BMRB Entry 4373
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4373
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Title: 1H, 15N, and 13C Resonance Assignment of the PH Domain from C. elegans UNC-89
Deposition date: 1999-07-29 Original release date: 2000-12-14
Authors: Blomberg, Niklas; Sattler, Michael; Nilges, Michael
Citation: Blomberg, Niklas; Sattler, Michael; Nilges, Michael. "1H, 15N, and 13C Resonance Assignment of the PH Domain from C. elegans UNC-89" J. Biomol. NMR 15, 269-270 (1999).
Assembly members:
PH domain from C. elegans UNC-89 protein, polymer, 112 residues, Formula weight is not available
Natural source: Common Name: C. elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
PH domain from C. elegans UNC-89 protein: GRIIRHDAFQVWEGDEPPKL
RYVFLFRNKIMFTEQDASTS
PPSYTHYSSIRLDKYNIRQH
TTDEDTIVLQPQEPGLPSFR
IKPKDFETSEYVRKAWLRDI
AEEQEKYAAERD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 231 |
15N chemical shifts | 99 |
1H chemical shifts | 669 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | UNC-89 PH domain | 1 |
Entities:
Entity 1, UNC-89 PH domain 112 residues - Formula weight is not available
1 | GLY | ARG | ILE | ILE | ARG | HIS | ASP | ALA | PHE | GLN | ||||
2 | VAL | TRP | GLU | GLY | ASP | GLU | PRO | PRO | LYS | LEU | ||||
3 | ARG | TYR | VAL | PHE | LEU | PHE | ARG | ASN | LYS | ILE | ||||
4 | MET | PHE | THR | GLU | GLN | ASP | ALA | SER | THR | SER | ||||
5 | PRO | PRO | SER | TYR | THR | HIS | TYR | SER | SER | ILE | ||||
6 | ARG | LEU | ASP | LYS | TYR | ASN | ILE | ARG | GLN | HIS | ||||
7 | THR | THR | ASP | GLU | ASP | THR | ILE | VAL | LEU | GLN | ||||
8 | PRO | GLN | GLU | PRO | GLY | LEU | PRO | SER | PHE | ARG | ||||
9 | ILE | LYS | PRO | LYS | ASP | PHE | GLU | THR | SER | GLU | ||||
10 | TYR | VAL | ARG | LYS | ALA | TRP | LEU | ARG | ASP | ILE | ||||
11 | ALA | GLU | GLU | GLN | GLU | LYS | TYR | ALA | ALA | GLU | ||||
12 | ARG | ASP |
Samples:
sample_1: PH domain from C. elegans UNC-89 protein, [U-13C; U-15N], 0.6 0.8 mM; Pi 5 mM; NaCl 50 mM; d6-DMSO 16%
experimental_conditions_1: ionic strength: 0.13 M; pH: 6.8; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
1H-15N HSQC NOESY | sample_1 | not available | experimental_conditions_1 |
1H-15N HSQC TOCSY | sample_1 | not available | experimental_conditions_1 |
CBCA(CO)NH | sample_1 | not available | experimental_conditions_1 |
CBCANH | sample_1 | not available | experimental_conditions_1 |
HNCA | sample_1 | not available | experimental_conditions_1 |
HN(CO)CA | sample_1 | not available | experimental_conditions_1 |
HBHA(CO)NH | sample_1 | not available | experimental_conditions_1 |
HCCH-TOCSY | sample_1 | not available | experimental_conditions_1 |
1H-13C HMQC NOESY | sample_1 | not available | experimental_conditions_1 |
2D 1H-1H NOESY | sample_1 | not available | experimental_conditions_1 |
HNHA-J | sample_1 | not available | experimental_conditions_1 |
Software:
XWIN-NMR - Acquisition
Xeasy - Spectral analysis
NMRPipe - Processing
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 500 MHz
Related Database Links:
PDB | |
EMBL | CCD63864 CCD63865 CCD63868 CCD63869 CCD63870 |
GB | AAB00542 |
REF | NP_001020984 NP_001020985 NP_001020988 NP_001020989 NP_001020990 |
SP | O01761 |
Download simulated HSQC data in one of the following formats:
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or all simulated shifts