BMRB Entry 19324

Name: Human FKBP12.6-Minor Form
Published: 2014-02-13

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19324

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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 FKBP12.6-Minor Form

Deposition date:

2013-06-26

Original release date:

2014-02-13

Authors:

Mustafi, Sourajit; Chen, Hui; Li, Hongmin; LeMaster, David; Hernandez, Griselda; Li, Zhong; Heroux, Annie

Citation:

Citation: Mustafi, Sourajit; Chen, Hui; Li, Hongmin; Lemaster, David; Hernandez, Griselda. "Analysing the visible conformational substates of the FK506-binding protein FKBP12." Biochem. J. 453, 371-380 (2013).
PubMed: 23688288

Assembly members:

Assembly members:
FKBP12.6, polymer, 107 residues, 11657.3 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):
FKBP12.6: GVEIETISPGDGRTFPKKGQ TCVVHYTGMLQNGKKFDSSR DRNKPFKFRIGKQEVIKGFE EGAAQMSLGQRAKLTCTPDV AYGATGHPGVIPPNATLIFD VELLNLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	307
15N chemical shifts	98
1H chemical shifts	217

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FKBP12.6	1

Entities:

Entity 1, FKBP12.6 107 residues - 11657.3 Da.

1

GLY

VAL

GLU

ILE

GLU

THR

ILE

SER

PRO

GLY

2

ASP

GLY

ARG

THR

PHE

PRO

LYS

GLY

GLN

3

THR

CYS

VAL

HIS

TYR

THR

GLY

MET

LEU

4

GLN

ASN

GLY

LYS

PHE

ASP

SER

ARG

5

ASP

ARG

ASN

LYS

PRO

PHE

LYS

PHE

ARG

ILE

6

GLY

LYS

GLN

GLU

VAL

ILE

LYS

GLY

PHE

GLU

7

GLU

GLY

ALA

GLN

MET

SER

LEU

GLY

GLN

8

ARG

ALA

LYS

LEU

THR

CYS

THR

PRO

ASP

VAL

9

ALA

TYR

GLY

ALA

THR

GLY

HIS

PRO

GLY

VAL

10

ILE

PRO

ASN

ALA

THR

LEU

ILE

PHE

ASP

11

VAL

GLU

LEU

ASN

LEU

GLU

Samples:

sample_1: FKBP12.6, [U-99% 13C; U-99% 15N], 1.5 mM; sodium phosphate 25 mM; DTT 2 mM; TCEP 2 mM; H2O 93%; D2O 7%

sample_2: FKBP12.6, [U-98% 15N], 1.5 mM; sodium phosphate 25 mM; DTT 2 mM; TCEP 2 mM; H2O, [U-98% 15N], 93%; D2O, [U-98% 15N], 7%

sample_conditions_1: ionic strength: 25 mM; pH: 7.00; pressure: 1 atm; temperature: 298.15 K

sample_condition_2: ionic strength: 25 mM; pH: 7.00; 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
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_condition_2
2D DQF-COSY	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 800 MHz

BMRB	16931 19240 19241 19323 19323
PDB	1C9H 3J8E 4C02 4IQ2 4IQC
DBJ	BAA07232 BAA13154 BAB23879 BAE44300 BAF93934
EMBL	CAH92123
GB	AAB30684 AAB30685 AAC37581 AAC64923 AAH02614
PRF	2201446A
REF	NP_001075614 NP_001091627 NP_001126241 NP_001253652 NP_004107
SP	P68106 P68107 P97534 Q8HYX6 Q9Z2I2
TPG	DAA24446
AlphaFold	P68106 P68107 P97534 Q8HYX6 Q9Z2I2