BMRB Entry 17016

Title:
solution structure of the CARMIL CAH3a/b domain bound to capping protein (CP_
Deposition date:
2010-06-23
Original release date:
2010-08-12
Authors:
Zwolak, Adam; Nico, Tjandra
Citation:

Citation: Zwolak, Adam; Uruno, Takehito; Piszczek, Grzegorz; Hammer, John; Tjandra, Nico. "Molecular basis for barbed end uncapping by CARMIL homology domain 3 of mouse CARMIL-1."  J. Biol. Chem. 285, 29014-29026 (2010).
PubMed: 20630878

Assembly members:

Assembly members:
CPalpha_subunit, polymer, 286 residues, Formula weight is not available
CPbeta_subunit, polymer, 277 residues, Formula weight is not available
CARMIL_CAH3a_b_domain, polymer, 81 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET

Data sets:
Data typeCount
13C chemical shifts1504
15N chemical shifts474
1H chemical shifts474

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CPalpha_subunit1
2CPbeta_subunit2
3CARMIL_CAH3a_b_domain3

Entities:

Entity 1, CPalpha_subunit 286 residues - Formula weight is not available

1   METALAASPPHEGLUASPARGVALSERASP
2   GLUGLULYSVALARGILEALAALALYSPHE
3   ILETHRHISALAPROPROGLYGLUPHEASN
4   GLUVALPHEASNASPVALARGLEULEULEU
5   ASNASNASPASNLEULEUARGGLUGLYALA
6   ALAHISALAPHEALAGLNTYRASNMETASP
7   GLNPHETHRPROVALLYSILEGLUGLYTYR
8   ASPASPGLNVALLEUILETHRGLUHISGLY
9   ASPLEUGLYASNSERARGPHELEUASPPRO
10   ARGASNGLNILESERPHELYSPHEASPHIS
11   LEUARGLYSGLUALASERASPPROGLNPRO
12   GLUASPVALASPGLYGLYLEULYSSERTRP
13   ARGGLUSERCYSASPSERALALEUARGALA
14   TYRVALLYSASPHISTYRSERASNGLYPHE
15   CYSTHRVALTYRALALYSTHRILEASPGLY
16   GLNGLNTHRILEILEALACYSILEGLUSER
17   HISGLNPHEGLNPROLYSASNPHETRPASN
18   GLYARGTRPARGSERGLUTRPLYSPHETHR
19   ILETHRPROPROSERALAGLNVALVALALA
20   VALLEULYSILEGLNVALHISTYRTYRGLU
21   ASPGLYASNVALGLNLEUVALSERHISLYS
22   ASPVALGLNASPSERVALTHRVALSERASN
23   GLUVALGLNTHRALALYSGLUPHEILELYS
24   ILEILEGLUSERALAGLUASNGLUTYRGLN
25   THRALAILESERGLUASNTYRGLNTHRMET
26   SERASPTHRTHRPHELYSALALEUARGARG
27   GLNLEUPROVALTHRARGTHRLYSILEASP
28   TRPASNLYSILELEUSERTYRLYSILEGLY
29   LYSGLUMETGLNASNALA

Entity 2, CPbeta_subunit 277 residues - Formula weight is not available

1   METSERASPGLNGLNLEUASPCYSALALEU
2   ASPLEUMETARGARGLEUPROPROGLNGLN
3   ILEGLULYSASNLEUSERASPLEUILEASP
4   LEUVALPROSERLEUCYSGLUASPLEULEU
5   SERSERVALASPGLNPROLEULYSILEALA
6   ARGASPLYSVALVALGLYLYSASPTYRLEU
7   LEUCYSASPTYRASNARGASPGLYASPSER
8   TYRARGSERPROTRPSERASNLYSTYRASP
9   PROPROLEUGLUASPGLYALAMETPROSER
10   ALAARGLEUARGLYSLEUGLUVALGLUALA
11   ASNASNALAPHEASPGLNTYRARGASPLEU
12   TYRPHEGLUGLYGLYVALSERSERVALTYR
13   LEUTRPASPLEUASPHISGLYPHEALAGLY
14   VALILELEUILELYSLYSALAGLYASPGLY
15   SERLYSLYSILELYSGLYCYSTRPASPSER
16   ILEHISVALVALGLUVALGLNGLULYSSER
17   SERGLYARGTHRALAHISTYRLYSLEUTHR
18   SERTHRVALMETLEUTRPLEUGLNTHRASN
19   LYSTHRGLYSERGLYTHRMETASNLEUGLY
20   GLYSERLEUTHRARGGLNMETGLULYSASP
21   GLUTHRVALSERASPSERSERPROHISILE
22   ALAASNILEGLYARGLEUVALGLUASPMET
23   GLUASNLYSILEARGSERTHRLEUASNGLU
24   ILETYRPHEGLYLYSTHRLYSASPILEVAL
25   ASNGLYLEUARGSERVALGLNTHRPHEALA
26   ASPLYSSERLYSGLNGLUALALEULYSASN
27   ASPLEUVALGLUALALEULYSARGLYSGLN
28   GLNCYSILEGLNPROASPASN

Entity 3, CARMIL_CAH3a_b_domain 81 residues - Formula weight is not available

1   GLYALAMETGLYSERTRPSERVALARGGLN
2   GLULYSARGSERSERGLYLEUILESERGLU
3   LEUPROSERGLUGLUGLYARGARGLEUGLU
4   HISPHETHRLYSLEUARGPROLYSARGASN
5   LYSLYSGLNGLNPROTHRGLNALAALAVAL
6   CYSTHRILESERILELEUPROGLNASPGLY
7   GLUGLNASNGLYLEUMETGLYARGVALASP
8   GLUGLYVALASPGLUPHEPHETHRLYSLYS
9   VAL

Samples:

CP_chemical_shift_perturpation: CPalpha subunit, [U-99% 15N; U-80% 2H], 0.35 mM; CPbeta subunit, [U-99% 15N; U-80% 2H], 0.35 mM; CARMIL CAH3a/b domain, [U-2H], 0.39 mM; H2O 93%; D2O 7%

CAH3a_b_chemical_shift_perturpation: CARMIL CAH3a/b domain, [U-99% 15N; U-80% 2H], 0.35 mM; CPalpha subunit, [U-2H], 0.39 mM; CPbeta subunit, [U-2H], 0.39 mM; H2O 93%; D2O 7%

intermolecular_PRE: CPalpha subunit, [U-99% 15N; U-80% 2H], 0.35 mM; CPbeta subunit, [U-99% 15N; U-80% 2H], 0.35 mM; CARMIL CAH3a/b domain, [U-2H; spin labeled at 1 or 5 postions], 0.39 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCCP_chemical_shift_perturpationisotropicsample_conditions_1
2D 1H-15N HSQCCAH3a_b_chemical_shift_perturpationisotropicsample_conditions_1
2D 1H-15N HSQCintermolecular_PREisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PIPP, Garrett - chemical shift assignment, chemical shift calculation, peak picking

X-PLOR NIH v2.23, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

DBJ BAE27053 BAE27635 BAE28985 BAE30242 BAE31154 BAE33851 BAE35614 BAE37051 BAE40579 BAG35935 BAC31591
GB AAC00566 AAH16232 AAH85506 AAI66464 EDL07559 AAA52222 AAA52227 AAA87395 AAH02053 AAH24601 AAH12229 AAI67257 AAR96060
REF NP_001103095 NP_033927 XP_002715812 XP_002918295 XP_003990521 NP_001005903 NP_001080116 NP_001090922 NP_001106915 NP_001127638 NP_081101 XP_006516802 XP_006516803 XP_006516804 XP_006516805
SP B2GUZ5 P47753 P79136 Q5R507 Q5XI32 Q6EDY6
PDB
EMBL CAA71401 CAB06626 CAH93159 CAL69434
TPG DAA32069
AlphaFold Q6EDY6 B2GUZ5 P47753 Q5R507 P79136 Q5XI32

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks