BMRB Entry 6822
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR6822
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: The Structure of the Hamp Domain Implies a Rotational Mechanism in Transmembrane Signalling PubMed: 16959572
Deposition date: 2005-09-09 Original release date: 2006-10-19
Authors: Coles, M.; Truffault, V.; Hulko, M.; Martin, J.; Lupas, A.
Citation: Hulko, M.; Berndt, F.; Gruber, M.; Linder, J.; Truffault, V.; Schultz, A.; Martin, J.; Schultz, J.; Lupas, A.; Coles, M.. "The HAMP domain structure implies helix rotation in transmembrane signaling" Cell 126, 929-940 (2006).
Assembly members:
hypothetical protein AF1503, polymer, 56 residues, Formula weight is not available
Natural source: Common Name: Archaeoglobus fulgidus Taxonomy ID: 2234 Superkingdom: Archaea Kingdom: not available Genus/species: Archaeoglobus fulgidus
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
hypothetical protein AF1503: GSSTITRPIIELSNTADKIA
EGNLEAEVPHQNRADEIGIL
AKSIERLRRSLKVAME
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 229 |
| 15N chemical shifts | 55 |
| 1H chemical shifts | 397 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hypothetical protein AF1503 chain A | 1 |
| 2 | hypothetical protein AF1503 chain B | 1 |
Entities:
Entity 1, hypothetical protein AF1503 chain A 56 residues - Formula weight is not available
| 1 | GLY | SER | SER | THR | ILE | THR | ARG | PRO | ILE | ILE | ||||
| 2 | GLU | LEU | SER | ASN | THR | ALA | ASP | LYS | ILE | ALA | ||||
| 3 | GLU | GLY | ASN | LEU | GLU | ALA | GLU | VAL | PRO | HIS | ||||
| 4 | GLN | ASN | ARG | ALA | ASP | GLU | ILE | GLY | ILE | LEU | ||||
| 5 | ALA | LYS | SER | ILE | GLU | ARG | LEU | ARG | ARG | SER | ||||
| 6 | LEU | LYS | VAL | ALA | MET | GLU |
Samples:
sample_1: hypothetical protein AF1503 1.0 mM; phosphate buffer 20 mM; NACL 150 mM; H2O 90%; D2O 10%
sample_2: hypothetical protein AF1503, [U-15N], 1.0 mM; phosphate buffer 20 mM; NACL 150 mM; H2O 90%; D2O 10%
sample_3: hypothetical protein AF1503, [U-13C; U-15N], 1.0 mM; phosphate buffer 20 mM; NACL 150 mM; H2O 90%; D2O 10%
sample_cond_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | not available | not available | not available |
| 2D NOESY | not available | not available | not available |
| HNHA | not available | not available | not available |
| 2D 12C-FILTERED/13C-EDITED NOESY | not available | not available | not available |
| 3D-NNH-NOESY | not available | not available | not available |
| 3D-CNH-NOESY | not available | not available | not available |
Software:
X-PLOR vNIH-2.9.7 - refinement, structure solution
xwinnmr v3.5 - processing
SPARKY v3.110 - data analysis
NMR spectrometers:
- Bruker DMX 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts