BMRB Entry 17926

Name: PARTIAL 3D STRUCTURE OF THE C-TERMINAL PART OF THE FREE ARAB THALIANA CP12-2 IN ITS OXIDIZED FORM
Published: 2012-04-23

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PDB ID: 2lj9
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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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

Deposition date:

2011-09-09

Original release date:

2012-04-23

Authors:

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

Citation:

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).
PubMed: 22514274

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a(+)

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1

Data type	Count
13C chemical shifts	187
15N chemical shifts	53
1H chemical shifts	278
heteronuclear NOE values	19

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CP12 PROTEIN-LIKE PROTEIN	1

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

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ALA

PRO

GLU

GLY

ILE

SER

ASP

4

VAL

GLU

LYS

SER

ILE

LYS

GLU

ALA

GLN

5

GLU

THR

CYS

ALA

GLY

ASP

PRO

VAL

SER

GLY

6

GLU

CYS

VAL

ALA

TRP

ASP

GLU

VAL

GLU

7

GLU

LEU

SER

ALA

SER

HIS

ALA

ARG

8

ASP

LYS

ALA

ASP

GLY

SER

ASP

PRO

9

LEU

GLU

TYR

CYS

LYS

ASP

ASN

PRO

GLU

10

THR

ASN

GLU

CYS

ARG

THR

TYR

ASP

ASN

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_5	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1 15N TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_4	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_4	isotropic	sample_conditions_1
HETERONUCLEAR NOE 15N	sample_2	isotropic	sample_conditions_1
HBHANH	sample_1	isotropic	sample_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

PDB	2LJ9 3QV1 3RVD
EMBL	CAB82955
GB	AAM20142 AAM45071 AAM63795 AEE80349 EFH52933
REF	NP_191800 XP_002876674
SP	Q9LZP9
AlphaFold	Q9LZP9