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 19770

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19770

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Title: Backbone NMR Assignment of Humicola insolens cutinase   PubMed: 24832484

Deposition date: 2014-02-06 Original release date: 2021-12-07

Authors: Wimmer, Reinhard; Kold, David; Svendsen, Allan; Petersen, Evamaria

Citation: Kold, David; Dauter, Zbigniew; Laustsen, Anne; Brzozowski, Andrzej; Turkenburg, Johan; Nielsen, Anders; Koldsoe, Heidi; Petersen, Evamaria; Schioett, Birgit; De Maria, Leonardo; Wilson, Keith; Svendsen, Allan; Wimmer, Reinhard. "Thermodynamic and structural investigation of the specific SDS binding of Humicola insolens cutinase"  Protein Sci. 23, 1023-1035 (2014).

Assembly members:
cutinase, polymer, 194 residues, Formula weight is not available

Natural source:   Common Name: ascomycetes   Taxonomy ID: 34413   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Humicola insolens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: N/A

Entity Sequences (FASTA):
cutinase: XLGAIENGLESGSANACPDA ILIFARGSTEPGNMGITVGP ALANGLESHIRNIWIQGVGG PYDAALATNFLPRGTSQANI DEGKRLFALANQKCPNTPVV AGGYSQGAALIAAAVSELSG AVKEQVKGVALFGYTQNLQN RGGIPNYPRERTKVFCNVGD AVCTGTLIITPAHLSYTIEA RGEAARFLRDRIRA

Data sets:
Data typeCount
13C chemical shifts364
15N chemical shifts156
1H chemical shifts283

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cutinase1

Entities:

Entity 1, cutinase 194 residues - Formula weight is not available

Residue GLU 1 was converted into pyroglutamate when expressing the protein in minimal media in E.coli

1   PCALEUGLYALAILEGLUASNGLYLEUGLU
2   SERGLYSERALAASNALACYSPROASPALA
3   ILELEUILEPHEALAARGGLYSERTHRGLU
4   PROGLYASNMETGLYILETHRVALGLYPRO
5   ALALEUALAASNGLYLEUGLUSERHISILE
6   ARGASNILETRPILEGLNGLYVALGLYGLY
7   PROTYRASPALAALALEUALATHRASNPHE
8   LEUPROARGGLYTHRSERGLNALAASNILE
9   ASPGLUGLYLYSARGLEUPHEALALEUALA
10   ASNGLNLYSCYSPROASNTHRPROVALVAL
11   ALAGLYGLYTYRSERGLNGLYALAALALEU
12   ILEALAALAALAVALSERGLULEUSERGLY
13   ALAVALLYSGLUGLNVALLYSGLYVALALA
14   LEUPHEGLYTYRTHRGLNASNLEUGLNASN
15   ARGGLYGLYILEPROASNTYRPROARGGLU
16   ARGTHRLYSVALPHECYSASNVALGLYASP
17   ALAVALCYSTHRGLYTHRLEUILEILETHR
18   PROALAHISLEUSERTYRTHRILEGLUALA
19   ARGGLYGLUALAALAARGPHELEUARGASP
20   ARGILEARGALA

Samples:

sample_1: cutinase, [U-98% 13C; U-98% 15N], 0.3 ± 0.05 mM; potassium phosphate 20 mM; sodium azide 2 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298.1 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

CARA v1.5.5, Keller and Wuthrich - chemical shift assignment, processing

NMR spectrometers:

  • Bruker DRX 600 MHz

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