BMRB Entry 28038

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

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28038

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, 13C, 15N chemical shift assignments of FKBP12 protein from the pathogenic fungi Candida auris PubMed: 31950462

Deposition date: 2019-11-05 Original release date: 2020-02-26

Authors: Bashir, Qamar; LeMaster, David; Hernandez, Griselda

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).

Assembly members:
FKBP12, polymer, 111 residues, 11807.46 Da.

Natural source: Common Name: budding yeasts Taxonomy ID: 498019 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Candida auris

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

Entity Sequences (FASTA):
FKBP12: MAPNTTEVEIISEGDGKVFP KVGDTVTIHYTGTLENGKKF DSSRDRGKPFQCTIGVGHVI KGWDIGIPKLSVGSQAKLTI PGHEAYGSRGFPGLIPPDAT LIFDVELLGVN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	491
15N chemical shifts	107
1H chemical shifts	756

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FKBP12	1

Entities:

Entity 1, FKBP12 111 residues - 11807.46 Da.

1

MET

ALA

PRO

ASN

THR

GLU

VAL

GLU

ILE

2

ILE

SER

GLU

GLY

ASP

GLY

LYS

VAL

PHE

PRO

3

LYS

VAL

GLY

ASP

THR

VAL

THR

ILE

HIS

TYR

4

THR

GLY

THR

LEU

GLU

ASN

GLY

LYS

PHE

5

ASP

SER

ARG

ASP

ARG

GLY

LYS

PRO

PHE

6

GLN

CYS

THR

ILE

GLY

VAL

GLY

HIS

VAL

ILE

7

LYS

GLY

TRP

ASP

ILE

GLY

ILE

PRO

LYS

LEU

8

SER

VAL

GLY

SER

GLN

ALA

LYS

LEU

THR

ILE

9

PRO

GLY

HIS

GLU

ALA

TYR

GLY

SER

ARG

GLY

10

PHE

PRO

GLY

LEU

ILE

PRO

ASP

ALA

THR

11

LEU

ILE

PHE

ASP

VAL

GLU

LEU

GLY

VAL

12

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
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	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(CA)CO	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

Software:

Felix vND, Felix NMR - chemical shift assignment

TOPSPIN v3.2.7, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance III 600 MHz

Biological Magnetic Resonance Data Bank