BMRB Entry 19483

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19483
MolProbity Validation Chart

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Title:
Solution structure of the WW domain of HYPB
Deposition date:
2013-09-10
Original release date:
2014-02-12
Authors:
Gao, Yong-Guang
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:
WW_HYPB, polymer, 48 residues, 5535.180 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):
WW_HYPB: GSKPKTIVLPPNWKTARDPE GKIYYYHVITRQTQWDPPTW ESPGDDAS

Data sets:
Data typeCount
13C chemical shifts147
15N chemical shifts44
1H chemical shifts218

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WW domain of HYPB1

Entities:

Entity 1, WW domain of HYPB 48 residues - 5535.180 Da.

1   GLYSERLYSPROLYSTHRILEVALLEUPRO
2   PROASNTRPLYSTHRALAARGASPPROGLU
3   GLYLYSILETYRTYRTYRHISVALILETHR
4   ARGGLNTHRGLNTRPASPPROPROTHRTRP
5   GLUSERPROGLYASPASPALASER

Samples:

sample_1: WW domain of HYPB, [U-99% 13C; U-99% 15N], 500 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.08 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - data analysis

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

Molmol, Koradi, Billeter and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19487 19488
PDB
DBJ BAB21823 BAD32524 BAG10485
EMBL CAC28349 CAD28492
GB AAC26194 AAC26846 AAH31601 AAH59049 AAH90954
REF NP_001074809 NP_001101659 NP_054878 XP_001113652 XP_001495700
SP E9Q5F9 Q9BYW2
TPG DAA16805
AlphaFold E9Q5F9 Q9BYW2

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