5fwi - Revision history

OCA at 13:29, 26 July 2023

OCA — Wed, 26 Jul 2023 13:29:33 GMT

←Older revision		Revision as of 13:29, 26 July 2023
Line 3:		Line 3:
	<StructureSection load='5fwi' size='340' side='right'caption='[[5fwi]], [[Resolution\|resolution]] 3.40Å' scene=''>		<StructureSection load='5fwi' size='340' side='right'caption='[[5fwi]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fwi]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWI OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5FWI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fwi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FWI FirstGlance]. <br>
-	</td></tr><tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"~~><span class~~=~~'plainlinks'~~>[~~http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1~~]~~, with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=~~3.4~~.19.12 3.4.19.12] </span>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 3.4Å</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5fwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwi OCA], [~~http~~://pdbe.org/5fwi PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5fwi RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5fwi PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5fwi ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwi OCA], [https://pdbe.org/5fwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fwi RCSB], [https://www.ebi.ac.uk/pdbsum/5fwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fwi ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/UBP7_HUMAN UBP7_HUMAN]] Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked Ubiquitin chains.<ref>PMID:11923872</ref> <ref>PMID:14506283</ref> <ref>PMID:15053880</ref> <ref>PMID:16160161</ref> <ref>PMID:16964248</ref> <ref>PMID:18716620</ref> <ref>PMID:18590780</ref> <ref>PMID:20153724</ref> <ref>PMID:21745816</ref> <ref>PMID:22411829</ref> <ref>PMID:22689415</ref> <ref>PMID:22466611</ref> <ref>PMID:22466612</ref>	+	[https://www.uniprot.org/uniprot/UBP7_HUMAN UBP7_HUMAN] Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked Ubiquitin chains.<ref>PMID:11923872</ref> <ref>PMID:14506283</ref> <ref>PMID:15053880</ref> <ref>PMID:16160161</ref> <ref>PMID:16964248</ref> <ref>PMID:18716620</ref> <ref>PMID:18590780</ref> <ref>PMID:20153724</ref> <ref>PMID:21745816</ref> <ref>PMID:22411829</ref> <ref>PMID:22689415</ref> <ref>PMID:22466611</ref> <ref>PMID:22466612</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ubiquitinyl hydrolase 1]]~~	+	[[Category: Kim RQ]]
-	~~[[Category: Dijk, W J.van]]~~	+	[[Category: Sixma TK]]
-	[[Category: Kim~~, R Q~~]]	+	[[Category: Van Dijk WJ]]
-	[[Category: Sixma~~, T K~~]]	+
-	[[Category: ~~Deubiquitinase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Ubiquitin-like]]~~	+
-	~~[[Category: Usp~~]]	+

OCA at 07:40, 6 May 2020

OCA — Wed, 06 May 2020 07:40:27 GMT

←Older revision		Revision as of 07:40, 6 May 2020
Line 1:		Line 1:

	==structure of usp7 catalytic domain and three ubl-domains==		==structure of usp7 catalytic domain and three ubl-domains==
-	<StructureSection load='5fwi' size='340' side='right' caption='[[5fwi]], [[Resolution\|resolution]] 3.40Å' scene=''>	+	<StructureSection load='5fwi' size='340' side='right'caption='[[5fwi]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fwi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWI OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5FWI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fwi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FWI FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5fwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwi OCA], [http://pdbe.org/5fwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fwi RCSB], [http://www.ebi.ac.uk/pdbsum/5fwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fwi ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwi OCA], [http://pdbe.org/5fwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fwi RCSB], [http://www.ebi.ac.uk/pdbsum/5fwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fwi ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 5fwi" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5fwi" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thioesterase 3D structures\|Thioesterase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
	[[Category: Dijk, W J.van]]		[[Category: Dijk, W J.van]]

OCA at 17:29, 12 July 2016

OCA — Tue, 12 Jul 2016 17:29:42 GMT

←Older revision		Revision as of 17:29, 12 July 2016
Line 1:		Line 1:

-	==~~Not yet~~==	+	==structure of usp7 catalytic domain and three ubl-domains==
	<StructureSection load='5fwi' size='340' side='right' caption='[[5fwi]], [[Resolution\|resolution]] 3.40Å' scene=''>		<StructureSection load='5fwi' size='340' side='right' caption='[[5fwi]], [[Resolution\|resolution]] 3.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5fwi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FWI FirstGlance]. <br>		<table><tr><td colspan='2'>[[5fwi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FWI FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwi OCA], [http://pdbe.org/5fwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fwi RCSB], [http://www.ebi.ac.uk/pdbsum/5fwi PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwi OCA], [http://pdbe.org/5fwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fwi RCSB], [http://www.ebi.ac.uk/pdbsum/5fwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fwi ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
		+	[[Category: Dijk, W J.van]]
	[[Category: Kim, R Q]]		[[Category: Kim, R Q]]
	[[Category: Sixma, T K]]		[[Category: Sixma, T K]]
-	[[Category: VanDijk, W J]]
	[[Category: Deubiquitinase]]		[[Category: Deubiquitinase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Ubiquitin-like]]		[[Category: Ubiquitin-like]]
	[[Category: Usp]]		[[Category: Usp]]

OCA at 23:09, 23 June 2016

OCA — Thu, 23 Jun 2016 23:09:02 GMT

←Older revision		Revision as of 23:09, 23 June 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5fwi is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Not yet==
		+	<StructureSection load='5fwi' size='340' side='right' caption='[[5fwi]], [[Resolution\|resolution]] 3.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5fwi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FWI FirstGlance]. <br>
		+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwi OCA], [http://pdbe.org/5fwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fwi RCSB], [http://www.ebi.ac.uk/pdbsum/5fwi PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/UBP7_HUMAN UBP7_HUMAN]] Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked Ubiquitin chains.<ref>PMID:11923872</ref> <ref>PMID:14506283</ref> <ref>PMID:15053880</ref> <ref>PMID:16160161</ref> <ref>PMID:16964248</ref> <ref>PMID:18716620</ref> <ref>PMID:18590780</ref> <ref>PMID:20153724</ref> <ref>PMID:21745816</ref> <ref>PMID:22411829</ref> <ref>PMID:22689415</ref> <ref>PMID:22466611</ref> <ref>PMID:22466612</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Ubiquitin conjugation is an important signal in cellular pathways, changing the fate of a target protein, by degradation, relocalisation or complex formation. These signals are balanced by deubiquitinating enzymes (DUBs), which antagonize ubiquitination of specific protein substrates. Because ubiquitination pathways are critically important, DUB activity is often carefully controlled. USP7 is a highly abundant DUB with numerous targets that plays complex roles in diverse pathways, including DNA regulation, p53 stress response and endosomal protein recycling. Full-length USP7 switches between an inactive and an active state, tuned by the positioning of 5 Ubl folds in the C-terminal HUBL domain. The active state requires interaction between the last two Ubls (USP7(45)) and the catalytic domain (USP7(CD)), and this can be promoted by allosteric interaction from the first 3 Ubl domains of USP7 (USP7(123)) interacting with GMPS. Here we study the transition between USP7 states. We provide a crystal structure of USP7(CD123) and show that CD and Ubl123 are connected via an extended charged alpha helix. Mutational analysis is used to determine whether the charge and rigidity of this 'connector helix' are important for full USP7 activity.

-	~~Authors:~~ Kim, R.Q.~~, vanDijk, W~~.J.~~, Sixma, T~~.K.	+	Structure of USP7 catalytic domain and three Ubl-domains reveals a connector alpha-helix with regulatory role.,Kim RQ, van Dijk WJ, Sixma TK J Struct Biol. 2016 Jul;195(1):11-8. doi: 10.1016/j.jsb.2016.05.005. Epub 2016, May 13. PMID:27183903<ref>PMID:27183903</ref>

-	~~Description~~: ~~Not yet~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
-	[[Category: Kim, R.Q]]	+	<div class="pdbe-citations 5fwi" style="background-color:#fffaf0;"></div>
-	[[Category: Sixma, T.K]]	+	== References ==
-	[[Category: ~~Vandijk~~, W.J]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ubiquitinyl hydrolase 1]]
		+	[[Category: Kim, R Q]]
		+	[[Category: Sixma, T K]]
		+	[[Category: VanDijk, W J]]
		+	[[Category: Deubiquitinase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Ubiquitin-like]]
		+	[[Category: Usp]]

OCA at 00:51, 10 March 2016

OCA — Thu, 10 Mar 2016 00:51:29 GMT

←Older revision		Revision as of 00:51, 10 March 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5fwi is ON HOLD	+	The entry 5fwi is ON HOLD until Paper Publication

	Authors: Kim, R.Q., vanDijk, W.J., Sixma, T.K.		Authors: Kim, R.Q., vanDijk, W.J., Sixma, T.K.

OCA: Protected "5fwi" [edit=sysop:move=sysop]

OCA — Fri, 26 Feb 2016 15:39:31 GMT

Protected "5fwi" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:39, 26 February 2016

OCA: New page: '''Unreleased structure''' The entry 5fwi is ON HOLD Authors: Kim, R.Q., vanDijk, W.J., Sixma, T.K. Description: Not yet Category: Unreleased Structures Category: Kim, R.Q [[Ca...

OCA — Fri, 26 Feb 2016 15:39:30 GMT

New page: '''Unreleased structure''' The entry 5fwi is ON HOLD Authors: Kim, R.Q., vanDijk, W.J., Sixma, T.K. Description: Not yet Category: Unreleased Structures Category: Kim, R.Q [[Ca...

New page

'''Unreleased structure'''

The entry 5fwi is ON HOLD

Authors: Kim, R.Q., vanDijk, W.J., Sixma, T.K.

Description: Not yet
[[Category: Unreleased Structures]]
[[Category: Kim, R.Q]]
[[Category: Sixma, T.K]]
[[Category: Vandijk, W.J]]