BMRB Entry 4558
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4558
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Title: 1H, 13C, and 15N Assignments for YopH-NT PubMed: 11693571
Deposition date: 1999-12-12 Original release date: 2001-06-26
Authors: Khandelwal, P.; Keliikuli, Kai; Smit, C.; Saper, M.; Zuiderweg, Erik
Citation: Khandelwal, P.; Keliikuli, Kai; Smit, C.; Saper, M.; Zuiderweg, Erik. "Letter to the editor: 1H, 15N and 13C Assignments of the N-terminal Domain of Yersinia outer Protein H in its apo form and in Complex with a Phosphotyrosine Peptide" J. Biomol. NMR 21, 69-70 (2001).
Assembly members:
YopH N-terminal domain, polymer, 136 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: 633 Superkingdom: Eukaryota Kingdom: not available Genus/species: Yersinia pseudotuberculosis
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
YopH N-terminal domain: MNLSLSDLHRQVSRLVQQES
GDCTGKLRGNVAANKETTFQ
GLTIASGARESEKVFAQTVL
SHVANVVLTQEDTAKLLQST
VKHNLNNYDLRSVGNGNSVL
VSLRSDQMTLQDAKVLLEAA
LRQESGARGSHHHHHH
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 526 |
13C chemical shifts | 432 |
15N chemical shifts | 123 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | YopH-NT | 1 |
Entities:
Entity 1, YopH-NT 136 residues - Formula weight is not available
1 | MET | ASN | LEU | SER | LEU | SER | ASP | LEU | HIS | ARG | ||||
2 | GLN | VAL | SER | ARG | LEU | VAL | GLN | GLN | GLU | SER | ||||
3 | GLY | ASP | CYS | THR | GLY | LYS | LEU | ARG | GLY | ASN | ||||
4 | VAL | ALA | ALA | ASN | LYS | GLU | THR | THR | PHE | GLN | ||||
5 | GLY | LEU | THR | ILE | ALA | SER | GLY | ALA | ARG | GLU | ||||
6 | SER | GLU | LYS | VAL | PHE | ALA | GLN | THR | VAL | LEU | ||||
7 | SER | HIS | VAL | ALA | ASN | VAL | VAL | LEU | THR | GLN | ||||
8 | GLU | ASP | THR | ALA | LYS | LEU | LEU | GLN | SER | THR | ||||
9 | VAL | LYS | HIS | ASN | LEU | ASN | ASN | TYR | ASP | LEU | ||||
10 | ARG | SER | VAL | GLY | ASN | GLY | ASN | SER | VAL | LEU | ||||
11 | VAL | SER | LEU | ARG | SER | ASP | GLN | MET | THR | LEU | ||||
12 | GLN | ASP | ALA | LYS | VAL | LEU | LEU | GLU | ALA | ALA | ||||
13 | LEU | ARG | GLN | GLU | SER | GLY | ALA | ARG | GLY | SER | ||||
14 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: YopH N-terminal domain, [U-90% 2H; U-13C; U-15N], 0.8 mM
sample_2: YopH N-terminal domain, [U-13C; U-15N], mM
sample_conditions_set_1: pH: 6.5; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
HNCA | not available | not available | sample_conditions_set_1 |
HNCOCA | not available | not available | sample_conditions_set_1 |
HNCO | not available | not available | sample_conditions_set_1 |
HN(CA)CO | not available | not available | sample_conditions_set_1 |
HNCACB | not available | not available | sample_conditions_set_1 |
CBCACONH | not available | not available | sample_conditions_set_1 |
HCCH-TOCSY | not available | not available | sample_conditions_set_1 |
Software:
No software information available
NMR spectrometers:
- Varian . 800 MHz
- Bruker . 600 MHz
- Bruker . 500 MHz
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
or all simulated shifts