7qza - Revision history

OCA at 07:54, 1 May 2024

OCA — Wed, 01 May 2024 07:54:07 GMT

←Older revision		Revision as of 07:54, 1 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7qza]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QZA FirstGlance]. <br>		<table><tr><td colspan='2'>[[7qza]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QZA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 2.698Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=7qza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qza OCA], [https://pdbe.org/7qza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qza RCSB], [https://www.ebi.ac.uk/pdbsum/7qza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qza 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=7qza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qza OCA], [https://pdbe.org/7qza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qza RCSB], [https://www.ebi.ac.uk/pdbsum/7qza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qza ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/Q88HV5_PSEPK Q88HV5_PSEPK]]	+	[https://www.uniprot.org/uniprot/Q88HV5_PSEPK Q88HV5_PSEPK]
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	DyP-type peroxidases (DyPs) are microbial enzymes that catalyze the oxidation of a wide range of substrates, including synthetic dyes, lignin-derived compounds, and metals, such as Mn(2+) and Fe(2+), and have enormous biotechnological potential in biorefineries. However, many questions on the molecular basis of enzyme function and stability remain unanswered. In this work, high-resolution structures of PpDyP wild-type and two engineered variants (6E10 and 29E4) generated by directed evolution were obtained. The X-ray crystal structures revealed the typical ferredoxin-like folds, with three heme access pathways, two tunnels, and one cavity, limited by three long loops including catalytic residues. Variant 6E10 displays significantly increased loops' flexibility that favors function over stability: despite the considerably higher catalytic efficiency, this variant shows poorer protein stability compared to wild-type and 29E4 variants. Constant-pH MD simulations revealed a more positively charged microenvironment near the heme pocket of variant 6E10, particularly in the neutral to alkaline pH range. This microenvironment affects enzyme activity by modulating the pK a of essential residues in the heme vicinity and should account for variant 6E10 improved activity at pH 7-8 compared to the wild-type and 29E4 that show optimal enzymatic activity close to pH 4. Our findings shed light on the structure-function relationships of DyPs at the molecular level, including their pH-dependent conformational plasticity. These are essential for understanding and engineering the catalytic properties of DyPs for future biotechnological applications.	+
-		+
-	Unveiling molecular details behind improved activity at neutral to alkaline pH of an engineered DyP-type peroxidase.,Borges PT, Silva D, Silva TFD, Brissos V, Canellas M, Lucas MF, Masgrau L, Melo EP, Machuqueiro M, Frazao C, Martins LO Comput Struct Biotechnol J. 2022 Jul 21;20:3899-3910. doi:, 10.1016/j.csbj.2022.07.032. eCollection 2022. PMID:35950185<ref>PMID:35950185</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 7qza" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 03:12, 8 September 2022

OCA — Thu, 08 Sep 2022 03:12:42 GMT

←Older revision		Revision as of 03:12, 8 September 2022
Line 1:		Line 1:

	==Crystal structure of a DyP-type peroxidase 29E4 variant from Pseudomonas putida==		==Crystal structure of a DyP-type peroxidase 29E4 variant from Pseudomonas putida==
-	<StructureSection load='7qza' size='340' side='right'caption='[[7qza]]' scene=''>	+	<StructureSection load='7qza' size='340' side='right'caption='[[7qza]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QZA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7qza]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QZA FirstGlance]. <br>
-	</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=7qza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qza OCA], [https://pdbe.org/7qza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qza RCSB], [https://www.ebi.ac.uk/pdbsum/7qza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qza ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=7qza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qza OCA], [https://pdbe.org/7qza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qza RCSB], [https://www.ebi.ac.uk/pdbsum/7qza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qza ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/Q88HV5_PSEPK Q88HV5_PSEPK]]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	DyP-type peroxidases (DyPs) are microbial enzymes that catalyze the oxidation of a wide range of substrates, including synthetic dyes, lignin-derived compounds, and metals, such as Mn(2+) and Fe(2+), and have enormous biotechnological potential in biorefineries. However, many questions on the molecular basis of enzyme function and stability remain unanswered. In this work, high-resolution structures of PpDyP wild-type and two engineered variants (6E10 and 29E4) generated by directed evolution were obtained. The X-ray crystal structures revealed the typical ferredoxin-like folds, with three heme access pathways, two tunnels, and one cavity, limited by three long loops including catalytic residues. Variant 6E10 displays significantly increased loops' flexibility that favors function over stability: despite the considerably higher catalytic efficiency, this variant shows poorer protein stability compared to wild-type and 29E4 variants. Constant-pH MD simulations revealed a more positively charged microenvironment near the heme pocket of variant 6E10, particularly in the neutral to alkaline pH range. This microenvironment affects enzyme activity by modulating the pK a of essential residues in the heme vicinity and should account for variant 6E10 improved activity at pH 7-8 compared to the wild-type and 29E4 that show optimal enzymatic activity close to pH 4. Our findings shed light on the structure-function relationships of DyPs at the molecular level, including their pH-dependent conformational plasticity. These are essential for understanding and engineering the catalytic properties of DyPs for future biotechnological applications.
		+
		+	Unveiling molecular details behind improved activity at neutral to alkaline pH of an engineered DyP-type peroxidase.,Borges PT, Silva D, Silva TFD, Brissos V, Canellas M, Lucas MF, Masgrau L, Melo EP, Machuqueiro M, Frazao C, Martins LO Comput Struct Biotechnol J. 2022 Jul 21;20:3899-3910. doi:, 10.1016/j.csbj.2022.07.032. eCollection 2022. PMID:35950185<ref>PMID:35950185</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7qza" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Pseudomonas putida]]
	[[Category: Borges PT]]		[[Category: Borges PT]]
	[[Category: Frazao C]]		[[Category: Frazao C]]
	[[Category: Martins LO]]		[[Category: Martins LO]]
	[[Category: Silva D]]		[[Category: Silva D]]

OCA at 11:06, 31 August 2022

OCA — Wed, 31 Aug 2022 11:06:08 GMT

←Older revision		Revision as of 11:06, 31 August 2022
Line 1:		Line 1:

	==Crystal structure of a DyP-type peroxidase 29E4 variant from Pseudomonas putida==		==Crystal structure of a DyP-type peroxidase 29E4 variant from Pseudomonas putida==
-	<StructureSection load='7qza' size='340' side='right'caption='[[7qza]]~~, [[Resolution\|resolution]] 2.70Å~~' scene=''>	+	<StructureSection load='7qza' size='340' side='right'caption='[[7qza]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[7qza]] is a 8 chain structure.~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QZA FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QZA FirstGlance]. <br>
-	</td></tr>~~<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>~~	+	</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=7qza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qza OCA], [https://pdbe.org/7qza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qza RCSB], [https://www.ebi.ac.uk/pdbsum/7qza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qza 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=7qza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qza OCA], [https://pdbe.org/7qza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qza RCSB], [https://www.ebi.ac.uk/pdbsum/7qza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qza ProSAT]</span></td></tr>	+
	</table>		</table>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	DyP-type peroxidases (DyPs) are microbial enzymes that catalyze the oxidation of a wide range of substrates, including synthetic dyes, lignin-derived compounds, and metals, such as Mn(2+) and Fe(2+), and have enormous biotechnological potential in biorefineries. However, many questions on the molecular basis of enzyme function and stability remain unanswered. In this work, high-resolution structures of PpDyP wild-type and two engineered variants (6E10 and 29E4) generated by directed evolution were obtained. The X-ray crystal structures revealed the typical ferredoxin-like folds, with three heme access pathways, two tunnels, and one cavity, limited by three long loops including catalytic residues. Variant 6E10 displays significantly increased loops' flexibility that favors function over stability: despite the considerably higher catalytic efficiency, this variant shows poorer protein stability compared to wild-type and 29E4 variants. Constant-pH MD simulations revealed a more positively charged microenvironment near the heme pocket of variant 6E10, particularly in the neutral to alkaline pH range. This microenvironment affects enzyme activity by modulating the pK a of essential residues in the heme vicinity and should account for variant 6E10 improved activity at pH 7-8 compared to the wild-type and 29E4 that show optimal enzymatic activity close to pH 4. Our findings shed light on the structure-function relationships of DyPs at the molecular level, including their pH-dependent conformational plasticity. These are essential for understanding and engineering the catalytic properties of DyPs for future biotechnological applications.
-
-	Unveiling molecular details behind improved activity at neutral to alkaline pH of an engineered DyP-type peroxidase.,Borges PT, Silva D, Silva TFD, Brissos V, Canellas M, Lucas MF, Masgrau L, Melo EP, Machuqueiro M, Frazao C, Martins LO Comput Struct Biotechnol J. 2022 Jul 21;20:3899-3910. doi:, 10.1016/j.csbj.2022.07.032. eCollection 2022. PMID:35950185<ref>PMID:35950185</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 7qza" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Borges~~, P T~~]]	+	[[Category: Borges PT]]
-	[[Category: Frazao, C]]	+	[[Category: Frazao C]]
-	[[Category: Martins~~, L O~~]]	+	[[Category: Martins LO]]
-	[[Category: Silva, D]]	+	[[Category: Silva D]]
-	~~[[Category: Directed evolution]]~~	+
-	~~[[Category: Dyp]]~~	+
-	~~[[Category: Heme]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Pseudomonas putida~~]]	+

OCA at 05:12, 25 August 2022

OCA — Thu, 25 Aug 2022 05:12:38 GMT

←Older revision		Revision as of 05:12, 25 August 2022
Line 1:		Line 1:

	==Crystal structure of a DyP-type peroxidase 29E4 variant from Pseudomonas putida==		==Crystal structure of a DyP-type peroxidase 29E4 variant from Pseudomonas putida==
-	<StructureSection load='7qza' size='340' side='right'caption='[[7qza]]' scene=''>	+	<StructureSection load='7qza' size='340' side='right'caption='[[7qza]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QZA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7qza]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QZA FirstGlance]. <br>
-	</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=7qza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qza OCA], [https://pdbe.org/7qza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qza RCSB], [https://www.ebi.ac.uk/pdbsum/7qza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qza ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=7qza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qza OCA], [https://pdbe.org/7qza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qza RCSB], [https://www.ebi.ac.uk/pdbsum/7qza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qza ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	DyP-type peroxidases (DyPs) are microbial enzymes that catalyze the oxidation of a wide range of substrates, including synthetic dyes, lignin-derived compounds, and metals, such as Mn(2+) and Fe(2+), and have enormous biotechnological potential in biorefineries. However, many questions on the molecular basis of enzyme function and stability remain unanswered. In this work, high-resolution structures of PpDyP wild-type and two engineered variants (6E10 and 29E4) generated by directed evolution were obtained. The X-ray crystal structures revealed the typical ferredoxin-like folds, with three heme access pathways, two tunnels, and one cavity, limited by three long loops including catalytic residues. Variant 6E10 displays significantly increased loops' flexibility that favors function over stability: despite the considerably higher catalytic efficiency, this variant shows poorer protein stability compared to wild-type and 29E4 variants. Constant-pH MD simulations revealed a more positively charged microenvironment near the heme pocket of variant 6E10, particularly in the neutral to alkaline pH range. This microenvironment affects enzyme activity by modulating the pK a of essential residues in the heme vicinity and should account for variant 6E10 improved activity at pH 7-8 compared to the wild-type and 29E4 that show optimal enzymatic activity close to pH 4. Our findings shed light on the structure-function relationships of DyPs at the molecular level, including their pH-dependent conformational plasticity. These are essential for understanding and engineering the catalytic properties of DyPs for future biotechnological applications.
		+
		+	Unveiling molecular details behind improved activity at neutral to alkaline pH of an engineered DyP-type peroxidase.,Borges PT, Silva D, Silva TFD, Brissos V, Canellas M, Lucas MF, Masgrau L, Melo EP, Machuqueiro M, Frazao C, Martins LO Comput Struct Biotechnol J. 2022 Jul 21;20:3899-3910. doi:, 10.1016/j.csbj.2022.07.032. eCollection 2022. PMID:35950185<ref>PMID:35950185</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7qza" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Borges PT]]	+	[[Category: Borges, P T]]
-	[[Category: Frazao C]]	+	[[Category: Frazao, C]]
-	[[Category: Martins LO]]	+	[[Category: Martins, L O]]
-	[[Category: Silva D]]	+	[[Category: Silva, D]]
		+	[[Category: Directed evolution]]
		+	[[Category: Dyp]]
		+	[[Category: Heme]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Pseudomonas putida]]

OCA at 04:52, 3 August 2022

OCA — Wed, 03 Aug 2022 04:52:05 GMT

←Older revision		Revision as of 04:52, 3 August 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7qza is ~~ON HOLD until Paper Publication~~	+	==Crystal structure of a DyP-type peroxidase 29E4 variant from Pseudomonas putida==
-		+	<StructureSection load='7qza' size='340' side='right'caption='[[7qza]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QZA FirstGlance]. <br>
-	~~Description~~:	+	</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=7qza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qza OCA], [https://pdbe.org/7qza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qza RCSB], [https://www.ebi.ac.uk/pdbsum/7qza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qza ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Borges PT]]
		+	[[Category: Frazao C]]
		+	[[Category: Martins LO]]
		+	[[Category: Silva D]]

OCA at 10:20, 27 April 2022

OCA — Wed, 27 Apr 2022 10:20:34 GMT

←Older revision		Revision as of 10:20, 27 April 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7qza is ON HOLD	+	The entry 7qza is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "7qza" [edit=sysop:move=sysop]

OCA — Wed, 09 Feb 2022 06:08:41 GMT

Protected "7qza" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:08, 9 February 2022

OCA: New page: '''Unreleased structure''' The entry 7qza is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 09 Feb 2022 06:08:40 GMT

New page: '''Unreleased structure''' The entry 7qza is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7qza is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]