BMRB Entry 19994
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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/BMR19994
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Title: 3D NMR structure of the transmembrane domain of the full-length inner membrane protein YgaP from Escherichia coli PubMed: 24958726
Deposition date: 2014-05-29 Original release date: 2014-09-10
Authors: Eichmann, Cedric; Tzitzilonis, Christos; Bordignon, Enrica; Maslennikov, Innokentiy; Choe, Senyon; Riek, Roland
Citation: Eichmann, Cedric; Tzitzilonis, Christos; Bordignon, Enrica; Maslennikov, Innokentiy; Choe, Senyon; Riek, Roland. "Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coli." J. Biol. Chem. 289, 23482-23503 (2014).
Assembly members:
entity, polymer, 68 residues, 7157.559 Da.
Natural source: Common Name: E. coli Taxonomy ID: 83333 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: KSQPLPLMRQVQIAAGGLIL
IGVVLGYTVNSGFFLLSGFV
GAGLLFAGISGFSGMARLLD
KMPWNQRA
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 298 |
15N chemical shifts | 61 |
13C chemical shifts | 12 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_2 | 1 |
Entities:
Entity 1, entity_1 68 residues - 7157.559 Da.
1 | LYS | SER | GLN | PRO | LEU | PRO | LEU | MET | ARG | GLN | ||||
2 | VAL | GLN | ILE | ALA | ALA | GLY | GLY | LEU | ILE | LEU | ||||
3 | ILE | GLY | VAL | VAL | LEU | GLY | TYR | THR | VAL | ASN | ||||
4 | SER | GLY | PHE | PHE | LEU | LEU | SER | GLY | PHE | VAL | ||||
5 | GLY | ALA | GLY | LEU | LEU | PHE | ALA | GLY | ILE | SER | ||||
6 | GLY | PHE | SER | GLY | MET | ALA | ARG | LEU | LEU | ASP | ||||
7 | LYS | MET | PRO | TRP | ASN | GLN | ARG | ALA |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; H2O 95%; D2O 5%
sample_2: entity, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 95%; D2O 5%
sample_conditions_1: temperature: 273 K; pH: 7.0; pressure: 1 atm; ionic strength: 0 M
sample_conditions_2: temperature: 273 K; pH: 7.0; pressure: 1 atm; ionic strength: 0 M
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_2 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_2 |
Software:
XEASY, Bartels et al. - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
PDB | |
DBJ | BAB36952 BAE76780 BAG78445 BAI26930 BAI31960 |
EMBL | CAP77107 CAQ33005 CAQ99590 CAR04179 CAR09287 |
GB | AAC75715 AAG57776 AAN44189 AAN81669 AAP18017 |
REF | NP_311556 NP_417154 NP_708482 WP_001229436 WP_001229438 |
SP | P55734 |
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