BMRB Entry 30404

Name: NMR structure of the Rous sarcoma virus matrix protein (M-domain) in the presence of myo-inositol hexakisphosphate
Published: 2018-10-15

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PDB ID: 6ce5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30404
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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 the Rous sarcoma virus matrix protein (M-domain) in the presence of myo-inositol hexakisphosphate

Deposition date:

2018-02-11

Original release date:

2018-10-15

Authors:

Vlach, J.; Saad, J.

Citation:

Citation: Vlach, Jiri; Eastep, Gunnar; Ghanam, Ruba; Watanabe, Susan; Carter, Carol; Saad, Jamil. "Structural basis for targeting avian sarcoma virus Gag polyprotein to the plasma membrane for virus assembly" J. Biol. Chem. 293, 18828-18840 (2018).
PubMed: 30309983

Assembly members:

Assembly members:
entity_1, polymer, 87 residues, 9209.771 Da.

Natural source:

Natural source: Common Name: RSV-PrC Taxonomy ID: 11888 Superkingdom: Viruses Kingdom: not available Genus/species: Alpharetrovirus Rous sarcoma virus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SEAVIKVISSACKTYCGKTS PSKKEIGAMLSLLQKEGLLM SPSDLYSPGSWDPITAALSQ RAMILGKSGELKTWGLVLGA LKAAREE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	379
15N chemical shifts	87
1H chemical shifts	615

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 87 residues - 9209.771 Da.

1

SER

GLU

ALA

VAL

ILE

LYS

VAL

ILE

SER

2

ALA

CYS

LYS

THR

TYR

CYS

GLY

LYS

THR

SER

3

PRO

SER

LYS

GLU

ILE

GLY

ALA

MET

LEU

4

SER

LEU

GLN

LYS

GLU

GLY

LEU

MET

5

SER

PRO

SER

ASP

LEU

TYR

SER

PRO

GLY

SER

6

TRP

ASP

PRO

ILE

THR

ALA

LEU

SER

GLN

7

ARG

ALA

MET

ILE

LEU

GLY

LYS

SER

GLY

GLU

8

LEU

LYS

THR

TRP

GLY

LEU

VAL

LEU

GLY

ALA

9

LEU

LYS

ALA

ARG

GLU

Samples:

sample_1: Matrix protein, [U-95% 15N], 0.5 mM; sodium phosphate 50 mM; tcep 2 mM; IP6 2 mM

sample_2: Matrix protein, [U-95% 13C; U-95% 15N], 0.5 mM; sodium phosphate 50 mM; tcep 2 mM; IP6 2 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1

Software:

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

Analysis, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

unio, Herrmann - structure calculation

NMR spectrometers:

Bruker AvanceII 700 MHz

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