BMRB Entry 27738

Name: 15N, 13C and 1H backbone resonance assignments of Human FKBP12 protein
Published: 2019-03-08

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27738

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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:

15N, 13C and 1H backbone resonance assignments of Human FKBP12 protein

Deposition date:

2018-12-20

Original release date:

2019-03-08

Authors:

Gobeil, Sophie; Bobay, Benjamin; Spicer, Leonard; Venters, Ronald

Citation:

Citation: Gobeil, Sophie; Bobay, Benjamin; Spicer, Leonard; Venters, Ronald. "15N, 13C and 1H resonance assignments of FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillus fumigatus" Biomol. NMR Assignments 13, 207-212 (2019).
PubMed: 30707421

Assembly members:

Assembly members:
FKBP12, polymer, 107 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FKBP12: GVQVETISPGDGRTFPKRGQ TCVVHYTGMLEDGKKFDSSR DRNKPFKFMLGKQEVIRGWE EGVAQMSVGQRAKLTISPDY AYGATGHPGIIPPHATLVFD VELLKLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	304
15N chemical shifts	99
1H chemical shifts	206

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 107 residues - Formula weight is not available

1

GLY

VAL

GLN

VAL

GLU

THR

ILE

SER

PRO

GLY

2

ASP

GLY

ARG

THR

PHE

PRO

LYS

ARG

GLY

GLN

3

THR

CYS

VAL

HIS

TYR

THR

GLY

MET

LEU

4

GLU

ASP

GLY

LYS

PHE

ASP

SER

ARG

5

ASP

ARG

ASN

LYS

PRO

PHE

LYS

PHE

MET

LEU

6

GLY

LYS

GLN

GLU

VAL

ILE

ARG

GLY

TRP

GLU

7

GLU

GLY

VAL

ALA

GLN

MET

SER

VAL

GLY

GLN

8

ARG

ALA

LYS

LEU

THR

ILE

SER

PRO

ASP

TYR

9

ALA

TYR

GLY

ALA

THR

GLY

HIS

PRO

GLY

ILE

10

ILE

PRO

HIS

ALA

THR

LEU

VAL

PHE

ASP

11

VAL

GLU

LEU

LYS

LEU

GLU

Samples:

sample_1: FKBP12, [U-98% 13C; U-98% 15N], 0.7 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1

Software:

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

Bruker Avance 600 MHz