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 25275

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25275
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: Solution structure of eEF1Bdelta CAR domain   PubMed: 25635048

Deposition date: 2014-10-09 Original release date: 2015-02-02

Authors: Wu, Huiwen; Feng, Yingang

Citation: Wu, Huiwen; Gong, Weibin; Yao, Xingzhe; Wang, Jinfeng; Perrett, Sarah; Feng, Yingang. "Evolutionarily Conserved Binding of Translationally-Controlled Tumor Protein to Eukaryotic Elongation Factor 1B"  J. Biol. Chem. 290, 8694-8710 (2015).

Assembly members:
entity, polymer, 44 residues, 5000.408 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: GPGSEDDDIDLFGSDNEEED KEAAQLREERLRQYAEKKAK KPAL

Data sets:
Data typeCount
13C chemical shifts173
15N chemical shifts44
1H chemical shifts274

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 44 residues - 5000.408 Da.

1   GLYPROGLYSERGLUASPASPASPILEASP
2   LEUPHEGLYSERASPASNGLUGLUGLUASP
3   LYSGLUALAALAGLNLEUARGGLUGLUARG
4   LEUARGGLNTYRALAGLULYSLYSALALYS
5   LYSPROALALEU

Samples:

sample_1: entity, [U-13C; U-15N], .02 – .08 mM; TRIS 20 mM; sodium chloride 200 mM; DSS 0.01%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 220 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

Felix, Accelrys Software Inc. - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

BMRB 25276
PDB
DBJ BAB14925 BAE01260 BAE02383 BAG36963 BAG56855
EMBL CAA79716
GB AAH00678 AAH07847 AAH09907 AAH12819 AAH62535
REF NP_001123525 NP_001123527 NP_001123528 NP_001123529 NP_001182132
SP P29692 Q4R3D4

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts