BMRB Entry 15543

Name: Solution conformation of RNA-bound NELF-E RRM
Published: 2008-11-03

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PDB ID: 2jx2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15543
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 conformation of RNA-bound NELF-E RRM

Deposition date:

2007-11-02

Original release date:

2008-11-03

Authors:

Jampani, N. Rao; Schweimer, Kristian; Wenzel, Sabine; Woehrl, Birgitta; Roesch, Paul

Citation:

Citation: Jampani, N. Rao; Schweimer, Kristian; Wenzel, Sabine; Woehrl, Birgitta; Roesch, Paul. "RRMNELF-E RRM Undergoes Major Structural Changes in Flexible Protein Regions on Target RNA Binding" Biochemistry 47, 3756-3761 (2008).
PubMed: 18303858

Assembly members:

Assembly members:
rna_bound_nelfe-rrm, polymer, 121 residues, 9494.886 Da.
TAR(49-57), polymer, 9 residues, Formula weight is not available

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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rna_bound_nelfe-rrm: MGSSHHHHHHSSGLVPRGSH MGPFRRSDSFPERRAPRKGN TLYVYGEDMTPTLLRGAFSP FGNIIDLSMDPPRNCAFVTY EKMESADQAVAELNGTQVES VQLKVNIARKQPMLDAATGK S
TAR(49-57): UAGGGAACC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	224
15N chemical shifts	91
1H chemical shifts	510

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	nelfe-rrm	1
2	TAR(49-57)	2

Entities:

Entity 1, nelfe-rrm 121 residues - 9494.886 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

GLY

PRO

PHE

ARG

SER

ASP

SER

PHE

4

PRO

GLU

ARG

ALA

PRO

ARG

LYS

GLY

ASN

5

THR

LEU

TYR

VAL

TYR

GLY

GLU

ASP

MET

THR

6

PRO

THR

LEU

ARG

GLY

ALA

PHE

SER

PRO

7

PHE

GLY

ASN

ILE

ASP

LEU

SER

MET

ASP

8

PRO

ARG

ASN

CYS

ALA

PHE

VAL

THR

TYR

9

GLU

LYS

MET

GLU

SER

ALA

ASP

GLN

ALA

VAL

10

ALA

GLU

LEU

ASN

GLY

THR

GLN

VAL

GLU

SER

11

VAL

GLN

LEU

LYS

VAL

ASN

ILE

ALA

ARG

LYS

12

GLN

PRO

MET

LEU

ASP

ALA

THR

GLY

LYS

13

SER

Entity 2, TAR(49-57) 9 residues - Formula weight is not available

1

U

A

G

A

C

Samples:

sample_1: rna bound nelfe-rrm, [U-98% 13C; U-98% 15N], 0.4 mM; TAR(49-57) 0.8 mM

sample_conditions_1: pH: 6.9; 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 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

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 800 MHz

PDB	2BZ2 2JX2
DBJ	BAB28206 BAE20893 BAE27605 BAG62393 BAG63891
EMBL	CAA34231 CAE83971 CAN87695 CAN87696
GB	AAA36308 AAA39680 AAB67979 AAC37523 AAC84161
REF	NP_001039328 NP_001039329 NP_001069672 NP_001095295 NP_001159373
SP	P18615 P19426 Q0V898
TPG	DAA16391
AlphaFold	P18615 P19426 Q0V898