BMRB Entry 11146

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PDB ID: 2e9h
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11146
MolProbity Validation Chart

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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 the eIF-5_eIF-2B domain from human Eukaryotic translation initiation factor 5

Deposition date:

2010-03-31

Original release date:

2011-04-01

Authors:

Tomizawa, T.; Tochio, N.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Tomizawa, T.; Tochio, N.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.. "Solution structure of the eIF-5_eIF-2B domain from human Eukaryotic translation initiation factor 5" .

Assembly members:

Assembly members:
eIF-5_eIF-2B domain, polymer, 157 residues, Formula weight is not available
ZN, non-polymer, 65.409 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: cell free synthesis Host organism: E. coli - cell free Vector: P060411-05

Entity Sequences (FASTA):

Entity Sequences (FASTA):
eIF-5_eIF-2B domain: GSSGSSGMSVNVNRSVSDQF YRYKMPRLIAKVEGKGNGIK TVIVNMVDVAKALNRPPTYP TKYFGCELGAQTQFDVKNDR YIVNGSHEANKLQDMLDGFI KKFVLCPECENPETDLHVNP KKQTIGNSCKACGYRGMLDT HHKLCTFILKNPPENSD

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	677
15N chemical shifts	159
1H chemical shifts	1079

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	eIF-5_eIF-2B domain	1
2	ZINC ION	2

Entities:

Entity 1, eIF-5_eIF-2B domain 157 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

MET

SER

VAL

2

ASN

VAL

ASN

ARG

SER

VAL

SER

ASP

GLN

PHE

3

TYR

ARG

TYR

LYS

MET

PRO

ARG

LEU

ILE

ALA

4

LYS

VAL

GLU

GLY

LYS

GLY

ASN

GLY

ILE

LYS

5

THR

VAL

ILE

VAL

ASN

MET

VAL

ASP

VAL

ALA

6

LYS

ALA

LEU

ASN

ARG

PRO

THR

TYR

PRO

7

THR

LYS

TYR

PHE

GLY

CYS

GLU

LEU

GLY

ALA

8

GLN

THR

GLN

PHE

ASP

VAL

LYS

ASN

ASP

ARG

9

TYR

ILE

VAL

ASN

GLY

SER

HIS

GLU

ALA

ASN

10

LYS

LEU

GLN

ASP

MET

LEU

ASP

GLY

PHE

ILE

11

LYS

PHE

VAL

LEU

CYS

PRO

GLU

CYS

GLU

12

ASN

PRO

GLU

THR

ASP

LEU

HIS

VAL

ASN

PRO

13

LYS

GLN

THR

ILE

GLY

ASN

SER

CYS

LYS

14

ALA

CYS

GLY

TYR

ARG

GLY

MET

LEU

ASP

THR

15

HIS

LYS

LEU

CYS

THR

PHE

ILE

LEU

LYS

16

ASN

PRO

GLU

ASN

SER

ASP

Entity 2, ZINC ION - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: eIF-5_eIF-2B domain, [U-13C; U-15N], 1.32 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	isotropic	condition_1
3D 15N-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20060524, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9747, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

Bruker AVANCE 900 MHz

PDB	2E9H 2G2K
DBJ	BAB15593 BAC36325 BAE34918 BAE36460 BAE37319
EMBL	CAB45711 CAD97610 CAG32503 CAG32993 CAH93306
GB	AAA41112 AAC50572 AAH07728 AAH15630 AAH19769
REF	NP_001006488 NP_001008209 NP_001126945 NP_001180152 NP_001960
SP	P55010 P59325 Q07205 Q5R4L0
TPG	DAA17435
AlphaFold	P55010 P59325 Q07205 Q5R4L0