BMRB Entry 16370
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16370
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Title: Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin. Northeast Structural Genomics Target HR3158.
Deposition date: 2009-06-29 Original release date: 2009-06-29
Authors: Rossi, Paolo; Shastry, Ritu; Ciccosanti, Colleen; Hamilton, Keith; Xiao, Rong; Acton, Thomas; G.V.T., Swapna; Nair, Rajeesh; Everett, John; Rost, Burkhard; Montelione, Gaetano
Citation: Rossi, Paolo; Montelione, Gaetano. "Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin. Northeast Structural Genomics Target HR3158." Not known ., .-..
Assembly members:
Ig-like C2-type 2 Domain, polymer, 116 residues, 13338.323 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):
Ig-like C2-type 2 Domain: MGHHHHHHSHEHKRAPMFIY
KPQSKKVLEGDSVKLECQIS
AIPPPKLFWKRNNEMVQFNT
DRISLYQDNTGRVTLLIKDV
NKKDAGWYTVSAVNEAGVTT
CNTRLDVTARPNQTLP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 458 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 726 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ig-like C2-type 2 Domain | 1 |
Entities:
Entity 1, Ig-like C2-type 2 Domain 116 residues - 13338.323 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | GLU | HIS | LYS | ARG | ALA | PRO | MET | PHE | ILE | TYR | ||||
| 3 | LYS | PRO | GLN | SER | LYS | LYS | VAL | LEU | GLU | GLY | ||||
| 4 | ASP | SER | VAL | LYS | LEU | GLU | CYS | GLN | ILE | SER | ||||
| 5 | ALA | ILE | PRO | PRO | PRO | LYS | LEU | PHE | TRP | LYS | ||||
| 6 | ARG | ASN | ASN | GLU | MET | VAL | GLN | PHE | ASN | THR | ||||
| 7 | ASP | ARG | ILE | SER | LEU | TYR | GLN | ASP | ASN | THR | ||||
| 8 | GLY | ARG | VAL | THR | LEU | LEU | ILE | LYS | ASP | VAL | ||||
| 9 | ASN | LYS | LYS | ASP | ALA | GLY | TRP | TYR | THR | VAL | ||||
| 10 | SER | ALA | VAL | ASN | GLU | ALA | GLY | VAL | THR | THR | ||||
| 11 | CYS | ASN | THR | ARG | LEU | ASP | VAL | THR | ALA | ARG | ||||
| 12 | PRO | ASN | GLN | THR | LEU | PRO |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 0.87 mM; sodium chloride 200 mM; MES 20 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; Calcium Chloride 5 mM; H2O 90%; D2O 10%
sample_2: entity, [U-5% 13C], 0.68 mM; sodium chloride 200 mM; MES 20 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; Calcium Chloride 5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC hires | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N het_NOE | sample_2 | isotropic | sample_conditions_1 |
| 1D 15N_T1 series | sample_2 | isotropic | sample_conditions_1 |
| 1D 15N_T2 series | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
TOPSPIN v2.1, Bruker Biospin - collection
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
SPARKY v2.113, Goddard - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PINE, Bahrami, Markley, Assadi, and Eghbalnia - data analysis
Molmol, Koradi, Billeter and Wuthrich - structure visualization
PSVS v1.3, Bhattacharya and Montelione - structure validation
PyMol, DeLano Scientific - structure visualization
PDBStat v5.1, Tejero, Montelione - PDB processing
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts