BMRB Entry 34211
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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/BMR34211
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Title: Complex structure of PACSIN SH3 domain and TRPV4 proline rich region
Deposition date: 2017-11-30 Original release date: 2018-09-24
Authors: Glogowski, N.; Goretzki, B.; Diehl, E.; Duchardt-Ferner, E.; Hacker, C.; Hellmich, U.
Citation: Goretzki, B.; Glogowski, N.; Diehl, E.; Duchardt-Ferner, E.; Hacker, C.; Gaudet, R.; Hellmich, U.. "Complex structure of PACSIN SH3 domain and TRPV4 proline rich region" . ., .-..
Assembly members:
entity_1, polymer, 67 residues, 7398.386 Da.
entity_2, polymer, 15 residues, 1616.941 Da.
Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MKVPGVRVRALYDYTGQEAD
ELSFKAGEELMKISEEDEQG
WCKGRLLTGHVGLYPANYVE
KVGLAAA
entity_2: TKGPAPNPPPILKVW
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 227 |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 463 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 67 residues - 7398.386 Da.
| 1 | MET | LYS | VAL | PRO | GLY | VAL | ARG | VAL | ARG | ALA | ||||
| 2 | LEU | TYR | ASP | TYR | THR | GLY | GLN | GLU | ALA | ASP | ||||
| 3 | GLU | LEU | SER | PHE | LYS | ALA | GLY | GLU | GLU | LEU | ||||
| 4 | MET | LYS | ILE | SER | GLU | GLU | ASP | GLU | GLN | GLY | ||||
| 5 | TRP | CYS | LYS | GLY | ARG | LEU | LEU | THR | GLY | HIS | ||||
| 6 | VAL | GLY | LEU | TYR | PRO | ALA | ASN | TYR | VAL | GLU | ||||
| 7 | LYS | VAL | GLY | LEU | ALA | ALA | ALA |
Entity 2, entity_2 15 residues - 1616.941 Da.
| 1 | THR | LYS | GLY | PRO | ALA | PRO | ASN | PRO | PRO | PRO | ||||
| 2 | ILE | LEU | LYS | VAL | TRP |
Samples:
sample_1: Pacsin 3 SH3, [U-13C; U-15N], 250 uM; PRR, unlabeled, 1.25 mM
sample_4: Pacsin 3 SH3, unlabeled, 256.8 uM; PRR, selectively 13C P124 and 15N A125, 1.284 mM
sample_5: Pacsin 3 SH3, [U-13C; U-15N], 256.8 uM; PRR, selectively 13C P128, 1.284 mM
sample_6: Pacsin 3 SH3, [U-13C; U-15N], 576 uM; PRR, unlabeled, 2.88 mM
sample_7: Pacsin 3 SH3, [U-13C; U-15N], 250 uM
sample_8: Pacsin 3 SH3, unlabeled, 235 uM; PRR, selectively 13C P126, 1.175 mM
sample_9: Pacsin 3 SH3, unlabeled, 235 uM; PRR, selectively 13C K122 P130, 1.175 mM
sample_10: Pacsin 3 SH3, unlabeled, 229 uM; PRR, selectively 13C P129 K133, 1.145 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY-HSQC | sample_6 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_6 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_6 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_6 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_6 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_7 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_7 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_7 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_7 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_7 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_7 | isotropic | sample_conditions_1 |
| 2D 13C filtered and 13C edited NOESY-HSQC | sample_6 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_6 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_6 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_6 | isotropic | sample_conditions_1 |
| 3D 13C filtered and 13C edited NOESY-HSQC aromatic | sample_6 | isotropic | sample_conditions_1 |
| 3D 13C filtered and 13C edited NOESY-HSQC aliphatic | sample_6 | isotropic | sample_conditions_1 |
| 2D 13C filtered TOCSY | sample_6 | isotropic | sample_conditions_1 |
| 3D 13C filtered NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-13C NOESY-HSQC | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_9 | isotropic | sample_conditions_1 |
| 2D 1H-13C NOESY-HSQC | sample_5 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_5 | isotropic | sample_conditions_1 |
| 2D 1H-13C NOESY-HSQC | sample_8 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_8 | isotropic | sample_conditions_1 |
| 2D 1H-13C NOESY-HSQC | sample_9 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_10 | isotropic | sample_conditions_1 |
| 2D 1H-13C NOESY-HSQC | sample_10 | isotropic | sample_conditions_1 |
Software:
CYANA v3.9, Guentert - structure calculation
CARA v3.9, Keller and Wuthrich - chemical shift assignment
Analysis, CCPN - data analysis
TOPSPIN, Bruker Biospin - processing
OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 950 MHz
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts