BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19487

Title: Solution structure of the PP2WW mutant (KPP2WW) of HYPB   PubMed: 24412394

Deposition date: 2013-09-10 Original release date: 2014-02-12

Authors: Gao, Yong-Guang; Hu, Hong-Yu

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).

Assembly members:
KPP2WW, polymer, 56 residues, 6193.844 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
KPP2WW: GSDLPPPSPPAAATIVLPPN WKTARDPEGKIYYYHVITRQ TQWDPPTWESPGDDAS

Data sets:
Data typeCount
13C chemical shifts174
15N chemical shifts49
1H chemical shifts261

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PP2WW mutant (KPP2WW) of HYPB1

Entities:

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

1   GLYSERASPLEUPROPROPROSERPROPRO
2   ALAALAALATHRILEVALLEUPROPROASN
3   TRPLYSTHRALAARGASPPROGLUGLYLYS
4   ILETYRTYRTYRHISVALILETHRARGGLN
5   THRGLNTRPASPPROPROTHRTRPGLUSER
6   PROGLYASPASPALASER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_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, . - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19483
PDB
GB AAC26194 AAC26846
REF XP_007534044

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts