data_4KMX # _entry.id 4KMX # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4KMX RCSB RCSB079538 WWPDB D_1000079538 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4KM6 'Human folate receptor alpha (FOLR1) at acidic pH, orthorhombic form' unspecified PDB 4KM7 'Human folate receptor alpha (FOLR1) at acidic pH, triclinic form' unspecified PDB 4KMY 'Human folate receptor beta (FOLR2) at neutral pH' unspecified PDB 4KMZ 'Human folate receptor beta (FOLR2) in complex with folate' unspecified PDB 4KN0 'Human folate receptor beta (FOLR2) in complex with the antifolate methotrexate' unspecified PDB 4KN1 'Human folate receptor beta (FOLR2) in complex with the antifolate aminopterin' unspecified PDB 4KN2 'Human folate receptor beta (FOLR2) in complex with antifolate pemetrexed' unspecified # _pdbx_database_status.entry_id 4KMX _pdbx_database_status.status_code REL _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2013-05-08 _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Wibowo, A.S.' 1 'Dann III, C.E.' 2 # _citation.id primary _citation.title 'Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.' _citation.journal_abbrev Proc.Natl.Acad.Sci.USA _citation.journal_volume 110 _citation.page_first 15180 _citation.page_last 15188 _citation.year 2013 _citation.journal_id_ASTM PNASA6 _citation.country US _citation.journal_id_ISSN 0027-8424 _citation.journal_id_CSD 0040 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 23934049 _citation.pdbx_database_id_DOI 10.1073/pnas.1308827110 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Wibowo, A.S.' 1 primary 'Singh, M.' 2 primary 'Reeder, K.M.' 3 primary 'Carter, J.J.' 4 primary 'Kovach, A.R.' 5 primary 'Meng, W.' 6 primary 'Ratnam, M.' 7 primary 'Zhang, F.' 8 primary 'Dann, C.E.' 9 # _cell.entry_id 4KMX _cell.length_a 99.193 _cell.length_b 99.193 _cell.length_c 56.869 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4KMX _symmetry.space_group_name_H-M 'P 65' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 170 _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 man 'Folate receptor alpha' 24348.438 1 ? ? 'UNP residues 28-234' ? 2 non-polymer syn 'POTASSIUM ION' 39.098 1 ? ? ? ? 3 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 5 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? 6 water nat water 18.015 195 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;FR-alpha, Adult folate-binding protein, FBP, Folate receptor 1, Folate receptor, adult, KB cells FBP, Ovarian tumor-associated antigen MOv18 ; # _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 ;WARTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLY ECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTV LCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMS ; _entity_poly.pdbx_seq_one_letter_code_can ;WARTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLY ECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTV LCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMS ; _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 TRP n 1 2 ALA n 1 3 ARG n 1 4 THR n 1 5 GLU n 1 6 LEU n 1 7 LEU n 1 8 ASN n 1 9 VAL n 1 10 CYS n 1 11 MET n 1 12 ASN n 1 13 ALA n 1 14 LYS n 1 15 HIS n 1 16 HIS n 1 17 LYS n 1 18 GLU n 1 19 LYS n 1 20 PRO n 1 21 GLY n 1 22 PRO n 1 23 GLU n 1 24 ASP n 1 25 LYS n 1 26 LEU n 1 27 HIS n 1 28 GLU n 1 29 GLN n 1 30 CYS n 1 31 ARG n 1 32 PRO n 1 33 TRP n 1 34 ARG n 1 35 LYS n 1 36 ASN n 1 37 ALA n 1 38 CYS n 1 39 CYS n 1 40 SER n 1 41 THR n 1 42 ASN n 1 43 THR n 1 44 SER n 1 45 GLN n 1 46 GLU n 1 47 ALA n 1 48 HIS n 1 49 LYS n 1 50 ASP n 1 51 VAL n 1 52 SER n 1 53 TYR n 1 54 LEU n 1 55 TYR n 1 56 ARG n 1 57 PHE n 1 58 ASN n 1 59 TRP n 1 60 ASN n 1 61 HIS n 1 62 CYS n 1 63 GLY n 1 64 GLU n 1 65 MET n 1 66 ALA n 1 67 PRO n 1 68 ALA n 1 69 CYS n 1 70 LYS n 1 71 ARG n 1 72 HIS n 1 73 PHE n 1 74 ILE n 1 75 GLN n 1 76 ASP n 1 77 THR n 1 78 CYS n 1 79 LEU n 1 80 TYR n 1 81 GLU n 1 82 CYS n 1 83 SER n 1 84 PRO n 1 85 ASN n 1 86 LEU n 1 87 GLY n 1 88 PRO n 1 89 TRP n 1 90 ILE n 1 91 GLN n 1 92 GLN n 1 93 VAL n 1 94 ASP n 1 95 GLN n 1 96 SER n 1 97 TRP n 1 98 ARG n 1 99 LYS n 1 100 GLU n 1 101 ARG n 1 102 VAL n 1 103 LEU n 1 104 ASN n 1 105 VAL n 1 106 PRO n 1 107 LEU n 1 108 CYS n 1 109 LYS n 1 110 GLU n 1 111 ASP n 1 112 CYS n 1 113 GLU n 1 114 GLN n 1 115 TRP n 1 116 TRP n 1 117 GLU n 1 118 ASP n 1 119 CYS n 1 120 ARG n 1 121 THR n 1 122 SER n 1 123 TYR n 1 124 THR n 1 125 CYS n 1 126 LYS n 1 127 SER n 1 128 ASN n 1 129 TRP n 1 130 HIS n 1 131 LYS n 1 132 GLY n 1 133 TRP n 1 134 ASN n 1 135 TRP n 1 136 THR n 1 137 SER n 1 138 GLY n 1 139 PHE n 1 140 ASN n 1 141 LYS n 1 142 CYS n 1 143 ALA n 1 144 VAL n 1 145 GLY n 1 146 ALA n 1 147 ALA n 1 148 CYS n 1 149 GLN n 1 150 PRO n 1 151 PHE n 1 152 HIS n 1 153 PHE n 1 154 TYR n 1 155 PHE n 1 156 PRO n 1 157 THR n 1 158 PRO n 1 159 THR n 1 160 VAL n 1 161 LEU n 1 162 CYS n 1 163 ASN n 1 164 GLU n 1 165 ILE n 1 166 TRP n 1 167 THR n 1 168 HIS n 1 169 SER n 1 170 TYR n 1 171 LYS n 1 172 VAL n 1 173 SER n 1 174 ASN n 1 175 TYR n 1 176 SER n 1 177 ARG n 1 178 GLY n 1 179 SER n 1 180 GLY n 1 181 ARG n 1 182 CYS n 1 183 ILE n 1 184 GLN n 1 185 MET n 1 186 TRP n 1 187 PHE n 1 188 ASP n 1 189 PRO n 1 190 ALA n 1 191 GLN n 1 192 GLY n 1 193 ASN n 1 194 PRO n 1 195 ASN n 1 196 GLU n 1 197 GLU n 1 198 VAL n 1 199 ALA n 1 200 ARG n 1 201 PHE n 1 202 TYR n 1 203 ALA n 1 204 ALA n 1 205 ALA n 1 206 MET n 1 207 SER n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene FOLR1 _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name human _entity_src_gen.pdbx_host_org_scientific_name 'Spodoptera frugiperda' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7108 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line Sf9 _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name pFASTBAC _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code FOLR1_HUMAN _struct_ref.pdbx_db_accession P15328 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;WARTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLY ECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTV LCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMS ; _struct_ref.pdbx_align_begin 28 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4KMX _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 207 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P15328 _struct_ref_seq.db_align_beg 28 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 234 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 28 _struct_ref_seq.pdbx_auth_seq_align_end 234 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 K non-polymer . 'POTASSIUM ION' ? 'K 1' 39.098 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4KMX _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.35 _exptl_crystal.density_percent_sol 63.31 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M Citrate, pH 4.5, 0.1 M LiCl, 17.5 % PEG 8000, Vapor diffusion, sitting drop, temperature 298K' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type APS-1/SBC-1 _diffrn_detector.pdbx_collection_date 1996-03-01 _diffrn_detector.details 'THE APS-1/SBC-1 AND THE SBC-2 WERE TWO DIFFERENT DETECTORS WITH THE SBC-2 BEING A NEWER VERSION' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'SAGITALLY FOCUSED SI(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 19-ID' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 19-ID _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.0000 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4KMX _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 30.000 _reflns.d_resolution_high 2.200 _reflns.number_obs 15749 _reflns.number_all ? _reflns.percent_possible_obs 96.400 _reflns.pdbx_Rmerge_I_obs 0.096 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 6.700 _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 ? # loop_ _reflns_shell.pdbx_diffrn_id _reflns_shell.pdbx_ordinal _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.percent_possible_all _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 1 1 2.200 2.240 90.400 0.574 ? ? ? ? ? ? ? ? ? 1 2 2.240 2.280 94.200 0.541 ? ? ? ? ? ? ? ? ? 1 3 2.280 2.320 97.700 0.506 ? ? ? ? ? ? ? ? ? 1 4 2.320 2.370 97.200 0.487 ? ? ? ? ? ? ? ? ? 1 5 2.370 2.420 100.000 0.439 ? ? ? ? ? ? ? ? ? 1 6 2.420 2.480 97.200 0.398 ? ? ? ? ? ? ? ? ? 1 7 2.480 2.540 99.700 0.324 ? ? ? ? ? ? ? ? ? 1 8 2.540 2.610 97.400 0.274 ? ? ? ? ? ? ? ? ? 1 9 2.610 2.680 98.400 0.237 ? ? ? ? ? ? ? ? ? 1 10 2.680 2.770 98.400 0.205 ? ? ? ? ? ? ? ? ? 1 11 2.770 2.870 96.700 0.184 ? ? ? ? ? ? ? ? ? 1 12 2.870 2.990 97.100 0.155 ? ? ? ? ? ? ? ? ? 1 13 2.990 3.120 97.400 0.131 ? ? ? ? ? ? ? ? ? 1 14 3.120 3.290 97.000 0.091 ? ? ? ? ? ? ? ? ? 1 15 3.290 3.490 96.300 0.074 ? ? ? ? ? ? ? ? ? 1 16 3.490 3.760 95.400 0.060 ? ? ? ? ? ? ? ? ? 1 17 3.760 4.140 95.900 0.048 ? ? ? ? ? ? ? ? ? 1 18 4.140 4.730 93.800 0.045 ? ? ? ? ? ? ? ? ? 1 19 4.730 5.960 95.200 0.042 ? ? ? ? ? ? ? ? ? 1 20 5.960 30.000 92.500 0.038 ? ? ? ? ? ? ? ? ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4KMX _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 15747 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.93 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 28.635 _refine.ls_d_res_high 2.200 _refine.ls_percent_reflns_obs 96.49 _refine.ls_R_factor_obs 0.1680 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1659 _refine.ls_R_factor_R_free 0.2065 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.02 _refine.ls_number_reflns_R_free 791 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min 0.830 _refine.occupancy_max 1.000 _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] -4.7880 _refine.aniso_B[2][2] -4.7880 _refine.aniso_B[3][3] 9.5761 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][3] -0.0000 _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol 0.399 _refine.solvent_model_param_bsol 53.201 _refine.pdbx_solvent_vdw_probe_radii 1.10 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.83 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.32 _refine.pdbx_overall_phase_error 20.81 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1627 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 54 _refine_hist.number_atoms_solvent 195 _refine_hist.number_atoms_total 1876 _refine_hist.d_res_high 2.200 _refine_hist.d_res_low 28.635 # 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 f_bond_d 0.004 ? ? 1749 'X-RAY DIFFRACTION' ? f_angle_d 0.852 ? ? 2365 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 13.142 ? ? 624 'X-RAY DIFFRACTION' ? f_chiral_restr 0.067 ? ? 237 'X-RAY DIFFRACTION' ? f_plane_restr 0.004 ? ? 301 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 2.2001 2.3379 2397 0.2337 95.00 0.2770 . . 134 . . . . 'X-RAY DIFFRACTION' . 2.3379 2.5183 2515 0.2059 99.00 0.2606 . . 149 . . . . 'X-RAY DIFFRACTION' . 2.5183 2.7716 2526 0.1715 98.00 0.2491 . . 134 . . . . 'X-RAY DIFFRACTION' . 2.7716 3.1722 2520 0.1516 97.00 0.2091 . . 120 . . . . 'X-RAY DIFFRACTION' . 3.1722 3.9949 2491 0.1361 96.00 0.1707 . . 127 . . . . 'X-RAY DIFFRACTION' . 3.9949 28.6370 2507 0.1696 94.00 0.1856 . . 127 . . . . # _struct.entry_id 4KMX _struct.title 'Human folate receptor alpha (FOLR1) at acidic pH, hexagonal form' _struct.pdbx_descriptor 'Folate receptor alpha' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4KMX _struct_keywords.text ;Folate Receptor Alpha, FOLR1, folate receptor, Folic acid, folates, 5-methyltetrahydrofolate, antifolates, folate-conjugates, GPI-anchored protein on eukaryotic membrane, TRANSPORT PROTEIN, MEMBRANE PROTEIN ; _struct_keywords.pdbx_keywords 'MEMBRANE PROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 4 ? F N N 5 ? G N N 4 ? H N N 6 ? # _struct_biol.id 1 _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 ARG A 3 ? LEU A 7 ? ARG A 30 LEU A 34 5 ? 5 HELX_P HELX_P2 2 ASP A 24 ? GLU A 28 ? ASP A 51 GLU A 55 5 ? 5 HELX_P HELX_P3 3 CYS A 30 ? ARG A 34 ? CYS A 57 ARG A 61 5 ? 5 HELX_P HELX_P4 4 ALA A 66 ? SER A 83 ? ALA A 93 SER A 110 1 ? 18 HELX_P HELX_P5 5 LEU A 86 ? ILE A 90 ? LEU A 113 ILE A 117 5 ? 5 HELX_P HELX_P6 6 CYS A 108 ? CYS A 119 ? CYS A 135 CYS A 146 1 ? 12 HELX_P HELX_P7 7 PHE A 151 ? PHE A 155 ? PHE A 178 PHE A 182 1 ? 5 HELX_P HELX_P8 8 THR A 157 ? ILE A 165 ? THR A 184 ILE A 192 1 ? 9 HELX_P HELX_P9 9 ASP A 188 ? GLY A 192 ? ASP A 215 GLY A 219 5 ? 5 HELX_P HELX_P10 10 PRO A 194 ? MET A 206 ? PRO A 221 MET A 233 1 ? 13 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 10 SG ? ? ? 1_555 A CYS 38 SG ? ? A CYS 37 A CYS 65 1_555 ? ? ? ? ? ? ? 2.029 ? disulf2 disulf ? ? A CYS 30 SG ? ? ? 1_555 A CYS 78 SG ? ? A CYS 57 A CYS 105 1_555 ? ? ? ? ? ? ? 2.032 ? disulf3 disulf ? ? A CYS 39 SG ? ? ? 1_555 A CYS 82 SG ? ? A CYS 66 A CYS 109 1_555 ? ? ? ? ? ? ? 2.024 ? disulf4 disulf ? ? A CYS 62 SG ? ? ? 1_555 A CYS 148 SG ? ? A CYS 89 A CYS 175 1_555 ? ? ? ? ? ? ? 2.038 ? disulf5 disulf ? ? A CYS 69 SG ? ? ? 1_555 A CYS 119 SG ? ? A CYS 96 A CYS 146 1_555 ? ? ? ? ? ? ? 2.032 ? disulf6 disulf ? ? A CYS 108 SG ? ? ? 1_555 A CYS 182 SG ? ? A CYS 135 A CYS 209 1_555 ? ? ? ? ? ? ? 2.029 ? disulf7 disulf ? ? A CYS 112 SG ? ? ? 1_555 A CYS 162 SG ? ? A CYS 139 A CYS 189 1_555 ? ? ? ? ? ? ? 2.041 ? disulf8 disulf ? ? A CYS 125 SG ? ? ? 1_555 A CYS 142 SG ? ? A CYS 152 A CYS 169 1_555 ? ? ? ? ? ? ? 2.026 ? covale1 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 303 A NAG 304 1_555 ? ? ? ? ? ? ? 1.408 ? covale2 covale ? ? D NAG . O6 ? ? ? 1_555 F FUC . C1 ? ? A NAG 303 A FUC 305 1_555 ? ? ? ? ? ? ? 1.422 ? covale3 covale ? ? A ASN 174 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 201 A NAG 306 1_555 ? ? ? ? ? ? ? 1.428 ? covale4 covale ? ? A ASN 134 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 161 A NAG 303 1_555 ? ? ? ? ? ? ? 1.444 ? metalc1 metalc ? ? A SER 83 OG ? ? ? 1_555 B K . K ? ? A SER 110 A K 301 1_555 ? ? ? ? ? ? ? 3.243 ? metalc2 metalc ? ? A ASN 85 OD1 ? ? ? 1_555 B K . K ? ? A ASN 112 A K 301 1_555 ? ? ? ? ? ? ? 3.382 ? # 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 ? # 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 # 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 CYS A 10 ? MET A 11 ? CYS A 37 MET A 38 A 2 LYS A 17 ? GLU A 18 ? LYS A 44 GLU A 45 B 1 TYR A 123 ? THR A 124 ? TYR A 150 THR A 151 B 2 GLN A 149 ? PRO A 150 ? GLN A 176 PRO A 177 # 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 CYS A 10 ? N CYS A 37 O GLU A 18 ? O GLU A 45 B 1 2 N THR A 124 ? N THR A 151 O GLN A 149 ? O GLN A 176 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE K A 301' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CL A 302' AC3 Software ? ? ? ? 8 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 161 RESIDUES 303 TO 305' AC4 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A 306 BOUND TO ASN A 201' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 5 TRP A 33 ? TRP A 60 . ? 1_555 ? 2 AC1 5 SER A 83 ? SER A 110 . ? 1_555 ? 3 AC1 5 ASN A 85 ? ASN A 112 . ? 1_555 ? 4 AC1 5 ASN A 193 ? ASN A 220 . ? 1_555 ? 5 AC1 5 ASN A 195 ? ASN A 222 . ? 1_555 ? 6 AC2 3 ARG A 98 ? ARG A 125 . ? 1_555 ? 7 AC2 3 HOH H . ? HOH A 439 . ? 1_555 ? 8 AC2 3 HOH H . ? HOH A 582 . ? 1_555 ? 9 AC3 8 ASN A 134 ? ASN A 161 . ? 1_555 ? 10 AC3 8 SER A 137 ? SER A 164 . ? 1_555 ? 11 AC3 8 LYS A 141 ? LYS A 168 . ? 1_555 ? 12 AC3 8 ALA A 143 ? ALA A 170 . ? 1_555 ? 13 AC3 8 VAL A 144 ? VAL A 171 . ? 1_555 ? 14 AC3 8 ARG A 177 ? ARG A 204 . ? 5_565 ? 15 AC3 8 GLY A 178 ? GLY A 205 . ? 5_565 ? 16 AC3 8 HOH H . ? HOH A 497 . ? 1_555 ? 17 AC4 2 ASN A 174 ? ASN A 201 . ? 1_555 ? 18 AC4 2 TYR A 175 ? TYR A 202 . ? 1_555 ? # _atom_sites.entry_id 4KMX _atom_sites.fract_transf_matrix[1][1] 0.010081 _atom_sites.fract_transf_matrix[1][2] 0.005820 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.011641 _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] 0.017584 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CL K 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 . TRP A 1 1 ? 34.967 61.735 -4.487 1.00 22.40 ? 28 TRP A N 1 ATOM 2 C CA . TRP A 1 1 ? 34.586 62.132 -3.139 1.00 24.64 ? 28 TRP A CA 1 ATOM 3 C C . TRP A 1 1 ? 33.373 63.054 -3.176 1.00 29.41 ? 28 TRP A C 1 ATOM 4 O O . TRP A 1 1 ? 33.310 63.979 -3.986 1.00 30.63 ? 28 TRP A O 1 ATOM 5 C CB . TRP A 1 1 ? 35.747 62.831 -2.432 1.00 25.83 ? 28 TRP A CB 1 ATOM 6 C CG . TRP A 1 1 ? 36.933 61.939 -2.192 1.00 29.46 ? 28 TRP A CG 1 ATOM 7 C CD1 . TRP A 1 1 ? 38.019 61.780 -3.003 1.00 29.14 ? 28 TRP A CD1 1 ATOM 8 C CD2 . TRP A 1 1 ? 37.150 61.085 -1.060 1.00 28.57 ? 28 TRP A CD2 1 ATOM 9 N NE1 . TRP A 1 1 ? 38.897 60.882 -2.449 1.00 27.58 ? 28 TRP A NE1 1 ATOM 10 C CE2 . TRP A 1 1 ? 38.390 60.440 -1.256 1.00 29.01 ? 28 TRP A CE2 1 ATOM 11 C CE3 . TRP A 1 1 ? 36.415 60.802 0.097 1.00 24.57 ? 28 TRP A CE3 1 ATOM 12 C CZ2 . TRP A 1 1 ? 38.915 59.531 -0.337 1.00 25.83 ? 28 TRP A CZ2 1 ATOM 13 C CZ3 . TRP A 1 1 ? 36.934 59.898 1.007 1.00 27.89 ? 28 TRP A CZ3 1 ATOM 14 C CH2 . TRP A 1 1 ? 38.174 59.272 0.784 1.00 28.87 ? 28 TRP A CH2 1 ATOM 15 N N . ALA A 1 2 ? 32.413 62.785 -2.296 1.00 28.40 ? 29 ALA A N 1 ATOM 16 C CA . ALA A 1 2 ? 31.211 63.596 -2.188 1.00 32.45 ? 29 ALA A CA 1 ATOM 17 C C . ALA A 1 2 ? 31.568 65.033 -1.831 1.00 34.41 ? 29 ALA A C 1 ATOM 18 O O . ALA A 1 2 ? 32.483 65.277 -1.035 1.00 32.41 ? 29 ALA A O 1 ATOM 19 C CB . ALA A 1 2 ? 30.270 63.009 -1.144 1.00 19.19 ? 29 ALA A CB 1 ATOM 20 N N . ARG A 1 3 ? 30.848 65.977 -2.434 1.00 30.61 ? 30 ARG A N 1 ATOM 21 C CA . ARG A 1 3 ? 31.005 67.387 -2.112 1.00 28.09 ? 30 ARG A CA 1 ATOM 22 C C . ARG A 1 3 ? 30.231 67.680 -0.836 1.00 27.19 ? 30 ARG A C 1 ATOM 23 O O . ARG A 1 3 ? 29.126 68.230 -0.865 1.00 29.55 ? 30 ARG A O 1 ATOM 24 C CB . ARG A 1 3 ? 30.535 68.265 -3.275 1.00 32.83 ? 30 ARG A CB 1 ATOM 25 C CG . ARG A 1 3 ? 31.386 68.105 -4.534 1.00 34.66 ? 30 ARG A CG 1 ATOM 26 C CD . ARG A 1 3 ? 30.672 68.613 -5.773 1.00 40.28 ? 30 ARG A CD 1 ATOM 27 N NE . ARG A 1 3 ? 30.805 70.053 -5.953 1.00 50.85 ? 30 ARG A NE 1 ATOM 28 C CZ . ARG A 1 3 ? 30.018 70.782 -6.742 1.00 55.67 ? 30 ARG A CZ 1 ATOM 29 N NH1 . ARG A 1 3 ? 29.026 70.206 -7.417 1.00 52.70 ? 30 ARG A NH1 1 ATOM 30 N NH2 . ARG A 1 3 ? 30.214 72.090 -6.845 1.00 54.72 ? 30 ARG A NH2 1 ATOM 31 N N . THR A 1 4 ? 30.836 67.300 0.284 1.00 25.92 ? 31 THR A N 1 ATOM 32 C CA . THR A 1 4 ? 30.204 67.381 1.594 1.00 31.15 ? 31 THR A CA 1 ATOM 33 C C . THR A 1 4 ? 29.903 68.809 2.064 1.00 33.51 ? 31 THR A C 1 ATOM 34 O O . THR A 1 4 ? 29.101 69.007 2.974 1.00 35.59 ? 31 THR A O 1 ATOM 35 C CB . THR A 1 4 ? 31.055 66.659 2.657 1.00 34.05 ? 31 THR A CB 1 ATOM 36 O OG1 . THR A 1 4 ? 32.397 67.158 2.613 1.00 35.37 ? 31 THR A OG1 1 ATOM 37 C CG2 . THR A 1 4 ? 31.070 65.154 2.395 1.00 29.65 ? 31 THR A CG2 1 ATOM 38 N N . GLU A 1 5 ? 30.547 69.796 1.452 1.00 28.94 ? 32 GLU A N 1 ATOM 39 C CA . GLU A 1 5 ? 30.235 71.188 1.744 1.00 31.64 ? 32 GLU A CA 1 ATOM 40 C C . GLU A 1 5 ? 28.863 71.557 1.181 1.00 35.40 ? 32 GLU A C 1 ATOM 41 O O . GLU A 1 5 ? 28.361 72.655 1.426 1.00 37.73 ? 32 GLU A O 1 ATOM 42 C CB . GLU A 1 5 ? 31.312 72.130 1.188 1.00 30.66 ? 32 GLU A CB 1 ATOM 43 C CG . GLU A 1 5 ? 31.278 72.322 -0.326 1.00 38.91 ? 32 GLU A CG 1 ATOM 44 C CD . GLU A 1 5 ? 31.971 71.202 -1.096 1.00 42.87 ? 32 GLU A CD 1 ATOM 45 O OE1 . GLU A 1 5 ? 32.429 70.223 -0.467 1.00 41.94 ? 32 GLU A OE1 1 ATOM 46 O OE2 . GLU A 1 5 ? 32.060 71.306 -2.339 1.00 43.73 ? 32 GLU A OE2 1 ATOM 47 N N . LEU A 1 6 ? 28.263 70.634 0.427 1.00 30.62 ? 33 LEU A N 1 ATOM 48 C CA . LEU A 1 6 ? 26.941 70.846 -0.153 1.00 24.47 ? 33 LEU A CA 1 ATOM 49 C C . LEU A 1 6 ? 25.905 69.915 0.454 1.00 25.42 ? 33 LEU A C 1 ATOM 50 O O . LEU A 1 6 ? 24.736 69.946 0.071 1.00 27.16 ? 33 LEU A O 1 ATOM 51 C CB . LEU A 1 6 ? 26.970 70.628 -1.669 1.00 21.56 ? 33 LEU A CB 1 ATOM 52 C CG . LEU A 1 6 ? 27.921 71.475 -2.513 1.00 23.51 ? 33 LEU A CG 1 ATOM 53 C CD1 . LEU A 1 6 ? 27.819 71.080 -3.982 1.00 23.12 ? 33 LEU A CD1 1 ATOM 54 C CD2 . LEU A 1 6 ? 27.649 72.967 -2.321 1.00 26.18 ? 33 LEU A CD2 1 ATOM 55 N N . LEU A 1 7 ? 26.331 69.080 1.396 1.00 23.02 ? 34 LEU A N 1 ATOM 56 C CA . LEU A 1 7 ? 25.468 68.019 1.894 1.00 18.58 ? 34 LEU A CA 1 ATOM 57 C C . LEU A 1 7 ? 25.267 68.106 3.391 1.00 24.51 ? 34 LEU A C 1 ATOM 58 O O . LEU A 1 7 ? 26.223 68.269 4.146 1.00 25.23 ? 34 LEU A O 1 ATOM 59 C CB . LEU A 1 7 ? 26.049 66.648 1.532 1.00 24.14 ? 34 LEU A CB 1 ATOM 60 C CG . LEU A 1 7 ? 26.203 66.383 0.034 1.00 29.60 ? 34 LEU A CG 1 ATOM 61 C CD1 . LEU A 1 7 ? 26.801 65.003 -0.208 1.00 31.27 ? 34 LEU A CD1 1 ATOM 62 C CD2 . LEU A 1 7 ? 24.853 66.527 -0.665 1.00 26.97 ? 34 LEU A CD2 1 ATOM 63 N N . ASN A 1 8 ? 24.017 67.976 3.821 1.00 23.01 ? 35 ASN A N 1 ATOM 64 C CA . ASN A 1 8 ? 23.703 68.077 5.236 1.00 28.40 ? 35 ASN A CA 1 ATOM 65 C C . ASN A 1 8 ? 24.370 69.334 5.811 1.00 34.72 ? 35 ASN A C 1 ATOM 66 O O . ASN A 1 8 ? 25.053 69.280 6.840 1.00 31.96 ? 35 ASN A O 1 ATOM 67 C CB . ASN A 1 8 ? 24.161 66.811 5.975 1.00 26.71 ? 35 ASN A CB 1 ATOM 68 C CG . ASN A 1 8 ? 23.442 66.611 7.300 1.00 30.54 ? 35 ASN A CG 1 ATOM 69 O OD1 . ASN A 1 8 ? 22.227 66.793 7.395 1.00 30.81 ? 35 ASN A OD1 1 ATOM 70 N ND2 . ASN A 1 8 ? 24.193 66.251 8.333 1.00 25.25 ? 35 ASN A ND2 1 ATOM 71 N N . VAL A 1 9 ? 24.182 70.459 5.119 1.00 33.63 ? 36 VAL A N 1 ATOM 72 C CA . VAL A 1 9 ? 24.778 71.731 5.522 1.00 32.49 ? 36 VAL A CA 1 ATOM 73 C C . VAL A 1 9 ? 23.761 72.858 5.725 1.00 28.18 ? 36 VAL A C 1 ATOM 74 O O . VAL A 1 9 ? 22.718 72.907 5.073 1.00 27.74 ? 36 VAL A O 1 ATOM 75 C CB . VAL A 1 9 ? 25.844 72.217 4.509 1.00 32.38 ? 36 VAL A CB 1 ATOM 76 C CG1 . VAL A 1 9 ? 27.065 71.303 4.542 1.00 37.08 ? 36 VAL A CG1 1 ATOM 77 C CG2 . VAL A 1 9 ? 25.255 72.297 3.109 1.00 24.12 ? 36 VAL A CG2 1 ATOM 78 N N . CYS A 1 10 ? 24.094 73.765 6.636 1.00 23.14 ? 37 CYS A N 1 ATOM 79 C CA . CYS A 1 10 ? 23.326 74.975 6.862 1.00 24.18 ? 37 CYS A CA 1 ATOM 80 C C . CYS A 1 10 ? 24.261 76.169 6.707 1.00 31.88 ? 37 CYS A C 1 ATOM 81 O O . CYS A 1 10 ? 25.379 76.161 7.227 1.00 33.20 ? 37 CYS A O 1 ATOM 82 C CB . CYS A 1 10 ? 22.736 74.971 8.272 1.00 23.81 ? 37 CYS A CB 1 ATOM 83 S SG . CYS A 1 10 ? 21.892 73.434 8.731 1.00 26.06 ? 37 CYS A SG 1 ATOM 84 N N . MET A 1 11 ? 23.811 77.188 5.983 1.00 28.60 ? 38 MET A N 1 ATOM 85 C CA . MET A 1 11 ? 24.589 78.404 5.828 1.00 27.99 ? 38 MET A CA 1 ATOM 86 C C . MET A 1 11 ? 24.261 79.340 6.982 1.00 33.44 ? 38 MET A C 1 ATOM 87 O O . MET A 1 11 ? 23.114 79.775 7.136 1.00 33.04 ? 38 MET A O 1 ATOM 88 C CB . MET A 1 11 ? 24.273 79.081 4.493 1.00 28.71 ? 38 MET A CB 1 ATOM 89 C CG . MET A 1 11 ? 25.111 80.330 4.204 1.00 28.09 ? 38 MET A CG 1 ATOM 90 S SD . MET A 1 11 ? 26.805 79.936 3.720 1.00 39.15 ? 38 MET A SD 1 ATOM 91 C CE . MET A 1 11 ? 27.006 81.021 2.307 1.00 39.62 ? 38 MET A CE 1 ATOM 92 N N . ASN A 1 12 ? 25.266 79.636 7.798 1.00 35.87 ? 39 ASN A N 1 ATOM 93 C CA . ASN A 1 12 ? 25.073 80.498 8.956 1.00 34.72 ? 39 ASN A CA 1 ATOM 94 C C . ASN A 1 12 ? 25.350 81.966 8.639 1.00 39.13 ? 39 ASN A C 1 ATOM 95 O O . ASN A 1 12 ? 25.808 82.299 7.539 1.00 34.95 ? 39 ASN A O 1 ATOM 96 C CB . ASN A 1 12 ? 25.908 80.015 10.154 1.00 38.80 ? 39 ASN A CB 1 ATOM 97 C CG . ASN A 1 12 ? 27.412 80.162 9.937 1.00 44.93 ? 39 ASN A CG 1 ATOM 98 O OD1 . ASN A 1 12 ? 27.866 80.958 9.114 1.00 46.70 ? 39 ASN A OD1 1 ATOM 99 N ND2 . ASN A 1 12 ? 28.192 79.393 10.691 1.00 45.51 ? 39 ASN A ND2 1 ATOM 100 N N . ALA A 1 13 ? 25.072 82.830 9.615 1.00 37.60 ? 40 ALA A N 1 ATOM 101 C CA . ALA A 1 13 ? 25.162 84.275 9.439 1.00 41.97 ? 40 ALA A CA 1 ATOM 102 C C . ALA A 1 13 ? 26.571 84.770 9.122 1.00 41.72 ? 40 ALA A C 1 ATOM 103 O O . ALA A 1 13 ? 26.736 85.843 8.546 1.00 40.96 ? 40 ALA A O 1 ATOM 104 C CB . ALA A 1 13 ? 24.613 84.992 10.670 1.00 44.17 ? 40 ALA A CB 1 ATOM 105 N N . LYS A 1 14 ? 27.583 83.993 9.500 1.00 41.95 ? 41 LYS A N 1 ATOM 106 C CA . LYS A 1 14 ? 28.966 84.344 9.182 1.00 44.28 ? 41 LYS A CA 1 ATOM 107 C C . LYS A 1 14 ? 29.376 83.689 7.868 1.00 41.00 ? 41 LYS A C 1 ATOM 108 O O . LYS A 1 14 ? 30.557 83.639 7.520 1.00 40.97 ? 41 LYS A O 1 ATOM 109 C CB . LYS A 1 14 ? 29.909 83.941 10.320 1.00 43.58 ? 41 LYS A CB 1 ATOM 110 N N . HIS A 1 15 ? 28.375 83.184 7.154 1.00 42.69 ? 42 HIS A N 1 ATOM 111 C CA . HIS A 1 15 ? 28.549 82.564 5.840 1.00 43.24 ? 42 HIS A CA 1 ATOM 112 C C . HIS A 1 15 ? 29.522 81.385 5.828 1.00 41.23 ? 42 HIS A C 1 ATOM 113 O O . HIS A 1 15 ? 30.261 81.172 4.867 1.00 39.26 ? 42 HIS A O 1 ATOM 114 C CB . HIS A 1 15 ? 28.897 83.616 4.790 1.00 44.70 ? 42 HIS A CB 1 ATOM 115 C CG . HIS A 1 15 ? 27.906 84.737 4.731 1.00 49.05 ? 42 HIS A CG 1 ATOM 116 N ND1 . HIS A 1 15 ? 28.118 85.950 5.348 1.00 49.29 ? 42 HIS A ND1 1 ATOM 117 C CD2 . HIS A 1 15 ? 26.680 84.812 4.160 1.00 43.84 ? 42 HIS A CD2 1 ATOM 118 C CE1 . HIS A 1 15 ? 27.073 86.734 5.141 1.00 50.12 ? 42 HIS A CE1 1 ATOM 119 N NE2 . HIS A 1 15 ? 26.187 86.068 4.425 1.00 45.29 ? 42 HIS A NE2 1 ATOM 120 N N . HIS A 1 16 ? 29.500 80.618 6.911 1.00 42.12 ? 43 HIS A N 1 ATOM 121 C CA . HIS A 1 16 ? 30.175 79.332 6.955 1.00 44.56 ? 43 HIS A CA 1 ATOM 122 C C . HIS A 1 16 ? 29.129 78.225 6.966 1.00 43.61 ? 43 HIS A C 1 ATOM 123 O O . HIS A 1 16 ? 28.052 78.382 7.539 1.00 45.27 ? 43 HIS A O 1 ATOM 124 C CB . HIS A 1 16 ? 31.057 79.228 8.199 1.00 49.48 ? 43 HIS A CB 1 ATOM 125 C CG . HIS A 1 16 ? 32.097 80.301 8.291 1.00 59.98 ? 43 HIS A CG 1 ATOM 126 N ND1 . HIS A 1 16 ? 33.072 80.473 7.334 1.00 62.68 ? 43 HIS A ND1 1 ATOM 127 C CD2 . HIS A 1 16 ? 32.315 81.253 9.229 1.00 63.77 ? 43 HIS A CD2 1 ATOM 128 C CE1 . HIS A 1 16 ? 33.845 81.491 7.675 1.00 65.16 ? 43 HIS A CE1 1 ATOM 129 N NE2 . HIS A 1 16 ? 33.408 81.979 8.821 1.00 65.22 ? 43 HIS A NE2 1 ATOM 130 N N . LYS A 1 17 ? 29.439 77.113 6.316 1.00 39.82 ? 44 LYS A N 1 ATOM 131 C CA . LYS A 1 17 ? 28.572 75.950 6.355 1.00 44.25 ? 44 LYS A CA 1 ATOM 132 C C . LYS A 1 17 ? 28.710 75.295 7.722 1.00 48.81 ? 44 LYS A C 1 ATOM 133 O O . LYS A 1 17 ? 29.821 75.006 8.165 1.00 49.81 ? 44 LYS A O 1 ATOM 134 C CB . LYS A 1 17 ? 28.971 74.957 5.264 1.00 48.70 ? 44 LYS A CB 1 ATOM 135 C CG . LYS A 1 17 ? 29.005 75.538 3.858 1.00 52.25 ? 44 LYS A CG 1 ATOM 136 C CD . LYS A 1 17 ? 27.608 75.714 3.277 1.00 50.56 ? 44 LYS A CD 1 ATOM 137 C CE . LYS A 1 17 ? 27.675 76.300 1.876 1.00 51.62 ? 44 LYS A CE 1 ATOM 138 N NZ . LYS A 1 17 ? 28.673 75.591 1.024 1.00 52.81 ? 44 LYS A NZ 1 ATOM 139 N N . GLU A 1 18 ? 27.587 75.076 8.398 1.00 44.71 ? 45 GLU A N 1 ATOM 140 C CA . GLU A 1 18 ? 27.599 74.341 9.657 1.00 40.31 ? 45 GLU A CA 1 ATOM 141 C C . GLU A 1 18 ? 26.603 73.185 9.629 1.00 41.89 ? 45 GLU A C 1 ATOM 142 O O . GLU A 1 18 ? 25.765 73.094 8.729 1.00 42.64 ? 45 GLU A O 1 ATOM 143 C CB . GLU A 1 18 ? 27.337 75.265 10.846 1.00 40.76 ? 45 GLU A CB 1 ATOM 144 C CG . GLU A 1 18 ? 25.999 75.970 10.819 1.00 48.62 ? 45 GLU A CG 1 ATOM 145 C CD . GLU A 1 18 ? 25.811 76.893 12.006 1.00 54.59 ? 45 GLU A CD 1 ATOM 146 O OE1 . GLU A 1 18 ? 26.826 77.306 12.601 1.00 55.41 ? 45 GLU A OE1 1 ATOM 147 O OE2 . GLU A 1 18 ? 24.648 77.198 12.349 1.00 61.39 ? 45 GLU A OE2 1 ATOM 148 N N . LYS A 1 19 ? 26.707 72.299 10.613 1.00 35.72 ? 46 LYS A N 1 ATOM 149 C CA . LYS A 1 19 ? 25.884 71.100 10.645 1.00 35.08 ? 46 LYS A CA 1 ATOM 150 C C . LYS A 1 19 ? 24.504 71.392 11.223 1.00 33.15 ? 46 LYS A C 1 ATOM 151 O O . LYS A 1 19 ? 24.362 72.243 12.101 1.00 31.72 ? 46 LYS A O 1 ATOM 152 C CB . LYS A 1 19 ? 26.583 70.001 11.446 1.00 39.30 ? 46 LYS A CB 1 ATOM 153 N N . PRO A 1 20 ? 23.476 70.696 10.718 1.00 30.87 ? 47 PRO A N 1 ATOM 154 C CA . PRO A 1 20 ? 22.137 70.824 11.300 1.00 32.26 ? 47 PRO A CA 1 ATOM 155 C C . PRO A 1 20 ? 22.092 70.169 12.681 1.00 35.36 ? 47 PRO A C 1 ATOM 156 O O . PRO A 1 20 ? 23.072 69.556 13.106 1.00 38.13 ? 47 PRO A O 1 ATOM 157 C CB . PRO A 1 20 ? 21.253 70.062 10.311 1.00 29.93 ? 47 PRO A CB 1 ATOM 158 C CG . PRO A 1 20 ? 22.164 69.089 9.662 1.00 25.92 ? 47 PRO A CG 1 ATOM 159 C CD . PRO A 1 20 ? 23.495 69.779 9.566 1.00 26.67 ? 47 PRO A CD 1 ATOM 160 N N . GLY A 1 21 ? 20.970 70.311 13.376 1.00 33.68 ? 48 GLY A N 1 ATOM 161 C CA . GLY A 1 21 ? 20.816 69.732 14.694 1.00 30.81 ? 48 GLY A CA 1 ATOM 162 C C . GLY A 1 21 ? 19.352 69.585 15.044 1.00 34.14 ? 48 GLY A C 1 ATOM 163 O O . GLY A 1 21 ? 18.487 69.743 14.182 1.00 31.96 ? 48 GLY A O 1 ATOM 164 N N . PRO A 1 22 ? 19.063 69.267 16.312 1.00 33.46 ? 49 PRO A N 1 ATOM 165 C CA . PRO A 1 22 ? 17.679 69.131 16.766 1.00 38.72 ? 49 PRO A CA 1 ATOM 166 C C . PRO A 1 22 ? 16.900 70.417 16.511 1.00 39.44 ? 49 PRO A C 1 ATOM 167 O O . PRO A 1 22 ? 17.389 71.513 16.794 1.00 39.86 ? 49 PRO A O 1 ATOM 168 C CB . PRO A 1 22 ? 17.830 68.883 18.270 1.00 42.50 ? 49 PRO A CB 1 ATOM 169 C CG . PRO A 1 22 ? 19.182 68.273 18.407 1.00 42.79 ? 49 PRO A CG 1 ATOM 170 C CD . PRO A 1 22 ? 20.028 68.969 17.382 1.00 39.49 ? 49 PRO A CD 1 ATOM 171 N N . GLU A 1 23 ? 15.700 70.268 15.966 1.00 32.52 ? 50 GLU A N 1 ATOM 172 C CA . GLU A 1 23 ? 14.845 71.401 15.648 1.00 33.43 ? 50 GLU A CA 1 ATOM 173 C C . GLU A 1 23 ? 14.540 72.231 16.885 1.00 33.00 ? 50 GLU A C 1 ATOM 174 O O . GLU A 1 23 ? 14.284 71.683 17.952 1.00 39.42 ? 50 GLU A O 1 ATOM 175 C CB . GLU A 1 23 ? 13.546 70.889 15.039 1.00 33.63 ? 50 GLU A CB 1 ATOM 176 C CG . GLU A 1 23 ? 12.646 71.956 14.480 1.00 33.83 ? 50 GLU A CG 1 ATOM 177 C CD . GLU A 1 23 ? 11.523 71.359 13.676 1.00 32.35 ? 50 GLU A CD 1 ATOM 178 O OE1 . GLU A 1 23 ? 10.669 70.680 14.280 1.00 35.09 ? 50 GLU A OE1 1 ATOM 179 O OE2 . GLU A 1 23 ? 11.511 71.546 12.442 1.00 30.59 ? 50 GLU A OE2 1 ATOM 180 N N . ASP A 1 24 ? 14.559 73.553 16.747 1.00 30.36 ? 51 ASP A N 1 ATOM 181 C CA . ASP A 1 24 ? 14.253 74.416 17.887 1.00 32.03 ? 51 ASP A CA 1 ATOM 182 C C . ASP A 1 24 ? 12.752 74.503 18.177 1.00 32.59 ? 51 ASP A C 1 ATOM 183 O O . ASP A 1 24 ? 11.922 74.054 17.382 1.00 30.00 ? 51 ASP A O 1 ATOM 184 C CB . ASP A 1 24 ? 14.880 75.813 17.733 1.00 33.89 ? 51 ASP A CB 1 ATOM 185 C CG . ASP A 1 24 ? 14.332 76.588 16.540 1.00 32.37 ? 51 ASP A CG 1 ATOM 186 O OD1 . ASP A 1 24 ? 13.144 76.425 16.182 1.00 33.70 ? 51 ASP A OD1 1 ATOM 187 O OD2 . ASP A 1 24 ? 15.101 77.378 15.962 1.00 30.99 ? 51 ASP A OD2 1 ATOM 188 N N . LYS A 1 25 ? 12.419 75.083 19.324 1.00 31.53 ? 52 LYS A N 1 ATOM 189 C CA . LYS A 1 25 ? 11.038 75.171 19.782 1.00 34.02 ? 52 LYS A CA 1 ATOM 190 C C . LYS A 1 25 ? 10.158 76.001 18.845 1.00 36.35 ? 52 LYS A C 1 ATOM 191 O O . LYS A 1 25 ? 9.024 75.623 18.546 1.00 37.23 ? 52 LYS A O 1 ATOM 192 C CB . LYS A 1 25 ? 10.997 75.746 21.201 1.00 39.22 ? 52 LYS A CB 1 ATOM 193 C CG . LYS A 1 25 ? 9.617 75.790 21.830 1.00 46.56 ? 52 LYS A CG 1 ATOM 194 C CD . LYS A 1 25 ? 9.009 74.405 21.944 1.00 50.47 ? 52 LYS A CD 1 ATOM 195 C CE . LYS A 1 25 ? 7.896 74.395 22.972 1.00 56.24 ? 52 LYS A CE 1 ATOM 196 N NZ . LYS A 1 25 ? 8.381 74.862 24.302 1.00 60.98 ? 52 LYS A NZ 1 ATOM 197 N N . LEU A 1 26 ? 10.685 77.131 18.383 1.00 35.37 ? 53 LEU A N 1 ATOM 198 C CA . LEU A 1 26 ? 9.935 78.020 17.502 1.00 30.17 ? 53 LEU A CA 1 ATOM 199 C C . LEU A 1 26 ? 9.445 77.293 16.251 1.00 29.59 ? 53 LEU A C 1 ATOM 200 O O . LEU A 1 26 ? 8.411 77.641 15.687 1.00 31.91 ? 53 LEU A O 1 ATOM 201 C CB . LEU A 1 26 ? 10.785 79.234 17.112 1.00 29.08 ? 53 LEU A CB 1 ATOM 202 C CG . LEU A 1 26 ? 10.128 80.260 16.182 1.00 29.24 ? 53 LEU A CG 1 ATOM 203 C CD1 . LEU A 1 26 ? 8.911 80.903 16.837 1.00 27.93 ? 53 LEU A CD1 1 ATOM 204 C CD2 . LEU A 1 26 ? 11.128 81.318 15.778 1.00 29.97 ? 53 LEU A CD2 1 ATOM 205 N N . HIS A 1 27 ? 10.187 76.275 15.828 1.00 29.95 ? 54 HIS A N 1 ATOM 206 C CA . HIS A 1 27 ? 9.868 75.567 14.594 1.00 22.41 ? 54 HIS A CA 1 ATOM 207 C C . HIS A 1 27 ? 9.208 74.210 14.835 1.00 26.64 ? 54 HIS A C 1 ATOM 208 O O . HIS A 1 27 ? 9.263 73.323 13.977 1.00 29.67 ? 54 HIS A O 1 ATOM 209 C CB . HIS A 1 27 ? 11.130 75.406 13.736 1.00 19.58 ? 54 HIS A CB 1 ATOM 210 C CG . HIS A 1 27 ? 11.627 76.692 13.155 1.00 26.48 ? 54 HIS A CG 1 ATOM 211 N ND1 . HIS A 1 27 ? 12.322 77.625 13.896 1.00 28.20 ? 54 HIS A ND1 1 ATOM 212 C CD2 . HIS A 1 27 ? 11.509 77.214 11.911 1.00 26.35 ? 54 HIS A CD2 1 ATOM 213 C CE1 . HIS A 1 27 ? 12.617 78.660 13.132 1.00 25.33 ? 54 HIS A CE1 1 ATOM 214 N NE2 . HIS A 1 27 ? 12.134 78.438 11.923 1.00 27.38 ? 54 HIS A NE2 1 ATOM 215 N N . GLU A 1 28 ? 8.575 74.058 15.996 1.00 28.24 ? 55 GLU A N 1 ATOM 216 C CA . GLU A 1 28 ? 7.919 72.804 16.353 1.00 34.72 ? 55 GLU A CA 1 ATOM 217 C C . GLU A 1 28 ? 6.912 72.326 15.305 1.00 36.32 ? 55 GLU A C 1 ATOM 218 O O . GLU A 1 28 ? 6.698 71.125 15.152 1.00 39.44 ? 55 GLU A O 1 ATOM 219 C CB . GLU A 1 28 ? 7.244 72.905 17.725 1.00 45.21 ? 55 GLU A CB 1 ATOM 220 C CG . GLU A 1 28 ? 6.430 71.668 18.094 1.00 56.18 ? 55 GLU A CG 1 ATOM 221 C CD . GLU A 1 28 ? 5.995 71.648 19.551 1.00 66.66 ? 55 GLU A CD 1 ATOM 222 O OE1 . GLU A 1 28 ? 6.874 71.556 20.437 1.00 70.97 ? 55 GLU A OE1 1 ATOM 223 O OE2 . GLU A 1 28 ? 4.774 71.715 19.808 1.00 68.23 ? 55 GLU A OE2 1 ATOM 224 N N . GLN A 1 29 ? 6.296 73.254 14.580 1.00 31.35 ? 56 GLN A N 1 ATOM 225 C CA . GLN A 1 29 ? 5.282 72.869 13.602 1.00 31.62 ? 56 GLN A CA 1 ATOM 226 C C . GLN A 1 29 ? 5.896 72.351 12.302 1.00 33.23 ? 56 GLN A C 1 ATOM 227 O O . GLN A 1 29 ? 5.221 71.696 11.507 1.00 36.25 ? 56 GLN A O 1 ATOM 228 C CB . GLN A 1 29 ? 4.310 74.021 13.331 1.00 34.74 ? 56 GLN A CB 1 ATOM 229 C CG . GLN A 1 29 ? 4.911 75.196 12.593 1.00 32.36 ? 56 GLN A CG 1 ATOM 230 C CD . GLN A 1 29 ? 3.985 76.398 12.596 1.00 34.52 ? 56 GLN A CD 1 ATOM 231 O OE1 . GLN A 1 29 ? 4.117 77.287 13.429 1.00 35.78 ? 56 GLN A OE1 1 ATOM 232 N NE2 . GLN A 1 29 ? 3.037 76.424 11.666 1.00 34.66 ? 56 GLN A NE2 1 ATOM 233 N N . CYS A 1 30 ? 7.175 72.647 12.092 1.00 26.85 ? 57 CYS A N 1 ATOM 234 C CA . CYS A 1 30 ? 7.911 72.091 10.966 1.00 27.57 ? 57 CYS A CA 1 ATOM 235 C C . CYS A 1 30 ? 8.298 70.635 11.296 1.00 35.23 ? 57 CYS A C 1 ATOM 236 O O . CYS A 1 30 ? 9.479 70.284 11.376 1.00 33.63 ? 57 CYS A O 1 ATOM 237 C CB . CYS A 1 30 ? 9.136 72.960 10.651 1.00 29.35 ? 57 CYS A CB 1 ATOM 238 S SG . CYS A 1 30 ? 8.744 74.719 10.312 1.00 28.91 ? 57 CYS A SG 1 ATOM 239 N N . ARG A 1 31 ? 7.275 69.801 11.479 1.00 35.90 ? 58 ARG A N 1 ATOM 240 C CA . ARG A 1 31 ? 7.422 68.426 11.972 1.00 42.51 ? 58 ARG A CA 1 ATOM 241 C C . ARG A 1 31 ? 8.458 67.566 11.252 1.00 35.02 ? 58 ARG A C 1 ATOM 242 O O . ARG A 1 31 ? 9.239 66.882 11.904 1.00 36.54 ? 58 ARG A O 1 ATOM 243 C CB . ARG A 1 31 ? 6.071 67.699 11.952 1.00 51.46 ? 58 ARG A CB 1 ATOM 244 C CG . ARG A 1 31 ? 5.022 68.301 12.863 1.00 63.86 ? 58 ARG A CG 1 ATOM 245 C CD . ARG A 1 31 ? 5.339 68.044 14.327 1.00 75.05 ? 58 ARG A CD 1 ATOM 246 N NE . ARG A 1 31 ? 4.444 68.795 15.201 1.00 81.35 ? 58 ARG A NE 1 ATOM 247 C CZ . ARG A 1 31 ? 4.421 68.686 16.524 1.00 85.87 ? 58 ARG A CZ 1 ATOM 248 N NH1 . ARG A 1 31 ? 5.243 67.845 17.138 1.00 85.59 ? 58 ARG A NH1 1 ATOM 249 N NH2 . ARG A 1 31 ? 3.571 69.417 17.233 1.00 89.09 ? 58 ARG A NH2 1 ATOM 250 N N . PRO A 1 32 ? 8.451 67.579 9.908 1.00 32.74 ? 59 PRO A N 1 ATOM 251 C CA . PRO A 1 32 ? 9.339 66.694 9.148 1.00 33.54 ? 59 PRO A CA 1 ATOM 252 C C . PRO A 1 32 ? 10.817 66.851 9.509 1.00 34.84 ? 59 PRO A C 1 ATOM 253 O O . PRO A 1 32 ? 11.586 65.914 9.295 1.00 38.12 ? 59 PRO A O 1 ATOM 254 C CB . PRO A 1 32 ? 9.091 67.126 7.698 1.00 31.73 ? 59 PRO A CB 1 ATOM 255 C CG . PRO A 1 32 ? 7.692 67.629 7.706 1.00 25.51 ? 59 PRO A CG 1 ATOM 256 C CD . PRO A 1 32 ? 7.569 68.354 9.016 1.00 29.48 ? 59 PRO A CD 1 ATOM 257 N N . TRP A 1 33 ? 11.195 68.003 10.059 1.00 31.62 ? 60 TRP A N 1 ATOM 258 C CA . TRP A 1 33 ? 12.599 68.326 10.317 1.00 28.29 ? 60 TRP A CA 1 ATOM 259 C C . TRP A 1 33 ? 12.980 68.247 11.792 1.00 27.84 ? 60 TRP A C 1 ATOM 260 O O . TRP A 1 33 ? 14.041 68.729 12.189 1.00 33.46 ? 60 TRP A O 1 ATOM 261 C CB . TRP A 1 33 ? 12.916 69.732 9.785 1.00 30.91 ? 60 TRP A CB 1 ATOM 262 C CG . TRP A 1 33 ? 12.806 69.816 8.306 1.00 31.44 ? 60 TRP A CG 1 ATOM 263 C CD1 . TRP A 1 33 ? 13.773 69.504 7.403 1.00 31.57 ? 60 TRP A CD1 1 ATOM 264 C CD2 . TRP A 1 33 ? 11.652 70.200 7.545 1.00 30.24 ? 60 TRP A CD2 1 ATOM 265 N NE1 . TRP A 1 33 ? 13.302 69.686 6.130 1.00 28.27 ? 60 TRP A NE1 1 ATOM 266 C CE2 . TRP A 1 33 ? 12.003 70.107 6.184 1.00 28.80 ? 60 TRP A CE2 1 ATOM 267 C CE3 . TRP A 1 33 ? 10.361 70.615 7.880 1.00 27.94 ? 60 TRP A CE3 1 ATOM 268 C CZ2 . TRP A 1 33 ? 11.113 70.413 5.158 1.00 25.59 ? 60 TRP A CZ2 1 ATOM 269 C CZ3 . TRP A 1 33 ? 9.475 70.917 6.858 1.00 26.08 ? 60 TRP A CZ3 1 ATOM 270 C CH2 . TRP A 1 33 ? 9.856 70.817 5.516 1.00 21.24 ? 60 TRP A CH2 1 ATOM 271 N N . ARG A 1 34 ? 12.119 67.640 12.599 1.00 30.77 ? 61 ARG A N 1 ATOM 272 C CA . ARG A 1 34 ? 12.327 67.597 14.043 1.00 42.57 ? 61 ARG A CA 1 ATOM 273 C C . ARG A 1 34 ? 13.708 67.071 14.450 1.00 41.53 ? 61 ARG A C 1 ATOM 274 O O . ARG A 1 34 ? 14.326 67.600 15.373 1.00 43.21 ? 61 ARG A O 1 ATOM 275 C CB . ARG A 1 34 ? 11.225 66.776 14.721 1.00 51.22 ? 61 ARG A CB 1 ATOM 276 C CG . ARG A 1 34 ? 11.177 66.933 16.234 1.00 56.35 ? 61 ARG A CG 1 ATOM 277 C CD . ARG A 1 34 ? 10.065 66.096 16.842 1.00 68.36 ? 61 ARG A CD 1 ATOM 278 N NE . ARG A 1 34 ? 10.196 64.686 16.484 1.00 79.15 ? 61 ARG A NE 1 ATOM 279 C CZ . ARG A 1 34 ? 10.927 63.804 17.161 1.00 83.38 ? 61 ARG A CZ 1 ATOM 280 N NH1 . ARG A 1 34 ? 11.597 64.181 18.243 1.00 85.58 ? 61 ARG A NH1 1 ATOM 281 N NH2 . ARG A 1 34 ? 10.987 62.542 16.756 1.00 82.50 ? 61 ARG A NH2 1 ATOM 282 N N . LYS A 1 35 ? 14.194 66.044 13.757 1.00 41.80 ? 62 LYS A N 1 ATOM 283 C CA . LYS A 1 35 ? 15.438 65.374 14.155 1.00 43.11 ? 62 LYS A CA 1 ATOM 284 C C . LYS A 1 35 ? 16.710 65.953 13.533 1.00 39.49 ? 62 LYS A C 1 ATOM 285 O O . LYS A 1 35 ? 17.809 65.728 14.039 1.00 42.69 ? 62 LYS A O 1 ATOM 286 C CB . LYS A 1 35 ? 15.361 63.872 13.862 1.00 43.16 ? 62 LYS A CB 1 ATOM 287 C CG . LYS A 1 35 ? 14.409 63.116 14.773 1.00 54.78 ? 62 LYS A CG 1 ATOM 288 C CD . LYS A 1 35 ? 14.308 61.651 14.385 1.00 66.08 ? 62 LYS A CD 1 ATOM 289 C CE . LYS A 1 35 ? 13.345 60.904 15.297 1.00 76.54 ? 62 LYS A CE 1 ATOM 290 N NZ . LYS A 1 35 ? 13.155 59.482 14.880 1.00 83.70 ? 62 LYS A NZ 1 ATOM 291 N N . ASN A 1 36 ? 16.562 66.689 12.438 1.00 37.83 ? 63 ASN A N 1 ATOM 292 C CA . ASN A 1 36 ? 17.719 67.199 11.711 1.00 36.50 ? 63 ASN A CA 1 ATOM 293 C C . ASN A 1 36 ? 17.357 68.453 10.918 1.00 35.95 ? 63 ASN A C 1 ATOM 294 O O . ASN A 1 36 ? 16.751 68.370 9.847 1.00 34.25 ? 63 ASN A O 1 ATOM 295 C CB . ASN A 1 36 ? 18.270 66.112 10.784 1.00 35.84 ? 63 ASN A CB 1 ATOM 296 C CG . ASN A 1 36 ? 19.699 66.373 10.364 1.00 38.12 ? 63 ASN A CG 1 ATOM 297 O OD1 . ASN A 1 36 ? 20.515 66.842 11.156 1.00 41.19 ? 63 ASN A OD1 1 ATOM 298 N ND2 . ASN A 1 36 ? 20.011 66.069 9.109 1.00 36.89 ? 63 ASN A ND2 1 ATOM 299 N N . ALA A 1 37 ? 17.737 69.613 11.447 1.00 32.34 ? 64 ALA A N 1 ATOM 300 C CA . ALA A 1 37 ? 17.272 70.886 10.907 1.00 26.96 ? 64 ALA A CA 1 ATOM 301 C C . ALA A 1 37 ? 18.315 71.994 10.985 1.00 28.37 ? 64 ALA A C 1 ATOM 302 O O . ALA A 1 37 ? 19.165 72.009 11.881 1.00 30.78 ? 64 ALA A O 1 ATOM 303 C CB . ALA A 1 37 ? 15.994 71.328 11.635 1.00 28.42 ? 64 ALA A CB 1 ATOM 304 N N . CYS A 1 38 ? 18.228 72.931 10.045 1.00 25.42 ? 65 CYS A N 1 ATOM 305 C CA . CYS A 1 38 ? 19.028 74.148 10.091 1.00 29.78 ? 65 CYS A CA 1 ATOM 306 C C . CYS A 1 38 ? 18.353 75.191 10.978 1.00 28.53 ? 65 CYS A C 1 ATOM 307 O O . CYS A 1 38 ? 18.932 76.229 11.289 1.00 33.75 ? 65 CYS A O 1 ATOM 308 C CB . CYS A 1 38 ? 19.240 74.707 8.686 1.00 23.84 ? 65 CYS A CB 1 ATOM 309 S SG . CYS A 1 38 ? 20.203 73.635 7.624 1.00 28.28 ? 65 CYS A SG 1 ATOM 310 N N . CYS A 1 39 ? 17.118 74.912 11.371 1.00 26.18 ? 66 CYS A N 1 ATOM 311 C CA . CYS A 1 39 ? 16.428 75.726 12.365 1.00 29.98 ? 66 CYS A CA 1 ATOM 312 C C . CYS A 1 39 ? 16.555 75.009 13.704 1.00 31.41 ? 66 CYS A C 1 ATOM 313 O O . CYS A 1 39 ? 15.596 74.426 14.207 1.00 33.34 ? 66 CYS A O 1 ATOM 314 C CB . CYS A 1 39 ? 14.955 75.907 11.984 1.00 28.02 ? 66 CYS A CB 1 ATOM 315 S SG . CYS A 1 39 ? 14.025 74.356 11.831 1.00 27.60 ? 66 CYS A SG 1 ATOM 316 N N . SER A 1 40 ? 17.754 75.050 14.274 1.00 35.83 ? 67 SER A N 1 ATOM 317 C CA . SER A 1 40 ? 18.086 74.175 15.388 1.00 43.46 ? 67 SER A CA 1 ATOM 318 C C . SER A 1 40 ? 18.521 74.904 16.651 1.00 46.77 ? 67 SER A C 1 ATOM 319 O O . SER A 1 40 ? 18.976 76.045 16.608 1.00 38.76 ? 67 SER A O 1 ATOM 320 C CB . SER A 1 40 ? 19.180 73.191 14.972 1.00 44.86 ? 67 SER A CB 1 ATOM 321 O OG . SER A 1 40 ? 20.334 73.890 14.546 1.00 46.65 ? 67 SER A OG 1 ATOM 322 N N . THR A 1 41 ? 18.381 74.203 17.772 1.00 59.28 ? 68 THR A N 1 ATOM 323 C CA . THR A 1 41 ? 18.808 74.685 19.078 1.00 67.67 ? 68 THR A CA 1 ATOM 324 C C . THR A 1 41 ? 20.271 75.119 19.066 1.00 67.53 ? 68 THR A C 1 ATOM 325 O O . THR A 1 41 ? 20.588 76.273 19.353 1.00 68.53 ? 68 THR A O 1 ATOM 326 C CB . THR A 1 41 ? 18.616 73.587 20.144 1.00 74.88 ? 68 THR A CB 1 ATOM 327 O OG1 . THR A 1 41 ? 17.232 73.212 20.203 1.00 71.28 ? 68 THR A OG1 1 ATOM 328 C CG2 . THR A 1 41 ? 19.071 74.076 21.512 1.00 82.81 ? 68 THR A CG2 1 ATOM 329 N N . LYS A 1 49 ? 16.106 87.551 18.415 1.00 63.10 ? 76 LYS A N 1 ATOM 330 C CA . LYS A 1 49 ? 16.788 86.294 18.127 1.00 64.14 ? 76 LYS A CA 1 ATOM 331 C C . LYS A 1 49 ? 16.378 85.724 16.767 1.00 61.33 ? 76 LYS A C 1 ATOM 332 O O . LYS A 1 49 ? 17.152 85.774 15.810 1.00 64.91 ? 76 LYS A O 1 ATOM 333 C CB . LYS A 1 49 ? 16.529 85.280 19.238 1.00 64.68 ? 76 LYS A CB 1 ATOM 334 N N . ASP A 1 50 ? 15.159 85.196 16.683 1.00 50.53 ? 77 ASP A N 1 ATOM 335 C CA . ASP A 1 50 ? 14.688 84.544 15.462 1.00 43.03 ? 77 ASP A CA 1 ATOM 336 C C . ASP A 1 50 ? 14.369 85.526 14.340 1.00 42.68 ? 77 ASP A C 1 ATOM 337 O O . ASP A 1 50 ? 14.198 86.723 14.569 1.00 46.37 ? 77 ASP A O 1 ATOM 338 C CB . ASP A 1 50 ? 13.449 83.687 15.742 1.00 42.27 ? 77 ASP A CB 1 ATOM 339 C CG . ASP A 1 50 ? 12.164 84.508 15.788 1.00 39.61 ? 77 ASP A CG 1 ATOM 340 O OD1 . ASP A 1 50 ? 11.636 84.854 14.707 1.00 33.51 ? 77 ASP A OD1 1 ATOM 341 O OD2 . ASP A 1 50 ? 11.682 84.799 16.906 1.00 41.01 ? 77 ASP A OD2 1 ATOM 342 N N . VAL A 1 51 ? 14.283 84.994 13.126 1.00 39.64 ? 78 VAL A N 1 ATOM 343 C CA . VAL A 1 51 ? 13.907 85.769 11.951 1.00 36.49 ? 78 VAL A CA 1 ATOM 344 C C . VAL A 1 51 ? 12.878 84.979 11.139 1.00 33.54 ? 78 VAL A C 1 ATOM 345 O O . VAL A 1 51 ? 12.911 84.978 9.915 1.00 32.74 ? 78 VAL A O 1 ATOM 346 C CB . VAL A 1 51 ? 15.137 86.070 11.068 1.00 36.25 ? 78 VAL A CB 1 ATOM 347 C CG1 . VAL A 1 51 ? 16.120 86.963 11.808 1.00 33.34 ? 78 VAL A CG1 1 ATOM 348 C CG2 . VAL A 1 51 ? 15.817 84.773 10.641 1.00 39.51 ? 78 VAL A CG2 1 ATOM 349 N N . SER A 1 52 ? 11.954 84.322 11.831 1.00 32.86 ? 79 SER A N 1 ATOM 350 C CA . SER A 1 52 ? 11.106 83.310 11.204 1.00 31.57 ? 79 SER A CA 1 ATOM 351 C C . SER A 1 52 ? 9.822 83.838 10.562 1.00 27.89 ? 79 SER A C 1 ATOM 352 O O . SER A 1 52 ? 9.052 84.567 11.181 1.00 22.30 ? 79 SER A O 1 ATOM 353 C CB . SER A 1 52 ? 10.758 82.209 12.208 1.00 22.62 ? 79 SER A CB 1 ATOM 354 O OG . SER A 1 52 ? 9.802 81.330 11.652 1.00 24.32 ? 79 SER A OG 1 ATOM 355 N N . TYR A 1 53 ? 9.593 83.432 9.318 1.00 25.80 ? 80 TYR A N 1 ATOM 356 C CA . TYR A 1 53 ? 8.359 83.751 8.622 1.00 23.34 ? 80 TYR A CA 1 ATOM 357 C C . TYR A 1 53 ? 7.207 82.862 9.093 1.00 28.32 ? 80 TYR A C 1 ATOM 358 O O . TYR A 1 53 ? 6.154 82.810 8.464 1.00 28.39 ? 80 TYR A O 1 ATOM 359 C CB . TYR A 1 53 ? 8.543 83.636 7.106 1.00 19.80 ? 80 TYR A CB 1 ATOM 360 C CG . TYR A 1 53 ? 9.002 84.917 6.453 1.00 20.92 ? 80 TYR A CG 1 ATOM 361 C CD1 . TYR A 1 53 ? 9.591 85.932 7.201 1.00 22.61 ? 80 TYR A CD1 1 ATOM 362 C CD2 . TYR A 1 53 ? 8.820 85.126 5.089 1.00 21.92 ? 80 TYR A CD2 1 ATOM 363 C CE1 . TYR A 1 53 ? 10.002 87.116 6.602 1.00 25.82 ? 80 TYR A CE1 1 ATOM 364 C CE2 . TYR A 1 53 ? 9.225 86.302 4.487 1.00 20.64 ? 80 TYR A CE2 1 ATOM 365 C CZ . TYR A 1 53 ? 9.814 87.295 5.246 1.00 24.88 ? 80 TYR A CZ 1 ATOM 366 O OH . TYR A 1 53 ? 10.213 88.470 4.644 1.00 26.36 ? 80 TYR A OH 1 ATOM 367 N N . LEU A 1 54 ? 7.409 82.157 10.200 1.00 28.70 ? 81 LEU A N 1 ATOM 368 C CA . LEU A 1 54 ? 6.303 81.445 10.826 1.00 29.05 ? 81 LEU A CA 1 ATOM 369 C C . LEU A 1 54 ? 5.355 82.443 11.492 1.00 27.45 ? 81 LEU A C 1 ATOM 370 O O . LEU A 1 54 ? 4.211 82.114 11.788 1.00 28.93 ? 81 LEU A O 1 ATOM 371 C CB . LEU A 1 54 ? 6.804 80.399 11.830 1.00 28.75 ? 81 LEU A CB 1 ATOM 372 C CG . LEU A 1 54 ? 7.501 79.171 11.230 1.00 28.79 ? 81 LEU A CG 1 ATOM 373 C CD1 . LEU A 1 54 ? 8.070 78.265 12.317 1.00 24.05 ? 81 LEU A CD1 1 ATOM 374 C CD2 . LEU A 1 54 ? 6.537 78.403 10.335 1.00 28.76 ? 81 LEU A CD2 1 ATOM 375 N N . TYR A 1 55 ? 5.826 83.668 11.719 1.00 25.93 ? 82 TYR A N 1 ATOM 376 C CA . TYR A 1 55 ? 4.961 84.699 12.288 1.00 28.09 ? 82 TYR A CA 1 ATOM 377 C C . TYR A 1 55 ? 5.326 86.148 11.924 1.00 30.39 ? 82 TYR A C 1 ATOM 378 O O . TYR A 1 55 ? 4.500 87.045 12.078 1.00 29.99 ? 82 TYR A O 1 ATOM 379 C CB . TYR A 1 55 ? 4.867 84.546 13.809 1.00 25.88 ? 82 TYR A CB 1 ATOM 380 C CG . TYR A 1 55 ? 6.099 85.001 14.562 1.00 25.73 ? 82 TYR A CG 1 ATOM 381 C CD1 . TYR A 1 55 ? 6.184 86.292 15.061 1.00 23.81 ? 82 TYR A CD1 1 ATOM 382 C CD2 . TYR A 1 55 ? 7.170 84.141 14.777 1.00 25.30 ? 82 TYR A CD2 1 ATOM 383 C CE1 . TYR A 1 55 ? 7.297 86.720 15.756 1.00 26.36 ? 82 TYR A CE1 1 ATOM 384 C CE2 . TYR A 1 55 ? 8.295 84.562 15.473 1.00 31.17 ? 82 TYR A CE2 1 ATOM 385 C CZ . TYR A 1 55 ? 8.349 85.855 15.962 1.00 30.73 ? 82 TYR A CZ 1 ATOM 386 O OH . TYR A 1 55 ? 9.451 86.297 16.656 1.00 29.54 ? 82 TYR A OH 1 ATOM 387 N N . ARG A 1 56 ? 6.545 86.378 11.441 1.00 28.22 ? 83 ARG A N 1 ATOM 388 C CA . ARG A 1 56 ? 6.985 87.737 11.116 1.00 28.98 ? 83 ARG A CA 1 ATOM 389 C C . ARG A 1 56 ? 6.491 88.255 9.759 1.00 30.02 ? 83 ARG A C 1 ATOM 390 O O . ARG A 1 56 ? 6.695 89.422 9.421 1.00 28.03 ? 83 ARG A O 1 ATOM 391 C CB . ARG A 1 56 ? 8.509 87.847 11.197 1.00 30.85 ? 83 ARG A CB 1 ATOM 392 C CG . ARG A 1 56 ? 9.059 87.744 12.612 1.00 33.68 ? 83 ARG A CG 1 ATOM 393 C CD . ARG A 1 56 ? 10.580 87.708 12.618 1.00 36.20 ? 83 ARG A CD 1 ATOM 394 N NE . ARG A 1 56 ? 11.112 87.562 13.971 1.00 36.61 ? 83 ARG A NE 1 ATOM 395 C CZ . ARG A 1 56 ? 11.389 88.583 14.776 1.00 33.13 ? 83 ARG A CZ 1 ATOM 396 N NH1 . ARG A 1 56 ? 11.183 89.826 14.364 1.00 28.11 ? 83 ARG A NH1 1 ATOM 397 N NH2 . ARG A 1 56 ? 11.870 88.362 15.993 1.00 31.80 ? 83 ARG A NH2 1 ATOM 398 N N . PHE A 1 57 ? 5.840 87.393 8.986 1.00 25.55 ? 84 PHE A N 1 ATOM 399 C CA . PHE A 1 57 ? 5.359 87.782 7.669 1.00 21.85 ? 84 PHE A CA 1 ATOM 400 C C . PHE A 1 57 ? 3.840 87.804 7.615 1.00 24.86 ? 84 PHE A C 1 ATOM 401 O O . PHE A 1 57 ? 3.181 86.869 8.056 1.00 29.41 ? 84 PHE A O 1 ATOM 402 C CB . PHE A 1 57 ? 5.910 86.847 6.593 1.00 20.07 ? 84 PHE A CB 1 ATOM 403 C CG . PHE A 1 57 ? 5.616 87.299 5.189 1.00 20.80 ? 84 PHE A CG 1 ATOM 404 C CD1 . PHE A 1 57 ? 6.470 88.177 4.537 1.00 19.70 ? 84 PHE A CD1 1 ATOM 405 C CD2 . PHE A 1 57 ? 4.495 86.837 4.515 1.00 18.04 ? 84 PHE A CD2 1 ATOM 406 C CE1 . PHE A 1 57 ? 6.210 88.585 3.239 1.00 21.14 ? 84 PHE A CE1 1 ATOM 407 C CE2 . PHE A 1 57 ? 4.227 87.242 3.222 1.00 19.51 ? 84 PHE A CE2 1 ATOM 408 C CZ . PHE A 1 57 ? 5.083 88.119 2.580 1.00 20.58 ? 84 PHE A CZ 1 ATOM 409 N N . ASN A 1 58 ? 3.291 88.881 7.068 1.00 26.72 ? 85 ASN A N 1 ATOM 410 C CA . ASN A 1 58 ? 1.847 89.028 6.949 1.00 29.95 ? 85 ASN A CA 1 ATOM 411 C C . ASN A 1 58 ? 1.276 88.296 5.725 1.00 28.40 ? 85 ASN A C 1 ATOM 412 O O . ASN A 1 58 ? 1.277 88.829 4.611 1.00 24.58 ? 85 ASN A O 1 ATOM 413 C CB . ASN A 1 58 ? 1.479 90.513 6.912 1.00 28.80 ? 85 ASN A CB 1 ATOM 414 C CG . ASN A 1 58 ? -0.019 90.748 6.919 1.00 29.32 ? 85 ASN A CG 1 ATOM 415 O OD1 . ASN A 1 58 ? -0.788 89.912 7.386 1.00 28.96 ? 85 ASN A OD1 1 ATOM 416 N ND2 . ASN A 1 58 ? -0.438 91.897 6.404 1.00 27.96 ? 85 ASN A ND2 1 ATOM 417 N N . TRP A 1 59 ? 0.804 87.071 5.942 1.00 23.52 ? 86 TRP A N 1 ATOM 418 C CA . TRP A 1 59 ? 0.124 86.301 4.902 1.00 22.62 ? 86 TRP A CA 1 ATOM 419 C C . TRP A 1 59 ? -1.199 86.965 4.521 1.00 22.19 ? 86 TRP A C 1 ATOM 420 O O . TRP A 1 59 ? -1.682 86.825 3.395 1.00 23.00 ? 86 TRP A O 1 ATOM 421 C CB . TRP A 1 59 ? -0.134 84.857 5.372 1.00 24.37 ? 86 TRP A CB 1 ATOM 422 C CG . TRP A 1 59 ? 1.092 84.171 5.910 1.00 26.49 ? 86 TRP A CG 1 ATOM 423 C CD1 . TRP A 1 59 ? 1.296 83.736 7.185 1.00 29.51 ? 86 TRP A CD1 1 ATOM 424 C CD2 . TRP A 1 59 ? 2.294 83.873 5.186 1.00 21.94 ? 86 TRP A CD2 1 ATOM 425 N NE1 . TRP A 1 59 ? 2.549 83.174 7.299 1.00 26.25 ? 86 TRP A NE1 1 ATOM 426 C CE2 . TRP A 1 59 ? 3.180 83.248 6.086 1.00 23.38 ? 86 TRP A CE2 1 ATOM 427 C CE3 . TRP A 1 59 ? 2.707 84.075 3.865 1.00 23.25 ? 86 TRP A CE3 1 ATOM 428 C CZ2 . TRP A 1 59 ? 4.453 82.818 5.706 1.00 25.76 ? 86 TRP A CZ2 1 ATOM 429 C CZ3 . TRP A 1 59 ? 3.973 83.649 3.489 1.00 24.07 ? 86 TRP A CZ3 1 ATOM 430 C CH2 . TRP A 1 59 ? 4.832 83.031 4.408 1.00 24.42 ? 86 TRP A CH2 1 ATOM 431 N N . ASN A 1 60 ? -1.782 87.683 5.474 1.00 21.69 ? 87 ASN A N 1 ATOM 432 C CA . ASN A 1 60 ? -3.091 88.299 5.286 1.00 25.08 ? 87 ASN A CA 1 ATOM 433 C C . ASN A 1 60 ? -3.001 89.751 4.826 1.00 29.56 ? 87 ASN A C 1 ATOM 434 O O . ASN A 1 60 ? -3.729 90.609 5.327 1.00 24.99 ? 87 ASN A O 1 ATOM 435 C CB . ASN A 1 60 ? -3.908 88.234 6.580 1.00 22.85 ? 87 ASN A CB 1 ATOM 436 C CG . ASN A 1 60 ? -4.162 86.811 7.045 1.00 29.85 ? 87 ASN A CG 1 ATOM 437 O OD1 . ASN A 1 60 ? -4.219 85.881 6.242 1.00 32.53 ? 87 ASN A OD1 1 ATOM 438 N ND2 . ASN A 1 60 ? -4.317 86.638 8.349 1.00 31.18 ? 87 ASN A ND2 1 ATOM 439 N N . HIS A 1 61 ? -2.121 90.025 3.868 1.00 26.98 ? 88 HIS A N 1 ATOM 440 C CA . HIS A 1 61 ? -1.930 91.396 3.402 1.00 25.73 ? 88 HIS A CA 1 ATOM 441 C C . HIS A 1 61 ? -3.075 91.877 2.515 1.00 25.01 ? 88 HIS A C 1 ATOM 442 O O . HIS A 1 61 ? -3.238 93.076 2.315 1.00 23.62 ? 88 HIS A O 1 ATOM 443 C CB . HIS A 1 61 ? -0.580 91.560 2.689 1.00 21.77 ? 88 HIS A CB 1 ATOM 444 C CG . HIS A 1 61 ? -0.294 90.498 1.671 1.00 19.73 ? 88 HIS A CG 1 ATOM 445 N ND1 . HIS A 1 61 ? 0.408 89.352 1.969 1.00 17.70 ? 88 HIS A ND1 1 ATOM 446 C CD2 . HIS A 1 61 ? -0.597 90.421 0.352 1.00 16.76 ? 88 HIS A CD2 1 ATOM 447 C CE1 . HIS A 1 61 ? 0.518 88.607 0.882 1.00 19.58 ? 88 HIS A CE1 1 ATOM 448 N NE2 . HIS A 1 61 ? -0.085 89.233 -0.111 1.00 18.93 ? 88 HIS A NE2 1 ATOM 449 N N . CYS A 1 62 ? -3.856 90.940 1.981 1.00 23.04 ? 89 CYS A N 1 ATOM 450 C CA . CYS A 1 62 ? -5.051 91.278 1.204 1.00 22.21 ? 89 CYS A CA 1 ATOM 451 C C . CYS A 1 62 ? -6.282 90.552 1.759 1.00 23.44 ? 89 CYS A C 1 ATOM 452 O O . CYS A 1 62 ? -6.922 89.775 1.059 1.00 28.01 ? 89 CYS A O 1 ATOM 453 C CB . CYS A 1 62 ? -4.853 90.926 -0.278 1.00 17.24 ? 89 CYS A CB 1 ATOM 454 S SG . CYS A 1 62 ? -3.694 91.984 -1.185 1.00 25.84 ? 89 CYS A SG 1 ATOM 455 N N . GLY A 1 63 ? -6.606 90.801 3.022 1.00 26.90 ? 90 GLY A N 1 ATOM 456 C CA . GLY A 1 63 ? -7.648 90.044 3.696 1.00 26.17 ? 90 GLY A CA 1 ATOM 457 C C . GLY A 1 63 ? -7.106 88.695 4.140 1.00 31.77 ? 90 GLY A C 1 ATOM 458 O O . GLY A 1 63 ? -5.929 88.396 3.946 1.00 30.80 ? 90 GLY A O 1 ATOM 459 N N . GLU A 1 64 ? -7.957 87.870 4.736 1.00 34.24 ? 91 GLU A N 1 ATOM 460 C CA . GLU A 1 64 ? -7.499 86.595 5.270 1.00 35.76 ? 91 GLU A CA 1 ATOM 461 C C . GLU A 1 64 ? -7.157 85.592 4.167 1.00 31.75 ? 91 GLU A C 1 ATOM 462 O O . GLU A 1 64 ? -7.964 85.311 3.285 1.00 32.58 ? 91 GLU A O 1 ATOM 463 C CB . GLU A 1 64 ? -8.535 85.999 6.227 1.00 40.62 ? 91 GLU A CB 1 ATOM 464 C CG . GLU A 1 64 ? -8.002 84.829 7.042 1.00 55.02 ? 91 GLU A CG 1 ATOM 465 C CD . GLU A 1 64 ? -9.089 84.082 7.791 1.00 72.30 ? 91 GLU A CD 1 ATOM 466 O OE1 . GLU A 1 64 ? -10.177 84.660 8.010 1.00 78.30 ? 91 GLU A OE1 1 ATOM 467 O OE2 . GLU A 1 64 ? -8.856 82.909 8.155 1.00 77.09 ? 91 GLU A OE2 1 ATOM 468 N N . MET A 1 65 ? -5.945 85.059 4.224 1.00 30.80 ? 92 MET A N 1 ATOM 469 C CA . MET A 1 65 ? -5.541 83.984 3.331 1.00 30.09 ? 92 MET A CA 1 ATOM 470 C C . MET A 1 65 ? -6.292 82.700 3.698 1.00 28.70 ? 92 MET A C 1 ATOM 471 O O . MET A 1 65 ? -6.479 82.402 4.878 1.00 34.23 ? 92 MET A O 1 ATOM 472 C CB . MET A 1 65 ? -4.026 83.776 3.421 1.00 24.95 ? 92 MET A CB 1 ATOM 473 C CG . MET A 1 65 ? -3.500 82.600 2.622 1.00 24.50 ? 92 MET A CG 1 ATOM 474 S SD . MET A 1 65 ? -1.699 82.507 2.659 1.00 24.30 ? 92 MET A SD 1 ATOM 475 C CE . MET A 1 65 ? -1.253 83.841 1.551 1.00 16.28 ? 92 MET A CE 1 ATOM 476 N N . ALA A 1 66 ? -6.740 81.954 2.691 1.00 28.07 ? 93 ALA A N 1 ATOM 477 C CA . ALA A 1 66 ? -7.409 80.676 2.938 1.00 31.63 ? 93 ALA A CA 1 ATOM 478 C C . ALA A 1 66 ? -6.444 79.701 3.610 1.00 31.15 ? 93 ALA A C 1 ATOM 479 O O . ALA A 1 66 ? -5.267 79.651 3.260 1.00 28.13 ? 93 ALA A O 1 ATOM 480 C CB . ALA A 1 66 ? -7.948 80.084 1.638 1.00 26.53 ? 93 ALA A CB 1 ATOM 481 N N . PRO A 1 67 ? -6.941 78.933 4.591 1.00 30.00 ? 94 PRO A N 1 ATOM 482 C CA . PRO A 1 67 ? -6.153 77.911 5.288 1.00 29.59 ? 94 PRO A CA 1 ATOM 483 C C . PRO A 1 67 ? -5.395 76.978 4.337 1.00 33.12 ? 94 PRO A C 1 ATOM 484 O O . PRO A 1 67 ? -4.231 76.684 4.589 1.00 29.37 ? 94 PRO A O 1 ATOM 485 C CB . PRO A 1 67 ? -7.214 77.129 6.062 1.00 28.16 ? 94 PRO A CB 1 ATOM 486 C CG . PRO A 1 67 ? -8.277 78.125 6.328 1.00 30.37 ? 94 PRO A CG 1 ATOM 487 C CD . PRO A 1 67 ? -8.309 79.038 5.131 1.00 31.15 ? 94 PRO A CD 1 ATOM 488 N N . ALA A 1 68 ? -6.043 76.521 3.270 1.00 34.06 ? 95 ALA A N 1 ATOM 489 C CA . ALA A 1 68 ? -5.401 75.607 2.333 1.00 31.47 ? 95 ALA A CA 1 ATOM 490 C C . ALA A 1 68 ? -4.206 76.275 1.666 1.00 34.60 ? 95 ALA A C 1 ATOM 491 O O . ALA A 1 68 ? -3.200 75.622 1.368 1.00 29.01 ? 95 ALA A O 1 ATOM 492 C CB . ALA A 1 68 ? -6.394 75.115 1.288 1.00 32.18 ? 95 ALA A CB 1 ATOM 493 N N . CYS A 1 69 ? -4.320 77.582 1.439 1.00 30.53 ? 96 CYS A N 1 ATOM 494 C CA . CYS A 1 69 ? -3.227 78.347 0.856 1.00 28.92 ? 96 CYS A CA 1 ATOM 495 C C . CYS A 1 69 ? -2.112 78.550 1.871 1.00 28.55 ? 96 CYS A C 1 ATOM 496 O O . CYS A 1 69 ? -0.937 78.336 1.568 1.00 24.99 ? 96 CYS A O 1 ATOM 497 C CB . CYS A 1 69 ? -3.714 79.707 0.347 1.00 28.82 ? 96 CYS A CB 1 ATOM 498 S SG . CYS A 1 69 ? -2.428 80.668 -0.481 1.00 25.39 ? 96 CYS A SG 1 ATOM 499 N N . LYS A 1 70 ? -2.481 78.959 3.079 1.00 25.37 ? 97 LYS A N 1 ATOM 500 C CA . LYS A 1 70 ? -1.479 79.238 4.093 1.00 27.57 ? 97 LYS A CA 1 ATOM 501 C C . LYS A 1 70 ? -0.625 78.012 4.429 1.00 28.80 ? 97 LYS A C 1 ATOM 502 O O . LYS A 1 70 ? 0.556 78.154 4.735 1.00 29.42 ? 97 LYS A O 1 ATOM 503 C CB . LYS A 1 70 ? -2.096 79.822 5.366 1.00 28.47 ? 97 LYS A CB 1 ATOM 504 C CG . LYS A 1 70 ? -1.024 80.324 6.327 1.00 39.00 ? 97 LYS A CG 1 ATOM 505 C CD . LYS A 1 70 ? -1.556 80.663 7.707 1.00 46.50 ? 97 LYS A CD 1 ATOM 506 C CE . LYS A 1 70 ? -0.392 80.865 8.678 1.00 48.47 ? 97 LYS A CE 1 ATOM 507 N NZ . LYS A 1 70 ? -0.836 81.266 10.042 1.00 50.03 ? 97 LYS A NZ 1 ATOM 508 N N . ARG A 1 71 ? -1.226 76.821 4.376 1.00 29.87 ? 98 ARG A N 1 ATOM 509 C CA . ARG A 1 71 ? -0.509 75.575 4.662 1.00 29.03 ? 98 ARG A CA 1 ATOM 510 C C . ARG A 1 71 ? 0.739 75.418 3.805 1.00 28.32 ? 98 ARG A C 1 ATOM 511 O O . ARG A 1 71 ? 1.784 75.003 4.295 1.00 26.85 ? 98 ARG A O 1 ATOM 512 C CB . ARG A 1 71 ? -1.412 74.356 4.461 1.00 28.06 ? 98 ARG A CB 1 ATOM 513 C CG . ARG A 1 71 ? -2.148 73.924 5.716 1.00 41.53 ? 98 ARG A CG 1 ATOM 514 C CD . ARG A 1 71 ? -3.146 72.810 5.432 1.00 48.01 ? 98 ARG A CD 1 ATOM 515 N NE . ARG A 1 71 ? -4.508 73.245 5.725 1.00 55.41 ? 98 ARG A NE 1 ATOM 516 C CZ . ARG A 1 71 ? -5.552 73.021 4.938 1.00 55.12 ? 98 ARG A CZ 1 ATOM 517 N NH1 . ARG A 1 71 ? -5.402 72.355 3.800 1.00 60.38 ? 98 ARG A NH1 1 ATOM 518 N NH2 . ARG A 1 71 ? -6.747 73.462 5.291 1.00 50.57 ? 98 ARG A NH2 1 ATOM 519 N N . HIS A 1 72 ? 0.616 75.740 2.521 1.00 29.16 ? 99 HIS A N 1 ATOM 520 C CA . HIS A 1 72 ? 1.746 75.663 1.605 1.00 27.97 ? 99 HIS A CA 1 ATOM 521 C C . HIS A 1 72 ? 2.819 76.665 1.993 1.00 24.89 ? 99 HIS A C 1 ATOM 522 O O . HIS A 1 72 ? 4.011 76.378 1.893 1.00 26.88 ? 99 HIS A O 1 ATOM 523 C CB . HIS A 1 72 ? 1.294 75.911 0.166 1.00 29.65 ? 99 HIS A CB 1 ATOM 524 C CG . HIS A 1 72 ? 0.394 74.846 -0.374 1.00 31.88 ? 99 HIS A CG 1 ATOM 525 N ND1 . HIS A 1 72 ? 0.872 73.684 -0.943 1.00 31.47 ? 99 HIS A ND1 1 ATOM 526 C CD2 . HIS A 1 72 ? -0.957 74.762 -0.427 1.00 31.89 ? 99 HIS A CD2 1 ATOM 527 C CE1 . HIS A 1 72 ? -0.144 72.935 -1.328 1.00 33.98 ? 99 HIS A CE1 1 ATOM 528 N NE2 . HIS A 1 72 ? -1.265 73.565 -1.024 1.00 35.29 ? 99 HIS A NE2 1 ATOM 529 N N . PHE A 1 73 ? 2.396 77.844 2.438 1.00 23.97 ? 100 PHE A N 1 ATOM 530 C CA . PHE A 1 73 ? 3.350 78.868 2.851 1.00 26.54 ? 100 PHE A CA 1 ATOM 531 C C . PHE A 1 73 ? 4.083 78.486 4.134 1.00 27.86 ? 100 PHE A C 1 ATOM 532 O O . PHE A 1 73 ? 5.242 78.849 4.321 1.00 29.08 ? 100 PHE A O 1 ATOM 533 C CB . PHE A 1 73 ? 2.697 80.251 2.938 1.00 21.91 ? 100 PHE A CB 1 ATOM 534 C CG . PHE A 1 73 ? 2.549 80.915 1.604 1.00 23.42 ? 100 PHE A CG 1 ATOM 535 C CD1 . PHE A 1 73 ? 3.660 81.414 0.941 1.00 22.84 ? 100 PHE A CD1 1 ATOM 536 C CD2 . PHE A 1 73 ? 1.310 81.010 0.991 1.00 23.35 ? 100 PHE A CD2 1 ATOM 537 C CE1 . PHE A 1 73 ? 3.534 82.010 -0.298 1.00 22.31 ? 100 PHE A CE1 1 ATOM 538 C CE2 . PHE A 1 73 ? 1.180 81.603 -0.246 1.00 20.47 ? 100 PHE A CE2 1 ATOM 539 C CZ . PHE A 1 73 ? 2.293 82.107 -0.894 1.00 21.16 ? 100 PHE A CZ 1 ATOM 540 N N . ILE A 1 74 ? 3.417 77.726 4.995 1.00 26.13 ? 101 ILE A N 1 ATOM 541 C CA . ILE A 1 74 ? 4.081 77.134 6.154 1.00 26.25 ? 101 ILE A CA 1 ATOM 542 C C . ILE A 1 74 ? 5.123 76.093 5.730 1.00 25.23 ? 101 ILE A C 1 ATOM 543 O O . ILE A 1 74 ? 6.248 76.099 6.223 1.00 23.69 ? 101 ILE A O 1 ATOM 544 C CB . ILE A 1 74 ? 3.072 76.473 7.106 1.00 27.85 ? 101 ILE A CB 1 ATOM 545 C CG1 . ILE A 1 74 ? 2.116 77.528 7.664 1.00 30.41 ? 101 ILE A CG1 1 ATOM 546 C CG2 . ILE A 1 74 ? 3.799 75.760 8.237 1.00 27.91 ? 101 ILE A CG2 1 ATOM 547 C CD1 . ILE A 1 74 ? 2.819 78.653 8.391 1.00 27.94 ? 101 ILE A CD1 1 ATOM 548 N N . GLN A 1 75 ? 4.736 75.196 4.827 1.00 21.54 ? 102 GLN A N 1 ATOM 549 C CA . GLN A 1 75 ? 5.657 74.196 4.288 1.00 25.04 ? 102 GLN A CA 1 ATOM 550 C C . GLN A 1 75 ? 6.866 74.879 3.655 1.00 25.94 ? 102 GLN A C 1 ATOM 551 O O . GLN A 1 75 ? 8.008 74.468 3.868 1.00 26.35 ? 102 GLN A O 1 ATOM 552 C CB . GLN A 1 75 ? 4.952 73.329 3.243 1.00 24.53 ? 102 GLN A CB 1 ATOM 553 C CG . GLN A 1 75 ? 3.771 72.541 3.789 1.00 28.33 ? 102 GLN A CG 1 ATOM 554 C CD . GLN A 1 75 ? 3.052 71.765 2.717 1.00 35.05 ? 102 GLN A CD 1 ATOM 555 O OE1 . GLN A 1 75 ? 3.534 71.649 1.592 1.00 34.34 ? 102 GLN A OE1 1 ATOM 556 N NE2 . GLN A 1 75 ? 1.884 71.233 3.054 1.00 42.15 ? 102 GLN A NE2 1 ATOM 557 N N . ASP A 1 76 ? 6.578 75.920 2.878 1.00 21.28 ? 103 ASP A N 1 ATOM 558 C CA . ASP A 1 76 ? 7.560 76.751 2.184 1.00 23.71 ? 103 ASP A CA 1 ATOM 559 C C . ASP A 1 76 ? 8.523 77.387 3.192 1.00 25.10 ? 103 ASP A C 1 ATOM 560 O O . ASP A 1 76 ? 9.742 77.270 3.067 1.00 23.08 ? 103 ASP A O 1 ATOM 561 C CB . ASP A 1 76 ? 6.791 77.815 1.381 1.00 23.01 ? 103 ASP A CB 1 ATOM 562 C CG . ASP A 1 76 ? 7.682 78.878 0.758 1.00 25.93 ? 103 ASP A CG 1 ATOM 563 O OD1 . ASP A 1 76 ? 8.673 78.533 0.081 1.00 22.25 ? 103 ASP A OD1 1 ATOM 564 O OD2 . ASP A 1 76 ? 7.360 80.077 0.925 1.00 23.41 ? 103 ASP A OD2 1 ATOM 565 N N . THR A 1 77 ? 7.962 78.042 4.203 1.00 24.82 ? 104 THR A N 1 ATOM 566 C CA . THR A 1 77 ? 8.748 78.630 5.277 1.00 22.58 ? 104 THR A CA 1 ATOM 567 C C . THR A 1 77 ? 9.620 77.583 5.970 1.00 27.31 ? 104 THR A C 1 ATOM 568 O O . THR A 1 77 ? 10.803 77.814 6.221 1.00 28.20 ? 104 THR A O 1 ATOM 569 C CB . THR A 1 77 ? 7.835 79.300 6.325 1.00 21.44 ? 104 THR A CB 1 ATOM 570 O OG1 . THR A 1 77 ? 7.061 80.334 5.699 1.00 19.90 ? 104 THR A OG1 1 ATOM 571 C CG2 . THR A 1 77 ? 8.662 79.903 7.451 1.00 17.78 ? 104 THR A CG2 1 ATOM 572 N N . CYS A 1 78 ? 9.025 76.434 6.279 1.00 27.27 ? 105 CYS A N 1 ATOM 573 C CA . CYS A 1 78 ? 9.733 75.355 6.958 1.00 27.57 ? 105 CYS A CA 1 ATOM 574 C C . CYS A 1 78 ? 10.915 74.829 6.143 1.00 26.07 ? 105 CYS A C 1 ATOM 575 O O . CYS A 1 78 ? 12.018 74.699 6.665 1.00 26.13 ? 105 CYS A O 1 ATOM 576 C CB . CYS A 1 78 ? 8.772 74.220 7.319 1.00 31.44 ? 105 CYS A CB 1 ATOM 577 S SG . CYS A 1 78 ? 7.598 74.637 8.636 1.00 27.43 ? 105 CYS A SG 1 ATOM 578 N N . LEU A 1 79 ? 10.689 74.542 4.864 1.00 26.41 ? 106 LEU A N 1 ATOM 579 C CA . LEU A 1 79 ? 11.774 74.102 3.989 1.00 26.28 ? 106 LEU A CA 1 ATOM 580 C C . LEU A 1 79 ? 12.944 75.096 4.030 1.00 21.95 ? 106 LEU A C 1 ATOM 581 O O . LEU A 1 79 ? 14.080 74.726 4.342 1.00 20.33 ? 106 LEU A O 1 ATOM 582 C CB . LEU A 1 79 ? 11.274 73.925 2.551 1.00 22.59 ? 106 LEU A CB 1 ATOM 583 C CG . LEU A 1 79 ? 12.274 73.365 1.525 1.00 23.43 ? 106 LEU A CG 1 ATOM 584 C CD1 . LEU A 1 79 ? 12.629 71.908 1.812 1.00 20.22 ? 106 LEU A CD1 1 ATOM 585 C CD2 . LEU A 1 79 ? 11.737 73.508 0.104 1.00 23.06 ? 106 LEU A CD2 1 ATOM 586 N N . TYR A 1 80 ? 12.652 76.359 3.729 1.00 21.54 ? 107 TYR A N 1 ATOM 587 C CA . TYR A 1 80 ? 13.676 77.402 3.673 1.00 23.40 ? 107 TYR A CA 1 ATOM 588 C C . TYR A 1 80 ? 14.476 77.532 4.970 1.00 26.81 ? 107 TYR A C 1 ATOM 589 O O . TYR A 1 80 ? 15.703 77.656 4.944 1.00 23.54 ? 107 TYR A O 1 ATOM 590 C CB . TYR A 1 80 ? 13.060 78.756 3.297 1.00 17.68 ? 107 TYR A CB 1 ATOM 591 C CG . TYR A 1 80 ? 14.037 79.906 3.398 1.00 21.88 ? 107 TYR A CG 1 ATOM 592 C CD1 . TYR A 1 80 ? 14.928 80.184 2.362 1.00 20.71 ? 107 TYR A CD1 1 ATOM 593 C CD2 . TYR A 1 80 ? 14.088 80.700 4.539 1.00 19.48 ? 107 TYR A CD2 1 ATOM 594 C CE1 . TYR A 1 80 ? 15.836 81.227 2.460 1.00 19.16 ? 107 TYR A CE1 1 ATOM 595 C CE2 . TYR A 1 80 ? 14.986 81.740 4.643 1.00 19.45 ? 107 TYR A CE2 1 ATOM 596 C CZ . TYR A 1 80 ? 15.857 82.000 3.602 1.00 21.62 ? 107 TYR A CZ 1 ATOM 597 O OH . TYR A 1 80 ? 16.748 83.037 3.712 1.00 23.04 ? 107 TYR A OH 1 ATOM 598 N N . GLU A 1 81 ? 13.779 77.500 6.100 1.00 22.41 ? 108 GLU A N 1 ATOM 599 C CA . GLU A 1 81 ? 14.412 77.774 7.388 1.00 22.45 ? 108 GLU A CA 1 ATOM 600 C C . GLU A 1 81 ? 15.047 76.548 8.051 1.00 27.11 ? 108 GLU A C 1 ATOM 601 O O . GLU A 1 81 ? 15.930 76.692 8.892 1.00 21.22 ? 108 GLU A O 1 ATOM 602 C CB . GLU A 1 81 ? 13.407 78.451 8.340 1.00 22.52 ? 108 GLU A CB 1 ATOM 603 C CG . GLU A 1 81 ? 12.836 79.758 7.769 1.00 21.04 ? 108 GLU A CG 1 ATOM 604 C CD . GLU A 1 81 ? 11.884 80.490 8.702 1.00 19.58 ? 108 GLU A CD 1 ATOM 605 O OE1 . GLU A 1 81 ? 11.597 80.000 9.818 1.00 23.37 ? 108 GLU A OE1 1 ATOM 606 O OE2 . GLU A 1 81 ? 11.415 81.574 8.303 1.00 26.39 ? 108 GLU A OE2 1 ATOM 607 N N . CYS A 1 82 ? 14.611 75.349 7.663 1.00 26.78 ? 109 CYS A N 1 ATOM 608 C CA . CYS A 1 82 ? 14.987 74.136 8.389 1.00 28.03 ? 109 CYS A CA 1 ATOM 609 C C . CYS A 1 82 ? 15.739 73.091 7.570 1.00 24.89 ? 109 CYS A C 1 ATOM 610 O O . CYS A 1 82 ? 16.489 72.303 8.120 1.00 27.16 ? 109 CYS A O 1 ATOM 611 C CB . CYS A 1 82 ? 13.746 73.484 9.004 1.00 27.91 ? 109 CYS A CB 1 ATOM 612 S SG . CYS A 1 82 ? 12.890 74.540 10.165 1.00 28.70 ? 109 CYS A SG 1 ATOM 613 N N . SER A 1 83 ? 15.520 73.071 6.263 1.00 23.19 ? 110 SER A N 1 ATOM 614 C CA . SER A 1 83 ? 16.124 72.051 5.417 1.00 24.36 ? 110 SER A CA 1 ATOM 615 C C . SER A 1 83 ? 17.652 72.080 5.403 1.00 24.69 ? 110 SER A C 1 ATOM 616 O O . SER A 1 83 ? 18.246 73.117 5.119 1.00 25.01 ? 110 SER A O 1 ATOM 617 C CB . SER A 1 83 ? 15.629 72.201 3.990 1.00 26.35 ? 110 SER A CB 1 ATOM 618 O OG . SER A 1 83 ? 16.410 71.394 3.128 1.00 26.19 ? 110 SER A OG 1 ATOM 619 N N . PRO A 1 84 ? 18.289 70.929 5.699 1.00 24.22 ? 111 PRO A N 1 ATOM 620 C CA . PRO A 1 84 ? 19.741 70.752 5.584 1.00 22.07 ? 111 PRO A CA 1 ATOM 621 C C . PRO A 1 84 ? 20.128 70.175 4.216 1.00 25.60 ? 111 PRO A C 1 ATOM 622 O O . PRO A 1 84 ? 21.275 69.756 4.021 1.00 24.59 ? 111 PRO A O 1 ATOM 623 C CB . PRO A 1 84 ? 20.031 69.729 6.675 1.00 22.38 ? 111 PRO A CB 1 ATOM 624 C CG . PRO A 1 84 ? 18.817 68.841 6.649 1.00 21.55 ? 111 PRO A CG 1 ATOM 625 C CD . PRO A 1 84 ? 17.647 69.745 6.301 1.00 24.57 ? 111 PRO A CD 1 ATOM 626 N N . ASN A 1 85 ? 19.179 70.160 3.282 1.00 25.08 ? 112 ASN A N 1 ATOM 627 C CA . ASN A 1 85 ? 19.405 69.574 1.963 1.00 25.44 ? 112 ASN A CA 1 ATOM 628 C C . ASN A 1 85 ? 19.225 70.544 0.796 1.00 28.56 ? 112 ASN A C 1 ATOM 629 O O . ASN A 1 85 ? 18.771 70.142 -0.280 1.00 26.01 ? 112 ASN A O 1 ATOM 630 C CB . ASN A 1 85 ? 18.498 68.358 1.753 1.00 27.49 ? 112 ASN A CB 1 ATOM 631 C CG . ASN A 1 85 ? 18.614 67.342 2.874 1.00 30.84 ? 112 ASN A CG 1 ATOM 632 O OD1 . ASN A 1 85 ? 17.630 67.025 3.546 1.00 31.84 ? 112 ASN A OD1 1 ATOM 633 N ND2 . ASN A 1 85 ? 19.819 66.826 3.084 1.00 27.92 ? 112 ASN A ND2 1 ATOM 634 N N . LEU A 1 86 ? 19.587 71.808 1.005 1.00 23.87 ? 113 LEU A N 1 ATOM 635 C CA . LEU A 1 86 ? 19.539 72.812 -0.060 1.00 25.00 ? 113 LEU A CA 1 ATOM 636 C C . LEU A 1 86 ? 20.946 73.259 -0.498 1.00 24.20 ? 113 LEU A C 1 ATOM 637 O O . LEU A 1 86 ? 21.088 74.135 -1.347 1.00 25.74 ? 113 LEU A O 1 ATOM 638 C CB . LEU A 1 86 ? 18.702 74.029 0.375 1.00 24.44 ? 113 LEU A CB 1 ATOM 639 C CG . LEU A 1 86 ? 17.252 73.773 0.819 1.00 23.19 ? 113 LEU A CG 1 ATOM 640 C CD1 . LEU A 1 86 ? 16.551 75.071 1.263 1.00 20.09 ? 113 LEU A CD1 1 ATOM 641 C CD2 . LEU A 1 86 ? 16.449 73.074 -0.277 1.00 19.48 ? 113 LEU A CD2 1 ATOM 642 N N . GLY A 1 87 ? 21.976 72.644 0.079 1.00 20.21 ? 114 GLY A N 1 ATOM 643 C CA . GLY A 1 87 ? 23.361 72.977 -0.232 1.00 21.06 ? 114 GLY A CA 1 ATOM 644 C C . GLY A 1 87 ? 23.690 73.294 -1.688 1.00 24.58 ? 114 GLY A C 1 ATOM 645 O O . GLY A 1 87 ? 24.306 74.318 -1.977 1.00 28.41 ? 114 GLY A O 1 ATOM 646 N N . PRO A 1 88 ? 23.291 72.415 -2.619 1.00 24.43 ? 115 PRO A N 1 ATOM 647 C CA . PRO A 1 88 ? 23.633 72.623 -4.031 1.00 24.05 ? 115 PRO A CA 1 ATOM 648 C C . PRO A 1 88 ? 23.084 73.922 -4.623 1.00 26.15 ? 115 PRO A C 1 ATOM 649 O O . PRO A 1 88 ? 23.553 74.335 -5.687 1.00 23.83 ? 115 PRO A O 1 ATOM 650 C CB . PRO A 1 88 ? 23.000 71.407 -4.725 1.00 23.08 ? 115 PRO A CB 1 ATOM 651 C CG . PRO A 1 88 ? 22.999 70.348 -3.672 1.00 23.98 ? 115 PRO A CG 1 ATOM 652 C CD . PRO A 1 88 ? 22.660 71.102 -2.397 1.00 25.02 ? 115 PRO A CD 1 ATOM 653 N N . TRP A 1 89 ? 22.127 74.559 -3.946 1.00 22.18 ? 116 TRP A N 1 ATOM 654 C CA . TRP A 1 89 ? 21.504 75.771 -4.477 1.00 23.30 ? 116 TRP A CA 1 ATOM 655 C C . TRP A 1 89 ? 21.807 77.013 -3.643 1.00 26.03 ? 116 TRP A C 1 ATOM 656 O O . TRP A 1 89 ? 21.408 78.115 -4.003 1.00 23.77 ? 116 TRP A O 1 ATOM 657 C CB . TRP A 1 89 ? 19.993 75.567 -4.678 1.00 20.83 ? 116 TRP A CB 1 ATOM 658 C CG . TRP A 1 89 ? 19.730 74.342 -5.498 1.00 22.21 ? 116 TRP A CG 1 ATOM 659 C CD1 . TRP A 1 89 ? 19.758 74.245 -6.862 1.00 19.92 ? 116 TRP A CD1 1 ATOM 660 C CD2 . TRP A 1 89 ? 19.452 73.022 -5.007 1.00 21.70 ? 116 TRP A CD2 1 ATOM 661 N NE1 . TRP A 1 89 ? 19.503 72.953 -7.249 1.00 23.61 ? 116 TRP A NE1 1 ATOM 662 C CE2 . TRP A 1 89 ? 19.315 72.181 -6.129 1.00 24.72 ? 116 TRP A CE2 1 ATOM 663 C CE3 . TRP A 1 89 ? 19.308 72.471 -3.729 1.00 20.81 ? 116 TRP A CE3 1 ATOM 664 C CZ2 . TRP A 1 89 ? 19.042 70.817 -6.011 1.00 23.49 ? 116 TRP A CZ2 1 ATOM 665 C CZ3 . TRP A 1 89 ? 19.031 71.119 -3.614 1.00 22.60 ? 116 TRP A CZ3 1 ATOM 666 C CH2 . TRP A 1 89 ? 18.904 70.308 -4.749 1.00 23.42 ? 116 TRP A CH2 1 ATOM 667 N N . ILE A 1 90 ? 22.537 76.829 -2.545 1.00 24.91 ? 117 ILE A N 1 ATOM 668 C CA . ILE A 1 90 ? 22.920 77.943 -1.679 1.00 23.77 ? 117 ILE A CA 1 ATOM 669 C C . ILE A 1 90 ? 23.909 78.880 -2.373 1.00 27.12 ? 117 ILE A C 1 ATOM 670 O O . ILE A 1 90 ? 24.899 78.433 -2.960 1.00 24.74 ? 117 ILE A O 1 ATOM 671 C CB . ILE A 1 90 ? 23.521 77.447 -0.348 1.00 27.06 ? 117 ILE A CB 1 ATOM 672 C CG1 . ILE A 1 90 ? 22.457 76.717 0.479 1.00 23.06 ? 117 ILE A CG1 1 ATOM 673 C CG2 . ILE A 1 90 ? 24.117 78.604 0.436 1.00 27.50 ? 117 ILE A CG2 1 ATOM 674 C CD1 . ILE A 1 90 ? 22.986 76.117 1.769 1.00 23.34 ? 117 ILE A CD1 1 ATOM 675 N N . GLN A 1 91 ? 23.631 80.182 -2.312 1.00 26.63 ? 118 GLN A N 1 ATOM 676 C CA . GLN A 1 91 ? 24.488 81.179 -2.952 1.00 28.38 ? 118 GLN A CA 1 ATOM 677 C C . GLN A 1 91 ? 25.394 81.875 -1.942 1.00 28.45 ? 118 GLN A C 1 ATOM 678 O O . GLN A 1 91 ? 25.125 81.862 -0.743 1.00 31.77 ? 118 GLN A O 1 ATOM 679 C CB . GLN A 1 91 ? 23.643 82.201 -3.712 1.00 24.33 ? 118 GLN A CB 1 ATOM 680 C CG . GLN A 1 91 ? 22.741 81.566 -4.759 1.00 24.94 ? 118 GLN A CG 1 ATOM 681 C CD . GLN A 1 91 ? 23.529 80.852 -5.837 1.00 25.74 ? 118 GLN A CD 1 ATOM 682 O OE1 . GLN A 1 91 ? 24.378 81.450 -6.488 1.00 31.38 ? 118 GLN A OE1 1 ATOM 683 N NE2 . GLN A 1 91 ? 23.264 79.565 -6.017 1.00 24.14 ? 118 GLN A NE2 1 ATOM 684 N N . GLN A 1 92 ? 26.470 82.477 -2.435 1.00 29.77 ? 119 GLN A N 1 ATOM 685 C CA . GLN A 1 92 ? 27.436 83.151 -1.573 1.00 36.74 ? 119 GLN A CA 1 ATOM 686 C C . GLN A 1 92 ? 26.880 84.431 -0.943 1.00 35.92 ? 119 GLN A C 1 ATOM 687 O O . GLN A 1 92 ? 27.104 84.688 0.239 1.00 34.78 ? 119 GLN A O 1 ATOM 688 C CB . GLN A 1 92 ? 28.724 83.460 -2.345 1.00 46.27 ? 119 GLN A CB 1 ATOM 689 C CG . GLN A 1 92 ? 29.781 84.184 -1.518 1.00 60.95 ? 119 GLN A CG 1 ATOM 690 C CD . GLN A 1 92 ? 30.256 83.369 -0.325 1.00 71.29 ? 119 GLN A CD 1 ATOM 691 O OE1 . GLN A 1 92 ? 30.326 82.139 -0.382 1.00 73.71 ? 119 GLN A OE1 1 ATOM 692 N NE2 . GLN A 1 92 ? 30.584 84.055 0.767 1.00 73.57 ? 119 GLN A NE2 1 ATOM 693 N N . VAL A 1 93 ? 26.162 85.226 -1.733 1.00 33.90 ? 120 VAL A N 1 ATOM 694 C CA . VAL A 1 93 ? 25.592 86.488 -1.250 1.00 33.67 ? 120 VAL A CA 1 ATOM 695 C C . VAL A 1 93 ? 24.114 86.335 -0.882 1.00 27.13 ? 120 VAL A C 1 ATOM 696 O O . VAL A 1 93 ? 23.326 85.795 -1.654 1.00 26.00 ? 120 VAL A O 1 ATOM 697 C CB . VAL A 1 93 ? 25.760 87.626 -2.285 1.00 31.62 ? 120 VAL A CB 1 ATOM 698 C CG1 . VAL A 1 93 ? 25.047 88.893 -1.820 1.00 27.44 ? 120 VAL A CG1 1 ATOM 699 C CG2 . VAL A 1 93 ? 27.243 87.901 -2.546 1.00 28.84 ? 120 VAL A CG2 1 ATOM 700 N N . ASP A 1 94 ? 23.746 86.801 0.306 1.00 29.71 ? 121 ASP A N 1 ATOM 701 C CA . ASP A 1 94 ? 22.381 86.631 0.799 1.00 28.33 ? 121 ASP A CA 1 ATOM 702 C C . ASP A 1 94 ? 21.957 87.809 1.664 1.00 26.71 ? 121 ASP A C 1 ATOM 703 O O . ASP A 1 94 ? 21.093 87.676 2.533 1.00 27.29 ? 121 ASP A O 1 ATOM 704 C CB . ASP A 1 94 ? 22.262 85.324 1.593 1.00 24.81 ? 121 ASP A CB 1 ATOM 705 C CG . ASP A 1 94 ? 23.310 85.208 2.689 1.00 29.84 ? 121 ASP A CG 1 ATOM 706 O OD1 . ASP A 1 94 ? 23.617 86.234 3.329 1.00 32.59 ? 121 ASP A OD1 1 ATOM 707 O OD2 . ASP A 1 94 ? 23.837 84.095 2.907 1.00 23.64 ? 121 ASP A OD2 1 ATOM 708 N N . GLN A 1 95 ? 22.570 88.964 1.419 1.00 26.56 ? 122 GLN A N 1 ATOM 709 C CA . GLN A 1 95 ? 22.367 90.129 2.271 1.00 22.27 ? 122 GLN A CA 1 ATOM 710 C C . GLN A 1 95 ? 20.916 90.592 2.334 1.00 23.45 ? 122 GLN A C 1 ATOM 711 O O . GLN A 1 95 ? 20.509 91.221 3.317 1.00 24.26 ? 122 GLN A O 1 ATOM 712 C CB . GLN A 1 95 ? 23.289 91.286 1.852 1.00 29.09 ? 122 GLN A CB 1 ATOM 713 C CG . GLN A 1 95 ? 23.123 91.753 0.411 1.00 30.49 ? 122 GLN A CG 1 ATOM 714 C CD . GLN A 1 95 ? 24.106 92.850 0.046 1.00 39.94 ? 122 GLN A CD 1 ATOM 715 O OE1 . GLN A 1 95 ? 25.211 92.910 0.583 1.00 42.55 ? 122 GLN A OE1 1 ATOM 716 N NE2 . GLN A 1 95 ? 23.703 93.733 -0.862 1.00 41.77 ? 122 GLN A NE2 1 ATOM 717 N N . SER A 1 96 ? 20.132 90.282 1.300 1.00 23.81 ? 123 SER A N 1 ATOM 718 C CA . SER A 1 96 ? 18.727 90.694 1.295 1.00 24.20 ? 123 SER A CA 1 ATOM 719 C C . SER A 1 96 ? 17.798 89.651 1.907 1.00 23.69 ? 123 SER A C 1 ATOM 720 O O . SER A 1 96 ? 16.602 89.887 2.027 1.00 28.40 ? 123 SER A O 1 ATOM 721 C CB . SER A 1 96 ? 18.251 91.101 -0.109 1.00 22.56 ? 123 SER A CB 1 ATOM 722 O OG . SER A 1 96 ? 18.070 89.977 -0.953 1.00 25.99 ? 123 SER A OG 1 ATOM 723 N N . TRP A 1 97 ? 18.356 88.512 2.309 1.00 27.09 ? 124 TRP A N 1 ATOM 724 C CA . TRP A 1 97 ? 17.565 87.402 2.848 1.00 22.21 ? 124 TRP A CA 1 ATOM 725 C C . TRP A 1 97 ? 17.760 87.248 4.349 1.00 23.46 ? 124 TRP A C 1 ATOM 726 O O . TRP A 1 97 ? 18.812 87.584 4.880 1.00 24.94 ? 124 TRP A O 1 ATOM 727 C CB . TRP A 1 97 ? 17.905 86.093 2.117 1.00 20.69 ? 124 TRP A CB 1 ATOM 728 C CG . TRP A 1 97 ? 17.531 86.154 0.669 1.00 21.04 ? 124 TRP A CG 1 ATOM 729 C CD1 . TRP A 1 97 ? 18.260 86.711 -0.345 1.00 22.61 ? 124 TRP A CD1 1 ATOM 730 C CD2 . TRP A 1 97 ? 16.314 85.682 0.077 1.00 21.75 ? 124 TRP A CD2 1 ATOM 731 N NE1 . TRP A 1 97 ? 17.576 86.606 -1.532 1.00 20.90 ? 124 TRP A NE1 1 ATOM 732 C CE2 . TRP A 1 97 ? 16.378 85.979 -1.301 1.00 21.60 ? 124 TRP A CE2 1 ATOM 733 C CE3 . TRP A 1 97 ? 15.173 85.039 0.578 1.00 21.71 ? 124 TRP A CE3 1 ATOM 734 C CZ2 . TRP A 1 97 ? 15.350 85.648 -2.185 1.00 24.03 ? 124 TRP A CZ2 1 ATOM 735 C CZ3 . TRP A 1 97 ? 14.154 84.708 -0.300 1.00 19.31 ? 124 TRP A CZ3 1 ATOM 736 C CH2 . TRP A 1 97 ? 14.249 85.013 -1.666 1.00 25.33 ? 124 TRP A CH2 1 ATOM 737 N N . ARG A 1 98 ? 16.734 86.753 5.035 1.00 25.72 ? 125 ARG A N 1 ATOM 738 C CA . ARG A 1 98 ? 16.803 86.591 6.484 1.00 23.01 ? 125 ARG A CA 1 ATOM 739 C C . ARG A 1 98 ? 17.805 85.513 6.884 1.00 21.77 ? 125 ARG A C 1 ATOM 740 O O . ARG A 1 98 ? 18.497 85.642 7.892 1.00 21.89 ? 125 ARG A O 1 ATOM 741 C CB . ARG A 1 98 ? 15.417 86.318 7.082 1.00 24.83 ? 125 ARG A CB 1 ATOM 742 C CG . ARG A 1 98 ? 14.762 85.006 6.666 1.00 19.37 ? 125 ARG A CG 1 ATOM 743 C CD . ARG A 1 98 ? 13.265 85.061 6.995 1.00 21.56 ? 125 ARG A CD 1 ATOM 744 N NE . ARG A 1 98 ? 12.551 83.813 6.717 1.00 18.83 ? 125 ARG A NE 1 ATOM 745 C CZ . ARG A 1 98 ? 12.051 83.492 5.530 1.00 20.22 ? 125 ARG A CZ 1 ATOM 746 N NH1 . ARG A 1 98 ? 12.205 84.317 4.502 1.00 18.98 ? 125 ARG A NH1 1 ATOM 747 N NH2 . ARG A 1 98 ? 11.402 82.347 5.365 1.00 20.37 ? 125 ARG A NH2 1 ATOM 748 N N . LYS A 1 99 ? 17.884 84.451 6.091 1.00 18.99 ? 126 LYS A N 1 ATOM 749 C CA . LYS A 1 99 ? 18.910 83.438 6.296 1.00 25.28 ? 126 LYS A CA 1 ATOM 750 C C . LYS A 1 99 ? 19.669 83.242 4.989 1.00 24.33 ? 126 LYS A C 1 ATOM 751 O O . LYS A 1 99 ? 20.199 84.199 4.434 1.00 23.52 ? 126 LYS A O 1 ATOM 752 C CB . LYS A 1 99 ? 18.312 82.122 6.817 1.00 22.49 ? 126 LYS A CB 1 ATOM 753 C CG . LYS A 1 99 ? 17.532 82.275 8.125 1.00 21.19 ? 126 LYS A CG 1 ATOM 754 C CD . LYS A 1 99 ? 17.024 80.940 8.650 1.00 25.91 ? 126 LYS A CD 1 ATOM 755 C CE . LYS A 1 99 ? 18.167 80.095 9.191 1.00 30.69 ? 126 LYS A CE 1 ATOM 756 N NZ . LYS A 1 99 ? 17.687 78.786 9.703 1.00 28.73 ? 126 LYS A NZ 1 ATOM 757 N N . GLU A 1 100 ? 19.705 82.012 4.491 1.00 22.67 ? 127 GLU A N 1 ATOM 758 C CA . GLU A 1 100 ? 20.430 81.711 3.264 1.00 23.05 ? 127 GLU A CA 1 ATOM 759 C C . GLU A 1 100 ? 19.725 82.259 2.027 1.00 27.41 ? 127 GLU A C 1 ATOM 760 O O . GLU A 1 100 ? 18.542 82.597 2.066 1.00 28.13 ? 127 GLU A O 1 ATOM 761 C CB . GLU A 1 100 ? 20.629 80.197 3.117 1.00 21.61 ? 127 GLU A CB 1 ATOM 762 C CG . GLU A 1 100 ? 19.440 79.462 2.496 1.00 21.75 ? 127 GLU A CG 1 ATOM 763 C CD . GLU A 1 100 ? 18.388 79.036 3.511 1.00 22.19 ? 127 GLU A CD 1 ATOM 764 O OE1 . GLU A 1 100 ? 18.428 79.509 4.666 1.00 20.67 ? 127 GLU A OE1 1 ATOM 765 O OE2 . GLU A 1 100 ? 17.518 78.220 3.147 1.00 22.20 ? 127 GLU A OE2 1 ATOM 766 N N . ARG A 1 101 ? 20.471 82.357 0.934 1.00 20.07 ? 128 ARG A N 1 ATOM 767 C CA . ARG A 1 101 ? 19.891 82.604 -0.375 1.00 24.97 ? 128 ARG A CA 1 ATOM 768 C C . ARG A 1 101 ? 20.059 81.344 -1.221 1.00 25.94 ? 128 ARG A C 1 ATOM 769 O O . ARG A 1 101 ? 21.173 80.858 -1.407 1.00 25.98 ? 128 ARG A O 1 ATOM 770 C CB . ARG A 1 101 ? 20.560 83.804 -1.049 1.00 26.79 ? 128 ARG A CB 1 ATOM 771 C CG . ARG A 1 101 ? 20.417 83.869 -2.570 1.00 31.16 ? 128 ARG A CG 1 ATOM 772 C CD . ARG A 1 101 ? 18.966 83.857 -3.031 1.00 40.14 ? 128 ARG A CD 1 ATOM 773 N NE . ARG A 1 101 ? 18.792 84.516 -4.329 1.00 43.79 ? 128 ARG A NE 1 ATOM 774 C CZ . ARG A 1 101 ? 17.687 84.448 -5.073 1.00 41.10 ? 128 ARG A CZ 1 ATOM 775 N NH1 . ARG A 1 101 ? 16.637 83.731 -4.671 1.00 29.18 ? 128 ARG A NH1 1 ATOM 776 N NH2 . ARG A 1 101 ? 17.631 85.094 -6.234 1.00 37.86 ? 128 ARG A NH2 1 ATOM 777 N N . VAL A 1 102 ? 18.947 80.800 -1.699 1.00 20.16 ? 129 VAL A N 1 ATOM 778 C CA . VAL A 1 102 ? 18.992 79.666 -2.604 1.00 22.55 ? 129 VAL A CA 1 ATOM 779 C C . VAL A 1 102 ? 18.490 80.102 -3.975 1.00 23.39 ? 129 VAL A C 1 ATOM 780 O O . VAL A 1 102 ? 17.668 81.008 -4.085 1.00 23.70 ? 129 VAL A O 1 ATOM 781 C CB . VAL A 1 102 ? 18.168 78.451 -2.080 1.00 29.07 ? 129 VAL A CB 1 ATOM 782 C CG1 . VAL A 1 102 ? 18.856 77.801 -0.876 1.00 21.02 ? 129 VAL A CG1 1 ATOM 783 C CG2 . VAL A 1 102 ? 16.722 78.854 -1.758 1.00 20.87 ? 129 VAL A CG2 1 ATOM 784 N N . LEU A 1 103 ? 18.983 79.454 -5.020 1.00 25.80 ? 130 LEU A N 1 ATOM 785 C CA . LEU A 1 103 ? 18.636 79.839 -6.377 1.00 24.98 ? 130 LEU A CA 1 ATOM 786 C C . LEU A 1 103 ? 18.290 78.611 -7.203 1.00 25.94 ? 130 LEU A C 1 ATOM 787 O O . LEU A 1 103 ? 19.091 77.685 -7.318 1.00 26.99 ? 130 LEU A O 1 ATOM 788 C CB . LEU A 1 103 ? 19.798 80.605 -7.021 1.00 27.97 ? 130 LEU A CB 1 ATOM 789 C CG . LEU A 1 103 ? 19.680 81.094 -8.468 1.00 29.76 ? 130 LEU A CG 1 ATOM 790 C CD1 . LEU A 1 103 ? 18.521 82.068 -8.621 1.00 29.48 ? 130 LEU A CD1 1 ATOM 791 C CD2 . LEU A 1 103 ? 20.993 81.746 -8.918 1.00 29.15 ? 130 LEU A CD2 1 ATOM 792 N N . ASN A 1 104 ? 17.082 78.606 -7.757 1.00 24.45 ? 131 ASN A N 1 ATOM 793 C CA . ASN A 1 104 ? 16.654 77.567 -8.686 1.00 26.04 ? 131 ASN A CA 1 ATOM 794 C C . ASN A 1 104 ? 16.507 76.175 -8.082 1.00 25.01 ? 131 ASN A C 1 ATOM 795 O O . ASN A 1 104 ? 16.766 75.175 -8.746 1.00 28.09 ? 131 ASN A O 1 ATOM 796 C CB . ASN A 1 104 ? 17.572 77.542 -9.911 1.00 27.09 ? 131 ASN A CB 1 ATOM 797 C CG . ASN A 1 104 ? 17.440 78.800 -10.753 1.00 31.81 ? 131 ASN A CG 1 ATOM 798 O OD1 . ASN A 1 104 ? 16.372 79.417 -10.808 1.00 34.01 ? 131 ASN A OD1 1 ATOM 799 N ND2 . ASN A 1 104 ? 18.523 79.194 -11.398 1.00 33.62 ? 131 ASN A ND2 1 ATOM 800 N N . VAL A 1 105 ? 16.076 76.118 -6.827 1.00 26.03 ? 132 VAL A N 1 ATOM 801 C CA . VAL A 1 105 ? 15.743 74.849 -6.189 1.00 28.02 ? 132 VAL A CA 1 ATOM 802 C C . VAL A 1 105 ? 14.670 74.120 -6.998 1.00 29.39 ? 132 VAL A C 1 ATOM 803 O O . VAL A 1 105 ? 13.594 74.667 -7.240 1.00 30.97 ? 132 VAL A O 1 ATOM 804 C CB . VAL A 1 105 ? 15.238 75.059 -4.749 1.00 26.32 ? 132 VAL A CB 1 ATOM 805 C CG1 . VAL A 1 105 ? 14.716 73.745 -4.169 1.00 24.88 ? 132 VAL A CG1 1 ATOM 806 C CG2 . VAL A 1 105 ? 16.346 75.651 -3.875 1.00 22.37 ? 132 VAL A CG2 1 ATOM 807 N N . PRO A 1 106 ? 14.965 72.880 -7.425 1.00 30.27 ? 133 PRO A N 1 ATOM 808 C CA . PRO A 1 106 ? 14.056 72.127 -8.297 1.00 28.18 ? 133 PRO A CA 1 ATOM 809 C C . PRO A 1 106 ? 12.823 71.596 -7.564 1.00 29.97 ? 133 PRO A C 1 ATOM 810 O O . PRO A 1 106 ? 12.722 70.409 -7.271 1.00 34.51 ? 133 PRO A O 1 ATOM 811 C CB . PRO A 1 106 ? 14.938 70.986 -8.813 1.00 31.50 ? 133 PRO A CB 1 ATOM 812 C CG . PRO A 1 106 ? 15.966 70.788 -7.751 1.00 30.18 ? 133 PRO A CG 1 ATOM 813 C CD . PRO A 1 106 ? 16.221 72.151 -7.166 1.00 31.24 ? 133 PRO A CD 1 ATOM 814 N N . LEU A 1 107 ? 11.885 72.491 -7.280 1.00 29.75 ? 134 LEU A N 1 ATOM 815 C CA . LEU A 1 107 ? 10.643 72.127 -6.616 1.00 30.19 ? 134 LEU A CA 1 ATOM 816 C C . LEU A 1 107 ? 9.886 71.087 -7.443 1.00 32.80 ? 134 LEU A C 1 ATOM 817 O O . LEU A 1 107 ? 9.802 71.200 -8.669 1.00 30.37 ? 134 LEU A O 1 ATOM 818 C CB . LEU A 1 107 ? 9.782 73.374 -6.415 1.00 24.57 ? 134 LEU A CB 1 ATOM 819 C CG . LEU A 1 107 ? 8.552 73.238 -5.521 1.00 29.46 ? 134 LEU A CG 1 ATOM 820 C CD1 . LEU A 1 107 ? 8.949 72.685 -4.158 1.00 31.41 ? 134 LEU A CD1 1 ATOM 821 C CD2 . LEU A 1 107 ? 7.838 74.585 -5.386 1.00 29.46 ? 134 LEU A CD2 1 ATOM 822 N N . CYS A 1 108 ? 9.343 70.072 -6.779 1.00 28.26 ? 135 CYS A N 1 ATOM 823 C CA . CYS A 1 108 ? 8.610 69.025 -7.491 1.00 32.59 ? 135 CYS A CA 1 ATOM 824 C C . CYS A 1 108 ? 7.371 69.593 -8.181 1.00 31.53 ? 135 CYS A C 1 ATOM 825 O O . CYS A 1 108 ? 6.743 70.526 -7.681 1.00 29.62 ? 135 CYS A O 1 ATOM 826 C CB . CYS A 1 108 ? 8.220 67.880 -6.552 1.00 32.18 ? 135 CYS A CB 1 ATOM 827 S SG . CYS A 1 108 ? 9.599 66.856 -5.976 1.00 32.64 ? 135 CYS A SG 1 ATOM 828 N N . LYS A 1 109 ? 7.034 69.020 -9.332 1.00 35.28 ? 136 LYS A N 1 ATOM 829 C CA . LYS A 1 109 ? 5.886 69.452 -10.127 1.00 38.29 ? 136 LYS A CA 1 ATOM 830 C C . LYS A 1 109 ? 4.602 69.587 -9.297 1.00 39.28 ? 136 LYS A C 1 ATOM 831 O O . LYS A 1 109 ? 3.910 70.604 -9.376 1.00 39.99 ? 136 LYS A O 1 ATOM 832 C CB . LYS A 1 109 ? 5.670 68.467 -11.273 1.00 42.71 ? 136 LYS A CB 1 ATOM 833 C CG . LYS A 1 109 ? 4.736 68.931 -12.369 1.00 50.16 ? 136 LYS A CG 1 ATOM 834 C CD . LYS A 1 109 ? 4.475 67.784 -13.342 1.00 61.08 ? 136 LYS A CD 1 ATOM 835 C CE . LYS A 1 109 ? 3.718 68.241 -14.576 1.00 70.08 ? 136 LYS A CE 1 ATOM 836 N NZ . LYS A 1 109 ? 4.586 69.029 -15.494 1.00 76.45 ? 136 LYS A NZ 1 ATOM 837 N N . GLU A 1 110 ? 4.298 68.564 -8.500 1.00 36.59 ? 137 GLU A N 1 ATOM 838 C CA . GLU A 1 110 ? 3.064 68.526 -7.713 1.00 36.87 ? 137 GLU A CA 1 ATOM 839 C C . GLU A 1 110 ? 3.017 69.592 -6.632 1.00 34.93 ? 137 GLU A C 1 ATOM 840 O O . GLU A 1 110 ? 1.988 70.237 -6.438 1.00 34.52 ? 137 GLU A O 1 ATOM 841 C CB . GLU A 1 110 ? 2.870 67.158 -7.055 1.00 41.39 ? 137 GLU A CB 1 ATOM 842 C CG . GLU A 1 110 ? 2.862 66.004 -8.019 1.00 53.33 ? 137 GLU A CG 1 ATOM 843 C CD . GLU A 1 110 ? 4.246 65.682 -8.535 1.00 60.57 ? 137 GLU A CD 1 ATOM 844 O OE1 . GLU A 1 110 ? 4.355 65.293 -9.716 1.00 68.07 ? 137 GLU A OE1 1 ATOM 845 O OE2 . GLU A 1 110 ? 5.219 65.822 -7.762 1.00 52.71 ? 137 GLU A OE2 1 ATOM 846 N N . ASP A 1 111 ? 4.121 69.744 -5.907 1.00 30.86 ? 138 ASP A N 1 ATOM 847 C CA . ASP A 1 111 ? 4.204 70.733 -4.841 1.00 34.71 ? 138 ASP A CA 1 ATOM 848 C C . ASP A 1 111 ? 3.788 72.087 -5.387 1.00 33.05 ? 138 ASP A C 1 ATOM 849 O O . ASP A 1 111 ? 2.958 72.771 -4.801 1.00 36.38 ? 138 ASP A O 1 ATOM 850 C CB . ASP A 1 111 ? 5.621 70.804 -4.268 1.00 30.90 ? 138 ASP A CB 1 ATOM 851 C CG . ASP A 1 111 ? 6.010 69.542 -3.511 1.00 32.08 ? 138 ASP A CG 1 ATOM 852 O OD1 . ASP A 1 111 ? 6.209 69.623 -2.280 1.00 30.67 ? 138 ASP A OD1 1 ATOM 853 O OD2 . ASP A 1 111 ? 6.109 68.472 -4.144 1.00 28.54 ? 138 ASP A OD2 1 ATOM 854 N N . CYS A 1 112 ? 4.350 72.443 -6.537 1.00 31.84 ? 139 CYS A N 1 ATOM 855 C CA . CYS A 1 112 ? 4.064 73.715 -7.186 1.00 30.35 ? 139 CYS A CA 1 ATOM 856 C C . CYS A 1 112 ? 2.620 73.820 -7.696 1.00 34.64 ? 139 CYS A C 1 ATOM 857 O O . CYS A 1 112 ? 1.932 74.811 -7.439 1.00 34.47 ? 139 CYS A O 1 ATOM 858 C CB . CYS A 1 112 ? 5.051 73.952 -8.330 1.00 28.98 ? 139 CYS A CB 1 ATOM 859 S SG . CYS A 1 112 ? 4.802 75.497 -9.210 1.00 37.22 ? 139 CYS A SG 1 ATOM 860 N N . GLU A 1 113 ? 2.160 72.800 -8.413 1.00 32.25 ? 140 GLU A N 1 ATOM 861 C CA . GLU A 1 113 ? 0.808 72.829 -8.965 1.00 35.97 ? 140 GLU A CA 1 ATOM 862 C C . GLU A 1 113 ? -0.273 72.895 -7.881 1.00 37.91 ? 140 GLU A C 1 ATOM 863 O O . GLU A 1 113 ? -1.224 73.674 -7.990 1.00 28.05 ? 140 GLU A O 1 ATOM 864 C CB . GLU A 1 113 ? 0.583 71.653 -9.919 1.00 36.98 ? 140 GLU A CB 1 ATOM 865 C CG . GLU A 1 113 ? 1.409 71.775 -11.193 1.00 49.87 ? 140 GLU A CG 1 ATOM 866 C CD . GLU A 1 113 ? 1.241 70.601 -12.143 1.00 62.14 ? 140 GLU A CD 1 ATOM 867 O OE1 . GLU A 1 113 ? 0.691 69.555 -11.731 1.00 68.25 ? 140 GLU A OE1 1 ATOM 868 O OE2 . GLU A 1 113 ? 1.670 70.730 -13.310 1.00 63.09 ? 140 GLU A OE2 1 ATOM 869 N N . GLN A 1 114 ? -0.111 72.093 -6.832 1.00 34.56 ? 141 GLN A N 1 ATOM 870 C CA . GLN A 1 114 ? -1.068 72.057 -5.733 1.00 34.88 ? 141 GLN A CA 1 ATOM 871 C C . GLN A 1 114 ? -1.062 73.379 -4.961 1.00 33.68 ? 141 GLN A C 1 ATOM 872 O O . GLN A 1 114 ? -2.101 73.862 -4.520 1.00 29.93 ? 141 GLN A O 1 ATOM 873 C CB . GLN A 1 114 ? -0.754 70.888 -4.797 1.00 37.43 ? 141 GLN A CB 1 ATOM 874 C CG . GLN A 1 114 ? -1.863 70.554 -3.815 1.00 50.49 ? 141 GLN A CG 1 ATOM 875 C CD . GLN A 1 114 ? -3.153 70.127 -4.505 1.00 62.68 ? 141 GLN A CD 1 ATOM 876 O OE1 . GLN A 1 114 ? -3.133 69.579 -5.610 1.00 66.48 ? 141 GLN A OE1 1 ATOM 877 N NE2 . GLN A 1 114 ? -4.282 70.382 -3.853 1.00 64.12 ? 141 GLN A NE2 1 ATOM 878 N N . TRP A 1 115 ? 0.129 73.946 -4.800 1.00 32.73 ? 142 TRP A N 1 ATOM 879 C CA . TRP A 1 115 ? 0.311 75.247 -4.176 1.00 27.32 ? 142 TRP A CA 1 ATOM 880 C C . TRP A 1 115 ? -0.525 76.279 -4.934 1.00 27.34 ? 142 TRP A C 1 ATOM 881 O O . TRP A 1 115 ? -1.317 77.016 -4.345 1.00 25.24 ? 142 TRP A O 1 ATOM 882 C CB . TRP A 1 115 ? 1.796 75.603 -4.232 1.00 23.12 ? 142 TRP A CB 1 ATOM 883 C CG . TRP A 1 115 ? 2.230 76.826 -3.485 1.00 26.39 ? 142 TRP A CG 1 ATOM 884 C CD1 . TRP A 1 115 ? 1.452 77.673 -2.745 1.00 30.06 ? 142 TRP A CD1 1 ATOM 885 C CD2 . TRP A 1 115 ? 3.567 77.344 -3.415 1.00 25.46 ? 142 TRP A CD2 1 ATOM 886 N NE1 . TRP A 1 115 ? 2.227 78.686 -2.216 1.00 26.06 ? 142 TRP A NE1 1 ATOM 887 C CE2 . TRP A 1 115 ? 3.526 78.506 -2.617 1.00 24.14 ? 142 TRP A CE2 1 ATOM 888 C CE3 . TRP A 1 115 ? 4.796 76.932 -3.947 1.00 24.08 ? 142 TRP A CE3 1 ATOM 889 C CZ2 . TRP A 1 115 ? 4.664 79.260 -2.341 1.00 25.66 ? 142 TRP A CZ2 1 ATOM 890 C CZ3 . TRP A 1 115 ? 5.930 77.686 -3.671 1.00 23.25 ? 142 TRP A CZ3 1 ATOM 891 C CH2 . TRP A 1 115 ? 5.854 78.835 -2.875 1.00 24.09 ? 142 TRP A CH2 1 ATOM 892 N N . TRP A 1 116 ? -0.359 76.297 -6.250 1.00 28.73 ? 143 TRP A N 1 ATOM 893 C CA . TRP A 1 116 ? -1.046 77.241 -7.126 1.00 32.53 ? 143 TRP A CA 1 ATOM 894 C C . TRP A 1 116 ? -2.568 77.086 -7.074 1.00 31.86 ? 143 TRP A C 1 ATOM 895 O O . TRP A 1 116 ? -3.300 78.073 -7.034 1.00 26.67 ? 143 TRP A O 1 ATOM 896 C CB . TRP A 1 116 ? -0.533 77.062 -8.558 1.00 34.94 ? 143 TRP A CB 1 ATOM 897 C CG . TRP A 1 116 ? -1.091 78.018 -9.575 1.00 32.22 ? 143 TRP A CG 1 ATOM 898 C CD1 . TRP A 1 116 ? -0.698 79.309 -9.792 1.00 28.53 ? 143 TRP A CD1 1 ATOM 899 C CD2 . TRP A 1 116 ? -2.112 77.743 -10.543 1.00 29.65 ? 143 TRP A CD2 1 ATOM 900 N NE1 . TRP A 1 116 ? -1.417 79.855 -10.826 1.00 27.91 ? 143 TRP A NE1 1 ATOM 901 C CE2 . TRP A 1 116 ? -2.293 78.916 -11.304 1.00 29.66 ? 143 TRP A CE2 1 ATOM 902 C CE3 . TRP A 1 116 ? -2.893 76.619 -10.838 1.00 30.13 ? 143 TRP A CE3 1 ATOM 903 C CZ2 . TRP A 1 116 ? -3.230 79.001 -12.337 1.00 30.87 ? 143 TRP A CZ2 1 ATOM 904 C CZ3 . TRP A 1 116 ? -3.821 76.702 -11.866 1.00 32.86 ? 143 TRP A CZ3 1 ATOM 905 C CH2 . TRP A 1 116 ? -3.981 77.884 -12.603 1.00 36.23 ? 143 TRP A CH2 1 ATOM 906 N N . GLU A 1 117 ? -3.039 75.843 -7.072 1.00 32.72 ? 144 GLU A N 1 ATOM 907 C CA . GLU A 1 117 ? -4.469 75.579 -7.005 1.00 37.70 ? 144 GLU A CA 1 ATOM 908 C C . GLU A 1 117 ? -5.076 75.922 -5.644 1.00 30.90 ? 144 GLU A C 1 ATOM 909 O O . GLU A 1 117 ? -6.181 76.455 -5.576 1.00 28.21 ? 144 GLU A O 1 ATOM 910 C CB . GLU A 1 117 ? -4.768 74.120 -7.381 1.00 44.56 ? 144 GLU A CB 1 ATOM 911 C CG . GLU A 1 117 ? -4.694 73.850 -8.878 1.00 53.08 ? 144 GLU A CG 1 ATOM 912 C CD . GLU A 1 117 ? -4.481 72.383 -9.207 1.00 66.25 ? 144 GLU A CD 1 ATOM 913 O OE1 . GLU A 1 117 ? -5.025 71.521 -8.484 1.00 70.16 ? 144 GLU A OE1 1 ATOM 914 O OE2 . GLU A 1 117 ? -3.761 72.092 -10.187 1.00 68.59 ? 144 GLU A OE2 1 ATOM 915 N N . ASP A 1 118 ? -4.361 75.614 -4.566 1.00 26.80 ? 145 ASP A N 1 ATOM 916 C CA . ASP A 1 118 ? -4.888 75.833 -3.218 1.00 27.80 ? 145 ASP A CA 1 ATOM 917 C C . ASP A 1 118 ? -4.931 77.307 -2.830 1.00 27.35 ? 145 ASP A C 1 ATOM 918 O O . ASP A 1 118 ? -5.550 77.674 -1.832 1.00 29.37 ? 145 ASP A O 1 ATOM 919 C CB . ASP A 1 118 ? -4.071 75.063 -2.176 1.00 25.21 ? 145 ASP A CB 1 ATOM 920 C CG . ASP A 1 118 ? -4.320 73.567 -2.224 1.00 34.35 ? 145 ASP A CG 1 ATOM 921 O OD1 . ASP A 1 118 ? -5.273 73.133 -2.904 1.00 34.12 ? 145 ASP A OD1 1 ATOM 922 O OD2 . ASP A 1 118 ? -3.565 72.823 -1.565 1.00 38.68 ? 145 ASP A OD2 1 ATOM 923 N N . CYS A 1 119 ? -4.257 78.146 -3.609 1.00 25.20 ? 146 CYS A N 1 ATOM 924 C CA . CYS A 1 119 ? -4.205 79.578 -3.331 1.00 20.33 ? 146 CYS A CA 1 ATOM 925 C C . CYS A 1 119 ? -5.098 80.385 -4.278 1.00 26.81 ? 146 CYS A C 1 ATOM 926 O O . CYS A 1 119 ? -5.116 81.613 -4.231 1.00 25.51 ? 146 CYS A O 1 ATOM 927 C CB . CYS A 1 119 ? -2.760 80.081 -3.401 1.00 20.48 ? 146 CYS A CB 1 ATOM 928 S SG . CYS A 1 119 ? -1.695 79.557 -2.016 1.00 25.44 ? 146 CYS A SG 1 ATOM 929 N N . ARG A 1 120 ? -5.850 79.689 -5.127 1.00 32.20 ? 147 ARG A N 1 ATOM 930 C CA . ARG A 1 120 ? -6.745 80.347 -6.078 1.00 31.63 ? 147 ARG A CA 1 ATOM 931 C C . ARG A 1 120 ? -7.707 81.342 -5.427 1.00 31.33 ? 147 ARG A C 1 ATOM 932 O O . ARG A 1 120 ? -7.959 82.420 -5.976 1.00 25.26 ? 147 ARG A O 1 ATOM 933 C CB . ARG A 1 120 ? -7.552 79.314 -6.878 1.00 31.71 ? 147 ARG A CB 1 ATOM 934 C CG . ARG A 1 120 ? -8.589 79.939 -7.808 1.00 28.66 ? 147 ARG A CG 1 ATOM 935 C CD . ARG A 1 120 ? -9.408 78.890 -8.544 1.00 41.97 ? 147 ARG A CD 1 ATOM 936 N NE . ARG A 1 120 ? -10.150 78.027 -7.626 1.00 49.53 ? 147 ARG A NE 1 ATOM 937 C CZ . ARG A 1 120 ? -11.305 78.359 -7.052 1.00 50.45 ? 147 ARG A CZ 1 ATOM 938 N NH1 . ARG A 1 120 ? -11.859 79.540 -7.292 1.00 42.96 ? 147 ARG A NH1 1 ATOM 939 N NH2 . ARG A 1 120 ? -11.904 77.508 -6.229 1.00 56.22 ? 147 ARG A NH2 1 ATOM 940 N N . THR A 1 121 ? -8.252 80.978 -4.269 1.00 30.30 ? 148 THR A N 1 ATOM 941 C CA . THR A 1 121 ? -9.293 81.790 -3.635 1.00 31.08 ? 148 THR A CA 1 ATOM 942 C C . THR A 1 121 ? -8.728 82.856 -2.698 1.00 30.34 ? 148 THR A C 1 ATOM 943 O O . THR A 1 121 ? -9.474 83.600 -2.068 1.00 31.93 ? 148 THR A O 1 ATOM 944 C CB . THR A 1 121 ? -10.296 80.917 -2.863 1.00 28.85 ? 148 THR A CB 1 ATOM 945 O OG1 . THR A 1 121 ? -9.611 80.227 -1.812 1.00 29.72 ? 148 THR A OG1 1 ATOM 946 C CG2 . THR A 1 121 ? -10.948 79.903 -3.800 1.00 23.00 ? 148 THR A CG2 1 ATOM 947 N N . SER A 1 122 ? -7.406 82.924 -2.611 1.00 28.95 ? 149 SER A N 1 ATOM 948 C CA . SER A 1 122 ? -6.753 83.938 -1.803 1.00 21.54 ? 149 SER A CA 1 ATOM 949 C C . SER A 1 122 ? -6.403 85.142 -2.670 1.00 20.52 ? 149 SER A C 1 ATOM 950 O O . SER A 1 122 ? -6.555 85.108 -3.893 1.00 18.43 ? 149 SER A O 1 ATOM 951 C CB . SER A 1 122 ? -5.489 83.376 -1.149 1.00 24.38 ? 149 SER A CB 1 ATOM 952 O OG . SER A 1 122 ? -5.808 82.368 -0.212 1.00 28.86 ? 149 SER A OG 1 ATOM 953 N N . TYR A 1 123 ? -5.924 86.203 -2.029 1.00 24.82 ? 150 TYR A N 1 ATOM 954 C CA . TYR A 1 123 ? -5.592 87.436 -2.731 1.00 24.48 ? 150 TYR A CA 1 ATOM 955 C C . TYR A 1 123 ? -4.174 87.885 -2.404 1.00 26.00 ? 150 TYR A C 1 ATOM 956 O O . TYR A 1 123 ? -3.636 87.552 -1.352 1.00 21.58 ? 150 TYR A O 1 ATOM 957 C CB . TYR A 1 123 ? -6.587 88.539 -2.353 1.00 23.36 ? 150 TYR A CB 1 ATOM 958 C CG . TYR A 1 123 ? -8.006 88.257 -2.790 1.00 26.83 ? 150 TYR A CG 1 ATOM 959 C CD1 . TYR A 1 123 ? -8.551 88.900 -3.895 1.00 32.73 ? 150 TYR A CD1 1 ATOM 960 C CD2 . TYR A 1 123 ? -8.798 87.339 -2.106 1.00 26.66 ? 150 TYR A CD2 1 ATOM 961 C CE1 . TYR A 1 123 ? -9.851 88.645 -4.307 1.00 38.36 ? 150 TYR A CE1 1 ATOM 962 C CE2 . TYR A 1 123 ? -10.103 87.075 -2.509 1.00 29.71 ? 150 TYR A CE2 1 ATOM 963 C CZ . TYR A 1 123 ? -10.621 87.729 -3.615 1.00 38.49 ? 150 TYR A CZ 1 ATOM 964 O OH . TYR A 1 123 ? -11.911 87.479 -4.033 1.00 43.63 ? 150 TYR A OH 1 ATOM 965 N N . THR A 1 124 ? -3.577 88.650 -3.310 1.00 30.16 ? 151 THR A N 1 ATOM 966 C CA . THR A 1 124 ? -2.272 89.252 -3.067 1.00 26.53 ? 151 THR A CA 1 ATOM 967 C C . THR A 1 124 ? -2.161 90.545 -3.869 1.00 22.01 ? 151 THR A C 1 ATOM 968 O O . THR A 1 124 ? -3.010 90.827 -4.711 1.00 24.90 ? 151 THR A O 1 ATOM 969 C CB . THR A 1 124 ? -1.123 88.289 -3.434 1.00 21.44 ? 151 THR A CB 1 ATOM 970 O OG1 . THR A 1 124 ? 0.114 88.810 -2.940 1.00 22.31 ? 151 THR A OG1 1 ATOM 971 C CG2 . THR A 1 124 ? -1.035 88.113 -4.934 1.00 16.55 ? 151 THR A CG2 1 ATOM 972 N N . CYS A 1 125 ? -1.116 91.328 -3.619 1.00 25.10 ? 152 CYS A N 1 ATOM 973 C CA . CYS A 1 125 ? -0.998 92.642 -4.249 1.00 23.93 ? 152 CYS A CA 1 ATOM 974 C C . CYS A 1 125 ? 0.270 92.800 -5.088 1.00 24.29 ? 152 CYS A C 1 ATOM 975 O O . CYS A 1 125 ? 0.520 93.865 -5.651 1.00 23.14 ? 152 CYS A O 1 ATOM 976 C CB . CYS A 1 125 ? -1.066 93.748 -3.191 1.00 17.84 ? 152 CYS A CB 1 ATOM 977 S SG . CYS A 1 125 ? 0.181 93.591 -1.897 1.00 25.01 ? 152 CYS A SG 1 ATOM 978 N N . LYS A 1 126 ? 1.072 91.746 -5.160 1.00 22.39 ? 153 LYS A N 1 ATOM 979 C CA . LYS A 1 126 ? 2.324 91.800 -5.906 1.00 23.30 ? 153 LYS A CA 1 ATOM 980 C C . LYS A 1 126 ? 2.843 90.381 -6.174 1.00 20.19 ? 153 LYS A C 1 ATOM 981 O O . LYS A 1 126 ? 2.434 89.430 -5.511 1.00 20.29 ? 153 LYS A O 1 ATOM 982 C CB . LYS A 1 126 ? 3.364 92.659 -5.161 1.00 24.97 ? 153 LYS A CB 1 ATOM 983 C CG . LYS A 1 126 ? 4.084 91.950 -4.015 1.00 24.81 ? 153 LYS A CG 1 ATOM 984 C CD . LYS A 1 126 ? 4.760 92.928 -3.041 1.00 22.98 ? 153 LYS A CD 1 ATOM 985 C CE . LYS A 1 126 ? 5.649 93.966 -3.747 1.00 22.14 ? 153 LYS A CE 1 ATOM 986 N NZ . LYS A 1 126 ? 6.673 93.353 -4.634 1.00 22.13 ? 153 LYS A NZ 1 ATOM 987 N N . SER A 1 127 ? 3.732 90.243 -7.155 1.00 23.97 ? 154 SER A N 1 ATOM 988 C CA . SER A 1 127 ? 4.238 88.929 -7.562 1.00 20.80 ? 154 SER A CA 1 ATOM 989 C C . SER A 1 127 ? 5.608 88.598 -6.969 1.00 23.02 ? 154 SER A C 1 ATOM 990 O O . SER A 1 127 ? 5.947 87.430 -6.786 1.00 25.00 ? 154 SER A O 1 ATOM 991 C CB . SER A 1 127 ? 4.293 88.829 -9.086 1.00 23.37 ? 154 SER A CB 1 ATOM 992 O OG . SER A 1 127 ? 5.181 89.797 -9.615 1.00 29.20 ? 154 SER A OG 1 ATOM 993 N N . ASN A 1 128 ? 6.397 89.624 -6.678 1.00 26.14 ? 155 ASN A N 1 ATOM 994 C CA . ASN A 1 128 ? 7.671 89.430 -5.994 1.00 19.50 ? 155 ASN A CA 1 ATOM 995 C C . ASN A 1 128 ? 7.529 89.737 -4.505 1.00 20.19 ? 155 ASN A C 1 ATOM 996 O O . ASN A 1 128 ? 7.635 90.891 -4.089 1.00 24.96 ? 155 ASN A O 1 ATOM 997 C CB . ASN A 1 128 ? 8.752 90.312 -6.620 1.00 20.79 ? 155 ASN A CB 1 ATOM 998 C CG . ASN A 1 128 ? 10.132 90.034 -6.064 1.00 23.59 ? 155 ASN A CG 1 ATOM 999 O OD1 . ASN A 1 128 ? 10.279 89.435 -5.002 1.00 26.61 ? 155 ASN A OD1 1 ATOM 1000 N ND2 . ASN A 1 128 ? 11.155 90.479 -6.780 1.00 26.73 ? 155 ASN A ND2 1 ATOM 1001 N N . TRP A 1 129 ? 7.286 88.701 -3.707 1.00 19.71 ? 156 TRP A N 1 ATOM 1002 C CA . TRP A 1 129 ? 7.119 88.862 -2.266 1.00 17.36 ? 156 TRP A CA 1 ATOM 1003 C C . TRP A 1 129 ? 8.452 89.038 -1.535 1.00 22.34 ? 156 TRP A C 1 ATOM 1004 O O . TRP A 1 129 ? 8.476 89.236 -0.321 1.00 26.38 ? 156 TRP A O 1 ATOM 1005 C CB . TRP A 1 129 ? 6.359 87.679 -1.666 1.00 14.28 ? 156 TRP A CB 1 ATOM 1006 C CG . TRP A 1 129 ? 4.914 87.597 -2.058 1.00 17.99 ? 156 TRP A CG 1 ATOM 1007 C CD1 . TRP A 1 129 ? 4.295 88.261 -3.081 1.00 20.81 ? 156 TRP A CD1 1 ATOM 1008 C CD2 . TRP A 1 129 ? 3.903 86.799 -1.428 1.00 19.10 ? 156 TRP A CD2 1 ATOM 1009 N NE1 . TRP A 1 129 ? 2.965 87.923 -3.124 1.00 18.31 ? 156 TRP A NE1 1 ATOM 1010 C CE2 . TRP A 1 129 ? 2.699 87.028 -2.121 1.00 19.07 ? 156 TRP A CE2 1 ATOM 1011 C CE3 . TRP A 1 129 ? 3.901 85.911 -0.346 1.00 20.37 ? 156 TRP A CE3 1 ATOM 1012 C CZ2 . TRP A 1 129 ? 1.507 86.402 -1.769 1.00 21.38 ? 156 TRP A CZ2 1 ATOM 1013 C CZ3 . TRP A 1 129 ? 2.716 85.293 0.003 1.00 18.86 ? 156 TRP A CZ3 1 ATOM 1014 C CH2 . TRP A 1 129 ? 1.537 85.540 -0.704 1.00 19.60 ? 156 TRP A CH2 1 ATOM 1015 N N . HIS A 1 130 ? 9.561 88.971 -2.264 1.00 20.79 ? 157 HIS A N 1 ATOM 1016 C CA . HIS A 1 130 ? 10.862 89.172 -1.630 1.00 22.51 ? 157 HIS A CA 1 ATOM 1017 C C . HIS A 1 130 ? 11.214 90.649 -1.407 1.00 22.65 ? 157 HIS A C 1 ATOM 1018 O O . HIS A 1 130 ? 12.099 90.962 -0.610 1.00 20.46 ? 157 HIS A O 1 ATOM 1019 C CB . HIS A 1 130 ? 11.990 88.474 -2.404 1.00 21.86 ? 157 HIS A CB 1 ATOM 1020 C CG . HIS A 1 130 ? 13.335 88.666 -1.778 1.00 21.64 ? 157 HIS A CG 1 ATOM 1021 N ND1 . HIS A 1 130 ? 13.637 88.200 -0.517 1.00 21.41 ? 157 HIS A ND1 1 ATOM 1022 C CD2 . HIS A 1 130 ? 14.443 89.312 -2.218 1.00 19.53 ? 157 HIS A CD2 1 ATOM 1023 C CE1 . HIS A 1 130 ? 14.879 88.536 -0.213 1.00 23.67 ? 157 HIS A CE1 1 ATOM 1024 N NE2 . HIS A 1 130 ? 15.388 89.211 -1.226 1.00 23.69 ? 157 HIS A NE2 1 ATOM 1025 N N . LYS A 1 131 ? 10.521 91.554 -2.093 1.00 21.35 ? 158 LYS A N 1 ATOM 1026 C CA . LYS A 1 131 ? 10.841 92.979 -1.977 1.00 28.25 ? 158 LYS A CA 1 ATOM 1027 C C . LYS A 1 131 ? 9.635 93.901 -2.204 1.00 29.64 ? 158 LYS A C 1 ATOM 1028 O O . LYS A 1 131 ? 8.590 93.474 -2.706 1.00 23.94 ? 158 LYS A O 1 ATOM 1029 C CB . LYS A 1 131 ? 11.951 93.350 -2.958 1.00 30.89 ? 158 LYS A CB 1 ATOM 1030 C CG . LYS A 1 131 ? 11.493 93.385 -4.402 1.00 36.92 ? 158 LYS A CG 1 ATOM 1031 C CD . LYS A 1 131 ? 12.582 93.917 -5.323 1.00 47.73 ? 158 LYS A CD 1 ATOM 1032 C CE . LYS A 1 131 ? 12.035 94.170 -6.722 1.00 52.51 ? 158 LYS A CE 1 ATOM 1033 N NZ . LYS A 1 131 ? 13.101 94.619 -7.662 1.00 57.04 ? 158 LYS A NZ 1 ATOM 1034 N N . GLY A 1 132 ? 9.792 95.164 -1.818 1.00 25.43 ? 159 GLY A N 1 ATOM 1035 C CA . GLY A 1 132 ? 8.806 96.189 -2.109 1.00 21.26 ? 159 GLY A CA 1 ATOM 1036 C C . GLY A 1 132 ? 7.638 96.290 -1.142 1.00 24.45 ? 159 GLY A C 1 ATOM 1037 O O . GLY A 1 132 ? 6.656 96.961 -1.440 1.00 25.96 ? 159 GLY A O 1 ATOM 1038 N N . TRP A 1 133 ? 7.729 95.625 0.006 1.00 22.48 ? 160 TRP A N 1 ATOM 1039 C CA . TRP A 1 133 ? 6.680 95.726 1.016 1.00 25.70 ? 160 TRP A CA 1 ATOM 1040 C C . TRP A 1 133 ? 6.843 96.994 1.847 1.00 29.06 ? 160 TRP A C 1 ATOM 1041 O O . TRP A 1 133 ? 7.944 97.540 1.962 1.00 27.64 ? 160 TRP A O 1 ATOM 1042 C CB . TRP A 1 133 ? 6.681 94.514 1.955 1.00 20.93 ? 160 TRP A CB 1 ATOM 1043 C CG . TRP A 1 133 ? 6.319 93.212 1.308 1.00 22.33 ? 160 TRP A CG 1 ATOM 1044 C CD1 . TRP A 1 133 ? 7.175 92.211 0.941 1.00 20.26 ? 160 TRP A CD1 1 ATOM 1045 C CD2 . TRP A 1 133 ? 5.002 92.762 0.964 1.00 23.29 ? 160 TRP A CD2 1 ATOM 1046 N NE1 . TRP A 1 133 ? 6.473 91.167 0.387 1.00 20.99 ? 160 TRP A NE1 1 ATOM 1047 C CE2 . TRP A 1 133 ? 5.138 91.477 0.389 1.00 22.11 ? 160 TRP A CE2 1 ATOM 1048 C CE3 . TRP A 1 133 ? 3.721 93.322 1.080 1.00 19.03 ? 160 TRP A CE3 1 ATOM 1049 C CZ2 . TRP A 1 133 ? 4.041 90.743 -0.076 1.00 21.92 ? 160 TRP A CZ2 1 ATOM 1050 C CZ3 . TRP A 1 133 ? 2.633 92.593 0.622 1.00 19.46 ? 160 TRP A CZ3 1 ATOM 1051 C CH2 . TRP A 1 133 ? 2.801 91.314 0.052 1.00 24.49 ? 160 TRP A CH2 1 ATOM 1052 N N . ASN A 1 134 ? 5.738 97.449 2.431 1.00 27.75 ? 161 ASN A N 1 ATOM 1053 C CA . ASN A 1 134 ? 5.760 98.550 3.385 1.00 29.19 ? 161 ASN A CA 1 ATOM 1054 C C . ASN A 1 134 ? 5.840 97.981 4.799 1.00 28.71 ? 161 ASN A C 1 ATOM 1055 O O . ASN A 1 134 ? 4.903 97.322 5.259 1.00 29.07 ? 161 ASN A O 1 ATOM 1056 C CB . ASN A 1 134 ? 4.510 99.419 3.211 1.00 33.03 ? 161 ASN A CB 1 ATOM 1057 C CG . ASN A 1 134 ? 4.540 100.679 4.063 1.00 34.73 ? 161 ASN A CG 1 ATOM 1058 O OD1 . ASN A 1 134 ? 5.098 100.691 5.157 1.00 37.66 ? 161 ASN A OD1 1 ATOM 1059 N ND2 . ASN A 1 134 ? 3.930 101.744 3.563 1.00 41.42 ? 161 ASN A ND2 1 ATOM 1060 N N . TRP A 1 135 ? 6.962 98.222 5.477 1.00 29.07 ? 162 TRP A N 1 ATOM 1061 C CA . TRP A 1 135 ? 7.231 97.607 6.784 1.00 33.41 ? 162 TRP A CA 1 ATOM 1062 C C . TRP A 1 135 ? 7.023 98.547 7.977 1.00 33.95 ? 162 TRP A C 1 ATOM 1063 O O . TRP A 1 135 ? 7.483 98.265 9.086 1.00 31.62 ? 162 TRP A O 1 ATOM 1064 C CB . TRP A 1 135 ? 8.652 97.018 6.830 1.00 25.15 ? 162 TRP A CB 1 ATOM 1065 C CG . TRP A 1 135 ? 8.854 95.829 5.927 1.00 24.82 ? 162 TRP A CG 1 ATOM 1066 C CD1 . TRP A 1 135 ? 9.300 95.847 4.638 1.00 26.75 ? 162 TRP A CD1 1 ATOM 1067 C CD2 . TRP A 1 135 ? 8.618 94.451 6.250 1.00 25.30 ? 162 TRP A CD2 1 ATOM 1068 N NE1 . TRP A 1 135 ? 9.359 94.567 4.136 1.00 23.34 ? 162 TRP A NE1 1 ATOM 1069 C CE2 . TRP A 1 135 ? 8.948 93.691 5.107 1.00 25.76 ? 162 TRP A CE2 1 ATOM 1070 C CE3 . TRP A 1 135 ? 8.166 93.785 7.395 1.00 24.71 ? 162 TRP A CE3 1 ATOM 1071 C CZ2 . TRP A 1 135 ? 8.836 92.297 5.075 1.00 22.75 ? 162 TRP A CZ2 1 ATOM 1072 C CZ3 . TRP A 1 135 ? 8.055 92.405 7.363 1.00 23.35 ? 162 TRP A CZ3 1 ATOM 1073 C CH2 . TRP A 1 135 ? 8.387 91.676 6.211 1.00 24.38 ? 162 TRP A CH2 1 ATOM 1074 N N . THR A 1 136 ? 6.321 99.651 7.746 1.00 33.67 ? 163 THR A N 1 ATOM 1075 C CA . THR A 1 136 ? 6.094 100.663 8.780 1.00 40.44 ? 163 THR A CA 1 ATOM 1076 C C . THR A 1 136 ? 5.479 100.125 10.079 1.00 42.31 ? 163 THR A C 1 ATOM 1077 O O . THR A 1 136 ? 5.878 100.524 11.174 1.00 45.89 ? 163 THR A O 1 ATOM 1078 C CB . THR A 1 136 ? 5.222 101.821 8.241 1.00 42.84 ? 163 THR A CB 1 ATOM 1079 O OG1 . THR A 1 136 ? 5.979 102.582 7.293 1.00 44.32 ? 163 THR A OG1 1 ATOM 1080 C CG2 . THR A 1 136 ? 4.775 102.735 9.371 1.00 47.85 ? 163 THR A CG2 1 ATOM 1081 N N . SER A 1 137 ? 4.515 99.221 9.960 1.00 37.05 ? 164 SER A N 1 ATOM 1082 C CA . SER A 1 137 ? 3.788 98.732 11.127 1.00 37.72 ? 164 SER A CA 1 ATOM 1083 C C . SER A 1 137 ? 4.538 97.651 11.916 1.00 41.19 ? 164 SER A C 1 ATOM 1084 O O . SER A 1 137 ? 4.054 97.184 12.950 1.00 43.25 ? 164 SER A O 1 ATOM 1085 C CB . SER A 1 137 ? 2.416 98.200 10.708 1.00 38.34 ? 164 SER A CB 1 ATOM 1086 O OG . SER A 1 137 ? 2.547 97.035 9.919 1.00 40.56 ? 164 SER A OG 1 ATOM 1087 N N . GLY A 1 138 ? 5.713 97.251 11.437 1.00 34.33 ? 165 GLY A N 1 ATOM 1088 C CA . GLY A 1 138 ? 6.436 96.157 12.063 1.00 33.12 ? 165 GLY A CA 1 ATOM 1089 C C . GLY A 1 138 ? 6.229 94.850 11.317 1.00 36.41 ? 165 GLY A C 1 ATOM 1090 O O . GLY A 1 138 ? 6.934 93.866 11.547 1.00 38.76 ? 165 GLY A O 1 ATOM 1091 N N . PHE A 1 139 ? 5.244 94.838 10.426 1.00 35.33 ? 166 PHE A N 1 ATOM 1092 C CA . PHE A 1 139 ? 5.052 93.724 9.506 1.00 33.08 ? 166 PHE A CA 1 ATOM 1093 C C . PHE A 1 139 ? 4.718 94.277 8.121 1.00 25.28 ? 166 PHE A C 1 ATOM 1094 O O . PHE A 1 139 ? 4.486 95.471 7.970 1.00 26.59 ? 166 PHE A O 1 ATOM 1095 C CB . PHE A 1 139 ? 3.970 92.757 10.010 1.00 33.30 ? 166 PHE A CB 1 ATOM 1096 C CG . PHE A 1 139 ? 2.652 93.416 10.303 1.00 30.25 ? 166 PHE A CG 1 ATOM 1097 C CD1 . PHE A 1 139 ? 1.671 93.502 9.324 1.00 32.47 ? 166 PHE A CD1 1 ATOM 1098 C CD2 . PHE A 1 139 ? 2.392 93.951 11.558 1.00 31.30 ? 166 PHE A CD2 1 ATOM 1099 C CE1 . PHE A 1 139 ? 0.449 94.115 9.591 1.00 33.20 ? 166 PHE A CE1 1 ATOM 1100 C CE2 . PHE A 1 139 ? 1.176 94.566 11.834 1.00 33.41 ? 166 PHE A CE2 1 ATOM 1101 C CZ . PHE A 1 139 ? 0.203 94.650 10.848 1.00 31.63 ? 166 PHE A CZ 1 ATOM 1102 N N . ASN A 1 140 ? 4.698 93.408 7.117 1.00 24.20 ? 167 ASN A N 1 ATOM 1103 C CA . ASN A 1 140 ? 4.521 93.839 5.730 1.00 22.47 ? 167 ASN A CA 1 ATOM 1104 C C . ASN A 1 140 ? 3.070 94.114 5.323 1.00 22.43 ? 167 ASN A C 1 ATOM 1105 O O . ASN A 1 140 ? 2.180 93.295 5.548 1.00 23.17 ? 167 ASN A O 1 ATOM 1106 C CB . ASN A 1 140 ? 5.142 92.810 4.781 1.00 25.36 ? 167 ASN A CB 1 ATOM 1107 C CG . ASN A 1 140 ? 4.557 91.420 4.965 1.00 25.28 ? 167 ASN A CG 1 ATOM 1108 O OD1 . ASN A 1 140 ? 4.738 90.797 6.009 1.00 26.68 ? 167 ASN A OD1 1 ATOM 1109 N ND2 . ASN A 1 140 ? 3.850 90.929 3.950 1.00 19.44 ? 167 ASN A ND2 1 ATOM 1110 N N . LYS A 1 141 ? 2.847 95.286 4.735 1.00 25.45 ? 168 LYS A N 1 ATOM 1111 C CA . LYS A 1 141 ? 1.578 95.616 4.099 1.00 26.29 ? 168 LYS A CA 1 ATOM 1112 C C . LYS A 1 141 ? 1.856 96.023 2.660 1.00 19.27 ? 168 LYS A C 1 ATOM 1113 O O . LYS A 1 141 ? 2.958 96.458 2.342 1.00 18.89 ? 168 LYS A O 1 ATOM 1114 C CB . LYS A 1 141 ? 0.860 96.741 4.851 1.00 26.30 ? 168 LYS A CB 1 ATOM 1115 C CG . LYS A 1 141 ? 0.337 96.324 6.219 1.00 28.77 ? 168 LYS A CG 1 ATOM 1116 C CD . LYS A 1 141 ? -0.288 97.496 6.952 1.00 37.22 ? 168 LYS A CD 1 ATOM 1117 C CE . LYS A 1 141 ? -0.764 97.089 8.340 1.00 42.25 ? 168 LYS A CE 1 ATOM 1118 N NZ . LYS A 1 141 ? -1.441 98.218 9.051 1.00 46.49 ? 168 LYS A NZ 1 ATOM 1119 N N . CYS A 1 142 ? 0.871 95.852 1.787 1.00 21.49 ? 169 CYS A N 1 ATOM 1120 C CA . CYS A 1 142 ? 1.016 96.270 0.403 1.00 23.38 ? 169 CYS A CA 1 ATOM 1121 C C . CYS A 1 142 ? 1.327 97.757 0.382 1.00 29.19 ? 169 CYS A C 1 ATOM 1122 O O . CYS A 1 142 ? 0.690 98.538 1.080 1.00 28.49 ? 169 CYS A O 1 ATOM 1123 C CB . CYS A 1 142 ? -0.270 96.010 -0.380 1.00 22.70 ? 169 CYS A CB 1 ATOM 1124 S SG . CYS A 1 142 ? -0.858 94.306 -0.311 1.00 22.66 ? 169 CYS A SG 1 ATOM 1125 N N . ALA A 1 143 ? 2.318 98.142 -0.409 1.00 29.75 ? 170 ALA A N 1 ATOM 1126 C CA . ALA A 1 143 ? 2.648 99.545 -0.575 1.00 29.93 ? 170 ALA A CA 1 ATOM 1127 C C . ALA A 1 143 ? 1.528 100.260 -1.325 1.00 33.10 ? 170 ALA A C 1 ATOM 1128 O O . ALA A 1 143 ? 0.746 99.630 -2.046 1.00 33.30 ? 170 ALA A O 1 ATOM 1129 C CB . ALA A 1 143 ? 3.964 99.690 -1.320 1.00 28.90 ? 170 ALA A CB 1 ATOM 1130 N N . VAL A 1 144 ? 1.452 101.574 -1.136 1.00 31.69 ? 171 VAL A N 1 ATOM 1131 C CA . VAL A 1 144 ? 0.544 102.423 -1.897 1.00 33.47 ? 171 VAL A CA 1 ATOM 1132 C C . VAL A 1 144 ? 0.730 102.157 -3.386 1.00 36.70 ? 171 VAL A C 1 ATOM 1133 O O . VAL A 1 144 ? 1.861 102.120 -3.878 1.00 37.14 ? 171 VAL A O 1 ATOM 1134 C CB . VAL A 1 144 ? 0.806 103.927 -1.613 1.00 42.56 ? 171 VAL A CB 1 ATOM 1135 C CG1 . VAL A 1 144 ? -0.040 104.807 -2.526 1.00 42.22 ? 171 VAL A CG1 1 ATOM 1136 C CG2 . VAL A 1 144 ? 0.534 104.253 -0.147 1.00 38.96 ? 171 VAL A CG2 1 ATOM 1137 N N . GLY A 1 145 ? -0.376 101.962 -4.099 1.00 33.60 ? 172 GLY A N 1 ATOM 1138 C CA . GLY A 1 145 ? -0.314 101.700 -5.525 1.00 33.26 ? 172 GLY A CA 1 ATOM 1139 C C . GLY A 1 145 ? -0.347 100.223 -5.883 1.00 34.82 ? 172 GLY A C 1 ATOM 1140 O O . GLY A 1 145 ? -0.563 99.868 -7.042 1.00 43.28 ? 172 GLY A O 1 ATOM 1141 N N . ALA A 1 146 ? -0.138 99.359 -4.893 1.00 27.31 ? 173 ALA A N 1 ATOM 1142 C CA . ALA A 1 146 ? -0.164 97.912 -5.118 1.00 24.78 ? 173 ALA A CA 1 ATOM 1143 C C . ALA A 1 146 ? -1.555 97.361 -4.824 1.00 28.28 ? 173 ALA A C 1 ATOM 1144 O O . ALA A 1 146 ? -1.942 97.212 -3.667 1.00 31.15 ? 173 ALA A O 1 ATOM 1145 C CB . ALA A 1 146 ? 0.884 97.217 -4.260 1.00 21.30 ? 173 ALA A CB 1 ATOM 1146 N N . ALA A 1 147 ? -2.304 97.069 -5.882 1.00 27.44 ? 174 ALA A N 1 ATOM 1147 C CA . ALA A 1 147 ? -3.700 96.672 -5.747 1.00 27.99 ? 174 ALA A CA 1 ATOM 1148 C C . ALA A 1 147 ? -3.853 95.189 -5.425 1.00 26.03 ? 174 ALA A C 1 ATOM 1149 O O . ALA A 1 147 ? -3.243 94.339 -6.068 1.00 23.24 ? 174 ALA A O 1 ATOM 1150 C CB . ALA A 1 147 ? -4.466 97.014 -7.012 1.00 30.79 ? 174 ALA A CB 1 ATOM 1151 N N . CYS A 1 148 ? -4.665 94.890 -4.419 1.00 25.34 ? 175 CYS A N 1 ATOM 1152 C CA . CYS A 1 148 ? -5.012 93.512 -4.111 1.00 27.95 ? 175 CYS A CA 1 ATOM 1153 C C . CYS A 1 148 ? -5.874 92.938 -5.231 1.00 26.03 ? 175 CYS A C 1 ATOM 1154 O O . CYS A 1 148 ? -6.781 93.601 -5.728 1.00 29.08 ? 175 CYS A O 1 ATOM 1155 C CB . CYS A 1 148 ? -5.741 93.422 -2.770 1.00 23.21 ? 175 CYS A CB 1 ATOM 1156 S SG . CYS A 1 148 ? -4.696 93.752 -1.340 1.00 25.16 ? 175 CYS A SG 1 ATOM 1157 N N . GLN A 1 149 ? -5.564 91.711 -5.633 1.00 24.82 ? 176 GLN A N 1 ATOM 1158 C CA . GLN A 1 149 ? -6.274 91.030 -6.709 1.00 21.35 ? 176 GLN A CA 1 ATOM 1159 C C . GLN A 1 149 ? -6.286 89.535 -6.405 1.00 24.62 ? 176 GLN A C 1 ATOM 1160 O O . GLN A 1 149 ? -5.573 89.080 -5.509 1.00 24.39 ? 176 GLN A O 1 ATOM 1161 C CB . GLN A 1 149 ? -5.584 91.286 -8.053 1.00 22.97 ? 176 GLN A CB 1 ATOM 1162 C CG . GLN A 1 149 ? -5.391 92.763 -8.417 1.00 24.57 ? 176 GLN A CG 1 ATOM 1163 C CD . GLN A 1 149 ? -6.683 93.454 -8.835 1.00 28.96 ? 176 GLN A CD 1 ATOM 1164 O OE1 . GLN A 1 149 ? -7.761 92.868 -8.771 1.00 26.70 ? 176 GLN A OE1 1 ATOM 1165 N NE2 . GLN A 1 149 ? -6.572 94.708 -9.277 1.00 27.38 ? 176 GLN A NE2 1 ATOM 1166 N N . PRO A 1 150 ? -7.100 88.762 -7.141 1.00 27.06 ? 177 PRO A N 1 ATOM 1167 C CA . PRO A 1 150 ? -7.065 87.309 -6.966 1.00 22.11 ? 177 PRO A CA 1 ATOM 1168 C C . PRO A 1 150 ? -5.641 86.793 -7.146 1.00 24.25 ? 177 PRO A C 1 ATOM 1169 O O . PRO A 1 150 ? -4.886 87.352 -7.944 1.00 23.44 ? 177 PRO A O 1 ATOM 1170 C CB . PRO A 1 150 ? -7.964 86.803 -8.099 1.00 23.34 ? 177 PRO A CB 1 ATOM 1171 C CG . PRO A 1 150 ? -8.932 87.909 -8.312 1.00 29.24 ? 177 PRO A CG 1 ATOM 1172 C CD . PRO A 1 150 ? -8.133 89.175 -8.109 1.00 30.78 ? 177 PRO A CD 1 ATOM 1173 N N . PHE A 1 151 ? -5.286 85.748 -6.405 1.00 24.15 ? 178 PHE A N 1 ATOM 1174 C CA . PHE A 1 151 ? -3.930 85.208 -6.419 1.00 26.54 ? 178 PHE A CA 1 ATOM 1175 C C . PHE A 1 151 ? -3.375 85.007 -7.828 1.00 25.00 ? 178 PHE A C 1 ATOM 1176 O O . PHE A 1 151 ? -2.226 85.350 -8.099 1.00 26.01 ? 178 PHE A O 1 ATOM 1177 C CB . PHE A 1 151 ? -3.880 83.882 -5.651 1.00 25.17 ? 178 PHE A CB 1 ATOM 1178 C CG . PHE A 1 151 ? -2.669 83.732 -4.783 1.00 23.92 ? 178 PHE A CG 1 ATOM 1179 C CD1 . PHE A 1 151 ? -2.551 84.459 -3.608 1.00 26.17 ? 178 PHE A CD1 1 ATOM 1180 C CD2 . PHE A 1 151 ? -1.649 82.866 -5.134 1.00 29.29 ? 178 PHE A CD2 1 ATOM 1181 C CE1 . PHE A 1 151 ? -1.436 84.327 -2.801 1.00 28.73 ? 178 PHE A CE1 1 ATOM 1182 C CE2 . PHE A 1 151 ? -0.524 82.727 -4.329 1.00 27.64 ? 178 PHE A CE2 1 ATOM 1183 C CZ . PHE A 1 151 ? -0.416 83.463 -3.166 1.00 24.63 ? 178 PHE A CZ 1 ATOM 1184 N N . HIS A 1 152 ? -4.192 84.456 -8.720 1.00 26.53 ? 179 HIS A N 1 ATOM 1185 C CA . HIS A 1 152 ? -3.726 84.094 -10.059 1.00 24.41 ? 179 HIS A CA 1 ATOM 1186 C C . HIS A 1 152 ? -3.583 85.288 -10.987 1.00 26.63 ? 179 HIS A C 1 ATOM 1187 O O . HIS A 1 152 ? -3.038 85.161 -12.081 1.00 28.60 ? 179 HIS A O 1 ATOM 1188 C CB . HIS A 1 152 ? -4.633 83.031 -10.686 1.00 28.70 ? 179 HIS A CB 1 ATOM 1189 C CG . HIS A 1 152 ? -4.569 81.705 -9.991 1.00 29.92 ? 179 HIS A CG 1 ATOM 1190 N ND1 . HIS A 1 152 ? -5.417 80.660 -10.299 1.00 30.73 ? 179 HIS A ND1 1 ATOM 1191 C CD2 . HIS A 1 152 ? -3.761 81.253 -9.004 1.00 27.03 ? 179 HIS A CD2 1 ATOM 1192 C CE1 . HIS A 1 152 ? -5.133 79.625 -9.529 1.00 28.49 ? 179 HIS A CE1 1 ATOM 1193 N NE2 . HIS A 1 152 ? -4.132 79.959 -8.733 1.00 27.89 ? 179 HIS A NE2 1 ATOM 1194 N N . PHE A 1 153 ? -4.074 86.445 -10.548 1.00 28.30 ? 180 PHE A N 1 ATOM 1195 C CA . PHE A 1 153 ? -3.810 87.704 -11.238 1.00 23.38 ? 180 PHE A CA 1 ATOM 1196 C C . PHE A 1 153 ? -2.307 87.999 -11.210 1.00 27.00 ? 180 PHE A C 1 ATOM 1197 O O . PHE A 1 153 ? -1.723 88.391 -12.222 1.00 23.61 ? 180 PHE A O 1 ATOM 1198 C CB . PHE A 1 153 ? -4.594 88.845 -10.585 1.00 20.68 ? 180 PHE A CB 1 ATOM 1199 C CG . PHE A 1 153 ? -4.319 90.202 -11.179 1.00 24.91 ? 180 PHE A CG 1 ATOM 1200 C CD1 . PHE A 1 153 ? -5.141 90.721 -12.171 1.00 24.60 ? 180 PHE A CD1 1 ATOM 1201 C CD2 . PHE A 1 153 ? -3.249 90.967 -10.733 1.00 26.28 ? 180 PHE A CD2 1 ATOM 1202 C CE1 . PHE A 1 153 ? -4.897 91.971 -12.711 1.00 29.04 ? 180 PHE A CE1 1 ATOM 1203 C CE2 . PHE A 1 153 ? -2.997 92.224 -11.269 1.00 23.04 ? 180 PHE A CE2 1 ATOM 1204 C CZ . PHE A 1 153 ? -3.821 92.726 -12.258 1.00 28.05 ? 180 PHE A CZ 1 ATOM 1205 N N . TYR A 1 154 ? -1.675 87.800 -10.055 1.00 25.36 ? 181 TYR A N 1 ATOM 1206 C CA . TYR A 1 154 ? -0.232 88.013 -9.961 1.00 25.66 ? 181 TYR A CA 1 ATOM 1207 C C . TYR A 1 154 ? 0.559 86.753 -10.301 1.00 28.40 ? 181 TYR A C 1 ATOM 1208 O O . TYR A 1 154 ? 1.701 86.835 -10.759 1.00 27.58 ? 181 TYR A O 1 ATOM 1209 C CB . TYR A 1 154 ? 0.172 88.589 -8.598 1.00 19.19 ? 181 TYR A CB 1 ATOM 1210 C CG . TYR A 1 154 ? -0.253 90.032 -8.444 1.00 19.97 ? 181 TYR A CG 1 ATOM 1211 C CD1 . TYR A 1 154 ? 0.457 91.052 -9.061 1.00 21.42 ? 181 TYR A CD1 1 ATOM 1212 C CD2 . TYR A 1 154 ? -1.382 90.373 -7.710 1.00 19.83 ? 181 TYR A CD2 1 ATOM 1213 C CE1 . TYR A 1 154 ? 0.067 92.370 -8.939 1.00 23.72 ? 181 TYR A CE1 1 ATOM 1214 C CE2 . TYR A 1 154 ? -1.782 91.693 -7.584 1.00 24.80 ? 181 TYR A CE2 1 ATOM 1215 C CZ . TYR A 1 154 ? -1.054 92.685 -8.200 1.00 25.22 ? 181 TYR A CZ 1 ATOM 1216 O OH . TYR A 1 154 ? -1.439 93.998 -8.078 1.00 24.85 ? 181 TYR A OH 1 ATOM 1217 N N . PHE A 1 155 ? -0.062 85.593 -10.099 1.00 25.29 ? 182 PHE A N 1 ATOM 1218 C CA . PHE A 1 155 ? 0.572 84.313 -10.417 1.00 19.65 ? 182 PHE A CA 1 ATOM 1219 C C . PHE A 1 155 ? -0.307 83.511 -11.371 1.00 21.91 ? 182 PHE A C 1 ATOM 1220 O O . PHE A 1 155 ? -1.001 82.576 -10.959 1.00 28.02 ? 182 PHE A O 1 ATOM 1221 C CB . PHE A 1 155 ? 0.849 83.528 -9.136 1.00 18.37 ? 182 PHE A CB 1 ATOM 1222 C CG . PHE A 1 155 ? 1.618 84.310 -8.105 1.00 22.66 ? 182 PHE A CG 1 ATOM 1223 C CD1 . PHE A 1 155 ? 2.960 84.614 -8.302 1.00 22.38 ? 182 PHE A CD1 1 ATOM 1224 C CD2 . PHE A 1 155 ? 0.999 84.744 -6.940 1.00 21.82 ? 182 PHE A CD2 1 ATOM 1225 C CE1 . PHE A 1 155 ? 3.673 85.336 -7.352 1.00 18.77 ? 182 PHE A CE1 1 ATOM 1226 C CE2 . PHE A 1 155 ? 1.702 85.463 -5.986 1.00 17.38 ? 182 PHE A CE2 1 ATOM 1227 C CZ . PHE A 1 155 ? 3.044 85.759 -6.192 1.00 16.05 ? 182 PHE A CZ 1 ATOM 1228 N N . PRO A 1 156 ? -0.295 83.887 -12.656 1.00 26.52 ? 183 PRO A N 1 ATOM 1229 C CA . PRO A 1 156 ? -1.243 83.307 -13.620 1.00 31.78 ? 183 PRO A CA 1 ATOM 1230 C C . PRO A 1 156 ? -0.957 81.851 -13.997 1.00 29.53 ? 183 PRO A C 1 ATOM 1231 O O . PRO A 1 156 ? -1.815 81.215 -14.602 1.00 29.28 ? 183 PRO A O 1 ATOM 1232 C CB . PRO A 1 156 ? -1.119 84.229 -14.840 1.00 29.76 ? 183 PRO A CB 1 ATOM 1233 C CG . PRO A 1 156 ? 0.226 84.880 -14.698 1.00 29.99 ? 183 PRO A CG 1 ATOM 1234 C CD . PRO A 1 156 ? 0.469 85.012 -13.226 1.00 27.68 ? 183 PRO A CD 1 ATOM 1235 N N . THR A 1 157 ? 0.218 81.337 -13.644 1.00 32.18 ? 184 THR A N 1 ATOM 1236 C CA . THR A 1 157 ? 0.539 79.922 -13.849 1.00 31.04 ? 184 THR A CA 1 ATOM 1237 C C . THR A 1 157 ? 1.365 79.422 -12.668 1.00 28.79 ? 184 THR A C 1 ATOM 1238 O O . THR A 1 157 ? 2.001 80.220 -11.984 1.00 25.10 ? 184 THR A O 1 ATOM 1239 C CB . THR A 1 157 ? 1.329 79.680 -15.163 1.00 32.63 ? 184 THR A CB 1 ATOM 1240 O OG1 . THR A 1 157 ? 2.638 80.252 -15.058 1.00 29.06 ? 184 THR A OG1 1 ATOM 1241 C CG2 . THR A 1 157 ? 0.604 80.286 -16.358 1.00 31.44 ? 184 THR A CG2 1 ATOM 1242 N N . PRO A 1 158 ? 1.343 78.102 -12.411 1.00 28.12 ? 185 PRO A N 1 ATOM 1243 C CA . PRO A 1 158 ? 2.162 77.544 -11.327 1.00 27.87 ? 185 PRO A CA 1 ATOM 1244 C C . PRO A 1 158 ? 3.629 77.966 -11.447 1.00 29.45 ? 185 PRO A C 1 ATOM 1245 O O . PRO A 1 158 ? 4.259 78.268 -10.441 1.00 31.49 ? 185 PRO A O 1 ATOM 1246 C CB . PRO A 1 158 ? 2.016 76.030 -11.525 1.00 27.09 ? 185 PRO A CB 1 ATOM 1247 C CG . PRO A 1 158 ? 0.652 75.870 -12.145 1.00 25.17 ? 185 PRO A CG 1 ATOM 1248 C CD . PRO A 1 158 ? 0.477 77.082 -13.038 1.00 26.67 ? 185 PRO A CD 1 ATOM 1249 N N . THR A 1 159 ? 4.148 78.001 -12.669 1.00 27.00 ? 186 THR A N 1 ATOM 1250 C CA . THR A 1 159 ? 5.526 78.404 -12.918 1.00 29.90 ? 186 THR A CA 1 ATOM 1251 C C . THR A 1 159 ? 5.823 79.822 -12.419 1.00 26.60 ? 186 THR A C 1 ATOM 1252 O O . THR A 1 159 ? 6.853 80.069 -11.798 1.00 29.89 ? 186 THR A O 1 ATOM 1253 C CB . THR A 1 159 ? 5.873 78.288 -14.421 1.00 32.60 ? 186 THR A CB 1 ATOM 1254 O OG1 . THR A 1 159 ? 5.947 76.903 -14.787 1.00 35.90 ? 186 THR A OG1 1 ATOM 1255 C CG2 . THR A 1 159 ? 7.202 78.964 -14.728 1.00 24.27 ? 186 THR A CG2 1 ATOM 1256 N N . VAL A 1 160 ? 4.918 80.753 -12.687 1.00 26.32 ? 187 VAL A N 1 ATOM 1257 C CA . VAL A 1 160 ? 5.114 82.126 -12.237 1.00 25.44 ? 187 VAL A CA 1 ATOM 1258 C C . VAL A 1 160 ? 5.053 82.207 -10.717 1.00 27.06 ? 187 VAL A C 1 ATOM 1259 O O . VAL A 1 160 ? 5.872 82.890 -10.105 1.00 29.08 ? 187 VAL A O 1 ATOM 1260 C CB . VAL A 1 160 ? 4.107 83.098 -12.883 1.00 26.14 ? 187 VAL A CB 1 ATOM 1261 C CG1 . VAL A 1 160 ? 4.281 84.499 -12.315 1.00 25.21 ? 187 VAL A CG1 1 ATOM 1262 C CG2 . VAL A 1 160 ? 4.287 83.107 -14.396 1.00 23.06 ? 187 VAL A CG2 1 ATOM 1263 N N . LEU A 1 161 ? 4.105 81.493 -10.111 1.00 23.78 ? 188 LEU A N 1 ATOM 1264 C CA . LEU A 1 161 ? 4.030 81.423 -8.651 1.00 26.55 ? 188 LEU A CA 1 ATOM 1265 C C . LEU A 1 161 ? 5.338 80.939 -8.041 1.00 24.47 ? 188 LEU A C 1 ATOM 1266 O O . LEU A 1 161 ? 5.982 81.652 -7.271 1.00 23.66 ? 188 LEU A O 1 ATOM 1267 C CB . LEU A 1 161 ? 2.894 80.501 -8.190 1.00 24.33 ? 188 LEU A CB 1 ATOM 1268 C CG . LEU A 1 161 ? 2.890 80.154 -6.692 1.00 25.95 ? 188 LEU A CG 1 ATOM 1269 C CD1 . LEU A 1 161 ? 2.887 81.405 -5.815 1.00 22.75 ? 188 LEU A CD1 1 ATOM 1270 C CD2 . LEU A 1 161 ? 1.724 79.244 -6.327 1.00 23.62 ? 188 LEU A CD2 1 ATOM 1271 N N . CYS A 1 162 ? 5.725 79.721 -8.394 1.00 21.99 ? 189 CYS A N 1 ATOM 1272 C CA . CYS A 1 162 ? 6.835 79.053 -7.731 1.00 23.65 ? 189 CYS A CA 1 ATOM 1273 C C . CYS A 1 162 ? 8.181 79.699 -8.048 1.00 20.47 ? 189 CYS A C 1 ATOM 1274 O O . CYS A 1 162 ? 9.059 79.768 -7.188 1.00 20.87 ? 189 CYS A O 1 ATOM 1275 C CB . CYS A 1 162 ? 6.848 77.567 -8.098 1.00 25.96 ? 189 CYS A CB 1 ATOM 1276 S SG . CYS A 1 162 ? 5.321 76.703 -7.647 1.00 30.39 ? 189 CYS A SG 1 ATOM 1277 N N . ASN A 1 163 ? 8.332 80.165 -9.285 1.00 21.77 ? 190 ASN A N 1 ATOM 1278 C CA . ASN A 1 163 ? 9.586 80.756 -9.739 1.00 25.96 ? 190 ASN A CA 1 ATOM 1279 C C . ASN A 1 163 ? 9.743 82.219 -9.337 1.00 28.16 ? 190 ASN A C 1 ATOM 1280 O O . ASN A 1 163 ? 10.853 82.672 -9.074 1.00 27.93 ? 190 ASN A O 1 ATOM 1281 C CB . ASN A 1 163 ? 9.737 80.616 -11.257 1.00 24.96 ? 190 ASN A CB 1 ATOM 1282 C CG . ASN A 1 163 ? 9.933 79.170 -11.699 1.00 29.47 ? 190 ASN A CG 1 ATOM 1283 O OD1 . ASN A 1 163 ? 9.645 78.232 -10.954 1.00 30.62 ? 190 ASN A OD1 1 ATOM 1284 N ND2 . ASN A 1 163 ? 10.428 78.988 -12.918 1.00 25.97 ? 190 ASN A ND2 1 ATOM 1285 N N . GLU A 1 164 ? 8.637 82.957 -9.279 1.00 24.62 ? 191 GLU A N 1 ATOM 1286 C CA . GLU A 1 164 ? 8.725 84.400 -9.069 1.00 25.10 ? 191 GLU A CA 1 ATOM 1287 C C . GLU A 1 164 ? 8.403 84.889 -7.656 1.00 23.21 ? 191 GLU A C 1 ATOM 1288 O O . GLU A 1 164 ? 8.913 85.930 -7.233 1.00 25.79 ? 191 GLU A O 1 ATOM 1289 C CB . GLU A 1 164 ? 7.882 85.151 -10.104 1.00 27.81 ? 191 GLU A CB 1 ATOM 1290 C CG . GLU A 1 164 ? 8.400 84.992 -11.523 1.00 36.08 ? 191 GLU A CG 1 ATOM 1291 C CD . GLU A 1 164 ? 7.669 85.867 -12.522 1.00 47.25 ? 191 GLU A CD 1 ATOM 1292 O OE1 . GLU A 1 164 ? 7.248 86.985 -12.154 1.00 46.69 ? 191 GLU A OE1 1 ATOM 1293 O OE2 . GLU A 1 164 ? 7.517 85.434 -13.683 1.00 54.55 ? 191 GLU A OE2 1 ATOM 1294 N N . ILE A 1 165 ? 7.571 84.155 -6.927 1.00 21.34 ? 192 ILE A N 1 ATOM 1295 C CA . ILE A 1 165 ? 7.111 84.651 -5.633 1.00 21.78 ? 192 ILE A CA 1 ATOM 1296 C C . ILE A 1 165 ? 8.271 84.993 -4.699 1.00 21.95 ? 192 ILE A C 1 ATOM 1297 O O . ILE A 1 165 ? 8.233 85.999 -4.002 1.00 22.27 ? 192 ILE A O 1 ATOM 1298 C CB . ILE A 1 165 ? 6.087 83.701 -4.942 1.00 22.59 ? 192 ILE A CB 1 ATOM 1299 C CG1 . ILE A 1 165 ? 5.449 84.404 -3.738 1.00 21.16 ? 192 ILE A CG1 1 ATOM 1300 C CG2 . ILE A 1 165 ? 6.736 82.368 -4.544 1.00 17.95 ? 192 ILE A CG2 1 ATOM 1301 C CD1 . ILE A 1 165 ? 4.175 83.745 -3.234 1.00 20.21 ? 192 ILE A CD1 1 ATOM 1302 N N . TRP A 1 166 ? 9.304 84.162 -4.688 1.00 25.04 ? 193 TRP A N 1 ATOM 1303 C CA . TRP A 1 166 ? 10.489 84.474 -3.904 1.00 24.65 ? 193 TRP A CA 1 ATOM 1304 C C . TRP A 1 166 ? 11.685 84.686 -4.826 1.00 24.53 ? 193 TRP A C 1 ATOM 1305 O O . TRP A 1 166 ? 12.781 84.192 -4.564 1.00 25.19 ? 193 TRP A O 1 ATOM 1306 C CB . TRP A 1 166 ? 10.788 83.381 -2.882 1.00 22.79 ? 193 TRP A CB 1 ATOM 1307 C CG . TRP A 1 166 ? 9.684 83.121 -1.913 1.00 18.69 ? 193 TRP A CG 1 ATOM 1308 C CD1 . TRP A 1 166 ? 9.003 81.952 -1.753 1.00 18.19 ? 193 TRP A CD1 1 ATOM 1309 C CD2 . TRP A 1 166 ? 9.127 84.044 -0.961 1.00 21.17 ? 193 TRP A CD2 1 ATOM 1310 N NE1 . TRP A 1 166 ? 8.055 82.086 -0.763 1.00 24.06 ? 193 TRP A NE1 1 ATOM 1311 C CE2 . TRP A 1 166 ? 8.111 83.359 -0.261 1.00 23.47 ? 193 TRP A CE2 1 ATOM 1312 C CE3 . TRP A 1 166 ? 9.388 85.381 -0.635 1.00 20.80 ? 193 TRP A CE3 1 ATOM 1313 C CZ2 . TRP A 1 166 ? 7.362 83.960 0.749 1.00 24.05 ? 193 TRP A CZ2 1 ATOM 1314 C CZ3 . TRP A 1 166 ? 8.643 85.978 0.366 1.00 20.02 ? 193 TRP A CZ3 1 ATOM 1315 C CH2 . TRP A 1 166 ? 7.642 85.268 1.047 1.00 24.27 ? 193 TRP A CH2 1 ATOM 1316 N N . THR A 1 167 ? 11.447 85.428 -5.903 1.00 21.44 ? 194 THR A N 1 ATOM 1317 C CA . THR A 1 167 ? 12.468 85.789 -6.880 1.00 26.96 ? 194 THR A CA 1 ATOM 1318 C C . THR A 1 167 ? 13.481 84.667 -7.188 1.00 29.19 ? 194 THR A C 1 ATOM 1319 O O . THR A 1 167 ? 14.682 84.789 -6.923 1.00 26.53 ? 194 THR A O 1 ATOM 1320 C CB . THR A 1 167 ? 13.163 87.136 -6.515 1.00 21.63 ? 194 THR A CB 1 ATOM 1321 O OG1 . THR A 1 167 ? 14.017 87.541 -7.588 1.00 28.77 ? 194 THR A OG1 1 ATOM 1322 C CG2 . THR A 1 167 ? 13.969 87.028 -5.216 1.00 21.24 ? 194 THR A CG2 1 ATOM 1323 N N . HIS A 1 168 ? 12.966 83.576 -7.747 1.00 23.47 ? 195 HIS A N 1 ATOM 1324 C CA . HIS A 1 168 ? 13.788 82.482 -8.263 1.00 26.85 ? 195 HIS A CA 1 ATOM 1325 C C . HIS A 1 168 ? 14.488 81.633 -7.209 1.00 28.12 ? 195 HIS A C 1 ATOM 1326 O O . HIS A 1 168 ? 15.470 80.954 -7.508 1.00 25.17 ? 195 HIS A O 1 ATOM 1327 C CB . HIS A 1 168 ? 14.779 83.006 -9.302 1.00 25.55 ? 195 HIS A CB 1 ATOM 1328 C CG . HIS A 1 168 ? 14.106 83.619 -10.488 1.00 25.74 ? 195 HIS A CG 1 ATOM 1329 N ND1 . HIS A 1 168 ? 13.432 82.868 -11.426 1.00 26.11 ? 195 HIS A ND1 1 ATOM 1330 C CD2 . HIS A 1 168 ? 13.955 84.912 -10.860 1.00 23.88 ? 195 HIS A CD2 1 ATOM 1331 C CE1 . HIS A 1 168 ? 12.914 83.671 -12.339 1.00 27.68 ? 195 HIS A CE1 1 ATOM 1332 N NE2 . HIS A 1 168 ? 13.218 84.914 -12.019 1.00 27.99 ? 195 HIS A NE2 1 ATOM 1333 N N . SER A 1 169 ? 13.968 81.663 -5.984 1.00 24.17 ? 196 SER A N 1 ATOM 1334 C CA . SER A 1 169 ? 14.403 80.726 -4.959 1.00 24.68 ? 196 SER A CA 1 ATOM 1335 C C . SER A 1 169 ? 14.086 79.315 -5.427 1.00 27.41 ? 196 SER A C 1 ATOM 1336 O O . SER A 1 169 ? 14.867 78.391 -5.212 1.00 29.09 ? 196 SER A O 1 ATOM 1337 C CB . SER A 1 169 ? 13.708 81.008 -3.633 1.00 28.42 ? 196 SER A CB 1 ATOM 1338 O OG . SER A 1 169 ? 14.283 82.137 -2.999 1.00 40.74 ? 196 SER A OG 1 ATOM 1339 N N . TYR A 1 170 ? 12.935 79.162 -6.078 1.00 21.63 ? 197 TYR A N 1 ATOM 1340 C CA . TYR A 1 170 ? 12.583 77.902 -6.712 1.00 19.94 ? 197 TYR A CA 1 ATOM 1341 C C . TYR A 1 170 ? 12.659 78.022 -8.229 1.00 24.40 ? 197 TYR A C 1 ATOM 1342 O O . TYR A 1 170 ? 12.422 79.088 -8.801 1.00 21.38 ? 197 TYR A O 1 ATOM 1343 C CB . TYR A 1 170 ? 11.160 77.474 -6.358 1.00 21.27 ? 197 TYR A CB 1 ATOM 1344 C CG . TYR A 1 170 ? 10.866 77.238 -4.893 1.00 21.98 ? 197 TYR A CG 1 ATOM 1345 C CD1 . TYR A 1 170 ? 11.444 76.175 -4.208 1.00 19.48 ? 197 TYR A CD1 1 ATOM 1346 C CD2 . TYR A 1 170 ? 9.962 78.051 -4.208 1.00 21.65 ? 197 TYR A CD2 1 ATOM 1347 C CE1 . TYR A 1 170 ? 11.157 75.943 -2.873 1.00 24.73 ? 197 TYR A CE1 1 ATOM 1348 C CE2 . TYR A 1 170 ? 9.663 77.829 -2.873 1.00 26.38 ? 197 TYR A CE2 1 ATOM 1349 C CZ . TYR A 1 170 ? 10.262 76.772 -2.210 1.00 29.78 ? 197 TYR A CZ 1 ATOM 1350 O OH . TYR A 1 170 ? 9.978 76.547 -0.882 1.00 28.56 ? 197 TYR A OH 1 ATOM 1351 N N . LYS A 1 171 ? 12.987 76.911 -8.875 1.00 25.18 ? 198 LYS A N 1 ATOM 1352 C CA . LYS A 1 171 ? 12.695 76.742 -10.284 1.00 27.34 ? 198 LYS A CA 1 ATOM 1353 C C . LYS A 1 171 ? 11.908 75.444 -10.413 1.00 29.24 ? 198 LYS A C 1 ATOM 1354 O O . LYS A 1 171 ? 12.484 74.359 -10.363 1.00 29.37 ? 198 LYS A O 1 ATOM 1355 C CB . LYS A 1 171 ? 13.975 76.693 -11.118 1.00 27.73 ? 198 LYS A CB 1 ATOM 1356 C CG . LYS A 1 171 ? 13.714 76.581 -12.609 1.00 30.62 ? 198 LYS A CG 1 ATOM 1357 C CD . LYS A 1 171 ? 15.010 76.552 -13.402 1.00 41.34 ? 198 LYS A CD 1 ATOM 1358 C CE . LYS A 1 171 ? 14.740 76.411 -14.891 1.00 52.42 ? 198 LYS A CE 1 ATOM 1359 N NZ . LYS A 1 171 ? 13.862 77.500 -15.412 1.00 58.97 ? 198 LYS A NZ 1 ATOM 1360 N N . VAL A 1 172 ? 10.588 75.556 -10.548 1.00 28.99 ? 199 VAL A N 1 ATOM 1361 C CA . VAL A 1 172 ? 9.741 74.366 -10.600 1.00 27.80 ? 199 VAL A CA 1 ATOM 1362 C C . VAL A 1 172 ? 10.269 73.339 -11.608 1.00 26.77 ? 199 VAL A C 1 ATOM 1363 O O . VAL A 1 172 ? 10.606 73.671 -12.743 1.00 25.38 ? 199 VAL A O 1 ATOM 1364 C CB . VAL A 1 172 ? 8.248 74.694 -10.876 1.00 30.46 ? 199 VAL A CB 1 ATOM 1365 C CG1 . VAL A 1 172 ? 8.087 75.449 -12.187 1.00 29.50 ? 199 VAL A CG1 1 ATOM 1366 C CG2 . VAL A 1 172 ? 7.425 73.410 -10.881 1.00 30.41 ? 199 VAL A CG2 1 ATOM 1367 N N . SER A 1 173 ? 10.354 72.093 -11.160 1.00 29.83 ? 200 SER A N 1 ATOM 1368 C CA . SER A 1 173 ? 10.929 71.013 -11.945 1.00 29.93 ? 200 SER A CA 1 ATOM 1369 C C . SER A 1 173 ? 9.869 70.281 -12.765 1.00 39.16 ? 200 SER A C 1 ATOM 1370 O O . SER A 1 173 ? 8.698 70.217 -12.379 1.00 39.17 ? 200 SER A O 1 ATOM 1371 C CB . SER A 1 173 ? 11.624 70.023 -11.014 1.00 29.16 ? 200 SER A CB 1 ATOM 1372 O OG . SER A 1 173 ? 12.138 68.920 -11.733 1.00 39.15 ? 200 SER A OG 1 ATOM 1373 N N . ASN A 1 174 ? 10.287 69.726 -13.897 1.00 45.19 ? 201 ASN A N 1 ATOM 1374 C CA . ASN A 1 174 ? 9.408 68.867 -14.682 1.00 48.85 ? 201 ASN A CA 1 ATOM 1375 C C . ASN A 1 174 ? 9.311 67.466 -14.069 1.00 41.61 ? 201 ASN A C 1 ATOM 1376 O O . ASN A 1 174 ? 8.435 66.679 -14.434 1.00 46.56 ? 201 ASN A O 1 ATOM 1377 C CB . ASN A 1 174 ? 9.863 68.798 -16.140 1.00 58.90 ? 201 ASN A CB 1 ATOM 1378 C CG . ASN A 1 174 ? 11.192 68.085 -16.305 1.00 72.17 ? 201 ASN A CG 1 ATOM 1379 O OD1 . ASN A 1 174 ? 12.164 68.370 -15.603 1.00 72.76 ? 201 ASN A OD1 1 ATOM 1380 N ND2 . ASN A 1 174 ? 11.237 67.146 -17.238 1.00 83.25 ? 201 ASN A ND2 1 ATOM 1381 N N . TYR A 1 175 ? 10.207 67.173 -13.129 1.00 33.21 ? 202 TYR A N 1 ATOM 1382 C CA . TYR A 1 175 ? 10.174 65.916 -12.385 1.00 38.21 ? 202 TYR A CA 1 ATOM 1383 C C . TYR A 1 175 ? 9.124 65.941 -11.277 1.00 37.31 ? 202 TYR A C 1 ATOM 1384 O O . TYR A 1 175 ? 8.759 67.002 -10.777 1.00 39.00 ? 202 TYR A O 1 ATOM 1385 C CB . TYR A 1 175 ? 11.544 65.600 -11.770 1.00 40.55 ? 202 TYR A CB 1 ATOM 1386 C CG . TYR A 1 175 ? 12.634 65.280 -12.769 1.00 45.29 ? 202 TYR A CG 1 ATOM 1387 C CD1 . TYR A 1 175 ? 12.642 64.072 -13.462 1.00 50.68 ? 202 TYR A CD1 1 ATOM 1388 C CD2 . TYR A 1 175 ? 13.667 66.177 -13.004 1.00 51.55 ? 202 TYR A CD2 1 ATOM 1389 C CE1 . TYR A 1 175 ? 13.644 63.777 -14.371 1.00 55.21 ? 202 TYR A CE1 1 ATOM 1390 C CE2 . TYR A 1 175 ? 14.672 65.892 -13.908 1.00 58.19 ? 202 TYR A CE2 1 ATOM 1391 C CZ . TYR A 1 175 ? 14.657 64.693 -14.589 1.00 62.38 ? 202 TYR A CZ 1 ATOM 1392 O OH . TYR A 1 175 ? 15.662 64.418 -15.489 1.00 68.03 ? 202 TYR A OH 1 ATOM 1393 N N . SER A 1 176 ? 8.669 64.757 -10.882 1.00 39.31 ? 203 SER A N 1 ATOM 1394 C CA . SER A 1 176 ? 7.632 64.609 -9.866 1.00 42.22 ? 203 SER A CA 1 ATOM 1395 C C . SER A 1 176 ? 8.189 63.924 -8.618 1.00 42.38 ? 203 SER A C 1 ATOM 1396 O O . SER A 1 176 ? 9.265 63.329 -8.661 1.00 46.07 ? 203 SER A O 1 ATOM 1397 C CB . SER A 1 176 ? 6.472 63.780 -10.431 1.00 46.61 ? 203 SER A CB 1 ATOM 1398 O OG . SER A 1 176 ? 5.952 64.347 -11.626 1.00 42.37 ? 203 SER A OG 1 ATOM 1399 N N . ARG A 1 177 ? 7.456 64.004 -7.510 1.00 40.78 ? 204 ARG A N 1 ATOM 1400 C CA . ARG A 1 177 ? 7.849 63.317 -6.279 1.00 38.84 ? 204 ARG A CA 1 ATOM 1401 C C . ARG A 1 177 ? 8.175 61.845 -6.541 1.00 40.58 ? 204 ARG A C 1 ATOM 1402 O O . ARG A 1 177 ? 7.486 61.170 -7.308 1.00 41.45 ? 204 ARG A O 1 ATOM 1403 C CB . ARG A 1 177 ? 6.745 63.420 -5.221 1.00 33.85 ? 204 ARG A CB 1 ATOM 1404 C CG . ARG A 1 177 ? 6.583 64.796 -4.612 1.00 36.33 ? 204 ARG A CG 1 ATOM 1405 C CD . ARG A 1 177 ? 5.514 64.817 -3.519 1.00 38.05 ? 204 ARG A CD 1 ATOM 1406 N NE . ARG A 1 177 ? 5.586 66.056 -2.751 1.00 37.62 ? 204 ARG A NE 1 ATOM 1407 C CZ . ARG A 1 177 ? 5.041 66.248 -1.554 1.00 37.50 ? 204 ARG A CZ 1 ATOM 1408 N NH1 . ARG A 1 177 ? 4.359 65.279 -0.960 1.00 39.64 ? 204 ARG A NH1 1 ATOM 1409 N NH2 . ARG A 1 177 ? 5.187 67.419 -0.946 1.00 29.78 ? 204 ARG A NH2 1 ATOM 1410 N N . GLY A 1 178 ? 9.224 61.350 -5.895 1.00 40.38 ? 205 GLY A N 1 ATOM 1411 C CA . GLY A 1 178 ? 9.630 59.967 -6.066 1.00 42.62 ? 205 GLY A CA 1 ATOM 1412 C C . GLY A 1 178 ? 10.665 59.794 -7.160 1.00 40.74 ? 205 GLY A C 1 ATOM 1413 O O . GLY A 1 178 ? 11.315 58.755 -7.254 1.00 44.44 ? 205 GLY A O 1 ATOM 1414 N N . SER A 1 179 ? 10.829 60.821 -7.986 1.00 36.96 ? 206 SER A N 1 ATOM 1415 C CA . SER A 1 179 ? 11.797 60.767 -9.072 1.00 33.18 ? 206 SER A CA 1 ATOM 1416 C C . SER A 1 179 ? 13.222 60.719 -8.537 1.00 38.10 ? 206 SER A C 1 ATOM 1417 O O . SER A 1 179 ? 14.121 60.201 -9.197 1.00 42.45 ? 206 SER A O 1 ATOM 1418 C CB . SER A 1 179 ? 11.638 61.976 -9.992 1.00 31.81 ? 206 SER A CB 1 ATOM 1419 O OG . SER A 1 179 ? 12.076 63.157 -9.346 1.00 34.26 ? 206 SER A OG 1 ATOM 1420 N N . GLY A 1 180 ? 13.419 61.267 -7.341 1.00 37.94 ? 207 GLY A N 1 ATOM 1421 C CA . GLY A 1 180 ? 14.744 61.410 -6.769 1.00 29.43 ? 207 GLY A CA 1 ATOM 1422 C C . GLY A 1 180 ? 15.462 62.624 -7.330 1.00 34.84 ? 207 GLY A C 1 ATOM 1423 O O . GLY A 1 180 ? 16.647 62.833 -7.071 1.00 33.47 ? 207 GLY A O 1 ATOM 1424 N N . ARG A 1 181 ? 14.742 63.433 -8.103 1.00 34.62 ? 208 ARG A N 1 ATOM 1425 C CA . ARG A 1 181 ? 15.361 64.544 -8.813 1.00 35.59 ? 208 ARG A CA 1 ATOM 1426 C C . ARG A 1 181 ? 14.665 65.885 -8.600 1.00 30.62 ? 208 ARG A C 1 ATOM 1427 O O . ARG A 1 181 ? 14.956 66.852 -9.299 1.00 29.31 ? 208 ARG A O 1 ATOM 1428 C CB . ARG A 1 181 ? 15.461 64.235 -10.307 1.00 43.05 ? 208 ARG A CB 1 ATOM 1429 C CG . ARG A 1 181 ? 16.274 62.991 -10.617 1.00 50.83 ? 208 ARG A CG 1 ATOM 1430 C CD . ARG A 1 181 ? 16.673 62.946 -12.076 1.00 61.46 ? 208 ARG A CD 1 ATOM 1431 N NE . ARG A 1 181 ? 17.418 61.733 -12.396 1.00 69.70 ? 208 ARG A NE 1 ATOM 1432 C CZ . ARG A 1 181 ? 18.011 61.508 -13.564 1.00 73.79 ? 208 ARG A CZ 1 ATOM 1433 N NH1 . ARG A 1 181 ? 17.951 62.418 -14.526 1.00 72.58 ? 208 ARG A NH1 1 ATOM 1434 N NH2 . ARG A 1 181 ? 18.669 60.375 -13.767 1.00 79.16 ? 208 ARG A NH2 1 ATOM 1435 N N . CYS A 1 182 ? 13.750 65.949 -7.641 1.00 24.63 ? 209 CYS A N 1 ATOM 1436 C CA . CYS A 1 182 ? 13.154 67.237 -7.283 1.00 28.20 ? 209 CYS A CA 1 ATOM 1437 C C . CYS A 1 182 ? 12.980 67.369 -5.774 1.00 26.78 ? 209 CYS A C 1 ATOM 1438 O O . CYS A 1 182 ? 12.818 66.378 -5.065 1.00 30.43 ? 209 CYS A O 1 ATOM 1439 C CB . CYS A 1 182 ? 11.828 67.475 -8.026 1.00 22.52 ? 209 CYS A CB 1 ATOM 1440 S SG . CYS A 1 182 ? 10.525 66.269 -7.683 1.00 27.84 ? 209 CYS A SG 1 ATOM 1441 N N . ILE A 1 183 ? 13.034 68.601 -5.289 1.00 27.04 ? 210 ILE A N 1 ATOM 1442 C CA . ILE A 1 183 ? 12.923 68.868 -3.866 1.00 27.57 ? 210 ILE A CA 1 ATOM 1443 C C . ILE A 1 183 ? 11.458 68.989 -3.434 1.00 30.23 ? 210 ILE A C 1 ATOM 1444 O O . ILE A 1 183 ? 10.680 69.727 -4.036 1.00 26.98 ? 210 ILE A O 1 ATOM 1445 C CB . ILE A 1 183 ? 13.696 70.145 -3.489 1.00 23.94 ? 210 ILE A CB 1 ATOM 1446 C CG1 . ILE A 1 183 ? 15.204 69.924 -3.673 1.00 26.61 ? 210 ILE A CG1 1 ATOM 1447 C CG2 . ILE A 1 183 ? 13.376 70.567 -2.066 1.00 20.15 ? 210 ILE A CG2 1 ATOM 1448 C CD1 . ILE A 1 183 ? 15.841 68.997 -2.642 1.00 25.78 ? 210 ILE A CD1 1 ATOM 1449 N N . GLN A 1 184 ? 11.104 68.242 -2.391 1.00 34.38 ? 211 GLN A N 1 ATOM 1450 C CA . GLN A 1 184 ? 9.768 68.253 -1.796 1.00 34.95 ? 211 GLN A CA 1 ATOM 1451 C C . GLN A 1 184 ? 9.672 69.280 -0.686 1.00 28.06 ? 211 GLN A C 1 ATOM 1452 O O . GLN A 1 184 ? 10.620 69.464 0.072 1.00 30.42 ? 211 GLN A O 1 ATOM 1453 C CB . GLN A 1 184 ? 9.483 66.900 -1.170 1.00 39.84 ? 211 GLN A CB 1 ATOM 1454 C CG . GLN A 1 184 ? 8.644 65.989 -1.989 1.00 46.01 ? 211 GLN A CG 1 ATOM 1455 C CD . GLN A 1 184 ? 8.645 64.598 -1.412 1.00 45.14 ? 211 GLN A CD 1 ATOM 1456 O OE1 . GLN A 1 184 ? 9.467 63.767 -1.788 1.00 54.09 ? 211 GLN A OE1 1 ATOM 1457 N NE2 . GLN A 1 184 ? 7.745 64.343 -0.470 1.00 37.18 ? 211 GLN A NE2 1 ATOM 1458 N N . MET A 1 185 ? 8.503 69.898 -0.559 1.00 28.60 ? 212 MET A N 1 ATOM 1459 C CA . MET A 1 185 ? 8.269 70.974 0.404 1.00 33.25 ? 212 MET A CA 1 ATOM 1460 C C . MET A 1 185 ? 7.809 70.418 1.758 1.00 33.57 ? 212 MET A C 1 ATOM 1461 O O . MET A 1 185 ? 7.733 71.142 2.756 1.00 28.94 ? 212 MET A O 1 ATOM 1462 C CB . MET A 1 185 ? 7.203 71.922 -0.158 1.00 36.22 ? 212 MET A CB 1 ATOM 1463 C CG . MET A 1 185 ? 7.365 73.379 0.213 1.00 46.82 ? 212 MET A CG 1 ATOM 1464 S SD . MET A 1 185 ? 6.076 74.407 -0.538 1.00 41.66 ? 212 MET A SD 1 ATOM 1465 C CE . MET A 1 185 ? 6.407 74.116 -2.270 1.00 18.71 ? 212 MET A CE 1 ATOM 1466 N N . TRP A 1 186 ? 7.494 69.126 1.778 1.00 27.98 ? 213 TRP A N 1 ATOM 1467 C CA . TRP A 1 186 ? 6.982 68.471 2.974 1.00 26.47 ? 213 TRP A CA 1 ATOM 1468 C C . TRP A 1 186 ? 7.054 66.971 2.748 1.00 32.89 ? 213 TRP A C 1 ATOM 1469 O O . TRP A 1 186 ? 7.131 66.514 1.607 1.00 33.29 ? 213 TRP A O 1 ATOM 1470 C CB . TRP A 1 186 ? 5.529 68.893 3.223 1.00 28.74 ? 213 TRP A CB 1 ATOM 1471 C CG . TRP A 1 186 ? 5.031 68.680 4.626 1.00 30.98 ? 213 TRP A CG 1 ATOM 1472 C CD1 . TRP A 1 186 ? 4.327 67.603 5.094 1.00 35.38 ? 213 TRP A CD1 1 ATOM 1473 C CD2 . TRP A 1 186 ? 5.180 69.574 5.740 1.00 31.38 ? 213 TRP A CD2 1 ATOM 1474 N NE1 . TRP A 1 186 ? 4.036 67.770 6.426 1.00 32.08 ? 213 TRP A NE1 1 ATOM 1475 C CE2 . TRP A 1 186 ? 4.546 68.972 6.847 1.00 32.51 ? 213 TRP A CE2 1 ATOM 1476 C CE3 . TRP A 1 186 ? 5.790 70.823 5.909 1.00 29.67 ? 213 TRP A CE3 1 ATOM 1477 C CZ2 . TRP A 1 186 ? 4.505 69.578 8.107 1.00 29.78 ? 213 TRP A CZ2 1 ATOM 1478 C CZ3 . TRP A 1 186 ? 5.748 71.421 7.158 1.00 25.39 ? 213 TRP A CZ3 1 ATOM 1479 C CH2 . TRP A 1 186 ? 5.114 70.798 8.240 1.00 25.69 ? 213 TRP A CH2 1 ATOM 1480 N N . PHE A 1 187 ? 7.022 66.205 3.833 1.00 33.43 ? 214 PHE A N 1 ATOM 1481 C CA . PHE A 1 187 ? 7.106 64.755 3.744 1.00 32.41 ? 214 PHE A CA 1 ATOM 1482 C C . PHE A 1 187 ? 6.826 64.131 5.101 1.00 38.44 ? 214 PHE A C 1 ATOM 1483 O O . PHE A 1 187 ? 6.805 64.820 6.121 1.00 39.97 ? 214 PHE A O 1 ATOM 1484 C CB . PHE A 1 187 ? 8.497 64.334 3.265 1.00 31.83 ? 214 PHE A CB 1 ATOM 1485 C CG . PHE A 1 187 ? 9.608 64.804 4.161 1.00 29.29 ? 214 PHE A CG 1 ATOM 1486 C CD1 . PHE A 1 187 ? 10.062 64.009 5.201 1.00 31.73 ? 214 PHE A CD1 1 ATOM 1487 C CD2 . PHE A 1 187 ? 10.185 66.052 3.976 1.00 30.65 ? 214 PHE A CD2 1 ATOM 1488 C CE1 . PHE A 1 187 ? 11.081 64.444 6.037 1.00 33.43 ? 214 PHE A CE1 1 ATOM 1489 C CE2 . PHE A 1 187 ? 11.204 66.493 4.807 1.00 27.71 ? 214 PHE A CE2 1 ATOM 1490 C CZ . PHE A 1 187 ? 11.651 65.688 5.838 1.00 29.20 ? 214 PHE A CZ 1 ATOM 1491 N N . ASP A 1 188 ? 6.617 62.821 5.101 1.00 38.54 ? 215 ASP A N 1 ATOM 1492 C CA . ASP A 1 188 ? 6.440 62.060 6.328 1.00 36.78 ? 215 ASP A CA 1 ATOM 1493 C C . ASP A 1 188 ? 7.807 61.533 6.750 1.00 43.28 ? 215 ASP A C 1 ATOM 1494 O O . ASP A 1 188 ? 8.353 60.639 6.104 1.00 42.79 ? 215 ASP A O 1 ATOM 1495 C CB . ASP A 1 188 ? 5.479 60.901 6.071 1.00 42.34 ? 215 ASP A CB 1 ATOM 1496 C CG . ASP A 1 188 ? 5.145 60.115 7.327 1.00 48.06 ? 215 ASP A CG 1 ATOM 1497 O OD1 . ASP A 1 188 ? 5.772 60.351 8.381 1.00 46.90 ? 215 ASP A OD1 1 ATOM 1498 O OD2 . ASP A 1 188 ? 4.252 59.245 7.248 1.00 54.78 ? 215 ASP A OD2 1 ATOM 1499 N N . PRO A 1 189 ? 8.370 62.097 7.830 1.00 46.54 ? 216 PRO A N 1 ATOM 1500 C CA . PRO A 1 189 ? 9.724 61.757 8.290 1.00 42.00 ? 216 PRO A CA 1 ATOM 1501 C C . PRO A 1 189 ? 9.867 60.305 8.761 1.00 45.30 ? 216 PRO A C 1 ATOM 1502 O O . PRO A 1 189 ? 10.982 59.776 8.782 1.00 44.01 ? 216 PRO A O 1 ATOM 1503 C CB . PRO A 1 189 ? 9.953 62.727 9.457 1.00 39.07 ? 216 PRO A CB 1 ATOM 1504 C CG . PRO A 1 189 ? 8.583 63.058 9.943 1.00 43.86 ? 216 PRO A CG 1 ATOM 1505 C CD . PRO A 1 189 ? 7.720 63.085 8.710 1.00 44.77 ? 216 PRO A CD 1 ATOM 1506 N N . ALA A 1 190 ? 8.762 59.669 9.135 1.00 51.06 ? 217 ALA A N 1 ATOM 1507 C CA . ALA A 1 190 ? 8.806 58.263 9.532 1.00 55.14 ? 217 ALA A CA 1 ATOM 1508 C C . ALA A 1 190 ? 9.228 57.399 8.349 1.00 57.23 ? 217 ALA A C 1 ATOM 1509 O O . ALA A 1 190 ? 9.744 56.295 8.524 1.00 55.42 ? 217 ALA A O 1 ATOM 1510 C CB . ALA A 1 190 ? 7.458 57.809 10.069 1.00 54.60 ? 217 ALA A CB 1 ATOM 1511 N N . GLN A 1 191 ? 9.007 57.915 7.144 1.00 55.34 ? 218 GLN A N 1 ATOM 1512 C CA . GLN A 1 191 ? 9.375 57.204 5.928 1.00 58.17 ? 218 GLN A CA 1 ATOM 1513 C C . GLN A 1 191 ? 10.685 57.745 5.352 1.00 56.63 ? 218 GLN A C 1 ATOM 1514 O O . GLN A 1 191 ? 10.954 57.600 4.161 1.00 60.14 ? 218 GLN A O 1 ATOM 1515 C CB . GLN A 1 191 ? 8.255 57.311 4.890 1.00 59.91 ? 218 GLN A CB 1 ATOM 1516 C CG . GLN A 1 191 ? 6.848 57.121 5.458 1.00 67.01 ? 218 GLN A CG 1 ATOM 1517 C CD . GLN A 1 191 ? 6.647 55.760 6.101 1.00 74.64 ? 218 GLN A CD 1 ATOM 1518 O OE1 . GLN A 1 191 ? 7.378 54.812 5.815 1.00 78.53 ? 218 GLN A OE1 1 ATOM 1519 N NE2 . GLN A 1 191 ? 5.653 55.659 6.979 1.00 76.52 ? 218 GLN A NE2 1 ATOM 1520 N N . GLY A 1 192 ? 11.498 58.362 6.205 1.00 49.65 ? 219 GLY A N 1 ATOM 1521 C CA . GLY A 1 192 ? 12.745 58.969 5.770 1.00 48.23 ? 219 GLY A CA 1 ATOM 1522 C C . GLY A 1 192 ? 12.585 60.362 5.173 1.00 47.12 ? 219 GLY A C 1 ATOM 1523 O O . GLY A 1 192 ? 11.466 60.837 4.961 1.00 50.24 ? 219 GLY A O 1 ATOM 1524 N N . ASN A 1 193 ? 13.713 61.016 4.906 1.00 44.93 ? 220 ASN A N 1 ATOM 1525 C CA . ASN A 1 193 ? 13.728 62.331 4.265 1.00 39.86 ? 220 ASN A CA 1 ATOM 1526 C C . ASN A 1 193 ? 14.111 62.203 2.790 1.00 38.05 ? 220 ASN A C 1 ATOM 1527 O O . ASN A 1 193 ? 15.275 61.995 2.461 1.00 38.56 ? 220 ASN A O 1 ATOM 1528 C CB . ASN A 1 193 ? 14.705 63.265 4.991 1.00 38.70 ? 220 ASN A CB 1 ATOM 1529 C CG . ASN A 1 193 ? 14.642 64.702 4.488 1.00 43.01 ? 220 ASN A CG 1 ATOM 1530 O OD1 . ASN A 1 193 ? 14.365 64.958 3.313 1.00 38.73 ? 220 ASN A OD1 1 ATOM 1531 N ND2 . ASN A 1 193 ? 14.905 65.650 5.385 1.00 42.01 ? 220 ASN A ND2 1 ATOM 1532 N N . PRO A 1 194 ? 13.127 62.338 1.895 1.00 38.16 ? 221 PRO A N 1 ATOM 1533 C CA . PRO A 1 194 ? 13.334 62.112 0.458 1.00 38.81 ? 221 PRO A CA 1 ATOM 1534 C C . PRO A 1 194 ? 14.276 63.117 -0.223 1.00 39.34 ? 221 PRO A C 1 ATOM 1535 O O . PRO A 1 194 ? 14.812 62.816 -1.287 1.00 35.92 ? 221 PRO A O 1 ATOM 1536 C CB . PRO A 1 194 ? 11.917 62.236 -0.118 1.00 37.57 ? 221 PRO A CB 1 ATOM 1537 C CG . PRO A 1 194 ? 11.198 63.117 0.846 1.00 35.34 ? 221 PRO A CG 1 ATOM 1538 C CD . PRO A 1 194 ? 11.748 62.763 2.197 1.00 37.45 ? 221 PRO A CD 1 ATOM 1539 N N . ASN A 1 195 ? 14.480 64.290 0.368 1.00 37.20 ? 222 ASN A N 1 ATOM 1540 C CA . ASN A 1 195 ? 15.307 65.299 -0.286 1.00 30.46 ? 222 ASN A CA 1 ATOM 1541 C C . ASN A 1 195 ? 16.807 65.084 -0.095 1.00 30.61 ? 222 ASN A C 1 ATOM 1542 O O . ASN A 1 195 ? 17.616 65.713 -0.775 1.00 30.07 ? 222 ASN A O 1 ATOM 1543 C CB . ASN A 1 195 ? 14.908 66.709 0.144 1.00 30.19 ? 222 ASN A CB 1 ATOM 1544 C CG . ASN A 1 195 ? 13.505 67.091 -0.313 1.00 34.05 ? 222 ASN A CG 1 ATOM 1545 O OD1 . ASN A 1 195 ? 13.075 66.732 -1.408 1.00 36.91 ? 222 ASN A OD1 1 ATOM 1546 N ND2 . ASN A 1 195 ? 12.787 67.819 0.531 1.00 27.84 ? 222 ASN A ND2 1 ATOM 1547 N N . GLU A 1 196 ? 17.174 64.193 0.823 1.00 30.21 ? 223 GLU A N 1 ATOM 1548 C CA . GLU A 1 196 ? 18.583 63.861 1.047 1.00 35.88 ? 223 GLU A CA 1 ATOM 1549 C C . GLU A 1 196 ? 19.249 63.257 -0.188 1.00 38.98 ? 223 GLU A C 1 ATOM 1550 O O . GLU A 1 196 ? 20.363 63.637 -0.549 1.00 38.75 ? 223 GLU A O 1 ATOM 1551 C CB . GLU A 1 196 ? 18.742 62.918 2.244 1.00 37.67 ? 223 GLU A CB 1 ATOM 1552 C CG . GLU A 1 196 ? 18.441 63.577 3.582 1.00 48.71 ? 223 GLU A CG 1 ATOM 1553 C CD . GLU A 1 196 ? 18.422 62.589 4.733 1.00 51.49 ? 223 GLU A CD 1 ATOM 1554 O OE1 . GLU A 1 196 ? 18.886 61.445 4.549 1.00 53.94 ? 223 GLU A OE1 1 ATOM 1555 O OE2 . GLU A 1 196 ? 17.936 62.959 5.821 1.00 47.51 ? 223 GLU A OE2 1 ATOM 1556 N N . GLU A 1 197 ? 18.568 62.314 -0.831 1.00 38.42 ? 224 GLU A N 1 ATOM 1557 C CA . GLU A 1 197 ? 19.088 61.710 -2.052 1.00 39.16 ? 224 GLU A CA 1 ATOM 1558 C C . GLU A 1 197 ? 19.036 62.691 -3.222 1.00 35.42 ? 224 GLU A C 1 ATOM 1559 O O . GLU A 1 197 ? 19.872 62.632 -4.124 1.00 36.34 ? 224 GLU A O 1 ATOM 1560 C CB . GLU A 1 197 ? 18.331 60.422 -2.397 1.00 46.74 ? 224 GLU A CB 1 ATOM 1561 C CG . GLU A 1 197 ? 18.842 59.731 -3.654 1.00 56.53 ? 224 GLU A CG 1 ATOM 1562 C CD . GLU A 1 197 ? 20.358 59.539 -3.648 1.00 65.49 ? 224 GLU A CD 1 ATOM 1563 O OE1 . GLU A 1 197 ? 20.903 59.069 -2.619 1.00 64.24 ? 224 GLU A OE1 1 ATOM 1564 O OE2 . GLU A 1 197 ? 21.003 59.866 -4.673 1.00 66.06 ? 224 GLU A OE2 1 ATOM 1565 N N . VAL A 1 198 ? 18.049 63.584 -3.207 1.00 28.46 ? 225 VAL A N 1 ATOM 1566 C CA . VAL A 1 198 ? 17.947 64.632 -4.220 1.00 29.86 ? 225 VAL A CA 1 ATOM 1567 C C . VAL A 1 198 ? 19.136 65.596 -4.123 1.00 32.26 ? 225 VAL A C 1 ATOM 1568 O O . VAL A 1 198 ? 19.740 65.965 -5.130 1.00 32.23 ? 225 VAL A O 1 ATOM 1569 C CB . VAL A 1 198 ? 16.617 65.416 -4.106 1.00 31.54 ? 225 VAL A CB 1 ATOM 1570 C CG1 . VAL A 1 198 ? 16.524 66.471 -5.202 1.00 26.46 ? 225 VAL A CG1 1 ATOM 1571 C CG2 . VAL A 1 198 ? 15.416 64.460 -4.167 1.00 31.00 ? 225 VAL A CG2 1 ATOM 1572 N N . ALA A 1 199 ? 19.476 65.997 -2.904 1.00 32.26 ? 226 ALA A N 1 ATOM 1573 C CA . ALA A 1 199 ? 20.647 66.838 -2.690 1.00 28.98 ? 226 ALA A CA 1 ATOM 1574 C C . ALA A 1 199 ? 21.918 66.108 -3.132 1.00 31.34 ? 226 ALA A C 1 ATOM 1575 O O . ALA A 1 199 ? 22.755 66.673 -3.840 1.00 30.38 ? 226 ALA A O 1 ATOM 1576 C CB . ALA A 1 199 ? 20.746 67.258 -1.225 1.00 26.97 ? 226 ALA A CB 1 ATOM 1577 N N . ARG A 1 200 ? 22.055 64.848 -2.721 1.00 27.43 ? 227 ARG A N 1 ATOM 1578 C CA . ARG A 1 200 ? 23.220 64.059 -3.096 1.00 28.45 ? 227 ARG A CA 1 ATOM 1579 C C . ARG A 1 200 ? 23.335 63.966 -4.614 1.00 33.29 ? 227 ARG A C 1 ATOM 1580 O O . ARG A 1 200 ? 24.424 64.078 -5.178 1.00 36.38 ? 227 ARG A O 1 ATOM 1581 C CB . ARG A 1 200 ? 23.166 62.664 -2.462 1.00 33.81 ? 227 ARG A CB 1 ATOM 1582 N N . PHE A 1 201 ? 22.200 63.774 -5.274 1.00 31.76 ? 228 PHE A N 1 ATOM 1583 C CA . PHE A 1 201 ? 22.176 63.661 -6.726 1.00 33.00 ? 228 PHE A CA 1 ATOM 1584 C C . PHE A 1 201 ? 22.725 64.915 -7.414 1.00 31.43 ? 228 PHE A C 1 ATOM 1585 O O . PHE A 1 201 ? 23.595 64.828 -8.281 1.00 31.68 ? 228 PHE A O 1 ATOM 1586 C CB . PHE A 1 201 ? 20.757 63.376 -7.221 1.00 30.90 ? 228 PHE A CB 1 ATOM 1587 C CG . PHE A 1 201 ? 20.636 63.388 -8.711 1.00 32.52 ? 228 PHE A CG 1 ATOM 1588 C CD1 . PHE A 1 201 ? 20.945 62.257 -9.452 1.00 36.32 ? 228 PHE A CD1 1 ATOM 1589 C CD2 . PHE A 1 201 ? 20.235 64.534 -9.376 1.00 32.29 ? 228 PHE A CD2 1 ATOM 1590 C CE1 . PHE A 1 201 ? 20.844 62.269 -10.829 1.00 40.25 ? 228 PHE A CE1 1 ATOM 1591 C CE2 . PHE A 1 201 ? 20.136 64.555 -10.751 1.00 35.85 ? 228 PHE A CE2 1 ATOM 1592 C CZ . PHE A 1 201 ? 20.440 63.424 -11.481 1.00 39.59 ? 228 PHE A CZ 1 ATOM 1593 N N . TYR A 1 202 ? 22.210 66.077 -7.025 1.00 27.88 ? 229 TYR A N 1 ATOM 1594 C CA . TYR A 1 202 ? 22.620 67.340 -7.638 1.00 29.83 ? 229 TYR A CA 1 ATOM 1595 C C . TYR A 1 202 ? 24.034 67.780 -7.274 1.00 31.08 ? 229 TYR A C 1 ATOM 1596 O O . TYR A 1 202 ? 24.712 68.411 -8.077 1.00 31.89 ? 229 TYR A O 1 ATOM 1597 C CB . TYR A 1 202 ? 21.595 68.439 -7.349 1.00 25.95 ? 229 TYR A CB 1 ATOM 1598 C CG . TYR A 1 202 ? 20.361 68.265 -8.190 1.00 28.30 ? 229 TYR A CG 1 ATOM 1599 C CD1 . TYR A 1 202 ? 20.377 68.583 -9.537 1.00 30.61 ? 229 TYR A CD1 1 ATOM 1600 C CD2 . TYR A 1 202 ? 19.196 67.734 -7.654 1.00 30.19 ? 229 TYR A CD2 1 ATOM 1601 C CE1 . TYR A 1 202 ? 19.256 68.404 -10.328 1.00 37.20 ? 229 TYR A CE1 1 ATOM 1602 C CE2 . TYR A 1 202 ? 18.066 67.550 -8.437 1.00 33.84 ? 229 TYR A CE2 1 ATOM 1603 C CZ . TYR A 1 202 ? 18.104 67.890 -9.775 1.00 35.10 ? 229 TYR A CZ 1 ATOM 1604 O OH . TYR A 1 202 ? 16.994 67.716 -10.566 1.00 38.62 ? 229 TYR A OH 1 ATOM 1605 N N . ALA A 1 203 ? 24.474 67.434 -6.070 1.00 30.40 ? 230 ALA A N 1 ATOM 1606 C CA . ALA A 1 203 ? 25.845 67.690 -5.658 1.00 29.40 ? 230 ALA A CA 1 ATOM 1607 C C . ALA A 1 203 ? 26.826 66.909 -6.536 1.00 37.43 ? 230 ALA A C 1 ATOM 1608 O O . ALA A 1 203 ? 27.935 67.370 -6.814 1.00 42.05 ? 230 ALA A O 1 ATOM 1609 C CB . ALA A 1 203 ? 26.032 67.328 -4.189 1.00 28.85 ? 230 ALA A CB 1 ATOM 1610 N N . ALA A 1 204 ? 26.406 65.723 -6.968 1.00 39.60 ? 231 ALA A N 1 ATOM 1611 C CA . ALA A 1 204 ? 27.239 64.850 -7.790 1.00 38.45 ? 231 ALA A CA 1 ATOM 1612 C C . ALA A 1 204 ? 27.239 65.269 -9.258 1.00 40.99 ? 231 ALA A C 1 ATOM 1613 O O . ALA A 1 204 ? 28.191 64.999 -9.989 1.00 39.63 ? 231 ALA A O 1 ATOM 1614 C CB . ALA A 1 204 ? 26.773 63.402 -7.658 1.00 36.88 ? 231 ALA A CB 1 ATOM 1615 N N . ALA A 1 205 ? 26.164 65.925 -9.685 1.00 44.13 ? 232 ALA A N 1 ATOM 1616 C CA . ALA A 1 205 ? 25.980 66.260 -11.093 1.00 51.02 ? 232 ALA A CA 1 ATOM 1617 C C . ALA A 1 205 ? 26.469 67.666 -11.427 1.00 60.98 ? 232 ALA A C 1 ATOM 1618 O O . ALA A 1 205 ? 26.994 67.910 -12.515 1.00 66.93 ? 232 ALA A O 1 ATOM 1619 C CB . ALA A 1 205 ? 24.519 66.103 -11.484 1.00 50.06 ? 232 ALA A CB 1 ATOM 1620 N N . MET A 1 206 ? 26.293 68.589 -10.487 1.00 59.93 ? 233 MET A N 1 ATOM 1621 C CA . MET A 1 206 ? 26.639 69.984 -10.717 1.00 59.07 ? 233 MET A CA 1 ATOM 1622 C C . MET A 1 206 ? 28.115 70.234 -10.443 1.00 60.98 ? 233 MET A C 1 ATOM 1623 O O . MET A 1 206 ? 28.937 70.193 -11.357 1.00 64.44 ? 233 MET A O 1 ATOM 1624 C CB . MET A 1 206 ? 25.767 70.902 -9.851 1.00 56.12 ? 233 MET A CB 1 ATOM 1625 C CG . MET A 1 206 ? 24.265 70.725 -10.071 1.00 51.53 ? 233 MET A CG 1 ATOM 1626 S SD . MET A 1 206 ? 23.251 71.737 -8.964 1.00 79.56 ? 233 MET A SD 1 ATOM 1627 C CE . MET A 1 206 ? 23.634 73.390 -9.540 1.00 91.95 ? 233 MET A CE 1 HETATM 1628 K K . K B 2 . ? 14.677 68.663 3.363 1.00 32.60 ? 301 K A K 1 HETATM 1629 CL CL . CL C 3 . ? 13.904 87.006 3.644 1.00 29.37 ? 302 CL A CL 1 HETATM 1630 C C1 . NAG D 4 . ? 3.719 103.012 4.220 1.00 34.14 ? 303 NAG A C1 1 HETATM 1631 C C2 . NAG D 4 . ? 3.533 104.021 3.099 1.00 33.91 ? 303 NAG A C2 1 HETATM 1632 C C3 . NAG D 4 . ? 3.536 105.417 3.694 1.00 39.53 ? 303 NAG A C3 1 HETATM 1633 C C4 . NAG D 4 . ? 2.438 105.524 4.747 1.00 45.09 ? 303 NAG A C4 1 HETATM 1634 C C5 . NAG D 4 . ? 2.378 104.339 5.713 1.00 47.28 ? 303 NAG A C5 1 HETATM 1635 C C6 . NAG D 4 . ? 0.990 104.310 6.346 1.00 52.00 ? 303 NAG A C6 1 HETATM 1636 C C7 . NAG D 4 . ? 4.302 103.264 0.936 1.00 34.58 ? 303 NAG A C7 1 HETATM 1637 C C8 . NAG D 4 . ? 5.300 103.443 -0.170 1.00 31.93 ? 303 NAG A C8 1 HETATM 1638 N N2 . NAG D 4 . ? 4.558 103.890 2.083 1.00 28.76 ? 303 NAG A N2 1 HETATM 1639 O O3 . NAG D 4 . ? 3.303 106.341 2.655 1.00 38.26 ? 303 NAG A O3 1 HETATM 1640 O O4 . NAG D 4 . ? 2.625 106.697 5.508 1.00 49.79 ? 303 NAG A O4 1 HETATM 1641 O O5 . NAG D 4 . ? 2.610 103.085 5.095 1.00 42.91 ? 303 NAG A O5 1 HETATM 1642 O O6 . NAG D 4 . ? 0.967 103.445 7.457 1.00 57.64 ? 303 NAG A O6 1 HETATM 1643 O O7 . NAG D 4 . ? 3.303 102.562 0.767 1.00 31.57 ? 303 NAG A O7 1 HETATM 1644 C C1 . NAG E 4 . ? 1.908 107.832 5.085 1.00 55.29 ? 304 NAG A C1 1 HETATM 1645 C C2 . NAG E 4 . ? 1.273 108.763 6.108 1.00 63.13 ? 304 NAG A C2 1 HETATM 1646 C C3 . NAG E 4 . ? 0.794 110.049 5.447 1.00 64.88 ? 304 NAG A C3 1 HETATM 1647 C C4 . NAG E 4 . ? 1.918 110.667 4.623 1.00 65.64 ? 304 NAG A C4 1 HETATM 1648 C C5 . NAG E 4 . ? 2.500 109.631 3.664 1.00 62.52 ? 304 NAG A C5 1 HETATM 1649 C C6 . NAG E 4 . ? 3.680 110.187 2.874 1.00 60.48 ? 304 NAG A C6 1 HETATM 1650 C C7 . NAG E 4 . ? 0.273 107.642 8.009 1.00 64.91 ? 304 NAG A C7 1 HETATM 1651 C C8 . NAG E 4 . ? -0.956 107.000 8.580 1.00 60.39 ? 304 NAG A C8 1 HETATM 1652 N N2 . NAG E 4 . ? 0.168 108.090 6.761 1.00 66.45 ? 304 NAG A N2 1 HETATM 1653 O O3 . NAG E 4 . ? 0.363 110.946 6.445 1.00 67.01 ? 304 NAG A O3 1 HETATM 1654 O O4 . NAG E 4 . ? 1.430 111.772 3.892 1.00 66.80 ? 304 NAG A O4 1 HETATM 1655 O O5 . NAG E 4 . ? 2.933 108.493 4.376 1.00 57.75 ? 304 NAG A O5 1 HETATM 1656 O O6 . NAG E 4 . ? 4.110 109.224 1.935 1.00 58.58 ? 304 NAG A O6 1 HETATM 1657 O O7 . NAG E 4 . ? 1.308 107.735 8.674 1.00 65.34 ? 304 NAG A O7 1 HETATM 1658 C C1 . FUC F 5 . ? -0.097 103.367 8.397 0.83 61.22 ? 305 FUC A C1 1 HETATM 1659 C C2 . FUC F 5 . ? -0.376 101.981 8.967 0.83 61.03 ? 305 FUC A C2 1 HETATM 1660 C C3 . FUC F 5 . ? 0.765 101.537 9.875 0.83 63.26 ? 305 FUC A C3 1 HETATM 1661 C C4 . FUC F 5 . ? 1.084 102.617 10.900 0.83 65.18 ? 305 FUC A C4 1 HETATM 1662 C C5 . FUC F 5 . ? 1.266 103.965 10.210 0.83 65.19 ? 305 FUC A C5 1 HETATM 1663 C C6 . FUC F 5 . ? 1.539 105.077 11.219 0.83 64.60 ? 305 FUC A C6 1 HETATM 1664 O O2 . FUC F 5 . ? -0.527 101.056 7.914 0.83 59.47 ? 305 FUC A O2 1 HETATM 1665 O O3 . FUC F 5 . ? 0.395 100.360 10.552 0.83 65.06 ? 305 FUC A O3 1 HETATM 1666 O O4 . FUC F 5 . ? 0.036 102.693 11.843 0.83 64.00 ? 305 FUC A O4 1 HETATM 1667 O O5 . FUC F 5 . ? 0.107 104.270 9.463 0.83 62.97 ? 305 FUC A O5 1 HETATM 1668 C C1 . NAG G 4 . ? 12.225 66.383 -17.932 0.85 63.80 ? 306 NAG A C1 1 HETATM 1669 C C2 . NAG G 4 . ? 12.060 64.880 -18.141 0.85 66.33 ? 306 NAG A C2 1 HETATM 1670 C C3 . NAG G 4 . ? 13.406 64.171 -18.257 0.85 70.57 ? 306 NAG A C3 1 HETATM 1671 C C4 . NAG G 4 . ? 14.386 64.937 -19.141 0.85 74.00 ? 306 NAG A C4 1 HETATM 1672 C C5 . NAG G 4 . ? 14.413 66.419 -18.785 0.85 72.57 ? 306 NAG A C5 1 HETATM 1673 C C6 . NAG G 4 . ? 15.342 67.187 -19.718 0.85 73.57 ? 306 NAG A C6 1 HETATM 1674 C C7 . NAG G 4 . ? 10.074 63.799 -17.202 0.85 59.20 ? 306 NAG A C7 1 HETATM 1675 C C8 . NAG G 4 . ? 9.524 63.783 -18.598 0.85 56.20 ? 306 NAG A C8 1 HETATM 1676 N N2 . NAG G 4 . ? 11.293 64.315 -17.042 0.85 63.11 ? 306 NAG A N2 1 HETATM 1677 O O3 . NAG G 4 . ? 13.202 62.889 -18.802 0.85 69.86 ? 306 NAG A O3 1 HETATM 1678 O O4 . NAG G 4 . ? 15.682 64.397 -18.989 0.85 75.52 ? 306 NAG A O4 1 HETATM 1679 O O5 . NAG G 4 . ? 13.111 66.953 -18.872 0.85 68.73 ? 306 NAG A O5 1 HETATM 1680 O O6 . NAG G 4 . ? 14.874 67.078 -21.044 0.85 74.86 ? 306 NAG A O6 1 HETATM 1681 O O7 . NAG G 4 . ? 9.408 63.348 -16.268 0.85 57.50 ? 306 NAG A O7 1 HETATM 1682 O O . HOH H 6 . ? 20.840 89.001 -1.605 1.00 12.89 ? 401 HOH A O 1 HETATM 1683 O O . HOH H 6 . ? -6.948 80.053 -1.488 1.00 26.32 ? 402 HOH A O 1 HETATM 1684 O O . HOH H 6 . ? 17.626 75.635 5.374 1.00 21.61 ? 403 HOH A O 1 HETATM 1685 O O . HOH H 6 . ? 4.492 84.782 9.121 1.00 27.04 ? 404 HOH A O 1 HETATM 1686 O O . HOH H 6 . ? 13.556 80.143 -11.000 1.00 27.85 ? 405 HOH A O 1 HETATM 1687 O O . HOH H 6 . ? 10.676 81.714 -6.107 1.00 23.67 ? 406 HOH A O 1 HETATM 1688 O O . HOH H 6 . ? 6.149 92.587 -7.400 1.00 21.56 ? 407 HOH A O 1 HETATM 1689 O O . HOH H 6 . ? 10.398 81.409 2.709 1.00 26.19 ? 408 HOH A O 1 HETATM 1690 O O . HOH H 6 . ? 4.041 96.489 -2.170 1.00 29.40 ? 409 HOH A O 1 HETATM 1691 O O . HOH H 6 . ? 23.247 81.984 1.272 1.00 22.46 ? 410 HOH A O 1 HETATM 1692 O O . HOH H 6 . ? -3.386 87.939 1.350 1.00 21.94 ? 411 HOH A O 1 HETATM 1693 O O . HOH H 6 . ? -1.493 95.092 3.182 1.00 26.33 ? 412 HOH A O 1 HETATM 1694 O O . HOH H 6 . ? 5.976 74.824 25.520 1.00 29.21 ? 413 HOH A O 1 HETATM 1695 O O . HOH H 6 . ? 10.165 94.090 1.380 1.00 21.37 ? 414 HOH A O 1 HETATM 1696 O O . HOH H 6 . ? 16.425 82.340 -1.251 1.00 22.84 ? 415 HOH A O 1 HETATM 1697 O O . HOH H 6 . ? -5.729 86.346 0.887 1.00 20.31 ? 416 HOH A O 1 HETATM 1698 O O . HOH H 6 . ? 5.973 76.161 15.242 1.00 25.30 ? 417 HOH A O 1 HETATM 1699 O O . HOH H 6 . ? 19.045 88.019 8.972 1.00 27.06 ? 418 HOH A O 1 HETATM 1700 O O . HOH H 6 . ? 21.302 93.345 4.836 1.00 22.83 ? 419 HOH A O 1 HETATM 1701 O O . HOH H 6 . ? 3.185 76.311 -15.445 1.00 21.56 ? 420 HOH A O 1 HETATM 1702 O O . HOH H 6 . ? 10.643 76.292 -14.155 1.00 32.83 ? 421 HOH A O 1 HETATM 1703 O O . HOH H 6 . ? 18.653 77.858 7.032 1.00 25.60 ? 422 HOH A O 1 HETATM 1704 O O . HOH H 6 . ? 14.517 81.738 12.786 1.00 19.79 ? 423 HOH A O 1 HETATM 1705 O O . HOH H 6 . ? 18.088 65.485 6.265 1.00 39.82 ? 424 HOH A O 1 HETATM 1706 O O . HOH H 6 . ? 22.468 70.541 1.742 1.00 27.45 ? 425 HOH A O 1 HETATM 1707 O O . HOH H 6 . ? 22.164 67.082 1.965 1.00 22.62 ? 426 HOH A O 1 HETATM 1708 O O . HOH H 6 . ? 34.612 66.224 -5.072 1.00 31.79 ? 427 HOH A O 1 HETATM 1709 O O . HOH H 6 . ? -6.910 83.454 -8.334 1.00 22.97 ? 428 HOH A O 1 HETATM 1710 O O . HOH H 6 . ? 21.407 77.262 -8.374 1.00 25.82 ? 429 HOH A O 1 HETATM 1711 O O . HOH H 6 . ? 25.784 84.892 -4.669 1.00 37.62 ? 430 HOH A O 1 HETATM 1712 O O . HOH H 6 . ? -4.386 96.014 -10.785 1.00 25.60 ? 431 HOH A O 1 HETATM 1713 O O . HOH H 6 . ? 7.390 91.165 11.274 1.00 32.45 ? 432 HOH A O 1 HETATM 1714 O O . HOH H 6 . ? -9.168 84.903 -5.273 1.00 29.37 ? 433 HOH A O 1 HETATM 1715 O O . HOH H 6 . ? 26.785 63.750 -3.944 1.00 25.53 ? 434 HOH A O 1 HETATM 1716 O O . HOH H 6 . ? 20.440 73.338 3.547 1.00 25.03 ? 435 HOH A O 1 HETATM 1717 O O . HOH H 6 . ? 3.305 98.380 7.431 1.00 32.63 ? 436 HOH A O 1 HETATM 1718 O O . HOH H 6 . ? 3.805 93.066 -8.843 1.00 32.73 ? 437 HOH A O 1 HETATM 1719 O O . HOH H 6 . ? 9.261 60.362 3.193 1.00 35.95 ? 438 HOH A O 1 HETATM 1720 O O . HOH H 6 . ? 12.017 87.177 1.494 1.00 21.95 ? 439 HOH A O 1 HETATM 1721 O O . HOH H 6 . ? 4.145 80.161 -17.273 1.00 45.75 ? 440 HOH A O 1 HETATM 1722 O O . HOH H 6 . ? 1.983 86.570 10.477 1.00 42.44 ? 441 HOH A O 1 HETATM 1723 O O . HOH H 6 . ? 15.640 79.265 11.915 1.00 30.58 ? 442 HOH A O 1 HETATM 1724 O O . HOH H 6 . ? 7.750 81.443 3.252 1.00 28.50 ? 443 HOH A O 1 HETATM 1725 O O . HOH H 6 . ? 10.071 89.124 2.129 1.00 27.65 ? 444 HOH A O 1 HETATM 1726 O O . HOH H 6 . ? 3.368 73.219 -0.993 1.00 45.01 ? 445 HOH A O 1 HETATM 1727 O O . HOH H 6 . ? -1.381 97.402 -8.698 1.00 30.16 ? 446 HOH A O 1 HETATM 1728 O O . HOH H 6 . ? 20.941 65.668 5.312 1.00 33.88 ? 447 HOH A O 1 HETATM 1729 O O . HOH H 6 . ? 21.150 77.107 5.244 1.00 33.68 ? 448 HOH A O 1 HETATM 1730 O O . HOH H 6 . ? 26.168 76.033 -3.042 1.00 35.26 ? 449 HOH A O 1 HETATM 1731 O O . HOH H 6 . ? 9.867 87.978 -8.912 1.00 34.31 ? 450 HOH A O 1 HETATM 1732 O O . HOH H 6 . ? 2.179 95.090 -7.521 1.00 28.66 ? 451 HOH A O 1 HETATM 1733 O O . HOH H 6 . ? 34.179 63.890 0.735 1.00 31.44 ? 452 HOH A O 1 HETATM 1734 O O . HOH H 6 . ? -8.077 76.086 -7.709 1.00 48.28 ? 453 HOH A O 1 HETATM 1735 O O . HOH H 6 . ? 12.321 88.051 -10.046 1.00 38.16 ? 454 HOH A O 1 HETATM 1736 O O . HOH H 6 . ? 27.165 82.139 -5.238 1.00 36.49 ? 455 HOH A O 1 HETATM 1737 O O . HOH H 6 . ? 11.441 91.604 2.250 1.00 34.70 ? 456 HOH A O 1 HETATM 1738 O O . HOH H 6 . ? 11.267 81.529 -14.991 1.00 41.71 ? 457 HOH A O 1 HETATM 1739 O O . HOH H 6 . ? 9.035 82.902 -14.694 1.00 43.85 ? 458 HOH A O 1 HETATM 1740 O O . HOH H 6 . ? 16.679 60.528 0.540 1.00 43.57 ? 459 HOH A O 1 HETATM 1741 O O . HOH H 6 . ? -0.459 86.417 8.420 1.00 39.25 ? 460 HOH A O 1 HETATM 1742 O O . HOH H 6 . ? 27.622 68.529 7.465 1.00 38.02 ? 461 HOH A O 1 HETATM 1743 O O . HOH H 6 . ? -10.131 92.364 -7.395 1.00 33.42 ? 462 HOH A O 1 HETATM 1744 O O . HOH H 6 . ? 8.997 88.714 18.328 1.00 32.67 ? 463 HOH A O 1 HETATM 1745 O O . HOH H 6 . ? -5.669 84.187 9.262 1.00 50.73 ? 464 HOH A O 1 HETATM 1746 O O . HOH H 6 . ? -10.775 88.752 4.639 1.00 36.32 ? 465 HOH A O 1 HETATM 1747 O O . HOH H 6 . ? 14.219 73.061 -12.112 1.00 41.51 ? 466 HOH A O 1 HETATM 1748 O O . HOH H 6 . ? -1.822 84.077 9.370 1.00 33.08 ? 467 HOH A O 1 HETATM 1749 O O . HOH H 6 . ? 6.852 61.306 2.647 1.00 44.44 ? 468 HOH A O 1 HETATM 1750 O O . HOH H 6 . ? 22.450 64.608 1.283 1.00 35.99 ? 469 HOH A O 1 HETATM 1751 O O . HOH H 6 . ? -1.682 95.512 -10.682 1.00 40.95 ? 470 HOH A O 1 HETATM 1752 O O . HOH H 6 . ? 19.806 76.063 3.401 1.00 42.59 ? 471 HOH A O 1 HETATM 1753 O O . HOH H 6 . ? 21.046 78.302 8.206 1.00 39.30 ? 472 HOH A O 1 HETATM 1754 O O . HOH H 6 . ? 16.543 60.133 5.740 1.00 52.72 ? 473 HOH A O 1 HETATM 1755 O O . HOH H 6 . ? 6.618 61.715 0.023 1.00 31.71 ? 474 HOH A O 1 HETATM 1756 O O . HOH H 6 . ? 8.624 95.438 -5.815 1.00 36.34 ? 475 HOH A O 1 HETATM 1757 O O . HOH H 6 . ? 16.651 89.630 9.030 1.00 35.70 ? 476 HOH A O 1 HETATM 1758 O O . HOH H 6 . ? 4.426 95.906 -6.557 1.00 34.67 ? 477 HOH A O 1 HETATM 1759 O O . HOH H 6 . ? -7.142 76.890 -10.173 1.00 40.47 ? 478 HOH A O 1 HETATM 1760 O O . HOH H 6 . ? 16.712 73.836 -11.047 1.00 36.14 ? 479 HOH A O 1 HETATM 1761 O O . HOH H 6 . ? 15.817 66.596 7.985 1.00 34.13 ? 480 HOH A O 1 HETATM 1762 O O . HOH H 6 . ? 10.986 92.095 -9.241 1.00 42.20 ? 481 HOH A O 1 HETATM 1763 O O . HOH H 6 . ? 20.727 66.485 13.847 1.00 44.12 ? 482 HOH A O 1 HETATM 1764 O O . HOH H 6 . ? 9.110 61.309 -2.677 1.00 43.75 ? 483 HOH A O 1 HETATM 1765 O O . HOH H 6 . ? -4.392 82.410 -14.812 1.00 32.27 ? 484 HOH A O 1 HETATM 1766 O O . HOH H 6 . ? 17.034 78.599 14.311 1.00 38.30 ? 485 HOH A O 1 HETATM 1767 O O . HOH H 6 . ? 8.410 75.769 -15.939 1.00 39.55 ? 486 HOH A O 1 HETATM 1768 O O . HOH H 6 . ? 7.496 88.969 -10.344 1.00 29.74 ? 487 HOH A O 1 HETATM 1769 O O . HOH H 6 . ? 4.538 97.622 -4.623 1.00 38.57 ? 488 HOH A O 1 HETATM 1770 O O . HOH H 6 . ? 2.361 82.107 9.917 1.00 35.06 ? 489 HOH A O 1 HETATM 1771 O O . HOH H 6 . ? 14.346 75.997 21.089 1.00 49.27 ? 490 HOH A O 1 HETATM 1772 O O . HOH H 6 . ? 12.863 64.771 11.753 1.00 41.43 ? 491 HOH A O 1 HETATM 1773 O O . HOH H 6 . ? 14.293 92.095 -8.589 1.00 56.59 ? 492 HOH A O 1 HETATM 1774 O O . HOH H 6 . ? 9.382 62.480 -12.533 1.00 36.67 ? 493 HOH A O 1 HETATM 1775 O O . HOH H 6 . ? 16.809 69.240 -12.852 1.00 45.88 ? 494 HOH A O 1 HETATM 1776 O O . HOH H 6 . ? 17.989 88.113 -4.099 1.00 39.43 ? 495 HOH A O 1 HETATM 1777 O O . HOH H 6 . ? -9.099 76.621 2.530 1.00 33.52 ? 496 HOH A O 1 HETATM 1778 O O . HOH H 6 . ? 1.993 100.496 6.263 1.00 36.60 ? 497 HOH A O 1 HETATM 1779 O O . HOH H 6 . ? 32.965 61.634 1.814 1.00 41.66 ? 498 HOH A O 1 HETATM 1780 O O . HOH H 6 . ? 6.796 98.863 -3.590 1.00 45.40 ? 499 HOH A O 1 HETATM 1781 O O . HOH H 6 . ? 11.540 64.570 -3.704 1.00 35.49 ? 500 HOH A O 1 HETATM 1782 O O . HOH H 6 . ? 10.187 91.038 11.971 1.00 39.46 ? 501 HOH A O 1 HETATM 1783 O O . HOH H 6 . ? 4.643 61.457 -7.519 1.00 37.74 ? 502 HOH A O 1 HETATM 1784 O O . HOH H 6 . ? -3.736 77.202 7.265 1.00 45.24 ? 503 HOH A O 1 HETATM 1785 O O . HOH H 6 . ? 0.072 94.626 -12.754 1.00 44.95 ? 504 HOH A O 1 HETATM 1786 O O . HOH H 6 . ? 22.516 74.022 13.070 1.00 47.70 ? 505 HOH A O 1 HETATM 1787 O O . HOH H 6 . ? 24.112 81.845 12.202 1.00 51.56 ? 506 HOH A O 1 HETATM 1788 O O . HOH H 6 . ? 3.769 91.759 -11.443 1.00 54.32 ? 507 HOH A O 1 HETATM 1789 O O . HOH H 6 . ? -10.360 83.800 0.987 1.00 50.40 ? 508 HOH A O 1 HETATM 1790 O O . HOH H 6 . ? 2.385 66.436 8.902 1.00 52.80 ? 509 HOH A O 1 HETATM 1791 O O . HOH H 6 . ? 15.728 92.824 -2.397 1.00 51.09 ? 510 HOH A O 1 HETATM 1792 O O . HOH H 6 . ? -3.911 83.228 7.226 1.00 48.62 ? 511 HOH A O 1 HETATM 1793 O O . HOH H 6 . ? 14.413 64.524 8.785 1.00 49.69 ? 512 HOH A O 1 HETATM 1794 O O . HOH H 6 . ? 10.558 97.357 -5.540 1.00 51.33 ? 513 HOH A O 1 HETATM 1795 O O . HOH H 6 . ? 22.301 76.173 11.795 1.00 58.15 ? 514 HOH A O 1 HETATM 1796 O O . HOH H 6 . ? -11.223 81.510 2.193 1.00 52.78 ? 515 HOH A O 1 HETATM 1797 O O . HOH H 6 . ? -4.675 78.961 8.905 1.00 48.39 ? 516 HOH A O 1 HETATM 1798 O O . HOH H 6 . ? 6.710 101.657 -2.999 1.00 48.63 ? 517 HOH A O 1 HETATM 1799 O O . HOH H 6 . ? 18.001 94.087 -2.739 1.00 59.74 ? 518 HOH A O 1 HETATM 1800 O O . HOH H 6 . ? 8.241 64.745 13.429 1.00 43.04 ? 519 HOH A O 1 HETATM 1801 O O . HOH H 6 . ? 21.934 91.261 -2.831 1.00 50.86 ? 520 HOH A O 1 HETATM 1802 O O . HOH H 6 . ? 13.107 78.580 19.712 1.00 36.79 ? 521 HOH A O 1 HETATM 1803 O O . HOH H 6 . ? 14.269 69.866 -13.011 1.00 58.20 ? 522 HOH A O 1 HETATM 1804 O O . HOH H 6 . ? 8.459 93.088 -8.931 1.00 58.85 ? 523 HOH A O 1 HETATM 1805 O O . HOH H 6 . ? 1.742 68.597 10.348 1.00 54.72 ? 524 HOH A O 1 HETATM 1806 O O . HOH H 6 . ? 13.996 80.525 18.149 1.00 44.17 ? 525 HOH A O 1 HETATM 1807 O O . HOH H 6 . ? -11.405 79.306 0.217 1.00 43.06 ? 526 HOH A O 1 HETATM 1808 O O . HOH H 6 . ? 11.349 80.065 -0.028 1.00 30.54 ? 527 HOH A O 1 HETATM 1809 O O . HOH H 6 . ? -7.799 80.882 -11.927 1.00 41.39 ? 528 HOH A O 1 HETATM 1810 O O . HOH H 6 . ? 12.497 96.144 -0.451 1.00 37.19 ? 529 HOH A O 1 HETATM 1811 O O . HOH H 6 . ? 12.205 79.483 -16.704 1.00 61.13 ? 530 HOH A O 1 HETATM 1812 O O . HOH H 6 . ? 7.819 100.425 -0.583 1.00 45.81 ? 531 HOH A O 1 HETATM 1813 O O . HOH H 6 . ? 12.310 97.278 -3.245 1.00 42.92 ? 532 HOH A O 1 HETATM 1814 O O . HOH H 6 . ? -0.153 97.224 -14.458 1.00 53.07 ? 533 HOH A O 1 HETATM 1815 O O . HOH H 6 . ? 10.931 84.111 1.978 1.00 25.12 ? 534 HOH A O 1 HETATM 1816 O O . HOH H 6 . ? -6.512 81.488 -13.855 1.00 38.50 ? 535 HOH A O 1 HETATM 1817 O O . HOH H 6 . ? 11.917 82.326 0.596 1.00 39.49 ? 536 HOH A O 1 HETATM 1818 O O . HOH H 6 . ? 19.551 72.521 -9.997 1.00 40.63 ? 537 HOH A O 1 HETATM 1819 O O . HOH H 6 . ? -9.110 73.908 6.674 1.00 44.54 ? 538 HOH A O 1 HETATM 1820 O O . HOH H 6 . ? 2.928 88.616 -12.875 1.00 43.03 ? 539 HOH A O 1 HETATM 1821 O O . HOH H 6 . ? 3.674 77.808 -18.614 1.00 58.10 ? 540 HOH A O 1 HETATM 1822 O O . HOH H 6 . ? 5.443 88.478 -13.422 1.00 43.11 ? 541 HOH A O 1 HETATM 1823 O O . HOH H 6 . ? 14.387 80.042 15.488 1.00 41.66 ? 542 HOH A O 1 HETATM 1824 O O . HOH H 6 . ? 15.971 58.382 3.779 1.00 60.29 ? 543 HOH A O 1 HETATM 1825 O O . HOH H 6 . ? 0.719 100.670 3.285 1.00 31.86 ? 544 HOH A O 1 HETATM 1826 O O . HOH H 6 . ? 8.657 69.129 15.518 1.00 40.70 ? 545 HOH A O 1 HETATM 1827 O O . HOH H 6 . ? 18.198 59.283 -10.367 1.00 57.05 ? 546 HOH A O 1 HETATM 1828 O O . HOH H 6 . ? 28.462 66.225 4.612 1.00 40.68 ? 547 HOH A O 1 HETATM 1829 O O . HOH H 6 . ? -11.741 84.518 -6.792 1.00 47.75 ? 548 HOH A O 1 HETATM 1830 O O . HOH H 6 . ? 1.417 74.250 10.751 1.00 42.86 ? 549 HOH A O 1 HETATM 1831 O O . HOH H 6 . ? 3.818 73.120 17.741 1.00 47.07 ? 550 HOH A O 1 HETATM 1832 O O . HOH H 6 . ? 2.164 72.368 15.848 1.00 52.96 ? 551 HOH A O 1 HETATM 1833 O O . HOH H 6 . ? 28.847 72.632 12.695 1.00 43.84 ? 552 HOH A O 1 HETATM 1834 O O . HOH H 6 . ? 27.306 65.658 8.036 1.00 48.15 ? 553 HOH A O 1 HETATM 1835 O O . HOH H 6 . ? -0.193 74.438 8.590 1.00 51.84 ? 554 HOH A O 1 HETATM 1836 O O . HOH H 6 . ? -3.113 80.614 11.815 1.00 54.49 ? 555 HOH A O 1 HETATM 1837 O O . HOH H 6 . ? 35.447 66.561 -7.502 1.00 27.56 ? 556 HOH A O 1 HETATM 1838 O O . HOH H 6 . ? 4.567 65.127 8.865 1.00 44.19 ? 557 HOH A O 1 HETATM 1839 O O . HOH H 6 . ? 23.213 65.703 10.763 1.00 43.46 ? 558 HOH A O 1 HETATM 1840 O O . HOH H 6 . ? 28.902 79.897 -1.148 1.00 58.91 ? 559 HOH A O 1 HETATM 1841 O O . HOH H 6 . ? -5.999 85.336 12.138 1.00 52.41 ? 560 HOH A O 1 HETATM 1842 O O . HOH H 6 . ? 14.267 90.515 -6.455 1.00 31.14 ? 561 HOH A O 1 HETATM 1843 O O . HOH H 6 . ? -1.625 72.537 -11.747 1.00 45.88 ? 562 HOH A O 1 HETATM 1844 O O . HOH H 6 . ? 3.365 65.920 1.732 1.00 41.31 ? 563 HOH A O 1 HETATM 1845 O O . HOH H 6 . ? -3.450 72.668 1.840 1.00 40.32 ? 564 HOH A O 1 HETATM 1846 O O . HOH H 6 . ? 24.002 76.618 -7.404 1.00 42.56 ? 565 HOH A O 1 HETATM 1847 O O . HOH H 6 . ? 7.920 75.710 27.036 1.00 48.49 ? 566 HOH A O 1 HETATM 1848 O O . HOH H 6 . ? 21.250 85.164 -6.055 1.00 43.59 ? 567 HOH A O 1 HETATM 1849 O O . HOH H 6 . ? -4.205 97.046 0.813 1.00 47.47 ? 568 HOH A O 1 HETATM 1850 O O . HOH H 6 . ? 31.694 72.823 -4.339 1.00 50.61 ? 569 HOH A O 1 HETATM 1851 O O . HOH H 6 . ? 22.806 85.790 -4.276 1.00 47.95 ? 570 HOH A O 1 HETATM 1852 O O . HOH H 6 . ? 24.405 62.727 -10.297 1.00 59.35 ? 571 HOH A O 1 HETATM 1853 O O . HOH H 6 . ? 11.221 58.959 1.169 1.00 45.89 ? 572 HOH A O 1 HETATM 1854 O O . HOH H 6 . ? 30.963 79.400 11.824 1.00 56.26 ? 573 HOH A O 1 HETATM 1855 O O . HOH H 6 . ? 26.646 60.569 -5.049 1.00 53.38 ? 574 HOH A O 1 HETATM 1856 O O . HOH H 6 . ? 3.462 63.974 3.695 1.00 45.96 ? 575 HOH A O 1 HETATM 1857 O O . HOH H 6 . ? 14.005 58.435 1.999 1.00 59.11 ? 576 HOH A O 1 HETATM 1858 O O . HOH H 6 . ? 1.006 71.478 6.150 1.00 40.78 ? 577 HOH A O 1 HETATM 1859 O O . HOH H 6 . ? 4.409 72.987 -13.034 1.00 37.16 ? 578 HOH A O 1 HETATM 1860 O O . HOH H 6 . ? 8.051 77.727 29.290 1.00 42.70 ? 579 HOH A O 1 HETATM 1861 O O . HOH H 6 . ? 14.509 92.337 -0.081 1.00 41.19 ? 580 HOH A O 1 HETATM 1862 O O . HOH H 6 . ? -8.762 91.862 -1.178 1.00 45.62 ? 581 HOH A O 1 HETATM 1863 O O . HOH H 6 . ? 14.232 89.917 4.395 1.00 46.57 ? 582 HOH A O 1 HETATM 1864 O O . HOH H 6 . ? 29.483 61.133 -4.292 1.00 37.16 ? 583 HOH A O 1 HETATM 1865 O O . HOH H 6 . ? 16.704 86.850 -8.577 1.00 36.86 ? 584 HOH A O 1 HETATM 1866 O O . HOH H 6 . ? -3.439 97.906 -1.474 1.00 59.20 ? 585 HOH A O 1 HETATM 1867 O O . HOH H 6 . ? 21.161 78.578 10.941 1.00 55.95 ? 586 HOH A O 1 HETATM 1868 O O . HOH H 6 . ? 6.449 72.149 -14.728 1.00 58.62 ? 587 HOH A O 1 HETATM 1869 O O . HOH H 6 . ? 16.015 90.127 6.462 1.00 42.62 ? 588 HOH A O 1 HETATM 1870 O O . HOH H 6 . ? -1.454 70.617 1.816 1.00 47.92 ? 589 HOH A O 1 HETATM 1871 O O . HOH H 6 . ? -9.156 76.057 -2.674 1.00 55.36 ? 590 HOH A O 1 HETATM 1872 O O . HOH H 6 . ? 0.192 68.748 5.270 1.00 51.61 ? 591 HOH A O 1 HETATM 1873 O O . HOH H 6 . ? -10.984 90.745 -0.926 1.00 58.64 ? 592 HOH A O 1 HETATM 1874 O O . HOH H 6 . ? 34.630 60.613 3.578 1.00 51.98 ? 593 HOH A O 1 HETATM 1875 O O . HOH H 6 . ? -8.158 77.899 -3.990 1.00 42.44 ? 594 HOH A O 1 HETATM 1876 O O . HOH H 6 . ? 30.296 74.806 -7.711 1.00 52.12 ? 595 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 1 N N . TRP A 1 ? 0.3004 0.3220 0.2289 0.0077 -0.0200 -0.0797 28 TRP A N 2 C CA . TRP A 1 ? 0.3318 0.3503 0.2543 0.0075 -0.0276 -0.0830 28 TRP A CA 3 C C . TRP A 1 ? 0.3902 0.4149 0.3122 -0.0002 -0.0198 -0.0762 28 TRP A C 4 O O . TRP A 1 ? 0.3949 0.4315 0.3372 -0.0026 -0.0095 -0.0725 28 TRP A O 5 C CB . TRP A 1 ? 0.3342 0.3623 0.2847 0.0141 -0.0341 -0.0951 28 TRP A CB 6 C CG . TRP A 1 ? 0.3814 0.4054 0.3324 0.0240 -0.0445 -0.1038 28 TRP A CG 7 C CD1 . TRP A 1 ? 0.3672 0.3995 0.3406 0.0281 -0.0416 -0.1085 28 TRP A CD1 8 C CD2 . TRP A 1 ? 0.3826 0.3930 0.3097 0.0326 -0.0591 -0.1086 28 TRP A CD2 9 N NE1 . TRP A 1 ? 0.3515 0.3779 0.3185 0.0389 -0.0545 -0.1170 28 TRP A NE1 10 C CE2 . TRP A 1 ? 0.3843 0.3962 0.3216 0.0426 -0.0657 -0.1167 28 TRP A CE2 11 C CE3 . TRP A 1 ? 0.3467 0.3433 0.2435 0.0337 -0.0664 -0.1065 28 TRP A CE3 12 C CZ2 . TRP A 1 ? 0.3549 0.3544 0.2721 0.0550 -0.0805 -0.1223 28 TRP A CZ2 13 C CZ3 . TRP A 1 ? 0.4007 0.3833 0.2755 0.0455 -0.0798 -0.1111 28 TRP A CZ3 14 C CH2 . TRP A 1 ? 0.4095 0.3932 0.2941 0.0567 -0.0873 -0.1187 28 TRP A CH2 15 N N . ALA A 2 ? 0.3883 0.4043 0.2864 -0.0034 -0.0240 -0.0741 29 ALA A N 16 C CA . ALA A 2 ? 0.4378 0.4605 0.3346 -0.0099 -0.0177 -0.0690 29 ALA A CA 17 C C . ALA A 2 ? 0.4490 0.4838 0.3746 -0.0082 -0.0157 -0.0738 29 ALA A C 18 O O . ALA A 2 ? 0.4193 0.4547 0.3574 -0.0029 -0.0233 -0.0837 29 ALA A O 19 C CB . ALA A 2 ? 0.2837 0.2944 0.1511 -0.0131 -0.0223 -0.0678 29 ALA A CB 20 N N . ARG A 3 ? 0.3940 0.4384 0.3305 -0.0120 -0.0056 -0.0676 30 ARG A N 21 C CA . ARG A 3 ? 0.3505 0.4035 0.3135 -0.0113 -0.0016 -0.0713 30 ARG A CA 22 C C . ARG A 3 ? 0.3436 0.3947 0.2948 -0.0126 -0.0071 -0.0751 30 ARG A C 23 O O . ARG A 3 ? 0.3735 0.4288 0.3205 -0.0159 -0.0015 -0.0698 30 ARG A O 24 C CB . ARG A 3 ? 0.4034 0.4643 0.3796 -0.0127 0.0120 -0.0618 30 ARG A CB 25 C CG . ARG A 3 ? 0.4220 0.4847 0.4103 -0.0104 0.0195 -0.0580 30 ARG A CG 26 C CD . ARG A 3 ? 0.4919 0.5599 0.4788 -0.0100 0.0319 -0.0457 30 ARG A CD 27 N NE . ARG A 3 ? 0.6164 0.6873 0.6285 -0.0084 0.0429 -0.0431 30 ARG A NE 28 C CZ . ARG A 3 ? 0.6770 0.7510 0.6872 -0.0061 0.0532 -0.0321 30 ARG A CZ 29 N NH1 . ARG A 3 ? 0.6461 0.7245 0.6316 -0.0050 0.0526 -0.0243 30 ARG A NH1 30 N NH2 . ARG A 3 ? 0.6578 0.7303 0.6911 -0.0042 0.0641 -0.0295 30 ARG A NH2 31 N N . THR A 4 ? 0.3315 0.3769 0.2765 -0.0087 -0.0184 -0.0848 31 THR A N 32 C CA . THR A 4 ? 0.4048 0.4464 0.3325 -0.0084 -0.0246 -0.0890 31 THR A CA 33 C C . THR A 4 ? 0.4244 0.4755 0.3731 -0.0090 -0.0210 -0.0941 31 THR A C 34 O O . THR A 4 ? 0.4561 0.5061 0.3902 -0.0097 -0.0229 -0.0957 31 THR A O 35 C CB . THR A 4 ? 0.4487 0.4818 0.3632 -0.0009 -0.0384 -0.0984 31 THR A CB 36 O OG1 . THR A 4 ? 0.4522 0.4939 0.3977 0.0045 -0.0429 -0.1096 31 THR A OG1 37 C CG2 . THR A 4 ? 0.4074 0.4259 0.2932 -0.0002 -0.0414 -0.0920 31 THR A CG2 38 N N . GLU A 5 ? 0.3526 0.4118 0.3353 -0.0087 -0.0147 -0.0968 32 GLU A N 39 C CA . GLU A 5 ? 0.3773 0.4429 0.3819 -0.0097 -0.0089 -0.1008 32 GLU A CA 40 C C . GLU A 5 ? 0.4275 0.4950 0.4227 -0.0133 0.0013 -0.0883 32 GLU A C 41 O O . GLU A 5 ? 0.4514 0.5226 0.4595 -0.0134 0.0066 -0.0897 32 GLU A O 42 C CB . GLU A 5 ? 0.3497 0.4205 0.3946 -0.0092 -0.0023 -0.1065 32 GLU A CB 43 C CG . GLU A 5 ? 0.4508 0.5218 0.5057 -0.0112 0.0119 -0.0932 32 GLU A CG 44 C CD . GLU A 5 ? 0.5041 0.5734 0.5513 -0.0102 0.0102 -0.0895 32 GLU A CD 45 O OE1 . GLU A 5 ? 0.4980 0.5646 0.5310 -0.0077 -0.0023 -0.0964 32 GLU A OE1 46 O OE2 . GLU A 5 ? 0.5126 0.5825 0.5667 -0.0107 0.0215 -0.0796 32 GLU A OE2 47 N N . LEU A 6 ? 0.3747 0.4403 0.3482 -0.0156 0.0035 -0.0774 33 LEU A N 48 C CA . LEU A 6 ? 0.2983 0.3692 0.2623 -0.0181 0.0113 -0.0670 33 LEU A CA 49 C C . LEU A 6 ? 0.3212 0.3902 0.2546 -0.0221 0.0069 -0.0656 33 LEU A C 50 O O . LEU A 6 ? 0.3436 0.4195 0.2687 -0.0248 0.0120 -0.0593 33 LEU A O 51 C CB . LEU A 6 ? 0.2597 0.3335 0.2261 -0.0177 0.0190 -0.0565 33 LEU A CB 52 C CG . LEU A 6 ? 0.2749 0.3491 0.2692 -0.0143 0.0276 -0.0545 33 LEU A CG 53 C CD1 . LEU A 6 ? 0.2713 0.3480 0.2592 -0.0127 0.0348 -0.0433 33 LEU A CD1 54 C CD2 . LEU A 6 ? 0.3009 0.3772 0.3166 -0.0122 0.0354 -0.0548 33 LEU A CD2 55 N N . LEU A 7 ? 0.3079 0.2512 0.3155 0.0032 0.0589 0.0700 34 LEU A N 56 C CA . LEU A 7 ? 0.2750 0.1934 0.2376 0.0121 0.0684 0.0807 34 LEU A CA 57 C C . LEU A 7 ? 0.3576 0.2743 0.2995 0.0355 0.0573 0.0750 34 LEU A C 58 O O . LEU A 7 ? 0.3589 0.2902 0.3093 0.0550 0.0430 0.0618 34 LEU A O 59 C CB . LEU A 7 ? 0.3558 0.2615 0.2999 0.0189 0.0792 0.0859 34 LEU A CB 60 C CG . LEU A 7 ? 0.4195 0.3269 0.3784 -0.0015 0.0891 0.0898 34 LEU A CG 61 C CD1 . LEU A 7 ? 0.4503 0.3471 0.3909 0.0081 0.0957 0.0907 34 LEU A CD1 62 C CD2 . LEU A 7 ? 0.3825 0.3005 0.3419 -0.0201 0.0769 0.0805 34 LEU A CD2 63 N N . ASN A 8 ? 0.3533 0.2533 0.2677 0.0348 0.0642 0.0845 35 ASN A N 64 C CA . ASN A 8 ? 0.4304 0.3273 0.3213 0.0579 0.0557 0.0811 35 ASN A CA 65 C C . ASN A 8 ? 0.4919 0.4146 0.4125 0.0666 0.0334 0.0629 35 ASN A C 66 O O . ASN A 8 ? 0.4569 0.3873 0.3702 0.0925 0.0200 0.0516 35 ASN A O 67 C CB . ASN A 8 ? 0.4261 0.3072 0.2818 0.0833 0.0604 0.0842 35 ASN A CB 68 C CG . ASN A 8 ? 0.4915 0.3591 0.3099 0.1055 0.0608 0.0884 35 ASN A CG 69 O OD1 . ASN A 8 ? 0.4962 0.3611 0.3132 0.0922 0.0668 0.0916 35 ASN A OD1 70 N ND2 . ASN A 8 ? 0.4305 0.2992 0.2297 0.1369 0.0515 0.0813 35 ASN A ND2 71 N N . VAL A 9 ? 0.4627 0.3980 0.4171 0.0455 0.0294 0.0594 36 VAL A N 72 C CA . VAL A 9 ? 0.4294 0.3873 0.4179 0.0490 0.0096 0.0416 36 VAL A CA 73 C C . VAL A 9 ? 0.3733 0.3313 0.3663 0.0407 0.0048 0.0415 36 VAL A C 74 O O . VAL A 9 ? 0.3742 0.3210 0.3589 0.0232 0.0175 0.0548 36 VAL A O 75 C CB . VAL A 9 ? 0.4066 0.3823 0.4415 0.0328 0.0075 0.0341 36 VAL A CB 76 C CG1 . VAL A 9 ? 0.4632 0.4460 0.4996 0.0464 0.0065 0.0286 36 VAL A CG1 77 C CG2 . VAL A 9 ? 0.3022 0.2692 0.3452 0.0049 0.0244 0.0487 36 VAL A CG2 78 N N . CYS A 10 ? 0.3002 0.2722 0.3070 0.0546 -0.0147 0.0248 37 CYS A N 79 C CA . CYS A 10 ? 0.3094 0.2837 0.3256 0.0486 -0.0223 0.0211 37 CYS A CA 80 C C . CYS A 10 ? 0.3840 0.3778 0.4496 0.0422 -0.0381 0.0024 37 CYS A C 81 O O . CYS A 10 ? 0.3896 0.3991 0.4727 0.0564 -0.0520 -0.0144 37 CYS A O 82 C CB . CYS A 10 ? 0.3175 0.2875 0.2999 0.0745 -0.0315 0.0173 37 CYS A CB 83 S SG . CYS A 10 ? 0.3728 0.3196 0.2978 0.0881 -0.0126 0.0373 37 CYS A SG 84 N N . MET A 11 ? 0.3350 0.3279 0.4240 0.0210 -0.0354 0.0050 38 MET A N 85 C CA . MET A 11 ? 0.3062 0.3137 0.4435 0.0128 -0.0480 -0.0115 38 MET A CA 86 C C . MET A 11 ? 0.3745 0.3856 0.5107 0.0281 -0.0673 -0.0269 38 MET A C 87 O O . MET A 11 ? 0.3799 0.3796 0.4959 0.0266 -0.0650 -0.0192 38 MET A O 88 C CB . MET A 11 ? 0.3096 0.3109 0.4702 -0.0152 -0.0345 -0.0003 38 MET A CB 89 C CG . MET A 11 ? 0.2803 0.2930 0.4941 -0.0267 -0.0431 -0.0150 38 MET A CG 90 S SD . MET A 11 ? 0.3998 0.4322 0.6556 -0.0308 -0.0425 -0.0249 38 MET A SD 91 C CE . MET A 11 ? 0.3920 0.4211 0.6923 -0.0607 -0.0285 -0.0177 38 MET A CE 92 N N . ASN A 12 ? 0.3922 0.4206 0.5502 0.0440 -0.0870 -0.0498 39 ASN A N 93 C CA . ASN A 12 ? 0.3761 0.4096 0.5336 0.0616 -0.1080 -0.0680 39 ASN A CA 94 C C . ASN A 12 ? 0.4138 0.4526 0.6202 0.0452 -0.1172 -0.0821 39 ASN A C 95 O O . ASN A 12 ? 0.3484 0.3882 0.5913 0.0210 -0.1067 -0.0777 39 ASN A O 96 C CB . ASN A 12 ? 0.4254 0.4744 0.5744 0.0926 -0.1267 -0.0874 39 ASN A CB 97 C CG . ASN A 12 ? 0.4786 0.5509 0.6776 0.0894 -0.1371 -0.1073 39 ASN A CG 98 O OD1 . ASN A 12 ? 0.4830 0.5611 0.7302 0.0654 -0.1348 -0.1119 39 ASN A OD1 99 N ND2 . ASN A 12 ? 0.4852 0.5712 0.6727 0.1150 -0.1480 -0.1192 39 ASN A ND2 100 N N . ALA A 13 ? 0.3939 0.4348 0.5999 0.0595 -0.1360 -0.0986 40 ALA A N 101 C CA . ALA A 13 ? 0.4354 0.4764 0.6830 0.0457 -0.1450 -0.1121 40 ALA A CA 102 C C . ALA A 13 ? 0.4057 0.4647 0.7148 0.0346 -0.1532 -0.1322 40 ALA A C 103 O O . ALA A 13 ? 0.3836 0.4387 0.7338 0.0143 -0.1517 -0.1369 40 ALA A O 104 C CB . ALA A 13 ? 0.4692 0.5091 0.7000 0.0675 -0.1654 -0.1279 40 ALA A CB 105 N N . LYS A 14 ? 0.3998 0.4783 0.7160 0.0482 -0.1611 -0.1441 41 LYS A N 106 C CA . LYS A 14 ? 0.4024 0.5016 0.7783 0.0378 -0.1671 -0.1631 41 LYS A CA 107 C C . LYS A 14 ? 0.3562 0.4552 0.7462 0.0159 -0.1436 -0.1436 41 LYS A C 108 O O . LYS A 14 ? 0.3403 0.4528 0.7634 0.0099 -0.1403 -0.1519 41 LYS A O 109 C CB . LYS A 14 ? 0.3902 0.5068 0.7589 0.0657 -0.1846 -0.1866 41 LYS A CB 110 N N . HIS A 15 ? 0.3979 0.4751 0.7489 0.0064 -0.1224 -0.1145 42 HIS A N 111 C CA . HIS A 15 ? 0.4053 0.4774 0.7601 -0.0134 -0.0983 -0.0931 42 HIS A CA 112 C C . HIS A 15 ? 0.3746 0.4632 0.7289 -0.0035 -0.0969 -0.0955 42 HIS A C 113 O O . HIS A 15 ? 0.3377 0.4336 0.7206 -0.0190 -0.0840 -0.0903 42 HIS A O 114 C CB . HIS A 15 ? 0.4109 0.4785 0.8091 -0.0395 -0.0861 -0.0900 42 HIS A CB 115 C CG . HIS A 15 ? 0.4772 0.5239 0.8627 -0.0456 -0.0835 -0.0834 42 HIS A CG 116 N ND1 . HIS A 15 ? 0.4741 0.5205 0.8784 -0.0408 -0.0959 -0.1007 42 HIS A ND1 117 C CD2 . HIS A 15 ? 0.4281 0.4545 0.7830 -0.0541 -0.0703 -0.0621 42 HIS A CD2 118 C CE1 . HIS A 15 ? 0.4965 0.5238 0.8840 -0.0465 -0.0907 -0.0900 42 HIS A CE1 119 N NE2 . HIS A 15 ? 0.4494 0.4652 0.8062 -0.0540 -0.0754 -0.0669 42 HIS A NE2 120 N N . HIS A 16 ? 0.3961 0.4895 0.7150 0.0243 -0.1095 -0.1028 43 HIS A N 121 C CA . HIS A 16 ? 0.4293 0.5319 0.7321 0.0380 -0.1062 -0.1006 43 HIS A CA 122 C C . HIS A 16 ? 0.4462 0.5253 0.6856 0.0461 -0.0917 -0.0765 43 HIS A C 123 O O . HIS A 16 ? 0.4837 0.5477 0.6886 0.0539 -0.0935 -0.0705 43 HIS A O 124 C CB . HIS A 16 ? 0.4812 0.6073 0.7914 0.0668 -0.1314 -0.1282 43 HIS A CB 125 C CG . HIS A 16 ? 0.5835 0.7354 0.9599 0.0595 -0.1478 -0.1559 43 HIS A CG 126 N ND1 . HIS A 16 ? 0.5951 0.7623 1.0241 0.0384 -0.1390 -0.1586 43 HIS A ND1 127 C CD2 . HIS A 16 ? 0.6242 0.7831 1.0157 0.0694 -0.1683 -0.1806 43 HIS A CD2 128 C CE1 . HIS A 16 ? 0.6153 0.7867 1.0738 0.0350 -0.1470 -0.1791 43 HIS A CE1 129 N NE2 . HIS A 16 ? 0.6240 0.7910 1.0629 0.0531 -0.1653 -0.1937 43 HIS A NE2 130 N N . LYS A 17 ? 0.4569 0.4081 0.6477 -0.0377 0.0175 -0.1137 44 LYS A N 131 C CA . LYS A 17 ? 0.5097 0.4628 0.7088 -0.0320 0.0183 -0.1016 44 LYS A CA 132 C C . LYS A 17 ? 0.5598 0.5287 0.7662 -0.0241 0.0030 -0.1038 44 LYS A C 133 O O . LYS A 17 ? 0.5599 0.5469 0.7859 -0.0260 -0.0094 -0.1121 44 LYS A O 134 C CB . LYS A 17 ? 0.5553 0.5223 0.7728 -0.0324 0.0229 -0.0879 44 LYS A CB 135 C CG . LYS A 17 ? 0.6065 0.5705 0.8082 -0.0333 0.0342 -0.0820 44 LYS A CG 136 C CD . LYS A 17 ? 0.5947 0.5506 0.7758 -0.0289 0.0433 -0.0724 44 LYS A CD 137 C CE . LYS A 17 ? 0.6117 0.5676 0.7820 -0.0292 0.0521 -0.0689 44 LYS A CE 138 N NZ . LYS A 17 ? 0.6149 0.5858 0.8058 -0.0286 0.0527 -0.0683 44 LYS A NZ 139 N N . GLU A 18 ? 0.5159 0.4872 0.6956 -0.0103 0.0039 -0.0886 45 GLU A N 140 C CA . GLU A 18 ? 0.4545 0.4501 0.6270 0.0045 -0.0081 -0.0771 45 GLU A CA 141 C C . GLU A 18 ? 0.4721 0.4723 0.6472 0.0145 -0.0003 -0.0510 45 GLU A C 142 O O . GLU A 18 ? 0.4858 0.4708 0.6635 0.0109 0.0130 -0.0448 45 GLU A O 143 C CB . GLU A 18 ? 0.4712 0.4700 0.6076 0.0146 -0.0161 -0.0857 45 GLU A CB 144 C CG . GLU A 18 ? 0.5882 0.5672 0.6918 0.0188 -0.0052 -0.0813 45 GLU A CG 145 C CD . GLU A 18 ? 0.6735 0.6573 0.7434 0.0285 -0.0139 -0.0919 45 GLU A CD 146 O OE1 . GLU A 18 ? 0.6776 0.6754 0.7524 0.0278 -0.0274 -0.1103 45 GLU A OE1 147 O OE2 . GLU A 18 ? 0.7723 0.7477 0.8124 0.0374 -0.0077 -0.0833 45 GLU A OE2 148 N N . LYS A 19 ? 0.3864 0.4084 0.5623 0.0281 -0.0080 -0.0362 46 LYS A N 149 C CA . LYS A 19 ? 0.3730 0.4005 0.5593 0.0376 0.0007 -0.0109 46 LYS A CA 150 C C . LYS A 19 ? 0.3624 0.3821 0.5149 0.0497 0.0087 0.0007 46 LYS A C 151 O O . LYS A 19 ? 0.3557 0.3760 0.4737 0.0571 0.0024 -0.0060 46 LYS A O 152 C CB . LYS A 19 ? 0.4127 0.4653 0.6154 0.0486 -0.0083 0.0028 46 LYS A CB 153 N N . PRO A 20 ? 0.3317 0.3450 0.4961 0.0517 0.0227 0.0162 47 PRO A N 154 C CA . PRO A 20 ? 0.3603 0.3681 0.4972 0.0639 0.0314 0.0288 47 PRO A CA 155 C C . PRO A 20 ? 0.3972 0.4238 0.5225 0.0828 0.0277 0.0484 47 PRO A C 156 O O . PRO A 20 ? 0.4216 0.4654 0.5616 0.0867 0.0185 0.0527 47 PRO A O 157 C CB . PRO A 20 ? 0.3238 0.3244 0.4888 0.0602 0.0467 0.0380 47 PRO A CB 158 C CG . PRO A 20 ? 0.2548 0.2658 0.4641 0.0524 0.0447 0.0392 47 PRO A CG 159 C CD . PRO A 20 ? 0.2650 0.2773 0.4712 0.0427 0.0312 0.0205 47 PRO A CD 160 N N . GLY A 21 ? 0.3861 0.4095 0.4840 0.0955 0.0352 0.0604 48 GLY A N 161 C CA . GLY A 21 ? 0.3493 0.3893 0.4319 0.1159 0.0344 0.0812 48 GLY A CA 162 C C . GLY A 21 ? 0.3989 0.4315 0.4669 0.1266 0.0500 0.0980 48 GLY A C 163 O O . GLY A 21 ? 0.3736 0.3901 0.4507 0.1176 0.0611 0.0938 48 GLY A O 164 N N . PRO A 22 ? 0.3936 0.4389 0.4389 0.1471 0.0513 0.1171 49 PRO A N 165 C CA . PRO A 22 ? 0.4673 0.5062 0.4978 0.1586 0.0673 0.1342 49 PRO A CA 166 C C . PRO A 22 ? 0.4924 0.5143 0.4919 0.1520 0.0674 0.1158 49 PRO A C 167 O O . PRO A 22 ? 0.5078 0.5295 0.4772 0.1499 0.0535 0.0964 49 PRO A O 168 C CB . PRO A 22 ? 0.5186 0.5764 0.5197 0.1829 0.0638 0.1526 49 PRO A CB 169 C CG . PRO A 22 ? 0.5102 0.5855 0.5300 0.1848 0.0516 0.1541 49 PRO A CG 170 C CD . PRO A 22 ? 0.4663 0.5342 0.4997 0.1622 0.0386 0.1243 49 PRO A CD 171 N N . GLU A 23 ? 0.4058 0.4141 0.4157 0.1490 0.0834 0.1208 50 GLU A N 172 C CA . GLU A 23 ? 0.4319 0.4233 0.4150 0.1438 0.0855 0.1053 50 GLU A CA 173 C C . GLU A 23 ? 0.4417 0.4370 0.3751 0.1581 0.0801 0.1055 50 GLU A C 174 O O . GLU A 23 ? 0.5226 0.5308 0.4443 0.1759 0.0846 0.1261 50 GLU A O 175 C CB . GLU A 23 ? 0.4303 0.4119 0.4355 0.1427 0.1041 0.1138 50 GLU A CB 176 C CG . GLU A 23 ? 0.4458 0.4097 0.4298 0.1367 0.1070 0.0971 50 GLU A CG 177 C CD . GLU A 23 ? 0.4198 0.3804 0.4289 0.1232 0.1180 0.0972 50 GLU A CD 178 O OE1 . GLU A 23 ? 0.4512 0.4183 0.4636 0.1272 0.1284 0.1124 50 GLU A OE1 179 O OE2 . GLU A 23 ? 0.3950 0.3485 0.4189 0.1064 0.1141 0.0811 50 GLU A OE2 180 N N . ASP A 24 ? 0.4214 0.4059 0.3261 0.1513 0.0715 0.0828 51 ASP A N 181 C CA . ASP A 24 ? 0.4565 0.4454 0.3151 0.1644 0.0657 0.0794 51 ASP A CA 182 C C . ASP A 24 ? 0.4722 0.4524 0.3135 0.1733 0.0807 0.0907 51 ASP A C 183 O O . ASP A 24 ? 0.4353 0.4042 0.3005 0.1675 0.0948 0.0966 51 ASP A O 184 C CB . ASP A 24 ? 0.4895 0.4710 0.3270 0.1544 0.0513 0.0499 51 ASP A CB 185 C CG . ASP A 24 ? 0.4774 0.4334 0.3191 0.1386 0.0580 0.0344 51 ASP A CG 186 O OD1 . ASP A 24 ? 0.4977 0.4427 0.3402 0.1401 0.0718 0.0431 51 ASP A OD1 187 O OD2 . ASP A 24 ? 0.4619 0.4092 0.3064 0.1256 0.0499 0.0132 51 ASP A OD2 188 N N . LYS A 25 ? 0.4700 0.4574 0.2707 0.1882 0.0772 0.0919 52 LYS A N 189 C CA . LYS A 25 ? 0.5086 0.4908 0.2932 0.1977 0.0904 0.1021 52 LYS A CA 190 C C . LYS A 25 ? 0.5456 0.5046 0.3311 0.1840 0.0950 0.0855 52 LYS A C 191 O O . LYS A 25 ? 0.5521 0.5038 0.3586 0.1824 0.1062 0.0921 52 LYS A O 192 C CB . LYS A 25 ? 0.5791 0.5765 0.3345 0.2107 0.0803 0.0976 52 LYS A CB 193 C CG . LYS A 25 ? 0.6723 0.6677 0.4291 0.2162 0.0897 0.1031 52 LYS A CG 194 C CD . LYS A 25 ? 0.7089 0.7109 0.4977 0.2226 0.1077 0.1262 52 LYS A CD 195 C CE . LYS A 25 ? 0.7822 0.7894 0.5653 0.2341 0.1151 0.1330 52 LYS A CE 196 N NZ . LYS A 25 ? 0.8468 0.8715 0.5987 0.2479 0.1038 0.1308 52 LYS A NZ 197 N N . LEU A 26 ? 0.5428 0.4911 0.3100 0.1741 0.0850 0.0620 53 LEU A N 198 C CA . LEU A 26 ? 0.4823 0.4090 0.2550 0.1595 0.0854 0.0460 53 LEU A CA 199 C C . LEU A 26 ? 0.4667 0.3835 0.2741 0.1503 0.0971 0.0514 53 LEU A C 200 O O . LEU A 26 ? 0.4971 0.4020 0.3134 0.1416 0.0975 0.0478 53 LEU A O 201 C CB . LEU A 26 ? 0.4763 0.3932 0.2355 0.1482 0.0739 0.0209 53 LEU A CB 202 C CG . LEU A 26 ? 0.4818 0.3792 0.2501 0.1311 0.0724 0.0076 53 LEU A CG 203 C CD1 . LEU A 26 ? 0.4685 0.3657 0.2271 0.1332 0.0704 0.0097 53 LEU A CD1 204 C CD2 . LEU A 26 ? 0.4949 0.3844 0.2593 0.1194 0.0640 -0.0139 53 LEU A CD2 205 N N . HIS A 27 ? 0.4595 0.3846 0.2940 0.1498 0.1022 0.0595 54 HIS A N 206 C CA . HIS A 27 ? 0.3524 0.2718 0.2272 0.1393 0.1104 0.0609 54 HIS A CA 207 C C . HIS A 27 ? 0.3927 0.3231 0.2966 0.1430 0.1209 0.0833 54 HIS A C 208 O O . HIS A 27 ? 0.4166 0.3514 0.3593 0.1289 0.1227 0.0846 54 HIS A O 209 C CB . HIS A 27 ? 0.3081 0.2280 0.2077 0.1272 0.1032 0.0508 54 HIS A CB 210 C CG . HIS A 27 ? 0.4069 0.3115 0.2877 0.1167 0.0948 0.0280 54 HIS A CG 211 N ND1 . HIS A 27 ? 0.4382 0.3430 0.2901 0.1173 0.0829 0.0171 54 HIS A ND1 212 C CD2 . HIS A 27 ? 0.4057 0.2983 0.2971 0.1009 0.0929 0.0154 54 HIS A CD2 213 C CE1 . HIS A 27 ? 0.4099 0.2977 0.2548 0.1066 0.0805 -0.0020 54 HIS A CE1 214 N NE2 . HIS A 27 ? 0.4298 0.3114 0.2989 0.0959 0.0855 -0.0012 54 HIS A NE2 215 N N . GLU A 28 ? 0.4468 0.3265 0.2997 0.0758 0.0846 0.0812 55 GLU A N 216 C CA . GLU A 28 ? 0.5354 0.3971 0.3868 0.0729 0.1017 0.0960 55 GLU A CA 217 C C . GLU A 28 ? 0.5414 0.4084 0.4300 0.0618 0.1172 0.0892 55 GLU A C 218 O O . GLU A 28 ? 0.5814 0.4337 0.4834 0.0585 0.1266 0.0983 55 GLU A O 219 C CB . GLU A 28 ? 0.6849 0.5366 0.4961 0.0741 0.1138 0.1067 55 GLU A CB 220 C CG . GLU A 28 ? 0.8289 0.6640 0.6416 0.0700 0.1336 0.1237 55 GLU A CG 221 C CD . GLU A 28 ? 0.9793 0.8051 0.7485 0.0735 0.1438 0.1387 55 GLU A CD 222 O OE1 . GLU A 28 ? 1.0465 0.8657 0.7842 0.0819 0.1319 0.1503 55 GLU A OE1 223 O OE2 . GLU A 28 ? 0.9995 0.8268 0.7662 0.0676 0.1637 0.1397 55 GLU A OE2 224 N N . GLN A 29 ? 0.4652 0.3539 0.3721 0.0557 0.1196 0.0736 56 GLN A N 225 C CA . GLN A 29 ? 0.4538 0.3525 0.3950 0.0438 0.1332 0.0675 56 GLN A CA 226 C C . GLN A 29 ? 0.4606 0.3664 0.4356 0.0409 0.1243 0.0588 56 GLN A C 227 O O . GLN A 29 ? 0.4887 0.3981 0.4904 0.0302 0.1344 0.0545 56 GLN A O 228 C CB . GLN A 29 ? 0.4827 0.4047 0.4326 0.0384 0.1406 0.0572 56 GLN A CB 229 C CG . GLN A 29 ? 0.4402 0.3851 0.4041 0.0414 0.1250 0.0433 56 GLN A CG 230 C CD . GLN A 29 ? 0.4598 0.4235 0.4284 0.0389 0.1336 0.0367 56 GLN A CD 231 O OE1 . GLN A 29 ? 0.4858 0.4450 0.4289 0.0457 0.1316 0.0351 56 GLN A OE1 232 N NE2 . GLN A 29 ? 0.4434 0.4284 0.4452 0.0288 0.1434 0.0326 56 GLN A NE2 233 N N . CYS A 30 ? 0.3791 0.2881 0.3529 0.0499 0.1056 0.0558 57 CYS A N 234 C CA . CYS A 30 ? 0.3773 0.2911 0.3793 0.0498 0.0977 0.0490 57 CYS A CA 235 C C . CYS A 30 ? 0.4846 0.3691 0.4849 0.0529 0.1026 0.0612 57 CYS A C 236 O O . CYS A 30 ? 0.4680 0.3437 0.4661 0.0632 0.0908 0.0670 57 CYS A O 237 C CB . CYS A 30 ? 0.3940 0.3237 0.3976 0.0590 0.0768 0.0434 57 CYS A CB 238 S SG . CYS A 30 ? 0.3761 0.3375 0.3850 0.0562 0.0712 0.0309 57 CYS A SG 239 N N . ARG A 31 ? 0.4966 0.3667 0.5006 0.0439 0.1206 0.0664 58 ARG A N 240 C CA . ARG A 31 ? 0.5914 0.4303 0.5935 0.0459 0.1289 0.0812 58 ARG A CA 241 C C . ARG A 31 ? 0.4930 0.3211 0.5164 0.0513 0.1224 0.0786 58 ARG A C 242 O O . ARG A 31 ? 0.5227 0.3292 0.5366 0.0618 0.1195 0.0945 58 ARG A O 243 C CB . ARG A 31 ? 0.7040 0.5336 0.7177 0.0318 0.1496 0.0833 58 ARG A CB 244 C CG . ARG A 31 ? 0.8665 0.7016 0.8583 0.0284 0.1601 0.0911 58 ARG A CG 245 C CD . ARG A 31 ? 1.0269 0.8415 0.9833 0.0390 0.1615 0.1131 58 ARG A CD 246 N NE . ARG A 31 ? 1.1123 0.9352 1.0435 0.0376 0.1708 0.1179 58 ARG A NE 247 C CZ . ARG A 31 ? 1.1853 0.9954 1.0819 0.0445 0.1755 0.1361 58 ARG A CZ 248 N NH1 . ARG A 31 ? 1.1927 0.9823 1.0772 0.0529 0.1708 0.1536 58 ARG A NH1 249 N NH2 . ARG A 31 ? 1.2304 1.0496 1.1049 0.0433 0.1856 0.1376 58 ARG A NH2 250 N N . PRO A 32 ? 0.4491 0.2930 0.5017 0.0443 0.1210 0.0593 59 PRO A N 251 C CA . PRO A 32 ? 0.4558 0.2884 0.5300 0.0488 0.1183 0.0542 59 PRO A CA 252 C C . PRO A 32 ? 0.4763 0.3065 0.5411 0.0667 0.1022 0.0641 59 PRO A C 253 O O . PRO A 32 ? 0.5194 0.3314 0.5976 0.0741 0.1029 0.0682 59 PRO A O 254 C CB . PRO A 32 ? 0.4150 0.2765 0.5142 0.0389 0.1163 0.0304 59 PRO A CB 255 C CG . PRO A 32 ? 0.3314 0.2081 0.4298 0.0243 0.1257 0.0260 59 PRO A CG 256 C CD . PRO A 32 ? 0.3929 0.2667 0.4606 0.0316 0.1234 0.0419 59 PRO A CD 257 N N . TRP A 33 ? 0.4367 0.2844 0.4803 0.0731 0.0884 0.0682 60 TRP A N 258 C CA . TRP A 33 ? 0.3952 0.2476 0.4320 0.0880 0.0703 0.0762 60 TRP A CA 259 C C . TRP A 33 ? 0.4055 0.2420 0.4103 0.0973 0.0654 0.0991 60 TRP A C 260 O O . TRP A 33 ? 0.4776 0.3224 0.4712 0.1078 0.0483 0.1067 60 TRP A O 261 C CB . TRP A 33 ? 0.4166 0.3026 0.4554 0.0881 0.0554 0.0632 60 TRP A CB 262 C CG . TRP A 33 ? 0.4060 0.3125 0.4762 0.0815 0.0571 0.0438 60 TRP A CG 263 C CD1 . TRP A 33 ? 0.3977 0.3119 0.4901 0.0879 0.0508 0.0380 60 TRP A CD1 264 C CD2 . TRP A 33 ? 0.3805 0.3051 0.4634 0.0671 0.0664 0.0285 60 TRP A CD2 265 N NE1 . TRP A 33 ? 0.3409 0.2771 0.4561 0.0781 0.0552 0.0191 60 TRP A NE1 266 C CE2 . TRP A 33 ? 0.3466 0.2904 0.4572 0.0648 0.0641 0.0135 60 TRP A CE2 267 C CE3 . TRP A 33 ? 0.3530 0.2815 0.4272 0.0562 0.0767 0.0270 60 TRP A CE3 268 C CZ2 . TRP A 33 ? 0.2918 0.2601 0.4205 0.0513 0.0703 -0.0023 60 TRP A CZ2 269 C CZ3 . TRP A 33 ? 0.3144 0.2668 0.4097 0.0432 0.0831 0.0122 60 TRP A CZ3 270 C CH2 . TRP A 33 ? 0.2376 0.2103 0.3592 0.0404 0.0792 -0.0020 60 TRP A CH2 271 N N . ARG A 34 ? 0.3250 0.2848 0.5596 0.0434 0.0182 0.1930 61 ARG A N 272 C CA . ARG A 34 ? 0.4775 0.4505 0.6896 0.0553 0.0322 0.2214 61 ARG A CA 273 C C . ARG A 34 ? 0.4726 0.4383 0.6670 0.0679 0.0205 0.2167 61 ARG A C 274 O O . ARG A 34 ? 0.5024 0.4849 0.6543 0.0777 0.0263 0.2213 61 ARG A O 275 C CB . ARG A 34 ? 0.5749 0.5549 0.8162 0.0465 0.0406 0.2480 61 ARG A CB 276 C CG . ARG A 34 ? 0.6458 0.6421 0.8533 0.0557 0.0594 0.2709 61 ARG A CG 277 C CD . ARG A 34 ? 0.7846 0.7866 1.0261 0.0490 0.0689 0.2954 61 ARG A CD 278 N NE . ARG A 34 ? 0.9150 0.8968 1.1958 0.0426 0.0518 0.2998 61 ARG A NE 279 C CZ . ARG A 34 ? 0.9756 0.9452 1.2472 0.0499 0.0463 0.3119 61 ARG A CZ 280 N NH1 . ARG A 34 ? 1.0170 0.9947 1.2400 0.0623 0.0527 0.3223 61 ARG A NH1 281 N NH2 . ARG A 34 ? 0.9591 0.9069 1.2686 0.0443 0.0339 0.3138 61 ARG A NH2 282 N N . LYS A 35 ? 0.4737 0.4142 0.7001 0.0668 0.0041 0.2065 62 LYS A N 283 C CA . LYS A 35 ? 0.4929 0.4283 0.7166 0.0800 -0.0058 0.2071 62 LYS A CA 284 C C . LYS A 35 ? 0.4512 0.3903 0.6589 0.0890 -0.0137 0.1730 62 LYS A C 285 O O . LYS A 35 ? 0.4901 0.4382 0.6939 0.1023 -0.0211 0.1773 62 LYS A O 286 C CB . LYS A 35 ? 0.4900 0.3977 0.7521 0.0742 -0.0130 0.2104 62 LYS A CB 287 C CG . LYS A 35 ? 0.6316 0.5432 0.9067 0.0672 -0.0050 0.2428 62 LYS A CG 288 C CD . LYS A 35 ? 0.7716 0.6532 1.0861 0.0611 -0.0111 0.2445 62 LYS A CD 289 C CE . LYS A 35 ? 0.8965 0.7835 1.2280 0.0546 -0.0020 0.2771 62 LYS A CE 290 N NZ . LYS A 35 ? 0.9844 0.8401 1.3558 0.0472 -0.0070 0.2788 62 LYS A NZ 291 N N . ASN A 36 ? 0.4345 0.3697 0.6332 0.0802 -0.0122 0.1387 63 ASN A N 292 C CA . ASN A 36 ? 0.4219 0.3583 0.6067 0.0858 -0.0158 0.1024 63 ASN A CA 293 C C . ASN A 36 ? 0.4220 0.3654 0.5784 0.0762 -0.0086 0.0739 63 ASN A C 294 O O . ASN A 36 ? 0.4042 0.3267 0.5704 0.0649 -0.0110 0.0588 63 ASN A O 295 C CB . ASN A 36 ? 0.4139 0.3143 0.6334 0.0882 -0.0231 0.0874 63 ASN A CB 296 C CG . ASN A 36 ? 0.4425 0.3475 0.6586 0.1000 -0.0235 0.0605 63 ASN A CG 297 O OD1 . ASN A 36 ? 0.4745 0.4117 0.6789 0.1103 -0.0255 0.0672 63 ASN A OD1 298 N ND2 . ASN A 36 ? 0.4347 0.3069 0.6602 0.0973 -0.0213 0.0300 63 ASN A ND2 299 N N . ALA A 37 ? 0.3796 0.3505 0.4989 0.0798 -0.0009 0.0672 64 ALA A N 300 C CA . ALA A 37 ? 0.3181 0.2962 0.4100 0.0723 0.0098 0.0474 64 ALA A CA 301 C C . ALA A 37 ? 0.3417 0.3370 0.3990 0.0764 0.0149 0.0230 64 ALA A C 302 O O . ALA A 37 ? 0.3704 0.3830 0.4162 0.0833 0.0110 0.0292 64 ALA A O 303 C CB . ALA A 37 ? 0.3351 0.3255 0.4190 0.0678 0.0229 0.0735 64 ALA A CB 304 N N . CYS A 38 ? 0.3113 0.3022 0.3525 0.0707 0.0223 -0.0031 65 CYS A N 305 C CA . CYS A 38 ? 0.3728 0.3779 0.3809 0.0715 0.0311 -0.0259 65 CYS A CA 306 C C . CYS A 38 ? 0.3637 0.3824 0.3379 0.0692 0.0471 -0.0151 65 CYS A C 307 O O . CYS A 38 ? 0.4374 0.4660 0.3789 0.0679 0.0559 -0.0308 65 CYS A O 308 C CB . CYS A 38 ? 0.3042 0.2943 0.3073 0.0669 0.0352 -0.0568 65 CYS A CB 309 S SG . CYS A 38 ? 0.3586 0.3259 0.3899 0.0704 0.0249 -0.0762 65 CYS A SG 310 N N . CYS A 39 ? 0.3313 0.3483 0.3153 0.0679 0.0532 0.0115 66 CYS A N 311 C CA . CYS A 39 ? 0.3863 0.4125 0.3405 0.0682 0.0736 0.0264 66 CYS A CA 312 C C . CYS A 39 ? 0.4048 0.4386 0.3501 0.0722 0.0702 0.0531 66 CYS A C 313 O O . CYS A 39 ? 0.4243 0.4567 0.3858 0.0730 0.0764 0.0831 66 CYS A O 314 C CB . CYS A 39 ? 0.3551 0.3780 0.3314 0.0655 0.0861 0.0428 66 CYS A CB 315 S SG . CYS A 39 ? 0.3326 0.3503 0.3658 0.0621 0.0712 0.0739 66 CYS A SG 316 N N . SER A 40 ? 0.4656 0.5088 0.3869 0.0740 0.0594 0.0442 67 SER A N 317 C CA . SER A 40 ? 0.5612 0.6120 0.4782 0.0784 0.0478 0.0708 67 SER A CA 318 C C . SER A 40 ? 0.6200 0.6811 0.4761 0.0757 0.0528 0.0728 67 SER A C 319 O O . SER A 40 ? 0.5294 0.5931 0.3501 0.0697 0.0599 0.0462 67 SER A O 320 C CB . SER A 40 ? 0.5652 0.6194 0.5197 0.0839 0.0224 0.0670 67 SER A CB 321 O OG . SER A 40 ? 0.5875 0.6523 0.5326 0.0823 0.0161 0.0360 67 SER A OG 322 N N . THR A 41 ? 0.7824 0.8462 0.6238 0.0787 0.0485 0.1048 68 THR A N 323 C CA . THR A 41 ? 0.9084 0.9789 0.6837 0.0744 0.0485 0.1111 68 THR A CA 324 C C . THR A 41 ? 0.9053 0.9940 0.6664 0.0694 0.0245 0.0865 68 THR A C 325 O O . THR A 41 ? 0.9349 1.0235 0.6455 0.0593 0.0322 0.0631 68 THR A O 326 C CB . THR A 41 ? 1.0014 1.0727 0.7710 0.0798 0.0402 0.1534 68 THR A CB 327 O OG1 . THR A 41 ? 0.9550 1.0112 0.7419 0.0827 0.0651 0.1780 68 THR A OG1 328 C CG2 . THR A 41 ? 1.1260 1.1990 0.8216 0.0711 0.0363 0.1568 68 THR A CG2 329 N N . LYS A 49 ? 0.6969 1.0836 0.6170 -0.0626 -0.0444 -0.0125 76 LYS A N 330 C CA . LYS A 49 ? 0.7008 1.0956 0.6405 -0.0525 -0.0471 0.0203 76 LYS A CA 331 C C . LYS A 49 ? 0.6785 1.0216 0.6303 -0.0418 -0.0338 0.0317 76 LYS A C 332 O O . LYS A 49 ? 0.7239 1.0451 0.6974 -0.0402 -0.0299 0.0335 76 LYS A O 333 C CB . LYS A 49 ? 0.6989 1.1336 0.6252 -0.0469 -0.0537 0.0444 76 LYS A CB 334 N N . ASP A 50 ? 0.5527 0.8765 0.4906 -0.0347 -0.0264 0.0382 77 ASP A N 335 C CA . ASP A 50 ? 0.4694 0.7485 0.4170 -0.0249 -0.0153 0.0484 77 ASP A CA 336 C C . ASP A 50 ? 0.4804 0.7149 0.4264 -0.0265 -0.0077 0.0258 77 ASP A C 337 O O . ASP A 50 ? 0.5305 0.7648 0.4666 -0.0346 -0.0083 0.0016 77 ASP A O 338 C CB . ASP A 50 ? 0.4648 0.7394 0.4019 -0.0177 -0.0101 0.0606 77 ASP A CB 339 C CG . ASP A 50 ? 0.4439 0.7002 0.3609 -0.0208 -0.0060 0.0381 77 ASP A CG 340 O OD1 . ASP A 50 ? 0.3796 0.5953 0.2982 -0.0182 0.0007 0.0272 77 ASP A OD1 341 O OD2 . ASP A 50 ? 0.4586 0.7417 0.3580 -0.0253 -0.0090 0.0321 77 ASP A OD2 342 N N . VAL A 51 ? 0.4513 0.6480 0.4069 -0.0183 0.0004 0.0342 78 VAL A N 343 C CA . VAL A 51 ? 0.4274 0.5802 0.3790 -0.0167 0.0082 0.0176 78 VAL A CA 344 C C . VAL A 51 ? 0.4019 0.5233 0.3492 -0.0073 0.0145 0.0252 78 VAL A C 345 O O . VAL A 51 ? 0.4030 0.4885 0.3525 -0.0020 0.0208 0.0237 78 VAL A O 346 C CB . VAL A 51 ? 0.4241 0.5603 0.3929 -0.0166 0.0122 0.0175 78 VAL A CB 347 C CG1 . VAL A 51 ? 0.3743 0.5407 0.3516 -0.0272 0.0060 0.0058 78 VAL A CG1 348 C CG2 . VAL A 51 ? 0.4602 0.5944 0.4466 -0.0095 0.0147 0.0425 78 VAL A CG2 349 N N . SER A 52 ? 0.3905 0.5264 0.3315 -0.0055 0.0130 0.0326 79 SER A N 350 C CA . SER A 52 ? 0.3805 0.4942 0.3247 0.0025 0.0182 0.0427 79 SER A CA 351 C C . SER A 52 ? 0.3476 0.4323 0.2798 0.0047 0.0208 0.0264 79 SER A C 352 O O . SER A 52 ? 0.2776 0.3710 0.1986 0.0010 0.0192 0.0138 79 SER A O 353 C CB . SER A 52 ? 0.2559 0.3983 0.2054 0.0045 0.0178 0.0617 79 SER A CB 354 O OG . SER A 52 ? 0.2826 0.4033 0.2379 0.0107 0.0240 0.0673 79 SER A OG 355 N N . TYR A 53 ? 0.3313 0.3825 0.2665 0.0110 0.0249 0.0272 80 TYR A N 356 C CA . TYR A 53 ? 0.3115 0.3375 0.2376 0.0146 0.0255 0.0147 80 TYR A CA 357 C C . TYR A 53 ? 0.3698 0.4047 0.3016 0.0164 0.0256 0.0207 80 TYR A C 358 O O . TYR A 53 ? 0.3774 0.3934 0.3078 0.0200 0.0255 0.0133 80 TYR A O 359 C CB . TYR A 53 ? 0.2796 0.2690 0.2038 0.0208 0.0288 0.0125 80 TYR A CB 360 C CG . TYR A 53 ? 0.3035 0.2743 0.2171 0.0211 0.0304 -0.0001 80 TYR A CG 361 C CD1 . TYR A 53 ? 0.3193 0.3073 0.2326 0.0146 0.0300 -0.0072 80 TYR A CD1 362 C CD2 . TYR A 53 ? 0.3307 0.2671 0.2349 0.0281 0.0332 -0.0053 80 TYR A CD2 363 C CE1 . TYR A 53 ? 0.3678 0.3373 0.2760 0.0149 0.0344 -0.0187 80 TYR A CE1 364 C CE2 . TYR A 53 ? 0.3235 0.2418 0.2190 0.0299 0.0372 -0.0144 80 TYR A CE2 365 C CZ . TYR A 53 ? 0.3705 0.3046 0.2703 0.0233 0.0387 -0.0209 80 TYR A CZ 366 O OH . TYR A 53 ? 0.3971 0.3117 0.2927 0.0252 0.0454 -0.0298 80 TYR A OH 367 N N . LEU A 54 ? 0.3620 0.4268 0.3016 0.0144 0.0262 0.0350 81 LEU A N 368 C CA . LEU A 54 ? 0.3609 0.4363 0.3067 0.0159 0.0286 0.0409 81 LEU A CA 369 C C . LEU A 54 ? 0.3421 0.4258 0.2751 0.0125 0.0269 0.0259 81 LEU A C 370 O O . LEU A 54 ? 0.3589 0.4437 0.2968 0.0140 0.0296 0.0256 81 LEU A O 371 C CB . LEU A 54 ? 0.3433 0.4484 0.3007 0.0165 0.0318 0.0635 81 LEU A CB 372 C CG . LEU A 54 ? 0.3401 0.4363 0.3175 0.0211 0.0373 0.0812 81 LEU A CG 373 C CD1 . LEU A 54 ? 0.2649 0.3942 0.2546 0.0229 0.0409 0.1063 81 LEU A CD1 374 C CD2 . LEU A 54 ? 0.3448 0.4135 0.3345 0.0249 0.0428 0.0779 81 LEU A CD2 375 N N . TYR A 55 ? 0.3258 0.4142 0.2453 0.0075 0.0239 0.0129 82 TYR A N 376 C CA . TYR A 55 ? 0.3553 0.4480 0.2639 0.0038 0.0246 -0.0032 82 TYR A CA 377 C C . TYR A 55 ? 0.3917 0.4725 0.2907 0.0000 0.0241 -0.0220 82 TYR A C 378 O O . TYR A 55 ? 0.3901 0.4655 0.2839 -0.0015 0.0269 -0.0364 82 TYR A O 379 C CB . TYR A 55 ? 0.3177 0.4458 0.2199 -0.0007 0.0258 0.0023 82 TYR A CB 380 C CG . TYR A 55 ? 0.3099 0.4646 0.2029 -0.0074 0.0215 0.0017 82 TYR A CG 381 C CD1 . TYR A 55 ? 0.2875 0.4498 0.1674 -0.0153 0.0211 -0.0183 82 TYR A CD1 382 C CD2 . TYR A 55 ? 0.2960 0.4692 0.1961 -0.0062 0.0181 0.0207 82 TYR A CD2 383 C CE1 . TYR A 55 ? 0.3131 0.5021 0.1864 -0.0228 0.0160 -0.0218 82 TYR A CE1 384 C CE2 . TYR A 55 ? 0.3629 0.5645 0.2570 -0.0126 0.0121 0.0198 82 TYR A CE2 385 C CZ . TYR A 55 ? 0.3591 0.5691 0.2394 -0.0214 0.0103 -0.0026 82 TYR A CZ 386 O OH . TYR A 55 ? 0.3354 0.5756 0.2114 -0.0291 0.0032 -0.0066 82 TYR A OH 387 N N . ARG A 56 ? 0.3654 0.4413 0.2654 -0.0012 0.0225 -0.0213 83 ARG A N 388 C CA . ARG A 56 ? 0.3805 0.4450 0.2756 -0.0049 0.0245 -0.0382 83 ARG A CA 389 C C . ARG A 56 ? 0.4065 0.4334 0.3009 0.0024 0.0277 -0.0453 83 ARG A C 390 O O . ARG A 56 ? 0.3864 0.4001 0.2785 0.0012 0.0320 -0.0582 83 ARG A O 391 C CB . ARG A 56 ? 0.3988 0.4748 0.2987 -0.0094 0.0225 -0.0352 83 ARG A CB 392 C CG . ARG A 56 ? 0.4215 0.5392 0.3192 -0.0178 0.0177 -0.0330 83 ARG A CG 393 C CD . ARG A 56 ? 0.4455 0.5769 0.3531 -0.0216 0.0140 -0.0278 83 ARG A CD 394 N NE . ARG A 56 ? 0.4368 0.6128 0.3415 -0.0290 0.0068 -0.0246 83 ARG A NE 395 C CZ . ARG A 56 ? 0.3880 0.5849 0.2859 -0.0394 0.0045 -0.0434 83 ARG A CZ 396 N NH1 . ARG A 56 ? 0.3318 0.5070 0.2291 -0.0436 0.0110 -0.0659 83 ARG A NH1 397 N NH2 . ARG A 56 ? 0.3585 0.5988 0.2508 -0.0456 -0.0038 -0.0397 83 ARG A NH2 398 N N . PHE A 57 ? 0.3544 0.3650 0.2514 0.0101 0.0260 -0.0369 84 PHE A N 399 C CA . PHE A 57 ? 0.3195 0.2978 0.2129 0.0181 0.0269 -0.0421 84 PHE A CA 400 C C . PHE A 57 ? 0.3585 0.3327 0.2532 0.0219 0.0251 -0.0469 84 PHE A C 401 O O . PHE A 57 ? 0.4098 0.3959 0.3116 0.0217 0.0228 -0.0405 84 PHE A O 402 C CB . PHE A 57 ? 0.3028 0.2629 0.1971 0.0239 0.0258 -0.0316 84 PHE A CB 403 C CG . PHE A 57 ? 0.3258 0.2535 0.2109 0.0325 0.0264 -0.0367 84 PHE A CG 404 C CD1 . PHE A 57 ? 0.3199 0.2299 0.1986 0.0347 0.0321 -0.0400 84 PHE A CD1 405 C CD2 . PHE A 57 ? 0.2952 0.2115 0.1787 0.0387 0.0216 -0.0377 84 PHE A CD2 406 C CE1 . PHE A 57 ? 0.3517 0.2326 0.2191 0.0443 0.0336 -0.0423 84 PHE A CE1 407 C CE2 . PHE A 57 ? 0.3265 0.2163 0.1983 0.0475 0.0206 -0.0415 84 PHE A CE2 408 C CZ . PHE A 57 ? 0.3495 0.2211 0.2113 0.0510 0.0269 -0.0428 84 PHE A CZ 409 N N . ASN A 58 ? 0.3891 0.3465 0.2798 0.0259 0.0273 -0.0572 85 ASN A N 410 C CA . ASN A 58 ? 0.4296 0.3834 0.3250 0.0304 0.0254 -0.0616 85 ASN A CA 411 C C . ASN A 58 ? 0.4157 0.3519 0.3113 0.0392 0.0182 -0.0571 85 ASN A C 412 O O . ASN A 58 ? 0.3773 0.2920 0.2647 0.0469 0.0171 -0.0593 85 ASN A O 413 C CB . ASN A 58 ? 0.4184 0.3634 0.3126 0.0317 0.0318 -0.0732 85 ASN A CB 414 C CG . ASN A 58 ? 0.4221 0.3666 0.3252 0.0361 0.0307 -0.0770 85 ASN A CG 415 O OD1 . ASN A 58 ? 0.4104 0.3679 0.3221 0.0349 0.0270 -0.0736 85 ASN A OD1 416 N ND2 . ASN A 58 ? 0.4095 0.3392 0.3137 0.0419 0.0353 -0.0830 85 ASN A ND2 417 N N . TRP A 59 ? 0.3538 0.2836 0.2561 0.0486 0.0585 0.0175 86 TRP A N 418 C CA . TRP A 59 ? 0.3347 0.2669 0.2578 0.0404 0.0610 0.0136 86 TRP A CA 419 C C . TRP A 59 ? 0.3168 0.2703 0.2559 0.0434 0.0582 -0.0016 86 TRP A C 420 O O . TRP A 59 ? 0.3228 0.2752 0.2761 0.0413 0.0522 -0.0096 86 TRP A O 421 C CB . TRP A 59 ? 0.3546 0.2858 0.2856 0.0284 0.0737 0.0245 86 TRP A CB 422 C CG . TRP A 59 ? 0.3941 0.3034 0.3090 0.0274 0.0743 0.0387 86 TRP A CG 423 C CD1 . TRP A 59 ? 0.4383 0.3444 0.3385 0.0248 0.0818 0.0512 86 TRP A CD1 424 C CD2 . TRP A 59 ? 0.3444 0.2334 0.2559 0.0305 0.0661 0.0407 86 TRP A CD2 425 N NE1 . TRP A 59 ? 0.4087 0.2908 0.2978 0.0267 0.0761 0.0605 86 TRP A NE1 426 C CE2 . TRP A 59 ? 0.3720 0.2460 0.2703 0.0305 0.0673 0.0534 86 TRP A CE2 427 C CE3 . TRP A 59 ? 0.3609 0.2444 0.2780 0.0338 0.0583 0.0328 86 TRP A CE3 428 C CZ2 . TRP A 59 ? 0.4085 0.2655 0.3049 0.0348 0.0604 0.0564 86 TRP A CZ2 429 C CZ3 . TRP A 59 ? 0.3775 0.2467 0.2905 0.0371 0.0545 0.0367 86 TRP A CZ3 430 C CH2 . TRP A 59 ? 0.3882 0.2458 0.2936 0.0381 0.0553 0.0474 86 TRP A CH2 431 N N . ASN A 60 ? 0.3050 0.2780 0.2410 0.0501 0.0615 -0.0071 87 ASN A N 432 C CA . ASN A 60 ? 0.3332 0.3319 0.2879 0.0554 0.0592 -0.0237 87 ASN A CA 433 C C . ASN A 60 ? 0.3954 0.3865 0.3411 0.0698 0.0395 -0.0367 87 ASN A C 434 O O . ASN A 60 ? 0.3302 0.3403 0.2791 0.0811 0.0359 -0.0501 87 ASN A O 435 C CB . ASN A 60 ? 0.2928 0.3233 0.2519 0.0559 0.0753 -0.0250 87 ASN A CB 436 C CG . ASN A 60 ? 0.3758 0.4137 0.3446 0.0385 0.0944 -0.0101 87 ASN A CG 437 O OD1 . ASN A 60 ? 0.4081 0.4350 0.3929 0.0266 0.0940 -0.0054 87 ASN A OD1 438 N ND2 . ASN A 60 ? 0.3913 0.4455 0.3479 0.0369 0.1101 -0.0024 87 ASN A ND2 439 N N . HIS A 61 ? 0.3758 0.3394 0.3100 0.0696 0.0265 -0.0329 88 HIS A N 440 C CA . HIS A 61 ? 0.3685 0.3184 0.2908 0.0801 0.0060 -0.0411 88 HIS A CA 441 C C . HIS A 61 ? 0.3519 0.3091 0.2894 0.0855 -0.0063 -0.0575 88 HIS A C 442 O O . HIS A 61 ? 0.3398 0.2882 0.2695 0.0964 -0.0250 -0.0671 88 HIS A O 443 C CB . HIS A 61 ? 0.3339 0.2550 0.2385 0.0756 -0.0021 -0.0292 88 HIS A CB 444 C CG . HIS A 61 ? 0.3085 0.2225 0.2186 0.0655 0.0046 -0.0228 88 HIS A CG 445 N ND1 . HIS A 61 ? 0.2831 0.1952 0.1942 0.0580 0.0183 -0.0113 88 HIS A ND1 446 C CD2 . HIS A 61 ? 0.2728 0.1789 0.1851 0.0636 -0.0026 -0.0277 88 HIS A CD2 447 C CE1 . HIS A 61 ? 0.3080 0.2126 0.2234 0.0527 0.0195 -0.0109 88 HIS A CE1 448 N NE2 . HIS A 61 ? 0.3009 0.2023 0.2158 0.0558 0.0076 -0.0206 88 HIS A NE2 449 N N . CYS A 62 ? 0.3152 0.2855 0.2747 0.0781 0.0015 -0.0608 89 CYS A N 450 C CA . CYS A 62 ? 0.2947 0.2755 0.2736 0.0836 -0.0107 -0.0781 89 CYS A CA 451 C C . CYS A 62 ? 0.2861 0.3054 0.2992 0.0798 0.0041 -0.0861 89 CYS A C 452 O O . CYS A 62 ? 0.3342 0.3601 0.3697 0.0720 0.0049 -0.0898 89 CYS A O 453 C CB . CYS A 62 ? 0.2410 0.1986 0.2152 0.0783 -0.0210 -0.0766 89 CYS A CB 454 S SG . CYS A 62 ? 0.3756 0.2938 0.3124 0.0819 -0.0401 -0.0690 89 CYS A SG 455 N N . GLY A 63 ? 0.3198 0.3655 0.3368 0.0848 0.0157 -0.0888 90 GLY A N 456 C CA . GLY A 63 ? 0.2867 0.3731 0.3345 0.0776 0.0351 -0.0920 90 GLY A CA 457 C C . GLY A 63 ? 0.3606 0.4416 0.4050 0.0591 0.0554 -0.0707 90 GLY A C 458 O O . GLY A 63 ? 0.3675 0.4155 0.3872 0.0551 0.0533 -0.0565 90 GLY A O 459 N N . GLU A 64 ? 0.3723 0.4860 0.4426 0.0475 0.0743 -0.0681 91 GLU A N 460 C CA . GLU A 64 ? 0.3960 0.5015 0.4612 0.0293 0.0917 -0.0465 91 GLU A CA 461 C C . GLU A 64 ? 0.3526 0.4286 0.4252 0.0173 0.0840 -0.0396 91 GLU A C 462 O O . GLU A 64 ? 0.3508 0.4345 0.4525 0.0131 0.0764 -0.0501 91 GLU A O 463 C CB . GLU A 64 ? 0.4349 0.5835 0.5249 0.0173 0.1146 -0.0430 91 GLU A CB 464 C CG . GLU A 64 ? 0.6264 0.7626 0.7015 -0.0006 0.1322 -0.0177 91 GLU A CG 465 C CD . GLU A 64 ? 0.8224 0.9994 0.9251 -0.0185 0.1551 -0.0105 91 GLU A CD 466 O OE1 . GLU A 64 ? 0.8740 1.0979 1.0031 -0.0131 0.1621 -0.0265 91 GLU A OE1 467 O OE2 . GLU A 64 ? 0.8893 1.0516 0.9883 -0.0383 0.1656 0.0112 91 GLU A OE2 468 N N . MET A 65 ? 0.3605 0.4030 0.4068 0.0135 0.0844 -0.0238 92 MET A N 469 C CA . MET A 65 ? 0.3592 0.3741 0.4100 0.0037 0.0787 -0.0175 92 MET A CA 470 C C . MET A 65 ? 0.3288 0.3553 0.4062 -0.0160 0.0909 -0.0084 92 MET A C 471 O O . MET A 65 ? 0.3943 0.4366 0.4697 -0.0245 0.1078 0.0039 92 MET A O 472 C CB . MET A 65 ? 0.3162 0.2972 0.3345 0.0069 0.0765 -0.0046 92 MET A CB 473 C CG . MET A 65 ? 0.3190 0.2721 0.3397 -0.0004 0.0712 0.0008 92 MET A CG 474 S SD . MET A 65 ? 0.3380 0.2592 0.3260 0.0072 0.0676 0.0115 92 MET A SD 475 C CE . MET A 65 ? 0.2420 0.1598 0.2168 0.0216 0.0539 -0.0016 92 MET A CE 476 N N . ALA A 66 ? 0.3160 0.3337 0.4170 -0.0239 0.0815 -0.0140 93 ALA A N 477 C CA . ALA A 66 ? 0.3501 0.3729 0.4790 -0.0450 0.0893 -0.0043 93 ALA A CA 478 C C . ALA A 66 ? 0.3617 0.3543 0.4676 -0.0541 0.0959 0.0177 93 ALA A C 479 O O . ALA A 66 ? 0.3432 0.3034 0.4221 -0.0443 0.0872 0.0200 93 ALA A O 480 C CB . ALA A 66 ? 0.2802 0.2920 0.4360 -0.0493 0.0725 -0.0166 93 ALA A CB 481 N N . PRO A 67 ? 0.3327 0.3535 0.4537 -0.0087 0.0814 0.0614 94 PRO A N 482 C CA . PRO A 67 ? 0.3255 0.3447 0.4542 -0.0117 0.0763 0.0779 94 PRO A CA 483 C C . PRO A 67 ? 0.3700 0.3672 0.5212 -0.0131 0.0617 0.0702 94 PRO A C 484 O O . PRO A 67 ? 0.3278 0.3176 0.4706 -0.0119 0.0562 0.0708 94 PRO A O 485 C CB . PRO A 67 ? 0.2929 0.3303 0.4466 -0.0177 0.0813 0.1047 94 PRO A CB 486 C CG . PRO A 67 ? 0.3195 0.3762 0.4584 -0.0148 0.0935 0.1015 94 PRO A CG 487 C CD . PRO A 67 ? 0.3378 0.3786 0.4671 -0.0108 0.0913 0.0738 94 PRO A CD 488 N N . ALA A 68 ? 0.3747 0.3644 0.5549 -0.0145 0.0549 0.0612 95 ALA A N 489 C CA . ALA A 68 ? 0.3389 0.3128 0.5439 -0.0135 0.0394 0.0495 95 ALA A CA 490 C C . ALA A 68 ? 0.3898 0.3577 0.5671 -0.0062 0.0359 0.0288 95 ALA A C 491 O O . ALA A 68 ? 0.3195 0.2782 0.5045 -0.0041 0.0250 0.0228 95 ALA A O 492 C CB . ALA A 68 ? 0.3366 0.3089 0.5771 -0.0141 0.0323 0.0392 95 ALA A CB 493 N N . CYS A 69 ? 0.3457 0.3202 0.4942 -0.0024 0.0446 0.0192 96 CYS A N 494 C CA . CYS A 69 ? 0.3338 0.3062 0.4588 0.0037 0.0422 0.0043 96 CYS A CA 495 C C . CYS A 69 ? 0.3381 0.3070 0.4397 0.0038 0.0441 0.0119 96 CYS A C 496 O O . CYS A 69 ? 0.2967 0.2595 0.3933 0.0068 0.0365 0.0056 96 CYS A O 497 C CB . CYS A 69 ? 0.3350 0.3159 0.4440 0.0070 0.0497 -0.0048 96 CYS A CB 498 S SG . CYS A 69 ? 0.2974 0.2804 0.3868 0.0138 0.0459 -0.0178 96 CYS A SG 499 N N . LYS A 70 ? 0.3000 0.2764 0.3874 0.0016 0.0538 0.0246 97 LYS A N 500 C CA . LYS A 70 ? 0.3352 0.3129 0.3992 0.0031 0.0556 0.0299 97 LYS A CA 501 C C . LYS A 70 ? 0.3496 0.3196 0.4251 0.0007 0.0473 0.0402 97 LYS A C 502 O O . LYS A 70 ? 0.3644 0.3303 0.4232 0.0032 0.0442 0.0379 97 LYS A O 503 C CB . LYS A 70 ? 0.3462 0.3411 0.3943 0.0034 0.0667 0.0398 97 LYS A CB 504 C CG . LYS A 70 ? 0.4869 0.4865 0.5086 0.0074 0.0675 0.0392 97 LYS A CG 505 C CD . LYS A 70 ? 0.5783 0.6030 0.5858 0.0098 0.0770 0.0489 97 LYS A CD 506 C CE . LYS A 70 ? 0.6084 0.6399 0.5935 0.0142 0.0753 0.0490 97 LYS A CE 507 N NZ . LYS A 70 ? 0.6228 0.6868 0.5914 0.0196 0.0837 0.0549 97 LYS A NZ 508 N N . ARG A 71 ? 0.3530 0.3210 0.4608 -0.0041 0.0427 0.0518 98 ARG A N 509 C CA . ARG A 71 ? 0.3383 0.2982 0.4666 -0.0068 0.0329 0.0630 98 ARG A CA 510 C C . ARG A 71 ? 0.3346 0.2810 0.4603 -0.0019 0.0217 0.0449 98 ARG A C 511 O O . ARG A 71 ? 0.3192 0.2609 0.4402 -0.0015 0.0169 0.0505 98 ARG A O 512 C CB . ARG A 71 ? 0.3114 0.2688 0.4861 -0.0125 0.0263 0.0747 98 ARG A CB 513 C CG . ARG A 71 ? 0.4727 0.4460 0.6592 -0.0188 0.0337 0.1059 98 ARG A CG 514 C CD . ARG A 71 ? 0.5380 0.5089 0.7772 -0.0252 0.0265 0.1186 98 ARG A CD 515 N NE . ARG A 71 ? 0.6256 0.6140 0.8659 -0.0281 0.0382 0.1290 98 ARG A NE 516 C CZ . ARG A 71 ? 0.6133 0.5982 0.8829 -0.0304 0.0351 0.1224 98 ARG A CZ 517 N NH1 . ARG A 71 ? 0.6756 0.6420 0.9766 -0.0292 0.0197 0.1036 98 ARG A NH1 518 N NH2 . ARG A 71 ? 0.5503 0.5529 0.8183 -0.0328 0.0466 0.1331 98 ARG A NH2 519 N N . HIS A 72 ? 0.3447 0.2891 0.4741 0.0024 0.0176 0.0240 99 HIS A N 520 C CA . HIS A 72 ? 0.3321 0.2721 0.4586 0.0087 0.0078 0.0062 99 HIS A CA 521 C C . HIS A 72 ? 0.3046 0.2462 0.3948 0.0115 0.0128 0.0048 99 HIS A C 522 O O . HIS A 72 ? 0.3328 0.2700 0.4186 0.0146 0.0056 0.0004 99 HIS A O 523 C CB . HIS A 72 ? 0.3476 0.2951 0.4837 0.0141 0.0039 -0.0138 99 HIS A CB 524 C CG . HIS A 72 ? 0.3629 0.3089 0.5394 0.0132 -0.0050 -0.0182 99 HIS A CG 525 N ND1 . HIS A 72 ? 0.3489 0.2905 0.5563 0.0171 -0.0211 -0.0297 99 HIS A ND1 526 C CD2 . HIS A 72 ? 0.3560 0.3048 0.5509 0.0092 -0.0014 -0.0140 99 HIS A CD2 527 C CE1 . HIS A 72 ? 0.3683 0.3092 0.6136 0.0156 -0.0280 -0.0333 99 HIS A CE1 528 N NE2 . HIS A 72 ? 0.3859 0.3311 0.6237 0.0103 -0.0157 -0.0227 99 HIS A NE2 529 N N . PHE A 73 ? 0.2984 0.2465 0.3659 0.0110 0.0240 0.0072 100 PHE A N 530 C CA . PHE A 73 ? 0.3400 0.2893 0.3790 0.0137 0.0272 0.0046 100 PHE A CA 531 C C . PHE A 73 ? 0.3613 0.3082 0.3890 0.0120 0.0273 0.0169 100 PHE A C 532 O O . PHE A 73 ? 0.3829 0.3273 0.3946 0.0147 0.0245 0.0131 100 PHE A O 533 C CB . PHE A 73 ? 0.2836 0.2405 0.3085 0.0147 0.0364 0.0008 100 PHE A CB 534 C CG . PHE A 73 ? 0.2993 0.2608 0.3296 0.0180 0.0348 -0.0110 100 PHE A CG 535 C CD1 . PHE A 73 ? 0.2933 0.2570 0.3174 0.0220 0.0297 -0.0176 100 PHE A CD1 536 C CD2 . PHE A 73 ? 0.2922 0.2595 0.3357 0.0173 0.0382 -0.0134 100 PHE A CD2 537 C CE1 . PHE A 73 ? 0.2805 0.2556 0.3114 0.0255 0.0284 -0.0242 100 PHE A CE1 538 C CE2 . PHE A 73 ? 0.2509 0.2273 0.2998 0.0210 0.0366 -0.0221 100 PHE A CE2 539 C CZ . PHE A 73 ? 0.2597 0.2418 0.3025 0.0253 0.0319 -0.0265 100 PHE A CZ 540 N N . ILE A 74 ? 0.3346 0.2852 0.3731 0.0077 0.0302 0.0333 101 ILE A N 541 C CA . ILE A 74 ? 0.3371 0.2901 0.3703 0.0062 0.0293 0.0489 101 ILE A CA 542 C C . ILE A 74 ? 0.3233 0.2630 0.3723 0.0064 0.0169 0.0479 101 ILE A C 543 O O . ILE A 74 ? 0.3094 0.2472 0.3437 0.0083 0.0140 0.0495 101 ILE A O 544 C CB . ILE A 74 ? 0.3483 0.3143 0.3956 0.0014 0.0350 0.0719 101 ILE A CB 545 C CG1 . ILE A 74 ? 0.3809 0.3650 0.4096 0.0031 0.0474 0.0715 101 ILE A CG1 546 C CG2 . ILE A 74 ? 0.3473 0.3201 0.3929 0.0002 0.0331 0.0917 101 ILE A CG2 547 C CD1 . ILE A 74 ? 0.3578 0.3514 0.3525 0.0091 0.0515 0.0624 101 ILE A CD1 548 N N . GLN A 75 ? 0.2685 0.2003 0.3496 0.0053 0.0085 0.0437 102 GLN A N 549 C CA . GLN A 75 ? 0.3097 0.2305 0.4111 0.0074 -0.0054 0.0375 102 GLN A CA 550 C C . GLN A 75 ? 0.3292 0.2491 0.4072 0.0139 -0.0083 0.0197 102 GLN A C 551 O O . GLN A 75 ? 0.3370 0.2518 0.4122 0.0158 -0.0150 0.0201 102 GLN A O 552 C CB . GLN A 75 ? 0.2917 0.2078 0.4324 0.0078 -0.0152 0.0277 102 GLN A CB 553 C CG . GLN A 75 ? 0.3288 0.2452 0.5023 0.0005 -0.0146 0.0472 102 GLN A CG 554 C CD . GLN A 75 ? 0.4015 0.3132 0.6171 0.0016 -0.0259 0.0338 102 GLN A CD 555 O OE1 . GLN A 75 ? 0.3910 0.3013 0.6126 0.0091 -0.0358 0.0090 102 GLN A OE1 556 N NE2 . GLN A 75 ? 0.4807 0.3936 0.7271 -0.0050 -0.0249 0.0498 102 GLN A NE2 557 N N . ASP A 76 ? 0.2726 0.1995 0.3366 0.0171 -0.0033 0.0063 103 ASP A N 558 C CA . ASP A 76 ? 0.3079 0.2396 0.3533 0.0229 -0.0048 -0.0070 103 ASP A CA 559 C C . ASP A 76 ? 0.3351 0.2647 0.3540 0.0222 -0.0011 0.0000 103 ASP A C 560 O O . ASP A 76 ? 0.3120 0.2399 0.3251 0.0254 -0.0073 -0.0039 103 ASP A O 561 C CB . ASP A 76 ? 0.2973 0.2394 0.3375 0.0246 0.0016 -0.0152 103 ASP A CB 562 C CG . ASP A 76 ? 0.3366 0.2878 0.3608 0.0293 0.0017 -0.0225 103 ASP A CG 563 O OD1 . ASP A 76 ? 0.2872 0.2440 0.3143 0.0344 -0.0063 -0.0297 103 ASP A OD1 564 O OD2 . ASP A 76 ? 0.3074 0.2623 0.3197 0.0282 0.0091 -0.0206 103 ASP A OD2 565 N N . THR A 77 ? 0.3354 0.2678 0.3398 0.0191 0.0083 0.0088 104 THR A N 566 C CA . THR A 77 ? 0.3141 0.2482 0.2955 0.0198 0.0109 0.0131 104 THR A CA 567 C C . THR A 77 ? 0.3750 0.3043 0.3584 0.0189 0.0049 0.0233 104 THR A C 568 O O . THR A 77 ? 0.3914 0.3188 0.3613 0.0214 0.0011 0.0206 104 THR A O 569 C CB . THR A 77 ? 0.3004 0.2445 0.2695 0.0185 0.0210 0.0193 104 THR A CB 570 O OG1 . THR A 77 ? 0.2798 0.2272 0.2490 0.0196 0.0258 0.0093 104 THR A OG1 571 C CG2 . THR A 77 ? 0.2596 0.2098 0.2061 0.0214 0.0219 0.0197 104 THR A CG2 572 N N . CYS A 78 ? 0.3680 0.2959 0.3721 0.0152 0.0033 0.0365 105 CYS A N 573 C CA . CYS A 78 ? 0.3700 0.2942 0.3832 0.0137 -0.0032 0.0502 105 CYS A CA 574 C C . CYS A 78 ? 0.3517 0.2649 0.3738 0.0173 -0.0151 0.0385 105 CYS A C 575 O O . CYS A 78 ? 0.3566 0.2681 0.3679 0.0187 -0.0187 0.0419 105 CYS A O 576 C CB . CYS A 78 ? 0.4083 0.3338 0.4524 0.0083 -0.0041 0.0691 105 CYS A CB 577 S SG . CYS A 78 ? 0.3540 0.3020 0.3863 0.0050 0.0101 0.0902 105 CYS A SG 578 N N . LEU A 79 ? 0.3508 0.2604 0.3922 0.0199 -0.0213 0.0237 106 LEU A N 579 C CA . LEU A 79 ? 0.3476 0.2540 0.3970 0.0257 -0.0326 0.0093 106 LEU A CA 580 C C . LEU A 79 ? 0.3014 0.2121 0.3205 0.0291 -0.0304 0.0035 106 LEU A C 581 O O . LEU A 79 ? 0.2834 0.1905 0.2987 0.0310 -0.0364 0.0049 106 LEU A O 582 C CB . LEU A 79 ? 0.2926 0.2042 0.3616 0.0305 -0.0381 -0.0092 106 LEU A CB 583 C CG . LEU A 79 ? 0.2975 0.2140 0.3786 0.0392 -0.0510 -0.0274 106 LEU A CG 584 C CD1 . LEU A 79 ? 0.2502 0.1549 0.3631 0.0394 -0.0643 -0.0252 106 LEU A CD1 585 C CD2 . LEU A 79 ? 0.2837 0.2161 0.3762 0.0461 -0.0540 -0.0469 106 LEU A CD2 586 N N . TYR A 80 ? 0.2994 0.2179 0.3010 0.0298 -0.0224 -0.0020 107 TYR A N 587 C CA . TYR A 80 ? 0.3283 0.2517 0.3091 0.0325 -0.0214 -0.0066 107 TYR A CA 588 C C . TYR A 80 ? 0.3789 0.2975 0.3422 0.0308 -0.0207 0.0023 107 TYR A C 589 O O . TYR A 80 ? 0.3400 0.2587 0.2957 0.0335 -0.0258 -0.0006 107 TYR A O 590 C CB . TYR A 80 ? 0.2559 0.1873 0.2285 0.0323 -0.0137 -0.0106 107 TYR A CB 591 C CG . TYR A 80 ? 0.3126 0.2479 0.2710 0.0339 -0.0137 -0.0124 107 TYR A CG 592 C CD1 . TYR A 80 ? 0.2929 0.2387 0.2554 0.0381 -0.0188 -0.0173 107 TYR A CD1 593 C CD2 . TYR A 80 ? 0.2880 0.2200 0.2319 0.0319 -0.0097 -0.0092 107 TYR A CD2 594 C CE1 . TYR A 80 ? 0.2741 0.2239 0.2300 0.0386 -0.0198 -0.0161 107 TYR A CE1 595 C CE2 . TYR A 80 ? 0.2891 0.2233 0.2268 0.0333 -0.0120 -0.0122 107 TYR A CE2 596 C CZ . TYR A 80 ? 0.3115 0.2531 0.2569 0.0358 -0.0171 -0.0141 107 TYR A CZ 597 O OH . TYR A 80 ? 0.3287 0.2729 0.2738 0.0364 -0.0202 -0.0143 107 TYR A OH 598 N N . GLU A 81 ? 0.3252 0.2438 0.2824 0.0272 -0.0145 0.0134 108 GLU A N 599 C CA . GLU A 81 ? 0.3312 0.2527 0.2692 0.0272 -0.0129 0.0204 108 GLU A CA 600 C C . GLU A 81 ? 0.3893 0.3074 0.3334 0.0263 -0.0188 0.0332 108 GLU A C 601 O O . GLU A 81 ? 0.3187 0.2401 0.2474 0.0278 -0.0202 0.0368 108 GLU A O 602 C CB . GLU A 81 ? 0.3323 0.2648 0.2585 0.0262 -0.0033 0.0250 108 GLU A CB 603 C CG . GLU A 81 ? 0.3139 0.2488 0.2367 0.0275 0.0012 0.0121 108 GLU A CG 604 C CD . GLU A 81 ? 0.2946 0.2423 0.2069 0.0283 0.0094 0.0124 108 GLU A CD 605 O OE1 . GLU A 81 ? 0.3410 0.3007 0.2461 0.0285 0.0130 0.0239 108 GLU A OE1 606 O OE2 . GLU A 81 ? 0.3802 0.3292 0.2932 0.0296 0.0120 0.0015 108 GLU A OE2 607 N N . CYS A 82 ? 0.3785 0.2905 0.3487 0.0242 -0.0235 0.0396 109 CYS A N 608 C CA . CYS A 82 ? 0.3905 0.2998 0.3748 0.0222 -0.0293 0.0563 109 CYS A CA 609 C C . CYS A 82 ? 0.3464 0.2437 0.3558 0.0244 -0.0425 0.0496 109 CYS A C 610 O O . CYS A 82 ? 0.3736 0.2674 0.3909 0.0243 -0.0492 0.0599 109 CYS A O 611 C CB . CYS A 82 ? 0.3807 0.2962 0.3834 0.0170 -0.0249 0.0762 109 CYS A CB 612 S SG . CYS A 82 ? 0.3929 0.3306 0.3671 0.0166 -0.0101 0.0851 109 CYS A SG 613 N N . SER A 83 ? 0.3052 0.2745 0.3015 0.0313 -0.0037 -0.0386 110 SER A N 614 C CA . SER A 83 ? 0.3105 0.2898 0.3252 0.0327 -0.0017 -0.0395 110 SER A CA 615 C C . SER A 83 ? 0.3088 0.2931 0.3364 0.0328 -0.0089 -0.0360 110 SER A C 616 O O . SER A 83 ? 0.3102 0.2992 0.3408 0.0308 -0.0124 -0.0354 110 SER A O 617 C CB . SER A 83 ? 0.3294 0.3200 0.3517 0.0328 0.0049 -0.0447 110 SER A CB 618 O OG . SER A 83 ? 0.3198 0.3179 0.3574 0.0341 0.0071 -0.0455 110 SER A OG 619 N N . PRO A 84 ? 0.3001 0.2832 0.3371 0.0352 -0.0109 -0.0336 111 PRO A N 620 C CA . PRO A 84 ? 0.2638 0.2547 0.3200 0.0365 -0.0171 -0.0306 111 PRO A CA 621 C C . PRO A 84 ? 0.2977 0.3015 0.3735 0.0383 -0.0083 -0.0336 111 PRO A C 622 O O . PRO A 84 ? 0.2758 0.2870 0.3716 0.0405 -0.0101 -0.0315 111 PRO A O 623 C CB . PRO A 84 ? 0.2727 0.2523 0.3253 0.0396 -0.0235 -0.0265 111 PRO A CB 624 C CG . PRO A 84 ? 0.2688 0.2403 0.3099 0.0405 -0.0140 -0.0291 111 PRO A CG 625 C CD . PRO A 84 ? 0.3106 0.2831 0.3399 0.0371 -0.0078 -0.0332 111 PRO A CD 626 N N . ASN A 85 ? 0.2925 0.2981 0.3624 0.0377 0.0010 -0.0386 112 ASN A N 627 C CA . ASN A 85 ? 0.2907 0.3035 0.3724 0.0395 0.0099 -0.0421 112 ASN A CA 628 C C . ASN A 85 ? 0.3296 0.3474 0.4082 0.0376 0.0152 -0.0456 112 ASN A C 629 O O . ASN A 85 ? 0.2981 0.3159 0.3742 0.0387 0.0226 -0.0502 112 ASN A O 630 C CB . ASN A 85 ? 0.3202 0.3273 0.3970 0.0411 0.0156 -0.0456 112 ASN A CB 631 C CG . ASN A 85 ? 0.3657 0.3641 0.4421 0.0431 0.0118 -0.0419 112 ASN A CG 632 O OD1 . ASN A 85 ? 0.3858 0.3749 0.4492 0.0419 0.0123 -0.0423 112 ASN A OD1 633 N ND2 . ASN A 85 ? 0.3230 0.3236 0.4140 0.0466 0.0085 -0.0382 112 ASN A ND2 634 N N . LEU A 86 ? 0.2703 0.2899 0.3467 0.0348 0.0110 -0.0435 113 LEU A N 635 C CA . LEU A 86 ? 0.2856 0.3071 0.3571 0.0331 0.0160 -0.0459 113 LEU A CA 636 C C . LEU A 86 ? 0.2673 0.2960 0.3561 0.0318 0.0184 -0.0434 113 LEU A C 637 O O . LEU A 86 ? 0.2884 0.3167 0.3730 0.0299 0.0237 -0.0445 113 LEU A O 638 C CB . LEU A 86 ? 0.2863 0.3023 0.3399 0.0308 0.0115 -0.0460 113 LEU A CB 639 C CG . LEU A 86 ? 0.2770 0.2874 0.3165 0.0319 0.0106 -0.0485 113 LEU A CG 640 C CD1 . LEU A 86 ? 0.2449 0.2497 0.2687 0.0306 0.0071 -0.0483 113 LEU A CD1 641 C CD2 . LEU A 86 ? 0.2303 0.2419 0.2681 0.0340 0.0168 -0.0539 113 LEU A CD2 642 N N . GLY A 87 ? 0.2082 0.2427 0.3171 0.0328 0.0148 -0.0399 114 GLY A N 643 C CA . GLY A 87 ? 0.2079 0.2519 0.3402 0.0314 0.0169 -0.0375 114 GLY A CA 644 C C . GLY A 87 ? 0.2509 0.2967 0.3862 0.0310 0.0309 -0.0400 114 GLY A C 645 O O . GLY A 87 ? 0.2967 0.3451 0.4377 0.0269 0.0332 -0.0387 114 GLY A O 646 N N . PRO A 88 ? 0.2523 0.2942 0.3816 0.0349 0.0407 -0.0437 115 PRO A N 647 C CA . PRO A 88 ? 0.2490 0.2883 0.3766 0.0352 0.0550 -0.0462 115 PRO A CA 648 C C . PRO A 88 ? 0.2858 0.3168 0.3910 0.0317 0.0570 -0.0475 115 PRO A C 649 O O . PRO A 88 ? 0.2585 0.2854 0.3614 0.0310 0.0688 -0.0483 115 PRO A O 650 C CB . PRO A 88 ? 0.2426 0.2745 0.3597 0.0400 0.0614 -0.0507 115 PRO A CB 651 C CG . PRO A 88 ? 0.2487 0.2848 0.3777 0.0426 0.0535 -0.0489 115 PRO A CG 652 C CD . PRO A 88 ? 0.2625 0.3007 0.3876 0.0392 0.0397 -0.0456 115 PRO A CD 653 N N . TRP A 89 ? 0.2424 0.2696 0.3308 0.0300 0.0467 -0.0476 116 TRP A N 654 C CA . TRP A 89 ? 0.2672 0.2851 0.3330 0.0279 0.0476 -0.0489 116 TRP A CA 655 C C . TRP A 89 ? 0.3009 0.3199 0.3681 0.0230 0.0402 -0.0453 116 TRP A C 656 O O . TRP A 89 ? 0.2811 0.2916 0.3304 0.0213 0.0409 -0.0457 116 TRP A O 657 C CB . TRP A 89 ? 0.2462 0.2565 0.2889 0.0310 0.0438 -0.0531 116 TRP A CB 658 C CG . TRP A 89 ? 0.2651 0.2727 0.3061 0.0348 0.0499 -0.0572 116 TRP A CG 659 C CD1 . TRP A 89 ? 0.2434 0.2417 0.2718 0.0366 0.0593 -0.0605 116 TRP A CD1 660 C CD2 . TRP A 89 ? 0.2543 0.2658 0.3044 0.0370 0.0474 -0.0585 116 TRP A CD2 661 N NE1 . TRP A 89 ? 0.2905 0.2868 0.3196 0.0397 0.0622 -0.0642 116 TRP A NE1 662 C CE2 . TRP A 89 ? 0.2970 0.3019 0.3405 0.0398 0.0552 -0.0630 116 TRP A CE2 663 C CE3 . TRP A 89 ? 0.2377 0.2549 0.2981 0.0368 0.0397 -0.0563 116 TRP A CE3 664 C CZ2 . TRP A 89 ? 0.2796 0.2844 0.3284 0.0420 0.0555 -0.0654 116 TRP A CZ2 665 C CZ3 . TRP A 89 ? 0.2589 0.2755 0.3241 0.0392 0.0406 -0.0582 116 TRP A CZ3 666 C CH2 . TRP A 89 ? 0.2727 0.2838 0.3332 0.0416 0.0484 -0.0629 116 TRP A CH2 667 N N . ILE A 90 ? 0.2772 0.3049 0.3642 0.0210 0.0325 -0.0418 117 ILE A N 668 C CA . ILE A 90 ? 0.2625 0.2897 0.3509 0.0157 0.0239 -0.0387 117 ILE A CA 669 C C . ILE A 90 ? 0.3013 0.3296 0.3996 0.0107 0.0316 -0.0373 117 ILE A C 670 O O . ILE A 90 ? 0.2610 0.2974 0.3817 0.0105 0.0405 -0.0366 117 ILE A O 671 C CB . ILE A 90 ? 0.2958 0.3302 0.4020 0.0150 0.0119 -0.0355 117 ILE A CB 672 C CG1 . ILE A 90 ? 0.2521 0.2809 0.3432 0.0189 0.0050 -0.0363 117 ILE A CG1 673 C CG2 . ILE A 90 ? 0.3009 0.3339 0.4103 0.0086 0.0026 -0.0327 117 ILE A CG2 674 C CD1 . ILE A 90 ? 0.2511 0.2822 0.3536 0.0194 -0.0067 -0.0330 117 ILE A CD1 675 N N . GLN A 91 ? 0.3038 0.3227 0.3853 0.0067 0.0295 -0.0368 118 GLN A N 676 C CA . GLN A 91 ? 0.3246 0.3413 0.4123 0.0008 0.0376 -0.0354 118 GLN A CA 677 C C . GLN A 91 ? 0.3177 0.3397 0.4237 -0.0065 0.0276 -0.0323 118 GLN A C 678 O O . GLN A 91 ? 0.3610 0.3826 0.4637 -0.0068 0.0133 -0.0315 118 GLN A O 679 C CB . GLN A 91 ? 0.2897 0.2895 0.3452 0.0012 0.0428 -0.0369 118 GLN A CB 680 C CG . GLN A 91 ? 0.3060 0.2992 0.3423 0.0082 0.0502 -0.0404 118 GLN A CG 681 C CD . GLN A 91 ? 0.3110 0.3071 0.3600 0.0093 0.0647 -0.0410 118 GLN A CD 682 O OE1 . GLN A 91 ? 0.3817 0.3743 0.4362 0.0052 0.0757 -0.0394 118 GLN A OE1 683 N NE2 . GLN A 91 ? 0.2874 0.2888 0.3412 0.0147 0.0659 -0.0433 118 GLN A NE2 684 N N . GLN A 92 ? 0.3269 0.3526 0.4516 -0.0128 0.0355 -0.0307 119 GLN A N 685 C CA . GLN A 92 ? 0.4058 0.4377 0.5523 -0.0210 0.0257 -0.0283 119 GLN A CA 686 C C . GLN A 92 ? 0.4096 0.4256 0.5296 -0.0256 0.0164 -0.0282 119 GLN A C 687 O O . GLN A 92 ? 0.3936 0.4100 0.5179 -0.0293 0.0008 -0.0271 119 GLN A O 688 C CB . GLN A 92 ? 0.5135 0.5541 0.6904 -0.0272 0.0388 -0.0270 119 GLN A CB 689 C CG . GLN A 92 ? 0.6877 0.7363 0.8920 -0.0370 0.0280 -0.0249 119 GLN A CG 690 C CD . GLN A 92 ? 0.8052 0.8687 1.0348 -0.0354 0.0098 -0.0238 119 GLN A CD 691 O OE1 . GLN A 92 ? 0.8277 0.9019 1.0711 -0.0280 0.0111 -0.0238 119 GLN A OE1 692 N NE2 . GLN A 92 ? 0.8335 0.8951 1.0667 -0.0422 -0.0079 -0.0229 119 GLN A NE2 693 N N . VAL A 93 ? 0.3990 0.3991 0.4899 -0.0249 0.0255 -0.0293 120 VAL A N 694 C CA . VAL A 93 ? 0.4109 0.3937 0.4748 -0.0283 0.0187 -0.0293 120 VAL A CA 695 C C . VAL A 93 ? 0.3418 0.3146 0.3742 -0.0202 0.0129 -0.0311 120 VAL A C 696 O O . VAL A 93 ? 0.3321 0.3037 0.3522 -0.0129 0.0201 -0.0330 120 VAL A O 697 C CB . VAL A 93 ? 0.3939 0.3628 0.4448 -0.0327 0.0319 -0.0288 120 VAL A CB 698 C CG1 . VAL A 93 ? 0.3581 0.3067 0.3777 -0.0345 0.0252 -0.0289 120 VAL A CG1 699 C CG2 . VAL A 93 ? 0.3441 0.3227 0.4289 -0.0424 0.0387 -0.0269 120 VAL A CG2 700 N N . ASP A 94 ? 0.3813 0.3463 0.4013 -0.0215 -0.0001 -0.0309 121 ASP A N 701 C CA . ASP A 94 ? 0.3752 0.3318 0.3695 -0.0141 -0.0047 -0.0326 121 ASP A CA 702 C C . ASP A 94 ? 0.3685 0.3071 0.3392 -0.0166 -0.0125 -0.0324 121 ASP A C 703 O O . ASP A 94 ? 0.3835 0.3154 0.3380 -0.0123 -0.0189 -0.0332 121 ASP A O 704 C CB . ASP A 94 ? 0.3230 0.2906 0.3289 -0.0101 -0.0118 -0.0326 121 ASP A CB 705 C CG . ASP A 94 ? 0.3791 0.3514 0.4033 -0.0159 -0.0242 -0.0304 121 ASP A CG 706 O OD1 . ASP A 94 ? 0.4202 0.3817 0.4362 -0.0221 -0.0318 -0.0297 121 ASP A OD1 707 O OD2 . ASP A 94 ? 0.2888 0.2746 0.3349 -0.0143 -0.0271 -0.0296 121 ASP A OD2 708 N N . GLN A 95 ? 0.3705 0.2999 0.3387 -0.0239 -0.0108 -0.0314 122 GLN A N 709 C CA . GLN A 95 ? 0.3297 0.2401 0.2765 -0.0277 -0.0185 -0.0314 122 GLN A CA 710 C C . GLN A 95 ? 0.3607 0.2556 0.2748 -0.0194 -0.0167 -0.0329 122 GLN A C 711 O O . GLN A 95 ? 0.3826 0.2621 0.2772 -0.0197 -0.0238 -0.0333 122 GLN A O 712 C CB . GLN A 95 ? 0.4174 0.3197 0.3681 -0.0376 -0.0152 -0.0302 122 GLN A CB 713 C CG . GLN A 95 ? 0.4398 0.3365 0.3821 -0.0359 0.0001 -0.0300 122 GLN A CG 714 C CD . GLN A 95 ? 0.5607 0.4484 0.5083 -0.0469 0.0049 -0.0285 122 GLN A CD 715 O OE1 . GLN A 95 ? 0.5828 0.4785 0.5553 -0.0566 -0.0012 -0.0277 122 GLN A OE1 716 N NE2 . GLN A 95 ? 0.5977 0.4676 0.5217 -0.0455 0.0153 -0.0281 122 GLN A NE2 717 N N . SER A 96 ? 0.3662 0.2641 0.2743 -0.0117 -0.0074 -0.0340 123 SER A N 718 C CA . SER A 96 ? 0.3838 0.2698 0.2659 -0.0030 -0.0062 -0.0357 123 SER A CA 719 C C . SER A 96 ? 0.3739 0.2686 0.2577 0.0042 -0.0093 -0.0373 123 SER A C 720 O O . SER A 96 ? 0.4412 0.3290 0.3088 0.0115 -0.0083 -0.0389 123 SER A O 721 C CB . SER A 96 ? 0.3687 0.2493 0.2394 0.0019 0.0030 -0.0362 123 SER A CB 722 O OG . SER A 96 ? 0.4029 0.2985 0.2860 0.0065 0.0077 -0.0375 123 SER A OG 723 N N . TRP A 97 ? 0.4050 0.3147 0.3096 0.0022 -0.0125 -0.0368 124 TRP A N 724 C CA . TRP A 97 ? 0.3397 0.2571 0.2472 0.0081 -0.0140 -0.0381 124 TRP A CA 725 C C . TRP A 97 ? 0.3591 0.2699 0.2623 0.0055 -0.0228 -0.0369 124 TRP A C 726 O O . TRP A 97 ? 0.3773 0.2847 0.2854 -0.0017 -0.0300 -0.0351 124 TRP A O 727 C CB . TRP A 97 ? 0.3068 0.2428 0.2368 0.0094 -0.0101 -0.0386 124 TRP A CB 728 C CG . TRP A 97 ? 0.3110 0.2495 0.2389 0.0131 -0.0017 -0.0403 124 TRP A CG 729 C CD1 . TRP A 97 ? 0.3313 0.2673 0.2606 0.0098 0.0040 -0.0395 124 TRP A CD1 730 C CD2 . TRP A 97 ? 0.3211 0.2623 0.2429 0.0209 0.0015 -0.0433 124 TRP A CD2 731 N NE1 . TRP A 97 ? 0.3130 0.2477 0.2334 0.0156 0.0102 -0.0416 124 TRP A NE1 732 C CE2 . TRP A 97 ? 0.3216 0.2605 0.2385 0.0224 0.0075 -0.0442 124 TRP A CE2 733 C CE3 . TRP A 97 ? 0.3198 0.2646 0.2403 0.0264 0.0000 -0.0455 124 TRP A CE3 734 C CZ2 . TRP A 97 ? 0.3545 0.2942 0.2643 0.0294 0.0095 -0.0473 124 TRP A CZ2 735 C CZ3 . TRP A 97 ? 0.2889 0.2375 0.2073 0.0327 0.0027 -0.0487 124 TRP A CZ3 736 C CH2 . TRP A 97 ? 0.3680 0.3140 0.2805 0.0343 0.0061 -0.0498 124 TRP A CH2 737 N N . ARG A 98 ? 0.3920 0.2996 0.2856 0.0111 -0.0224 -0.0380 125 ARG A N 738 C CA . ARG A 98 ? 0.3650 0.2613 0.2479 0.0096 -0.0296 -0.0368 125 ARG A CA 739 C C . ARG A 98 ? 0.3397 0.2463 0.2414 0.0061 -0.0365 -0.0348 125 ARG A C 740 O O . ARG A 98 ? 0.3461 0.2430 0.2424 0.0018 -0.0466 -0.0330 125 ARG A O 741 C CB . ARG A 98 ? 0.3955 0.2846 0.2634 0.0166 -0.0244 -0.0383 125 ARG A CB 742 C CG . ARG A 98 ? 0.3157 0.2209 0.1992 0.0215 -0.0185 -0.0396 125 ARG A CG 743 C CD . ARG A 98 ? 0.3493 0.2486 0.2213 0.0281 -0.0110 -0.0418 125 ARG A CD 744 N NE . ARG A 98 ? 0.3050 0.2183 0.1922 0.0317 -0.0055 -0.0435 125 ARG A NE 745 C CZ . ARG A 98 ? 0.3127 0.2411 0.2144 0.0348 -0.0016 -0.0461 125 ARG A CZ 746 N NH1 . ARG A 98 ? 0.2967 0.2269 0.1976 0.0354 -0.0021 -0.0469 125 ARG A NH1 747 N NH2 . ARG A 98 ? 0.3065 0.2459 0.2216 0.0371 0.0026 -0.0480 125 ARG A NH2 748 N N . LYS A 99 ? 0.2913 0.2161 0.2141 0.0085 -0.0317 -0.0352 126 LYS A N 749 C CA . LYS A 99 ? 0.3602 0.2961 0.3041 0.0061 -0.0373 -0.0333 126 LYS A CA 750 C C . LYS A 99 ? 0.3344 0.2873 0.3027 0.0045 -0.0318 -0.0335 126 LYS A C 751 O O . LYS A 99 ? 0.3239 0.2756 0.2940 0.0001 -0.0304 -0.0334 126 LYS A O 752 C CB . LYS A 99 ? 0.3241 0.2621 0.2684 0.0111 -0.0360 -0.0332 126 LYS A CB 753 C CG . LYS A 99 ? 0.3229 0.2413 0.2409 0.0129 -0.0387 -0.0328 126 LYS A CG 754 C CD . LYS A 99 ? 0.3825 0.3011 0.3010 0.0168 -0.0362 -0.0323 126 LYS A CD 755 C CE . LYS A 99 ? 0.4385 0.3591 0.3684 0.0150 -0.0463 -0.0291 126 LYS A CE 756 N NZ . LYS A 99 ? 0.4154 0.3331 0.3432 0.0190 -0.0434 -0.0282 126 LYS A NZ 757 N N . GLU A 100 ? 0.4203 0.2130 0.2279 0.0017 -0.0092 0.0187 127 GLU A N 758 C CA . GLU A 100 ? 0.3985 0.2394 0.2381 -0.0020 -0.0112 0.0018 127 GLU A CA 759 C C . GLU A 100 ? 0.4503 0.3101 0.2812 -0.0001 -0.0028 -0.0070 127 GLU A C 760 O O . GLU A 100 ? 0.4719 0.3130 0.2840 0.0077 0.0048 -0.0022 127 GLU A O 761 C CB . GLU A 100 ? 0.3512 0.2197 0.2500 0.0059 -0.0141 -0.0122 127 GLU A CB 762 C CG . GLU A 100 ? 0.3399 0.2210 0.2655 0.0173 -0.0061 -0.0234 127 GLU A CG 763 C CD . GLU A 100 ? 0.3581 0.2054 0.2797 0.0248 -0.0032 -0.0127 127 GLU A CD 764 O OE1 . GLU A 100 ? 0.3616 0.1720 0.2518 0.0219 -0.0054 0.0042 127 GLU A OE1 765 O OE2 . GLU A 100 ? 0.3453 0.2038 0.2943 0.0324 0.0011 -0.0212 127 GLU A OE2 766 N N . ARG A 101 ? 0.3397 0.2386 0.1842 -0.0073 -0.0044 -0.0194 128 ARG A N 767 C CA . ARG A 101 ? 0.3920 0.3173 0.2392 -0.0058 0.0024 -0.0310 128 ARG A CA 768 C C . ARG A 101 ? 0.3704 0.3407 0.2746 -0.0002 0.0033 -0.0521 128 ARG A C 769 O O . ARG A 101 ? 0.3529 0.3508 0.2834 -0.0043 -0.0022 -0.0608 128 ARG A O 770 C CB . ARG A 101 ? 0.4244 0.3579 0.2358 -0.0206 0.0002 -0.0288 128 ARG A CB 771 C CG . ARG A 101 ? 0.4618 0.4363 0.2860 -0.0229 0.0047 -0.0445 128 ARG A CG 772 C CD . ARG A 101 ? 0.5778 0.5466 0.4006 -0.0112 0.0130 -0.0469 128 ARG A CD 773 N NE . ARG A 101 ? 0.6211 0.6127 0.4298 -0.0174 0.0158 -0.0540 128 ARG A NE 774 C CZ . ARG A 101 ? 0.5821 0.5831 0.3964 -0.0094 0.0221 -0.0598 128 ARG A CZ 775 N NH1 . ARG A 101 ? 0.4271 0.4194 0.2621 0.0047 0.0268 -0.0597 128 ARG A NH1 776 N NH2 . ARG A 101 ? 0.5396 0.5599 0.3391 -0.0166 0.0231 -0.0648 128 ARG A NH2 777 N N . VAL A 102 ? 0.2886 0.2658 0.2115 0.0098 0.0099 -0.0600 129 VAL A N 778 C CA . VAL A 102 ? 0.2898 0.3058 0.2611 0.0147 0.0110 -0.0808 129 VAL A CA 779 C C . VAL A 102 ? 0.2932 0.3363 0.2593 0.0122 0.0173 -0.0913 129 VAL A C 780 O O . VAL A 102 ? 0.3139 0.3404 0.2460 0.0118 0.0216 -0.0816 129 VAL A O 781 C CB . VAL A 102 ? 0.3660 0.3701 0.3682 0.0262 0.0118 -0.0832 129 VAL A CB 782 C CG1 . VAL A 102 ? 0.2664 0.2503 0.2818 0.0281 0.0037 -0.0764 129 VAL A CG1 783 C CG2 . VAL A 102 ? 0.2785 0.2572 0.2575 0.0313 0.0186 -0.0714 129 VAL A CG2 784 N N . LEU A 103 ? 0.2988 0.3835 0.2980 0.0111 0.0175 -0.1112 130 LEU A N 785 C CA . LEU A 103 ? 0.2803 0.3938 0.2749 0.0067 0.0227 -0.1221 130 LEU A CA 786 C C . LEU A 103 ? 0.2681 0.4108 0.3066 0.0136 0.0253 -0.1431 130 LEU A C 787 O O . LEU A 103 ? 0.2632 0.4262 0.3360 0.0166 0.0223 -0.1571 130 LEU A O 788 C CB . LEU A 103 ? 0.3146 0.4540 0.2941 -0.0069 0.0205 -0.1255 130 LEU A CB 789 C CG . LEU A 103 ? 0.3290 0.5012 0.3003 -0.0151 0.0247 -0.1366 130 LEU A CG 790 C CD1 . LEU A 103 ? 0.3468 0.4940 0.2791 -0.0154 0.0280 -0.1240 130 LEU A CD1 791 C CD2 . LEU A 103 ? 0.3169 0.5155 0.2753 -0.0304 0.0215 -0.1387 130 LEU A CD2 792 N N . ASN A 104 ? 0.2499 0.3932 0.2858 0.0166 0.0305 -0.1448 131 ASN A N 793 C CA . ASN A 104 ? 0.2495 0.4197 0.3203 0.0204 0.0329 -0.1645 131 ASN A CA 794 C C . ASN A 104 ? 0.2279 0.3876 0.3348 0.0298 0.0298 -0.1707 131 ASN A C 795 O O . ASN A 104 ? 0.2508 0.4291 0.3874 0.0304 0.0269 -0.1852 131 ASN A O 796 C CB . ASN A 104 ? 0.2461 0.4550 0.3282 0.0121 0.0315 -0.1785 131 ASN A CB 797 C CG . ASN A 104 ? 0.3138 0.5314 0.3634 0.0009 0.0329 -0.1697 131 ASN A CG 798 O OD1 . ASN A 104 ? 0.3549 0.5555 0.3819 0.0014 0.0351 -0.1578 131 ASN A OD1 799 N ND2 . ASN A 104 ? 0.3286 0.5723 0.3766 -0.0089 0.0311 -0.1743 131 ASN A ND2 800 N N . VAL A 105 ? 0.2554 0.3791 0.3545 0.0344 0.0278 -0.1539 132 VAL A N 801 C CA . VAL A 105 ? 0.2761 0.3842 0.4042 0.0416 0.0242 -0.1566 132 VAL A CA 802 C C . VAL A 105 ? 0.2829 0.4044 0.4295 0.0429 0.0274 -0.1681 132 VAL A C 803 O O . VAL A 105 ? 0.3087 0.4298 0.4381 0.0411 0.0326 -0.1601 132 VAL A O 804 C CB . VAL A 105 ? 0.2740 0.3419 0.3842 0.0442 0.0229 -0.1344 132 VAL A CB 805 C CG1 . VAL A 105 ? 0.2519 0.3038 0.3897 0.0493 0.0192 -0.1363 132 VAL A CG1 806 C CG2 . VAL A 105 ? 0.2351 0.2869 0.3280 0.0420 0.0182 -0.1233 132 VAL A CG2 807 N N . PRO A 106 ? 0.2811 0.4113 0.4576 0.0435 0.0219 -0.1816 133 PRO A N 808 C CA . PRO A 106 ? 0.2469 0.3875 0.4361 0.0402 0.0219 -0.1895 133 PRO A CA 809 C C . PRO A 106 ? 0.2749 0.3937 0.4702 0.0432 0.0229 -0.1826 133 PRO A C 810 O O . PRO A 106 ? 0.3293 0.4355 0.5466 0.0451 0.0174 -0.1883 133 PRO A O 811 C CB . PRO A 106 ? 0.2770 0.4279 0.4919 0.0408 0.0148 -0.2055 133 PRO A CB 812 C CG . PRO A 106 ? 0.2632 0.3980 0.4855 0.0475 0.0098 -0.2020 133 PRO A CG 813 C CD . PRO A 106 ? 0.2861 0.4174 0.4836 0.0472 0.0147 -0.1899 133 PRO A CD 814 N N . LEU A 107 ? 0.2802 0.3952 0.4551 0.0438 0.0301 -0.1702 134 LEU A N 815 C CA . LEU A 107 ? 0.2912 0.3894 0.4666 0.0439 0.0309 -0.1575 134 LEU A CA 816 C C . LEU A 107 ? 0.3112 0.4247 0.5103 0.0398 0.0296 -0.1717 134 LEU A C 817 O O . LEU A 107 ? 0.2703 0.4115 0.4722 0.0363 0.0320 -0.1851 134 LEU A O 818 C CB . LEU A 107 ? 0.2307 0.3280 0.3749 0.0444 0.0381 -0.1391 134 LEU A CB 819 C CG . LEU A 107 ? 0.2995 0.3809 0.4391 0.0458 0.0406 -0.1218 134 LEU A CG 820 C CD1 . LEU A 107 ? 0.3338 0.3825 0.4772 0.0475 0.0357 -0.1125 134 LEU A CD1 821 C CD2 . LEU A 107 ? 0.3102 0.3921 0.4170 0.0497 0.0481 -0.1053 134 LEU A CD2 822 N N . CYS A 108 ? 0.2552 0.3494 0.4690 0.0386 0.0251 -0.1681 135 CYS A N 823 C CA . CYS A 108 ? 0.3000 0.4042 0.5340 0.0327 0.0224 -0.1806 135 CYS A CA 824 C C . CYS A 108 ? 0.2816 0.4106 0.5058 0.0274 0.0290 -0.1750 135 CYS A C 825 O O . CYS A 108 ? 0.2641 0.3930 0.4684 0.0295 0.0347 -0.1564 135 CYS A O 826 C CB . CYS A 108 ? 0.3000 0.3753 0.5474 0.0302 0.0153 -0.1748 135 CYS A CB 827 S SG . CYS A 108 ? 0.3093 0.3559 0.5748 0.0366 0.0044 -0.1861 135 CYS A SG 828 N N . LYS A 109 ? 0.4293 0.3428 0.5685 0.0213 -0.0780 -0.1960 136 LYS A N 829 C CA . LYS A 109 ? 0.4647 0.3866 0.6034 0.0189 -0.0847 -0.2018 136 LYS A CA 830 C C . LYS A 109 ? 0.4690 0.3870 0.6366 0.0101 -0.0887 -0.1923 136 LYS A C 831 O O . LYS A 109 ? 0.4788 0.4062 0.6344 0.0081 -0.0851 -0.1892 136 LYS A O 832 C CB . LYS A 109 ? 0.5171 0.4378 0.6678 0.0214 -0.0995 -0.2178 136 LYS A CB 833 C CG . LYS A 109 ? 0.6114 0.5416 0.7529 0.0221 -0.1065 -0.2262 136 LYS A CG 834 C CD . LYS A 109 ? 0.7455 0.6706 0.9045 0.0245 -0.1229 -0.2414 136 LYS A CD 835 C CE . LYS A 109 ? 0.8617 0.7952 1.0059 0.0275 -0.1299 -0.2509 136 LYS A CE 836 N NZ . LYS A 109 ? 0.9557 0.8946 1.0546 0.0345 -0.1181 -0.2523 136 LYS A NZ 837 N N . GLU A 110 ? 0.4271 0.3308 0.6324 0.0043 -0.0949 -0.1856 137 GLU A N 838 C CA . GLU A 110 ? 0.4210 0.3195 0.6605 -0.0062 -0.0975 -0.1721 137 GLU A CA 839 C C . GLU A 110 ? 0.4001 0.2971 0.6299 -0.0093 -0.0824 -0.1534 137 GLU A C 840 O O . GLU A 110 ? 0.3892 0.2920 0.6302 -0.0162 -0.0814 -0.1452 137 GLU A O 841 C CB . GLU A 110 ? 0.4712 0.3530 0.7486 -0.0117 -0.1038 -0.1645 137 GLU A CB 842 C CG . GLU A 110 ? 0.6187 0.4986 0.9092 -0.0092 -0.1191 -0.1820 137 GLU A CG 843 C CD . GLU A 110 ? 0.7196 0.5983 0.9836 0.0013 -0.1180 -0.1943 137 GLU A CD 844 O OE1 . GLU A 110 ? 0.8151 0.6988 1.0726 0.0063 -0.1274 -0.2114 137 GLU A OE1 845 O OE2 . GLU A 110 ? 0.6265 0.4996 0.8765 0.0046 -0.1074 -0.1860 137 GLU A OE2 846 N N . ASP A 111 ? 0.3576 0.2466 0.5684 -0.0041 -0.0708 -0.1456 138 ASP A N 847 C CA . ASP A 111 ? 0.4121 0.2965 0.6102 -0.0049 -0.0552 -0.1264 138 ASP A CA 848 C C . ASP A 111 ? 0.3945 0.2943 0.5667 -0.0040 -0.0502 -0.1321 138 ASP A C 849 O O . ASP A 111 ? 0.4342 0.3415 0.6067 -0.0089 -0.0413 -0.1096 138 ASP A O 850 C CB . ASP A 111 ? 0.3745 0.2527 0.5468 0.0035 -0.0449 -0.1225 138 ASP A CB 851 C CG . ASP A 111 ? 0.3879 0.2494 0.5817 0.0030 -0.0486 -0.1143 138 ASP A CG 852 O OD1 . ASP A 111 ? 0.3748 0.2239 0.5666 0.0031 -0.0389 -0.0932 138 ASP A OD1 853 O OD2 . ASP A 111 ? 0.3383 0.1988 0.5471 0.0034 -0.0609 -0.1281 138 ASP A OD2 854 N N . CYS A 112 ? 0.3855 0.3008 0.5236 0.0037 -0.0516 -0.1503 139 CYS A N 855 C CA . CYS A 112 ? 0.3728 0.3053 0.4749 0.0068 -0.0457 -0.1548 139 CYS A CA 856 C C . CYS A 112 ? 0.4179 0.3586 0.5396 0.0007 -0.0580 -0.1604 139 CYS A C 857 O O . CYS A 112 ? 0.4164 0.3710 0.5222 -0.0007 -0.0488 -0.1428 139 CYS A O 858 C CB . CYS A 112 ? 0.3650 0.3089 0.4274 0.0149 -0.0420 -0.1634 139 CYS A CB 859 S SG . CYS A 112 ? 0.4803 0.4409 0.4928 0.0181 -0.0320 -0.1590 139 CYS A SG 860 N N . GLU A 113 ? 0.3786 0.3193 0.5274 -0.0015 -0.0744 -0.1709 140 GLU A N 861 C CA . GLU A 113 ? 0.4154 0.3663 0.5849 -0.0068 -0.0878 -0.1761 140 GLU A CA 862 C C . GLU A 113 ? 0.4270 0.3790 0.6343 -0.0187 -0.0849 -0.1523 140 GLU A C 863 O O . GLU A 113 ? 0.2979 0.2679 0.5001 -0.0204 -0.0831 -0.1429 140 GLU A O 864 C CB . GLU A 113 ? 0.4218 0.3712 0.6120 -0.0054 -0.1042 -0.1900 140 GLU A CB 865 C CG . GLU A 113 ? 0.5971 0.5516 0.7461 0.0063 -0.1032 -0.2039 140 GLU A CG 866 C CD . GLU A 113 ? 0.7475 0.6979 0.9157 0.0083 -0.1191 -0.2182 140 GLU A CD 867 O OE1 . GLU A 113 ? 0.8130 0.7551 1.0251 0.0014 -0.1299 -0.2174 140 GLU A OE1 868 O OE2 . GLU A 113 ? 0.7681 0.7222 0.9068 0.0166 -0.1196 -0.2284 140 GLU A OE2 869 N N . GLN A 114 ? 0.3796 0.3146 0.6188 -0.0252 -0.0808 -0.1363 141 GLN A N 870 C CA . GLN A 114 ? 0.3728 0.3085 0.6442 -0.0353 -0.0725 -0.1059 141 GLN A CA 871 C C . GLN A 114 ? 0.3659 0.3127 0.6010 -0.0316 -0.0507 -0.0791 141 GLN A C 872 O O . GLN A 114 ? 0.3104 0.2697 0.5572 -0.0369 -0.0446 -0.0588 141 GLN A O 873 C CB . GLN A 114 ? 0.4020 0.3115 0.7085 -0.0412 -0.0719 -0.0957 141 GLN A CB 874 C CG . GLN A 114 ? 0.5547 0.4619 0.9016 -0.0528 -0.0658 -0.0680 141 GLN A CG 875 C CD . GLN A 114 ? 0.6920 0.6150 1.0746 -0.0601 -0.0803 -0.0764 141 GLN A CD 876 O OE1 . GLN A 114 ? 0.7382 0.6649 1.1228 -0.0567 -0.0975 -0.1024 141 GLN A OE1 877 N NE2 . GLN A 114 ? 0.6984 0.6317 1.1060 -0.0685 -0.0721 -0.0530 141 GLN A NE2 878 N N . TRP A 115 ? 0.3698 0.3120 0.5619 -0.0223 -0.0393 -0.0797 142 TRP A N 879 C CA . TRP A 115 ? 0.3120 0.2629 0.4632 -0.0175 -0.0196 -0.0580 142 TRP A CA 880 C C . TRP A 115 ? 0.3117 0.2861 0.4408 -0.0157 -0.0205 -0.0610 142 TRP A C 881 O O . TRP A 115 ? 0.2829 0.2677 0.4085 -0.0178 -0.0102 -0.0374 142 TRP A O 882 C CB . TRP A 115 ? 0.2745 0.2186 0.3853 -0.0079 -0.0117 -0.0678 142 TRP A CB 883 C CG . TRP A 115 ? 0.3286 0.2766 0.3976 -0.0029 0.0083 -0.0466 142 TRP A CG 884 C CD1 . TRP A 115 ? 0.3756 0.3311 0.4353 -0.0050 0.0206 -0.0187 142 TRP A CD1 885 C CD2 . TRP A 115 ? 0.3307 0.2750 0.3618 0.0052 0.0181 -0.0523 142 TRP A CD2 886 N NE1 . TRP A 115 ? 0.3397 0.2946 0.3559 0.0015 0.0367 -0.0067 142 TRP A NE1 887 C CE2 . TRP A 115 ? 0.3230 0.2718 0.3225 0.0072 0.0354 -0.0272 142 TRP A CE2 888 C CE3 . TRP A 115 ? 0.3180 0.2563 0.3405 0.0110 0.0141 -0.0766 142 TRP A CE3 889 C CZ2 . TRP A 115 ? 0.3556 0.3028 0.3165 0.0139 0.0478 -0.0261 142 TRP A CZ2 890 C CZ3 . TRP A 115 ? 0.3197 0.2583 0.3056 0.0177 0.0274 -0.0755 142 TRP A CZ3 891 C CH2 . TRP A 115 ? 0.3388 0.2817 0.2950 0.0186 0.0437 -0.0506 142 TRP A CH2 892 N N . TRP A 116 ? 0.3323 0.3135 0.4460 -0.0108 -0.0332 -0.0905 143 TRP A N 893 C CA . TRP A 116 ? 0.3829 0.3832 0.4699 -0.0066 -0.0364 -0.0980 143 TRP A CA 894 C C . TRP A 116 ? 0.3569 0.3703 0.4833 -0.0143 -0.0455 -0.0888 143 TRP A C 895 O O . TRP A 116 ? 0.2918 0.3212 0.4003 -0.0124 -0.0393 -0.0763 143 TRP A O 896 C CB . TRP A 116 ? 0.4208 0.4202 0.4868 0.0007 -0.0501 -0.1336 143 TRP A CB 897 C CG . TRP A 116 ? 0.3932 0.4075 0.4235 0.0074 -0.0542 -0.1449 143 TRP A CG 898 C CD1 . TRP A 116 ? 0.3638 0.3839 0.3365 0.0156 -0.0398 -0.1418 143 TRP A CD1 899 C CD2 . TRP A 116 ? 0.3518 0.3749 0.3999 0.0073 -0.0748 -0.1626 143 TRP A CD2 900 N NE1 . TRP A 116 ? 0.3593 0.3888 0.3124 0.0206 -0.0480 -0.1501 143 TRP A NE1 901 C CE2 . TRP A 116 ? 0.3656 0.3987 0.3626 0.0169 -0.0720 -0.1691 143 TRP A CE2 902 C CE3 . TRP A 116 ? 0.3401 0.3625 0.4424 0.0002 -0.0960 -0.1740 143 TRP A CE3 903 C CZ2 . TRP A 116 ? 0.3776 0.4189 0.3763 0.0204 -0.0859 -0.1773 143 TRP A CZ2 904 C CZ3 . TRP A 116 ? 0.3699 0.4032 0.4754 0.0032 -0.1148 -0.1920 143 TRP A CZ3 905 C CH2 . TRP A 116 ? 0.4273 0.4698 0.4795 0.0143 -0.1085 -0.1916 143 TRP A CH2 906 N N . GLU A 117 ? 0.3519 0.3585 0.5328 -0.0230 -0.0601 -0.0954 144 GLU A N 907 C CA . GLU A 117 ? 0.3954 0.4151 0.6220 -0.0319 -0.0691 -0.0880 144 GLU A CA 908 C C . GLU A 117 ? 0.3026 0.3257 0.5458 -0.0384 -0.0509 -0.0512 144 GLU A C 909 O O . GLU A 117 ? 0.2584 0.3003 0.5130 -0.0408 -0.0499 -0.0399 144 GLU A O 910 C CB . GLU A 117 ? 0.4672 0.4768 0.7489 -0.0405 -0.0897 -0.1059 144 GLU A CB 911 C CG . GLU A 117 ? 0.5775 0.5894 0.8500 -0.0345 -0.1121 -0.1426 144 GLU A CG 912 C CD . GLU A 117 ? 0.7369 0.7308 1.0496 -0.0400 -0.1297 -0.1620 144 GLU A CD 913 O OE1 . GLU A 117 ? 0.7729 0.7602 1.1327 -0.0503 -0.1290 -0.1467 144 GLU A OE1 914 O OE2 . GLU A 117 ? 0.7793 0.7662 1.0607 -0.0287 -0.1354 -0.1822 144 GLU A OE2 915 N N . ASP A 118 ? 0.2568 0.2609 0.5006 -0.0401 -0.0368 -0.0331 145 ASP A N 916 C CA . ASP A 118 ? 0.2653 0.2673 0.5238 -0.0455 -0.0190 0.0023 145 ASP A CA 917 C C . ASP A 118 ? 0.2715 0.2861 0.4818 -0.0378 -0.0014 0.0217 145 ASP A C 918 O O . ASP A 118 ? 0.2935 0.3105 0.5120 -0.0408 0.0131 0.0507 145 ASP A O 919 C CB . ASP A 118 ? 0.2384 0.2124 0.5070 -0.0478 -0.0101 0.0153 145 ASP A CB 920 C CG . ASP A 118 ? 0.3406 0.2995 0.6650 -0.0580 -0.0241 0.0054 145 ASP A CG 921 O OD1 . ASP A 118 ? 0.3210 0.2925 0.6829 -0.0652 -0.0391 -0.0073 145 ASP A OD1 922 O OD2 . ASP A 118 ? 0.4018 0.3352 0.7325 -0.0584 -0.0205 0.0102 145 ASP A OD2 923 N N . CYS A 119 ? 0.3034 0.2710 0.3831 0.0081 -0.0420 -0.0207 146 CYS A N 924 C CA . CYS A 119 ? 0.2476 0.2184 0.3064 0.0101 -0.0379 -0.0184 146 CYS A CA 925 C C . CYS A 119 ? 0.3277 0.3031 0.3878 0.0151 -0.0443 -0.0282 146 CYS A C 926 O O . CYS A 119 ? 0.3164 0.2927 0.3602 0.0178 -0.0430 -0.0276 146 CYS A O 927 C CB . CYS A 119 ? 0.2598 0.2260 0.2922 0.0126 -0.0375 -0.0156 146 CYS A CB 928 S SG . CYS A 119 ? 0.3265 0.2886 0.3514 0.0088 -0.0296 -0.0040 146 CYS A SG 929 N N . ARG A 120 ? 0.3884 0.3661 0.4688 0.0171 -0.0522 -0.0379 147 ARG A N 930 C CA . ARG A 120 ? 0.3790 0.3614 0.4615 0.0236 -0.0601 -0.0487 147 ARG A CA 931 C C . ARG A 120 ? 0.3724 0.3609 0.4572 0.0228 -0.0553 -0.0473 147 ARG A C 932 O O . ARG A 120 ? 0.3002 0.2886 0.3710 0.0292 -0.0598 -0.0517 147 ARG A O 933 C CB . ARG A 120 ? 0.3694 0.3553 0.4800 0.0256 -0.0696 -0.0607 147 ARG A CB 934 C CG . ARG A 120 ? 0.3274 0.3193 0.4422 0.0337 -0.0790 -0.0733 147 ARG A CG 935 C CD . ARG A 120 ? 0.4838 0.4806 0.6301 0.0361 -0.0895 -0.0873 147 ARG A CD 936 N NE . ARG A 120 ? 0.5665 0.5674 0.7482 0.0257 -0.0833 -0.0843 147 ARG A NE 937 C CZ . ARG A 120 ? 0.5683 0.5787 0.7697 0.0218 -0.0786 -0.0850 147 ARG A CZ 938 N NH1 . ARG A 120 ? 0.4759 0.4915 0.6650 0.0282 -0.0809 -0.0898 147 ARG A NH1 939 N NH2 . ARG A 120 ? 0.6292 0.6439 0.8630 0.0115 -0.0712 -0.0804 147 ARG A NH2 940 N N . THR A 121 ? 0.3517 0.3457 0.4538 0.0155 -0.0462 -0.0410 148 THR A N 941 C CA . THR A 121 ? 0.3561 0.3598 0.4651 0.0153 -0.0415 -0.0416 148 THR A CA 942 C C . THR A 121 ? 0.3551 0.3577 0.4400 0.0155 -0.0339 -0.0331 148 THR A C 943 O O . THR A 121 ? 0.3714 0.3825 0.4592 0.0163 -0.0299 -0.0338 148 THR A O 944 C CB . THR A 121 ? 0.3135 0.3273 0.4552 0.0077 -0.0343 -0.0394 148 THR A CB 945 O OG1 . THR A 121 ? 0.3265 0.3368 0.4658 0.0008 -0.0240 -0.0257 148 THR A OG1 946 C CG2 . THR A 121 ? 0.2292 0.2445 0.4003 0.0074 -0.0433 -0.0501 148 THR A CG2 947 N N . SER A 122 ? 0.3480 0.3412 0.4108 0.0154 -0.0327 -0.0266 149 SER A N 948 C CA . SER A 122 ? 0.2619 0.2534 0.3032 0.0162 -0.0275 -0.0206 149 SER A CA 949 C C . SER A 122 ? 0.2578 0.2423 0.2795 0.0223 -0.0348 -0.0251 149 SER A C 950 O O . SER A 122 ? 0.2326 0.2137 0.2539 0.0264 -0.0431 -0.0315 149 SER A O 951 C CB . SER A 122 ? 0.3034 0.2893 0.3336 0.0128 -0.0222 -0.0115 149 SER A CB 952 O OG . SER A 122 ? 0.3536 0.3442 0.3987 0.0076 -0.0145 -0.0046 149 SER A OG 953 N N . TYR A 123 ? 0.3183 0.3006 0.3241 0.0234 -0.0319 -0.0217 150 TYR A N 954 C CA . TYR A 123 ? 0.3226 0.2964 0.3112 0.0281 -0.0379 -0.0240 150 TYR A CA 955 C C . TYR A 123 ? 0.3501 0.3167 0.3211 0.0261 -0.0350 -0.0179 150 TYR A C 956 O O . TYR A 123 ? 0.2931 0.2629 0.2638 0.0229 -0.0288 -0.0133 150 TYR A O 957 C CB . TYR A 123 ? 0.3063 0.2839 0.2975 0.0323 -0.0397 -0.0287 150 TYR A CB 958 C CG . TYR A 123 ? 0.3412 0.3271 0.3510 0.0353 -0.0439 -0.0368 150 TYR A CG 959 C CD1 . TYR A 123 ? 0.4190 0.3997 0.4249 0.0422 -0.0538 -0.0438 150 TYR A CD1 960 C CD2 . TYR A 123 ? 0.3274 0.3264 0.3593 0.0313 -0.0379 -0.0374 150 TYR A CD2 961 C CE1 . TYR A 123 ? 0.4811 0.4706 0.5057 0.0459 -0.0590 -0.0532 150 TYR A CE1 962 C CE2 . TYR A 123 ? 0.3557 0.3641 0.4089 0.0333 -0.0417 -0.0461 150 TYR A CE2 963 C CZ . TYR A 123 ? 0.4695 0.4736 0.5194 0.0410 -0.0529 -0.0551 150 TYR A CZ 964 O OH . TYR A 123 ? 0.5237 0.5380 0.5960 0.0441 -0.0581 -0.0657 150 TYR A OH 965 N N . THR A 124 ? 0.4108 0.3679 0.3674 0.0284 -0.0396 -0.0176 151 THR A N 966 C CA . THR A 124 ? 0.3714 0.3222 0.3145 0.0260 -0.0371 -0.0127 151 THR A CA 967 C C . THR A 124 ? 0.3216 0.2619 0.2527 0.0289 -0.0420 -0.0122 151 THR A C 968 O O . THR A 124 ? 0.3595 0.2969 0.2898 0.0338 -0.0477 -0.0153 151 THR A O 969 C CB . THR A 124 ? 0.3080 0.2588 0.2477 0.0228 -0.0348 -0.0096 151 THR A CB 970 O OG1 . THR A 124 ? 0.3229 0.2708 0.2541 0.0199 -0.0316 -0.0060 151 THR A OG1 971 C CG2 . THR A 124 ? 0.2493 0.1967 0.1828 0.0257 -0.0395 -0.0111 151 THR A CG2 972 N N . CYS A 125 ? 0.3657 0.2996 0.2883 0.0262 -0.0401 -0.0082 152 CYS A N 973 C CA . CYS A 125 ? 0.3581 0.2798 0.2712 0.0279 -0.0441 -0.0058 152 CYS A CA 974 C C . CYS A 125 ? 0.3683 0.2838 0.2706 0.0243 -0.0415 0.0008 152 CYS A C 975 O O . CYS A 125 ? 0.3602 0.2644 0.2545 0.0244 -0.0433 0.0053 152 CYS A O 976 C CB . CYS A 125 ? 0.2811 0.1995 0.1973 0.0282 -0.0452 -0.0079 152 CYS A CB 977 S SG . CYS A 125 ? 0.3688 0.2930 0.2884 0.0230 -0.0395 -0.0075 152 CYS A SG 978 N N . LYS A 126 ? 0.3414 0.2646 0.2446 0.0212 -0.0371 0.0016 153 LYS A N 979 C CA . LYS A 126 ? 0.3563 0.2778 0.2512 0.0178 -0.0335 0.0069 153 LYS A CA 980 C C . LYS A 126 ? 0.3127 0.2448 0.2095 0.0174 -0.0311 0.0048 153 LYS A C 981 O O . LYS A 126 ? 0.3087 0.2473 0.2149 0.0180 -0.0315 0.0006 153 LYS A O 982 C CB . LYS A 126 ? 0.3777 0.2957 0.2752 0.0120 -0.0302 0.0095 153 LYS A CB 983 C CG . LYS A 126 ? 0.3698 0.2973 0.2757 0.0091 -0.0270 0.0059 153 LYS A CG 984 C CD . LYS A 126 ? 0.3457 0.2702 0.2571 0.0058 -0.0267 0.0049 153 LYS A CD 985 C CE . LYS A 126 ? 0.3385 0.2548 0.2481 0.0008 -0.0250 0.0103 153 LYS A CE 986 N NZ . LYS A 126 ? 0.3374 0.2599 0.2434 -0.0027 -0.0195 0.0141 153 LYS A NZ 987 N N . SER A 127 ? 0.3627 0.2967 0.2512 0.0167 -0.0285 0.0079 154 SER A N 988 C CA . SER A 127 ? 0.3187 0.2629 0.2086 0.0180 -0.0277 0.0044 154 SER A CA 989 C C . SER A 127 ? 0.3432 0.2939 0.2375 0.0128 -0.0226 0.0045 154 SER A C 990 O O . SER A 127 ? 0.3639 0.3221 0.2638 0.0137 -0.0231 0.0002 154 SER A O 991 C CB . SER A 127 ? 0.3548 0.3009 0.2322 0.0231 -0.0288 0.0055 154 SER A CB 992 O OG . SER A 127 ? 0.4331 0.3762 0.3001 0.0199 -0.0233 0.0134 154 SER A OG 993 N N . ASN A 128 ? 0.3842 0.3315 0.2776 0.0077 -0.0187 0.0089 155 ASN A N 994 C CA . ASN A 128 ? 0.2955 0.2496 0.1957 0.0031 -0.0149 0.0073 155 ASN A CA 995 C C . ASN A 128 ? 0.3024 0.2538 0.2110 0.0016 -0.0164 0.0047 155 ASN A C 996 O O . ASN A 128 ? 0.3641 0.3093 0.2749 -0.0012 -0.0163 0.0063 155 ASN A O 997 C CB . ASN A 128 ? 0.3125 0.2672 0.2101 -0.0021 -0.0092 0.0125 155 ASN A CB 998 C CG . ASN A 128 ? 0.3416 0.3063 0.2486 -0.0064 -0.0057 0.0090 155 ASN A CG 999 O OD1 . ASN A 128 ? 0.3763 0.3444 0.2904 -0.0053 -0.0083 0.0032 155 ASN A OD1 1000 N ND2 . ASN A 128 ? 0.3795 0.3496 0.2866 -0.0110 0.0006 0.0128 155 ASN A ND2 1001 N N . TRP A 129 ? 0.2933 0.2493 0.2065 0.0042 -0.0182 0.0008 156 TRP A N 1002 C CA . TRP A 129 ? 0.2620 0.2175 0.1801 0.0048 -0.0191 -0.0014 156 TRP A CA 1003 C C . TRP A 129 ? 0.3220 0.2825 0.2444 0.0025 -0.0179 -0.0042 156 TRP A C 1004 O O . TRP A 129 ? 0.3721 0.3334 0.2970 0.0044 -0.0193 -0.0070 156 TRP A O 1005 C CB . TRP A 129 ? 0.2212 0.1794 0.1419 0.0083 -0.0203 -0.0023 156 TRP A CB 1006 C CG . TRP A 129 ? 0.2690 0.2240 0.1906 0.0105 -0.0221 -0.0014 156 TRP A CG 1007 C CD1 . TRP A 129 ? 0.3076 0.2578 0.2254 0.0112 -0.0240 -0.0006 156 TRP A CD1 1008 C CD2 . TRP A 129 ? 0.2804 0.2373 0.2080 0.0125 -0.0223 -0.0014 156 TRP A CD2 1009 N NE1 . TRP A 129 ? 0.2745 0.2245 0.1968 0.0140 -0.0263 -0.0019 156 TRP A NE1 1010 C CE2 . TRP A 129 ? 0.2801 0.2347 0.2099 0.0140 -0.0246 -0.0022 156 TRP A CE2 1011 C CE3 . TRP A 129 ? 0.2940 0.2544 0.2256 0.0132 -0.0204 0.0000 156 TRP A CE3 1012 C CZ2 . TRP A 129 ? 0.3053 0.2626 0.2444 0.0152 -0.0247 -0.0027 156 TRP A CZ2 1013 C CZ3 . TRP A 129 ? 0.2719 0.2336 0.2111 0.0139 -0.0194 0.0016 156 TRP A CZ3 1014 C CH2 . TRP A 129 ? 0.2797 0.2407 0.2242 0.0144 -0.0214 -0.0002 156 TRP A CH2 1015 N N . HIS A 130 ? 0.3005 0.2657 0.2238 -0.0006 -0.0153 -0.0044 157 HIS A N 1016 C CA . HIS A 130 ? 0.3178 0.2893 0.2482 -0.0028 -0.0146 -0.0087 157 HIS A CA 1017 C C . HIS A 130 ? 0.3190 0.2859 0.2557 -0.0074 -0.0142 -0.0087 157 HIS A C 1018 O O . HIS A 130 ? 0.2868 0.2582 0.2323 -0.0084 -0.0155 -0.0143 157 HIS A O 1019 C CB . HIS A 130 ? 0.3056 0.2872 0.2379 -0.0042 -0.0118 -0.0105 157 HIS A CB 1020 C CG . HIS A 130 ? 0.2967 0.2866 0.2390 -0.0063 -0.0115 -0.0165 157 HIS A CG 1021 N ND1 . HIS A 130 ? 0.2919 0.2846 0.2370 -0.0018 -0.0158 -0.0224 157 HIS A ND1 1022 C CD2 . HIS A 130 ? 0.2648 0.2614 0.2160 -0.0122 -0.0074 -0.0176 157 HIS A CD2 1023 C CE1 . HIS A 130 ? 0.3143 0.3153 0.2699 -0.0040 -0.0158 -0.0286 157 HIS A CE1 1024 N NE2 . HIS A 130 ? 0.3116 0.3156 0.2729 -0.0111 -0.0104 -0.0259 157 HIS A NE2 1025 N N . LYS A 131 ? 0.3069 0.2642 0.2402 -0.0096 -0.0135 -0.0030 158 LYS A N 1026 C CA . LYS A 131 ? 0.3941 0.3442 0.3350 -0.0145 -0.0138 -0.0021 158 LYS A CA 1027 C C . LYS A 131 ? 0.4180 0.3544 0.3539 -0.0131 -0.0168 0.0022 158 LYS A C 1028 O O . LYS A 131 ? 0.3500 0.2835 0.2760 -0.0090 -0.0176 0.0051 158 LYS A O 1029 C CB . LYS A 131 ? 0.4248 0.3781 0.3706 -0.0219 -0.0076 0.0024 158 LYS A CB 1030 C CG . LYS A 131 ? 0.5069 0.4556 0.4403 -0.0225 -0.0034 0.0120 158 LYS A CG 1031 C CD . LYS A 131 ? 0.6412 0.5935 0.5790 -0.0302 0.0044 0.0184 158 LYS A CD 1032 C CE . LYS A 131 ? 0.7090 0.6549 0.6312 -0.0294 0.0082 0.0294 158 LYS A CE 1033 N NZ . LYS A 131 ? 0.7638 0.7152 0.6882 -0.0367 0.0180 0.0376 158 LYS A NZ 1034 N N . GLY A 132 ? 0.3645 0.2925 0.3092 -0.0160 -0.0194 0.0012 159 GLY A N 1035 C CA . GLY A 132 ? 0.3177 0.2310 0.2591 -0.0148 -0.0231 0.0051 159 GLY A CA 1036 C C . GLY A 132 ? 0.3590 0.2708 0.2990 -0.0071 -0.0295 -0.0014 159 GLY A C 1037 O O . GLY A 132 ? 0.3830 0.2843 0.3192 -0.0044 -0.0333 0.0007 159 GLY A O 1038 N N . TRP A 133 ? 0.3296 0.2525 0.2720 -0.0030 -0.0308 -0.0090 160 TRP A N 1039 C CA . TRP A 133 ? 0.3703 0.2950 0.3113 0.0045 -0.0354 -0.0150 160 TRP A CA 1040 C C . TRP A 133 ? 0.4111 0.3309 0.3622 0.0061 -0.0418 -0.0226 160 TRP A C 1041 O O . TRP A 133 ? 0.3900 0.3083 0.3518 0.0015 -0.0427 -0.0251 160 TRP A O 1042 C CB . TRP A 133 ? 0.3064 0.2447 0.2441 0.0092 -0.0334 -0.0186 160 TRP A CB 1043 C CG . TRP A 133 ? 0.3252 0.2675 0.2556 0.0089 -0.0289 -0.0129 160 TRP A CG 1044 C CD1 . TRP A 133 ? 0.2975 0.2454 0.2269 0.0063 -0.0254 -0.0108 160 TRP A CD1 1045 C CD2 . TRP A 133 ? 0.3390 0.2808 0.2650 0.0118 -0.0285 -0.0101 160 TRP A CD2 1046 N NE1 . TRP A 133 ? 0.3078 0.2574 0.2323 0.0075 -0.0235 -0.0071 160 TRP A NE1 1047 C CE2 . TRP A 133 ? 0.3235 0.2697 0.2468 0.0105 -0.0252 -0.0065 160 TRP A CE2 1048 C CE3 . TRP A 133 ? 0.2860 0.2250 0.2120 0.0157 -0.0314 -0.0116 160 TRP A CE3 1049 C CZ2 . TRP A 133 ? 0.3212 0.2683 0.2434 0.0124 -0.0247 -0.0045 160 TRP A CZ2 1050 C CZ3 . TRP A 133 ? 0.2912 0.2325 0.2158 0.0175 -0.0303 -0.0094 160 TRP A CZ3 1051 C CH2 . TRP A 133 ? 0.3540 0.2990 0.2775 0.0156 -0.0271 -0.0060 160 TRP A CH2 1052 N N . ASN A 134 ? 0.3954 0.3140 0.3451 0.0130 -0.0466 -0.0273 161 ASN A N 1053 C CA . ASN A 134 ? 0.4112 0.3278 0.3703 0.0174 -0.0543 -0.0374 161 ASN A CA 1054 C C . ASN A 134 ? 0.4003 0.3331 0.3575 0.0252 -0.0549 -0.0463 161 ASN A C 1055 O O . ASN A 134 ? 0.4046 0.3466 0.3531 0.0313 -0.0525 -0.0461 161 ASN A O 1056 C CB . ASN A 134 ? 0.4630 0.3704 0.4214 0.0221 -0.0599 -0.0388 161 ASN A CB 1057 C CG . ASN A 134 ? 0.4822 0.3852 0.4521 0.0270 -0.0696 -0.0503 161 ASN A CG 1058 O OD1 . ASN A 134 ? 0.5142 0.4274 0.4894 0.0311 -0.0723 -0.0601 161 ASN A OD1 1059 N ND2 . ASN A 134 ? 0.5708 0.4584 0.5445 0.0277 -0.0759 -0.0499 161 ASN A ND2 1060 N N . TRP A 135 ? 0.4006 0.3376 0.3663 0.0253 -0.0580 -0.0537 162 TRP A N 1061 C CA . TRP A 135 ? 0.4519 0.4044 0.4130 0.0338 -0.0588 -0.0616 162 TRP A CA 1062 C C . TRP A 135 ? 0.4555 0.4127 0.4218 0.0439 -0.0679 -0.0757 162 TRP A C 1063 O O . TRP A 135 ? 0.4227 0.3923 0.3863 0.0519 -0.0704 -0.0841 162 TRP A O 1064 C CB . TRP A 135 ? 0.3442 0.3020 0.3093 0.0299 -0.0570 -0.0623 162 TRP A CB 1065 C CG . TRP A 135 ? 0.3423 0.3008 0.3000 0.0235 -0.0486 -0.0510 162 TRP A CG 1066 C CD1 . TRP A 135 ? 0.3679 0.3187 0.3298 0.0136 -0.0445 -0.0432 162 TRP A CD1 1067 C CD2 . TRP A 135 ? 0.3497 0.3170 0.2947 0.0275 -0.0436 -0.0464 162 TRP A CD2 1068 N NE1 . TRP A 135 ? 0.3262 0.2817 0.2791 0.0120 -0.0383 -0.0361 162 TRP A NE1 1069 C CE2 . TRP A 135 ? 0.3569 0.3212 0.3007 0.0199 -0.0381 -0.0378 162 TRP A CE2 1070 C CE3 . TRP A 135 ? 0.3423 0.3197 0.2769 0.0370 -0.0432 -0.0483 162 TRP A CE3 1071 C CZ2 . TRP A 135 ? 0.3200 0.2896 0.2549 0.0214 -0.0336 -0.0323 162 TRP A CZ2 1072 C CZ3 . TRP A 135 ? 0.3268 0.3082 0.2519 0.0374 -0.0375 -0.0405 162 TRP A CZ3 1073 C CH2 . TRP A 135 ? 0.3410 0.3177 0.2675 0.0295 -0.0335 -0.0332 162 TRP A CH2 1074 N N . THR A 136 ? 0.4530 0.4003 0.4260 0.0448 -0.0736 -0.0789 163 THR A N 1075 C CA . THR A 136 ? 0.5352 0.4859 0.5154 0.0550 -0.0840 -0.0942 163 THR A CA 1076 C C . THR A 136 ? 0.5567 0.5273 0.5236 0.0687 -0.0833 -0.1012 163 THR A C 1077 O O . THR A 136 ? 0.5980 0.5780 0.5678 0.0786 -0.0906 -0.1150 163 THR A O 1078 C CB . THR A 136 ? 0.5681 0.5041 0.5556 0.0547 -0.0902 -0.0954 163 THR A CB 1079 O OG1 . THR A 136 ? 0.5884 0.5054 0.5902 0.0436 -0.0927 -0.0909 163 THR A OG1 1080 C CG2 . THR A 136 ? 0.6275 0.5699 0.6207 0.0678 -0.1012 -0.1126 163 THR A CG2 1081 N N . SER A 137 ? 0.4924 0.4699 0.4455 0.0698 -0.0745 -0.0917 164 SER A N 1082 C CA . SER A 137 ? 0.4987 0.4953 0.4392 0.0820 -0.0716 -0.0956 164 SER A CA 1083 C C . SER A 137 ? 0.5424 0.5513 0.4714 0.0859 -0.0668 -0.0933 164 SER A C 1084 O O . SER A 137 ? 0.5673 0.5924 0.4837 0.0965 -0.0634 -0.0946 164 SER A O 1085 C CB . SER A 137 ? 0.5076 0.5075 0.4416 0.0809 -0.0636 -0.0863 164 SER A CB 1086 O OG . SER A 137 ? 0.5386 0.5346 0.4678 0.0713 -0.0544 -0.0719 164 SER A OG 1087 N N . GLY A 138 ? 0.4565 0.4584 0.3895 0.0780 -0.0664 -0.0895 165 GLY A N 1088 C CA . GLY A 138 ? 0.4416 0.4530 0.3637 0.0816 -0.0626 -0.0866 165 GLY A CA 1089 C C . GLY A 138 ? 0.4868 0.4950 0.4014 0.0733 -0.0520 -0.0704 165 GLY A C 1090 O O . GLY A 138 ? 0.5179 0.5294 0.4254 0.0738 -0.0491 -0.0660 165 GLY A O 1091 N N . PHE A 139 ? 0.4747 0.4763 0.3916 0.0667 -0.0474 -0.0625 166 PHE A N 1092 C CA . PHE A 139 ? 0.4487 0.4453 0.3629 0.0580 -0.0395 -0.0492 166 PHE A CA 1093 C C . PHE A 139 ? 0.3513 0.3346 0.2746 0.0487 -0.0403 -0.0459 166 PHE A C 1094 O O . PHE A 139 ? 0.3674 0.3449 0.2979 0.0493 -0.0462 -0.0523 166 PHE A O 1095 C CB . PHE A 139 ? 0.4514 0.4577 0.3560 0.0620 -0.0313 -0.0413 166 PHE A CB 1096 C CG . PHE A 139 ? 0.4103 0.4228 0.3162 0.0668 -0.0310 -0.0448 166 PHE A CG 1097 C CD1 . PHE A 139 ? 0.4381 0.4448 0.3509 0.0608 -0.0290 -0.0407 166 PHE A CD1 1098 C CD2 . PHE A 139 ? 0.4211 0.4468 0.3214 0.0786 -0.0332 -0.0534 166 PHE A CD2 1099 C CE1 . PHE A 139 ? 0.4440 0.4578 0.3596 0.0660 -0.0293 -0.0453 166 PHE A CE1 1100 C CE2 . PHE A 139 ? 0.4444 0.4781 0.3468 0.0839 -0.0330 -0.0581 166 PHE A CE2 1101 C CZ . PHE A 139 ? 0.4210 0.4487 0.3319 0.0773 -0.0310 -0.0541 166 PHE A CZ 1102 N N . ASN A 140 ? 0.3396 0.3177 0.2622 0.0411 -0.0351 -0.0363 167 ASN A N 1103 C CA . ASN A 140 ? 0.3199 0.2858 0.2479 0.0334 -0.0357 -0.0324 167 ASN A CA 1104 C C . ASN A 140 ? 0.3199 0.2839 0.2483 0.0347 -0.0355 -0.0308 167 ASN A C 1105 O O . ASN A 140 ? 0.3277 0.2993 0.2535 0.0368 -0.0308 -0.0273 167 ASN A O 1106 C CB . ASN A 140 ? 0.3580 0.3211 0.2846 0.0265 -0.0314 -0.0248 167 ASN A CB 1107 C CG . ASN A 140 ? 0.3564 0.3260 0.2780 0.0280 -0.0259 -0.0188 167 ASN A CG 1108 O OD1 . ASN A 140 ? 0.3731 0.3506 0.2900 0.0327 -0.0241 -0.0189 167 ASN A OD1 1109 N ND2 . ASN A 140 ? 0.2834 0.2491 0.2063 0.0243 -0.0238 -0.0135 167 ASN A ND2 1110 N N . LYS A 141 ? 0.3601 0.3137 0.2933 0.0335 -0.0409 -0.0335 168 LYS A N 1111 C CA . LYS A 141 ? 0.3718 0.3212 0.3058 0.0348 -0.0423 -0.0324 168 LYS A CA 1112 C C . LYS A 141 ? 0.2880 0.2221 0.2220 0.0285 -0.0441 -0.0266 168 LYS A C 1113 O O . LYS A 141 ? 0.2851 0.2117 0.2210 0.0236 -0.0450 -0.0251 168 LYS A O 1114 C CB . LYS A 141 ? 0.3702 0.3213 0.3080 0.0424 -0.0486 -0.0418 168 LYS A CB 1115 C CG . LYS A 141 ? 0.3962 0.3655 0.3316 0.0504 -0.0455 -0.0469 168 LYS A CG 1116 C CD . LYS A 141 ? 0.5006 0.4735 0.4401 0.0593 -0.0526 -0.0584 168 LYS A CD 1117 C CE . LYS A 141 ? 0.5588 0.5527 0.4937 0.0684 -0.0484 -0.0632 168 LYS A CE 1118 N NZ . LYS A 141 ? 0.6091 0.6094 0.5480 0.0787 -0.0557 -0.0763 168 LYS A NZ 1119 N N . CYS A 142 ? 0.3179 0.2486 0.2498 0.0290 -0.0443 -0.0234 169 CYS A N 1120 C CA . CYS A 142 ? 0.3477 0.2643 0.2761 0.0252 -0.0463 -0.0174 169 CYS A CA 1121 C C . CYS A 142 ? 0.4248 0.3276 0.3565 0.0251 -0.0526 -0.0192 169 CYS A C 1122 O O . CYS A 142 ? 0.4145 0.3170 0.3508 0.0309 -0.0583 -0.0267 169 CYS A O 1123 C CB . CYS A 142 ? 0.3402 0.2561 0.2662 0.0288 -0.0480 -0.0166 169 CYS A CB 1124 S SG . CYS A 142 ? 0.3338 0.2652 0.2620 0.0288 -0.0419 -0.0158 169 CYS A SG 1125 N N . ALA A 143 ? 0.4360 0.3279 0.3665 0.0186 -0.0514 -0.0125 170 ALA A N 1126 C CA . ALA A 143 ? 0.4420 0.3177 0.3777 0.0169 -0.0570 -0.0120 170 ALA A CA 1127 C C . ALA A 143 ? 0.4882 0.3507 0.4187 0.0218 -0.0632 -0.0098 170 ALA A C 1128 O O . ALA A 143 ? 0.4928 0.3579 0.4146 0.0248 -0.0620 -0.0068 170 ALA A O 1129 C CB . ALA A 143 ? 0.4308 0.2997 0.3675 0.0076 -0.0521 -0.0033 170 ALA A CB 1130 N N . VAL A 144 ? 0.4729 0.3211 0.4101 0.0233 -0.0709 -0.0124 171 VAL A N 1131 C CA . VAL A 144 ? 0.5027 0.3342 0.4349 0.0282 -0.0782 -0.0095 171 VAL A CA 1132 C C . VAL A 144 ? 0.5513 0.3734 0.4697 0.0246 -0.0737 0.0044 171 VAL A C 1133 O O . VAL A 144 ? 0.5585 0.3768 0.4758 0.0161 -0.0671 0.0136 171 VAL A O 1134 C CB . VAL A 144 ? 0.6206 0.4332 0.5634 0.0281 -0.0870 -0.0118 171 VAL A CB 1135 C CG1 . VAL A 144 ? 0.6256 0.4173 0.5614 0.0332 -0.0950 -0.0065 171 VAL A CG1 1136 C CG2 . VAL A 144 ? 0.5672 0.3904 0.5227 0.0344 -0.0933 -0.0280 171 VAL A CG2 1137 N N . GLY A 145 ? 0.5161 0.3364 0.4242 0.0318 -0.0772 0.0052 172 GLY A N 1138 C CA . GLY A 145 ? 0.5195 0.3323 0.4118 0.0313 -0.0742 0.0169 172 GLY A CA 1139 C C . GLY A 145 ? 0.5352 0.3664 0.4216 0.0312 -0.0674 0.0165 172 GLY A C 1140 O O . GLY A 145 ? 0.6476 0.4765 0.5205 0.0341 -0.0668 0.0226 172 GLY A O 1141 N N . ALA A 146 ? 0.4309 0.2798 0.3270 0.0287 -0.0630 0.0090 173 ALA A N 1142 C CA . ALA A 146 ? 0.3942 0.2593 0.2879 0.0284 -0.0575 0.0079 173 ALA A CA 1143 C C . ALA A 146 ? 0.4337 0.3089 0.3320 0.0357 -0.0616 -0.0010 173 ALA A C 1144 O O . ALA A 146 ? 0.4631 0.3485 0.3720 0.0367 -0.0614 -0.0086 173 ALA A O 1145 C CB . ALA A 146 ? 0.3436 0.2209 0.2448 0.0217 -0.0503 0.0064 173 ALA A CB 1146 N N . ALA A 147 ? 0.4261 0.2997 0.3169 0.0412 -0.0651 -0.0004 174 ALA A N 1147 C CA . ALA A 147 ? 0.4277 0.3102 0.3257 0.0483 -0.0701 -0.0096 174 ALA A CA 1148 C C . ALA A 147 ? 0.3938 0.2944 0.3010 0.0459 -0.0647 -0.0137 174 ALA A C 1149 O O . ALA A 147 ? 0.3591 0.2625 0.2615 0.0432 -0.0611 -0.0099 174 ALA A O 1150 C CB . ALA A 147 ? 0.4698 0.3429 0.3572 0.0565 -0.0780 -0.0090 174 ALA A CB 1151 N N . CYS A 148 ? 0.3762 0.2891 0.2974 0.0471 -0.0640 -0.0212 175 CYS A N 1152 C CA . CYS A 148 ? 0.4003 0.3288 0.3329 0.0449 -0.0592 -0.0241 175 CYS A CA 1153 C C . CYS A 148 ? 0.3745 0.3050 0.3094 0.0499 -0.0647 -0.0283 175 CYS A C 1154 O O . CYS A 148 ? 0.4147 0.3412 0.3488 0.0571 -0.0725 -0.0331 175 CYS A O 1155 C CB . CYS A 148 ? 0.3311 0.2729 0.2777 0.0453 -0.0560 -0.0297 175 CYS A CB 1156 S SG . CYS A 148 ? 0.3559 0.2999 0.3001 0.0410 -0.0497 -0.0268 175 CYS A SG 1157 N N . GLN A 149 ? 0.3561 0.2927 0.2942 0.0471 -0.0618 -0.0274 176 GLN A N 1158 C CA . GLN A 149 ? 0.3098 0.2496 0.2518 0.0523 -0.0679 -0.0331 176 GLN A CA 1159 C C . GLN A 149 ? 0.3419 0.2934 0.3002 0.0475 -0.0635 -0.0352 176 GLN A C 1160 O O . GLN A 149 ? 0.3371 0.2916 0.2981 0.0407 -0.0557 -0.0302 176 GLN A O 1161 C CB . GLN A 149 ? 0.3405 0.2699 0.2623 0.0562 -0.0717 -0.0288 176 GLN A CB 1162 C CG . GLN A 149 ? 0.3717 0.2859 0.2759 0.0597 -0.0751 -0.0231 176 GLN A CG 1163 C CD . GLN A 149 ? 0.4283 0.3389 0.3333 0.0694 -0.0851 -0.0300 176 GLN A CD 1164 O OE1 . GLN A 149 ? 0.3906 0.3123 0.3116 0.0730 -0.0891 -0.0401 176 GLN A OE1 1165 N NE2 . GLN A 149 ? 0.4189 0.3136 0.3078 0.0737 -0.0895 -0.0245 176 GLN A NE2 1166 N N . PRO A 150 ? 0.3668 0.3244 0.3369 0.0516 -0.0693 -0.0431 177 PRO A N 1167 C CA . PRO A 150 ? 0.2955 0.2615 0.2829 0.0469 -0.0664 -0.0451 177 PRO A CA 1168 C C . PRO A 150 ? 0.3284 0.2898 0.3033 0.0431 -0.0625 -0.0384 177 PRO A C 1169 O O . PRO A 150 ? 0.3272 0.2814 0.2819 0.0464 -0.0644 -0.0353 177 PRO A O 1170 C CB . PRO A 150 ? 0.3064 0.2764 0.3039 0.0542 -0.0766 -0.0561 177 PRO A CB 1171 C CG . PRO A 150 ? 0.3825 0.3512 0.3774 0.0613 -0.0829 -0.0611 177 PRO A CG 1172 C CD . PRO A 150 ? 0.4141 0.3709 0.3844 0.0612 -0.0799 -0.0517 177 PRO A CD 1173 N N . PHE A 151 ? 0.3214 0.2875 0.3086 0.0366 -0.0567 -0.0358 178 PHE A N 1174 C CA . PHE A 151 ? 0.3559 0.3189 0.3335 0.0334 -0.0531 -0.0306 178 PHE A CA 1175 C C . PHE A 151 ? 0.3411 0.3019 0.3067 0.0391 -0.0592 -0.0341 178 PHE A C 1176 O O . PHE A 151 ? 0.3608 0.3182 0.3093 0.0386 -0.0565 -0.0290 178 PHE A O 1177 C CB . PHE A 151 ? 0.3311 0.2985 0.3268 0.0278 -0.0491 -0.0292 178 PHE A CB 1178 C CG . PHE A 151 ? 0.3190 0.2840 0.3058 0.0230 -0.0421 -0.0212 178 PHE A CG 1179 C CD1 . PHE A 151 ? 0.3491 0.3144 0.3307 0.0202 -0.0356 -0.0154 178 PHE A CD1 1180 C CD2 . PHE A 151 ? 0.3883 0.3518 0.3725 0.0226 -0.0431 -0.0210 178 PHE A CD2 1181 C CE1 . PHE A 151 ? 0.3848 0.3486 0.3584 0.0173 -0.0306 -0.0095 178 PHE A CE1 1182 C CE2 . PHE A 151 ? 0.3705 0.3324 0.3472 0.0193 -0.0377 -0.0149 178 PHE A CE2 1183 C CZ . PHE A 151 ? 0.3343 0.2962 0.3055 0.0167 -0.0316 -0.0091 178 PHE A CZ 1184 N N . HIS A 152 ? 0.3560 0.3206 0.3314 0.0450 -0.0675 -0.0434 179 HIS A N 1185 C CA . HIS A 152 ? 0.3325 0.2979 0.2971 0.0524 -0.0740 -0.0485 179 HIS A CA 1186 C C . HIS A 152 ? 0.3706 0.3309 0.3101 0.0594 -0.0765 -0.0460 179 HIS A C 1187 O O . HIS A 152 ? 0.4001 0.3617 0.3247 0.0660 -0.0798 -0.0477 179 HIS A O 1188 C CB . HIS A 152 ? 0.3778 0.3495 0.3631 0.0576 -0.0835 -0.0613 179 HIS A CB 1189 C CG . HIS A 152 ? 0.3843 0.3588 0.3937 0.0508 -0.0816 -0.0627 179 HIS A CG 1190 N ND1 . HIS A 152 ? 0.3841 0.3633 0.4200 0.0526 -0.0893 -0.0736 179 HIS A ND1 1191 C CD2 . HIS A 152 ? 0.3477 0.3199 0.3595 0.0426 -0.0734 -0.0543 179 HIS A CD2 1192 C CE1 . HIS A 152 ? 0.3502 0.3285 0.4038 0.0451 -0.0854 -0.0705 179 HIS A CE1 1193 N NE2 . HIS A 152 ? 0.3493 0.3232 0.3870 0.0395 -0.0758 -0.0586 179 HIS A NE2 1194 N N . PHE A 153 ? 0.3954 0.3499 0.3298 0.0586 -0.0750 -0.0417 180 PHE A N 1195 C CA . PHE A 153 ? 0.3442 0.2900 0.2543 0.0635 -0.0760 -0.0357 180 PHE A CA 1196 C C . PHE A 153 ? 0.3964 0.3389 0.2906 0.0581 -0.0676 -0.0254 180 PHE A C 1197 O O . PHE A 153 ? 0.3609 0.3008 0.2352 0.0627 -0.0677 -0.0212 180 PHE A O 1198 C CB . PHE A 153 ? 0.3115 0.2509 0.2232 0.0630 -0.0765 -0.0338 180 PHE A CB 1199 C CG . PHE A 153 ? 0.3770 0.3040 0.2655 0.0671 -0.0777 -0.0261 180 PHE A CG 1200 C CD1 . PHE A 153 ? 0.3781 0.3004 0.2563 0.0781 -0.0871 -0.0298 180 PHE A CD1 1201 C CD2 . PHE A 153 ? 0.4004 0.3196 0.2785 0.0601 -0.0700 -0.0153 180 PHE A CD2 1202 C CE1 . PHE A 153 ? 0.4463 0.3546 0.3025 0.0820 -0.0882 -0.0208 180 PHE A CE1 1203 C CE2 . PHE A 153 ? 0.3701 0.2760 0.2295 0.0627 -0.0708 -0.0069 180 PHE A CE2 1204 C CZ . PHE A 153 ? 0.4396 0.3391 0.2871 0.0735 -0.0796 -0.0086 180 PHE A CZ 1205 N N . TYR A 154 ? 0.3723 0.3160 0.2753 0.0488 -0.0601 -0.0213 181 TYR A N 1206 C CA . TYR A 154 ? 0.3801 0.3227 0.2722 0.0434 -0.0527 -0.0136 181 TYR A CA 1207 C C . TYR A 154 ? 0.4107 0.3623 0.3059 0.0434 -0.0518 -0.0172 181 TYR A C 1208 O O . TYR A 154 ? 0.4035 0.3574 0.2872 0.0425 -0.0474 -0.0132 181 TYR A O 1209 C CB . TYR A 154 ? 0.2974 0.2365 0.1950 0.0352 -0.0465 -0.0084 181 TYR A CB 1210 C CG . TYR A 154 ? 0.3130 0.2419 0.2039 0.0358 -0.0476 -0.0043 181 TYR A CG 1211 C CD1 . TYR A 154 ? 0.3393 0.2597 0.2148 0.0353 -0.0456 0.0034 181 TYR A CD1 1212 C CD2 . TYR A 154 ? 0.3082 0.2361 0.2093 0.0371 -0.0507 -0.0083 181 TYR A CD2 1213 C CE1 . TYR A 154 ? 0.3740 0.2825 0.2448 0.0360 -0.0478 0.0073 181 TYR A CE1 1214 C CE2 . TYR A 154 ? 0.3761 0.2944 0.2719 0.0389 -0.0533 -0.0061 181 TYR A CE2 1215 C CZ . TYR A 154 ? 0.3901 0.2973 0.2709 0.0384 -0.0525 0.0017 181 TYR A CZ 1216 O OH . TYR A 154 ? 0.3908 0.2859 0.2677 0.0402 -0.0561 0.0041 181 TYR A OH 1217 N N . PHE A 155 ? 0.3639 0.3209 0.2762 0.0446 -0.0561 -0.0252 182 PHE A N 1218 C CA . PHE A 155 ? 0.2880 0.2524 0.2062 0.0458 -0.0575 -0.0304 182 PHE A CA 1219 C C . PHE A 155 ? 0.3125 0.2815 0.2387 0.0544 -0.0674 -0.0416 182 PHE A C 1220 O O . PHE A 155 ? 0.3820 0.3528 0.3299 0.0532 -0.0713 -0.0479 182 PHE A O 1221 C CB . PHE A 155 ? 0.2663 0.2312 0.2006 0.0384 -0.0536 -0.0291 182 PHE A CB 1222 C CG . PHE A 155 ? 0.3238 0.2852 0.2519 0.0315 -0.0454 -0.0204 182 PHE A CG 1223 C CD1 . PHE A 155 ? 0.3236 0.2868 0.2398 0.0297 -0.0409 -0.0167 182 PHE A CD1 1224 C CD2 . PHE A 155 ? 0.3119 0.2699 0.2472 0.0274 -0.0426 -0.0170 182 PHE A CD2 1225 C CE1 . PHE A 155 ? 0.2797 0.2403 0.1932 0.0238 -0.0348 -0.0107 182 PHE A CE1 1226 C CE2 . PHE A 155 ? 0.2581 0.2139 0.1882 0.0226 -0.0367 -0.0111 182 PHE A CE2 1227 C CZ . PHE A 155 ? 0.2445 0.2010 0.1645 0.0208 -0.0334 -0.0084 182 PHE A CZ 1228 N N . PRO A 156 ? 0.3758 0.3469 0.2849 0.0635 -0.0717 -0.0442 183 PRO A N 1229 C CA . PRO A 156 ? 0.4389 0.4146 0.3539 0.0740 -0.0831 -0.0566 183 PRO A CA 1230 C C . PRO A 156 ? 0.4030 0.3872 0.3317 0.0777 -0.0891 -0.0677 183 PRO A C 1231 O O . PRO A 156 ? 0.3944 0.3826 0.3355 0.0854 -0.0997 -0.0802 183 PRO A O 1232 C CB . PRO A 156 ? 0.4228 0.3981 0.3099 0.0837 -0.0849 -0.0539 183 PRO A CB 1233 C CG . PRO A 156 ? 0.4322 0.4058 0.3015 0.0775 -0.0735 -0.0411 183 PRO A CG 1234 C CD . PRO A 156 ? 0.4000 0.3682 0.2835 0.0647 -0.0662 -0.0348 183 PRO A CD 1235 N N . THR A 157 ? 0.4359 0.4227 0.3640 0.0729 -0.0835 -0.0646 184 THR A N 1236 C CA . THR A 157 ? 0.4143 0.4073 0.3578 0.0759 -0.0897 -0.0752 184 THR A CA 1237 C C . THR A 157 ? 0.3837 0.3733 0.3370 0.0657 -0.0826 -0.0688 184 THR A C 1238 O O . THR A 157 ? 0.3417 0.3280 0.2841 0.0586 -0.0729 -0.0575 184 THR A O 1239 C CB . THR A 157 ? 0.4366 0.4406 0.3625 0.0872 -0.0933 -0.0822 184 THR A CB 1240 O OG1 . THR A 157 ? 0.3968 0.4035 0.3040 0.0830 -0.0825 -0.0720 184 THR A OG1 1241 C CG2 . THR A 157 ? 0.4259 0.4331 0.3357 0.0991 -0.0998 -0.0869 184 THR A CG2 1242 N N . PRO A 158 ? 0.3679 0.3577 0.3429 0.0654 -0.0884 -0.0763 185 PRO A N 1243 C CA . PRO A 158 ? 0.3636 0.3493 0.3461 0.0576 -0.0830 -0.0702 185 PRO A CA 1244 C C . PRO A 158 ? 0.3883 0.3798 0.3507 0.0577 -0.0764 -0.0659 185 PRO A C 1245 O O . PRO A 158 ? 0.4163 0.4040 0.3761 0.0502 -0.0686 -0.0568 185 PRO A O 1246 C CB . PRO A 158 ? 0.3460 0.3316 0.3515 0.0612 -0.0933 -0.0816 185 PRO A CB 1247 C CG . PRO A 158 ? 0.3166 0.3029 0.3367 0.0658 -0.1022 -0.0908 185 PRO A CG 1248 C CD . PRO A 158 ? 0.3418 0.3338 0.3375 0.0722 -0.1010 -0.0906 185 PRO A CD 1249 N N . THR A 159 ? 0.3585 0.3604 0.3071 0.0665 -0.0793 -0.0728 186 THR A N 1250 C CA . THR A 159 ? 0.3980 0.4085 0.3294 0.0667 -0.0721 -0.0693 186 THR A CA 1251 C C . THR A 159 ? 0.3624 0.3689 0.2793 0.0588 -0.0607 -0.0554 186 THR A C 1252 O O . THR A 159 ? 0.4044 0.4124 0.3187 0.0529 -0.0535 -0.0499 186 THR A O 1253 C CB . THR A 159 ? 0.4322 0.4569 0.3495 0.0788 -0.0761 -0.0784 186 THR A CB 1254 O OG1 . THR A 159 ? 0.4673 0.4974 0.3994 0.0864 -0.0869 -0.0931 186 THR A OG1 1255 C CG2 . THR A 159 ? 0.3294 0.3648 0.2280 0.0776 -0.0656 -0.0722 186 THR A CG2 1256 N N . VAL A 160 ? 0.3634 0.3644 0.2723 0.0591 -0.0602 -0.0508 187 VAL A N 1257 C CA . VAL A 160 ? 0.3581 0.3532 0.2553 0.0521 -0.0511 -0.0384 187 VAL A CA 1258 C C . VAL A 160 ? 0.3772 0.3640 0.2869 0.0427 -0.0474 -0.0329 187 VAL A C 1259 O O . VAL A 160 ? 0.4047 0.3905 0.3096 0.0365 -0.0401 -0.0259 187 VAL A O 1260 C CB . VAL A 160 ? 0.3726 0.3622 0.2585 0.0561 -0.0530 -0.0354 187 VAL A CB 1261 C CG1 . VAL A 160 ? 0.3665 0.3476 0.2437 0.0486 -0.0450 -0.0231 187 VAL A CG1 1262 C CG2 . VAL A 160 ? 0.3364 0.3351 0.2049 0.0669 -0.0557 -0.0393 187 VAL A CG2 1263 N N . LEU A 161 ? 0.3318 0.3136 0.2582 0.0420 -0.0524 -0.0363 188 LEU A N 1264 C CA . LEU A 161 ? 0.3655 0.3410 0.3023 0.0345 -0.0485 -0.0308 188 LEU A CA 1265 C C . LEU A 161 ? 0.3380 0.3164 0.2753 0.0318 -0.0452 -0.0297 188 LEU A C 1266 O O . LEU A 161 ? 0.3299 0.3071 0.2618 0.0269 -0.0391 -0.0237 188 LEU A O 1267 C CB . LEU A 161 ? 0.3320 0.3037 0.2886 0.0341 -0.0534 -0.0342 188 LEU A CB 1268 C CG . LEU A 161 ? 0.3510 0.3177 0.3175 0.0277 -0.0489 -0.0277 188 LEU A CG 1269 C CD1 . LEU A 161 ? 0.3143 0.2786 0.2715 0.0233 -0.0417 -0.0197 188 LEU A CD1 1270 C CD2 . LEU A 161 ? 0.3154 0.2789 0.3031 0.0264 -0.0522 -0.0293 188 LEU A CD2 1271 N N . CYS A 162 ? 0.3028 0.2851 0.2478 0.0358 -0.0505 -0.0370 189 CYS A N 1272 C CA . CYS A 162 ? 0.3220 0.3060 0.2704 0.0345 -0.0496 -0.0374 189 CYS A CA 1273 C C . CYS A 162 ? 0.2829 0.2762 0.2188 0.0342 -0.0442 -0.0370 189 CYS A C 1274 O O . CYS A 162 ? 0.2877 0.2815 0.2239 0.0309 -0.0408 -0.0346 189 CYS A O 1275 C CB . CYS A 162 ? 0.3467 0.3314 0.3083 0.0398 -0.0583 -0.0465 189 CYS A CB 1276 S SG . CYS A 162 ? 0.3994 0.3731 0.3823 0.0383 -0.0640 -0.0464 189 CYS A SG 1277 N N . ASN A 163 ? 0.3002 0.3015 0.2254 0.0379 -0.0434 -0.0394 190 ASN A N 1278 C CA . ASN A 163 ? 0.3531 0.3653 0.2680 0.0371 -0.0369 -0.0384 190 ASN A CA 1279 C C . ASN A 163 ? 0.3848 0.3930 0.2922 0.0298 -0.0285 -0.0284 190 ASN A C 1280 O O . ASN A 163 ? 0.3800 0.3943 0.2867 0.0256 -0.0226 -0.0265 190 ASN A O 1281 C CB . ASN A 163 ? 0.3397 0.3638 0.2448 0.0450 -0.0382 -0.0441 190 ASN A CB 1282 C CG . ASN A 163 ? 0.3915 0.4230 0.3053 0.0533 -0.0471 -0.0568 190 ASN A CG 1283 O OD1 . ASN A 163 ? 0.4037 0.4275 0.3322 0.0530 -0.0534 -0.0604 190 ASN A OD1 1284 N ND2 . ASN A 163 ? 0.3451 0.3916 0.2499 0.0612 -0.0475 -0.0635 190 ASN A ND2 1285 N N . GLU A 164 ? 0.3444 0.3424 0.2484 0.0284 -0.0288 -0.0230 191 GLU A N 1286 C CA . GLU A 164 ? 0.3546 0.3474 0.2515 0.0226 -0.0224 -0.0142 191 GLU A CA 1287 C C . GLU A 164 ? 0.3315 0.3149 0.2356 0.0171 -0.0217 -0.0106 191 GLU A C 1288 O O . GLU A 164 ? 0.3653 0.3465 0.2680 0.0118 -0.0169 -0.0059 191 GLU A O 1289 C CB . GLU A 164 ? 0.3944 0.3829 0.2793 0.0260 -0.0231 -0.0104 191 GLU A CB 1290 C CG . GLU A 164 ? 0.4995 0.4990 0.3722 0.0318 -0.0215 -0.0119 191 GLU A CG 1291 C CD . GLU A 164 ? 0.6480 0.6422 0.5049 0.0360 -0.0217 -0.0062 191 GLU A CD 1292 O OE1 . GLU A 164 ? 0.6459 0.6282 0.5001 0.0315 -0.0197 0.0018 191 GLU A OE1 1293 O OE2 . GLU A 164 ? 0.7413 0.7433 0.5880 0.0450 -0.0247 -0.0104 191 GLU A OE2 1294 N N . ILE A 165 ? 0.3857 0.2652 0.1601 -0.0049 -0.0519 -0.0137 192 ILE A N 1295 C CA . ILE A 165 ? 0.3873 0.2638 0.1765 -0.0041 -0.0481 -0.0119 192 ILE A CA 1296 C C . ILE A 165 ? 0.3860 0.2822 0.1658 -0.0155 -0.0363 -0.0075 192 ILE A C 1297 O O . ILE A 165 ? 0.3975 0.2818 0.1670 -0.0223 -0.0357 -0.0054 192 ILE A O 1298 C CB . ILE A 165 ? 0.3818 0.2643 0.2121 0.0117 -0.0470 -0.0148 192 ILE A CB 1299 C CG1 . ILE A 165 ? 0.3643 0.2357 0.2041 0.0129 -0.0431 -0.0131 192 ILE A CG1 1300 C CG2 . ILE A 165 ? 0.3041 0.2212 0.1565 0.0167 -0.0366 -0.0150 192 ILE A CG2 1301 C CD1 . ILE A 165 ? 0.3404 0.2080 0.2196 0.0288 -0.0434 -0.0149 192 ILE A CD1 1302 N N . TRP A 166 ? 0.4139 0.3392 0.1982 -0.0177 -0.0277 -0.0062 193 TRP A N 1303 C CA . TRP A 166 ? 0.4054 0.3496 0.1816 -0.0294 -0.0187 -0.0012 193 TRP A CA 1304 C C . TRP A 166 ? 0.4089 0.3608 0.1623 -0.0411 -0.0162 0.0020 193 TRP A C 1305 O O . TRP A 166 ? 0.4041 0.3837 0.1692 -0.0445 -0.0073 0.0051 193 TRP A O 1306 C CB . TRP A 166 ? 0.3623 0.3365 0.1673 -0.0234 -0.0095 -0.0002 193 TRP A CB 1307 C CG . TRP A 166 ? 0.3046 0.2732 0.1324 -0.0118 -0.0091 -0.0018 193 TRP A CG 1308 C CD1 . TRP A 166 ? 0.2837 0.2631 0.1443 0.0027 -0.0073 -0.0038 193 TRP A CD1 1309 C CD2 . TRP A 166 ? 0.3442 0.2948 0.1652 -0.0134 -0.0092 -0.0015 193 TRP A CD2 1310 N NE1 . TRP A 166 ? 0.3564 0.3262 0.2317 0.0103 -0.0054 -0.0037 193 TRP A NE1 1311 C CE2 . TRP A 166 ? 0.3634 0.3150 0.2135 0.0009 -0.0060 -0.0028 193 TRP A CE2 1312 C CE3 . TRP A 166 ? 0.3545 0.2875 0.1484 -0.0253 -0.0113 -0.0005 193 TRP A CE3 1313 C CZ2 . TRP A 166 ? 0.3757 0.3113 0.2268 0.0039 -0.0031 -0.0032 193 TRP A CZ2 1314 C CZ3 . TRP A 166 ? 0.3498 0.2663 0.1444 -0.0224 -0.0096 -0.0020 193 TRP A CZ3 1315 C CH2 . TRP A 166 ? 0.3941 0.3119 0.2161 -0.0078 -0.0048 -0.0034 193 TRP A CH2 1316 N N . THR A 167 ? 0.3819 0.3129 0.1197 -0.0429 -0.0230 0.0017 194 THR A N 1317 C CA . THR A 167 ? 0.4521 0.3900 0.1822 -0.0494 -0.0191 0.0052 194 THR A CA 1318 C C . THR A 167 ? 0.4681 0.4337 0.2073 -0.0478 -0.0091 0.0054 194 THR A C 1319 O O . THR A 167 ? 0.4265 0.4094 0.1720 -0.0549 -0.0008 0.0103 194 THR A O 1320 C CB . THR A 167 ? 0.3879 0.3214 0.1126 -0.0613 -0.0178 0.0107 194 THR A CB 1321 O OG1 . THR A 167 ? 0.4816 0.4160 0.1954 -0.0672 -0.0149 0.0146 194 THR A OG1 1322 C CG2 . THR A 167 ? 0.3712 0.3254 0.1105 -0.0659 -0.0110 0.0132 194 THR A CG2 1323 N N . HIS A 168 ? 0.3949 0.3621 0.1346 -0.0388 -0.0107 -0.0003 195 HIS A N 1324 C CA . HIS A 168 ? 0.4284 0.4179 0.1737 -0.0367 -0.0014 -0.0018 195 HIS A CA 1325 C C . HIS A 168 ? 0.4249 0.4472 0.1962 -0.0378 0.0088 0.0004 195 HIS A C 1326 O O . HIS A 168 ? 0.3771 0.4209 0.1581 -0.0391 0.0187 0.0015 195 HIS A O 1327 C CB . HIS A 168 ? 0.4172 0.4053 0.1484 -0.0424 0.0041 0.0021 195 HIS A CB 1328 C CG . HIS A 168 ? 0.4358 0.3981 0.1442 -0.0405 -0.0051 0.0000 195 HIS A CG 1329 N ND1 . HIS A 168 ? 0.4468 0.3998 0.1456 -0.0318 -0.0108 -0.0074 195 HIS A ND1 1330 C CD2 . HIS A 168 ? 0.4233 0.3665 0.1176 -0.0467 -0.0107 0.0044 195 HIS A CD2 1331 C CE1 . HIS A 168 ? 0.4804 0.4103 0.1608 -0.0329 -0.0196 -0.0067 195 HIS A CE1 1332 N NE2 . HIS A 168 ? 0.4874 0.4113 0.1648 -0.0420 -0.0192 0.0007 195 HIS A NE2 1333 N N . SER A 169 ? 0.3685 0.3944 0.1554 -0.0359 0.0065 0.0014 196 SER A N 1334 C CA . SER A 169 ? 0.3540 0.4105 0.1734 -0.0325 0.0141 0.0036 196 SER A CA 1335 C C . SER A 169 ? 0.3754 0.4452 0.2208 -0.0188 0.0162 -0.0023 196 SER A C 1336 O O . SER A 169 ? 0.3796 0.4780 0.2476 -0.0179 0.0249 -0.0006 196 SER A O 1337 C CB . SER A 169 ? 0.3989 0.4510 0.2299 -0.0295 0.0109 0.0052 196 SER A CB 1338 O OG . SER A 169 ? 0.5631 0.6101 0.3746 -0.0431 0.0107 0.0105 196 SER A OG 1339 N N . TYR A 170 ? 0.3100 0.3581 0.1538 -0.0083 0.0071 -0.0092 197 TYR A N 1340 C CA . TYR A 170 ? 0.2791 0.3346 0.1440 0.0044 0.0066 -0.0164 197 TYR A CA 1341 C C . TYR A 170 ? 0.3513 0.3895 0.1865 0.0036 0.0029 -0.0221 197 TYR A C 1342 O O . TYR A 170 ? 0.3330 0.3451 0.1344 -0.0028 -0.0040 -0.0212 197 TYR A O 1343 C CB . TYR A 170 ? 0.2914 0.3353 0.1813 0.0185 -0.0026 -0.0205 197 TYR A CB 1344 C CG . TYR A 170 ? 0.2859 0.3439 0.2055 0.0223 0.0015 -0.0153 197 TYR A CG 1345 C CD1 . TYR A 170 ? 0.2328 0.3230 0.1842 0.0257 0.0108 -0.0122 197 TYR A CD1 1346 C CD2 . TYR A 170 ? 0.2894 0.3273 0.2057 0.0233 -0.0037 -0.0133 197 TYR A CD2 1347 C CE1 . TYR A 170 ? 0.2873 0.3894 0.2630 0.0295 0.0145 -0.0065 197 TYR A CE1 1348 C CE2 . TYR A 170 ? 0.3378 0.3869 0.2778 0.0275 0.0015 -0.0087 197 TYR A CE2 1349 C CZ . TYR A 170 ? 0.3608 0.4418 0.3289 0.0305 0.0104 -0.0050 197 TYR A CZ 1350 O OH . TYR A 170 ? 0.3352 0.4265 0.3235 0.0346 0.0157 0.0007 197 TYR A OH 1351 N N . LYS A 171 ? 0.3524 0.4046 0.1997 0.0102 0.0077 -0.0280 198 LYS A N 1352 C CA . LYS A 171 ? 0.3944 0.4267 0.2176 0.0146 0.0017 -0.0363 198 LYS A CA 1353 C C . LYS A 171 ? 0.4060 0.4425 0.2624 0.0305 -0.0040 -0.0454 198 LYS A C 1354 O O . LYS A 171 ? 0.3910 0.4525 0.2726 0.0351 0.0054 -0.0483 198 LYS A O 1355 C CB . LYS A 171 ? 0.4037 0.4462 0.2039 0.0065 0.0147 -0.0359 198 LYS A CB 1356 C CG . LYS A 171 ? 0.4591 0.4782 0.2262 0.0105 0.0093 -0.0446 198 LYS A CG 1357 C CD . LYS A 171 ? 0.5994 0.6285 0.3429 0.0027 0.0254 -0.0436 198 LYS A CD 1358 C CE . LYS A 171 ? 0.7607 0.7647 0.4662 0.0072 0.0207 -0.0528 198 LYS A CE 1359 N NZ . LYS A 171 ? 0.8676 0.8356 0.5375 0.0043 0.0038 -0.0510 198 LYS A NZ 1360 N N . VAL A 172 ? 0.4097 0.4219 0.2700 0.0390 -0.0198 -0.0495 199 VAL A N 1361 C CA . VAL A 172 ? 0.3815 0.3963 0.2784 0.0543 -0.0271 -0.0575 199 VAL A CA 1362 C C . VAL A 172 ? 0.3667 0.3894 0.2612 0.0592 -0.0232 -0.0672 199 VAL A C 1363 O O . VAL A 172 ? 0.3682 0.3744 0.2217 0.0549 -0.0245 -0.0717 199 VAL A O 1364 C CB . VAL A 172 ? 0.4254 0.4083 0.3236 0.0622 -0.0467 -0.0610 199 VAL A CB 1365 C CG1 . VAL A 172 ? 0.4403 0.3910 0.2895 0.0576 -0.0581 -0.0650 199 VAL A CG1 1366 C CG2 . VAL A 172 ? 0.4086 0.3963 0.3505 0.0780 -0.0541 -0.0685 199 VAL A CG2 1367 N N . SER A 173 ? 0.3824 0.4301 0.3209 0.0683 -0.0177 -0.0702 200 SER A N 1368 C CA . SER A 173 ? 0.3781 0.4374 0.3219 0.0735 -0.0116 -0.0798 200 SER A CA 1369 C C . SER A 173 ? 0.4990 0.5379 0.4510 0.0869 -0.0281 -0.0926 200 SER A C 1370 O O . SER A 173 ? 0.4946 0.5221 0.4714 0.0949 -0.0420 -0.0925 200 SER A O 1371 C CB . SER A 173 ? 0.3396 0.4378 0.3305 0.0760 0.0028 -0.0757 200 SER A CB 1372 O OG . SER A 173 ? 0.4585 0.5685 0.4604 0.0820 0.0091 -0.0856 200 SER A OG 1373 N N . ASN A 174 ? 0.5838 0.6175 0.5156 0.0895 -0.0265 -0.1038 201 ASN A N 1374 C CA . ASN A 174 ? 0.6327 0.6491 0.5743 0.1025 -0.0423 -0.1177 201 ASN A CA 1375 C C . ASN A 174 ? 0.5113 0.5548 0.5150 0.1139 -0.0386 -0.1213 201 ASN A C 1376 O O . ASN A 174 ? 0.5699 0.6024 0.5967 0.1260 -0.0531 -0.1313 201 ASN A O 1377 C CB . ASN A 174 ? 0.7826 0.7803 0.6750 0.1015 -0.0422 -0.1296 201 ASN A CB 1378 C CG . ASN A 174 ? 0.9403 0.9652 0.8365 0.0995 -0.0197 -0.1328 201 ASN A CG 1379 O OD1 . ASN A 174 ? 0.9367 0.9872 0.8408 0.0905 -0.0016 -0.1219 201 ASN A OD1 1380 N ND2 . ASN A 174 ? 1.0843 1.1028 0.9761 0.1080 -0.0210 -0.1481 201 ASN A ND2 1381 N N . TYR A 175 ? 0.3586 0.3826 0.5206 0.0169 -0.0341 -0.1931 202 TYR A N 1382 C CA . TYR A 175 ? 0.4111 0.4268 0.6141 0.0143 -0.0358 -0.1936 202 TYR A CA 1383 C C . TYR A 175 ? 0.4051 0.4056 0.6069 0.0096 -0.0342 -0.1816 202 TYR A C 1384 O O . TYR A 175 ? 0.4429 0.4348 0.6042 0.0076 -0.0309 -0.1700 202 TYR A O 1385 C CB . TYR A 175 ? 0.4438 0.4488 0.6482 0.0125 -0.0338 -0.1865 202 TYR A CB 1386 C CG . TYR A 175 ? 0.4950 0.5147 0.7110 0.0167 -0.0360 -0.1993 202 TYR A CG 1387 C CD1 . TYR A 175 ? 0.5423 0.5763 0.8071 0.0202 -0.0420 -0.2161 202 TYR A CD1 1388 C CD2 . TYR A 175 ? 0.5860 0.6058 0.7667 0.0173 -0.0325 -0.1948 202 TYR A CD2 1389 C CE1 . TYR A 175 ? 0.5915 0.6400 0.8664 0.0244 -0.0447 -0.2287 202 TYR A CE1 1390 C CE2 . TYR A 175 ? 0.6622 0.6956 0.8533 0.0210 -0.0342 -0.2062 202 TYR A CE2 1391 C CZ . TYR A 175 ? 0.6950 0.7430 0.9319 0.0247 -0.0405 -0.2235 202 TYR A CZ 1392 O OH . TYR A 175 ? 0.7587 0.8213 1.0050 0.0289 -0.0428 -0.2357 202 TYR A OH 1393 N N . SER A 176 ? 0.4158 0.4131 0.6646 0.0080 -0.0365 -0.1835 203 SER A N 1394 C CA . SER A 176 ? 0.4518 0.4380 0.7143 0.0037 -0.0355 -0.1737 203 SER A CA 1395 C C . SER A 176 ? 0.4452 0.4197 0.7453 0.0007 -0.0345 -0.1622 203 SER A C 1396 O O . SER A 176 ? 0.4859 0.4606 0.8038 0.0019 -0.0352 -0.1633 203 SER A O 1397 C CB . SER A 176 ? 0.4878 0.4866 0.7967 0.0054 -0.0398 -0.1867 203 SER A CB 1398 O OG . SER A 176 ? 0.4352 0.4505 0.7240 0.0100 -0.0422 -0.2002 203 SER A OG 1399 N N . ARG A 177 ? 0.4237 0.3882 0.7377 -0.0030 -0.0325 -0.1490 204 ARG A N 1400 C CA . ARG A 177 ? 0.3890 0.3421 0.7446 -0.0057 -0.0306 -0.1305 204 ARG A CA 1401 C C . ARG A 177 ? 0.3872 0.3474 0.8072 -0.0044 -0.0333 -0.1345 204 ARG A C 1402 O O . ARG A 177 ? 0.3831 0.3552 0.8367 -0.0027 -0.0371 -0.1486 204 ARG A O 1403 C CB . ARG A 177 ? 0.3220 0.2673 0.6968 -0.0097 -0.0277 -0.1123 204 ARG A CB 1404 C CG . ARG A 177 ? 0.3753 0.3108 0.6942 -0.0108 -0.0255 -0.1039 204 ARG A CG 1405 C CD . ARG A 177 ? 0.3909 0.3198 0.7352 -0.0149 -0.0222 -0.0810 204 ARG A CD 1406 N NE . ARG A 177 ? 0.4051 0.3230 0.7012 -0.0143 -0.0207 -0.0688 204 ARG A NE 1407 C CZ . ARG A 177 ? 0.4023 0.3305 0.6919 -0.0123 -0.0149 -0.0328 204 ARG A CZ 1408 N NH1 . ARG A 177 ? 0.4084 0.3397 0.7582 -0.0154 -0.0102 -0.0098 204 ARG A NH1 1409 N NH2 . ARG A 177 ? 0.3236 0.2602 0.5476 -0.0063 -0.0139 -0.0195 204 ARG A NH2 1410 N N . GLY A 178 ? 0.3810 0.3345 0.8189 -0.0045 -0.0321 -0.1222 205 GLY A N 1411 C CA . GLY A 178 ? 0.3872 0.3471 0.8851 -0.0030 -0.0352 -0.1248 205 GLY A CA 1412 C C . GLY A 178 ? 0.3643 0.3338 0.8497 0.0008 -0.0394 -0.1457 205 GLY A C 1413 O O . GLY A 178 ? 0.3957 0.3695 0.9234 0.0023 -0.0424 -0.1483 205 GLY A O 1414 N N . SER A 179 ? 0.3343 0.3082 0.7620 0.0026 -0.0392 -0.1586 206 SER A N 1415 C CA . SER A 179 ? 0.2880 0.2725 0.7003 0.0064 -0.0419 -0.1747 206 SER A CA 1416 C C . SER A 179 ? 0.3554 0.3321 0.7604 0.0063 -0.0402 -0.1665 206 SER A C 1417 O O . SER A 179 ? 0.4037 0.3889 0.8204 0.0091 -0.0432 -0.1775 206 SER A O 1418 C CB . SER A 179 ? 0.2895 0.2795 0.6396 0.0081 -0.0403 -0.1825 206 SER A CB 1419 O OG . SER A 179 ? 0.3426 0.3201 0.6390 0.0060 -0.0350 -0.1690 206 SER A OG 1420 N N . GLY A 180 ? 0.3644 0.3258 0.7512 0.0035 -0.0358 -0.1475 207 GLY A N 1421 C CA . GLY A 180 ? 0.2638 0.2174 0.6370 0.0040 -0.0339 -0.1389 207 GLY A CA 1422 C C . GLY A 180 ? 0.3531 0.3077 0.6628 0.0055 -0.0316 -0.1450 207 GLY A C 1423 O O . GLY A 180 ? 0.3422 0.2928 0.6367 0.0065 -0.0303 -0.1415 207 GLY A O 1424 N N . ARG A 181 ? 0.3604 0.3208 0.6341 0.0056 -0.0308 -0.1521 208 ARG A N 1425 C CA . ARG A 181 ? 0.3906 0.3536 0.6081 0.0069 -0.0280 -0.1544 208 ARG A CA 1426 C C . ARG A 181 ? 0.3469 0.3034 0.5133 0.0053 -0.0246 -0.1455 208 ARG A C 1427 O O . ARG A 181 ? 0.3381 0.3029 0.4728 0.0069 -0.0232 -0.1489 208 ARG A O 1428 C CB . ARG A 181 ? 0.4739 0.4571 0.7045 0.0106 -0.0311 -0.1733 208 ARG A CB 1429 C CG . ARG A 181 ? 0.5552 0.5457 0.8305 0.0127 -0.0351 -0.1831 208 ARG A CG 1430 C CD . ARG A 181 ? 0.6804 0.6931 0.9616 0.0175 -0.0384 -0.2026 208 ARG A CD 1431 N NE . ARG A 181 ? 0.7672 0.7884 1.0928 0.0200 -0.0433 -0.2137 208 ARG A NE 1432 C CZ . ARG A 181 ? 0.8089 0.8495 1.1450 0.0248 -0.0471 -0.2310 208 ARG A CZ 1433 N NH1 . ARG A 181 ? 0.7997 0.8528 1.1051 0.0275 -0.0459 -0.2376 208 ARG A NH1 1434 N NH2 . ARG A 181 ? 0.8606 0.9084 1.2386 0.0271 -0.0525 -0.2410 208 ARG A NH2 1435 N N . CYS A 182 ? 0.2708 0.2193 0.4459 0.0033 -0.0247 -0.1378 209 CYS A N 1436 C CA . CYS A 182 ? 0.3340 0.2763 0.4611 0.0022 -0.0223 -0.1292 209 CYS A CA 1437 C C . CYS A 182 ? 0.3177 0.2470 0.4529 0.0014 -0.0223 -0.1169 209 CYS A C 1438 O O . CYS A 182 ? 0.3488 0.2731 0.5344 0.0008 -0.0235 -0.1112 209 CYS A O 1439 C CB . CYS A 182 ? 0.2627 0.2121 0.3811 0.0018 -0.0230 -0.1343 209 CYS A CB 1440 S SG . CYS A 182 ? 0.3080 0.2607 0.4890 0.0004 -0.0266 -0.1399 209 CYS A SG 1441 N N . ILE A 183 ? 0.3386 0.2622 0.4265 0.0021 -0.0207 -0.1094 210 ILE A N 1442 C CA . ILE A 183 ? 0.3483 0.2593 0.4398 0.0040 -0.0220 -0.0978 210 ILE A CA 1443 C C . ILE A 183 ? 0.3803 0.2885 0.4798 0.0030 -0.0234 -0.0944 210 ILE A C 1444 O O . ILE A 183 ? 0.3481 0.2649 0.4121 0.0016 -0.0231 -0.1004 210 ILE A O 1445 C CB . ILE A 183 ? 0.3206 0.2298 0.3591 0.0070 -0.0214 -0.0932 210 ILE A CB 1446 C CG1 . ILE A 183 ? 0.3535 0.2629 0.3946 0.0079 -0.0198 -0.0940 210 ILE A CG1 1447 C CG2 . ILE A 183 ? 0.2773 0.1808 0.3074 0.0131 -0.0246 -0.0754 210 ILE A CG2 1448 C CD1 . ILE A 183 ? 0.3317 0.2298 0.4179 0.0122 -0.0221 -0.0855 210 ILE A CD1 1449 N N . GLN A 184 ? 0.4201 0.3222 0.5638 0.0038 -0.0224 -0.0734 211 GLN A N 1450 C CA . GLN A 184 ? 0.4227 0.3329 0.5725 0.0030 -0.0204 -0.0549 211 GLN A CA 1451 C C . GLN A 184 ? 0.3486 0.2693 0.4483 0.0094 -0.0190 -0.0289 211 GLN A C 1452 O O . GLN A 184 ? 0.3827 0.3044 0.4686 0.0153 -0.0183 -0.0129 211 GLN A O 1453 C CB . GLN A 184 ? 0.4622 0.3709 0.6804 0.0013 -0.0169 -0.0332 211 GLN A CB 1454 C CG . GLN A 184 ? 0.5237 0.4283 0.7960 -0.0055 -0.0187 -0.0516 211 GLN A CG 1455 C CD . GLN A 184 ? 0.4898 0.3958 0.8296 -0.0068 -0.0153 -0.0298 211 GLN A CD 1456 O OE1 . GLN A 184 ? 0.5939 0.5042 0.9571 -0.0064 -0.0167 -0.0381 211 GLN A OE1 1457 N NE2 . GLN A 184 ? 0.3792 0.2876 0.7456 -0.0073 -0.0101 0.0010 211 GLN A NE2 1458 N N . MET A 185 ? 0.3603 0.2902 0.4362 0.0093 -0.0193 -0.0252 212 MET A N 1459 C CA . MET A 185 ? 0.4320 0.3741 0.4573 0.0165 -0.0197 -0.0049 212 MET A CA 1460 C C . MET A 185 ? 0.4235 0.3778 0.4743 0.0217 -0.0145 0.0334 212 MET A C 1461 O O . MET A 185 ? 0.3723 0.3399 0.3873 0.0305 -0.0147 0.0544 212 MET A O 1462 C CB . MET A 185 ? 0.4810 0.4280 0.4674 0.0146 -0.0229 -0.0208 212 MET A CB 1463 C CG . MET A 185 ? 0.6353 0.5886 0.5551 0.0210 -0.0271 -0.0187 212 MET A CG 1464 S SD . MET A 185 ? 0.5825 0.5398 0.4607 0.0188 -0.0313 -0.0387 212 MET A SD 1465 C CE . MET A 185 ? 0.2846 0.2362 0.1902 0.0063 -0.0256 -0.0669 212 MET A CE 1466 N N . TRP A 186 ? 0.3325 0.2836 0.4470 0.0172 -0.0100 0.0424 213 TRP A N 1467 C CA . TRP A 186 ? 0.2986 0.2617 0.4454 0.0216 -0.0034 0.0805 213 TRP A CA 1468 C C . TRP A 186 ? 0.3579 0.3105 0.5812 0.0152 0.0003 0.0841 213 TRP A C 1469 O O . TRP A 186 ? 0.3586 0.2977 0.6087 0.0070 -0.0033 0.0539 213 TRP A O 1470 C CB . TRP A 186 ? 0.3262 0.3043 0.4613 0.0213 -0.0017 0.0894 213 TRP A CB 1471 C CG . TRP A 186 ? 0.3450 0.3426 0.4895 0.0298 0.0053 0.1320 213 TRP A CG 1472 C CD1 . TRP A 186 ? 0.3788 0.3824 0.5830 0.0274 0.0133 0.1574 213 TRP A CD1 1473 C CD2 . TRP A 186 ? 0.3609 0.3768 0.4547 0.0433 0.0049 0.1543 213 TRP A CD2 1474 N NE1 . TRP A 186 ? 0.3338 0.3599 0.5250 0.0387 0.0192 0.1949 213 TRP A NE1 1475 C CE2 . TRP A 186 ? 0.3595 0.3956 0.4799 0.0468 0.0138 0.1839 213 TRP A CE2 1476 C CE3 . TRP A 186 ? 0.3598 0.3792 0.3884 0.0511 -0.0022 0.1439 213 TRP A CE3 1477 C CZ2 . TRP A 186 ? 0.3299 0.3895 0.4122 0.0539 0.0159 0.1858 213 TRP A CZ2 1478 C CZ3 . TRP A 186 ? 0.3100 0.3466 0.3082 0.0545 -0.0007 0.1411 213 TRP A CZ3 1479 C CH2 . TRP A 186 ? 0.2982 0.3546 0.3233 0.0571 0.0080 0.1621 213 TRP A CH2 1480 N N . PHE A 187 ? 0.3503 0.3102 0.6098 0.0200 0.0071 0.1209 214 PHE A N 1481 C CA . PHE A 187 ? 0.3152 0.2647 0.6517 0.0146 0.0107 0.1287 214 PHE A CA 1482 C C . PHE A 187 ? 0.3770 0.3474 0.7360 0.0202 0.0199 0.1698 214 PHE A C 1483 O O . PHE A 187 ? 0.4050 0.3951 0.7185 0.0298 0.0228 0.1899 214 PHE A O 1484 C CB . PHE A 187 ? 0.3095 0.2423 0.6575 0.0143 0.0066 0.1112 214 PHE A CB 1485 C CG . PHE A 187 ? 0.2885 0.2269 0.5974 0.0256 0.0070 0.1287 214 PHE A CG 1486 C CD1 . PHE A 187 ? 0.3083 0.2614 0.6360 0.0293 0.0128 0.1529 214 PHE A CD1 1487 C CD2 . PHE A 187 ? 0.3276 0.2677 0.5695 0.0299 0.0017 0.1118 214 PHE A CD2 1488 C CE1 . PHE A 187 ? 0.3404 0.3014 0.6285 0.0391 0.0127 0.1628 214 PHE A CE1 1489 C CE2 . PHE A 187 ? 0.2992 0.2447 0.5089 0.0409 0.0009 0.1263 214 PHE A CE2 1490 C CZ . PHE A 187 ? 0.3073 0.2636 0.5385 0.0452 0.0063 0.1498 214 PHE A CZ 1491 N N . ASP A 188 ? 0.3556 0.3292 0.7796 0.0142 0.0237 0.1745 215 ASP A N 1492 C CA . ASP A 188 ? 0.3168 0.3141 0.7666 0.0188 0.0327 0.2077 215 ASP A CA 1493 C C . ASP A 188 ? 0.3988 0.3943 0.8512 0.0229 0.0328 0.2112 215 ASP A C 1494 O O . ASP A 188 ? 0.3826 0.3657 0.8775 0.0173 0.0294 0.1961 215 ASP A O 1495 C CB . ASP A 188 ? 0.3612 0.3633 0.8842 0.0117 0.0358 0.2111 215 ASP A CB 1496 C CG . ASP A 188 ? 0.4145 0.4424 0.9691 0.0172 0.0459 0.2470 215 ASP A CG 1497 O OD1 . ASP A 188 ? 0.4060 0.4479 0.9281 0.0260 0.0507 0.2661 215 ASP A OD1 1498 O OD2 . ASP A 188 ? 0.4777 0.5125 1.0910 0.0137 0.0488 0.2540 215 ASP A OD2 1499 N N . PRO A 189 ? 0.4179 0.4926 0.8577 0.0616 0.0339 0.2366 216 PRO A N 1500 C CA . PRO A 189 ? 0.3731 0.4398 0.7828 0.0766 0.0368 0.2235 216 PRO A CA 1501 C C . PRO A 189 ? 0.4144 0.4703 0.8363 0.0797 0.0317 0.2345 216 PRO A C 1502 O O . PRO A 189 ? 0.4105 0.4520 0.8099 0.0918 0.0275 0.2211 216 PRO A O 1503 C CB . PRO A 189 ? 0.3351 0.4276 0.7216 0.0873 0.0576 0.2268 216 PRO A CB 1504 C CG . PRO A 189 ? 0.3809 0.4936 0.7919 0.0790 0.0672 0.2507 216 PRO A CG 1505 C CD . PRO A 189 ? 0.3865 0.4898 0.8245 0.0639 0.0528 0.2504 216 PRO A CD 1506 N N . ALA A 190 ? 0.4729 0.5369 0.9305 0.0699 0.0319 0.2587 217 ALA A N 1507 C CA . ALA A 190 ? 0.5251 0.5744 0.9954 0.0715 0.0262 0.2706 217 ALA A CA 1508 C C . ALA A 190 ? 0.5668 0.5750 1.0326 0.0671 0.0033 0.2545 217 ALA A C 1509 O O . ALA A 190 ? 0.5547 0.5388 1.0121 0.0740 -0.0029 0.2549 217 ALA A O 1510 C CB . ALA A 190 ? 0.4969 0.5659 1.0117 0.0604 0.0299 0.3001 217 ALA A CB 1511 N N . GLN A 191 ? 0.5454 0.5438 1.0135 0.0569 -0.0090 0.2400 218 GLN A N 1512 C CA . GLN A 191 ? 0.5966 0.5562 1.0574 0.0527 -0.0309 0.2224 218 GLN A CA 1513 C C . GLN A 191 ? 0.5936 0.5425 1.0156 0.0662 -0.0320 0.1945 218 GLN A C 1514 O O . GLN A 191 ? 0.6493 0.5730 1.0628 0.0627 -0.0481 0.1762 218 GLN A O 1515 C CB . GLN A 191 ? 0.6102 0.5660 1.1002 0.0330 -0.0465 0.2240 218 GLN A CB 1516 C CG . GLN A 191 ? 0.6766 0.6579 1.2116 0.0202 -0.0435 0.2524 218 GLN A CG 1517 C CD . GLN A 191 ? 0.7723 0.7403 1.3233 0.0185 -0.0466 0.2697 218 GLN A CD 1518 O OE1 . GLN A 191 ? 0.8409 0.7713 1.3716 0.0231 -0.0570 0.2590 218 GLN A OE1 1519 N NE2 . GLN A 191 ? 0.7742 0.7726 1.3606 0.0133 -0.0370 0.2971 218 GLN A NE2 1520 N N . GLY A 192 ? 0.5055 0.4762 0.9048 0.0819 -0.0152 0.1910 219 GLY A N 1521 C CA . GLY A 192 ? 0.4980 0.4688 0.8658 0.0953 -0.0145 0.1656 219 GLY A CA 1522 C C . GLY A 192 ? 0.4805 0.4651 0.8448 0.0890 -0.0102 0.1551 219 GLY A C 1523 O O . GLY A 192 ? 0.5112 0.5019 0.8956 0.0747 -0.0100 0.1665 219 GLY A O 1524 N N . ASN A 193 ? 0.4587 0.4502 0.7981 0.1007 -0.0064 0.1334 220 ASN A N 1525 C CA . ASN A 193 ? 0.3938 0.3943 0.7266 0.0963 -0.0021 0.1210 220 ASN A CA 1526 C C . ASN A 193 ? 0.3811 0.3556 0.7090 0.0935 -0.0186 0.1002 220 ASN A C 1527 O O . ASN A 193 ? 0.3937 0.3659 0.7053 0.1057 -0.0212 0.0802 220 ASN A O 1528 C CB . ASN A 193 ? 0.3762 0.4070 0.6871 0.1092 0.0154 0.1096 220 ASN A CB 1529 C CG . ASN A 193 ? 0.4301 0.4700 0.7342 0.1040 0.0235 0.0993 220 ASN A CG 1530 O OD1 . ASN A 193 ? 0.3803 0.4013 0.6898 0.0960 0.0138 0.0916 220 ASN A OD1 1531 N ND2 . ASN A 193 ? 0.4136 0.4800 0.7026 0.1086 0.0409 0.0982 220 ASN A ND2 1532 N N . PRO A 194 ? 0.3835 0.3414 0.7249 0.0781 -0.0298 0.1036 221 PRO A N 1533 C CA . PRO A 194 ? 0.4035 0.3331 0.7381 0.0739 -0.0481 0.0843 221 PRO A CA 1534 C C . PRO A 194 ? 0.4156 0.3491 0.7301 0.0810 -0.0435 0.0599 221 PRO A C 1535 O O . PRO A 194 ? 0.3844 0.2983 0.6821 0.0813 -0.0563 0.0384 221 PRO A O 1536 C CB . PRO A 194 ? 0.3834 0.3056 0.7384 0.0559 -0.0578 0.0964 221 PRO A CB 1537 C CG . PRO A 194 ? 0.3417 0.2933 0.7077 0.0537 -0.0398 0.1158 221 PRO A CG 1538 C CD . PRO A 194 ? 0.3638 0.3330 0.7263 0.0649 -0.0256 0.1248 221 PRO A CD 1539 N N . ASN A 195 ? 0.3829 0.3442 0.6862 0.0823 -0.0235 0.0593 222 ASN A N 1540 C CA . ASN A 195 ? 0.3068 0.2756 0.5750 0.0792 -0.0154 0.0330 222 ASN A CA 1541 C C . ASN A 195 ? 0.3114 0.2970 0.5548 0.0898 -0.0093 0.0110 222 ASN A C 1542 O O . ASN A 195 ? 0.3121 0.3033 0.5273 0.0863 -0.0049 -0.0124 222 ASN A O 1543 C CB . ASN A 195 ? 0.3001 0.2861 0.5608 0.0737 0.0027 0.0386 222 ASN A CB 1544 C CG . ASN A 195 ? 0.3479 0.3193 0.6264 0.0644 -0.0036 0.0554 222 ASN A CG 1545 O OD1 . ASN A 195 ? 0.3906 0.3386 0.6734 0.0579 -0.0207 0.0514 222 ASN A OD1 1546 N ND2 . ASN A 195 ? 0.2608 0.2481 0.5490 0.0655 0.0099 0.0740 222 ASN A ND2 1547 N N . GLU A 196 ? 0.2995 0.2948 0.5535 0.1030 -0.0087 0.0195 223 GLU A N 1548 C CA . GLU A 196 ? 0.3719 0.3869 0.6045 0.1162 -0.0045 -0.0002 223 GLU A CA 1549 C C . GLU A 196 ? 0.4233 0.4191 0.6385 0.1188 -0.0194 -0.0228 223 GLU A C 1550 O O . GLU A 196 ? 0.4225 0.4381 0.6118 0.1216 -0.0134 -0.0466 223 GLU A O 1551 C CB . GLU A 196 ? 0.3863 0.4115 0.6334 0.1328 -0.0026 0.0159 223 GLU A CB 1552 C CG . GLU A 196 ? 0.5134 0.5681 0.7694 0.1354 0.0155 0.0332 223 GLU A CG 1553 C CD . GLU A 196 ? 0.5439 0.6037 0.8087 0.1493 0.0159 0.0518 223 GLU A CD 1554 O OE1 . GLU A 196 ? 0.5811 0.6252 0.8430 0.1602 0.0045 0.0484 223 GLU A OE1 1555 O OE2 . GLU A 196 ? 0.4884 0.5639 0.7529 0.1466 0.0266 0.0672 223 GLU A OE2 1556 N N . GLU A 197 ? 0.4240 0.3824 0.6534 0.1177 -0.0392 -0.0156 224 GLU A N 1557 C CA . GLU A 197 ? 0.4470 0.3824 0.6583 0.1216 -0.0553 -0.0369 224 GLU A CA 1558 C C . GLU A 197 ? 0.4070 0.3392 0.5997 0.1084 -0.0551 -0.0532 224 GLU A C 1559 O O . GLU A 197 ? 0.4274 0.3588 0.5946 0.1130 -0.0592 -0.0765 224 GLU A O 1560 C CB . GLU A 197 ? 0.5512 0.4431 0.7818 0.1232 -0.0780 -0.0254 224 GLU A CB 1561 C CG . GLU A 197 ? 0.6916 0.5555 0.9007 0.1298 -0.0965 -0.0485 224 GLU A CG 1562 C CD . GLU A 197 ? 0.8074 0.6944 0.9866 0.1488 -0.0898 -0.0713 224 GLU A CD 1563 O OE1 . GLU A 197 ? 0.7850 0.6891 0.9668 0.1634 -0.0821 -0.0650 224 GLU A OE1 1564 O OE2 . GLU A 197 ? 0.8220 0.7129 0.9751 0.1500 -0.0917 -0.0951 224 GLU A OE2 1565 N N . VAL A 198 ? 0.3155 0.2462 0.5197 0.0937 -0.0497 -0.0399 225 VAL A N 1566 C CA . VAL A 198 ? 0.3410 0.2681 0.5255 0.0820 -0.0470 -0.0525 225 VAL A CA 1567 C C . VAL A 198 ? 0.3706 0.3294 0.5258 0.0815 -0.0273 -0.0715 225 VAL A C 1568 O O . VAL A 198 ? 0.3793 0.3368 0.5086 0.0787 -0.0274 -0.0914 225 VAL A O 1569 C CB . VAL A 198 ? 0.3586 0.2791 0.5607 0.0692 -0.0441 -0.0324 225 VAL A CB 1570 C CG1 . VAL A 198 ? 0.3050 0.2176 0.4829 0.0595 -0.0416 -0.0450 225 VAL A CG1 1571 C CG2 . VAL A 198 ? 0.3490 0.2442 0.5848 0.0670 -0.0636 -0.0126 225 VAL A CG2 1572 N N . ALA A 199 ? 0.3595 0.3478 0.5186 0.0838 -0.0105 -0.0652 226 ALA A N 1573 C CA . ALA A 199 ? 0.3152 0.3365 0.4495 0.0818 0.0072 -0.0835 226 ALA A CA 1574 C C . ALA A 199 ? 0.3458 0.3810 0.4639 0.0935 0.0023 -0.1052 226 ALA A C 1575 O O . ALA A 199 ? 0.3373 0.3862 0.4308 0.0883 0.0087 -0.1254 226 ALA A O 1576 C CB . ALA A 199 ? 0.2771 0.3275 0.4200 0.0842 0.0233 -0.0731 226 ALA A CB 1577 N N . ARG A 200 ? 0.2933 0.3247 0.4242 0.1102 -0.0087 -0.1000 227 ARG A N 1578 C CA . ARG A 200 ? 0.3075 0.3510 0.4224 0.1259 -0.0143 -0.1194 227 ARG A CA 1579 C C . ARG A 200 ? 0.3826 0.4036 0.4786 0.1235 -0.0260 -0.1359 227 ARG A C 1580 O O . ARG A 200 ? 0.4221 0.4652 0.4950 0.1283 -0.0219 -0.1574 227 ARG A O 1581 C CB . ARG A 200 ? 0.3743 0.4057 0.5045 0.1455 -0.0261 -0.1083 227 ARG A CB 1582 N N . PHE A 201 ? 0.3734 0.3535 0.4797 0.1163 -0.0405 -0.1258 228 PHE A N 1583 C CA . PHE A 201 ? 0.4033 0.3590 0.4914 0.1152 -0.0535 -0.1404 228 PHE A CA 1584 C C . PHE A 201 ? 0.3855 0.3612 0.4475 0.1032 -0.0385 -0.1555 228 PHE A C 1585 O O . PHE A 201 ? 0.3940 0.3782 0.4316 0.1094 -0.0395 -0.1755 228 PHE A O 1586 C CB . PHE A 201 ? 0.3850 0.2977 0.4912 0.1071 -0.0712 -0.1256 228 PHE A CB 1587 C CG . PHE A 201 ? 0.4204 0.3088 0.5066 0.1055 -0.0846 -0.1404 228 PHE A CG 1588 C CD1 . PHE A 201 ? 0.4797 0.3448 0.5556 0.1200 -0.1043 -0.1536 228 PHE A CD1 1589 C CD2 . PHE A 201 ? 0.4217 0.3091 0.4961 0.0913 -0.0776 -0.1415 228 PHE A CD2 1590 C CE1 . PHE A 201 ? 0.5436 0.3873 0.5985 0.1204 -0.1171 -0.1682 228 PHE A CE1 1591 C CE2 . PHE A 201 ? 0.4808 0.3472 0.5343 0.0917 -0.0896 -0.1547 228 PHE A CE2 1592 C CZ . PHE A 201 ? 0.5381 0.3840 0.5821 0.1063 -0.1095 -0.1685 228 PHE A CZ 1593 N N . TYR A 202 ? 0.3372 0.3190 0.4032 0.0867 -0.0241 -0.1451 229 TYR A N 1594 C CA . TYR A 202 ? 0.3664 0.3601 0.4071 0.0728 -0.0090 -0.1565 229 TYR A CA 1595 C C . TYR A 202 ? 0.3727 0.4112 0.3969 0.0722 0.0089 -0.1730 229 TYR A C 1596 O O . TYR A 202 ? 0.3874 0.4372 0.3869 0.0650 0.0173 -0.1881 229 TYR A O 1597 C CB . TYR A 202 ? 0.3194 0.3001 0.3664 0.0570 0.0001 -0.1403 229 TYR A CB 1598 C CG . TYR A 202 ? 0.3599 0.3016 0.4138 0.0551 -0.0167 -0.1303 229 TYR A CG 1599 C CD1 . TYR A 202 ? 0.4028 0.3276 0.4326 0.0521 -0.0218 -0.1418 229 TYR A CD1 1600 C CD2 . TYR A 202 ? 0.3792 0.3038 0.4642 0.0568 -0.0281 -0.1094 229 TYR A CD2 1601 C CE1 . TYR A 202 ? 0.4952 0.3873 0.5309 0.0514 -0.0388 -0.1340 229 TYR A CE1 1602 C CE2 . TYR A 202 ? 0.4327 0.3264 0.5266 0.0540 -0.0450 -0.1010 229 TYR A CE2 1603 C CZ . TYR A 202 ? 0.4624 0.3401 0.5311 0.0518 -0.0509 -0.1142 229 TYR A CZ 1604 O OH . TYR A 202 ? 0.5136 0.3635 0.5902 0.0500 -0.0687 -0.1073 229 TYR A OH 1605 N N . ALA A 203 ? 0.3503 0.4163 0.3884 0.0799 0.0145 -0.1696 230 ALA A N 1606 C CA . ALA A 203 ? 0.3257 0.4393 0.3518 0.0806 0.0284 -0.1844 230 ALA A CA 1607 C C . ALA A 203 ? 0.4300 0.5514 0.4409 0.0903 0.0186 -0.1930 230 ALA A C 1608 O O . ALA A 203 ? 0.4841 0.6324 0.4813 0.0803 0.0265 -0.1946 230 ALA A O 1609 C CB . ALA A 203 ? 0.3043 0.4431 0.3488 0.0898 0.0327 -0.1757 230 ALA A CB 1610 N N . ALA A 204 ? 0.4647 0.5593 0.4806 0.1103 0.0001 -0.1971 231 ALA A N 1611 C CA . ALA A 204 ? 0.4542 0.5520 0.4550 0.1231 -0.0106 -0.2049 231 ALA A CA 1612 C C . ALA A 204 ? 0.4986 0.5803 0.4786 0.1140 -0.0129 -0.2101 231 ALA A C 1613 O O . ALA A 204 ? 0.4810 0.5788 0.4461 0.1186 -0.0136 -0.2155 231 ALA A O 1614 C CB . ALA A 204 ? 0.4409 0.5080 0.4524 0.1474 -0.0311 -0.2047 231 ALA A CB 1615 N N . ALA A 205 ? 0.5488 0.5993 0.5287 0.1025 -0.0139 -0.2074 232 ALA A N 1616 C CA . ALA A 205 ? 0.6498 0.6794 0.6093 0.0961 -0.0179 -0.2100 232 ALA A CA 1617 C C . ALA A 205 ? 0.7756 0.8230 0.7181 0.0747 0.0030 -0.2070 232 ALA A C 1618 O O . ALA A 205 ? 0.8575 0.9059 0.7795 0.0718 0.0056 -0.2095 232 ALA A O 1619 C CB . ALA A 205 ? 0.6510 0.6323 0.6189 0.0966 -0.0347 -0.2064 232 ALA A CB 1620 N N . MET A 206 ? 0.7560 0.8143 0.7066 0.0604 0.0175 -0.2006 233 MET A N 1621 C CA . MET A 206 ? 0.7481 0.8134 0.6828 0.0396 0.0352 -0.1953 233 MET A CA 1622 C C . MET A 206 ? 0.7591 0.8654 0.6923 0.0343 0.0455 -0.1953 233 MET A C 1623 O O . MET A 206 ? 0.8043 0.9201 0.7239 0.0354 0.0462 -0.1991 233 MET A O 1624 C CB . MET A 206 ? 0.7115 0.7662 0.6547 0.0268 0.0446 -0.1878 233 MET A CB 1625 C CG . MET A 206 ? 0.6639 0.6790 0.6151 0.0314 0.0337 -0.1876 233 MET A CG 1626 S SD . MET A 206 ? 1.0181 1.0218 0.9829 0.0183 0.0460 -0.1733 233 MET A SD 1627 C CE . MET A 206 ? 1.1874 1.1869 1.1193 -0.0030 0.0649 -0.1712 233 MET A CE # 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 TRP 1 28 28 TRP TRP A . n A 1 2 ALA 2 29 29 ALA ALA A . n A 1 3 ARG 3 30 30 ARG ARG A . n A 1 4 THR 4 31 31 THR THR A . n A 1 5 GLU 5 32 32 GLU GLU A . n A 1 6 LEU 6 33 33 LEU LEU A . n A 1 7 LEU 7 34 34 LEU LEU A . n A 1 8 ASN 8 35 35 ASN ASN A . n A 1 9 VAL 9 36 36 VAL VAL A . n A 1 10 CYS 10 37 37 CYS CYS A . n A 1 11 MET 11 38 38 MET MET A . n A 1 12 ASN 12 39 39 ASN ASN A . n A 1 13 ALA 13 40 40 ALA ALA A . n A 1 14 LYS 14 41 41 LYS ALA A . n A 1 15 HIS 15 42 42 HIS HIS A . n A 1 16 HIS 16 43 43 HIS HIS A . n A 1 17 LYS 17 44 44 LYS LYS A . n A 1 18 GLU 18 45 45 GLU GLU A . n A 1 19 LYS 19 46 46 LYS ALA A . n A 1 20 PRO 20 47 47 PRO PRO A . n A 1 21 GLY 21 48 48 GLY GLY A . n A 1 22 PRO 22 49 49 PRO PRO A . n A 1 23 GLU 23 50 50 GLU GLU A . n A 1 24 ASP 24 51 51 ASP ASP A . n A 1 25 LYS 25 52 52 LYS LYS A . n A 1 26 LEU 26 53 53 LEU LEU A . n A 1 27 HIS 27 54 54 HIS HIS A . n A 1 28 GLU 28 55 55 GLU GLU A . n A 1 29 GLN 29 56 56 GLN GLN A . n A 1 30 CYS 30 57 57 CYS CYS A . n A 1 31 ARG 31 58 58 ARG ARG A . n A 1 32 PRO 32 59 59 PRO PRO A . n A 1 33 TRP 33 60 60 TRP TRP A . n A 1 34 ARG 34 61 61 ARG ARG A . n A 1 35 LYS 35 62 62 LYS LYS A . n A 1 36 ASN 36 63 63 ASN ASN A . n A 1 37 ALA 37 64 64 ALA ALA A . n A 1 38 CYS 38 65 65 CYS CYS A . n A 1 39 CYS 39 66 66 CYS CYS A . n A 1 40 SER 40 67 67 SER SER A . n A 1 41 THR 41 68 68 THR THR A . n A 1 42 ASN 42 69 ? ? ? A . n A 1 43 THR 43 70 ? ? ? A . n A 1 44 SER 44 71 ? ? ? A . n A 1 45 GLN 45 72 ? ? ? A . n A 1 46 GLU 46 73 ? ? ? A . n A 1 47 ALA 47 74 ? ? ? A . n A 1 48 HIS 48 75 ? ? ? A . n A 1 49 LYS 49 76 76 LYS ALA A . n A 1 50 ASP 50 77 77 ASP ASP A . n A 1 51 VAL 51 78 78 VAL VAL A . n A 1 52 SER 52 79 79 SER SER A . n A 1 53 TYR 53 80 80 TYR TYR A . n A 1 54 LEU 54 81 81 LEU LEU A . n A 1 55 TYR 55 82 82 TYR TYR A . n A 1 56 ARG 56 83 83 ARG ARG A . n A 1 57 PHE 57 84 84 PHE PHE A . n A 1 58 ASN 58 85 85 ASN ASN A . n A 1 59 TRP 59 86 86 TRP TRP A . n A 1 60 ASN 60 87 87 ASN ASN A . n A 1 61 HIS 61 88 88 HIS HIS A . n A 1 62 CYS 62 89 89 CYS CYS A . n A 1 63 GLY 63 90 90 GLY GLY A . n A 1 64 GLU 64 91 91 GLU GLU A . n A 1 65 MET 65 92 92 MET MET A . n A 1 66 ALA 66 93 93 ALA ALA A . n A 1 67 PRO 67 94 94 PRO PRO A . n A 1 68 ALA 68 95 95 ALA ALA A . n A 1 69 CYS 69 96 96 CYS CYS A . n A 1 70 LYS 70 97 97 LYS LYS A . n A 1 71 ARG 71 98 98 ARG ARG A . n A 1 72 HIS 72 99 99 HIS HIS A . n A 1 73 PHE 73 100 100 PHE PHE A . n A 1 74 ILE 74 101 101 ILE ILE A . n A 1 75 GLN 75 102 102 GLN GLN A . n A 1 76 ASP 76 103 103 ASP ASP A . n A 1 77 THR 77 104 104 THR THR A . n A 1 78 CYS 78 105 105 CYS CYS A . n A 1 79 LEU 79 106 106 LEU LEU A . n A 1 80 TYR 80 107 107 TYR TYR A . n A 1 81 GLU 81 108 108 GLU GLU A . n A 1 82 CYS 82 109 109 CYS CYS A . n A 1 83 SER 83 110 110 SER SER A . n A 1 84 PRO 84 111 111 PRO PRO A . n A 1 85 ASN 85 112 112 ASN ASN A . n A 1 86 LEU 86 113 113 LEU LEU A . n A 1 87 GLY 87 114 114 GLY GLY A . n A 1 88 PRO 88 115 115 PRO PRO A . n A 1 89 TRP 89 116 116 TRP TRP A . n A 1 90 ILE 90 117 117 ILE ILE A . n A 1 91 GLN 91 118 118 GLN GLN A . n A 1 92 GLN 92 119 119 GLN GLN A . n A 1 93 VAL 93 120 120 VAL VAL A . n A 1 94 ASP 94 121 121 ASP ASP A . n A 1 95 GLN 95 122 122 GLN GLN A . n A 1 96 SER 96 123 123 SER SER A . n A 1 97 TRP 97 124 124 TRP TRP A . n A 1 98 ARG 98 125 125 ARG ARG A . n A 1 99 LYS 99 126 126 LYS LYS A . n A 1 100 GLU 100 127 127 GLU GLU A . n A 1 101 ARG 101 128 128 ARG ARG A . n A 1 102 VAL 102 129 129 VAL VAL A . n A 1 103 LEU 103 130 130 LEU LEU A . n A 1 104 ASN 104 131 131 ASN ASN A . n A 1 105 VAL 105 132 132 VAL VAL A . n A 1 106 PRO 106 133 133 PRO PRO A . n A 1 107 LEU 107 134 134 LEU LEU A . n A 1 108 CYS 108 135 135 CYS CYS A . n A 1 109 LYS 109 136 136 LYS LYS A . n A 1 110 GLU 110 137 137 GLU GLU A . n A 1 111 ASP 111 138 138 ASP ASP A . n A 1 112 CYS 112 139 139 CYS CYS A . n A 1 113 GLU 113 140 140 GLU GLU A . n A 1 114 GLN 114 141 141 GLN GLN A . n A 1 115 TRP 115 142 142 TRP TRP A . n A 1 116 TRP 116 143 143 TRP TRP A . n A 1 117 GLU 117 144 144 GLU GLU A . n A 1 118 ASP 118 145 145 ASP ASP A . n A 1 119 CYS 119 146 146 CYS CYS A . n A 1 120 ARG 120 147 147 ARG ARG A . n A 1 121 THR 121 148 148 THR THR A . n A 1 122 SER 122 149 149 SER SER A . n A 1 123 TYR 123 150 150 TYR TYR A . n A 1 124 THR 124 151 151 THR THR A . n A 1 125 CYS 125 152 152 CYS CYS A . n A 1 126 LYS 126 153 153 LYS LYS A . n A 1 127 SER 127 154 154 SER SER A . n A 1 128 ASN 128 155 155 ASN ASN A . n A 1 129 TRP 129 156 156 TRP TRP A . n A 1 130 HIS 130 157 157 HIS HIS A . n A 1 131 LYS 131 158 158 LYS LYS A . n A 1 132 GLY 132 159 159 GLY GLY A . n A 1 133 TRP 133 160 160 TRP TRP A . n A 1 134 ASN 134 161 161 ASN ASN A . n A 1 135 TRP 135 162 162 TRP TRP A . n A 1 136 THR 136 163 163 THR THR A . n A 1 137 SER 137 164 164 SER SER A . n A 1 138 GLY 138 165 165 GLY GLY A . n A 1 139 PHE 139 166 166 PHE PHE A . n A 1 140 ASN 140 167 167 ASN ASN A . n A 1 141 LYS 141 168 168 LYS LYS A . n A 1 142 CYS 142 169 169 CYS CYS A . n A 1 143 ALA 143 170 170 ALA ALA A . n A 1 144 VAL 144 171 171 VAL VAL A . n A 1 145 GLY 145 172 172 GLY GLY A . n A 1 146 ALA 146 173 173 ALA ALA A . n A 1 147 ALA 147 174 174 ALA ALA A . n A 1 148 CYS 148 175 175 CYS CYS A . n A 1 149 GLN 149 176 176 GLN GLN A . n A 1 150 PRO 150 177 177 PRO PRO A . n A 1 151 PHE 151 178 178 PHE PHE A . n A 1 152 HIS 152 179 179 HIS HIS A . n A 1 153 PHE 153 180 180 PHE PHE A . n A 1 154 TYR 154 181 181 TYR TYR A . n A 1 155 PHE 155 182 182 PHE PHE A . n A 1 156 PRO 156 183 183 PRO PRO A . n A 1 157 THR 157 184 184 THR THR A . n A 1 158 PRO 158 185 185 PRO PRO A . n A 1 159 THR 159 186 186 THR THR A . n A 1 160 VAL 160 187 187 VAL VAL A . n A 1 161 LEU 161 188 188 LEU LEU A . n A 1 162 CYS 162 189 189 CYS CYS A . n A 1 163 ASN 163 190 190 ASN ASN A . n A 1 164 GLU 164 191 191 GLU GLU A . n A 1 165 ILE 165 192 192 ILE ILE A . n A 1 166 TRP 166 193 193 TRP TRP A . n A 1 167 THR 167 194 194 THR THR A . n A 1 168 HIS 168 195 195 HIS HIS A . n A 1 169 SER 169 196 196 SER SER A . n A 1 170 TYR 170 197 197 TYR TYR A . n A 1 171 LYS 171 198 198 LYS LYS A . n A 1 172 VAL 172 199 199 VAL VAL A . n A 1 173 SER 173 200 200 SER SER A . n A 1 174 ASN 174 201 201 ASN ASN A . n A 1 175 TYR 175 202 202 TYR TYR A . n A 1 176 SER 176 203 203 SER SER A . n A 1 177 ARG 177 204 204 ARG ARG A . n A 1 178 GLY 178 205 205 GLY GLY A . n A 1 179 SER 179 206 206 SER SER A . n A 1 180 GLY 180 207 207 GLY GLY A . n A 1 181 ARG 181 208 208 ARG ARG A . n A 1 182 CYS 182 209 209 CYS CYS A . n A 1 183 ILE 183 210 210 ILE ILE A . n A 1 184 GLN 184 211 211 GLN GLN A . n A 1 185 MET 185 212 212 MET MET A . n A 1 186 TRP 186 213 213 TRP TRP A . n A 1 187 PHE 187 214 214 PHE PHE A . n A 1 188 ASP 188 215 215 ASP ASP A . n A 1 189 PRO 189 216 216 PRO PRO A . n A 1 190 ALA 190 217 217 ALA ALA A . n A 1 191 GLN 191 218 218 GLN GLN A . n A 1 192 GLY 192 219 219 GLY GLY A . n A 1 193 ASN 193 220 220 ASN ASN A . n A 1 194 PRO 194 221 221 PRO PRO A . n A 1 195 ASN 195 222 222 ASN ASN A . n A 1 196 GLU 196 223 223 GLU GLU A . n A 1 197 GLU 197 224 224 GLU GLU A . n A 1 198 VAL 198 225 225 VAL VAL A . n A 1 199 ALA 199 226 226 ALA ALA A . n A 1 200 ARG 200 227 227 ARG ALA A . n A 1 201 PHE 201 228 228 PHE PHE A . n A 1 202 TYR 202 229 229 TYR TYR A . n A 1 203 ALA 203 230 230 ALA ALA A . n A 1 204 ALA 204 231 231 ALA ALA A . n A 1 205 ALA 205 232 232 ALA ALA A . n A 1 206 MET 206 233 233 MET MET A . n A 1 207 SER 207 234 ? ? ? 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 K 1 301 301 K K A . C 3 CL 1 302 302 CL CL A . D 4 NAG 1 303 303 NAG NAG A . E 4 NAG 2 304 304 NAG NAG A . F 5 FUC 3 305 305 FUC FUC A . G 4 NAG 1 306 306 NAG NAG A . H 6 HOH 1 401 401 HOH HOH A . H 6 HOH 2 402 402 HOH HOH A . H 6 HOH 3 403 403 HOH HOH A . H 6 HOH 4 404 404 HOH HOH A . H 6 HOH 5 405 405 HOH HOH A . H 6 HOH 6 406 406 HOH HOH A . H 6 HOH 7 407 407 HOH HOH A . H 6 HOH 8 408 408 HOH HOH A . H 6 HOH 9 409 409 HOH HOH A . H 6 HOH 10 410 410 HOH HOH A . H 6 HOH 11 411 411 HOH HOH A . H 6 HOH 12 412 412 HOH HOH A . H 6 HOH 13 413 413 HOH HOH A . H 6 HOH 14 414 414 HOH HOH A . H 6 HOH 15 415 415 HOH HOH A . H 6 HOH 16 416 416 HOH HOH A . H 6 HOH 17 417 417 HOH HOH A . H 6 HOH 18 418 418 HOH HOH A . H 6 HOH 19 419 419 HOH HOH A . H 6 HOH 20 420 420 HOH HOH A . H 6 HOH 21 421 421 HOH HOH A . H 6 HOH 22 422 422 HOH HOH A . H 6 HOH 23 423 423 HOH HOH A . H 6 HOH 24 424 424 HOH HOH A . H 6 HOH 25 425 425 HOH HOH A . H 6 HOH 26 426 426 HOH HOH A . H 6 HOH 27 427 427 HOH HOH A . H 6 HOH 28 428 428 HOH HOH A . H 6 HOH 29 429 429 HOH HOH A . H 6 HOH 30 430 430 HOH HOH A . H 6 HOH 31 431 431 HOH HOH A . H 6 HOH 32 432 432 HOH HOH A . H 6 HOH 33 433 433 HOH HOH A . H 6 HOH 34 434 434 HOH HOH A . H 6 HOH 35 435 435 HOH HOH A . H 6 HOH 36 436 436 HOH HOH A . H 6 HOH 37 437 437 HOH HOH A . H 6 HOH 38 438 438 HOH HOH A . H 6 HOH 39 439 439 HOH HOH A . H 6 HOH 40 440 440 HOH HOH A . H 6 HOH 41 441 441 HOH HOH A . H 6 HOH 42 442 442 HOH HOH A . H 6 HOH 43 443 443 HOH HOH A . H 6 HOH 44 444 444 HOH HOH A . H 6 HOH 45 445 445 HOH HOH A . H 6 HOH 46 446 446 HOH HOH A . H 6 HOH 47 447 447 HOH HOH A . H 6 HOH 48 448 448 HOH HOH A . H 6 HOH 49 449 449 HOH HOH A . H 6 HOH 50 450 450 HOH HOH A . H 6 HOH 51 451 451 HOH HOH A . H 6 HOH 52 452 452 HOH HOH A . H 6 HOH 53 453 453 HOH HOH A . H 6 HOH 54 454 454 HOH HOH A . H 6 HOH 55 455 455 HOH HOH A . H 6 HOH 56 456 456 HOH HOH A . H 6 HOH 57 457 457 HOH HOH A . H 6 HOH 58 458 458 HOH HOH A . H 6 HOH 59 459 459 HOH HOH A . H 6 HOH 60 460 460 HOH HOH A . H 6 HOH 61 461 461 HOH HOH A . H 6 HOH 62 462 462 HOH HOH A . H 6 HOH 63 463 463 HOH HOH A . H 6 HOH 64 464 464 HOH HOH A . H 6 HOH 65 465 465 HOH HOH A . H 6 HOH 66 466 466 HOH HOH A . H 6 HOH 67 467 467 HOH HOH A . H 6 HOH 68 468 468 HOH HOH A . H 6 HOH 69 469 469 HOH HOH A . H 6 HOH 70 470 470 HOH HOH A . H 6 HOH 71 471 471 HOH HOH A . H 6 HOH 72 472 472 HOH HOH A . H 6 HOH 73 473 473 HOH HOH A . H 6 HOH 74 474 474 HOH HOH A . H 6 HOH 75 475 475 HOH HOH A . H 6 HOH 76 476 476 HOH HOH A . H 6 HOH 77 477 477 HOH HOH A . H 6 HOH 78 478 478 HOH HOH A . H 6 HOH 79 479 479 HOH HOH A . H 6 HOH 80 480 480 HOH HOH A . H 6 HOH 81 481 481 HOH HOH A . H 6 HOH 82 482 482 HOH HOH A . H 6 HOH 83 483 483 HOH HOH A . H 6 HOH 84 484 484 HOH HOH A . H 6 HOH 85 485 485 HOH HOH A . H 6 HOH 86 486 486 HOH HOH A . H 6 HOH 87 487 487 HOH HOH A . H 6 HOH 88 488 488 HOH HOH A . H 6 HOH 89 489 489 HOH HOH A . H 6 HOH 90 490 490 HOH HOH A . H 6 HOH 91 491 491 HOH HOH A . H 6 HOH 92 492 492 HOH HOH A . H 6 HOH 93 493 493 HOH HOH A . H 6 HOH 94 494 494 HOH HOH A . H 6 HOH 95 495 495 HOH HOH A . H 6 HOH 96 496 496 HOH HOH A . H 6 HOH 97 497 497 HOH HOH A . H 6 HOH 98 498 498 HOH HOH A . H 6 HOH 99 499 499 HOH HOH A . H 6 HOH 100 500 500 HOH HOH A . H 6 HOH 101 501 501 HOH HOH A . H 6 HOH 102 502 502 HOH HOH A . H 6 HOH 103 503 503 HOH HOH A . H 6 HOH 104 504 504 HOH HOH A . H 6 HOH 105 505 505 HOH HOH A . H 6 HOH 106 506 506 HOH HOH A . H 6 HOH 107 507 507 HOH HOH A . H 6 HOH 108 508 508 HOH HOH A . H 6 HOH 109 509 509 HOH HOH A . H 6 HOH 110 510 510 HOH HOH A . H 6 HOH 111 511 511 HOH HOH A . H 6 HOH 112 512 512 HOH HOH A . H 6 HOH 113 513 513 HOH HOH A . H 6 HOH 114 514 514 HOH HOH A . H 6 HOH 115 515 515 HOH HOH A . H 6 HOH 116 516 516 HOH HOH A . H 6 HOH 117 517 517 HOH HOH A . H 6 HOH 118 518 518 HOH HOH A . H 6 HOH 119 519 519 HOH HOH A . H 6 HOH 120 520 520 HOH HOH A . H 6 HOH 121 521 521 HOH HOH A . H 6 HOH 122 522 522 HOH HOH A . H 6 HOH 123 523 523 HOH HOH A . H 6 HOH 124 524 524 HOH HOH A . H 6 HOH 125 525 525 HOH HOH A . H 6 HOH 126 526 526 HOH HOH A . H 6 HOH 127 527 527 HOH HOH A . H 6 HOH 128 528 528 HOH HOH A . H 6 HOH 129 529 529 HOH HOH A . H 6 HOH 130 530 530 HOH HOH A . H 6 HOH 131 531 531 HOH HOH A . H 6 HOH 132 532 532 HOH HOH A . H 6 HOH 133 533 533 HOH HOH A . H 6 HOH 134 534 534 HOH HOH A . H 6 HOH 135 535 535 HOH HOH A . H 6 HOH 136 536 536 HOH HOH A . H 6 HOH 137 537 537 HOH HOH A . H 6 HOH 138 538 538 HOH HOH A . H 6 HOH 139 539 539 HOH HOH A . H 6 HOH 140 540 540 HOH HOH A . H 6 HOH 141 541 541 HOH HOH A . H 6 HOH 142 542 542 HOH HOH A . H 6 HOH 143 543 543 HOH HOH A . H 6 HOH 144 544 544 HOH HOH A . H 6 HOH 145 545 545 HOH HOH A . H 6 HOH 146 546 546 HOH HOH A . H 6 HOH 147 547 547 HOH HOH A . H 6 HOH 148 548 548 HOH HOH A . H 6 HOH 149 549 549 HOH HOH A . H 6 HOH 150 550 550 HOH HOH A . H 6 HOH 151 551 551 HOH HOH A . H 6 HOH 152 552 552 HOH HOH A . H 6 HOH 153 553 553 HOH HOH A . H 6 HOH 154 554 554 HOH HOH A . H 6 HOH 155 555 555 HOH HOH A . H 6 HOH 156 556 556 HOH HOH A . H 6 HOH 157 557 557 HOH HOH A . H 6 HOH 158 558 558 HOH HOH A . H 6 HOH 159 559 559 HOH HOH A . H 6 HOH 160 560 560 HOH HOH A . H 6 HOH 161 561 561 HOH HOH A . H 6 HOH 162 562 562 HOH HOH A . H 6 HOH 163 563 563 HOH HOH A . H 6 HOH 164 564 564 HOH HOH A . H 6 HOH 165 565 565 HOH HOH A . H 6 HOH 166 566 566 HOH HOH A . H 6 HOH 167 567 567 HOH HOH A . H 6 HOH 168 568 568 HOH HOH A . H 6 HOH 169 569 569 HOH HOH A . H 6 HOH 170 570 570 HOH HOH A . H 6 HOH 171 571 571 HOH HOH A . H 6 HOH 172 572 572 HOH HOH A . H 6 HOH 173 573 573 HOH HOH A . H 6 HOH 174 574 574 HOH HOH A . H 6 HOH 175 575 575 HOH HOH A . H 6 HOH 176 576 576 HOH HOH A . H 6 HOH 177 577 577 HOH HOH A . H 6 HOH 178 578 578 HOH HOH A . H 6 HOH 179 579 579 HOH HOH A . H 6 HOH 180 580 580 HOH HOH A . H 6 HOH 181 581 581 HOH HOH A . H 6 HOH 182 582 582 HOH HOH A . H 6 HOH 183 583 583 HOH HOH A . H 6 HOH 184 584 584 HOH HOH A . H 6 HOH 185 585 585 HOH HOH A . H 6 HOH 186 586 586 HOH HOH A . H 6 HOH 187 587 587 HOH HOH A . H 6 HOH 188 588 588 HOH HOH A . H 6 HOH 189 589 589 HOH HOH A . H 6 HOH 190 590 590 HOH HOH A . H 6 HOH 191 591 591 HOH HOH A . H 6 HOH 192 592 592 HOH HOH A . H 6 HOH 193 593 593 HOH HOH A . H 6 HOH 194 594 594 HOH HOH A . H 6 HOH 195 595 595 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 174 A ASN 201 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 134 A ASN 161 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details 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 # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # _pdbx_struct_conn_angle.id 1 _pdbx_struct_conn_angle.ptnr1_label_atom_id OG _pdbx_struct_conn_angle.ptnr1_label_alt_id ? _pdbx_struct_conn_angle.ptnr1_label_asym_id A _pdbx_struct_conn_angle.ptnr1_label_comp_id SER _pdbx_struct_conn_angle.ptnr1_label_seq_id 83 _pdbx_struct_conn_angle.ptnr1_auth_atom_id ? _pdbx_struct_conn_angle.ptnr1_auth_asym_id A _pdbx_struct_conn_angle.ptnr1_auth_comp_id SER _pdbx_struct_conn_angle.ptnr1_auth_seq_id 110 _pdbx_struct_conn_angle.ptnr1_PDB_ins_code ? _pdbx_struct_conn_angle.ptnr1_symmetry 1_555 _pdbx_struct_conn_angle.ptnr2_label_atom_id K _pdbx_struct_conn_angle.ptnr2_label_alt_id ? _pdbx_struct_conn_angle.ptnr2_label_asym_id B _pdbx_struct_conn_angle.ptnr2_label_comp_id K _pdbx_struct_conn_angle.ptnr2_label_seq_id . _pdbx_struct_conn_angle.ptnr2_auth_atom_id ? _pdbx_struct_conn_angle.ptnr2_auth_asym_id A _pdbx_struct_conn_angle.ptnr2_auth_comp_id K _pdbx_struct_conn_angle.ptnr2_auth_seq_id 301 _pdbx_struct_conn_angle.ptnr2_PDB_ins_code ? _pdbx_struct_conn_angle.ptnr2_symmetry 1_555 _pdbx_struct_conn_angle.ptnr3_label_atom_id OD1 _pdbx_struct_conn_angle.ptnr3_label_alt_id ? _pdbx_struct_conn_angle.ptnr3_label_asym_id A _pdbx_struct_conn_angle.ptnr3_label_comp_id ASN _pdbx_struct_conn_angle.ptnr3_label_seq_id 85 _pdbx_struct_conn_angle.ptnr3_auth_atom_id ? _pdbx_struct_conn_angle.ptnr3_auth_asym_id A _pdbx_struct_conn_angle.ptnr3_auth_comp_id ASN _pdbx_struct_conn_angle.ptnr3_auth_seq_id 112 _pdbx_struct_conn_angle.ptnr3_PDB_ins_code ? _pdbx_struct_conn_angle.ptnr3_symmetry 1_555 _pdbx_struct_conn_angle.value 86.9 _pdbx_struct_conn_angle.value_esd ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-08-07 2 'Structure model' 1 1 2013-10-02 3 'Structure model' 1 2 2017-11-15 # _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' 'Database references' 2 3 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 3 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_software.name' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 31.6295 67.0841 -1.3423 0.2390 0.2883 0.2015 -0.0084 -0.0102 -0.0794 1.8465 1.8105 1.7027 -0.8755 -0.6408 0.9522 0.0658 -0.0781 0.3516 0.1562 0.1428 -0.4229 0.1976 0.0340 -0.1693 'X-RAY DIFFRACTION' 2 ? refined 26.4702 77.2763 6.3797 0.2364 0.2656 0.3860 0.0353 -0.0586 -0.0288 1.7429 1.7344 1.8009 -1.5461 -0.4713 0.6352 -0.5162 -0.4883 0.5694 0.3864 0.5924 -0.7274 0.1583 0.4152 -0.1529 'X-RAY DIFFRACTION' 3 ? refined 17.6179 73.9906 13.9153 0.2918 0.2642 0.2666 0.1027 0.0493 0.0346 2.5684 1.3327 0.5746 -1.3994 -0.8426 0.8511 -0.2926 -0.8413 -0.3595 0.5391 0.3539 -0.2576 -0.2604 0.2000 0.0423 'X-RAY DIFFRACTION' 4 ? refined 8.0964 70.6435 12.0385 0.3624 0.2382 0.3449 0.0547 0.1059 0.0693 3.0395 1.4530 1.4253 0.1922 -0.5172 -0.9376 -0.2112 -0.3655 -0.6564 0.7100 0.0514 0.0771 0.4780 -0.0552 0.2867 'X-RAY DIFFRACTION' 5 ? refined 16.5262 70.1557 13.7509 0.3006 0.3034 0.3820 0.0810 0.0183 0.1218 3.4797 5.6417 2.9440 0.7401 -1.3217 -1.5923 0.0955 -0.7975 -1.1385 0.4925 0.3168 0.2353 0.3086 0.1028 0.0645 'X-RAY DIFFRACTION' 6 ? refined 8.5804 85.8215 10.8942 0.2576 0.3355 0.1684 -0.0012 0.0203 -0.0065 2.9006 2.3604 0.7603 -0.2934 -1.4816 -0.1514 0.0959 -0.7998 -0.0603 0.0610 -0.1622 -0.1253 -0.1163 0.1918 0.0368 'X-RAY DIFFRACTION' 7 ? refined -3.4660 86.5233 3.8875 0.2310 0.2201 0.2147 0.0360 0.0631 -0.0187 2.6314 3.1000 2.8210 -0.5054 1.9251 0.6454 -0.1379 -0.4453 -0.3086 0.1558 -0.1585 0.5401 0.0905 -0.5819 0.1590 'X-RAY DIFFRACTION' 8 ? refined 5.0503 76.9620 4.3016 0.2347 0.1718 0.2794 0.0108 0.0159 0.0244 4.8896 0.4999 0.6145 -1.0006 1.2271 -0.2575 0.1507 -0.3325 -0.6783 0.2498 0.0256 0.2486 0.1314 -0.1077 -0.1065 'X-RAY DIFFRACTION' 9 ? refined 20.6835 80.2126 0.7139 0.2235 0.2244 0.2559 0.0125 0.0002 -0.0379 0.4561 2.7394 1.2199 -0.1505 -0.1936 0.0962 0.0007 0.0256 -0.0852 0.0326 -0.0536 -0.4453 -0.1745 0.1539 -0.0070 'X-RAY DIFFRACTION' 10 ? refined 15.9123 77.0148 -4.8115 0.2202 0.2866 0.2789 0.0359 0.0254 -0.1205 0.8752 0.9729 2.7931 0.5510 0.6561 -0.3005 -0.0020 0.5232 -0.6828 0.2164 0.1214 -0.1302 -0.1612 0.2176 -0.3051 'X-RAY DIFFRACTION' 11 ? refined 0.5996 73.2552 -7.0505 0.2869 0.2317 0.4723 -0.0153 -0.0679 -0.1371 0.3359 1.9802 1.2680 -0.7441 0.0287 0.4514 0.2660 0.4316 -1.2465 -0.2736 0.0604 0.5970 0.3402 -0.2241 0.1379 'X-RAY DIFFRACTION' 12 ? refined 1.5774 89.2390 -3.7244 0.2279 0.1705 0.1472 0.0175 -0.0308 -0.0026 2.1997 1.4688 1.1579 -0.9493 0.5566 0.6771 0.0079 0.0603 0.0229 -0.1295 -0.0600 0.1075 -0.1436 -0.0037 0.0620 'X-RAY DIFFRACTION' 13 ? refined 11.2105 78.9208 -7.8073 0.2921 0.2990 0.1233 0.0073 -0.0115 -0.0220 1.5258 2.5014 0.1185 -0.0615 0.1653 -0.4435 -0.0502 0.1898 -0.2162 -0.5078 -0.0625 0.2091 -0.4314 0.4457 -0.0335 'X-RAY DIFFRACTION' 14 ? refined 9.9047 65.5788 -3.4599 0.2360 0.1280 0.5211 -0.0066 -0.0248 -0.0954 2.5855 0.8495 0.5712 -1.3198 0.4244 0.3017 -0.0258 -0.0793 -1.6340 0.0112 0.0666 0.2188 0.1350 -0.1170 0.1907 'X-RAY DIFFRACTION' 15 ? refined 18.1523 63.9740 -2.0245 0.2909 0.2482 0.5023 0.0962 -0.0335 -0.0289 1.7344 1.2175 3.3726 -1.0510 0.0669 -0.1493 0.1399 -0.1827 -0.6616 -0.2950 0.3869 0.5319 0.3942 0.4302 0.5873 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 28:33) ; 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 34:43) ; 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 44:54) ; 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 55:60) ; 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 61:68) ; 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 76:85) ; 'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 86:93) ; 'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 94:109) ; 'X-RAY DIFFRACTION' 9 9 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 110:126) ; 'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 127:135) ; 'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 136:145) ; 'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 146:191) ; 'X-RAY DIFFRACTION' 13 13 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 192:201) ; 'X-RAY DIFFRACTION' 14 14 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 202:215) ; 'X-RAY DIFFRACTION' 15 15 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 216:233) ; # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 SCALEPACK . ? program 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data scaling' http://www.hkl-xray.com/ ? ? 2 PHENIX 1.7_650 ? package 'Paul D. Adams' PDAdams@lbl.gov refinement http://www.phenix-online.org/ C++ ? 3 PDB_EXTRACT 3.11 'April 22, 2011' package PDB deposit@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 4 HKL-2000 . ? ? ? ? 'data collection' ? ? ? 5 DENZO . ? ? ? ? 'data reduction' ? ? ? 6 PHASER . ? ? ? ? phasing ? ? ? # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 O4 _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 NAG _pdbx_validate_close_contact.auth_seq_id_1 303 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 O5 _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 NAG _pdbx_validate_close_contact.auth_seq_id_2 304 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.15 # 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 TYR A 82 ? ? -152.74 -17.05 2 1 ASN A 87 ? ? -94.91 44.18 3 1 ASP A 121 ? ? -147.16 26.04 4 1 LYS A 126 ? ? -126.23 -123.48 5 1 THR A 194 ? ? 38.64 63.40 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A LYS 41 ? CG ? A LYS 14 CG 2 1 Y 1 A LYS 41 ? CD ? A LYS 14 CD 3 1 Y 1 A LYS 41 ? CE ? A LYS 14 CE 4 1 Y 1 A LYS 41 ? NZ ? A LYS 14 NZ 5 1 Y 1 A LYS 46 ? CG ? A LYS 19 CG 6 1 Y 1 A LYS 46 ? CD ? A LYS 19 CD 7 1 Y 1 A LYS 46 ? CE ? A LYS 19 CE 8 1 Y 1 A LYS 46 ? NZ ? A LYS 19 NZ 9 1 Y 1 A LYS 76 ? CG ? A LYS 49 CG 10 1 Y 1 A LYS 76 ? CD ? A LYS 49 CD 11 1 Y 1 A LYS 76 ? CE ? A LYS 49 CE 12 1 Y 1 A LYS 76 ? NZ ? A LYS 49 NZ 13 1 Y 1 A ARG 227 ? CG ? A ARG 200 CG 14 1 Y 1 A ARG 227 ? CD ? A ARG 200 CD 15 1 Y 1 A ARG 227 ? NE ? A ARG 200 NE 16 1 Y 1 A ARG 227 ? CZ ? A ARG 200 CZ 17 1 Y 1 A ARG 227 ? NH1 ? A ARG 200 NH1 18 1 Y 1 A ARG 227 ? NH2 ? A ARG 200 NH2 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A ASN 69 ? A ASN 42 2 1 Y 1 A THR 70 ? A THR 43 3 1 Y 1 A SER 71 ? A SER 44 4 1 Y 1 A GLN 72 ? A GLN 45 5 1 Y 1 A GLU 73 ? A GLU 46 6 1 Y 1 A ALA 74 ? A ALA 47 7 1 Y 1 A HIS 75 ? A HIS 48 8 1 Y 1 A SER 234 ? A SER 207 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'POTASSIUM ION' K 3 'CHLORIDE ION' CL 4 N-ACETYL-D-GLUCOSAMINE NAG 5 ALPHA-L-FUCOSE FUC 6 water HOH #