BMRB Entry 16465

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16465
MolProbity Validation Chart

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Title:
CALMODULIN WRAPS AROUND ITS BINDING DOMAIN IN THE PLASMA MEMBRANE CA2+ PUMP ANCHORED BY A NOVEL 18-1 MOTIF
Deposition date:
2009-08-21
Original release date:
2009-08-24
Authors:
Juranic, Nenad; Atanasova, Macura; Filoteo, Adelaida; Macura, Slobodan; Prendergast, Franklyn; Penniston, John; Strehler, Emanuel
Citation:

Citation: Juranic, Nenad; Atanasova, Elena; Filoteo, Adelaida; Macura, Slobodan; Prendergast, Franklyn; Penniston, John; Strehler, Emanuel. "Calmodulin Wraps around Its Binding Domain in the Plasma Membrane Ca2+ Pump Anchored by a Novel 18-1 Motif."  J. Biol. Chem. 285, 4015-4024 (2010).
PubMed: 19996092

Assembly members:

Assembly members:
entity_1, polymer, 148 residues, 16721.465 Da.
entity_2, polymer, 28 residues, 3360.028 Da.
CA, non-polymer, 40.078 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
entity_2: LRRGQILWFRGLNRIQTQIK VVKAFHSS

Data sets:
Data typeCount
13C chemical shifts758
15N chemical shifts191
1H chemical shifts1228

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Calmodulin1
2helical peptide2
3CALCIUM ION_13
4CALCIUM ION_23
5CALCIUM ION_33
6CALCIUM ION_43

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, helical peptide 28 residues - 3360.028 Da.

1   LEUARGARGGLYGLNILELEUTRPPHEARG
2   GLYLEUASNARGILEGLNTHRGLNILELYS
3   VALVALLYSALAPHEHISSERSER

Entity 3, CALCIUM ION_1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 1 – 2 mM; entity_2, [U-99% 13C; U-99% 15N], 1 mM; H2O 95%; D2O 5%

sample_2: entity_1, [U-99% 13C; U-99% 15N], 1 – 2 mM; entity_2, [U-99% 13C; U-99% 15N], 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_1anisotropicsample_conditions_2
3D HNCOsample_2anisotropicsample_conditions_2
3D HNHAsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1

Software:

X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinenment

FELIX vFelix NMR 2007, Accelrys Software Inc. - peak picking, processing

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - geometry optimization, refinenment

PREDITOR, Berjanskii MV, Neal S, Wishart DS - data analysis, torsion angles prediction

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 15184 15185 15186 15187 15188 15191 15470 15624 15650 15852 1634 16418 1648 16764 17264 17360 17771 17807 18027 18028 18556 19036 19238 19586 19604 25253 25257 26503 26626 26627 4056 4270 4284 4310 4284
PDB
DBJ BAA08302 BAA11896 BAA19786 BAA19787 BAA19788 BAC27813 BAJ17688
EMBL CAA10601 CAA32050 CAA32062 CAA32119 CAA32120 CAD97686 CAH18241 CAL38204 CAL38232
GB AAA35635 AAA35641 AAA37365 AAA40862 AAA40863 AAA50819 AAB17578 AAF70246 AAX23599 AAZ73120
PIR JC1305 MCON
PRF 0409298A 0608335A
REF NP_001008160 NP_001009759 NP_001027633 NP_001039714 NP_001040234 NP_001028098 NP_001675 XP_001156333 XP_001488333 XP_002760713
SP O02367 O16305 O96081 P02594 P05932
TPG DAA13808 DAA18029 DAA19590 DAA24777 DAA24988 DAA21543
AlphaFold O02367 O16305 O96081 P02594 P05932

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