BMRB Entry 19753
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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/BMR19753
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Title: Solution NMR Structure plectin repeat domain 6 (4403-4606) of Plectin from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR6354E
Deposition date: 2014-01-24 Original release date: 2014-02-24
Authors: Pulavarti, Surya VSRK; Eletsky, Alexander; Huang, Yuanpeng; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation: Pulavarti, Surya VSRK; Eletsky, Alexander; Huang, Yuanpeng; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure plectin repeat domain 6 (4403-4606) of Plectin from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR6354E" Not known ., .-..
Assembly members:
Plectin, polymer, 215 residues, 23730 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):
Plectin: MGHHHHHHSHMQLASWSDPT
EETGPVAGILDTETLEKVSI
TEAMHRNLVDNITGQRLLEA
QACTGGIIDPSTGERFPVTD
AVNKGLVDKIMVDRINLAQK
AFCGFEDPRTKTKMSAAQAL
KKGWLYYEAGQRFLEVQYLT
GGLIEPDTPGRVPLDEALQR
GTVDARTAQKLRDVGAYSKY
LTCPKTKLKISYKDALDRSM
VEEGTGLRLLEAAAQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 662 |
| 15N chemical shifts | 195 |
| 1H chemical shifts | 483 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Plectin repeat domain 6 | 1 |
Entities:
Entity 1, Plectin repeat domain 6 215 residues - 23730 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | GLN | LEU | ALA | SER | TRP | SER | ASP | PRO | THR | ||||
| 3 | GLU | GLU | THR | GLY | PRO | VAL | ALA | GLY | ILE | LEU | ||||
| 4 | ASP | THR | GLU | THR | LEU | GLU | LYS | VAL | SER | ILE | ||||
| 5 | THR | GLU | ALA | MET | HIS | ARG | ASN | LEU | VAL | ASP | ||||
| 6 | ASN | ILE | THR | GLY | GLN | ARG | LEU | LEU | GLU | ALA | ||||
| 7 | GLN | ALA | CYS | THR | GLY | GLY | ILE | ILE | ASP | PRO | ||||
| 8 | SER | THR | GLY | GLU | ARG | PHE | PRO | VAL | THR | ASP | ||||
| 9 | ALA | VAL | ASN | LYS | GLY | LEU | VAL | ASP | LYS | ILE | ||||
| 10 | MET | VAL | ASP | ARG | ILE | ASN | LEU | ALA | GLN | LYS | ||||
| 11 | ALA | PHE | CYS | GLY | PHE | GLU | ASP | PRO | ARG | THR | ||||
| 12 | LYS | THR | LYS | MET | SER | ALA | ALA | GLN | ALA | LEU | ||||
| 13 | LYS | LYS | GLY | TRP | LEU | TYR | TYR | GLU | ALA | GLY | ||||
| 14 | GLN | ARG | PHE | LEU | GLU | VAL | GLN | TYR | LEU | THR | ||||
| 15 | GLY | GLY | LEU | ILE | GLU | PRO | ASP | THR | PRO | GLY | ||||
| 16 | ARG | VAL | PRO | LEU | ASP | GLU | ALA | LEU | GLN | ARG | ||||
| 17 | GLY | THR | VAL | ASP | ALA | ARG | THR | ALA | GLN | LYS | ||||
| 18 | LEU | ARG | ASP | VAL | GLY | ALA | TYR | SER | LYS | TYR | ||||
| 19 | LEU | THR | CYS | PRO | LYS | THR | LYS | LEU | LYS | ILE | ||||
| 20 | SER | TYR | LYS | ASP | ALA | LEU | ASP | ARG | SER | MET | ||||
| 21 | VAL | GLU | GLU | GLY | THR | GLY | LEU | ARG | LEU | LEU | ||||
| 22 | GLU | ALA | ALA | ALA | GLN |
Samples:
sample_1: Plectin, [U-100% 13C; U-100% 15N; U-2H; ILV-1H], 1 mM; MES pH 6.5 20 mM; NaCL 100 mM; CaCL2 5 mM; DTT 10 mM; NaN3 0.02%; Proteinase Inhibitors 1 ratio; DSS 50 uM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; 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 ct [13C,1H] HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D HMCM[CG]CBCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HMCMCBCA | sample_1 | isotropic | sample_conditions_1 |
| 3D [H]-NOESY-[NH/CH] ( mix= 250 ms) | sample_1 | isotropic | sample_conditions_1 |
Software:
vnmrj, Varian - Data collection
prosa, Guntert - processing
CARA, Keller and Wuthrich - data analysis
autoassign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CSI, CSI (Wishart and Sykes) - Secondary structure analysis
TALOS+, (TALOS+) -Shen, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts