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Biological Magnetic Resonance Data Bank


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BMRB Entry 17926

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17926
MolProbity Validation Chart

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Title: PARTIAL 3D STRUCTURE OF THE C-TERMINAL PART OF THE FREE ARAB THALIANA CP12-2 IN ITS OXIDIZED FORM   PubMed: 22514274

Deposition date: 2011-09-09 Original release date: 2012-04-23

Authors: Trivelli, X.; Sparla, F.; Marri, L.; Trost, P.

Citation: Fermani, Simona; Trivelli, Xavier; Sparla, Francesca; Thumiger, Anton; Calvaresi, Matteo; Marri, Lucia; Falini, Giuseppe; Zerbetto, Francesco; Trost, Paolo. "Conformational selection and folding-upon-binding of the intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly"  J. Biol. Chem. 287, 21372-21383 (2012).

Assembly members:
CP12_PROTEIN, polymer, 99 residues, 2637.736 Da.

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

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

Entity Sequences (FASTA):
CP12_PROTEIN: MGSSHHHHHHSSGLVPRGSH MAAPEGGISDVVEKSIKEAQ ETCAGDPVSGECVAAWDEVE ELSAAASHARDKKKADGSDP LEEYCKDNPETNECRTYDN

Data sets:
Data typeCount
13C chemical shifts187
15N chemical shifts53
1H chemical shifts278
heteronuclear NOE values19

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CP12 PROTEIN-LIKE PROTEIN1

Entities:

Entity 1, CP12 PROTEIN-LIKE PROTEIN 99 residues - 2637.736 Da.

Residues 1-21 (MGS...SHM) represent a non-native affinity tag. Numeration of the protein starts at AAPEGG...

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALAALAPROGLUGLYGLYILESERASP
4   VALVALGLULYSSERILELYSGLUALAGLN
5   GLUTHRCYSALAGLYASPPROVALSERGLY
6   GLUCYSVALALAALATRPASPGLUVALGLU
7   GLULEUSERALAALAALASERHISALAARG
8   ASPLYSLYSLYSALAASPGLYSERASPPRO
9   LEUGLUGLUTYRCYSLYSASPASNPROGLU
10   THRASNGLUCYSARGTHRTYRASPASN

Samples:

sample_1: CP12-2, [U-13C; U-15N], 1 mM; D2O, [U-2H], 5%; TSP 0.1-0.2 mM; H2O 95%; potassium phosphate 25 mM; sodium azide 0.05 w/v %

sample_2: CP12-2, [U-15N], 1 mM; D2O, [U-2H], 5%; TSP 0.1-0.2 mM; H2O 95%; potassium phosphate 25 mM; sodium azide 0.05 w/v %

sample_3: CP12-2 1 mM; D2O, [U-2H], 5%; TSP 0.1-0.2 mM; H2O 95%; potassium phosphate 25 mM; sodium azide 0.05 w/v %

sample_4: CP12-2 1 mM; D2O, [U-2H], 100%; TSP 0.1-0.2 mM; potassium phosphate 25 mM; sodium azide 0.05 w/v %

sample_5: CP12-2, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-2H], 100%; TSP 0.1-0.2 mM; potassium phosphate 25 mM; sodium azide 0.05 w/v %

sample_conditions_1: pH: 7; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_5isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1 15N TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
HETERONUCLEAR NOE 15Nsample_2isotropicsample_conditions_1
HBHANHsample_1isotropicsample_conditions_1

Software:

Procheck, LASKOWSKI, MACARTHUR, SMITH, JONES, HUTCHINSON, MORRIS, MOSS - refinement

CNSSOLVE v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

TOPSPIN v1.3, Bruker Biospin - collection

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

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

NMRView, Johnson, One Moon Scientific - data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

    Related Database Links:

    PDB
    EMBL CAB82955
    GB AAM20142 AAM45071 AAM63795 AEE80349 EFH52933
    REF NP_191800 XP_002876674
    SP Q9LZP9

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