BMRB Entry 19505

Name: WW Domain Strand-Swapped Dimer
Published: 2014-09-29

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PDB ID: 2mdw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19505
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:

WW Domain Strand-Swapped Dimer

Deposition date:

2013-09-18

Original release date:

2014-09-29

Authors:

Kier, Brandon; Sheffler, William; Baker, David

Citation:

Citation: Kier, Brandon; Sheffler, William; Baker, David. "Covalent Assembly of Homooligomeric Proteins Using Structure-templating Hubs" Biochemistry ., .-..

Assembly members:

Assembly members:
entity, polymer, 27 residues, 3363.901 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: KLPPGWEKRCFYFNRITGKR QFERPSD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	192

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	WW Domain Strand-Swapped Dimer 1	1
2	WW Domain Strand-Swapped Dimer 2	1

Entities:

Entity 1, WW Domain Strand-Swapped Dimer 1 27 residues - 3363.901 Da.

1

LYS

LEU

PRO

GLY

TRP

GLU

LYS

ARG

CYS

2

PHE

TYR

PHE

ASN

ARG

ILE

THR

GLY

LYS

ARG

3

GLN

PHE

GLU

ARG

PRO

SER

ASP

Samples:

sample_1: WW Domain Strand-Swapped Dimer mM; sodium phosphate 50 mM; DSS 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.11 M; pH: 6.5; pressure: 1 atm; temperature: 280 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1

Software:

Foldit, David Baker et al, University of Washington - design

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 700 MHz