BMRB Entry 11219

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PDB ID: 2dl3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11219
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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:

Solution structure of the first SH3 domain of human sorbin and Sh3 domain-containing protein 1

Deposition date:

2010-07-22

Original release date:

2011-07-21

Authors:

Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.

Citation:

Citation: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.. "Solution structure of the first SH3 domain of human sorbin and Sh3 domain-containing protein 1" .

Assembly members:

Assembly members:
SH3 domain, polymer, 68 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: cell free synthesis Host organism: E. coli - cell free Vector: P050613-04

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH3 domain: GSSGSSGRPARAKFDFKAQT LKELPLQKGDIVYIYKQIDQ NWYEGEHHGRVGIFPRTYIE LLSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	295
15N chemical shifts	63
1H chemical shifts	457

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sorbin and SH3 domain-containing protein 1	1

Entities:

Entity 1, Sorbin and SH3 domain-containing protein 1 68 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ARG

PRO

ALA

2

ARG

ALA

LYS

PHE

ASP

PHE

LYS

ALA

GLN

THR

3

LEU

LYS

GLU

LEU

PRO

LEU

GLN

LYS

GLY

ASP

4

ILE

VAL

TYR

ILE

TYR

LYS

GLN

ILE

ASP

GLN

5

ASN

TRP

TYR

GLU

GLY

GLU

HIS

GLY

ARG

6

VAL

GLY

ILE

PHE

PRO

ARG

THR

TYR

ILE

GLU

7

LEU

SER

GLY

PRO

SER

GLY

Samples:

sample_1: SH3 domain, [U-13C; U-15N], 1.00 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9296, Kobayashi N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 900 MHz

PDB	2DL3 4LNP
GB	KFP25985 KFV06230 KFZ48496