BMRB Entry 15072
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15072
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase PubMed: 17355883
Deposition date: 2006-12-12 Original release date: 2007-04-17
Authors: Carbajo, Rodrigo; Neuhaus, David; Kellas, Fiona; Yang, Ji-Chun; Runswick, Michael; Montgomery, Martin; Walker, John
Citation: Carbajo, Rodrigo; Kellas, Fiona; Yang, Ji-Chun; Runswick, Michael; Montgomery, Martin; Walker, John; Neuhaus, David. "How the N-terminal Domain of the OSCP Subunit of Bovine F1Fo-ATP Synthase Interacts with the N-terminal Region of an Alpha Subunit" J. Mol. Biol. 368, 310-318 (2007).
Assembly members:
oscp-nt, polymer, 120 residues, Formula weight is not available
alpha-nt, polymer, 25 residues, Formula weight is not available
Natural source: Common Name: Cow Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
oscp-nt: FAKLVRPPVQIYGIEGRYAT
ALYSAASKQNKLEQVEKELL
RVGQILKEPKMAASLLNPYV
KRSVKVKSLSDMTAKEKFSP
LTSNLINLLAENGRLTNTPA
VISAFSTMMSVHRGEVPCTV
alpha-nt: QKTGTAEVSSILEERILGAD
TSVDL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 222 |
15N chemical shifts | 100 |
1H chemical shifts | 738 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | OSCP N-terminal 1-120 | 1 |
2 | alpha N-terminal 1-25 | 2 |
Entities:
Entity 1, OSCP N-terminal 1-120 120 residues - Formula weight is not available
1 | PHE | ALA | LYS | LEU | VAL | ARG | PRO | PRO | VAL | GLN | |
2 | ILE | TYR | GLY | ILE | GLU | GLY | ARG | TYR | ALA | THR | |
3 | ALA | LEU | TYR | SER | ALA | ALA | SER | LYS | GLN | ASN | |
4 | LYS | LEU | GLU | GLN | VAL | GLU | LYS | GLU | LEU | LEU | |
5 | ARG | VAL | GLY | GLN | ILE | LEU | LYS | GLU | PRO | LYS | |
6 | MET | ALA | ALA | SER | LEU | LEU | ASN | PRO | TYR | VAL | |
7 | LYS | ARG | SER | VAL | LYS | VAL | LYS | SER | LEU | SER | |
8 | ASP | MET | THR | ALA | LYS | GLU | LYS | PHE | SER | PRO | |
9 | LEU | THR | SER | ASN | LEU | ILE | ASN | LEU | LEU | ALA | |
10 | GLU | ASN | GLY | ARG | LEU | THR | ASN | THR | PRO | ALA | |
11 | VAL | ILE | SER | ALA | PHE | SER | THR | MET | MET | SER | |
12 | VAL | HIS | ARG | GLY | GLU | VAL | PRO | CYS | THR | VAL |
Entity 2, alpha N-terminal 1-25 25 residues - Formula weight is not available
1 | GLN | LYS | THR | GLY | THR | ALA | GLU | VAL | SER | SER | ||||
2 | ILE | LEU | GLU | GLU | ARG | ILE | LEU | GLY | ALA | ASP | ||||
3 | THR | SER | VAL | ASP | LEU |
Samples:
sample_1: oscp-nt, [U-99% 13C; U-99% 15N], 0.5 mM; alpha-nt 1.5 mM
sample_conditions_1: ionic strength: 0.5 M; pH: 6.5; pressure: 1 atm; temperature: 300 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
SPARKY, Goddard - chemical shift assignment
X-PLOR, Brunger - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker DMX 600 MHz
- Bruker DRX 500 MHz
Related Database Links:
PDB | |
GB | AAA30676 AAI02205 ELR58089 AAB59266 AAI16060 ACD02421 EFB21996 EGW04262 |
PRF | 1002210A |
REF | NP_776669 XP_005674722 XP_005893414 XP_005956973 XP_005956974 NP_001172071 NP_001268629 NP_001274083 NP_777109 XP_001506958 |
SP | P13621 P19483 P80021 |
TPG | DAA33707 DAA15776 |
DBJ | BAK09231 |
EMBL | CAA45865 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts