BMRB Entry 15575

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15575
MolProbity Validation Chart

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Title:
Solution Structure of the Tandem WW Domains of FBP21
Deposition date:
2007-11-30
Original release date:
2007-11-30
Authors:
Huang, Xiaojuan; Zhang, Jiahai; Wu, Jihui; Shi, Yunyu
Citation:

Citation: Huang, Xiaojuan; Beullens, Monique; Zhang, Jiahai; Zhou, Yi; Nicolaescu, Emilia; Lesage, Bart; Hu, Qi; Wu, Jihui; Bollen, Mathieu; Shi, Yunyu. "Structure and Function of the Two Tandem WW Domains of the Pre-mRNA Splicing Factor FBP21 (Formin-binding Protein 21)"  J. Biol. Chem. 284, 25375-25387 (2009).
PubMed: 19592703

Assembly members:

Assembly members:
FBP21, polymer, 83 residues, 8691.426 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: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FBP21: DPSKGRWVEGITSEGYHYYY DLISGASQWEKPEGFQGDLK KTAVKTVWVEGLSEDGFTYY YNTETGESRWEKPDDLEHHH HHH

Data sets:
Data typeCount
13C chemical shifts259
15N chemical shifts77
1H chemical shifts467

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1FBP211

Entities:

Entity 1, FBP21 83 residues - 8691.426 Da.

1   ASPPROSERLYSGLYARGTRPVALGLUGLY
2   ILETHRSERGLUGLYTYRHISTYRTYRTYR
3   ASPLEUILESERGLYALASERGLNTRPGLU
4   LYSPROGLUGLYPHEGLNGLYASPLEULYS
5   LYSTHRALAVALLYSTHRVALTRPVALGLU
6   GLYLEUSERGLUASPGLYPHETHRTYRTYR
7   TYRASNTHRGLUTHRGLYGLUSERARGTRP
8   GLULYSPROASPASPLEUGLUHISHISHIS
9   HISHISHIS

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1.0 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_2: entity, [U-99% 15N], 0.5 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 293 K

sample_conditions_2: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_2
2D 1H-1H NOESYsample_1isotropicsample_conditions_2
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CNSSOLVE v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

xwinnmr, Bruker Biospin - collection

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

Molmol, Koradi, Billeter and Wuthrich - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

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

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Bruker DMX 600 MHz

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