BMRB Entry 18027
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18027
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Title: Solution NMR structure of CaM bound to iNOS CaM binding domain peptide PubMed: 22486744
Deposition date: 2011-10-29 Original release date: 2012-05-15
Authors: Piazza, Michael; Futrega, Kathryn; Spratt, Donald; Dieckmann, Thorsten; Guillemette, J.
Citation: Piazza, Michael; Futrega, Kathryn; Spratt, Donald; Dieckmann, Thorsten; Guillemette, J.. "Structure and Dynamics of Calmodulin (CaM) Bound to Nitric Oxide Synthase Peptides: Effects of a Phosphomimetic CaM Mutation" Biochemistry 51, 3651-3661 (2012).
Assembly members:
CaM, polymer, 148 residues, 16721.465 Da.
iNOS, polymer, 17 residues, 1967.644 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
Entity Sequences (FASTA):
CaM: ADQLTEEQIAEFKEAFSLFD
KDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTD
SEEEIREAFRVFDKDGNGYI
SAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEE
FVQMMTAK
iNOS: LKVLVKAVLFACMLMRK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 431 |
| 15N chemical shifts | 162 |
| 1H chemical shifts | 986 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CaM | 1 |
| 2 | iNOS | 2 |
Entities:
Entity 1, CaM 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, iNOS 17 residues - 1967.644 Da.
| 1 | LEU | LYS | VAL | LEU | VAL | LYS | ALA | VAL | LEU | PHE | ||||
| 2 | ALA | CYS | MET | LEU | MET | ARG | LYS |
Samples:
sample_1: entity_1, [U-99% 13C; U-99% 15N], 1.0 mM; entity_2 1.0 mM; potassium chloride 100 mM; calcium chloride 10 mM; sodium azide 0.2 mM; H2O 90%; D2O 10%
sample_2: entity_1 1.0 mM; entity_2, [U-99% 13C; U-99% 15N], 1.0 mM; potassium chloride 100 mM; calcium chloride 10 mM; sodium azide 0.2 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | 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 HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 700 MHz
Related Database Links:
| BMRB | 15184 15185 15186 15187 15188 15191 15470 15624 15650 15852 1634 16418 16465 1648 16764 17264 17360 17771 17807 18028 18556 19036 19238 19586 19604 25253 25257 26503 26626 26627 4056 4270 4284 4310 |
| PDB | |
| DBJ | BAA08302 BAA11896 BAA19786 BAA19787 BAA19788 BAA05531 BAA37123 BAG65119 |
| EMBL | CAA10601 CAA32050 CAA32062 CAA32119 CAA32120 CAA51512 |
| GB | AAA35635 AAA35641 AAA37365 AAA40862 AAA40863 AAA36375 AAA56666 AAA59171 AAB49041 AAB60366 |
| PIR | JC1305 MCON |
| PRF | 0409298A 0608335A 2001203A 2019232A |
| REF | NP_001008160 NP_001009759 NP_001027633 NP_001039714 NP_001040234 NP_000616 XP_001106048 XP_001106185 XP_001106245 XP_002827195 |
| SP | O02367 O16305 O96081 P02594 P05932 P35228 |
| TPG | DAA13808 DAA18029 DAA19590 DAA24777 DAA24988 |
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
SPARKY: Backbone
or all simulated shifts