data_6535 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 'Backbone 1H and 15N Chemical Shift Assignments for T antigen origin binding domain in the presence of RPA32C' ; _BMRB_accession_number 6535 _BMRB_flat_file_name bmr6535.str _Entry_type original _Submission_date 2005-03-04 _Accession_date 2005-03-07 _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 Arunkumar Alphonse I. . 2 Chazin Walter J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 3 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 222 "15N chemical shifts" 222 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-09-28 original author . stop_ _Original_release_date 2005-09-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Insights into hRPA32 C-terminal domain-mediated assembly of the simian virus 40 replisome.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15793585 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Arunkumar Alphonse I. . 2 Klimovich Vitaly . . 3 Jiang Xiaohua . . 4 Ott Robert D. . 5 Mizoue Laura . . 6 Fanning Ellen . . 7 Chazin Walter J. . stop_ _Journal_abbreviation 'Nat. Struct. Mol. Biol.' _Journal_volume 12 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 332 _Page_last 339 _Year 2005 _Details . loop_ _Keyword 'DNA replication' NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Tag-OBD (131-259) - RPA32C complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Tag-OBD $Tag-OBD RPA32C $RPA32C stop_ _System_molecular_weight 26000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'DNA replication, recombination and repair' stop_ _Database_query_date . _Details 'T antigen origin binding domain in complex with RPA32 C-terminal domain' save_ ######################## # Monomeric polymers # ######################## save_Tag-OBD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Tag-OBD _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 131 _Mol_residue_sequence ; GSKVEDPKDFPSELLSFLSH AVFSNRTLACFAIYTTKEKA ALLYKKIMEKYSVTFISRHN SYNHNILFFLTPHRHRVSAI NNYAQKLCTFSFLICKGVNK EYLMYSALTRDPFSVIEESL PGGLKEHDFNP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 129 GLY 2 130 SER 3 131 LYS 4 132 VAL 5 133 GLU 6 134 ASP 7 135 PRO 8 136 LYS 9 137 ASP 10 138 PHE 11 139 PRO 12 140 SER 13 141 GLU 14 142 LEU 15 143 LEU 16 144 SER 17 145 PHE 18 146 LEU 19 147 SER 20 148 HIS 21 149 ALA 22 150 VAL 23 151 PHE 24 152 SER 25 153 ASN 26 154 ARG 27 155 THR 28 156 LEU 29 157 ALA 30 158 CYS 31 159 PHE 32 160 ALA 33 161 ILE 34 162 TYR 35 163 THR 36 164 THR 37 165 LYS 38 166 GLU 39 167 LYS 40 168 ALA 41 169 ALA 42 170 LEU 43 171 LEU 44 172 TYR 45 173 LYS 46 174 LYS 47 175 ILE 48 176 MET 49 177 GLU 50 178 LYS 51 179 TYR 52 180 SER 53 181 VAL 54 182 THR 55 183 PHE 56 184 ILE 57 185 SER 58 186 ARG 59 187 HIS 60 188 ASN 61 189 SER 62 190 TYR 63 191 ASN 64 192 HIS 65 193 ASN 66 194 ILE 67 195 LEU 68 196 PHE 69 197 PHE 70 198 LEU 71 199 THR 72 200 PRO 73 201 HIS 74 202 ARG 75 203 HIS 76 204 ARG 77 205 VAL 78 206 SER 79 207 ALA 80 208 ILE 81 209 ASN 82 210 ASN 83 211 TYR 84 212 ALA 85 213 GLN 86 214 LYS 87 215 LEU 88 216 CYS 89 217 THR 90 218 PHE 91 219 SER 92 220 PHE 93 221 LEU 94 222 ILE 95 223 CYS 96 224 LYS 97 225 GLY 98 226 VAL 99 227 ASN 100 228 LYS 101 229 GLU 102 230 TYR 103 231 LEU 104 232 MET 105 233 TYR 106 234 SER 107 235 ALA 108 236 LEU 109 237 THR 110 238 ARG 111 239 ASP 112 240 PRO 113 241 PHE 114 242 SER 115 243 VAL 116 244 ILE 117 245 GLU 118 246 GLU 119 247 SER 120 248 LEU 121 249 PRO 122 250 GLY 123 251 GLY 124 252 LEU 125 253 LYS 126 254 GLU 127 255 HIS 128 256 ASP 129 257 PHE 130 258 ASN 131 259 PRO 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 17060 RPA32C 100.00 97 100.00 100.00 1.88e-42 BMRB 4460 RPA32(172-270) 100.00 103 100.00 100.00 1.85e-42 PDB 1DPU "Solution Structure Of The C-Terminal Domain Of Human Rpa32 Complexed With Ung2(73-88)" 100.00 99 100.00 100.00 1.58e-42 PDB 1Z1D "Structural Model For The Interaction Between Rpa32 C- Terminal Domain And Sv40 T Antigen Origin Binding Domain" 100.00 103 100.00 100.00 1.85e-42 PDB 2PI2 "Full-Length Replication Protein A Subunits Rpa14 And Rpa32" 100.00 270 100.00 100.00 5.62e-41 PDB 2Z6K "Crystal Structure Of Full-Length Human Rpa1432 HETERODIMER" 100.00 270 100.00 100.00 5.62e-41 PDB 4MQV "Crystal Complex Of Rpa32c And Smarcal1 N-terminus" 100.00 69 100.00 100.00 1.41e-42 PDB 4OU0 "Crystal Structure Of Rpa32c" 100.00 73 98.55 98.55 5.32e-41 DBJ BAG35795 "unnamed protein product [Homo sapiens]" 100.00 270 100.00 100.00 5.99e-41 DBJ BAG59456 "unnamed protein product [Homo sapiens]" 100.00 104 100.00 100.00 1.60e-42 DBJ BAG60901 "unnamed protein product [Homo sapiens]" 100.00 264 100.00 100.00 4.47e-41 DBJ BAG62374 "unnamed protein product [Homo sapiens]" 100.00 174 100.00 100.00 6.59e-42 DBJ BAI47325 "replication protein A2, 32kDa [synthetic construct]" 100.00 270 100.00 100.00 5.62e-41 EMBL CAG29344 "RPA2 [Homo sapiens]" 100.00 270 100.00 100.00 5.62e-41 EMBL CAH90667 "hypothetical protein [Pongo abelii]" 100.00 270 97.10 100.00 3.17e-40 GB AAA36560 "replication protein A [Homo sapiens]" 100.00 270 100.00 100.00 5.62e-41 GB AAH01630 "Replication protein A2, 32kDa [Homo sapiens]" 100.00 270 100.00 100.00 5.62e-41 GB AAH12157 "Replication protein A2, 32kDa [Homo sapiens]" 100.00 270 100.00 100.00 5.62e-41 GB AAH21257 "Replication protein A2, 32kDa [Homo sapiens]" 100.00 270 100.00 100.00 5.62e-41 GB AAX84514 "replication protein A2, 32kDa [Homo sapiens]" 100.00 270 100.00 100.00 5.62e-41 REF NP_001125362 "replication protein A 32 kDa subunit [Pongo abelii]" 100.00 343 97.10 100.00 2.55e-38 REF NP_001231871 "replication protein A 32 kDa subunit [Sus scrofa]" 100.00 270 97.10 100.00 6.77e-40 REF NP_001247563 "replication protein A 32 kDa subunit [Macaca mulatta]" 100.00 270 100.00 100.00 5.68e-41 REF NP_001273005 "replication protein A 32 kDa subunit isoform 2 [Homo sapiens]" 100.00 174 100.00 100.00 6.59e-42 REF NP_001284487 "replication protein A 32 kDa subunit isoform 3 [Homo sapiens]" 100.00 278 100.00 100.00 6.70e-41 SP P15927 "RecName: Full=Replication protein A 32 kDa subunit; Short=RP-A p32; AltName: Full=Replication factor A protein 2; Short=RF-A pr" 100.00 270 100.00 100.00 5.62e-41 SP Q5RC43 "RecName: Full=Replication protein A 32 kDa subunit; Short=RP-A p32; AltName: Full=Replication factor A protein 2; Short=RF-A pr" 100.00 270 97.10 100.00 3.17e-40 stop_ save_ save_RPA32C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'RPA32 C-terminal domain' _Molecular_mass . _Mol_thiol_state 'all free' _Details . _Residue_count 103 _Mol_residue_sequence ; ANGLTVAQNQVLNLIKACPR PEGLNFQDLKNQLKHMSVSS IKQAVDFLSNEGHIYSTVDD DHFKSTDAE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 202 ALA 2 203 ASN 3 204 GLY 4 205 LEU 5 206 THR 6 207 VAL 7 208 ALA 8 209 GLN 9 210 ASN 10 211 GLN 11 212 VAL 12 213 LEU 13 214 ASN 14 215 LEU 15 216 ILE 16 217 LYS 17 218 ALA 18 219 CYS 19 220 PRO 20 221 ARG 21 222 PRO 22 223 GLU 23 224 GLY 24 225 LEU 25 226 ASN 26 227 PHE 27 228 GLN 28 229 ASP 29 230 LEU 30 231 LYS 31 232 ASN 32 233 GLN 33 234 LEU 34 235 LYS 35 236 HIS 36 237 MET 37 238 SER 38 239 VAL 39 240 SER 40 241 SER 41 242 ILE 42 243 LYS 43 244 GLN 44 245 ALA 45 246 VAL 46 247 ASP 47 248 PHE 48 249 LEU 49 250 SER 50 251 ASN 51 252 GLU 52 253 GLY 53 254 HIS 54 255 ILE 55 256 TYR 56 257 SER 57 258 THR 58 259 VAL 59 260 ASP 60 261 ASP 61 262 ASP 62 263 HIS 63 264 PHE 64 265 LYS 65 266 SER 66 267 THR 67 268 ASP 68 269 ALA 69 270 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Tag-OBD 'Simian viurs40' . Viruses . 'Simian viurs40' 'Simian virus40' $RPA32C 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_name $Tag-OBD 'recombinant technology' . . . . . $RPA32C '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 _Isotopic_labeling $Tag-OBD 0.2 mM [U-15N] $RPA32C 0.6 mM unlabeled Tris 20 mM 2H MgCl2 5 mM . DTT 2 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tag-OBD 0.2 mM unlabeled $RPA32C 0.6 mM [U-15N] Tris 20 mM 2H MgCl2 5 mM . DTT 2 mM . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version . loop_ _Vendor _Address _Electronic_address 'Accelrys Inc' . . stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_with_cryoprobe _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_HSQC _Sample_label . save_ save_1H15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.02 pH temperature 298 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 internal indirect . . . 0.10132905 $entry_citation $entry_citation 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_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 1H15N_HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name Tag-OBD _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 . 3 LYS H H 8.454 0.02 1 2 . 3 LYS N N 119.62 0.03 1 3 . 4 VAL H H 8.299 0.02 1 4 . 4 VAL N N 119.16 0.03 1 5 . 5 GLU H H 8.480 0.02 1 6 . 5 GLU N N 121.58 0.03 1 7 . 6 ASP H H 8.332 0.02 1 8 . 6 ASP N N 119.92 0.03 1 9 . 8 LYS H H 8.491 0.02 1 10 . 8 LYS N N 113.66 0.03 1 11 . 9 ASP H H 7.789 0.02 1 12 . 9 ASP N N 112.98 0.03 1 13 . 10 PHE H H 10.390 0.02 1 14 . 10 PHE N N 115.59 0.03 1 15 . 12 SER H H 8.463 0.02 1 16 . 12 SER N N 115.24 0.03 1 17 . 13 GLU H H 10.870 0.02 1 18 . 13 GLU N N 117.48 0.03 1 19 . 15 LEU H H 6.981 0.02 1 20 . 15 LEU N N 111.93 0.03 1 21 . 17 PHE H H 7.155 0.02 1 22 . 17 PHE N N 114.51 0.03 1 23 . 18 LEU H H 7.067 0.02 1 24 . 18 LEU N N 114.24 0.03 1 25 . 19 SER H H 8.081 0.02 1 26 . 19 SER N N 108.19 0.03 1 27 . 21 ALA H H 7.564 0.02 1 28 . 21 ALA N N 121.08 0.03 1 29 . 22 VAL H H 8.446 0.02 1 30 . 22 VAL N N 116.32 0.03 1 31 . 23 PHE H H 8.305 0.02 1 32 . 23 PHE N N 116.29 0.03 1 33 . 24 SER H H 7.646 0.02 1 34 . 24 SER N N 111.76 0.03 1 35 . 26 ARG H H 8.134 0.02 1 36 . 26 ARG N N 117.24 0.03 1 37 . 27 THR H H 8.436 0.02 1 38 . 27 THR N N 111.00 0.03 1 39 . 28 LEU H H 8.915 0.02 1 40 . 28 LEU N N 118.67 0.03 1 41 . 29 ALA H H 8.768 0.02 1 42 . 29 ALA N N 116.27 0.03 1 43 . 30 CYS H H 6.152 0.02 1 44 . 30 CYS N N 115.46 0.03 1 45 . 31 PHE H H 8.025 0.02 1 46 . 31 PHE N N 120.71 0.03 1 47 . 32 ALA H H 8.764 0.02 1 48 . 32 ALA N N 114.16 0.03 1 49 . 33 ILE H H 9.539 0.02 1 50 . 33 ILE N N 116.43 0.03 1 51 . 34 TYR H H 9.489 0.02 1 52 . 34 TYR N N 127.90 0.03 1 53 . 35 THR H H 8.738 0.02 1 54 . 35 THR N N 116.08 0.03 1 55 . 36 THR H H 8.216 0.02 1 56 . 36 THR N N 106.71 0.03 1 57 . 37 LYS H H 9.682 0.02 1 58 . 37 LYS N N 117.67 0.03 1 59 . 38 GLU H H 8.841 0.02 1 60 . 38 GLU N N 113.41 0.03 1 61 . 39 LYS H H 7.419 0.02 1 62 . 39 LYS N N 112.88 0.03 1 63 . 40 ALA H H 9.183 0.02 1 64 . 40 ALA N N 119.24 0.03 1 65 . 41 ALA H H 7.978 0.02 1 66 . 41 ALA N N 115.62 0.03 1 67 . 42 LEU H H 6.929 0.02 1 68 . 42 LEU N N 114.47 0.03 1 69 . 43 LEU H H 8.829 0.02 1 70 . 43 LEU N N 114.56 0.03 1 71 . 44 TYR H H 8.213 0.02 1 72 . 44 TYR N N 116.42 0.03 1 73 . 45 LYS H H 6.862 0.02 1 74 . 45 LYS N N 108.95 0.03 1 75 . 46 LYS H H 7.746 0.02 1 76 . 46 LYS N N 113.62 0.03 1 77 . 47 ILE H H 9.374 0.02 1 78 . 47 ILE N N 115.85 0.03 1 79 . 48 MET H H 6.767 0.02 1 80 . 48 MET N N 113.49 0.03 1 81 . 49 GLU H H 7.203 0.02 1 82 . 49 GLU N N 111.54 0.03 1 83 . 51 TYR H H 7.834 0.02 1 84 . 51 TYR N N 107.49 0.03 1 85 . 52 SER H H 7.405 0.02 1 86 . 52 SER N N 110.39 0.03 1 87 . 53 VAL H H 6.403 0.02 1 88 . 53 VAL N N 101.63 0.03 1 89 . 54 THR H H 8.541 0.02 1 90 . 54 THR N N 112.15 0.03 1 91 . 55 PHE H H 7.468 0.02 1 92 . 55 PHE N N 115.39 0.03 1 93 . 56 ILE H H 7.687 0.02 1 94 . 56 ILE N N 122.55 0.03 1 95 . 57 SER H H 9.92 0.02 1 96 . 57 SER N N 114.63 0.03 1 97 . 58 ARG H H 9.145 0.02 1 98 . 58 ARG N N 117.94 0.03 1 99 . 59 HIS H H 9.808 0.02 1 100 . 59 HIS N N 120.79 0.03 1 101 . 60 ASN H H 8.976 0.02 1 102 . 60 ASN N N 118.32 0.03 1 103 . 61 SER H H 7.946 0.02 1 104 . 61 SER N N 111.17 0.03 1 105 . 62 TYR H H 9.241 0.02 1 106 . 62 TYR N N 123.12 0.03 1 107 . 63 ASN H H 8.712 0.02 1 108 . 63 ASN N N 110.40 0.03 1 109 . 64 HIS H H 8.637 0.02 1 110 . 64 HIS N N 116.81 0.03 1 111 . 65 ASN H H 9.547 0.02 1 112 . 65 ASN N N 118.09 0.03 1 113 . 66 ILE H H 8.952 0.02 1 114 . 66 ILE N N 113.81 0.03 1 115 . 67 LEU H H 10.020 0.02 1 116 . 67 LEU N N 124.36 0.03 1 117 . 68 PHE H H 9.779 0.02 1 118 . 68 PHE N N 123.55 0.03 1 119 . 70 LEU H H 8.518 0.02 1 120 . 70 LEU N N 116.53 0.03 1 121 . 71 THR H H 9.333 0.02 1 122 . 71 THR N N 109.28 0.03 1 123 . 73 HIS H H 7.050 0.02 1 124 . 73 HIS N N 112.79 0.03 1 125 . 75 HIS H H 9.421 0.02 1 126 . 75 HIS N N 113.86 0.03 1 127 . 76 ARG H H 9.217 0.02 1 128 . 76 ARG N N 117.80 0.03 1 129 . 77 VAL H H 9.288 0.02 1 130 . 77 VAL N N 121.24 0.03 1 131 . 78 SER H H 8.599 0.02 1 132 . 78 SER N N 108.05 0.03 1 133 . 79 ALA H H 7.125 0.02 1 134 . 79 ALA N N 121.61 0.03 1 135 . 81 ASN H H 8.671 0.02 1 136 . 81 ASN N N 113.43 0.03 1 137 . 82 ASN H H 8.266 0.02 1 138 . 82 ASN N N 112.19 0.03 1 139 . 83 TYR H H 7.558 0.02 1 140 . 83 TYR N N 115.47 0.03 1 141 . 84 ALA H H 8.386 0.02 1 142 . 84 ALA N N 115.40 0.03 1 143 . 85 GLN H H 8.857 0.02 1 144 . 85 GLN N N 112.08 0.03 1 145 . 86 LYS H H 7.120 0.02 1 146 . 86 LYS N N 112.81 0.03 1 147 . 87 LEU H H 6.952 0.02 1 148 . 87 LEU N N 113.15 0.03 1 149 . 88 CYS H H 7.608 0.02 1 150 . 88 CYS N N 112.57 0.03 1 151 . 93 LEU H H 8.143 0.02 1 152 . 93 LEU N N 119.85 0.03 1 153 . 94 ILE H H 8.868 0.02 1 154 . 94 ILE N N 122.88 0.03 1 155 . 95 CYS H H 8.979 0.02 1 156 . 95 CYS N N 125.15 0.03 1 157 . 96 LYS H H 9.135 0.02 1 158 . 96 LYS N N 121.26 0.03 1 159 . 97 GLY H H 9.096 0.02 1 160 . 97 GLY N N 103.03 0.03 1 161 . 98 VAL H H 7.705 0.02 1 162 . 98 VAL N N 119.10 0.03 1 163 . 99 ASN H H 8.143 0.02 1 164 . 99 ASN N N 119.02 0.03 1 165 . 100 LYS H H 7.176 0.02 1 166 . 100 LYS N N 115.74 0.03 1 167 . 101 GLU H H 9.25 0.02 1 168 . 101 GLU N N 117.40 0.03 1 169 . 102 TYR H H 8.419 0.02 1 170 . 102 TYR N N 113.68 0.03 1 171 . 103 LEU H H 7.988 0.02 1 172 . 103 LEU N N 115.13 0.03 1 173 . 104 MET H H 7.260 0.02 1 174 . 104 MET N N 113.84 0.03 1 175 . 105 TYR H H 7.356 0.02 1 176 . 105 TYR N N 113.40 0.03 1 177 . 106 SER H H 7.961 0.02 1 178 . 106 SER N N 105.48 0.03 1 179 . 107 ALA H H 7.469 0.02 1 180 . 107 ALA N N 120.08 0.03 1 181 . 108 LEU H H 7.178 0.02 1 182 . 108 LEU N N 111.46 0.03 1 183 . 110 ARG H H 7.517 0.02 1 184 . 110 ARG N N 118.51 0.03 1 185 . 111 ASP H H 8.098 0.02 1 186 . 111 ASP N N 115.97 0.03 1 187 . 113 PHE H H 9.060 0.02 1 188 . 113 PHE N N 127.39 0.03 1 189 . 114 SER H H 7.221 0.02 1 190 . 114 SER N N 102.79 0.03 1 191 . 115 VAL H H 9.160 0.02 1 192 . 115 VAL N N 118.62 0.03 1 193 . 116 ILE H H 9.351 0.02 1 194 . 116 ILE N N 124.94 0.03 1 195 . 117 GLU H H 7.335 0.02 1 196 . 117 GLU N N 110.09 0.03 1 197 . 118 GLU H H 8.368 0.02 1 198 . 118 GLU N N 112.87 0.03 1 199 . 119 SER H H 8.818 0.02 1 200 . 119 SER N N 110.91 0.03 1 201 . 120 LEU H H 6.803 0.02 1 202 . 120 LEU N N 118.88 0.03 1 203 . 122 GLY H H 9.213 0.02 1 204 . 122 GLY N N 112.13 0.03 1 205 . 123 GLY H H 8.282 0.02 1 206 . 123 GLY N N 104.15 0.03 1 207 . 124 LEU H H 5.775 0.02 1 208 . 124 LEU N N 114.39 0.03 1 209 . 126 GLU H H 8.237 0.02 1 210 . 126 GLU N N 117.37 0.03 1 211 . 127 HIS H H 7.745 0.02 1 212 . 127 HIS N N 109.59 0.03 1 213 . 128 ASP H H 7.603 0.02 1 214 . 128 ASP N N 115.57 0.03 1 215 . 129 PHE H H 7.464 0.02 1 216 . 129 PHE N N 113.39 0.03 1 stop_ save_ save_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 1H15N_HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name RPA32C _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 . 1 ALA H H 8.489 0.02 1 2 . 1 ALA N N 125.05 0.03 1 3 . 2 ASN H H 8.212 0.02 1 4 . 2 ASN N N 116.60 0.03 1 5 . 3 GLY H H 8.313 0.02 1 6 . 3 GLY N N 108.08 0.03 1 7 . 4 LEU H H 7.702 0.02 1 8 . 4 LEU N N 120.77 0.03 1 9 . 5 THR H H 8.055 0.02 1 10 . 5 THR N N 111.09 0.03 1 11 . 6 VAL H H 8.624 0.02 1 12 . 6 VAL N N 121.32 0.03 1 13 . 7 ALA H H 8.353 0.02 1 14 . 7 ALA N N 121.13 0.03 1 15 . 8 GLN H H 7.474 0.02 1 16 . 8 GLN N N 114.70 0.03 1 17 . 9 ASN H H 8.648 0.02 1 18 . 9 ASN N N 116.81 0.03 1 19 . 10 GLN H H 8.399 0.02 1 20 . 10 GLN N N 119.58 0.03 1 21 . 11 VAL H H 7.700 0.02 1 22 . 11 VAL N N 118.71 0.03 1 23 . 13 ASN H H 8.617 0.02 1 24 . 13 ASN N N 116.25 0.03 1 25 . 14 LEU H H 7.382 0.02 1 26 . 14 LEU N N 120.35 0.03 1 27 . 15 ILE H H 7.743 0.02 1 28 . 15 ILE N N 120.27 0.03 1 29 . 16 LYS H H 9.011 0.02 1 30 . 16 LYS N N 120.52 0.03 1 31 . 17 ALA H H 7.300 0.02 1 32 . 17 ALA N N 117.80 0.03 1 33 . 18 CYS H H 7.293 0.02 1 34 . 18 CYS N N 120.75 0.03 1 35 . 20 ARG H H 7.625 0.02 1 36 . 20 ARG N N 122.31 0.03 1 37 . 22 GLU H H 9.954 0.02 1 38 . 22 GLU N N 115.74 0.03 1 39 . 23 GLY H H 7.498 0.02 1 40 . 23 GLY N N 108.26 0.03 1 41 . 25 ASN H H 8.796 0.02 1 42 . 25 ASN N N 122.30 0.03 1 43 . 28 ASP H H 7.967 0.02 1 44 . 28 ASP N N 119.21 0.03 1 45 . 29 LEU H H 7.745 0.02 1 46 . 29 LEU N N 120.12 0.03 1 47 . 30 LYS H H 7.974 0.02 1 48 . 30 LYS N N 117.35 0.03 1 49 . 31 ASN H H 7.853 0.02 1 50 . 31 ASN N N 115.35 0.03 1 51 . 32 GLN H H 7.645 0.02 1 52 . 32 GLN N N 116.56 0.03 1 53 . 33 LEU H H 7.697 0.02 1 54 . 33 LEU N N 123.59 0.03 1 55 . 34 LYS H H 7.571 0.02 1 56 . 34 LYS N N 118.37 0.03 1 57 . 35 HIS H H 8.519 0.02 1 58 . 35 HIS N N 114.49 0.03 1 59 . 36 MET H H 7.607 0.02 1 60 . 36 MET N N 122.31 0.03 1 61 . 37 SER H H 8.519 0.02 1 62 . 37 SER N N 117.33 0.03 1 63 . 39 SER H H 8.413 0.02 1 64 . 39 SER N N 122.51 0.03 1 65 . 40 SER H H 7.993 0.02 1 66 . 40 SER N N 119.58 0.03 1 67 . 42 LYS H H 8.694 0.02 1 68 . 42 LYS N N 120.42 0.03 1 69 . 43 GLN H H 8.217 0.02 1 70 . 43 GLN N N 117.15 0.03 1 71 . 44 ALA H H 7.801 0.02 1 72 . 44 ALA N N 122.49 0.03 1 73 . 45 VAL H H 8.573 0.02 1 74 . 45 VAL N N 118.12 0.03 1 75 . 46 ASP H H 8.645 0.02 1 76 . 46 ASP N N 122.05 0.03 1 77 . 47 PHE H H 8.045 0.02 1 78 . 47 PHE N N 121.03 0.03 1 79 . 48 LEU H H 8.784 0.02 1 80 . 48 LEU N N 117.89 0.03 1 81 . 49 SER H H 8.605 0.02 1 82 . 49 SER N N 115.77 0.03 1 83 . 50 ASN H H 8.490 0.02 1 84 . 50 ASN N N 123.36 0.03 1 85 . 51 GLU H H 7.954 0.02 1 86 . 51 GLU N N 115.02 0.03 1 87 . 52 GLY H H 7.544 0.02 1 88 . 52 GLY N N 105.22 0.03 1 89 . 53 HIS H H 8.399 0.02 1 90 . 53 HIS N N 118.48 0.03 1 91 . 54 ILE H H 7.377 0.02 1 92 . 54 ILE N N 109.08 0.03 1 93 . 55 TYR H H 9.100 0.02 1 94 . 55 TYR N N 117.26 0.03 1 95 . 59 ASP H H 7.832 0.02 1 96 . 59 ASP N N 116.98 0.03 1 97 . 60 ASP H H 8.092 0.02 1 98 . 60 ASP N N 114.25 0.03 1 99 . 61 ASP H H 8.490 0.02 1 100 . 61 ASP N N 117.13 0.03 1 101 . 62 HIS H H 6.882 0.02 1 102 . 62 HIS N N 116.11 0.03 1 103 . 64 LYS H H 8.515 0.02 1 104 . 64 LYS N N 120.16 0.03 1 105 . 65 SER H H 8.637 0.02 1 106 . 65 SER N N 114.66 0.03 1 107 . 66 THR H H 8.231 0.02 1 108 . 66 THR N N 119.07 0.03 1 109 . 67 ASP H H 8.487 0.02 1 110 . 67 ASP N N 121.83 0.03 1 111 . 68 ALA H H 8.130 0.02 1 112 . 68 ALA N N 124.93 0.03 1 113 . 69 GLU H H 8.017 0.02 1 114 . 69 GLU N N 125.38 0.03 1 stop_ save_ save_chem_shift_list_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 1H15N_HSQC stop_ loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name RPA32C _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 . 1 ALA H H 8.489 0.02 1 2 . 1 ALA N N 125.05 0.03 1 3 . 2 ASN H H 8.212 0.02 1 4 . 2 ASN N N 116.60 0.03 1 5 . 3 GLY H H 8.313 0.02 1 6 . 3 GLY N N 108.08 0.03 1 7 . 4 LEU H H 7.702 0.02 1 8 . 4 LEU N N 120.77 0.03 1 9 . 5 THR H H 8.055 0.02 1 10 . 5 THR N N 111.09 0.03 1 11 . 6 VAL H H 8.624 0.02 1 12 . 6 VAL N N 121.32 0.03 1 13 . 7 ALA H H 8.353 0.02 1 14 . 7 ALA N N 121.13 0.03 1 15 . 8 GLN H H 7.474 0.02 1 16 . 8 GLN N N 114.70 0.03 1 17 . 9 ASN H H 8.648 0.02 1 18 . 9 ASN N N 116.81 0.03 1 19 . 10 GLN H H 8.399 0.02 1 20 . 10 GLN N N 119.58 0.03 1 21 . 11 VAL H H 7.700 0.02 1 22 . 11 VAL N N 118.71 0.03 1 23 . 13 ASN H H 8.617 0.02 1 24 . 13 ASN N N 116.25 0.03 1 25 . 14 LEU H H 7.382 0.02 1 26 . 14 LEU N N 120.35 0.03 1 27 . 15 ILE H H 7.743 0.02 1 28 . 15 ILE N N 120.27 0.03 1 29 . 16 LYS H H 9.011 0.02 1 30 . 16 LYS N N 120.52 0.03 1 31 . 17 ALA H H 7.300 0.02 1 32 . 17 ALA N N 117.80 0.03 1 33 . 18 CYS H H 7.293 0.02 1 34 . 18 CYS N N 120.75 0.03 1 35 . 20 ARG H H 7.625 0.02 1 36 . 20 ARG N N 122.31 0.03 1 37 . 22 GLU H H 9.954 0.02 1 38 . 22 GLU N N 115.74 0.03 1 39 . 23 GLY H H 7.498 0.02 1 40 . 23 GLY N N 108.26 0.03 1 41 . 25 ASN H H 8.796 0.02 1 42 . 25 ASN N N 122.30 0.03 1 43 . 28 ASP H H 7.967 0.02 1 44 . 28 ASP N N 119.21 0.03 1 45 . 29 LEU H H 7.745 0.02 1 46 . 29 LEU N N 120.12 0.03 1 47 . 30 LYS H H 7.974 0.02 1 48 . 30 LYS N N 117.35 0.03 1 49 . 31 ASN H H 7.853 0.02 1 50 . 31 ASN N N 115.35 0.03 1 51 . 32 GLN H H 7.645 0.02 1 52 . 32 GLN N N 116.56 0.03 1 53 . 33 LEU H H 7.697 0.02 1 54 . 33 LEU N N 123.59 0.03 1 55 . 34 LYS H H 7.571 0.02 1 56 . 34 LYS N N 118.37 0.03 1 57 . 35 HIS H H 8.519 0.02 1 58 . 35 HIS N N 114.49 0.03 1 59 . 36 MET H H 7.607 0.02 1 60 . 36 MET N N 122.31 0.03 1 61 . 37 SER H H 8.519 0.02 1 62 . 37 SER N N 117.33 0.03 1 63 . 39 SER H H 8.413 0.02 1 64 . 39 SER N N 122.51 0.03 1 65 . 40 SER H H 7.993 0.02 1 66 . 40 SER N N 119.58 0.03 1 67 . 42 LYS H H 8.694 0.02 1 68 . 42 LYS N N 120.42 0.03 1 69 . 43 GLN H H 8.217 0.02 1 70 . 43 GLN N N 117.15 0.03 1 71 . 44 ALA H H 7.801 0.02 1 72 . 44 ALA N N 122.49 0.03 1 73 . 45 VAL H H 8.573 0.02 1 74 . 45 VAL N N 118.12 0.03 1 75 . 46 ASP H H 8.645 0.02 1 76 . 46 ASP N N 122.05 0.03 1 77 . 47 PHE H H 8.045 0.02 1 78 . 47 PHE N N 121.03 0.03 1 79 . 48 LEU H H 8.784 0.02 1 80 . 48 LEU N N 117.89 0.03 1 81 . 49 SER H H 8.605 0.02 1 82 . 49 SER N N 115.77 0.03 1 83 . 50 ASN H H 8.490 0.02 1 84 . 50 ASN N N 123.36 0.03 1 85 . 51 GLU H H 7.954 0.02 1 86 . 51 GLU N N 115.02 0.03 1 87 . 52 GLY H H 7.544 0.02 1 88 . 52 GLY N N 105.22 0.03 1 89 . 53 HIS H H 8.399 0.02 1 90 . 53 HIS N N 118.48 0.03 1 91 . 54 ILE H H 7.377 0.02 1 92 . 54 ILE N N 109.08 0.03 1 93 . 55 TYR H H 9.100 0.02 1 94 . 55 TYR N N 117.26 0.03 1 95 . 59 ASP H H 7.832 0.02 1 96 . 59 ASP N N 116.98 0.03 1 97 . 60 ASP H H 8.092 0.02 1 98 . 60 ASP N N 114.25 0.03 1 99 . 61 ASP H H 8.490 0.02 1 100 . 61 ASP N N 117.13 0.03 1 101 . 62 HIS H H 6.882 0.02 1 102 . 62 HIS N N 116.11 0.03 1 103 . 64 LYS H H 8.515 0.02 1 104 . 64 LYS N N 120.16 0.03 1 105 . 65 SER H H 8.637 0.02 1 106 . 65 SER N N 114.66 0.03 1 107 . 66 THR H H 8.231 0.02 1 108 . 66 THR N N 119.07 0.03 1 109 . 67 ASP H H 8.487 0.02 1 110 . 67 ASP N N 121.83 0.03 1 111 . 68 ALA H H 8.130 0.02 1 112 . 68 ALA N N 124.93 0.03 1 113 . 69 GLU H H 8.017 0.02 1 114 . 69 GLU N N 125.38 0.03 1 stop_ save_