BMRB Entry 6498
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6498
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Title: Backbone and side-chain 1H, 13C, and 15N Chemical Shift Assignments for SIP (1-77) PubMed: 15996101
Deposition date: 2005-02-08 Original release date: 2005-08-16
Authors: Bhattacharya, Shibani; Lee, Young-Tae; Michowski, Wojciech; Filipek, Anna; Kuznicki, Jacek; Chazin, Walter
Citation: Bhattacharya, Shibani; Lee, Young-Tae; Michowski, Wojciech; Filipek, Anna; Kuznicki, Jacek; Chazin, Walter. "The Modular Structure of SIP Facilitates Its Role in Stabilizing Multiprotein Assemblies(,)." Biochemistry 44, 9462-9471 (2005).
Assembly members:
single chain biopolymer, polymer, 77 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
Entity Sequences (FASTA):
single chain biopolymer: MASVLEELQKDLEEVKVLLE
KSTRKRLRDTLTSEKSKIET
ELKNKMQQKSQKKPELDNEK
PAAVVAPLTTGYTVKIS
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 561 |
| 13C chemical shifts | 335 |
| 15N chemical shifts | 77 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SIP N-Domain, SIP (1-77) | 1 |
Entities:
Entity 1, SIP N-Domain, SIP (1-77) 77 residues - Formula weight is not available
| 1 | MET | ALA | SER | VAL | LEU | GLU | GLU | LEU | GLN | LYS | ||||
| 2 | ASP | LEU | GLU | GLU | VAL | LYS | VAL | LEU | LEU | GLU | ||||
| 3 | LYS | SER | THR | ARG | LYS | ARG | LEU | ARG | ASP | THR | ||||
| 4 | LEU | THR | SER | GLU | LYS | SER | LYS | ILE | GLU | THR | ||||
| 5 | GLU | LEU | LYS | ASN | LYS | MET | GLN | GLN | LYS | SER | ||||
| 6 | GLN | LYS | LYS | PRO | GLU | LEU | ASP | ASN | GLU | LYS | ||||
| 7 | PRO | ALA | ALA | VAL | VAL | ALA | PRO | LEU | THR | THR | ||||
| 8 | GLY | TYR | THR | VAL | LYS | ILE | SER |
Samples:
Sample_1: single chain biopolymer, [U-100% 13C; U-100% 15N], 1.0 mM; NaPi 20.0 mM; NaCl 50 mM; H2O 90%
Sample_2: single chain biopolymer, [U-100% 13C], 1 mM; NaPi 20 mM; NaCl 50 mM; D2O 100%
Sample_3: single chain biopolymer, [U-10% 13C], 1 mM; NaPi 20 mM; NaCl 50 mM; D2O 100%
Exp_cond_1: pH: 7.0; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-15N HSQC | not available | not available | not available |
| 1H-13C CT-HSQC | not available | not available | not available |
| 3D-HNCO | not available | not available | not available |
| 3D-HNCACB | not available | not available | not available |
| 3D-CBCA(CO)NH | not available | not available | not available |
| 3D-HC(CCO)NH | not available | not available | not available |
| 3D-(H)CC(CO)NH | not available | not available | not available |
| 3D-HCCH-TOCSY | not available | not available | not available |
Software:
FELIX v2000 - processing, analysis
NMR spectrometers:
- Bruker AVANCE 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts