BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27313

Title: HusA from porphyromonas gingivalis   PubMed: 30291238

Deposition date: 2017-11-14 Original release date: 2018-10-02

Authors: Gell, David; Kwan, Ann

Citation: Gao, Jin-Long; Kwan, Ann; Yammine, Anthony; Zhou, Xiaoyan; Trewhella, Jill; Hugrass, Barbara; Collins, Daniel; Horne, James; Ye, Ping; Harty, Derek; Nguyen, Ky-Anh; Gell, David; Hunter, Neil. "Structural properties of a haemophore facilitate targeted elimination of the pathogen Porphyromonas gingivalis"  Nat. Commun. 9, 4097-4097 (2018).

Assembly members:
HusA, polymer, 201 residues, 21726.6 Da.

Natural source:   Common Name: Porphyromonas gingivalis   Taxonomy ID: 837   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Porphyromonas gingivalis

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

Entity Sequences (FASTA):
HusA: MGQGTAYAEVMNRKVAALDS VPPTEYATLAADFSRIAAVE GSDWMAAYYTAYCRIIPAFG NPSEADRLCEEAESMLSKAE SLGGDLSEIACLRSMAASAR LLVNPQERWQTYGAESSRQL AVALEANPANPRAYFLQAQS LLYTPAQFGGGKDKALPFAE KSVSCYAAATVSPAYAPHWG EQQARQLLMLCKAETQELVP R

Data sets:
Data typeCount
13C chemical shifts622
15N chemical shifts201
1H chemical shifts1333

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HusA trans-Pro2001
2HusA cis-Pro2001

Entities:

Entity 1, HusA trans-Pro200 201 residues - 21726.6 Da.

Residues 1, 2 are from the expression vector. Residues 3 to 196 correspond to UniProt: Q7MSY3, residues 24-217 Porphyromonas gingivalis gene PG_2227 Residues 197-201 are derived from the expression vector

1   METGLYGLNGLYTHRALATYRALAGLUVAL
2   METASNARGLYSVALALAALALEUASPSER
3   VALPROPROTHRGLUTYRALATHRLEUALA
4   ALAASPPHESERARGILEALAALAVALGLU
5   GLYSERASPTRPMETALAALATYRTYRTHR
6   ALATYRCYSARGILEILEPROALAPHEGLY
7   ASNPROSERGLUALAASPARGLEUCYSGLU
8   GLUALAGLUSERMETLEUSERLYSALAGLU
9   SERLEUGLYGLYASPLEUSERGLUILEALA
10   CYSLEUARGSERMETALAALASERALAARG
11   LEULEUVALASNPROGLNGLUARGTRPGLN
12   THRTYRGLYALAGLUSERSERARGGLNLEU
13   ALAVALALALEUGLUALAASNPROALAASN
14   PROARGALATYRPHELEUGLNALAGLNSER
15   LEULEUTYRTHRPROALAGLNPHEGLYGLY
16   GLYLYSASPLYSALALEUPROPHEALAGLU
17   LYSSERVALSERCYSTYRALAALAALATHR
18   VALSERPROALATYRALAPROHISTRPGLY
19   GLUGLNGLNALAARGGLNLEULEUMETLEU
20   CYSLYSALAGLUTHRGLNGLULEUVALPRO
21   ARG

Samples:

sample_1: HusA, [U-13C; U-15N], 0.9 mM; sodium phosphate 10 mM; DSS 20 uM

sample_2: HusA, [U-13C; U-15N], 0.9 mM; sodium phosphate 10 mM; DSS 20 uM

sample_3: HusA 0.9 mM; sodium phosphate 10 mM; DSS 20 uM

sample_4: HusA 0.9 mM; sodium phosphate 10 mM; DSS 20 uM

sample_conditions_1: ionic strength: 0.01 M; pH: 6.9; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.01 M; pH: 6.9; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBCBCGCDHDsample_1isotropicsample_conditions_1
3D HBCBCGCDHDCEHEsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_2
2D 1H-1H COSYsample_4isotropicsample_conditions_2
2D 1H-1H NOESYsample_4isotropicsample_conditions_2
2D 1H-1H NOESYsample_3isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D CCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2

Software:

TOPSPIN v3.1, Bruker Biospin - collection, processing

SPARKY v3.115, Goddard - chemical shift assignment

TALOS vTalos+, Cornilescu, Delaglio and Bax - chemical shift calculation

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH v2.45, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

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

Related Database Links:

NCBI PG_RS09910
GB AAQ67167.1

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