BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19751

Title: Solution structure of ORF2   PubMed: 25784551

Deposition date: 2014-01-24 Original release date: 2015-03-23

Authors: Miyakawa, Takuya; Kobayashi, Hidetomo; Tashiro, Mitsuru; Yamanaka, Hiroyasu; Tanokura, Masaru

Citation: Kobayashi, Hidetomo; Yoshida, Toru; Miyakawa, Takuya; Tashiro, Mitsuru; Okamoto, Keinosuke; Yamanaka, Hiroyasu; Tanokura, Masaru; Tsuge, Hideaki. "Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria"  J. Biol. Chem. ., .-. (2015).

Assembly members:
entity, polymer, 133 residues, 13751.540 Da.

Natural source:   Common Name: g-proteobacteria   Taxonomy ID: 646   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Aeromonas sobria

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: GPVQESVTMDGKQYSTIEVN GQTYLIPDNGSKKRVARSLD SKVPQQTLRRGDVLMQGAAS PELTVSGTLLVEADDASAKA LATRHGLNFKQSSGGIALLE AKPGTDLNAIATKLKSEGVN VQIELSGAEQQPK

Data sets:
Data typeCount
13C chemical shifts416
15N chemical shifts119
1H chemical shifts794

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ORF21

Entities:

Entity 1, ORF2 133 residues - 13751.540 Da.

1   GLYPROVALGLNGLUSERVALTHRMETASP
2   GLYLYSGLNTYRSERTHRILEGLUVALASN
3   GLYGLNTHRTYRLEUILEPROASPASNGLY
4   SERLYSLYSARGVALALAARGSERLEUASP
5   SERLYSVALPROGLNGLNTHRLEUARGARG
6   GLYASPVALLEUMETGLNGLYALAALASER
7   PROGLULEUTHRVALSERGLYTHRLEULEU
8   VALGLUALAASPASPALASERALALYSALA
9   LEUALATHRARGHISGLYLEUASNPHELYS
10   GLNSERSERGLYGLYILEALALEULEUGLU
11   ALALYSPROGLYTHRASPLEUASNALAILE
12   ALATHRLYSLEULYSSERGLUGLYVALASN
13   VALGLNILEGLULEUSERGLYALAGLUGLN
14   GLNPROLYS

Samples:

sample_1: ORF2, [U-99% 13C; U-99% 15N], 0.9 mM; MOPS 18 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, peak picking, refinement, structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AEB49524 AHH32619 EKB12965 EKB17107 EKB21458
REF WP_005333882 WP_005352955 WP_005361466 WP_019445376 WP_021229060

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts