BMRB Entry 19787

Name: Human FKBP51-FK506 binding domain 1
Published: 2014-08-06

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19787

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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 FKBP51-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:
FKBP51, polymer, 122 residues, 13537.59 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):
FKBP51: MEQGEDITSKKDRGVLKIVK RVGNGEETPMIGDKVYVHYK GKLSNGKKFDSSHDRNEPFV FSLGKGQVIKAWDIGVATMK KGEICHLLCKPEYAYGSAGS LPKIPSNATLFFEIELLDFK GE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	351
15N chemical shifts	114
1H chemical shifts	250

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FKBP51	1

Entities:

Entity 1, FKBP51 122 residues - 13537.59 Da.

1

MET

GLU

GLN

GLY

GLU

ASP

ILE

THR

SER

LYS

2

LYS

ASP

ARG

GLY

VAL

LEU

LYS

ILE

VAL

LYS

3

ARG

VAL

GLY

ASN

GLY

GLU

THR

PRO

MET

4

ILE

GLY

ASP

LYS

VAL

TYR

VAL

HIS

TYR

LYS

5

GLY

LYS

LEU

SER

ASN

GLY

LYS

PHE

ASP

6

SER

HIS

ASP

ARG

ASN

GLU

PRO

PHE

VAL

7

PHE

SER

LEU

GLY

LYS

GLY

GLN

VAL

ILE

LYS

8

ALA

TRP

ASP

ILE

GLY

VAL

ALA

THR

MET

LYS

9

LYS

GLY

GLU

ILE

CYS

HIS

LEU

CYS

LYS

10

PRO

GLU

TYR

ALA

TYR

GLY

SER

ALA

GLY

SER

11

LEU

PRO

LYS

ILE

PRO

SER

ASN

ALA

THR

LEU

12

PHE

GLU

ILE

GLU

LEU

ASP

PHE

LYS

13

GLY

GLU

Samples:

sample_1: FKBP51, [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: FKBP51, [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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	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

Software:

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 900 MHz
Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	3O5P 3O5E 3O5F 3O5G 3O5I 3O5J 3O5K 3O5L 3O5M 3O5O 3O5P 3O5Q 3O5R 4DRH 4DRI 4DRK 4DRM 4DRN 4DRO 4DRP 4DRQ 4JFI 4JFJ 4JFK 4JFL 4JFM 4R0X 4TW6 4TW7 4TX0 4W9O 4W9P 4W9Q 5DIT
DBJ	BAD93130
GB	AAI18470
REF	NP_001139249 XP_003897552 XP_012387759 XP_013833287 XP_013833288