BMRB Entry 28037

Name: 1H, 13C, 15N chemical shift assignments of FKBP12 protein from the pathogenic fungi Candida glabrata
Published: 2020-02-26

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28037

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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, 15N chemical shift assignments of FKBP12 protein from the pathogenic fungi Candida glabrata

Deposition date:

2019-11-05

Original release date:

2020-02-26

Authors:

Bashir, Qamar; LeMaster, David; Hernandez, Griselda

Citation:

Citation: Bashir, Qamar; LeMaster, David; Hernandez, Griselda. "1H, 13C, 15 N chemical shift assignments of the FKBP12 protein from the pathogenic fungi Candida auris and Candida glabrata" Biomol. NMR Assignments 14, 105-109 (2020).
PubMed: 31950462

Assembly members:

Assembly members:
FKBP12, polymer, 114 residues, 12156.89 Da.

Natural source:

Natural source: Common Name: budding yeasts Taxonomy ID: 5478 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Candida glabrata

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11-a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FKBP12: MSETIEGGVKIDRLSPGDGK TFPKQGDLVTIHYTGTLENG QKFDSSVDRGSPFQCNIGVG QVIKGWDAGIPKLSVGEKAR LTIPGPYAYGPRGFPGLIPP NATLIFDVELLKVN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	496
15N chemical shifts	111
1H chemical shifts	771

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FKBP12	1

Entities:

Entity 1, FKBP12 114 residues - 12156.89 Da.

FKBP12 from candida glabrata

1

MET

SER

GLU

THR

ILE

GLU

GLY

VAL

LYS

2

ILE

ASP

ARG

LEU

SER

PRO

GLY

ASP

GLY

LYS

3

THR

PHE

PRO

LYS

GLN

GLY

ASP

LEU

VAL

THR

4

ILE

HIS

TYR

THR

GLY

THR

LEU

GLU

ASN

GLY

5

GLN

LYS

PHE

ASP

SER

VAL

ASP

ARG

GLY

6

SER

PRO

PHE

GLN

CYS

ASN

ILE

GLY

VAL

GLY

7

GLN

VAL

ILE

LYS

GLY

TRP

ASP

ALA

GLY

ILE

8

PRO

LYS

LEU

SER

VAL

GLY

GLU

LYS

ALA

ARG

9

LEU

THR

ILE

PRO

GLY

PRO

TYR

ALA

TYR

GLY

10

PRO

ARG

GLY

PHE

PRO

GLY

LEU

ILE

PRO

11

ASN

ALA

THR

LEU

ILE

PHE

ASP

VAL

GLU

LEU

12

LEU

LYS

VAL

ASN

Samples:

sample_1: FKBP12, [U-99% 15N], 1 mM; DTT 2 mM; TCEP 2 mM; sodium phosphate 25 mM

sample_2: FKBP12, [U-99% 13C; U-99% 15N], 1 mM; DTT 2 mM; TCEP 2 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298.1 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298.1 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

Felix vND, Felix NMR - chemical shift assignment

TOPSPIN v3.2.7, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance III 600 MHz