4x5i - Revision history

OCA at 06:53, 3 April 2024

OCA — Wed, 03 Apr 2024 06:53:13 GMT

←Older revision		Revision as of 06:53, 3 April 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4x5i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X5I FirstGlance]. <br>		<table><tr><td colspan='2'>[[4x5i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X5I FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 1.8Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=4x5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5i OCA], [https://pdbe.org/4x5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x5i RCSB], [https://www.ebi.ac.uk/pdbsum/4x5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x5i 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=4x5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5i OCA], [https://pdbe.org/4x5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x5i RCSB], [https://www.ebi.ac.uk/pdbsum/4x5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x5i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.		[https://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	A high-pressure crystallographic study was conducted on Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP(+) in crystal forms containing both the open and closed conformations of the M20 loop under high-pressure conditions of up to 800 MPa. At pressures between 270 and 500 MPa the crystal form containing the open conformation exhibited a phase transition from P21 to C2. Several structural changes in ecDHFR were observed at high pressure that were also accompanied by structural changes in the NADP(+) cofactor and the hydration structure. In the crystal form with the closed conformation the M20 loop moved as the pressure changed, with accompanying conformational changes around the active site, including NADP(+) and folate. These movements were consistent with the suggested hypothesis that movement of the M20 loop was necessary for ecDHFR to catalyze the reaction. In the crystal form with the open conformation the nicotinamide ring of the NADP(+) cofactor undergoes a large flip as an intermediate step in the reaction, despite being in a crystalline state. Furthermore, observation of the water molecules between Arg57 and folate elucidated an early step in the substrate-binding pathway. These results demonstrate the possibility of using high-pressure protein crystallography as a method to capture high-energy substates or transient structures related to the protein reaction cycle.
-
-	High-pressure protein crystal structure analysis of Escherichia coli dihydrofolate reductase complexed with folate and NADP().,Nagae T, Yamada H, Watanabe N Acta Crystallogr D Struct Biol. 2018 Sep 1;74(Pt 9):895-905. doi:, 10.1107/S2059798318009397. Epub 2018 Sep 3. PMID:30198899<ref>PMID:30198899</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4x5i" style="background-color:#fffaf0;"></div>

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

OCA at 21:13, 12 April 2023

OCA — Wed, 12 Apr 2023 21:13:43 GMT

←Older revision		Revision as of 21:13, 12 April 2023
Line 1:		Line 1:

	==ecDHFR complexed with folate and NADP+ at 660 MPa==		==ecDHFR complexed with folate and NADP+ at 660 MPa==
-	<StructureSection load='4x5i' size='340' side='right' caption='[[4x5i]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='4x5i' size='340' side='right'caption='[[4x5i]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4x5i]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5I OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4X5I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4x5i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X5I FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4x5f\|4x5f]], [[4x5g\|4x5g]], [[4x5h\|4x5h]], [[4x5j\|4x5j]]</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=4x5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5i OCA], [https://pdbe.org/4x5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x5i RCSB], [https://www.ebi.ac.uk/pdbsum/4x5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x5i ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">folA, tmrA, b0048, JW0047 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=4x5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5i OCA], [~~http~~://pdbe.org/4x5i PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4x5i RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4x5i PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4x5i ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.	+	[https://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 20:

	==See Also==		==See Also==
-	*[[Dihydrofolate reductase\|Dihydrofolate reductase]]	+	*[[Dihydrofolate reductase 3D structures\|Dihydrofolate reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Dihydrofolate reductase~~]]	+	[[Category: Escherichia coli K-12]]
-	[[Category: ~~Ecoli~~]]	+	[[Category: Large Structures]]
-	[[Category: Nagae, T]]	+	[[Category: Nagae T]]
-	[[Category: Watanabe, N]]	+	[[Category: Watanabe N]]
-	[[Category: Yamada, H]]	+	[[Category: Yamada H]]
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 20:03, 19 September 2018

OCA — Wed, 19 Sep 2018 20:03:42 GMT

←Older revision		Revision as of 20:03, 19 September 2018
Line 1:		Line 1:
		+
	==ecDHFR complexed with folate and NADP+ at 660 MPa==		==ecDHFR complexed with folate and NADP+ at 660 MPa==
	<StructureSection load='4x5i' size='340' side='right' caption='[[4x5i]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='4x5i' size='340' side='right' caption='[[4x5i]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4x5i]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X5I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4x5i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X5I FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4x5f\|4x5f]], [[4x5g\|4x5g]], [[4x5h\|4x5h]], [[4x5j\|4x5j]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4x5f\|4x5f]], [[4x5g\|4x5g]], [[4x5h\|4x5h]], [[4x5j\|4x5j]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">folA, tmrA, b0048, JW0047 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=4x5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5i OCA], [http://pdbe.org/4x5i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x5i RCSB], [http://www.ebi.ac.uk/pdbsum/4x5i 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=4x5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5i OCA], [http://pdbe.org/4x5i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x5i RCSB], [http://www.ebi.ac.uk/pdbsum/4x5i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x5i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.		[[http://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	A high-pressure crystallographic study was conducted on Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP(+) in crystal forms containing both the open and closed conformations of the M20 loop under high-pressure conditions of up to 800 MPa. At pressures between 270 and 500 MPa the crystal form containing the open conformation exhibited a phase transition from P21 to C2. Several structural changes in ecDHFR were observed at high pressure that were also accompanied by structural changes in the NADP(+) cofactor and the hydration structure. In the crystal form with the closed conformation the M20 loop moved as the pressure changed, with accompanying conformational changes around the active site, including NADP(+) and folate. These movements were consistent with the suggested hypothesis that movement of the M20 loop was necessary for ecDHFR to catalyze the reaction. In the crystal form with the open conformation the nicotinamide ring of the NADP(+) cofactor undergoes a large flip as an intermediate step in the reaction, despite being in a crystalline state. Furthermore, observation of the water molecules between Arg57 and folate elucidated an early step in the substrate-binding pathway. These results demonstrate the possibility of using high-pressure protein crystallography as a method to capture high-energy substates or transient structures related to the protein reaction cycle.
		+
		+	High-pressure protein crystal structure analysis of Escherichia coli dihydrofolate reductase complexed with folate and NADP().,Nagae T, Yamada H, Watanabe N Acta Crystallogr D Struct Biol. 2018 Sep 1;74(Pt 9):895-905. doi:, 10.1107/S2059798318009397. Epub 2018 Sep 3. PMID:30198899<ref>PMID:30198899</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4x5i" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Dihydrofolate reductase\|Dihydrofolate reductase]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Dihydrofolate reductase]]		[[Category: Dihydrofolate reductase]]
		+	[[Category: Ecoli]]
	[[Category: Nagae, T]]		[[Category: Nagae, T]]
	[[Category: Watanabe, N]]		[[Category: Watanabe, N]]
	[[Category: Yamada, H]]		[[Category: Yamada, H]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 20:22, 13 January 2016

OCA — Wed, 13 Jan 2016 20:22:01 GMT

←Older revision		Revision as of 20:22, 13 January 2016
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==ecDHFR complexed with folate and NADP+ at 660 MPa==
-		+	<StructureSection load='4x5i' size='340' side='right' caption='[[4x5i]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~The entry~~ 4x5i is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4x5i]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X5I FirstGlance]. <br>
-	~~Authors~~: ~~Yamada~~, H., ~~Watanabe~~, N., ~~Nagae~~, T.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4x5f\|4x5f]], [[4x5g\|4x5g]], [[4x5h\|4x5h]], [[4x5j\|4x5j]]</td></tr>
-	~~Description~~: ~~ecDHFR complexed with~~ folate and ~~NADP+ at 660 MPa~~	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span></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=4x5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x5i OCA], [http://pdbe.org/4x5i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x5i RCSB], [http://www.ebi.ac.uk/pdbsum/4x5i PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Dihydrofolate reductase]]
		+	[[Category: Nagae, T]]
	[[Category: Watanabe, N]]		[[Category: Watanabe, N]]
	[[Category: Yamada, H]]		[[Category: Yamada, H]]
-	[[Category: ~~Nagae, T~~]]	+	[[Category: Oxidoreductase]]

OCA at 23:05, 30 November 2015

OCA — Mon, 30 Nov 2015 23:05:12 GMT

←Older revision		Revision as of 23:05, 30 November 2015
Line 8:		Line 8:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Watanabe, N]]		[[Category: Watanabe, N]]
-	[[Category: Nagae, T]]
	[[Category: Yamada, H]]		[[Category: Yamada, H]]
		+	[[Category: Nagae, T]]

OCA at 13:47, 31 December 2014

OCA — Wed, 31 Dec 2014 13:47:42 GMT

←Older revision		Revision as of 13:47, 31 December 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4x5i is ON HOLD	+	The entry 4x5i is ON HOLD until Paper Publication

	Authors: Yamada, H., Watanabe, N., Nagae, T.		Authors: Yamada, H., Watanabe, N., Nagae, T.

OCA at 20:30, 24 December 2014

OCA — Wed, 24 Dec 2014 20:30:59 GMT

←Older revision		Revision as of 20:30, 24 December 2014
Line 6:		Line 6:

	Description: ecDHFR complexed with folate and NADP+ at 660 MPa		Description: ecDHFR complexed with folate and NADP+ at 660 MPa
		+	[[Category: Unreleased Structures]]
		+	[[Category: Watanabe, N]]
		+	[[Category: Nagae, T]]
		+	[[Category: Yamada, H]]

OCA: Protected "4x5i" [edit=sysop:move=sysop]

OCA — Wed, 10 Dec 2014 14:24:32 GMT

Protected "4x5i" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:24, 10 December 2014

OCA: New page: '''Unreleased structure''' The entry 4x5i is ON HOLD Authors: Yamada, H., Watanabe, N., Nagae, T. Description: ecDHFR complexed with folate and NADP+ at 660 MPa

OCA — Wed, 10 Dec 2014 14:24:31 GMT

New page: '''Unreleased structure''' The entry 4x5i is ON HOLD Authors: Yamada, H., Watanabe, N., Nagae, T. Description: ecDHFR complexed with folate and NADP+ at 660 MPa

New page

'''Unreleased structure'''

The entry 4x5i is ON HOLD

Authors: Yamada, H., Watanabe, N., Nagae, T.

Description: ecDHFR complexed with folate and NADP+ at 660 MPa