BMRB Entry 30739

Name: Solution NMR structure of the unmyristoylated feline immunodeficiency virus matrix protein
Published: 2020-07-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30739

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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 unmyristoylated feline immunodeficiency virus matrix protein

Deposition date: 2020-03-24 Original release date: 2020-07-20

Authors: Brown, J.; Summers, H.; Brown, L.; Marchant, J.; Canova, P.; O'Hern, C.; Abbott, S.; Nyaunu, C.; Maxwell, S.; Johnson, T.; Moser, M.; Carter, H.; Ablan, S.; Freed, E.; Summers, M.

Citation: Brown, J.; Summers, H.; Brown, L.; Marchant, J.; Canova, P.; O'Hern, C.; Abbott, S.; Nyaunu, C.; Maxwell, S.; Johnson, T.; Moser, M.; Carter, H.; Ablan, S.; Freed, E.; Summers, M.. "Solution NMR structure of the unmyristoylated feline immunodeficiency virus matrix protein" . ., .-..

Assembly members:
entity_1, polymer, 126 residues, 13988.002 Da.

Natural source: Common Name: FIV Taxonomy ID: 11673 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus FIV

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

Entity Sequences (FASTA):
entity_1: GNGQGRDWKMAIKRCSNVAV GVGGKSKKFGEGNFRWAIRM ANVSTGREPGDIPETLDQLR LVICDLQERREKFGSSKEID MAIVTLKVFAVAGLLNMTVS TAAAAENMYSQMGLDTRPHH HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	472
15N chemical shifts	124
1H chemical shifts	611

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 126 residues - 13988.002 Da.

1

GLY

ASN

GLY

GLN

GLY

ARG

ASP

TRP

LYS

MET

2

ALA

ILE

LYS

ARG

CYS

SER

ASN

VAL

ALA

VAL

3

GLY

VAL

GLY

LYS

SER

LYS

PHE

GLY

4

GLU

GLY

ASN

PHE

ARG

TRP

ALA

ILE

ARG

MET

5

ALA

ASN

VAL

SER

THR

GLY

ARG

GLU

PRO

GLY

6

ASP

ILE

PRO

GLU

THR

LEU

ASP

GLN

LEU

ARG

7

LEU

VAL

ILE

CYS

ASP

LEU

GLN

GLU

ARG

8

GLU

LYS

PHE

GLY

SER

LYS

GLU

ILE

ASP

9

MET

ALA

ILE

VAL

THR

LEU

LYS

VAL

PHE

ALA

10

VAL

ALA

GLY

LEU

ASN

MET

THR

VAL

SER

11

THR

ALA

GLU

ASN

MET

TYR

SER

12

GLN

MET

GLY

LEU

ASP

THR

ARG

PRO

HIS

13

HIS

Samples:

sample_1: sodium phosphate 50 mM; DTT 10 mM; sodium chloride 5 mM; glucose 4 g/L; ammonium chloride, [U-99% 15N], 1 g/L; Unmyristoylated Feline Immunodeficiency Virus Matrix Protein, [U-15N], 300 uM

sample_2: sodium phosphate 50 mM; DTT, [U-98% 2H], 10 mM; sodium chloride 5 mM; Unmyristoylated Feline Immunodeficiency Virus Matrix Protein 300 uM

sample_3: sodium phosphate 50 mM; DTT 10 mM; sodium chloride 5 mM; glucose, [U-99% 13C], 4 g/L; ammonium chloride, [U-99% 15N], 1 g/L; Unmyristoylated Feline Immunodeficiency Virus Matrix Protein, [U-13C; U-15N], 300 uM

sample_4: sodium phosphate 50 mM; DTT, [U-98% 2H], 10 mM; sodium chloride 5 mM; glucose, [U-99% 13C], 4 g/L; ammonium chloride 1 g/L; Unmyristoylated Feline Immunodeficiency Virus Matrix Protein, [U-13C], 300 uM

sample_conditions_1: ionic strength: 5 mM; pH: 8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 5 mM; pH: 8 pD; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 5 mM; pH: 5; pressure: 1 atm; temperature: 298 K

sample_conditions_4: ionic strength: 5 mM; pH: 5 pD; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_4
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_3
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_3
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_3
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_3
2D 1H-13 HMQC	sample_4	isotropic	sample_conditions_2
4D HMQC-NOESY-HMQC	sample_4	isotropic	sample_conditions_2
4D HSQC-NOESY-HMQC	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_3
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_3	isotropic	sample_conditions_3
3D HN(CA)CO	sample_3	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

NMRFx, Johnson, One Moon Scientific - processing

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

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

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

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMR spectrometers:

Bruker DMX 600 MHz
Bruker DMX 500 MHz

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