BMRB Entry 34144

Name: NMR structure of TIA-1 RRM1 domain
Published: 2017-06-23

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PDB ID: 5o2v
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34144
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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:

NMR structure of TIA-1 RRM1 domain

Deposition date:

2017-05-22

Original release date:

2017-06-23

Authors:

Jagtap, P.

Citation:

Citation: Sonntag, Miriam; Jagtap, Pravin Kumar Ankush; Simon, Bernd; Appavou, Marie-Sousai; Geerlof, Arie; Stehle, Ralf; Gabel, Frank; Hennig, Janosch; Sattler, Michael. "Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins" Angew. Chem. Int. Ed. Engl. 56, 9322-9325 (2017).
PubMed: 28636238

Assembly members:

Assembly members:
entity_1, polymer, 92 residues, 10275.843 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEDEMPKTLYVGNLSRDVTE ALILQLFSQIGPCKNCKMIM DTAGNDPYCFVEFHEHRHAA AALAAMNGRKIMGKEVKVNW ATTPSSQKKDTS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	383
15N chemical shifts	88
1H chemical shifts	599

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 92 residues - 10275.843 Da.

1

MET

GLU

ASP

GLU

MET

PRO

LYS

THR

LEU

TYR

2

VAL

GLY

ASN

LEU

SER

ARG

ASP

VAL

THR

GLU

3

ALA

LEU

ILE

LEU

GLN

LEU

PHE

SER

GLN

ILE

4

GLY

PRO

CYS

LYS

ASN

CYS

LYS

MET

ILE

MET

5

ASP

THR

ALA

GLY

ASN

ASP

PRO

TYR

CYS

PHE

6

VAL

GLU

PHE

HIS

GLU

HIS

ARG

HIS

ALA

7

ALA

LEU

ALA

MET

ASN

GLY

ARG

LYS

8

ILE

MET

GLY

LYS

GLU

VAL

LYS

VAL

ASN

TRP

9

ALA

THR

PRO

SER

GLN

LYS

ASP

10

THR

SER

Samples:

sample_1: entity_1, [U-15N; U-13C], 0.5 mM

sample_2: entity_1, [U-15N], 0.5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement

Analysis, CCPN - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker AvanceIII 800 MHz
Bruker AvanceIII 600 MHz

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