BMRB Entry 15014
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15014
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Title: Solution structure of the RING domain from human TRAF6. PubMed: 17327397
Deposition date: 2006-11-02 Original release date: 2007-04-24
Authors: Mercier, Pascal; Lewis, Michael; Hau, David; Saltibus, Linda; Xiao, Wei; Spyracopoulos, Leo
Citation: Mercier, Pascal; Lewis, Michael; Hau, David; Saltibus, Linda; Xiao, Wei; Spyracopoulos, Leo. "Structure, Interactions, and Dynamics of the RING Domain from Human TRAF6" Protein Sci. 16, 602-614 (2007).
Assembly members:
hTRAF6, polymer, 63 residues, 7019.326 Da.
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
hTRAF6: GPLGSKYECPICLMALREAV
QTPCGHRFCKACIIKSIRDA
GHKCPVDNEILLENQLFPDN
FAK
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
Data type | Count |
13C chemical shifts | 256 |
15N chemical shifts | 61 |
1H chemical shifts | 413 |
heteronuclear NOE values | 54 |
T1 relaxation values | 55 |
T2 relaxation values | 55 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | polypeptide | 1 |
2 | zinc ion 1 | 2 |
3 | zinc ion 2 | 2 |
Entities:
Entity 1, polypeptide 63 residues - 7019.326 Da.
The N-terminal sequence GPLGS is an artefact from cloning.
1 | GLY | PRO | LEU | GLY | SER | LYS | TYR | GLU | CYS | PRO | ||||
2 | ILE | CYS | LEU | MET | ALA | LEU | ARG | GLU | ALA | VAL | ||||
3 | GLN | THR | PRO | CYS | GLY | HIS | ARG | PHE | CYS | LYS | ||||
4 | ALA | CYS | ILE | ILE | LYS | SER | ILE | ARG | ASP | ALA | ||||
5 | GLY | HIS | LYS | CYS | PRO | VAL | ASP | ASN | GLU | ILE | ||||
6 | LEU | LEU | GLU | ASN | GLN | LEU | PHE | PRO | ASP | ASN | ||||
7 | PHE | ALA | LYS |
Entity 2, zinc ion 1 - Zn - 65.409 Da.
1 | ZN |
Samples:
sample_1: hTRAF6, [U-99% 13C; U-99% 15N], 0.5 ± 0.1 mM; phosphate mM; NaCl mM; DTT mM; DSS mM; H2O%; D2O%
sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; pressure: 1 atm; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D HNHB | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HACA(CO)CANHh | sample_1 | isotropic | sample_conditions_1 |
3D H(CC)-TOCSY-(CO)NNH | sample_1 | isotropic | sample_conditions_1 |
3D (H)CCTOCSY(CO)NNH | sample_1 | isotropic | sample_conditions_1 |
2D (HB)CB(CGCD)HD | sample_1 | isotropic | sample_conditions_1 |
2D (HB)CB(CGCDCE)HE | sample_1 | isotropic | sample_conditions_1 |
3D HNN(CO,CA) | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe v2.5 Rev 2006.184.15.37, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - processing
CYANA v2.1, P Guntert, C Mumenthaler and K Wuthrich - structure solution
NMRView v6.5, B Johnson, One Moon Scientific - chemical shift assignment
ProcheckNMR v3.5.4, RA Laskowski and M MacArthur - quality assessment
X-PLOR NIH v2.15, CD Schwieters, JJ Kuszewski, N Tjandra and GM Clore - refinement, structure solution
VNMRJ v2.1, Varian - collection
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Related Database Links:
SWS | Q9Y4K3 |
BMRB | 11340 |
PDB | |
DBJ | BAA12705 BAC30850 BAE33263 BAF85667 BAG10993 |
EMBL | CAE54432 |
GB | AAB38751 AAH31052 AAH60705 AAI02523 AAO38054 |
REF | NP_001029833 NP_001098756 NP_001129268 NP_001290202 NP_001292890 |
SP | A7XUJ6 B6CJY4 B6CJY5 P70196 Q3ZCC3 |
TPG | DAA21840 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts