BMRB Entry 19904

Name: Solution structure of the PPIase domain of TbPar42
Published: 2015-04-13

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PDB ID: 2n87
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19904
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the PPIase domain of TbPar42

Deposition date: 2014-04-10 Original release date: 2015-04-13

Authors: Rehic, Edisa; Bayer, Peter

Citation: Rehic, Edisa; Hoenig, Dana; Rueppel, Alma; Matena, Anja; Bayer, Peter. "Solution structure of TbPar42" Not known ., .-..

Assembly members:
entity, polymer, 120 residues, 13522.351 Da.

Natural source: Common Name: Trypanosoma brucei Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei

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

Entity Sequences (FASTA):
entity: PTERHFYHVLVKHKDVRRPS SLAPRNKGEKITRSRADAIN LAQAILAQHKERKTWSLDEF VQVVRDFSECGSAKRDGDLG MVESGTYTEGFDTVAFSLKS GEVSAPVETELGVHLIYRVE

Data sets:

assigned_chemical_shifts
- TbPar42_Shifts

Data type	Count
13C chemical shifts	473
15N chemical shifts	122
1H chemical shifts	818

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PPIase domain of TbPar42	1

Entities:

Entity 1, PPIase domain of TbPar42 120 residues - 13522.351 Da.

1	PRO	THR	GLU	ARG	HIS	PHE	TYR	HIS	VAL	LEU
2	VAL	LYS	HIS	LYS	ASP	VAL	ARG	ARG	PRO	SER
3	SER	LEU	ALA	PRO	ARG	ASN	LYS	GLY	GLU	LYS
4	ILE	THR	ARG	SER	ARG	ALA	ASP	ALA	ILE	ASN
5	LEU	ALA	GLN	ALA	ILE	LEU	ALA	GLN	HIS	LYS
6	GLU	ARG	LYS	THR	TRP	SER	LEU	ASP	GLU	PHE
7	VAL	GLN	VAL	VAL	ARG	ASP	PHE	SER	GLU	CYS
8	GLY	SER	ALA	LYS	ARG	ASP	GLY	ASP	LEU	GLY
9	MET	VAL	GLU	SER	GLY	THR	TYR	THR	GLU	GLY
10	PHE	ASP	THR	VAL	ALA	PHE	SER	LEU	LYS	SER
11	GLY	GLU	VAL	SER	ALA	PRO	VAL	GLU	THR	GLU
12	LEU	GLY	VAL	HIS	LEU	ILE	TYR	ARG	VAL	GLU

Samples:

sample_1: PPIase domain of TbPar42500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; H2O 90%; D2O 10%

sample_2: PPIase domain of TbPar42500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; D20 99.9%

sample_3: PPIase domain of TbPar42, [U-100% 13C; U-100% 15N], 500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; H2O 90%; D2O 10%

sample_5: PPIase domain of TbPar42, [U-100% 15N], 500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; D20 100%

sample_4: PPIase domain of TbPar42, [U-100% 15N], 500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; H2O 90%; D20 10%

sample_6: PPIase domain of TbPar42, [U-100% 13C], 500 – 550 uM; potassium phosphate 50 mM; DSS 50 uM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.26; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HN(CA)CO	sample_3	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNHAHB	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_6	isotropic	sample_conditions_1
3D HCCH-COSY	sample_6	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_5	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPN, CCPN - chemical shift assignment, chemical shift calculation, data analysis, peak picking

TALOS, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance Ultrashield 700 MHz

PDB	2MNT
EMBL	CBH12319
GB	AAX69643 AAZ12312
REF	XP_011774600 XP_845871

Biological Magnetic Resonance Data Bank