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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15334
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Hastings, Curtis; Lee, Seok-Yong; Cho, Ho; Yan, Dalai; Kustu, Sydney; Wemmer, David. "High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain." Biochemistry 42, 9081-9090 (2003).
PubMed: 12885241
Assembly members:
NtrC4 Receiver domain dimer, polymer, 121 residues, 13671.741 Da.
Natural source: Common Name: AQUIFEX AEOLICUS VF5 Taxonomy ID: 63363 Superkingdom: Bacteria Kingdom: not available Genus/species: Aquifex aeolicus
Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI Vector: PET21A
Entity Sequences (FASTA):
NtrC4 Receiver domain dimer: MKRVLVVDDEESITSSLSAI
LEEEGYHPDTAKTLREAEKK
IKELFFPVIVLDVWMPDGDG
VNFIDFIKENSPDSVVIVIT
GHGSVDTAVKAIKKGAYEFL
EKPFSVERFLLTIKHAFEEY
S
Data type | Count |
13C chemical shifts | 384 |
15N chemical shifts | 115 |
1H chemical shifts | 821 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | NtrC4 Receiver domain 1 | 1 |
2 | NtrC4 Receiver domain 2 | 1 |
Entity 1, NtrC4 Receiver domain 1 121 residues - 13671.741 Da.
1 | MET | LYS | ARG | VAL | LEU | VAL | VAL | ASP | ASP | GLU | ||||
2 | GLU | SER | ILE | THR | SER | SER | LEU | SER | ALA | ILE | ||||
3 | LEU | GLU | GLU | GLU | GLY | TYR | HIS | PRO | ASP | THR | ||||
4 | ALA | LYS | THR | LEU | ARG | GLU | ALA | GLU | LYS | LYS | ||||
5 | ILE | LYS | GLU | LEU | PHE | PHE | PRO | VAL | ILE | VAL | ||||
6 | LEU | ASP | VAL | TRP | MET | PRO | ASP | GLY | ASP | GLY | ||||
7 | VAL | ASN | PHE | ILE | ASP | PHE | ILE | LYS | GLU | ASN | ||||
8 | SER | PRO | ASP | SER | VAL | VAL | ILE | VAL | ILE | THR | ||||
9 | GLY | HIS | GLY | SER | VAL | ASP | THR | ALA | VAL | LYS | ||||
10 | ALA | ILE | LYS | LYS | GLY | ALA | TYR | GLU | PHE | LEU | ||||
11 | GLU | LYS | PRO | PHE | SER | VAL | GLU | ARG | PHE | LEU | ||||
12 | LEU | THR | ILE | LYS | HIS | ALA | PHE | GLU | GLU | TYR | ||||
13 | SER |
sample_1: NtrC4Ra, [U-100% 13C; U-100% 15N], 1 ± 0.2 mM
sample_2: NtrC4Ra, [U-100% 13C], 0.8 mM
sample_3: NtrC4Ra 0.8 mM
sample_conditions_1: ionic strength: 0 M; pH: 8.0; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
15N-IPAP-HSQC | sample_1 | isotropic | sample_conditions_1 |
[F1] 13C-edited [F3] 13C-filtered HSQC-NOESY | sample_2 | isotropic | sample_conditions_1 |
HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH v2.1.2, Schwieters, Kuszewski, Tjandra and Clore - structure solution
SPARKY v3.12, Goddard - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks