BMRB Entry 18563
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18563
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Title: Solution NMR Structure of Ig like domain (805-892) of Obscurin-like protein 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8578K
Deposition date: 2012-06-30 Original release date: 2013-01-03
Authors: Pulavarti, Surya VSRK; Eletsky, Alex; Sukumaran, Dinesh; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Pederson, Kari; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas
Citation: Pulavarti, Surya VSRK; Eletsky, Alex; Sukumaran, Dinesh; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Pederson, Kari; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Ig like domain (805-892) of Obscurin-like protein 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8578K" To be published ., .-..
Assembly members:
HR8578K, polymer, 91 residues, 10165.419 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HR8578K: SHMPVHIVDPREHVFVHAIT
SECVMLACEVDREDAPVRWY
KDGQEVEESDFVVLENEGPH
RRLVLPATQPSDGGEFQCVA
GDECAYFTVTI
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 612 |
| 13C chemical shifts | 393 |
| 15N chemical shifts | 92 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR8578K | 1 |
Entities:
Entity 1, HR8578K 91 residues - 10165.419 Da.
| 1 | SER | HIS | MET | PRO | VAL | HIS | ILE | VAL | ASP | PRO | ||||
| 2 | ARG | GLU | HIS | VAL | PHE | VAL | HIS | ALA | ILE | THR | ||||
| 3 | SER | GLU | CYS | VAL | MET | LEU | ALA | CYS | GLU | VAL | ||||
| 4 | ASP | ARG | GLU | ASP | ALA | PRO | VAL | ARG | TRP | TYR | ||||
| 5 | LYS | ASP | GLY | GLN | GLU | VAL | GLU | GLU | SER | ASP | ||||
| 6 | PHE | VAL | VAL | LEU | GLU | ASN | GLU | GLY | PRO | HIS | ||||
| 7 | ARG | ARG | LEU | VAL | LEU | PRO | ALA | THR | GLN | PRO | ||||
| 8 | SER | ASP | GLY | GLY | GLU | PHE | GLN | CYS | VAL | ALA | ||||
| 9 | GLY | ASP | GLU | CYS | ALA | TYR | PHE | THR | VAL | THR | ||||
| 10 | ILE |
Samples:
sample_1: HR8578K.009, [U-100% 13C; U-100% 15N], 1.0 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%
sample_2: HR8578K.010, [U-5% 13C; U-100% 15N], 1.0 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%
sample_3: HR8578K.010, [U-5% 13C; U-100% 15N], 0.6 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; PF1 Phage 12.5 mg/mL; H2O 80%
sample_4: HR8578K.010, [U-5% 13C; U-100% 15N], 0.6 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; PEG 4%; H2O 80%
sample_conditions_1: pH: 6.5; 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-13C (CT-27 ms) HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C (CT-28 ms) HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C (CT-56 ms) HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C (CT-42 ms) HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY (Aliphatic) | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY (Aromatic) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC J-mod | sample_3 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC J-mod | sample_4 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC J-mod | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution
AutoStructure v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment
CARA v1.8.4, Keller and Wuthrich - peak picking, data analysis
XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment
CSI, Wishart, D.S. and B.D. Sykes. - data analysis
VNMRJ, Varian - collection
PROSA, Guntert - processing
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
PSVS, Bhattacharya, Montelione - structure validation
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts