BMRB Entry 12021

Name: 1H and 13C Assignments for PPTI (Pseudocerastes Persicus Trypsin Inhibitor)
Published: 2019-05-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR12021

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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:

1H and 13C Assignments for PPTI (Pseudocerastes Persicus Trypsin Inhibitor)

Deposition date:

2018-06-19

Original release date:

2019-05-09

Authors:

Amininasab, Mehriar; Banijamali, Seyede Elnaz

Citation:

Citation: Banijamali, Seyede Elnaz; Amininasab, Mehriar; Zaeifi, Davood. "Structural characterization of PPTI, a kunitz-type protein from the venom of Pseudocerastes persicus." PLoS ONE 14, e0214657-e0214657 (2019).
PubMed: 30973886

Assembly members:

Assembly members:
PPTI, polymer, 68 residues, 7642.7 Da.

Natural source:

Natural source: Common Name: Pseudocerastes persicus Taxonomy ID: 47769 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Pseudocerastes persicus

Experimental source:

Experimental source: Production method: purified from the natural source Host organism: Pseudocerastes persicus Vector: NA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PPTI: XDRPKFCYLPDDPGVCKAHI PRFYYNPASNKCKEFIYGGC GGNANNFETRAECRHTCVAS RKGGPRRP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	64
1H chemical shifts	407

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PPTI	1

Entities:

Entity 1, PPTI 68 residues - 7642.7 Da.

1

PCA

ASP

ARG

PRO

LYS

PHE

CYS

TYR

LEU

PRO

2

ASP

PRO

GLY

VAL

CYS

LYS

ALA

HIS

ILE

3

PRO

ARG

PHE

TYR

ASN

PRO

ALA

SER

ASN

4

LYS

CYS

LYS

GLU

PHE

ILE

TYR

GLY

CYS

5

GLY

ASN

ALA

ASN

PHE

GLU

THR

ARG

6

ALA

GLU

CYS

ARG

HIS

THR

CYS

VAL

ALA

SER

7

ARG

LYS

GLY

PRO

ARG

PRO

Samples:

sample_1: PPTI 2.0 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.0 M; pH: 4.0; pressure: 1 atm; temperature: 293.0 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DRX 500 MHz