BMRB Entry 5960

Name: 1H, 13C, 15N- Chemical Shift Assignments for Myristoylated HIV-1 Matrix Protein
Published: 2007-03-23

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PDB ID: 2h3q
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5960
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, 15N- Chemical Shift Assignments for Myristoylated HIV-1 Matrix Protein

Deposition date:

2003-10-01

Original release date:

2007-03-23

Authors:

Tang, Chun; Loeliger, Erin; Luncsford, Paz; Kinde, Isaac; Beckett, Dorothy; Summers, Michael

Citation:

Citation: Tang, Chun; Loeliger, Erin; Luncsford, Paz; Kinde, Isaac; Beckett, Dorothy; Summers, Michael. "From the Cover: Entropic switch regulates myristate exposure in the HIV-1 matrix protein" Proc. Natl. Acad. Sci. U.S.A. 101, 517-522 (2004).
PubMed: 14699046

Assembly members:

Assembly members:
p17, polymer, 132 residues, 228.371 Da.

Natural source:

Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus Human immunodeficiency virus 1

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p17: XGARASVLSGGELDKWEKIR LRPGGKKQYKLKHIVWASRE LERFAVNPGLLETSEGCRQI LGQLQPSLQTGSEELRSLYN TIAVLYCVHQRIDVKDTKEA LDKIEEEQNKSKKKAQQAAA DTGNNSQVSQNY

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
1H chemical shifts	581
15N chemical shifts	130
13C chemical shifts	500

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	matrix monomer	1

Entities:

Entity 1, matrix monomer 132 residues - 228.371 Da.

1

MYR

GLY

ALA

ARG

ALA

SER

VAL

LEU

SER

GLY

2

GLY

GLU

LEU

ASP

LYS

TRP

GLU

LYS

ILE

ARG

3

LEU

ARG

PRO

GLY

LYS

GLN

TYR

LYS

4

LEU

LYS

HIS

ILE

VAL

TRP

ALA

SER

ARG

GLU

5

LEU

GLU

ARG

PHE

ALA

VAL

ASN

PRO

GLY

LEU

6

LEU

GLU

THR

SER

GLU

GLY

CYS

ARG

GLN

ILE

7

LEU

GLY

GLN

LEU

GLN

PRO

SER

LEU

GLN

THR

8

GLY

SER

GLU

LEU

ARG

SER

LEU

TYR

ASN

9

THR

ILE

ALA

VAL

LEU

TYR

CYS

VAL

HIS

GLN

10

ARG

ILE

ASP

VAL

LYS

ASP

THR

LYS

GLU

ALA

11

LEU

ASP

LYS

ILE

GLU

GLN

ASN

LYS

12

SER

LYS

ALA

GLN

ALA

13

ASP

THR

GLY

ASN

SER

GLN

VAL

SER

GLN

14

ASN

TYR

Samples:

sample_1: p17, [U-13C; U-15N], 0.2 mM; sodium phosophate buffer 50 mM; NaCl 50 mM; DTT 5 mM; DTT 5 mM

cond_1: pH: 5.5; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	not available	cond_1
2D 1H-13C HMQC	sample_1	not available	cond_1
2D 1H-1H NOESY	sample_1	not available	cond_1
3D 13C-edited HMQC-NOESY	sample_1	not available	cond_1
2D 13C-edited HMQC-NOESY	sample_1	not available	cond_1
4D 13C, 13C-edited HMQC-NOESY-HMQC	sample_1	not available	cond_1
3D 15N- edited NOESY-HSQC	sample_1	not available	cond_1
3D HNCA	sample_1	not available	cond_1
3D HN(CO)CA	sample_1	not available	cond_1
3D HNCO	sample_1	not available	cond_1

Software:

NMRPIPE - processing

NMRVIEW v5.0.4 - processing

NMR spectrometers:

Bruker AVANCE 800 MHz
Bruker AVANCE 600 MHz

BMRB	15114 15116 18715 18716 5316 7250 7267 7275 7309
PDB	1HIW 1L6N 1UPH 2GOL 2H3F 2H3I 2H3Q 2H3V 2H3Z 2HMX 2JMG 2LYA 2LYB 2NV3 4JMU
DBJ	BAF34641 BAG48474
EMBL	CBI61180 CBI61181 CBI61182 CBI61183 CBI61184
GB	AAA44987 AAB00898 AAB60571 AAC28445 AAC29216
SP	P12493 P12497
AlphaFold	P12493 P12497