BMRB Entry 6902

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

Data sets:
Data typeCount
15N chemical shifts119
1H chemical shifts868

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1hFKBP38D1

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   METARGGLUTRPLEUASPILELEUGLYASN
2   GLYLEULEUARGLYSLYSTHRLEUVALPRO
3   GLYPROPROGLYSERSERARGPROVALLYS
4   GLYGLNVALVALTHRVALHISLEUGLNTHR
5   SERLEUGLUASNGLYTHRARGVALGLNGLU
6   GLUPROGLULEUVALPHETHRLEUGLYASP
7   CYSASPVALILEGLNALALEUASPLEUSER
8   VALPROLEUMETASPVALGLYGLUTHRALA
9   METVALTHRALAASPSERLYSTYRCYSTYR
10   GLYPROGLNGLYARGSERPROTYRILEPRO
11   PROHISALAALALEUCYSLEUGLUVALTHR
12   LEULYSTHRALAVALASPGLYPROASPLEU
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:

NameSampleSample stateSample 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

Related Database Links:

BMRB 6923
PDB
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

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks