BMRB Entry 16887

Name: Backbone 1H, 13C, 15N Chemical Shift Assignments for HIV-2 unmyristoylated matrix protein
Published: 2010-08-12

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PDB ID: 2k4e
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16887
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone 1H, 13C, 15N Chemical Shift Assignments for HIV-2 unmyristoylated matrix protein

Deposition date:

2010-04-21

Original release date:

2010-08-12

Authors:

Saad, Jamil; Ablan, Sherimay; Ghanam, Ruba; Kim, Andrew; Andrews, Kalola; Nagashima, Kunio; Freed, Eric; Summers, Michael

Citation:

Citation: Saad, Jamil; Ablan, Sherimay; Ghanam, Ruba; Kim, Andrew; Andrews, Kalola; Nagashima, Kunio; Soheilian, Ferri; Freed, Eric; Summers, Michael. "Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting." J. Mol. Biol. 382, 434-447 (2008).
PubMed: 18657545

Assembly members:

Assembly members:
HIV2, polymer, 134 residues, 14899.383 Da.

Natural source:

Natural source: Common Name: Human immunodeficiency virus 2 Taxonomy ID: 11709 Superkingdom: virus Kingdom: not available Genus/species: Lentivirus HIV2

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HIV2: GARNSVLRGKKADELERIRL RPGGKKKYRLKHIVWAANKL DRFGLAESLLESKEGCQKIL TVLDPMVPTGSENLKSLFNT VCVIWCIHAEEKVKDTEGAK QIVRRHLVAETGTAEKMPST SRPTAPSSEKGGNY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	380
15N chemical shifts	126
1H chemical shifts	737

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HIV-2 unmyristoylated matrix protein	1

Entities:

Entity 1, HIV-2 unmyristoylated matrix protein 134 residues - 14899.383 Da.

1

GLY

ALA

ARG

ASN

SER

VAL

LEU

ARG

GLY

LYS

2

LYS

ALA

ASP

GLU

LEU

GLU

ARG

ILE

ARG

LEU

3

ARG

PRO

GLY

LYS

TYR

ARG

LEU

4

LYS

HIS

ILE

VAL

TRP

ALA

ASN

LYS

LEU

5

ASP

ARG

PHE

GLY

LEU

ALA

GLU

SER

LEU

6

GLU

SER

LYS

GLU

GLY

CYS

GLN

LYS

ILE

LEU

7

THR

VAL

LEU

ASP

PRO

MET

VAL

PRO

THR

GLY

8

SER

GLU

ASN

LEU

LYS

SER

LEU

PHE

ASN

THR

9

VAL

CYS

VAL

ILE

TRP

CYS

ILE

HIS

ALA

GLU

10

GLU

LYS

VAL

LYS

ASP

THR

GLU

GLY

ALA

LYS

11

GLN

ILE

VAL

ARG

HIS

LEU

VAL

ALA

GLU

12

THR

GLY

THR

ALA

GLU

LYS

MET

PRO

SER

THR

13

SER

ARG

PRO

THR

ALA

PRO

SER

GLU

LYS

14

GLY

ASN

TYR

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

BMRB	16888 16889
PDB	2K4E 2K4H 2K4I
EMBL	CAA28909
GB	AAB00763
PRF	1306388A
SP	P04584 P04590
AlphaFold	P04584 P04590

BMRB Entry 16887

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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