BMRB Entry 25573

Name: NMR Structure of the Myristylated Feline Immunodeficiency Virus Matrix Protein
Published: 2015-05-26

Click here to enlarge.

PDB ID: 2n1r
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25573
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR Structure of the Myristylated Feline Immunodeficiency Virus Matrix Protein

Deposition date:

2015-04-15

Original release date:

2015-05-26

Authors:

Brown, Lola; Cox, Cassiah; Button, Ryan; Baptiste, Janae; Bahlow, Kennedy; Spurrier, Vaughn; Luttge, Benjamin; Kuo, Lillian; Freed, Eric; Summers, Michael; Kyser, Jenna; Summers, Holly

Citation:

Citation: Brown, Lola; Cox, Cassiah; Baptiste, Janae; Summers, Holly; Button, Ryan; Bahlow, Kennedy; Spurrier, Vaughn; Kyser, Jenna; Luttge, Benjamin; Kuo, Lillian; Freed, Eric; Summers, Michael. "NMR structure of the myristylated feline immunodeficiency virus matrix protein" Viruses 7, 2210-2229 (2015).
PubMed: 25941825

Assembly members:

Assembly members:
Feline_Immunodeficiency_Virus_Matrix_Protein, polymer, 135 residues, 14729.074 Da.

Natural source:

Natural source: Common Name: domestic cat Taxonomy ID: 9685 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Felis catus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11/pET17

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Feline_Immunodeficiency_Virus_Matrix_Protein: XGNGASRDWKMAIKRCSNVA VGVGGKSKKFGEGNFRWAIR MANVSTGREPGDIPETLDQL RLVICDLQERREKFGSSKEI DMAIVTLKVFAVAGLLNMTV STAAAAENMYSQMGLDTRPS MKEAGGKEEGPPQAY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	321
15N chemical shifts	120
1H chemical shifts	560

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Feline Immunodeficiency Virus Matrix Protein	1

Entities:

Entity 1, Feline Immunodeficiency Virus Matrix Protein 135 residues - 14729.074 Da.

1

MYR

GLY

ASN

GLY

ALA

SER

ARG

ASP

TRP

LYS

2

MET

ALA

ILE

LYS

ARG

CYS

SER

ASN

VAL

ALA

3

VAL

GLY

VAL

GLY

LYS

SER

LYS

PHE

4

GLY

GLU

GLY

ASN

PHE

ARG

TRP

ALA

ILE

ARG

5

MET

ALA

ASN

VAL

SER

THR

GLY

ARG

GLU

PRO

6

GLY

ASP

ILE

PRO

GLU

THR

LEU

ASP

GLN

LEU

7

ARG

LEU

VAL

ILE

CYS

ASP

LEU

GLN

GLU

ARG

8

ARG

GLU

LYS

PHE

GLY

SER

LYS

GLU

ILE

9

ASP

MET

ALA

ILE

VAL

THR

LEU

LYS

VAL

PHE

10

ALA

VAL

ALA

GLY

LEU

ASN

MET

THR

VAL

11

SER

THR

ALA

GLU

ASN

MET

TYR

12

SER

GLN

MET

GLY

LEU

ASP

THR

ARG

PRO

SER

13

MET

LYS

GLU

ALA

GLY

LYS

GLU

GLY

14

PRO

GLN

ALA

TYR

Samples:

90_H2O-15N_labeled: sodium phosphate 50 mM; sodium chloride 150 mM; DTT 10 mM; ammonium chloride, [U-99% 15N], 1 g/L; glucose 4 g/L; MYRISTIC ACID 0.5 mg/mL; H2O 90%; D2O 10%; Feline Immunodeficiency Virus Matrix Protein, [U-90% 15N], mM

D2O-13C: sodium phosphate 50 mM; sodium chloride 150 mM; DTT 10 mM; glucose, [U-100% 13C], 4 g/L; ammonium chloride 1 g/L; MYRISTIC ACID 0.5 mg/mL; D2O 100%; Feline Immunodeficiency Virus Matrix Protein, [U-100% 13C], mM

D2O-13C_1: sodium phosphate 50 mM; sodium chloride 150 mM; DTT 10 mM; glucose, [U-100% 13C], 4 g/L; ammonium chloride 1 g/L; MYRISTIC ACID 0.5 mg/mL; D2O 100%; Feline Immunodeficiency Virus Matrix Protein, [U-100% 13C], mM

D2O-13C_2: sodium phosphate 50 mM; sodium chloride 150 mM; DTT 10 mM; glucose, [U-100% 13C], 4 g/L; ammonium chloride 1 g/L; MYRISTIC ACID 0.5 mg/mL; D2O 100%; Feline Immunodeficiency Virus Matrix Protein, [U-100% 13C], mM

90_H2O-15N_labeled_1: sodium phosphate 50 mM; sodium chloride 150 mM; DTT 10 mM; ammonium chloride, [U-99% 15N], 1 g/L; glucose 4 g/L; MYRISTIC ACID 0.5 mg/mL; H2O 90%; D2O 10%; Feline Immunodeficiency Virus Matrix Protein, [U-90% 15N], mM

standard: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N-1HN HSQC	90_H2O-15N_labeled_1	isotropic	standard
13C-1HN HNCA	90_H2O-15N_labeled	isotropic	standard
13C-1HN HN(CO)CA	90_H2O-15N_labeled	isotropic	standard
CBCANH	90_H2O-15N_labeled	isotropic	standard
CBCA(CO)NH	90_H2O-15N_labeled	isotropic	standard
CARBON-NITROGEN NOESY (CNNOE)	90_H2O-15N_labeled	isotropic	standard
15N EDITED 3D NOESY	90_H2O-15N_labeled_1	isotropic	standard
1H-13C HMQC	D2O-13C_2	isotropic	standard
CARBON CARBON NOSEY (CCNOE)	D2O-13C_2	isotropic	standard
1H-1H NOESY	D2O-13C	isotropic	standard
13C-1H HMQC NOESY	D2O-13C	isotropic	standard

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker DMX 800 MHz
Bruker DMX 600 MHz

PDB	2N1R 4IC9
EMBL	CAA40317
GB	AAB59936
REF	NP_040972
SP	P16087
AlphaFold	P16087