BMRB Entry 15407

Name: Third SH3 domain of CD2AP
Published: 2007-10-16

Click here to enlarge.

PDB ID: 2jte
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15407
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:

Third SH3 domain of CD2AP

Deposition date:

2007-07-28

Original release date:

2007-10-16

Authors:

van Nuland, Nico; Ortega Roldan, Jose-Luis; Romero Romero, Maria-Luisa; AB, Eiso; Ora, Ari; Lopez Mayorga, Obdulio; Azuaga, Ana

Citation:

Citation: Ortega Roldan, Jose-Luis; Romero Romero, Maria-Luisa; Ora, Ari; AB, Eiso; Lopez Mayorga, Obdulio; Azuaga, Ana; van Nuland, Nico. "The high resolution NMR structure of the third SH3 domain of CD2AP" J. Biomol. NMR 39, 331-336 (2007).
PubMed: 17922258

Assembly members:

Assembly members:
SH3-C, polymer, 64 residues, 7148.993 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM-11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH3-C: GAMGAKEYCRTLFPYTGTNE DELTFREGEIIHLISKETGE AGWWKGELNGKEGVFPDNFA VQIS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	275
15N chemical shifts	68
1H chemical shifts	433

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SH3-C	1

Entities:

Entity 1, SH3-C 64 residues - 7148.993 Da.

1

GLY

ALA

MET

GLY

ALA

LYS

GLU

TYR

CYS

ARG

2

THR

LEU

PHE

PRO

TYR

THR

GLY

THR

ASN

GLU

3

ASP

GLU

LEU

THR

PHE

ARG

GLU

GLY

GLU

ILE

4

ILE

HIS

LEU

ILE

SER

LYS

GLU

THR

GLY

GLU

5

ALA

GLY

TRP

LYS

GLY

GLU

LEU

ASN

GLY

6

LYS

GLU

GLY

VAL

PHE

PRO

ASP

ASN

PHE

ALA

7

VAL

GLN

ILE

SER

Samples:

sample_1: SH3-C, [U-98% 13C; U-98% 15N], 1 mM

sample_2: SH3-C, [U-98% 15N], 1 mM

sample_3: SH3-C 1 mM

sample_4: SH3-C 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 2.0; 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	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-15N TOCSY	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

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Varian Uniform NMR System 600 MHz
Varian INOVA 800 MHz