BMRB Entry 18504

Name: pfsub2 solution NMR structure
Published: 2012-10-01

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PDB ID: 2lu1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18504
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

pfsub2 solution NMR structure

Deposition date:

2012-06-06

Original release date:

2012-10-01

Authors:

HE, Yanan; CHEN, Yihong; RUAN, Biao; O'BROCHTA, David; BRYAN, Philip; ORBAN, John

Citation:

Citation: He, Yanan; Chen, Yihong; Oganesyan, Natalia; Ruan, Biao; Bryan, David; Orban, Philip. "Solution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum." Proteins 80, 2810-2817 (2012).
PubMed: 23011838

Assembly members:

Assembly members:
pfsub2, polymer, 149 residues, 10570.397 Da.

Natural source:

Natural source: Common Name: Malaria parasite P. falciparum Taxonomy ID: 5833 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium falciparum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pPal7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
pfsub2: TSNKKILLNVDKLVDQYLLN LKNNHTSKQELILVLKGELD LHSKNMKNVINNAKKNLEKY FKEHFKEFDKISYDISTPIN FLCIFIPTLFDMNNMDLLKQ ALLILHNDLHEYVENWSFSS TYHTYEADYIKEQDSVYDRS PKKKYIKAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	471
15N chemical shifts	118
1H chemical shifts	562

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	pfsub2	1

Entities:

Entity 1, pfsub2 149 residues - 10570.397 Da.

1

THR

SER

ASN

LYS

ILE

LEU

ASN

VAL

2

ASP

LYS

LEU

VAL

ASP

GLN

TYR

LEU

ASN

3

LEU

LYS

ASN

HIS

THR

SER

LYS

GLN

GLU

4

LEU

ILE

LEU

VAL

LEU

LYS

GLY

GLU

LEU

ASP

5

LEU

HIS

SER

LYS

ASN

MET

LYS

ASN

VAL

ILE

6

ASN

ALA

LYS

ASN

LEU

GLU

LYS

TYR

7

PHE

LYS

GLU

HIS

PHE

LYS

GLU

PHE

ASP

LYS

8

ILE

SER

TYR

ASP

ILE

SER

THR

PRO

ILE

ASN

9

PHE

LEU

CYS

ILE

PHE

ILE

PRO

THR

LEU

PHE

10

ASP

MET

ASN

MET

ASP

LEU

LYS

GLN

11

ALA

LEU

ILE

LEU

HIS

ASN

ASP

LEU

HIS

12

GLU

TYR

VAL

GLU

ASN

TRP

SER

PHE

SER

13

THR

TYR

HIS

THR

TYR

GLU

ALA

ASP

TYR

ILE

14

LYS

GLU

GLN

ASP

SER

VAL

TYR

ASP

ARG

SER

15

PRO

LYS

TYR

ILE

LYS

ALA

SER

Samples:

sample_1: pfsub2, [U-13C; U-15N], 0.3 – 0.4 mM; potassium phosphate 100 mM; sodium azide 10 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.21, Brunger A. T. et.al. - refinement

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2LU1
EMBL	CAB37326 CAB43592 CDO65172
GB	AAN35964 AAY33847 ETW15317 ETW30319 ETW35903
REF	XP_001348051 XP_012763770