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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34140
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: Franco-Echevarria, E.; Gonzalez-Polo, N.; Zorrilla, S.; Martinez-Lumbreras, S.; Santiveri, C.; Campos-Olivas, R.; Sanchez, M.; Calvo, O.; Gonzalez, B.; Perez-Canadillas, J.. "The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition." Nucleic Acids Res. 45, 10293-10305 (2017).
PubMed: 28973465
Assembly members:
entity_1, polymer, 179 residues, 20051.533 Da.
Natural source: Common Name: Baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Data type | Count |
13C chemical shifts | 453 |
15N chemical shifts | 182 |
1H chemical shifts | 1203 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
Entity 1, entity_1 179 residues - 20051.533 Da.
1 | SER | ILE | GLY | ALA | PRO | ASN | THR | THR | PHE | GLY | ||||
2 | THR | ASN | ASN | HIS | HIS | LEU | TYR | PRO | ASP | GLU | ||||
3 | LEU | ASN | VAL | SER | ASN | ASN | PRO | HIS | TYR | ARG | ||||
4 | PRO | LYS | PRO | VAL | SER | TYR | ASP | SER | THR | LEU | ||||
5 | PRO | PRO | ASP | HIS | ILE | LYS | VAL | TYR | SER | ARG | ||||
6 | THR | LEU | PHE | ILE | GLY | GLY | VAL | PRO | LEU | ASN | ||||
7 | MET | LYS | GLU | TRP | ASP | LEU | ALA | ASN | VAL | LEU | ||||
8 | LYS | PRO | PHE | ALA | GLU | VAL | GLN | SER | VAL | ILE | ||||
9 | LEU | ASN | ASN | SER | ARG | LYS | HIS | ALA | PHE | VAL | ||||
10 | LYS | VAL | TYR | SER | ARG | HIS | GLU | ALA | GLU | ASN | ||||
11 | VAL | LEU | GLN | ASN | PHE | ASN | LYS | ASP | GLY | ALA | ||||
12 | LEU | PRO | LEU | ARG | THR | ARG | TRP | GLY | VAL | GLY | ||||
13 | PHE | GLY | PRO | ARG | ASP | CYS | CYS | ASP | TYR | GLN | ||||
14 | HIS | GLY | TYR | SER | ILE | ILE | PRO | MET | HIS | ARG | ||||
15 | LEU | THR | ASP | ALA | ASP | LYS | LYS | TRP | SER | VAL | ||||
16 | SER | ALA | GLN | TRP | GLY | GLY | THR | SER | GLY | GLN | ||||
17 | PRO | LEU | VAL | THR | GLY | ILE | VAL | PHE | GLU | GLU | ||||
18 | PRO | ASP | ILE | ILE | VAL | GLY | GLU | GLY | VAL |
sample_1: DTT 1 mM; Nrd1, [U-100% 13C; U-100% 15N], 600 uM; potassium phosphate 25 mM; sodium chloride 25 mM
sample_2: DTT 1 mM; Nrd1 800 uM; potassium phosphate 25 mM; sodium chloride 25 mM
sample_3: DTT 1 mM; Nrd1, [U-100% 13C; U-100% 15N] expect for Phe and Leu residues, 400 uM; potassium phosphate 25 mM; sodium chloride 25 mM
sample_4: DTT 1 mM; Nrd1, [U-100% 13C; U-100% 15N] expect for Ile residues, 400 uM; potassium phosphate 25 mM; sodium chloride 25 mM
sample_5: DTT 1 mM; Nrd1, [U-100% 13C; U-100% 15N] expect for Arg residues, 400 uM; potassium phosphate 25 mM; sodium chloride 25 mM
sample_conditions_1: ionic strength: 59.1 mM; pH: 6.5; 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY F1filtered | sample_3 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY F1filtered | sample_4 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY F1filtered | sample_5 | isotropic | sample_conditions_1 |
AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
Analysis, CCPN - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks