BMRB Entry 6189

Title:
Solution structure of SEP domain from human p47
Deposition date:
2004-04-22
Original release date:
2004-11-08
Authors:
Soukenik, M.; Leidert, M.; Sievert, V.; Buessow, K.; Leitner, D.; Labudde, D.; Ball, L.; Oschkinat, H.
Citation:

Citation: Soukenik, M.; Diehl, A.; Leidert, M.; Sievert, V.; Bussow, K.; Leitner, D.; Labudde, D.; Ball, L.; Lechner, A.; Nagler, D.; Oschkinat, H.. "The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L"  FEBS Lett. 576, 358-362 (2004).
PubMed: 15498563

Assembly members:

Assembly members:
NSFL1 cofactor p47, polymer, 102 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts609
13C chemical shifts311
15N chemical shifts106

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NSFL1 cofactor p471

Entities:

Entity 1, NSFL1 cofactor p47 102 residues - Formula weight is not available

1   GLYSERGLULYSARGGLNHISSERSERGLN
2   ASPVALHISVALVALLEULYSLEUTRPLYS
3   SERGLYPHESERLEUASPASNGLYGLULEU
4   ARGSERTYRGLNASPPROSERASNALAGLN
5   PHELEUGLUSERILEARGARGGLYGLUVAL
6   PROALAGLULEUARGARGLEUALAHISGLY
7   GLYGLNVALASNLEUASPMETGLUASPHIS
8   ARGASPGLUASPPHEVALLYSPROLYSGLY
9   ALAPHELYSALAPHETHRGLYGLUGLYGLN
10   LYSLEUGLYSERTHRALAPROGLNVALLEU
11   SERTHR

Samples:

sample_1: NSFL1 cofactor p47, [U-15N], 2 mM; phosphate buffer 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: NSFL1 cofactor p47, [U-15N; U-13C], 1 mM; phosphate buffer 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_3: NSFL1 cofactor p47, [U-15N; U-13C], 1 mM; phosphate buffer 20 mM; sodium chloride 100 mM; D2O 100%

sample_cond_1: pH: 5.6; temperature: 300 K; ionic strength: 120 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablesample_cond_1
3D 15N-separated NOESYnot availablenot availablesample_cond_1
3D 13C-separated NOESYnot availablenot availablesample_cond_1

Software:

XWINNMR v3.5, Bruker - processing

Paste-Papst v1.4, Labudde,D., Leitner,D. - collection

Platon v2.0, Labudde,D., Leitner,D. -

Sparky v3.1 - data analysis

Aria-CNS v1.2, Nilges. M. - structure solution, refinement

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAA91731 BAD97054 BAD97061 BAE88340 BAG37821
EMBL CAH90897
GB AAD44488 AAH02801 AAP97139 ABM84115 ABM87512
REF NP_001125510 NP_001193665 NP_001253592 NP_057227 NP_061327
SP Q5RBG3 Q9UNZ2
AlphaFold Q5RBG3 Q9UNZ2

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