BMRB Entry 17204
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17204
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Title: the 1H, 13C and 15N resonance assignment of ubiquitin-like small archaeal modifier protein from Haloferax volcanii PubMed: 23823798
Deposition date: 2010-09-24 Original release date: 2014-03-04
Authors: Zhang, Wen; Fan, Kai; Zhang, Jiahai; Tu, Xiaoming
Citation: Liao, Shanhui; Zhang, Wen; Fan, Kai; Ye, Kaiqin; Zhang, Xuecheng; Zhang, Jiahai; Xu, Chao; Tu, Xiaoming. "Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP2) from Haloferax volcanii." Sci. Rep. 3, 2136-2136 (2013).
Assembly members:
ubiquitin-like_small_archaeal_modifier_protein, polymer, 74 residues, Formula weight is not available
Natural source: Common Name: Haloferax volcanii Taxonomy ID: 2246 Superkingdom: Archaea Kingdom: not available Genus/species: Haloferax volcanii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ubiquitin-like_small_archaeal_modifier_protein: MNVTVEVVGEETSEVAVDDD
GTYADLVRAVDLSPHEVTVL
VDGRPVPEDQSVEVDRVKVL
RLIKGGLEHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 179 |
15N chemical shifts | 61 |
1H chemical shifts | 367 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ubiquitin-like small archaeal modifier protein | 1 |
Entities:
Entity 1, ubiquitin-like small archaeal modifier protein 74 residues - Formula weight is not available
1 | MET | ASN | VAL | THR | VAL | GLU | VAL | VAL | GLY | GLU | ||||
2 | GLU | THR | SER | GLU | VAL | ALA | VAL | ASP | ASP | ASP | ||||
3 | GLY | THR | TYR | ALA | ASP | LEU | VAL | ARG | ALA | VAL | ||||
4 | ASP | LEU | SER | PRO | HIS | GLU | VAL | THR | VAL | LEU | ||||
5 | VAL | ASP | GLY | ARG | PRO | VAL | PRO | GLU | ASP | GLN | ||||
6 | SER | VAL | GLU | VAL | ASP | ARG | VAL | LYS | VAL | LEU | ||||
7 | ARG | LEU | ILE | LYS | GLY | GLY | LEU | GLU | HIS | HIS | ||||
8 | HIS | HIS | HIS | HIS |
Samples:
sample_1: submit 2, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 25 mM; sodium chloride 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.125 M; pH: 6.7; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment, collection
NMR spectrometers:
- Bruker DMX 500 MHz
Related Database Links:
BMRB | 17939 |
PDB | |
GB | ADE03392 AKU06380 ELK50451 ELY23894 ELZ70132 |
REF | WP_004045316 WP_004065555 WP_008609462 |
SP | D4GZE7 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts