BMRB Entry 15972

Name: 1H, 13C and 15N resonance assignments of the PDZ of MAST205 in complex with the C-terminal tail from the rabies virus glycoprotein
Published: 2009-01-15

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15972

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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:

1H, 13C and 15N resonance assignments of the PDZ of MAST205 in complex with the C-terminal tail from the rabies virus glycoprotein

Deposition date:

2008-10-03

Original release date:

2009-01-15

Authors:

Wolff, Nicolas; Terrien, Elouan; Simenel, Catherine; Lafon, Monique; Delepierre, Muriel

Citation:

Citation: Terrien, Elouan; Simenel, Catherine; Prehaud, Christophe; Buc, Henri; Delepierre, Muriel; Lafon, Monique; Wolff, Nicolas. "1H, 13C and 15N resonance assignments of the PDZ of microtubule-associated serine/threonine kinase 205 (MAST205) in complex with the C-terminal motif from the rabies virus glycoprotein" Biomol. NMR Assignments 3, 45-48 (2009).
PubMed: 19636944

Assembly members:

Assembly members:
Mast205, polymer, 96 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PDEST15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Mast205: GGSMRPPIIIHRAGKKYGFT LRAIRVYMGDSDVYTVHHMV WHVEDGGPASEAGLRQGDLI THVNGEPVHGLVHTEVVELI LKSGNKVAISTTPLEN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	402
15N chemical shifts	93
1H chemical shifts	645

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit 1	1

Entities:

Entity 1, subunit 1 96 residues - Formula weight is not available

1

GLY

SER

MET

ARG

PRO

ILE

2

HIS

ARG

ALA

GLY

LYS

TYR

GLY

PHE

THR

3

LEU

ARG

ALA

ILE

ARG

VAL

TYR

MET

GLY

ASP

4

SER

ASP

VAL

TYR

THR

VAL

HIS

MET

VAL

5

TRP

HIS

VAL

GLU

ASP

GLY

PRO

ALA

SER

6

GLU

ALA

GLY

LEU

ARG

GLN

GLY

ASP

LEU

ILE

7

THR

HIS

VAL

ASN

GLY

GLU

PRO

VAL

HIS

GLY

8

LEU

VAL

HIS

THR

GLU

VAL

GLU

LEU

ILE

9

LEU

LYS

SER

GLY

ASN

LYS

VAL

ALA

ILE

SER

10

THR

PRO

LEU

GLU

ASN

Samples:

sample_1: Tris; NaCl, [U-100% 13C; U-100% 15N], 800 uM; Mast205 800 uM; H2O 88%; D2O 12%

sample_conditions_1: ionic strength: 150 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	16967
PDB	2KQF 2KYL
DBJ	BAA34527 BAB40778
EMBL	CAD38775
GB	AAH65499 EAX06948 EAX06949 EFB27522 EHB01606
REF	NP_055927 XP_001105315 XP_002810932 XP_004025774 XP_004285802
SP	Q6P0Q8
AlphaFold	Q6P0Q8