BMRB Entry 25275

Name: Solution structure of eEF1Bdelta CAR domain
Published: 2015-02-02

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PDB ID: 2mvm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25275
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of eEF1Bdelta CAR domain

Deposition date:

2014-10-09

Original release date:

2015-02-02

Authors:

Wu, Huiwen; Feng, Yingang

Citation:

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).
PubMed: 25635048

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPGSEDDDIDLFGSDNEEED KEAAQLREERLRQYAEKKAK KPAL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	173
15N chemical shifts	44
1H chemical shifts	274

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 44 residues - 5000.408 Da.

1

GLY

PRO

GLY

SER

GLU

ASP

ILE

ASP

2

LEU

PHE

GLY

SER

ASP

ASN

GLU

ASP

3

LYS

GLU

ALA

GLN

LEU

ARG

GLU

ARG

4

LEU

ARG

GLN

TYR

ALA

GLU

LYS

ALA

LYS

5

LYS

PRO

ALA

LEU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHANH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-COSY	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

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

BMRB	25276
PDB	2MVM 2MVN
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
AlphaFold	P29692 Q4R3D4