BMRB Entry 4841
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR4841
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: Spronk, Christian; Jansen, Jacobus; Tessari, Marco; Kaan, Anita; Aelen, Jan; Lasonder, Edwin; Stunnenberg, Hendrik; Vuister, Geerten. "Letter to the Editor: Sequence-specific Assignment of the PAH2 Domain of Sin3B
free and bound to Mad1" J. Biomol. NMR 19, 377-378 (2001).
PubMed: 11370785
Assembly members:
mSin3B-PAH2 domain, polymer, 105 residues, Formula weight is not available
Sin interaction domain of human Mad1, polymer, 13 residues, Formula weight is not available
Natural source: Common Name: mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX2T
Entity Sequences (FASTA):
mSin3B-PAH2 domain: ESDSVEFNNAISYVNKIKTR
FLDHPEIYRSFLEILHTYQK
EQLHTKGRPFRGMSEEEVFT
EVANLFRGQEDLLSEFGQFL
PEAKRSLFTGNGSAEMNSGQ
KNEEK
Sin interaction domain of human Mad1: NIQMLLEAADYLE
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 816 |
| 13C chemical shifts | 439 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PAH2 | 1 |
| 2 | Mad1 | 2 |
Entities:
Entity 1, PAH2 105 residues - Formula weight is not available
| 1 | GLU | SER | ASP | SER | VAL | GLU | PHE | ASN | ASN | ALA | ||||
| 2 | ILE | SER | TYR | VAL | ASN | LYS | ILE | LYS | THR | ARG | ||||
| 3 | PHE | LEU | ASP | HIS | PRO | GLU | ILE | TYR | ARG | SER | ||||
| 4 | PHE | LEU | GLU | ILE | LEU | HIS | THR | TYR | GLN | LYS | ||||
| 5 | GLU | GLN | LEU | HIS | THR | LYS | GLY | ARG | PRO | PHE | ||||
| 6 | ARG | GLY | MET | SER | GLU | GLU | GLU | VAL | PHE | THR | ||||
| 7 | GLU | VAL | ALA | ASN | LEU | PHE | ARG | GLY | GLN | GLU | ||||
| 8 | ASP | LEU | LEU | SER | GLU | PHE | GLY | GLN | PHE | LEU | ||||
| 9 | PRO | GLU | ALA | LYS | ARG | SER | LEU | PHE | THR | GLY | ||||
| 10 | ASN | GLY | SER | ALA | GLU | MET | ASN | SER | GLY | GLN | ||||
| 11 | LYS | ASN | GLU | GLU | LYS |
Entity 2, Mad1 13 residues - Formula weight is not available
| 1 | ASN | ILE | GLN | MET | LEU | LEU | GLU | ALA | ALA | ASP | ||||
| 2 | TYR | LEU | GLU |
Samples:
Typical_sample: mSin3B-PAH2 domain, [U-100% 13C; U-100% 15N], 1.0 mM; Sin interaction domain of human Mad1 1.0 mM; Potassium_Phosphate 50 mM; NaN3 mM; protease inhibitors mM
sample_conditions: pH: 6.3; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 13C-NOESY-HSQC | Typical_sample | not available | sample_conditions |
| 15N-NOESY-HSQC | Typical_sample | not available | sample_conditions |
| 15N-HMQC-NOESY-HSQC | Typical_sample | not available | sample_conditions |
| (13C-FILTERED)-NOESY-(13C-EDITED)-HSQC | Typical_sample | not available | sample_conditions |
| HNCA | Typical_sample | not available | sample_conditions |
| HNCO | Typical_sample | not available | sample_conditions |
| HN(CO)CA | Typical_sample | not available | sample_conditions |
| CBCA(CO)NNH | Typical_sample | not available | sample_conditions |
| HNCACB | Typical_sample | not available | sample_conditions |
| (H)CCH-TOCSY | Typical_sample | not available | sample_conditions |
| 15N-HSQC | Typical_sample | not available | sample_conditions |
| 13C-HSQC | Typical_sample | not available | sample_conditions |
| (13C/15N-FILTERED)-NOESY | Typical_sample | not available | sample_conditions |
| (13C/15N-FILTERED)-TOCSY | Typical_sample | not available | sample_conditions |
| HNHA | Typical_sample | not available | sample_conditions |
| HBHA(CBCACO)NNH | Typical_sample | not available | sample_conditions |
Software:
NMRPipe v1.7 - Data processing
XEASY v1.3.9 - Spectral analysis
CNS v1.0 - structure calculations
ARIA v1.0 - structure calculations and iterative NOE-assignment
NMR spectrometers:
- Varian Inova 500 MHz
- Varian Inova 750 MHz
- Bruker DRX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks