BMRB Entry 17855
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17855
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for high mobility group protein-like protein NHP1 from Babesia bovis T2Bo. Seattle Structure Genomics Center for Infectious Disease (SSGCID)
Deposition date: 2011-08-11 Original release date: 2011-08-31
Authors: Barnwal, Ravi; Varani, Gabriele
Citation: Barnwal, Ravi Pratap; Varani, Gabriele. "1H and 15N Assigned Chemical Shifts for high mobility group protein-like protein NHP1 from Babesia bovis" Not known ., .-..
Assembly members:
high_mobility_group_protein-like_protein_NHP1, polymer, 97 residues, 11140.849 Da.
Natural source: Common Name: Babesia bovis Taxonomy ID: 5865 Superkingdom: Eukaryota Kingdom: not available Genus/species: Babesia bovis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
high_mobility_group_protein-like_protein_NHP1: MAGASDRTGVRRPRKAKKDP
NAPKRALSSYMFFAKEKRVE
IIAENPEIAKDVAAIGKMIG
AAWNALSDEEKKPYERMSDE
DRVRYEREKAEYAQRKV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 386 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 544 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NHP1 | 1 |
Entities:
Entity 1, NHP1 97 residues - 11140.849 Da.
| 1 | MET | ALA | GLY | ALA | SER | ASP | ARG | THR | GLY | VAL | ||||
| 2 | ARG | ARG | PRO | ARG | LYS | ALA | LYS | LYS | ASP | PRO | ||||
| 3 | ASN | ALA | PRO | LYS | ARG | ALA | LEU | SER | SER | TYR | ||||
| 4 | MET | PHE | PHE | ALA | LYS | GLU | LYS | ARG | VAL | GLU | ||||
| 5 | ILE | ILE | ALA | GLU | ASN | PRO | GLU | ILE | ALA | LYS | ||||
| 6 | ASP | VAL | ALA | ALA | ILE | GLY | LYS | MET | ILE | GLY | ||||
| 7 | ALA | ALA | TRP | ASN | ALA | LEU | SER | ASP | GLU | GLU | ||||
| 8 | LYS | LYS | PRO | TYR | GLU | ARG | MET | SER | ASP | GLU | ||||
| 9 | ASP | ARG | VAL | ARG | TYR | GLU | ARG | GLU | LYS | ALA | ||||
| 10 | GLU | TYR | ALA | GLN | ARG | LYS | VAL |
Samples:
sample_1: high mobility group protein-like protein NHP1, [U-98% 13C; U-98% 15N], 1.2 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker AMX 500 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts