BMRB Entry 19487

Name: Solution structure of the PP2WW mutant (KPP2WW) of HYPB
Published: 2014-02-12

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PDB ID: 2mdi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19487
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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 PP2WW mutant (KPP2WW) of HYPB

Deposition date:

2013-09-10

Original release date:

2014-02-12

Authors:

Gao, Yong-Guang; Hu, Hong-Yu

Citation:

Citation: Gao, Yong-Guang; Yang, Hui; Zhao, Jian; Jiang, Ya-Jun; Hu, Hong-Yu. "Autoinhibitory Structure of the WW Domain of HYPB/SETD2 Regulates Its Interaction with the Proline-Rich Region of Huntingtin." Structure ., .-. (2014).
PubMed: 24412394

Assembly members:

Assembly members:
KPP2WW, polymer, 56 residues, 6193.844 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 Host organism: Escherichia coli Vector: pET-32M

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KPP2WW: GSDLPPPSPPAAATIVLPPN WKTARDPEGKIYYYHVITRQ TQWDPPTWESPGDDAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	174
15N chemical shifts	49
1H chemical shifts	261

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PP2WW mutant (KPP2WW) of HYPB	1

Entities:

Entity 1, PP2WW mutant (KPP2WW) of HYPB 56 residues - 6193.844 Da.

1

GLY

SER

ASP

LEU

PRO

SER

PRO

2

ALA

THR

ILE

VAL

LEU

PRO

ASN

3

TRP

LYS

THR

ALA

ARG

ASP

PRO

GLU

GLY

LYS

4

ILE

TYR

HIS

VAL

ILE

THR

ARG

GLN

5

THR

GLN

TRP

ASP

PRO

THR

TRP

GLU

SER

6

PRO

GLY

ASP

ALA

SER

Samples:

sample_1: KPP2WW, [U-99% 13C; U-99% 15N], 500 uM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.05 w/v; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.08 M; pH: 6.5; pressure: 1 atm; temperature: 273 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 HNHA	sample_1	isotropic	sample_conditions_1
3D C(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-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ARIA, Linge, O'Donoghue and Nilges - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	19483
PDB	2MDC 2MDI
GB	AAC26194 AAC26846
REF	XP_007534044