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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
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NMR-STAR v3 text file.
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Citation: Barnwal, Ravi Pratap; Varani, Gabriele. "1H and 15N Assigned Chemical Shifts for high mobility group protein-like protein NHP1 from Babesia bovis" .
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 Vector: pET28-ava
Entity Sequences (FASTA):
high_mobility_group_protein-like_protein_NHP1: MAGASDRTGVRRPRKAKKDP
NAPKRALSSYMFFAKEKRVE
IIAENPEIAKDVAAIGKMIG
AAWNALSDEEKKPYERMSDE
DRVRYEREKAEYAQRKV
Data type | Count |
13C chemical shifts | 386 |
15N chemical shifts | 89 |
1H chemical shifts | 544 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | NHP1 | 1 |
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 |
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
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 |
TOPSPIN v2.1, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
PDB | |
DBJ | BAN64348 BAN64485 |
GB | AAA27799 EDO05788 |
REF | XP_001609356 |
SP | P40632 |
AlphaFold | P40632 |
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