BMRB Entry 25961

Name: Solution structure of Q388A3 PDZ domain
Published: 2016-02-22

Click here to enlarge.

PDB ID: 2nb4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25961
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:

Solution structure of Q388A3 PDZ domain

Deposition date:

2016-01-24

Original release date:

2016-02-22

Authors:

Mei, Song

Citation:

Citation: Mei, Song; Dong, Yuanqiu; Zhang, Jiahai; Zhang, Xuecheng; Tu, Xiaoming. "Solution structure of Q388A3 PDZ domain from Trypanosoma brucei" J. Struct. Biol. 194, 214-217 (2016).
PubMed: 26917351

Assembly members:

Assembly members:
entity, polymer, 105 residues, 10985.538 Da.

Natural source:

Natural source: Common Name: kinetoplastids Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: p28b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: PLTRPYLGFRVAVGRDSSGC TTLSIQEVTQTYTGSNGGAD LMGPAFAAGLRVGDQLVRFA GYTVTELAAFNTVVARHVRP SASIPVVFSRDGVVMSATIV VGELE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	276
15N chemical shifts	102
1H chemical shifts	574

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 105 residues - 10985.538 Da.

1

PRO

LEU

THR

ARG

PRO

TYR

LEU

GLY

PHE

ARG

2

VAL

ALA

VAL

GLY

ARG

ASP

SER

GLY

CYS

3

THR

LEU

SER

ILE

GLN

GLU

VAL

THR

GLN

4

THR

TYR

THR

GLY

SER

ASN

GLY

ALA

ASP

5

LEU

MET

GLY

PRO

ALA

PHE

ALA

GLY

LEU

6

ARG

VAL

GLY

ASP

GLN

LEU

VAL

ARG

PHE

ALA

7

GLY

TYR

THR

VAL

THR

GLU

LEU

ALA

PHE

8

ASN

THR

VAL

ALA

ARG

HIS

VAL

ARG

PRO

9

SER

ALA

SER

ILE

PRO

VAL

PHE

SER

ARG

10

ASP

GLY

VAL

MET

SER

ALA

THR

ILE

VAL

11

VAL

GLY

GLU

LEU

GLU

Samples:

sample_1: sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DMX 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks