BMRB Entry 27033

Name: 1H, 13C and 15N Chemical Shift Assignments of cyclophilin 2 from Trichomonas vaginalis
Published: 2017-09-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27033

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H, 13C and 15N Chemical Shift Assignments of cyclophilin 2 from Trichomonas vaginalis

Deposition date:

2017-02-12

Original release date:

2017-09-15

Authors:

Martin, Tesmine; Lou, Yuan-Chao; Chen, Chinpan

Citation:

Citation: Martin, Tesmine; Lou, Yuan-Chao; Aryal, Sarita; Tai, Jung-Hsiang; Chen, Chinpan. "1H, 13C and 15N resonance assignments and secondary structures of cyclophilin 2 from Trichomonas vaginalis" Biomol. NMR Assignments 12, 27-30 (2018).
PubMed: 28875299

Assembly members:

Assembly members:
cyclophilin_2_from_Trichomonas_vaginalis, polymer, 194 residues, 20947 Da.

Natural source:

Natural source: Common Name: Trichomonas vaginalis Taxonomy ID: 5722 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trichomonas vaginalis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cyclophilin_2_from_Trichomonas_vaginalis: MLAFFATRVISAPKVTKKVF FKISINGEDAGTIKFGLFGD DVPKTAENFRALCTGEKGMG KLGKPLHYKGSPFHRVIPNF MIQGGDITSGNGYGGESIYG SKFADESFKITHDGPGLLSM ANSGPNTNGSQFFITTVPCP WLNGKHVVFGKVIEGMEIVK KIESLGSQSGTPKAKIIIAD CGEITELEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	750
15N chemical shifts	175
1H chemical shifts	1115

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TvCyP2 monomer	1

Entities:

Entity 1, TvCyP2 monomer 194 residues - 20947 Da.

1

MET

LEU

ALA

PHE

ALA

THR

ARG

VAL

ILE

2

SER

ALA

PRO

LYS

VAL

THR

LYS

VAL

PHE

3

PHE

LYS

ILE

SER

ILE

ASN

GLY

GLU

ASP

ALA

4

GLY

THR

ILE

LYS

PHE

GLY

LEU

PHE

GLY

ASP

5

ASP

VAL

PRO

LYS

THR

ALA

GLU

ASN

PHE

ARG

6

ALA

LEU

CYS

THR

GLY

GLU

LYS

GLY

MET

GLY

7

LYS

LEU

GLY

LYS

PRO

LEU

HIS

TYR

LYS

GLY

8

SER

PRO

PHE

HIS

ARG

VAL

ILE

PRO

ASN

PHE

9

MET

ILE

GLN

GLY

ASP

ILE

THR

SER

GLY

10

ASN

GLY

TYR

GLY

GLU

SER

ILE

TYR

GLY

11

SER

LYS

PHE

ALA

ASP

GLU

SER

PHE

LYS

ILE

12

THR

HIS

ASP

GLY

PRO

GLY

LEU

SER

MET

13

ALA

ASN

SER

GLY

PRO

ASN

THR

ASN

GLY

SER

14

GLN

PHE

ILE

THR

VAL

PRO

CYS

PRO

15

TRP

LEU

ASN

GLY

LYS

HIS

VAL

PHE

GLY

16

LYS

VAL

ILE

GLU

GLY

MET

GLU

ILE

VAL

LYS

17

LYS

ILE

GLU

SER

LEU

GLY

SER

GLN

SER

GLY

18

THR

PRO

LYS

ALA

LYS

ILE

ALA

ASP

19

CYS

GLY

GLU

ILE

THR

GLU

LEU

GLU

HIS

20

HIS

Samples:

sample_1: cyclophilin 2 from Trichomonas vaginalis, [U-100% 13C; U-100% 15N], 0.6 ± 0.01 mM

sample_conditions_1: ionic strength: 170 mM; pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

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 HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	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

Software:

TOPSPIN v3.1, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 600 MHz
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