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 16061

Title: Solution Structure of HybE from Escherichia coli   PubMed: 19636963

Deposition date: 2008-12-17 Original release date: 2009-04-14

Authors: Jin, Changwen; Shao, Xuan; Lu, Jie; Li, You

Citation: Shao, Xuan; Lu, Jie; Xia, Bin; Jin, Changwen. "1H, 13C and 15N resonance assignments of the chaperone HybE of hydrogenase-2 from Escherichia coli"  Biomol. NMR Assignments 3, 129-131 (2009).

Assembly members:
HybE, polymer, 162 residues, 17979.689 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
HybE: MTEEIAGFQTSPKAQVQAAF EEIARRSMHDLSFLHPSMPV YVSDFTLFEGQWTGCVITPW MLSAVIFPGPDQLWPLRKVS EKIGLQLPYGTMTFTVGELD GVSQYLSCSLMSPLSHSMSI EEGQRLTDDCARMILSLPVT NPDVPHAGRRALLFGRRSGE NA

Data sets:
Data typeCount
13C chemical shifts662
15N chemical shifts159
1H chemical shifts1069

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HybE1

Entities:

Entity 1, HybE 162 residues - 17979.689 Da.

1   METTHRGLUGLUILEALAGLYPHEGLNTHR
2   SERPROLYSALAGLNVALGLNALAALAPHE
3   GLUGLUILEALAARGARGSERMETHISASP
4   LEUSERPHELEUHISPROSERMETPROVAL
5   TYRVALSERASPPHETHRLEUPHEGLUGLY
6   GLNTRPTHRGLYCYSVALILETHRPROTRP
7   METLEUSERALAVALILEPHEPROGLYPRO
8   ASPGLNLEUTRPPROLEUARGLYSVALSER
9   GLULYSILEGLYLEUGLNLEUPROTYRGLY
10   THRMETTHRPHETHRVALGLYGLULEUASP
11   GLYVALSERGLNTYRLEUSERCYSSERLEU
12   METSERPROLEUSERHISSERMETSERILE
13   GLUGLUGLYGLNARGLEUTHRASPASPCYS
14   ALAARGMETILELEUSERLEUPROVALTHR
15   ASNPROASPVALPROHISALAGLYARGARG
16   ALALEULEUPHEGLYARGARGSERGLYGLU
17   ASNALA

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; NaCl 50 mM; PBS 50 mM

sample_2: entity, [U-99% 15N], 1 mM; NaCl 50 mM; PBS 50 mM

sample_conditions_1: ionic strength: 100 mM; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB37300 BAE77053 BAG78801 BAI27283 BAI32397
EMBL CAP77457 CAQ33334 CAQ90428 CAQ99956 CAR04606
GB AAA21593 AAA69159 AAC76028 AAG58129 AAN44517
REF NP_311904 NP_417466 NP_708810 WP_000133813 WP_000134002
SP P0AAN1 P0AAN2 Q8XBW0

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