6s0s - Revision history

OCA at 12:32, 24 January 2024

OCA — Wed, 24 Jan 2024 12:32:31 GMT

←Older revision		Revision as of 12:32, 24 January 2024
Line 1:		Line 1:

	==The crystal structure of kanamycin B dioxygenase (KanJ) from Streptomyces kanamyceticus in complex with nickel, ribostamycin B and 2-oxoglutarate==		==The crystal structure of kanamycin B dioxygenase (KanJ) from Streptomyces kanamyceticus in complex with nickel, ribostamycin B and 2-oxoglutarate==
-	<StructureSection load='6s0s' size='340' side='right'caption='[[6s0s]]' scene=''>	+	<StructureSection load='6s0s' size='340' side='right'caption='[[6s0s]], [[Resolution\|resolution]] 2.40Å' 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=6S0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S0S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6s0s]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_kanamyceticus Streptomyces kanamyceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S0S 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=6s0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s0s OCA], [https://pdbe.org/6s0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s0s RCSB], [https://www.ebi.ac.uk/pdbsum/6s0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s0s ProSAT]</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]] 2.4Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=RIO:RIBOSTAMYCIN'>RIO</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=6s0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s0s OCA], [https://pdbe.org/6s0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s0s RCSB], [https://www.ebi.ac.uk/pdbsum/6s0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s0s ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/KANJ_STRKN KANJ_STRKN] Mediates the conversion of kanamycin B into 2'-dehydrokanamycin A during the transformation of kanamycin B to kanamycin A.<ref>PMID:22374809</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Kanamycin A is an aminoglycoside antibiotic isolated from Streptomyces kanamyceticus and used against a wide spectrum of bacteria, including Mycobacterium tuberculosis. Biosynthesis of kanamycin involves an oxidative deamination step catalyzed by kanamycin B dioxygenase (KanJ), thereby the C2' position of kanamycin B is transformed into a keto group upon release of ammonia. Here we present for the first time, structural models of KanJ with several ligands, which along with the results of ITC binding assays and HPLC activity tests explain substrate specificity of the enzyme. The large size of the binding pocket suggests that KanJ can accept a broad range of substrates, which was confirmed by activity tests. Specificity of the enzyme with respect to its substrate is determined by, the hydrogen bond interactions between the methylamino group of the antibiotic and highly conserved Asp134 and Cys150 as well as, between hydroxyl groups of the substrate and Asn120 and Gln80. Upon antibiotic binding, the C-terminus loop is significantly rearranged and Gln80 and Asn120, which are directly involved in substrate recognition, change their conformations. Based on reaction energy profiles obtained by density functional theory (DFT) simulations, we propose a mechanism of ketone formation involving the reactive Fe(IV) =O and proceeding either via OH rebound, which yields a hemiaminal intermediate or by abstraction of two hydrogen atoms, which leads to an imine species. At acidic pH, the latter involves a lower barrier than the OH rebound, whereas at basic pH, the barrier leading to an imine vanishes completely.
		+
		+	A study on the structure, mechanism and biochemistry of kanamycin B dioxygenase (KanJ) - an enzyme with a broad range of substrates.,Mrugala B, Milaczewska A, Porebski PJ, Niedzialkowska E, Guzik M, Minor W, Borowski T FEBS J. 2020 Jun 27. doi: 10.1111/febs.15462. PMID:32592631<ref>PMID:32592631</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6s0s" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Dioxygenase 3D structures\|Dioxygenase 3D structures]]		*[[Dioxygenase 3D structures\|Dioxygenase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Streptomyces kanamyceticus]]
	[[Category: Borowski T]]		[[Category: Borowski T]]
	[[Category: Minor W]]		[[Category: Minor W]]

OCA at 11:08, 30 March 2022

OCA — Wed, 30 Mar 2022 11:08:01 GMT

←Older revision		Revision as of 11:08, 30 March 2022
Line 1:		Line 1:

	==The crystal structure of kanamycin B dioxygenase (KanJ) from Streptomyces kanamyceticus in complex with nickel, ribostamycin B and 2-oxoglutarate==		==The crystal structure of kanamycin B dioxygenase (KanJ) from Streptomyces kanamyceticus in complex with nickel, ribostamycin B and 2-oxoglutarate==
-	<StructureSection load='6s0s' size='340' side='right'caption='[[6s0s]]~~, [[Resolution\|resolution]] 2.40Å~~' scene=''>	+	<StructureSection load='6s0s' size='340' side='right'caption='[[6s0s]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[6s0s]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1441 As 4.1441].~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S0S OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6S0S FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S0S FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=RIO:RIBOSTAMYCIN'>RIO</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=6s0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s0s OCA], [https://pdbe.org/6s0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s0s RCSB], [https://www.ebi.ac.uk/pdbsum/6s0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s0s ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">kanJ, kacB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1967 AS 4.1441])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.37 1.14.11.37] </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=6s0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s0s OCA], [~~http~~://pdbe.org/6s0s PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6s0s RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6s0s PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6s0s ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[http://www.uniprot.org/uniprot/KANJ_STRKN KANJ_STRKN]] Mediates the conversion of kanamycin B into 2'-dehydrokanamycin A during the transformation of kanamycin B to kanamycin A.<ref>PMID:22374809</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Kanamycin A is an aminoglycoside antibiotic isolated from Streptomyces kanamyceticus and used against a wide spectrum of bacteria, including Mycobacterium tuberculosis. Biosynthesis of kanamycin involves an oxidative deamination step catalyzed by kanamycin B dioxygenase (KanJ), thereby the C2' position of kanamycin B is transformed into a keto group upon release of ammonia. Here we present for the first time, structural models of KanJ with several ligands, which along with the results of ITC binding assays and HPLC activity tests explain substrate specificity of the enzyme. The large size of the binding pocket suggests that KanJ can accept a broad range of substrates, which was confirmed by activity tests. Specificity of the enzyme with respect to its substrate is determined by, the hydrogen bond interactions between the methylamino group of the antibiotic and highly conserved Asp134 and Cys150 as well as, between hydroxyl groups of the substrate and Asn120 and Gln80. Upon antibiotic binding, the C-terminus loop is significantly rearranged and Gln80 and Asn120, which are directly involved in substrate recognition, change their conformations. Based on reaction energy profiles obtained by density functional theory (DFT) simulations, we propose a mechanism of ketone formation involving the reactive Fe(IV) =O and proceeding either via OH rebound, which yields a hemiaminal intermediate or by abstraction of two hydrogen atoms, which leads to an imine species. At acidic pH, the latter involves a lower barrier than the OH rebound, whereas at basic pH, the barrier leading to an imine vanishes completely.
-
-	A study on the structure, mechanism and biochemistry of kanamycin B dioxygenase (KanJ) - an enzyme with a broad range of substrates.,Mrugala B, Milaczewska A, Porebski PJ, Niedzialkowska E, Guzik M, Minor W, Borowski T FEBS J. 2020 Jun 27. doi: 10.1111/febs.15462. PMID:32592631<ref>PMID:32592631</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 6s0s" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Dioxygenase 3D structures\|Dioxygenase 3D structures]]		*[[Dioxygenase 3D structures\|Dioxygenase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: As 4 1441]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Oxidoreductase]]~~	+	[[Category: Borowski T]]
-	[[Category: Borowski, T]]	+	[[Category: Minor W]]
-	[[Category: Minor, W]]	+	[[Category: Mrugala B]]
-	[[Category: Mrugala, B]]	+	[[Category: Niedzialkowska E]]
-	[[Category: Niedzialkowska, E]]	+	[[Category: Porebski PJ]]
-	[[Category: Porebski~~, P J]]~~	+
-	~~[[Category: 2-oxoglutarate]]~~	+
-	~~[[Category: Alpha-ketoglutarate dioxygenase]]~~	+
-	~~[[Category: Kanamycin biosynthesis]]~~	+
-	~~[[Category: Kanj]]~~	+
-	~~[[Category: Metal binding protein]]~~	+
-	~~[[Category: Non-heme iron dioxygenase]]~~	+
-	~~[[Category: Ribostamycin b~~]]	+

OCA at 07:07, 25 November 2020

OCA — Wed, 25 Nov 2020 07:07:36 GMT

←Older revision		Revision as of 07:07, 25 November 2020
Line 1:		Line 1:

	==The crystal structure of kanamycin B dioxygenase (KanJ) from Streptomyces kanamyceticus in complex with nickel, ribostamycin B and 2-oxoglutarate==		==The crystal structure of kanamycin B dioxygenase (KanJ) from Streptomyces kanamyceticus in complex with nickel, ribostamycin B and 2-oxoglutarate==
-	<StructureSection load='6s0s' size='340' side='right'caption='[[6s0s]]' scene=''>	+	<StructureSection load='6s0s' size='340' side='right'caption='[[6s0s]], [[Resolution\|resolution]] 2.40Å' 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=6S0S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6S0S FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6s0s]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1441 As 4.1441]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S0S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6S0S FirstGlance]. <br>
-	</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=6s0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s0s OCA], [http://pdbe.org/6s0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s0s RCSB], [http://www.ebi.ac.uk/pdbsum/6s0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s0s 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=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=RIO:RIBOSTAMYCIN'>RIO</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">kanJ, kacB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1967 AS 4.1441])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.37 1.14.11.37] </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=6s0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s0s OCA], [http://pdbe.org/6s0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s0s RCSB], [http://www.ebi.ac.uk/pdbsum/6s0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s0s ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KANJ_STRKN KANJ_STRKN]] Mediates the conversion of kanamycin B into 2'-dehydrokanamycin A during the transformation of kanamycin B to kanamycin A.<ref>PMID:22374809</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Kanamycin A is an aminoglycoside antibiotic isolated from Streptomyces kanamyceticus and used against a wide spectrum of bacteria, including Mycobacterium tuberculosis. Biosynthesis of kanamycin involves an oxidative deamination step catalyzed by kanamycin B dioxygenase (KanJ), thereby the C2' position of kanamycin B is transformed into a keto group upon release of ammonia. Here we present for the first time, structural models of KanJ with several ligands, which along with the results of ITC binding assays and HPLC activity tests explain substrate specificity of the enzyme. The large size of the binding pocket suggests that KanJ can accept a broad range of substrates, which was confirmed by activity tests. Specificity of the enzyme with respect to its substrate is determined by, the hydrogen bond interactions between the methylamino group of the antibiotic and highly conserved Asp134 and Cys150 as well as, between hydroxyl groups of the substrate and Asn120 and Gln80. Upon antibiotic binding, the C-terminus loop is significantly rearranged and Gln80 and Asn120, which are directly involved in substrate recognition, change their conformations. Based on reaction energy profiles obtained by density functional theory (DFT) simulations, we propose a mechanism of ketone formation involving the reactive Fe(IV) =O and proceeding either via OH rebound, which yields a hemiaminal intermediate or by abstraction of two hydrogen atoms, which leads to an imine species. At acidic pH, the latter involves a lower barrier than the OH rebound, whereas at basic pH, the barrier leading to an imine vanishes completely.
		+
		+	A study on the structure, mechanism and biochemistry of kanamycin B dioxygenase (KanJ) - an enzyme with a broad range of substrates.,Mrugala B, Milaczewska A, Porebski PJ, Niedzialkowska E, Guzik M, Minor W, Borowski T FEBS J. 2020 Jun 27. doi: 10.1111/febs.15462. PMID:32592631<ref>PMID:32592631</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6s0s" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Dioxygenase 3D structures\|Dioxygenase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: As 4 1441]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Borowski T]]	+	[[Category: Oxidoreductase]]
-	[[Category: Minor W]]	+	[[Category: Borowski, T]]
-	[[Category: Mrugala B]]	+	[[Category: Minor, W]]
-	[[Category: Niedzialkowska E]]	+	[[Category: Mrugala, B]]
-	[[Category: Porebski PJ]]	+	[[Category: Niedzialkowska, E]]
		+	[[Category: Porebski, P J]]
		+	[[Category: 2-oxoglutarate]]
		+	[[Category: Alpha-ketoglutarate dioxygenase]]
		+	[[Category: Kanamycin biosynthesis]]
		+	[[Category: Kanj]]
		+	[[Category: Metal binding protein]]
		+	[[Category: Non-heme iron dioxygenase]]
		+	[[Category: Ribostamycin b]]

OCA at 14:03, 8 July 2020

OCA — Wed, 08 Jul 2020 14:03:39 GMT

←Older revision		Revision as of 14:03, 8 July 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The ~~entry~~ 6s0s is ~~ON HOLD until Paper Publication~~	+	==The crystal structure of kanamycin B dioxygenase (KanJ) from Streptomyces kanamyceticus in complex with nickel, ribostamycin B and 2-oxoglutarate==
-		+	<StructureSection load='6s0s' size='340' side='right'caption='[[6s0s]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S0S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6S0S FirstGlance]. <br>
-	~~Description~~:	+	</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=6s0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s0s OCA], [http://pdbe.org/6s0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s0s RCSB], [http://www.ebi.ac.uk/pdbsum/6s0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s0s ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Borowski T]]
		+	[[Category: Minor W]]
		+	[[Category: Mrugala B]]
		+	[[Category: Niedzialkowska E]]
		+	[[Category: Porebski PJ]]

OCA at 07:21, 2 October 2019

OCA — Wed, 02 Oct 2019 07:21:21 GMT

←Older revision		Revision as of 07:21, 2 October 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6s0s is ON HOLD	+	The entry 6s0s is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6s0s" [edit=sysop:move=sysop]

OCA — Wed, 26 Jun 2019 05:27:46 GMT

Protected "6s0s" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:27, 26 June 2019

OCA: New page: '''Unreleased structure''' The entry 6s0s is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 26 Jun 2019 05:27:45 GMT

New page: '''Unreleased structure''' The entry 6s0s is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6s0s is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]