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 15470

Title: Resonance assignment of the Calmodulin-Munc13-1 peptide complex   PubMed: 20013162

Authors: Rodriguez-Castaneda, Fernando; Carlomagno, Teresa; Brose, Nils; Griesinger, Christian

Citation: Rodriguez-Castaneda, Fernando; Coudevylle, Nicolas; Becker, Stefan; Brose, Nils; Carlomagno, Teresa; Griesinger, Christian. "(1)H, (13)C and (15)N resonance assignments of the Calmodulin-Munc13-1 peptide complex."  Biomol. NMR assignments 4, 45-48 (2009).

Assembly members:
calmodulin, polymer, 148 residues, 16700 Da.
Munc13-1_(458-492), polymer, 36 residues, 4170 Da.
CA, non-polymer, 40.078 Da.

Natural source:   Common Name: African clawed frog   Taxonomy ID: 8355   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Xenopus laevis

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

Entity Sequences (FASTA):
calmodulin: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREANIDGDGQVNYEE FVQMMTAK
Munc13-1_(458-492): GSRAKANWLRAFNKVRMQLQ EARGEGEMSKSLWFKG

Data sets:
Data typeCount
13C chemical shifts666
15N chemical shifts191
1H chemical shifts1105

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1calmodulin1
2Munc13-12
3Calcium I3
4Calcium II3
5Calcium III3
6Calcium IV3

Entities:

Entity 1, calmodulin 148 residues - 16700 Da.

1   ALAASPGLNLEUTHRGLUGLUGLNILEALA
2   GLUPHELYSGLUALAPHESERLEUPHEASP
3   LYSASPGLYASPGLYTHRILETHRTHRLYS
4   GLULEUGLYTHRVALMETARGSERLEUGLY
5   GLNASNPROTHRGLUALAGLULEUGLNASP
6   METILEASNGLUVALASPALAASPGLYASN
7   GLYTHRILEASPPHEPROGLUPHELEUTHR
8   METMETALAARGLYSMETLYSASPTHRASP
9   SERGLUGLUGLUILEARGGLUALAPHEARG
10   VALPHEASPLYSASPGLYASNGLYTYRILE
11   SERALAALAGLULEUARGHISVALMETTHR
12   ASNLEUGLYGLULYSLEUTHRASPGLUGLU
13   VALASPGLUMETILEARGGLUALAASNILE
14   ASPGLYASPGLYGLNVALASNTYRGLUGLU
15   PHEVALGLNMETMETTHRALALYS

Entity 2, Munc13-1 36 residues - 4170 Da.

1   GLYSERARGALALYSALAASNTRPLEUARG
2   ALAPHEASNLYSVALARGMETGLNLEUGLN
3   GLUALAARGGLYGLUGLYGLUMETSERLYS
4   SERLEUTRPPHELYSGLY

Entity 3, Calcium I - Ca - 40.078 Da.

1   CA

Samples:

13C15NCaM_Munc13-1: calmodulin, [U-13C; U-15N], 1.5 ± 0.2 mM; Munc13-1 1.8 ± 0.2 mM; Calcium chloride 10 ± 1 mM; Bis-Tris 20 ± 2 mM; Potassium chloride 150 ± 15 mM

13C15NMunc13-1_CaM: Munc13-1, [U-13C; U-15N], 0.5 ± 0.1 mM; calmodulin 0.6 ± 0.1 mM; Calcium chloride 10 ± 1 mM; Bis-Tris 20 ± 2 mM; potassium chloride 150 ± 15 mM

13C15NCaM_Munc13-1D2O: calmodulin, [U-13C; U-15N], 1.5 ± 0.2 mM; Munc13-1 1.8 ± 0.2 mM; Calcium chloride 10 ± 1 mM; Bis-Tris 20 ± 2 mM; Potassium chloride 150 ± 15 mM

15NCaM_Munc13-1Pf1: calmodulin, [U-15N], 1.5 ± 0.2 mM; Munc13-1 1.8 ± 0.2 mM; Calcium chloride 10 ± 1 mM; Bis-Tris 20 ± 2 mM; Potassium chloride 150 ± 15 mM; Bacteriophage Pf1 4.2 ± 0.4 mg

13C15NMunc13-1_CaMPf1: Munc13-1, [U-13C; U-15N], 0.5 ± 0.1 mM; calmodulin 0.6 ± 0.1 mM; Calcium chloride 10 ± 1 mM; Bis-Tris 20 ± 2 mM; Potassium chloride 150 ± 15 mM; Bacteriophage Pf1 4.2 ± 0.4 mg

single: ionic strength: 0.16 M; pH: 6.8; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC13C15NCaM_Munc13-1isotropicsingle
2D 1H-13C HSQC13C15NCaM_Munc13-1D2Oisotropicsingle
3D CBCA(CO)NH13C15NCaM_Munc13-1isotropicsingle
3D HNCACB13C15NCaM_Munc13-1isotropicsingle
3D HNCO13C15NCaM_Munc13-1isotropicsingle
3D HN(CA)CO13C15NCaM_Munc13-1isotropicsingle
3D 1H-15N NOESY13C15NCaM_Munc13-1isotropicsingle
3D 1H-13C NOESY13C15NCaM_Munc13-1D2Oisotropicsingle
3D H(CCO)NH13C15NCaM_Munc13-1isotropicsingle
3D C(CO)NH13C15NCaM_Munc13-1isotropicsingle
3D HCCH-TOCSY13C15NCaM_Munc13-1D2Oisotropicsingle
2D HBCBCaro13C15NCaM_Munc13-1D2Oisotropicsingle
3D HMBCMet13C15NCaM_Munc13-1D2Oisotropicsingle
2D 1H-15N HSQC13C15NMunc13-1_CaMisotropicsingle
2D 1H-13C HSQC13C15NMunc13-1_CaMisotropicsingle
3D CBCA(CO)NH13C15NMunc13-1_CaMisotropicsingle
3D C(CO)NH13C15NMunc13-1_CaMisotropicsingle
3D HNCO13C15NMunc13-1_CaMisotropicsingle
3D HNCACB13C15NMunc13-1_CaMisotropicsingle
3D H(CCO)NH13C15NMunc13-1_CaMisotropicsingle
3D HCCH-TOCSY13C15NMunc13-1_CaMisotropicsingle
3D 1H-15N NOESY13C15NMunc13-1_CaMisotropicsingle
3D 1H-13C NOESY13C15NMunc13-1_CaMisotropicsingle
3D HN(CA)CO13C15NMunc13-1_CaMisotropicsingle
2D HBCBCaro13C15NMunc13-1_CaMisotropicsingle
2D 1H-15N HSQC15NCaM_Munc13-1Pf1anisotropicsingle
2D 1H-15N HSQC13C15NMunc13-1_CaMPf1anisotropicsingle

Software:

xwinnmr v3.1, Bruker Biospin - collection, processing

FELIX v2004, Accelrys Software Inc. - processing

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

SPARKY v3.110, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker DRX 600 MHz
  • Bruker Avance 700 MHz
  • Bruker DMX 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 4056 4270 4284 5480 5770 6541 15184 15185 15186 15187 15188 15191 15624 15650 15852 1634 16418 16465 1648 16764 17264 17360 17771 17807 18027 18028 18556 19036 19238 19586 19604 25253 25257 26503 26626 26627 4056 4270 4284 4310
PDB
DBJ BAA08302 BAA11896 BAA19786 BAA19787 BAA19788 BAA82984 BAE27895 BAJ17676
EMBL CAA10601 CAA32050 CAA32062 CAA32119 CAA32120 Q62768
GB AAA35635 AAA35641 AAA37365 AAA40862 AAA40863 AAC52266 AAI72223 AAX09281 EDL28951 ELK19163
PIR JC1305 MCON
PRF 0409298A 0608335A
REF NP_001008160 NP_001009759 NP_001039714 NP_001040234 NP_001080864 NP_001025044 NP_001073890 NP_074052 XP_002688619 XP_002801170
SP O16305 P02594 P21251 P62144 P62145 Q4KUS2 Q62768 Q9UPW8
TPG DAA13808 DAA18029 DAA19590 DAA24777 DAA24988 DAA28231