BMRB Entry 12014

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for cyclophilin 1 from Trichomonas vaginalis
Published: 2018-12-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR12014

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for cyclophilin 1 from Trichomonas vaginalis

Deposition date:

2017-11-22

Original release date:

2018-12-11

Authors:

Martin, Tesmine; Wei, Shu-Yi; Chen, Chinpan

Citation:

Citation: Martin, Tesmine; Lou, Yuan-Chao; Chou, Chun-Chi; Wei, Shu-Yi; Sadotra, Sushant; Cho, Chao-Cheng; Lin, Meng-Hsuan; Tai, Jung-Hsiang; Hsu, Chun-Hua; Chen, Chinpan. "Structural basis of interaction between dimeric cyclophilin 1 and Myb1 transcription factor in Trichomonas vaginalis." Sci. Rep. 8, 5410-5410 (2018).
PubMed: 29615721

Assembly members:

Assembly members:
TvCyP1, polymer, 175 residues, Formula weight is not available

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: pET 28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TvCyP1: GSMLKRPKTFFDISIRGDKV GKIVFELFNDIVPKTAENFR ALCTGEKGIGKSGMPLSYKG TMFHRIIPQFMIQGGDFTRF NGTGGESIYGMKFDDENFKV KHDKPGLLSMANAGPNTNGS QFFITTVETPWLDGHHCVFG QVIEGMDIVKQIESCGTESG RPRAMCMVTDCGEMK

Data sets:

assigned_chemical_shifts
- backbone_chem_shift_list_TvCyP1

Data type	Count
13C chemical shifts	289
15N chemical shifts	160
1H chemical shifts	160

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protomer 1	1
2	protomer 2	1

Entities:

Entity 1, protomer 1 175 residues - Formula weight is not available

1

GLY

SER

MET

LEU

LYS

ARG

PRO

LYS

THR

PHE

2

PHE

ASP

ILE

SER

ILE

ARG

GLY

ASP

LYS

VAL

3

GLY

LYS

ILE

VAL

PHE

GLU

LEU

PHE

ASN

ASP

4

ILE

VAL

PRO

LYS

THR

ALA

GLU

ASN

PHE

ARG

5

ALA

LEU

CYS

THR

GLY

GLU

LYS

GLY

ILE

GLY

6

LYS

SER

GLY

MET

PRO

LEU

SER

TYR

LYS

GLY

7

THR

MET

PHE

HIS

ARG

ILE

PRO

GLN

PHE

8

MET

ILE

GLN

GLY

ASP

PHE

THR

ARG

PHE

9

ASN

GLY

THR

GLY

GLU

SER

ILE

TYR

GLY

10

MET

LYS

PHE

ASP

GLU

ASN

PHE

LYS

VAL

11

LYS

HIS

ASP

LYS

PRO

GLY

LEU

SER

MET

12

ALA

ASN

ALA

GLY

PRO

ASN

THR

ASN

GLY

SER

13

GLN

PHE

ILE

THR

VAL

GLU

THR

PRO

14

TRP

LEU

ASP

GLY

HIS

CYS

VAL

PHE

GLY

15

GLN

VAL

ILE

GLU

GLY

MET

ASP

ILE

VAL

LYS

16

GLN

ILE

GLU

SER

CYS

GLY

THR

GLU

SER

GLY

17

ARG

PRO

ARG

ALA

MET

CYS

MET

VAL

THR

ASP

18

CYS

GLY

GLU

MET

LYS

Samples:

sample_1: TvCyP1, [U-13C; U-15N; U-2H], 0.5 mM; sodium chloride 50 mM; sodium azide 0.5 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: pH: 6.0; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

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