BMRB Entry 30289

Name: Solution NMR Structure of the C-terminal Headpiece Domain of Villin 4 from A.thaliana, the First Non-Vertebrate Headpiece Structure
Published: 2017-05-08

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PDB ID: 5vnt
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30289
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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 NMR Structure of the C-terminal Headpiece Domain of Villin 4 from A.thaliana, the First Non-Vertebrate Headpiece Structure

Deposition date: 2017-05-01 Original release date: 2017-05-08

Authors: Miears, H.; Smirnov, S.

Citation: Miears, H.; Smirnov, S.. "Solution NMR Structure of the C-terminal Headpiece Domain of Villin 4 from A.thaliana, the First Non-Vertebrate Headpiece Structure" . ., .-..

Assembly members:
entity_1, polymer, 63 residues, 7500.623 Da.

Natural source: Common Name: Mouse-ear cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

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

Entity Sequences (FASTA):
entity_1: LPAHPYDRLKTTSTDPVSDI DVTRREAYLSSEEFKEKFGM TKEAFYKLPKWKQNKFKMAV QLF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	253
15N chemical shifts	66
1H chemical shifts	320

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 63 residues - 7500.623 Da.

1

LEU

PRO

ALA

HIS

PRO

TYR

ASP

ARG

LEU

LYS

2

THR

SER

THR

ASP

PRO

VAL

SER

ASP

ILE

3

ASP

VAL

THR

ARG

GLU

ALA

TYR

LEU

SER

4

SER

GLU

PHE

LYS

GLU

LYS

PHE

GLY

MET

5

THR

LYS

GLU

ALA

PHE

TYR

LYS

LEU

PRO

LYS

6

TRP

LYS

GLN

ASN

LYS

PHE

LYS

MET

ALA

VAL

7

GLN

LEU

PHE

Samples:

sample_1: PIPES, none, 20.0 mM; atVHP, none, 1.0 mM; sodium azide, none, 0.01%; sodium chloride, none, 50 mM

sample_2: PIPES, none, 20.0 mM; atVHP, none, 1.0 mM; sodium azide, none, 0.01%; sodium chloride, none, 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N-HSQC	sample_1	isotropic	sample_conditions_1
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 1H-15N NOESY	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 C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCC(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRPipe v8.9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v9.0, Johnson, One Moon Scientific - peak picking

TOPSPIN v3.1, Bruker Biospin - collection

NMR spectrometers:

Bruker AvanceIII 500 MHz
Bruker AvanceIII 600 MHz
Bruker AvanceIII 850 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts