BMRB Entry 19782

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19782
MolProbity Validation Chart

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Title:
Chemical shifts assignments of the RodA hydrophobin from the opportunistic pathogen Aspergillus fumigatus
Deposition date:
2014-02-10
Original release date:
2019-03-18
Authors:
Pille, Ariane; Kwan, Ann H.; Cheung, Ivan; Hampsey, Matthew; Delepierre, Muriel; Sunde, Margaret; Guijarro, J. Inaki
Citation:

Citation: Pille, Ariane; Kwan, Ann H.; Cheung, Ivan; Hampsey, Matthew; Aimanianda, Vishukumar; Delepierre, Muriel; Latge, Jean-Paul; Sunde, Margaret; Guijarro, J. Inaki. "1H, 13C and 15N resonance assignments of the RodA hydrophobin from the opportunistic pathogen Aspergillus fumigatus"  Biomol. NMR Assignments ., .-..

Assembly members:

Assembly members:
RodA, polymer, 142 residues, 14426.43 Da.

Natural source:

Natural source:   Common Name: ascomycetes   Taxonomy ID: 746128   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Aspergillus fumigatus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHUE-RodA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RodA: SLPQHDVNAAGNGVGNKGNA NVRFPVPDDITVKQATEKCG DQAQLSCCNKATYAGDVTDI DEGILAGTLKNLIGGGSGTE GLGLFNQCSKLDLQIPVIGI PIQALVNQKCKQNIACCQNS PSDASGSLIGLGLPCIALGS IL

Data sets:
Data typeCount
13C chemical shifts566
15N chemical shifts153
1H chemical shifts948

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1RodA1

Entities:

Entity 1, RodA 142 residues - 14426.43 Da.

The recombinant protein consists of residues 19-159 of RodA and an additional N-terminal Ser residue. The 18 N-terminal residues coded by the RodA gene, which correspond to the secretion signal and are expected to be cleaved by A. fumigatus upon secretion, were not cloned.

1   SERLEUPROGLNHISASPVALASNALAALA
2   GLYASNGLYVALGLYASNLYSGLYASNALA
3   ASNVALARGPHEPROVALPROASPASPILE
4   THRVALLYSGLNALATHRGLULYSCYSGLY
5   ASPGLNALAGLNLEUSERCYSCYSASNLYS
6   ALATHRTYRALAGLYASPVALTHRASPILE
7   ASPGLUGLYILELEUALAGLYTHRLEULYS
8   ASNLEUILEGLYGLYGLYSERGLYTHRGLU
9   GLYLEUGLYLEUPHEASNGLNCYSSERLYS
10   LEUASPLEUGLNILEPROVALILEGLYILE
11   PROILEGLNALALEUVALASNGLNLYSCYS
12   LYSGLNASNILEALACYSCYSGLNASNSER
13   PROSERASPALASERGLYSERLEUILEGLY
14   LEUGLYLEUPROCYSILEALALEUGLYSER
15   ILELEU

Samples:

sample_1: RodA, [U-98% 13C; U-98% 15N], 360 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 4.3; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CC-TOCSY)NNHsample_1isotropicsample_conditions_1
3D C(CC-TOCSY)NNHsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

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

Analysis, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

  • Agilent Direct Drive 600 MHz

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