BMRB Entry 25902

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25902
MolProbity Validation Chart

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Title:
actinin-1 EF hand 3,4 Bound to Cav1.2 IQ Motif
Deposition date:
2015-11-17
Original release date:
2016-10-27
Authors:
Turner, Matthew; Ames, James
Citation:

Citation: Turner, Matthew; Anderson, David; Rajan, Sahana; Hell, Johannes; Ames, James. "Chemical shift assignments of the C-terminal EF-hand domain of alpha-actinin-1"  Biomol. NMR Assign. 10, 219-222 (2016).
PubMed: 26861220

Assembly members:

Assembly members:
actinin-1, polymer, 89 residues, Formula weight is not available
IQ-Motif, polymer, 25 residues, Formula weight is not available

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: pET15-b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
actinin-1: MGSSHHHHHSSGLVPRGSHM DTADQVMASFKILAGDKNYI TMDELRRELPPDQAEYCIAR MAPYTGPDSVPGALDYMSFS TALYGESDL
IQ-Motif: TVGKFYATFLIQEYFRKFKK RKEQG

Data sets:
Data typeCount
13C chemical shifts258
15N chemical shifts64
1H chemical shifts433

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1EF hand1
2Cav1.2IQMotif2

Entities:

Entity 1, EF hand 89 residues - Formula weight is not available

residues 824-892 of actinin-1 EF hand c-lobe. Contains a non native 6His tag at the c-terminus (MGSSHHHHHSSGLVPRGSHM)

1   METGLYSERSERHISHISHISHISHISSER
2   SERGLYLEUVALPROARGGLYSERHISMET
3   ASPTHRALAASPGLNVALMETALASERPHE
4   LYSILELEUALAGLYASPLYSASNTYRILE
5   THRMETASPGLULEUARGARGGLULEUPRO
6   PROASPGLNALAGLUTYRCYSILEALAARG
7   METALAPROTYRTHRGLYPROASPSERVAL
8   PROGLYALALEUASPTYRMETSERPHESER
9   THRALALEUTYRGLYGLUSERASPLEU

Entity 2, Cav1.2IQMotif 25 residues - Formula weight is not available

1   THRVALGLYLYSPHETYRALATHRPHELEU
2   ILEGLNGLUTYRPHEARGLYSPHELYSLYS
3   ARGLYSGLUGLNGLY

Samples:

sample_1: actinin-1 EF hand 3,4, [U-99% 15N], 0.5 mM; Cav1.2 IQ-Motif 0.5 mM; Tris 20 mM

sample_2: actinin-1 EF hand 3,4, [U-99% 13C; U-99% 15N], 0.5 mM; Cav1.2 IQ-Motif 0.5 mM; Tris 20 mM

sample_3: actinin-1 EF hand 3,4, [U-99% 13C; U-99% 15N], 0.5 mM; Cav1.2 IQ-Motif 0.5 mM; Tris 20 mM

sample_conditions_1: ionic strength: 0.020 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection

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

SPARKY v1.2, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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