BMRB Entry 11601

Name: pET22-hESRP1-RRM3
Published: 2016-01-29

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PDB ID: 2rvj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11601
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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:

pET22-hESRP1-RRM3

Deposition date:

2015-10-23

Original release date:

2016-01-29

Authors:

Yang, Yinshan; Allemand, Frederic; Guichou, Jean-Francois; Labesse, Gilles

Citation:

Citation: Yang, Yinshan; Allemand, Frederic; Guichou, Jean-Francois; Labesse, Gilles. "NMR structure of hESRP1-RRM3" .

Assembly members:

Assembly members:
hESRP1-RRM3, polymer, 104 residues, 11834.749 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22-hESRP1-RRM3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hESRP1-RRM3: MPPTNVRDCIRLRGLPYAAT IEDILDFLGEFATDIRTHGV HMVLNHQGRPSGDAFIQMKS ADRAFMAAQKCHKKNMKDRY VEVFQCSAEEMNFVLMGGTL NRLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	289
15N chemical shifts	97
1H chemical shifts	205

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hESRP1-RRM3	1

Entities:

Entity 1, hESRP1-RRM3 104 residues - 11834.749 Da.

1

MET

PRO

THR

ASN

VAL

ARG

ASP

CYS

ILE

2

ARG

LEU

ARG

GLY

LEU

PRO

TYR

ALA

THR

3

ILE

GLU

ASP

ILE

LEU

ASP

PHE

LEU

GLY

GLU

4

PHE

ALA

THR

ASP

ILE

ARG

THR

HIS

GLY

VAL

5

HIS

MET

VAL

LEU

ASN

HIS

GLN

GLY

ARG

PRO

6

SER

GLY

ASP

ALA

PHE

ILE

GLN

MET

LYS

SER

7

ALA

ASP

ARG

ALA

PHE

MET

ALA

GLN

LYS

8

CYS

HIS

LYS

ASN

MET

LYS

ASP

ARG

TYR

9

VAL

GLU

VAL

PHE

GLN

CYS

SER

ALA

GLU

10

MET

ASN

PHE

VAL

LEU

MET

GLY

THR

LEU

11

ASN

ARG

LEU

GLU

Samples:

sample_1: hESRP1-RRM3, [U-99% 13C; U-99% 15N], 0.6 mM; D2O, [U-2H], 10%; H2O 90%; Na2HPO4/KH2PO4 20 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 5.4; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker DRX 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks