BMRB Entry 6004
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6004
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Title: 1H, 13C, 15N assignments of human Cofilin PubMed: 15213453
Deposition date: 2003-11-14 Original release date: 2004-11-15
Authors: Zierler-Gould, K.; Pope, B.; Weeds, A.; Ball, L.
Citation: Zierler-Gould, K.; Pope, B.; Weeds, A.; Ball, L.. "Letter to the editor: Backbone and sidechain 1H, 13C and 15N resonance assignments of human cofilin " J. Biomol. NMR 29, 429-430 (2004).
Assembly members:
cofilin, polymer, 166 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
cofilin: MASGVAVSDGVIKVFNDMKV
RKSSTPEEVKKRKKAVLFCL
SEDKKNIILEEGKEILVGDV
GQTVDDPYATFVKMLPDKDC
RYALYDATYETKESKKEDLV
FIFWAPESAPLKSKMIYASS
KDAIKKKLTGIKHELQANCY
EEVKDRCTLAEKLGGSAVIS
LEGKPL
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 1166 |
13C chemical shifts | 534 |
15N chemical shifts | 164 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | cofilin | 1 |
Entities:
Entity 1, cofilin 166 residues - Formula weight is not available
1 | MET | ALA | SER | GLY | VAL | ALA | VAL | SER | ASP | GLY | ||||
2 | VAL | ILE | LYS | VAL | PHE | ASN | ASP | MET | LYS | VAL | ||||
3 | ARG | LYS | SER | SER | THR | PRO | GLU | GLU | VAL | LYS | ||||
4 | LYS | ARG | LYS | LYS | ALA | VAL | LEU | PHE | CYS | LEU | ||||
5 | SER | GLU | ASP | LYS | LYS | ASN | ILE | ILE | LEU | GLU | ||||
6 | GLU | GLY | LYS | GLU | ILE | LEU | VAL | GLY | ASP | VAL | ||||
7 | GLY | GLN | THR | VAL | ASP | ASP | PRO | TYR | ALA | THR | ||||
8 | PHE | VAL | LYS | MET | LEU | PRO | ASP | LYS | ASP | CYS | ||||
9 | ARG | TYR | ALA | LEU | TYR | ASP | ALA | THR | TYR | GLU | ||||
10 | THR | LYS | GLU | SER | LYS | LYS | GLU | ASP | LEU | VAL | ||||
11 | PHE | ILE | PHE | TRP | ALA | PRO | GLU | SER | ALA | PRO | ||||
12 | LEU | LYS | SER | LYS | MET | ILE | TYR | ALA | SER | SER | ||||
13 | LYS | ASP | ALA | ILE | LYS | LYS | LYS | LEU | THR | GLY | ||||
14 | ILE | LYS | HIS | GLU | LEU | GLN | ALA | ASN | CYS | TYR | ||||
15 | GLU | GLU | VAL | LYS | ASP | ARG | CYS | THR | LEU | ALA | ||||
16 | GLU | LYS | LEU | GLY | GLY | SER | ALA | VAL | ILE | SER | ||||
17 | LEU | GLU | GLY | LYS | PRO | LEU |
Samples:
sample_1: cofilin, [U-15N; U-13C], 0.8 mM; phosphate buffer 10 mM; H2O 90%; D2O 10%
sample_2: cofilin, [U-15N], 1 mM; phosphate buffer 10 mM; H2O 90%; D2O 10%
sample_cond_1: pH: 6.0; temperature: 300 K; ionic strength: 10 mM; pressure: 1 atm
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 13C-separated NOESY-HSQC in H2O (aliphatic centred) | not available | not available | not available |
3D 13C-separated NOESY-HSQC in H2O (aromatic centred) | not available | not available | not available |
3D 15N-separated NOESY-HSQC | not available | not available | not available |
3D HNHA | not available | not available | not available |
3D HNHB | not available | not available | not available |
2D NOESY | not available | not available | not available |
2D TOCSY | not available | not available | not available |
2D DQF-COSY | not available | not available | not available |
Software:
XWINNMR v1.3 - acquisition, processing
AZARA v2.1 - processing, viewing
ANSIG v3.3 - assignment, integration, creation of NOE restraint lists
CNS v1.1 - structure solution, refinement
NMR spectrometers:
- Bruker DMX 750 MHz
Related Database Links:
PDB | |
DBJ | BAA00364 BAA00589 BAB29074 BAB32114 BAC34363 |
EMBL | CAA44694 CAA64685 |
GB | AAA31020 AAA64501 AAH11005 AAH12265 AAH12318 |
REF | NP_001004043 NP_001009484 NP_001015655 NP_001253534 NP_005498 |
SP | P10668 P18760 P23528 P45592 Q4R5C0 |
TPG | DAA13572 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts