BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15014

Title: Solution structure of the RING domain from human TRAF6.   PubMed: 17327397

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

Data sets:
Data typeCount
13C chemical shifts256
15N chemical shifts61
1H chemical shifts413
heteronuclear NOE values54
T1 relaxation values55
T2 relaxation values55

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1polypeptide1
2zinc ion 12
3zinc ion 22

Entities:

Entity 1, polypeptide 63 residues - 7019.326 Da.

The N-terminal sequence GPLGS is an artefact from cloning.

1   GLYPROLEUGLYSERLYSTYRGLUCYSPRO
2   ILECYSLEUMETALALEUARGGLUALAVAL
3   GLNTHRPROCYSGLYHISARGPHECYSLYS
4   ALACYSILEILELYSSERILEARGASPALA
5   GLYHISLYSCYSPROVALASPASNGLUILE
6   LEULEUGLUASNGLNLEUPHEPROASPASN
7   PHEALALYS

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:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HACA(CO)CANHhsample_1isotropicsample_conditions_1
3D H(CC)-TOCSY-(CO)NNHsample_1isotropicsample_conditions_1
3D (H)CCTOCSY(CO)NNHsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
3D HNN(CO,CA)sample_1isotropicsample_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