BMRB Entry 17918

Name: Solution structure of the TbPIN1
Published: 2012-08-21

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PDB ID: 2lj4
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/BMR17918
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the TbPIN1

Deposition date:

2011-09-06

Original release date:

2012-08-21

Authors:

Sun, Lifang; Lin, Donghai; Zhao, Yufen

Citation:

Citation: Sun, Lifang; Wu, Xueji; Peng, Yu; Goh, Jian-Yuan; Liou, Yih-Cherng; Lin, Donghai; Zhao, Yufen. "Solution Structural Analysis of the Single-Domain Parvulin TbPin1" PLoS One 7, e43017-e43017 (2012).
PubMed: 22900083

Assembly members:

Assembly members:
Prolyl_Cis/trans_Isomerase_TbPIN1, polymer, 115 residues, 12515.130 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Prolyl_Cis/trans_Isomerase_TbPIN1: MSEKLRAAHLLVKFSGSRNP VSRRTGDSTADVTYEDAIKE LQKWSQRIASGEVSFEEAAS QRSDCGSYASGGDLGFFSSG EMMKPFEDAVRALKIGDISP IVQTDSGLHIIKRLA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	456
15N chemical shifts	122
1H chemical shifts	801

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TbPIN1	1

Entities:

Entity 1, TbPIN1 115 residues - 12515.130 Da.

1

MET

SER

GLU

LYS

LEU

ARG

ALA

HIS

LEU

2

LEU

VAL

LYS

PHE

SER

GLY

SER

ARG

ASN

PRO

3

VAL

SER

ARG

THR

GLY

ASP

SER

THR

ALA

4

ASP

VAL

THR

TYR

GLU

ASP

ALA

ILE

LYS

GLU

5

LEU

GLN

LYS

TRP

SER

GLN

ARG

ILE

ALA

SER

6

GLY

GLU

VAL

SER

PHE

GLU

ALA

SER

7

GLN

ARG

SER

ASP

CYS

GLY

SER

TYR

ALA

SER

8

GLY

ASP

LEU

GLY

PHE

SER

GLY

9

GLU

MET

LYS

PRO

PHE

GLU

ASP

ALA

VAL

10

ARG

ALA

LEU

LYS

ILE

GLY

ASP

ILE

SER

PRO

11

ILE

VAL

GLN

THR

ASP

SER

GLY

LEU

HIS

ILE

12

ILE

LYS

ARG

LEU

ALA

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

PDB	2LJ4
EMBL	CBH13077
GB	AAX69357 AAZ12840
REF	XP_011775354 XP_846906

BMRB Entry 17918

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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