data_4KN0 # _entry.id 4KN0 # _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 4KN0 RCSB RCSB079541 WWPDB D_1000079541 # 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 4KMX 'Human folate receptor alpha (FOLR1) at acidic pH' 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 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 4KN0 _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 4KN0 _cell.length_a 97.601 _cell.length_b 97.601 _cell.length_c 99.374 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 12 _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 4KN0 _symmetry.space_group_name_H-M 'P 61 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 178 _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 beta' 24021.988 1 ? ? 'UNP residues 24-228' ? 2 non-polymer syn METHOTREXATE 454.439 1 ? ? ? ? 3 non-polymer syn 'POTASSIUM ION' 39.098 1 ? ? ? ? 4 non-polymer syn 'CHLORIDE ION' 35.453 2 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 6 water nat water 18.015 228 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'FR-beta, Folate receptor 2, Folate receptor, fetal/placental, Placental folate-binding protein, FBP' # _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 ;GSRTDLLNVCMDAKHHKTKPGPEDKLHDQCSPWKKNACCTASTSQELHKDTSRLYNFNWDHCGKMEPACKRHFIQDTCLY ECSPNLGPWIQQVNQSWRKERFLDVPLCKEDCQRWWEDCHTSHTCKSNWHRGWDWTSGVNKCPAGALCRTFESYFPTPAA LCEGLWSHSYKVSNYSRGSGRCIQMWFDSAQGNPNEEVARFYAAAMH ; _entity_poly.pdbx_seq_one_letter_code_can ;GSRTDLLNVCMDAKHHKTKPGPEDKLHDQCSPWKKNACCTASTSQELHKDTSRLYNFNWDHCGKMEPACKRHFIQDTCLY ECSPNLGPWIQQVNQSWRKERFLDVPLCKEDCQRWWEDCHTSHTCKSNWHRGWDWTSGVNKCPAGALCRTFESYFPTPAA LCEGLWSHSYKVSNYSRGSGRCIQMWFDSAQGNPNEEVARFYAAAMH ; _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 GLY n 1 2 SER n 1 3 ARG n 1 4 THR n 1 5 ASP 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 ASP n 1 13 ALA n 1 14 LYS n 1 15 HIS n 1 16 HIS n 1 17 LYS n 1 18 THR 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 ASP n 1 29 GLN n 1 30 CYS n 1 31 SER n 1 32 PRO n 1 33 TRP n 1 34 LYS n 1 35 LYS n 1 36 ASN n 1 37 ALA n 1 38 CYS n 1 39 CYS n 1 40 THR n 1 41 ALA n 1 42 SER n 1 43 THR n 1 44 SER n 1 45 GLN n 1 46 GLU n 1 47 LEU n 1 48 HIS n 1 49 LYS n 1 50 ASP n 1 51 THR n 1 52 SER n 1 53 ARG n 1 54 LEU n 1 55 TYR n 1 56 ASN n 1 57 PHE n 1 58 ASN n 1 59 TRP n 1 60 ASP n 1 61 HIS n 1 62 CYS n 1 63 GLY n 1 64 LYS n 1 65 MET n 1 66 GLU 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 ASN 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 PHE n 1 103 LEU n 1 104 ASP 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 GLN n 1 114 ARG n 1 115 TRP n 1 116 TRP n 1 117 GLU n 1 118 ASP n 1 119 CYS n 1 120 HIS n 1 121 THR n 1 122 SER n 1 123 HIS 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 ARG n 1 132 GLY n 1 133 TRP n 1 134 ASP n 1 135 TRP n 1 136 THR n 1 137 SER n 1 138 GLY n 1 139 VAL n 1 140 ASN n 1 141 LYS n 1 142 CYS n 1 143 PRO n 1 144 ALA n 1 145 GLY n 1 146 ALA n 1 147 LEU n 1 148 CYS n 1 149 ARG n 1 150 THR n 1 151 PHE n 1 152 GLU n 1 153 SER n 1 154 TYR n 1 155 PHE n 1 156 PRO n 1 157 THR n 1 158 PRO n 1 159 ALA n 1 160 ALA n 1 161 LEU n 1 162 CYS n 1 163 GLU n 1 164 GLY n 1 165 LEU n 1 166 TRP n 1 167 SER 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 SER 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 HIS 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 FOLR2 _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 'Chinese hamster' _entity_src_gen.pdbx_host_org_scientific_name 'Cricetulus griseus' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 10029 _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 CHO _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 pSGHV0 _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code FOLR2_HUMAN _struct_ref.pdbx_db_accession P14207 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;RTDLLNVCMDAKHHKTKPGPEDKLHDQCSPWKKNACCTASTSQELHKDTSRLYNFNWDHCGKMEPACKRHFIQDTCLYEC SPNLGPWIQQVNQSWRKERFLDVPLCKEDCQRWWEDCHTSHTCKSNWHRGWDWTSGVNKCPAGALCRTFESYFPTPAALC EGLWSHSYKVSNYSRGSGRCIQMWFDSAQGNPNEEVARFYAAAMH ; _struct_ref.pdbx_align_begin 24 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4KN0 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 3 _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 P14207 _struct_ref_seq.db_align_beg 24 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 228 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 24 _struct_ref_seq.pdbx_auth_seq_align_end 228 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4KN0 GLY A 1 ? UNP P14207 ? ? 'EXPRESSION TAG' 22 1 1 4KN0 SER A 2 ? UNP P14207 ? ? 'EXPRESSION TAG' 23 2 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 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 MTX non-polymer . METHOTREXATE ? 'C20 H22 N8 O5' 454.439 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.crystals_number 1 _exptl.entry_id 4KN0 _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.density_Matthews 2.88 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 57.22 _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.pH 8.0 _exptl_crystal_grow.temp 293 _exptl_crystal_grow.pdbx_details '0.2 M Lithium sulfate, 0.1 M Tris-HCl pH 8.0, 20% (w/v) PEG 3350, Vapor diffusion, sitting drop, temperature 293K' _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_pH_range ? # _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 NOIR-1 _diffrn_detector.pdbx_collection_date 2011-01-30 _diffrn_detector.details 'The NOIR-1 detector was built by E. Westbrook; 180 cm lens focused CCD' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator 'SAGITALLY FOCUSED Si(111)' _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0008 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ALS BEAMLINE 4.2.2' _diffrn_source.pdbx_wavelength_list 1.0008 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_site ALS _diffrn_source.pdbx_synchrotron_beamline 4.2.2 # _reflns.entry_id 4KN0 _reflns.d_resolution_high 2.100 _reflns.d_resolution_low 50.000 _reflns.number_obs 16898 _reflns.pdbx_Rmerge_I_obs 0.123 _reflns.pdbx_netI_over_sigmaI 7.300 _reflns.pdbx_chi_squared 0.812 _reflns.pdbx_redundancy 8.700 _reflns.percent_possible_obs 100.000 _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.number_all ? _reflns.pdbx_Rsym_value ? _reflns.B_iso_Wilson_estimate ? _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_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # loop_ _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.number_measured_obs _reflns_shell.number_measured_all _reflns_shell.number_unique_obs _reflns_shell.Rmerge_I_obs _reflns_shell.meanI_over_sigI_obs _reflns_shell.pdbx_Rsym_value _reflns_shell.pdbx_chi_squared _reflns_shell.pdbx_redundancy _reflns_shell.percent_possible_obs _reflns_shell.number_unique_all _reflns_shell.percent_possible_all _reflns_shell.pdbx_ordinal _reflns_shell.pdbx_diffrn_id 2.100 2.140 ? ? ? 0.495 ? ? 1.121 6.900 ? 825 99.800 1 1 2.140 2.180 ? ? ? 0.426 ? ? 1.229 8.500 ? 829 100.000 2 1 2.180 2.220 ? ? ? 0.359 ? ? 0.646 8.900 ? 817 100.000 3 1 2.220 2.260 ? ? ? 0.336 ? ? 0.634 8.900 ? 818 100.000 4 1 2.260 2.310 ? ? ? 0.331 ? ? 0.569 8.900 ? 826 100.000 5 1 2.310 2.370 ? ? ? 0.310 ? ? 0.569 8.900 ? 827 100.000 6 1 2.370 2.420 ? ? ? 0.284 ? ? 0.570 8.900 ? 826 100.000 7 1 2.420 2.490 ? ? ? 0.276 ? ? 0.598 8.900 ? 831 100.000 8 1 2.490 2.560 ? ? ? 0.223 ? ? 0.631 8.900 ? 827 100.000 9 1 2.560 2.650 ? ? ? 0.198 ? ? 0.669 8.900 ? 827 100.000 10 1 2.650 2.740 ? ? ? 0.168 ? ? 0.678 8.900 ? 836 100.000 11 1 2.740 2.850 ? ? ? 0.160 ? ? 0.678 8.900 ? 836 100.000 12 1 2.850 2.980 ? ? ? 0.146 ? ? 0.827 8.900 ? 834 100.000 13 1 2.980 3.140 ? ? ? 0.124 ? ? 0.816 8.800 ? 843 100.000 14 1 3.140 3.330 ? ? ? 0.107 ? ? 0.846 8.800 ? 854 100.000 15 1 3.330 3.590 ? ? ? 0.099 ? ? 0.951 8.800 ? 850 100.000 16 1 3.590 3.950 ? ? ? 0.084 ? ? 0.980 8.700 ? 860 100.000 17 1 3.950 4.520 ? ? ? 0.073 ? ? 1.254 8.600 ? 872 100.000 18 1 4.520 5.700 ? ? ? 0.061 ? ? 1.003 8.500 ? 884 100.000 19 1 5.700 50.000 ? ? ? 0.059 ? ? 1.046 7.800 ? 976 99.900 20 1 # _refine.entry_id 4KN0 _refine.ls_d_res_high 2.1000 _refine.ls_d_res_low 48.8010 _refine.pdbx_ls_sigma_F 1.340 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_percent_reflns_obs 99.8200 _refine.ls_number_reflns_obs 16841 _refine.ls_number_reflns_all ? _refine.pdbx_ls_cross_valid_method ? _refine.pdbx_R_Free_selection_details ? _refine.details ? _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.1814 _refine.ls_R_factor_R_work 0.1784 _refine.ls_wR_factor_R_work ? _refine.ls_R_factor_R_free 0.2309 _refine.ls_wR_factor_R_free ? _refine.ls_percent_reflns_R_free 5.8600 _refine.ls_number_reflns_R_free 987 _refine.ls_R_factor_R_free_error ? _refine.B_iso_mean 25.2370 _refine.solvent_model_param_bsol 38.5200 _refine.solvent_model_param_ksol 0.3460 _refine.pdbx_isotropic_thermal_model ? _refine.aniso_B[1][1] -4.3119 _refine.aniso_B[2][2] -4.3119 _refine.aniso_B[3][3] 8.6239 _refine.aniso_B[1][2] -0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][3] 0.0000 _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.5800 _refine.overall_SU_B ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.pdbx_solvent_vdw_probe_radii 1.1000 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.8300 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.pdbx_starting_model 'PDB ENTRY 4KMZ' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.overall_FOM_work_R_set 0.8508 _refine.B_iso_max 77.190 _refine.B_iso_min 10.840 _refine.pdbx_overall_phase_error 20.7600 _refine.occupancy_max 1.000 _refine.occupancy_min 0.440 _refine.pdbx_ls_sigma_I ? _refine.ls_redundancy_reflns_obs ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.overall_FOM_free_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1652 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 92 _refine_hist.number_atoms_solvent 228 _refine_hist.number_atoms_total 1972 _refine_hist.d_res_high 2.1000 _refine_hist.d_res_low 48.8010 # loop_ _refine_ls_restr.type _refine_ls_restr.number _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function _refine_ls_restr.pdbx_refine_id f_bond_d 1820 0.013 ? ? ? 'X-RAY DIFFRACTION' f_angle_d 2461 1.266 ? ? ? 'X-RAY DIFFRACTION' f_chiral_restr 245 0.090 ? ? ? 'X-RAY DIFFRACTION' f_plane_restr 315 0.007 ? ? ? 'X-RAY DIFFRACTION' f_dihedral_angle_d 656 14.138 ? ? ? 'X-RAY DIFFRACTION' # loop_ _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.percent_reflns_obs _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_R_work _refine_ls_shell.R_factor_R_free _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.number_reflns_all _refine_ls_shell.number_reflns_obs _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.pdbx_refine_id 2.1003 2.2110 7 100.0000 2220 . 0.2098 0.2678 . 132 . 2352 . . 'X-RAY DIFFRACTION' 2.2110 2.3495 7 100.0000 2182 . 0.1732 0.2503 . 161 . 2343 . . 'X-RAY DIFFRACTION' 2.3495 2.5309 7 100.0000 2230 . 0.1978 0.2870 . 130 . 2360 . . 'X-RAY DIFFRACTION' 2.5309 2.7856 7 100.0000 2231 . 0.1967 0.2434 . 153 . 2384 . . 'X-RAY DIFFRACTION' 2.7856 3.1886 7 100.0000 2242 . 0.1847 0.2389 . 140 . 2382 . . 'X-RAY DIFFRACTION' 3.1886 4.0170 7 100.0000 2307 . 0.1551 0.2135 . 132 . 2439 . . 'X-RAY DIFFRACTION' 4.0170 48.8137 7 100.0000 2442 . 0.1747 0.1993 . 139 . 2581 . . 'X-RAY DIFFRACTION' # _struct.entry_id 4KN0 _struct.title 'Human folate receptor beta (FOLR2) in complex with the antifolate methotrexate' _struct.pdbx_descriptor 'Folate receptor beta' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4KN0 _struct_keywords.text ;Folate Receptor Beta, FOLR2, 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 5 ? H N N 5 ? I N N 5 ? J 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 24 LEU A 28 5 ? 5 HELX_P HELX_P2 2 HIS A 27 ? LYS A 34 ? HIS A 48 LYS A 55 5 ? 8 HELX_P HELX_P3 3 THR A 40 ? LEU A 47 ? THR A 61 LEU A 68 1 ? 8 HELX_P HELX_P4 4 GLU A 66 ? SER A 83 ? GLU A 87 SER A 104 1 ? 18 HELX_P HELX_P5 5 LEU A 86 ? PRO A 88 ? LEU A 107 PRO A 109 5 ? 3 HELX_P HELX_P6 6 CYS A 108 ? CYS A 119 ? CYS A 129 CYS A 140 1 ? 12 HELX_P HELX_P7 7 PHE A 151 ? PHE A 155 ? PHE A 172 PHE A 176 1 ? 5 HELX_P HELX_P8 8 THR A 157 ? LEU A 165 ? THR A 178 LEU A 186 1 ? 9 HELX_P HELX_P9 9 PRO A 194 ? MET A 206 ? PRO A 215 MET A 227 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 31 A CYS 59 1_555 ? ? ? ? ? ? ? 2.087 ? disulf2 disulf ? ? A CYS 30 SG ? ? ? 1_555 A CYS 78 SG ? ? A CYS 51 A CYS 99 1_555 ? ? ? ? ? ? ? 2.033 ? disulf3 disulf ? ? A CYS 39 SG ? ? ? 1_555 A CYS 82 SG ? ? A CYS 60 A CYS 103 1_555 ? ? ? ? ? ? ? 2.037 ? disulf4 disulf ? ? A CYS 62 SG ? ? ? 1_555 A CYS 148 SG ? ? A CYS 83 A CYS 169 1_555 ? ? ? ? ? ? ? 2.061 ? disulf5 disulf ? ? A CYS 69 SG ? ? ? 1_555 A CYS 119 SG ? ? A CYS 90 A CYS 140 1_555 ? ? ? ? ? ? ? 2.043 ? disulf6 disulf ? ? A CYS 108 SG ? ? ? 1_555 A CYS 182 SG ? ? A CYS 129 A CYS 203 1_555 ? ? ? ? ? ? ? 2.024 ? disulf7 disulf ? ? A CYS 112 SG ? ? ? 1_555 A CYS 162 SG ? ? A CYS 133 A CYS 183 1_555 ? ? ? ? ? ? ? 2.068 ? disulf8 disulf ? ? A CYS 125 SG ? ? ? 1_555 A CYS 142 SG ? ? A CYS 146 A CYS 163 1_555 ? ? ? ? ? ? ? 2.098 ? covale1 covale ? ? H NAG . O4 ? ? ? 1_555 I NAG . C1 ? ? A NAG 307 A NAG 308 1_555 ? ? ? ? ? ? ? 1.433 ? covale2 covale ? ? A ASN 94 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 115 A NAG 307 1_555 ? ? ? ? ? ? ? 1.437 ? covale3 covale ? ? A ASN 174 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 195 A NAG 305 1_555 ? ? ? ? ? ? ? 1.449 ? covale4 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 305 A NAG 306 1_555 ? ? ? ? ? ? ? 1.471 ? metalc1 metalc ? ? A SER 83 OG ? ? ? 1_555 C K . K ? ? A SER 104 A K 302 1_555 ? ? ? ? ? ? ? 3.002 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 2 ? B ? 2 ? C ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel B 1 2 ? parallel C 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 ILE A 90 ? GLN A 92 ? ILE A 111 GLN A 113 A 2 GLU A 100 ? PHE A 102 ? GLU A 121 PHE A 123 B 1 VAL A 105 ? LEU A 107 ? VAL A 126 LEU A 128 B 2 TYR A 170 ? VAL A 172 ? TYR A 191 VAL A 193 C 1 HIS A 123 ? THR A 124 ? HIS A 144 THR A 145 C 2 ARG A 149 ? THR A 150 ? ARG A 170 THR A 171 # 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 GLN A 91 ? N GLN A 112 O ARG A 101 ? O ARG A 122 B 1 2 N VAL A 105 ? N VAL A 126 O LYS A 171 ? O LYS A 192 C 1 2 N THR A 124 ? N THR A 145 O ARG A 149 ? O ARG A 170 # 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 ? ? ? ? 19 'BINDING SITE FOR RESIDUE MTX A 301' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE K A 302' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CL A 303' AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 305' AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 306' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 307' AC7 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 308' # 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 19 TYR A 55 ? TYR A 76 . ? 1_555 ? 2 AC1 19 PHE A 57 ? PHE A 78 . ? 1_555 ? 3 AC1 19 ASP A 76 ? ASP A 97 . ? 1_555 ? 4 AC1 19 TYR A 80 ? TYR A 101 . ? 1_555 ? 5 AC1 19 GLN A 95 ? GLN A 116 . ? 1_555 ? 6 AC1 19 TRP A 97 ? TRP A 118 . ? 1_555 ? 7 AC1 19 ARG A 98 ? ARG A 119 . ? 1_555 ? 8 AC1 19 HIS A 130 ? HIS A 151 . ? 1_555 ? 9 AC1 19 ARG A 131 ? ARG A 152 . ? 1_555 ? 10 AC1 19 GLY A 132 ? GLY A 153 . ? 1_555 ? 11 AC1 19 TRP A 133 ? TRP A 154 . ? 1_555 ? 12 AC1 19 TRP A 135 ? TRP A 156 . ? 1_555 ? 13 AC1 19 TRP A 166 ? TRP A 187 . ? 1_555 ? 14 AC1 19 SER A 169 ? SER A 190 . ? 1_555 ? 15 AC1 19 HOH J . ? HOH A 415 . ? 1_555 ? 16 AC1 19 HOH J . ? HOH A 441 . ? 1_555 ? 17 AC1 19 HOH J . ? HOH A 444 . ? 1_555 ? 18 AC1 19 HOH J . ? HOH A 485 . ? 1_555 ? 19 AC1 19 HOH J . ? HOH A 521 . ? 1_555 ? 20 AC2 5 TRP A 33 ? TRP A 54 . ? 1_555 ? 21 AC2 5 SER A 83 ? SER A 104 . ? 1_555 ? 22 AC2 5 ASN A 85 ? ASN A 106 . ? 1_555 ? 23 AC2 5 ASN A 193 ? ASN A 214 . ? 1_555 ? 24 AC2 5 ASN A 195 ? ASN A 216 . ? 1_555 ? 25 AC3 2 ARG A 71 ? ARG A 92 . ? 1_555 ? 26 AC3 2 ARG A 114 ? ARG A 135 . ? 1_555 ? 27 AC4 6 THR A 157 ? THR A 178 . ? 9_554 ? 28 AC4 6 PRO A 158 ? PRO A 179 . ? 9_554 ? 29 AC4 6 ALA A 159 ? ALA A 180 . ? 9_554 ? 30 AC4 6 ASN A 174 ? ASN A 195 . ? 1_555 ? 31 AC4 6 NAG G . ? NAG A 306 . ? 1_555 ? 32 AC4 6 HOH J . ? HOH A 460 . ? 9_554 ? 33 AC5 3 GLN A 113 ? GLN A 134 . ? 9_554 ? 34 AC5 3 TRP A 116 ? TRP A 137 . ? 9_554 ? 35 AC5 3 NAG F . ? NAG A 305 . ? 1_555 ? 36 AC6 3 GLN A 92 ? GLN A 113 . ? 1_555 ? 37 AC6 3 ASN A 94 ? ASN A 115 . ? 1_555 ? 38 AC6 3 NAG I . ? NAG A 308 . ? 1_555 ? 39 AC7 2 ASP A 5 ? ASP A 26 . ? 9_554 ? 40 AC7 2 NAG H . ? NAG A 307 . ? 1_555 ? # _atom_sites.entry_id 4KN0 _atom_sites.fract_transf_matrix[1][1] 0.010246 _atom_sites.fract_transf_matrix[1][2] 0.005915 _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] 0.011831 _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] 0.010063 _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 . ARG A 1 3 ? 13.560 -45.313 -25.323 1.00 44.42 ? 24 ARG A N 1 ATOM 2 C CA . ARG A 1 3 ? 12.443 -44.377 -25.127 1.00 40.44 ? 24 ARG A CA 1 ATOM 3 C C . ARG A 1 3 ? 11.299 -45.005 -24.324 1.00 35.29 ? 24 ARG A C 1 ATOM 4 O O . ARG A 1 3 ? 10.986 -44.548 -23.215 1.00 29.76 ? 24 ARG A O 1 ATOM 5 C CB . ARG A 1 3 ? 11.925 -43.846 -26.464 1.00 43.87 ? 24 ARG A CB 1 ATOM 6 C CG . ARG A 1 3 ? 12.817 -42.767 -27.081 1.00 47.71 ? 24 ARG A CG 1 ATOM 7 C CD . ARG A 1 3 ? 12.187 -42.159 -28.337 1.00 50.09 ? 24 ARG A CD 1 ATOM 8 N NE . ARG A 1 3 ? 11.986 -43.159 -29.369 1.00 53.87 ? 24 ARG A NE 1 ATOM 9 C CZ . ARG A 1 3 ? 12.732 -43.244 -30.460 1.00 62.11 ? 24 ARG A CZ 1 ATOM 10 N NH1 . ARG A 1 3 ? 13.721 -42.380 -30.653 1.00 63.89 ? 24 ARG A NH1 1 ATOM 11 N NH2 . ARG A 1 3 ? 12.491 -44.189 -31.363 1.00 66.74 ? 24 ARG A NH2 1 ATOM 12 N N . THR A 1 4 ? 10.698 -46.077 -24.851 1.00 34.02 ? 25 THR A N 1 ATOM 13 C CA . THR A 1 4 ? 9.616 -46.718 -24.106 1.00 32.46 ? 25 THR A CA 1 ATOM 14 C C . THR A 1 4 ? 10.096 -47.290 -22.774 1.00 31.34 ? 25 THR A C 1 ATOM 15 O O . THR A 1 4 ? 9.329 -47.337 -21.804 1.00 30.95 ? 25 THR A O 1 ATOM 16 C CB . THR A 1 4 ? 8.843 -47.783 -24.928 1.00 47.57 ? 25 THR A CB 1 ATOM 17 O OG1 . THR A 1 4 ? 9.768 -48.699 -25.527 1.00 52.88 ? 25 THR A OG1 1 ATOM 18 C CG2 . THR A 1 4 ? 8.026 -47.115 -26.019 1.00 46.64 ? 25 THR A CG2 1 ATOM 19 N N . ASP A 1 5 ? 11.361 -47.710 -22.726 1.00 31.99 ? 26 ASP A N 1 ATOM 20 C CA . ASP A 1 5 ? 11.991 -48.162 -21.483 1.00 32.32 ? 26 ASP A CA 1 ATOM 21 C C . ASP A 1 5 ? 11.903 -47.171 -20.325 1.00 30.48 ? 26 ASP A C 1 ATOM 22 O O . ASP A 1 5 ? 12.061 -47.556 -19.173 1.00 28.13 ? 26 ASP A O 1 ATOM 23 C CB . ASP A 1 5 ? 13.449 -48.540 -21.742 1.00 37.76 ? 26 ASP A CB 1 ATOM 24 C CG . ASP A 1 5 ? 13.565 -49.831 -22.549 1.00 46.66 ? 26 ASP A CG 1 ATOM 25 O OD1 . ASP A 1 5 ? 12.561 -50.579 -22.574 1.00 49.33 ? 26 ASP A OD1 1 ATOM 26 O OD2 . ASP A 1 5 ? 14.626 -50.092 -23.167 1.00 50.74 ? 26 ASP A OD2 1 ATOM 27 N N . LEU A 1 6 ? 11.638 -45.899 -20.628 1.00 30.82 ? 27 LEU A N 1 ATOM 28 C CA . LEU A 1 6 ? 11.533 -44.855 -19.596 1.00 27.22 ? 27 LEU A CA 1 ATOM 29 C C . LEU A 1 6 ? 10.097 -44.670 -19.038 1.00 22.97 ? 27 LEU A C 1 ATOM 30 O O . LEU A 1 6 ? 9.883 -44.012 -18.022 1.00 20.45 ? 27 LEU A O 1 ATOM 31 C CB . LEU A 1 6 ? 12.077 -43.530 -20.147 1.00 28.25 ? 27 LEU A CB 1 ATOM 32 C CG . LEU A 1 6 ? 13.540 -43.519 -20.640 1.00 31.21 ? 27 LEU A CG 1 ATOM 33 C CD1 . LEU A 1 6 ? 13.897 -42.221 -21.388 1.00 32.44 ? 27 LEU A CD1 1 ATOM 34 C CD2 . LEU A 1 6 ? 14.485 -43.745 -19.464 1.00 30.39 ? 27 LEU A CD2 1 ATOM 35 N N . LEU A 1 7 ? 9.112 -45.258 -19.700 1.00 25.61 ? 28 LEU A N 1 ATOM 36 C CA . LEU A 1 7 ? 7.720 -45.117 -19.264 1.00 20.68 ? 28 LEU A CA 1 ATOM 37 C C . LEU A 1 7 ? 7.350 -46.123 -18.173 1.00 21.44 ? 28 LEU A C 1 ATOM 38 O O . LEU A 1 7 ? 7.784 -47.269 -18.214 1.00 22.27 ? 28 LEU A O 1 ATOM 39 C CB . LEU A 1 7 ? 6.807 -45.309 -20.471 1.00 23.73 ? 28 LEU A CB 1 ATOM 40 C CG . LEU A 1 7 ? 7.261 -44.406 -21.619 1.00 25.09 ? 28 LEU A CG 1 ATOM 41 C CD1 . LEU A 1 7 ? 6.349 -44.542 -22.793 1.00 26.74 ? 28 LEU A CD1 1 ATOM 42 C CD2 . LEU A 1 7 ? 7.362 -42.934 -21.136 1.00 21.44 ? 28 LEU A CD2 1 ATOM 43 N N . ASN A 1 8 ? 6.545 -45.699 -17.205 1.00 19.42 ? 29 ASN A N 1 ATOM 44 C CA . ASN A 1 8 ? 5.936 -46.619 -16.239 1.00 21.20 ? 29 ASN A CA 1 ATOM 45 C C . ASN A 1 8 ? 6.971 -47.481 -15.499 1.00 22.86 ? 29 ASN A C 1 ATOM 46 O O . ASN A 1 8 ? 6.915 -48.709 -15.527 1.00 24.17 ? 29 ASN A O 1 ATOM 47 C CB . ASN A 1 8 ? 4.875 -47.513 -16.926 1.00 21.67 ? 29 ASN A CB 1 ATOM 48 C CG . ASN A 1 8 ? 3.810 -48.030 -15.943 1.00 26.71 ? 29 ASN A CG 1 ATOM 49 O OD1 . ASN A 1 8 ? 3.301 -47.276 -15.095 1.00 26.41 ? 29 ASN A OD1 1 ATOM 50 N ND2 . ASN A 1 8 ? 3.477 -49.326 -16.048 1.00 25.46 ? 29 ASN A ND2 1 ATOM 51 N N . VAL A 1 9 ? 7.903 -46.820 -14.836 1.00 22.61 ? 30 VAL A N 1 ATOM 52 C CA . VAL A 1 9 ? 8.891 -47.501 -14.009 1.00 23.40 ? 30 VAL A CA 1 ATOM 53 C C . VAL A 1 9 ? 8.946 -46.843 -12.633 1.00 22.81 ? 30 VAL A C 1 ATOM 54 O O . VAL A 1 9 ? 8.445 -45.739 -12.438 1.00 22.05 ? 30 VAL A O 1 ATOM 55 C CB . VAL A 1 9 ? 10.290 -47.434 -14.633 1.00 23.92 ? 30 VAL A CB 1 ATOM 56 C CG1 . VAL A 1 9 ? 10.316 -48.136 -16.006 1.00 23.68 ? 30 VAL A CG1 1 ATOM 57 C CG2 . VAL A 1 9 ? 10.733 -45.992 -14.746 1.00 24.69 ? 30 VAL A CG2 1 ATOM 58 N N . CYS A 1 10 ? 9.540 -47.551 -11.684 1.00 22.79 ? 31 CYS A N 1 ATOM 59 C CA . CYS A 1 10 ? 9.790 -47.030 -10.353 1.00 20.25 ? 31 CYS A CA 1 ATOM 60 C C . CYS A 1 10 ? 11.296 -46.974 -10.186 1.00 20.40 ? 31 CYS A C 1 ATOM 61 O O . CYS A 1 10 ? 12.005 -47.913 -10.541 1.00 21.72 ? 31 CYS A O 1 ATOM 62 C CB . CYS A 1 10 ? 9.207 -47.980 -9.312 1.00 19.03 ? 31 CYS A CB 1 ATOM 63 S SG . CYS A 1 10 ? 7.451 -48.121 -9.379 1.00 22.74 ? 31 CYS A SG 1 ATOM 64 N N . MET A 1 11 ? 11.803 -45.895 -9.634 1.00 18.45 ? 32 MET A N 1 ATOM 65 C CA . MET A 1 11 ? 13.242 -45.834 -9.448 1.00 19.07 ? 32 MET A CA 1 ATOM 66 C C . MET A 1 11 ? 13.680 -46.709 -8.277 1.00 18.57 ? 32 MET A C 1 ATOM 67 O O . MET A 1 11 ? 12.889 -47.117 -7.427 1.00 21.88 ? 32 MET A O 1 ATOM 68 C CB . MET A 1 11 ? 13.729 -44.391 -9.286 1.00 23.11 ? 32 MET A CB 1 ATOM 69 C CG . MET A 1 11 ? 13.198 -43.636 -8.081 1.00 23.72 ? 32 MET A CG 1 ATOM 70 S SD . MET A 1 11 ? 14.239 -42.140 -7.801 1.00 37.65 ? 32 MET A SD 1 ATOM 71 C CE . MET A 1 11 ? 13.569 -41.628 -6.219 1.00 25.74 ? 32 MET A CE 1 ATOM 72 N N . ASP A 1 12 ? 14.948 -47.019 -8.268 1.00 18.35 ? 33 ASP A N 1 ATOM 73 C CA . ASP A 1 12 ? 15.522 -47.852 -7.238 1.00 21.87 ? 33 ASP A CA 1 ATOM 74 C C . ASP A 1 12 ? 15.891 -46.893 -6.099 1.00 21.37 ? 33 ASP A C 1 ATOM 75 O O . ASP A 1 12 ? 16.981 -46.294 -6.095 1.00 21.37 ? 33 ASP A O 1 ATOM 76 C CB . ASP A 1 12 ? 16.774 -48.547 -7.827 1.00 22.13 ? 33 ASP A CB 1 ATOM 77 C CG . ASP A 1 12 ? 17.419 -49.541 -6.864 1.00 25.80 ? 33 ASP A CG 1 ATOM 78 O OD1 . ASP A 1 12 ? 17.083 -49.505 -5.657 1.00 26.61 ? 33 ASP A OD1 1 ATOM 79 O OD2 . ASP A 1 12 ? 18.275 -50.339 -7.325 1.00 26.11 ? 33 ASP A OD2 1 ATOM 80 N N . ALA A 1 13 ? 14.979 -46.733 -5.150 1.00 20.96 ? 34 ALA A N 1 ATOM 81 C CA . ALA A 1 13 ? 15.217 -45.869 -3.989 1.00 22.19 ? 34 ALA A CA 1 ATOM 82 C C . ALA A 1 13 ? 14.597 -46.505 -2.747 1.00 23.02 ? 34 ALA A C 1 ATOM 83 O O . ALA A 1 13 ? 14.026 -47.591 -2.820 1.00 23.70 ? 34 ALA A O 1 ATOM 84 C CB . ALA A 1 13 ? 14.700 -44.416 -4.232 1.00 14.05 ? 34 ALA A CB 1 ATOM 85 N N . LYS A 1 14 ? 14.712 -45.832 -1.610 1.00 24.96 ? 35 LYS A N 1 ATOM 86 C CA . LYS A 1 14 ? 14.542 -46.479 -0.307 1.00 25.04 ? 35 LYS A CA 1 ATOM 87 C C . LYS A 1 14 ? 13.244 -47.286 -0.128 1.00 25.16 ? 35 LYS A C 1 ATOM 88 O O . LYS A 1 14 ? 13.281 -48.437 0.339 1.00 23.44 ? 35 LYS A O 1 ATOM 89 C CB . LYS A 1 14 ? 14.641 -45.443 0.819 1.00 23.04 ? 35 LYS A CB 1 ATOM 90 C CG . LYS A 1 14 ? 14.575 -46.091 2.214 1.00 23.37 ? 35 LYS A CG 1 ATOM 91 C CD . LYS A 1 14 ? 14.930 -45.093 3.293 1.00 22.53 ? 35 LYS A CD 1 ATOM 92 C CE . LYS A 1 14 ? 14.808 -45.707 4.672 1.00 25.28 ? 35 LYS A CE 1 ATOM 93 N NZ . LYS A 1 14 ? 15.054 -44.704 5.745 1.00 26.18 ? 35 LYS A NZ 1 ATOM 94 N N . HIS A 1 15 ? 12.112 -46.674 -0.489 1.00 20.09 ? 36 HIS A N 1 ATOM 95 C CA . HIS A 1 15 ? 10.806 -47.252 -0.217 1.00 21.91 ? 36 HIS A CA 1 ATOM 96 C C . HIS A 1 15 ? 10.046 -47.696 -1.482 1.00 21.88 ? 36 HIS A C 1 ATOM 97 O O . HIS A 1 15 ? 9.029 -48.376 -1.392 1.00 20.70 ? 36 HIS A O 1 ATOM 98 C CB . HIS A 1 15 ? 9.935 -46.290 0.603 1.00 20.86 ? 36 HIS A CB 1 ATOM 99 C CG . HIS A 1 15 ? 10.524 -45.928 1.933 1.00 21.42 ? 36 HIS A CG 1 ATOM 100 N ND1 . HIS A 1 15 ? 10.552 -46.801 3.000 1.00 22.68 ? 36 HIS A ND1 1 ATOM 101 C CD2 . HIS A 1 15 ? 11.097 -44.778 2.373 1.00 19.08 ? 36 HIS A CD2 1 ATOM 102 C CE1 . HIS A 1 15 ? 11.128 -46.212 4.036 1.00 22.44 ? 36 HIS A CE1 1 ATOM 103 N NE2 . HIS A 1 15 ? 11.451 -44.979 3.687 1.00 20.95 ? 36 HIS A NE2 1 ATOM 104 N N . HIS A 1 16 ? 10.563 -47.350 -2.653 1.00 21.10 ? 37 HIS A N 1 ATOM 105 C CA . HIS A 1 16 ? 9.856 -47.657 -3.891 1.00 20.00 ? 37 HIS A CA 1 ATOM 106 C C . HIS A 1 16 ? 9.591 -49.124 -4.090 1.00 17.93 ? 37 HIS A C 1 ATOM 107 O O . HIS A 1 16 ? 10.456 -49.954 -3.842 1.00 17.60 ? 37 HIS A O 1 ATOM 108 C CB . HIS A 1 16 ? 10.616 -47.128 -5.103 1.00 20.34 ? 37 HIS A CB 1 ATOM 109 C CG . HIS A 1 16 ? 10.475 -45.653 -5.277 1.00 18.60 ? 37 HIS A CG 1 ATOM 110 N ND1 . HIS A 1 16 ? 10.989 -44.752 -4.373 1.00 16.60 ? 37 HIS A ND1 1 ATOM 111 C CD2 . HIS A 1 16 ? 9.835 -44.926 -6.220 1.00 19.22 ? 37 HIS A CD2 1 ATOM 112 C CE1 . HIS A 1 16 ? 10.681 -43.529 -4.762 1.00 16.61 ? 37 HIS A CE1 1 ATOM 113 N NE2 . HIS A 1 16 ? 9.971 -43.606 -5.875 1.00 17.41 ? 37 HIS A NE2 1 ATOM 114 N N . LYS A 1 17 ? 8.382 -49.423 -4.555 1.00 18.19 ? 38 LYS A N 1 ATOM 115 C CA . LYS A 1 17 ? 8.085 -50.725 -5.138 1.00 21.90 ? 38 LYS A CA 1 ATOM 116 C C . LYS A 1 17 ? 9.002 -51.006 -6.341 1.00 19.77 ? 38 LYS A C 1 ATOM 117 O O . LYS A 1 17 ? 9.522 -50.088 -6.969 1.00 20.32 ? 38 LYS A O 1 ATOM 118 C CB . LYS A 1 17 ? 6.614 -50.787 -5.580 1.00 22.81 ? 38 LYS A CB 1 ATOM 119 C CG . LYS A 1 17 ? 5.610 -50.717 -4.441 1.00 24.73 ? 38 LYS A CG 1 ATOM 120 C CD . LYS A 1 17 ? 4.218 -51.184 -4.861 1.00 24.45 ? 38 LYS A CD 1 ATOM 121 C CE . LYS A 1 17 ? 3.598 -50.229 -5.844 1.00 23.09 ? 38 LYS A CE 1 ATOM 122 N NZ . LYS A 1 17 ? 2.305 -50.751 -6.439 1.00 27.32 ? 38 LYS A NZ 1 ATOM 123 N N . THR A 1 18 ? 9.182 -52.277 -6.670 1.00 21.23 ? 39 THR A N 1 ATOM 124 C CA . THR A 1 18 ? 9.973 -52.684 -7.833 1.00 24.54 ? 39 THR A CA 1 ATOM 125 C C . THR A 1 18 ? 9.386 -52.196 -9.167 1.00 25.19 ? 39 THR A C 1 ATOM 126 O O . THR A 1 18 ? 10.129 -51.843 -10.080 1.00 25.62 ? 39 THR A O 1 ATOM 127 C CB . THR A 1 18 ? 10.087 -54.215 -7.905 1.00 32.69 ? 39 THR A CB 1 ATOM 128 O OG1 . THR A 1 18 ? 10.588 -54.716 -6.656 1.00 35.87 ? 39 THR A OG1 1 ATOM 129 C CG2 . THR A 1 18 ? 11.037 -54.610 -9.024 1.00 36.35 ? 39 THR A CG2 1 ATOM 130 N N . LYS A 1 19 ? 8.060 -52.191 -9.267 1.00 25.10 ? 40 LYS A N 1 ATOM 131 C CA . LYS A 1 19 ? 7.327 -51.877 -10.509 1.00 26.87 ? 40 LYS A CA 1 ATOM 132 C C . LYS A 1 19 ? 5.999 -51.200 -10.150 1.00 24.30 ? 40 LYS A C 1 ATOM 133 O O . LYS A 1 19 ? 5.468 -51.445 -9.069 1.00 23.46 ? 40 LYS A O 1 ATOM 134 C CB . LYS A 1 19 ? 7.042 -53.176 -11.319 1.00 25.16 ? 40 LYS A CB 1 ATOM 135 N N . PRO A 1 20 ? 5.458 -50.363 -11.055 1.00 23.30 ? 41 PRO A N 1 ATOM 136 C CA . PRO A 1 20 ? 4.203 -49.667 -10.752 1.00 22.51 ? 41 PRO A CA 1 ATOM 137 C C . PRO A 1 20 ? 3.056 -50.664 -10.731 1.00 25.45 ? 41 PRO A C 1 ATOM 138 O O . PRO A 1 20 ? 3.113 -51.672 -11.428 1.00 26.54 ? 41 PRO A O 1 ATOM 139 C CB . PRO A 1 20 ? 4.035 -48.708 -11.950 1.00 22.18 ? 41 PRO A CB 1 ATOM 140 C CG . PRO A 1 20 ? 5.455 -48.423 -12.400 1.00 23.12 ? 41 PRO A CG 1 ATOM 141 C CD . PRO A 1 20 ? 6.102 -49.816 -12.264 1.00 25.65 ? 41 PRO A CD 1 ATOM 142 N N . GLY A 1 21 ? 2.016 -50.368 -9.960 1.00 26.26 ? 42 GLY A N 1 ATOM 143 C CA . GLY A 1 21 ? 0.850 -51.223 -9.885 1.00 28.10 ? 42 GLY A CA 1 ATOM 144 C C . GLY A 1 21 ? -0.216 -50.526 -9.065 1.00 30.28 ? 42 GLY A C 1 ATOM 145 O O . GLY A 1 21 ? 0.075 -49.534 -8.370 1.00 28.65 ? 42 GLY A O 1 ATOM 146 N N . PRO A 1 22 ? -1.450 -51.044 -9.124 1.00 26.84 ? 43 PRO A N 1 ATOM 147 C CA . PRO A 1 22 ? -2.565 -50.359 -8.468 1.00 27.11 ? 43 PRO A CA 1 ATOM 148 C C . PRO A 1 22 ? -2.461 -50.435 -6.953 1.00 27.16 ? 43 PRO A C 1 ATOM 149 O O . PRO A 1 22 ? -1.961 -51.427 -6.413 1.00 28.24 ? 43 PRO A O 1 ATOM 150 C CB . PRO A 1 22 ? -3.799 -51.131 -8.954 1.00 28.21 ? 43 PRO A CB 1 ATOM 151 C CG . PRO A 1 22 ? -3.317 -51.995 -10.098 1.00 31.79 ? 43 PRO A CG 1 ATOM 152 C CD . PRO A 1 22 ? -1.872 -52.265 -9.833 1.00 29.30 ? 43 PRO A CD 1 ATOM 153 N N . GLU A 1 23 ? -2.913 -49.382 -6.286 1.00 25.39 ? 44 GLU A N 1 ATOM 154 C CA . GLU A 1 23 ? -2.957 -49.327 -4.820 1.00 26.26 ? 44 GLU A CA 1 ATOM 155 C C . GLU A 1 23 ? -4.240 -48.624 -4.397 1.00 28.14 ? 44 GLU A C 1 ATOM 156 O O . GLU A 1 23 ? -4.277 -47.393 -4.195 1.00 24.91 ? 44 GLU A O 1 ATOM 157 C CB . GLU A 1 23 ? -1.765 -48.566 -4.266 1.00 23.15 ? 44 GLU A CB 1 ATOM 158 C CG . GLU A 1 23 ? -0.426 -49.167 -4.639 1.00 25.41 ? 44 GLU A CG 1 ATOM 159 C CD . GLU A 1 23 ? -0.147 -50.480 -3.897 1.00 28.96 ? 44 GLU A CD 1 ATOM 160 O OE1 . GLU A 1 23 ? 0.922 -51.086 -4.175 1.00 30.17 ? 44 GLU A OE1 1 ATOM 161 O OE2 . GLU A 1 23 ? -0.975 -50.888 -3.033 1.00 29.77 ? 44 GLU A OE2 1 ATOM 162 N N . ASP A 1 24 ? -5.294 -49.409 -4.274 1.00 28.74 ? 45 ASP A N 1 ATOM 163 C CA . ASP A 1 24 ? -6.606 -48.850 -4.011 1.00 35.00 ? 45 ASP A CA 1 ATOM 164 C C . ASP A 1 24 ? -6.677 -48.090 -2.678 1.00 33.65 ? 45 ASP A C 1 ATOM 165 O O . ASP A 1 24 ? -7.579 -47.280 -2.462 1.00 34.89 ? 45 ASP A O 1 ATOM 166 C CB . ASP A 1 24 ? -7.647 -49.958 -4.038 1.00 41.36 ? 45 ASP A CB 1 ATOM 167 C CG . ASP A 1 24 ? -9.027 -49.455 -3.699 1.00 50.66 ? 45 ASP A CG 1 ATOM 168 O OD1 . ASP A 1 24 ? -9.636 -48.784 -4.565 1.00 52.80 ? 45 ASP A OD1 1 ATOM 169 O OD2 . ASP A 1 24 ? -9.510 -49.734 -2.573 1.00 55.14 ? 45 ASP A OD2 1 ATOM 170 N N . LYS A 1 25 ? -5.732 -48.373 -1.790 1.00 29.67 ? 46 LYS A N 1 ATOM 171 C CA . LYS A 1 25 ? -5.784 -47.870 -0.422 1.00 28.73 ? 46 LYS A CA 1 ATOM 172 C C . LYS A 1 25 ? -4.771 -46.737 -0.119 1.00 26.35 ? 46 LYS A C 1 ATOM 173 O O . LYS A 1 25 ? -4.572 -46.394 1.037 1.00 26.23 ? 46 LYS A O 1 ATOM 174 C CB . LYS A 1 25 ? -5.637 -49.054 0.594 1.00 28.89 ? 46 LYS A CB 1 ATOM 175 N N . LEU A 1 26 ? -4.148 -46.160 -1.149 1.00 25.09 ? 47 LEU A N 1 ATOM 176 C CA . LEU A 1 26 ? -3.322 -44.949 -0.964 1.00 24.52 ? 47 LEU A CA 1 ATOM 177 C C . LEU A 1 26 ? -4.071 -43.907 -0.105 1.00 26.54 ? 47 LEU A C 1 ATOM 178 O O . LEU A 1 26 ? -5.261 -43.619 -0.328 1.00 27.09 ? 47 LEU A O 1 ATOM 179 C CB . LEU A 1 26 ? -2.863 -44.338 -2.312 1.00 18.86 ? 47 LEU A CB 1 ATOM 180 C CG . LEU A 1 26 ? -1.918 -45.174 -3.202 1.00 20.29 ? 47 LEU A CG 1 ATOM 181 C CD1 . LEU A 1 26 ? -1.333 -44.351 -4.381 1.00 14.90 ? 47 LEU A CD1 1 ATOM 182 C CD2 . LEU A 1 26 ? -0.757 -45.823 -2.378 1.00 21.55 ? 47 LEU A CD2 1 ATOM 183 N N . HIS A 1 27 ? -3.355 -43.358 0.872 1.00 24.68 ? 48 HIS A N 1 ATOM 184 C CA . HIS A 1 27 ? -3.915 -42.471 1.882 1.00 26.42 ? 48 HIS A CA 1 ATOM 185 C C . HIS A 1 27 ? -3.995 -40.991 1.437 1.00 23.72 ? 48 HIS A C 1 ATOM 186 O O . HIS A 1 27 ? -3.083 -40.448 0.775 1.00 17.97 ? 48 HIS A O 1 ATOM 187 C CB . HIS A 1 27 ? -3.093 -42.591 3.169 1.00 26.58 ? 48 HIS A CB 1 ATOM 188 C CG . HIS A 1 27 ? -3.630 -41.804 4.322 1.00 28.02 ? 48 HIS A CG 1 ATOM 189 N ND1 . HIS A 1 27 ? -3.076 -40.607 4.730 1.00 28.96 ? 48 HIS A ND1 1 ATOM 190 C CD2 . HIS A 1 27 ? -4.650 -42.057 5.175 1.00 29.09 ? 48 HIS A CD2 1 ATOM 191 C CE1 . HIS A 1 27 ? -3.741 -40.151 5.777 1.00 29.22 ? 48 HIS A CE1 1 ATOM 192 N NE2 . HIS A 1 27 ? -4.699 -41.014 6.068 1.00 30.88 ? 48 HIS A NE2 1 ATOM 193 N N . ASP A 1 28 ? -5.128 -40.385 1.775 1.00 24.32 ? 49 ASP A N 1 ATOM 194 C CA . ASP A 1 28 ? -5.337 -38.942 1.688 1.00 22.90 ? 49 ASP A CA 1 ATOM 195 C C . ASP A 1 28 ? -4.769 -38.294 0.433 1.00 21.13 ? 49 ASP A C 1 ATOM 196 O O . ASP A 1 28 ? -5.255 -38.544 -0.680 1.00 21.90 ? 49 ASP A O 1 ATOM 197 C CB . ASP A 1 28 ? -4.805 -38.262 2.951 1.00 25.04 ? 49 ASP A CB 1 ATOM 198 C CG . ASP A 1 28 ? -5.334 -36.837 3.103 1.00 28.37 ? 49 ASP A CG 1 ATOM 199 O OD1 . ASP A 1 28 ? -6.162 -36.446 2.256 1.00 28.67 ? 49 ASP A OD1 1 ATOM 200 O OD2 . ASP A 1 28 ? -4.927 -36.118 4.043 1.00 26.26 ? 49 ASP A OD2 1 ATOM 201 N N . GLN A 1 29 ? -3.743 -37.464 0.597 1.00 19.91 ? 50 GLN A N 1 ATOM 202 C CA . GLN A 1 29 ? -3.230 -36.663 -0.524 1.00 17.27 ? 50 GLN A CA 1 ATOM 203 C C . GLN A 1 29 ? -2.605 -37.511 -1.640 1.00 17.54 ? 50 GLN A C 1 ATOM 204 O O . GLN A 1 29 ? -2.481 -37.035 -2.774 1.00 17.89 ? 50 GLN A O 1 ATOM 205 C CB . GLN A 1 29 ? -2.218 -35.596 -0.049 1.00 18.30 ? 50 GLN A CB 1 ATOM 206 C CG . GLN A 1 29 ? -2.847 -34.484 0.766 1.00 19.16 ? 50 GLN A CG 1 ATOM 207 C CD . GLN A 1 29 ? -1.854 -33.380 1.141 1.00 20.33 ? 50 GLN A CD 1 ATOM 208 O OE1 . GLN A 1 29 ? -1.749 -33.015 2.316 1.00 19.13 ? 50 GLN A OE1 1 ATOM 209 N NE2 . GLN A 1 29 ? -1.128 -32.838 0.138 1.00 16.10 ? 50 GLN A NE2 1 ATOM 210 N N . CYS A 1 30 ? -2.201 -38.743 -1.333 1.00 16.84 ? 51 CYS A N 1 ATOM 211 C CA . CYS A 1 30 ? -1.659 -39.649 -2.367 1.00 16.78 ? 51 CYS A CA 1 ATOM 212 C C . CYS A 1 30 ? -2.759 -40.433 -3.156 1.00 17.34 ? 51 CYS A C 1 ATOM 213 O O . CYS A 1 30 ? -2.469 -41.136 -4.129 1.00 18.16 ? 51 CYS A O 1 ATOM 214 C CB . CYS A 1 30 ? -0.639 -40.633 -1.761 1.00 16.27 ? 51 CYS A CB 1 ATOM 215 S SG . CYS A 1 30 ? 0.747 -39.883 -0.841 1.00 20.55 ? 51 CYS A SG 1 ATOM 216 N N . SER A 1 31 ? -4.019 -40.296 -2.759 1.00 20.05 ? 52 SER A N 1 ATOM 217 C CA . SER A 1 31 ? -5.085 -41.047 -3.417 1.00 19.05 ? 52 SER A CA 1 ATOM 218 C C . SER A 1 31 ? -5.218 -40.868 -4.949 1.00 21.68 ? 52 SER A C 1 ATOM 219 O O . SER A 1 31 ? -5.696 -41.801 -5.621 1.00 20.85 ? 52 SER A O 1 ATOM 220 C CB . SER A 1 31 ? -6.439 -40.835 -2.722 1.00 21.89 ? 52 SER A CB 1 ATOM 221 O OG . SER A 1 31 ? -6.943 -39.547 -2.976 1.00 21.53 ? 52 SER A OG 1 ATOM 222 N N . PRO A 1 32 ? -4.789 -39.698 -5.516 1.00 19.82 ? 53 PRO A N 1 ATOM 223 C CA . PRO A 1 32 ? -4.870 -39.505 -6.989 1.00 20.53 ? 53 PRO A CA 1 ATOM 224 C C . PRO A 1 32 ? -3.962 -40.461 -7.797 1.00 19.44 ? 53 PRO A C 1 ATOM 225 O O . PRO A 1 32 ? -4.171 -40.665 -9.024 1.00 16.74 ? 53 PRO A O 1 ATOM 226 C CB . PRO A 1 32 ? -4.410 -38.040 -7.191 1.00 20.05 ? 53 PRO A CB 1 ATOM 227 C CG . PRO A 1 32 ? -4.758 -37.355 -5.881 1.00 18.25 ? 53 PRO A CG 1 ATOM 228 C CD . PRO A 1 32 ? -4.410 -38.451 -4.830 1.00 17.89 ? 53 PRO A CD 1 ATOM 229 N N . TRP A 1 33 ? -2.974 -41.029 -7.111 1.00 15.16 ? 54 TRP A N 1 ATOM 230 C CA . TRP A 1 33 ? -2.078 -42.032 -7.701 1.00 17.70 ? 54 TRP A CA 1 ATOM 231 C C . TRP A 1 33 ? -2.614 -43.478 -7.586 1.00 20.52 ? 54 TRP A C 1 ATOM 232 O O . TRP A 1 33 ? -1.915 -44.430 -7.961 1.00 19.79 ? 54 TRP A O 1 ATOM 233 C CB . TRP A 1 33 ? -0.702 -41.977 -7.015 1.00 17.17 ? 54 TRP A CB 1 ATOM 234 C CG . TRP A 1 33 ? 0.166 -40.804 -7.454 1.00 19.63 ? 54 TRP A CG 1 ATOM 235 C CD1 . TRP A 1 33 ? 1.053 -40.800 -8.477 1.00 20.09 ? 54 TRP A CD1 1 ATOM 236 C CD2 . TRP A 1 33 ? 0.220 -39.498 -6.872 1.00 17.74 ? 54 TRP A CD2 1 ATOM 237 N NE1 . TRP A 1 33 ? 1.656 -39.576 -8.578 1.00 18.29 ? 54 TRP A NE1 1 ATOM 238 C CE2 . TRP A 1 33 ? 1.155 -38.747 -7.618 1.00 18.33 ? 54 TRP A CE2 1 ATOM 239 C CE3 . TRP A 1 33 ? -0.440 -38.880 -5.812 1.00 20.02 ? 54 TRP A CE3 1 ATOM 240 C CZ2 . TRP A 1 33 ? 1.459 -37.416 -7.329 1.00 14.91 ? 54 TRP A CZ2 1 ATOM 241 C CZ3 . TRP A 1 33 ? -0.140 -37.548 -5.526 1.00 18.25 ? 54 TRP A CZ3 1 ATOM 242 C CH2 . TRP A 1 33 ? 0.812 -36.841 -6.281 1.00 16.39 ? 54 TRP A CH2 1 ATOM 243 N N . LYS A 1 34 ? -3.849 -43.641 -7.096 1.00 21.42 ? 55 LYS A N 1 ATOM 244 C CA . LYS A 1 34 ? -4.317 -44.964 -6.688 1.00 21.72 ? 55 LYS A CA 1 ATOM 245 C C . LYS A 1 34 ? -4.462 -45.966 -7.832 1.00 23.95 ? 55 LYS A C 1 ATOM 246 O O . LYS A 1 34 ? -4.468 -47.154 -7.590 1.00 26.55 ? 55 LYS A O 1 ATOM 247 C CB . LYS A 1 34 ? -5.623 -44.893 -5.877 1.00 21.47 ? 55 LYS A CB 1 ATOM 248 C CG . LYS A 1 34 ? -6.862 -44.564 -6.711 1.00 24.08 ? 55 LYS A CG 1 ATOM 249 C CD . LYS A 1 34 ? -8.109 -44.540 -5.828 1.00 28.76 ? 55 LYS A CD 1 ATOM 250 C CE . LYS A 1 34 ? -9.199 -43.693 -6.433 1.00 33.82 ? 55 LYS A CE 1 ATOM 251 N NZ . LYS A 1 34 ? -10.539 -44.030 -5.878 1.00 39.18 ? 55 LYS A NZ 1 ATOM 252 N N . LYS A 1 35 ? -4.588 -45.502 -9.064 1.00 25.06 ? 56 LYS A N 1 ATOM 253 C CA . LYS A 1 35 ? -4.726 -46.432 -10.179 1.00 29.31 ? 56 LYS A CA 1 ATOM 254 C C . LYS A 1 35 ? -3.358 -46.999 -10.591 1.00 28.98 ? 56 LYS A C 1 ATOM 255 O O . LYS A 1 35 ? -3.275 -48.081 -11.159 1.00 27.27 ? 56 LYS A O 1 ATOM 256 C CB . LYS A 1 35 ? -5.438 -45.785 -11.365 1.00 34.08 ? 56 LYS A CB 1 ATOM 257 C CG . LYS A 1 35 ? -6.904 -45.450 -11.098 1.00 40.06 ? 56 LYS A CG 1 ATOM 258 C CD . LYS A 1 35 ? -7.706 -46.713 -10.794 1.00 45.69 ? 56 LYS A CD 1 ATOM 259 C CE . LYS A 1 35 ? -8.834 -46.449 -9.784 1.00 48.68 ? 56 LYS A CE 1 ATOM 260 N NZ . LYS A 1 35 ? -10.089 -45.911 -10.388 1.00 50.10 ? 56 LYS A NZ 1 ATOM 261 N N . ASN A 1 36 ? -2.279 -46.276 -10.280 1.00 26.68 ? 57 ASN A N 1 ATOM 262 C CA . ASN A 1 36 ? -0.961 -46.723 -10.710 1.00 24.21 ? 57 ASN A CA 1 ATOM 263 C C . ASN A 1 36 ? 0.145 -45.999 -9.966 1.00 22.19 ? 57 ASN A C 1 ATOM 264 O O . ASN A 1 36 ? 0.370 -44.799 -10.187 1.00 20.37 ? 57 ASN A O 1 ATOM 265 C CB . ASN A 1 36 ? -0.815 -46.500 -12.210 1.00 25.68 ? 57 ASN A CB 1 ATOM 266 C CG . ASN A 1 36 ? 0.325 -47.311 -12.816 1.00 25.59 ? 57 ASN A CG 1 ATOM 267 O OD1 . ASN A 1 36 ? 0.616 -48.424 -12.382 1.00 24.18 ? 57 ASN A OD1 1 ATOM 268 N ND2 . ASN A 1 36 ? 0.962 -46.755 -13.828 1.00 25.88 ? 57 ASN A ND2 1 ATOM 269 N N . ALA A 1 37 ? 0.809 -46.722 -9.070 1.00 20.08 ? 58 ALA A N 1 ATOM 270 C CA . ALA A 1 37 ? 1.673 -46.089 -8.070 1.00 21.77 ? 58 ALA A CA 1 ATOM 271 C C . ALA A 1 37 ? 2.935 -46.889 -7.792 1.00 24.81 ? 58 ALA A C 1 ATOM 272 O O . ALA A 1 37 ? 2.907 -48.110 -7.883 1.00 16.88 ? 58 ALA A O 1 ATOM 273 C CB . ALA A 1 37 ? 0.926 -45.943 -6.784 1.00 22.08 ? 58 ALA A CB 1 ATOM 274 N N . CYS A 1 38 ? 4.005 -46.176 -7.411 1.00 21.23 ? 59 CYS A N 1 ATOM 275 C CA . CYS A 1 38 ? 5.268 -46.761 -6.993 1.00 23.84 ? 59 CYS A CA 1 ATOM 276 C C . CYS A 1 38 ? 5.373 -46.860 -5.476 1.00 25.47 ? 59 CYS A C 1 ATOM 277 O O . CYS A 1 38 ? 6.404 -47.336 -4.947 1.00 24.25 ? 59 CYS A O 1 ATOM 278 C CB . CYS A 1 38 ? 6.440 -45.889 -7.505 1.00 21.50 ? 59 CYS A CB 1 ATOM 279 S SG . CYS A 1 38 ? 6.766 -46.154 -9.254 1.00 21.80 ? 59 CYS A SG 1 ATOM 280 N N . CYS A 1 39 ? 4.343 -46.370 -4.782 1.00 15.39 ? 60 CYS A N 1 ATOM 281 C CA . CYS A 1 39 ? 4.357 -46.364 -3.320 1.00 22.15 ? 60 CYS A CA 1 ATOM 282 C C . CYS A 1 39 ? 3.334 -47.350 -2.797 1.00 21.81 ? 60 CYS A C 1 ATOM 283 O O . CYS A 1 39 ? 2.311 -47.538 -3.430 1.00 23.38 ? 60 CYS A O 1 ATOM 284 C CB . CYS A 1 39 ? 4.046 -44.957 -2.778 1.00 19.88 ? 60 CYS A CB 1 ATOM 285 S SG . CYS A 1 39 ? 2.392 -44.327 -3.209 1.00 22.92 ? 60 CYS A SG 1 ATOM 286 N N . THR A 1 40 ? 3.624 -47.986 -1.662 1.00 20.61 ? 61 THR A N 1 ATOM 287 C CA . THR A 1 40 ? 2.668 -48.853 -0.992 1.00 22.49 ? 61 THR A CA 1 ATOM 288 C C . THR A 1 40 ? 1.641 -48.021 -0.201 1.00 24.37 ? 61 THR A C 1 ATOM 289 O O . THR A 1 40 ? 1.868 -46.838 0.104 1.00 23.11 ? 61 THR A O 1 ATOM 290 C CB . THR A 1 40 ? 3.376 -49.817 -0.020 1.00 24.63 ? 61 THR A CB 1 ATOM 291 O OG1 . THR A 1 40 ? 4.098 -49.062 0.958 1.00 24.03 ? 61 THR A OG1 1 ATOM 292 C CG2 . THR A 1 40 ? 4.369 -50.737 -0.760 1.00 24.83 ? 61 THR A CG2 1 ATOM 293 N N . ALA A 1 41 ? 0.518 -48.641 0.146 1.00 24.54 ? 62 ALA A N 1 ATOM 294 C CA . ALA A 1 41 ? -0.469 -47.964 0.977 1.00 24.00 ? 62 ALA A CA 1 ATOM 295 C C . ALA A 1 41 ? 0.183 -47.500 2.286 1.00 24.75 ? 62 ALA A C 1 ATOM 296 O O . ALA A 1 41 ? -0.014 -46.356 2.733 1.00 22.29 ? 62 ALA A O 1 ATOM 297 C CB . ALA A 1 41 ? -1.643 -48.903 1.270 1.00 22.76 ? 62 ALA A CB 1 ATOM 298 N N . SER A 1 42 ? 0.972 -48.387 2.894 1.00 22.65 ? 63 SER A N 1 ATOM 299 C CA . SER A 1 42 ? 1.639 -48.053 4.147 1.00 24.96 ? 63 SER A CA 1 ATOM 300 C C . SER A 1 42 ? 2.615 -46.842 4.046 1.00 23.04 ? 63 SER A C 1 ATOM 301 O O . SER A 1 42 ? 2.623 -45.994 4.925 1.00 23.46 ? 63 SER A O 1 ATOM 302 C CB . SER A 1 42 ? 2.280 -49.316 4.762 1.00 29.78 ? 63 SER A CB 1 ATOM 303 O OG . SER A 1 42 ? 3.598 -49.117 5.215 1.00 34.22 ? 63 SER A OG 1 ATOM 304 N N . THR A 1 43 ? 3.413 -46.771 2.985 1.00 20.40 ? 64 THR A N 1 ATOM 305 C CA . THR A 1 43 ? 4.225 -45.591 2.712 1.00 22.74 ? 64 THR A CA 1 ATOM 306 C C . THR A 1 43 ? 3.358 -44.314 2.626 1.00 21.99 ? 64 THR A C 1 ATOM 307 O O . THR A 1 43 ? 3.690 -43.282 3.225 1.00 22.76 ? 64 THR A O 1 ATOM 308 C CB . THR A 1 43 ? 5.025 -45.749 1.369 1.00 24.22 ? 64 THR A CB 1 ATOM 309 O OG1 . THR A 1 43 ? 6.021 -46.778 1.502 1.00 24.63 ? 64 THR A OG1 1 ATOM 310 C CG2 . THR A 1 43 ? 5.693 -44.443 0.972 1.00 20.35 ? 64 THR A CG2 1 ATOM 311 N N . SER A 1 44 ? 2.254 -44.393 1.890 1.00 20.06 ? 65 SER A N 1 ATOM 312 C CA . SER A 1 44 ? 1.415 -43.222 1.639 1.00 21.81 ? 65 SER A CA 1 ATOM 313 C C . SER A 1 44 ? 0.841 -42.735 2.958 1.00 23.11 ? 65 SER A C 1 ATOM 314 O O . SER A 1 44 ? 0.730 -41.551 3.195 1.00 23.56 ? 65 SER A O 1 ATOM 315 C CB . SER A 1 44 ? 0.285 -43.554 0.672 1.00 22.52 ? 65 SER A CB 1 ATOM 316 O OG . SER A 1 44 ? -0.752 -44.289 1.314 1.00 21.02 ? 65 SER A OG 1 ATOM 317 N N . GLN A 1 45 ? 0.509 -43.676 3.824 1.00 21.38 ? 66 GLN A N 1 ATOM 318 C CA . GLN A 1 45 ? 0.013 -43.353 5.139 1.00 25.88 ? 66 GLN A CA 1 ATOM 319 C C . GLN A 1 45 ? 1.082 -42.693 6.019 1.00 25.75 ? 66 GLN A C 1 ATOM 320 O O . GLN A 1 45 ? 0.844 -41.679 6.653 1.00 29.06 ? 66 GLN A O 1 ATOM 321 C CB . GLN A 1 45 ? -0.469 -44.631 5.807 1.00 28.62 ? 66 GLN A CB 1 ATOM 322 C CG . GLN A 1 45 ? -1.457 -44.406 6.866 1.00 35.97 ? 66 GLN A CG 1 ATOM 323 C CD . GLN A 1 45 ? -2.143 -45.712 7.281 1.00 43.95 ? 66 GLN A CD 1 ATOM 324 O OE1 . GLN A 1 45 ? -1.718 -46.817 6.886 1.00 45.43 ? 66 GLN A OE1 1 ATOM 325 N NE2 . GLN A 1 45 ? -3.216 -45.587 8.058 1.00 45.42 ? 66 GLN A NE2 1 ATOM 326 N N . GLU A 1 46 ? 2.257 -43.283 6.062 1.00 21.45 ? 67 GLU A N 1 ATOM 327 C CA . GLU A 1 46 ? 3.284 -42.800 6.967 1.00 24.59 ? 67 GLU A CA 1 ATOM 328 C C . GLU A 1 46 ? 3.769 -41.412 6.534 1.00 21.98 ? 67 GLU A C 1 ATOM 329 O O . GLU A 1 46 ? 4.092 -40.589 7.372 1.00 23.19 ? 67 GLU A O 1 ATOM 330 C CB . GLU A 1 46 ? 4.453 -43.794 7.031 1.00 25.40 ? 67 GLU A CB 1 ATOM 331 C CG . GLU A 1 46 ? 5.550 -43.382 7.975 1.00 27.61 ? 67 GLU A CG 1 ATOM 332 C CD . GLU A 1 46 ? 5.114 -43.379 9.442 1.00 32.99 ? 67 GLU A CD 1 ATOM 333 O OE1 . GLU A 1 46 ? 4.079 -44.018 9.767 1.00 34.60 ? 67 GLU A OE1 1 ATOM 334 O OE2 . GLU A 1 46 ? 5.819 -42.742 10.271 1.00 34.80 ? 67 GLU A OE2 1 ATOM 335 N N . LEU A 1 47 ? 3.764 -41.145 5.231 1.00 20.66 ? 68 LEU A N 1 ATOM 336 C CA . LEU A 1 47 ? 4.343 -39.892 4.736 1.00 25.18 ? 68 LEU A CA 1 ATOM 337 C C . LEU A 1 47 ? 3.540 -38.643 5.100 1.00 25.53 ? 68 LEU A C 1 ATOM 338 O O . LEU A 1 47 ? 4.078 -37.536 5.041 1.00 23.38 ? 68 LEU A O 1 ATOM 339 C CB . LEU A 1 47 ? 4.646 -39.936 3.242 1.00 23.42 ? 68 LEU A CB 1 ATOM 340 C CG . LEU A 1 47 ? 3.453 -39.881 2.292 1.00 24.84 ? 68 LEU A CG 1 ATOM 341 C CD1 . LEU A 1 47 ? 2.966 -38.449 2.037 1.00 23.53 ? 68 LEU A CD1 1 ATOM 342 C CD2 . LEU A 1 47 ? 3.884 -40.530 1.007 1.00 23.46 ? 68 LEU A CD2 1 ATOM 343 N N . HIS A 1 48 ? 2.283 -38.813 5.519 1.00 22.95 ? 69 HIS A N 1 ATOM 344 C CA . HIS A 1 48 ? 1.490 -37.675 6.013 1.00 25.16 ? 69 HIS A CA 1 ATOM 345 C C . HIS A 1 48 ? 1.891 -37.193 7.424 1.00 28.71 ? 69 HIS A C 1 ATOM 346 O O . HIS A 1 48 ? 1.524 -36.099 7.843 1.00 28.26 ? 69 HIS A O 1 ATOM 347 C CB . HIS A 1 48 ? -0.030 -37.970 5.950 1.00 23.89 ? 69 HIS A CB 1 ATOM 348 C CG . HIS A 1 48 ? -0.564 -38.008 4.555 1.00 22.69 ? 69 HIS A CG 1 ATOM 349 N ND1 . HIS A 1 48 ? -0.163 -38.955 3.640 1.00 22.54 ? 69 HIS A ND1 1 ATOM 350 C CD2 . HIS A 1 48 ? -1.433 -37.195 3.902 1.00 24.53 ? 69 HIS A CD2 1 ATOM 351 C CE1 . HIS A 1 48 ? -0.767 -38.731 2.482 1.00 24.42 ? 69 HIS A CE1 1 ATOM 352 N NE2 . HIS A 1 48 ? -1.556 -37.680 2.617 1.00 23.09 ? 69 HIS A NE2 1 ATOM 353 N N . LYS A 1 49 ? 2.633 -38.008 8.159 1.00 24.86 ? 70 LYS A N 1 ATOM 354 C CA . LYS A 1 49 ? 2.907 -37.693 9.552 1.00 26.17 ? 70 LYS A CA 1 ATOM 355 C C . LYS A 1 49 ? 4.086 -36.754 9.721 1.00 25.40 ? 70 LYS A C 1 ATOM 356 O O . LYS A 1 49 ? 4.999 -36.735 8.893 1.00 25.77 ? 70 LYS A O 1 ATOM 357 C CB . LYS A 1 49 ? 3.161 -38.961 10.352 1.00 29.32 ? 70 LYS A CB 1 ATOM 358 C CG . LYS A 1 49 ? 2.000 -39.955 10.307 1.00 33.79 ? 70 LYS A CG 1 ATOM 359 C CD . LYS A 1 49 ? 2.321 -41.152 11.150 1.00 38.41 ? 70 LYS A CD 1 ATOM 360 C CE . LYS A 1 49 ? 1.051 -41.908 11.493 1.00 45.91 ? 70 LYS A CE 1 ATOM 361 N NZ . LYS A 1 49 ? 0.494 -42.647 10.323 1.00 49.66 ? 70 LYS A NZ 1 ATOM 362 N N . ASP A 1 50 ? 4.056 -35.977 10.797 1.00 23.00 ? 71 ASP A N 1 ATOM 363 C CA . ASP A 1 50 ? 5.202 -35.182 11.184 1.00 26.51 ? 71 ASP A CA 1 ATOM 364 C C . ASP A 1 50 ? 6.361 -36.086 11.576 1.00 25.59 ? 71 ASP A C 1 ATOM 365 O O . ASP A 1 50 ? 6.145 -37.135 12.205 1.00 24.31 ? 71 ASP A O 1 ATOM 366 C CB . ASP A 1 50 ? 4.811 -34.282 12.336 1.00 32.61 ? 71 ASP A CB 1 ATOM 367 C CG . ASP A 1 50 ? 4.036 -33.070 11.855 1.00 35.49 ? 71 ASP A CG 1 ATOM 368 O OD1 . ASP A 1 50 ? 4.469 -32.454 10.837 1.00 36.28 ? 71 ASP A OD1 1 ATOM 369 O OD2 . ASP A 1 50 ? 3.003 -32.759 12.470 1.00 36.68 ? 71 ASP A OD2 1 ATOM 370 N N . THR A 1 51 ? 7.578 -35.701 11.177 1.00 20.76 ? 72 THR A N 1 ATOM 371 C CA . THR A 1 51 ? 8.765 -36.511 11.463 1.00 18.87 ? 72 THR A CA 1 ATOM 372 C C . THR A 1 51 ? 8.423 -38.008 11.347 1.00 19.65 ? 72 THR A C 1 ATOM 373 O O . THR A 1 51 ? 8.569 -38.757 12.288 1.00 20.65 ? 72 THR A O 1 ATOM 374 C CB . THR A 1 51 ? 9.384 -36.182 12.865 1.00 26.45 ? 72 THR A CB 1 ATOM 375 O OG1 . THR A 1 51 ? 9.464 -34.756 13.031 1.00 27.36 ? 72 THR A OG1 1 ATOM 376 C CG2 . THR A 1 51 ? 10.788 -36.803 13.031 1.00 22.63 ? 72 THR A CG2 1 ATOM 377 N N . SER A 1 52 ? 7.968 -38.415 10.168 1.00 20.98 ? 73 SER A N 1 ATOM 378 C CA . SER A 1 52 ? 7.511 -39.771 9.935 1.00 24.92 ? 73 SER A CA 1 ATOM 379 C C . SER A 1 52 ? 8.668 -40.766 9.999 1.00 25.91 ? 73 SER A C 1 ATOM 380 O O . SER A 1 52 ? 9.840 -40.376 9.927 1.00 24.97 ? 73 SER A O 1 ATOM 381 C CB . SER A 1 52 ? 6.839 -39.852 8.563 1.00 26.05 ? 73 SER A CB 1 ATOM 382 O OG . SER A 1 52 ? 7.811 -39.876 7.540 1.00 26.01 ? 73 SER A OG 1 ATOM 383 N N . ARG A 1 53 ? 8.334 -42.051 10.093 1.00 23.42 ? 74 ARG A N 1 ATOM 384 C CA . ARG A 1 53 ? 9.354 -43.094 10.127 1.00 25.10 ? 74 ARG A CA 1 ATOM 385 C C . ARG A 1 53 ? 10.047 -43.289 8.764 1.00 23.59 ? 74 ARG A C 1 ATOM 386 O O . ARG A 1 53 ? 11.045 -43.951 8.692 1.00 24.95 ? 74 ARG A O 1 ATOM 387 C CB . ARG A 1 53 ? 8.786 -44.456 10.694 1.00 24.28 ? 74 ARG A CB 1 ATOM 388 N N . LEU A 1 54 ? 9.545 -42.695 7.689 1.00 22.33 ? 75 LEU A N 1 ATOM 389 C CA . LEU A 1 54 ? 10.174 -42.945 6.389 1.00 24.48 ? 75 LEU A CA 1 ATOM 390 C C . LEU A 1 54 ? 11.668 -42.526 6.306 1.00 23.08 ? 75 LEU A C 1 ATOM 391 O O . LEU A 1 54 ? 12.501 -43.294 5.783 1.00 22.85 ? 75 LEU A O 1 ATOM 392 C CB . LEU A 1 54 ? 9.358 -42.341 5.236 1.00 23.54 ? 75 LEU A CB 1 ATOM 393 C CG . LEU A 1 54 ? 7.959 -42.938 5.024 1.00 24.45 ? 75 LEU A CG 1 ATOM 394 C CD1 . LEU A 1 54 ? 7.256 -42.173 3.924 1.00 23.31 ? 75 LEU A CD1 1 ATOM 395 C CD2 . LEU A 1 54 ? 8.049 -44.427 4.651 1.00 26.76 ? 75 LEU A CD2 1 ATOM 396 N N . TYR A 1 55 ? 11.998 -41.349 6.842 1.00 21.45 ? 76 TYR A N 1 ATOM 397 C CA . TYR A 1 55 ? 13.384 -40.850 6.913 1.00 19.62 ? 76 TYR A CA 1 ATOM 398 C C . TYR A 1 55 ? 13.639 -40.095 8.232 1.00 21.35 ? 76 TYR A C 1 ATOM 399 O O . TYR A 1 55 ? 14.678 -39.451 8.419 1.00 19.55 ? 76 TYR A O 1 ATOM 400 C CB . TYR A 1 55 ? 13.637 -39.886 5.741 1.00 17.37 ? 76 TYR A CB 1 ATOM 401 C CG . TYR A 1 55 ? 13.261 -40.455 4.385 1.00 17.48 ? 76 TYR A CG 1 ATOM 402 C CD1 . TYR A 1 55 ? 14.147 -41.267 3.681 1.00 16.62 ? 76 TYR A CD1 1 ATOM 403 C CD2 . TYR A 1 55 ? 12.008 -40.200 3.821 1.00 15.78 ? 76 TYR A CD2 1 ATOM 404 C CE1 . TYR A 1 55 ? 13.802 -41.809 2.439 1.00 16.36 ? 76 TYR A CE1 1 ATOM 405 C CE2 . TYR A 1 55 ? 11.664 -40.719 2.589 1.00 15.47 ? 76 TYR A CE2 1 ATOM 406 C CZ . TYR A 1 55 ? 12.568 -41.533 1.896 1.00 18.56 ? 76 TYR A CZ 1 ATOM 407 O OH . TYR A 1 55 ? 12.231 -42.061 0.654 1.00 19.10 ? 76 TYR A OH 1 ATOM 408 N N . ASN A 1 56 ? 12.670 -40.142 9.140 1.00 22.27 ? 77 ASN A N 1 ATOM 409 C CA . ASN A 1 56 ? 12.761 -39.367 10.364 1.00 21.06 ? 77 ASN A CA 1 ATOM 410 C C . ASN A 1 56 ? 12.968 -37.889 10.021 1.00 20.54 ? 77 ASN A C 1 ATOM 411 O O . ASN A 1 56 ? 13.698 -37.170 10.708 1.00 18.32 ? 77 ASN A O 1 ATOM 412 C CB . ASN A 1 56 ? 13.882 -39.897 11.276 1.00 23.57 ? 77 ASN A CB 1 ATOM 413 C CG . ASN A 1 56 ? 13.681 -41.379 11.642 1.00 26.73 ? 77 ASN A CG 1 ATOM 414 O OD1 . ASN A 1 56 ? 12.557 -41.815 11.876 1.00 25.62 ? 77 ASN A OD1 1 ATOM 415 N ND2 . ASN A 1 56 ? 14.766 -42.146 11.662 1.00 27.50 ? 77 ASN A ND2 1 ATOM 416 N N . PHE A 1 57 ? 12.293 -37.429 8.977 1.00 19.88 ? 78 PHE A N 1 ATOM 417 C CA . PHE A 1 57 ? 12.472 -36.040 8.556 1.00 20.23 ? 78 PHE A CA 1 ATOM 418 C C . PHE A 1 57 ? 11.470 -35.067 9.181 1.00 19.99 ? 78 PHE A C 1 ATOM 419 O O . PHE A 1 57 ? 10.253 -35.245 9.053 1.00 20.14 ? 78 PHE A O 1 ATOM 420 C CB . PHE A 1 57 ? 12.437 -35.914 7.039 1.00 21.42 ? 78 PHE A CB 1 ATOM 421 C CG . PHE A 1 57 ? 12.925 -34.565 6.540 1.00 21.68 ? 78 PHE A CG 1 ATOM 422 C CD1 . PHE A 1 57 ? 14.295 -34.290 6.460 1.00 19.08 ? 78 PHE A CD1 1 ATOM 423 C CD2 . PHE A 1 57 ? 12.020 -33.578 6.171 1.00 21.97 ? 78 PHE A CD2 1 ATOM 424 C CE1 . PHE A 1 57 ? 14.754 -33.052 6.026 1.00 20.98 ? 78 PHE A CE1 1 ATOM 425 C CE2 . PHE A 1 57 ? 12.477 -32.327 5.720 1.00 22.49 ? 78 PHE A CE2 1 ATOM 426 C CZ . PHE A 1 57 ? 13.834 -32.059 5.658 1.00 20.96 ? 78 PHE A CZ 1 ATOM 427 N N . ASN A 1 58 ? 11.995 -34.020 9.823 1.00 18.88 ? 79 ASN A N 1 ATOM 428 C CA . ASN A 1 58 ? 11.186 -32.994 10.506 1.00 18.15 ? 79 ASN A CA 1 ATOM 429 C C . ASN A 1 58 ? 10.976 -31.721 9.652 1.00 19.23 ? 79 ASN A C 1 ATOM 430 O O . ASN A 1 58 ? 11.935 -30.960 9.359 1.00 15.48 ? 79 ASN A O 1 ATOM 431 C CB . ASN A 1 58 ? 11.805 -32.637 11.875 1.00 18.13 ? 79 ASN A CB 1 ATOM 432 C CG . ASN A 1 58 ? 10.930 -31.666 12.696 1.00 22.86 ? 79 ASN A CG 1 ATOM 433 O OD1 . ASN A 1 58 ? 9.764 -31.402 12.351 1.00 23.71 ? 79 ASN A OD1 1 ATOM 434 N ND2 . ASN A 1 58 ? 11.500 -31.134 13.784 1.00 22.05 ? 79 ASN A ND2 1 ATOM 435 N N . TRP A 1 59 ? 9.731 -31.497 9.224 1.00 19.51 ? 80 TRP A N 1 ATOM 436 C CA . TRP A 1 59 ? 9.397 -30.266 8.502 1.00 17.08 ? 80 TRP A CA 1 ATOM 437 C C . TRP A 1 59 ? 9.390 -29.046 9.428 1.00 19.83 ? 80 TRP A C 1 ATOM 438 O O . TRP A 1 59 ? 9.546 -27.890 8.968 1.00 19.73 ? 80 TRP A O 1 ATOM 439 C CB . TRP A 1 59 ? 8.018 -30.402 7.851 1.00 18.61 ? 80 TRP A CB 1 ATOM 440 C CG . TRP A 1 59 ? 7.995 -31.328 6.686 1.00 18.75 ? 80 TRP A CG 1 ATOM 441 C CD1 . TRP A 1 59 ? 8.827 -31.313 5.599 1.00 20.74 ? 80 TRP A CD1 1 ATOM 442 C CD2 . TRP A 1 59 ? 7.086 -32.402 6.477 1.00 21.62 ? 80 TRP A CD2 1 ATOM 443 N NE1 . TRP A 1 59 ? 8.489 -32.323 4.726 1.00 21.68 ? 80 TRP A NE1 1 ATOM 444 C CE2 . TRP A 1 59 ? 7.421 -33.004 5.245 1.00 21.99 ? 80 TRP A CE2 1 ATOM 445 C CE3 . TRP A 1 59 ? 6.007 -32.909 7.209 1.00 23.44 ? 80 TRP A CE3 1 ATOM 446 C CZ2 . TRP A 1 59 ? 6.710 -34.083 4.720 1.00 23.92 ? 80 TRP A CZ2 1 ATOM 447 C CZ3 . TRP A 1 59 ? 5.304 -34.001 6.684 1.00 26.39 ? 80 TRP A CZ3 1 ATOM 448 C CH2 . TRP A 1 59 ? 5.666 -34.570 5.454 1.00 25.46 ? 80 TRP A CH2 1 ATOM 449 N N . ASP A 1 60 ? 9.148 -29.300 10.721 1.00 21.00 ? 81 ASP A N 1 ATOM 450 C CA . ASP A 1 60 ? 8.971 -28.239 11.716 1.00 22.48 ? 81 ASP A CA 1 ATOM 451 C C . ASP A 1 60 ? 10.306 -27.936 12.387 1.00 22.57 ? 81 ASP A C 1 ATOM 452 O O . ASP A 1 60 ? 10.386 -27.796 13.612 1.00 21.38 ? 81 ASP A O 1 ATOM 453 C CB . ASP A 1 60 ? 7.953 -28.674 12.782 1.00 25.18 ? 81 ASP A CB 1 ATOM 454 C CG . ASP A 1 60 ? 6.588 -29.015 12.188 1.00 27.10 ? 81 ASP A CG 1 ATOM 455 O OD1 . ASP A 1 60 ? 6.135 -28.355 11.220 1.00 25.83 ? 81 ASP A OD1 1 ATOM 456 O OD2 . ASP A 1 60 ? 5.950 -29.941 12.703 1.00 30.32 ? 81 ASP A OD2 1 ATOM 457 N N . HIS A 1 61 ? 11.367 -27.849 11.589 1.00 21.42 ? 82 HIS A N 1 ATOM 458 C CA . HIS A 1 61 ? 12.699 -27.660 12.157 1.00 19.36 ? 82 HIS A CA 1 ATOM 459 C C . HIS A 1 61 ? 12.954 -26.201 12.576 1.00 23.35 ? 82 HIS A C 1 ATOM 460 O O . HIS A 1 61 ? 13.881 -25.938 13.321 1.00 26.61 ? 82 HIS A O 1 ATOM 461 C CB . HIS A 1 61 ? 13.761 -28.151 11.167 1.00 16.09 ? 82 HIS A CB 1 ATOM 462 C CG . HIS A 1 61 ? 13.587 -27.613 9.782 1.00 16.42 ? 82 HIS A CG 1 ATOM 463 N ND1 . HIS A 1 61 ? 12.927 -28.303 8.789 1.00 17.57 ? 82 HIS A ND1 1 ATOM 464 C CD2 . HIS A 1 61 ? 13.946 -26.424 9.239 1.00 16.01 ? 82 HIS A CD2 1 ATOM 465 C CE1 . HIS A 1 61 ? 12.909 -27.571 7.684 1.00 18.39 ? 82 HIS A CE1 1 ATOM 466 N NE2 . HIS A 1 61 ? 13.521 -26.423 7.932 1.00 15.04 ? 82 HIS A NE2 1 ATOM 467 N N . CYS A 1 62 ? 12.150 -25.252 12.091 1.00 20.25 ? 83 CYS A N 1 ATOM 468 C CA . CYS A 1 62 ? 12.252 -23.883 12.578 1.00 23.66 ? 83 CYS A CA 1 ATOM 469 C C . CYS A 1 62 ? 10.884 -23.452 13.103 1.00 25.62 ? 83 CYS A C 1 ATOM 470 O O . CYS A 1 62 ? 10.220 -22.598 12.525 1.00 24.30 ? 83 CYS A O 1 ATOM 471 C CB . CYS A 1 62 ? 12.744 -22.938 11.469 1.00 22.89 ? 83 CYS A CB 1 ATOM 472 S SG . CYS A 1 62 ? 14.528 -23.070 11.156 1.00 21.31 ? 83 CYS A SG 1 ATOM 473 N N . GLY A 1 63 ? 10.463 -24.080 14.190 1.00 29.09 ? 84 GLY A N 1 ATOM 474 C CA . GLY A 1 63 ? 9.095 -23.961 14.654 1.00 29.21 ? 84 GLY A CA 1 ATOM 475 C C . GLY A 1 63 ? 8.137 -24.686 13.718 1.00 27.55 ? 84 GLY A C 1 ATOM 476 O O . GLY A 1 63 ? 8.549 -25.338 12.769 1.00 26.46 ? 84 GLY A O 1 ATOM 477 N N . LYS A 1 64 ? 6.846 -24.550 13.982 1.00 28.71 ? 85 LYS A N 1 ATOM 478 C CA . LYS A 1 64 ? 5.829 -25.261 13.229 1.00 28.34 ? 85 LYS A CA 1 ATOM 479 C C . LYS A 1 64 ? 5.671 -24.700 11.815 1.00 24.86 ? 85 LYS A C 1 ATOM 480 O O . LYS A 1 64 ? 5.518 -23.499 11.626 1.00 25.14 ? 85 LYS A O 1 ATOM 481 C CB . LYS A 1 64 ? 4.485 -25.194 13.978 1.00 32.50 ? 85 LYS A CB 1 ATOM 482 C CG . LYS A 1 64 ? 3.252 -25.582 13.134 1.00 36.76 ? 85 LYS A CG 1 ATOM 483 C CD . LYS A 1 64 ? 2.638 -26.920 13.590 1.00 42.74 ? 85 LYS A CD 1 ATOM 484 C CE . LYS A 1 64 ? 3.684 -28.034 13.552 1.00 46.43 ? 85 LYS A CE 1 ATOM 485 N NZ . LYS A 1 64 ? 3.142 -29.400 13.788 1.00 48.88 ? 85 LYS A NZ 1 ATOM 486 N N . MET A 1 65 ? 5.708 -25.580 10.824 1.00 20.38 ? 86 MET A N 1 ATOM 487 C CA . MET A 1 65 ? 5.423 -25.190 9.455 1.00 21.17 ? 86 MET A CA 1 ATOM 488 C C . MET A 1 65 ? 3.889 -25.096 9.300 1.00 24.56 ? 86 MET A C 1 ATOM 489 O O . MET A 1 65 ? 3.157 -25.987 9.766 1.00 23.54 ? 86 MET A O 1 ATOM 490 C CB . MET A 1 65 ? 6.025 -26.216 8.494 1.00 18.36 ? 86 MET A CB 1 ATOM 491 C CG . MET A 1 65 ? 5.572 -26.048 7.054 1.00 19.22 ? 86 MET A CG 1 ATOM 492 S SD . MET A 1 65 ? 6.012 -27.475 6.034 1.00 20.04 ? 86 MET A SD 1 ATOM 493 C CE . MET A 1 65 ? 7.792 -27.189 5.806 1.00 14.44 ? 86 MET A CE 1 ATOM 494 N N . GLU A 1 66 ? 3.403 -24.008 8.698 1.00 23.02 ? 87 GLU A N 1 ATOM 495 C CA . GLU A 1 66 ? 1.956 -23.787 8.566 1.00 24.73 ? 87 GLU A CA 1 ATOM 496 C C . GLU A 1 66 ? 1.281 -24.850 7.680 1.00 22.43 ? 87 GLU A C 1 ATOM 497 O O . GLU A 1 66 ? 1.871 -25.326 6.722 1.00 21.15 ? 87 GLU A O 1 ATOM 498 C CB . GLU A 1 66 ? 1.682 -22.390 8.014 1.00 28.45 ? 87 GLU A CB 1 ATOM 499 C CG . GLU A 1 66 ? 2.303 -21.284 8.856 1.00 35.32 ? 87 GLU A CG 1 ATOM 500 C CD . GLU A 1 66 ? 1.622 -21.156 10.217 1.00 40.69 ? 87 GLU A CD 1 ATOM 501 O OE1 . GLU A 1 66 ? 0.450 -21.575 10.316 1.00 42.08 ? 87 GLU A OE1 1 ATOM 502 O OE2 . GLU A 1 66 ? 2.254 -20.648 11.181 1.00 42.59 ? 87 GLU A OE2 1 ATOM 503 N N . PRO A 1 67 ? 0.033 -25.195 7.992 1.00 19.98 ? 88 PRO A N 1 ATOM 504 C CA . PRO A 1 67 ? -0.717 -26.198 7.217 1.00 23.38 ? 88 PRO A CA 1 ATOM 505 C C . PRO A 1 67 ? -0.748 -25.872 5.709 1.00 22.97 ? 88 PRO A C 1 ATOM 506 O O . PRO A 1 67 ? -0.550 -26.778 4.896 1.00 21.07 ? 88 PRO A O 1 ATOM 507 C CB . PRO A 1 67 ? -2.141 -26.105 7.805 1.00 25.49 ? 88 PRO A CB 1 ATOM 508 C CG . PRO A 1 67 ? -1.890 -25.689 9.258 1.00 25.51 ? 88 PRO A CG 1 ATOM 509 C CD . PRO A 1 67 ? -0.688 -24.743 9.192 1.00 22.03 ? 88 PRO A CD 1 ATOM 510 N N . ALA A 1 68 ? -0.988 -24.609 5.342 1.00 19.96 ? 89 ALA A N 1 ATOM 511 C CA . ALA A 1 68 ? -1.107 -24.263 3.924 1.00 19.78 ? 89 ALA A CA 1 ATOM 512 C C . ALA A 1 68 ? 0.209 -24.546 3.204 1.00 21.79 ? 89 ALA A C 1 ATOM 513 O O . ALA A 1 68 ? 0.232 -24.771 1.991 1.00 22.72 ? 89 ALA A O 1 ATOM 514 C CB . ALA A 1 68 ? -1.499 -22.814 3.754 1.00 20.07 ? 89 ALA A CB 1 ATOM 515 N N . CYS A 1 69 ? 1.308 -24.534 3.962 1.00 22.99 ? 90 CYS A N 1 ATOM 516 C CA . CYS A 1 69 ? 2.619 -24.817 3.395 1.00 21.97 ? 90 CYS A CA 1 ATOM 517 C C . CYS A 1 69 ? 2.937 -26.317 3.423 1.00 19.74 ? 90 CYS A C 1 ATOM 518 O O . CYS A 1 69 ? 3.409 -26.863 2.453 1.00 18.43 ? 90 CYS A O 1 ATOM 519 C CB . CYS A 1 69 ? 3.696 -24.054 4.145 1.00 22.06 ? 90 CYS A CB 1 ATOM 520 S SG . CYS A 1 69 ? 5.392 -24.479 3.652 1.00 22.82 ? 90 CYS A SG 1 ATOM 521 N N . LYS A 1 70 ? 2.665 -26.964 4.548 1.00 19.52 ? 91 LYS A N 1 ATOM 522 C CA . LYS A 1 70 ? 2.979 -28.370 4.725 1.00 17.94 ? 91 LYS A CA 1 ATOM 523 C C . LYS A 1 70 ? 2.232 -29.295 3.730 1.00 20.31 ? 91 LYS A C 1 ATOM 524 O O . LYS A 1 70 ? 2.767 -30.325 3.300 1.00 21.89 ? 91 LYS A O 1 ATOM 525 C CB . LYS A 1 70 ? 2.718 -28.775 6.174 1.00 19.43 ? 91 LYS A CB 1 ATOM 526 C CG . LYS A 1 70 ? 3.079 -30.248 6.528 1.00 24.19 ? 91 LYS A CG 1 ATOM 527 C CD . LYS A 1 70 ? 2.889 -30.503 8.042 1.00 28.86 ? 91 LYS A CD 1 ATOM 528 C CE . LYS A 1 70 ? 3.852 -29.598 8.825 1.00 32.66 ? 91 LYS A CE 1 ATOM 529 N NZ . LYS A 1 70 ? 3.786 -29.763 10.301 1.00 36.50 ? 91 LYS A NZ 1 ATOM 530 N N . ARG A 1 71 ? 1.023 -28.922 3.327 1.00 20.06 ? 92 ARG A N 1 ATOM 531 C CA . ARG A 1 71 ? 0.299 -29.733 2.349 1.00 20.31 ? 92 ARG A CA 1 ATOM 532 C C . ARG A 1 71 ? 1.105 -29.916 1.061 1.00 19.24 ? 92 ARG A C 1 ATOM 533 O O . ARG A 1 71 ? 0.969 -30.957 0.411 1.00 17.77 ? 92 ARG A O 1 ATOM 534 C CB . ARG A 1 71 ? -1.081 -29.137 2.007 1.00 19.82 ? 92 ARG A CB 1 ATOM 535 C CG . ARG A 1 71 ? -1.017 -27.792 1.275 1.00 22.82 ? 92 ARG A CG 1 ATOM 536 C CD . ARG A 1 71 ? -2.422 -27.115 1.200 1.00 28.98 ? 92 ARG A CD 1 ATOM 537 N NE . ARG A 1 71 ? -2.374 -25.698 0.806 1.00 29.71 ? 92 ARG A NE 1 ATOM 538 C CZ . ARG A 1 71 ? -3.450 -24.972 0.487 1.00 31.04 ? 92 ARG A CZ 1 ATOM 539 N NH1 . ARG A 1 71 ? -4.662 -25.529 0.491 1.00 30.65 ? 92 ARG A NH1 1 ATOM 540 N NH2 . ARG A 1 71 ? -3.325 -23.693 0.141 1.00 30.64 ? 92 ARG A NH2 1 ATOM 541 N N . HIS A 1 72 ? 1.896 -28.897 0.678 1.00 15.49 ? 93 HIS A N 1 ATOM 542 C CA . HIS A 1 72 ? 2.741 -28.986 -0.511 1.00 15.03 ? 93 HIS A CA 1 ATOM 543 C C . HIS A 1 72 ? 3.917 -29.937 -0.337 1.00 14.16 ? 93 HIS A C 1 ATOM 544 O O . HIS A 1 72 ? 4.237 -30.667 -1.270 1.00 15.33 ? 93 HIS A O 1 ATOM 545 C CB . HIS A 1 72 ? 3.262 -27.593 -0.990 1.00 14.80 ? 93 HIS A CB 1 ATOM 546 C CG . HIS A 1 72 ? 2.162 -26.664 -1.373 1.00 15.69 ? 93 HIS A CG 1 ATOM 547 N ND1 . HIS A 1 72 ? 1.448 -26.809 -2.541 1.00 17.11 ? 93 HIS A ND1 1 ATOM 548 C CD2 . HIS A 1 72 ? 1.613 -25.607 -0.717 1.00 15.94 ? 93 HIS A CD2 1 ATOM 549 C CE1 . HIS A 1 72 ? 0.494 -25.894 -2.582 1.00 18.59 ? 93 HIS A CE1 1 ATOM 550 N NE2 . HIS A 1 72 ? 0.576 -25.147 -1.492 1.00 16.93 ? 93 HIS A NE2 1 ATOM 551 N N . PHE A 1 73 ? 4.568 -29.911 0.835 1.00 15.32 ? 94 PHE A N 1 ATOM 552 C CA . PHE A 1 73 ? 5.635 -30.869 1.109 1.00 14.78 ? 94 PHE A CA 1 ATOM 553 C C . PHE A 1 73 ? 5.070 -32.291 1.161 1.00 17.60 ? 94 PHE A C 1 ATOM 554 O O . PHE A 1 73 ? 5.736 -33.209 0.718 1.00 18.65 ? 94 PHE A O 1 ATOM 555 C CB . PHE A 1 73 ? 6.413 -30.526 2.384 1.00 15.92 ? 94 PHE A CB 1 ATOM 556 C CG . PHE A 1 73 ? 7.331 -29.330 2.220 1.00 16.18 ? 94 PHE A CG 1 ATOM 557 C CD1 . PHE A 1 73 ? 8.631 -29.494 1.781 1.00 17.04 ? 94 PHE A CD1 1 ATOM 558 C CD2 . PHE A 1 73 ? 6.859 -28.045 2.440 1.00 16.12 ? 94 PHE A CD2 1 ATOM 559 C CE1 . PHE A 1 73 ? 9.480 -28.407 1.610 1.00 16.75 ? 94 PHE A CE1 1 ATOM 560 C CE2 . PHE A 1 73 ? 7.693 -26.937 2.277 1.00 18.40 ? 94 PHE A CE2 1 ATOM 561 C CZ . PHE A 1 73 ? 9.006 -27.125 1.846 1.00 18.34 ? 94 PHE A CZ 1 ATOM 562 N N . ILE A 1 74 ? 3.831 -32.465 1.664 1.00 18.15 ? 95 ILE A N 1 ATOM 563 C CA . ILE A 1 74 ? 3.203 -33.789 1.655 1.00 14.43 ? 95 ILE A CA 1 ATOM 564 C C . ILE A 1 74 ? 2.958 -34.204 0.205 1.00 15.38 ? 95 ILE A C 1 ATOM 565 O O . ILE A 1 74 ? 3.271 -35.325 -0.198 1.00 17.31 ? 95 ILE A O 1 ATOM 566 C CB . ILE A 1 74 ? 1.903 -33.828 2.475 1.00 17.54 ? 95 ILE A CB 1 ATOM 567 C CG1 . ILE A 1 74 ? 2.230 -33.718 3.975 1.00 18.25 ? 95 ILE A CG1 1 ATOM 568 C CG2 . ILE A 1 74 ? 1.080 -35.142 2.161 1.00 14.12 ? 95 ILE A CG2 1 ATOM 569 C CD1 . ILE A 1 74 ? 1.025 -33.633 4.910 1.00 16.62 ? 95 ILE A CD1 1 ATOM 570 N N . GLN A 1 75 ? 2.429 -33.278 -0.587 1.00 13.48 ? 96 GLN A N 1 ATOM 571 C CA . GLN A 1 75 ? 2.115 -33.558 -1.978 1.00 13.15 ? 96 GLN A CA 1 ATOM 572 C C . GLN A 1 75 ? 3.385 -33.915 -2.765 1.00 14.26 ? 96 GLN A C 1 ATOM 573 O O . GLN A 1 75 ? 3.399 -34.862 -3.570 1.00 13.90 ? 96 GLN A O 1 ATOM 574 C CB . GLN A 1 75 ? 1.440 -32.335 -2.620 1.00 15.04 ? 96 GLN A CB 1 ATOM 575 C CG . GLN A 1 75 ? 0.808 -32.625 -3.994 1.00 15.34 ? 96 GLN A CG 1 ATOM 576 C CD . GLN A 1 75 ? -0.479 -33.435 -3.864 1.00 17.05 ? 96 GLN A CD 1 ATOM 577 O OE1 . GLN A 1 75 ? -1.051 -33.542 -2.774 1.00 17.33 ? 96 GLN A OE1 1 ATOM 578 N NE2 . GLN A 1 75 ? -0.932 -34.011 -4.970 1.00 17.60 ? 96 GLN A NE2 1 ATOM 579 N N . ASP A 1 76 ? 4.429 -33.103 -2.584 1.00 13.26 ? 97 ASP A N 1 ATOM 580 C CA . ASP A 1 76 ? 5.716 -33.379 -3.210 1.00 12.69 ? 97 ASP A CA 1 ATOM 581 C C . ASP A 1 76 ? 6.239 -34.788 -2.823 1.00 17.67 ? 97 ASP A C 1 ATOM 582 O O . ASP A 1 76 ? 6.803 -35.490 -3.645 1.00 19.14 ? 97 ASP A O 1 ATOM 583 C CB . ASP A 1 76 ? 6.730 -32.315 -2.769 1.00 14.27 ? 97 ASP A CB 1 ATOM 584 C CG . ASP A 1 76 ? 8.154 -32.644 -3.213 1.00 17.32 ? 97 ASP A CG 1 ATOM 585 O OD1 . ASP A 1 76 ? 8.386 -32.713 -4.440 1.00 18.16 ? 97 ASP A OD1 1 ATOM 586 O OD2 . ASP A 1 76 ? 9.044 -32.783 -2.346 1.00 17.83 ? 97 ASP A OD2 1 ATOM 587 N N . THR A 1 77 ? 6.073 -35.185 -1.565 1.00 16.72 ? 98 THR A N 1 ATOM 588 C CA . THR A 1 77 ? 6.517 -36.525 -1.151 1.00 16.83 ? 98 THR A CA 1 ATOM 589 C C . THR A 1 77 ? 5.666 -37.619 -1.811 1.00 15.85 ? 98 THR A C 1 ATOM 590 O O . THR A 1 77 ? 6.206 -38.666 -2.179 1.00 14.20 ? 98 THR A O 1 ATOM 591 C CB . THR A 1 77 ? 6.453 -36.696 0.381 1.00 19.48 ? 98 THR A CB 1 ATOM 592 O OG1 . THR A 1 77 ? 7.251 -35.686 1.008 1.00 20.24 ? 98 THR A OG1 1 ATOM 593 C CG2 . THR A 1 77 ? 6.942 -38.101 0.821 1.00 13.74 ? 98 THR A CG2 1 ATOM 594 N N . CYS A 1 78 ? 4.350 -37.383 -1.968 1.00 16.25 ? 99 CYS A N 1 ATOM 595 C CA . CYS A 1 78 ? 3.494 -38.325 -2.714 1.00 18.07 ? 99 CYS A CA 1 ATOM 596 C C . CYS A 1 78 ? 4.039 -38.502 -4.125 1.00 17.83 ? 99 CYS A C 1 ATOM 597 O O . CYS A 1 78 ? 4.115 -39.629 -4.640 1.00 18.40 ? 99 CYS A O 1 ATOM 598 C CB . CYS A 1 78 ? 2.044 -37.845 -2.865 1.00 18.43 ? 99 CYS A CB 1 ATOM 599 S SG . CYS A 1 78 ? 1.002 -37.955 -1.432 1.00 18.40 ? 99 CYS A SG 1 ATOM 600 N N . LEU A 1 79 ? 4.382 -37.383 -4.768 1.00 17.69 ? 100 LEU A N 1 ATOM 601 C CA . LEU A 1 79 ? 4.925 -37.464 -6.127 1.00 16.96 ? 100 LEU A CA 1 ATOM 602 C C . LEU A 1 79 ? 6.236 -38.257 -6.112 1.00 16.96 ? 100 LEU A C 1 ATOM 603 O O . LEU A 1 79 ? 6.414 -39.210 -6.872 1.00 19.24 ? 100 LEU A O 1 ATOM 604 C CB . LEU A 1 79 ? 5.137 -36.089 -6.761 1.00 14.82 ? 100 LEU A CB 1 ATOM 605 C CG . LEU A 1 79 ? 5.770 -36.117 -8.171 1.00 16.32 ? 100 LEU A CG 1 ATOM 606 C CD1 . LEU A 1 79 ? 4.756 -36.544 -9.233 1.00 18.05 ? 100 LEU A CD1 1 ATOM 607 C CD2 . LEU A 1 79 ? 6.365 -34.749 -8.600 1.00 18.65 ? 100 LEU A CD2 1 ATOM 608 N N . TYR A 1 80 ? 7.152 -37.858 -5.242 1.00 16.11 ? 101 TYR A N 1 ATOM 609 C CA . TYR A 1 80 ? 8.456 -38.523 -5.177 1.00 16.66 ? 101 TYR A CA 1 ATOM 610 C C . TYR A 1 80 ? 8.310 -40.034 -4.899 1.00 17.77 ? 101 TYR A C 1 ATOM 611 O O . TYR A 1 80 ? 8.903 -40.871 -5.586 1.00 18.53 ? 101 TYR A O 1 ATOM 612 C CB . TYR A 1 80 ? 9.346 -37.862 -4.118 1.00 16.79 ? 101 TYR A CB 1 ATOM 613 C CG . TYR A 1 80 ? 10.679 -38.581 -3.853 1.00 20.86 ? 101 TYR A CG 1 ATOM 614 C CD1 . TYR A 1 80 ? 11.829 -38.241 -4.556 1.00 16.16 ? 101 TYR A CD1 1 ATOM 615 C CD2 . TYR A 1 80 ? 10.775 -39.603 -2.895 1.00 21.96 ? 101 TYR A CD2 1 ATOM 616 C CE1 . TYR A 1 80 ? 13.026 -38.900 -4.325 1.00 16.95 ? 101 TYR A CE1 1 ATOM 617 C CE2 . TYR A 1 80 ? 11.986 -40.255 -2.648 1.00 21.15 ? 101 TYR A CE2 1 ATOM 618 C CZ . TYR A 1 80 ? 13.104 -39.903 -3.377 1.00 19.84 ? 101 TYR A CZ 1 ATOM 619 O OH . TYR A 1 80 ? 14.303 -40.544 -3.153 1.00 19.94 ? 101 TYR A OH 1 ATOM 620 N N . GLU A 1 81 ? 7.536 -40.383 -3.879 1.00 18.81 ? 102 GLU A N 1 ATOM 621 C CA . GLU A 1 81 ? 7.428 -41.789 -3.468 1.00 19.13 ? 102 GLU A CA 1 ATOM 622 C C . GLU A 1 81 ? 6.471 -42.559 -4.377 1.00 21.94 ? 102 GLU A C 1 ATOM 623 O O . GLU A 1 81 ? 6.599 -43.768 -4.496 1.00 24.11 ? 102 GLU A O 1 ATOM 624 C CB . GLU A 1 81 ? 6.931 -41.922 -2.022 1.00 18.97 ? 102 GLU A CB 1 ATOM 625 C CG . GLU A 1 81 ? 7.795 -41.227 -0.965 1.00 19.18 ? 102 GLU A CG 1 ATOM 626 C CD . GLU A 1 81 ? 9.142 -41.902 -0.709 1.00 21.46 ? 102 GLU A CD 1 ATOM 627 O OE1 . GLU A 1 81 ? 9.362 -43.058 -1.182 1.00 21.52 ? 102 GLU A OE1 1 ATOM 628 O OE2 . GLU A 1 81 ? 9.984 -41.268 -0.015 1.00 19.45 ? 102 GLU A OE2 1 ATOM 629 N N . CYS A 1 82 ? 5.516 -41.881 -5.016 1.00 19.99 ? 103 CYS A N 1 ATOM 630 C CA . CYS A 1 82 ? 4.456 -42.636 -5.742 1.00 18.62 ? 103 CYS A CA 1 ATOM 631 C C . CYS A 1 82 ? 4.471 -42.602 -7.279 1.00 20.34 ? 103 CYS A C 1 ATOM 632 O O . CYS A 1 82 ? 3.918 -43.494 -7.930 1.00 23.04 ? 103 CYS A O 1 ATOM 633 C CB . CYS A 1 82 ? 3.047 -42.225 -5.271 1.00 16.44 ? 103 CYS A CB 1 ATOM 634 S SG . CYS A 1 82 ? 2.749 -42.342 -3.496 1.00 21.13 ? 103 CYS A SG 1 ATOM 635 N N . SER A 1 83 ? 5.049 -41.563 -7.871 1.00 20.69 ? 104 SER A N 1 ATOM 636 C CA . SER A 1 83 ? 4.955 -41.389 -9.325 1.00 19.66 ? 104 SER A CA 1 ATOM 637 C C . SER A 1 83 ? 5.600 -42.494 -10.156 1.00 18.27 ? 104 SER A C 1 ATOM 638 O O . SER A 1 83 ? 6.772 -42.788 -9.982 1.00 18.71 ? 104 SER A O 1 ATOM 639 C CB . SER A 1 83 ? 5.602 -40.080 -9.733 1.00 21.88 ? 104 SER A CB 1 ATOM 640 O OG . SER A 1 83 ? 5.451 -39.927 -11.133 1.00 24.33 ? 104 SER A OG 1 ATOM 641 N N . PRO A 1 84 ? 4.841 -43.095 -11.089 1.00 19.15 ? 105 PRO A N 1 ATOM 642 C CA . PRO A 1 84 ? 5.447 -44.041 -12.029 1.00 19.97 ? 105 PRO A CA 1 ATOM 643 C C . PRO A 1 84 ? 5.772 -43.308 -13.325 1.00 22.86 ? 105 PRO A C 1 ATOM 644 O O . PRO A 1 84 ? 6.035 -43.946 -14.337 1.00 22.93 ? 105 PRO A O 1 ATOM 645 C CB . PRO A 1 84 ? 4.308 -45.027 -12.286 1.00 20.47 ? 105 PRO A CB 1 ATOM 646 C CG . PRO A 1 84 ? 3.095 -44.151 -12.278 1.00 22.77 ? 105 PRO A CG 1 ATOM 647 C CD . PRO A 1 84 ? 3.387 -43.017 -11.274 1.00 20.49 ? 105 PRO A CD 1 ATOM 648 N N . ASN A 1 85 ? 5.784 -41.976 -13.286 1.00 20.52 ? 106 ASN A N 1 ATOM 649 C CA . ASN A 1 85 ? 5.907 -41.207 -14.514 1.00 20.28 ? 106 ASN A CA 1 ATOM 650 C C . ASN A 1 85 ? 7.123 -40.281 -14.580 1.00 20.78 ? 106 ASN A C 1 ATOM 651 O O . ASN A 1 85 ? 7.084 -39.249 -15.239 1.00 20.90 ? 106 ASN A O 1 ATOM 652 C CB . ASN A 1 85 ? 4.611 -40.425 -14.741 1.00 16.15 ? 106 ASN A CB 1 ATOM 653 C CG . ASN A 1 85 ? 3.398 -41.365 -14.912 1.00 20.83 ? 106 ASN A CG 1 ATOM 654 O OD1 . ASN A 1 85 ? 3.466 -42.360 -15.647 1.00 21.25 ? 106 ASN A OD1 1 ATOM 655 N ND2 . ASN A 1 85 ? 2.310 -41.074 -14.201 1.00 21.25 ? 106 ASN A ND2 1 ATOM 656 N N . LEU A 1 86 ? 8.202 -40.648 -13.899 1.00 21.09 ? 107 LEU A N 1 ATOM 657 C CA . LEU A 1 86 ? 9.377 -39.775 -13.823 1.00 18.78 ? 107 LEU A CA 1 ATOM 658 C C . LEU A 1 86 ? 10.634 -40.462 -14.394 1.00 19.58 ? 107 LEU A C 1 ATOM 659 O O . LEU A 1 86 ? 11.757 -39.947 -14.247 1.00 19.28 ? 107 LEU A O 1 ATOM 660 C CB . LEU A 1 86 ? 9.638 -39.352 -12.369 1.00 16.84 ? 107 LEU A CB 1 ATOM 661 C CG . LEU A 1 86 ? 8.526 -38.575 -11.667 1.00 19.51 ? 107 LEU A CG 1 ATOM 662 C CD1 . LEU A 1 86 ? 8.874 -38.347 -10.155 1.00 19.67 ? 107 LEU A CD1 1 ATOM 663 C CD2 . LEU A 1 86 ? 8.278 -37.251 -12.385 1.00 17.40 ? 107 LEU A CD2 1 ATOM 664 N N . GLY A 1 87 ? 10.437 -41.613 -15.035 1.00 17.49 ? 108 GLY A N 1 ATOM 665 C CA . GLY A 1 87 ? 11.508 -42.338 -15.705 1.00 20.14 ? 108 GLY A CA 1 ATOM 666 C C . GLY A 1 87 ? 12.501 -41.468 -16.479 1.00 22.66 ? 108 GLY A C 1 ATOM 667 O O . GLY A 1 87 ? 13.704 -41.594 -16.308 1.00 22.98 ? 108 GLY A O 1 ATOM 668 N N . PRO A 1 88 ? 12.000 -40.563 -17.335 1.00 21.83 ? 109 PRO A N 1 ATOM 669 C CA . PRO A 1 88 ? 12.883 -39.759 -18.192 1.00 20.70 ? 109 PRO A CA 1 ATOM 670 C C . PRO A 1 88 ? 13.881 -38.895 -17.416 1.00 20.60 ? 109 PRO A C 1 ATOM 671 O O . PRO A 1 88 ? 14.844 -38.419 -18.018 1.00 20.43 ? 109 PRO A O 1 ATOM 672 C CB . PRO A 1 88 ? 11.899 -38.853 -18.936 1.00 19.62 ? 109 PRO A CB 1 ATOM 673 C CG . PRO A 1 88 ? 10.652 -39.665 -18.997 1.00 19.75 ? 109 PRO A CG 1 ATOM 674 C CD . PRO A 1 88 ? 10.579 -40.349 -17.658 1.00 18.41 ? 109 PRO A CD 1 ATOM 675 N N . TRP A 1 89 ? 13.640 -38.692 -16.121 1.00 19.08 ? 110 TRP A N 1 ATOM 676 C CA . TRP A 1 89 ? 14.488 -37.826 -15.307 1.00 17.58 ? 110 TRP A CA 1 ATOM 677 C C . TRP A 1 89 ? 15.298 -38.598 -14.271 1.00 18.74 ? 110 TRP A C 1 ATOM 678 O O . TRP A 1 89 ? 16.035 -38.009 -13.492 1.00 18.88 ? 110 TRP A O 1 ATOM 679 C CB . TRP A 1 89 ? 13.654 -36.721 -14.663 1.00 15.45 ? 110 TRP A CB 1 ATOM 680 C CG . TRP A 1 89 ? 13.019 -35.932 -15.739 1.00 17.54 ? 110 TRP A CG 1 ATOM 681 C CD1 . TRP A 1 89 ? 13.609 -34.965 -16.502 1.00 19.28 ? 110 TRP A CD1 1 ATOM 682 C CD2 . TRP A 1 89 ? 11.704 -36.108 -16.254 1.00 17.30 ? 110 TRP A CD2 1 ATOM 683 N NE1 . TRP A 1 89 ? 12.734 -34.516 -17.451 1.00 20.69 ? 110 TRP A NE1 1 ATOM 684 C CE2 . TRP A 1 89 ? 11.550 -35.199 -17.320 1.00 19.63 ? 110 TRP A CE2 1 ATOM 685 C CE3 . TRP A 1 89 ? 10.641 -36.942 -15.918 1.00 20.17 ? 110 TRP A CE3 1 ATOM 686 C CZ2 . TRP A 1 89 ? 10.371 -35.078 -18.029 1.00 20.00 ? 110 TRP A CZ2 1 ATOM 687 C CZ3 . TRP A 1 89 ? 9.442 -36.829 -16.644 1.00 23.06 ? 110 TRP A CZ3 1 ATOM 688 C CH2 . TRP A 1 89 ? 9.327 -35.909 -17.685 1.00 22.45 ? 110 TRP A CH2 1 ATOM 689 N N . ILE A 1 90 ? 15.177 -39.925 -14.292 1.00 17.36 ? 111 ILE A N 1 ATOM 690 C CA . ILE A 1 90 ? 15.930 -40.747 -13.368 1.00 18.48 ? 111 ILE A CA 1 ATOM 691 C C . ILE A 1 90 ? 17.437 -40.671 -13.679 1.00 21.36 ? 111 ILE A C 1 ATOM 692 O O . ILE A 1 90 ? 17.848 -40.818 -14.837 1.00 24.69 ? 111 ILE A O 1 ATOM 693 C CB . ILE A 1 90 ? 15.446 -42.223 -13.418 1.00 19.51 ? 111 ILE A CB 1 ATOM 694 C CG1 . ILE A 1 90 ? 14.084 -42.371 -12.708 1.00 18.59 ? 111 ILE A CG1 1 ATOM 695 C CG2 . ILE A 1 90 ? 16.517 -43.140 -12.821 1.00 20.13 ? 111 ILE A CG2 1 ATOM 696 C CD1 . ILE A 1 90 ? 13.446 -43.832 -12.791 1.00 14.07 ? 111 ILE A CD1 1 ATOM 697 N N . GLN A 1 91 ? 18.248 -40.433 -12.651 1.00 19.43 ? 112 GLN A N 1 ATOM 698 C CA . GLN A 1 91 ? 19.713 -40.514 -12.768 1.00 21.68 ? 112 GLN A CA 1 ATOM 699 C C . GLN A 1 91 ? 20.327 -41.467 -11.738 1.00 21.63 ? 112 GLN A C 1 ATOM 700 O O . GLN A 1 91 ? 19.782 -41.666 -10.642 1.00 19.60 ? 112 GLN A O 1 ATOM 701 C CB . GLN A 1 91 ? 20.341 -39.136 -12.540 1.00 24.23 ? 112 GLN A CB 1 ATOM 702 C CG . GLN A 1 91 ? 19.898 -38.073 -13.539 1.00 26.34 ? 112 GLN A CG 1 ATOM 703 C CD . GLN A 1 91 ? 20.701 -38.129 -14.837 1.00 31.27 ? 112 GLN A CD 1 ATOM 704 O OE1 . GLN A 1 91 ? 21.939 -38.037 -14.834 1.00 31.77 ? 112 GLN A OE1 1 ATOM 705 N NE2 . GLN A 1 91 ? 19.998 -38.276 -15.950 1.00 31.59 ? 112 GLN A NE2 1 ATOM 706 N N . GLN A 1 92 ? 21.490 -42.014 -12.067 1.00 20.69 ? 113 GLN A N 1 ATOM 707 C CA . GLN A 1 92 ? 22.228 -42.855 -11.128 1.00 26.06 ? 113 GLN A CA 1 ATOM 708 C C . GLN A 1 92 ? 22.917 -41.990 -10.077 1.00 26.80 ? 113 GLN A C 1 ATOM 709 O O . GLN A 1 92 ? 23.409 -40.910 -10.401 1.00 28.38 ? 113 GLN A O 1 ATOM 710 C CB . GLN A 1 92 ? 23.270 -43.654 -11.906 1.00 35.39 ? 113 GLN A CB 1 ATOM 711 C CG . GLN A 1 92 ? 22.658 -44.326 -13.146 1.00 41.89 ? 113 GLN A CG 1 ATOM 712 C CD . GLN A 1 92 ? 21.621 -45.397 -12.778 1.00 45.35 ? 113 GLN A CD 1 ATOM 713 O OE1 . GLN A 1 92 ? 21.982 -46.477 -12.284 1.00 50.34 ? 113 GLN A OE1 1 ATOM 714 N NE2 . GLN A 1 92 ? 20.332 -45.098 -13.011 1.00 41.04 ? 113 GLN A NE2 1 ATOM 715 N N . VAL A 1 93 ? 22.962 -42.456 -8.830 1.00 23.63 ? 114 VAL A N 1 ATOM 716 C CA . VAL A 1 93 ? 23.605 -41.688 -7.772 1.00 22.90 ? 114 VAL A CA 1 ATOM 717 C C . VAL A 1 93 ? 24.327 -42.603 -6.762 1.00 26.28 ? 114 VAL A C 1 ATOM 718 O O . VAL A 1 93 ? 23.930 -43.756 -6.562 1.00 25.34 ? 114 VAL A O 1 ATOM 719 C CB . VAL A 1 93 ? 22.584 -40.742 -7.061 1.00 22.32 ? 114 VAL A CB 1 ATOM 720 C CG1 . VAL A 1 93 ? 21.700 -41.528 -6.122 1.00 22.48 ? 114 VAL A CG1 1 ATOM 721 C CG2 . VAL A 1 93 ? 23.319 -39.674 -6.293 1.00 25.72 ? 114 VAL A CG2 1 ATOM 722 N N . ASN A 1 94 ? 25.414 -42.105 -6.171 1.00 29.55 ? 115 ASN A N 1 ATOM 723 C CA . ASN A 1 94 ? 26.110 -42.824 -5.106 1.00 36.60 ? 115 ASN A CA 1 ATOM 724 C C . ASN A 1 94 ? 25.640 -42.369 -3.723 1.00 36.76 ? 115 ASN A C 1 ATOM 725 O O . ASN A 1 94 ? 26.191 -41.405 -3.153 1.00 38.93 ? 115 ASN A O 1 ATOM 726 C CB . ASN A 1 94 ? 27.625 -42.618 -5.209 1.00 44.09 ? 115 ASN A CB 1 ATOM 727 C CG . ASN A 1 94 ? 28.201 -43.149 -6.507 1.00 51.40 ? 115 ASN A CG 1 ATOM 728 O OD1 . ASN A 1 94 ? 27.899 -44.271 -6.917 1.00 51.88 ? 115 ASN A OD1 1 ATOM 729 N ND2 . ASN A 1 94 ? 29.025 -42.342 -7.165 1.00 58.40 ? 115 ASN A ND2 1 ATOM 730 N N . GLN A 1 95 ? 24.632 -43.051 -3.185 1.00 32.31 ? 116 GLN A N 1 ATOM 731 C CA . GLN A 1 95 ? 24.142 -42.752 -1.839 1.00 30.79 ? 116 GLN A CA 1 ATOM 732 C C . GLN A 1 95 ? 23.810 -44.018 -1.090 1.00 30.63 ? 116 GLN A C 1 ATOM 733 O O . GLN A 1 95 ? 23.449 -45.019 -1.696 1.00 31.04 ? 116 GLN A O 1 ATOM 734 C CB . GLN A 1 95 ? 22.918 -41.832 -1.873 1.00 27.94 ? 116 GLN A CB 1 ATOM 735 C CG . GLN A 1 95 ? 23.275 -40.380 -2.175 1.00 29.66 ? 116 GLN A CG 1 ATOM 736 C CD . GLN A 1 95 ? 22.074 -39.438 -2.149 1.00 28.03 ? 116 GLN A CD 1 ATOM 737 O OE1 . GLN A 1 95 ? 21.184 -39.511 -3.001 1.00 25.84 ? 116 GLN A OE1 1 ATOM 738 N NE2 . GLN A 1 95 ? 22.067 -38.524 -1.183 1.00 30.02 ? 116 GLN A NE2 1 ATOM 739 N N . SER A 1 96 ? 23.901 -43.961 0.234 1.00 29.39 ? 117 SER A N 1 ATOM 740 C CA . SER A 1 96 ? 23.773 -45.170 1.027 1.00 29.81 ? 117 SER A CA 1 ATOM 741 C C . SER A 1 96 ? 22.328 -45.647 1.058 1.00 28.51 ? 117 SER A C 1 ATOM 742 O O . SER A 1 96 ? 22.095 -46.825 1.257 1.00 28.41 ? 117 SER A O 1 ATOM 743 C CB . SER A 1 96 ? 24.266 -44.944 2.447 1.00 29.71 ? 117 SER A CB 1 ATOM 744 O OG . SER A 1 96 ? 23.363 -44.094 3.134 1.00 30.46 ? 117 SER A OG 1 ATOM 745 N N . TRP A 1 97 ? 21.370 -44.736 0.849 1.00 27.06 ? 118 TRP A N 1 ATOM 746 C CA . TRP A 1 97 ? 19.941 -45.036 1.053 1.00 25.57 ? 118 TRP A CA 1 ATOM 747 C C . TRP A 1 97 ? 19.090 -45.045 -0.221 1.00 25.08 ? 118 TRP A C 1 ATOM 748 O O . TRP A 1 97 ? 17.886 -45.263 -0.147 1.00 24.29 ? 118 TRP A O 1 ATOM 749 C CB . TRP A 1 97 ? 19.309 -44.084 2.083 1.00 25.44 ? 118 TRP A CB 1 ATOM 750 C CG . TRP A 1 97 ? 19.613 -42.632 1.804 1.00 24.89 ? 118 TRP A CG 1 ATOM 751 C CD1 . TRP A 1 97 ? 20.777 -41.978 2.104 1.00 26.48 ? 118 TRP A CD1 1 ATOM 752 C CD2 . TRP A 1 97 ? 18.771 -41.673 1.141 1.00 22.49 ? 118 TRP A CD2 1 ATOM 753 N NE1 . TRP A 1 97 ? 20.718 -40.671 1.668 1.00 26.66 ? 118 TRP A NE1 1 ATOM 754 C CE2 . TRP A 1 97 ? 19.498 -40.452 1.082 1.00 25.47 ? 118 TRP A CE2 1 ATOM 755 C CE3 . TRP A 1 97 ? 17.485 -41.720 0.593 1.00 22.08 ? 118 TRP A CE3 1 ATOM 756 C CZ2 . TRP A 1 97 ? 18.971 -39.280 0.494 1.00 25.30 ? 118 TRP A CZ2 1 ATOM 757 C CZ3 . TRP A 1 97 ? 16.943 -40.546 0.020 1.00 22.68 ? 118 TRP A CZ3 1 ATOM 758 C CH2 . TRP A 1 97 ? 17.700 -39.349 -0.032 1.00 24.06 ? 118 TRP A CH2 1 ATOM 759 N N . ARG A 1 98 ? 19.705 -44.790 -1.378 1.00 24.21 ? 119 ARG A N 1 ATOM 760 C CA . ARG A 1 98 ? 19.050 -45.001 -2.671 1.00 19.57 ? 119 ARG A CA 1 ATOM 761 C C . ARG A 1 98 ? 20.121 -45.125 -3.737 1.00 21.26 ? 119 ARG A C 1 ATOM 762 O O . ARG A 1 98 ? 21.238 -44.638 -3.540 1.00 22.55 ? 119 ARG A O 1 ATOM 763 C CB . ARG A 1 98 ? 18.083 -43.853 -3.018 1.00 19.99 ? 119 ARG A CB 1 ATOM 764 C CG . ARG A 1 98 ? 18.719 -42.489 -3.106 1.00 20.22 ? 119 ARG A CG 1 ATOM 765 C CD . ARG A 1 98 ? 17.706 -41.377 -3.458 1.00 21.50 ? 119 ARG A CD 1 ATOM 766 N NE . ARG A 1 98 ? 18.370 -40.081 -3.446 1.00 23.46 ? 119 ARG A NE 1 ATOM 767 C CZ . ARG A 1 98 ? 17.752 -38.899 -3.472 1.00 22.35 ? 119 ARG A CZ 1 ATOM 768 N NH1 . ARG A 1 98 ? 16.424 -38.833 -3.517 1.00 17.92 ? 119 ARG A NH1 1 ATOM 769 N NH2 . ARG A 1 98 ? 18.483 -37.783 -3.448 1.00 18.73 ? 119 ARG A NH2 1 ATOM 770 N N . LYS A 1 99 ? 19.789 -45.788 -4.846 1.00 20.86 ? 120 LYS A N 1 ATOM 771 C CA . LYS A 1 99 ? 20.707 -45.959 -5.993 1.00 20.32 ? 120 LYS A CA 1 ATOM 772 C C . LYS A 1 99 ? 20.411 -44.963 -7.131 1.00 21.14 ? 120 LYS A C 1 ATOM 773 O O . LYS A 1 99 ? 21.221 -44.755 -8.024 1.00 23.60 ? 120 LYS A O 1 ATOM 774 C CB . LYS A 1 99 ? 20.622 -47.410 -6.520 1.00 21.08 ? 120 LYS A CB 1 ATOM 775 N N . GLU A 1 100 ? 19.238 -44.358 -7.095 1.00 20.52 ? 121 GLU A N 1 ATOM 776 C CA . GLU A 1 100 ? 18.822 -43.403 -8.137 1.00 22.74 ? 121 GLU A CA 1 ATOM 777 C C . GLU A 1 100 ? 18.068 -42.236 -7.540 1.00 22.06 ? 121 GLU A C 1 ATOM 778 O O . GLU A 1 100 ? 17.530 -42.324 -6.411 1.00 21.36 ? 121 GLU A O 1 ATOM 779 C CB . GLU A 1 100 ? 17.912 -44.077 -9.176 1.00 23.31 ? 121 GLU A CB 1 ATOM 780 C CG . GLU A 1 100 ? 18.579 -45.237 -9.910 1.00 25.22 ? 121 GLU A CG 1 ATOM 781 C CD . GLU A 1 100 ? 17.639 -45.975 -10.854 1.00 25.96 ? 121 GLU A CD 1 ATOM 782 O OE1 . GLU A 1 100 ? 18.108 -46.359 -11.932 1.00 28.29 ? 121 GLU A OE1 1 ATOM 783 O OE2 . GLU A 1 100 ? 16.455 -46.203 -10.523 1.00 26.41 ? 121 GLU A OE2 1 ATOM 784 N N . ARG A 1 101 ? 18.000 -41.147 -8.302 1.00 20.44 ? 122 ARG A N 1 ATOM 785 C CA . ARG A 1 101 ? 17.164 -40.021 -7.913 1.00 22.81 ? 122 ARG A CA 1 ATOM 786 C C . ARG A 1 101 ? 16.727 -39.294 -9.189 1.00 21.98 ? 122 ARG A C 1 ATOM 787 O O . ARG A 1 101 ? 17.002 -39.759 -10.305 1.00 22.21 ? 122 ARG A O 1 ATOM 788 C CB . ARG A 1 101 ? 17.940 -39.082 -6.995 1.00 28.49 ? 122 ARG A CB 1 ATOM 789 C CG . ARG A 1 101 ? 19.109 -38.379 -7.693 1.00 37.77 ? 122 ARG A CG 1 ATOM 790 C CD . ARG A 1 101 ? 19.715 -37.344 -6.768 1.00 46.04 ? 122 ARG A CD 1 ATOM 791 N NE . ARG A 1 101 ? 20.397 -36.258 -7.467 1.00 53.81 ? 122 ARG A NE 1 ATOM 792 C CZ . ARG A 1 101 ? 19.832 -35.093 -7.771 1.00 57.92 ? 122 ARG A CZ 1 ATOM 793 N NH1 . ARG A 1 101 ? 20.536 -34.160 -8.385 1.00 59.49 ? 122 ARG A NH1 1 ATOM 794 N NH2 . ARG A 1 101 ? 18.565 -34.852 -7.454 1.00 59.06 ? 122 ARG A NH2 1 ATOM 795 N N . PHE A 1 102 ? 16.053 -38.165 -9.038 1.00 19.76 ? 123 PHE A N 1 ATOM 796 C CA . PHE A 1 102 ? 15.527 -37.451 -10.203 1.00 20.53 ? 123 PHE A CA 1 ATOM 797 C C . PHE A 1 102 ? 16.297 -36.188 -10.370 1.00 20.08 ? 123 PHE A C 1 ATOM 798 O O . PHE A 1 102 ? 16.710 -35.591 -9.381 1.00 17.95 ? 123 PHE A O 1 ATOM 799 C CB . PHE A 1 102 ? 14.072 -37.038 -9.976 1.00 24.27 ? 123 PHE A CB 1 ATOM 800 C CG . PHE A 1 102 ? 13.172 -38.175 -9.636 1.00 24.19 ? 123 PHE A CG 1 ATOM 801 C CD1 . PHE A 1 102 ? 12.457 -38.167 -8.457 1.00 24.21 ? 123 PHE A CD1 1 ATOM 802 C CD2 . PHE A 1 102 ? 13.069 -39.255 -10.483 1.00 23.89 ? 123 PHE A CD2 1 ATOM 803 C CE1 . PHE A 1 102 ? 11.627 -39.218 -8.130 1.00 26.34 ? 123 PHE A CE1 1 ATOM 804 C CE2 . PHE A 1 102 ? 12.230 -40.315 -10.172 1.00 27.00 ? 123 PHE A CE2 1 ATOM 805 C CZ . PHE A 1 102 ? 11.506 -40.303 -8.993 1.00 27.04 ? 123 PHE A CZ 1 ATOM 806 N N . LEU A 1 103 ? 16.434 -35.758 -11.623 1.00 20.07 ? 124 LEU A N 1 ATOM 807 C CA . LEU A 1 103 ? 17.097 -34.503 -11.968 1.00 17.11 ? 124 LEU A CA 1 ATOM 808 C C . LEU A 1 103 ? 16.294 -33.732 -13.030 1.00 15.05 ? 124 LEU A C 1 ATOM 809 O O . LEU A 1 103 ? 15.938 -34.307 -14.062 1.00 14.22 ? 124 LEU A O 1 ATOM 810 C CB . LEU A 1 103 ? 18.515 -34.789 -12.496 1.00 16.41 ? 124 LEU A CB 1 ATOM 811 C CG . LEU A 1 103 ? 19.362 -33.576 -12.927 1.00 16.86 ? 124 LEU A CG 1 ATOM 812 C CD1 . LEU A 1 103 ? 19.741 -32.729 -11.723 1.00 15.09 ? 124 LEU A CD1 1 ATOM 813 C CD2 . LEU A 1 103 ? 20.656 -33.996 -13.659 1.00 17.33 ? 124 LEU A CD2 1 ATOM 814 N N . ASP A 1 104 ? 16.057 -32.438 -12.792 1.00 14.38 ? 125 ASP A N 1 ATOM 815 C CA . ASP A 1 104 ? 15.454 -31.536 -13.793 1.00 15.19 ? 125 ASP A CA 1 ATOM 816 C C . ASP A 1 104 ? 14.030 -31.960 -14.281 1.00 16.13 ? 125 ASP A C 1 ATOM 817 O O . ASP A 1 104 ? 13.668 -31.737 -15.445 1.00 14.79 ? 125 ASP A O 1 ATOM 818 C CB . ASP A 1 104 ? 16.417 -31.344 -14.973 1.00 13.18 ? 125 ASP A CB 1 ATOM 819 C CG . ASP A 1 104 ? 17.611 -30.393 -14.623 1.00 20.94 ? 125 ASP A CG 1 ATOM 820 O OD1 . ASP A 1 104 ? 17.354 -29.293 -14.070 1.00 16.58 ? 125 ASP A OD1 1 ATOM 821 O OD2 . ASP A 1 104 ? 18.789 -30.743 -14.919 1.00 20.78 ? 125 ASP A OD2 1 ATOM 822 N N . VAL A 1 105 ? 13.258 -32.593 -13.391 1.00 14.55 ? 126 VAL A N 1 ATOM 823 C CA . VAL A 1 105 ? 11.831 -32.812 -13.628 1.00 14.13 ? 126 VAL A CA 1 ATOM 824 C C . VAL A 1 105 ? 11.125 -31.453 -13.904 1.00 13.27 ? 126 VAL A C 1 ATOM 825 O O . VAL A 1 105 ? 11.228 -30.533 -13.108 1.00 11.55 ? 126 VAL A O 1 ATOM 826 C CB . VAL A 1 105 ? 11.194 -33.570 -12.437 1.00 13.25 ? 126 VAL A CB 1 ATOM 827 C CG1 . VAL A 1 105 ? 9.644 -33.669 -12.583 1.00 17.65 ? 126 VAL A CG1 1 ATOM 828 C CG2 . VAL A 1 105 ? 11.806 -34.966 -12.353 1.00 14.12 ? 126 VAL A CG2 1 ATOM 829 N N . PRO A 1 106 ? 10.437 -31.336 -15.056 1.00 13.06 ? 127 PRO A N 1 ATOM 830 C CA . PRO A 1 106 ? 9.824 -30.067 -15.467 1.00 12.74 ? 127 PRO A CA 1 ATOM 831 C C . PRO A 1 106 ? 8.506 -29.802 -14.729 1.00 16.74 ? 127 PRO A C 1 ATOM 832 O O . PRO A 1 106 ? 7.426 -30.096 -15.248 1.00 17.74 ? 127 PRO A O 1 ATOM 833 C CB . PRO A 1 106 ? 9.548 -30.296 -16.957 1.00 12.90 ? 127 PRO A CB 1 ATOM 834 C CG . PRO A 1 106 ? 9.299 -31.765 -17.079 1.00 12.96 ? 127 PRO A CG 1 ATOM 835 C CD . PRO A 1 106 ? 10.239 -32.398 -16.066 1.00 13.35 ? 127 PRO A CD 1 ATOM 836 N N . LEU A 1 107 ? 8.611 -29.243 -13.538 1.00 16.01 ? 128 LEU A N 1 ATOM 837 C CA . LEU A 1 107 ? 7.468 -28.885 -12.717 1.00 20.01 ? 128 LEU A CA 1 ATOM 838 C C . LEU A 1 107 ? 6.707 -27.688 -13.294 1.00 19.46 ? 128 LEU A C 1 ATOM 839 O O . LEU A 1 107 ? 7.294 -26.651 -13.592 1.00 19.65 ? 128 LEU A O 1 ATOM 840 C CB . LEU A 1 107 ? 7.952 -28.561 -11.302 1.00 20.38 ? 128 LEU A CB 1 ATOM 841 C CG . LEU A 1 107 ? 6.856 -28.232 -10.294 1.00 21.23 ? 128 LEU A CG 1 ATOM 842 C CD1 . LEU A 1 107 ? 5.868 -29.409 -10.123 1.00 19.01 ? 128 LEU A CD1 1 ATOM 843 C CD2 . LEU A 1 107 ? 7.493 -27.865 -8.949 1.00 19.20 ? 128 LEU A CD2 1 ATOM 844 N N . CYS A 1 108 ? 5.396 -27.841 -13.459 1.00 21.49 ? 129 CYS A N 1 ATOM 845 C CA . CYS A 1 108 ? 4.541 -26.775 -14.014 1.00 19.21 ? 129 CYS A CA 1 ATOM 846 C C . CYS A 1 108 ? 4.696 -25.522 -13.153 1.00 15.83 ? 129 CYS A C 1 ATOM 847 O O . CYS A 1 108 ? 4.654 -25.603 -11.925 1.00 15.83 ? 129 CYS A O 1 ATOM 848 C CB . CYS A 1 108 ? 3.061 -27.221 -14.058 1.00 19.87 ? 129 CYS A CB 1 ATOM 849 S SG . CYS A 1 108 ? 2.671 -28.667 -15.160 1.00 24.86 ? 129 CYS A SG 1 ATOM 850 N N . LYS A 1 109 ? 4.846 -24.365 -13.798 1.00 20.88 ? 130 LYS A N 1 ATOM 851 C CA . LYS A 1 109 ? 5.250 -23.166 -13.066 1.00 20.21 ? 130 LYS A CA 1 ATOM 852 C C . LYS A 1 109 ? 4.249 -22.801 -11.987 1.00 19.32 ? 130 LYS A C 1 ATOM 853 O O . LYS A 1 109 ? 4.630 -22.390 -10.895 1.00 16.92 ? 130 LYS A O 1 ATOM 854 C CB . LYS A 1 109 ? 5.490 -21.986 -14.014 1.00 22.33 ? 130 LYS A CB 1 ATOM 855 C CG . LYS A 1 109 ? 4.399 -21.770 -15.019 1.00 25.44 ? 130 LYS A CG 1 ATOM 856 C CD . LYS A 1 109 ? 4.871 -20.759 -16.069 1.00 31.52 ? 130 LYS A CD 1 ATOM 857 C CE . LYS A 1 109 ? 3.720 -20.312 -16.978 1.00 33.55 ? 130 LYS A CE 1 ATOM 858 N NZ . LYS A 1 109 ? 4.208 -19.401 -18.046 1.00 37.52 ? 130 LYS A NZ 1 ATOM 859 N N . GLU A 1 110 ? 2.960 -22.989 -12.274 1.00 20.54 ? 131 GLU A N 1 ATOM 860 C CA . GLU A 1 110 ? 1.956 -22.680 -11.262 1.00 22.24 ? 131 GLU A CA 1 ATOM 861 C C . GLU A 1 110 ? 2.083 -23.528 -9.985 1.00 19.64 ? 131 GLU A C 1 ATOM 862 O O . GLU A 1 110 ? 1.886 -23.013 -8.885 1.00 19.59 ? 131 GLU A O 1 ATOM 863 C CB . GLU A 1 110 ? 0.546 -22.737 -11.835 1.00 26.97 ? 131 GLU A CB 1 ATOM 864 C CG . GLU A 1 110 ? 0.316 -21.707 -12.942 1.00 35.74 ? 131 GLU A CG 1 ATOM 865 C CD . GLU A 1 110 ? 0.619 -22.237 -14.359 1.00 41.53 ? 131 GLU A CD 1 ATOM 866 O OE1 . GLU A 1 110 ? 1.224 -23.336 -14.495 1.00 40.45 ? 131 GLU A OE1 1 ATOM 867 O OE2 . GLU A 1 110 ? 0.230 -21.545 -15.334 1.00 44.36 ? 131 GLU A OE2 1 ATOM 868 N N . ASP A 1 111 ? 2.411 -24.812 -10.106 1.00 17.37 ? 132 ASP A N 1 ATOM 869 C CA . ASP A 1 111 ? 2.611 -25.620 -8.891 1.00 15.56 ? 132 ASP A CA 1 ATOM 870 C C . ASP A 1 111 ? 3.780 -25.085 -8.038 1.00 18.75 ? 132 ASP A C 1 ATOM 871 O O . ASP A 1 111 ? 3.699 -25.039 -6.796 1.00 18.82 ? 132 ASP A O 1 ATOM 872 C CB . ASP A 1 111 ? 2.836 -27.101 -9.221 1.00 16.78 ? 132 ASP A CB 1 ATOM 873 C CG . ASP A 1 111 ? 1.522 -27.840 -9.490 1.00 21.05 ? 132 ASP A CG 1 ATOM 874 O OD1 . ASP A 1 111 ? 0.471 -27.187 -9.364 1.00 22.74 ? 132 ASP A OD1 1 ATOM 875 O OD2 . ASP A 1 111 ? 1.548 -29.050 -9.827 1.00 24.20 ? 132 ASP A OD2 1 ATOM 876 N N . CYS A 1 112 ? 4.860 -24.680 -8.708 1.00 16.37 ? 133 CYS A N 1 ATOM 877 C CA . CYS A 1 112 ? 5.983 -24.095 -7.986 1.00 15.71 ? 133 CYS A CA 1 ATOM 878 C C . CYS A 1 112 ? 5.543 -22.759 -7.362 1.00 16.26 ? 133 CYS A C 1 ATOM 879 O O . CYS A 1 112 ? 5.764 -22.521 -6.160 1.00 15.81 ? 133 CYS A O 1 ATOM 880 C CB . CYS A 1 112 ? 7.199 -23.879 -8.902 1.00 16.56 ? 133 CYS A CB 1 ATOM 881 S SG . CYS A 1 112 ? 8.577 -23.226 -7.939 1.00 28.04 ? 133 CYS A SG 1 ATOM 882 N N . GLN A 1 113 ? 4.931 -21.896 -8.179 1.00 13.76 ? 134 GLN A N 1 ATOM 883 C CA . GLN A 1 113 ? 4.455 -20.597 -7.681 1.00 17.99 ? 134 GLN A CA 1 ATOM 884 C C . GLN A 1 113 ? 3.557 -20.748 -6.425 1.00 25.17 ? 134 GLN A C 1 ATOM 885 O O . GLN A 1 113 ? 3.762 -20.064 -5.406 1.00 22.93 ? 134 GLN A O 1 ATOM 886 C CB . GLN A 1 113 ? 3.664 -19.848 -8.751 1.00 16.19 ? 134 GLN A CB 1 ATOM 887 C CG . GLN A 1 113 ? 3.310 -18.380 -8.359 1.00 27.35 ? 134 GLN A CG 1 ATOM 888 C CD . GLN A 1 113 ? 4.523 -17.436 -8.472 1.00 30.90 ? 134 GLN A CD 1 ATOM 889 O OE1 . GLN A 1 113 ? 5.346 -17.585 -9.378 1.00 33.45 ? 134 GLN A OE1 1 ATOM 890 N NE2 . GLN A 1 113 ? 4.637 -16.474 -7.549 1.00 29.12 ? 134 GLN A NE2 1 ATOM 891 N N . ARG A 1 114 ? 2.544 -21.618 -6.529 1.00 20.15 ? 135 ARG A N 1 ATOM 892 C CA . ARG A 1 114 ? 1.579 -21.799 -5.446 1.00 18.83 ? 135 ARG A CA 1 ATOM 893 C C . ARG A 1 114 ? 2.270 -22.306 -4.171 1.00 19.79 ? 135 ARG A C 1 ATOM 894 O O . ARG A 1 114 ? 1.941 -21.879 -3.054 1.00 20.29 ? 135 ARG A O 1 ATOM 895 C CB . ARG A 1 114 ? 0.465 -22.768 -5.878 1.00 17.20 ? 135 ARG A CB 1 ATOM 896 C CG . ARG A 1 114 ? -0.570 -23.112 -4.797 1.00 18.48 ? 135 ARG A CG 1 ATOM 897 C CD . ARG A 1 114 ? -1.412 -21.895 -4.344 1.00 19.82 ? 135 ARG A CD 1 ATOM 898 N NE . ARG A 1 114 ? -2.471 -22.301 -3.414 1.00 20.97 ? 135 ARG A NE 1 ATOM 899 C CZ . ARG A 1 114 ? -3.735 -22.551 -3.763 1.00 24.33 ? 135 ARG A CZ 1 ATOM 900 N NH1 . ARG A 1 114 ? -4.130 -22.411 -5.037 1.00 23.61 ? 135 ARG A NH1 1 ATOM 901 N NH2 . ARG A 1 114 ? -4.615 -22.929 -2.830 1.00 25.18 ? 135 ARG A NH2 1 ATOM 902 N N . TRP A 1 115 ? 3.218 -23.232 -4.353 1.00 18.67 ? 136 TRP A N 1 ATOM 903 C CA . TRP A 1 115 ? 3.975 -23.827 -3.260 1.00 15.15 ? 136 TRP A CA 1 ATOM 904 C C . TRP A 1 115 ? 4.755 -22.702 -2.570 1.00 15.77 ? 136 TRP A C 1 ATOM 905 O O . TRP A 1 115 ? 4.699 -22.543 -1.347 1.00 16.35 ? 136 TRP A O 1 ATOM 906 C CB . TRP A 1 115 ? 4.969 -24.845 -3.848 1.00 15.29 ? 136 TRP A CB 1 ATOM 907 C CG . TRP A 1 115 ? 5.755 -25.705 -2.857 1.00 15.70 ? 136 TRP A CG 1 ATOM 908 C CD1 . TRP A 1 115 ? 5.784 -25.590 -1.489 1.00 15.85 ? 136 TRP A CD1 1 ATOM 909 C CD2 . TRP A 1 115 ? 6.618 -26.813 -3.191 1.00 14.88 ? 136 TRP A CD2 1 ATOM 910 N NE1 . TRP A 1 115 ? 6.629 -26.564 -0.962 1.00 19.01 ? 136 TRP A NE1 1 ATOM 911 C CE2 . TRP A 1 115 ? 7.140 -27.326 -1.983 1.00 15.35 ? 136 TRP A CE2 1 ATOM 912 C CE3 . TRP A 1 115 ? 7.000 -27.417 -4.402 1.00 16.74 ? 136 TRP A CE3 1 ATOM 913 C CZ2 . TRP A 1 115 ? 8.038 -28.429 -1.942 1.00 13.97 ? 136 TRP A CZ2 1 ATOM 914 C CZ3 . TRP A 1 115 ? 7.887 -28.529 -4.360 1.00 18.56 ? 136 TRP A CZ3 1 ATOM 915 C CH2 . TRP A 1 115 ? 8.391 -29.009 -3.134 1.00 16.86 ? 136 TRP A CH2 1 ATOM 916 N N . TRP A 1 116 ? 5.496 -21.928 -3.360 1.00 13.07 ? 137 TRP A N 1 ATOM 917 C CA . TRP A 1 116 ? 6.313 -20.861 -2.793 1.00 17.41 ? 137 TRP A CA 1 ATOM 918 C C . TRP A 1 116 ? 5.449 -19.873 -2.037 1.00 19.08 ? 137 TRP A C 1 ATOM 919 O O . TRP A 1 116 ? 5.735 -19.536 -0.881 1.00 17.57 ? 137 TRP A O 1 ATOM 920 C CB . TRP A 1 116 ? 7.080 -20.134 -3.893 1.00 18.70 ? 137 TRP A CB 1 ATOM 921 C CG . TRP A 1 116 ? 8.009 -19.062 -3.461 1.00 20.52 ? 137 TRP A CG 1 ATOM 922 C CD1 . TRP A 1 116 ? 9.265 -19.212 -2.920 1.00 18.97 ? 137 TRP A CD1 1 ATOM 923 C CD2 . TRP A 1 116 ? 7.810 -17.650 -3.634 1.00 21.50 ? 137 TRP A CD2 1 ATOM 924 N NE1 . TRP A 1 116 ? 9.852 -17.969 -2.740 1.00 18.37 ? 137 TRP A NE1 1 ATOM 925 C CE2 . TRP A 1 116 ? 8.976 -16.997 -3.156 1.00 23.72 ? 137 TRP A CE2 1 ATOM 926 C CE3 . TRP A 1 116 ? 6.762 -16.876 -4.145 1.00 22.35 ? 137 TRP A CE3 1 ATOM 927 C CZ2 . TRP A 1 116 ? 9.113 -15.588 -3.166 1.00 24.85 ? 137 TRP A CZ2 1 ATOM 928 C CZ3 . TRP A 1 116 ? 6.902 -15.469 -4.170 1.00 25.01 ? 137 TRP A CZ3 1 ATOM 929 C CH2 . TRP A 1 116 ? 8.068 -14.845 -3.677 1.00 25.41 ? 137 TRP A CH2 1 ATOM 930 N N . GLU A 1 117 ? 4.361 -19.434 -2.657 1.00 20.21 ? 138 GLU A N 1 ATOM 931 C CA . GLU A 1 117 ? 3.480 -18.475 -1.981 1.00 21.69 ? 138 GLU A CA 1 ATOM 932 C C . GLU A 1 117 ? 2.896 -19.014 -0.671 1.00 20.13 ? 138 GLU A C 1 ATOM 933 O O . GLU A 1 117 ? 2.824 -18.300 0.330 1.00 21.40 ? 138 GLU A O 1 ATOM 934 C CB . GLU A 1 117 ? 2.351 -18.028 -2.916 1.00 25.99 ? 138 GLU A CB 1 ATOM 935 C CG . GLU A 1 117 ? 2.864 -17.101 -4.023 1.00 31.76 ? 138 GLU A CG 1 ATOM 936 C CD . GLU A 1 117 ? 1.826 -16.846 -5.094 1.00 37.76 ? 138 GLU A CD 1 ATOM 937 O OE1 . GLU A 1 117 ? 0.808 -17.586 -5.141 1.00 41.47 ? 138 GLU A OE1 1 ATOM 938 O OE2 . GLU A 1 117 ? 2.034 -15.925 -5.900 1.00 38.63 ? 138 GLU A OE2 1 ATOM 939 N N . ASP A 1 118 ? 2.460 -20.264 -0.678 1.00 16.29 ? 139 ASP A N 1 ATOM 940 C CA . ASP A 1 118 ? 1.770 -20.806 0.485 1.00 17.32 ? 139 ASP A CA 1 ATOM 941 C C . ASP A 1 118 ? 2.773 -21.004 1.641 1.00 18.28 ? 139 ASP A C 1 ATOM 942 O O . ASP A 1 118 ? 2.362 -21.207 2.774 1.00 20.53 ? 139 ASP A O 1 ATOM 943 C CB . ASP A 1 118 ? 1.116 -22.145 0.148 1.00 17.12 ? 139 ASP A CB 1 ATOM 944 C CG . ASP A 1 118 ? -0.260 -21.994 -0.524 1.00 22.27 ? 139 ASP A CG 1 ATOM 945 O OD1 . ASP A 1 118 ? -0.779 -20.852 -0.587 1.00 24.18 ? 139 ASP A OD1 1 ATOM 946 O OD2 . ASP A 1 118 ? -0.811 -23.023 -0.991 1.00 18.56 ? 139 ASP A OD2 1 ATOM 947 N N . CYS A 1 119 ? 4.074 -20.997 1.340 1.00 13.68 ? 140 CYS A N 1 ATOM 948 C CA . CYS A 1 119 ? 5.093 -21.166 2.374 1.00 15.67 ? 140 CYS A CA 1 ATOM 949 C C . CYS A 1 119 ? 5.738 -19.857 2.907 1.00 20.24 ? 140 CYS A C 1 ATOM 950 O O . CYS A 1 119 ? 6.615 -19.915 3.765 1.00 21.33 ? 140 CYS A O 1 ATOM 951 C CB . CYS A 1 119 ? 6.191 -22.135 1.891 1.00 15.71 ? 140 CYS A CB 1 ATOM 952 S SG . CYS A 1 119 ? 5.540 -23.826 1.722 1.00 22.83 ? 140 CYS A SG 1 ATOM 953 N N . HIS A 1 120 ? 5.308 -18.696 2.417 1.00 23.84 ? 141 HIS A N 1 ATOM 954 C CA . HIS A 1 120 ? 5.895 -17.426 2.859 1.00 26.01 ? 141 HIS A CA 1 ATOM 955 C C . HIS A 1 120 ? 5.897 -17.227 4.380 1.00 26.44 ? 141 HIS A C 1 ATOM 956 O O . HIS A 1 120 ? 6.851 -16.683 4.937 1.00 25.53 ? 141 HIS A O 1 ATOM 957 C CB . HIS A 1 120 ? 5.210 -16.219 2.193 1.00 30.00 ? 141 HIS A CB 1 ATOM 958 C CG . HIS A 1 120 ? 5.700 -15.951 0.810 1.00 33.82 ? 141 HIS A CG 1 ATOM 959 N ND1 . HIS A 1 120 ? 5.094 -15.047 -0.039 1.00 40.56 ? 141 HIS A ND1 1 ATOM 960 C CD2 . HIS A 1 120 ? 6.735 -16.480 0.120 1.00 34.44 ? 141 HIS A CD2 1 ATOM 961 C CE1 . HIS A 1 120 ? 5.733 -15.041 -1.197 1.00 40.54 ? 141 HIS A CE1 1 ATOM 962 N NE2 . HIS A 1 120 ? 6.735 -15.901 -1.124 1.00 37.38 ? 141 HIS A NE2 1 ATOM 963 N N . THR A 1 121 ? 4.829 -17.648 5.055 1.00 25.59 ? 142 THR A N 1 ATOM 964 C CA . THR A 1 121 ? 4.767 -17.465 6.496 1.00 25.25 ? 142 THR A CA 1 ATOM 965 C C . THR A 1 121 ? 5.491 -18.566 7.270 1.00 22.70 ? 142 THR A C 1 ATOM 966 O O . THR A 1 121 ? 5.455 -18.579 8.501 1.00 22.77 ? 142 THR A O 1 ATOM 967 C CB . THR A 1 121 ? 3.311 -17.340 7.001 1.00 27.28 ? 142 THR A CB 1 ATOM 968 O OG1 . THR A 1 121 ? 2.518 -18.405 6.448 1.00 26.06 ? 142 THR A OG1 1 ATOM 969 C CG2 . THR A 1 121 ? 2.715 -15.965 6.577 1.00 27.77 ? 142 THR A CG2 1 ATOM 970 N N . SER A 1 122 ? 6.142 -19.491 6.567 1.00 20.59 ? 143 SER A N 1 ATOM 971 C CA . SER A 1 122 ? 6.898 -20.527 7.275 1.00 20.14 ? 143 SER A CA 1 ATOM 972 C C . SER A 1 122 ? 8.407 -20.162 7.420 1.00 21.98 ? 143 SER A C 1 ATOM 973 O O . SER A 1 122 ? 8.847 -19.129 6.941 1.00 20.60 ? 143 SER A O 1 ATOM 974 C CB . SER A 1 122 ? 6.668 -21.901 6.640 1.00 19.35 ? 143 SER A CB 1 ATOM 975 O OG . SER A 1 122 ? 5.275 -22.254 6.713 1.00 21.92 ? 143 SER A OG 1 ATOM 976 N N . HIS A 1 123 ? 9.172 -21.007 8.102 1.00 20.48 ? 144 HIS A N 1 ATOM 977 C CA . HIS A 1 123 ? 10.559 -20.709 8.418 1.00 20.28 ? 144 HIS A CA 1 ATOM 978 C C . HIS A 1 123 ? 11.492 -21.881 8.090 1.00 20.06 ? 144 HIS A C 1 ATOM 979 O O . HIS A 1 123 ? 11.084 -23.023 8.094 1.00 16.21 ? 144 HIS A O 1 ATOM 980 C CB . HIS A 1 123 ? 10.691 -20.333 9.886 1.00 21.13 ? 144 HIS A CB 1 ATOM 981 C CG . HIS A 1 123 ? 10.005 -19.051 10.225 1.00 23.48 ? 144 HIS A CG 1 ATOM 982 N ND1 . HIS A 1 123 ? 8.679 -18.994 10.595 1.00 24.84 ? 144 HIS A ND1 1 ATOM 983 C CD2 . HIS A 1 123 ? 10.450 -17.774 10.212 1.00 24.15 ? 144 HIS A CD2 1 ATOM 984 C CE1 . HIS A 1 123 ? 8.341 -17.736 10.817 1.00 24.97 ? 144 HIS A CE1 1 ATOM 985 N NE2 . HIS A 1 123 ? 9.395 -16.975 10.583 1.00 25.42 ? 144 HIS A NE2 1 ATOM 986 N N . THR A 1 124 ? 12.753 -21.597 7.803 1.00 20.81 ? 145 THR A N 1 ATOM 987 C CA . THR A 1 124 ? 13.700 -22.694 7.630 1.00 18.75 ? 145 THR A CA 1 ATOM 988 C C . THR A 1 124 ? 15.080 -22.160 7.914 1.00 17.05 ? 145 THR A C 1 ATOM 989 O O . THR A 1 124 ? 15.248 -20.957 8.123 1.00 17.40 ? 145 THR A O 1 ATOM 990 C CB . THR A 1 124 ? 13.646 -23.351 6.220 1.00 16.55 ? 145 THR A CB 1 ATOM 991 O OG1 . THR A 1 124 ? 14.489 -24.524 6.203 1.00 15.17 ? 145 THR A OG1 1 ATOM 992 C CG2 . THR A 1 124 ? 14.115 -22.387 5.141 1.00 16.54 ? 145 THR A CG2 1 ATOM 993 N N . CYS A 1 125 ? 16.062 -23.055 7.926 1.00 13.41 ? 146 CYS A N 1 ATOM 994 C CA . CYS A 1 125 ? 17.420 -22.681 8.261 1.00 17.74 ? 146 CYS A CA 1 ATOM 995 C C . CYS A 1 125 ? 18.390 -23.057 7.127 1.00 18.61 ? 146 CYS A C 1 ATOM 996 O O . CYS A 1 125 ? 19.602 -22.873 7.267 1.00 18.40 ? 146 CYS A O 1 ATOM 997 C CB . CYS A 1 125 ? 17.833 -23.348 9.585 1.00 16.05 ? 146 CYS A CB 1 ATOM 998 S SG . CYS A 1 125 ? 17.882 -25.177 9.491 1.00 19.89 ? 146 CYS A SG 1 ATOM 999 N N . LYS A 1 126 ? 17.858 -23.617 6.031 1.00 16.81 ? 147 LYS A N 1 ATOM 1000 C CA . LYS A 1 126 ? 18.685 -24.100 4.910 1.00 16.38 ? 147 LYS A CA 1 ATOM 1001 C C . LYS A 1 126 ? 17.966 -23.963 3.561 1.00 18.05 ? 147 LYS A C 1 ATOM 1002 O O . LYS A 1 126 ? 16.741 -24.163 3.476 1.00 18.93 ? 147 LYS A O 1 ATOM 1003 C CB . LYS A 1 126 ? 19.078 -25.579 5.116 1.00 15.69 ? 147 LYS A CB 1 ATOM 1004 C CG . LYS A 1 126 ? 20.195 -25.844 6.184 1.00 18.94 ? 147 LYS A CG 1 ATOM 1005 C CD . LYS A 1 126 ? 20.229 -27.344 6.568 1.00 18.95 ? 147 LYS A CD 1 ATOM 1006 C CE . LYS A 1 126 ? 20.254 -28.244 5.325 1.00 18.23 ? 147 LYS A CE 1 ATOM 1007 N NZ . LYS A 1 126 ? 21.440 -28.033 4.433 1.00 17.10 ? 147 LYS A NZ 1 ATOM 1008 N N . SER A 1 127 ? 18.718 -23.654 2.505 1.00 14.91 ? 148 SER A N 1 ATOM 1009 C CA . SER A 1 127 ? 18.130 -23.535 1.169 1.00 17.03 ? 148 SER A CA 1 ATOM 1010 C C . SER A 1 127 ? 18.239 -24.848 0.374 1.00 18.38 ? 148 SER A C 1 ATOM 1011 O O . SER A 1 127 ? 17.787 -24.932 -0.756 1.00 21.37 ? 148 SER A O 1 ATOM 1012 C CB . SER A 1 127 ? 18.760 -22.382 0.376 1.00 18.46 ? 148 SER A CB 1 ATOM 1013 O OG . SER A 1 127 ? 20.136 -22.650 0.141 1.00 21.66 ? 148 SER A OG 1 ATOM 1014 N N . ASN A 1 128 ? 18.843 -25.864 0.966 1.00 17.35 ? 149 ASN A N 1 ATOM 1015 C CA . ASN A 1 128 ? 18.875 -27.199 0.352 1.00 17.60 ? 149 ASN A CA 1 ATOM 1016 C C . ASN A 1 128 ? 18.602 -28.206 1.453 1.00 17.59 ? 149 ASN A C 1 ATOM 1017 O O . ASN A 1 128 ? 19.308 -28.221 2.474 1.00 19.35 ? 149 ASN A O 1 ATOM 1018 C CB . ASN A 1 128 ? 20.214 -27.496 -0.337 1.00 16.69 ? 149 ASN A CB 1 ATOM 1019 C CG . ASN A 1 128 ? 20.300 -28.929 -0.847 1.00 20.29 ? 149 ASN A CG 1 ATOM 1020 O OD1 . ASN A 1 128 ? 20.071 -29.891 -0.095 1.00 22.40 ? 149 ASN A OD1 1 ATOM 1021 N ND2 . ASN A 1 128 ? 20.619 -29.083 -2.127 1.00 18.88 ? 149 ASN A ND2 1 ATOM 1022 N N . TRP A 1 129 ? 17.556 -29.011 1.283 1.00 17.52 ? 150 TRP A N 1 ATOM 1023 C CA . TRP A 1 129 ? 17.112 -29.869 2.376 1.00 17.54 ? 150 TRP A CA 1 ATOM 1024 C C . TRP A 1 129 ? 17.500 -31.333 2.159 1.00 19.10 ? 150 TRP A C 1 ATOM 1025 O O . TRP A 1 129 ? 17.128 -32.205 2.943 1.00 20.02 ? 150 TRP A O 1 ATOM 1026 C CB . TRP A 1 129 ? 15.584 -29.798 2.537 1.00 17.49 ? 150 TRP A CB 1 ATOM 1027 C CG . TRP A 1 129 ? 15.041 -28.519 3.096 1.00 17.41 ? 150 TRP A CG 1 ATOM 1028 C CD1 . TRP A 1 129 ? 15.715 -27.322 3.275 1.00 17.62 ? 150 TRP A CD1 1 ATOM 1029 C CD2 . TRP A 1 129 ? 13.684 -28.288 3.531 1.00 18.95 ? 150 TRP A CD2 1 ATOM 1030 N NE1 . TRP A 1 129 ? 14.849 -26.368 3.796 1.00 17.99 ? 150 TRP A NE1 1 ATOM 1031 C CE2 . TRP A 1 129 ? 13.601 -26.933 3.951 1.00 19.89 ? 150 TRP A CE2 1 ATOM 1032 C CE3 . TRP A 1 129 ? 12.529 -29.096 3.598 1.00 18.04 ? 150 TRP A CE3 1 ATOM 1033 C CZ2 . TRP A 1 129 ? 12.414 -26.380 4.462 1.00 20.41 ? 150 TRP A CZ2 1 ATOM 1034 C CZ3 . TRP A 1 129 ? 11.349 -28.541 4.084 1.00 18.71 ? 150 TRP A CZ3 1 ATOM 1035 C CH2 . TRP A 1 129 ? 11.298 -27.192 4.509 1.00 19.55 ? 150 TRP A CH2 1 ATOM 1036 N N . HIS A 1 130 ? 18.191 -31.604 1.065 1.00 16.34 ? 151 HIS A N 1 ATOM 1037 C CA . HIS A 1 130 ? 18.675 -32.952 0.758 1.00 16.70 ? 151 HIS A CA 1 ATOM 1038 C C . HIS A 1 130 ? 20.032 -33.229 1.467 1.00 21.03 ? 151 HIS A C 1 ATOM 1039 O O . HIS A 1 130 ? 20.217 -34.288 2.054 1.00 21.66 ? 151 HIS A O 1 ATOM 1040 C CB . HIS A 1 130 ? 18.736 -33.088 -0.771 1.00 17.83 ? 151 HIS A CB 1 ATOM 1041 C CG . HIS A 1 130 ? 19.575 -34.210 -1.270 1.00 23.62 ? 151 HIS A CG 1 ATOM 1042 N ND1 . HIS A 1 130 ? 20.285 -34.125 -2.451 1.00 27.99 ? 151 HIS A ND1 1 ATOM 1043 C CD2 . HIS A 1 130 ? 19.805 -35.452 -0.778 1.00 24.93 ? 151 HIS A CD2 1 ATOM 1044 C CE1 . HIS A 1 130 ? 20.936 -35.258 -2.655 1.00 29.04 ? 151 HIS A CE1 1 ATOM 1045 N NE2 . HIS A 1 130 ? 20.666 -36.080 -1.653 1.00 28.82 ? 151 HIS A NE2 1 ATOM 1046 N N . ARG A 1 131 ? 20.948 -32.259 1.455 1.00 22.85 ? 152 ARG A N 1 ATOM 1047 C CA . ARG A 1 131 ? 22.277 -32.440 2.073 1.00 23.73 ? 152 ARG A CA 1 ATOM 1048 C C . ARG A 1 131 ? 22.639 -31.388 3.115 1.00 20.99 ? 152 ARG A C 1 ATOM 1049 O O . ARG A 1 131 ? 22.343 -30.197 2.933 1.00 20.29 ? 152 ARG A O 1 ATOM 1050 C CB . ARG A 1 131 ? 23.389 -32.491 1.010 1.00 24.79 ? 152 ARG A CB 1 ATOM 1051 C CG . ARG A 1 131 ? 23.211 -33.589 -0.033 1.00 26.20 ? 152 ARG A CG 1 ATOM 1052 C CD . ARG A 1 131 ? 24.465 -33.726 -0.892 1.00 26.32 ? 152 ARG A CD 1 ATOM 1053 N NE . ARG A 1 131 ? 24.312 -34.731 -1.938 1.00 25.46 ? 152 ARG A NE 1 ATOM 1054 C CZ . ARG A 1 131 ? 24.676 -36.012 -1.816 1.00 26.31 ? 152 ARG A CZ 1 ATOM 1055 N NH1 . ARG A 1 131 ? 25.186 -36.470 -0.677 1.00 23.24 ? 152 ARG A NH1 1 ATOM 1056 N NH2 . ARG A 1 131 ? 24.517 -36.839 -2.844 1.00 27.17 ? 152 ARG A NH2 1 ATOM 1057 N N . GLY A 1 132 ? 23.272 -31.834 4.209 1.00 18.77 ? 153 GLY A N 1 ATOM 1058 C CA . GLY A 1 132 ? 23.901 -30.905 5.140 1.00 20.27 ? 153 GLY A CA 1 ATOM 1059 C C . GLY A 1 132 ? 23.257 -30.774 6.519 1.00 22.46 ? 153 GLY A C 1 ATOM 1060 O O . GLY A 1 132 ? 23.686 -29.944 7.336 1.00 20.84 ? 153 GLY A O 1 ATOM 1061 N N . TRP A 1 133 ? 22.238 -31.589 6.805 1.00 21.53 ? 154 TRP A N 1 ATOM 1062 C CA . TRP A 1 133 ? 21.618 -31.520 8.125 1.00 21.13 ? 154 TRP A CA 1 ATOM 1063 C C . TRP A 1 133 ? 22.504 -32.134 9.186 1.00 22.31 ? 154 TRP A C 1 ATOM 1064 O O . TRP A 1 133 ? 23.339 -33.014 8.889 1.00 19.24 ? 154 TRP A O 1 ATOM 1065 C CB . TRP A 1 133 ? 20.295 -32.277 8.153 1.00 20.15 ? 154 TRP A CB 1 ATOM 1066 C CG . TRP A 1 133 ? 19.239 -31.706 7.275 1.00 16.91 ? 154 TRP A CG 1 ATOM 1067 C CD1 . TRP A 1 133 ? 18.869 -32.162 6.041 1.00 15.62 ? 154 TRP A CD1 1 ATOM 1068 C CD2 . TRP A 1 133 ? 18.392 -30.588 7.568 1.00 13.94 ? 154 TRP A CD2 1 ATOM 1069 N NE1 . TRP A 1 133 ? 17.840 -31.395 5.539 1.00 15.00 ? 154 TRP A NE1 1 ATOM 1070 C CE2 . TRP A 1 133 ? 17.525 -30.418 6.453 1.00 15.67 ? 154 TRP A CE2 1 ATOM 1071 C CE3 . TRP A 1 133 ? 18.265 -29.723 8.665 1.00 14.87 ? 154 TRP A CE3 1 ATOM 1072 C CZ2 . TRP A 1 133 ? 16.540 -29.404 6.403 1.00 12.73 ? 154 TRP A CZ2 1 ATOM 1073 C CZ3 . TRP A 1 133 ? 17.280 -28.706 8.628 1.00 15.58 ? 154 TRP A CZ3 1 ATOM 1074 C CH2 . TRP A 1 133 ? 16.429 -28.559 7.496 1.00 14.19 ? 154 TRP A CH2 1 ATOM 1075 N N . ASP A 1 134 ? 22.304 -31.678 10.424 1.00 22.33 ? 155 ASP A N 1 ATOM 1076 C CA . ASP A 1 134 ? 22.836 -32.371 11.592 1.00 21.38 ? 155 ASP A CA 1 ATOM 1077 C C . ASP A 1 134 ? 21.880 -33.528 11.954 1.00 20.95 ? 155 ASP A C 1 ATOM 1078 O O . ASP A 1 134 ? 20.802 -33.309 12.518 1.00 19.68 ? 155 ASP A O 1 ATOM 1079 C CB . ASP A 1 134 ? 22.957 -31.419 12.775 1.00 22.56 ? 155 ASP A CB 1 ATOM 1080 C CG . ASP A 1 134 ? 23.469 -32.113 14.040 1.00 27.67 ? 155 ASP A CG 1 ATOM 1081 O OD1 . ASP A 1 134 ? 23.583 -33.371 14.063 1.00 28.11 ? 155 ASP A OD1 1 ATOM 1082 O OD2 . ASP A 1 134 ? 23.751 -31.400 15.027 1.00 30.34 ? 155 ASP A OD2 1 ATOM 1083 N N . TRP A 1 135 ? 22.277 -34.753 11.633 1.00 23.03 ? 156 TRP A N 1 ATOM 1084 C CA . TRP A 1 135 ? 21.442 -35.930 11.906 1.00 23.31 ? 156 TRP A CA 1 ATOM 1085 C C . TRP A 1 135 ? 21.819 -36.683 13.170 1.00 24.94 ? 156 TRP A C 1 ATOM 1086 O O . TRP A 1 135 ? 21.354 -37.806 13.378 1.00 25.53 ? 156 TRP A O 1 ATOM 1087 C CB . TRP A 1 135 ? 21.527 -36.916 10.743 1.00 24.63 ? 156 TRP A CB 1 ATOM 1088 C CG . TRP A 1 135 ? 20.728 -36.540 9.566 1.00 22.40 ? 156 TRP A CG 1 ATOM 1089 C CD1 . TRP A 1 135 ? 21.177 -35.952 8.415 1.00 21.51 ? 156 TRP A CD1 1 ATOM 1090 C CD2 . TRP A 1 135 ? 19.324 -36.729 9.405 1.00 22.25 ? 156 TRP A CD2 1 ATOM 1091 N NE1 . TRP A 1 135 ? 20.130 -35.758 7.551 1.00 21.63 ? 156 TRP A NE1 1 ATOM 1092 C CE2 . TRP A 1 135 ? 18.981 -36.229 8.130 1.00 20.91 ? 156 TRP A CE2 1 ATOM 1093 C CE3 . TRP A 1 135 ? 18.320 -37.289 10.212 1.00 23.95 ? 156 TRP A CE3 1 ATOM 1094 C CZ2 . TRP A 1 135 ? 17.672 -36.261 7.640 1.00 21.34 ? 156 TRP A CZ2 1 ATOM 1095 C CZ3 . TRP A 1 135 ? 17.008 -37.305 9.725 1.00 23.55 ? 156 TRP A CZ3 1 ATOM 1096 C CH2 . TRP A 1 135 ? 16.703 -36.802 8.453 1.00 21.63 ? 156 TRP A CH2 1 ATOM 1097 N N . THR A 1 136 ? 22.673 -36.095 14.005 1.00 25.73 ? 157 THR A N 1 ATOM 1098 C CA . THR A 1 136 ? 23.249 -36.828 15.133 1.00 25.74 ? 157 THR A CA 1 ATOM 1099 C C . THR A 1 136 ? 22.207 -37.257 16.163 1.00 26.59 ? 157 THR A C 1 ATOM 1100 O O . THR A 1 136 ? 22.405 -38.238 16.839 1.00 29.76 ? 157 THR A O 1 ATOM 1101 C CB . THR A 1 136 ? 24.435 -36.062 15.835 1.00 30.69 ? 157 THR A CB 1 ATOM 1102 O OG1 . THR A 1 136 ? 23.970 -34.816 16.372 1.00 29.86 ? 157 THR A OG1 1 ATOM 1103 C CG2 . THR A 1 136 ? 25.595 -35.803 14.856 1.00 29.37 ? 157 THR A CG2 1 ATOM 1104 N N . SER A 1 137 ? 21.086 -36.555 16.267 1.00 27.29 ? 158 SER A N 1 ATOM 1105 C CA . SER A 1 137 ? 20.059 -36.939 17.239 1.00 29.48 ? 158 SER A CA 1 ATOM 1106 C C . SER A 1 137 ? 19.118 -38.040 16.707 1.00 29.20 ? 158 SER A C 1 ATOM 1107 O O . SER A 1 137 ? 18.249 -38.532 17.428 1.00 29.00 ? 158 SER A O 1 ATOM 1108 C CB . SER A 1 137 ? 19.207 -35.729 17.633 1.00 30.30 ? 158 SER A CB 1 ATOM 1109 O OG . SER A 1 137 ? 18.188 -35.510 16.651 1.00 31.15 ? 158 SER A OG 1 ATOM 1110 N N . GLY A 1 138 ? 19.254 -38.384 15.433 1.00 29.37 ? 159 GLY A N 1 ATOM 1111 C CA . GLY A 1 138 ? 18.294 -39.267 14.797 1.00 28.71 ? 159 GLY A CA 1 ATOM 1112 C C . GLY A 1 138 ? 17.307 -38.519 13.913 1.00 24.85 ? 159 GLY A C 1 ATOM 1113 O O . GLY A 1 138 ? 16.698 -39.100 13.033 1.00 26.46 ? 159 GLY A O 1 ATOM 1114 N N . VAL A 1 139 ? 17.162 -37.222 14.146 1.00 21.03 ? 160 VAL A N 1 ATOM 1115 C CA . VAL A 1 139 ? 16.264 -36.393 13.371 1.00 18.74 ? 160 VAL A CA 1 ATOM 1116 C C . VAL A 1 139 ? 17.031 -35.159 12.881 1.00 21.34 ? 160 VAL A C 1 ATOM 1117 O O . VAL A 1 139 ? 17.896 -34.636 13.604 1.00 22.92 ? 160 VAL A O 1 ATOM 1118 C CB . VAL A 1 139 ? 15.091 -35.948 14.260 1.00 21.41 ? 160 VAL A CB 1 ATOM 1119 C CG1 . VAL A 1 139 ? 14.223 -34.931 13.549 1.00 17.99 ? 160 VAL A CG1 1 ATOM 1120 C CG2 . VAL A 1 139 ? 14.256 -37.177 14.748 1.00 18.52 ? 160 VAL A CG2 1 ATOM 1121 N N . ASN A 1 140 ? 16.727 -34.695 11.669 1.00 25.19 ? 161 ASN A N 1 ATOM 1122 C CA . ASN A 1 140 ? 17.414 -33.542 11.106 1.00 24.65 ? 161 ASN A CA 1 ATOM 1123 C C . ASN A 1 140 ? 17.266 -32.285 11.977 1.00 27.02 ? 161 ASN A C 1 ATOM 1124 O O . ASN A 1 140 ? 16.140 -31.887 12.344 1.00 22.63 ? 161 ASN A O 1 ATOM 1125 C CB . ASN A 1 140 ? 16.908 -33.243 9.686 1.00 20.83 ? 161 ASN A CB 1 ATOM 1126 C CG . ASN A 1 140 ? 15.408 -32.964 9.654 1.00 20.81 ? 161 ASN A CG 1 ATOM 1127 O OD1 . ASN A 1 140 ? 14.598 -33.835 9.980 1.00 22.48 ? 161 ASN A OD1 1 ATOM 1128 N ND2 . ASN A 1 140 ? 15.037 -31.750 9.236 1.00 19.12 ? 161 ASN A ND2 1 ATOM 1129 N N . LYS A 1 141 ? 18.411 -31.677 12.297 1.00 26.92 ? 162 LYS A N 1 ATOM 1130 C CA . LYS A 1 141 ? 18.446 -30.385 12.995 1.00 26.95 ? 162 LYS A CA 1 ATOM 1131 C C . LYS A 1 141 ? 19.351 -29.408 12.250 1.00 22.32 ? 162 LYS A C 1 ATOM 1132 O O . LYS A 1 141 ? 20.273 -29.804 11.548 1.00 22.65 ? 162 LYS A O 1 ATOM 1133 C CB . LYS A 1 141 ? 18.875 -30.553 14.467 1.00 32.04 ? 162 LYS A CB 1 ATOM 1134 C CG . LYS A 1 141 ? 18.061 -31.618 15.223 1.00 38.88 ? 162 LYS A CG 1 ATOM 1135 C CD . LYS A 1 141 ? 18.326 -31.609 16.725 1.00 45.84 ? 162 LYS A CD 1 ATOM 1136 C CE . LYS A 1 141 ? 17.520 -30.501 17.410 1.00 50.87 ? 162 LYS A CE 1 ATOM 1137 N NZ . LYS A 1 141 ? 17.581 -30.538 18.911 1.00 56.31 ? 162 LYS A NZ 1 ATOM 1138 N N . CYS A 1 142 ? 19.077 -28.124 12.405 1.00 20.51 ? 163 CYS A N 1 ATOM 1139 C CA . CYS A 1 142 ? 19.877 -27.088 11.778 1.00 18.06 ? 163 CYS A CA 1 ATOM 1140 C C . CYS A 1 142 ? 21.329 -27.251 12.238 1.00 18.39 ? 163 CYS A C 1 ATOM 1141 O O . CYS A 1 142 ? 21.571 -27.350 13.419 1.00 19.85 ? 163 CYS A O 1 ATOM 1142 C CB . CYS A 1 142 ? 19.334 -25.730 12.202 1.00 18.09 ? 163 CYS A CB 1 ATOM 1143 S SG . CYS A 1 142 ? 17.648 -25.484 11.553 1.00 26.65 ? 163 CYS A SG 1 ATOM 1144 N N . PRO A 1 143 ? 22.284 -27.300 11.295 1.00 16.66 ? 164 PRO A N 1 ATOM 1145 C CA . PRO A 1 143 ? 23.713 -27.467 11.599 1.00 18.49 ? 164 PRO A CA 1 ATOM 1146 C C . PRO A 1 143 ? 24.359 -26.138 11.955 1.00 19.86 ? 164 PRO A C 1 ATOM 1147 O O . PRO A 1 143 ? 23.733 -25.073 11.825 1.00 17.03 ? 164 PRO A O 1 ATOM 1148 C CB . PRO A 1 143 ? 24.294 -27.937 10.263 1.00 18.65 ? 164 PRO A CB 1 ATOM 1149 C CG . PRO A 1 143 ? 23.424 -27.231 9.246 1.00 18.54 ? 164 PRO A CG 1 ATOM 1150 C CD . PRO A 1 143 ? 22.025 -27.205 9.842 1.00 17.04 ? 164 PRO A CD 1 ATOM 1151 N N . ALA A 1 144 ? 25.620 -26.201 12.361 1.00 21.45 ? 165 ALA A N 1 ATOM 1152 C CA . ALA A 1 144 ? 26.380 -25.000 12.717 1.00 21.42 ? 165 ALA A CA 1 ATOM 1153 C C . ALA A 1 144 ? 26.325 -23.969 11.594 1.00 17.93 ? 165 ALA A C 1 ATOM 1154 O O . ALA A 1 144 ? 26.467 -24.303 10.422 1.00 19.33 ? 165 ALA A O 1 ATOM 1155 C CB . ALA A 1 144 ? 27.837 -25.377 13.045 1.00 19.32 ? 165 ALA A CB 1 ATOM 1156 N N . GLY A 1 145 ? 26.076 -22.718 11.942 1.00 18.21 ? 166 GLY A N 1 ATOM 1157 C CA . GLY A 1 145 ? 26.093 -21.637 10.960 1.00 16.79 ? 166 GLY A CA 1 ATOM 1158 C C . GLY A 1 145 ? 24.782 -21.355 10.272 1.00 18.35 ? 166 GLY A C 1 ATOM 1159 O O . GLY A 1 145 ? 24.692 -20.443 9.456 1.00 21.60 ? 166 GLY A O 1 ATOM 1160 N N . ALA A 1 146 ? 23.750 -22.119 10.616 1.00 18.92 ? 167 ALA A N 1 ATOM 1161 C CA . ALA A 1 146 ? 22.486 -22.049 9.892 1.00 20.88 ? 167 ALA A CA 1 ATOM 1162 C C . ALA A 1 146 ? 21.394 -21.474 10.792 1.00 23.72 ? 167 ALA A C 1 ATOM 1163 O O . ALA A 1 146 ? 20.893 -22.176 11.669 1.00 25.90 ? 167 ALA A O 1 ATOM 1164 C CB . ALA A 1 146 ? 22.087 -23.456 9.383 1.00 19.17 ? 167 ALA A CB 1 ATOM 1165 N N . LEU A 1 147 ? 21.030 -20.208 10.591 1.00 21.10 ? 168 LEU A N 1 ATOM 1166 C CA . LEU A 1 147 ? 20.010 -19.597 11.438 1.00 20.18 ? 168 LEU A CA 1 ATOM 1167 C C . LEU A 1 147 ? 18.629 -19.836 10.849 1.00 19.90 ? 168 LEU A C 1 ATOM 1168 O O . LEU A 1 147 ? 18.471 -19.997 9.617 1.00 19.18 ? 168 LEU A O 1 ATOM 1169 C CB . LEU A 1 147 ? 20.244 -18.094 11.626 1.00 20.84 ? 168 LEU A CB 1 ATOM 1170 C CG . LEU A 1 147 ? 21.473 -17.605 12.402 1.00 23.89 ? 168 LEU A CG 1 ATOM 1171 C CD1 . LEU A 1 147 ? 21.489 -16.078 12.463 1.00 25.07 ? 168 LEU A CD1 1 ATOM 1172 C CD2 . LEU A 1 147 ? 21.502 -18.173 13.816 1.00 25.95 ? 168 LEU A CD2 1 ATOM 1173 N N . CYS A 1 148 ? 17.634 -19.853 11.725 1.00 17.24 ? 169 CYS A N 1 ATOM 1174 C CA . CYS A 1 148 ? 16.251 -19.828 11.279 1.00 21.25 ? 169 CYS A CA 1 ATOM 1175 C C . CYS A 1 148 ? 15.915 -18.443 10.709 1.00 22.38 ? 169 CYS A C 1 ATOM 1176 O O . CYS A 1 148 ? 16.236 -17.412 11.338 1.00 21.61 ? 169 CYS A O 1 ATOM 1177 C CB . CYS A 1 148 ? 15.289 -20.211 12.427 1.00 23.39 ? 169 CYS A CB 1 ATOM 1178 S SG . CYS A 1 148 ? 15.295 -22.065 12.784 1.00 31.42 ? 169 CYS A SG 1 ATOM 1179 N N . ARG A 1 149 ? 15.289 -18.441 9.520 1.00 20.95 ? 170 ARG A N 1 ATOM 1180 C CA . ARG A 1 149 ? 14.868 -17.213 8.821 1.00 22.19 ? 170 ARG A CA 1 ATOM 1181 C C . ARG A 1 149 ? 13.509 -17.463 8.116 1.00 20.26 ? 170 ARG A C 1 ATOM 1182 O O . ARG A 1 149 ? 13.026 -18.601 8.060 1.00 18.43 ? 170 ARG A O 1 ATOM 1183 C CB . ARG A 1 149 ? 15.912 -16.824 7.774 1.00 20.84 ? 170 ARG A CB 1 ATOM 1184 C CG . ARG A 1 149 ? 17.355 -16.616 8.311 1.00 16.01 ? 170 ARG A CG 1 ATOM 1185 C CD . ARG A 1 149 ? 18.365 -16.461 7.144 1.00 18.79 ? 170 ARG A CD 1 ATOM 1186 N NE . ARG A 1 149 ? 19.748 -16.667 7.589 1.00 19.46 ? 170 ARG A NE 1 ATOM 1187 C CZ . ARG A 1 149 ? 20.490 -15.759 8.227 1.00 16.55 ? 170 ARG A CZ 1 ATOM 1188 N NH1 . ARG A 1 149 ? 19.998 -14.541 8.486 1.00 15.29 ? 170 ARG A NH1 1 ATOM 1189 N NH2 . ARG A 1 149 ? 21.735 -16.071 8.617 1.00 13.50 ? 170 ARG A NH2 1 ATOM 1190 N N . THR A 1 150 ? 12.904 -16.415 7.565 1.00 18.37 ? 171 THR A N 1 ATOM 1191 C CA . THR A 1 150 ? 11.694 -16.603 6.792 1.00 19.76 ? 171 THR A CA 1 ATOM 1192 C C . THR A 1 150 ? 12.028 -17.458 5.578 1.00 18.02 ? 171 THR A C 1 ATOM 1193 O O . THR A 1 150 ? 13.172 -17.491 5.140 1.00 16.31 ? 171 THR A O 1 ATOM 1194 C CB . THR A 1 150 ? 11.095 -15.289 6.313 1.00 20.84 ? 171 THR A CB 1 ATOM 1195 O OG1 . THR A 1 150 ? 12.075 -14.586 5.542 1.00 22.26 ? 171 THR A OG1 1 ATOM 1196 C CG2 . THR A 1 150 ? 10.650 -14.429 7.517 1.00 22.50 ? 171 THR A CG2 1 ATOM 1197 N N . PHE A 1 151 ? 11.024 -18.152 5.052 1.00 17.02 ? 172 PHE A N 1 ATOM 1198 C CA . PHE A 1 151 ? 11.207 -18.991 3.869 1.00 17.66 ? 172 PHE A CA 1 ATOM 1199 C C . PHE A 1 151 ? 11.851 -18.191 2.759 1.00 20.42 ? 172 PHE A C 1 ATOM 1200 O O . PHE A 1 151 ? 12.781 -18.662 2.098 1.00 22.41 ? 172 PHE A O 1 ATOM 1201 C CB . PHE A 1 151 ? 9.861 -19.558 3.383 1.00 17.92 ? 172 PHE A CB 1 ATOM 1202 C CG . PHE A 1 151 ? 9.810 -21.066 3.379 1.00 22.64 ? 172 PHE A CG 1 ATOM 1203 C CD1 . PHE A 1 151 ? 9.949 -21.780 4.565 1.00 24.93 ? 172 PHE A CD1 1 ATOM 1204 C CD2 . PHE A 1 151 ? 9.608 -21.765 2.204 1.00 23.52 ? 172 PHE A CD2 1 ATOM 1205 C CE1 . PHE A 1 151 ? 9.891 -23.204 4.575 1.00 27.32 ? 172 PHE A CE1 1 ATOM 1206 C CE2 . PHE A 1 151 ? 9.540 -23.168 2.205 1.00 24.86 ? 172 PHE A CE2 1 ATOM 1207 C CZ . PHE A 1 151 ? 9.688 -23.892 3.392 1.00 25.74 ? 172 PHE A CZ 1 ATOM 1208 N N . GLU A 1 152 ? 11.328 -16.983 2.545 1.00 20.76 ? 173 GLU A N 1 ATOM 1209 C CA . GLU A 1 152 ? 11.821 -16.121 1.482 1.00 23.19 ? 173 GLU A CA 1 ATOM 1210 C C . GLU A 1 152 ? 13.294 -15.766 1.587 1.00 21.51 ? 173 GLU A C 1 ATOM 1211 O O . GLU A 1 152 ? 13.923 -15.504 0.561 1.00 20.23 ? 173 GLU A O 1 ATOM 1212 C CB . GLU A 1 152 ? 11.033 -14.833 1.433 1.00 27.85 ? 173 GLU A CB 1 ATOM 1213 C CG . GLU A 1 152 ? 9.871 -14.959 0.528 1.00 37.63 ? 173 GLU A CG 1 ATOM 1214 C CD . GLU A 1 152 ? 9.052 -13.695 0.480 1.00 46.00 ? 173 GLU A CD 1 ATOM 1215 O OE1 . GLU A 1 152 ? 8.002 -13.674 1.167 1.00 48.59 ? 173 GLU A OE1 1 ATOM 1216 O OE2 . GLU A 1 152 ? 9.472 -12.738 -0.227 1.00 48.95 ? 173 GLU A OE2 1 ATOM 1217 N N . SER A 1 153 ? 13.831 -15.717 2.805 1.00 19.48 ? 174 SER A N 1 ATOM 1218 C CA . SER A 1 153 ? 15.268 -15.464 2.979 1.00 21.23 ? 174 SER A CA 1 ATOM 1219 C C . SER A 1 153 ? 16.112 -16.538 2.302 1.00 21.77 ? 174 SER A C 1 ATOM 1220 O O . SER A 1 153 ? 17.065 -16.232 1.592 1.00 21.82 ? 174 SER A O 1 ATOM 1221 C CB . SER A 1 153 ? 15.661 -15.390 4.464 1.00 22.05 ? 174 SER A CB 1 ATOM 1222 O OG . SER A 1 153 ? 14.954 -14.338 5.121 1.00 27.20 ? 174 SER A OG 1 ATOM 1223 N N . TYR A 1 154 ? 15.771 -17.799 2.544 1.00 18.54 ? 175 TYR A N 1 ATOM 1224 C CA . TYR A 1 154 ? 16.478 -18.911 1.910 1.00 18.13 ? 175 TYR A CA 1 ATOM 1225 C C . TYR A 1 154 ? 16.018 -19.255 0.480 1.00 19.18 ? 175 TYR A C 1 ATOM 1226 O O . TYR A 1 154 ? 16.789 -19.821 -0.305 1.00 16.47 ? 175 TYR A O 1 ATOM 1227 C CB . TYR A 1 154 ? 16.396 -20.149 2.803 1.00 16.30 ? 175 TYR A CB 1 ATOM 1228 C CG . TYR A 1 154 ? 17.310 -20.029 4.007 1.00 18.20 ? 175 TYR A CG 1 ATOM 1229 C CD1 . TYR A 1 154 ? 18.682 -20.063 3.852 1.00 17.58 ? 175 TYR A CD1 1 ATOM 1230 C CD2 . TYR A 1 154 ? 16.799 -19.871 5.291 1.00 17.56 ? 175 TYR A CD2 1 ATOM 1231 C CE1 . TYR A 1 154 ? 19.551 -19.964 4.967 1.00 16.31 ? 175 TYR A CE1 1 ATOM 1232 C CE2 . TYR A 1 154 ? 17.647 -19.750 6.397 1.00 19.14 ? 175 TYR A CE2 1 ATOM 1233 C CZ . TYR A 1 154 ? 19.028 -19.800 6.216 1.00 17.79 ? 175 TYR A CZ 1 ATOM 1234 O OH . TYR A 1 154 ? 19.879 -19.690 7.296 1.00 17.07 ? 175 TYR A OH 1 ATOM 1235 N N . PHE A 1 155 ? 14.771 -18.897 0.148 1.00 19.92 ? 176 PHE A N 1 ATOM 1236 C CA . PHE A 1 155 ? 14.202 -19.167 -1.169 1.00 20.19 ? 176 PHE A CA 1 ATOM 1237 C C . PHE A 1 155 ? 13.617 -17.882 -1.733 1.00 22.29 ? 176 PHE A C 1 ATOM 1238 O O . PHE A 1 155 ? 12.411 -17.641 -1.648 1.00 21.48 ? 176 PHE A O 1 ATOM 1239 C CB . PHE A 1 155 ? 13.082 -20.196 -1.043 1.00 21.31 ? 176 PHE A CB 1 ATOM 1240 C CG . PHE A 1 155 ? 13.500 -21.456 -0.352 1.00 21.47 ? 176 PHE A CG 1 ATOM 1241 C CD1 . PHE A 1 155 ? 14.479 -22.272 -0.903 1.00 21.80 ? 176 PHE A CD1 1 ATOM 1242 C CD2 . PHE A 1 155 ? 12.900 -21.842 0.838 1.00 21.03 ? 176 PHE A CD2 1 ATOM 1243 C CE1 . PHE A 1 155 ? 14.849 -23.466 -0.275 1.00 22.40 ? 176 PHE A CE1 1 ATOM 1244 C CE2 . PHE A 1 155 ? 13.277 -23.029 1.471 1.00 21.69 ? 176 PHE A CE2 1 ATOM 1245 C CZ . PHE A 1 155 ? 14.258 -23.839 0.911 1.00 20.93 ? 176 PHE A CZ 1 ATOM 1246 N N . PRO A 1 156 ? 14.476 -17.039 -2.303 1.00 22.70 ? 177 PRO A N 1 ATOM 1247 C CA . PRO A 1 156 ? 14.009 -15.698 -2.663 1.00 20.41 ? 177 PRO A CA 1 ATOM 1248 C C . PRO A 1 156 ? 13.022 -15.666 -3.830 1.00 19.57 ? 177 PRO A C 1 ATOM 1249 O O . PRO A 1 156 ? 12.344 -14.657 -3.991 1.00 20.80 ? 177 PRO A O 1 ATOM 1250 C CB . PRO A 1 156 ? 15.303 -14.928 -2.990 1.00 23.71 ? 177 PRO A CB 1 ATOM 1251 C CG . PRO A 1 156 ? 16.410 -15.983 -3.020 1.00 25.68 ? 177 PRO A CG 1 ATOM 1252 C CD . PRO A 1 156 ? 15.945 -17.184 -2.280 1.00 21.27 ? 177 PRO A CD 1 ATOM 1253 N N . THR A 1 157 ? 12.952 -16.745 -4.618 1.00 18.68 ? 178 THR A N 1 ATOM 1254 C CA . THR A 1 157 ? 11.993 -16.883 -5.698 1.00 18.76 ? 178 THR A CA 1 ATOM 1255 C C . THR A 1 157 ? 11.450 -18.311 -5.726 1.00 21.10 ? 178 THR A C 1 ATOM 1256 O O . THR A 1 157 ? 12.022 -19.207 -5.127 1.00 19.88 ? 178 THR A O 1 ATOM 1257 C CB . THR A 1 157 ? 12.633 -16.580 -7.086 1.00 22.80 ? 178 THR A CB 1 ATOM 1258 O OG1 . THR A 1 157 ? 13.653 -17.544 -7.341 1.00 20.24 ? 178 THR A OG1 1 ATOM 1259 C CG2 . THR A 1 157 ? 13.230 -15.145 -7.166 1.00 19.17 ? 178 THR A CG2 1 ATOM 1260 N N . PRO A 1 158 ? 10.321 -18.520 -6.413 1.00 21.82 ? 179 PRO A N 1 ATOM 1261 C CA . PRO A 1 158 ? 9.780 -19.884 -6.583 1.00 20.39 ? 179 PRO A CA 1 ATOM 1262 C C . PRO A 1 158 ? 10.831 -20.845 -7.117 1.00 18.77 ? 179 PRO A C 1 ATOM 1263 O O . PRO A 1 158 ? 10.991 -21.927 -6.562 1.00 16.94 ? 179 PRO A O 1 ATOM 1264 C CB . PRO A 1 158 ? 8.639 -19.698 -7.591 1.00 20.56 ? 179 PRO A CB 1 ATOM 1265 C CG . PRO A 1 158 ? 8.138 -18.221 -7.312 1.00 20.41 ? 179 PRO A CG 1 ATOM 1266 C CD . PRO A 1 158 ? 9.422 -17.461 -6.931 1.00 22.45 ? 179 PRO A CD 1 ATOM 1267 N N . ALA A 1 159 ? 11.575 -20.465 -8.145 1.00 18.26 ? 180 ALA A N 1 ATOM 1268 C CA . ALA A 1 159 ? 12.605 -21.396 -8.639 1.00 17.69 ? 180 ALA A CA 1 ATOM 1269 C C . ALA A 1 159 ? 13.628 -21.787 -7.555 1.00 18.15 ? 180 ALA A C 1 ATOM 1270 O O . ALA A 1 159 ? 14.049 -22.959 -7.476 1.00 18.15 ? 180 ALA A O 1 ATOM 1271 C CB . ALA A 1 159 ? 13.288 -20.890 -9.922 1.00 13.00 ? 180 ALA A CB 1 ATOM 1272 N N . ALA A 1 160 ? 14.003 -20.842 -6.698 1.00 16.36 ? 181 ALA A N 1 ATOM 1273 C CA . ALA A 1 160 ? 14.979 -21.167 -5.650 1.00 16.25 ? 181 ALA A CA 1 ATOM 1274 C C . ALA A 1 160 ? 14.429 -22.234 -4.708 1.00 18.00 ? 181 ALA A C 1 ATOM 1275 O O . ALA A 1 160 ? 15.164 -23.112 -4.238 1.00 19.56 ? 181 ALA A O 1 ATOM 1276 C CB . ALA A 1 160 ? 15.405 -19.913 -4.876 1.00 16.48 ? 181 ALA A CB 1 ATOM 1277 N N . LEU A 1 161 ? 13.129 -22.179 -4.424 1.00 16.34 ? 182 LEU A N 1 ATOM 1278 C CA . LEU A 1 161 ? 12.530 -23.247 -3.647 1.00 16.41 ? 182 LEU A CA 1 ATOM 1279 C C . LEU A 1 161 ? 12.500 -24.576 -4.443 1.00 14.99 ? 182 LEU A C 1 ATOM 1280 O O . LEU A 1 161 ? 13.115 -25.568 -4.042 1.00 13.28 ? 182 LEU A O 1 ATOM 1281 C CB . LEU A 1 161 ? 11.131 -22.855 -3.168 1.00 18.28 ? 182 LEU A CB 1 ATOM 1282 C CG . LEU A 1 161 ? 10.258 -23.969 -2.597 1.00 17.51 ? 182 LEU A CG 1 ATOM 1283 C CD1 . LEU A 1 161 ? 10.924 -24.591 -1.392 1.00 15.65 ? 182 LEU A CD1 1 ATOM 1284 C CD2 . LEU A 1 161 ? 8.851 -23.393 -2.238 1.00 18.19 ? 182 LEU A CD2 1 ATOM 1285 N N . CYS A 1 162 ? 11.799 -24.592 -5.574 1.00 14.45 ? 183 CYS A N 1 ATOM 1286 C CA . CYS A 1 162 ? 11.539 -25.857 -6.268 1.00 17.04 ? 183 CYS A CA 1 ATOM 1287 C C . CYS A 1 162 ? 12.819 -26.514 -6.816 1.00 19.06 ? 183 CYS A C 1 ATOM 1288 O O . CYS A 1 162 ? 12.936 -27.737 -6.817 1.00 17.93 ? 183 CYS A O 1 ATOM 1289 C CB . CYS A 1 162 ? 10.480 -25.650 -7.368 1.00 18.10 ? 183 CYS A CB 1 ATOM 1290 S SG . CYS A 1 162 ? 8.962 -24.845 -6.711 1.00 27.19 ? 183 CYS A SG 1 ATOM 1291 N N . GLU A 1 163 ? 13.777 -25.691 -7.261 1.00 18.24 ? 184 GLU A N 1 ATOM 1292 C CA . GLU A 1 163 ? 15.025 -26.202 -7.820 1.00 20.44 ? 184 GLU A CA 1 ATOM 1293 C C . GLU A 1 163 ? 16.078 -26.465 -6.736 1.00 19.57 ? 184 GLU A C 1 ATOM 1294 O O . GLU A 1 163 ? 16.795 -27.442 -6.833 1.00 20.36 ? 184 GLU A O 1 ATOM 1295 C CB . GLU A 1 163 ? 15.586 -25.281 -8.944 1.00 17.27 ? 184 GLU A CB 1 ATOM 1296 C CG . GLU A 1 163 ? 14.487 -24.925 -9.963 1.00 21.31 ? 184 GLU A CG 1 ATOM 1297 C CD . GLU A 1 163 ? 14.953 -24.124 -11.177 1.00 24.72 ? 184 GLU A CD 1 ATOM 1298 O OE1 . GLU A 1 163 ? 16.109 -23.617 -11.200 1.00 27.92 ? 184 GLU A OE1 1 ATOM 1299 O OE2 . GLU A 1 163 ? 14.137 -24.005 -12.122 1.00 23.92 ? 184 GLU A OE2 1 ATOM 1300 N N . GLY A 1 164 ? 16.162 -25.623 -5.707 1.00 17.69 ? 185 GLY A N 1 ATOM 1301 C CA . GLY A 1 164 ? 17.254 -25.763 -4.738 1.00 17.17 ? 185 GLY A CA 1 ATOM 1302 C C . GLY A 1 164 ? 16.965 -26.841 -3.709 1.00 19.06 ? 185 GLY A C 1 ATOM 1303 O O . GLY A 1 164 ? 17.886 -27.495 -3.184 1.00 17.86 ? 185 GLY A O 1 ATOM 1304 N N . LEU A 1 165 ? 15.671 -27.060 -3.448 1.00 15.84 ? 186 LEU A N 1 ATOM 1305 C CA . LEU A 1 165 ? 15.234 -27.891 -2.331 1.00 18.40 ? 186 LEU A CA 1 ATOM 1306 C C . LEU A 1 165 ? 15.863 -29.302 -2.328 1.00 18.74 ? 186 LEU A C 1 ATOM 1307 O O . LEU A 1 165 ? 16.423 -29.732 -1.316 1.00 15.26 ? 186 LEU A O 1 ATOM 1308 C CB . LEU A 1 165 ? 13.721 -28.002 -2.343 1.00 22.34 ? 186 LEU A CB 1 ATOM 1309 C CG . LEU A 1 165 ? 12.943 -28.551 -1.162 1.00 25.15 ? 186 LEU A CG 1 ATOM 1310 C CD1 . LEU A 1 165 ? 13.191 -27.794 0.169 1.00 17.85 ? 186 LEU A CD1 1 ATOM 1311 C CD2 . LEU A 1 165 ? 11.444 -28.522 -1.588 1.00 25.25 ? 186 LEU A CD2 1 ATOM 1312 N N . TRP A 1 166 ? 15.796 -30.004 -3.456 1.00 18.65 ? 187 TRP A N 1 ATOM 1313 C CA . TRP A 1 166 ? 16.318 -31.369 -3.508 1.00 19.47 ? 187 TRP A CA 1 ATOM 1314 C C . TRP A 1 166 ? 17.486 -31.497 -4.504 1.00 19.53 ? 187 TRP A C 1 ATOM 1315 O O . TRP A 1 166 ? 17.588 -32.491 -5.213 1.00 21.05 ? 187 TRP A O 1 ATOM 1316 C CB . TRP A 1 166 ? 15.199 -32.381 -3.869 1.00 19.92 ? 187 TRP A CB 1 ATOM 1317 C CG . TRP A 1 166 ? 13.941 -32.280 -3.055 1.00 18.65 ? 187 TRP A CG 1 ATOM 1318 C CD1 . TRP A 1 166 ? 12.662 -32.102 -3.534 1.00 18.22 ? 187 TRP A CD1 1 ATOM 1319 C CD2 . TRP A 1 166 ? 13.820 -32.370 -1.628 1.00 20.46 ? 187 TRP A CD2 1 ATOM 1320 N NE1 . TRP A 1 166 ? 11.761 -32.070 -2.491 1.00 15.79 ? 187 TRP A NE1 1 ATOM 1321 C CE2 . TRP A 1 166 ? 12.442 -32.217 -1.312 1.00 17.47 ? 187 TRP A CE2 1 ATOM 1322 C CE3 . TRP A 1 166 ? 14.742 -32.551 -0.578 1.00 21.83 ? 187 TRP A CE3 1 ATOM 1323 C CZ2 . TRP A 1 166 ? 11.963 -32.252 0.008 1.00 18.87 ? 187 TRP A CZ2 1 ATOM 1324 C CZ3 . TRP A 1 166 ? 14.259 -32.585 0.747 1.00 21.39 ? 187 TRP A CZ3 1 ATOM 1325 C CH2 . TRP A 1 166 ? 12.888 -32.419 1.021 1.00 19.30 ? 187 TRP A CH2 1 ATOM 1326 N N . SER A 1 167 ? 18.360 -30.491 -4.575 1.00 18.32 ? 188 SER A N 1 ATOM 1327 C CA . SER A 1 167 ? 19.543 -30.570 -5.439 1.00 18.84 ? 188 SER A CA 1 ATOM 1328 C C . SER A 1 167 ? 19.152 -30.652 -6.913 1.00 18.63 ? 188 SER A C 1 ATOM 1329 O O . SER A 1 167 ? 19.642 -31.514 -7.643 1.00 17.01 ? 188 SER A O 1 ATOM 1330 C CB . SER A 1 167 ? 20.436 -31.787 -5.076 1.00 18.75 ? 188 SER A CB 1 ATOM 1331 O OG . SER A 1 167 ? 20.997 -31.634 -3.785 1.00 21.13 ? 188 SER A OG 1 ATOM 1332 N N . HIS A 1 168 ? 18.262 -29.757 -7.335 1.00 18.86 ? 189 HIS A N 1 ATOM 1333 C CA . HIS A 1 168 ? 17.820 -29.681 -8.737 1.00 18.54 ? 189 HIS A CA 1 ATOM 1334 C C . HIS A 1 168 ? 17.035 -30.885 -9.218 1.00 18.13 ? 189 HIS A C 1 ATOM 1335 O O . HIS A 1 168 ? 17.060 -31.221 -10.392 1.00 16.75 ? 189 HIS A O 1 ATOM 1336 C CB . HIS A 1 168 ? 19.012 -29.371 -9.655 1.00 17.06 ? 189 HIS A CB 1 ATOM 1337 C CG . HIS A 1 168 ? 19.528 -27.987 -9.455 1.00 18.42 ? 189 HIS A CG 1 ATOM 1338 N ND1 . HIS A 1 168 ? 18.999 -26.899 -10.118 1.00 18.20 ? 189 HIS A ND1 1 ATOM 1339 C CD2 . HIS A 1 168 ? 20.453 -27.495 -8.598 1.00 18.68 ? 189 HIS A CD2 1 ATOM 1340 C CE1 . HIS A 1 168 ? 19.613 -25.801 -9.714 1.00 19.21 ? 189 HIS A CE1 1 ATOM 1341 N NE2 . HIS A 1 168 ? 20.490 -26.135 -8.783 1.00 20.29 ? 189 HIS A NE2 1 ATOM 1342 N N . SER A 1 169 ? 16.315 -31.529 -8.310 1.00 18.97 ? 190 SER A N 1 ATOM 1343 C CA . SER A 1 169 ? 15.461 -32.624 -8.738 1.00 20.63 ? 190 SER A CA 1 ATOM 1344 C C . SER A 1 169 ? 14.341 -32.081 -9.620 1.00 20.52 ? 190 SER A C 1 ATOM 1345 O O . SER A 1 169 ? 13.890 -32.789 -10.517 1.00 19.49 ? 190 SER A O 1 ATOM 1346 C CB . SER A 1 169 ? 14.885 -33.390 -7.543 1.00 23.41 ? 190 SER A CB 1 ATOM 1347 O OG . SER A 1 169 ? 13.871 -32.610 -6.943 1.00 27.68 ? 190 SER A OG 1 ATOM 1348 N N . TYR A 1 170 ? 13.899 -30.837 -9.364 1.00 19.66 ? 191 TYR A N 1 ATOM 1349 C CA . TYR A 1 170 ? 12.986 -30.132 -10.269 1.00 17.96 ? 191 TYR A CA 1 ATOM 1350 C C . TYR A 1 170 ? 13.692 -29.011 -11.022 1.00 17.24 ? 191 TYR A C 1 ATOM 1351 O O . TYR A 1 170 ? 14.641 -28.399 -10.510 1.00 17.19 ? 191 TYR A O 1 ATOM 1352 C CB . TYR A 1 170 ? 11.818 -29.430 -9.533 1.00 14.33 ? 191 TYR A CB 1 ATOM 1353 C CG . TYR A 1 170 ? 10.797 -30.279 -8.824 1.00 13.55 ? 191 TYR A CG 1 ATOM 1354 C CD1 . TYR A 1 170 ? 9.981 -31.178 -9.536 1.00 10.84 ? 191 TYR A CD1 1 ATOM 1355 C CD2 . TYR A 1 170 ? 10.594 -30.141 -7.458 1.00 13.78 ? 191 TYR A CD2 1 ATOM 1356 C CE1 . TYR A 1 170 ? 9.001 -31.930 -8.883 1.00 15.12 ? 191 TYR A CE1 1 ATOM 1357 C CE2 . TYR A 1 170 ? 9.628 -30.890 -6.797 1.00 16.45 ? 191 TYR A CE2 1 ATOM 1358 C CZ . TYR A 1 170 ? 8.827 -31.775 -7.518 1.00 18.50 ? 191 TYR A CZ 1 ATOM 1359 O OH . TYR A 1 170 ? 7.850 -32.497 -6.868 1.00 20.67 ? 191 TYR A OH 1 ATOM 1360 N N . LYS A 1 171 ? 13.187 -28.713 -12.224 1.00 14.86 ? 192 LYS A N 1 ATOM 1361 C CA . LYS A 1 171 ? 13.361 -27.373 -12.804 1.00 18.03 ? 192 LYS A CA 1 ATOM 1362 C C . LYS A 1 171 ? 11.959 -26.849 -12.983 1.00 16.13 ? 192 LYS A C 1 ATOM 1363 O O . LYS A 1 171 ? 11.021 -27.636 -13.112 1.00 17.29 ? 192 LYS A O 1 ATOM 1364 C CB . LYS A 1 171 ? 14.059 -27.410 -14.161 1.00 16.48 ? 192 LYS A CB 1 ATOM 1365 C CG . LYS A 1 171 ? 13.300 -28.226 -15.208 1.00 16.07 ? 192 LYS A CG 1 ATOM 1366 C CD . LYS A 1 171 ? 13.985 -28.116 -16.574 1.00 15.94 ? 192 LYS A CD 1 ATOM 1367 C CE . LYS A 1 171 ? 13.268 -29.013 -17.585 1.00 15.92 ? 192 LYS A CE 1 ATOM 1368 N NZ . LYS A 1 171 ? 13.921 -29.000 -18.918 1.00 19.11 ? 192 LYS A NZ 1 ATOM 1369 N N . VAL A 1 172 ? 11.804 -25.537 -12.987 1.00 14.56 ? 193 VAL A N 1 ATOM 1370 C CA . VAL A 1 172 ? 10.490 -24.933 -13.160 1.00 16.44 ? 193 VAL A CA 1 ATOM 1371 C C . VAL A 1 172 ? 10.241 -24.815 -14.643 1.00 17.26 ? 193 VAL A C 1 ATOM 1372 O O . VAL A 1 172 ? 10.954 -24.112 -15.330 1.00 16.58 ? 193 VAL A O 1 ATOM 1373 C CB . VAL A 1 172 ? 10.417 -23.516 -12.547 1.00 20.15 ? 193 VAL A CB 1 ATOM 1374 C CG1 . VAL A 1 172 ? 9.022 -22.904 -12.777 1.00 20.45 ? 193 VAL A CG1 1 ATOM 1375 C CG2 . VAL A 1 172 ? 10.773 -23.572 -11.029 1.00 14.27 ? 193 VAL A CG2 1 ATOM 1376 N N . SER A 1 173 ? 9.252 -25.547 -15.145 1.00 17.63 ? 194 SER A N 1 ATOM 1377 C CA . SER A 1 173 ? 8.919 -25.491 -16.554 1.00 19.81 ? 194 SER A CA 1 ATOM 1378 C C . SER A 1 173 ? 8.258 -24.133 -16.823 1.00 23.83 ? 194 SER A C 1 ATOM 1379 O O . SER A 1 173 ? 7.633 -23.580 -15.934 1.00 25.51 ? 194 SER A O 1 ATOM 1380 C CB . SER A 1 173 ? 7.946 -26.625 -16.897 1.00 16.34 ? 194 SER A CB 1 ATOM 1381 O OG . SER A 1 173 ? 7.649 -26.566 -18.264 1.00 19.83 ? 194 SER A OG 1 ATOM 1382 N N . ASN A 1 174 ? 8.416 -23.583 -18.025 1.00 24.32 ? 195 ASN A N 1 ATOM 1383 C CA . ASN A 1 174 ? 7.633 -22.400 -18.406 1.00 23.17 ? 195 ASN A CA 1 ATOM 1384 C C . ASN A 1 174 ? 6.251 -22.787 -18.953 1.00 22.00 ? 195 ASN A C 1 ATOM 1385 O O . ASN A 1 174 ? 5.447 -21.933 -19.250 1.00 21.93 ? 195 ASN A O 1 ATOM 1386 C CB . ASN A 1 174 ? 8.360 -21.527 -19.424 1.00 23.14 ? 195 ASN A CB 1 ATOM 1387 C CG . ASN A 1 174 ? 7.720 -20.165 -19.557 1.00 25.03 ? 195 ASN A CG 1 ATOM 1388 O OD1 . ASN A 1 174 ? 7.360 -19.557 -18.553 1.00 21.46 ? 195 ASN A OD1 1 ATOM 1389 N ND2 . ASN A 1 174 ? 7.527 -19.698 -20.790 1.00 32.36 ? 195 ASN A ND2 1 ATOM 1390 N N . TYR A 1 175 ? 5.999 -24.088 -19.095 1.00 22.98 ? 196 TYR A N 1 ATOM 1391 C CA . TYR A 1 175 ? 4.675 -24.586 -19.484 1.00 24.65 ? 196 TYR A CA 1 ATOM 1392 C C . TYR A 1 175 ? 3.723 -24.591 -18.289 1.00 25.75 ? 196 TYR A C 1 ATOM 1393 O O . TYR A 1 175 ? 4.175 -24.673 -17.148 1.00 22.63 ? 196 TYR A O 1 ATOM 1394 C CB . TYR A 1 175 ? 4.785 -26.020 -20.014 1.00 22.48 ? 196 TYR A CB 1 ATOM 1395 C CG . TYR A 1 175 ? 5.383 -26.112 -21.400 1.00 23.22 ? 196 TYR A CG 1 ATOM 1396 C CD1 . TYR A 1 175 ? 4.712 -25.588 -22.507 1.00 24.09 ? 196 TYR A CD1 1 ATOM 1397 C CD2 . TYR A 1 175 ? 6.616 -26.733 -21.603 1.00 22.94 ? 196 TYR A CD2 1 ATOM 1398 C CE1 . TYR A 1 175 ? 5.253 -25.684 -23.776 1.00 26.11 ? 196 TYR A CE1 1 ATOM 1399 C CE2 . TYR A 1 175 ? 7.171 -26.824 -22.864 1.00 23.61 ? 196 TYR A CE2 1 ATOM 1400 C CZ . TYR A 1 175 ? 6.488 -26.310 -23.939 1.00 27.99 ? 196 TYR A CZ 1 ATOM 1401 O OH . TYR A 1 175 ? 7.044 -26.424 -25.191 1.00 32.95 ? 196 TYR A OH 1 ATOM 1402 N N . SER A 1 176 ? 2.416 -24.565 -18.543 1.00 28.76 ? 197 SER A N 1 ATOM 1403 C CA . SER A 1 176 ? 1.447 -24.479 -17.455 1.00 30.91 ? 197 SER A CA 1 ATOM 1404 C C . SER A 1 176 ? 0.687 -25.767 -17.122 1.00 31.23 ? 197 SER A C 1 ATOM 1405 O O . SER A 1 176 ? 0.587 -26.680 -17.947 1.00 27.97 ? 197 SER A O 1 ATOM 1406 C CB . SER A 1 176 ? 0.435 -23.366 -17.740 1.00 36.00 ? 197 SER A CB 1 ATOM 1407 O OG . SER A 1 176 ? 1.070 -22.096 -17.665 1.00 40.40 ? 197 SER A OG 1 ATOM 1408 N N . ARG A 1 177 ? 0.142 -25.806 -15.901 1.00 31.76 ? 198 ARG A N 1 ATOM 1409 C CA . ARG A 1 177 ? -0.757 -26.869 -15.471 1.00 31.51 ? 198 ARG A CA 1 ATOM 1410 C C . ARG A 1 177 ? -1.738 -27.100 -16.593 1.00 35.46 ? 198 ARG A C 1 ATOM 1411 O O . ARG A 1 177 ? -2.340 -26.147 -17.071 1.00 38.67 ? 198 ARG A O 1 ATOM 1412 C CB . ARG A 1 177 ? -1.527 -26.453 -14.209 1.00 30.46 ? 198 ARG A CB 1 ATOM 1413 C CG . ARG A 1 177 ? -0.633 -26.245 -12.965 1.00 29.99 ? 198 ARG A CG 1 ATOM 1414 C CD . ARG A 1 177 ? -1.451 -25.760 -11.770 1.00 30.59 ? 198 ARG A CD 1 ATOM 1415 N NE . ARG A 1 177 ? -2.711 -26.494 -11.711 1.00 28.16 ? 198 ARG A NE 1 ATOM 1416 C CZ . ARG A 1 177 ? -2.810 -27.709 -11.209 1.00 28.17 ? 198 ARG A CZ 1 ATOM 1417 N NH1 . ARG A 1 177 ? -1.709 -28.304 -10.709 1.00 21.67 ? 198 ARG A NH1 1 ATOM 1418 N NH2 . ARG A 1 177 ? -4.000 -28.323 -11.202 1.00 27.97 ? 198 ARG A NH2 1 ATOM 1419 N N . GLY A 1 178 ? -1.881 -28.348 -17.039 1.00 32.71 ? 199 GLY A N 1 ATOM 1420 C CA . GLY A 1 178 ? -2.909 -28.654 -18.019 1.00 34.17 ? 199 GLY A CA 1 ATOM 1421 C C . GLY A 1 178 ? -2.434 -28.644 -19.466 1.00 34.16 ? 199 GLY A C 1 ATOM 1422 O O . GLY A 1 178 ? -3.203 -28.969 -20.386 1.00 35.58 ? 199 GLY A O 1 ATOM 1423 N N . SER A 1 179 ? -1.168 -28.291 -19.683 1.00 25.59 ? 200 SER A N 1 ATOM 1424 C CA . SER A 1 179 ? -0.668 -28.195 -21.045 1.00 26.86 ? 200 SER A CA 1 ATOM 1425 C C . SER A 1 179 ? -0.231 -29.561 -21.559 1.00 25.80 ? 200 SER A C 1 ATOM 1426 O O . SER A 1 179 ? -0.050 -29.741 -22.750 1.00 24.04 ? 200 SER A O 1 ATOM 1427 C CB . SER A 1 179 ? 0.533 -27.268 -21.095 1.00 25.98 ? 200 SER A CB 1 ATOM 1428 O OG . SER A 1 179 ? 1.532 -27.774 -20.235 1.00 24.84 ? 200 SER A OG 1 ATOM 1429 N N . GLY A 1 180 ? -0.037 -30.516 -20.658 1.00 24.84 ? 201 GLY A N 1 ATOM 1430 C CA . GLY A 1 180 ? 0.499 -31.808 -21.056 1.00 25.09 ? 201 GLY A CA 1 ATOM 1431 C C . GLY A 1 180 ? 1.972 -31.700 -21.427 1.00 26.12 ? 201 GLY A C 1 ATOM 1432 O O . GLY A 1 180 ? 2.498 -32.555 -22.131 1.00 29.02 ? 201 GLY A O 1 ATOM 1433 N N . ARG A 1 181 ? 2.635 -30.633 -20.976 1.00 22.67 ? 202 ARG A N 1 ATOM 1434 C CA . ARG A 1 181 ? 4.060 -30.430 -21.261 1.00 22.74 ? 202 ARG A CA 1 ATOM 1435 C C . ARG A 1 181 ? 4.844 -30.105 -19.995 1.00 22.30 ? 202 ARG A C 1 ATOM 1436 O O . ARG A 1 181 ? 5.979 -29.621 -20.074 1.00 22.18 ? 202 ARG A O 1 ATOM 1437 C CB . ARG A 1 181 ? 4.259 -29.294 -22.259 1.00 23.88 ? 202 ARG A CB 1 ATOM 1438 C CG . ARG A 1 181 ? 3.729 -29.597 -23.660 1.00 25.54 ? 202 ARG A CG 1 ATOM 1439 C CD . ARG A 1 181 ? 4.540 -30.682 -24.309 1.00 23.62 ? 202 ARG A CD 1 ATOM 1440 N NE . ARG A 1 181 ? 4.042 -30.918 -25.652 1.00 25.29 ? 202 ARG A NE 1 ATOM 1441 C CZ . ARG A 1 181 ? 3.160 -31.863 -25.946 1.00 23.69 ? 202 ARG A CZ 1 ATOM 1442 N NH1 . ARG A 1 181 ? 2.720 -32.670 -24.979 1.00 21.74 ? 202 ARG A NH1 1 ATOM 1443 N NH2 . ARG A 1 181 ? 2.725 -32.009 -27.193 1.00 25.50 ? 202 ARG A NH2 1 ATOM 1444 N N . CYS A 1 182 ? 4.220 -30.328 -18.835 1.00 19.81 ? 203 CYS A N 1 ATOM 1445 C CA . CYS A 1 182 ? 4.950 -30.261 -17.578 1.00 18.68 ? 203 CYS A CA 1 ATOM 1446 C C . CYS A 1 182 ? 4.334 -31.225 -16.576 1.00 17.52 ? 203 CYS A C 1 ATOM 1447 O O . CYS A 1 182 ? 3.168 -31.561 -16.704 1.00 15.98 ? 203 CYS A O 1 ATOM 1448 C CB . CYS A 1 182 ? 4.939 -28.847 -16.995 1.00 15.67 ? 203 CYS A CB 1 ATOM 1449 S SG . CYS A 1 182 ? 3.329 -28.054 -16.973 1.00 22.96 ? 203 CYS A SG 1 ATOM 1450 N N . ILE A 1 183 ? 5.125 -31.644 -15.583 1.00 15.29 ? 204 ILE A N 1 ATOM 1451 C CA . ILE A 1 183 ? 4.675 -32.539 -14.531 1.00 15.71 ? 204 ILE A CA 1 ATOM 1452 C C . ILE A 1 183 ? 3.870 -31.762 -13.488 1.00 18.87 ? 204 ILE A C 1 ATOM 1453 O O . ILE A 1 183 ? 4.334 -30.717 -12.963 1.00 20.23 ? 204 ILE A O 1 ATOM 1454 C CB . ILE A 1 183 ? 5.875 -33.227 -13.821 1.00 14.04 ? 204 ILE A CB 1 ATOM 1455 C CG1 . ILE A 1 183 ? 6.545 -34.243 -14.755 1.00 13.40 ? 204 ILE A CG1 1 ATOM 1456 C CG2 . ILE A 1 183 ? 5.413 -33.887 -12.504 1.00 12.78 ? 204 ILE A CG2 1 ATOM 1457 C CD1 . ILE A 1 183 ? 5.633 -35.342 -15.250 1.00 14.70 ? 204 ILE A CD1 1 ATOM 1458 N N . GLN A 1 184 ? 2.651 -32.228 -13.222 1.00 16.77 ? 205 GLN A N 1 ATOM 1459 C CA . GLN A 1 184 ? 1.850 -31.651 -12.153 1.00 18.21 ? 205 GLN A CA 1 ATOM 1460 C C . GLN A 1 184 ? 2.099 -32.420 -10.878 1.00 19.82 ? 205 GLN A C 1 ATOM 1461 O O . GLN A 1 184 ? 1.990 -33.644 -10.843 1.00 21.33 ? 205 GLN A O 1 ATOM 1462 C CB . GLN A 1 184 ? 0.341 -31.618 -12.481 1.00 19.84 ? 205 GLN A CB 1 ATOM 1463 C CG . GLN A 1 184 ? -0.003 -30.640 -13.583 1.00 24.32 ? 205 GLN A CG 1 ATOM 1464 C CD . GLN A 1 184 ? -1.458 -30.719 -14.043 1.00 26.97 ? 205 GLN A CD 1 ATOM 1465 O OE1 . GLN A 1 184 ? -1.729 -30.865 -15.229 1.00 31.65 ? 205 GLN A OE1 1 ATOM 1466 N NE2 . GLN A 1 184 ? -2.385 -30.617 -13.115 1.00 23.63 ? 205 GLN A NE2 1 ATOM 1467 N N . MET A 1 185 ? 2.442 -31.674 -9.834 1.00 21.14 ? 206 MET A N 1 ATOM 1468 C CA . MET A 1 185 ? 2.471 -32.168 -8.473 1.00 19.46 ? 206 MET A CA 1 ATOM 1469 C C . MET A 1 185 ? 1.050 -32.375 -7.970 1.00 19.00 ? 206 MET A C 1 ATOM 1470 O O . MET A 1 185 ? 0.782 -33.332 -7.256 1.00 19.43 ? 206 MET A O 1 ATOM 1471 C CB . MET A 1 185 ? 3.110 -31.097 -7.590 1.00 20.37 ? 206 MET A CB 1 ATOM 1472 C CG . MET A 1 185 ? 3.967 -31.619 -6.474 1.00 23.88 ? 206 MET A CG 1 ATOM 1473 S SD . MET A 1 185 ? 4.997 -30.260 -5.797 1.00 31.92 ? 206 MET A SD 1 ATOM 1474 C CE . MET A 1 185 ? 3.877 -29.633 -4.569 1.00 15.62 ? 206 MET A CE 1 ATOM 1475 N N . TRP A 1 186 ? 0.173 -31.411 -8.263 1.00 18.24 ? 207 TRP A N 1 ATOM 1476 C CA . TRP A 1 186 ? -1.239 -31.466 -7.827 1.00 17.21 ? 207 TRP A CA 1 ATOM 1477 C C . TRP A 1 186 ? -2.153 -31.797 -9.022 1.00 18.40 ? 207 TRP A C 1 ATOM 1478 O O . TRP A 1 186 ? -2.216 -31.042 -9.991 1.00 17.93 ? 207 TRP A O 1 ATOM 1479 C CB . TRP A 1 186 ? -1.689 -30.128 -7.240 1.00 15.35 ? 207 TRP A CB 1 ATOM 1480 C CG . TRP A 1 186 ? -1.222 -29.852 -5.830 1.00 19.16 ? 207 TRP A CG 1 ATOM 1481 C CD1 . TRP A 1 186 ? -0.063 -29.195 -5.442 1.00 18.60 ? 207 TRP A CD1 1 ATOM 1482 C CD2 . TRP A 1 186 ? -1.890 -30.224 -4.624 1.00 18.99 ? 207 TRP A CD2 1 ATOM 1483 N NE1 . TRP A 1 186 ? -0.003 -29.131 -4.066 1.00 19.00 ? 207 TRP A NE1 1 ATOM 1484 C CE2 . TRP A 1 186 ? -1.107 -29.765 -3.548 1.00 18.37 ? 207 TRP A CE2 1 ATOM 1485 C CE3 . TRP A 1 186 ? -3.084 -30.892 -4.351 1.00 21.74 ? 207 TRP A CE3 1 ATOM 1486 C CZ2 . TRP A 1 186 ? -1.488 -29.949 -2.225 1.00 19.54 ? 207 TRP A CZ2 1 ATOM 1487 C CZ3 . TRP A 1 186 ? -3.453 -31.083 -3.036 1.00 23.23 ? 207 TRP A CZ3 1 ATOM 1488 C CH2 . TRP A 1 186 ? -2.655 -30.618 -1.989 1.00 21.16 ? 207 TRP A CH2 1 ATOM 1489 N N . PHE A 1 187 ? -2.850 -32.923 -8.976 1.00 14.97 ? 208 PHE A N 1 ATOM 1490 C CA . PHE A 1 187 ? -3.838 -33.200 -10.012 1.00 15.98 ? 208 PHE A CA 1 ATOM 1491 C C . PHE A 1 187 ? -4.945 -34.061 -9.429 1.00 21.61 ? 208 PHE A C 1 ATOM 1492 O O . PHE A 1 187 ? -4.713 -34.854 -8.520 1.00 19.68 ? 208 PHE A O 1 ATOM 1493 C CB . PHE A 1 187 ? -3.201 -33.922 -11.214 1.00 18.65 ? 208 PHE A CB 1 ATOM 1494 C CG . PHE A 1 187 ? -2.517 -35.204 -10.834 1.00 19.98 ? 208 PHE A CG 1 ATOM 1495 C CD1 . PHE A 1 187 ? -1.158 -35.216 -10.528 1.00 19.32 ? 208 PHE A CD1 1 ATOM 1496 C CD2 . PHE A 1 187 ? -3.235 -36.380 -10.736 1.00 20.50 ? 208 PHE A CD2 1 ATOM 1497 C CE1 . PHE A 1 187 ? -0.516 -36.372 -10.144 1.00 19.40 ? 208 PHE A CE1 1 ATOM 1498 C CE2 . PHE A 1 187 ? -2.591 -37.555 -10.359 1.00 23.90 ? 208 PHE A CE2 1 ATOM 1499 C CZ . PHE A 1 187 ? -1.231 -37.551 -10.056 1.00 21.02 ? 208 PHE A CZ 1 ATOM 1500 N N . ASP A 1 188 ? -6.155 -33.916 -9.947 1.00 24.78 ? 209 ASP A N 1 ATOM 1501 C CA . ASP A 1 188 ? -7.165 -34.908 -9.609 1.00 28.31 ? 209 ASP A CA 1 ATOM 1502 C C . ASP A 1 188 ? -7.105 -35.966 -10.693 1.00 30.25 ? 209 ASP A C 1 ATOM 1503 O O . ASP A 1 188 ? -6.551 -35.749 -11.777 1.00 28.19 ? 209 ASP A O 1 ATOM 1504 C CB . ASP A 1 188 ? -8.546 -34.294 -9.564 1.00 31.91 ? 209 ASP A CB 1 ATOM 1505 C CG . ASP A 1 188 ? -9.013 -33.862 -10.926 1.00 36.58 ? 209 ASP A CG 1 ATOM 1506 O OD1 . ASP A 1 188 ? -9.523 -34.732 -11.660 1.00 39.78 ? 209 ASP A OD1 1 ATOM 1507 O OD2 . ASP A 1 188 ? -8.839 -32.667 -11.264 1.00 37.82 ? 209 ASP A OD2 1 ATOM 1508 N N . SER A 1 189 ? -7.695 -37.113 -10.430 1.00 33.02 ? 210 SER A N 1 ATOM 1509 C CA . SER A 1 189 ? -7.514 -38.195 -11.391 1.00 37.74 ? 210 SER A CA 1 ATOM 1510 C C . SER A 1 189 ? -8.656 -38.413 -12.383 1.00 36.22 ? 210 SER A C 1 ATOM 1511 O O . SER A 1 189 ? -8.642 -39.414 -13.081 1.00 35.76 ? 210 SER A O 1 ATOM 1512 C CB . SER A 1 189 ? -7.218 -39.496 -10.660 1.00 40.24 ? 210 SER A CB 1 ATOM 1513 O OG . SER A 1 189 ? -5.828 -39.706 -10.704 1.00 43.36 ? 210 SER A OG 1 ATOM 1514 N N . ALA A 1 190 ? -9.602 -37.476 -12.476 1.00 35.51 ? 211 ALA A N 1 ATOM 1515 C CA . ALA A 1 190 ? -10.853 -37.727 -13.232 1.00 38.51 ? 211 ALA A CA 1 ATOM 1516 C C . ALA A 1 190 ? -10.655 -38.171 -14.690 1.00 37.61 ? 211 ALA A C 1 ATOM 1517 O O . ALA A 1 190 ? -11.367 -39.036 -15.179 1.00 39.03 ? 211 ALA A O 1 ATOM 1518 C CB . ALA A 1 190 ? -11.803 -36.514 -13.168 1.00 38.73 ? 211 ALA A CB 1 ATOM 1519 N N . GLN A 1 191 ? -9.704 -37.566 -15.387 1.00 36.23 ? 212 GLN A N 1 ATOM 1520 C CA . GLN A 1 191 ? -9.420 -37.971 -16.765 1.00 38.50 ? 212 GLN A CA 1 ATOM 1521 C C . GLN A 1 191 ? -8.156 -38.816 -16.897 1.00 35.84 ? 212 GLN A C 1 ATOM 1522 O O . GLN A 1 191 ? -7.524 -38.832 -17.970 1.00 38.30 ? 212 GLN A O 1 ATOM 1523 C CB . GLN A 1 191 ? -9.351 -36.746 -17.692 1.00 38.90 ? 212 GLN A CB 1 ATOM 1524 C CG . GLN A 1 191 ? -10.745 -36.165 -17.971 1.00 43.44 ? 212 GLN A CG 1 ATOM 1525 C CD . GLN A 1 191 ? -10.754 -35.056 -19.022 1.00 44.97 ? 212 GLN A CD 1 ATOM 1526 O OE1 . GLN A 1 191 ? -9.818 -34.917 -19.825 1.00 46.17 ? 212 GLN A OE1 1 ATOM 1527 N NE2 . GLN A 1 191 ? -11.814 -34.259 -19.015 1.00 43.73 ? 212 GLN A NE2 1 ATOM 1528 N N . GLY A 1 192 ? -7.787 -39.505 -15.813 1.00 29.32 ? 213 GLY A N 1 ATOM 1529 C CA . GLY A 1 192 ? -6.526 -40.227 -15.775 1.00 25.06 ? 213 GLY A CA 1 ATOM 1530 C C . GLY A 1 192 ? -5.447 -39.423 -15.071 1.00 23.05 ? 213 GLY A C 1 ATOM 1531 O O . GLY A 1 192 ? -5.676 -38.283 -14.644 1.00 23.66 ? 213 GLY A O 1 ATOM 1532 N N . ASN A 1 193 ? -4.275 -40.029 -14.917 1.00 20.66 ? 214 ASN A N 1 ATOM 1533 C CA . ASN A 1 193 ? -3.097 -39.342 -14.394 1.00 20.38 ? 214 ASN A CA 1 ATOM 1534 C C . ASN A 1 193 ? -2.470 -38.564 -15.557 1.00 19.44 ? 214 ASN A C 1 ATOM 1535 O O . ASN A 1 193 ? -2.004 -39.164 -16.525 1.00 18.99 ? 214 ASN A O 1 ATOM 1536 C CB . ASN A 1 193 ? -2.105 -40.377 -13.826 1.00 21.89 ? 214 ASN A CB 1 ATOM 1537 C CG . ASN A 1 193 ? -0.894 -39.742 -13.211 1.00 22.29 ? 214 ASN A CG 1 ATOM 1538 O OD1 . ASN A 1 193 ? -0.430 -38.704 -13.680 1.00 23.77 ? 214 ASN A OD1 1 ATOM 1539 N ND2 . ASN A 1 193 ? -0.361 -40.361 -12.143 1.00 20.07 ? 214 ASN A ND2 1 ATOM 1540 N N . PRO A 1 194 ? -2.492 -37.226 -15.477 1.00 18.51 ? 215 PRO A N 1 ATOM 1541 C CA . PRO A 1 194 ? -2.082 -36.380 -16.610 1.00 21.61 ? 215 PRO A CA 1 ATOM 1542 C C . PRO A 1 194 ? -0.578 -36.426 -16.854 1.00 18.95 ? 215 PRO A C 1 ATOM 1543 O O . PRO A 1 194 ? -0.107 -36.115 -17.939 1.00 19.56 ? 215 PRO A O 1 ATOM 1544 C CB . PRO A 1 194 ? -2.494 -34.966 -16.177 1.00 23.92 ? 215 PRO A CB 1 ATOM 1545 C CG . PRO A 1 194 ? -2.535 -35.014 -14.665 1.00 23.67 ? 215 PRO A CG 1 ATOM 1546 C CD . PRO A 1 194 ? -2.911 -36.447 -14.297 1.00 19.45 ? 215 PRO A CD 1 ATOM 1547 N N . ASN A 1 195 ? 0.178 -36.836 -15.855 1.00 14.22 ? 216 ASN A N 1 ATOM 1548 C CA . ASN A 1 195 ? 1.617 -36.970 -16.045 1.00 15.33 ? 216 ASN A CA 1 ATOM 1549 C C . ASN A 1 195 ? 2.070 -38.152 -16.936 1.00 18.17 ? 216 ASN A C 1 ATOM 1550 O O . ASN A 1 195 ? 3.212 -38.170 -17.379 1.00 18.61 ? 216 ASN A O 1 ATOM 1551 C CB . ASN A 1 195 ? 2.313 -37.022 -14.693 1.00 14.72 ? 216 ASN A CB 1 ATOM 1552 C CG . ASN A 1 195 ? 2.131 -35.724 -13.889 1.00 17.34 ? 216 ASN A CG 1 ATOM 1553 O OD1 . ASN A 1 195 ? 2.001 -34.619 -14.462 1.00 14.85 ? 216 ASN A OD1 1 ATOM 1554 N ND2 . ASN A 1 195 ? 2.091 -35.857 -12.555 1.00 17.96 ? 216 ASN A ND2 1 ATOM 1555 N N . GLU A 1 196 ? 1.195 -39.123 -17.212 1.00 15.65 ? 217 GLU A N 1 ATOM 1556 C CA . GLU A 1 196 ? 1.579 -40.220 -18.107 1.00 19.62 ? 217 GLU A CA 1 ATOM 1557 C C . GLU A 1 196 ? 1.926 -39.691 -19.499 1.00 19.43 ? 217 GLU A C 1 ATOM 1558 O O . GLU A 1 196 ? 2.931 -40.056 -20.091 1.00 19.53 ? 217 GLU A O 1 ATOM 1559 C CB . GLU A 1 196 ? 0.448 -41.249 -18.249 1.00 23.24 ? 217 GLU A CB 1 ATOM 1560 C CG . GLU A 1 196 ? 0.101 -41.932 -16.957 1.00 29.46 ? 217 GLU A CG 1 ATOM 1561 C CD . GLU A 1 196 ? -1.101 -42.898 -17.076 1.00 35.47 ? 217 GLU A CD 1 ATOM 1562 O OE1 . GLU A 1 196 ? -1.711 -43.026 -18.180 1.00 36.74 ? 217 GLU A OE1 1 ATOM 1563 O OE2 . GLU A 1 196 ? -1.426 -43.540 -16.046 1.00 36.18 ? 217 GLU A OE2 1 ATOM 1564 N N . GLU A 1 197 ? 1.041 -38.857 -20.020 1.00 18.18 ? 218 GLU A N 1 ATOM 1565 C CA . GLU A 1 197 ? 1.212 -38.251 -21.315 1.00 19.16 ? 218 GLU A CA 1 ATOM 1566 C C . GLU A 1 197 ? 2.501 -37.416 -21.306 1.00 16.19 ? 218 GLU A C 1 ATOM 1567 O O . GLU A 1 197 ? 3.232 -37.390 -22.289 1.00 16.12 ? 218 GLU A O 1 ATOM 1568 C CB . GLU A 1 197 ? -0.025 -37.394 -21.659 1.00 23.58 ? 218 GLU A CB 1 ATOM 1569 C CG . GLU A 1 197 ? 0.231 -36.370 -22.748 1.00 29.95 ? 218 GLU A CG 1 ATOM 1570 C CD . GLU A 1 197 ? -0.880 -35.295 -22.901 1.00 45.29 ? 218 GLU A CD 1 ATOM 1571 O OE1 . GLU A 1 197 ? -1.626 -35.018 -21.924 1.00 44.91 ? 218 GLU A OE1 1 ATOM 1572 O OE2 . GLU A 1 197 ? -0.989 -34.728 -24.017 1.00 43.84 ? 218 GLU A OE2 1 ATOM 1573 N N . VAL A 1 198 ? 2.805 -36.774 -20.186 1.00 16.71 ? 219 VAL A N 1 ATOM 1574 C CA . VAL A 1 198 ? 4.022 -35.941 -20.108 1.00 16.65 ? 219 VAL A CA 1 ATOM 1575 C C . VAL A 1 198 ? 5.314 -36.766 -20.187 1.00 18.60 ? 219 VAL A C 1 ATOM 1576 O O . VAL A 1 198 ? 6.270 -36.403 -20.877 1.00 18.27 ? 219 VAL A O 1 ATOM 1577 C CB . VAL A 1 198 ? 4.058 -35.072 -18.827 1.00 16.67 ? 219 VAL A CB 1 ATOM 1578 C CG1 . VAL A 1 198 ? 5.389 -34.295 -18.731 1.00 16.37 ? 219 VAL A CG1 1 ATOM 1579 C CG2 . VAL A 1 198 ? 2.841 -34.087 -18.772 1.00 16.23 ? 219 VAL A CG2 1 ATOM 1580 N N . ALA A 1 199 ? 5.341 -37.869 -19.456 1.00 16.17 ? 220 ALA A N 1 ATOM 1581 C CA . ALA A 1 199 ? 6.501 -38.756 -19.443 1.00 16.36 ? 220 ALA A CA 1 ATOM 1582 C C . ALA A 1 199 ? 6.730 -39.279 -20.843 1.00 16.83 ? 220 ALA A C 1 ATOM 1583 O O . ALA A 1 199 ? 7.857 -39.386 -21.306 1.00 19.87 ? 220 ALA A O 1 ATOM 1584 C CB . ALA A 1 199 ? 6.264 -39.905 -18.456 1.00 15.27 ? 220 ALA A CB 1 ATOM 1585 N N . ARG A 1 200 ? 5.631 -39.551 -21.531 1.00 18.28 ? 221 ARG A N 1 ATOM 1586 C CA A ARG A 1 200 ? 5.645 -40.086 -22.885 0.56 19.93 ? 221 ARG A CA 1 ATOM 1587 C CA B ARG A 1 200 ? 5.681 -40.098 -22.880 0.44 19.76 ? 221 ARG A CA 1 ATOM 1588 C C . ARG A 1 200 ? 6.238 -39.070 -23.862 1.00 19.48 ? 221 ARG A C 1 ATOM 1589 O O . ARG A 1 200 ? 7.100 -39.402 -24.687 1.00 20.54 ? 221 ARG A O 1 ATOM 1590 C CB A ARG A 1 200 ? 4.203 -40.448 -23.273 0.56 21.24 ? 221 ARG A CB 1 ATOM 1591 C CB B ARG A 1 200 ? 4.283 -40.561 -23.309 0.44 20.98 ? 221 ARG A CB 1 ATOM 1592 C CG A ARG A 1 200 ? 3.972 -41.050 -24.643 0.56 22.37 ? 221 ARG A CG 1 ATOM 1593 C CG B ARG A 1 200 ? 4.237 -41.644 -24.375 0.44 22.25 ? 221 ARG A CG 1 ATOM 1594 C CD A ARG A 1 200 ? 2.475 -41.467 -24.796 0.56 23.68 ? 221 ARG A CD 1 ATOM 1595 C CD B ARG A 1 200 ? 2.944 -42.465 -24.228 0.44 23.60 ? 221 ARG A CD 1 ATOM 1596 N NE A ARG A 1 200 ? 2.038 -42.408 -23.759 0.56 24.65 ? 221 ARG A NE 1 ATOM 1597 N NE B ARG A 1 200 ? 2.520 -43.167 -25.440 0.44 25.04 ? 221 ARG A NE 1 ATOM 1598 C CZ A ARG A 1 200 ? 1.010 -42.229 -22.921 0.56 24.58 ? 221 ARG A CZ 1 ATOM 1599 C CZ B ARG A 1 200 ? 2.877 -44.410 -25.756 0.44 25.76 ? 221 ARG A CZ 1 ATOM 1600 N NH1 A ARG A 1 200 ? 0.253 -41.136 -22.969 0.56 21.60 ? 221 ARG A NH1 1 ATOM 1601 N NH1 B ARG A 1 200 ? 3.695 -45.086 -24.962 0.44 23.92 ? 221 ARG A NH1 1 ATOM 1602 N NH2 A ARG A 1 200 ? 0.729 -43.173 -22.027 0.56 25.85 ? 221 ARG A NH2 1 ATOM 1603 N NH2 B ARG A 1 200 ? 2.429 -44.974 -26.876 0.44 24.78 ? 221 ARG A NH2 1 ATOM 1604 N N . PHE A 1 201 ? 5.777 -37.826 -23.757 1.00 16.48 ? 222 PHE A N 1 ATOM 1605 C CA . PHE A 1 201 ? 6.289 -36.755 -24.595 1.00 18.55 ? 222 PHE A CA 1 ATOM 1606 C C . PHE A 1 201 ? 7.798 -36.526 -24.388 1.00 18.36 ? 222 PHE A C 1 ATOM 1607 O O . PHE A 1 201 ? 8.549 -36.496 -25.370 1.00 18.61 ? 222 PHE A O 1 ATOM 1608 C CB . PHE A 1 201 ? 5.525 -35.439 -24.382 1.00 17.86 ? 222 PHE A CB 1 ATOM 1609 C CG . PHE A 1 201 ? 6.096 -34.275 -25.171 1.00 21.11 ? 222 PHE A CG 1 ATOM 1610 C CD1 . PHE A 1 201 ? 5.764 -34.097 -26.514 1.00 23.04 ? 222 PHE A CD1 1 ATOM 1611 C CD2 . PHE A 1 201 ? 6.972 -33.355 -24.564 1.00 20.76 ? 222 PHE A CD2 1 ATOM 1612 C CE1 . PHE A 1 201 ? 6.288 -33.017 -27.239 1.00 25.01 ? 222 PHE A CE1 1 ATOM 1613 C CE2 . PHE A 1 201 ? 7.496 -32.276 -25.280 1.00 19.40 ? 222 PHE A CE2 1 ATOM 1614 C CZ . PHE A 1 201 ? 7.157 -32.100 -26.610 1.00 22.89 ? 222 PHE A CZ 1 ATOM 1615 N N . TYR A 1 202 ? 8.239 -36.372 -23.141 1.00 16.59 ? 223 TYR A N 1 ATOM 1616 C CA . TYR A 1 202 ? 9.678 -36.113 -22.890 1.00 17.03 ? 223 TYR A CA 1 ATOM 1617 C C . TYR A 1 202 ? 10.624 -37.287 -23.138 1.00 19.93 ? 223 TYR A C 1 ATOM 1618 O O . TYR A 1 202 ? 11.794 -37.069 -23.508 1.00 18.43 ? 223 TYR A O 1 ATOM 1619 C CB . TYR A 1 202 ? 9.931 -35.491 -21.515 1.00 16.11 ? 223 TYR A CB 1 ATOM 1620 C CG . TYR A 1 202 ? 9.445 -34.049 -21.501 1.00 15.86 ? 223 TYR A CG 1 ATOM 1621 C CD1 . TYR A 1 202 ? 10.136 -33.072 -22.195 1.00 15.71 ? 223 TYR A CD1 1 ATOM 1622 C CD2 . TYR A 1 202 ? 8.248 -33.698 -20.860 1.00 13.43 ? 223 TYR A CD2 1 ATOM 1623 C CE1 . TYR A 1 202 ? 9.689 -31.758 -22.234 1.00 18.09 ? 223 TYR A CE1 1 ATOM 1624 C CE2 . TYR A 1 202 ? 7.790 -32.394 -20.872 1.00 15.01 ? 223 TYR A CE2 1 ATOM 1625 C CZ . TYR A 1 202 ? 8.523 -31.422 -21.560 1.00 17.45 ? 223 TYR A CZ 1 ATOM 1626 O OH . TYR A 1 202 ? 8.078 -30.133 -21.610 1.00 20.30 ? 223 TYR A OH 1 ATOM 1627 N N . ALA A 1 203 ? 10.146 -38.524 -22.939 1.00 19.45 ? 224 ALA A N 1 ATOM 1628 C CA . ALA A 1 203 ? 10.985 -39.678 -23.271 1.00 21.09 ? 224 ALA A CA 1 ATOM 1629 C C . ALA A 1 203 ? 11.508 -39.519 -24.709 1.00 22.58 ? 224 ALA A C 1 ATOM 1630 O O . ALA A 1 203 ? 12.685 -39.741 -24.985 1.00 23.18 ? 224 ALA A O 1 ATOM 1631 C CB . ALA A 1 203 ? 10.215 -41.055 -23.095 1.00 16.30 ? 224 ALA A CB 1 ATOM 1632 N N . ALA A 1 204 ? 10.624 -39.134 -25.624 1.00 21.30 ? 225 ALA A N 1 ATOM 1633 C CA . ALA A 1 204 ? 11.012 -38.994 -27.021 1.00 24.99 ? 225 ALA A CA 1 ATOM 1634 C C . ALA A 1 204 ? 11.689 -37.656 -27.276 1.00 26.35 ? 225 ALA A C 1 ATOM 1635 O O . ALA A 1 204 ? 12.688 -37.607 -27.986 1.00 27.21 ? 225 ALA A O 1 ATOM 1636 C CB . ALA A 1 204 ? 9.808 -39.187 -27.955 1.00 27.11 ? 225 ALA A CB 1 ATOM 1637 N N . ALA A 1 205 ? 11.165 -36.578 -26.682 1.00 26.38 ? 226 ALA A N 1 ATOM 1638 C CA . ALA A 1 205 ? 11.716 -35.226 -26.905 1.00 26.26 ? 226 ALA A CA 1 ATOM 1639 C C . ALA A 1 205 ? 13.155 -35.024 -26.379 1.00 29.34 ? 226 ALA A C 1 ATOM 1640 O O . ALA A 1 205 ? 13.937 -34.264 -26.934 1.00 28.95 ? 226 ALA A O 1 ATOM 1641 C CB . ALA A 1 205 ? 10.781 -34.164 -26.315 1.00 18.01 ? 226 ALA A CB 1 ATOM 1642 N N . MET A 1 206 ? 13.479 -35.684 -25.278 1.00 17.91 ? 227 MET A N 1 ATOM 1643 C CA . MET A 1 206 ? 14.837 -35.658 -24.701 1.00 20.91 ? 227 MET A CA 1 ATOM 1644 C C . MET A 1 206 ? 15.794 -36.637 -25.354 1.00 24.79 ? 227 MET A C 1 ATOM 1645 O O . MET A 1 206 ? 16.960 -36.656 -25.004 1.00 26.13 ? 227 MET A O 1 ATOM 1646 C CB . MET A 1 206 ? 14.786 -35.992 -23.197 1.00 18.16 ? 227 MET A CB 1 ATOM 1647 C CG . MET A 1 206 ? 14.097 -34.891 -22.387 1.00 18.79 ? 227 MET A CG 1 ATOM 1648 S SD . MET A 1 206 ? 13.655 -35.385 -20.712 1.00 22.38 ? 227 MET A SD 1 ATOM 1649 C CE . MET A 1 206 ? 15.261 -35.207 -19.916 1.00 25.90 ? 227 MET A CE 1 ATOM 1650 N N . HIS A 1 207 ? 15.312 -37.450 -26.288 1.00 27.67 ? 228 HIS A N 1 ATOM 1651 C CA . HIS A 1 207 ? 16.123 -38.558 -26.813 1.00 32.44 ? 228 HIS A CA 1 ATOM 1652 C C . HIS A 1 207 ? 17.254 -38.135 -27.761 1.00 35.12 ? 228 HIS A C 1 ATOM 1653 O O . HIS A 1 207 ? 18.414 -38.521 -27.553 1.00 35.95 ? 228 HIS A O 1 ATOM 1654 C CB . HIS A 1 207 ? 15.230 -39.600 -27.483 1.00 35.70 ? 228 HIS A CB 1 ATOM 1655 C CG . HIS A 1 207 ? 15.971 -40.805 -27.968 1.00 40.05 ? 228 HIS A CG 1 ATOM 1656 N ND1 . HIS A 1 207 ? 16.589 -41.694 -27.112 1.00 40.72 ? 228 HIS A ND1 1 ATOM 1657 C CD2 . HIS A 1 207 ? 16.203 -41.262 -29.224 1.00 39.31 ? 228 HIS A CD2 1 ATOM 1658 C CE1 . HIS A 1 207 ? 17.170 -42.647 -27.821 1.00 39.83 ? 228 HIS A CE1 1 ATOM 1659 N NE2 . HIS A 1 207 ? 16.948 -42.407 -29.103 1.00 38.60 ? 228 HIS A NE2 1 ATOM 1660 O OXT . HIS A 1 207 ? 17.054 -37.402 -28.740 1.00 34.89 ? 228 HIS A OXT 1 HETATM 1661 N N1 . MTX B 2 . ? 14.228 -35.979 -3.210 1.00 21.88 ? 301 MTX A N1 1 HETATM 1662 C C2 . MTX B 2 . ? 13.235 -35.370 -3.946 1.00 20.05 ? 301 MTX A C2 1 HETATM 1663 N NA2 . MTX B 2 . ? 13.487 -35.006 -5.194 1.00 16.68 ? 301 MTX A NA2 1 HETATM 1664 N N3 . MTX B 2 . ? 11.987 -35.153 -3.397 1.00 19.74 ? 301 MTX A N3 1 HETATM 1665 C C4 . MTX B 2 . ? 11.739 -35.541 -2.096 1.00 21.57 ? 301 MTX A C4 1 HETATM 1666 N NA4 . MTX B 2 . ? 10.532 -35.364 -1.567 1.00 21.37 ? 301 MTX A NA4 1 HETATM 1667 C C4A . MTX B 2 . ? 12.739 -36.145 -1.342 1.00 23.14 ? 301 MTX A C4A 1 HETATM 1668 N N5 . MTX B 2 . ? 12.490 -36.545 -0.035 1.00 23.52 ? 301 MTX A N5 1 HETATM 1669 C C6 . MTX B 2 . ? 13.514 -37.160 0.698 1.00 23.54 ? 301 MTX A C6 1 HETATM 1670 C C7 . MTX B 2 . ? 14.777 -37.344 0.134 1.00 24.55 ? 301 MTX A C7 1 HETATM 1671 N N8 . MTX B 2 . ? 15.020 -36.950 -1.166 1.00 24.64 ? 301 MTX A N8 1 HETATM 1672 C C8A . MTX B 2 . ? 13.998 -36.350 -1.905 1.00 24.04 ? 301 MTX A C8A 1 HETATM 1673 C C9 . MTX B 2 . ? 13.292 -37.598 2.129 1.00 22.82 ? 301 MTX A C9 1 HETATM 1674 N N10 . MTX B 2 . ? 13.948 -36.646 3.024 1.00 22.60 ? 301 MTX A N10 1 HETATM 1675 C CM . MTX B 2 . ? 13.331 -35.316 3.207 1.00 19.96 ? 301 MTX A CM 1 HETATM 1676 C C11 . MTX B 2 . ? 18.012 -37.145 3.930 1.00 23.11 ? 301 MTX A C11 1 HETATM 1677 C C12 . MTX B 2 . ? 17.195 -38.277 3.746 1.00 21.11 ? 301 MTX A C12 1 HETATM 1678 C C13 . MTX B 2 . ? 15.836 -38.116 3.443 1.00 21.54 ? 301 MTX A C13 1 HETATM 1679 C C14 . MTX B 2 . ? 15.308 -36.835 3.335 1.00 20.38 ? 301 MTX A C14 1 HETATM 1680 C C15 . MTX B 2 . ? 16.125 -35.722 3.524 1.00 22.25 ? 301 MTX A C15 1 HETATM 1681 C C16 . MTX B 2 . ? 17.475 -35.860 3.823 1.00 21.88 ? 301 MTX A C16 1 HETATM 1682 C C . MTX B 2 . ? 19.472 -37.291 4.286 1.00 24.86 ? 301 MTX A C 1 HETATM 1683 O O . MTX B 2 . ? 19.868 -38.475 4.911 1.00 29.10 ? 301 MTX A O 1 HETATM 1684 N N . MTX B 2 . ? 20.336 -36.308 4.036 1.00 25.14 ? 301 MTX A N 1 HETATM 1685 C CA . MTX B 2 . ? 21.716 -36.342 4.484 1.00 27.24 ? 301 MTX A CA 1 HETATM 1686 C CT . MTX B 2 . ? 22.188 -34.968 4.892 1.00 25.46 ? 301 MTX A CT 1 HETATM 1687 O O1 . MTX B 2 . ? 23.355 -34.569 4.625 1.00 26.59 ? 301 MTX A O1 1 HETATM 1688 O O2 . MTX B 2 . ? 21.421 -34.194 5.494 1.00 21.01 ? 301 MTX A O2 1 HETATM 1689 C CB . MTX B 2 . ? 22.582 -36.794 3.313 1.00 31.22 ? 301 MTX A CB 1 HETATM 1690 C CG . MTX B 2 . ? 22.722 -38.297 3.301 1.00 37.43 ? 301 MTX A CG 1 HETATM 1691 C CD . MTX B 2 . ? 23.706 -38.670 2.223 1.00 39.98 ? 301 MTX A CD 1 HETATM 1692 O OE1 . MTX B 2 . ? 24.933 -38.490 2.406 1.00 44.77 ? 301 MTX A OE1 1 HETATM 1693 O OE2 . MTX B 2 . ? 23.302 -39.154 1.148 1.00 36.82 ? 301 MTX A OE2 1 HETATM 1694 K K . K C 3 . ? 2.627 -38.992 -11.533 1.00 20.31 ? 302 K A K 1 HETATM 1695 CL CL . CL D 4 . ? -7.113 -23.209 -0.528 1.00 54.59 ? 303 CL A CL 1 HETATM 1696 CL CL . CL E 4 . ? 15.171 -47.591 8.281 0.50 57.34 ? 304 CL A CL 1 HETATM 1697 C C1 . NAG F 5 . ? 7.116 -18.324 -21.000 1.00 23.42 ? 305 NAG A C1 1 HETATM 1698 C C2 . NAG F 5 . ? 8.006 -17.597 -22.018 1.00 24.30 ? 305 NAG A C2 1 HETATM 1699 C C3 . NAG F 5 . ? 7.502 -16.166 -22.299 1.00 28.65 ? 305 NAG A C3 1 HETATM 1700 C C4 . NAG F 5 . ? 5.998 -16.145 -22.590 1.00 35.39 ? 305 NAG A C4 1 HETATM 1701 C C5 . NAG F 5 . ? 5.297 -16.839 -21.426 1.00 34.14 ? 305 NAG A C5 1 HETATM 1702 C C6 . NAG F 5 . ? 3.782 -16.852 -21.602 1.00 39.26 ? 305 NAG A C6 1 HETATM 1703 C C7 . NAG F 5 . ? 10.394 -18.108 -22.283 1.00 22.53 ? 305 NAG A C7 1 HETATM 1704 C C8 . NAG F 5 . ? 11.774 -18.026 -21.684 1.00 19.69 ? 305 NAG A C8 1 HETATM 1705 N N2 . NAG F 5 . ? 9.385 -17.572 -21.558 1.00 23.09 ? 305 NAG A N2 1 HETATM 1706 O O3 . NAG F 5 . ? 8.205 -15.637 -23.392 1.00 25.50 ? 305 NAG A O3 1 HETATM 1707 O O4 . NAG F 5 . ? 5.489 -14.829 -22.778 1.00 42.15 ? 305 NAG A O4 1 HETATM 1708 O O5 . NAG F 5 . ? 5.746 -18.168 -21.329 1.00 26.20 ? 305 NAG A O5 1 HETATM 1709 O O6 . NAG F 5 . ? 3.443 -17.771 -22.619 1.00 42.21 ? 305 NAG A O6 1 HETATM 1710 O O7 . NAG F 5 . ? 10.242 -18.654 -23.389 1.00 20.67 ? 305 NAG A O7 1 HETATM 1711 C C1 . NAG G 5 . ? 5.466 -13.726 -23.751 1.00 53.46 ? 306 NAG A C1 1 HETATM 1712 C C2 . NAG G 5 . ? 4.641 -12.459 -23.503 1.00 60.73 ? 306 NAG A C2 1 HETATM 1713 C C3 . NAG G 5 . ? 4.397 -11.644 -24.760 1.00 62.66 ? 306 NAG A C3 1 HETATM 1714 C C4 . NAG G 5 . ? 5.757 -11.287 -25.346 1.00 61.28 ? 306 NAG A C4 1 HETATM 1715 C C5 . NAG G 5 . ? 6.532 -12.591 -25.635 1.00 58.77 ? 306 NAG A C5 1 HETATM 1716 C C6 . NAG G 5 . ? 7.939 -12.354 -26.225 1.00 56.81 ? 306 NAG A C6 1 HETATM 1717 C C7 . NAG G 5 . ? 3.252 -12.562 -21.585 1.00 67.85 ? 306 NAG A C7 1 HETATM 1718 C C8 . NAG G 5 . ? 1.872 -12.727 -21.017 1.00 68.62 ? 306 NAG A C8 1 HETATM 1719 N N2 . NAG G 5 . ? 3.374 -12.784 -22.888 1.00 64.85 ? 306 NAG A N2 1 HETATM 1720 O O3 . NAG G 5 . ? 3.646 -10.490 -24.419 1.00 65.48 ? 306 NAG A O3 1 HETATM 1721 O O4 . NAG G 5 . ? 5.586 -10.434 -26.476 1.00 61.36 ? 306 NAG A O4 1 HETATM 1722 O O5 . NAG G 5 . ? 6.648 -13.421 -24.483 1.00 56.71 ? 306 NAG A O5 1 HETATM 1723 O O6 . NAG G 5 . ? 9.009 -12.561 -25.320 1.00 52.50 ? 306 NAG A O6 1 HETATM 1724 O O7 . NAG G 5 . ? 4.218 -12.236 -20.879 1.00 68.41 ? 306 NAG A O7 1 HETATM 1725 C C1 . NAG H 5 . ? 29.578 -43.099 -8.254 1.00 41.65 ? 307 NAG A C1 1 HETATM 1726 C C2 . NAG H 5 . ? 29.616 -42.049 -9.370 1.00 48.24 ? 307 NAG A C2 1 HETATM 1727 C C3 . NAG H 5 . ? 30.479 -42.527 -10.535 1.00 51.71 ? 307 NAG A C3 1 HETATM 1728 C C4 . NAG H 5 . ? 31.842 -42.999 -10.028 1.00 54.98 ? 307 NAG A C4 1 HETATM 1729 C C5 . NAG H 5 . ? 31.703 -44.054 -8.925 1.00 50.02 ? 307 NAG A C5 1 HETATM 1730 C C6 . NAG H 5 . ? 33.066 -44.526 -8.381 1.00 49.57 ? 307 NAG A C6 1 HETATM 1731 C C7 . NAG H 5 . ? 27.937 -40.357 -9.829 1.00 49.90 ? 307 NAG A C7 1 HETATM 1732 C C8 . NAG H 5 . ? 26.575 -39.966 -10.338 1.00 48.16 ? 307 NAG A C8 1 HETATM 1733 N N2 . NAG H 5 . ? 28.293 -41.651 -9.853 1.00 50.04 ? 307 NAG A N2 1 HETATM 1734 O O3 . NAG H 5 . ? 30.604 -41.482 -11.486 1.00 50.23 ? 307 NAG A O3 1 HETATM 1735 O O4 . NAG H 5 . ? 32.575 -43.534 -11.105 1.00 62.68 ? 307 NAG A O4 1 HETATM 1736 O O5 . NAG H 5 . ? 30.869 -43.576 -7.880 1.00 45.32 ? 307 NAG A O5 1 HETATM 1737 O O6 . NAG H 5 . ? 33.804 -43.509 -7.714 1.00 49.95 ? 307 NAG A O6 1 HETATM 1738 O O7 . NAG H 5 . ? 28.693 -39.483 -9.406 1.00 50.23 ? 307 NAG A O7 1 HETATM 1739 C C1 . NAG I 5 . ? 33.951 -43.184 -11.296 1.00 68.40 ? 308 NAG A C1 1 HETATM 1740 C C2 . NAG I 5 . ? 34.710 -44.293 -12.027 1.00 71.78 ? 308 NAG A C2 1 HETATM 1741 C C3 . NAG I 5 . ? 36.103 -43.856 -12.470 1.00 72.91 ? 308 NAG A C3 1 HETATM 1742 C C4 . NAG I 5 . ? 36.101 -42.473 -13.115 1.00 72.04 ? 308 NAG A C4 1 HETATM 1743 C C5 . NAG I 5 . ? 35.358 -41.482 -12.214 1.00 70.50 ? 308 NAG A C5 1 HETATM 1744 C C6 . NAG I 5 . ? 35.248 -40.078 -12.802 1.00 69.23 ? 308 NAG A C6 1 HETATM 1745 C C7 . NAG I 5 . ? 34.057 -46.521 -11.310 1.00 76.61 ? 308 NAG A C7 1 HETATM 1746 C C8 . NAG I 5 . ? 34.279 -47.631 -10.319 1.00 77.19 ? 308 NAG A C8 1 HETATM 1747 N N2 . NAG I 5 . ? 34.827 -45.448 -11.152 1.00 74.10 ? 308 NAG A N2 1 HETATM 1748 O O3 . NAG I 5 . ? 36.609 -44.807 -13.381 1.00 74.33 ? 308 NAG A O3 1 HETATM 1749 O O4 . NAG I 5 . ? 37.440 -42.070 -13.350 1.00 71.72 ? 308 NAG A O4 1 HETATM 1750 O O5 . NAG I 5 . ? 34.043 -41.927 -11.941 1.00 69.35 ? 308 NAG A O5 1 HETATM 1751 O O6 . NAG I 5 . ? 34.498 -39.287 -11.905 1.00 67.80 ? 308 NAG A O6 1 HETATM 1752 O O7 . NAG I 5 . ? 33.208 -46.613 -12.208 1.00 76.86 ? 308 NAG A O7 1 HETATM 1753 O O . HOH J 6 . ? -0.340 -26.121 -7.187 1.00 15.90 ? 401 HOH A O 1 HETATM 1754 O O . HOH J 6 . ? 17.638 -35.338 -16.147 1.00 15.97 ? 402 HOH A O 1 HETATM 1755 O O . HOH J 6 . ? 6.569 -47.257 -0.899 1.00 13.81 ? 403 HOH A O 1 HETATM 1756 O O . HOH J 6 . ? 10.321 -43.616 -9.653 1.00 18.72 ? 404 HOH A O 1 HETATM 1757 O O . HOH J 6 . ? 16.796 -27.488 -11.819 1.00 19.07 ? 405 HOH A O 1 HETATM 1758 O O . HOH J 6 . ? 8.489 -32.702 0.333 1.00 17.59 ? 406 HOH A O 1 HETATM 1759 O O . HOH J 6 . ? 14.858 -29.855 -6.338 1.00 15.19 ? 407 HOH A O 1 HETATM 1760 O O . HOH J 6 . ? 18.917 -32.765 -16.562 0.50 19.21 ? 408 HOH A O 1 HETATM 1761 O O . HOH J 6 . ? 20.472 -33.933 15.044 1.00 22.20 ? 409 HOH A O 1 HETATM 1762 O O . HOH J 6 . ? 8.553 -42.044 -7.944 1.00 19.25 ? 410 HOH A O 1 HETATM 1763 O O . HOH J 6 . ? -2.231 -35.271 -7.210 1.00 17.22 ? 411 HOH A O 1 HETATM 1764 O O . HOH J 6 . ? 8.738 -42.855 -12.088 1.00 17.89 ? 412 HOH A O 1 HETATM 1765 O O . HOH J 6 . ? 13.990 -42.689 -1.488 1.00 20.26 ? 413 HOH A O 1 HETATM 1766 O O . HOH J 6 . ? 5.506 -43.142 -17.602 1.00 18.96 ? 414 HOH A O 1 HETATM 1767 O O . HOH J 6 . ? 10.149 -34.365 -5.299 1.00 20.41 ? 415 HOH A O 1 HETATM 1768 O O . HOH J 6 . ? 5.421 -21.064 13.821 1.00 43.18 ? 416 HOH A O 1 HETATM 1769 O O . HOH J 6 . ? 10.453 -38.817 7.153 1.00 16.51 ? 417 HOH A O 1 HETATM 1770 O O . HOH J 6 . ? 20.459 -28.582 -15.025 1.00 15.40 ? 418 HOH A O 1 HETATM 1771 O O . HOH J 6 . ? 1.896 -26.441 -5.517 1.00 14.63 ? 419 HOH A O 1 HETATM 1772 O O . HOH J 6 . ? -7.646 -41.438 2.655 1.00 29.23 ? 420 HOH A O 1 HETATM 1773 O O . HOH J 6 . ? 3.475 -20.655 5.374 1.00 17.46 ? 421 HOH A O 1 HETATM 1774 O O . HOH J 6 . ? -1.141 -42.891 -11.408 1.00 23.12 ? 422 HOH A O 1 HETATM 1775 O O . HOH J 6 . ? 27.936 -26.154 8.797 1.00 23.03 ? 423 HOH A O 1 HETATM 1776 O O . HOH J 6 . ? 12.231 -49.784 -7.099 1.00 21.68 ? 424 HOH A O 1 HETATM 1777 O O . HOH J 6 . ? 24.853 -35.682 11.052 1.00 25.64 ? 425 HOH A O 1 HETATM 1778 O O . HOH J 6 . ? 10.129 -50.268 -12.478 1.00 22.08 ? 426 HOH A O 1 HETATM 1779 O O . HOH J 6 . ? 3.978 -42.633 -19.828 1.00 16.52 ? 427 HOH A O 1 HETATM 1780 O O . HOH J 6 . ? 11.709 -44.216 -1.771 1.00 16.63 ? 428 HOH A O 1 HETATM 1781 O O . HOH J 6 . ? 20.816 -23.903 -6.896 1.00 35.61 ? 429 HOH A O 1 HETATM 1782 O O . HOH J 6 . ? 15.821 -36.470 -6.745 1.00 22.78 ? 430 HOH A O 1 HETATM 1783 O O . HOH J 6 . ? 17.270 -27.406 14.389 1.00 33.05 ? 431 HOH A O 1 HETATM 1784 O O . HOH J 6 . ? 6.862 -37.901 5.673 1.00 22.84 ? 432 HOH A O 1 HETATM 1785 O O . HOH J 6 . ? 9.858 -24.327 -20.391 1.00 19.96 ? 433 HOH A O 1 HETATM 1786 O O . HOH J 6 . ? 7.898 -45.315 -2.310 1.00 22.96 ? 434 HOH A O 1 HETATM 1787 O O . HOH J 6 . ? 22.539 -18.929 8.476 1.00 22.56 ? 435 HOH A O 1 HETATM 1788 O O . HOH J 6 . ? 8.100 -23.325 9.732 1.00 19.59 ? 436 HOH A O 1 HETATM 1789 O O . HOH J 6 . ? 9.841 -33.438 2.554 1.00 22.77 ? 437 HOH A O 1 HETATM 1790 O O . HOH J 6 . ? 26.428 -22.058 14.901 1.00 21.22 ? 438 HOH A O 1 HETATM 1791 O O . HOH J 6 . ? -1.730 -38.605 -19.165 1.00 18.03 ? 439 HOH A O 1 HETATM 1792 O O . HOH J 6 . ? 14.364 -30.951 14.077 1.00 24.51 ? 440 HOH A O 1 HETATM 1793 O O . HOH J 6 . ? 10.178 -38.416 0.442 1.00 23.97 ? 441 HOH A O 1 HETATM 1794 O O . HOH J 6 . ? 10.023 -27.328 -19.551 1.00 20.93 ? 442 HOH A O 1 HETATM 1795 O O . HOH J 6 . ? 7.692 -32.968 10.480 1.00 26.74 ? 443 HOH A O 1 HETATM 1796 O O . HOH J 6 . ? 16.870 -35.514 -4.331 1.00 32.59 ? 444 HOH A O 1 HETATM 1797 O O . HOH J 6 . ? -12.064 -34.238 -10.877 1.00 27.86 ? 445 HOH A O 1 HETATM 1798 O O . HOH J 6 . ? -3.506 -34.608 -3.287 1.00 13.86 ? 446 HOH A O 1 HETATM 1799 O O . HOH J 6 . ? 10.424 -25.244 9.782 1.00 19.63 ? 447 HOH A O 1 HETATM 1800 O O . HOH J 6 . ? 17.716 -47.941 -3.483 1.00 35.81 ? 448 HOH A O 1 HETATM 1801 O O . HOH J 6 . ? 21.624 -22.604 3.141 1.00 25.75 ? 449 HOH A O 1 HETATM 1802 O O . HOH J 6 . ? 10.367 -40.745 13.183 1.00 29.54 ? 450 HOH A O 1 HETATM 1803 O O . HOH J 6 . ? 2.425 -45.002 -16.152 1.00 19.28 ? 451 HOH A O 1 HETATM 1804 O O . HOH J 6 . ? -4.091 -42.994 -10.343 1.00 20.67 ? 452 HOH A O 1 HETATM 1805 O O . HOH J 6 . ? 0.132 -43.212 -13.829 1.00 22.55 ? 453 HOH A O 1 HETATM 1806 O O . HOH J 6 . ? 9.626 -37.597 4.721 1.00 25.85 ? 454 HOH A O 1 HETATM 1807 O O . HOH J 6 . ? 21.967 -24.544 -1.130 1.00 25.44 ? 455 HOH A O 1 HETATM 1808 O O . HOH J 6 . ? 23.580 -31.106 -3.744 1.00 22.78 ? 456 HOH A O 1 HETATM 1809 O O . HOH J 6 . ? -6.498 -35.904 -15.750 1.00 33.41 ? 457 HOH A O 1 HETATM 1810 O O . HOH J 6 . ? 5.915 -50.432 2.603 1.00 49.32 ? 458 HOH A O 1 HETATM 1811 O O . HOH J 6 . ? 14.557 -17.189 -10.022 1.00 15.67 ? 459 HOH A O 1 HETATM 1812 O O . HOH J 6 . ? 7.240 -16.172 -10.432 1.00 35.72 ? 460 HOH A O 1 HETATM 1813 O O . HOH J 6 . ? 1.546 -23.817 -21.238 1.00 34.59 ? 461 HOH A O 1 HETATM 1814 O O . HOH J 6 . ? 23.420 -28.835 0.406 1.00 26.63 ? 462 HOH A O 1 HETATM 1815 O O . HOH J 6 . ? 23.364 -46.410 -8.390 1.00 27.96 ? 463 HOH A O 1 HETATM 1816 O O . HOH J 6 . ? 0.598 -32.938 -16.210 1.00 23.22 ? 464 HOH A O 1 HETATM 1817 O O . HOH J 6 . ? 18.419 -14.024 0.703 1.00 41.39 ? 465 HOH A O 1 HETATM 1818 O O . HOH J 6 . ? -0.142 -51.462 -0.539 1.00 37.13 ? 466 HOH A O 1 HETATM 1819 O O . HOH J 6 . ? 2.205 -17.916 3.087 1.00 29.05 ? 467 HOH A O 1 HETATM 1820 O O . HOH J 6 . ? 21.652 -25.533 2.800 1.00 26.68 ? 468 HOH A O 1 HETATM 1821 O O . HOH J 6 . ? 16.336 -16.889 -6.561 1.00 35.45 ? 469 HOH A O 1 HETATM 1822 O O . HOH J 6 . ? 8.930 -15.706 3.646 1.00 27.10 ? 470 HOH A O 1 HETATM 1823 O O . HOH J 6 . ? 1.202 -51.266 2.452 1.00 27.78 ? 471 HOH A O 1 HETATM 1824 O O . HOH J 6 . ? 21.508 -27.360 -4.362 1.00 26.17 ? 472 HOH A O 1 HETATM 1825 O O . HOH J 6 . ? 14.917 -48.277 -11.744 1.00 43.63 ? 473 HOH A O 1 HETATM 1826 O O . HOH J 6 . ? 26.071 -30.879 11.252 1.00 33.43 ? 474 HOH A O 1 HETATM 1827 O O . HOH J 6 . ? -3.447 -50.176 -1.653 1.00 30.20 ? 475 HOH A O 1 HETATM 1828 O O . HOH J 6 . ? 15.601 -38.951 -20.652 1.00 27.71 ? 476 HOH A O 1 HETATM 1829 O O . HOH J 6 . ? 1.234 -27.904 10.047 1.00 35.29 ? 477 HOH A O 1 HETATM 1830 O O . HOH J 6 . ? 7.589 -41.677 -26.001 1.00 28.72 ? 478 HOH A O 1 HETATM 1831 O O . HOH J 6 . ? 14.879 -28.401 15.085 1.00 31.52 ? 479 HOH A O 1 HETATM 1832 O O . HOH J 6 . ? 8.018 -16.481 7.454 1.00 30.27 ? 480 HOH A O 1 HETATM 1833 O O . HOH J 6 . ? -6.910 -35.742 -0.264 1.00 24.83 ? 481 HOH A O 1 HETATM 1834 O O . HOH J 6 . ? 22.634 -41.167 -14.709 1.00 30.58 ? 482 HOH A O 1 HETATM 1835 O O . HOH J 6 . ? -4.305 -42.919 -15.280 1.00 34.65 ? 483 HOH A O 1 HETATM 1836 O O . HOH J 6 . ? -1.957 -22.518 7.023 1.00 39.43 ? 484 HOH A O 1 HETATM 1837 O O . HOH J 6 . ? 24.793 -33.919 6.933 1.00 27.09 ? 485 HOH A O 1 HETATM 1838 O O . HOH J 6 . ? 23.264 -25.882 0.740 1.00 26.68 ? 486 HOH A O 1 HETATM 1839 O O . HOH J 6 . ? -7.351 -50.043 -10.124 1.00 28.24 ? 487 HOH A O 1 HETATM 1840 O O . HOH J 6 . ? -5.115 -52.191 -4.748 1.00 26.35 ? 488 HOH A O 1 HETATM 1841 O O . HOH J 6 . ? 8.040 -51.042 -1.055 1.00 33.93 ? 489 HOH A O 1 HETATM 1842 O O . HOH J 6 . ? 7.741 -36.493 7.907 1.00 24.41 ? 490 HOH A O 1 HETATM 1843 O O . HOH J 6 . ? 8.415 -43.417 -15.869 1.00 28.68 ? 491 HOH A O 1 HETATM 1844 O O . HOH J 6 . ? 9.932 -36.583 2.238 1.00 25.85 ? 492 HOH A O 1 HETATM 1845 O O . HOH J 6 . ? 17.233 -33.028 19.668 1.00 52.84 ? 493 HOH A O 1 HETATM 1846 O O . HOH J 6 . ? 12.554 -50.198 -2.201 1.00 39.33 ? 494 HOH A O 1 HETATM 1847 O O . HOH J 6 . ? 8.128 -23.721 -22.541 1.00 32.31 ? 495 HOH A O 1 HETATM 1848 O O . HOH J 6 . ? -2.923 -33.907 4.390 1.00 31.26 ? 496 HOH A O 1 HETATM 1849 O O . HOH J 6 . ? 8.213 -54.262 -4.886 1.00 29.30 ? 497 HOH A O 1 HETATM 1850 O O . HOH J 6 . ? 14.921 -13.082 -0.370 1.00 38.12 ? 498 HOH A O 1 HETATM 1851 O O . HOH J 6 . ? 17.583 -22.790 -3.319 1.00 37.68 ? 499 HOH A O 1 HETATM 1852 O O . HOH J 6 . ? 4.782 -51.395 -17.860 1.00 40.69 ? 500 HOH A O 1 HETATM 1853 O O . HOH J 6 . ? 26.403 -39.429 -6.587 1.00 37.98 ? 501 HOH A O 1 HETATM 1854 O O . HOH J 6 . ? -5.516 -28.009 1.099 1.00 31.01 ? 502 HOH A O 1 HETATM 1855 O O . HOH J 6 . ? 24.030 -36.162 -14.174 1.00 30.57 ? 503 HOH A O 1 HETATM 1856 O O . HOH J 6 . ? 17.415 -37.576 -17.500 1.00 19.93 ? 504 HOH A O 1 HETATM 1857 O O . HOH J 6 . ? 17.830 -40.958 11.521 1.00 31.64 ? 505 HOH A O 1 HETATM 1858 O O . HOH J 6 . ? 12.559 -26.535 -19.130 1.00 30.44 ? 506 HOH A O 1 HETATM 1859 O O . HOH J 6 . ? 6.434 -47.989 4.192 1.00 41.75 ? 507 HOH A O 1 HETATM 1860 O O . HOH J 6 . ? 12.859 -24.765 -17.016 1.00 44.66 ? 508 HOH A O 1 HETATM 1861 O O . HOH J 6 . ? 15.696 -34.879 17.712 1.00 44.65 ? 509 HOH A O 1 HETATM 1862 O O . HOH J 6 . ? 26.891 -33.558 11.931 1.00 41.18 ? 510 HOH A O 1 HETATM 1863 O O . HOH J 6 . ? 25.978 -39.389 -0.637 1.00 36.71 ? 511 HOH A O 1 HETATM 1864 O O . HOH J 6 . ? 12.495 -39.367 -30.025 1.00 34.81 ? 512 HOH A O 1 HETATM 1865 O O . HOH J 6 . ? 21.627 -20.407 -0.870 1.00 37.63 ? 513 HOH A O 1 HETATM 1866 O O . HOH J 6 . ? 16.507 -41.793 -17.078 1.00 23.96 ? 514 HOH A O 1 HETATM 1867 O O . HOH J 6 . ? 6.767 -53.304 -1.908 1.00 37.28 ? 515 HOH A O 1 HETATM 1868 O O . HOH J 6 . ? 21.956 -22.295 6.015 1.00 36.68 ? 516 HOH A O 1 HETATM 1869 O O . HOH J 6 . ? 0.000 -28.070 -24.843 0.50 30.21 ? 517 HOH A O 1 HETATM 1870 O O . HOH J 6 . ? 1.252 -45.294 8.887 1.00 44.50 ? 518 HOH A O 1 HETATM 1871 O O . HOH J 6 . ? 0.690 -18.794 -15.380 1.00 42.89 ? 519 HOH A O 1 HETATM 1872 O O . HOH J 6 . ? -5.530 -49.545 -12.127 1.00 32.69 ? 520 HOH A O 1 HETATM 1873 O O . HOH J 6 . ? 24.807 -41.447 1.220 1.00 28.70 ? 521 HOH A O 1 HETATM 1874 O O . HOH J 6 . ? 0.000 -39.110 -24.843 0.50 22.15 ? 522 HOH A O 1 HETATM 1875 O O . HOH J 6 . ? -5.312 -42.588 -12.855 1.00 35.98 ? 523 HOH A O 1 HETATM 1876 O O . HOH J 6 . ? 1.743 -19.888 -19.669 1.00 45.78 ? 524 HOH A O 1 HETATM 1877 O O . HOH J 6 . ? 22.707 -47.708 -2.221 1.00 31.30 ? 525 HOH A O 1 HETATM 1878 O O . HOH J 6 . ? -4.570 -24.870 -12.802 1.00 39.72 ? 526 HOH A O 1 HETATM 1879 O O . HOH J 6 . ? -4.356 -25.372 4.038 1.00 44.64 ? 527 HOH A O 1 HETATM 1880 O O . HOH J 6 . ? 26.492 -38.873 -3.880 1.00 42.71 ? 528 HOH A O 1 HETATM 1881 O O . HOH J 6 . ? -0.590 -29.629 8.733 1.00 39.59 ? 529 HOH A O 1 HETATM 1882 O O . HOH J 6 . ? 11.878 -22.816 -19.592 1.00 28.04 ? 530 HOH A O 1 HETATM 1883 O O . HOH J 6 . ? 7.553 -21.281 12.012 1.00 37.18 ? 531 HOH A O 1 HETATM 1884 O O . HOH J 6 . ? 11.925 -46.092 7.253 1.00 34.86 ? 532 HOH A O 1 HETATM 1885 O O . HOH J 6 . ? 2.405 -37.568 -25.012 1.00 30.54 ? 533 HOH A O 1 HETATM 1886 O O . HOH J 6 . ? 19.855 -43.812 -15.573 1.00 48.78 ? 534 HOH A O 1 HETATM 1887 O O . HOH J 6 . ? 2.000 -36.754 12.875 1.00 42.18 ? 535 HOH A O 1 HETATM 1888 O O . HOH J 6 . ? -7.849 -36.096 -21.513 1.00 21.62 ? 536 HOH A O 1 HETATM 1889 O O . HOH J 6 . ? 17.437 -40.899 -19.492 1.00 35.41 ? 537 HOH A O 1 HETATM 1890 O O . HOH J 6 . ? -4.313 -23.481 6.218 1.00 45.29 ? 538 HOH A O 1 HETATM 1891 O O . HOH J 6 . ? -9.364 -34.304 -0.375 1.00 46.24 ? 539 HOH A O 1 HETATM 1892 O O . HOH J 6 . ? 24.123 -41.846 4.282 1.00 42.01 ? 540 HOH A O 1 HETATM 1893 O O . HOH J 6 . ? -7.123 -52.755 -9.968 1.00 36.07 ? 541 HOH A O 1 HETATM 1894 O O . HOH J 6 . ? 12.802 -49.786 -13.176 1.00 36.84 ? 542 HOH A O 1 HETATM 1895 O O . HOH J 6 . ? -9.091 -32.573 -20.026 1.00 34.34 ? 543 HOH A O 1 HETATM 1896 O O . HOH J 6 . ? 10.644 -34.387 15.763 1.00 35.02 ? 544 HOH A O 1 HETATM 1897 O O . HOH J 6 . ? 8.475 -51.193 -14.552 1.00 36.99 ? 545 HOH A O 1 HETATM 1898 O O . HOH J 6 . ? 1.989 -26.286 -25.343 1.00 33.43 ? 546 HOH A O 1 HETATM 1899 O O . HOH J 6 . ? 25.293 -39.478 16.938 1.00 49.31 ? 547 HOH A O 1 HETATM 1900 O O . HOH J 6 . ? 3.600 -52.738 -8.013 1.00 24.92 ? 548 HOH A O 1 HETATM 1901 O O . HOH J 6 . ? -3.246 -36.728 -20.331 1.00 24.37 ? 549 HOH A O 1 HETATM 1902 O O . HOH J 6 . ? 24.070 -39.162 -12.557 1.00 37.11 ? 550 HOH A O 1 HETATM 1903 O O . HOH J 6 . ? 27.181 -32.633 6.893 1.00 43.36 ? 551 HOH A O 1 HETATM 1904 O O . HOH J 6 . ? 0.123 -19.564 3.926 1.00 37.23 ? 552 HOH A O 1 HETATM 1905 O O . HOH J 6 . ? -8.968 -47.423 -6.836 1.00 46.00 ? 553 HOH A O 1 HETATM 1906 O O . HOH J 6 . ? 12.034 -40.084 15.177 1.00 33.78 ? 554 HOH A O 1 HETATM 1907 O O . HOH J 6 . ? -3.929 -38.325 -22.585 1.00 35.60 ? 555 HOH A O 1 HETATM 1908 O O . HOH J 6 . ? 4.108 -52.720 -13.769 1.00 33.67 ? 556 HOH A O 1 HETATM 1909 O O . HOH J 6 . ? 4.825 -16.642 10.559 1.00 39.71 ? 557 HOH A O 1 HETATM 1910 O O . HOH J 6 . ? 6.746 -20.711 -10.690 1.00 35.88 ? 558 HOH A O 1 HETATM 1911 O O . HOH J 6 . ? 10.744 -12.869 -5.664 1.00 32.37 ? 559 HOH A O 1 HETATM 1912 O O . HOH J 6 . ? 3.114 -21.625 -21.217 1.00 43.04 ? 560 HOH A O 1 HETATM 1913 O O . HOH J 6 . ? -1.262 -29.695 5.902 1.00 41.63 ? 561 HOH A O 1 HETATM 1914 O O . HOH J 6 . ? 17.356 -42.758 4.985 1.00 34.01 ? 562 HOH A O 1 HETATM 1915 O O . HOH J 6 . ? 1.463 -50.143 -14.313 1.00 25.60 ? 563 HOH A O 1 HETATM 1916 O O . HOH J 6 . ? 24.670 -21.111 16.528 1.00 39.39 ? 564 HOH A O 1 HETATM 1917 O O . HOH J 6 . ? -7.025 -44.553 -2.158 1.00 27.43 ? 565 HOH A O 1 HETATM 1918 O O . HOH J 6 . ? 17.445 -44.177 -16.721 1.00 37.02 ? 566 HOH A O 1 HETATM 1919 O O . HOH J 6 . ? 16.624 -12.366 5.117 1.00 41.84 ? 567 HOH A O 1 HETATM 1920 O O . HOH J 6 . ? -0.547 -19.579 6.494 1.00 46.30 ? 568 HOH A O 1 HETATM 1921 O O . HOH J 6 . ? 2.182 -45.061 -19.033 1.00 50.41 ? 569 HOH A O 1 HETATM 1922 O O . HOH J 6 . ? 27.306 -42.222 1.882 1.00 33.28 ? 570 HOH A O 1 HETATM 1923 O O . HOH J 6 . ? 10.011 -14.011 11.301 1.00 46.53 ? 571 HOH A O 1 HETATM 1924 O O . HOH J 6 . ? 21.567 -24.548 -4.811 1.00 45.19 ? 572 HOH A O 1 HETATM 1925 O O . HOH J 6 . ? 0.276 -53.001 -7.087 1.00 38.53 ? 573 HOH A O 1 HETATM 1926 O O . HOH J 6 . ? 5.201 -28.725 -27.401 1.00 49.09 ? 574 HOH A O 1 HETATM 1927 O O . HOH J 6 . ? 14.259 -13.803 8.584 1.00 22.63 ? 575 HOH A O 1 HETATM 1928 O O . HOH J 6 . ? 24.194 -19.005 18.328 1.00 44.05 ? 576 HOH A O 1 HETATM 1929 O O . HOH J 6 . ? 15.018 -39.702 -23.423 1.00 25.02 ? 577 HOH A O 1 HETATM 1930 O O . HOH J 6 . ? 6.178 -54.812 -6.170 1.00 39.06 ? 578 HOH A O 1 HETATM 1931 O O . HOH J 6 . ? 17.218 -13.158 8.694 1.00 21.86 ? 579 HOH A O 1 HETATM 1932 O O . HOH J 6 . ? 25.394 -36.257 8.260 1.00 30.51 ? 580 HOH A O 1 HETATM 1933 O O . HOH J 6 . ? 17.860 -37.756 -22.130 1.00 41.00 ? 581 HOH A O 1 HETATM 1934 O O . HOH J 6 . ? 11.547 -33.497 -7.605 1.00 27.87 ? 582 HOH A O 1 HETATM 1935 O O . HOH J 6 . ? 4.719 -21.223 -23.609 1.00 33.26 ? 583 HOH A O 1 HETATM 1936 O O . HOH J 6 . ? -7.645 -41.059 -7.948 1.00 35.23 ? 584 HOH A O 1 HETATM 1937 O O . HOH J 6 . ? 26.798 -28.706 12.581 1.00 32.37 ? 585 HOH A O 1 HETATM 1938 O O . HOH J 6 . ? 1.514 -24.136 -23.653 1.00 41.64 ? 586 HOH A O 1 HETATM 1939 O O . HOH J 6 . ? 5.133 -19.988 11.022 1.00 42.47 ? 587 HOH A O 1 HETATM 1940 O O . HOH J 6 . ? -4.407 -37.218 6.644 1.00 43.00 ? 588 HOH A O 1 HETATM 1941 O O . HOH J 6 . ? 2.318 -47.261 7.988 1.00 56.62 ? 589 HOH A O 1 HETATM 1942 O O . HOH J 6 . ? 12.548 -12.375 -2.565 1.00 31.14 ? 590 HOH A O 1 HETATM 1943 O O . HOH J 6 . ? 9.641 -29.559 15.781 1.00 44.73 ? 591 HOH A O 1 HETATM 1944 O O . HOH J 6 . ? 12.367 -51.980 -5.016 1.00 44.42 ? 592 HOH A O 1 HETATM 1945 O O . HOH J 6 . ? 21.755 -32.081 17.037 1.00 44.77 ? 593 HOH A O 1 HETATM 1946 O O . HOH J 6 . ? 14.423 -48.146 -26.009 1.00 39.57 ? 594 HOH A O 1 HETATM 1947 O O . HOH J 6 . ? 24.006 -38.668 7.314 1.00 38.44 ? 595 HOH A O 1 HETATM 1948 O O . HOH J 6 . ? -1.836 -19.184 2.026 1.00 47.82 ? 596 HOH A O 1 HETATM 1949 O O . HOH J 6 . ? 12.179 -44.332 12.077 1.00 39.18 ? 597 HOH A O 1 HETATM 1950 O O . HOH J 6 . ? 23.676 -28.581 15.020 1.00 38.60 ? 598 HOH A O 1 HETATM 1951 O O . HOH J 6 . ? -8.011 -42.243 -12.362 1.00 34.35 ? 599 HOH A O 1 HETATM 1952 O O . HOH J 6 . ? 13.563 -38.740 -32.695 1.00 36.30 ? 600 HOH A O 1 HETATM 1953 O O . HOH J 6 . ? -1.316 -40.815 8.176 1.00 35.16 ? 601 HOH A O 1 HETATM 1954 O O . HOH J 6 . ? 17.015 -41.027 -24.193 1.00 39.24 ? 602 HOH A O 1 HETATM 1955 O O . HOH J 6 . ? 20.481 -27.456 15.993 1.00 62.51 ? 603 HOH A O 1 HETATM 1956 O O . HOH J 6 . ? -2.415 -24.704 -19.662 1.00 48.60 ? 604 HOH A O 1 HETATM 1957 O O . HOH J 6 . ? 4.387 -54.244 -3.162 1.00 38.10 ? 605 HOH A O 1 HETATM 1958 O O . HOH J 6 . ? -6.988 -37.669 7.683 1.00 51.57 ? 606 HOH A O 1 HETATM 1959 O O . HOH J 6 . ? 17.268 -22.134 -9.288 1.00 43.34 ? 607 HOH A O 1 HETATM 1960 O O . HOH J 6 . ? 3.884 -52.514 2.945 1.00 44.60 ? 608 HOH A O 1 HETATM 1961 O O . HOH J 6 . ? 8.167 -19.170 0.327 1.00 36.62 ? 609 HOH A O 1 HETATM 1962 O O . HOH J 6 . ? 14.379 -32.309 16.661 1.00 42.60 ? 610 HOH A O 1 HETATM 1963 O O . HOH J 6 . ? 1.895 -15.414 -0.076 1.00 48.41 ? 611 HOH A O 1 HETATM 1964 O O . HOH J 6 . ? 8.903 -31.633 15.723 1.00 64.90 ? 612 HOH A O 1 HETATM 1965 O O . HOH J 6 . ? 24.629 -38.241 12.062 1.00 38.24 ? 613 HOH A O 1 HETATM 1966 O O . HOH J 6 . ? 19.938 -48.892 1.099 1.00 33.68 ? 614 HOH A O 1 HETATM 1967 O O . HOH J 6 . ? 16.665 -10.049 9.237 1.00 39.78 ? 615 HOH A O 1 HETATM 1968 O O . HOH J 6 . ? 21.521 -26.920 -13.281 1.00 25.65 ? 616 HOH A O 1 HETATM 1969 O O . HOH J 6 . ? -6.837 -48.872 -7.574 1.00 27.96 ? 617 HOH A O 1 HETATM 1970 O O . HOH J 6 . ? 14.860 -40.667 14.944 1.00 30.10 ? 618 HOH A O 1 HETATM 1971 O O . HOH J 6 . ? 22.272 -23.836 14.135 1.00 44.39 ? 619 HOH A O 1 HETATM 1972 O O . HOH J 6 . ? 19.845 -48.504 -1.653 1.00 46.28 ? 620 HOH A O 1 HETATM 1973 O O . HOH J 6 . ? -9.568 -40.225 -4.223 1.00 41.97 ? 621 HOH A O 1 HETATM 1974 O O . HOH J 6 . ? 26.062 -35.235 1.602 1.00 40.85 ? 622 HOH A O 1 HETATM 1975 O O . HOH J 6 . ? 18.309 -17.765 -5.833 1.00 40.32 ? 623 HOH A O 1 HETATM 1976 O O . HOH J 6 . ? 15.724 -46.749 -28.810 1.00 45.28 ? 624 HOH A O 1 HETATM 1977 O O . HOH J 6 . ? -8.640 -42.740 -9.731 1.00 46.08 ? 625 HOH A O 1 HETATM 1978 O O . HOH J 6 . ? -8.793 -39.677 -6.231 1.00 42.10 ? 626 HOH A O 1 HETATM 1979 O O . HOH J 6 . ? -7.588 -41.415 -19.525 1.00 37.14 ? 627 HOH A O 1 HETATM 1980 O O . HOH J 6 . ? 16.719 -24.565 14.729 1.00 49.51 ? 628 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 . ARG A 3 ? 0.6319 0.7034 0.3526 0.0181 0.0684 -0.1493 24 ARG A N 2 C CA . ARG A 3 ? 0.5798 0.6524 0.3044 -0.0036 0.0457 -0.1303 24 ARG A CA 3 C C . ARG A 3 ? 0.5175 0.5675 0.2560 -0.0120 0.0192 -0.1359 24 ARG A C 4 O O . ARG A 3 ? 0.4280 0.4973 0.2052 -0.0202 0.0117 -0.1217 24 ARG A O 5 C CB . ARG A 3 ? 0.6455 0.6999 0.3213 -0.0095 0.0396 -0.1255 24 ARG A CB 6 C CG . ARG A 3 ? 0.6875 0.7679 0.3573 -0.0094 0.0616 -0.1092 24 ARG A CG 7 C CD . ARG A 3 ? 0.7405 0.8011 0.3616 -0.0138 0.0529 -0.1026 24 ARG A CD 8 N NE . ARG A 3 ? 0.8190 0.8430 0.3850 -0.0035 0.0497 -0.1254 24 ARG A NE 9 C CZ . ARG A 3 ? 0.9412 0.9563 0.4624 0.0071 0.0710 -0.1321 24 ARG A CZ 10 N NH1 . ARG A 3 ? 0.9494 0.9963 0.4818 0.0069 0.0968 -0.1160 24 ARG A NH1 11 N NH2 . ARG A 3 ? 1.0339 1.0053 0.4965 0.0168 0.0665 -0.1546 24 ARG A NH2 12 N N . THR A 4 ? 0.5271 0.5328 0.2327 -0.0114 0.0048 -0.1559 25 THR A N 13 C CA . THR A 4 ? 0.5085 0.4928 0.2320 -0.0238 -0.0216 -0.1587 25 THR A CA 14 C C . THR A 4 ? 0.4781 0.4683 0.2444 -0.0157 -0.0154 -0.1646 25 THR A C 15 O O . THR A 4 ? 0.4619 0.4534 0.2609 -0.0281 -0.0322 -0.1546 25 THR A O 16 C CB . THR A 4 ? 0.7321 0.6627 0.4125 -0.0287 -0.0434 -0.1779 25 THR A CB 17 O OG1 . THR A 4 ? 0.8255 0.7184 0.4652 -0.0132 -0.0237 -0.2019 25 THR A OG1 18 C CG2 . THR A 4 ? 0.7255 0.6652 0.3813 -0.0352 -0.0602 -0.1698 25 THR A CG2 19 N N . ASP A 5 ? 0.4833 0.4790 0.2533 0.0082 0.0088 -0.1773 26 ASP A N 20 C CA . ASP A 5 ? 0.4691 0.4722 0.2869 0.0236 0.0154 -0.1743 26 ASP A CA 21 C C . ASP A 5 ? 0.4165 0.4582 0.2835 0.0127 0.0120 -0.1440 26 ASP A C 22 O O . ASP A 5 ? 0.3752 0.4139 0.2799 0.0190 0.0088 -0.1354 26 ASP A O 23 C CB . ASP A 5 ? 0.5321 0.5519 0.3506 0.0547 0.0441 -0.1872 26 ASP A CB 24 C CG . ASP A 5 ? 0.6789 0.6397 0.4544 0.0708 0.0476 -0.2122 26 ASP A CG 25 O OD1 . ASP A 5 ? 0.7387 0.6437 0.4919 0.0571 0.0248 -0.2228 26 ASP A OD1 26 O OD2 . ASP A 5 ? 0.7312 0.7003 0.4965 0.0930 0.0731 -0.2184 26 ASP A OD2 27 N N . LEU A 6 ? 0.4130 0.4846 0.2733 -0.0028 0.0122 -0.1279 27 LEU A N 28 C CA . LEU A 6 ? 0.3469 0.4452 0.2420 -0.0126 0.0093 -0.1012 27 LEU A CA 29 C C . LEU A 6 ? 0.2953 0.3785 0.1988 -0.0281 -0.0134 -0.0874 27 LEU A C 30 O O . LEU A 6 ? 0.2510 0.3457 0.1804 -0.0320 -0.0163 -0.0676 27 LEU A O 31 C CB . LEU A 6 ? 0.3535 0.4852 0.2347 -0.0200 0.0231 -0.0893 27 LEU A CB 32 C CG . LEU A 6 ? 0.3801 0.5438 0.2618 -0.0081 0.0491 -0.0964 27 LEU A CG 33 C CD1 . LEU A 6 ? 0.3954 0.5737 0.2637 -0.0209 0.0574 -0.0776 27 LEU A CD1 34 C CD2 . LEU A 6 ? 0.3451 0.5325 0.2769 0.0024 0.0551 -0.0898 27 LEU A CD2 35 N N . LEU A 7 ? 0.3443 0.4035 0.2251 -0.0368 -0.0294 -0.0976 28 LEU A N 36 C CA . LEU A 7 ? 0.2779 0.3352 0.1728 -0.0518 -0.0503 -0.0825 28 LEU A CA 37 C C . LEU A 7 ? 0.2832 0.3206 0.2107 -0.0528 -0.0587 -0.0804 28 LEU A C 38 O O . LEU A 7 ? 0.3058 0.3124 0.2281 -0.0463 -0.0576 -0.0981 28 LEU A O 39 C CB . LEU A 7 ? 0.3314 0.3764 0.1937 -0.0630 -0.0668 -0.0901 28 LEU A CB 40 C CG . LEU A 7 ? 0.3568 0.4104 0.1861 -0.0566 -0.0554 -0.0879 28 LEU A CG 41 C CD1 . LEU A 7 ? 0.3916 0.4311 0.1934 -0.0618 -0.0724 -0.0911 28 LEU A CD1 42 C CD2 . LEU A 7 ? 0.2964 0.3761 0.1421 -0.0547 -0.0459 -0.0623 28 LEU A CD2 43 N N . ASN A 8 ? 0.2431 0.2948 0.2001 -0.0592 -0.0655 -0.0580 29 ASN A N 44 C CA . ASN A 8 ? 0.2617 0.2970 0.2466 -0.0652 -0.0746 -0.0514 29 ASN A CA 45 C C . ASN A 8 ? 0.2874 0.2982 0.2829 -0.0507 -0.0646 -0.0592 29 ASN A C 46 O O . ASN A 8 ? 0.3178 0.2912 0.3092 -0.0528 -0.0713 -0.0713 29 ASN A O 47 C CB . ASN A 8 ? 0.2772 0.2938 0.2524 -0.0856 -0.0956 -0.0602 29 ASN A CB 48 C CG . ASN A 8 ? 0.3284 0.3469 0.3395 -0.0991 -0.1052 -0.0414 29 ASN A CG 49 O OD1 . ASN A 8 ? 0.3055 0.3552 0.3429 -0.0942 -0.0982 -0.0176 29 ASN A OD1 50 N ND2 . ASN A 8 ? 0.3256 0.3079 0.3337 -0.1115 -0.1147 -0.0518 29 ASN A ND2 51 N N . VAL A 9 ? 0.2740 0.3036 0.2813 -0.0365 -0.0506 -0.0512 30 VAL A N 52 C CA . VAL A 9 ? 0.2831 0.3002 0.3059 -0.0204 -0.0432 -0.0534 30 VAL A CA 53 C C . VAL A 9 ? 0.2623 0.2966 0.3079 -0.0179 -0.0407 -0.0308 30 VAL A C 54 O O . VAL A 9 ? 0.2462 0.3008 0.2908 -0.0250 -0.0404 -0.0170 30 VAL A O 55 C CB . VAL A 9 ? 0.2886 0.3182 0.3022 -0.0032 -0.0284 -0.0687 30 VAL A CB 56 C CG1 . VAL A 9 ? 0.3041 0.3105 0.2850 -0.0010 -0.0277 -0.0939 30 VAL A CG1 57 C CG2 . VAL A 9 ? 0.2852 0.3549 0.2982 -0.0068 -0.0195 -0.0583 30 VAL A CG2 58 N N . CYS A 10 ? 0.2614 0.2824 0.3223 -0.0060 -0.0396 -0.0275 31 CYS A N 59 C CA . CYS A 10 ? 0.2203 0.2536 0.2955 -0.0018 -0.0382 -0.0087 31 CYS A CA 60 C C . CYS A 10 ? 0.2135 0.2647 0.2971 0.0144 -0.0316 -0.0139 31 CYS A C 61 O O . CYS A 10 ? 0.2320 0.2734 0.3197 0.0294 -0.0290 -0.0268 31 CYS A O 62 C CB . CYS A 10 ? 0.2107 0.2160 0.2963 -0.0021 -0.0447 0.0034 31 CYS A CB 63 S SG . CYS A 10 ? 0.2597 0.2574 0.3469 -0.0239 -0.0519 0.0144 31 CYS A SG 64 N N . MET A 11 ? 0.1791 0.2565 0.2654 0.0121 -0.0295 -0.0035 32 MET A N 65 C CA . MET A 11 ? 0.1727 0.2778 0.2741 0.0235 -0.0259 -0.0057 32 MET A CA 66 C C . MET A 11 ? 0.1645 0.2589 0.2820 0.0388 -0.0330 0.0026 32 MET A C 67 O O . MET A 11 ? 0.2177 0.2831 0.3305 0.0371 -0.0396 0.0135 32 MET A O 68 C CB . MET A 11 ? 0.2157 0.3499 0.3125 0.0105 -0.0244 0.0023 32 MET A CB 69 C CG . MET A 11 ? 0.2322 0.3524 0.3168 0.0018 -0.0321 0.0185 32 MET A CG 70 S SD . MET A 11 ? 0.4021 0.5489 0.4795 -0.0137 -0.0339 0.0247 32 MET A SD 71 C CE . MET A 11 ? 0.2707 0.3838 0.3236 -0.0161 -0.0436 0.0394 32 MET A CE 72 N N . ASP A 12 ? 0.1462 0.2675 0.2835 0.0549 -0.0309 -0.0010 33 ASP A N 73 C CA . ASP A 12 ? 0.1872 0.3031 0.3405 0.0739 -0.0390 0.0079 33 ASP A CA 74 C C . ASP A 12 ? 0.1724 0.3118 0.3276 0.0633 -0.0489 0.0245 33 ASP A C 75 O O . ASP A 12 ? 0.1551 0.3338 0.3233 0.0600 -0.0494 0.0239 33 ASP A O 76 C CB . ASP A 12 ? 0.1737 0.3170 0.3503 0.1001 -0.0316 -0.0030 33 ASP A CB 77 C CG . ASP A 12 ? 0.2180 0.3523 0.4098 0.1246 -0.0395 0.0075 33 ASP A CG 78 O OD1 . ASP A 12 ? 0.2377 0.3545 0.4190 0.1174 -0.0504 0.0251 33 ASP A OD1 79 O OD2 . ASP A 12 ? 0.2156 0.3561 0.4202 0.1476 -0.0308 0.0005 33 ASP A OD2 80 N N . ALA A 13 ? 0.1842 0.2924 0.3198 0.0543 -0.0557 0.0371 34 ALA A N 81 C CA . ALA A 13 ? 0.2067 0.3155 0.3208 0.0434 -0.0617 0.0455 34 ALA A CA 82 C C . ALA A 13 ? 0.2362 0.3080 0.3305 0.0486 -0.0651 0.0566 34 ALA A C 83 O O . ALA A 13 ? 0.2522 0.2983 0.3499 0.0572 -0.0629 0.0589 34 ALA A O 84 C CB . ALA A 13 ? 0.1104 0.2201 0.2034 0.0219 -0.0582 0.0458 34 ALA A CB 85 N N . LYS A 14 ? 0.2702 0.3365 0.3416 0.0421 -0.0699 0.0630 35 LYS A N 86 C CA . LYS A 14 ? 0.2856 0.3273 0.3387 0.0503 -0.0732 0.0721 35 LYS A CA 87 C C . LYS A 14 ? 0.3019 0.3094 0.3445 0.0508 -0.0642 0.0780 35 LYS A C 88 O O . LYS A 14 ? 0.2865 0.2756 0.3286 0.0619 -0.0659 0.0838 35 LYS A O 89 C CB . LYS A 14 ? 0.2717 0.3085 0.2951 0.0420 -0.0777 0.0758 35 LYS A CB 90 C CG . LYS A 14 ? 0.2908 0.3057 0.2916 0.0525 -0.0811 0.0848 35 LYS A CG 91 C CD . LYS A 14 ? 0.2902 0.3039 0.2618 0.0473 -0.0881 0.0869 35 LYS A CD 92 C CE . LYS A 14 ? 0.3407 0.3340 0.2859 0.0595 -0.0897 0.0969 35 LYS A CE 93 N NZ . LYS A 14 ? 0.3628 0.3554 0.2764 0.0550 -0.0948 0.0995 35 LYS A NZ 94 N N . HIS A 15 ? 0.2426 0.2434 0.2772 0.0384 -0.0549 0.0773 36 HIS A N 95 C CA . HIS A 15 ? 0.2753 0.2543 0.3030 0.0343 -0.0464 0.0839 36 HIS A CA 96 C C . HIS A 15 ? 0.2671 0.2464 0.3179 0.0274 -0.0436 0.0825 36 HIS A C 97 O O . HIS A 15 ? 0.2559 0.2210 0.3098 0.0212 -0.0397 0.0898 36 HIS A O 98 C CB . HIS A 15 ? 0.2733 0.2459 0.2732 0.0289 -0.0382 0.0857 36 HIS A CB 99 C CG . HIS A 15 ? 0.2943 0.2550 0.2646 0.0356 -0.0428 0.0874 36 HIS A CG 100 N ND1 . HIS A 15 ? 0.3213 0.2631 0.2774 0.0428 -0.0453 0.0960 36 HIS A ND1 101 C CD2 . HIS A 15 ? 0.2713 0.2334 0.2202 0.0361 -0.0463 0.0831 36 HIS A CD2 102 C CE1 . HIS A 15 ? 0.3306 0.2644 0.2576 0.0486 -0.0507 0.0965 36 HIS A CE1 103 N NE2 . HIS A 15 ? 0.3085 0.2556 0.2318 0.0446 -0.0507 0.0888 36 HIS A NE2 104 N N . HIS A 16 ? 0.2460 0.2420 0.3138 0.0276 -0.0474 0.0737 37 HIS A N 105 C CA . HIS A 16 ? 0.2266 0.2201 0.3131 0.0214 -0.0485 0.0709 37 HIS A CA 106 C C . HIS A 16 ? 0.2077 0.1691 0.3046 0.0232 -0.0522 0.0707 37 HIS A C 107 O O . HIS A 16 ? 0.2075 0.1536 0.3076 0.0382 -0.0564 0.0681 37 HIS A O 108 C CB . HIS A 16 ? 0.2209 0.2382 0.3136 0.0221 -0.0475 0.0522 37 HIS A CB 109 C CG . HIS A 16 ? 0.1964 0.2349 0.2755 0.0129 -0.0436 0.0527 37 HIS A CG 110 N ND1 . HIS A 16 ? 0.1741 0.2184 0.2380 0.0130 -0.0451 0.0594 37 HIS A ND1 111 C CD2 . HIS A 16 ? 0.2036 0.2509 0.2757 0.0030 -0.0389 0.0471 37 HIS A CD2 112 C CE1 . HIS A 16 ? 0.1777 0.2282 0.2253 0.0041 -0.0410 0.0580 37 HIS A CE1 113 N NE2 . HIS A 16 ? 0.1844 0.2392 0.2380 -0.0005 -0.0371 0.0523 37 HIS A NE2 114 N N . LYS A 17 ? 0.2134 0.1646 0.3130 0.0069 -0.0506 0.0725 38 LYS A N 115 C CA . LYS A 17 ? 0.2711 0.1864 0.3747 0.0010 -0.0558 0.0650 38 LYS A CA 116 C C . LYS A 17 ? 0.2463 0.1573 0.3478 0.0120 -0.0571 0.0384 38 LYS A C 117 O O . LYS A 17 ? 0.2422 0.1867 0.3431 0.0159 -0.0527 0.0272 38 LYS A O 118 C CB . LYS A 17 ? 0.2798 0.1975 0.3894 -0.0244 -0.0569 0.0705 38 LYS A CB 119 C CG . LYS A 17 ? 0.2994 0.2266 0.4134 -0.0339 -0.0512 0.0967 38 LYS A CG 120 C CD . LYS A 17 ? 0.2900 0.2233 0.4157 -0.0584 -0.0536 0.1015 38 LYS A CD 121 C CE . LYS A 17 ? 0.2569 0.2276 0.3928 -0.0680 -0.0553 0.0968 38 LYS A CE 122 N NZ . LYS A 17 ? 0.3034 0.2854 0.4492 -0.0898 -0.0617 0.0974 38 LYS A NZ 123 N N . THR A 18 ? 0.2815 0.1473 0.3778 0.0174 -0.0617 0.0288 39 THR A N 124 C CA . THR A 18 ? 0.3300 0.1844 0.4179 0.0316 -0.0601 0.0022 39 THR A CA 125 C C . THR A 18 ? 0.3370 0.2054 0.4147 0.0143 -0.0598 -0.0151 39 THR A C 126 O O . THR A 18 ? 0.3385 0.2257 0.4093 0.0259 -0.0531 -0.0335 39 THR A O 127 C CB . THR A 18 ? 0.4603 0.2469 0.5348 0.0407 -0.0656 -0.0052 39 THR A CB 128 O OG1 . THR A 18 ? 0.5041 0.2739 0.5849 0.0581 -0.0675 0.0139 39 THR A OG1 129 C CG2 . THR A 18 ? 0.5151 0.2897 0.5763 0.0641 -0.0600 -0.0337 39 THR A CG2 130 N N . LYS A 19 ? 0.3375 0.2008 0.4152 -0.0132 -0.0670 -0.0072 40 LYS A N 131 C CA . LYS A 19 ? 0.3603 0.2334 0.4270 -0.0322 -0.0721 -0.0209 40 LYS A CA 132 C C . LYS A 19 ? 0.3114 0.2175 0.3946 -0.0557 -0.0762 0.0005 40 LYS A C 133 O O . LYS A 19 ? 0.2965 0.1996 0.3951 -0.0622 -0.0761 0.0225 40 LYS A O 134 C CB . LYS A 19 ? 0.3661 0.1798 0.4102 -0.0422 -0.0831 -0.0404 40 LYS A CB 135 N N . PRO A 20 ? 0.2890 0.2279 0.3684 -0.0661 -0.0788 -0.0043 41 PRO A N 136 C CA . PRO A 20 ? 0.2599 0.2371 0.3582 -0.0821 -0.0816 0.0173 41 PRO A CA 137 C C . PRO A 20 ? 0.2987 0.2606 0.4077 -0.1076 -0.0936 0.0249 41 PRO A C 138 O O . PRO A 20 ? 0.3317 0.2533 0.4233 -0.1173 -0.1033 0.0070 41 PRO A O 139 C CB . PRO A 20 ? 0.2502 0.2573 0.3352 -0.0838 -0.0841 0.0070 41 PRO A CB 140 C CG . PRO A 20 ? 0.2720 0.2707 0.3358 -0.0634 -0.0740 -0.0119 41 PRO A CG 141 C CD . PRO A 20 ? 0.3221 0.2724 0.3800 -0.0576 -0.0757 -0.0257 41 PRO A CD 142 N N . GLY A 21 ? 0.2917 0.2866 0.4194 -0.1114 -0.0871 0.0491 42 GLY A N 143 C CA . GLY A 21 ? 0.3124 0.3059 0.4492 -0.1310 -0.0927 0.0579 42 GLY A CA 144 C C . GLY A 21 ? 0.3168 0.3587 0.4751 -0.1278 -0.0829 0.0839 42 GLY A C 145 O O . GLY A 21 ? 0.2888 0.3512 0.4486 -0.1084 -0.0706 0.0945 42 GLY A O 146 N N . PRO A 22 ? 0.3449 0.2741 0.4006 -0.1013 -0.0655 -0.0403 43 PRO A N 147 C CA . PRO A 22 ? 0.3290 0.2917 0.4094 -0.1093 -0.0715 -0.0388 43 PRO A CA 148 C C . PRO A 22 ? 0.3249 0.2880 0.4192 -0.1109 -0.0561 -0.0182 43 PRO A C 149 O O . PRO A 22 ? 0.3470 0.2841 0.4418 -0.1116 -0.0409 -0.0096 43 PRO A O 150 C CB . PRO A 22 ? 0.3336 0.3013 0.4369 -0.1264 -0.0772 -0.0602 43 PRO A CB 151 C CG . PRO A 22 ? 0.3965 0.3319 0.4793 -0.1277 -0.0814 -0.0778 43 PRO A CG 152 C CD . PRO A 22 ? 0.3835 0.2874 0.4422 -0.1138 -0.0653 -0.0602 43 PRO A CD 153 N N . GLU A 23 ? 0.2916 0.2811 0.3920 -0.1087 -0.0585 -0.0096 44 GLU A N 154 C CA . GLU A 23 ? 0.3001 0.2904 0.4074 -0.1088 -0.0449 0.0087 44 GLU A CA 155 C C . GLU A 23 ? 0.3082 0.3245 0.4366 -0.1150 -0.0463 0.0083 44 GLU A C 156 O O . GLU A 23 ? 0.2649 0.2989 0.3825 -0.1073 -0.0503 0.0136 44 GLU A O 157 C CB . GLU A 23 ? 0.2686 0.2602 0.3509 -0.0950 -0.0439 0.0230 44 GLU A CB 158 C CG . GLU A 23 ? 0.3087 0.2814 0.3754 -0.0861 -0.0417 0.0264 44 GLU A CG 159 C CD . GLU A 23 ? 0.3604 0.3093 0.4308 -0.0853 -0.0264 0.0376 44 GLU A CD 160 O OE1 . GLU A 23 ? 0.3846 0.3174 0.4442 -0.0759 -0.0219 0.0426 44 GLU A OE1 161 O OE2 . GLU A 23 ? 0.3676 0.3126 0.4511 -0.0920 -0.0159 0.0433 44 GLU A OE2 162 N N . ASP A 24 ? 0.3067 0.3239 0.4613 -0.1254 -0.0379 0.0008 45 ASP A N 163 C CA . ASP A 24 ? 0.3698 0.4144 0.5456 -0.1282 -0.0363 -0.0017 45 ASP A CA 164 C C . ASP A 24 ? 0.3531 0.3999 0.5254 -0.1225 -0.0247 0.0188 45 ASP A C 165 O O . ASP A 24 ? 0.3573 0.4264 0.5419 -0.1209 -0.0240 0.0207 45 ASP A O 166 C CB . ASP A 24 ? 0.4418 0.4855 0.6442 -0.1437 -0.0281 -0.0112 45 ASP A CB 167 C CG . ASP A 24 ? 0.5404 0.6147 0.7697 -0.1473 -0.0259 -0.0104 45 ASP A CG 168 O OD1 . ASP A 24 ? 0.5544 0.6611 0.7907 -0.1453 -0.0422 -0.0214 45 ASP A OD1 169 O OD2 . ASP A 24 ? 0.5954 0.6613 0.8383 -0.1500 -0.0070 0.0026 45 ASP A OD2 170 N N . LYS A 25 ? 0.3166 0.3400 0.4705 -0.1189 -0.0153 0.0352 46 LYS A N 171 C CA . LYS A 25 ? 0.3102 0.3296 0.4519 -0.1127 -0.0017 0.0539 46 LYS A CA 172 C C . LYS A 25 ? 0.2922 0.3142 0.3948 -0.1000 -0.0096 0.0594 46 LYS A C 173 O O . LYS A 25 ? 0.3003 0.3145 0.3818 -0.0932 -0.0005 0.0721 46 LYS A O 174 C CB . LYS A 25 ? 0.3222 0.3122 0.4632 -0.1120 0.0196 0.0679 46 LYS A CB 175 N N . LEU A 26 ? 0.2765 0.3077 0.3690 -0.0972 -0.0252 0.0490 47 LEU A N 176 C CA . LEU A 26 ? 0.2773 0.3128 0.3414 -0.0889 -0.0302 0.0510 47 LEU A CA 177 C C . LEU A 26 ? 0.3035 0.3447 0.3604 -0.0872 -0.0215 0.0574 47 LEU A C 178 O O . LEU A 26 ? 0.2995 0.3532 0.3765 -0.0895 -0.0178 0.0559 47 LEU A O 179 C CB . LEU A 26 ? 0.2046 0.2480 0.2638 -0.0858 -0.0424 0.0393 47 LEU A CB 180 C CG . LEU A 26 ? 0.2267 0.2599 0.2842 -0.0843 -0.0490 0.0335 47 LEU A CG 181 C CD1 . LEU A 26 ? 0.1617 0.1982 0.2064 -0.0773 -0.0562 0.0253 47 LEU A CD1 182 C CD2 . LEU A 26 ? 0.2502 0.2714 0.2974 -0.0806 -0.0448 0.0440 47 LEU A CD2 183 N N . HIS A 27 ? 0.2921 0.3251 0.3205 -0.0825 -0.0184 0.0637 48 HIS A N 184 C CA . HIS A 27 ? 0.3210 0.3500 0.3328 -0.0800 -0.0073 0.0700 48 HIS A CA 185 C C . HIS A 27 ? 0.2886 0.3232 0.2893 -0.0783 -0.0077 0.0632 48 HIS A C 186 O O . HIS A 27 ? 0.2182 0.2547 0.2099 -0.0781 -0.0162 0.0549 48 HIS A O 187 C CB . HIS A 27 ? 0.3381 0.3537 0.3180 -0.0754 -0.0054 0.0775 48 HIS A CB 188 C CG . HIS A 27 ? 0.3688 0.3731 0.3229 -0.0717 0.0073 0.0835 48 HIS A CG 189 N ND1 . HIS A 27 ? 0.3924 0.3926 0.3154 -0.0717 0.0046 0.0767 48 HIS A ND1 190 C CD2 . HIS A 27 ? 0.3867 0.3791 0.3397 -0.0681 0.0254 0.0952 48 HIS A CD2 191 C CE1 . HIS A 27 ? 0.4090 0.3933 0.3081 -0.0674 0.0194 0.0834 48 HIS A CE1 192 N NE2 . HIS A 27 ? 0.4256 0.4052 0.3424 -0.0639 0.0329 0.0960 48 HIS A NE2 193 N N . ASP A 28 ? 0.2949 0.3303 0.2987 -0.0758 0.0051 0.0682 49 ASP A N 194 C CA . ASP A 28 ? 0.2837 0.3162 0.2704 -0.0712 0.0126 0.0660 49 ASP A CA 195 C C . ASP A 28 ? 0.2594 0.2981 0.2456 -0.0690 0.0042 0.0563 49 ASP A C 196 O O . ASP A 28 ? 0.2562 0.3112 0.2647 -0.0655 -0.0026 0.0536 49 ASP A O 197 C CB . ASP A 28 ? 0.3311 0.3419 0.2786 -0.0714 0.0209 0.0673 49 ASP A CB 198 C CG . ASP A 28 ? 0.3834 0.3824 0.3121 -0.0667 0.0370 0.0672 49 ASP A CG 199 O OD1 . ASP A 28 ? 0.3764 0.3876 0.3252 -0.0604 0.0421 0.0696 49 ASP A OD1 200 O OD2 . ASP A 28 ? 0.3757 0.3534 0.2685 -0.0682 0.0446 0.0643 49 ASP A OD2 201 N N . GLN A 29 ? 0.2569 0.2823 0.2174 -0.0708 0.0052 0.0501 50 GLN A N 202 C CA . GLN A 29 ? 0.2247 0.2493 0.1821 -0.0671 0.0050 0.0429 50 GLN A CA 203 C C . GLN A 29 ? 0.2191 0.2544 0.1931 -0.0667 -0.0097 0.0381 50 GLN A C 204 O O . GLN A 29 ? 0.2237 0.2592 0.1969 -0.0592 -0.0088 0.0346 50 GLN A O 205 C CB . GLN A 29 ? 0.2524 0.2587 0.1844 -0.0729 0.0125 0.0353 50 GLN A CB 206 C CG . GLN A 29 ? 0.2773 0.2648 0.1859 -0.0714 0.0313 0.0372 50 GLN A CG 207 C CD . GLN A 29 ? 0.3070 0.2737 0.1918 -0.0806 0.0396 0.0251 50 GLN A CD 208 O OE1 . GLN A 29 ? 0.3047 0.2567 0.1654 -0.0875 0.0441 0.0210 50 GLN A OE1 209 N NE2 . GLN A 29 ? 0.2525 0.2157 0.1433 -0.0808 0.0431 0.0184 50 GLN A NE2 210 N N . CYS A 30 ? 0.2051 0.2450 0.1896 -0.0723 -0.0204 0.0391 51 CYS A N 211 C CA . CYS A 30 ? 0.1982 0.2432 0.1960 -0.0712 -0.0316 0.0349 51 CYS A CA 212 C C . CYS A 30 ? 0.1948 0.2507 0.2133 -0.0690 -0.0375 0.0337 51 CYS A C 213 O O . CYS A 30 ? 0.2028 0.2594 0.2278 -0.0677 -0.0463 0.0278 51 CYS A O 214 C CB . CYS A 30 ? 0.1920 0.2349 0.1912 -0.0759 -0.0382 0.0371 51 CYS A CB 215 S SG . CYS A 30 ? 0.2524 0.2940 0.2344 -0.0801 -0.0386 0.0349 51 CYS A SG 216 N N . SER A 31 ? 0.2222 0.2875 0.2521 -0.0691 -0.0324 0.0380 52 SER A N 217 C CA . SER A 31 ? 0.1946 0.2771 0.2520 -0.0703 -0.0398 0.0342 52 SER A CA 218 C C . SER A 31 ? 0.2244 0.3179 0.2816 -0.0616 -0.0514 0.0245 52 SER A C 219 O O . SER A 31 ? 0.2038 0.3083 0.2802 -0.0659 -0.0633 0.0158 52 SER A O 220 C CB . SER A 31 ? 0.2197 0.3158 0.2965 -0.0711 -0.0305 0.0415 52 SER A CB 221 O OG . SER A 31 ? 0.2156 0.3196 0.2830 -0.0594 -0.0242 0.0448 52 SER A OG 222 N N . PRO A 32 ? 0.2108 0.2985 0.2438 -0.0491 -0.0470 0.0251 53 PRO A N 223 C CA . PRO A 32 ? 0.2207 0.3147 0.2446 -0.0358 -0.0561 0.0180 53 PRO A CA 224 C C . PRO A 32 ? 0.2134 0.2947 0.2308 -0.0381 -0.0661 0.0088 53 PRO A C 225 O O . PRO A 32 ? 0.1803 0.2662 0.1897 -0.0285 -0.0770 0.0002 53 PRO A O 226 C CB . PRO A 32 ? 0.2286 0.3084 0.2248 -0.0219 -0.0407 0.0240 53 PRO A CB 227 C CG . PRO A 32 ? 0.2063 0.2829 0.2042 -0.0275 -0.0260 0.0327 53 PRO A CG 228 C CD . PRO A 32 ? 0.1978 0.2717 0.2101 -0.0456 -0.0310 0.0321 53 PRO A CD 229 N N . TRP A 33 ? 0.1642 0.2297 0.1822 -0.0484 -0.0620 0.0111 54 TRP A N 230 C CA . TRP A 33 ? 0.2023 0.2534 0.2166 -0.0502 -0.0675 0.0053 54 TRP A CA 231 C C . TRP A 33 ? 0.2304 0.2834 0.2658 -0.0621 -0.0757 -0.0007 54 TRP A C 232 O O . TRP A 33 ? 0.2278 0.2642 0.2598 -0.0641 -0.0772 -0.0048 54 TRP A O 233 C CB . TRP A 33 ? 0.2020 0.2395 0.2107 -0.0534 -0.0589 0.0121 54 TRP A CB 234 C CG . TRP A 33 ? 0.2416 0.2708 0.2333 -0.0443 -0.0492 0.0136 54 TRP A CG 235 C CD1 . TRP A 33 ? 0.2558 0.2715 0.2361 -0.0352 -0.0456 0.0112 54 TRP A CD1 236 C CD2 . TRP A 33 ? 0.2199 0.2492 0.2048 -0.0444 -0.0380 0.0175 54 TRP A CD2 237 N NE1 . TRP A 33 ? 0.2383 0.2471 0.2094 -0.0301 -0.0318 0.0139 54 TRP A NE1 238 C CE2 . TRP A 33 ? 0.2358 0.2519 0.2090 -0.0364 -0.0272 0.0167 54 TRP A CE2 239 C CE3 . TRP A 33 ? 0.2464 0.2818 0.2325 -0.0500 -0.0332 0.0214 54 TRP A CE3 240 C CZ2 . TRP A 33 ? 0.1976 0.2059 0.1630 -0.0365 -0.0115 0.0180 54 TRP A CZ2 241 C CZ3 . TRP A 33 ? 0.2312 0.2575 0.2046 -0.0489 -0.0190 0.0223 54 TRP A CZ3 242 C CH2 . TRP A 33 ? 0.2151 0.2278 0.1798 -0.0435 -0.0083 0.0198 54 TRP A CH2 243 N N . LYS A 34 ? 0.2281 0.2990 0.2867 -0.0698 -0.0780 -0.0011 55 LYS A N 244 C CA . LYS A 34 ? 0.2242 0.2928 0.3081 -0.0843 -0.0787 -0.0048 55 LYS A CA 245 C C . LYS A 34 ? 0.2535 0.3163 0.3402 -0.0875 -0.0890 -0.0221 55 LYS A C 246 O O . LYS A 34 ? 0.2868 0.3354 0.3867 -0.0983 -0.0842 -0.0259 55 LYS A O 247 C CB . LYS A 34 ? 0.2051 0.2931 0.3175 -0.0910 -0.0731 -0.0011 55 LYS A CB 248 C CG . LYS A 34 ? 0.2224 0.3403 0.3520 -0.0874 -0.0838 -0.0123 55 LYS A CG 249 C CD . LYS A 34 ? 0.2635 0.4017 0.4276 -0.0942 -0.0751 -0.0067 55 LYS A CD 250 C CE . LYS A 34 ? 0.3102 0.4856 0.4893 -0.0853 -0.0850 -0.0098 55 LYS A CE 251 N NZ . LYS A 34 ? 0.3555 0.5553 0.5778 -0.0939 -0.0781 -0.0104 55 LYS A NZ 252 N N . LYS A 35 ? 0.2702 0.3412 0.3407 -0.0772 -0.1018 -0.0326 56 LYS A N 253 C CA . LYS A 35 ? 0.3282 0.3921 0.3935 -0.0796 -0.1117 -0.0511 56 LYS A CA 254 C C . LYS A 35 ? 0.3452 0.3715 0.3845 -0.0764 -0.1086 -0.0512 56 LYS A C 255 O O . LYS A 35 ? 0.3309 0.3378 0.3673 -0.0832 -0.1119 -0.0647 56 LYS A O 256 C CB . LYS A 35 ? 0.3857 0.4727 0.4366 -0.0672 -0.1260 -0.0609 56 LYS A CB 257 C CG . LYS A 35 ? 0.4389 0.5651 0.5182 -0.0721 -0.1299 -0.0597 56 LYS A CG 258 C CD . LYS A 35 ? 0.4983 0.6288 0.6088 -0.0946 -0.1286 -0.0687 56 LYS A CD 259 C CE . LYS A 35 ? 0.5136 0.6736 0.6623 -0.1025 -0.1219 -0.0600 56 LYS A CE 260 N NZ . LYS A 35 ? 0.5142 0.7111 0.6781 -0.0980 -0.1382 -0.0600 56 LYS A NZ 261 N N . ASN A 36 ? 0.3255 0.3415 0.3467 -0.0649 -0.0970 -0.0360 57 ASN A N 262 C CA . ASN A 36 ? 0.3111 0.2974 0.3113 -0.0576 -0.0888 -0.0335 57 ASN A CA 263 C C . ASN A 36 ? 0.2869 0.2720 0.2843 -0.0513 -0.0760 -0.0161 57 ASN A C 264 O O . ASN A 36 ? 0.2653 0.2577 0.2508 -0.0414 -0.0731 -0.0119 57 ASN A O 265 C CB . ASN A 36 ? 0.3442 0.3193 0.3123 -0.0428 -0.0957 -0.0451 57 ASN A CB 266 C CG . ASN A 36 ? 0.3616 0.3012 0.3095 -0.0367 -0.0865 -0.0462 57 ASN A CG 267 O OD1 . ASN A 36 ? 0.3454 0.2683 0.3050 -0.0466 -0.0803 -0.0457 57 ASN A OD1 268 N ND2 . ASN A 36 ? 0.3807 0.3057 0.2970 -0.0182 -0.0823 -0.0461 57 ASN A ND2 269 N N . ALA A 37 ? 0.2591 0.2357 0.2681 -0.0570 -0.0678 -0.0066 58 ALA A N 270 C CA . ALA A 37 ? 0.2761 0.2618 0.2894 -0.0549 -0.0604 0.0080 58 ALA A CA 271 C C . ALA A 37 ? 0.3181 0.2912 0.3334 -0.0505 -0.0526 0.0173 58 ALA A C 272 O O . ALA A 37 ? 0.2230 0.1782 0.2403 -0.0522 -0.0493 0.0164 58 ALA A O 273 C CB . ALA A 37 ? 0.2702 0.2710 0.2979 -0.0644 -0.0607 0.0141 58 ALA A CB 274 N N . CYS A 38 ? 0.2684 0.2525 0.2859 -0.0453 -0.0487 0.0260 59 CYS A N 275 C CA . CYS A 38 ? 0.2987 0.2829 0.3243 -0.0392 -0.0431 0.0372 59 CYS A CA 276 C C . CYS A 38 ? 0.3102 0.3122 0.3454 -0.0429 -0.0460 0.0479 59 CYS A C 277 O O . CYS A 38 ? 0.2897 0.2994 0.3325 -0.0356 -0.0440 0.0590 59 CYS A O 278 C CB . CYS A 38 ? 0.2654 0.2573 0.2943 -0.0320 -0.0378 0.0389 59 CYS A CB 279 S SG . CYS A 38 ? 0.2848 0.2470 0.2966 -0.0196 -0.0282 0.0327 59 CYS A SG 280 N N . CYS A 39 ? 0.1807 0.1905 0.2137 -0.0517 -0.0503 0.0453 60 CYS A N 281 C CA . CYS A 39 ? 0.2619 0.2846 0.2953 -0.0533 -0.0522 0.0549 60 CYS A CA 282 C C . CYS A 39 ? 0.2623 0.2706 0.2959 -0.0563 -0.0470 0.0591 60 CYS A C 283 O O . CYS A 39 ? 0.2840 0.2823 0.3220 -0.0632 -0.0457 0.0501 60 CYS A O 284 C CB . CYS A 39 ? 0.2298 0.2679 0.2576 -0.0600 -0.0561 0.0502 60 CYS A CB 285 S SG . CYS A 39 ? 0.2714 0.3036 0.2957 -0.0671 -0.0543 0.0412 60 CYS A SG 286 N N . THR A 40 ? 0.2483 0.2564 0.2782 -0.0504 -0.0433 0.0726 61 THR A N 287 C CA . THR A 40 ? 0.2777 0.2690 0.3079 -0.0524 -0.0329 0.0793 61 THR A CA 288 C C . THR A 40 ? 0.3002 0.2996 0.3261 -0.0597 -0.0330 0.0781 61 THR A C 289 O O . THR A 40 ? 0.2816 0.2982 0.2981 -0.0607 -0.0411 0.0748 61 THR A O 290 C CB . THR A 40 ? 0.3100 0.2943 0.3313 -0.0379 -0.0252 0.0978 61 THR A CB 291 O OG1 . THR A 40 ? 0.2986 0.3078 0.3065 -0.0304 -0.0356 0.1043 61 THR A OG1 292 C CG2 . THR A 40 ? 0.3147 0.2878 0.3408 -0.0278 -0.0206 0.1020 61 THR A CG2 293 N N . ALA A 41 ? 0.3044 0.2894 0.3385 -0.0650 -0.0213 0.0809 62 ALA A N 294 C CA . ALA A 41 ? 0.2970 0.2871 0.3280 -0.0692 -0.0168 0.0832 62 ALA A CA 295 C C . ALA A 41 ? 0.3141 0.3095 0.3169 -0.0584 -0.0182 0.0948 62 ALA A C 296 O O . ALA A 41 ? 0.2838 0.2896 0.2736 -0.0606 -0.0225 0.0913 62 ALA A O 297 C CB . ALA A 41 ? 0.2809 0.2535 0.3303 -0.0753 0.0007 0.0875 62 ALA A CB 298 N N . SER A 42 ? 0.2941 0.2816 0.2849 -0.0454 -0.0146 0.1082 63 SER A N 299 C CA . SER A 42 ? 0.3305 0.3266 0.2912 -0.0326 -0.0196 0.1184 63 SER A CA 300 C C . SER A 42 ? 0.2992 0.3236 0.2525 -0.0352 -0.0403 0.1071 63 SER A C 301 O O . SER A 42 ? 0.3097 0.3415 0.2402 -0.0349 -0.0457 0.1051 63 SER A O 302 C CB . SER A 42 ? 0.3995 0.3836 0.3484 -0.0137 -0.0112 0.1373 63 SER A CB 303 O OG . SER A 42 ? 0.4530 0.4611 0.3861 -0.0001 -0.0276 0.1418 63 SER A OG 304 N N . THR A 43 ? 0.2554 0.2921 0.2277 -0.0384 -0.0491 0.0990 64 THR A N 305 C CA . THR A 43 ? 0.2766 0.3366 0.2509 -0.0446 -0.0633 0.0865 64 THR A CA 306 C C . THR A 43 ? 0.2699 0.3267 0.2387 -0.0575 -0.0613 0.0742 64 THR A C 307 O O . THR A 43 ? 0.2811 0.3483 0.2354 -0.0617 -0.0679 0.0670 64 THR A O 308 C CB . THR A 43 ? 0.2851 0.3514 0.2838 -0.0456 -0.0661 0.0808 64 THR A CB 309 O OG1 . THR A 43 ? 0.2865 0.3591 0.2904 -0.0315 -0.0674 0.0931 64 THR A OG1 310 C CG2 . THR A 43 ? 0.2276 0.3125 0.2332 -0.0543 -0.0742 0.0672 64 THR A CG2 311 N N . SER A 44 ? 0.2463 0.2893 0.2268 -0.0631 -0.0519 0.0713 65 SER A N 312 C CA . SER A 44 ? 0.2697 0.3112 0.2479 -0.0713 -0.0481 0.0622 65 SER A CA 313 C C . SER A 44 ? 0.2961 0.3314 0.2505 -0.0707 -0.0423 0.0668 65 SER A C 314 O O . SER A 44 ? 0.3063 0.3416 0.2470 -0.0753 -0.0412 0.0594 65 SER A O 315 C CB . SER A 44 ? 0.2745 0.3092 0.2720 -0.0746 -0.0419 0.0596 65 SER A CB 316 O OG . SER A 44 ? 0.2571 0.2822 0.2592 -0.0747 -0.0317 0.0682 65 SER A OG 317 N N . GLN A 45 ? 0.2802 0.3057 0.2265 -0.0635 -0.0358 0.0796 66 GLN A N 318 C CA . GLN A 45 ? 0.3504 0.3652 0.2678 -0.0591 -0.0279 0.0863 66 GLN A CA 319 C C . GLN A 45 ? 0.3561 0.3804 0.2420 -0.0561 -0.0412 0.0814 66 GLN A C 320 O O . GLN A 45 ? 0.4083 0.4264 0.2693 -0.0594 -0.0392 0.0751 66 GLN A O 321 C CB . GLN A 45 ? 0.3912 0.3897 0.3063 -0.0493 -0.0146 0.1033 66 GLN A CB 322 C CG . GLN A 45 ? 0.4974 0.4779 0.3914 -0.0449 0.0023 0.1121 66 GLN A CG 323 C CD . GLN A 45 ? 0.6022 0.5625 0.5053 -0.0375 0.0227 0.1292 66 GLN A CD 324 O OE1 . GLN A 45 ? 0.6166 0.5742 0.5355 -0.0344 0.0230 0.1342 66 GLN A OE1 325 N NE2 . GLN A 45 ? 0.6296 0.5721 0.5240 -0.0345 0.0436 0.1384 66 GLN A NE2 326 N N . GLU A 46 ? 0.2957 0.3357 0.1835 -0.0496 -0.0548 0.0837 67 GLU A N 327 C CA . GLU A 46 ? 0.3385 0.3953 0.2006 -0.0462 -0.0711 0.0784 67 GLU A CA 328 C C . GLU A 46 ? 0.2991 0.3683 0.1676 -0.0627 -0.0797 0.0574 67 GLU A C 329 O O . GLU A 46 ? 0.3222 0.3950 0.1640 -0.0668 -0.0876 0.0469 67 GLU A O 330 C CB . GLU A 46 ? 0.3390 0.4169 0.2093 -0.0332 -0.0840 0.0874 67 GLU A CB 331 C CG . GLU A 46 ? 0.3652 0.4677 0.2161 -0.0272 -0.1035 0.0796 67 GLU A CG 332 C CD . GLU A 46 ? 0.4552 0.5406 0.2577 -0.0137 -0.1007 0.0845 67 GLU A CD 333 O OE1 . GLU A 46 ? 0.4910 0.5485 0.2753 -0.0052 -0.0821 0.1026 67 GLU A OE1 334 O OE2 . GLU A 46 ? 0.4805 0.5778 0.2638 -0.0111 -0.1159 0.0699 67 GLU A OE2 335 N N . LEU A 47 ? 0.2710 0.3423 0.1715 -0.0716 -0.0758 0.0509 68 LEU A N 336 C CA . LEU A 47 ? 0.3226 0.4022 0.2319 -0.0856 -0.0792 0.0329 68 LEU A CA 337 C C . LEU A 47 ? 0.3418 0.4005 0.2276 -0.0941 -0.0674 0.0235 68 LEU A C 338 O O . LEU A 47 ? 0.3145 0.3751 0.1988 -0.1062 -0.0683 0.0074 68 LEU A O 339 C CB . LEU A 47 ? 0.2873 0.3712 0.2312 -0.0886 -0.0756 0.0304 68 LEU A CB 340 C CG . LEU A 47 ? 0.3095 0.3738 0.2603 -0.0878 -0.0608 0.0333 68 LEU A CG 341 C CD1 . LEU A 47 ? 0.3003 0.3516 0.2421 -0.0956 -0.0493 0.0230 68 LEU A CD1 342 C CD2 . LEU A 47 ? 0.2818 0.3508 0.2588 -0.0841 -0.0618 0.0352 68 LEU A CD2 343 N N . HIS A 48 ? 0.3218 0.3595 0.1906 -0.0879 -0.0540 0.0336 69 HIS A N 344 C CA . HIS A 48 ? 0.3661 0.3813 0.2084 -0.0925 -0.0398 0.0276 69 HIS A CA 345 C C . HIS A 48 ? 0.4275 0.4364 0.2269 -0.0940 -0.0463 0.0197 69 HIS A C 346 O O . HIS A 48 ? 0.4375 0.4253 0.2109 -0.1003 -0.0354 0.0099 69 HIS A O 347 C CB . HIS A 48 ? 0.3550 0.3532 0.1994 -0.0847 -0.0211 0.0418 69 HIS A CB 348 C CG . HIS A 48 ? 0.3262 0.3301 0.2059 -0.0853 -0.0155 0.0433 69 HIS A CG 349 N ND1 . HIS A 48 ? 0.3094 0.3286 0.2185 -0.0840 -0.0253 0.0458 69 HIS A ND1 350 C CD2 . HIS A 48 ? 0.3497 0.3462 0.2362 -0.0850 -0.0018 0.0424 69 HIS A CD2 351 C CE1 . HIS A 48 ? 0.3257 0.3467 0.2556 -0.0837 -0.0199 0.0445 69 HIS A CE1 352 N NE2 . HIS A 48 ? 0.3165 0.3263 0.2344 -0.0831 -0.0063 0.0435 69 HIS A NE2 353 N N . LYS A 49 ? 0.3602 0.3304 0.2541 -0.0682 -0.0031 0.0804 70 LYS A N 354 C CA . LYS A 49 ? 0.3838 0.3527 0.2579 -0.0673 -0.0021 0.0856 70 LYS A CA 355 C C . LYS A 49 ? 0.3768 0.3435 0.2449 -0.0582 -0.0082 0.0794 70 LYS A C 356 O O . LYS A 49 ? 0.3802 0.3410 0.2578 -0.0536 -0.0150 0.0748 70 LYS A O 357 C CB . LYS A 49 ? 0.4324 0.3857 0.2958 -0.0730 -0.0054 0.0982 70 LYS A CB 358 C CG . LYS A 49 ? 0.4861 0.4405 0.3573 -0.0829 0.0008 0.1047 70 LYS A CG 359 C CD . LYS A 49 ? 0.5521 0.4906 0.4166 -0.0850 -0.0027 0.1147 70 LYS A CD 360 C CE . LYS A 49 ? 0.6441 0.5872 0.5132 -0.0948 0.0059 0.1213 70 LYS A CE 361 N NZ . LYS A 49 ? 0.6860 0.6257 0.5751 -0.1020 0.0052 0.1201 70 LYS A NZ 362 N N . ASP A 50 ? 0.3493 0.3223 0.2025 -0.0559 -0.0056 0.0787 71 ASP A N 363 C CA . ASP A 50 ? 0.3971 0.3669 0.2433 -0.0483 -0.0123 0.0735 71 ASP A CA 364 C C . ASP A 50 ? 0.3931 0.3471 0.2320 -0.0472 -0.0219 0.0800 71 ASP A C 365 O O . ASP A 50 ? 0.3823 0.3287 0.2126 -0.0517 -0.0219 0.0902 71 ASP A O 366 C CB . ASP A 50 ? 0.4760 0.4562 0.3070 -0.0464 -0.0076 0.0706 71 ASP A CB 367 C CG . ASP A 50 ? 0.5044 0.4986 0.3454 -0.0436 -0.0013 0.0604 71 ASP A CG 368 O OD1 . ASP A 50 ? 0.5101 0.5030 0.3655 -0.0396 -0.0048 0.0537 71 ASP A OD1 369 O OD2 . ASP A 50 ? 0.5172 0.5241 0.3522 -0.0453 0.0069 0.0595 71 ASP A OD2 370 N N . THR A 51 ? 0.3314 0.2810 0.1763 -0.0409 -0.0301 0.0738 72 THR A N 371 C CA . THR A 51 ? 0.3132 0.2494 0.1542 -0.0381 -0.0405 0.0782 72 THR A CA 372 C C . THR A 51 ? 0.3268 0.2509 0.1688 -0.0435 -0.0415 0.0886 72 THR A C 373 O O . THR A 51 ? 0.3454 0.2619 0.1772 -0.0437 -0.0437 0.0963 72 THR A O 374 C CB . THR A 51 ? 0.4164 0.3515 0.2372 -0.0346 -0.0453 0.0800 72 THR A CB 375 O OG1 . THR A 51 ? 0.4242 0.3706 0.2447 -0.0308 -0.0433 0.0694 72 THR A OG1 376 C CG2 . THR A 51 ? 0.3712 0.2955 0.1932 -0.0291 -0.0574 0.0811 72 THR A CG2 377 N N . SER A 52 ? 0.3378 0.2624 0.1971 -0.0462 -0.0389 0.0862 73 SER A N 378 C CA . SER A 52 ? 0.3899 0.3031 0.2538 -0.0521 -0.0395 0.0940 73 SER A CA 379 C C . SER A 52 ? 0.4079 0.3037 0.2726 -0.0480 -0.0513 0.0976 73 SER A C 380 O O . SER A 52 ? 0.3955 0.2914 0.2619 -0.0402 -0.0585 0.0917 73 SER A O 381 C CB . SER A 52 ? 0.3954 0.3153 0.2790 -0.0546 -0.0353 0.0873 73 SER A CB 382 O OG . SER A 52 ? 0.3910 0.3093 0.2880 -0.0483 -0.0419 0.0791 73 SER A OG 383 N N . ARG A 53 ? 0.3809 0.2622 0.2467 -0.0531 -0.0534 0.1066 74 ARG A N 384 C CA . ARG A 53 ? 0.4067 0.2707 0.2762 -0.0481 -0.0648 0.1091 74 ARG A CA 385 C C . ARG A 53 ? 0.3812 0.2442 0.2709 -0.0427 -0.0709 0.0980 74 ARG A C 386 O O . ARG A 53 ? 0.4007 0.2522 0.2950 -0.0365 -0.0812 0.0971 74 ARG A O 387 C CB . ARG A 53 ? 0.4012 0.2513 0.2699 -0.0539 -0.0641 0.1197 74 ARG A CB 388 N N . LEU A 54 ? 0.3559 0.2337 0.2586 -0.0438 -0.0641 0.0881 75 LEU A N 389 C CA . LEU A 54 ? 0.3762 0.2563 0.2977 -0.0383 -0.0687 0.0767 75 LEU A CA 390 C C . LEU A 54 ? 0.3565 0.2400 0.2806 -0.0285 -0.0763 0.0698 75 LEU A C 391 O O . LEU A 54 ? 0.3520 0.2289 0.2874 -0.0228 -0.0845 0.0649 75 LEU A O 392 C CB . LEU A 54 ? 0.3548 0.2517 0.2878 -0.0410 -0.0603 0.0681 75 LEU A CB 393 C CG . LEU A 54 ? 0.3656 0.2609 0.3027 -0.0502 -0.0544 0.0718 75 LEU A CG 394 C CD1 . LEU A 54 ? 0.3414 0.2557 0.2885 -0.0510 -0.0474 0.0628 75 LEU A CD1 395 C CD2 . LEU A 54 ? 0.3969 0.2749 0.3448 -0.0516 -0.0617 0.0724 75 LEU A CD2 396 N N . TYR A 55 ? 0.3353 0.2293 0.2503 -0.0264 -0.0739 0.0687 76 TYR A N 397 C CA . TYR A 55 ? 0.3097 0.2085 0.2272 -0.0185 -0.0808 0.0627 76 TYR A CA 398 C C . TYR A 55 ? 0.3372 0.2369 0.2372 -0.0178 -0.0819 0.0673 76 TYR A C 399 O O . TYR A 55 ? 0.3118 0.2179 0.2132 -0.0125 -0.0867 0.0618 76 TYR A O 400 C CB . TYR A 55 ? 0.2707 0.1875 0.2017 -0.0167 -0.0760 0.0516 76 TYR A CB 401 C CG . TYR A 55 ? 0.2659 0.1863 0.2121 -0.0175 -0.0737 0.0458 76 TYR A CG 402 C CD1 . TYR A 55 ? 0.2511 0.1698 0.2106 -0.0117 -0.0807 0.0392 76 TYR A CD1 403 C CD2 . TYR A 55 ? 0.2418 0.1685 0.1893 -0.0233 -0.0650 0.0459 76 TYR A CD2 404 C CE1 . TYR A 55 ? 0.2420 0.1652 0.2145 -0.0118 -0.0789 0.0322 76 TYR A CE1 405 C CE2 . TYR A 55 ? 0.2321 0.1633 0.1926 -0.0237 -0.0637 0.0397 76 TYR A CE2 406 C CZ . TYR A 55 ? 0.2678 0.1971 0.2403 -0.0179 -0.0706 0.0325 76 TYR A CZ 407 O OH . TYR A 55 ? 0.2685 0.2036 0.2534 -0.0176 -0.0697 0.0246 76 TYR A OH 408 N N . ASN A 56 ? 0.3557 0.2509 0.2397 -0.0235 -0.0771 0.0765 77 ASN A N 409 C CA . ASN A 56 ? 0.3451 0.2438 0.2112 -0.0229 -0.0769 0.0794 77 ASN A CA 410 C C . ASN A 56 ? 0.3314 0.2461 0.2029 -0.0210 -0.0728 0.0689 77 ASN A C 411 O O . ASN A 56 ? 0.3043 0.2228 0.1692 -0.0172 -0.0771 0.0656 77 ASN A O 412 C CB . ASN A 56 ? 0.3833 0.2719 0.2403 -0.0169 -0.0890 0.0836 77 ASN A CB 413 C CG . ASN A 56 ? 0.4292 0.3021 0.2845 -0.0181 -0.0916 0.0932 77 ASN A CG 414 O OD1 . ASN A 56 ? 0.4180 0.2876 0.2681 -0.0253 -0.0839 0.1006 77 ASN A OD1 415 N ND2 . ASN A 56 ? 0.4399 0.3036 0.3014 -0.0113 -0.1026 0.0926 77 ASN A ND2 416 N N . PHE A 57 ? 0.3162 0.2396 0.1996 -0.0238 -0.0648 0.0639 78 PHE A N 417 C CA . PHE A 57 ? 0.3142 0.2505 0.2040 -0.0224 -0.0613 0.0553 78 PHE A CA 418 C C . PHE A 57 ? 0.3125 0.2552 0.1917 -0.0252 -0.0535 0.0554 78 PHE A C 419 O O . PHE A 57 ? 0.3144 0.2592 0.1918 -0.0297 -0.0460 0.0588 78 PHE A O 420 C CB . PHE A 57 ? 0.3208 0.2643 0.2288 -0.0225 -0.0580 0.0496 78 PHE A CB 421 C CG . PHE A 57 ? 0.3177 0.2722 0.2338 -0.0208 -0.0563 0.0423 78 PHE A CG 422 C CD1 . PHE A 57 ? 0.2814 0.2387 0.2048 -0.0170 -0.0629 0.0375 78 PHE A CD1 423 C CD2 . PHE A 57 ? 0.3186 0.2804 0.2359 -0.0231 -0.0485 0.0406 78 PHE A CD2 424 C CE1 . PHE A 57 ? 0.2997 0.2660 0.2314 -0.0169 -0.0612 0.0320 78 PHE A CE1 425 C CE2 . PHE A 57 ? 0.3201 0.2892 0.2451 -0.0220 -0.0476 0.0353 78 PHE A CE2 426 C CZ . PHE A 57 ? 0.2978 0.2688 0.2299 -0.0196 -0.0536 0.0315 78 PHE A CZ 427 N N . ASN A 58 ? 0.2988 0.2458 0.1727 -0.0223 -0.0557 0.0505 79 ASN A N 428 C CA . ASN A 58 ? 0.2906 0.2441 0.1548 -0.0232 -0.0497 0.0480 79 ASN A CA 429 C C . ASN A 58 ? 0.2973 0.2588 0.1747 -0.0226 -0.0453 0.0401 79 ASN A C 430 O O . ASN A 58 ? 0.2463 0.2093 0.1325 -0.0201 -0.0497 0.0341 79 ASN A O 431 C CB . ASN A 58 ? 0.2960 0.2484 0.1445 -0.0200 -0.0557 0.0465 79 ASN A CB 432 C CG . ASN A 58 ? 0.3573 0.3172 0.1941 -0.0201 -0.0496 0.0426 79 ASN A CG 433 O OD1 . ASN A 58 ? 0.3653 0.3308 0.2048 -0.0227 -0.0406 0.0425 79 ASN A OD1 434 N ND2 . ASN A 58 ? 0.3507 0.3119 0.1753 -0.0166 -0.0550 0.0381 79 ASN A ND2 435 N N . TRP A 59 ? 0.2982 0.2650 0.1780 -0.0251 -0.0369 0.0407 80 TRP A N 436 C CA . TRP A 59 ? 0.2617 0.2349 0.1523 -0.0239 -0.0332 0.0346 80 TRP A CA 437 C C . TRP A 59 ? 0.2982 0.2734 0.1819 -0.0210 -0.0336 0.0280 80 TRP A C 438 O O . TRP A 59 ? 0.2933 0.2698 0.1866 -0.0192 -0.0337 0.0222 80 TRP A O 439 C CB . TRP A 59 ? 0.2776 0.2569 0.1726 -0.0263 -0.0251 0.0366 80 TRP A CB 440 C CG . TRP A 59 ? 0.2760 0.2549 0.1814 -0.0285 -0.0250 0.0400 80 TRP A CG 441 C CD1 . TRP A 59 ? 0.2972 0.2762 0.2145 -0.0273 -0.0284 0.0382 80 TRP A CD1 442 C CD2 . TRP A 59 ? 0.3120 0.2917 0.2177 -0.0326 -0.0214 0.0447 80 TRP A CD2 443 N NE1 . TRP A 59 ? 0.3067 0.2867 0.2306 -0.0294 -0.0274 0.0405 80 TRP A NE1 444 C CE2 . TRP A 59 ? 0.3128 0.2922 0.2305 -0.0329 -0.0235 0.0444 80 TRP A CE2 445 C CE3 . TRP A 59 ? 0.3372 0.3189 0.2346 -0.0365 -0.0161 0.0490 80 TRP A CE3 446 C CZ2 . TRP A 59 ? 0.3356 0.3151 0.2580 -0.0366 -0.0216 0.0471 80 TRP A CZ2 447 C CZ3 . TRP A 59 ? 0.3727 0.3544 0.2758 -0.0414 -0.0138 0.0531 80 TRP A CZ3 448 C CH2 . TRP A 59 ? 0.3572 0.3370 0.2730 -0.0412 -0.0171 0.0515 80 TRP A CH2 449 N N . ASP A 60 ? 0.3186 0.2939 0.1854 -0.0207 -0.0336 0.0290 81 ASP A N 450 C CA . ASP A 60 ? 0.3390 0.3180 0.1971 -0.0174 -0.0334 0.0213 81 ASP A CA 451 C C . ASP A 60 ? 0.3430 0.3175 0.1970 -0.0147 -0.0430 0.0167 81 ASP A C 452 O O . ASP A 60 ? 0.3325 0.3089 0.1708 -0.0126 -0.0454 0.0137 81 ASP A O 453 C CB . ASP A 60 ? 0.3771 0.3622 0.2175 -0.0186 -0.0275 0.0243 81 ASP A CB 454 C CG . ASP A 60 ? 0.3973 0.3892 0.2431 -0.0220 -0.0179 0.0283 81 ASP A CG 455 O OD1 . ASP A 60 ? 0.3753 0.3702 0.2361 -0.0209 -0.0151 0.0244 81 ASP A OD1 456 O OD2 . ASP A 60 ? 0.4406 0.4353 0.2760 -0.0259 -0.0135 0.0357 81 ASP A OD2 457 N N . HIS A 61 ? 0.3250 0.2955 0.1932 -0.0148 -0.0485 0.0158 82 HIS A N 458 C CA . HIS A 61 ? 0.3000 0.2681 0.1675 -0.0127 -0.0582 0.0113 82 HIS A CA 459 C C . HIS A 61 ? 0.3490 0.3182 0.2201 -0.0106 -0.0609 0.0000 82 HIS A C 460 O O . HIS A 61 ? 0.3915 0.3603 0.2593 -0.0086 -0.0690 -0.0057 82 HIS A O 461 C CB . HIS A 61 ? 0.2542 0.2202 0.1371 -0.0139 -0.0627 0.0139 82 HIS A CB 462 C CG . HIS A 61 ? 0.2516 0.2197 0.1526 -0.0161 -0.0578 0.0136 82 HIS A CG 463 N ND1 . HIS A 61 ? 0.2641 0.2334 0.1700 -0.0181 -0.0519 0.0198 82 HIS A ND1 464 C CD2 . HIS A 61 ? 0.2415 0.2106 0.1561 -0.0169 -0.0580 0.0083 82 HIS A CD2 465 C CE1 . HIS A 61 ? 0.2689 0.2410 0.1891 -0.0193 -0.0489 0.0185 82 HIS A CE1 466 N NE2 . HIS A 61 ? 0.2248 0.1961 0.1505 -0.0189 -0.0523 0.0125 82 HIS A NE2 467 N N . CYS A 62 ? 0.3067 0.2770 0.1857 -0.0106 -0.0551 -0.0038 83 CYS A N 468 C CA . CYS A 62 ? 0.3491 0.3184 0.2313 -0.0080 -0.0579 -0.0152 83 CYS A CA 469 C C . CYS A 62 ? 0.3756 0.3493 0.2483 -0.0051 -0.0510 -0.0191 83 CYS A C 470 O O . CYS A 62 ? 0.3557 0.3285 0.2390 -0.0040 -0.0471 -0.0223 83 CYS A O 471 C CB . CYS A 62 ? 0.3336 0.2983 0.2377 -0.0102 -0.0591 -0.0171 83 CYS A CB 472 S SG . CYS A 62 ? 0.3098 0.2732 0.2267 -0.0133 -0.0682 -0.0173 83 CYS A SG 473 N N . GLY A 63 ? 0.4244 0.4037 0.2771 -0.0037 -0.0495 -0.0182 84 GLY A N 474 C CA . GLY A 63 ? 0.4265 0.4140 0.2695 -0.0017 -0.0410 -0.0201 84 GLY A CA 475 C C . GLY A 63 ? 0.4025 0.3927 0.2514 -0.0052 -0.0325 -0.0099 84 GLY A C 476 O O . GLY A 63 ? 0.3873 0.3726 0.2455 -0.0088 -0.0335 -0.0019 84 GLY A O 477 N N . LYS A 64 ? 0.4156 0.4152 0.2599 -0.0039 -0.0242 -0.0117 85 LYS A N 478 C CA . LYS A 64 ? 0.4074 0.4122 0.2570 -0.0075 -0.0162 -0.0033 85 LYS A CA 479 C C . LYS A 64 ? 0.3577 0.3588 0.2282 -0.0070 -0.0159 -0.0034 85 LYS A C 480 O O . LYS A 64 ? 0.3587 0.3584 0.2382 -0.0026 -0.0170 -0.0117 85 LYS A O 481 C CB . LYS A 64 ? 0.4585 0.4778 0.2987 -0.0061 -0.0072 -0.0065 85 LYS A CB 482 C CG . LYS A 64 ? 0.5062 0.5336 0.3569 -0.0089 0.0012 -0.0014 85 LYS A CG 483 C CD . LYS A 64 ? 0.5833 0.6182 0.4225 -0.0156 0.0078 0.0090 85 LYS A CD 484 C CE . LYS A 64 ? 0.6364 0.6586 0.4692 -0.0204 0.0018 0.0195 85 LYS A CE 485 N NZ . LYS A 64 ? 0.6692 0.6939 0.4941 -0.0278 0.0069 0.0315 85 LYS A NZ 486 N N . MET A 65 ? 0.2992 0.2982 0.1768 -0.0114 -0.0148 0.0059 86 MET A N 487 C CA . MET A 65 ? 0.3039 0.3021 0.1984 -0.0112 -0.0137 0.0072 86 MET A CA 488 C C . MET A 65 ? 0.3420 0.3516 0.2395 -0.0099 -0.0058 0.0061 86 MET A C 489 O O . MET A 65 ? 0.3290 0.3468 0.2186 -0.0132 -0.0003 0.0099 86 MET A O 490 C CB . MET A 65 ? 0.2677 0.2619 0.1678 -0.0157 -0.0156 0.0157 86 MET A CB 491 C CG . MET A 65 ? 0.2731 0.2697 0.1877 -0.0158 -0.0135 0.0182 86 MET A CG 492 S SD . MET A 65 ? 0.2822 0.2779 0.2013 -0.0207 -0.0145 0.0262 86 MET A SD 493 C CE . MET A 65 ? 0.2127 0.1999 0.1359 -0.0204 -0.0223 0.0255 86 MET A CE 494 N N . GLU A 66 ? 0.3183 0.3289 0.2275 -0.0053 -0.0056 0.0010 87 GLU A N 495 C CA . GLU A 66 ? 0.3342 0.3572 0.2482 -0.0025 0.0008 -0.0017 87 GLU A CA 496 C C . GLU A 66 ? 0.3008 0.3312 0.2203 -0.0074 0.0050 0.0062 87 GLU A C 497 O O . GLU A 66 ? 0.2848 0.3092 0.2096 -0.0104 0.0019 0.0123 87 GLU A O 498 C CB . GLU A 66 ? 0.3782 0.3979 0.3048 0.0044 -0.0017 -0.0080 87 GLU A CB 499 C CG . GLU A 66 ? 0.4690 0.4802 0.3928 0.0091 -0.0066 -0.0175 87 GLU A CG 500 C CD . GLU A 66 ? 0.5369 0.5592 0.4498 0.0127 -0.0024 -0.0268 87 GLU A CD 501 O OE1 . GLU A 66 ? 0.5496 0.5871 0.4621 0.0130 0.0050 -0.0267 87 GLU A OE1 502 O OE2 . GLU A 66 ? 0.5652 0.5828 0.4702 0.0151 -0.0062 -0.0347 87 GLU A OE2 503 N N . PRO A 67 ? 0.2650 0.3099 0.1843 -0.0080 0.0120 0.0052 88 PRO A N 504 C CA . PRO A 67 ? 0.3030 0.3562 0.2292 -0.0132 0.0158 0.0112 88 PRO A CA 505 C C . PRO A 67 ? 0.2937 0.3450 0.2342 -0.0109 0.0122 0.0127 88 PRO A C 506 O O . PRO A 67 ? 0.2689 0.3188 0.2128 -0.0156 0.0111 0.0185 88 PRO A O 507 C CB . PRO A 67 ? 0.3230 0.3948 0.2507 -0.0121 0.0238 0.0065 88 PRO A CB 508 C CG . PRO A 67 ? 0.3279 0.4003 0.2410 -0.0099 0.0255 0.0013 88 PRO A CG 509 C CD . PRO A 67 ? 0.2898 0.3456 0.2018 -0.0047 0.0170 -0.0025 88 PRO A CD 510 N N . ALA A 68 ? 0.2531 0.3039 0.2013 -0.0034 0.0100 0.0075 89 ALA A N 511 C CA . ALA A 68 ? 0.2471 0.2973 0.2070 -0.0008 0.0066 0.0103 89 ALA A CA 512 C C . ALA A 68 ? 0.2773 0.3149 0.2358 -0.0043 0.0015 0.0165 89 ALA A C 513 O O . ALA A 68 ? 0.2864 0.3257 0.2512 -0.0049 -0.0003 0.0208 89 ALA A O 514 C CB . ALA A 68 ? 0.2488 0.2974 0.2163 0.0081 0.0041 0.0050 89 ALA A CB 515 N N . CYS A 69 ? 0.2988 0.3257 0.2490 -0.0062 -0.0008 0.0163 90 CYS A N 516 C CA . CYS A 69 ? 0.2892 0.3065 0.2392 -0.0093 -0.0053 0.0211 90 CYS A CA 517 C C . CYS A 69 ? 0.2622 0.2807 0.2073 -0.0154 -0.0045 0.0253 90 CYS A C 518 O O . CYS A 69 ? 0.2442 0.2623 0.1936 -0.0175 -0.0064 0.0289 90 CYS A O 519 C CB . CYS A 69 ? 0.2954 0.3015 0.2415 -0.0082 -0.0094 0.0180 90 CYS A CB 520 S SG . CYS A 69 ? 0.3076 0.3051 0.2544 -0.0126 -0.0145 0.0226 90 CYS A SG 521 N N . LYS A 70 ? 0.2620 0.2819 0.1979 -0.0180 -0.0018 0.0247 91 LYS A N 522 C CA . LYS A 70 ? 0.2443 0.2621 0.1752 -0.0237 -0.0019 0.0295 91 LYS A CA 523 C C . LYS A 70 ? 0.2692 0.2942 0.2084 -0.0270 0.0003 0.0322 91 LYS A C 524 O O . LYS A 70 ? 0.2903 0.3109 0.2305 -0.0305 -0.0022 0.0353 91 LYS A O 525 C CB . LYS A 70 ? 0.2673 0.2855 0.1854 -0.0259 0.0010 0.0299 91 LYS A CB 526 C CG . LYS A 70 ? 0.3316 0.3443 0.2430 -0.0318 0.0000 0.0365 91 LYS A CG 527 C CD . LYS A 70 ? 0.3960 0.4090 0.2916 -0.0338 0.0027 0.0384 91 LYS A CD 528 C CE . LYS A 70 ? 0.4488 0.4562 0.3358 -0.0288 -0.0020 0.0338 91 LYS A CE 529 N NZ . LYS A 70 ? 0.5029 0.5117 0.3722 -0.0295 -0.0004 0.0348 91 LYS A NZ 530 N N . ARG A 71 ? 0.2598 0.2962 0.2061 -0.0254 0.0041 0.0299 92 ARG A N 531 C CA . ARG A 71 ? 0.2572 0.3019 0.2125 -0.0284 0.0052 0.0310 92 ARG A CA 532 C C . ARG A 71 ? 0.2431 0.2842 0.2037 -0.0275 0.0002 0.0322 92 ARG A C 533 O O . ARG A 71 ? 0.2220 0.2658 0.1872 -0.0310 -0.0006 0.0328 92 ARG A O 534 C CB . ARG A 71 ? 0.2433 0.3027 0.2072 -0.0254 0.0088 0.0274 92 ARG A CB 535 C CG . ARG A 71 ? 0.2795 0.3392 0.2484 -0.0176 0.0058 0.0253 92 ARG A CG 536 C CD . ARG A 71 ? 0.3500 0.4239 0.3271 -0.0129 0.0087 0.0209 92 ARG A CD 537 N NE . ARG A 71 ? 0.3591 0.4299 0.3398 -0.0046 0.0054 0.0192 92 ARG A NE 538 C CZ . ARG A 71 ? 0.3696 0.4508 0.3589 0.0018 0.0056 0.0156 92 ARG A CZ 539 N NH1 . ARG A 71 ? 0.3567 0.4549 0.3530 0.0004 0.0095 0.0126 92 ARG A NH1 540 N NH2 . ARG A 71 ? 0.3657 0.4404 0.3581 0.0095 0.0015 0.0152 92 ARG A NH2 541 N N . HIS A 72 ? 0.1972 0.2336 0.1579 -0.0230 -0.0028 0.0320 93 HIS A N 542 C CA . HIS A 72 ? 0.1903 0.2257 0.1550 -0.0223 -0.0065 0.0335 93 HIS A CA 543 C C . HIS A 72 ? 0.1830 0.2105 0.1445 -0.0254 -0.0094 0.0346 93 HIS A C 544 O O . HIS A 72 ? 0.1954 0.2260 0.1612 -0.0263 -0.0112 0.0342 93 HIS A O 545 C CB . HIS A 72 ? 0.1878 0.2204 0.1542 -0.0178 -0.0084 0.0347 93 HIS A CB 546 C CG . HIS A 72 ? 0.1953 0.2346 0.1664 -0.0133 -0.0072 0.0341 93 HIS A CG 547 N ND1 . HIS A 72 ? 0.2078 0.2578 0.1844 -0.0117 -0.0075 0.0349 93 HIS A ND1 548 C CD2 . HIS A 72 ? 0.1990 0.2362 0.1703 -0.0092 -0.0064 0.0318 93 HIS A CD2 549 C CE1 . HIS A 72 ? 0.2238 0.2781 0.2042 -0.0067 -0.0071 0.0339 93 HIS A CE1 550 N NE2 . HIS A 72 ? 0.2064 0.2527 0.1842 -0.0049 -0.0063 0.0318 93 HIS A NE2 551 N N . PHE A 73 ? 0.2032 0.2216 0.1573 -0.0263 -0.0104 0.0350 94 PHE A N 552 C CA . PHE A 73 ? 0.1998 0.2106 0.1512 -0.0283 -0.0141 0.0360 94 PHE A CA 553 C C . PHE A 73 ? 0.2356 0.2460 0.1873 -0.0324 -0.0135 0.0372 94 PHE A C 554 O O . PHE A 73 ? 0.2490 0.2560 0.2038 -0.0331 -0.0171 0.0368 94 PHE A O 555 C CB . PHE A 73 ? 0.2201 0.2220 0.1628 -0.0278 -0.0163 0.0362 94 PHE A CB 556 C CG . PHE A 73 ? 0.2231 0.2233 0.1686 -0.0250 -0.0188 0.0345 94 PHE A CG 557 C CD1 . PHE A 73 ? 0.2331 0.2316 0.1829 -0.0249 -0.0229 0.0342 94 PHE A CD1 558 C CD2 . PHE A 73 ? 0.2219 0.2228 0.1676 -0.0226 -0.0170 0.0327 94 PHE A CD2 559 C CE1 . PHE A 73 ? 0.2281 0.2259 0.1823 -0.0239 -0.0247 0.0332 94 PHE A CE1 560 C CE2 . PHE A 73 ? 0.2506 0.2480 0.2004 -0.0211 -0.0196 0.0316 94 PHE A CE2 561 C CZ . PHE A 73 ? 0.2488 0.2449 0.2030 -0.0225 -0.0232 0.0323 94 PHE A CZ 562 N N . ILE A 74 ? 0.2416 0.2561 0.1917 -0.0351 -0.0090 0.0381 95 ILE A N 563 C CA . ILE A 74 ? 0.1939 0.2080 0.1466 -0.0405 -0.0082 0.0398 95 ILE A CA 564 C C . ILE A 74 ? 0.1996 0.2210 0.1637 -0.0401 -0.0097 0.0361 95 ILE A C 565 O O . ILE A 74 ? 0.2242 0.2410 0.1924 -0.0423 -0.0131 0.0353 95 ILE A O 566 C CB . ILE A 74 ? 0.2320 0.2521 0.1821 -0.0445 -0.0021 0.0416 95 ILE A CB 567 C CG1 . ILE A 74 ? 0.2482 0.2609 0.1844 -0.0454 -0.0010 0.0454 95 ILE A CG1 568 C CG2 . ILE A 74 ? 0.1857 0.2076 0.1433 -0.0514 -0.0009 0.0430 95 ILE A CG2 569 C CD1 . ILE A 74 ? 0.2261 0.2476 0.1578 -0.0490 0.0063 0.0471 95 ILE A CD1 570 N N . GLN A 75 ? 0.1703 0.2028 0.1391 -0.0366 -0.0080 0.0336 96 GLN A N 571 C CA . GLN A 75 ? 0.1598 0.2021 0.1376 -0.0356 -0.0096 0.0299 96 GLN A CA 572 C C . GLN A 75 ? 0.1746 0.2136 0.1534 -0.0333 -0.0141 0.0281 96 GLN A C 573 O O . GLN A 75 ? 0.1671 0.2091 0.1519 -0.0342 -0.0167 0.0241 96 GLN A O 574 C CB . GLN A 75 ? 0.1791 0.2328 0.1596 -0.0310 -0.0079 0.0291 96 GLN A CB 575 C CG . GLN A 75 ? 0.1758 0.2427 0.1644 -0.0298 -0.0094 0.0254 96 GLN A CG 576 C CD . GLN A 75 ? 0.1925 0.2669 0.1884 -0.0345 -0.0077 0.0226 96 GLN A CD 577 O OE1 . GLN A 75 ? 0.1973 0.2693 0.1919 -0.0382 -0.0039 0.0245 96 GLN A OE1 578 N NE2 . GLN A 75 ? 0.1935 0.2781 0.1971 -0.0347 -0.0103 0.0178 96 GLN A NE2 579 N N . ASP A 76 ? 0.1649 0.1996 0.1392 -0.0302 -0.0151 0.0300 97 ASP A N 580 C CA . ASP A 76 ? 0.1574 0.1913 0.1335 -0.0282 -0.0186 0.0282 97 ASP A CA 581 C C . ASP A 76 ? 0.2232 0.2479 0.2004 -0.0302 -0.0223 0.0262 97 ASP A C 582 O O . ASP A 76 ? 0.2390 0.2668 0.2216 -0.0287 -0.0253 0.0217 97 ASP A O 583 C CB . ASP A 76 ? 0.1801 0.2096 0.1523 -0.0263 -0.0189 0.0309 97 ASP A CB 584 C CG . ASP A 76 ? 0.2177 0.2476 0.1929 -0.0248 -0.0221 0.0288 97 ASP A CG 585 O OD1 . ASP A 76 ? 0.2231 0.2639 0.2030 -0.0232 -0.0220 0.0264 97 ASP A OD1 586 O OD2 . ASP A 76 ? 0.2277 0.2491 0.2007 -0.0249 -0.0248 0.0292 97 ASP A OD2 587 N N . THR A 77 ? 0.2166 0.2301 0.1884 -0.0332 -0.0224 0.0298 98 THR A N 588 C CA . THR A 77 ? 0.2216 0.2237 0.1942 -0.0350 -0.0268 0.0297 98 THR A CA 589 C C . THR A 77 ? 0.2059 0.2098 0.1866 -0.0382 -0.0274 0.0264 98 THR A C 590 O O . THR A 77 ? 0.1850 0.1832 0.1713 -0.0374 -0.0324 0.0226 98 THR A O 591 C CB . THR A 77 ? 0.2625 0.2524 0.2252 -0.0379 -0.0266 0.0362 98 THR A CB 592 O OG1 . THR A 77 ? 0.2749 0.2636 0.2307 -0.0348 -0.0271 0.0376 98 THR A OG1 593 C CG2 . THR A 77 ? 0.1945 0.1700 0.1574 -0.0395 -0.0323 0.0381 98 THR A CG2 594 N N . CYS A 78 ? 0.2074 0.2197 0.1903 -0.0415 -0.0229 0.0267 99 CYS A N 595 C CA . CYS A 78 ? 0.2257 0.2424 0.2186 -0.0449 -0.0239 0.0220 99 CYS A CA 596 C C . CYS A 78 ? 0.2175 0.2430 0.2171 -0.0399 -0.0276 0.0137 99 CYS A C 597 O O . CYS A 78 ? 0.2231 0.2456 0.2305 -0.0407 -0.0319 0.0078 99 CYS A O 598 C CB . CYS A 78 ? 0.2248 0.2543 0.2211 -0.0478 -0.0189 0.0221 99 CYS A CB 599 S SG . CYS A 78 ? 0.2271 0.2526 0.2195 -0.0552 -0.0132 0.0294 99 CYS A SG 600 N N . LEU A 79 ? 0.2128 0.2497 0.2095 -0.0350 -0.0258 0.0132 100 LEU A N 601 C CA . LEU A 79 ? 0.1984 0.2468 0.1993 -0.0304 -0.0282 0.0061 100 LEU A CA 602 C C . LEU A 79 ? 0.2002 0.2408 0.2032 -0.0278 -0.0328 0.0023 100 LEU A C 603 O O . LEU A 79 ? 0.2259 0.2692 0.2360 -0.0262 -0.0366 -0.0061 100 LEU A O 604 C CB . LEU A 79 ? 0.1686 0.2294 0.1649 -0.0263 -0.0252 0.0088 100 LEU A CB 605 C CG . LEU A 79 ? 0.1822 0.2573 0.1806 -0.0219 -0.0267 0.0029 100 LEU A CG 606 C CD1 . LEU A 79 ? 0.1983 0.2867 0.2010 -0.0214 -0.0280 -0.0036 100 LEU A CD1 607 C CD2 . LEU A 79 ? 0.2109 0.2940 0.2036 -0.0190 -0.0236 0.0086 100 LEU A CD2 608 N N . TYR A 80 ? 0.1943 0.2259 0.1919 -0.0269 -0.0329 0.0074 101 TYR A N 609 C CA . TYR A 80 ? 0.2023 0.2280 0.2028 -0.0235 -0.0377 0.0037 101 TYR A CA 610 C C . TYR A 80 ? 0.2188 0.2310 0.2253 -0.0250 -0.0432 0.0002 101 TYR A C 611 O O . TYR A 80 ? 0.2254 0.2391 0.2397 -0.0211 -0.0478 -0.0085 101 TYR A O 612 C CB . TYR A 80 ? 0.2086 0.2264 0.2028 -0.0228 -0.0378 0.0100 101 TYR A CB 613 C CG . TYR A 80 ? 0.2612 0.2723 0.2592 -0.0188 -0.0438 0.0066 101 TYR A CG 614 C CD1 . TYR A 80 ? 0.1959 0.2192 0.1988 -0.0143 -0.0443 0.0016 101 TYR A CD1 615 C CD2 . TYR A 80 ? 0.2813 0.2745 0.2785 -0.0197 -0.0491 0.0088 101 TYR A CD2 616 C CE1 . TYR A 80 ? 0.2053 0.2248 0.2137 -0.0099 -0.0500 -0.0027 101 TYR A CE1 617 C CE2 . TYR A 80 ? 0.2718 0.2587 0.2732 -0.0148 -0.0558 0.0056 101 TYR A CE2 618 C CZ . TYR A 80 ? 0.2484 0.2493 0.2563 -0.0095 -0.0563 -0.0011 101 TYR A CZ 619 O OH . TYR A 80 ? 0.2489 0.2459 0.2630 -0.0039 -0.0632 -0.0055 101 TYR A OH 620 N N . GLU A 81 ? 0.2375 0.2364 0.2406 -0.0306 -0.0427 0.0069 102 GLU A N 621 C CA . GLU A 81 ? 0.2455 0.2278 0.2537 -0.0332 -0.0482 0.0063 102 GLU A CA 622 C C . GLU A 81 ? 0.2760 0.2629 0.2946 -0.0362 -0.0491 -0.0011 102 GLU A C 623 O O . GLU A 81 ? 0.3044 0.2800 0.3315 -0.0365 -0.0551 -0.0059 102 GLU A O 624 C CB . GLU A 81 ? 0.2513 0.2183 0.2511 -0.0394 -0.0467 0.0178 102 GLU A CB 625 C CG . GLU A 81 ? 0.2597 0.2212 0.2480 -0.0368 -0.0468 0.0248 102 GLU A CG 626 C CD . GLU A 81 ? 0.2918 0.2420 0.2818 -0.0313 -0.0549 0.0232 102 GLU A CD 627 O OE1 . GLU A 81 ? 0.2919 0.2344 0.2916 -0.0296 -0.0609 0.0177 102 GLU A OE1 628 O OE2 . GLU A 81 ? 0.2691 0.2183 0.2517 -0.0281 -0.0559 0.0267 102 GLU A OE2 629 N N . CYS A 82 ? 0.2458 0.2488 0.2649 -0.0379 -0.0441 -0.0027 103 CYS A N 630 C CA . CYS A 82 ? 0.2233 0.2311 0.2530 -0.0419 -0.0455 -0.0098 103 CYS A CA 631 C C . CYS A 82 ? 0.2368 0.2634 0.2726 -0.0366 -0.0473 -0.0222 103 CYS A C 632 O O . CYS A 82 ? 0.2670 0.2952 0.3132 -0.0384 -0.0512 -0.0313 103 CYS A O 633 C CB . CYS A 82 ? 0.1945 0.2068 0.2233 -0.0492 -0.0398 -0.0035 103 CYS A CB 634 S SG . CYS A 82 ? 0.2625 0.2571 0.2833 -0.0567 -0.0363 0.0107 103 CYS A SG 635 N N . SER A 83 ? 0.2309 0.2052 0.3499 -0.0089 -0.0654 0.0183 104 SER A N 636 C CA . SER A 83 ? 0.2219 0.1924 0.3327 -0.0153 -0.0795 0.0146 104 SER A CA 637 C C . SER A 83 ? 0.2180 0.1692 0.3069 -0.0211 -0.0887 0.0050 104 SER A C 638 O O . SER A 83 ? 0.2330 0.1755 0.3023 -0.0157 -0.0816 -0.0034 104 SER A O 639 C CB . SER A 83 ? 0.2562 0.2258 0.3493 -0.0103 -0.0761 0.0099 104 SER A CB 640 O OG . SER A 83 ? 0.2927 0.2558 0.3758 -0.0162 -0.0894 0.0069 104 SER A OG 641 N N . PRO A 84 ? 0.2319 0.1741 0.3216 -0.0318 -0.1048 0.0073 105 PRO A N 642 C CA . PRO A 84 ? 0.2629 0.1770 0.3189 -0.0349 -0.1117 -0.0018 105 PRO A CA 643 C C . PRO A 84 ? 0.3102 0.2158 0.3424 -0.0335 -0.1153 -0.0064 105 PRO A C 644 O O . PRO A 84 ? 0.3292 0.2108 0.3311 -0.0352 -0.1200 -0.0109 105 PRO A O 645 C CB . PRO A 84 ? 0.2691 0.1777 0.3307 -0.0453 -0.1227 0.0070 105 PRO A CB 646 C CG . PRO A 84 ? 0.2790 0.2130 0.3733 -0.0489 -0.1275 0.0200 105 PRO A CG 647 C CD . PRO A 84 ? 0.2348 0.1913 0.3524 -0.0398 -0.1151 0.0210 105 PRO A CD 648 N N . ASN A 85 ? 0.2719 0.1936 0.3143 -0.0301 -0.1123 -0.0051 106 ASN A N 649 C CA . ASN A 85 ? 0.2783 0.1920 0.3000 -0.0298 -0.1158 -0.0075 106 ASN A CA 650 C C . ASN A 85 ? 0.2899 0.2044 0.2953 -0.0232 -0.1061 -0.0154 106 ASN A C 651 O O . ASN A 85 ? 0.2940 0.2090 0.2911 -0.0228 -0.1069 -0.0150 106 ASN A O 652 C CB . ASN A 85 ? 0.2141 0.1418 0.2579 -0.0335 -0.1241 0.0034 106 ASN A CB 653 C CG . ASN A 85 ? 0.2686 0.1958 0.3270 -0.0425 -0.1355 0.0135 106 ASN A CG 654 O OD1 . ASN A 85 ? 0.2894 0.1938 0.3241 -0.0479 -0.1426 0.0107 106 ASN A OD1 655 N ND2 . ASN A 85 ? 0.2532 0.2048 0.3495 -0.0439 -0.1365 0.0265 106 ASN A ND2 656 N N . LEU A 86 ? 0.2949 0.2109 0.2955 -0.0175 -0.0951 -0.0206 107 LEU A N 657 C CA . LEU A 86 ? 0.2665 0.1906 0.2563 -0.0120 -0.0836 -0.0237 107 LEU A CA 658 C C . LEU A 86 ? 0.2880 0.2012 0.2546 -0.0067 -0.0765 -0.0300 107 LEU A C 659 O O . LEU A 86 ? 0.2814 0.2067 0.2443 -0.0026 -0.0661 -0.0301 107 LEU A O 660 C CB . LEU A 86 ? 0.2299 0.1726 0.2374 -0.0085 -0.0736 -0.0194 107 LEU A CB 661 C CG . LEU A 86 ? 0.2547 0.2058 0.2808 -0.0092 -0.0746 -0.0118 107 LEU A CG 662 C CD1 . LEU A 86 ? 0.2519 0.2106 0.2850 -0.0049 -0.0636 -0.0082 107 LEU A CD1 663 C CD2 . LEU A 86 ? 0.2320 0.1809 0.2483 -0.0104 -0.0779 -0.0108 107 LEU A CD2 664 N N . GLY A 87 ? 0.2751 0.1644 0.2250 -0.0067 -0.0820 -0.0335 108 GLY A N 665 C CA . GLY A 87 ? 0.3240 0.1955 0.2456 0.0019 -0.0735 -0.0385 108 GLY A CA 666 C C . GLY A 87 ? 0.3596 0.2356 0.2658 0.0062 -0.0642 -0.0397 108 GLY A C 667 O O . GLY A 87 ? 0.3597 0.2481 0.2652 0.0154 -0.0499 -0.0383 108 GLY A O 668 N N . PRO A 88 ? 0.3553 0.2233 0.2509 -0.0007 -0.0722 -0.0407 109 PRO A N 669 C CA . PRO A 88 ? 0.3476 0.2149 0.2241 0.0021 -0.0635 -0.0417 109 PRO A CA 670 C C . PRO A 88 ? 0.3278 0.2300 0.2249 0.0032 -0.0516 -0.0365 109 PRO A C 671 O O . PRO A 88 ? 0.3281 0.2349 0.2133 0.0058 -0.0415 -0.0350 109 PRO A O 672 C CB . PRO A 88 ? 0.3409 0.1959 0.2087 -0.0074 -0.0777 -0.0425 109 PRO A CB 673 C CG . PRO A 88 ? 0.3426 0.1882 0.2194 -0.0117 -0.0892 -0.0391 109 PRO A CG 674 C CD . PRO A 88 ? 0.3134 0.1721 0.2138 -0.0107 -0.0893 -0.0389 109 PRO A CD 675 N N . TRP A 89 ? 0.2921 0.2158 0.2170 0.0002 -0.0533 -0.0327 110 TRP A N 676 C CA . TRP A 89 ? 0.2593 0.2098 0.1988 -0.0023 -0.0465 -0.0270 110 TRP A CA 677 C C . TRP A 89 ? 0.2620 0.2313 0.2189 0.0036 -0.0391 -0.0229 110 TRP A C 678 O O . TRP A 89 ? 0.2524 0.2432 0.2215 -0.0002 -0.0362 -0.0168 110 TRP A O 679 C CB . TRP A 89 ? 0.2288 0.1818 0.1765 -0.0104 -0.0541 -0.0249 110 TRP A CB 680 C CG . TRP A 89 ? 0.2665 0.2031 0.1968 -0.0144 -0.0608 -0.0274 110 TRP A CG 681 C CD1 . TRP A 89 ? 0.2953 0.2293 0.2078 -0.0184 -0.0580 -0.0272 110 TRP A CD1 682 C CD2 . TRP A 89 ? 0.2696 0.1898 0.1980 -0.0153 -0.0723 -0.0295 110 TRP A CD2 683 N NE1 . TRP A 89 ? 0.3251 0.2392 0.2219 -0.0205 -0.0669 -0.0301 110 TRP A NE1 684 C CE2 . TRP A 89 ? 0.3095 0.2176 0.2187 -0.0185 -0.0755 -0.0304 110 TRP A CE2 685 C CE3 . TRP A 89 ? 0.3021 0.2188 0.2456 -0.0148 -0.0803 -0.0287 110 TRP A CE3 686 C CZ2 . TRP A 89 ? 0.3170 0.2157 0.2274 -0.0189 -0.0830 -0.0278 110 TRP A CZ2 687 C CZ3 . TRP A 89 ? 0.3416 0.2489 0.2856 -0.0175 -0.0902 -0.0259 110 TRP A CZ3 688 C CH2 . TRP A 89 ? 0.3420 0.2411 0.2700 -0.0188 -0.0912 -0.0252 110 TRP A CH2 689 N N . ILE A 90 ? 0.2491 0.2070 0.2037 0.0121 -0.0374 -0.0258 111 ILE A N 690 C CA . ILE A 90 ? 0.2535 0.2265 0.2223 0.0198 -0.0305 -0.0218 111 ILE A CA 691 C C . ILE A 90 ? 0.2821 0.2767 0.2529 0.0269 -0.0178 -0.0150 111 ILE A C 692 O O . ILE A 90 ? 0.3338 0.3183 0.2860 0.0337 -0.0100 -0.0162 111 ILE A O 693 C CB . ILE A 90 ? 0.2776 0.2268 0.2370 0.0278 -0.0313 -0.0264 111 ILE A CB 694 C CG1 . ILE A 90 ? 0.2653 0.2055 0.2354 0.0196 -0.0428 -0.0282 111 ILE A CG1 695 C CG2 . ILE A 90 ? 0.2789 0.2405 0.2453 0.0407 -0.0207 -0.0218 111 ILE A CG2 696 C CD1 . ILE A 90 ? 0.2211 0.1337 0.1798 0.0227 -0.0469 -0.0320 111 ILE A CD1 697 N N . GLN A 91 ? 0.2405 0.2645 0.2332 0.0253 -0.0160 -0.0065 112 GLN A N 698 C CA . GLN A 91 ? 0.2553 0.3088 0.2598 0.0324 -0.0048 0.0041 112 GLN A CA 699 C C . GLN A 91 ? 0.2428 0.3130 0.2658 0.0421 -0.0019 0.0106 112 GLN A C 700 O O . GLN A 91 ? 0.2168 0.2818 0.2463 0.0376 -0.0106 0.0086 112 GLN A O 701 C CB . GLN A 91 ? 0.2751 0.3545 0.2910 0.0172 -0.0084 0.0129 112 GLN A CB 702 C CG . GLN A 91 ? 0.3132 0.3777 0.3099 0.0077 -0.0105 0.0081 112 GLN A CG 703 C CD . GLN A 91 ? 0.3768 0.4467 0.3645 0.0157 0.0035 0.0118 112 GLN A CD 704 O OE1 . GLN A 91 ? 0.3662 0.4694 0.3715 0.0177 0.0128 0.0248 112 GLN A OE1 705 N NE2 . GLN A 91 ? 0.4011 0.4380 0.3610 0.0202 0.0050 0.0019 112 GLN A NE2 706 N N . GLN A 92 ? 0.2211 0.3123 0.2526 0.0562 0.0112 0.0200 113 GLN A N 707 C CA . GLN A 92 ? 0.2755 0.3875 0.3270 0.0670 0.0141 0.0291 113 GLN A CA 708 C C . GLN A 92 ? 0.2633 0.4124 0.3425 0.0520 0.0042 0.0417 113 GLN A C 709 O O . GLN A 92 ? 0.2740 0.4438 0.3607 0.0393 0.0025 0.0489 113 GLN A O 710 C CB . GLN A 92 ? 0.3895 0.5135 0.4416 0.0897 0.0334 0.0377 113 GLN A CB 711 C CG . GLN A 92 ? 0.5002 0.5783 0.5130 0.1023 0.0429 0.0255 113 GLN A CG 712 C CD . GLN A 92 ? 0.5655 0.6013 0.5565 0.1063 0.0360 0.0130 113 GLN A CD 713 O OE1 . GLN A 92 ? 0.6295 0.6622 0.6210 0.1220 0.0418 0.0162 113 GLN A OE1 714 N NE2 . GLN A 92 ? 0.5272 0.5316 0.5004 0.0916 0.0231 0.0002 113 GLN A NE2 715 N N . VAL A 93 ? 0.2178 0.3715 0.3084 0.0522 -0.0035 0.0448 114 VAL A N 716 C CA . VAL A 93 ? 0.1929 0.3743 0.3030 0.0364 -0.0161 0.0571 114 VAL A CA 717 C C . VAL A 93 ? 0.2230 0.4236 0.3522 0.0467 -0.0178 0.0677 114 VAL A C 718 O O . VAL A 93 ? 0.2206 0.4008 0.3414 0.0627 -0.0125 0.0608 114 VAL A O 719 C CB . VAL A 93 ? 0.2003 0.3546 0.2931 0.0165 -0.0307 0.0484 114 VAL A CB 720 C CG1 . VAL A 93 ? 0.2147 0.3412 0.2981 0.0217 -0.0343 0.0398 114 VAL A CG1 721 C CG2 . VAL A 93 ? 0.2338 0.4085 0.3351 -0.0034 -0.0440 0.0613 114 VAL A CG2 722 N N . ASN A 94 ? 0.2430 0.4824 0.3972 0.0370 -0.0261 0.0856 115 ASN A N 723 C CA . ASN A 94 ? 0.3226 0.5761 0.4918 0.0427 -0.0313 0.0958 115 ASN A CA 724 C C . ASN A 94 ? 0.3366 0.5679 0.4923 0.0244 -0.0505 0.0928 115 ASN A C 725 O O . ASN A 94 ? 0.3626 0.5993 0.5173 0.0033 -0.0627 0.1006 115 ASN A O 726 C CB . ASN A 94 ? 0.3971 0.6885 0.5895 0.0396 -0.0284 0.1141 115 ASN A CB 727 C CG . ASN A 94 ? 0.4802 0.7904 0.6826 0.0605 -0.0065 0.1193 115 ASN A CG 728 O OD1 . ASN A 94 ? 0.4952 0.7886 0.6875 0.0845 0.0075 0.1121 115 ASN A OD1 729 N ND2 . ASN A 94 ? 0.5545 0.8934 0.7709 0.0516 -0.0028 0.1319 115 ASN A ND2 730 N N . GLN A 95 ? 0.2969 0.4952 0.4356 0.0322 -0.0513 0.0808 116 GLN A N 731 C CA . GLN A 95 ? 0.2920 0.4642 0.4137 0.0188 -0.0662 0.0785 116 GLN A CA 732 C C . GLN A 95 ? 0.2982 0.4512 0.4143 0.0342 -0.0635 0.0740 116 GLN A C 733 O O . GLN A 95 ? 0.3074 0.4506 0.4216 0.0524 -0.0500 0.0661 116 GLN A O 734 C CB . GLN A 95 ? 0.2780 0.4124 0.3714 0.0052 -0.0683 0.0647 116 GLN A CB 735 C CG . GLN A 95 ? 0.2978 0.4417 0.3874 -0.0153 -0.0767 0.0707 116 GLN A CG 736 C CD . GLN A 95 ? 0.3008 0.4047 0.3595 -0.0258 -0.0780 0.0585 116 GLN A CD 737 O OE1 . GLN A 95 ? 0.2793 0.3698 0.3326 -0.0184 -0.0676 0.0468 116 GLN A OE1 738 N NE2 . GLN A 95 ? 0.3405 0.4234 0.3766 -0.0428 -0.0913 0.0626 116 GLN A NE2 739 N N . SER A 96 ? 0.2892 0.4307 0.3970 0.0258 -0.0770 0.0790 117 SER A N 740 C CA . SER A 96 ? 0.3012 0.4271 0.4045 0.0401 -0.0754 0.0775 117 SER A CA 741 C C . SER A 96 ? 0.3076 0.3891 0.3866 0.0450 -0.0662 0.0597 117 SER A C 742 O O . SER A 96 ? 0.3121 0.3797 0.3874 0.0599 -0.0596 0.0558 117 SER A O 743 C CB . SER A 96 ? 0.3045 0.4246 0.3998 0.0285 -0.0925 0.0870 117 SER A CB 744 O OG . SER A 96 ? 0.3374 0.4184 0.4016 0.0122 -0.1001 0.0801 117 SER A OG 745 N N . TRP A 97 ? 0.3014 0.3619 0.3649 0.0325 -0.0657 0.0506 118 TRP A N 746 C CA . TRP A 97 ? 0.3014 0.3240 0.3463 0.0342 -0.0588 0.0378 118 TRP A CA 747 C C . TRP A 97 ? 0.2961 0.3142 0.3425 0.0372 -0.0489 0.0275 118 TRP A C 748 O O . TRP A 97 ? 0.2978 0.2906 0.3346 0.0370 -0.0443 0.0194 118 TRP A O 749 C CB . TRP A 97 ? 0.3169 0.3112 0.3387 0.0203 -0.0651 0.0373 118 TRP A CB 750 C CG . TRP A 97 ? 0.3094 0.3109 0.3256 0.0049 -0.0724 0.0412 118 TRP A CG 751 C CD1 . TRP A 97 ? 0.3224 0.3426 0.3410 -0.0067 -0.0859 0.0531 118 TRP A CD1 752 C CD2 . TRP A 97 ? 0.2858 0.2760 0.2928 -0.0014 -0.0679 0.0346 118 TRP A CD2 753 N NE1 . TRP A 97 ? 0.3291 0.3468 0.3371 -0.0209 -0.0898 0.0534 118 TRP A NE1 754 C CE2 . TRP A 97 ? 0.3233 0.3217 0.3229 -0.0165 -0.0783 0.0417 118 TRP A CE2 755 C CE3 . TRP A 97 ? 0.2864 0.2612 0.2914 0.0036 -0.0575 0.0249 118 TRP A CE3 756 C CZ2 . TRP A 97 ? 0.3293 0.3166 0.3154 -0.0250 -0.0769 0.0379 118 TRP A CZ2 757 C CZ3 . TRP A 97 ? 0.2994 0.2673 0.2950 -0.0039 -0.0566 0.0222 118 TRP A CZ3 758 C CH2 . TRP A 97 ? 0.3191 0.2915 0.3036 -0.0171 -0.0655 0.0280 118 TRP A CH2 759 N N . ARG A 98 ? 0.2728 0.3156 0.3313 0.0393 -0.0460 0.0292 119 ARG A N 760 C CA . ARG A 98 ? 0.2172 0.2529 0.2734 0.0441 -0.0377 0.0201 119 ARG A CA 761 C C . ARG A 98 ? 0.2258 0.2885 0.2933 0.0528 -0.0319 0.0252 119 ARG A C 762 O O . ARG A 98 ? 0.2273 0.3203 0.3094 0.0500 -0.0354 0.0369 119 ARG A O 763 C CB . ARG A 98 ? 0.2292 0.2531 0.2772 0.0311 -0.0399 0.0144 119 ARG A CB 764 C CG . ARG A 98 ? 0.2262 0.2669 0.2752 0.0187 -0.0458 0.0206 119 ARG A CG 765 C CD . ARG A 98 ? 0.2522 0.2760 0.2886 0.0088 -0.0468 0.0149 119 ARG A CD 766 N NE . ARG A 98 ? 0.2756 0.3092 0.3066 -0.0043 -0.0534 0.0213 119 ARG A NE 767 C CZ . ARG A 98 ? 0.2728 0.2893 0.2870 -0.0139 -0.0559 0.0192 119 ARG A CZ 768 N NH1 . ARG A 98 ? 0.2268 0.2208 0.2334 -0.0104 -0.0514 0.0123 119 ARG A NH1 769 N NH2 . ARG A 98 ? 0.2281 0.2502 0.2333 -0.0273 -0.0632 0.0258 119 ARG A NH2 770 N N . LYS A 99 ? 0.2278 0.2781 0.2869 0.0631 -0.0230 0.0181 120 LYS A N 771 C CA . LYS A 99 ? 0.2136 0.2819 0.2766 0.0748 -0.0131 0.0225 120 LYS A CA 772 C C . LYS A 99 ? 0.2259 0.2945 0.2830 0.0657 -0.0121 0.0182 120 LYS A C 773 O O . LYS A 99 ? 0.2496 0.3365 0.3107 0.0716 -0.0040 0.0237 120 LYS A O 774 C CB . LYS A 99 ? 0.2370 0.2808 0.2831 0.0944 -0.0030 0.0176 120 LYS A CB 775 N N . GLU A 100 ? 0.2280 0.2761 0.2755 0.0524 -0.0194 0.0096 121 GLU A N 776 C CA . GLU A 100 ? 0.2602 0.3044 0.2996 0.0437 -0.0201 0.0052 121 GLU A CA 777 C C . GLU A 100 ? 0.2531 0.2927 0.2922 0.0275 -0.0295 0.0038 121 GLU A C 778 O O . GLU A 100 ? 0.2470 0.2772 0.2874 0.0240 -0.0341 0.0037 121 GLU A O 779 C CB . GLU A 100 ? 0.2844 0.2974 0.3038 0.0488 -0.0178 -0.0051 121 GLU A CB 780 C CG . GLU A 100 ? 0.3158 0.3199 0.3225 0.0669 -0.0068 -0.0050 121 GLU A CG 781 C CD . GLU A 100 ? 0.3486 0.3114 0.3265 0.0692 -0.0080 -0.0151 121 GLU A CD 782 O OE1 . GLU A 100 ? 0.3897 0.3388 0.3465 0.0803 0.0011 -0.0161 121 GLU A OE1 783 O OE2 . GLU A 100 ? 0.3620 0.3047 0.3368 0.0599 -0.0179 -0.0207 121 GLU A OE2 784 N N . ARG A 101 ? 0.2336 0.2758 0.2672 0.0189 -0.0309 0.0031 122 ARG A N 785 C CA . ARG A 101 ? 0.2697 0.3005 0.2966 0.0065 -0.0379 0.0013 122 ARG A CA 786 C C . ARG A 101 ? 0.2655 0.2885 0.2812 0.0028 -0.0379 -0.0034 122 ARG A C 787 O O . ARG A 101 ? 0.2701 0.2927 0.2809 0.0093 -0.0328 -0.0061 122 ARG A O 788 C CB . ARG A 101 ? 0.3369 0.3804 0.3652 -0.0041 -0.0433 0.0100 122 ARG A CB 789 C CG . ARG A 101 ? 0.4451 0.5127 0.4773 -0.0104 -0.0426 0.0174 122 ARG A CG 790 C CD . ARG A 101 ? 0.5492 0.6226 0.5775 -0.0261 -0.0523 0.0267 122 ARG A CD 791 N NE . ARG A 101 ? 0.6446 0.7307 0.6692 -0.0384 -0.0542 0.0326 122 ARG A NE 792 C CZ . ARG A 101 ? 0.7111 0.7760 0.7136 -0.0487 -0.0578 0.0289 122 ARG A CZ 793 N NH1 . ARG A 101 ? 0.7287 0.8047 0.7268 -0.0609 -0.0597 0.0352 122 ARG A NH1 794 N NH2 . ARG A 101 ? 0.7418 0.7750 0.7271 -0.0462 -0.0588 0.0202 122 ARG A NH2 795 N N . PHE A 102 ? 0.2436 0.2564 0.2510 -0.0064 -0.0430 -0.0041 123 PHE A N 796 C CA . PHE A 102 ? 0.2606 0.2634 0.2560 -0.0095 -0.0444 -0.0083 123 PHE A CA 797 C C . PHE A 102 ? 0.2553 0.2659 0.2417 -0.0196 -0.0455 -0.0035 123 PHE A C 798 O O . PHE A 102 ? 0.2280 0.2416 0.2126 -0.0272 -0.0488 0.0023 123 PHE A O 799 C CB . PHE A 102 ? 0.3151 0.2996 0.3074 -0.0108 -0.0489 -0.0110 123 PHE A CB 800 C CG . PHE A 102 ? 0.3124 0.2903 0.3163 -0.0047 -0.0493 -0.0132 123 PHE A CG 801 C CD1 . PHE A 102 ? 0.3120 0.2849 0.3229 -0.0039 -0.0487 -0.0100 123 PHE A CD1 802 C CD2 . PHE A 102 ? 0.3103 0.2833 0.3141 -0.0001 -0.0499 -0.0176 123 PHE A CD2 803 C CE1 . PHE A 102 ? 0.3362 0.3048 0.3597 0.0001 -0.0487 -0.0103 123 PHE A CE1 804 C CE2 . PHE A 102 ? 0.3499 0.3140 0.3620 0.0025 -0.0522 -0.0186 123 PHE A CE2 805 C CZ . PHE A 102 ? 0.3459 0.3108 0.3709 0.0020 -0.0516 -0.0146 123 PHE A CZ 806 N N . LEU A 103 ? 0.2593 0.2680 0.2354 -0.0210 -0.0438 -0.0056 124 LEU A N 807 C CA . LEU A 103 ? 0.2242 0.2373 0.1886 -0.0322 -0.0448 -0.0010 124 LEU A CA 808 C C . LEU A 103 ? 0.2115 0.2038 0.1564 -0.0341 -0.0472 -0.0066 124 LEU A C 809 O O . LEU A 103 ? 0.2049 0.1895 0.1458 -0.0270 -0.0453 -0.0122 124 LEU A O 810 C CB . LEU A 103 ? 0.2032 0.2430 0.1774 -0.0317 -0.0373 0.0061 124 LEU A CB 811 C CG . LEU A 103 ? 0.2084 0.2581 0.1742 -0.0456 -0.0376 0.0137 124 LEU A CG 812 C CD1 . LEU A 103 ? 0.1854 0.2382 0.1498 -0.0611 -0.0472 0.0217 124 LEU A CD1 813 C CD2 . LEU A 103 ? 0.1995 0.2792 0.1796 -0.0414 -0.0262 0.0225 124 LEU A CD2 814 N N . ASP A 104 ? 0.2130 0.1923 0.1412 -0.0435 -0.0521 -0.0047 125 ASP A N 815 C CA . ASP A 104 ? 0.2367 0.1966 0.1439 -0.0457 -0.0546 -0.0084 125 ASP A CA 816 C C . ASP A 104 ? 0.2531 0.1976 0.1620 -0.0360 -0.0585 -0.0147 125 ASP A C 817 O O . ASP A 104 ? 0.2441 0.1773 0.1406 -0.0350 -0.0606 -0.0182 125 ASP A O 818 C CB . ASP A 104 ? 0.2112 0.1793 0.1102 -0.0498 -0.0497 -0.0071 125 ASP A CB 819 C CG . ASP A 104 ? 0.3073 0.2875 0.2007 -0.0649 -0.0494 0.0023 125 ASP A CG 820 O OD1 . ASP A 104 ? 0.2630 0.2258 0.1410 -0.0729 -0.0542 0.0045 125 ASP A OD1 821 O OD2 . ASP A 104 ? 0.2921 0.2986 0.1987 -0.0670 -0.0426 0.0090 125 ASP A OD2 822 N N . VAL A 105 ? 0.2274 0.1727 0.1526 -0.0299 -0.0597 -0.0146 126 VAL A N 823 C CA . VAL A 105 ? 0.2233 0.1586 0.1551 -0.0236 -0.0649 -0.0162 126 VAL A CA 824 C C . VAL A 105 ? 0.2236 0.1424 0.1381 -0.0244 -0.0684 -0.0141 126 VAL A C 825 O O . VAL A 105 ? 0.2090 0.1189 0.1108 -0.0262 -0.0655 -0.0104 126 VAL A O 826 C CB . VAL A 105 ? 0.2030 0.1441 0.1563 -0.0181 -0.0633 -0.0135 126 VAL A CB 827 C CG1 . VAL A 105 ? 0.2558 0.1926 0.2224 -0.0128 -0.0686 -0.0108 126 VAL A CG1 828 C CG2 . VAL A 105 ? 0.2059 0.1585 0.1722 -0.0160 -0.0610 -0.0161 126 VAL A CG2 829 N N . PRO A 106 ? 0.2244 0.1363 0.1356 -0.0223 -0.0734 -0.0155 127 PRO A N 830 C CA . PRO A 106 ? 0.2306 0.1276 0.1258 -0.0211 -0.0756 -0.0127 127 PRO A CA 831 C C . PRO A 106 ? 0.2791 0.1721 0.1847 -0.0126 -0.0791 -0.0067 127 PRO A C 832 O O . PRO A 106 ? 0.2852 0.1822 0.2067 -0.0080 -0.0868 -0.0036 127 PRO A O 833 C CB . PRO A 106 ? 0.2343 0.1284 0.1276 -0.0208 -0.0794 -0.0148 127 PRO A CB 834 C CG . PRO A 106 ? 0.2264 0.1285 0.1373 -0.0197 -0.0839 -0.0172 127 PRO A CG 835 C CD . PRO A 106 ? 0.2251 0.1389 0.1433 -0.0209 -0.0772 -0.0191 127 PRO A CD 836 N N . LEU A 107 ? 0.2743 0.1610 0.1730 -0.0099 -0.0710 -0.0028 128 LEU A N 837 C CA . LEU A 107 ? 0.3236 0.2058 0.2309 0.0021 -0.0662 0.0056 128 LEU A CA 838 C C . LEU A 107 ? 0.3281 0.1934 0.2178 0.0093 -0.0681 0.0102 128 LEU A C 839 O O . LEU A 107 ? 0.3498 0.1929 0.2040 0.0047 -0.0680 0.0076 128 LEU A O 840 C CB . LEU A 107 ? 0.3377 0.2071 0.2295 0.0029 -0.0561 0.0078 128 LEU A CB 841 C CG . LEU A 107 ? 0.3505 0.2103 0.2456 0.0181 -0.0462 0.0173 128 LEU A CG 842 C CD1 . LEU A 107 ? 0.2978 0.1856 0.2389 0.0253 -0.0456 0.0226 128 LEU A CD1 843 C CD2 . LEU A 107 ? 0.3423 0.1784 0.2089 0.0168 -0.0376 0.0181 128 LEU A CD2 844 N N . CYS A 108 ? 0.3413 0.2181 0.2570 0.0203 -0.0706 0.0186 129 CYS A N 845 C CA . CYS A 108 ? 0.3201 0.1850 0.2249 0.0304 -0.0729 0.0256 129 CYS A CA 846 C C . CYS A 108 ? 0.3006 0.1337 0.1672 0.0390 -0.0599 0.0288 129 CYS A C 847 O O . CYS A 108 ? 0.3027 0.1304 0.1685 0.0454 -0.0479 0.0326 129 CYS A O 848 C CB . CYS A 108 ? 0.3054 0.1956 0.2537 0.0421 -0.0762 0.0389 129 CYS A CB 849 S SG . CYS A 108 ? 0.3464 0.2651 0.3329 0.0293 -0.0967 0.0375 129 CYS A SG 850 N N . LYS A 109 ? 0.3345 0.3217 0.1373 -0.0091 -0.0257 0.0183 130 LYS A N 851 C CA . LYS A 109 ? 0.3250 0.2982 0.1445 0.0005 -0.0224 0.0370 130 LYS A CA 852 C C . LYS A 109 ? 0.2976 0.2831 0.1535 0.0105 -0.0375 0.0402 130 LYS A C 853 O O . LYS A 109 ? 0.2595 0.2389 0.1446 0.0130 -0.0300 0.0425 130 LYS A O 854 C CB . LYS A 109 ? 0.3723 0.3257 0.1505 0.0039 -0.0212 0.0584 130 LYS A CB 855 C CG . LYS A 109 ? 0.4196 0.3850 0.1619 0.0109 -0.0441 0.0682 130 LYS A CG 856 C CD . LYS A 109 ? 0.5228 0.4610 0.2136 0.0130 -0.0371 0.0923 130 LYS A CD 857 C CE . LYS A 109 ? 0.5447 0.5090 0.2212 0.0234 -0.0619 0.1074 130 LYS A CE 858 N NZ . LYS A 109 ? 0.6138 0.5588 0.2531 0.0224 -0.0519 0.1304 130 LYS A NZ 859 N N . GLU A 110 ? 0.3053 0.3138 0.1613 0.0146 -0.0580 0.0371 131 GLU A N 860 C CA . GLU A 110 ? 0.3083 0.3330 0.2035 0.0235 -0.0695 0.0369 131 GLU A CA 861 C C . GLU A 110 ? 0.2628 0.2902 0.1932 0.0154 -0.0584 0.0217 131 GLU A C 862 O O . GLU A 110 ? 0.2529 0.2802 0.2114 0.0205 -0.0567 0.0245 131 GLU A O 863 C CB . GLU A 110 ? 0.3565 0.4160 0.2523 0.0295 -0.0940 0.0341 131 GLU A CB 864 C CG . GLU A 110 ? 0.4800 0.5377 0.3405 0.0449 -0.1090 0.0572 131 GLU A CG 865 C CD . GLU A 110 ? 0.5696 0.6313 0.3773 0.0340 -0.1123 0.0542 131 GLU A CD 866 O OE1 . GLU A 110 ? 0.5597 0.6183 0.3588 0.0146 -0.0976 0.0333 131 GLU A OE1 867 O OE2 . GLU A 110 ? 0.6153 0.6724 0.3978 0.0405 -0.1248 0.0703 131 GLU A OE2 868 N N . ASP A 111 ? 0.2359 0.2622 0.1621 0.0032 -0.0490 0.0062 132 ASP A N 869 C CA . ASP A 111 ? 0.2057 0.2270 0.1586 -0.0012 -0.0371 -0.0018 132 ASP A CA 870 C C . ASP A 111 ? 0.2474 0.2553 0.2097 0.0043 -0.0258 0.0090 132 ASP A C 871 O O . ASP A 111 ? 0.2398 0.2510 0.2242 0.0057 -0.0237 0.0100 132 ASP A O 872 C CB . ASP A 111 ? 0.2265 0.2387 0.1722 -0.0125 -0.0248 -0.0180 132 ASP A CB 873 C CG . ASP A 111 ? 0.2731 0.3029 0.2237 -0.0246 -0.0321 -0.0362 132 ASP A CG 874 O OD1 . ASP A 111 ? 0.2811 0.3373 0.2455 -0.0215 -0.0488 -0.0349 132 ASP A OD1 875 O OD2 . ASP A 111 ? 0.3190 0.3375 0.2632 -0.0376 -0.0195 -0.0536 132 ASP A OD2 876 N N . CYS A 112 ? 0.2267 0.2239 0.1714 0.0050 -0.0180 0.0151 133 CYS A N 877 C CA . CYS A 112 ? 0.2152 0.2093 0.1724 0.0069 -0.0080 0.0213 133 CYS A CA 878 C C . CYS A 112 ? 0.2187 0.2126 0.1865 0.0101 -0.0138 0.0291 133 CYS A C 879 O O . CYS A 112 ? 0.2036 0.2047 0.1925 0.0092 -0.0109 0.0272 133 CYS A O 880 C CB . CYS A 112 ? 0.2346 0.2204 0.1742 0.0035 0.0051 0.0231 133 CYS A CB 881 S SG . CYS A 112 ? 0.3684 0.3642 0.3330 0.0017 0.0170 0.0246 133 CYS A SG 882 N N . GLN A 113 ? 0.1955 0.1804 0.1470 0.0146 -0.0210 0.0378 134 GLN A N 883 C CA . GLN A 113 ? 0.2480 0.2246 0.2111 0.0210 -0.0232 0.0455 134 GLN A CA 884 C C . GLN A 113 ? 0.3228 0.3162 0.3174 0.0229 -0.0285 0.0367 134 GLN A C 885 O O . GLN A 113 ? 0.2897 0.2802 0.3015 0.0206 -0.0208 0.0337 134 GLN A O 886 C CB . GLN A 113 ? 0.2356 0.2017 0.1779 0.0326 -0.0340 0.0599 134 GLN A CB 887 C CG . GLN A 113 ? 0.3801 0.3253 0.3337 0.0432 -0.0308 0.0711 134 GLN A CG 888 C CD . GLN A 113 ? 0.4412 0.3522 0.3805 0.0346 -0.0095 0.0781 134 GLN A CD 889 O OE1 . GLN A 113 ? 0.4872 0.3872 0.3967 0.0273 -0.0018 0.0836 134 GLN A OE1 890 N NE2 . GLN A 113 ? 0.4168 0.3119 0.3778 0.0324 0.0031 0.0744 134 GLN A NE2 891 N N . ARG A 114 ? 0.2511 0.2627 0.2518 0.0241 -0.0394 0.0299 135 ARG A N 892 C CA . ARG A 114 ? 0.2193 0.2476 0.2484 0.0236 -0.0416 0.0205 135 ARG A CA 893 C C . ARG A 114 ? 0.2289 0.2572 0.2658 0.0144 -0.0298 0.0146 135 ARG A C 894 O O . ARG A 114 ? 0.2278 0.2617 0.2815 0.0125 -0.0254 0.0097 135 ARG A O 895 C CB . ARG A 114 ? 0.1896 0.2398 0.2241 0.0211 -0.0520 0.0108 135 ARG A CB 896 C CG . ARG A 114 ? 0.1894 0.2587 0.2540 0.0161 -0.0499 -0.0017 135 ARG A CG 897 C CD . ARG A 114 ? 0.1937 0.2740 0.2853 0.0280 -0.0534 -0.0009 135 ARG A CD 898 N NE . ARG A 114 ? 0.1905 0.2942 0.3121 0.0210 -0.0489 -0.0163 135 ARG A NE 899 C CZ . ARG A 114 ? 0.2134 0.3512 0.3597 0.0222 -0.0587 -0.0269 135 ARG A CZ 900 N NH1 . ARG A 114 ? 0.1997 0.3556 0.3418 0.0326 -0.0779 -0.0224 135 ARG A NH1 901 N NH2 . ARG A 114 ? 0.2079 0.3662 0.3828 0.0120 -0.0491 -0.0430 135 ARG A NH2 902 N N . TRP A 115 ? 0.2207 0.2441 0.2444 0.0101 -0.0245 0.0153 136 TRP A N 903 C CA . TRP A 115 ? 0.1739 0.2004 0.2015 0.0065 -0.0167 0.0148 136 TRP A CA 904 C C . TRP A 115 ? 0.1782 0.2094 0.2116 0.0046 -0.0127 0.0158 136 TRP A C 905 O O . TRP A 115 ? 0.1794 0.2213 0.2206 0.0003 -0.0104 0.0119 136 TRP A O 906 C CB . TRP A 115 ? 0.1816 0.2014 0.1979 0.0082 -0.0115 0.0173 136 TRP A CB 907 C CG . TRP A 115 ? 0.1842 0.2078 0.2044 0.0112 -0.0057 0.0215 136 TRP A CG 908 C CD1 . TRP A 115 ? 0.1804 0.2159 0.2060 0.0104 -0.0063 0.0243 136 TRP A CD1 909 C CD2 . TRP A 115 ? 0.1774 0.1933 0.1945 0.0182 0.0016 0.0247 136 TRP A CD2 910 N NE1 . TRP A 115 ? 0.2204 0.2579 0.2439 0.0187 -0.0031 0.0331 136 TRP A NE1 911 C CE2 . TRP A 115 ? 0.1791 0.2030 0.2010 0.0252 0.0026 0.0336 136 TRP A CE2 912 C CE3 . TRP A 115 ? 0.2078 0.2106 0.2176 0.0199 0.0085 0.0205 136 TRP A CE3 913 C CZ2 . TRP A 115 ? 0.1628 0.1809 0.1872 0.0388 0.0095 0.0416 136 TRP A CZ2 914 C CZ3 . TRP A 115 ? 0.2321 0.2269 0.2464 0.0304 0.0190 0.0237 136 TRP A CZ3 915 C CH2 . TRP A 115 ? 0.2050 0.2069 0.2288 0.0419 0.0188 0.0358 136 TRP A CH2 916 N N . TRP A 116 ? 0.1489 0.1718 0.1757 0.0046 -0.0096 0.0192 137 TRP A N 917 C CA . TRP A 116 ? 0.2005 0.2267 0.2343 -0.0024 -0.0020 0.0158 137 TRP A CA 918 C C . TRP A 116 ? 0.2194 0.2410 0.2645 -0.0045 -0.0002 0.0098 137 TRP A C 919 O O . TRP A 116 ? 0.1930 0.2280 0.2465 -0.0134 0.0046 0.0002 137 TRP A O 920 C CB . TRP A 116 ? 0.2258 0.2358 0.2487 -0.0049 0.0058 0.0203 137 TRP A CB 921 C CG . TRP A 116 ? 0.2458 0.2570 0.2769 -0.0173 0.0182 0.0134 137 TRP A CG 922 C CD1 . TRP A 116 ? 0.2128 0.2523 0.2556 -0.0271 0.0233 0.0047 137 TRP A CD1 923 C CD2 . TRP A 116 ? 0.2683 0.2508 0.2977 -0.0223 0.0292 0.0134 137 TRP A CD2 924 N NE1 . TRP A 116 ? 0.2050 0.2388 0.2543 -0.0429 0.0374 -0.0048 137 TRP A NE1 925 C CE2 . TRP A 116 ? 0.2897 0.2822 0.3293 -0.0405 0.0434 0.0008 137 TRP A CE2 926 C CE3 . TRP A 116 ? 0.2924 0.2421 0.3147 -0.0119 0.0288 0.0232 137 TRP A CE3 927 C CZ2 . TRP A 116 ? 0.3140 0.2757 0.3545 -0.0524 0.0618 -0.0043 137 TRP A CZ2 928 C CZ3 . TRP A 116 ? 0.3373 0.2530 0.3598 -0.0177 0.0458 0.0230 137 TRP A CZ3 929 C CH2 . TRP A 116 ? 0.3391 0.2569 0.3695 -0.0398 0.0642 0.0083 137 TRP A CH2 930 N N . GLU A 117 ? 0.2385 0.2448 0.2847 0.0046 -0.0043 0.0142 138 GLU A N 931 C CA . GLU A 117 ? 0.2534 0.2542 0.3168 0.0066 0.0000 0.0076 138 GLU A CA 932 C C . GLU A 117 ? 0.2220 0.2447 0.2981 0.0006 0.0006 -0.0044 138 GLU A C 933 O O . GLU A 117 ? 0.2342 0.2585 0.3202 -0.0068 0.0106 -0.0164 138 GLU A O 934 C CB . GLU A 117 ? 0.3104 0.2993 0.3778 0.0234 -0.0080 0.0170 138 GLU A CB 935 C CG . GLU A 117 ? 0.4000 0.3574 0.4492 0.0296 -0.0040 0.0318 138 GLU A CG 936 C CD . GLU A 117 ? 0.4794 0.4312 0.5241 0.0501 -0.0178 0.0469 138 GLU A CD 937 O OE1 . GLU A 117 ? 0.5124 0.4936 0.5698 0.0567 -0.0327 0.0428 138 GLU A OE1 938 O OE2 . GLU A 117 ? 0.5067 0.4268 0.5342 0.0590 -0.0136 0.0631 138 GLU A OE2 939 N N . ASP A 118 ? 0.1700 0.2061 0.2429 0.0016 -0.0068 -0.0026 139 ASP A N 940 C CA . ASP A 118 ? 0.1756 0.2268 0.2559 -0.0050 -0.0031 -0.0116 139 ASP A CA 941 C C . ASP A 118 ? 0.1886 0.2501 0.2559 -0.0159 0.0023 -0.0139 139 ASP A C 942 O O . ASP A 118 ? 0.2140 0.2863 0.2797 -0.0237 0.0080 -0.0209 139 ASP A O 943 C CB . ASP A 118 ? 0.1720 0.2285 0.2500 -0.0046 -0.0081 -0.0092 139 ASP A CB 944 C CG . ASP A 118 ? 0.2275 0.2927 0.3260 0.0017 -0.0143 -0.0145 139 ASP A CG 945 O OD1 . ASP A 118 ? 0.2452 0.3116 0.3619 0.0103 -0.0145 -0.0172 139 ASP A OD1 946 O OD2 . ASP A 118 ? 0.1781 0.2504 0.2767 -0.0015 -0.0182 -0.0168 139 ASP A OD2 947 N N . CYS A 119 ? 0.1330 0.1962 0.1906 -0.0163 0.0001 -0.0082 140 CYS A N 948 C CA . CYS A 119 ? 0.1539 0.2389 0.2025 -0.0241 0.0005 -0.0101 140 CYS A CA 949 C C . CYS A 119 ? 0.2066 0.3014 0.2609 -0.0372 0.0076 -0.0249 140 CYS A C 950 O O . CYS A 119 ? 0.2131 0.3364 0.2610 -0.0459 0.0055 -0.0298 140 CYS A O 951 C CB . CYS A 119 ? 0.1544 0.2469 0.1958 -0.0162 -0.0059 0.0025 140 CYS A CB 952 S SG . CYS A 119 ? 0.2529 0.3307 0.2840 -0.0061 -0.0079 0.0156 140 CYS A SG 953 N N . HIS A 120 ? 0.3156 0.3705 0.2199 0.0907 -0.0195 0.0188 141 HIS A N 954 C CA . HIS A 120 ? 0.3517 0.3743 0.2622 0.0911 -0.0063 0.0312 141 HIS A CA 955 C C . HIS A 120 ? 0.3596 0.3633 0.2816 0.0697 -0.0010 0.0183 141 HIS A C 956 O O . HIS A 120 ? 0.3556 0.3338 0.2808 0.0589 0.0082 0.0224 141 HIS A O 957 C CB . HIS A 120 ? 0.4003 0.4244 0.3152 0.1167 0.0003 0.0457 141 HIS A CB 958 C CG . HIS A 120 ? 0.4521 0.4800 0.3528 0.1366 0.0017 0.0666 141 HIS A CG 959 N ND1 . HIS A 120 ? 0.5358 0.5702 0.4353 0.1629 0.0056 0.0830 141 HIS A ND1 960 C CD2 . HIS A 120 ? 0.4650 0.4920 0.3517 0.1333 0.0004 0.0733 141 HIS A CD2 961 C CE1 . HIS A 120 ? 0.5379 0.5747 0.4276 0.1636 0.0089 0.0917 141 HIS A CE1 962 N NE2 . HIS A 120 ? 0.5012 0.5341 0.3849 0.1469 0.0060 0.0856 141 HIS A NE2 963 N N . THR A 121 ? 0.3416 0.3604 0.2701 0.0628 -0.0061 0.0014 142 THR A N 964 C CA . THR A 121 ? 0.3393 0.3436 0.2765 0.0421 -0.0008 -0.0114 142 THR A CA 965 C C . THR A 121 ? 0.3119 0.3112 0.2396 0.0189 -0.0064 -0.0195 142 THR A C 966 O O . THR A 121 ? 0.3145 0.3057 0.2451 0.0004 -0.0036 -0.0302 142 THR A O 967 C CB . THR A 121 ? 0.3556 0.3761 0.3048 0.0430 -0.0012 -0.0269 142 THR A CB 968 O OG1 . THR A 121 ? 0.3319 0.3822 0.2760 0.0474 -0.0125 -0.0363 142 THR A OG1 969 C CG2 . THR A 121 ? 0.3578 0.3755 0.3217 0.0648 0.0076 -0.0179 142 THR A CG2 970 N N . SER A 122 ? 0.2870 0.2920 0.2035 0.0203 -0.0140 -0.0143 143 SER A N 971 C CA . SER A 122 ? 0.2861 0.2842 0.1949 0.0012 -0.0189 -0.0192 143 SER A CA 972 C C . SER A 122 ? 0.3164 0.2952 0.2235 -0.0043 -0.0151 -0.0088 143 SER A C 973 O O . SER A 122 ? 0.3006 0.2696 0.2123 0.0052 -0.0069 0.0011 143 SER A O 974 C CB . SER A 122 ? 0.2726 0.2881 0.1746 0.0023 -0.0282 -0.0242 143 SER A CB 975 O OG . SER A 122 ? 0.2973 0.3321 0.2034 0.0030 -0.0302 -0.0383 143 SER A OG 976 N N . HIS A 123 ? 0.3010 0.2747 0.2024 -0.0194 -0.0203 -0.0116 144 HIS A N 977 C CA . HIS A 123 ? 0.3026 0.2633 0.2047 -0.0264 -0.0177 -0.0057 144 HIS A CA 978 C C . HIS A 123 ? 0.3012 0.2641 0.1971 -0.0284 -0.0265 -0.0019 144 HIS A C 979 O O . HIS A 123 ? 0.2518 0.2219 0.1424 -0.0308 -0.0337 -0.0061 144 HIS A O 980 C CB . HIS A 123 ? 0.3148 0.2689 0.2191 -0.0441 -0.0146 -0.0138 144 HIS A CB 981 C CG . HIS A 123 ? 0.3425 0.2919 0.2576 -0.0433 -0.0032 -0.0186 144 HIS A CG 982 N ND1 . HIS A 123 ? 0.3567 0.3130 0.2741 -0.0439 -0.0023 -0.0278 144 HIS A ND1 983 C CD2 . HIS A 123 ? 0.3509 0.2889 0.2777 -0.0416 0.0094 -0.0164 144 HIS A CD2 984 C CE1 . HIS A 123 ? 0.3562 0.3057 0.2870 -0.0419 0.0095 -0.0307 144 HIS A CE1 985 N NE2 . HIS A 123 ? 0.3641 0.3010 0.3008 -0.0404 0.0176 -0.0235 144 HIS A NE2 986 N N . THR A 124 ? 0.3118 0.2683 0.2107 -0.0278 -0.0242 0.0047 145 THR A N 987 C CA . THR A 124 ? 0.2858 0.2446 0.1821 -0.0303 -0.0324 0.0069 145 THR A CA 988 C C . THR A 124 ? 0.2641 0.2167 0.1668 -0.0356 -0.0290 0.0095 145 THR A C 989 O O . THR A 124 ? 0.2688 0.2147 0.1777 -0.0375 -0.0189 0.0090 145 THR A O 990 C CB . THR A 124 ? 0.2554 0.2233 0.1501 -0.0174 -0.0350 0.0106 145 THR A CB 991 O OG1 . THR A 124 ? 0.2372 0.2064 0.1327 -0.0213 -0.0422 0.0104 145 THR A OG1 992 C CG2 . THR A 124 ? 0.2552 0.2212 0.1520 -0.0058 -0.0265 0.0190 145 THR A CG2 993 N N . CYS A 125 ? 0.2169 0.1724 0.1204 -0.0382 -0.0366 0.0108 146 CYS A N 994 C CA . CYS A 125 ? 0.2692 0.2242 0.1807 -0.0439 -0.0351 0.0106 146 CYS A CA 995 C C . CYS A 125 ? 0.2774 0.2349 0.1947 -0.0358 -0.0352 0.0148 146 CYS A C 996 O O . CYS A 125 ? 0.2710 0.2308 0.1973 -0.0398 -0.0343 0.0132 146 CYS A O 997 C CB . CYS A 125 ? 0.2469 0.2070 0.1558 -0.0552 -0.0451 0.0073 146 CYS A CB 998 S SG . CYS A 125 ? 0.2945 0.2577 0.2033 -0.0492 -0.0550 0.0118 146 CYS A SG 999 N N . LYS A 126 ? 0.2551 0.2155 0.1681 -0.0255 -0.0362 0.0180 147 LYS A N 1000 C CA . LYS A 126 ? 0.2464 0.2117 0.1641 -0.0188 -0.0360 0.0203 147 LYS A CA 1001 C C . LYS A 126 ? 0.2682 0.2385 0.1792 -0.0067 -0.0310 0.0239 147 LYS A C 1002 O O . LYS A 126 ? 0.2800 0.2553 0.1839 -0.0027 -0.0333 0.0225 147 LYS A O 1003 C CB . LYS A 126 ? 0.2348 0.2052 0.1563 -0.0207 -0.0472 0.0176 147 LYS A CB 1004 C CG . LYS A 126 ? 0.2731 0.2437 0.2026 -0.0286 -0.0538 0.0165 147 LYS A CG 1005 C CD . LYS A 126 ? 0.2727 0.2439 0.2033 -0.0285 -0.0646 0.0172 147 LYS A CD 1006 C CE . LYS A 126 ? 0.2604 0.2352 0.1972 -0.0207 -0.0637 0.0155 147 LYS A CE 1007 N NZ . LYS A 126 ? 0.2399 0.2210 0.1889 -0.0167 -0.0599 0.0140 147 LYS A NZ 1008 N N . SER A 127 ? 0.2271 0.1992 0.1402 -0.0010 -0.0241 0.0276 148 SER A N 1009 C CA . SER A 127 ? 0.2540 0.2350 0.1580 0.0113 -0.0198 0.0322 148 SER A CA 1010 C C . SER A 127 ? 0.2652 0.2621 0.1709 0.0138 -0.0263 0.0261 148 SER A C 1011 O O . SER A 127 ? 0.3010 0.3118 0.1991 0.0229 -0.0241 0.0272 148 SER A O 1012 C CB . SER A 127 ? 0.2755 0.2488 0.1771 0.0167 -0.0059 0.0412 148 SER A CB 1013 O OG . SER A 127 ? 0.3129 0.2859 0.2241 0.0111 -0.0035 0.0381 148 SER A OG 1014 N N . ASN A 128 ? 0.2490 0.2450 0.1652 0.0061 -0.0337 0.0196 149 ASN A N 1015 C CA . ASN A 128 ? 0.2461 0.2545 0.1680 0.0072 -0.0384 0.0118 149 ASN A CA 1016 C C . ASN A 128 ? 0.2462 0.2483 0.1737 0.0000 -0.0470 0.0072 149 ASN A C 1017 O O . ASN A 128 ? 0.2702 0.2616 0.2033 -0.0060 -0.0509 0.0097 149 ASN A O 1018 C CB . ASN A 128 ? 0.2296 0.2417 0.1627 0.0071 -0.0355 0.0098 149 ASN A CB 1019 C CG . ASN A 128 ? 0.2680 0.2912 0.2117 0.0069 -0.0392 -0.0003 149 ASN A CG 1020 O OD1 . ASN A 128 ? 0.2941 0.3119 0.2450 0.0029 -0.0457 -0.0044 149 ASN A OD1 1021 N ND2 . ASN A 128 ? 0.2449 0.2828 0.1897 0.0110 -0.0336 -0.0047 149 ASN A ND2 1022 N N . TRP A 129 ? 0.2437 0.2533 0.1689 0.0006 -0.0491 0.0003 150 TRP A N 1023 C CA . TRP A 129 ? 0.2464 0.2462 0.1737 -0.0067 -0.0544 -0.0025 150 TRP A CA 1024 C C . TRP A 129 ? 0.2617 0.2615 0.2025 -0.0084 -0.0557 -0.0092 150 TRP A C 1025 O O . TRP A 129 ? 0.2762 0.2655 0.2189 -0.0137 -0.0579 -0.0108 150 TRP A O 1026 C CB . TRP A 129 ? 0.2471 0.2524 0.1651 -0.0075 -0.0535 -0.0077 150 TRP A CB 1027 C CG . TRP A 129 ? 0.2498 0.2519 0.1598 -0.0068 -0.0510 -0.0020 150 TRP A CG 1028 C CD1 . TRP A 129 ? 0.2567 0.2504 0.1625 -0.0057 -0.0495 0.0067 150 TRP A CD1 1029 C CD2 . TRP A 129 ? 0.2679 0.2755 0.1767 -0.0072 -0.0479 -0.0068 150 TRP A CD2 1030 N NE1 . TRP A 129 ? 0.2639 0.2553 0.1644 -0.0058 -0.0462 0.0081 150 TRP A NE1 1031 C CE2 . TRP A 129 ? 0.2839 0.2850 0.1870 -0.0060 -0.0457 -0.0001 150 TRP A CE2 1032 C CE3 . TRP A 129 ? 0.2526 0.2686 0.1643 -0.0086 -0.0471 -0.0177 150 TRP A CE3 1033 C CZ2 . TRP A 129 ? 0.2904 0.2939 0.1910 -0.0063 -0.0436 -0.0035 150 TRP A CZ2 1034 C CZ3 . TRP A 129 ? 0.2620 0.2771 0.1717 -0.0073 -0.0453 -0.0209 150 TRP A CZ3 1035 C CH2 . TRP A 129 ? 0.2746 0.2885 0.1796 -0.0065 -0.0435 -0.0142 150 TRP A CH2 1036 N N . HIS A 130 ? 0.2201 0.2307 0.1702 -0.0040 -0.0527 -0.0136 151 HIS A N 1037 C CA . HIS A 130 ? 0.2188 0.2295 0.1863 -0.0051 -0.0521 -0.0214 151 HIS A CA 1038 C C . HIS A 130 ? 0.2740 0.2711 0.2539 -0.0056 -0.0569 -0.0141 151 HIS A C 1039 O O . HIS A 130 ? 0.2823 0.2679 0.2728 -0.0071 -0.0593 -0.0137 151 HIS A O 1040 C CB . HIS A 130 ? 0.2241 0.2570 0.1963 -0.0010 -0.0459 -0.0319 151 HIS A CB 1041 C CG . HIS A 130 ? 0.2895 0.3245 0.2834 -0.0017 -0.0433 -0.0408 151 HIS A CG 1042 N ND1 . HIS A 130 ? 0.3371 0.3887 0.3376 0.0011 -0.0384 -0.0470 151 HIS A ND1 1043 C CD2 . HIS A 130 ? 0.3047 0.3267 0.3160 -0.0046 -0.0434 -0.0448 151 HIS A CD2 1044 C CE1 . HIS A 130 ? 0.3433 0.3935 0.3667 -0.0005 -0.0360 -0.0562 151 HIS A CE1 1045 N NE2 . HIS A 130 ? 0.3443 0.3754 0.3753 -0.0032 -0.0389 -0.0542 151 HIS A NE2 1046 N N . ARG A 131 ? 0.2968 0.2957 0.2758 -0.0039 -0.0578 -0.0081 152 ARG A N 1047 C CA . ARG A 131 ? 0.3051 0.2984 0.2979 -0.0036 -0.0631 -0.0036 152 ARG A CA 1048 C C . ARG A 131 ? 0.2748 0.2635 0.2593 -0.0067 -0.0673 0.0047 152 ARG A C 1049 O O . ARG A 131 ? 0.2690 0.2598 0.2420 -0.0081 -0.0624 0.0062 152 ARG A O 1050 C CB . ARG A 131 ? 0.3094 0.3142 0.3183 -0.0004 -0.0586 -0.0100 152 ARG A CB 1051 C CG . ARG A 131 ? 0.3204 0.3332 0.3418 0.0014 -0.0534 -0.0214 152 ARG A CG 1052 C CD . ARG A 131 ? 0.3121 0.3357 0.3523 0.0034 -0.0494 -0.0284 152 ARG A CD 1053 N NE . ARG A 131 ? 0.2932 0.3274 0.3468 0.0038 -0.0429 -0.0421 152 ARG A NE 1054 C CZ . ARG A 131 ? 0.2979 0.3267 0.3752 0.0049 -0.0433 -0.0483 152 ARG A CZ 1055 N NH1 . ARG A 131 ? 0.2610 0.2736 0.3485 0.0076 -0.0513 -0.0392 152 ARG A NH1 1056 N NH2 . ARG A 131 ? 0.3003 0.3408 0.3912 0.0036 -0.0350 -0.0639 152 ARG A NH2 1057 N N . GLY A 132 ? 0.2464 0.2296 0.2373 -0.0075 -0.0759 0.0099 153 GLY A N 1058 C CA . GLY A 132 ? 0.2654 0.2514 0.2533 -0.0111 -0.0802 0.0140 153 GLY A CA 1059 C C . GLY A 132 ? 0.3006 0.2796 0.2732 -0.0163 -0.0862 0.0206 153 GLY A C 1060 O O . GLY A 132 ? 0.2793 0.2640 0.2487 -0.0210 -0.0890 0.0216 153 GLY A O 1061 N N . TRP A 133 ? 0.2955 0.2635 0.2589 -0.0170 -0.0871 0.0235 154 TRP A N 1062 C CA . TRP A 133 ? 0.2979 0.2593 0.2455 -0.0230 -0.0911 0.0295 154 TRP A CA 1063 C C . TRP A 133 ? 0.3110 0.2735 0.2631 -0.0207 -0.0990 0.0370 154 TRP A C 1064 O O . TRP A 133 ? 0.2674 0.2297 0.2339 -0.0132 -0.1062 0.0406 154 TRP A O 1065 C CB . TRP A 133 ? 0.2932 0.2419 0.2304 -0.0255 -0.0879 0.0294 154 TRP A CB 1066 C CG . TRP A 133 ? 0.2526 0.2051 0.1847 -0.0267 -0.0794 0.0210 154 TRP A CG 1067 C CD1 . TRP A 133 ? 0.2323 0.1893 0.1719 -0.0224 -0.0736 0.0133 154 TRP A CD1 1068 C CD2 . TRP A 133 ? 0.2168 0.1729 0.1400 -0.0303 -0.0722 0.0182 154 TRP A CD2 1069 N NE1 . TRP A 133 ? 0.2251 0.1893 0.1556 -0.0229 -0.0681 0.0078 154 TRP A NE1 1070 C CE2 . TRP A 133 ? 0.2373 0.1993 0.1588 -0.0271 -0.0670 0.0114 154 TRP A CE2 1071 C CE3 . TRP A 133 ? 0.2298 0.1866 0.1487 -0.0353 -0.0691 0.0196 154 TRP A CE3 1072 C CZ2 . TRP A 133 ? 0.2000 0.1674 0.1165 -0.0268 -0.0596 0.0083 154 TRP A CZ2 1073 C CZ3 . TRP A 133 ? 0.2394 0.1988 0.1538 -0.0369 -0.0616 0.0153 154 TRP A CZ3 1074 C CH2 . TRP A 133 ? 0.2205 0.1845 0.1341 -0.0318 -0.0574 0.0106 154 TRP A CH2 1075 N N . ASP A 134 ? 0.3138 0.2795 0.2552 -0.0259 -0.0975 0.0391 155 ASP A N 1076 C CA . ASP A 134 ? 0.3019 0.2694 0.2410 -0.0233 -0.1044 0.0477 155 ASP A CA 1077 C C . ASP A 134 ? 0.3070 0.2544 0.2346 -0.0240 -0.1044 0.0561 155 ASP A C 1078 O O . ASP A 134 ? 0.2979 0.2391 0.2107 -0.0320 -0.0991 0.0550 155 ASP A O 1079 C CB . ASP A 134 ? 0.3150 0.2964 0.2458 -0.0292 -0.1033 0.0452 155 ASP A CB 1080 C CG . ASP A 134 ? 0.3796 0.3671 0.3045 -0.0253 -0.1110 0.0545 155 ASP A CG 1081 O OD1 . ASP A 134 ? 0.3888 0.3650 0.3142 -0.0179 -0.1156 0.0652 155 ASP A OD1 1082 O OD2 . ASP A 134 ? 0.4100 0.4136 0.3292 -0.0290 -0.1122 0.0514 155 ASP A OD2 1083 N N . TRP A 135 ? 0.3342 0.2704 0.2706 -0.0158 -0.1095 0.0641 156 TRP A N 1084 C CA . TRP A 135 ? 0.3489 0.2608 0.2761 -0.0163 -0.1077 0.0732 156 TRP A CA 1085 C C . TRP A 135 ? 0.3730 0.2812 0.2933 -0.0115 -0.1104 0.0871 156 TRP A C 1086 O O . TRP A 135 ? 0.3895 0.2747 0.3057 -0.0095 -0.1067 0.0968 156 TRP A O 1087 C CB . TRP A 135 ? 0.3639 0.2618 0.3102 -0.0096 -0.1047 0.0712 156 TRP A CB 1088 C CG . TRP A 135 ? 0.3327 0.2347 0.2837 -0.0148 -0.0942 0.0545 156 TRP A CG 1089 C CD1 . TRP A 135 ? 0.3114 0.2295 0.2764 -0.0121 -0.0922 0.0430 156 TRP A CD1 1090 C CD2 . TRP A 135 ? 0.3373 0.2298 0.2783 -0.0232 -0.0840 0.0470 156 TRP A CD2 1091 N NE1 . TRP A 135 ? 0.3130 0.2335 0.2754 -0.0169 -0.0827 0.0307 156 TRP A NE1 1092 C CE2 . TRP A 135 ? 0.3127 0.2194 0.2622 -0.0236 -0.0780 0.0316 156 TRP A CE2 1093 C CE3 . TRP A 135 ? 0.3699 0.2446 0.2957 -0.0305 -0.0789 0.0514 156 TRP A CE3 1094 C CZ2 . TRP A 135 ? 0.3195 0.2271 0.2641 -0.0299 -0.0688 0.0196 156 TRP A CZ2 1095 C CZ3 . TRP A 135 ? 0.3662 0.2400 0.2886 -0.0386 -0.0682 0.0376 156 TRP A CZ3 1096 C CH2 . TRP A 135 ? 0.3324 0.2244 0.2651 -0.0376 -0.0641 0.0216 156 TRP A CH2 1097 N N . THR A 136 ? 0.3760 0.3065 0.2950 -0.0088 -0.1156 0.0882 157 THR A N 1098 C CA . THR A 136 ? 0.3777 0.3100 0.2904 -0.0001 -0.1204 0.1025 157 THR A CA 1099 C C . THR A 136 ? 0.4014 0.3184 0.2905 -0.0062 -0.1150 0.1113 157 THR A C 1100 O O . THR A 136 ? 0.4471 0.3538 0.3298 0.0024 -0.1156 0.1265 157 THR A O 1101 C CB . THR A 136 ? 0.4290 0.3931 0.3441 0.0046 -0.1287 0.0999 157 THR A CB 1102 O OG1 . THR A 136 ? 0.4177 0.3956 0.3211 -0.0076 -0.1255 0.0893 157 THR A OG1 1103 C CG2 . THR A 136 ? 0.3990 0.3779 0.3391 0.0114 -0.1337 0.0922 157 THR A CG2 1104 N N . SER A 137 ? 0.4151 0.3298 0.2919 -0.0203 -0.1088 0.1021 158 SER A N 1105 C CA . SER A 137 ? 0.4547 0.3557 0.3098 -0.0278 -0.1031 0.1086 158 SER A CA 1106 C C . SER A 137 ? 0.4628 0.3311 0.3156 -0.0303 -0.0942 0.1132 158 SER A C 1107 O O . SER A 137 ? 0.4712 0.3236 0.3070 -0.0367 -0.0869 0.1191 158 SER A O 1108 C CB . SER A 137 ? 0.4647 0.3770 0.3097 -0.0424 -0.0992 0.0953 158 SER A CB 1109 O OG . SER A 137 ? 0.4787 0.3788 0.3262 -0.0508 -0.0926 0.0844 158 SER A OG 1110 N N . GLY A 138 ? 0.4624 0.3207 0.3328 -0.0266 -0.0933 0.1086 159 GLY A N 1111 C CA . GLY A 138 ? 0.4638 0.2921 0.3350 -0.0316 -0.0825 0.1074 159 GLY A CA 1112 C C . GLY A 138 ? 0.4156 0.2445 0.2840 -0.0438 -0.0789 0.0905 159 GLY A C 1113 O O . GLY A 138 ? 0.4354 0.2532 0.3166 -0.0460 -0.0678 0.0796 159 GLY A O 1114 N N . VAL A 139 ? 0.3621 0.2143 0.2224 -0.0494 -0.0834 0.0819 160 VAL A N 1115 C CA . VAL A 139 ? 0.3307 0.1908 0.1907 -0.0574 -0.0787 0.0652 160 VAL A CA 1116 C C . VAL A 139 ? 0.3523 0.2370 0.2214 -0.0529 -0.0863 0.0591 160 VAL A C 1117 O O . VAL A 139 ? 0.3650 0.2662 0.2394 -0.0494 -0.0897 0.0615 160 VAL A O 1118 C CB . VAL A 139 ? 0.3726 0.2303 0.2105 -0.0713 -0.0736 0.0618 160 VAL A CB 1119 C CG1 . VAL A 139 ? 0.3226 0.1960 0.1651 -0.0762 -0.0688 0.0431 160 VAL A CG1 1120 C CG2 . VAL A 139 ? 0.3478 0.1791 0.1765 -0.0780 -0.0623 0.0663 160 VAL A CG2 1121 N N . ASN A 140 ? 0.4037 0.2180 0.3354 -0.0619 -0.0346 0.1348 161 ASN A N 1122 C CA . ASN A 140 ? 0.3880 0.2268 0.3217 -0.0526 -0.0439 0.1147 161 ASN A CA 1123 C C . ASN A 140 ? 0.4250 0.2805 0.3213 -0.0524 -0.0391 0.1144 161 ASN A C 1124 O O . ASN A 140 ? 0.3696 0.2347 0.2555 -0.0624 -0.0218 0.1150 161 ASN A O 1125 C CB . ASN A 140 ? 0.3210 0.1801 0.2905 -0.0557 -0.0380 0.0914 161 ASN A CB 1126 C CG . ASN A 140 ? 0.3155 0.1871 0.2879 -0.0674 -0.0187 0.0883 161 ASN A CG 1127 O OD1 . ASN A 140 ? 0.3389 0.1975 0.3177 -0.0776 -0.0072 0.0989 161 ASN A OD1 1128 N ND2 . ASN A 140 ? 0.2864 0.1827 0.2574 -0.0661 -0.0151 0.0726 161 ASN A ND2 1129 N N . LYS A 141 ? 0.4271 0.2879 0.3079 -0.0412 -0.0540 0.1106 162 LYS A N 1130 C CA . LYS A 141 ? 0.4306 0.3105 0.2827 -0.0397 -0.0512 0.1044 162 LYS A CA 1131 C C . LYS A 141 ? 0.3612 0.2587 0.2279 -0.0309 -0.0606 0.0826 162 LYS A C 1132 O O . LYS A 141 ? 0.3595 0.2527 0.2484 -0.0242 -0.0730 0.0758 162 LYS A O 1133 C CB . LYS A 141 ? 0.5119 0.3825 0.3229 -0.0365 -0.0573 0.1220 162 LYS A CB 1134 C CG . LYS A 141 ? 0.6078 0.4615 0.4078 -0.0440 -0.0445 0.1420 162 LYS A CG 1135 C CD . LYS A 141 ? 0.7082 0.5630 0.4704 -0.0391 -0.0447 0.1534 162 LYS A CD 1136 C CE . LYS A 141 ? 0.7719 0.6498 0.5111 -0.0468 -0.0283 0.1451 162 LYS A CE 1137 N NZ . LYS A 141 ? 0.8528 0.7328 0.5539 -0.0444 -0.0253 0.1562 162 LYS A NZ 1138 N N . CYS A 142 ? 0.3353 0.2523 0.1916 -0.0319 -0.0532 0.0707 163 CYS A N 1139 C CA . CYS A 142 ? 0.2959 0.2271 0.1633 -0.0256 -0.0591 0.0513 163 CYS A CA 1140 C C . CYS A 142 ? 0.3033 0.2311 0.1643 -0.0158 -0.0770 0.0504 163 CYS A C 1141 O O . CYS A 142 ? 0.3318 0.2571 0.1652 -0.0129 -0.0828 0.0606 163 CYS A O 1142 C CB . CYS A 142 ? 0.2950 0.2435 0.1490 -0.0280 -0.0487 0.0418 163 CYS A CB 1143 S SG . CYS A 142 ? 0.3958 0.3512 0.2657 -0.0370 -0.0309 0.0387 163 CYS A SG 1144 N N . PRO A 143 ? 0.2721 0.2016 0.1592 -0.0109 -0.0859 0.0369 164 PRO A N 1145 C CA . PRO A 143 ? 0.2940 0.2238 0.1847 -0.0009 -0.1036 0.0309 164 PRO A CA 1146 C C . PRO A 143 ? 0.3082 0.2564 0.1902 0.0020 -0.1046 0.0144 164 PRO A C 1147 O O . PRO A 143 ? 0.2707 0.2291 0.1471 -0.0036 -0.0913 0.0072 164 PRO A O 1148 C CB . PRO A 143 ? 0.2841 0.2127 0.2119 -0.0005 -0.1068 0.0178 164 PRO A CB 1149 C CG . PRO A 143 ? 0.2776 0.2142 0.2126 -0.0095 -0.0904 0.0096 164 PRO A CG 1150 C CD . PRO A 143 ? 0.2664 0.1995 0.1814 -0.0153 -0.0790 0.0248 164 PRO A CD 1151 N N . ALA A 144 ? 0.3236 0.2782 0.2130 0.0108 -0.1170 0.0062 165 ALA A N 1152 C CA . ALA A 144 ? 0.3150 0.2910 0.2077 0.0124 -0.1126 -0.0116 165 ALA A CA 1153 C C . ALA A 144 ? 0.2620 0.2458 0.1735 0.0052 -0.0982 -0.0280 165 ALA A C 1154 O O . ALA A 144 ? 0.2746 0.2530 0.2070 0.0026 -0.0962 -0.0333 165 ALA A O 1155 C CB . ALA A 144 ? 0.2815 0.2629 0.1897 0.0218 -0.1270 -0.0201 165 ALA A CB 1156 N N . GLY A 145 ? 0.2639 0.2599 0.1682 0.0011 -0.0868 -0.0350 166 GLY A N 1157 C CA . GLY A 145 ? 0.2394 0.2387 0.1597 -0.0059 -0.0724 -0.0466 166 GLY A CA 1158 C C . GLY A 145 ? 0.2629 0.2558 0.1785 -0.0112 -0.0627 -0.0415 166 GLY A C 1159 O O . GLY A 145 ? 0.3009 0.2937 0.2261 -0.0165 -0.0517 -0.0477 166 GLY A O 1160 N N . ALA A 146 ? 0.2789 0.2628 0.1773 -0.0106 -0.0666 -0.0278 167 ALA A N 1161 C CA . ALA A 146 ? 0.3070 0.2829 0.2033 -0.0164 -0.0589 -0.0221 167 ALA A CA 1162 C C . ALA A 146 ? 0.3465 0.3284 0.2265 -0.0183 -0.0501 -0.0177 167 ALA A C 1163 O O . ALA A 146 ? 0.3796 0.3604 0.2442 -0.0191 -0.0501 -0.0054 167 ALA A O 1164 C CB . ALA A 146 ? 0.2861 0.2517 0.1907 -0.0179 -0.0618 -0.0097 167 ALA A CB 1165 N N . LEU A 147 ? 0.3101 0.2975 0.1943 -0.0196 -0.0418 -0.0279 168 LEU A N 1166 C CA . LEU A 147 ? 0.2986 0.2948 0.1733 -0.0213 -0.0328 -0.0283 168 LEU A CA 1167 C C . LEU A 147 ? 0.2929 0.2865 0.1768 -0.0246 -0.0250 -0.0214 168 LEU A C 1168 O O . LEU A 147 ? 0.2814 0.2675 0.1798 -0.0249 -0.0265 -0.0201 168 LEU A O 1169 C CB . LEU A 147 ? 0.3026 0.3058 0.1835 -0.0196 -0.0280 -0.0444 168 LEU A CB 1170 C CG . LEU A 147 ? 0.3407 0.3459 0.2211 -0.0151 -0.0323 -0.0522 168 LEU A CG 1171 C CD1 . LEU A 147 ? 0.3501 0.3581 0.2442 -0.0151 -0.0243 -0.0648 168 LEU A CD1 1172 C CD2 . LEU A 147 ? 0.3716 0.3847 0.2298 -0.0136 -0.0359 -0.0474 168 LEU A CD2 1173 N N . CYS A 148 ? 0.2591 0.2610 0.1349 -0.0277 -0.0167 -0.0188 169 CYS A N 1174 C CA . CYS A 148 ? 0.3041 0.3091 0.1944 -0.0306 -0.0084 -0.0181 169 CYS A CA 1175 C C . CYS A 148 ? 0.3117 0.3197 0.2188 -0.0267 -0.0061 -0.0310 169 CYS A C 1176 O O . CYS A 148 ? 0.3007 0.3150 0.2052 -0.0249 -0.0035 -0.0421 169 CYS A O 1177 C CB . CYS A 148 ? 0.3316 0.3466 0.2105 -0.0368 0.0026 -0.0144 169 CYS A CB 1178 S SG . CYS A 148 ? 0.4425 0.4452 0.3059 -0.0431 0.0016 0.0070 169 CYS A SG 1179 N N . ARG A 149 ? 0.2897 0.2925 0.2139 -0.0252 -0.0081 -0.0295 170 ARG A N 1180 C CA . ARG A 149 ? 0.3009 0.3015 0.2406 -0.0202 -0.0087 -0.0376 170 ARG A CA 1181 C C . ARG A 149 ? 0.2690 0.2740 0.2270 -0.0189 -0.0089 -0.0364 170 ARG A C 1182 O O . ARG A 149 ? 0.2437 0.2528 0.2036 -0.0232 -0.0076 -0.0303 170 ARG A O 1183 C CB . ARG A 149 ? 0.2898 0.2752 0.2270 -0.0181 -0.0159 -0.0365 170 ARG A CB 1184 C CG . ARG A 149 ? 0.2333 0.2162 0.1587 -0.0194 -0.0167 -0.0410 170 ARG A CG 1185 C CD . ARG A 149 ? 0.2734 0.2423 0.1984 -0.0204 -0.0212 -0.0406 170 ARG A CD 1186 N NE . ARG A 149 ? 0.2834 0.2537 0.2021 -0.0223 -0.0232 -0.0460 170 ARG A NE 1187 C CZ . ARG A 149 ? 0.2450 0.2181 0.1655 -0.0211 -0.0208 -0.0565 170 ARG A CZ 1188 N NH1 . ARG A 149 ? 0.2276 0.1999 0.1535 -0.0203 -0.0150 -0.0646 170 ARG A NH1 1189 N NH2 . ARG A 149 ? 0.2054 0.1806 0.1270 -0.0189 -0.0245 -0.0578 170 ARG A NH2 1190 N N . THR A 150 ? 0.2403 0.2438 0.2139 -0.0126 -0.0114 -0.0425 171 THR A N 1191 C CA . THR A 150 ? 0.2497 0.2587 0.2424 -0.0093 -0.0154 -0.0429 171 THR A CA 1192 C C . THR A 150 ? 0.2327 0.2330 0.2190 -0.0105 -0.0240 -0.0336 171 THR A C 1193 O O . THR A 150 ? 0.2205 0.2080 0.1910 -0.0120 -0.0274 -0.0285 171 THR A O 1194 C CB . THR A 150 ? 0.2589 0.2641 0.2687 0.0002 -0.0208 -0.0495 171 THR A CB 1195 O OG1 . THR A 150 ? 0.2884 0.2724 0.2850 0.0031 -0.0275 -0.0436 171 THR A OG1 1196 C CG2 . THR A 150 ? 0.2715 0.2888 0.2948 0.0014 -0.0114 -0.0634 171 THR A CG2 1197 N N . PHE A 151 ? 0.2117 0.2217 0.2133 -0.0105 -0.0267 -0.0342 172 PHE A N 1198 C CA . PHE A 151 ? 0.2220 0.2281 0.2209 -0.0120 -0.0348 -0.0290 172 PHE A CA 1199 C C . PHE A 151 ? 0.2665 0.2573 0.2522 -0.0071 -0.0444 -0.0251 172 PHE A C 1200 O O . PHE A 151 ? 0.2992 0.2817 0.2705 -0.0112 -0.0468 -0.0208 172 PHE A O 1201 C CB . PHE A 151 ? 0.2121 0.2340 0.2348 -0.0109 -0.0379 -0.0346 172 PHE A CB 1202 C CG . PHE A 151 ? 0.2681 0.2958 0.2961 -0.0197 -0.0336 -0.0332 172 PHE A CG 1203 C CD1 . PHE A 151 ? 0.2979 0.3265 0.3229 -0.0279 -0.0212 -0.0299 172 PHE A CD1 1204 C CD2 . PHE A 151 ? 0.2756 0.3071 0.3111 -0.0200 -0.0419 -0.0351 172 PHE A CD2 1205 C CE1 . PHE A 151 ? 0.3258 0.3549 0.3575 -0.0363 -0.0169 -0.0267 172 PHE A CE1 1206 C CE2 . PHE A 151 ? 0.2876 0.3235 0.3335 -0.0285 -0.0372 -0.0356 172 PHE A CE2 1207 C CZ . PHE A 151 ? 0.3001 0.3328 0.3452 -0.0366 -0.0246 -0.0305 172 PHE A CZ 1208 N N . GLU A 152 ? 0.2702 0.2567 0.2620 0.0013 -0.0494 -0.0271 173 GLU A N 1209 C CA . GLU A 152 ? 0.3123 0.2799 0.2889 0.0056 -0.0580 -0.0206 173 GLU A CA 1210 C C . GLU A 152 ? 0.3035 0.2546 0.2592 -0.0002 -0.0520 -0.0169 173 GLU A C 1211 O O . GLU A 152 ? 0.2980 0.2345 0.2362 -0.0019 -0.0559 -0.0108 173 GLU A O 1212 C CB . GLU A 152 ? 0.3690 0.3309 0.3584 0.0166 -0.0643 -0.0224 173 GLU A CB 1213 C CG . GLU A 152 ? 0.4859 0.4560 0.4877 0.0248 -0.0781 -0.0228 173 GLU A CG 1214 C CD . GLU A 152 ? 0.5884 0.5521 0.6074 0.0380 -0.0872 -0.0249 173 GLU A CD 1215 O OE1 . GLU A 152 ? 0.6042 0.5874 0.6544 0.0427 -0.0858 -0.0374 173 GLU A OE1 1216 O OE2 . GLU A 152 ? 0.6396 0.5782 0.6419 0.0431 -0.0950 -0.0145 173 GLU A OE2 1217 N N . SER A 153 ? 0.2760 0.2308 0.2332 -0.0037 -0.0423 -0.0218 174 SER A N 1218 C CA . SER A 153 ? 0.3069 0.2505 0.2492 -0.0093 -0.0372 -0.0220 174 SER A CA 1219 C C . SER A 153 ? 0.3176 0.2609 0.2487 -0.0162 -0.0384 -0.0191 174 SER A C 1220 O O . SER A 153 ? 0.3263 0.2576 0.2451 -0.0204 -0.0376 -0.0182 174 SER A O 1221 C CB . SER A 153 ? 0.3133 0.2659 0.2587 -0.0110 -0.0290 -0.0293 174 SER A CB 1222 O OG . SER A 153 ? 0.3734 0.3285 0.3317 -0.0056 -0.0262 -0.0359 174 SER A OG 1223 N N . TYR A 154 ? 0.2701 0.2265 0.2079 -0.0184 -0.0389 -0.0191 175 TYR A N 1224 C CA . TYR A 154 ? 0.2659 0.2232 0.1998 -0.0242 -0.0406 -0.0187 175 TYR A CA 1225 C C . TYR A 154 ? 0.2795 0.2375 0.2117 -0.0249 -0.0471 -0.0173 175 TYR A C 1226 O O . TYR A 154 ? 0.2476 0.2045 0.1738 -0.0305 -0.0476 -0.0197 175 TYR A O 1227 C CB . TYR A 154 ? 0.2366 0.2036 0.1792 -0.0265 -0.0385 -0.0185 175 TYR A CB 1228 C CG . TYR A 154 ? 0.2630 0.2287 0.1996 -0.0271 -0.0348 -0.0197 175 TYR A CG 1229 C CD1 . TYR A 154 ? 0.2587 0.2192 0.1900 -0.0295 -0.0359 -0.0238 175 TYR A CD1 1230 C CD2 . TYR A 154 ? 0.2529 0.2249 0.1892 -0.0255 -0.0305 -0.0189 175 TYR A CD2 1231 C CE1 . TYR A 154 ? 0.2434 0.2055 0.1708 -0.0285 -0.0352 -0.0269 175 TYR A CE1 1232 C CE2 . TYR A 154 ? 0.2757 0.2486 0.2028 -0.0255 -0.0290 -0.0208 175 TYR A CE2 1233 C CZ . TYR A 154 ? 0.2616 0.2296 0.1848 -0.0262 -0.0327 -0.0248 175 TYR A CZ 1234 O OH . TYR A 154 ? 0.2538 0.2253 0.1696 -0.0249 -0.0339 -0.0285 175 TYR A OH 1235 N N . PHE A 155 ? 0.2853 0.2476 0.2241 -0.0189 -0.0526 -0.0156 176 PHE A N 1236 C CA . PHE A 155 ? 0.2883 0.2543 0.2244 -0.0178 -0.0615 -0.0152 176 PHE A CA 1237 C C . PHE A 155 ? 0.3212 0.2768 0.2489 -0.0097 -0.0692 -0.0098 176 PHE A C 1238 O O . PHE A 155 ? 0.3031 0.2669 0.2461 -0.0016 -0.0759 -0.0111 176 PHE A O 1239 C CB . PHE A 155 ? 0.2887 0.2735 0.2473 -0.0169 -0.0640 -0.0203 176 PHE A CB 1240 C CG . PHE A 155 ? 0.2853 0.2760 0.2545 -0.0240 -0.0566 -0.0229 176 PHE A CG 1241 C CD1 . PHE A 155 ? 0.2917 0.2804 0.2563 -0.0305 -0.0561 -0.0255 176 PHE A CD1 1242 C CD2 . PHE A 155 ? 0.2725 0.2699 0.2566 -0.0245 -0.0500 -0.0230 176 PHE A CD2 1243 C CE1 . PHE A 155 ? 0.2942 0.2853 0.2716 -0.0354 -0.0515 -0.0270 176 PHE A CE1 1244 C CE2 . PHE A 155 ? 0.2784 0.2765 0.2691 -0.0308 -0.0443 -0.0219 176 PHE A CE2 1245 C CZ . PHE A 155 ? 0.2710 0.2646 0.2595 -0.0352 -0.0462 -0.0233 176 PHE A CZ 1246 N N . PRO A 156 ? 0.3403 0.2768 0.2453 -0.0120 -0.0682 -0.0039 177 PRO A N 1247 C CA . PRO A 156 ? 0.3196 0.2393 0.2166 -0.0038 -0.0749 0.0041 177 PRO A CA 1248 C C . PRO A 156 ? 0.3104 0.2325 0.2008 0.0034 -0.0906 0.0089 177 PRO A C 1249 O O . PRO A 156 ? 0.3294 0.2400 0.2207 0.0138 -0.0999 0.0153 177 PRO A O 1250 C CB . PRO A 156 ? 0.3771 0.2736 0.2502 -0.0114 -0.0669 0.0095 177 PRO A CB 1251 C CG . PRO A 156 ? 0.4002 0.3062 0.2694 -0.0233 -0.0579 0.0020 177 PRO A CG 1252 C CD . PRO A 156 ? 0.3292 0.2577 0.2213 -0.0221 -0.0583 -0.0058 177 PRO A CD 1253 N N . THR A 157 ? 0.2956 0.2328 0.1813 -0.0014 -0.0946 0.0048 178 THR A N 1254 C CA . THR A 157 ? 0.2944 0.2413 0.1771 0.0053 -0.1092 0.0058 178 THR A CA 1255 C C . THR A 157 ? 0.3057 0.2826 0.2132 0.0022 -0.1077 -0.0074 178 THR A C 1256 O O . THR A 157 ? 0.2845 0.2684 0.2024 -0.0064 -0.0971 -0.0142 178 THR A O 1257 C CB . THR A 157 ? 0.3601 0.2964 0.2100 0.0002 -0.1079 0.0143 178 THR A CB 1258 O OG1 . THR A 157 ? 0.3257 0.2717 0.1717 -0.0128 -0.0951 0.0065 178 THR A OG1 1259 C CG2 . THR A 157 ? 0.3343 0.2362 0.1579 0.0008 -0.1068 0.0291 178 THR A CG2 1260 N N . PRO A 158 ? 0.3289 0.2378 0.2622 -0.0446 0.0338 0.0308 179 PRO A N 1261 C CA . PRO A 158 ? 0.3037 0.2285 0.2426 -0.0372 0.0264 0.0297 179 PRO A CA 1262 C C . PRO A 158 ? 0.2754 0.2210 0.2169 -0.0374 0.0162 0.0293 179 PRO A C 1263 O O . PRO A 158 ? 0.2513 0.2018 0.1907 -0.0379 0.0093 0.0250 179 PRO A O 1264 C CB . PRO A 158 ? 0.3005 0.2302 0.2504 -0.0255 0.0289 0.0361 179 PRO A CB 1265 C CG . PRO A 158 ? 0.3062 0.2134 0.2558 -0.0253 0.0405 0.0387 179 PRO A CG 1266 C CD . PRO A 158 ? 0.3397 0.2355 0.2779 -0.0376 0.0430 0.0368 179 PRO A CD 1267 N N . ALA A 159 ? 0.2638 0.2203 0.2095 -0.0372 0.0160 0.0334 180 ALA A N 1268 C CA . ALA A 159 ? 0.2479 0.2254 0.1988 -0.0369 0.0085 0.0314 180 ALA A CA 1269 C C . ALA A 159 ? 0.2535 0.2331 0.2030 -0.0446 0.0023 0.0259 180 ALA A C 1270 O O . ALA A 159 ? 0.2479 0.2399 0.2020 -0.0409 -0.0059 0.0230 180 ALA A O 1271 C CB . ALA A 159 ? 0.1833 0.1727 0.1380 -0.0373 0.0117 0.0360 180 ALA A CB 1272 N N . ALA A 160 ? 0.2377 0.2040 0.1800 -0.0552 0.0055 0.0244 181 ALA A N 1273 C CA . ALA A 160 ? 0.2360 0.2058 0.1756 -0.0638 -0.0027 0.0199 181 ALA A CA 1274 C C . ALA A 160 ? 0.2632 0.2258 0.1948 -0.0608 -0.0097 0.0174 181 ALA A C 1275 O O . ALA A 160 ? 0.2791 0.2514 0.2125 -0.0611 -0.0207 0.0159 181 ALA A O 1276 C CB . ALA A 160 ? 0.2473 0.2019 0.1771 -0.0782 0.0021 0.0177 181 ALA A CB 1277 N N . LEU A 161 ? 0.2507 0.1962 0.1740 -0.0580 -0.0031 0.0172 182 LEU A N 1278 C CA . LEU A 161 ? 0.2567 0.1951 0.1716 -0.0561 -0.0079 0.0152 182 LEU A CA 1279 C C . LEU A 161 ? 0.2300 0.1842 0.1554 -0.0451 -0.0149 0.0164 182 LEU A C 1280 O O . LEU A 161 ? 0.2072 0.1658 0.1315 -0.0441 -0.0250 0.0158 182 LEU A O 1281 C CB . LEU A 161 ? 0.2897 0.2086 0.1962 -0.0566 0.0029 0.0135 182 LEU A CB 1282 C CG . LEU A 161 ? 0.2846 0.1969 0.1840 -0.0546 0.0014 0.0117 182 LEU A CG 1283 C CD1 . LEU A 161 ? 0.2699 0.1731 0.1517 -0.0631 -0.0077 0.0099 182 LEU A CD1 1284 C CD2 . LEU A 161 ? 0.2989 0.1964 0.1961 -0.0550 0.0152 0.0092 182 LEU A CD2 1285 N N . CYS A 162 ? 0.2176 0.1793 0.1523 -0.0370 -0.0099 0.0184 183 CYS A N 1286 C CA . CYS A 162 ? 0.2448 0.2169 0.1856 -0.0285 -0.0148 0.0178 183 CYS A CA 1287 C C . CYS A 162 ? 0.2616 0.2510 0.2117 -0.0248 -0.0221 0.0170 183 CYS A C 1288 O O . CYS A 162 ? 0.2461 0.2376 0.1975 -0.0196 -0.0283 0.0150 183 CYS A O 1289 C CB . CYS A 162 ? 0.2544 0.2319 0.2016 -0.0223 -0.0089 0.0200 183 CYS A CB 1290 S SG . CYS A 162 ? 0.3761 0.3372 0.3200 -0.0244 0.0006 0.0206 183 CYS A SG 1291 N N . GLU A 163 ? 0.2450 0.2457 0.2023 -0.0277 -0.0202 0.0181 184 GLU A N 1292 C CA . GLU A 163 ? 0.2618 0.2826 0.2323 -0.0244 -0.0247 0.0164 184 GLU A CA 1293 C C . GLU A 163 ? 0.2490 0.2725 0.2221 -0.0284 -0.0344 0.0152 184 GLU A C 1294 O O . GLU A 163 ? 0.2514 0.2868 0.2354 -0.0217 -0.0415 0.0135 184 GLU A O 1295 C CB . GLU A 163 ? 0.2144 0.2492 0.1927 -0.0266 -0.0171 0.0179 184 GLU A CB 1296 C CG . GLU A 163 ? 0.2690 0.2992 0.2415 -0.0230 -0.0099 0.0213 184 GLU A CG 1297 C CD . GLU A 163 ? 0.3078 0.3486 0.2828 -0.0251 -0.0026 0.0243 184 GLU A CD 1298 O OE1 . GLU A 163 ? 0.3428 0.3935 0.3246 -0.0314 -0.0005 0.0236 184 GLU A OE1 1299 O OE2 . GLU A 163 ? 0.3000 0.3394 0.2694 -0.0213 0.0007 0.0279 184 GLU A OE2 1300 N N . GLY A 164 ? 0.2322 0.2445 0.1954 -0.0389 -0.0352 0.0160 185 GLY A N 1301 C CA . GLY A 164 ? 0.2229 0.2412 0.1882 -0.0444 -0.0464 0.0155 185 GLY A CA 1302 C C . GLY A 164 ? 0.2554 0.2601 0.2087 -0.0418 -0.0569 0.0164 185 GLY A C 1303 O O . GLY A 164 ? 0.2351 0.2487 0.1946 -0.0399 -0.0698 0.0175 185 GLY A O 1304 N N . LEU A 165 ? 0.2271 0.2105 0.1642 -0.0413 -0.0514 0.0166 186 LEU A N 1305 C CA . LEU A 165 ? 0.2721 0.2361 0.1909 -0.0429 -0.0585 0.0178 186 LEU A CA 1306 C C . LEU A 165 ? 0.2719 0.2419 0.1982 -0.0329 -0.0712 0.0198 186 LEU A C 1307 O O . LEU A 165 ? 0.2328 0.1967 0.1502 -0.0356 -0.0838 0.0229 186 LEU A O 1308 C CB . LEU A 165 ? 0.3321 0.2781 0.2388 -0.0428 -0.0481 0.0166 186 LEU A CB 1309 C CG . LEU A 165 ? 0.3836 0.3051 0.2669 -0.0487 -0.0492 0.0170 186 LEU A CG 1310 C CD1 . LEU A 165 ? 0.3033 0.2098 0.1653 -0.0627 -0.0507 0.0166 186 LEU A CD1 1311 C CD2 . LEU A 165 ? 0.3876 0.3015 0.2703 -0.0471 -0.0359 0.0146 186 LEU A CD2 1312 N N . TRP A 166 ? 0.2620 0.2427 0.2039 -0.0214 -0.0682 0.0182 187 TRP A N 1313 C CA . TRP A 166 ? 0.2692 0.2516 0.2188 -0.0104 -0.0780 0.0191 187 TRP A CA 1314 C C . TRP A 166 ? 0.2511 0.2619 0.2292 -0.0011 -0.0791 0.0166 187 TRP A C 1315 O O . TRP A 166 ? 0.2657 0.2798 0.2543 0.0102 -0.0786 0.0141 187 TRP A O 1316 C CB . TRP A 166 ? 0.2836 0.2491 0.2242 -0.0052 -0.0731 0.0175 187 TRP A CB 1317 C CG . TRP A 166 ? 0.2837 0.2247 0.2001 -0.0145 -0.0686 0.0186 187 TRP A CG 1318 C CD1 . TRP A 166 ? 0.2814 0.2171 0.1936 -0.0170 -0.0570 0.0157 187 TRP A CD1 1319 C CD2 . TRP A 166 ? 0.3213 0.2412 0.2148 -0.0232 -0.0749 0.0225 187 TRP A CD2 1320 N NE1 . TRP A 166 ? 0.2648 0.1789 0.1562 -0.0263 -0.0541 0.0167 187 TRP A NE1 1321 C CE2 . TRP A 166 ? 0.2947 0.1971 0.1717 -0.0310 -0.0642 0.0207 187 TRP A CE2 1322 C CE3 . TRP A 166 ? 0.3431 0.2582 0.2280 -0.0258 -0.0890 0.0276 187 TRP A CE3 1323 C CZ2 . TRP A 166 ? 0.3294 0.2079 0.1796 -0.0419 -0.0647 0.0228 187 TRP A CZ2 1324 C CZ3 . TRP A 166 ? 0.3562 0.2458 0.2108 -0.0371 -0.0917 0.0308 187 TRP A CZ3 1325 C CH2 . TRP A 166 ? 0.3418 0.2129 0.1787 -0.0455 -0.0783 0.0279 187 TRP A CH2 1326 N N . SER A 167 ? 0.2250 0.2556 0.2154 -0.0068 -0.0789 0.0163 188 SER A N 1327 C CA . SER A 167 ? 0.2121 0.2724 0.2315 0.0002 -0.0786 0.0133 188 SER A CA 1328 C C . SER A 167 ? 0.2047 0.2723 0.2309 0.0059 -0.0647 0.0084 188 SER A C 1329 O O . SER A 167 ? 0.1749 0.2540 0.2174 0.0170 -0.0636 0.0045 188 SER A O 1330 C CB . SER A 167 ? 0.2033 0.2707 0.2385 0.0125 -0.0922 0.0146 188 SER A CB 1331 O OG . SER A 167 ? 0.2354 0.3015 0.2659 0.0066 -0.1075 0.0200 188 SER A OG 1332 N N . HIS A 168 ? 0.2147 0.2744 0.2276 -0.0016 -0.0542 0.0087 189 HIS A N 1333 C CA . HIS A 168 ? 0.2079 0.2739 0.2227 0.0016 -0.0424 0.0057 189 HIS A CA 1334 C C . HIS A 168 ? 0.2084 0.2635 0.2171 0.0102 -0.0416 0.0026 189 HIS A C 1335 O O . HIS A 168 ? 0.1860 0.2504 0.1999 0.0149 -0.0346 -0.0019 189 HIS A O 1336 C CB . HIS A 168 ? 0.1731 0.2664 0.2088 0.0027 -0.0369 0.0023 189 HIS A CB 1337 C CG . HIS A 168 ? 0.1869 0.2885 0.2247 -0.0092 -0.0339 0.0050 189 HIS A CG 1338 N ND1 . HIS A 168 ? 0.1891 0.2861 0.2163 -0.0166 -0.0234 0.0074 189 HIS A ND1 1339 C CD2 . HIS A 168 ? 0.1838 0.2951 0.2309 -0.0161 -0.0407 0.0061 189 HIS A CD2 1340 C CE1 . HIS A 168 ? 0.1995 0.3011 0.2294 -0.0276 -0.0222 0.0093 189 HIS A CE1 1341 N NE2 . HIS A 168 ? 0.2059 0.3172 0.2477 -0.0284 -0.0327 0.0079 189 HIS A NE2 1342 N N . SER A 169 ? 0.2305 0.2644 0.2259 0.0105 -0.0479 0.0045 190 SER A N 1343 C CA . SER A 169 ? 0.2582 0.2795 0.2461 0.0159 -0.0463 0.0012 190 SER A CA 1344 C C . SER A 169 ? 0.2597 0.2808 0.2392 0.0116 -0.0372 0.0004 190 SER A C 1345 O O . SER A 169 ? 0.2472 0.2684 0.2250 0.0153 -0.0338 -0.0042 190 SER A O 1346 C CB . SER A 169 ? 0.3064 0.3031 0.2798 0.0149 -0.0539 0.0040 190 SER A CB 1347 O OG . SER A 169 ? 0.3694 0.3545 0.3278 0.0050 -0.0507 0.0071 190 SER A OG 1348 N N . TYR A 170 ? 0.2507 0.2712 0.2250 0.0040 -0.0339 0.0049 191 TYR A N 1349 C CA . TYR A 170 ? 0.2295 0.2533 0.1996 0.0015 -0.0266 0.0062 191 TYR A CA 1350 C C . TYR A 170 ? 0.2133 0.2521 0.1896 -0.0009 -0.0211 0.0085 191 TYR A C 1351 O O . TYR A 170 ? 0.2091 0.2527 0.1914 -0.0044 -0.0220 0.0099 191 TYR A O 1352 C CB . TYR A 170 ? 0.1911 0.2011 0.1521 -0.0042 -0.0246 0.0101 191 TYR A CB 1353 C CG . TYR A 170 ? 0.1892 0.1838 0.1419 -0.0052 -0.0267 0.0085 191 TYR A CG 1354 C CD1 . TYR A 170 ? 0.1550 0.1503 0.1066 -0.0027 -0.0264 0.0050 191 TYR A CD1 1355 C CD2 . TYR A 170 ? 0.2002 0.1790 0.1443 -0.0106 -0.0281 0.0100 191 TYR A CD2 1356 C CE1 . TYR A 170 ? 0.2164 0.1975 0.1607 -0.0058 -0.0270 0.0032 191 TYR A CE1 1357 C CE2 . TYR A 170 ? 0.2421 0.2058 0.1769 -0.0134 -0.0280 0.0085 191 TYR A CE2 1358 C CZ . TYR A 170 ? 0.2671 0.2325 0.2033 -0.0111 -0.0272 0.0053 191 TYR A CZ 1359 O OH . TYR A 170 ? 0.3023 0.2532 0.2299 -0.0158 -0.0259 0.0035 191 TYR A OH 1360 N N . LYS A 171 ? 0.1821 0.2274 0.1551 -0.0004 -0.0159 0.0094 192 LYS A N 1361 C CA . LYS A 171 ? 0.2208 0.2716 0.1927 -0.0048 -0.0100 0.0149 192 LYS A CA 1362 C C . LYS A 171 ? 0.2023 0.2442 0.1663 -0.0051 -0.0091 0.0202 192 LYS A C 1363 O O . LYS A 171 ? 0.2187 0.2583 0.1800 -0.0023 -0.0121 0.0179 192 LYS A O 1364 C CB . LYS A 171 ? 0.1955 0.2620 0.1686 -0.0042 -0.0047 0.0130 192 LYS A CB 1365 C CG . LYS A 171 ? 0.1924 0.2611 0.1572 -0.0007 -0.0048 0.0098 192 LYS A CG 1366 C CD . LYS A 171 ? 0.1874 0.2699 0.1484 -0.0022 0.0023 0.0079 192 LYS A CD 1367 C CE . LYS A 171 ? 0.1906 0.2743 0.1400 -0.0004 0.0016 0.0030 192 LYS A CE 1368 N NZ . LYS A 171 ? 0.2298 0.3250 0.1711 -0.0031 0.0097 -0.0004 192 LYS A NZ 1369 N N . VAL A 172 ? 0.1847 0.2218 0.1467 -0.0085 -0.0051 0.0270 193 VAL A N 1370 C CA . VAL A 172 ? 0.2120 0.2419 0.1708 -0.0067 -0.0044 0.0330 193 VAL A CA 1371 C C . VAL A 172 ? 0.2208 0.2609 0.1742 -0.0047 -0.0043 0.0372 193 VAL A C 1372 O O . VAL A 172 ? 0.2126 0.2558 0.1616 -0.0075 -0.0002 0.0413 193 VAL A O 1373 C CB . VAL A 172 ? 0.2635 0.2799 0.2221 -0.0101 0.0008 0.0389 193 VAL A CB 1374 C CG1 . VAL A 172 ? 0.2689 0.2793 0.2288 -0.0053 0.0017 0.0455 193 VAL A CG1 1375 C CG2 . VAL A 172 ? 0.1926 0.1978 0.1519 -0.0147 0.0008 0.0340 193 VAL A CG2 1376 N N . SER A 173 ? 0.2242 0.2695 0.1762 -0.0013 -0.0090 0.0360 194 SER A N 1377 C CA . SER A 173 ? 0.2514 0.3065 0.1948 -0.0006 -0.0110 0.0400 194 SER A CA 1378 C C . SER A 173 ? 0.3045 0.3539 0.2469 0.0012 -0.0107 0.0525 194 SER A C 1379 O O . SER A 173 ? 0.3259 0.3659 0.2774 0.0036 -0.0098 0.0553 194 SER A O 1380 C CB . SER A 173 ? 0.2054 0.2675 0.1481 0.0009 -0.0174 0.0347 194 SER A CB 1381 O OG . SER A 173 ? 0.2501 0.3218 0.1814 0.0000 -0.0206 0.0385 194 SER A OG 1382 N N . ASN A 174 ? 0.3133 0.3666 0.2439 0.0001 -0.0108 0.0601 195 ASN A N 1383 C CA . ASN A 174 ? 0.3015 0.3483 0.2304 0.0038 -0.0129 0.0737 195 ASN A CA 1384 C C . ASN A 174 ? 0.2822 0.3398 0.2140 0.0088 -0.0232 0.0772 195 ASN A C 1385 O O . ASN A 174 ? 0.2812 0.3364 0.2158 0.0142 -0.0273 0.0889 195 ASN A O 1386 C CB . ASN A 174 ? 0.3080 0.3508 0.2202 -0.0003 -0.0091 0.0829 195 ASN A CB 1387 C CG . ASN A 174 ? 0.3369 0.3658 0.2484 0.0043 -0.0100 0.0982 195 ASN A CG 1388 O OD1 . ASN A 174 ? 0.2914 0.3078 0.2163 0.0082 -0.0069 0.0994 195 ASN A OD1 1389 N ND2 . ASN A 174 ? 0.4352 0.4644 0.3299 0.0043 -0.0142 0.1100 195 ASN A ND2 1390 N N . TYR A 175 ? 0.2905 0.3602 0.2223 0.0069 -0.0277 0.0670 196 TYR A N 1391 C CA . TYR A 175 ? 0.3056 0.3882 0.2427 0.0094 -0.0378 0.0678 196 TYR A CA 1392 C C . TYR A 175 ? 0.3127 0.3935 0.2722 0.0137 -0.0375 0.0658 196 TYR A C 1393 O O . TYR A 175 ? 0.2749 0.3444 0.2406 0.0127 -0.0300 0.0595 196 TYR A O 1394 C CB . TYR A 175 ? 0.2779 0.3707 0.2055 0.0036 -0.0410 0.0557 196 TYR A CB 1395 C CG . TYR A 175 ? 0.2934 0.3914 0.1973 -0.0013 -0.0419 0.0569 196 TYR A CG 1396 C CD1 . TYR A 175 ? 0.3060 0.4099 0.1995 -0.0013 -0.0504 0.0670 196 TYR A CD1 1397 C CD2 . TYR A 175 ? 0.2943 0.3896 0.1876 -0.0059 -0.0336 0.0468 196 TYR A CD2 1398 C CE1 . TYR A 175 ? 0.3396 0.4419 0.2104 -0.0071 -0.0491 0.0654 196 TYR A CE1 1399 C CE2 . TYR A 175 ? 0.3089 0.4085 0.1796 -0.0114 -0.0317 0.0463 196 TYR A CE2 1400 C CZ . TYR A 175 ? 0.3680 0.4688 0.2268 -0.0126 -0.0389 0.0550 196 TYR A CZ 1401 O OH . TYR A 175 ? 0.4387 0.5381 0.2751 -0.0188 -0.0354 0.0524 196 TYR A OH 1402 N N . SER A 176 ? 0.3426 0.4361 0.3141 0.0175 -0.0458 0.0702 197 SER A N 1403 C CA . SER A 176 ? 0.3619 0.4557 0.3569 0.0215 -0.0434 0.0682 197 SER A CA 1404 C C . SER A 176 ? 0.3590 0.4648 0.3627 0.0165 -0.0465 0.0570 197 SER A C 1405 O O . SER A 176 ? 0.3171 0.4346 0.3109 0.0111 -0.0538 0.0523 197 SER A O 1406 C CB . SER A 176 ? 0.4191 0.5188 0.4300 0.0311 -0.0482 0.0815 197 SER A CB 1407 O OG . SER A 176 ? 0.4829 0.5638 0.4882 0.0357 -0.0419 0.0910 197 SER A OG 1408 N N . ARG A 177 ? 0.3617 0.4628 0.3823 0.0172 -0.0397 0.0522 198 ARG A N 1409 C CA . ARG A 177 ? 0.3514 0.4628 0.3830 0.0118 -0.0408 0.0429 198 ARG A CA 1410 C C . ARG A 177 ? 0.3904 0.5272 0.4295 0.0118 -0.0536 0.0464 198 ARG A C 1411 O O . ARG A 177 ? 0.4233 0.5710 0.4751 0.0199 -0.0591 0.0576 198 ARG A O 1412 C CB . ARG A 177 ? 0.3324 0.4397 0.3851 0.0142 -0.0315 0.0412 198 ARG A CB 1413 C CG . ARG A 177 ? 0.3385 0.4198 0.3812 0.0120 -0.0195 0.0369 198 ARG A CG 1414 C CD . ARG A 177 ? 0.3419 0.4181 0.4024 0.0134 -0.0087 0.0346 198 ARG A CD 1415 N NE . ARG A 177 ? 0.2988 0.3939 0.3774 0.0100 -0.0102 0.0295 198 ARG A NE 1416 C CZ . ARG A 177 ? 0.3023 0.3945 0.3737 -0.0004 -0.0084 0.0199 198 ARG A CZ 1417 N NH1 . ARG A 177 ? 0.2352 0.3057 0.2823 -0.0062 -0.0062 0.0154 198 ARG A NH1 1418 N NH2 . ARG A 177 ? 0.2875 0.3983 0.3769 -0.0051 -0.0091 0.0152 198 ARG A NH2 1419 N N . GLY A 178 ? 0.3558 0.5009 0.3861 0.0026 -0.0590 0.0373 199 GLY A N 1420 C CA . GLY A 178 ? 0.3631 0.5343 0.4008 -0.0001 -0.0721 0.0389 199 GLY A CA 1421 C C . GLY A 178 ? 0.3690 0.5458 0.3832 -0.0018 -0.0824 0.0436 199 GLY A C 1422 O O . GLY A 178 ? 0.3800 0.5775 0.3944 -0.0061 -0.0950 0.0445 199 GLY A O 1423 N N . SER A 179 ? 0.2735 0.4323 0.2664 0.0001 -0.0768 0.0460 200 SER A N 1424 C CA . SER A 179 ? 0.2970 0.4585 0.2652 -0.0023 -0.0836 0.0503 200 SER A CA 1425 C C . SER A 179 ? 0.2915 0.4491 0.2396 -0.0131 -0.0824 0.0354 200 SER A C 1426 O O . SER A 179 ? 0.2761 0.4321 0.2051 -0.0171 -0.0856 0.0341 200 SER A O 1427 C CB . SER A 179 ? 0.2959 0.4406 0.2505 0.0026 -0.0760 0.0579 200 SER A CB 1428 O OG . SER A 179 ? 0.2881 0.4159 0.2397 0.0005 -0.0638 0.0475 200 SER A OG 1429 N N . GLY A 180 ? 0.2807 0.4306 0.2326 -0.0173 -0.0758 0.0234 201 GLY A N 1430 C CA . GLY A 180 ? 0.2928 0.4351 0.2254 -0.0260 -0.0733 0.0092 201 GLY A CA 1431 C C . GLY A 180 ? 0.3169 0.4452 0.2301 -0.0239 -0.0651 0.0078 201 GLY A C 1432 O O . GLY A 180 ? 0.3616 0.4848 0.2564 -0.0295 -0.0627 -0.0024 201 GLY A O 1433 N N . ARG A 181 ? 0.2737 0.3951 0.1923 -0.0161 -0.0595 0.0171 202 ARG A N 1434 C CA . ARG A 181 ? 0.2826 0.3940 0.1873 -0.0147 -0.0508 0.0160 202 ARG A CA 1435 C C . ARG A 181 ? 0.2772 0.3751 0.1950 -0.0092 -0.0420 0.0163 202 ARG A C 1436 O O . ARG A 181 ? 0.2791 0.3719 0.1918 -0.0075 -0.0353 0.0181 202 ARG A O 1437 C CB . ARG A 181 ? 0.2993 0.4166 0.1914 -0.0136 -0.0534 0.0286 202 ARG A CB 1438 C CG . ARG A 181 ? 0.3238 0.4462 0.2005 -0.0193 -0.0600 0.0273 202 ARG A CG 1439 C CD . ARG A 181 ? 0.3074 0.4246 0.1653 -0.0258 -0.0533 0.0130 202 ARG A CD 1440 N NE . ARG A 181 ? 0.3333 0.4535 0.1742 -0.0319 -0.0591 0.0120 202 ARG A NE 1441 C CZ . ARG A 181 ? 0.3119 0.4363 0.1520 -0.0376 -0.0657 0.0038 202 ARG A CZ 1442 N NH1 . ARG A 181 ? 0.2822 0.4067 0.1372 -0.0384 -0.0661 -0.0041 202 ARG A NH1 1443 N NH2 . ARG A 181 ? 0.3395 0.4669 0.1625 -0.0436 -0.0718 0.0035 202 ARG A NH2 1444 N N . CYS A 182 ? 0.2420 0.3350 0.1757 -0.0079 -0.0421 0.0147 203 CYS A N 1445 C CA . CYS A 182 ? 0.2298 0.3085 0.1714 -0.0050 -0.0351 0.0129 203 CYS A CA 1446 C C . CYS A 182 ? 0.2152 0.2862 0.1641 -0.0076 -0.0351 0.0056 203 CYS A C 1447 O O . CYS A 182 ? 0.1914 0.2703 0.1454 -0.0111 -0.0397 0.0043 203 CYS A O 1448 C CB . CYS A 182 ? 0.1897 0.2652 0.1406 -0.0006 -0.0325 0.0239 203 CYS A CB 1449 S SG . CYS A 182 ? 0.2738 0.3592 0.2394 0.0023 -0.0378 0.0330 203 CYS A SG 1450 N N . ILE A 183 ? 0.1919 0.2480 0.1412 -0.0066 -0.0305 0.0014 204 ILE A N 1451 C CA . ILE A 183 ? 0.2005 0.2442 0.1523 -0.0098 -0.0299 -0.0042 204 ILE A CA 1452 C C . ILE A 183 ? 0.2376 0.2790 0.2003 -0.0102 -0.0275 0.0013 204 ILE A C 1453 O O . ILE A 183 ? 0.2551 0.2927 0.2210 -0.0069 -0.0242 0.0074 204 ILE A O 1454 C CB . ILE A 183 ? 0.1865 0.2138 0.1332 -0.0076 -0.0274 -0.0087 204 ILE A CB 1455 C CG1 . ILE A 183 ? 0.1812 0.2083 0.1197 -0.0066 -0.0277 -0.0170 204 ILE A CG1 1456 C CG2 . ILE A 183 ? 0.1764 0.1866 0.1227 -0.0113 -0.0267 -0.0108 204 ILE A CG2 1457 C CD1 . ILE A 183 ? 0.2004 0.2255 0.1326 -0.0126 -0.0298 -0.0249 204 ILE A CD1 1458 N N . GLN A 184 ? 0.2080 0.2524 0.1769 -0.0152 -0.0282 -0.0015 205 GLN A N 1459 C CA . GLN A 184 ? 0.2234 0.2650 0.2035 -0.0163 -0.0233 0.0013 205 GLN A CA 1460 C C . GLN A 184 ? 0.2538 0.2739 0.2254 -0.0213 -0.0189 -0.0034 205 GLN A C 1461 O O . GLN A 184 ? 0.2781 0.2902 0.2421 -0.0265 -0.0203 -0.0098 205 GLN A O 1462 C CB . GLN A 184 ? 0.2327 0.2927 0.2286 -0.0192 -0.0251 0.0013 205 GLN A CB 1463 C CG . GLN A 184 ? 0.2794 0.3599 0.2846 -0.0129 -0.0309 0.0092 205 GLN A CG 1464 C CD . GLN A 184 ? 0.2991 0.4030 0.3225 -0.0152 -0.0361 0.0094 205 GLN A CD 1465 O OE1 . GLN A 184 ? 0.3534 0.4740 0.3752 -0.0158 -0.0455 0.0109 205 GLN A OE1 1466 N NE2 . GLN A 184 ? 0.2503 0.3565 0.2910 -0.0171 -0.0298 0.0077 205 GLN A NE2 1467 N N . MET A 185 ? 0.2747 0.2834 0.2453 -0.0203 -0.0137 0.0000 206 MET A N 1468 C CA . MET A 185 ? 0.2636 0.2516 0.2244 -0.0263 -0.0093 -0.0027 206 MET A CA 1469 C C . MET A 185 ? 0.2540 0.2446 0.2231 -0.0333 -0.0032 -0.0059 206 MET A C 1470 O O . MET A 185 ? 0.2677 0.2436 0.2268 -0.0413 -0.0008 -0.0101 206 MET A O 1471 C CB . MET A 185 ? 0.2796 0.2575 0.2367 -0.0248 -0.0052 0.0015 206 MET A CB 1472 C CG . MET A 185 ? 0.3373 0.2932 0.2767 -0.0288 -0.0063 0.0007 206 MET A CG 1473 S SD . MET A 185 ? 0.4428 0.3923 0.3777 -0.0276 -0.0046 0.0051 206 MET A SD 1474 C CE . MET A 185 ? 0.2413 0.1788 0.1735 -0.0352 0.0075 0.0032 206 MET A CE 1475 N N . TRP A 186 ? 0.2324 0.2405 0.2203 -0.0303 0.0002 -0.0032 207 TRP A N 1476 C CA . TRP A 186 ? 0.2113 0.2281 0.2143 -0.0359 0.0073 -0.0066 207 TRP A CA 1477 C C . TRP A 186 ? 0.2117 0.2554 0.2320 -0.0356 0.0004 -0.0076 207 TRP A C 1478 O O . TRP A 186 ? 0.1959 0.2576 0.2277 -0.0274 -0.0055 -0.0020 207 TRP A O 1479 C CB . TRP A 186 ? 0.1824 0.2015 0.1992 -0.0315 0.0167 -0.0035 207 TRP A CB 1480 C CG . TRP A 186 ? 0.2449 0.2382 0.2450 -0.0364 0.0263 -0.0052 207 TRP A CG 1481 C CD1 . TRP A 186 ? 0.2481 0.2253 0.2332 -0.0337 0.0257 -0.0019 207 TRP A CD1 1482 C CD2 . TRP A 186 ? 0.2487 0.2295 0.2433 -0.0468 0.0377 -0.0109 207 TRP A CD2 1483 N NE1 . TRP A 186 ? 0.2656 0.2212 0.2352 -0.0418 0.0348 -0.0052 207 TRP A NE1 1484 C CE2 . TRP A 186 ? 0.2561 0.2123 0.2297 -0.0499 0.0428 -0.0106 207 TRP A CE2 1485 C CE3 . TRP A 186 ? 0.2775 0.2660 0.2824 -0.0552 0.0446 -0.0166 207 TRP A CE3 1486 C CZ2 . TRP A 186 ? 0.2818 0.2193 0.2411 -0.0609 0.0547 -0.0154 207 TRP A CZ2 1487 C CZ3 . TRP A 186 ? 0.3067 0.2769 0.2992 -0.0662 0.0577 -0.0215 207 TRP A CZ3 1488 C CH2 . TRP A 186 ? 0.2974 0.2413 0.2655 -0.0690 0.0626 -0.0207 207 TRP A CH2 1489 N N . PHE A 187 ? 0.1675 0.2132 0.1879 -0.0457 0.0006 -0.0143 208 PHE A N 1490 C CA . PHE A 187 ? 0.1651 0.2387 0.2033 -0.0479 -0.0062 -0.0162 208 PHE A CA 1491 C C . PHE A 187 ? 0.2327 0.3094 0.2790 -0.0612 0.0003 -0.0239 208 PHE A C 1492 O O . PHE A 187 ? 0.2226 0.2741 0.2509 -0.0701 0.0070 -0.0284 208 PHE A O 1493 C CB . PHE A 187 ? 0.2033 0.2785 0.2270 -0.0479 -0.0175 -0.0177 208 PHE A CB 1494 C CG . PHE A 187 ? 0.2370 0.2852 0.2368 -0.0552 -0.0162 -0.0243 208 PHE A CG 1495 C CD1 . PHE A 187 ? 0.2424 0.2682 0.2237 -0.0491 -0.0161 -0.0221 208 PHE A CD1 1496 C CD2 . PHE A 187 ? 0.2457 0.2903 0.2430 -0.0679 -0.0150 -0.0324 208 PHE A CD2 1497 C CE1 . PHE A 187 ? 0.2583 0.2586 0.2202 -0.0534 -0.0158 -0.0268 208 PHE A CE1 1498 C CE2 . PHE A 187 ? 0.3063 0.3213 0.2807 -0.0734 -0.0135 -0.0374 208 PHE A CE2 1499 C CZ . PHE A 187 ? 0.2829 0.2756 0.2402 -0.0650 -0.0143 -0.0341 208 PHE A CZ 1500 N N . ASP A 188 ? 0.2534 0.3613 0.3268 -0.0633 -0.0021 -0.0251 209 ASP A N 1501 C CA . ASP A 188 ? 0.2937 0.4075 0.3745 -0.0788 0.0027 -0.0338 209 ASP A CA 1502 C C . ASP A 188 ? 0.3204 0.4387 0.3903 -0.0863 -0.0091 -0.0386 209 ASP A C 1503 O O . ASP A 188 ? 0.2940 0.4196 0.3576 -0.0786 -0.0206 -0.0350 209 ASP A O 1504 C CB . ASP A 188 ? 0.3147 0.4632 0.4344 -0.0787 0.0066 -0.0341 209 ASP A CB 1505 C CG . ASP A 188 ? 0.3549 0.5391 0.4959 -0.0715 -0.0088 -0.0294 209 ASP A CG 1506 O OD1 . ASP A 188 ? 0.3894 0.5896 0.5326 -0.0822 -0.0177 -0.0348 209 ASP A OD1 1507 O OD2 . ASP A 188 ? 0.3634 0.5573 0.5161 -0.0560 -0.0126 -0.0200 209 ASP A OD2 1508 N N . SER A 189 ? 0.3585 0.4716 0.4246 -0.1025 -0.0053 -0.0475 210 SER A N 1509 C CA . SER A 189 ? 0.4247 0.5344 0.4748 -0.1108 -0.0148 -0.0538 210 SER A CA 1510 C C . SER A 189 ? 0.3856 0.5329 0.4577 -0.1197 -0.0242 -0.0583 210 SER A C 1511 O O . SER A 189 ? 0.3863 0.5289 0.4436 -0.1306 -0.0303 -0.0660 210 SER A O 1512 C CB . SER A 189 ? 0.4775 0.5499 0.5017 -0.1238 -0.0071 -0.0610 210 SER A CB 1513 O OG . SER A 189 ? 0.5363 0.5783 0.5330 -0.1146 -0.0096 -0.0583 210 SER A OG 1514 N N . ALA A 190 ? 0.3526 0.5369 0.4597 -0.1148 -0.0261 -0.0537 211 ALA A N 1515 C CA . ALA A 190 ? 0.3683 0.5930 0.5020 -0.1252 -0.0352 -0.0582 211 ALA A CA 1516 C C . ALA A 190 ? 0.3590 0.5924 0.4775 -0.1277 -0.0522 -0.0597 211 ALA A C 1517 O O . ALA A 190 ? 0.3759 0.6135 0.4934 -0.1386 -0.0559 -0.0659 211 ALA A O 1518 C CB . ALA A 190 ? 0.3431 0.6078 0.5205 -0.1145 -0.0362 -0.0508 211 ALA A CB 1519 N N . GLN A 191 ? 0.3485 0.5768 0.4511 -0.1144 -0.0604 -0.0524 212 GLN A N 1520 C CA . GLN A 191 ? 0.3843 0.6129 0.4658 -0.1154 -0.0734 -0.0535 212 GLN A CA 1521 C C . GLN A 191 ? 0.3765 0.5664 0.4189 -0.1181 -0.0693 -0.0602 212 GLN A C 1522 O O . GLN A 191 ? 0.4161 0.6010 0.4381 -0.1132 -0.0765 -0.0590 212 GLN A O 1523 C CB . GLN A 191 ? 0.3790 0.6301 0.4687 -0.0998 -0.0860 -0.0406 212 GLN A CB 1524 C CG . GLN A 191 ? 0.4121 0.7000 0.5385 -0.0970 -0.0940 -0.0349 212 GLN A CG 1525 C CD . GLN A 191 ? 0.4249 0.7287 0.5551 -0.0820 -0.1079 -0.0215 212 GLN A CD 1526 O OE1 . GLN A 191 ? 0.4551 0.7433 0.5556 -0.0774 -0.1126 -0.0180 212 GLN A OE1 1527 N NE2 . GLN A 191 ? 0.3874 0.7200 0.5541 -0.0741 -0.1135 -0.0141 212 GLN A NE2 1528 N N . GLY A 192 ? 0.3072 0.4676 0.3391 -0.1247 -0.0569 -0.0666 213 GLY A N 1529 C CA . GLY A 192 ? 0.2777 0.3981 0.2765 -0.1226 -0.0520 -0.0710 213 GLY A CA 1530 C C . GLY A 192 ? 0.2600 0.3619 0.2540 -0.1054 -0.0458 -0.0614 213 GLY A C 1531 O O . GLY A 192 ? 0.2561 0.3734 0.2695 -0.0958 -0.0446 -0.0519 213 GLY A O 1532 N N . ASN A 193 ? 0.2491 0.3175 0.2183 -0.1018 -0.0415 -0.0644 214 ASN A N 1533 C CA . ASN A 193 ? 0.2529 0.3054 0.2160 -0.0865 -0.0377 -0.0562 214 ASN A CA 1534 C C . ASN A 193 ? 0.2366 0.3053 0.1967 -0.0763 -0.0450 -0.0514 214 ASN A C 1535 O O . ASN A 193 ? 0.2378 0.3022 0.1813 -0.0785 -0.0484 -0.0580 214 ASN A O 1536 C CB . ASN A 193 ? 0.2926 0.3059 0.2334 -0.0863 -0.0318 -0.0611 214 ASN A CB 1537 C CG . ASN A 193 ? 0.3037 0.3030 0.2402 -0.0721 -0.0291 -0.0532 214 ASN A CG 1538 O OD1 . ASN A 193 ? 0.3150 0.3305 0.2575 -0.0621 -0.0321 -0.0467 214 ASN A OD1 1539 N ND2 . ASN A 193 ? 0.2896 0.2582 0.2147 -0.0720 -0.0240 -0.0531 214 ASN A ND2 1540 N N . PRO A 194 ? 0.2143 0.2999 0.1890 -0.0661 -0.0465 -0.0404 215 PRO A N 1541 C CA . PRO A 194 ? 0.2490 0.3513 0.2209 -0.0581 -0.0538 -0.0340 215 PRO A CA 1542 C C . PRO A 194 ? 0.2280 0.3113 0.1807 -0.0506 -0.0504 -0.0344 215 PRO A C 1543 O O . PRO A 194 ? 0.2363 0.3281 0.1789 -0.0478 -0.0545 -0.0329 215 PRO A O 1544 C CB . PRO A 194 ? 0.2659 0.3836 0.2592 -0.0489 -0.0537 -0.0218 215 PRO A CB 1545 C CG . PRO A 194 ? 0.2663 0.3665 0.2666 -0.0492 -0.0431 -0.0225 215 PRO A CG 1546 C CD . PRO A 194 ? 0.2199 0.3067 0.2123 -0.0623 -0.0402 -0.0338 215 PRO A CD 1547 N N . ASN A 195 ? 0.1604 0.1912 0.1889 0.0161 -0.0559 0.0009 216 ASN A N 1548 C CA . ASN A 195 ? 0.1827 0.2072 0.1924 0.0153 -0.0616 -0.0025 216 ASN A CA 1549 C C . ASN A 195 ? 0.2155 0.2457 0.2293 0.0153 -0.0724 -0.0088 216 ASN A C 1550 O O . ASN A 195 ? 0.2248 0.2532 0.2290 0.0172 -0.0751 -0.0110 216 ASN A O 1551 C CB . ASN A 195 ? 0.1856 0.1949 0.1788 0.0099 -0.0567 -0.0008 216 ASN A CB 1552 C CG . ASN A 195 ? 0.2273 0.2247 0.2069 0.0071 -0.0436 0.0009 216 ASN A CG 1553 O OD1 . ASN A 195 ? 0.1952 0.1931 0.1762 0.0107 -0.0370 0.0014 216 ASN A OD1 1554 N ND2 . ASN A 195 ? 0.2457 0.2282 0.2086 0.0010 -0.0373 0.0021 216 ASN A ND2 1555 N N . GLU A 196 ? 0.1763 0.2121 0.2062 0.0118 -0.0760 -0.0132 217 GLU A N 1556 C CA . GLU A 196 ? 0.2265 0.2620 0.2570 0.0097 -0.0825 -0.0224 217 GLU A CA 1557 C C . GLU A 196 ? 0.2252 0.2698 0.2431 0.0146 -0.0896 -0.0267 217 GLU A C 1558 O O . GLU A 196 ? 0.2332 0.2697 0.2392 0.0163 -0.0890 -0.0313 217 GLU A O 1559 C CB . GLU A 196 ? 0.2639 0.3040 0.3153 0.0011 -0.0840 -0.0303 217 GLU A CB 1560 C CG . GLU A 196 ? 0.3442 0.3690 0.4059 -0.0035 -0.0723 -0.0255 217 GLU A CG 1561 C CD . GLU A 196 ? 0.4098 0.4388 0.4992 -0.0149 -0.0694 -0.0346 217 GLU A CD 1562 O OE1 . GLU A 196 ? 0.4146 0.4644 0.5168 -0.0209 -0.0808 -0.0467 217 GLU A OE1 1563 O OE2 . GLU A 196 ? 0.4218 0.4333 0.5194 -0.0189 -0.0553 -0.0300 217 GLU A OE2 1564 N N . GLU A 197 ? 0.2035 0.2635 0.2238 0.0177 -0.0928 -0.0229 218 GLU A N 1565 C CA . GLU A 197 ? 0.2202 0.2851 0.2228 0.0227 -0.0942 -0.0213 218 GLU A CA 1566 C C . GLU A 197 ? 0.1930 0.2442 0.1779 0.0295 -0.0866 -0.0170 218 GLU A C 1567 O O . GLU A 197 ? 0.2000 0.2458 0.1664 0.0331 -0.0863 -0.0204 218 GLU A O 1568 C CB . GLU A 197 ? 0.2663 0.3512 0.2786 0.0280 -0.0987 -0.0122 218 GLU A CB 1569 C CG . GLU A 197 ? 0.3543 0.4390 0.3447 0.0383 -0.0988 -0.0041 218 GLU A CG 1570 C CD . GLU A 197 ? 0.5388 0.6402 0.5416 0.0492 -0.1015 0.0105 218 GLU A CD 1571 O OE1 . GLU A 197 ? 0.5222 0.6326 0.5517 0.0520 -0.0985 0.0156 218 GLU A OE1 1572 O OE2 . GLU A 197 ? 0.5252 0.6297 0.5107 0.0572 -0.1057 0.0176 218 GLU A OE2 1573 N N . VAL A 198 ? 0.2001 0.2452 0.1894 0.0305 -0.0806 -0.0118 219 VAL A N 1574 C CA . VAL A 198 ? 0.2070 0.2409 0.1848 0.0319 -0.0705 -0.0094 219 VAL A CA 1575 C C . VAL A 198 ? 0.2331 0.2627 0.2110 0.0289 -0.0704 -0.0157 219 VAL A C 1576 O O . VAL A 198 ? 0.2327 0.2581 0.2032 0.0314 -0.0638 -0.0169 219 VAL A O 1577 C CB . VAL A 198 ? 0.2088 0.2352 0.1894 0.0278 -0.0609 -0.0051 219 VAL A CB 1578 C CG1 . VAL A 198 ? 0.2100 0.2284 0.1837 0.0244 -0.0516 -0.0071 219 VAL A CG1 1579 C CG2 . VAL A 198 ? 0.2021 0.2287 0.1859 0.0338 -0.0540 0.0030 219 VAL A CG2 1580 N N . ALA A 199 ? 0.1987 0.2282 0.1874 0.0248 -0.0750 -0.0180 220 ALA A N 1581 C CA . ALA A 199 ? 0.2001 0.2267 0.1950 0.0253 -0.0741 -0.0206 220 ALA A CA 1582 C C . ALA A 199 ? 0.2103 0.2319 0.1972 0.0286 -0.0716 -0.0282 220 ALA A C 1583 O O . ALA A 199 ? 0.2493 0.2676 0.2379 0.0318 -0.0642 -0.0298 220 ALA A O 1584 C CB . ALA A 199 ? 0.1841 0.2068 0.1891 0.0234 -0.0773 -0.0183 220 ALA A CB 1585 N N . ARG A 200 ? 0.2313 0.2536 0.2096 0.0269 -0.0775 -0.0335 221 ARG A N 1586 C CA A ARG A 200 ? 0.2601 0.2760 0.2212 0.0272 -0.0773 -0.0438 221 ARG A CA 1587 C CA B ARG A 200 ? 0.2580 0.2736 0.2193 0.0272 -0.0770 -0.0439 221 ARG A CA 1588 C C . ARG A 200 ? 0.2628 0.2755 0.2019 0.0339 -0.0705 -0.0410 221 ARG A C 1589 O O . ARG A 200 ? 0.2846 0.2846 0.2111 0.0361 -0.0604 -0.0467 221 ARG A O 1590 C CB A ARG A 200 ? 0.2741 0.2999 0.2329 0.0213 -0.0901 -0.0507 221 ARG A CB 1591 C CB B ARG A 200 ? 0.2715 0.2956 0.2299 0.0210 -0.0893 -0.0517 221 ARG A CB 1592 C CG A ARG A 200 ? 0.2977 0.3194 0.2329 0.0175 -0.0947 -0.0651 221 ARG A CG 1593 C CG B ARG A 200 ? 0.2963 0.3100 0.2392 0.0147 -0.0900 -0.0686 221 ARG A CG 1594 C CD A ARG A 200 ? 0.3047 0.3438 0.2513 0.0064 -0.1056 -0.0693 221 ARG A CD 1595 C CD B ARG A 200 ? 0.3053 0.3285 0.2629 0.0025 -0.1008 -0.0790 221 ARG A CD 1596 N NE A ARG A 200 ? 0.3081 0.3450 0.2836 -0.0020 -0.1056 -0.0752 221 ARG A NE 1597 N NE B ARG A 200 ? 0.3310 0.3515 0.2689 -0.0079 -0.1046 -0.0955 221 ARG A NE 1598 C CZ A ARG A 200 ? 0.2933 0.3457 0.2950 -0.0054 -0.1082 -0.0679 221 ARG A CZ 1599 C CZ B ARG A 200 ? 0.3500 0.3469 0.2818 -0.0166 -0.0972 -0.1152 221 ARG A CZ 1600 N NH1 A ARG A 200 ? 0.2475 0.3201 0.2533 -0.0007 -0.1115 -0.0545 221 ARG A NH1 1601 N NH1 B ARG A 200 ? 0.3283 0.3027 0.2778 -0.0132 -0.0792 -0.1107 221 ARG A NH1 1602 N NH2 A ARG A 200 ? 0.3043 0.3483 0.3296 -0.0133 -0.1051 -0.0742 221 ARG A NH2 1603 N NH2 B ARG A 200 ? 0.3464 0.3396 0.2554 -0.0293 -0.0992 -0.1298 221 ARG A NH2 1604 N N . PHE A 201 ? 0.2239 0.2440 0.1584 0.0380 -0.0719 -0.0312 222 PHE A N 1605 C CA . PHE A 201 ? 0.2599 0.2720 0.1730 0.0454 -0.0613 -0.0254 222 PHE A CA 1606 C C . PHE A 201 ? 0.2571 0.2600 0.1806 0.0446 -0.0445 -0.0255 222 PHE A C 1607 O O . PHE A 201 ? 0.2697 0.2603 0.1770 0.0482 -0.0319 -0.0279 222 PHE A O 1608 C CB . PHE A 201 ? 0.2502 0.2674 0.1609 0.0514 -0.0612 -0.0126 222 PHE A CB 1609 C CG . PHE A 201 ? 0.3037 0.3060 0.1924 0.0600 -0.0449 -0.0040 222 PHE A CG 1610 C CD1 . PHE A 201 ? 0.3414 0.3389 0.1951 0.0699 -0.0466 0.0001 222 PHE A CD1 1611 C CD2 . PHE A 201 ? 0.2987 0.2905 0.1995 0.0571 -0.0269 -0.0006 222 PHE A CD2 1612 C CE1 . PHE A 201 ? 0.3809 0.3589 0.2104 0.0796 -0.0274 0.0109 222 PHE A CE1 1613 C CE2 . PHE A 201 ? 0.2936 0.2670 0.1765 0.0636 -0.0067 0.0071 222 PHE A CE2 1614 C CZ . PHE A 201 ? 0.3529 0.3171 0.1997 0.0762 -0.0052 0.0145 222 PHE A CZ 1615 N N . TYR A 202 ? 0.2233 0.2336 0.1732 0.0392 -0.0441 -0.0233 223 TYR A N 1616 C CA . TYR A 202 ? 0.2226 0.2339 0.1907 0.0367 -0.0319 -0.0240 223 TYR A CA 1617 C C . TYR A 202 ? 0.2540 0.2661 0.2371 0.0384 -0.0282 -0.0293 223 TYR A C 1618 O O . TYR A 202 ? 0.2308 0.2429 0.2267 0.0393 -0.0137 -0.0302 223 TYR A O 1619 C CB . TYR A 202 ? 0.2007 0.2228 0.1885 0.0287 -0.0350 -0.0216 223 TYR A CB 1620 C CG . TYR A 202 ? 0.2050 0.2178 0.1798 0.0274 -0.0260 -0.0174 223 TYR A CG 1621 C CD1 . TYR A 202 ? 0.2084 0.2100 0.1786 0.0277 -0.0070 -0.0166 223 TYR A CD1 1622 C CD2 . TYR A 202 ? 0.1770 0.1884 0.1449 0.0272 -0.0322 -0.0133 223 TYR A CD2 1623 C CE1 . TYR A 202 ? 0.2478 0.2342 0.2054 0.0284 0.0061 -0.0110 223 TYR A CE1 1624 C CE2 . TYR A 202 ? 0.2044 0.2033 0.1624 0.0287 -0.0198 -0.0079 223 TYR A CE2 1625 C CZ . TYR A 202 ? 0.2420 0.2271 0.1940 0.0295 -0.0005 -0.0064 223 TYR A CZ 1626 O OH . TYR A 202 ? 0.2876 0.2544 0.2294 0.0327 0.0163 0.0006 223 TYR A OH 1627 N N . ALA A 203 ? 0.2474 0.2587 0.2328 0.0390 -0.0377 -0.0325 224 ALA A N 1628 C CA . ALA A 203 ? 0.2658 0.2711 0.2643 0.0431 -0.0293 -0.0367 224 ALA A CA 1629 C C . ALA A 203 ? 0.2970 0.2857 0.2751 0.0468 -0.0113 -0.0427 224 ALA A C 1630 O O . ALA A 203 ? 0.2989 0.2861 0.2957 0.0508 0.0048 -0.0431 224 ALA A O 1631 C CB . ALA A 203 ? 0.2089 0.2050 0.2056 0.0422 -0.0364 -0.0415 224 ALA A CB 1632 N N . ALA A 204 ? 0.2975 0.2748 0.2369 0.0465 -0.0136 -0.0462 225 ALA A N 1633 C CA . ALA A 204 ? 0.3618 0.3187 0.2689 0.0505 0.0032 -0.0512 225 ALA A CA 1634 C C . ALA A 204 ? 0.3802 0.3353 0.2857 0.0535 0.0188 -0.0427 225 ALA A C 1635 O O . ALA A 204 ? 0.3962 0.3378 0.2999 0.0566 0.0418 -0.0445 225 ALA A O 1636 C CB . ALA A 204 ? 0.4072 0.3548 0.2682 0.0493 -0.0085 -0.0580 225 ALA A CB 1637 N N . ALA A 205 ? 0.3761 0.3417 0.2845 0.0520 0.0105 -0.0339 226 ALA A N 1638 C CA . ALA A 205 ? 0.3778 0.3360 0.2839 0.0533 0.0289 -0.0264 226 ALA A CA 1639 C C . ALA A 205 ? 0.3989 0.3667 0.3492 0.0474 0.0448 -0.0282 226 ALA A C 1640 O O . ALA A 205 ? 0.3976 0.3538 0.3485 0.0474 0.0688 -0.0264 226 ALA A O 1641 C CB . ALA A 205 ? 0.2733 0.2363 0.1747 0.0530 0.0196 -0.0174 226 ALA A CB # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 GLY 1 22 ? ? ? A . n A 1 2 SER 2 23 ? ? ? A . n A 1 3 ARG 3 24 24 ARG ARG A . n A 1 4 THR 4 25 25 THR THR A . n A 1 5 ASP 5 26 26 ASP ASP A . n A 1 6 LEU 6 27 27 LEU LEU A . n A 1 7 LEU 7 28 28 LEU LEU A . n A 1 8 ASN 8 29 29 ASN ASN A . n A 1 9 VAL 9 30 30 VAL VAL A . n A 1 10 CYS 10 31 31 CYS CYS A . n A 1 11 MET 11 32 32 MET MET A . n A 1 12 ASP 12 33 33 ASP ASP A . n A 1 13 ALA 13 34 34 ALA ALA A . n A 1 14 LYS 14 35 35 LYS LYS A . n A 1 15 HIS 15 36 36 HIS HIS A . n A 1 16 HIS 16 37 37 HIS HIS A . n A 1 17 LYS 17 38 38 LYS LYS A . n A 1 18 THR 18 39 39 THR THR A . n A 1 19 LYS 19 40 40 LYS ALA A . n A 1 20 PRO 20 41 41 PRO PRO A . n A 1 21 GLY 21 42 42 GLY GLY A . n A 1 22 PRO 22 43 43 PRO PRO A . n A 1 23 GLU 23 44 44 GLU GLU A . n A 1 24 ASP 24 45 45 ASP ASP A . n A 1 25 LYS 25 46 46 LYS ALA A . n A 1 26 LEU 26 47 47 LEU LEU A . n A 1 27 HIS 27 48 48 HIS HIS A . n A 1 28 ASP 28 49 49 ASP ASP A . n A 1 29 GLN 29 50 50 GLN GLN A . n A 1 30 CYS 30 51 51 CYS CYS A . n A 1 31 SER 31 52 52 SER SER A . n A 1 32 PRO 32 53 53 PRO PRO A . n A 1 33 TRP 33 54 54 TRP TRP A . n A 1 34 LYS 34 55 55 LYS LYS A . n A 1 35 LYS 35 56 56 LYS LYS A . n A 1 36 ASN 36 57 57 ASN ASN A . n A 1 37 ALA 37 58 58 ALA ALA A . n A 1 38 CYS 38 59 59 CYS CYS A . n A 1 39 CYS 39 60 60 CYS CYS A . n A 1 40 THR 40 61 61 THR THR A . n A 1 41 ALA 41 62 62 ALA ALA A . n A 1 42 SER 42 63 63 SER SER A . n A 1 43 THR 43 64 64 THR THR A . n A 1 44 SER 44 65 65 SER SER A . n A 1 45 GLN 45 66 66 GLN GLN A . n A 1 46 GLU 46 67 67 GLU GLU A . n A 1 47 LEU 47 68 68 LEU LEU A . n A 1 48 HIS 48 69 69 HIS HIS A . n A 1 49 LYS 49 70 70 LYS LYS A . n A 1 50 ASP 50 71 71 ASP ASP A . n A 1 51 THR 51 72 72 THR THR A . n A 1 52 SER 52 73 73 SER SER A . n A 1 53 ARG 53 74 74 ARG ALA A . n A 1 54 LEU 54 75 75 LEU LEU A . n A 1 55 TYR 55 76 76 TYR TYR A . n A 1 56 ASN 56 77 77 ASN ASN A . n A 1 57 PHE 57 78 78 PHE PHE A . n A 1 58 ASN 58 79 79 ASN ASN A . n A 1 59 TRP 59 80 80 TRP TRP A . n A 1 60 ASP 60 81 81 ASP ASP A . n A 1 61 HIS 61 82 82 HIS HIS A . n A 1 62 CYS 62 83 83 CYS CYS A . n A 1 63 GLY 63 84 84 GLY GLY A . n A 1 64 LYS 64 85 85 LYS LYS A . n A 1 65 MET 65 86 86 MET MET A . n A 1 66 GLU 66 87 87 GLU GLU A . n A 1 67 PRO 67 88 88 PRO PRO A . n A 1 68 ALA 68 89 89 ALA ALA A . n A 1 69 CYS 69 90 90 CYS CYS A . n A 1 70 LYS 70 91 91 LYS LYS A . n A 1 71 ARG 71 92 92 ARG ARG A . n A 1 72 HIS 72 93 93 HIS HIS A . n A 1 73 PHE 73 94 94 PHE PHE A . n A 1 74 ILE 74 95 95 ILE ILE A . n A 1 75 GLN 75 96 96 GLN GLN A . n A 1 76 ASP 76 97 97 ASP ASP A . n A 1 77 THR 77 98 98 THR THR A . n A 1 78 CYS 78 99 99 CYS CYS A . n A 1 79 LEU 79 100 100 LEU LEU A . n A 1 80 TYR 80 101 101 TYR TYR A . n A 1 81 GLU 81 102 102 GLU GLU A . n A 1 82 CYS 82 103 103 CYS CYS A . n A 1 83 SER 83 104 104 SER SER A . n A 1 84 PRO 84 105 105 PRO PRO A . n A 1 85 ASN 85 106 106 ASN ASN A . n A 1 86 LEU 86 107 107 LEU LEU A . n A 1 87 GLY 87 108 108 GLY GLY A . n A 1 88 PRO 88 109 109 PRO PRO A . n A 1 89 TRP 89 110 110 TRP TRP A . n A 1 90 ILE 90 111 111 ILE ILE A . n A 1 91 GLN 91 112 112 GLN GLN A . n A 1 92 GLN 92 113 113 GLN GLN A . n A 1 93 VAL 93 114 114 VAL VAL A . n A 1 94 ASN 94 115 115 ASN ASN A . n A 1 95 GLN 95 116 116 GLN GLN A . n A 1 96 SER 96 117 117 SER SER A . n A 1 97 TRP 97 118 118 TRP TRP A . n A 1 98 ARG 98 119 119 ARG ARG A . n A 1 99 LYS 99 120 120 LYS ALA A . n A 1 100 GLU 100 121 121 GLU GLU A . n A 1 101 ARG 101 122 122 ARG ARG A . n A 1 102 PHE 102 123 123 PHE PHE A . n A 1 103 LEU 103 124 124 LEU LEU A . n A 1 104 ASP 104 125 125 ASP ASP A . n A 1 105 VAL 105 126 126 VAL VAL A . n A 1 106 PRO 106 127 127 PRO PRO A . n A 1 107 LEU 107 128 128 LEU LEU A . n A 1 108 CYS 108 129 129 CYS CYS A . n A 1 109 LYS 109 130 130 LYS LYS A . n A 1 110 GLU 110 131 131 GLU GLU A . n A 1 111 ASP 111 132 132 ASP ASP A . n A 1 112 CYS 112 133 133 CYS CYS A . n A 1 113 GLN 113 134 134 GLN GLN A . n A 1 114 ARG 114 135 135 ARG ARG A . n A 1 115 TRP 115 136 136 TRP TRP A . n A 1 116 TRP 116 137 137 TRP TRP A . n A 1 117 GLU 117 138 138 GLU GLU A . n A 1 118 ASP 118 139 139 ASP ASP A . n A 1 119 CYS 119 140 140 CYS CYS A . n A 1 120 HIS 120 141 141 HIS HIS A . n A 1 121 THR 121 142 142 THR THR A . n A 1 122 SER 122 143 143 SER SER A . n A 1 123 HIS 123 144 144 HIS HIS A . n A 1 124 THR 124 145 145 THR THR A . n A 1 125 CYS 125 146 146 CYS CYS A . n A 1 126 LYS 126 147 147 LYS LYS A . n A 1 127 SER 127 148 148 SER SER A . n A 1 128 ASN 128 149 149 ASN ASN A . n A 1 129 TRP 129 150 150 TRP TRP A . n A 1 130 HIS 130 151 151 HIS HIS A . n A 1 131 ARG 131 152 152 ARG ARG A . n A 1 132 GLY 132 153 153 GLY GLY A . n A 1 133 TRP 133 154 154 TRP TRP A . n A 1 134 ASP 134 155 155 ASP ASP A . n A 1 135 TRP 135 156 156 TRP TRP A . n A 1 136 THR 136 157 157 THR THR A . n A 1 137 SER 137 158 158 SER SER A . n A 1 138 GLY 138 159 159 GLY GLY A . n A 1 139 VAL 139 160 160 VAL VAL A . n A 1 140 ASN 140 161 161 ASN ASN A . n A 1 141 LYS 141 162 162 LYS LYS A . n A 1 142 CYS 142 163 163 CYS CYS A . n A 1 143 PRO 143 164 164 PRO PRO A . n A 1 144 ALA 144 165 165 ALA ALA A . n A 1 145 GLY 145 166 166 GLY GLY A . n A 1 146 ALA 146 167 167 ALA ALA A . n A 1 147 LEU 147 168 168 LEU LEU A . n A 1 148 CYS 148 169 169 CYS CYS A . n A 1 149 ARG 149 170 170 ARG ARG A . n A 1 150 THR 150 171 171 THR THR A . n A 1 151 PHE 151 172 172 PHE PHE A . n A 1 152 GLU 152 173 173 GLU GLU A . n A 1 153 SER 153 174 174 SER SER A . n A 1 154 TYR 154 175 175 TYR TYR A . n A 1 155 PHE 155 176 176 PHE PHE A . n A 1 156 PRO 156 177 177 PRO PRO A . n A 1 157 THR 157 178 178 THR THR A . n A 1 158 PRO 158 179 179 PRO PRO A . n A 1 159 ALA 159 180 180 ALA ALA A . n A 1 160 ALA 160 181 181 ALA ALA A . n A 1 161 LEU 161 182 182 LEU LEU A . n A 1 162 CYS 162 183 183 CYS CYS A . n A 1 163 GLU 163 184 184 GLU GLU A . n A 1 164 GLY 164 185 185 GLY GLY A . n A 1 165 LEU 165 186 186 LEU LEU A . n A 1 166 TRP 166 187 187 TRP TRP A . n A 1 167 SER 167 188 188 SER SER A . n A 1 168 HIS 168 189 189 HIS HIS A . n A 1 169 SER 169 190 190 SER SER A . n A 1 170 TYR 170 191 191 TYR TYR A . n A 1 171 LYS 171 192 192 LYS LYS A . n A 1 172 VAL 172 193 193 VAL VAL A . n A 1 173 SER 173 194 194 SER SER A . n A 1 174 ASN 174 195 195 ASN ASN A . n A 1 175 TYR 175 196 196 TYR TYR A . n A 1 176 SER 176 197 197 SER SER A . n A 1 177 ARG 177 198 198 ARG ARG A . n A 1 178 GLY 178 199 199 GLY GLY A . n A 1 179 SER 179 200 200 SER SER A . n A 1 180 GLY 180 201 201 GLY GLY A . n A 1 181 ARG 181 202 202 ARG ARG A . n A 1 182 CYS 182 203 203 CYS CYS A . n A 1 183 ILE 183 204 204 ILE ILE A . n A 1 184 GLN 184 205 205 GLN GLN A . n A 1 185 MET 185 206 206 MET MET A . n A 1 186 TRP 186 207 207 TRP TRP A . n A 1 187 PHE 187 208 208 PHE PHE A . n A 1 188 ASP 188 209 209 ASP ASP A . n A 1 189 SER 189 210 210 SER SER A . n A 1 190 ALA 190 211 211 ALA ALA A . n A 1 191 GLN 191 212 212 GLN GLN A . n A 1 192 GLY 192 213 213 GLY GLY A . n A 1 193 ASN 193 214 214 ASN ASN A . n A 1 194 PRO 194 215 215 PRO PRO A . n A 1 195 ASN 195 216 216 ASN ASN A . n A 1 196 GLU 196 217 217 GLU GLU A . n A 1 197 GLU 197 218 218 GLU GLU A . n A 1 198 VAL 198 219 219 VAL VAL A . n A 1 199 ALA 199 220 220 ALA ALA A . n A 1 200 ARG 200 221 221 ARG ARG A . n A 1 201 PHE 201 222 222 PHE PHE A . n A 1 202 TYR 202 223 223 TYR TYR A . n A 1 203 ALA 203 224 224 ALA ALA A . n A 1 204 ALA 204 225 225 ALA ALA A . n A 1 205 ALA 205 226 226 ALA ALA A . n A 1 206 MET 206 227 227 MET MET A . n A 1 207 HIS 207 228 228 HIS HIS 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 MTX 1 301 241 MTX MTX A . C 3 K 1 302 251 K K A . D 4 CL 1 303 261 CL CL A . E 4 CL 1 304 262 CL CL A . F 5 NAG 1 305 301 NAG NAG A . G 5 NAG 2 306 302 NAG NAG A . H 5 NAG 1 307 311 NAG NAG A . I 5 NAG 2 308 312 NAG NAG A . J 6 HOH 1 401 1 HOH HOH A . J 6 HOH 2 402 2 HOH HOH A . J 6 HOH 3 403 3 HOH HOH A . J 6 HOH 4 404 4 HOH HOH A . J 6 HOH 5 405 5 HOH HOH A . J 6 HOH 6 406 6 HOH HOH A . J 6 HOH 7 407 7 HOH HOH A . J 6 HOH 8 408 8 HOH HOH A . J 6 HOH 9 409 9 HOH HOH A . J 6 HOH 10 410 10 HOH HOH A . J 6 HOH 11 411 11 HOH HOH A . J 6 HOH 12 412 12 HOH HOH A . J 6 HOH 13 413 13 HOH HOH A . J 6 HOH 14 414 14 HOH HOH A . J 6 HOH 15 415 15 HOH HOH A . J 6 HOH 16 416 16 HOH HOH A . J 6 HOH 17 417 17 HOH HOH A . J 6 HOH 18 418 18 HOH HOH A . J 6 HOH 19 419 19 HOH HOH A . J 6 HOH 20 420 20 HOH HOH A . J 6 HOH 21 421 21 HOH HOH A . J 6 HOH 22 422 22 HOH HOH A . J 6 HOH 23 423 23 HOH HOH A . J 6 HOH 24 424 24 HOH HOH A . J 6 HOH 25 425 25 HOH HOH A . J 6 HOH 26 426 26 HOH HOH A . J 6 HOH 27 427 27 HOH HOH A . J 6 HOH 28 428 28 HOH HOH A . J 6 HOH 29 429 29 HOH HOH A . J 6 HOH 30 430 30 HOH HOH A . J 6 HOH 31 431 31 HOH HOH A . J 6 HOH 32 432 32 HOH HOH A . J 6 HOH 33 433 33 HOH HOH A . J 6 HOH 34 434 34 HOH HOH A . J 6 HOH 35 435 35 HOH HOH A . J 6 HOH 36 436 36 HOH HOH A . J 6 HOH 37 437 37 HOH HOH A . J 6 HOH 38 438 38 HOH HOH A . J 6 HOH 39 439 39 HOH HOH A . J 6 HOH 40 440 40 HOH HOH A . J 6 HOH 41 441 41 HOH HOH A . J 6 HOH 42 442 42 HOH HOH A . J 6 HOH 43 443 43 HOH HOH A . J 6 HOH 44 444 44 HOH HOH A . J 6 HOH 45 445 45 HOH HOH A . J 6 HOH 46 446 46 HOH HOH A . J 6 HOH 47 447 47 HOH HOH A . J 6 HOH 48 448 48 HOH HOH A . J 6 HOH 49 449 49 HOH HOH A . J 6 HOH 50 450 50 HOH HOH A . J 6 HOH 51 451 51 HOH HOH A . J 6 HOH 52 452 52 HOH HOH A . J 6 HOH 53 453 53 HOH HOH A . J 6 HOH 54 454 54 HOH HOH A . J 6 HOH 55 455 55 HOH HOH A . J 6 HOH 56 456 56 HOH HOH A . J 6 HOH 57 457 57 HOH HOH A . J 6 HOH 58 458 58 HOH HOH A . J 6 HOH 59 459 59 HOH HOH A . J 6 HOH 60 460 60 HOH HOH A . J 6 HOH 61 461 61 HOH HOH A . J 6 HOH 62 462 62 HOH HOH A . J 6 HOH 63 463 63 HOH HOH A . J 6 HOH 64 464 64 HOH HOH A . J 6 HOH 65 465 65 HOH HOH A . J 6 HOH 66 466 66 HOH HOH A . J 6 HOH 67 467 67 HOH HOH A . J 6 HOH 68 468 68 HOH HOH A . J 6 HOH 69 469 69 HOH HOH A . J 6 HOH 70 470 70 HOH HOH A . J 6 HOH 71 471 71 HOH HOH A . J 6 HOH 72 472 72 HOH HOH A . J 6 HOH 73 473 73 HOH HOH A . J 6 HOH 74 474 74 HOH HOH A . J 6 HOH 75 475 75 HOH HOH A . J 6 HOH 76 476 76 HOH HOH A . J 6 HOH 77 477 77 HOH HOH A . J 6 HOH 78 478 78 HOH HOH A . J 6 HOH 79 479 79 HOH HOH A . J 6 HOH 80 480 80 HOH HOH A . J 6 HOH 81 481 81 HOH HOH A . J 6 HOH 82 482 82 HOH HOH A . J 6 HOH 83 483 83 HOH HOH A . J 6 HOH 84 484 84 HOH HOH A . J 6 HOH 85 485 85 HOH HOH A . J 6 HOH 86 486 86 HOH HOH A . J 6 HOH 87 487 87 HOH HOH A . J 6 HOH 88 488 88 HOH HOH A . J 6 HOH 89 489 89 HOH HOH A . J 6 HOH 90 490 90 HOH HOH A . J 6 HOH 91 491 91 HOH HOH A . J 6 HOH 92 492 92 HOH HOH A . J 6 HOH 93 493 93 HOH HOH A . J 6 HOH 94 494 94 HOH HOH A . J 6 HOH 95 495 95 HOH HOH A . J 6 HOH 96 496 96 HOH HOH A . J 6 HOH 97 497 97 HOH HOH A . J 6 HOH 98 498 98 HOH HOH A . J 6 HOH 99 499 99 HOH HOH A . J 6 HOH 100 500 100 HOH HOH A . J 6 HOH 101 501 101 HOH HOH A . J 6 HOH 102 502 102 HOH HOH A . J 6 HOH 103 503 103 HOH HOH A . J 6 HOH 104 504 104 HOH HOH A . J 6 HOH 105 505 105 HOH HOH A . J 6 HOH 106 506 106 HOH HOH A . J 6 HOH 107 507 107 HOH HOH A . J 6 HOH 108 508 108 HOH HOH A . J 6 HOH 109 509 109 HOH HOH A . J 6 HOH 110 510 110 HOH HOH A . J 6 HOH 111 511 111 HOH HOH A . J 6 HOH 112 512 112 HOH HOH A . J 6 HOH 113 513 113 HOH HOH A . J 6 HOH 114 514 114 HOH HOH A . J 6 HOH 115 515 115 HOH HOH A . J 6 HOH 116 516 116 HOH HOH A . J 6 HOH 117 517 117 HOH HOH A . J 6 HOH 118 518 118 HOH HOH A . J 6 HOH 119 519 119 HOH HOH A . J 6 HOH 120 520 120 HOH HOH A . J 6 HOH 121 521 121 HOH HOH A . J 6 HOH 122 522 122 HOH HOH A . J 6 HOH 123 523 123 HOH HOH A . J 6 HOH 124 524 124 HOH HOH A . J 6 HOH 125 525 125 HOH HOH A . J 6 HOH 126 526 126 HOH HOH A . J 6 HOH 127 527 127 HOH HOH A . J 6 HOH 128 528 128 HOH HOH A . J 6 HOH 129 529 129 HOH HOH A . J 6 HOH 130 530 130 HOH HOH A . J 6 HOH 131 531 131 HOH HOH A . J 6 HOH 132 532 132 HOH HOH A . J 6 HOH 133 533 133 HOH HOH A . J 6 HOH 134 534 134 HOH HOH A . J 6 HOH 135 535 135 HOH HOH A . J 6 HOH 136 536 136 HOH HOH A . J 6 HOH 137 537 137 HOH HOH A . J 6 HOH 138 538 138 HOH HOH A . J 6 HOH 139 539 139 HOH HOH A . J 6 HOH 140 540 140 HOH HOH A . J 6 HOH 141 541 141 HOH HOH A . J 6 HOH 142 542 142 HOH HOH A . J 6 HOH 143 543 143 HOH HOH A . J 6 HOH 144 544 144 HOH HOH A . J 6 HOH 145 545 145 HOH HOH A . J 6 HOH 146 546 146 HOH HOH A . J 6 HOH 147 547 147 HOH HOH A . J 6 HOH 148 548 148 HOH HOH A . J 6 HOH 149 549 149 HOH HOH A . J 6 HOH 150 550 150 HOH HOH A . J 6 HOH 151 551 151 HOH HOH A . J 6 HOH 152 552 152 HOH HOH A . J 6 HOH 153 553 153 HOH HOH A . J 6 HOH 154 554 154 HOH HOH A . J 6 HOH 155 555 155 HOH HOH A . J 6 HOH 156 556 156 HOH HOH A . J 6 HOH 157 557 157 HOH HOH A . J 6 HOH 158 558 158 HOH HOH A . J 6 HOH 159 559 159 HOH HOH A . J 6 HOH 160 560 160 HOH HOH A . J 6 HOH 161 561 161 HOH HOH A . J 6 HOH 162 562 162 HOH HOH A . J 6 HOH 163 563 163 HOH HOH A . J 6 HOH 164 564 164 HOH HOH A . J 6 HOH 165 565 165 HOH HOH A . J 6 HOH 166 566 166 HOH HOH A . J 6 HOH 167 567 167 HOH HOH A . J 6 HOH 168 568 168 HOH HOH A . J 6 HOH 169 569 169 HOH HOH A . J 6 HOH 170 570 170 HOH HOH A . J 6 HOH 171 571 171 HOH HOH A . J 6 HOH 172 572 172 HOH HOH A . J 6 HOH 173 573 173 HOH HOH A . J 6 HOH 174 574 174 HOH HOH A . J 6 HOH 175 575 175 HOH HOH A . J 6 HOH 176 576 176 HOH HOH A . J 6 HOH 177 577 177 HOH HOH A . J 6 HOH 178 578 178 HOH HOH A . J 6 HOH 179 579 179 HOH HOH A . J 6 HOH 180 580 180 HOH HOH A . J 6 HOH 181 581 181 HOH HOH A . J 6 HOH 182 582 182 HOH HOH A . J 6 HOH 183 583 183 HOH HOH A . J 6 HOH 184 584 184 HOH HOH A . J 6 HOH 185 585 185 HOH HOH A . J 6 HOH 186 586 186 HOH HOH A . J 6 HOH 187 587 187 HOH HOH A . J 6 HOH 188 588 188 HOH HOH A . J 6 HOH 189 589 189 HOH HOH A . J 6 HOH 190 590 190 HOH HOH A . J 6 HOH 191 591 191 HOH HOH A . J 6 HOH 192 592 192 HOH HOH A . J 6 HOH 193 593 193 HOH HOH A . J 6 HOH 194 594 194 HOH HOH A . J 6 HOH 195 595 195 HOH HOH A . J 6 HOH 196 596 196 HOH HOH A . J 6 HOH 197 597 197 HOH HOH A . J 6 HOH 198 598 198 HOH HOH A . J 6 HOH 199 599 199 HOH HOH A . J 6 HOH 200 600 200 HOH HOH A . J 6 HOH 201 601 201 HOH HOH A . J 6 HOH 202 602 202 HOH HOH A . J 6 HOH 203 603 203 HOH HOH A . J 6 HOH 204 604 204 HOH HOH A . J 6 HOH 205 605 205 HOH HOH A . J 6 HOH 206 606 206 HOH HOH A . J 6 HOH 207 607 207 HOH HOH A . J 6 HOH 208 608 208 HOH HOH A . J 6 HOH 209 609 209 HOH HOH A . J 6 HOH 210 610 210 HOH HOH A . J 6 HOH 211 611 211 HOH HOH A . J 6 HOH 212 612 212 HOH HOH A . J 6 HOH 213 613 213 HOH HOH A . J 6 HOH 214 614 214 HOH HOH A . J 6 HOH 215 615 215 HOH HOH A . J 6 HOH 216 616 216 HOH HOH A . J 6 HOH 217 617 217 HOH HOH A . J 6 HOH 218 618 218 HOH HOH A . J 6 HOH 219 619 219 HOH HOH A . J 6 HOH 220 620 220 HOH HOH A . J 6 HOH 221 621 221 HOH HOH A . J 6 HOH 222 622 222 HOH HOH A . J 6 HOH 223 623 223 HOH HOH A . J 6 HOH 224 624 224 HOH HOH A . J 6 HOH 225 625 225 HOH HOH A . J 6 HOH 226 626 226 HOH HOH A . J 6 HOH 227 627 227 HOH HOH A . J 6 HOH 228 628 228 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 94 A ASN 115 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 174 A ASN 195 ? 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,I,J # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A CL 304 ? E CL . 2 1 A HOH 408 ? J HOH . 3 1 A HOH 517 ? J HOH . 4 1 A HOH 522 ? J HOH . # 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[2][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] 'X-RAY DIFFRACTION' 1 ? refined 10.1979 -47.3657 -11.6114 0.1569 0.1883 0.2204 0.0013 -0.0349 -0.0289 2.8950 4.1776 6.5075 -0.2605 0.3335 -1.4452 0.0135 0.1441 -0.1264 0.3912 -0.7325 -0.1086 -0.3659 0.6879 0.2937 'X-RAY DIFFRACTION' 2 ? refined -1.0626 -43.7761 -1.7475 0.1569 0.1938 0.1875 -0.0793 -0.0440 0.0445 2.7113 4.2138 3.4592 -1.6209 -2.4553 -0.1791 0.0084 -0.0209 0.0612 -0.1197 -0.4032 0.2514 0.1702 0.1562 -0.0658 'X-RAY DIFFRACTION' 3 ? refined 6.5328 -33.0012 4.8363 0.1912 0.1761 0.1126 -0.0345 -0.0192 0.0444 2.0813 1.1081 1.3722 -0.1662 0.4667 0.4102 0.0350 0.0031 -0.0474 -0.1684 -0.1112 0.0025 0.2689 0.1183 -0.1396 'X-RAY DIFFRACTION' 4 ? refined 15.4285 -38.9793 -9.9917 0.1373 0.1391 0.1424 0.0007 -0.0414 -0.0107 0.0596 3.4293 3.5250 -0.0860 0.0740 -1.8876 -0.0182 -0.0904 0.1103 0.0983 -0.1670 -0.0552 -0.1943 0.0467 0.3910 'X-RAY DIFFRACTION' 5 ? refined 3.8475 -21.8876 -5.5132 0.1378 0.1453 0.1446 0.0152 -0.0245 0.0260 5.1998 4.1637 5.3154 0.8722 -2.5285 1.4251 0.0615 -0.0758 0.0305 0.2648 0.2446 0.1822 -0.4399 -0.2031 -0.1621 'X-RAY DIFFRACTION' 6 ? refined 16.8543 -28.6821 6.7776 0.1701 0.1341 0.0779 -0.0306 -0.0647 0.0116 3.2126 1.3897 1.8844 0.1761 -1.4638 1.2279 0.1755 -0.1816 0.0006 0.0410 -0.1186 -0.1705 0.1237 0.0555 -0.0108 'X-RAY DIFFRACTION' 7 ? refined 16.6469 -21.0937 6.3335 0.1536 0.1305 0.0886 -0.0283 -0.0285 -0.0129 3.5349 2.8553 1.6778 0.4449 -0.1011 1.8341 0.0271 0.0179 0.0139 -0.2624 -0.0841 0.1735 0.1804 0.0181 -0.1357 'X-RAY DIFFRACTION' 8 ? refined 5.3550 -29.7139 -11.8704 0.1376 0.1619 0.1027 -0.0051 -0.0191 0.0119 1.7267 2.5114 2.3211 0.8868 -0.4257 0.2194 0.0772 -0.0298 -0.0271 0.3006 0.0486 0.1401 0.0056 0.0589 -0.0977 'X-RAY DIFFRACTION' 9 ? refined 5.3806 -37.8265 -22.1332 0.1709 0.1986 0.1324 0.0329 -0.0754 -0.0261 3.5932 5.0523 3.4676 0.0405 -2.6580 -0.1810 0.1260 -0.0452 -0.0155 0.3540 -0.1744 0.0125 -0.4066 0.0329 -0.1869 # 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.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 24 A 42 ;chain 'A' and (resseq 24:42) ; ? ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 43 A 69 ;chain 'A' and (resseq 43:69) ; ? ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 70 A 103 ;chain 'A' and (resseq 70:103) ; ? ? ? ? ? 'X-RAY DIFFRACTION' 4 4 A 104 A 129 ;chain 'A' and (resseq 104:129) ; ? ? ? ? ? 'X-RAY DIFFRACTION' 5 5 A 130 A 140 ;chain 'A' and (resseq 130:140) ; ? ? ? ? ? 'X-RAY DIFFRACTION' 6 6 A 141 A 160 ;chain 'A' and (resseq 141:160) ; ? ? ? ? ? 'X-RAY DIFFRACTION' 7 7 A 161 A 178 ;chain 'A' and (resseq 161:178) ; ? ? ? ? ? 'X-RAY DIFFRACTION' 8 8 A 179 A 215 ;chain 'A' and (resseq 179:215) ; ? ? ? ? ? 'X-RAY DIFFRACTION' 9 9 A 216 A 226 ;chain 'A' and (resseq 216:226) ; ? ? ? ? ? # 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 1.7.1_743 ? 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 ? ? ? # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASP A 49 ? ? 41.45 -112.53 2 1 ASN A 57 ? ? -164.78 108.07 3 1 THR A 72 ? ? 37.38 59.12 4 1 ASP A 81 ? ? -93.40 43.87 # 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 40 ? CG ? A LYS 19 CG 2 1 Y 1 A LYS 40 ? CD ? A LYS 19 CD 3 1 Y 1 A LYS 40 ? CE ? A LYS 19 CE 4 1 Y 1 A LYS 40 ? NZ ? A LYS 19 NZ 5 1 Y 1 A LYS 46 ? CG ? A LYS 25 CG 6 1 Y 1 A LYS 46 ? CD ? A LYS 25 CD 7 1 Y 1 A LYS 46 ? CE ? A LYS 25 CE 8 1 Y 1 A LYS 46 ? NZ ? A LYS 25 NZ 9 1 Y 1 A ARG 74 ? CG ? A ARG 53 CG 10 1 Y 1 A ARG 74 ? CD ? A ARG 53 CD 11 1 Y 1 A ARG 74 ? NE ? A ARG 53 NE 12 1 Y 1 A ARG 74 ? CZ ? A ARG 53 CZ 13 1 Y 1 A ARG 74 ? NH1 ? A ARG 53 NH1 14 1 Y 1 A ARG 74 ? NH2 ? A ARG 53 NH2 15 1 Y 1 A LYS 120 ? CG ? A LYS 99 CG 16 1 Y 1 A LYS 120 ? CD ? A LYS 99 CD 17 1 Y 1 A LYS 120 ? CE ? A LYS 99 CE 18 1 Y 1 A LYS 120 ? NZ ? A LYS 99 NZ # 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 GLY 22 ? A GLY 1 2 1 Y 1 A SER 23 ? A SER 2 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 METHOTREXATE MTX 3 'POTASSIUM ION' K 4 'CHLORIDE ION' CL 5 N-ACETYL-D-GLUCOSAMINE NAG 6 water HOH #