+Open data
-Basic information
Entry | Database: PDB / ID: 2kni | ||||||
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Title | High-resolution solution structure of the ASIC1a blocker PcTX1 | ||||||
Components | Psalmotoxin-1 | ||||||
Keywords | TOXIN / Psalmotoxin 1 / pi-theraphotoxin-Pc1a / cystine knot / spider toxin / peptide toxin / Disulfide bond / Ionic channel inhibitor / Knottin / Neurotoxin / Secreted / ASIC1a inhibitor / acid sensing ion channel 1a inhibitor | ||||||
Function / homology | Laminin - #10 / Laminin / ion channel regulator activity / Other non-globular / Special / toxin activity / extracellular region / Psalmotoxin-1 Function and homology information | ||||||
Biological species | Psalmopoeus cambridgei (Trinidad chevron tarantula) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | Best MolProbity score, model 1 | ||||||
Authors | King, G.F. / Mobli, M. / Saez, N.J. | ||||||
Citation | Journal: Mol.Pharmacol. / Year: 2011 Title: A dynamic pharmacophore drives the interaction between Psalmotoxin-1 and the putative drug target acid-sensing ion channel 1a. Authors: Saez, N.J. / Mobli, M. / Bieri, M. / Chassagnon, I.R. / Malde, A.K. / Gamsjaeger, R. / Mark, A.E. / Gooley, P.R. / Rash, L.D. / King, G.F. #1: Journal: Protein Sci. / Year: 2003 Title: Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated cation channels. Authors: Escoubas, P. / Bernard, C. / Lambeau, G. / Lazdunski, M. / Darbon, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kni.cif.gz | 314 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kni.ent.gz | 264.6 KB | Display | PDB format |
PDBx/mmJSON format | 2kni.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2kni_validation.pdf.gz | 457.5 KB | Display | wwPDB validaton report |
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Full document | 2kni_full_validation.pdf.gz | 648.6 KB | Display | |
Data in XML | 2kni_validation.xml.gz | 35.9 KB | Display | |
Data in CIF | 2kni_validation.cif.gz | 37.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kn/2kni ftp://data.pdbj.org/pub/pdb/validation_reports/kn/2kni | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4792.591 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Psalmopoeus cambridgei (Trinidad chevron tarantula) Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P60514 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using a combination of NOESY-derived distance restraints, TALOS-derived dihedral-angle restraints, and hydrogen-bond restraints derived from a long-range HNCO ...Text: This structure was determined using a combination of NOESY-derived distance restraints, TALOS-derived dihedral-angle restraints, and hydrogen-bond restraints derived from a long-range HNCO experiment. The author shows the MolProbity statistics as follows. MOLPROBITY OUTPUT SCORES: AVERAGE ALL-ATOM CLASHSCORE 0.0, AVERAGE RAMACHANDRAN OUTLIERS 0.0%, AVERAGE RAMACHANDRAN FAVORED 83.9%, AVERAGE MOLPROBITY SCORE 1.68, AVERAGE MOLPROBITY PERCENTILE RANK 89.4 |
-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 10 / pH: 6 / Pressure: AMBIENT / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 900 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: best molprobity score | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: Best MolProbity score / Conformers calculated total number: 300 / Conformers submitted total number: 25 / Representative conformer: 1 |