BMRB Entry 15038

Name: 1H, 13C, and 15N resonance assignments of FK506-binding domain of Plasmodium falciparum FKBP35
Published: 2007-06-27

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PDB ID: 2ofn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15038
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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, 13C, and 15N resonance assignments of FK506-binding domain of Plasmodium falciparum FKBP35

Deposition date:

2006-11-19

Original release date:

2007-06-27

Authors:

Kang, Congbao; Ye, Hong; Yoon, Hye Rim; Yoon, Ho Sup

Citation:

Citation: Kang, Cong Bao; Ye, Hong; Yoon, Hye Rim; Yoon, Ho Sup. "1H, 13C, and 15N resonance assignments of FK506-binding domain of Plasmodium falciparum FKBP35" Biomol. NMR Assignments 1, 27-28 (2007).
PubMed: 19636818

Assembly members:

Assembly members:
pfFKBP35FKBD, polymer, 135 residues, 14141 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: purified from the natural source Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
pfFKBP35FKBD: MTTEQEFEKVELTADGGVIK TILKKGDEGEENIPKKGNEV TVHYVGKLESTGKVFDSSFD RNVPFKFHLEQGEVIKGWDI CVSSMRKNEKCLVRIESMYG YGDEGCGESIPGNSVLLFEI ELLSFRELEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	514
15N chemical shifts	129
1H chemical shifts	883

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	pfFKBP35FKBD	1

Entities:

Entity 1, pfFKBP35FKBD 135 residues - 14141 Da.

1

MET

THR

GLU

GLN

GLU

PHE

GLU

LYS

VAL

2

GLU

LEU

THR

ALA

ASP

GLY

VAL

ILE

LYS

3

THR

ILE

LEU

LYS

GLY

ASP

GLU

GLY

GLU

4

GLU

ASN

ILE

PRO

LYS

GLY

ASN

GLU

VAL

5

THR

VAL

HIS

TYR

VAL

GLY

LYS

LEU

GLU

SER

6

THR

GLY

LYS

VAL

PHE

ASP

SER

PHE

ASP

7

ARG

ASN

VAL

PRO

PHE

LYS

PHE

HIS

LEU

GLU

8

GLN

GLY

GLU

VAL

ILE

LYS

GLY

TRP

ASP

ILE

9

CYS

VAL

SER

MET

ARG

LYS

ASN

GLU

LYS

10

CYS

LEU

VAL

ARG

ILE

GLU

SER

MET

TYR

GLY

11

TYR

GLY

ASP

GLU

GLY

CYS

GLY

GLU

SER

ILE

12

PRO

GLY

ASN

SER

VAL

LEU

PHE

GLU

ILE

13

GLU

LEU

SER

PHE

ARG

GLU

LEU

GLU

HIS

14

HIS

Samples:

sample_1: pfFKBP35FKBD, [U-13C; U-15N], 0.5 mM; Na-PO4 20 mM; NaCl 50 mM; DTT 1 mM; EDTA 0.1 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 20 mM; 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 HNCA	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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCC(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)CC(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
(H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

NMRPipe v2.3, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - processing

NMRView v5.2.2, B Johnson, One Moon Scientific - data analysis

NMR spectrometers:

Bruker Avance 600 MHz