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1HBS
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BU of 1hbs by Molmil
REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION
分子名称: HEMOGLOBIN S (DEOXY) (ALPHA CHAIN), HEMOGLOBIN S (DEOXY) (BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE
著者Padlan, E.A, Love, W.E.
登録日1982-06-02
公開日1982-07-29
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (3 Å)
主引用文献Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-A resolution.
J.Biol.Chem., 260, 1985
2LHB
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REFINEMENT OF A MOLECULAR MODEL FOR LAMPREY HEMOGLOBIN FROM PETROMYZON MARINUS
分子名称: CYANIDE ION, HEMOGLOBIN V (CYANO MET), PROTOPORPHYRIN IX CONTAINING FE
著者Honzatko, R.B, Hendrickson, W.A, Love, W.E.
登録日1985-08-16
公開日1986-01-21
最終更新日2024-02-21
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献Refinement of a molecular model for lamprey hemoglobin from Petromyzon marinus.
J.Mol.Biol., 184, 1985
1HBG
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GLYCERA DIBRANCHIATA HEMOGLOBIN. STRUCTURE AND REFINEMENT AT 1.5 ANGSTROMS RESOLUTION
分子名称: CARBON MONOXIDE, HEMOGLOBIN (CARBONMONOXY), PROTOPORPHYRIN IX CONTAINING FE
著者Arents, G.A, Braden, B.C, Padlan, E.A, Love, W.E.
登録日1991-02-11
公開日1992-07-15
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (1.5 Å)
主引用文献Glycera dibranchiata hemoglobin. Structure and refinement at 1.5 A resolution.
J.Mol.Biol., 210, 1989
2HBG
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GLYCERA DIBRANCHIATA HEMOGLOBIN. STRUCTURE AND REFINEMENT AT 1.5 ANGSTROMS RESOLUTION
分子名称: HEMOGLOBIN (DEOXY), PROTOPORPHYRIN IX CONTAINING FE
著者Arents, G.A, Love, W.E.
登録日1991-02-11
公開日1992-07-15
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.5 Å)
主引用文献Glycera dibranchiata hemoglobin. Structure and refinement at 1.5 A resolution.
J.Mol.Biol., 210, 1989
2HBS
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THE HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S
分子名称: HEMOGLOBIN S (DEOXY), ALPHA CHAIN, BETA CHAIN, ...
著者Harrington, D.J, Adachi, K, Royer Junior, W.E.
登録日1997-05-06
公開日1997-07-23
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (2.05 Å)
主引用文献The high resolution crystal structure of deoxyhemoglobin S.
J.Mol.Biol., 272, 1997
3LHB
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THE 2.7 ANGSTROM CRYSTAL STRUCTURE OF DEOXYGENATED HEMOGLOBIN FROM THE SEA LAMPREY (PETROMYZON MARINUS)
分子名称: PROTEIN (HEMOGLOBIN), PROTOPORPHYRIN IX CONTAINING FE
著者Heaslet, H.A, Royer Jr, W.E.
登録日1999-01-12
公開日1999-01-20
最終更新日2023-09-06
実験手法X-RAY DIFFRACTION (2.7 Å)
主引用文献The 2.7 A crystal structure of deoxygenated hemoglobin from the sea lamprey (Petromyzon marinus): structural basis for a lowered oxygen affinity and Bohr effect.
Structure Fold.Des., 7, 1999
2HIO
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HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN
分子名称: PROTEIN (HISTONE H2A), PROTEIN (HISTONE H2B), PROTEIN (HISTONE H3), ...
著者Arents, G, Moudrianakis, E.N.
登録日1999-06-15
公開日2000-01-12
最終更新日2023-12-27
実験手法X-RAY DIFFRACTION (3.1 Å)
主引用文献The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.
Proc.Natl.Acad.Sci.USA, 88, 1991
1HIO
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HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN, ALPHA CARBONS ONLY
分子名称: HISTONE H2A, HISTONE H2B, HISTONE H3, ...
著者Arents, G, Moudrianakis, E.N.
登録日1991-09-19
公開日1998-11-25
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (3.1 Å)
主引用文献The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.
Proc.Natl.Acad.Sci.USA, 88, 1991
1MYT
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CRYSTAL STRUCTURE TO 1.74 ANGSTROMS RESOLUTION OF METMYOGLOBIN FROM YELLOWFIN TUNA (THUNNUS ALBACARES): AN EXAMPLE OF A MYOGLOBIN LACKING THE D HELIX
分子名称: MYOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE
著者Birnbaum, G.I, Evans, S.V, Przybylska, M, Rose, D.R.
登録日1991-05-06
公開日1993-10-31
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.74 Å)
主引用文献1.70 A resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix.
Acta Crystallogr.,Sect.D, 50, 1994
1OXY
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CRYSTALLOGRAPHIC ANALYSIS OF OXYGENATED AND DEOXYGENATED STATES OF ARTHROPOD HEMOCYANIN SHOWS UNUSUAL DIFFERENCES
分子名称: COPPER (II) ION, HEMOCYANIN (SUBUNIT TYPE II), OXYGEN MOLECULE
著者Ton-that, H, Magnus, K.
登録日1995-01-06
公開日1995-02-27
最終更新日2024-06-05
実験手法X-RAY DIFFRACTION (2.4 Å)
主引用文献Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences.
Proteins, 19, 1994

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