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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19380
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Borin, Brendan; Tang, Wei; Krezel, Andrzej. "Helicobacter pylori RNA polymerase -subunit C-terminal domain shows features unique to -proteobacteria and binds NikR/DNA complexes." Protein Sci. 23, 454-463 (2014).
PubMed: 24442709
Assembly members:
RNAP_alpha_subunit_CTD, polymer, 126 residues, 12754.470 Da.
Natural source: Common Name: e-proteobacteria Taxonomy ID: 210 Superkingdom: Bacteria Kingdom: not available Genus/species: Helicobacter pylori
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETBNK
Entity Sequences (FASTA):
RNAP_alpha_subunit_CTD: MRGSHHHHHHGSLGVFGERP
IANTEYSGDYAQRDDAKDLS
AKIESMNLSARCFNCLDKIG
IKYVGELVLMSEEELKGVKN
MGKKSYDEIAEKLNDLGYPV
GTELSPEQRESLKKRLEKLE
DKGGND
Data type | Count |
13C chemical shifts | 340 |
15N chemical shifts | 112 |
1H chemical shifts | 736 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RNA polymerase alpha subunit C-terminal domain | 1 |
Entity 1, RNA polymerase alpha subunit C-terminal domain 126 residues - 12754.470 Da.
residues 1-12 represent a non-native His6 Ni-affinity tag. Contains native residues 231-344.
1 | MET | ARG | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
2 | GLY | SER | LEU | GLY | VAL | PHE | GLY | GLU | ARG | PRO | ||||
3 | ILE | ALA | ASN | THR | GLU | TYR | SER | GLY | ASP | TYR | ||||
4 | ALA | GLN | ARG | ASP | ASP | ALA | LYS | ASP | LEU | SER | ||||
5 | ALA | LYS | ILE | GLU | SER | MET | ASN | LEU | SER | ALA | ||||
6 | ARG | CYS | PHE | ASN | CYS | LEU | ASP | LYS | ILE | GLY | ||||
7 | ILE | LYS | TYR | VAL | GLY | GLU | LEU | VAL | LEU | MET | ||||
8 | SER | GLU | GLU | GLU | LEU | LYS | GLY | VAL | LYS | ASN | ||||
9 | MET | GLY | LYS | LYS | SER | TYR | ASP | GLU | ILE | ALA | ||||
10 | GLU | LYS | LEU | ASN | ASP | LEU | GLY | TYR | PRO | VAL | ||||
11 | GLY | THR | GLU | LEU | SER | PRO | GLU | GLN | ARG | GLU | ||||
12 | SER | LEU | LYS | LYS | ARG | LEU | GLU | LYS | LEU | GLU | ||||
13 | ASP | LYS | GLY | GLY | ASN | ASP |
sample_1: RNAP alpha subunit CTD, [U-15N], 1 mM; potassium phosphate 25 mM; potassium chloride 225 mM; TCEP 1 mM; H2O 90%; D2O 10%
sample_2: RNAP alpha subunit CTD, [U-13C; U-15N], 1 mM; potassium phosphate 25 mM; potassium chloride 225 mM; TCEP 1 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 7.3; pressure: 1 atm; temperature: 273 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCANH | sample_2 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HCCH TOCSY | sample_2 | isotropic | sample_conditions_1 |
TOPSPIN, Bruker Biospin - processing
SPARKY, Goddard - chemical shift assignment, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
ProcheckNMR, Laskowski and MacArthur - geometry optimization
PDB | |
DBJ | BAJ55821 BAJ56204 BAJ58801 BAJ60323 BAM97153 |
EMBL | CAJ99012 CAX29978 CBI65743 |
GB | AAD06815 AAD08336 ABF85305 ACD48738 ACI27991 |
REF | NP_208085 WP_000864476 WP_000864477 WP_000864478 WP_000864479 |
SP | P56001 Q17ZB4 Q1CRW7 Q9ZJT5 |
AlphaFold | P56001 Q17ZB4 Q1CRW7 Q9ZJT5 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks