BMRB Entry 50121
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50121
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Title: 1H, 15N assignments of single-stranded DNA binding domains from the 70 kDa subunit of Human Replication Protein A bound to ssDNA PubMed: 12881520
Deposition date: 2019-12-10 Original release date: 2019-12-20
Authors: Arunkumar, Alphonse
Citation: Arunkumar, Alphonse; Stauffer, Melissa; Bochkareva, Elena; Bochkarev, Alexey; Chazin, Walter. "Independent and Coordinated Functions of Replication Protein A Tandem High Affinity Single-stranded DNA Binding Domains" J. Biol. Chem. 278, 41077-41082 (2003).
Assembly members:
entity_1, polymer, 242 residues, 27071 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 Vector: pSV281
Entity Sequences (FASTA):
entity_1: QSKVVPIASLTPYQSKWTIC
ARVTNKSQIRTWSNSRGEGK
LFSLELVDESGEIRATAFNE
QVDKFFPLIEVNKVYYFSKG
TLKIANKQFTAVKNDYEMTF
NNETSVMPCEDDHHLPTVQF
DFTGIDDLENKSKDSLVDII
GICKSYEDATKITVRSNNAE
VAKRNIYLMDTSGKVVTATL
WGEDADKFDGSRQPVLAIKG
ARVSDFGGRSLSVLSSSTII
ANPDIPEAYKLRGYFDAEGG
AL
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 191 |
| 1H chemical shifts | 191 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RPA70AB | 1 |
Entities:
Entity 1, RPA70AB 242 residues - 27071 Da.
| 1 | GLN | SER | LYS | VAL | VAL | PRO | ILE | ALA | SER | LEU | ||||
| 2 | THR | PRO | TYR | GLN | SER | LYS | TRP | THR | ILE | CYS | ||||
| 3 | ALA | ARG | VAL | THR | ASN | LYS | SER | GLN | ILE | ARG | ||||
| 4 | THR | TRP | SER | ASN | SER | ARG | GLY | GLU | GLY | LYS | ||||
| 5 | LEU | PHE | SER | LEU | GLU | LEU | VAL | ASP | GLU | SER | ||||
| 6 | GLY | GLU | ILE | ARG | ALA | THR | ALA | PHE | ASN | GLU | ||||
| 7 | GLN | VAL | ASP | LYS | PHE | PHE | PRO | LEU | ILE | GLU | ||||
| 8 | VAL | ASN | LYS | VAL | TYR | TYR | PHE | SER | LYS | GLY | ||||
| 9 | THR | LEU | LYS | ILE | ALA | ASN | LYS | GLN | PHE | THR | ||||
| 10 | ALA | VAL | LYS | ASN | ASP | TYR | GLU | MET | THR | PHE | ||||
| 11 | ASN | ASN | GLU | THR | SER | VAL | MET | PRO | CYS | GLU | ||||
| 12 | ASP | ASP | HIS | HIS | LEU | PRO | THR | VAL | GLN | PHE | ||||
| 13 | ASP | PHE | THR | GLY | ILE | ASP | ASP | LEU | GLU | ASN | ||||
| 14 | LYS | SER | LYS | ASP | SER | LEU | VAL | ASP | ILE | ILE | ||||
| 15 | GLY | ILE | CYS | LYS | SER | TYR | GLU | ASP | ALA | THR | ||||
| 16 | LYS | ILE | THR | VAL | ARG | SER | ASN | ASN | ALA | GLU | ||||
| 17 | VAL | ALA | LYS | ARG | ASN | ILE | TYR | LEU | MET | ASP | ||||
| 18 | THR | SER | GLY | LYS | VAL | VAL | THR | ALA | THR | LEU | ||||
| 19 | TRP | GLY | GLU | ASP | ALA | ASP | LYS | PHE | ASP | GLY | ||||
| 20 | SER | ARG | GLN | PRO | VAL | LEU | ALA | ILE | LYS | GLY | ||||
| 21 | ALA | ARG | VAL | SER | ASP | PHE | GLY | GLY | ARG | SER | ||||
| 22 | LEU | SER | VAL | LEU | SER | SER | SER | THR | ILE | ILE | ||||
| 23 | ALA | ASN | PRO | ASP | ILE | PRO | GLU | ALA | TYR | LYS | ||||
| 24 | LEU | ARG | GLY | TYR | PHE | ASP | ALA | GLU | GLY | GLY | ||||
| 25 | ALA | LEU |
Samples:
sample_1: entity_1, [U-15N], 50 uM; TRIS 20 ± 1 mM; potassium chloride 150 ± 2 mM; glycerol 10 ± 1 % w/v; DTT 1 ± 0.1 mM
sample_conditions_1: ionic strength: 170 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 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts