BMRB Entry 6902

Name: Complete 1H and 15N assignment of the FK506-binding domain of human FKBP38
Published: 2006-04-24

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6902

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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:

Complete 1H and 15N assignment of the FK506-binding domain of human FKBP38

Deposition date:

2005-11-16

Original release date:

2006-04-24

Authors:

Maestre-Martinez, Mitcheell; Edlich, Frank; Jarczowski, Franziska; Weiwad, Matthias; Fischer, Gunter; Luecke, Christian

Citation:

Citation: Maestre-Martinez, Mitcheell; Edlich, Frank; Jarczowski, Franziska; Weiwad, Matthias; Fischer, Gunter; Luecke, Christian. "NMR Structure Note: Solution structure of the FK506-binding domain of human FKBP38" J. Biomol. NMR 34, 197-202 (2006).
PubMed: 16604427

Assembly members:

Assembly members:
hFKBP38D, polymer, 121 residues, 13056 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 Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hFKBP38D: MREWLDILGNGLLRKKTLVP GPPGSSRPVKGQVVTVHLQT SLENGTRVQEEPELVFTLGD CDVIQALDLSVPLMDVGETA MVTADSKYCYGPQGRSPYIP PHAALCLEVTLKTAVDGPDL E

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
15N chemical shifts	119
1H chemical shifts	868

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hFKBP38D	1

Entities:

Entity 1, hFKBP38D 121 residues - 13056 Da.

According to Swiss-Prot entry Q14318, the residue numbers have to be increased by 32 relative to the BMRB numbering

1

MET

ARG

GLU

TRP

LEU

ASP

ILE

LEU

GLY

ASN

2

GLY

LEU

ARG

LYS

THR

LEU

VAL

PRO

3

GLY

PRO

GLY

SER

ARG

PRO

VAL

LYS

4

GLY

GLN

VAL

THR

VAL

HIS

LEU

GLN

THR

5

SER

LEU

GLU

ASN

GLY

THR

ARG

VAL

GLN

GLU

6

GLU

PRO

GLU

LEU

VAL

PHE

THR

LEU

GLY

ASP

7

CYS

ASP

VAL

ILE

GLN

ALA

LEU

ASP

LEU

SER

8

VAL

PRO

LEU

MET

ASP

VAL

GLY

GLU

THR

ALA

9

MET

VAL

THR

ALA

ASP

SER

LYS

TYR

CYS

TYR

10

GLY

PRO

GLN

GLY

ARG

SER

PRO

TYR

ILE

PRO

11

PRO

HIS

ALA

LEU

CYS

LEU

GLU

VAL

THR

12

LEU

LYS

THR

ALA

VAL

ASP

GLY

PRO

ASP

LEU

13

GLU

Samples:

sample_1: hFKBP38D 1.3 ± 0.1 mM; sodium phosphate 20 ± 0.5 mM; sodium azide 0.05 ± 0.001 %

sample_2: hFKBP38D, [U-15N], 1.3 ± 0.1 mM; sodium phosphate 20 ± 0.5 mM; sodium azide 0.05 ± 0.001 %

conditions_1: pH: 6.7; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions

Software:

xwinnmr v3.5, Bruker - processing

AURELIA v2.5.9, Bruker - analysis

FELIX v2000, Accelrys - analysis

NMR spectrometers:

Bruker DRX 500 MHz
Bruker Avance 700 MHz

BMRB	6923
PDB	2AWG 2D9F 2F2D 2MF9 3EY6
DBJ	BAD96558 BAG36163 BAG72557 BAH13306
EMBL	CAD98028 CAL37783
GB	AAB00102 AAC28753 AAH09966 AAI22595 AAO39020
REF	NP_001247999 NP_001272500 NP_036313 XP_002761955 XP_002828980
SP	Q14318
AlphaFold	Q14318