BMRB Entry 19788

Name: Human FKBP52-FK506 binding domain 1
Published: 2014-08-06

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19788

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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:

Human FKBP52-FK506 binding domain 1

Deposition date:

2014-02-11

Original release date:

2014-08-06

Authors:

Mustafi, Sourajit; LeMaster, David; Hernandez, Griselda

Citation:

Citation: Mustafi, Sourajit; LeMaster, David; Hernandez, Griselda. "Differential Conformational Dynamics in the Closely Homologous FK506-binding Domains of FKBP51 and FKBP52" Biochem J. 461, 115-123 (2014).
PubMed: 24749623

Assembly members:

Assembly members:
FKBP52, polymer, 121 residues, 13387.38 Da.

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: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FKBP52: MEGVDISPKQDEGVLKVIKR EGTGTEMPMIGDRVFVHYTG WLLDGTKFDSSLDRKDKFSF DLGKGEVIKAWDIAIATMKV GEVCHITCKPEYAYGSAGSP PKIPPNATLVFEVELFEFKG E

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	341
15N chemical shifts	111
1H chemical shifts	111

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FKBP52	1

Entities:

Entity 1, FKBP52 121 residues - 13387.38 Da.

1

MET

GLU

GLY

VAL

ASP

ILE

SER

PRO

LYS

GLN

2

ASP

GLU

GLY

VAL

LEU

LYS

VAL

ILE

LYS

ARG

3

GLU

GLY

THR

GLY

THR

GLU

MET

PRO

MET

ILE

4

GLY

ASP

ARG

VAL

PHE

VAL

HIS

TYR

THR

GLY

5

TRP

LEU

ASP

GLY

THR

LYS

PHE

ASP

SER

6

SER

LEU

ASP

ARG

LYS

ASP

LYS

PHE

SER

PHE

7

ASP

LEU

GLY

LYS

GLY

GLU

VAL

ILE

LYS

ALA

8

TRP

ASP

ILE

ALA

ILE

ALA

THR

MET

LYS

VAL

9

GLY

GLU

VAL

CYS

HIS

ILE

THR

CYS

LYS

PRO

10

GLU

TYR

ALA

TYR

GLY

SER

ALA

GLY

SER

PRO

11

PRO

LYS

ILE

PRO

ASN

ALA

THR

LEU

VAL

12

PHE

GLU

VAL

GLU

LEU

PHE

GLU

PHE

LYS

GLY

13

GLU

Samples:

sample_1: FKBP52, [U-99% 13C; U-99% 15N], 1.0 mM; sodium phosphate 25 mM; DTT 2 mM; TCEP 2 mM; H2O 93%; D2O 7%

sample_2: FKBP52, [U-98% 15N], 1.0 mM; sodium phosphate 25 mM; DTT 2 mM; TCEP 2 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 25 mM; pH: 6.50; pressure: 1 atm; temperature: 298.15 K

sample_condition_2: ionic strength: 25 mM; pH: 6.50; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_condition_2
2D 1H-15N HSQC	sample_2	isotropic	sample_condition_2
2D 1H-15N HSQC	sample_2	isotropic	sample_condition_2
2D 1H-15N HSQC	sample_2	isotropic	sample_condition_2
2D 1H-15N HSQC	sample_2	isotropic	sample_condition_2
2D 1H-15N HSQC	sample_2	isotropic	sample_condition_2

Software:

Felix v2007, Accelrys Software Inc. - chemical shift assignment, peak picking, processing

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 600 MHz
Bruker Avance 700 MHz
Bruker Avance 600 MHz

PDB	4LAW 1N1A 4DRJ
EMBL	CAA34914
PIR	S14538