data_5209 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignments for the perdeuterated 22 kD palm-thumb domain of DNA polymerase B in complex with the XRCC1 N-terminal domain ; _BMRB_accession_number 5209 _BMRB_flat_file_name bmr5209.str _Entry_type original _Submission_date 2001-11-14 _Accession_date 2001-11-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gryk Michael R. . 2 Marintchev Assen . . 3 Maciejewski Mark W. . 4 Robertson Anthony . . 5 Mullen Mary A. . 6 Wilson Samuel H. . 7 Mullen Gregory P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 220 "13C chemical shifts" 505 "15N chemical shifts" 164 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-06-02 original author . stop_ _Original_release_date 2005-06-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Mapping of the interaction interface of DNA polymerase beta with XRCC1' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12467578 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gryk Michael R. . 2 Marintchev Assen . . 3 Maciejewski Mark W. . 4 Robertson Anthony . . 5 Wilson Samuel H. . 6 Mullen Gregory P. . stop_ _Journal_abbreviation Structure _Journal_volume 10 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1709 _Page_last 1720 _Year 2002 _Details . loop_ _Keyword 'Rattus norvegicus' 'DNA polymerase B' TROSY deuteration 'DNA repair' XRCC1-NTD 'X-ray cross-complementing group 1' stop_ save_ ################################## # Molecular system description # ################################## save_system_B-pol _Saveframe_category molecular_system _Mol_system_name 'Palm-Thumb Domain of DNA Polymerase B in complex with XRCC1-NTD' _Abbreviation_common B-pol _Enzyme_commission_number 2.7.7.7 loop_ _Mol_system_component_name _Mol_label 'B-Pol palm-thumb' $B-Pol XRCC1-NTD $XRCC1-NTD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'DNA polmerization (C-terminal domain)' 'DNA binding (N-terminal domain)' 'deoxyribose 5'-phosphate excision at incised abasic sites (N-terminal domain)' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_B-Pol _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DNA Polymerase B' _Abbreviation_common B-Pol _Molecular_mass 22022 _Mol_thiol_state 'all free' _Details 'First 3 residues: MGK are not native to full length B-Pol.' ############################## # Polymer residue sequence # ############################## _Residue_count 190 _Mol_residue_sequence ; MGKRIPREEMLQMQDIVLNE VKKLDPEYIATVCGSFRRGA ESSGDMDVLLTHPNFTSESS KQPKLLHRVVEQLQKVRFIT DTLSKGETKFMGVCQLPSEN DENEYPHRRIDIRLIPKDQY YCGVLYFTGSDIFNKNMRAH ALEKGFTINEYTIRPLGVTG VAGEPLPVDSEQDIFDYIQW RYREPKDRSE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 MET 2 -2 GLY 3 -1 LYS 4 149 ARG 5 150 ILE 6 151 PRO 7 152 ARG 8 153 GLU 9 154 GLU 10 155 MET 11 156 LEU 12 157 GLN 13 158 MET 14 159 GLN 15 160 ASP 16 161 ILE 17 162 VAL 18 163 LEU 19 164 ASN 20 165 GLU 21 166 VAL 22 167 LYS 23 168 LYS 24 169 LEU 25 170 ASP 26 171 PRO 27 172 GLU 28 173 TYR 29 174 ILE 30 175 ALA 31 176 THR 32 177 VAL 33 178 CYS 34 179 GLY 35 180 SER 36 181 PHE 37 182 ARG 38 183 ARG 39 184 GLY 40 185 ALA 41 186 GLU 42 187 SER 43 188 SER 44 189 GLY 45 190 ASP 46 191 MET 47 192 ASP 48 193 VAL 49 194 LEU 50 195 LEU 51 196 THR 52 197 HIS 53 198 PRO 54 199 ASN 55 200 PHE 56 201 THR 57 202 SER 58 203 GLU 59 204 SER 60 205 SER 61 206 LYS 62 207 GLN 63 208 PRO 64 209 LYS 65 210 LEU 66 211 LEU 67 212 HIS 68 213 ARG 69 214 VAL 70 215 VAL 71 216 GLU 72 217 GLN 73 218 LEU 74 219 GLN 75 220 LYS 76 221 VAL 77 222 ARG 78 223 PHE 79 224 ILE 80 225 THR 81 226 ASP 82 227 THR 83 228 LEU 84 229 SER 85 230 LYS 86 231 GLY 87 232 GLU 88 233 THR 89 234 LYS 90 235 PHE 91 236 MET 92 237 GLY 93 238 VAL 94 239 CYS 95 240 GLN 96 241 LEU 97 242 PRO 98 243 SER 99 244 GLU 100 245 ASN 101 246 ASP 102 247 GLU 103 248 ASN 104 249 GLU 105 250 TYR 106 251 PRO 107 252 HIS 108 253 ARG 109 254 ARG 110 255 ILE 111 256 ASP 112 257 ILE 113 258 ARG 114 259 LEU 115 260 ILE 116 261 PRO 117 262 LYS 118 263 ASP 119 264 GLN 120 265 TYR 121 266 TYR 122 267 CYS 123 268 GLY 124 269 VAL 125 270 LEU 126 271 TYR 127 272 PHE 128 273 THR 129 274 GLY 130 275 SER 131 276 ASP 132 277 ILE 133 278 PHE 134 279 ASN 135 280 LYS 136 281 ASN 137 282 MET 138 283 ARG 139 284 ALA 140 285 HIS 141 286 ALA 142 287 LEU 143 288 GLU 144 289 LYS 145 290 GLY 146 291 PHE 147 292 THR 148 293 ILE 149 294 ASN 150 295 GLU 151 296 TYR 152 297 THR 153 298 ILE 154 299 ARG 155 300 PRO 156 301 LEU 157 302 GLY 158 303 VAL 159 304 THR 160 305 GLY 161 306 VAL 162 307 ALA 163 308 GLY 164 309 GLU 165 310 PRO 166 311 LEU 167 312 PRO 168 313 VAL 169 314 ASP 170 315 SER 171 316 GLU 172 317 GLN 173 318 ASP 174 319 ILE 175 320 PHE 176 321 ASP 177 322 TYR 178 323 ILE 179 324 GLN 180 325 TRP 181 326 ARG 182 327 TYR 183 328 ARG 184 329 GLU 185 330 PRO 186 331 LYS 187 332 ASP 188 333 ARG 189 334 SER 190 335 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4282 XRCC1_NTD 100.00 183 100.00 100.00 1.94e-111 PDB 1XNA "Nmr Solution Structure Of The Single-Strand Break Repair Protein Xrcc1-N-Terminal Domain" 99.36 183 100.00 100.00 1.84e-110 PDB 1XNT "Nmr Solution Structure Of The Single-Strand Break Repair Protein Xrcc1-N-Terminal Domain" 99.36 183 100.00 100.00 1.84e-110 PDB 3K75 "X-Ray Crystal Structure Of Reduced Xrcc1 Bound To Dna Pol Beta Catalytic Domain" 100.00 189 100.00 100.00 4.35e-111 PDB 3K77 "X-Ray Crystal Structure Of Xrcc1" 98.73 161 100.00 100.00 2.74e-109 PDB 3LQC "X-Ray Crystal Structure Of Oxidized Xrcc1 Bound To Dna Pol B Thumb Domain" 100.00 189 100.00 100.00 4.35e-111 DBJ BAD92018 "X-ray repair cross complementing protein 1 variant [Homo sapiens]" 100.00 647 100.00 100.00 1.25e-105 DBJ BAG10574 "DNA-repair protein XRCC1 [synthetic construct]" 100.00 633 100.00 100.00 6.36e-106 DBJ BAG37732 "unnamed protein product [Homo sapiens]" 100.00 633 100.00 100.00 5.96e-106 DBJ BAG57023 "unnamed protein product [Homo sapiens]" 100.00 400 100.00 100.00 1.26e-109 EMBL CAG33009 "XRCC1 [Homo sapiens]" 100.00 633 100.00 100.00 6.36e-106 GB AAA63270 "DNA-repair protein [Homo sapiens]" 100.00 633 100.00 100.00 7.15e-106 GB AAH23593 "X-ray repair complementing defective repair in Chinese hamster cells 1 [Homo sapiens]" 100.00 633 100.00 100.00 6.36e-106 GB AAM34791 "X-ray repair complementing defective repair in Chinese hamster cells 1 [Homo sapiens]" 100.00 633 100.00 100.00 7.15e-106 GB EAW57201 "X-ray repair complementing defective repair in Chinese hamster cells 1, isoform CRA_a [Homo sapiens]" 100.00 236 100.00 100.00 4.12e-110 GB EAW57202 "X-ray repair complementing defective repair in Chinese hamster cells 1, isoform CRA_b [Homo sapiens]" 100.00 633 100.00 100.00 7.15e-106 REF NP_006288 "DNA repair protein XRCC1 [Homo sapiens]" 100.00 633 100.00 100.00 6.36e-106 REF XP_001100256 "PREDICTED: DNA repair protein XRCC1 [Macaca mulatta]" 100.00 617 99.36 99.36 1.53e-105 REF XP_001499917 "PREDICTED: DNA repair protein XRCC1 [Equus caballus]" 100.00 630 98.09 100.00 3.06e-104 REF XP_002829368 "PREDICTED: DNA repair protein XRCC1 [Pongo abelii]" 100.00 633 99.36 99.36 2.35e-105 REF XP_002923977 "PREDICTED: DNA repair protein XRCC1-like [Ailuropoda melanoleuca]" 100.00 630 97.45 100.00 7.45e-104 SP P18887 "RecName: Full=DNA repair protein XRCC1; AltName: Full=X-ray repair cross-complementing protein 1 [Homo sapiens]" 100.00 633 100.00 100.00 7.08e-106 stop_ save_ save_XRCC1-NTD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'XRCC1 N-terminal Domain' _Abbreviation_common XRCC1-NTD _Molecular_mass 17358 _Mol_thiol_state 'all free' _Details . _Residue_count 157 _Mol_residue_sequence ; MPEIRLRHVVSCSSQDSTHC AENLLKADTYRKWRAAKAGE KTISVVLQLEKEEQIHSVDI GNDGSAFVEVLVGSSAGGAG EQDYEVLLVTSSFMSPSESR SGSNPNRVRMFGPDKLVRAA AEKRWDRVKIVCSQPYSKDS PFGLSFVRFHSPPDKDE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PRO 3 GLU 4 ILE 5 ARG 6 LEU 7 ARG 8 HIS 9 VAL 10 VAL 11 SER 12 CYS 13 SER 14 SER 15 GLN 16 ASP 17 SER 18 THR 19 HIS 20 CYS 21 ALA 22 GLU 23 ASN 24 LEU 25 LEU 26 LYS 27 ALA 28 ASP 29 THR 30 TYR 31 ARG 32 LYS 33 TRP 34 ARG 35 ALA 36 ALA 37 LYS 38 ALA 39 GLY 40 GLU 41 LYS 42 THR 43 ILE 44 SER 45 VAL 46 VAL 47 LEU 48 GLN 49 LEU 50 GLU 51 LYS 52 GLU 53 GLU 54 GLN 55 ILE 56 HIS 57 SER 58 VAL 59 ASP 60 ILE 61 GLY 62 ASN 63 ASP 64 GLY 65 SER 66 ALA 67 PHE 68 VAL 69 GLU 70 VAL 71 LEU 72 VAL 73 GLY 74 SER 75 SER 76 ALA 77 GLY 78 GLY 79 ALA 80 GLY 81 GLU 82 GLN 83 ASP 84 TYR 85 GLU 86 VAL 87 LEU 88 LEU 89 VAL 90 THR 91 SER 92 SER 93 PHE 94 MET 95 SER 96 PRO 97 SER 98 GLU 99 SER 100 ARG 101 SER 102 GLY 103 SER 104 ASN 105 PRO 106 ASN 107 ARG 108 VAL 109 ARG 110 MET 111 PHE 112 GLY 113 PRO 114 ASP 115 LYS 116 LEU 117 VAL 118 ARG 119 ALA 120 ALA 121 ALA 122 GLU 123 LYS 124 ARG 125 TRP 126 ASP 127 ARG 128 VAL 129 LYS 130 ILE 131 VAL 132 CYS 133 SER 134 GLN 135 PRO 136 TYR 137 SER 138 LYS 139 ASP 140 SER 141 PRO 142 PHE 143 GLY 144 LEU 145 SER 146 PHE 147 VAL 148 ARG 149 PHE 150 HIS 151 SER 152 PRO 153 PRO 154 ASP 155 LYS 156 ASP 157 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value SWISS-PROT P18887 'DNA-repair protein XRCC1 (X-ray repair cross-complementing protein 1)' 100.00 633 100.00 100.00 1.56e-88 REF XP_001499917 'PREDICTED: similar to DNA-repair protein XRCC1 (X-ray repair cross-complementing protein 1) [Equus caballus]' 100.00 630 98.09 100.00 3.08e-87 REF XP_001100256 'PREDICTED: X-ray repair cross complementing protein 1 [Macaca mulatta]' 100.00 645 99.36 99.36 1.05e-87 REF NP_006288 'X-ray repair cross complementing protein 1 [Homo sapiens]' 100.00 633 100.00 100.00 1.43e-88 GenBank EAW57202 'X-ray repair complementing defective repair in Chinese hamster cells 1, isoform CRA_b [Homo sapiens]' 100.00 633 100.00 100.00 1.56e-88 GenBank EAW57201 'X-ray repair complementing defective repair in Chinese hamster cells 1, isoform CRA_a [Homo sapiens]' 100.00 236 100.00 100.00 8.23e-88 GenBank AAM34791 'X-ray repair complementing defective repair in Chinese hamster cells 1 [Homo sapiens]' 100.00 633 100.00 100.00 1.56e-88 GenBank AAH23593 'X-ray repair complementing defective repair in Chinese hamster cells 1 [Homo sapiens]' 100.00 633 100.00 100.00 1.43e-88 GenBank AAA63270 'DNA-repair protein' 100.00 633 100.00 100.00 1.56e-88 EMBL CAG33009 'XRCC1 [Homo sapiens]' 100.00 633 100.00 100.00 1.43e-88 DBJ BAG57023 'unnamed protein product [Homo sapiens]' 100.00 400 100.00 100.00 3.21e-89 DBJ BAG37732 'unnamed protein product [Homo sapiens]' 100.00 633 100.00 100.00 1.36e-88 DBJ BAG10574 'DNA-repair protein XRCC1 [synthetic construct]' 100.00 633 100.00 100.00 1.43e-88 DBJ BAD92018 'X-ray repair cross complementing protein 1 variant [Homo sapiens]' 100.00 647 100.00 100.00 1.83e-88 PDB 1XNT 'Nmr Solution Structure Of The Single-Strand Break Repair Protein Xrcc1-N-Terminal Domain' 99.36 183 100.00 100.00 1.77e-87 PDB 1XNA 'Nmr Solution Structure Of The Single-Strand Break Repair Protein Xrcc1-N-Terminal Domain' 99.36 183 100.00 100.00 1.77e-87 BMRB 4282 'XRCC1 NTD' 100.00 183 100.00 100.00 3.18e-88 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $B-Pol Rat 10116 Eukaryota Metazoa Rattus norvegicus $XRCC1-NTD Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $B-Pol 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid pET-28a(+) $XRCC1-NTD 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid pET-23a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'AEBSF is 4-(2-aminoethyl)-benzenesulfonyl fluoride.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $B-Pol 700 uM 500 900 ; [U-98% 13C; U-99% 15N; U-97% 2H; except V g-methyls, L d-methyls, I d-methyl, and labile protons. ; $XRCC1-NTD 1.1 mM 0.8 1.4 . phosphate 46 mM 40 50 . 'sodium chloride' 135 mM 130 140 . 'sodium azide' 0.002 % 0.0015 0.0025 . AEBSF 100 uM 95 105 . 'dithiothreitol (DTT)' 5 mM 4.5 5.5 . H2O 90 % . . . D2O 10 % . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task 'spectral processing' stop_ _Details ; Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. & Bax, A. (1995) J. Biomol NMR, 6, 277-293. ; save_ save_sbtools _Saveframe_category software _Name sbtools _Version . loop_ _Task 'NMR data processing script generation' stop_ _Details ; Web based program developed by Gryk, M.R. & Maciejewski, M.W. available from sbtools.uchc.edu. ; save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2 loop_ _Task 'spectral analysis' stop_ _Details ; Bartels, C., Xia, T., Billeter, M., Guntert, P., and Wuthrich, K. (1995) J. Biomol. NMR, 6, 1-10. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_TROSY_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TROSY 1H-15N HSQC' _Sample_label . save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_2D_CT_1H-13C_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CT 1H-13C HSQC' _Sample_label . save_ save_3D_TROSY_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _Sample_label . save_ save_3D_TROSY_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _Sample_label . save_ save_3D_(HM)CMC(CM)HM_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (HM)CMC(CM)HM' _Sample_label . save_ save_3D_15N,13C_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N,13C NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TROSY 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CT 1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (HM)CMC(CM)HM' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N,13C NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_complex_cond1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.2 pH temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_Shift_Set_1 _Saveframe_category assigned_chemical_shifts _Details ; Isotope induced shifts are uncorrected. No correction has been made for Bloch-Siegert effects. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $complex_cond1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'B-Pol palm-thumb' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 4 ARG H H 8.47 0.01 1 2 . 4 ARG N N 120.43 0.14 1 3 . 4 ARG C C 175.52 0.06 1 4 . 4 ARG CA C 55.17 0.27 1 5 . 4 ARG CB C 30.23 0.27 1 6 . 5 ILE H H 9.45 0.01 1 7 . 5 ILE N N 122.97 0.14 1 8 . 5 ILE CA C 58.53 0.27 1 9 . 5 ILE CG1 C 25.86 0.02 1 10 . 5 ILE CD1 C 13.24 0.02 1 11 . 5 ILE HD1 H 0.67 0.01 1 12 . 6 PRO C C 178.49 0.06 1 13 . 7 ARG H H 8.42 0.01 1 14 . 7 ARG N N 125.55 0.14 1 15 . 7 ARG C C 177.43 0.06 1 16 . 7 ARG CA C 60.03 0.27 1 17 . 7 ARG CB C 28.63 0.27 1 18 . 8 GLU H H 9.44 0.01 1 19 . 8 GLU N N 115.52 0.14 1 20 . 8 GLU C C 179.81 0.06 1 21 . 9 GLU H H 7.23 0.01 1 22 . 9 GLU N N 118.67 0.14 1 23 . 9 GLU C C 178.78 0.06 1 24 . 9 GLU CA C 58.48 0.27 1 25 . 10 MET H H 7.89 0.01 1 26 . 10 MET N N 120.12 0.14 1 27 . 10 MET C C 179.23 0.06 1 28 . 10 MET CA C 56.67 0.27 1 29 . 11 LEU H H 8.87 0.01 1 30 . 11 LEU N N 119.04 0.14 1 31 . 11 LEU C C 179.81 0.06 1 32 . 11 LEU CA C 57.88 0.27 1 33 . 11 LEU CB C 40.95 0.27 1 34 . 11 LEU CG C 26.97 0.11 1 35 . 11 LEU CD1 C 25.83 0.02 2 36 . 11 LEU HD1 H 1 0.01 2 37 . 11 LEU CD2 C 23.22 0.02 2 38 . 11 LEU HD2 H 1.08 0.01 2 39 . 12 GLN H H 7.09 0.01 1 40 . 12 GLN N N 118.47 0.14 1 41 . 12 GLN C C 179.16 0.06 1 42 . 12 GLN CA C 58.39 0.27 1 43 . 12 GLN CB C 29.12 0.27 1 44 . 13 MET H H 8.40 0.01 1 45 . 13 MET N N 119.90 0.14 1 46 . 13 MET C C 176.93 0.06 1 47 . 13 MET CA C 58.71 0.27 1 48 . 13 MET CB C 33.81 0.27 1 49 . 14 GLN H H 8.91 0.01 1 50 . 14 GLN N N 118.38 0.14 1 51 . 14 GLN C C 176.11 0.06 1 52 . 14 GLN CA C 59.19 0.27 1 53 . 14 GLN CB C 28.58 0.27 1 54 . 15 ASP H H 7.59 0.01 1 55 . 15 ASP N N 117.85 0.14 1 56 . 15 ASP C C 178.19 0.06 1 57 . 15 ASP CA C 57.37 0.27 1 58 . 15 ASP CB C 40.00 0.27 1 59 . 16 ILE H H 7.17 0.01 1 60 . 16 ILE N N 118.41 0.14 1 61 . 16 ILE C C 177.67 0.06 1 62 . 16 ILE CA C 64.92 0.27 1 63 . 16 ILE CB C 37.33 0.27 1 64 . 16 ILE CG1 C 28.29 0.02 1 65 . 16 ILE CD1 C 14.2 0.02 1 66 . 16 ILE HD1 H 0.65 0.01 1 67 . 17 VAL H H 7.38 0.01 1 68 . 17 VAL N N 116.68 0.14 1 69 . 17 VAL C C 177.24 0.06 1 70 . 17 VAL CA C 66.54 0.27 1 71 . 17 VAL CB C 31.54 0.27 1 72 . 17 VAL CG1 C 20.42 0.02 2 73 . 17 VAL HG1 H 0.63 0.01 2 74 . 17 VAL CG2 C 23.78 0.02 2 75 . 17 VAL HG2 H 0.73 0.01 2 76 . 18 LEU H H 8.83 0.01 1 77 . 18 LEU N N 116.23 0.14 1 78 . 18 LEU C C 180.44 0.06 1 79 . 18 LEU CA C 58.11 0.27 1 80 . 18 LEU CB C 39.32 0.27 1 81 . 18 LEU CG C 27.65 0.11 1 82 . 18 LEU CD1 C 24.51 0.02 2 83 . 18 LEU HD1 H 0.89 0.01 2 84 . 18 LEU CD2 C 22.8 0.02 2 85 . 18 LEU HD2 H 0.86 0.01 2 86 . 19 ASN H H 8.20 0.01 1 87 . 19 ASN N N 116.19 0.14 1 88 . 19 ASN C C 178.41 0.06 1 89 . 19 ASN CA C 55.78 0.27 1 90 . 19 ASN CB C 37.93 0.27 1 91 . 20 GLU H H 8.18 0.01 1 92 . 20 GLU N N 117.24 0.14 1 93 . 20 GLU C C 179.90 0.06 1 94 . 20 GLU CA C 58.14 0.27 1 95 . 20 GLU CB C 27.89 0.27 1 96 . 21 VAL H H 8.23 0.01 1 97 . 21 VAL N N 117.82 0.14 1 98 . 21 VAL C C 176.67 0.06 1 99 . 21 VAL CA C 66.87 0.27 1 100 . 21 VAL CG1 C 22.43 0.02 2 101 . 21 VAL HG1 H 0.66 0.01 2 102 . 21 VAL CG2 C 23.64 0.02 2 103 . 21 VAL HG2 H 0.76 0.01 2 104 . 22 LYS H H 7.61 0.01 1 105 . 22 LYS N N 117.86 0.14 1 106 . 22 LYS C C 178.53 0.06 1 107 . 22 LYS CA C 58.22 0.27 1 108 . 22 LYS CB C 31.19 0.27 1 109 . 23 LYS H H 7.32 0.01 1 110 . 23 LYS N N 115.86 0.14 1 111 . 23 LYS C C 178.83 0.06 1 112 . 23 LYS CA C 58.15 0.27 1 113 . 23 LYS CB C 31.69 0.27 1 114 . 24 LEU H H 7.36 0.01 1 115 . 24 LEU N N 118.91 0.14 1 116 . 24 LEU C C 178.12 0.06 1 117 . 24 LEU CA C 56.82 0.27 1 118 . 24 LEU CG C 25.86 0.11 1 119 . 24 LEU CD1 C 23.5 0.02 2 120 . 24 LEU HD1 H 0.83 0.01 2 121 . 24 LEU CD2 C 26.11 0.02 2 122 . 24 LEU HD2 H 0.82 0.01 2 123 . 25 ASP H H 7.81 0.01 1 124 . 25 ASP N N 114.73 0.14 1 125 . 25 ASP CA C 52.04 0.27 1 126 . 25 ASP CB C 42.13 0.27 1 127 . 26 PRO C C 177.06 0.06 1 128 . 27 GLU H H 8.61 0.01 1 129 . 27 GLU N N 115.59 0.14 1 130 . 27 GLU C C 178.69 0.06 1 131 . 27 GLU CA C 56.00 0.27 1 132 . 27 GLU CB C 28.66 0.27 1 133 . 28 TYR H H 7.56 0.01 1 134 . 28 TYR N N 115.72 0.14 1 135 . 28 TYR C C 177.60 0.06 1 136 . 28 TYR CA C 59.90 0.27 1 137 . 28 TYR CB C 40.00 0.27 1 138 . 29 ILE H H 8.15 0.01 1 139 . 29 ILE N N 119.71 0.14 1 140 . 29 ILE C C 174.06 0.06 1 141 . 29 ILE CA C 60.90 0.27 1 142 . 29 ILE CB C 39.10 0.27 1 143 . 29 ILE CG1 C 26.08 0.02 1 144 . 29 ILE CD1 C 13.47 0.02 1 145 . 29 ILE HD1 H 0.67 0.01 1 146 . 30 ALA H H 8.64 0.01 1 147 . 30 ALA N N 127.74 0.14 1 148 . 30 ALA C C 175.63 0.06 1 149 . 30 ALA CA C 49.50 0.27 1 150 . 30 ALA CB C 21.20 0.27 1 151 . 31 THR H H 8.50 0.01 1 152 . 31 THR N N 115.05 0.14 1 153 . 31 THR C C 173.47 0.06 1 154 . 31 THR CB C 71.31 0.27 1 155 . 32 VAL H H 9.67 0.01 1 156 . 32 VAL N N 130.66 0.14 1 157 . 32 VAL C C 176.75 0.06 1 158 . 32 VAL CA C 62.74 0.27 1 159 . 32 VAL CB C 30.54 0.27 1 160 . 32 VAL CG1 C 21.68 0.02 2 161 . 32 VAL HG1 H 0.91 0.01 2 162 . 32 VAL CG2 C 23.48 0.02 2 163 . 32 VAL HG2 H 0.92 0.01 2 164 . 33 CYS H H 8.72 0.01 1 165 . 33 CYS N N 125.13 0.14 1 166 . 33 CYS C C 173.39 0.06 1 167 . 33 CYS CA C 59.04 0.27 1 168 . 33 CYS CB C 26.49 0.27 1 169 . 34 GLY H H 7.87 0.01 1 170 . 34 GLY N N 109.13 0.14 1 171 . 34 GLY CA C 45.06 0.27 1 172 . 35 SER C C 177.54 0.06 1 173 . 36 PHE H H 8.69 0.01 1 174 . 36 PHE N N 123.33 0.14 1 175 . 36 PHE C C 179.63 0.06 1 176 . 36 PHE CA C 61.46 0.27 1 177 . 37 ARG H H 7.49 0.01 1 178 . 37 ARG N N 122.79 0.14 1 179 . 37 ARG C C 176.17 0.06 1 180 . 37 ARG CA C 58.32 0.27 1 181 . 37 ARG CB C 27.41 0.27 1 182 . 38 ARG H H 7.06 0.01 1 183 . 38 ARG N N 112.98 0.14 1 184 . 38 ARG C C 175.31 0.06 1 185 . 38 ARG CA C 55.53 0.27 1 186 . 38 ARG CB C 28.64 0.27 1 187 . 39 GLY H H 7.47 0.01 1 188 . 39 GLY N N 104.76 0.14 1 189 . 39 GLY C C 174.57 0.06 1 190 . 39 GLY CA C 44.57 0.27 1 191 . 40 ALA H H 7.49 0.01 1 192 . 40 ALA N N 121.34 0.14 1 193 . 40 ALA C C 179.03 0.06 1 194 . 40 ALA CA C 52.51 0.27 1 195 . 40 ALA CB C 19.96 0.27 1 196 . 41 GLU H H 9.01 0.01 1 197 . 41 GLU N N 120.53 0.14 1 198 . 41 GLU C C 175.87 0.06 1 199 . 42 SER H H 7.76 0.01 1 200 . 42 SER N N 113.12 0.14 1 201 . 42 SER C C 173.27 0.06 1 202 . 42 SER CA C 57.05 0.27 1 203 . 42 SER CB C 65.12 0.27 1 204 . 43 SER H H 8.98 0.01 1 205 . 43 SER N N 116.23 0.14 1 206 . 44 GLY C C 173.36 0.06 1 207 . 45 ASP H H 7.84 0.01 1 208 . 45 ASP N N 117.42 0.14 1 209 . 45 ASP C C 172.58 0.06 1 210 . 45 ASP CA C 52.51 0.27 1 211 . 45 ASP CB C 41.24 0.27 1 212 . 46 MET H H 8.11 0.01 1 213 . 46 MET N N 117.21 0.14 1 214 . 46 MET C C 172.84 0.06 1 215 . 46 MET CA C 54.70 0.27 1 216 . 46 MET CB C 33.83 0.27 1 217 . 47 ASP H H 9.33 0.01 1 218 . 47 ASP N N 129.21 0.14 1 219 . 47 ASP C C 174.54 0.06 1 220 . 47 ASP CA C 52.29 0.27 1 221 . 47 ASP CB C 41.06 0.27 1 222 . 48 VAL H H 9.02 0.01 1 223 . 48 VAL N N 123.65 0.14 1 224 . 48 VAL C C 174.09 0.06 1 225 . 48 VAL CA C 61.04 0.27 1 226 . 48 VAL CB C 33.23 0.27 1 227 . 48 VAL CG1 C 20.84 0.02 2 228 . 48 VAL HG1 H 0.7 0.01 2 229 . 48 VAL CG2 C 21.73 0.02 2 230 . 48 VAL HG2 H 0.96 0.01 2 231 . 49 LEU H H 8.97 0.01 1 232 . 49 LEU N N 129.10 0.14 1 233 . 49 LEU C C 176.06 0.06 1 234 . 49 LEU CA C 54.50 0.27 1 235 . 49 LEU CB C 41.36 0.27 1 236 . 49 LEU CG C 30.05 0.11 1 237 . 49 LEU CD1 C 24.94 0.02 2 238 . 49 LEU HD1 H 0.74 0.01 2 239 . 49 LEU CD2 C 23.59 0.02 2 240 . 49 LEU HD2 H 0.71 0.01 2 241 . 50 LEU H H 10.12 0.01 1 242 . 50 LEU N N 133.31 0.14 1 243 . 50 LEU C C 173.97 0.06 1 244 . 50 LEU CA C 53.03 0.27 1 245 . 50 LEU CB C 47.29 0.27 1 246 . 50 LEU CG C 26.79 0.11 1 247 . 50 LEU CD1 C 25.92 0.02 2 248 . 50 LEU HD1 H 0.7 0.01 2 249 . 50 LEU CD2 C 23.22 0.02 2 250 . 50 LEU HD2 H 0.67 0.01 2 251 . 51 THR H H 9.04 0.01 1 252 . 51 THR N N 118.01 0.14 1 253 . 51 THR C C 171.63 0.06 1 254 . 51 THR CA C 60.87 0.27 1 255 . 51 THR CB C 68.79 0.27 1 256 . 52 HIS H H 8.77 0.01 1 257 . 52 HIS N N 122.85 0.14 1 258 . 52 HIS CA C 55.04 0.27 1 259 . 52 HIS CB C 36.07 0.27 1 260 . 53 PRO C C 176.94 0.06 1 261 . 54 ASN H H 11.00 0.01 1 262 . 54 ASN N N 118.15 0.14 1 263 . 54 ASN C C 175.18 0.06 1 264 . 54 ASN CB C 37.51 0.27 1 265 . 55 PHE H H 8.49 0.01 1 266 . 55 PHE N N 122.42 0.14 1 267 . 55 PHE C C 172.65 0.06 1 268 . 55 PHE CA C 54.48 0.27 1 269 . 55 PHE CB C 39.42 0.27 1 270 . 56 THR H H 8.36 0.01 1 271 . 56 THR N N 116.19 0.14 1 272 . 56 THR CA C 59.90 0.27 1 273 . 56 THR CB C 71.51 0.27 1 274 . 57 SER C C 175.17 0.06 1 275 . 58 GLU H H 8.02 0.01 1 276 . 58 GLU N N 119.10 0.14 1 277 . 58 GLU C C 176.57 0.06 1 278 . 58 GLU CA C 56.08 0.27 1 279 . 58 GLU CB C 29.36 0.27 1 280 . 59 SER H H 7.65 0.01 1 281 . 59 SER N N 116.21 0.14 1 282 . 59 SER CA C 58.03 0.27 1 283 . 59 SER CB C 64.02 0.27 1 284 . 60 SER C C 174.70 0.06 1 285 . 61 LYS H H 8.47 0.01 1 286 . 61 LYS N N 121.64 0.14 1 287 . 61 LYS C C 176.27 0.06 1 288 . 61 LYS CA C 56.63 0.27 1 289 . 61 LYS CB C 31.82 0.27 1 290 . 62 GLN H H 7.93 0.01 1 291 . 62 GLN N N 120.75 0.14 1 292 . 62 GLN CA C 52.70 0.27 1 293 . 62 GLN CB C 29.35 0.27 1 294 . 64 LYS C C 177.92 0.06 1 295 . 65 LEU H H 7.56 0.01 1 296 . 65 LEU N N 116.17 0.14 1 297 . 65 LEU C C 180.43 0.06 1 298 . 65 LEU CA C 56.53 0.27 1 299 . 65 LEU CB C 42.05 0.27 1 300 . 65 LEU CG C 26.28 0.11 1 301 . 65 LEU CD1 C 26.72 0.02 2 302 . 65 LEU HD1 H 0.64 0.01 2 303 . 65 LEU CD2 C 21.31 0.02 2 304 . 65 LEU HD2 H 0.3 0.01 2 305 . 66 LEU H H 7.68 0.01 1 306 . 66 LEU N N 117.87 0.14 1 307 . 66 LEU C C 177.89 0.06 1 308 . 67 HIS H H 8.40 0.01 1 309 . 67 HIS N N 119.78 0.14 1 310 . 67 HIS C C 177.22 0.06 1 311 . 67 HIS CA C 59.09 0.27 1 312 . 67 HIS CB C 30.63 0.27 1 313 . 68 ARG H H 8.50 0.01 1 314 . 68 ARG N N 115.57 0.14 1 315 . 68 ARG C C 179.16 0.06 1 316 . 68 ARG CA C 58.99 0.27 1 317 . 69 VAL H H 6.67 0.01 1 318 . 69 VAL N N 118.36 0.14 1 319 . 69 VAL C C 176.76 0.06 1 320 . 69 VAL CA C 65.61 0.27 1 321 . 69 VAL CB C 31.13 0.27 1 322 . 69 VAL CG1 C 20.56 0.02 2 323 . 69 VAL HG1 H 0.52 0.01 2 324 . 69 VAL CG2 C 22.71 0.02 2 325 . 69 VAL HG2 H 0.6 0.01 2 326 . 70 VAL H H 7.52 0.01 1 327 . 70 VAL N N 119.19 0.14 1 328 . 70 VAL C C 177.38 0.06 1 329 . 70 VAL CA C 66.49 0.27 1 330 . 70 VAL CB C 31.37 0.27 1 331 . 70 VAL CG1 C 20.37 0.02 2 332 . 70 VAL HG1 H 0.13 0.01 2 333 . 70 VAL CG2 C 22.05 0.02 2 334 . 70 VAL HG2 H 0.29 0.01 2 335 . 71 GLU H H 8.49 0.01 1 336 . 71 GLU N N 116.93 0.14 1 337 . 71 GLU C C 179.69 0.06 1 338 . 71 GLU CA C 58.37 0.27 1 339 . 71 GLU CB C 28.96 0.27 1 340 . 72 GLN H H 7.58 0.01 1 341 . 72 GLN N N 120.23 0.14 1 342 . 72 GLN C C 177.76 0.06 1 343 . 72 GLN CA C 57.69 0.27 1 344 . 73 LEU H H 8.03 0.01 1 345 . 73 LEU N N 116.64 0.14 1 346 . 73 LEU C C 180.35 0.06 1 347 . 73 LEU CA C 56.44 0.27 1 348 . 73 LEU CB C 40.42 0.27 1 349 . 74 GLN H H 8.48 0.01 1 350 . 74 GLN N N 121.15 0.14 1 351 . 74 GLN C C 180.02 0.06 1 352 . 74 GLN CA C 58.21 0.27 1 353 . 74 GLN CB C 28.20 0.27 1 354 . 75 LYS H H 8.39 0.01 1 355 . 75 LYS N N 125.18 0.14 1 356 . 75 LYS C C 179.23 0.06 1 357 . 76 VAL H H 7.45 0.01 1 358 . 76 VAL N N 108.04 0.14 1 359 . 76 VAL C C 175.04 0.06 1 360 . 76 VAL CA C 60.38 0.27 1 361 . 76 VAL CB C 30.41 0.27 1 362 . 76 VAL CG1 C 18.51 0.02 2 363 . 76 VAL HG1 H 0.99 0.01 2 364 . 76 VAL CG2 C 20.77 0.02 2 365 . 76 VAL HG2 H 0.95 0.01 2 366 . 77 ARG H H 7.83 0.01 1 367 . 77 ARG N N 114.73 0.14 1 368 . 77 ARG C C 174.15 0.06 1 369 . 77 ARG CA C 56.82 0.27 1 370 . 77 ARG CB C 25.18 0.27 1 371 . 78 PHE H H 7.89 0.01 1 372 . 78 PHE N N 117.14 0.14 1 373 . 78 PHE C C 175.87 0.06 1 374 . 78 PHE CA C 58.76 0.27 1 375 . 79 ILE H H 6.74 0.01 1 376 . 79 ILE N N 114.71 0.14 1 377 . 79 ILE C C 176.31 0.06 1 378 . 79 ILE CA C 60.27 0.27 1 379 . 79 ILE CB C 37.81 0.27 1 380 . 79 ILE CG1 C 28.06 0.02 1 381 . 79 ILE CD1 C 14.07 0.02 1 382 . 79 ILE HD1 H 0.64 0.01 1 383 . 80 THR H H 9.02 0.01 1 384 . 80 THR N N 119.69 0.14 1 385 . 80 THR C C 174.92 0.06 1 386 . 80 THR CA C 61.72 0.27 1 387 . 80 THR CB C 68.07 0.27 1 388 . 81 ASP H H 7.66 0.01 1 389 . 81 ASP N N 119.01 0.14 1 390 . 81 ASP C C 174.70 0.06 1 391 . 81 ASP CA C 53.80 0.27 1 392 . 82 THR H H 8.80 0.01 1 393 . 82 THR N N 117.98 0.14 1 394 . 82 THR C C 173.27 0.06 1 395 . 82 THR CA C 62.50 0.27 1 396 . 82 THR CB C 70.42 0.27 1 397 . 83 LEU H H 8.79 0.01 1 398 . 83 LEU N N 126.55 0.14 1 399 . 83 LEU C C 177.00 0.06 1 400 . 83 LEU CB C 40.87 0.27 1 401 . 83 LEU CG C 27.41 0.11 1 402 . 83 LEU CD1 C 22.47 0.02 2 403 . 83 LEU HD1 H 0.71 0.01 2 404 . 83 LEU CD2 C 24.69 0.02 2 405 . 83 LEU HD2 H 0.64 0.01 2 406 . 84 SER H H 7.97 0.01 1 407 . 84 SER N N 111.50 0.14 1 408 . 84 SER C C 172.15 0.06 1 409 . 84 SER CA C 57.01 0.27 1 410 . 84 SER CB C 63.37 0.27 1 411 . 85 LYS H H 8.95 0.01 1 412 . 85 LYS N N 128.14 0.14 1 413 . 85 LYS C C 174.56 0.06 1 414 . 86 GLY H H 8.13 0.01 1 415 . 86 GLY N N 113.72 0.14 1 416 . 86 GLY C C 173.57 0.06 1 417 . 86 GLY CA C 43.95 0.27 1 418 . 87 GLU H H 8.76 0.01 1 419 . 87 GLU N N 118.90 0.14 1 420 . 88 THR H H 8.32 0.01 1 421 . 88 THR N N 101.70 0.14 1 422 . 88 THR C C 174.00 0.06 1 423 . 89 LYS H H 7.26 0.01 1 424 . 89 LYS N N 122.89 0.14 1 425 . 89 LYS C C 173.81 0.06 1 426 . 89 LYS CA C 56.03 0.27 1 427 . 89 LYS CB C 35.04 0.27 1 428 . 90 PHE H H 9.57 0.01 1 429 . 90 PHE N N 128.59 0.14 1 430 . 90 PHE C C 173.26 0.06 1 431 . 90 PHE CA C 55.74 0.27 1 432 . 90 PHE CB C 41.83 0.27 1 433 . 91 MET H H 8.33 0.01 1 434 . 91 MET N N 124.89 0.14 1 435 . 91 MET C C 175.12 0.06 1 436 . 91 MET CA C 53.62 0.27 1 437 . 91 MET CB C 35.43 0.27 1 438 . 92 GLY H H 9.19 0.01 1 439 . 92 GLY N N 111.20 0.14 1 440 . 92 GLY C C 170.78 0.06 1 441 . 92 GLY CA C 45.79 0.27 1 442 . 93 VAL H H 8.54 0.01 1 443 . 93 VAL N N 123.99 0.14 1 444 . 93 VAL C C 174.16 0.06 1 445 . 93 VAL CA C 59.95 0.27 1 446 . 93 VAL CB C 34.76 0.27 1 447 . 93 VAL CG1 C 22.65 0.02 2 448 . 93 VAL HG1 H 1 0.01 2 449 . 93 VAL CG2 C 20.67 0.02 2 450 . 93 VAL HG2 H 0.74 0.01 2 451 . 94 CYS H H 9.75 0.01 1 452 . 94 CYS N N 122.08 0.14 1 453 . 94 CYS C C 171.61 0.06 1 454 . 94 CYS CA C 54.10 0.27 1 455 . 94 CYS CB C 32.65 0.27 1 456 . 95 GLN H H 8.14 0.01 1 457 . 95 GLN N N 118.54 0.14 1 458 . 95 GLN C C 174.43 0.06 1 459 . 95 GLN CA C 54.27 0.27 1 460 . 95 GLN CB C 32.62 0.27 1 461 . 96 LEU H H 9.12 0.01 1 462 . 96 LEU N N 128.06 0.14 1 463 . 96 LEU CA C 52.73 0.27 1 464 . 96 LEU CB C 40.32 0.27 1 465 . 96 LEU CG C 25.99 0.11 1 466 . 96 LEU CD1 C 24.18 0.02 2 467 . 96 LEU HD1 H 0.62 0.01 2 468 . 96 LEU CD2 C 24.96 0.02 2 469 . 96 LEU HD2 H 0.47 0.01 2 470 . 97 PRO C C 176.61 0.06 1 471 . 98 SER H H 8.41 0.01 1 472 . 98 SER N N 114.24 0.14 1 473 . 98 SER C C 175.18 0.06 1 474 . 98 SER CA C 56.65 0.27 1 475 . 98 SER CB C 64.24 0.27 1 476 . 99 GLU H H 8.94 0.01 1 477 . 99 GLU N N 123.63 0.14 1 478 . 99 GLU C C 176.51 0.06 1 479 . 99 GLU CA C 56.47 0.27 1 480 . 99 GLU CB C 29.64 0.27 1 481 . 100 ASN H H 8.46 0.01 1 482 . 100 ASN N N 117.38 0.14 1 483 . 100 ASN C C 174.89 0.06 1 484 . 100 ASN CA C 52.95 0.27 1 485 . 100 ASN CB C 38.94 0.27 1 486 . 101 ASP H H 8.41 0.01 1 487 . 101 ASP N N 118.94 0.14 1 488 . 101 ASP C C 176.25 0.06 1 489 . 101 ASP CA C 55.08 0.27 1 490 . 101 ASP CB C 40.18 0.27 1 491 . 102 GLU H H 8.12 0.01 1 492 . 102 GLU N N 118.49 0.14 1 493 . 102 GLU C C 175.99 0.06 1 494 . 102 GLU CA C 56.12 0.27 1 495 . 102 GLU CB C 29.61 0.27 1 496 . 103 ASN H H 8.18 0.01 1 497 . 103 ASN N N 118.87 0.14 1 498 . 103 ASN C C 174.42 0.06 1 499 . 103 ASN CA C 52.51 0.27 1 500 . 103 ASN CB C 39.02 0.27 1 501 . 104 GLU H H 8.38 0.01 1 502 . 104 GLU N N 122.00 0.14 1 503 . 104 GLU C C 176.69 0.06 1 504 . 104 GLU CA C 55.71 0.27 1 505 . 104 GLU CB C 30.05 0.27 1 506 . 105 TYR H H 8.99 0.01 1 507 . 105 TYR N N 123.62 0.14 1 508 . 105 TYR CA C 57.08 0.27 1 509 . 105 TYR CB C 37.43 0.27 1 510 . 106 PRO C C 176.00 0.06 1 511 . 107 HIS H H 8.35 0.01 1 512 . 107 HIS N N 118.67 0.14 1 513 . 107 HIS C C 176.06 0.06 1 514 . 107 HIS CA C 56.68 0.27 1 515 . 107 HIS CB C 29.15 0.27 1 516 . 108 ARG H H 9.64 0.01 1 517 . 108 ARG N N 121.48 0.14 1 518 . 108 ARG C C 175.65 0.06 1 519 . 108 ARG CA C 51.73 0.27 1 520 . 109 ARG H H 8.72 0.01 1 521 . 109 ARG N N 122.20 0.14 1 522 . 109 ARG C C 174.13 0.06 1 523 . 109 ARG CA C 55.48 0.27 1 524 . 109 ARG CB C 28.71 0.27 1 525 . 110 ILE H H 7.95 0.01 1 526 . 110 ILE N N 118.59 0.14 1 527 . 110 ILE C C 171.96 0.06 1 528 . 110 ILE CA C 57.57 0.27 1 529 . 110 ILE CB C 40.78 0.27 1 530 . 110 ILE CG1 C 28.49 0.02 1 531 . 110 ILE CD1 C 14.23 0.02 1 532 . 110 ILE HD1 H 0.89 0.01 1 533 . 111 ASP H H 8.89 0.01 1 534 . 111 ASP N N 128.07 0.14 1 535 . 111 ASP C C 175.43 0.06 1 536 . 111 ASP CA C 51.84 0.27 1 537 . 111 ASP CB C 42.54 0.27 1 538 . 112 ILE H H 9.30 0.01 1 539 . 112 ILE N N 118.62 0.14 1 540 . 112 ILE C C 174.55 0.06 1 541 . 112 ILE CA C 59.92 0.27 1 542 . 112 ILE CB C 40.00 0.27 1 543 . 112 ILE CG1 C 26.32 0.02 1 544 . 112 ILE CD1 C 13.1 0.02 1 545 . 112 ILE HD1 H 0.53 0.01 1 546 . 113 ARG H H 8.83 0.01 1 547 . 113 ARG N N 125.68 0.14 1 548 . 113 ARG C C 173.81 0.06 1 549 . 113 ARG CA C 53.86 0.27 1 550 . 113 ARG CB C 32.34 0.27 1 551 . 114 LEU H H 9.01 0.01 1 552 . 114 LEU N N 126.44 0.14 1 553 . 114 LEU C C 174.71 0.06 1 554 . 114 LEU CA C 53.60 0.27 1 555 . 114 LEU CB C 43.47 0.27 1 556 . 114 LEU CG C 26.97 0.11 1 557 . 114 LEU CD1 C 22.9 0.02 2 558 . 114 LEU HD1 H 0.79 0.01 2 559 . 114 LEU CD2 C 27.33 0.02 2 560 . 114 LEU HD2 H 0.43 0.01 2 561 . 115 ILE H H 9.22 0.01 1 562 . 115 ILE N N 128.60 0.14 1 563 . 115 ILE CA C 56.87 0.27 1 564 . 115 ILE CB C 41.80 0.27 1 565 . 115 ILE CG1 C 26.61 0.02 1 566 . 115 ILE CD1 C 13.01 0.02 1 567 . 115 ILE HD1 H 0.99 0.01 1 568 . 116 PRO C C 178.60 0.06 1 569 . 117 LYS H H 9.46 0.01 1 570 . 117 LYS N N 125.93 0.14 1 571 . 117 LYS C C 178.49 0.06 1 572 . 117 LYS CA C 59.73 0.27 1 573 . 117 LYS CB C 30.87 0.27 1 574 . 118 ASP H H 9.39 0.01 1 575 . 118 ASP N N 112.57 0.14 1 576 . 118 ASP C C 176.65 0.06 1 577 . 118 ASP CA C 54.37 0.27 1 578 . 118 ASP CB C 40.00 0.27 1 579 . 119 GLN H H 8.01 0.01 1 580 . 119 GLN N N 118.30 0.14 1 581 . 119 GLN C C 176.93 0.06 1 582 . 119 GLN CA C 56.00 0.27 1 583 . 120 TYR H H 7.53 0.01 1 584 . 120 TYR N N 121.02 0.14 1 585 . 120 TYR C C 176.46 0.06 1 586 . 121 TYR H H 7.76 0.01 1 587 . 121 TYR N N 115.05 0.14 1 588 . 121 TYR C C 178.25 0.06 1 589 . 121 TYR CA C 63.58 0.27 1 590 . 121 TYR CB C 36.25 0.27 1 591 . 122 CYS H H 9.26 0.01 1 592 . 122 CYS N N 120.30 0.14 1 593 . 122 CYS C C 177.97 0.06 1 594 . 122 CYS CA C 64.36 0.27 1 595 . 122 CYS CB C 25.86 0.27 1 596 . 123 GLY H H 7.63 0.01 1 597 . 123 GLY N N 110.77 0.14 1 598 . 123 GLY C C 174.76 0.06 1 599 . 123 GLY CA C 47.37 0.27 1 600 . 124 VAL H H 8.87 0.01 1 601 . 124 VAL N N 124.28 0.14 1 602 . 124 VAL C C 179.08 0.06 1 603 . 124 VAL CA C 65.76 0.27 1 604 . 124 VAL CB C 31.62 0.27 1 605 . 124 VAL CG1 C 22.19 0.02 2 606 . 124 VAL HG1 H 0.15 0.01 2 607 . 124 VAL CG2 C 21.03 0.02 2 608 . 124 VAL HG2 H 0.91 0.01 2 609 . 125 LEU H H 8.48 0.01 1 610 . 125 LEU N N 123.18 0.14 1 611 . 125 LEU C C 180.12 0.06 1 612 . 125 LEU CA C 58.69 0.27 1 613 . 125 LEU CB C 42.04 0.27 1 614 . 125 LEU CG C 26.35 0.11 1 615 . 125 LEU CD1 C 25.46 0.02 2 616 . 125 LEU HD1 H 1.14 0.01 2 617 . 125 LEU CD2 C 27 0.02 2 618 . 125 LEU HD2 H 1.08 0.01 2 619 . 126 TYR H H 8.10 0.01 1 620 . 126 TYR N N 120.66 0.14 1 621 . 126 TYR C C 179.46 0.06 1 622 . 126 TYR CA C 61.09 0.27 1 623 . 126 TYR CB C 37.51 0.27 1 624 . 127 PHE H H 9.23 0.01 1 625 . 127 PHE N N 113.56 0.14 1 626 . 127 PHE C C 178.37 0.06 1 627 . 127 PHE CA C 60.89 0.27 1 628 . 127 PHE CB C 36.28 0.27 1 629 . 128 THR H H 7.95 0.01 1 630 . 128 THR N N 119.97 0.14 1 631 . 128 THR C C 172.80 0.06 1 632 . 129 GLY H H 7.04 0.01 1 633 . 129 GLY N N 107.05 0.14 1 634 . 129 GLY C C 175.31 0.06 1 635 . 129 GLY CA C 42.84 0.27 1 636 . 130 SER H H 7.49 0.01 1 637 . 130 SER N N 115.24 0.14 1 638 . 130 SER CB C 65.83 0.27 1 639 . 131 ASP C C 178.97 0.06 1 640 . 132 ILE H H 8.00 0.01 1 641 . 132 ILE N N 120.43 0.14 1 642 . 132 ILE C C 177.64 0.06 1 643 . 132 ILE CA C 63.36 0.27 1 644 . 132 ILE CG1 C 27.82 0.02 1 645 . 132 ILE CD1 C 11.96 0.02 1 646 . 132 ILE HD1 H 0.91 0.01 1 647 . 133 PHE H H 7.78 0.01 1 648 . 133 PHE N N 122.77 0.14 1 649 . 133 PHE C C 177.16 0.06 1 650 . 134 ASN H H 8.64 0.01 1 651 . 134 ASN N N 117.35 0.14 1 652 . 134 ASN C C 178.49 0.06 1 653 . 134 ASN CA C 55.77 0.27 1 654 . 134 ASN CB C 37.21 0.27 1 655 . 135 LYS H H 7.70 0.01 1 656 . 135 LYS N N 120.51 0.14 1 657 . 135 LYS C C 179.50 0.06 1 658 . 135 LYS CA C 59.39 0.27 1 659 . 136 ASN H H 8.44 0.01 1 660 . 136 ASN N N 120.89 0.14 1 661 . 136 ASN C C 178.46 0.06 1 662 . 136 ASN CA C 55.34 0.27 1 663 . 137 MET H H 9.24 0.01 1 664 . 137 MET N N 124.03 0.14 1 665 . 137 MET C C 177.74 0.06 1 666 . 137 MET CA C 58.75 0.27 1 667 . 138 ARG H H 8.18 0.01 1 668 . 138 ARG N N 118.21 0.14 1 669 . 138 ARG C C 179.12 0.06 1 670 . 138 ARG CA C 59.55 0.27 1 671 . 138 ARG CB C 29.61 0.27 1 672 . 139 ALA H H 7.87 0.01 1 673 . 139 ALA N N 121.57 0.14 1 674 . 139 ALA C C 180.44 0.06 1 675 . 139 ALA CB C 17.26 0.27 1 676 . 140 HIS H H 7.83 0.01 1 677 . 140 HIS N N 119.27 0.14 1 678 . 140 HIS C C 177.10 0.06 1 679 . 140 HIS CA C 58.96 0.27 1 680 . 141 ALA H H 8.48 0.01 1 681 . 141 ALA N N 119.12 0.14 1 682 . 141 ALA C C 179.52 0.06 1 683 . 141 ALA CA C 55.14 0.27 1 684 . 142 LEU H H 7.92 0.01 1 685 . 142 LEU N N 119.09 0.14 1 686 . 142 LEU C C 181.43 0.06 1 687 . 142 LEU CA C 57.80 0.27 1 688 . 142 LEU CB C 41.13 0.27 1 689 . 143 GLU H H 7.55 0.01 1 690 . 143 GLU N N 120.32 0.14 1 691 . 143 GLU C C 178.51 0.06 1 692 . 144 LYS H H 7.44 0.01 1 693 . 144 LYS N N 115.98 0.14 1 694 . 144 LYS C C 175.84 0.06 1 695 . 144 LYS CA C 53.78 0.27 1 696 . 145 GLY H H 7.89 0.01 1 697 . 145 GLY N N 106.47 0.14 1 698 . 145 GLY C C 173.12 0.06 1 699 . 145 GLY CA C 45.45 0.27 1 700 . 146 PHE H H 8.63 0.01 1 701 . 146 PHE N N 118.88 0.14 1 702 . 146 PHE C C 173.64 0.06 1 703 . 146 PHE CA C 56.58 0.27 1 704 . 146 PHE CB C 42.47 0.27 1 705 . 147 THR H H 9.02 0.01 1 706 . 147 THR N N 112.71 0.14 1 707 . 147 THR C C 173.20 0.06 1 708 . 147 THR CA C 58.13 0.27 1 709 . 147 THR CB C 69.71 0.27 1 710 . 148 ILE H H 7.99 0.01 1 711 . 148 ILE N N 129.03 0.14 1 712 . 148 ILE C C 174.25 0.06 1 713 . 148 ILE CA C 59.32 0.27 1 714 . 148 ILE CB C 40.86 0.27 1 715 . 148 ILE CG1 C 27.41 0.02 1 716 . 148 ILE CD1 C 15.06 0.02 1 717 . 148 ILE HD1 H 0.64 0.01 1 718 . 149 ASN H H 8.55 0.01 1 719 . 149 ASN N N 126.49 0.14 1 720 . 149 ASN C C 173.87 0.06 1 721 . 149 ASN CA C 50.86 0.27 1 722 . 149 ASN CB C 38.00 0.27 1 723 . 150 GLU H H 9.20 0.01 1 724 . 150 GLU N N 116.31 0.14 1 725 . 150 GLU C C 173.46 0.06 1 726 . 150 GLU CA C 57.89 0.27 1 727 . 150 GLU CB C 27.52 0.27 1 728 . 151 TYR H H 7.87 0.01 1 729 . 151 TYR N N 113.68 0.14 1 730 . 151 TYR C C 176.32 0.06 1 731 . 151 TYR CA C 57.88 0.27 1 732 . 152 THR H H 8.41 0.01 1 733 . 152 THR N N 107.51 0.14 1 734 . 152 THR C C 172.81 0.06 1 735 . 153 ILE H H 9.32 0.01 1 736 . 153 ILE N N 118.52 0.14 1 737 . 153 ILE C C 172.88 0.06 1 738 . 153 ILE CA C 58.40 0.27 1 739 . 153 ILE CB C 39.89 0.27 1 740 . 153 ILE CG1 C 28.69 0.02 1 741 . 153 ILE CD1 C 14.22 0.02 1 742 . 153 ILE HD1 H 0.54 0.01 1 743 . 154 ARG H H 8.32 0.01 1 744 . 154 ARG N N 123.77 0.14 1 745 . 154 ARG CA C 51.22 0.27 1 746 . 154 ARG CB C 32.55 0.27 1 747 . 155 PRO C C 175.02 0.06 1 748 . 156 LEU H H 7.97 0.01 1 749 . 156 LEU N N 120.76 0.14 1 750 . 156 LEU C C 177.55 0.06 1 751 . 156 LEU CA C 52.96 0.27 1 752 . 156 LEU CB C 43.07 0.27 1 753 . 156 LEU CG C 26.08 0.11 1 754 . 156 LEU CD1 C 25.5 0.02 2 755 . 156 LEU HD1 H 0.59 0.01 2 756 . 156 LEU CD2 C 22.85 0.02 2 757 . 156 LEU HD2 H 0.51 0.01 2 758 . 157 GLY H H 7.87 0.01 1 759 . 157 GLY N N 108.51 0.14 1 760 . 157 GLY CA C 43.88 0.27 1 761 . 159 THR C C 175.08 0.06 1 762 . 160 GLY H H 7.85 0.01 1 763 . 160 GLY N N 109.50 0.14 1 764 . 160 GLY CA C 45.06 0.27 1 765 . 161 VAL C C 177.67 0.06 1 766 . 162 ALA H H 8.96 0.01 1 767 . 162 ALA N N 134.87 0.14 1 768 . 162 ALA C C 177.44 0.06 1 769 . 162 ALA CA C 52.61 0.27 1 770 . 162 ALA CB C 17.90 0.27 1 771 . 163 GLY H H 8.83 0.01 1 772 . 163 GLY N N 107.18 0.14 1 773 . 163 GLY C C 173.08 0.06 1 774 . 163 GLY CA C 43.08 0.27 1 775 . 164 GLU H H 8.07 0.01 1 776 . 164 GLU N N 122.37 0.14 1 777 . 164 GLU CA C 53.98 0.27 1 778 . 164 GLU CB C 29.45 0.27 1 779 . 165 PRO C C 177.30 0.06 1 780 . 166 LEU H H 8.42 0.01 1 781 . 166 LEU N N 126.67 0.14 1 782 . 166 LEU CA C 52.23 0.27 1 783 . 166 LEU CB C 39.09 0.27 1 784 . 166 LEU CG C 25.96 0.11 1 785 . 166 LEU CD1 C 22.8 0.02 2 786 . 166 LEU HD1 H 1.03 0.01 2 787 . 166 LEU CD2 C 24.15 0.02 2 788 . 166 LEU HD2 H 0.3 0.01 2 789 . 167 PRO C C 177.88 0.06 1 790 . 168 VAL H H 9.24 0.01 1 791 . 168 VAL N N 126.07 0.14 1 792 . 168 VAL C C 175.43 0.06 1 793 . 168 VAL CA C 62.47 0.27 1 794 . 168 VAL CB C 35.06 0.27 1 795 . 168 VAL CG1 C 21.91 0.02 2 796 . 168 VAL HG1 H 1.13 0.01 2 797 . 168 VAL CG2 C 25.18 0.02 2 798 . 168 VAL HG2 H 1.27 0.01 2 799 . 169 ASP H H 10.03 0.01 1 800 . 169 ASP N N 129.15 0.14 1 801 . 169 ASP C C 173.60 0.06 1 802 . 169 ASP CB C 42.40 0.27 1 803 . 170 SER H H 7.48 0.01 1 804 . 170 SER N N 110.39 0.14 1 805 . 170 SER C C 174.34 0.06 1 806 . 170 SER CA C 56.63 0.27 1 807 . 170 SER CB C 64.36 0.27 1 808 . 171 GLU H H 9.17 0.01 1 809 . 171 GLU N N 118.69 0.14 1 810 . 171 GLU C C 179.55 0.06 1 811 . 171 GLU CA C 60.27 0.27 1 812 . 171 GLU CB C 31.29 0.27 1 813 . 172 GLN H H 8.89 0.01 1 814 . 172 GLN N N 118.38 0.14 1 815 . 172 GLN C C 177.93 0.06 1 816 . 172 GLN CA C 59.95 0.27 1 817 . 172 GLN CB C 26.30 0.27 1 818 . 173 ASP H H 7.75 0.01 1 819 . 173 ASP N N 118.22 0.14 1 820 . 173 ASP C C 177.53 0.06 1 821 . 173 ASP CB C 40.51 0.27 1 822 . 174 ILE H H 7.53 0.01 1 823 . 174 ILE N N 117.18 0.14 1 824 . 174 ILE C C 177.39 0.06 1 825 . 174 ILE CA C 66.15 0.27 1 826 . 174 ILE CG1 C 29.05 0.02 1 827 . 174 ILE CD1 C 15.87 0.02 1 828 . 174 ILE HD1 H 1.09 0.01 1 829 . 175 PHE H H 7.14 0.01 1 830 . 175 PHE N N 114.71 0.14 1 831 . 175 PHE C C 177.61 0.06 1 832 . 175 PHE CA C 62.21 0.27 1 833 . 176 ASP H H 8.36 0.01 1 834 . 176 ASP N N 118.61 0.14 1 835 . 176 ASP CA C 56.73 0.27 1 836 . 176 ASP CB C 38.88 0.27 1 837 . 177 TYR C C 179.07 0.06 1 838 . 178 ILE H H 6.84 0.01 1 839 . 178 ILE N N 106.37 0.14 1 840 . 178 ILE C C 172.79 0.06 1 841 . 178 ILE CA C 60.04 0.27 1 842 . 178 ILE CB C 37.03 0.27 1 843 . 178 ILE CG1 C 24.31 0.02 1 844 . 178 ILE CD1 C 14.78 0.02 1 845 . 178 ILE HD1 H 0.49 0.01 1 846 . 179 GLN H H 7.97 0.01 1 847 . 179 GLN N N 116.55 0.14 1 848 . 179 GLN C C 174.31 0.06 1 849 . 179 GLN CA C 56.34 0.27 1 850 . 179 GLN CB C 26.78 0.27 1 851 . 180 TRP H H 8.40 0.01 1 852 . 180 TRP N N 122.04 0.14 1 853 . 180 TRP C C 175.87 0.06 1 854 . 180 TRP CA C 53.24 0.27 1 855 . 180 TRP CB C 33.27 0.27 1 856 . 181 ARG H H 8.07 0.01 1 857 . 181 ARG N N 125.26 0.14 1 858 . 181 ARG C C 175.66 0.06 1 859 . 181 ARG CA C 56.27 0.27 1 860 . 181 ARG CB C 29.16 0.27 1 861 . 182 TYR H H 8.58 0.01 1 862 . 182 TYR N N 124.82 0.14 1 863 . 182 TYR CA C 59.63 0.27 1 864 . 182 TYR CB C 37.13 0.27 1 865 . 185 PRO C C 176.69 0.06 1 866 . 186 LYS H H 8.12 0.01 1 867 . 186 LYS N N 111.99 0.14 1 868 . 186 LYS C C 176.65 0.06 1 869 . 186 LYS CA C 57.01 0.27 1 870 . 186 LYS CB C 30.13 0.27 1 871 . 187 ASP H H 7.92 0.01 1 872 . 187 ASP N N 119.61 0.14 1 873 . 187 ASP C C 176.13 0.06 1 874 . 187 ASP CA C 53.72 0.27 1 875 . 187 ASP CB C 40.62 0.27 1 876 . 188 ARG H H 7.21 0.01 1 877 . 188 ARG N N 119.31 0.14 1 878 . 188 ARG C C 175.46 0.06 1 879 . 188 ARG CA C 54.95 0.27 1 880 . 188 ARG CB C 28.49 0.27 1 881 . 189 SER H H 7.94 0.01 1 882 . 189 SER N N 115.63 0.14 1 883 . 189 SER C C 175.54 0.06 1 884 . 189 SER CA C 60.58 0.27 1 885 . 189 SER CB C 61.71 0.27 1 886 . 190 GLU H H 7.83 0.01 1 887 . 190 GLU N N 126.04 0.14 1 888 . 190 GLU CA C 57.22 0.27 1 889 . 190 GLU CB C 31.16 0.27 1 stop_ save_