data_1YZP # _entry.id 1YZP # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.289 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1YZP RCSB RCSB032114 WWPDB D_1000032114 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1MNP 'Crystal structure manganese peroxidase' unspecified PDB 1YYD 'High resolution crystal structure of manganese peroxidase' unspecified PDB 1YYG 'Crystal structure of manganese peroxidase-Cd(II) complex' unspecified PDB 1MN1 'Manganese Peroxidase Substrate Binding Site Mutant D179N' unspecified PDB 1MN2 'Manganese Peroxidase Substrate Binding Site Mutant E35Q, D179N' unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1YZP _pdbx_database_status.recvd_initial_deposition_date 2005-02-28 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Sundaramoorthy, M.' 1 'Youngs, H.L.' 2 'Gold, M.H.' 3 'Poulos, T.L.' 4 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary 'High-Resolution Crystal Structure of Manganese Peroxidase: Substrate and Inhibitor Complexes.' Biochemistry 44 6463 6470 2005 BICHAW US 0006-2960 0033 ? 15850380 10.1021/bi047318e 1 'The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06 A resolution' J.Biol.Chem. 269 32759 32767 1994 JBCHA3 US 0021-9258 0071 ? ? ? 2 'Crystal structures of substrate binding site mutants of manganese peroxidase' J.Biol.Chem. 272 17574 17580 1997 JBCHA3 US 0021-9258 0071 ? ? ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Sundaramoorthy, M.' 1 primary 'Youngs, H.L.' 2 primary 'Gold, M.H.' 3 primary 'Poulos, T.L.' 4 1 'Sundaramoorthy, M.' 5 1 'Kishi, K.' 6 1 'Gold, M.G.' 7 1 'Poulos, T.L.' 8 2 'Sundaramoorthy, M.' 9 2 'Kishi, K.' 10 2 'Gold, M.G.' 11 2 'Poulos, T.L.' 12 # _cell.entry_id 1YZP _cell.length_a 160.595 _cell.length_b 45.356 _cell.length_c 52.817 _cell.angle_alpha 90.00 _cell.angle_beta 97.25 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1YZP _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 5 _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 'Peroxidase manganese-dependent I' 37482.973 1 1.11.1.13 ? 'Manganese peroxidase' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 2 ? ? ? ? 5 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487 1 ? ? ? ? 6 non-polymer syn GLYCEROL 92.094 1 ? ? ? ? 7 water nat water 18.015 543 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'MnP-1, MnP1, Manganese peroxidase isozyme 1' # _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 ;AVCPDGTRVSHAACCAFIPLAQDLQETIFQNECGEDAHEVIRLTFHDAIAISRSQGPKAGGGADGSMLLFPTVEPNFSAN NGIDDSVNNLIPFMQKHNTISAADLVQFAGAVALSNCPGAPRLEFLAGRPNKTIAAVDGLIPEPQDSVTKILQRFEDAGG FTPFEVVSLLASHSVARADKVDQTIDAAPFDSTPFTFDTQVFLEVLLKGVGFPGSANNTGEVASPLPLGSGSDTGEMRLQ SDFALAHDPRTACIWQGFVNEQAFMAASFRAAMSKLAVLGHNRNSLIDCSDVVPVPKPATGQPAMFPASTGPQDLELSCP SERFPTLTTQPGASQSLIAHCPDGSMSCPGVQFNGPA ; _entity_poly.pdbx_seq_one_letter_code_can ;AVCPDGTRVSHAACCAFIPLAQDLQETIFQNECGEDAHEVIRLTFHDAIAISRSQGPKAGGGADGSMLLFPTVEPNFSAN NGIDDSVNNLIPFMQKHNTISAADLVQFAGAVALSNCPGAPRLEFLAGRPNKTIAAVDGLIPEPQDSVTKILQRFEDAGG FTPFEVVSLLASHSVARADKVDQTIDAAPFDSTPFTFDTQVFLEVLLKGVGFPGSANNTGEVASPLPLGSGSDTGEMRLQ SDFALAHDPRTACIWQGFVNEQAFMAASFRAAMSKLAVLGHNRNSLIDCSDVVPVPKPATGQPAMFPASTGPQDLELSCP SERFPTLTTQPGASQSLIAHCPDGSMSCPGVQFNGPA ; _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 ALA n 1 2 VAL n 1 3 CYS n 1 4 PRO n 1 5 ASP n 1 6 GLY n 1 7 THR n 1 8 ARG n 1 9 VAL n 1 10 SER n 1 11 HIS n 1 12 ALA n 1 13 ALA n 1 14 CYS n 1 15 CYS n 1 16 ALA n 1 17 PHE n 1 18 ILE n 1 19 PRO n 1 20 LEU n 1 21 ALA n 1 22 GLN n 1 23 ASP n 1 24 LEU n 1 25 GLN n 1 26 GLU n 1 27 THR n 1 28 ILE n 1 29 PHE n 1 30 GLN n 1 31 ASN n 1 32 GLU n 1 33 CYS n 1 34 GLY n 1 35 GLU n 1 36 ASP n 1 37 ALA n 1 38 HIS n 1 39 GLU n 1 40 VAL n 1 41 ILE n 1 42 ARG n 1 43 LEU n 1 44 THR n 1 45 PHE n 1 46 HIS n 1 47 ASP n 1 48 ALA n 1 49 ILE n 1 50 ALA n 1 51 ILE n 1 52 SER n 1 53 ARG n 1 54 SER n 1 55 GLN n 1 56 GLY n 1 57 PRO n 1 58 LYS n 1 59 ALA n 1 60 GLY n 1 61 GLY n 1 62 GLY n 1 63 ALA n 1 64 ASP n 1 65 GLY n 1 66 SER n 1 67 MET n 1 68 LEU n 1 69 LEU n 1 70 PHE n 1 71 PRO n 1 72 THR n 1 73 VAL n 1 74 GLU n 1 75 PRO n 1 76 ASN n 1 77 PHE n 1 78 SER n 1 79 ALA n 1 80 ASN n 1 81 ASN n 1 82 GLY n 1 83 ILE n 1 84 ASP n 1 85 ASP n 1 86 SER n 1 87 VAL n 1 88 ASN n 1 89 ASN n 1 90 LEU n 1 91 ILE n 1 92 PRO n 1 93 PHE n 1 94 MET n 1 95 GLN n 1 96 LYS n 1 97 HIS n 1 98 ASN n 1 99 THR n 1 100 ILE n 1 101 SER n 1 102 ALA n 1 103 ALA n 1 104 ASP n 1 105 LEU n 1 106 VAL n 1 107 GLN n 1 108 PHE n 1 109 ALA n 1 110 GLY n 1 111 ALA n 1 112 VAL n 1 113 ALA n 1 114 LEU n 1 115 SER n 1 116 ASN n 1 117 CYS n 1 118 PRO n 1 119 GLY n 1 120 ALA n 1 121 PRO n 1 122 ARG n 1 123 LEU n 1 124 GLU n 1 125 PHE n 1 126 LEU n 1 127 ALA n 1 128 GLY n 1 129 ARG n 1 130 PRO n 1 131 ASN n 1 132 LYS n 1 133 THR n 1 134 ILE n 1 135 ALA n 1 136 ALA n 1 137 VAL n 1 138 ASP n 1 139 GLY n 1 140 LEU n 1 141 ILE n 1 142 PRO n 1 143 GLU n 1 144 PRO n 1 145 GLN n 1 146 ASP n 1 147 SER n 1 148 VAL n 1 149 THR n 1 150 LYS n 1 151 ILE n 1 152 LEU n 1 153 GLN n 1 154 ARG n 1 155 PHE n 1 156 GLU n 1 157 ASP n 1 158 ALA n 1 159 GLY n 1 160 GLY n 1 161 PHE n 1 162 THR n 1 163 PRO n 1 164 PHE n 1 165 GLU n 1 166 VAL n 1 167 VAL n 1 168 SER n 1 169 LEU n 1 170 LEU n 1 171 ALA n 1 172 SER n 1 173 HIS n 1 174 SER n 1 175 VAL n 1 176 ALA n 1 177 ARG n 1 178 ALA n 1 179 ASP n 1 180 LYS n 1 181 VAL n 1 182 ASP n 1 183 GLN n 1 184 THR n 1 185 ILE n 1 186 ASP n 1 187 ALA n 1 188 ALA n 1 189 PRO n 1 190 PHE n 1 191 ASP n 1 192 SER n 1 193 THR n 1 194 PRO n 1 195 PHE n 1 196 THR n 1 197 PHE n 1 198 ASP n 1 199 THR n 1 200 GLN n 1 201 VAL n 1 202 PHE n 1 203 LEU n 1 204 GLU n 1 205 VAL n 1 206 LEU n 1 207 LEU n 1 208 LYS n 1 209 GLY n 1 210 VAL n 1 211 GLY n 1 212 PHE n 1 213 PRO n 1 214 GLY n 1 215 SER n 1 216 ALA n 1 217 ASN n 1 218 ASN n 1 219 THR n 1 220 GLY n 1 221 GLU n 1 222 VAL n 1 223 ALA n 1 224 SER n 1 225 PRO n 1 226 LEU n 1 227 PRO n 1 228 LEU n 1 229 GLY n 1 230 SER n 1 231 GLY n 1 232 SER n 1 233 ASP n 1 234 THR n 1 235 GLY n 1 236 GLU n 1 237 MET n 1 238 ARG n 1 239 LEU n 1 240 GLN n 1 241 SER n 1 242 ASP n 1 243 PHE n 1 244 ALA n 1 245 LEU n 1 246 ALA n 1 247 HIS n 1 248 ASP n 1 249 PRO n 1 250 ARG n 1 251 THR n 1 252 ALA n 1 253 CYS n 1 254 ILE n 1 255 TRP n 1 256 GLN n 1 257 GLY n 1 258 PHE n 1 259 VAL n 1 260 ASN n 1 261 GLU n 1 262 GLN n 1 263 ALA n 1 264 PHE n 1 265 MET n 1 266 ALA n 1 267 ALA n 1 268 SER n 1 269 PHE n 1 270 ARG n 1 271 ALA n 1 272 ALA n 1 273 MET n 1 274 SER n 1 275 LYS n 1 276 LEU n 1 277 ALA n 1 278 VAL n 1 279 LEU n 1 280 GLY n 1 281 HIS n 1 282 ASN n 1 283 ARG n 1 284 ASN n 1 285 SER n 1 286 LEU n 1 287 ILE n 1 288 ASP n 1 289 CYS n 1 290 SER n 1 291 ASP n 1 292 VAL n 1 293 VAL n 1 294 PRO n 1 295 VAL n 1 296 PRO n 1 297 LYS n 1 298 PRO n 1 299 ALA n 1 300 THR n 1 301 GLY n 1 302 GLN n 1 303 PRO n 1 304 ALA n 1 305 MET n 1 306 PHE n 1 307 PRO n 1 308 ALA n 1 309 SER n 1 310 THR n 1 311 GLY n 1 312 PRO n 1 313 GLN n 1 314 ASP n 1 315 LEU n 1 316 GLU n 1 317 LEU n 1 318 SER n 1 319 CYS n 1 320 PRO n 1 321 SER n 1 322 GLU n 1 323 ARG n 1 324 PHE n 1 325 PRO n 1 326 THR n 1 327 LEU n 1 328 THR n 1 329 THR n 1 330 GLN n 1 331 PRO n 1 332 GLY n 1 333 ALA n 1 334 SER n 1 335 GLN n 1 336 SER n 1 337 LEU n 1 338 ILE n 1 339 ALA n 1 340 HIS n 1 341 CYS n 1 342 PRO n 1 343 ASP n 1 344 GLY n 1 345 SER n 1 346 MET n 1 347 SER n 1 348 CYS n 1 349 PRO n 1 350 GLY n 1 351 VAL n 1 352 GLN n 1 353 PHE n 1 354 ASN n 1 355 GLY n 1 356 PRO n 1 357 ALA 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 ? _entity_src_nat.pdbx_organism_scientific 'Phanerochaete chrysosporium' _entity_src_nat.pdbx_ncbi_taxonomy_id 5306 _entity_src_nat.genus Phanerochaete _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code PEM1_PHACH _struct_ref.pdbx_db_accession Q02567 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;AVCPDGTRVSHAACCAFIPLAQDLQETIFQNECGEDAHEVIRLTFHDAIAISRSQGPKAGGGADGSMLLFPTVEPNFSAN NGIDDSVNNLIPFMQKHNTISAADLVQFAGAVALSNCPGAPRLEFLAGRPNKTIAAVDGLIPEPQDSVTKILQRFEDAGG FTPFEVVSLLASHSVARADKVDQTIDAAPFDSTPFTFDTQVFLEVLLKGVGFPGSANNTGEVASPLPLGSGSDTGEMRLQ SDFALAHDPRTACIWQGFVNEQAFMAASFRAAMSKLAVLGHNRNSLIDCSDVVPVPKPATGQPAMFPASTGPQDLELSCP SERFPTLTTQPGASQSLIAHCPDGSMSCPGVQFNGPA ; _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 1YZP _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 357 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q02567 _struct_ref_seq.db_align_beg 22 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 378 _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 357 # 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 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HEM non-polymer . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 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 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 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 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1YZP _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.16 _exptl_crystal.density_percent_sol 43 _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 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.5 _exptl_crystal_grow.pdbx_details 'PEG 8K, sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 110 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type 'RIGAKU RAXIS IV' _diffrn_detector.pdbx_collection_date 1998-10-19 _diffrn_detector.details Mirrors # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Yale mirror' _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 RU200' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.5418 # _reflns.entry_id 1YZP _reflns.observed_criterion_sigma_F 0 _reflns.observed_criterion_sigma_I 0 _reflns.d_resolution_high 1.6 _reflns.d_resolution_low 161 _reflns.number_all 44812 _reflns.number_obs 43385 _reflns.percent_possible_obs 96 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.043 _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.6 _reflns_shell.d_res_low 1.68 _reflns_shell.percent_possible_all 55 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _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 1YZP _refine.ls_d_res_high 1.6 _refine.ls_d_res_low 8.0 _refine.pdbx_ls_sigma_F 4 _refine.pdbx_ls_sigma_I ? _refine.ls_number_reflns_all 44377 _refine.ls_number_reflns_obs 36995 _refine.ls_number_reflns_R_free 3709 _refine.ls_percent_reflns_obs ? _refine.ls_R_factor_all 0.1723 _refine.ls_R_factor_obs 0.153 _refine.ls_R_factor_R_work 0.1475 _refine.ls_R_factor_R_free 0.2033 _refine.ls_redundancy_reflns_obs ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.ls_percent_reflns_R_free ? _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_method_to_determine_struct 'FOURIER SYNTHESIS' _refine.pdbx_starting_model 'pdb entry 1YYD' _refine.pdbx_ls_cross_valid_method throught _refine.pdbx_R_Free_selection_details Random _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_stereochemistry_target_values SHELXL _refine.solvent_model_details ? _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.occupancy_max ? _refine.occupancy_min ? _refine.pdbx_isotropic_thermal_model ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][2] ? _refine.aniso_B[2][3] ? _refine.aniso_B[3][3] ? _refine.details ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_SU_B ? _refine.overall_SU_ML ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2629 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 90 _refine_hist.number_atoms_solvent 543 _refine_hist.number_atoms_total 3262 _refine_hist.d_res_high 1.6 _refine_hist.d_res_low 8.0 # 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 s_bond_d 0.008 ? ? ? 'X-RAY DIFFRACTION' ? s_angle_d 0.023 ? ? ? 'X-RAY DIFFRACTION' ? s_similar_dist 0.000 ? ? ? 'X-RAY DIFFRACTION' ? s_anti_bump_dis_restr 0.014 ? ? ? 'X-RAY DIFFRACTION' ? s_zero_chiral_vol 0.113 ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 1YZP _struct.title 'Substrate-free manganese peroxidase' _struct.pdbx_descriptor 'Peroxidase manganese-dependent I (E.C.1.11.1.13)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1YZP _struct_keywords.pdbx_keywords OXIDOREDUCTASE _struct_keywords.text 'Peroxidase, heme enzyme, Mn-binding protein, Ca-binding site, glycosylation, OXIDOREDUCTASE' # 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 2 ? D N N 3 ? E N N 4 ? F N N 4 ? G N N 5 ? H N N 6 ? I N N 7 ? # _struct_biol.id 1 _struct_biol.pdbx_parent_biol_id ? _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 HIS A 11 ? CYS A 15 ? HIS A 11 CYS A 15 5 ? 5 HELX_P HELX_P2 2 ALA A 16 ? ILE A 28 ? ALA A 16 ILE A 28 1 ? 13 HELX_P HELX_P3 3 GLY A 34 ? ALA A 50 ? GLY A 34 ALA A 50 1 ? 17 HELX_P HELX_P4 4 GLY A 56 ? GLY A 60 ? GLY A 56 GLY A 60 5 ? 5 HELX_P HELX_P5 5 GLY A 65 ? PHE A 70 ? GLY A 65 PHE A 70 1 ? 6 HELX_P HELX_P6 6 VAL A 73 ? ASN A 81 ? VAL A 73 ASN A 81 5 ? 9 HELX_P HELX_P7 7 ILE A 83 ? HIS A 97 ? ILE A 83 HIS A 97 1 ? 15 HELX_P HELX_P8 8 SER A 101 ? ASN A 116 ? SER A 101 ASN A 116 1 ? 16 HELX_P HELX_P9 9 SER A 147 ? GLY A 160 ? SER A 147 GLY A 160 1 ? 14 HELX_P HELX_P10 10 THR A 162 ? LEU A 170 ? THR A 162 LEU A 170 1 ? 9 HELX_P HELX_P11 11 ALA A 171 ? VAL A 175 ? ALA A 171 VAL A 175 5 ? 5 HELX_P HELX_P12 12 THR A 199 ? LEU A 206 ? THR A 199 LEU A 206 1 ? 8 HELX_P HELX_P13 13 GLN A 240 ? ASP A 248 ? GLN A 240 ASP A 248 1 ? 9 HELX_P HELX_P14 14 THR A 251 ? GLY A 257 ? THR A 251 GLY A 257 1 ? 7 HELX_P HELX_P15 15 GLU A 261 ? ALA A 277 ? GLU A 261 ALA A 277 1 ? 17 HELX_P HELX_P16 16 ASN A 282 ? LEU A 286 ? ASN A 282 LEU A 286 5 ? 5 HELX_P HELX_P17 17 SER A 290 ? VAL A 293 ? SER A 290 VAL A 293 5 ? 4 HELX_P HELX_P18 18 GLY A 311 ? LEU A 315 ? GLY A 311 LEU A 315 5 ? 5 # _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 3 SG ? ? ? 1_555 A CYS 15 SG ? ? A CYS 3 A CYS 15 1_555 ? ? ? ? ? ? ? 2.011 ? disulf2 disulf ? ? A CYS 14 SG ? ? ? 1_555 A CYS 289 SG ? ? A CYS 14 A CYS 289 1_555 ? ? ? ? ? ? ? 2.022 ? disulf3 disulf ? ? A CYS 33 SG ? ? ? 1_555 A CYS 117 SG ? ? A CYS 33 A CYS 117 1_555 ? ? ? ? ? ? ? 2.034 ? disulf4 disulf ? ? A CYS 253 SG ? ? ? 1_555 A CYS 319 SG ? ? A CYS 253 A CYS 319 1_555 ? ? ? ? ? ? ? 2.052 ? disulf5 disulf ? ? A CYS 341 SG ? ? ? 1_555 A CYS 348 SG ? ? A CYS 341 A CYS 348 1_555 ? ? ? ? ? ? ? 2.040 ? covale1 covale ? ? A ASN 131 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 131 A NAG 361 1_555 ? ? ? ? ? ? ? 1.458 ? covale2 covale ? ? A SER 336 OG ? ? ? 1_555 D MAN . C1 ? ? A SER 336 A MAN 364 1_555 ? ? ? ? ? ? ? 1.421 ? covale3 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 361 A NAG 362 1_555 ? ? ? ? ? ? ? 1.410 ? metalc1 metalc ? ? A HIS 173 NE2 ? ? ? 1_555 G HEM . FE ? ? A HIS 173 A HEM 396 1_555 ? ? ? ? ? ? ? 2.133 ? metalc2 metalc ? ? E CA . CA ? ? ? 1_555 A ASP 191 OD2 ? ? A CA 371 A ASP 191 1_555 ? ? ? ? ? ? ? 2.410 ? metalc3 metalc ? ? E CA . CA ? ? ? 1_555 A ASP 198 OD1 ? ? A CA 371 A ASP 198 1_555 ? ? ? ? ? ? ? 2.443 ? metalc4 metalc ? ? E CA . CA ? ? ? 1_555 A SER 174 OG ? ? A CA 371 A SER 174 1_555 ? ? ? ? ? ? ? 2.459 ? metalc5 metalc ? ? E CA . CA ? ? ? 1_555 A THR 193 O ? ? A CA 371 A THR 193 1_555 ? ? ? ? ? ? ? 2.394 ? metalc6 metalc ? ? E CA . CA ? ? ? 1_555 A THR 193 OG1 ? ? A CA 371 A THR 193 1_555 ? ? ? ? ? ? ? 2.524 ? metalc7 metalc ? ? E CA . CA ? ? ? 1_555 A THR 196 O ? ? A CA 371 A THR 196 1_555 ? ? ? ? ? ? ? 2.511 ? metalc8 metalc ? ? E CA . CA ? ? ? 1_555 A ASP 191 OD1 ? ? A CA 371 A ASP 191 1_555 ? ? ? ? ? ? ? 2.644 ? metalc9 metalc ? ? E CA . CA ? ? ? 1_555 A SER 174 O ? ? A CA 371 A SER 174 1_555 ? ? ? ? ? ? ? 2.395 ? metalc10 metalc ? ? F CA . CA ? ? ? 1_555 I HOH . O ? ? A CA 372 A HOH 1128 1_555 ? ? ? ? ? ? ? 2.377 ? metalc11 metalc ? ? F CA . CA ? ? ? 1_555 I HOH . O ? ? A CA 372 A HOH 1085 1_555 ? ? ? ? ? ? ? 2.379 ? metalc12 metalc ? ? F CA . CA ? ? ? 1_555 A ASP 47 OD2 ? ? A CA 372 A ASP 47 1_555 ? ? ? ? ? ? ? 2.287 ? metalc13 metalc ? ? F CA . CA ? ? ? 1_555 A GLY 62 O ? ? A CA 372 A GLY 62 1_555 ? ? ? ? ? ? ? 2.506 ? metalc14 metalc ? ? F CA . CA ? ? ? 1_555 A ASP 64 OD1 ? ? A CA 372 A ASP 64 1_555 ? ? ? ? ? ? ? 2.502 ? metalc15 metalc ? ? F CA . CA ? ? ? 1_555 A SER 66 OG ? ? A CA 372 A SER 66 1_555 ? ? ? ? ? ? ? 2.472 ? metalc16 metalc ? ? F CA . CA ? ? ? 1_555 A ASP 47 O ? ? A CA 372 A ASP 47 1_555 ? ? ? ? ? ? ? 2.499 ? metalc17 metalc ? ? G HEM . FE ? ? ? 1_555 I HOH . O ? ? A HEM 396 A HOH 1138 1_555 ? ? ? ? ? ? ? 1.803 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 2 ? B ? 2 ? C ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 LEU A 126 ? ALA A 127 ? LEU A 126 ALA A 127 A 2 ILE A 287 ? ASP A 288 ? ILE A 287 ASP A 288 B 1 ARG A 177 ? ALA A 178 ? ARG A 177 ALA A 178 B 2 ALA A 188 ? PRO A 189 ? ALA A 188 PRO A 189 C 1 GLU A 221 ? VAL A 222 ? GLU A 221 VAL A 222 C 2 ARG A 238 ? LEU A 239 ? ARG A 238 LEU A 239 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N ALA A 127 ? N ALA A 127 O ILE A 287 ? O ILE A 287 B 1 2 N ALA A 178 ? N ALA A 178 O ALA A 188 ? O ALA A 188 C 1 2 N VAL A 222 ? N VAL A 222 O ARG A 238 ? O ARG A 238 # 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 ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG A 361' AC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG A 362' AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE MAN A 364' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 371' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 372' AC6 Software ? ? ? ? 27 'BINDING SITE FOR RESIDUE HEM A 396' AC7 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GOL A 401' # 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 10 ASN A 98 ? ASN A 98 . ? 1_555 ? 2 AC1 10 THR A 99 ? THR A 99 . ? 1_555 ? 3 AC1 10 ILE A 100 ? ILE A 100 . ? 1_555 ? 4 AC1 10 ASN A 131 ? ASN A 131 . ? 1_555 ? 5 AC1 10 NAG C . ? NAG A 362 . ? 1_555 ? 6 AC1 10 HOH I . ? HOH A 1090 . ? 1_555 ? 7 AC1 10 HOH I . ? HOH A 1118 . ? 1_555 ? 8 AC1 10 HOH I . ? HOH A 1248 . ? 1_555 ? 9 AC1 10 HOH I . ? HOH A 1313 . ? 1_555 ? 10 AC1 10 HOH I . ? HOH A 1537 . ? 1_555 ? 11 AC2 8 MET A 94 ? MET A 94 . ? 1_555 ? 12 AC2 8 GLN A 95 ? GLN A 95 . ? 1_555 ? 13 AC2 8 ASN A 98 ? ASN A 98 . ? 1_555 ? 14 AC2 8 NAG B . ? NAG A 361 . ? 1_555 ? 15 AC2 8 HOH I . ? HOH A 1233 . ? 1_555 ? 16 AC2 8 HOH I . ? HOH A 1406 . ? 1_555 ? 17 AC2 8 HOH I . ? HOH A 1487 . ? 1_555 ? 18 AC2 8 HOH I . ? HOH A 1529 . ? 1_555 ? 19 AC3 7 HIS A 11 ? HIS A 11 . ? 1_554 ? 20 AC3 7 PRO A 331 ? PRO A 331 . ? 1_555 ? 21 AC3 7 GLY A 332 ? GLY A 332 . ? 1_555 ? 22 AC3 7 SER A 334 ? SER A 334 . ? 1_555 ? 23 AC3 7 GLN A 335 ? GLN A 335 . ? 1_555 ? 24 AC3 7 SER A 336 ? SER A 336 . ? 1_555 ? 25 AC3 7 HOH I . ? HOH A 1135 . ? 1_555 ? 26 AC4 5 SER A 174 ? SER A 174 . ? 1_555 ? 27 AC4 5 ASP A 191 ? ASP A 191 . ? 1_555 ? 28 AC4 5 THR A 193 ? THR A 193 . ? 1_555 ? 29 AC4 5 THR A 196 ? THR A 196 . ? 1_555 ? 30 AC4 5 ASP A 198 ? ASP A 198 . ? 1_555 ? 31 AC5 6 ASP A 47 ? ASP A 47 . ? 1_555 ? 32 AC5 6 GLY A 62 ? GLY A 62 . ? 1_555 ? 33 AC5 6 ASP A 64 ? ASP A 64 . ? 1_555 ? 34 AC5 6 SER A 66 ? SER A 66 . ? 1_555 ? 35 AC5 6 HOH I . ? HOH A 1085 . ? 1_555 ? 36 AC5 6 HOH I . ? HOH A 1128 . ? 1_555 ? 37 AC6 27 HIS A 38 ? HIS A 38 . ? 1_555 ? 38 AC6 27 GLU A 39 ? GLU A 39 . ? 1_555 ? 39 AC6 27 ARG A 42 ? ARG A 42 . ? 1_555 ? 40 AC6 27 PHE A 45 ? PHE A 45 . ? 1_555 ? 41 AC6 27 GLU A 143 ? GLU A 143 . ? 1_555 ? 42 AC6 27 PRO A 144 ? PRO A 144 . ? 1_555 ? 43 AC6 27 ILE A 151 ? ILE A 151 . ? 1_555 ? 44 AC6 27 LEU A 169 ? LEU A 169 . ? 1_555 ? 45 AC6 27 LEU A 170 ? LEU A 170 . ? 1_555 ? 46 AC6 27 SER A 172 ? SER A 172 . ? 1_555 ? 47 AC6 27 HIS A 173 ? HIS A 173 . ? 1_555 ? 48 AC6 27 VAL A 175 ? VAL A 175 . ? 1_555 ? 49 AC6 27 ALA A 176 ? ALA A 176 . ? 1_555 ? 50 AC6 27 ARG A 177 ? ARG A 177 . ? 1_555 ? 51 AC6 27 ALA A 178 ? ALA A 178 . ? 1_555 ? 52 AC6 27 ASP A 179 ? ASP A 179 . ? 1_555 ? 53 AC6 27 LYS A 180 ? LYS A 180 . ? 1_555 ? 54 AC6 27 VAL A 181 ? VAL A 181 . ? 1_555 ? 55 AC6 27 PHE A 190 ? PHE A 190 . ? 1_555 ? 56 AC6 27 LEU A 239 ? LEU A 239 . ? 1_555 ? 57 AC6 27 HOH I . ? HOH A 1074 . ? 1_555 ? 58 AC6 27 HOH I . ? HOH A 1109 . ? 1_555 ? 59 AC6 27 HOH I . ? HOH A 1138 . ? 1_555 ? 60 AC6 27 HOH I . ? HOH A 1195 . ? 1_555 ? 61 AC6 27 HOH I . ? HOH A 1501 . ? 1_555 ? 62 AC6 27 HOH I . ? HOH A 1502 . ? 1_555 ? 63 AC6 27 HOH I . ? HOH A 1523 . ? 1_555 ? 64 AC7 9 ASP A 23 ? ASP A 23 . ? 1_555 ? 65 AC7 9 THR A 27 ? THR A 27 . ? 1_555 ? 66 AC7 9 PRO A 92 ? PRO A 92 . ? 1_555 ? 67 AC7 9 LYS A 96 ? LYS A 96 . ? 1_555 ? 68 AC7 9 GLU A 156 ? GLU A 156 . ? 1_565 ? 69 AC7 9 HOH I . ? HOH A 1092 . ? 1_565 ? 70 AC7 9 HOH I . ? HOH A 1299 . ? 1_555 ? 71 AC7 9 HOH I . ? HOH A 1383 . ? 1_565 ? 72 AC7 9 HOH I . ? HOH A 1550 . ? 1_555 ? # _database_PDB_matrix.entry_id 1YZP _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] 0.000000 _database_PDB_matrix.origx_vector[2] 0.000000 _database_PDB_matrix.origx_vector[3] 0.000000 # _atom_sites.entry_id 1YZP _atom_sites.fract_transf_matrix[1][1] 0.006227 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000793 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.022048 _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] 0.019086 _atom_sites.fract_transf_vector[1] 0.000000 _atom_sites.fract_transf_vector[2] 0.000000 _atom_sites.fract_transf_vector[3] 0.000000 # loop_ _atom_type.symbol C CA FE 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 . ALA A 1 1 ? 37.624 37.821 64.308 1.00 28.48 ? 1 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? 38.263 39.104 64.528 1.00 27.08 ? 1 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 37.929 40.058 63.383 1.00 24.83 ? 1 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? 37.556 39.622 62.296 1.00 29.42 ? 1 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 39.777 38.976 64.648 1.00 35.42 ? 1 ALA A CB 1 ATOM 6 N N . VAL A 1 2 ? 38.064 41.341 63.686 1.00 22.42 ? 2 VAL A N 1 ATOM 7 C CA . VAL A 1 2 ? 37.885 42.385 62.696 1.00 31.89 ? 2 VAL A CA 1 ATOM 8 C C . VAL A 1 2 ? 39.240 43.024 62.415 1.00 32.47 ? 2 VAL A C 1 ATOM 9 O O . VAL A 1 2 ? 39.837 43.596 63.318 1.00 40.01 ? 2 VAL A O 1 ATOM 10 C CB . VAL A 1 2 ? 36.905 43.484 63.154 1.00 24.21 ? 2 VAL A CB 1 ATOM 11 C CG1 . VAL A 1 2 ? 36.758 44.509 62.035 1.00 26.70 ? 2 VAL A CG1 1 ATOM 12 C CG2 . VAL A 1 2 ? 35.562 42.858 63.473 1.00 26.32 ? 2 VAL A CG2 1 ATOM 13 N N . CYS A 1 3 ? 39.704 42.884 61.190 1.00 29.94 ? 3 CYS A N 1 ATOM 14 C CA . CYS A 1 3 ? 40.992 43.426 60.764 1.00 35.49 ? 3 CYS A CA 1 ATOM 15 C C . CYS A 1 3 ? 40.922 44.931 60.570 1.00 46.82 ? 3 CYS A C 1 ATOM 16 O O . CYS A 1 3 ? 39.830 45.489 60.403 1.00 31.35 ? 3 CYS A O 1 ATOM 17 C CB . CYS A 1 3 ? 41.361 42.724 59.446 1.00 25.53 ? 3 CYS A CB 1 ATOM 18 S SG . CYS A 1 3 ? 41.424 40.932 59.694 1.00 26.08 ? 3 CYS A SG 1 ATOM 19 N N . PRO A 1 4 ? 42.070 45.594 60.543 1.00 40.12 ? 4 PRO A N 1 ATOM 20 C CA . PRO A 1 4 ? 42.056 47.062 60.504 1.00 53.00 ? 4 PRO A CA 1 ATOM 21 C C . PRO A 1 4 ? 41.306 47.586 59.292 1.00 56.57 ? 4 PRO A C 1 ATOM 22 O O . PRO A 1 4 ? 40.767 48.696 59.286 1.00 48.50 ? 4 PRO A O 1 ATOM 23 C CB . PRO A 1 4 ? 43.538 47.434 60.471 1.00 42.60 ? 4 PRO A CB 1 ATOM 24 C CG . PRO A 1 4 ? 44.237 46.231 61.017 1.00 36.66 ? 4 PRO A CG 1 ATOM 25 C CD . PRO A 1 4 ? 43.438 45.061 60.489 1.00 39.60 ? 4 PRO A CD 1 ATOM 26 N N . ASP A 1 5 ? 41.206 46.784 58.232 1.00 40.77 ? 5 ASP A N 1 ATOM 27 C CA . ASP A 1 5 ? 40.468 47.281 57.065 1.00 49.13 ? 5 ASP A CA 1 ATOM 28 C C . ASP A 1 5 ? 38.970 47.053 57.197 1.00 42.70 ? 5 ASP A C 1 ATOM 29 O O . ASP A 1 5 ? 38.187 47.286 56.280 1.00 48.46 ? 5 ASP A O 1 ATOM 30 C CB . ASP A 1 5 ? 41.002 46.592 55.808 1.00 36.98 ? 5 ASP A CB 1 ATOM 31 C CG . ASP A 1 5 ? 40.480 45.174 55.649 1.00 58.85 ? 5 ASP A CG 1 ATOM 32 O OD1 . ASP A 1 5 ? 40.078 44.553 56.658 1.00 35.81 ? 5 ASP A OD1 1 ATOM 33 O OD2 . ASP A 1 5 ? 40.497 44.693 54.491 1.00 37.05 ? 5 ASP A OD2 1 ATOM 34 N N . GLY A 1 6 ? 38.546 46.455 58.313 1.00 30.28 ? 6 GLY A N 1 ATOM 35 C CA . GLY A 1 6 ? 37.128 46.156 58.411 1.00 23.17 ? 6 GLY A CA 1 ATOM 36 C C . GLY A 1 6 ? 36.785 44.740 58.015 1.00 38.83 ? 6 GLY A C 1 ATOM 37 O O . GLY A 1 6 ? 35.639 44.319 58.183 1.00 34.05 ? 6 GLY A O 1 ATOM 38 N N . THR A 1 7 ? 37.731 43.942 57.506 1.00 26.85 ? 7 THR A N 1 ATOM 39 C CA . THR A 1 7 ? 37.342 42.576 57.144 1.00 29.12 ? 7 THR A CA 1 ATOM 40 C C . THR A 1 7 ? 37.123 41.723 58.378 1.00 30.26 ? 7 THR A C 1 ATOM 41 O O . THR A 1 7 ? 37.915 41.708 59.324 1.00 30.11 ? 7 THR A O 1 ATOM 42 C CB . THR A 1 7 ? 38.417 41.940 56.242 1.00 24.22 ? 7 THR A CB 1 ATOM 43 O OG1 . THR A 1 7 ? 38.671 42.826 55.140 1.00 37.27 ? 7 THR A OG1 1 ATOM 44 C CG2 . THR A 1 7 ? 37.921 40.642 55.625 1.00 25.03 ? 7 THR A CG2 1 ATOM 45 N N . ARG A 1 8 ? 36.016 40.970 58.417 1.00 27.07 ? 8 ARG A N 1 ATOM 46 C CA . ARG A 1 8 ? 35.855 40.039 59.539 1.00 26.50 ? 8 ARG A CA 1 ATOM 47 C C . ARG A 1 8 ? 36.552 38.731 59.178 1.00 40.61 ? 8 ARG A C 1 ATOM 48 O O . ARG A 1 8 ? 36.328 38.199 58.085 1.00 32.66 ? 8 ARG A O 1 ATOM 49 C CB . ARG A 1 8 ? 34.369 39.837 59.838 1.00 22.81 ? 8 ARG A CB 1 ATOM 50 C CG . ARG A 1 8 ? 34.111 38.905 61.004 1.00 32.13 ? 8 ARG A CG 1 ATOM 51 C CD . ARG A 1 8 ? 32.784 39.197 61.690 1.00 32.59 ? 8 ARG A CD 1 ATOM 52 N NE . ARG A 1 8 ? 31.719 38.378 61.120 1.00 48.86 ? 8 ARG A NE 1 ATOM 53 C CZ . ARG A 1 8 ? 31.352 37.178 61.550 1.00 31.27 ? 8 ARG A CZ 1 ATOM 54 N NH1 . ARG A 1 8 ? 31.949 36.639 62.614 1.00 29.12 ? 8 ARG A NH1 1 ATOM 55 N NH2 . ARG A 1 8 ? 30.370 36.537 60.925 1.00 62.11 ? 8 ARG A NH2 1 ATOM 56 N N . VAL A 1 9 ? 37.450 38.224 60.018 1.00 35.73 ? 9 VAL A N 1 ATOM 57 C CA . VAL A 1 9 ? 38.105 36.953 59.701 1.00 27.53 ? 9 VAL A CA 1 ATOM 58 C C . VAL A 1 9 ? 38.059 36.039 60.936 1.00 41.47 ? 9 VAL A C 1 ATOM 59 O O . VAL A 1 9 ? 37.706 36.526 62.009 1.00 30.36 ? 9 VAL A O 1 ATOM 60 C CB . VAL A 1 9 ? 39.581 37.116 59.295 1.00 26.51 ? 9 VAL A CB 1 ATOM 61 C CG1 . VAL A 1 9 ? 39.692 38.100 58.135 1.00 26.32 ? 9 VAL A CG1 1 ATOM 62 C CG2 . VAL A 1 9 ? 40.379 37.589 60.501 1.00 24.77 ? 9 VAL A CG2 1 ATOM 63 N N . SER A 1 10 ? 38.405 34.802 60.668 1.00 29.87 ? 10 SER A N 1 ATOM 64 C CA . SER A 1 10 ? 38.508 33.641 61.515 1.00 29.93 ? 10 SER A CA 1 ATOM 65 C C . SER A 1 10 ? 39.358 33.906 62.758 1.00 38.05 ? 10 SER A C 1 ATOM 66 O O . SER A 1 10 ? 38.986 33.579 63.880 1.00 44.84 ? 10 SER A O 1 ATOM 67 C CB . SER A 1 10 ? 39.190 32.510 60.721 1.00 32.19 ? 10 SER A CB 1 ATOM 68 O OG . SER A 1 10 ? 40.525 32.887 60.351 1.00 30.02 ? 10 SER A OG 1 ATOM 69 N N . HIS A 1 11 ? 40.570 34.406 62.552 1.00 25.57 ? 11 HIS A N 1 ATOM 70 C CA . HIS A 1 11 ? 41.498 34.650 63.654 1.00 23.39 ? 11 HIS A CA 1 ATOM 71 C C . HIS A 1 11 ? 42.240 35.944 63.364 1.00 23.68 ? 11 HIS A C 1 ATOM 72 O O . HIS A 1 11 ? 42.604 36.220 62.218 1.00 25.60 ? 11 HIS A O 1 ATOM 73 C CB . HIS A 1 11 ? 42.541 33.540 63.795 1.00 32.81 ? 11 HIS A CB 1 ATOM 74 C CG . HIS A 1 11 ? 42.016 32.150 63.639 1.00 50.07 ? 11 HIS A CG 1 ATOM 75 N ND1 . HIS A 1 11 ? 41.665 31.364 64.716 1.00 51.05 ? 11 HIS A ND1 1 ATOM 76 C CD2 . HIS A 1 11 ? 41.788 31.394 62.539 1.00 35.18 ? 11 HIS A CD2 1 ATOM 77 C CE1 . HIS A 1 11 ? 41.241 30.191 64.276 1.00 51.64 ? 11 HIS A CE1 1 ATOM 78 N NE2 . HIS A 1 11 ? 41.298 30.181 62.953 1.00 49.93 ? 11 HIS A NE2 1 ATOM 79 N N . ALA A 1 12 ? 42.522 36.698 64.415 1.00 20.80 ? 12 ALA A N 1 ATOM 80 C CA . ALA A 1 12 ? 43.240 37.950 64.187 1.00 25.33 ? 12 ALA A CA 1 ATOM 81 C C . ALA A 1 12 ? 44.581 37.728 63.499 1.00 21.77 ? 12 ALA A C 1 ATOM 82 O O . ALA A 1 12 ? 45.055 38.615 62.792 1.00 30.93 ? 12 ALA A O 1 ATOM 83 C CB . ALA A 1 12 ? 43.457 38.693 65.501 1.00 32.87 ? 12 ALA A CB 1 ATOM 84 N N . ALA A 1 13 ? 45.229 36.584 63.716 1.00 24.79 ? 13 ALA A N 1 ATOM 85 C CA . ALA A 1 13 ? 46.552 36.420 63.102 1.00 29.57 ? 13 ALA A CA 1 ATOM 86 C C . ALA A 1 13 ? 46.453 36.317 61.587 1.00 25.74 ? 13 ALA A C 1 ATOM 87 O O . ALA A 1 13 ? 47.433 36.491 60.861 1.00 24.01 ? 13 ALA A O 1 ATOM 88 C CB . ALA A 1 13 ? 47.255 35.222 63.704 1.00 28.20 ? 13 ALA A CB 1 ATOM 89 N N . CYS A 1 14 ? 45.237 36.089 61.078 1.00 19.62 ? 14 CYS A N 1 ATOM 90 C CA . CYS A 1 14 ? 45.110 36.026 59.622 1.00 23.85 ? 14 CYS A CA 1 ATOM 91 C C . CYS A 1 14 ? 45.008 37.408 58.997 1.00 19.50 ? 14 CYS A C 1 ATOM 92 O O . CYS A 1 14 ? 45.173 37.524 57.780 1.00 18.34 ? 14 CYS A O 1 ATOM 93 C CB . CYS A 1 14 ? 43.882 35.216 59.194 1.00 18.50 ? 14 CYS A CB 1 ATOM 94 S SG . CYS A 1 14 ? 43.825 33.581 59.950 1.00 21.35 ? 14 CYS A SG 1 ATOM 95 N N . CYS A 1 15 ? 44.791 38.436 59.817 1.00 21.29 ? 15 CYS A N 1 ATOM 96 C CA . CYS A 1 15 ? 44.589 39.763 59.240 1.00 28.54 ? 15 CYS A CA 1 ATOM 97 C C . CYS A 1 15 ? 45.689 40.233 58.303 1.00 15.02 ? 15 CYS A C 1 ATOM 98 O O . CYS A 1 15 ? 45.374 40.855 57.275 1.00 20.52 ? 15 CYS A O 1 ATOM 99 C CB . CYS A 1 15 ? 44.393 40.812 60.342 1.00 24.00 ? 15 CYS A CB 1 ATOM 100 S SG . CYS A 1 15 ? 42.781 40.637 61.148 1.00 24.91 ? 15 CYS A SG 1 ATOM 101 N N . ALA A 1 16 ? 46.939 39.962 58.665 1.00 18.61 ? 16 ALA A N 1 ATOM 102 C CA . ALA A 1 16 ? 48.058 40.540 57.924 1.00 15.95 ? 16 ALA A CA 1 ATOM 103 C C . ALA A 1 16 ? 48.093 39.969 56.503 1.00 17.84 ? 16 ALA A C 1 ATOM 104 O O . ALA A 1 16 ? 48.720 40.600 55.633 1.00 18.24 ? 16 ALA A O 1 ATOM 105 C CB . ALA A 1 16 ? 49.365 40.301 58.650 1.00 15.97 ? 16 ALA A CB 1 ATOM 106 N N . PHE A 1 17 ? 47.474 38.792 56.342 1.00 14.92 ? 17 PHE A N 1 ATOM 107 C CA . PHE A 1 17 ? 47.507 38.192 55.010 1.00 17.14 ? 17 PHE A CA 1 ATOM 108 C C . PHE A 1 17 ? 46.622 38.965 54.030 1.00 15.53 ? 17 PHE A C 1 ATOM 109 O O . PHE A 1 17 ? 46.858 38.832 52.830 1.00 18.05 ? 17 PHE A O 1 ATOM 110 C CB . PHE A 1 17 ? 47.083 36.722 55.010 1.00 14.30 ? 17 PHE A CB 1 ATOM 111 C CG . PHE A 1 17 ? 48.138 35.864 55.719 1.00 14.86 ? 17 PHE A CG 1 ATOM 112 C CD1 . PHE A 1 17 ? 48.050 35.667 57.090 1.00 19.02 ? 17 PHE A CD1 1 ATOM 113 C CD2 . PHE A 1 17 ? 49.202 35.318 55.026 1.00 13.61 ? 17 PHE A CD2 1 ATOM 114 C CE1 . PHE A 1 17 ? 49.045 34.939 57.754 1.00 18.11 ? 17 PHE A CE1 1 ATOM 115 C CE2 . PHE A 1 17 ? 50.198 34.603 55.671 1.00 16.13 ? 17 PHE A CE2 1 ATOM 116 C CZ . PHE A 1 17 ? 50.116 34.426 57.046 1.00 16.34 ? 17 PHE A CZ 1 ATOM 117 N N . ILE A 1 18 ? 45.688 39.768 54.528 1.00 17.73 ? 18 ILE A N 1 ATOM 118 C CA . ILE A 1 18 ? 44.844 40.533 53.588 1.00 21.19 ? 18 ILE A CA 1 ATOM 119 C C . ILE A 1 18 ? 45.625 41.566 52.801 1.00 18.96 ? 18 ILE A C 1 ATOM 120 O O . ILE A 1 18 ? 45.614 41.556 51.553 1.00 18.62 ? 18 ILE A O 1 ATOM 121 C CB . ILE A 1 18 ? 43.619 41.145 54.284 1.00 17.78 ? 18 ILE A CB 1 ATOM 122 C CG1 . ILE A 1 18 ? 42.740 40.065 54.921 1.00 14.88 ? 18 ILE A CG1 1 ATOM 123 C CG2 . ILE A 1 18 ? 42.788 42.027 53.359 1.00 19.04 ? 18 ILE A CG2 1 ATOM 124 C CD1 . ILE A 1 18 ? 41.692 40.565 55.894 1.00 16.90 ? 18 ILE A CD1 1 ATOM 125 N N . PRO A 1 19 ? 46.319 42.506 53.408 1.00 17.61 ? 19 PRO A N 1 ATOM 126 C CA . PRO A 1 19 ? 47.106 43.452 52.586 1.00 16.71 ? 19 PRO A CA 1 ATOM 127 C C . PRO A 1 19 ? 48.227 42.747 51.831 1.00 19.68 ? 19 PRO A C 1 ATOM 128 O O . PRO A 1 19 ? 48.705 43.256 50.809 1.00 17.27 ? 19 PRO A O 1 ATOM 129 C CB . PRO A 1 19 ? 47.694 44.419 53.616 1.00 25.88 ? 19 PRO A CB 1 ATOM 130 C CG . PRO A 1 19 ? 47.660 43.672 54.911 1.00 18.43 ? 19 PRO A CG 1 ATOM 131 C CD . PRO A 1 19 ? 46.381 42.856 54.846 1.00 23.36 ? 19 PRO A CD 1 ATOM 132 N N . LEU A 1 20 ? 48.645 41.569 52.310 1.00 17.65 ? 20 LEU A N 1 ATOM 133 C CA . LEU A 1 20 ? 49.709 40.860 51.580 1.00 19.30 ? 20 LEU A CA 1 ATOM 134 C C . LEU A 1 20 ? 49.148 40.336 50.265 1.00 19.85 ? 20 LEU A C 1 ATOM 135 O O . LEU A 1 20 ? 49.770 40.498 49.214 1.00 19.52 ? 20 LEU A O 1 ATOM 136 C CB . LEU A 1 20 ? 50.325 39.734 52.427 1.00 14.54 ? 20 LEU A CB 1 ATOM 137 C CG . LEU A 1 20 ? 51.225 38.738 51.681 1.00 12.22 ? 20 LEU A CG 1 ATOM 138 C CD1 . LEU A 1 20 ? 52.401 39.483 51.050 1.00 16.60 ? 20 LEU A CD1 1 ATOM 139 C CD2 . LEU A 1 20 ? 51.652 37.620 52.606 1.00 14.67 ? 20 LEU A CD2 1 ATOM 140 N N . ALA A 1 21 ? 47.950 39.745 50.301 1.00 18.23 ? 21 ALA A N 1 ATOM 141 C CA . ALA A 1 21 ? 47.338 39.323 49.038 1.00 13.71 ? 21 ALA A CA 1 ATOM 142 C C . ALA A 1 21 ? 47.148 40.507 48.110 1.00 17.82 ? 21 ALA A C 1 ATOM 143 O O . ALA A 1 21 ? 47.414 40.432 46.913 1.00 17.48 ? 21 ALA A O 1 ATOM 144 C CB . ALA A 1 21 ? 45.993 38.640 49.257 1.00 18.57 ? 21 ALA A CB 1 ATOM 145 N N . GLN A 1 22 ? 46.650 41.607 48.663 1.00 15.67 ? 22 GLN A N 1 ATOM 146 C CA . GLN A 1 22 ? 46.418 42.773 47.791 1.00 20.53 ? 22 GLN A CA 1 ATOM 147 C C . GLN A 1 22 ? 47.709 43.228 47.148 1.00 14.65 ? 22 GLN A C 1 ATOM 148 O O . GLN A 1 22 ? 47.800 43.635 45.988 1.00 20.19 ? 22 GLN A O 1 ATOM 149 C CB . GLN A 1 22 ? 45.790 43.885 48.655 0.52 7.86 ? 22 GLN A CB 1 ATOM 150 C CG . GLN A 1 22 ? 44.396 43.478 49.117 0.52 8.70 ? 22 GLN A CG 1 ATOM 151 C CD . GLN A 1 22 ? 43.721 44.574 49.925 0.52 42.43 ? 22 GLN A CD 1 ATOM 152 O OE1 . GLN A 1 22 ? 42.658 44.374 50.513 0.52 21.57 ? 22 GLN A OE1 1 ATOM 153 N NE2 . GLN A 1 22 ? 44.347 45.749 49.964 0.52 42.90 ? 22 GLN A NE2 1 ATOM 154 N N . ASP A 1 23 ? 48.793 43.270 47.928 1.00 13.03 ? 23 ASP A N 1 ATOM 155 C CA . ASP A 1 23 ? 50.070 43.746 47.391 1.00 13.91 ? 23 ASP A CA 1 ATOM 156 C C . ASP A 1 23 ? 50.604 42.768 46.352 1.00 17.96 ? 23 ASP A C 1 ATOM 157 O O . ASP A 1 23 ? 51.159 43.214 45.344 1.00 15.80 ? 23 ASP A O 1 ATOM 158 C CB . ASP A 1 23 ? 51.081 43.850 48.523 1.00 14.03 ? 23 ASP A CB 1 ATOM 159 C CG . ASP A 1 23 ? 52.244 44.792 48.307 1.00 24.29 ? 23 ASP A CG 1 ATOM 160 O OD1 . ASP A 1 23 ? 52.399 45.474 47.275 1.00 17.29 ? 23 ASP A OD1 1 ATOM 161 O OD2 . ASP A 1 23 ? 53.058 44.873 49.265 1.00 24.01 ? 23 ASP A OD2 1 ATOM 162 N N . LEU A 1 24 ? 50.486 41.466 46.616 1.00 15.39 ? 24 LEU A N 1 ATOM 163 C CA . LEU A 1 24 ? 50.944 40.492 45.618 1.00 14.38 ? 24 LEU A CA 1 ATOM 164 C C . LEU A 1 24 ? 50.161 40.643 44.303 1.00 12.05 ? 24 LEU A C 1 ATOM 165 O O . LEU A 1 24 ? 50.784 40.666 43.238 1.00 18.59 ? 24 LEU A O 1 ATOM 166 C CB . LEU A 1 24 ? 50.730 39.064 46.134 1.00 13.83 ? 24 LEU A CB 1 ATOM 167 C CG . LEU A 1 24 ? 51.666 38.635 47.276 1.00 13.17 ? 24 LEU A CG 1 ATOM 168 C CD1 . LEU A 1 24 ? 51.101 37.356 47.900 1.00 16.58 ? 24 LEU A CD1 1 ATOM 169 C CD2 . LEU A 1 24 ? 53.092 38.459 46.787 1.00 14.52 ? 24 LEU A CD2 1 ATOM 170 N N . GLN A 1 25 ? 48.837 40.811 44.417 1.00 10.32 ? 25 GLN A N 1 ATOM 171 C CA . GLN A 1 25 ? 48.048 40.980 43.189 1.00 14.42 ? 25 GLN A CA 1 ATOM 172 C C . GLN A 1 25 ? 48.395 42.262 42.445 1.00 19.92 ? 25 GLN A C 1 ATOM 173 O O . GLN A 1 25 ? 48.616 42.249 41.241 1.00 17.81 ? 25 GLN A O 1 ATOM 174 C CB . GLN A 1 25 ? 46.556 40.953 43.543 1.00 16.87 ? 25 GLN A CB 1 ATOM 175 C CG . GLN A 1 25 ? 46.054 39.604 44.047 1.00 17.06 ? 25 GLN A CG 1 ATOM 176 C CD . GLN A 1 25 ? 45.808 38.598 42.927 1.00 14.65 ? 25 GLN A CD 1 ATOM 177 O OE1 . GLN A 1 25 ? 46.553 38.565 41.936 1.00 15.06 ? 25 GLN A OE1 1 ATOM 178 N NE2 . GLN A 1 25 ? 44.806 37.766 43.125 1.00 19.14 ? 25 GLN A NE2 1 ATOM 179 N N . GLU A 1 26 ? 48.468 43.413 43.117 1.00 16.57 ? 26 GLU A N 1 ATOM 180 C CA . GLU A 1 26 ? 48.775 44.650 42.425 1.00 16.62 ? 26 GLU A CA 1 ATOM 181 C C . GLU A 1 26 ? 50.185 44.670 41.872 1.00 22.15 ? 26 GLU A C 1 ATOM 182 O O . GLU A 1 26 ? 50.368 45.173 40.759 1.00 19.34 ? 26 GLU A O 1 ATOM 183 C CB . GLU A 1 26 ? 48.544 45.828 43.391 1.00 21.88 ? 26 GLU A CB 1 ATOM 184 C CG . GLU A 1 26 ? 47.052 45.972 43.688 1.00 24.72 ? 26 GLU A CG 1 ATOM 185 C CD . GLU A 1 26 ? 46.710 46.556 45.039 1.00 45.06 ? 26 GLU A CD 1 ATOM 186 O OE1 . GLU A 1 26 ? 47.448 47.356 45.618 1.00 36.41 ? 26 GLU A OE1 1 ATOM 187 O OE2 . GLU A 1 26 ? 45.543 46.169 45.552 1.00 75.44 ? 26 GLU A OE2 1 ATOM 188 N N . THR A 1 27 ? 51.158 44.077 42.573 1.00 15.40 ? 27 THR A N 1 ATOM 189 C CA . THR A 1 27 ? 52.550 44.236 42.214 1.00 14.39 ? 27 THR A CA 1 ATOM 190 C C . THR A 1 27 ? 53.114 43.196 41.266 1.00 13.80 ? 27 THR A C 1 ATOM 191 O O . THR A 1 27 ? 53.835 43.540 40.317 1.00 16.34 ? 27 THR A O 1 ATOM 192 C CB . THR A 1 27 ? 53.440 44.246 43.491 1.00 13.19 ? 27 THR A CB 1 ATOM 193 O OG1 . THR A 1 27 ? 52.870 45.211 44.368 1.00 21.31 ? 27 THR A OG1 1 ATOM 194 C CG2 . THR A 1 27 ? 54.829 44.756 43.147 1.00 16.12 ? 27 THR A CG2 1 ATOM 195 N N . ILE A 1 28 ? 52.844 41.909 41.526 1.00 13.80 ? 28 ILE A N 1 ATOM 196 C CA . ILE A 1 28 ? 53.432 40.916 40.637 1.00 14.26 ? 28 ILE A CA 1 ATOM 197 C C . ILE A 1 28 ? 52.435 40.043 39.887 1.00 14.26 ? 28 ILE A C 1 ATOM 198 O O . ILE A 1 28 ? 52.843 39.528 38.836 1.00 17.28 ? 28 ILE A O 1 ATOM 199 C CB . ILE A 1 28 ? 54.443 40.011 41.384 1.00 15.79 ? 28 ILE A CB 1 ATOM 200 C CG1 . ILE A 1 28 ? 53.837 39.230 42.545 1.00 12.51 ? 28 ILE A CG1 1 ATOM 201 C CG2 . ILE A 1 28 ? 55.598 40.872 41.894 1.00 14.68 ? 28 ILE A CG2 1 ATOM 202 C CD1 . ILE A 1 28 ? 54.851 38.326 43.239 1.00 13.99 ? 28 ILE A CD1 1 ATOM 203 N N . PHE A 1 29 ? 51.194 39.848 40.298 1.00 14.78 ? 29 PHE A N 1 ATOM 204 C CA . PHE A 1 29 ? 50.322 38.954 39.521 1.00 14.30 ? 29 PHE A CA 1 ATOM 205 C C . PHE A 1 29 ? 49.313 39.724 38.670 1.00 17.93 ? 29 PHE A C 1 ATOM 206 O O . PHE A 1 29 ? 48.937 39.120 37.660 1.00 14.80 ? 29 PHE A O 1 ATOM 207 C CB . PHE A 1 29 ? 49.555 37.967 40.395 1.00 15.34 ? 29 PHE A CB 1 ATOM 208 C CG . PHE A 1 29 ? 50.404 37.133 41.355 1.00 14.22 ? 29 PHE A CG 1 ATOM 209 C CD1 . PHE A 1 29 ? 49.916 36.862 42.624 1.00 12.60 ? 29 PHE A CD1 1 ATOM 210 C CD2 . PHE A 1 29 ? 51.633 36.616 40.985 1.00 17.65 ? 29 PHE A CD2 1 ATOM 211 C CE1 . PHE A 1 29 ? 50.665 36.116 43.521 1.00 13.60 ? 29 PHE A CE1 1 ATOM 212 C CE2 . PHE A 1 29 ? 52.411 35.884 41.891 1.00 13.07 ? 29 PHE A CE2 1 ATOM 213 C CZ . PHE A 1 29 ? 51.918 35.639 43.157 1.00 12.13 ? 29 PHE A CZ 1 ATOM 214 N N . GLN A 1 30 ? 48.829 40.878 39.100 1.00 17.80 ? 30 GLN A N 1 ATOM 215 C CA . GLN A 1 30 ? 47.735 41.599 38.415 1.00 14.84 ? 30 GLN A CA 1 ATOM 216 C C . GLN A 1 30 ? 46.550 40.705 38.091 1.00 15.77 ? 30 GLN A C 1 ATOM 217 O O . GLN A 1 30 ? 45.904 40.811 37.034 1.00 18.81 ? 30 GLN A O 1 ATOM 218 C CB . GLN A 1 30 ? 48.247 42.262 37.136 1.00 15.66 ? 30 GLN A CB 1 ATOM 219 C CG . GLN A 1 30 ? 49.249 43.394 37.390 1.00 21.11 ? 30 GLN A CG 1 ATOM 220 C CD . GLN A 1 30 ? 50.671 42.895 37.570 1.00 20.35 ? 30 GLN A CD 1 ATOM 221 O OE1 . GLN A 1 30 ? 51.092 42.009 36.826 1.00 17.07 ? 30 GLN A OE1 1 ATOM 222 N NE2 . GLN A 1 30 ? 51.449 43.471 38.501 1.00 17.58 ? 30 GLN A NE2 1 ATOM 223 N N . ASN A 1 31 ? 46.195 39.862 39.057 1.00 16.34 ? 31 ASN A N 1 ATOM 224 C CA . ASN A 1 31 ? 45.048 38.982 38.986 1.00 16.68 ? 31 ASN A CA 1 ATOM 225 C C . ASN A 1 31 ? 45.062 38.058 37.785 1.00 15.08 ? 31 ASN A C 1 ATOM 226 O O . ASN A 1 31 ? 44.025 37.462 37.492 1.00 22.39 ? 31 ASN A O 1 ATOM 227 C CB . ASN A 1 31 ? 43.737 39.781 39.004 1.00 19.82 ? 31 ASN A CB 1 ATOM 228 C CG . ASN A 1 31 ? 43.675 40.660 40.254 1.00 23.12 ? 31 ASN A CG 1 ATOM 229 O OD1 . ASN A 1 31 ? 43.544 41.877 40.156 1.00 49.34 ? 31 ASN A OD1 1 ATOM 230 N ND2 . ASN A 1 31 ? 43.669 40.047 41.414 1.00 36.89 ? 31 ASN A ND2 1 ATOM 231 N N . GLU A 1 32 ? 46.217 37.856 37.171 1.00 13.39 ? 32 GLU A N 1 ATOM 232 C CA . GLU A 1 32 ? 46.392 36.934 36.052 1.00 17.41 ? 32 GLU A CA 1 ATOM 233 C C . GLU A 1 32 ? 47.097 35.636 36.495 1.00 20.08 ? 32 GLU A C 1 ATOM 234 O O . GLU A 1 32 ? 47.916 35.640 37.436 1.00 14.17 ? 32 GLU A O 1 ATOM 235 C CB . GLU A 1 32 ? 47.214 37.570 34.924 1.00 17.63 ? 32 GLU A CB 1 ATOM 236 C CG . GLU A 1 32 ? 46.686 38.867 34.345 1.00 19.22 ? 32 GLU A CG 1 ATOM 237 C CD . GLU A 1 32 ? 45.436 38.762 33.495 1.00 66.14 ? 32 GLU A CD 1 ATOM 238 O OE1 . GLU A 1 32 ? 44.820 39.818 33.186 1.00 38.89 ? 32 GLU A OE1 1 ATOM 239 O OE2 . GLU A 1 32 ? 44.984 37.655 33.110 1.00 33.57 ? 32 GLU A OE2 1 ATOM 240 N N . CYS A 1 33 ? 46.807 34.574 35.766 1.00 17.12 ? 33 CYS A N 1 ATOM 241 C CA . CYS A 1 33 ? 47.495 33.293 35.909 1.00 14.66 ? 33 CYS A CA 1 ATOM 242 C C . CYS A 1 33 ? 48.680 33.256 34.959 1.00 12.71 ? 33 CYS A C 1 ATOM 243 O O . CYS A 1 33 ? 48.771 32.385 34.075 1.00 15.41 ? 33 CYS A O 1 ATOM 244 C CB . CYS A 1 33 ? 46.518 32.150 35.620 1.00 18.59 ? 33 CYS A CB 1 ATOM 245 S SG . CYS A 1 33 ? 47.213 30.491 35.864 1.00 16.15 ? 33 CYS A SG 1 ATOM 246 N N . GLY A 1 34 ? 49.510 34.293 35.015 1.00 14.43 ? 34 GLY A N 1 ATOM 247 C CA . GLY A 1 34 ? 50.544 34.573 34.058 1.00 14.04 ? 34 GLY A CA 1 ATOM 248 C C . GLY A 1 34 ? 51.932 34.153 34.523 1.00 18.00 ? 34 GLY A C 1 ATOM 249 O O . GLY A 1 34 ? 52.078 33.383 35.470 1.00 16.24 ? 34 GLY A O 1 ATOM 250 N N . GLU A 1 35 ? 52.926 34.697 33.847 1.00 14.45 ? 35 GLU A N 1 ATOM 251 C CA . GLU A 1 35 ? 54.306 34.335 34.106 1.00 15.04 ? 35 GLU A CA 1 ATOM 252 C C . GLU A 1 35 ? 54.668 34.429 35.589 1.00 12.68 ? 35 GLU A C 1 ATOM 253 O O . GLU A 1 35 ? 55.221 33.479 36.161 1.00 14.66 ? 35 GLU A O 1 ATOM 254 C CB . GLU A 1 35 ? 55.230 35.250 33.288 1.00 18.02 ? 35 GLU A CB 1 ATOM 255 C CG . GLU A 1 35 ? 56.678 34.945 33.643 1.00 20.14 ? 35 GLU A CG 1 ATOM 256 C CD . GLU A 1 35 ? 57.310 33.891 32.763 1.00 36.53 ? 35 GLU A CD 1 ATOM 257 O OE1 . GLU A 1 35 ? 58.558 33.924 32.646 1.00 53.63 ? 35 GLU A OE1 1 ATOM 258 O OE2 . GLU A 1 35 ? 56.598 33.065 32.161 1.00 22.92 ? 35 GLU A OE2 1 ATOM 259 N N . ASP A 1 36 ? 54.346 35.548 36.229 1.00 13.84 ? 36 ASP A N 1 ATOM 260 C CA . ASP A 1 36 ? 54.828 35.693 37.606 1.00 15.74 ? 36 ASP A CA 1 ATOM 261 C C . ASP A 1 36 ? 54.058 34.725 38.502 1.00 14.67 ? 36 ASP A C 1 ATOM 262 O O . ASP A 1 36 ? 54.674 34.191 39.433 1.00 17.43 ? 36 ASP A O 1 ATOM 263 C CB . ASP A 1 36 ? 54.712 37.111 38.162 1.00 14.55 ? 36 ASP A CB 1 ATOM 264 C CG . ASP A 1 36 ? 55.801 38.038 37.647 1.00 21.13 ? 36 ASP A CG 1 ATOM 265 O OD1 . ASP A 1 36 ? 55.822 39.229 38.058 1.00 17.94 ? 36 ASP A OD1 1 ATOM 266 O OD2 . ASP A 1 36 ? 56.578 37.574 36.776 1.00 15.75 ? 36 ASP A OD2 1 ATOM 267 N N . ALA A 1 37 ? 52.774 34.550 38.241 1.00 12.23 ? 37 ALA A N 1 ATOM 268 C CA . ALA A 1 37 ? 51.948 33.561 38.946 1.00 14.68 ? 37 ALA A CA 1 ATOM 269 C C . ALA A 1 37 ? 52.577 32.174 38.784 1.00 22.06 ? 37 ALA A C 1 ATOM 270 O O . ALA A 1 37 ? 52.766 31.447 39.764 1.00 14.86 ? 37 ALA A O 1 ATOM 271 C CB . ALA A 1 37 ? 50.506 33.563 38.496 1.00 11.23 ? 37 ALA A CB 1 ATOM 272 N N . HIS A 1 38 ? 52.872 31.783 37.544 1.00 15.85 ? 38 HIS A N 1 ATOM 273 C CA . HIS A 1 38 ? 53.470 30.489 37.263 1.00 13.49 ? 38 HIS A CA 1 ATOM 274 C C . HIS A 1 38 ? 54.729 30.256 38.105 1.00 14.61 ? 38 HIS A C 1 ATOM 275 O O . HIS A 1 38 ? 54.889 29.169 38.684 1.00 15.80 ? 38 HIS A O 1 ATOM 276 C CB . HIS A 1 38 ? 53.834 30.355 35.781 1.00 15.85 ? 38 HIS A CB 1 ATOM 277 C CG . HIS A 1 38 ? 52.612 30.261 34.907 1.00 17.57 ? 38 HIS A CG 1 ATOM 278 N ND1 . HIS A 1 38 ? 52.691 30.407 33.539 1.00 17.10 ? 38 HIS A ND1 1 ATOM 279 C CD2 . HIS A 1 38 ? 51.307 30.100 35.210 1.00 19.48 ? 38 HIS A CD2 1 ATOM 280 C CE1 . HIS A 1 38 ? 51.471 30.242 33.029 1.00 13.72 ? 38 HIS A CE1 1 ATOM 281 N NE2 . HIS A 1 38 ? 50.603 30.081 34.025 1.00 14.92 ? 38 HIS A NE2 1 ATOM 282 N N . GLU A 1 39 ? 55.595 31.250 38.134 1.00 13.71 ? 39 GLU A N 1 ATOM 283 C CA . GLU A 1 39 ? 56.914 31.119 38.793 1.00 10.21 ? 39 GLU A CA 1 ATOM 284 C C . GLU A 1 39 ? 56.755 30.948 40.290 1.00 17.50 ? 39 GLU A C 1 ATOM 285 O O . GLU A 1 39 ? 57.462 30.114 40.886 1.00 16.32 ? 39 GLU A O 1 ATOM 286 C CB . GLU A 1 39 ? 57.734 32.372 38.446 1.00 11.32 ? 39 GLU A CB 1 ATOM 287 C CG . GLU A 1 39 ? 58.171 32.337 36.981 1.00 14.39 ? 39 GLU A CG 1 ATOM 288 C CD . GLU A 1 39 ? 59.291 33.279 36.602 1.00 31.61 ? 39 GLU A CD 1 ATOM 289 O OE1 . GLU A 1 39 ? 59.302 33.764 35.451 1.00 35.75 ? 39 GLU A OE1 1 ATOM 290 O OE2 . GLU A 1 39 ? 60.191 33.548 37.415 1.00 51.25 ? 39 GLU A OE2 1 ATOM 291 N N . VAL A 1 40 ? 55.798 31.664 40.865 1.00 13.31 ? 40 VAL A N 1 ATOM 292 C CA . VAL A 1 40 ? 55.560 31.517 42.317 1.00 15.00 ? 40 VAL A CA 1 ATOM 293 C C . VAL A 1 40 ? 54.964 30.169 42.635 1.00 16.05 ? 40 VAL A C 1 ATOM 294 O O . VAL A 1 40 ? 55.247 29.554 43.656 1.00 14.20 ? 40 VAL A O 1 ATOM 295 C CB . VAL A 1 40 ? 54.658 32.648 42.834 1.00 12.24 ? 40 VAL A CB 1 ATOM 296 C CG1 . VAL A 1 40 ? 54.131 32.407 44.224 1.00 13.01 ? 40 VAL A CG1 1 ATOM 297 C CG2 . VAL A 1 40 ? 55.521 33.917 42.846 1.00 13.70 ? 40 VAL A CG2 1 ATOM 298 N N . ILE A 1 41 ? 54.066 29.677 41.766 1.00 14.04 ? 41 ILE A N 1 ATOM 299 C CA . ILE A 1 41 ? 53.471 28.363 42.024 1.00 14.69 ? 41 ILE A CA 1 ATOM 300 C C . ILE A 1 41 ? 54.561 27.289 41.973 1.00 11.87 ? 41 ILE A C 1 ATOM 301 O O . ILE A 1 41 ? 54.573 26.453 42.881 1.00 15.54 ? 41 ILE A O 1 ATOM 302 C CB . ILE A 1 41 ? 52.350 28.035 41.026 1.00 13.26 ? 41 ILE A CB 1 ATOM 303 C CG1 . ILE A 1 41 ? 51.172 29.020 41.158 1.00 15.39 ? 41 ILE A CG1 1 ATOM 304 C CG2 . ILE A 1 41 ? 51.893 26.599 41.169 1.00 13.29 ? 41 ILE A CG2 1 ATOM 305 C CD1 . ILE A 1 41 ? 50.338 29.075 39.879 1.00 15.71 ? 41 ILE A CD1 1 ATOM 306 N N . ARG A 1 42 ? 55.488 27.386 41.030 1.00 11.46 ? 42 ARG A N 1 ATOM 307 C CA . ARG A 1 42 ? 56.587 26.407 41.044 1.00 13.43 ? 42 ARG A CA 1 ATOM 308 C C . ARG A 1 42 ? 57.414 26.577 42.316 1.00 17.05 ? 42 ARG A C 1 ATOM 309 O O . ARG A 1 42 ? 57.765 25.588 42.946 1.00 15.79 ? 42 ARG A O 1 ATOM 310 C CB A ARG A 1 42 ? 57.447 26.472 39.796 0.50 12.90 ? 42 ARG A CB 1 ATOM 311 C CB B ARG A 1 42 ? 57.425 26.683 39.801 0.50 11.91 ? 42 ARG A CB 1 ATOM 312 C CG A ARG A 1 42 ? 58.290 25.224 39.524 0.50 9.79 ? 42 ARG A CG 1 ATOM 313 C CG B ARG A 1 42 ? 58.678 25.848 39.629 0.50 13.41 ? 42 ARG A CG 1 ATOM 314 C CD A ARG A 1 42 ? 59.363 25.538 38.498 0.50 14.30 ? 42 ARG A CD 1 ATOM 315 C CD B ARG A 1 42 ? 59.241 26.047 38.221 0.50 14.62 ? 42 ARG A CD 1 ATOM 316 N NE A ARG A 1 42 ? 60.221 24.406 38.156 0.50 18.54 ? 42 ARG A NE 1 ATOM 317 N NE B ARG A 1 42 ? 60.618 25.594 38.159 0.50 20.06 ? 42 ARG A NE 1 ATOM 318 C CZ A ARG A 1 42 ? 61.499 24.587 37.826 0.50 16.04 ? 42 ARG A CZ 1 ATOM 319 C CZ B ARG A 1 42 ? 61.703 26.303 37.921 0.50 35.55 ? 42 ARG A CZ 1 ATOM 320 N NH1 A ARG A 1 42 ? 61.987 25.822 37.829 0.50 15.35 ? 42 ARG A NH1 1 ATOM 321 N NH1 B ARG A 1 42 ? 61.665 27.612 37.694 0.50 34.48 ? 42 ARG A NH1 1 ATOM 322 N NH2 A ARG A 1 42 ? 62.280 23.574 37.510 0.50 23.00 ? 42 ARG A NH2 1 ATOM 323 N NH2 B ARG A 1 42 ? 62.882 25.680 37.906 0.50 54.62 ? 42 ARG A NH2 1 ATOM 324 N N . LEU A 1 43 ? 57.685 27.808 42.764 1.00 16.56 ? 43 LEU A N 1 ATOM 325 C CA . LEU A 1 43 ? 58.440 27.981 44.023 1.00 16.06 ? 43 LEU A CA 1 ATOM 326 C C . LEU A 1 43 ? 57.773 27.293 45.204 1.00 14.91 ? 43 LEU A C 1 ATOM 327 O O . LEU A 1 43 ? 58.468 26.705 46.033 1.00 14.30 ? 43 LEU A O 1 ATOM 328 C CB . LEU A 1 43 ? 58.658 29.454 44.328 1.00 15.24 ? 43 LEU A CB 1 ATOM 329 C CG . LEU A 1 43 ? 59.362 29.828 45.643 1.00 14.33 ? 43 LEU A CG 1 ATOM 330 C CD1 . LEU A 1 43 ? 60.782 29.275 45.699 1.00 15.76 ? 43 LEU A CD1 1 ATOM 331 C CD2 . LEU A 1 43 ? 59.335 31.355 45.760 1.00 18.39 ? 43 LEU A CD2 1 ATOM 332 N N . THR A 1 44 ? 56.447 27.320 45.303 1.00 13.67 ? 44 THR A N 1 ATOM 333 C CA . THR A 1 44 ? 55.792 26.683 46.447 1.00 11.78 ? 44 THR A CA 1 ATOM 334 C C . THR A 1 44 ? 56.160 25.214 46.535 1.00 14.23 ? 44 THR A C 1 ATOM 335 O O . THR A 1 44 ? 56.440 24.692 47.613 1.00 15.25 ? 44 THR A O 1 ATOM 336 C CB . THR A 1 44 ? 54.258 26.852 46.505 1.00 16.86 ? 44 THR A CB 1 ATOM 337 O OG1 . THR A 1 44 ? 53.671 25.971 45.551 1.00 25.99 ? 44 THR A OG1 1 ATOM 338 C CG2 . THR A 1 44 ? 53.887 28.287 46.149 1.00 11.80 ? 44 THR A CG2 1 ATOM 339 N N . PHE A 1 45 ? 56.223 24.573 45.363 1.00 14.98 ? 45 PHE A N 1 ATOM 340 C CA . PHE A 1 45 ? 56.609 23.166 45.327 1.00 16.68 ? 45 PHE A CA 1 ATOM 341 C C . PHE A 1 45 ? 58.084 22.972 45.615 1.00 16.32 ? 45 PHE A C 1 ATOM 342 O O . PHE A 1 45 ? 58.421 22.107 46.435 1.00 16.08 ? 45 PHE A O 1 ATOM 343 C CB . PHE A 1 45 ? 56.229 22.591 43.960 1.00 15.24 ? 45 PHE A CB 1 ATOM 344 C CG . PHE A 1 45 ? 56.853 21.233 43.678 1.00 14.23 ? 45 PHE A CG 1 ATOM 345 C CD1 . PHE A 1 45 ? 57.630 21.072 42.537 1.00 20.00 ? 45 PHE A CD1 1 ATOM 346 C CD2 . PHE A 1 45 ? 56.647 20.151 44.506 1.00 19.97 ? 45 PHE A CD2 1 ATOM 347 C CE1 . PHE A 1 45 ? 58.218 19.861 42.229 1.00 19.69 ? 45 PHE A CE1 1 ATOM 348 C CE2 . PHE A 1 45 ? 57.279 18.954 44.223 1.00 19.26 ? 45 PHE A CE2 1 ATOM 349 C CZ . PHE A 1 45 ? 58.059 18.803 43.098 1.00 15.80 ? 45 PHE A CZ 1 ATOM 350 N N . HIS A 1 46 ? 58.998 23.714 44.995 1.00 11.47 ? 46 HIS A N 1 ATOM 351 C CA . HIS A 1 46 ? 60.424 23.508 45.282 1.00 14.65 ? 46 HIS A CA 1 ATOM 352 C C . HIS A 1 46 ? 60.729 23.871 46.738 1.00 18.48 ? 46 HIS A C 1 ATOM 353 O O . HIS A 1 46 ? 61.598 23.269 47.380 1.00 15.79 ? 46 HIS A O 1 ATOM 354 C CB . HIS A 1 46 ? 61.312 24.299 44.318 1.00 15.51 ? 46 HIS A CB 1 ATOM 355 C CG . HIS A 1 46 ? 61.302 23.777 42.911 1.00 17.35 ? 46 HIS A CG 1 ATOM 356 N ND1 . HIS A 1 46 ? 62.440 23.675 42.150 1.00 13.25 ? 46 HIS A ND1 1 ATOM 357 C CD2 . HIS A 1 46 ? 60.310 23.317 42.119 1.00 16.28 ? 46 HIS A CD2 1 ATOM 358 C CE1 . HIS A 1 46 ? 62.170 23.178 40.952 1.00 16.70 ? 46 HIS A CE1 1 ATOM 359 N NE2 . HIS A 1 46 ? 60.866 22.942 40.913 1.00 15.12 ? 46 HIS A NE2 1 ATOM 360 N N . ASP A 1 47 ? 60.047 24.871 47.310 1.00 15.71 ? 47 ASP A N 1 ATOM 361 C CA . ASP A 1 47 ? 60.343 25.169 48.718 1.00 13.77 ? 47 ASP A CA 1 ATOM 362 C C . ASP A 1 47 ? 59.926 23.955 49.551 1.00 19.85 ? 47 ASP A C 1 ATOM 363 O O . ASP A 1 47 ? 60.706 23.393 50.314 1.00 14.93 ? 47 ASP A O 1 ATOM 364 C CB . ASP A 1 47 ? 59.574 26.408 49.200 1.00 13.06 ? 47 ASP A CB 1 ATOM 365 C CG . ASP A 1 47 ? 60.021 26.805 50.606 1.00 13.52 ? 47 ASP A CG 1 ATOM 366 O OD1 . ASP A 1 47 ? 59.308 27.610 51.238 1.00 15.04 ? 47 ASP A OD1 1 ATOM 367 O OD2 . ASP A 1 47 ? 61.134 26.384 50.986 1.00 16.47 ? 47 ASP A OD2 1 ATOM 368 N N . ALA A 1 48 ? 58.690 23.513 49.356 1.00 11.30 ? 48 ALA A N 1 ATOM 369 C CA . ALA A 1 48 ? 58.077 22.504 50.202 1.00 11.25 ? 48 ALA A CA 1 ATOM 370 C C . ALA A 1 48 ? 58.734 21.132 50.050 1.00 13.88 ? 48 ALA A C 1 ATOM 371 O O . ALA A 1 48 ? 58.862 20.415 51.047 1.00 15.85 ? 48 ALA A O 1 ATOM 372 C CB . ALA A 1 48 ? 56.583 22.356 49.925 1.00 13.44 ? 48 ALA A CB 1 ATOM 373 N N . ILE A 1 49 ? 59.078 20.686 48.840 1.00 13.41 ? 49 ILE A N 1 ATOM 374 C CA . ILE A 1 49 ? 59.487 19.279 48.701 1.00 12.24 ? 49 ILE A CA 1 ATOM 375 C C . ILE A 1 49 ? 60.913 18.989 49.169 1.00 14.61 ? 49 ILE A C 1 ATOM 376 O O . ILE A 1 49 ? 61.269 17.801 49.251 1.00 15.67 ? 49 ILE A O 1 ATOM 377 C CB . ILE A 1 49 ? 59.282 18.880 47.222 1.00 12.84 ? 49 ILE A CB 1 ATOM 378 C CG1 . ILE A 1 49 ? 59.090 17.367 47.052 1.00 12.88 ? 49 ILE A CG1 1 ATOM 379 C CG2 . ILE A 1 49 ? 60.422 19.378 46.360 1.00 16.28 ? 49 ILE A CG2 1 ATOM 380 C CD1 . ILE A 1 49 ? 57.787 16.859 47.624 1.00 15.03 ? 49 ILE A CD1 1 ATOM 381 N N . ALA A 1 50 ? 61.705 20.012 49.523 1.00 13.15 ? 50 ALA A N 1 ATOM 382 C CA . ALA A 1 50 ? 63.102 19.788 49.914 1.00 12.82 ? 50 ALA A CA 1 ATOM 383 C C . ALA A 1 50 ? 63.161 19.372 51.378 1.00 16.89 ? 50 ALA A C 1 ATOM 384 O O . ALA A 1 50 ? 63.465 20.157 52.283 1.00 14.37 ? 50 ALA A O 1 ATOM 385 C CB . ALA A 1 50 ? 63.937 21.014 49.611 1.00 13.35 ? 50 ALA A CB 1 ATOM 386 N N . ILE A 1 51 ? 62.763 18.119 51.580 1.00 16.24 ? 51 ILE A N 1 ATOM 387 C CA . ILE A 1 51 ? 62.698 17.520 52.906 1.00 13.77 ? 51 ILE A CA 1 ATOM 388 C C . ILE A 1 51 ? 62.804 16.000 52.738 1.00 15.95 ? 51 ILE A C 1 ATOM 389 O O . ILE A 1 51 ? 62.402 15.480 51.685 1.00 16.93 ? 51 ILE A O 1 ATOM 390 C CB . ILE A 1 51 ? 61.393 17.841 53.643 1.00 12.89 ? 51 ILE A CB 1 ATOM 391 C CG1 . ILE A 1 51 ? 61.346 17.187 55.035 1.00 12.44 ? 51 ILE A CG1 1 ATOM 392 C CG2 . ILE A 1 51 ? 60.175 17.448 52.823 1.00 13.46 ? 51 ILE A CG2 1 ATOM 393 C CD1 . ILE A 1 51 ? 60.201 17.651 55.886 1.00 22.20 ? 51 ILE A CD1 1 ATOM 394 N N . SER A 1 52 ? 63.430 15.291 53.670 1.00 15.42 ? 52 SER A N 1 ATOM 395 C CA . SER A 1 52 ? 63.575 13.837 53.486 1.00 20.23 ? 52 SER A CA 1 ATOM 396 C C . SER A 1 52 ? 63.381 13.111 54.807 1.00 23.18 ? 52 SER A C 1 ATOM 397 O O . SER A 1 52 ? 64.092 13.336 55.798 1.00 18.67 ? 52 SER A O 1 ATOM 398 C CB . SER A 1 52 ? 64.941 13.512 52.903 1.00 18.77 ? 52 SER A CB 1 ATOM 399 O OG . SER A 1 52 ? 65.338 12.169 53.130 1.00 15.89 ? 52 SER A OG 1 ATOM 400 N N . ARG A 1 53 ? 62.411 12.202 54.851 1.00 21.72 ? 53 ARG A N 1 ATOM 401 C CA . ARG A 1 53 ? 62.229 11.430 56.085 1.00 18.52 ? 53 ARG A CA 1 ATOM 402 C C . ARG A 1 53 ? 63.476 10.597 56.334 1.00 19.48 ? 53 ARG A C 1 ATOM 403 O O . ARG A 1 53 ? 63.900 10.369 57.468 1.00 20.99 ? 53 ARG A O 1 ATOM 404 C CB . ARG A 1 53 ? 61.046 10.471 55.916 1.00 19.20 ? 53 ARG A CB 1 ATOM 405 C CG . ARG A 1 53 ? 59.726 11.194 55.751 1.00 17.64 ? 53 ARG A CG 1 ATOM 406 C CD . ARG A 1 53 ? 58.713 10.281 55.087 1.00 20.44 ? 53 ARG A CD 1 ATOM 407 N NE . ARG A 1 53 ? 57.364 10.500 55.596 1.00 37.07 ? 53 ARG A NE 1 ATOM 408 C CZ . ARG A 1 53 ? 56.399 9.604 55.374 1.00 53.59 ? 53 ARG A CZ 1 ATOM 409 N NH1 . ARG A 1 53 ? 56.614 8.492 54.676 1.00 33.70 ? 53 ARG A NH1 1 ATOM 410 N NH2 . ARG A 1 53 ? 55.189 9.830 55.858 1.00 34.48 ? 53 ARG A NH2 1 ATOM 411 N N . SER A 1 54 ? 64.046 10.069 55.250 1.00 20.22 ? 54 SER A N 1 ATOM 412 C CA . SER A 1 54 ? 65.120 9.095 55.490 1.00 23.28 ? 54 SER A CA 1 ATOM 413 C C . SER A 1 54 ? 66.425 9.767 55.873 1.00 21.93 ? 54 SER A C 1 ATOM 414 O O . SER A 1 54 ? 67.165 9.252 56.737 1.00 19.16 ? 54 SER A O 1 ATOM 415 C CB . SER A 1 54 ? 65.279 8.146 54.311 1.00 21.48 ? 54 SER A CB 1 ATOM 416 O OG . SER A 1 54 ? 65.732 8.780 53.144 1.00 23.32 ? 54 SER A OG 1 ATOM 417 N N . GLN A 1 55 ? 66.697 10.944 55.289 1.00 20.74 ? 55 GLN A N 1 ATOM 418 C CA . GLN A 1 55 ? 67.946 11.620 55.643 1.00 16.02 ? 55 GLN A CA 1 ATOM 419 C C . GLN A 1 55 ? 67.864 12.347 56.972 1.00 19.21 ? 55 GLN A C 1 ATOM 420 O O . GLN A 1 55 ? 68.900 12.594 57.598 1.00 25.94 ? 55 GLN A O 1 ATOM 421 C CB . GLN A 1 55 ? 68.439 12.576 54.558 1.00 19.53 ? 55 GLN A CB 1 ATOM 422 C CG . GLN A 1 55 ? 68.627 11.913 53.202 1.00 20.96 ? 55 GLN A CG 1 ATOM 423 C CD . GLN A 1 55 ? 69.063 12.931 52.159 1.00 44.02 ? 55 GLN A CD 1 ATOM 424 O OE1 . GLN A 1 55 ? 70.012 13.680 52.379 1.00 28.34 ? 55 GLN A OE1 1 ATOM 425 N NE2 . GLN A 1 55 ? 68.385 12.965 51.026 1.00 29.11 ? 55 GLN A NE2 1 ATOM 426 N N . GLY A 1 56 ? 66.675 12.709 57.422 1.00 19.77 ? 56 GLY A N 1 ATOM 427 C CA . GLY A 1 56 ? 66.563 13.496 58.642 1.00 18.70 ? 56 GLY A CA 1 ATOM 428 C C . GLY A 1 56 ? 66.522 14.997 58.374 1.00 25.00 ? 56 GLY A C 1 ATOM 429 O O . GLY A 1 56 ? 66.722 15.518 57.280 1.00 17.80 ? 56 GLY A O 1 ATOM 430 N N . PRO A 1 57 ? 66.229 15.725 59.444 1.00 16.11 ? 57 PRO A N 1 ATOM 431 C CA . PRO A 1 57 ? 66.011 17.165 59.404 1.00 18.09 ? 57 PRO A CA 1 ATOM 432 C C . PRO A 1 57 ? 67.169 17.943 58.799 1.00 14.99 ? 57 PRO A C 1 ATOM 433 O O . PRO A 1 57 ? 66.960 19.033 58.245 1.00 18.73 ? 57 PRO A O 1 ATOM 434 C CB . PRO A 1 57 ? 65.855 17.564 60.877 1.00 29.58 ? 57 PRO A CB 1 ATOM 435 C CG . PRO A 1 57 ? 65.457 16.309 61.576 1.00 29.39 ? 57 PRO A CG 1 ATOM 436 C CD . PRO A 1 57 ? 66.074 15.171 60.812 1.00 21.99 ? 57 PRO A CD 1 ATOM 437 N N . LYS A 1 58 ? 68.400 17.461 58.929 1.00 15.92 ? 58 LYS A N 1 ATOM 438 C CA . LYS A 1 58 ? 69.533 18.237 58.435 1.00 18.85 ? 58 LYS A CA 1 ATOM 439 C C . LYS A 1 58 ? 69.474 18.379 56.922 1.00 21.43 ? 58 LYS A C 1 ATOM 440 O O . LYS A 1 58 ? 70.155 19.208 56.334 1.00 19.58 ? 58 LYS A O 1 ATOM 441 C CB . LYS A 1 58 ? 70.824 17.484 58.796 1.00 25.96 ? 58 LYS A CB 1 ATOM 442 C CG . LYS A 1 58 ? 71.598 18.129 59.935 1.00 58.49 ? 58 LYS A CG 1 ATOM 443 C CD . LYS A 1 58 ? 71.317 17.487 61.279 1.00 60.47 ? 58 LYS A CD 1 ATOM 444 C CE . LYS A 1 58 ? 72.188 18.064 62.382 1.00 62.26 ? 58 LYS A CE 1 ATOM 445 N NZ . LYS A 1 58 ? 73.278 17.153 62.829 1.00 31.18 ? 58 LYS A NZ 1 ATOM 446 N N . ALA A 1 59 ? 68.694 17.515 56.260 1.00 16.83 ? 59 ALA A N 1 ATOM 447 C CA . ALA A 1 59 ? 68.695 17.572 54.794 1.00 16.32 ? 59 ALA A CA 1 ATOM 448 C C . ALA A 1 59 ? 67.785 18.698 54.311 1.00 14.43 ? 59 ALA A C 1 ATOM 449 O O . ALA A 1 59 ? 67.887 19.068 53.146 1.00 16.40 ? 59 ALA A O 1 ATOM 450 C CB . ALA A 1 59 ? 68.192 16.249 54.211 1.00 18.03 ? 59 ALA A CB 1 ATOM 451 N N . GLY A 1 60 ? 66.855 19.145 55.142 1.00 15.55 ? 60 GLY A N 1 ATOM 452 C CA . GLY A 1 60 ? 65.871 20.130 54.710 1.00 16.91 ? 60 GLY A CA 1 ATOM 453 C C . GLY A 1 60 ? 64.668 20.208 55.631 1.00 13.61 ? 60 GLY A C 1 ATOM 454 O O . GLY A 1 60 ? 64.165 19.241 56.196 1.00 15.94 ? 60 GLY A O 1 ATOM 455 N N . GLY A 1 61 ? 64.085 21.417 55.725 1.00 11.58 ? 61 GLY A N 1 ATOM 456 C CA . GLY A 1 61 ? 62.940 21.589 56.605 1.00 18.51 ? 61 GLY A CA 1 ATOM 457 C C . GLY A 1 61 ? 61.611 21.697 55.873 1.00 15.78 ? 61 GLY A C 1 ATOM 458 O O . GLY A 1 61 ? 60.625 22.089 56.511 1.00 14.49 ? 61 GLY A O 1 ATOM 459 N N . GLY A 1 62 ? 61.519 21.297 54.604 1.00 13.83 ? 62 GLY A N 1 ATOM 460 C CA . GLY A 1 62 ? 60.211 21.311 53.942 1.00 10.63 ? 62 GLY A CA 1 ATOM 461 C C . GLY A 1 62 ? 59.712 22.717 53.597 1.00 14.04 ? 62 GLY A C 1 ATOM 462 O O . GLY A 1 62 ? 60.488 23.561 53.129 1.00 12.97 ? 62 GLY A O 1 ATOM 463 N N . ALA A 1 63 ? 58.427 23.011 53.827 1.00 14.08 ? 63 ALA A N 1 ATOM 464 C CA . ALA A 1 63 ? 57.814 24.297 53.504 1.00 11.67 ? 63 ALA A CA 1 ATOM 465 C C . ALA A 1 63 ? 58.216 25.310 54.578 1.00 11.42 ? 63 ALA A C 1 ATOM 466 O O . ALA A 1 63 ? 57.430 25.554 55.495 1.00 14.29 ? 63 ALA A O 1 ATOM 467 C CB . ALA A 1 63 ? 56.285 24.191 53.453 1.00 12.36 ? 63 ALA A CB 1 ATOM 468 N N . ASP A 1 64 ? 59.441 25.793 54.473 1.00 12.62 ? 64 ASP A N 1 ATOM 469 C CA . ASP A 1 64 ? 60.079 26.546 55.569 1.00 12.13 ? 64 ASP A CA 1 ATOM 470 C C . ASP A 1 64 ? 60.682 27.837 55.052 1.00 15.20 ? 64 ASP A C 1 ATOM 471 O O . ASP A 1 64 ? 61.401 28.565 55.750 1.00 16.42 ? 64 ASP A O 1 ATOM 472 C CB . ASP A 1 64 ? 61.154 25.620 56.180 1.00 14.88 ? 64 ASP A CB 1 ATOM 473 C CG . ASP A 1 64 ? 62.298 25.320 55.233 1.00 19.94 ? 64 ASP A CG 1 ATOM 474 O OD1 . ASP A 1 64 ? 62.207 25.684 54.035 1.00 12.38 ? 64 ASP A OD1 1 ATOM 475 O OD2 . ASP A 1 64 ? 63.295 24.699 55.661 1.00 16.48 ? 64 ASP A OD2 1 ATOM 476 N N . GLY A 1 65 ? 60.381 28.215 53.786 1.00 12.09 ? 65 GLY A N 1 ATOM 477 C CA . GLY A 1 65 ? 60.927 29.478 53.309 1.00 12.79 ? 65 GLY A CA 1 ATOM 478 C C . GLY A 1 65 ? 62.424 29.484 53.110 1.00 9.40 ? 65 GLY A C 1 ATOM 479 O O . GLY A 1 65 ? 63.054 30.551 52.922 1.00 14.15 ? 65 GLY A O 1 ATOM 480 N N . SER A 1 66 ? 63.061 28.306 53.051 1.00 13.98 ? 66 SER A N 1 ATOM 481 C CA . SER A 1 66 ? 64.521 28.197 52.923 1.00 14.25 ? 66 SER A CA 1 ATOM 482 C C . SER A 1 66 ? 65.005 28.816 51.619 1.00 13.34 ? 66 SER A C 1 ATOM 483 O O . SER A 1 66 ? 66.095 29.378 51.501 1.00 17.91 ? 66 SER A O 1 ATOM 484 C CB . SER A 1 66 ? 64.940 26.724 53.012 1.00 14.62 ? 66 SER A CB 1 ATOM 485 O OG . SER A 1 66 ? 64.400 25.941 51.935 1.00 15.45 ? 66 SER A OG 1 ATOM 486 N N . MET A 1 67 ? 64.126 28.800 50.596 1.00 12.86 ? 67 MET A N 1 ATOM 487 C CA . MET A 1 67 ? 64.575 29.412 49.332 1.00 11.29 ? 67 MET A CA 1 ATOM 488 C C . MET A 1 67 ? 64.756 30.921 49.477 1.00 11.90 ? 67 MET A C 1 ATOM 489 O O . MET A 1 67 ? 65.590 31.504 48.775 1.00 15.15 ? 67 MET A O 1 ATOM 490 C CB . MET A 1 67 ? 63.491 29.142 48.272 1.00 14.76 ? 67 MET A CB 1 ATOM 491 C CG . MET A 1 67 ? 63.408 27.632 47.948 1.00 13.55 ? 67 MET A CG 1 ATOM 492 S SD . MET A 1 67 ? 64.619 27.286 46.652 1.00 18.93 ? 67 MET A SD 1 ATOM 493 C CE . MET A 1 67 ? 64.384 25.556 46.291 1.00 16.31 ? 67 MET A CE 1 ATOM 494 N N . LEU A 1 68 ? 63.937 31.583 50.298 1.00 12.91 ? 68 LEU A N 1 ATOM 495 C CA . LEU A 1 68 ? 64.027 33.014 50.527 1.00 11.66 ? 68 LEU A CA 1 ATOM 496 C C . LEU A 1 68 ? 65.083 33.340 51.595 1.00 14.41 ? 68 LEU A C 1 ATOM 497 O O . LEU A 1 68 ? 65.773 34.348 51.458 1.00 16.15 ? 68 LEU A O 1 ATOM 498 C CB . LEU A 1 68 ? 62.729 33.660 51.034 1.00 14.17 ? 68 LEU A CB 1 ATOM 499 C CG . LEU A 1 68 ? 61.414 33.375 50.320 1.00 27.93 ? 68 LEU A CG 1 ATOM 500 C CD1 . LEU A 1 68 ? 60.356 34.395 50.711 1.00 13.64 ? 68 LEU A CD1 1 ATOM 501 C CD2 . LEU A 1 68 ? 61.551 33.315 48.810 1.00 22.04 ? 68 LEU A CD2 1 ATOM 502 N N . LEU A 1 69 ? 65.160 32.517 52.646 1.00 15.91 ? 69 LEU A N 1 ATOM 503 C CA . LEU A 1 69 ? 66.117 32.824 53.712 1.00 15.23 ? 69 LEU A CA 1 ATOM 504 C C . LEU A 1 69 ? 67.560 32.511 53.357 1.00 14.13 ? 69 LEU A C 1 ATOM 505 O O . LEU A 1 69 ? 68.504 33.077 53.946 1.00 15.54 ? 69 LEU A O 1 ATOM 506 C CB . LEU A 1 69 ? 65.652 32.071 54.977 1.00 17.45 ? 69 LEU A CB 1 ATOM 507 C CG . LEU A 1 69 ? 64.292 32.569 55.499 1.00 12.15 ? 69 LEU A CG 1 ATOM 508 C CD1 . LEU A 1 69 ? 63.783 31.678 56.619 1.00 23.11 ? 69 LEU A CD1 1 ATOM 509 C CD2 . LEU A 1 69 ? 64.406 34.027 55.925 1.00 13.39 ? 69 LEU A CD2 1 ATOM 510 N N . PHE A 1 70 ? 67.782 31.579 52.427 1.00 12.75 ? 70 PHE A N 1 ATOM 511 C CA . PHE A 1 70 ? 69.131 31.243 51.969 1.00 12.68 ? 70 PHE A CA 1 ATOM 512 C C . PHE A 1 70 ? 69.136 31.318 50.449 1.00 16.17 ? 70 PHE A C 1 ATOM 513 O O . PHE A 1 70 ? 69.311 30.350 49.718 1.00 16.23 ? 70 PHE A O 1 ATOM 514 C CB . PHE A 1 70 ? 69.547 29.838 52.443 1.00 14.74 ? 70 PHE A CB 1 ATOM 515 C CG . PHE A 1 70 ? 69.554 29.709 53.968 1.00 15.39 ? 70 PHE A CG 1 ATOM 516 C CD1 . PHE A 1 70 ? 70.695 29.992 54.727 1.00 15.29 ? 70 PHE A CD1 1 ATOM 517 C CD2 . PHE A 1 70 ? 68.424 29.320 54.656 1.00 15.88 ? 70 PHE A CD2 1 ATOM 518 C CE1 . PHE A 1 70 ? 70.634 29.847 56.096 1.00 14.44 ? 70 PHE A CE1 1 ATOM 519 C CE2 . PHE A 1 70 ? 68.339 29.213 56.036 1.00 17.93 ? 70 PHE A CE2 1 ATOM 520 C CZ . PHE A 1 70 ? 69.477 29.504 56.764 1.00 18.99 ? 70 PHE A CZ 1 ATOM 521 N N . PRO A 1 71 ? 68.941 32.524 49.922 1.00 14.99 ? 71 PRO A N 1 ATOM 522 C CA . PRO A 1 71 ? 68.703 32.677 48.491 1.00 13.66 ? 71 PRO A CA 1 ATOM 523 C C . PRO A 1 71 ? 69.886 32.328 47.622 1.00 15.44 ? 71 PRO A C 1 ATOM 524 O O . PRO A 1 71 ? 69.725 32.148 46.409 1.00 17.01 ? 71 PRO A O 1 ATOM 525 C CB . PRO A 1 71 ? 68.354 34.165 48.359 1.00 13.26 ? 71 PRO A CB 1 ATOM 526 C CG . PRO A 1 71 ? 69.079 34.804 49.513 1.00 16.83 ? 71 PRO A CG 1 ATOM 527 C CD . PRO A 1 71 ? 68.912 33.816 50.644 1.00 13.61 ? 71 PRO A CD 1 ATOM 528 N N . THR A 1 72 ? 71.095 32.230 48.201 1.00 13.74 ? 72 THR A N 1 ATOM 529 C CA . THR A 1 72 ? 72.230 31.860 47.365 1.00 14.90 ? 72 THR A CA 1 ATOM 530 C C . THR A 1 72 ? 72.568 30.378 47.376 1.00 16.24 ? 72 THR A C 1 ATOM 531 O O . THR A 1 72 ? 73.529 29.970 46.695 1.00 16.38 ? 72 THR A O 1 ATOM 532 C CB . THR A 1 72 ? 73.518 32.612 47.791 1.00 18.43 ? 72 THR A CB 1 ATOM 533 O OG1 . THR A 1 72 ? 73.912 32.144 49.093 1.00 19.97 ? 72 THR A OG1 1 ATOM 534 C CG2 . THR A 1 72 ? 73.243 34.096 47.885 1.00 18.21 ? 72 THR A CG2 1 ATOM 535 N N . VAL A 1 73 ? 71.825 29.552 48.092 1.00 16.64 ? 73 VAL A N 1 ATOM 536 C CA . VAL A 1 73 ? 72.152 28.123 48.188 1.00 14.87 ? 73 VAL A CA 1 ATOM 537 C C . VAL A 1 73 ? 71.298 27.321 47.210 1.00 12.46 ? 73 VAL A C 1 ATOM 538 O O . VAL A 1 73 ? 71.759 27.053 46.106 1.00 18.49 ? 73 VAL A O 1 ATOM 539 C CB . VAL A 1 73 ? 71.958 27.654 49.645 1.00 20.70 ? 73 VAL A CB 1 ATOM 540 C CG1 . VAL A 1 73 ? 72.314 26.188 49.831 1.00 17.41 ? 73 VAL A CG1 1 ATOM 541 C CG2 . VAL A 1 73 ? 72.804 28.511 50.582 1.00 18.38 ? 73 VAL A CG2 1 ATOM 542 N N . GLU A 1 74 ? 70.089 26.927 47.618 1.00 15.16 ? 74 GLU A N 1 ATOM 543 C CA . GLU A 1 74 ? 69.197 26.101 46.821 1.00 12.71 ? 74 GLU A CA 1 ATOM 544 C C . GLU A 1 74 ? 68.855 26.668 45.443 1.00 12.55 ? 74 GLU A C 1 ATOM 545 O O . GLU A 1 74 ? 68.896 25.860 44.501 1.00 15.45 ? 74 GLU A O 1 ATOM 546 C CB . GLU A 1 74 ? 67.878 25.789 47.537 1.00 12.99 ? 74 GLU A CB 1 ATOM 547 C CG . GLU A 1 74 ? 68.085 24.921 48.787 1.00 17.98 ? 74 GLU A CG 1 ATOM 548 C CD . GLU A 1 74 ? 66.789 24.833 49.575 1.00 18.86 ? 74 GLU A CD 1 ATOM 549 O OE1 . GLU A 1 74 ? 66.661 25.506 50.614 1.00 13.34 ? 74 GLU A OE1 1 ATOM 550 O OE2 . GLU A 1 74 ? 65.860 24.157 49.074 1.00 14.08 ? 74 GLU A OE2 1 ATOM 551 N N . PRO A 1 75 ? 68.570 27.949 45.287 1.00 16.32 ? 75 PRO A N 1 ATOM 552 C CA . PRO A 1 75 ? 68.237 28.453 43.942 1.00 14.30 ? 75 PRO A CA 1 ATOM 553 C C . PRO A 1 75 ? 69.348 28.221 42.938 1.00 17.31 ? 75 PRO A C 1 ATOM 554 O O . PRO A 1 75 ? 69.062 28.229 41.735 1.00 19.12 ? 75 PRO A O 1 ATOM 555 C CB . PRO A 1 75 ? 68.049 29.963 44.160 1.00 15.59 ? 75 PRO A CB 1 ATOM 556 C CG . PRO A 1 75 ? 67.588 30.063 45.586 1.00 16.52 ? 75 PRO A CG 1 ATOM 557 C CD . PRO A 1 75 ? 68.420 29.013 46.290 1.00 15.74 ? 75 PRO A CD 1 ATOM 558 N N . ASN A 1 76 ? 70.584 28.012 43.400 1.00 13.98 ? 76 ASN A N 1 ATOM 559 C CA . ASN A 1 76 ? 71.698 27.762 42.506 1.00 14.55 ? 76 ASN A CA 1 ATOM 560 C C . ASN A 1 76 ? 71.933 26.286 42.249 1.00 18.17 ? 76 ASN A C 1 ATOM 561 O O . ASN A 1 76 ? 72.896 25.927 41.544 1.00 22.34 ? 76 ASN A O 1 ATOM 562 C CB . ASN A 1 76 ? 72.988 28.369 43.087 1.00 23.17 ? 76 ASN A CB 1 ATOM 563 C CG . ASN A 1 76 ? 73.073 29.865 42.881 1.00 52.66 ? 76 ASN A CG 1 ATOM 564 O OD1 . ASN A 1 76 ? 73.343 30.645 43.800 1.00 38.46 ? 76 ASN A OD1 1 ATOM 565 N ND2 . ASN A 1 76 ? 72.862 30.225 41.618 1.00 40.55 ? 76 ASN A ND2 1 ATOM 566 N N . PHE A 1 77 ? 71.150 25.384 42.820 1.00 16.38 ? 77 PHE A N 1 ATOM 567 C CA . PHE A 1 77 ? 71.338 23.982 42.469 1.00 14.77 ? 77 PHE A CA 1 ATOM 568 C C . PHE A 1 77 ? 70.799 23.826 41.036 1.00 21.15 ? 77 PHE A C 1 ATOM 569 O O . PHE A 1 77 ? 69.839 24.493 40.660 1.00 14.57 ? 77 PHE A O 1 ATOM 570 C CB . PHE A 1 77 ? 70.564 23.011 43.342 1.00 13.70 ? 77 PHE A CB 1 ATOM 571 C CG . PHE A 1 77 ? 70.950 23.003 44.816 1.00 15.32 ? 77 PHE A CG 1 ATOM 572 C CD1 . PHE A 1 77 ? 72.235 23.375 45.208 1.00 20.38 ? 77 PHE A CD1 1 ATOM 573 C CD2 . PHE A 1 77 ? 70.003 22.659 45.766 1.00 14.93 ? 77 PHE A CD2 1 ATOM 574 C CE1 . PHE A 1 77 ? 72.573 23.380 46.553 1.00 18.60 ? 77 PHE A CE1 1 ATOM 575 C CE2 . PHE A 1 77 ? 70.357 22.580 47.107 1.00 16.91 ? 77 PHE A CE2 1 ATOM 576 C CZ . PHE A 1 77 ? 71.632 22.972 47.480 1.00 14.26 ? 77 PHE A CZ 1 ATOM 577 N N . SER A 1 78 ? 71.391 22.931 40.272 1.00 17.12 ? 78 SER A N 1 ATOM 578 C CA . SER A 1 78 ? 70.943 22.840 38.870 1.00 14.18 ? 78 SER A CA 1 ATOM 579 C C . SER A 1 78 ? 69.476 22.466 38.784 1.00 16.02 ? 78 SER A C 1 ATOM 580 O O . SER A 1 78 ? 68.736 23.004 37.956 1.00 17.73 ? 78 SER A O 1 ATOM 581 C CB . SER A 1 78 ? 71.835 21.823 38.139 1.00 22.34 ? 78 SER A CB 1 ATOM 582 O OG . SER A 1 78 ? 71.777 20.574 38.812 1.00 31.24 ? 78 SER A OG 1 ATOM 583 N N . ALA A 1 79 ? 68.924 21.630 39.648 1.00 15.62 ? 79 ALA A N 1 ATOM 584 C CA . ALA A 1 79 ? 67.496 21.278 39.570 1.00 15.09 ? 79 ALA A CA 1 ATOM 585 C C . ALA A 1 79 ? 66.572 22.445 39.862 1.00 15.52 ? 79 ALA A C 1 ATOM 586 O O . ALA A 1 79 ? 65.380 22.394 39.574 1.00 14.91 ? 79 ALA A O 1 ATOM 587 C CB . ALA A 1 79 ? 67.186 20.118 40.509 1.00 16.11 ? 79 ALA A CB 1 ATOM 588 N N . ASN A 1 80 ? 67.084 23.493 40.508 1.00 15.79 ? 80 ASN A N 1 ATOM 589 C CA . ASN A 1 80 ? 66.339 24.700 40.799 1.00 16.53 ? 80 ASN A CA 1 ATOM 590 C C . ASN A 1 80 ? 66.600 25.800 39.779 1.00 17.19 ? 80 ASN A C 1 ATOM 591 O O . ASN A 1 80 ? 66.260 26.952 40.048 1.00 21.01 ? 80 ASN A O 1 ATOM 592 C CB . ASN A 1 80 ? 66.717 25.221 42.212 1.00 15.14 ? 80 ASN A CB 1 ATOM 593 C CG . ASN A 1 80 ? 66.115 24.306 43.263 1.00 15.91 ? 80 ASN A CG 1 ATOM 594 O OD1 . ASN A 1 80 ? 64.965 23.856 43.166 1.00 16.71 ? 80 ASN A OD1 1 ATOM 595 N ND2 . ASN A 1 80 ? 66.896 23.931 44.271 1.00 13.12 ? 80 ASN A ND2 1 ATOM 596 N N . ASN A 1 81 ? 67.153 25.500 38.617 1.00 16.65 ? 81 ASN A N 1 ATOM 597 C CA . ASN A 1 81 ? 67.379 26.525 37.582 1.00 16.44 ? 81 ASN A CA 1 ATOM 598 C C . ASN A 1 81 ? 66.085 27.248 37.226 1.00 17.63 ? 81 ASN A C 1 ATOM 599 O O . ASN A 1 81 ? 65.088 26.558 37.040 1.00 17.86 ? 81 ASN A O 1 ATOM 600 C CB . ASN A 1 81 ? 67.916 25.814 36.337 1.00 18.07 ? 81 ASN A CB 1 ATOM 601 C CG . ASN A 1 81 ? 68.617 26.792 35.410 1.00 27.51 ? 81 ASN A CG 1 ATOM 602 O OD1 . ASN A 1 81 ? 68.808 27.964 35.734 1.00 20.65 ? 81 ASN A OD1 1 ATOM 603 N ND2 . ASN A 1 81 ? 68.946 26.261 34.235 1.00 25.72 ? 81 ASN A ND2 1 ATOM 604 N N . GLY A 1 82 ? 66.088 28.566 37.270 1.00 21.01 ? 82 GLY A N 1 ATOM 605 C CA . GLY A 1 82 ? 64.965 29.431 36.937 1.00 14.29 ? 82 GLY A CA 1 ATOM 606 C C . GLY A 1 82 ? 64.208 29.888 38.155 1.00 22.04 ? 82 GLY A C 1 ATOM 607 O O . GLY A 1 82 ? 63.394 30.810 38.116 1.00 16.06 ? 82 GLY A O 1 ATOM 608 N N . ILE A 1 83 ? 64.418 29.234 39.293 1.00 14.52 ? 83 ILE A N 1 ATOM 609 C CA . ILE A 1 83 ? 63.673 29.611 40.499 1.00 16.52 ? 83 ILE A CA 1 ATOM 610 C C . ILE A 1 83 ? 64.108 30.966 41.052 1.00 18.21 ? 83 ILE A C 1 ATOM 611 O O . ILE A 1 83 ? 63.355 31.595 41.803 1.00 15.77 ? 83 ILE A O 1 ATOM 612 C CB A ILE A 1 83 ? 63.830 28.539 41.597 0.50 17.13 ? 83 ILE A CB 1 ATOM 613 C CB B ILE A 1 83 ? 63.964 28.507 41.548 0.50 21.30 ? 83 ILE A CB 1 ATOM 614 C CG1 A ILE A 1 83 ? 62.558 28.304 42.408 0.50 20.56 ? 83 ILE A CG1 1 ATOM 615 C CG1 B ILE A 1 83 ? 63.306 27.177 41.182 0.50 11.89 ? 83 ILE A CG1 1 ATOM 616 C CG2 A ILE A 1 83 ? 65.014 28.911 42.475 0.50 14.44 ? 83 ILE A CG2 1 ATOM 617 C CG2 B ILE A 1 83 ? 63.678 28.914 42.974 0.50 10.50 ? 83 ILE A CG2 1 ATOM 618 C CD1 A ILE A 1 83 ? 61.341 28.012 41.555 0.50 35.55 ? 83 ILE A CD1 1 ATOM 619 C CD1 B ILE A 1 83 ? 61.840 27.077 41.515 0.50 13.76 ? 83 ILE A CD1 1 ATOM 620 N N . ASP A 1 84 ? 65.298 31.437 40.672 1.00 14.05 ? 84 ASP A N 1 ATOM 621 C CA . ASP A 1 84 ? 65.787 32.716 41.187 1.00 14.02 ? 84 ASP A CA 1 ATOM 622 C C . ASP A 1 84 ? 64.808 33.865 40.980 1.00 22.43 ? 84 ASP A C 1 ATOM 623 O O . ASP A 1 84 ? 64.605 34.682 41.896 1.00 16.90 ? 84 ASP A O 1 ATOM 624 C CB . ASP A 1 84 ? 67.118 33.143 40.563 1.00 15.76 ? 84 ASP A CB 1 ATOM 625 C CG . ASP A 1 84 ? 67.122 33.095 39.053 1.00 21.37 ? 84 ASP A CG 1 ATOM 626 O OD1 . ASP A 1 84 ? 68.176 33.447 38.473 1.00 25.91 ? 84 ASP A OD1 1 ATOM 627 O OD2 . ASP A 1 84 ? 66.127 32.679 38.418 1.00 21.83 ? 84 ASP A OD2 1 ATOM 628 N N . ASP A 1 85 ? 64.177 33.984 39.811 1.00 19.81 ? 85 ASP A N 1 ATOM 629 C CA . ASP A 1 85 ? 63.223 35.096 39.643 1.00 19.57 ? 85 ASP A CA 1 ATOM 630 C C . ASP A 1 85 ? 62.118 35.132 40.690 1.00 13.31 ? 85 ASP A C 1 ATOM 631 O O . ASP A 1 85 ? 61.787 36.210 41.220 1.00 17.86 ? 85 ASP A O 1 ATOM 632 C CB . ASP A 1 85 ? 62.591 35.005 38.246 1.00 21.20 ? 85 ASP A CB 1 ATOM 633 C CG . ASP A 1 85 ? 63.530 35.488 37.146 1.00 25.69 ? 85 ASP A CG 1 ATOM 634 O OD1 . ASP A 1 85 ? 64.623 36.030 37.414 1.00 23.92 ? 85 ASP A OD1 1 ATOM 635 O OD2 . ASP A 1 85 ? 63.139 35.278 35.975 1.00 57.53 ? 85 ASP A OD2 1 ATOM 636 N N . SER A 1 86 ? 61.482 34.009 41.022 1.00 11.00 ? 86 SER A N 1 ATOM 637 C CA . SER A 1 86 ? 60.402 33.972 42.001 1.00 11.82 ? 86 SER A CA 1 ATOM 638 C C . SER A 1 86 ? 60.907 34.333 43.399 1.00 17.40 ? 86 SER A C 1 ATOM 639 O O . SER A 1 86 ? 60.264 35.034 44.178 1.00 16.43 ? 86 SER A O 1 ATOM 640 C CB . SER A 1 86 ? 59.717 32.617 42.083 1.00 16.07 ? 86 SER A CB 1 ATOM 641 O OG . SER A 1 86 ? 60.585 31.542 42.382 1.00 17.36 ? 86 SER A OG 1 ATOM 642 N N . VAL A 1 87 ? 62.087 33.823 43.752 1.00 15.64 ? 87 VAL A N 1 ATOM 643 C CA . VAL A 1 87 ? 62.650 34.175 45.057 1.00 12.80 ? 87 VAL A CA 1 ATOM 644 C C . VAL A 1 87 ? 62.927 35.670 45.141 1.00 12.74 ? 87 VAL A C 1 ATOM 645 O O . VAL A 1 87 ? 62.584 36.335 46.133 1.00 17.13 ? 87 VAL A O 1 ATOM 646 C CB . VAL A 1 87 ? 63.991 33.417 45.223 1.00 13.80 ? 87 VAL A CB 1 ATOM 647 C CG1 . VAL A 1 87 ? 64.794 34.070 46.336 1.00 11.69 ? 87 VAL A CG1 1 ATOM 648 C CG2 . VAL A 1 87 ? 63.674 31.949 45.523 1.00 15.20 ? 87 VAL A CG2 1 ATOM 649 N N . ASN A 1 88 ? 63.594 36.222 44.126 1.00 16.58 ? 88 ASN A N 1 ATOM 650 C CA . ASN A 1 88 ? 63.822 37.669 44.117 1.00 17.17 ? 88 ASN A CA 1 ATOM 651 C C . ASN A 1 88 ? 62.509 38.430 44.066 1.00 21.26 ? 88 ASN A C 1 ATOM 652 O O . ASN A 1 88 ? 62.459 39.560 44.563 1.00 15.87 ? 88 ASN A O 1 ATOM 653 C CB . ASN A 1 88 ? 64.716 38.070 42.951 1.00 13.85 ? 88 ASN A CB 1 ATOM 654 C CG . ASN A 1 88 ? 66.119 37.509 43.163 1.00 14.82 ? 88 ASN A CG 1 ATOM 655 O OD1 . ASN A 1 88 ? 66.531 37.301 44.308 1.00 19.60 ? 88 ASN A OD1 1 ATOM 656 N ND2 . ASN A 1 88 ? 66.838 37.331 42.067 1.00 19.33 ? 88 ASN A ND2 1 ATOM 657 N N . ASN A 1 89 ? 61.449 37.917 43.431 1.00 14.64 ? 89 ASN A N 1 ATOM 658 C CA . ASN A 1 89 ? 60.183 38.667 43.508 1.00 13.36 ? 89 ASN A CA 1 ATOM 659 C C . ASN A 1 89 ? 59.523 38.627 44.886 1.00 17.97 ? 89 ASN A C 1 ATOM 660 O O . ASN A 1 89 ? 58.792 39.552 45.258 1.00 18.55 ? 89 ASN A O 1 ATOM 661 C CB . ASN A 1 89 ? 59.162 38.087 42.504 1.00 14.38 ? 89 ASN A CB 1 ATOM 662 C CG . ASN A 1 89 ? 59.287 38.804 41.171 1.00 19.49 ? 89 ASN A CG 1 ATOM 663 O OD1 . ASN A 1 89 ? 60.000 39.796 41.069 1.00 15.10 ? 89 ASN A OD1 1 ATOM 664 N ND2 . ASN A 1 89 ? 58.566 38.343 40.161 1.00 16.50 ? 89 ASN A ND2 1 ATOM 665 N N . LEU A 1 90 ? 59.684 37.552 45.676 1.00 12.62 ? 90 LEU A N 1 ATOM 666 C CA . LEU A 1 90 ? 59.006 37.510 46.970 1.00 12.82 ? 90 LEU A CA 1 ATOM 667 C C . LEU A 1 90 ? 59.812 38.127 48.108 1.00 10.16 ? 90 LEU A C 1 ATOM 668 O O . LEU A 1 90 ? 59.229 38.571 49.110 1.00 12.51 ? 90 LEU A O 1 ATOM 669 C CB . LEU A 1 90 ? 58.741 36.020 47.310 1.00 13.58 ? 90 LEU A CB 1 ATOM 670 C CG . LEU A 1 90 ? 57.619 35.385 46.499 1.00 12.22 ? 90 LEU A CG 1 ATOM 671 C CD1 . LEU A 1 90 ? 57.154 34.082 47.142 1.00 15.12 ? 90 LEU A CD1 1 ATOM 672 C CD2 . LEU A 1 90 ? 56.401 36.322 46.464 1.00 12.63 ? 90 LEU A CD2 1 ATOM 673 N N . ILE A 1 91 ? 61.141 38.143 48.022 1.00 14.60 ? 91 ILE A N 1 ATOM 674 C CA . ILE A 1 91 ? 61.923 38.743 49.122 1.00 11.92 ? 91 ILE A CA 1 ATOM 675 C C . ILE A 1 91 ? 61.505 40.152 49.474 1.00 15.87 ? 91 ILE A C 1 ATOM 676 O O . ILE A 1 91 ? 61.427 40.446 50.675 1.00 16.04 ? 91 ILE A O 1 ATOM 677 C CB . ILE A 1 91 ? 63.421 38.688 48.805 1.00 16.45 ? 91 ILE A CB 1 ATOM 678 C CG1 . ILE A 1 91 ? 63.983 37.293 49.033 1.00 18.70 ? 91 ILE A CG1 1 ATOM 679 C CG2 . ILE A 1 91 ? 64.214 39.743 49.565 1.00 15.65 ? 91 ILE A CG2 1 ATOM 680 C CD1 . ILE A 1 91 ? 65.389 37.092 48.491 1.00 23.48 ? 91 ILE A CD1 1 ATOM 681 N N . PRO A 1 92 ? 61.165 41.038 48.544 1.00 16.22 ? 92 PRO A N 1 ATOM 682 C CA . PRO A 1 92 ? 60.692 42.371 48.968 1.00 17.71 ? 92 PRO A CA 1 ATOM 683 C C . PRO A 1 92 ? 59.411 42.295 49.785 1.00 16.92 ? 92 PRO A C 1 ATOM 684 O O . PRO A 1 92 ? 59.205 43.132 50.674 1.00 17.88 ? 92 PRO A O 1 ATOM 685 C CB . PRO A 1 92 ? 60.468 43.103 47.639 1.00 19.57 ? 92 PRO A CB 1 ATOM 686 C CG . PRO A 1 92 ? 61.467 42.435 46.728 1.00 19.11 ? 92 PRO A CG 1 ATOM 687 C CD . PRO A 1 92 ? 61.341 40.980 47.085 1.00 16.73 ? 92 PRO A CD 1 ATOM 688 N N . PHE A 1 93 ? 58.524 41.319 49.537 1.00 14.16 ? 93 PHE A N 1 ATOM 689 C CA . PHE A 1 93 ? 57.323 41.196 50.361 1.00 16.04 ? 93 PHE A CA 1 ATOM 690 C C . PHE A 1 93 ? 57.690 40.682 51.755 1.00 16.61 ? 93 PHE A C 1 ATOM 691 O O . PHE A 1 93 ? 57.052 41.064 52.730 1.00 16.09 ? 93 PHE A O 1 ATOM 692 C CB . PHE A 1 93 ? 56.308 40.238 49.725 1.00 15.45 ? 93 PHE A CB 1 ATOM 693 C CG . PHE A 1 93 ? 55.794 40.801 48.398 1.00 14.53 ? 93 PHE A CG 1 ATOM 694 C CD1 . PHE A 1 93 ? 56.528 40.609 47.247 1.00 14.84 ? 93 PHE A CD1 1 ATOM 695 C CD2 . PHE A 1 93 ? 54.617 41.529 48.371 1.00 17.15 ? 93 PHE A CD2 1 ATOM 696 C CE1 . PHE A 1 93 ? 56.085 41.134 46.046 1.00 17.71 ? 93 PHE A CE1 1 ATOM 697 C CE2 . PHE A 1 93 ? 54.195 42.096 47.184 1.00 18.68 ? 93 PHE A CE2 1 ATOM 698 C CZ . PHE A 1 93 ? 54.942 41.902 46.038 1.00 16.61 ? 93 PHE A CZ 1 ATOM 699 N N . MET A 1 94 ? 58.636 39.759 51.835 1.00 16.78 ? 94 MET A N 1 ATOM 700 C CA . MET A 1 94 ? 59.058 39.272 53.162 1.00 15.85 ? 94 MET A CA 1 ATOM 701 C C . MET A 1 94 ? 59.586 40.450 53.987 1.00 14.82 ? 94 MET A C 1 ATOM 702 O O . MET A 1 94 ? 59.339 40.522 55.189 1.00 20.92 ? 94 MET A O 1 ATOM 703 C CB . MET A 1 94 ? 60.206 38.281 52.952 1.00 19.39 ? 94 MET A CB 1 ATOM 704 C CG . MET A 1 94 ? 60.807 37.793 54.258 1.00 15.19 ? 94 MET A CG 1 ATOM 705 S SD . MET A 1 94 ? 62.262 36.786 53.980 1.00 19.76 ? 94 MET A SD 1 ATOM 706 C CE . MET A 1 94 ? 63.463 38.010 53.452 1.00 17.81 ? 94 MET A CE 1 ATOM 707 N N . GLN A 1 95 ? 60.313 41.369 53.364 1.00 17.09 ? 95 GLN A N 1 ATOM 708 C CA . GLN A 1 95 ? 60.871 42.496 54.103 1.00 20.96 ? 95 GLN A CA 1 ATOM 709 C C . GLN A 1 95 ? 59.818 43.497 54.516 1.00 27.16 ? 95 GLN A C 1 ATOM 710 O O . GLN A 1 95 ? 59.880 44.068 55.602 1.00 21.96 ? 95 GLN A O 1 ATOM 711 C CB . GLN A 1 95 ? 61.934 43.200 53.245 1.00 19.55 ? 95 GLN A CB 1 ATOM 712 C CG . GLN A 1 95 ? 63.089 42.261 52.906 1.00 16.86 ? 95 GLN A CG 1 ATOM 713 C CD . GLN A 1 95 ? 64.131 42.954 52.045 1.00 21.10 ? 95 GLN A CD 1 ATOM 714 O OE1 . GLN A 1 95 ? 65.339 42.759 52.207 1.00 24.43 ? 95 GLN A OE1 1 ATOM 715 N NE2 . GLN A 1 95 ? 63.666 43.721 51.069 1.00 21.45 ? 95 GLN A NE2 1 ATOM 716 N N . LYS A 1 96 ? 58.852 43.731 53.634 1.00 16.31 ? 96 LYS A N 1 ATOM 717 C CA . LYS A 1 96 ? 57.798 44.697 53.915 1.00 23.34 ? 96 LYS A CA 1 ATOM 718 C C . LYS A 1 96 ? 56.714 44.102 54.791 1.00 23.67 ? 96 LYS A C 1 ATOM 719 O O . LYS A 1 96 ? 56.318 44.695 55.804 1.00 24.62 ? 96 LYS A O 1 ATOM 720 C CB . LYS A 1 96 ? 57.252 45.209 52.586 1.00 20.13 ? 96 LYS A CB 1 ATOM 721 C CG . LYS A 1 96 ? 56.010 46.090 52.676 1.00 25.33 ? 96 LYS A CG 1 ATOM 722 C CD . LYS A 1 96 ? 55.623 46.435 51.239 1.00 32.09 ? 96 LYS A CD 1 ATOM 723 C CE . LYS A 1 96 ? 54.419 47.348 51.129 1.00 37.72 ? 96 LYS A CE 1 ATOM 724 N NZ . LYS A 1 96 ? 54.233 47.747 49.696 1.00 35.41 ? 96 LYS A NZ 1 ATOM 725 N N . HIS A 1 97 ? 56.173 42.935 54.438 1.00 17.61 ? 97 HIS A N 1 ATOM 726 C CA . HIS A 1 97 ? 55.120 42.341 55.258 1.00 18.30 ? 97 HIS A CA 1 ATOM 727 C C . HIS A 1 97 ? 55.722 41.522 56.388 1.00 25.40 ? 97 HIS A C 1 ATOM 728 O O . HIS A 1 97 ? 55.684 40.301 56.407 1.00 19.60 ? 97 HIS A O 1 ATOM 729 C CB . HIS A 1 97 ? 54.247 41.446 54.348 1.00 17.52 ? 97 HIS A CB 1 ATOM 730 C CG . HIS A 1 97 ? 53.471 42.315 53.392 1.00 20.94 ? 97 HIS A CG 1 ATOM 731 N ND1 . HIS A 1 97 ? 52.245 42.855 53.672 1.00 16.50 ? 97 HIS A ND1 1 ATOM 732 C CD2 . HIS A 1 97 ? 53.829 42.799 52.175 1.00 20.20 ? 97 HIS A CD2 1 ATOM 733 C CE1 . HIS A 1 97 ? 51.858 43.619 52.668 1.00 16.90 ? 97 HIS A CE1 1 ATOM 734 N NE2 . HIS A 1 97 ? 52.791 43.580 51.735 1.00 19.39 ? 97 HIS A NE2 1 ATOM 735 N N . ASN A 1 98 ? 56.359 42.192 57.339 1.00 21.38 ? 98 ASN A N 1 ATOM 736 C CA . ASN A 1 98 ? 57.383 41.579 58.159 1.00 17.63 ? 98 ASN A CA 1 ATOM 737 C C . ASN A 1 98 ? 56.805 40.998 59.431 1.00 23.99 ? 98 ASN A C 1 ATOM 738 O O . ASN A 1 98 ? 57.524 40.732 60.396 1.00 26.37 ? 98 ASN A O 1 ATOM 739 C CB . ASN A 1 98 ? 58.486 42.594 58.462 1.00 25.82 ? 98 ASN A CB 1 ATOM 740 C CG . ASN A 1 98 ? 58.048 43.739 59.361 1.00 29.17 ? 98 ASN A CG 1 ATOM 741 O OD1 . ASN A 1 98 ? 56.864 44.034 59.523 1.00 25.07 ? 98 ASN A OD1 1 ATOM 742 N ND2 . ASN A 1 98 ? 59.045 44.382 59.969 1.00 25.14 ? 98 ASN A ND2 1 ATOM 743 N N . THR A 1 99 ? 55.494 40.756 59.412 1.00 17.02 ? 99 THR A N 1 ATOM 744 C CA . THR A 1 99 ? 54.953 39.950 60.499 1.00 14.68 ? 99 THR A CA 1 ATOM 745 C C . THR A 1 99 ? 54.617 38.550 59.973 1.00 17.69 ? 99 THR A C 1 ATOM 746 O O . THR A 1 99 ? 54.109 37.728 60.727 1.00 22.12 ? 99 THR A O 1 ATOM 747 C CB . THR A 1 99 ? 53.687 40.524 61.141 1.00 21.11 ? 99 THR A CB 1 ATOM 748 O OG1 . THR A 1 99 ? 52.584 40.477 60.238 1.00 22.76 ? 99 THR A OG1 1 ATOM 749 C CG2 . THR A 1 99 ? 53.885 41.972 61.565 1.00 21.84 ? 99 THR A CG2 1 ATOM 750 N N . ILE A 1 100 ? 54.893 38.296 58.690 1.00 15.83 ? 100 ILE A N 1 ATOM 751 C CA . ILE A 1 100 ? 54.555 36.960 58.151 1.00 17.95 ? 100 ILE A CA 1 ATOM 752 C C . ILE A 1 100 ? 55.834 36.231 57.795 1.00 15.91 ? 100 ILE A C 1 ATOM 753 O O . ILE A 1 100 ? 56.684 36.782 57.109 1.00 17.85 ? 100 ILE A O 1 ATOM 754 C CB . ILE A 1 100 ? 53.638 37.146 56.922 1.00 16.34 ? 100 ILE A CB 1 ATOM 755 C CG1 . ILE A 1 100 ? 52.217 37.604 57.337 1.00 18.13 ? 100 ILE A CG1 1 ATOM 756 C CG2 . ILE A 1 100 ? 53.575 35.907 56.046 1.00 15.09 ? 100 ILE A CG2 1 ATOM 757 C CD1 . ILE A 1 100 ? 51.465 38.323 56.216 1.00 17.26 ? 100 ILE A CD1 1 ATOM 758 N N . SER A 1 101 ? 56.035 35.000 58.278 1.00 13.29 ? 101 SER A N 1 ATOM 759 C CA . SER A 1 101 ? 57.270 34.295 57.991 1.00 11.62 ? 101 SER A CA 1 ATOM 760 C C . SER A 1 101 ? 57.476 34.042 56.500 1.00 17.35 ? 101 SER A C 1 ATOM 761 O O . SER A 1 101 ? 56.499 33.964 55.751 1.00 15.73 ? 101 SER A O 1 ATOM 762 C CB . SER A 1 101 ? 57.262 32.948 58.732 1.00 18.91 ? 101 SER A CB 1 ATOM 763 O OG . SER A 1 101 ? 56.247 32.121 58.181 1.00 18.18 ? 101 SER A OG 1 ATOM 764 N N . ALA A 1 102 ? 58.731 33.921 56.087 1.00 15.28 ? 102 ALA A N 1 ATOM 765 C CA . ALA A 1 102 ? 59.088 33.556 54.726 1.00 15.34 ? 102 ALA A CA 1 ATOM 766 C C . ALA A 1 102 ? 58.308 32.301 54.311 1.00 14.97 ? 102 ALA A C 1 ATOM 767 O O . ALA A 1 102 ? 57.796 32.275 53.189 1.00 16.09 ? 102 ALA A O 1 ATOM 768 C CB . ALA A 1 102 ? 60.577 33.317 54.539 1.00 15.17 ? 102 ALA A CB 1 ATOM 769 N N . ALA A 1 103 ? 58.229 31.320 55.206 1.00 14.36 ? 103 ALA A N 1 ATOM 770 C CA . ALA A 1 103 ? 57.570 30.064 54.859 1.00 14.89 ? 103 ALA A CA 1 ATOM 771 C C . ALA A 1 103 ? 56.091 30.278 54.568 1.00 14.16 ? 103 ALA A C 1 ATOM 772 O O . ALA A 1 103 ? 55.526 29.764 53.580 1.00 14.49 ? 103 ALA A O 1 ATOM 773 C CB . ALA A 1 103 ? 57.752 29.045 55.991 1.00 16.89 ? 103 ALA A CB 1 ATOM 774 N N . ASP A 1 104 ? 55.401 30.982 55.466 1.00 15.13 ? 104 ASP A N 1 ATOM 775 C CA . ASP A 1 104 ? 53.991 31.302 55.227 1.00 16.35 ? 104 ASP A CA 1 ATOM 776 C C . ASP A 1 104 ? 53.827 32.154 53.961 1.00 19.21 ? 104 ASP A C 1 ATOM 777 O O . ASP A 1 104 ? 52.896 31.904 53.173 1.00 15.05 ? 104 ASP A O 1 ATOM 778 C CB . ASP A 1 104 ? 53.397 32.091 56.395 1.00 17.83 ? 104 ASP A CB 1 ATOM 779 C CG . ASP A 1 104 ? 53.150 31.294 57.662 1.00 15.64 ? 104 ASP A CG 1 ATOM 780 O OD1 . ASP A 1 104 ? 53.451 30.082 57.715 1.00 17.98 ? 104 ASP A OD1 1 ATOM 781 O OD2 . ASP A 1 104 ? 52.557 31.910 58.583 1.00 16.55 ? 104 ASP A OD2 1 ATOM 782 N N . LEU A 1 105 ? 54.720 33.121 53.755 1.00 14.90 ? 105 LEU A N 1 ATOM 783 C CA . LEU A 1 105 ? 54.673 33.971 52.566 1.00 14.94 ? 105 LEU A CA 1 ATOM 784 C C . LEU A 1 105 ? 54.703 33.113 51.295 1.00 14.15 ? 105 LEU A C 1 ATOM 785 O O . LEU A 1 105 ? 53.917 33.372 50.374 1.00 14.82 ? 105 LEU A O 1 ATOM 786 C CB . LEU A 1 105 ? 55.844 34.951 52.529 1.00 13.88 ? 105 LEU A CB 1 ATOM 787 C CG . LEU A 1 105 ? 56.144 35.679 51.216 1.00 15.72 ? 105 LEU A CG 1 ATOM 788 C CD1 . LEU A 1 105 ? 54.971 36.565 50.783 1.00 16.50 ? 105 LEU A CD1 1 ATOM 789 C CD2 . LEU A 1 105 ? 57.389 36.552 51.356 1.00 12.80 ? 105 LEU A CD2 1 ATOM 790 N N . VAL A 1 106 ? 55.598 32.117 51.256 1.00 12.40 ? 106 VAL A N 1 ATOM 791 C CA . VAL A 1 106 ? 55.721 31.330 50.024 1.00 11.21 ? 106 VAL A CA 1 ATOM 792 C C . VAL A 1 106 ? 54.441 30.548 49.766 1.00 14.84 ? 106 VAL A C 1 ATOM 793 O O . VAL A 1 106 ? 53.908 30.459 48.648 1.00 16.14 ? 106 VAL A O 1 ATOM 794 C CB . VAL A 1 106 ? 56.878 30.326 50.141 1.00 15.71 ? 106 VAL A CB 1 ATOM 795 C CG1 . VAL A 1 106 ? 56.798 29.308 49.008 1.00 11.45 ? 106 VAL A CG1 1 ATOM 796 C CG2 . VAL A 1 106 ? 58.215 31.055 50.085 1.00 14.93 ? 106 VAL A CG2 1 ATOM 797 N N . GLN A 1 107 ? 53.903 29.892 50.803 1.00 11.86 ? 107 GLN A N 1 ATOM 798 C CA . GLN A 1 107 ? 52.695 29.089 50.620 1.00 12.71 ? 107 GLN A CA 1 ATOM 799 C C . GLN A 1 107 ? 51.518 29.958 50.246 1.00 12.09 ? 107 GLN A C 1 ATOM 800 O O . GLN A 1 107 ? 50.753 29.623 49.338 1.00 17.19 ? 107 GLN A O 1 ATOM 801 C CB . GLN A 1 107 ? 52.434 28.249 51.874 1.00 13.71 ? 107 GLN A CB 1 ATOM 802 C CG . GLN A 1 107 ? 53.464 27.140 52.058 1.00 14.83 ? 107 GLN A CG 1 ATOM 803 C CD . GLN A 1 107 ? 53.799 26.366 50.806 1.00 14.06 ? 107 GLN A CD 1 ATOM 804 O OE1 . GLN A 1 107 ? 54.974 26.146 50.463 1.00 17.48 ? 107 GLN A OE1 1 ATOM 805 N NE2 . GLN A 1 107 ? 52.806 25.793 50.162 1.00 10.22 ? 107 GLN A NE2 1 ATOM 806 N N . PHE A 1 108 ? 51.326 31.064 50.963 1.00 12.93 ? 108 PHE A N 1 ATOM 807 C CA . PHE A 1 108 ? 50.178 31.923 50.685 1.00 15.91 ? 108 PHE A CA 1 ATOM 808 C C . PHE A 1 108 ? 50.270 32.526 49.282 1.00 15.11 ? 108 PHE A C 1 ATOM 809 O O . PHE A 1 108 ? 49.285 32.643 48.527 1.00 15.88 ? 108 PHE A O 1 ATOM 810 C CB . PHE A 1 108 ? 50.173 33.029 51.768 1.00 14.31 ? 108 PHE A CB 1 ATOM 811 C CG . PHE A 1 108 ? 48.917 33.888 51.678 1.00 13.74 ? 108 PHE A CG 1 ATOM 812 C CD1 . PHE A 1 108 ? 49.010 35.225 51.330 1.00 12.61 ? 108 PHE A CD1 1 ATOM 813 C CD2 . PHE A 1 108 ? 47.688 33.356 51.992 1.00 13.81 ? 108 PHE A CD2 1 ATOM 814 C CE1 . PHE A 1 108 ? 47.886 36.031 51.254 1.00 12.70 ? 108 PHE A CE1 1 ATOM 815 C CE2 . PHE A 1 108 ? 46.558 34.141 51.822 1.00 12.59 ? 108 PHE A CE2 1 ATOM 816 C CZ . PHE A 1 108 ? 46.646 35.479 51.506 1.00 13.57 ? 108 PHE A CZ 1 ATOM 817 N N . ALA A 1 109 ? 51.476 32.956 48.888 1.00 14.53 ? 109 ALA A N 1 ATOM 818 C CA . ALA A 1 109 ? 51.640 33.561 47.562 1.00 15.93 ? 109 ALA A CA 1 ATOM 819 C C . ALA A 1 109 ? 51.254 32.531 46.494 1.00 17.65 ? 109 ALA A C 1 ATOM 820 O O . ALA A 1 109 ? 50.637 32.896 45.488 1.00 16.24 ? 109 ALA A O 1 ATOM 821 C CB . ALA A 1 109 ? 53.050 34.064 47.347 1.00 12.04 ? 109 ALA A CB 1 ATOM 822 N N . GLY A 1 110 ? 51.566 31.259 46.766 1.00 13.92 ? 110 GLY A N 1 ATOM 823 C CA . GLY A 1 110 ? 51.222 30.204 45.792 1.00 13.85 ? 110 GLY A CA 1 ATOM 824 C C . GLY A 1 110 ? 49.709 30.070 45.716 1.00 15.57 ? 110 GLY A C 1 ATOM 825 O O . GLY A 1 110 ? 49.090 29.926 44.647 1.00 14.71 ? 110 GLY A O 1 ATOM 826 N N . ALA A 1 111 ? 49.050 30.147 46.867 1.00 15.00 ? 111 ALA A N 1 ATOM 827 C CA . ALA A 1 111 ? 47.596 30.089 46.891 1.00 10.05 ? 111 ALA A CA 1 ATOM 828 C C . ALA A 1 111 ? 46.957 31.266 46.143 1.00 13.58 ? 111 ALA A C 1 ATOM 829 O O . ALA A 1 111 ? 45.946 31.082 45.420 1.00 14.75 ? 111 ALA A O 1 ATOM 830 C CB . ALA A 1 111 ? 47.083 29.987 48.316 1.00 13.22 ? 111 ALA A CB 1 ATOM 831 N N . VAL A 1 112 ? 47.494 32.458 46.342 1.00 15.07 ? 112 VAL A N 1 ATOM 832 C CA . VAL A 1 112 ? 46.979 33.652 45.669 1.00 14.40 ? 112 VAL A CA 1 ATOM 833 C C . VAL A 1 112 ? 47.161 33.510 44.160 1.00 22.34 ? 112 VAL A C 1 ATOM 834 O O . VAL A 1 112 ? 46.248 33.714 43.357 1.00 16.08 ? 112 VAL A O 1 ATOM 835 C CB . VAL A 1 112 ? 47.704 34.934 46.105 1.00 13.38 ? 112 VAL A CB 1 ATOM 836 C CG1 . VAL A 1 112 ? 47.235 36.120 45.268 1.00 13.06 ? 112 VAL A CG1 1 ATOM 837 C CG2 . VAL A 1 112 ? 47.371 35.200 47.576 1.00 16.13 ? 112 VAL A CG2 1 ATOM 838 N N . ALA A 1 113 ? 48.379 33.136 43.770 1.00 13.90 ? 113 ALA A N 1 ATOM 839 C CA . ALA A 1 113 ? 48.627 32.975 42.325 1.00 13.07 ? 113 ALA A CA 1 ATOM 840 C C . ALA A 1 113 ? 47.663 31.979 41.688 1.00 13.37 ? 113 ALA A C 1 ATOM 841 O O . ALA A 1 113 ? 47.080 32.233 40.637 1.00 16.39 ? 113 ALA A O 1 ATOM 842 C CB . ALA A 1 113 ? 50.060 32.489 42.123 1.00 13.42 ? 113 ALA A CB 1 ATOM 843 N N . LEU A 1 114 ? 47.481 30.818 42.333 1.00 13.87 ? 114 LEU A N 1 ATOM 844 C CA . LEU A 1 114 ? 46.601 29.801 41.788 1.00 13.16 ? 114 LEU A CA 1 ATOM 845 C C . LEU A 1 114 ? 45.172 30.300 41.683 1.00 17.20 ? 114 LEU A C 1 ATOM 846 O O . LEU A 1 114 ? 44.408 29.844 40.829 1.00 17.24 ? 114 LEU A O 1 ATOM 847 C CB . LEU A 1 114 ? 46.596 28.537 42.663 1.00 16.90 ? 114 LEU A CB 1 ATOM 848 C CG . LEU A 1 114 ? 47.754 27.574 42.359 1.00 19.56 ? 114 LEU A CG 1 ATOM 849 C CD1 . LEU A 1 114 ? 48.095 26.754 43.602 1.00 24.52 ? 114 LEU A CD1 1 ATOM 850 C CD2 . LEU A 1 114 ? 47.365 26.686 41.181 1.00 22.51 ? 114 LEU A CD2 1 ATOM 851 N N . SER A 1 115 ? 44.762 31.195 42.582 1.00 14.41 ? 115 SER A N 1 ATOM 852 C CA . SER A 1 115 ? 43.353 31.619 42.536 1.00 16.36 ? 115 SER A CA 1 ATOM 853 C C . SER A 1 115 ? 43.072 32.414 41.258 1.00 18.67 ? 115 SER A C 1 ATOM 854 O O . SER A 1 115 ? 41.896 32.633 40.949 1.00 16.51 ? 115 SER A O 1 ATOM 855 C CB . SER A 1 115 ? 43.006 32.486 43.752 1.00 15.87 ? 115 SER A CB 1 ATOM 856 O OG . SER A 1 115 ? 43.468 33.820 43.608 1.00 17.33 ? 115 SER A OG 1 ATOM 857 N N . ASN A 1 116 ? 44.114 32.864 40.557 1.00 18.72 ? 116 ASN A N 1 ATOM 858 C CA . ASN A 1 116 ? 43.955 33.655 39.333 1.00 15.35 ? 116 ASN A CA 1 ATOM 859 C C . ASN A 1 116 ? 43.813 32.752 38.099 1.00 16.72 ? 116 ASN A C 1 ATOM 860 O O . ASN A 1 116 ? 43.593 33.273 36.999 1.00 17.73 ? 116 ASN A O 1 ATOM 861 C CB . ASN A 1 116 ? 45.138 34.591 39.065 1.00 11.62 ? 116 ASN A CB 1 ATOM 862 C CG . ASN A 1 116 ? 45.311 35.679 40.110 1.00 14.19 ? 116 ASN A CG 1 ATOM 863 O OD1 . ASN A 1 116 ? 44.374 36.002 40.845 1.00 15.84 ? 116 ASN A OD1 1 ATOM 864 N ND2 . ASN A 1 116 ? 46.530 36.231 40.184 1.00 15.59 ? 116 ASN A ND2 1 ATOM 865 N N . CYS A 1 117 ? 43.910 31.433 38.282 1.00 16.58 ? 117 CYS A N 1 ATOM 866 C CA . CYS A 1 117 ? 43.824 30.494 37.165 1.00 15.66 ? 117 CYS A CA 1 ATOM 867 C C . CYS A 1 117 ? 42.423 29.862 37.129 1.00 19.87 ? 117 CYS A C 1 ATOM 868 O O . CYS A 1 117 ? 42.082 29.035 37.993 1.00 14.22 ? 117 CYS A O 1 ATOM 869 C CB . CYS A 1 117 ? 44.844 29.356 37.338 1.00 12.36 ? 117 CYS A CB 1 ATOM 870 S SG . CYS A 1 117 ? 46.518 29.950 37.697 1.00 15.64 ? 117 CYS A SG 1 ATOM 871 N N . PRO A 1 118 ? 41.608 30.171 36.120 1.00 15.96 ? 118 PRO A N 1 ATOM 872 C CA . PRO A 1 118 ? 40.254 29.640 36.093 1.00 15.27 ? 118 PRO A CA 1 ATOM 873 C C . PRO A 1 118 ? 40.169 28.121 36.205 1.00 13.85 ? 118 PRO A C 1 ATOM 874 O O . PRO A 1 118 ? 40.920 27.420 35.517 1.00 14.88 ? 118 PRO A O 1 ATOM 875 C CB . PRO A 1 118 ? 39.701 30.121 34.735 1.00 14.67 ? 118 PRO A CB 1 ATOM 876 C CG . PRO A 1 118 ? 40.506 31.348 34.441 1.00 15.92 ? 118 PRO A CG 1 ATOM 877 C CD . PRO A 1 118 ? 41.887 31.091 34.997 1.00 13.71 ? 118 PRO A CD 1 ATOM 878 N N . GLY A 1 119 ? 39.327 27.702 37.153 1.00 12.03 ? 119 GLY A N 1 ATOM 879 C CA . GLY A 1 119 ? 39.201 26.270 37.423 1.00 11.08 ? 119 GLY A CA 1 ATOM 880 C C . GLY A 1 119 ? 40.013 25.851 38.636 1.00 16.93 ? 119 GLY A C 1 ATOM 881 O O . GLY A 1 119 ? 39.794 24.749 39.161 1.00 16.13 ? 119 GLY A O 1 ATOM 882 N N . ALA A 1 120 ? 40.944 26.675 39.136 1.00 13.80 ? 120 ALA A N 1 ATOM 883 C CA . ALA A 1 120 ? 41.735 26.208 40.285 1.00 14.40 ? 120 ALA A CA 1 ATOM 884 C C . ALA A 1 120 ? 40.897 26.143 41.546 1.00 14.23 ? 120 ALA A C 1 ATOM 885 O O . ALA A 1 120 ? 39.955 26.896 41.777 1.00 17.34 ? 120 ALA A O 1 ATOM 886 C CB . ALA A 1 120 ? 42.887 27.193 40.544 1.00 16.00 ? 120 ALA A CB 1 ATOM 887 N N . PRO A 1 121 ? 41.322 25.276 42.466 1.00 17.61 ? 121 PRO A N 1 ATOM 888 C CA . PRO A 1 121 ? 40.644 25.209 43.766 1.00 14.45 ? 121 PRO A CA 1 ATOM 889 C C . PRO A 1 121 ? 41.138 26.337 44.670 1.00 17.13 ? 121 PRO A C 1 ATOM 890 O O . PRO A 1 121 ? 42.163 26.972 44.418 1.00 17.08 ? 121 PRO A O 1 ATOM 891 C CB . PRO A 1 121 ? 41.170 23.879 44.319 1.00 20.99 ? 121 PRO A CB 1 ATOM 892 C CG . PRO A 1 121 ? 42.543 23.744 43.722 1.00 15.52 ? 121 PRO A CG 1 ATOM 893 C CD . PRO A 1 121 ? 42.451 24.332 42.332 1.00 16.45 ? 121 PRO A CD 1 ATOM 894 N N . ARG A 1 122 ? 40.381 26.576 45.730 1.00 15.37 ? 122 ARG A N 1 ATOM 895 C CA . ARG A 1 122 ? 40.795 27.613 46.703 1.00 12.56 ? 122 ARG A CA 1 ATOM 896 C C . ARG A 1 122 ? 41.592 26.882 47.770 1.00 14.69 ? 122 ARG A C 1 ATOM 897 O O . ARG A 1 122 ? 40.999 26.057 48.485 1.00 19.06 ? 122 ARG A O 1 ATOM 898 C CB . ARG A 1 122 ? 39.533 28.258 47.248 1.00 12.73 ? 122 ARG A CB 1 ATOM 899 C CG . ARG A 1 122 ? 39.746 29.431 48.165 1.00 13.71 ? 122 ARG A CG 1 ATOM 900 C CD . ARG A 1 122 ? 38.425 29.919 48.755 1.00 17.84 ? 122 ARG A CD 1 ATOM 901 N NE . ARG A 1 122 ? 38.661 31.136 49.539 1.00 15.82 ? 122 ARG A NE 1 ATOM 902 C CZ . ARG A 1 122 ? 37.808 31.622 50.423 1.00 18.56 ? 122 ARG A CZ 1 ATOM 903 N NH1 . ARG A 1 122 ? 36.650 31.010 50.620 1.00 19.80 ? 122 ARG A NH1 1 ATOM 904 N NH2 . ARG A 1 122 ? 38.132 32.729 51.102 1.00 21.11 ? 122 ARG A NH2 1 ATOM 905 N N . LEU A 1 123 ? 42.922 27.013 47.738 1.00 15.44 ? 123 LEU A N 1 ATOM 906 C CA . LEU A 1 123 ? 43.683 26.078 48.578 1.00 10.14 ? 123 LEU A CA 1 ATOM 907 C C . LEU A 1 123 ? 43.418 26.247 50.059 1.00 16.48 ? 123 LEU A C 1 ATOM 908 O O . LEU A 1 123 ? 43.249 27.368 50.520 1.00 19.42 ? 123 LEU A O 1 ATOM 909 C CB . LEU A 1 123 ? 45.186 26.391 48.397 1.00 13.56 ? 123 LEU A CB 1 ATOM 910 C CG . LEU A 1 123 ? 45.713 26.042 46.995 1.00 22.18 ? 123 LEU A CG 1 ATOM 911 C CD1 . LEU A 1 123 ? 47.222 26.265 46.928 1.00 22.49 ? 123 LEU A CD1 1 ATOM 912 C CD2 . LEU A 1 123 ? 45.356 24.603 46.620 1.00 15.20 ? 123 LEU A CD2 1 ATOM 913 N N . GLU A 1 124 ? 43.597 25.185 50.848 1.00 13.09 ? 124 GLU A N 1 ATOM 914 C CA . GLU A 1 124 ? 43.664 25.458 52.289 1.00 14.43 ? 124 GLU A CA 1 ATOM 915 C C . GLU A 1 124 ? 44.934 26.291 52.522 1.00 13.04 ? 124 GLU A C 1 ATOM 916 O O . GLU A 1 124 ? 45.967 26.153 51.844 1.00 15.71 ? 124 GLU A O 1 ATOM 917 C CB . GLU A 1 124 ? 43.839 24.112 53.015 1.00 18.08 ? 124 GLU A CB 1 ATOM 918 C CG . GLU A 1 124 ? 43.995 24.226 54.533 1.00 15.64 ? 124 GLU A CG 1 ATOM 919 C CD . GLU A 1 124 ? 44.172 22.825 55.129 1.00 23.76 ? 124 GLU A CD 1 ATOM 920 O OE1 . GLU A 1 124 ? 43.244 22.320 55.798 1.00 22.14 ? 124 GLU A OE1 1 ATOM 921 O OE2 . GLU A 1 124 ? 45.242 22.247 54.878 1.00 19.93 ? 124 GLU A OE2 1 ATOM 922 N N . PHE A 1 125 ? 44.820 27.166 53.538 1.00 14.47 ? 125 PHE A N 1 ATOM 923 C CA . PHE A 1 125 ? 46.040 27.895 53.900 1.00 11.70 ? 125 PHE A CA 1 ATOM 924 C C . PHE A 1 125 ? 46.139 27.969 55.434 1.00 14.22 ? 125 PHE A C 1 ATOM 925 O O . PHE A 1 125 ? 45.322 28.632 56.071 1.00 17.30 ? 125 PHE A O 1 ATOM 926 C CB . PHE A 1 125 ? 46.077 29.301 53.321 1.00 11.57 ? 125 PHE A CB 1 ATOM 927 C CG . PHE A 1 125 ? 47.295 30.072 53.839 1.00 13.03 ? 125 PHE A CG 1 ATOM 928 C CD1 . PHE A 1 125 ? 48.574 29.691 53.483 1.00 12.98 ? 125 PHE A CD1 1 ATOM 929 C CD2 . PHE A 1 125 ? 47.088 31.160 54.688 1.00 14.89 ? 125 PHE A CD2 1 ATOM 930 C CE1 . PHE A 1 125 ? 49.683 30.374 54.020 1.00 16.32 ? 125 PHE A CE1 1 ATOM 931 C CE2 . PHE A 1 125 ? 48.201 31.805 55.248 1.00 17.84 ? 125 PHE A CE2 1 ATOM 932 C CZ . PHE A 1 125 ? 49.486 31.407 54.921 1.00 21.74 ? 125 PHE A CZ 1 ATOM 933 N N . LEU A 1 126 ? 47.100 27.227 55.963 1.00 13.60 ? 126 LEU A N 1 ATOM 934 C CA . LEU A 1 126 ? 47.350 27.262 57.403 1.00 15.06 ? 126 LEU A CA 1 ATOM 935 C C . LEU A 1 126 ? 48.541 28.189 57.614 1.00 16.96 ? 126 LEU A C 1 ATOM 936 O O . LEU A 1 126 ? 49.377 28.237 56.697 1.00 17.64 ? 126 LEU A O 1 ATOM 937 C CB . LEU A 1 126 ? 47.689 25.865 57.940 1.00 15.19 ? 126 LEU A CB 1 ATOM 938 C CG . LEU A 1 126 ? 46.682 24.764 57.558 1.00 16.12 ? 126 LEU A CG 1 ATOM 939 C CD1 . LEU A 1 126 ? 47.031 23.439 58.226 1.00 14.76 ? 126 LEU A CD1 1 ATOM 940 C CD2 . LEU A 1 126 ? 45.267 25.194 57.935 1.00 14.00 ? 126 LEU A CD2 1 ATOM 941 N N . ALA A 1 127 ? 48.578 28.855 58.773 1.00 16.40 ? 127 ALA A N 1 ATOM 942 C CA . ALA A 1 127 ? 49.636 29.838 58.998 1.00 17.54 ? 127 ALA A CA 1 ATOM 943 C C . ALA A 1 127 ? 50.385 29.503 60.290 1.00 15.64 ? 127 ALA A C 1 ATOM 944 O O . ALA A 1 127 ? 49.878 28.729 61.087 1.00 16.77 ? 127 ALA A O 1 ATOM 945 C CB . ALA A 1 127 ? 49.095 31.254 59.047 1.00 18.44 ? 127 ALA A CB 1 ATOM 946 N N . GLY A 1 128 ? 51.511 30.153 60.511 1.00 16.53 ? 128 GLY A N 1 ATOM 947 C CA . GLY A 1 128 ? 52.276 29.955 61.727 1.00 13.83 ? 128 GLY A CA 1 ATOM 948 C C . GLY A 1 128 ? 53.587 29.233 61.567 1.00 18.91 ? 128 GLY A C 1 ATOM 949 O O . GLY A 1 128 ? 54.275 28.889 62.557 1.00 17.49 ? 128 GLY A O 1 ATOM 950 N N . ARG A 1 129 ? 54.048 28.971 60.349 1.00 15.58 ? 129 ARG A N 1 ATOM 951 C CA . ARG A 1 129 ? 55.337 28.293 60.222 1.00 15.21 ? 129 ARG A CA 1 ATOM 952 C C . ARG A 1 129 ? 56.438 29.255 60.676 1.00 12.13 ? 129 ARG A C 1 ATOM 953 O O . ARG A 1 129 ? 56.411 30.461 60.400 1.00 13.15 ? 129 ARG A O 1 ATOM 954 C CB . ARG A 1 129 ? 55.614 27.973 58.742 1.00 14.18 ? 129 ARG A CB 1 ATOM 955 C CG . ARG A 1 129 ? 54.536 27.104 58.099 1.00 14.18 ? 129 ARG A CG 1 ATOM 956 C CD . ARG A 1 129 ? 54.658 27.141 56.571 1.00 16.72 ? 129 ARG A CD 1 ATOM 957 N NE . ARG A 1 129 ? 53.583 26.387 55.897 1.00 14.64 ? 129 ARG A NE 1 ATOM 958 C CZ . ARG A 1 129 ? 52.343 26.852 55.779 1.00 13.91 ? 129 ARG A CZ 1 ATOM 959 N NH1 . ARG A 1 129 ? 52.061 28.070 56.226 1.00 13.67 ? 129 ARG A NH1 1 ATOM 960 N NH2 . ARG A 1 129 ? 51.409 26.100 55.198 1.00 14.04 ? 129 ARG A NH2 1 ATOM 961 N N . PRO A 1 130 ? 57.393 28.742 61.442 1.00 14.81 ? 130 PRO A N 1 ATOM 962 C CA . PRO A 1 130 ? 58.451 29.625 61.948 1.00 17.85 ? 130 PRO A CA 1 ATOM 963 C C . PRO A 1 130 ? 59.242 30.328 60.856 1.00 20.71 ? 130 PRO A C 1 ATOM 964 O O . PRO A 1 130 ? 59.312 29.864 59.718 1.00 16.58 ? 130 PRO A O 1 ATOM 965 C CB . PRO A 1 130 ? 59.352 28.630 62.698 1.00 20.65 ? 130 PRO A CB 1 ATOM 966 C CG . PRO A 1 130 ? 58.440 27.533 63.119 1.00 24.13 ? 130 PRO A CG 1 ATOM 967 C CD . PRO A 1 130 ? 57.459 27.377 61.979 1.00 22.43 ? 130 PRO A CD 1 ATOM 968 N N . ASN A 1 131 ? 59.911 31.413 61.223 1.00 16.46 ? 131 ASN A N 1 ATOM 969 C CA . ASN A 1 131 ? 60.760 32.175 60.307 1.00 14.09 ? 131 ASN A CA 1 ATOM 970 C C . ASN A 1 131 ? 62.232 31.847 60.444 1.00 18.10 ? 131 ASN A C 1 ATOM 971 O O . ASN A 1 131 ? 63.096 32.591 59.974 1.00 23.25 ? 131 ASN A O 1 ATOM 972 C CB . ASN A 1 131 ? 60.542 33.663 60.566 1.00 18.19 ? 131 ASN A CB 1 ATOM 973 C CG . ASN A 1 131 ? 60.975 34.558 59.427 1.00 19.93 ? 131 ASN A CG 1 ATOM 974 O OD1 . ASN A 1 131 ? 60.630 34.305 58.261 1.00 18.04 ? 131 ASN A OD1 1 ATOM 975 N ND2 . ASN A 1 131 ? 61.682 35.628 59.800 1.00 18.77 ? 131 ASN A ND2 1 ATOM 976 N N . LYS A 1 132 ? 62.592 30.671 60.962 1.00 13.49 ? 132 LYS A N 1 ATOM 977 C CA . LYS A 1 132 ? 64.019 30.328 60.943 1.00 17.55 ? 132 LYS A CA 1 ATOM 978 C C . LYS A 1 132 ? 64.123 28.881 60.464 1.00 17.96 ? 132 LYS A C 1 ATOM 979 O O . LYS A 1 132 ? 63.254 28.112 60.833 1.00 19.00 ? 132 LYS A O 1 ATOM 980 C CB . LYS A 1 132 ? 64.619 30.401 62.355 1.00 25.44 ? 132 LYS A CB 1 ATOM 981 C CG . LYS A 1 132 ? 64.276 31.679 63.103 1.00 52.90 ? 132 LYS A CG 1 ATOM 982 C CD . LYS A 1 132 ? 65.036 31.812 64.412 1.00 51.49 ? 132 LYS A CD 1 ATOM 983 C CE . LYS A 1 132 ? 65.169 33.275 64.817 1.00 56.64 ? 132 LYS A CE 1 ATOM 984 N NZ . LYS A 1 132 ? 66.550 33.800 64.624 1.00 69.43 ? 132 LYS A NZ 1 ATOM 985 N N . THR A 1 133 ? 65.179 28.586 59.727 1.00 17.51 ? 133 THR A N 1 ATOM 986 C CA . THR A 1 133 ? 65.370 27.219 59.232 1.00 14.43 ? 133 THR A CA 1 ATOM 987 C C . THR A 1 133 ? 66.823 27.081 58.798 1.00 18.10 ? 133 THR A C 1 ATOM 988 O O . THR A 1 133 ? 67.672 27.872 59.221 1.00 18.18 ? 133 THR A O 1 ATOM 989 C CB . THR A 1 133 ? 64.335 26.899 58.133 1.00 13.47 ? 133 THR A CB 1 ATOM 990 O OG1 . THR A 1 133 ? 64.421 25.516 57.757 1.00 14.56 ? 133 THR A OG1 1 ATOM 991 C CG2 . THR A 1 133 ? 64.630 27.689 56.858 1.00 16.08 ? 133 THR A CG2 1 ATOM 992 N N . ILE A 1 134 ? 67.139 26.095 57.991 1.00 14.61 ? 134 ILE A N 1 ATOM 993 C CA . ILE A 1 134 ? 68.437 25.846 57.399 1.00 16.30 ? 134 ILE A CA 1 ATOM 994 C C . ILE A 1 134 ? 68.291 25.732 55.888 1.00 18.98 ? 134 ILE A C 1 ATOM 995 O O . ILE A 1 134 ? 67.180 25.540 55.384 1.00 17.68 ? 134 ILE A O 1 ATOM 996 C CB . ILE A 1 134 ? 68.989 24.501 57.940 1.00 17.50 ? 134 ILE A CB 1 ATOM 997 C CG1 . ILE A 1 134 ? 67.956 23.380 57.826 1.00 20.80 ? 134 ILE A CG1 1 ATOM 998 C CG2 . ILE A 1 134 ? 69.426 24.680 59.395 1.00 21.35 ? 134 ILE A CG2 1 ATOM 999 C CD1 . ILE A 1 134 ? 68.586 22.004 57.838 1.00 23.20 ? 134 ILE A CD1 1 ATOM 1000 N N . ALA A 1 135 ? 69.425 25.824 55.197 1.00 15.89 ? 135 ALA A N 1 ATOM 1001 C CA . ALA A 1 135 ? 69.363 25.655 53.740 1.00 16.23 ? 135 ALA A CA 1 ATOM 1002 C C . ALA A 1 135 ? 69.245 24.165 53.461 1.00 20.28 ? 135 ALA A C 1 ATOM 1003 O O . ALA A 1 135 ? 69.847 23.314 54.118 1.00 16.95 ? 135 ALA A O 1 ATOM 1004 C CB . ALA A 1 135 ? 70.595 26.251 53.080 1.00 14.38 ? 135 ALA A CB 1 ATOM 1005 N N . ALA A 1 136 ? 68.435 23.763 52.483 1.00 14.40 ? 136 ALA A N 1 ATOM 1006 C CA . ALA A 1 136 ? 68.365 22.322 52.223 1.00 13.11 ? 136 ALA A CA 1 ATOM 1007 C C . ALA A 1 136 ? 69.585 21.843 51.466 1.00 11.12 ? 136 ALA A C 1 ATOM 1008 O O . ALA A 1 136 ? 70.350 22.635 50.883 1.00 14.69 ? 136 ALA A O 1 ATOM 1009 C CB . ALA A 1 136 ? 67.105 22.087 51.376 1.00 18.35 ? 136 ALA A CB 1 ATOM 1010 N N . VAL A 1 137 ? 69.716 20.515 51.404 1.00 13.33 ? 137 VAL A N 1 ATOM 1011 C CA . VAL A 1 137 ? 70.750 19.881 50.597 1.00 13.51 ? 137 VAL A CA 1 ATOM 1012 C C . VAL A 1 137 ? 70.302 19.620 49.160 1.00 16.25 ? 137 VAL A C 1 ATOM 1013 O O . VAL A 1 137 ? 69.102 19.686 48.847 1.00 17.66 ? 137 VAL A O 1 ATOM 1014 C CB . VAL A 1 137 ? 71.199 18.576 51.272 1.00 16.84 ? 137 VAL A CB 1 ATOM 1015 C CG1 . VAL A 1 137 ? 71.546 18.909 52.729 1.00 18.70 ? 137 VAL A CG1 1 ATOM 1016 C CG2 . VAL A 1 137 ? 70.142 17.486 51.199 1.00 20.03 ? 137 VAL A CG2 1 ATOM 1017 N N . ASP A 1 138 ? 71.273 19.379 48.272 1.00 14.16 ? 138 ASP A N 1 ATOM 1018 C CA . ASP A 1 138 ? 70.929 19.161 46.850 1.00 15.95 ? 138 ASP A CA 1 ATOM 1019 C C . ASP A 1 138 ? 70.323 17.774 46.667 1.00 18.52 ? 138 ASP A C 1 ATOM 1020 O O . ASP A 1 138 ? 70.393 16.920 47.559 1.00 20.13 ? 138 ASP A O 1 ATOM 1021 C CB . ASP A 1 138 ? 72.202 19.339 46.028 1.00 19.33 ? 138 ASP A CB 1 ATOM 1022 C CG . ASP A 1 138 ? 72.038 19.633 44.556 1.00 16.42 ? 138 ASP A CG 1 ATOM 1023 O OD1 . ASP A 1 138 ? 73.076 19.883 43.919 1.00 15.64 ? 138 ASP A OD1 1 ATOM 1024 O OD2 . ASP A 1 138 ? 70.914 19.596 44.007 1.00 17.51 ? 138 ASP A OD2 1 ATOM 1025 N N . GLY A 1 139 ? 69.692 17.516 45.527 1.00 13.34 ? 139 GLY A N 1 ATOM 1026 C CA . GLY A 1 139 ? 69.195 16.193 45.175 1.00 14.60 ? 139 GLY A CA 1 ATOM 1027 C C . GLY A 1 139 ? 67.783 15.915 45.613 1.00 17.16 ? 139 GLY A C 1 ATOM 1028 O O . GLY A 1 139 ? 67.275 14.794 45.390 1.00 22.02 ? 139 GLY A O 1 ATOM 1029 N N . LEU A 1 140 ? 67.097 16.848 46.251 1.00 13.23 ? 140 LEU A N 1 ATOM 1030 C CA . LEU A 1 140 ? 65.760 16.623 46.763 1.00 16.63 ? 140 LEU A CA 1 ATOM 1031 C C . LEU A 1 140 ? 64.635 16.992 45.793 1.00 15.63 ? 140 LEU A C 1 ATOM 1032 O O . LEU A 1 140 ? 63.455 16.769 46.041 1.00 17.14 ? 140 LEU A O 1 ATOM 1033 C CB . LEU A 1 140 ? 65.580 17.415 48.070 1.00 14.43 ? 140 LEU A CB 1 ATOM 1034 C CG . LEU A 1 140 ? 66.548 17.031 49.210 1.00 17.05 ? 140 LEU A CG 1 ATOM 1035 C CD1 . LEU A 1 140 ? 66.250 17.847 50.457 1.00 15.34 ? 140 LEU A CD1 1 ATOM 1036 C CD2 . LEU A 1 140 ? 66.419 15.537 49.499 1.00 22.81 ? 140 LEU A CD2 1 ATOM 1037 N N . ILE A 1 141 ? 64.951 17.724 44.746 1.00 15.35 ? 141 ILE A N 1 ATOM 1038 C CA . ILE A 1 141 ? 63.953 18.206 43.796 1.00 12.23 ? 141 ILE A CA 1 ATOM 1039 C C . ILE A 1 141 ? 63.864 17.236 42.618 1.00 13.21 ? 141 ILE A C 1 ATOM 1040 O O . ILE A 1 141 ? 64.882 16.993 41.962 1.00 16.21 ? 141 ILE A O 1 ATOM 1041 C CB . ILE A 1 141 ? 64.421 19.587 43.284 1.00 17.30 ? 141 ILE A CB 1 ATOM 1042 C CG1 . ILE A 1 141 ? 64.634 20.596 44.425 1.00 13.92 ? 141 ILE A CG1 1 ATOM 1043 C CG2 . ILE A 1 141 ? 63.398 20.148 42.296 1.00 19.95 ? 141 ILE A CG2 1 ATOM 1044 C CD1 . ILE A 1 141 ? 63.405 20.826 45.277 1.00 16.04 ? 141 ILE A CD1 1 ATOM 1045 N N . PRO A 1 142 ? 62.658 16.749 42.334 1.00 15.46 ? 142 PRO A N 1 ATOM 1046 C CA . PRO A 1 142 ? 62.509 15.847 41.174 1.00 18.47 ? 142 PRO A CA 1 ATOM 1047 C C . PRO A 1 142 ? 62.934 16.558 39.895 1.00 22.51 ? 142 PRO A C 1 ATOM 1048 O O . PRO A 1 142 ? 62.796 17.775 39.781 1.00 17.79 ? 142 PRO A O 1 ATOM 1049 C CB . PRO A 1 142 ? 61.014 15.536 41.140 1.00 18.46 ? 142 PRO A CB 1 ATOM 1050 C CG . PRO A 1 142 ? 60.511 15.823 42.513 1.00 18.72 ? 142 PRO A CG 1 ATOM 1051 C CD . PRO A 1 142 ? 61.407 16.905 43.077 1.00 15.94 ? 142 PRO A CD 1 ATOM 1052 N N . GLU A 1 143 ? 63.430 15.822 38.923 1.00 16.98 ? 143 GLU A N 1 ATOM 1053 C CA . GLU A 1 143 ? 63.892 16.388 37.652 1.00 16.99 ? 143 GLU A CA 1 ATOM 1054 C C . GLU A 1 143 ? 63.215 15.657 36.470 1.00 13.89 ? 143 GLU A C 1 ATOM 1055 O O . GLU A 1 143 ? 62.809 14.498 36.627 1.00 16.33 ? 143 GLU A O 1 ATOM 1056 C CB . GLU A 1 143 ? 65.406 16.283 37.543 1.00 17.57 ? 143 GLU A CB 1 ATOM 1057 C CG . GLU A 1 143 ? 66.147 17.173 38.555 1.00 18.10 ? 143 GLU A CG 1 ATOM 1058 C CD . GLU A 1 143 ? 67.623 17.240 38.177 1.00 25.15 ? 143 GLU A CD 1 ATOM 1059 O OE1 . GLU A 1 143 ? 68.427 16.477 38.743 1.00 24.81 ? 143 GLU A OE1 1 ATOM 1060 O OE2 . GLU A 1 143 ? 68.000 18.070 37.323 1.00 26.44 ? 143 GLU A OE2 1 ATOM 1061 N N . PRO A 1 144 ? 63.004 16.343 35.363 1.00 16.56 ? 144 PRO A N 1 ATOM 1062 C CA . PRO A 1 144 ? 62.180 15.775 34.292 1.00 16.80 ? 144 PRO A CA 1 ATOM 1063 C C . PRO A 1 144 ? 62.850 14.593 33.603 1.00 20.88 ? 144 PRO A C 1 ATOM 1064 O O . PRO A 1 144 ? 62.099 13.842 32.960 1.00 17.05 ? 144 PRO A O 1 ATOM 1065 C CB . PRO A 1 144 ? 61.970 16.939 33.317 1.00 16.18 ? 144 PRO A CB 1 ATOM 1066 C CG . PRO A 1 144 ? 63.138 17.847 33.564 1.00 21.77 ? 144 PRO A CG 1 ATOM 1067 C CD . PRO A 1 144 ? 63.462 17.706 35.031 1.00 18.41 ? 144 PRO A CD 1 ATOM 1068 N N . GLN A 1 145 ? 64.143 14.340 33.799 1.00 16.47 ? 145 GLN A N 1 ATOM 1069 C CA . GLN A 1 145 ? 64.786 13.151 33.231 1.00 20.75 ? 145 GLN A CA 1 ATOM 1070 C C . GLN A 1 145 ? 64.657 11.940 34.146 1.00 13.21 ? 145 GLN A C 1 ATOM 1071 O O . GLN A 1 145 ? 65.034 10.812 33.820 1.00 16.12 ? 145 GLN A O 1 ATOM 1072 C CB . GLN A 1 145 ? 66.265 13.462 32.949 1.00 18.71 ? 145 GLN A CB 1 ATOM 1073 C CG . GLN A 1 145 ? 67.058 13.726 34.231 1.00 17.99 ? 145 GLN A CG 1 ATOM 1074 C CD . GLN A 1 145 ? 67.200 15.213 34.524 1.00 25.61 ? 145 GLN A CD 1 ATOM 1075 O OE1 . GLN A 1 145 ? 66.364 16.030 34.123 1.00 21.40 ? 145 GLN A OE1 1 ATOM 1076 N NE2 . GLN A 1 145 ? 68.233 15.597 35.262 1.00 22.78 ? 145 GLN A NE2 1 ATOM 1077 N N . ASP A 1 146 ? 64.078 12.145 35.324 1.00 15.14 ? 146 ASP A N 1 ATOM 1078 C CA . ASP A 1 146 ? 64.048 11.077 36.324 1.00 13.45 ? 146 ASP A CA 1 ATOM 1079 C C . ASP A 1 146 ? 63.026 10.003 35.940 1.00 15.02 ? 146 ASP A C 1 ATOM 1080 O O . ASP A 1 146 ? 61.982 10.288 35.331 1.00 18.63 ? 146 ASP A O 1 ATOM 1081 C CB . ASP A 1 146 ? 63.661 11.649 37.697 1.00 15.71 ? 146 ASP A CB 1 ATOM 1082 C CG . ASP A 1 146 ? 64.748 12.495 38.350 1.00 17.01 ? 146 ASP A CG 1 ATOM 1083 O OD1 . ASP A 1 146 ? 64.406 13.185 39.339 1.00 17.05 ? 146 ASP A OD1 1 ATOM 1084 O OD2 . ASP A 1 146 ? 65.891 12.485 37.882 1.00 15.53 ? 146 ASP A OD2 1 ATOM 1085 N N . SER A 1 147 ? 63.284 8.768 36.333 1.00 16.54 ? 147 SER A N 1 ATOM 1086 C CA . SER A 1 147 ? 62.322 7.692 36.101 1.00 15.81 ? 147 SER A CA 1 ATOM 1087 C C . SER A 1 147 ? 61.137 7.806 37.049 1.00 19.00 ? 147 SER A C 1 ATOM 1088 O O . SER A 1 147 ? 61.236 8.458 38.090 1.00 17.28 ? 147 SER A O 1 ATOM 1089 C CB . SER A 1 147 ? 62.990 6.333 36.403 1.00 14.86 ? 147 SER A CB 1 ATOM 1090 O OG . SER A 1 147 ? 63.103 6.215 37.822 1.00 18.16 ? 147 SER A OG 1 ATOM 1091 N N . VAL A 1 148 ? 60.045 7.096 36.752 1.00 12.01 ? 148 VAL A N 1 ATOM 1092 C CA . VAL A 1 148 ? 58.866 7.113 37.596 1.00 13.67 ? 148 VAL A CA 1 ATOM 1093 C C . VAL A 1 148 ? 59.215 6.506 38.960 1.00 19.07 ? 148 VAL A C 1 ATOM 1094 O O . VAL A 1 148 ? 58.831 7.049 39.992 1.00 16.59 ? 148 VAL A O 1 ATOM 1095 C CB . VAL A 1 148 ? 57.737 6.291 36.927 1.00 17.85 ? 148 VAL A CB 1 ATOM 1096 C CG1 . VAL A 1 148 ? 56.588 6.077 37.900 1.00 12.58 ? 148 VAL A CG1 1 ATOM 1097 C CG2 . VAL A 1 148 ? 57.258 7.039 35.679 1.00 16.73 ? 148 VAL A CG2 1 ATOM 1098 N N . THR A 1 149 ? 59.995 5.418 38.969 1.00 15.53 ? 149 THR A N 1 ATOM 1099 C CA . THR A 1 149 ? 60.390 4.852 40.263 1.00 14.31 ? 149 THR A CA 1 ATOM 1100 C C . THR A 1 149 ? 61.104 5.866 41.161 1.00 14.69 ? 149 THR A C 1 ATOM 1101 O O . THR A 1 149 ? 60.786 6.010 42.346 1.00 16.89 ? 149 THR A O 1 ATOM 1102 C CB . THR A 1 149 ? 61.330 3.663 40.011 1.00 18.70 ? 149 THR A CB 1 ATOM 1103 O OG1 . THR A 1 149 ? 60.583 2.558 39.476 1.00 17.25 ? 149 THR A OG1 1 ATOM 1104 C CG2 . THR A 1 149 ? 61.929 3.215 41.357 1.00 17.47 ? 149 THR A CG2 1 ATOM 1105 N N . LYS A 1 150 ? 62.057 6.590 40.580 1.00 14.28 ? 150 LYS A N 1 ATOM 1106 C CA . LYS A 1 150 ? 62.792 7.659 41.261 1.00 11.10 ? 150 LYS A CA 1 ATOM 1107 C C . LYS A 1 150 ? 61.873 8.766 41.749 1.00 19.74 ? 150 LYS A C 1 ATOM 1108 O O . LYS A 1 150 ? 61.947 9.218 42.885 1.00 18.23 ? 150 LYS A O 1 ATOM 1109 C CB . LYS A 1 150 ? 63.848 8.277 40.339 1.00 13.80 ? 150 LYS A CB 1 ATOM 1110 C CG . LYS A 1 150 ? 64.780 9.227 41.098 1.00 22.79 ? 150 LYS A CG 1 ATOM 1111 C CD . LYS A 1 150 ? 65.919 9.720 40.207 1.00 19.81 ? 150 LYS A CD 1 ATOM 1112 C CE . LYS A 1 150 ? 66.775 10.748 40.949 1.00 20.08 ? 150 LYS A CE 1 ATOM 1113 N NZ . LYS A 1 150 ? 68.134 10.832 40.367 1.00 39.11 ? 150 LYS A NZ 1 ATOM 1114 N N . ILE A 1 151 ? 60.987 9.238 40.865 1.00 16.54 ? 151 ILE A N 1 ATOM 1115 C CA . ILE A 1 151 ? 60.035 10.278 41.245 1.00 18.54 ? 151 ILE A CA 1 ATOM 1116 C C . ILE A 1 151 ? 59.119 9.827 42.358 1.00 13.89 ? 151 ILE A C 1 ATOM 1117 O O . ILE A 1 151 ? 58.959 10.465 43.404 1.00 17.58 ? 151 ILE A O 1 ATOM 1118 C CB . ILE A 1 151 ? 59.249 10.727 39.995 1.00 17.17 ? 151 ILE A CB 1 ATOM 1119 C CG1 . ILE A 1 151 ? 60.129 11.456 38.959 1.00 13.75 ? 151 ILE A CG1 1 ATOM 1120 C CG2 . ILE A 1 151 ? 58.041 11.570 40.374 1.00 16.20 ? 151 ILE A CG2 1 ATOM 1121 C CD1 . ILE A 1 151 ? 59.396 11.530 37.611 1.00 18.84 ? 151 ILE A CD1 1 ATOM 1122 N N . LEU A 1 152 ? 58.498 8.645 42.228 1.00 16.65 ? 152 LEU A N 1 ATOM 1123 C CA . LEU A 1 152 ? 57.575 8.180 43.255 1.00 14.34 ? 152 LEU A CA 1 ATOM 1124 C C . LEU A 1 152 ? 58.310 8.017 44.585 1.00 16.18 ? 152 LEU A C 1 ATOM 1125 O O . LEU A 1 152 ? 57.794 8.396 45.637 1.00 15.53 ? 152 LEU A O 1 ATOM 1126 C CB . LEU A 1 152 ? 56.893 6.859 42.816 1.00 13.90 ? 152 LEU A CB 1 ATOM 1127 C CG . LEU A 1 152 ? 55.893 7.075 41.651 1.00 17.10 ? 152 LEU A CG 1 ATOM 1128 C CD1 . LEU A 1 152 ? 55.252 5.756 41.241 1.00 21.03 ? 152 LEU A CD1 1 ATOM 1129 C CD2 . LEU A 1 152 ? 54.834 8.108 42.012 1.00 12.73 ? 152 LEU A CD2 1 ATOM 1130 N N . GLN A 1 153 ? 59.550 7.535 44.523 1.00 14.87 ? 153 GLN A N 1 ATOM 1131 C CA . GLN A 1 153 ? 60.335 7.364 45.753 1.00 17.90 ? 153 GLN A CA 1 ATOM 1132 C C . GLN A 1 153 ? 60.600 8.745 46.359 1.00 19.53 ? 153 GLN A C 1 ATOM 1133 O O . GLN A 1 153 ? 60.512 8.819 47.578 1.00 17.86 ? 153 GLN A O 1 ATOM 1134 C CB . GLN A 1 153 ? 61.668 6.656 45.493 1.00 19.26 ? 153 GLN A CB 1 ATOM 1135 C CG . GLN A 1 153 ? 62.278 6.060 46.765 1.00 29.16 ? 153 GLN A CG 1 ATOM 1136 C CD . GLN A 1 153 ? 63.130 7.031 47.557 1.00 39.73 ? 153 GLN A CD 1 ATOM 1137 O OE1 . GLN A 1 153 ? 63.500 8.062 46.985 1.00 40.99 ? 153 GLN A OE1 1 ATOM 1138 N NE2 . GLN A 1 153 ? 63.333 6.815 48.852 1.00 28.25 ? 153 GLN A NE2 1 ATOM 1139 N N . ARG A 1 154 ? 60.977 9.727 45.542 1.00 15.66 ? 154 ARG A N 1 ATOM 1140 C CA . ARG A 1 154 ? 61.293 11.036 46.127 1.00 14.63 ? 154 ARG A CA 1 ATOM 1141 C C . ARG A 1 154 ? 60.078 11.539 46.891 1.00 17.35 ? 154 ARG A C 1 ATOM 1142 O O . ARG A 1 154 ? 60.173 12.086 48.011 1.00 17.89 ? 154 ARG A O 1 ATOM 1143 C CB . ARG A 1 154 ? 61.735 11.990 45.009 1.00 17.53 ? 154 ARG A CB 1 ATOM 1144 C CG . ARG A 1 154 ? 62.133 13.398 45.449 1.00 13.53 ? 154 ARG A CG 1 ATOM 1145 C CD . ARG A 1 154 ? 63.492 13.416 46.146 1.00 15.43 ? 154 ARG A CD 1 ATOM 1146 N NE . ARG A 1 154 ? 63.403 13.111 47.578 1.00 18.67 ? 154 ARG A NE 1 ATOM 1147 C CZ . ARG A 1 154 ? 62.963 13.921 48.536 1.00 17.51 ? 154 ARG A CZ 1 ATOM 1148 N NH1 . ARG A 1 154 ? 62.541 15.155 48.274 1.00 16.01 ? 154 ARG A NH1 1 ATOM 1149 N NH2 . ARG A 1 154 ? 62.899 13.504 49.797 1.00 13.53 ? 154 ARG A NH2 1 ATOM 1150 N N . PHE A 1 155 ? 58.879 11.421 46.281 1.00 15.09 ? 155 PHE A N 1 ATOM 1151 C CA . PHE A 1 155 ? 57.696 11.976 46.942 1.00 17.41 ? 155 PHE A CA 1 ATOM 1152 C C . PHE A 1 155 ? 57.311 11.190 48.186 1.00 15.74 ? 155 PHE A C 1 ATOM 1153 O O . PHE A 1 155 ? 56.812 11.680 49.209 1.00 17.10 ? 155 PHE A O 1 ATOM 1154 C CB . PHE A 1 155 ? 56.545 11.984 45.931 1.00 16.16 ? 155 PHE A CB 1 ATOM 1155 C CG . PHE A 1 155 ? 56.492 13.226 45.057 1.00 14.18 ? 155 PHE A CG 1 ATOM 1156 C CD1 . PHE A 1 155 ? 55.785 14.348 45.449 1.00 16.54 ? 155 PHE A CD1 1 ATOM 1157 C CD2 . PHE A 1 155 ? 57.135 13.254 43.823 1.00 18.55 ? 155 PHE A CD2 1 ATOM 1158 C CE1 . PHE A 1 155 ? 55.703 15.491 44.658 1.00 16.09 ? 155 PHE A CE1 1 ATOM 1159 C CE2 . PHE A 1 155 ? 57.049 14.380 43.015 1.00 22.83 ? 155 PHE A CE2 1 ATOM 1160 C CZ . PHE A 1 155 ? 56.313 15.484 43.413 1.00 19.70 ? 155 PHE A CZ 1 ATOM 1161 N N . GLU A 1 156 ? 57.570 9.869 48.156 1.00 17.38 ? 156 GLU A N 1 ATOM 1162 C CA . GLU A 1 156 ? 57.229 9.080 49.336 1.00 15.20 ? 156 GLU A CA 1 ATOM 1163 C C . GLU A 1 156 ? 58.213 9.439 50.463 1.00 12.74 ? 156 GLU A C 1 ATOM 1164 O O . GLU A 1 156 ? 57.762 9.444 51.595 1.00 16.92 ? 156 GLU A O 1 ATOM 1165 C CB . GLU A 1 156 ? 57.383 7.581 49.069 1.00 23.69 ? 156 GLU A CB 1 ATOM 1166 C CG . GLU A 1 156 ? 57.216 6.721 50.321 1.00 25.96 ? 156 GLU A CG 1 ATOM 1167 C CD . GLU A 1 156 ? 57.315 5.249 49.958 1.00 45.72 ? 156 GLU A CD 1 ATOM 1168 O OE1 . GLU A 1 156 ? 56.751 4.421 50.697 1.00 51.92 ? 156 GLU A OE1 1 ATOM 1169 O OE2 . GLU A 1 156 ? 57.938 4.933 48.919 1.00 43.72 ? 156 GLU A OE2 1 ATOM 1170 N N . ASP A 1 157 ? 59.469 9.652 50.078 1.00 17.10 ? 157 ASP A N 1 ATOM 1171 C CA . ASP A 1 157 ? 60.499 9.955 51.091 1.00 14.15 ? 157 ASP A CA 1 ATOM 1172 C C . ASP A 1 157 ? 60.227 11.346 51.659 1.00 18.77 ? 157 ASP A C 1 ATOM 1173 O O . ASP A 1 157 ? 60.430 11.656 52.836 1.00 19.12 ? 157 ASP A O 1 ATOM 1174 C CB . ASP A 1 157 ? 61.882 9.865 50.459 1.00 14.52 ? 157 ASP A CB 1 ATOM 1175 C CG . ASP A 1 157 ? 62.947 10.275 51.493 1.00 19.24 ? 157 ASP A CG 1 ATOM 1176 O OD1 . ASP A 1 157 ? 63.692 11.240 51.258 1.00 19.04 ? 157 ASP A OD1 1 ATOM 1177 O OD2 . ASP A 1 157 ? 62.964 9.615 52.548 1.00 19.84 ? 157 ASP A OD2 1 ATOM 1178 N N . ALA A 1 158 ? 59.757 12.262 50.807 1.00 15.10 ? 158 ALA A N 1 ATOM 1179 C CA . ALA A 1 158 ? 59.561 13.640 51.251 1.00 11.99 ? 158 ALA A CA 1 ATOM 1180 C C . ALA A 1 158 ? 58.377 13.787 52.188 1.00 16.30 ? 158 ALA A C 1 ATOM 1181 O O . ALA A 1 158 ? 58.431 14.524 53.181 1.00 19.00 ? 158 ALA A O 1 ATOM 1182 C CB . ALA A 1 158 ? 59.388 14.581 50.067 1.00 13.90 ? 158 ALA A CB 1 ATOM 1183 N N . GLY A 1 159 ? 57.255 13.111 51.929 1.00 13.64 ? 159 GLY A N 1 ATOM 1184 C CA . GLY A 1 159 ? 56.154 13.229 52.876 1.00 19.75 ? 159 GLY A CA 1 ATOM 1185 C C . GLY A 1 159 ? 55.091 12.151 52.791 1.00 18.74 ? 159 GLY A C 1 ATOM 1186 O O . GLY A 1 159 ? 53.915 12.443 53.043 1.00 17.91 ? 159 GLY A O 1 ATOM 1187 N N . GLY A 1 160 ? 55.429 10.912 52.436 1.00 15.04 ? 160 GLY A N 1 ATOM 1188 C CA . GLY A 1 160 ? 54.359 9.897 52.434 1.00 16.65 ? 160 GLY A CA 1 ATOM 1189 C C . GLY A 1 160 ? 53.418 10.019 51.253 1.00 17.27 ? 160 GLY A C 1 ATOM 1190 O O . GLY A 1 160 ? 52.347 9.406 51.277 1.00 20.41 ? 160 GLY A O 1 ATOM 1191 N N . PHE A 1 161 ? 53.738 10.806 50.211 1.00 16.56 ? 161 PHE A N 1 ATOM 1192 C CA . PHE A 1 161 ? 52.746 10.976 49.124 1.00 16.70 ? 161 PHE A CA 1 ATOM 1193 C C . PHE A 1 161 ? 52.543 9.681 48.354 1.00 17.26 ? 161 PHE A C 1 ATOM 1194 O O . PHE A 1 161 ? 53.509 9.001 47.986 1.00 16.24 ? 161 PHE A O 1 ATOM 1195 C CB . PHE A 1 161 ? 53.234 12.022 48.088 1.00 17.13 ? 161 PHE A CB 1 ATOM 1196 C CG . PHE A 1 161 ? 53.273 13.426 48.660 1.00 14.56 ? 161 PHE A CG 1 ATOM 1197 C CD1 . PHE A 1 161 ? 54.457 13.958 49.130 1.00 19.42 ? 161 PHE A CD1 1 ATOM 1198 C CD2 . PHE A 1 161 ? 52.102 14.166 48.745 1.00 15.83 ? 161 PHE A CD2 1 ATOM 1199 C CE1 . PHE A 1 161 ? 54.459 15.227 49.685 1.00 19.48 ? 161 PHE A CE1 1 ATOM 1200 C CE2 . PHE A 1 161 ? 52.106 15.442 49.284 1.00 20.72 ? 161 PHE A CE2 1 ATOM 1201 C CZ . PHE A 1 161 ? 53.288 15.956 49.774 1.00 19.17 ? 161 PHE A CZ 1 ATOM 1202 N N . THR A 1 162 ? 51.262 9.409 48.049 1.00 17.52 ? 162 THR A N 1 ATOM 1203 C CA . THR A 1 162 ? 50.966 8.228 47.230 1.00 14.46 ? 162 THR A CA 1 ATOM 1204 C C . THR A 1 162 ? 51.082 8.572 45.742 1.00 15.56 ? 162 THR A C 1 ATOM 1205 O O . THR A 1 162 ? 51.070 9.754 45.382 1.00 15.94 ? 162 THR A O 1 ATOM 1206 C CB . THR A 1 162 ? 49.526 7.770 47.522 1.00 19.54 ? 162 THR A CB 1 ATOM 1207 O OG1 . THR A 1 162 ? 48.676 8.859 47.127 1.00 17.14 ? 162 THR A OG1 1 ATOM 1208 C CG2 . THR A 1 162 ? 49.299 7.571 49.015 1.00 17.10 ? 162 THR A CG2 1 ATOM 1209 N N . PRO A 1 163 ? 51.148 7.595 44.842 1.00 16.98 ? 163 PRO A N 1 ATOM 1210 C CA . PRO A 1 163 ? 51.189 7.923 43.412 1.00 14.42 ? 163 PRO A CA 1 ATOM 1211 C C . PRO A 1 163 ? 49.972 8.739 42.990 1.00 12.23 ? 163 PRO A C 1 ATOM 1212 O O . PRO A 1 163 ? 50.086 9.630 42.144 1.00 15.65 ? 163 PRO A O 1 ATOM 1213 C CB . PRO A 1 163 ? 51.163 6.523 42.765 1.00 17.03 ? 163 PRO A CB 1 ATOM 1214 C CG . PRO A 1 163 ? 51.974 5.710 43.740 1.00 15.42 ? 163 PRO A CG 1 ATOM 1215 C CD . PRO A 1 163 ? 51.454 6.166 45.082 1.00 15.22 ? 163 PRO A CD 1 ATOM 1216 N N . PHE A 1 164 ? 48.822 8.526 43.594 1.00 13.17 ? 164 PHE A N 1 ATOM 1217 C CA . PHE A 1 164 ? 47.638 9.336 43.256 1.00 18.55 ? 164 PHE A CA 1 ATOM 1218 C C . PHE A 1 164 ? 47.906 10.793 43.601 1.00 17.34 ? 164 PHE A C 1 ATOM 1219 O O . PHE A 1 164 ? 47.656 11.691 42.781 1.00 15.02 ? 164 PHE A O 1 ATOM 1220 C CB . PHE A 1 164 ? 46.392 8.811 43.987 1.00 13.50 ? 164 PHE A CB 1 ATOM 1221 C CG . PHE A 1 164 ? 45.155 9.652 43.700 1.00 18.78 ? 164 PHE A CG 1 ATOM 1222 C CD1 . PHE A 1 164 ? 44.422 9.418 42.542 1.00 16.86 ? 164 PHE A CD1 1 ATOM 1223 C CD2 . PHE A 1 164 ? 44.728 10.651 44.560 1.00 18.94 ? 164 PHE A CD2 1 ATOM 1224 C CE1 . PHE A 1 164 ? 43.291 10.164 42.256 1.00 15.28 ? 164 PHE A CE1 1 ATOM 1225 C CE2 . PHE A 1 164 ? 43.635 11.446 44.252 1.00 18.04 ? 164 PHE A CE2 1 ATOM 1226 C CZ . PHE A 1 164 ? 42.937 11.226 43.076 1.00 19.35 ? 164 PHE A CZ 1 ATOM 1227 N N . GLU A 1 165 ? 48.491 11.012 44.790 1.00 14.07 ? 165 GLU A N 1 ATOM 1228 C CA . GLU A 1 165 ? 48.752 12.410 45.185 1.00 16.47 ? 165 GLU A CA 1 ATOM 1229 C C . GLU A 1 165 ? 49.772 13.083 44.281 1.00 17.37 ? 165 GLU A C 1 ATOM 1230 O O . GLU A 1 165 ? 49.672 14.281 43.949 1.00 16.32 ? 165 GLU A O 1 ATOM 1231 C CB . GLU A 1 165 ? 49.201 12.444 46.664 1.00 16.37 ? 165 GLU A CB 1 ATOM 1232 C CG . GLU A 1 165 ? 48.009 12.123 47.585 1.00 13.73 ? 165 GLU A CG 1 ATOM 1233 C CD . GLU A 1 165 ? 48.476 11.901 49.016 1.00 19.40 ? 165 GLU A CD 1 ATOM 1234 O OE1 . GLU A 1 165 ? 47.676 12.173 49.935 1.00 23.43 ? 165 GLU A OE1 1 ATOM 1235 O OE2 . GLU A 1 165 ? 49.598 11.384 49.201 1.00 19.11 ? 165 GLU A OE2 1 ATOM 1236 N N . VAL A 1 166 ? 50.780 12.296 43.866 1.00 17.46 ? 166 VAL A N 1 ATOM 1237 C CA . VAL A 1 166 ? 51.831 12.807 42.990 1.00 12.87 ? 166 VAL A CA 1 ATOM 1238 C C . VAL A 1 166 ? 51.236 13.264 41.658 1.00 12.55 ? 166 VAL A C 1 ATOM 1239 O O . VAL A 1 166 ? 51.477 14.364 41.173 1.00 15.24 ? 166 VAL A O 1 ATOM 1240 C CB . VAL A 1 166 ? 52.939 11.789 42.729 1.00 13.08 ? 166 VAL A CB 1 ATOM 1241 C CG1 . VAL A 1 166 ? 53.890 12.266 41.640 1.00 15.20 ? 166 VAL A CG1 1 ATOM 1242 C CG2 . VAL A 1 166 ? 53.706 11.508 44.026 1.00 15.38 ? 166 VAL A CG2 1 ATOM 1243 N N . VAL A 1 167 ? 50.443 12.383 41.030 1.00 12.77 ? 167 VAL A N 1 ATOM 1244 C CA . VAL A 1 167 ? 49.861 12.836 39.742 1.00 11.99 ? 167 VAL A CA 1 ATOM 1245 C C . VAL A 1 167 ? 48.888 13.974 39.934 1.00 13.08 ? 167 VAL A C 1 ATOM 1246 O O . VAL A 1 167 ? 48.791 14.876 39.098 1.00 15.31 ? 167 VAL A O 1 ATOM 1247 C CB . VAL A 1 167 ? 49.166 11.626 39.072 1.00 16.92 ? 167 VAL A CB 1 ATOM 1248 C CG1 . VAL A 1 167 ? 48.536 12.086 37.774 1.00 14.09 ? 167 VAL A CG1 1 ATOM 1249 C CG2 . VAL A 1 167 ? 50.194 10.514 38.848 1.00 16.24 ? 167 VAL A CG2 1 ATOM 1250 N N . SER A 1 168 ? 48.169 14.001 41.062 1.00 12.35 ? 168 SER A N 1 ATOM 1251 C CA . SER A 1 168 ? 47.286 15.086 41.454 1.00 13.88 ? 168 SER A CA 1 ATOM 1252 C C . SER A 1 168 ? 48.016 16.425 41.483 1.00 13.40 ? 168 SER A C 1 ATOM 1253 O O . SER A 1 168 ? 47.516 17.433 41.002 1.00 16.25 ? 168 SER A O 1 ATOM 1254 C CB . SER A 1 168 ? 46.706 14.844 42.853 1.00 13.11 ? 168 SER A CB 1 ATOM 1255 O OG . SER A 1 168 ? 45.785 13.770 42.807 1.00 13.08 ? 168 SER A OG 1 ATOM 1256 N N . LEU A 1 169 ? 49.219 16.432 42.072 1.00 13.73 ? 169 LEU A N 1 ATOM 1257 C CA . LEU A 1 169 ? 49.978 17.684 42.158 1.00 12.13 ? 169 LEU A CA 1 ATOM 1258 C C . LEU A 1 169 ? 50.407 18.155 40.783 1.00 12.84 ? 169 LEU A C 1 ATOM 1259 O O . LEU A 1 169 ? 50.590 19.351 40.530 1.00 14.90 ? 169 LEU A O 1 ATOM 1260 C CB . LEU A 1 169 ? 51.221 17.442 43.053 1.00 13.60 ? 169 LEU A CB 1 ATOM 1261 C CG . LEU A 1 169 ? 50.911 17.344 44.538 1.00 13.50 ? 169 LEU A CG 1 ATOM 1262 C CD1 . LEU A 1 169 ? 52.151 16.936 45.352 1.00 19.49 ? 169 LEU A CD1 1 ATOM 1263 C CD2 . LEU A 1 169 ? 50.313 18.625 45.092 1.00 12.96 ? 169 LEU A CD2 1 ATOM 1264 N N . LEU A 1 170 ? 50.562 17.191 39.870 1.00 12.95 ? 170 LEU A N 1 ATOM 1265 C CA . LEU A 1 170 ? 50.986 17.511 38.513 1.00 14.71 ? 170 LEU A CA 1 ATOM 1266 C C . LEU A 1 170 ? 49.861 18.146 37.727 1.00 16.55 ? 170 LEU A C 1 ATOM 1267 O O . LEU A 1 170 ? 50.100 18.687 36.652 1.00 17.52 ? 170 LEU A O 1 ATOM 1268 C CB . LEU A 1 170 ? 51.544 16.262 37.825 1.00 17.56 ? 170 LEU A CB 1 ATOM 1269 C CG . LEU A 1 170 ? 53.021 16.018 38.160 1.00 17.56 ? 170 LEU A CG 1 ATOM 1270 C CD1 . LEU A 1 170 ? 53.437 14.649 37.646 1.00 16.41 ? 170 LEU A CD1 1 ATOM 1271 C CD2 . LEU A 1 170 ? 53.886 17.081 37.475 1.00 24.78 ? 170 LEU A CD2 1 ATOM 1272 N N . ALA A 1 171 ? 48.688 18.352 38.319 1.00 13.83 ? 171 ALA A N 1 ATOM 1273 C CA . ALA A 1 171 ? 47.691 19.213 37.647 1.00 9.27 ? 171 ALA A CA 1 ATOM 1274 C C . ALA A 1 171 ? 48.260 20.615 37.490 1.00 15.12 ? 171 ALA A C 1 ATOM 1275 O O . ALA A 1 171 ? 47.765 21.384 36.663 1.00 14.89 ? 171 ALA A O 1 ATOM 1276 C CB . ALA A 1 171 ? 46.396 19.229 38.430 1.00 14.59 ? 171 ALA A CB 1 ATOM 1277 N N . SER A 1 172 ? 49.263 20.988 38.319 1.00 15.74 ? 172 SER A N 1 ATOM 1278 C CA . SER A 1 172 ? 49.887 22.305 38.166 1.00 12.58 ? 172 SER A CA 1 ATOM 1279 C C . SER A 1 172 ? 50.585 22.445 36.818 1.00 16.26 ? 172 SER A C 1 ATOM 1280 O O . SER A 1 172 ? 50.775 23.567 36.368 1.00 13.11 ? 172 SER A O 1 ATOM 1281 C CB . SER A 1 172 ? 50.901 22.591 39.277 1.00 16.05 ? 172 SER A CB 1 ATOM 1282 O OG . SER A 1 172 ? 51.967 21.667 39.141 1.00 25.46 ? 172 SER A OG 1 ATOM 1283 N N . HIS A 1 173 ? 50.878 21.348 36.109 1.00 12.41 ? 173 HIS A N 1 ATOM 1284 C CA . HIS A 1 173 ? 51.444 21.513 34.771 1.00 11.94 ? 173 HIS A CA 1 ATOM 1285 C C . HIS A 1 173 ? 50.372 21.928 33.761 1.00 15.78 ? 173 HIS A C 1 ATOM 1286 O O . HIS A 1 173 ? 50.752 22.206 32.619 1.00 16.13 ? 173 HIS A O 1 ATOM 1287 C CB . HIS A 1 173 ? 52.203 20.255 34.358 1.00 15.13 ? 173 HIS A CB 1 ATOM 1288 C CG . HIS A 1 173 ? 53.547 20.211 35.056 1.00 14.20 ? 173 HIS A CG 1 ATOM 1289 N ND1 . HIS A 1 173 ? 54.522 19.318 34.691 1.00 17.88 ? 173 HIS A ND1 1 ATOM 1290 C CD2 . HIS A 1 173 ? 54.069 20.961 36.054 1.00 17.30 ? 173 HIS A CD2 1 ATOM 1291 C CE1 . HIS A 1 173 ? 55.600 19.523 35.440 1.00 17.23 ? 173 HIS A CE1 1 ATOM 1292 N NE2 . HIS A 1 173 ? 55.355 20.498 36.279 1.00 14.40 ? 173 HIS A NE2 1 ATOM 1293 N N . SER A 1 174 ? 49.123 22.095 34.191 1.00 14.06 ? 174 SER A N 1 ATOM 1294 C CA . SER A 1 174 ? 48.057 22.715 33.393 1.00 12.29 ? 174 SER A CA 1 ATOM 1295 C C . SER A 1 174 ? 48.281 24.227 33.281 1.00 21.54 ? 174 SER A C 1 ATOM 1296 O O . SER A 1 174 ? 47.654 24.910 32.475 1.00 15.74 ? 174 SER A O 1 ATOM 1297 C CB . SER A 1 174 ? 46.674 22.483 34.017 1.00 13.96 ? 174 SER A CB 1 ATOM 1298 O OG . SER A 1 174 ? 45.654 23.008 33.155 1.00 13.32 ? 174 SER A OG 1 ATOM 1299 N N . VAL A 1 175 ? 49.099 24.811 34.159 1.00 14.76 ? 175 VAL A N 1 ATOM 1300 C CA . VAL A 1 175 ? 49.368 26.262 34.113 1.00 14.74 ? 175 VAL A CA 1 ATOM 1301 C C . VAL A 1 175 ? 50.871 26.471 34.282 1.00 16.83 ? 175 VAL A C 1 ATOM 1302 O O . VAL A 1 175 ? 51.404 26.933 35.292 1.00 18.09 ? 175 VAL A O 1 ATOM 1303 C CB . VAL A 1 175 ? 48.587 27.026 35.194 1.00 14.59 ? 175 VAL A CB 1 ATOM 1304 C CG1 . VAL A 1 175 ? 47.110 27.050 34.859 1.00 13.61 ? 175 VAL A CG1 1 ATOM 1305 C CG2 . VAL A 1 175 ? 48.818 26.366 36.567 1.00 15.98 ? 175 VAL A CG2 1 ATOM 1306 N N . ALA A 1 176 ? 51.624 26.004 33.286 1.00 13.11 ? 176 ALA A N 1 ATOM 1307 C CA . ALA A 1 176 ? 53.063 25.884 33.480 1.00 12.02 ? 176 ALA A CA 1 ATOM 1308 C C . ALA A 1 176 ? 53.791 25.961 32.153 1.00 18.19 ? 176 ALA A C 1 ATOM 1309 O O . ALA A 1 176 ? 53.329 25.439 31.127 1.00 13.43 ? 176 ALA A O 1 ATOM 1310 C CB . ALA A 1 176 ? 53.333 24.527 34.116 1.00 14.95 ? 176 ALA A CB 1 ATOM 1311 N N . ARG A 1 177 ? 54.910 26.676 32.172 1.00 12.44 ? 177 ARG A N 1 ATOM 1312 C CA . ARG A 1 177 ? 55.799 26.737 31.013 1.00 14.54 ? 177 ARG A CA 1 ATOM 1313 C C . ARG A 1 177 ? 57.263 26.520 31.419 1.00 17.16 ? 177 ARG A C 1 ATOM 1314 O O . ARG A 1 177 ? 57.583 26.538 32.612 1.00 16.33 ? 177 ARG A O 1 ATOM 1315 C CB . ARG A 1 177 ? 55.641 28.065 30.263 1.00 13.96 ? 177 ARG A CB 1 ATOM 1316 C CG . ARG A 1 177 ? 54.184 28.438 30.051 1.00 17.92 ? 177 ARG A CG 1 ATOM 1317 C CD . ARG A 1 177 ? 53.992 29.665 29.185 1.00 19.80 ? 177 ARG A CD 1 ATOM 1318 N NE . ARG A 1 177 ? 54.449 30.872 29.888 1.00 15.66 ? 177 ARG A NE 1 ATOM 1319 C CZ . ARG A 1 177 ? 54.157 32.090 29.439 1.00 23.88 ? 177 ARG A CZ 1 ATOM 1320 N NH1 . ARG A 1 177 ? 53.408 32.229 28.355 1.00 16.46 ? 177 ARG A NH1 1 ATOM 1321 N NH2 . ARG A 1 177 ? 54.603 33.149 30.087 1.00 14.24 ? 177 ARG A NH2 1 ATOM 1322 N N . ALA A 1 178 ? 58.107 26.275 30.425 1.00 15.07 ? 178 ALA A N 1 ATOM 1323 C CA . ALA A 1 178 ? 59.515 25.936 30.560 1.00 13.58 ? 178 ALA A CA 1 ATOM 1324 C C . ALA A 1 178 ? 60.405 26.975 29.875 1.00 25.58 ? 178 ALA A C 1 ATOM 1325 O O . ALA A 1 178 ? 60.261 27.199 28.664 1.00 17.75 ? 178 ALA A O 1 ATOM 1326 C CB . ALA A 1 178 ? 59.852 24.577 29.964 1.00 16.93 ? 178 ALA A CB 1 ATOM 1327 N N . ASP A 1 179 ? 61.321 27.562 30.650 1.00 16.99 ? 179 ASP A N 1 ATOM 1328 C CA . ASP A 1 179 ? 62.344 28.428 30.078 1.00 16.51 ? 179 ASP A CA 1 ATOM 1329 C C . ASP A 1 179 ? 63.711 27.758 30.026 1.00 22.29 ? 179 ASP A C 1 ATOM 1330 O O . ASP A 1 179 ? 64.584 28.213 29.278 1.00 21.33 ? 179 ASP A O 1 ATOM 1331 C CB . ASP A 1 179 ? 62.554 29.737 30.848 1.00 17.70 ? 179 ASP A CB 1 ATOM 1332 C CG . ASP A 1 179 ? 61.321 30.601 30.952 1.00 29.02 ? 179 ASP A CG 1 ATOM 1333 O OD1 . ASP A 1 179 ? 60.395 30.475 30.125 1.00 25.50 ? 179 ASP A OD1 1 ATOM 1334 O OD2 . ASP A 1 179 ? 61.253 31.386 31.917 1.00 24.01 ? 179 ASP A OD2 1 ATOM 1335 N N . LYS A 1 180 ? 63.956 26.738 30.855 1.00 17.46 ? 180 LYS A N 1 ATOM 1336 C CA . LYS A 1 180 ? 65.347 26.295 30.971 1.00 19.97 ? 180 LYS A CA 1 ATOM 1337 C C . LYS A 1 180 ? 65.593 24.966 30.287 1.00 17.41 ? 180 LYS A C 1 ATOM 1338 O O . LYS A 1 180 ? 66.744 24.611 30.017 1.00 21.96 ? 180 LYS A O 1 ATOM 1339 C CB . LYS A 1 180 ? 65.706 26.158 32.464 1.00 24.82 ? 180 LYS A CB 1 ATOM 1340 C CG . LYS A 1 180 ? 65.576 27.453 33.240 1.00 18.93 ? 180 LYS A CG 1 ATOM 1341 C CD . LYS A 1 180 ? 66.517 28.531 32.710 1.00 21.25 ? 180 LYS A CD 1 ATOM 1342 C CE . LYS A 1 180 ? 66.315 29.787 33.563 1.00 25.93 ? 180 LYS A CE 1 ATOM 1343 N NZ . LYS A 1 180 ? 66.752 31.009 32.828 1.00 36.59 ? 180 LYS A NZ 1 ATOM 1344 N N . VAL A 1 181 ? 64.526 24.224 29.990 1.00 15.40 ? 181 VAL A N 1 ATOM 1345 C CA . VAL A 1 181 ? 64.752 22.879 29.454 1.00 12.71 ? 181 VAL A CA 1 ATOM 1346 C C . VAL A 1 181 ? 65.405 22.964 28.086 1.00 16.01 ? 181 VAL A C 1 ATOM 1347 O O . VAL A 1 181 ? 66.285 22.208 27.705 1.00 20.04 ? 181 VAL A O 1 ATOM 1348 C CB . VAL A 1 181 ? 63.419 22.116 29.331 1.00 20.62 ? 181 VAL A CB 1 ATOM 1349 C CG1 . VAL A 1 181 ? 63.624 20.770 28.650 1.00 20.29 ? 181 VAL A CG1 1 ATOM 1350 C CG2 . VAL A 1 181 ? 62.750 21.918 30.685 1.00 19.88 ? 181 VAL A CG2 1 ATOM 1351 N N . ASP A 1 182 ? 64.933 23.939 27.297 1.00 19.75 ? 182 ASP A N 1 ATOM 1352 C CA . ASP A 1 182 ? 65.586 24.140 25.999 1.00 21.54 ? 182 ASP A CA 1 ATOM 1353 C C . ASP A 1 182 ? 66.156 25.543 25.990 1.00 26.15 ? 182 ASP A C 1 ATOM 1354 O O . ASP A 1 182 ? 65.386 26.504 26.096 1.00 37.87 ? 182 ASP A O 1 ATOM 1355 C CB A ASP A 1 182 ? 64.540 23.942 24.904 0.50 37.70 ? 182 ASP A CB 1 ATOM 1356 C CB B ASP A 1 182 ? 64.640 23.971 24.804 0.50 41.47 ? 182 ASP A CB 1 ATOM 1357 C CG A ASP A 1 182 ? 64.992 24.252 23.497 0.50 51.70 ? 182 ASP A CG 1 ATOM 1358 C CG B ASP A 1 182 ? 65.249 24.662 23.587 0.50 54.16 ? 182 ASP A CG 1 ATOM 1359 O OD1 A ASP A 1 182 ? 65.819 25.156 23.239 0.50 31.73 ? 182 ASP A OD1 1 ATOM 1360 O OD1 B ASP A 1 182 ? 66.284 24.167 23.089 0.50 52.28 ? 182 ASP A OD1 1 ATOM 1361 O OD2 A ASP A 1 182 ? 64.438 23.583 22.589 0.50 31.55 ? 182 ASP A OD2 1 ATOM 1362 O OD2 B ASP A 1 182 ? 64.752 25.730 23.166 0.50 76.92 ? 182 ASP A OD2 1 ATOM 1363 N N . GLN A 1 183 ? 67.462 25.725 25.805 1.00 29.78 ? 183 GLN A N 1 ATOM 1364 C CA . GLN A 1 183 ? 67.870 27.131 25.941 1.00 47.20 ? 183 GLN A CA 1 ATOM 1365 C C . GLN A 1 183 ? 67.507 27.979 24.741 1.00 41.78 ? 183 GLN A C 1 ATOM 1366 O O . GLN A 1 183 ? 67.555 29.211 24.803 1.00 39.30 ? 183 GLN A O 1 ATOM 1367 C CB . GLN A 1 183 ? 69.341 27.224 26.333 1.00 73.46 ? 183 GLN A CB 1 ATOM 1368 C CG . GLN A 1 183 ? 69.680 26.642 27.690 1.00 91.77 ? 183 GLN A CG 1 ATOM 1369 C CD . GLN A 1 183 ? 69.123 27.361 28.900 1.00 92.67 ? 183 GLN A CD 1 ATOM 1370 O OE1 . GLN A 1 183 ? 68.605 26.723 29.828 1.00 43.90 ? 183 GLN A OE1 1 ATOM 1371 N NE2 . GLN A 1 183 ? 69.252 28.682 28.980 1.00 81.85 ? 183 GLN A NE2 1 ATOM 1372 N N . THR A 1 184 ? 67.050 27.414 23.621 1.00 23.49 ? 184 THR A N 1 ATOM 1373 C CA . THR A 1 184 ? 66.819 28.286 22.461 1.00 28.31 ? 184 THR A CA 1 ATOM 1374 C C . THR A 1 184 ? 65.456 28.957 22.508 1.00 30.04 ? 184 THR A C 1 ATOM 1375 O O . THR A 1 184 ? 65.213 30.008 21.915 1.00 39.83 ? 184 THR A O 1 ATOM 1376 C CB . THR A 1 184 ? 66.948 27.420 21.188 1.00 41.09 ? 184 THR A CB 1 ATOM 1377 O OG1 . THR A 1 184 ? 65.909 26.424 21.192 1.00 29.73 ? 184 THR A OG1 1 ATOM 1378 C CG2 . THR A 1 184 ? 68.266 26.651 21.257 1.00 34.01 ? 184 THR A CG2 1 ATOM 1379 N N . ILE A 1 185 ? 64.519 28.392 23.264 1.00 22.26 ? 185 ILE A N 1 ATOM 1380 C CA . ILE A 1 185 ? 63.186 28.994 23.337 1.00 21.14 ? 185 ILE A CA 1 ATOM 1381 C C . ILE A 1 185 ? 62.810 29.319 24.783 1.00 18.89 ? 185 ILE A C 1 ATOM 1382 O O . ILE A 1 185 ? 63.385 28.733 25.699 1.00 21.96 ? 185 ILE A O 1 ATOM 1383 C CB . ILE A 1 185 ? 62.159 27.990 22.782 1.00 23.10 ? 185 ILE A CB 1 ATOM 1384 C CG1 . ILE A 1 185 ? 62.150 26.671 23.569 1.00 22.64 ? 185 ILE A CG1 1 ATOM 1385 C CG2 . ILE A 1 185 ? 62.426 27.772 21.297 1.00 26.71 ? 185 ILE A CG2 1 ATOM 1386 C CD1 . ILE A 1 185 ? 61.263 25.608 22.932 1.00 19.50 ? 185 ILE A CD1 1 ATOM 1387 N N . ASP A 1 186 ? 61.854 30.224 24.943 1.00 21.31 ? 186 ASP A N 1 ATOM 1388 C CA . ASP A 1 186 ? 61.364 30.545 26.281 1.00 24.40 ? 186 ASP A CA 1 ATOM 1389 C C . ASP A 1 186 ? 59.867 30.268 26.368 1.00 19.88 ? 186 ASP A C 1 ATOM 1390 O O . ASP A 1 186 ? 59.115 30.347 25.396 1.00 20.28 ? 186 ASP A O 1 ATOM 1391 C CB . ASP A 1 186 ? 61.616 32.034 26.575 1.00 43.98 ? 186 ASP A CB 1 ATOM 1392 C CG . ASP A 1 186 ? 63.019 32.241 27.127 1.00 76.93 ? 186 ASP A CG 1 ATOM 1393 O OD1 . ASP A 1 186 ? 63.505 31.371 27.884 1.00 63.30 ? 186 ASP A OD1 1 ATOM 1394 O OD2 . ASP A 1 186 ? 63.639 33.267 26.776 1.00 136.45 ? 186 ASP A OD2 1 ATOM 1395 N N . ALA A 1 187 ? 59.411 30.046 27.594 1.00 20.33 ? 187 ALA A N 1 ATOM 1396 C CA . ALA A 1 187 ? 57.986 29.994 27.859 1.00 17.37 ? 187 ALA A CA 1 ATOM 1397 C C . ALA A 1 187 ? 57.278 28.953 26.982 1.00 14.62 ? 187 ALA A C 1 ATOM 1398 O O . ALA A 1 187 ? 56.182 29.230 26.501 1.00 15.77 ? 187 ALA A O 1 ATOM 1399 C CB . ALA A 1 187 ? 57.351 31.359 27.639 1.00 17.38 ? 187 ALA A CB 1 ATOM 1400 N N . ALA A 1 188 ? 57.846 27.760 26.900 1.00 16.63 ? 188 ALA A N 1 ATOM 1401 C CA . ALA A 1 188 ? 57.189 26.657 26.185 1.00 14.90 ? 188 ALA A CA 1 ATOM 1402 C C . ALA A 1 188 ? 56.142 26.006 27.078 1.00 16.51 ? 188 ALA A C 1 ATOM 1403 O O . ALA A 1 188 ? 56.481 25.359 28.087 1.00 16.32 ? 188 ALA A O 1 ATOM 1404 C CB . ALA A 1 188 ? 58.262 25.650 25.800 1.00 18.33 ? 188 ALA A CB 1 ATOM 1405 N N . PRO A 1 189 ? 54.856 26.140 26.770 1.00 17.25 ? 189 PRO A N 1 ATOM 1406 C CA . PRO A 1 189 ? 53.814 25.659 27.673 1.00 12.94 ? 189 PRO A CA 1 ATOM 1407 C C . PRO A 1 189 ? 53.665 24.144 27.732 1.00 14.52 ? 189 PRO A C 1 ATOM 1408 O O . PRO A 1 189 ? 53.875 23.496 26.696 1.00 17.86 ? 189 PRO A O 1 ATOM 1409 C CB . PRO A 1 189 ? 52.542 26.240 27.046 1.00 13.19 ? 189 PRO A CB 1 ATOM 1410 C CG . PRO A 1 189 ? 52.868 26.443 25.593 1.00 14.58 ? 189 PRO A CG 1 ATOM 1411 C CD . PRO A 1 189 ? 54.323 26.802 25.556 1.00 14.55 ? 189 PRO A CD 1 ATOM 1412 N N . PHE A 1 190 ? 53.263 23.582 28.872 1.00 14.08 ? 190 PHE A N 1 ATOM 1413 C CA . PHE A 1 190 ? 53.047 22.128 28.919 1.00 14.17 ? 190 PHE A CA 1 ATOM 1414 C C . PHE A 1 190 ? 51.655 21.736 28.439 1.00 14.73 ? 190 PHE A C 1 ATOM 1415 O O . PHE A 1 190 ? 51.388 20.554 28.164 1.00 16.23 ? 190 PHE A O 1 ATOM 1416 C CB . PHE A 1 190 ? 53.258 21.613 30.357 1.00 12.25 ? 190 PHE A CB 1 ATOM 1417 C CG . PHE A 1 190 ? 54.682 21.807 30.849 1.00 11.32 ? 190 PHE A CG 1 ATOM 1418 C CD1 . PHE A 1 190 ? 55.719 21.908 29.931 1.00 13.40 ? 190 PHE A CD1 1 ATOM 1419 C CD2 . PHE A 1 190 ? 54.970 21.873 32.204 1.00 16.86 ? 190 PHE A CD2 1 ATOM 1420 C CE1 . PHE A 1 190 ? 57.029 22.071 30.383 1.00 18.06 ? 190 PHE A CE1 1 ATOM 1421 C CE2 . PHE A 1 190 ? 56.269 22.021 32.679 1.00 18.29 ? 190 PHE A CE2 1 ATOM 1422 C CZ . PHE A 1 190 ? 57.289 22.160 31.749 1.00 17.99 ? 190 PHE A CZ 1 ATOM 1423 N N . ASP A 1 191 ? 50.685 22.652 28.312 1.00 15.51 ? 191 ASP A N 1 ATOM 1424 C CA . ASP A 1 191 ? 49.420 22.315 27.620 1.00 11.93 ? 191 ASP A CA 1 ATOM 1425 C C . ASP A 1 191 ? 48.993 23.525 26.814 1.00 15.04 ? 191 ASP A C 1 ATOM 1426 O O . ASP A 1 191 ? 49.672 24.562 26.859 1.00 14.52 ? 191 ASP A O 1 ATOM 1427 C CB . ASP A 1 191 ? 48.380 21.800 28.585 1.00 14.09 ? 191 ASP A CB 1 ATOM 1428 C CG . ASP A 1 191 ? 47.560 22.764 29.410 1.00 14.49 ? 191 ASP A CG 1 ATOM 1429 O OD1 . ASP A 1 191 ? 47.776 23.989 29.384 1.00 16.22 ? 191 ASP A OD1 1 ATOM 1430 O OD2 . ASP A 1 191 ? 46.754 22.291 30.263 1.00 13.84 ? 191 ASP A OD2 1 ATOM 1431 N N . SER A 1 192 ? 47.917 23.438 26.028 1.00 12.71 ? 192 SER A N 1 ATOM 1432 C CA . SER A 1 192 ? 47.557 24.522 25.130 1.00 18.35 ? 192 SER A CA 1 ATOM 1433 C C . SER A 1 192 ? 46.822 25.668 25.814 1.00 16.87 ? 192 SER A C 1 ATOM 1434 O O . SER A 1 192 ? 46.399 26.595 25.122 1.00 15.63 ? 192 SER A O 1 ATOM 1435 C CB . SER A 1 192 ? 46.666 24.002 23.981 1.00 13.96 ? 192 SER A CB 1 ATOM 1436 O OG . SER A 1 192 ? 45.539 23.319 24.484 1.00 15.95 ? 192 SER A OG 1 ATOM 1437 N N . THR A 1 193 ? 46.660 25.582 27.129 1.00 12.69 ? 193 THR A N 1 ATOM 1438 C CA . THR A 1 193 ? 45.905 26.572 27.894 1.00 14.55 ? 193 THR A CA 1 ATOM 1439 C C . THR A 1 193 ? 46.681 26.813 29.211 1.00 14.97 ? 193 THR A C 1 ATOM 1440 O O . THR A 1 193 ? 46.177 26.562 30.298 1.00 15.04 ? 193 THR A O 1 ATOM 1441 C CB . THR A 1 193 ? 44.512 26.038 28.204 1.00 13.86 ? 193 THR A CB 1 ATOM 1442 O OG1 . THR A 1 193 ? 44.596 24.784 28.909 1.00 14.24 ? 193 THR A OG1 1 ATOM 1443 C CG2 . THR A 1 193 ? 43.724 25.769 26.926 1.00 13.06 ? 193 THR A CG2 1 ATOM 1444 N N . PRO A 1 194 ? 47.884 27.339 29.086 1.00 16.67 ? 194 PRO A N 1 ATOM 1445 C CA . PRO A 1 194 ? 48.762 27.512 30.282 1.00 12.01 ? 194 PRO A CA 1 ATOM 1446 C C . PRO A 1 194 ? 48.297 28.608 31.230 1.00 13.98 ? 194 PRO A C 1 ATOM 1447 O O . PRO A 1 194 ? 48.959 28.813 32.260 1.00 15.07 ? 194 PRO A O 1 ATOM 1448 C CB . PRO A 1 194 ? 50.089 27.912 29.647 1.00 12.46 ? 194 PRO A CB 1 ATOM 1449 C CG . PRO A 1 194 ? 49.626 28.694 28.435 1.00 13.63 ? 194 PRO A CG 1 ATOM 1450 C CD . PRO A 1 194 ? 48.552 27.791 27.852 1.00 14.11 ? 194 PRO A CD 1 ATOM 1451 N N . PHE A 1 195 ? 47.226 29.314 30.900 1.00 15.35 ? 195 PHE A N 1 ATOM 1452 C CA . PHE A 1 195 ? 46.640 30.312 31.769 1.00 14.78 ? 195 PHE A CA 1 ATOM 1453 C C . PHE A 1 195 ? 45.339 29.803 32.378 1.00 18.19 ? 195 PHE A C 1 ATOM 1454 O O . PHE A 1 195 ? 44.627 30.582 33.023 1.00 16.69 ? 195 PHE A O 1 ATOM 1455 C CB . PHE A 1 195 ? 46.349 31.622 31.010 1.00 16.60 ? 195 PHE A CB 1 ATOM 1456 C CG . PHE A 1 195 ? 47.577 32.114 30.254 1.00 16.77 ? 195 PHE A CG 1 ATOM 1457 C CD1 . PHE A 1 195 ? 48.780 32.344 30.910 1.00 13.43 ? 195 PHE A CD1 1 ATOM 1458 C CD2 . PHE A 1 195 ? 47.531 32.325 28.889 1.00 17.21 ? 195 PHE A CD2 1 ATOM 1459 C CE1 . PHE A 1 195 ? 49.890 32.754 30.202 1.00 18.66 ? 195 PHE A CE1 1 ATOM 1460 C CE2 . PHE A 1 195 ? 48.637 32.735 28.175 1.00 18.52 ? 195 PHE A CE2 1 ATOM 1461 C CZ . PHE A 1 195 ? 49.842 32.930 28.830 1.00 19.07 ? 195 PHE A CZ 1 ATOM 1462 N N . THR A 1 196 ? 44.982 28.545 32.152 1.00 14.89 ? 196 THR A N 1 ATOM 1463 C CA . THR A 1 196 ? 43.712 27.972 32.578 1.00 15.62 ? 196 THR A CA 1 ATOM 1464 C C . THR A 1 196 ? 43.932 26.624 33.292 1.00 12.81 ? 196 THR A C 1 ATOM 1465 O O . THR A 1 196 ? 44.615 25.773 32.784 1.00 12.20 ? 196 THR A O 1 ATOM 1466 C CB . THR A 1 196 ? 42.815 27.628 31.362 1.00 16.22 ? 196 THR A CB 1 ATOM 1467 O OG1 . THR A 1 196 ? 42.654 28.806 30.532 1.00 19.29 ? 196 THR A OG1 1 ATOM 1468 C CG2 . THR A 1 196 ? 41.453 27.195 31.881 1.00 19.24 ? 196 THR A CG2 1 ATOM 1469 N N . PHE A 1 197 ? 43.408 26.527 34.501 1.00 12.74 ? 197 PHE A N 1 ATOM 1470 C CA . PHE A 1 197 ? 43.675 25.353 35.322 1.00 13.13 ? 197 PHE A CA 1 ATOM 1471 C C . PHE A 1 197 ? 42.646 24.291 34.933 1.00 14.68 ? 197 PHE A C 1 ATOM 1472 O O . PHE A 1 197 ? 41.715 24.038 35.698 1.00 15.09 ? 197 PHE A O 1 ATOM 1473 C CB . PHE A 1 197 ? 43.555 25.698 36.801 1.00 13.55 ? 197 PHE A CB 1 ATOM 1474 C CG . PHE A 1 197 ? 44.221 24.661 37.702 1.00 16.93 ? 197 PHE A CG 1 ATOM 1475 C CD1 . PHE A 1 197 ? 43.478 23.594 38.204 1.00 16.50 ? 197 PHE A CD1 1 ATOM 1476 C CD2 . PHE A 1 197 ? 45.556 24.813 38.013 1.00 16.63 ? 197 PHE A CD2 1 ATOM 1477 C CE1 . PHE A 1 197 ? 44.092 22.700 39.067 1.00 17.38 ? 197 PHE A CE1 1 ATOM 1478 C CE2 . PHE A 1 197 ? 46.183 23.889 38.835 1.00 18.25 ? 197 PHE A CE2 1 ATOM 1479 C CZ . PHE A 1 197 ? 45.452 22.802 39.309 1.00 17.82 ? 197 PHE A CZ 1 ATOM 1480 N N . ASP A 1 198 ? 42.804 23.724 33.742 1.00 14.47 ? 198 ASP A N 1 ATOM 1481 C CA . ASP A 1 198 ? 41.862 22.731 33.219 1.00 12.92 ? 198 ASP A CA 1 ATOM 1482 C C . ASP A 1 198 ? 42.538 21.383 33.053 1.00 15.29 ? 198 ASP A C 1 ATOM 1483 O O . ASP A 1 198 ? 43.692 21.224 33.493 1.00 14.44 ? 198 ASP A O 1 ATOM 1484 C CB . ASP A 1 198 ? 41.311 23.243 31.890 1.00 16.32 ? 198 ASP A CB 1 ATOM 1485 C CG . ASP A 1 198 ? 42.444 23.565 30.924 1.00 15.06 ? 198 ASP A CG 1 ATOM 1486 O OD1 . ASP A 1 198 ? 43.613 23.227 31.205 1.00 12.13 ? 198 ASP A OD1 1 ATOM 1487 O OD2 . ASP A 1 198 ? 42.151 24.182 29.872 1.00 16.00 ? 198 ASP A OD2 1 ATOM 1488 N N . THR A 1 199 ? 41.853 20.387 32.470 1.00 12.75 ? 199 THR A N 1 ATOM 1489 C CA . THR A 1 199 ? 42.488 19.056 32.385 1.00 12.81 ? 199 THR A CA 1 ATOM 1490 C C . THR A 1 199 ? 43.253 18.844 31.081 1.00 14.26 ? 199 THR A C 1 ATOM 1491 O O . THR A 1 199 ? 43.680 17.718 30.751 1.00 13.37 ? 199 THR A O 1 ATOM 1492 C CB . THR A 1 199 ? 41.395 17.978 32.550 1.00 12.62 ? 199 THR A CB 1 ATOM 1493 O OG1 . THR A 1 199 ? 40.573 17.912 31.364 1.00 14.39 ? 199 THR A OG1 1 ATOM 1494 C CG2 . THR A 1 199 ? 40.481 18.246 33.727 1.00 15.30 ? 199 THR A CG2 1 ATOM 1495 N N . GLN A 1 200 ? 43.469 19.896 30.266 1.00 11.57 ? 200 GLN A N 1 ATOM 1496 C CA . GLN A 1 200 ? 44.110 19.732 28.969 1.00 11.62 ? 200 GLN A CA 1 ATOM 1497 C C . GLN A 1 200 ? 45.457 19.022 29.033 1.00 16.74 ? 200 GLN A C 1 ATOM 1498 O O . GLN A 1 200 ? 45.798 18.189 28.147 1.00 13.33 ? 200 GLN A O 1 ATOM 1499 C CB . GLN A 1 200 ? 44.268 21.068 28.232 1.00 12.66 ? 200 GLN A CB 1 ATOM 1500 C CG . GLN A 1 200 ? 42.962 21.651 27.713 1.00 14.84 ? 200 GLN A CG 1 ATOM 1501 C CD . GLN A 1 200 ? 42.220 20.827 26.672 1.00 15.67 ? 200 GLN A CD 1 ATOM 1502 O OE1 . GLN A 1 200 ? 40.983 20.742 26.740 1.00 16.76 ? 200 GLN A OE1 1 ATOM 1503 N NE2 . GLN A 1 200 ? 42.896 20.192 25.729 1.00 15.41 ? 200 GLN A NE2 1 ATOM 1504 N N . VAL A 1 201 ? 46.298 19.371 30.023 1.00 13.33 ? 201 VAL A N 1 ATOM 1505 C CA . VAL A 1 201 ? 47.609 18.688 30.107 1.00 12.91 ? 201 VAL A CA 1 ATOM 1506 C C . VAL A 1 201 ? 47.452 17.179 30.192 1.00 11.94 ? 201 VAL A C 1 ATOM 1507 O O . VAL A 1 201 ? 48.247 16.447 29.582 1.00 15.60 ? 201 VAL A O 1 ATOM 1508 C CB . VAL A 1 201 ? 48.436 19.183 31.312 1.00 15.77 ? 201 VAL A CB 1 ATOM 1509 C CG1 . VAL A 1 201 ? 47.848 18.817 32.659 1.00 14.44 ? 201 VAL A CG1 1 ATOM 1510 C CG2 . VAL A 1 201 ? 49.890 18.702 31.206 1.00 11.59 ? 201 VAL A CG2 1 ATOM 1511 N N . PHE A 1 202 ? 46.441 16.698 30.907 1.00 14.03 ? 202 PHE A N 1 ATOM 1512 C CA . PHE A 1 202 ? 46.292 15.231 31.000 1.00 12.63 ? 202 PHE A CA 1 ATOM 1513 C C . PHE A 1 202 ? 45.982 14.616 29.645 1.00 16.90 ? 202 PHE A C 1 ATOM 1514 O O . PHE A 1 202 ? 46.544 13.610 29.212 1.00 17.32 ? 202 PHE A O 1 ATOM 1515 C CB . PHE A 1 202 ? 45.237 14.897 32.056 1.00 11.11 ? 202 PHE A CB 1 ATOM 1516 C CG . PHE A 1 202 ? 45.763 15.253 33.457 1.00 14.23 ? 202 PHE A CG 1 ATOM 1517 C CD1 . PHE A 1 202 ? 45.358 16.409 34.090 1.00 16.85 ? 202 PHE A CD1 1 ATOM 1518 C CD2 . PHE A 1 202 ? 46.696 14.425 34.076 1.00 15.40 ? 202 PHE A CD2 1 ATOM 1519 C CE1 . PHE A 1 202 ? 45.888 16.767 35.331 1.00 17.68 ? 202 PHE A CE1 1 ATOM 1520 C CE2 . PHE A 1 202 ? 47.200 14.749 35.331 1.00 17.49 ? 202 PHE A CE2 1 ATOM 1521 C CZ . PHE A 1 202 ? 46.788 15.918 35.950 1.00 14.30 ? 202 PHE A CZ 1 ATOM 1522 N N . LEU A 1 203 ? 45.102 15.312 28.898 1.00 13.54 ? 203 LEU A N 1 ATOM 1523 C CA . LEU A 1 203 ? 44.780 14.827 27.552 1.00 11.10 ? 203 LEU A CA 1 ATOM 1524 C C . LEU A 1 203 ? 45.962 14.922 26.608 1.00 14.22 ? 203 LEU A C 1 ATOM 1525 O O . LEU A 1 203 ? 46.307 14.039 25.832 1.00 14.49 ? 203 LEU A O 1 ATOM 1526 C CB . LEU A 1 203 ? 43.641 15.723 26.998 1.00 16.05 ? 203 LEU A CB 1 ATOM 1527 C CG . LEU A 1 203 ? 43.279 15.473 25.520 1.00 19.87 ? 203 LEU A CG 1 ATOM 1528 C CD1 . LEU A 1 203 ? 42.982 14.001 25.321 1.00 16.21 ? 203 LEU A CD1 1 ATOM 1529 C CD2 . LEU A 1 203 ? 42.050 16.300 25.173 1.00 20.30 ? 203 LEU A CD2 1 ATOM 1530 N N . GLU A 1 204 ? 46.615 16.097 26.605 1.00 14.94 ? 204 GLU A N 1 ATOM 1531 C CA . GLU A 1 204 ? 47.607 16.388 25.561 1.00 17.36 ? 204 GLU A CA 1 ATOM 1532 C C . GLU A 1 204 ? 48.873 15.566 25.685 1.00 14.68 ? 204 GLU A C 1 ATOM 1533 O O . GLU A 1 204 ? 49.548 15.269 24.692 1.00 15.97 ? 204 GLU A O 1 ATOM 1534 C CB . GLU A 1 204 ? 47.889 17.908 25.588 1.00 11.54 ? 204 GLU A CB 1 ATOM 1535 C CG . GLU A 1 204 ? 46.659 18.637 25.026 1.00 11.36 ? 204 GLU A CG 1 ATOM 1536 C CD . GLU A 1 204 ? 46.761 20.149 25.116 1.00 15.57 ? 204 GLU A CD 1 ATOM 1537 O OE1 . GLU A 1 204 ? 47.871 20.717 25.239 1.00 16.10 ? 204 GLU A OE1 1 ATOM 1538 O OE2 . GLU A 1 204 ? 45.671 20.771 25.093 1.00 18.73 ? 204 GLU A OE2 1 ATOM 1539 N N . VAL A 1 205 ? 49.201 15.184 26.927 1.00 12.66 ? 205 VAL A N 1 ATOM 1540 C CA . VAL A 1 205 ? 50.418 14.387 27.096 1.00 17.04 ? 205 VAL A CA 1 ATOM 1541 C C . VAL A 1 205 ? 50.187 12.996 26.516 1.00 18.64 ? 205 VAL A C 1 ATOM 1542 O O . VAL A 1 205 ? 51.172 12.343 26.196 1.00 20.06 ? 205 VAL A O 1 ATOM 1543 C CB . VAL A 1 205 ? 50.779 14.271 28.591 1.00 20.37 ? 205 VAL A CB 1 ATOM 1544 C CG1 . VAL A 1 205 ? 51.837 13.188 28.778 1.00 15.67 ? 205 VAL A CG1 1 ATOM 1545 C CG2 . VAL A 1 205 ? 51.300 15.630 29.073 1.00 15.16 ? 205 VAL A CG2 1 ATOM 1546 N N . LEU A 1 206 ? 48.919 12.608 26.376 1.00 16.28 ? 206 LEU A N 1 ATOM 1547 C CA . LEU A 1 206 ? 48.582 11.279 25.856 1.00 15.44 ? 206 LEU A CA 1 ATOM 1548 C C . LEU A 1 206 ? 48.544 11.241 24.327 1.00 20.55 ? 206 LEU A C 1 ATOM 1549 O O . LEU A 1 206 ? 48.310 10.169 23.746 1.00 17.29 ? 206 LEU A O 1 ATOM 1550 C CB . LEU A 1 206 ? 47.283 10.742 26.443 1.00 16.77 ? 206 LEU A CB 1 ATOM 1551 C CG . LEU A 1 206 ? 47.330 10.263 27.904 1.00 13.66 ? 206 LEU A CG 1 ATOM 1552 C CD1 . LEU A 1 206 ? 45.920 9.956 28.402 1.00 16.36 ? 206 LEU A CD1 1 ATOM 1553 C CD2 . LEU A 1 206 ? 48.231 9.052 28.042 1.00 14.09 ? 206 LEU A CD2 1 ATOM 1554 N N . LEU A 1 207 ? 48.753 12.364 23.634 1.00 14.55 ? 207 LEU A N 1 ATOM 1555 C CA . LEU A 1 207 ? 48.781 12.382 22.174 1.00 15.83 ? 207 LEU A CA 1 ATOM 1556 C C . LEU A 1 207 ? 50.170 12.021 21.640 1.00 19.90 ? 207 LEU A C 1 ATOM 1557 O O . LEU A 1 207 ? 51.190 12.306 22.256 1.00 18.14 ? 207 LEU A O 1 ATOM 1558 C CB . LEU A 1 207 ? 48.397 13.770 21.651 1.00 15.84 ? 207 LEU A CB 1 ATOM 1559 C CG . LEU A 1 207 ? 47.054 14.305 22.127 1.00 17.94 ? 207 LEU A CG 1 ATOM 1560 C CD1 . LEU A 1 207 ? 46.939 15.799 21.934 1.00 19.68 ? 207 LEU A CD1 1 ATOM 1561 C CD2 . LEU A 1 207 ? 45.942 13.568 21.373 1.00 20.49 ? 207 LEU A CD2 1 ATOM 1562 N N . LYS A 1 208 ? 50.244 11.374 20.497 1.00 19.41 ? 208 LYS A N 1 ATOM 1563 C CA . LYS A 1 208 ? 51.512 11.001 19.862 1.00 13.65 ? 208 LYS A CA 1 ATOM 1564 C C . LYS A 1 208 ? 52.331 12.252 19.578 1.00 17.25 ? 208 LYS A C 1 ATOM 1565 O O . LYS A 1 208 ? 51.780 13.217 19.033 1.00 17.48 ? 208 LYS A O 1 ATOM 1566 C CB . LYS A 1 208 ? 51.204 10.311 18.522 1.00 20.93 ? 208 LYS A CB 1 ATOM 1567 C CG . LYS A 1 208 ? 52.379 10.195 17.567 1.00 22.68 ? 208 LYS A CG 1 ATOM 1568 C CD . LYS A 1 208 ? 51.883 9.997 16.138 1.00 53.72 ? 208 LYS A CD 1 ATOM 1569 C CE . LYS A 1 208 ? 50.511 10.627 15.954 1.00 78.82 ? 208 LYS A CE 1 ATOM 1570 N NZ . LYS A 1 208 ? 50.414 11.532 14.779 1.00 57.49 ? 208 LYS A NZ 1 ATOM 1571 N N . GLY A 1 209 ? 53.613 12.254 19.948 1.00 16.74 ? 209 GLY A N 1 ATOM 1572 C CA . GLY A 1 209 ? 54.413 13.455 19.679 1.00 16.09 ? 209 GLY A CA 1 ATOM 1573 C C . GLY A 1 209 ? 54.743 13.570 18.208 1.00 19.91 ? 209 GLY A C 1 ATOM 1574 O O . GLY A 1 209 ? 54.953 12.528 17.558 1.00 21.05 ? 209 GLY A O 1 ATOM 1575 N N . VAL A 1 210 ? 54.824 14.788 17.667 1.00 20.08 ? 210 VAL A N 1 ATOM 1576 C CA . VAL A 1 210 ? 55.141 14.933 16.243 1.00 22.06 ? 210 VAL A CA 1 ATOM 1577 C C . VAL A 1 210 ? 56.310 15.856 15.976 1.00 23.86 ? 210 VAL A C 1 ATOM 1578 O O . VAL A 1 210 ? 56.714 16.061 14.830 1.00 19.22 ? 210 VAL A O 1 ATOM 1579 C CB . VAL A 1 210 ? 53.901 15.392 15.441 1.00 16.33 ? 210 VAL A CB 1 ATOM 1580 C CG1 . VAL A 1 210 ? 52.907 14.229 15.482 1.00 20.99 ? 210 VAL A CG1 1 ATOM 1581 C CG2 . VAL A 1 210 ? 53.294 16.652 16.038 1.00 19.76 ? 210 VAL A CG2 1 ATOM 1582 N N . GLY A 1 211 ? 56.914 16.430 17.011 1.00 15.96 ? 211 GLY A N 1 ATOM 1583 C CA . GLY A 1 211 ? 58.023 17.357 16.762 1.00 13.69 ? 211 GLY A CA 1 ATOM 1584 C C . GLY A 1 211 ? 58.430 17.972 18.104 1.00 19.61 ? 211 GLY A C 1 ATOM 1585 O O . GLY A 1 211 ? 57.955 17.480 19.130 1.00 19.76 ? 211 GLY A O 1 ATOM 1586 N N . PHE A 1 212 ? 59.253 19.002 18.056 1.00 19.04 ? 212 PHE A N 1 ATOM 1587 C CA . PHE A 1 212 ? 59.778 19.671 19.240 1.00 17.83 ? 212 PHE A CA 1 ATOM 1588 C C . PHE A 1 212 ? 59.589 21.177 19.090 1.00 18.57 ? 212 PHE A C 1 ATOM 1589 O O . PHE A 1 212 ? 59.774 21.663 17.964 1.00 21.46 ? 212 PHE A O 1 ATOM 1590 C CB . PHE A 1 212 ? 61.265 19.362 19.409 1.00 18.21 ? 212 PHE A CB 1 ATOM 1591 C CG . PHE A 1 212 ? 61.503 17.903 19.791 1.00 20.23 ? 212 PHE A CG 1 ATOM 1592 C CD1 . PHE A 1 212 ? 61.644 16.948 18.801 1.00 21.80 ? 212 PHE A CD1 1 ATOM 1593 C CD2 . PHE A 1 212 ? 61.615 17.509 21.111 1.00 21.12 ? 212 PHE A CD2 1 ATOM 1594 C CE1 . PHE A 1 212 ? 61.954 15.636 19.099 1.00 18.14 ? 212 PHE A CE1 1 ATOM 1595 C CE2 . PHE A 1 212 ? 61.831 16.176 21.414 1.00 23.72 ? 212 PHE A CE2 1 ATOM 1596 C CZ . PHE A 1 212 ? 61.935 15.217 20.412 1.00 15.77 ? 212 PHE A CZ 1 ATOM 1597 N N . PRO A 1 213 ? 59.245 21.890 20.155 1.00 13.98 ? 213 PRO A N 1 ATOM 1598 C CA . PRO A 1 213 ? 59.047 23.335 20.033 1.00 12.82 ? 213 PRO A CA 1 ATOM 1599 C C . PRO A 1 213 ? 60.334 24.104 19.747 1.00 21.49 ? 213 PRO A C 1 ATOM 1600 O O . PRO A 1 213 ? 60.269 25.204 19.191 1.00 19.98 ? 213 PRO A O 1 ATOM 1601 C CB . PRO A 1 213 ? 58.461 23.740 21.386 1.00 17.48 ? 213 PRO A CB 1 ATOM 1602 C CG . PRO A 1 213 ? 58.957 22.677 22.326 1.00 17.27 ? 213 PRO A CG 1 ATOM 1603 C CD . PRO A 1 213 ? 59.023 21.404 21.521 1.00 16.22 ? 213 PRO A CD 1 ATOM 1604 N N . GLY A 1 214 ? 61.467 23.546 20.136 1.00 19.77 ? 214 GLY A N 1 ATOM 1605 C CA . GLY A 1 214 ? 62.794 24.105 19.905 1.00 18.11 ? 214 GLY A CA 1 ATOM 1606 C C . GLY A 1 214 ? 63.679 23.016 19.318 1.00 27.77 ? 214 GLY A C 1 ATOM 1607 O O . GLY A 1 214 ? 63.433 22.559 18.196 1.00 27.10 ? 214 GLY A O 1 ATOM 1608 N N . SER A 1 215 ? 64.726 22.629 20.033 1.00 26.79 ? 215 SER A N 1 ATOM 1609 C CA . SER A 1 215 ? 65.621 21.599 19.515 1.00 24.85 ? 215 SER A CA 1 ATOM 1610 C C . SER A 1 215 ? 65.205 20.220 20.011 1.00 22.81 ? 215 SER A C 1 ATOM 1611 O O . SER A 1 215 ? 64.418 20.109 20.950 1.00 26.50 ? 215 SER A O 1 ATOM 1612 C CB . SER A 1 215 ? 67.081 21.849 19.882 1.00 26.48 ? 215 SER A CB 1 ATOM 1613 O OG . SER A 1 215 ? 67.180 22.494 21.134 1.00 34.90 ? 215 SER A OG 1 ATOM 1614 N N . ALA A 1 216 ? 65.761 19.189 19.380 1.00 30.33 ? 216 ALA A N 1 ATOM 1615 C CA . ALA A 1 216 ? 65.305 17.821 19.609 1.00 43.92 ? 216 ALA A CA 1 ATOM 1616 C C . ALA A 1 216 ? 66.161 17.069 20.608 1.00 29.32 ? 216 ALA A C 1 ATOM 1617 O O . ALA A 1 216 ? 65.950 15.888 20.906 1.00 47.78 ? 216 ALA A O 1 ATOM 1618 C CB . ALA A 1 216 ? 65.281 17.056 18.288 1.00 26.92 ? 216 ALA A CB 1 ATOM 1619 N N . ASN A 1 217 ? 67.184 17.733 21.142 1.00 21.17 ? 217 ASN A N 1 ATOM 1620 C CA . ASN A 1 217 ? 68.078 16.939 21.999 1.00 52.39 ? 217 ASN A CA 1 ATOM 1621 C C . ASN A 1 217 ? 68.204 17.484 23.409 1.00 31.05 ? 217 ASN A C 1 ATOM 1622 O O . ASN A 1 217 ? 69.336 17.639 23.862 1.00 37.25 ? 217 ASN A O 1 ATOM 1623 C CB . ASN A 1 217 ? 69.484 17.023 21.361 1.00 70.11 ? 217 ASN A CB 1 ATOM 1624 C CG . ASN A 1 217 ? 69.728 18.476 20.959 1.00 88.94 ? 217 ASN A CG 1 ATOM 1625 O OD1 . ASN A 1 217 ? 69.416 19.392 21.725 1.00 55.78 ? 217 ASN A OD1 1 ATOM 1626 N ND2 . ASN A 1 217 ? 70.225 18.668 19.743 1.00 145.16 ? 217 ASN A ND2 1 ATOM 1627 N N . ASN A 1 218 ? 67.130 17.837 24.098 1.00 26.36 ? 218 ASN A N 1 ATOM 1628 C CA . ASN A 1 218 ? 67.306 18.395 25.438 1.00 20.25 ? 218 ASN A CA 1 ATOM 1629 C C . ASN A 1 218 ? 67.051 17.329 26.495 1.00 20.47 ? 218 ASN A C 1 ATOM 1630 O O . ASN A 1 218 ? 66.071 16.591 26.400 1.00 21.67 ? 218 ASN A O 1 ATOM 1631 C CB . ASN A 1 218 ? 66.297 19.536 25.671 1.00 20.29 ? 218 ASN A CB 1 ATOM 1632 C CG . ASN A 1 218 ? 66.450 20.643 24.641 1.00 26.70 ? 218 ASN A CG 1 ATOM 1633 O OD1 . ASN A 1 218 ? 65.485 21.052 23.994 1.00 29.59 ? 218 ASN A OD1 1 ATOM 1634 N ND2 . ASN A 1 218 ? 67.679 21.142 24.499 1.00 21.48 ? 218 ASN A ND2 1 ATOM 1635 N N . THR A 1 219 ? 67.883 17.303 27.531 1.00 17.87 ? 219 THR A N 1 ATOM 1636 C CA . THR A 1 219 ? 67.616 16.399 28.646 1.00 23.51 ? 219 THR A CA 1 ATOM 1637 C C . THR A 1 219 ? 66.260 16.709 29.275 1.00 19.92 ? 219 THR A C 1 ATOM 1638 O O . THR A 1 219 ? 65.894 17.874 29.431 1.00 20.12 ? 219 THR A O 1 ATOM 1639 C CB . THR A 1 219 ? 68.681 16.584 29.751 1.00 26.23 ? 219 THR A CB 1 ATOM 1640 O OG1 . THR A 1 219 ? 69.956 16.374 29.136 1.00 28.71 ? 219 THR A OG1 1 ATOM 1641 C CG2 . THR A 1 219 ? 68.502 15.537 30.835 1.00 26.40 ? 219 THR A CG2 1 ATOM 1642 N N . GLY A 1 220 ? 65.526 15.648 29.596 1.00 19.26 ? 220 GLY A N 1 ATOM 1643 C CA . GLY A 1 220 ? 64.251 15.761 30.275 1.00 15.31 ? 220 GLY A CA 1 ATOM 1644 C C . GLY A 1 220 ? 63.069 16.036 29.357 1.00 18.97 ? 220 GLY A C 1 ATOM 1645 O O . GLY A 1 220 ? 61.948 16.220 29.836 1.00 16.27 ? 220 GLY A O 1 ATOM 1646 N N . GLU A 1 221 ? 63.296 16.089 28.052 1.00 18.98 ? 221 GLU A N 1 ATOM 1647 C CA . GLU A 1 221 ? 62.251 16.462 27.093 1.00 21.88 ? 221 GLU A CA 1 ATOM 1648 C C . GLU A 1 221 ? 61.940 15.310 26.140 1.00 17.91 ? 221 GLU A C 1 ATOM 1649 O O . GLU A 1 221 ? 62.877 14.591 25.794 1.00 18.56 ? 221 GLU A O 1 ATOM 1650 C CB . GLU A 1 221 ? 62.740 17.639 26.229 1.00 15.71 ? 221 GLU A CB 1 ATOM 1651 C CG . GLU A 1 221 ? 61.628 18.249 25.378 1.00 18.32 ? 221 GLU A CG 1 ATOM 1652 C CD . GLU A 1 221 ? 62.076 19.421 24.528 1.00 28.11 ? 221 GLU A CD 1 ATOM 1653 O OE1 . GLU A 1 221 ? 63.262 19.824 24.583 1.00 24.22 ? 221 GLU A OE1 1 ATOM 1654 O OE2 . GLU A 1 221 ? 61.220 19.971 23.789 1.00 20.76 ? 221 GLU A OE2 1 ATOM 1655 N N . VAL A 1 222 ? 60.701 15.242 25.664 1.00 15.07 ? 222 VAL A N 1 ATOM 1656 C CA . VAL A 1 222 ? 60.382 14.236 24.648 1.00 17.12 ? 222 VAL A CA 1 ATOM 1657 C C . VAL A 1 222 ? 59.508 14.896 23.580 1.00 17.79 ? 222 VAL A C 1 ATOM 1658 O O . VAL A 1 222 ? 59.095 16.043 23.780 1.00 17.64 ? 222 VAL A O 1 ATOM 1659 C CB . VAL A 1 222 ? 59.652 13.008 25.206 1.00 23.65 ? 222 VAL A CB 1 ATOM 1660 C CG1 . VAL A 1 222 ? 60.578 12.085 25.997 1.00 17.52 ? 222 VAL A CG1 1 ATOM 1661 C CG2 . VAL A 1 222 ? 58.464 13.459 26.044 1.00 15.44 ? 222 VAL A CG2 1 ATOM 1662 N N . ALA A 1 223 ? 59.219 14.215 22.468 1.00 14.76 ? 223 ALA A N 1 ATOM 1663 C CA . ALA A 1 223 ? 58.445 14.900 21.419 1.00 13.97 ? 223 ALA A CA 1 ATOM 1664 C C . ALA A 1 223 ? 57.083 15.383 21.909 1.00 13.51 ? 223 ALA A C 1 ATOM 1665 O O . ALA A 1 223 ? 56.411 14.793 22.747 1.00 17.50 ? 223 ALA A O 1 ATOM 1666 C CB . ALA A 1 223 ? 58.279 13.967 20.209 1.00 14.96 ? 223 ALA A CB 1 ATOM 1667 N N . SER A 1 224 ? 56.645 16.500 21.302 1.00 16.72 ? 224 SER A N 1 ATOM 1668 C CA . SER A 1 224 ? 55.438 17.244 21.640 1.00 13.26 ? 224 SER A CA 1 ATOM 1669 C C . SER A 1 224 ? 54.381 17.003 20.546 1.00 18.04 ? 224 SER A C 1 ATOM 1670 O O . SER A 1 224 ? 54.790 16.956 19.374 1.00 14.72 ? 224 SER A O 1 ATOM 1671 C CB . SER A 1 224 ? 55.774 18.740 21.606 1.00 12.71 ? 224 SER A CB 1 ATOM 1672 O OG . SER A 1 224 ? 54.590 19.540 21.667 1.00 18.60 ? 224 SER A OG 1 ATOM 1673 N N . PRO A 1 225 ? 53.113 17.000 20.921 1.00 17.63 ? 225 PRO A N 1 ATOM 1674 C CA . PRO A 1 225 ? 52.049 16.846 19.913 1.00 16.69 ? 225 PRO A CA 1 ATOM 1675 C C . PRO A 1 225 ? 51.695 18.166 19.231 1.00 17.96 ? 225 PRO A C 1 ATOM 1676 O O . PRO A 1 225 ? 50.965 18.160 18.226 1.00 18.84 ? 225 PRO A O 1 ATOM 1677 C CB . PRO A 1 225 ? 50.873 16.369 20.770 1.00 20.38 ? 225 PRO A CB 1 ATOM 1678 C CG . PRO A 1 225 ? 51.063 17.084 22.070 1.00 16.60 ? 225 PRO A CG 1 ATOM 1679 C CD . PRO A 1 225 ? 52.556 17.140 22.271 1.00 17.27 ? 225 PRO A CD 1 ATOM 1680 N N . LEU A 1 226 ? 52.102 19.284 19.822 1.00 16.17 ? 226 LEU A N 1 ATOM 1681 C CA . LEU A 1 226 ? 51.740 20.624 19.335 1.00 14.98 ? 226 LEU A CA 1 ATOM 1682 C C . LEU A 1 226 ? 52.970 21.531 19.313 1.00 14.34 ? 226 LEU A C 1 ATOM 1683 O O . LEU A 1 226 ? 53.002 22.579 19.971 1.00 16.13 ? 226 LEU A O 1 ATOM 1684 C CB . LEU A 1 226 ? 50.665 21.250 20.234 1.00 19.49 ? 226 LEU A CB 1 ATOM 1685 C CG . LEU A 1 226 ? 49.351 20.443 20.281 1.00 26.38 ? 226 LEU A CG 1 ATOM 1686 C CD1 . LEU A 1 226 ? 48.519 20.794 21.506 1.00 20.28 ? 226 LEU A CD1 1 ATOM 1687 C CD2 . LEU A 1 226 ? 48.544 20.675 19.015 1.00 18.09 ? 226 LEU A CD2 1 ATOM 1688 N N . PRO A 1 227 ? 53.993 21.151 18.566 1.00 17.43 ? 227 PRO A N 1 ATOM 1689 C CA . PRO A 1 227 ? 55.298 21.825 18.591 1.00 14.37 ? 227 PRO A CA 1 ATOM 1690 C C . PRO A 1 227 ? 55.353 23.172 17.878 1.00 18.41 ? 227 PRO A C 1 ATOM 1691 O O . PRO A 1 227 ? 56.283 23.979 17.996 1.00 20.68 ? 227 PRO A O 1 ATOM 1692 C CB . PRO A 1 227 ? 56.201 20.800 17.907 1.00 17.43 ? 227 PRO A CB 1 ATOM 1693 C CG . PRO A 1 227 ? 55.286 20.163 16.894 1.00 20.60 ? 227 PRO A CG 1 ATOM 1694 C CD . PRO A 1 227 ? 53.943 20.044 17.582 1.00 14.87 ? 227 PRO A CD 1 ATOM 1695 N N . LEU A 1 228 ? 54.324 23.515 17.087 1.00 20.65 ? 228 LEU A N 1 ATOM 1696 C CA . LEU A 1 228 ? 54.370 24.754 16.322 1.00 18.70 ? 228 LEU A CA 1 ATOM 1697 C C . LEU A 1 228 ? 54.429 26.010 17.180 1.00 22.38 ? 228 LEU A C 1 ATOM 1698 O O . LEU A 1 228 ? 53.539 26.264 17.985 1.00 17.16 ? 228 LEU A O 1 ATOM 1699 C CB . LEU A 1 228 ? 53.144 24.880 15.400 1.00 13.16 ? 228 LEU A CB 1 ATOM 1700 C CG . LEU A 1 228 ? 53.088 26.185 14.598 1.00 18.77 ? 228 LEU A CG 1 ATOM 1701 C CD1 . LEU A 1 228 ? 54.267 26.260 13.633 1.00 17.91 ? 228 LEU A CD1 1 ATOM 1702 C CD2 . LEU A 1 228 ? 51.771 26.242 13.811 1.00 14.76 ? 228 LEU A CD2 1 ATOM 1703 N N . GLY A 1 229 ? 55.388 26.880 16.885 1.00 18.51 ? 229 GLY A N 1 ATOM 1704 C CA . GLY A 1 229 ? 55.429 28.186 17.521 1.00 18.84 ? 229 GLY A CA 1 ATOM 1705 C C . GLY A 1 229 ? 55.731 29.281 16.521 1.00 22.80 ? 229 GLY A C 1 ATOM 1706 O O . GLY A 1 229 ? 56.176 29.027 15.407 1.00 20.61 ? 229 GLY A O 1 ATOM 1707 N N . SER A 1 230 ? 55.405 30.512 16.890 1.00 17.80 ? 230 SER A N 1 ATOM 1708 C CA . SER A 1 230 ? 55.748 31.629 15.989 1.00 20.94 ? 230 SER A CA 1 ATOM 1709 C C . SER A 1 230 ? 55.928 32.896 16.830 1.00 15.79 ? 230 SER A C 1 ATOM 1710 O O . SER A 1 230 ? 55.143 33.093 17.762 1.00 19.98 ? 230 SER A O 1 ATOM 1711 C CB . SER A 1 230 ? 54.631 31.818 14.959 1.00 25.98 ? 230 SER A CB 1 ATOM 1712 O OG . SER A 1 230 ? 55.078 32.715 13.951 1.00 24.49 ? 230 SER A OG 1 ATOM 1713 N N . GLY A 1 231 ? 56.971 33.673 16.544 1.00 22.92 ? 231 GLY A N 1 ATOM 1714 C CA . GLY A 1 231 ? 57.232 34.878 17.336 1.00 26.76 ? 231 GLY A CA 1 ATOM 1715 C C . GLY A 1 231 ? 57.416 34.483 18.795 1.00 19.01 ? 231 GLY A C 1 ATOM 1716 O O . GLY A 1 231 ? 58.220 33.596 19.040 1.00 25.18 ? 231 GLY A O 1 ATOM 1717 N N . SER A 1 232 ? 56.641 35.060 19.720 1.00 18.66 ? 232 SER A N 1 ATOM 1718 C CA . SER A 1 232 ? 56.847 34.663 21.105 1.00 23.78 ? 232 SER A CA 1 ATOM 1719 C C . SER A 1 232 ? 55.833 33.602 21.551 1.00 28.78 ? 232 SER A C 1 ATOM 1720 O O . SER A 1 232 ? 55.923 33.197 22.717 1.00 23.84 ? 232 SER A O 1 ATOM 1721 C CB A SER A 1 232 ? 56.883 35.804 22.103 0.50 38.97 ? 232 SER A CB 1 ATOM 1722 C CB B SER A 1 232 ? 56.682 35.903 21.998 0.50 35.69 ? 232 SER A CB 1 ATOM 1723 O OG A SER A 1 232 ? 56.549 37.073 21.600 0.50 29.16 ? 232 SER A OG 1 ATOM 1724 O OG B SER A 1 232 ? 55.327 36.325 21.941 0.50 16.61 ? 232 SER A OG 1 ATOM 1725 N N . ASP A 1 233 ? 54.960 33.159 20.660 1.00 20.69 ? 233 ASP A N 1 ATOM 1726 C CA . ASP A 1 233 ? 53.995 32.084 20.942 1.00 19.48 ? 233 ASP A CA 1 ATOM 1727 C C . ASP A 1 233 ? 54.666 30.722 20.788 1.00 21.79 ? 233 ASP A C 1 ATOM 1728 O O . ASP A 1 233 ? 54.585 30.060 19.755 1.00 20.24 ? 233 ASP A O 1 ATOM 1729 C CB . ASP A 1 233 ? 52.774 32.142 19.998 1.00 16.39 ? 233 ASP A CB 1 ATOM 1730 C CG . ASP A 1 233 ? 51.893 33.345 20.271 1.00 26.98 ? 233 ASP A CG 1 ATOM 1731 O OD1 . ASP A 1 233 ? 52.058 34.054 21.289 1.00 19.64 ? 233 ASP A OD1 1 ATOM 1732 O OD2 . ASP A 1 233 ? 50.981 33.594 19.449 1.00 22.31 ? 233 ASP A OD2 1 ATOM 1733 N N . THR A 1 234 ? 55.446 30.349 21.783 1.00 19.92 ? 234 THR A N 1 ATOM 1734 C CA . THR A 1 234 ? 56.250 29.132 21.737 1.00 15.44 ? 234 THR A CA 1 ATOM 1735 C C . THR A 1 234 ? 55.346 27.891 21.727 1.00 13.05 ? 234 THR A C 1 ATOM 1736 O O . THR A 1 234 ? 54.290 27.903 22.365 1.00 16.81 ? 234 THR A O 1 ATOM 1737 C CB . THR A 1 234 ? 57.157 29.071 22.994 1.00 20.39 ? 234 THR A CB 1 ATOM 1738 O OG1 . THR A 1 234 ? 57.950 30.279 23.029 1.00 20.01 ? 234 THR A OG1 1 ATOM 1739 C CG2 . THR A 1 234 ? 58.120 27.895 22.921 1.00 17.09 ? 234 THR A CG2 1 ATOM 1740 N N . GLY A 1 235 ? 55.786 26.899 20.948 1.00 15.22 ? 235 GLY A N 1 ATOM 1741 C CA . GLY A 1 235 ? 55.035 25.670 20.874 1.00 16.55 ? 235 GLY A CA 1 ATOM 1742 C C . GLY A 1 235 ? 55.028 24.890 22.190 1.00 19.38 ? 235 GLY A C 1 ATOM 1743 O O . GLY A 1 235 ? 55.815 25.148 23.094 1.00 18.96 ? 235 GLY A O 1 ATOM 1744 N N . GLU A 1 236 ? 54.113 23.935 22.312 1.00 15.98 ? 236 GLU A N 1 ATOM 1745 C CA . GLU A 1 236 ? 54.000 23.082 23.471 1.00 15.55 ? 236 GLU A CA 1 ATOM 1746 C C . GLU A 1 236 ? 55.239 22.205 23.670 1.00 17.80 ? 236 GLU A C 1 ATOM 1747 O O . GLU A 1 236 ? 55.779 21.626 22.725 1.00 14.82 ? 236 GLU A O 1 ATOM 1748 C CB . GLU A 1 236 ? 52.768 22.184 23.325 1.00 13.55 ? 236 GLU A CB 1 ATOM 1749 C CG . GLU A 1 236 ? 52.668 21.178 24.456 1.00 15.67 ? 236 GLU A CG 1 ATOM 1750 C CD . GLU A 1 236 ? 51.288 20.548 24.502 1.00 16.60 ? 236 GLU A CD 1 ATOM 1751 O OE1 . GLU A 1 236 ? 51.173 19.303 24.446 1.00 15.74 ? 236 GLU A OE1 1 ATOM 1752 O OE2 . GLU A 1 236 ? 50.316 21.330 24.604 1.00 17.58 ? 236 GLU A OE2 1 ATOM 1753 N N . MET A 1 237 ? 55.695 22.108 24.921 1.00 14.74 ? 237 MET A N 1 ATOM 1754 C CA . MET A 1 237 ? 56.782 21.218 25.316 1.00 15.03 ? 237 MET A CA 1 ATOM 1755 C C . MET A 1 237 ? 56.223 20.016 26.099 1.00 16.70 ? 237 MET A C 1 ATOM 1756 O O . MET A 1 237 ? 55.280 20.237 26.881 1.00 15.15 ? 237 MET A O 1 ATOM 1757 C CB . MET A 1 237 ? 57.748 21.955 26.279 1.00 13.43 ? 237 MET A CB 1 ATOM 1758 C CG . MET A 1 237 ? 58.882 21.084 26.782 1.00 14.90 ? 237 MET A CG 1 ATOM 1759 S SD . MET A 1 237 ? 60.242 22.009 27.550 1.00 18.47 ? 237 MET A SD 1 ATOM 1760 C CE . MET A 1 237 ? 61.000 22.733 26.096 1.00 21.55 ? 237 MET A CE 1 ATOM 1761 N N . ARG A 1 238 ? 56.861 18.855 25.953 1.00 14.35 ? 238 ARG A N 1 ATOM 1762 C CA . ARG A 1 238 ? 56.517 17.687 26.763 1.00 15.97 ? 238 ARG A CA 1 ATOM 1763 C C . ARG A 1 238 ? 57.698 17.214 27.620 1.00 18.26 ? 238 ARG A C 1 ATOM 1764 O O . ARG A 1 238 ? 58.788 16.952 27.111 1.00 16.84 ? 238 ARG A O 1 ATOM 1765 C CB . ARG A 1 238 ? 56.036 16.518 25.887 1.00 14.22 ? 238 ARG A CB 1 ATOM 1766 C CG . ARG A 1 238 ? 55.518 15.329 26.697 1.00 14.90 ? 238 ARG A CG 1 ATOM 1767 C CD . ARG A 1 238 ? 55.013 14.234 25.741 1.00 14.38 ? 238 ARG A CD 1 ATOM 1768 N NE . ARG A 1 238 ? 53.721 14.641 25.159 1.00 13.16 ? 238 ARG A NE 1 ATOM 1769 C CZ . ARG A 1 238 ? 53.109 13.882 24.235 1.00 15.75 ? 238 ARG A CZ 1 ATOM 1770 N NH1 . ARG A 1 238 ? 53.676 12.750 23.818 1.00 14.91 ? 238 ARG A NH1 1 ATOM 1771 N NH2 . ARG A 1 238 ? 51.935 14.236 23.738 1.00 15.85 ? 238 ARG A NH2 1 ATOM 1772 N N . LEU A 1 239 ? 57.470 17.095 28.936 1.00 13.71 ? 239 LEU A N 1 ATOM 1773 C CA . LEU A 1 239 ? 58.557 16.631 29.811 1.00 17.20 ? 239 LEU A CA 1 ATOM 1774 C C . LEU A 1 239 ? 58.614 15.097 29.775 1.00 18.00 ? 239 LEU A C 1 ATOM 1775 O O . LEU A 1 239 ? 57.561 14.440 29.813 1.00 16.95 ? 239 LEU A O 1 ATOM 1776 C CB . LEU A 1 239 ? 58.285 17.071 31.253 1.00 19.04 ? 239 LEU A CB 1 ATOM 1777 C CG . LEU A 1 239 ? 58.234 18.569 31.546 1.00 13.50 ? 239 LEU A CG 1 ATOM 1778 C CD1 . LEU A 1 239 ? 58.073 18.838 33.029 1.00 16.78 ? 239 LEU A CD1 1 ATOM 1779 C CD2 . LEU A 1 239 ? 59.455 19.301 31.005 1.00 16.68 ? 239 LEU A CD2 1 ATOM 1780 N N . GLN A 1 240 ? 59.800 14.511 29.755 1.00 17.03 ? 240 GLN A N 1 ATOM 1781 C CA . GLN A 1 240 ? 59.909 13.044 29.873 1.00 12.35 ? 240 GLN A CA 1 ATOM 1782 C C . GLN A 1 240 ? 59.159 12.541 31.085 1.00 17.44 ? 240 GLN A C 1 ATOM 1783 O O . GLN A 1 240 ? 58.651 11.408 31.041 1.00 18.32 ? 240 GLN A O 1 ATOM 1784 C CB . GLN A 1 240 ? 61.400 12.658 30.030 1.00 14.93 ? 240 GLN A CB 1 ATOM 1785 C CG . GLN A 1 240 ? 61.657 11.157 29.926 1.00 20.31 ? 240 GLN A CG 1 ATOM 1786 C CD . GLN A 1 240 ? 61.557 10.323 31.175 1.00 24.78 ? 240 GLN A CD 1 ATOM 1787 O OE1 . GLN A 1 240 ? 61.282 9.115 31.169 1.00 19.01 ? 240 GLN A OE1 1 ATOM 1788 N NE2 . GLN A 1 240 ? 61.612 11.030 32.319 1.00 17.54 ? 240 GLN A NE2 1 ATOM 1789 N N . SER A 1 241 ? 59.214 13.235 32.217 1.00 13.64 ? 241 SER A N 1 ATOM 1790 C CA . SER A 1 241 ? 58.602 12.700 33.431 1.00 14.04 ? 241 SER A CA 1 ATOM 1791 C C . SER A 1 241 ? 57.085 12.622 33.328 1.00 15.62 ? 241 SER A C 1 ATOM 1792 O O . SER A 1 241 ? 56.463 11.651 33.794 1.00 14.85 ? 241 SER A O 1 ATOM 1793 C CB . SER A 1 241 ? 58.970 13.615 34.621 1.00 14.12 ? 241 SER A CB 1 ATOM 1794 O OG . SER A 1 241 ? 58.951 14.971 34.201 1.00 16.24 ? 241 SER A OG 1 ATOM 1795 N N . ASP A 1 242 ? 56.463 13.658 32.741 1.00 15.90 ? 242 ASP A N 1 ATOM 1796 C CA . ASP A 1 242 ? 55.010 13.690 32.535 1.00 17.30 ? 242 ASP A CA 1 ATOM 1797 C C . ASP A 1 242 ? 54.621 12.560 31.564 1.00 22.57 ? 242 ASP A C 1 ATOM 1798 O O . ASP A 1 242 ? 53.718 11.775 31.864 1.00 18.43 ? 242 ASP A O 1 ATOM 1799 C CB . ASP A 1 242 ? 54.551 15.043 31.962 1.00 14.42 ? 242 ASP A CB 1 ATOM 1800 C CG . ASP A 1 242 ? 54.549 16.158 32.991 1.00 15.78 ? 242 ASP A CG 1 ATOM 1801 O OD1 . ASP A 1 242 ? 54.517 17.355 32.622 1.00 16.12 ? 242 ASP A OD1 1 ATOM 1802 O OD2 . ASP A 1 242 ? 54.615 15.810 34.199 1.00 15.30 ? 242 ASP A OD2 1 ATOM 1803 N N . PHE A 1 243 ? 55.375 12.446 30.465 1.00 14.17 ? 243 PHE A N 1 ATOM 1804 C CA . PHE A 1 243 ? 55.140 11.327 29.536 1.00 17.58 ? 243 PHE A CA 1 ATOM 1805 C C . PHE A 1 243 ? 55.285 9.979 30.221 1.00 15.27 ? 243 PHE A C 1 ATOM 1806 O O . PHE A 1 243 ? 54.441 9.091 30.051 1.00 15.44 ? 243 PHE A O 1 ATOM 1807 C CB . PHE A 1 243 ? 56.146 11.441 28.380 1.00 17.08 ? 243 PHE A CB 1 ATOM 1808 C CG . PHE A 1 243 ? 56.067 10.281 27.397 1.00 15.32 ? 243 PHE A CG 1 ATOM 1809 C CD1 . PHE A 1 243 ? 56.987 9.253 27.445 1.00 19.45 ? 243 PHE A CD1 1 ATOM 1810 C CD2 . PHE A 1 243 ? 55.056 10.262 26.442 1.00 15.02 ? 243 PHE A CD2 1 ATOM 1811 C CE1 . PHE A 1 243 ? 56.949 8.193 26.547 1.00 21.31 ? 243 PHE A CE1 1 ATOM 1812 C CE2 . PHE A 1 243 ? 55.039 9.232 25.519 1.00 20.68 ? 243 PHE A CE2 1 ATOM 1813 C CZ . PHE A 1 243 ? 55.976 8.213 25.551 1.00 22.37 ? 243 PHE A CZ 1 ATOM 1814 N N . ALA A 1 244 ? 56.350 9.861 31.046 1.00 14.23 ? 244 ALA A N 1 ATOM 1815 C CA . ALA A 1 244 ? 56.572 8.567 31.702 1.00 14.75 ? 244 ALA A CA 1 ATOM 1816 C C . ALA A 1 244 ? 55.436 8.250 32.652 1.00 18.14 ? 244 ALA A C 1 ATOM 1817 O O . ALA A 1 244 ? 54.961 7.114 32.757 1.00 14.81 ? 244 ALA A O 1 ATOM 1818 C CB . ALA A 1 244 ? 57.911 8.554 32.426 1.00 14.71 ? 244 ALA A CB 1 ATOM 1819 N N . LEU A 1 245 ? 55.022 9.242 33.427 1.00 14.50 ? 245 LEU A N 1 ATOM 1820 C CA . LEU A 1 245 ? 53.941 9.019 34.379 1.00 14.50 ? 245 LEU A CA 1 ATOM 1821 C C . LEU A 1 245 ? 52.647 8.631 33.668 1.00 15.77 ? 245 LEU A C 1 ATOM 1822 O O . LEU A 1 245 ? 51.846 7.842 34.169 1.00 15.82 ? 245 LEU A O 1 ATOM 1823 C CB . LEU A 1 245 ? 53.740 10.244 35.269 1.00 14.13 ? 245 LEU A CB 1 ATOM 1824 C CG . LEU A 1 245 ? 54.843 10.410 36.321 1.00 15.61 ? 245 LEU A CG 1 ATOM 1825 C CD1 . LEU A 1 245 ? 54.928 11.849 36.810 1.00 17.11 ? 245 LEU A CD1 1 ATOM 1826 C CD2 . LEU A 1 245 ? 54.676 9.441 37.476 1.00 14.02 ? 245 LEU A CD2 1 ATOM 1827 N N . ALA A 1 246 ? 52.416 9.215 32.496 1.00 15.30 ? 246 ALA A N 1 ATOM 1828 C CA . ALA A 1 246 ? 51.155 8.930 31.788 1.00 17.89 ? 246 ALA A CA 1 ATOM 1829 C C . ALA A 1 246 ? 51.099 7.504 31.264 1.00 17.39 ? 246 ALA A C 1 ATOM 1830 O O . ALA A 1 246 ? 50.003 7.000 31.002 1.00 16.26 ? 246 ALA A O 1 ATOM 1831 C CB . ALA A 1 246 ? 50.994 9.963 30.673 1.00 14.24 ? 246 ALA A CB 1 ATOM 1832 N N . HIS A 1 247 ? 52.253 6.862 31.083 1.00 12.87 ? 247 HIS A N 1 ATOM 1833 C CA . HIS A 1 247 ? 52.284 5.510 30.525 1.00 12.26 ? 247 HIS A CA 1 ATOM 1834 C C . HIS A 1 247 ? 52.704 4.446 31.527 1.00 19.08 ? 247 HIS A C 1 ATOM 1835 O O . HIS A 1 247 ? 52.499 3.258 31.282 1.00 18.45 ? 247 HIS A O 1 ATOM 1836 C CB . HIS A 1 247 ? 53.214 5.446 29.300 1.00 17.22 ? 247 HIS A CB 1 ATOM 1837 C CG . HIS A 1 247 ? 52.705 6.382 28.230 1.00 15.20 ? 247 HIS A CG 1 ATOM 1838 N ND1 . HIS A 1 247 ? 51.459 6.158 27.670 1.00 16.67 ? 247 HIS A ND1 1 ATOM 1839 C CD2 . HIS A 1 247 ? 53.196 7.482 27.654 1.00 14.51 ? 247 HIS A CD2 1 ATOM 1840 C CE1 . HIS A 1 247 ? 51.213 7.114 26.778 1.00 16.56 ? 247 HIS A CE1 1 ATOM 1841 N NE2 . HIS A 1 247 ? 52.251 7.933 26.755 1.00 17.62 ? 247 HIS A NE2 1 ATOM 1842 N N . ASP A 1 248 ? 53.289 4.781 32.671 1.00 14.12 ? 248 ASP A N 1 ATOM 1843 C CA . ASP A 1 248 ? 53.751 3.700 33.575 1.00 13.27 ? 248 ASP A CA 1 ATOM 1844 C C . ASP A 1 248 ? 52.553 2.996 34.198 1.00 15.15 ? 248 ASP A C 1 ATOM 1845 O O . ASP A 1 248 ? 51.548 3.656 34.513 1.00 18.04 ? 248 ASP A O 1 ATOM 1846 C CB . ASP A 1 248 ? 54.541 4.392 34.702 1.00 19.65 ? 248 ASP A CB 1 ATOM 1847 C CG . ASP A 1 248 ? 55.270 3.388 35.587 1.00 15.02 ? 248 ASP A CG 1 ATOM 1848 O OD1 . ASP A 1 248 ? 54.620 2.859 36.511 1.00 16.20 ? 248 ASP A OD1 1 ATOM 1849 O OD2 . ASP A 1 248 ? 56.485 3.170 35.362 1.00 16.50 ? 248 ASP A OD2 1 ATOM 1850 N N . PRO A 1 249 ? 52.626 1.687 34.421 1.00 15.98 ? 249 PRO A N 1 ATOM 1851 C CA . PRO A 1 249 ? 51.493 0.947 34.982 1.00 14.56 ? 249 PRO A CA 1 ATOM 1852 C C . PRO A 1 249 ? 51.059 1.453 36.339 1.00 20.68 ? 249 PRO A C 1 ATOM 1853 O O . PRO A 1 249 ? 49.888 1.353 36.709 1.00 17.65 ? 249 PRO A O 1 ATOM 1854 C CB . PRO A 1 249 ? 52.015 -0.498 35.117 1.00 17.65 ? 249 PRO A CB 1 ATOM 1855 C CG . PRO A 1 249 ? 53.005 -0.566 33.989 1.00 14.81 ? 249 PRO A CG 1 ATOM 1856 C CD . PRO A 1 249 ? 53.732 0.775 34.034 1.00 18.97 ? 249 PRO A CD 1 ATOM 1857 N N . ARG A 1 250 ? 51.983 2.033 37.112 1.00 15.22 ? 250 ARG A N 1 ATOM 1858 C CA . ARG A 1 250 ? 51.571 2.526 38.422 1.00 14.93 ? 250 ARG A CA 1 ATOM 1859 C C . ARG A 1 250 ? 50.688 3.765 38.390 1.00 20.38 ? 250 ARG A C 1 ATOM 1860 O O . ARG A 1 250 ? 49.962 4.086 39.338 1.00 17.45 ? 250 ARG A O 1 ATOM 1861 C CB . ARG A 1 250 ? 52.854 2.898 39.213 1.00 12.24 ? 250 ARG A CB 1 ATOM 1862 C CG . ARG A 1 250 ? 53.637 1.642 39.573 1.00 13.43 ? 250 ARG A CG 1 ATOM 1863 C CD . ARG A 1 250 ? 55.039 2.006 40.034 1.00 16.60 ? 250 ARG A CD 1 ATOM 1864 N NE . ARG A 1 250 ? 55.923 2.295 38.905 1.00 16.40 ? 250 ARG A NE 1 ATOM 1865 C CZ . ARG A 1 250 ? 57.242 2.381 39.000 1.00 16.88 ? 250 ARG A CZ 1 ATOM 1866 N NH1 . ARG A 1 250 ? 57.845 2.204 40.190 1.00 13.89 ? 250 ARG A NH1 1 ATOM 1867 N NH2 . ARG A 1 250 ? 57.921 2.629 37.890 1.00 12.88 ? 250 ARG A NH2 1 ATOM 1868 N N . THR A 1 251 ? 50.829 4.550 37.325 1.00 14.45 ? 251 THR A N 1 ATOM 1869 C CA . THR A 1 251 ? 50.171 5.850 37.333 1.00 18.39 ? 251 THR A CA 1 ATOM 1870 C C . THR A 1 251 ? 49.330 6.111 36.091 1.00 19.92 ? 251 THR A C 1 ATOM 1871 O O . THR A 1 251 ? 48.645 7.148 36.047 1.00 17.06 ? 251 THR A O 1 ATOM 1872 C CB . THR A 1 251 ? 51.262 6.948 37.403 1.00 11.25 ? 251 THR A CB 1 ATOM 1873 O OG1 . THR A 1 251 ? 52.316 6.644 36.495 1.00 13.43 ? 251 THR A OG1 1 ATOM 1874 C CG2 . THR A 1 251 ? 51.845 7.000 38.821 1.00 15.06 ? 251 THR A CG2 1 ATOM 1875 N N . ALA A 1 252 ? 49.366 5.248 35.085 1.00 15.35 ? 252 ALA A N 1 ATOM 1876 C CA . ALA A 1 252 ? 48.617 5.477 33.853 1.00 17.12 ? 252 ALA A CA 1 ATOM 1877 C C . ALA A 1 252 ? 47.127 5.675 34.064 1.00 15.45 ? 252 ALA A C 1 ATOM 1878 O O . ALA A 1 252 ? 46.510 6.556 33.456 1.00 15.49 ? 252 ALA A O 1 ATOM 1879 C CB . ALA A 1 252 ? 48.853 4.368 32.842 1.00 17.52 ? 252 ALA A CB 1 ATOM 1880 N N . CYS A 1 253 ? 46.465 4.850 34.883 1.00 13.48 ? 253 CYS A N 1 ATOM 1881 C CA . CYS A 1 253 ? 45.021 5.057 35.022 1.00 14.49 ? 253 CYS A CA 1 ATOM 1882 C C . CYS A 1 253 ? 44.682 6.311 35.818 1.00 20.99 ? 253 CYS A C 1 ATOM 1883 O O . CYS A 1 253 ? 43.684 6.996 35.551 1.00 17.86 ? 253 CYS A O 1 ATOM 1884 C CB . CYS A 1 253 ? 44.367 3.817 35.662 1.00 21.59 ? 253 CYS A CB 1 ATOM 1885 S SG . CYS A 1 253 ? 44.372 2.343 34.576 1.00 19.16 ? 253 CYS A SG 1 ATOM 1886 N N . ILE A 1 254 ? 45.525 6.643 36.803 1.00 13.68 ? 254 ILE A N 1 ATOM 1887 C CA . ILE A 1 254 ? 45.351 7.904 37.513 1.00 13.84 ? 254 ILE A CA 1 ATOM 1888 C C . ILE A 1 254 ? 45.496 9.096 36.572 1.00 17.12 ? 254 ILE A C 1 ATOM 1889 O O . ILE A 1 254 ? 44.676 10.030 36.605 1.00 16.36 ? 254 ILE A O 1 ATOM 1890 C CB . ILE A 1 254 ? 46.381 8.003 38.669 1.00 15.79 ? 254 ILE A CB 1 ATOM 1891 C CG1 . ILE A 1 254 ? 46.165 6.880 39.699 1.00 14.43 ? 254 ILE A CG1 1 ATOM 1892 C CG2 . ILE A 1 254 ? 46.265 9.381 39.315 1.00 16.27 ? 254 ILE A CG2 1 ATOM 1893 C CD1 . ILE A 1 254 ? 47.357 6.570 40.571 1.00 17.83 ? 254 ILE A CD1 1 ATOM 1894 N N . TRP A 1 255 ? 46.529 9.042 35.718 1.00 13.34 ? 255 TRP A N 1 ATOM 1895 C CA . TRP A 1 255 ? 46.722 10.133 34.754 1.00 10.39 ? 255 TRP A CA 1 ATOM 1896 C C . TRP A 1 255 ? 45.467 10.267 33.887 1.00 18.12 ? 255 TRP A C 1 ATOM 1897 O O . TRP A 1 255 ? 44.907 11.350 33.711 1.00 16.55 ? 255 TRP A O 1 ATOM 1898 C CB . TRP A 1 255 ? 47.932 9.836 33.854 1.00 12.51 ? 255 TRP A CB 1 ATOM 1899 C CG . TRP A 1 255 ? 48.283 10.999 32.984 1.00 16.76 ? 255 TRP A CG 1 ATOM 1900 C CD1 . TRP A 1 255 ? 47.756 11.300 31.757 1.00 12.73 ? 255 TRP A CD1 1 ATOM 1901 C CD2 . TRP A 1 255 ? 49.264 12.011 33.257 1.00 15.37 ? 255 TRP A CD2 1 ATOM 1902 N NE1 . TRP A 1 255 ? 48.317 12.451 31.267 1.00 16.49 ? 255 TRP A NE1 1 ATOM 1903 C CE2 . TRP A 1 255 ? 49.244 12.910 32.174 1.00 13.87 ? 255 TRP A CE2 1 ATOM 1904 C CE3 . TRP A 1 255 ? 50.117 12.243 34.345 1.00 13.84 ? 255 TRP A CE3 1 ATOM 1905 C CZ2 . TRP A 1 255 ? 50.065 14.046 32.112 1.00 17.86 ? 255 TRP A CZ2 1 ATOM 1906 C CZ3 . TRP A 1 255 ? 50.915 13.366 34.272 1.00 14.56 ? 255 TRP A CZ3 1 ATOM 1907 C CH2 . TRP A 1 255 ? 50.893 14.247 33.190 1.00 15.20 ? 255 TRP A CH2 1 ATOM 1908 N N . GLN A 1 256 ? 45.057 9.142 33.278 1.00 15.10 ? 256 GLN A N 1 ATOM 1909 C CA . GLN A 1 256 ? 43.879 9.236 32.392 1.00 12.66 ? 256 GLN A CA 1 ATOM 1910 C C . GLN A 1 256 ? 42.652 9.686 33.144 1.00 13.48 ? 256 GLN A C 1 ATOM 1911 O O . GLN A 1 256 ? 41.763 10.324 32.563 1.00 17.62 ? 256 GLN A O 1 ATOM 1912 C CB . GLN A 1 256 ? 43.616 7.884 31.713 1.00 14.42 ? 256 GLN A CB 1 ATOM 1913 C CG . GLN A 1 256 ? 42.476 7.921 30.688 1.00 11.72 ? 256 GLN A CG 1 ATOM 1914 C CD . GLN A 1 256 ? 42.275 6.548 30.057 1.00 12.53 ? 256 GLN A CD 1 ATOM 1915 O OE1 . GLN A 1 256 ? 43.125 6.082 29.280 1.00 17.97 ? 256 GLN A OE1 1 ATOM 1916 N NE2 . GLN A 1 256 ? 41.158 5.925 30.426 1.00 16.32 ? 256 GLN A NE2 1 ATOM 1917 N N . GLY A 1 257 ? 42.500 9.277 34.409 1.00 15.20 ? 257 GLY A N 1 ATOM 1918 C CA . GLY A 1 257 ? 41.326 9.570 35.208 1.00 15.36 ? 257 GLY A CA 1 ATOM 1919 C C . GLY A 1 257 ? 41.047 11.060 35.385 1.00 15.80 ? 257 GLY A C 1 ATOM 1920 O O . GLY A 1 257 ? 39.967 11.434 35.859 1.00 16.66 ? 257 GLY A O 1 ATOM 1921 N N . PHE A 1 258 ? 42.035 11.916 35.103 1.00 15.24 ? 258 PHE A N 1 ATOM 1922 C CA . PHE A 1 258 ? 41.784 13.346 35.233 1.00 12.64 ? 258 PHE A CA 1 ATOM 1923 C C . PHE A 1 258 ? 41.332 13.911 33.886 1.00 16.31 ? 258 PHE A C 1 ATOM 1924 O O . PHE A 1 258 ? 40.818 15.031 33.901 1.00 17.17 ? 258 PHE A O 1 ATOM 1925 C CB . PHE A 1 258 ? 42.976 14.131 35.774 1.00 14.31 ? 258 PHE A CB 1 ATOM 1926 C CG . PHE A 1 258 ? 43.256 13.801 37.242 1.00 16.46 ? 258 PHE A CG 1 ATOM 1927 C CD1 . PHE A 1 258 ? 44.534 13.425 37.635 1.00 15.48 ? 258 PHE A CD1 1 ATOM 1928 C CD2 . PHE A 1 258 ? 42.256 13.859 38.192 1.00 14.52 ? 258 PHE A CD2 1 ATOM 1929 C CE1 . PHE A 1 258 ? 44.789 13.111 38.967 1.00 16.37 ? 258 PHE A CE1 1 ATOM 1930 C CE2 . PHE A 1 258 ? 42.495 13.565 39.524 1.00 20.15 ? 258 PHE A CE2 1 ATOM 1931 C CZ . PHE A 1 258 ? 43.774 13.207 39.906 1.00 17.95 ? 258 PHE A CZ 1 ATOM 1932 N N . VAL A 1 259 ? 41.555 13.244 32.764 1.00 14.18 ? 259 VAL A N 1 ATOM 1933 C CA . VAL A 1 259 ? 41.127 13.827 31.472 1.00 13.78 ? 259 VAL A CA 1 ATOM 1934 C C . VAL A 1 259 ? 39.626 14.117 31.541 1.00 14.21 ? 259 VAL A C 1 ATOM 1935 O O . VAL A 1 259 ? 38.826 13.218 31.800 1.00 13.75 ? 259 VAL A O 1 ATOM 1936 C CB . VAL A 1 259 ? 41.384 12.860 30.300 1.00 17.76 ? 259 VAL A CB 1 ATOM 1937 C CG1 . VAL A 1 259 ? 40.796 13.403 28.997 1.00 15.78 ? 259 VAL A CG1 1 ATOM 1938 C CG2 . VAL A 1 259 ? 42.873 12.582 30.137 1.00 15.29 ? 259 VAL A CG2 1 ATOM 1939 N N . ASN A 1 260 ? 39.220 15.359 31.288 1.00 12.50 ? 260 ASN A N 1 ATOM 1940 C CA . ASN A 1 260 ? 37.824 15.741 31.226 1.00 14.68 ? 260 ASN A CA 1 ATOM 1941 C C . ASN A 1 260 ? 37.122 15.568 32.561 1.00 22.07 ? 260 ASN A C 1 ATOM 1942 O O . ASN A 1 260 ? 35.902 15.453 32.662 1.00 20.43 ? 260 ASN A O 1 ATOM 1943 C CB . ASN A 1 260 ? 37.074 14.955 30.124 1.00 13.52 ? 260 ASN A CB 1 ATOM 1944 C CG . ASN A 1 260 ? 35.792 15.694 29.776 1.00 15.06 ? 260 ASN A CG 1 ATOM 1945 O OD1 . ASN A 1 260 ? 35.788 16.934 29.713 1.00 15.82 ? 260 ASN A OD1 1 ATOM 1946 N ND2 . ASN A 1 260 ? 34.692 14.979 29.604 1.00 20.46 ? 260 ASN A ND2 1 ATOM 1947 N N . GLU A 1 261 ? 37.914 15.553 33.644 1.00 14.23 ? 261 GLU A N 1 ATOM 1948 C CA . GLU A 1 261 ? 37.277 15.472 34.965 1.00 16.10 ? 261 GLU A CA 1 ATOM 1949 C C . GLU A 1 261 ? 37.779 16.634 35.824 1.00 20.52 ? 261 GLU A C 1 ATOM 1950 O O . GLU A 1 261 ? 38.560 16.416 36.753 1.00 16.70 ? 261 GLU A O 1 ATOM 1951 C CB . GLU A 1 261 ? 37.611 14.137 35.643 1.00 13.05 ? 261 GLU A CB 1 ATOM 1952 C CG . GLU A 1 261 ? 37.035 12.948 34.877 1.00 17.52 ? 261 GLU A CG 1 ATOM 1953 C CD . GLU A 1 261 ? 35.529 12.863 35.060 1.00 25.21 ? 261 GLU A CD 1 ATOM 1954 O OE1 . GLU A 1 261 ? 34.920 12.086 34.293 1.00 30.97 ? 261 GLU A OE1 1 ATOM 1955 O OE2 . GLU A 1 261 ? 34.948 13.541 35.925 1.00 21.22 ? 261 GLU A OE2 1 ATOM 1956 N N . GLN A 1 262 ? 37.327 17.829 35.468 1.00 15.12 ? 262 GLN A N 1 ATOM 1957 C CA . GLN A 1 262 ? 37.787 19.076 36.073 1.00 17.72 ? 262 GLN A CA 1 ATOM 1958 C C . GLN A 1 262 ? 37.623 19.063 37.588 1.00 18.98 ? 262 GLN A C 1 ATOM 1959 O O . GLN A 1 262 ? 38.531 19.445 38.334 1.00 14.46 ? 262 GLN A O 1 ATOM 1960 C CB . GLN A 1 262 ? 36.966 20.245 35.497 1.00 19.89 ? 262 GLN A CB 1 ATOM 1961 C CG . GLN A 1 262 ? 37.219 21.582 36.224 1.00 19.85 ? 262 GLN A CG 1 ATOM 1962 C CD . GLN A 1 262 ? 38.650 22.007 35.916 1.00 22.79 ? 262 GLN A CD 1 ATOM 1963 O OE1 . GLN A 1 262 ? 39.122 21.694 34.823 1.00 17.09 ? 262 GLN A OE1 1 ATOM 1964 N NE2 . GLN A 1 262 ? 39.300 22.722 36.844 1.00 20.21 ? 262 GLN A NE2 1 ATOM 1965 N N . ALA A 1 263 ? 36.429 18.750 38.091 1.00 18.05 ? 263 ALA A N 1 ATOM 1966 C CA . ALA A 1 263 ? 36.199 18.955 39.526 1.00 14.96 ? 263 ALA A CA 1 ATOM 1967 C C . ALA A 1 263 ? 37.002 17.931 40.327 1.00 17.06 ? 263 ALA A C 1 ATOM 1968 O O . ALA A 1 263 ? 37.482 18.195 41.441 1.00 15.61 ? 263 ALA A O 1 ATOM 1969 C CB . ALA A 1 263 ? 34.709 18.835 39.860 1.00 22.07 ? 263 ALA A CB 1 ATOM 1970 N N . PHE A 1 264 ? 37.111 16.751 39.732 1.00 16.77 ? 264 PHE A N 1 ATOM 1971 C CA . PHE A 1 264 ? 37.907 15.695 40.375 1.00 16.60 ? 264 PHE A CA 1 ATOM 1972 C C . PHE A 1 264 ? 39.365 16.126 40.408 1.00 15.45 ? 264 PHE A C 1 ATOM 1973 O O . PHE A 1 264 ? 40.053 15.995 41.430 1.00 15.66 ? 264 PHE A O 1 ATOM 1974 C CB . PHE A 1 264 ? 37.665 14.419 39.568 1.00 14.15 ? 264 PHE A CB 1 ATOM 1975 C CG . PHE A 1 264 ? 38.458 13.218 40.064 1.00 12.70 ? 264 PHE A CG 1 ATOM 1976 C CD1 . PHE A 1 264 ? 38.596 12.947 41.418 1.00 17.28 ? 264 PHE A CD1 1 ATOM 1977 C CD2 . PHE A 1 264 ? 39.004 12.357 39.125 1.00 17.87 ? 264 PHE A CD2 1 ATOM 1978 C CE1 . PHE A 1 264 ? 39.262 11.784 41.798 1.00 19.75 ? 264 PHE A CE1 1 ATOM 1979 C CE2 . PHE A 1 264 ? 39.695 11.213 39.506 1.00 20.81 ? 264 PHE A CE2 1 ATOM 1980 C CZ . PHE A 1 264 ? 39.853 10.957 40.863 1.00 13.62 ? 264 PHE A CZ 1 ATOM 1981 N N . MET A 1 265 ? 39.843 16.693 39.298 1.00 12.72 ? 265 MET A N 1 ATOM 1982 C CA . MET A 1 265 ? 41.244 17.119 39.269 1.00 13.08 ? 265 MET A CA 1 ATOM 1983 C C . MET A 1 265 ? 41.484 18.204 40.322 1.00 19.88 ? 265 MET A C 1 ATOM 1984 O O . MET A 1 265 ? 42.434 18.158 41.118 1.00 17.65 ? 265 MET A O 1 ATOM 1985 C CB . MET A 1 265 ? 41.615 17.617 37.874 1.00 16.45 ? 265 MET A CB 1 ATOM 1986 C CG . MET A 1 265 ? 43.071 18.075 37.739 1.00 16.55 ? 265 MET A CG 1 ATOM 1987 S SD . MET A 1 265 ? 43.345 19.075 36.244 1.00 17.79 ? 265 MET A SD 1 ATOM 1988 C CE . MET A 1 265 ? 42.498 20.587 36.718 1.00 19.18 ? 265 MET A CE 1 ATOM 1989 N N . ALA A 1 266 ? 40.611 19.208 40.317 1.00 13.75 ? 266 ALA A N 1 ATOM 1990 C CA . ALA A 1 266 ? 40.823 20.336 41.231 1.00 14.47 ? 266 ALA A CA 1 ATOM 1991 C C . ALA A 1 266 ? 40.716 19.871 42.688 1.00 13.01 ? 266 ALA A C 1 ATOM 1992 O O . ALA A 1 266 ? 41.543 20.290 43.499 1.00 13.84 ? 266 ALA A O 1 ATOM 1993 C CB . ALA A 1 266 ? 39.810 21.429 40.925 1.00 18.81 ? 266 ALA A CB 1 ATOM 1994 N N . ALA A 1 267 ? 39.731 19.041 43.036 1.00 15.96 ? 267 ALA A N 1 ATOM 1995 C CA . ALA A 1 267 ? 39.620 18.583 44.430 1.00 18.39 ? 267 ALA A CA 1 ATOM 1996 C C . ALA A 1 267 ? 40.838 17.755 44.815 1.00 17.94 ? 267 ALA A C 1 ATOM 1997 O O . ALA A 1 267 ? 41.377 17.873 45.927 1.00 16.25 ? 267 ALA A O 1 ATOM 1998 C CB . ALA A 1 267 ? 38.367 17.738 44.656 1.00 18.48 ? 267 ALA A CB 1 ATOM 1999 N N . SER A 1 268 ? 41.292 16.881 43.927 1.00 16.41 ? 268 SER A N 1 ATOM 2000 C CA . SER A 1 268 ? 42.473 16.065 44.202 1.00 18.43 ? 268 SER A CA 1 ATOM 2001 C C . SER A 1 268 ? 43.722 16.908 44.387 1.00 17.71 ? 268 SER A C 1 ATOM 2002 O O . SER A 1 268 ? 44.542 16.646 45.279 1.00 14.07 ? 268 SER A O 1 ATOM 2003 C CB . SER A 1 268 ? 42.692 15.012 43.102 1.00 15.73 ? 268 SER A CB 1 ATOM 2004 O OG . SER A 1 268 ? 41.485 14.233 42.990 1.00 15.39 ? 268 SER A OG 1 ATOM 2005 N N . PHE A 1 269 ? 43.884 17.938 43.557 1.00 13.83 ? 269 PHE A N 1 ATOM 2006 C CA . PHE A 1 269 ? 45.028 18.859 43.689 1.00 13.93 ? 269 PHE A CA 1 ATOM 2007 C C . PHE A 1 269 ? 44.960 19.597 45.026 1.00 17.86 ? 269 PHE A C 1 ATOM 2008 O O . PHE A 1 269 ? 45.959 19.726 45.765 1.00 14.20 ? 269 PHE A O 1 ATOM 2009 C CB . PHE A 1 269 ? 45.009 19.850 42.527 1.00 16.89 ? 269 PHE A CB 1 ATOM 2010 C CG . PHE A 1 269 ? 46.134 20.875 42.522 1.00 18.65 ? 269 PHE A CG 1 ATOM 2011 C CD1 . PHE A 1 269 ? 47.397 20.513 42.069 1.00 12.41 ? 269 PHE A CD1 1 ATOM 2012 C CD2 . PHE A 1 269 ? 45.933 22.169 42.983 1.00 17.05 ? 269 PHE A CD2 1 ATOM 2013 C CE1 . PHE A 1 269 ? 48.463 21.393 42.135 1.00 11.04 ? 269 PHE A CE1 1 ATOM 2014 C CE2 . PHE A 1 269 ? 46.980 23.095 42.978 1.00 14.22 ? 269 PHE A CE2 1 ATOM 2015 C CZ . PHE A 1 269 ? 48.225 22.709 42.494 1.00 13.32 ? 269 PHE A CZ 1 ATOM 2016 N N . ARG A 1 270 ? 43.761 20.095 45.381 1.00 14.91 ? 270 ARG A N 1 ATOM 2017 C CA . ARG A 1 270 ? 43.648 20.760 46.671 1.00 13.66 ? 270 ARG A CA 1 ATOM 2018 C C . ARG A 1 270 ? 44.057 19.803 47.806 1.00 17.18 ? 270 ARG A C 1 ATOM 2019 O O . ARG A 1 270 ? 44.763 20.235 48.718 1.00 17.17 ? 270 ARG A O 1 ATOM 2020 C CB . ARG A 1 270 ? 42.225 21.198 46.985 1.00 15.22 ? 270 ARG A CB 1 ATOM 2021 C CG . ARG A 1 270 ? 42.138 22.102 48.213 1.00 14.72 ? 270 ARG A CG 1 ATOM 2022 C CD . ARG A 1 270 ? 40.672 22.455 48.468 1.00 17.46 ? 270 ARG A CD 1 ATOM 2023 N NE . ARG A 1 270 ? 40.519 23.406 49.557 1.00 21.77 ? 270 ARG A NE 1 ATOM 2024 C CZ . ARG A 1 270 ? 40.431 23.240 50.861 1.00 27.18 ? 270 ARG A CZ 1 ATOM 2025 N NH1 . ARG A 1 270 ? 40.492 22.048 51.442 1.00 22.12 ? 270 ARG A NH1 1 ATOM 2026 N NH2 . ARG A 1 270 ? 40.302 24.296 51.660 1.00 25.29 ? 270 ARG A NH2 1 ATOM 2027 N N . ALA A 1 271 ? 43.582 18.561 47.725 1.00 12.83 ? 271 ALA A N 1 ATOM 2028 C CA . ALA A 1 271 ? 43.904 17.641 48.820 1.00 13.83 ? 271 ALA A CA 1 ATOM 2029 C C . ALA A 1 271 ? 45.417 17.443 48.903 1.00 15.79 ? 271 ALA A C 1 ATOM 2030 O O . ALA A 1 271 ? 45.993 17.471 49.994 1.00 16.75 ? 271 ALA A O 1 ATOM 2031 C CB . ALA A 1 271 ? 43.172 16.320 48.643 1.00 15.44 ? 271 ALA A CB 1 ATOM 2032 N N . ALA A 1 272 ? 46.091 17.268 47.774 1.00 12.88 ? 272 ALA A N 1 ATOM 2033 C CA . ALA A 1 272 ? 47.531 16.980 47.777 1.00 14.54 ? 272 ALA A CA 1 ATOM 2034 C C . ALA A 1 272 ? 48.291 18.232 48.192 1.00 17.48 ? 272 ALA A C 1 ATOM 2035 O O . ALA A 1 272 ? 49.281 18.137 48.915 1.00 16.06 ? 272 ALA A O 1 ATOM 2036 C CB . ALA A 1 272 ? 47.969 16.506 46.397 1.00 15.89 ? 272 ALA A CB 1 ATOM 2037 N N . MET A 1 273 ? 47.821 19.414 47.769 1.00 14.43 ? 273 MET A N 1 ATOM 2038 C CA . MET A 1 273 ? 48.530 20.632 48.168 1.00 14.09 ? 273 MET A CA 1 ATOM 2039 C C . MET A 1 273 ? 48.372 20.874 49.667 1.00 16.91 ? 273 MET A C 1 ATOM 2040 O O . MET A 1 273 ? 49.220 21.536 50.285 1.00 18.30 ? 273 MET A O 1 ATOM 2041 C CB . MET A 1 273 ? 48.020 21.875 47.427 1.00 14.51 ? 273 MET A CB 1 ATOM 2042 C CG . MET A 1 273 ? 48.413 21.835 45.957 1.00 16.94 ? 273 MET A CG 1 ATOM 2043 S SD . MET A 1 273 ? 50.185 22.182 45.775 1.00 20.60 ? 273 MET A SD 1 ATOM 2044 C CE . MET A 1 273 ? 50.320 23.743 46.638 1.00 25.36 ? 273 MET A CE 1 ATOM 2045 N N . SER A 1 274 ? 47.268 20.424 50.252 1.00 12.72 ? 274 SER A N 1 ATOM 2046 C CA . SER A 1 274 ? 47.066 20.645 51.679 1.00 17.84 ? 274 SER A CA 1 ATOM 2047 C C . SER A 1 274 ? 48.201 19.922 52.415 1.00 21.45 ? 274 SER A C 1 ATOM 2048 O O . SER A 1 274 ? 48.665 20.419 53.428 1.00 17.40 ? 274 SER A O 1 ATOM 2049 C CB A SER A 1 274 ? 45.723 20.085 52.136 0.50 22.52 ? 274 SER A CB 1 ATOM 2050 C CB B SER A 1 274 ? 45.726 20.069 52.129 0.50 21.60 ? 274 SER A CB 1 ATOM 2051 O OG A SER A 1 274 ? 45.489 20.435 53.489 0.50 27.20 ? 274 SER A OG 1 ATOM 2052 O OG B SER A 1 274 ? 45.762 19.706 53.499 0.50 26.14 ? 274 SER A OG 1 ATOM 2053 N N . LYS A 1 275 ? 48.595 18.765 51.913 1.00 14.33 ? 275 LYS A N 1 ATOM 2054 C CA . LYS A 1 275 ? 49.710 17.987 52.505 1.00 14.28 ? 275 LYS A CA 1 ATOM 2055 C C . LYS A 1 275 ? 51.045 18.627 52.189 1.00 19.50 ? 275 LYS A C 1 ATOM 2056 O O . LYS A 1 275 ? 51.925 18.781 53.041 1.00 16.08 ? 275 LYS A O 1 ATOM 2057 C CB . LYS A 1 275 ? 49.571 16.583 51.983 1.00 17.24 ? 275 LYS A CB 1 ATOM 2058 C CG . LYS A 1 275 ? 50.489 15.442 52.323 1.00 31.34 ? 275 LYS A CG 1 ATOM 2059 C CD . LYS A 1 275 ? 49.700 14.153 52.082 1.00 27.29 ? 275 LYS A CD 1 ATOM 2060 C CE . LYS A 1 275 ? 50.500 12.883 52.235 1.00 46.67 ? 275 LYS A CE 1 ATOM 2061 N NZ . LYS A 1 275 ? 49.592 11.708 52.439 1.00 44.88 ? 275 LYS A NZ 1 ATOM 2062 N N . LEU A 1 276 ? 51.257 19.027 50.930 1.00 15.78 ? 276 LEU A N 1 ATOM 2063 C CA . LEU A 1 276 ? 52.523 19.614 50.504 1.00 13.41 ? 276 LEU A CA 1 ATOM 2064 C C . LEU A 1 276 ? 52.823 20.878 51.291 1.00 15.64 ? 276 LEU A C 1 ATOM 2065 O O . LEU A 1 276 ? 53.977 21.122 51.699 1.00 14.99 ? 276 LEU A O 1 ATOM 2066 C CB . LEU A 1 276 ? 52.424 19.932 48.992 1.00 17.09 ? 276 LEU A CB 1 ATOM 2067 C CG . LEU A 1 276 ? 53.686 20.575 48.381 1.00 13.38 ? 276 LEU A CG 1 ATOM 2068 C CD1 . LEU A 1 276 ? 54.823 19.555 48.365 1.00 19.49 ? 276 LEU A CD1 1 ATOM 2069 C CD2 . LEU A 1 276 ? 53.429 21.049 46.960 1.00 27.05 ? 276 LEU A CD2 1 ATOM 2070 N N . ALA A 1 277 ? 51.801 21.713 51.490 1.00 15.16 ? 277 ALA A N 1 ATOM 2071 C CA . ALA A 1 277 ? 52.042 23.036 52.090 1.00 14.36 ? 277 ALA A CA 1 ATOM 2072 C C . ALA A 1 277 ? 52.498 22.981 53.544 1.00 20.06 ? 277 ALA A C 1 ATOM 2073 O O . ALA A 1 277 ? 52.990 23.974 54.106 1.00 19.66 ? 277 ALA A O 1 ATOM 2074 C CB . ALA A 1 277 ? 50.757 23.850 51.975 1.00 17.13 ? 277 ALA A CB 1 ATOM 2075 N N . VAL A 1 278 ? 52.298 21.826 54.187 1.00 16.18 ? 278 VAL A N 1 ATOM 2076 C CA . VAL A 1 278 ? 52.726 21.728 55.577 1.00 16.85 ? 278 VAL A CA 1 ATOM 2077 C C . VAL A 1 278 ? 53.871 20.752 55.770 1.00 22.38 ? 278 VAL A C 1 ATOM 2078 O O . VAL A 1 278 ? 54.152 20.401 56.928 1.00 14.87 ? 278 VAL A O 1 ATOM 2079 C CB . VAL A 1 278 ? 51.551 21.370 56.518 1.00 19.08 ? 278 VAL A CB 1 ATOM 2080 C CG1 . VAL A 1 278 ? 50.503 22.478 56.394 1.00 20.73 ? 278 VAL A CG1 1 ATOM 2081 C CG2 . VAL A 1 278 ? 50.923 20.035 56.208 1.00 17.03 ? 278 VAL A CG2 1 ATOM 2082 N N . LEU A 1 279 ? 54.572 20.369 54.699 1.00 11.93 ? 279 LEU A N 1 ATOM 2083 C CA . LEU A 1 279 ? 55.746 19.502 54.911 1.00 13.33 ? 279 LEU A CA 1 ATOM 2084 C C . LEU A 1 279 ? 56.730 20.178 55.881 1.00 16.88 ? 279 LEU A C 1 ATOM 2085 O O . LEU A 1 279 ? 56.965 21.383 55.703 1.00 15.53 ? 279 LEU A O 1 ATOM 2086 C CB . LEU A 1 279 ? 56.447 19.255 53.572 1.00 12.56 ? 279 LEU A CB 1 ATOM 2087 C CG . LEU A 1 279 ? 55.701 18.297 52.626 1.00 16.93 ? 279 LEU A CG 1 ATOM 2088 C CD1 . LEU A 1 279 ? 56.589 17.954 51.428 1.00 16.86 ? 279 LEU A CD1 1 ATOM 2089 C CD2 . LEU A 1 279 ? 55.301 17.013 53.331 1.00 18.44 ? 279 LEU A CD2 1 ATOM 2090 N N . GLY A 1 280 ? 57.278 19.442 56.828 1.00 12.68 ? 280 GLY A N 1 ATOM 2091 C CA . GLY A 1 280 ? 58.206 19.983 57.830 1.00 16.77 ? 280 GLY A CA 1 ATOM 2092 C C . GLY A 1 280 ? 57.476 20.527 59.038 1.00 18.56 ? 280 GLY A C 1 ATOM 2093 O O . GLY A 1 280 ? 58.077 21.096 59.964 1.00 16.57 ? 280 GLY A O 1 ATOM 2094 N N . HIS A 1 281 ? 56.161 20.368 59.120 1.00 17.04 ? 281 HIS A N 1 ATOM 2095 C CA . HIS A 1 281 ? 55.373 20.886 60.234 1.00 14.21 ? 281 HIS A CA 1 ATOM 2096 C C . HIS A 1 281 ? 54.283 19.902 60.661 1.00 17.53 ? 281 HIS A C 1 ATOM 2097 O O . HIS A 1 281 ? 53.866 19.122 59.813 1.00 20.36 ? 281 HIS A O 1 ATOM 2098 C CB . HIS A 1 281 ? 54.622 22.179 59.819 1.00 14.52 ? 281 HIS A CB 1 ATOM 2099 C CG . HIS A 1 281 ? 55.606 23.223 59.377 1.00 15.33 ? 281 HIS A CG 1 ATOM 2100 N ND1 . HIS A 1 281 ? 55.892 23.465 58.045 1.00 21.70 ? 281 HIS A ND1 1 ATOM 2101 C CD2 . HIS A 1 281 ? 56.389 24.052 60.092 1.00 12.44 ? 281 HIS A CD2 1 ATOM 2102 C CE1 . HIS A 1 281 ? 56.803 24.432 57.972 1.00 12.13 ? 281 HIS A CE1 1 ATOM 2103 N NE2 . HIS A 1 281 ? 57.121 24.802 59.198 1.00 18.76 ? 281 HIS A NE2 1 ATOM 2104 N N . ASN A 1 282 ? 53.820 20.054 61.885 1.00 14.96 ? 282 ASN A N 1 ATOM 2105 C CA . ASN A 1 282 ? 52.615 19.366 62.383 1.00 18.77 ? 282 ASN A CA 1 ATOM 2106 C C . ASN A 1 282 ? 51.425 20.254 62.083 1.00 23.17 ? 282 ASN A C 1 ATOM 2107 O O . ASN A 1 282 ? 51.285 21.366 62.599 1.00 18.11 ? 282 ASN A O 1 ATOM 2108 C CB . ASN A 1 282 ? 52.738 19.220 63.914 1.00 21.67 ? 282 ASN A CB 1 ATOM 2109 C CG . ASN A 1 282 ? 51.692 18.265 64.455 1.00 30.97 ? 282 ASN A CG 1 ATOM 2110 O OD1 . ASN A 1 282 ? 50.556 18.257 63.992 1.00 23.91 ? 282 ASN A OD1 1 ATOM 2111 N ND2 . ASN A 1 282 ? 52.070 17.493 65.463 1.00 22.71 ? 282 ASN A ND2 1 ATOM 2112 N N . ARG A 1 283 ? 50.505 19.821 61.218 1.00 18.05 ? 283 ARG A N 1 ATOM 2113 C CA . ARG A 1 283 ? 49.396 20.694 60.859 1.00 17.43 ? 283 ARG A CA 1 ATOM 2114 C C . ARG A 1 283 ? 48.555 21.085 62.062 1.00 21.66 ? 283 ARG A C 1 ATOM 2115 O O . ARG A 1 283 ? 47.806 22.055 62.010 1.00 19.00 ? 283 ARG A O 1 ATOM 2116 C CB . ARG A 1 283 ? 48.525 20.032 59.772 1.00 19.63 ? 283 ARG A CB 1 ATOM 2117 C CG . ARG A 1 283 ? 47.692 18.851 60.203 1.00 21.98 ? 283 ARG A CG 1 ATOM 2118 C CD . ARG A 1 283 ? 46.662 18.450 59.135 1.00 23.23 ? 283 ARG A CD 1 ATOM 2119 N NE . ARG A 1 283 ? 45.514 19.346 59.143 1.00 33.75 ? 283 ARG A NE 1 ATOM 2120 C CZ . ARG A 1 283 ? 45.138 20.132 58.131 1.00 27.95 ? 283 ARG A CZ 1 ATOM 2121 N NH1 . ARG A 1 283 ? 45.810 20.118 56.989 1.00 21.20 ? 283 ARG A NH1 1 ATOM 2122 N NH2 . ARG A 1 283 ? 44.090 20.936 58.291 1.00 26.50 ? 283 ARG A NH2 1 ATOM 2123 N N . ASN A 1 284 ? 48.652 20.346 63.174 1.00 22.06 ? 284 ASN A N 1 ATOM 2124 C CA . ASN A 1 284 ? 47.860 20.666 64.365 1.00 22.01 ? 284 ASN A CA 1 ATOM 2125 C C . ASN A 1 284 ? 48.468 21.846 65.112 1.00 13.27 ? 284 ASN A C 1 ATOM 2126 O O . ASN A 1 284 ? 47.897 22.327 66.089 1.00 24.24 ? 284 ASN A O 1 ATOM 2127 C CB . ASN A 1 284 ? 47.813 19.430 65.265 1.00 17.10 ? 284 ASN A CB 1 ATOM 2128 C CG . ASN A 1 284 ? 47.153 18.259 64.562 1.00 26.88 ? 284 ASN A CG 1 ATOM 2129 O OD1 . ASN A 1 284 ? 47.807 17.260 64.252 1.00 39.99 ? 284 ASN A OD1 1 ATOM 2130 N ND2 . ASN A 1 284 ? 45.843 18.326 64.352 1.00 23.87 ? 284 ASN A ND2 1 ATOM 2131 N N . SER A 1 285 ? 49.626 22.293 64.640 1.00 16.10 ? 285 SER A N 1 ATOM 2132 C CA . SER A 1 285 ? 50.326 23.417 65.250 1.00 19.75 ? 285 SER A CA 1 ATOM 2133 C C . SER A 1 285 ? 50.156 24.700 64.440 1.00 22.71 ? 285 SER A C 1 ATOM 2134 O O . SER A 1 285 ? 50.706 25.736 64.822 1.00 17.70 ? 285 SER A O 1 ATOM 2135 C CB . SER A 1 285 ? 51.815 23.061 65.374 1.00 31.27 ? 285 SER A CB 1 ATOM 2136 O OG . SER A 1 285 ? 51.949 21.874 66.142 1.00 71.03 ? 285 SER A OG 1 ATOM 2137 N N . LEU A 1 286 ? 49.423 24.635 63.319 1.00 14.70 ? 286 LEU A N 1 ATOM 2138 C CA . LEU A 1 286 ? 49.268 25.797 62.442 1.00 17.36 ? 286 LEU A CA 1 ATOM 2139 C C . LEU A 1 286 ? 47.826 26.271 62.471 1.00 15.38 ? 286 LEU A C 1 ATOM 2140 O O . LEU A 1 286 ? 46.910 25.469 62.612 1.00 18.23 ? 286 LEU A O 1 ATOM 2141 C CB . LEU A 1 286 ? 49.714 25.446 61.027 1.00 20.30 ? 286 LEU A CB 1 ATOM 2142 C CG . LEU A 1 286 ? 51.158 24.922 60.917 1.00 20.31 ? 286 LEU A CG 1 ATOM 2143 C CD1 . LEU A 1 286 ? 51.415 24.471 59.485 1.00 24.17 ? 286 LEU A CD1 1 ATOM 2144 C CD2 . LEU A 1 286 ? 52.142 26.026 61.316 1.00 17.85 ? 286 LEU A CD2 1 ATOM 2145 N N . ILE A 1 287 ? 47.608 27.582 62.424 1.00 14.27 ? 287 ILE A N 1 ATOM 2146 C CA . ILE A 1 287 ? 46.258 28.093 62.567 1.00 16.33 ? 287 ILE A CA 1 ATOM 2147 C C . ILE A 1 287 ? 45.572 28.159 61.203 1.00 17.38 ? 287 ILE A C 1 ATOM 2148 O O . ILE A 1 287 ? 46.293 28.224 60.222 1.00 19.66 ? 287 ILE A O 1 ATOM 2149 C CB . ILE A 1 287 ? 46.294 29.521 63.151 1.00 20.86 ? 287 ILE A CB 1 ATOM 2150 C CG1 . ILE A 1 287 ? 44.905 30.042 63.523 1.00 32.94 ? 287 ILE A CG1 1 ATOM 2151 C CG2 . ILE A 1 287 ? 46.996 30.437 62.164 1.00 16.95 ? 287 ILE A CG2 1 ATOM 2152 C CD1 . ILE A 1 287 ? 44.929 30.995 64.709 1.00 44.98 ? 287 ILE A CD1 1 ATOM 2153 N N . ASP A 1 288 ? 44.252 28.095 61.141 1.00 16.17 ? 288 ASP A N 1 ATOM 2154 C CA . ASP A 1 288 ? 43.599 28.005 59.823 1.00 16.80 ? 288 ASP A CA 1 ATOM 2155 C C . ASP A 1 288 ? 43.259 29.415 59.342 1.00 20.95 ? 288 ASP A C 1 ATOM 2156 O O . ASP A 1 288 ? 42.451 30.096 59.975 1.00 23.54 ? 288 ASP A O 1 ATOM 2157 C CB . ASP A 1 288 ? 42.342 27.129 59.906 1.00 17.39 ? 288 ASP A CB 1 ATOM 2158 C CG . ASP A 1 288 ? 41.840 26.767 58.512 1.00 26.80 ? 288 ASP A CG 1 ATOM 2159 O OD1 . ASP A 1 288 ? 41.069 25.784 58.390 1.00 25.32 ? 288 ASP A OD1 1 ATOM 2160 O OD2 . ASP A 1 288 ? 42.194 27.523 57.579 1.00 19.86 ? 288 ASP A OD2 1 ATOM 2161 N N . CYS A 1 289 ? 43.949 29.803 58.270 1.00 16.18 ? 289 CYS A N 1 ATOM 2162 C CA . CYS A 1 289 ? 43.690 31.117 57.678 1.00 19.81 ? 289 CYS A CA 1 ATOM 2163 C C . CYS A 1 289 ? 43.156 30.935 56.254 1.00 16.21 ? 289 CYS A C 1 ATOM 2164 O O . CYS A 1 289 ? 43.365 31.841 55.451 1.00 20.52 ? 289 CYS A O 1 ATOM 2165 C CB . CYS A 1 289 ? 44.944 31.980 57.640 1.00 17.92 ? 289 CYS A CB 1 ATOM 2166 S SG . CYS A 1 289 ? 45.447 32.573 59.285 1.00 22.01 ? 289 CYS A SG 1 ATOM 2167 N N . SER A 1 290 ? 42.442 29.851 56.003 1.00 16.45 ? 290 SER A N 1 ATOM 2168 C CA . SER A 1 290 ? 41.909 29.626 54.656 1.00 15.17 ? 290 SER A CA 1 ATOM 2169 C C . SER A 1 290 ? 40.945 30.699 54.190 1.00 24.75 ? 290 SER A C 1 ATOM 2170 O O . SER A 1 290 ? 40.771 30.868 52.971 1.00 19.43 ? 290 SER A O 1 ATOM 2171 C CB . SER A 1 290 ? 41.236 28.254 54.559 1.00 16.69 ? 290 SER A CB 1 ATOM 2172 O OG . SER A 1 290 ? 42.178 27.198 54.757 1.00 18.42 ? 290 SER A OG 1 ATOM 2173 N N . ASP A 1 291 ? 40.285 31.396 55.113 1.00 18.28 ? 291 ASP A N 1 ATOM 2174 C CA . ASP A 1 291 ? 39.268 32.368 54.682 1.00 14.26 ? 291 ASP A CA 1 ATOM 2175 C C . ASP A 1 291 ? 39.846 33.644 54.093 1.00 19.78 ? 291 ASP A C 1 ATOM 2176 O O . ASP A 1 291 ? 39.102 34.492 53.547 1.00 22.36 ? 291 ASP A O 1 ATOM 2177 C CB . ASP A 1 291 ? 38.355 32.670 55.873 1.00 17.47 ? 291 ASP A CB 1 ATOM 2178 C CG . ASP A 1 291 ? 39.105 33.171 57.091 1.00 37.37 ? 291 ASP A CG 1 ATOM 2179 O OD1 . ASP A 1 291 ? 38.698 34.239 57.593 1.00 34.37 ? 291 ASP A OD1 1 ATOM 2180 O OD2 . ASP A 1 291 ? 40.074 32.509 57.534 1.00 28.06 ? 291 ASP A OD2 1 ATOM 2181 N N . VAL A 1 292 ? 41.169 33.818 54.210 1.00 15.33 ? 292 VAL A N 1 ATOM 2182 C CA . VAL A 1 292 ? 41.789 34.975 53.593 1.00 14.18 ? 292 VAL A CA 1 ATOM 2183 C C . VAL A 1 292 ? 42.445 34.641 52.261 1.00 16.10 ? 292 VAL A C 1 ATOM 2184 O O . VAL A 1 292 ? 43.037 35.510 51.615 1.00 18.34 ? 292 VAL A O 1 ATOM 2185 C CB . VAL A 1 292 ? 42.723 35.754 54.539 1.00 17.50 ? 292 VAL A CB 1 ATOM 2186 C CG1 . VAL A 1 292 ? 41.909 36.222 55.754 1.00 23.29 ? 292 VAL A CG1 1 ATOM 2187 C CG2 . VAL A 1 292 ? 43.935 34.956 54.966 1.00 19.90 ? 292 VAL A CG2 1 ATOM 2188 N N . VAL A 1 293 ? 42.362 33.391 51.795 1.00 15.62 ? 293 VAL A N 1 ATOM 2189 C CA . VAL A 1 293 ? 42.789 33.056 50.436 1.00 16.70 ? 293 VAL A CA 1 ATOM 2190 C C . VAL A 1 293 ? 41.742 33.612 49.449 1.00 16.97 ? 293 VAL A C 1 ATOM 2191 O O . VAL A 1 293 ? 40.552 33.383 49.687 1.00 16.16 ? 293 VAL A O 1 ATOM 2192 C CB . VAL A 1 293 ? 42.853 31.540 50.215 1.00 18.71 ? 293 VAL A CB 1 ATOM 2193 C CG1 . VAL A 1 293 ? 43.179 31.237 48.755 1.00 21.07 ? 293 VAL A CG1 1 ATOM 2194 C CG2 . VAL A 1 293 ? 43.883 30.872 51.125 1.00 20.66 ? 293 VAL A CG2 1 ATOM 2195 N N . PRO A 1 294 ? 42.149 34.342 48.429 1.00 18.60 ? 294 PRO A N 1 ATOM 2196 C CA . PRO A 1 294 ? 41.138 34.885 47.481 1.00 23.07 ? 294 PRO A CA 1 ATOM 2197 C C . PRO A 1 294 ? 40.266 33.806 46.858 1.00 16.94 ? 294 PRO A C 1 ATOM 2198 O O . PRO A 1 294 ? 40.745 32.685 46.684 1.00 19.83 ? 294 PRO A O 1 ATOM 2199 C CB . PRO A 1 294 ? 42.010 35.568 46.425 1.00 16.20 ? 294 PRO A CB 1 ATOM 2200 C CG . PRO A 1 294 ? 43.232 35.991 47.197 1.00 23.09 ? 294 PRO A CG 1 ATOM 2201 C CD . PRO A 1 294 ? 43.513 34.814 48.106 1.00 16.94 ? 294 PRO A CD 1 ATOM 2202 N N . VAL A 1 295 ? 39.000 34.061 46.523 1.00 14.25 ? 295 VAL A N 1 ATOM 2203 C CA . VAL A 1 295 ? 38.157 33.035 45.894 1.00 15.60 ? 295 VAL A CA 1 ATOM 2204 C C . VAL A 1 295 ? 38.608 32.844 44.463 1.00 14.34 ? 295 VAL A C 1 ATOM 2205 O O . VAL A 1 295 ? 38.946 33.828 43.783 1.00 17.73 ? 295 VAL A O 1 ATOM 2206 C CB . VAL A 1 295 ? 36.688 33.480 45.917 1.00 23.09 ? 295 VAL A CB 1 ATOM 2207 C CG1 . VAL A 1 295 ? 35.798 32.513 45.150 1.00 21.64 ? 295 VAL A CG1 1 ATOM 2208 C CG2 . VAL A 1 295 ? 36.211 33.624 47.361 1.00 25.70 ? 295 VAL A CG2 1 ATOM 2209 N N . PRO A 1 296 ? 38.757 31.613 44.000 1.00 16.78 ? 296 PRO A N 1 ATOM 2210 C CA . PRO A 1 296 ? 39.376 31.447 42.676 1.00 16.11 ? 296 PRO A CA 1 ATOM 2211 C C . PRO A 1 296 ? 38.429 31.823 41.542 1.00 17.73 ? 296 PRO A C 1 ATOM 2212 O O . PRO A 1 296 ? 37.222 31.757 41.759 1.00 18.65 ? 296 PRO A O 1 ATOM 2213 C CB . PRO A 1 296 ? 39.694 29.941 42.638 1.00 18.96 ? 296 PRO A CB 1 ATOM 2214 C CG . PRO A 1 296 ? 38.625 29.362 43.511 1.00 22.36 ? 296 PRO A CG 1 ATOM 2215 C CD . PRO A 1 296 ? 38.538 30.333 44.675 1.00 19.65 ? 296 PRO A CD 1 ATOM 2216 N N . LYS A 1 297 ? 39.023 32.164 40.399 1.00 17.29 ? 297 LYS A N 1 ATOM 2217 C CA . LYS A 1 297 ? 38.237 32.367 39.171 1.00 17.62 ? 297 LYS A CA 1 ATOM 2218 C C . LYS A 1 297 ? 37.601 31.019 38.812 1.00 20.50 ? 297 LYS A C 1 ATOM 2219 O O . LYS A 1 297 ? 38.252 29.978 38.744 1.00 18.91 ? 297 LYS A O 1 ATOM 2220 C CB . LYS A 1 297 ? 39.087 32.854 38.000 1.00 22.36 ? 297 LYS A CB 1 ATOM 2221 C CG . LYS A 1 297 ? 39.754 34.215 38.146 1.00 19.18 ? 297 LYS A CG 1 ATOM 2222 C CD . LYS A 1 297 ? 40.523 34.563 36.884 1.00 16.09 ? 297 LYS A CD 1 ATOM 2223 C CE . LYS A 1 297 ? 41.484 35.734 37.114 1.00 20.71 ? 297 LYS A CE 1 ATOM 2224 N NZ . LYS A 1 297 ? 42.500 35.750 36.006 1.00 19.92 ? 297 LYS A NZ 1 ATOM 2225 N N . PRO A 1 298 ? 36.299 31.007 38.526 1.00 19.98 ? 298 PRO A N 1 ATOM 2226 C CA . PRO A 1 298 ? 35.636 29.741 38.162 1.00 21.56 ? 298 PRO A CA 1 ATOM 2227 C C . PRO A 1 298 ? 36.005 29.334 36.733 1.00 16.23 ? 298 PRO A C 1 ATOM 2228 O O . PRO A 1 298 ? 36.351 30.200 35.936 1.00 22.93 ? 298 PRO A O 1 ATOM 2229 C CB . PRO A 1 298 ? 34.151 30.111 38.198 1.00 21.50 ? 298 PRO A CB 1 ATOM 2230 C CG . PRO A 1 298 ? 34.112 31.585 37.924 1.00 22.90 ? 298 PRO A CG 1 ATOM 2231 C CD . PRO A 1 298 ? 35.398 32.169 38.484 1.00 27.00 ? 298 PRO A CD 1 ATOM 2232 N N . ALA A 1 299 ? 35.930 28.047 36.449 1.00 16.32 ? 299 ALA A N 1 ATOM 2233 C CA . ALA A 1 299 ? 36.072 27.534 35.090 1.00 15.66 ? 299 ALA A CA 1 ATOM 2234 C C . ALA A 1 299 ? 34.838 27.906 34.262 1.00 24.81 ? 299 ALA A C 1 ATOM 2235 O O . ALA A 1 299 ? 33.750 28.118 34.816 1.00 20.97 ? 299 ALA A O 1 ATOM 2236 C CB . ALA A 1 299 ? 36.123 26.006 35.161 1.00 17.69 ? 299 ALA A CB 1 ATOM 2237 N N . THR A 1 300 ? 34.950 27.840 32.930 1.00 17.37 ? 300 THR A N 1 ATOM 2238 C CA . THR A 1 300 ? 33.709 28.060 32.170 1.00 19.62 ? 300 THR A CA 1 ATOM 2239 C C . THR A 1 300 ? 32.807 26.832 32.252 1.00 20.94 ? 300 THR A C 1 ATOM 2240 O O . THR A 1 300 ? 31.615 26.886 31.905 1.00 18.80 ? 300 THR A O 1 ATOM 2241 C CB . THR A 1 300 ? 33.994 28.300 30.677 1.00 20.02 ? 300 THR A CB 1 ATOM 2242 O OG1 . THR A 1 300 ? 34.693 27.136 30.197 1.00 26.75 ? 300 THR A OG1 1 ATOM 2243 C CG2 . THR A 1 300 ? 34.853 29.504 30.387 1.00 20.21 ? 300 THR A CG2 1 ATOM 2244 N N . GLY A 1 301 ? 33.361 25.673 32.601 1.00 17.88 ? 301 GLY A N 1 ATOM 2245 C CA . GLY A 1 301 ? 32.548 24.467 32.684 1.00 19.80 ? 301 GLY A CA 1 ATOM 2246 C C . GLY A 1 301 ? 32.578 23.644 31.409 1.00 19.78 ? 301 GLY A C 1 ATOM 2247 O O . GLY A 1 301 ? 31.990 22.562 31.349 1.00 23.50 ? 301 GLY A O 1 ATOM 2248 N N . GLN A 1 302 ? 33.278 24.080 30.366 1.00 17.83 ? 302 GLN A N 1 ATOM 2249 C CA . GLN A 1 302 ? 33.361 23.325 29.120 1.00 15.90 ? 302 GLN A CA 1 ATOM 2250 C C . GLN A 1 302 ? 34.198 22.049 29.298 1.00 21.74 ? 302 GLN A C 1 ATOM 2251 O O . GLN A 1 302 ? 35.179 22.050 30.059 1.00 15.15 ? 302 GLN A O 1 ATOM 2252 C CB . GLN A 1 302 ? 34.023 24.124 27.998 1.00 14.93 ? 302 GLN A CB 1 ATOM 2253 C CG . GLN A 1 302 ? 33.232 25.294 27.451 1.00 40.01 ? 302 GLN A CG 1 ATOM 2254 C CD . GLN A 1 302 ? 33.868 25.808 26.161 1.00 24.93 ? 302 GLN A CD 1 ATOM 2255 O OE1 . GLN A 1 302 ? 34.990 26.309 26.183 1.00 23.65 ? 302 GLN A OE1 1 ATOM 2256 N NE2 . GLN A 1 302 ? 33.172 25.593 25.052 1.00 53.22 ? 302 GLN A NE2 1 ATOM 2257 N N . PRO A 1 303 ? 33.837 20.996 28.562 1.00 21.57 ? 303 PRO A N 1 ATOM 2258 C CA . PRO A 1 303 ? 34.598 19.750 28.579 1.00 15.96 ? 303 PRO A CA 1 ATOM 2259 C C . PRO A 1 303 ? 35.942 19.945 27.887 1.00 20.48 ? 303 PRO A C 1 ATOM 2260 O O . PRO A 1 303 ? 36.177 20.895 27.138 1.00 16.75 ? 303 PRO A O 1 ATOM 2261 C CB . PRO A 1 303 ? 33.782 18.783 27.714 1.00 20.01 ? 303 PRO A CB 1 ATOM 2262 C CG . PRO A 1 303 ? 32.411 19.386 27.704 1.00 28.10 ? 303 PRO A CG 1 ATOM 2263 C CD . PRO A 1 303 ? 32.680 20.873 27.650 1.00 25.04 ? 303 PRO A CD 1 ATOM 2264 N N . ALA A 1 304 ? 36.848 19.035 28.225 1.00 15.52 ? 304 ALA A N 1 ATOM 2265 C CA . ALA A 1 304 ? 38.138 19.037 27.530 1.00 12.67 ? 304 ALA A CA 1 ATOM 2266 C C . ALA A 1 304 ? 37.897 18.740 26.047 1.00 15.16 ? 304 ALA A C 1 ATOM 2267 O O . ALA A 1 304 ? 36.902 18.094 25.754 1.00 16.35 ? 304 ALA A O 1 ATOM 2268 C CB . ALA A 1 304 ? 39.028 17.939 28.128 1.00 18.33 ? 304 ALA A CB 1 ATOM 2269 N N . MET A 1 305 ? 38.780 19.218 25.181 1.00 14.43 ? 305 MET A N 1 ATOM 2270 C CA . MET A 1 305 ? 38.634 19.001 23.732 1.00 11.41 ? 305 MET A CA 1 ATOM 2271 C C . MET A 1 305 ? 39.987 18.778 23.065 1.00 13.42 ? 305 MET A C 1 ATOM 2272 O O . MET A 1 305 ? 41.003 19.332 23.488 1.00 15.85 ? 305 MET A O 1 ATOM 2273 C CB . MET A 1 305 ? 37.994 20.229 23.080 1.00 12.01 ? 305 MET A CB 1 ATOM 2274 C CG . MET A 1 305 ? 36.645 20.649 23.629 1.00 14.39 ? 305 MET A CG 1 ATOM 2275 S SD . MET A 1 305 ? 36.071 22.186 22.871 1.00 21.69 ? 305 MET A SD 1 ATOM 2276 C CE . MET A 1 305 ? 37.151 23.394 23.526 1.00 14.60 ? 305 MET A CE 1 ATOM 2277 N N . PHE A 1 306 ? 39.999 17.990 21.980 1.00 14.45 ? 306 PHE A N 1 ATOM 2278 C CA . PHE A 1 306 ? 41.267 17.842 21.260 1.00 14.20 ? 306 PHE A CA 1 ATOM 2279 C C . PHE A 1 306 ? 41.580 19.152 20.540 1.00 18.74 ? 306 PHE A C 1 ATOM 2280 O O . PHE A 1 306 ? 40.711 19.684 19.840 1.00 17.02 ? 306 PHE A O 1 ATOM 2281 C CB . PHE A 1 306 ? 41.149 16.728 20.219 1.00 14.07 ? 306 PHE A CB 1 ATOM 2282 C CG . PHE A 1 306 ? 41.061 15.332 20.813 1.00 12.70 ? 306 PHE A CG 1 ATOM 2283 C CD1 . PHE A 1 306 ? 39.825 14.792 21.118 1.00 13.21 ? 306 PHE A CD1 1 ATOM 2284 C CD2 . PHE A 1 306 ? 42.224 14.596 20.995 1.00 15.26 ? 306 PHE A CD2 1 ATOM 2285 C CE1 . PHE A 1 306 ? 39.709 13.464 21.532 1.00 20.27 ? 306 PHE A CE1 1 ATOM 2286 C CE2 . PHE A 1 306 ? 42.113 13.282 21.431 1.00 19.35 ? 306 PHE A CE2 1 ATOM 2287 C CZ . PHE A 1 306 ? 40.876 12.736 21.705 1.00 22.49 ? 306 PHE A CZ 1 ATOM 2288 N N . PRO A 1 307 ? 42.768 19.694 20.703 1.00 19.49 ? 307 PRO A N 1 ATOM 2289 C CA . PRO A 1 307 ? 43.143 20.892 19.931 1.00 17.26 ? 307 PRO A CA 1 ATOM 2290 C C . PRO A 1 307 ? 43.198 20.545 18.439 1.00 21.55 ? 307 PRO A C 1 ATOM 2291 O O . PRO A 1 307 ? 43.420 19.397 18.024 1.00 21.69 ? 307 PRO A O 1 ATOM 2292 C CB . PRO A 1 307 ? 44.564 21.198 20.416 1.00 20.55 ? 307 PRO A CB 1 ATOM 2293 C CG . PRO A 1 307 ? 44.633 20.559 21.766 1.00 21.76 ? 307 PRO A CG 1 ATOM 2294 C CD . PRO A 1 307 ? 43.799 19.315 21.687 1.00 21.17 ? 307 PRO A CD 1 ATOM 2295 N N . ALA A 1 308 ? 42.969 21.570 17.619 1.00 21.11 ? 308 ALA A N 1 ATOM 2296 C CA . ALA A 1 308 ? 43.012 21.332 16.176 1.00 19.78 ? 308 ALA A CA 1 ATOM 2297 C C . ALA A 1 308 ? 44.369 20.747 15.779 1.00 18.14 ? 308 ALA A C 1 ATOM 2298 O O . ALA A 1 308 ? 45.401 21.078 16.383 1.00 21.70 ? 308 ALA A O 1 ATOM 2299 C CB . ALA A 1 308 ? 42.768 22.661 15.491 1.00 21.36 ? 308 ALA A CB 1 ATOM 2300 N N . SER A 1 309 ? 44.363 19.872 14.794 1.00 20.79 ? 309 SER A N 1 ATOM 2301 C CA . SER A 1 309 ? 45.488 19.113 14.284 1.00 22.62 ? 309 SER A CA 1 ATOM 2302 C C . SER A 1 309 ? 45.669 17.785 15.030 1.00 25.38 ? 309 SER A C 1 ATOM 2303 O O . SER A 1 309 ? 46.500 16.970 14.600 1.00 22.75 ? 309 SER A O 1 ATOM 2304 C CB . SER A 1 309 ? 46.792 19.897 14.260 1.00 18.70 ? 309 SER A CB 1 ATOM 2305 O OG . SER A 1 309 ? 47.463 19.832 15.504 1.00 21.49 ? 309 SER A OG 1 ATOM 2306 N N . THR A 1 310 ? 44.842 17.562 16.061 1.00 22.87 ? 310 THR A N 1 ATOM 2307 C CA . THR A 1 310 ? 44.863 16.309 16.806 1.00 18.95 ? 310 THR A CA 1 ATOM 2308 C C . THR A 1 310 ? 43.499 15.650 16.921 1.00 15.84 ? 310 THR A C 1 ATOM 2309 O O . THR A 1 310 ? 42.425 16.229 16.750 1.00 23.05 ? 310 THR A O 1 ATOM 2310 C CB . THR A 1 310 ? 45.409 16.464 18.237 1.00 17.93 ? 310 THR A CB 1 ATOM 2311 O OG1 . THR A 1 310 ? 44.444 17.154 19.030 1.00 19.73 ? 310 THR A OG1 1 ATOM 2312 C CG2 . THR A 1 310 ? 46.682 17.287 18.201 1.00 17.98 ? 310 THR A CG2 1 ATOM 2313 N N . GLY A 1 311 ? 43.489 14.350 17.243 1.00 17.11 ? 311 GLY A N 1 ATOM 2314 C CA . GLY A 1 311 ? 42.176 13.722 17.392 1.00 14.16 ? 311 GLY A CA 1 ATOM 2315 C C . GLY A 1 311 ? 42.367 12.359 18.051 1.00 17.63 ? 311 GLY A C 1 ATOM 2316 O O . GLY A 1 311 ? 43.499 12.063 18.445 1.00 16.48 ? 311 GLY A O 1 ATOM 2317 N N . PRO A 1 312 ? 41.291 11.624 18.289 1.00 16.56 ? 312 PRO A N 1 ATOM 2318 C CA . PRO A 1 312 ? 41.348 10.353 19.024 1.00 27.81 ? 312 PRO A CA 1 ATOM 2319 C C . PRO A 1 312 ? 42.257 9.323 18.401 1.00 16.40 ? 312 PRO A C 1 ATOM 2320 O O . PRO A 1 312 ? 42.845 8.457 19.066 1.00 21.65 ? 312 PRO A O 1 ATOM 2321 C CB . PRO A 1 312 ? 39.899 9.849 19.042 1.00 21.31 ? 312 PRO A CB 1 ATOM 2322 C CG . PRO A 1 312 ? 39.117 11.121 18.912 1.00 28.90 ? 312 PRO A CG 1 ATOM 2323 C CD . PRO A 1 312 ? 39.906 12.021 17.998 1.00 18.92 ? 312 PRO A CD 1 ATOM 2324 N N . GLN A 1 313 ? 42.503 9.441 17.095 1.00 17.73 ? 313 GLN A N 1 ATOM 2325 C CA . GLN A 1 313 ? 43.429 8.498 16.472 1.00 15.59 ? 313 GLN A CA 1 ATOM 2326 C C . GLN A 1 313 ? 44.879 8.752 16.902 1.00 17.54 ? 313 GLN A C 1 ATOM 2327 O O . GLN A 1 313 ? 45.745 7.948 16.566 1.00 21.03 ? 313 GLN A O 1 ATOM 2328 C CB . GLN A 1 313 ? 43.369 8.690 14.943 1.00 20.80 ? 313 GLN A CB 1 ATOM 2329 C CG . GLN A 1 313 ? 43.927 10.037 14.502 1.00 24.26 ? 313 GLN A CG 1 ATOM 2330 C CD . GLN A 1 313 ? 42.911 11.156 14.451 1.00 30.21 ? 313 GLN A CD 1 ATOM 2331 O OE1 . GLN A 1 313 ? 41.861 11.145 15.092 1.00 22.53 ? 313 GLN A OE1 1 ATOM 2332 N NE2 . GLN A 1 313 ? 43.190 12.193 13.653 1.00 46.62 ? 313 GLN A NE2 1 ATOM 2333 N N . ASP A 1 314 ? 45.146 9.896 17.540 1.00 16.64 ? 314 ASP A N 1 ATOM 2334 C CA . ASP A 1 314 ? 46.521 10.220 17.954 1.00 17.71 ? 314 ASP A CA 1 ATOM 2335 C C . ASP A 1 314 ? 46.782 9.761 19.392 1.00 24.68 ? 314 ASP A C 1 ATOM 2336 O O . ASP A 1 314 ? 47.897 9.894 19.905 1.00 18.77 ? 314 ASP A O 1 ATOM 2337 C CB . ASP A 1 314 ? 46.733 11.728 17.852 1.00 14.54 ? 314 ASP A CB 1 ATOM 2338 C CG . ASP A 1 314 ? 46.556 12.218 16.421 1.00 15.81 ? 314 ASP A CG 1 ATOM 2339 O OD1 . ASP A 1 314 ? 45.913 13.269 16.260 1.00 23.41 ? 314 ASP A OD1 1 ATOM 2340 O OD2 . ASP A 1 314 ? 47.021 11.571 15.471 1.00 19.72 ? 314 ASP A OD2 1 ATOM 2341 N N . LEU A 1 315 ? 45.772 9.201 20.056 1.00 17.53 ? 315 LEU A N 1 ATOM 2342 C CA . LEU A 1 315 ? 45.950 8.761 21.438 1.00 16.02 ? 315 LEU A CA 1 ATOM 2343 C C . LEU A 1 315 ? 46.938 7.621 21.591 1.00 22.29 ? 315 LEU A C 1 ATOM 2344 O O . LEU A 1 315 ? 46.893 6.602 20.890 1.00 19.13 ? 315 LEU A O 1 ATOM 2345 C CB . LEU A 1 315 ? 44.606 8.360 22.075 1.00 16.73 ? 315 LEU A CB 1 ATOM 2346 C CG . LEU A 1 315 ? 43.673 9.548 22.358 1.00 15.79 ? 315 LEU A CG 1 ATOM 2347 C CD1 . LEU A 1 315 ? 42.258 9.075 22.644 1.00 27.31 ? 315 LEU A CD1 1 ATOM 2348 C CD2 . LEU A 1 315 ? 44.175 10.407 23.509 1.00 22.39 ? 315 LEU A CD2 1 ATOM 2349 N N . GLU A 1 316 ? 47.744 7.713 22.656 1.00 17.05 ? 316 GLU A N 1 ATOM 2350 C CA . GLU A 1 316 ? 48.596 6.569 23.019 1.00 14.88 ? 316 GLU A CA 1 ATOM 2351 C C . GLU A 1 316 ? 48.179 6.122 24.413 1.00 22.12 ? 316 GLU A C 1 ATOM 2352 O O . GLU A 1 316 ? 48.652 6.694 25.407 1.00 20.19 ? 316 GLU A O 1 ATOM 2353 C CB . GLU A 1 316 ? 50.078 6.997 23.043 1.00 18.42 ? 316 GLU A CB 1 ATOM 2354 C CG . GLU A 1 316 ? 50.567 7.632 21.760 1.00 20.59 ? 316 GLU A CG 1 ATOM 2355 C CD . GLU A 1 316 ? 52.028 8.011 21.719 1.00 27.04 ? 316 GLU A CD 1 ATOM 2356 O OE1 . GLU A 1 316 ? 52.531 8.784 22.564 1.00 20.44 ? 316 GLU A OE1 1 ATOM 2357 O OE2 . GLU A 1 316 ? 52.698 7.590 20.749 1.00 37.62 ? 316 GLU A OE2 1 ATOM 2358 N N . LEU A 1 317 ? 47.207 5.212 24.475 1.00 19.81 ? 317 LEU A N 1 ATOM 2359 C CA . LEU A 1 317 ? 46.545 4.903 25.728 1.00 11.89 ? 317 LEU A CA 1 ATOM 2360 C C . LEU A 1 317 ? 47.232 3.777 26.514 1.00 16.09 ? 317 LEU A C 1 ATOM 2361 O O . LEU A 1 317 ? 47.742 2.831 25.913 1.00 18.81 ? 317 LEU A O 1 ATOM 2362 C CB . LEU A 1 317 ? 45.105 4.483 25.465 1.00 13.56 ? 317 LEU A CB 1 ATOM 2363 C CG . LEU A 1 317 ? 44.207 5.547 24.844 1.00 17.33 ? 317 LEU A CG 1 ATOM 2364 C CD1 . LEU A 1 317 ? 42.797 5.006 24.700 1.00 18.36 ? 317 LEU A CD1 1 ATOM 2365 C CD2 . LEU A 1 317 ? 44.226 6.784 25.727 1.00 16.85 ? 317 LEU A CD2 1 ATOM 2366 N N . SER A 1 318 ? 47.166 3.875 27.838 1.00 15.72 ? 318 SER A N 1 ATOM 2367 C CA . SER A 1 318 ? 47.869 2.961 28.717 1.00 17.28 ? 318 SER A CA 1 ATOM 2368 C C . SER A 1 318 ? 47.093 2.496 29.929 1.00 21.54 ? 318 SER A C 1 ATOM 2369 O O . SER A 1 318 ? 47.701 1.961 30.871 1.00 25.16 ? 318 SER A O 1 ATOM 2370 C CB . SER A 1 318 ? 49.196 3.605 29.165 1.00 16.67 ? 318 SER A CB 1 ATOM 2371 O OG . SER A 1 318 ? 50.033 3.812 28.036 1.00 16.65 ? 318 SER A OG 1 ATOM 2372 N N . CYS A 1 319 ? 45.788 2.671 29.964 1.00 15.41 ? 319 CYS A N 1 ATOM 2373 C CA . CYS A 1 319 ? 44.962 2.234 31.084 1.00 14.41 ? 319 CYS A CA 1 ATOM 2374 C C . CYS A 1 319 ? 43.912 1.238 30.585 1.00 16.60 ? 319 CYS A C 1 ATOM 2375 O O . CYS A 1 319 ? 42.915 1.661 30.021 1.00 18.09 ? 319 CYS A O 1 ATOM 2376 C CB . CYS A 1 319 ? 44.255 3.420 31.735 1.00 20.33 ? 319 CYS A CB 1 ATOM 2377 S SG . CYS A 1 319 ? 43.129 2.933 33.054 1.00 18.63 ? 319 CYS A SG 1 ATOM 2378 N N . PRO A 1 320 ? 44.133 -0.046 30.813 1.00 16.45 ? 320 PRO A N 1 ATOM 2379 C CA . PRO A 1 320 ? 43.223 -1.068 30.283 1.00 17.01 ? 320 PRO A CA 1 ATOM 2380 C C . PRO A 1 320 ? 41.836 -1.085 30.911 1.00 23.10 ? 320 PRO A C 1 ATOM 2381 O O . PRO A 1 320 ? 40.912 -1.707 30.357 1.00 26.20 ? 320 PRO A O 1 ATOM 2382 C CB . PRO A 1 320 ? 43.936 -2.373 30.616 1.00 19.29 ? 320 PRO A CB 1 ATOM 2383 C CG . PRO A 1 320 ? 45.317 -2.025 31.038 1.00 34.90 ? 320 PRO A CG 1 ATOM 2384 C CD . PRO A 1 320 ? 45.238 -0.630 31.598 1.00 20.00 ? 320 PRO A CD 1 ATOM 2385 N N . SER A 1 321 ? 41.657 -0.530 32.098 1.00 19.29 ? 321 SER A N 1 ATOM 2386 C CA . SER A 1 321 ? 40.451 -0.764 32.880 1.00 19.18 ? 321 SER A CA 1 ATOM 2387 C C . SER A 1 321 ? 39.514 0.427 32.933 1.00 23.24 ? 321 SER A C 1 ATOM 2388 O O . SER A 1 321 ? 38.533 0.401 33.679 1.00 27.74 ? 321 SER A O 1 ATOM 2389 C CB . SER A 1 321 ? 40.833 -1.138 34.320 1.00 26.21 ? 321 SER A CB 1 ATOM 2390 O OG . SER A 1 321 ? 41.723 -0.172 34.876 1.00 30.10 ? 321 SER A OG 1 ATOM 2391 N N . GLU A 1 322 ? 39.818 1.495 32.202 1.00 20.67 ? 322 GLU A N 1 ATOM 2392 C CA . GLU A 1 322 ? 38.938 2.655 32.249 1.00 20.85 ? 322 GLU A CA 1 ATOM 2393 C C . GLU A 1 322 ? 38.700 3.168 30.834 1.00 16.35 ? 322 GLU A C 1 ATOM 2394 O O . GLU A 1 322 ? 39.670 3.288 30.081 1.00 18.15 ? 322 GLU A O 1 ATOM 2395 C CB . GLU A 1 322 ? 39.567 3.761 33.108 1.00 23.92 ? 322 GLU A CB 1 ATOM 2396 C CG . GLU A 1 322 ? 39.801 3.296 34.533 1.00 24.32 ? 322 GLU A CG 1 ATOM 2397 C CD . GLU A 1 322 ? 40.082 4.389 35.537 1.00 56.16 ? 322 GLU A CD 1 ATOM 2398 O OE1 . GLU A 1 322 ? 40.515 4.031 36.660 1.00 36.27 ? 322 GLU A OE1 1 ATOM 2399 O OE2 . GLU A 1 322 ? 39.916 5.577 35.189 1.00 62.79 ? 322 GLU A OE2 1 ATOM 2400 N N . ARG A 1 323 ? 37.451 3.478 30.511 1.00 21.19 ? 323 ARG A N 1 ATOM 2401 C CA . ARG A 1 323 ? 37.186 3.937 29.129 1.00 23.78 ? 323 ARG A CA 1 ATOM 2402 C C . ARG A 1 323 ? 37.644 5.379 28.907 1.00 21.77 ? 323 ARG A C 1 ATOM 2403 O O . ARG A 1 323 ? 37.322 6.244 29.723 1.00 20.77 ? 323 ARG A O 1 ATOM 2404 C CB . ARG A 1 323 ? 35.669 3.902 28.886 1.00 32.05 ? 323 ARG A CB 1 ATOM 2405 C CG . ARG A 1 323 ? 35.252 4.103 27.439 1.00 28.70 ? 323 ARG A CG 1 ATOM 2406 C CD . ARG A 1 323 ? 33.734 4.150 27.357 1.00 38.89 ? 323 ARG A CD 1 ATOM 2407 N NE . ARG A 1 323 ? 33.090 2.843 27.540 1.00 52.45 ? 323 ARG A NE 1 ATOM 2408 C CZ . ARG A 1 323 ? 31.961 2.729 28.234 1.00 24.59 ? 323 ARG A CZ 1 ATOM 2409 N NH1 . ARG A 1 323 ? 31.447 3.858 28.746 1.00 65.11 ? 323 ARG A NH1 1 ATOM 2410 N NH2 . ARG A 1 323 ? 31.305 1.598 28.442 1.00 48.49 ? 323 ARG A NH2 1 ATOM 2411 N N . PHE A 1 324 ? 38.347 5.657 27.816 1.00 23.00 ? 324 PHE A N 1 ATOM 2412 C CA . PHE A 1 324 ? 38.732 7.044 27.527 1.00 19.07 ? 324 PHE A CA 1 ATOM 2413 C C . PHE A 1 324 ? 37.491 7.812 27.084 1.00 22.84 ? 324 PHE A C 1 ATOM 2414 O O . PHE A 1 324 ? 36.715 7.290 26.286 1.00 25.79 ? 324 PHE A O 1 ATOM 2415 C CB . PHE A 1 324 ? 39.777 7.072 26.418 1.00 22.39 ? 324 PHE A CB 1 ATOM 2416 C CG . PHE A 1 324 ? 40.449 8.432 26.298 1.00 20.08 ? 324 PHE A CG 1 ATOM 2417 C CD1 . PHE A 1 324 ? 39.941 9.384 25.432 1.00 20.74 ? 324 PHE A CD1 1 ATOM 2418 C CD2 . PHE A 1 324 ? 41.575 8.717 27.064 1.00 22.53 ? 324 PHE A CD2 1 ATOM 2419 C CE1 . PHE A 1 324 ? 40.559 10.619 25.309 1.00 22.49 ? 324 PHE A CE1 1 ATOM 2420 C CE2 . PHE A 1 324 ? 42.184 9.953 26.966 1.00 25.93 ? 324 PHE A CE2 1 ATOM 2421 C CZ . PHE A 1 324 ? 41.646 10.917 26.123 1.00 31.41 ? 324 PHE A CZ 1 ATOM 2422 N N . PRO A 1 325 ? 37.252 9.000 27.612 1.00 17.26 ? 325 PRO A N 1 ATOM 2423 C CA . PRO A 1 325 ? 36.015 9.719 27.314 1.00 19.66 ? 325 PRO A CA 1 ATOM 2424 C C . PRO A 1 325 ? 35.897 10.132 25.848 1.00 20.75 ? 325 PRO A C 1 ATOM 2425 O O . PRO A 1 325 ? 36.900 10.252 25.144 1.00 20.53 ? 325 PRO A O 1 ATOM 2426 C CB . PRO A 1 325 ? 36.047 10.925 28.252 1.00 20.15 ? 325 PRO A CB 1 ATOM 2427 C CG . PRO A 1 325 ? 37.512 11.135 28.519 1.00 18.18 ? 325 PRO A CG 1 ATOM 2428 C CD . PRO A 1 325 ? 38.095 9.737 28.577 1.00 20.38 ? 325 PRO A CD 1 ATOM 2429 N N . THR A 1 326 ? 34.631 10.314 25.448 1.00 21.36 ? 326 THR A N 1 ATOM 2430 C CA . THR A 1 326 ? 34.287 10.889 24.151 1.00 17.94 ? 326 THR A CA 1 ATOM 2431 C C . THR A 1 326 ? 34.422 12.411 24.204 1.00 16.07 ? 326 THR A C 1 ATOM 2432 O O . THR A 1 326 ? 33.639 13.058 24.902 1.00 21.32 ? 326 THR A O 1 ATOM 2433 C CB . THR A 1 326 ? 32.836 10.542 23.737 1.00 30.26 ? 326 THR A CB 1 ATOM 2434 O OG1 . THR A 1 326 ? 32.717 9.115 23.657 1.00 29.36 ? 326 THR A OG1 1 ATOM 2435 C CG2 . THR A 1 326 ? 32.534 11.035 22.326 1.00 31.00 ? 326 THR A CG2 1 ATOM 2436 N N . LEU A 1 327 ? 35.360 12.943 23.425 1.00 15.12 ? 327 LEU A N 1 ATOM 2437 C CA . LEU A 1 327 ? 35.594 14.384 23.411 1.00 22.73 ? 327 LEU A CA 1 ATOM 2438 C C . LEU A 1 327 ? 35.415 14.949 22.004 1.00 19.91 ? 327 LEU A C 1 ATOM 2439 O O . LEU A 1 327 ? 35.705 14.239 21.045 1.00 22.69 ? 327 LEU A O 1 ATOM 2440 C CB . LEU A 1 327 ? 37.002 14.694 23.923 1.00 19.86 ? 327 LEU A CB 1 ATOM 2441 C CG . LEU A 1 327 ? 37.369 14.116 25.291 1.00 18.31 ? 327 LEU A CG 1 ATOM 2442 C CD1 . LEU A 1 327 ? 38.812 14.524 25.619 1.00 20.61 ? 327 LEU A CD1 1 ATOM 2443 C CD2 . LEU A 1 327 ? 36.413 14.587 26.361 1.00 17.02 ? 327 LEU A CD2 1 ATOM 2444 N N . THR A 1 328 ? 35.048 16.220 21.884 1.00 16.73 ? 328 THR A N 1 ATOM 2445 C CA . THR A 1 328 ? 35.030 16.836 20.551 1.00 18.58 ? 328 THR A CA 1 ATOM 2446 C C . THR A 1 328 ? 36.414 17.370 20.191 1.00 25.79 ? 328 THR A C 1 ATOM 2447 O O . THR A 1 328 ? 37.271 17.538 21.057 1.00 18.73 ? 328 THR A O 1 ATOM 2448 C CB . THR A 1 328 ? 34.043 18.020 20.522 1.00 23.33 ? 328 THR A CB 1 ATOM 2449 O OG1 . THR A 1 328 ? 34.453 18.967 21.533 1.00 22.67 ? 328 THR A OG1 1 ATOM 2450 C CG2 . THR A 1 328 ? 32.655 17.522 20.913 1.00 22.51 ? 328 THR A CG2 1 ATOM 2451 N N . THR A 1 329 ? 36.591 17.750 18.928 1.00 22.15 ? 329 THR A N 1 ATOM 2452 C CA . THR A 1 329 ? 37.847 18.306 18.449 1.00 19.91 ? 329 THR A CA 1 ATOM 2453 C C . THR A 1 329 ? 37.616 19.740 17.970 1.00 19.39 ? 329 THR A C 1 ATOM 2454 O O . THR A 1 329 ? 36.618 20.015 17.305 1.00 21.67 ? 329 THR A O 1 ATOM 2455 C CB . THR A 1 329 ? 38.393 17.495 17.269 1.00 18.62 ? 329 THR A CB 1 ATOM 2456 O OG1 . THR A 1 329 ? 38.635 16.135 17.659 1.00 21.77 ? 329 THR A OG1 1 ATOM 2457 C CG2 . THR A 1 329 ? 39.703 18.083 16.761 1.00 19.63 ? 329 THR A CG2 1 ATOM 2458 N N . GLN A 1 330 ? 38.545 20.634 18.299 1.00 18.23 ? 330 GLN A N 1 ATOM 2459 C CA . GLN A 1 330 ? 38.405 21.997 17.783 1.00 18.94 ? 330 GLN A CA 1 ATOM 2460 C C . GLN A 1 330 ? 38.632 21.983 16.276 1.00 27.61 ? 330 GLN A C 1 ATOM 2461 O O . GLN A 1 330 ? 39.481 21.242 15.752 1.00 23.51 ? 330 GLN A O 1 ATOM 2462 C CB . GLN A 1 330 ? 39.395 22.923 18.485 1.00 33.05 ? 330 GLN A CB 1 ATOM 2463 C CG . GLN A 1 330 ? 39.021 23.068 19.957 1.00 71.04 ? 330 GLN A CG 1 ATOM 2464 C CD . GLN A 1 330 ? 39.134 24.498 20.446 1.00 77.53 ? 330 GLN A CD 1 ATOM 2465 O OE1 . GLN A 1 330 ? 38.353 25.374 20.077 1.00 29.44 ? 330 GLN A OE1 1 ATOM 2466 N NE2 . GLN A 1 330 ? 40.133 24.681 21.301 1.00 44.59 ? 330 GLN A NE2 1 ATOM 2467 N N . PRO A 1 331 ? 37.764 22.712 15.576 1.00 26.05 ? 331 PRO A N 1 ATOM 2468 C CA . PRO A 1 331 ? 37.835 22.711 14.114 1.00 38.41 ? 331 PRO A CA 1 ATOM 2469 C C . PRO A 1 331 ? 39.152 23.328 13.641 1.00 30.74 ? 331 PRO A C 1 ATOM 2470 O O . PRO A 1 331 ? 39.728 24.145 14.358 1.00 26.16 ? 331 PRO A O 1 ATOM 2471 C CB . PRO A 1 331 ? 36.619 23.519 13.681 1.00 41.20 ? 331 PRO A CB 1 ATOM 2472 C CG . PRO A 1 331 ? 36.136 24.249 14.884 1.00 36.55 ? 331 PRO A CG 1 ATOM 2473 C CD . PRO A 1 331 ? 36.648 23.517 16.091 1.00 25.79 ? 331 PRO A CD 1 ATOM 2474 N N . GLY A 1 332 ? 39.585 22.906 12.462 1.00 30.94 ? 332 GLY A N 1 ATOM 2475 C CA . GLY A 1 332 ? 40.754 23.423 11.775 1.00 31.95 ? 332 GLY A CA 1 ATOM 2476 C C . GLY A 1 332 ? 41.688 22.303 11.359 1.00 19.48 ? 332 GLY A C 1 ATOM 2477 O O . GLY A 1 332 ? 41.864 21.349 12.112 1.00 29.37 ? 332 GLY A O 1 ATOM 2478 N N . ALA A 1 333 ? 42.401 22.467 10.244 1.00 30.82 ? 333 ALA A N 1 ATOM 2479 C CA . ALA A 1 333 ? 43.308 21.387 9.839 1.00 35.85 ? 333 ALA A CA 1 ATOM 2480 C C . ALA A 1 333 ? 44.713 21.582 10.375 1.00 28.45 ? 333 ALA A C 1 ATOM 2481 O O . ALA A 1 333 ? 45.516 20.648 10.437 1.00 57.27 ? 333 ALA A O 1 ATOM 2482 C CB . ALA A 1 333 ? 43.321 21.257 8.325 1.00 92.01 ? 333 ALA A CB 1 ATOM 2483 N N . SER A 1 334 ? 45.069 22.780 10.879 1.00 18.50 ? 334 SER A N 1 ATOM 2484 C CA . SER A 1 334 ? 46.456 22.800 11.367 1.00 20.84 ? 334 SER A CA 1 ATOM 2485 C C . SER A 1 334 ? 46.516 23.412 12.757 1.00 27.12 ? 334 SER A C 1 ATOM 2486 O O . SER A 1 334 ? 45.537 24.011 13.212 1.00 23.18 ? 334 SER A O 1 ATOM 2487 C CB . SER A 1 334 ? 47.317 23.566 10.354 1.00 24.93 ? 334 SER A CB 1 ATOM 2488 O OG . SER A 1 334 ? 46.971 24.936 10.404 1.00 22.53 ? 334 SER A OG 1 ATOM 2489 N N . GLN A 1 335 ? 47.611 23.198 13.485 1.00 18.39 ? 335 GLN A N 1 ATOM 2490 C CA . GLN A 1 335 ? 47.685 23.663 14.866 1.00 17.49 ? 335 GLN A CA 1 ATOM 2491 C C . GLN A 1 335 ? 47.516 25.169 15.023 1.00 13.99 ? 335 GLN A C 1 ATOM 2492 O O . GLN A 1 335 ? 48.022 25.996 14.261 1.00 18.46 ? 335 GLN A O 1 ATOM 2493 C CB . GLN A 1 335 ? 49.063 23.254 15.437 1.00 22.19 ? 335 GLN A CB 1 ATOM 2494 C CG . GLN A 1 335 ? 49.171 23.605 16.914 1.00 21.06 ? 335 GLN A CG 1 ATOM 2495 C CD . GLN A 1 335 ? 50.584 23.638 17.453 1.00 20.77 ? 335 GLN A CD 1 ATOM 2496 O OE1 . GLN A 1 335 ? 50.902 24.514 18.278 1.00 27.72 ? 335 GLN A OE1 1 ATOM 2497 N NE2 . GLN A 1 335 ? 51.440 22.721 17.029 1.00 15.55 ? 335 GLN A NE2 1 ATOM 2498 N N . SER A 1 336 ? 46.778 25.565 16.065 1.00 15.06 ? 336 SER A N 1 ATOM 2499 C CA . SER A 1 336 ? 46.711 26.981 16.424 1.00 22.12 ? 336 SER A CA 1 ATOM 2500 C C . SER A 1 336 ? 47.901 27.358 17.300 1.00 21.67 ? 336 SER A C 1 ATOM 2501 O O . SER A 1 336 ? 48.337 26.566 18.145 1.00 24.10 ? 336 SER A O 1 ATOM 2502 C CB . SER A 1 336 ? 45.452 27.280 17.251 1.00 19.50 ? 336 SER A CB 1 ATOM 2503 O OG . SER A 1 336 ? 44.280 27.005 16.483 1.00 25.76 ? 336 SER A OG 1 ATOM 2504 N N . LEU A 1 337 ? 48.410 28.565 17.134 1.00 17.96 ? 337 LEU A N 1 ATOM 2505 C CA . LEU A 1 337 ? 49.456 28.983 18.065 1.00 17.98 ? 337 LEU A CA 1 ATOM 2506 C C . LEU A 1 337 ? 48.910 29.059 19.487 1.00 22.09 ? 337 LEU A C 1 ATOM 2507 O O . LEU A 1 337 ? 47.752 29.412 19.669 1.00 19.90 ? 337 LEU A O 1 ATOM 2508 C CB . LEU A 1 337 ? 49.992 30.359 17.668 1.00 22.17 ? 337 LEU A CB 1 ATOM 2509 C CG . LEU A 1 337 ? 50.715 30.364 16.314 1.00 25.81 ? 337 LEU A CG 1 ATOM 2510 C CD1 . LEU A 1 337 ? 50.989 31.800 15.882 1.00 27.32 ? 337 LEU A CD1 1 ATOM 2511 C CD2 . LEU A 1 337 ? 52.008 29.566 16.435 1.00 23.47 ? 337 LEU A CD2 1 ATOM 2512 N N . ILE A 1 338 ? 49.791 28.772 20.455 1.00 18.09 ? 338 ILE A N 1 ATOM 2513 C CA . ILE A 1 338 ? 49.409 28.934 21.857 1.00 13.52 ? 338 ILE A CA 1 ATOM 2514 C C . ILE A 1 338 ? 49.867 30.318 22.322 1.00 14.08 ? 338 ILE A C 1 ATOM 2515 O O . ILE A 1 338 ? 51.049 30.623 22.264 1.00 16.60 ? 338 ILE A O 1 ATOM 2516 C CB . ILE A 1 338 ? 50.055 27.805 22.684 1.00 15.45 ? 338 ILE A CB 1 ATOM 2517 C CG1 . ILE A 1 338 ? 49.632 26.400 22.239 1.00 17.78 ? 338 ILE A CG1 1 ATOM 2518 C CG2 . ILE A 1 338 ? 49.702 27.978 24.154 1.00 22.40 ? 338 ILE A CG2 1 ATOM 2519 C CD1 . ILE A 1 338 ? 50.450 25.254 22.782 1.00 15.14 ? 338 ILE A CD1 1 ATOM 2520 N N . ALA A 1 339 ? 48.915 31.175 22.669 1.00 15.66 ? 339 ALA A N 1 ATOM 2521 C CA . ALA A 1 339 ? 49.147 32.579 22.981 1.00 12.55 ? 339 ALA A CA 1 ATOM 2522 C C . ALA A 1 339 ? 50.152 32.723 24.121 1.00 17.68 ? 339 ALA A C 1 ATOM 2523 O O . ALA A 1 339 ? 49.996 32.073 25.158 1.00 18.81 ? 339 ALA A O 1 ATOM 2524 C CB . ALA A 1 339 ? 47.832 33.245 23.379 1.00 16.34 ? 339 ALA A CB 1 ATOM 2525 N N . HIS A 1 340 ? 51.131 33.592 23.904 1.00 19.52 ? 340 HIS A N 1 ATOM 2526 C CA . HIS A 1 340 ? 52.140 33.900 24.917 1.00 24.95 ? 340 HIS A CA 1 ATOM 2527 C C . HIS A 1 340 ? 51.559 34.674 26.105 1.00 25.85 ? 340 HIS A C 1 ATOM 2528 O O . HIS A 1 340 ? 52.131 34.636 27.200 1.00 20.15 ? 340 HIS A O 1 ATOM 2529 C CB . HIS A 1 340 ? 53.289 34.702 24.297 1.00 21.47 ? 340 HIS A CB 1 ATOM 2530 C CG . HIS A 1 340 ? 54.428 34.964 25.235 1.00 26.51 ? 340 HIS A CG 1 ATOM 2531 N ND1 . HIS A 1 340 ? 55.226 33.938 25.711 1.00 22.11 ? 340 HIS A ND1 1 ATOM 2532 C CD2 . HIS A 1 340 ? 54.931 36.100 25.773 1.00 26.26 ? 340 HIS A CD2 1 ATOM 2533 C CE1 . HIS A 1 340 ? 56.166 34.430 26.499 1.00 19.40 ? 340 HIS A CE1 1 ATOM 2534 N NE2 . HIS A 1 340 ? 56.020 35.749 26.555 1.00 22.24 ? 340 HIS A NE2 1 ATOM 2535 N N . CYS A 1 341 ? 50.468 35.386 25.885 1.00 21.66 ? 341 CYS A N 1 ATOM 2536 C CA . CYS A 1 341 ? 49.855 36.280 26.871 1.00 22.20 ? 341 CYS A CA 1 ATOM 2537 C C . CYS A 1 341 ? 48.436 35.900 27.225 1.00 22.70 ? 341 CYS A C 1 ATOM 2538 O O . CYS A 1 341 ? 47.644 35.474 26.379 1.00 23.76 ? 341 CYS A O 1 ATOM 2539 C CB . CYS A 1 341 ? 49.883 37.719 26.336 1.00 33.03 ? 341 CYS A CB 1 ATOM 2540 S SG . CYS A 1 341 ? 51.543 38.441 26.207 1.00 27.28 ? 341 CYS A SG 1 ATOM 2541 N N . PRO A 1 342 ? 48.030 36.103 28.472 1.00 22.94 ? 342 PRO A N 1 ATOM 2542 C CA . PRO A 1 342 ? 46.665 35.799 28.907 1.00 24.91 ? 342 PRO A CA 1 ATOM 2543 C C . PRO A 1 342 ? 45.547 36.488 28.137 1.00 26.15 ? 342 PRO A C 1 ATOM 2544 O O . PRO A 1 342 ? 44.448 35.922 27.987 1.00 27.30 ? 342 PRO A O 1 ATOM 2545 C CB . PRO A 1 342 ? 46.651 36.251 30.379 1.00 23.78 ? 342 PRO A CB 1 ATOM 2546 C CG . PRO A 1 342 ? 48.077 36.161 30.794 1.00 25.21 ? 342 PRO A CG 1 ATOM 2547 C CD . PRO A 1 342 ? 48.892 36.557 29.578 1.00 26.72 ? 342 PRO A CD 1 ATOM 2548 N N . ASP A 1 343 ? 45.770 37.681 27.615 1.00 26.30 ? 343 ASP A N 1 ATOM 2549 C CA . ASP A 1 343 ? 44.731 38.373 26.852 1.00 35.95 ? 343 ASP A CA 1 ATOM 2550 C C . ASP A 1 343 ? 44.861 38.157 25.351 1.00 44.31 ? 343 ASP A C 1 ATOM 2551 O O . ASP A 1 343 ? 44.158 38.792 24.556 1.00 35.70 ? 343 ASP A O 1 ATOM 2552 C CB . ASP A 1 343 ? 44.764 39.879 27.116 1.00 25.61 ? 343 ASP A CB 1 ATOM 2553 C CG . ASP A 1 343 ? 46.060 40.502 26.636 1.00 35.58 ? 343 ASP A CG 1 ATOM 2554 O OD1 . ASP A 1 343 ? 47.022 39.763 26.342 1.00 42.62 ? 343 ASP A OD1 1 ATOM 2555 O OD2 . ASP A 1 343 ? 46.098 41.744 26.536 1.00 70.85 ? 343 ASP A OD2 1 ATOM 2556 N N . GLY A 1 344 ? 45.733 37.238 24.958 1.00 38.18 ? 344 GLY A N 1 ATOM 2557 C CA . GLY A 1 344 ? 45.751 36.753 23.590 1.00 49.91 ? 344 GLY A CA 1 ATOM 2558 C C . GLY A 1 344 ? 46.949 37.232 22.804 1.00 55.45 ? 344 GLY A C 1 ATOM 2559 O O . GLY A 1 344 ? 47.328 36.539 21.857 1.00 68.51 ? 344 GLY A O 1 ATOM 2560 N N . SER A 1 345 ? 47.516 38.372 23.211 1.00 42.63 ? 345 SER A N 1 ATOM 2561 C CA . SER A 1 345 ? 48.726 38.859 22.577 1.00 64.04 ? 345 SER A CA 1 ATOM 2562 C C . SER A 1 345 ? 49.977 38.001 22.816 1.00 73.61 ? 345 SER A C 1 ATOM 2563 O O . SER A 1 345 ? 49.963 36.791 23.073 1.00 29.17 ? 345 SER A O 1 ATOM 2564 C CB . SER A 1 345 ? 49.087 40.281 23.014 1.00 46.10 ? 345 SER A CB 1 ATOM 2565 O OG . SER A 1 345 ? 48.314 40.671 24.137 1.00 73.02 ? 345 SER A OG 1 ATOM 2566 N N . MET A 1 346 ? 51.061 38.759 22.670 1.00 52.50 ? 346 MET A N 1 ATOM 2567 C CA . MET A 1 346 ? 52.437 38.291 22.750 1.00 54.78 ? 346 MET A CA 1 ATOM 2568 C C . MET A 1 346 ? 53.298 39.321 23.493 1.00 72.54 ? 346 MET A C 1 ATOM 2569 O O . MET A 1 346 ? 54.525 39.183 23.535 1.00 55.70 ? 346 MET A O 1 ATOM 2570 C CB . MET A 1 346 ? 53.015 38.086 21.355 1.00 60.53 ? 346 MET A CB 1 ATOM 2571 C CG . MET A 1 346 ? 52.591 36.900 20.514 1.00 24.13 ? 346 MET A CG 1 ATOM 2572 S SD . MET A 1 346 ? 53.839 36.577 19.221 1.00 78.06 ? 346 MET A SD 1 ATOM 2573 C CE . MET A 1 346 ? 52.882 35.595 18.067 1.00 89.42 ? 346 MET A CE 1 ATOM 2574 N N . SER A 1 347 ? 52.647 40.346 24.037 1.00 91.68 ? 347 SER A N 1 ATOM 2575 C CA . SER A 1 347 ? 53.312 41.422 24.768 1.00 98.08 ? 347 SER A CA 1 ATOM 2576 C C . SER A 1 347 ? 52.738 41.691 26.150 1.00 76.59 ? 347 SER A C 1 ATOM 2577 O O . SER A 1 347 ? 51.806 42.472 26.341 1.00 37.32 ? 347 SER A O 1 ATOM 2578 C CB . SER A 1 347 ? 53.245 42.682 23.890 1.00 102.95 ? 347 SER A CB 1 ATOM 2579 O OG . SER A 1 347 ? 53.030 42.288 22.539 1.00 96.26 ? 347 SER A OG 1 ATOM 2580 N N . CYS A 1 348 ? 53.294 41.065 27.186 1.00 41.72 ? 348 CYS A N 1 ATOM 2581 C CA . CYS A 1 348 ? 52.791 41.122 28.545 1.00 22.45 ? 348 CYS A CA 1 ATOM 2582 C C . CYS A 1 348 ? 53.903 40.802 29.550 1.00 28.34 ? 348 CYS A C 1 ATOM 2583 O O . CYS A 1 348 ? 53.826 39.811 30.263 1.00 20.92 ? 348 CYS A O 1 ATOM 2584 C CB . CYS A 1 348 ? 51.668 40.105 28.748 1.00 21.19 ? 348 CYS A CB 1 ATOM 2585 S SG . CYS A 1 348 ? 52.181 38.473 28.144 1.00 27.30 ? 348 CYS A SG 1 ATOM 2586 N N . PRO A 1 349 ? 54.858 41.712 29.661 1.00 40.82 ? 349 PRO A N 1 ATOM 2587 C CA . PRO A 1 349 ? 56.078 41.489 30.446 1.00 41.36 ? 349 PRO A CA 1 ATOM 2588 C C . PRO A 1 349 ? 55.793 41.427 31.942 1.00 27.24 ? 349 PRO A C 1 ATOM 2589 O O . PRO A 1 349 ? 54.991 42.201 32.472 1.00 43.57 ? 349 PRO A O 1 ATOM 2590 C CB . PRO A 1 349 ? 56.926 42.722 30.108 1.00 44.40 ? 349 PRO A CB 1 ATOM 2591 C CG . PRO A 1 349 ? 55.910 43.791 29.851 1.00 55.62 ? 349 PRO A CG 1 ATOM 2592 C CD . PRO A 1 349 ? 54.757 43.103 29.175 1.00 44.74 ? 349 PRO A CD 1 ATOM 2593 N N . GLY A 1 350 ? 56.360 40.447 32.633 1.00 30.91 ? 350 GLY A N 1 ATOM 2594 C CA . GLY A 1 350 ? 56.067 40.286 34.054 1.00 25.23 ? 350 GLY A CA 1 ATOM 2595 C C . GLY A 1 350 ? 56.958 41.206 34.883 1.00 21.66 ? 350 GLY A C 1 ATOM 2596 O O . GLY A 1 350 ? 58.130 41.344 34.523 1.00 22.47 ? 350 GLY A O 1 ATOM 2597 N N . VAL A 1 351 ? 56.381 41.774 35.928 1.00 18.12 ? 351 VAL A N 1 ATOM 2598 C CA . VAL A 1 351 ? 57.176 42.588 36.879 1.00 14.41 ? 351 VAL A CA 1 ATOM 2599 C C . VAL A 1 351 ? 58.268 41.681 37.435 1.00 16.58 ? 351 VAL A C 1 ATOM 2600 O O . VAL A 1 351 ? 57.960 40.531 37.785 1.00 15.05 ? 351 VAL A O 1 ATOM 2601 C CB . VAL A 1 351 ? 56.251 43.049 38.026 1.00 17.52 ? 351 VAL A CB 1 ATOM 2602 C CG1 . VAL A 1 351 ? 57.036 43.699 39.154 1.00 18.78 ? 351 VAL A CG1 1 ATOM 2603 C CG2 . VAL A 1 351 ? 55.219 44.032 37.449 1.00 19.40 ? 351 VAL A CG2 1 ATOM 2604 N N . GLN A 1 352 ? 59.504 42.162 37.456 1.00 16.19 ? 352 GLN A N 1 ATOM 2605 C CA . GLN A 1 352 ? 60.598 41.364 38.028 1.00 13.81 ? 352 GLN A CA 1 ATOM 2606 C C . GLN A 1 352 ? 61.514 42.276 38.840 1.00 17.44 ? 352 GLN A C 1 ATOM 2607 O O . GLN A 1 352 ? 61.925 43.332 38.340 1.00 16.30 ? 352 GLN A O 1 ATOM 2608 C CB . GLN A 1 352 ? 61.377 40.640 36.937 1.00 12.54 ? 352 GLN A CB 1 ATOM 2609 C CG . GLN A 1 352 ? 62.553 39.808 37.445 1.00 15.07 ? 352 GLN A CG 1 ATOM 2610 C CD . GLN A 1 352 ? 62.074 38.719 38.380 1.00 21.93 ? 352 GLN A CD 1 ATOM 2611 O OE1 . GLN A 1 352 ? 62.509 38.613 39.540 1.00 22.18 ? 352 GLN A OE1 1 ATOM 2612 N NE2 . GLN A 1 352 ? 61.102 37.953 37.907 1.00 13.70 ? 352 GLN A NE2 1 ATOM 2613 N N . PHE A 1 353 ? 61.739 41.877 40.087 1.00 16.72 ? 353 PHE A N 1 ATOM 2614 C CA . PHE A 1 353 ? 62.689 42.570 40.959 1.00 20.07 ? 353 PHE A CA 1 ATOM 2615 C C . PHE A 1 353 ? 64.065 41.903 40.916 1.00 15.38 ? 353 PHE A C 1 ATOM 2616 O O . PHE A 1 353 ? 64.161 40.677 40.794 1.00 17.93 ? 353 PHE A O 1 ATOM 2617 C CB . PHE A 1 353 ? 62.166 42.525 42.408 1.00 14.63 ? 353 PHE A CB 1 ATOM 2618 C CG . PHE A 1 353 ? 60.897 43.338 42.593 1.00 16.02 ? 353 PHE A CG 1 ATOM 2619 C CD1 . PHE A 1 353 ? 60.921 44.716 42.552 1.00 17.93 ? 353 PHE A CD1 1 ATOM 2620 C CD2 . PHE A 1 353 ? 59.681 42.722 42.803 1.00 25.67 ? 353 PHE A CD2 1 ATOM 2621 C CE1 . PHE A 1 353 ? 59.773 45.452 42.750 1.00 22.16 ? 353 PHE A CE1 1 ATOM 2622 C CE2 . PHE A 1 353 ? 58.518 43.453 43.000 1.00 23.90 ? 353 PHE A CE2 1 ATOM 2623 C CZ . PHE A 1 353 ? 58.553 44.837 42.965 1.00 20.69 ? 353 PHE A CZ 1 ATOM 2624 N N . ASN A 1 354 ? 65.120 42.697 40.964 1.00 17.19 ? 354 ASN A N 1 ATOM 2625 C CA . ASN A 1 354 ? 66.473 42.159 41.106 1.00 14.75 ? 354 ASN A CA 1 ATOM 2626 C C . ASN A 1 354 ? 66.602 41.725 42.563 1.00 17.71 ? 354 ASN A C 1 ATOM 2627 O O . ASN A 1 354 ? 65.878 42.247 43.406 1.00 18.02 ? 354 ASN A O 1 ATOM 2628 C CB . ASN A 1 354 ? 67.538 43.238 40.886 1.00 26.15 ? 354 ASN A CB 1 ATOM 2629 C CG . ASN A 1 354 ? 67.449 43.822 39.483 1.00 30.77 ? 354 ASN A CG 1 ATOM 2630 O OD1 . ASN A 1 354 ? 67.524 45.036 39.304 1.00 52.32 ? 354 ASN A OD1 1 ATOM 2631 N ND2 . ASN A 1 354 ? 67.313 42.915 38.529 1.00 29.70 ? 354 ASN A ND2 1 ATOM 2632 N N . GLY A 1 355 ? 67.524 40.792 42.834 1.00 22.54 ? 355 GLY A N 1 ATOM 2633 C CA . GLY A 1 355 ? 67.625 40.328 44.222 1.00 15.86 ? 355 GLY A CA 1 ATOM 2634 C C . GLY A 1 355 ? 68.819 39.402 44.343 1.00 19.30 ? 355 GLY A C 1 ATOM 2635 O O . GLY A 1 355 ? 69.588 39.244 43.396 1.00 21.88 ? 355 GLY A O 1 ATOM 2636 N N . PRO A 1 356 ? 69.011 38.830 45.525 1.00 19.44 ? 356 PRO A N 1 ATOM 2637 C CA . PRO A 1 356 ? 70.248 38.089 45.793 1.00 19.81 ? 356 PRO A CA 1 ATOM 2638 C C . PRO A 1 356 ? 70.276 36.689 45.198 1.00 31.04 ? 356 PRO A C 1 ATOM 2639 O O . PRO A 1 356 ? 71.334 36.056 45.178 1.00 26.97 ? 356 PRO A O 1 ATOM 2640 C CB . PRO A 1 356 ? 70.242 38.045 47.320 1.00 19.68 ? 356 PRO A CB 1 ATOM 2641 C CG . PRO A 1 356 ? 68.792 38.044 47.694 1.00 23.52 ? 356 PRO A CG 1 ATOM 2642 C CD . PRO A 1 356 ? 68.102 38.910 46.673 1.00 18.60 ? 356 PRO A CD 1 ATOM 2643 N N . ALA A 1 357 ? 69.150 36.158 44.710 1.00 19.05 ? 357 ALA A N 1 ATOM 2644 C CA . ALA A 1 357 ? 69.164 34.807 44.164 1.00 19.03 ? 357 ALA A CA 1 ATOM 2645 C C . ALA A 1 357 ? 69.664 34.747 42.722 1.00 17.81 ? 357 ALA A C 1 ATOM 2646 O O . ALA A 1 357 ? 69.507 35.806 42.059 1.00 22.65 ? 357 ALA A O 1 ATOM 2647 C CB . ALA A 1 357 ? 67.781 34.178 44.274 1.00 23.98 ? 357 ALA A CB 1 ATOM 2648 O OXT . ALA A 1 357 ? 70.179 33.746 42.289 1.00 22.28 ? 357 ALA A OXT 1 HETATM 2649 C C1 . NAG B 2 . ? 62.024 36.641 58.808 1.00 18.41 ? 361 NAG A C1 1 HETATM 2650 C C2 . NAG B 2 . ? 61.518 37.973 59.331 1.00 15.80 ? 361 NAG A C2 1 HETATM 2651 C C3 . NAG B 2 . ? 61.991 39.131 58.440 1.00 23.40 ? 361 NAG A C3 1 HETATM 2652 C C4 . NAG B 2 . ? 63.481 38.998 58.132 1.00 18.90 ? 361 NAG A C4 1 HETATM 2653 C C5 . NAG B 2 . ? 63.812 37.603 57.554 1.00 20.22 ? 361 NAG A C5 1 HETATM 2654 C C6 . NAG B 2 . ? 65.296 37.428 57.279 1.00 22.37 ? 361 NAG A C6 1 HETATM 2655 C C7 . NAG B 2 . ? 59.444 37.716 60.567 1.00 25.46 ? 361 NAG A C7 1 HETATM 2656 C C8 . NAG B 2 . ? 57.941 37.529 60.544 1.00 18.23 ? 361 NAG A C8 1 HETATM 2657 N N2 . NAG B 2 . ? 60.061 38.014 59.413 1.00 20.62 ? 361 NAG A N2 1 HETATM 2658 O O3 . NAG B 2 . ? 61.720 40.388 59.033 1.00 22.78 ? 361 NAG A O3 1 HETATM 2659 O O4 . NAG B 2 . ? 63.798 39.934 57.098 1.00 23.20 ? 361 NAG A O4 1 HETATM 2660 O O5 . NAG B 2 . ? 63.427 36.619 58.501 1.00 21.40 ? 361 NAG A O5 1 HETATM 2661 O O6 . NAG B 2 . ? 65.994 37.638 58.491 1.00 23.90 ? 361 NAG A O6 1 HETATM 2662 O O7 . NAG B 2 . ? 60.102 37.520 61.596 1.00 20.46 ? 361 NAG A O7 1 HETATM 2663 C C1 . NAG C 2 . ? 64.344 41.190 57.432 1.00 24.31 ? 362 NAG A C1 1 HETATM 2664 C C2 . NAG C 2 . ? 65.184 41.723 56.260 1.00 24.57 ? 362 NAG A C2 1 HETATM 2665 C C3 . NAG C 2 . ? 65.639 43.147 56.592 1.00 35.12 ? 362 NAG A C3 1 HETATM 2666 C C4 . NAG C 2 . ? 64.434 44.030 56.959 1.00 33.16 ? 362 NAG A C4 1 HETATM 2667 C C5 . NAG C 2 . ? 63.586 43.378 58.059 1.00 26.10 ? 362 NAG A C5 1 HETATM 2668 C C6 . NAG C 2 . ? 62.264 44.062 58.389 1.00 20.97 ? 362 NAG A C6 1 HETATM 2669 C C7 . NAG C 2 . ? 66.695 40.302 54.950 1.00 23.02 ? 362 NAG A C7 1 HETATM 2670 C C8 . NAG C 2 . ? 68.020 39.556 54.914 1.00 22.48 ? 362 NAG A C8 1 HETATM 2671 N N2 . NAG C 2 . ? 66.323 40.832 56.115 1.00 21.57 ? 362 NAG A N2 1 HETATM 2672 O O3 . NAG C 2 . ? 66.347 43.688 55.501 1.00 33.03 ? 362 NAG A O3 1 HETATM 2673 O O4 . NAG C 2 . ? 64.912 45.281 57.434 1.00 34.04 ? 362 NAG A O4 1 HETATM 2674 O O5 . NAG C 2 . ? 63.250 42.042 57.719 1.00 27.52 ? 362 NAG A O5 1 HETATM 2675 O O6 . NAG C 2 . ? 61.643 43.421 59.488 1.00 22.24 ? 362 NAG A O6 1 HETATM 2676 O O7 . NAG C 2 . ? 66.020 40.442 53.931 1.00 20.64 ? 362 NAG A O7 1 HETATM 2677 C C1 . MAN D 3 . ? 43.775 28.068 15.687 1.00 23.69 ? 364 MAN A C1 1 HETATM 2678 C C2 . MAN D 3 . ? 42.323 27.781 15.298 1.00 37.41 ? 364 MAN A C2 1 HETATM 2679 C C3 . MAN D 3 . ? 42.256 26.573 14.351 1.00 33.77 ? 364 MAN A C3 1 HETATM 2680 C C4 . MAN D 3 . ? 43.205 26.762 13.168 1.00 34.01 ? 364 MAN A C4 1 HETATM 2681 C C5 . MAN D 3 . ? 44.632 27.140 13.609 1.00 31.18 ? 364 MAN A C5 1 HETATM 2682 C C6 . MAN D 3 . ? 45.500 27.589 12.423 1.00 35.04 ? 364 MAN A C6 1 HETATM 2683 O O2 . MAN D 3 . ? 41.754 28.907 14.662 1.00 40.67 ? 364 MAN A O2 1 HETATM 2684 O O3 . MAN D 3 . ? 40.930 26.396 13.913 1.00 52.74 ? 364 MAN A O3 1 HETATM 2685 O O4 . MAN D 3 . ? 43.270 25.564 12.425 1.00 37.66 ? 364 MAN A O4 1 HETATM 2686 O O5 . MAN D 3 . ? 44.619 28.208 14.532 1.00 31.08 ? 364 MAN A O5 1 HETATM 2687 O O6 . MAN D 3 . ? 46.853 27.751 12.776 1.00 36.45 ? 364 MAN A O6 1 HETATM 2688 CA CA . CA E 4 . ? 45.786 24.337 31.090 1.00 15.56 ? 371 CA A CA 1 HETATM 2689 CA CA . CA F 4 . ? 62.327 24.603 51.782 1.00 14.37 ? 372 CA A CA 1 HETATM 2690 C CHA . HEM G 5 . ? 57.588 23.997 35.520 1.00 18.00 ? 396 HEM A CHA 1 HETATM 2691 C CHB . HEM G 5 . ? 59.380 19.584 36.321 1.00 20.84 ? 396 HEM A CHB 1 HETATM 2692 C CHC . HEM G 5 . ? 56.102 18.775 39.764 1.00 19.28 ? 396 HEM A CHC 1 HETATM 2693 C CHD . HEM G 5 . ? 54.418 23.284 39.118 1.00 15.65 ? 396 HEM A CHD 1 HETATM 2694 C C1A . HEM G 5 . ? 58.463 22.908 35.520 1.00 21.99 ? 396 HEM A C1A 1 HETATM 2695 C C2A . HEM G 5 . ? 59.633 22.767 34.689 1.00 18.03 ? 396 HEM A C2A 1 HETATM 2696 C C3A . HEM G 5 . ? 60.043 21.481 34.780 1.00 19.07 ? 396 HEM A C3A 1 HETATM 2697 C C4A . HEM G 5 . ? 59.185 20.840 35.746 1.00 16.77 ? 396 HEM A C4A 1 HETATM 2698 C CMA . HEM G 5 . ? 61.359 20.898 34.267 1.00 22.93 ? 396 HEM A CMA 1 HETATM 2699 C CAA . HEM G 5 . ? 60.129 23.817 33.701 1.00 18.11 ? 396 HEM A CAA 1 HETATM 2700 C CBA . HEM G 5 . ? 61.031 24.864 34.348 1.00 22.44 ? 396 HEM A CBA 1 HETATM 2701 C CGA . HEM G 5 . ? 61.835 25.628 33.312 1.00 19.75 ? 396 HEM A CGA 1 HETATM 2702 O O1A . HEM G 5 . ? 62.650 25.038 32.578 1.00 19.03 ? 396 HEM A O1A 1 HETATM 2703 O O2A . HEM G 5 . ? 61.597 26.854 33.202 1.00 21.22 ? 396 HEM A O2A 1 HETATM 2704 C C1B . HEM G 5 . ? 58.567 18.966 37.263 1.00 19.75 ? 396 HEM A C1B 1 HETATM 2705 C C2B . HEM G 5 . ? 58.814 17.630 37.770 1.00 19.00 ? 396 HEM A C2B 1 HETATM 2706 C C3B . HEM G 5 . ? 57.774 17.334 38.588 1.00 16.08 ? 396 HEM A C3B 1 HETATM 2707 C C4B . HEM G 5 . ? 56.972 18.539 38.705 1.00 21.93 ? 396 HEM A C4B 1 HETATM 2708 C CMB . HEM G 5 . ? 59.999 16.770 37.354 1.00 24.26 ? 396 HEM A CMB 1 HETATM 2709 C CAB . HEM G 5 . ? 57.501 16.164 39.267 1.00 19.60 ? 396 HEM A CAB 1 HETATM 2710 C CBB . HEM G 5 . ? 57.857 14.802 38.911 1.00 25.65 ? 396 HEM A CBB 1 HETATM 2711 C C1C . HEM G 5 . ? 55.552 20.036 40.033 1.00 23.48 ? 396 HEM A C1C 1 HETATM 2712 C C2C . HEM G 5 . ? 54.554 20.273 41.053 1.00 19.27 ? 396 HEM A C2C 1 HETATM 2713 C C3C . HEM G 5 . ? 54.128 21.547 40.926 1.00 20.88 ? 396 HEM A C3C 1 HETATM 2714 C C4C . HEM G 5 . ? 54.792 22.089 39.760 1.00 17.79 ? 396 HEM A C4C 1 HETATM 2715 C CMC . HEM G 5 . ? 54.140 19.210 42.065 1.00 19.98 ? 396 HEM A CMC 1 HETATM 2716 C CAC . HEM G 5 . ? 53.403 22.344 41.810 1.00 24.01 ? 396 HEM A CAC 1 HETATM 2717 C CBC . HEM G 5 . ? 52.272 21.929 42.606 1.00 25.49 ? 396 HEM A CBC 1 HETATM 2718 C C1D . HEM G 5 . ? 55.068 23.825 38.017 1.00 13.24 ? 396 HEM A C1D 1 HETATM 2719 C C2D . HEM G 5 . ? 54.789 25.140 37.479 1.00 14.16 ? 396 HEM A C2D 1 HETATM 2720 C C3D . HEM G 5 . ? 55.655 25.322 36.454 1.00 18.36 ? 396 HEM A C3D 1 HETATM 2721 C C4D . HEM G 5 . ? 56.501 24.156 36.365 1.00 18.88 ? 396 HEM A C4D 1 HETATM 2722 C CMD . HEM G 5 . ? 53.736 26.123 37.978 1.00 15.51 ? 396 HEM A CMD 1 HETATM 2723 C CAD . HEM G 5 . ? 55.704 26.528 35.527 1.00 14.64 ? 396 HEM A CAD 1 HETATM 2724 C CBD . HEM G 5 . ? 56.798 27.529 35.880 1.00 25.08 ? 396 HEM A CBD 1 HETATM 2725 C CGD . HEM G 5 . ? 56.776 28.684 34.890 1.00 28.27 ? 396 HEM A CGD 1 HETATM 2726 O O1D . HEM G 5 . ? 57.636 29.568 35.009 1.00 24.40 ? 396 HEM A O1D 1 HETATM 2727 O O2D . HEM G 5 . ? 55.922 28.650 33.972 1.00 21.08 ? 396 HEM A O2D 1 HETATM 2728 N NA . HEM G 5 . ? 58.191 21.704 36.134 1.00 20.76 ? 396 HEM A NA 1 HETATM 2729 N NB . HEM G 5 . ? 57.553 19.560 37.982 1.00 16.17 ? 396 HEM A NB 1 HETATM 2730 N NC . HEM G 5 . ? 55.568 21.108 39.173 1.00 17.67 ? 396 HEM A NC 1 HETATM 2731 N ND . HEM G 5 . ? 56.138 23.258 37.348 1.00 17.34 ? 396 HEM A ND 1 HETATM 2732 FE FE . HEM G 5 . ? 56.802 21.399 37.562 1.00 18.39 ? 396 HEM A FE 1 HETATM 2733 C C1 . GOL H 6 . ? 57.998 45.804 47.210 1.00 34.30 ? 401 GOL A C1 1 HETATM 2734 O O1 . GOL H 6 . ? 59.182 46.591 47.226 1.00 40.88 ? 401 GOL A O1 1 HETATM 2735 C C2 . GOL H 6 . ? 56.829 46.787 47.137 1.00 22.91 ? 401 GOL A C2 1 HETATM 2736 O O2 . GOL H 6 . ? 56.716 47.497 48.360 1.00 29.87 ? 401 GOL A O2 1 HETATM 2737 C C3 . GOL H 6 . ? 55.569 46.118 46.647 1.00 22.48 ? 401 GOL A C3 1 HETATM 2738 O O3 . GOL H 6 . ? 54.417 46.930 46.744 1.00 24.35 ? 401 GOL A O3 1 HETATM 2739 O O . HOH I 7 . ? 54.893 17.736 30.033 1.00 15.02 ? 1001 HOH A O 1 HETATM 2740 O O . HOH I 7 . ? 62.653 26.031 27.384 1.00 22.94 ? 1002 HOH A O 1 HETATM 2741 O O . HOH I 7 . ? 53.285 18.686 27.868 1.00 14.43 ? 1003 HOH A O 1 HETATM 2742 O O . HOH I 7 . ? 48.732 25.722 54.096 1.00 14.39 ? 1004 HOH A O 1 HETATM 2743 O O . HOH I 7 . ? 47.287 7.472 30.909 1.00 12.96 ? 1005 HOH A O 1 HETATM 2744 O O . HOH I 7 . ? 45.171 29.346 28.932 1.00 21.46 ? 1006 HOH A O 1 HETATM 2745 O O . HOH I 7 . ? 51.746 9.953 24.970 1.00 17.06 ? 1007 HOH A O 1 HETATM 2746 O O . HOH I 7 . ? 52.099 30.428 26.410 1.00 18.06 ? 1008 HOH A O 1 HETATM 2747 O O . HOH I 7 . ? 61.753 6.925 32.566 1.00 23.93 ? 1009 HOH A O 1 HETATM 2748 O O . HOH I 7 . ? 68.149 20.138 44.040 1.00 18.47 ? 1010 HOH A O 1 HETATM 2749 O O . HOH I 7 . ? 44.898 22.843 49.704 1.00 16.01 ? 1011 HOH A O 1 HETATM 2750 O O . HOH I 7 . ? 60.332 30.735 57.136 1.00 16.28 ? 1012 HOH A O 1 HETATM 2751 O O . HOH I 7 . ? 52.254 27.903 19.775 1.00 20.32 ? 1013 HOH A O 1 HETATM 2752 O O . HOH I 7 . ? 59.119 27.139 58.693 1.00 17.66 ? 1014 HOH A O 1 HETATM 2753 O O . HOH I 7 . ? 35.253 15.676 37.639 1.00 16.41 ? 1015 HOH A O 1 HETATM 2754 O O . HOH I 7 . ? 66.363 22.686 46.729 1.00 14.86 ? 1016 HOH A O 1 HETATM 2755 O O . HOH I 7 . ? 53.071 29.800 23.828 1.00 18.50 ? 1017 HOH A O 1 HETATM 2756 O O . HOH I 7 . ? 43.916 28.893 45.749 1.00 15.27 ? 1018 HOH A O 1 HETATM 2757 O O . HOH I 7 . ? 55.044 31.332 25.192 1.00 15.75 ? 1019 HOH A O 1 HETATM 2758 O O . HOH I 7 . ? 37.851 27.735 40.225 1.00 17.96 ? 1020 HOH A O 1 HETATM 2759 O O . HOH I 7 . ? 57.257 35.749 40.135 1.00 16.73 ? 1021 HOH A O 1 HETATM 2760 O O . HOH I 7 . ? 57.011 2.518 42.917 1.00 18.27 ? 1022 HOH A O 1 HETATM 2761 O O . HOH I 7 . ? 72.214 23.204 55.541 1.00 14.71 ? 1023 HOH A O 1 HETATM 2762 O O . HOH I 7 . ? 50.339 24.394 30.789 1.00 12.10 ? 1024 HOH A O 1 HETATM 2763 O O . HOH I 7 . ? 50.826 36.528 36.612 1.00 17.02 ? 1025 HOH A O 1 HETATM 2764 O O . HOH I 7 . ? 52.367 17.074 25.760 1.00 15.52 ? 1026 HOH A O 1 HETATM 2765 O O . HOH I 7 . ? 67.349 19.774 46.751 1.00 13.20 ? 1027 HOH A O 1 HETATM 2766 O O . HOH I 7 . ? 53.095 41.913 58.011 1.00 20.61 ? 1028 HOH A O 1 HETATM 2767 O O . HOH I 7 . ? 50.395 26.656 49.278 1.00 16.72 ? 1029 HOH A O 1 HETATM 2768 O O . HOH I 7 . ? 45.248 14.014 45.689 1.00 15.80 ? 1030 HOH A O 1 HETATM 2769 O O . HOH I 7 . ? 67.326 17.632 43.027 1.00 15.32 ? 1031 HOH A O 1 HETATM 2770 O O . HOH I 7 . ? 45.904 6.109 28.941 1.00 21.19 ? 1032 HOH A O 1 HETATM 2771 O O . HOH I 7 . ? 58.803 10.408 23.097 1.00 33.37 ? 1033 HOH A O 1 HETATM 2772 O O . HOH I 7 . ? 45.720 23.589 17.838 1.00 19.68 ? 1034 HOH A O 1 HETATM 2773 O O . HOH I 7 . ? 70.103 27.030 39.323 1.00 19.75 ? 1035 HOH A O 1 HETATM 2774 O O . HOH I 7 . ? 56.469 12.028 23.255 1.00 17.90 ? 1036 HOH A O 1 HETATM 2775 O O . HOH I 7 . ? 34.644 17.514 24.330 1.00 19.53 ? 1037 HOH A O 1 HETATM 2776 O O . HOH I 7 . ? 52.248 36.271 31.501 1.00 22.08 ? 1038 HOH A O 1 HETATM 2777 O O . HOH I 7 . ? 53.639 40.809 36.552 1.00 18.92 ? 1039 HOH A O 1 HETATM 2778 O O . HOH I 7 . ? 58.132 30.657 31.032 1.00 45.26 ? 1040 HOH A O 1 HETATM 2779 O O . HOH I 7 . ? 47.944 6.064 44.806 1.00 19.27 ? 1041 HOH A O 1 HETATM 2780 O O . HOH I 7 . ? 47.622 23.024 54.114 1.00 16.76 ? 1042 HOH A O 1 HETATM 2781 O O . HOH I 7 . ? 71.829 25.900 56.616 1.00 17.74 ? 1043 HOH A O 1 HETATM 2782 O O . HOH I 7 . ? 70.409 19.786 41.258 1.00 18.88 ? 1044 HOH A O 1 HETATM 2783 O O . HOH I 7 . ? 58.126 26.745 19.256 1.00 26.56 ? 1045 HOH A O 1 HETATM 2784 O O . HOH I 7 . ? 67.600 41.038 49.799 1.00 25.93 ? 1046 HOH A O 1 HETATM 2785 O O . HOH I 7 . ? 56.161 38.033 54.527 1.00 16.83 ? 1047 HOH A O 1 HETATM 2786 O O . HOH I 7 . ? 39.687 18.304 48.139 1.00 18.41 ? 1048 HOH A O 1 HETATM 2787 O O . HOH I 7 . ? 53.761 17.490 57.523 1.00 20.65 ? 1049 HOH A O 1 HETATM 2788 O O . HOH I 7 . ? 56.699 15.914 35.616 1.00 20.45 ? 1050 HOH A O 1 HETATM 2789 O O . HOH I 7 . ? 44.146 43.357 57.718 1.00 30.17 ? 1051 HOH A O 1 HETATM 2790 O O . HOH I 7 . ? 62.511 21.629 22.007 1.00 16.80 ? 1052 HOH A O 1 HETATM 2791 O O . HOH I 7 . ? 64.717 16.516 55.860 1.00 18.25 ? 1053 HOH A O 1 HETATM 2792 O O . HOH I 7 . ? 59.789 -0.545 36.186 1.00 18.75 ? 1054 HOH A O 1 HETATM 2793 O O . HOH I 7 . ? 71.899 21.090 57.135 1.00 16.91 ? 1055 HOH A O 1 HETATM 2794 O O . HOH I 7 . ? 67.557 29.824 39.877 1.00 20.35 ? 1056 HOH A O 1 HETATM 2795 O O . HOH I 7 . ? 60.016 33.366 29.986 1.00 36.45 ? 1057 HOH A O 1 HETATM 2796 O O . HOH I 7 . ? 62.776 12.483 41.400 1.00 21.88 ? 1058 HOH A O 1 HETATM 2797 O O . HOH I 7 . ? 39.567 29.473 58.412 1.00 40.70 ? 1059 HOH A O 1 HETATM 2798 O O . HOH I 7 . ? 51.016 42.229 55.963 1.00 19.49 ? 1060 HOH A O 1 HETATM 2799 O O . HOH I 7 . ? 64.338 20.734 37.555 1.00 27.07 ? 1061 HOH A O 1 HETATM 2800 O O . HOH I 7 . ? 64.536 45.569 41.003 1.00 22.14 ? 1062 HOH A O 1 HETATM 2801 O O . HOH I 7 . ? 58.077 5.873 29.521 1.00 23.23 ? 1063 HOH A O 1 HETATM 2802 O O . HOH I 7 . ? 64.679 40.929 45.676 1.00 19.01 ? 1064 HOH A O 1 HETATM 2803 O O . HOH I 7 . ? 55.327 21.757 63.756 1.00 24.11 ? 1065 HOH A O 1 HETATM 2804 O O . HOH I 7 . ? 73.138 22.666 51.129 1.00 19.48 ? 1066 HOH A O 1 HETATM 2805 O O . HOH I 7 . ? 37.365 11.017 22.537 1.00 21.55 ? 1067 HOH A O 1 HETATM 2806 O O . HOH I 7 . ? 71.974 32.332 51.082 1.00 16.20 ? 1068 HOH A O 1 HETATM 2807 O O . HOH I 7 . ? 75.216 21.147 44.775 1.00 23.11 ? 1069 HOH A O 1 HETATM 2808 O O . HOH I 7 . ? 67.000 36.620 52.490 1.00 22.34 ? 1070 HOH A O 1 HETATM 2809 O O . HOH I 7 . ? 58.215 33.201 24.298 1.00 29.96 ? 1071 HOH A O 1 HETATM 2810 O O . HOH I 7 . ? 48.672 26.706 51.607 1.00 19.93 ? 1072 HOH A O 1 HETATM 2811 O O . HOH I 7 . ? 56.117 24.239 62.909 1.00 23.38 ? 1073 HOH A O 1 HETATM 2812 O O . HOH I 7 . ? 64.179 23.147 33.716 1.00 23.15 ? 1074 HOH A O 1 HETATM 2813 O O . HOH I 7 . ? 58.102 14.700 55.861 1.00 21.95 ? 1075 HOH A O 1 HETATM 2814 O O . HOH I 7 . ? 64.984 12.899 43.384 1.00 37.31 ? 1076 HOH A O 1 HETATM 2815 O O . HOH I 7 . ? 63.022 36.034 62.195 1.00 25.84 ? 1077 HOH A O 1 HETATM 2816 O O . HOH I 7 . ? 36.394 20.496 42.633 1.00 19.38 ? 1078 HOH A O 1 HETATM 2817 O O . HOH I 7 . ? 42.172 17.891 14.092 1.00 29.18 ? 1079 HOH A O 1 HETATM 2818 O O . HOH I 7 . ? 69.548 17.176 41.285 1.00 21.40 ? 1080 HOH A O 1 HETATM 2819 O O . HOH I 7 . ? 38.079 23.444 32.926 1.00 19.92 ? 1081 HOH A O 1 HETATM 2820 O O . HOH I 7 . ? 47.235 24.760 19.840 1.00 27.36 ? 1082 HOH A O 1 HETATM 2821 O O . HOH I 7 . ? 66.077 8.113 37.100 1.00 20.55 ? 1083 HOH A O 1 HETATM 2822 O O . HOH I 7 . ? 56.837 27.373 52.329 1.00 14.67 ? 1084 HOH A O 1 HETATM 2823 O O . HOH I 7 . ? 63.302 24.310 49.632 1.00 12.37 ? 1085 HOH A O 1 HETATM 2824 O O . HOH I 7 . ? 42.608 10.295 38.359 1.00 19.52 ? 1086 HOH A O 1 HETATM 2825 O O . HOH I 7 . ? 65.474 23.593 54.444 1.00 14.28 ? 1087 HOH A O 1 HETATM 2826 O O . HOH I 7 . ? 54.939 8.110 45.746 1.00 17.31 ? 1088 HOH A O 1 HETATM 2827 O O . HOH I 7 . ? 58.651 18.914 23.637 1.00 18.28 ? 1089 HOH A O 1 HETATM 2828 O O . HOH I 7 . ? 58.798 38.535 56.966 1.00 16.89 ? 1090 HOH A O 1 HETATM 2829 O O . HOH I 7 . ? 68.337 27.684 49.914 1.00 16.34 ? 1091 HOH A O 1 HETATM 2830 O O . HOH I 7 . ? 54.802 3.167 44.290 1.00 18.67 ? 1092 HOH A O 1 HETATM 2831 O O . HOH I 7 . ? 54.464 10.381 21.754 1.00 19.33 ? 1093 HOH A O 1 HETATM 2832 O O . HOH I 7 . ? 40.804 28.719 51.229 1.00 17.06 ? 1094 HOH A O 1 HETATM 2833 O O . HOH I 7 . ? 47.346 24.020 50.535 1.00 16.89 ? 1095 HOH A O 1 HETATM 2834 O O . HOH I 7 . ? 38.661 29.960 31.326 1.00 20.40 ? 1096 HOH A O 1 HETATM 2835 O O . HOH I 7 . ? 39.217 20.320 31.278 1.00 15.06 ? 1097 HOH A O 1 HETATM 2836 O O . HOH I 7 . ? 51.106 17.523 59.721 1.00 30.46 ? 1098 HOH A O 1 HETATM 2837 O O . HOH I 7 . ? 52.293 17.078 55.226 1.00 20.40 ? 1099 HOH A O 1 HETATM 2838 O O . HOH I 7 . ? 65.251 29.744 27.144 1.00 37.70 ? 1100 HOH A O 1 HETATM 2839 O O . HOH I 7 . ? 42.635 26.411 63.695 1.00 27.87 ? 1101 HOH A O 1 HETATM 2840 O O . HOH I 7 . ? 73.874 19.811 49.170 1.00 27.23 ? 1102 HOH A O 1 HETATM 2841 O O . HOH I 7 . ? 45.887 28.874 24.794 1.00 36.64 ? 1103 HOH A O 1 HETATM 2842 O O . HOH I 7 . ? 39.919 7.448 32.515 1.00 38.37 ? 1104 HOH A O 1 HETATM 2843 O O . HOH I 7 . ? 53.652 35.704 29.223 1.00 19.23 ? 1105 HOH A O 1 HETATM 2844 O O . HOH I 7 . ? 57.555 45.834 35.115 1.00 16.99 ? 1106 HOH A O 1 HETATM 2845 O O . HOH I 7 . ? 52.484 47.611 43.048 1.00 19.18 ? 1107 HOH A O 1 HETATM 2846 O O . HOH I 7 . ? 59.918 8.088 28.987 1.00 22.74 ? 1108 HOH A O 1 HETATM 2847 O O . HOH I 7 . ? 59.208 28.179 33.605 1.00 36.74 ? 1109 HOH A O 1 HETATM 2848 O O . HOH I 7 . ? 57.830 4.896 45.986 1.00 23.24 ? 1110 HOH A O 1 HETATM 2849 O O . HOH I 7 . ? 64.501 10.345 47.867 1.00 23.42 ? 1111 HOH A O 1 HETATM 2850 O O . HOH I 7 . ? 36.092 9.739 20.170 1.00 22.21 ? 1112 HOH A O 1 HETATM 2851 O O . HOH I 7 . ? 68.531 23.504 23.820 1.00 30.58 ? 1113 HOH A O 1 HETATM 2852 O O . HOH I 7 . ? 56.664 16.786 57.277 1.00 20.49 ? 1114 HOH A O 1 HETATM 2853 O O . HOH I 7 . ? 43.689 10.119 47.891 1.00 29.30 ? 1115 HOH A O 1 HETATM 2854 O O . HOH I 7 . ? 43.893 2.620 21.695 1.00 25.84 ? 1116 HOH A O 1 HETATM 2855 O O . HOH I 7 . ? 65.180 20.908 59.258 1.00 19.56 ? 1117 HOH A O 1 HETATM 2856 O O . HOH I 7 . ? 65.165 34.350 59.666 1.00 24.13 ? 1118 HOH A O 1 HETATM 2857 O O . HOH I 7 . ? 43.343 3.566 28.275 1.00 23.26 ? 1119 HOH A O 1 HETATM 2858 O O . HOH I 7 . ? 41.228 28.191 28.134 1.00 23.77 ? 1120 HOH A O 1 HETATM 2859 O O . HOH I 7 . ? 55.375 37.649 29.517 1.00 28.50 ? 1121 HOH A O 1 HETATM 2860 O O . HOH I 7 . ? 66.071 14.473 41.162 1.00 21.15 ? 1122 HOH A O 1 HETATM 2861 O O . HOH I 7 . ? 55.282 32.587 61.807 1.00 23.67 ? 1123 HOH A O 1 HETATM 2862 O O . HOH I 7 . ? 60.598 11.711 21.912 1.00 27.37 ? 1124 HOH A O 1 HETATM 2863 O O . HOH I 7 . ? 36.595 20.467 31.861 1.00 21.33 ? 1125 HOH A O 1 HETATM 2864 O O . HOH I 7 . ? 53.789 33.919 59.875 1.00 17.76 ? 1126 HOH A O 1 HETATM 2865 O O . HOH I 7 . ? 61.614 7.397 53.453 1.00 24.65 ? 1127 HOH A O 1 HETATM 2866 O O . HOH I 7 . ? 63.771 22.859 52.506 1.00 14.40 ? 1128 HOH A O 1 HETATM 2867 O O . HOH I 7 . ? 40.187 13.085 45.071 1.00 23.49 ? 1129 HOH A O 1 HETATM 2868 O O . HOH I 7 . ? 58.091 4.150 33.356 1.00 17.99 ? 1130 HOH A O 1 HETATM 2869 O O . HOH I 7 . ? 36.226 27.464 27.937 1.00 25.05 ? 1131 HOH A O 1 HETATM 2870 O O . HOH I 7 . ? 56.367 5.067 31.353 1.00 20.77 ? 1132 HOH A O 1 HETATM 2871 O O . HOH I 7 . ? 47.146 4.307 37.871 1.00 17.34 ? 1133 HOH A O 1 HETATM 2872 O O . HOH I 7 . ? 48.337 0.961 39.264 1.00 19.76 ? 1134 HOH A O 1 HETATM 2873 O O . HOH I 7 . ? 46.837 30.114 15.558 1.00 24.90 ? 1135 HOH A O 1 HETATM 2874 O O . HOH I 7 . ? 72.945 26.607 59.084 1.00 17.46 ? 1136 HOH A O 1 HETATM 2875 O O . HOH I 7 . ? 64.649 23.504 59.700 1.00 18.84 ? 1137 HOH A O 1 HETATM 2876 O O . HOH I 7 . ? 58.139 22.006 38.608 1.00 27.61 ? 1138 HOH A O 1 HETATM 2877 O O . HOH I 7 . ? 43.765 5.851 19.120 1.00 25.61 ? 1139 HOH A O 1 HETATM 2878 O O . HOH I 7 . ? 54.081 19.662 67.756 1.00 35.91 ? 1140 HOH A O 1 HETATM 2879 O O . HOH I 7 . ? 45.210 -3.416 34.713 1.00 29.25 ? 1141 HOH A O 1 HETATM 2880 O O . HOH I 7 . ? 53.240 38.100 35.174 1.00 19.16 ? 1142 HOH A O 1 HETATM 2881 O O . HOH I 7 . ? 42.627 38.290 51.340 1.00 27.90 ? 1143 HOH A O 1 HETATM 2882 O O . HOH I 7 . ? 38.790 34.475 32.802 1.00 28.12 ? 1144 HOH A O 1 HETATM 2883 O O . HOH I 7 . ? 46.277 4.209 21.818 1.00 24.75 ? 1145 HOH A O 1 HETATM 2884 O O . HOH I 7 . ? 31.640 27.595 35.936 1.00 34.75 ? 1146 HOH A O 1 HETATM 2885 O O . HOH I 7 . ? 41.328 19.374 50.251 1.00 22.95 ? 1147 HOH A O 1 HETATM 2886 O O . HOH I 7 . ? 49.871 13.687 17.546 1.00 32.69 ? 1148 HOH A O 1 HETATM 2887 O O . HOH I 7 . ? 69.770 14.275 48.532 1.00 32.15 ? 1149 HOH A O 1 HETATM 2888 O O . HOH I 7 . ? 58.310 38.021 31.322 1.00 52.53 ? 1150 HOH A O 1 HETATM 2889 O O . HOH I 7 . ? 62.358 0.668 38.682 1.00 23.06 ? 1151 HOH A O 1 HETATM 2890 O O . HOH I 7 . ? 67.549 20.157 29.197 1.00 30.66 ? 1152 HOH A O 1 HETATM 2891 O O . HOH I 7 . ? 39.274 38.101 34.968 1.00 36.64 ? 1153 HOH A O 1 HETATM 2892 O O . HOH I 7 . ? 61.342 26.225 59.874 1.00 21.12 ? 1154 HOH A O 1 HETATM 2893 O O . HOH I 7 . ? 41.849 36.589 40.516 1.00 23.87 ? 1155 HOH A O 1 HETATM 2894 O O . HOH I 7 . ? 69.236 15.061 59.972 1.00 41.27 ? 1156 HOH A O 1 HETATM 2895 O O . HOH I 7 . ? 50.239 29.041 65.139 1.00 26.58 ? 1157 HOH A O 1 HETATM 2896 O O . HOH I 7 . ? 68.218 13.620 38.562 1.00 20.89 ? 1158 HOH A O 1 HETATM 2897 O O . HOH I 7 . ? 42.458 24.262 18.694 1.00 25.43 ? 1159 HOH A O 1 HETATM 2898 O O . HOH I 7 . ? 64.483 18.207 22.819 1.00 30.35 ? 1160 HOH A O 1 HETATM 2899 O O . HOH I 7 . ? 44.982 34.950 33.938 1.00 19.81 ? 1161 HOH A O 1 HETATM 2900 O O . HOH I 7 . ? 45.711 13.982 49.670 1.00 34.28 ? 1162 HOH A O 1 HETATM 2901 O O . HOH I 7 . ? 60.455 3.728 36.592 1.00 14.49 ? 1163 HOH A O 1 HETATM 2902 O O . HOH I 7 . ? 51.154 26.041 67.516 1.00 19.91 ? 1164 HOH A O 1 HETATM 2903 O O . HOH I 7 . ? 61.210 31.875 39.246 1.00 18.64 ? 1165 HOH A O 1 HETATM 2904 O O . HOH I 7 . ? 59.284 4.117 43.751 1.00 17.81 ? 1166 HOH A O 1 HETATM 2905 O O . HOH I 7 . ? 60.586 21.851 59.264 1.00 18.31 ? 1167 HOH A O 1 HETATM 2906 O O . HOH I 7 . ? 43.408 33.044 32.498 1.00 20.22 ? 1168 HOH A O 1 HETATM 2907 O O . HOH I 7 . ? 64.106 9.084 44.717 1.00 19.12 ? 1169 HOH A O 1 HETATM 2908 O O . HOH I 7 . ? 38.879 10.410 32.060 1.00 22.99 ? 1170 HOH A O 1 HETATM 2909 O O . HOH I 7 . ? 49.550 17.985 15.928 1.00 29.87 ? 1171 HOH A O 1 HETATM 2910 O O . HOH I 7 . ? 58.455 23.711 16.198 1.00 22.51 ? 1172 HOH A O 1 HETATM 2911 O O . HOH I 7 . ? 73.339 21.331 41.516 1.00 21.04 ? 1173 HOH A O 1 HETATM 2912 O O . HOH I 7 . ? 38.224 24.784 46.450 1.00 25.52 ? 1174 HOH A O 1 HETATM 2913 O O . HOH I 7 . ? 47.632 2.244 35.765 1.00 18.54 ? 1175 HOH A O 1 HETATM 2914 O O . HOH I 7 . ? 41.198 1.316 37.117 1.00 27.52 ? 1176 HOH A O 1 HETATM 2915 O O . HOH I 7 . ? 61.342 32.236 22.292 1.00 51.66 ? 1177 HOH A O 1 HETATM 2916 O O . HOH I 7 . ? 55.129 5.400 45.973 1.00 17.67 ? 1178 HOH A O 1 HETATM 2917 O O . HOH I 7 . ? 42.803 5.205 38.338 1.00 31.26 ? 1179 HOH A O 1 HETATM 2918 O O . HOH I 7 . ? 32.376 8.075 21.177 1.00 25.18 ? 1180 HOH A O 1 HETATM 2919 O O . HOH I 7 . ? 60.348 29.381 12.331 1.00 56.47 ? 1181 HOH A O 1 HETATM 2920 O O . HOH I 7 . ? 50.239 41.623 34.262 1.00 29.70 ? 1182 HOH A O 1 HETATM 2921 O O . HOH I 7 . ? 38.144 9.392 36.580 1.00 21.33 ? 1183 HOH A O 1 HETATM 2922 O O . HOH I 7 . ? 30.442 23.863 25.955 1.00 26.89 ? 1184 HOH A O 1 HETATM 2923 O O . HOH I 7 . ? 42.498 37.552 29.021 1.00 31.73 ? 1185 HOH A O 1 HETATM 2924 O O . HOH I 7 . ? 54.896 26.019 64.275 1.00 43.64 ? 1186 HOH A O 1 HETATM 2925 O O . HOH I 7 . ? 30.125 20.421 25.400 1.00 30.92 ? 1187 HOH A O 1 HETATM 2926 O O . HOH I 7 . ? 52.005 21.371 14.682 1.00 23.90 ? 1188 HOH A O 1 HETATM 2927 O O . HOH I 7 . ? 34.499 12.217 30.744 1.00 36.74 ? 1189 HOH A O 1 HETATM 2928 O O . HOH I 7 . ? 32.661 16.062 25.383 1.00 29.75 ? 1190 HOH A O 1 HETATM 2929 O O . HOH I 7 . ? 62.745 15.295 57.822 1.00 20.77 ? 1191 HOH A O 1 HETATM 2930 O O . HOH I 7 . ? 58.891 31.390 20.605 1.00 31.88 ? 1192 HOH A O 1 HETATM 2931 O O . HOH I 7 . ? 61.335 23.184 16.308 1.00 31.23 ? 1193 HOH A O 1 HETATM 2932 O O . HOH I 7 . ? 55.284 30.723 32.550 1.00 18.19 ? 1195 HOH A O 1 HETATM 2933 O O . HOH I 7 . ? 60.034 5.649 34.268 1.00 16.74 ? 1196 HOH A O 1 HETATM 2934 O O . HOH I 7 . ? 39.122 25.773 33.808 1.00 17.74 ? 1197 HOH A O 1 HETATM 2935 O O . HOH I 7 . ? 47.764 18.675 55.717 1.00 23.19 ? 1198 HOH A O 1 HETATM 2936 O O . HOH I 7 . ? 42.909 38.871 45.047 1.00 24.14 ? 1199 HOH A O 1 HETATM 2937 O O . HOH I 7 . ? 76.272 33.435 49.782 1.00 19.36 ? 1200 HOH A O 1 HETATM 2938 O O . HOH I 7 . ? 37.663 27.490 32.090 1.00 20.09 ? 1201 HOH A O 1 HETATM 2939 O O . HOH I 7 . ? 66.093 42.060 47.637 1.00 26.78 ? 1202 HOH A O 1 HETATM 2940 O O . HOH I 7 . ? 33.354 37.720 64.779 1.00 37.60 ? 1203 HOH A O 1 HETATM 2941 O O . HOH I 7 . ? 60.173 14.508 57.556 1.00 20.63 ? 1204 HOH A O 1 HETATM 2942 O O . HOH I 7 . ? 64.748 23.783 36.302 1.00 32.10 ? 1205 HOH A O 1 HETATM 2943 O O . HOH I 7 . ? 50.081 3.390 41.952 1.00 22.73 ? 1206 HOH A O 1 HETATM 2944 O O . HOH I 7 . ? 66.812 30.905 59.545 1.00 21.82 ? 1207 HOH A O 1 HETATM 2945 O O . HOH I 7 . ? 39.023 26.775 51.223 1.00 28.54 ? 1208 HOH A O 1 HETATM 2946 O O . HOH I 7 . ? 67.736 10.454 36.971 1.00 23.09 ? 1209 HOH A O 1 HETATM 2947 O O . HOH I 7 . ? 52.987 14.251 54.858 1.00 25.40 ? 1210 HOH A O 1 HETATM 2948 O O . HOH I 7 . ? 73.592 37.203 46.352 1.00 26.67 ? 1211 HOH A O 1 HETATM 2949 O O . HOH I 7 . ? 40.517 20.166 13.773 1.00 28.31 ? 1212 HOH A O 1 HETATM 2950 O O . HOH I 7 . ? 66.231 20.011 36.098 1.00 26.04 ? 1213 HOH A O 1 HETATM 2951 O O . HOH I 7 . ? 62.609 19.863 60.029 1.00 24.19 ? 1214 HOH A O 1 HETATM 2952 O O . HOH I 7 . ? 65.955 32.564 35.631 1.00 30.96 ? 1215 HOH A O 1 HETATM 2953 O O . HOH I 7 . ? 41.688 7.974 39.161 1.00 22.96 ? 1216 HOH A O 1 HETATM 2954 O O . HOH I 7 . ? 43.993 12.877 47.700 1.00 24.05 ? 1217 HOH A O 1 HETATM 2955 O O . HOH I 7 . ? 48.370 49.129 43.431 1.00 30.66 ? 1218 HOH A O 1 HETATM 2956 O O . HOH I 7 . ? 58.813 34.996 28.407 1.00 45.22 ? 1219 HOH A O 1 HETATM 2957 O O . HOH I 7 . ? 37.554 25.503 49.267 1.00 28.43 ? 1220 HOH A O 1 HETATM 2958 O O . HOH I 7 . ? 37.638 19.899 47.446 1.00 22.71 ? 1221 HOH A O 1 HETATM 2959 O O . HOH I 7 . ? 41.445 38.338 24.404 1.00 29.11 ? 1222 HOH A O 1 HETATM 2960 O O . HOH I 7 . ? 49.950 16.858 56.583 1.00 32.31 ? 1223 HOH A O 1 HETATM 2961 O O . HOH I 7 . ? 68.076 35.796 54.873 1.00 22.20 ? 1224 HOH A O 1 HETATM 2962 O O . HOH I 7 . ? 43.868 1.054 23.895 1.00 20.91 ? 1225 HOH A O 1 HETATM 2963 O O . HOH I 7 . ? 65.931 37.581 39.144 1.00 33.56 ? 1226 HOH A O 1 HETATM 2964 O O . HOH I 7 . ? 74.907 25.117 43.548 1.00 26.65 ? 1227 HOH A O 1 HETATM 2965 O O . HOH I 7 . ? 43.965 -1.306 34.684 1.00 32.02 ? 1228 HOH A O 1 HETATM 2966 O O . HOH I 7 . ? 61.931 30.091 34.534 1.00 42.88 ? 1229 HOH A O 1 HETATM 2967 O O . HOH I 7 . ? 41.437 22.031 22.787 1.00 23.70 ? 1230 HOH A O 1 HETATM 2968 O O . HOH I 7 . ? 46.335 8.506 48.107 1.00 25.65 ? 1231 HOH A O 1 HETATM 2969 O O . HOH I 7 . ? 45.115 27.004 22.685 1.00 48.61 ? 1232 HOH A O 1 HETATM 2970 O O . HOH I 7 . ? 67.093 39.222 51.768 1.00 27.74 ? 1233 HOH A O 1 HETATM 2971 O O . HOH I 7 . ? 67.089 18.623 33.654 1.00 26.71 ? 1234 HOH A O 1 HETATM 2972 O O . HOH I 7 . ? 37.382 36.110 56.207 1.00 31.63 ? 1235 HOH A O 1 HETATM 2973 O O . HOH I 7 . ? 59.803 32.522 63.942 1.00 37.03 ? 1236 HOH A O 1 HETATM 2974 O O . HOH I 7 . ? 32.419 19.677 24.423 1.00 35.00 ? 1237 HOH A O 1 HETATM 2975 O O . HOH I 7 . ? 41.537 34.911 33.373 1.00 27.68 ? 1238 HOH A O 1 HETATM 2976 O O . HOH I 7 . ? 59.908 2.539 32.265 1.00 26.56 ? 1239 HOH A O 1 HETATM 2977 O O . HOH I 7 . ? 45.663 17.194 55.068 1.00 32.97 ? 1240 HOH A O 1 HETATM 2978 O O . HOH I 7 . ? 53.234 38.895 32.358 1.00 38.71 ? 1241 HOH A O 1 HETATM 2979 O O . HOH I 7 . ? 43.182 40.450 50.115 1.00 24.66 ? 1242 HOH A O 1 HETATM 2980 O O . HOH I 7 . ? 39.386 7.346 37.688 1.00 35.20 ? 1243 HOH A O 1 HETATM 2981 O O . HOH I 7 . ? 59.110 29.628 18.795 1.00 40.19 ? 1245 HOH A O 1 HETATM 2982 O O . HOH I 7 . ? 39.008 28.771 61.272 1.00 38.12 ? 1246 HOH A O 1 HETATM 2983 O O . HOH I 7 . ? 75.614 23.106 42.062 1.00 82.13 ? 1247 HOH A O 1 HETATM 2984 O O . HOH I 7 . ? 60.109 40.875 61.324 1.00 31.86 ? 1248 HOH A O 1 HETATM 2985 O O . HOH I 7 . ? 67.906 23.438 33.553 1.00 38.57 ? 1249 HOH A O 1 HETATM 2986 O O . HOH I 7 . ? 62.006 23.551 60.673 1.00 23.67 ? 1250 HOH A O 1 HETATM 2987 O O . HOH I 7 . ? 50.729 47.727 46.221 1.00 34.95 ? 1251 HOH A O 1 HETATM 2988 O O . HOH I 7 . ? 46.880 14.237 14.044 1.00 51.09 ? 1252 HOH A O 1 HETATM 2989 O O . HOH I 7 . ? 37.869 26.058 29.630 1.00 26.38 ? 1253 HOH A O 1 HETATM 2990 O O . HOH I 7 . ? 33.256 0.363 27.509 1.00 79.80 ? 1254 HOH A O 1 HETATM 2991 O O . HOH I 7 . ? 34.178 41.425 56.445 1.00 34.40 ? 1255 HOH A O 1 HETATM 2992 O O . HOH I 7 . ? 60.179 8.293 24.469 1.00 33.85 ? 1256 HOH A O 1 HETATM 2993 O O . HOH I 7 . ? 64.759 43.876 48.826 1.00 28.53 ? 1257 HOH A O 1 HETATM 2994 O O . HOH I 7 . ? 35.381 18.767 46.950 1.00 23.06 ? 1258 HOH A O 1 HETATM 2995 O O . HOH I 7 . ? 37.115 23.502 39.309 1.00 29.29 ? 1259 HOH A O 1 HETATM 2996 O O . HOH I 7 . ? 67.651 33.452 58.323 1.00 31.36 ? 1260 HOH A O 1 HETATM 2997 O O . HOH I 7 . ? 46.422 -0.146 35.879 1.00 34.69 ? 1261 HOH A O 1 HETATM 2998 O O . HOH I 7 . ? 38.456 37.161 53.932 1.00 25.24 ? 1262 HOH A O 1 HETATM 2999 O O . HOH I 7 . ? 43.620 40.253 47.394 1.00 23.67 ? 1263 HOH A O 1 HETATM 3000 O O . HOH I 7 . ? 48.537 8.575 52.355 1.00 62.23 ? 1264 HOH A O 1 HETATM 3001 O O . HOH I 7 . ? 42.424 41.030 43.338 1.00 26.59 ? 1265 HOH A O 1 HETATM 3002 O O . HOH I 7 . ? 44.030 19.166 66.100 1.00 33.12 ? 1266 HOH A O 1 HETATM 3003 O O . HOH I 7 . ? 68.889 40.095 40.549 1.00 29.27 ? 1267 HOH A O 1 HETATM 3004 O O . HOH I 7 . ? 73.201 33.761 44.026 1.00 43.04 ? 1268 HOH A O 1 HETATM 3005 O O . HOH I 7 . ? 33.815 7.109 25.667 1.00 40.11 ? 1269 HOH A O 1 HETATM 3006 O O . HOH I 7 . ? 71.254 28.603 59.684 1.00 30.40 ? 1270 HOH A O 1 HETATM 3007 O O . HOH I 7 . ? 35.613 26.672 38.626 1.00 61.84 ? 1271 HOH A O 1 HETATM 3008 O O . HOH I 7 . ? 42.871 25.741 21.081 1.00 59.45 ? 1272 HOH A O 1 HETATM 3009 O O . HOH I 7 . ? 61.208 8.445 26.728 1.00 33.94 ? 1273 HOH A O 1 HETATM 3010 O O . HOH I 7 . ? 55.777 2.406 30.718 1.00 28.50 ? 1274 HOH A O 1 HETATM 3011 O O . HOH I 7 . ? 47.524 39.815 61.286 1.00 35.43 ? 1275 HOH A O 1 HETATM 3012 O O . HOH I 7 . ? 50.554 38.807 32.248 1.00 52.89 ? 1276 HOH A O 1 HETATM 3013 O O . HOH I 7 . ? 57.265 34.249 62.071 1.00 27.06 ? 1277 HOH A O 1 HETATM 3014 O O . HOH I 7 . ? 50.131 3.371 24.005 1.00 39.54 ? 1278 HOH A O 1 HETATM 3015 O O . HOH I 7 . ? 59.489 37.375 35.957 1.00 25.13 ? 1279 HOH A O 1 HETATM 3016 O O . HOH I 7 . ? 50.948 1.317 27.734 1.00 39.94 ? 1280 HOH A O 1 HETATM 3017 O O . HOH I 7 . ? 36.600 14.309 18.206 1.00 32.73 ? 1281 HOH A O 1 HETATM 3018 O O . HOH I 7 . ? 35.254 29.050 48.841 1.00 30.77 ? 1282 HOH A O 1 HETATM 3019 O O . HOH I 7 . ? 53.133 50.095 48.384 1.00 45.06 ? 1283 HOH A O 1 HETATM 3020 O O . HOH I 7 . ? 65.303 10.074 31.165 1.00 44.59 ? 1284 HOH A O 1 HETATM 3021 O O . HOH I 7 . ? 56.520 14.344 12.729 1.00 28.31 ? 1285 HOH A O 1 HETATM 3022 O O . HOH I 7 . ? 40.018 38.392 39.493 1.00 31.35 ? 1286 HOH A O 1 HETATM 3023 O O . HOH I 7 . ? 43.870 1.065 38.298 1.00 32.05 ? 1288 HOH A O 1 HETATM 3024 O O . HOH I 7 . ? 56.655 44.961 32.786 1.00 34.75 ? 1289 HOH A O 1 HETATM 3025 O O . HOH I 7 . ? 48.223 43.688 33.778 1.00 41.17 ? 1290 HOH A O 1 HETATM 3026 O O . HOH I 7 . ? 46.245 -0.679 38.872 1.00 30.96 ? 1291 HOH A O 1 HETATM 3027 O O . HOH I 7 . ? 69.825 19.309 27.620 1.00 39.55 ? 1292 HOH A O 1 HETATM 3028 O O . HOH I 7 . ? 64.717 15.244 23.743 1.00 28.96 ? 1293 HOH A O 1 HETATM 3029 O O . HOH I 7 . ? 34.912 30.371 42.153 1.00 30.03 ? 1294 HOH A O 1 HETATM 3030 O O . HOH I 7 . ? 40.411 25.229 54.168 1.00 47.87 ? 1295 HOH A O 1 HETATM 3031 O O . HOH I 7 . ? 41.561 35.476 42.798 1.00 26.14 ? 1296 HOH A O 1 HETATM 3032 O O . HOH I 7 . ? 46.711 2.753 40.902 1.00 40.13 ? 1297 HOH A O 1 HETATM 3033 O O . HOH I 7 . ? 37.711 22.393 46.257 1.00 44.81 ? 1298 HOH A O 1 HETATM 3034 O O . HOH I 7 . ? 56.086 44.769 49.044 1.00 36.00 ? 1299 HOH A O 1 HETATM 3035 O O . HOH I 7 . ? 35.809 28.891 46.454 1.00 36.66 ? 1300 HOH A O 1 HETATM 3036 O O . HOH I 7 . ? 51.531 10.977 54.002 1.00 39.95 ? 1302 HOH A O 1 HETATM 3037 O O . HOH I 7 . ? 58.506 17.218 59.554 1.00 38.39 ? 1303 HOH A O 1 HETATM 3038 O O . HOH I 7 . ? 42.590 36.958 31.851 1.00 31.34 ? 1304 HOH A O 1 HETATM 3039 O O . HOH I 7 . ? 66.376 11.494 49.759 1.00 40.83 ? 1305 HOH A O 1 HETATM 3040 O O . HOH I 7 . ? 64.108 12.511 27.146 1.00 28.42 ? 1306 HOH A O 1 HETATM 3041 O O . HOH I 7 . ? 62.648 26.759 63.310 1.00 31.65 ? 1307 HOH A O 1 HETATM 3042 O O . HOH I 7 . ? 67.151 22.303 35.834 1.00 33.26 ? 1308 HOH A O 1 HETATM 3043 O O . HOH I 7 . ? 41.416 13.496 47.460 1.00 30.20 ? 1309 HOH A O 1 HETATM 3044 O O . HOH I 7 . ? 71.987 14.107 50.440 1.00 34.16 ? 1310 HOH A O 1 HETATM 3045 O O . HOH I 7 . ? 45.554 33.173 26.220 1.00 32.16 ? 1311 HOH A O 1 HETATM 3046 O O . HOH I 7 . ? 75.863 30.968 44.993 1.00 29.62 ? 1312 HOH A O 1 HETATM 3047 O O . HOH I 7 . ? 59.021 35.630 63.504 1.00 32.68 ? 1313 HOH A O 1 HETATM 3048 O O . HOH I 7 . ? 66.504 20.107 31.865 1.00 38.69 ? 1314 HOH A O 1 HETATM 3049 O O . HOH I 7 . ? 62.560 12.356 22.903 1.00 49.55 ? 1315 HOH A O 1 HETATM 3050 O O . HOH I 7 . ? 35.389 27.833 41.391 1.00 28.62 ? 1316 HOH A O 1 HETATM 3051 O O . HOH I 7 . ? 44.684 3.545 39.324 1.00 39.26 ? 1317 HOH A O 1 HETATM 3052 O O . HOH I 7 . ? 70.112 21.641 26.141 1.00 52.72 ? 1318 HOH A O 1 HETATM 3053 O O . HOH I 7 . ? 37.769 36.557 47.177 1.00 27.94 ? 1319 HOH A O 1 HETATM 3054 O O . HOH I 7 . ? 35.454 7.103 24.046 1.00 35.47 ? 1320 HOH A O 1 HETATM 3055 O O . HOH I 7 . ? 61.189 11.729 18.610 1.00 52.73 ? 1321 HOH A O 1 HETATM 3056 O O . HOH I 7 . ? 45.331 27.989 20.402 1.00 32.94 ? 1322 HOH A O 1 HETATM 3057 O O . HOH I 7 . ? 65.659 26.056 18.474 1.00 40.49 ? 1323 HOH A O 1 HETATM 3058 O O . HOH I 7 . ? 33.334 17.234 31.403 1.00 33.53 ? 1324 HOH A O 1 HETATM 3059 O O . HOH I 7 . ? 74.822 34.839 52.472 1.00 34.77 ? 1325 HOH A O 1 HETATM 3060 O O . HOH I 7 . ? 70.866 18.345 36.680 1.00 56.13 ? 1326 HOH A O 1 HETATM 3061 O O . HOH I 7 . ? 41.941 38.182 34.638 1.00 37.75 ? 1327 HOH A O 1 HETATM 3062 O O . HOH I 7 . ? 42.218 23.020 59.430 1.00 74.19 ? 1328 HOH A O 1 HETATM 3063 O O . HOH I 7 . ? 46.058 25.383 7.965 1.00 36.01 ? 1329 HOH A O 1 HETATM 3064 O O . HOH I 7 . ? 62.859 32.773 32.795 1.00 78.62 ? 1330 HOH A O 1 HETATM 3065 O O . HOH I 7 . ? 64.597 6.537 32.536 1.00 42.32 ? 1331 HOH A O 1 HETATM 3066 O O . HOH I 7 . ? 38.857 16.007 48.884 1.00 39.72 ? 1332 HOH A O 1 HETATM 3067 O O . HOH I 7 . ? 66.577 6.064 38.229 1.00 47.12 ? 1333 HOH A O 1 HETATM 3068 O O . HOH I 7 . ? 68.387 13.426 42.027 1.00 42.20 ? 1334 HOH A O 1 HETATM 3069 O O . HOH I 7 . ? 67.306 22.832 31.395 1.00 157.91 ? 1335 HOH A O 1 HETATM 3070 O O . HOH I 7 . ? 41.191 42.106 49.918 1.00 26.02 ? 1336 HOH A O 1 HETATM 3071 O O . HOH I 7 . ? 59.159 33.035 14.528 1.00 39.52 ? 1337 HOH A O 1 HETATM 3072 O O . HOH I 7 . ? 48.912 15.331 15.354 1.00 41.36 ? 1338 HOH A O 1 HETATM 3073 O O . HOH I 7 . ? 60.492 45.872 50.452 1.00 43.30 ? 1339 HOH A O 1 HETATM 3074 O O . HOH I 7 . ? 50.908 13.189 55.774 1.00 39.02 ? 1340 HOH A O 1 HETATM 3075 O O . HOH I 7 . ? 70.785 16.263 37.877 1.00 40.98 ? 1341 HOH A O 1 HETATM 3076 O O . HOH I 7 . ? 37.902 31.046 64.836 1.00 41.34 ? 1342 HOH A O 1 HETATM 3077 O O . HOH I 7 . ? 48.974 20.293 11.454 1.00 48.90 ? 1343 HOH A O 1 HETATM 3078 O O . HOH I 7 . ? 36.252 26.482 45.604 1.00 40.82 ? 1344 HOH A O 1 HETATM 3079 O O . HOH I 7 . ? 61.637 26.696 16.541 1.00 57.46 ? 1345 HOH A O 1 HETATM 3080 O O . HOH I 7 . ? 59.860 12.591 59.575 1.00 33.95 ? 1346 HOH A O 1 HETATM 3081 O O . HOH I 7 . ? 50.195 44.186 57.445 1.00 53.46 ? 1347 HOH A O 1 HETATM 3082 O O . HOH I 7 . ? 37.564 21.119 10.959 1.00 43.64 ? 1348 HOH A O 1 HETATM 3083 O O . HOH I 7 . ? 59.092 -0.015 31.844 1.00 50.77 ? 1349 HOH A O 1 HETATM 3084 O O . HOH I 7 . ? 71.079 38.496 41.728 1.00 52.80 ? 1350 HOH A O 1 HETATM 3085 O O . HOH I 7 . ? 66.005 8.354 34.313 1.00 31.90 ? 1351 HOH A O 1 HETATM 3086 O O . HOH I 7 . ? 53.915 44.321 58.796 1.00 40.90 ? 1352 HOH A O 1 HETATM 3087 O O . HOH I 7 . ? 42.030 17.849 52.189 1.00 36.39 ? 1353 HOH A O 1 HETATM 3088 O O . HOH I 7 . ? 55.968 29.851 64.442 1.00 34.71 ? 1354 HOH A O 1 HETATM 3089 O O . HOH I 7 . ? 55.540 13.089 57.132 1.00 41.53 ? 1355 HOH A O 1 HETATM 3090 O O . HOH I 7 . ? 62.638 32.227 35.847 1.00 34.18 ? 1356 HOH A O 1 HETATM 3091 O O . HOH I 7 . ? 50.971 38.423 35.319 1.00 43.08 ? 1357 HOH A O 1 HETATM 3092 O O . HOH I 7 . ? 49.667 0.598 32.035 1.00 38.12 ? 1358 HOH A O 1 HETATM 3093 O O . HOH I 7 . ? 58.327 21.523 62.784 1.00 39.62 ? 1359 HOH A O 1 HETATM 3094 O O . HOH I 7 . ? 64.982 3.537 37.936 1.00 47.74 ? 1360 HOH A O 1 HETATM 3095 O O . HOH I 7 . ? 53.598 44.288 64.906 1.00 62.10 ? 1361 HOH A O 1 HETATM 3096 O O . HOH I 7 . ? 48.420 9.071 14.937 1.00 37.18 ? 1362 HOH A O 1 HETATM 3097 O O . HOH I 7 . ? 59.589 35.752 24.804 1.00 50.40 ? 1363 HOH A O 1 HETATM 3098 O O . HOH I 7 . ? 34.418 7.550 30.176 1.00 41.50 ? 1364 HOH A O 1 HETATM 3099 O O . HOH I 7 . ? 46.850 32.498 19.747 1.00 51.55 ? 1365 HOH A O 1 HETATM 3100 O O . HOH I 7 . ? 65.816 10.058 59.419 1.00 39.54 ? 1366 HOH A O 1 HETATM 3101 O O . HOH I 7 . ? 73.335 18.423 39.523 1.00 39.56 ? 1367 HOH A O 1 HETATM 3102 O O . HOH I 7 . ? 71.145 31.759 43.960 1.00 23.62 ? 1368 HOH A O 1 HETATM 3103 O O . HOH I 7 . ? 71.921 16.020 42.821 1.00 43.64 ? 1369 HOH A O 1 HETATM 3104 O O . HOH I 7 . ? 52.932 7.750 55.447 1.00 32.24 ? 1370 HOH A O 1 HETATM 3105 O O . HOH I 7 . ? 68.449 43.402 46.471 1.00 29.66 ? 1371 HOH A O 1 HETATM 3106 O O . HOH I 7 . ? 38.961 25.418 56.121 1.00 47.39 ? 1372 HOH A O 1 HETATM 3107 O O . HOH I 7 . ? 71.643 28.722 31.428 1.00 73.64 ? 1373 HOH A O 1 HETATM 3108 O O . HOH I 7 . ? 47.121 44.168 58.676 1.00 46.76 ? 1374 HOH A O 1 HETATM 3109 O O . HOH I 7 . ? 65.228 20.998 33.643 1.00 46.96 ? 1375 HOH A O 1 HETATM 3110 O O . HOH I 7 . ? 70.068 13.583 36.271 1.00 35.13 ? 1376 HOH A O 1 HETATM 3111 O O . HOH I 7 . ? 42.746 19.524 55.149 1.00 52.58 ? 1377 HOH A O 1 HETATM 3112 O O . HOH I 7 . ? 42.357 40.672 35.100 1.00 33.28 ? 1378 HOH A O 1 HETATM 3113 O O . HOH I 7 . ? 50.203 22.380 12.210 1.00 27.15 ? 1379 HOH A O 1 HETATM 3114 O O . HOH I 7 . ? 44.337 24.730 62.624 1.00 35.21 ? 1380 HOH A O 1 HETATM 3115 O O . HOH I 7 . ? 35.367 18.202 33.397 1.00 33.80 ? 1381 HOH A O 1 HETATM 3116 O O . HOH I 7 . ? 67.374 20.895 61.590 1.00 34.72 ? 1382 HOH A O 1 HETATM 3117 O O . HOH I 7 . ? 58.176 1.646 44.693 1.00 102.36 ? 1383 HOH A O 1 HETATM 3118 O O . HOH I 7 . ? 44.164 31.045 27.180 1.00 35.51 ? 1384 HOH A O 1 HETATM 3119 O O . HOH I 7 . ? 61.566 21.798 13.952 1.00 35.68 ? 1385 HOH A O 1 HETATM 3120 O O . HOH I 7 . ? 33.130 15.351 32.957 1.00 28.76 ? 1386 HOH A O 1 HETATM 3121 O O . HOH I 7 . ? 58.784 23.942 63.947 1.00 39.85 ? 1387 HOH A O 1 HETATM 3122 O O . HOH I 7 . ? 77.331 33.236 46.719 1.00 29.04 ? 1388 HOH A O 1 HETATM 3123 O O . HOH I 7 . ? 69.357 35.387 39.332 1.00 43.89 ? 1389 HOH A O 1 HETATM 3124 O O . HOH I 7 . ? 77.433 20.852 43.295 1.00 42.29 ? 1390 HOH A O 1 HETATM 3125 O O . HOH I 7 . ? 52.843 28.505 67.969 1.00 38.03 ? 1391 HOH A O 1 HETATM 3126 O O . HOH I 7 . ? 49.469 35.353 20.395 1.00 27.42 ? 1392 HOH A O 1 HETATM 3127 O O . HOH I 7 . ? 33.479 45.307 59.921 1.00 34.25 ? 1393 HOH A O 1 HETATM 3128 O O . HOH I 7 . ? 66.002 10.930 44.292 1.00 31.20 ? 1394 HOH A O 1 HETATM 3129 O O . HOH I 7 . ? 53.245 4.660 25.055 1.00 46.11 ? 1395 HOH A O 1 HETATM 3130 O O . HOH I 7 . ? 48.442 45.962 50.129 1.00 35.59 ? 1396 HOH A O 1 HETATM 3131 O O . HOH I 7 . ? 44.593 32.555 21.441 1.00 51.18 ? 1397 HOH A O 1 HETATM 3132 O O . HOH I 7 . ? 31.069 38.575 58.287 1.00 27.69 ? 1398 HOH A O 1 HETATM 3133 O O . HOH I 7 . ? 32.379 42.633 60.273 1.00 25.92 ? 1401 HOH A O 1 HETATM 3134 O O . HOH I 7 . ? 59.820 29.594 39.581 1.00 19.28 ? 1402 HOH A O 1 HETATM 3135 O O . HOH I 7 . ? 63.070 13.168 59.745 1.00 31.82 ? 1403 HOH A O 1 HETATM 3136 O O . HOH I 7 . ? 52.939 46.066 56.479 1.00 48.98 ? 1404 HOH A O 1 HETATM 3137 O O . HOH I 7 . ? 35.305 24.442 38.131 1.00 53.40 ? 1405 HOH A O 1 HETATM 3138 O O . HOH I 7 . ? 63.174 43.455 61.874 1.00 40.89 ? 1406 HOH A O 1 HETATM 3139 O O . HOH I 7 . ? 65.985 24.309 62.071 1.00 30.33 ? 1407 HOH A O 1 HETATM 3140 O O . HOH I 7 . ? 68.790 23.490 62.608 1.00 29.81 ? 1408 HOH A O 1 HETATM 3141 O O . HOH I 7 . ? 73.694 15.743 51.013 1.00 29.44 ? 1409 HOH A O 1 HETATM 3142 O O . HOH I 7 . ? 61.155 20.341 39.306 1.00 91.39 ? 1410 HOH A O 1 HETATM 3143 O O . HOH I 7 . ? 65.092 5.300 42.691 1.00 45.22 ? 1411 HOH A O 1 HETATM 3144 O O . HOH I 7 . ? 67.962 20.067 17.149 1.00 43.52 ? 1412 HOH A O 1 HETATM 3145 O O . HOH I 7 . ? 35.743 24.574 31.862 1.00 52.35 ? 1413 HOH A O 1 HETATM 3146 O O . HOH I 7 . ? 48.096 16.915 12.092 1.00 56.63 ? 1414 HOH A O 1 HETATM 3147 O O . HOH I 7 . ? 51.888 22.530 9.790 1.00 50.88 ? 1415 HOH A O 1 HETATM 3148 O O . HOH I 7 . ? 46.117 30.188 22.930 1.00 23.47 ? 1416 HOH A O 1 HETATM 3149 O O . HOH I 7 . ? 47.458 30.853 25.992 1.00 30.83 ? 1417 HOH A O 1 HETATM 3150 O O . HOH I 7 . ? 65.604 31.331 25.026 1.00 52.67 ? 1418 HOH A O 1 HETATM 3151 O O . HOH I 7 . ? 73.410 37.371 49.327 1.00 37.74 ? 1419 HOH A O 1 HETATM 3152 O O . HOH I 7 . ? 57.212 26.301 66.397 1.00 74.26 ? 1420 HOH A O 1 HETATM 3153 O O . HOH I 7 . ? 35.379 20.243 15.206 1.00 54.09 ? 1421 HOH A O 1 HETATM 3154 O O . HOH I 7 . ? 44.684 39.678 30.604 1.00 30.53 ? 1423 HOH A O 1 HETATM 3155 O O . HOH I 7 . ? 55.567 40.120 26.804 1.00 28.63 ? 1424 HOH A O 1 HETATM 3156 O O . HOH I 7 . ? 65.264 12.673 29.667 1.00 34.72 ? 1425 HOH A O 1 HETATM 3157 O O . HOH I 7 . ? 39.464 37.600 49.347 1.00 33.38 ? 1426 HOH A O 1 HETATM 3158 O O . HOH I 7 . ? 76.154 35.772 50.245 1.00 45.95 ? 1427 HOH A O 1 HETATM 3159 O O . HOH I 7 . ? 48.035 39.215 28.354 1.00 52.00 ? 1428 HOH A O 1 HETATM 3160 O O . HOH I 7 . ? 39.622 41.454 52.547 1.00 55.97 ? 1429 HOH A O 1 HETATM 3161 O O . HOH I 7 . ? 36.618 5.936 32.639 1.00 44.08 ? 1430 HOH A O 1 HETATM 3162 O O . HOH I 7 . ? 63.308 9.921 26.901 1.00 30.35 ? 1431 HOH A O 1 HETATM 3163 O O . HOH I 7 . ? 67.750 43.321 50.875 1.00 39.96 ? 1432 HOH A O 1 HETATM 3164 O O . HOH I 7 . ? 37.093 32.497 35.038 1.00 33.50 ? 1433 HOH A O 1 HETATM 3165 O O . HOH I 7 . ? 44.889 34.667 65.907 1.00 40.82 ? 1434 HOH A O 1 HETATM 3166 O O . HOH I 7 . ? 37.427 29.200 54.027 1.00 37.52 ? 1435 HOH A O 1 HETATM 3167 O O . HOH I 7 . ? 53.753 52.055 49.636 1.00 49.00 ? 1436 HOH A O 1 HETATM 3168 O O . HOH I 7 . ? 57.403 14.745 10.293 1.00 51.63 ? 1437 HOH A O 1 HETATM 3169 O O . HOH I 7 . ? 69.395 18.967 33.137 1.00 33.22 ? 1438 HOH A O 1 HETATM 3170 O O . HOH I 7 . ? 50.889 19.868 9.107 1.00 50.51 ? 1439 HOH A O 1 HETATM 3171 O O . HOH I 7 . ? 65.921 45.542 43.672 1.00 86.26 ? 1440 HOH A O 1 HETATM 3172 O O . HOH I 7 . ? 57.512 37.980 27.457 1.00 37.89 ? 1441 HOH A O 1 HETATM 3173 O O . HOH I 7 . ? 42.537 25.293 9.148 1.00 58.51 ? 1442 HOH A O 1 HETATM 3174 O O . HOH I 7 . ? 61.771 28.740 65.412 1.00 31.04 ? 1443 HOH A O 1 HETATM 3175 O O . HOH I 7 . ? 35.623 22.339 40.615 1.00 37.35 ? 1444 HOH A O 1 HETATM 3176 O O . HOH I 7 . ? 57.615 4.637 27.142 1.00 37.46 ? 1445 HOH A O 1 HETATM 3177 O O . HOH I 7 . ? 62.005 17.294 59.757 1.00 46.80 ? 1446 HOH A O 1 HETATM 3178 O O . HOH I 7 . ? 67.088 12.144 47.206 1.00 55.06 ? 1447 HOH A O 1 HETATM 3179 O O . HOH I 7 . ? 41.110 18.262 9.722 1.00 49.82 ? 1448 HOH A O 1 HETATM 3180 O O . HOH I 7 . ? 30.679 6.316 26.522 1.00 40.03 ? 1449 HOH A O 1 HETATM 3181 O O . HOH I 7 . ? 36.080 41.935 67.502 1.00 75.82 ? 1450 HOH A O 1 HETATM 3182 O O . HOH I 7 . ? 55.027 7.512 19.962 1.00 32.24 ? 1451 HOH A O 1 HETATM 3183 O O . HOH I 7 . ? 34.202 22.738 34.803 1.00 43.84 ? 1452 HOH A O 1 HETATM 3184 O O . HOH I 7 . ? 55.073 17.343 66.835 1.00 44.03 ? 1453 HOH A O 1 HETATM 3185 O O . HOH I 7 . ? 49.194 7.016 16.604 1.00 39.12 ? 1454 HOH A O 1 HETATM 3186 O O . HOH I 7 . ? 50.675 46.768 51.567 1.00 41.16 ? 1455 HOH A O 1 HETATM 3187 O O . HOH I 7 . ? 59.747 39.224 33.773 1.00 33.04 ? 1456 HOH A O 1 HETATM 3188 O O . HOH I 7 . ? 63.017 46.635 50.678 1.00 78.66 ? 1457 HOH A O 1 HETATM 3189 O O . HOH I 7 . ? 48.197 49.943 47.402 1.00 43.97 ? 1458 HOH A O 1 HETATM 3190 O O . HOH I 7 . ? 47.292 40.433 32.107 1.00 58.52 ? 1459 HOH A O 1 HETATM 3191 O O . HOH I 7 . ? 36.706 36.492 50.774 1.00 60.19 ? 1460 HOH A O 1 HETATM 3192 O O . HOH I 7 . ? 44.657 43.877 23.725 1.00 43.59 ? 1461 HOH A O 1 HETATM 3193 O O . HOH I 7 . ? 60.768 -1.456 34.319 1.00 37.33 ? 1462 HOH A O 1 HETATM 3194 O O . HOH I 7 . ? 43.363 29.751 18.982 1.00 45.08 ? 1463 HOH A O 1 HETATM 3195 O O . HOH I 7 . ? 74.225 39.738 44.870 1.00 51.64 ? 1464 HOH A O 1 HETATM 3196 O O . HOH I 7 . ? 59.102 7.244 53.998 1.00 58.08 ? 1465 HOH A O 1 HETATM 3197 O O . HOH I 7 . ? 56.139 10.313 18.643 1.00 38.55 ? 1466 HOH A O 1 HETATM 3198 O O . HOH I 7 . ? 44.688 16.567 52.166 1.00 34.07 ? 1467 HOH A O 1 HETATM 3199 O O . HOH I 7 . ? 43.800 16.295 65.294 1.00 44.97 ? 1468 HOH A O 1 HETATM 3200 O O . HOH I 7 . ? 57.067 47.062 57.152 1.00 35.19 ? 1469 HOH A O 1 HETATM 3201 O O . HOH I 7 . ? 79.099 28.093 42.801 1.00 39.76 ? 1470 HOH A O 1 HETATM 3202 O O . HOH I 7 . ? 36.829 35.122 35.832 1.00 32.14 ? 1471 HOH A O 1 HETATM 3203 O O . HOH I 7 . ? 36.998 18.860 13.308 1.00 68.77 ? 1472 HOH A O 1 HETATM 3204 O O . HOH I 7 . ? 75.611 35.795 45.922 1.00 41.49 ? 1473 HOH A O 1 HETATM 3205 O O . HOH I 7 . ? 38.555 40.178 37.607 1.00 87.02 ? 1474 HOH A O 1 HETATM 3206 O O . HOH I 7 . ? 56.282 5.034 53.028 1.00 49.28 ? 1475 HOH A O 1 HETATM 3207 O O . HOH I 7 . ? 43.873 14.091 51.746 1.00 51.58 ? 1477 HOH A O 1 HETATM 3208 O O . HOH I 7 . ? 40.478 22.936 54.237 1.00 42.10 ? 1478 HOH A O 1 HETATM 3209 O O . HOH I 7 . ? 66.290 40.784 37.600 1.00 55.29 ? 1479 HOH A O 1 HETATM 3210 O O . HOH I 7 . ? 43.454 42.392 45.882 1.00 36.69 ? 1480 HOH A O 1 HETATM 3211 O O . HOH I 7 . ? 68.832 42.543 53.365 1.00 51.39 ? 1481 HOH A O 1 HETATM 3212 O O . HOH I 7 . ? 74.389 17.127 49.145 1.00 38.40 ? 1482 HOH A O 1 HETATM 3213 O O . HOH I 7 . ? 61.940 7.815 59.149 1.00 52.26 ? 1483 HOH A O 1 HETATM 3214 O O . HOH I 7 . ? 35.898 38.833 52.925 1.00 43.60 ? 1484 HOH A O 1 HETATM 3215 O O . HOH I 7 . ? 40.369 37.867 43.803 1.00 30.68 ? 1485 HOH A O 1 HETATM 3216 O O . HOH I 7 . ? 32.843 21.376 13.207 1.00 53.67 ? 1486 HOH A O 1 HETATM 3217 O O . HOH I 7 . ? 65.399 47.366 56.350 1.00 55.73 ? 1487 HOH A O 1 HETATM 3218 O O . HOH I 7 . ? 59.300 46.583 56.267 1.00 97.80 ? 1488 HOH A O 1 HETATM 3219 O O . HOH I 7 . ? 60.910 4.794 30.680 1.00 43.19 ? 1489 HOH A O 1 HETATM 3220 O O . HOH I 7 . ? 64.204 37.738 34.883 1.00 46.22 ? 1490 HOH A O 1 HETATM 3221 O O . HOH I 7 . ? 50.280 39.983 63.976 1.00 67.57 ? 1491 HOH A O 1 HETATM 3222 O O . HOH I 7 . ? 28.924 37.852 57.887 1.00 52.97 ? 1492 HOH A O 1 HETATM 3223 O O . HOH I 7 . ? 36.431 35.871 41.115 1.00 64.39 ? 1493 HOH A O 1 HETATM 3224 O O . HOH I 7 . ? 31.753 13.453 27.520 1.00 49.57 ? 1494 HOH A O 1 HETATM 3225 O O . HOH I 7 . ? 71.913 40.705 49.404 1.00 71.43 ? 1495 HOH A O 1 HETATM 3226 O O . HOH I 7 . ? 50.582 17.590 9.169 1.00 49.15 ? 1496 HOH A O 1 HETATM 3227 O O . HOH I 7 . ? 70.777 41.244 46.025 1.00 42.04 ? 1497 HOH A O 1 HETATM 3228 O O . HOH I 7 . ? 38.715 35.640 66.335 1.00 58.93 ? 1498 HOH A O 1 HETATM 3229 O O . HOH I 7 . ? 63.582 20.163 16.304 1.00 46.30 ? 1499 HOH A O 1 HETATM 3230 O O . HOH I 7 . ? 71.643 11.418 48.598 1.00 83.25 ? 1500 HOH A O 1 HETATM 3231 O O . HOH I 7 . ? 60.437 21.932 37.909 1.00 73.62 ? 1501 HOH A O 1 HETATM 3232 O O . HOH I 7 . ? 59.700 28.979 37.010 1.00 38.07 ? 1502 HOH A O 1 HETATM 3233 O O . HOH I 7 . ? 59.207 35.387 38.656 1.00 33.02 ? 1503 HOH A O 1 HETATM 3234 O O . HOH I 7 . ? 39.788 21.748 29.124 1.00 18.29 ? 1504 HOH A O 1 HETATM 3235 O O . HOH I 7 . ? 33.446 18.318 35.588 1.00 32.65 ? 1505 HOH A O 1 HETATM 3236 O O . HOH I 7 . ? 40.087 25.469 28.743 1.00 31.31 ? 1506 HOH A O 1 HETATM 3237 O O . HOH I 7 . ? 40.134 38.726 52.809 1.00 36.96 ? 1507 HOH A O 1 HETATM 3238 O O . HOH I 7 . ? 38.059 22.248 43.698 1.00 39.54 ? 1508 HOH A O 1 HETATM 3239 O O . HOH I 7 . ? 41.595 35.005 67.594 1.00 50.83 ? 1509 HOH A O 1 HETATM 3240 O O . HOH I 7 . ? 39.703 14.969 15.407 1.00 35.78 ? 1510 HOH A O 1 HETATM 3241 O O . HOH I 7 . ? 33.170 32.291 41.564 1.00 50.42 ? 1511 HOH A O 1 HETATM 3242 O O . HOH I 7 . ? 51.781 41.592 32.141 1.00 50.19 ? 1512 HOH A O 1 HETATM 3243 O O . HOH I 7 . ? 77.127 25.916 41.874 1.00 55.95 ? 1513 HOH A O 1 HETATM 3244 O O . HOH I 7 . ? 32.476 8.732 27.569 1.00 40.79 ? 1514 HOH A O 1 HETATM 3245 O O . HOH I 7 . ? 37.834 23.363 30.113 1.00 33.21 ? 1515 HOH A O 1 HETATM 3246 O O . HOH I 7 . ? 36.048 33.333 52.944 1.00 45.96 ? 1516 HOH A O 1 HETATM 3247 O O . HOH I 7 . ? 35.775 25.494 42.982 1.00 46.28 ? 1517 HOH A O 1 HETATM 3248 O O . HOH I 7 . ? 47.338 5.920 18.186 1.00 54.38 ? 1518 HOH A O 1 HETATM 3249 O O . HOH I 7 . ? 43.880 34.060 29.942 1.00 46.08 ? 1519 HOH A O 1 HETATM 3250 O O . HOH I 7 . ? 35.950 10.736 38.640 1.00 46.11 ? 1520 HOH A O 1 HETATM 3251 O O . HOH I 7 . ? 70.157 30.841 40.141 1.00 52.08 ? 1521 HOH A O 1 HETATM 3252 O O . HOH I 7 . ? 64.234 43.785 36.456 1.00 51.27 ? 1522 HOH A O 1 HETATM 3253 O O . HOH I 7 . ? 59.152 30.667 33.681 1.00 52.53 ? 1523 HOH A O 1 HETATM 3254 O O . HOH I 7 . ? 60.917 35.554 34.428 1.00 48.58 ? 1524 HOH A O 1 HETATM 3255 O O . HOH I 7 . ? 42.832 43.068 37.084 1.00 73.00 ? 1525 HOH A O 1 HETATM 3256 O O . HOH I 7 . ? 69.367 16.026 62.677 1.00 56.93 ? 1526 HOH A O 1 HETATM 3257 O O . HOH I 7 . ? 33.250 46.319 62.477 1.00 59.62 ? 1527 HOH A O 1 HETATM 3258 O O . HOH I 7 . ? 60.529 43.272 62.706 1.00 73.42 ? 1528 HOH A O 1 HETATM 3259 O O . HOH I 7 . ? 65.714 47.567 58.827 1.00 49.35 ? 1529 HOH A O 1 HETATM 3260 O O . HOH I 7 . ? 35.327 39.414 64.555 1.00 49.09 ? 1530 HOH A O 1 HETATM 3261 O O . HOH I 7 . ? 72.506 15.614 48.731 1.00 50.21 ? 1531 HOH A O 1 HETATM 3262 O O . HOH I 7 . ? 71.689 14.174 53.869 1.00 67.38 ? 1532 HOH A O 1 HETATM 3263 O O . HOH I 7 . ? 34.808 38.972 55.872 1.00 42.86 ? 1533 HOH A O 1 HETATM 3264 O O . HOH I 7 . ? 37.729 16.105 13.298 1.00 51.73 ? 1534 HOH A O 1 HETATM 3265 O O . HOH I 7 . ? 45.109 1.011 20.043 1.00 58.75 ? 1535 HOH A O 1 HETATM 3266 O O . HOH I 7 . ? 36.647 20.963 49.900 1.00 57.61 ? 1536 HOH A O 1 HETATM 3267 O O . HOH I 7 . ? 65.109 38.015 61.395 1.00 52.60 ? 1537 HOH A O 1 HETATM 3268 O O . HOH I 7 . ? 51.278 0.898 30.260 1.00 77.46 ? 1538 HOH A O 1 HETATM 3269 O O . HOH I 7 . ? 33.336 26.561 39.963 1.00 46.83 ? 1539 HOH A O 1 HETATM 3270 O O . HOH I 7 . ? 64.321 4.957 58.839 1.00 52.78 ? 1540 HOH A O 1 HETATM 3271 O O . HOH I 7 . ? 62.107 1.740 33.952 1.00 59.52 ? 1541 HOH A O 1 HETATM 3272 O O . HOH I 7 . ? 33.053 36.856 57.296 1.00 54.26 ? 1542 HOH A O 1 HETATM 3273 O O . HOH I 7 . ? 69.656 11.052 35.266 1.00 60.30 ? 1543 HOH A O 1 HETATM 3274 O O . HOH I 7 . ? 51.119 6.693 18.515 1.00 59.06 ? 1544 HOH A O 1 HETATM 3275 O O . HOH I 7 . ? 65.419 25.729 63.792 1.00 62.24 ? 1545 HOH A O 1 HETATM 3276 O O . HOH I 7 . ? 38.677 42.328 66.136 1.00 43.98 ? 1546 HOH A O 1 HETATM 3277 O O . HOH I 7 . ? 69.271 30.187 33.833 1.00 97.57 ? 1547 HOH A O 1 HETATM 3278 O O . HOH I 7 . ? 63.060 46.858 53.668 1.00 51.22 ? 1548 HOH A O 1 HETATM 3279 O O . HOH I 7 . ? 37.882 26.952 54.085 1.00 44.44 ? 1549 HOH A O 1 HETATM 3280 O O . HOH I 7 . ? 58.776 47.733 49.808 1.00 57.77 ? 1550 HOH A O 1 HETATM 3281 O O . HOH I 7 . ? 62.521 39.784 33.922 1.00 53.11 ? 1551 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 18 S SG . CYS A 3 ? 0.3475 0.3824 0.2610 0.0407 0.0093 -0.0147 3 CYS A SG 94 S SG . CYS A 14 ? 0.2858 0.3532 0.1722 -0.0338 -0.0222 0.0009 14 CYS A SG 100 S SG . CYS A 15 ? 0.3674 0.3113 0.2677 0.0482 0.0005 -0.0248 15 CYS A SG 245 S SG . CYS A 33 ? 0.2580 0.1716 0.1841 0.0090 -0.0389 -0.0068 33 CYS A SG 492 S SD . MET A 67 ? 0.2108 0.2261 0.2824 -0.0159 -0.0085 0.0126 67 MET A SD 705 S SD . MET A 94 ? 0.2959 0.2349 0.2198 -0.0281 -0.0818 -0.0270 94 MET A SD 870 S SG . CYS A 117 ? 0.2529 0.1578 0.1834 -0.0028 -0.0366 -0.0245 117 CYS A SG 1759 S SD . MET A 237 ? 0.2565 0.2151 0.2303 -0.0423 -0.0634 -0.0329 237 MET A SD 1885 S SG . CYS A 253 ? 0.3342 0.1722 0.2218 0.0037 -0.0672 -0.0238 253 CYS A SG 1987 S SD . MET A 265 ? 0.2270 0.2460 0.2028 -0.0175 -0.0286 0.0073 265 MET A SD 2043 S SD . MET A 273 ? 0.2398 0.2582 0.2848 0.0084 -0.0436 0.0410 273 MET A SD 2166 S SG . CYS A 289 ? 0.2773 0.3435 0.2155 -0.0098 -0.0705 -0.0119 289 CYS A SG 2275 S SD . MET A 305 ? 0.2649 0.1890 0.3701 0.0324 -0.0728 0.0580 305 MET A SD 2377 S SG . CYS A 319 ? 0.2702 0.1976 0.2399 -0.0099 -0.0408 0.0099 319 CYS A SG 2540 S SG . CYS A 341 ? 0.6302 0.2057 0.2005 0.0092 -0.0521 0.0066 341 CYS A SG 2572 S SD . MET A 346 ? 0.7543 1.2994 0.9123 0.7662 0.0874 -0.5348 346 MET A SD 2585 S SG . CYS A 348 ? 0.6003 0.2007 0.2364 0.0368 -0.0963 -0.0369 348 CYS A SG 2688 CA CA . CA E . ? 0.2028 0.2035 0.1848 -0.0102 -0.0592 0.0055 371 CA A CA 2689 CA CA . CA F . ? 0.1807 0.1922 0.1731 -0.0093 -0.0427 -0.0069 372 CA A CA 2732 FE FE . HEM G . ? 0.2539 0.2401 0.2047 -0.0131 -0.0418 -0.0134 396 HEM A FE # 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 ALA 1 1 1 ALA ALA A . n A 1 2 VAL 2 2 2 VAL VAL A . n A 1 3 CYS 3 3 3 CYS CYS A . n A 1 4 PRO 4 4 4 PRO PRO A . n A 1 5 ASP 5 5 5 ASP ASP A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 THR 7 7 7 THR THR A . n A 1 8 ARG 8 8 8 ARG ARG A . n A 1 9 VAL 9 9 9 VAL VAL A . n A 1 10 SER 10 10 10 SER SER A . n A 1 11 HIS 11 11 11 HIS HIS A . n A 1 12 ALA 12 12 12 ALA ALA A . n A 1 13 ALA 13 13 13 ALA ALA A . n A 1 14 CYS 14 14 14 CYS CYS A . n A 1 15 CYS 15 15 15 CYS CYS A . n A 1 16 ALA 16 16 16 ALA ALA A . n A 1 17 PHE 17 17 17 PHE PHE A . n A 1 18 ILE 18 18 18 ILE ILE A . n A 1 19 PRO 19 19 19 PRO PRO A . n A 1 20 LEU 20 20 20 LEU LEU A . n A 1 21 ALA 21 21 21 ALA ALA A . n A 1 22 GLN 22 22 22 GLN GLN A . n A 1 23 ASP 23 23 23 ASP ASP A . n A 1 24 LEU 24 24 24 LEU LEU A . n A 1 25 GLN 25 25 25 GLN GLN A . n A 1 26 GLU 26 26 26 GLU GLN A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 ILE 28 28 28 ILE ILE A . n A 1 29 PHE 29 29 29 PHE PHE A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 ASN 31 31 31 ASN ASN A . n A 1 32 GLU 32 32 32 GLU GLU A . n A 1 33 CYS 33 33 33 CYS CYS A . n A 1 34 GLY 34 34 34 GLY GLY A . n A 1 35 GLU 35 35 35 GLU GLU A . n A 1 36 ASP 36 36 36 ASP ASP A . n A 1 37 ALA 37 37 37 ALA ALA A . n A 1 38 HIS 38 38 38 HIS HIS A . n A 1 39 GLU 39 39 39 GLU GLU A . n A 1 40 VAL 40 40 40 VAL VAL A . n A 1 41 ILE 41 41 41 ILE ILE A . n A 1 42 ARG 42 42 42 ARG ARG A . n A 1 43 LEU 43 43 43 LEU LEU A . n A 1 44 THR 44 44 44 THR THR A . n A 1 45 PHE 45 45 45 PHE PHE A . n A 1 46 HIS 46 46 46 HIS HIS A . n A 1 47 ASP 47 47 47 ASP ASP A . n A 1 48 ALA 48 48 48 ALA ALA A . n A 1 49 ILE 49 49 49 ILE ILE A . n A 1 50 ALA 50 50 50 ALA ALA A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 SER 52 52 52 SER SER A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 SER 54 54 54 SER SER A . n A 1 55 GLN 55 55 55 GLN GLN A . n A 1 56 GLY 56 56 56 GLY GLY A . n A 1 57 PRO 57 57 57 PRO PRO A . n A 1 58 LYS 58 58 58 LYS LYS A . n A 1 59 ALA 59 59 59 ALA ALA A . n A 1 60 GLY 60 60 60 GLY GLY A . n A 1 61 GLY 61 61 61 GLY GLY A . n A 1 62 GLY 62 62 62 GLY GLY A . n A 1 63 ALA 63 63 63 ALA ALA A . n A 1 64 ASP 64 64 64 ASP ASP A . n A 1 65 GLY 65 65 65 GLY GLY A . n A 1 66 SER 66 66 66 SER SER A . n A 1 67 MET 67 67 67 MET MET A . n A 1 68 LEU 68 68 68 LEU LEU A . n A 1 69 LEU 69 69 69 LEU LEU A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 PRO 71 71 71 PRO PRO A . n A 1 72 THR 72 72 72 THR THR A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 GLU 74 74 74 GLU GLU A . n A 1 75 PRO 75 75 75 PRO PRO A . n A 1 76 ASN 76 76 76 ASN ASN A . n A 1 77 PHE 77 77 77 PHE PHE A . n A 1 78 SER 78 78 78 SER SER A . n A 1 79 ALA 79 79 79 ALA ALA A . n A 1 80 ASN 80 80 80 ASN ASN A . n A 1 81 ASN 81 81 81 ASN ASN A . n A 1 82 GLY 82 82 82 GLY GLY A . n A 1 83 ILE 83 83 83 ILE ILE A . n A 1 84 ASP 84 84 84 ASP ASP A . n A 1 85 ASP 85 85 85 ASP ASP A . n A 1 86 SER 86 86 86 SER SER A . n A 1 87 VAL 87 87 87 VAL VAL A . n A 1 88 ASN 88 88 88 ASN ASN A . n A 1 89 ASN 89 89 89 ASN ASN A . n A 1 90 LEU 90 90 90 LEU LEU A . n A 1 91 ILE 91 91 91 ILE ILE A . n A 1 92 PRO 92 92 92 PRO PRO A . n A 1 93 PHE 93 93 93 PHE PHE A . n A 1 94 MET 94 94 94 MET MET A . n A 1 95 GLN 95 95 95 GLN GLN A . n A 1 96 LYS 96 96 96 LYS LYS A . n A 1 97 HIS 97 97 97 HIS HIS A . n A 1 98 ASN 98 98 98 ASN ASN A . n A 1 99 THR 99 99 99 THR THR A . n A 1 100 ILE 100 100 100 ILE ILE A . n A 1 101 SER 101 101 101 SER SER A . n A 1 102 ALA 102 102 102 ALA ALA A . n A 1 103 ALA 103 103 103 ALA ALA A . n A 1 104 ASP 104 104 104 ASP ASP A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 VAL 106 106 106 VAL VAL A . n A 1 107 GLN 107 107 107 GLN GLN A . n A 1 108 PHE 108 108 108 PHE PHE A . n A 1 109 ALA 109 109 109 ALA ALA A . n A 1 110 GLY 110 110 110 GLY GLY A . n A 1 111 ALA 111 111 111 ALA ALA A . n A 1 112 VAL 112 112 112 VAL VAL A . n A 1 113 ALA 113 113 113 ALA ALA A . n A 1 114 LEU 114 114 114 LEU LEU A . n A 1 115 SER 115 115 115 SER SER A . n A 1 116 ASN 116 116 116 ASN ASN A . n A 1 117 CYS 117 117 117 CYS CYS A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 GLY 119 119 119 GLY GLY A . n A 1 120 ALA 120 120 120 ALA ALA A . n A 1 121 PRO 121 121 121 PRO PRO A . n A 1 122 ARG 122 122 122 ARG ARG A . n A 1 123 LEU 123 123 123 LEU LEU A . n A 1 124 GLU 124 124 124 GLU GLU A . n A 1 125 PHE 125 125 125 PHE PHE A . n A 1 126 LEU 126 126 126 LEU LEU A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 ARG 129 129 129 ARG ARG A . n A 1 130 PRO 130 130 130 PRO PRO A . n A 1 131 ASN 131 131 131 ASN ASN A . n A 1 132 LYS 132 132 132 LYS LYS A . n A 1 133 THR 133 133 133 THR THR A . n A 1 134 ILE 134 134 134 ILE ILE A . n A 1 135 ALA 135 135 135 ALA ALA A . n A 1 136 ALA 136 136 136 ALA ALA A . n A 1 137 VAL 137 137 137 VAL VAL A . n A 1 138 ASP 138 138 138 ASP ASP A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 LEU 140 140 140 LEU LEU A . n A 1 141 ILE 141 141 141 ILE ILE A . n A 1 142 PRO 142 142 142 PRO PRO A . n A 1 143 GLU 143 143 143 GLU GLU A . n A 1 144 PRO 144 144 144 PRO PRO A . n A 1 145 GLN 145 145 145 GLN GLN A . n A 1 146 ASP 146 146 146 ASP ASP A . n A 1 147 SER 147 147 147 SER SER A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 THR 149 149 149 THR THR A . n A 1 150 LYS 150 150 150 LYS LYS A . n A 1 151 ILE 151 151 151 ILE ILE A . n A 1 152 LEU 152 152 152 LEU LEU A . n A 1 153 GLN 153 153 153 GLN GLN A . n A 1 154 ARG 154 154 154 ARG ARG A . n A 1 155 PHE 155 155 155 PHE PHE A . n A 1 156 GLU 156 156 156 GLU GLU A . n A 1 157 ASP 157 157 157 ASP ASP A . n A 1 158 ALA 158 158 158 ALA ALA A . n A 1 159 GLY 159 159 159 GLY GLY A . n A 1 160 GLY 160 160 160 GLY GLY A . n A 1 161 PHE 161 161 161 PHE PHE A . n A 1 162 THR 162 162 162 THR THR A . n A 1 163 PRO 163 163 163 PRO PRO A . n A 1 164 PHE 164 164 164 PHE PHE A . n A 1 165 GLU 165 165 165 GLU GLU A . n A 1 166 VAL 166 166 166 VAL VAL A . n A 1 167 VAL 167 167 167 VAL VAL A . n A 1 168 SER 168 168 168 SER SER A . n A 1 169 LEU 169 169 169 LEU LEU A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 ALA 171 171 171 ALA ALA A . n A 1 172 SER 172 172 172 SER SER A . n A 1 173 HIS 173 173 173 HIS HIS A . n A 1 174 SER 174 174 174 SER SER A . n A 1 175 VAL 175 175 175 VAL VAL A . n A 1 176 ALA 176 176 176 ALA ALA A . n A 1 177 ARG 177 177 177 ARG ARG A . n A 1 178 ALA 178 178 178 ALA ALA A . n A 1 179 ASP 179 179 179 ASP ASP A . n A 1 180 LYS 180 180 180 LYS LYS A . n A 1 181 VAL 181 181 181 VAL VAL A . n A 1 182 ASP 182 182 182 ASP ASP A . n A 1 183 GLN 183 183 183 GLN GLN A . n A 1 184 THR 184 184 184 THR THR A . n A 1 185 ILE 185 185 185 ILE ILE A . n A 1 186 ASP 186 186 186 ASP ASP A . n A 1 187 ALA 187 187 187 ALA ALA A . n A 1 188 ALA 188 188 188 ALA ALA A . n A 1 189 PRO 189 189 189 PRO PRO A . n A 1 190 PHE 190 190 190 PHE PHE A . n A 1 191 ASP 191 191 191 ASP ASP A . n A 1 192 SER 192 192 192 SER SER A . n A 1 193 THR 193 193 193 THR THR A . n A 1 194 PRO 194 194 194 PRO PRO A . n A 1 195 PHE 195 195 195 PHE PHE A . n A 1 196 THR 196 196 196 THR THR A . n A 1 197 PHE 197 197 197 PHE PHE A . n A 1 198 ASP 198 198 198 ASP ASP A . n A 1 199 THR 199 199 199 THR THR A . n A 1 200 GLN 200 200 200 GLN GLN A . n A 1 201 VAL 201 201 201 VAL VAL A . n A 1 202 PHE 202 202 202 PHE PHE A . n A 1 203 LEU 203 203 203 LEU LEU A . n A 1 204 GLU 204 204 204 GLU GLU A . n A 1 205 VAL 205 205 205 VAL VAL A . n A 1 206 LEU 206 206 206 LEU LEU A . n A 1 207 LEU 207 207 207 LEU LEU A . n A 1 208 LYS 208 208 208 LYS LYS A . n A 1 209 GLY 209 209 209 GLY GLY A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 GLY 211 211 211 GLY GLY A . n A 1 212 PHE 212 212 212 PHE PHE A . n A 1 213 PRO 213 213 213 PRO PRO A . n A 1 214 GLY 214 214 214 GLY GLY A . n A 1 215 SER 215 215 215 SER SER A . n A 1 216 ALA 216 216 216 ALA ALA A . n A 1 217 ASN 217 217 217 ASN ASN A . n A 1 218 ASN 218 218 218 ASN ASN A . n A 1 219 THR 219 219 219 THR THR A . n A 1 220 GLY 220 220 220 GLY GLY A . n A 1 221 GLU 221 221 221 GLU GLU A . n A 1 222 VAL 222 222 222 VAL VAL A . n A 1 223 ALA 223 223 223 ALA ALA A . n A 1 224 SER 224 224 224 SER SER A . n A 1 225 PRO 225 225 225 PRO PRO A . n A 1 226 LEU 226 226 226 LEU LEU A . n A 1 227 PRO 227 227 227 PRO PRO A . n A 1 228 LEU 228 228 228 LEU LEU A . n A 1 229 GLY 229 229 229 GLY GLY A . n A 1 230 SER 230 230 230 SER SER A . n A 1 231 GLY 231 231 231 GLY GLY A . n A 1 232 SER 232 232 232 SER SER A . n A 1 233 ASP 233 233 233 ASP ASP A . n A 1 234 THR 234 234 234 THR THR A . n A 1 235 GLY 235 235 235 GLY GLY A . n A 1 236 GLU 236 236 236 GLU GLU A . n A 1 237 MET 237 237 237 MET MET A . n A 1 238 ARG 238 238 238 ARG ARG A . n A 1 239 LEU 239 239 239 LEU LEU A . n A 1 240 GLN 240 240 240 GLN GLN A . n A 1 241 SER 241 241 241 SER SER A . n A 1 242 ASP 242 242 242 ASP ASP A . n A 1 243 PHE 243 243 243 PHE PHE A . n A 1 244 ALA 244 244 244 ALA ALA A . n A 1 245 LEU 245 245 245 LEU LEU A . n A 1 246 ALA 246 246 246 ALA ALA A . n A 1 247 HIS 247 247 247 HIS HIS A . n A 1 248 ASP 248 248 248 ASP ASP A . n A 1 249 PRO 249 249 249 PRO PRO A . n A 1 250 ARG 250 250 250 ARG ARG A . n A 1 251 THR 251 251 251 THR THR A . n A 1 252 ALA 252 252 252 ALA ALA A . n A 1 253 CYS 253 253 253 CYS CYS A . n A 1 254 ILE 254 254 254 ILE ILE A . n A 1 255 TRP 255 255 255 TRP TRP A . n A 1 256 GLN 256 256 256 GLN GLN A . n A 1 257 GLY 257 257 257 GLY GLY A . n A 1 258 PHE 258 258 258 PHE PHE A . n A 1 259 VAL 259 259 259 VAL VAL A . n A 1 260 ASN 260 260 260 ASN ASN A . n A 1 261 GLU 261 261 261 GLU GLU A . n A 1 262 GLN 262 262 262 GLN GLN A . n A 1 263 ALA 263 263 263 ALA ALA A . n A 1 264 PHE 264 264 264 PHE PHE A . n A 1 265 MET 265 265 265 MET MET A . n A 1 266 ALA 266 266 266 ALA ALA A . n A 1 267 ALA 267 267 267 ALA ALA A . n A 1 268 SER 268 268 268 SER SER A . n A 1 269 PHE 269 269 269 PHE PHE A . n A 1 270 ARG 270 270 270 ARG ARG A . n A 1 271 ALA 271 271 271 ALA ALA A . n A 1 272 ALA 272 272 272 ALA ALA A . n A 1 273 MET 273 273 273 MET MET A . n A 1 274 SER 274 274 274 SER SER A . n A 1 275 LYS 275 275 275 LYS LYS A . n A 1 276 LEU 276 276 276 LEU LEU A . n A 1 277 ALA 277 277 277 ALA ALA A . n A 1 278 VAL 278 278 278 VAL VAL A . n A 1 279 LEU 279 279 279 LEU LEU A . n A 1 280 GLY 280 280 280 GLY GLY A . n A 1 281 HIS 281 281 281 HIS HIS A . n A 1 282 ASN 282 282 282 ASN ASN A . n A 1 283 ARG 283 283 283 ARG ARG A . n A 1 284 ASN 284 284 284 ASN ASN A . n A 1 285 SER 285 285 285 SER SER A . n A 1 286 LEU 286 286 286 LEU LEU A . n A 1 287 ILE 287 287 287 ILE ILE A . n A 1 288 ASP 288 288 288 ASP ASP A . n A 1 289 CYS 289 289 289 CYS CYS A . n A 1 290 SER 290 290 290 SER SER A . n A 1 291 ASP 291 291 291 ASP ASP A . n A 1 292 VAL 292 292 292 VAL VAL A . n A 1 293 VAL 293 293 293 VAL VAL A . n A 1 294 PRO 294 294 294 PRO PRO A . n A 1 295 VAL 295 295 295 VAL VAL A . n A 1 296 PRO 296 296 296 PRO PRO A . n A 1 297 LYS 297 297 297 LYS LYS A . n A 1 298 PRO 298 298 298 PRO PRO A . n A 1 299 ALA 299 299 299 ALA ALA A . n A 1 300 THR 300 300 300 THR THR A . n A 1 301 GLY 301 301 301 GLY GLY A . n A 1 302 GLN 302 302 302 GLN GLN A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 ALA 304 304 304 ALA ALA A . n A 1 305 MET 305 305 305 MET MET A . n A 1 306 PHE 306 306 306 PHE PHE A . n A 1 307 PRO 307 307 307 PRO PRO A . n A 1 308 ALA 308 308 308 ALA ALA A . n A 1 309 SER 309 309 309 SER SER A . n A 1 310 THR 310 310 310 THR THR A . n A 1 311 GLY 311 311 311 GLY GLY A . n A 1 312 PRO 312 312 312 PRO PRO A . n A 1 313 GLN 313 313 313 GLN GLN A . n A 1 314 ASP 314 314 314 ASP ASP A . n A 1 315 LEU 315 315 315 LEU LEU A . n A 1 316 GLU 316 316 316 GLU GLU A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 SER 318 318 318 SER SER A . n A 1 319 CYS 319 319 319 CYS CYS A . n A 1 320 PRO 320 320 320 PRO PRO A . n A 1 321 SER 321 321 321 SER SER A . n A 1 322 GLU 322 322 322 GLU GLU A . n A 1 323 ARG 323 323 323 ARG ARG A . n A 1 324 PHE 324 324 324 PHE PHE A . n A 1 325 PRO 325 325 325 PRO PRO A . n A 1 326 THR 326 326 326 THR THR A . n A 1 327 LEU 327 327 327 LEU LEU A . n A 1 328 THR 328 328 328 THR THR A . n A 1 329 THR 329 329 329 THR THR A . n A 1 330 GLN 330 330 330 GLN GLN A . n A 1 331 PRO 331 331 331 PRO PRO A . n A 1 332 GLY 332 332 332 GLY GLY A . n A 1 333 ALA 333 333 333 ALA ALA A . n A 1 334 SER 334 334 334 SER SER A . n A 1 335 GLN 335 335 335 GLN GLN A . n A 1 336 SER 336 336 336 SER SER A . n A 1 337 LEU 337 337 337 LEU LEU A . n A 1 338 ILE 338 338 338 ILE ILE A . n A 1 339 ALA 339 339 339 ALA ALA A . n A 1 340 HIS 340 340 340 HIS HIS A . n A 1 341 CYS 341 341 341 CYS CYS A . n A 1 342 PRO 342 342 342 PRO PRO A . n A 1 343 ASP 343 343 343 ASP ASP A . n A 1 344 GLY 344 344 344 GLY GLY A . n A 1 345 SER 345 345 345 SER SER A . n A 1 346 MET 346 346 346 MET MET A . n A 1 347 SER 347 347 347 SER SER A . n A 1 348 CYS 348 348 348 CYS CYS A . n A 1 349 PRO 349 349 349 PRO PRO A . n A 1 350 GLY 350 350 350 GLY GLY A . n A 1 351 VAL 351 351 351 VAL VAL A . n A 1 352 GLN 352 352 352 GLN GLN A . n A 1 353 PHE 353 353 353 PHE PHE A . n A 1 354 ASN 354 354 354 ASN ASN A . n A 1 355 GLY 355 355 355 GLY GLY A . n A 1 356 PRO 356 356 356 PRO PRO A . n A 1 357 ALA 357 357 357 ALA ALA 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 1 361 361 NAG NAG A . C 2 NAG 2 362 362 NAG NAG A . D 3 MAN 1 364 364 MAN MAN A . E 4 CA 1 371 371 CA CAL A . F 4 CA 1 372 372 CA CAL A . G 5 HEM 1 396 396 HEM HEM A . H 6 GOL 1 401 401 GOL GOL A . I 7 HOH 1 1001 1001 HOH HOH A . I 7 HOH 2 1002 1002 HOH HOH A . I 7 HOH 3 1003 1003 HOH HOH A . I 7 HOH 4 1004 1004 HOH HOH A . I 7 HOH 5 1005 1005 HOH HOH A . I 7 HOH 6 1006 1006 HOH HOH A . I 7 HOH 7 1007 1007 HOH HOH A . I 7 HOH 8 1008 1008 HOH HOH A . I 7 HOH 9 1009 1009 HOH HOH A . I 7 HOH 10 1010 1010 HOH HOH A . I 7 HOH 11 1011 1011 HOH HOH A . I 7 HOH 12 1012 1012 HOH HOH A . I 7 HOH 13 1013 1013 HOH HOH A . I 7 HOH 14 1014 1014 HOH HOH A . I 7 HOH 15 1015 1015 HOH HOH A . I 7 HOH 16 1016 1016 HOH HOH A . I 7 HOH 17 1017 1017 HOH HOH A . I 7 HOH 18 1018 1018 HOH HOH A . I 7 HOH 19 1019 1019 HOH HOH A . I 7 HOH 20 1020 1020 HOH HOH A . I 7 HOH 21 1021 1021 HOH HOH A . I 7 HOH 22 1022 1022 HOH HOH A . I 7 HOH 23 1023 1023 HOH HOH A . I 7 HOH 24 1024 1024 HOH HOH A . I 7 HOH 25 1025 1025 HOH HOH A . I 7 HOH 26 1026 1026 HOH HOH A . I 7 HOH 27 1027 1027 HOH HOH A . I 7 HOH 28 1028 1028 HOH HOH A . I 7 HOH 29 1029 1029 HOH HOH A . I 7 HOH 30 1030 1030 HOH HOH A . I 7 HOH 31 1031 1031 HOH HOH A . I 7 HOH 32 1032 1032 HOH HOH A . I 7 HOH 33 1033 1033 HOH HOH A . I 7 HOH 34 1034 1034 HOH HOH A . I 7 HOH 35 1035 1035 HOH HOH A . I 7 HOH 36 1036 1036 HOH HOH A . I 7 HOH 37 1037 1037 HOH HOH A . I 7 HOH 38 1038 1038 HOH HOH A . I 7 HOH 39 1039 1039 HOH HOH A . I 7 HOH 40 1040 1040 HOH HOH A . I 7 HOH 41 1041 1041 HOH HOH A . I 7 HOH 42 1042 1042 HOH HOH A . I 7 HOH 43 1043 1043 HOH HOH A . I 7 HOH 44 1044 1044 HOH HOH A . I 7 HOH 45 1045 1045 HOH HOH A . I 7 HOH 46 1046 1046 HOH HOH A . I 7 HOH 47 1047 1047 HOH HOH A . I 7 HOH 48 1048 1048 HOH HOH A . I 7 HOH 49 1049 1049 HOH HOH A . I 7 HOH 50 1050 1050 HOH HOH A . I 7 HOH 51 1051 1051 HOH HOH A . I 7 HOH 52 1052 1052 HOH HOH A . I 7 HOH 53 1053 1053 HOH HOH A . I 7 HOH 54 1054 1054 HOH HOH A . I 7 HOH 55 1055 1055 HOH HOH A . I 7 HOH 56 1056 1056 HOH HOH A . I 7 HOH 57 1057 1057 HOH HOH A . I 7 HOH 58 1058 1058 HOH HOH A . I 7 HOH 59 1059 1059 HOH HOH A . I 7 HOH 60 1060 1060 HOH HOH A . I 7 HOH 61 1061 1061 HOH HOH A . I 7 HOH 62 1062 1062 HOH HOH A . I 7 HOH 63 1063 1063 HOH HOH A . I 7 HOH 64 1064 1064 HOH HOH A . I 7 HOH 65 1065 1065 HOH HOH A . I 7 HOH 66 1066 1066 HOH HOH A . I 7 HOH 67 1067 1067 HOH HOH A . I 7 HOH 68 1068 1068 HOH HOH A . I 7 HOH 69 1069 1069 HOH HOH A . I 7 HOH 70 1070 1070 HOH HOH A . I 7 HOH 71 1071 1071 HOH HOH A . I 7 HOH 72 1072 1072 HOH HOH A . I 7 HOH 73 1073 1073 HOH HOH A . I 7 HOH 74 1074 1074 HOH HOH A . I 7 HOH 75 1075 1075 HOH HOH A . I 7 HOH 76 1076 1076 HOH HOH A . I 7 HOH 77 1077 1077 HOH HOH A . I 7 HOH 78 1078 1078 HOH HOH A . I 7 HOH 79 1079 1079 HOH HOH A . I 7 HOH 80 1080 1080 HOH HOH A . I 7 HOH 81 1081 1081 HOH HOH A . I 7 HOH 82 1082 1082 HOH HOH A . I 7 HOH 83 1083 1083 HOH HOH A . I 7 HOH 84 1084 1084 HOH HOH A . I 7 HOH 85 1085 1085 HOH HOH A . I 7 HOH 86 1086 1086 HOH HOH A . I 7 HOH 87 1087 1087 HOH HOH A . I 7 HOH 88 1088 1088 HOH HOH A . I 7 HOH 89 1089 1089 HOH HOH A . I 7 HOH 90 1090 1090 HOH HOH A . I 7 HOH 91 1091 1091 HOH HOH A . I 7 HOH 92 1092 1092 HOH HOH A . I 7 HOH 93 1093 1093 HOH HOH A . I 7 HOH 94 1094 1094 HOH HOH A . I 7 HOH 95 1095 1095 HOH HOH A . I 7 HOH 96 1096 1096 HOH HOH A . I 7 HOH 97 1097 1097 HOH HOH A . I 7 HOH 98 1098 1098 HOH HOH A . I 7 HOH 99 1099 1099 HOH HOH A . I 7 HOH 100 1100 1100 HOH HOH A . I 7 HOH 101 1101 1101 HOH HOH A . I 7 HOH 102 1102 1102 HOH HOH A . I 7 HOH 103 1103 1103 HOH HOH A . I 7 HOH 104 1104 1104 HOH HOH A . I 7 HOH 105 1105 1105 HOH HOH A . I 7 HOH 106 1106 1106 HOH HOH A . I 7 HOH 107 1107 1107 HOH HOH A . I 7 HOH 108 1108 1108 HOH HOH A . I 7 HOH 109 1109 1109 HOH HOH A . I 7 HOH 110 1110 1110 HOH HOH A . I 7 HOH 111 1111 1111 HOH HOH A . I 7 HOH 112 1112 1112 HOH HOH A . I 7 HOH 113 1113 1113 HOH HOH A . I 7 HOH 114 1114 1114 HOH HOH A . I 7 HOH 115 1115 1115 HOH HOH A . I 7 HOH 116 1116 1116 HOH HOH A . I 7 HOH 117 1117 1117 HOH HOH A . I 7 HOH 118 1118 1118 HOH HOH A . I 7 HOH 119 1119 1119 HOH HOH A . I 7 HOH 120 1120 1120 HOH HOH A . I 7 HOH 121 1121 1121 HOH HOH A . I 7 HOH 122 1122 1122 HOH HOH A . I 7 HOH 123 1123 1123 HOH HOH A . I 7 HOH 124 1124 1124 HOH HOH A . I 7 HOH 125 1125 1125 HOH HOH A . I 7 HOH 126 1126 1126 HOH HOH A . I 7 HOH 127 1127 1127 HOH HOH A . I 7 HOH 128 1128 1128 HOH HOH A . I 7 HOH 129 1129 1129 HOH HOH A . I 7 HOH 130 1130 1130 HOH HOH A . I 7 HOH 131 1131 1131 HOH HOH A . I 7 HOH 132 1132 1132 HOH HOH A . I 7 HOH 133 1133 1133 HOH HOH A . I 7 HOH 134 1134 1134 HOH HOH A . I 7 HOH 135 1135 1135 HOH HOH A . I 7 HOH 136 1136 1136 HOH HOH A . I 7 HOH 137 1137 1137 HOH HOH A . I 7 HOH 138 1138 1138 HOH HOH A . I 7 HOH 139 1139 1139 HOH HOH A . I 7 HOH 140 1140 1140 HOH HOH A . I 7 HOH 141 1141 1141 HOH HOH A . I 7 HOH 142 1142 1142 HOH HOH A . I 7 HOH 143 1143 1143 HOH HOH A . I 7 HOH 144 1144 1144 HOH HOH A . I 7 HOH 145 1145 1145 HOH HOH A . I 7 HOH 146 1146 1146 HOH HOH A . I 7 HOH 147 1147 1147 HOH HOH A . I 7 HOH 148 1148 1148 HOH HOH A . I 7 HOH 149 1149 1149 HOH HOH A . I 7 HOH 150 1150 1150 HOH HOH A . I 7 HOH 151 1151 1151 HOH HOH A . I 7 HOH 152 1152 1152 HOH HOH A . I 7 HOH 153 1153 1153 HOH HOH A . I 7 HOH 154 1154 1154 HOH HOH A . I 7 HOH 155 1155 1155 HOH HOH A . I 7 HOH 156 1156 1156 HOH HOH A . I 7 HOH 157 1157 1157 HOH HOH A . I 7 HOH 158 1158 1158 HOH HOH A . I 7 HOH 159 1159 1159 HOH HOH A . I 7 HOH 160 1160 1160 HOH HOH A . I 7 HOH 161 1161 1161 HOH HOH A . I 7 HOH 162 1162 1162 HOH HOH A . I 7 HOH 163 1163 1163 HOH HOH A . I 7 HOH 164 1164 1164 HOH HOH A . I 7 HOH 165 1165 1165 HOH HOH A . I 7 HOH 166 1166 1166 HOH HOH A . I 7 HOH 167 1167 1167 HOH HOH A . I 7 HOH 168 1168 1168 HOH HOH A . I 7 HOH 169 1169 1169 HOH HOH A . I 7 HOH 170 1170 1170 HOH HOH A . I 7 HOH 171 1171 1171 HOH HOH A . I 7 HOH 172 1172 1172 HOH HOH A . I 7 HOH 173 1173 1173 HOH HOH A . I 7 HOH 174 1174 1174 HOH HOH A . I 7 HOH 175 1175 1175 HOH HOH A . I 7 HOH 176 1176 1176 HOH HOH A . I 7 HOH 177 1177 1177 HOH HOH A . I 7 HOH 178 1178 1178 HOH HOH A . I 7 HOH 179 1179 1179 HOH HOH A . I 7 HOH 180 1180 1180 HOH HOH A . I 7 HOH 181 1181 1181 HOH HOH A . I 7 HOH 182 1182 1182 HOH HOH A . I 7 HOH 183 1183 1183 HOH HOH A . I 7 HOH 184 1184 1184 HOH HOH A . I 7 HOH 185 1185 1185 HOH HOH A . I 7 HOH 186 1186 1186 HOH HOH A . I 7 HOH 187 1187 1187 HOH HOH A . I 7 HOH 188 1188 1188 HOH HOH A . I 7 HOH 189 1189 1189 HOH HOH A . I 7 HOH 190 1190 1190 HOH HOH A . I 7 HOH 191 1191 1191 HOH HOH A . I 7 HOH 192 1192 1192 HOH HOH A . I 7 HOH 193 1193 1193 HOH HOH A . I 7 HOH 194 1195 1195 HOH HOH A . I 7 HOH 195 1196 1196 HOH HOH A . I 7 HOH 196 1197 1197 HOH HOH A . I 7 HOH 197 1198 1198 HOH HOH A . I 7 HOH 198 1199 1199 HOH HOH A . I 7 HOH 199 1200 1200 HOH HOH A . I 7 HOH 200 1201 1201 HOH HOH A . I 7 HOH 201 1202 1202 HOH HOH A . I 7 HOH 202 1203 1203 HOH HOH A . I 7 HOH 203 1204 1204 HOH HOH A . I 7 HOH 204 1205 1205 HOH HOH A . I 7 HOH 205 1206 1206 HOH HOH A . I 7 HOH 206 1207 1207 HOH HOH A . I 7 HOH 207 1208 1208 HOH HOH A . I 7 HOH 208 1209 1209 HOH HOH A . I 7 HOH 209 1210 1210 HOH HOH A . I 7 HOH 210 1211 1211 HOH HOH A . I 7 HOH 211 1212 1212 HOH HOH A . I 7 HOH 212 1213 1213 HOH HOH A . I 7 HOH 213 1214 1214 HOH HOH A . I 7 HOH 214 1215 1215 HOH HOH A . I 7 HOH 215 1216 1216 HOH HOH A . I 7 HOH 216 1217 1217 HOH HOH A . I 7 HOH 217 1218 1218 HOH HOH A . I 7 HOH 218 1219 1219 HOH HOH A . I 7 HOH 219 1220 1220 HOH HOH A . I 7 HOH 220 1221 1221 HOH HOH A . I 7 HOH 221 1222 1222 HOH HOH A . I 7 HOH 222 1223 1223 HOH HOH A . I 7 HOH 223 1224 1224 HOH HOH A . I 7 HOH 224 1225 1225 HOH HOH A . I 7 HOH 225 1226 1226 HOH HOH A . I 7 HOH 226 1227 1227 HOH HOH A . I 7 HOH 227 1228 1228 HOH HOH A . I 7 HOH 228 1229 1229 HOH HOH A . I 7 HOH 229 1230 1230 HOH HOH A . I 7 HOH 230 1231 1231 HOH HOH A . I 7 HOH 231 1232 1232 HOH HOH A . I 7 HOH 232 1233 1233 HOH HOH A . I 7 HOH 233 1234 1234 HOH HOH A . I 7 HOH 234 1235 1235 HOH HOH A . I 7 HOH 235 1236 1236 HOH HOH A . I 7 HOH 236 1237 1237 HOH HOH A . I 7 HOH 237 1238 1238 HOH HOH A . I 7 HOH 238 1239 1239 HOH HOH A . I 7 HOH 239 1240 1240 HOH HOH A . I 7 HOH 240 1241 1241 HOH HOH A . I 7 HOH 241 1242 1242 HOH HOH A . I 7 HOH 242 1243 1243 HOH HOH A . I 7 HOH 243 1245 1245 HOH HOH A . I 7 HOH 244 1246 1246 HOH HOH A . I 7 HOH 245 1247 1247 HOH HOH A . I 7 HOH 246 1248 1248 HOH HOH A . I 7 HOH 247 1249 1249 HOH HOH A . I 7 HOH 248 1250 1250 HOH HOH A . I 7 HOH 249 1251 1251 HOH HOH A . I 7 HOH 250 1252 1252 HOH HOH A . I 7 HOH 251 1253 1253 HOH HOH A . I 7 HOH 252 1254 1254 HOH HOH A . I 7 HOH 253 1255 1255 HOH HOH A . I 7 HOH 254 1256 1256 HOH HOH A . I 7 HOH 255 1257 1257 HOH HOH A . I 7 HOH 256 1258 1258 HOH HOH A . I 7 HOH 257 1259 1259 HOH HOH A . I 7 HOH 258 1260 1260 HOH HOH A . I 7 HOH 259 1261 1261 HOH HOH A . I 7 HOH 260 1262 1262 HOH HOH A . I 7 HOH 261 1263 1263 HOH HOH A . I 7 HOH 262 1264 1264 HOH HOH A . I 7 HOH 263 1265 1265 HOH HOH A . I 7 HOH 264 1266 1266 HOH HOH A . I 7 HOH 265 1267 1267 HOH HOH A . I 7 HOH 266 1268 1268 HOH HOH A . I 7 HOH 267 1269 1269 HOH HOH A . I 7 HOH 268 1270 1270 HOH HOH A . I 7 HOH 269 1271 1271 HOH HOH A . I 7 HOH 270 1272 1272 HOH HOH A . I 7 HOH 271 1273 1273 HOH HOH A . I 7 HOH 272 1274 1274 HOH HOH A . I 7 HOH 273 1275 1275 HOH HOH A . I 7 HOH 274 1276 1276 HOH HOH A . I 7 HOH 275 1277 1277 HOH HOH A . I 7 HOH 276 1278 1278 HOH HOH A . I 7 HOH 277 1279 1279 HOH HOH A . I 7 HOH 278 1280 1280 HOH HOH A . I 7 HOH 279 1281 1281 HOH HOH A . I 7 HOH 280 1282 1282 HOH HOH A . I 7 HOH 281 1283 1283 HOH HOH A . I 7 HOH 282 1284 1284 HOH HOH A . I 7 HOH 283 1285 1285 HOH HOH A . I 7 HOH 284 1286 1286 HOH HOH A . I 7 HOH 285 1288 1288 HOH HOH A . I 7 HOH 286 1289 1289 HOH HOH A . I 7 HOH 287 1290 1290 HOH HOH A . I 7 HOH 288 1291 1291 HOH HOH A . I 7 HOH 289 1292 1292 HOH HOH A . I 7 HOH 290 1293 1293 HOH HOH A . I 7 HOH 291 1294 1294 HOH HOH A . I 7 HOH 292 1295 1295 HOH HOH A . I 7 HOH 293 1296 1296 HOH HOH A . I 7 HOH 294 1297 1297 HOH HOH A . I 7 HOH 295 1298 1298 HOH HOH A . I 7 HOH 296 1299 1299 HOH HOH A . I 7 HOH 297 1300 1300 HOH HOH A . I 7 HOH 298 1302 1302 HOH HOH A . I 7 HOH 299 1303 1303 HOH HOH A . I 7 HOH 300 1304 1304 HOH HOH A . I 7 HOH 301 1305 1305 HOH HOH A . I 7 HOH 302 1306 1306 HOH HOH A . I 7 HOH 303 1307 1307 HOH HOH A . I 7 HOH 304 1308 1308 HOH HOH A . I 7 HOH 305 1309 1309 HOH HOH A . I 7 HOH 306 1310 1310 HOH HOH A . I 7 HOH 307 1311 1311 HOH HOH A . I 7 HOH 308 1312 1312 HOH HOH A . I 7 HOH 309 1313 1313 HOH HOH A . I 7 HOH 310 1314 1314 HOH HOH A . I 7 HOH 311 1315 1315 HOH HOH A . I 7 HOH 312 1316 1316 HOH HOH A . I 7 HOH 313 1317 1317 HOH HOH A . I 7 HOH 314 1318 1318 HOH HOH A . I 7 HOH 315 1319 1319 HOH HOH A . I 7 HOH 316 1320 1320 HOH HOH A . I 7 HOH 317 1321 1321 HOH HOH A . I 7 HOH 318 1322 1322 HOH HOH A . I 7 HOH 319 1323 1323 HOH HOH A . I 7 HOH 320 1324 1324 HOH HOH A . I 7 HOH 321 1325 1325 HOH HOH A . I 7 HOH 322 1326 1326 HOH HOH A . I 7 HOH 323 1327 1327 HOH HOH A . I 7 HOH 324 1328 1328 HOH HOH A . I 7 HOH 325 1329 1329 HOH HOH A . I 7 HOH 326 1330 1330 HOH HOH A . I 7 HOH 327 1331 1331 HOH HOH A . I 7 HOH 328 1332 1332 HOH HOH A . I 7 HOH 329 1333 1333 HOH HOH A . I 7 HOH 330 1334 1334 HOH HOH A . I 7 HOH 331 1335 1335 HOH HOH A . I 7 HOH 332 1336 1336 HOH HOH A . I 7 HOH 333 1337 1337 HOH HOH A . I 7 HOH 334 1338 1338 HOH HOH A . I 7 HOH 335 1339 1339 HOH HOH A . I 7 HOH 336 1340 1340 HOH HOH A . I 7 HOH 337 1341 1341 HOH HOH A . I 7 HOH 338 1342 1342 HOH HOH A . I 7 HOH 339 1343 1343 HOH HOH A . I 7 HOH 340 1344 1344 HOH HOH A . I 7 HOH 341 1345 1345 HOH HOH A . I 7 HOH 342 1346 1346 HOH HOH A . I 7 HOH 343 1347 1347 HOH HOH A . I 7 HOH 344 1348 1348 HOH HOH A . I 7 HOH 345 1349 1349 HOH HOH A . I 7 HOH 346 1350 1350 HOH HOH A . I 7 HOH 347 1351 1351 HOH HOH A . I 7 HOH 348 1352 1352 HOH HOH A . I 7 HOH 349 1353 1353 HOH HOH A . I 7 HOH 350 1354 1354 HOH HOH A . I 7 HOH 351 1355 1355 HOH HOH A . I 7 HOH 352 1356 1356 HOH HOH A . I 7 HOH 353 1357 1357 HOH HOH A . I 7 HOH 354 1358 1358 HOH HOH A . I 7 HOH 355 1359 1359 HOH HOH A . I 7 HOH 356 1360 1360 HOH HOH A . I 7 HOH 357 1361 1361 HOH HOH A . I 7 HOH 358 1362 1362 HOH HOH A . I 7 HOH 359 1363 1363 HOH HOH A . I 7 HOH 360 1364 1364 HOH HOH A . I 7 HOH 361 1365 1365 HOH HOH A . I 7 HOH 362 1366 1366 HOH HOH A . I 7 HOH 363 1367 1367 HOH HOH A . I 7 HOH 364 1368 1368 HOH HOH A . I 7 HOH 365 1369 1369 HOH HOH A . I 7 HOH 366 1370 1370 HOH HOH A . I 7 HOH 367 1371 1371 HOH HOH A . I 7 HOH 368 1372 1372 HOH HOH A . I 7 HOH 369 1373 1373 HOH HOH A . I 7 HOH 370 1374 1374 HOH HOH A . I 7 HOH 371 1375 1375 HOH HOH A . I 7 HOH 372 1376 1376 HOH HOH A . I 7 HOH 373 1377 1377 HOH HOH A . I 7 HOH 374 1378 1378 HOH HOH A . I 7 HOH 375 1379 1379 HOH HOH A . I 7 HOH 376 1380 1380 HOH HOH A . I 7 HOH 377 1381 1381 HOH HOH A . I 7 HOH 378 1382 1382 HOH HOH A . I 7 HOH 379 1383 1383 HOH HOH A . I 7 HOH 380 1384 1384 HOH HOH A . I 7 HOH 381 1385 1385 HOH HOH A . I 7 HOH 382 1386 1386 HOH HOH A . I 7 HOH 383 1387 1387 HOH HOH A . I 7 HOH 384 1388 1388 HOH HOH A . I 7 HOH 385 1389 1389 HOH HOH A . I 7 HOH 386 1390 1390 HOH HOH A . I 7 HOH 387 1391 1391 HOH HOH A . I 7 HOH 388 1392 1392 HOH HOH A . I 7 HOH 389 1393 1393 HOH HOH A . I 7 HOH 390 1394 1394 HOH HOH A . I 7 HOH 391 1395 1395 HOH HOH A . I 7 HOH 392 1396 1396 HOH HOH A . I 7 HOH 393 1397 1397 HOH HOH A . I 7 HOH 394 1398 1398 HOH HOH A . I 7 HOH 395 1401 1401 HOH HOH A . I 7 HOH 396 1402 1402 HOH HOH A . I 7 HOH 397 1403 1403 HOH HOH A . I 7 HOH 398 1404 1404 HOH HOH A . I 7 HOH 399 1405 1405 HOH HOH A . I 7 HOH 400 1406 1406 HOH HOH A . I 7 HOH 401 1407 1407 HOH HOH A . I 7 HOH 402 1408 1408 HOH HOH A . I 7 HOH 403 1409 1409 HOH HOH A . I 7 HOH 404 1410 1410 HOH HOH A . I 7 HOH 405 1411 1411 HOH HOH A . I 7 HOH 406 1412 1412 HOH HOH A . I 7 HOH 407 1413 1413 HOH HOH A . I 7 HOH 408 1414 1414 HOH HOH A . I 7 HOH 409 1415 1415 HOH HOH A . I 7 HOH 410 1416 1416 HOH HOH A . I 7 HOH 411 1417 1417 HOH HOH A . I 7 HOH 412 1418 1418 HOH HOH A . I 7 HOH 413 1419 1419 HOH HOH A . I 7 HOH 414 1420 1420 HOH HOH A . I 7 HOH 415 1421 1421 HOH HOH A . I 7 HOH 416 1423 1423 HOH HOH A . I 7 HOH 417 1424 1424 HOH HOH A . I 7 HOH 418 1425 1425 HOH HOH A . I 7 HOH 419 1426 1426 HOH HOH A . I 7 HOH 420 1427 1427 HOH HOH A . I 7 HOH 421 1428 1428 HOH HOH A . I 7 HOH 422 1429 1429 HOH HOH A . I 7 HOH 423 1430 1430 HOH HOH A . I 7 HOH 424 1431 1431 HOH HOH A . I 7 HOH 425 1432 1432 HOH HOH A . I 7 HOH 426 1433 1433 HOH HOH A . I 7 HOH 427 1434 1434 HOH HOH A . I 7 HOH 428 1435 1435 HOH HOH A . I 7 HOH 429 1436 1436 HOH HOH A . I 7 HOH 430 1437 1437 HOH HOH A . I 7 HOH 431 1438 1438 HOH HOH A . I 7 HOH 432 1439 1439 HOH HOH A . I 7 HOH 433 1440 1440 HOH HOH A . I 7 HOH 434 1441 1441 HOH HOH A . I 7 HOH 435 1442 1442 HOH HOH A . I 7 HOH 436 1443 1443 HOH HOH A . I 7 HOH 437 1444 1444 HOH HOH A . I 7 HOH 438 1445 1445 HOH HOH A . I 7 HOH 439 1446 1446 HOH HOH A . I 7 HOH 440 1447 1447 HOH HOH A . I 7 HOH 441 1448 1448 HOH HOH A . I 7 HOH 442 1449 1449 HOH HOH A . I 7 HOH 443 1450 1450 HOH HOH A . I 7 HOH 444 1451 1451 HOH HOH A . I 7 HOH 445 1452 1452 HOH HOH A . I 7 HOH 446 1453 1453 HOH HOH A . I 7 HOH 447 1454 1454 HOH HOH A . I 7 HOH 448 1455 1455 HOH HOH A . I 7 HOH 449 1456 1456 HOH HOH A . I 7 HOH 450 1457 1457 HOH HOH A . I 7 HOH 451 1458 1458 HOH HOH A . I 7 HOH 452 1459 1459 HOH HOH A . I 7 HOH 453 1460 1460 HOH HOH A . I 7 HOH 454 1461 1461 HOH HOH A . I 7 HOH 455 1462 1462 HOH HOH A . I 7 HOH 456 1463 1463 HOH HOH A . I 7 HOH 457 1464 1464 HOH HOH A . I 7 HOH 458 1465 1465 HOH HOH A . I 7 HOH 459 1466 1466 HOH HOH A . I 7 HOH 460 1467 1467 HOH HOH A . I 7 HOH 461 1468 1468 HOH HOH A . I 7 HOH 462 1469 1469 HOH HOH A . I 7 HOH 463 1470 1470 HOH HOH A . I 7 HOH 464 1471 1471 HOH HOH A . I 7 HOH 465 1472 1472 HOH HOH A . I 7 HOH 466 1473 1473 HOH HOH A . I 7 HOH 467 1474 1474 HOH HOH A . I 7 HOH 468 1475 1475 HOH HOH A . I 7 HOH 469 1477 1477 HOH HOH A . I 7 HOH 470 1478 1478 HOH HOH A . I 7 HOH 471 1479 1479 HOH HOH A . I 7 HOH 472 1480 1480 HOH HOH A . I 7 HOH 473 1481 1481 HOH HOH A . I 7 HOH 474 1482 1482 HOH HOH A . I 7 HOH 475 1483 1483 HOH HOH A . I 7 HOH 476 1484 1484 HOH HOH A . I 7 HOH 477 1485 1485 HOH HOH A . I 7 HOH 478 1486 1486 HOH HOH A . I 7 HOH 479 1487 1487 HOH HOH A . I 7 HOH 480 1488 1488 HOH HOH A . I 7 HOH 481 1489 1489 HOH HOH A . I 7 HOH 482 1490 1490 HOH HOH A . I 7 HOH 483 1491 1491 HOH HOH A . I 7 HOH 484 1492 1492 HOH HOH A . I 7 HOH 485 1493 1493 HOH HOH A . I 7 HOH 486 1494 1494 HOH HOH A . I 7 HOH 487 1495 1495 HOH HOH A . I 7 HOH 488 1496 1496 HOH HOH A . I 7 HOH 489 1497 1497 HOH HOH A . I 7 HOH 490 1498 1498 HOH HOH A . I 7 HOH 491 1499 1499 HOH HOH A . I 7 HOH 492 1500 1500 HOH HOH A . I 7 HOH 493 1501 1501 HOH HOH A . I 7 HOH 494 1502 1502 HOH HOH A . I 7 HOH 495 1503 1503 HOH HOH A . I 7 HOH 496 1504 1504 HOH HOH A . I 7 HOH 497 1505 1505 HOH HOH A . I 7 HOH 498 1506 1506 HOH HOH A . I 7 HOH 499 1507 1507 HOH HOH A . I 7 HOH 500 1508 1508 HOH HOH A . I 7 HOH 501 1509 1509 HOH HOH A . I 7 HOH 502 1510 1510 HOH HOH A . I 7 HOH 503 1511 1511 HOH HOH A . I 7 HOH 504 1512 1512 HOH HOH A . I 7 HOH 505 1513 1513 HOH HOH A . I 7 HOH 506 1514 1514 HOH HOH A . I 7 HOH 507 1515 1515 HOH HOH A . I 7 HOH 508 1516 1516 HOH HOH A . I 7 HOH 509 1517 1517 HOH HOH A . I 7 HOH 510 1518 1518 HOH HOH A . I 7 HOH 511 1519 1519 HOH HOH A . I 7 HOH 512 1520 1520 HOH HOH A . I 7 HOH 513 1521 1521 HOH HOH A . I 7 HOH 514 1522 1522 HOH HOH A . I 7 HOH 515 1523 1523 HOH HOH A . I 7 HOH 516 1524 1524 HOH HOH A . I 7 HOH 517 1525 1525 HOH HOH A . I 7 HOH 518 1526 1526 HOH HOH A . I 7 HOH 519 1527 1527 HOH HOH A . I 7 HOH 520 1528 1528 HOH HOH A . I 7 HOH 521 1529 1529 HOH HOH A . I 7 HOH 522 1530 1530 HOH HOH A . I 7 HOH 523 1531 1531 HOH HOH A . I 7 HOH 524 1532 1532 HOH HOH A . I 7 HOH 525 1533 1533 HOH HOH A . I 7 HOH 526 1534 1534 HOH HOH A . I 7 HOH 527 1535 1535 HOH HOH A . I 7 HOH 528 1536 1536 HOH HOH A . I 7 HOH 529 1537 1537 HOH HOH A . I 7 HOH 530 1538 1538 HOH HOH A . I 7 HOH 531 1539 1539 HOH HOH A . I 7 HOH 532 1540 1540 HOH HOH A . I 7 HOH 533 1541 1541 HOH HOH A . I 7 HOH 534 1542 1542 HOH HOH A . I 7 HOH 535 1543 1543 HOH HOH A . I 7 HOH 536 1544 1544 HOH HOH A . I 7 HOH 537 1545 1545 HOH HOH A . I 7 HOH 538 1546 1546 HOH HOH A . I 7 HOH 539 1547 1547 HOH HOH A . I 7 HOH 540 1548 1548 HOH HOH A . I 7 HOH 541 1549 1549 HOH HOH A . I 7 HOH 542 1550 1550 HOH HOH A . I 7 HOH 543 1551 1551 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 131 A ASN 131 ? ASN 'GLYCOSYLATION SITE' 2 A SER 336 A SER 336 ? SER '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_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 NE2 ? A HIS 173 ? A HIS 173 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 NA ? G HEM . ? A HEM 396 ? 1_555 96.0 ? 2 NE2 ? A HIS 173 ? A HIS 173 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 NB ? G HEM . ? A HEM 396 ? 1_555 89.6 ? 3 NA ? G HEM . ? A HEM 396 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 NB ? G HEM . ? A HEM 396 ? 1_555 91.6 ? 4 NE2 ? A HIS 173 ? A HIS 173 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 NC ? G HEM . ? A HEM 396 ? 1_555 90.3 ? 5 NA ? G HEM . ? A HEM 396 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 NC ? G HEM . ? A HEM 396 ? 1_555 173.3 ? 6 NB ? G HEM . ? A HEM 396 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 NC ? G HEM . ? A HEM 396 ? 1_555 86.1 ? 7 NE2 ? A HIS 173 ? A HIS 173 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 ND ? G HEM . ? A HEM 396 ? 1_555 96.0 ? 8 NA ? G HEM . ? A HEM 396 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 ND ? G HEM . ? A HEM 396 ? 1_555 90.7 ? 9 NB ? G HEM . ? A HEM 396 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 ND ? G HEM . ? A HEM 396 ? 1_555 173.7 ? 10 NC ? G HEM . ? A HEM 396 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 ND ? G HEM . ? A HEM 396 ? 1_555 90.9 ? 11 NE2 ? A HIS 173 ? A HIS 173 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 O ? I HOH . ? A HOH 1138 ? 1_555 173.8 ? 12 NA ? G HEM . ? A HEM 396 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 O ? I HOH . ? A HOH 1138 ? 1_555 81.3 ? 13 NB ? G HEM . ? A HEM 396 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 O ? I HOH . ? A HOH 1138 ? 1_555 84.9 ? 14 NC ? G HEM . ? A HEM 396 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 O ? I HOH . ? A HOH 1138 ? 1_555 92.2 ? 15 ND ? G HEM . ? A HEM 396 ? 1_555 FE ? G HEM . ? A HEM 396 ? 1_555 O ? I HOH . ? A HOH 1138 ? 1_555 89.7 ? 16 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 89.3 ? 17 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG ? A SER 174 ? A SER 174 ? 1_555 81.4 ? 18 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG ? A SER 174 ? A SER 174 ? 1_555 70.6 ? 19 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 193 ? A THR 193 ? 1_555 127.6 ? 20 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 193 ? A THR 193 ? 1_555 125.7 ? 21 OG ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 193 ? A THR 193 ? 1_555 142.1 ? 22 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG1 ? A THR 193 ? A THR 193 ? 1_555 92.5 ? 23 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG1 ? A THR 193 ? A THR 193 ? 1_555 72.7 ? 24 OG ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG1 ? A THR 193 ? A THR 193 ? 1_555 142.7 ? 25 O ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OG1 ? A THR 193 ? A THR 193 ? 1_555 68.1 ? 26 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 154.8 ? 27 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 79.2 ? 28 OG ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 73.6 ? 29 O ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 76.6 ? 30 OG1 ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A THR 196 ? A THR 196 ? 1_555 105.2 ? 31 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 50.5 ? 32 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 129.8 ? 33 OG ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 120.7 ? 34 O ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 77.6 ? 35 OG1 ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 79.7 ? 36 O ? A THR 196 ? A THR 196 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 149.5 ? 37 OD2 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A SER 174 ? A SER 174 ? 1_555 95.1 ? 38 OD1 ? A ASP 198 ? A ASP 198 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A SER 174 ? A SER 174 ? 1_555 140.8 ? 39 OG ? A SER 174 ? A SER 174 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A SER 174 ? A SER 174 ? 1_555 71.7 ? 40 O ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A SER 174 ? A SER 174 ? 1_555 80.9 ? 41 OG1 ? A THR 193 ? A THR 193 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A SER 174 ? A SER 174 ? 1_555 145.6 ? 42 O ? A THR 196 ? A THR 196 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A SER 174 ? A SER 174 ? 1_555 80.6 ? 43 OD1 ? A ASP 191 ? A ASP 191 ? 1_555 CA ? E CA . ? A CA 371 ? 1_555 O ? A SER 174 ? A SER 174 ? 1_555 79.5 ? 44 O ? I HOH . ? A HOH 1128 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? I HOH . ? A HOH 1085 ? 1_555 86.3 ? 45 O ? I HOH . ? A HOH 1128 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 173.9 ? 46 O ? I HOH . ? A HOH 1085 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 89.7 ? 47 O ? I HOH . ? A HOH 1128 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A GLY 62 ? A GLY 62 ? 1_555 88.7 ? 48 O ? I HOH . ? A HOH 1085 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A GLY 62 ? A GLY 62 ? 1_555 137.3 ? 49 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A GLY 62 ? A GLY 62 ? 1_555 97.4 ? 50 O ? I HOH . ? A HOH 1128 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 94.1 ? 51 O ? I HOH . ? A HOH 1085 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 152.5 ? 52 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 87.2 ? 53 O ? A GLY 62 ? A GLY 62 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 70.2 ? 54 O ? I HOH . ? A HOH 1128 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 82.5 ? 55 O ? I HOH . ? A HOH 1085 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 77.2 ? 56 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 92.1 ? 57 O ? A GLY 62 ? A GLY 62 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 143.8 ? 58 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 OG ? A SER 66 ? A SER 66 ? 1_555 75.6 ? 59 O ? I HOH . ? A HOH 1128 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A ASP 47 ? A ASP 47 ? 1_555 102.6 ? 60 O ? I HOH . ? A HOH 1085 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A ASP 47 ? A ASP 47 ? 1_555 71.1 ? 61 OD2 ? A ASP 47 ? A ASP 47 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A ASP 47 ? A ASP 47 ? 1_555 80.5 ? 62 O ? A GLY 62 ? A GLY 62 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A ASP 47 ? A ASP 47 ? 1_555 68.8 ? 63 OD1 ? A ASP 64 ? A ASP 64 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A ASP 47 ? A ASP 47 ? 1_555 135.0 ? 64 OG ? A SER 66 ? A SER 66 ? 1_555 CA ? F CA . ? A CA 372 ? 1_555 O ? A ASP 47 ? A ASP 47 ? 1_555 147.4 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2005-05-10 2 'Structure model' 1 1 2008-04-30 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2018-01-24 # _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' 4 4 'Structure model' 'Database references' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 4 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category citation_author # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 4 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_citation_author.name' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal DENZO 'data reduction' . ? 1 SCALEPACK 'data scaling' . ? 2 SHELXL refinement . ? 3 SHELXL-97 refinement . ? 4 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CD _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 GLU _pdbx_validate_rmsd_bond.auth_seq_id_1 26 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 OE2 _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 GLU _pdbx_validate_rmsd_bond.auth_seq_id_2 26 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.332 _pdbx_validate_rmsd_bond.bond_target_value 1.252 _pdbx_validate_rmsd_bond.bond_deviation 0.080 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.011 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE A ARG 323 ? ? CZ A ARG 323 ? ? NH1 A ARG 323 ? ? 116.88 120.30 -3.42 0.50 N 2 1 NE A ARG 323 ? ? CZ A ARG 323 ? ? NH2 A ARG 323 ? ? 125.15 120.30 4.85 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 31 ? ? 56.59 19.02 2 1 CYS A 33 ? ? -91.03 51.27 3 1 VAL A 73 ? ? -98.39 -86.19 4 1 THR A 133 ? ? -163.21 -161.31 5 1 SER A 309 ? ? 88.75 -3.77 6 1 SER A 345 ? ? -67.51 -155.70 7 1 CYS A 348 ? ? -157.12 69.21 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-D-MANNOSE MAN 4 'CALCIUM ION' CA 5 'PROTOPORPHYRIN IX CONTAINING FE' HEM 6 GLYCEROL GOL 7 water HOH #