5f5o - Revision history

OCA at 09:11, 20 March 2024

OCA — Wed, 20 Mar 2024 09:11:47 GMT

←Older revision		Revision as of 09:11, 20 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/NCAP_MABVO NCAP_MABVO] Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. During replication, encapsidation by NP is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).		[https://www.uniprot.org/uniprot/NCAP_MABVO NCAP_MABVO] Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. During replication, encapsidation by NP is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Marburg virus (MARV) encodes a nucleoprotein (NP) to encapsidate its genome by oligomerization and form a ribonucleoprotein complex (RNP). According to previous investigation on nonsegmented negative-sense RNA viruses (nsNSV), the newly synthesized NPs must be prevented from indiscriminately binding to noncognate RNAs. During the viral RNA synthesis process, the RNPs undergo a transition from an RNA-bound form to a template-free form, to open access for the interaction between the viral polymerase and the RNA template. In filoviruses, this transition is regulated by VP35 peptide and other viral components. To further understand the dynamic process of filovirus RNP formation, we report here the structure of MARV NPcore, both in the apo form and in the VP35 peptide-chaperoned form. These structures reveal a typical bilobed structure, with a positive-charged RNA binding groove between two lobes. In the apo form, the MARV NP exists in an interesting hexameric state formed by the hydrophobic interaction within the long helix of the NPcore C-terminal region, which shows high structural flexibility among filoviruses and may imply critical function during RNP formation. Moreover, the VP35 peptide-chaperoned NPcore remains in a monomeric state and completely loses its affinity for single-stranded RNA (ssRNA). The structural comparison reveals that the RNA binding groove undergoes a transition from closed state to open state, chaperoned by VP35 peptide, thus preventing the interaction for viral RNA. Our investigation provides considerable structural insight into the filovirus RNP working mechanism and may support the development of antiviral therapies targeting the RNP formation of filovirus.IMPORTANCE Marburg virus is one of the most dangerous viruses, with high morbidity and mortality. A recent outbreak in Angola in 2005 caused the deaths of 272 persons. NP is one of the most essential proteins, as it encapsidates and protects the whole virus genome simultaneously with self-assembly oligomerization. Here we report the structures of MARV NPcore in two different forms. In the MARV NP apo form, we identify an interesting hexamer formed by hydrophobic interaction within a long helix, which is highly conserved and flexible among filoviruses and may indicate its critical function during the virus RNP formation. Moreover, the structural comparison with the NP-VP35 peptide complex reveals a structural transition chaperoned by VP35, in which the RNA binding groove undergoes a transition from closed state to open state. Finally, we discussed the high conservation and critical role of the VP35 binding pocket and its potential use for therapeutic development.
-
-	Structural Insight into Nucleoprotein Conformation Change Chaperoned by VP35 Peptide in Marburg Virus.,Liu B, Dong S, Li G, Wang W, Liu X, Wang Y, Yang C, Rao Z, Guo Y J Virol. 2017 Jul 27;91(16). pii: e00825-17. doi: 10.1128/JVI.00825-17. Print, 2017 Aug 15. PMID:28566377<ref>PMID:28566377</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5f5o" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Nucleoprotein 3D structures\|Nucleoprotein 3D structures]]		*[[Nucleoprotein 3D structures\|Nucleoprotein 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:48, 12 July 2023

OCA — Wed, 12 Jul 2023 08:48:28 GMT

←Older revision		Revision as of 08:48, 12 July 2023
Line 1:		Line 1:

	==Crystal structure of Marburg virus nucleoprotein core domain bound to VP35 regulation peptide==		==Crystal structure of Marburg virus nucleoprotein core domain bound to VP35 regulation peptide==
-	<StructureSection load='5f5o' size='340' side='right' caption='[[5f5o]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='5f5o' size='340' side='right'caption='[[5f5o]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5f5o]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lake_victoria_marburgvirus_(strain_ozolin~~-~~75)~~ Lake ~~victoria~~ marburgvirus ~~(strain ozolin~~-~~75)~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F5O OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5F5O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5f5o]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Lake_Victoria_marburgvirus_-_Ozolin Lake Victoria marburgvirus - Ozolin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F5O FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=SO4:SULFATE+ION'>SO4</scene~~></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]] 2.2Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[5f5m\|5f5m]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~"><~~b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">NP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=482820 Lake Victoria marburgvirus (strain Ozolin-75)])~~</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=5f5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f5o OCA], [https://pdbe.org/5f5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f5o RCSB], [https://www.ebi.ac.uk/pdbsum/5f5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f5o ProSAT]</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=5f5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f5o OCA], [~~http~~://pdbe.org/5f5o PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5f5o RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5f5o PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5f5o ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NCAP_MABVO NCAP_MABVO]] Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. During replication, encapsidation by NP is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity)~~. [[http://www.uniprot.org/uniprot/VP35_MABVO VP35_MABVO]] Acts as a polymerase cofactor in the RNA polymerase transcription and replication complex~~.	+	[https://www.uniprot.org/uniprot/NCAP_MABVO NCAP_MABVO] Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. During replication, encapsidation by NP is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5f5o" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5f5o" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Nucleoprotein 3D structures\|Nucleoprotein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Dong, S S~~]]	+	[[Category: Lake Victoria marburgvirus - Ozolin]]
-	[[Category: ~~Guo, Y~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Li, G B~~]]	+	[[Category: Dong SS]]
-	[[Category: ~~Liu, B C~~]]	+	[[Category: Guo Y]]
-	[[Category: ~~Liu, X~~]]	+	[[Category: Li GB]]
-	[[Category: ~~Wang, W J~~]]	+	[[Category: Liu BC]]
-	[[Category: ~~Wang, W M~~]]	+	[[Category: Liu X]]
-	[[Category: ~~Complex~~]]	+	[[Category: Wang WJ]]
-	[[Category: ~~Filovirus]]~~	+	[[Category: Wang WM]]
-	~~[[Category: Marburg virus]]~~	+
-	~~[[Category: Npbp]]~~	+
-	~~[[Category: Nuclear protein-peptide complex]]~~	+
-	~~[[Category: Nucleocapsid]]~~	+
-	~~[[Category: Nucleoprotein]]~~	+
-	~~[[Category: Vp35 peptide~~]]	+

OCA at 01:14, 16 November 2017

OCA — Thu, 16 Nov 2017 01:14:54 GMT

←Older revision		Revision as of 01:14, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='5f5o' size='340' side='right' caption='[[5f5o]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='5f5o' size='340' side='right' caption='[[5f5o]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5f5o]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F5O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5f5o]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Lake_victoria_marburgvirus_(strain_ozolin-75) Lake victoria marburgvirus (strain ozolin-75)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F5O FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5f5m\|5f5m]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5f5m\|5f5m]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=482820 Lake Victoria marburgvirus (strain Ozolin-75)])</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=5f5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f5o OCA], [http://pdbe.org/5f5o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f5o RCSB], [http://www.ebi.ac.uk/pdbsum/5f5o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f5o ProSAT]</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=5f5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f5o OCA], [http://pdbe.org/5f5o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f5o RCSB], [http://www.ebi.ac.uk/pdbsum/5f5o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f5o ProSAT]</span></td></tr>
	</table>		</table>

OCA at 10:40, 3 August 2017

OCA — Thu, 03 Aug 2017 10:40:22 GMT

←Older revision		Revision as of 10:40, 3 August 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5f5o is ~~ON HOLD until Jun 24 2018~~	+	==Crystal structure of Marburg virus nucleoprotein core domain bound to VP35 regulation peptide==
		+	<StructureSection load='5f5o' size='340' side='right' caption='[[5f5o]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5f5o]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F5O FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5f5m\|5f5m]]</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=5f5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f5o OCA], [http://pdbe.org/5f5o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f5o RCSB], [http://www.ebi.ac.uk/pdbsum/5f5o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f5o ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NCAP_MABVO NCAP_MABVO]] Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. During replication, encapsidation by NP is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity). [[http://www.uniprot.org/uniprot/VP35_MABVO VP35_MABVO]] Acts as a polymerase cofactor in the RNA polymerase transcription and replication complex.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Marburg virus (MARV) encodes a nucleoprotein (NP) to encapsidate its genome by oligomerization and form a ribonucleoprotein complex (RNP). According to previous investigation on nonsegmented negative-sense RNA viruses (nsNSV), the newly synthesized NPs must be prevented from indiscriminately binding to noncognate RNAs. During the viral RNA synthesis process, the RNPs undergo a transition from an RNA-bound form to a template-free form, to open access for the interaction between the viral polymerase and the RNA template. In filoviruses, this transition is regulated by VP35 peptide and other viral components. To further understand the dynamic process of filovirus RNP formation, we report here the structure of MARV NPcore, both in the apo form and in the VP35 peptide-chaperoned form. These structures reveal a typical bilobed structure, with a positive-charged RNA binding groove between two lobes. In the apo form, the MARV NP exists in an interesting hexameric state formed by the hydrophobic interaction within the long helix of the NPcore C-terminal region, which shows high structural flexibility among filoviruses and may imply critical function during RNP formation. Moreover, the VP35 peptide-chaperoned NPcore remains in a monomeric state and completely loses its affinity for single-stranded RNA (ssRNA). The structural comparison reveals that the RNA binding groove undergoes a transition from closed state to open state, chaperoned by VP35 peptide, thus preventing the interaction for viral RNA. Our investigation provides considerable structural insight into the filovirus RNP working mechanism and may support the development of antiviral therapies targeting the RNP formation of filovirus.IMPORTANCE Marburg virus is one of the most dangerous viruses, with high morbidity and mortality. A recent outbreak in Angola in 2005 caused the deaths of 272 persons. NP is one of the most essential proteins, as it encapsidates and protects the whole virus genome simultaneously with self-assembly oligomerization. Here we report the structures of MARV NPcore in two different forms. In the MARV NP apo form, we identify an interesting hexamer formed by hydrophobic interaction within a long helix, which is highly conserved and flexible among filoviruses and may indicate its critical function during the virus RNP formation. Moreover, the structural comparison with the NP-VP35 peptide complex reveals a structural transition chaperoned by VP35, in which the RNA binding groove undergoes a transition from closed state to open state. Finally, we discussed the high conservation and critical role of the VP35 binding pocket and its potential use for therapeutic development.

-	~~Authors: Guo, Y~~., Liu, B~~.C.~~, ~~Liu, X.~~, Li, G~~.B.~~, Wang, W~~.M.~~, ~~Dong~~, S.S., ~~Wang, W.J~~.	+	Structural Insight into Nucleoprotein Conformation Change Chaperoned by VP35 Peptide in Marburg Virus.,Liu B, Dong S, Li G, Wang W, Liu X, Wang Y, Yang C, Rao Z, Guo Y J Virol. 2017 Jul 27;91(16). pii: e00825-17. doi: 10.1128/JVI.00825-17. Print, 2017 Aug 15. PMID:28566377<ref>PMID:28566377</ref>

-	~~Description: Crystal structure~~ of ~~Marburg virus nucleoprotein core domain bound to VP35 regulation peptide~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category: Unreleased Structures]]~~	+	</div>
-	~~[[Category~~: ~~Liu, X]]~~	+	<div class="pdbe-citations 5f5o" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Wang~~, ~~W.M~~]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Dong, S S]]
	[[Category: Guo, Y]]		[[Category: Guo, Y]]
-	[[Category: ~~Dong~~, ~~S.S~~]]	+	[[Category: Li, G B]]
-	[[Category: Liu, B.C]]	+	[[Category: Liu, B C]]
-	[[Category: Li, ~~G.B~~]]	+	[[Category: Liu, X]]
-	[[Category: Wang, W.J]]	+	[[Category: Wang, W J]]
		+	[[Category: Wang, W M]]
		+	[[Category: Complex]]
		+	[[Category: Filovirus]]
		+	[[Category: Marburg virus]]
		+	[[Category: Npbp]]
		+	[[Category: Nuclear protein-peptide complex]]
		+	[[Category: Nucleocapsid]]
		+	[[Category: Nucleoprotein]]
		+	[[Category: Vp35 peptide]]

OCA at 07:30, 24 May 2017

OCA — Wed, 24 May 2017 07:30:20 GMT

←Older revision		Revision as of 07:30, 24 May 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5f5o is ON HOLD until ~~May~~ 24 2018	+	The entry 5f5o is ON HOLD until Jun 24 2018

	Authors: Guo, Y., Liu, B.C., Liu, X., Li, G.B., Wang, W.M., Dong, S.S., Wang, W.J.		Authors: Guo, Y., Liu, B.C., Liu, X., Li, G.B., Wang, W.M., Dong, S.S., Wang, W.J.

OCA at 06:32, 10 May 2017

OCA — Wed, 10 May 2017 06:32:02 GMT

←Older revision		Revision as of 06:32, 10 May 2017
Line 7:		Line 7:
	Description: Crystal structure of Marburg virus nucleoprotein core domain bound to VP35 regulation peptide		Description: Crystal structure of Marburg virus nucleoprotein core domain bound to VP35 regulation peptide
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Liu, X]]
	[[Category: Wang, W.M]]		[[Category: Wang, W.M]]
	[[Category: Guo, Y]]		[[Category: Guo, Y]]
	[[Category: Dong, S.S]]		[[Category: Dong, S.S]]
-	[[Category: Liu, X]]
	[[Category: Liu, B.C]]		[[Category: Liu, B.C]]
	[[Category: Li, G.B]]		[[Category: Li, G.B]]
	[[Category: Wang, W.J]]		[[Category: Wang, W.J]]

OCA at 05:11, 12 April 2017

OCA — Wed, 12 Apr 2017 05:11:36 GMT

←Older revision		Revision as of 05:11, 12 April 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5f5o is ON HOLD until ~~Apr 11~~ 2018	+	The entry 5f5o is ON HOLD until May 24 2018

	Authors: Guo, Y., Liu, B.C., Liu, X., Li, G.B., Wang, W.M., Dong, S.S., Wang, W.J.		Authors: Guo, Y., Liu, B.C., Liu, X., Li, G.B., Wang, W.M., Dong, S.S., Wang, W.J.

OCA at 07:11, 5 April 2017

OCA — Wed, 05 Apr 2017 07:11:26 GMT

←Older revision		Revision as of 07:11, 5 April 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5f5o is ON HOLD until Apr 04 2018	+	The entry 5f5o is ON HOLD until Apr 11 2018

	Authors: Guo, Y., Liu, B.C., Liu, X., Li, G.B., Wang, W.M., Dong, S.S., Wang, W.J.		Authors: Guo, Y., Liu, B.C., Liu, X., Li, G.B., Wang, W.M., Dong, S.S., Wang, W.J.

OCA at 08:43, 9 March 2017

OCA — Thu, 09 Mar 2017 08:43:10 GMT

←Older revision		Revision as of 08:43, 9 March 2017
Line 8:		Line 8:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Wang, W.M]]		[[Category: Wang, W.M]]
		+	[[Category: Guo, Y]]
	[[Category: Dong, S.S]]		[[Category: Dong, S.S]]
	[[Category: Liu, X]]		[[Category: Liu, X]]
		+	[[Category: Liu, B.C]]
	[[Category: Li, G.B]]		[[Category: Li, G.B]]
	[[Category: Wang, W.J]]		[[Category: Wang, W.J]]
-	[[Category: Guo, Y]]
-	[[Category: Liu, B.C]]

OCA at 12:50, 9 December 2016

OCA — Fri, 09 Dec 2016 12:50:45 GMT

←Older revision		Revision as of 12:50, 9 December 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5f5o is ON HOLD until ~~Paper Publication~~	+	The entry 5f5o is ON HOLD until Apr 04 2018

	Authors: Guo, Y., Liu, B.C., Liu, X., Li, G.B., Wang, W.M., Dong, S.S., Wang, W.J.		Authors: Guo, Y., Liu, B.C., Liu, X., Li, G.B., Wang, W.M., Dong, S.S., Wang, W.J.