File:Allosteric-Regulation-of-Serine-Protease-HtrA2-through-Novel-Non-Canonical-Substrate-Binding-Pocket-pone.0055416.s006.ogv

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Allosteric-Regulation-of-Serine-Protease-HtrA2-through-Novel-Non-Canonical-Substrate-Binding-Pocket-pone.0055416.s006.ogv (Ogg multiplexed audio/video file, Theora/Vorbis, length 35 s, 640 × 480 pixels, 2.43 Mbps overall, file size: 10.26 MB)

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English: Orientation of active site triad and oxyanion hole formation during MD simulation of HtrA2-peptide complex. From this visual representation of HtrA2 peptide (GSAWFSF) complex during MD simulation it can be seen that the catalytic triad residues H65, D95, S173 reorient to form an active conformation along with oxyanion hole residues (N172, G171 and F170). All the residues involved are represented as sticks. This movie shows proper active site and oxyanion hole formation.
Date
Source Movie S1 from Bejugam P, Kuppili R, Singh N, Gadewal N, Chaganti L, Sastry G, Bose K (2013). "Allosteric Regulation of Serine Protease HtrA2 through Novel Non-Canonical Substrate Binding Pocket". PLOS ONE. DOI:10.1371/journal.pone.0055416. PMID 23388716.
Author Bejugam P, Kuppili R, Singh N, Gadewal N, Chaganti L, Sastry G, Bose K
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This file was published in a Public Library of Science journal. Their website states that the content of all PLOS journals is published under the Creative Commons Attribution 4.0 license (or its previous version depending on the publication date), unless indicated otherwise.
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Date/TimeThumbnailDimensionsUserComment
current11:22, 3 March 201335 s, 640 × 480 (10.26 MB)Open Access Media Importer Bot (talk | contribs)Automatically uploaded media file from Open Access source. Please report problems or suggestions here.

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Format Bitrate Download Status Encode time
VP9 480P 1.2 Mbps Completed 07:42, 17 August 2018 1 min 16 s
VP9 360P 599 kbps Completed 07:42, 17 August 2018 1 min 10 s
VP9 240P 304 kbps Completed 07:42, 17 August 2018 58 s
WebM 360P 503 kbps Completed 11:24, 3 March 2013 1 min 3 s
QuickTime 144p (MJPEG) 1.12 Mbps Completed 13:51, 15 October 2024 2.0 s

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