BMRB Entry 4078

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4078

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, 15N and 13C Resonance Assignments and Secondary Structure of Group II Phospholipase A2 from Agkistrodon piscivorus piscivorus: Presence of an Amino-Terminal Helix in Solution

Deposition date:

1997-12-07

Original release date:

2001-02-16

Authors:

Jerala, Roman; Almeida, Paulo; Ye, Qiang; Biltonen, Rodney; Rule, Gordon

Citation:

Citation: Jerala, Roman; Almeida, Paulo; Ye, Qiang; Biltonen, Rodney; Rule, Gordon. "1H, 15N and 13C Resonance Assignments and Secondary Structure of Group II Phospholipase A2 from Agkistrodon piscivorus piscivorus: Presence of an Amino-Terminal Helix in Solution" J. Biomol. NMR 7, 107-120 (1996).

Assembly members:

Assembly members:
phospholipase A2, polymer, 123 residues, 14000 Da.

Natural source:

Natural source: Common Name: eastern cottonmouth Taxonomy ID: 8715 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Agkistrodon piscivorus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
phospholipase A2: SLFQFEKLIKKMTGKSGMLW YSAYGCYCGWGGQGRPKDAT DRCCFVHDCCYGKVTGCNPK MDIYTYSVENGNIVCGGTNP CKKQICECDRAAAICFRDNL KTYDSKTYWKYPKKNCKEES EPC

Data sets:

assigned_chemical_shifts
- chemical_shift_assignment

Data type	Count
1H chemical shifts	735
13C chemical shifts	462
15N chemical shifts	129

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	App-D49 PLA2	1

Entities:

Entity 1, App-D49 PLA2 123 residues - 14000 Da.

1

SER

LEU

PHE

GLN

PHE

GLU

LYS

LEU

ILE

LYS

2

LYS

MET

THR

GLY

LYS

SER

GLY

MET

LEU

TRP

3

TYR

SER

ALA

TYR

GLY

CYS

TYR

CYS

GLY

TRP

4

GLY

GLN

GLY

ARG

PRO

LYS

ASP

ALA

THR

5

ASP

ARG

CYS

PHE

VAL

HIS

ASP

CYS

6

TYR

GLY

LYS

VAL

THR

GLY

CYS

ASN

PRO

LYS

7

MET

ASP

ILE

TYR

THR

TYR

SER

VAL

GLU

ASN

8

GLY

ASN

ILE

VAL

CYS

GLY

THR

ASN

PRO

9

CYS

LYS

GLN

ILE

CYS

GLU

CYS

ASP

ARG

10

ALA

ILE

CYS

PHE

ARG

ASP

ASN

LEU

11

LYS

THR

TYR

ASP

SER

LYS

THR

TYR

TRP

LYS

12

TYR

PRO

LYS

ASN

CYS

LYS

GLU

SER

13

GLU

PRO

CYS

Samples:

sample_one: phospholipase A2, [U-15N], 0.2 mM; sodium phosphate 20 mM; KCL 100 mM; D2O 5%; H2O 95%

sample_two: phospholipase A2, [U-13C; U-15N], 0.2 mM; sodium phosphate 20 mM; KCL 100 mM; D2O 5%; H2O 95%

sample_conditions: pH: 4.3; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
not available	not available	not available	sample_conditions

Software:

No software information available

NMR spectrometers:

Varian UnityPlus 500 MHz

PDB	1VAP
GB	AAB25792 AAB26655
SP	P51972
AlphaFold	P51972