Search Results -- Motif search

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-- Showing result chains 1 to 25 (of 985 total) -- next >>
107l
Resolution: 1.8 Å
Title
Structural basis of alpha-helix propensity at two sites in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
107lA
108l
Resolution: 1.8 Å
Title
Structural basis of alpha-helix propensity at two sites in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
108lA
109l
Resolution: 1.85 Å
Title
Structural basis of alpha-helix propensity at two sites in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
109lA
110l
Resolution: 1.7 Å
Title
Structural basis of alpha-helix propensity at two sites in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
110lA
111l
Resolution: 1.8 Å
Title
Structural basis of alpha-helix propensity at two sites in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
111lA
112l
Resolution: 1.8 Å
Title
Structural basis of alpha-helix propensity at two sites in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
112lA
113l
Resolution: 1.8 Å
Title
Structural basis of alpha-helix propensity at two sites in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
113lA
114l
Resolution: 1.8 Å
Title
Structural basis of alpha-helix propensity at two sites in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
114lA
115l
Resolution: 1.8 Å
Title
Structural basis of alpha-helix propensity at two sites in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
115lA
118l
Resolution: 1.8 Å
Title
The energetic cost and the structural consequences of burying a hydroxyl group within the core of a protein determined from ala to ser and val to thr substitutions in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
118lA
119l
Resolution: 1.65 Å
Title
The energetic cost and the structural consequences of burying a hydroxyl group within the core of a protein determined from ala to ser and val to thr substitutions in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
119lA
120l
Resolution: 1.8 Å
Title
The energetic cost and the structural consequences of burying a hydroxyl group within the core of a protein determined from ala to ser and val to thr substitutions in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
120lA
122l
Resolution: 1.8 Å
Title
The energetic cost and the structural consequences of burying a hydroxyl group within the core of a protein determined from ala to ser and val to thr substitutions in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
122lA
123l
Resolution: 1.8 Å
Title
The energetic cost and the structural consequences of burying a hydroxyl group within the core of a protein determined from ala to ser and val to thr substitutions in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
123lA
125l
Resolution: 1.85 Å
Title
The energetic cost and the structural consequences of burying a hydroxyl group within the core of a protein determined from ala to ser and val to thr substitutions in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
125lA
126l
Resolution: 1.8 Å
Title
The energetic cost and the structural consequences of burying a hydroxyl group within the core of a protein determined from ala to ser and val to thr substitutions in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
126lA
127l
Resolution: 1.85 Å
Title
The energetic cost and the structural consequences of burying a hydroxyl group within the core of a protein determined from ala to ser and val to thr substitutions in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
127lA
128l
Resolution: 1.7 Å
Title
The energetic cost and the structural consequences of burying a hydroxyl group within the core of a protein determined from ala to ser and val to thr substitutions in t4 lysozyme
Classification
Hydrolase(o-glycosyl)
Chain A
128lA
129l
Resolution: 1.7 Å
Title
Structures of randomly generated mutants of t4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent
Classification
Hydrolase(o-glycosyl)
Chain A
129lA
130l
Resolution: 1.7 Å
Title
Structures of randomly generated mutants of t4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent
Classification
Hydrolase(o-glycosyl)
Chain A
130lA
131l
Resolution: 1.7 Å
Title
Structures of randomly generated mutants of t4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent
Classification
Hydrolase(o-glycosyl)
Chain A
131lA
137l
Resolution: 1.85 Å
Title
Structural basis of amino acid alpha helix propensity
Classification
Hydrolase(o-glycosyl)
Chain A
137lA
Chain B
137lB
138l
Resolution: 1.7 Å
Title
Rapid crystallization of t4 lysozyme by intermolecular disulfide crosslinking
Classification
Hydrolase(o-glycosyl)
Chain A
138lA
139l
Resolution: 1.7 Å
Title
Rapid crystallization of t4 lysozyme by intermolecular disulfide crosslinking
Classification
Hydrolase(o-glycosyl)
Chain A
139lA