data_50115 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 13C, and 15N Chemical Shift Assignments for ChiZ N-terminal Domain ; _BMRB_accession_number 50115 _BMRB_flat_file_name bmr50115.str _Entry_type original _Submission_date 2019-12-06 _Accession_date 2019-12-06 _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 Escobar Cristian A. . 2 Cross Timothy A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count H_exch_rates 1 assigned_chemical_shifts 1 heteronucl_NOE 1 T1_relaxation 1 T2_relaxation 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 52 "13C chemical shifts" 183 "15N chemical shifts" 52 "T1 relaxation values" 50 "T2 relaxation values" 50 "H exchange rates" 50 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-06-23 original BMRB . stop_ _Original_release_date 2019-12-09 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hicks Alan . . 2 Escobar Cristian A. . 3 Cross Timothy A. . 4 Zhou Huan-Xiang . . stop_ _Journal_abbreviation Biomolecules _Journal_volume 10 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 946 _Page_last 946 _Year 2020 _Details https://www.mdpi.com/2218-273X/10/6/946/htm save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name ChiZ1-64 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'N-terminal domain' $entity_1 stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'Involved in Mycobacterium tuberculosis cell division' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 67 _Mol_residue_sequence ; SNAMTPVRPPHTPDPLNLRG PLDGPRWRRAEPAQSRRPGR SRPGGAPLRYHRTGVGMSRT GHGSRPV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 SER 2 -1 ASN 3 0 ALA 4 1 MET 5 2 THR 6 3 PRO 7 4 VAL 8 5 ARG 9 6 PRO 10 7 PRO 11 8 HIS 12 9 THR 13 10 PRO 14 11 ASP 15 12 PRO 16 13 LEU 17 14 ASN 18 15 LEU 19 16 ARG 20 17 GLY 21 18 PRO 22 19 LEU 23 20 ASP 24 21 GLY 25 22 PRO 26 23 ARG 27 24 TRP 28 25 ARG 29 26 ARG 30 27 ALA 31 28 GLU 32 29 PRO 33 30 ALA 34 31 GLN 35 32 SER 36 33 ARG 37 34 ARG 38 35 PRO 39 36 GLY 40 37 ARG 41 38 SER 42 39 ARG 43 40 PRO 44 41 GLY 45 42 GLY 46 43 ALA 47 44 PRO 48 45 LEU 49 46 ARG 50 47 TYR 51 48 HIS 52 49 ARG 53 50 THR 54 51 GLY 55 52 VAL 56 53 GLY 57 54 MET 58 55 SER 59 56 ARG 60 57 THR 61 58 GLY 62 59 HIS 63 60 GLY 64 61 SER 65 62 ARG 66 63 PRO 67 64 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 'Mycobacterium tuberculosis' 1773 Bacteria . Mycobacterium tuberculosis stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli BL21(DE3) plasmid pTBSG1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '13C-15N uniformly label ChiZ1-64 sample concentration was 1 mM at pH 7.0' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-13C; U-15N]' 'sodium phosphate' 20 mM 'natural abundance' DSS 50 uM 'natural abundance' D2O 10 '% v/v' 'natural abundance' 'sodium chloride' 25 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_software_2 _Saveframe_category software _Name CcpNMR _Version 2.4.2 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_15N-(1H)_NOE_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-(1H) NOE' _Sample_label $sample_1 save_ save_Het._Nuc._T1_relaxation_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'Het. Nuc. T1 relaxation' _Sample_label $sample_1 save_ save_Het._Nuc._T2_relaxation_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'Het. Nuc. T2 relaxation' _Sample_label $sample_1 save_ save_CLEANEX-PM_(15N-HSQC)_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'CLEANEX-PM (15N-HSQC)' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'ChiZ1-64 sample' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 45 . mM pH 7.0 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_assigned_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCO' '3D HNCACB' '3D CBCA(CO)NH' HN(CA)CO stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name 'N-terminal 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 -1 2 ASN C C 174.939 . 1 2 -1 2 ASN CA C 53.232 . 1 3 -1 2 ASN CB C 39.112 . 1 4 0 3 ALA H H 8.428 . 1 5 0 3 ALA C C 177.635 . 1 6 0 3 ALA CA C 52.819 . 1 7 0 3 ALA CB C 19.150 . 1 8 0 3 ALA N N 124.529 . 1 9 1 4 MET H H 8.391 . 1 10 1 4 MET C C 176.172 . 1 11 1 4 MET CA C 55.336 . 1 12 1 4 MET CB C 32.786 . 1 13 1 4 MET N N 119.421 . 1 14 2 5 THR H H 8.182 . 1 15 2 5 THR C C 172.665 . 1 16 2 5 THR CA C 59.958 . 1 17 2 5 THR CB C 69.782 . 1 18 2 5 THR N N 119.702 . 1 19 3 6 PRO C C 176.799 . 1 20 3 6 PRO CA C 63.052 . 1 21 3 6 PRO CB C 32.154 . 1 22 4 7 VAL H H 8.296 . 1 23 4 7 VAL C C 176.047 . 1 24 4 7 VAL CA C 62.353 . 1 25 4 7 VAL CB C 32.702 . 1 26 4 7 VAL N N 121.310 . 1 27 5 8 ARG H H 8.431 . 1 28 5 8 ARG C C 173.621 . 1 29 5 8 ARG CA C 53.740 . 1 30 5 8 ARG CB C 30.253 . 1 31 5 8 ARG N N 126.551 . 1 32 7 10 PRO C C 176.579 . 1 33 7 10 PRO CA C 63.033 . 1 34 7 10 PRO CB C 32.082 . 1 35 8 11 HIS H H 8.374 . 1 36 8 11 HIS C C 175.109 . 1 37 8 11 HIS CA C 56.200 . 1 38 8 11 HIS CB C 30.487 . 1 39 8 11 HIS N N 119.308 . 1 40 9 12 THR H H 8.123 . 1 41 9 12 THR C C 172.364 . 1 42 9 12 THR CA C 59.614 . 1 43 9 12 THR CB C 69.935 . 1 44 9 12 THR N N 119.008 . 1 45 10 13 PRO C C 176.156 . 1 46 10 13 PRO CA C 62.908 . 1 47 10 13 PRO CB C 32.164 . 1 48 11 14 ASP H H 8.486 . 1 49 11 14 ASP C C 175.111 . 1 50 11 14 ASP CA C 52.322 . 1 51 11 14 ASP CB C 41.267 . 1 52 11 14 ASP N N 122.305 . 1 53 12 15 PRO CA C 63.712 . 1 54 12 15 PRO CB C 32.085 . 1 55 13 16 LEU H H 8.403 . 1 56 13 16 LEU C C 177.428 . 1 57 13 16 LEU CA C 55.561 . 1 58 13 16 LEU CB C 41.699 . 1 59 13 16 LEU N N 119.948 . 1 60 14 17 ASN H H 8.133 . 1 61 14 17 ASN C C 175.058 . 1 62 14 17 ASN CA C 53.330 . 1 63 14 17 ASN CB C 38.538 . 1 64 14 17 ASN N N 118.207 . 1 65 15 18 LEU H H 8.193 . 1 66 15 18 LEU C C 177.535 . 1 67 15 18 LEU CA C 55.557 . 1 68 15 18 LEU CB C 42.254 . 1 69 15 18 LEU N N 122.169 . 1 70 16 19 ARG H H 8.368 . 1 71 16 19 ARG C C 176.480 . 1 72 16 19 ARG CA C 56.114 . 1 73 16 19 ARG CB C 30.826 . 1 74 16 19 ARG N N 120.879 . 1 75 17 20 GLY H H 8.278 . 1 76 17 20 GLY C C 172.149 . 1 77 17 20 GLY CA C 44.684 . 1 78 17 20 GLY N N 110.062 . 1 79 18 21 PRO C C 177.592 . 1 80 18 21 PRO CA C 63.487 . 1 81 18 21 PRO CB C 32.127 . 1 82 19 22 LEU H H 8.419 . 1 83 19 22 LEU C C 177.137 . 1 84 19 22 LEU CA C 55.287 . 1 85 19 22 LEU CB C 41.822 . 1 86 19 22 LEU N N 121.183 . 1 87 20 23 ASP H H 8.066 . 1 88 20 23 ASP C C 176.256 . 1 89 20 23 ASP CA C 54.222 . 1 90 20 23 ASP CB C 41.526 . 1 91 20 23 ASP N N 119.877 . 1 92 21 24 GLY H H 8.078 . 1 93 21 24 GLY C C 171.998 . 1 94 21 24 GLY CA C 44.966 . 1 95 21 24 GLY N N 108.664 . 1 96 22 25 PRO CA C 63.471 . 1 97 22 25 PRO CB C 31.878 . 1 98 23 26 ARG H H 8.396 . 1 99 23 26 ARG C C 176.369 . 1 100 23 26 ARG CA C 56.729 . 1 101 23 26 ARG CB C 30.367 . 1 102 23 26 ARG N N 120.315 . 1 103 24 27 TRP H H 7.925 . 1 104 24 27 TRP C C 175.968 . 1 105 24 27 TRP CA C 57.350 . 1 106 24 27 TRP CB C 29.540 . 1 107 24 27 TRP N N 120.550 . 1 108 25 28 ARG H H 7.913 . 1 109 25 28 ARG C C 175.560 . 1 110 25 28 ARG CA C 55.865 . 1 111 25 28 ARG CB C 31.081 . 1 112 25 28 ARG N N 122.538 . 1 113 26 29 ARG H H 8.177 . 1 114 26 29 ARG C C 175.775 . 1 115 26 29 ARG CA C 56.127 . 1 116 26 29 ARG CB C 30.879 . 1 117 26 29 ARG N N 122.431 . 1 118 27 30 ALA H H 8.345 . 1 119 27 30 ALA C C 177.298 . 1 120 27 30 ALA CA C 52.298 . 1 121 27 30 ALA CB C 19.298 . 1 122 27 30 ALA N N 125.708 . 1 123 28 31 GLU H H 8.375 . 1 124 28 31 GLU C C 174.680 . 1 125 28 31 GLU CA C 54.275 . 1 126 28 31 GLU CB C 29.758 . 1 127 28 31 GLU N N 122.053 . 1 128 29 32 PRO C C 176.866 . 1 129 29 32 PRO CA C 63.195 . 1 130 29 32 PRO CB C 32.105 . 1 131 30 33 ALA H H 8.495 . 1 132 30 33 ALA C C 178.078 . 1 133 30 33 ALA CA C 52.820 . 1 134 30 33 ALA CB C 18.990 . 1 135 30 33 ALA N N 124.222 . 1 136 31 34 GLN H H 8.410 . 1 137 31 34 GLN C C 176.163 . 1 138 31 34 GLN CA C 55.910 . 1 139 31 34 GLN CB C 29.470 . 1 140 31 34 GLN N N 119.146 . 1 141 32 35 SER H H 8.338 . 1 142 32 35 SER C C 174.493 . 1 143 32 35 SER CA C 58.465 . 1 144 32 35 SER CB C 63.797 . 1 145 32 35 SER N N 116.972 . 1 146 33 36 ARG H H 8.389 . 1 147 33 36 ARG C C 176.051 . 1 148 33 36 ARG CA C 56.009 . 1 149 33 36 ARG CB C 30.770 . 1 150 33 36 ARG N N 122.983 . 1 151 34 37 ARG H H 8.412 . 1 152 34 37 ARG C C 174.268 . 1 153 34 37 ARG CA C 54.089 . 1 154 34 37 ARG CB C 30.144 . 1 155 34 37 ARG N N 123.610 . 1 156 35 38 PRO C C 177.535 . 1 157 35 38 PRO CA C 63.438 . 1 158 35 38 PRO CB C 32.171 . 1 159 36 39 GLY H H 8.560 . 1 160 36 39 GLY C C 174.150 . 1 161 36 39 GLY CA C 45.282 . 1 162 36 39 GLY N N 109.552 . 1 163 37 40 ARG H H 8.315 . 1 164 37 40 ARG C C 176.528 . 1 165 37 40 ARG CA C 55.988 . 1 166 37 40 ARG CB C 30.911 . 1 167 37 40 ARG N N 120.669 . 1 168 38 41 SER H H 8.502 . 1 169 38 41 SER C C 174.116 . 1 170 38 41 SER CA C 58.391 . 1 171 38 41 SER CB C 63.883 . 1 172 38 41 SER N N 117.653 . 1 173 39 42 ARG H H 8.444 . 1 174 39 42 ARG CA C 54.006 . 1 175 39 42 ARG CB C 30.305 . 1 176 39 42 ARG N N 123.734 . 1 177 40 43 PRO C C 177.631 . 1 178 40 43 PRO CA C 63.485 . 1 179 40 43 PRO CB C 32.098 . 1 180 41 44 GLY H H 8.605 . 1 181 41 44 GLY C C 174.689 . 1 182 41 44 GLY CA C 45.358 . 1 183 41 44 GLY N N 110.031 . 1 184 42 45 GLY H H 8.282 . 1 185 42 45 GLY C C 173.514 . 1 186 42 45 GLY CA C 44.971 . 1 187 42 45 GLY N N 108.681 . 1 188 43 46 ALA H H 8.219 . 1 189 43 46 ALA C C 175.584 . 1 190 43 46 ALA CA C 50.651 . 1 191 43 46 ALA CB C 18.174 . 1 192 43 46 ALA N N 124.969 . 1 193 44 47 PRO C C 176.803 . 1 194 44 47 PRO CA C 62.919 . 1 195 44 47 PRO CB C 32.101 . 1 196 45 48 LEU H H 8.328 . 1 197 45 48 LEU C C 177.237 . 1 198 45 48 LEU CA C 55.291 . 1 199 45 48 LEU CB C 42.234 . 1 200 45 48 LEU N N 122.458 . 1 201 46 49 ARG H H 8.251 . 1 202 46 49 ARG C C 175.620 . 1 203 46 49 ARG CA C 55.883 . 1 204 46 49 ARG CB C 30.954 . 1 205 46 49 ARG N N 121.556 . 1 206 47 50 TYR H H 8.195 . 1 207 47 50 TYR C C 175.320 . 1 208 47 50 TYR CA C 57.655 . 1 209 47 50 TYR CB C 38.970 . 1 210 47 50 TYR N N 121.125 . 1 211 48 51 HIS H H 8.289 . 1 212 48 51 HIS C C 174.900 . 1 213 48 51 HIS CA C 56.038 . 1 214 48 51 HIS CB C 31.084 . 1 215 48 51 HIS N N 122.049 . 1 216 49 52 ARG H H 8.435 . 1 217 49 52 ARG C C 176.262 . 1 218 49 52 ARG CA C 56.181 . 1 219 49 52 ARG CB C 30.927 . 1 220 49 52 ARG N N 123.318 . 1 221 50 53 THR H H 8.284 . 1 222 50 53 THR C C 175.001 . 1 223 50 53 THR CA C 62.005 . 1 224 50 53 THR CB C 69.895 . 1 225 50 53 THR N N 115.157 . 1 226 51 54 GLY H H 8.493 . 1 227 51 54 GLY C C 174.166 . 1 228 51 54 GLY CA C 45.324 . 1 229 51 54 GLY N N 111.306 . 1 230 52 55 VAL H H 8.084 . 1 231 52 55 VAL C C 176.898 . 1 232 52 55 VAL CA C 62.474 . 1 233 52 55 VAL CB C 32.570 . 1 234 52 55 VAL N N 119.150 . 1 235 53 56 GLY H H 8.609 . 1 236 53 56 GLY C C 174.261 . 1 237 53 56 GLY CA C 45.428 . 1 238 53 56 GLY N N 112.607 . 1 239 54 57 MET H H 8.234 . 1 240 54 57 MET C C 176.413 . 1 241 54 57 MET CA C 55.503 . 1 242 54 57 MET CB C 32.991 . 1 243 54 57 MET N N 119.910 . 1 244 55 58 SER H H 8.427 . 1 245 55 58 SER C C 174.775 . 1 246 55 58 SER CA C 58.407 . 1 247 55 58 SER CB C 63.789 . 1 248 55 58 SER N N 117.156 . 1 249 56 59 ARG H H 8.573 . 1 250 56 59 ARG C C 176.579 . 1 251 56 59 ARG CA C 56.392 . 1 252 56 59 ARG CB C 30.771 . 1 253 56 59 ARG N N 123.365 . 1 254 57 60 THR H H 8.206 . 1 255 57 60 THR C C 175.109 . 1 256 57 60 THR CA C 62.024 . 1 257 57 60 THR CB C 69.942 . 1 258 57 60 THR N N 114.279 . 1 259 58 61 GLY H H 8.441 . 1 260 58 61 GLY C C 174.099 . 1 261 58 61 GLY CA C 45.301 . 1 262 58 61 GLY N N 111.084 . 1 263 59 62 HIS C C 176.095 . 1 264 59 62 HIS CA C 56.504 . 1 265 59 62 HIS CB C 30.693 . 1 266 60 63 GLY H H 8.557 . 1 267 60 63 GLY C C 174.161 . 1 268 60 63 GLY CA C 45.392 . 1 269 60 63 GLY N N 110.626 . 1 270 61 64 SER H H 8.299 . 1 271 61 64 SER C C 174.187 . 1 272 61 64 SER CA C 58.313 . 1 273 61 64 SER CB C 63.999 . 1 274 61 64 SER N N 115.963 . 1 275 62 65 ARG H H 8.329 . 1 276 62 65 ARG C C 174.187 . 1 277 62 65 ARG CA C 54.095 . 1 278 62 65 ARG CB C 30.354 . 1 279 62 65 ARG N N 123.734 . 1 280 63 66 PRO C C 176.106 . 1 281 63 66 PRO CA C 63.516 . 1 282 63 66 PRO CB C 31.889 . 1 283 64 67 VAL H H 7.767 . 1 284 64 67 VAL C C 181.137 . 1 285 64 67 VAL CA C 63.516 . 1 286 64 67 VAL CB C 33.162 . 1 287 64 67 VAL N N 124.116 . 1 stop_ save_ save_heteronucl_T1_relaxation_1 _Saveframe_category T1_relaxation _Details ; Bruker pulse sequence used hsqct1etf3gpsi with the following delays: 10 ms, 62.5 ms, 125 ms, 250 ms, 500 ms, 750 ms, 1000 ms, and 1500 ms. Relaxation delay between scans: 6 s ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 800 _T1_coherence_type Sz _T1_value_units ms _Mol_system_component_name 'N-terminal domain' _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 3 ALA N 1198.02 51.98 2 4 MET N 824.71 26.27 3 5 THR N 771.63 13.84 4 7 VAL N 712.32 5.52 5 8 ARG N 599.2 3.57 6 12 THR N 597.36 13.24 7 14 ASP N 583.97 7.77 8 16 LEU N 550.62 10.07 9 17 ASN N 544.24 8.04 10 18 LEU N 572.21 7.46 11 19 ARG N 562.16 6.57 12 20 GLY N 593.01 6.38 13 22 LEU N 572.05 10.81 14 23 ASP N 573.56 7.23 15 24 GLY N 611.09 6.93 16 26 ARG N 530.96 14.06 17 27 TRP N 523.07 10.65 18 28 ARG N 502.02 14.4 19 29 ARG N 549.4 16.28 20 30 ALA N 561.22 8.08 21 31 GLU N 644.71 5.16 22 33 ALA N 598.78 8.68 23 34 GLN N 620.97 14.01 24 35 SER N 590.64 10.73 25 36 ARG N 541.04 20.03 26 37 ARG N 569.55 9.52 27 39 GLY N 575.4 11.09 28 40 ARG N 540.03 28.9 29 41 SER N 586.41 14.63 30 42 ARG N 597.68 10.92 31 44 GLY N 620.06 8.92 32 45 GLY N 666.16 3.66 33 46 ALA N 672.42 6.31 34 48 LEU N 597.58 2.97 35 49 ARG N 552.92 13.8 36 50 TYR N 534.32 12.37 37 52 ARG N 526.06 26.8 38 53 THR N 520.8 11.61 39 54 GLY N 552.3 12.32 40 55 VAL N 590.92 8.24 41 56 GLY N 601.41 11.79 42 57 MET N 573.88 14.43 43 58 SER N 596.55 11.49 44 59 ARG N 529.81 28.78 45 60 THR N 569.27 12.89 46 61 GLY N 597.11 12.85 47 63 GLY N 674.38 16.65 48 64 SER N 658.09 20.9 49 65 ARG N 728.12 22.17 50 67 VAL N 1014.49 12.68 stop_ save_ save_heteronucl_T2_relaxation_1 _Saveframe_category T2_relaxation _Details ; Bruker pulse sequence used hsqct2etf3gpsi with the following delays: 5 ms, 30 ms, 62.5 ms, 125 ms, 187.5 ms, 250 ms, 312.5 ms and 375 ms. Relaxation delay between scans: 4 s ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 800 _T2_coherence_type S(+,-) _T2_value_units ms _Mol_system_component_name 'N-terminal domain' _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 3 ALA N 301.66 23.52 . . 2 4 MET N 359.83 23.36 . . 3 5 THR N 345.49 23.01 . . 4 7 VAL N 378.31 10.88 . . 5 8 ARG N 242.69 10.23 . . 6 12 THR N 210.8 15.55 . . 7 14 ASP N 182.5 6.66 . . 8 16 LEU N 222.49 6.08 . . 9 17 ASN N 211.65 9.52 . . 10 18 LEU N 192.69 8.78 . . 11 19 ARG N 248.05 8.7 . . 12 20 GLY N 260.39 12.74 . . 13 22 LEU N 246.15 7.21 . . 14 23 ASP N 242.83 8.16 . . 15 24 GLY N 241.61 10.49 . . 16 26 ARG N 196.78 9.49 . . 17 27 TRP N 200.01 7.02 . . 18 28 ARG N 151.52 6.13 . . 19 29 ARG N 162.63 7.38 . . 20 30 ALA N 169.47 6.68 . . 21 31 GLU N 204.65 6.15 . . 22 33 ALA N 182.63 10.15 . . 23 34 GLN N 243.38 13.37 . . 24 35 SER N 222.98 9.99 . . 25 36 ARG N 191.42 9.07 . . 26 37 ARG N 194.95 9.89 . . 27 39 GLY N 244.78 13.29 . . 28 40 ARG N 246.72 10.4 . . 29 41 SER N 237.95 10.29 . . 30 42 ARG N 198.12 12.18 . . 31 44 GLY N 279.46 15.13 . . 32 45 GLY N 267.62 14.77 . . 33 46 ALA N 209.69 10.76 . . 34 48 LEU N 177.09 3.9 . . 35 49 ARG N 234.83 9.64 . . 36 50 TYR N 223.94 10.05 . . 37 52 ARG N 196.54 14.53 . . 38 53 THR N 216.52 10.68 . . 39 54 GLY N 257.17 15.74 . . 40 55 VAL N 280.06 15.55 . . 41 56 GLY N 268.14 18.78 . . 42 57 MET N 284.16 17.16 . . 43 58 SER N 271.42 11.99 . . 44 59 ARG N 208.05 8.42 . . 45 60 THR N 261.14 12.89 . . 46 61 GLY N 287.12 14.08 . . 47 63 GLY N 311.45 18.63 . . 48 64 SER N 292.4 15.04 . . 49 65 ARG N 257.15 18.11 . . 50 67 VAL N 426.9 20.21 . . stop_ save_ save_heteronucl_NOEs_1 _Saveframe_category heteronuclear_NOE _Details 'Bruker pulse sequence used hsqcnoef3gpsi.' loop_ _Experiment_label '15N-(1H) NOE' stop_ loop_ _Sample_label . stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 800 _Mol_system_component_name 'N-terminal domain' _Atom_one_atom_name N _Atom_two_atom_name H _Heteronuclear_NOE_value_type 'peak height' _NOE_reference_value 1 _NOE_reference_description . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 3 ALA -0.568355258 0.01690597 4 MET -0.177764187 0.001570941 5 THR -0.123780066 0.00784854 7 VAL 0.023465098 0.000744661 8 ARG 0.220341512 0.001574756 11 HIS 0.171034217 0.0547767 12 THR 0.324830027 0.003080989 14 ASP 0.295022684 0.001042116 16 LEU 0.421153605 0.001775605 17 ASN 0.425169246 0.000304873 18 LEU 0.323108998 0.00063961 19 ARG 0.381970335 0.005768456 20 GLY 0.269921243 0.004643777 22 LEU 0.329330984 0.001836239 23 ASP 0.337199796 0.006823316 24 GLY 0.299853604 0.006058023 26 ARG 0.449797513 0.009260597 27 TRP 0.485942331 0.002854047 28 ARG 0.473602694 0.00150055 29 ARG 0.400644034 0.008691909 30 ALA 0.377175888 0.008405192 31 GLU 0.322995963 0.007304838 33 ALA 0.238085717 0.002975584 34 GLN 0.252649997 0.004900584 35 SER 0.240155988 0.007161383 36 ARG 0.282545297 0.003187269 37 ARG 0.300083087 0.00512462 39 GLY 0.266372369 0.004840164 40 ARG 0.310895586 0.007847337 41 SER 0.213799758 0.00723066 42 ARG 0.259162788 0.00316471 44 GLY 0.203542714 0.006035989 45 GLY 0.177720153 0.001819841 46 ALA 0.202861105 0.000174365 48 LEU 0.273299299 0.000566736 49 ARG 0.292816951 0.001490737 50 TYR 0.392084258 0.010920257 51 HIS 0.403293499 0.006917514 52 ARG 0.328024883 0.001713005 53 THR 0.313528742 0.002754613 54 GLY 0.267660614 0.000482354 55 VAL 0.30493628 0.007692115 56 GLY 0.219241515 0.003709537 57 MET 0.221203741 0.000367736 58 SER 0.174383881 0.007861537 59 ARG 0.206375885 0.011168771 60 THR 0.203341493 0.004662129 61 GLY 0.172898463 0.007670177 63 GLY 0.044091746 0.006315449 64 SER 0.066487153 0.002588903 65 ARG -0.060217776 0.002108636 67 VAL -0.669888228 0.00555573 stop_ save_ save_H_exch_rates_1 _Saveframe_category H_exchange_rates _Details ; Bruker pulse sequence used: fhsqccxf3gpph. Spin lock times used: 10 ms, 15 ms, 20 ms, 25 ms, 30 ms, 40 ms, 50 ms, 75 ms, and 100 ms. relaxation delay of 3 s was used. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _H_exchange_rate_units s-1 _Mol_system_component_name 'N-terminal domain' _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Atom_name _H_exchange_rate_value _H_exchange_rate_min_value _H_exchange_rate_max_value _H_exchange_rate_value_error 3 ALA H 14.24 . . 0.31 4 MET H 9.98 . . 0.14 5 THR H 3.33 . . 0.06 7 VAL H 0.64 . . 0.02 8 ARG H 1.17 . . 0.03 12 THR H 8.8 . . 0.26 14 ASP H 2.41 . . 0.04 16 LEU H 0.75 . . 0.03 17 ASN H 2.43 . . 0.03 18 LEU H 3.06 . . 0.08 19 ARG H 2.06 . . 0.03 20 GLY H 8.34 . . 0.16 22 LEU H 1.31 . . 0.01 23 ASP H 1.11 . . 0.02 24 GLY H 0.83 . . 0.02 26 ARG H 5.92 . . 0.1 27 TRP H 2.29 . . 0.11 28 ARG H 3.2 . . 0.08 29 ARG H 4.37 . . 0.05 30 ALA H 3.39 . . 0.04 31 GLU H 1.37 . . 0.01 33 ALA H 3.58 . . 0.07 34 GLN H 7.25 . . 0.12 35 SER H 16.41 . . 0.22 36 ARG H 12.54 . . 0.31 37 ARG H 8 . . 0.11 39 GLY H 10.82 . . 0.18 40 ARG H 13.9 . . 0.24 41 SER H 22.3 . . 0.87 42 ARG H 9.34 . . 0.16 44 GLY H 12.24 . . 0.24 45 GLY H 9.5 . . 0.15 46 ALA H 3.47 . . 0.06 48 LEU H 1.04 . . 0.03 49 ARG H 4.46 . . 0.07 50 TYR H 4.9 . . 0.05 51 HIS H 19.33 . . 0.49 52 ARG H 21.49 . . 0.51 53 THR H 12.22 . . 0.21 54 GLY H 16.64 . . 0.14 55 VAL H 4.45 . . 0.05 56 GLY H 7.18 . . 0.14 57 MET H 9.31 . . 0.17 58 SER H 19.5 . . 0.32 59 ARG H 23.06 . . 1.04 60 THR H 12.95 . . 0.3 61 GLY H 17.9 . . 0.23 63 GLY H 25.55 . . 1.01 64 SER H 15.58 . . 0.51 65 ARG H 4.2 . . 0.03 stop_ save_