BMRB Entry 6536

Name: 1H,15N,13C backbone and sidechain assignment for human ADAP hSH3-1 domain in reduced form
Published: 2015-05-08

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PDB ID: 2gtj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6536
MolProbity Validation Chart

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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,15N,13C backbone and sidechain assignment for human ADAP hSH3-1 domain in reduced form

Deposition date:

2005-03-07

Original release date:

2015-05-08

Authors:

Zimmermann, Juergen; Freund, Christian

Citation:

Citation: Zimmermann, Juergen; Freund, Christian. "NMR assignment of the reduced and oxidized forms of the human ADAP hSH3-1 domain" J. Biomol. NMR 32, 94-94 (2005).

Assembly members:

Assembly members:
hSH3-1 domain, polymer, 96 residues, 11861.6 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hSH3-1 domain: EKKEQKEKEKKEQEIKKKFK LTGPIQVIHLAKACCDVKGG KNELSFKQGEQIEIIRITDN PEGKWLGRTARGSYGYIKTT AVEIDYDSLKLKKDLE

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
13C chemical shifts	239
15N chemical shifts	85
1H chemical shifts	479

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hSH3-1 domain	1

Entities:

Entity 1, hSH3-1 domain 96 residues - 11861.6 Da.

1

GLU

LYS

GLU

GLN

LYS

GLU

LYS

GLU

LYS

2

LYS

GLU

GLN

GLU

ILE

LYS

PHE

LYS

3

LEU

THR

GLY

PRO

ILE

GLN

VAL

ILE

HIS

LEU

4

ALA

LYS

ALA

CYS

ASP

VAL

LYS

GLY

5

LYS

ASN

GLU

LEU

SER

PHE

LYS

GLN

GLY

GLU

6

GLN

ILE

GLU

ILE

ARG

ILE

THR

ASP

ASN

7

PRO

GLU

GLY

LYS

TRP

LEU

GLY

ARG

THR

ALA

8

ARG

GLY

SER

TYR

GLY

TYR

ILE

LYS

THR

9

ALA

VAL

GLU

ILE

ASP

TYR

ASP

SER

LEU

LYS

10

LEU

LYS

ASP

LEU

GLU

Samples:

sample_1: SH3 domain, [U-13C; U-15N], 1.0 ± 0.05 mM; NaCl 20 mM; Potassiumdihydrogenphosphate 50 mM; Dithtiothreitol 10 mM

conditions_1: pH: 7.0; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N_NOESY	sample_1	isotropic	conditions_1
13C_NOESY	sample_1	isotropic	conditions_1
HNCO	sample_1	isotropic	conditions_1
2D_NOESY	sample_1	isotropic	conditions_1
15N_HSQC	sample_1	isotropic	conditions_1

Software:

AZARA v2.0 - data processing

ANSIG v3.3 - assignment

NMR spectrometers:

Bruker Avance 600 MHz

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