Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15738
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Citation: Yang, Chun-Jun; Chen, Heng-Li; Cheng, Hsi-Tsung; Chiu, Chui-Lin; Cheng, Jya-Wei. "Structural Characterization and DNA Binding Sequence Selection of the CsrA Protein from Helicobacter pylori" .
Assembly members:
HP1442, polymer, 85 residues, Formula weight is not available
Natural source: Common Name: Helicobacter pylori Taxonomy ID: 210 Superkingdom: Bacteria Kingdom: not available Genus/species: Helicobacter pylori
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETBlue-2
Entity Sequences (FASTA):
HP1442: MALILSRKVNEGIVIDDNIH
IKVISIDRGSVRLGFEAPES
TLILRAELKEAIVSENQKAS
VCVDESLLENIKKVIKPLEH
HHHHH
Data type | Count |
13C chemical shifts | 227 |
15N chemical shifts | 75 |
1H chemical shifts | 147 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HP1442, chain A | 1 |
2 | HP1442, chain B | 1 |
Entity 1, HP1442, chain A 85 residues - Formula weight is not available
Residues 78-85 represent a non-native affinity tag and residue 2 is an artefact from cloning.
1 | MET | ALA | LEU | ILE | LEU | SER | ARG | LYS | VAL | ASN | ||||
2 | GLU | GLY | ILE | VAL | ILE | ASP | ASP | ASN | ILE | HIS | ||||
3 | ILE | LYS | VAL | ILE | SER | ILE | ASP | ARG | GLY | SER | ||||
4 | VAL | ARG | LEU | GLY | PHE | GLU | ALA | PRO | GLU | SER | ||||
5 | THR | LEU | ILE | LEU | ARG | ALA | GLU | LEU | LYS | GLU | ||||
6 | ALA | ILE | VAL | SER | GLU | ASN | GLN | LYS | ALA | SER | ||||
7 | VAL | CYS | VAL | ASP | GLU | SER | LEU | LEU | GLU | ASN | ||||
8 | ILE | LYS | LYS | VAL | ILE | LYS | PRO | LEU | GLU | HIS | ||||
9 | HIS | HIS | HIS | HIS | HIS |
sample_1: HP1442, [U-13C; U-15N], 1 mM; potassium phosphate 30 mM; sodium chloride 50 mM; EDTA 0.1 mM; DTT 5 mM; sodium azide 10 mM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
SPARKY, Goddard - chemical shift assignment, data analysis
xwinnmr, Bruker Biospin - collection, processing
GB | NP_208233 AAD08480 ABF85435 ACD48869 ACJ08568 ACX98483 |
UNP | O25983 |
DBJ | BAJ57406 BAJ58911 BAJ60431 BAM97263 BAM98719 |
EMBL | CAX30116 CBI65651 |
REF | NP_208233 WP_000906438 WP_000906439 WP_000906441 WP_000906442 |
SP | B2UVI7 B6JNU0 O25983 |
AlphaFold | O25983 B2UVI7 B6JNU0 O25983 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks