BMRB Entry 16883
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16883
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Title: the N-terminal domain of human H-REV107 PubMed: 20526701
Deposition date: 2010-04-20 Original release date: 2010-06-15
Authors: Ren, Xiaobai; Xia, Bin
Citation: Ren, Xiaobai; Lin, Jian; Jin, Changwen; Xia, Bin. "1H, 13C and 15N resonance assignments of human H-REV107 N-terminal domain." Biomol. NMR Assignments 4, 175-178 (2010).
Assembly members:
H-REV107N, polymer, 125 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
H-REV107N: MRAPIPEPKPGDLIEIFRPF
YRHWAIYVGDGYVVHLAPPS
EVAGAGAASVMSALTDKAIV
KKELLYDVAGSDKYQVNNKH
DDKYSPLPCSKIIQRAEELV
GQEVLYKLTSENCEHFVNEL
RYGVA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 518 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 800 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | H-REV107N | 1 |
Entities:
Entity 1, H-REV107N 125 residues - Formula weight is not available
| 1 | MET | ARG | ALA | PRO | ILE | PRO | GLU | PRO | LYS | PRO | ||||
| 2 | GLY | ASP | LEU | ILE | GLU | ILE | PHE | ARG | PRO | PHE | ||||
| 3 | TYR | ARG | HIS | TRP | ALA | ILE | TYR | VAL | GLY | ASP | ||||
| 4 | GLY | TYR | VAL | VAL | HIS | LEU | ALA | PRO | PRO | SER | ||||
| 5 | GLU | VAL | ALA | GLY | ALA | GLY | ALA | ALA | SER | VAL | ||||
| 6 | MET | SER | ALA | LEU | THR | ASP | LYS | ALA | ILE | VAL | ||||
| 7 | LYS | LYS | GLU | LEU | LEU | TYR | ASP | VAL | ALA | GLY | ||||
| 8 | SER | ASP | LYS | TYR | GLN | VAL | ASN | ASN | LYS | HIS | ||||
| 9 | ASP | ASP | LYS | TYR | SER | PRO | LEU | PRO | CYS | SER | ||||
| 10 | LYS | ILE | ILE | GLN | ARG | ALA | GLU | GLU | LEU | VAL | ||||
| 11 | GLY | GLN | GLU | VAL | LEU | TYR | LYS | LEU | THR | SER | ||||
| 12 | GLU | ASN | CYS | GLU | HIS | PHE | VAL | ASN | GLU | LEU | ||||
| 13 | ARG | TYR | GLY | VAL | ALA |
Samples:
sample_1: H-REV107N, [U-13C; U-15N], 1 mM; sodium phosphate 30 mM; sodium chloride 30 mM; DTT 10 mM; H2O 90%; D2O 10%; sodium azide 0.05 w/v; DSS 0.02 w/v
sample_conditions_1: ionic strength: 60 mM; 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 HNCACB | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe v2.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5, Johnson, One Moon Scientific - data analysis
xwinnmr v3.5, Bruker Biospin - collection
TOPSPIN v2.1, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB08108 BAG35901 BAH08749 BAI46481 |
| EMBL | CAA63423 CAH92805 |
| GB | AAH01387 AAI03808 AAI03809 AAL26892 ABM83494 |
| REF | NP_001121675 NP_001128980 NP_001244356 NP_009000 XP_002833696 |
| SP | P53816 Q5R611 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts