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- PDB-1nar: CRYSTAL STRUCTURE OF NARBONIN REFINED AT 1.8 ANGSTROMS RESOLUTION -
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Open data
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Basic information
Entry | Database: PDB / ID: 1nar | ||||||
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Title | CRYSTAL STRUCTURE OF NARBONIN REFINED AT 1.8 ANGSTROMS RESOLUTION | ||||||
![]() | NARBONIN | ||||||
![]() | PLANT SEED PROTEIN | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Hennig, M. / Schlesier, B. / Wilson, K.S. | ||||||
![]() | ![]() Title: Crystal structure of narbonin at 1.8 A resolution. Authors: Hennig, M. / Pfeffer-Hennig, S. / Dauter, Z. / Wilson, K.S. / Schlesier, B. / Nong, V.H. #1: ![]() Title: A Tim Barrel Protein without Enzymatic Activity? Crystal Structure of Narbonin at 1.8 Angstroms Resolution Authors: Hennig, M. / Schlesier, B. / Dauter, Z. / Pfeffer, S. / Betzel, C. / Hoehne, W.E. / Wilson, K.S. #2: ![]() Title: Narbonin, a 2S Globulin from Vicia Narbonensis L. Crystallization and Preliminary Crystallographic Data Authors: Hennig, M. / Schlesier, B. / Pfeffer, S. / Hoehne, W.E. | ||||||
History |
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Remark 700 | SHEET THE SHEET PRESENTED AS *A* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. ...SHEET THE SHEET PRESENTED AS *A* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 82.4 KB | Display | ![]() |
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PDB format | ![]() | 61.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 417.7 KB | Display | ![]() |
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Full document | ![]() | 429 KB | Display | |
Data in XML | ![]() | 20 KB | Display | |
Data in CIF | ![]() | 30.6 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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Unit cell |
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Atom site foot note | 1: GLY 38 - PHE 39 OMEGA = 9.34 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: CIS PROLINE - PRO 139 3: TRP 261 - ASN 262 OMEGA = 12.67 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 33140.184 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Water | ChemComp-HOH / |
Sequence details | THE AMINO ACID SEQUENCE WAS DETERMINED BY INTERPRETATION OF THE ELECTRON DENSITY (REF. 1). FOR ...THE AMINO ACID SEQUENCE WAS DETERMINED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.48 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 9.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 10 Å / Num. obs: 27227 / % possible obs: 95.5 % / Num. measured all: 124224 / Rmerge(I) obs: 0.056 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 1.85 Å / Rmerge(I) obs: 0.078 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.8→10 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 10 Å / Num. reflection all: 27227 / σ(F): 0 / Rfactor all: 0.159 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 21 Å2 |