+Open data
-Basic information
Entry | Database: PDB / ID: 1hxl | ||||||
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Title | MINIPROTEIN MP-2 (V10A) COMPLEX WITH STREPTAVIDIN | ||||||
Components |
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Keywords | UNKNOWN FUNCTION / CONFORMATIONAL ENSEMBLE / MINI-PROTEINS / DISULPHIDE CONSTRAINED LOOPS / ENTROPICALLY RESTRAINED PROTEINS / PEPTIDES | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Streptomyces avidinii (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Yang, H.W. / Liu, D.Q. / Fan, X. / White, M.A. / Fox, R.O. | ||||||
Citation | Journal: To be Published Title: Conformational Ensemble Analysis of Ligand Binding in Streptavidin Mini-Protein Complexes Authors: Yang, H.W. / Liu, D.Q. / Fan, X. / White, M.A. / Fox, R.O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hxl.cif.gz | 57.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hxl.ent.gz | 46.1 KB | Display | PDB format |
PDBx/mmJSON format | 1hxl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1hxl_validation.pdf.gz | 455.1 KB | Display | wwPDB validaton report |
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Full document | 1hxl_full_validation.pdf.gz | 459.1 KB | Display | |
Data in XML | 1hxl_validation.xml.gz | 12.6 KB | Display | |
Data in CIF | 1hxl_validation.cif.gz | 16.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hx/1hxl ftp://data.pdbj.org/pub/pdb/validation_reports/hx/1hxl | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is a tetramer generated from the dimer in the asymmetric unit generated by the two fold axis -x,y,1/2-z |
-Components
#1: Protein | Mass: 13409.466 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces avidinii (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P22629 #2: Protein/peptide | Mass: 1625.917 Da / Num. of mol.: 2 / Mutation: V10A / Source method: obtained synthetically / Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 51.1 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.8 Details: 100 MM POTASSIUM ACETATE, AMMONIUM SULFATE, pH 4.80, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 108 K |
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Diffraction source | Source: ROTATING ANODE / Type: MACSCIENCE / Wavelength: 1.5418 |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: Jan 13, 1999 / Details: MULTILAYER |
Radiation | Monochromator: MULTILAYER OPTICS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. obs: 28454 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 7.86 % / Biso Wilson estimate: 10.9 Å2 / Rmerge(I) obs: 0.076 / Rsym value: 0.076 / Net I/σ(I): 11.7 |
Reflection shell | Resolution: 1.8→1.83 Å / Redundancy: 8.2 % / Rmerge(I) obs: 0.221 / Rsym value: 0.221 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: MP-2 STREPTAVIDIN COMPLEX Resolution: 1.8→41.29 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 745224.08 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 42.68 Å2 / ksol: 0.351 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.8→41.29 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.83 Å / Rfactor Rfree error: 0.023 / Total num. of bins used: 20
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Xplor file |
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