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1RDI
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BU of 1rdi by Molmil
MANNOSE-BINDING PROTEIN, SUBTILISIN DIGEST FRAGMENT COMPLEX WITH ALPHA-METHYL-L-FUCOPYRANOSIDE
Descriptor: CALCIUM ION, CHLORIDE ION, MANNOSE-BINDING PROTEIN-C, ...
Authors:Ng, K.K.-S, Drickamer, K, Weis, W.I.
Deposit date:1995-09-05
Release date:1996-03-08
Last modified:2020-07-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural analysis of monosaccharide recognition by rat liver mannose-binding protein.
J.Biol.Chem., 271, 1996
1CBY
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BU of 1cby by Molmil
DELTA-ENDOTOXIN
Descriptor: DELTA-ENDOTOXIN CYTB
Authors:Li, J.
Deposit date:1995-09-05
Release date:1996-10-14
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.6 Å)
Cite:Structure of the mosquitocidal delta-endotoxin CytB from Bacillus thuringiensis sp. kyushuensis and implications for membrane pore formation.
J.Mol.Biol., 257, 1996
1RNG
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BU of 1rng by Molmil
SOLUTION STRUCTURE OF THE CUUG HAIRPIN: A NOVEL RNA TETRALOOP MOTIF
Descriptor: RNA (5'-R(*GP*GP*CP*GP*CP*UP*UP*GP*CP*GP*UP*C)-3')
Authors:Jucker, F.M, Pardi, A.
Deposit date:1995-09-05
Release date:1995-12-07
Last modified:2024-05-22
Method:SOLUTION NMR
Cite:Solution structure of the CUUG hairpin loop: a novel RNA tetraloop motif.
Biochemistry, 34, 1995
232D
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BU of 232d by Molmil
THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE DNA DECAMER D(AGGCATGCCT)
Descriptor: COBALT HEXAMMINE(III), DNA (5'-D(*AP*GP*GP*CP*AP*TP*GP*CP*CP*T)-3')
Authors:Nunn, C.M, Neidle, S.
Deposit date:1995-09-05
Release date:1996-03-22
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.3 Å)
Cite:The high resolution crystal structure of the DNA decamer d(AGGCATGCCT).
J.Mol.Biol., 256, 1996
1ANJ
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BU of 1anj by Molmil
ALKALINE PHOSPHATASE (K328H)
Descriptor: ALKALINE PHOSPHATASE, PHOSPHATE ION, ZINC ION
Authors:Murphy, J.E, Tibbitts, T.T, Kantrowitz, E.R.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases.
J.Mol.Biol., 253, 1995
1ANI
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BU of 1ani by Molmil
ALKALINE PHOSPHATASE (D153H, K328H)
Descriptor: ALKALINE PHOSPHATASE, PHOSPHATE ION, ZINC ION
Authors:Murphy, J.E, Tibbitts, T.T, Kantrowitz, E.R.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases.
J.Mol.Biol., 253, 1995
1GBD
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BU of 1gbd by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBF
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BU of 1gbf by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.15 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1CWD
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BU of 1cwd by Molmil
HUMAN P56LCK TYROSINE KINASE COMPLEXED WITH PHOSPHOPEPTIDE
Descriptor: (PHOSPHONOMETHYL)PHENYLALANINE-CONTAINING PEPTIDE PRO-GLU-GLY-ASP-PM3-GLU-GLU-VAL-LEU, P56LCK TYROSINE KINASE
Authors:Mikol, V.
Deposit date:1995-09-06
Release date:1996-12-07
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.25 Å)
Cite:The crystal structures of the SH2 domain of p56lck complexed with two phosphopeptides suggest a gated peptide binding site.
J.Mol.Biol., 246, 1995
1CWC
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BU of 1cwc by Molmil
IMPROVED BINDING AFFINITY FOR CYCLOPHILIN A BY A CYCLOSPORIN DERIVATIVE SINGLY MODIFIED AT ITS EFFECTOR DOMAIN
Descriptor: CYCLOSPORIN A, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A
Authors:Mikol, V.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (1.86 Å)
Cite:Improved Binding Affinity for Cyclophilin a by a Cyclosporin Derivative Singly Modified at its Effector Domain.
J.Med.Chem., 37, 1994
1CWE
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BU of 1cwe by Molmil
HUMAN P56LCK TYROSINE KINASE COMPLEXED WITH PHOSPHOPEPTIDE
Descriptor: P56LCK TYROSINE KINASE, PHOSPHOPEPTIDE ACQ-PMP-GLU-GLU-ILE-PRO
Authors:Mikol, V.
Deposit date:1995-09-06
Release date:1996-12-07
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:The crystal structures of the SH2 domain of p56lck complexed with two phosphopeptides suggest a gated peptide binding site.
J.Mol.Biol., 246, 1995
1CWA
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BU of 1cwa by Molmil
X-RAY STRUCTURE OF A MONOMERIC CYCLOPHILIN A-CYCLOSPORIN A CRYSTAL COMPLEX AT 2.1 ANGSTROMS RESOLUTION
Descriptor: CYCLOSPORIN A, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A
Authors:Mikol, V, Kallen, J, Walkinshaw, M.D.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:X-Ray Structure of a Monomeric Cyclophilin A-Cyclosporin a Crystal Complex at 2.1 A Resolution.
J.Mol.Biol., 234, 1993
1GBL
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BU of 1gbl by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.15 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBI
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BU of 1gbi by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBJ
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BU of 1gbj by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA
Descriptor: ALPHA-LYTIC PROTEASE, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBC
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BU of 1gbc by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBH
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BU of 1gbh by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBE
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BU of 1gbe by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU
Descriptor: ALPHA-LYTIC PROTEASE, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1FVL
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BU of 1fvl by Molmil
THE NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF FLAVORIDIN, AN ANTAGONIST OF THE PLATELET GP IIB-IIIA RECEPTOR
Descriptor: FLAVORIDIN
Authors:Senn, H, Klaus, W.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2022-02-23
Method:SOLUTION NMR
Cite:The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP IIb-IIIa receptor.
J.Mol.Biol., 232, 1993
2ANH
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BU of 2anh by Molmil
ALKALINE PHOSPHATASE (D153H)
Descriptor: ALKALINE PHOSPHATASE, PHOSPHATE ION, ZINC ION
Authors:Murphy, J.E, Tibbitts, T.T, Kantrowitz, E.R.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases.
J.Mol.Biol., 253, 1995
1GBK
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BU of 1gbk by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.13 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBB
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BU of 1gbb by Molmil
Alpha-lytic protease with met 190 replaced by ALA AND GLY 216 replaced by ALA complex with METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-ALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.15 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1GBM
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BU of 1gbm by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID
Descriptor: ALPHA-LYTIC PROTEASE, METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.28 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995
1CWB
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BU of 1cwb by Molmil
THE X-RAY STRUCTURE OF (MEBM2T)1-CYCLOSPORIN COMPLEXED WITH CYCLOPHILIN A PROVIDES AN EXPLANATION FOR ITS ANOMALOUSLY HIGH IMMUNOSUPPRESSIVE ACTIVITY
Descriptor: CYCLOSPORIN A, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A
Authors:Mikol, V, Kallen, J, Walkinshaw, M.D.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2024-06-05
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:The X-Ray Structure of (Mebm2T)1-Cyclosporin Complexed with Cyclophilin a Provides an Explanation for its Anomalously High Immunosuppressive Activity.
Protein Eng., 7, 1994
1GBA
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BU of 1gba by Molmil
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA
Descriptor: ALPHA-LYTIC PROTEASE, SULFATE ION
Authors:Mace, J.E, Agard, D.A.
Deposit date:1995-09-06
Release date:1996-01-29
Last modified:2021-11-03
Method:X-RAY DIFFRACTION (2.15 Å)
Cite:Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
J.Mol.Biol., 254, 1995

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