BMRB Entry 16262
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16262
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Title: NMR solution structure of the N-terminal domain of the DNA polymerase alpha p68 subunit
Deposition date: 2009-04-22 Original release date: 2012-08-06
Authors: Huang, Hao; Weiner, Brian; Zhang, Haijiang; Fuller, Brian; Gao, Yue; Wile, Brian; Chazin, Walter; Fanning, Ellen
Citation: Huang, Hao; Weiner, Brian; Zhang, Haijiang; Fuller, Brian; Gao, Yue; Wile, Brian; Chazin, Walter; Fanning, Ellen. "The N-terminal domain of the p68 subunit tethers DNA polymerase alpha-primase to a replicative helicase for primosome function" Not known ., .-..
Assembly members:
p68N, polymer, 101 residues, 8700.943 Da.
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):
p68N: MGSSHHHHHHGSSLEVLFQG
PGSMSASAQQLAEELQIFGL
DCEEALIEKLVELCVQYGQN
EEGMVGELIAFCTSTHKVGL
TSEILNSFEHEFLSKRLSKA
R
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 235 |
15N chemical shifts | 83 |
1H chemical shifts | 550 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | p68N | 1 |
Entities:
Entity 1, p68N 101 residues - 8700.943 Da.
1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
2 | GLY | SER | SER | LEU | GLU | VAL | LEU | PHE | GLN | GLY | ||||
3 | PRO | GLY | SER | MET | SER | ALA | SER | ALA | GLN | GLN | ||||
4 | LEU | ALA | GLU | GLU | LEU | GLN | ILE | PHE | GLY | LEU | ||||
5 | ASP | CYS | GLU | GLU | ALA | LEU | ILE | GLU | LYS | LEU | ||||
6 | VAL | GLU | LEU | CYS | VAL | GLN | TYR | GLY | GLN | ASN | ||||
7 | GLU | GLU | GLY | MET | VAL | GLY | GLU | LEU | ILE | ALA | ||||
8 | PHE | CYS | THR | SER | THR | HIS | LYS | VAL | GLY | LEU | ||||
9 | THR | SER | GLU | ILE | LEU | ASN | SER | PHE | GLU | HIS | ||||
10 | GLU | PHE | LEU | SER | LYS | ARG | LEU | SER | LYS | ALA | ||||
11 | ARG |
Samples:
sample_1: p68N, [U-100% 13C; U-100% 15N], 0.75 mM; NACL 50 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1.0 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N 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 H(CC)(CO)NH TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D (H)CC(CO)NH TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution
AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
PDB | |
DBJ | BAG73551 |
EMBL | CAG33018 |
GB | AAA16459 AAH01347 AAH02990 ABM82949 ABM86141 |
REF | NP_001253937 NP_002680 XP_001169495 XP_003828668 XP_003909632 |
SP | Q14181 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts