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Biological Magnetic Resonance Data Bank


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BMRB Entry 18896

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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/BMR18896
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Title: NMR STRUCTURE OF A BI-FUNCTIONAL LYSOZYME-PROTEASE INHIBITOR FROM THE DEFENSE GLAND OF COPTOTERMES FORMOSANUS SHIRAKI SOLDIERS

Deposition date: 2012-12-13 Original release date: 2013-11-26

Authors: Negulescu, H.; Guo, Y.; Garner, T.; Goodwin, O.; Henderson, G.; Laine, R.; Macnaughtan, M.

Citation: Negulescu, H.; Guo, Y.; Garner, T.; Goodwin, O.; Henderson, G.; Laine, R.; Macnaughtan, M.. "Bi-Functional Lysozyme-Protease Inhibitor Protein from the Defense Gland of Coptotermes Formosanus Shiraki Soldiers (Isoptera: Rhinotermitidae)"  To be Published ., .-..

Assembly members:
Lyso-Prot_Inhib, polymer, 75 residues, 8578.631 Da.

Natural source:   Common Name: Formosan subterranean termite   Taxonomy ID: 36987   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Coptotermes Formosanus

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

Entity Sequences (FASTA):
Lyso-Prot_Inhib: MAHHHHHHVDDDDKPEDCQL FCPMIYAPICATDGVSQRTF SNPCDLKVYNCWNPDNPYKE VKVGECDDANKPVPI

Data sets:
Data typeCount
13C chemical shifts199
15N chemical shifts57
1H chemical shifts281

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Lyso-Prot_Inhib1

Entities:

Entity 1, Lyso-Prot_Inhib 75 residues - 8578.631 Da.

1   METALAHISHISHISHISHISHISVALASP
2   ASPASPASPLYSPROGLUASPCYSGLNLEU
3   PHECYSPROMETILETYRALAPROILECYS
4   ALATHRASPGLYVALSERGLNARGTHRPHE
5   SERASNPROCYSASPLEULYSVALTYRASN
6   CYSTRPASNPROASPASNPROTYRLYSGLU
7   VALLYSVALGLYGLUCYSASPASPALAASN
8   LYSPROVALPROILE

Samples:

sample: Lyso-Prot_Inhib, [U-13C; U-15N], 1.0 mM; potassium phosphate 50 mM; sodium chloride 50 mM; D2O, [U-99% 2H], 10%; DSS 0.01%; H2O 90%

sample_conditions_1: ionic strength: 0.12 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions_1
2D 1H-13C HSQCsampleisotropicsample_conditions_1
2D 1H-1H NOESYsampleisotropicsample_conditions_1
2D 1H-1H TOCSYsampleisotropicsample_conditions_1
2D 1H-1H COSYsampleisotropicsample_conditions_1
3D 1H-15N NOESYsampleisotropicsample_conditions_1
3D 1H-15N TOCSYsampleisotropicsample_conditions_1
3D HNCACBsampleisotropicsample_conditions_1
3D HN(COCA)CBsampleisotropicsample_conditions_1
3D HNCOsampleisotropicsample_conditions_1
3D HCACOsampleisotropicsample_conditions_1
3D 1H-13C NOESYsampleisotropicsample_conditions_1
3D HCCH-TOCSYsampleisotropicsample_conditions_1
3D HNHBsampleisotropicsample_conditions_1

Software:

NMRPipe v7.8, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNMR v2.2.2, CCPN - chemical shift assignment, data analysis, peak picking

TALO+, Cornilescu, Delaglio and Bax - data analysis

PROSAII, Guntert - validation

Procheck v3.4.4, Laskowski and MacArthur, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - validation

MolProbity v3.19, Richardson - validation

VNMRJ, Varian - collection

PSVS v1.4, Bhattacharya and Montelione - validation

X-PLOR v2.31, Brunger, Schwieters, Kuszewski, Tjandra and Clore - data analysis, refinement, structure solution

NMR spectrometers:

  • Varian VS-700 700 MHz

Related Database Links:

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Download simulated HSQC data in one of the following formats:
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