Click here to enlarge.
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/BMR15020
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Peterson, F.; Deng, Q.; Zettl, M.; Prehoda, K.; Lim, W.; Way, M.; Volkman, B.. "Multiple WASP-interacting protein recognition motifs are required for a functional interaction with N-WASP" J. Biol. Chem. 282, 8446-8453 (2007).
PubMed: 17229736
Assembly members:
WIP-EVH1_polypeptide, polymer, 169 residues, Formula weight is not available
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 Vector: pBH4
Entity Sequences (FASTA):
WIP-EVH1_polypeptide: GSESRFYFHPISDLPPPEPY
VQTTKSYPSKLARNESRGGL
VPRGSGGSLFSFLGKKCVTM
SSAVVQLYAADRNCMWSKKC
SGVACLVKDNPQRSYFLRIF
DIKDGKLLWEQELYNNFVYN
SPRGYFHTFAGDTCQVALNF
ANEEEAKKFRKAVTDLLGRR
QRKSEKRRD
Data type | Count |
13C chemical shifts | 578 |
15N chemical shifts | 139 |
1H chemical shifts | 918 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | WIP-EVH1 polypeptide | 1 |
Entity 1, WIP-EVH1 polypeptide 169 residues - Formula weight is not available
1 | GLY | SER | GLU | SER | ARG | PHE | TYR | PHE | HIS | PRO | ||||
2 | ILE | SER | ASP | LEU | PRO | PRO | PRO | GLU | PRO | TYR | ||||
3 | VAL | GLN | THR | THR | LYS | SER | TYR | PRO | SER | LYS | ||||
4 | LEU | ALA | ARG | ASN | GLU | SER | ARG | GLY | GLY | LEU | ||||
5 | VAL | PRO | ARG | GLY | SER | GLY | GLY | SER | LEU | PHE | ||||
6 | SER | PHE | LEU | GLY | LYS | LYS | CYS | VAL | THR | MET | ||||
7 | SER | SER | ALA | VAL | VAL | GLN | LEU | TYR | ALA | ALA | ||||
8 | ASP | ARG | ASN | CYS | MET | TRP | SER | LYS | LYS | CYS | ||||
9 | SER | GLY | VAL | ALA | CYS | LEU | VAL | LYS | ASP | ASN | ||||
10 | PRO | GLN | ARG | SER | TYR | PHE | LEU | ARG | ILE | PHE | ||||
11 | ASP | ILE | LYS | ASP | GLY | LYS | LEU | LEU | TRP | GLU | ||||
12 | GLN | GLU | LEU | TYR | ASN | ASN | PHE | VAL | TYR | ASN | ||||
13 | SER | PRO | ARG | GLY | TYR | PHE | HIS | THR | PHE | ALA | ||||
14 | GLY | ASP | THR | CYS | GLN | VAL | ALA | LEU | ASN | PHE | ||||
15 | ALA | ASN | GLU | GLU | GLU | ALA | LYS | LYS | PHE | ARG | ||||
16 | LYS | ALA | VAL | THR | ASP | LEU | LEU | GLY | ARG | ARG | ||||
17 | GLN | ARG | LYS | SER | GLU | LYS | ARG | ARG | ASP |
sample_1: WIP-EVH1 polypeptide, [U-99% 13C; U-99% 15N], 1.0 mM; sodium phosphate, none, 20 mM; Dithiothreitol, none, 1 mM; H2O, none, 90 mM; D2O, none, 10 mM
sample_conditions_1: ionic strength: 0.044 M; pH: 7.0; pressure: 1 atm; temperature: 303 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 15N-separated NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 13C-separated NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 13C-separated NOESY (AROMATIC) | sample_1 | isotropic | sample_conditions_1 |
X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement
xwinnmr v3.5, Bruker - collection
NMRPipe v2004, Delagio,F. et al. - processing
XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis
SPSCAN v1.1.0, R.W. Glaser - data analysis
GARANT v2.1, C. Bartels - data analysis
CYANA v2.1, Guntert, P. - structural calculation
PDB | |
DBJ | BAA11082 BAA20128 BAA21534 BAB29159 BAE24270 |
EMBL | CAC69994 CAH89371 CAH91010 CAL26602 |
GB | AAH19951 AAH52955 AAH55045 AAH58642 AAI51608 |
REF | NP_001103835 NP_001128797 NP_001161217 NP_001253726 NP_003932 |
SP | O00401 O08816 Q91YD9 Q95107 |
TPG | DAA30422 |
AlphaFold | O00401 O08816 Q91YD9 Q95107 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks