BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30353

Title: Solution structure of Rap1b/talin complex   PubMed: 29170462

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

Data typeCount
13C chemical shifts1391
15N chemical shifts399
1H chemical shifts2388

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 93 residues - 10607.293 Da.

1   GLYALAMETASPPROGLUPHEMETVALALA
2   LEUSERLEULYSILESERILEGLYASNVAL
3   VALLYSTHRMETGLNPHEGLUPROSERTHR
4   METVALTYRASPALACYSARGMETILEARG
5   GLUARGILEPROGLUALALEUALAGLYPRO
6   PROASNASPPHEGLYLEUPHELEUSERASP
7   ASPASPPROLYSLYSGLYILETRPLEUGLU
8   ALAGLYLYSALALEUASPTYRTYRMETLEU
9   ARGASNGLYASPTHRMETGLUTYRARGLYS
10   LYSGLNARG

Entity 2, entity_2 168 residues - 19200.734 Da.

1   HISMETARGGLUTYRLYSLEUVALVALLEU
2   GLYSERVALGLYVALGLYLYSSERALALEU
3   THRVALGLNPHEVALGLNGLYILEPHEVAL
4   GLULYSTYRASPPROTHRILEGLUASPSER
5   TYRARGLYSGLNVALGLUVALASPALAGLN
6   GLNCYSMETLEUGLUILELEUASPTHRALA
7   GLYTHRGLUGLNPHETHRALAMETARGASP
8   LEUTYRMETLYSASNGLYGLNGLYPHEALA
9   LEUVALTYRSERILETHRALAGLNSERTHR
10   PHEASNASPLEUGLNASPLEUARGGLUGLN
11   ILELEUARGVALLYSASPTHRASPASPVAL
12   PROMETILELEUVALGLYASNLYSCYSASP
13   LEUGLUASPGLUARGVALVALGLYLYSGLU
14   GLNGLYGLNASNLEUALAARGGLNTRPASN
15   ASNCYSALAPHELEUGLUSERSERALALYS
16   SERLYSILEASNVALASNGLUILEPHETYR
17   ASPLEUVALARGGLNILEASNARG

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:

NameSampleSample stateSample conditions
3D_15N/13C-edited NOESYsample_1isotropicsample_conditions_1
3D_15N/13C-edited NOESYsample_2isotropicsample_conditions_1
3D_15N-edited NOESYsample_3isotropicsample_conditions_1
3D_15N/13C-filtered NOESYsample_4isotropicsample_conditions_2
Standard triple-resonance experimentssample_5isotropicsample_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

Related Database Links: