+Open data
-Basic information
Entry | Database: PDB / ID: 2mz4 | ||||||
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Title | Solution Structure of mu-SLPTX-Ssm6a | ||||||
Components | Mu-scoloptoxin-Ssm6a | ||||||
Keywords | TOXIN / mu-SLPTX-Ssm6a / Gating modifier / Sodium 1.7 channel | ||||||
Function / homology | Diphtheria Toxin Repressor; domain 2 - #50 / Diphtheria Toxin Repressor; domain 2 / sodium channel regulator activity / toxin activity / Orthogonal Bundle / extracellular region / Mainly Alpha / Mu-scoloptoxin(03)-Ssm2a Function and homology information | ||||||
Biological species | Scolopendra mutilans (arthropod) | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
Authors | Kim, J.H. / Kim, J.I. | ||||||
Citation | Journal: To be Published Title: Solution Structure of mu-SLPTX-Ssm6a, a Gating Modifier of human Nav1.7 channels Authors: Kim, J.H. / Kim, J.I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mz4.cif.gz | 275.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mz4.ent.gz | 233 KB | Display | PDB format |
PDBx/mmJSON format | 2mz4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2mz4_validation.pdf.gz | 431.5 KB | Display | wwPDB validaton report |
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Full document | 2mz4_full_validation.pdf.gz | 592.6 KB | Display | |
Data in XML | 2mz4_validation.xml.gz | 27.6 KB | Display | |
Data in CIF | 2mz4_validation.cif.gz | 34.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mz/2mz4 ftp://data.pdbj.org/pub/pdb/validation_reports/mz/2mz4 | HTTPS FTP |
-Related structure data
Similar structure data | |
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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: 5333.003 Da / Num. of mol.: 1 / Fragment: UNP residues 66-111 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Scolopendra mutilans (arthropod) / Production host: Escherichia coli (E. coli) / References: UniProt: P0DL36 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.0 mM protein, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1.0 mM / Component: protein-1 |
Sample conditions | Ionic strength: 0 / pH: 3.7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software | Name: X-PLOR NIH / Developer: Schwieters, Kuszewski, Tjandra and Clore / Classification: refinement |
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Refinement | Method: distance geometry / Software ordinal: 1 |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |