BMRB Entry 16260

Name: NMR assignments of FK506 binding domain from Plasmodium vivax
Published: 2009-10-16

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PDB ID: 2ki3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16260
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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:

NMR assignments of FK506 binding domain from Plasmodium vivax

Deposition date:

2009-04-19

Original release date:

2009-10-16

Authors:

Alag, Reema; Yoon, Ho Sup; Shin, Joon

Citation:

Citation: Alag, Reema; Shin, Joon; Yoon, Ho Sup. "NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax" Biomol. NMR Assignments 3, 243-245 (2009).
PubMed: 19774494

Assembly members:

Assembly members:
PvFKBD, polymer, 126 residues, 13971.799 Da.

Natural source:

Natural source: Common Name: malaria parasite Taxonomy ID: not available Superkingdom: Eukaryota Kingdom: Alveolata Genus/species: Plasmodium vivax

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PvFKBD: MEQETLEQVHLTEDGGVVKT ILRKGEGGEENAPKKGNEVT VHYVGKLESSGKVFDSSRER NVPFKFHLGQGEVIKGWDIC VASMTKNEKCSVRLDSKYGY GEEGCGESIPGNSVLIFEIE LISFRE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	497
15N chemical shifts	127
1H chemical shifts	850

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Domain	1

Entities:

Entity 1, Domain 126 residues - 13971.799 Da.

1

MET

GLU

GLN

GLU

THR

LEU

GLU

GLN

VAL

HIS

2

LEU

THR

GLU

ASP

GLY

VAL

LYS

THR

3

ILE

LEU

ARG

LYS

GLY

GLU

GLY

GLU

4

ASN

ALA

PRO

LYS

GLY

ASN

GLU

VAL

THR

5

VAL

HIS

TYR

VAL

GLY

LYS

LEU

GLU

SER

6

GLY

LYS

VAL

PHE

ASP

SER

ARG

GLU

ARG

7

ASN

VAL

PRO

PHE

LYS

PHE

HIS

LEU

GLY

GLN

8

GLY

GLU

VAL

ILE

LYS

GLY

TRP

ASP

ILE

CYS

9

VAL

ALA

SER

MET

THR

LYS

ASN

GLU

LYS

CYS

10

SER

VAL

ARG

LEU

ASP

SER

LYS

TYR

GLY

TYR

11

GLY

GLU

GLY

CYS

GLY

GLU

SER

ILE

PRO

12

GLY

ASN

SER

VAL

LEU

ILE

PHE

GLU

ILE

GLU

13

LEU

ILE

SER

PHE

ARG

GLU

Samples:

sample_1: PvFKBD, [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%; H2O 90%; D2O 10%

sample_2: PvFKBD, [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%; D2O 100%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 700 MHz

PDB	2KI3 3IHZ 3NI6 3PA7 4ITZ 4J4O 4MGV
GB	EDL44272 KMZ77558 KMZ84718 KMZ89996 KMZ96554
REF	XP_001613999