5v1y - Revision history

OCA at 13:39, 4 October 2023

OCA — Wed, 04 Oct 2023 13:39:45 GMT

←Older revision		Revision as of 13:39, 4 October 2023
Line 3:		Line 3:
	<StructureSection load='5v1y' size='340' side='right'caption='[[5v1y]], [[Resolution\|resolution]] 1.42Å' scene=''>		<StructureSection load='5v1y' size='340' side='right'caption='[[5v1y]], [[Resolution\|resolution]] 1.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5v1y]] is a 6 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=5V1Y OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5V1Y FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5v1y]] is a 6 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=5V1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V1Y FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[5v1z\|5v1z]]</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]] 1.421Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">ADRM1, GP110 ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&srchmode=5&id=9606 HUMAN]), UBB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PSMD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5v1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1y OCA], [https://pdbe.org/5v1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v1y RCSB], [https://www.ebi.ac.uk/pdbsum/5v1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1y 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=5v1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1y OCA], [~~http~~://pdbe.org/5v1y PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5v1y RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5v1y PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1y ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ADRM1_HUMAN ADRM1_HUMAN]] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:16990800</ref> <ref>PMID:17139257</ref> <ref>PMID:16815440</ref> <ref>PMID:16906146</ref> <ref>PMID:18497817</ref> [[http://www.uniprot.org/uniprot/PSMD1_HUMAN PSMD1_HUMAN]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[http://www.uniprot.org/uniprot/UBB_HUMAN UBB_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>	+	[https://www.uniprot.org/uniprot/ADRM1_HUMAN ADRM1_HUMAN] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:16990800</ref> <ref>PMID:17139257</ref> <ref>PMID:16815440</ref> <ref>PMID:16906146</ref> <ref>PMID:18497817</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 20:

	==See Also==		==See Also==
-	*[[~~Ubiquitin~~\|~~Ubiquitin~~]]	+	*[[3D structures of ubiquitin\|3D structures of ubiquitin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hemmis~~, C W~~]]	+	[[Category: Hemmis CW]]
-	[[Category: Hill~~, C P~~]]	+	[[Category: Hill CP]]
-	[[Category: Robinson, H]]	+	[[Category: Robinson H]]
-	[[Category: VanderLinden~~, R T~~]]	+	[[Category: VanderLinden RT]]
-	[[Category: Yao, T]]	+	[[Category: Yao T]]
-	~~[[Category: Proteasome]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Rpn13]]~~	+
-	~~[[Category: Rpn2]]~~	+
-	~~[[Category: Ubiquitin~~]]	+

OCA at 09:34, 4 December 2019

OCA — Wed, 04 Dec 2019 09:34:05 GMT

←Older revision		Revision as of 09:34, 4 December 2019
Line 1:		Line 1:

	==Crystal structure of the ternary RPN13 PRU-RPN2 (940-953)-ubiquitin complex==		==Crystal structure of the ternary RPN13 PRU-RPN2 (940-953)-ubiquitin complex==
-	<StructureSection load='5v1y' size='340' side='right' caption='[[5v1y]], [[Resolution\|resolution]] 1.42Å' scene=''>	+	<StructureSection load='5v1y' size='340' side='right'caption='[[5v1y]], [[Resolution\|resolution]] 1.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5v1y]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V1Y FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5v1y]] is a 6 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=5V1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V1Y FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5v1z\|5v1z]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5v1z\|5v1z]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADRM1, GP110 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), UBB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PSMD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5v1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1y OCA], [http://pdbe.org/5v1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v1y RCSB], [http://www.ebi.ac.uk/pdbsum/5v1y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1y 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=5v1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1y OCA], [http://pdbe.org/5v1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v1y RCSB], [http://www.ebi.ac.uk/pdbsum/5v1y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1y ProSAT]</span></td></tr>
	</table>		</table>
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5v1y" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5v1y" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ubiquitin\|Ubiquitin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Hemmis, C W]]		[[Category: Hemmis, C W]]
	[[Category: Hill, C P]]		[[Category: Hill, C P]]

OCA at 06:14, 10 May 2017

OCA — Wed, 10 May 2017 06:14:12 GMT

←Older revision		Revision as of 06:14, 10 May 2017
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/ADRM1_HUMAN ADRM1_HUMAN]] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:16990800</ref> <ref>PMID:17139257</ref> <ref>PMID:16815440</ref> <ref>PMID:16906146</ref> <ref>PMID:18497817</ref> [[http://www.uniprot.org/uniprot/PSMD1_HUMAN PSMD1_HUMAN]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[http://www.uniprot.org/uniprot/UBB_HUMAN UBB_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>		[[http://www.uniprot.org/uniprot/ADRM1_HUMAN ADRM1_HUMAN]] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:16990800</ref> <ref>PMID:17139257</ref> <ref>PMID:16815440</ref> <ref>PMID:16906146</ref> <ref>PMID:18497817</ref> [[http://www.uniprot.org/uniprot/PSMD1_HUMAN PSMD1_HUMAN]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[http://www.uniprot.org/uniprot/UBB_HUMAN UBB_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The 26S proteasome is a large cellular assembly that mediates the selective degradation of proteins in the nucleus and cytosol and is an established target for anti-cancer therapeutics. Protein substrates are typically targeted to the proteasome through modification with a polyubiquitin chain, which can be recognized by several proteasome-associated ubiquitin receptors. One of these receptors, RPN13/ADRM1, is recruited to the proteasome through direct interaction with the large scaffolding protein RPN2 within the 19S regulatory particle. To better understand the interactions between RPN13, RPN2, and ubiquitin, we used human proteins to map the RPN13-binding epitope to the C-terminal 14 residues of RPN2, which, like ubiquitin, binds the N-terminal PRU domain of RPN13. We also report crystal structures of the RPN13 PRU domain in complex with peptides corresponding to the RPN2 C-terminus and ubiquitin. Through mutational analysis, we validated the RPN2 binding interface revealed by our structures and quantified binding interactions with surface plasmon resonance and fluorescence polarization. In contrast to a previous report, we find that RPN13 binds ubiquitin with an affinity similar to that of other proteasome-associated ubiquitin receptors and that RPN2, ubiquitin, and the deubiquitylase UCH37 bind to RPN13 with independent energetics. These findings provide a detailed characterization of interactions that are important for proteasome function, indicate ubiquitin affinities that are consistent with the role of RPN13 as a proteasomal ubiquitin receptor, and have major implications for the development of novel anticancer therapeutics.
		+
		+	Structure and energetics of pairwise interactions between proteasome subunits RPN2, RPN13, and ubiquitin clarify a substrate recruitment mechanism.,VanderLinden RT, Hemmis CW, Yao T, Robinson H, Hill CP J Biol Chem. 2017 Apr 25. pii: jbc.M117.785287. doi: 10.1074/jbc.M117.785287. PMID:28442575<ref>PMID:28442575</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5v1y" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:12, 4 May 2017

OCA — Thu, 04 May 2017 13:12:33 GMT

←Older revision		Revision as of 13:12, 4 May 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5v1y is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Crystal structure of the ternary RPN13 PRU-RPN2 (940-953)-ubiquitin complex==
-		+	<StructureSection load='5v1y' size='340' side='right' caption='[[5v1y]], [[Resolution\|resolution]] 1.42Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5v1y]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V1Y FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5v1z\|5v1z]]</td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<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=5v1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1y OCA], [http://pdbe.org/5v1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v1y RCSB], [http://www.ebi.ac.uk/pdbsum/5v1y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1y ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ADRM1_HUMAN ADRM1_HUMAN]] Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.<ref>PMID:16990800</ref> <ref>PMID:17139257</ref> <ref>PMID:16815440</ref> <ref>PMID:16906146</ref> <ref>PMID:18497817</ref> [[http://www.uniprot.org/uniprot/PSMD1_HUMAN PSMD1_HUMAN]] Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. [[http://www.uniprot.org/uniprot/UBB_HUMAN UBB_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Hemmis, C W]]
		+	[[Category: Hill, C P]]
		+	[[Category: Robinson, H]]
		+	[[Category: VanderLinden, R T]]
		+	[[Category: Yao, T]]
		+	[[Category: Proteasome]]
		+	[[Category: Protein binding]]
		+	[[Category: Rpn13]]
		+	[[Category: Rpn2]]
		+	[[Category: Ubiquitin]]

OCA at 19:37, 15 March 2017

OCA — Wed, 15 Mar 2017 19:37:54 GMT

←Older revision		Revision as of 19:37, 15 March 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5v1y is ON HOLD	+	The entry 5v1y is ON HOLD until Paper Publication

-	Authors: ~~Hemmis, Casey W, VanderLinden, Ryan T, Yao, T, Robinson, H, Hill, Christopher P~~	+	Authors:

-	Description: ~~RRU Complex 940~~	+	Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Hemmis, Casey W, Vanderlinden, Ryan T, Yao, T, Robinson, H, Hill, Christopher P]]

OCA: Protected "5v1y" [edit=sysop:move=sysop]

OCA — Thu, 09 Mar 2017 15:14:48 GMT

Protected "5v1y" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:14, 9 March 2017

OCA: New page: '''Unreleased structure''' The entry 5v1y is ON HOLD Authors: Hemmis, Casey W, VanderLinden, Ryan T, Yao, T, Robinson, H, Hill, Christopher P Description: RRU Complex 940 [[Category: U...

OCA — Thu, 09 Mar 2017 15:14:47 GMT

New page: '''Unreleased structure''' The entry 5v1y is ON HOLD Authors: Hemmis, Casey W, VanderLinden, Ryan T, Yao, T, Robinson, H, Hill, Christopher P Description: RRU Complex 940 [[Category: U...

New page

'''Unreleased structure'''

The entry 5v1y is ON HOLD

Authors: Hemmis, Casey W, VanderLinden, Ryan T, Yao, T, Robinson, H, Hill, Christopher P

Description: RRU Complex 940
[[Category: Unreleased Structures]]
[[Category: Hemmis, Casey W, Vanderlinden, Ryan T, Yao, T, Robinson, H, Hill, Christopher P]]