3DPA
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1L41
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3TIM
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3TMS
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1L48
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1L51
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1L60
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1L67
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4BP2
| CRYSTALLOGRAPHIC REFINEMENT OF BOVINE PRO-PHOSPHOLIPASE A2 AT 1.6 ANGSTROMS RESOLUTION | Descriptor: | (4S)-2-METHYL-2,4-PENTANEDIOL, CALCIUM ION, PHOSPHOLIPASE A2 | Authors: | Finzel, B.C, Weber, P.C, Ohlendorf, D.H, Salemme, F.R. | Deposit date: | 1990-09-07 | Release date: | 1991-10-15 | Last modified: | 2017-11-29 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Crystallographic refinement of bovine pro-phospholipase A2 at 1.6 A resolution. Acta Crystallogr.,Sect.B, 47, 1991
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1L74
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1L37
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1L56
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1SH1
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5RUB
| CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE FROM RHODOSPIRILLUM RUBRUM AT 1.7 ANGSTROMS RESOLUTION | Descriptor: | RUBISCO (RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE) | Authors: | Schneider, G, Lindqvist, Y, Lundqvist, T. | Deposit date: | 1990-05-29 | Release date: | 1991-10-15 | Last modified: | 2024-03-06 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7 A resolution. J.Mol.Biol., 211, 1990
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1L49
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1L54
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1L68
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1LAP
| MOLECULAR STRUCTURE OF LEUCINE AMINOPEPTIDASE AT 2.7-ANGSTROMS RESOLUTION | Descriptor: | Cytosol aminopeptidase, ZINC ION | Authors: | Burley, S.K, David, P.R, Taylor, A, Lipscomb, W.N. | Deposit date: | 1990-08-01 | Release date: | 1991-10-15 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.7 Å) | Cite: | Molecular structure of leucine aminopeptidase at 2.7-A resolution. Proc.Natl.Acad.Sci.USA, 87, 1990
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1L43
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1L61
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1L53
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1L66
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2GCT
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2TRX
| CRYSTAL STRUCTURE OF THIOREDOXIN FROM ESCHERICHIA COLI AT 1.68 ANGSTROMS RESOLUTION | Descriptor: | (4S)-2-METHYL-2,4-PENTANEDIOL, COPPER (II) ION, THIOREDOXIN | Authors: | Katti, S.K, Lemaster, D.M, Eklund, H. | Deposit date: | 1990-03-19 | Release date: | 1991-10-15 | Last modified: | 2017-11-29 | Method: | X-RAY DIFFRACTION (1.68 Å) | Cite: | Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution. J.Mol.Biol., 212, 1990
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1FXI
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