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Open data
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Basic information
Entry | Database: PDB / ID: 1nls | ||||||
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Title | CONCANAVALIN A AND ITS BOUND SOLVENT AT 0.94A RESOLUTION | ||||||
![]() | CONCANAVALIN A | ||||||
![]() | AGGLUTININ / CONCANAVALIN A / LECTIN | ||||||
Function / homology | ![]() regulation of defense response to virus / D-mannose binding / defense response / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Deacon, A.M. / Gleichmann, T. / Helliwell, J.R. / Kalb(Gilboa), A.J. | ||||||
![]() | Journal: J.Chem.Soc.,Faraday Trans. / Year: 1997 Title: The Structure of Concanavalin a and its Bound Solvent Determined with Small-Molecule Accuracy at 0.94 A Resolution Authors: Deacon, A. / Gleichmann, T. / Kalb(Gilboa), A.J. / Price, H. / Raftery, J. / Bradbrook, G. / Yariv, J. / Helliwell, J.R. #1: ![]() Title: Neutron Laue Diffraction Study of Concanavalin A. The Proton of Asp28 Authors: Habash, J. / Raftery, J. / Weisgerber, S. / Cassetta, A. / Lehmann, M.S. / Hoghoj, P. / Wilkinson, C. / Campbell, J.W. / Helliwell, J.R. #2: ![]() Title: High-Resolution Structures of Single-Metal-Substituted Concanavalin A: The Co,Ca-Protein at 1.6 A and the Ni,Ca-Protein at 2.0 A Authors: Emmerich, C. / Helliwell, J.R. / Redshaw, M. / Naismith, J.H. / Harrop, S.J. / Raftery, J. / Kalb(Gilboa), A.J. / Yariv, J. / Dauter, Z. / Wilson, K.S. #3: ![]() Title: High Resolution Crystallographic Studies of Native Concanavalin a Using Rapid Laue Data Collection Methods and the Introduction of a Monochromatic Large-Angle Oscillation Technique (Lot) Authors: Weisgerber, S. / Helliwell, J.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 117.1 KB | Display | ![]() |
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PDB format | ![]() | 90.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 415.3 KB | Display | ![]() |
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Full document | ![]() | 419 KB | Display | |
Data in XML | ![]() | 14.5 KB | Display | |
Data in CIF | ![]() | 22.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Details | CONCANAVALIN A EXISTS AS A TETRAMER, ALTHOUGH THE ASYMMETRIC UNIT CONTAINS A MONOMER. THE TETRAMER CAN BE GENERATED BY SYMMETRY OPERATORS. |
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Components
#1: Protein | Mass: 25622.385 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Chemical | ChemComp-MN / |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49 % |
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Crystal grow | pH: 6.8 / Details: pH 6.8 |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: CCD / Date: 1994 / Details: MIRROR + MONO POINT FOCUSSING |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Num. obs: 116923 / % possible obs: 75.4 % / Redundancy: 4.3 % / Rmerge(I) obs: 0.093 |
Reflection shell | Resolution: 0.94→1.01 Å / Rmerge(I) obs: 0.15 / % possible all: 30.4 |
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Processing
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Refinement | Resolution: 0.94→8 Å / Num. parameters: 19158 / Num. restraintsaints: 23649 Stereochemistry target values: 0.02A BOND LENGTH ESDS RESTRAINT Details: RESIDUE THR 120 IS POORLY DEFINED IN ELECTRON DENSITY. THE FOLLOWING RESIDUES HAVE SIDE CHAINS MODELLED WITH TWO CONFORMATIONS AND WERE REFINED WITH COMPLEMENTARY OCCUPANCIES: LEU 9, SER 21, ...Details: RESIDUE THR 120 IS POORLY DEFINED IN ELECTRON DENSITY. THE FOLLOWING RESIDUES HAVE SIDE CHAINS MODELLED WITH TWO CONFORMATIONS AND WERE REFINED WITH COMPLEMENTARY OCCUPANCIES: LEU 9, SER 21, ILE 25, ILE 27, LYS 39, MET 42, LYS 59, ARG 60, VAL 65, SER 72, ASP 78, LEU 107, SER 110, SER 113, ASN 124, SER 164, SER 185, VAL 188, GLU 192, THR 196, SER 204, SER 215, ASP 218, SER 220, SER 223. CIS PEPTIDES 1 AND 2 ARE DUE TO POORLY DEFINED ELECTRON DENSITY.
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Solvent computation | Solvent model: SHELXL SWAT | ||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.06 Å / Luzzati sigma a obs: 0.02 Å | ||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 0.94→8 Å
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