Atomistry » Chlorine » PDB 102l-161l
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Chlorine in PDB, part 1 (files: 1-40), PDB 102l-161l

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-161l).
  1. 102l (Cl: 2) - How Amino-Acid Insertions Are Allowed in An Alpha-Helix of T4 Lysozyme
  2. 103l (Cl: 2) - How Amino-Acid Insertions Are Allowed in An Alpha-Helix of T4 Lysozyme
  3. 107l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
  4. 108l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
  5. 109l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
  6. 110l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
  7. 111l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
  8. 112l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
  9. 113l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
  10. 114l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
  11. 115l (Cl: 2) - Structural Basis of Alpha-Helix Propensity at Two Sites in T4 Lysozyme
  12. 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
  13. 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
  14. 11gs (Cl: 4) - Glutathione S-Transferase Complexed with Ethacrynic Acid- Glutathione Conjugate (Form II)
  15. 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
  16. 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
  17. 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
  18. 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
  19. 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
  20. 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
  21. 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
  22. 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
  23. 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
  24. 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
  25. 138l (Cl: 2) - Rapid Crystallization of T4 Lysozyme By Intermolecular Disulfide Crosslinking
  26. 139l (Cl: 2) - Rapid Crystallization of T4 Lysozyme By Intermolecular Disulfide Crosslinking
  27. 140l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
  28. 141l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
  29. 142l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
  30. 143l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
  31. 144l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
  32. 146l (Cl: 2) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
  33. 147l (Cl: 1) - Role of Backbone Flexibility in the Accommodation of Variants That Repack the Core of T4 Lysozyme
  34. 155l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
  35. 156l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
  36. 157l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
  37. 158l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
  38. 159l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
  39. 160l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
  40. 161l (Cl: 2) - Control of Enzyme Activity By An Engineered Disulfide Bond
Page generated: Wed Nov 4 03:35:34 2020

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