BMRB Entry 11212
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11212
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Title: Solution structure of the first ig-like domain of Myosin-binding protein C, slow-type
Deposition date: 2010-07-22 Original release date: 2011-07-21
Authors: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.
Citation: Qin, X.; Nagashima, T.; Hayashi, F.; Yokoyama, S.. "Solution structure of the first ig-like domain of Myosin-binding protein C, slow-type" . ., .-..
Assembly members:
IG domain, polymer, 126 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: cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
IG domain: GSSGSSGILFIEKPQGGTVK
VGEDITFIAKVKAEDLLRKP
TIKWFKGKWMDLASKAGKHL
QLKETFERHSRVYTFEMQII
KAKDNFAGNYRCEVTYKDKF
DSCSFDLEVHESTGTTPNID
SGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 550 |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 865 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | IG domain of Myosin-binding protein C, slow-type | 1 |
Entities:
Entity 1, IG domain of Myosin-binding protein C, slow-type 126 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | ILE | LEU | PHE | ||||
| 2 | ILE | GLU | LYS | PRO | GLN | GLY | GLY | THR | VAL | LYS | ||||
| 3 | VAL | GLY | GLU | ASP | ILE | THR | PHE | ILE | ALA | LYS | ||||
| 4 | VAL | LYS | ALA | GLU | ASP | LEU | LEU | ARG | LYS | PRO | ||||
| 5 | THR | ILE | LYS | TRP | PHE | LYS | GLY | LYS | TRP | MET | ||||
| 6 | ASP | LEU | ALA | SER | LYS | ALA | GLY | LYS | HIS | LEU | ||||
| 7 | GLN | LEU | LYS | GLU | THR | PHE | GLU | ARG | HIS | SER | ||||
| 8 | ARG | VAL | TYR | THR | PHE | GLU | MET | GLN | ILE | ILE | ||||
| 9 | LYS | ALA | LYS | ASP | ASN | PHE | ALA | GLY | ASN | TYR | ||||
| 10 | ARG | CYS | GLU | VAL | THR | TYR | LYS | ASP | LYS | PHE | ||||
| 11 | ASP | SER | CYS | SER | PHE | ASP | LEU | GLU | VAL | HIS | ||||
| 12 | GLU | SER | THR | GLY | THR | THR | PRO | ASN | ILE | ASP | ||||
| 13 | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: IG domain, [U-13C; U-15N], 1.32 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | sample_1 | isotropic | condition_1 |
| 3D 13C-separated NOESY | sample_1 | isotropic | condition_1 |
Software:
VNMR v6.1C, Varian - collection
NMRPipe v20031121, Delaglio F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.9296, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAF85665 BAG51755 BAG59277 BAH13954 |
| EMBL | CAD38625 CAD38925 CAD89907 CAD89927 CAD91144 |
| GB | AAI43504 AAI43505 ACE86664 ACE87348 EAW97664 |
| REF | NP_001241647 NP_001241648 NP_001241649 NP_002456 NP_996555 |
| SP | Q00872 |
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or all simulated shifts