Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR11038
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Ko, Sunggeon; Yu, Eun Young; Shin, Joon; Yoo, Hyun Hee; Tanaka, Toshiyuki; Kim, Woo Taek; Cho, Hyun-Soo; Lee, Weontae; Chung, In Kwon. "Solution structure of the DNA binding domain of rice telomere binding protein RTBP1" Biochemistry 48, 827-838 (2009).
PubMed: 19152316
Assembly members:
The DNA binding domain of RTBP1, polymer, 122 residues, 13862.927 Da.
Natural source: Common Name: Oryza sativa Taxonomy ID: 4530 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Oryza sativa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PGEX 4T-1
Entity Sequences (FASTA):
The DNA binding domain of RTBP1: GSPFADPNSLALANVPLSRS
KRPDFGQRRIRRPFTVAEVE
LLVEAVEHLGTGRWRDVKFR
AFENVHHRTYVDLKDKWKTL
VHTASIAPQQRRGAPVPQEL
LDRVLAAQAYWSVDSSGRIV
TL
Data type | Count |
13C chemical shifts | 409 |
15N chemical shifts | 113 |
1H chemical shifts | 678 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | The DNA binding domain of RTBP1 | 1 |
Entity 1, The DNA binding domain of RTBP1 122 residues - 13862.927 Da.
First G and S and "VDSSGRIVTL" in C-terminal were from cloining artifacts.
1 | GLY | SER | PRO | PHE | ALA | ASP | PRO | ASN | SER | LEU | ||||
2 | ALA | LEU | ALA | ASN | VAL | PRO | LEU | SER | ARG | SER | ||||
3 | LYS | ARG | PRO | ASP | PHE | GLY | GLN | ARG | ARG | ILE | ||||
4 | ARG | ARG | PRO | PHE | THR | VAL | ALA | GLU | VAL | GLU | ||||
5 | LEU | LEU | VAL | GLU | ALA | VAL | GLU | HIS | LEU | GLY | ||||
6 | THR | GLY | ARG | TRP | ARG | ASP | VAL | LYS | PHE | ARG | ||||
7 | ALA | PHE | GLU | ASN | VAL | HIS | HIS | ARG | THR | TYR | ||||
8 | VAL | ASP | LEU | LYS | ASP | LYS | TRP | LYS | THR | LEU | ||||
9 | VAL | HIS | THR | ALA | SER | ILE | ALA | PRO | GLN | GLN | ||||
10 | ARG | ARG | GLY | ALA | PRO | VAL | PRO | GLN | GLU | LEU | ||||
11 | LEU | ASP | ARG | VAL | LEU | ALA | ALA | GLN | ALA | TYR | ||||
12 | TRP | SER | VAL | ASP | SER | SER | GLY | ARG | ILE | VAL | ||||
13 | THR | LEU |
sample_1: The DNA binding domai of RTBP1, [U-99% 15N], 1 mM; Potassium phosphate 50 mM; NaCl 100 mM; NaN3 1 mM; H2O 90%; D2O 10%
sample_2: The DNA binding domai of RTBP1, [U-100% 13C], 1 mM; Potassium phosphate 50 mM; NaCl 100 mM; NaN3 1 mM; D2O 100%
sample_3: The DNA binding domai of RTBP1, [U-99% 13C; U-99% 15N], 1 mM; Potassium phosphate 50 mM; NaCl 100 mM; NaN3 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 Pa; temperature: 303 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
3D HNCO | sample_3 | isotropic | sample_conditions_1 |
3D HNCA | sample_3 | isotropic | sample_conditions_1 |
3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
CYANA v2.2.5, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
CYANA, Bruker Biospin - processing
CYANA, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CYANA, Goddard - chemical shift assignment, peak picking
CYANA, Cornilescu, Delaglio and Bax - data analysis
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks