BMRB Entry 11507

Title:
Solution structure of IseA, an inhibitor protein of DL-endopeptidases from Bacillus subtilis
Deposition date:
2012-08-09
Original release date:
2012-10-29
Authors:
Arai, Ryoichi; Li, Hua; Tochio, Naoya; Fukui, Sadaharu; Kobayashi, Naoya; Kitaura, Chikashi; Watanabe, Satoru; Kigawa, Takanori; Sekiguchi, Junichi
Citation:

Citation: Arai, Ryoichi; Fukui, Sadaharu; Kobayashi, Naoya; Sekiguchi, Junichi. "Solution structure of IseA, an inhibitor protein of DL-endopeptidases from Bacillus subtilis, reveals a novel fold with a characteristic inhibitory loop"  J. Biol. Chem. ., .-. (2012).
PubMed: 23091053

Assembly members:

Assembly members:
IseA, polymer, 159 residues, 17728.545 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: pCR2.1

Data sets:
Data typeCount
13C chemical shifts716
15N chemical shifts163
1H chemical shifts1130

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1an inhibitor protein of DL-endopeptidases1

Entities:

Entity 1, an inhibitor protein of DL-endopeptidases 159 residues - 17728.545 Da.

The first residue G1 is a cloning artifact residue. In the sequence for the NMR experiment, the original residue numbers K24-I181 of Bacillus subtilis IseA without the signal peptide were renumbered K2-I159.

1   GLYLYSASNTHRSERGLYASPLEUSERGLN
2   LYSGLNALALEUGLNLEUALALEUSERALA
3   ARGGLUHISPHETRPASNTHRMETSERGLY
4   HISASNPROLYSVALLYSLYSALAVALCYS
5   PROSERGLYTHRPHEGLUTYRGLNASNLEU
6   GLNTYRVALTYRMETCYSSERASPLEUGLY
7   THRLYSALALYSALAVALASNTYRLEUTHR
8   PROILEPHETHRLYSTHRALAILEGLULYS
9   GLYPHELYSASPTYRHISPHETHRVALSER
10   LYSGLYLYSLEUALAVALPROILEGLYASP
11   GLYASPASNLEULEUASNTRPLYSLYSSER
12   THRALALYSLEUILESERLYSLYSGLYSER
13   THRILETHRTYRGLUPHETHRVALPROTHR
14   LEUASPGLYSERPROSERALALYSARGLYS
15   VALTHRPHEVALLYSGLUASNLYSLYSTRP
16   LYSVALASNGLNPHEASPALAVALILE

Samples:

sample_1: IseA, [U-13C; U-15N], 1.12 mM; TRIS, [U-2H], 20 mM; sodium chloride 300 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.3 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CCO)NHsample_1isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HC(C)H-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N IPAP HSQCsample_1isotropicsample_conditions_1
2D 1H-15N IPAP HSQCsample_1anisotropicsample_conditions_1

Software:

CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAI85525 BAM52492 BAM58068 GAK81498
EMBL CAB13721 CCU58457 CEI57032 CEJ77457 CJT21338
GB ADV92744 AEP91018 AFI28543 AFQ57773 AGA23038
REF NP_389720 WP_004399558 WP_014479968 WP_014664171 WP_015714038
SP O34841
AlphaFold O34841

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