Chlorine in PDB, part 1 (files: 1-40),
PDB 102l-159l
Experimental structures of coordination spheres of Chlorine (Cl) in bioorganic
molecules from X-Ray and NMR experiments. Coordination spheres were calculated with 5.0 Angstroms radius
around Chlorine atoms. PDB files: 1-40 (PDB 102l-159l).
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102l (Cl: 2) - How Amino-Acid Insertions Are Allowed in An Alpha-Helix of T4 Lysozyme
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103l (Cl: 2) - How Amino-Acid Insertions Are Allowed in An Alpha-Helix of T4 Lysozyme
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107l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
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108l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
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109l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
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110l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
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111l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
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112l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
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113l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
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114l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
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115l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
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118l (Cl: 2) - 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
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119l (Cl: 2) - 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
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11gs (Cl: 4) - Glutathione S-Transferase Complexed with Ethacrynic Acid- Glutathione Conjugate (Form II)
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120l (Cl: 2) - 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
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122l (Cl: 2) - 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
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123l (Cl: 2) - 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
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125l (Cl: 2) - 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
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126l (Cl: 2) - 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
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127l (Cl: 3) - 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
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128l (Cl: 1) - 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
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129l (Cl: 2) - 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
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130l (Cl: 2) - 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
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131l (Cl: 2) - 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
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138l (Cl: 2) - Rapid Crystallization of T4 Lysozyme By Intermolecular Disulfide Crosslinking
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139l (Cl: 2) - Rapid Crystallization of T4 Lysozyme By Intermolecular Disulfide Crosslinking
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13sl (Cl: 4) - Pandda Analysis Group Deposition -- Idol Ring Domain in Complex with Z275151340
Other atoms:
Zn (8);
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13sm (Cl: 2) - Pandda Analysis Group Deposition -- Idol Ring Domain in Complex with Z275179946
Other atoms:
Zn (8);
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140l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
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141l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
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142l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
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143l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
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144l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
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146l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
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147l (Cl: 1) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
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155l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
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156l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
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157l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
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158l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
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159l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
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