+Open data
-Basic information
Entry | Database: PDB / ID: 2jzm | ||||||
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Title | Chymotrypsin inhibitor C1 from Nicotiana alata | ||||||
Components | Proteinase inhibitor | ||||||
Keywords | HYDROLASE INHIBITOR / protein / proteinase inhibitor / chymotrypsin inhibitor / plant / insecticidal | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Nicotiana alata (Persian tobacco) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Model details | refined structure | ||||||
Authors | Schirra, H.J. / Anderson, M.A. / Craik, D.J. | ||||||
Citation | Journal: Protein Pept.Lett. / Year: 2008 Title: Structural refinement of insecticidal plant proteinase inhibitors from Nicotiana alata. Authors: Schirra, H.J. / Anderson, M.A. / Craik, D.J. #1: Journal: J.Mol.Biol. / Year: 1994 Title: The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata. Authors: Nielsen, K.J. / Heath, R.L. / Anderson, M.A. / Craik, D.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jzm.cif.gz | 294.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jzm.ent.gz | 255.5 KB | Display | PDB format |
PDBx/mmJSON format | 2jzm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jz/2jzm ftp://data.pdbj.org/pub/pdb/validation_reports/jz/2jzm | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 5746.476 Da / Num. of mol.: 1 / Fragment: residues 1-53 (UNP residues 54-106) / Source method: isolated from a natural source / Source: (natural) Nicotiana alata (Persian tobacco) / References: UniProt: Q9SQ77, UniProt: Q40378*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR / Details: refined structure | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample | Conc.: 1.2 mM / Component: C1 | |||||||||
Sample conditions | Ionic strength: 0 / Pressure: ambient / Temperature: 313 K |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 Details: MEthod followed the protocol of Linge et al., Proteins 50, 496 (2003) with the modifications in Nederveen et al., Proteins 59, 662 (2005), as above | ||||||||||||||||||||
NMR constraints | NOE constraints total: 538 / NOE intraresidue total count: 291 / NOE long range total count: 55 / NOE medium range total count: 22 / NOE sequential total count: 120 / Protein chi angle constraints total count: 18 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 26 / Protein psi angle constraints total count: 0 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0 Å / Torsion angle constraint violation method: cns_solve | ||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.013 Å / Distance rms dev error: 0.002 Å |