5c6e - Revision history

OCA at 12:19, 6 March 2024

2024-03-06T12:19:07Z

←Older revision		Revision as of 12:19, 6 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5c6e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C6E FirstGlance]. <br>		<table><tr><td colspan='2'>[[5c6e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C6E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <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">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution\|Resolution]] 1.7Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <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=5c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6e OCA], [https://pdbe.org/5c6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c6e RCSB], [https://www.ebi.ac.uk/pdbsum/5c6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6e 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=5c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6e OCA], [https://pdbe.org/5c6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c6e RCSB], [https://www.ebi.ac.uk/pdbsum/5c6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE] Involved in oxygen transport from the lung to the various peripheral tissues.		[https://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE] Involved in oxygen transport from the lung to the various peripheral tissues.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Neutron crystallography provides direct visual evidence of the atomic positions of deuterium-exchanged H atoms, enabling the accurate determination of the protonation/deuteration state of hydrated biomolecules. Comparison of two neutron structures of hemoglobins, human deoxyhemoglobin (T state) and equine cyanomethemoglobin (R state), offers a direct observation of histidine residues that are likely to contribute to the Bohr effect. Previous studies have shown that the T-state N-terminal and C-terminal salt bridges appear to have a partial instead of a primary overall contribution. Four conserved histidine residues [alphaHis72(EF1), alphaHis103(G10), alphaHis89(FG1), alphaHis112(G19) and betaHis97(FG4)] can become protonated/deuterated from the R to the T state, while two histidine residues [alphaHis20(B1) and betaHis117(G19)] can lose a proton/deuteron. alphaHis103(G10), located in the alpha1:beta1 dimer interface, appears to be a Bohr group that undergoes structural changes: in the R state it is singly protonated/deuterated and hydrogen-bonded through a water network to betaAsn108(G10) and in the T state it is doubly protonated/deuterated with the network uncoupled. The very long-term H/D exchange of the amide protons identifies regions that are accessible to exchange as well as regions that are impermeable to exchange. The liganded relaxed state (R state) has comparable levels of exchange (17.1% non-exchanged) compared with the deoxy tense state (T state; 11.8% non-exchanged). Interestingly, the regions of non-exchanged protons shift from the tetramer interfaces in the T-state interface (alpha1:beta2 and alpha2:beta1) to the cores of the individual monomers and to the dimer interfaces (alpha1:beta1 and alpha2:beta2) in the R state. The comparison of regions of stability in the two states allows a visualization of the conservation of fold energy necessary for ligand binding and release.
-
-	Visualizing the Bohr effect in hemoglobin: neutron structure of equine cyanomethemoglobin in the R state and comparison with human deoxyhemoglobin in the T state.,Dajnowicz S, Seaver S, Hanson BL, Fisher SZ, Langan P, Kovalevsky AY, Mueser TC Acta Crystallogr D Struct Biol. 2016 Jul 1;72(Pt 7):892-903. doi:, 10.1107/S2059798316009049. Epub 2016 Jun 28. PMID:27377386<ref>PMID:27377386</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5c6e" style="background-color:#fffaf0;"></div>

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

OCA at 06:21, 7 June 2023

2023-06-07T06:21:40Z

←Older revision		Revision as of 06:21, 7 June 2023
Line 3:		Line 3:
	<StructureSection load='5c6e' size='340' side='right'caption='[[5c6e]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='5c6e' size='340' side='right'caption='[[5c6e]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5c6e]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5C6E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5c6e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C6E FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5c8i\|5c8i]], [[5ccd\|5ccd]]~~</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=5c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6e OCA], [https://pdbe.org/5c6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c6e RCSB], [https://www.ebi.ac.uk/pdbsum/5c6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6e 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=5c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6e OCA], [~~http~~://pdbe.org/5c6e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5c6e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5c6e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6e ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE~~]] Involved in oxygen transport from the lung to the various peripheral tissues. [[http://www.uniprot.org/uniprot/HBB_HORSE HBB_HORSE]~~] Involved in oxygen transport from the lung to the various peripheral tissues.	+	[https://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE] Involved in oxygen transport from the lung to the various peripheral tissues.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 28:		Line 27:
	[[Category: Equus caballus]]		[[Category: Equus caballus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dajnowicz, S]]	+	[[Category: Dajnowicz S]]
-	[[Category: Fisher~~, S Z~~]]	+	[[Category: Fisher SZ]]
-	[[Category: Hanson~~, B L~~]]	+	[[Category: Hanson BL]]
-	[[Category: Kovalevsky~~, A Y~~]]	+	[[Category: Kovalevsky AY]]
-	[[Category: Langan, P]]	+	[[Category: Langan P]]
-	[[Category: Mueser~~, T C~~]]	+	[[Category: Mueser TC]]
-	[[Category: Sean, S]]	+	[[Category: Sean S]]
-	~~[[Category: Equine hemoglobin]]~~	+
-	~~[[Category: Oxygen transport]]~~	+
-	~~[[Category: R-state~~]]	+

OCA at 07:27, 27 November 2019

2019-11-27T07:27:07Z

←Older revision		Revision as of 07:27, 27 November 2019
Line 1:		Line 1:

	==Joint X-ray/neutron structure of equine cyanomet hemoglobin in R state==		==Joint X-ray/neutron structure of equine cyanomet hemoglobin in R state==
-	<StructureSection load='5c6e' size='340' side='right' caption='[[5c6e]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='5c6e' size='340' side='right'caption='[[5c6e]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5c6e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C6E FirstGlance]. <br>		<table><tr><td colspan='2'>[[5c6e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C6E FirstGlance]. <br>
Line 27:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Equus caballus]]		[[Category: Equus caballus]]
		+	[[Category: Large Structures]]
	[[Category: Dajnowicz, S]]		[[Category: Dajnowicz, S]]
	[[Category: Fisher, S Z]]		[[Category: Fisher, S Z]]

OCA at 04:26, 21 September 2017

2017-09-21T04:26:52Z

←Older revision		Revision as of 04:26, 21 September 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5c6e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5c6e" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Hemoglobin 3D structures\|Hemoglobin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:55, 14 July 2016

2016-07-14T11:55:13Z

←Older revision		Revision as of 11:55, 14 July 2016
Line 12:		Line 12:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
-	X-~~ray and neutron crystallographic techniques provide complementary information on~~ the ~~structure~~ and ~~function~~ of ~~biological macromolecules~~. X-~~ray~~ and ~~neutron~~ (XN) ~~crystallographic data have been combined~~ in a ~~joint structure-refinement procedure~~ that ~~has been developed using recent advances~~ in ~~modern computational methodologies, including cross~~-~~validated maximum-likelihood target functions~~ with ~~gradient~~-~~based optimization and simulated annealing~~. The ~~XN approach for complete~~ (~~including hydrogen~~) ~~macromolecular structure analysis provides more accurate and complete structures~~, ~~as demonstrated for diisopropyl fluorophosphatase, photoactive yellow protein~~ and ~~human aldose reductase~~. ~~Furthermore, this method has several practical advantages, including~~ the ~~easier determination~~ of the ~~orientation~~ of ~~water molecules, hydroxyl groups~~ and ~~some amino-acid side chains~~.	+	Neutron crystallography provides direct visual evidence of the atomic positions of deuterium-exchanged H atoms, enabling the accurate determination of the protonation/deuteration state of hydrated biomolecules. Comparison of two neutron structures of hemoglobins, human deoxyhemoglobin (T state) and equine cyanomethemoglobin (R state), offers a direct observation of histidine residues that are likely to contribute to the Bohr effect. Previous studies have shown that the T-state N-terminal and C-terminal salt bridges appear to have a partial instead of a primary overall contribution. Four conserved histidine residues [alphaHis72(EF1), alphaHis103(G10), alphaHis89(FG1), alphaHis112(G19) and betaHis97(FG4)] can become protonated/deuterated from the R to the T state, while two histidine residues [alphaHis20(B1) and betaHis117(G19)] can lose a proton/deuteron. alphaHis103(G10), located in the alpha1:beta1 dimer interface, appears to be a Bohr group that undergoes structural changes: in the R state it is singly protonated/deuterated and hydrogen-bonded through a water network to betaAsn108(G10) and in the T state it is doubly protonated/deuterated with the network uncoupled. The very long-term H/D exchange of the amide protons identifies regions that are accessible to exchange as well as regions that are impermeable to exchange. The liganded relaxed state (R state) has comparable levels of exchange (17.1% non-exchanged) compared with the deoxy tense state (T state; 11.8% non-exchanged). Interestingly, the regions of non-exchanged protons shift from the tetramer interfaces in the T-state interface (alpha1:beta2 and alpha2:beta1) to the cores of the individual monomers and to the dimer interfaces (alpha1:beta1 and alpha2:beta2) in the R state. The comparison of regions of stability in the two states allows a visualization of the conservation of fold energy necessary for ligand binding and release.

-	~~Generalized X-ray and~~ neutron ~~crystallographic analysis: more accurate~~ and ~~complete structures for biological macromolecules~~.,~~Adams PD~~, ~~Mustyakimov M~~, ~~Afonine PV~~, Langan P Acta Crystallogr D Biol ~~Crystallogr~~. ~~2009 Jun~~;65(Pt 6):~~567~~-73. doi:, 10.1107/~~S0907444909011548~~. Epub ~~2009 May 15~~. PMID:~~19465771~~<ref>PMID:~~19465771~~</ref>	+	Visualizing the Bohr effect in hemoglobin: neutron structure of equine cyanomethemoglobin in the R state and comparison with human deoxyhemoglobin in the T state.,Dajnowicz S, Seaver S, Hanson BL, Fisher SZ, Langan P, Kovalevsky AY, Mueser TC Acta Crystallogr D Struct Biol. 2016 Jul 1;72(Pt 7):892-903. doi:, 10.1107/S2059798316009049. Epub 2016 Jun 28. PMID:27377386<ref>PMID:27377386</ref>

	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

OCA at 02:23, 13 July 2016

2016-07-13T02:23:52Z

←Older revision		Revision as of 02:23, 13 July 2016
Line 6:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5c8i\|5c8i]], [[5ccd\|5ccd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5c8i\|5c8i]], [[5ccd\|5ccd]]</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=5c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6e OCA], [http://pdbe.org/5c6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6e RCSB], [http://www.ebi.ac.uk/pdbsum/5c6e 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=5c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6e OCA], [http://pdbe.org/5c6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6e RCSB], [http://www.ebi.ac.uk/pdbsum/5c6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 23:14, 23 June 2016

2016-06-23T23:14:57Z

←Older revision		Revision as of 23:14, 23 June 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5c6e is ~~ON HOLD until Paper~~ Publication	+	==Joint X-ray/neutron structure of equine cyanomet hemoglobin in R state==
		+	<StructureSection load='5c6e' size='340' side='right' caption='[[5c6e]], [[Resolution\|resolution]] 1.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5c6e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C6E FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5c8i\|5c8i]], [[5ccd\|5ccd]]</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=5c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6e OCA], [http://pdbe.org/5c6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6e RCSB], [http://www.ebi.ac.uk/pdbsum/5c6e PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues. [[http://www.uniprot.org/uniprot/HBB_HORSE HBB_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	X-ray and neutron crystallographic techniques provide complementary information on the structure and function of biological macromolecules. X-ray and neutron (XN) crystallographic data have been combined in a joint structure-refinement procedure that has been developed using recent advances in modern computational methodologies, including cross-validated maximum-likelihood target functions with gradient-based optimization and simulated annealing. The XN approach for complete (including hydrogen) macromolecular structure analysis provides more accurate and complete structures, as demonstrated for diisopropyl fluorophosphatase, photoactive yellow protein and human aldose reductase. Furthermore, this method has several practical advantages, including the easier determination of the orientation of water molecules, hydroxyl groups and some amino-acid side chains.

-	~~Authors~~: ~~Dajnowicz, S~~., ~~Sean~~, S., ~~Hanson, B.L., Fisher, S.Z.~~, Langan, P., ~~Kovalevsky, A~~.Y.~~, Mueser, T.C~~.	+	Generalized X-ray and neutron crystallographic analysis: more accurate and complete structures for biological macromolecules.,Adams PD, Mustyakimov M, Afonine PV, Langan P Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):567-73. doi:, 10.1107/S0907444909011548. Epub 2009 May 15. PMID:19465771<ref>PMID:19465771</ref>

-	~~Description: Joint X-ray~~/~~neutron structure~~ of ~~equine cyanomet hemoglobin in R state~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5c6e" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Equus caballus]]
	[[Category: Dajnowicz, S]]		[[Category: Dajnowicz, S]]
-	~~[[Category: Kovalevsky, A.Y]]~~	+	[[Category: Fisher, S Z]]
-	[[Category: Fisher, S.Z]]	+	[[Category: Hanson, B L]]
-	[[Category: ~~Sean~~, S]]	+	[[Category: Kovalevsky, A Y]]
-	[[Category: ~~Mueser~~, ~~T.C~~]]	+
	[[Category: Langan, P]]		[[Category: Langan, P]]
-	[[Category: ~~Hanson~~, ~~B.L~~]]	+	[[Category: Mueser, T C]]
		+	[[Category: Sean, S]]
		+	[[Category: Equine hemoglobin]]
		+	[[Category: Oxygen transport]]
		+	[[Category: R-state]]

OCA at 09:18, 2 March 2016

2016-03-02T09:18:50Z

←Older revision		Revision as of 09:18, 2 March 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5c6e is ON HOLD	+	The entry 5c6e is ON HOLD until Paper Publication

	Authors: Dajnowicz, S., Sean, S., Hanson, B.L., Fisher, S.Z., Langan, P., Kovalevsky, A.Y., Mueser, T.C.		Authors: Dajnowicz, S., Sean, S., Hanson, B.L., Fisher, S.Z., Langan, P., Kovalevsky, A.Y., Mueser, T.C.

OCA at 10:22, 16 December 2015

2015-12-16T10:22:15Z

←Older revision		Revision as of 10:22, 16 December 2015
Line 7:		Line 7:
	Description: Joint X-ray/neutron structure of equine cyanomet hemoglobin in R state		Description: Joint X-ray/neutron structure of equine cyanomet hemoglobin in R state
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Dajnowicz, S]]
	[[Category: Kovalevsky, A.Y]]		[[Category: Kovalevsky, A.Y]]
		+	[[Category: Fisher, S.Z]]
	[[Category: Sean, S]]		[[Category: Sean, S]]
	[[Category: Mueser, T.C]]		[[Category: Mueser, T.C]]
-	[[Category: Hanson, B.L]]
-	[[Category: Dajnowicz, S]]
-	[[Category: Fisher, S.Z]]
	[[Category: Langan, P]]		[[Category: Langan, P]]
		+	[[Category: Hanson, B.L]]

OCA at 18:15, 5 August 2015

2015-08-05T18:15:42Z

←Older revision		Revision as of 18:15, 5 August 2015
Line 3:		Line 3:
	The entry 5c6e is ON HOLD		The entry 5c6e is ON HOLD

-	Authors: Dajnowicz, S, Sean, S, Hanson, B.L., Fisher, S.Z., Langan, P, Kovalevsky, A.Y., Mueser, T.C.	+	Authors: Dajnowicz, S., Sean, S., Hanson, B.L., Fisher, S.Z., Langan, P., Kovalevsky, A.Y., Mueser, T.C.

-	Description: ""Joint X-ray/neutron structure of equine cyanomet hemoglobin in R state""	+	Description: Joint X-ray/neutron structure of equine cyanomet hemoglobin in R state
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Langan, P,~~ Kovalevsky, A.Y]]	+	[[Category: Kovalevsky, A.Y]]
-	[[Category: ~~Dajnowicz, S,~~ Sean, S~~, Hanson, B.L~~]]	+	[[Category: Sean, S]]
	[[Category: Mueser, T.C]]		[[Category: Mueser, T.C]]
		+	[[Category: Hanson, B.L]]
		+	[[Category: Dajnowicz, S]]
	[[Category: Fisher, S.Z]]		[[Category: Fisher, S.Z]]
		+	[[Category: Langan, P]]