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
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Title: Solution Structure of the Tandem WW Domains of FBP21 PubMed: 19592703
Deposition date: 2007-11-30 Original release date: 2007-11-30
Authors: Huang, Xiaojuan; Zhang, Jiahai; Wu, Jihui; Shi, Yunyu
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).
Assembly members:
FBP21, polymer, 83 residues, 8691.426 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):
FBP21: DPSKGRWVEGITSEGYHYYY
DLISGASQWEKPEGFQGDLK
KTAVKTVWVEGLSEDGFTYY
YNTETGESRWEKPDDLEHHH
HHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 259 |
15N chemical shifts | 77 |
1H chemical shifts | 467 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | FBP21 | 1 |
Entities:
Entity 1, FBP21 83 residues - 8691.426 Da.
1 | ASP | PRO | SER | LYS | GLY | ARG | TRP | VAL | GLU | GLY | ||||
2 | ILE | THR | SER | GLU | GLY | TYR | HIS | TYR | TYR | TYR | ||||
3 | ASP | LEU | ILE | SER | GLY | ALA | SER | GLN | TRP | GLU | ||||
4 | LYS | PRO | GLU | GLY | PHE | GLN | GLY | ASP | LEU | LYS | ||||
5 | LYS | THR | ALA | VAL | LYS | THR | VAL | TRP | VAL | GLU | ||||
6 | GLY | LEU | SER | GLU | ASP | GLY | PHE | THR | TYR | TYR | ||||
7 | TYR | ASN | THR | GLU | THR | GLY | GLU | SER | ARG | TRP | ||||
8 | GLU | LYS | PRO | ASP | ASP | LEU | GLU | HIS | HIS | HIS | ||||
9 | HIS | HIS | HIS |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_2 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_2 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts