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Biological Magnetic Resonance Data Bank


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BMRB Entry 19036

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19036
MolProbity Validation Chart

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Title: NMR structure of the complex of an N-terminally acetylated alpha-synuclein peptide with calmodulin   PubMed: 23607618

Deposition date: 2013-02-13 Original release date: 2013-05-06

Authors: Gruschus, James; Yap, Thai Leong; Pistolesi, Sara; Maltsev, Alexander; Lee, Jennifer

Citation: Gruschus, James; Yap, Thai Leong; Pistolesi, Sara; Maltsev, Alexander; Lee, Jennifer. "NMR Structure of Calmodulin Complexed to an N-Terminally Acetylated -Synuclein Peptide."  Biochemistry 52, 3436-3445 (2013).

Assembly members:
calmodulin, polymer, 148 residues, 16721.465 Da.
peptide, polymer, 20 residues, 1953.383 Da.
ACETYL GROUP, non-polymer, 44.053 Da.
CALCIUM ION, non-polymer, 40.078 Da.

Natural source:   Common Name: Humans   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
calmodulin: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
peptide: MDVFMKGLSKAKEGVVAAAX

Data sets:
Data typeCount
13C chemical shifts308
15N chemical shifts157
1H chemical shifts341

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1calmodulin1
2peptide2
3ACETYL GROUP3
4CALCIUM ION_14
5CALCIUM ION_24
6CALCIUM ION_34
7CALCIUM ION_44

Entities:

Entity 1, calmodulin 148 residues - 16721.465 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   VALASPGLUMETILEARGGLUALAASPILE
14   ASPGLYASPGLYGLNVALASNTYRGLUGLU
15   PHEVALGLNMETMETTHRALALYS

Entity 2, peptide 20 residues - 1953.383 Da.

1   METASPVALPHEMETLYSGLYLEUSERLYS
2   ALALYSGLUGLYVALVALALAALAALANH2

Entity 3, ACETYL GROUP - C2 H4 O - 44.053 Da.

1   ACE

Entity 4, CALCIUM ION_1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: calmodulin, [U-99% 13C; U-99% 15N], 600 uM; peptide 600 uM; MES 50 mM; potassium chloride 100 mM; CALCIUM ION 3 mM; H2O 95%; D2O 5%

sample_2: peptide, [U-13C; U-15N]-Met,Val,Phe,Gly,Leu,Ala, 700 uM; calmodulin 700 uM; MES 50 mM; potassium chloride 100 mM; CALCIUM ION 3 mM; sodium azide .1%; H2O 95%; D2O 5%

sample_3: calmodulin, [U-99% 13C; U-99% 15N], 150 uM; peptide 150 uM; MES 50 mM; potassium chloride 100 mM; CALCIUM ION 3 mM; Pf1 phage 10 mg/mL; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.36; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3anisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3anisotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15184 15185 15186 15187 15188 15191 15470 15624 15650 15852 1634 16418 16465 1648 16764 17264 17360 17771 17807 18027 18028 18556 19238 19586 19604 25253 25257 26503 26626 26627 4056 4270 4284 4310 16300 16302 16342 16543 16546 16547 16548 16904 17214 17498 17665 18232 18857 18860 19257 19337 19338 19344 19345 19346 19347 19348 19349 19350 19351 5744 6968
PDB
DBJ BAA08302 BAA11896 BAA19786 BAA19787 BAA19788 BAA06625 BAB29375 BAE33670 BAF82858 BAG73790
EMBL CAA10601 CAA32050 CAA32062 CAA32119 CAA32120 CAG33339 CAG46454
GB AAA35635 AAA35641 AAA37365 AAA40862 AAA40863 AAA16117 AAA93538 AAA98487 AAA98493 AAB20688
PIR JC1305 MCON
PRF 0409298A 0608335A
REF NP_001008160 NP_001009759 NP_001027633 NP_001039714 NP_001040234 NP_000336 NP_001009158 NP_001029213 NP_001032222 NP_001035916
SP O02367 O16305 O96081 P02594 P05932 O55042 P37377 P37840 P61138 P61139
TPG DAA13808 DAA18029 DAA19590 DAA24777 DAA24988 DAA28796

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts