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- PDB-1n4i: Solution structure of spruce budworm antifreeze protein at 5 degr... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1n4i | ||||||
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Title | Solution structure of spruce budworm antifreeze protein at 5 degrees celsius | ||||||
![]() | thermal hysteresis protein | ||||||
![]() | ANTIFREEZE PROTEIN / BETA-HELIX / ICE / INSECT | ||||||
Function / homology | Choristoneura fumiferana antifreeze / Insect antifreeze protein superfamily / Choristoneura fumiferana antifreeze protein (CfAFP) / Insect antifreeze protein / UDP N-Acetylglucosamine Acyltransferase; domain 1 / 3 Solenoid / Mainly Beta / Thermal hysteresis protein![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Graether, S.P. / Gagne, S.M. / Spyracopoulos, L. / Jia, Z. / Davies, P.L. / Sykes, B.D. | ||||||
![]() | ![]() Title: Spruce Budworm Antifreeze Protein: Changes in Structure and Dynamics at Low Temperature Authors: Graether, S.P. / Gagne, S.M. / Spyracopoulos, L. / Jia, Z. / Davies, P.L. / Sykes, B.D. #1: ![]() Title: Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect Authors: Graether, S.P. / Kuiper, M.J. / Gagne, S.M. / Walkver, V.K. / Jia, Z. / Sykes, B.D. / Davies, P.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 596.7 KB | Display | ![]() |
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PDB format | ![]() | 514 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 9068.034 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Plasmid: pET21 / Production host: ![]() ![]() |
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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 standard 3D homonuclear techniques. |
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Sample preparation
Details | Contents: Uniform lableing with 13C, 15N / Solvent system: 90% H2O, 10% D20 |
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Sample conditions | Ionic strength: 0 / pH: 5.5 / Pressure: ambient / Temperature: 278 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 25 |