M. tuberculosis [4Fe-4S] protein WhiB1 is a four-helix bundle that forms a NO-sensitive complex with sigmaA and regulates the major virulence factor ESX-1
AGENLYFQGA MDWRHKAVCR DEDPELFFPV GNSGPALAQI ADAKLVCNRC PVTTECLSWA LNTGQDSGVW GGMSEDERRA LKRRNARTKA RTGV
Polymer type: polypeptide(L)
Total | 1H | 13C | 15N | |
---|---|---|---|---|
All | 75.8 % (794 of 1048) | 69.2 % (378 of 546) | 82.3 % (330 of 401) | 85.1 % (86 of 101) |
Backbone | 89.0 % (495 of 556) | 84.5 % (163 of 193) | 91.2 % (249 of 273) | 92.2 % (83 of 90) |
Sidechain | 64.5 % (372 of 577) | 61.2 % (216 of 353) | 71.8 % (153 of 213) | 27.3 % (3 of 11) |
Aromatic | 71.8 % (56 of 78) | 71.8 % (28 of 39) | 69.4 % (25 of 36) | 100.0 % (3 of 3) |
Methyl | 83.0 % (73 of 88) | 81.8 % (36 of 44) | 84.1 % (37 of 44) |
1. Transcriptional regulator WhiB1
AGENLYFQGA MDWRHKAVCR DEDPELFFPV GNSGPALAQI ADAKLVCNRC PVTTECLSWA LNTGQDSGVW GGMSEDERRA LKRRNARTKA RTGVSolvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.1013291 |
Atom type | Mol. common name | Atom group | Value | Ref. method | Ref. type | Shift ratio |
---|---|---|---|---|---|---|
13C | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.2514495 |
1H | DSS | methyl protons | 0.0 ppm | internal | direct | 1.0 |
15N | DSS | methyl protons | 0.0 ppm | internal | indirect | 0.1013291 |
Bruker Avance - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Bruker Avance - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Bruker Avance - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Bruker Avance - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Bruker Avance - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Bruker Avance - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Bruker Avance - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Bruker Avance - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Bruker Avance - 800 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Bruker Avance - 600 MHz
State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0 (±0.05), Details 0.3 mM WhiB1 protein, 25 mM sodium phosphate, 250 mM sodium chloride, 90% H2O/10% D2O
# | Name | Isotope labeling | Type | Concentration |
---|---|---|---|---|
1 | WhiB1 protein | natural abundance | 0.3 mM | |
2 | sodium chloride | natural abundance | 250 mM | |
3 | sodium phosphate | natural abundance | 25 mM |
Properties
Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints | combined_34153_5oay.nef |
Input source #2: Coordindates | 5oay.cif |
Diamagnetism of the molecular assembly | False (excluding Oxygen atoms) |
Whether the assembly has a disulfide bond | None |
Whether the assembly has a other bond | True (see coodinates for details) |
Whether the assembly contains a cyclic polymer | None |
Overall data processing status | Warning |
Disulfide bonds
NoneOther bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)
Ptnr_site_1 | Ptnr_site_2 | Redox_state_prediction_1 | Redox_state_prediction_2 | Distance (Å) |
---|---|---|---|---|
1:19:CYS:SG | 2:1:SF4:FE3 | unknown | unknown | n/a |
1:47:CYS:SG | 2:1:SF4:FE4 | unknown | unknown | n/a |
1:50:CYS:SG | 2:1:SF4:FE1 | unknown | unknown | n/a |
1:56:CYS:SG | 2:1:SF4:FE2 | unknown | unknown | n/a |
Non-standard residues
Chain_ID | Seq_ID | Comp_ID | Chem_comp_name | Experimental evidences |
---|---|---|---|---|
B | 1 | SF4 | IRON/SULFUR CLUSTER | None |
Sequence alignments
------------------10--------20--------30--------40--------50--------60--------70--------80---- AGENLYFQGAMDWRHKAVCRDEDPELFFPVGNSGPALAQIADAKLVCNRCPVTTECLSWALNTGQDSGVWGGMSEDERRALKRRNARTKARTGV |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| AGENLYFQGAMDWRHKAVCRDEDPELFFPVGNSGPALAQIADAKLVCNRCPVTTECLSWALNTGQDSGVWGGMSEDERRALKRRNARTKARTGV --------10--------20--------30--------40--------50--------60--------70--------80--------90----
Chain assignments
Entity_assembly_ID (NMR) | Auth_asym_ID (model) | Length | Unmapped | Conflict | Sequence coverage (%) |
---|---|---|---|---|---|
A | A | 94 | 0 | 0 | 100.0 |
Content subtype: combined_34153_5oay.nef
Assigned chemical shifts
------------------10--------20--------30--------40--------50--------60--------70--------80---- AGENLYFQGAMDWRHKAVCRDEDPELFFPVGNSGPALAQIADAKLVCNRCPVTTECLSWALNTGQDSGVWGGMSEDERRALKRRNARTKARTGV ||||||||||||||||| |||||||||||||||||||||||||||||||| |||||||||||||||||| ||||||||||||||||||||||| AGENLYFQGAMDWRHKA.CRDEDPELFFPVGNSGPALAQIADAKLVCNRC..TTECLSWALNTGQDSGVW.GMSEDERRALKRRNARTKARTGV
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 546 | 373 | 68.3 |
13C chemical shifts | 401 | 322 | 80.3 |
15N chemical shifts | 110 | 86 | 78.2 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 193 | 170 | 88.1 |
13C chemical shifts | 188 | 177 | 94.1 |
15N chemical shifts | 90 | 83 | 92.2 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 353 | 203 | 57.5 |
13C chemical shifts | 213 | 145 | 68.1 |
15N chemical shifts | 20 | 3 | 15.0 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 46 | 38 | 82.6 |
13C chemical shifts | 46 | 38 | 82.6 |
Atom group | # of target shifts | # of assigned shifts | Completeness (%) |
---|---|---|---|
1H chemical shifts | 39 | 28 | 71.8 |
13C chemical shifts | 36 | 25 | 69.4 |
15N chemical shifts | 3 | 3 | 100.0 |
Covalent bonds
Distance restraints
------------------10--------20--------30--------40--------50--------60--------70--------80---- AGENLYFQGAMDWRHKAVCRDEDPELFFPVGNSGPALAQIADAKLVCNRCPVTTECLSWALNTGQDSGVWGGMSEDERRALKRRNARTKARTGV ||||||| |||||||| |||| |||||||||||||||||||||| || ||| ||||||||||||| |||||||||||||| AGENLYF..AMDWRHKA..RDED.ELFFPVGNSGPALAQIADAKLV.NR...TTE.LSWALNTGQDSGV...MSEDERRALKRRNA ------------------10--------20--------30--------40--------50--------60--------70------
------------------10--------20--------30--------40--------50--------60--------70--------80---- AGENLYFQGAMDWRHKAVCRDEDPELFFPVGNSGPALAQIADAKLVCNRCPVTTECLSWALNTGQDSGVWGGMSEDERRALKRRNARTKARTGV |||||||||||| |||||||||||||| ||||||||||| ||||||||||||| ..........MDWRHKAVCRDE............PALAQIADAKLVCN....TTECLSWALNT..........SEDERRALKRRNA ------------------10--------20--------30--------40--------50--------60--------70------
Dihedral angle restraints
------------------10--------20--------30--------40--------50--------60--------70--------80---- AGENLYFQGAMDWRHKAVCRDEDPELFFPVGNSGPALAQIADAKLVCNRCPVTTECLSWALNTGQDSGVWGGMSEDERRALKRRNARTKARTGV ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| ||||||||||||||| .........AMDWRHKAVCRDEDPELFFPVGNSGPALAQIADAKLVCNRCPVTTECLSWALNTGQDSGVW.GMSEDERRALKRRNA ------------------10--------20--------30--------40--------50--------60--------70------