOH A . I 5 HOH 56 425 56 HOH HOH A . I 5 HOH 57 426 57 HOH HOH A . I 5 HOH 58 427 58 HOH HOH A . I 5 HOH 59 428 59 HOH HOH A . I 5 HOH 60 429 60 HOH HOH A . I 5 HOH 61 430 61 HOH HOH A . I 5 HOH 62 431 62 HOH HOH A . I 5 HOH 63 432 63 HOH HOH A . I 5 HOH 64 433 64 HOH HOH A . I 5 HOH 65 434 65 HOH HOH A . I 5 HOH 66 435 66 HOH HOH A . I 5 HOH 67 436 67 HOH HOH A . I 5 HOH 68 437 68 HOH HOH A . I 5 HOH 69 438 69 HOH HOH A . I 5 HOH 70 439 70 HOH HOH A . I 5 HOH 71 440 71 HOH HOH A . I 5 HOH 72 441 72 HOH HOH A . I 5 HOH 73 442 73 HOH HOH A . I 5 HOH 74 443 74 HOH HOH A . I 5 HOH 75 444 75 HOH HOH A . I 5 HOH 76 445 76 HOH HOH A . I 5 HOH 77 446 77 HOH HOH A . I 5 HOH 78 447 78 HOH HOH A . I 5 HOH 79 448 79 HOH HOH A . I 5 HOH 80 449 80 HOH HOH A . I 5 HOH 81 450 81 HOH HOH A . I 5 HOH 82 451 82 HOH HOH A . I 5 HOH 83 452 83 HOH HOH A . I 5 HOH 84 453 84 HOH HOH A . I 5 HOH 85 454 85 HOH HOH A . I 5 HOH 86 455 86 HOH HOH A . I 5 HOH 87 456 87 HOH HOH A . I 5 HOH 88 457 88 HOH HOH A . I 5 HOH 89 458 89 HOH HOH A . I 5 HOH 90 459 90 HOH HOH A . I 5 HOH 91 460 91 HOH HOH A . I 5 HOH 92 461 92 HOH HOH A . I 5 HOH 93 462 93 HOH HOH A . I 5 HOH 94 463 94 HOH HOH A . I 5 HOH 95 464 95 HOH HOH A . I 5 HOH 96 465 96 HOH HOH A . I 5 HOH 97 466 97 HOH HOH A . I 5 HOH 98 467 98 HOH HOH A . I 5 HOH 99 468 99 HOH HOH A . I 5 HOH 100 469 100 HOH HOH A . I 5 HOH 101 470 101 HOH HOH A . I 5 HOH 102 471 102 HOH HOH A . I 5 HOH 103 472 103 HOH HOH A . I 5 HOH 104 473 104 HOH HOH A . I 5 HOH 105 474 105 HOH HOH A . I 5 HOH 106 475 106 HOH HOH A . I 5 HOH 107 476 107 HOH HOH A . I 5 HOH 108 477 108 HOH HOH A . I 5 HOH 109 478 109 HOH HOH A . I 5 HOH 110 479 110 HOH HOH A . I 5 HOH 111 480 111 HOH HOH A . I 5 HOH 112 481 112 HOH HOH A . I 5 HOH 113 482 113 HOH HOH A . I 5 HOH 114 483 114 HOH HOH A . I 5 HOH 115 484 115 HOH HOH A . I 5 HOH 116 485 116 HOH HOH A . I 5 HOH 117 486 117 HOH HOH A . I 5 HOH 118 487 118 HOH HOH A . I 5 HOH 119 488 119 HOH HOH A . I 5 HOH 120 489 120 HOH HOH A . I 5 HOH 121 490 121 HOH HOH A . I 5 HOH 122 491 122 HOH HOH A . I 5 HOH 123 492 123 HOH HOH A . I 5 HOH 124 493 124 HOH HOH A . I 5 HOH 125 494 125 HOH HOH A . I 5 HOH 126 495 126 HOH HOH A . I 5 HOH 127 496 127 HOH HOH A . I 5 HOH 128 497 128 HOH HOH A . I 5 HOH 129 498 129 HOH HOH A . I 5 HOH 130 499 130 HOH HOH A . I 5 HOH 131 500 131 HOH HOH A . I 5 HOH 132 501 132 HOH HOH A . I 5 HOH 133 502 133 HOH HOH A . I 5 HOH 134 503 134 HOH HOH A . I 5 HOH 135 504 135 HOH HOH A . I 5 HOH 136 505 136 HOH HOH A . I 5 HOH 137 506 137 HOH HOH A . I 5 HOH 138 507 138 HOH HOH A . I 5 HOH 139 508 139 HOH HOH A . I 5 HOH 140 509 140 HOH HOH A . I 5 HOH 141 510 141 HOH HOH A . I 5 HOH 142 511 142 HOH HOH A . I 5 HOH 143 512 143 HOH HOH A . I 5 HOH 144 513 144 HOH HOH A . I 5 HOH 145 514 145 HOH HOH A . I 5 HOH 146 515 146 HOH HOH A . I 5 HOH 147 516 147 HOH HOH A . I 5 HOH 148 517 148 HOH HOH A . I 5 HOH 149 518 149 HOH HOH A . I 5 HOH 150 519 150 HOH HOH A . I 5 HOH 151 520 151 HOH HOH A . I 5 HOH 152 521 152 HOH HOH A . I 5 HOH 153 522 153 HOH HOH A . I 5 HOH 154 523 154 HOH HOH A . I 5 HOH 155 524 155 HOH HOH A . I 5 HOH 156 525 156 HOH HOH A . I 5 HOH 157 526 157 HOH HOH A . I 5 HOH 158 527 158 HOH HOH A . I 5 HOH 159 528 159 HOH HOH A . I 5 HOH 160 529 160 HOH HOH A . I 5 HOH 161 530 161 HOH HOH A . I 5 HOH 162 531 162 HOH HOH A . I 5 HOH 163 532 163 HOH HOH A . I 5 HOH 164 533 164 HOH HOH A . I 5 HOH 165 534 165 HOH HOH A . I 5 HOH 166 535 166 HOH HOH A . I 5 HOH 167 536 167 HOH HOH A . I 5 HOH 168 537 168 HOH HOH A . I 5 HOH 169 538 169 HOH HOH A . I 5 HOH 170 539 170 HOH HOH A . I 5 HOH 171 540 171 HOH HOH A . I 5 HOH 172 541 172 HOH HOH A . I 5 HOH 173 542 173 HOH HOH A . I 5 HOH 174 543 174 HOH HOH A . I 5 HOH 175 544 175 HOH HOH A . I 5 HOH 176 545 176 HOH HOH A . I 5 HOH 177 546 177 HOH HOH A . I 5 HOH 178 547 178 HOH HOH A . I 5 HOH 179 548 179 HOH HOH A . I 5 HOH 180 549 180 HOH HOH A . I 5 HOH 181 550 181 HOH HOH A . I 5 HOH 182 551 182 HOH HOH A . I 5 HOH 183 552 183 HOH HOH A . I 5 HOH 184 553 185 HOH HOH A . I 5 HOH 185 554 186 HOH HOH A . I 5 HOH 186 555 187 HOH HOH A . I 5 HOH 187 556 188 HOH HOH A . I 5 HOH 188 557 189 HOH HOH A . I 5 HOH 189 558 190 HOH HOH A . I 5 HOH 190 559 191 HOH HOH A . I 5 HOH 191 560 192 HOH HOH A . I 5 HOH 192 561 193 HOH HOH A . I 5 HOH 193 562 194 HOH HOH A . I 5 HOH 194 563 195 HOH HOH A . I 5 HOH 195 564 196 HOH HOH A . I 5 HOH 196 565 197 HOH HOH A . I 5 HOH 197 566 198 HOH HOH A . I 5 HOH 198 567 200 HOH HOH A . I 5 HOH 199 568 201 HOH HOH A . I 5 HOH 200 569 202 HOH HOH A . I 5 HOH 201 570 203 HOH HOH A . I 5 HOH 202 571 204 HOH HOH A . I 5 HOH 203 572 205 HOH HOH A . I 5 HOH 204 573 206 HOH HOH A . I 5 HOH 205 574 207 HOH HOH A . I 5 HOH 206 575 208 HOH HOH A . I 5 HOH 207 576 209 HOH HOH A . I 5 HOH 208 577 210 HOH HOH A . I 5 HOH 209 578 211 HOH HOH A . I 5 HOH 210 579 212 HOH HOH A . I 5 HOH 211 580 213 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 2006-08-01 2 'Structure model' 1 1 2008-04-30 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 CNS refinement 1.1 ? 1 AUTOMAR 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 AMoRE phasing . ? 4 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 CA _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 LEU _pdbx_validate_rmsd_angle.auth_seq_id_1 320 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 CB _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 LEU _pdbx_validate_rmsd_angle.auth_seq_id_2 320 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 CG _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 LEU _pdbx_validate_rmsd_angle.auth_seq_id_3 320 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 131.24 _pdbx_validate_rmsd_angle.angle_target_value 115.30 _pdbx_validate_rmsd_angle.angle_deviation 15.94 _pdbx_validate_rmsd_angle.angle_standard_deviation 2.30 _pdbx_validate_rmsd_angle.linker_flag 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 ASP A 169 ? ? -106.03 79.29 2 1 THR A 184 ? ? -78.92 49.96 3 1 TYR A 185 ? ? -149.61 17.38 4 1 ALA A 190 ? ? -58.35 -6.81 5 1 GLN A 193 ? ? -96.28 50.06 6 1 ASN A 205 ? ? -48.24 -14.90 7 1 SER A 206 ? ? -93.36 43.13 8 1 ASP A 207 ? ? 173.62 121.27 9 1 CYS A 343 ? ? -96.40 39.44 10 1 GLN A 345 ? ? -28.74 120.11 11 1 ASN A 346 ? ? -68.92 68.84 # 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 BETA-D-MANNOSE BMA 5 water HOH #