data_4885 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N and 13C Resonance Assignments of the NTPase Subdomain of the Hepatitis C Virus NS3 RNA Helicase ; _BMRB_accession_number 4885 _BMRB_flat_file_name bmr4885.str _Entry_type original _Submission_date 2000-10-25 _Accession_date 2000-10-25 _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 Liu Dingjiang . . 2 Wyss Daniel F. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 119 "13C chemical shifts" 356 "15N chemical shifts" 119 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-11-14 original author . stop_ _Original_release_date 2001-11-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone 1H, 15N and 13C Resonance Assignments of the NTPase Subdomain of the Hepatitis C Virus NS3 RNA Helicase ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21228260 _PubMed_ID 11330818 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Dingjiang . . 2 Wyss Daniel . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 283 _Page_last 284 _Year 2001 _Details . loop_ _Keyword HCV NMR helicase stop_ save_ ################################## # Molecular system description # ################################## save_HCV_helicase _Saveframe_category molecular_system _Mol_system_name 'HCV NS3 RNA helicase' _Abbreviation_common 'HCV helicase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HCV helicase NTPase domain' $d1-HCVh stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomeric _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function NTPase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_d1-HCVh _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'HCV helicase' _Name_variant 'NTPase domain of HCV RNA helicase' _Abbreviation_common d1-HCVh _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 144 _Mol_residue_sequence ; SPVFTDNSSPPAVPQSFQVA HLHAPTGSGKSTKVPAAYAA QGYKVLVLNPSVAATLGFGA YMSKAHGVDPNIRTGVRTIT TGSPITYSTYGKFLADGGCS GGAYDIIICDECHSTDATSI LGIGTVLDQAETAGARLVVL ATAT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 181 SER 2 182 PRO 3 183 VAL 4 184 PHE 5 185 THR 6 186 ASP 7 187 ASN 8 188 SER 9 189 SER 10 190 PRO 11 191 PRO 12 192 ALA 13 193 VAL 14 194 PRO 15 195 GLN 16 196 SER 17 197 PHE 18 198 GLN 19 199 VAL 20 200 ALA 21 201 HIS 22 202 LEU 23 203 HIS 24 204 ALA 25 205 PRO 26 206 THR 27 207 GLY 28 208 SER 29 209 GLY 30 210 LYS 31 211 SER 32 212 THR 33 213 LYS 34 214 VAL 35 215 PRO 36 216 ALA 37 217 ALA 38 218 TYR 39 219 ALA 40 220 ALA 41 221 GLN 42 222 GLY 43 223 TYR 44 224 LYS 45 225 VAL 46 226 LEU 47 227 VAL 48 228 LEU 49 229 ASN 50 230 PRO 51 231 SER 52 232 VAL 53 233 ALA 54 234 ALA 55 235 THR 56 236 LEU 57 237 GLY 58 238 PHE 59 239 GLY 60 240 ALA 61 241 TYR 62 242 MET 63 243 SER 64 244 LYS 65 245 ALA 66 246 HIS 67 247 GLY 68 248 VAL 69 249 ASP 70 250 PRO 71 251 ASN 72 252 ILE 73 253 ARG 74 254 THR 75 255 GLY 76 256 VAL 77 257 ARG 78 258 THR 79 259 ILE 80 260 THR 81 261 THR 82 262 GLY 83 263 SER 84 264 PRO 85 265 ILE 86 266 THR 87 267 TYR 88 268 SER 89 269 THR 90 270 TYR 91 271 GLY 92 272 LYS 93 273 PHE 94 274 LEU 95 275 ALA 96 276 ASP 97 277 GLY 98 278 GLY 99 279 CYS 100 280 SER 101 281 GLY 102 282 GLY 103 283 ALA 104 284 TYR 105 285 ASP 106 286 ILE 107 287 ILE 108 288 ILE 109 289 CYS 110 290 ASP 111 291 GLU 112 292 CYS 113 293 HIS 114 294 SER 115 295 THR 116 296 ASP 117 297 ALA 118 298 THR 119 299 SER 120 300 ILE 121 301 LEU 122 302 GLY 123 303 ILE 124 304 GLY 125 305 THR 126 306 VAL 127 307 LEU 128 308 ASP 129 309 GLN 130 310 ALA 131 311 GLU 132 312 THR 133 313 ALA 134 314 GLY 135 315 ALA 136 316 ARG 137 317 LEU 138 318 VAL 139 319 VAL 140 320 LEU 141 321 ALA 142 322 THR 143 323 ALA 144 324 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 PDB 1A1V "Hepatitis C Virus Ns3 Helicase Domain Complexed With Single Stranded Sdna" 100.00 476 99.31 99.31 5.51e-91 PDB 1HEI "Structure Of The Hepatitis C Virus Rna Helicase Domain" 100.00 451 100.00 100.00 4.62e-93 PDB 4OJQ "Crystal Structure Of Hepatitis C Virus Ns3 Helicase Inhibitor Co- Complex With Fragment 1 [(5-bromo-1h-indol-3-yl)acetic Acid]" 100.00 464 100.00 100.00 9.39e-93 PDB 4OK3 "Crystal Structure Of Hepatitis C Virus Ns3 Helicase Inhibitor Co- Complex With Compound 7 [[1-(3-chlorobenzyl)-1h-indol-3-yl]ac" 100.00 464 100.00 100.00 9.39e-93 PDB 4OK5 "Crystal Structure Of Hepatitis C Virus Ns3 Helicase Inhibitor Co- Complex With Compound 9 [1-(3-ethynylbenzyl)-1h-indol-3-yl]ac" 100.00 464 100.00 100.00 9.39e-93 PDB 4OK6 "Crystal Structure Of Hepatitis C Virus Ns3 Helicase Inhibitor Co- Complex With Compound 13 [[1-(2-methoxy-5-nitrobenzyl)-1h-ind" 100.00 464 100.00 100.00 9.39e-93 PDB 4OKS "Crystal Structure Of Hepatitis C Virus Ns3 Helicase Inhibitor Co- Complex With Compound 19 [[6-(3,5-diaminophenyl)-1-(2-methoxy" 100.00 464 100.00 100.00 9.39e-93 DBJ BAA01582 "polyprotein precursor [Hepatitis C virus]" 100.00 3011 98.61 100.00 1.34e-86 DBJ BAA03178 "NS3 protein [Hepatitis C virus]" 90.28 284 96.92 99.23 8.54e-82 DBJ BAA08120 "HCV polyprotein [Hepatitis C virus]" 100.00 3010 97.92 100.00 6.10e-86 DBJ BAA09073 "polyprotein [Hepatitis C virus]" 100.00 3010 97.22 99.31 3.07e-85 DBJ BAA09075 "polyprotein [Hepatitis C virus]" 100.00 3010 97.22 99.31 3.01e-85 EMBL CAC03609 "unnamed protein product [Hepatitis C virus]" 100.00 3011 98.61 100.00 1.74e-86 EMBL CAJ20150 "non structural protein 3 [Hepatitis C virus]" 100.00 503 97.22 100.00 6.55e-90 EMBL CAJ20155 "non structural protein 3 [Hepatitis C virus]" 100.00 503 98.61 100.00 2.65e-91 EMBL CAJ20158 "non structural protein 3 [Hepatitis C virus]" 100.00 503 100.00 100.00 6.55e-92 EMBL CAJ20165 "non structural protein 3 [Hepatitis C virus]" 100.00 503 97.92 99.31 4.64e-90 GB AAA45534 "polyprotein [Hepatitis C virus subtype 1a]" 100.00 3011 97.92 98.61 1.11e-84 GB AAA45676 "polyprotein [Hepatitis C virus subtype 1a]" 100.00 3011 98.61 99.31 2.39e-86 GB AAA45677 "polyprotein, partial [Hepatitis C virus]" 100.00 2436 98.61 99.31 1.69e-86 GB AAB02124 "NS3, partial [Hepatitis C virus]" 98.61 428 100.00 100.00 1.56e-91 GB AAB02125 "polyprotein, partial [Hepatitis C virus]" 98.61 428 97.89 100.00 1.65e-89 REF NP_671491 "polyprotein [Hepatitis C virus]" 100.00 3011 100.00 100.00 4.80e-87 REF NP_803144 "NS3 protease/helicase' [Hepatitis C virus]" 100.00 631 100.00 100.00 4.76e-91 SP P26664 "RecName: Full=Genome polyprotein; Contains: RecName: Full=Core protein p21; AltName: Full=Capsid protein C; AltName: Full=p21; " 100.00 3011 98.61 99.31 2.39e-86 SP P27958 "RecName: Full=Genome polyprotein; Contains: RecName: Full=Core protein p21; AltName: Full=Capsid protein C; AltName: Full=p21; " 100.00 3011 97.92 98.61 1.11e-84 SP Q03463 "RecName: Full=Genome polyprotein; Contains: RecName: Full=Core protein p21; AltName: Full=Capsid protein C; AltName: Full=p21; " 100.00 3011 98.61 100.00 1.34e-86 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $d1-HCVh 'hepatitis C virus' 31646 viruses . viruses 'hepatitis C virus' 1a stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $d1-HCVh 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $d1-HCVh . mM 0.075 0.5 '[U-15N; U-13C; U-2H]' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 98 _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 4.1.2 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ save_1H-15N_TOCSY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCOCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _Sample_label . save_ save_HNCOCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCACB _Sample_label . save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.1 n/a temperature 293 0.5 K 'ionic strength' 0.1 0.02 M 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 TSP H 1 'methyl protons' ppm 0 external direct cylindrical external parallel_to_Bo . DSS C 13 'methyl protons' ppm 0 . indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0 . indirect . . . 0.101329118 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'HCV helicase NTPase domain' _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 . 2 PRO CA C 62.34 . 1 2 . 2 PRO CB C 30.83 . 1 3 . 2 PRO C C 176.34 . 1 4 . 3 VAL N N 119.26 . 1 5 . 3 VAL H H 7.97 . 1 6 . 3 VAL CA C 61.49 . 1 7 . 3 VAL CB C 31.67 . 1 8 . 3 VAL C C 175.65 . 1 9 . 4 PHE N N 123.91 . 1 10 . 4 PHE H H 8.34 . 1 11 . 4 PHE CA C 56.71 . 1 12 . 4 PHE CB C 38.99 . 1 13 . 11 PRO CA C 62.35 . 1 14 . 11 PRO CB C 29.98 . 1 15 . 11 PRO C C 176.71 . 1 16 . 12 ALA N N 125.13 . 1 17 . 12 ALA H H 8.29 . 1 18 . 12 ALA CA C 50.91 . 1 19 . 12 ALA CB C 17.79 . 1 20 . 12 ALA C C 177.09 . 1 21 . 13 VAL N N 121.67 . 1 22 . 13 VAL H H 8.32 . 1 23 . 13 VAL CA C 60.15 . 1 24 . 13 VAL CB C 30.34 . 1 25 . 15 GLN N N 123.91 . 1 26 . 15 GLN H H 8.34 . 1 27 . 15 GLN CA C 56.57 . 1 28 . 15 GLN CB C 27.87 . 1 29 . 15 GLN C C 178.91 . 1 30 . 16 SER N N 111.39 . 1 31 . 16 SER H H 7.54 . 1 32 . 16 SER CA C 55.94 . 1 33 . 16 SER CB C 64.31 . 1 34 . 16 SER C C 171.81 . 1 35 . 17 PHE N N 119.38 . 1 36 . 17 PHE H H 8.30 . 1 37 . 17 PHE CA C 59.33 . 1 38 . 17 PHE CB C 39.26 . 1 39 . 17 PHE C C 175.19 . 1 40 . 18 GLN N N 124.38 . 1 41 . 18 GLN H H 6.70 . 1 42 . 18 GLN CA C 53.13 . 1 43 . 18 GLN CB C 33.05 . 1 44 . 18 GLN C C 172.03 . 1 45 . 19 VAL N N 119.53 . 1 46 . 19 VAL H H 7.84 . 1 47 . 19 VAL CA C 60.00 . 1 48 . 19 VAL CB C 31.77 . 1 49 . 19 VAL C C 175.23 . 1 50 . 20 ALA N N 129.75 . 1 51 . 20 ALA H H 9.21 . 1 52 . 20 ALA CA C 49.13 . 1 53 . 20 ALA CB C 21.95 . 1 54 . 20 ALA C C 175.04 . 1 55 . 21 HIS N N 119.64 . 1 56 . 21 HIS H H 8.59 . 1 57 . 21 HIS CA C 55.02 . 1 58 . 21 HIS CB C 31.64 . 1 59 . 21 HIS C C 174.46 . 1 60 . 22 LEU N N 124.67 . 1 61 . 22 LEU H H 8.50 . 1 62 . 22 LEU CA C 53.04 . 1 63 . 22 LEU CB C 44.66 . 1 64 . 22 LEU C C 173.59 . 1 65 . 23 HIS N N 127.54 . 1 66 . 23 HIS H H 8.71 . 1 67 . 23 HIS CA C 53.42 . 1 68 . 23 HIS CB C 29.70 . 1 69 . 23 HIS C C 174.18 . 1 70 . 24 ALA N N 127.20 . 1 71 . 24 ALA H H 8.39 . 1 72 . 24 ALA CA C 48.81 . 1 73 . 24 ALA CB C 19.42 . 1 74 . 32 THR N N 109.18 . 1 75 . 32 THR H H 7.48 . 1 76 . 32 THR CA C 60.67 . 1 77 . 32 THR C C 173.12 . 1 78 . 33 LYS N N 123.64 . 1 79 . 33 LYS H H 8.13 . 1 80 . 33 LYS CA C 58.81 . 1 81 . 33 LYS CB C 32.09 . 1 82 . 33 LYS C C 178.59 . 1 83 . 34 VAL N N 115.88 . 1 84 . 34 VAL H H 7.79 . 1 85 . 34 VAL CA C 67.10 . 1 86 . 34 VAL CB C 27.89 . 1 87 . 35 PRO CA C 65.15 . 1 88 . 35 PRO CB C 29.14 . 1 89 . 35 PRO C C 177.49 . 1 90 . 36 ALA N N 116.10 . 1 91 . 36 ALA H H 7.33 . 1 92 . 36 ALA CA C 54.42 . 1 93 . 36 ALA CB C 16.02 . 1 94 . 36 ALA C C 179.66 . 1 95 . 37 ALA N N 121.58 . 1 96 . 37 ALA H H 7.83 . 1 97 . 37 ALA CA C 53.70 . 1 98 . 37 ALA CB C 16.59 . 1 99 . 37 ALA C C 181.31 . 1 100 . 38 TYR N N 116.21 . 1 101 . 38 TYR H H 7.58 . 1 102 . 38 TYR CA C 59.11 . 1 103 . 38 TYR CB C 37.71 . 1 104 . 38 TYR C C 179.44 . 1 105 . 39 ALA N N 122.58 . 1 106 . 39 ALA H H 8.57 . 1 107 . 39 ALA CA C 53.48 . 1 108 . 39 ALA CB C 16.72 . 1 109 . 39 ALA C C 182.19 . 1 110 . 40 ALA N N 121.68 . 1 111 . 40 ALA H H 8.05 . 1 112 . 40 ALA CA C 53.60 . 1 113 . 40 ALA CB C 16.77 . 1 114 . 40 ALA C C 178.99 . 1 115 . 41 GLN N N 114.54 . 1 116 . 41 GLN H H 7.32 . 1 117 . 41 GLN CA C 55.00 . 1 118 . 41 GLN CB C 29.04 . 1 119 . 41 GLN C C 175.63 . 1 120 . 42 GLY N N 104.92 . 1 121 . 42 GLY H H 7.74 . 1 122 . 42 GLY CA C 44.20 . 1 123 . 42 GLY C C 174.06 . 1 124 . 43 TYR N N 117.74 . 1 125 . 43 TYR H H 7.07 . 1 126 . 43 TYR CA C 56.97 . 1 127 . 43 TYR CB C 39.08 . 1 128 . 43 TYR C C 174.60 . 1 129 . 44 LYS N N 120.51 . 1 130 . 44 LYS H H 9.71 . 1 131 . 44 LYS CA C 55.13 . 1 132 . 44 LYS CB C 31.93 . 1 133 . 44 LYS C C 171.97 . 1 134 . 45 VAL N N 125.14 . 1 135 . 45 VAL H H 8.97 . 1 136 . 45 VAL CA C 59.83 . 1 137 . 45 VAL CB C 34.93 . 1 138 . 45 VAL C C 172.25 . 1 139 . 46 LEU N N 129.34 . 1 140 . 46 LEU H H 8.37 . 1 141 . 46 LEU CA C 51.52 . 1 142 . 46 LEU CB C 41.77 . 1 143 . 46 LEU C C 173.88 . 1 144 . 47 VAL N N 126.21 . 1 145 . 47 VAL H H 8.87 . 1 146 . 47 VAL CA C 59.83 . 1 147 . 47 VAL CB C 31.26 . 1 148 . 47 VAL C C 174.74 . 1 149 . 48 LEU N N 126.51 . 1 150 . 48 LEU H H 8.73 . 1 151 . 48 LEU CA C 51.46 . 1 152 . 48 LEU CB C 43.40 . 1 153 . 48 LEU C C 174.54 . 1 154 . 49 ASN N N 117.17 . 1 155 . 49 ASN H H 7.63 . 1 156 . 49 ASN CA C 50.25 . 1 157 . 49 ASN CB C 43.41 . 1 158 . 50 PRO CA C 64.34 . 1 159 . 50 PRO CB C 32.09 . 1 160 . 50 PRO C C 177.28 . 1 161 . 51 SER N N 110.02 . 1 162 . 51 SER H H 8.73 . 1 163 . 51 SER CA C 55.47 . 1 164 . 51 SER CB C 63.60 . 1 165 . 52 VAL CA C 66.13 . 1 166 . 52 VAL C C 176.64 . 1 167 . 53 ALA N N 120.54 . 1 168 . 53 ALA H H 8.20 . 1 169 . 53 ALA CA C 54.42 . 1 170 . 53 ALA CB C 17.12 . 1 171 . 53 ALA C C 181.29 . 1 172 . 54 ALA N N 120.22 . 1 173 . 54 ALA H H 7.99 . 1 174 . 54 ALA CA C 53.51 . 1 175 . 54 ALA CB C 16.35 . 1 176 . 54 ALA C C 178.70 . 1 177 . 55 THR N N 115.14 . 1 178 . 55 THR H H 7.49 . 1 179 . 55 THR CA C 67.37 . 1 180 . 55 THR C C 175.60 . 1 181 . 56 LEU N N 116.81 . 1 182 . 56 LEU H H 8.20 . 1 183 . 56 LEU CA C 56.82 . 1 184 . 56 LEU CB C 39.99 . 1 185 . 56 LEU C C 180.98 . 1 186 . 57 GLY N N 107.20 . 1 187 . 57 GLY H H 7.89 . 1 188 . 57 GLY CA C 45.77 . 1 189 . 57 GLY C C 176.71 . 1 190 . 58 PHE N N 121.69 . 1 191 . 58 PHE H H 8.17 . 1 192 . 58 PHE CA C 59.04 . 1 193 . 58 PHE CB C 37.03 . 1 194 . 58 PHE C C 178.59 . 1 195 . 59 GLY N N 103.80 . 1 196 . 59 GLY H H 7.46 . 1 197 . 59 GLY CA C 47.23 . 1 198 . 59 GLY C C 175.08 . 1 199 . 60 ALA N N 122.67 . 1 200 . 60 ALA H H 7.77 . 1 201 . 60 ALA CA C 53.96 . 1 202 . 60 ALA CB C 17.36 . 1 203 . 60 ALA C C 180.25 . 1 204 . 61 TYR N N 118.35 . 1 205 . 61 TYR H H 8.01 . 1 206 . 61 TYR CA C 60.79 . 1 207 . 61 TYR CB C 37.72 . 1 208 . 62 MET N N 117.19 . 1 209 . 62 MET H H 8.56 . 1 210 . 62 MET CA C 57.02 . 1 211 . 62 MET CB C 29.92 . 1 212 . 62 MET C C 179.32 . 1 213 . 63 SER N N 115.21 . 1 214 . 63 SER H H 7.70 . 1 215 . 63 SER CA C 60.96 . 1 216 . 63 SER CB C 62.65 . 1 217 . 63 SER C C 177.09 . 1 218 . 64 LYS N N 119.07 . 1 219 . 64 LYS H H 7.40 . 1 220 . 64 LYS CA C 57.29 . 1 221 . 64 LYS CB C 31.78 . 1 222 . 64 LYS C C 177.86 . 1 223 . 65 ALA N N 118.47 . 1 224 . 65 ALA H H 8.48 . 1 225 . 65 ALA CA C 52.72 . 1 226 . 65 ALA CB C 18.62 . 1 227 . 65 ALA C C 175.68 . 1 228 . 66 HIS N N 111.39 . 1 229 . 66 HIS H H 7.54 . 1 230 . 66 HIS CA C 54.69 . 1 231 . 66 HIS CB C 30.79 . 1 232 . 66 HIS C C 175.69 . 1 233 . 67 GLY N N 108.65 . 1 234 . 67 GLY H H 7.41 . 1 235 . 67 GLY CA C 46.23 . 1 236 . 67 GLY C C 173.81 . 1 237 . 68 VAL N N 118.01 . 1 238 . 68 VAL H H 7.13 . 1 239 . 68 VAL CA C 59.42 . 1 240 . 68 VAL CB C 34.11 . 1 241 . 68 VAL C C 172.75 . 1 242 . 69 ASP N N 124.85 . 1 243 . 69 ASP H H 8.26 . 1 244 . 69 ASP CA C 49.59 . 1 245 . 69 ASP CB C 40.11 . 1 246 . 70 PRO CA C 61.22 . 1 247 . 70 PRO CB C 31.53 . 1 248 . 70 PRO C C 176.01 . 1 249 . 71 ASN N N 122.84 . 1 250 . 71 ASN H H 9.28 . 1 251 . 71 ASN CA C 53.23 . 1 252 . 71 ASN CB C 38.56 . 1 253 . 71 ASN C C 175.70 . 1 254 . 72 ILE N N 124.91 . 1 255 . 72 ILE H H 9.40 . 1 256 . 72 ILE CA C 58.70 . 1 257 . 72 ILE CB C 39.77 . 1 258 . 72 ILE C C 175.62 . 1 259 . 73 ARG N N 111.59 . 1 260 . 73 ARG H H 7.75 . 1 261 . 73 ARG CA C 54.82 . 1 262 . 73 ARG CB C 30.25 . 1 263 . 73 ARG C C 173.73 . 1 264 . 74 THR N N 115.87 . 1 265 . 74 THR H H 7.79 . 1 266 . 74 THR CA C 59.16 . 1 267 . 74 THR CB C 72.73 . 1 268 . 75 GLY CA C 45.73 . 1 269 . 76 VAL N N 111.97 . 1 270 . 76 VAL H H 7.28 . 1 271 . 76 VAL CA C 61.37 . 1 272 . 76 VAL CB C 31.81 . 1 273 . 76 VAL C C 175.48 . 1 274 . 77 ARG N N 119.53 . 1 275 . 77 ARG H H 7.22 . 1 276 . 77 ARG CA C 55.80 . 1 277 . 77 ARG CB C 31.25 . 1 278 . 78 THR CA C 60.51 . 1 279 . 78 THR CB C 70.23 . 1 280 . 78 THR C C 173.32 . 1 281 . 79 ILE N N 127.11 . 1 282 . 79 ILE H H 9.69 . 1 283 . 79 ILE CA C 59.99 . 1 284 . 79 ILE CB C 40.23 . 1 285 . 80 THR CA C 59.83 . 1 286 . 80 THR CB C 68.53 . 1 287 . 80 THR C C 174.59 . 1 288 . 81 THR N N 116.87 . 1 289 . 81 THR H H 9.27 . 1 290 . 81 THR CA C 59.80 . 1 291 . 81 THR CB C 69.23 . 1 292 . 81 THR C C 176.51 . 1 293 . 82 GLY N N 109.96 . 1 294 . 82 GLY H H 8.41 . 1 295 . 82 GLY CA C 44.31 . 1 296 . 82 GLY C C 174.06 . 1 297 . 83 SER N N 114.88 . 1 298 . 83 SER H H 7.53 . 1 299 . 83 SER CA C 55.49 . 1 300 . 83 SER CB C 64.02 . 1 301 . 84 PRO CA C 63.46 . 1 302 . 84 PRO CB C 31.39 . 1 303 . 84 PRO C C 175.89 . 1 304 . 85 ILE N N 119.26 . 1 305 . 85 ILE H H 8.01 . 1 306 . 85 ILE CA C 59.60 . 1 307 . 85 ILE CB C 39.23 . 1 308 . 85 ILE C C 174.63 . 1 309 . 86 THR N N 123.93 . 1 310 . 86 THR H H 8.92 . 1 311 . 86 THR CA C 60.17 . 1 312 . 86 THR CB C 69.93 . 1 313 . 86 THR C C 178.11 . 1 314 . 87 TYR N N 125.14 . 1 315 . 87 TYR H H 8.97 . 1 316 . 87 TYR CA C 56.47 . 1 317 . 87 TYR CB C 39.23 . 1 318 . 87 TYR C C 174.77 . 1 319 . 88 SER N N 114.69 . 1 320 . 88 SER H H 8.98 . 1 321 . 88 SER CA C 53.82 . 1 322 . 88 SER CB C 65.01 . 1 323 . 88 SER C C 174.59 . 1 324 . 89 THR N N 112.40 . 1 325 . 89 THR H H 7.56 . 1 326 . 89 THR CA C 59.17 . 1 327 . 89 THR CB C 68.93 . 1 328 . 89 THR C C 179.12 . 1 329 . 90 TYR N N 120.90 . 1 330 . 90 TYR H H 7.53 . 1 331 . 90 TYR CA C 63.11 . 1 332 . 90 TYR CB C 37.11 . 1 333 . 90 TYR C C 178.33 . 1 334 . 91 GLY N N 104.30 . 1 335 . 91 GLY H H 9.24 . 1 336 . 91 GLY CA C 46.90 . 1 337 . 91 GLY C C 176.31 . 1 338 . 92 LYS N N 124.35 . 1 339 . 92 LYS H H 8.09 . 1 340 . 92 LYS CA C 56.10 . 1 341 . 92 LYS CB C 31.10 . 1 342 . 92 LYS C C 176.64 . 1 343 . 93 PHE N N 119.80 . 1 344 . 93 PHE H H 7.64 . 1 345 . 93 PHE CA C 59.63 . 1 346 . 93 PHE CB C 38.60 . 1 347 . 93 PHE C C 178.25 . 1 348 . 94 LEU N N 118.93 . 1 349 . 94 LEU H H 8.06 . 1 350 . 94 LEU CA C 56.88 . 1 351 . 94 LEU CB C 40.21 . 1 352 . 94 LEU C C 180.97 . 1 353 . 95 ALA N N 124.46 . 1 354 . 95 ALA H H 8.01 . 1 355 . 95 ALA CA C 54.13 . 1 356 . 95 ALA CB C 16.90 . 1 357 . 95 ALA C C 179.23 . 1 358 . 96 ASP N N 116.55 . 1 359 . 96 ASP H H 8.07 . 1 360 . 96 ASP CA C 54.01 . 1 361 . 96 ASP CB C 40.41 . 1 362 . 96 ASP C C 176.14 . 1 363 . 97 GLY N N 105.55 . 1 364 . 97 GLY H H 7.53 . 1 365 . 97 GLY CA C 43.90 . 1 366 . 97 GLY C C 175.13 . 1 367 . 98 GLY N N 109.45 . 1 368 . 98 GLY H H 7.91 . 1 369 . 98 GLY CA C 43.81 . 1 370 . 98 GLY C C 175.69 . 1 371 . 99 CYS N N 123.44 . 1 372 . 99 CYS H H 8.97 . 1 373 . 99 CYS CA C 60.97 . 1 374 . 99 CYS CB C 27.37 . 1 375 . 99 CYS C C 174.77 . 1 376 . 100 SER N N 115.06 . 1 377 . 100 SER H H 7.98 . 1 378 . 100 SER CA C 58.28 . 1 379 . 100 SER CB C 62.51 . 1 380 . 100 SER C C 175.32 . 1 381 . 101 GLY N N 110.51 . 1 382 . 101 GLY H H 8.26 . 1 383 . 101 GLY CA C 45.55 . 1 384 . 101 GLY C C 174.75 . 1 385 . 102 GLY N N 109.61 . 1 386 . 102 GLY H H 7.97 . 1 387 . 102 GLY CA C 44.76 . 1 388 . 102 GLY C C 172.38 . 1 389 . 103 ALA N N 121.93 . 1 390 . 103 ALA H H 7.43 . 1 391 . 103 ALA CA C 51.83 . 1 392 . 103 ALA CB C 18.32 . 1 393 . 103 ALA C C 175.98 . 1 394 . 104 TYR N N 114.03 . 1 395 . 104 TYR H H 7.67 . 1 396 . 104 TYR CA C 55.85 . 1 397 . 104 TYR CB C 40.23 . 1 398 . 104 TYR C C 175.12 . 1 399 . 105 ASP N N 119.31 . 1 400 . 105 ASP H H 8.49 . 1 401 . 105 ASP CA C 56.01 . 1 402 . 105 ASP CB C 43.45 . 1 403 . 105 ASP C C 175.61 . 1 404 . 106 ILE N N 118.35 . 1 405 . 106 ILE H H 8.01 . 1 406 . 106 ILE CA C 57.85 . 1 407 . 106 ILE CB C 40.89 . 1 408 . 106 ILE C C 174.31 . 1 409 . 107 ILE N N 124.85 . 1 410 . 107 ILE H H 8.26 . 1 411 . 107 ILE CA C 59.25 . 1 412 . 107 ILE CB C 40.13 . 1 413 . 107 ILE C C 174.10 . 1 414 . 108 ILE N N 127.19 . 1 415 . 108 ILE H H 9.61 . 1 416 . 108 ILE CA C 59.26 . 1 417 . 108 ILE CB C 37.72 . 1 418 . 108 ILE C C 174.57 . 1 419 . 109 CYS N N 126.48 . 1 420 . 109 CYS H H 9.36 . 1 421 . 109 CYS CA C 57.90 . 1 422 . 109 CYS CB C 26.61 . 1 423 . 109 CYS C C 173.54 . 1 424 . 110 ASP N N 123.90 . 1 425 . 110 ASP H H 8.68 . 1 426 . 110 ASP CA C 52.39 . 1 427 . 110 ASP CB C 41.98 . 1 428 . 110 ASP C C 177.40 . 1 429 . 111 GLU N N 119.40 . 1 430 . 111 GLU H H 8.52 . 1 431 . 111 GLU CA C 55.74 . 1 432 . 111 GLU CB C 25.54 . 1 433 . 111 GLU C C 178.40 . 1 434 . 112 CYS N N 113.11 . 1 435 . 112 CYS H H 8.61 . 1 436 . 112 CYS CA C 59.84 . 1 437 . 112 CYS CB C 25.93 . 1 438 . 112 CYS C C 174.23 . 1 439 . 113 HIS N N 120.58 . 1 440 . 113 HIS H H 8.49 . 1 441 . 113 HIS CA C 55.15 . 1 442 . 113 HIS CB C 29.14 . 1 443 . 113 HIS C C 175.54 . 1 444 . 114 SER N N 116.92 . 1 445 . 114 SER H H 7.71 . 1 446 . 114 SER CA C 59.21 . 1 447 . 114 SER CB C 63.57 . 1 448 . 114 SER C C 174.62 . 1 449 . 115 THR N N 112.10 . 1 450 . 115 THR H H 8.38 . 1 451 . 115 THR CA C 60.25 . 1 452 . 115 THR CB C 68.13 . 1 453 . 115 THR C C 174.71 . 1 454 . 116 ASP N N 121.58 . 1 455 . 116 ASP H H 7.83 . 1 456 . 116 ASP CA C 53.70 . 1 457 . 116 ASP CB C 41.04 . 1 458 . 116 ASP C C 176.10 . 1 459 . 117 ALA N N 125.27 . 1 460 . 117 ALA H H 8.79 . 1 461 . 117 ALA CA C 55.02 . 1 462 . 117 ALA CB C 16.98 . 1 463 . 117 ALA C C 180.24 . 1 464 . 118 THR N N 113.40 . 1 465 . 118 THR H H 8.20 . 1 466 . 118 THR CA C 65.88 . 1 467 . 118 THR CB C 66.96 . 1 468 . 118 THR C C 176.23 . 1 469 . 119 SER N N 120.56 . 1 470 . 119 SER H H 7.87 . 1 471 . 119 SER CA C 61.13 . 1 472 . 119 SER CB C 61.92 . 1 473 . 119 SER C C 174.79 . 1 474 . 120 ILE N N 112.25 . 1 475 . 120 ILE H H 7.45 . 1 476 . 120 ILE CA C 63.98 . 1 477 . 120 ILE CB C 36.50 . 1 478 . 120 ILE C C 179.70 . 1 479 . 121 LEU N N 120.56 . 1 480 . 121 LEU H H 7.87 . 1 481 . 121 LEU CA C 56.29 . 1 482 . 121 LEU CB C 40.52 . 1 483 . 121 LEU C C 180.65 . 1 484 . 122 GLY N N 111.76 . 1 485 . 122 GLY H H 8.93 . 1 486 . 122 GLY CA C 47.00 . 1 487 . 122 GLY C C 173.78 . 1 488 . 123 ILE N N 122.90 . 1 489 . 123 ILE H H 8.64 . 1 490 . 123 ILE CA C 65.22 . 1 491 . 123 ILE CB C 37.33 . 1 492 . 123 ILE C C 178.10 . 1 493 . 124 GLY N N 104.61 . 1 494 . 124 GLY H H 8.10 . 1 495 . 124 GLY CA C 46.63 . 1 496 . 124 GLY C C 176.31 . 1 497 . 125 THR N N 118.25 . 1 498 . 125 THR H H 8.17 . 1 499 . 125 THR CA C 66.35 . 1 500 . 125 THR CB C 67.82 . 1 501 . 125 THR C C 175.90 . 1 502 . 126 VAL N N 122.05 . 1 503 . 126 VAL H H 8.11 . 1 504 . 126 VAL CA C 66.86 . 1 505 . 126 VAL CB C 30.68 . 1 506 . 126 VAL C C 177.94 . 1 507 . 127 LEU N N 116.03 . 1 508 . 127 LEU H H 8.41 . 1 509 . 127 LEU CA C 57.15 . 1 510 . 127 LEU CB C 39.36 . 1 511 . 127 LEU C C 179.97 . 1 512 . 128 ASP N N 117.87 . 1 513 . 128 ASP H H 8.05 . 1 514 . 128 ASP CA C 55.92 . 1 515 . 128 ASP CB C 41.63 . 1 516 . 128 ASP C C 178.34 . 1 517 . 129 GLN N N 114.34 . 1 518 . 129 GLN H H 8.01 . 1 519 . 129 GLN CA C 56.23 . 1 520 . 129 GLN CB C 30.43 . 1 521 . 129 GLN C C 178.21 . 1 522 . 130 ALA N N 121.23 . 1 523 . 130 ALA H H 8.76 . 1 524 . 130 ALA CA C 56.24 . 1 525 . 130 ALA CB C 18.12 . 1 526 . 130 ALA C C 178.12 . 1 527 . 131 GLU N N 118.06 . 1 528 . 131 GLU H H 8.45 . 1 529 . 131 GLU CA C 58.85 . 1 530 . 131 GLU CB C 26.73 . 1 531 . 131 GLU C C 181.54 . 1 532 . 132 THR N N 116.61 . 1 533 . 132 THR H H 8.31 . 1 534 . 132 THR CA C 64.31 . 1 535 . 132 THR CB C 67.59 . 1 536 . 132 THR C C 175.38 . 1 537 . 133 ALA N N 121.31 . 1 538 . 133 ALA H H 7.78 . 1 539 . 133 ALA CA C 51.66 . 1 540 . 133 ALA CB C 17.93 . 1 541 . 133 ALA C C 177.90 . 1 542 . 134 GLY N N 106.48 . 1 543 . 134 GLY H H 7.72 . 1 544 . 134 GLY CA C 44.68 . 1 545 . 134 GLY C C 174.84 . 1 546 . 135 ALA N N 122.37 . 1 547 . 135 ALA H H 7.99 . 1 548 . 135 ALA CA C 52.12 . 1 549 . 135 ALA CB C 17.46 . 1 550 . 135 ALA C C 176.73 . 1 551 . 136 ARG N N 118.34 . 1 552 . 136 ARG H H 9.29 . 1 553 . 136 ARG CA C 55.02 . 1 554 . 136 ARG CB C 30.34 . 1 555 . 136 ARG C C 175.27 . 1 556 . 137 LEU N N 116.46 . 1 557 . 137 LEU H H 7.16 . 1 558 . 137 LEU CA C 52.88 . 1 559 . 137 LEU CB C 45.37 . 1 560 . 137 LEU C C 174.26 . 1 561 . 138 VAL N N 125.33 . 1 562 . 138 VAL H H 7.84 . 1 563 . 138 VAL CA C 58.83 . 1 564 . 138 VAL CB C 33.41 . 1 565 . 138 VAL C C 173.84 . 1 566 . 139 VAL N N 125.33 . 1 567 . 139 VAL H H 9.03 . 1 568 . 139 VAL CA C 58.89 . 1 569 . 139 VAL CB C 32.94 . 1 570 . 139 VAL C C 174.33 . 1 571 . 140 LEU N N 129.06 . 1 572 . 140 LEU H H 8.92 . 1 573 . 140 LEU CA C 53.20 . 1 574 . 140 LEU CB C 39.17 . 1 575 . 140 LEU C C 174.96 . 1 576 . 141 ALA N N 129.40 . 1 577 . 141 ALA H H 8.61 . 1 578 . 141 ALA CA C 49.83 . 1 579 . 141 ALA CB C 20.96 . 1 580 . 141 ALA C C 175.56 . 1 581 . 142 THR N N 115.14 . 1 582 . 142 THR H H 8.50 . 1 583 . 142 THR CA C 59.58 . 1 584 . 142 THR CB C 68.55 . 1 585 . 142 THR C C 172.07 . 1 586 . 143 ALA N N 127.20 . 1 587 . 143 ALA H H 8.39 . 1 588 . 143 ALA CA C 50.97 . 1 589 . 143 ALA CB C 19.42 . 1 590 . 143 ALA C C 177.37 . 1 591 . 144 THR N N 117.95 . 1 592 . 144 THR H H 7.74 . 1 593 . 144 THR CA C 62.22 . 1 594 . 144 THR CB C 69.13 . 1 stop_ save_