BMRB Entry 30353
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30353
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of Rap1b/talin complex PubMed: 29170462
Deposition date: 2017-10-12 Original release date: 2017-11-28
Authors: Zhu, L.; Yang, J.; Qin, J.
Citation: Zhu, Liang; Yang, Jun; Bromberger, Thomas; Holly, Ashley; Lu, Fan; Liu, Huan; Sun, Kevin; Klapproth, Sarah; Hirbawi, Jamila; Byzova, Tatiana; Plow, Edward; Moser, Markus; Qin, Jun. "Structure of Rap1b bound to talin reveals a pathway for triggering integrin activation" Nat. Commun. 8, 1744-1744 (2017).
Assembly members:
entity_1, polymer, 93 residues, 10607.293 Da.
entity_2, polymer, 168 residues, 19200.734 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GAMDPEFMVALSLKISIGNV
VKTMQFEPSTMVYDACRMIR
ERIPEALAGPPNDFGLFLSD
DDPKKGIWLEAGKALDYYML
RNGDTMEYRKKQR
entity_2: HMREYKLVVLGSVGVGKSAL
TVQFVQGIFVEKYDPTIEDS
YRKQVEVDAQQCMLEILDTA
GTEQFTAMRDLYMKNGQGFA
LVYSITAQSTFNDLQDLREQ
ILRVKDTDDVPMILVGNKCD
LEDERVVGKEQGQNLARQWN
NCAFLESSAKSKINVNEIFY
DLVRQINR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 1391 |
| 15N chemical shifts | 399 |
| 1H chemical shifts | 2388 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 93 residues - 10607.293 Da.
| 1 | GLY | ALA | MET | ASP | PRO | GLU | PHE | MET | VAL | ALA | ||||
| 2 | LEU | SER | LEU | LYS | ILE | SER | ILE | GLY | ASN | VAL | ||||
| 3 | VAL | LYS | THR | MET | GLN | PHE | GLU | PRO | SER | THR | ||||
| 4 | MET | VAL | TYR | ASP | ALA | CYS | ARG | MET | ILE | ARG | ||||
| 5 | GLU | ARG | ILE | PRO | GLU | ALA | LEU | ALA | GLY | PRO | ||||
| 6 | PRO | ASN | ASP | PHE | GLY | LEU | PHE | LEU | SER | ASP | ||||
| 7 | ASP | ASP | PRO | LYS | LYS | GLY | ILE | TRP | LEU | GLU | ||||
| 8 | ALA | GLY | LYS | ALA | LEU | ASP | TYR | TYR | MET | LEU | ||||
| 9 | ARG | ASN | GLY | ASP | THR | MET | GLU | TYR | ARG | LYS | ||||
| 10 | LYS | GLN | ARG |
Entity 2, entity_2 168 residues - 19200.734 Da.
| 1 | HIS | MET | ARG | GLU | TYR | LYS | LEU | VAL | VAL | LEU | ||||
| 2 | GLY | SER | VAL | GLY | VAL | GLY | LYS | SER | ALA | LEU | ||||
| 3 | THR | VAL | GLN | PHE | VAL | GLN | GLY | ILE | PHE | VAL | ||||
| 4 | GLU | LYS | TYR | ASP | PRO | THR | ILE | GLU | ASP | SER | ||||
| 5 | TYR | ARG | LYS | GLN | VAL | GLU | VAL | ASP | ALA | GLN | ||||
| 6 | GLN | CYS | MET | LEU | GLU | ILE | LEU | ASP | THR | ALA | ||||
| 7 | GLY | THR | GLU | GLN | PHE | THR | ALA | MET | ARG | ASP | ||||
| 8 | LEU | TYR | MET | LYS | ASN | GLY | GLN | GLY | PHE | ALA | ||||
| 9 | LEU | VAL | TYR | SER | ILE | THR | ALA | GLN | SER | THR | ||||
| 10 | PHE | ASN | ASP | LEU | GLN | ASP | LEU | ARG | GLU | GLN | ||||
| 11 | ILE | LEU | ARG | VAL | LYS | ASP | THR | ASP | ASP | VAL | ||||
| 12 | PRO | MET | ILE | LEU | VAL | GLY | ASN | LYS | CYS | ASP | ||||
| 13 | LEU | GLU | ASP | GLU | ARG | VAL | VAL | GLY | LYS | GLU | ||||
| 14 | GLN | GLY | GLN | ASN | LEU | ALA | ARG | GLN | TRP | ASN | ||||
| 15 | ASN | CYS | ALA | PHE | LEU | GLU | SER | SER | ALA | LYS | ||||
| 16 | SER | LYS | ILE | ASN | VAL | ASN | GLU | ILE | PHE | TYR | ||||
| 17 | ASP | LEU | VAL | ARG | GLN | ILE | ASN | ARG |
Samples:
sample_3: Rap1b 0.7 mM; talin-F0, [U-15N; U-2H], 0.5 mM; NaCl 50 mM; MgCl2 5 mM
sample_4: Rap1b 0.7 mM; talin-F0, [U-13C; U-15N], 0.5 mM; NaCl 50 mM; MgCl2 5 mM
sample_5: Rap1b, [U-13C; U-15N], 0.6 mM; NaCl 50 mM; MgCl2 5 mM
sample_1: Rap1b, [U-13C; U-15N], 0.6 mM; talin-F0 0.9 mM; NaCl 50 mM; MgCl2 5 mM
sample_2: Rap1b 0.7 mM; talin-F0, [U-13C; U-15N], 0.5 mM; NaCl 50 mM; MgCl2 5 mM
sample_conditions_1: ionic strength: 55 mM; pH: 6.6; pressure: 101325 Pa; temperature: 301 K
sample_conditions_2: ionic strength: 55 mM; pH: 6.6; pressure: 101325 Pa; temperature: 301 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D_15N/13C-edited NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_15N/13C-edited NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D_15N-edited NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D_15N/13C-filtered NOESY | sample_4 | isotropic | sample_conditions_2 |
| Standard triple-resonance experiments | sample_5 | isotropic | sample_conditions_1 |
Software:
PASA, Xu, Wang, Yang, Vaynberg, Qin - chemical shift assignment
PIPP, Garrett - peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker AvanceIII 850 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