Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16465
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: Juranic, Nenad; Atanasova, Elena; Filoteo, Adelaida; Macura, Slobodan; Prendergast, Franklyn; Penniston, John; Strehler, Emanuel. "Calmodulin Wraps around Its Binding Domain in the Plasma Membrane Ca2+ Pump Anchored by a Novel 18-1 Motif." J. Biol. Chem. 285, 4015-4024 (2010).
PubMed: 19996092
Assembly members:
entity_1, polymer, 148 residues, 16721.465 Da.
entity_2, polymer, 28 residues, 3360.028 Da.
CA, non-polymer, 40.078 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b
Entity Sequences (FASTA):
entity_1: ADQLTEEQIAEFKEAFSLFD
KDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTD
SEEEIREAFRVFDKDGNGYI
SAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEE
FVQMMTAK
entity_2: LRRGQILWFRGLNRIQTQIK
VVKAFHSS
Data type | Count |
13C chemical shifts | 758 |
15N chemical shifts | 191 |
1H chemical shifts | 1228 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Calmodulin | 1 |
2 | helical peptide | 2 |
3 | CALCIUM ION_1 | 3 |
4 | CALCIUM ION_2 | 3 |
5 | CALCIUM ION_3 | 3 |
6 | CALCIUM ION_4 | 3 |
Entity 1, Calmodulin 148 residues - 16721.465 Da.
1 | ALA | ASP | GLN | LEU | THR | GLU | GLU | GLN | ILE | ALA | ||||
2 | GLU | PHE | LYS | GLU | ALA | PHE | SER | LEU | PHE | ASP | ||||
3 | LYS | ASP | GLY | ASP | GLY | THR | ILE | THR | THR | LYS | ||||
4 | GLU | LEU | GLY | THR | VAL | MET | ARG | SER | LEU | GLY | ||||
5 | GLN | ASN | PRO | THR | GLU | ALA | GLU | LEU | GLN | ASP | ||||
6 | MET | ILE | ASN | GLU | VAL | ASP | ALA | ASP | GLY | ASN | ||||
7 | GLY | THR | ILE | ASP | PHE | PRO | GLU | PHE | LEU | THR | ||||
8 | MET | MET | ALA | ARG | LYS | MET | LYS | ASP | THR | ASP | ||||
9 | SER | GLU | GLU | GLU | ILE | ARG | GLU | ALA | PHE | ARG | ||||
10 | VAL | PHE | ASP | LYS | ASP | GLY | ASN | GLY | TYR | ILE | ||||
11 | SER | ALA | ALA | GLU | LEU | ARG | HIS | VAL | MET | THR | ||||
12 | ASN | LEU | GLY | GLU | LYS | LEU | THR | ASP | GLU | GLU | ||||
13 | VAL | ASP | GLU | MET | ILE | ARG | GLU | ALA | ASP | ILE | ||||
14 | ASP | GLY | ASP | GLY | GLN | VAL | ASN | TYR | GLU | GLU | ||||
15 | PHE | VAL | GLN | MET | MET | THR | ALA | LYS |
Entity 2, helical peptide 28 residues - 3360.028 Da.
1 | LEU | ARG | ARG | GLY | GLN | ILE | LEU | TRP | PHE | ARG | ||||
2 | GLY | LEU | ASN | ARG | ILE | GLN | THR | GLN | ILE | LYS | ||||
3 | VAL | VAL | LYS | ALA | PHE | HIS | SER | SER |
Entity 3, CALCIUM ION_1 - Ca - 40.078 Da.
1 | CA |
sample_1: entity_1, [U-99% 13C; U-99% 15N], 1 2 mM; entity_2, [U-99% 13C; U-99% 15N], 1 mM; H2O 95%; D2O 5%
sample_2: entity_1, [U-99% 13C; U-99% 15N], 1 2 mM; entity_2, [U-99% 13C; U-99% 15N], 1 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | anisotropic | sample_conditions_2 |
3D HNCO | sample_2 | anisotropic | sample_conditions_2 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_2 | isotropic | sample_conditions_1 |
X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinenment
FELIX vFelix NMR 2007, Accelrys Software Inc. - peak picking, processing
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - geometry optimization, refinenment
PREDITOR, Berjanskii MV, Neal S, Wishart DS - data analysis, torsion angles prediction
BMRB | 15184 15185 15186 15187 15188 15191 15470 15624 15650 15852 1634 16418 1648 16764 17264 17360 17771 17807 18027 18028 18556 19036 19238 19586 19604 25253 25257 26503 26626 26627 4056 4270 4284 4310 4284 |
PDB | |
DBJ | BAA08302 BAA11896 BAA19786 BAA19787 BAA19788 BAC27813 BAJ17688 |
EMBL | CAA10601 CAA32050 CAA32062 CAA32119 CAA32120 CAD97686 CAH18241 CAL38204 CAL38232 |
GB | AAA35635 AAA35641 AAA37365 AAA40862 AAA40863 AAA50819 AAB17578 AAF70246 AAX23599 AAZ73120 |
PIR | JC1305 MCON |
PRF | 0409298A 0608335A |
REF | NP_001008160 NP_001009759 NP_001027633 NP_001039714 NP_001040234 NP_001028098 NP_001675 XP_001156333 XP_001488333 XP_002760713 |
SP | O02367 O16305 O96081 P02594 P05932 |
TPG | DAA13808 DAA18029 DAA19590 DAA24777 DAA24988 DAA21543 |
AlphaFold | O96081 P05932 P02594 O16305 O02367 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks