BMRB Entry 34161
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34161
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: Solution structure of the complex of TRPV5(655-725) with a Calmodulin E32Q/E68Q double mutant PubMed: 29584409
Deposition date: 2017-07-09 Original release date: 2018-04-20
Authors: Vuister, G.; Bokhovchuk, F.; Bate, N.; Kovalevskaya, N.; Goult, B.; Spronk, C.
Citation: Bokhovchuk, F.; Bate, N.; Kovalevskaya, N.; Goult, B.; Spronk, C.; Vuister, G.. "The Structural Basis of Calcium Dependent Inactivation of the Transient Receptor Potential Vanilloid 5 Channel." Biochemistry 57, 2623-2635 (2018).
Assembly members:
entity_1, polymer, 150 residues, 16937.652 Da.
entity_2, polymer, 73 residues, 7722.194 Da.
entity_CA, non-polymer, 40.078 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 BL21
Entity Sequences (FASTA):
entity_1: SMADQLTEEQIAEFKEAFSL
FDKDGDGTITTKQLGTVMRS
LGQNPTEAELQDMINEVDAD
GNGTIDFPQFLTMMARKMKD
TDSEEEIREAFRVFDKDGNG
YISAAELRHVMTNLGEKLTD
EEVDEMIREADIDGDGQVNY
EEFVQMMTAK
entity_2: GADKEDDQEHPSEKQPSGAE
SGTLARASLALPTSSLSRTA
SQSSSHRGWEILRQNTLGHL
NLGLNLSEGDGEE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 482 |
| 15N chemical shifts | 181 |
| 1H chemical shifts | 1103 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
| 3 | entity_3, 1 | 3 |
| 4 | entity_3, 2 | 3 |
Entities:
Entity 1, entity_1 150 residues - 16937.652 Da.
| 1 | SER | MET | ALA | ASP | GLN | LEU | THR | GLU | GLU | GLN | |
| 2 | ILE | ALA | GLU | PHE | LYS | GLU | ALA | PHE | SER | LEU | |
| 3 | PHE | ASP | LYS | ASP | GLY | ASP | GLY | THR | ILE | THR | |
| 4 | THR | LYS | GLN | LEU | GLY | THR | VAL | MET | ARG | SER | |
| 5 | LEU | GLY | GLN | ASN | PRO | THR | GLU | ALA | GLU | LEU | |
| 6 | GLN | ASP | MET | ILE | ASN | GLU | VAL | ASP | ALA | ASP | |
| 7 | GLY | ASN | GLY | THR | ILE | ASP | PHE | PRO | GLN | PHE | |
| 8 | LEU | THR | MET | MET | ALA | ARG | LYS | MET | LYS | ASP | |
| 9 | THR | ASP | SER | GLU | GLU | GLU | ILE | ARG | GLU | ALA | |
| 10 | PHE | ARG | VAL | PHE | ASP | LYS | ASP | GLY | ASN | GLY | |
| 11 | TYR | ILE | SER | ALA | ALA | GLU | LEU | ARG | HIS | VAL | |
| 12 | MET | THR | ASN | LEU | GLY | GLU | LYS | LEU | THR | ASP | |
| 13 | GLU | GLU | VAL | ASP | GLU | MET | ILE | ARG | GLU | ALA | |
| 14 | ASP | ILE | ASP | GLY | ASP | GLY | GLN | VAL | ASN | TYR | |
| 15 | GLU | GLU | PHE | VAL | GLN | MET | MET | THR | ALA | LYS |
Entity 2, entity_2 73 residues - 7722.194 Da.
| 1 | GLY | ALA | ASP | LYS | GLU | ASP | ASP | GLN | GLU | HIS | ||||
| 2 | PRO | SER | GLU | LYS | GLN | PRO | SER | GLY | ALA | GLU | ||||
| 3 | SER | GLY | THR | LEU | ALA | ARG | ALA | SER | LEU | ALA | ||||
| 4 | LEU | PRO | THR | SER | SER | LEU | SER | ARG | THR | ALA | ||||
| 5 | SER | GLN | SER | SER | SER | HIS | ARG | GLY | TRP | GLU | ||||
| 6 | ILE | LEU | ARG | GLN | ASN | THR | LEU | GLY | HIS | LEU | ||||
| 7 | ASN | LEU | GLY | LEU | ASN | LEU | SER | GLU | GLY | ASP | ||||
| 8 | GLY | GLU | GLU |
Entity 3, entity_3, 1 - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: Calmodulin, [U-99% 13C; U-99% 15N], 220 ± 0.05 uM; hTRPV5(655-725) 220 ± 0.05 uM
sample_2: Calmodulin, [U-99% 15N], 380 ± 0.05 uM; hTRPV5(655-725), [U-99% 13C; U-99% 15N], 380 ± 0.05 uM
sample_conditions_1: ionic strength: 84 mM; pH: 7.4; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
Software:
Analysis v2.4, CCPN - chemical shift assignment, peak picking
AnalysisAssign v3.0, CCPN - chemical shift assignment
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
YASARA v15.6, Yasara Biosciences; Krieger et al. - refinement
NMRPipe v7.9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing
NMR spectrometers:
- Bruker AVI 500 MHz
- Bruker AVIII 600 MHz
- Bruker AVII 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts