data_4KM6 # _entry.id 4KM6 # _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 4KM6 RCSB RCSB079512 WWPDB D_1000079512 # 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 4KN0 'Human folate receptor beta (FOLR2) in complex with the antifolate methotrexate' unspecified PDB 4KN1 'Human folate receptor beta (FOLR2) in complex with the antifolate aminopterin' unspecified PDB 4KN2 'Human folate receptor beta (FOLR2) in complex with antifolate pemetrexed' unspecified # _pdbx_database_status.entry_id 4KM6 _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 'Singh, M.' 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 4KM6 _cell.length_a 36.519 _cell.length_b 63.339 _cell.length_c 71.169 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4KM6 _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Folate receptor alpha' 24322.357 1 ? ? 'UNP residues 28-234' ? 2 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 4 water nat water 18.015 126 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name ;FR-alpha, Adult folate-binding protein, FBP, Folate receptor 1, Folate receptor, adult, KB cells FBP, Ovarian tumor-associated antigen MOv18 ; # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;GSSRTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCL YECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPT VLCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMS ; _entity_poly.pdbx_seq_one_letter_code_can ;GSSRTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCL YECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPT VLCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMS ; _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 SER n 1 4 ARG n 1 5 THR n 1 6 GLU n 1 7 LEU n 1 8 LEU n 1 9 ASN n 1 10 VAL n 1 11 CYS n 1 12 MET n 1 13 ASN n 1 14 ALA n 1 15 LYS n 1 16 HIS n 1 17 HIS n 1 18 LYS n 1 19 GLU n 1 20 LYS n 1 21 PRO n 1 22 GLY n 1 23 PRO n 1 24 GLU n 1 25 ASP n 1 26 LYS n 1 27 LEU n 1 28 HIS n 1 29 GLU n 1 30 GLN n 1 31 CYS n 1 32 ARG n 1 33 PRO n 1 34 TRP n 1 35 ARG n 1 36 LYS n 1 37 ASN n 1 38 ALA n 1 39 CYS n 1 40 CYS n 1 41 SER n 1 42 THR n 1 43 ASN n 1 44 THR n 1 45 SER n 1 46 GLN n 1 47 GLU n 1 48 ALA n 1 49 HIS n 1 50 LYS n 1 51 ASP n 1 52 VAL n 1 53 SER n 1 54 TYR n 1 55 LEU n 1 56 TYR n 1 57 ARG n 1 58 PHE n 1 59 ASN n 1 60 TRP n 1 61 ASN n 1 62 HIS n 1 63 CYS n 1 64 GLY n 1 65 GLU n 1 66 MET n 1 67 ALA n 1 68 PRO n 1 69 ALA n 1 70 CYS n 1 71 LYS n 1 72 ARG n 1 73 HIS n 1 74 PHE n 1 75 ILE n 1 76 GLN n 1 77 ASP n 1 78 THR n 1 79 CYS n 1 80 LEU n 1 81 TYR n 1 82 GLU n 1 83 CYS n 1 84 SER n 1 85 PRO n 1 86 ASN n 1 87 LEU n 1 88 GLY n 1 89 PRO n 1 90 TRP n 1 91 ILE n 1 92 GLN n 1 93 GLN n 1 94 VAL n 1 95 ASP n 1 96 GLN n 1 97 SER n 1 98 TRP n 1 99 ARG n 1 100 LYS n 1 101 GLU n 1 102 ARG n 1 103 VAL n 1 104 LEU n 1 105 ASN n 1 106 VAL n 1 107 PRO n 1 108 LEU n 1 109 CYS n 1 110 LYS n 1 111 GLU n 1 112 ASP n 1 113 CYS n 1 114 GLU n 1 115 GLN n 1 116 TRP n 1 117 TRP n 1 118 GLU n 1 119 ASP n 1 120 CYS n 1 121 ARG n 1 122 THR n 1 123 SER n 1 124 TYR n 1 125 THR n 1 126 CYS n 1 127 LYS n 1 128 SER n 1 129 ASN n 1 130 TRP n 1 131 HIS n 1 132 LYS n 1 133 GLY n 1 134 TRP n 1 135 ASN n 1 136 TRP n 1 137 THR n 1 138 SER n 1 139 GLY n 1 140 PHE n 1 141 ASN n 1 142 LYS n 1 143 CYS n 1 144 ALA n 1 145 VAL n 1 146 GLY n 1 147 ALA n 1 148 ALA n 1 149 CYS n 1 150 GLN n 1 151 PRO n 1 152 PHE n 1 153 HIS n 1 154 PHE n 1 155 TYR n 1 156 PHE n 1 157 PRO n 1 158 THR n 1 159 PRO n 1 160 THR n 1 161 VAL n 1 162 LEU n 1 163 CYS n 1 164 ASN n 1 165 GLU n 1 166 ILE n 1 167 TRP n 1 168 THR n 1 169 HIS n 1 170 SER n 1 171 TYR n 1 172 LYS n 1 173 VAL n 1 174 SER n 1 175 ASN n 1 176 TYR n 1 177 SER n 1 178 ARG n 1 179 GLY n 1 180 SER n 1 181 GLY n 1 182 ARG n 1 183 CYS n 1 184 ILE n 1 185 GLN n 1 186 MET n 1 187 TRP n 1 188 PHE n 1 189 ASP n 1 190 PRO n 1 191 ALA n 1 192 GLN n 1 193 GLY n 1 194 ASN n 1 195 PRO n 1 196 ASN n 1 197 GLU n 1 198 GLU n 1 199 VAL n 1 200 ALA n 1 201 ARG n 1 202 PHE n 1 203 TYR n 1 204 ALA n 1 205 ALA n 1 206 ALA n 1 207 MET n 1 208 SER n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'FOLR, FOLR1, 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 FOLR1_HUMAN _struct_ref.pdbx_db_accession P15328 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;WARTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLY ECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTV LCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMS ; _struct_ref.pdbx_align_begin 28 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4KM6 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 4 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 208 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P15328 _struct_ref_seq.db_align_beg 30 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 234 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 30 _struct_ref_seq.pdbx_auth_seq_align_end 234 # 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 4KM6 GLY A 1 ? UNP P15328 ? ? 'EXPRESSION TAG' 27 1 1 4KM6 SER A 2 ? UNP P15328 ? ? 'EXPRESSION TAG' 28 2 1 4KM6 SER A 3 ? UNP P15328 ? ? 'EXPRESSION TAG' 29 3 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 4KM6 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 1.65 _exptl_crystal.density_percent_sol 25.55 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details ;12 mg/mL co-purified with methotrexate in 0.1 M sodium citrate, , 35 % (v/v) jeffamine ED-2001 (MTX not present in structure), pH 5.5, Vapor diffusion, sitting drop, temperature 293K ; # _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 2011-03-02 _diffrn_detector.details 'The NOIR-1 detector was built by E. Westbrook; 180 cm lens focused CCD' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'SAGITALLY FOCUSED Si(III)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ALS BEAMLINE 4.2.2' _diffrn_source.pdbx_synchrotron_site ALS _diffrn_source.pdbx_synchrotron_beamline 4.2.2 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.0000 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4KM6 _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 50.000 _reflns.d_resolution_high 1.550 _reflns.number_obs 24336 _reflns.number_all ? _reflns.percent_possible_obs 98.300 _reflns.pdbx_Rmerge_I_obs 0.087 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 10.000 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 5.700 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # loop_ _reflns_shell.pdbx_diffrn_id _reflns_shell.pdbx_ordinal _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.percent_possible_all _reflns_shell.Rmerge_I_obs _reflns_shell.pdbx_Rsym_value _reflns_shell.meanI_over_sigI_obs _reflns_shell.pdbx_redundancy _reflns_shell.percent_possible_obs _reflns_shell.number_unique_all _reflns_shell.number_measured_all _reflns_shell.number_measured_obs _reflns_shell.number_unique_obs _reflns_shell.pdbx_chi_squared 1 1 1.550 1.580 86.800 0.495 ? ? 4.500 ? ? ? ? ? ? 1 2 1.580 1.610 90.900 0.456 ? ? 4.800 ? ? ? ? ? ? 1 3 1.610 1.640 94.500 0.427 ? ? 5.000 ? ? ? ? ? ? 1 4 1.640 1.670 97.000 0.429 ? ? 5.300 ? ? ? ? ? ? 1 5 1.670 1.710 99.100 0.372 ? ? 5.500 ? ? ? ? ? ? 1 6 1.710 1.750 99.900 0.338 ? ? 5.700 ? ? ? ? ? ? 1 7 1.750 1.790 99.900 0.320 ? ? 5.900 ? ? ? ? ? ? 1 8 1.790 1.840 99.900 0.262 ? ? 5.900 ? ? ? ? ? ? 1 9 1.840 1.890 100.000 0.242 ? ? 6.000 ? ? ? ? ? ? 1 10 1.890 1.950 100.000 0.218 ? ? 6.000 ? ? ? ? ? ? 1 11 1.950 2.020 100.000 0.179 ? ? 6.000 ? ? ? ? ? ? 1 12 2.020 2.100 100.000 0.165 ? ? 5.900 ? ? ? ? ? ? 1 13 2.100 2.200 100.000 0.142 ? ? 6.000 ? ? ? ? ? ? 1 14 2.200 2.320 99.800 0.130 ? ? 6.000 ? ? ? ? ? ? 1 15 2.320 2.460 100.000 0.113 ? ? 6.000 ? ? ? ? ? ? 1 16 2.460 2.650 99.900 0.096 ? ? 6.000 ? ? ? ? ? ? 1 17 2.650 2.920 99.800 0.078 ? ? 6.000 ? ? ? ? ? ? 1 18 2.920 3.340 99.800 0.058 ? ? 5.900 ? ? ? ? ? ? 1 19 3.340 4.210 99.500 0.045 ? ? 5.900 ? ? ? ? ? ? 1 20 4.210 50.000 98.600 0.038 ? ? 5.600 ? ? ? ? ? ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4KM6 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 23197 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.00 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 32.491 _refine.ls_d_res_high 1.55 _refine.ls_percent_reflns_obs 93.90 _refine.ls_R_factor_obs 0.1710 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1684 _refine.ls_R_factor_R_free 0.1999 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 8.22 _refine.ls_number_reflns_R_free 1906 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min 0.830 _refine.occupancy_max 1.000 _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] -4.8842 _refine.aniso_B[2][2] -4.5171 _refine.aniso_B[3][3] 9.4013 _refine.aniso_B[1][2] -0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][3] 0.0000 _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol 0.428 _refine.solvent_model_param_bsol 40.912 _refine.pdbx_solvent_vdw_probe_radii 0.80 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.47 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.19 _refine.pdbx_overall_phase_error 20.19 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 1667 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 43 _refine_hist.number_atoms_solvent 126 _refine_hist.number_atoms_total 1836 _refine_hist.d_res_high 1.55 _refine_hist.d_res_low 32.491 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function f_bond_d 0.007 ? ? 1777 'X-RAY DIFFRACTION' ? f_angle_d 1.163 ? ? 2401 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 14.613 ? ? 642 'X-RAY DIFFRACTION' ? f_chiral_restr 0.081 ? ? 239 'X-RAY DIFFRACTION' ? f_plane_restr 0.007 ? ? 309 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 1.55 1.5874 1229 0.2323 77.00 0.2800 . . 110 . . . . 'X-RAY DIFFRACTION' . 1.5874 1.6303 1325 0.2033 84.00 0.2579 . . 115 . . . . 'X-RAY DIFFRACTION' . 1.6303 1.6783 1377 0.2059 87.00 0.2582 . . 122 . . . . 'X-RAY DIFFRACTION' . 1.6783 1.7324 1482 0.1896 91.00 0.2411 . . 133 . . . . 'X-RAY DIFFRACTION' . 1.7324 1.7944 1467 0.1827 93.00 0.2299 . . 134 . . . . 'X-RAY DIFFRACTION' . 1.7944 1.8662 1511 0.1737 94.00 0.2315 . . 134 . . . . 'X-RAY DIFFRACTION' . 1.8662 1.9511 1519 0.1708 95.00 0.2446 . . 138 . . . . 'X-RAY DIFFRACTION' . 1.9511 2.0540 1574 0.1649 97.00 0.2076 . . 141 . . . . 'X-RAY DIFFRACTION' . 2.0540 2.1826 1568 0.1602 98.00 0.2164 . . 141 . . . . 'X-RAY DIFFRACTION' . 2.1826 2.3511 1607 0.1653 99.00 0.1913 . . 144 . . . . 'X-RAY DIFFRACTION' . 2.3511 2.5876 1608 0.1747 99.00 0.2012 . . 143 . . . . 'X-RAY DIFFRACTION' . 2.5876 2.9618 1624 0.1725 99.00 0.1951 . . 146 . . . . 'X-RAY DIFFRACTION' . 2.9618 3.7308 1658 0.1498 100.00 0.1682 . . 149 . . . . 'X-RAY DIFFRACTION' . 3.7308 32.4983 1742 0.1602 99.00 0.1759 . . 156 . . . . # _struct.entry_id 4KM6 _struct.title 'Human folate receptor alpha (FOLR1) at acidic pH, orthorhombic form' _struct.pdbx_descriptor 'Folate receptor alpha' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4KM6 _struct_keywords.text ;Folate Receptor Alpha, FOLR1, folate receptor, Folic acid, folates, 5-methyltetrahydrofolate, antifolates, folate-conjugates, GPI-anchored protein on eukaryotic membrane, TRANSPORT PROTEIN, MEMBRANE PROTEIN ; _struct_keywords.pdbx_keywords 'MEMBRANE PROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 4 ? # _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 CYS A 31 ? ARG A 35 ? CYS A 57 ARG A 61 5 ? 5 HELX_P HELX_P2 2 ALA A 67 ? SER A 84 ? ALA A 93 SER A 110 1 ? 18 HELX_P HELX_P3 3 LEU A 87 ? ILE A 91 ? LEU A 113 ILE A 117 5 ? 5 HELX_P HELX_P4 4 CYS A 109 ? CYS A 120 ? CYS A 135 CYS A 146 1 ? 12 HELX_P HELX_P5 5 PHE A 152 ? PHE A 156 ? PHE A 178 PHE A 182 1 ? 5 HELX_P HELX_P6 6 THR A 158 ? ILE A 166 ? THR A 184 ILE A 192 1 ? 9 HELX_P HELX_P7 7 ASP A 189 ? GLY A 193 ? ASP A 215 GLY A 219 5 ? 5 HELX_P HELX_P8 8 PRO A 195 ? MET A 207 ? PRO A 221 MET A 233 1 ? 13 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 11 SG ? ? ? 1_555 A CYS 39 SG ? ? A CYS 37 A CYS 65 1_555 ? ? ? ? ? ? ? 2.014 ? disulf2 disulf ? ? A CYS 31 SG ? ? ? 1_555 A CYS 79 SG ? ? A CYS 57 A CYS 105 1_555 ? ? ? ? ? ? ? 2.033 ? disulf3 disulf ? ? A CYS 40 SG ? ? ? 1_555 A CYS 83 SG ? ? A CYS 66 A CYS 109 1_555 ? ? ? ? ? ? ? 2.024 ? disulf4 disulf ? ? A CYS 63 SG ? ? ? 1_555 A CYS 149 SG ? ? A CYS 89 A CYS 175 1_555 ? ? ? ? ? ? ? 2.018 ? disulf5 disulf ? ? A CYS 70 SG ? ? ? 1_555 A CYS 120 SG ? ? A CYS 96 A CYS 146 1_555 ? ? ? ? ? ? ? 2.038 ? disulf6 disulf ? ? A CYS 109 SG ? ? ? 1_555 A CYS 183 SG ? ? A CYS 135 A CYS 209 1_555 ? ? ? ? ? ? ? 2.070 ? disulf7 disulf ? ? A CYS 113 SG ? ? ? 1_555 A CYS 163 SG ? ? A CYS 139 A CYS 189 1_555 ? ? ? ? ? ? ? 2.056 ? disulf8 disulf ? ? A CYS 126 SG ? ? ? 1_555 A CYS 143 SG ? ? A CYS 152 A CYS 169 1_555 ? ? ? ? ? ? ? 2.062 ? covale1 covale ? ? A ASN 43 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 69 A NAG 304 1_555 ? ? ? ? ? ? ? 1.419 ? covale2 covale ? ? A ASN 135 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 161 A NAG 302 1_555 ? ? ? ? ? ? ? 1.449 ? covale3 covale ? ? A ASN 175 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 201 A NAG 303 1_555 ? ? ? ? ? ? ? 1.461 ? metalc1 metalc ? ? A SER 84 OG ? ? ? 1_555 B CA . CA ? ? A SER 110 A CA 301 1_555 ? ? ? ? ? ? ? 3.052 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 2 ? B ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel B 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 CYS A 11 ? MET A 12 ? CYS A 37 MET A 38 A 2 LYS A 18 ? GLU A 19 ? LYS A 44 GLU A 45 B 1 TYR A 124 ? THR A 125 ? TYR A 150 THR A 151 B 2 GLN A 150 ? PRO A 151 ? GLN A 176 PRO A 177 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N CYS A 11 ? N CYS A 37 O GLU A 19 ? O GLU A 45 B 1 2 N THR A 125 ? N THR A 151 O GLN A 150 ? O GLN A 176 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 301' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 302' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 303' AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 304' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 5 TRP A 34 ? TRP A 60 . ? 1_555 ? 2 AC1 5 SER A 84 ? SER A 110 . ? 1_555 ? 3 AC1 5 ASN A 86 ? ASN A 112 . ? 1_555 ? 4 AC1 5 ASN A 194 ? ASN A 220 . ? 1_555 ? 5 AC1 5 ASN A 196 ? ASN A 222 . ? 1_555 ? 6 AC2 7 GLU A 118 ? GLU A 144 . ? 1_655 ? 7 AC2 7 ASN A 135 ? ASN A 161 . ? 1_555 ? 8 AC2 7 THR A 137 ? THR A 163 . ? 1_555 ? 9 AC2 7 LYS A 142 ? LYS A 168 . ? 1_555 ? 10 AC2 7 VAL A 145 ? VAL A 171 . ? 1_555 ? 11 AC2 7 HOH F . ? HOH A 410 . ? 1_655 ? 12 AC2 7 HOH F . ? HOH A 424 . ? 1_555 ? 13 AC3 5 GLU A 29 ? GLU A 55 . ? 2_465 ? 14 AC3 5 SER A 97 ? SER A 123 . ? 1_455 ? 15 AC3 5 ASN A 175 ? ASN A 201 . ? 1_555 ? 16 AC3 5 TYR A 176 ? TYR A 202 . ? 1_555 ? 17 AC3 5 HOH F . ? HOH A 499 . ? 1_455 ? 18 AC4 6 LYS A 15 ? LYS A 41 . ? 1_555 ? 19 AC4 6 ASN A 43 ? ASN A 69 . ? 1_555 ? 20 AC4 6 GLU A 47 ? GLU A 73 . ? 1_555 ? 21 AC4 6 HIS A 49 ? HIS A 75 . ? 1_555 ? 22 AC4 6 LYS A 50 ? LYS A 76 . ? 1_555 ? 23 AC4 6 HOH F . ? HOH A 497 . ? 1_555 ? # _atom_sites.entry_id 4KM6 _atom_sites.fract_transf_matrix[1][1] 0.027383 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.015788 _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] 0.014051 _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 CA 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 4 ? 4.363 49.981 46.532 1.00 49.58 ? 30 ARG A N 1 ATOM 2 C CA . ARG A 1 4 ? 3.159 49.375 45.977 1.00 44.62 ? 30 ARG A CA 1 ATOM 3 C C . ARG A 1 4 ? 2.412 50.401 45.142 1.00 45.49 ? 30 ARG A C 1 ATOM 4 O O . ARG A 1 4 ? 1.691 51.234 45.682 1.00 48.67 ? 30 ARG A O 1 ATOM 5 C CB . ARG A 1 4 ? 2.266 48.840 47.100 1.00 41.22 ? 30 ARG A CB 1 ATOM 6 C CG . ARG A 1 4 ? 1.098 47.998 46.625 1.00 34.87 ? 30 ARG A CG 1 ATOM 7 C CD . ARG A 1 4 ? 0.432 47.275 47.791 1.00 32.82 ? 30 ARG A CD 1 ATOM 8 N NE . ARG A 1 4 ? -0.621 46.376 47.330 1.00 26.66 ? 30 ARG A NE 1 ATOM 9 C CZ . ARG A 1 4 ? -1.909 46.695 47.330 1.00 26.90 ? 30 ARG A CZ 1 ATOM 10 N NH1 . ARG A 1 4 ? -2.292 47.891 47.787 1.00 24.38 ? 30 ARG A NH1 1 ATOM 11 N NH2 . ARG A 1 4 ? -2.812 45.818 46.887 1.00 23.73 ? 30 ARG A NH2 1 ATOM 12 N N . THR A 1 5 ? 2.590 50.333 43.824 1.00 43.02 ? 31 THR A N 1 ATOM 13 C CA . THR A 1 5 ? 1.996 51.311 42.911 1.00 42.42 ? 31 THR A CA 1 ATOM 14 C C . THR A 1 5 ? 1.028 50.667 41.903 1.00 39.29 ? 31 THR A C 1 ATOM 15 O O . THR A 1 5 ? -0.168 50.548 42.168 1.00 43.75 ? 31 THR A O 1 ATOM 16 C CB . THR A 1 5 ? 3.094 52.135 42.179 1.00 75.37 ? 31 THR A CB 1 ATOM 17 O OG1 . THR A 1 5 ? 2.561 52.708 40.979 1.00 77.32 ? 31 THR A OG1 1 ATOM 18 C CG2 . THR A 1 5 ? 4.308 51.260 41.832 1.00 72.43 ? 31 THR A CG2 1 ATOM 19 N N . GLU A 1 6 ? 1.556 50.268 40.752 1.00 32.69 ? 32 GLU A N 1 ATOM 20 C CA . GLU A 1 6 ? 0.779 49.656 39.681 1.00 32.88 ? 32 GLU A CA 1 ATOM 21 C C . GLU A 1 6 ? 0.255 48.286 40.106 1.00 23.11 ? 32 GLU A C 1 ATOM 22 O O . GLU A 1 6 ? 1.042 47.421 40.471 1.00 26.27 ? 32 GLU A O 1 ATOM 23 C CB . GLU A 1 6 ? 1.689 49.477 38.464 1.00 42.80 ? 32 GLU A CB 1 ATOM 24 C CG . GLU A 1 6 ? 1.011 48.872 37.265 1.00 50.50 ? 32 GLU A CG 1 ATOM 25 C CD . GLU A 1 6 ? -0.020 49.799 36.687 1.00 60.32 ? 32 GLU A CD 1 ATOM 26 O OE1 . GLU A 1 6 ? 0.238 51.021 36.670 1.00 67.03 ? 32 GLU A OE1 1 ATOM 27 O OE2 . GLU A 1 6 ? -1.089 49.317 36.262 1.00 62.00 ? 32 GLU A OE2 1 ATOM 28 N N . LEU A 1 7 ? -1.063 48.081 40.052 1.00 20.92 ? 33 LEU A N 1 ATOM 29 C CA . LEU A 1 7 ? -1.629 46.804 40.470 1.00 15.49 ? 33 LEU A CA 1 ATOM 30 C C . LEU A 1 7 ? -2.268 46.053 39.303 1.00 18.11 ? 33 LEU A C 1 ATOM 31 O O . LEU A 1 7 ? -2.491 44.847 39.384 1.00 19.74 ? 33 LEU A O 1 ATOM 32 C CB . LEU A 1 7 ? -2.659 46.999 41.585 1.00 15.00 ? 33 LEU A CB 1 ATOM 33 C CG . LEU A 1 7 ? -2.213 47.764 42.830 1.00 16.03 ? 33 LEU A CG 1 ATOM 34 C CD1 . LEU A 1 7 ? -3.351 47.884 43.825 1.00 26.20 ? 33 LEU A CD1 1 ATOM 35 C CD2 . LEU A 1 7 ? -1.015 47.067 43.474 1.00 15.53 ? 33 LEU A CD2 1 ATOM 36 N N . LEU A 1 8 ? -2.582 46.770 38.229 1.00 16.03 ? 34 LEU A N 1 ATOM 37 C CA . LEU A 1 8 ? -3.290 46.166 37.100 1.00 16.24 ? 34 LEU A CA 1 ATOM 38 C C . LEU A 1 8 ? -2.351 45.878 35.932 1.00 16.32 ? 34 LEU A C 1 ATOM 39 O O . LEU A 1 8 ? -1.500 46.704 35.588 1.00 17.62 ? 34 LEU A O 1 ATOM 40 C CB . LEU A 1 8 ? -4.417 47.088 36.642 1.00 16.31 ? 34 LEU A CB 1 ATOM 41 C CG . LEU A 1 8 ? -5.442 47.473 37.715 1.00 16.82 ? 34 LEU A CG 1 ATOM 42 C CD1 . LEU A 1 8 ? -6.508 48.423 37.151 1.00 18.75 ? 34 LEU A CD1 1 ATOM 43 C CD2 . LEU A 1 8 ? -6.085 46.216 38.295 1.00 21.27 ? 34 LEU A CD2 1 ATOM 44 N N . ASN A 1 9 ? -2.498 44.701 35.331 1.00 14.70 ? 35 ASN A N 1 ATOM 45 C CA . ASN A 1 9 ? -1.724 44.321 34.147 1.00 12.85 ? 35 ASN A CA 1 ATOM 46 C C . ASN A 1 9 ? -0.223 44.474 34.366 1.00 15.62 ? 35 ASN A C 1 ATOM 47 O O . ASN A 1 9 ? 0.473 45.169 33.617 1.00 17.51 ? 35 ASN A O 1 ATOM 48 C CB . ASN A 1 9 ? -2.192 45.101 32.916 1.00 15.70 ? 35 ASN A CB 1 ATOM 49 C CG . ASN A 1 9 ? -1.818 44.408 31.621 1.00 16.02 ? 35 ASN A CG 1 ATOM 50 O OD1 . ASN A 1 9 ? -2.029 43.212 31.472 1.00 21.04 ? 35 ASN A OD1 1 ATOM 51 N ND2 . ASN A 1 9 ? -1.264 45.166 30.677 1.00 18.25 ? 35 ASN A ND2 1 ATOM 52 N N . VAL A 1 10 ? 0.272 43.801 35.398 1.00 15.86 ? 36 VAL A N 1 ATOM 53 C CA . VAL A 1 10 ? 1.658 43.977 35.798 1.00 12.68 ? 36 VAL A CA 1 ATOM 54 C C . VAL A 1 10 ? 2.226 42.634 36.226 1.00 14.45 ? 36 VAL A C 1 ATOM 55 O O . VAL A 1 10 ? 1.479 41.718 36.548 1.00 13.99 ? 36 VAL A O 1 ATOM 56 C CB . VAL A 1 10 ? 1.792 45.050 36.904 1.00 18.85 ? 36 VAL A CB 1 ATOM 57 C CG1 . VAL A 1 10 ? 1.251 44.539 38.237 1.00 17.27 ? 36 VAL A CG1 1 ATOM 58 C CG2 . VAL A 1 10 ? 3.247 45.515 37.033 1.00 24.76 ? 36 VAL A CG2 1 ATOM 59 N N . CYS A 1 11 ? 3.555 42.524 36.175 1.00 14.90 ? 37 CYS A N 1 ATOM 60 C CA . CYS A 1 11 ? 4.267 41.292 36.457 1.00 16.48 ? 37 CYS A CA 1 ATOM 61 C C . CYS A 1 11 ? 5.429 41.623 37.374 1.00 14.55 ? 37 CYS A C 1 ATOM 62 O O . CYS A 1 11 ? 5.841 42.786 37.460 1.00 17.03 ? 37 CYS A O 1 ATOM 63 C CB . CYS A 1 11 ? 4.845 40.701 35.169 1.00 22.99 ? 37 CYS A CB 1 ATOM 64 S SG . CYS A 1 11 ? 3.688 40.601 33.787 1.00 22.48 ? 37 CYS A SG 1 ATOM 65 N N . MET A 1 12 ? 5.947 40.597 38.051 1.00 14.50 ? 38 MET A N 1 ATOM 66 C CA . MET A 1 12 ? 7.226 40.705 38.735 1.00 17.00 ? 38 MET A CA 1 ATOM 67 C C . MET A 1 12 ? 8.144 39.692 38.087 1.00 19.49 ? 38 MET A C 1 ATOM 68 O O . MET A 1 12 ? 7.803 38.499 38.025 1.00 21.84 ? 38 MET A O 1 ATOM 69 C CB . MET A 1 12 ? 7.065 40.408 40.226 1.00 18.92 ? 38 MET A CB 1 ATOM 70 C CG . MET A 1 12 ? 8.362 40.504 41.021 1.00 22.85 ? 38 MET A CG 1 ATOM 71 S SD . MET A 1 12 ? 8.839 42.215 41.304 1.00 25.42 ? 38 MET A SD 1 ATOM 72 C CE . MET A 1 12 ? 7.476 42.784 42.329 1.00 22.59 ? 38 MET A CE 1 ATOM 73 N N . ASN A 1 13 ? 9.298 40.135 37.590 1.00 19.27 ? 39 ASN A N 1 ATOM 74 C CA . ASN A 1 13 ? 10.205 39.208 36.908 1.00 19.60 ? 39 ASN A CA 1 ATOM 75 C C . ASN A 1 13 ? 11.161 38.473 37.854 1.00 19.80 ? 39 ASN A C 1 ATOM 76 O O . ASN A 1 13 ? 11.126 38.690 39.066 1.00 20.07 ? 39 ASN A O 1 ATOM 77 C CB . ASN A 1 13 ? 10.950 39.879 35.738 1.00 24.05 ? 39 ASN A CB 1 ATOM 78 C CG . ASN A 1 13 ? 11.993 40.902 36.183 1.00 26.53 ? 39 ASN A CG 1 ATOM 79 O OD1 . ASN A 1 13 ? 12.492 40.868 37.306 1.00 25.44 ? 39 ASN A OD1 1 ATOM 80 N ND2 . ASN A 1 13 ? 12.343 41.814 35.275 1.00 32.60 ? 39 ASN A ND2 1 ATOM 81 N N . ALA A 1 14 ? 12.006 37.608 37.297 1.00 19.10 ? 40 ALA A N 1 ATOM 82 C CA . ALA A 1 14 ? 12.917 36.791 38.091 1.00 20.25 ? 40 ALA A CA 1 ATOM 83 C C . ALA A 1 14 ? 14.005 37.599 38.792 1.00 21.72 ? 40 ALA A C 1 ATOM 84 O O . ALA A 1 14 ? 14.650 37.094 39.715 1.00 20.58 ? 40 ALA A O 1 ATOM 85 C CB . ALA A 1 14 ? 13.545 35.699 37.220 1.00 19.67 ? 40 ALA A CB 1 ATOM 86 N N . LYS A 1 15 ? 14.224 38.834 38.333 1.00 20.59 ? 41 LYS A N 1 ATOM 87 C CA . LYS A 1 15 ? 15.166 39.744 38.983 1.00 23.10 ? 41 LYS A CA 1 ATOM 88 C C . LYS A 1 15 ? 14.426 40.631 39.991 1.00 21.30 ? 41 LYS A C 1 ATOM 89 O O . LYS A 1 15 ? 15.016 41.549 40.582 1.00 22.32 ? 41 LYS A O 1 ATOM 90 C CB . LYS A 1 15 ? 15.876 40.627 37.950 1.00 29.53 ? 41 LYS A CB 1 ATOM 91 C CG . LYS A 1 15 ? 16.330 39.886 36.702 1.00 35.36 ? 41 LYS A CG 1 ATOM 92 C CD . LYS A 1 15 ? 17.338 38.825 37.038 1.00 37.09 ? 41 LYS A CD 1 ATOM 93 C CE . LYS A 1 15 ? 17.635 37.912 35.843 1.00 42.16 ? 41 LYS A CE 1 ATOM 94 N NZ . LYS A 1 15 ? 18.222 38.624 34.674 1.00 43.15 ? 41 LYS A NZ 1 ATOM 95 N N . HIS A 1 16 ? 13.138 40.338 40.177 1.00 20.74 ? 42 HIS A N 1 ATOM 96 C CA . HIS A 1 16 ? 12.289 41.054 41.127 1.00 19.78 ? 42 HIS A CA 1 ATOM 97 C C . HIS A 1 16 ? 12.156 42.545 40.837 1.00 20.34 ? 42 HIS A C 1 ATOM 98 O O . HIS A 1 16 ? 12.172 43.373 41.743 1.00 25.23 ? 42 HIS A O 1 ATOM 99 C CB . HIS A 1 16 ? 12.708 40.739 42.564 1.00 19.38 ? 42 HIS A CB 1 ATOM 100 C CG . HIS A 1 16 ? 12.659 39.269 42.868 1.00 17.31 ? 42 HIS A CG 1 ATOM 101 N ND1 . HIS A 1 16 ? 13.777 38.474 42.857 1.00 24.44 ? 42 HIS A ND1 1 ATOM 102 C CD2 . HIS A 1 16 ? 11.605 38.453 43.123 1.00 18.03 ? 42 HIS A CD2 1 ATOM 103 C CE1 . HIS A 1 16 ? 13.426 37.222 43.126 1.00 25.72 ? 42 HIS A CE1 1 ATOM 104 N NE2 . HIS A 1 16 ? 12.118 37.189 43.285 1.00 21.25 ? 42 HIS A NE2 1 ATOM 105 N N . HIS A 1 17 ? 12.022 42.858 39.550 1.00 20.88 ? 43 HIS A N 1 ATOM 106 C CA . HIS A 1 17 ? 11.583 44.171 39.101 1.00 23.67 ? 43 HIS A CA 1 ATOM 107 C C . HIS A 1 17 ? 10.200 44.026 38.481 1.00 21.28 ? 43 HIS A C 1 ATOM 108 O O . HIS A 1 17 ? 9.884 43.007 37.845 1.00 17.05 ? 43 HIS A O 1 ATOM 109 C CB . HIS A 1 17 ? 12.534 44.736 38.045 1.00 28.61 ? 43 HIS A CB 1 ATOM 110 C CG . HIS A 1 17 ? 13.904 45.040 38.557 1.00 43.44 ? 43 HIS A CG 1 ATOM 111 N ND1 . HIS A 1 17 ? 15.040 44.498 38.000 1.00 51.12 ? 43 HIS A ND1 1 ATOM 112 C CD2 . HIS A 1 17 ? 14.326 45.845 39.563 1.00 50.48 ? 43 HIS A CD2 1 ATOM 113 C CE1 . HIS A 1 17 ? 16.104 44.944 38.646 1.00 54.57 ? 43 HIS A CE1 1 ATOM 114 N NE2 . HIS A 1 17 ? 15.695 45.762 39.601 1.00 54.65 ? 43 HIS A NE2 1 ATOM 115 N N . LYS A 1 18 ? 9.357 45.037 38.654 1.00 18.71 ? 44 LYS A N 1 ATOM 116 C CA . LYS A 1 18 ? 8.074 45.012 37.971 1.00 16.47 ? 44 LYS A CA 1 ATOM 117 C C . LYS A 1 18 ? 8.253 45.213 36.471 1.00 15.02 ? 44 LYS A C 1 ATOM 118 O O . LYS A 1 18 ? 9.146 45.940 36.034 1.00 18.31 ? 44 LYS A O 1 ATOM 119 C CB . LYS A 1 18 ? 7.148 46.088 38.528 1.00 20.83 ? 44 LYS A CB 1 ATOM 120 C CG . LYS A 1 18 ? 6.641 45.758 39.928 1.00 34.50 ? 44 LYS A CG 1 ATOM 121 C CD . LYS A 1 18 ? 5.386 46.548 40.264 1.00 46.79 ? 44 LYS A CD 1 ATOM 122 C CE . LYS A 1 18 ? 4.202 45.621 40.497 1.00 51.52 ? 44 LYS A CE 1 ATOM 123 N NZ . LYS A 1 18 ? 3.046 46.377 41.060 1.00 55.67 ? 44 LYS A NZ 1 ATOM 124 N N . GLU A 1 19 ? 7.392 44.566 35.693 1.00 17.07 ? 45 GLU A N 1 ATOM 125 C CA . GLU A 1 19 ? 7.450 44.642 34.239 1.00 21.84 ? 45 GLU A CA 1 ATOM 126 C C . GLU A 1 19 ? 6.039 44.609 33.709 1.00 17.28 ? 45 GLU A C 1 ATOM 127 O O . GLU A 1 19 ? 5.109 44.205 34.414 1.00 21.84 ? 45 GLU A O 1 ATOM 128 C CB . GLU A 1 19 ? 8.202 43.438 33.654 1.00 23.31 ? 45 GLU A CB 1 ATOM 129 C CG . GLU A 1 19 ? 9.704 43.471 33.733 1.00 33.04 ? 45 GLU A CG 1 ATOM 130 C CD . GLU A 1 19 ? 10.327 42.339 32.930 1.00 37.49 ? 45 GLU A CD 1 ATOM 131 O OE1 . GLU A 1 19 ? 9.593 41.398 32.570 1.00 38.25 ? 45 GLU A OE1 1 ATOM 132 O OE2 . GLU A 1 19 ? 11.540 42.396 32.657 1.00 45.12 ? 45 GLU A OE2 1 ATOM 133 N N . LYS A 1 20 ? 5.870 44.998 32.455 1.00 17.02 ? 46 LYS A N 1 ATOM 134 C CA . LYS A 1 20 ? 4.572 44.856 31.812 1.00 16.23 ? 46 LYS A CA 1 ATOM 135 C C . LYS A 1 20 ? 4.549 43.525 31.068 1.00 18.50 ? 46 LYS A C 1 ATOM 136 O O . LYS A 1 20 ? 5.599 43.021 30.650 1.00 16.80 ? 46 LYS A O 1 ATOM 137 C CB . LYS A 1 20 ? 4.308 46.033 30.864 1.00 17.31 ? 46 LYS A CB 1 ATOM 138 C CG . LYS A 1 20 ? 4.111 47.378 31.568 1.00 24.41 ? 46 LYS A CG 1 ATOM 139 C CD . LYS A 1 20 ? 3.020 47.334 32.628 1.00 30.64 ? 46 LYS A CD 1 ATOM 140 C CE . LYS A 1 20 ? 1.641 47.653 32.052 1.00 37.32 ? 46 LYS A CE 1 ATOM 141 N NZ . LYS A 1 20 ? 0.621 47.875 33.134 1.00 34.39 ? 46 LYS A NZ 1 ATOM 142 N N . PRO A 1 21 ? 3.362 42.929 30.924 1.00 15.72 ? 47 PRO A N 1 ATOM 143 C CA . PRO A 1 21 ? 3.268 41.663 30.193 1.00 14.50 ? 47 PRO A CA 1 ATOM 144 C C . PRO A 1 21 ? 3.507 41.799 28.694 1.00 19.22 ? 47 PRO A C 1 ATOM 145 O O . PRO A 1 21 ? 3.620 42.905 28.160 1.00 21.89 ? 47 PRO A O 1 ATOM 146 C CB . PRO A 1 21 ? 1.827 41.201 30.447 1.00 16.20 ? 47 PRO A CB 1 ATOM 147 C CG . PRO A 1 21 ? 1.076 42.440 30.835 1.00 16.85 ? 47 PRO A CG 1 ATOM 148 C CD . PRO A 1 21 ? 2.073 43.351 31.508 1.00 16.04 ? 47 PRO A CD 1 ATOM 149 N N . GLY A 1 22 ? 3.583 40.661 28.021 1.00 16.57 ? 48 GLY A N 1 ATOM 150 C CA . GLY A 1 22 ? 3.827 40.635 26.595 1.00 20.67 ? 48 GLY A CA 1 ATOM 151 C C . GLY A 1 22 ? 3.451 39.292 25.998 1.00 20.67 ? 48 GLY A C 1 ATOM 152 O O . GLY A 1 22 ? 2.877 38.439 26.680 1.00 16.71 ? 48 GLY A O 1 ATOM 153 N N . PRO A 1 23 ? 3.766 39.093 24.714 1.00 21.76 ? 49 PRO A N 1 ATOM 154 C CA . PRO A 1 23 ? 3.474 37.803 24.079 1.00 21.45 ? 49 PRO A CA 1 ATOM 155 C C . PRO A 1 23 ? 4.203 36.669 24.802 1.00 24.01 ? 49 PRO A C 1 ATOM 156 O O . PRO A 1 23 ? 5.378 36.798 25.163 1.00 23.84 ? 49 PRO A O 1 ATOM 157 C CB . PRO A 1 23 ? 3.990 37.985 22.644 1.00 27.60 ? 49 PRO A CB 1 ATOM 158 C CG . PRO A 1 23 ? 4.958 39.152 22.707 1.00 29.73 ? 49 PRO A CG 1 ATOM 159 C CD . PRO A 1 23 ? 4.447 40.037 23.807 1.00 24.96 ? 49 PRO A CD 1 ATOM 160 N N . GLU A 1 24 ? 3.497 35.563 25.013 1.00 17.60 ? 50 GLU A N 1 ATOM 161 C CA . GLU A 1 24 ? 4.020 34.443 25.775 1.00 20.08 ? 50 GLU A CA 1 ATOM 162 C C . GLU A 1 24 ? 5.299 33.884 25.157 1.00 22.63 ? 50 GLU A C 1 ATOM 163 O O . GLU A 1 24 ? 5.447 33.872 23.929 1.00 27.89 ? 50 GLU A O 1 ATOM 164 C CB . GLU A 1 24 ? 2.943 33.365 25.819 1.00 19.11 ? 50 GLU A CB 1 ATOM 165 C CG . GLU A 1 24 ? 3.267 32.160 26.666 1.00 18.55 ? 50 GLU A CG 1 ATOM 166 C CD . GLU A 1 24 ? 2.025 31.316 26.901 1.00 19.93 ? 50 GLU A CD 1 ATOM 167 O OE1 . GLU A 1 24 ? 1.507 30.729 25.925 1.00 23.80 ? 50 GLU A OE1 1 ATOM 168 O OE2 . GLU A 1 24 ? 1.556 31.264 28.062 1.00 20.17 ? 50 GLU A OE2 1 ATOM 169 N N . ASP A 1 25 ? 6.233 33.431 25.994 1.00 20.12 ? 51 ASP A N 1 ATOM 170 C CA . ASP A 1 25 ? 7.464 32.825 25.461 1.00 19.65 ? 51 ASP A CA 1 ATOM 171 C C . ASP A 1 25 ? 7.278 31.359 25.061 1.00 19.05 ? 51 ASP A C 1 ATOM 172 O O . ASP A 1 25 ? 6.281 30.744 25.424 1.00 21.43 ? 51 ASP A O 1 ATOM 173 C CB . ASP A 1 25 ? 8.671 33.015 26.402 1.00 21.16 ? 51 ASP A CB 1 ATOM 174 C CG . ASP A 1 25 ? 8.544 32.252 27.721 1.00 27.75 ? 51 ASP A CG 1 ATOM 175 O OD1 . ASP A 1 25 ? 7.777 31.271 27.819 1.00 25.62 ? 51 ASP A OD1 1 ATOM 176 O OD2 . ASP A 1 25 ? 9.253 32.629 28.677 1.00 33.04 ? 51 ASP A OD2 1 ATOM 177 N N . LYS A 1 26 ? 8.239 30.816 24.320 1.00 22.98 ? 52 LYS A N 1 ATOM 178 C CA . LYS A 1 26 ? 8.141 29.448 23.815 1.00 30.24 ? 52 LYS A CA 1 ATOM 179 C C . LYS A 1 26 ? 8.162 28.370 24.913 1.00 30.19 ? 52 LYS A C 1 ATOM 180 O O . LYS A 1 26 ? 7.468 27.357 24.799 1.00 27.71 ? 52 LYS A O 1 ATOM 181 C CB . LYS A 1 26 ? 9.223 29.179 22.765 1.00 36.29 ? 52 LYS A CB 1 ATOM 182 C CG . LYS A 1 26 ? 9.035 27.857 22.060 1.00 43.12 ? 52 LYS A CG 1 ATOM 183 C CD . LYS A 1 26 ? 9.498 27.883 20.622 1.00 51.17 ? 52 LYS A CD 1 ATOM 184 C CE . LYS A 1 26 ? 8.989 26.641 19.903 1.00 56.86 ? 52 LYS A CE 1 ATOM 185 N NZ . LYS A 1 26 ? 9.878 26.218 18.789 1.00 62.54 ? 52 LYS A NZ 1 ATOM 186 N N . LEU A 1 27 ? 8.942 28.582 25.973 1.00 26.05 ? 53 LEU A N 1 ATOM 187 C CA . LEU A 1 27 ? 8.963 27.625 27.081 1.00 26.18 ? 53 LEU A CA 1 ATOM 188 C C . LEU A 1 27 ? 7.567 27.387 27.667 1.00 24.05 ? 53 LEU A C 1 ATOM 189 O O . LEU A 1 27 ? 7.226 26.261 28.037 1.00 23.27 ? 53 LEU A O 1 ATOM 190 C CB . LEU A 1 27 ? 9.936 28.059 28.186 1.00 26.65 ? 53 LEU A CB 1 ATOM 191 C CG . LEU A 1 27 ? 10.075 27.030 29.317 1.00 27.60 ? 53 LEU A CG 1 ATOM 192 C CD1 . LEU A 1 27 ? 11.507 26.859 29.734 1.00 34.14 ? 53 LEU A CD1 1 ATOM 193 C CD2 . LEU A 1 27 ? 9.221 27.383 30.523 1.00 27.19 ? 53 LEU A CD2 1 ATOM 194 N N . HIS A 1 28 ? 6.763 28.444 27.741 1.00 16.29 ? 54 HIS A N 1 ATOM 195 C CA . HIS A 1 28 ? 5.450 28.369 28.358 1.00 15.11 ? 54 HIS A CA 1 ATOM 196 C C . HIS A 1 28 ? 4.335 28.103 27.342 1.00 17.60 ? 54 HIS A C 1 ATOM 197 O O . HIS A 1 28 ? 3.181 28.411 27.611 1.00 17.99 ? 54 HIS A O 1 ATOM 198 C CB . HIS A 1 28 ? 5.167 29.670 29.124 1.00 13.35 ? 54 HIS A CB 1 ATOM 199 C CG . HIS A 1 28 ? 6.003 29.845 30.350 1.00 16.49 ? 54 HIS A CG 1 ATOM 200 N ND1 . HIS A 1 28 ? 7.275 30.355 30.319 1.00 14.97 ? 54 HIS A ND1 1 ATOM 201 C CD2 . HIS A 1 28 ? 5.735 29.568 31.657 1.00 14.90 ? 54 HIS A CD2 1 ATOM 202 C CE1 . HIS A 1 28 ? 7.778 30.379 31.550 1.00 19.54 ? 54 HIS A CE1 1 ATOM 203 N NE2 . HIS A 1 28 ? 6.851 29.912 32.372 1.00 17.35 ? 54 HIS A NE2 1 ATOM 204 N N . GLU A 1 29 ? 4.673 27.504 26.201 1.00 19.94 ? 55 GLU A N 1 ATOM 205 C CA . GLU A 1 29 ? 3.685 27.240 25.146 1.00 26.76 ? 55 GLU A CA 1 ATOM 206 C C . GLU A 1 29 ? 2.425 26.495 25.629 1.00 24.69 ? 55 GLU A C 1 ATOM 207 O O . GLU A 1 29 ? 1.312 26.744 25.135 1.00 26.35 ? 55 GLU A O 1 ATOM 208 C CB . GLU A 1 29 ? 4.335 26.487 23.981 1.00 35.56 ? 55 GLU A CB 1 ATOM 209 C CG . GLU A 1 29 ? 3.370 26.142 22.858 1.00 47.58 ? 55 GLU A CG 1 ATOM 210 C CD . GLU A 1 29 ? 4.053 26.006 21.510 1.00 59.14 ? 55 GLU A CD 1 ATOM 211 O OE1 . GLU A 1 29 ? 5.301 25.949 21.476 1.00 62.55 ? 55 GLU A OE1 1 ATOM 212 O OE2 . GLU A 1 29 ? 3.338 25.965 20.483 1.00 63.45 ? 55 GLU A OE2 1 ATOM 213 N N . GLN A 1 30 ? 2.587 25.592 26.592 1.00 20.70 ? 56 GLN A N 1 ATOM 214 C CA . GLN A 1 30 ? 1.446 24.813 27.072 1.00 19.79 ? 56 GLN A CA 1 ATOM 215 C C . GLN A 1 30 ? 0.511 25.655 27.943 1.00 19.68 ? 56 GLN A C 1 ATOM 216 O O . GLN A 1 30 ? -0.633 25.244 28.203 1.00 22.09 ? 56 GLN A O 1 ATOM 217 C CB . GLN A 1 30 ? 1.908 23.579 27.843 1.00 25.32 ? 56 GLN A CB 1 ATOM 218 C CG . GLN A 1 30 ? 2.593 23.887 29.158 1.00 26.50 ? 56 GLN A CG 1 ATOM 219 C CD . GLN A 1 30 ? 3.350 22.688 29.699 1.00 31.64 ? 56 GLN A CD 1 ATOM 220 O OE1 . GLN A 1 30 ? 4.586 22.656 29.682 1.00 33.68 ? 56 GLN A OE1 1 ATOM 221 N NE2 . GLN A 1 30 ? 2.613 21.683 30.164 1.00 36.00 ? 56 GLN A NE2 1 ATOM 222 N N . CYS A 1 31 ? 0.990 26.818 28.385 1.00 19.86 ? 57 CYS A N 1 ATOM 223 C CA . CYS A 1 31 ? 0.181 27.750 29.175 1.00 14.34 ? 57 CYS A CA 1 ATOM 224 C C . CYS A 1 31 ? -0.732 28.563 28.242 1.00 15.67 ? 57 CYS A C 1 ATOM 225 O O . CYS A 1 31 ? -0.650 29.799 28.168 1.00 16.77 ? 57 CYS A O 1 ATOM 226 C CB . CYS A 1 31 ? 1.080 28.672 30.013 1.00 13.14 ? 57 CYS A CB 1 ATOM 227 S SG . CYS A 1 31 ? 2.110 27.797 31.215 1.00 16.94 ? 57 CYS A SG 1 ATOM 228 N N . ARG A 1 32 ? -1.612 27.844 27.550 1.00 17.30 ? 58 ARG A N 1 ATOM 229 C CA . ARG A 1 32 ? -2.405 28.390 26.451 1.00 18.04 ? 58 ARG A CA 1 ATOM 230 C C . ARG A 1 32 ? -3.280 29.608 26.755 1.00 16.98 ? 58 ARG A C 1 ATOM 231 O O . ARG A 1 32 ? -3.463 30.446 25.876 1.00 19.01 ? 58 ARG A O 1 ATOM 232 C CB . ARG A 1 32 ? -3.249 27.285 25.804 1.00 24.80 ? 58 ARG A CB 1 ATOM 233 C CG . ARG A 1 32 ? -2.467 26.416 24.818 1.00 35.82 ? 58 ARG A CG 1 ATOM 234 C CD . ARG A 1 32 ? -3.361 25.402 24.114 1.00 47.21 ? 58 ARG A CD 1 ATOM 235 N NE . ARG A 1 32 ? -2.780 24.939 22.854 1.00 54.71 ? 58 ARG A NE 1 ATOM 236 C CZ . ARG A 1 32 ? -3.381 25.043 21.671 1.00 61.75 ? 58 ARG A CZ 1 ATOM 237 N NH1 . ARG A 1 32 ? -4.589 25.586 21.580 1.00 63.89 ? 58 ARG A NH1 1 ATOM 238 N NH2 . ARG A 1 32 ? -2.781 24.595 20.576 1.00 65.39 ? 58 ARG A NH2 1 ATOM 239 N N . PRO A 1 33 ? -3.845 29.708 27.976 1.00 16.62 ? 59 PRO A N 1 ATOM 240 C CA . PRO A 1 33 ? -4.740 30.854 28.180 1.00 17.27 ? 59 PRO A CA 1 ATOM 241 C C . PRO A 1 33 ? -4.035 32.218 28.105 1.00 15.83 ? 59 PRO A C 1 ATOM 242 O O . PRO A 1 33 ? -4.698 33.239 27.859 1.00 19.33 ? 59 PRO A O 1 ATOM 243 C CB . PRO A 1 33 ? -5.271 30.616 29.590 1.00 16.79 ? 59 PRO A CB 1 ATOM 244 C CG . PRO A 1 33 ? -5.314 29.095 29.693 1.00 17.37 ? 59 PRO A CG 1 ATOM 245 C CD . PRO A 1 33 ? -3.991 28.721 29.066 1.00 17.20 ? 59 PRO A CD 1 ATOM 246 N N . TRP A 1 34 ? -2.724 32.233 28.299 1.00 17.00 ? 60 TRP A N 1 ATOM 247 C CA . TRP A 1 34 ? -1.994 33.497 28.399 1.00 15.01 ? 60 TRP A CA 1 ATOM 248 C C . TRP A 1 34 ? -1.185 33.823 27.163 1.00 18.95 ? 60 TRP A C 1 ATOM 249 O O . TRP A 1 34 ? -0.351 34.729 27.200 1.00 22.77 ? 60 TRP A O 1 ATOM 250 C CB . TRP A 1 34 ? -1.077 33.464 29.618 1.00 15.76 ? 60 TRP A CB 1 ATOM 251 C CG . TRP A 1 34 ? -1.874 33.362 30.874 1.00 13.07 ? 60 TRP A CG 1 ATOM 252 C CD1 . TRP A 1 34 ? -2.436 34.394 31.564 1.00 15.08 ? 60 TRP A CD1 1 ATOM 253 C CD2 . TRP A 1 34 ? -2.247 32.166 31.560 1.00 12.52 ? 60 TRP A CD2 1 ATOM 254 N NE1 . TRP A 1 34 ? -3.114 33.911 32.660 1.00 16.93 ? 60 TRP A NE1 1 ATOM 255 C CE2 . TRP A 1 34 ? -3.024 32.545 32.671 1.00 15.06 ? 60 TRP A CE2 1 ATOM 256 C CE3 . TRP A 1 34 ? -2.002 30.805 31.341 1.00 13.81 ? 60 TRP A CE3 1 ATOM 257 C CZ2 . TRP A 1 34 ? -3.552 31.616 33.564 1.00 15.84 ? 60 TRP A CZ2 1 ATOM 258 C CZ3 . TRP A 1 34 ? -2.529 29.885 32.231 1.00 16.06 ? 60 TRP A CZ3 1 ATOM 259 C CH2 . TRP A 1 34 ? -3.284 30.297 33.331 1.00 14.37 ? 60 TRP A CH2 1 ATOM 260 N N . ARG A 1 35 ? -1.437 33.094 26.080 1.00 18.97 ? 61 ARG A N 1 ATOM 261 C CA . ARG A 1 35 ? -0.688 33.240 24.833 1.00 21.32 ? 61 ARG A CA 1 ATOM 262 C C . ARG A 1 35 ? -0.494 34.696 24.392 1.00 22.77 ? 61 ARG A C 1 ATOM 263 O O . ARG A 1 35 ? 0.561 35.069 23.873 1.00 24.64 ? 61 ARG A O 1 ATOM 264 C CB . ARG A 1 35 ? -1.401 32.467 23.721 1.00 27.51 ? 61 ARG A CB 1 ATOM 265 C CG . ARG A 1 35 ? -0.624 32.357 22.427 1.00 37.68 ? 61 ARG A CG 1 ATOM 266 C CD . ARG A 1 35 ? -1.235 31.289 21.534 1.00 49.01 ? 61 ARG A CD 1 ATOM 267 N NE . ARG A 1 35 ? -2.595 31.625 21.121 1.00 58.05 ? 61 ARG A NE 1 ATOM 268 C CZ . ARG A 1 35 ? -2.965 31.827 19.860 1.00 65.48 ? 61 ARG A CZ 1 ATOM 269 N NH1 . ARG A 1 35 ? -2.076 31.718 18.879 1.00 67.75 ? 61 ARG A NH1 1 ATOM 270 N NH2 . ARG A 1 35 ? -4.228 32.127 19.577 1.00 67.31 ? 61 ARG A NH2 1 ATOM 271 N N . LYS A 1 36 ? -1.517 35.518 24.586 1.00 21.17 ? 62 LYS A N 1 ATOM 272 C CA . LYS A 1 36 ? -1.505 36.857 24.008 1.00 27.92 ? 62 LYS A CA 1 ATOM 273 C C . LYS A 1 36 ? -1.034 37.945 24.968 1.00 27.55 ? 62 LYS A C 1 ATOM 274 O O . LYS A 1 36 ? -0.579 39.008 24.534 1.00 30.59 ? 62 LYS A O 1 ATOM 275 C CB . LYS A 1 36 ? -2.882 37.205 23.449 1.00 33.35 ? 62 LYS A CB 1 ATOM 276 C CG . LYS A 1 36 ? -3.163 36.578 22.095 1.00 41.68 ? 62 LYS A CG 1 ATOM 277 C CD . LYS A 1 36 ? -2.004 36.848 21.144 1.00 50.67 ? 62 LYS A CD 1 ATOM 278 C CE . LYS A 1 36 ? -2.463 36.987 19.698 1.00 57.66 ? 62 LYS A CE 1 ATOM 279 N NZ . LYS A 1 36 ? -1.735 38.099 19.014 1.00 60.82 ? 62 LYS A NZ 1 ATOM 280 N N . ASN A 1 37 ? -1.149 37.687 26.264 1.00 20.90 ? 63 ASN A N 1 ATOM 281 C CA . ASN A 1 37 ? -0.802 38.694 27.263 1.00 21.27 ? 63 ASN A CA 1 ATOM 282 C C . ASN A 1 37 ? -0.330 37.969 28.508 1.00 21.56 ? 63 ASN A C 1 ATOM 283 O O . ASN A 1 37 ? -1.146 37.467 29.292 1.00 23.57 ? 63 ASN A O 1 ATOM 284 C CB . ASN A 1 37 ? -2.015 39.566 27.595 1.00 19.52 ? 63 ASN A CB 1 ATOM 285 C CG . ASN A 1 37 ? -1.648 40.805 28.394 1.00 26.67 ? 63 ASN A CG 1 ATOM 286 O OD1 . ASN A 1 37 ? -0.670 41.486 28.085 1.00 29.70 ? 63 ASN A OD1 1 ATOM 287 N ND2 . ASN A 1 37 ? -2.440 41.112 29.420 1.00 23.59 ? 63 ASN A ND2 1 ATOM 288 N N . ALA A 1 38 ? 0.987 37.890 28.678 1.00 17.78 ? 64 ALA A N 1 ATOM 289 C CA . ALA A 1 38 ? 1.571 37.003 29.677 1.00 15.14 ? 64 ALA A CA 1 ATOM 290 C C . ALA A 1 38 ? 2.727 37.665 30.392 1.00 15.54 ? 64 ALA A C 1 ATOM 291 O O . ALA A 1 38 ? 3.441 38.480 29.799 1.00 17.19 ? 64 ALA A O 1 ATOM 292 C CB . ALA A 1 38 ? 2.070 35.743 29.002 1.00 16.94 ? 64 ALA A CB 1 ATOM 293 N N . CYS A 1 39 ? 2.935 37.279 31.648 1.00 14.04 ? 65 CYS A N 1 ATOM 294 C CA . CYS A 1 39 ? 4.138 37.679 32.379 1.00 14.68 ? 65 CYS A CA 1 ATOM 295 C C . CYS A 1 39 ? 5.284 36.715 32.096 1.00 15.24 ? 65 CYS A C 1 ATOM 296 O O . CYS A 1 39 ? 6.405 36.965 32.515 1.00 20.72 ? 65 CYS A O 1 ATOM 297 C CB . CYS A 1 39 ? 3.880 37.691 33.880 1.00 15.74 ? 65 CYS A CB 1 ATOM 298 S SG . CYS A 1 39 ? 2.715 38.938 34.372 1.00 19.03 ? 65 CYS A SG 1 ATOM 299 N N . CYS A 1 40 ? 4.991 35.619 31.409 1.00 17.19 ? 66 CYS A N 1 ATOM 300 C CA . CYS A 1 40 ? 6.018 34.665 31.007 1.00 15.59 ? 66 CYS A CA 1 ATOM 301 C C . CYS A 1 40 ? 6.279 34.957 29.544 1.00 19.73 ? 66 CYS A C 1 ATOM 302 O O . CYS A 1 40 ? 5.918 34.174 28.652 1.00 19.77 ? 66 CYS A O 1 ATOM 303 C CB . CYS A 1 40 ? 5.543 33.222 31.210 1.00 14.42 ? 66 CYS A CB 1 ATOM 304 S SG . CYS A 1 40 ? 3.931 32.764 30.438 1.00 17.12 ? 66 CYS A SG 1 ATOM 305 N N . SER A 1 41 ? 6.907 36.103 29.314 1.00 20.34 ? 67 SER A N 1 ATOM 306 C CA . SER A 1 41 ? 6.892 36.749 28.011 1.00 20.49 ? 67 SER A CA 1 ATOM 307 C C . SER A 1 41 ? 8.263 36.785 27.360 1.00 24.82 ? 67 SER A C 1 ATOM 308 O O . SER A 1 41 ? 9.284 36.601 28.020 1.00 23.82 ? 67 SER A O 1 ATOM 309 C CB . SER A 1 41 ? 6.388 38.179 28.167 1.00 22.75 ? 67 SER A CB 1 ATOM 310 O OG . SER A 1 41 ? 7.270 38.929 28.989 1.00 27.41 ? 67 SER A OG 1 ATOM 311 N N . THR A 1 42 ? 8.263 37.036 26.056 1.00 26.64 ? 68 THR A N 1 ATOM 312 C CA . THR A 1 42 ? 9.485 37.268 25.310 1.00 36.28 ? 68 THR A CA 1 ATOM 313 C C . THR A 1 42 ? 10.129 38.577 25.760 1.00 40.64 ? 68 THR A C 1 ATOM 314 O O . THR A 1 42 ? 9.476 39.432 26.374 1.00 34.24 ? 68 THR A O 1 ATOM 315 C CB . THR A 1 42 ? 9.204 37.330 23.792 1.00 40.94 ? 68 THR A CB 1 ATOM 316 O OG1 . THR A 1 42 ? 8.273 38.384 23.509 1.00 39.08 ? 68 THR A OG1 1 ATOM 317 C CG2 . THR A 1 42 ? 8.622 36.004 23.304 1.00 40.24 ? 68 THR A CG2 1 ATOM 318 N N . ASN A 1 43 ? 11.412 38.735 25.452 1.00 48.00 ? 69 ASN A N 1 ATOM 319 C CA . ASN A 1 43 ? 12.140 39.937 25.843 1.00 54.91 ? 69 ASN A CA 1 ATOM 320 C C . ASN A 1 43 ? 12.596 40.754 24.650 1.00 58.82 ? 69 ASN A C 1 ATOM 321 O O . ASN A 1 43 ? 13.087 40.210 23.661 1.00 61.22 ? 69 ASN A O 1 ATOM 322 C CB . ASN A 1 43 ? 13.352 39.579 26.695 1.00 58.40 ? 69 ASN A CB 1 ATOM 323 C CG . ASN A 1 43 ? 12.986 38.762 27.900 1.00 58.67 ? 69 ASN A CG 1 ATOM 324 O OD1 . ASN A 1 43 ? 11.921 38.949 28.494 1.00 49.08 ? 69 ASN A OD1 1 ATOM 325 N ND2 . ASN A 1 43 ? 13.861 37.841 28.268 1.00 68.07 ? 69 ASN A ND2 1 ATOM 326 N N . THR A 1 44 ? 12.455 42.068 24.761 1.00 59.72 ? 70 THR A N 1 ATOM 327 C CA . THR A 1 44 ? 12.807 42.959 23.668 1.00 60.23 ? 70 THR A CA 1 ATOM 328 C C . THR A 1 44 ? 14.315 43.218 23.597 1.00 59.01 ? 70 THR A C 1 ATOM 329 O O . THR A 1 44 ? 14.832 43.644 22.561 1.00 62.20 ? 70 THR A O 1 ATOM 330 C CB . THR A 1 44 ? 12.053 44.289 23.782 1.00 62.98 ? 70 THR A CB 1 ATOM 331 O OG1 . THR A 1 44 ? 12.450 44.975 24.979 1.00 63.39 ? 70 THR A OG1 1 ATOM 332 C CG2 . THR A 1 44 ? 10.548 44.056 23.806 1.00 60.89 ? 70 THR A CG2 1 ATOM 333 N N . SER A 1 45 ? 15.018 42.951 24.695 1.00 53.53 ? 71 SER A N 1 ATOM 334 C CA . SER A 1 45 ? 16.469 43.138 24.741 1.00 52.24 ? 71 SER A CA 1 ATOM 335 C C . SER A 1 45 ? 17.166 41.800 24.975 1.00 52.49 ? 71 SER A C 1 ATOM 336 O O . SER A 1 45 ? 16.517 40.800 25.288 1.00 46.76 ? 71 SER A O 1 ATOM 337 C CB . SER A 1 45 ? 16.847 44.121 25.850 1.00 48.90 ? 71 SER A CB 1 ATOM 338 O OG . SER A 1 45 ? 16.439 43.630 27.118 1.00 47.55 ? 71 SER A OG 1 ATOM 339 N N . GLN A 1 46 ? 18.489 41.791 24.833 1.00 57.00 ? 72 GLN A N 1 ATOM 340 C CA . GLN A 1 46 ? 19.277 40.571 25.004 1.00 57.45 ? 72 GLN A CA 1 ATOM 341 C C . GLN A 1 46 ? 19.511 40.239 26.477 1.00 56.41 ? 72 GLN A C 1 ATOM 342 O O . GLN A 1 46 ? 20.648 40.034 26.902 1.00 59.88 ? 72 GLN A O 1 ATOM 343 C CB . GLN A 1 46 ? 20.614 40.676 24.258 1.00 60.67 ? 72 GLN A CB 1 ATOM 344 C CG . GLN A 1 46 ? 20.498 40.567 22.732 1.00 63.47 ? 72 GLN A CG 1 ATOM 345 C CD . GLN A 1 46 ? 19.741 41.731 22.108 1.00 65.97 ? 72 GLN A CD 1 ATOM 346 O OE1 . GLN A 1 46 ? 20.049 42.898 22.364 1.00 68.26 ? 72 GLN A OE1 1 ATOM 347 N NE2 . GLN A 1 46 ? 18.742 41.417 21.290 1.00 63.45 ? 72 GLN A NE2 1 ATOM 348 N N . GLU A 1 47 ? 18.429 40.193 27.250 1.00 52.63 ? 73 GLU A N 1 ATOM 349 C CA . GLU A 1 47 ? 18.497 39.767 28.641 1.00 52.22 ? 73 GLU A CA 1 ATOM 350 C C . GLU A 1 47 ? 18.987 38.325 28.694 1.00 55.50 ? 73 GLU A C 1 ATOM 351 O O . GLU A 1 47 ? 18.578 37.497 27.875 1.00 53.68 ? 73 GLU A O 1 ATOM 352 C CB . GLU A 1 47 ? 17.125 39.890 29.304 1.00 46.58 ? 73 GLU A CB 1 ATOM 353 N N . ALA A 1 48 ? 19.867 38.034 29.651 1.00 58.74 ? 74 ALA A N 1 ATOM 354 C CA . ALA A 1 48 ? 20.408 36.688 29.817 1.00 59.25 ? 74 ALA A CA 1 ATOM 355 C C . ALA A 1 48 ? 19.298 35.654 29.970 1.00 56.94 ? 74 ALA A C 1 ATOM 356 O O . ALA A 1 48 ? 18.355 35.834 30.748 1.00 51.14 ? 74 ALA A O 1 ATOM 357 C CB . ALA A 1 48 ? 21.366 36.631 31.001 1.00 59.27 ? 74 ALA A CB 1 ATOM 358 N N . HIS A 1 49 ? 19.410 34.576 29.205 1.00 61.61 ? 75 HIS A N 1 ATOM 359 C CA . HIS A 1 49 ? 18.398 33.532 29.227 1.00 61.82 ? 75 HIS A CA 1 ATOM 360 C C . HIS A 1 49 ? 18.648 32.560 30.370 1.00 59.26 ? 75 HIS A C 1 ATOM 361 O O . HIS A 1 49 ? 19.629 31.816 30.359 1.00 61.33 ? 75 HIS A O 1 ATOM 362 C CB . HIS A 1 49 ? 18.367 32.796 27.893 1.00 65.07 ? 75 HIS A CB 1 ATOM 363 N N . LYS A 1 50 ? 17.767 32.588 31.363 1.00 54.26 ? 76 LYS A N 1 ATOM 364 C CA . LYS A 1 50 ? 17.766 31.579 32.414 1.00 53.15 ? 76 LYS A CA 1 ATOM 365 C C . LYS A 1 50 ? 16.322 31.266 32.769 1.00 49.01 ? 76 LYS A C 1 ATOM 366 O O . LYS A 1 50 ? 15.611 32.107 33.323 1.00 47.03 ? 76 LYS A O 1 ATOM 367 C CB . LYS A 1 50 ? 18.528 32.061 33.634 1.00 53.38 ? 76 LYS A CB 1 ATOM 368 N N . ASP A 1 51 ? 15.885 30.061 32.422 1.00 48.48 ? 77 ASP A N 1 ATOM 369 C CA . ASP A 1 51 ? 14.542 29.619 32.764 1.00 47.14 ? 77 ASP A CA 1 ATOM 370 C C . ASP A 1 51 ? 14.463 29.380 34.267 1.00 39.61 ? 77 ASP A C 1 ATOM 371 O O . ASP A 1 51 ? 15.262 28.621 34.822 1.00 40.20 ? 77 ASP A O 1 ATOM 372 C CB . ASP A 1 51 ? 14.186 28.332 32.011 1.00 54.12 ? 77 ASP A CB 1 ATOM 373 C CG . ASP A 1 51 ? 14.307 28.479 30.503 1.00 63.47 ? 77 ASP A CG 1 ATOM 374 O OD1 . ASP A 1 51 ? 14.008 29.577 29.983 1.00 66.96 ? 77 ASP A OD1 1 ATOM 375 O OD2 . ASP A 1 51 ? 14.688 27.490 29.834 1.00 65.74 ? 77 ASP A OD2 1 ATOM 376 N N . VAL A 1 52 ? 13.517 30.038 34.935 1.00 29.62 ? 78 VAL A N 1 ATOM 377 C CA . VAL A 1 52 ? 13.285 29.748 36.347 1.00 25.60 ? 78 VAL A CA 1 ATOM 378 C C . VAL A 1 52 ? 11.952 29.038 36.515 1.00 22.59 ? 78 VAL A C 1 ATOM 379 O O . VAL A 1 52 ? 11.499 28.805 37.635 1.00 25.74 ? 78 VAL A O 1 ATOM 380 C CB . VAL A 1 52 ? 13.330 31.004 37.243 1.00 24.14 ? 78 VAL A CB 1 ATOM 381 C CG1 . VAL A 1 52 ? 14.666 31.716 37.104 1.00 28.62 ? 78 VAL A CG1 1 ATOM 382 C CG2 . VAL A 1 52 ? 12.169 31.946 36.931 1.00 23.15 ? 78 VAL A CG2 1 ATOM 383 N N . SER A 1 53 ? 11.339 28.672 35.395 1.00 19.56 ? 79 SER A N 1 ATOM 384 C CA . SER A 1 53 ? 10.038 27.998 35.418 1.00 17.14 ? 79 SER A CA 1 ATOM 385 C C . SER A 1 53 ? 10.086 26.668 36.166 1.00 17.79 ? 79 SER A C 1 ATOM 386 O O . SER A 1 53 ? 11.109 25.976 36.166 1.00 19.15 ? 79 SER A O 1 ATOM 387 C CB . SER A 1 53 ? 9.533 27.763 33.995 1.00 18.59 ? 79 SER A CB 1 ATOM 388 O OG . SER A 1 53 ? 8.292 27.083 33.985 1.00 18.08 ? 79 SER A OG 1 ATOM 389 N N . TYR A 1 54 ? 8.976 26.323 36.810 1.00 16.34 ? 80 TYR A N 1 ATOM 390 C CA . TYR A 1 54 ? 8.834 25.003 37.416 1.00 14.74 ? 80 TYR A CA 1 ATOM 391 C C . TYR A 1 54 ? 8.409 23.959 36.389 1.00 18.24 ? 80 TYR A C 1 ATOM 392 O O . TYR A 1 54 ? 8.480 22.774 36.667 1.00 17.67 ? 80 TYR A O 1 ATOM 393 C CB . TYR A 1 54 ? 7.777 25.051 38.526 1.00 12.44 ? 80 TYR A CB 1 ATOM 394 C CG . TYR A 1 54 ? 8.314 25.351 39.912 1.00 16.73 ? 80 TYR A CG 1 ATOM 395 C CD1 . TYR A 1 54 ? 9.650 25.659 40.111 1.00 19.47 ? 80 TYR A CD1 1 ATOM 396 C CD2 . TYR A 1 54 ? 7.482 25.281 41.025 1.00 17.57 ? 80 TYR A CD2 1 ATOM 397 C CE1 . TYR A 1 54 ? 10.146 25.906 41.382 1.00 21.18 ? 80 TYR A CE1 1 ATOM 398 C CE2 . TYR A 1 54 ? 7.966 25.526 42.295 1.00 21.07 ? 80 TYR A CE2 1 ATOM 399 C CZ . TYR A 1 54 ? 9.297 25.839 42.469 1.00 24.58 ? 80 TYR A CZ 1 ATOM 400 O OH . TYR A 1 54 ? 9.778 26.077 43.738 1.00 30.26 ? 80 TYR A OH 1 ATOM 401 N N . LEU A 1 55 ? 7.940 24.388 35.214 1.00 13.72 ? 81 LEU A N 1 ATOM 402 C CA . LEU A 1 55 ? 7.398 23.448 34.215 1.00 15.00 ? 81 LEU A CA 1 ATOM 403 C C . LEU A 1 55 ? 8.306 22.280 33.837 1.00 20.75 ? 81 LEU A C 1 ATOM 404 O O . LEU A 1 55 ? 7.833 21.147 33.678 1.00 25.08 ? 81 LEU A O 1 ATOM 405 C CB . LEU A 1 55 ? 6.960 24.186 32.949 1.00 14.24 ? 81 LEU A CB 1 ATOM 406 C CG . LEU A 1 55 ? 5.735 25.075 33.138 1.00 14.50 ? 81 LEU A CG 1 ATOM 407 C CD1 . LEU A 1 55 ? 5.509 25.943 31.919 1.00 18.41 ? 81 LEU A CD1 1 ATOM 408 C CD2 . LEU A 1 55 ? 4.487 24.237 33.425 1.00 16.89 ? 81 LEU A CD2 1 ATOM 409 N N . TYR A 1 56 ? 9.597 22.548 33.684 1.00 16.50 ? 82 TYR A N 1 ATOM 410 C CA . TYR A 1 56 ? 10.542 21.496 33.338 1.00 16.79 ? 82 TYR A CA 1 ATOM 411 C C . TYR A 1 56 ? 11.594 21.365 34.430 1.00 16.60 ? 82 TYR A C 1 ATOM 412 O O . TYR A 1 56 ? 12.707 20.909 34.183 1.00 16.45 ? 82 TYR A O 1 ATOM 413 C CB . TYR A 1 56 ? 11.194 21.799 31.983 1.00 15.92 ? 82 TYR A CB 1 ATOM 414 C CG . TYR A 1 56 ? 10.185 21.896 30.849 1.00 16.98 ? 82 TYR A CG 1 ATOM 415 C CD1 . TYR A 1 56 ? 9.554 23.096 30.555 1.00 16.13 ? 82 TYR A CD1 1 ATOM 416 C CD2 . TYR A 1 56 ? 9.849 20.778 30.088 1.00 17.69 ? 82 TYR A CD2 1 ATOM 417 C CE1 . TYR A 1 56 ? 8.618 23.183 29.535 1.00 16.96 ? 82 TYR A CE1 1 ATOM 418 C CE2 . TYR A 1 56 ? 8.924 20.863 29.054 1.00 16.40 ? 82 TYR A CE2 1 ATOM 419 C CZ . TYR A 1 56 ? 8.312 22.063 28.786 1.00 17.35 ? 82 TYR A CZ 1 ATOM 420 O OH . TYR A 1 56 ? 7.391 22.152 27.757 1.00 22.37 ? 82 TYR A OH 1 ATOM 421 N N . ARG A 1 57 ? 11.236 21.775 35.641 1.00 20.21 ? 83 ARG A N 1 ATOM 422 C CA . ARG A 1 57 ? 12.183 21.775 36.752 1.00 20.50 ? 83 ARG A CA 1 ATOM 423 C C . ARG A 1 57 ? 11.636 21.045 37.981 1.00 18.73 ? 83 ARG A C 1 ATOM 424 O O . ARG A 1 57 ? 12.320 20.214 38.579 1.00 22.97 ? 83 ARG A O 1 ATOM 425 C CB . ARG A 1 57 ? 12.606 23.217 37.056 1.00 25.71 ? 83 ARG A CB 1 ATOM 426 C CG . ARG A 1 57 ? 13.270 23.501 38.386 1.00 34.58 ? 83 ARG A CG 1 ATOM 427 C CD . ARG A 1 57 ? 13.869 24.908 38.316 1.00 43.48 ? 83 ARG A CD 1 ATOM 428 N NE . ARG A 1 57 ? 14.052 25.575 39.602 1.00 51.21 ? 83 ARG A NE 1 ATOM 429 C CZ . ARG A 1 57 ? 13.485 26.738 39.922 1.00 55.77 ? 83 ARG A CZ 1 ATOM 430 N NH1 . ARG A 1 57 ? 12.691 27.361 39.058 1.00 53.68 ? 83 ARG A NH1 1 ATOM 431 N NH2 . ARG A 1 57 ? 13.713 27.281 41.110 1.00 59.21 ? 83 ARG A NH2 1 ATOM 432 N N . PHE A 1 58 ? 10.396 21.322 38.344 1.00 13.48 ? 84 PHE A N 1 ATOM 433 C CA . PHE A 1 58 ? 9.843 20.734 39.555 1.00 12.09 ? 84 PHE A CA 1 ATOM 434 C C . PHE A 1 58 ? 9.444 19.286 39.345 1.00 13.55 ? 84 PHE A C 1 ATOM 435 O O . PHE A 1 58 ? 8.813 18.938 38.336 1.00 17.08 ? 84 PHE A O 1 ATOM 436 C CB . PHE A 1 58 ? 8.636 21.549 40.046 1.00 13.51 ? 84 PHE A CB 1 ATOM 437 C CG . PHE A 1 58 ? 8.227 21.223 41.456 1.00 13.73 ? 84 PHE A CG 1 ATOM 438 C CD1 . PHE A 1 58 ? 8.801 21.898 42.532 1.00 16.29 ? 84 PHE A CD1 1 ATOM 439 C CD2 . PHE A 1 58 ? 7.295 20.235 41.710 1.00 15.81 ? 84 PHE A CD2 1 ATOM 440 C CE1 . PHE A 1 58 ? 8.424 21.600 43.848 1.00 17.71 ? 84 PHE A CE1 1 ATOM 441 C CE2 . PHE A 1 58 ? 6.913 19.925 43.021 1.00 14.43 ? 84 PHE A CE2 1 ATOM 442 C CZ . PHE A 1 58 ? 7.482 20.616 44.089 1.00 12.68 ? 84 PHE A CZ 1 ATOM 443 N N . ASN A 1 59 ? 9.795 18.438 40.313 1.00 12.71 ? 85 ASN A N 1 ATOM 444 C CA . ASN A 1 59 ? 9.530 17.016 40.228 1.00 11.79 ? 85 ASN A CA 1 ATOM 445 C C . ASN A 1 59 ? 8.193 16.688 40.874 1.00 13.76 ? 85 ASN A C 1 ATOM 446 O O . ASN A 1 59 ? 8.112 16.475 42.086 1.00 14.04 ? 85 ASN A O 1 ATOM 447 C CB . ASN A 1 59 ? 10.677 16.260 40.906 1.00 12.32 ? 85 ASN A CB 1 ATOM 448 C CG . ASN A 1 59 ? 10.485 14.766 40.913 1.00 13.03 ? 85 ASN A CG 1 ATOM 449 O OD1 . ASN A 1 59 ? 9.678 14.218 40.153 1.00 14.68 ? 85 ASN A OD1 1 ATOM 450 N ND2 . ASN A 1 59 ? 11.222 14.090 41.785 1.00 14.58 ? 85 ASN A ND2 1 ATOM 451 N N . TRP A 1 60 ? 7.147 16.659 40.050 1.00 13.86 ? 86 TRP A N 1 ATOM 452 C CA . TRP A 1 60 ? 5.812 16.304 40.497 1.00 12.80 ? 86 TRP A CA 1 ATOM 453 C C . TRP A 1 60 ? 5.758 14.872 40.992 1.00 14.37 ? 86 TRP A C 1 ATOM 454 O O . TRP A 1 60 ? 4.881 14.512 41.791 1.00 14.07 ? 86 TRP A O 1 ATOM 455 C CB . TRP A 1 60 ? 4.809 16.494 39.352 1.00 14.33 ? 86 TRP A CB 1 ATOM 456 C CG . TRP A 1 60 ? 4.993 17.791 38.616 1.00 16.93 ? 86 TRP A CG 1 ATOM 457 C CD1 . TRP A 1 60 ? 5.464 17.950 37.342 1.00 19.91 ? 86 TRP A CD1 1 ATOM 458 C CD2 . TRP A 1 60 ? 4.732 19.112 39.117 1.00 17.06 ? 86 TRP A CD2 1 ATOM 459 N NE1 . TRP A 1 60 ? 5.506 19.287 37.021 1.00 18.96 ? 86 TRP A NE1 1 ATOM 460 C CE2 . TRP A 1 60 ? 5.068 20.019 38.096 1.00 20.75 ? 86 TRP A CE2 1 ATOM 461 C CE3 . TRP A 1 60 ? 4.257 19.612 40.336 1.00 13.18 ? 86 TRP A CE3 1 ATOM 462 C CZ2 . TRP A 1 60 ? 4.936 21.400 38.260 1.00 18.08 ? 86 TRP A CZ2 1 ATOM 463 C CZ3 . TRP A 1 60 ? 4.140 20.965 40.498 1.00 13.74 ? 86 TRP A CZ3 1 ATOM 464 C CH2 . TRP A 1 60 ? 4.479 21.849 39.469 1.00 18.46 ? 86 TRP A CH2 1 ATOM 465 N N . ASN A 1 61 ? 6.679 14.049 40.499 1.00 13.10 ? 87 ASN A N 1 ATOM 466 C CA . ASN A 1 61 ? 6.716 12.638 40.839 1.00 15.65 ? 87 ASN A CA 1 ATOM 467 C C . ASN A 1 61 ? 7.686 12.280 41.958 1.00 16.82 ? 87 ASN A C 1 ATOM 468 O O . ASN A 1 61 ? 8.271 11.208 41.954 1.00 17.65 ? 87 ASN A O 1 ATOM 469 C CB . ASN A 1 61 ? 7.000 11.807 39.584 1.00 16.99 ? 87 ASN A CB 1 ATOM 470 C CG . ASN A 1 61 ? 6.057 12.157 38.453 1.00 25.09 ? 87 ASN A CG 1 ATOM 471 O OD1 . ASN A 1 61 ? 4.850 11.996 38.578 1.00 24.81 ? 87 ASN A OD1 1 ATOM 472 N ND2 . ASN A 1 61 ? 6.600 12.674 37.356 1.00 34.85 ? 87 ASN A ND2 1 ATOM 473 N N . HIS A 1 62 ? 7.822 13.175 42.931 1.00 14.27 ? 88 HIS A N 1 ATOM 474 C CA . HIS A 1 62 ? 8.748 12.950 44.032 1.00 12.85 ? 88 HIS A CA 1 ATOM 475 C C . HIS A 1 62 ? 8.360 11.751 44.900 1.00 13.10 ? 88 HIS A C 1 ATOM 476 O O . HIS A 1 62 ? 9.235 11.145 45.534 1.00 16.39 ? 88 HIS A O 1 ATOM 477 C CB . HIS A 1 62 ? 8.876 14.210 44.891 1.00 12.20 ? 88 HIS A CB 1 ATOM 478 C CG . HIS A 1 62 ? 7.565 14.828 45.270 1.00 11.26 ? 88 HIS A CG 1 ATOM 479 N ND1 . HIS A 1 62 ? 6.960 15.827 44.529 1.00 11.28 ? 88 HIS A ND1 1 ATOM 480 C CD2 . HIS A 1 62 ? 6.752 14.614 46.331 1.00 11.67 ? 88 HIS A CD2 1 ATOM 481 C CE1 . HIS A 1 62 ? 5.836 16.192 45.113 1.00 14.18 ? 88 HIS A CE1 1 ATOM 482 N NE2 . HIS A 1 62 ? 5.693 15.477 46.223 1.00 13.20 ? 88 HIS A NE2 1 ATOM 483 N N . CYS A 1 63 ? 7.077 11.400 44.928 1.00 13.48 ? 89 CYS A N 1 ATOM 484 C CA . CYS A 1 63 ? 6.638 10.204 45.644 1.00 12.69 ? 89 CYS A CA 1 ATOM 485 C C . CYS A 1 63 ? 6.026 9.147 44.729 1.00 20.49 ? 89 CYS A C 1 ATOM 486 O O . CYS A 1 63 ? 5.079 8.458 45.118 1.00 32.44 ? 89 CYS A O 1 ATOM 487 C CB . CYS A 1 63 ? 5.640 10.567 46.750 1.00 15.45 ? 89 CYS A CB 1 ATOM 488 S SG . CYS A 1 63 ? 6.446 11.314 48.199 1.00 15.85 ? 89 CYS A SG 1 ATOM 489 N N . GLY A 1 64 ? 6.577 8.998 43.530 1.00 24.09 ? 90 GLY A N 1 ATOM 490 C CA . GLY A 1 64 ? 6.060 8.020 42.586 1.00 26.50 ? 90 GLY A CA 1 ATOM 491 C C . GLY A 1 64 ? 5.247 8.769 41.548 1.00 22.62 ? 90 GLY A C 1 ATOM 492 O O . GLY A 1 64 ? 5.178 10.000 41.586 1.00 23.62 ? 90 GLY A O 1 ATOM 493 N N . GLU A 1 65 ? 4.600 8.041 40.641 1.00 24.86 ? 91 GLU A N 1 ATOM 494 C CA . GLU A 1 65 ? 3.845 8.678 39.560 1.00 24.44 ? 91 GLU A CA 1 ATOM 495 C C . GLU A 1 65 ? 2.671 9.498 40.105 1.00 21.20 ? 91 GLU A C 1 ATOM 496 O O . GLU A 1 65 ? 1.783 8.963 40.769 1.00 25.63 ? 91 GLU A O 1 ATOM 497 C CB . GLU A 1 65 ? 3.325 7.606 38.591 1.00 29.96 ? 91 GLU A CB 1 ATOM 498 C CG . GLU A 1 65 ? 2.817 8.146 37.252 1.00 37.72 ? 91 GLU A CG 1 ATOM 499 C CD . GLU A 1 65 ? 2.272 7.050 36.336 1.00 45.36 ? 91 GLU A CD 1 ATOM 500 O OE1 . GLU A 1 65 ? 2.749 5.894 36.420 1.00 47.19 ? 91 GLU A OE1 1 ATOM 501 O OE2 . GLU A 1 65 ? 1.364 7.349 35.531 1.00 47.45 ? 91 GLU A OE2 1 ATOM 502 N N . MET A 1 66 ? 2.683 10.798 39.838 1.00 16.73 ? 92 MET A N 1 ATOM 503 C CA . MET A 1 66 ? 1.530 11.620 40.146 1.00 15.33 ? 92 MET A CA 1 ATOM 504 C C . MET A 1 66 ? 0.464 11.286 39.110 1.00 19.04 ? 92 MET A C 1 ATOM 505 O O . MET A 1 66 ? 0.779 11.126 37.930 1.00 21.80 ? 92 MET A O 1 ATOM 506 C CB . MET A 1 66 ? 1.906 13.097 40.091 1.00 13.07 ? 92 MET A CB 1 ATOM 507 C CG . MET A 1 66 ? 0.688 14.015 40.255 1.00 11.69 ? 92 MET A CG 1 ATOM 508 S SD . MET A 1 66 ? 1.149 15.759 40.243 1.00 15.93 ? 92 MET A SD 1 ATOM 509 C CE . MET A 1 66 ? 1.852 15.985 41.875 1.00 14.51 ? 92 MET A CE 1 ATOM 510 N N . ALA A 1 67 ? -0.788 11.145 39.544 1.00 11.55 ? 93 ALA A N 1 ATOM 511 C CA . ALA A 1 67 ? -1.866 10.823 38.619 1.00 11.94 ? 93 ALA A CA 1 ATOM 512 C C . ALA A 1 67 ? -1.996 11.974 37.632 1.00 16.75 ? 93 ALA A C 1 ATOM 513 O O . ALA A 1 67 ? -1.830 13.133 38.015 1.00 14.52 ? 93 ALA A O 1 ATOM 514 C CB . ALA A 1 67 ? -3.180 10.601 39.366 1.00 13.95 ? 93 ALA A CB 1 ATOM 515 N N . PRO A 1 68 ? -2.259 11.653 36.355 1.00 12.39 ? 94 PRO A N 1 ATOM 516 C CA . PRO A 1 68 ? -2.341 12.687 35.325 1.00 12.45 ? 94 PRO A CA 1 ATOM 517 C C . PRO A 1 68 ? -3.366 13.762 35.674 1.00 12.00 ? 94 PRO A C 1 ATOM 518 O O . PRO A 1 68 ? -3.132 14.918 35.352 1.00 12.32 ? 94 PRO A O 1 ATOM 519 C CB . PRO A 1 68 ? -2.767 11.896 34.084 1.00 14.64 ? 94 PRO A CB 1 ATOM 520 C CG . PRO A 1 68 ? -2.140 10.545 34.299 1.00 17.14 ? 94 PRO A CG 1 ATOM 521 C CD . PRO A 1 68 ? -2.316 10.295 35.779 1.00 13.64 ? 94 PRO A CD 1 ATOM 522 N N . ALA A 1 69 ? -4.474 13.401 36.316 1.00 11.84 ? 95 ALA A N 1 ATOM 523 C CA . ALA A 1 69 ? -5.475 14.417 36.658 1.00 12.71 ? 95 ALA A CA 1 ATOM 524 C C . ALA A 1 69 ? -4.959 15.414 37.684 1.00 15.46 ? 95 ALA A C 1 ATOM 525 O O . ALA A 1 69 ? -5.332 16.590 37.668 1.00 15.71 ? 95 ALA A O 1 ATOM 526 C CB . ALA A 1 69 ? -6.755 13.789 37.139 1.00 13.30 ? 95 ALA A CB 1 ATOM 527 N N . CYS A 1 70 ? -4.109 14.938 38.581 1.00 11.90 ? 96 CYS A N 1 ATOM 528 C CA . CYS A 1 70 ? -3.497 15.785 39.592 1.00 9.92 ? 96 CYS A CA 1 ATOM 529 C C . CYS A 1 70 ? -2.453 16.668 38.911 1.00 12.17 ? 96 CYS A C 1 ATOM 530 O O . CYS A 1 70 ? -2.378 17.876 39.160 1.00 12.66 ? 96 CYS A O 1 ATOM 531 C CB . CYS A 1 70 ? -2.838 14.889 40.644 1.00 10.74 ? 96 CYS A CB 1 ATOM 532 S SG . CYS A 1 70 ? -2.140 15.791 42.028 1.00 12.61 ? 96 CYS A SG 1 ATOM 533 N N . LYS A 1 71 ? -1.652 16.070 38.031 1.00 12.63 ? 97 LYS A N 1 ATOM 534 C CA . LYS A 1 71 ? -0.620 16.838 37.344 1.00 11.39 ? 97 LYS A CA 1 ATOM 535 C C . LYS A 1 71 ? -1.219 17.993 36.557 1.00 12.84 ? 97 LYS A C 1 ATOM 536 O O . LYS A 1 71 ? -0.667 19.081 36.543 1.00 12.32 ? 97 LYS A O 1 ATOM 537 C CB . LYS A 1 71 ? 0.182 15.947 36.399 1.00 12.02 ? 97 LYS A CB 1 ATOM 538 C CG . LYS A 1 71 ? 1.331 16.692 35.743 1.00 13.03 ? 97 LYS A CG 1 ATOM 539 C CD . LYS A 1 71 ? 2.109 15.742 34.864 1.00 17.55 ? 97 LYS A CD 1 ATOM 540 C CE . LYS A 1 71 ? 3.217 16.492 34.122 1.00 21.15 ? 97 LYS A CE 1 ATOM 541 N NZ . LYS A 1 71 ? 3.901 15.606 33.137 1.00 23.72 ? 97 LYS A NZ 1 ATOM 542 N N . ARG A 1 72 ? -2.352 17.757 35.905 1.00 11.02 ? 98 ARG A N 1 ATOM 543 C CA . ARG A 1 72 ? -2.999 18.812 35.135 1.00 10.47 ? 98 ARG A CA 1 ATOM 544 C C . ARG A 1 72 ? -3.252 20.040 35.995 1.00 10.70 ? 98 ARG A C 1 ATOM 545 O O . ARG A 1 72 ? -2.993 21.165 35.556 1.00 11.08 ? 98 ARG A O 1 ATOM 546 C CB . ARG A 1 72 ? -4.299 18.312 34.515 1.00 12.87 ? 98 ARG A CB 1 ATOM 547 C CG . ARG A 1 72 ? -4.935 19.303 33.561 1.00 16.90 ? 98 ARG A CG 1 ATOM 548 C CD . ARG A 1 72 ? -6.225 18.721 32.974 1.00 24.27 ? 98 ARG A CD 1 ATOM 549 N NE . ARG A 1 72 ? -7.254 18.692 34.005 1.00 32.69 ? 98 ARG A NE 1 ATOM 550 C CZ . ARG A 1 72 ? -8.133 19.670 34.205 1.00 27.84 ? 98 ARG A CZ 1 ATOM 551 N NH1 . ARG A 1 72 ? -8.136 20.740 33.417 1.00 29.49 ? 98 ARG A NH1 1 ATOM 552 N NH2 . ARG A 1 72 ? -9.025 19.569 35.179 1.00 32.74 ? 98 ARG A NH2 1 ATOM 553 N N . HIS A 1 73 ? -3.737 19.845 37.216 1.00 11.22 ? 99 HIS A N 1 ATOM 554 C CA . HIS A 1 73 ? -3.917 20.992 38.117 1.00 12.71 ? 99 HIS A CA 1 ATOM 555 C C . HIS A 1 73 ? -2.621 21.704 38.464 1.00 13.43 ? 99 HIS A C 1 ATOM 556 O O . HIS A 1 73 ? -2.584 22.934 38.576 1.00 12.59 ? 99 HIS A O 1 ATOM 557 C CB . HIS A 1 73 ? -4.610 20.569 39.409 1.00 11.96 ? 99 HIS A CB 1 ATOM 558 C CG . HIS A 1 73 ? -6.030 20.162 39.216 1.00 12.72 ? 99 HIS A CG 1 ATOM 559 N ND1 . HIS A 1 73 ? -7.065 21.075 39.156 1.00 16.43 ? 99 HIS A ND1 1 ATOM 560 C CD2 . HIS A 1 73 ? -6.585 18.940 39.074 1.00 15.34 ? 99 HIS A CD2 1 ATOM 561 C CE1 . HIS A 1 73 ? -8.199 20.420 38.978 1.00 16.12 ? 99 HIS A CE1 1 ATOM 562 N NE2 . HIS A 1 73 ? -7.940 19.127 38.924 1.00 15.81 ? 99 HIS A NE2 1 ATOM 563 N N . PHE A 1 74 ? -1.565 20.931 38.672 1.00 12.13 ? 100 PHE A N 1 ATOM 564 C CA . PHE A 1 74 ? -0.270 21.521 38.977 1.00 10.55 ? 100 PHE A CA 1 ATOM 565 C C . PHE A 1 74 ? 0.307 22.306 37.808 1.00 11.49 ? 100 PHE A C 1 ATOM 566 O O . PHE A 1 74 ? 0.951 23.337 38.003 1.00 11.56 ? 100 PHE A O 1 ATOM 567 C CB . PHE A 1 74 ? 0.679 20.476 39.543 1.00 9.87 ? 100 PHE A CB 1 ATOM 568 C CG . PHE A 1 74 ? 0.458 20.227 41.002 1.00 11.00 ? 100 PHE A CG 1 ATOM 569 C CD1 . PHE A 1 74 ? 0.900 21.160 41.944 1.00 11.05 ? 100 PHE A CD1 1 ATOM 570 C CD2 . PHE A 1 74 ? -0.200 19.092 41.444 1.00 12.38 ? 100 PHE A CD2 1 ATOM 571 C CE1 . PHE A 1 74 ? 0.688 20.958 43.288 1.00 10.28 ? 100 PHE A CE1 1 ATOM 572 C CE2 . PHE A 1 74 ? -0.412 18.884 42.795 1.00 11.22 ? 100 PHE A CE2 1 ATOM 573 C CZ . PHE A 1 74 ? 0.012 19.816 43.716 1.00 8.61 ? 100 PHE A CZ 1 ATOM 574 N N . ILE A 1 75 ? 0.009 21.867 36.589 1.00 10.84 ? 101 ILE A N 1 ATOM 575 C CA . ILE A 1 75 ? 0.394 22.636 35.415 1.00 9.49 ? 101 ILE A CA 1 ATOM 576 C C . ILE A 1 75 ? -0.379 23.963 35.379 1.00 15.28 ? 101 ILE A C 1 ATOM 577 O O . ILE A 1 75 ? 0.195 25.016 35.104 1.00 11.72 ? 101 ILE A O 1 ATOM 578 C CB . ILE A 1 75 ? 0.193 21.849 34.103 1.00 12.62 ? 101 ILE A CB 1 ATOM 579 C CG1 . ILE A 1 75 ? 1.095 20.602 34.069 1.00 16.07 ? 101 ILE A CG1 1 ATOM 580 C CG2 . ILE A 1 75 ? 0.434 22.760 32.891 1.00 15.65 ? 101 ILE A CG2 1 ATOM 581 C CD1 . ILE A 1 75 ? 2.581 20.875 34.298 1.00 21.42 ? 101 ILE A CD1 1 ATOM 582 N N . GLN A 1 76 ? -1.673 23.912 35.678 1.00 11.36 ? 102 GLN A N 1 ATOM 583 C CA . GLN A 1 76 ? -2.499 25.122 35.669 1.00 13.64 ? 102 GLN A CA 1 ATOM 584 C C . GLN A 1 76 ? -1.979 26.096 36.710 1.00 13.18 ? 102 GLN A C 1 ATOM 585 O O . GLN A 1 76 ? -1.827 27.286 36.432 1.00 11.79 ? 102 GLN A O 1 ATOM 586 C CB . GLN A 1 76 ? -3.984 24.797 35.921 1.00 10.87 ? 102 GLN A CB 1 ATOM 587 C CG . GLN A 1 76 ? -4.619 23.928 34.828 1.00 13.53 ? 102 GLN A CG 1 ATOM 588 C CD . GLN A 1 76 ? -6.108 23.741 35.025 1.00 19.95 ? 102 GLN A CD 1 ATOM 589 O OE1 . GLN A 1 76 ? -6.618 23.872 36.138 1.00 26.57 ? 102 GLN A OE1 1 ATOM 590 N NE2 . GLN A 1 76 ? -6.814 23.457 33.943 1.00 22.23 ? 102 GLN A NE2 1 ATOM 591 N N . ASP A 1 77 ? -1.680 25.568 37.894 1.00 11.17 ? 103 ASP A N 1 ATOM 592 C CA . ASP A 1 77 ? -1.149 26.333 39.032 1.00 10.73 ? 103 ASP A CA 1 ATOM 593 C C . ASP A 1 77 ? 0.149 27.043 38.654 1.00 11.83 ? 103 ASP A C 1 ATOM 594 O O . ASP A 1 77 ? 0.301 28.245 38.886 1.00 11.98 ? 103 ASP A O 1 ATOM 595 C CB . ASP A 1 77 ? -0.930 25.322 40.171 1.00 12.87 ? 103 ASP A CB 1 ATOM 596 C CG . ASP A 1 77 ? -0.232 25.897 41.392 1.00 14.86 ? 103 ASP A CG 1 ATOM 597 O OD1 . ASP A 1 77 ? -0.619 26.979 41.862 1.00 16.33 ? 103 ASP A OD1 1 ATOM 598 O OD2 . ASP A 1 77 ? 0.674 25.209 41.924 1.00 17.27 ? 103 ASP A OD2 1 ATOM 599 N N . THR A 1 78 ? 1.069 26.292 38.053 1.00 12.21 ? 104 THR A N 1 ATOM 600 C CA . THR A 1 78 ? 2.364 26.803 37.634 1.00 11.39 ? 104 THR A CA 1 ATOM 601 C C . THR A 1 78 ? 2.187 27.879 36.573 1.00 12.54 ? 104 THR A C 1 ATOM 602 O O . THR A 1 78 ? 2.821 28.942 36.628 1.00 11.33 ? 104 THR A O 1 ATOM 603 C CB . THR A 1 78 ? 3.219 25.657 37.059 1.00 11.49 ? 104 THR A CB 1 ATOM 604 O OG1 . THR A 1 78 ? 3.365 24.640 38.052 1.00 17.59 ? 104 THR A OG1 1 ATOM 605 C CG2 . THR A 1 78 ? 4.603 26.144 36.667 1.00 11.05 ? 104 THR A CG2 1 ATOM 606 N N . CYS A 1 79 ? 1.338 27.596 35.592 1.00 10.43 ? 105 CYS A N 1 ATOM 607 C CA . CYS A 1 79 ? 1.047 28.571 34.537 1.00 11.73 ? 105 CYS A CA 1 ATOM 608 C C . CYS A 1 79 ? 0.452 29.876 35.077 1.00 10.93 ? 105 CYS A C 1 ATOM 609 O O . CYS A 1 79 ? 0.842 30.947 34.632 1.00 11.24 ? 105 CYS A O 1 ATOM 610 C CB . CYS A 1 79 ? 0.115 27.972 33.471 1.00 13.26 ? 105 CYS A CB 1 ATOM 611 S SG . CYS A 1 79 ? 0.849 26.724 32.395 1.00 13.46 ? 105 CYS A SG 1 ATOM 612 N N . LEU A 1 80 ? -0.495 29.785 36.012 1.00 9.23 ? 106 LEU A N 1 ATOM 613 C CA . LEU A 1 80 ? -1.079 30.994 36.602 1.00 10.03 ? 106 LEU A CA 1 ATOM 614 C C . LEU A 1 80 ? 0.005 31.818 37.300 1.00 11.05 ? 106 LEU A C 1 ATOM 615 O O . LEU A 1 80 ? 0.145 33.005 37.044 1.00 11.17 ? 106 LEU A O 1 ATOM 616 C CB . LEU A 1 80 ? -2.191 30.650 37.587 1.00 9.69 ? 106 LEU A CB 1 ATOM 617 C CG . LEU A 1 80 ? -2.868 31.862 38.247 1.00 10.36 ? 106 LEU A CG 1 ATOM 618 C CD1 . LEU A 1 80 ? -3.803 32.577 37.266 1.00 10.32 ? 106 LEU A CD1 1 ATOM 619 C CD2 . LEU A 1 80 ? -3.604 31.422 39.529 1.00 14.51 ? 106 LEU A CD2 1 ATOM 620 N N . TYR A 1 81 ? 0.783 31.171 38.159 1.00 10.09 ? 107 TYR A N 1 ATOM 621 C CA . TYR A 1 81 ? 1.840 31.868 38.882 1.00 10.55 ? 107 TYR A CA 1 ATOM 622 C C . TYR A 1 81 ? 2.827 32.539 37.916 1.00 11.67 ? 107 TYR A C 1 ATOM 623 O O . TYR A 1 81 ? 3.192 33.703 38.091 1.00 12.52 ? 107 TYR A O 1 ATOM 624 C CB . TYR A 1 81 ? 2.573 30.899 39.828 1.00 11.41 ? 107 TYR A CB 1 ATOM 625 C CG . TYR A 1 81 ? 3.787 31.519 40.484 1.00 11.88 ? 107 TYR A CG 1 ATOM 626 C CD1 . TYR A 1 81 ? 3.677 32.219 41.683 1.00 15.15 ? 107 TYR A CD1 1 ATOM 627 C CD2 . TYR A 1 81 ? 5.045 31.442 39.896 1.00 11.77 ? 107 TYR A CD2 1 ATOM 628 C CE1 . TYR A 1 81 ? 4.796 32.807 42.276 1.00 10.45 ? 107 TYR A CE1 1 ATOM 629 C CE2 . TYR A 1 81 ? 6.159 32.035 40.482 1.00 10.98 ? 107 TYR A CE2 1 ATOM 630 C CZ . TYR A 1 81 ? 6.023 32.721 41.673 1.00 9.29 ? 107 TYR A CZ 1 ATOM 631 O OH . TYR A 1 81 ? 7.130 33.317 42.258 1.00 12.26 ? 107 TYR A OH 1 ATOM 632 N N . GLU A 1 82 ? 3.261 31.814 36.890 1.00 9.09 ? 108 GLU A N 1 ATOM 633 C CA . GLU A 1 82 ? 4.339 32.319 36.037 1.00 10.15 ? 108 GLU A CA 1 ATOM 634 C C . GLU A 1 82 ? 3.853 33.264 34.955 1.00 12.24 ? 108 GLU A C 1 ATOM 635 O O . GLU A 1 82 ? 4.619 34.098 34.477 1.00 13.68 ? 108 GLU A O 1 ATOM 636 C CB . GLU A 1 82 ? 5.127 31.153 35.439 1.00 10.49 ? 108 GLU A CB 1 ATOM 637 C CG . GLU A 1 82 ? 5.772 30.324 36.543 1.00 14.00 ? 108 GLU A CG 1 ATOM 638 C CD . GLU A 1 82 ? 6.541 29.135 36.057 1.00 17.36 ? 108 GLU A CD 1 ATOM 639 O OE1 . GLU A 1 82 ? 6.574 28.885 34.832 1.00 17.77 ? 108 GLU A OE1 1 ATOM 640 O OE2 . GLU A 1 82 ? 7.116 28.450 36.929 1.00 14.80 ? 108 GLU A OE2 1 ATOM 641 N N . CYS A 1 83 ? 2.578 33.169 34.584 1.00 11.10 ? 109 CYS A N 1 ATOM 642 C CA . CYS A 1 83 ? 2.111 33.923 33.422 1.00 10.45 ? 109 CYS A CA 1 ATOM 643 C C . CYS A 1 83 ? 1.027 34.957 33.692 1.00 11.89 ? 109 CYS A C 1 ATOM 644 O O . CYS A 1 83 ? 0.826 35.855 32.870 1.00 12.73 ? 109 CYS A O 1 ATOM 645 C CB . CYS A 1 83 ? 1.601 32.974 32.335 1.00 12.82 ? 109 CYS A CB 1 ATOM 646 S SG . CYS A 1 83 ? 2.785 31.742 31.757 1.00 13.42 ? 109 CYS A SG 1 ATOM 647 N N . SER A 1 84 ? 0.312 34.852 34.809 1.00 11.84 ? 110 SER A N 1 ATOM 648 C CA . SER A 1 84 ? -0.813 35.776 35.001 1.00 9.32 ? 110 SER A CA 1 ATOM 649 C C . SER A 1 84 ? -0.389 37.233 35.179 1.00 10.80 ? 110 SER A C 1 ATOM 650 O O . SER A 1 84 ? 0.452 37.533 36.039 1.00 13.42 ? 110 SER A O 1 ATOM 651 C CB . SER A 1 84 ? -1.644 35.411 36.218 1.00 12.43 ? 110 SER A CB 1 ATOM 652 O OG . SER A 1 84 ? -2.613 36.442 36.429 1.00 11.36 ? 110 SER A OG 1 ATOM 653 N N . PRO A 1 85 ? -0.979 38.155 34.387 1.00 10.58 ? 111 PRO A N 1 ATOM 654 C CA . PRO A 1 85 ? -0.722 39.573 34.648 1.00 10.89 ? 111 PRO A CA 1 ATOM 655 C C . PRO A 1 85 ? -1.799 40.202 35.546 1.00 11.74 ? 111 PRO A C 1 ATOM 656 O O . PRO A 1 85 ? -1.918 41.452 35.647 1.00 13.11 ? 111 PRO A O 1 ATOM 657 C CB . PRO A 1 85 ? -0.794 40.175 33.243 1.00 11.79 ? 111 PRO A CB 1 ATOM 658 C CG . PRO A 1 85 ? -1.938 39.383 32.605 1.00 13.28 ? 111 PRO A CG 1 ATOM 659 C CD . PRO A 1 85 ? -1.832 37.968 33.195 1.00 13.35 ? 111 PRO A CD 1 ATOM 660 N N . ASN A 1 86 ? -2.569 39.345 36.207 1.00 11.40 ? 112 ASN A N 1 ATOM 661 C CA . ASN A 1 86 ? -3.699 39.812 37.015 1.00 9.69 ? 112 ASN A CA 1 ATOM 662 C C . ASN A 1 86 ? -3.558 39.467 38.503 1.00 9.08 ? 112 ASN A C 1 ATOM 663 O O . ASN A 1 86 ? -4.568 39.393 39.211 1.00 14.06 ? 112 ASN A O 1 ATOM 664 C CB . ASN A 1 86 ? -5.002 39.247 36.444 1.00 10.80 ? 112 ASN A CB 1 ATOM 665 C CG . ASN A 1 86 ? -5.240 39.678 35.011 1.00 14.19 ? 112 ASN A CG 1 ATOM 666 O OD1 . ASN A 1 86 ? -5.431 38.845 34.110 1.00 20.10 ? 112 ASN A OD1 1 ATOM 667 N ND2 . ASN A 1 86 ? -5.241 40.976 34.785 1.00 11.57 ? 112 ASN A ND2 1 ATOM 668 N N . LEU A 1 87 ? -2.321 39.266 38.979 1.00 10.35 ? 113 LEU A N 1 ATOM 669 C CA . LEU A 1 87 ? -2.071 38.982 40.388 1.00 11.34 ? 113 LEU A CA 1 ATOM 670 C C . LEU A 1 87 ? -1.519 40.194 41.148 1.00 12.61 ? 113 LEU A C 1 ATOM 671 O O . LEU A 1 87 ? -1.240 40.106 42.351 1.00 12.46 ? 113 LEU A O 1 ATOM 672 C CB . LEU A 1 87 ? -1.126 37.784 40.555 1.00 12.64 ? 113 LEU A CB 1 ATOM 673 C CG . LEU A 1 87 ? -1.582 36.510 39.848 1.00 14.06 ? 113 LEU A CG 1 ATOM 674 C CD1 . LEU A 1 87 ? -0.561 35.382 40.058 1.00 15.31 ? 113 LEU A CD1 1 ATOM 675 C CD2 . LEU A 1 87 ? -2.955 36.125 40.364 1.00 12.36 ? 113 LEU A CD2 1 ATOM 676 N N . GLY A 1 88 ? -1.387 41.325 40.456 1.00 12.35 ? 114 GLY A N 1 ATOM 677 C CA . GLY A 1 88 ? -0.840 42.541 41.050 1.00 14.86 ? 114 GLY A CA 1 ATOM 678 C C . GLY A 1 88 ? -1.369 42.934 42.418 1.00 13.28 ? 114 GLY A C 1 ATOM 679 O O . GLY A 1 88 ? -0.578 43.320 43.290 1.00 15.51 ? 114 GLY A O 1 ATOM 680 N N . PRO A 1 89 ? -2.694 42.845 42.625 1.00 12.61 ? 115 PRO A N 1 ATOM 681 C CA . PRO A 1 89 ? -3.224 43.224 43.940 1.00 11.40 ? 115 PRO A CA 1 ATOM 682 C C . PRO A 1 89 ? -2.695 42.382 45.101 1.00 12.18 ? 115 PRO A C 1 ATOM 683 O O . PRO A 1 89 ? -2.843 42.835 46.245 1.00 15.09 ? 115 PRO A O 1 ATOM 684 C CB . PRO A 1 89 ? -4.736 43.035 43.777 1.00 12.74 ? 115 PRO A CB 1 ATOM 685 C CG . PRO A 1 89 ? -4.966 43.271 42.313 1.00 12.84 ? 115 PRO A CG 1 ATOM 686 C CD . PRO A 1 89 ? -3.768 42.685 41.625 1.00 13.32 ? 115 PRO A CD 1 ATOM 687 N N . TRP A 1 90 ? -2.077 41.225 44.823 1.00 9.99 ? 116 TRP A N 1 ATOM 688 C CA . TRP A 1 90 ? -1.621 40.308 45.877 1.00 10.50 ? 116 TRP A CA 1 ATOM 689 C C . TRP A 1 90 ? -0.109 40.177 45.952 1.00 9.62 ? 116 TRP A C 1 ATOM 690 O O . TRP A 1 90 ? 0.411 39.387 46.734 1.00 11.41 ? 116 TRP A O 1 ATOM 691 C CB . TRP A 1 90 ? -2.284 38.924 45.719 1.00 9.21 ? 116 TRP A CB 1 ATOM 692 C CG . TRP A 1 90 ? -3.770 39.048 45.778 1.00 10.79 ? 116 TRP A CG 1 ATOM 693 C CD1 . TRP A 1 90 ? -4.559 39.147 46.907 1.00 9.61 ? 116 TRP A CD1 1 ATOM 694 C CD2 . TRP A 1 90 ? -4.670 39.166 44.655 1.00 11.01 ? 116 TRP A CD2 1 ATOM 695 N NE1 . TRP A 1 90 ? -5.879 39.317 46.541 1.00 12.37 ? 116 TRP A NE1 1 ATOM 696 C CE2 . TRP A 1 90 ? -5.971 39.323 45.176 1.00 12.49 ? 116 TRP A CE2 1 ATOM 697 C CE3 . TRP A 1 90 ? -4.491 39.152 43.270 1.00 12.78 ? 116 TRP A CE3 1 ATOM 698 C CZ2 . TRP A 1 90 ? -7.092 39.462 44.348 1.00 11.21 ? 116 TRP A CZ2 1 ATOM 699 C CZ3 . TRP A 1 90 ? -5.609 39.284 42.455 1.00 12.17 ? 116 TRP A CZ3 1 ATOM 700 C CH2 . TRP A 1 90 ? -6.886 39.434 42.997 1.00 11.19 ? 116 TRP A CH2 1 ATOM 701 N N . ILE A 1 91 ? 0.590 40.968 45.155 1.00 11.46 ? 117 ILE A N 1 ATOM 702 C CA . ILE A 1 91 ? 2.034 40.904 45.123 1.00 11.24 ? 117 ILE A CA 1 ATOM 703 C C . ILE A 1 91 ? 2.599 41.558 46.381 1.00 14.09 ? 117 ILE A C 1 ATOM 704 O O . ILE A 1 91 ? 2.244 42.690 46.718 1.00 13.29 ? 117 ILE A O 1 ATOM 705 C CB . ILE A 1 91 ? 2.596 41.569 43.856 1.00 9.79 ? 117 ILE A CB 1 ATOM 706 C CG1 . ILE A 1 91 ? 2.219 40.701 42.648 1.00 13.68 ? 117 ILE A CG1 1 ATOM 707 C CG2 . ILE A 1 91 ? 4.114 41.732 43.962 1.00 12.89 ? 117 ILE A CG2 1 ATOM 708 C CD1 . ILE A 1 91 ? 2.772 41.210 41.330 1.00 16.73 ? 117 ILE A CD1 1 ATOM 709 N N . GLN A 1 92 ? 3.460 40.826 47.090 1.00 13.56 ? 118 GLN A N 1 ATOM 710 C CA . GLN A 1 92 ? 4.180 41.398 48.221 1.00 12.88 ? 118 GLN A CA 1 ATOM 711 C C . GLN A 1 92 ? 5.556 41.797 47.752 1.00 12.98 ? 118 GLN A C 1 ATOM 712 O O . GLN A 1 92 ? 6.454 40.956 47.624 1.00 15.15 ? 118 GLN A O 1 ATOM 713 C CB . GLN A 1 92 ? 4.308 40.429 49.394 1.00 16.51 ? 118 GLN A CB 1 ATOM 714 C CG . GLN A 1 92 ? 4.806 41.185 50.640 1.00 23.99 ? 118 GLN A CG 1 ATOM 715 C CD . GLN A 1 92 ? 5.050 40.282 51.802 1.00 30.20 ? 118 GLN A CD 1 ATOM 716 O OE1 . GLN A 1 92 ? 5.378 39.111 51.628 1.00 38.68 ? 118 GLN A OE1 1 ATOM 717 N NE2 . GLN A 1 92 ? 4.877 40.804 53.002 1.00 28.45 ? 118 GLN A NE2 1 ATOM 718 N N . GLN A 1 93 ? 5.742 43.078 47.495 1.00 17.46 ? 119 GLN A N 1 ATOM 719 C CA . GLN A 1 93 ? 6.979 43.472 46.850 1.00 21.49 ? 119 GLN A CA 1 ATOM 720 C C . GLN A 1 93 ? 8.226 43.401 47.736 1.00 21.19 ? 119 GLN A C 1 ATOM 721 O O . GLN A 1 93 ? 9.329 43.403 47.213 1.00 24.88 ? 119 GLN A O 1 ATOM 722 C CB . GLN A 1 93 ? 6.847 44.838 46.180 1.00 30.29 ? 119 GLN A CB 1 ATOM 723 C CG . GLN A 1 93 ? 6.233 45.913 47.039 1.00 37.52 ? 119 GLN A CG 1 ATOM 724 C CD . GLN A 1 93 ? 5.982 47.167 46.237 1.00 46.50 ? 119 GLN A CD 1 ATOM 725 O OE1 . GLN A 1 93 ? 5.192 47.157 45.293 1.00 48.51 ? 119 GLN A OE1 1 ATOM 726 N NE2 . GLN A 1 93 ? 6.673 48.249 46.585 1.00 47.86 ? 119 GLN A NE2 1 ATOM 727 N N . VAL A 1 94 ? 8.065 43.327 49.057 1.00 17.17 ? 120 VAL A N 1 ATOM 728 C CA . VAL A 1 94 ? 9.251 43.294 49.927 1.00 20.56 ? 120 VAL A CA 1 ATOM 729 C C . VAL A 1 94 ? 9.913 41.923 49.938 1.00 19.66 ? 120 VAL A C 1 ATOM 730 O O . VAL A 1 94 ? 11.064 41.796 50.374 1.00 23.34 ? 120 VAL A O 1 ATOM 731 C CB . VAL A 1 94 ? 8.969 43.684 51.403 1.00 19.55 ? 120 VAL A CB 1 ATOM 732 C CG1 . VAL A 1 94 ? 8.614 45.147 51.534 1.00 19.25 ? 120 VAL A CG1 1 ATOM 733 C CG2 . VAL A 1 94 ? 7.884 42.785 52.003 1.00 21.12 ? 120 VAL A CG2 1 ATOM 734 N N . ASP A 1 95 ? 9.187 40.908 49.475 1.00 17.23 ? 121 ASP A N 1 ATOM 735 C CA . ASP A 1 95 ? 9.694 39.546 49.511 1.00 20.46 ? 121 ASP A CA 1 ATOM 736 C C . ASP A 1 95 ? 10.261 39.158 48.149 1.00 19.90 ? 121 ASP A C 1 ATOM 737 O O . ASP A 1 95 ? 9.516 38.985 47.178 1.00 19.03 ? 121 ASP A O 1 ATOM 738 C CB . ASP A 1 95 ? 8.583 38.573 49.920 1.00 21.67 ? 121 ASP A CB 1 ATOM 739 C CG . ASP A 1 95 ? 9.113 37.191 50.244 1.00 26.67 ? 121 ASP A CG 1 ATOM 740 O OD1 . ASP A 1 95 ? 10.189 36.819 49.730 1.00 25.09 ? 121 ASP A OD1 1 ATOM 741 O OD2 . ASP A 1 95 ? 8.459 36.471 51.021 1.00 25.89 ? 121 ASP A OD2 1 ATOM 742 N N . GLN A 1 96 ? 11.580 38.997 48.100 1.00 25.04 ? 122 GLN A N 1 ATOM 743 C CA . GLN A 1 96 ? 12.270 38.679 46.859 1.00 26.47 ? 122 GLN A CA 1 ATOM 744 C C . GLN A 1 96 ? 12.848 37.273 46.913 1.00 24.39 ? 122 GLN A C 1 ATOM 745 O O . GLN A 1 96 ? 13.818 36.968 46.222 1.00 29.30 ? 122 GLN A O 1 ATOM 746 C CB . GLN A 1 96 ? 13.348 39.736 46.588 1.00 30.17 ? 122 GLN A CB 1 ATOM 747 C CG . GLN A 1 96 ? 12.768 41.142 46.519 1.00 34.03 ? 122 GLN A CG 1 ATOM 748 C CD . GLN A 1 96 ? 13.808 42.216 46.270 1.00 39.35 ? 122 GLN A CD 1 ATOM 749 O OE1 . GLN A 1 96 ? 14.959 42.105 46.697 1.00 39.63 ? 122 GLN A OE1 1 ATOM 750 N NE2 . GLN A 1 96 ? 13.400 43.274 45.575 1.00 39.23 ? 122 GLN A NE2 1 ATOM 751 N N . SER A 1 97 ? 12.225 36.408 47.713 1.00 21.62 ? 123 SER A N 1 ATOM 752 C CA . SER A 1 97 ? 12.753 35.059 47.936 1.00 24.22 ? 123 SER A CA 1 ATOM 753 C C . SER A 1 97 ? 12.117 33.989 47.053 1.00 25.74 ? 123 SER A C 1 ATOM 754 O O . SER A 1 97 ? 12.518 32.826 47.102 1.00 29.69 ? 123 SER A O 1 ATOM 755 C CB . SER A 1 97 ? 12.633 34.652 49.407 1.00 24.37 ? 123 SER A CB 1 ATOM 756 O OG . SER A 1 97 ? 11.286 34.419 49.774 1.00 28.82 ? 123 SER A OG 1 ATOM 757 N N . TRP A 1 98 ? 11.131 34.357 46.244 1.00 18.11 ? 124 TRP A N 1 ATOM 758 C CA . TRP A 1 98 ? 10.526 33.384 45.333 1.00 19.16 ? 124 TRP A CA 1 ATOM 759 C C . TRP A 1 98 ? 11.156 33.490 43.945 1.00 16.05 ? 124 TRP A C 1 ATOM 760 O O . TRP A 1 98 ? 11.903 34.431 43.672 1.00 17.46 ? 124 TRP A O 1 ATOM 761 C CB . TRP A 1 98 ? 9.002 33.538 45.289 1.00 17.88 ? 124 TRP A CB 1 ATOM 762 C CG . TRP A 1 98 ? 8.375 33.067 46.565 1.00 16.88 ? 124 TRP A CG 1 ATOM 763 C CD1 . TRP A 1 98 ? 8.668 33.501 47.828 1.00 18.94 ? 124 TRP A CD1 1 ATOM 764 C CD2 . TRP A 1 98 ? 7.357 32.063 46.711 1.00 13.34 ? 124 TRP A CD2 1 ATOM 765 N NE1 . TRP A 1 98 ? 7.890 32.826 48.747 1.00 19.72 ? 124 TRP A NE1 1 ATOM 766 C CE2 . TRP A 1 98 ? 7.081 31.941 48.086 1.00 16.49 ? 124 TRP A CE2 1 ATOM 767 C CE3 . TRP A 1 98 ? 6.649 31.265 45.811 1.00 13.84 ? 124 TRP A CE3 1 ATOM 768 C CZ2 . TRP A 1 98 ? 6.135 31.038 48.584 1.00 15.78 ? 124 TRP A CZ2 1 ATOM 769 C CZ3 . TRP A 1 98 ? 5.707 30.357 46.312 1.00 16.22 ? 124 TRP A CZ3 1 ATOM 770 C CH2 . TRP A 1 98 ? 5.470 30.254 47.683 1.00 15.55 ? 124 TRP A CH2 1 ATOM 771 N N . ARG A 1 99 ? 10.856 32.527 43.070 1.00 18.14 ? 125 ARG A N 1 ATOM 772 C CA . ARG A 1 99 ? 11.517 32.515 41.774 1.00 16.42 ? 125 ARG A CA 1 ATOM 773 C C . ARG A 1 99 ? 11.080 33.735 40.974 1.00 16.69 ? 125 ARG A C 1 ATOM 774 O O . ARG A 1 99 ? 11.878 34.300 40.215 1.00 17.97 ? 125 ARG A O 1 ATOM 775 C CB . ARG A 1 99 ? 11.252 31.211 41.017 1.00 15.41 ? 125 ARG A CB 1 ATOM 776 C CG . ARG A 1 99 ? 9.811 30.945 40.614 1.00 14.66 ? 125 ARG A CG 1 ATOM 777 C CD . ARG A 1 99 ? 9.727 29.499 40.185 1.00 15.12 ? 125 ARG A CD 1 ATOM 778 N NE . ARG A 1 99 ? 8.435 29.125 39.636 1.00 14.74 ? 125 ARG A NE 1 ATOM 779 C CZ . ARG A 1 99 ? 7.384 28.770 40.363 1.00 15.38 ? 125 ARG A CZ 1 ATOM 780 N NH1 . ARG A 1 99 ? 7.449 28.774 41.689 1.00 18.64 ? 125 ARG A NH1 1 ATOM 781 N NH2 . ARG A 1 99 ? 6.261 28.422 39.764 1.00 16.77 ? 125 ARG A NH2 1 ATOM 782 N N . LYS A 1 100 ? 9.822 34.135 41.160 1.00 15.12 ? 126 LYS A N 1 ATOM 783 C CA . LYS A 1 100 ? 9.338 35.410 40.638 1.00 15.30 ? 126 LYS A CA 1 ATOM 784 C C . LYS A 1 100 ? 8.594 36.161 41.735 1.00 14.49 ? 126 LYS A C 1 ATOM 785 O O . LYS A 1 100 ? 9.174 36.434 42.787 1.00 16.36 ? 126 LYS A O 1 ATOM 786 C CB . LYS A 1 100 ? 8.509 35.206 39.362 1.00 16.52 ? 126 LYS A CB 1 ATOM 787 C CG . LYS A 1 100 ? 9.321 34.521 38.247 1.00 21.33 ? 126 LYS A CG 1 ATOM 788 C CD . LYS A 1 100 ? 8.948 35.013 36.862 1.00 25.93 ? 126 LYS A CD 1 ATOM 789 C CE . LYS A 1 100 ? 7.600 34.500 36.436 1.00 23.43 ? 126 LYS A CE 1 ATOM 790 N NZ . LYS A 1 100 ? 7.151 35.161 35.161 1.00 23.41 ? 126 LYS A NZ 1 ATOM 791 N N . GLU A 1 101 ? 7.339 36.515 41.501 1.00 13.47 ? 127 GLU A N 1 ATOM 792 C CA . GLU A 1 101 ? 6.599 37.284 42.498 1.00 13.95 ? 127 GLU A CA 1 ATOM 793 C C . GLU A 1 101 ? 6.355 36.475 43.777 1.00 12.47 ? 127 GLU A C 1 ATOM 794 O O . GLU A 1 101 ? 6.296 35.242 43.742 1.00 13.83 ? 127 GLU A O 1 ATOM 795 C CB . GLU A 1 101 ? 5.269 37.767 41.919 1.00 12.85 ? 127 GLU A CB 1 ATOM 796 C CG . GLU A 1 101 ? 4.189 36.694 41.818 1.00 16.47 ? 127 GLU A CG 1 ATOM 797 C CD . GLU A 1 101 ? 4.238 35.881 40.521 1.00 16.54 ? 127 GLU A CD 1 ATOM 798 O OE1 . GLU A 1 101 ? 5.234 35.954 39.768 1.00 15.60 ? 127 GLU A OE1 1 ATOM 799 O OE2 . GLU A 1 101 ? 3.247 35.170 40.246 1.00 13.84 ? 127 GLU A OE2 1 ATOM 800 N N . ARG A 1 102 ? 6.244 37.168 44.911 1.00 11.33 ? 128 ARG A N 1 ATOM 801 C CA . ARG A 1 102 ? 5.626 36.535 46.073 1.00 13.01 ? 128 ARG A CA 1 ATOM 802 C C . ARG A 1 102 ? 4.209 37.056 46.105 1.00 15.83 ? 128 ARG A C 1 ATOM 803 O O . ARG A 1 102 ? 4.008 38.274 46.173 1.00 14.05 ? 128 ARG A O 1 ATOM 804 C CB . ARG A 1 102 ? 6.368 36.929 47.352 1.00 15.70 ? 128 ARG A CB 1 ATOM 805 C CG . ARG A 1 102 ? 5.632 36.588 48.657 1.00 18.07 ? 128 ARG A CG 1 ATOM 806 C CD . ARG A 1 102 ? 5.223 35.137 48.726 1.00 22.51 ? 128 ARG A CD 1 ATOM 807 N NE . ARG A 1 102 ? 5.259 34.619 50.093 1.00 21.64 ? 128 ARG A NE 1 ATOM 808 C CZ . ARG A 1 102 ? 4.426 33.691 50.555 1.00 18.06 ? 128 ARG A CZ 1 ATOM 809 N NH1 . ARG A 1 102 ? 3.480 33.199 49.763 1.00 14.94 ? 128 ARG A NH1 1 ATOM 810 N NH2 . ARG A 1 102 ? 4.543 33.256 51.807 1.00 14.92 ? 128 ARG A NH2 1 ATOM 811 N N . VAL A 1 103 ? 3.226 36.165 46.011 1.00 10.76 ? 129 VAL A N 1 ATOM 812 C CA . VAL A 1 103 ? 1.831 36.578 46.186 1.00 11.35 ? 129 VAL A CA 1 ATOM 813 C C . VAL A 1 103 ? 1.307 36.038 47.506 1.00 10.91 ? 129 VAL A C 1 ATOM 814 O O . VAL A 1 103 ? 1.781 35.001 47.998 1.00 11.86 ? 129 VAL A O 1 ATOM 815 C CB . VAL A 1 103 ? 0.890 36.179 45.025 1.00 11.76 ? 129 VAL A CB 1 ATOM 816 C CG1 . VAL A 1 103 ? 1.246 36.923 43.760 1.00 15.50 ? 129 VAL A CG1 1 ATOM 817 C CG2 . VAL A 1 103 ? 0.903 34.657 44.786 1.00 13.24 ? 129 VAL A CG2 1 ATOM 818 N N . LEU A 1 104 ? 0.364 36.765 48.092 1.00 10.16 ? 130 LEU A N 1 ATOM 819 C CA . LEU A 1 104 ? -0.235 36.399 49.372 1.00 9.78 ? 130 LEU A CA 1 ATOM 820 C C . LEU A 1 104 ? -1.755 36.464 49.299 1.00 10.69 ? 130 LEU A C 1 ATOM 821 O O . LEU A 1 104 ? -2.342 37.497 48.922 1.00 10.60 ? 130 LEU A O 1 ATOM 822 C CB . LEU A 1 104 ? 0.259 37.324 50.486 1.00 13.22 ? 130 LEU A CB 1 ATOM 823 C CG . LEU A 1 104 ? 1.650 37.038 51.033 1.00 15.09 ? 130 LEU A CG 1 ATOM 824 C CD1 . LEU A 1 104 ? 2.065 38.177 51.961 1.00 13.23 ? 130 LEU A CD1 1 ATOM 825 C CD2 . LEU A 1 104 ? 1.643 35.706 51.769 1.00 20.30 ? 130 LEU A CD2 1 ATOM 826 N N . ASN A 1 105 ? -2.375 35.342 49.650 1.00 10.73 ? 131 ASN A N 1 ATOM 827 C CA . ASN A 1 105 ? -3.810 35.266 49.866 1.00 11.20 ? 131 ASN A CA 1 ATOM 828 C C . ASN A 1 105 ? -4.626 35.570 48.618 1.00 11.89 ? 131 ASN A C 1 ATOM 829 O O . ASN A 1 105 ? -5.683 36.191 48.693 1.00 12.20 ? 131 ASN A O 1 ATOM 830 C CB . ASN A 1 105 ? -4.192 36.151 51.050 1.00 12.29 ? 131 ASN A CB 1 ATOM 831 C CG . ASN A 1 105 ? -3.545 35.690 52.341 1.00 12.77 ? 131 ASN A CG 1 ATOM 832 O OD1 . ASN A 1 105 ? -3.695 34.537 52.746 1.00 14.53 ? 131 ASN A OD1 1 ATOM 833 N ND2 . ASN A 1 105 ? -2.791 36.580 52.979 1.00 15.07 ? 131 ASN A ND2 1 ATOM 834 N N . VAL A 1 106 ? -4.141 35.092 47.476 1.00 9.43 ? 132 VAL A N 1 ATOM 835 C CA . VAL A 1 106 ? -4.876 35.190 46.222 1.00 10.18 ? 132 VAL A CA 1 ATOM 836 C C . VAL A 1 106 ? -6.181 34.400 46.382 1.00 12.13 ? 132 VAL A C 1 ATOM 837 O O . VAL A 1 106 ? -6.147 33.223 46.759 1.00 12.21 ? 132 VAL A O 1 ATOM 838 C CB . VAL A 1 106 ? -4.040 34.614 45.059 1.00 10.87 ? 132 VAL A CB 1 ATOM 839 C CG1 . VAL A 1 106 ? -4.896 34.462 43.805 1.00 14.08 ? 132 VAL A CG1 1 ATOM 840 C CG2 . VAL A 1 106 ? -2.790 35.499 44.789 1.00 9.90 ? 132 VAL A CG2 1 ATOM 841 N N . PRO A 1 107 ? -7.335 35.035 46.098 1.00 12.77 ? 133 PRO A N 1 ATOM 842 C CA . PRO A 1 107 ? -8.633 34.396 46.352 1.00 11.06 ? 133 PRO A CA 1 ATOM 843 C C . PRO A 1 107 ? -9.013 33.394 45.269 1.00 10.93 ? 133 PRO A C 1 ATOM 844 O O . PRO A 1 107 ? -9.854 33.665 44.411 1.00 13.97 ? 133 PRO A O 1 ATOM 845 C CB . PRO A 1 107 ? -9.610 35.581 46.370 1.00 13.17 ? 133 PRO A CB 1 ATOM 846 C CG . PRO A 1 107 ? -8.999 36.580 45.441 1.00 11.84 ? 133 PRO A CG 1 ATOM 847 C CD . PRO A 1 107 ? -7.490 36.425 45.624 1.00 11.01 ? 133 PRO A CD 1 ATOM 848 N N . LEU A 1 108 ? -8.422 32.215 45.366 1.00 13.29 ? 134 LEU A N 1 ATOM 849 C CA . LEU A 1 108 ? -8.667 31.142 44.422 1.00 11.76 ? 134 LEU A CA 1 ATOM 850 C C . LEU A 1 108 ? -10.138 30.704 44.449 1.00 13.63 ? 134 LEU A C 1 ATOM 851 O O . LEU A 1 108 ? -10.718 30.486 45.518 1.00 15.72 ? 134 LEU A O 1 ATOM 852 C CB . LEU A 1 108 ? -7.744 29.974 44.757 1.00 13.04 ? 134 LEU A CB 1 ATOM 853 C CG . LEU A 1 108 ? -7.841 28.755 43.853 1.00 16.29 ? 134 LEU A CG 1 ATOM 854 C CD1 . LEU A 1 108 ? -7.468 29.178 42.469 1.00 18.12 ? 134 LEU A CD1 1 ATOM 855 C CD2 . LEU A 1 108 ? -6.898 27.669 44.363 1.00 18.17 ? 134 LEU A CD2 1 ATOM 856 N N . CYS A 1 109 ? -10.751 30.578 43.271 1.00 12.41 ? 135 CYS A N 1 ATOM 857 C CA . CYS A 1 109 ? -12.133 30.125 43.192 1.00 13.29 ? 135 CYS A CA 1 ATOM 858 C C . CYS A 1 109 ? -12.343 28.773 43.864 1.00 11.01 ? 135 CYS A C 1 ATOM 859 O O . CYS A 1 109 ? -11.466 27.905 43.854 1.00 13.26 ? 135 CYS A O 1 ATOM 860 C CB . CYS A 1 109 ? -12.617 30.062 41.745 1.00 15.46 ? 135 CYS A CB 1 ATOM 861 S SG . CYS A 1 109 ? -12.754 31.673 40.982 1.00 19.00 ? 135 CYS A SG 1 ATOM 862 N N . LYS A 1 110 ? -13.520 28.631 44.460 1.00 13.05 ? 136 LYS A N 1 ATOM 863 C CA . LYS A 1 110 ? -13.844 27.447 45.236 1.00 12.79 ? 136 LYS A CA 1 ATOM 864 C C . LYS A 1 110 ? -13.696 26.182 44.401 1.00 14.19 ? 136 LYS A C 1 ATOM 865 O O . LYS A 1 110 ? -13.109 25.199 44.866 1.00 14.98 ? 136 LYS A O 1 ATOM 866 C CB . LYS A 1 110 ? -15.260 27.592 45.786 1.00 16.35 ? 136 LYS A CB 1 ATOM 867 C CG . LYS A 1 110 ? -15.781 26.429 46.597 1.00 22.51 ? 136 LYS A CG 1 ATOM 868 C CD . LYS A 1 110 ? -17.172 26.768 47.117 1.00 26.32 ? 136 LYS A CD 1 ATOM 869 C CE . LYS A 1 110 ? -17.943 25.527 47.575 1.00 35.23 ? 136 LYS A CE 1 ATOM 870 N NZ . LYS A 1 110 ? -17.380 24.944 48.819 1.00 42.47 ? 136 LYS A NZ 1 ATOM 871 N N . GLU A 1 111 ? -14.197 26.210 43.169 1.00 13.07 ? 137 GLU A N 1 ATOM 872 C CA . GLU A 1 111 ? -14.158 25.014 42.314 1.00 17.47 ? 137 GLU A CA 1 ATOM 873 C C . GLU A 1 111 ? -12.732 24.605 41.978 1.00 16.95 ? 137 GLU A C 1 ATOM 874 O O . GLU A 1 111 ? -12.402 23.412 41.995 1.00 17.53 ? 137 GLU A O 1 ATOM 875 C CB . GLU A 1 111 ? -14.919 25.236 41.005 1.00 21.71 ? 137 GLU A CB 1 ATOM 876 C CG . GLU A 1 111 ? -16.418 25.460 41.145 1.00 27.73 ? 137 GLU A CG 1 ATOM 877 C CD . GLU A 1 111 ? -16.790 26.915 40.936 1.00 32.33 ? 137 GLU A CD 1 ATOM 878 O OE1 . GLU A 1 111 ? -16.014 27.779 41.385 1.00 29.50 ? 137 GLU A OE1 1 ATOM 879 O OE2 . GLU A 1 111 ? -17.845 27.188 40.313 1.00 37.78 ? 137 GLU A OE2 1 ATOM 880 N N . ASP A 1 112 ? -11.894 25.582 41.645 1.00 14.39 ? 138 ASP A N 1 ATOM 881 C CA . ASP A 1 112 ? -10.508 25.300 41.299 1.00 14.39 ? 138 ASP A CA 1 ATOM 882 C C . ASP A 1 112 ? -9.811 24.565 42.430 1.00 16.70 ? 138 ASP A C 1 ATOM 883 O O . ASP A 1 112 ? -9.066 23.617 42.201 1.00 18.71 ? 138 ASP A O 1 ATOM 884 C CB . ASP A 1 112 ? -9.761 26.596 40.999 1.00 14.23 ? 138 ASP A CB 1 ATOM 885 C CG . ASP A 1 112 ? -10.332 27.323 39.813 1.00 20.36 ? 138 ASP A CG 1 ATOM 886 O OD1 . ASP A 1 112 ? -11.538 27.637 39.838 1.00 21.32 ? 138 ASP A OD1 1 ATOM 887 O OD2 . ASP A 1 112 ? -9.579 27.566 38.849 1.00 17.73 ? 138 ASP A OD2 1 ATOM 888 N N . CYS A 1 113 ? -10.083 24.992 43.656 1.00 10.91 ? 139 CYS A N 1 ATOM 889 C CA . CYS A 1 113 ? -9.473 24.390 44.828 1.00 11.80 ? 139 CYS A CA 1 ATOM 890 C C . CYS A 1 113 ? -10.032 23.004 45.155 1.00 13.86 ? 139 CYS A C 1 ATOM 891 O O . CYS A 1 113 ? -9.279 22.037 45.365 1.00 12.63 ? 139 CYS A O 1 ATOM 892 C CB . CYS A 1 113 ? -9.678 25.310 46.018 1.00 14.20 ? 139 CYS A CB 1 ATOM 893 S SG . CYS A 1 113 ? -8.894 24.680 47.509 1.00 19.27 ? 139 CYS A SG 1 ATOM 894 N N . GLU A 1 114 ? -11.359 22.882 45.185 1.00 10.74 ? 140 GLU A N 1 ATOM 895 C CA . GLU A 1 114 ? -11.974 21.617 45.585 1.00 12.23 ? 140 GLU A CA 1 ATOM 896 C C . GLU A 1 114 ? -11.688 20.509 44.588 1.00 13.71 ? 140 GLU A C 1 ATOM 897 O O . GLU A 1 114 ? -11.432 19.381 44.974 1.00 13.78 ? 140 GLU A O 1 ATOM 898 C CB . GLU A 1 114 ? -13.469 21.777 45.832 1.00 13.15 ? 140 GLU A CB 1 ATOM 899 C CG . GLU A 1 114 ? -13.708 22.707 47.014 1.00 14.94 ? 140 GLU A CG 1 ATOM 900 C CD . GLU A 1 114 ? -15.156 22.788 47.441 1.00 25.99 ? 140 GLU A CD 1 ATOM 901 O OE1 . GLU A 1 114 ? -16.044 22.419 46.646 1.00 28.75 ? 140 GLU A OE1 1 ATOM 902 O OE2 . GLU A 1 114 ? -15.402 23.243 48.578 1.00 32.12 ? 140 GLU A OE2 1 ATOM 903 N N . GLN A 1 115 ? -11.671 20.844 43.305 1.00 13.56 ? 141 GLN A N 1 ATOM 904 C CA . GLN A 1 115 ? -11.435 19.820 42.283 1.00 11.96 ? 141 GLN A CA 1 ATOM 905 C C . GLN A 1 115 ? -9.962 19.421 42.197 1.00 13.84 ? 141 GLN A C 1 ATOM 906 O O . GLN A 1 115 ? -9.653 18.275 41.870 1.00 14.40 ? 141 GLN A O 1 ATOM 907 C CB . GLN A 1 115 ? -11.974 20.283 40.927 1.00 14.16 ? 141 GLN A CB 1 ATOM 908 C CG . GLN A 1 115 ? -13.495 20.434 40.913 1.00 15.43 ? 141 GLN A CG 1 ATOM 909 C CD . GLN A 1 115 ? -14.006 20.932 39.588 1.00 22.52 ? 141 GLN A CD 1 ATOM 910 O OE1 . GLN A 1 115 ? -13.440 20.622 38.538 1.00 27.95 ? 141 GLN A OE1 1 ATOM 911 N NE2 . GLN A 1 115 ? -15.072 21.722 39.623 1.00 23.18 ? 141 GLN A NE2 1 ATOM 912 N N . TRP A 1 116 ? -9.063 20.364 42.490 1.00 12.83 ? 142 TRP A N 1 ATOM 913 C CA . TRP A 1 116 ? -7.636 20.094 42.583 1.00 9.89 ? 142 TRP A CA 1 ATOM 914 C C . TRP A 1 116 ? -7.431 19.073 43.688 1.00 12.06 ? 142 TRP A C 1 ATOM 915 O O . TRP A 1 116 ? -6.733 18.068 43.499 1.00 11.15 ? 142 TRP A O 1 ATOM 916 C CB . TRP A 1 116 ? -6.921 21.411 42.925 1.00 9.22 ? 142 TRP A CB 1 ATOM 917 C CG . TRP A 1 116 ? -5.418 21.425 43.021 1.00 12.57 ? 142 TRP A CG 1 ATOM 918 C CD1 . TRP A 1 116 ? -4.543 20.398 42.807 1.00 11.34 ? 142 TRP A CD1 1 ATOM 919 C CD2 . TRP A 1 116 ? -4.621 22.564 43.372 1.00 11.32 ? 142 TRP A CD2 1 ATOM 920 N NE1 . TRP A 1 116 ? -3.244 20.838 42.994 1.00 13.42 ? 142 TRP A NE1 1 ATOM 921 C CE2 . TRP A 1 116 ? -3.271 22.163 43.350 1.00 14.72 ? 142 TRP A CE2 1 ATOM 922 C CE3 . TRP A 1 116 ? -4.927 23.886 43.706 1.00 13.86 ? 142 TRP A CE3 1 ATOM 923 C CZ2 . TRP A 1 116 ? -2.222 23.044 43.644 1.00 17.39 ? 142 TRP A CZ2 1 ATOM 924 C CZ3 . TRP A 1 116 ? -3.897 24.755 43.998 1.00 13.08 ? 142 TRP A CZ3 1 ATOM 925 C CH2 . TRP A 1 116 ? -2.558 24.335 43.971 1.00 14.57 ? 142 TRP A CH2 1 ATOM 926 N N . TRP A 1 117 ? -8.049 19.322 44.837 1.00 12.14 ? 143 TRP A N 1 ATOM 927 C CA . TRP A 1 117 ? -7.928 18.414 45.982 1.00 9.63 ? 143 TRP A CA 1 ATOM 928 C C . TRP A 1 117 ? -8.453 17.016 45.670 1.00 11.79 ? 143 TRP A C 1 ATOM 929 O O . TRP A 1 117 ? -7.806 16.018 45.991 1.00 12.47 ? 143 TRP A O 1 ATOM 930 C CB . TRP A 1 117 ? -8.636 19.042 47.189 1.00 9.65 ? 143 TRP A CB 1 ATOM 931 C CG . TRP A 1 117 ? -8.601 18.234 48.452 1.00 10.19 ? 143 TRP A CG 1 ATOM 932 C CD1 . TRP A 1 117 ? -7.609 18.239 49.394 1.00 10.24 ? 143 TRP A CD1 1 ATOM 933 C CD2 . TRP A 1 117 ? -9.608 17.324 48.926 1.00 11.15 ? 143 TRP A CD2 1 ATOM 934 N NE1 . TRP A 1 117 ? -7.940 17.384 50.422 1.00 11.01 ? 143 TRP A NE1 1 ATOM 935 C CE2 . TRP A 1 117 ? -9.160 16.815 50.162 1.00 12.12 ? 143 TRP A CE2 1 ATOM 936 C CE3 . TRP A 1 117 ? -10.841 16.888 48.422 1.00 13.30 ? 143 TRP A CE3 1 ATOM 937 C CZ2 . TRP A 1 117 ? -9.899 15.892 50.904 1.00 14.27 ? 143 TRP A CZ2 1 ATOM 938 C CZ3 . TRP A 1 117 ? -11.575 15.976 49.158 1.00 15.31 ? 143 TRP A CZ3 1 ATOM 939 C CH2 . TRP A 1 117 ? -11.101 15.476 50.382 1.00 17.26 ? 143 TRP A CH2 1 ATOM 940 N N . GLU A 1 118 ? -9.624 16.944 45.045 1.00 13.15 ? 144 GLU A N 1 ATOM 941 C CA . GLU A 1 118 ? -10.223 15.686 44.659 1.00 14.45 ? 144 GLU A CA 1 ATOM 942 C C . GLU A 1 118 ? -9.332 14.938 43.687 1.00 12.77 ? 144 GLU A C 1 ATOM 943 O O . GLU A 1 118 ? -9.069 13.742 43.859 1.00 12.46 ? 144 GLU A O 1 ATOM 944 C CB . GLU A 1 118 ? -11.575 15.965 44.004 1.00 16.79 ? 144 GLU A CB 1 ATOM 945 C CG . GLU A 1 118 ? -12.307 14.726 43.584 1.00 23.48 ? 144 GLU A CG 1 ATOM 946 C CD . GLU A 1 118 ? -12.726 13.899 44.764 1.00 39.88 ? 144 GLU A CD 1 ATOM 947 O OE1 . GLU A 1 118 ? -13.196 14.496 45.755 1.00 43.96 ? 144 GLU A OE1 1 ATOM 948 O OE2 . GLU A 1 118 ? -12.578 12.659 44.714 1.00 48.03 ? 144 GLU A OE2 1 ATOM 949 N N . ASP A 1 119 ? -8.856 15.639 42.664 1.00 13.40 ? 145 ASP A N 1 ATOM 950 C CA . ASP A 1 119 ? -8.157 14.960 41.588 1.00 11.09 ? 145 ASP A CA 1 ATOM 951 C C . ASP A 1 119 ? -6.788 14.440 42.011 1.00 12.44 ? 145 ASP A C 1 ATOM 952 O O . ASP A 1 119 ? -6.173 13.662 41.287 1.00 11.98 ? 145 ASP A O 1 ATOM 953 C CB . ASP A 1 119 ? -8.049 15.859 40.360 1.00 11.58 ? 145 ASP A CB 1 ATOM 954 C CG . ASP A 1 119 ? -9.393 16.074 39.689 1.00 18.43 ? 145 ASP A CG 1 ATOM 955 O OD1 . ASP A 1 119 ? -10.349 15.349 40.044 1.00 21.52 ? 145 ASP A OD1 1 ATOM 956 O OD2 . ASP A 1 119 ? -9.505 16.966 38.815 1.00 17.34 ? 145 ASP A OD2 1 ATOM 957 N N . CYS A 1 120 ? -6.332 14.860 43.186 1.00 10.80 ? 146 CYS A N 1 ATOM 958 C CA . CYS A 1 120 ? -5.018 14.458 43.675 1.00 10.44 ? 146 CYS A CA 1 ATOM 959 C C . CYS A 1 120 ? -5.114 13.377 44.734 1.00 11.86 ? 146 CYS A C 1 ATOM 960 O O . CYS A 1 120 ? -4.099 12.958 45.286 1.00 11.76 ? 146 CYS A O 1 ATOM 961 C CB . CYS A 1 120 ? -4.240 15.668 44.210 1.00 10.44 ? 146 CYS A CB 1 ATOM 962 S SG . CYS A 1 120 ? -3.681 16.798 42.903 1.00 14.15 ? 146 CYS A SG 1 ATOM 963 N N . ARG A 1 121 ? -6.325 12.891 44.983 1.00 12.21 ? 147 ARG A N 1 ATOM 964 C CA . ARG A 1 121 ? -6.555 11.850 45.993 1.00 12.97 ? 147 ARG A CA 1 ATOM 965 C C . ARG A 1 121 ? -5.640 10.629 45.859 1.00 15.28 ? 147 ARG A C 1 ATOM 966 O O . ARG A 1 121 ? -5.208 10.054 46.863 1.00 16.96 ? 147 ARG A O 1 ATOM 967 C CB . ARG A 1 121 ? -8.015 11.398 45.944 1.00 15.44 ? 147 ARG A CB 1 ATOM 968 C CG . ARG A 1 121 ? -8.354 10.275 46.909 1.00 18.52 ? 147 ARG A CG 1 ATOM 969 C CD . ARG A 1 121 ? -9.846 9.957 46.865 1.00 20.94 ? 147 ARG A CD 1 ATOM 970 N NE . ARG A 1 121 ? -10.141 8.724 47.588 1.00 31.90 ? 147 ARG A NE 1 ATOM 971 C CZ . ARG A 1 121 ? -10.236 7.533 47.006 1.00 34.26 ? 147 ARG A CZ 1 ATOM 972 N NH1 . ARG A 1 121 ? -10.068 7.420 45.695 1.00 30.62 ? 147 ARG A NH1 1 ATOM 973 N NH2 . ARG A 1 121 ? -10.505 6.458 47.734 1.00 38.58 ? 147 ARG A NH2 1 ATOM 974 N N . THR A 1 122 ? -5.337 10.232 44.627 1.00 13.63 ? 148 THR A N 1 ATOM 975 C CA . THR A 1 122 ? -4.599 8.975 44.403 1.00 15.35 ? 148 THR A CA 1 ATOM 976 C C . THR A 1 122 ? -3.108 9.212 44.175 1.00 15.22 ? 148 THR A C 1 ATOM 977 O O . THR A 1 122 ? -2.362 8.293 43.808 1.00 16.63 ? 148 THR A O 1 ATOM 978 C CB . THR A 1 122 ? -5.176 8.185 43.223 1.00 18.26 ? 148 THR A CB 1 ATOM 979 O OG1 . THR A 1 122 ? -4.941 8.911 42.008 1.00 19.04 ? 148 THR A OG1 1 ATOM 980 C CG2 . THR A 1 122 ? -6.665 7.944 43.414 1.00 17.77 ? 148 THR A CG2 1 ATOM 981 N N . SER A 1 123 ? -2.673 10.452 44.362 1.00 11.47 ? 149 SER A N 1 ATOM 982 C CA . SER A 1 123 ? -1.270 10.783 44.265 1.00 11.29 ? 149 SER A CA 1 ATOM 983 C C . SER A 1 123 ? -0.668 10.849 45.661 1.00 12.62 ? 149 SER A C 1 ATOM 984 O O . SER A 1 123 ? -1.383 10.677 46.670 1.00 17.75 ? 149 SER A O 1 ATOM 985 C CB . SER A 1 123 ? -1.103 12.106 43.524 1.00 11.19 ? 149 SER A CB 1 ATOM 986 O OG . SER A 1 123 ? -1.669 11.966 42.235 1.00 13.30 ? 149 SER A OG 1 ATOM 987 N N . TYR A 1 124 ? 0.643 11.062 45.707 1.00 12.25 ? 150 TYR A N 1 ATOM 988 C CA . TYR A 1 124 ? 1.391 10.938 46.941 1.00 14.59 ? 150 TYR A CA 1 ATOM 989 C C . TYR A 1 124 ? 2.336 12.104 47.090 1.00 13.97 ? 150 TYR A C 1 ATOM 990 O O . TYR A 1 124 ? 2.783 12.683 46.096 1.00 12.97 ? 150 TYR A O 1 ATOM 991 C CB . TYR A 1 124 ? 2.198 9.637 46.930 1.00 14.46 ? 150 TYR A CB 1 ATOM 992 C CG . TYR A 1 124 ? 1.355 8.397 46.926 1.00 18.41 ? 150 TYR A CG 1 ATOM 993 C CD1 . TYR A 1 124 ? 0.952 7.813 45.729 1.00 24.45 ? 150 TYR A CD1 1 ATOM 994 C CD2 . TYR A 1 124 ? 0.952 7.817 48.106 1.00 17.29 ? 150 TYR A CD2 1 ATOM 995 C CE1 . TYR A 1 124 ? 0.179 6.673 45.713 1.00 28.18 ? 150 TYR A CE1 1 ATOM 996 C CE2 . TYR A 1 124 ? 0.160 6.665 48.106 1.00 20.74 ? 150 TYR A CE2 1 ATOM 997 C CZ . TYR A 1 124 ? -0.219 6.104 46.902 1.00 28.14 ? 150 TYR A CZ 1 ATOM 998 O OH . TYR A 1 124 ? -0.998 4.970 46.879 1.00 32.23 ? 150 TYR A OH 1 ATOM 999 N N . THR A 1 125 ? 2.625 12.481 48.329 1.00 12.84 ? 151 THR A N 1 ATOM 1000 C CA . THR A 1 125 ? 3.624 13.527 48.567 1.00 12.01 ? 151 THR A CA 1 ATOM 1001 C C . THR A 1 125 ? 4.250 13.311 49.936 1.00 11.03 ? 151 THR A C 1 ATOM 1002 O O . THR A 1 125 ? 3.811 12.453 50.690 1.00 12.47 ? 151 THR A O 1 ATOM 1003 C CB . THR A 1 125 ? 3.034 14.962 48.461 1.00 11.36 ? 151 THR A CB 1 ATOM 1004 O OG1 . THR A 1 125 ? 4.103 15.924 48.479 1.00 12.14 ? 151 THR A OG1 1 ATOM 1005 C CG2 . THR A 1 125 ? 2.050 15.258 49.622 1.00 11.74 ? 151 THR A CG2 1 ATOM 1006 N N . CYS A 1 126 ? 5.268 14.098 50.263 1.00 13.70 ? 152 CYS A N 1 ATOM 1007 C CA . CYS A 1 126 ? 6.028 13.871 51.483 1.00 13.31 ? 152 CYS A CA 1 ATOM 1008 C C . CYS A 1 126 ? 6.066 15.108 52.377 1.00 13.05 ? 152 CYS A C 1 ATOM 1009 O O . CYS A 1 126 ? 6.743 15.116 53.409 1.00 15.94 ? 152 CYS A O 1 ATOM 1010 C CB . CYS A 1 126 ? 7.463 13.419 51.153 1.00 13.19 ? 152 CYS A CB 1 ATOM 1011 S SG . CYS A 1 126 ? 8.358 14.616 50.114 1.00 15.53 ? 152 CYS A SG 1 ATOM 1012 N N . LYS A 1 127 ? 5.344 16.155 51.984 1.00 13.25 ? 153 LYS A N 1 ATOM 1013 C CA . LYS A 1 127 ? 5.321 17.381 52.791 1.00 15.48 ? 153 LYS A CA 1 ATOM 1014 C C . LYS A 1 127 ? 4.116 18.220 52.460 1.00 13.94 ? 153 LYS A C 1 ATOM 1015 O O . LYS A 1 127 ? 3.535 18.074 51.380 1.00 12.69 ? 153 LYS A O 1 ATOM 1016 C CB . LYS A 1 127 ? 6.596 18.197 52.585 1.00 20.26 ? 153 LYS A CB 1 ATOM 1017 C CG . LYS A 1 127 ? 6.906 18.508 51.138 1.00 20.78 ? 153 LYS A CG 1 ATOM 1018 C CD . LYS A 1 127 ? 8.432 18.572 50.901 1.00 23.88 ? 153 LYS A CD 1 ATOM 1019 C CE . LYS A 1 127 ? 8.975 19.978 50.992 1.00 25.91 ? 153 LYS A CE 1 ATOM 1020 N NZ . LYS A 1 127 ? 8.956 20.545 52.372 1.00 25.78 ? 153 LYS A NZ 1 ATOM 1021 N N . SER A 1 128 ? 3.728 19.084 53.397 1.00 12.82 ? 154 SER A N 1 ATOM 1022 C CA . SER A 1 128 ? 2.589 19.969 53.177 1.00 14.62 ? 154 SER A CA 1 ATOM 1023 C C . SER A 1 128 ? 2.991 21.352 52.649 1.00 17.09 ? 154 SER A C 1 ATOM 1024 O O . SER A 1 128 ? 2.159 22.054 52.074 1.00 17.91 ? 154 SER A O 1 ATOM 1025 C CB . SER A 1 128 ? 1.764 20.128 54.455 1.00 21.38 ? 154 SER A CB 1 ATOM 1026 O OG . SER A 1 128 ? 2.549 20.694 55.485 1.00 27.85 ? 154 SER A OG 1 ATOM 1027 N N . ASN A 1 129 ? 4.237 21.768 52.855 1.00 16.62 ? 155 ASN A N 1 ATOM 1028 C CA . ASN A 1 129 ? 4.676 23.059 52.315 1.00 16.02 ? 155 ASN A CA 1 ATOM 1029 C C . ASN A 1 129 ? 5.703 22.786 51.232 1.00 17.97 ? 155 ASN A C 1 ATOM 1030 O O . ASN A 1 129 ? 6.803 22.307 51.524 1.00 20.99 ? 155 ASN A O 1 ATOM 1031 C CB . ASN A 1 129 ? 5.276 23.943 53.410 1.00 23.68 ? 155 ASN A CB 1 ATOM 1032 C CG . ASN A 1 129 ? 5.799 25.269 52.874 1.00 37.43 ? 155 ASN A CG 1 ATOM 1033 O OD1 . ASN A 1 129 ? 5.542 25.642 51.724 1.00 39.57 ? 155 ASN A OD1 1 ATOM 1034 N ND2 . ASN A 1 129 ? 6.520 26.002 53.721 1.00 44.56 ? 155 ASN A ND2 1 ATOM 1035 N N . TRP A 1 130 ? 5.340 23.059 49.983 1.00 14.67 ? 156 TRP A N 1 ATOM 1036 C CA . TRP A 1 130 ? 6.200 22.706 48.843 1.00 11.58 ? 156 TRP A CA 1 ATOM 1037 C C . TRP A 1 130 ? 7.182 23.805 48.415 1.00 13.16 ? 156 TRP A C 1 ATOM 1038 O O . TRP A 1 130 ? 7.950 23.609 47.466 1.00 13.15 ? 156 TRP A O 1 ATOM 1039 C CB . TRP A 1 130 ? 5.349 22.315 47.627 1.00 11.16 ? 156 TRP A CB 1 ATOM 1040 C CG . TRP A 1 130 ? 4.690 20.980 47.703 1.00 10.01 ? 156 TRP A CG 1 ATOM 1041 C CD1 . TRP A 1 130 ? 4.490 20.215 48.820 1.00 12.01 ? 156 TRP A CD1 1 ATOM 1042 C CD2 . TRP A 1 130 ? 4.165 20.216 46.599 1.00 10.19 ? 156 TRP A CD2 1 ATOM 1043 N NE1 . TRP A 1 130 ? 3.877 19.034 48.475 1.00 11.84 ? 156 TRP A NE1 1 ATOM 1044 C CE2 . TRP A 1 130 ? 3.657 19.019 47.124 1.00 11.44 ? 156 TRP A CE2 1 ATOM 1045 C CE3 . TRP A 1 130 ? 4.069 20.451 45.226 1.00 11.77 ? 156 TRP A CE3 1 ATOM 1046 C CZ2 . TRP A 1 130 ? 3.068 18.036 46.316 1.00 12.11 ? 156 TRP A CZ2 1 ATOM 1047 C CZ3 . TRP A 1 130 ? 3.483 19.472 44.426 1.00 11.21 ? 156 TRP A CZ3 1 ATOM 1048 C CH2 . TRP A 1 130 ? 2.979 18.290 44.975 1.00 13.06 ? 156 TRP A CH2 1 ATOM 1049 N N . HIS A 1 131 ? 7.166 24.955 49.082 1.00 13.28 ? 157 HIS A N 1 ATOM 1050 C CA . HIS A 1 131 ? 8.084 26.030 48.718 1.00 16.46 ? 157 HIS A CA 1 ATOM 1051 C C . HIS A 1 131 ? 9.498 25.756 49.226 1.00 19.89 ? 157 HIS A C 1 ATOM 1052 O O . HIS A 1 131 ? 10.482 26.136 48.584 1.00 26.56 ? 157 HIS A O 1 ATOM 1053 C CB . HIS A 1 131 ? 7.589 27.373 49.243 1.00 18.32 ? 157 HIS A CB 1 ATOM 1054 C CG . HIS A 1 131 ? 8.488 28.511 48.909 1.00 22.51 ? 157 HIS A CG 1 ATOM 1055 N ND1 . HIS A 1 131 ? 8.824 28.839 47.602 1.00 23.08 ? 157 HIS A ND1 1 ATOM 1056 C CD2 . HIS A 1 131 ? 9.158 29.382 49.687 1.00 24.21 ? 157 HIS A CD2 1 ATOM 1057 C CE1 . HIS A 1 131 ? 9.652 29.853 47.608 1.00 25.08 ? 157 HIS A CE1 1 ATOM 1058 N NE2 . HIS A 1 131 ? 9.871 30.222 48.866 1.00 26.77 ? 157 HIS A NE2 1 ATOM 1059 N N . LYS A 1 132 ? 9.596 25.104 50.377 1.00 18.56 ? 158 LYS A N 1 ATOM 1060 C CA . LYS A 1 132 ? 10.882 24.977 51.059 1.00 24.80 ? 158 LYS A CA 1 ATOM 1061 C C . LYS A 1 132 ? 11.102 23.572 51.570 1.00 20.96 ? 158 LYS A C 1 ATOM 1062 O O . LYS A 1 132 ? 10.152 22.814 51.729 1.00 21.82 ? 158 LYS A O 1 ATOM 1063 C CB . LYS A 1 132 ? 10.912 25.931 52.250 1.00 36.86 ? 158 LYS A CB 1 ATOM 1064 C CG . LYS A 1 132 ? 12.049 26.923 52.227 1.00 45.70 ? 158 LYS A CG 1 ATOM 1065 C CD . LYS A 1 132 ? 12.014 27.763 50.970 1.00 50.56 ? 158 LYS A CD 1 ATOM 1066 C CE . LYS A 1 132 ? 12.529 29.160 51.258 1.00 59.62 ? 158 LYS A CE 1 ATOM 1067 N NZ . LYS A 1 132 ? 11.836 29.764 52.438 1.00 63.70 ? 158 LYS A NZ 1 ATOM 1068 N N . GLY A 1 133 ? 12.360 23.223 51.830 1.00 20.75 ? 159 GLY A N 1 ATOM 1069 C CA . GLY A 1 133 ? 12.649 21.965 52.495 1.00 22.69 ? 159 GLY A CA 1 ATOM 1070 C C . GLY A 1 133 ? 12.915 20.757 51.614 1.00 20.89 ? 159 GLY A C 1 ATOM 1071 O O . GLY A 1 133 ? 13.045 19.649 52.130 1.00 23.04 ? 159 GLY A O 1 ATOM 1072 N N . TRP A 1 134 ? 13.006 20.953 50.303 1.00 16.93 ? 160 TRP A N 1 ATOM 1073 C CA . TRP A 1 134 ? 13.326 19.846 49.407 1.00 14.99 ? 160 TRP A CA 1 ATOM 1074 C C . TRP A 1 134 ? 14.819 19.602 49.364 1.00 15.24 ? 160 TRP A C 1 ATOM 1075 O O . TRP A 1 134 ? 15.615 20.482 49.692 1.00 18.52 ? 160 TRP A O 1 ATOM 1076 C CB . TRP A 1 134 ? 12.886 20.154 47.985 1.00 13.25 ? 160 TRP A CB 1 ATOM 1077 C CG . TRP A 1 134 ? 11.431 20.307 47.802 1.00 11.97 ? 160 TRP A CG 1 ATOM 1078 C CD1 . TRP A 1 134 ? 10.744 21.479 47.690 1.00 12.84 ? 160 TRP A CD1 1 ATOM 1079 C CD2 . TRP A 1 134 ? 10.464 19.255 47.677 1.00 13.81 ? 160 TRP A CD2 1 ATOM 1080 N NE1 . TRP A 1 134 ? 9.407 21.220 47.513 1.00 12.95 ? 160 TRP A NE1 1 ATOM 1081 C CE2 . TRP A 1 134 ? 9.208 19.865 47.499 1.00 13.56 ? 160 TRP A CE2 1 ATOM 1082 C CE3 . TRP A 1 134 ? 10.541 17.865 47.690 1.00 11.58 ? 160 TRP A CE3 1 ATOM 1083 C CZ2 . TRP A 1 134 ? 8.022 19.125 47.344 1.00 13.87 ? 160 TRP A CZ2 1 ATOM 1084 C CZ3 . TRP A 1 134 ? 9.360 17.118 47.546 1.00 12.17 ? 160 TRP A CZ3 1 ATOM 1085 C CH2 . TRP A 1 134 ? 8.118 17.755 47.371 1.00 12.26 ? 160 TRP A CH2 1 ATOM 1086 N N . ASN A 1 135 ? 15.201 18.407 48.931 1.00 14.75 ? 161 ASN A N 1 ATOM 1087 C CA . ASN A 1 135 ? 16.594 18.123 48.656 1.00 13.67 ? 161 ASN A CA 1 ATOM 1088 C C . ASN A 1 135 ? 16.796 18.319 47.159 1.00 15.48 ? 161 ASN A C 1 ATOM 1089 O O . ASN A 1 135 ? 16.270 17.540 46.364 1.00 14.84 ? 161 ASN A O 1 ATOM 1090 C CB . ASN A 1 135 ? 16.902 16.684 49.073 1.00 12.84 ? 161 ASN A CB 1 ATOM 1091 C CG . ASN A 1 135 ? 18.343 16.300 48.844 1.00 19.14 ? 161 ASN A CG 1 ATOM 1092 O OD1 . ASN A 1 135 ? 19.096 16.984 48.142 1.00 19.47 ? 161 ASN A OD1 1 ATOM 1093 N ND2 . ASN A 1 135 ? 18.743 15.185 49.438 1.00 19.78 ? 161 ASN A ND2 1 ATOM 1094 N N . TRP A 1 136 ? 17.539 19.357 46.771 1.00 13.12 ? 162 TRP A N 1 ATOM 1095 C CA . TRP A 1 136 ? 17.709 19.666 45.353 1.00 12.45 ? 162 TRP A CA 1 ATOM 1096 C C . TRP A 1 136 ? 19.066 19.228 44.780 1.00 13.87 ? 162 TRP A C 1 ATOM 1097 O O . TRP A 1 136 ? 19.430 19.638 43.671 1.00 16.97 ? 162 TRP A O 1 ATOM 1098 C CB . TRP A 1 136 ? 17.560 21.176 45.129 1.00 14.22 ? 162 TRP A CB 1 ATOM 1099 C CG . TRP A 1 136 ? 16.149 21.739 45.236 1.00 13.52 ? 162 TRP A CG 1 ATOM 1100 C CD1 . TRP A 1 136 ? 15.551 22.289 46.343 1.00 15.38 ? 162 TRP A CD1 1 ATOM 1101 C CD2 . TRP A 1 136 ? 15.191 21.843 44.171 1.00 14.42 ? 162 TRP A CD2 1 ATOM 1102 N NE1 . TRP A 1 136 ? 14.276 22.714 46.028 1.00 16.31 ? 162 TRP A NE1 1 ATOM 1103 C CE2 . TRP A 1 136 ? 14.032 22.448 44.709 1.00 14.25 ? 162 TRP A CE2 1 ATOM 1104 C CE3 . TRP A 1 136 ? 15.204 21.481 42.823 1.00 15.96 ? 162 TRP A CE3 1 ATOM 1105 C CZ2 . TRP A 1 136 ? 12.896 22.711 43.927 1.00 16.92 ? 162 TRP A CZ2 1 ATOM 1106 C CZ3 . TRP A 1 136 ? 14.067 21.732 42.052 1.00 17.67 ? 162 TRP A CZ3 1 ATOM 1107 C CH2 . TRP A 1 136 ? 12.931 22.343 42.611 1.00 18.72 ? 162 TRP A CH2 1 ATOM 1108 N N . THR A 1 137 ? 19.833 18.431 45.515 1.00 12.72 ? 163 THR A N 1 ATOM 1109 C CA . THR A 1 137 ? 21.205 18.162 45.085 1.00 14.43 ? 163 THR A CA 1 ATOM 1110 C C . THR A 1 137 ? 21.320 17.401 43.754 1.00 15.21 ? 163 THR A C 1 ATOM 1111 O O . THR A 1 137 ? 22.339 17.513 43.065 1.00 16.75 ? 163 THR A O 1 ATOM 1112 C CB . THR A 1 137 ? 22.031 17.449 46.175 1.00 16.44 ? 163 THR A CB 1 ATOM 1113 O OG1 . THR A 1 137 ? 21.409 16.198 46.489 1.00 18.87 ? 163 THR A OG1 1 ATOM 1114 C CG2 . THR A 1 137 ? 22.099 18.303 47.427 1.00 17.04 ? 163 THR A CG2 1 ATOM 1115 N N . SER A 1 138 ? 20.277 16.662 43.380 1.00 17.47 ? 164 SER A N 1 ATOM 1116 C CA . SER A 1 138 ? 20.316 15.915 42.128 1.00 18.67 ? 164 SER A CA 1 ATOM 1117 C C . SER A 1 138 ? 19.978 16.813 40.931 1.00 23.66 ? 164 SER A C 1 ATOM 1118 O O . SER A 1 138 ? 20.103 16.391 39.773 1.00 29.36 ? 164 SER A O 1 ATOM 1119 C CB . SER A 1 138 ? 19.343 14.730 42.194 1.00 20.81 ? 164 SER A CB 1 ATOM 1120 O OG . SER A 1 138 ? 18.007 15.197 42.316 1.00 26.85 ? 164 SER A OG 1 ATOM 1121 N N . GLY A 1 139 ? 19.572 18.051 41.206 1.00 18.16 ? 165 GLY A N 1 ATOM 1122 C CA . GLY A 1 139 ? 19.117 18.960 40.165 1.00 20.03 ? 165 GLY A CA 1 ATOM 1123 C C . GLY A 1 139 ? 17.609 19.155 40.198 1.00 21.87 ? 165 GLY A C 1 ATOM 1124 O O . GLY A 1 139 ? 17.093 20.245 39.962 1.00 25.09 ? 165 GLY A O 1 ATOM 1125 N N . PHE A 1 140 ? 16.888 18.083 40.497 1.00 20.03 ? 166 PHE A N 1 ATOM 1126 C CA . PHE A 1 140 ? 15.445 18.182 40.675 1.00 17.11 ? 166 PHE A CA 1 ATOM 1127 C C . PHE A 1 140 ? 15.160 17.925 42.153 1.00 15.66 ? 166 PHE A C 1 ATOM 1128 O O . PHE A 1 140 ? 16.032 17.417 42.868 1.00 15.42 ? 166 PHE A O 1 ATOM 1129 C CB . PHE A 1 140 ? 14.709 17.188 39.763 1.00 18.80 ? 166 PHE A CB 1 ATOM 1130 C CG . PHE A 1 140 ? 15.259 15.787 39.828 1.00 19.47 ? 166 PHE A CG 1 ATOM 1131 C CD1 . PHE A 1 140 ? 14.769 14.881 40.756 1.00 17.96 ? 166 PHE A CD1 1 ATOM 1132 C CD2 . PHE A 1 140 ? 16.283 15.383 38.977 1.00 20.51 ? 166 PHE A CD2 1 ATOM 1133 C CE1 . PHE A 1 140 ? 15.276 13.605 40.832 1.00 22.84 ? 166 PHE A CE1 1 ATOM 1134 C CE2 . PHE A 1 140 ? 16.800 14.104 39.047 1.00 23.72 ? 166 PHE A CE2 1 ATOM 1135 C CZ . PHE A 1 140 ? 16.291 13.209 39.981 1.00 25.20 ? 166 PHE A CZ 1 ATOM 1136 N N . ASN A 1 141 ? 13.969 18.283 42.619 1.00 16.83 ? 167 ASN A N 1 ATOM 1137 C CA . ASN A 1 141 ? 13.657 18.128 44.039 1.00 14.89 ? 167 ASN A CA 1 ATOM 1138 C C . ASN A 1 141 ? 13.290 16.699 44.411 1.00 16.32 ? 167 ASN A C 1 ATOM 1139 O O . ASN A 1 141 ? 12.513 16.041 43.714 1.00 17.10 ? 167 ASN A O 1 ATOM 1140 C CB . ASN A 1 141 ? 12.528 19.063 44.462 1.00 14.30 ? 167 ASN A CB 1 ATOM 1141 C CG . ASN A 1 141 ? 11.305 18.928 43.585 1.00 14.62 ? 167 ASN A CG 1 ATOM 1142 O OD1 . ASN A 1 141 ? 11.376 19.171 42.379 1.00 15.80 ? 167 ASN A OD1 1 ATOM 1143 N ND2 . ASN A 1 141 ? 10.176 18.550 44.182 1.00 15.17 ? 167 ASN A ND2 1 ATOM 1144 N N . LYS A 1 142 ? 13.866 16.209 45.503 1.00 14.51 ? 168 LYS A N 1 ATOM 1145 C CA . LYS A 1 142 ? 13.479 14.911 46.043 1.00 14.40 ? 168 LYS A CA 1 ATOM 1146 C C . LYS A 1 142 ? 13.132 15.108 47.511 1.00 17.13 ? 168 LYS A C 1 ATOM 1147 O O . LYS A 1 142 ? 13.528 16.114 48.122 1.00 15.61 ? 168 LYS A O 1 ATOM 1148 C CB . LYS A 1 142 ? 14.623 13.904 45.894 1.00 18.66 ? 168 LYS A CB 1 ATOM 1149 C CG . LYS A 1 142 ? 15.096 13.703 44.462 1.00 21.84 ? 168 LYS A CG 1 ATOM 1150 C CD . LYS A 1 142 ? 16.105 12.555 44.359 1.00 25.87 ? 168 LYS A CD 1 ATOM 1151 C CE . LYS A 1 142 ? 17.328 12.797 45.226 1.00 34.97 ? 168 LYS A CE 1 ATOM 1152 N NZ . LYS A 1 142 ? 18.453 11.913 44.826 1.00 43.82 ? 168 LYS A NZ 1 ATOM 1153 N N . CYS A 1 143 ? 12.376 14.173 48.073 1.00 16.60 ? 169 CYS A N 1 ATOM 1154 C CA . CYS A 1 143 ? 12.042 14.238 49.486 1.00 16.78 ? 169 CYS A CA 1 ATOM 1155 C C . CYS A 1 143 ? 13.299 14.145 50.343 1.00 18.89 ? 169 CYS A C 1 ATOM 1156 O O . CYS A 1 143 ? 14.217 13.348 50.072 1.00 22.82 ? 169 CYS A O 1 ATOM 1157 C CB . CYS A 1 143 ? 11.096 13.102 49.867 1.00 14.37 ? 169 CYS A CB 1 ATOM 1158 S SG . CYS A 1 143 ? 9.484 13.251 49.055 1.00 23.75 ? 169 CYS A SG 1 ATOM 1159 N N . ALA A 1 144 ? 13.326 14.966 51.385 1.00 21.43 ? 170 ALA A N 1 ATOM 1160 C CA . ALA A 1 144 ? 14.398 14.928 52.365 1.00 24.61 ? 170 ALA A CA 1 ATOM 1161 C C . ALA A 1 144 ? 14.390 13.607 53.118 1.00 25.77 ? 170 ALA A C 1 ATOM 1162 O O . ALA A 1 144 ? 13.356 12.944 53.217 1.00 24.23 ? 170 ALA A O 1 ATOM 1163 C CB . ALA A 1 144 ? 14.256 16.089 53.337 1.00 28.74 ? 170 ALA A CB 1 ATOM 1164 N N . VAL A 1 145 ? 15.544 13.226 53.655 1.00 27.86 ? 171 VAL A N 1 ATOM 1165 C CA . VAL A 1 145 ? 15.624 12.015 54.460 1.00 28.68 ? 171 VAL A CA 1 ATOM 1166 C C . VAL A 1 145 ? 14.679 12.106 55.661 1.00 33.45 ? 171 VAL A C 1 ATOM 1167 O O . VAL A 1 145 ? 14.603 13.142 56.326 1.00 37.01 ? 171 VAL A O 1 ATOM 1168 C CB . VAL A 1 145 ? 17.080 11.731 54.907 1.00 38.39 ? 171 VAL A CB 1 ATOM 1169 C CG1 . VAL A 1 145 ? 17.621 12.867 55.766 1.00 43.51 ? 171 VAL A CG1 1 ATOM 1170 C CG2 . VAL A 1 145 ? 17.180 10.393 55.628 1.00 41.55 ? 171 VAL A CG2 1 ATOM 1171 N N . GLY A 1 146 ? 13.918 11.040 55.904 1.00 34.36 ? 172 GLY A N 1 ATOM 1172 C CA . GLY A 1 146 ? 12.944 11.044 56.983 1.00 34.26 ? 172 GLY A CA 1 ATOM 1173 C C . GLY A 1 146 ? 11.565 11.579 56.639 1.00 34.21 ? 172 GLY A C 1 ATOM 1174 O O . GLY A 1 146 ? 10.642 11.477 57.448 1.00 36.76 ? 172 GLY A O 1 ATOM 1175 N N . ALA A 1 147 ? 11.414 12.168 55.453 1.00 28.33 ? 173 ALA A N 1 ATOM 1176 C CA . ALA A 1 147 ? 10.121 12.694 55.023 1.00 26.95 ? 173 ALA A CA 1 ATOM 1177 C C . ALA A 1 147 ? 9.298 11.631 54.297 1.00 29.53 ? 173 ALA A C 1 ATOM 1178 O O . ALA A 1 147 ? 9.450 11.441 53.093 1.00 33.77 ? 173 ALA A O 1 ATOM 1179 C CB . ALA A 1 147 ? 10.316 13.900 54.125 1.00 28.57 ? 173 ALA A CB 1 ATOM 1180 N N . ALA A 1 148 ? 8.402 10.970 55.024 1.00 23.63 ? 174 ALA A N 1 ATOM 1181 C CA . ALA A 1 148 ? 7.657 9.833 54.489 1.00 19.86 ? 174 ALA A CA 1 ATOM 1182 C C . ALA A 1 148 ? 6.663 10.201 53.387 1.00 15.90 ? 174 ALA A C 1 ATOM 1183 O O . ALA A 1 148 ? 5.840 11.110 53.540 1.00 16.67 ? 174 ALA A O 1 ATOM 1184 C CB . ALA A 1 148 ? 6.935 9.103 55.613 1.00 22.54 ? 174 ALA A CB 1 ATOM 1185 N N . CYS A 1 149 ? 6.705 9.454 52.287 1.00 15.01 ? 175 CYS A N 1 ATOM 1186 C CA . CYS A 1 149 ? 5.675 9.572 51.263 1.00 13.96 ? 175 CYS A CA 1 ATOM 1187 C C . CYS A 1 149 ? 4.354 9.015 51.787 1.00 12.19 ? 175 CYS A C 1 ATOM 1188 O O . CYS A 1 149 ? 4.318 7.930 52.364 1.00 15.13 ? 175 CYS A O 1 ATOM 1189 C CB . CYS A 1 149 ? 6.093 8.837 49.993 1.00 15.70 ? 175 CYS A CB 1 ATOM 1190 S SG . CYS A 1 149 ? 7.387 9.755 49.068 1.00 20.48 ? 175 CYS A SG 1 ATOM 1191 N N . GLN A 1 150 ? 3.283 9.773 51.578 1.00 12.32 ? 176 GLN A N 1 ATOM 1192 C CA . GLN A 1 150 ? 1.943 9.414 52.019 1.00 11.36 ? 176 GLN A CA 1 ATOM 1193 C C . GLN A 1 150 ? 0.932 9.839 50.963 1.00 11.56 ? 176 GLN A C 1 ATOM 1194 O O . GLN A 1 150 ? 1.233 10.678 50.118 1.00 12.97 ? 176 GLN A O 1 ATOM 1195 C CB . GLN A 1 150 ? 1.598 10.120 53.346 1.00 12.05 ? 176 GLN A CB 1 ATOM 1196 C CG . GLN A 1 150 ? 2.545 9.868 54.523 1.00 12.08 ? 176 GLN A CG 1 ATOM 1197 C CD . GLN A 1 150 ? 2.393 8.496 55.136 1.00 14.41 ? 176 GLN A CD 1 ATOM 1198 O OE1 . GLN A 1 150 ? 1.889 7.571 54.494 1.00 15.44 ? 176 GLN A OE1 1 ATOM 1199 N NE2 . GLN A 1 150 ? 2.826 8.352 56.386 1.00 14.30 ? 176 GLN A NE2 1 ATOM 1200 N N . PRO A 1 151 ? -0.293 9.284 51.016 1.00 12.16 ? 177 PRO A N 1 ATOM 1201 C CA . PRO A 1 151 ? -1.343 9.802 50.127 1.00 13.65 ? 177 PRO A CA 1 ATOM 1202 C C . PRO A 1 151 ? -1.523 11.316 50.262 1.00 14.08 ? 177 PRO A C 1 ATOM 1203 O O . PRO A 1 151 ? -1.300 11.885 51.337 1.00 13.85 ? 177 PRO A O 1 ATOM 1204 C CB . PRO A 1 151 ? -2.596 9.078 50.620 1.00 14.49 ? 177 PRO A CB 1 ATOM 1205 C CG . PRO A 1 151 ? -2.091 7.814 51.214 1.00 14.44 ? 177 PRO A CG 1 ATOM 1206 C CD . PRO A 1 151 ? -0.778 8.172 51.859 1.00 14.03 ? 177 PRO A CD 1 ATOM 1207 N N . PHE A 1 152 ? -1.892 11.976 49.169 1.00 12.90 ? 178 PHE A N 1 ATOM 1208 C CA . PHE A 1 152 ? -2.031 13.426 49.176 1.00 14.50 ? 178 PHE A CA 1 ATOM 1209 C C . PHE A 1 152 ? -2.875 13.952 50.338 1.00 13.46 ? 178 PHE A C 1 ATOM 1210 O O . PHE A 1 152 ? -2.491 14.920 51.005 1.00 14.93 ? 178 PHE A O 1 ATOM 1211 C CB . PHE A 1 152 ? -2.639 13.911 47.861 1.00 17.36 ? 178 PHE A CB 1 ATOM 1212 C CG . PHE A 1 152 ? -1.763 14.881 47.121 1.00 17.86 ? 178 PHE A CG 1 ATOM 1213 C CD1 . PHE A 1 152 ? -0.606 14.433 46.490 1.00 17.19 ? 178 PHE A CD1 1 ATOM 1214 C CD2 . PHE A 1 152 ? -2.078 16.225 47.056 1.00 26.09 ? 178 PHE A CD2 1 ATOM 1215 C CE1 . PHE A 1 152 ? 0.224 15.303 45.810 1.00 20.22 ? 178 PHE A CE1 1 ATOM 1216 C CE2 . PHE A 1 152 ? -1.251 17.109 46.376 1.00 18.92 ? 178 PHE A CE2 1 ATOM 1217 C CZ . PHE A 1 152 ? -0.105 16.643 45.745 1.00 20.88 ? 178 PHE A CZ 1 ATOM 1218 N N . HIS A 1 153 ? -4.007 13.303 50.599 1.00 12.61 ? 179 HIS A N 1 ATOM 1219 C CA . HIS A 1 153 ? -4.886 13.755 51.671 1.00 14.89 ? 179 HIS A CA 1 ATOM 1220 C C . HIS A 1 153 ? -4.352 13.527 53.092 1.00 13.69 ? 179 HIS A C 1 ATOM 1221 O O . HIS A 1 153 ? -4.937 14.010 54.059 1.00 14.34 ? 179 HIS A O 1 ATOM 1222 C CB . HIS A 1 153 ? -6.287 13.172 51.490 1.00 12.41 ? 179 HIS A CB 1 ATOM 1223 C CG . HIS A 1 153 ? -6.976 13.674 50.259 1.00 13.77 ? 179 HIS A CG 1 ATOM 1224 N ND1 . HIS A 1 153 ? -8.215 13.221 49.862 1.00 14.31 ? 179 HIS A ND1 1 ATOM 1225 C CD2 . HIS A 1 153 ? -6.598 14.584 49.331 1.00 11.26 ? 179 HIS A CD2 1 ATOM 1226 C CE1 . HIS A 1 153 ? -8.573 13.830 48.744 1.00 15.57 ? 179 HIS A CE1 1 ATOM 1227 N NE2 . HIS A 1 153 ? -7.606 14.663 48.400 1.00 13.60 ? 179 HIS A NE2 1 ATOM 1228 N N . PHE A 1 154 ? -3.235 12.814 53.217 1.00 11.19 ? 180 PHE A N 1 ATOM 1229 C CA . PHE A 1 154 ? -2.553 12.689 54.498 1.00 12.31 ? 180 PHE A CA 1 ATOM 1230 C C . PHE A 1 154 ? -1.978 14.045 54.864 1.00 13.60 ? 180 PHE A C 1 ATOM 1231 O O . PHE A 1 154 ? -2.150 14.536 55.988 1.00 13.76 ? 180 PHE A O 1 ATOM 1232 C CB . PHE A 1 154 ? -1.449 11.637 54.396 1.00 13.44 ? 180 PHE A CB 1 ATOM 1233 C CG . PHE A 1 154 ? -0.660 11.433 55.673 1.00 13.30 ? 180 PHE A CG 1 ATOM 1234 C CD1 . PHE A 1 154 ? 0.368 12.314 56.023 1.00 12.50 ? 180 PHE A CD1 1 ATOM 1235 C CD2 . PHE A 1 154 ? -0.925 10.351 56.505 1.00 12.28 ? 180 PHE A CD2 1 ATOM 1236 C CE1 . PHE A 1 154 ? 1.101 12.121 57.184 1.00 14.42 ? 180 PHE A CE1 1 ATOM 1237 C CE2 . PHE A 1 154 ? -0.193 10.150 57.680 1.00 14.14 ? 180 PHE A CE2 1 ATOM 1238 C CZ . PHE A 1 154 ? 0.823 11.051 58.014 1.00 15.36 ? 180 PHE A CZ 1 ATOM 1239 N N . TYR A 1 155 ? -1.315 14.670 53.897 1.00 9.90 ? 181 TYR A N 1 ATOM 1240 C CA . TYR A 1 155 ? -0.664 15.951 54.144 1.00 12.73 ? 181 TYR A CA 1 ATOM 1241 C C . TYR A 1 155 ? -1.607 17.134 53.909 1.00 13.71 ? 181 TYR A C 1 ATOM 1242 O O . TYR A 1 155 ? -1.392 18.204 54.466 1.00 13.68 ? 181 TYR A O 1 ATOM 1243 C CB . TYR A 1 155 ? 0.606 16.088 53.294 1.00 12.98 ? 181 TYR A CB 1 ATOM 1244 C CG . TYR A 1 155 ? 1.743 15.254 53.822 1.00 12.13 ? 181 TYR A CG 1 ATOM 1245 C CD1 . TYR A 1 155 ? 2.369 15.579 55.017 1.00 15.52 ? 181 TYR A CD1 1 ATOM 1246 C CD2 . TYR A 1 155 ? 2.196 14.138 53.135 1.00 10.18 ? 181 TYR A CD2 1 ATOM 1247 C CE1 . TYR A 1 155 ? 3.411 14.809 55.522 1.00 15.57 ? 181 TYR A CE1 1 ATOM 1248 C CE2 . TYR A 1 155 ? 3.243 13.357 53.640 1.00 14.62 ? 181 TYR A CE2 1 ATOM 1249 C CZ . TYR A 1 155 ? 3.844 13.701 54.830 1.00 15.97 ? 181 TYR A CZ 1 ATOM 1250 O OH . TYR A 1 155 ? 4.882 12.945 55.335 1.00 16.90 ? 181 TYR A OH 1 ATOM 1251 N N . PHE A 1 156 ? -2.643 16.926 53.098 1.00 11.91 ? 182 PHE A N 1 ATOM 1252 C CA . PHE A 1 156 ? -3.642 17.963 52.797 1.00 9.68 ? 182 PHE A CA 1 ATOM 1253 C C . PHE A 1 156 ? -5.048 17.422 53.049 1.00 11.00 ? 182 PHE A C 1 ATOM 1254 O O . PHE A 1 156 ? -5.710 16.939 52.123 1.00 12.32 ? 182 PHE A O 1 ATOM 1255 C CB . PHE A 1 156 ? -3.529 18.390 51.336 1.00 12.46 ? 182 PHE A CB 1 ATOM 1256 C CG . PHE A 1 156 ? -2.158 18.857 50.951 1.00 11.18 ? 182 PHE A CG 1 ATOM 1257 C CD1 . PHE A 1 156 ? -1.643 20.028 51.480 1.00 11.00 ? 182 PHE A CD1 1 ATOM 1258 C CD2 . PHE A 1 156 ? -1.373 18.121 50.064 1.00 12.79 ? 182 PHE A CD2 1 ATOM 1259 C CE1 . PHE A 1 156 ? -0.375 20.462 51.132 1.00 13.20 ? 182 PHE A CE1 1 ATOM 1260 C CE2 . PHE A 1 156 ? -0.109 18.561 49.704 1.00 13.57 ? 182 PHE A CE2 1 ATOM 1261 C CZ . PHE A 1 156 ? 0.396 19.728 50.243 1.00 14.56 ? 182 PHE A CZ 1 ATOM 1262 N N . PRO A 1 157 ? -5.497 17.454 54.317 1.00 11.96 ? 183 PRO A N 1 ATOM 1263 C CA . PRO A 1 157 ? -6.728 16.717 54.648 1.00 13.94 ? 183 PRO A CA 1 ATOM 1264 C C . PRO A 1 157 ? -8.015 17.346 54.099 1.00 15.64 ? 183 PRO A C 1 ATOM 1265 O O . PRO A 1 157 ? -9.027 16.650 54.040 1.00 15.08 ? 183 PRO A O 1 ATOM 1266 C CB . PRO A 1 157 ? -6.747 16.724 56.178 1.00 14.50 ? 183 PRO A CB 1 ATOM 1267 C CG . PRO A 1 157 ? -5.319 16.921 56.579 1.00 17.54 ? 183 PRO A CG 1 ATOM 1268 C CD . PRO A 1 157 ? -4.752 17.848 55.525 1.00 15.16 ? 183 PRO A CD 1 ATOM 1269 N N . THR A 1 158 ? -7.991 18.632 53.740 1.00 13.32 ? 184 THR A N 1 ATOM 1270 C CA . THR A 1 158 ? -9.160 19.283 53.130 1.00 9.72 ? 184 THR A CA 1 ATOM 1271 C C . THR A 1 158 ? -8.689 20.135 51.968 1.00 10.43 ? 184 THR A C 1 ATOM 1272 O O . THR A 1 158 ? -7.505 20.432 51.884 1.00 11.78 ? 184 THR A O 1 ATOM 1273 C CB . THR A 1 158 ? -9.894 20.197 54.126 1.00 17.17 ? 184 THR A CB 1 ATOM 1274 O OG1 . THR A 1 158 ? -9.041 21.290 54.488 1.00 19.22 ? 184 THR A OG1 1 ATOM 1275 C CG2 . THR A 1 158 ? -10.295 19.424 55.369 1.00 21.33 ? 184 THR A CG2 1 ATOM 1276 N N . PRO A 1 159 ? -9.613 20.530 51.068 1.00 12.98 ? 185 PRO A N 1 ATOM 1277 C CA . PRO A 1 159 ? -9.202 21.437 49.993 1.00 10.60 ? 185 PRO A CA 1 ATOM 1278 C C . PRO A 1 159 ? -8.602 22.733 50.535 1.00 12.68 ? 185 PRO A C 1 ATOM 1279 O O . PRO A 1 159 ? -7.625 23.242 49.967 1.00 13.20 ? 185 PRO A O 1 ATOM 1280 C CB . PRO A 1 159 ? -10.520 21.747 49.288 1.00 13.70 ? 185 PRO A CB 1 ATOM 1281 C CG . PRO A 1 159 ? -11.312 20.451 49.444 1.00 17.54 ? 185 PRO A CG 1 ATOM 1282 C CD . PRO A 1 159 ? -10.973 19.989 50.845 1.00 15.26 ? 185 PRO A CD 1 ATOM 1283 N N . THR A 1 160 ? -9.172 23.277 51.610 1.00 12.68 ? 186 THR A N 1 ATOM 1284 C CA . THR A 1 160 ? -8.600 24.499 52.193 1.00 13.46 ? 186 THR A CA 1 ATOM 1285 C C . THR A 1 160 ? -7.127 24.335 52.585 1.00 14.38 ? 186 THR A C 1 ATOM 1286 O O . THR A 1 160 ? -6.292 25.185 52.258 1.00 12.48 ? 186 THR A O 1 ATOM 1287 C CB . THR A 1 160 ? -9.423 24.982 53.391 1.00 16.26 ? 186 THR A CB 1 ATOM 1288 O OG1 . THR A 1 160 ? -10.704 25.417 52.923 1.00 18.82 ? 186 THR A OG1 1 ATOM 1289 C CG2 . THR A 1 160 ? -8.727 26.146 54.098 1.00 16.92 ? 186 THR A CG2 1 ATOM 1290 N N . VAL A 1 161 ? -6.793 23.226 53.250 1.00 10.78 ? 187 VAL A N 1 ATOM 1291 C CA . VAL A 1 161 ? -5.417 22.965 53.623 1.00 10.88 ? 187 VAL A CA 1 ATOM 1292 C C . VAL A 1 161 ? -4.520 22.866 52.390 1.00 11.27 ? 187 VAL A C 1 ATOM 1293 O O . VAL A 1 161 ? -3.437 23.425 52.378 1.00 11.32 ? 187 VAL A O 1 ATOM 1294 C CB . VAL A 1 161 ? -5.293 21.676 54.464 1.00 13.94 ? 187 VAL A CB 1 ATOM 1295 C CG1 . VAL A 1 161 ? -3.836 21.412 54.818 1.00 15.75 ? 187 VAL A CG1 1 ATOM 1296 C CG2 . VAL A 1 161 ? -6.140 21.791 55.730 1.00 18.67 ? 187 VAL A CG2 1 ATOM 1297 N N . LEU A 1 162 ? -4.972 22.158 51.352 1.00 11.47 ? 188 LEU A N 1 ATOM 1298 C CA . LEU A 1 162 ? -4.177 22.048 50.125 1.00 11.25 ? 188 LEU A CA 1 ATOM 1299 C C . LEU A 1 162 ? -3.890 23.416 49.525 1.00 11.48 ? 188 LEU A C 1 ATOM 1300 O O . LEU A 1 162 ? -2.733 23.821 49.383 1.00 10.74 ? 188 LEU A O 1 ATOM 1301 C CB . LEU A 1 162 ? -4.873 21.174 49.079 1.00 11.49 ? 188 LEU A CB 1 ATOM 1302 C CG . LEU A 1 162 ? -4.238 21.238 47.678 1.00 11.86 ? 188 LEU A CG 1 ATOM 1303 C CD1 . LEU A 1 162 ? -2.835 20.651 47.725 1.00 14.00 ? 188 LEU A CD1 1 ATOM 1304 C CD2 . LEU A 1 162 ? -5.098 20.508 46.636 1.00 14.25 ? 188 LEU A CD2 1 ATOM 1305 N N . CYS A 1 163 ? -4.937 24.154 49.204 1.00 11.93 ? 189 CYS A N 1 ATOM 1306 C CA . CYS A 1 163 ? -4.741 25.382 48.442 1.00 12.60 ? 189 CYS A CA 1 ATOM 1307 C C . CYS A 1 163 ? -4.018 26.452 49.245 1.00 12.93 ? 189 CYS A C 1 ATOM 1308 O O . CYS A 1 163 ? -3.189 27.174 48.699 1.00 12.32 ? 189 CYS A O 1 ATOM 1309 C CB . CYS A 1 163 ? -6.077 25.885 47.919 1.00 13.90 ? 189 CYS A CB 1 ATOM 1310 S SG . CYS A 1 163 ? -6.907 24.585 46.991 1.00 18.41 ? 189 CYS A SG 1 ATOM 1311 N N . ASN A 1 164 ? -4.310 26.534 50.536 1.00 12.50 ? 190 ASN A N 1 ATOM 1312 C CA . ASN A 1 164 ? -3.723 27.576 51.362 1.00 12.87 ? 190 ASN A CA 1 ATOM 1313 C C . ASN A 1 164 ? -2.311 27.247 51.837 1.00 12.81 ? 190 ASN A C 1 ATOM 1314 O O . ASN A 1 164 ? -1.484 28.146 51.959 1.00 12.95 ? 190 ASN A O 1 ATOM 1315 C CB . ASN A 1 164 ? -4.625 27.886 52.561 1.00 13.62 ? 190 ASN A CB 1 ATOM 1316 C CG . ASN A 1 164 ? -5.948 28.501 52.161 1.00 13.42 ? 190 ASN A CG 1 ATOM 1317 O OD1 . ASN A 1 164 ? -6.302 28.565 50.976 1.00 14.04 ? 190 ASN A OD1 1 ATOM 1318 N ND2 . ASN A 1 164 ? -6.690 28.962 53.155 1.00 15.03 ? 190 ASN A ND2 1 ATOM 1319 N N . GLU A 1 165 ? -2.013 25.970 52.093 1.00 10.96 ? 191 GLU A N 1 ATOM 1320 C CA . GLU A 1 165 ? -0.718 25.641 52.688 1.00 10.47 ? 191 GLU A CA 1 ATOM 1321 C C . GLU A 1 165 ? 0.347 25.228 51.690 1.00 9.64 ? 191 GLU A C 1 ATOM 1322 O O . GLU A 1 165 ? 1.523 25.400 51.974 1.00 11.75 ? 191 GLU A O 1 ATOM 1323 C CB . GLU A 1 165 ? -0.885 24.531 53.735 1.00 16.13 ? 191 GLU A CB 1 ATOM 1324 C CG . GLU A 1 165 ? -1.867 24.857 54.853 1.00 23.80 ? 191 GLU A CG 1 ATOM 1325 C CD . GLU A 1 165 ? -1.316 25.831 55.866 1.00 36.98 ? 191 GLU A CD 1 ATOM 1326 O OE1 . GLU A 1 165 ? -0.129 25.697 56.235 1.00 43.88 ? 191 GLU A OE1 1 ATOM 1327 O OE2 . GLU A 1 165 ? -2.070 26.730 56.301 1.00 37.74 ? 191 GLU A OE2 1 ATOM 1328 N N . ILE A 1 166 ? -0.045 24.682 50.541 1.00 10.39 ? 192 ILE A N 1 ATOM 1329 C CA . ILE A 1 166 ? 0.948 24.096 49.631 1.00 10.34 ? 192 ILE A CA 1 ATOM 1330 C C . ILE A 1 166 ? 2.028 25.104 49.210 1.00 12.05 ? 192 ILE A C 1 ATOM 1331 O O . ILE A 1 166 ? 3.217 24.779 49.168 1.00 12.20 ? 192 ILE A O 1 ATOM 1332 C CB . ILE A 1 166 ? 0.306 23.383 48.420 1.00 11.95 ? 192 ILE A CB 1 ATOM 1333 C CG1 . ILE A 1 166 ? 1.366 22.554 47.686 1.00 13.93 ? 192 ILE A CG1 1 ATOM 1334 C CG2 . ILE A 1 166 ? -0.362 24.377 47.473 1.00 12.69 ? 192 ILE A CG2 1 ATOM 1335 C CD1 . ILE A 1 166 ? 0.777 21.470 46.794 1.00 14.02 ? 192 ILE A CD1 1 ATOM 1336 N N . TRP A 1 167 ? 1.614 26.338 48.937 1.00 10.49 ? 193 TRP A N 1 ATOM 1337 C CA . TRP A 1 167 ? 2.549 27.414 48.617 1.00 12.89 ? 193 TRP A CA 1 ATOM 1338 C C . TRP A 1 167 ? 2.564 28.512 49.684 1.00 13.43 ? 193 TRP A C 1 ATOM 1339 O O . TRP A 1 167 ? 2.661 29.701 49.359 1.00 13.26 ? 193 TRP A O 1 ATOM 1340 C CB . TRP A 1 167 ? 2.229 28.003 47.240 1.00 11.66 ? 193 TRP A CB 1 ATOM 1341 C CG . TRP A 1 167 ? 2.267 26.985 46.106 1.00 11.20 ? 193 TRP A CG 1 ATOM 1342 C CD1 . TRP A 1 167 ? 1.251 26.674 45.261 1.00 13.69 ? 193 TRP A CD1 1 ATOM 1343 C CD2 . TRP A 1 167 ? 3.385 26.162 45.713 1.00 14.84 ? 193 TRP A CD2 1 ATOM 1344 N NE1 . TRP A 1 167 ? 1.663 25.713 44.359 1.00 13.23 ? 193 TRP A NE1 1 ATOM 1345 C CE2 . TRP A 1 167 ? 2.967 25.382 44.619 1.00 16.36 ? 193 TRP A CE2 1 ATOM 1346 C CE3 . TRP A 1 167 ? 4.690 26.009 46.184 1.00 15.36 ? 193 TRP A CE3 1 ATOM 1347 C CZ2 . TRP A 1 167 ? 3.815 24.459 43.985 1.00 16.96 ? 193 TRP A CZ2 1 ATOM 1348 C CZ3 . TRP A 1 167 ? 5.534 25.109 45.545 1.00 15.18 ? 193 TRP A CZ3 1 ATOM 1349 C CH2 . TRP A 1 167 ? 5.091 24.348 44.461 1.00 14.23 ? 193 TRP A CH2 1 ATOM 1350 N N . THR A 1 168 ? 2.468 28.106 50.948 1.00 14.59 ? 194 THR A N 1 ATOM 1351 C CA . THR A 1 168 ? 2.659 29.010 52.090 1.00 14.21 ? 194 THR A CA 1 ATOM 1352 C C . THR A 1 168 ? 1.820 30.277 51.969 1.00 12.67 ? 194 THR A C 1 ATOM 1353 O O . THR A 1 168 ? 2.349 31.386 51.926 1.00 13.77 ? 194 THR A O 1 ATOM 1354 C CB . THR A 1 168 ? 4.135 29.408 52.256 1.00 23.28 ? 194 THR A CB 1 ATOM 1355 O OG1 . THR A 1 168 ? 4.960 28.266 52.002 1.00 26.52 ? 194 THR A OG1 1 ATOM 1356 C CG2 . THR A 1 168 ? 4.404 29.936 53.676 1.00 21.36 ? 194 THR A CG2 1 ATOM 1357 N N . HIS A 1 169 ? 0.511 30.069 51.873 1.00 12.85 ? 195 HIS A N 1 ATOM 1358 C CA . HIS A 1 169 ? -0.467 31.159 51.826 1.00 13.26 ? 195 HIS A CA 1 ATOM 1359 C C . HIS A 1 169 ? -0.416 32.023 50.574 1.00 13.44 ? 195 HIS A C 1 ATOM 1360 O O . HIS A 1 169 ? -0.942 33.140 50.585 1.00 13.63 ? 195 HIS A O 1 ATOM 1361 C CB . HIS A 1 169 ? -0.412 31.989 53.107 1.00 16.16 ? 195 HIS A CB 1 ATOM 1362 C CG . HIS A 1 169 ? -0.698 31.178 54.339 1.00 27.32 ? 195 HIS A CG 1 ATOM 1363 N ND1 . HIS A 1 169 ? -1.954 30.673 54.609 1.00 27.36 ? 195 HIS A ND1 1 ATOM 1364 C CD2 . HIS A 1 169 ? 0.113 30.750 55.324 1.00 34.72 ? 195 HIS A CD2 1 ATOM 1365 C CE1 . HIS A 1 169 ? -1.901 29.982 55.736 1.00 32.27 ? 195 HIS A CE1 1 ATOM 1366 N NE2 . HIS A 1 169 ? -0.668 30.004 56.192 1.00 36.76 ? 195 HIS A NE2 1 ATOM 1367 N N . SER A 1 170 ? 0.188 31.509 49.496 1.00 11.72 ? 196 SER A N 1 ATOM 1368 C CA . SER A 1 170 ? 0.075 32.173 48.190 1.00 11.57 ? 196 SER A CA 1 ATOM 1369 C C . SER A 1 170 ? -1.391 32.305 47.784 1.00 12.32 ? 196 SER A C 1 ATOM 1370 O O . SER A 1 170 ? -1.808 33.341 47.235 1.00 12.67 ? 196 SER A O 1 ATOM 1371 C CB . SER A 1 170 ? 0.855 31.429 47.109 1.00 12.78 ? 196 SER A CB 1 ATOM 1372 O OG . SER A 1 170 ? 2.251 31.473 47.344 1.00 14.26 ? 196 SER A OG 1 ATOM 1373 N N . TYR A 1 171 ? -2.158 31.244 48.021 1.00 11.32 ? 197 TYR A N 1 ATOM 1374 C CA . TYR A 1 171 ? -3.606 31.295 47.851 1.00 10.49 ? 197 TYR A CA 1 ATOM 1375 C C . TYR A 1 171 ? -4.312 31.351 49.192 1.00 9.95 ? 197 TYR A C 1 ATOM 1376 O O . TYR A 1 171 ? -3.844 30.800 50.185 1.00 10.59 ? 197 TYR A O 1 ATOM 1377 C CB . TYR A 1 171 ? -4.124 30.037 47.165 1.00 11.42 ? 197 TYR A CB 1 ATOM 1378 C CG . TYR A 1 171 ? -3.632 29.788 45.768 1.00 14.75 ? 197 TYR A CG 1 ATOM 1379 C CD1 . TYR A 1 171 ? -3.963 30.641 44.729 1.00 16.53 ? 197 TYR A CD1 1 ATOM 1380 C CD2 . TYR A 1 171 ? -2.886 28.647 45.474 1.00 16.97 ? 197 TYR A CD2 1 ATOM 1381 C CE1 . TYR A 1 171 ? -3.523 30.394 43.440 1.00 19.53 ? 197 TYR A CE1 1 ATOM 1382 C CE2 . TYR A 1 171 ? -2.454 28.390 44.186 1.00 16.70 ? 197 TYR A CE2 1 ATOM 1383 C CZ . TYR A 1 171 ? -2.780 29.263 43.178 1.00 20.37 ? 197 TYR A CZ 1 ATOM 1384 O OH . TYR A 1 171 ? -2.347 29.005 41.896 1.00 23.52 ? 197 TYR A OH 1 ATOM 1385 N N . LYS A 1 172 ? -5.478 31.980 49.190 1.00 11.26 ? 198 LYS A N 1 ATOM 1386 C CA . LYS A 1 172 ? -6.445 31.843 50.276 1.00 12.28 ? 198 LYS A CA 1 ATOM 1387 C C . LYS A 1 172 ? -7.737 31.507 49.580 1.00 13.66 ? 198 LYS A C 1 ATOM 1388 O O . LYS A 1 172 ? -8.366 32.391 49.006 1.00 15.23 ? 198 LYS A O 1 ATOM 1389 C CB . LYS A 1 172 ? -6.604 33.153 51.046 1.00 15.39 ? 198 LYS A CB 1 ATOM 1390 C CG . LYS A 1 172 ? -7.564 33.042 52.232 1.00 19.28 ? 198 LYS A CG 1 ATOM 1391 C CD . LYS A 1 172 ? -7.430 34.258 53.141 1.00 24.05 ? 198 LYS A CD 1 ATOM 1392 C CE . LYS A 1 172 ? -7.843 33.926 54.559 1.00 35.83 ? 198 LYS A CE 1 ATOM 1393 N NZ . LYS A 1 172 ? -9.159 33.237 54.577 1.00 44.64 ? 198 LYS A NZ 1 ATOM 1394 N N . VAL A 1 173 ? -8.129 30.233 49.598 1.00 12.17 ? 199 VAL A N 1 ATOM 1395 C CA . VAL A 1 173 ? -9.296 29.838 48.818 1.00 13.05 ? 199 VAL A CA 1 ATOM 1396 C C . VAL A 1 173 ? -10.537 30.648 49.199 1.00 13.41 ? 199 VAL A C 1 ATOM 1397 O O . VAL A 1 173 ? -10.804 30.901 50.383 1.00 14.74 ? 199 VAL A O 1 ATOM 1398 C CB . VAL A 1 173 ? -9.568 28.323 48.896 1.00 12.13 ? 199 VAL A CB 1 ATOM 1399 C CG1 . VAL A 1 173 ? -9.703 27.868 50.327 1.00 15.28 ? 199 VAL A CG1 1 ATOM 1400 C CG2 . VAL A 1 173 ? -10.797 27.957 48.089 1.00 12.57 ? 199 VAL A CG2 1 ATOM 1401 N N . SER A 1 174 ? -11.265 31.091 48.176 1.00 13.79 ? 200 SER A N 1 ATOM 1402 C CA . SER A 1 174 ? -12.431 31.945 48.350 1.00 14.03 ? 200 SER A CA 1 ATOM 1403 C C . SER A 1 174 ? -13.683 31.137 48.641 1.00 17.30 ? 200 SER A C 1 ATOM 1404 O O . SER A 1 174 ? -13.758 29.949 48.305 1.00 17.24 ? 200 SER A O 1 ATOM 1405 C CB . SER A 1 174 ? -12.640 32.755 47.073 1.00 13.97 ? 200 SER A CB 1 ATOM 1406 O OG . SER A 1 174 ? -13.663 33.718 47.222 1.00 15.01 ? 200 SER A OG 1 ATOM 1407 N N . ASN A 1 175 ? -14.670 31.771 49.268 1.00 17.05 ? 201 ASN A N 1 ATOM 1408 C CA . ASN A 1 175 ? -15.990 31.163 49.340 1.00 18.72 ? 201 ASN A CA 1 ATOM 1409 C C . ASN A 1 175 ? -16.766 31.448 48.053 1.00 18.42 ? 201 ASN A C 1 ATOM 1410 O O . ASN A 1 175 ? -17.853 30.898 47.841 1.00 18.96 ? 201 ASN A O 1 ATOM 1411 C CB . ASN A 1 175 ? -16.772 31.598 50.598 1.00 22.96 ? 201 ASN A CB 1 ATOM 1412 C CG . ASN A 1 175 ? -17.045 33.092 50.653 1.00 28.18 ? 201 ASN A CG 1 ATOM 1413 O OD1 . ASN A 1 175 ? -16.262 33.905 50.162 1.00 28.47 ? 201 ASN A OD1 1 ATOM 1414 N ND2 . ASN A 1 175 ? -18.172 33.462 51.263 1.00 32.75 ? 201 ASN A ND2 1 ATOM 1415 N N . TYR A 1 176 ? -16.202 32.296 47.190 1.00 18.46 ? 202 TYR A N 1 ATOM 1416 C CA . TYR A 1 176 ? -16.829 32.628 45.906 1.00 17.79 ? 202 TYR A CA 1 ATOM 1417 C C . TYR A 1 176 ? -16.463 31.612 44.828 1.00 16.96 ? 202 TYR A C 1 ATOM 1418 O O . TYR A 1 176 ? -15.436 30.951 44.920 1.00 17.46 ? 202 TYR A O 1 ATOM 1419 C CB . TYR A 1 176 ? -16.409 34.013 45.441 1.00 20.20 ? 202 TYR A CB 1 ATOM 1420 C CG . TYR A 1 176 ? -17.187 35.125 46.078 1.00 22.40 ? 202 TYR A CG 1 ATOM 1421 C CD1 . TYR A 1 176 ? -18.461 35.445 45.624 1.00 22.54 ? 202 TYR A CD1 1 ATOM 1422 C CD2 . TYR A 1 176 ? -16.647 35.877 47.117 1.00 25.46 ? 202 TYR A CD2 1 ATOM 1423 C CE1 . TYR A 1 176 ? -19.186 36.468 46.198 1.00 28.67 ? 202 TYR A CE1 1 ATOM 1424 C CE2 . TYR A 1 176 ? -17.374 36.907 47.699 1.00 29.62 ? 202 TYR A CE2 1 ATOM 1425 C CZ . TYR A 1 176 ? -18.641 37.195 47.231 1.00 33.96 ? 202 TYR A CZ 1 ATOM 1426 O OH . TYR A 1 176 ? -19.374 38.218 47.801 1.00 39.94 ? 202 TYR A OH 1 ATOM 1427 N N . SER A 1 177 ? -17.315 31.491 43.813 1.00 17.03 ? 203 SER A N 1 ATOM 1428 C CA . SER A 1 177 ? -17.101 30.510 42.754 1.00 17.65 ? 203 SER A CA 1 ATOM 1429 C C . SER A 1 177 ? -16.847 31.201 41.422 1.00 16.32 ? 203 SER A C 1 ATOM 1430 O O . SER A 1 177 ? -17.066 32.401 41.290 1.00 17.66 ? 203 SER A O 1 ATOM 1431 C CB . SER A 1 177 ? -18.306 29.573 42.620 1.00 21.29 ? 203 SER A CB 1 ATOM 1432 O OG . SER A 1 177 ? -18.484 28.786 43.782 1.00 26.16 ? 203 SER A OG 1 ATOM 1433 N N . ARG A 1 178 ? -16.424 30.429 40.427 1.00 19.00 ? 204 ARG A N 1 ATOM 1434 C CA . ARG A 1 178 ? -16.202 30.966 39.090 1.00 17.89 ? 204 ARG A CA 1 ATOM 1435 C C . ARG A 1 178 ? -17.435 31.720 38.596 1.00 15.50 ? 204 ARG A C 1 ATOM 1436 O O . ARG A 1 178 ? -18.562 31.349 38.913 1.00 16.68 ? 204 ARG A O 1 ATOM 1437 C CB . ARG A 1 178 ? -15.895 29.832 38.121 1.00 20.19 ? 204 ARG A CB 1 ATOM 1438 C CG . ARG A 1 178 ? -14.513 29.228 38.317 1.00 20.44 ? 204 ARG A CG 1 ATOM 1439 C CD . ARG A 1 178 ? -14.203 28.250 37.191 1.00 23.76 ? 204 ARG A CD 1 ATOM 1440 N NE . ARG A 1 178 ? -12.797 27.855 37.204 1.00 22.75 ? 204 ARG A NE 1 ATOM 1441 C CZ . ARG A 1 178 ? -12.159 27.322 36.167 1.00 29.25 ? 204 ARG A CZ 1 ATOM 1442 N NH1 . ARG A 1 178 ? -12.792 27.130 35.016 1.00 29.81 ? 204 ARG A NH1 1 ATOM 1443 N NH2 . ARG A 1 178 ? -10.877 26.992 36.280 1.00 28.66 ? 204 ARG A NH2 1 ATOM 1444 N N . GLY A 1 179 ? -17.205 32.797 37.849 1.00 17.36 ? 205 GLY A N 1 ATOM 1445 C CA . GLY A 1 179 ? -18.295 33.559 37.272 1.00 20.16 ? 205 GLY A CA 1 ATOM 1446 C C . GLY A 1 179 ? -18.789 34.700 38.143 1.00 20.72 ? 205 GLY A C 1 ATOM 1447 O O . GLY A 1 179 ? -19.608 35.500 37.693 1.00 22.53 ? 205 GLY A O 1 ATOM 1448 N N . SER A 1 180 ? -18.286 34.781 39.375 1.00 15.66 ? 206 SER A N 1 ATOM 1449 C CA . SER A 1 180 ? -18.723 35.797 40.334 1.00 18.72 ? 206 SER A CA 1 ATOM 1450 C C . SER A 1 180 ? -17.984 37.123 40.150 1.00 17.29 ? 206 SER A C 1 ATOM 1451 O O . SER A 1 180 ? -18.430 38.170 40.636 1.00 18.65 ? 206 SER A O 1 ATOM 1452 C CB . SER A 1 180 ? -18.508 35.302 41.764 1.00 15.63 ? 206 SER A CB 1 ATOM 1453 O OG . SER A 1 180 ? -17.132 35.100 42.038 1.00 18.56 ? 206 SER A OG 1 ATOM 1454 N N . GLY A 1 181 ? -16.848 37.054 39.460 1.00 16.66 ? 207 GLY A N 1 ATOM 1455 C CA . GLY A 1 181 ? -15.943 38.182 39.337 1.00 17.22 ? 207 GLY A CA 1 ATOM 1456 C C . GLY A 1 181 ? -15.236 38.505 40.642 1.00 15.73 ? 207 GLY A C 1 ATOM 1457 O O . GLY A 1 181 ? -14.708 39.615 40.800 1.00 19.73 ? 207 GLY A O 1 ATOM 1458 N N . ARG A 1 182 ? -15.214 37.555 41.573 1.00 14.43 ? 208 ARG A N 1 ATOM 1459 C CA . ARG A 1 182 ? -14.637 37.819 42.888 1.00 14.58 ? 208 ARG A CA 1 ATOM 1460 C C . ARG A 1 182 ? -13.634 36.767 43.310 1.00 12.43 ? 208 ARG A C 1 ATOM 1461 O O . ARG A 1 182 ? -13.197 36.742 44.464 1.00 17.48 ? 208 ARG A O 1 ATOM 1462 C CB . ARG A 1 182 ? -15.732 37.996 43.935 1.00 19.51 ? 208 ARG A CB 1 ATOM 1463 C CG . ARG A 1 182 ? -16.559 39.235 43.634 1.00 22.04 ? 208 ARG A CG 1 ATOM 1464 C CD . ARG A 1 182 ? -17.792 39.397 44.474 1.00 29.93 ? 208 ARG A CD 1 ATOM 1465 N NE . ARG A 1 182 ? -18.610 40.487 43.936 1.00 30.89 ? 208 ARG A NE 1 ATOM 1466 C CZ . ARG A 1 182 ? -19.537 41.137 44.626 1.00 33.06 ? 208 ARG A CZ 1 ATOM 1467 N NH1 . ARG A 1 182 ? -19.761 40.819 45.891 1.00 36.70 ? 208 ARG A NH1 1 ATOM 1468 N NH2 . ARG A 1 182 ? -20.231 42.115 44.054 1.00 36.33 ? 208 ARG A NH2 1 ATOM 1469 N N . CYS A 1 183 ? -13.255 35.901 42.378 1.00 12.41 ? 209 CYS A N 1 ATOM 1470 C CA . CYS A 1 183 ? -12.195 34.954 42.663 1.00 13.70 ? 209 CYS A CA 1 ATOM 1471 C C . CYS A 1 183 ? -11.372 34.684 41.413 1.00 11.06 ? 209 CYS A C 1 ATOM 1472 O O . CYS A 1 183 ? -11.870 34.813 40.283 1.00 11.97 ? 209 CYS A O 1 ATOM 1473 C CB . CYS A 1 183 ? -12.770 33.657 43.222 1.00 13.49 ? 209 CYS A CB 1 ATOM 1474 S SG . CYS A 1 183 ? -13.991 32.852 42.150 1.00 17.44 ? 209 CYS A SG 1 ATOM 1475 N N . ILE A 1 184 ? -10.121 34.297 41.643 1.00 12.77 ? 210 ILE A N 1 ATOM 1476 C CA . ILE A 1 184 ? -9.165 34.032 40.579 1.00 14.33 ? 210 ILE A CA 1 ATOM 1477 C C . ILE A 1 184 ? -9.251 32.577 40.161 1.00 13.16 ? 210 ILE A C 1 ATOM 1478 O O . ILE A 1 184 ? -9.205 31.667 41.006 1.00 14.28 ? 210 ILE A O 1 ATOM 1479 C CB . ILE A 1 184 ? -7.751 34.327 41.082 1.00 12.46 ? 210 ILE A CB 1 ATOM 1480 C CG1 . ILE A 1 184 ? -7.590 35.832 41.304 1.00 13.41 ? 210 ILE A CG1 1 ATOM 1481 C CG2 . ILE A 1 184 ? -6.675 33.750 40.128 1.00 13.62 ? 210 ILE A CG2 1 ATOM 1482 C CD1 . ILE A 1 184 ? -7.615 36.665 40.019 1.00 12.63 ? 210 ILE A CD1 1 ATOM 1483 N N . GLN A 1 185 ? -9.378 32.333 38.863 1.00 12.18 ? 211 GLN A N 1 ATOM 1484 C CA . GLN A 1 185 ? -9.353 30.961 38.392 1.00 15.10 ? 211 GLN A CA 1 ATOM 1485 C C . GLN A 1 185 ? -8.025 30.604 37.732 1.00 11.20 ? 211 GLN A C 1 ATOM 1486 O O . GLN A 1 185 ? -7.338 31.485 37.177 1.00 14.47 ? 211 GLN A O 1 ATOM 1487 C CB . GLN A 1 185 ? -10.519 30.686 37.464 1.00 22.48 ? 211 GLN A CB 1 ATOM 1488 C CG . GLN A 1 185 ? -10.622 31.615 36.307 1.00 23.02 ? 211 GLN A CG 1 ATOM 1489 C CD . GLN A 1 185 ? -11.971 31.488 35.643 1.00 26.53 ? 211 GLN A CD 1 ATOM 1490 O OE1 . GLN A 1 185 ? -12.899 32.233 35.959 1.00 30.45 ? 211 GLN A OE1 1 ATOM 1491 N NE2 . GLN A 1 185 ? -12.090 30.544 34.715 1.00 24.53 ? 211 GLN A NE2 1 ATOM 1492 N N . MET A 1 186 ? -7.690 29.316 37.763 1.00 13.48 ? 212 MET A N 1 ATOM 1493 C CA . MET A 1 186 ? -6.366 28.854 37.371 1.00 15.86 ? 212 MET A CA 1 ATOM 1494 C C . MET A 1 186 ? -6.234 28.582 35.878 1.00 18.64 ? 212 MET A C 1 ATOM 1495 O O . MET A 1 186 ? -5.131 28.304 35.398 1.00 20.51 ? 212 MET A O 1 ATOM 1496 C CB . MET A 1 186 ? -6.012 27.582 38.155 1.00 18.40 ? 212 MET A CB 1 ATOM 1497 C CG . MET A 1 186 ? -6.226 27.760 39.651 1.00 23.29 ? 212 MET A CG 1 ATOM 1498 S SD . MET A 1 186 ? -5.930 26.282 40.618 1.00 36.04 ? 212 MET A SD 1 ATOM 1499 C CE . MET A 1 186 ? -4.567 25.758 39.657 1.00 17.76 ? 212 MET A CE 1 ATOM 1500 N N . TRP A 1 187 ? -7.353 28.606 35.159 1.00 15.69 ? 213 TRP A N 1 ATOM 1501 C CA . TRP A 1 187 ? -7.354 28.345 33.719 1.00 15.22 ? 213 TRP A CA 1 ATOM 1502 C C . TRP A 1 187 ? -8.622 28.951 33.153 1.00 18.35 ? 213 TRP A C 1 ATOM 1503 O O . TRP A 1 187 ? -9.572 29.225 33.904 1.00 20.23 ? 213 TRP A O 1 ATOM 1504 C CB . TRP A 1 187 ? -7.366 26.843 33.462 1.00 16.57 ? 213 TRP A CB 1 ATOM 1505 C CG . TRP A 1 187 ? -6.780 26.362 32.135 1.00 19.19 ? 213 TRP A CG 1 ATOM 1506 C CD1 . TRP A 1 187 ? -7.476 25.940 31.035 1.00 20.81 ? 213 TRP A CD1 1 ATOM 1507 C CD2 . TRP A 1 187 ? -5.387 26.209 31.807 1.00 17.39 ? 213 TRP A CD2 1 ATOM 1508 N NE1 . TRP A 1 187 ? -6.602 25.538 30.047 1.00 24.91 ? 213 TRP A NE1 1 ATOM 1509 C CE2 . TRP A 1 187 ? -5.315 25.698 30.497 1.00 21.86 ? 213 TRP A CE2 1 ATOM 1510 C CE3 . TRP A 1 187 ? -4.195 26.470 32.492 1.00 16.83 ? 213 TRP A CE3 1 ATOM 1511 C CZ2 . TRP A 1 187 ? -4.094 25.420 29.865 1.00 22.20 ? 213 TRP A CZ2 1 ATOM 1512 C CZ3 . TRP A 1 187 ? -2.995 26.192 31.875 1.00 18.36 ? 213 TRP A CZ3 1 ATOM 1513 C CH2 . TRP A 1 187 ? -2.946 25.675 30.574 1.00 21.85 ? 213 TRP A CH2 1 ATOM 1514 N N . PHE A 1 188 ? -8.638 29.179 31.843 1.00 20.30 ? 214 PHE A N 1 ATOM 1515 C CA . PHE A 1 188 ? -9.823 29.713 31.162 1.00 21.57 ? 214 PHE A CA 1 ATOM 1516 C C . PHE A 1 188 ? -9.659 29.551 29.655 1.00 20.89 ? 214 PHE A C 1 ATOM 1517 O O . PHE A 1 188 ? -8.559 29.285 29.170 1.00 20.42 ? 214 PHE A O 1 ATOM 1518 C CB . PHE A 1 188 ? -10.059 31.194 31.512 1.00 18.96 ? 214 PHE A CB 1 ATOM 1519 C CG . PHE A 1 188 ? -8.881 32.082 31.228 1.00 16.68 ? 214 PHE A CG 1 ATOM 1520 C CD1 . PHE A 1 188 ? -7.899 32.281 32.190 1.00 18.66 ? 214 PHE A CD1 1 ATOM 1521 C CD2 . PHE A 1 188 ? -8.747 32.716 30.003 1.00 19.39 ? 214 PHE A CD2 1 ATOM 1522 C CE1 . PHE A 1 188 ? -6.807 33.083 31.935 1.00 19.01 ? 214 PHE A CE1 1 ATOM 1523 C CE2 . PHE A 1 188 ? -7.660 33.527 29.737 1.00 22.66 ? 214 PHE A CE2 1 ATOM 1524 C CZ . PHE A 1 188 ? -6.689 33.710 30.703 1.00 22.33 ? 214 PHE A CZ 1 ATOM 1525 N N . ASP A 1 189 ? -10.755 29.698 28.914 1.00 27.02 ? 215 ASP A N 1 ATOM 1526 C CA . ASP A 1 189 ? -10.684 29.752 27.455 1.00 29.92 ? 215 ASP A CA 1 ATOM 1527 C C . ASP A 1 189 ? -10.471 31.214 27.102 1.00 30.39 ? 215 ASP A C 1 ATOM 1528 O O . ASP A 1 189 ? -11.291 32.065 27.451 1.00 35.47 ? 215 ASP A O 1 ATOM 1529 C CB . ASP A 1 189 ? -11.979 29.222 26.827 1.00 35.63 ? 215 ASP A CB 1 ATOM 1530 C CG . ASP A 1 189 ? -11.941 29.201 25.298 1.00 43.57 ? 215 ASP A CG 1 ATOM 1531 O OD1 . ASP A 1 189 ? -11.257 30.047 24.686 1.00 43.80 ? 215 ASP A OD1 1 ATOM 1532 O OD2 . ASP A 1 189 ? -12.615 28.329 24.702 1.00 47.68 ? 215 ASP A OD2 1 ATOM 1533 N N . PRO A 1 190 ? -9.358 31.520 26.424 1.00 29.44 ? 216 PRO A N 1 ATOM 1534 C CA . PRO A 1 190 ? -9.069 32.928 26.135 1.00 30.62 ? 216 PRO A CA 1 ATOM 1535 C C . PRO A 1 190 ? -9.987 33.531 25.067 1.00 35.96 ? 216 PRO A C 1 ATOM 1536 O O . PRO A 1 190 ? -10.223 34.738 25.097 1.00 37.51 ? 216 PRO A O 1 ATOM 1537 C CB . PRO A 1 190 ? -7.609 32.898 25.653 1.00 32.55 ? 216 PRO A CB 1 ATOM 1538 C CG . PRO A 1 190 ? -7.410 31.504 25.117 1.00 31.71 ? 216 PRO A CG 1 ATOM 1539 C CD . PRO A 1 190 ? -8.276 30.619 25.984 1.00 31.30 ? 216 PRO A CD 1 ATOM 1540 N N . ALA A 1 191 ? -10.498 32.712 24.150 1.00 40.51 ? 217 ALA A N 1 ATOM 1541 C CA . ALA A 1 191 ? -11.410 33.195 23.108 1.00 44.46 ? 217 ALA A CA 1 ATOM 1542 C C . ALA A 1 191 ? -12.730 33.691 23.692 1.00 46.70 ? 217 ALA A C 1 ATOM 1543 O O . ALA A 1 191 ? -13.466 34.442 23.049 1.00 48.28 ? 217 ALA A O 1 ATOM 1544 C CB . ALA A 1 191 ? -11.667 32.107 22.073 1.00 48.24 ? 217 ALA A CB 1 ATOM 1545 N N . GLN A 1 192 ? -13.023 33.255 24.912 1.00 46.24 ? 218 GLN A N 1 ATOM 1546 C CA . GLN A 1 192 ? -14.255 33.620 25.589 1.00 50.34 ? 218 GLN A CA 1 ATOM 1547 C C . GLN A 1 192 ? -13.958 34.695 26.628 1.00 49.77 ? 218 GLN A C 1 ATOM 1548 O O . GLN A 1 192 ? -14.856 35.178 27.320 1.00 52.46 ? 218 GLN A O 1 ATOM 1549 C CB . GLN A 1 192 ? -14.873 32.374 26.224 1.00 54.56 ? 218 GLN A CB 1 ATOM 1550 C CG . GLN A 1 192 ? -14.881 31.180 25.266 1.00 61.96 ? 218 GLN A CG 1 ATOM 1551 C CD . GLN A 1 192 ? -15.510 29.934 25.854 1.00 65.20 ? 218 GLN A CD 1 ATOM 1552 O OE1 . GLN A 1 192 ? -15.301 29.604 27.024 1.00 63.92 ? 218 GLN A OE1 1 ATOM 1553 N NE2 . GLN A 1 192 ? -16.286 29.228 25.038 1.00 67.82 ? 218 GLN A NE2 1 ATOM 1554 N N . GLY A 1 193 ? -12.683 35.069 26.720 1.00 43.20 ? 219 GLY A N 1 ATOM 1555 C CA . GLY A 1 193 ? -12.263 36.174 27.562 1.00 38.07 ? 219 GLY A CA 1 ATOM 1556 C C . GLY A 1 193 ? -11.545 35.741 28.826 1.00 29.95 ? 219 GLY A C 1 ATOM 1557 O O . GLY A 1 193 ? -11.858 34.681 29.381 1.00 30.21 ? 219 GLY A O 1 ATOM 1558 N N . ASN A 1 194 ? -10.597 36.567 29.274 1.00 26.05 ? 220 ASN A N 1 ATOM 1559 C CA . ASN A 1 194 ? -9.892 36.373 30.550 1.00 22.01 ? 220 ASN A CA 1 ATOM 1560 C C . ASN A 1 194 ? -10.681 36.951 31.729 1.00 22.91 ? 220 ASN A C 1 ATOM 1561 O O . ASN A 1 194 ? -10.720 38.173 31.929 1.00 24.07 ? 220 ASN A O 1 ATOM 1562 C CB . ASN A 1 194 ? -8.495 37.008 30.515 1.00 23.75 ? 220 ASN A CB 1 ATOM 1563 C CG . ASN A 1 194 ? -7.659 36.687 31.761 1.00 19.61 ? 220 ASN A CG 1 ATOM 1564 O OD1 . ASN A 1 194 ? -8.191 36.423 32.839 1.00 20.98 ? 220 ASN A OD1 1 ATOM 1565 N ND2 . ASN A 1 194 ? -6.341 36.699 31.609 1.00 19.20 ? 220 ASN A ND2 1 ATOM 1566 N N . PRO A 1 195 ? -11.263 36.062 32.545 1.00 19.33 ? 221 PRO A N 1 ATOM 1567 C CA . PRO A 1 195 ? -12.144 36.428 33.659 1.00 18.28 ? 221 PRO A CA 1 ATOM 1568 C C . PRO A 1 195 ? -11.391 37.033 34.846 1.00 19.44 ? 221 PRO A C 1 ATOM 1569 O O . PRO A 1 195 ? -11.993 37.712 35.681 1.00 22.19 ? 221 PRO A O 1 ATOM 1570 C CB . PRO A 1 195 ? -12.776 35.085 34.055 1.00 20.12 ? 221 PRO A CB 1 ATOM 1571 C CG . PRO A 1 195 ? -11.778 34.061 33.632 1.00 23.23 ? 221 PRO A CG 1 ATOM 1572 C CD . PRO A 1 195 ? -11.080 34.603 32.424 1.00 22.93 ? 221 PRO A CD 1 ATOM 1573 N N . ASN A 1 196 ? -10.087 36.805 34.924 1.00 13.93 ? 222 ASN A N 1 ATOM 1574 C CA . ASN A 1 196 ? -9.326 37.335 36.044 1.00 12.99 ? 222 ASN A CA 1 ATOM 1575 C C . ASN A 1 196 ? -9.026 38.822 35.956 1.00 11.59 ? 222 ASN A C 1 ATOM 1576 O O . ASN A 1 196 ? -8.669 39.439 36.954 1.00 13.19 ? 222 ASN A O 1 ATOM 1577 C CB . ASN A 1 196 ? -8.018 36.558 36.214 1.00 11.61 ? 222 ASN A CB 1 ATOM 1578 C CG . ASN A 1 196 ? -8.248 35.133 36.679 1.00 13.10 ? 222 ASN A CG 1 ATOM 1579 O OD1 . ASN A 1 196 ? -9.260 34.829 37.317 1.00 13.05 ? 222 ASN A OD1 1 ATOM 1580 N ND2 . ASN A 1 196 ? -7.308 34.241 36.351 1.00 13.40 ? 222 ASN A ND2 1 ATOM 1581 N N . GLU A 1 197 ? -9.177 39.400 34.770 1.00 13.47 ? 223 GLU A N 1 ATOM 1582 C CA . GLU A 1 197 ? -8.987 40.836 34.609 1.00 11.94 ? 223 GLU A CA 1 ATOM 1583 C C . GLU A 1 197 ? -9.990 41.621 35.457 1.00 15.75 ? 223 GLU A C 1 ATOM 1584 O O . GLU A 1 197 ? -9.625 42.588 36.138 1.00 15.86 ? 223 GLU A O 1 ATOM 1585 C CB . GLU A 1 197 ? -9.095 41.236 33.133 1.00 17.56 ? 223 GLU A CB 1 ATOM 1586 C CG . GLU A 1 197 ? -7.965 40.643 32.265 1.00 21.88 ? 223 GLU A CG 1 ATOM 1587 C CD . GLU A 1 197 ? -8.145 40.924 30.782 1.00 31.18 ? 223 GLU A CD 1 ATOM 1588 O OE1 . GLU A 1 197 ? -9.162 41.551 30.410 1.00 34.62 ? 223 GLU A OE1 1 ATOM 1589 O OE2 . GLU A 1 197 ? -7.275 40.510 29.985 1.00 31.40 ? 223 GLU A OE2 1 ATOM 1590 N N . GLU A 1 198 ? -11.250 41.207 35.408 1.00 14.93 ? 224 GLU A N 1 ATOM 1591 C CA . GLU A 1 198 ? -12.304 41.809 36.216 1.00 15.70 ? 224 GLU A CA 1 ATOM 1592 C C . GLU A 1 198 ? -12.046 41.626 37.711 1.00 14.78 ? 224 GLU A C 1 ATOM 1593 O O . GLU A 1 198 ? -12.313 42.514 38.530 1.00 12.91 ? 224 GLU A O 1 ATOM 1594 C CB . GLU A 1 198 ? -13.641 41.176 35.844 1.00 23.92 ? 224 GLU A CB 1 ATOM 1595 C CG . GLU A 1 198 ? -14.788 41.599 36.714 1.00 37.68 ? 224 GLU A CG 1 ATOM 1596 C CD . GLU A 1 198 ? -16.107 41.509 35.984 1.00 53.34 ? 224 GLU A CD 1 ATOM 1597 O OE1 . GLU A 1 198 ? -16.134 41.812 34.773 1.00 58.61 ? 224 GLU A OE1 1 ATOM 1598 O OE2 . GLU A 1 198 ? -17.111 41.132 36.620 1.00 58.59 ? 224 GLU A OE2 1 ATOM 1599 N N . VAL A 1 199 ? -11.539 40.459 38.065 1.00 13.78 ? 225 VAL A N 1 ATOM 1600 C CA . VAL A 1 199 ? -11.289 40.116 39.456 1.00 9.93 ? 225 VAL A CA 1 ATOM 1601 C C . VAL A 1 199 ? -10.178 41.011 40.005 1.00 12.16 ? 225 VAL A C 1 ATOM 1602 O O . VAL A 1 199 ? -10.305 41.536 41.104 1.00 13.23 ? 225 VAL A O 1 ATOM 1603 C CB . VAL A 1 199 ? -10.924 38.621 39.603 1.00 10.82 ? 225 VAL A CB 1 ATOM 1604 C CG1 . VAL A 1 199 ? -10.649 38.276 41.060 1.00 13.09 ? 225 VAL A CG1 1 ATOM 1605 C CG2 . VAL A 1 199 ? -12.075 37.764 39.060 1.00 12.88 ? 225 VAL A CG2 1 ATOM 1606 N N . ALA A 1 200 ? -9.108 41.214 39.236 1.00 10.51 ? 226 ALA A N 1 ATOM 1607 C CA . ALA A 1 200 ? -8.036 42.105 39.686 1.00 10.73 ? 226 ALA A CA 1 ATOM 1608 C C . ALA A 1 200 ? -8.591 43.516 39.880 1.00 13.35 ? 226 ALA A C 1 ATOM 1609 O O . ALA A 1 200 ? -8.227 44.200 40.849 1.00 15.27 ? 226 ALA A O 1 ATOM 1610 C CB . ALA A 1 200 ? -6.872 42.120 38.692 1.00 11.53 ? 226 ALA A CB 1 ATOM 1611 N N . ARG A 1 201 ? -9.461 43.968 38.968 1.00 13.21 ? 227 ARG A N 1 ATOM 1612 C CA . ARG A 1 201 ? -10.028 45.304 39.083 1.00 16.52 ? 227 ARG A CA 1 ATOM 1613 C C . ARG A 1 201 ? -10.823 45.419 40.373 1.00 15.13 ? 227 ARG A C 1 ATOM 1614 O O . ARG A 1 201 ? -10.737 46.443 41.070 1.00 16.83 ? 227 ARG A O 1 ATOM 1615 C CB . ARG A 1 201 ? -10.953 45.626 37.902 1.00 19.39 ? 227 ARG A CB 1 ATOM 1616 C CG . ARG A 1 201 ? -10.240 46.098 36.654 1.00 19.31 ? 227 ARG A CG 1 ATOM 1617 C CD . ARG A 1 201 ? -11.241 46.678 35.657 1.00 18.48 ? 227 ARG A CD 1 ATOM 1618 N NE . ARG A 1 201 ? -12.110 45.660 35.056 1.00 22.80 ? 227 ARG A NE 1 ATOM 1619 C CZ . ARG A 1 201 ? -11.782 44.938 33.985 1.00 22.30 ? 227 ARG A CZ 1 ATOM 1620 N NH1 . ARG A 1 201 ? -10.600 45.097 33.400 1.00 22.38 ? 227 ARG A NH1 1 ATOM 1621 N NH2 . ARG A 1 201 ? -12.637 44.046 33.497 1.00 29.39 ? 227 ARG A NH2 1 ATOM 1622 N N . PHE A 1 202 ? -11.596 44.381 40.689 1.00 12.73 ? 228 PHE A N 1 ATOM 1623 C CA . PHE A 1 202 ? -12.428 44.431 41.884 1.00 16.70 ? 228 PHE A CA 1 ATOM 1624 C C . PHE A 1 202 ? -11.538 44.595 43.126 1.00 18.31 ? 228 PHE A C 1 ATOM 1625 O O . PHE A 1 202 ? -11.787 45.467 43.957 1.00 19.85 ? 228 PHE A O 1 ATOM 1626 C CB . PHE A 1 202 ? -13.297 43.179 41.982 1.00 16.83 ? 228 PHE A CB 1 ATOM 1627 C CG . PHE A 1 202 ? -14.158 43.126 43.214 1.00 20.04 ? 228 PHE A CG 1 ATOM 1628 C CD1 . PHE A 1 202 ? -13.660 42.619 44.415 1.00 21.10 ? 228 PHE A CD1 1 ATOM 1629 C CD2 . PHE A 1 202 ? -15.470 43.565 43.173 1.00 23.92 ? 228 PHE A CD2 1 ATOM 1630 C CE1 . PHE A 1 202 ? -14.461 42.558 45.556 1.00 26.63 ? 228 PHE A CE1 1 ATOM 1631 C CE2 . PHE A 1 202 ? -16.274 43.511 44.305 1.00 28.28 ? 228 PHE A CE2 1 ATOM 1632 C CZ . PHE A 1 202 ? -15.768 43.013 45.498 1.00 28.85 ? 228 PHE A CZ 1 ATOM 1633 N N . TYR A 1 203 ? -10.491 43.774 43.245 1.00 13.22 ? 229 TYR A N 1 ATOM 1634 C CA . TYR A 1 203 ? -9.667 43.808 44.449 1.00 14.36 ? 229 TYR A CA 1 ATOM 1635 C C . TYR A 1 203 ? -8.696 44.992 44.499 1.00 17.91 ? 229 TYR A C 1 ATOM 1636 O O . TYR A 1 203 ? -8.354 45.459 45.582 1.00 22.87 ? 229 TYR A O 1 ATOM 1637 C CB . TYR A 1 203 ? -8.975 42.445 44.688 1.00 11.99 ? 229 TYR A CB 1 ATOM 1638 C CG . TYR A 1 203 ? -9.986 41.398 45.106 1.00 13.17 ? 229 TYR A CG 1 ATOM 1639 C CD1 . TYR A 1 203 ? -10.519 41.403 46.391 1.00 14.96 ? 229 TYR A CD1 1 ATOM 1640 C CD2 . TYR A 1 203 ? -10.447 40.440 44.206 1.00 13.09 ? 229 TYR A CD2 1 ATOM 1641 C CE1 . TYR A 1 203 ? -11.463 40.472 46.774 1.00 16.40 ? 229 TYR A CE1 1 ATOM 1642 C CE2 . TYR A 1 203 ? -11.384 39.506 44.580 1.00 15.73 ? 229 TYR A CE2 1 ATOM 1643 C CZ . TYR A 1 203 ? -11.892 39.521 45.859 1.00 16.97 ? 229 TYR A CZ 1 ATOM 1644 O OH . TYR A 1 203 ? -12.828 38.597 46.239 1.00 18.41 ? 229 TYR A OH 1 ATOM 1645 N N . ALA A 1 204 ? -8.280 45.498 43.341 1.00 17.53 ? 230 ALA A N 1 ATOM 1646 C CA . ALA A 1 204 ? -7.472 46.726 43.318 1.00 18.84 ? 230 ALA A CA 1 ATOM 1647 C C . ALA A 1 204 ? -8.256 47.886 43.919 1.00 22.99 ? 230 ALA A C 1 ATOM 1648 O O . ALA A 1 204 ? -7.678 48.772 44.540 1.00 25.96 ? 230 ALA A O 1 ATOM 1649 C CB . ALA A 1 204 ? -7.002 47.077 41.903 1.00 16.65 ? 230 ALA A CB 1 ATOM 1650 N N . ALA A 1 205 ? -9.571 47.884 43.728 1.00 21.38 ? 231 ALA A N 1 ATOM 1651 C CA . ALA A 1 205 ? -10.414 48.959 44.249 1.00 26.63 ? 231 ALA A CA 1 ATOM 1652 C C . ALA A 1 205 ? -10.653 48.790 45.748 1.00 32.60 ? 231 ALA A C 1 ATOM 1653 O O . ALA A 1 205 ? -10.990 49.749 46.439 1.00 37.79 ? 231 ALA A O 1 ATOM 1654 C CB . ALA A 1 205 ? -11.732 49.015 43.497 1.00 26.08 ? 231 ALA A CB 1 ATOM 1655 N N . ALA A 1 206 ? -10.480 47.565 46.241 1.00 32.41 ? 232 ALA A N 1 ATOM 1656 C CA . ALA A 1 206 ? -10.694 47.261 47.655 1.00 34.39 ? 232 ALA A CA 1 ATOM 1657 C C . ALA A 1 206 ? -9.395 47.150 48.468 1.00 37.74 ? 232 ALA A C 1 ATOM 1658 O O . ALA A 1 206 ? -9.393 47.404 49.676 1.00 44.14 ? 232 ALA A O 1 ATOM 1659 C CB . ALA A 1 206 ? -11.521 45.996 47.801 1.00 32.51 ? 232 ALA A CB 1 ATOM 1660 N N . MET A 1 207 ? -8.296 46.774 47.818 1.00 33.82 ? 233 MET A N 1 ATOM 1661 C CA . MET A 1 207 ? -7.028 46.564 48.525 1.00 36.61 ? 233 MET A CA 1 ATOM 1662 C C . MET A 1 207 ? -6.022 47.679 48.293 1.00 40.00 ? 233 MET A C 1 ATOM 1663 O O . MET A 1 207 ? -5.220 47.619 47.361 1.00 38.72 ? 233 MET A O 1 ATOM 1664 C CB . MET A 1 207 ? -6.393 45.238 48.121 1.00 35.72 ? 233 MET A CB 1 ATOM 1665 C CG . MET A 1 207 ? -7.169 44.029 48.566 1.00 36.39 ? 233 MET A CG 1 ATOM 1666 S SD . MET A 1 207 ? -6.468 42.548 47.831 1.00 34.83 ? 233 MET A SD 1 ATOM 1667 C CE . MET A 1 207 ? -4.844 42.488 48.615 1.00 19.49 ? 233 MET A CE 1 HETATM 1668 CA CA . CA B 2 . ? -4.908 35.657 34.576 1.00 16.37 ? 301 CA A CA 1 HETATM 1669 C C1 . NAG C 3 . ? 20.132 14.774 49.390 1.00 16.95 ? 302 NAG A C1 1 HETATM 1670 C C2 . NAG C 3 . ? 20.422 14.208 50.773 1.00 23.52 ? 302 NAG A C2 1 HETATM 1671 C C3 . NAG C 3 . ? 21.847 13.692 50.772 1.00 24.17 ? 302 NAG A C3 1 HETATM 1672 C C4 . NAG C 3 . ? 22.021 12.649 49.679 1.00 25.78 ? 302 NAG A C4 1 HETATM 1673 C C5 . NAG C 3 . ? 21.518 13.130 48.324 1.00 25.63 ? 302 NAG A C5 1 HETATM 1674 C C6 . NAG C 3 . ? 21.403 11.953 47.365 1.00 30.87 ? 302 NAG A C6 1 HETATM 1675 C C7 . NAG C 3 . ? 19.112 15.343 52.495 1.00 37.42 ? 302 NAG A C7 1 HETATM 1676 C C8 . NAG C 3 . ? 19.044 16.496 53.451 1.00 36.71 ? 302 NAG A C8 1 HETATM 1677 N N2 . NAG C 3 . ? 20.246 15.215 51.803 1.00 31.45 ? 302 NAG A N2 1 HETATM 1678 O O3 . NAG C 3 . ? 22.130 13.125 52.026 1.00 32.19 ? 302 NAG A O3 1 HETATM 1679 O O4 . NAG C 3 . ? 23.397 12.365 49.560 1.00 26.07 ? 302 NAG A O4 1 HETATM 1680 O O5 . NAG C 3 . ? 20.243 13.745 48.427 1.00 21.36 ? 302 NAG A O5 1 HETATM 1681 O O6 . NAG C 3 . ? 20.867 12.401 46.140 1.00 37.30 ? 302 NAG A O6 1 HETATM 1682 O O7 . NAG C 3 . ? 18.151 14.578 52.375 1.00 39.20 ? 302 NAG A O7 1 HETATM 1683 C C1 . NAG D 3 . ? -18.484 34.889 51.257 0.83 27.28 ? 303 NAG A C1 1 HETATM 1684 C C2 . NAG D 3 . ? -19.883 35.153 50.693 0.83 26.37 ? 303 NAG A C2 1 HETATM 1685 C C3 . NAG D 3 . ? -20.244 36.634 50.626 0.83 33.85 ? 303 NAG A C3 1 HETATM 1686 C C4 . NAG D 3 . ? -19.744 37.431 51.824 0.83 37.42 ? 303 NAG A C4 1 HETATM 1687 C C5 . NAG D 3 . ? -18.315 37.045 52.204 0.83 37.25 ? 303 NAG A C5 1 HETATM 1688 C C6 . NAG D 3 . ? -17.875 37.774 53.472 0.83 39.85 ? 303 NAG A C6 1 HETATM 1689 C C7 . NAG D 3 . ? -20.538 33.423 49.131 0.83 19.57 ? 303 NAG A C7 1 HETATM 1690 C C8 . NAG D 3 . ? -20.696 32.988 47.704 0.83 17.76 ? 303 NAG A C8 1 HETATM 1691 N N2 . NAG D 3 . ? -19.983 34.607 49.354 0.83 23.25 ? 303 NAG A N2 1 HETATM 1692 O O3 . NAG D 3 . ? -21.646 36.765 50.540 0.83 37.52 ? 303 NAG A O3 1 HETATM 1693 O O4 . NAG D 3 . ? -19.779 38.800 51.491 0.83 39.85 ? 303 NAG A O4 1 HETATM 1694 O O5 . NAG D 3 . ? -18.235 35.649 52.422 0.83 34.22 ? 303 NAG A O5 1 HETATM 1695 O O6 . NAG D 3 . ? -18.473 37.153 54.587 0.83 40.56 ? 303 NAG A O6 1 HETATM 1696 O O7 . NAG D 3 . ? -20.925 32.707 50.045 0.83 22.98 ? 303 NAG A O7 1 HETATM 1697 C C1 . NAG E 3 . ? 14.289 37.092 29.395 0.84 49.21 ? 304 NAG A C1 1 HETATM 1698 C C2 . NAG E 3 . ? 14.620 35.603 29.457 0.84 55.37 ? 304 NAG A C2 1 HETATM 1699 C C3 . NAG E 3 . ? 14.154 34.976 30.769 0.84 56.95 ? 304 NAG A C3 1 HETATM 1700 C C4 . NAG E 3 . ? 14.490 35.852 31.969 0.84 58.19 ? 304 NAG A C4 1 HETATM 1701 C C5 . NAG E 3 . ? 14.069 37.297 31.721 0.84 55.61 ? 304 NAG A C5 1 HETATM 1702 C C6 . NAG E 3 . ? 14.448 38.200 32.888 0.84 55.89 ? 304 NAG A C6 1 HETATM 1703 C C7 . NAG E 3 . ? 14.648 33.981 27.643 0.84 62.66 ? 304 NAG A C7 1 HETATM 1704 C C8 . NAG E 3 . ? 14.514 34.030 26.150 0.84 63.05 ? 304 NAG A C8 1 HETATM 1705 N N2 . NAG E 3 . ? 14.010 34.925 28.328 0.84 58.92 ? 304 NAG A N2 1 HETATM 1706 O O3 . NAG E 3 . ? 14.773 33.721 30.937 0.84 56.48 ? 304 NAG A O3 1 HETATM 1707 O O4 . NAG E 3 . ? 13.832 35.347 33.109 0.84 61.01 ? 304 NAG A O4 1 HETATM 1708 O O5 . NAG E 3 . ? 14.710 37.766 30.560 0.84 52.70 ? 304 NAG A O5 1 HETATM 1709 O O6 . NAG E 3 . ? 15.817 38.025 33.178 0.84 56.62 ? 304 NAG A O6 1 HETATM 1710 O O7 . NAG E 3 . ? 15.311 33.096 28.180 0.84 64.53 ? 304 NAG A O7 1 HETATM 1711 O O . HOH F 4 . ? 7.861 27.756 45.296 1.00 24.79 ? 401 HOH A O 1 HETATM 1712 O O . HOH F 4 . ? 11.725 12.017 46.225 1.00 21.22 ? 402 HOH A O 1 HETATM 1713 O O . HOH F 4 . ? -6.404 44.220 32.562 1.00 34.99 ? 403 HOH A O 1 HETATM 1714 O O . HOH F 4 . ? 10.341 43.014 44.591 1.00 31.64 ? 404 HOH A O 1 HETATM 1715 O O . HOH F 4 . ? -11.500 28.027 53.431 1.00 28.00 ? 405 HOH A O 1 HETATM 1716 O O . HOH F 4 . ? 16.845 23.058 49.376 1.00 38.10 ? 406 HOH A O 1 HETATM 1717 O O . HOH F 4 . ? 10.226 47.292 40.653 1.00 32.96 ? 407 HOH A O 1 HETATM 1718 O O . HOH F 4 . ? -16.550 23.698 44.284 1.00 26.48 ? 408 HOH A O 1 HETATM 1719 O O . HOH F 4 . ? -19.686 29.783 45.766 1.00 31.71 ? 409 HOH A O 1 HETATM 1720 O O . HOH F 4 . ? -11.377 13.100 47.255 1.00 25.56 ? 410 HOH A O 1 HETATM 1721 O O . HOH F 4 . ? 6.536 40.225 31.225 1.00 25.03 ? 411 HOH A O 1 HETATM 1722 O O . HOH F 4 . ? -4.227 34.639 25.396 1.00 29.06 ? 412 HOH A O 1 HETATM 1723 O O . HOH F 4 . ? -5.138 33.535 23.165 1.00 44.36 ? 413 HOH A O 1 HETATM 1724 O O . HOH F 4 . ? 3.065 29.804 44.206 1.00 40.92 ? 414 HOH A O 1 HETATM 1725 O O . HOH F 4 . ? 5.944 19.726 33.938 1.00 32.46 ? 415 HOH A O 1 HETATM 1726 O O . HOH F 4 . ? 6.119 36.707 52.524 1.00 37.67 ? 416 HOH A O 1 HETATM 1727 O O . HOH F 4 . ? 14.655 34.522 44.492 1.00 28.46 ? 417 HOH A O 1 HETATM 1728 O O . HOH F 4 . ? 8.202 46.075 31.204 1.00 16.02 ? 418 HOH A O 1 HETATM 1729 O O . HOH F 4 . ? 14.800 43.618 35.778 1.00 42.16 ? 419 HOH A O 1 HETATM 1730 O O . HOH F 4 . ? 5.217 24.593 27.783 1.00 24.99 ? 420 HOH A O 1 HETATM 1731 O O . HOH F 4 . ? 0.435 29.034 24.208 1.00 36.36 ? 421 HOH A O 1 HETATM 1732 O O . HOH F 4 . ? -1.740 22.995 27.226 1.00 25.93 ? 422 HOH A O 1 HETATM 1733 O O . HOH F 4 . ? -3.710 37.449 30.062 1.00 21.57 ? 423 HOH A O 1 HETATM 1734 O O . HOH F 4 . ? 24.598 13.106 53.102 1.00 21.97 ? 424 HOH A O 1 HETATM 1735 O O . HOH F 4 . ? 11.975 11.142 41.953 1.00 31.20 ? 425 HOH A O 1 HETATM 1736 O O . HOH F 4 . ? -11.011 25.704 32.768 1.00 35.05 ? 426 HOH A O 1 HETATM 1737 O O . HOH F 4 . ? -9.873 23.255 32.887 1.00 34.50 ? 427 HOH A O 1 HETATM 1738 O O . HOH F 4 . ? -14.346 46.575 44.820 1.00 29.58 ? 428 HOH A O 1 HETATM 1739 O O . HOH F 4 . ? -18.641 25.582 43.773 1.00 32.91 ? 429 HOH A O 1 HETATM 1740 O O . HOH F 4 . ? -15.486 35.515 37.553 1.00 28.35 ? 430 HOH A O 1 HETATM 1741 O O . HOH F 4 . ? 11.157 31.248 33.209 1.00 36.51 ? 431 HOH A O 1 HETATM 1742 O O . HOH F 4 . ? 8.753 31.473 34.664 1.00 19.26 ? 432 HOH A O 1 HETATM 1743 O O . HOH F 4 . ? 9.742 38.879 29.048 1.00 34.64 ? 433 HOH A O 1 HETATM 1744 O O . HOH F 4 . ? 2.462 6.072 50.393 1.00 43.10 ? 434 HOH A O 1 HETATM 1745 O O . HOH F 4 . ? -19.484 31.798 53.200 1.00 43.81 ? 435 HOH A O 1 HETATM 1746 O O . HOH F 4 . ? -20.210 38.761 42.432 1.00 24.04 ? 436 HOH A O 1 HETATM 1747 O O . HOH F 4 . ? -0.465 8.032 41.887 1.00 53.46 ? 437 HOH A O 1 HETATM 1748 O O . HOH F 4 . ? -1.661 7.391 39.015 1.00 39.70 ? 438 HOH A O 1 HETATM 1749 O O . HOH F 4 . ? -0.648 44.247 28.143 1.00 32.36 ? 439 HOH A O 1 HETATM 1750 O O . HOH F 4 . ? -14.089 21.992 51.269 1.00 48.42 ? 440 HOH A O 1 HETATM 1751 O O . HOH F 4 . ? 12.752 43.394 51.502 1.00 30.31 ? 441 HOH A O 1 HETATM 1752 O O . HOH F 4 . ? 7.775 28.789 52.985 1.00 33.97 ? 442 HOH A O 1 HETATM 1753 O O . HOH F 4 . ? 8.997 7.546 51.753 1.00 32.81 ? 443 HOH A O 1 HETATM 1754 O O . HOH F 4 . ? -10.753 22.808 38.296 1.00 45.64 ? 444 HOH A O 1 HETATM 1755 O O . HOH F 4 . ? -14.463 27.838 50.838 1.00 44.06 ? 445 HOH A O 1 HETATM 1756 O O . HOH F 4 . ? 14.252 26.034 35.514 1.00 38.38 ? 446 HOH A O 1 HETATM 1757 O O . HOH F 4 . ? 2.743 45.724 44.300 1.00 42.42 ? 447 HOH A O 1 HETATM 1758 O O . HOH F 4 . ? -1.149 35.734 55.181 1.00 38.11 ? 448 HOH A O 1 HETATM 1759 O O . HOH F 4 . ? -13.307 30.272 30.091 1.00 38.74 ? 449 HOH A O 1 HETATM 1760 O O . HOH F 4 . ? -15.933 47.609 43.340 1.00 30.12 ? 450 HOH A O 1 HETATM 1761 O O . HOH F 4 . ? -21.014 25.943 44.647 1.00 43.38 ? 451 HOH A O 1 HETATM 1762 O O . HOH F 4 . ? 13.053 9.782 40.077 1.00 38.69 ? 452 HOH A O 1 HETATM 1763 O O . HOH F 4 . ? 9.646 29.756 43.906 1.00 12.93 ? 453 HOH A O 1 HETATM 1764 O O . HOH F 4 . ? 3.991 33.341 46.199 1.00 12.01 ? 454 HOH A O 1 HETATM 1765 O O . HOH F 4 . ? -2.097 42.616 38.006 1.00 19.67 ? 455 HOH A O 1 HETATM 1766 O O . HOH F 4 . ? -4.901 43.315 36.044 1.00 14.15 ? 456 HOH A O 1 HETATM 1767 O O . HOH F 4 . ? 3.126 44.717 48.564 1.00 16.92 ? 457 HOH A O 1 HETATM 1768 O O . HOH F 4 . ? 4.654 12.668 43.980 1.00 13.12 ? 458 HOH A O 1 HETATM 1769 O O . HOH F 4 . ? -0.750 28.422 49.112 1.00 13.69 ? 459 HOH A O 1 HETATM 1770 O O . HOH F 4 . ? 9.794 36.806 45.575 1.00 13.01 ? 460 HOH A O 1 HETATM 1771 O O . HOH F 4 . ? 7.017 39.917 45.003 1.00 15.41 ? 461 HOH A O 1 HETATM 1772 O O . HOH F 4 . ? -3.812 31.721 52.697 1.00 17.48 ? 462 HOH A O 1 HETATM 1773 O O . HOH F 4 . ? -9.622 29.983 52.784 1.00 15.89 ? 463 HOH A O 1 HETATM 1774 O O . HOH F 4 . ? 5.158 14.886 30.703 1.00 23.32 ? 464 HOH A O 1 HETATM 1775 O O . HOH F 4 . ? 1.490 28.735 42.352 1.00 23.47 ? 465 HOH A O 1 HETATM 1776 O O . HOH F 4 . ? -7.394 44.161 35.371 1.00 18.03 ? 466 HOH A O 1 HETATM 1777 O O . HOH F 4 . ? -4.566 11.655 42.152 1.00 14.23 ? 467 HOH A O 1 HETATM 1778 O O . HOH F 4 . ? 20.006 22.003 42.334 1.00 19.05 ? 468 HOH A O 1 HETATM 1779 O O . HOH F 4 . ? 2.336 10.960 43.341 1.00 17.99 ? 469 HOH A O 1 HETATM 1780 O O . HOH F 4 . ? -11.974 22.882 52.618 1.00 19.87 ? 470 HOH A O 1 HETATM 1781 O O . HOH F 4 . ? 17.815 15.969 44.737 1.00 17.64 ? 471 HOH A O 1 HETATM 1782 O O . HOH F 4 . ? 0.533 44.483 45.413 1.00 17.09 ? 472 HOH A O 1 HETATM 1783 O O . HOH F 4 . ? 13.399 23.752 48.809 1.00 29.88 ? 473 HOH A O 1 HETATM 1784 O O . HOH F 4 . ? 0.492 39.499 37.954 1.00 13.85 ? 474 HOH A O 1 HETATM 1785 O O . HOH F 4 . ? 14.493 34.464 40.532 1.00 15.14 ? 475 HOH A O 1 HETATM 1786 O O . HOH F 4 . ? -3.107 8.342 47.399 1.00 21.85 ? 476 HOH A O 1 HETATM 1787 O O . HOH F 4 . ? -9.824 22.768 56.496 1.00 29.60 ? 477 HOH A O 1 HETATM 1788 O O . HOH F 4 . ? 8.828 19.124 35.732 1.00 22.16 ? 478 HOH A O 1 HETATM 1789 O O . HOH F 4 . ? 2.814 36.327 36.859 1.00 17.08 ? 479 HOH A O 1 HETATM 1790 O O . HOH F 4 . ? -5.570 12.969 56.469 1.00 21.05 ? 480 HOH A O 1 HETATM 1791 O O . HOH F 4 . ? -5.205 10.945 49.405 1.00 15.59 ? 481 HOH A O 1 HETATM 1792 O O . HOH F 4 . ? -4.297 42.206 32.392 1.00 20.28 ? 482 HOH A O 1 HETATM 1793 O O . HOH F 4 . ? -12.556 35.482 48.862 1.00 26.79 ? 483 HOH A O 1 HETATM 1794 O O . HOH F 4 . ? -12.477 39.858 33.144 1.00 22.65 ? 484 HOH A O 1 HETATM 1795 O O . HOH F 4 . ? -9.873 11.780 51.511 1.00 23.10 ? 485 HOH A O 1 HETATM 1796 O O . HOH F 4 . ? 18.792 21.117 48.530 1.00 21.27 ? 486 HOH A O 1 HETATM 1797 O O . HOH F 4 . ? 9.716 48.209 47.376 1.00 42.58 ? 487 HOH A O 1 HETATM 1798 O O . HOH F 4 . ? -9.944 34.546 49.991 1.00 20.32 ? 488 HOH A O 1 HETATM 1799 O O . HOH F 4 . ? -6.179 37.538 53.863 1.00 23.89 ? 489 HOH A O 1 HETATM 1800 O O . HOH F 4 . ? -19.400 28.594 39.132 1.00 28.42 ? 490 HOH A O 1 HETATM 1801 O O . HOH F 4 . ? -8.305 39.019 48.158 1.00 21.70 ? 491 HOH A O 1 HETATM 1802 O O . HOH F 4 . ? 4.930 18.612 56.071 1.00 26.60 ? 492 HOH A O 1 HETATM 1803 O O . HOH F 4 . ? -8.041 36.750 49.877 1.00 23.07 ? 493 HOH A O 1 HETATM 1804 O O . HOH F 4 . ? 2.560 25.646 54.476 1.00 45.74 ? 494 HOH A O 1 HETATM 1805 O O . HOH F 4 . ? -4.520 7.148 39.991 1.00 30.58 ? 495 HOH A O 1 HETATM 1806 O O . HOH F 4 . ? -8.278 46.668 34.112 1.00 22.96 ? 496 HOH A O 1 HETATM 1807 O O . HOH F 4 . ? 11.525 36.827 34.499 1.00 26.18 ? 497 HOH A O 1 HETATM 1808 O O . HOH F 4 . ? 11.531 17.048 51.878 1.00 30.40 ? 498 HOH A O 1 HETATM 1809 O O . HOH F 4 . ? 13.346 39.209 50.306 1.00 25.60 ? 499 HOH A O 1 HETATM 1810 O O . HOH F 4 . ? 5.433 28.123 43.558 1.00 25.26 ? 500 HOH A O 1 HETATM 1811 O O . HOH F 4 . ? -20.558 32.180 40.885 1.00 16.74 ? 501 HOH A O 1 HETATM 1812 O O . HOH F 4 . ? -13.164 25.092 50.000 1.00 34.41 ? 502 HOH A O 1 HETATM 1813 O O . HOH F 4 . ? 9.515 40.664 44.769 1.00 24.51 ? 503 HOH A O 1 HETATM 1814 O O . HOH F 4 . ? -11.529 18.073 37.841 1.00 33.23 ? 504 HOH A O 1 HETATM 1815 O O . HOH F 4 . ? -8.494 37.801 52.311 1.00 31.06 ? 505 HOH A O 1 HETATM 1816 O O . HOH F 4 . ? -19.945 32.724 43.621 1.00 18.53 ? 506 HOH A O 1 HETATM 1817 O O . HOH F 4 . ? -3.163 50.176 39.116 1.00 42.71 ? 507 HOH A O 1 HETATM 1818 O O . HOH F 4 . ? 3.112 25.048 40.736 1.00 27.83 ? 508 HOH A O 1 HETATM 1819 O O . HOH F 4 . ? 3.897 27.559 41.402 1.00 26.14 ? 509 HOH A O 1 HETATM 1820 O O . HOH F 4 . ? -7.679 16.991 36.254 1.00 24.06 ? 510 HOH A O 1 HETATM 1821 O O . HOH F 4 . ? -5.007 39.673 30.935 1.00 28.74 ? 511 HOH A O 1 HETATM 1822 O O . HOH F 4 . ? -18.819 41.997 41.704 1.00 36.11 ? 512 HOH A O 1 HETATM 1823 O O . HOH F 4 . ? -11.685 15.780 54.117 1.00 21.41 ? 513 HOH A O 1 HETATM 1824 O O . HOH F 4 . ? -14.598 37.719 36.000 1.00 29.88 ? 514 HOH A O 1 HETATM 1825 O O . HOH F 4 . ? -16.271 41.896 40.004 1.00 29.67 ? 515 HOH A O 1 HETATM 1826 O O . HOH F 4 . ? 11.585 24.780 33.627 1.00 28.05 ? 516 HOH A O 1 HETATM 1827 O O . HOH F 4 . ? 17.931 22.717 40.332 1.00 28.98 ? 517 HOH A O 1 HETATM 1828 O O . HOH F 4 . ? -6.474 9.402 51.099 1.00 29.29 ? 518 HOH A O 1 HETATM 1829 O O . HOH F 4 . ? 6.354 20.706 54.949 1.00 32.93 ? 519 HOH A O 1 HETATM 1830 O O . HOH F 4 . ? 9.451 9.002 40.899 1.00 48.81 ? 520 HOH A O 1 HETATM 1831 O O . HOH F 4 . ? 10.031 24.479 45.872 1.00 29.75 ? 521 HOH A O 1 HETATM 1832 O O . HOH F 4 . ? -12.936 34.162 38.017 1.00 29.82 ? 522 HOH A O 1 HETATM 1833 O O . HOH F 4 . ? 7.213 16.659 55.592 1.00 48.02 ? 523 HOH A O 1 HETATM 1834 O O . HOH F 4 . ? -13.678 32.792 30.460 1.00 55.20 ? 524 HOH A O 1 HETATM 1835 O O . HOH F 4 . ? 8.827 16.578 35.651 1.00 34.99 ? 525 HOH A O 1 HETATM 1836 O O . HOH F 4 . ? 8.120 14.896 37.632 1.00 27.35 ? 526 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 4 ? 0.7107 0.5351 0.6379 -0.0448 -0.0451 -0.1327 30 ARG A N 2 C CA . ARG A 4 ? 0.6454 0.4751 0.5748 -0.0220 -0.0382 -0.1225 30 ARG A CA 3 C C . ARG A 4 ? 0.6664 0.4612 0.6009 -0.0101 -0.0234 -0.1190 30 ARG A C 4 O O . ARG A 4 ? 0.7184 0.4927 0.6380 0.0006 -0.0141 -0.1319 30 ARG A O 5 C CB . ARG A 4 ? 0.6033 0.4546 0.5084 -0.0079 -0.0390 -0.1318 30 ARG A CB 6 C CG . ARG A 4 ? 0.5155 0.3863 0.4231 0.0120 -0.0330 -0.1154 30 ARG A CG 7 C CD . ARG A 4 ? 0.4830 0.3921 0.3719 0.0210 -0.0348 -0.1164 30 ARG A CD 8 N NE . ARG A 4 ? 0.3938 0.3292 0.2898 0.0339 -0.0293 -0.0929 30 ARG A NE 9 C CZ . ARG A 4 ? 0.3995 0.3368 0.2859 0.0536 -0.0178 -0.0889 30 ARG A CZ 10 N NH1 . ARG A 4 ? 0.3826 0.2930 0.2509 0.0666 -0.0085 -0.1086 30 ARG A NH1 11 N NH2 . ARG A 4 ? 0.3471 0.3128 0.2416 0.0604 -0.0156 -0.0648 30 ARG A NH2 12 N N . THR A 5 ? 0.6285 0.4205 0.5855 -0.0114 -0.0205 -0.1002 31 THR A N 13 C CA . THR A 5 ? 0.6271 0.3918 0.5930 -0.0023 -0.0070 -0.0914 31 THR A CA 14 C C . THR A 5 ? 0.5788 0.3585 0.5554 0.0138 -0.0013 -0.0715 31 THR A C 15 O O . THR A 5 ? 0.6370 0.4213 0.6040 0.0331 0.0042 -0.0711 31 THR A O 16 C CB . THR A 5 ? 1.0476 0.7924 1.0238 -0.0202 -0.0084 -0.0841 31 THR A CB 17 O OG1 . THR A 5 ? 1.0756 0.8046 1.0575 -0.0100 -0.0016 -0.0655 31 THR A OG1 18 C CG2 . THR A 5 ? 0.9943 0.7704 0.9874 -0.0366 -0.0202 -0.0753 31 THR A CG2 19 N N . GLU A 6 ? 0.4865 0.2766 0.4790 0.0059 -0.0034 -0.0538 32 GLU A N 20 C CA . GLU A 6 ? 0.4804 0.2866 0.4824 0.0162 0.0009 -0.0343 32 GLU A CA 21 C C . GLU A 6 ? 0.3490 0.1882 0.3410 0.0209 -0.0030 -0.0321 32 GLU A C 22 O O . GLU A 6 ? 0.3834 0.2393 0.3755 0.0108 -0.0119 -0.0359 32 GLU A O 23 C CB . GLU A 6 ? 0.5960 0.4148 0.6154 0.0036 -0.0010 -0.0195 32 GLU A CB 24 C CG . GLU A 6 ? 0.6839 0.5233 0.7114 0.0098 0.0046 -0.0001 32 GLU A CG 25 C CD . GLU A 6 ? 0.8099 0.6433 0.8389 0.0212 0.0129 0.0117 32 GLU A CD 26 O OE1 . GLU A 6 ? 0.9010 0.7125 0.9332 0.0200 0.0134 0.0094 32 GLU A OE1 27 O OE2 . GLU A 6 ? 0.8256 0.6775 0.8525 0.0306 0.0184 0.0246 32 GLU A OE2 28 N N . LEU A 7 ? 0.3196 0.1717 0.3037 0.0357 0.0037 -0.0224 33 LEU A N 29 C CA . LEU A 7 ? 0.2432 0.1278 0.2174 0.0374 -0.0009 -0.0168 33 LEU A CA 30 C C . LEU A 7 ? 0.2678 0.1727 0.2475 0.0367 0.0009 0.0041 33 LEU A C 31 O O . LEU A 7 ? 0.2831 0.2094 0.2576 0.0321 -0.0054 0.0099 33 LEU A O 32 C CB . LEU A 7 ? 0.2399 0.1327 0.1975 0.0524 0.0029 -0.0220 33 LEU A CB 33 C CG . LEU A 7 ? 0.2639 0.1372 0.2081 0.0545 0.0018 -0.0463 33 LEU A CG 34 C CD1 . LEU A 7 ? 0.3939 0.2822 0.3196 0.0731 0.0081 -0.0497 33 LEU A CD1 35 C CD2 . LEU A 7 ? 0.2545 0.1375 0.1980 0.0373 -0.0114 -0.0567 33 LEU A CD2 36 N N . LEU A 8 ? 0.2406 0.1384 0.2301 0.0401 0.0088 0.0159 34 LEU A N 37 C CA . LEU A 8 ? 0.2351 0.1555 0.2265 0.0381 0.0102 0.0357 34 LEU A CA 38 C C . LEU A 8 ? 0.2334 0.1527 0.2338 0.0258 0.0085 0.0388 34 LEU A C 39 O O . LEU A 8 ? 0.2514 0.1539 0.2643 0.0230 0.0113 0.0359 34 LEU A O 40 C CB . LEU A 8 ? 0.2328 0.1576 0.2292 0.0516 0.0208 0.0521 34 LEU A CB 41 C CG . LEU A 8 ? 0.2407 0.1703 0.2283 0.0691 0.0262 0.0513 34 LEU A CG 42 C CD1 . LEU A 8 ? 0.2596 0.1967 0.2562 0.0840 0.0382 0.0698 34 LEU A CD1 43 C CD2 . LEU A 8 ? 0.2903 0.2523 0.2655 0.0658 0.0184 0.0558 34 LEU A CD2 44 N N . ASN A 9 ? 0.2094 0.1465 0.2027 0.0181 0.0038 0.0445 35 ASN A N 45 C CA . ASN A 9 ? 0.1838 0.1237 0.1807 0.0092 0.0040 0.0465 35 ASN A CA 46 C C . ASN A 9 ? 0.2200 0.1464 0.2272 0.0053 0.0027 0.0343 35 ASN A C 47 O O . ASN A 9 ? 0.2402 0.1646 0.2604 0.0027 0.0072 0.0386 35 ASN A O 48 C CB . ASN A 9 ? 0.2140 0.1643 0.2183 0.0102 0.0117 0.0637 35 ASN A CB 49 C CG . ASN A 9 ? 0.2149 0.1797 0.2140 0.0011 0.0116 0.0676 35 ASN A CG 50 O OD1 . ASN A 9 ? 0.2819 0.2527 0.2647 -0.0049 0.0059 0.0631 35 ASN A OD1 51 N ND2 . ASN A 9 ? 0.2373 0.2071 0.2492 0.0000 0.0178 0.0761 35 ASN A ND2 52 N N . VAL A 10 ? 0.2256 0.1482 0.2289 0.0040 -0.0041 0.0224 36 VAL A N 53 C CA . VAL A 10 ? 0.1837 0.0998 0.1982 -0.0002 -0.0067 0.0132 36 VAL A CA 54 C C . VAL A 10 ? 0.2052 0.1284 0.2155 -0.0018 -0.0129 0.0078 36 VAL A C 55 O O . VAL A 10 ? 0.2022 0.1290 0.2005 -0.0002 -0.0168 0.0089 36 VAL A O 56 C CB . VAL A 10 ? 0.2657 0.1671 0.2837 0.0003 -0.0084 0.0041 36 VAL A CB 57 C CG1 . VAL A 10 ? 0.2488 0.1542 0.2533 0.0042 -0.0141 -0.0040 36 VAL A CG1 58 C CG2 . VAL A 10 ? 0.3369 0.2340 0.3697 -0.0089 -0.0116 -0.0012 36 VAL A CG2 59 N N . CYS A 11 ? 0.2056 0.1324 0.2281 -0.0047 -0.0137 0.0050 37 CYS A N 60 C CA . CYS A 11 ? 0.2230 0.1569 0.2463 -0.0031 -0.0173 0.0029 37 CYS A CA 61 C C . CYS A 11 ? 0.1910 0.1330 0.2287 -0.0072 -0.0223 -0.0004 37 CYS A C 62 O O . CYS A 11 ? 0.2202 0.1598 0.2671 -0.0137 -0.0224 -0.0016 37 CYS A O 63 C CB . CYS A 11 ? 0.3035 0.2418 0.3282 0.0000 -0.0105 0.0062 37 CYS A CB 64 S SG . CYS A 11 ? 0.3039 0.2387 0.3114 -0.0001 -0.0046 0.0104 37 CYS A SG 65 N N . MET A 12 ? 0.1863 0.1379 0.2266 -0.0047 -0.0273 -0.0001 38 MET A N 66 C CA . MET A 12 ? 0.2068 0.1755 0.2635 -0.0089 -0.0319 0.0011 38 MET A CA 67 C C . MET A 12 ? 0.2311 0.2111 0.2984 -0.0003 -0.0269 0.0084 38 MET A C 68 O O . MET A 12 ? 0.2658 0.2386 0.3255 0.0084 -0.0260 0.0093 38 MET A O 69 C CB . MET A 12 ? 0.2296 0.2072 0.2821 -0.0115 -0.0418 -0.0017 38 MET A CB 70 C CG . MET A 12 ? 0.2657 0.2679 0.3346 -0.0184 -0.0486 0.0014 38 MET A CG 71 S SD . MET A 12 ? 0.2983 0.2969 0.3705 -0.0353 -0.0531 -0.0073 38 MET A SD 72 C CE . MET A 12 ? 0.2774 0.2573 0.3237 -0.0359 -0.0568 -0.0226 38 MET A CE 73 N N . ASN A 13 ? 0.2168 0.2137 0.3018 -0.0021 -0.0232 0.0143 39 ASN A N 74 C CA . ASN A 13 ? 0.2130 0.2238 0.3081 0.0104 -0.0154 0.0216 39 ASN A CA 75 C C . ASN A 13 ? 0.2024 0.2360 0.3137 0.0148 -0.0201 0.0298 39 ASN A C 76 O O . ASN A 13 ? 0.2024 0.2442 0.3160 0.0055 -0.0310 0.0296 39 ASN A O 77 C CB . ASN A 13 ? 0.2602 0.2862 0.3672 0.0101 -0.0065 0.0282 39 ASN A CB 78 C CG . ASN A 13 ? 0.2755 0.3271 0.4056 -0.0038 -0.0125 0.0371 39 ASN A CG 79 O OD1 . ASN A 13 ? 0.2540 0.3194 0.3933 -0.0105 -0.0220 0.0392 39 ASN A OD1 80 N ND2 . ASN A 13 ? 0.3460 0.4067 0.4859 -0.0102 -0.0077 0.0441 39 ASN A ND2 81 N N . ALA A 14 ? 0.1859 0.2319 0.3079 0.0303 -0.0113 0.0376 40 ALA A N 82 C CA . ALA A 14 ? 0.1864 0.2563 0.3269 0.0389 -0.0136 0.0497 40 ALA A CA 83 C C . ALA A 14 ? 0.1831 0.2945 0.3477 0.0256 -0.0214 0.0616 40 ALA A C 84 O O . ALA A 14 ? 0.1546 0.2925 0.3348 0.0275 -0.0272 0.0734 40 ALA A O 85 C CB . ALA A 14 ? 0.1773 0.2473 0.3228 0.0629 0.0007 0.0547 40 ALA A CB 86 N N . LYS A 15 ? 0.1651 0.2835 0.3337 0.0109 -0.0222 0.0605 41 LYS A N 87 C CA . LYS A 15 ? 0.1790 0.3313 0.3673 -0.0083 -0.0326 0.0701 41 LYS A CA 88 C C . LYS A 15 ? 0.1678 0.3009 0.3405 -0.0293 -0.0465 0.0559 41 LYS A C 89 O O . LYS A 15 ? 0.1721 0.3221 0.3537 -0.0503 -0.0575 0.0577 41 LYS A O 90 C CB . LYS A 15 ? 0.2497 0.4193 0.4531 -0.0149 -0.0269 0.0791 41 LYS A CB 91 C CG . LYS A 15 ? 0.3171 0.4994 0.5270 0.0086 -0.0094 0.0879 41 LYS A CG 92 C CD . LYS A 15 ? 0.3207 0.5384 0.5503 0.0262 -0.0051 0.1037 41 LYS A CD 93 C CE . LYS A 15 ? 0.3845 0.6045 0.6131 0.0557 0.0149 0.1067 41 LYS A CE 94 N NZ . LYS A 15 ? 0.3846 0.6312 0.6236 0.0549 0.0244 0.1161 41 LYS A NZ 95 N N . HIS A 16 ? 0.1803 0.2788 0.3289 -0.0236 -0.0460 0.0417 42 HIS A N 96 C CA . HIS A 16 ? 0.1806 0.2603 0.3107 -0.0372 -0.0560 0.0271 42 HIS A CA 97 C C . HIS A 16 ? 0.1951 0.2562 0.3215 -0.0534 -0.0581 0.0183 42 HIS A C 98 O O . HIS A 16 ? 0.2604 0.3178 0.3803 -0.0698 -0.0686 0.0088 42 HIS A O 99 C CB . HIS A 16 ? 0.1652 0.2726 0.2985 -0.0447 -0.0684 0.0301 42 HIS A CB 100 C CG . HIS A 16 ? 0.1335 0.2532 0.2711 -0.0274 -0.0662 0.0409 42 HIS A CG 101 N ND1 . HIS A 16 ? 0.2044 0.3579 0.3664 -0.0186 -0.0642 0.0599 42 HIS A ND1 102 C CD2 . HIS A 16 ? 0.1540 0.2547 0.2762 -0.0169 -0.0650 0.0374 42 HIS A CD2 103 C CE1 . HIS A 16 ? 0.2221 0.3718 0.3833 -0.0026 -0.0618 0.0666 42 HIS A CE1 104 N NE2 . HIS A 16 ? 0.1840 0.3020 0.3214 -0.0032 -0.0632 0.0534 42 HIS A NE2 105 N N . HIS A 17 ? 0.2051 0.2534 0.3349 -0.0484 -0.0478 0.0217 43 HIS A N 106 C CA . HIS A 17 ? 0.2505 0.2729 0.3760 -0.0591 -0.0472 0.0155 43 HIS A CA 107 C C . HIS A 17 ? 0.2363 0.2296 0.3427 -0.0460 -0.0383 0.0089 43 HIS A C 108 O O . HIS A 17 ? 0.1832 0.1798 0.2849 -0.0314 -0.0306 0.0127 43 HIS A O 109 C CB . HIS A 17 ? 0.2999 0.3391 0.4480 -0.0655 -0.0428 0.0306 43 HIS A CB 110 C CG . HIS A 17 ? 0.4693 0.5418 0.6393 -0.0821 -0.0525 0.0411 43 HIS A CG 111 N ND1 . HIS A 17 ? 0.5446 0.6597 0.7381 -0.0768 -0.0478 0.0606 43 HIS A ND1 112 C CD2 . HIS A 17 ? 0.5581 0.6302 0.7296 -0.1049 -0.0671 0.0355 43 HIS A CD2 113 C CE1 . HIS A 17 ? 0.5725 0.7168 0.7839 -0.0964 -0.0596 0.0699 43 HIS A CE1 114 N NE2 . HIS A 17 ? 0.5901 0.7043 0.7820 -0.1124 -0.0704 0.0522 43 HIS A NE2 115 N N . LYS A 18 ? 0.2171 0.1816 0.3121 -0.0513 -0.0393 -0.0006 44 LYS A N 116 C CA . LYS A 18 ? 0.2002 0.1446 0.2811 -0.0397 -0.0307 -0.0019 44 LYS A CA 117 C C . LYS A 18 ? 0.1764 0.1261 0.2683 -0.0372 -0.0212 0.0110 44 LYS A C 118 O O . LYS A 18 ? 0.2091 0.1672 0.3194 -0.0471 -0.0214 0.0196 44 LYS A O 119 C CB . LYS A 18 ? 0.2695 0.1843 0.3378 -0.0422 -0.0320 -0.0128 44 LYS A CB 120 C CG . LYS A 18 ? 0.4490 0.3622 0.4996 -0.0400 -0.0387 -0.0262 44 LYS A CG 121 C CD . LYS A 18 ? 0.6192 0.5057 0.6528 -0.0332 -0.0347 -0.0356 44 LYS A CD 122 C CE . LYS A 18 ? 0.6810 0.5771 0.6994 -0.0194 -0.0319 -0.0338 44 LYS A CE 123 N NZ . LYS A 18 ? 0.7448 0.6233 0.7470 -0.0105 -0.0278 -0.0423 44 LYS A NZ 124 N N . GLU A 19 ? 0.2069 0.1547 0.2869 -0.0257 -0.0137 0.0133 45 GLU A N 125 C CA . GLU A 19 ? 0.2624 0.2201 0.3475 -0.0226 -0.0044 0.0246 45 GLU A CA 126 C C . GLU A 19 ? 0.2143 0.1599 0.2826 -0.0164 0.0003 0.0251 45 GLU A C 127 O O . GLU A 19 ? 0.2808 0.2151 0.3338 -0.0125 -0.0032 0.0176 45 GLU A O 128 C CB . GLU A 19 ? 0.2733 0.2530 0.3595 -0.0143 0.0004 0.0275 45 GLU A CB 129 C CG . GLU A 19 ? 0.3807 0.3858 0.4888 -0.0176 -0.0004 0.0350 45 GLU A CG 130 C CD . GLU A 19 ? 0.4305 0.4561 0.5379 -0.0036 0.0088 0.0385 45 GLU A CD 131 O OE1 . GLU A 19 ? 0.4515 0.4637 0.5381 0.0067 0.0129 0.0306 45 GLU A OE1 132 O OE2 . GLU A 19 ? 0.5109 0.5656 0.6379 -0.0029 0.0120 0.0493 45 GLU A OE2 133 N N . LYS A 20 ? 0.2069 0.1612 0.2787 -0.0160 0.0078 0.0364 46 LYS A N 134 C CA . LYS A 20 ? 0.2028 0.1550 0.2590 -0.0114 0.0118 0.0403 46 LYS A CA 135 C C . LYS A 20 ? 0.2328 0.1975 0.2726 -0.0067 0.0147 0.0370 46 LYS A C 136 O O . LYS A 20 ? 0.2053 0.1832 0.2498 -0.0043 0.0181 0.0360 46 LYS A O 137 C CB . LYS A 20 ? 0.2107 0.1679 0.2790 -0.0141 0.0179 0.0566 46 LYS A CB 138 C CG . LYS A 20 ? 0.3042 0.2376 0.3856 -0.0171 0.0158 0.0585 46 LYS A CG 139 C CD . LYS A 20 ? 0.3948 0.3083 0.4613 -0.0106 0.0128 0.0480 46 LYS A CD 140 C CE . LYS A 20 ? 0.4801 0.3984 0.5395 -0.0030 0.0184 0.0595 46 LYS A CE 141 N NZ . LYS A 20 ? 0.4518 0.3545 0.5002 0.0054 0.0172 0.0518 46 LYS A NZ 142 N N . PRO A 21 ? 0.2058 0.1660 0.2255 -0.0054 0.0134 0.0352 47 PRO A N 143 C CA . PRO A 21 ? 0.1956 0.1599 0.1954 -0.0037 0.0148 0.0293 47 PRO A CA 144 C C . PRO A 21 ? 0.2498 0.2347 0.2457 -0.0041 0.0233 0.0361 47 PRO A C 145 O O . PRO A 21 ? 0.2735 0.2734 0.2848 -0.0065 0.0278 0.0500 47 PRO A O 146 C CB . PRO A 21 ? 0.2259 0.1825 0.2072 -0.0070 0.0089 0.0292 47 PRO A CB 147 C CG . PRO A 21 ? 0.2297 0.1883 0.2223 -0.0073 0.0091 0.0401 47 PRO A CG 148 C CD . PRO A 21 ? 0.2147 0.1658 0.2288 -0.0055 0.0101 0.0382 47 PRO A CD 149 N N . GLY A 22 ? 0.2234 0.2083 0.1979 -0.0019 0.0254 0.0264 48 GLY A N 150 C CA . GLY A 22 ? 0.2713 0.2786 0.2357 -0.0014 0.0340 0.0294 48 GLY A CA 151 C C . GLY A 22 ? 0.2863 0.2823 0.2166 -0.0016 0.0336 0.0136 48 GLY A C 152 O O . GLY A 22 ? 0.2493 0.2190 0.1664 -0.0043 0.0254 0.0037 48 GLY A O 153 N N . PRO A 23 ? 0.2989 0.3144 0.2134 0.0003 0.0421 0.0111 49 PRO A N 154 C CA . PRO A 23 ? 0.3132 0.3121 0.1899 -0.0004 0.0420 -0.0085 49 PRO A CA 155 C C . PRO A 23 ? 0.3582 0.3228 0.2315 0.0116 0.0423 -0.0263 49 PRO A C 156 O O . PRO A 23 ? 0.3464 0.3176 0.2418 0.0253 0.0493 -0.0244 49 PRO A O 157 C CB . PRO A 23 ? 0.3839 0.4163 0.2483 0.0034 0.0540 -0.0078 49 PRO A CB 158 C CG . PRO A 23 ? 0.3879 0.4515 0.2902 0.0104 0.0615 0.0118 49 PRO A CG 159 C CD . PRO A 23 ? 0.3215 0.3752 0.2516 0.0030 0.0521 0.0260 49 PRO A CD 160 N N . GLU A 24 ? 0.3033 0.2507 0.1148 -0.0308 0.0162 0.0292 50 GLU A N 161 C CA . GLU A 24 ? 0.3165 0.2781 0.1684 -0.0270 0.0240 0.0135 50 GLU A CA 162 C C . GLU A 24 ? 0.3382 0.3251 0.1965 -0.0289 0.0479 0.0081 50 GLU A C 163 O O . GLU A 24 ? 0.4134 0.4092 0.2371 -0.0293 0.0591 0.0059 50 GLU A O 164 C CB . GLU A 24 ? 0.3033 0.2631 0.1599 -0.0178 0.0136 -0.0058 50 GLU A CB 165 C CG . GLU A 24 ? 0.2812 0.2457 0.1779 -0.0125 0.0187 -0.0191 50 GLU A CG 166 C CD . GLU A 24 ? 0.2982 0.2555 0.2035 -0.0094 0.0044 -0.0309 50 GLU A CD 167 O OE1 . GLU A 24 ? 0.3551 0.3104 0.2387 -0.0110 0.0006 -0.0467 50 GLU A OE1 168 O OE2 . GLU A 24 ? 0.2929 0.2482 0.2252 -0.0069 -0.0035 -0.0238 50 GLU A OE2 169 N N . ASP A 25 ? 0.2869 0.2897 0.1880 -0.0278 0.0563 0.0072 51 ASP A N 170 C CA . ASP A 25 ? 0.2654 0.3003 0.1809 -0.0240 0.0812 0.0026 51 ASP A CA 171 C C . ASP A 25 ? 0.2590 0.2917 0.1732 -0.0060 0.0896 -0.0250 51 ASP A C 172 O O . ASP A 25 ? 0.2975 0.3054 0.2112 -0.0013 0.0738 -0.0381 51 ASP A O 173 C CB . ASP A 25 ? 0.2591 0.3208 0.2242 -0.0297 0.0864 0.0163 51 ASP A CB 174 C CG . ASP A 25 ? 0.3319 0.3877 0.3346 -0.0197 0.0743 0.0093 51 ASP A CG 175 O OD1 . ASP A 25 ? 0.3122 0.3491 0.3119 -0.0063 0.0699 -0.0076 51 ASP A OD1 176 O OD2 . ASP A 25 ? 0.3828 0.4541 0.4183 -0.0270 0.0683 0.0223 51 ASP A OD2 177 N N . LYS A 26 ? 0.3003 0.3581 0.2146 0.0038 0.1149 -0.0332 52 LYS A N 178 C CA . LYS A 26 ? 0.3996 0.4454 0.3040 0.0232 0.1246 -0.0633 52 LYS A CA 179 C C . LYS A 26 ? 0.3886 0.4199 0.3387 0.0357 0.1183 -0.0726 52 LYS A C 180 O O . LYS A 26 ? 0.3719 0.3695 0.3115 0.0436 0.1113 -0.0955 52 LYS A O 181 C CB . LYS A 26 ? 0.4698 0.5472 0.3619 0.0369 0.1539 -0.0683 52 LYS A CB 182 C CG . LYS A 26 ? 0.5713 0.6260 0.4410 0.0595 0.1544 -0.0989 52 LYS A CG 183 C CD . LYS A 26 ? 0.6823 0.7528 0.5092 0.0699 0.1695 -0.1021 52 LYS A CD 184 C CE . LYS A 26 ? 0.7780 0.8114 0.5711 0.0868 0.1613 -0.1357 52 LYS A CE 185 N NZ . LYS A 26 ? 0.8476 0.8920 0.6365 0.0711 0.1977 -0.1599 52 LYS A NZ 186 N N . LEU A 27 ? 0.3117 0.3668 0.3112 0.0358 0.1187 -0.0536 53 LEU A N 187 C CA . LEU A 27 ? 0.3041 0.3465 0.3443 0.0481 0.1112 -0.0563 53 LEU A CA 188 C C . LEU A 27 ? 0.2939 0.2958 0.3243 0.0402 0.0869 -0.0605 53 LEU A C 189 O O . LEU A 27 ? 0.2881 0.2637 0.3323 0.0502 0.0833 -0.0717 53 LEU A O 190 C CB . LEU A 27 ? 0.2817 0.3601 0.3708 0.0462 0.1092 -0.0322 53 LEU A CB 191 C CG . LEU A 27 ? 0.2833 0.3531 0.4123 0.0623 0.1024 -0.0307 53 LEU A CG 192 C CD1 . LEU A 27 ? 0.3390 0.4531 0.5052 0.0714 0.1059 -0.0174 53 LEU A CD1 193 C CD2 . LEU A 27 ? 0.2840 0.3340 0.4150 0.0499 0.0771 -0.0184 53 LEU A CD2 194 N N . HIS A 28 ? 0.2041 0.2018 0.2129 0.0231 0.0712 -0.0496 54 HIS A N 195 C CA . HIS A 28 ? 0.1982 0.1715 0.2043 0.0167 0.0504 -0.0488 54 HIS A CA 196 C C . HIS A 28 ? 0.2485 0.2018 0.2184 0.0115 0.0425 -0.0662 54 HIS A C 197 O O . HIS A 28 ? 0.2576 0.2037 0.2221 0.0033 0.0250 -0.0612 54 HIS A O 198 C CB . HIS A 28 ? 0.1741 0.1540 0.1792 0.0063 0.0374 -0.0277 54 HIS A CB 199 C CG . HIS A 28 ? 0.1978 0.1923 0.2362 0.0082 0.0365 -0.0130 54 HIS A CG 200 N ND1 . HIS A 28 ? 0.1652 0.1861 0.2175 0.0048 0.0455 -0.0037 54 HIS A ND1 201 C CD2 . HIS A 28 ? 0.1721 0.1624 0.2316 0.0120 0.0262 -0.0048 54 HIS A CD2 202 C CE1 . HIS A 28 ? 0.2097 0.2418 0.2908 0.0059 0.0376 0.0077 54 HIS A CE1 203 N NE2 . HIS A 28 ? 0.1886 0.2005 0.2702 0.0115 0.0264 0.0070 54 HIS A NE2 204 N N . GLU A 29 ? 0.2882 0.2359 0.2335 0.0174 0.0547 -0.0872 55 GLU A N 205 C CA . GLU A 29 ? 0.3942 0.3242 0.2984 0.0108 0.0439 -0.1067 55 GLU A CA 206 C C . GLU A 29 ? 0.3705 0.2776 0.2898 0.0019 0.0223 -0.1137 55 GLU A C 207 O O . GLU A 29 ? 0.3989 0.3059 0.2965 -0.0100 0.0037 -0.1169 55 GLU A O 208 C CB . GLU A 29 ? 0.5187 0.4403 0.3921 0.0223 0.0611 -0.1327 55 GLU A CB 209 C CG . GLU A 29 ? 0.6920 0.5952 0.5206 0.0167 0.0429 -0.1493 55 GLU A CG 210 C CD . GLU A 29 ? 0.8521 0.7593 0.6358 0.0305 0.0571 -0.1615 55 GLU A CD 211 O OE1 . GLU A 29 ? 0.8858 0.8108 0.6800 0.0462 0.0827 -0.1588 55 GLU A OE1 212 O OE2 . GLU A 29 ? 0.9252 0.8214 0.6642 0.0268 0.0424 -0.1723 55 GLU A OE2 213 N N . GLN A 30 ? 0.3120 0.2037 0.2708 0.0067 0.0240 -0.1126 56 GLN A N 214 C CA . GLN A 30 ? 0.3009 0.1727 0.2782 -0.0050 0.0060 -0.1137 56 GLN A CA 215 C C . GLN A 30 ? 0.2854 0.1809 0.2814 -0.0143 -0.0079 -0.0893 56 GLN A C 216 O O . GLN A 30 ? 0.3117 0.2049 0.3228 -0.0272 -0.0233 -0.0873 56 GLN A O 217 C CB . GLN A 30 ? 0.3687 0.2187 0.3747 0.0036 0.0117 -0.1077 56 GLN A CB 218 C CG . GLN A 30 ? 0.3653 0.2342 0.4074 0.0135 0.0194 -0.0836 56 GLN A CG 219 C CD . GLN A 30 ? 0.4297 0.2828 0.4897 0.0267 0.0261 -0.0786 56 GLN A CD 220 O OE1 . GLN A 30 ? 0.4496 0.3140 0.5159 0.0438 0.0393 -0.0780 56 GLN A OE1 221 N NE2 . GLN A 30 ? 0.4900 0.3189 0.5589 0.0186 0.0170 -0.0742 56 GLN A NE2 222 N N . CYS A 31 ? 0.2804 0.1990 0.2753 -0.0078 -0.0022 -0.0703 57 CYS A N 223 C CA . CYS A 31 ? 0.2014 0.1384 0.2048 -0.0105 -0.0128 -0.0490 57 CYS A CA 224 C C . CYS A 31 ? 0.2246 0.1729 0.1978 -0.0162 -0.0258 -0.0501 57 CYS A C 225 O O . CYS A 31 ? 0.2417 0.1990 0.1963 -0.0118 -0.0263 -0.0374 57 CYS A O 226 C CB . CYS A 31 ? 0.1812 0.1281 0.1898 -0.0021 -0.0046 -0.0320 57 CYS A CB 227 S SG . CYS A 31 ? 0.2182 0.1618 0.2638 0.0066 0.0055 -0.0255 57 CYS A SG 228 N N . ARG A 32 ? 0.2476 0.1931 0.2165 -0.0267 -0.0386 -0.0643 58 ARG A N 229 C CA . ARG A 32 ? 0.2634 0.2217 0.2004 -0.0322 -0.0539 -0.0685 58 ARG A CA 230 C C . ARG A 32 ? 0.2409 0.2248 0.1794 -0.0266 -0.0648 -0.0458 58 ARG A C 231 O O . ARG A 32 ? 0.2758 0.2666 0.1800 -0.0236 -0.0719 -0.0423 58 ARG A O 232 C CB . ARG A 32 ? 0.3508 0.3029 0.2885 -0.0485 -0.0709 -0.0891 58 ARG A CB 233 C CG . ARG A 32 ? 0.5115 0.4327 0.4167 -0.0500 -0.0627 -0.1185 58 ARG A CG 234 C CD . ARG A 32 ? 0.6601 0.5735 0.5600 -0.0694 -0.0760 -0.1336 58 ARG A CD 235 N NE . ARG A 32 ? 0.7809 0.6674 0.6303 -0.0672 -0.0689 -0.1538 58 ARG A NE 236 C CZ . ARG A 32 ? 0.8707 0.7806 0.6950 -0.0761 -0.0786 -0.1661 58 ARG A CZ 237 N NH1 . ARG A 32 ? 0.8752 0.8308 0.7217 -0.0789 -0.1026 -0.1593 58 ARG A NH1 238 N NH2 . ARG A 32 ? 0.9522 0.8168 0.7155 -0.0712 -0.0750 -0.1791 58 ARG A NH2 239 N N . PRO A 33 ? 0.2196 0.2170 0.1948 -0.0224 -0.0655 -0.0294 59 PRO A N 240 C CA . PRO A 33 ? 0.2206 0.2411 0.1946 -0.0114 -0.0745 -0.0107 59 PRO A CA 241 C C . PRO A 33 ? 0.2184 0.2230 0.1599 0.0021 -0.0674 -0.0005 59 PRO A C 242 O O . PRO A 33 ? 0.2648 0.2777 0.1919 0.0131 -0.0766 0.0123 59 PRO A O 243 C CB . PRO A 33 ? 0.1955 0.2316 0.2109 -0.0066 -0.0699 0.0028 59 PRO A CB 244 C CG . PRO A 33 ? 0.1951 0.2264 0.2386 -0.0249 -0.0702 -0.0081 59 PRO A CG 245 C CD . PRO A 33 ? 0.2134 0.2098 0.2305 -0.0272 -0.0608 -0.0265 59 PRO A CD 246 N N . TRP A 34 ? 0.2437 0.2259 0.1765 0.0009 -0.0523 -0.0044 60 TRP A N 247 C CA . TRP A 34 ? 0.2321 0.1969 0.1414 0.0076 -0.0463 0.0072 60 TRP A CA 248 C C . TRP A 34 ? 0.2968 0.2524 0.1708 0.0006 -0.0409 0.0045 60 TRP A C 249 O O . TRP A 34 ? 0.3553 0.2956 0.2144 -0.0003 -0.0337 0.0149 60 TRP A O 250 C CB . TRP A 34 ? 0.2387 0.1930 0.1670 0.0089 -0.0353 0.0097 60 TRP A CB 251 C CG . TRP A 34 ? 0.1937 0.1569 0.1460 0.0185 -0.0385 0.0162 60 TRP A CG 252 C CD1 . TRP A 34 ? 0.2209 0.1828 0.1693 0.0304 -0.0392 0.0254 60 TRP A CD1 253 C CD2 . TRP A 34 ? 0.1704 0.1489 0.1563 0.0160 -0.0364 0.0137 60 TRP A CD2 254 N NE1 . TRP A 34 ? 0.2291 0.2100 0.2040 0.0354 -0.0355 0.0290 60 TRP A NE1 255 C CE2 . TRP A 34 ? 0.1955 0.1849 0.1919 0.0285 -0.0371 0.0254 60 TRP A CE2 256 C CE3 . TRP A 34 ? 0.1797 0.1593 0.1857 0.0052 -0.0330 0.0034 60 TRP A CE3 257 C CZ2 . TRP A 34 ? 0.1886 0.1966 0.2165 0.0278 -0.0335 0.0311 60 TRP A CZ2 258 C CZ3 . TRP A 34 ? 0.1943 0.1837 0.2325 0.0035 -0.0321 0.0088 60 TRP A CZ3 259 C CH2 . TRP A 34 ? 0.1633 0.1698 0.2129 0.0134 -0.0317 0.0245 60 TRP A CH2 260 N N . ARG A 35 ? 0.3364 0.2598 0.1246 0.0210 -0.0377 -0.0444 61 ARG A N 261 C CA . ARG A 35 ? 0.3776 0.3064 0.1261 0.0212 -0.0292 -0.0331 61 ARG A CA 262 C C . ARG A 35 ? 0.4047 0.3227 0.1376 0.0234 -0.0326 -0.0046 61 ARG A C 263 O O . ARG A 35 ? 0.4307 0.3509 0.1546 0.0208 -0.0166 0.0099 61 ARG A O 264 C CB . ARG A 35 ? 0.4527 0.4034 0.1891 0.0156 -0.0318 -0.0393 61 ARG A CB 265 C CG . ARG A 35 ? 0.5912 0.5500 0.2906 0.0132 -0.0192 -0.0321 61 ARG A CG 266 C CD . ARG A 35 ? 0.7314 0.7099 0.4210 0.0035 -0.0200 -0.0461 61 ARG A CD 267 N NE . ARG A 35 ? 0.8453 0.8328 0.5276 0.0004 -0.0418 -0.0410 61 ARG A NE 268 C CZ . ARG A 35 ? 0.9462 0.9480 0.5938 -0.0035 -0.0497 -0.0317 61 ARG A CZ 269 N NH1 . ARG A 35 ? 0.9840 0.9893 0.6007 -0.0037 -0.0351 -0.0279 61 ARG A NH1 270 N NH2 . ARG A 35 ? 0.9654 0.9794 0.6127 -0.0057 -0.0718 -0.0252 61 ARG A NH2 271 N N . LYS A 36 ? 0.3821 0.2941 0.1283 0.0265 -0.0495 0.0061 62 LYS A N 272 C CA . LYS A 36 ? 0.4708 0.3770 0.2132 0.0281 -0.0508 0.0367 62 LYS A CA 273 C C . LYS A 36 ? 0.4604 0.3466 0.2399 0.0244 -0.0434 0.0485 62 LYS A C 274 O O . LYS A 36 ? 0.5027 0.3801 0.2796 0.0227 -0.0359 0.0731 62 LYS A O 275 C CB . LYS A 36 ? 0.5404 0.4530 0.2737 0.0356 -0.0727 0.0474 62 LYS A CB 276 C CG . LYS A 36 ? 0.6529 0.5875 0.3432 0.0345 -0.0790 0.0467 62 LYS A CG 277 C CD . LYS A 36 ? 0.7782 0.7117 0.4355 0.0308 -0.0604 0.0620 62 LYS A CD 278 C CE . LYS A 36 ? 0.8691 0.8240 0.4978 0.0282 -0.0680 0.0763 62 LYS A CE 279 N NZ . LYS A 36 ? 0.9189 0.8628 0.5294 0.0291 -0.0565 0.1075 62 LYS A NZ 280 N N . ASN A 37 ? 0.3691 0.2452 0.1796 0.0218 -0.0446 0.0307 63 ASN A N 281 C CA . ASN A 37 ? 0.3716 0.2242 0.2123 0.0154 -0.0390 0.0381 63 ASN A CA 282 C C . ASN A 37 ? 0.3698 0.2191 0.2302 0.0087 -0.0358 0.0148 63 ASN A C 283 O O . ASN A 37 ? 0.3941 0.2365 0.2648 0.0120 -0.0436 -0.0028 63 ASN A O 284 C CB . ASN A 37 ? 0.3507 0.1842 0.2069 0.0224 -0.0489 0.0472 63 ASN A CB 285 C CG . ASN A 37 ? 0.4446 0.2460 0.3227 0.0149 -0.0395 0.0582 63 ASN A CG 286 O OD1 . ASN A 37 ? 0.4860 0.2817 0.3608 0.0063 -0.0283 0.0736 63 ASN A OD1 287 N ND2 . ASN A 37 ? 0.4063 0.1842 0.3059 0.0169 -0.0422 0.0499 63 ASN A ND2 288 N N . ALA A 38 ? 0.3177 0.1737 0.1842 -0.0006 -0.0241 0.0160 64 ALA A N 289 C CA . ALA A 38 ? 0.2776 0.1386 0.1590 -0.0052 -0.0222 -0.0035 64 ALA A CA 290 C C . ALA A 38 ? 0.2766 0.1333 0.1807 -0.0197 -0.0159 0.0040 64 ALA A C 291 O O . ALA A 38 ? 0.2958 0.1557 0.2016 -0.0266 -0.0073 0.0231 64 ALA A O 292 C CB . ALA A 38 ? 0.2972 0.1835 0.1631 0.0007 -0.0147 -0.0127 64 ALA A CB 293 N N . CYS A 39 ? 0.2543 0.1048 0.1744 -0.0257 -0.0204 -0.0109 65 CYS A N 294 C CA . CYS A 39 ? 0.2540 0.1081 0.1957 -0.0419 -0.0180 -0.0063 65 CYS A CA 295 C C . CYS A 39 ? 0.2457 0.1359 0.1975 -0.0398 -0.0104 -0.0062 65 CYS A C 296 O O . CYS A 39 ? 0.3025 0.2070 0.2776 -0.0525 -0.0086 0.0010 65 CYS A O 297 C CB . CYS A 39 ? 0.2639 0.1125 0.2215 -0.0452 -0.0241 -0.0198 65 CYS A CB 298 S SG . CYS A 39 ? 0.3034 0.1471 0.2724 -0.0397 -0.0189 -0.0175 65 CYS A SG 299 N N . CYS A 40 ? 0.2710 0.1754 0.2068 -0.0245 -0.0056 -0.0144 66 CYS A N 300 C CA . CYS A 40 ? 0.2380 0.1729 0.1816 -0.0190 0.0069 -0.0138 66 CYS A CA 301 C C . CYS A 40 ? 0.2924 0.2382 0.2188 -0.0155 0.0213 0.0009 66 CYS A C 302 O O . CYS A 40 ? 0.3006 0.2507 0.1998 -0.0037 0.0287 -0.0056 66 CYS A O 303 C CB . CYS A 40 ? 0.2266 0.1625 0.1587 -0.0051 0.0070 -0.0341 66 CYS A CB 304 S SG . CYS A 40 ? 0.2797 0.1979 0.1729 0.0061 0.0025 -0.0483 66 CYS A SG 305 N N . SER A 41 ? 0.2955 0.2429 0.2346 -0.0275 0.0259 0.0204 67 SER A N 306 C CA . SER A 41 ? 0.3051 0.2514 0.2221 -0.0263 0.0369 0.0376 67 SER A CA 307 C C . SER A 41 ? 0.3461 0.3188 0.2781 -0.0306 0.0581 0.0531 67 SER A C 308 O O . SER A 41 ? 0.3139 0.3078 0.2834 -0.0378 0.0615 0.0544 67 SER A O 309 C CB . SER A 41 ? 0.3426 0.2622 0.2597 -0.0360 0.0289 0.0506 67 SER A CB 310 O OG . SER A 41 ? 0.3904 0.3098 0.3411 -0.0541 0.0293 0.0576 67 SER A OG 311 N N . THR A 42 ? 0.3790 0.3514 0.2817 -0.0262 0.0721 0.0662 68 THR A N 312 C CA . THR A 42 ? 0.4907 0.4834 0.4045 -0.0309 0.0961 0.0841 68 THR A CA 313 C C . THR A 42 ? 0.5353 0.5258 0.4830 -0.0503 0.0959 0.1020 68 THR A C 314 O O . THR A 42 ? 0.4624 0.4271 0.4113 -0.0583 0.0795 0.1024 68 THR A O 315 C CB . THR A 42 ? 0.5688 0.5541 0.4327 -0.0228 0.1109 0.0945 68 THR A CB 316 O OG1 . THR A 42 ? 0.5620 0.5208 0.4020 -0.0252 0.0977 0.1059 68 THR A OG1 317 C CG2 . THR A 42 ? 0.5723 0.5581 0.3988 -0.0075 0.1122 0.0744 68 THR A CG2 318 N N . ASN A 43 ? 0.6105 0.6266 0.5868 -0.0584 0.1160 0.1166 69 ASN A N 319 C CA . ASN A 43 ? 0.6860 0.7026 0.6975 -0.0805 0.1176 0.1331 69 ASN A CA 320 C C . ASN A 43 ? 0.7413 0.7541 0.7395 -0.0853 0.1415 0.1574 69 ASN A C 321 O O . ASN A 43 ? 0.7704 0.8005 0.7553 -0.0755 0.1646 0.1638 69 ASN A O 322 C CB . ASN A 43 ? 0.6983 0.7531 0.7676 -0.0916 0.1181 0.1320 69 ASN A CB 323 C CG . ASN A 43 ? 0.6968 0.7549 0.7774 -0.0869 0.0953 0.1106 69 ASN A CG 324 O OD1 . ASN A 43 ? 0.5935 0.6196 0.6515 -0.0862 0.0756 0.0978 69 ASN A OD1 325 N ND2 . ASN A 43 ? 0.7912 0.8876 0.9076 -0.0824 0.0994 0.1081 69 ASN A ND2 326 N N . THR A 44 ? 0.7608 0.7474 0.7609 -0.1008 0.1384 0.1710 70 THR A N 327 C CA . THR A 44 ? 0.7760 0.7520 0.7605 -0.1060 0.1611 0.1963 70 THR A CA 328 C C . THR A 44 ? 0.7357 0.7425 0.7640 -0.1221 0.1774 0.2029 70 THR A C 329 O O . THR A 44 ? 0.7809 0.7874 0.7950 -0.1230 0.1962 0.2151 70 THR A O 330 C CB . THR A 44 ? 0.8316 0.7628 0.7986 -0.1138 0.1498 0.2041 70 THR A CB 331 O OG1 . THR A 44 ? 0.8259 0.7503 0.8321 -0.1359 0.1376 0.1960 70 THR A OG1 332 C CG2 . THR A 44 ? 0.8271 0.7316 0.7548 -0.0955 0.1312 0.1963 70 THR A CG2 333 N N . SER A 45 ? 0.6397 0.6739 0.7202 -0.1348 0.1678 0.1937 71 SER A N 334 C CA . SER A 45 ? 0.5963 0.6652 0.7235 -0.1495 0.1787 0.1978 71 SER A CA 335 C C . SER A 45 ? 0.5717 0.6890 0.7338 -0.1379 0.1835 0.1911 71 SER A C 336 O O . SER A 45 ? 0.5014 0.6224 0.6531 -0.1219 0.1762 0.1814 71 SER A O 337 C CB . SER A 45 ? 0.5464 0.6069 0.7048 -0.1761 0.1610 0.1920 71 SER A CB 338 O OG . SER A 45 ? 0.5234 0.5866 0.6966 -0.1777 0.1357 0.1758 71 SER A OG 339 N N . GLN A 46 ? 0.6027 0.7562 0.8068 -0.1453 0.1962 0.1966 72 GLN A N 340 C CA . GLN A 46 ? 0.5806 0.7803 0.8221 -0.1320 0.2025 0.1923 72 GLN A CA 341 C C . GLN A 46 ? 0.5444 0.7682 0.8305 -0.1404 0.1746 0.1825 72 GLN A C 342 O O . GLN A 46 ? 0.5581 0.8222 0.8950 -0.1460 0.1727 0.1847 72 GLN A O 343 C CB . GLN A 46 ? 0.6015 0.8311 0.8727 -0.1348 0.2270 0.2034 72 GLN A CB 344 C CG . GLN A 46 ? 0.6584 0.8704 0.8827 -0.1204 0.2569 0.2103 72 GLN A CG 345 C CD . GLN A 46 ? 0.7220 0.8882 0.8963 -0.1298 0.2578 0.2186 72 GLN A CD 346 O OE1 . GLN A 46 ? 0.7489 0.9059 0.9389 -0.1521 0.2526 0.2260 72 GLN A OE1 347 N NE2 . GLN A 46 ? 0.7211 0.8570 0.8327 -0.1128 0.2633 0.2167 72 GLN A NE2 348 N N . GLU A 47 ? 0.5123 0.7104 0.7772 -0.1411 0.1519 0.1721 73 GLU A N 349 C CA . GLU A 47 ? 0.4916 0.7064 0.7863 -0.1469 0.1236 0.1606 73 GLU A CA 350 C C . GLU A 47 ? 0.5107 0.7665 0.8317 -0.1244 0.1304 0.1588 73 GLU A C 351 O O . GLU A 47 ? 0.4976 0.7494 0.7925 -0.1010 0.1511 0.1578 73 GLU A O 352 C CB . GLU A 47 ? 0.4459 0.6193 0.7046 -0.1487 0.1019 0.1487 73 GLU A CB 353 N N . ALA A 48 ? 0.5246 0.8157 0.8917 -0.1303 0.1134 0.1572 74 ALA A N 354 C CA . ALA A 48 ? 0.5094 0.8372 0.9046 -0.1077 0.1181 0.1568 74 ALA A CA 355 C C . ALA A 48 ? 0.4964 0.8064 0.8605 -0.0863 0.1163 0.1449 74 ALA A C 356 O O . ALA A 48 ? 0.4379 0.7232 0.7818 -0.0945 0.0933 0.1350 74 ALA A O 357 C CB . ALA A 48 ? 0.4822 0.8450 0.9248 -0.1187 0.0929 0.1579 74 ALA A CB 358 N N . HIS A 49 ? 0.5558 0.8733 0.9118 -0.0591 0.1419 0.1437 75 HIS A N 359 C CA . HIS A 49 ? 0.5768 0.8739 0.8982 -0.0369 0.1452 0.1294 75 HIS A CA 360 C C . HIS A 49 ? 0.5273 0.8455 0.8788 -0.0264 0.1267 0.1239 75 HIS A C 361 O O . HIS A 49 ? 0.5349 0.8793 0.9162 -0.0128 0.1353 0.1290 75 HIS A O 362 C CB . HIS A 49 ? 0.6348 0.9177 0.9198 -0.0136 0.1796 0.1249 75 HIS A CB 363 N N . LYS A 50 ? 0.4815 0.7721 0.8082 -0.0322 0.0964 0.1086 76 LYS A N 364 C CA . LYS A 50 ? 0.4594 0.7598 0.8004 -0.0197 0.0801 0.1020 76 LYS A CA 365 C C . LYS A 50 ? 0.4458 0.6916 0.7248 -0.0133 0.0661 0.0770 76 LYS A C 366 O O . LYS A 50 ? 0.4388 0.6550 0.6931 -0.0317 0.0434 0.0684 76 LYS A O 367 C CB . LYS A 50 ? 0.4341 0.7696 0.8247 -0.0412 0.0505 0.1138 76 LYS A CB 368 N N . ASP A 51 ? 0.4520 0.6830 0.7070 0.0124 0.0821 0.0652 77 ASP A N 369 C CA . ASP A 51 ? 0.4683 0.6519 0.6708 0.0191 0.0707 0.0415 77 ASP A CA 370 C C . ASP A 51 ? 0.3687 0.5522 0.5840 0.0145 0.0421 0.0378 77 ASP A C 371 O O . ASP A 51 ? 0.3533 0.5679 0.6062 0.0251 0.0418 0.0478 77 ASP A O 372 C CB . ASP A 51 ? 0.5709 0.7391 0.7462 0.0452 0.0968 0.0293 77 ASP A CB 373 C CG . ASP A 51 ? 0.6967 0.8630 0.8518 0.0496 0.1265 0.0323 77 ASP A CG 374 O OD1 . ASP A 51 ? 0.7504 0.9065 0.8870 0.0339 0.1222 0.0360 77 ASP A OD1 375 O OD2 . ASP A 51 ? 0.7240 0.8954 0.8783 0.0692 0.1557 0.0312 77 ASP A OD2 376 N N . VAL A 52 ? 0.2644 0.4126 0.4484 -0.0007 0.0192 0.0250 78 VAL A N 377 C CA . VAL A 52 ? 0.2172 0.3554 0.4000 -0.0045 -0.0055 0.0184 78 VAL A CA 378 C C . VAL A 52 ? 0.2101 0.3024 0.3457 0.0084 -0.0048 -0.0045 78 VAL A C 379 O O . VAL A 52 ? 0.2608 0.3334 0.3837 0.0058 -0.0222 -0.0133 78 VAL A O 380 C CB . VAL A 52 ? 0.1999 0.3317 0.3857 -0.0344 -0.0321 0.0209 78 VAL A CB 381 C CG1 . VAL A 52 ? 0.2239 0.4033 0.4600 -0.0511 -0.0339 0.0431 78 VAL A CG1 382 C CG2 . VAL A 52 ? 0.2170 0.3023 0.3604 -0.0453 -0.0335 0.0075 78 VAL A CG2 383 N N . SER A 53 ? 0.1863 0.2620 0.2949 0.0213 0.0159 -0.0141 79 SER A N 384 C CA . SER A 53 ? 0.1831 0.2185 0.2496 0.0314 0.0175 -0.0364 79 SER A CA 385 C C . SER A 53 ? 0.1915 0.2232 0.2614 0.0481 0.0197 -0.0424 79 SER A C 386 O O . SER A 53 ? 0.1882 0.2497 0.2896 0.0607 0.0306 -0.0296 79 SER A O 387 C CB . SER A 53 ? 0.2143 0.2393 0.2528 0.0406 0.0386 -0.0440 79 SER A CB 388 O OG . SER A 53 ? 0.2316 0.2220 0.2332 0.0480 0.0389 -0.0657 79 SER A OG 389 N N . TYR A 54 ? 0.1954 0.1903 0.2353 0.0488 0.0110 -0.0604 80 TYR A N 390 C CA . TYR A 54 ? 0.1822 0.1642 0.2137 0.0607 0.0170 -0.0622 80 TYR A CA 391 C C . TYR A 54 ? 0.2410 0.2050 0.2472 0.0592 0.0418 -0.0543 80 TYR A C 392 O O . TYR A 54 ? 0.2323 0.1930 0.2462 0.0570 0.0501 -0.0501 80 TYR A O 393 C CB . TYR A 54 ? 0.1713 0.1261 0.1753 0.0427 0.0035 -0.0603 80 TYR A CB 394 C CG . TYR A 54 ? 0.2193 0.1758 0.2405 0.0443 -0.0200 -0.0657 80 TYR A CG 395 C CD1 . TYR A 54 ? 0.2283 0.2224 0.2891 0.0445 -0.0297 -0.0500 80 TYR A CD1 396 C CD2 . TYR A 54 ? 0.2425 0.1844 0.2407 0.0301 -0.0238 -0.0585 80 TYR A CD2 397 C CE1 . TYR A 54 ? 0.2442 0.2463 0.3142 0.0334 -0.0530 -0.0403 80 TYR A CE1 398 C CE2 . TYR A 54 ? 0.2872 0.2233 0.2899 0.0282 -0.0464 -0.0609 80 TYR A CE2 399 C CZ . TYR A 54 ? 0.3118 0.2741 0.3478 0.0275 -0.0655 -0.0533 80 TYR A CZ 400 O OH . TYR A 54 ? 0.3821 0.3488 0.4186 0.0149 -0.0893 -0.0445 80 TYR A OH 401 N N . LEU A 55 ? 0.1581 0.1744 0.1888 0.0253 0.0075 -0.0038 81 LEU A N 402 C CA . LEU A 55 ? 0.1743 0.1968 0.1987 0.0264 0.0054 -0.0028 81 LEU A CA 403 C C . LEU A 55 ? 0.2470 0.2719 0.2693 0.0255 0.0047 -0.0050 81 LEU A C 404 O O . LEU A 55 ? 0.3031 0.3297 0.3201 0.0258 0.0012 -0.0091 81 LEU A O 405 C CB . LEU A 55 ? 0.1655 0.1922 0.1835 0.0331 0.0077 0.0031 81 LEU A CB 406 C CG . LEU A 55 ? 0.1696 0.1953 0.1860 0.0363 0.0084 0.0067 81 LEU A CG 407 C CD1 . LEU A 55 ? 0.2202 0.2494 0.2299 0.0442 0.0130 0.0159 81 LEU A CD1 408 C CD2 . LEU A 55 ? 0.1972 0.2317 0.2129 0.0349 0.0032 0.0036 81 LEU A CD2 409 N N . TYR A 56 ? 0.1913 0.2178 0.2178 0.0258 0.0080 -0.0032 82 TYR A N 410 C CA . TYR A 56 ? 0.1949 0.2240 0.2189 0.0268 0.0086 -0.0041 82 TYR A CA 411 C C . TYR A 56 ? 0.1885 0.2199 0.2222 0.0231 0.0091 -0.0041 82 TYR A C 412 O O . TYR A 56 ? 0.1844 0.2217 0.2191 0.0249 0.0110 -0.0023 82 TYR A O 413 C CB . TYR A 56 ? 0.1836 0.2191 0.2022 0.0327 0.0129 0.0008 82 TYR A CB 414 C CG . TYR A 56 ? 0.2003 0.2379 0.2071 0.0385 0.0120 0.0014 82 TYR A CG 415 C CD1 . TYR A 56 ? 0.1888 0.2279 0.1962 0.0406 0.0140 0.0075 82 TYR A CD1 416 C CD2 . TYR A 56 ? 0.2128 0.2521 0.2073 0.0436 0.0090 -0.0046 82 TYR A CD2 417 C CE1 . TYR A 56 ? 0.2007 0.2469 0.1970 0.0475 0.0127 0.0093 82 TYR A CE1 418 C CE2 . TYR A 56 ? 0.1975 0.2449 0.1806 0.0503 0.0066 -0.0057 82 TYR A CE2 419 C CZ . TYR A 56 ? 0.2071 0.2605 0.1916 0.0524 0.0083 0.0022 82 TYR A CZ 420 O OH . TYR A 56 ? 0.2697 0.3372 0.2430 0.0606 0.0056 0.0027 82 TYR A OH 421 N N . ARG A 57 ? 0.2336 0.2629 0.2714 0.0196 0.0077 -0.0038 83 ARG A N 422 C CA . ARG A 57 ? 0.2326 0.2704 0.2760 0.0170 0.0064 -0.0032 83 ARG A CA 423 C C . ARG A 57 ? 0.2135 0.2464 0.2518 0.0149 0.0026 -0.0062 83 ARG A C 424 O O . ARG A 57 ? 0.2653 0.3021 0.3054 0.0153 0.0023 -0.0043 83 ARG A O 425 C CB . ARG A 57 ? 0.2919 0.3351 0.3500 0.0112 0.0074 -0.0051 83 ARG A CB 426 C CG . ARG A 57 ? 0.3998 0.4493 0.4648 0.0026 0.0033 -0.0085 83 ARG A CG 427 C CD . ARG A 57 ? 0.5121 0.5566 0.5833 -0.0084 0.0048 -0.0071 83 ARG A CD 428 N NE . ARG A 57 ? 0.6113 0.6518 0.6826 -0.0188 -0.0004 -0.0148 83 ARG A NE 429 C CZ . ARG A 57 ? 0.6791 0.6965 0.7436 -0.0238 0.0003 -0.0203 83 ARG A CZ 430 N NH1 . ARG A 57 ? 0.6606 0.6592 0.7198 -0.0180 0.0066 -0.0164 83 ARG A NH1 431 N NH2 . ARG A 57 ? 0.7253 0.7379 0.7865 -0.0332 -0.0049 -0.0297 83 ARG A NH2 432 N N . PHE A 58 ? 0.1510 0.1767 0.1845 0.0140 0.0009 -0.0091 84 PHE A N 433 C CA . PHE A 58 ? 0.1348 0.1592 0.1656 0.0127 -0.0013 -0.0104 84 PHE A CA 434 C C . PHE A 58 ? 0.1553 0.1768 0.1829 0.0140 -0.0010 -0.0086 84 PHE A C 435 O O . PHE A 58 ? 0.2016 0.2201 0.2271 0.0149 -0.0012 -0.0099 84 PHE A O 436 C CB . PHE A 58 ? 0.1544 0.1754 0.1834 0.0127 -0.0019 -0.0127 84 PHE A CB 437 C CG . PHE A 58 ? 0.1568 0.1802 0.1846 0.0129 -0.0032 -0.0138 84 PHE A CG 438 C CD1 . PHE A 58 ? 0.1863 0.2154 0.2171 0.0131 -0.0050 -0.0197 84 PHE A CD1 439 C CD2 . PHE A 58 ? 0.1837 0.2070 0.2100 0.0133 -0.0026 -0.0101 84 PHE A CD2 440 C CE1 . PHE A 58 ? 0.2036 0.2382 0.2311 0.0153 -0.0060 -0.0206 84 PHE A CE1 441 C CE2 . PHE A 58 ? 0.1646 0.1923 0.1914 0.0146 -0.0025 -0.0091 84 PHE A CE2 442 C CZ . PHE A 58 ? 0.1412 0.1743 0.1663 0.0164 -0.0041 -0.0138 84 PHE A CZ 443 N N . ASN A 59 ? 0.1432 0.1671 0.1726 0.0149 -0.0009 -0.0068 85 ASN A N 444 C CA . ASN A 59 ? 0.1326 0.1530 0.1624 0.0177 0.0002 -0.0058 85 ASN A CA 445 C C . ASN A 59 ? 0.1570 0.1773 0.1886 0.0167 -0.0013 -0.0063 85 ASN A C 446 O O . ASN A 59 ? 0.1581 0.1830 0.1923 0.0176 -0.0005 -0.0025 85 ASN A O 447 C CB . ASN A 59 ? 0.1362 0.1600 0.1717 0.0209 0.0024 -0.0016 85 ASN A CB 448 C CG . ASN A 59 ? 0.1473 0.1631 0.1845 0.0248 0.0042 -0.0014 85 ASN A CG 449 O OD1 . ASN A 59 ? 0.1739 0.1798 0.2043 0.0278 0.0046 -0.0046 85 ASN A OD1 450 N ND2 . ASN A 59 ? 0.1646 0.1852 0.2043 0.0293 0.0025 -0.0010 85 ASN A ND2 451 N N . TRP A 60 ? 0.1583 0.1766 0.1918 0.0151 -0.0036 -0.0104 86 TRP A N 452 C CA . TRP A 60 ? 0.1406 0.1634 0.1822 0.0133 -0.0053 -0.0101 86 TRP A CA 453 C C . TRP A 60 ? 0.1592 0.1768 0.2101 0.0136 -0.0047 -0.0082 86 TRP A C 454 O O . TRP A 60 ? 0.1518 0.1742 0.2087 0.0102 -0.0040 -0.0027 86 TRP A O 455 C CB . TRP A 60 ? 0.1574 0.1842 0.2029 0.0107 -0.0092 -0.0145 86 TRP A CB 456 C CG . TRP A 60 ? 0.1937 0.2203 0.2292 0.0123 -0.0080 -0.0141 86 TRP A CG 457 C CD1 . TRP A 60 ? 0.2333 0.2584 0.2649 0.0144 -0.0090 -0.0181 86 TRP A CD1 458 C CD2 . TRP A 60 ? 0.1966 0.2239 0.2275 0.0131 -0.0051 -0.0094 86 TRP A CD2 459 N NE1 . TRP A 60 ? 0.2227 0.2484 0.2493 0.0156 -0.0065 -0.0141 86 TRP A NE1 460 C CE2 . TRP A 60 ? 0.2453 0.2708 0.2725 0.0148 -0.0045 -0.0099 86 TRP A CE2 461 C CE3 . TRP A 60 ? 0.1467 0.1759 0.1781 0.0137 -0.0031 -0.0057 86 TRP A CE3 462 C CZ2 . TRP A 60 ? 0.2124 0.2360 0.2385 0.0168 -0.0017 -0.0071 86 TRP A CZ2 463 C CZ3 . TRP A 60 ? 0.1555 0.1823 0.1843 0.0162 -0.0011 -0.0055 86 TRP A CZ3 464 C CH2 . TRP A 60 ? 0.2172 0.2404 0.2439 0.0176 -0.0002 -0.0061 86 TRP A CH2 465 N N . ASN A 61 ? 0.1493 0.1530 0.1953 0.0167 -0.0028 -0.0101 87 ASN A N 466 C CA . ASN A 61 ? 0.1869 0.1746 0.2329 0.0164 0.0004 -0.0065 87 ASN A CA 467 C C . ASN A 61 ? 0.2001 0.1915 0.2475 0.0255 0.0052 0.0022 87 ASN A C 468 O O . ASN A 61 ? 0.2171 0.1932 0.2602 0.0304 0.0095 0.0052 87 ASN A O 469 C CB . ASN A 61 ? 0.2145 0.1799 0.2510 0.0162 0.0007 -0.0144 87 ASN A CB 470 C CG . ASN A 61 ? 0.3177 0.2843 0.3512 0.0074 -0.0055 -0.0232 87 ASN A CG 471 O OD1 . ASN A 61 ? 0.3107 0.2812 0.3508 -0.0031 -0.0093 -0.0227 87 ASN A OD1 472 N ND2 . ASN A 61 ? 0.4439 0.4118 0.4684 0.0122 -0.0064 -0.0296 87 ASN A ND2 473 N N . HIS A 62 ? 0.1612 0.1727 0.2083 0.0264 0.0037 0.0052 88 HIS A N 474 C CA . HIS A 62 ? 0.1420 0.1612 0.1849 0.0306 0.0048 0.0103 88 HIS A CA 475 C C . HIS A 62 ? 0.1457 0.1595 0.1927 0.0342 0.0104 0.0217 88 HIS A C 476 O O . HIS A 62 ? 0.1881 0.2038 0.2309 0.0397 0.0133 0.0277 88 HIS A O 477 C CB . HIS A 62 ? 0.1299 0.1634 0.1703 0.0272 0.0013 0.0073 88 HIS A CB 478 C CG . HIS A 62 ? 0.1163 0.1535 0.1579 0.0239 0.0006 0.0066 88 HIS A CG 479 N ND1 . HIS A 62 ? 0.1169 0.1517 0.1600 0.0195 -0.0014 0.0008 88 HIS A ND1 480 C CD2 . HIS A 62 ? 0.1191 0.1632 0.1609 0.0251 0.0029 0.0131 88 HIS A CD2 481 C CE1 . HIS A 62 ? 0.1521 0.1920 0.1947 0.0189 -0.0007 0.0024 88 HIS A CE1 482 N NE2 . HIS A 62 ? 0.1378 0.1843 0.1797 0.0221 0.0019 0.0097 88 HIS A NE2 483 N N . CYS A 63 ? 0.1489 0.1569 0.2065 0.0302 0.0122 0.0263 89 CYS A N 484 C CA . CYS A 63 ? 0.1409 0.1386 0.2026 0.0302 0.0180 0.0383 89 CYS A CA 485 C C . CYS A 63 ? 0.2492 0.2169 0.3123 0.0203 0.0192 0.0353 89 CYS A C 486 O O . CYS A 63 ? 0.4002 0.3612 0.4710 0.0120 0.0218 0.0429 89 CYS A O 487 C CB . CYS A 63 ? 0.1672 0.1851 0.2349 0.0278 0.0188 0.0466 89 CYS A CB 488 S SG . CYS A 63 ? 0.1682 0.2112 0.2228 0.0365 0.0186 0.0487 89 CYS A SG 489 N N . GLY A 64 ? 0.3033 0.2533 0.3586 0.0208 0.0175 0.0242 90 GLY A N 490 C CA . GLY A 64 ? 0.3454 0.2640 0.3975 0.0110 0.0174 0.0174 90 GLY A CA 491 C C . GLY A 64 ? 0.2934 0.2206 0.3456 -0.0006 0.0087 0.0047 90 GLY A C 492 O O . GLY A 64 ? 0.2965 0.2499 0.3510 0.0014 0.0048 0.0031 90 GLY A O 493 N N . GLU A 65 ? 0.3302 0.2352 0.3792 -0.0129 0.0055 -0.0041 91 GLU A N 494 C CA . GLU A 65 ? 0.3215 0.2379 0.3691 -0.0230 -0.0037 -0.0157 91 GLU A CA 495 C C . GLU A 65 ? 0.2642 0.2138 0.3274 -0.0308 -0.0078 -0.0088 91 GLU A C 496 O O . GLU A 65 ? 0.3150 0.2677 0.3909 -0.0411 -0.0068 -0.0003 91 GLU A O 497 C CB . GLU A 65 ? 0.4042 0.2956 0.4387 -0.0355 -0.0071 -0.0255 91 GLU A CB 498 C CG . GLU A 65 ? 0.5016 0.4044 0.5271 -0.0420 -0.0156 -0.0380 91 GLU A CG 499 C CD . GLU A 65 ? 0.6120 0.4909 0.6206 -0.0558 -0.0188 -0.0475 91 GLU A CD 500 O OE1 . GLU A 65 ? 0.6504 0.4958 0.6467 -0.0533 -0.0154 -0.0473 91 GLU A OE1 501 O OE2 . GLU A 65 ? 0.6324 0.5296 0.6409 -0.0669 -0.0261 -0.0539 91 GLU A OE2 502 N N . MET A 66 ? 0.1998 0.1738 0.2621 -0.0249 -0.0110 -0.0111 92 MET A N 503 C CA . MET A 66 ? 0.1681 0.1719 0.2424 -0.0295 -0.0142 -0.0057 92 MET A CA 504 C C . MET A 66 ? 0.2126 0.2205 0.2903 -0.0446 -0.0225 -0.0124 92 MET A C 505 O O . MET A 66 ? 0.2563 0.2517 0.3203 -0.0458 -0.0266 -0.0241 92 MET A O 506 C CB . MET A 66 ? 0.1350 0.1566 0.2049 -0.0177 -0.0142 -0.0067 92 MET A CB 507 C CG . MET A 66 ? 0.1049 0.1550 0.1843 -0.0190 -0.0163 -0.0015 92 MET A CG 508 S SD . MET A 66 ? 0.1594 0.2184 0.2274 -0.0044 -0.0134 -0.0023 92 MET A SD 509 C CE . MET A 66 ? 0.1438 0.1998 0.2079 0.0039 -0.0068 0.0024 92 MET A CE 510 N N . ALA A 67 ? 0.1076 0.1347 0.1964 -0.0536 -0.0229 -0.0047 93 ALA A N 511 C CA . ALA A 67 ? 0.1095 0.1465 0.1979 -0.0658 -0.0281 -0.0116 93 ALA A CA 512 C C . ALA A 67 ? 0.1655 0.2223 0.2485 -0.0578 -0.0327 -0.0178 93 ALA A C 513 O O . ALA A 67 ? 0.1324 0.2033 0.2162 -0.0447 -0.0300 -0.0121 93 ALA A O 514 C CB . ALA A 67 ? 0.1221 0.1801 0.2279 -0.0724 -0.0261 -0.0018 93 ALA A CB 515 N N . PRO A 68 ? 0.2063 0.1145 0.1500 -0.0239 0.0385 -0.0172 94 PRO A N 516 C CA . PRO A 68 ? 0.2141 0.1180 0.1410 -0.0284 0.0315 -0.0201 94 PRO A CA 517 C C . PRO A 68 ? 0.2016 0.1216 0.1327 -0.0287 0.0154 -0.0186 94 PRO A C 518 O O . PRO A 68 ? 0.2064 0.1297 0.1321 -0.0275 0.0098 -0.0173 94 PRO A O 519 C CB . PRO A 68 ? 0.2573 0.1383 0.1608 -0.0385 0.0348 -0.0276 94 PRO A CB 520 C CG . PRO A 68 ? 0.2904 0.1608 0.2001 -0.0370 0.0514 -0.0281 94 PRO A CG 521 C CD . PRO A 68 ? 0.2311 0.1206 0.1663 -0.0294 0.0497 -0.0220 94 PRO A CD 522 N N . ALA A 69 ? 0.1929 0.1216 0.1354 -0.0303 0.0096 -0.0187 95 ALA A N 523 C CA . ALA A 69 ? 0.1961 0.1396 0.1473 -0.0303 -0.0036 -0.0171 95 ALA A CA 524 C C . ALA A 69 ? 0.2223 0.1803 0.1848 -0.0221 -0.0042 -0.0110 95 ALA A C 525 O O . ALA A 69 ? 0.2220 0.1887 0.1864 -0.0214 -0.0129 -0.0095 95 ALA A O 526 C CB . ALA A 69 ? 0.1971 0.1457 0.1625 -0.0340 -0.0067 -0.0190 95 ALA A CB 527 N N . CYS A 70 ? 0.1743 0.1336 0.1440 -0.0159 0.0045 -0.0075 96 CYS A N 528 C CA . CYS A 70 ? 0.1429 0.1132 0.1207 -0.0087 0.0030 -0.0022 96 CYS A CA 529 C C . CYS A 70 ? 0.1734 0.1431 0.1458 -0.0074 0.0028 -0.0022 96 CYS A C 530 O O . CYS A 70 ? 0.1759 0.1545 0.1507 -0.0053 -0.0029 -0.0004 96 CYS A O 531 C CB . CYS A 70 ? 0.1516 0.1202 0.1362 -0.0029 0.0101 0.0018 96 CYS A CB 532 S SG . CYS A 70 ? 0.1698 0.1487 0.1606 0.0050 0.0053 0.0080 96 CYS A SG 533 N N . LYS A 71 ? 0.1856 0.1430 0.1512 -0.0089 0.0111 -0.0046 97 LYS A N 534 C CA . LYS A 71 ? 0.1725 0.1261 0.1343 -0.0079 0.0146 -0.0051 97 LYS A CA 535 C C . LYS A 71 ? 0.1958 0.1482 0.1438 -0.0119 0.0067 -0.0069 97 LYS A C 536 O O . LYS A 71 ? 0.1871 0.1440 0.1370 -0.0094 0.0059 -0.0054 97 LYS A O 537 C CB . LYS A 71 ? 0.1889 0.1245 0.1434 -0.0102 0.0279 -0.0082 97 LYS A CB 538 C CG . LYS A 71 ? 0.2039 0.1335 0.1577 -0.0090 0.0355 -0.0088 97 LYS A CG 539 C CD . LYS A 71 ? 0.2700 0.1790 0.2180 -0.0113 0.0521 -0.0120 97 LYS A CD 540 C CE . LYS A 71 ? 0.3189 0.2184 0.2664 -0.0109 0.0631 -0.0133 97 LYS A CE 541 N NZ . LYS A 71 ? 0.3630 0.2371 0.3013 -0.0142 0.0826 -0.0172 97 LYS A NZ 542 N N . ARG A 72 ? 0.1792 0.1250 0.1143 -0.0180 0.0002 -0.0098 98 ARG A N 543 C CA . ARG A 72 ? 0.1775 0.1209 0.0993 -0.0212 -0.0098 -0.0105 98 ARG A CA 544 C C . ARG A 72 ? 0.1696 0.1310 0.1059 -0.0165 -0.0168 -0.0062 98 ARG A C 545 O O . ARG A 72 ? 0.1773 0.1372 0.1065 -0.0156 -0.0189 -0.0052 98 ARG A O 546 C CB . ARG A 72 ? 0.2131 0.1504 0.1255 -0.0282 -0.0198 -0.0137 98 ARG A CB 547 C CG . ARG A 72 ? 0.2716 0.2028 0.1676 -0.0315 -0.0324 -0.0138 98 ARG A CG 548 C CD . ARG A 72 ? 0.3684 0.2946 0.2590 -0.0389 -0.0454 -0.0172 98 ARG A CD 549 N NE . ARG A 72 ? 0.4579 0.4054 0.3789 -0.0372 -0.0518 -0.0153 98 ARG A NE 550 C CZ . ARG A 72 ? 0.3875 0.3479 0.3224 -0.0355 -0.0638 -0.0121 98 ARG A CZ 551 N NH1 . ARG A 72 ? 0.4155 0.3699 0.3353 -0.0352 -0.0727 -0.0099 98 ARG A NH1 552 N NH2 . ARG A 72 ? 0.4343 0.4113 0.3983 -0.0342 -0.0655 -0.0109 98 ARG A NH2 553 N N . HIS A 73 ? 0.1655 0.1409 0.1198 -0.0136 -0.0187 -0.0040 99 HIS A N 554 C CA . HIS A 73 ? 0.1759 0.1651 0.1418 -0.0095 -0.0228 -0.0005 99 HIS A CA 555 C C . HIS A 73 ? 0.1833 0.1754 0.1516 -0.0050 -0.0179 0.0012 99 HIS A C 556 O O . HIS A 73 ? 0.1704 0.1678 0.1400 -0.0035 -0.0209 0.0026 99 HIS A O 557 C CB . HIS A 73 ? 0.1587 0.1567 0.1390 -0.0076 -0.0227 0.0013 99 HIS A CB 558 C CG . HIS A 73 ? 0.1660 0.1649 0.1522 -0.0120 -0.0277 -0.0003 99 HIS A CG 559 N ND1 . HIS A 73 ? 0.2077 0.2138 0.2027 -0.0130 -0.0355 0.0007 99 HIS A ND1 560 C CD2 . HIS A 73 ? 0.2002 0.1941 0.1885 -0.0158 -0.0259 -0.0030 99 HIS A CD2 561 C CE1 . HIS A 73 ? 0.2003 0.2069 0.2051 -0.0172 -0.0393 -0.0013 99 HIS A CE1 562 N NE2 . HIS A 73 ? 0.2006 0.1996 0.2006 -0.0194 -0.0335 -0.0040 99 HIS A NE2 563 N N . PHE A 74 ? 0.1666 0.1556 0.1385 -0.0028 -0.0104 0.0011 100 PHE A N 564 C CA . PHE A 74 ? 0.1427 0.1355 0.1227 0.0010 -0.0068 0.0022 100 PHE A CA 565 C C . PHE A 74 ? 0.1604 0.1446 0.1315 -0.0009 -0.0024 0.0000 100 PHE A C 566 O O . PHE A 74 ? 0.1573 0.1468 0.1350 0.0010 -0.0018 0.0005 100 PHE A O 567 C CB . PHE A 74 ? 0.1303 0.1231 0.1217 0.0046 -0.0014 0.0034 100 PHE A CB 568 C CG . PHE A 74 ? 0.1393 0.1405 0.1382 0.0084 -0.0067 0.0070 100 PHE A CG 569 C CD1 . PHE A 74 ? 0.1348 0.1449 0.1402 0.0114 -0.0124 0.0090 100 PHE A CD1 570 C CD2 . PHE A 74 ? 0.1589 0.1561 0.1555 0.0084 -0.0056 0.0081 100 PHE A CD2 571 C CE1 . PHE A 74 ? 0.1244 0.1368 0.1295 0.0142 -0.0173 0.0122 100 PHE A CE1 572 C CE2 . PHE A 74 ? 0.1426 0.1426 0.1409 0.0118 -0.0089 0.0117 100 PHE A CE2 573 C CZ . PHE A 74 ? 0.1068 0.1131 0.1071 0.0147 -0.0150 0.0139 100 PHE A CZ 574 N N . ILE A 75 ? 0.1633 0.1320 0.1168 -0.0054 0.0008 -0.0027 101 ILE A N 575 C CA . ILE A 75 ? 0.1563 0.1109 0.0935 -0.0078 0.0054 -0.0044 101 ILE A CA 576 C C . ILE A 75 ? 0.2296 0.1894 0.1614 -0.0078 -0.0042 -0.0024 101 ILE A C 577 O O . ILE A 75 ? 0.1861 0.1433 0.1159 -0.0066 -0.0004 -0.0021 101 ILE A O 578 C CB . ILE A 75 ? 0.2120 0.1433 0.1240 -0.0135 0.0101 -0.0079 101 ILE A CB 579 C CG1 . ILE A 75 ? 0.2561 0.1797 0.1749 -0.0132 0.0235 -0.0099 101 ILE A CG1 580 C CG2 . ILE A 75 ? 0.2650 0.1769 0.1526 -0.0161 0.0140 -0.0090 101 ILE A CG2 581 C CD1 . ILE A 75 ? 0.3165 0.2427 0.2549 -0.0090 0.0359 -0.0094 101 ILE A CD1 582 N N . GLN A 76 ? 0.1773 0.1445 0.1097 -0.0088 -0.0155 -0.0011 102 GLN A N 583 C CA . GLN A 76 ? 0.2047 0.1772 0.1363 -0.0082 -0.0245 0.0015 102 GLN A CA 584 C C . GLN A 76 ? 0.1889 0.1750 0.1369 -0.0039 -0.0220 0.0034 102 GLN A C 585 O O . GLN A 76 ? 0.1731 0.1574 0.1175 -0.0029 -0.0216 0.0045 102 GLN A O 586 C CB . GLN A 76 ? 0.1650 0.1449 0.1030 -0.0099 -0.0358 0.0026 102 GLN A CB 587 C CG . GLN A 76 ? 0.2089 0.1750 0.1303 -0.0154 -0.0417 0.0000 102 GLN A CG 588 C CD . GLN A 76 ? 0.2830 0.2580 0.2170 -0.0174 -0.0541 0.0008 102 GLN A CD 589 O OE1 . GLN A 76 ? 0.3540 0.3448 0.3109 -0.0147 -0.0540 0.0026 102 GLN A OE1 590 N NE2 . GLN A 76 ? 0.3207 0.2842 0.2398 -0.0225 -0.0648 -0.0007 102 GLN A NE2 591 N N . ASP A 77 ? 0.1545 0.1516 0.1181 -0.0016 -0.0203 0.0036 103 ASP A N 592 C CA . ASP A 77 ? 0.1410 0.1491 0.1177 0.0016 -0.0195 0.0047 103 ASP A CA 593 C C . ASP A 77 ? 0.1553 0.1604 0.1338 0.0023 -0.0129 0.0032 103 ASP A C 594 O O . ASP A 77 ? 0.1551 0.1638 0.1366 0.0030 -0.0129 0.0035 103 ASP A O 595 C CB . ASP A 77 ? 0.1630 0.1770 0.1492 0.0035 -0.0195 0.0053 103 ASP A CB 596 C CG . ASP A 77 ? 0.1825 0.2043 0.1779 0.0062 -0.0207 0.0061 103 ASP A CG 597 O OD1 . ASP A 77 ? 0.1999 0.2254 0.1953 0.0061 -0.0228 0.0065 103 ASP A OD1 598 O OD2 . ASP A 77 ? 0.2100 0.2334 0.2126 0.0084 -0.0202 0.0064 103 ASP A OD2 599 N N . THR A 78 ? 0.1627 0.1601 0.1409 0.0019 -0.0056 0.0013 104 THR A N 600 C CA . THR A 78 ? 0.1515 0.1448 0.1364 0.0022 0.0036 -0.0007 104 THR A CA 601 C C . THR A 78 ? 0.1756 0.1567 0.1440 0.0003 0.0074 -0.0011 104 THR A C 602 O O . THR A 78 ? 0.1575 0.1400 0.1328 0.0009 0.0118 -0.0019 104 THR A O 603 C CB . THR A 78 ? 0.1549 0.1388 0.1428 0.0019 0.0133 -0.0025 104 THR A CB 604 O OG1 . THR A 78 ? 0.2238 0.2179 0.2265 0.0046 0.0092 -0.0010 104 THR A OG1 605 C CG2 . THR A 78 ? 0.1462 0.1261 0.1476 0.0023 0.0251 -0.0048 104 THR A CG2 606 N N . CYS A 79 ? 0.1612 0.1285 0.1067 -0.0022 0.0052 -0.0006 105 CYS A N 607 C CA . CYS A 79 ? 0.1899 0.1417 0.1140 -0.0037 0.0064 0.0002 105 CYS A CA 608 C C . CYS A 79 ? 0.1742 0.1367 0.1043 -0.0016 -0.0005 0.0031 105 CYS A C 609 O O . CYS A 79 ? 0.1829 0.1372 0.1069 -0.0012 0.0054 0.0034 105 CYS A O 610 C CB . CYS A 79 ? 0.2240 0.1589 0.1209 -0.0071 0.0004 0.0006 105 CYS A CB 611 S SG . CYS A 79 ? 0.2413 0.1517 0.1186 -0.0112 0.0129 -0.0036 105 CYS A SG 612 N N . LEU A 80 ? 0.1438 0.1218 0.0852 -0.0003 -0.0107 0.0051 106 LEU A N 613 C CA . LEU A 80 ? 0.1484 0.1352 0.0974 0.0016 -0.0149 0.0076 106 LEU A CA 614 C C . LEU A 80 ? 0.1548 0.1479 0.1171 0.0027 -0.0073 0.0056 106 LEU A C 615 O O . LEU A 80 ? 0.1587 0.1475 0.1184 0.0032 -0.0035 0.0062 106 LEU A O 616 C CB . LEU A 80 ? 0.1356 0.1358 0.0967 0.0024 -0.0233 0.0094 106 LEU A CB 617 C CG . LEU A 80 ? 0.1387 0.1461 0.1089 0.0043 -0.0251 0.0119 106 LEU A CG 618 C CD1 . LEU A 80 ? 0.1434 0.1434 0.1052 0.0050 -0.0310 0.0159 106 LEU A CD1 619 C CD2 . LEU A 80 ? 0.1827 0.2015 0.1670 0.0047 -0.0276 0.0123 106 LEU A CD2 620 N N . TYR A 81 ? 0.1348 0.1372 0.1116 0.0029 -0.0059 0.0032 107 TYR A N 621 C CA . TYR A 81 ? 0.1331 0.1425 0.1251 0.0031 -0.0019 0.0007 107 TYR A CA 622 C C . TYR A 81 ? 0.1513 0.1500 0.1422 0.0021 0.0092 -0.0016 107 TYR A C 623 O O . TYR A 81 ? 0.1599 0.1594 0.1563 0.0017 0.0132 -0.0029 107 TYR A O 624 C CB . TYR A 81 ? 0.1358 0.1548 0.1429 0.0039 -0.0048 -0.0008 107 TYR A CB 625 C CG . TYR A 81 ? 0.1334 0.1594 0.1586 0.0036 -0.0034 -0.0038 107 TYR A CG 626 C CD1 . TYR A 81 ? 0.1709 0.2047 0.2001 0.0031 -0.0098 -0.0044 107 TYR A CD1 627 C CD2 . TYR A 81 ? 0.1282 0.1518 0.1673 0.0031 0.0048 -0.0066 107 TYR A CD2 628 C CE1 . TYR A 81 ? 0.1038 0.1436 0.1497 0.0017 -0.0108 -0.0080 107 TYR A CE1 629 C CE2 . TYR A 81 ? 0.1080 0.1397 0.1693 0.0023 0.0048 -0.0099 107 TYR A CE2 630 C CZ . TYR A 81 ? 0.0829 0.1232 0.1470 0.0013 -0.0045 -0.0107 107 TYR A CZ 631 O OH . TYR A 81 ? 0.1106 0.1585 0.1965 -0.0005 -0.0068 -0.0148 107 TYR A OH 632 N N . GLU A 82 ? 0.1255 0.1116 0.1082 0.0013 0.0163 -0.0025 108 GLU A N 633 C CA . GLU A 82 ? 0.1430 0.1162 0.1264 0.0000 0.0307 -0.0053 108 GLU A CA 634 C C . GLU A 82 ? 0.1844 0.1385 0.1423 -0.0006 0.0356 -0.0033 108 GLU A C 635 O O . GLU A 82 ? 0.2057 0.1495 0.1644 -0.0014 0.0480 -0.0053 108 GLU A O 636 C CB . GLU A 82 ? 0.1494 0.1136 0.1354 -0.0008 0.0398 -0.0074 108 GLU A CB 637 C CG . GLU A 82 ? 0.1780 0.1609 0.1930 0.0009 0.0349 -0.0084 108 GLU A CG 638 C CD . GLU A 82 ? 0.2204 0.1960 0.2433 0.0010 0.0443 -0.0099 108 GLU A CD 639 O OE1 . GLU A 82 ? 0.2395 0.1932 0.2424 -0.0011 0.0563 -0.0109 108 GLU A OE1 640 O OE2 . GLU A 82 ? 0.1747 0.1647 0.2227 0.0031 0.0396 -0.0098 108 GLU A OE2 641 N N . CYS A 83 ? 0.1787 0.1276 0.1155 -0.0001 0.0256 0.0007 109 CYS A N 642 C CA . CYS A 83 ? 0.1873 0.1142 0.0957 -0.0003 0.0278 0.0036 109 CYS A CA 643 C C . CYS A 83 ? 0.2043 0.1368 0.1104 0.0021 0.0179 0.0083 109 CYS A C 644 O O . CYS A 83 ? 0.2273 0.1424 0.1141 0.0030 0.0208 0.0113 109 CYS A O 645 C CB . CYS A 83 ? 0.2332 0.1409 0.1128 -0.0023 0.0245 0.0047 109 CYS A CB 646 S SG . CYS A 83 ? 0.2467 0.1400 0.1233 -0.0054 0.0399 -0.0006 109 CYS A SG 647 N N . SER A 84 ? 0.1906 0.1442 0.1151 0.0034 0.0075 0.0094 110 SER A N 648 C CA . SER A 84 ? 0.1574 0.1146 0.0820 0.0059 -0.0004 0.0143 110 SER A CA 649 C C . SER A 84 ? 0.1753 0.1302 0.1047 0.0071 0.0085 0.0144 110 SER A C 650 O O . SER A 84 ? 0.1993 0.1643 0.1462 0.0059 0.0153 0.0100 110 SER A O 651 C CB . SER A 84 ? 0.1835 0.1610 0.1277 0.0066 -0.0092 0.0149 110 SER A CB 652 O OG . SER A 84 ? 0.1675 0.1475 0.1166 0.0092 -0.0130 0.0193 110 SER A OG 653 N N . PRO A 85 ? 0.1826 0.1233 0.0963 0.0094 0.0075 0.0196 111 PRO A N 654 C CA . PRO A 85 ? 0.1851 0.1238 0.1049 0.0108 0.0164 0.0201 111 PRO A CA 655 C C . PRO A 85 ? 0.1858 0.1384 0.1220 0.0134 0.0097 0.0236 111 PRO A C 656 O O . PRO A 85 ? 0.2035 0.1520 0.1426 0.0153 0.0158 0.0258 111 PRO A O 657 C CB . PRO A 85 ? 0.2151 0.1270 0.1060 0.0126 0.0196 0.0249 111 PRO A CB 658 C CG . PRO A 85 ? 0.2403 0.1480 0.1161 0.0138 0.0026 0.0300 111 PRO A CG 659 C CD . PRO A 85 ? 0.2318 0.1555 0.1201 0.0107 -0.0021 0.0252 111 PRO A CD 660 N N . ASN A 86 ? 0.1726 0.1399 0.1204 0.0133 -0.0004 0.0240 112 ASN A N 661 C CA . ASN A 86 ? 0.1419 0.1200 0.1064 0.0156 -0.0049 0.0274 112 ASN A CA 662 C C . ASN A 86 ? 0.1234 0.1166 0.1051 0.0132 -0.0021 0.0224 112 ASN A C 663 O O . ASN A 86 ? 0.1795 0.1807 0.1740 0.0142 -0.0054 0.0245 112 ASN A O 664 C CB . ASN A 86 ? 0.1560 0.1346 0.1200 0.0179 -0.0191 0.0332 112 ASN A CB 665 C CG . ASN A 86 ? 0.2121 0.1723 0.1546 0.0203 -0.0248 0.0390 112 ASN A CG 666 O OD1 . ASN A 86 ? 0.2955 0.2472 0.2212 0.0192 -0.0345 0.0401 112 ASN A OD1 667 N ND2 . ASN A 86 ? 0.1828 0.1341 0.1228 0.0235 -0.0190 0.0429 112 ASN A ND2 668 N N . LEU A 87 ? 0.1385 0.1341 0.1207 0.0099 0.0039 0.0161 113 LEU A N 669 C CA . LEU A 87 ? 0.1440 0.1501 0.1368 0.0075 0.0046 0.0117 113 LEU A CA 670 C C . LEU A 87 ? 0.1588 0.1637 0.1565 0.0054 0.0131 0.0080 113 LEU A C 671 O O . LEU A 87 ? 0.1539 0.1637 0.1557 0.0026 0.0131 0.0038 113 LEU A O 672 C CB . LEU A 87 ? 0.1589 0.1698 0.1517 0.0053 0.0017 0.0076 113 LEU A CB 673 C CG . LEU A 87 ? 0.1790 0.1894 0.1659 0.0063 -0.0051 0.0101 113 LEU A CG 674 C CD1 . LEU A 87 ? 0.1928 0.2069 0.1820 0.0047 -0.0057 0.0062 113 LEU A CD1 675 C CD2 . LEU A 87 ? 0.1539 0.1696 0.1460 0.0076 -0.0111 0.0133 113 LEU A CD2 676 N N . GLY A 88 ? 0.1595 0.1555 0.1542 0.0065 0.0202 0.0095 114 GLY A N 677 C CA . GLY A 88 ? 0.1908 0.1839 0.1900 0.0040 0.0296 0.0054 114 GLY A CA 678 C C . GLY A 88 ? 0.1680 0.1641 0.1724 0.0020 0.0313 0.0034 114 GLY A C 679 O O . GLY A 88 ? 0.1956 0.1920 0.2016 -0.0028 0.0344 -0.0032 114 GLY A O 680 N N . PRO A 89 ? 0.1584 0.1550 0.1656 0.0051 0.0296 0.0087 115 PRO A N 681 C CA . PRO A 89 ? 0.1426 0.1377 0.1528 0.0028 0.0350 0.0065 115 PRO A CA 682 C C . PRO A 89 ? 0.1536 0.1516 0.1576 -0.0017 0.0305 0.0008 115 PRO A C 683 O O . PRO A 89 ? 0.1942 0.1855 0.1935 -0.0052 0.0362 -0.0027 115 PRO A O 684 C CB . PRO A 89 ? 0.1561 0.1523 0.1756 0.0075 0.0339 0.0137 115 PRO A CB 685 C CG . PRO A 89 ? 0.1573 0.1524 0.1780 0.0123 0.0295 0.0200 115 PRO A CG 686 C CD . PRO A 89 ? 0.1670 0.1627 0.1762 0.0105 0.0248 0.0168 115 PRO A CD 687 N N . TRP A 90 ? 0.1241 0.1292 0.1262 -0.0017 0.0212 -0.0001 116 TRP A N 688 C CA . TRP A 90 ? 0.1319 0.1390 0.1279 -0.0048 0.0150 -0.0039 116 TRP A CA 689 C C . TRP A 90 ? 0.1193 0.1302 0.1163 -0.0080 0.0098 -0.0094 116 TRP A C 690 O O . TRP A 90 ? 0.1425 0.1553 0.1355 -0.0098 0.0020 -0.0118 116 TRP A O 691 C CB . TRP A 90 ? 0.1139 0.1257 0.1101 -0.0018 0.0086 0.0001 116 TRP A CB 692 C CG . TRP A 90 ? 0.1332 0.1424 0.1344 0.0006 0.0133 0.0048 116 TRP A CG 693 C CD1 . TRP A 90 ? 0.1215 0.1234 0.1201 -0.0007 0.0199 0.0044 116 TRP A CD1 694 C CD2 . TRP A 90 ? 0.1314 0.1438 0.1431 0.0048 0.0124 0.0106 116 TRP A CD2 695 N NE1 . TRP A 90 ? 0.1516 0.1543 0.1643 0.0026 0.0243 0.0095 116 TRP A NE1 696 C CE2 . TRP A 90 ? 0.1478 0.1579 0.1690 0.0061 0.0178 0.0136 116 TRP A CE2 697 C CE3 . TRP A 90 ? 0.1528 0.1674 0.1652 0.0073 0.0074 0.0135 116 TRP A CE3 698 C CZ2 . TRP A 90 ? 0.1252 0.1387 0.1619 0.0102 0.0157 0.0197 116 TRP A CZ2 699 C CZ3 . TRP A 90 ? 0.1422 0.1572 0.1628 0.0110 0.0043 0.0196 116 TRP A CZ3 700 C CH2 . TRP A 90 ? 0.1246 0.1409 0.1598 0.0126 0.0072 0.0228 116 TRP A CH2 701 N N . ILE A 91 ? 0.1402 0.1511 0.1440 -0.0085 0.0145 -0.0112 117 ILE A N 702 C CA . ILE A 91 ? 0.1330 0.1486 0.1453 -0.0116 0.0113 -0.0166 117 ILE A CA 703 C C . ILE A 91 ? 0.1707 0.1835 0.1810 -0.0176 0.0092 -0.0233 117 ILE A C 704 O O . ILE A 91 ? 0.1649 0.1696 0.1704 -0.0200 0.0172 -0.0251 117 ILE A O 705 C CB . ILE A 91 ? 0.1129 0.1262 0.1330 -0.0108 0.0200 -0.0168 117 ILE A CB 706 C CG1 . ILE A 91 ? 0.1634 0.1763 0.1799 -0.0060 0.0193 -0.0111 117 ILE A CG1 707 C CG2 . ILE A 91 ? 0.1456 0.1634 0.1810 -0.0150 0.0196 -0.0237 117 ILE A CG2 708 C CD1 . ILE A 91 ? 0.2044 0.2094 0.2217 -0.0051 0.0288 -0.0107 117 ILE A CD1 709 N N . GLN A 92 ? 0.1614 0.1793 0.1743 -0.0199 -0.0023 -0.0266 118 GLN A N 710 C CA . GLN A 92 ? 0.1548 0.1693 0.1652 -0.0265 -0.0082 -0.0336 118 GLN A CA 711 C C . GLN A 92 ? 0.1456 0.1683 0.1794 -0.0294 -0.0093 -0.0391 118 GLN A C 712 O O . GLN A 92 ? 0.1645 0.1971 0.2141 -0.0285 -0.0184 -0.0396 118 GLN A O 713 C CB . GLN A 92 ? 0.2056 0.2183 0.2033 -0.0275 -0.0228 -0.0337 118 GLN A CB 714 C CG . GLN A 92 ? 0.3076 0.3106 0.2934 -0.0352 -0.0293 -0.0409 118 GLN A CG 715 C CD . GLN A 92 ? 0.3936 0.3911 0.3626 -0.0365 -0.0457 -0.0407 118 GLN A CD 716 O OE1 . GLN A 92 ? 0.4954 0.5017 0.4724 -0.0320 -0.0551 -0.0367 118 GLN A OE1 717 N NE2 . GLN A 92 ? 0.3861 0.3661 0.3287 -0.0425 -0.0487 -0.0449 118 GLN A NE2 718 N N . GLN A 93 ? 0.2021 0.2201 0.2410 -0.0329 0.0013 -0.0432 119 GLN A N 719 C CA . GLN A 93 ? 0.2424 0.2671 0.3070 -0.0354 0.0045 -0.0482 119 GLN A CA 720 C C . GLN A 93 ? 0.2307 0.2628 0.3117 -0.0417 -0.0100 -0.0558 119 GLN A C 721 O O . GLN A 93 ? 0.2649 0.3059 0.3746 -0.0430 -0.0093 -0.0595 119 GLN A O 722 C CB . GLN A 93 ? 0.3560 0.3722 0.4226 -0.0369 0.0219 -0.0500 119 GLN A CB 723 C CG . GLN A 93 ? 0.4569 0.4617 0.5071 -0.0413 0.0263 -0.0530 119 GLN A CG 724 C CD . GLN A 93 ? 0.5731 0.5686 0.6251 -0.0408 0.0450 -0.0527 119 GLN A CD 725 O OE1 . GLN A 93 ? 0.6021 0.5933 0.6478 -0.0341 0.0536 -0.0449 119 GLN A OE1 726 N NE2 . GLN A 93 ? 0.5890 0.5800 0.6495 -0.0480 0.0505 -0.0610 119 GLN A NE2 727 N N . VAL A 94 ? 0.1874 0.2144 0.2505 -0.0456 -0.0232 -0.0582 120 VAL A N 728 C CA . VAL A 94 ? 0.2238 0.2564 0.3008 -0.0520 -0.0408 -0.0653 120 VAL A CA 729 C C . VAL A 94 ? 0.2027 0.2482 0.2961 -0.0477 -0.0564 -0.0618 120 VAL A C 730 O O . VAL A 94 ? 0.2398 0.2933 0.3537 -0.0507 -0.0701 -0.0650 120 VAL A O 731 C CB . VAL A 94 ? 0.2261 0.2441 0.2727 -0.0588 -0.0520 -0.0696 120 VAL A CB 732 C CG1 . VAL A 94 ? 0.2301 0.2351 0.2661 -0.0651 -0.0376 -0.0754 120 VAL A CG1 733 C CG2 . VAL A 94 ? 0.2606 0.2682 0.2737 -0.0542 -0.0557 -0.0624 120 VAL A CG2 734 N N . ASP A 95 ? 0.1751 0.2212 0.2584 -0.0400 -0.0531 -0.0534 121 ASP A N 735 C CA . ASP A 95 ? 0.2086 0.2645 0.3045 -0.0353 -0.0659 -0.0493 121 ASP A CA 736 C C . ASP A 95 ? 0.1874 0.2541 0.3145 -0.0310 -0.0547 -0.0476 121 ASP A C 737 O O . ASP A 95 ? 0.1808 0.2435 0.2987 -0.0266 -0.0400 -0.0430 121 ASP A O 738 C CB . ASP A 95 ? 0.2369 0.2846 0.3018 -0.0303 -0.0688 -0.0418 121 ASP A CB 739 C CG . ASP A 95 ? 0.2953 0.3497 0.3683 -0.0260 -0.0839 -0.0375 121 ASP A CG 740 O OD1 . ASP A 95 ? 0.2615 0.3272 0.3645 -0.0239 -0.0839 -0.0367 121 ASP A OD1 741 O OD2 . ASP A 95 ? 0.2979 0.3427 0.3431 -0.0237 -0.0897 -0.0326 121 ASP A OD2 742 N N . GLN A 96 ? 0.2385 0.3152 0.3977 -0.0318 -0.0603 -0.0500 122 GLN A N 743 C CA . GLN A 96 ? 0.2448 0.3275 0.4335 -0.0283 -0.0468 -0.0492 122 GLN A CA 744 C C . GLN A 96 ? 0.2133 0.3010 0.4123 -0.0222 -0.0548 -0.0433 122 GLN A C 745 O O . GLN A 96 ? 0.2650 0.3562 0.4921 -0.0200 -0.0475 -0.0435 122 GLN A O 746 C CB . GLN A 96 ? 0.2827 0.3667 0.4970 -0.0325 -0.0390 -0.0556 122 GLN A CB 747 C CG . GLN A 96 ? 0.3378 0.4145 0.5405 -0.0386 -0.0286 -0.0614 122 GLN A CG 748 C CD . GLN A 96 ? 0.3975 0.4738 0.6237 -0.0425 -0.0197 -0.0677 122 GLN A CD 749 O OE1 . GLN A 96 ? 0.3916 0.4745 0.6397 -0.0429 -0.0293 -0.0694 122 GLN A OE1 750 N NE2 . GLN A 96 ? 0.4005 0.4680 0.6220 -0.0452 -0.0008 -0.0709 122 GLN A NE2 751 N N . SER A 97 ? 0.1870 0.2723 0.3621 -0.0194 -0.0676 -0.0380 123 SER A N 752 C CA . SER A 97 ? 0.2165 0.3047 0.3989 -0.0139 -0.0756 -0.0322 123 SER A CA 753 C C . SER A 97 ? 0.2372 0.3245 0.4162 -0.0084 -0.0665 -0.0272 123 SER A C 754 O O . SER A 97 ? 0.2844 0.3731 0.4707 -0.0038 -0.0702 -0.0226 123 SER A O 755 C CB . SER A 97 ? 0.2281 0.3115 0.3863 -0.0140 -0.0938 -0.0290 123 SER A CB 756 O OG . SER A 97 ? 0.2993 0.3735 0.4221 -0.0132 -0.0940 -0.0260 123 SER A OG 757 N N . TRP A 98 ? 0.1448 0.2295 0.3137 -0.0090 -0.0547 -0.0282 124 TRP A N 758 C CA . TRP A 98 ? 0.1614 0.2429 0.3236 -0.0043 -0.0449 -0.0235 124 TRP A CA 759 C C . TRP A 98 ? 0.1152 0.1953 0.2992 -0.0041 -0.0261 -0.0257 124 TRP A C 760 O O . TRP A 98 ? 0.1254 0.2077 0.3303 -0.0077 -0.0194 -0.0310 124 TRP A O 761 C CB . TRP A 98 ? 0.1618 0.2326 0.2849 -0.0039 -0.0404 -0.0204 124 TRP A CB 762 C CG . TRP A 98 ? 0.1572 0.2256 0.2587 -0.0031 -0.0549 -0.0174 124 TRP A CG 763 C CD1 . TRP A 98 ? 0.1849 0.2532 0.2817 -0.0061 -0.0692 -0.0197 124 TRP A CD1 764 C CD2 . TRP A 98 ? 0.1218 0.1840 0.2011 0.0005 -0.0555 -0.0119 124 TRP A CD2 765 N NE1 . TRP A 98 ? 0.2066 0.2665 0.2762 -0.0043 -0.0772 -0.0154 124 TRP A NE1 766 C CE2 . TRP A 98 ? 0.1694 0.2267 0.2306 -0.0002 -0.0685 -0.0107 124 TRP A CE2 767 C CE3 . TRP A 98 ? 0.1318 0.1904 0.2037 0.0035 -0.0462 -0.0083 124 TRP A CE3 768 C CZ2 . TRP A 98 ? 0.1708 0.2197 0.2090 0.0025 -0.0702 -0.0058 124 TRP A CZ2 769 C CZ3 . TRP A 98 ? 0.1703 0.2234 0.2227 0.0059 -0.0496 -0.0039 124 TRP A CZ3 770 C CH2 . TRP A 98 ? 0.1686 0.2170 0.2055 0.0056 -0.0604 -0.0026 124 TRP A CH2 771 N N . ARG A 99 ? 0.1460 0.2198 0.3234 -0.0005 -0.0163 -0.0219 125 ARG A N 772 C CA . ARG A 99 ? 0.1208 0.1882 0.3150 -0.0006 0.0030 -0.0240 125 ARG A CA 773 C C . ARG A 99 ? 0.1341 0.1897 0.3103 -0.0038 0.0171 -0.0265 125 ARG A C 774 O O . ARG A 99 ? 0.1460 0.1965 0.3403 -0.0059 0.0323 -0.0304 125 ARG A O 775 C CB . ARG A 99 ? 0.1136 0.1728 0.2991 0.0031 0.0108 -0.0200 125 ARG A CB 776 C CG . ARG A 99 ? 0.1218 0.1694 0.2656 0.0037 0.0121 -0.0163 125 ARG A CG 777 C CD . ARG A 99 ? 0.1303 0.1727 0.2714 0.0067 0.0155 -0.0131 125 ARG A CD 778 N NE . ARG A 99 ? 0.1413 0.1720 0.2469 0.0065 0.0173 -0.0104 125 ARG A NE 779 C CZ . ARG A 99 ? 0.1542 0.1885 0.2418 0.0076 0.0052 -0.0072 125 ARG A CZ 780 N NH1 . ARG A 99 ? 0.1889 0.2349 0.2843 0.0089 -0.0087 -0.0060 125 ARG A NH1 781 N NH2 . ARG A 99 ? 0.1837 0.2082 0.2452 0.0070 0.0072 -0.0054 125 ARG A NH2 782 N N . LYS A 100 ? 0.1272 0.1776 0.2698 -0.0040 0.0128 -0.0239 126 LYS A N 783 C CA . LYS A 100 ? 0.1383 0.1787 0.2644 -0.0064 0.0224 -0.0253 126 LYS A CA 784 C C . LYS A 100 ? 0.1307 0.1761 0.2436 -0.0079 0.0107 -0.0253 126 LYS A C 785 O O . LYS A 100 ? 0.1459 0.2013 0.2744 -0.0103 0.0003 -0.0287 126 LYS A O 786 C CB . LYS A 100 ? 0.1689 0.1921 0.2666 -0.0046 0.0337 -0.0215 126 LYS A CB 787 C CG . LYS A 100 ? 0.2304 0.2430 0.3370 -0.0042 0.0485 -0.0226 126 LYS A CG 788 C CD . LYS A 100 ? 0.3056 0.2946 0.3851 -0.0048 0.0644 -0.0215 126 LYS A CD 789 C CE . LYS A 100 ? 0.2887 0.2686 0.3328 -0.0031 0.0577 -0.0162 126 LYS A CE 790 N NZ . LYS A 100 ? 0.3069 0.2622 0.3203 -0.0036 0.0688 -0.0145 126 LYS A NZ 791 N N . GLU A 101 ? 0.1298 0.1670 0.2149 -0.0069 0.0124 -0.0217 127 GLU A N 792 C CA . GLU A 101 ? 0.1393 0.1782 0.2127 -0.0085 0.0053 -0.0218 127 GLU A CA 793 C C . GLU A 101 ? 0.1192 0.1654 0.1892 -0.0080 -0.0098 -0.0206 127 GLU A C 794 O O . GLU A 101 ? 0.1357 0.1843 0.2054 -0.0050 -0.0145 -0.0175 127 GLU A O 795 C CB . GLU A 101 ? 0.1365 0.1655 0.1864 -0.0066 0.0108 -0.0173 127 GLU A CB 796 C CG . GLU A 101 ? 0.1876 0.2158 0.2224 -0.0033 0.0049 -0.0118 127 GLU A CG 797 C CD . GLU A 101 ? 0.1926 0.2138 0.2222 -0.0013 0.0101 -0.0095 127 GLU A CD 798 O OE1 . GLU A 101 ? 0.1793 0.1957 0.2178 -0.0021 0.0191 -0.0121 127 GLU A OE1 799 O OE2 . GLU A 101 ? 0.1637 0.1823 0.1799 0.0007 0.0060 -0.0055 127 GLU A OE2 800 N N . ARG A 102 ? 0.1062 0.1529 0.1712 -0.0111 -0.0163 -0.0232 128 ARG A N 801 C CA . ARG A 102 ? 0.1330 0.1788 0.1824 -0.0105 -0.0275 -0.0209 128 ARG A CA 802 C C . ARG A 102 ? 0.1784 0.2158 0.2071 -0.0100 -0.0209 -0.0180 128 ARG A C 803 O O . ARG A 102 ? 0.1586 0.1912 0.1842 -0.0127 -0.0145 -0.0205 128 ARG A O 804 C CB . ARG A 102 ? 0.1658 0.2129 0.2179 -0.0150 -0.0391 -0.0257 128 ARG A CB 805 C CG . ARG A 102 ? 0.2073 0.2457 0.2335 -0.0156 -0.0479 -0.0239 128 ARG A CG 806 C CD . ARG A 102 ? 0.2658 0.3043 0.2852 -0.0106 -0.0526 -0.0180 128 ARG A CD 807 N NE . ARG A 102 ? 0.2633 0.2939 0.2649 -0.0114 -0.0655 -0.0173 128 ARG A NE 808 C CZ . ARG A 102 ? 0.2272 0.2495 0.2096 -0.0085 -0.0660 -0.0125 128 ARG A CZ 809 N NH1 . ARG A 102 ? 0.1873 0.2107 0.1697 -0.0051 -0.0555 -0.0087 128 ARG A NH1 810 N NH2 . ARG A 102 ? 0.1978 0.2088 0.1600 -0.0093 -0.0774 -0.0116 128 ARG A NH2 811 N N . VAL A 103 ? 0.1186 0.1540 0.1363 -0.0066 -0.0214 -0.0130 129 VAL A N 812 C CA . VAL A 103 ? 0.1329 0.1614 0.1368 -0.0060 -0.0161 -0.0101 129 VAL A CA 813 C C . VAL A 103 ? 0.1341 0.1568 0.1237 -0.0067 -0.0211 -0.0094 129 VAL A C 814 O O . VAL A 103 ? 0.1462 0.1705 0.1341 -0.0059 -0.0296 -0.0088 129 VAL A O 815 C CB . VAL A 103 ? 0.1383 0.1669 0.1418 -0.0023 -0.0116 -0.0052 129 VAL A CB 816 C CG1 . VAL A 103 ? 0.1843 0.2116 0.1932 -0.0019 -0.0050 -0.0054 129 VAL A CG1 817 C CG2 . VAL A 103 ? 0.1557 0.1876 0.1596 0.0000 -0.0169 -0.0028 129 VAL A CG2 818 N N . LEU A 104 ? 0.1311 0.1450 0.1101 -0.0082 -0.0147 -0.0093 130 LEU A N 819 C CA . LEU A 104 ? 0.1360 0.1385 0.0971 -0.0095 -0.0152 -0.0089 130 LEU A CA 820 C C . LEU A 104 ? 0.1497 0.1469 0.1097 -0.0076 -0.0047 -0.0052 130 LEU A C 821 O O . LEU A 104 ? 0.1467 0.1428 0.1132 -0.0077 0.0040 -0.0048 130 LEU A O 822 C CB . LEU A 104 ? 0.1879 0.1793 0.1351 -0.0150 -0.0162 -0.0143 130 LEU A CB 823 C CG . LEU A 104 ? 0.2112 0.2050 0.1570 -0.0175 -0.0306 -0.0179 130 LEU A CG 824 C CD1 . LEU A 104 ? 0.1959 0.1781 0.1285 -0.0243 -0.0316 -0.0242 130 LEU A CD1 825 C CD2 . LEU A 104 ? 0.2836 0.2719 0.2157 -0.0154 -0.0398 -0.0147 130 LEU A CD2 826 N N . ASN A 105 ? 0.1530 0.1470 0.1077 -0.0058 -0.0053 -0.0023 131 ASN A N 827 C CA . ASN A 105 ? 0.1607 0.1481 0.1166 -0.0048 0.0049 0.0006 131 ASN A CA 828 C C . ASN A 105 ? 0.1588 0.1569 0.1360 -0.0018 0.0081 0.0040 131 ASN A C 829 O O . ASN A 105 ? 0.1614 0.1556 0.1467 -0.0013 0.0174 0.0057 131 ASN A O 830 C CB . ASN A 105 ? 0.1858 0.1553 0.1260 -0.0085 0.0149 -0.0020 131 ASN A CB 831 C CG . ASN A 105 ? 0.2063 0.1603 0.1188 -0.0117 0.0099 -0.0047 131 ASN A CG 832 O OD1 . ASN A 105 ? 0.2333 0.1821 0.1366 -0.0102 0.0072 -0.0024 131 ASN A OD1 833 N ND2 . ASN A 105 ? 0.2432 0.1883 0.1411 -0.0162 0.0075 -0.0094 131 ASN A ND2 834 N N . VAL A 106 ? 0.1210 0.1306 0.1067 0.0003 0.0003 0.0052 132 VAL A N 835 C CA . VAL A 106 ? 0.1233 0.1402 0.1235 0.0029 -0.0003 0.0088 132 VAL A CA 836 C C . VAL A 106 ? 0.1451 0.1619 0.1541 0.0040 0.0018 0.0117 132 VAL A C 837 O O . VAL A 106 ? 0.1480 0.1637 0.1522 0.0036 -0.0003 0.0113 132 VAL A O 838 C CB . VAL A 106 ? 0.1295 0.1532 0.1302 0.0039 -0.0081 0.0088 132 VAL A CB 839 C CG1 . VAL A 106 ? 0.1664 0.1934 0.1752 0.0060 -0.0112 0.0126 132 VAL A CG1 840 C CG2 . VAL A 106 ? 0.1182 0.1419 0.1161 0.0027 -0.0076 0.0058 132 VAL A CG2 841 N N . PRO A 107 ? 0.1477 0.1654 0.1723 0.0054 0.0064 0.0147 133 PRO A N 842 C CA . PRO A 107 ? 0.1209 0.1388 0.1604 0.0059 0.0100 0.0168 133 PRO A CA 843 C C . PRO A 107 ? 0.1128 0.1400 0.1624 0.0069 -0.0005 0.0187 133 PRO A C 844 O O . PRO A 107 ? 0.1435 0.1767 0.2107 0.0085 -0.0054 0.0220 133 PRO A O 845 C CB . PRO A 107 ? 0.1420 0.1588 0.1997 0.0075 0.0179 0.0195 133 PRO A CB 846 C CG . PRO A 107 ? 0.1249 0.1451 0.1798 0.0091 0.0125 0.0208 133 PRO A CG 847 C CD . PRO A 107 ? 0.1229 0.1407 0.1546 0.0068 0.0094 0.0163 133 PRO A CD 848 N N . LEU A 108 ? 0.1466 0.1734 0.1848 0.0057 -0.0042 0.0167 134 LEU A N 849 C CA . LEU A 108 ? 0.1236 0.1561 0.1670 0.0054 -0.0129 0.0173 134 LEU A CA 850 C C . LEU A 108 ? 0.1387 0.1742 0.2050 0.0049 -0.0114 0.0189 134 LEU A C 851 O O . LEU A 108 ? 0.1649 0.1952 0.2373 0.0043 -0.0008 0.0183 134 LEU A O 852 C CB . LEU A 108 ? 0.1460 0.1754 0.1739 0.0044 -0.0138 0.0149 134 LEU A CB 853 C CG . LEU A 108 ? 0.1858 0.2180 0.2152 0.0034 -0.0206 0.0145 134 LEU A CG 854 C CD1 . LEU A 108 ? 0.2095 0.2440 0.2350 0.0035 -0.0286 0.0150 134 LEU A CD1 855 C CD2 . LEU A 108 ? 0.2153 0.2433 0.2316 0.0034 -0.0192 0.0129 134 LEU A CD2 856 N N . CYS A 109 ? 0.1167 0.1591 0.1957 0.0049 -0.0221 0.0206 135 CYS A N 857 C CA . CYS A 109 ? 0.1169 0.1646 0.2236 0.0040 -0.0235 0.0217 135 CYS A CA 858 C C . CYS A 109 ? 0.0886 0.1332 0.1964 0.0014 -0.0172 0.0188 135 CYS A C 859 O O . CYS A 109 ? 0.1253 0.1659 0.2126 0.0003 -0.0183 0.0165 135 CYS A O 860 C CB . CYS A 109 ? 0.1395 0.1933 0.2546 0.0036 -0.0403 0.0236 135 CYS A CB 861 S SG . CYS A 109 ? 0.1827 0.2378 0.3015 0.0075 -0.0473 0.0289 135 CYS A SG 862 N N . LYS A 110 ? 0.1055 0.1509 0.2395 0.0007 -0.0090 0.0191 136 LYS A N 863 C CA . LYS A 110 ? 0.1033 0.1427 0.2398 -0.0017 0.0009 0.0165 136 LYS A CA 864 C C . LYS A 110 ? 0.1213 0.1641 0.2540 -0.0045 -0.0096 0.0142 136 LYS A C 865 O O . LYS A 110 ? 0.1399 0.1748 0.2546 -0.0053 -0.0043 0.0123 136 LYS A O 866 C CB . LYS A 110 ? 0.1363 0.1765 0.3085 -0.0023 0.0121 0.0170 136 LYS A CB 867 C CG . LYS A 110 ? 0.2149 0.2466 0.3937 -0.0051 0.0256 0.0144 136 LYS A CG 868 C CD . LYS A 110 ? 0.2498 0.2817 0.4687 -0.0056 0.0393 0.0149 136 LYS A CD 869 C CE . LYS A 110 ? 0.3585 0.3849 0.5951 -0.0092 0.0509 0.0118 136 LYS A CE 870 N NZ . LYS A 110 ? 0.4693 0.4729 0.6714 -0.0094 0.0690 0.0106 136 LYS A NZ 871 N N . GLU A 111 ? 0.0989 0.1513 0.2462 -0.0059 -0.0250 0.0146 137 GLU A N 872 C CA . GLU A 111 ? 0.1560 0.2090 0.2986 -0.0098 -0.0350 0.0116 137 GLU A CA 873 C C . GLU A 111 ? 0.1639 0.2096 0.2705 -0.0094 -0.0369 0.0103 137 GLU A C 874 O O . GLU A 111 ? 0.1762 0.2168 0.2731 -0.0117 -0.0343 0.0075 137 GLU A O 875 C CB . GLU A 111 ? 0.2015 0.2628 0.3606 -0.0119 -0.0539 0.0123 137 GLU A CB 876 C CG . GLU A 111 ? 0.2639 0.3308 0.4590 -0.0121 -0.0531 0.0129 137 GLU A CG 877 C CD . GLU A 111 ? 0.3198 0.3879 0.5205 -0.0077 -0.0559 0.0176 137 GLU A CD 878 O OE1 . GLU A 111 ? 0.2882 0.3554 0.4774 -0.0043 -0.0498 0.0201 137 GLU A OE1 879 O OE2 . GLU A 111 ? 0.3828 0.4526 0.6003 -0.0077 -0.0644 0.0187 137 GLU A OE2 880 N N . ASP A 112 ? 0.1375 0.1824 0.2269 -0.0066 -0.0404 0.0124 138 ASP A N 881 C CA . ASP A 112 ? 0.1491 0.1876 0.2100 -0.0060 -0.0409 0.0112 138 ASP A CA 882 C C . ASP A 112 ? 0.1834 0.2164 0.2345 -0.0049 -0.0295 0.0102 138 ASP A C 883 O O . ASP A 112 ? 0.2149 0.2431 0.2529 -0.0056 -0.0291 0.0085 138 ASP A O 884 C CB . ASP A 112 ? 0.1512 0.1893 0.2002 -0.0031 -0.0429 0.0134 138 ASP A CB 885 C CG . ASP A 112 ? 0.2270 0.2667 0.2797 -0.0034 -0.0550 0.0155 138 ASP A CG 886 O OD1 . ASP A 112 ? 0.2292 0.2754 0.3056 -0.0035 -0.0593 0.0174 138 ASP A OD1 887 O OD2 . ASP A 112 ? 0.2028 0.2358 0.2350 -0.0036 -0.0600 0.0154 138 ASP A OD2 888 N N . CYS A 113 ? 0.1089 0.1403 0.1654 -0.0030 -0.0199 0.0115 139 CYS A N 889 C CA . CYS A 113 ? 0.1276 0.1503 0.1705 -0.0016 -0.0106 0.0114 139 CYS A CA 890 C C . CYS A 113 ? 0.1537 0.1710 0.2018 -0.0035 -0.0048 0.0101 139 CYS A C 891 O O . CYS A 113 ? 0.1449 0.1559 0.1790 -0.0027 -0.0030 0.0099 139 CYS A O 892 C CB . CYS A 113 ? 0.1601 0.1776 0.2017 0.0000 -0.0017 0.0128 139 CYS A CB 893 S SG . CYS A 113 ? 0.2378 0.2395 0.2548 0.0017 0.0068 0.0134 139 CYS A SG 894 N N . GLU A 114 ? 0.1056 0.1256 0.1770 -0.0060 -0.0013 0.0093 140 GLU A N 895 C CA . GLU A 114 ? 0.1240 0.1377 0.2032 -0.0083 0.0070 0.0076 140 GLU A CA 896 C C . GLU A 114 ? 0.1433 0.1585 0.2191 -0.0111 -0.0006 0.0050 140 GLU A C 897 O O . GLU A 114 ? 0.1499 0.1563 0.2174 -0.0114 0.0063 0.0042 140 GLU A O 898 C CB . GLU A 114 ? 0.1239 0.1407 0.2349 -0.0108 0.0136 0.0068 140 GLU A CB 899 C CG . GLU A 114 ? 0.1495 0.1585 0.2597 -0.0083 0.0267 0.0090 140 GLU A CG 900 C CD . GLU A 114 ? 0.2782 0.2869 0.4223 -0.0104 0.0387 0.0082 140 GLU A CD 901 O OE1 . GLU A 114 ? 0.2989 0.3193 0.4743 -0.0136 0.0319 0.0063 140 GLU A OE1 902 O OE2 . GLU A 114 ? 0.3617 0.3571 0.5016 -0.0093 0.0551 0.0092 140 GLU A OE2 903 N N . GLN A 115 ? 0.1377 0.1612 0.2162 -0.0132 -0.0141 0.0038 141 GLN A N 904 C CA . GLN A 115 ? 0.1206 0.1417 0.1921 -0.0170 -0.0206 0.0005 141 GLN A CA 905 C C . GLN A 115 ? 0.1556 0.1693 0.2010 -0.0143 -0.0185 0.0011 141 GLN A C 906 O O . GLN A 115 ? 0.1672 0.1742 0.2057 -0.0164 -0.0161 -0.0012 141 GLN A O 907 C CB . GLN A 115 ? 0.1440 0.1715 0.2224 -0.0207 -0.0363 -0.0010 141 GLN A CB 908 C CG . GLN A 115 ? 0.1461 0.1824 0.2579 -0.0239 -0.0406 -0.0018 141 GLN A CG 909 C CD . GLN A 115 ? 0.2324 0.2738 0.3493 -0.0270 -0.0598 -0.0023 141 GLN A CD 910 O OE1 . GLN A 115 ? 0.3115 0.3456 0.4048 -0.0297 -0.0689 -0.0042 141 GLN A OE1 911 N NE2 . GLN A 115 ? 0.2275 0.2793 0.3740 -0.0264 -0.0659 -0.0001 141 GLN A NE2 912 N N . TRP A 116 ? 0.1461 0.1612 0.1801 -0.0099 -0.0189 0.0040 142 TRP A N 913 C CA . TRP A 116 ? 0.1164 0.1264 0.1329 -0.0066 -0.0166 0.0050 142 TRP A CA 914 C C . TRP A 116 ? 0.1476 0.1498 0.1608 -0.0043 -0.0073 0.0064 142 TRP A C 915 O O . TRP A 116 ? 0.1405 0.1366 0.1466 -0.0037 -0.0047 0.0061 142 TRP A O 916 C CB . TRP A 116 ? 0.1085 0.1225 0.1195 -0.0029 -0.0186 0.0074 142 TRP A CB 917 C CG . TRP A 116 ? 0.1553 0.1672 0.1551 0.0004 -0.0180 0.0084 142 TRP A CG 918 C CD1 . TRP A 116 ? 0.1432 0.1498 0.1379 0.0014 -0.0154 0.0081 142 TRP A CD1 919 C CD2 . TRP A 116 ? 0.1394 0.1548 0.1358 0.0031 -0.0199 0.0097 142 TRP A CD2 920 N NE1 . TRP A 116 ? 0.1699 0.1781 0.1619 0.0049 -0.0162 0.0094 142 TRP A NE1 921 C CE2 . TRP A 116 ? 0.1843 0.1980 0.1768 0.0056 -0.0195 0.0101 142 TRP A CE2 922 C CE3 . TRP A 116 ? 0.1695 0.1891 0.1680 0.0035 -0.0214 0.0104 142 TRP A CE3 923 C CZ2 . TRP A 116 ? 0.2170 0.2342 0.2094 0.0079 -0.0217 0.0106 142 TRP A CZ2 924 C CZ3 . TRP A 116 ? 0.1604 0.1818 0.1549 0.0055 -0.0227 0.0107 142 TRP A CZ3 925 C CH2 . TRP A 116 ? 0.1802 0.2010 0.1724 0.0074 -0.0235 0.0106 142 TRP A CH2 926 N N . TRP A 117 ? 0.1482 0.1480 0.1652 -0.0030 -0.0013 0.0083 143 TRP A N 927 C CA . TRP A 117 ? 0.1232 0.1109 0.1319 -0.0006 0.0080 0.0104 143 TRP A CA 928 C C . TRP A 117 ? 0.1502 0.1323 0.1653 -0.0036 0.0137 0.0081 143 TRP A C 929 O O . TRP A 117 ? 0.1654 0.1381 0.1702 -0.0011 0.0181 0.0098 143 TRP A O 930 C CB . TRP A 117 ? 0.1255 0.1070 0.1339 0.0002 0.0156 0.0121 143 TRP A CB 931 C CG . TRP A 117 ? 0.1432 0.1069 0.1369 0.0026 0.0262 0.0148 143 TRP A CG 932 C CD1 . TRP A 117 ? 0.1554 0.1080 0.1257 0.0072 0.0250 0.0188 143 TRP A CD1 933 C CD2 . TRP A 117 ? 0.1570 0.1095 0.1571 0.0005 0.0391 0.0140 143 TRP A CD2 934 N NE1 . TRP A 117 ? 0.1761 0.1090 0.1333 0.0085 0.0361 0.0211 143 TRP A NE1 935 C CE2 . TRP A 117 ? 0.1843 0.1164 0.1597 0.0044 0.0466 0.0181 143 TRP A CE2 936 C CE3 . TRP A 117 ? 0.1744 0.1314 0.1995 -0.0046 0.0447 0.0101 143 TRP A CE3 937 C CZ2 . TRP A 117 ? 0.2186 0.1325 0.1909 0.0036 0.0620 0.0187 143 TRP A CZ2 938 C CZ3 . TRP A 117 ? 0.2043 0.1460 0.2316 -0.0058 0.0600 0.0099 143 TRP A CZ3 939 C CH2 . TRP A 117 ? 0.2456 0.1649 0.2453 -0.0016 0.0699 0.0142 143 TRP A CH2 940 N N . GLU A 118 ? 0.1595 0.1471 0.1930 -0.0090 0.0129 0.0044 144 GLU A N 941 C CA . GLU A 118 ? 0.1745 0.1576 0.2168 -0.0135 0.0173 0.0008 144 GLU A CA 942 C C . GLU A 118 ? 0.1579 0.1384 0.1888 -0.0145 0.0132 -0.0010 144 GLU A C 943 O O . GLU A 118 ? 0.1590 0.1294 0.1849 -0.0143 0.0211 -0.0012 144 GLU A O 944 C CB . GLU A 118 ? 0.1926 0.1852 0.2602 -0.0197 0.0123 -0.0033 144 GLU A CB 945 C CG . GLU A 118 ? 0.2743 0.2632 0.3547 -0.0258 0.0156 -0.0082 144 GLU A CG 946 C CD . GLU A 118 ? 0.4845 0.4615 0.5691 -0.0248 0.0330 -0.0074 144 GLU A CD 947 O OE1 . GLU A 118 ? 0.5349 0.5097 0.6256 -0.0223 0.0412 -0.0047 144 GLU A OE1 948 O OE2 . GLU A 118 ? 0.5927 0.5597 0.6724 -0.0266 0.0400 -0.0093 144 GLU A OE2 949 N N . ASP A 119 ? 0.1654 0.1525 0.1913 -0.0154 0.0027 -0.0021 145 ASP A N 950 C CA . ASP A 119 ? 0.1417 0.1231 0.1566 -0.0179 0.0009 -0.0049 145 ASP A CA 951 C C . ASP A 119 ? 0.1651 0.1394 0.1681 -0.0120 0.0077 -0.0014 145 ASP A C 952 O O . ASP A 119 ? 0.1642 0.1308 0.1602 -0.0134 0.0109 -0.0034 145 ASP A O 953 C CB . ASP A 119 ? 0.1485 0.1341 0.1575 -0.0207 -0.0106 -0.0069 145 ASP A CB 954 C CG . ASP A 119 ? 0.2295 0.2199 0.2507 -0.0273 -0.0203 -0.0105 145 ASP A CG 955 O OD1 . ASP A 119 ? 0.2633 0.2541 0.3003 -0.0307 -0.0170 -0.0128 145 ASP A OD1 956 O OD2 . ASP A 119 ? 0.2163 0.2097 0.2328 -0.0289 -0.0315 -0.0108 145 ASP A OD2 957 N N . CYS A 120 ? 0.1446 0.1202 0.1456 -0.0056 0.0097 0.0038 146 CYS A N 958 C CA . CYS A 120 ? 0.1443 0.1148 0.1376 0.0007 0.0127 0.0080 146 CYS A CA 959 C C . CYS A 120 ? 0.1670 0.1263 0.1575 0.0040 0.0213 0.0114 146 CYS A C 960 O O . CYS A 120 ? 0.1693 0.1232 0.1545 0.0101 0.0225 0.0162 146 CYS A O 961 C CB . CYS A 120 ? 0.1429 0.1206 0.1333 0.0054 0.0062 0.0115 146 CYS A CB 962 S SG . CYS A 120 ? 0.1866 0.1732 0.1778 0.0031 -0.0009 0.0084 146 CYS A SG 963 N N . ARG A 121 ? 0.1063 0.1696 0.1881 -0.0031 -0.0068 0.0223 147 ARG A N 964 C CA . ARG A 121 ? 0.1175 0.1688 0.2063 -0.0063 0.0030 0.0210 147 ARG A CA 965 C C . ARG A 121 ? 0.1516 0.1877 0.2412 -0.0128 0.0065 0.0147 147 ARG A C 966 O O . ARG A 121 ? 0.1782 0.1978 0.2684 -0.0110 0.0136 0.0215 147 ARG A O 967 C CB . ARG A 121 ? 0.1353 0.2059 0.2456 -0.0123 0.0056 0.0190 147 ARG A CB 968 C CG . ARG A 121 ? 0.1731 0.2343 0.2961 -0.0175 0.0167 0.0212 147 ARG A CG 969 C CD . ARG A 121 ? 0.1886 0.2715 0.3355 -0.0240 0.0196 0.0196 147 ARG A CD 970 N NE . ARG A 121 ? 0.3241 0.3986 0.4892 -0.0319 0.0307 0.0230 147 ARG A NE 971 C CZ . ARG A 121 ? 0.3474 0.4192 0.5351 -0.0446 0.0330 0.0129 147 ARG A CZ 972 N NH1 . ARG A 121 ? 0.2971 0.3793 0.4870 -0.0514 0.0247 -0.0050 147 ARG A NH1 973 N NH2 . ARG A 121 ? 0.3978 0.4594 0.6087 -0.0513 0.0444 0.0203 147 ARG A NH2 974 N N . THR A 122 ? 0.1269 0.1721 0.2190 -0.0201 0.0019 0.0023 148 THR A N 975 C CA . THR A 122 ? 0.1494 0.1812 0.2526 -0.0267 0.0074 -0.0087 148 THR A CA 976 C C . THR A 122 ? 0.1568 0.1769 0.2444 -0.0217 0.0054 -0.0091 148 THR A C 977 O O . THR A 122 ? 0.1738 0.1853 0.2727 -0.0258 0.0098 -0.0203 148 THR A O 978 C CB . THR A 122 ? 0.1734 0.2258 0.2945 -0.0404 0.0067 -0.0299 148 THR A CB 979 O OG1 . THR A 122 ? 0.1802 0.2590 0.2843 -0.0423 -0.0029 -0.0369 148 THR A OG1 980 C CG2 . THR A 122 ? 0.1558 0.2236 0.2957 -0.0466 0.0082 -0.0300 148 THR A CG2 981 N N . SER A 123 ? 0.1164 0.1366 0.1829 -0.0133 -0.0004 0.0014 149 SER A N 982 C CA . SER A 123 ? 0.1219 0.1322 0.1749 -0.0088 -0.0022 0.0028 149 SER A CA 983 C C . SER A 123 ? 0.1468 0.1380 0.1946 -0.0010 0.0013 0.0151 149 SER A C 984 O O . SER A 123 ? 0.2111 0.1998 0.2636 0.0007 0.0056 0.0230 149 SER A O 985 C CB . SER A 123 ? 0.1209 0.1455 0.1588 -0.0065 -0.0105 0.0071 149 SER A CB 986 O OG . SER A 123 ? 0.1375 0.1893 0.1786 -0.0146 -0.0146 -0.0014 149 SER A OG 987 N N . TYR A 124 ? 0.1477 0.1314 0.1865 0.0027 -0.0004 0.0167 150 TYR A N 988 C CA . TYR A 124 ? 0.1821 0.1552 0.2172 0.0085 0.0018 0.0275 150 TYR A CA 989 C C . TYR A 124 ? 0.1798 0.1535 0.1977 0.0128 -0.0037 0.0293 150 TYR A C 990 O O . TYR A 124 ? 0.1672 0.1448 0.1807 0.0111 -0.0077 0.0239 150 TYR A O 991 C CB . TYR A 124 ? 0.1776 0.1413 0.2306 0.0082 0.0067 0.0280 150 TYR A CB 992 C CG . TYR A 124 ? 0.2207 0.1795 0.2994 0.0032 0.0142 0.0265 150 TYR A CG 993 C CD1 . TYR A 124 ? 0.2907 0.2530 0.3852 -0.0049 0.0165 0.0076 150 TYR A CD1 994 C CD2 . TYR A 124 ? 0.2044 0.1591 0.2934 0.0052 0.0194 0.0436 150 TYR A CD2 995 C CE1 . TYR A 124 ? 0.3298 0.2869 0.4538 -0.0114 0.0241 0.0027 150 TYR A CE1 996 C CE2 . TYR A 124 ? 0.2401 0.1888 0.3591 -0.0006 0.0275 0.0442 150 TYR A CE2 997 C CZ . TYR A 124 ? 0.3277 0.2753 0.4660 -0.0091 0.0299 0.0222 150 TYR A CZ 998 O OH . TYR A 124 ? 0.3701 0.3130 0.5414 -0.0161 0.0381 0.0187 150 TYR A OH 999 N N . THR A 125 ? 0.1684 0.1421 0.1776 0.0169 -0.0036 0.0366 151 THR A N 1000 C CA . THR A 125 ? 0.1613 0.1363 0.1587 0.0191 -0.0084 0.0351 151 THR A CA 1001 C C . THR A 125 ? 0.1489 0.1307 0.1395 0.0218 -0.0080 0.0425 151 THR A C 1002 O O . THR A 125 ? 0.1644 0.1508 0.1587 0.0226 -0.0039 0.0524 151 THR A O 1003 C CB . THR A 125 ? 0.1540 0.1302 0.1476 0.0196 -0.0103 0.0296 151 THR A CB 1004 O OG1 . THR A 125 ? 0.1657 0.1403 0.1551 0.0197 -0.0142 0.0264 151 THR A OG1 1005 C CG2 . THR A 125 ? 0.1574 0.1395 0.1491 0.0215 -0.0059 0.0285 151 THR A CG2 1006 N N . CYS A 126 ? 0.1839 0.1706 0.1661 0.0222 -0.0125 0.0392 152 CYS A N 1007 C CA . CYS A 126 ? 0.1762 0.1785 0.1512 0.0236 -0.0143 0.0464 152 CYS A CA 1008 C C . CYS A 126 ? 0.1727 0.1884 0.1347 0.0214 -0.0159 0.0347 152 CYS A C 1009 O O . CYS A 126 ? 0.2053 0.2424 0.1578 0.0205 -0.0187 0.0369 152 CYS A O 1010 C CB . CYS A 126 ? 0.1721 0.1753 0.1538 0.0251 -0.0184 0.0516 152 CYS A CB 1011 S SG . CYS A 126 ? 0.2040 0.2004 0.1855 0.0217 -0.0228 0.0379 152 CYS A SG 1012 N N . LYS A 127 ? 0.1776 0.1836 0.1423 0.0201 -0.0140 0.0217 153 LYS A N 1013 C CA . LYS A 127 ? 0.2039 0.2195 0.1648 0.0177 -0.0130 0.0050 153 LYS A CA 1014 C C . LYS A 127 ? 0.1843 0.1885 0.1568 0.0191 -0.0078 -0.0045 153 LYS A C 1015 O O . LYS A 127 ? 0.1698 0.1596 0.1526 0.0212 -0.0079 0.0030 153 LYS A O 1016 C CB . LYS A 127 ? 0.2637 0.2779 0.2281 0.0141 -0.0184 -0.0038 153 LYS A CB 1017 C CG . LYS A 127 ? 0.2729 0.2661 0.2505 0.0142 -0.0205 0.0006 153 LYS A CG 1018 C CD . LYS A 127 ? 0.3104 0.3079 0.2892 0.0109 -0.0261 0.0015 153 LYS A CD 1019 C CE . LYS A 127 ? 0.3331 0.3279 0.3234 0.0053 -0.0269 -0.0130 153 LYS A CE 1020 N NZ . LYS A 127 ? 0.3273 0.3393 0.3130 0.0014 -0.0259 -0.0317 153 LYS A NZ 1021 N N . SER A 128 ? 0.1662 0.1813 0.1396 0.0178 -0.0030 -0.0219 154 SER A N 1022 C CA . SER A 128 ? 0.1860 0.1911 0.1782 0.0208 0.0033 -0.0319 154 SER A CA 1023 C C . SER A 128 ? 0.2153 0.2031 0.2310 0.0201 0.0028 -0.0434 154 SER A C 1024 O O . SER A 128 ? 0.2221 0.1965 0.2620 0.0244 0.0063 -0.0431 154 SER A O 1025 C CB . SER A 128 ? 0.2660 0.2931 0.2531 0.0205 0.0122 -0.0468 154 SER A CB 1026 O OG . SER A 128 ? 0.3444 0.3910 0.3227 0.0148 0.0128 -0.0671 154 SER A OG 1027 N N . ASN A 129 ? 0.2094 0.1990 0.2231 0.0146 -0.0012 -0.0518 155 ASN A N 1028 C CA . ASN A 129 ? 0.1985 0.1698 0.2405 0.0125 -0.0008 -0.0601 155 ASN A CA 1029 C C . ASN A 129 ? 0.2269 0.1891 0.2668 0.0105 -0.0087 -0.0418 155 ASN A C 1030 O O . ASN A 129 ? 0.2665 0.2404 0.2904 0.0060 -0.0137 -0.0420 155 ASN A O 1031 C CB . ASN A 129 ? 0.2896 0.2719 0.3383 0.0053 0.0026 -0.0901 155 ASN A CB 1032 C CG . ASN A 129 ? 0.4586 0.4190 0.5445 0.0016 0.0042 -0.0988 155 ASN A CG 1033 O OD1 . ASN A 129 ? 0.4857 0.4237 0.5942 0.0060 0.0037 -0.0795 155 ASN A OD1 1034 N ND2 . ASN A 129 ? 0.5427 0.5129 0.6375 -0.0073 0.0064 -0.1275 155 ASN A ND2 1035 N N . TRP A 130 ? 0.1847 0.1315 0.2410 0.0137 -0.0096 -0.0248 156 TRP A N 1036 C CA . TRP A 130 ? 0.1479 0.0926 0.1996 0.0114 -0.0156 -0.0068 156 TRP A CA 1037 C C . TRP A 130 ? 0.1635 0.0989 0.2378 0.0058 -0.0163 -0.0069 156 TRP A C 1038 O O . TRP A 130 ? 0.1634 0.1010 0.2351 0.0030 -0.0199 0.0078 156 TRP A O 1039 C CB . TRP A 130 ? 0.1423 0.0862 0.1956 0.0157 -0.0170 0.0132 156 TRP A CB 1040 C CG . TRP A 130 ? 0.1314 0.0850 0.1638 0.0183 -0.0174 0.0162 156 TRP A CG 1041 C CD1 . TRP A 130 ? 0.1597 0.1202 0.1765 0.0192 -0.0152 0.0072 156 TRP A CD1 1042 C CD2 . TRP A 130 ? 0.1331 0.0935 0.1605 0.0190 -0.0198 0.0293 156 TRP A CD2 1043 N NE1 . TRP A 130 ? 0.1589 0.1247 0.1663 0.0206 -0.0152 0.0154 156 TRP A NE1 1044 C CE2 . TRP A 130 ? 0.1517 0.1175 0.1654 0.0200 -0.0180 0.0257 156 TRP A CE2 1045 C CE3 . TRP A 130 ? 0.1488 0.1160 0.1826 0.0175 -0.0228 0.0432 156 TRP A CE3 1046 C CZ2 . TRP A 130 ? 0.1589 0.1324 0.1689 0.0190 -0.0188 0.0313 156 TRP A CZ2 1047 C CZ3 . TRP A 130 ? 0.1402 0.1216 0.1642 0.0160 -0.0240 0.0468 156 TRP A CZ3 1048 C CH2 . TRP A 130 ? 0.1664 0.1485 0.1813 0.0168 -0.0224 0.0399 156 TRP A CH2 1049 N N . HIS A 131 ? 0.1595 0.0860 0.2591 0.0033 -0.0114 -0.0244 157 HIS A N 1050 C CA . HIS A 131 ? 0.1938 0.1094 0.3223 -0.0035 -0.0108 -0.0249 157 HIS A CA 1051 C C . HIS A 131 ? 0.2376 0.1667 0.3513 -0.0122 -0.0151 -0.0367 157 HIS A C 1052 O O . HIS A 131 ? 0.3187 0.2452 0.4451 -0.0182 -0.0170 -0.0279 157 HIS A O 1053 C CB . HIS A 131 ? 0.2089 0.1161 0.3712 -0.0037 -0.0024 -0.0404 157 HIS A CB 1054 C CG . HIS A 131 ? 0.2540 0.1569 0.4442 -0.0102 -0.0002 -0.0388 157 HIS A CG 1055 N ND1 . HIS A 131 ? 0.2581 0.1591 0.4596 -0.0101 -0.0020 -0.0102 157 HIS A ND1 1056 C CD2 . HIS A 131 ? 0.2689 0.1728 0.4780 -0.0176 0.0039 -0.0623 157 HIS A CD2 1057 C CE1 . HIS A 131 ? 0.2757 0.1730 0.5041 -0.0164 0.0012 -0.0149 157 HIS A CE1 1058 N NE2 . HIS A 131 ? 0.2948 0.1924 0.5298 -0.0211 0.0049 -0.0472 157 HIS A NE2 1059 N N . LYS A 132 ? 0.2230 0.1708 0.3113 -0.0130 -0.0168 -0.0541 158 LYS A N 1060 C CA . LYS A 132 ? 0.2988 0.2660 0.3775 -0.0214 -0.0217 -0.0672 158 LYS A CA 1061 C C . LYS A 132 ? 0.2542 0.2455 0.2967 -0.0177 -0.0274 -0.0601 158 LYS A C 1062 O O . LYS A 132 ? 0.2700 0.2629 0.2962 -0.0104 -0.0258 -0.0528 158 LYS A O 1063 C CB . LYS A 132 ? 0.4439 0.4187 0.5378 -0.0292 -0.0175 -0.1014 158 LYS A CB 1064 C CG . LYS A 132 ? 0.5472 0.5202 0.6690 -0.0408 -0.0178 -0.1148 158 LYS A CG 1065 C CD . LYS A 132 ? 0.6076 0.5514 0.7622 -0.0390 -0.0131 -0.0935 158 LYS A CD 1066 C CE . LYS A 132 ? 0.7128 0.6532 0.8994 -0.0454 -0.0064 -0.1076 158 LYS A CE 1067 N NZ . LYS A 132 ? 0.7593 0.7078 0.9532 -0.0449 0.0010 -0.1361 158 LYS A NZ 1068 N N . GLY A 133 ? 0.2475 0.2586 0.2825 -0.0226 -0.0338 -0.0604 159 GLY A N 1069 C CA . GLY A 133 ? 0.2720 0.3093 0.2807 -0.0187 -0.0392 -0.0521 159 GLY A CA 1070 C C . GLY A 133 ? 0.2531 0.2862 0.2543 -0.0112 -0.0414 -0.0270 159 GLY A C 1071 O O . GLY A 133 ? 0.2793 0.3298 0.2663 -0.0064 -0.0444 -0.0166 159 GLY A O 1072 N N . TRP A 134 ? 0.2055 0.2189 0.2189 -0.0107 -0.0390 -0.0172 160 TRP A N 1073 C CA . TRP A 134 ? 0.1824 0.1956 0.1914 -0.0052 -0.0393 -0.0002 160 TRP A CA 1074 C C . TRP A 134 ? 0.1778 0.2083 0.1930 -0.0079 -0.0436 0.0020 160 TRP A C 1075 O O . TRP A 134 ? 0.2131 0.2521 0.2384 -0.0158 -0.0463 -0.0079 160 TRP A O 1076 C CB . TRP A 134 ? 0.1635 0.1596 0.1805 -0.0052 -0.0351 0.0083 160 TRP A CB 1077 C CG . TRP A 134 ? 0.1525 0.1350 0.1674 -0.0016 -0.0317 0.0100 160 TRP A CG 1078 C CD1 . TRP A 134 ? 0.1631 0.1327 0.1921 -0.0034 -0.0292 0.0072 160 TRP A CD1 1079 C CD2 . TRP A 134 ? 0.1800 0.1611 0.1835 0.0045 -0.0299 0.0157 160 TRP A CD2 1080 N NE1 . TRP A 134 ? 0.1678 0.1311 0.1931 0.0020 -0.0268 0.0115 160 TRP A NE1 1081 C CE2 . TRP A 134 ? 0.1787 0.1493 0.1871 0.0059 -0.0273 0.0158 160 TRP A CE2 1082 C CE3 . TRP A 134 ? 0.1524 0.1396 0.1479 0.0087 -0.0296 0.0206 160 TRP A CE3 1083 C CZ2 . TRP A 134 ? 0.1852 0.1545 0.1873 0.0103 -0.0253 0.0198 160 TRP A CZ2 1084 C CZ3 . TRP A 134 ? 0.1629 0.1452 0.1543 0.0123 -0.0266 0.0237 160 TRP A CZ3 1085 C CH2 . TRP A 134 ? 0.1660 0.1409 0.1589 0.0125 -0.0249 0.0228 160 TRP A CH2 1086 N N . ASN A 135 ? 0.1701 0.2062 0.1841 -0.0016 -0.0432 0.0135 161 ASN A N 1087 C CA . ASN A 135 ? 0.1473 0.1994 0.1727 -0.0024 -0.0455 0.0170 161 ASN A CA 1088 C C . ASN A 135 ? 0.1705 0.2135 0.2041 -0.0048 -0.0396 0.0201 161 ASN A C 1089 O O . ASN A 135 ? 0.1657 0.2019 0.1962 0.0000 -0.0346 0.0244 161 ASN A O 1090 C CB . ASN A 135 ? 0.1320 0.1968 0.1590 0.0071 -0.0468 0.0278 161 ASN A CB 1091 C CG . ASN A 135 ? 0.1996 0.2835 0.2440 0.0084 -0.0486 0.0321 161 ASN A CG 1092 O OD1 . ASN A 135 ? 0.1997 0.2868 0.2532 0.0020 -0.0474 0.0271 161 ASN A OD1 1093 N ND2 . ASN A 135 ? 0.1999 0.2987 0.2531 0.0173 -0.0511 0.0440 161 ASN A ND2 1094 N N . TRP A 136 ? 0.1356 0.1821 0.1808 -0.0135 -0.0398 0.0175 162 TRP A N 1095 C CA . TRP A 136 ? 0.1256 0.1701 0.1773 -0.0173 -0.0338 0.0243 162 TRP A CA 1096 C C . TRP A 136 ? 0.1328 0.1980 0.1962 -0.0184 -0.0316 0.0264 162 TRP A C 1097 O O . TRP A 136 ? 0.1679 0.2395 0.2375 -0.0241 -0.0262 0.0319 162 TRP A O 1098 C CB . TRP A 136 ? 0.1476 0.1815 0.2112 -0.0267 -0.0331 0.0253 162 TRP A CB 1099 C CG . TRP A 136 ? 0.1469 0.1600 0.2069 -0.0250 -0.0321 0.0260 162 TRP A CG 1100 C CD1 . TRP A 136 ? 0.1734 0.1758 0.2351 -0.0252 -0.0343 0.0142 162 TRP A CD1 1101 C CD2 . TRP A 136 ? 0.1616 0.1678 0.2185 -0.0232 -0.0284 0.0387 162 TRP A CD2 1102 N NE1 . TRP A 136 ? 0.1904 0.1759 0.2536 -0.0223 -0.0314 0.0190 162 TRP A NE1 1103 C CE2 . TRP A 136 ? 0.1643 0.1528 0.2245 -0.0209 -0.0288 0.0358 162 TRP A CE2 1104 C CE3 . TRP A 136 ? 0.1785 0.1975 0.2304 -0.0238 -0.0248 0.0512 162 TRP A CE3 1105 C CZ2 . TRP A 136 ? 0.1997 0.1820 0.2612 -0.0181 -0.0268 0.0485 162 TRP A CZ2 1106 C CZ3 . TRP A 136 ? 0.2019 0.2188 0.2508 -0.0225 -0.0236 0.0630 162 TRP A CZ3 1107 C CH2 . TRP A 136 ? 0.2195 0.2175 0.2744 -0.0192 -0.0252 0.0633 162 TRP A CH2 1108 N N . THR A 137 ? 0.1117 0.1915 0.1803 -0.0131 -0.0352 0.0242 163 THR A N 1109 C CA . THR A 137 ? 0.1201 0.2221 0.2061 -0.0140 -0.0332 0.0253 163 THR A CA 1110 C C . THR A 137 ? 0.1270 0.2346 0.2162 -0.0107 -0.0229 0.0262 163 THR A C 1111 O O . THR A 137 ? 0.1356 0.2623 0.2385 -0.0147 -0.0181 0.0263 163 THR A O 1112 C CB . THR A 137 ? 0.1357 0.2571 0.2320 -0.0075 -0.0402 0.0262 163 THR A CB 1113 O OG1 . THR A 137 ? 0.1700 0.2846 0.2624 0.0046 -0.0392 0.0309 163 THR A OG1 1114 C CG2 . THR A 137 ? 0.1422 0.2706 0.2346 -0.0144 -0.0503 0.0210 163 THR A CG2 1115 N N . SER A 138 ? 0.1638 0.2585 0.2414 -0.0050 -0.0188 0.0245 164 SER A N 1116 C CA . SER A 138 ? 0.1748 0.2794 0.2552 -0.0037 -0.0083 0.0190 164 SER A CA 1117 C C . SER A 138 ? 0.2394 0.3512 0.3082 -0.0141 -0.0040 0.0229 164 SER A C 1118 O O . SER A 138 ? 0.3056 0.4364 0.3735 -0.0164 0.0050 0.0174 164 SER A O 1119 C CB . SER A 138 ? 0.2075 0.2986 0.2848 0.0046 -0.0054 0.0130 164 SER A CB 1120 O OG . SER A 138 ? 0.2963 0.3700 0.3538 0.0020 -0.0091 0.0161 164 SER A OG 1121 N N . GLY A 139 ? 0.1756 0.2760 0.2386 -0.0205 -0.0097 0.0326 165 GLY A N 1122 C CA . GLY A 139 ? 0.1994 0.3057 0.2561 -0.0290 -0.0068 0.0439 165 GLY A CA 1123 C C . GLY A 139 ? 0.2332 0.3218 0.2760 -0.0269 -0.0101 0.0481 165 GLY A C 1124 O O . GLY A 139 ? 0.2753 0.3578 0.3202 -0.0319 -0.0119 0.0617 165 GLY A O 1125 N N . PHE A 140 ? 0.2156 0.2961 0.2493 -0.0193 -0.0102 0.0377 166 PHE A N 1126 C CA . PHE A 140 ? 0.1875 0.2524 0.2104 -0.0169 -0.0135 0.0402 166 PHE A CA 1127 C C . PHE A 140 ? 0.1761 0.2191 0.1999 -0.0102 -0.0187 0.0344 166 PHE A C 1128 O O . PHE A 140 ? 0.1699 0.2150 0.2009 -0.0068 -0.0197 0.0293 166 PHE A O 1129 C CB . PHE A 140 ? 0.2078 0.2859 0.2205 -0.0162 -0.0090 0.0327 166 PHE A CB 1130 C CG . PHE A 140 ? 0.2125 0.2949 0.2324 -0.0113 -0.0033 0.0158 166 PHE A CG 1131 C CD1 . PHE A 140 ? 0.1984 0.2611 0.2227 -0.0036 -0.0045 0.0093 166 PHE A CD1 1132 C CD2 . PHE A 140 ? 0.2151 0.3221 0.2421 -0.0142 0.0045 0.0077 166 PHE A CD2 1133 C CE1 . PHE A 140 ? 0.2546 0.3185 0.2950 0.0019 0.0016 -0.0026 166 PHE A CE1 1134 C CE2 . PHE A 140 ? 0.2500 0.3588 0.2926 -0.0083 0.0113 -0.0088 166 PHE A CE2 1135 C CZ . PHE A 140 ? 0.2735 0.3587 0.3253 0.0002 0.0097 -0.0128 166 PHE A CZ 1136 N N . ASN A 141 ? 0.1701 0.1779 0.2914 0.0196 0.0473 0.0550 167 ASN A N 1137 C CA . ASN A 141 ? 0.1383 0.1636 0.2640 0.0189 0.0309 0.0564 167 ASN A CA 1138 C C . ASN A 141 ? 0.1580 0.1825 0.2797 0.0225 0.0307 0.0601 167 ASN A C 1139 O O . ASN A 141 ? 0.1796 0.1890 0.2810 0.0231 0.0380 0.0574 167 ASN A O 1140 C CB . ASN A 141 ? 0.1379 0.1638 0.2418 0.0150 0.0201 0.0502 167 ASN A CB 1141 C CG . ASN A 141 ? 0.1574 0.1666 0.2316 0.0151 0.0248 0.0455 167 ASN A CG 1142 O OD1 . ASN A 141 ? 0.1801 0.1749 0.2454 0.0156 0.0356 0.0438 167 ASN A OD1 1143 N ND2 . ASN A 141 ? 0.1689 0.1799 0.2277 0.0145 0.0165 0.0433 167 ASN A ND2 1144 N N . LYS A 142 ? 0.1234 0.1636 0.2643 0.0249 0.0224 0.0664 168 LYS A N 1145 C CA . LYS A 142 ? 0.1238 0.1633 0.2602 0.0288 0.0217 0.0707 168 LYS A CA 1146 C C . LYS A 142 ? 0.1547 0.2084 0.2879 0.0279 0.0044 0.0720 168 LYS A C 1147 O O . LYS A 142 ? 0.1284 0.1948 0.2699 0.0247 -0.0064 0.0708 168 LYS A O 1148 C CB . LYS A 142 ? 0.1683 0.2100 0.3309 0.0347 0.0312 0.0796 168 LYS A CB 1149 C CG . LYS A 142 ? 0.2127 0.2381 0.3789 0.0354 0.0505 0.0787 168 LYS A CG 1150 C CD . LYS A 142 ? 0.2552 0.2807 0.4470 0.0420 0.0621 0.0880 168 LYS A CD 1151 C CE . LYS A 142 ? 0.3501 0.3994 0.5790 0.0451 0.0529 0.0964 168 LYS A CE 1152 N NZ . LYS A 142 ? 0.4561 0.5017 0.7071 0.0486 0.0663 0.1036 168 LYS A NZ 1153 N N . CYS A 143 ? 0.1537 0.2036 0.2735 0.0302 0.0028 0.0737 169 CYS A N 1154 C CA . CYS A 143 ? 0.1547 0.2146 0.2683 0.0301 -0.0116 0.0757 169 CYS A CA 1155 C C . CYS A 143 ? 0.1672 0.2448 0.3056 0.0336 -0.0207 0.0845 169 CYS A C 1156 O O . CYS A 143 ? 0.2088 0.2893 0.3691 0.0393 -0.0139 0.0924 169 CYS A O 1157 C CB . CYS A 143 ? 0.1330 0.1833 0.2298 0.0329 -0.0083 0.0770 169 CYS A CB 1158 S SG . CYS A 143 ? 0.2664 0.3003 0.3359 0.0278 -0.0018 0.0659 169 CYS A SG 1159 N N . ALA A 144 ? 0.1967 0.2858 0.3318 0.0302 -0.0362 0.0831 170 ALA A N 1160 C CA . ALA A 144 ? 0.2267 0.3310 0.3772 0.0315 -0.0474 0.0882 170 ALA A CA 1161 C C . ALA A 144 ? 0.2447 0.3459 0.3886 0.0378 -0.0473 0.0951 170 ALA A C 1162 O O . ALA A 144 ? 0.2355 0.3250 0.3604 0.0400 -0.0426 0.0958 170 ALA A O 1163 C CB . ALA A 144 ? 0.2811 0.3918 0.4189 0.0246 -0.0620 0.0812 170 ALA A CB 1164 N N . VAL A 145 ? 0.2622 0.3737 0.4226 0.0408 -0.0521 0.1004 171 VAL A N 1165 C CA . VAL A 145 ? 0.2753 0.3844 0.4300 0.0475 -0.0529 0.1078 171 VAL A CA 1166 C C . VAL A 145 ? 0.3477 0.4514 0.4720 0.0464 -0.0627 0.1048 171 VAL A C 1167 O O . VAL A 145 ? 0.3946 0.5033 0.5085 0.0409 -0.0745 0.0983 171 VAL A O 1168 C CB . VAL A 145 ? 0.3856 0.5091 0.5639 0.0510 -0.0591 0.1141 171 VAL A CB 1169 C CG1 . VAL A 145 ? 0.4456 0.5832 0.6244 0.0458 -0.0764 0.1088 171 VAL A CG1 1170 C CG2 . VAL A 145 ? 0.4283 0.5484 0.6021 0.0592 -0.0581 0.1231 171 VAL A CG2 1171 N N . GLY A 146 ? 0.3683 0.4596 0.4776 0.0512 -0.0558 0.1089 172 GLY A N 1172 C CA . GLY A 146 ? 0.3798 0.4623 0.4596 0.0505 -0.0619 0.1065 172 GLY A CA 1173 C C . GLY A 146 ? 0.3891 0.4609 0.4498 0.0452 -0.0575 0.0991 172 GLY A C 1174 O O . GLY A 146 ? 0.4326 0.4945 0.4694 0.0447 -0.0591 0.0974 172 GLY A O 1175 N N . ALA A 147 ? 0.3108 0.3839 0.3816 0.0414 -0.0517 0.0949 173 ALA A N 1176 C CA . ALA A 147 ? 0.3017 0.3660 0.3562 0.0368 -0.0480 0.0883 173 ALA A CA 1177 C C . ALA A 147 ? 0.3407 0.3908 0.3904 0.0397 -0.0328 0.0891 173 ALA A C 1178 O O . ALA A 147 ? 0.3922 0.4385 0.4524 0.0393 -0.0224 0.0866 173 ALA A O 1179 C CB . ALA A 147 ? 0.3170 0.3872 0.3812 0.0311 -0.0491 0.0819 173 ALA A CB 1180 N N . ALA A 148 ? 0.2755 0.3153 0.3071 0.0414 -0.0302 0.0902 174 ALA A N 1181 C CA . ALA A 148 ? 0.2340 0.2592 0.2613 0.0432 -0.0149 0.0893 174 ALA A CA 1182 C C . ALA A 148 ? 0.1883 0.2059 0.2098 0.0365 -0.0074 0.0774 174 ALA A C 1183 O O . ALA A 148 ? 0.2021 0.2196 0.2117 0.0310 -0.0124 0.0698 174 ALA A O 1184 C CB . ALA A 148 ? 0.2770 0.2925 0.2869 0.0462 -0.0133 0.0932 174 ALA A CB 1185 N N . CYS A 149 ? 0.1771 0.1873 0.2060 0.0370 0.0051 0.0761 175 CYS A N 1186 C CA . CYS A 149 ? 0.1693 0.1710 0.1901 0.0310 0.0119 0.0652 175 CYS A CA 1187 C C . CYS A 149 ? 0.1546 0.1469 0.1616 0.0290 0.0160 0.0612 175 CYS A C 1188 O O . CYS A 149 ? 0.1945 0.1796 0.2007 0.0330 0.0229 0.0668 175 CYS A O 1189 C CB . CYS A 149 ? 0.1913 0.1850 0.2203 0.0315 0.0245 0.0644 175 CYS A CB 1190 S SG . CYS A 149 ? 0.2441 0.2460 0.2880 0.0317 0.0223 0.0656 175 CYS A SG 1191 N N . GLN A 150 ? 0.1593 0.1516 0.1571 0.0231 0.0127 0.0521 176 GLN A N 1192 C CA . GLN A 150 ? 0.1528 0.1378 0.1410 0.0202 0.0166 0.0470 176 GLN A CA 1193 C C . GLN A 150 ? 0.1561 0.1406 0.1425 0.0139 0.0174 0.0361 176 GLN A C 1194 O O . GLN A 150 ? 0.1717 0.1614 0.1598 0.0122 0.0126 0.0332 176 GLN A O 1195 C CB . GLN A 150 ? 0.1637 0.1517 0.1425 0.0205 0.0085 0.0488 176 GLN A CB 1196 C CG . GLN A 150 ? 0.1642 0.1540 0.1408 0.0266 0.0040 0.0596 176 GLN A CG 1197 C CD . GLN A 150 ? 0.1986 0.1772 0.1717 0.0313 0.0138 0.0658 176 GLN A CD 1198 O OE1 . GLN A 150 ? 0.2133 0.1832 0.1902 0.0302 0.0258 0.0626 176 GLN A OE1 1199 N NE2 . GLN A 150 ? 0.2004 0.1781 0.1649 0.0364 0.0091 0.0747 176 GLN A NE2 1200 N N . PRO A 151 ? 0.1669 0.1451 0.1501 0.0104 0.0233 0.0301 177 PRO A N 1201 C CA . PRO A 151 ? 0.1851 0.1658 0.1677 0.0045 0.0209 0.0201 177 PRO A CA 1202 C C . PRO A 151 ? 0.1883 0.1783 0.1684 0.0038 0.0100 0.0187 177 PRO A C 1203 O O . PRO A 151 ? 0.1856 0.1782 0.1625 0.0060 0.0056 0.0231 177 PRO A O 1204 C CB . PRO A 151 ? 0.1975 0.1725 0.1804 0.0014 0.0277 0.0155 177 PRO A CB 1205 C CG . PRO A 151 ? 0.2002 0.1652 0.1833 0.0052 0.0380 0.0218 177 PRO A CG 1206 C CD . PRO A 151 ? 0.1944 0.1631 0.1757 0.0117 0.0325 0.0324 177 PRO A CD 1207 N N . PHE A 152 ? 0.1721 0.1660 0.1522 0.0009 0.0059 0.0129 178 PHE A N 1208 C CA . PHE A 152 ? 0.1905 0.1917 0.1688 0.0009 -0.0027 0.0121 178 PHE A CA 1209 C C . PHE A 152 ? 0.1771 0.1801 0.1542 0.0004 -0.0047 0.0117 178 PHE A C 1210 O O . PHE A 152 ? 0.1958 0.2015 0.1698 0.0017 -0.0095 0.0146 178 PHE A O 1211 C CB . PHE A 152 ? 0.2263 0.2299 0.2035 -0.0016 -0.0060 0.0059 178 PHE A CB 1212 C CG . PHE A 152 ? 0.2331 0.2384 0.2072 0.0002 -0.0101 0.0080 178 PHE A CG 1213 C CD1 . PHE A 152 ? 0.2263 0.2269 0.2000 0.0017 -0.0058 0.0109 178 PHE A CD1 1214 C CD2 . PHE A 152 ? 0.3361 0.3464 0.3087 0.0008 -0.0163 0.0074 178 PHE A CD2 1215 C CE1 . PHE A 152 ? 0.2652 0.2658 0.2372 0.0033 -0.0075 0.0129 178 PHE A CE1 1216 C CE2 . PHE A 152 ? 0.2464 0.2565 0.2162 0.0025 -0.0181 0.0095 178 PHE A CE2 1217 C CZ . PHE A 152 ? 0.2729 0.2781 0.2425 0.0036 -0.0136 0.0121 178 PHE A CZ 1218 N N . HIS A 153 ? 0.1663 0.1665 0.1463 -0.0020 0.0003 0.0076 179 HIS A N 1219 C CA . HIS A 153 ? 0.1956 0.1953 0.1750 -0.0026 0.0011 0.0069 179 HIS A CA 1220 C C . HIS A 153 ? 0.1854 0.1783 0.1563 0.0002 0.0038 0.0133 179 HIS A C 1221 O O . HIS A 153 ? 0.1962 0.1860 0.1626 -0.0002 0.0050 0.0131 179 HIS A O 1222 C CB . HIS A 153 ? 0.1613 0.1607 0.1495 -0.0062 0.0063 0.0003 179 HIS A CB 1223 C CG . HIS A 153 ? 0.1732 0.1813 0.1685 -0.0088 0.0003 -0.0057 179 HIS A CG 1224 N ND1 . HIS A 153 ? 0.1752 0.1868 0.1817 -0.0128 0.0020 -0.0126 179 HIS A ND1 1225 C CD2 . HIS A 153 ? 0.1404 0.1544 0.1331 -0.0076 -0.0077 -0.0057 179 HIS A CD2 1226 C CE1 . HIS A 153 ? 0.1873 0.2075 0.1967 -0.0137 -0.0063 -0.0162 179 HIS A CE1 1227 N NE2 . HIS A 153 ? 0.1654 0.1860 0.1653 -0.0103 -0.0116 -0.0117 179 HIS A NE2 1228 N N . PHE A 154 ? 0.1556 0.1457 0.1238 0.0032 0.0047 0.0192 180 PHE A N 1229 C CA . PHE A 154 ? 0.1745 0.1601 0.1332 0.0066 0.0041 0.0264 180 PHE A CA 1230 C C . PHE A 154 ? 0.1906 0.1821 0.1441 0.0064 -0.0056 0.0276 180 PHE A C 1231 O O . PHE A 154 ? 0.1976 0.1850 0.1403 0.0062 -0.0071 0.0288 180 PHE A O 1232 C CB . PHE A 154 ? 0.1888 0.1724 0.1497 0.0107 0.0065 0.0333 180 PHE A CB 1233 C CG . PHE A 154 ? 0.1911 0.1716 0.1426 0.0153 0.0038 0.0422 180 PHE A CG 1234 C CD1 . PHE A 154 ? 0.1791 0.1676 0.1283 0.0165 -0.0072 0.0461 180 PHE A CD1 1235 C CD2 . PHE A 154 ? 0.1842 0.1535 0.1288 0.0184 0.0121 0.0469 180 PHE A CD2 1236 C CE1 . PHE A 154 ? 0.2070 0.1941 0.1470 0.0204 -0.0120 0.0542 180 PHE A CE1 1237 C CE2 . PHE A 154 ? 0.2127 0.1787 0.1460 0.0235 0.0084 0.0561 180 PHE A CE2 1238 C CZ . PHE A 154 ? 0.2258 0.2015 0.1565 0.0244 -0.0049 0.0596 180 PHE A CZ 1239 N N . TYR A 155 ? 0.1389 0.1383 0.0990 0.0060 -0.0111 0.0267 181 TYR A N 1240 C CA . TYR A 155 ? 0.1737 0.1786 0.1312 0.0052 -0.0192 0.0273 181 TYR A CA 1241 C C . TYR A 155 ? 0.1861 0.1919 0.1428 0.0023 -0.0201 0.0213 181 TYR A C 1242 O O . TYR A 155 ? 0.1873 0.1937 0.1387 0.0008 -0.0242 0.0208 181 TYR A O 1243 C CB . TYR A 155 ? 0.1717 0.1834 0.1380 0.0066 -0.0229 0.0300 181 TYR A CB 1244 C CG . TYR A 155 ? 0.1597 0.1726 0.1285 0.0102 -0.0242 0.0376 181 TYR A CG 1245 C CD1 . TYR A 155 ? 0.2039 0.2191 0.1666 0.0109 -0.0313 0.0419 181 TYR A CD1 1246 C CD2 . TYR A 155 ? 0.1326 0.1442 0.1098 0.0131 -0.0183 0.0408 181 TYR A CD2 1247 C CE1 . TYR A 155 ? 0.2023 0.2205 0.1686 0.0151 -0.0341 0.0501 181 TYR A CE1 1248 C CE2 . TYR A 155 ? 0.1868 0.2000 0.1687 0.0177 -0.0189 0.0492 181 TYR A CE2 1249 C CZ . TYR A 155 ? 0.2040 0.2215 0.1813 0.0191 -0.0276 0.0543 181 TYR A CZ 1250 O OH . TYR A 155 ? 0.2126 0.2336 0.1959 0.0245 -0.0299 0.0636 181 TYR A OH 1251 N N . PHE A 156 ? 0.1613 0.1673 0.1239 0.0013 -0.0162 0.0167 182 PHE A N 1252 C CA . PHE A 156 ? 0.1315 0.1397 0.0965 -0.0003 -0.0168 0.0120 182 PHE A CA 1253 C C . PHE A 156 ? 0.1478 0.1532 0.1169 -0.0016 -0.0108 0.0085 182 PHE A C 1254 O O . PHE A 156 ? 0.1605 0.1695 0.1382 -0.0024 -0.0099 0.0049 182 PHE A O 1255 C CB . PHE A 156 ? 0.1630 0.1767 0.1337 0.0001 -0.0200 0.0101 182 PHE A CB 1256 C CG . PHE A 156 ? 0.1466 0.1622 0.1161 0.0012 -0.0236 0.0133 182 PHE A CG 1257 C CD1 . PHE A 156 ? 0.1451 0.1613 0.1116 0.0005 -0.0267 0.0142 182 PHE A CD1 1258 C CD2 . PHE A 156 ? 0.1659 0.1818 0.1383 0.0023 -0.0226 0.0149 182 PHE A CD2 1259 C CE1 . PHE A 156 ? 0.1714 0.1901 0.1401 0.0008 -0.0294 0.0166 182 PHE A CE1 1260 C CE2 . PHE A 156 ? 0.1746 0.1921 0.1489 0.0033 -0.0244 0.0179 182 PHE A CE2 1261 C CZ . PHE A 156 ? 0.1866 0.2064 0.1603 0.0025 -0.0281 0.0187 182 PHE A CZ 1262 N N . PRO A 157 ? 0.1645 0.1627 0.1272 -0.0020 -0.0063 0.0091 183 PRO A N 1263 C CA . PRO A 157 ? 0.1890 0.1831 0.1575 -0.0032 0.0019 0.0062 183 PRO A CA 1264 C C . PRO A 157 ? 0.2041 0.2042 0.1861 -0.0046 0.0026 0.0011 183 PRO A C 1265 O O . PRO A 157 ? 0.1933 0.1937 0.1860 -0.0062 0.0083 -0.0023 183 PRO A O 1266 C CB . PRO A 157 ? 0.2048 0.1870 0.1594 -0.0030 0.0072 0.0089 183 PRO A CB 1267 C CG . PRO A 157 ? 0.2478 0.2293 0.1895 -0.0015 0.0002 0.0140 183 PRO A CG 1268 C CD . PRO A 157 ? 0.2118 0.2039 0.1604 -0.0017 -0.0078 0.0128 183 PRO A CD 1269 N N . THR A 158 ? 0.1728 0.1777 0.1556 -0.0038 -0.0024 0.0009 184 THR A N 1270 C CA . THR A 158 ? 0.1199 0.1322 0.1171 -0.0036 -0.0029 -0.0023 184 THR A CA 1271 C C . THR A 158 ? 0.1262 0.1460 0.1239 -0.0016 -0.0114 -0.0015 184 THR A C 1272 O O . THR A 158 ? 0.1475 0.1651 0.1348 -0.0010 -0.0147 0.0012 184 THR A O 1273 C CB . THR A 158 ? 0.2162 0.2225 0.2137 -0.0034 0.0035 -0.0025 184 THR A CB 1274 O OG1 . THR A 158 ? 0.2481 0.2498 0.2325 -0.0028 0.0011 -0.0001 184 THR A OG1 1275 C CG2 . THR A 158 ? 0.2742 0.2693 0.2669 -0.0051 0.0136 -0.0028 184 THR A CG2 1276 N N . PRO A 159 ? 0.1514 0.1801 0.1617 -0.0004 -0.0148 -0.0034 185 PRO A N 1277 C CA . PRO A 159 ? 0.1206 0.1539 0.1284 0.0024 -0.0218 -0.0016 185 PRO A CA 1278 C C . PRO A 159 ? 0.1516 0.1789 0.1513 0.0040 -0.0200 0.0014 185 PRO A C 1279 O O . PRO A 159 ? 0.1612 0.1874 0.1530 0.0053 -0.0234 0.0035 185 PRO A O 1280 C CB . PRO A 159 ? 0.1513 0.1947 0.1747 0.0041 -0.0252 -0.0033 185 PRO A CB 1281 C CG . PRO A 159 ? 0.1951 0.2420 0.2295 0.0004 -0.0229 -0.0078 185 PRO A CG 1282 C CD . PRO A 159 ? 0.1720 0.2078 0.1998 -0.0018 -0.0134 -0.0073 185 PRO A CD 1283 N N . THR A 160 ? 0.1528 0.1749 0.1542 0.0036 -0.0135 0.0012 186 THR A N 1284 C CA . THR A 160 ? 0.1682 0.1827 0.1604 0.0038 -0.0108 0.0028 186 THR A CA 1285 C C . THR A 160 ? 0.1864 0.1958 0.1641 0.0013 -0.0132 0.0037 186 THR A C 1286 O O . THR A 160 ? 0.1644 0.1726 0.1373 0.0016 -0.0154 0.0049 186 THR A O 1287 C CB . THR A 160 ? 0.2060 0.2124 0.1993 0.0028 -0.0017 0.0016 186 THR A CB 1288 O OG1 . THR A 160 ? 0.2304 0.2433 0.2413 0.0061 0.0004 0.0018 186 THR A OG1 1289 C CG2 . THR A 160 ? 0.2222 0.2182 0.2024 0.0012 0.0017 0.0019 186 THR A CG2 1290 N N . VAL A 161 ? 0.1436 0.1503 0.1157 -0.0009 -0.0126 0.0036 187 VAL A N 1291 C CA . VAL A 161 ? 0.1492 0.1535 0.1107 -0.0025 -0.0161 0.0054 187 VAL A CA 1292 C C . VAL A 161 ? 0.1508 0.1616 0.1158 -0.0010 -0.0216 0.0070 187 VAL A C 1293 O O . VAL A 161 ? 0.1527 0.1633 0.1140 -0.0018 -0.0242 0.0082 187 VAL A O 1294 C CB . VAL A 161 ? 0.1911 0.1916 0.1470 -0.0035 -0.0143 0.0065 187 VAL A CB 1295 C CG1 . VAL A 161 ? 0.2169 0.2172 0.1644 -0.0041 -0.0194 0.0096 187 VAL A CG1 1296 C CG2 . VAL A 161 ? 0.2565 0.2471 0.2057 -0.0049 -0.0071 0.0051 187 VAL A CG2 1297 N N . LEU A 162 ? 0.1493 0.1653 0.1213 0.0007 -0.0227 0.0064 188 LEU A N 1298 C CA . LEU A 162 ? 0.1453 0.1644 0.1178 0.0021 -0.0262 0.0076 188 LEU A CA 1299 C C . LEU A 162 ? 0.1487 0.1674 0.1201 0.0037 -0.0272 0.0085 188 LEU A C 1300 O O . LEU A 162 ? 0.1408 0.1578 0.1095 0.0034 -0.0278 0.0102 188 LEU A O 1301 C CB . LEU A 162 ? 0.1456 0.1684 0.1226 0.0028 -0.0273 0.0056 188 LEU A CB 1302 C CG . LEU A 162 ? 0.1514 0.1744 0.1250 0.0044 -0.0298 0.0064 188 LEU A CG 1303 C CD1 . LEU A 162 ? 0.1804 0.2002 0.1512 0.0038 -0.0281 0.0088 188 LEU A CD1 1304 C CD2 . LEU A 162 ? 0.1801 0.2060 0.1553 0.0041 -0.0322 0.0031 188 LEU A CD2 1305 N N . CYS A 163 ? 0.1528 0.1727 0.1278 0.0058 -0.0269 0.0079 189 CYS A N 1306 C CA . CYS A 163 ? 0.1623 0.1806 0.1359 0.0087 -0.0269 0.0097 189 CYS A CA 1307 C C . CYS A 163 ? 0.1696 0.1820 0.1397 0.0067 -0.0235 0.0099 189 CYS A C 1308 O O . CYS A 163 ? 0.1636 0.1732 0.1315 0.0074 -0.0226 0.0113 189 CYS A O 1309 C CB . CYS A 163 ? 0.1754 0.1974 0.1552 0.0125 -0.0278 0.0100 189 CYS A CB 1310 S SG . CYS A 163 ? 0.2283 0.2586 0.2128 0.0129 -0.0337 0.0080 189 CYS A SG 1311 N N . ASN A 164 ? 0.1655 0.1750 0.1343 0.0038 -0.0208 0.0081 190 ASN A N 1312 C CA . ASN A 164 ? 0.1742 0.1770 0.1378 0.0006 -0.0177 0.0070 190 ASN A CA 1313 C C . ASN A 164 ? 0.1748 0.1780 0.1341 -0.0035 -0.0212 0.0067 190 ASN A C 1314 O O . ASN A 164 ? 0.1780 0.1782 0.1360 -0.0061 -0.0204 0.0057 190 ASN A O 1315 C CB . ASN A 164 ? 0.1867 0.1834 0.1475 -0.0013 -0.0126 0.0048 190 ASN A CB 1316 C CG . ASN A 164 ? 0.1814 0.1781 0.1506 0.0030 -0.0080 0.0056 190 ASN A CG 1317 O OD1 . ASN A 164 ? 0.1847 0.1875 0.1611 0.0078 -0.0107 0.0081 190 ASN A OD1 1318 N ND2 . ASN A 164 ? 0.2046 0.1940 0.1726 0.0016 -0.0009 0.0039 190 ASN A ND2 1319 N N . GLU A 165 ? 0.1501 0.1572 0.1089 -0.0040 -0.0248 0.0077 191 GLU A N 1320 C CA . GLU A 165 ? 0.1441 0.1530 0.1007 -0.0071 -0.0290 0.0084 191 GLU A CA 1321 C C . GLU A 165 ? 0.1292 0.1436 0.0935 -0.0055 -0.0312 0.0110 191 GLU A C 1322 O O . GLU A 165 ? 0.1539 0.1711 0.1213 -0.0080 -0.0341 0.0116 191 GLU A O 1323 C CB . GLU A 165 ? 0.2180 0.2263 0.1687 -0.0079 -0.0308 0.0093 191 GLU A CB 1324 C CG . GLU A 165 ? 0.3210 0.3211 0.2620 -0.0098 -0.0268 0.0068 191 GLU A CG 1325 C CD . GLU A 165 ? 0.4934 0.4876 0.4241 -0.0148 -0.0280 0.0042 191 GLU A CD 1326 O OE1 . GLU A 165 ? 0.5802 0.5782 0.5089 -0.0173 -0.0347 0.0051 191 GLU A OE1 1327 O OE2 . GLU A 165 ? 0.5076 0.4934 0.4329 -0.0165 -0.0221 0.0010 191 GLU A OE2 1328 N N . ILE A 166 ? 0.1372 0.1529 0.1048 -0.0018 -0.0297 0.0123 192 ILE A N 1329 C CA . ILE A 166 ? 0.1339 0.1521 0.1069 -0.0003 -0.0298 0.0147 192 ILE A CA 1330 C C . ILE A 166 ? 0.1542 0.1716 0.1318 -0.0014 -0.0283 0.0151 192 ILE A C 1331 O O . ILE A 166 ? 0.1525 0.1733 0.1377 -0.0022 -0.0290 0.0170 192 ILE A O 1332 C CB . ILE A 166 ? 0.1551 0.1722 0.1269 0.0030 -0.0280 0.0149 192 ILE A CB 1333 C CG1 . ILE A 166 ? 0.1790 0.1959 0.1545 0.0039 -0.0261 0.0172 192 ILE A CG1 1334 C CG2 . ILE A 166 ? 0.1666 0.1805 0.1350 0.0054 -0.0265 0.0141 192 ILE A CG2 1335 C CD1 . ILE A 166 ? 0.1820 0.1966 0.1540 0.0055 -0.0244 0.0164 192 ILE A CD1 1336 N N . TRP A 167 ? 0.1369 0.1497 0.1118 -0.0012 -0.0254 0.0135 193 TRP A N 1337 C CA . TRP A 167 ? 0.1668 0.1769 0.1461 -0.0028 -0.0220 0.0132 193 TRP A CA 1338 C C . TRP A 167 ? 0.1747 0.1827 0.1528 -0.0076 -0.0219 0.0097 193 TRP A C 1339 O O . TRP A 167 ? 0.1744 0.1764 0.1529 -0.0081 -0.0166 0.0085 193 TRP A O 1340 C CB . TRP A 167 ? 0.1546 0.1579 0.1305 0.0018 -0.0164 0.0148 193 TRP A CB 1341 C CG . TRP A 167 ? 0.1498 0.1524 0.1232 0.0056 -0.0160 0.0172 193 TRP A CG 1342 C CD1 . TRP A 167 ? 0.1849 0.1852 0.1500 0.0096 -0.0167 0.0179 193 TRP A CD1 1343 C CD2 . TRP A 167 ? 0.1934 0.1973 0.1730 0.0052 -0.0143 0.0189 193 TRP A CD2 1344 N NE1 . TRP A 167 ? 0.1807 0.1788 0.1431 0.0110 -0.0155 0.0190 193 TRP A NE1 1345 C CE2 . TRP A 167 ? 0.2168 0.2164 0.1884 0.0087 -0.0129 0.0199 193 TRP A CE2 1346 C CE3 . TRP A 167 ? 0.1943 0.2028 0.1864 0.0022 -0.0141 0.0196 193 TRP A CE3 1347 C CZ2 . TRP A 167 ? 0.2243 0.2216 0.1987 0.0092 -0.0090 0.0215 193 TRP A CZ2 1348 C CZ3 . TRP A 167 ? 0.1901 0.1983 0.1884 0.0036 -0.0107 0.0222 193 TRP A CZ3 1349 C CH2 . TRP A 167 ? 0.1836 0.1850 0.1722 0.0071 -0.0072 0.0230 193 TRP A CH2 1350 N N . THR A 168 ? 0.1896 0.2005 0.1642 -0.0111 -0.0269 0.0081 194 THR A N 1351 C CA . THR A 168 ? 0.1872 0.1951 0.1577 -0.0172 -0.0277 0.0039 194 THR A CA 1352 C C . THR A 168 ? 0.1725 0.1707 0.1382 -0.0170 -0.0202 0.0015 194 THR A C 1353 O O . THR A 168 ? 0.1871 0.1807 0.1552 -0.0204 -0.0160 -0.0012 194 THR A O 1354 C CB . THR A 168 ? 0.2973 0.3100 0.2774 -0.0223 -0.0306 0.0024 194 THR A CB 1355 O OG1 . THR A 168 ? 0.3321 0.3542 0.3215 -0.0204 -0.0356 0.0064 194 THR A OG1 1356 C CG2 . THR A 168 ? 0.2756 0.2872 0.2487 -0.0300 -0.0353 -0.0026 194 THR A CG2 1357 N N . HIS A 169 ? 0.1774 0.1727 0.1382 -0.0127 -0.0178 0.0027 195 HIS A N 1358 C CA . HIS A 169 ? 0.1864 0.1732 0.1445 -0.0109 -0.0103 0.0018 195 HIS A CA 1359 C C . HIS A 169 ? 0.1883 0.1715 0.1509 -0.0064 -0.0047 0.0043 195 HIS A C 1360 O O . HIS A 169 ? 0.1939 0.1688 0.1553 -0.0053 0.0027 0.0039 195 HIS A O 1361 C CB . HIS A 169 ? 0.2283 0.2069 0.1789 -0.0177 -0.0072 -0.0034 195 HIS A CB 1362 C CG . HIS A 169 ? 0.3726 0.3513 0.3140 -0.0209 -0.0115 -0.0051 195 HIS A CG 1363 N ND1 . HIS A 169 ? 0.3747 0.3513 0.3134 -0.0174 -0.0087 -0.0039 195 HIS A ND1 1364 C CD2 . HIS A 169 ? 0.4680 0.4486 0.4026 -0.0266 -0.0182 -0.0074 195 HIS A CD2 1365 C CE1 . HIS A 169 ? 0.4410 0.4158 0.3696 -0.0209 -0.0120 -0.0054 195 HIS A CE1 1366 N NE2 . HIS A 169 ? 0.4983 0.4755 0.4229 -0.0262 -0.0185 -0.0071 195 HIS A NE2 1367 N N . SER A 170 ? 0.1637 0.1512 0.1302 -0.0033 -0.0069 0.0075 196 SER A N 1368 C CA . SER A 170 ? 0.1635 0.1458 0.1302 0.0026 -0.0016 0.0111 196 SER A CA 1369 C C . SER A 170 ? 0.1740 0.1556 0.1383 0.0092 -0.0010 0.0141 196 SER A C 1370 O O . SER A 170 ? 0.1812 0.1558 0.1445 0.0138 0.0050 0.0168 196 SER A O 1371 C CB . SER A 170 ? 0.1774 0.1625 0.1455 0.0049 -0.0034 0.0138 196 SER A CB 1372 O OG . SER A 170 ? 0.1936 0.1798 0.1685 -0.0003 -0.0025 0.0119 196 SER A OG 1373 N N . TYR A 171 ? 0.1588 0.1479 0.1235 0.0100 -0.0070 0.0139 197 TYR A N 1374 C CA . TYR A 171 ? 0.1468 0.1381 0.1137 0.0151 -0.0075 0.0159 197 TYR A CA 1375 C C . TYR A 171 ? 0.1395 0.1299 0.1086 0.0117 -0.0051 0.0128 197 TYR A C 1376 O O . TYR A 171 ? 0.1485 0.1392 0.1146 0.0059 -0.0066 0.0093 197 TYR A O 1377 C CB . TYR A 171 ? 0.1553 0.1553 0.1232 0.0177 -0.0149 0.0169 197 TYR A CB 1378 C CG . TYR A 171 ? 0.1995 0.1989 0.1619 0.0212 -0.0174 0.0196 197 TYR A CG 1379 C CD1 . TYR A 171 ? 0.2249 0.2199 0.1833 0.0276 -0.0158 0.0239 197 TYR A CD1 1380 C CD2 . TYR A 171 ? 0.2277 0.2296 0.1876 0.0186 -0.0206 0.0183 197 TYR A CD2 1381 C CE1 . TYR A 171 ? 0.2672 0.2587 0.2162 0.0309 -0.0174 0.0264 197 TYR A CE1 1382 C CE2 . TYR A 171 ? 0.2278 0.2263 0.1803 0.0215 -0.0212 0.0204 197 TYR A CE2 1383 C CZ . TYR A 171 ? 0.2784 0.2712 0.2242 0.0274 -0.0197 0.0242 197 TYR A CZ 1384 O OH . TYR A 171 ? 0.3242 0.3109 0.2586 0.0302 -0.0196 0.0262 197 TYR A OH 1385 N N . LYS A 172 ? 0.1549 0.1439 0.1290 0.0161 -0.0011 0.0146 198 LYS A N 1386 C CA . LYS A 172 ? 0.1668 0.1551 0.1448 0.0143 0.0023 0.0124 198 LYS A CA 1387 C C . LYS A 172 ? 0.1775 0.1749 0.1668 0.0208 -0.0009 0.0157 198 LYS A C 1388 O O . LYS A 172 ? 0.1955 0.1923 0.1910 0.0270 0.0019 0.0199 198 LYS A O 1389 C CB . LYS A 172 ? 0.2108 0.1870 0.1872 0.0129 0.0129 0.0111 198 LYS A CB 1390 C CG . LYS A 172 ? 0.2607 0.2327 0.2390 0.0108 0.0189 0.0086 198 LYS A CG 1391 C CD . LYS A 172 ? 0.3287 0.2850 0.3001 0.0068 0.0303 0.0055 198 LYS A CD 1392 C CE . LYS A 172 ? 0.4830 0.4313 0.4471 0.0013 0.0355 0.0009 198 LYS A CE 1393 N NZ . LYS A 172 ? 0.5882 0.5429 0.5649 0.0059 0.0367 0.0033 198 LYS A NZ 1394 N N . VAL A 173 ? 0.1543 0.1605 0.1475 0.0195 -0.0069 0.0141 199 VAL A N 1395 C CA . VAL A 173 ? 0.1577 0.1748 0.1632 0.0246 -0.0120 0.0163 199 VAL A CA 1396 C C . VAL A 173 ? 0.1576 0.1748 0.1770 0.0287 -0.0055 0.0185 199 VAL A C 1397 O O . VAL A 173 ? 0.1766 0.1861 0.1971 0.0256 0.0034 0.0161 199 VAL A O 1398 C CB . VAL A 173 ? 0.1422 0.1675 0.1512 0.0212 -0.0175 0.0130 199 VAL A CB 1399 C CG1 . VAL A 173 ? 0.1840 0.2039 0.1926 0.0160 -0.0110 0.0094 199 VAL A CG1 1400 C CG2 . VAL A 173 ? 0.1388 0.1765 0.1624 0.0251 -0.0236 0.0140 199 VAL A CG2 1401 N N . SER A 174 ? 0.1568 0.1816 0.1857 0.0361 -0.0098 0.0234 200 SER A N 1402 C CA . SER A 174 ? 0.1537 0.1802 0.1992 0.0418 -0.0041 0.0272 200 SER A CA 1403 C C . SER A 174 ? 0.1843 0.2230 0.2499 0.0415 -0.0062 0.0254 200 SER A C 1404 O O . SER A 174 ? 0.1798 0.2281 0.2469 0.0383 -0.0149 0.0221 200 SER A O 1405 C CB . SER A 174 ? 0.1510 0.1814 0.1983 0.0510 -0.0091 0.0346 200 SER A CB 1406 O OG . SER A 174 ? 0.1584 0.1895 0.2225 0.0580 -0.0026 0.0399 200 SER A OG 1407 N N . ASN A 175 ? 0.1759 0.2136 0.2584 0.0445 0.0031 0.0274 201 ASN A N 1408 C CA . ASN A 175 ? 0.1839 0.2355 0.2917 0.0458 0.0012 0.0269 201 ASN A CA 1409 C C . ASN A 175 ? 0.1690 0.2377 0.2932 0.0544 -0.0105 0.0331 201 ASN A C 1410 O O . ASN A 175 ? 0.1624 0.2474 0.3104 0.0556 -0.0162 0.0328 201 ASN A O 1411 C CB . ASN A 175 ? 0.2360 0.2791 0.3573 0.0451 0.0174 0.0261 201 ASN A CB 1412 C CG . ASN A 175 ? 0.3031 0.3379 0.4299 0.0521 0.0275 0.0323 201 ASN A CG 1413 O OD1 . ASN A 175 ? 0.3143 0.3416 0.4258 0.0549 0.0267 0.0355 201 ASN A OD1 1414 N ND2 . ASN A 175 ? 0.3532 0.3880 0.5031 0.0551 0.0388 0.0340 201 ASN A ND2 1415 N N . TYR A 176 ? 0.2688 0.1983 0.2344 0.0452 0.0656 0.0395 202 TYR A N 1416 C CA . TYR A 176 ? 0.2391 0.1873 0.2496 0.0300 0.0567 0.0288 202 TYR A CA 1417 C C . TYR A 176 ? 0.2235 0.1686 0.2523 0.0159 0.0538 0.0289 202 TYR A C 1418 O O . TYR A 176 ? 0.2433 0.1691 0.2510 0.0210 0.0531 0.0369 202 TYR A O 1419 C CB . TYR A 176 ? 0.2670 0.2232 0.2772 0.0340 0.0341 0.0185 202 TYR A CB 1420 C CG . TYR A 176 ? 0.2946 0.2533 0.3033 0.0442 0.0414 0.0124 202 TYR A CG 1421 C CD1 . TYR A 176 ? 0.2765 0.2581 0.3216 0.0454 0.0491 0.0119 202 TYR A CD1 1422 C CD2 . TYR A 176 ? 0.3508 0.2938 0.3229 0.0538 0.0409 0.0045 202 TYR A CD2 1423 C CE1 . TYR A 176 ? 0.3539 0.3357 0.3997 0.0598 0.0600 0.0080 202 TYR A CE1 1424 C CE2 . TYR A 176 ? 0.4064 0.3440 0.3749 0.0637 0.0526 -0.0045 202 TYR A CE2 1425 C CZ . TYR A 176 ? 0.4437 0.3972 0.4495 0.0687 0.0638 -0.0006 202 TYR A CZ 1426 O OH . TYR A 176 ? 0.5223 0.4686 0.5266 0.0836 0.0794 -0.0078 202 TYR A OH 1427 N N . SER A 177 ? 0.2036 0.1723 0.2713 0.0002 0.0526 0.0185 203 SER A N 1428 C CA . SER A 177 ? 0.2066 0.1737 0.2904 -0.0169 0.0522 0.0110 203 SER A CA 1429 C C . SER A 177 ? 0.1777 0.1714 0.2711 -0.0192 0.0256 0.0014 203 SER A C 1430 O O . SER A 177 ? 0.1876 0.2005 0.2827 -0.0082 0.0117 0.0030 203 SER A O 1431 C CB . SER A 177 ? 0.2365 0.2151 0.3572 -0.0391 0.0751 0.0005 203 SER A CB 1432 O OG . SER A 177 ? 0.3138 0.2572 0.4229 -0.0374 0.1079 0.0137 203 SER A OG 1433 N N . ARG A 178 ? 0.2112 0.2022 0.3085 -0.0318 0.0229 -0.0076 204 ARG A N 1434 C CA . ARG A 178 ? 0.1874 0.2051 0.2872 -0.0328 0.0009 -0.0153 204 ARG A CA 1435 C C . ARG A 178 ? 0.1315 0.2008 0.2568 -0.0318 -0.0105 -0.0210 204 ARG A C 1436 O O . ARG A 178 ? 0.1282 0.2227 0.2829 -0.0421 -0.0003 -0.0297 204 ARG A O 1437 C CB . ARG A 178 ? 0.2178 0.2297 0.3198 -0.0501 0.0053 -0.0309 204 ARG A CB 1438 C CG . ARG A 178 ? 0.2442 0.2113 0.3213 -0.0427 0.0140 -0.0219 204 ARG A CG 1439 C CD . ARG A 178 ? 0.2888 0.2480 0.3659 -0.0573 0.0200 -0.0402 204 ARG A CD 1440 N NE . ARG A 178 ? 0.2942 0.2197 0.3504 -0.0437 0.0265 -0.0293 204 ARG A NE 1441 C CZ . ARG A 178 ? 0.3818 0.2995 0.4301 -0.0478 0.0296 -0.0411 204 ARG A CZ 1442 N NH1 . ARG A 178 ? 0.3791 0.3207 0.4327 -0.0668 0.0244 -0.0668 204 ARG A NH1 1443 N NH2 . ARG A 178 ? 0.3870 0.2800 0.4221 -0.0311 0.0375 -0.0286 204 ARG A NH2 1444 N N . GLY A 179 ? 0.1526 0.2387 0.2682 -0.0168 -0.0289 -0.0136 205 GLY A N 1445 C CA . GLY A 179 ? 0.1638 0.3026 0.2997 -0.0061 -0.0406 -0.0128 205 GLY A CA 1446 C C . GLY A 179 ? 0.1709 0.3051 0.3113 0.0154 -0.0351 0.0018 205 GLY A C 1447 O O . GLY A 179 ? 0.1757 0.3495 0.3310 0.0336 -0.0427 0.0088 205 GLY A O 1448 N N . SER A 180 ? 0.1273 0.2155 0.2521 0.0164 -0.0213 0.0061 206 SER A N 1449 C CA . SER A 180 ? 0.1704 0.2468 0.2942 0.0342 -0.0117 0.0137 206 SER A CA 1450 C C . SER A 180 ? 0.1703 0.2151 0.2717 0.0506 -0.0159 0.0236 206 SER A C 1451 O O . SER A 180 ? 0.1912 0.2244 0.2931 0.0684 -0.0066 0.0286 206 SER A O 1452 C CB . SER A 180 ? 0.1467 0.1914 0.2559 0.0284 0.0054 0.0111 206 SER A CB 1453 O OG . SER A 180 ? 0.2066 0.2145 0.2842 0.0241 0.0014 0.0118 206 SER A OG 1454 N N . GLY A 181 ? 0.1740 0.2011 0.2577 0.0434 -0.0250 0.0251 207 GLY A N 1455 C CA . GLY A 181 ? 0.1994 0.1899 0.2649 0.0504 -0.0233 0.0316 207 GLY A CA 1456 C C . GLY A 181 ? 0.1978 0.1521 0.2477 0.0442 -0.0151 0.0214 207 GLY A C 1457 O O . GLY A 181 ? 0.2621 0.1843 0.3032 0.0467 -0.0086 0.0197 207 GLY A O 1458 N N . ARG A 182 ? 0.1814 0.1408 0.2261 0.0362 -0.0136 0.0136 208 ARG A N 1459 C CA . ARG A 182 ? 0.1974 0.1356 0.2208 0.0345 -0.0088 0.0031 208 ARG A CA 1460 C C . ARG A 182 ? 0.1735 0.1164 0.1825 0.0263 -0.0154 0.0012 208 ARG A C 1461 O O . ARG A 182 ? 0.2459 0.1853 0.2330 0.0283 -0.0146 -0.0059 208 ARG A O 1462 C CB . ARG A 182 ? 0.2608 0.1988 0.2816 0.0448 0.0055 0.0001 208 ARG A CB 1463 C CG . ARG A 182 ? 0.2914 0.2208 0.3253 0.0594 0.0147 0.0025 208 ARG A CG 1464 C CD . ARG A 182 ? 0.3868 0.3238 0.4268 0.0731 0.0319 0.0014 208 ARG A CD 1465 N NE . ARG A 182 ? 0.3930 0.3284 0.4524 0.0939 0.0406 0.0094 208 ARG A NE 1466 C CZ . ARG A 182 ? 0.4206 0.3508 0.4848 0.1123 0.0601 0.0074 208 ARG A CZ 1467 N NH1 . ARG A 182 ? 0.4737 0.3997 0.5211 0.1096 0.0731 -0.0044 208 ARG A NH1 1468 N NH2 . ARG A 182 ? 0.4562 0.3891 0.5349 0.1299 0.0645 0.0176 208 ARG A NH2 1469 N N . CYS A 183 ? 0.1667 0.1198 0.1852 0.0203 -0.0214 0.0078 209 CYS A N 1470 C CA . CYS A 183 ? 0.1861 0.1412 0.1933 0.0185 -0.0250 0.0095 209 CYS A CA 1471 C C . CYS A 183 ? 0.1475 0.1076 0.1652 0.0121 -0.0319 0.0117 209 CYS A C 1472 O O . CYS A 183 ? 0.1538 0.1180 0.1832 0.0086 -0.0327 0.0135 209 CYS A O 1473 C CB . CYS A 183 ? 0.1859 0.1385 0.1882 0.0223 -0.0122 0.0172 209 CYS A CB 1474 S SG . CYS A 183 ? 0.2242 0.1838 0.2549 0.0109 -0.0030 0.0167 209 CYS A SG 1475 N N . ILE A 184 ? 0.1690 0.1354 0.1810 0.0135 -0.0367 0.0120 210 ILE A N 1476 C CA . ILE A 184 ? 0.1831 0.1562 0.2051 0.0093 -0.0398 0.0138 210 ILE A CA 1477 C C . ILE A 184 ? 0.1706 0.1376 0.1918 0.0130 -0.0309 0.0198 210 ILE A C 1478 O O . ILE A 184 ? 0.1903 0.1505 0.2017 0.0232 -0.0233 0.0265 210 ILE A O 1479 C CB . ILE A 184 ? 0.1521 0.1449 0.1765 0.0099 -0.0479 0.0093 210 ILE A CB 1480 C CG1 . ILE A 184 ? 0.1627 0.1541 0.1926 -0.0021 -0.0517 -0.0038 210 ILE A CG1 1481 C CG2 . ILE A 184 ? 0.1583 0.1636 0.1957 0.0102 -0.0466 0.0136 210 ILE A CG2 1482 C CD1 . ILE A 184 ? 0.1539 0.1295 0.1964 -0.0118 -0.0450 -0.0010 210 ILE A CD1 1483 N N . GLN A 185 ? 0.1563 0.1222 0.1843 0.0060 -0.0287 0.0172 211 GLN A N 1484 C CA . GLN A 185 ? 0.1975 0.1515 0.2246 0.0059 -0.0167 0.0160 211 GLN A CA 1485 C C . GLN A 185 ? 0.1466 0.1042 0.1749 0.0111 -0.0142 0.0178 211 GLN A C 1486 O O . GLN A 185 ? 0.1811 0.1545 0.2143 0.0084 -0.0218 0.0179 211 GLN A O 1487 C CB . GLN A 185 ? 0.2887 0.2446 0.3209 -0.0073 -0.0142 0.0046 211 GLN A CB 1488 C CG . GLN A 185 ? 0.2892 0.2653 0.3203 -0.0106 -0.0258 0.0020 211 GLN A CG 1489 C CD . GLN A 185 ? 0.3247 0.3215 0.3618 -0.0194 -0.0295 -0.0092 211 GLN A CD 1490 O OE1 . GLN A 185 ? 0.3662 0.3791 0.4117 -0.0162 -0.0360 -0.0058 211 GLN A OE1 1491 N NE2 . GLN A 185 ? 0.2987 0.3001 0.3332 -0.0303 -0.0251 -0.0254 211 GLN A NE2 1492 N N . MET A 186 ? 0.1825 0.1216 0.2079 0.0191 0.0012 0.0201 212 MET A N 1493 C CA . MET A 186 ? 0.2098 0.1540 0.2389 0.0315 0.0074 0.0248 212 MET A CA 1494 C C . MET A 186 ? 0.2473 0.1861 0.2746 0.0223 0.0153 0.0126 212 MET A C 1495 O O . MET A 186 ? 0.2673 0.2128 0.2992 0.0322 0.0230 0.0152 212 MET A O 1496 C CB . MET A 186 ? 0.2514 0.1726 0.2751 0.0528 0.0254 0.0377 212 MET A CB 1497 C CG . MET A 186 ? 0.3141 0.2419 0.3289 0.0656 0.0193 0.0516 212 MET A CG 1498 S SD . MET A 186 ? 0.4871 0.3963 0.4859 0.0861 0.0405 0.0670 212 MET A SD 1499 C CE . MET A 186 ? 0.2487 0.1664 0.2596 0.0988 0.0473 0.0679 212 MET A CE 1500 N N . TRP A 187 ? 0.2143 0.1473 0.2345 0.0052 0.0140 -0.0019 213 TRP A N 1501 C CA . TRP A 187 ? 0.2114 0.1459 0.2210 -0.0037 0.0192 -0.0174 213 TRP A CA 1502 C C . TRP A 187 ? 0.2461 0.2009 0.2500 -0.0183 0.0049 -0.0282 213 TRP A C 1503 O O . TRP A 187 ? 0.2653 0.2246 0.2787 -0.0226 -0.0025 -0.0264 213 TRP A O 1504 C CB . TRP A 187 ? 0.2417 0.1410 0.2468 -0.0055 0.0433 -0.0321 213 TRP A CB 1505 C CG . TRP A 187 ? 0.2812 0.1761 0.2719 -0.0069 0.0559 -0.0481 213 TRP A CG 1506 C CD1 . TRP A 187 ? 0.3071 0.2022 0.2814 -0.0252 0.0591 -0.0772 213 TRP A CD1 1507 C CD2 . TRP A 187 ? 0.2584 0.1527 0.2495 0.0114 0.0684 -0.0386 213 TRP A CD2 1508 N NE1 . TRP A 187 ? 0.3668 0.2548 0.3247 -0.0190 0.0743 -0.0867 213 TRP A NE1 1509 C CE2 . TRP A 187 ? 0.3246 0.2111 0.2951 0.0042 0.0819 -0.0616 213 TRP A CE2 1510 C CE3 . TRP A 187 ? 0.2404 0.1491 0.2498 0.0328 0.0688 -0.0152 213 TRP A CE3 1511 C CZ2 . TRP A 187 ? 0.3306 0.2154 0.2975 0.0198 0.1002 -0.0592 213 TRP A CZ2 1512 C CZ3 . TRP A 187 ? 0.2562 0.1716 0.2696 0.0474 0.0845 -0.0128 213 TRP A CZ3 1513 C CH2 . TRP A 187 ? 0.3127 0.2127 0.3048 0.0418 0.1020 -0.0331 213 TRP A CH2 1514 N N . PHE A 188 ? 0.2706 0.2432 0.2577 -0.0222 0.0013 -0.0375 214 PHE A N 1515 C CA . PHE A 188 ? 0.2786 0.2838 0.2572 -0.0297 -0.0147 -0.0461 214 PHE A CA 1516 C C . PHE A 188 ? 0.2735 0.2970 0.2233 -0.0311 -0.0142 -0.0599 214 PHE A C 1517 O O . PHE A 188 ? 0.2768 0.2846 0.2143 -0.0253 -0.0002 -0.0583 214 PHE A O 1518 C CB . PHE A 188 ? 0.2389 0.2600 0.2214 -0.0188 -0.0288 -0.0226 214 PHE A CB 1519 C CG . PHE A 188 ? 0.2148 0.2288 0.1900 -0.0084 -0.0240 -0.0029 214 PHE A CG 1520 C CD1 . PHE A 188 ? 0.2396 0.2366 0.2329 -0.0061 -0.0181 0.0070 214 PHE A CD1 1521 C CD2 . PHE A 188 ? 0.2524 0.2812 0.2032 -0.0014 -0.0240 0.0052 214 PHE A CD2 1522 C CE1 . PHE A 188 ? 0.2432 0.2398 0.2395 -0.0030 -0.0113 0.0198 214 PHE A CE1 1523 C CE2 . PHE A 188 ? 0.2981 0.3163 0.2466 0.0045 -0.0126 0.0237 214 PHE A CE2 1524 C CZ . PHE A 188 ? 0.2900 0.2928 0.2658 0.0007 -0.0058 0.0287 214 PHE A CZ 1525 N N . ASP A 189 ? 0.3415 0.4050 0.2800 -0.0371 -0.0296 -0.0743 215 ASP A N 1526 C CA . ASP A 189 ? 0.3809 0.4738 0.2819 -0.0337 -0.0338 -0.0848 215 ASP A CA 1527 C C . ASP A 189 ? 0.3873 0.4961 0.2714 -0.0107 -0.0418 -0.0488 215 ASP A C 1528 O O . ASP A 189 ? 0.4411 0.5710 0.3356 -0.0016 -0.0562 -0.0330 215 ASP A O 1529 C CB . ASP A 189 ? 0.4388 0.5778 0.3373 -0.0488 -0.0487 -0.1171 215 ASP A CB 1530 C CG . ASP A 189 ? 0.5430 0.7091 0.4033 -0.0417 -0.0524 -0.1244 215 ASP A CG 1531 O OD1 . ASP A 189 ? 0.5555 0.7264 0.3821 -0.0209 -0.0517 -0.1000 215 ASP A OD1 1532 O OD2 . ASP A 189 ? 0.5884 0.7709 0.4524 -0.0572 -0.0539 -0.1537 215 ASP A OD2 1533 N N . PRO A 190 ? 0.4386 0.4165 0.2636 -0.0136 -0.0573 -0.1007 216 PRO A N 1534 C CA . PRO A 190 ? 0.4727 0.4380 0.2529 -0.0019 -0.0542 -0.0754 216 PRO A CA 1535 C C . PRO A 190 ? 0.5547 0.5309 0.2806 0.0100 -0.0758 -0.0739 216 PRO A C 1536 O O . PRO A 190 ? 0.5841 0.5538 0.2872 0.0226 -0.0803 -0.0486 216 PRO A O 1537 C CB . PRO A 190 ? 0.5117 0.4528 0.2723 -0.0063 -0.0249 -0.0768 216 PRO A CB 1538 C CG . PRO A 190 ? 0.4958 0.4416 0.2675 -0.0170 -0.0199 -0.1085 216 PRO A CG 1539 C CD . PRO A 190 ? 0.4659 0.4297 0.2938 -0.0226 -0.0356 -0.1189 216 PRO A CD 1540 N N . ALA A 191 ? 0.6102 0.6037 0.3251 0.0048 -0.0868 -0.0983 217 ALA A N 1541 C CA . ALA A 191 ? 0.6661 0.6745 0.3486 0.0112 -0.1046 -0.0919 217 ALA A CA 1542 C C . ALA A 191 ? 0.6746 0.7062 0.3935 0.0188 -0.1280 -0.0808 217 ALA A C 1543 O O . ALA A 191 ? 0.6989 0.7399 0.3957 0.0294 -0.1431 -0.0680 217 ALA A O 1544 C CB . ALA A 191 ? 0.7152 0.7327 0.3849 0.0012 -0.1104 -0.1216 217 ALA A CB 1545 N N . GLN A 192 ? 0.6468 0.6870 0.4231 0.0133 -0.1293 -0.0866 218 GLN A N 1546 C CA . GLN A 192 ? 0.6773 0.7395 0.4958 0.0178 -0.1454 -0.0798 218 GLN A CA 1547 C C . GLN A 192 ? 0.6719 0.7200 0.4991 0.0262 -0.1373 -0.0529 218 GLN A C 1548 O O . GLN A 192 ? 0.6900 0.7520 0.5514 0.0305 -0.1454 -0.0447 218 GLN A O 1549 C CB . GLN A 192 ? 0.7049 0.7849 0.5831 0.0039 -0.1475 -0.1046 218 GLN A CB 1550 C CG . GLN A 192 ? 0.7984 0.8842 0.6716 -0.0068 -0.1483 -0.1338 218 GLN A CG 1551 C CD . GLN A 192 ? 0.8137 0.9127 0.7507 -0.0209 -0.1450 -0.1567 218 GLN A CD 1552 O OE1 . GLN A 192 ? 0.7870 0.8773 0.7643 -0.0277 -0.1315 -0.1529 218 GLN A OE1 1553 N NE2 . GLN A 192 ? 0.8374 0.9560 0.7834 -0.0253 -0.1558 -0.1802 218 GLN A NE2 1554 N N . GLY A 193 ? 0.6084 0.6274 0.4055 0.0278 -0.1193 -0.0412 219 GLY A N 1555 C CA . GLY A 193 ? 0.5490 0.5491 0.3485 0.0351 -0.1090 -0.0158 219 GLY A CA 1556 C C . GLY A 193 ? 0.4355 0.4262 0.2764 0.0235 -0.0917 -0.0164 219 GLY A C 1557 O O . GLY A 193 ? 0.4213 0.4250 0.3014 0.0131 -0.0937 -0.0321 219 GLY A O 1558 N N . ASN A 194 ? 0.3950 0.3636 0.2310 0.0249 -0.0729 0.0010 220 ASN A N 1559 C CA . ASN A 194 ? 0.3325 0.2959 0.2078 0.0166 -0.0587 0.0029 220 ASN A CA 1560 C C . ASN A 194 ? 0.3303 0.3040 0.2360 0.0198 -0.0656 0.0122 220 ASN A C 1561 O O . ASN A 194 ? 0.3499 0.3157 0.2489 0.0276 -0.0627 0.0268 220 ASN A O 1562 C CB . ASN A 194 ? 0.3660 0.3068 0.2298 0.0155 -0.0363 0.0112 220 ASN A CB 1563 C CG . ASN A 194 ? 0.3001 0.2410 0.2039 0.0086 -0.0265 0.0089 220 ASN A CG 1564 O OD1 . ASN A 194 ? 0.3044 0.2567 0.2359 0.0076 -0.0347 0.0096 220 ASN A OD1 1565 N ND2 . ASN A 194 ? 0.2981 0.2272 0.2043 0.0047 -0.0087 0.0055 220 ASN A ND2 1566 N N . PRO A 195 ? 0.2688 0.2567 0.2090 0.0129 -0.0705 0.0033 221 PRO A N 1567 C CA . PRO A 195 ? 0.2422 0.2414 0.2111 0.0141 -0.0744 0.0085 221 PRO A CA 1568 C C . PRO A 195 ? 0.2575 0.2458 0.2352 0.0134 -0.0613 0.0188 221 PRO A C 1569 O O . PRO A 195 ? 0.2856 0.2798 0.2776 0.0162 -0.0615 0.0242 221 PRO A O 1570 C CB . PRO A 195 ? 0.2515 0.2626 0.2504 0.0042 -0.0765 -0.0051 221 PRO A CB 1571 C CG . PRO A 195 ? 0.2973 0.2960 0.2895 -0.0024 -0.0685 -0.0135 221 PRO A CG 1572 C CD . PRO A 195 ? 0.3088 0.2990 0.2633 0.0029 -0.0685 -0.0130 221 PRO A CD 1573 N N . ASN A 196 ? 0.1940 0.1694 0.1660 0.0100 -0.0505 0.0186 222 ASN A N 1574 C CA . ASN A 196 ? 0.1800 0.1508 0.1626 0.0098 -0.0420 0.0236 222 ASN A CA 1575 C C . ASN A 196 ? 0.1676 0.1306 0.1423 0.0147 -0.0357 0.0305 222 ASN A C 1576 O O . ASN A 196 ? 0.1834 0.1471 0.1708 0.0142 -0.0307 0.0308 222 ASN A O 1577 C CB . ASN A 196 ? 0.1626 0.1273 0.1514 0.0061 -0.0353 0.0185 222 ASN A CB 1578 C CG . ASN A 196 ? 0.1761 0.1430 0.1788 0.0027 -0.0383 0.0151 222 ASN A CG 1579 O OD1 . ASN A 196 ? 0.1707 0.1433 0.1818 0.0013 -0.0418 0.0177 222 ASN A OD1 1580 N ND2 . ASN A 196 ? 0.1801 0.1403 0.1888 0.0012 -0.0339 0.0090 222 ASN A ND2 1581 N N . GLU A 197 ? 0.2020 0.1558 0.1541 0.0198 -0.0352 0.0356 223 GLU A N 1582 C CA . GLU A 197 ? 0.1898 0.1293 0.1347 0.0255 -0.0257 0.0453 223 GLU A CA 1583 C C . GLU A 197 ? 0.2292 0.1767 0.1924 0.0306 -0.0309 0.0494 223 GLU A C 1584 O O . GLU A 197 ? 0.2285 0.1690 0.2051 0.0302 -0.0203 0.0500 223 GLU A O 1585 C CB . GLU A 197 ? 0.2783 0.2025 0.1865 0.0330 -0.0245 0.0547 223 GLU A CB 1586 C CG . GLU A 197 ? 0.3436 0.2561 0.2316 0.0269 -0.0121 0.0491 223 GLU A CG 1587 C CD . GLU A 197 ? 0.4828 0.3795 0.3225 0.0348 -0.0107 0.0585 223 GLU A CD 1588 O OE1 . GLU A 197 ? 0.5323 0.4286 0.3544 0.0474 -0.0235 0.0708 223 GLU A OE1 1589 O OE2 . GLU A 197 ? 0.4966 0.3818 0.3147 0.0297 0.0030 0.0534 223 GLU A OE2 1590 N N . GLU A 198 ? 0.2119 0.1752 0.1803 0.0345 -0.0457 0.0488 224 GLU A N 1591 C CA . GLU A 198 ? 0.2101 0.1844 0.2022 0.0389 -0.0492 0.0497 224 GLU A CA 1592 C C . GLU A 198 ? 0.1895 0.1704 0.2018 0.0302 -0.0409 0.0420 224 GLU A C 1593 O O . GLU A 198 ? 0.1607 0.1420 0.1878 0.0318 -0.0343 0.0410 224 GLU A O 1594 C CB . GLU A 198 ? 0.3038 0.2991 0.3058 0.0426 -0.0661 0.0457 224 GLU A CB 1595 C CG . GLU A 198 ? 0.4620 0.4728 0.4968 0.0454 -0.0675 0.0429 224 GLU A CG 1596 C CD . GLU A 198 ? 0.6492 0.6810 0.6965 0.0538 -0.0835 0.0396 224 GLU A CD 1597 O OE1 . GLU A 198 ? 0.7247 0.7543 0.7478 0.0622 -0.0902 0.0460 224 GLU A OE1 1598 O OE2 . GLU A 198 ? 0.6969 0.7496 0.7796 0.0506 -0.0866 0.0300 224 GLU A OE2 1599 N N . VAL A 199 ? 0.1760 0.1608 0.1866 0.0220 -0.0413 0.0364 225 VAL A N 1600 C CA . VAL A 199 ? 0.1227 0.1125 0.1422 0.0164 -0.0361 0.0320 225 VAL A CA 1601 C C . VAL A 199 ? 0.1532 0.1365 0.1722 0.0160 -0.0281 0.0287 225 VAL A C 1602 O O . VAL A 199 ? 0.1628 0.1513 0.1888 0.0151 -0.0239 0.0238 225 VAL A O 1603 C CB . VAL A 199 ? 0.1347 0.1252 0.1512 0.0110 -0.0385 0.0305 225 VAL A CB 1604 C CG1 . VAL A 199 ? 0.1629 0.1552 0.1792 0.0088 -0.0342 0.0306 225 VAL A CG1 1605 C CG2 . VAL A 199 ? 0.1553 0.1534 0.1806 0.0088 -0.0441 0.0287 225 VAL A CG2 1606 N N . ALA A 200 ? 0.1378 0.1107 0.1508 0.0156 -0.0245 0.0284 226 ALA A N 1607 C CA . ALA A 200 ? 0.1387 0.1077 0.1612 0.0133 -0.0154 0.0209 226 ALA A CA 1608 C C . ALA A 200 ? 0.1707 0.1335 0.2029 0.0162 -0.0072 0.0211 226 ALA A C 1609 O O . ALA A 200 ? 0.1888 0.1562 0.2350 0.0131 -0.0017 0.0097 226 ALA A O 1610 C CB . ALA A 200 ? 0.1535 0.1110 0.1736 0.0111 -0.0075 0.0198 226 ALA A CB 1611 N N . ARG A 201 ? 0.1744 0.1273 0.2003 0.0233 -0.0074 0.0328 227 ARG A N 1612 C CA . ARG A 201 ? 0.2151 0.1585 0.2539 0.0290 0.0009 0.0355 227 ARG A CA 1613 C C . ARG A 201 ? 0.1864 0.1462 0.2423 0.0277 -0.0005 0.0260 227 ARG A C 1614 O O . ARG A 201 ? 0.2035 0.1596 0.2765 0.0265 0.0105 0.0168 227 ARG A O 1615 C CB . ARG A 201 ? 0.2588 0.1919 0.2861 0.0414 -0.0047 0.0521 227 ARG A CB 1616 C CG . ARG A 201 ? 0.2739 0.1808 0.2791 0.0454 0.0046 0.0645 227 ARG A CG 1617 C CD . ARG A 201 ? 0.2713 0.1696 0.2614 0.0596 -0.0036 0.0797 227 ARG A CD 1618 N NE . ARG A 201 ? 0.3242 0.2420 0.3001 0.0639 -0.0260 0.0808 227 ARG A NE 1619 C CZ . ARG A 201 ? 0.3280 0.2451 0.2744 0.0624 -0.0315 0.0840 227 ARG A CZ 1620 N NH1 . ARG A 201 ? 0.3435 0.2389 0.2679 0.0582 -0.0151 0.0878 227 ARG A NH1 1621 N NH2 . ARG A 201 ? 0.4114 0.3515 0.3537 0.0646 -0.0505 0.0808 227 ARG A NH2 1622 N N . PHE A 202 ? 0.1517 0.1278 0.2041 0.0268 -0.0107 0.0265 228 PHE A N 1623 C CA . PHE A 202 ? 0.1933 0.1829 0.2584 0.0249 -0.0075 0.0184 228 PHE A CA 1624 C C . PHE A 202 ? 0.2138 0.2071 0.2748 0.0177 -0.0010 0.0047 228 PHE A C 1625 O O . PHE A 202 ? 0.2286 0.2244 0.3013 0.0169 0.0084 -0.0065 228 PHE A O 1626 C CB . PHE A 202 ? 0.1910 0.1941 0.2544 0.0228 -0.0148 0.0212 228 PHE A CB 1627 C CG . PHE A 202 ? 0.2243 0.2388 0.2982 0.0192 -0.0061 0.0138 228 PHE A CG 1628 C CD1 . PHE A 202 ? 0.2432 0.2596 0.2991 0.0127 -0.0005 0.0088 228 PHE A CD1 1629 C CD2 . PHE A 202 ? 0.2615 0.2852 0.3622 0.0236 -0.0031 0.0119 228 PHE A CD2 1630 C CE1 . PHE A 202 ? 0.3103 0.3340 0.3675 0.0091 0.0115 0.0029 228 PHE A CE1 1631 C CE2 . PHE A 202 ? 0.3096 0.3433 0.4218 0.0189 0.0099 0.0033 228 PHE A CE2 1632 C CZ . PHE A 202 ? 0.3259 0.3577 0.4127 0.0109 0.0190 -0.0007 228 PHE A CZ 1633 N N . TYR A 203 ? 0.1537 0.1492 0.1995 0.0137 -0.0071 0.0035 229 TYR A N 1634 C CA . TYR A 203 ? 0.1671 0.1718 0.2066 0.0098 -0.0071 -0.0101 229 TYR A CA 1635 C C . TYR A 203 ? 0.2072 0.2093 0.2638 0.0071 -0.0005 -0.0254 229 TYR A C 1636 O O . TYR A 203 ? 0.2659 0.2788 0.3243 0.0040 0.0009 -0.0430 229 TYR A O 1637 C CB . TYR A 203 ? 0.1415 0.1516 0.1626 0.0098 -0.0183 -0.0053 229 TYR A CB 1638 C CG . TYR A 203 ? 0.1609 0.1719 0.1677 0.0102 -0.0186 0.0055 229 TYR A CG 1639 C CD1 . TYR A 203 ? 0.1863 0.2031 0.1790 0.0093 -0.0129 0.0019 229 TYR A CD1 1640 C CD2 . TYR A 203 ? 0.1612 0.1664 0.1699 0.0102 -0.0216 0.0172 229 TYR A CD2 1641 C CE1 . TYR A 203 ? 0.2089 0.2229 0.1913 0.0079 -0.0070 0.0121 229 TYR A CE1 1642 C CE2 . TYR A 203 ? 0.1961 0.2011 0.2004 0.0082 -0.0180 0.0244 229 TYR A CE2 1643 C CZ . TYR A 203 ? 0.2150 0.2229 0.2071 0.0068 -0.0091 0.0231 229 TYR A CZ 1644 O OH . TYR A 203 ? 0.2352 0.2394 0.2250 0.0032 0.0001 0.0307 229 TYR A OH 1645 N N . ALA A 204 ? 0.2035 0.1904 0.2721 0.0076 0.0054 -0.0200 230 ALA A N 1646 C CA . ALA A 204 ? 0.2149 0.1939 0.3072 0.0032 0.0183 -0.0343 230 ALA A CA 1647 C C . ALA A 204 ? 0.2633 0.2384 0.3719 0.0037 0.0298 -0.0434 230 ALA A C 1648 O O . ALA A 204 ? 0.2932 0.2706 0.4226 -0.0024 0.0389 -0.0649 230 ALA A O 1649 C CB . ALA A 204 ? 0.1931 0.1492 0.2902 0.0041 0.0286 -0.0224 230 ALA A CB 1650 N N . ALA A 205 ? 0.2455 0.2165 0.3503 0.0108 0.0297 -0.0300 231 ALA A N 1651 C CA . ALA A 205 ? 0.3063 0.2733 0.4322 0.0130 0.0419 -0.0384 231 ALA A CA 1652 C C . ALA A 205 ? 0.3769 0.3650 0.4965 0.0076 0.0417 -0.0583 231 ALA A C 1653 O O . ALA A 205 ? 0.4365 0.4244 0.5748 0.0058 0.0546 -0.0754 231 ALA A O 1654 C CB . ALA A 205 ? 0.3003 0.2597 0.4308 0.0245 0.0402 -0.0189 231 ALA A CB 1655 N N . ALA A 206 ? 0.3789 0.3827 0.4699 0.0055 0.0288 -0.0555 232 ALA A N 1656 C CA . ALA A 206 ? 0.4049 0.4254 0.4763 0.0021 0.0288 -0.0694 232 ALA A CA 1657 C C . ALA A 206 ? 0.4475 0.4823 0.5042 -0.0022 0.0193 -0.0880 232 ALA A C 1658 O O . ALA A 206 ? 0.5288 0.5768 0.5714 -0.0049 0.0211 -0.1074 232 ALA A O 1659 C CB . ALA A 206 ? 0.3874 0.4124 0.4353 0.0043 0.0238 -0.0522 232 ALA A CB 1660 N N . MET A 207 ? 0.3966 0.4312 0.4572 -0.0022 0.0087 -0.0841 233 MET A N 1661 C CA . MET A 207 ? 0.4278 0.4815 0.4816 -0.0039 -0.0048 -0.1022 233 MET A CA 1662 C C . MET A 207 ? 0.4570 0.5127 0.5500 -0.0109 0.0016 -0.1265 233 MET A C 1663 O O . MET A 207 ? 0.4361 0.4854 0.5497 -0.0124 0.0020 -0.1221 233 MET A O 1664 C CB . MET A 207 ? 0.4209 0.4776 0.4586 0.0013 -0.0212 -0.0850 233 MET A CB 1665 C CG . MET A 207 ? 0.4426 0.4974 0.4427 0.0071 -0.0269 -0.0646 233 MET A CG 1666 S SD . MET A 207 ? 0.4265 0.4772 0.4198 0.0131 -0.0412 -0.0442 233 MET A SD 1667 C CE . MET A 207 ? 0.2232 0.2988 0.2185 0.0179 -0.0615 -0.0644 233 MET A CE # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'CHIRAL CENTER C1 ATOM OF NAG A 304 HAS SP2 HYBRIDIZATION' # 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 27 ? ? ? A . n A 1 2 SER 2 28 ? ? ? A . n A 1 3 SER 3 29 ? ? ? A . n A 1 4 ARG 4 30 30 ARG ARG A . n A 1 5 THR 5 31 31 THR THR A . n A 1 6 GLU 6 32 32 GLU GLU A . n A 1 7 LEU 7 33 33 LEU LEU A . n A 1 8 LEU 8 34 34 LEU LEU A . n A 1 9 ASN 9 35 35 ASN ASN A . n A 1 10 VAL 10 36 36 VAL VAL A . n A 1 11 CYS 11 37 37 CYS CYS A . n A 1 12 MET 12 38 38 MET MET A . n A 1 13 ASN 13 39 39 ASN ASN A . n A 1 14 ALA 14 40 40 ALA ALA A . n A 1 15 LYS 15 41 41 LYS LYS A . n A 1 16 HIS 16 42 42 HIS HIS A . n A 1 17 HIS 17 43 43 HIS HIS A . n A 1 18 LYS 18 44 44 LYS LYS A . n A 1 19 GLU 19 45 45 GLU GLU A . n A 1 20 LYS 20 46 46 LYS LYS A . n A 1 21 PRO 21 47 47 PRO PRO A . n A 1 22 GLY 22 48 48 GLY GLY A . n A 1 23 PRO 23 49 49 PRO PRO A . n A 1 24 GLU 24 50 50 GLU GLU A . n A 1 25 ASP 25 51 51 ASP ASP A . n A 1 26 LYS 26 52 52 LYS LYS A . n A 1 27 LEU 27 53 53 LEU LEU A . n A 1 28 HIS 28 54 54 HIS HIS A . n A 1 29 GLU 29 55 55 GLU GLU A . n A 1 30 GLN 30 56 56 GLN GLN A . n A 1 31 CYS 31 57 57 CYS CYS A . n A 1 32 ARG 32 58 58 ARG ARG A . n A 1 33 PRO 33 59 59 PRO PRO A . n A 1 34 TRP 34 60 60 TRP TRP A . n A 1 35 ARG 35 61 61 ARG ARG A . n A 1 36 LYS 36 62 62 LYS LYS A . n A 1 37 ASN 37 63 63 ASN ASN A . n A 1 38 ALA 38 64 64 ALA ALA A . n A 1 39 CYS 39 65 65 CYS CYS A . n A 1 40 CYS 40 66 66 CYS CYS A . n A 1 41 SER 41 67 67 SER SER A . n A 1 42 THR 42 68 68 THR THR A . n A 1 43 ASN 43 69 69 ASN ASN A . n A 1 44 THR 44 70 70 THR THR A . n A 1 45 SER 45 71 71 SER SER A . n A 1 46 GLN 46 72 72 GLN GLN A . n A 1 47 GLU 47 73 73 GLU GLU A . n A 1 48 ALA 48 74 74 ALA ALA A . n A 1 49 HIS 49 75 75 HIS HIS A . n A 1 50 LYS 50 76 76 LYS LYS A . n A 1 51 ASP 51 77 77 ASP ASP A . n A 1 52 VAL 52 78 78 VAL VAL A . n A 1 53 SER 53 79 79 SER SER A . n A 1 54 TYR 54 80 80 TYR TYR A . n A 1 55 LEU 55 81 81 LEU LEU A . n A 1 56 TYR 56 82 82 TYR TYR A . n A 1 57 ARG 57 83 83 ARG ARG A . n A 1 58 PHE 58 84 84 PHE PHE A . n A 1 59 ASN 59 85 85 ASN ASN A . n A 1 60 TRP 60 86 86 TRP TRP A . n A 1 61 ASN 61 87 87 ASN ASN A . n A 1 62 HIS 62 88 88 HIS HIS A . n A 1 63 CYS 63 89 89 CYS CYS A . n A 1 64 GLY 64 90 90 GLY GLY A . n A 1 65 GLU 65 91 91 GLU GLU A . n A 1 66 MET 66 92 92 MET MET A . n A 1 67 ALA 67 93 93 ALA ALA A . n A 1 68 PRO 68 94 94 PRO PRO A . n A 1 69 ALA 69 95 95 ALA ALA A . n A 1 70 CYS 70 96 96 CYS CYS A . n A 1 71 LYS 71 97 97 LYS LYS A . n A 1 72 ARG 72 98 98 ARG ARG A . n A 1 73 HIS 73 99 99 HIS HIS A . n A 1 74 PHE 74 100 100 PHE PHE A . n A 1 75 ILE 75 101 101 ILE ILE A . n A 1 76 GLN 76 102 102 GLN GLN A . n A 1 77 ASP 77 103 103 ASP ASP A . n A 1 78 THR 78 104 104 THR THR A . n A 1 79 CYS 79 105 105 CYS CYS A . n A 1 80 LEU 80 106 106 LEU LEU A . n A 1 81 TYR 81 107 107 TYR TYR A . n A 1 82 GLU 82 108 108 GLU GLU A . n A 1 83 CYS 83 109 109 CYS CYS A . n A 1 84 SER 84 110 110 SER SER A . n A 1 85 PRO 85 111 111 PRO PRO A . n A 1 86 ASN 86 112 112 ASN ASN A . n A 1 87 LEU 87 113 113 LEU LEU A . n A 1 88 GLY 88 114 114 GLY GLY A . n A 1 89 PRO 89 115 115 PRO PRO A . n A 1 90 TRP 90 116 116 TRP TRP A . n A 1 91 ILE 91 117 117 ILE ILE A . n A 1 92 GLN 92 118 118 GLN GLN A . n A 1 93 GLN 93 119 119 GLN GLN A . n A 1 94 VAL 94 120 120 VAL VAL A . n A 1 95 ASP 95 121 121 ASP ASP A . n A 1 96 GLN 96 122 122 GLN GLN A . n A 1 97 SER 97 123 123 SER SER A . n A 1 98 TRP 98 124 124 TRP TRP A . n A 1 99 ARG 99 125 125 ARG ARG A . n A 1 100 LYS 100 126 126 LYS LYS A . n A 1 101 GLU 101 127 127 GLU GLU A . n A 1 102 ARG 102 128 128 ARG ARG A . n A 1 103 VAL 103 129 129 VAL VAL A . n A 1 104 LEU 104 130 130 LEU LEU A . n A 1 105 ASN 105 131 131 ASN ASN A . n A 1 106 VAL 106 132 132 VAL VAL A . n A 1 107 PRO 107 133 133 PRO PRO A . n A 1 108 LEU 108 134 134 LEU LEU A . n A 1 109 CYS 109 135 135 CYS CYS A . n A 1 110 LYS 110 136 136 LYS LYS A . n A 1 111 GLU 111 137 137 GLU GLU A . n A 1 112 ASP 112 138 138 ASP ASP A . n A 1 113 CYS 113 139 139 CYS CYS A . n A 1 114 GLU 114 140 140 GLU GLU A . n A 1 115 GLN 115 141 141 GLN GLN A . n A 1 116 TRP 116 142 142 TRP TRP A . n A 1 117 TRP 117 143 143 TRP TRP A . n A 1 118 GLU 118 144 144 GLU GLU A . n A 1 119 ASP 119 145 145 ASP ASP A . n A 1 120 CYS 120 146 146 CYS CYS A . n A 1 121 ARG 121 147 147 ARG ARG A . n A 1 122 THR 122 148 148 THR THR A . n A 1 123 SER 123 149 149 SER SER A . n A 1 124 TYR 124 150 150 TYR TYR A . n A 1 125 THR 125 151 151 THR THR A . n A 1 126 CYS 126 152 152 CYS CYS A . n A 1 127 LYS 127 153 153 LYS LYS A . n A 1 128 SER 128 154 154 SER SER A . n A 1 129 ASN 129 155 155 ASN ASN A . n A 1 130 TRP 130 156 156 TRP TRP A . n A 1 131 HIS 131 157 157 HIS HIS A . n A 1 132 LYS 132 158 158 LYS LYS A . n A 1 133 GLY 133 159 159 GLY GLY A . n A 1 134 TRP 134 160 160 TRP TRP A . n A 1 135 ASN 135 161 161 ASN ASN A . n A 1 136 TRP 136 162 162 TRP TRP A . n A 1 137 THR 137 163 163 THR THR A . n A 1 138 SER 138 164 164 SER SER A . n A 1 139 GLY 139 165 165 GLY GLY A . n A 1 140 PHE 140 166 166 PHE PHE A . n A 1 141 ASN 141 167 167 ASN ASN A . n A 1 142 LYS 142 168 168 LYS LYS A . n A 1 143 CYS 143 169 169 CYS CYS A . n A 1 144 ALA 144 170 170 ALA ALA A . n A 1 145 VAL 145 171 171 VAL VAL A . n A 1 146 GLY 146 172 172 GLY GLY A . n A 1 147 ALA 147 173 173 ALA ALA A . n A 1 148 ALA 148 174 174 ALA ALA A . n A 1 149 CYS 149 175 175 CYS CYS A . n A 1 150 GLN 150 176 176 GLN GLN A . n A 1 151 PRO 151 177 177 PRO PRO A . n A 1 152 PHE 152 178 178 PHE PHE A . n A 1 153 HIS 153 179 179 HIS HIS A . n A 1 154 PHE 154 180 180 PHE PHE A . n A 1 155 TYR 155 181 181 TYR TYR A . n A 1 156 PHE 156 182 182 PHE PHE A . n A 1 157 PRO 157 183 183 PRO PRO A . n A 1 158 THR 158 184 184 THR THR A . n A 1 159 PRO 159 185 185 PRO PRO A . n A 1 160 THR 160 186 186 THR THR A . n A 1 161 VAL 161 187 187 VAL VAL A . n A 1 162 LEU 162 188 188 LEU LEU A . n A 1 163 CYS 163 189 189 CYS CYS A . n A 1 164 ASN 164 190 190 ASN ASN A . n A 1 165 GLU 165 191 191 GLU GLU A . n A 1 166 ILE 166 192 192 ILE ILE A . n A 1 167 TRP 167 193 193 TRP TRP A . n A 1 168 THR 168 194 194 THR THR A . n A 1 169 HIS 169 195 195 HIS HIS A . n A 1 170 SER 170 196 196 SER SER A . n A 1 171 TYR 171 197 197 TYR TYR A . n A 1 172 LYS 172 198 198 LYS LYS A . n A 1 173 VAL 173 199 199 VAL VAL A . n A 1 174 SER 174 200 200 SER SER A . n A 1 175 ASN 175 201 201 ASN ASN A . n A 1 176 TYR 176 202 202 TYR TYR A . n A 1 177 SER 177 203 203 SER SER A . n A 1 178 ARG 178 204 204 ARG ARG A . n A 1 179 GLY 179 205 205 GLY GLY A . n A 1 180 SER 180 206 206 SER SER A . n A 1 181 GLY 181 207 207 GLY GLY A . n A 1 182 ARG 182 208 208 ARG ARG A . n A 1 183 CYS 183 209 209 CYS CYS A . n A 1 184 ILE 184 210 210 ILE ILE A . n A 1 185 GLN 185 211 211 GLN GLN A . n A 1 186 MET 186 212 212 MET MET A . n A 1 187 TRP 187 213 213 TRP TRP A . n A 1 188 PHE 188 214 214 PHE PHE A . n A 1 189 ASP 189 215 215 ASP ASP A . n A 1 190 PRO 190 216 216 PRO PRO A . n A 1 191 ALA 191 217 217 ALA ALA A . n A 1 192 GLN 192 218 218 GLN GLN A . n A 1 193 GLY 193 219 219 GLY GLY A . n A 1 194 ASN 194 220 220 ASN ASN A . n A 1 195 PRO 195 221 221 PRO PRO A . n A 1 196 ASN 196 222 222 ASN ASN A . n A 1 197 GLU 197 223 223 GLU GLU A . n A 1 198 GLU 198 224 224 GLU GLU A . n A 1 199 VAL 199 225 225 VAL VAL A . n A 1 200 ALA 200 226 226 ALA ALA A . n A 1 201 ARG 201 227 227 ARG ARG A . n A 1 202 PHE 202 228 228 PHE PHE A . n A 1 203 TYR 203 229 229 TYR TYR A . n A 1 204 ALA 204 230 230 ALA ALA A . n A 1 205 ALA 205 231 231 ALA ALA A . n A 1 206 ALA 206 232 232 ALA ALA A . n A 1 207 MET 207 233 233 MET MET A . n A 1 208 SER 208 234 ? ? ? A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 CA 1 301 301 CA CA A . C 3 NAG 1 302 302 NAG NAG A . D 3 NAG 1 303 303 NAG NAG A . E 3 NAG 1 304 304 NAG NAG A . F 4 HOH 1 401 401 HOH HOH A . F 4 HOH 2 402 402 HOH HOH A . F 4 HOH 3 403 403 HOH HOH A . F 4 HOH 4 404 404 HOH HOH A . F 4 HOH 5 405 405 HOH HOH A . F 4 HOH 6 406 406 HOH HOH A . F 4 HOH 7 407 407 HOH HOH A . F 4 HOH 8 408 408 HOH HOH A . F 4 HOH 9 409 409 HOH HOH A . F 4 HOH 10 410 410 HOH HOH A . F 4 HOH 11 411 411 HOH HOH A . F 4 HOH 12 412 412 HOH HOH A . F 4 HOH 13 413 413 HOH HOH A . F 4 HOH 14 414 414 HOH HOH A . F 4 HOH 15 415 415 HOH HOH A . F 4 HOH 16 416 416 HOH HOH A . F 4 HOH 17 417 417 HOH HOH A . F 4 HOH 18 418 418 HOH HOH A . F 4 HOH 19 419 419 HOH HOH A . F 4 HOH 20 420 420 HOH HOH A . F 4 HOH 21 421 421 HOH HOH A . F 4 HOH 22 422 422 HOH HOH A . F 4 HOH 23 423 423 HOH HOH A . F 4 HOH 24 424 424 HOH HOH A . F 4 HOH 25 425 425 HOH HOH A . F 4 HOH 26 426 426 HOH HOH A . F 4 HOH 27 427 427 HOH HOH A . F 4 HOH 28 428 428 HOH HOH A . F 4 HOH 29 429 429 HOH HOH A . F 4 HOH 30 430 430 HOH HOH A . F 4 HOH 31 431 431 HOH HOH A . F 4 HOH 32 432 432 HOH HOH A . F 4 HOH 33 433 433 HOH HOH A . F 4 HOH 34 434 434 HOH HOH A . F 4 HOH 35 435 435 HOH HOH A . F 4 HOH 36 436 436 HOH HOH A . F 4 HOH 37 437 437 HOH HOH A . F 4 HOH 38 438 438 HOH HOH A . F 4 HOH 39 439 439 HOH HOH A . F 4 HOH 40 440 440 HOH HOH A . F 4 HOH 41 441 441 HOH HOH A . F 4 HOH 42 442 442 HOH HOH A . F 4 HOH 43 443 443 HOH HOH A . F 4 HOH 44 444 444 HOH HOH A . F 4 HOH 45 445 445 HOH HOH A . F 4 HOH 46 446 446 HOH HOH A . F 4 HOH 47 447 447 HOH HOH A . F 4 HOH 48 448 448 HOH HOH A . F 4 HOH 49 449 449 HOH HOH A . F 4 HOH 50 450 450 HOH HOH A . F 4 HOH 51 451 451 HOH HOH A . F 4 HOH 52 452 452 HOH HOH A . F 4 HOH 53 453 453 HOH HOH A . F 4 HOH 54 454 454 HOH HOH A . F 4 HOH 55 455 455 HOH HOH A . F 4 HOH 56 456 456 HOH HOH A . F 4 HOH 57 457 457 HOH HOH A . F 4 HOH 58 458 458 HOH HOH A . F 4 HOH 59 459 459 HOH HOH A . F 4 HOH 60 460 460 HOH HOH A . F 4 HOH 61 461 461 HOH HOH A . F 4 HOH 62 462 462 HOH HOH A . F 4 HOH 63 463 463 HOH HOH A . F 4 HOH 64 464 464 HOH HOH A . F 4 HOH 65 465 465 HOH HOH A . F 4 HOH 66 466 466 HOH HOH A . F 4 HOH 67 467 467 HOH HOH A . F 4 HOH 68 468 468 HOH HOH A . F 4 HOH 69 469 469 HOH HOH A . F 4 HOH 70 470 470 HOH HOH A . F 4 HOH 71 471 471 HOH HOH A . F 4 HOH 72 472 472 HOH HOH A . F 4 HOH 73 473 473 HOH HOH A . F 4 HOH 74 474 474 HOH HOH A . F 4 HOH 75 475 475 HOH HOH A . F 4 HOH 76 476 476 HOH HOH A . F 4 HOH 77 477 477 HOH HOH A . F 4 HOH 78 478 478 HOH HOH A . F 4 HOH 79 479 479 HOH HOH A . F 4 HOH 80 480 480 HOH HOH A . F 4 HOH 81 481 481 HOH HOH A . F 4 HOH 82 482 482 HOH HOH A . F 4 HOH 83 483 483 HOH HOH A . F 4 HOH 84 484 484 HOH HOH A . F 4 HOH 85 485 485 HOH HOH A . F 4 HOH 86 486 486 HOH HOH A . F 4 HOH 87 487 487 HOH HOH A . F 4 HOH 88 488 488 HOH HOH A . F 4 HOH 89 489 489 HOH HOH A . F 4 HOH 90 490 490 HOH HOH A . F 4 HOH 91 491 491 HOH HOH A . F 4 HOH 92 492 492 HOH HOH A . F 4 HOH 93 493 493 HOH HOH A . F 4 HOH 94 494 494 HOH HOH A . F 4 HOH 95 495 495 HOH HOH A . F 4 HOH 96 496 496 HOH HOH A . F 4 HOH 97 497 497 HOH HOH A . F 4 HOH 98 498 498 HOH HOH A . F 4 HOH 99 499 499 HOH HOH A . F 4 HOH 100 500 500 HOH HOH A . F 4 HOH 101 501 501 HOH HOH A . F 4 HOH 102 502 502 HOH HOH A . F 4 HOH 103 503 503 HOH HOH A . F 4 HOH 104 504 504 HOH HOH A . F 4 HOH 105 505 505 HOH HOH A . F 4 HOH 106 506 506 HOH HOH A . F 4 HOH 107 507 507 HOH HOH A . F 4 HOH 108 508 508 HOH HOH A . F 4 HOH 109 509 509 HOH HOH A . F 4 HOH 110 510 510 HOH HOH A . F 4 HOH 111 511 511 HOH HOH A . F 4 HOH 112 512 512 HOH HOH A . F 4 HOH 113 513 513 HOH HOH A . F 4 HOH 114 514 514 HOH HOH A . F 4 HOH 115 515 515 HOH HOH A . F 4 HOH 116 516 516 HOH HOH A . F 4 HOH 117 517 517 HOH HOH A . F 4 HOH 118 518 518 HOH HOH A . F 4 HOH 119 519 519 HOH HOH A . F 4 HOH 120 520 520 HOH HOH A . F 4 HOH 121 521 521 HOH HOH A . F 4 HOH 122 522 522 HOH HOH A . F 4 HOH 123 523 523 HOH HOH A . F 4 HOH 124 524 524 HOH HOH A . F 4 HOH 125 525 525 HOH HOH A . F 4 HOH 126 526 526 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 43 A ASN 69 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 135 A ASN 161 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 175 A ASN 201 ? 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 # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-08-07 2 'Structure model' 1 1 2013-10-02 3 'Structure model' 1 2 2017-11-15 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 3 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 3 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_software.name' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 5.4378 43.7735 37.0965 0.1458 0.0743 0.1931 -0.0159 -0.0191 -0.0010 4.2526 1.3321 4.0583 0.2310 0.0659 -2.0769 0.0462 -0.0463 0.3784 0.0959 -0.0528 -0.3302 -0.2516 0.2435 -0.0169 'X-RAY DIFFRACTION' 2 ? refined 2.6071 29.0825 27.1378 0.2096 0.1582 0.1505 -0.0024 0.0171 -0.0582 5.0839 4.4320 6.1364 -0.6046 0.5004 -1.4257 -0.0708 0.7537 -0.5805 -0.7794 0.0103 -0.1542 0.2621 0.1605 -0.0178 'X-RAY DIFFRACTION' 3 ? refined 9.4595 35.3347 29.0966 0.2679 0.2760 0.2582 -0.0308 0.0535 0.0353 2.4274 3.9970 2.9510 0.6280 -1.5517 -0.8922 0.0363 0.5860 0.3545 -0.5272 -0.2862 -0.7431 -0.2565 0.6509 0.1669 'X-RAY DIFFRACTION' 4 ? refined 6.7099 16.4358 39.3262 0.0236 0.0439 0.0663 0.0180 -0.0062 -0.0165 2.7947 1.5177 3.4917 -0.7635 -0.6483 -1.0238 -0.0107 0.0004 -0.1933 -0.1078 0.0065 0.0528 0.2069 -0.0569 0.0386 'X-RAY DIFFRACTION' 5 ? refined -1.5313 29.4372 42.2035 0.0756 0.1045 0.0703 0.0053 -0.0234 0.0072 0.8064 3.6215 0.7382 0.2717 -0.7456 0.0447 0.0092 -0.0101 -0.0042 -0.0630 0.0372 -0.0397 0.0160 0.0100 -0.0480 'X-RAY DIFFRACTION' 6 ? refined 8.0913 17.7292 47.3710 0.0986 0.0735 0.0914 0.0126 -0.0248 0.0229 6.8029 1.6450 1.7812 0.7488 -0.8592 -0.1212 -0.0375 -0.1349 0.2154 0.0999 0.0302 -0.0044 -0.0884 0.0991 0.0149 'X-RAY DIFFRACTION' 7 ? refined -0.4160 20.7701 50.8518 0.1071 0.1260 0.0763 0.0009 -0.0294 0.0160 1.0580 2.3163 0.9761 0.0187 -0.9804 -0.0719 -0.0017 -0.0636 -0.0312 0.0822 -0.0646 -0.0563 0.0042 0.0435 0.0506 'X-RAY DIFFRACTION' 8 ? refined -12.4018 32.2017 38.0680 0.1075 0.0870 0.1513 -0.0084 -0.0254 0.0051 6.8788 4.6263 6.8683 -1.4664 -3.9244 0.6796 -0.2293 0.2524 -0.2374 0.0461 0.0021 0.2534 0.2027 -0.2988 0.2115 'X-RAY DIFFRACTION' 9 ? refined -10.6354 40.4649 37.1838 0.1402 0.1132 0.1344 0.0223 -0.0388 0.0381 4.7990 5.1404 2.4517 -0.5655 -1.6572 1.7862 0.1382 0.2253 0.1677 -0.3784 -0.0312 0.1480 -0.1681 -0.2328 0.0192 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 30:49) ; 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 50:60) ; 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 61:80) ; 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 81:93) ; 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 94:146) ; 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 147:166) ; 'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 167:201) ; 'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 202:215) ; 'X-RAY DIFFRACTION' 9 9 ? ? ? ? ? ? ? ? ? ;chain 'A' and (resseq 216:233) ; # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 SCALEPACK . ? program 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data scaling' http://www.hkl-xray.com/ ? ? 2 PHENIX 1.7.3_928 ? 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 THR A 31 ? ? -119.21 -90.56 2 1 CYS A 66 ? ? -101.61 70.53 3 1 ASN A 87 ? ? -96.89 35.17 4 1 LYS A 126 ? ? -131.69 -123.02 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id A _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 304 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details PLANAR _pdbx_validate_chiral.omega . # 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 GLU 73 ? CG ? A GLU 47 CG 2 1 Y 1 A GLU 73 ? CD ? A GLU 47 CD 3 1 Y 1 A GLU 73 ? OE1 ? A GLU 47 OE1 4 1 Y 1 A GLU 73 ? OE2 ? A GLU 47 OE2 5 1 Y 1 A HIS 75 ? CG ? A HIS 49 CG 6 1 Y 1 A HIS 75 ? ND1 ? A HIS 49 ND1 7 1 Y 1 A HIS 75 ? CD2 ? A HIS 49 CD2 8 1 Y 1 A HIS 75 ? CE1 ? A HIS 49 CE1 9 1 Y 1 A HIS 75 ? NE2 ? A HIS 49 NE2 10 1 Y 1 A LYS 76 ? CG ? A LYS 50 CG 11 1 Y 1 A LYS 76 ? CD ? A LYS 50 CD 12 1 Y 1 A LYS 76 ? CE ? A LYS 50 CE 13 1 Y 1 A LYS 76 ? NZ ? A LYS 50 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 27 ? A GLY 1 2 1 Y 1 A SER 28 ? A SER 2 3 1 Y 1 A SER 29 ? A SER 3 4 1 Y 1 A SER 234 ? A SER 208 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'CALCIUM ION' CA 3 N-ACETYL-D-GLUCOSAMINE NAG 4 water HOH #