BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB and PDB entries for Lysozyme
Introduction Mechanism Sequence Details BMRB and PDB entries Bibliography

BMRB entries with matching PDB entry

  • BMRB 1093 - PDB 1E8L - Sequential 1H NMR Assignments and Secondary Structure of Hen Egg White Lysozyme in Solution
  • BMRB 4751 - PDB 1IVM - Assignment of 1H and 15N resonances of mouse lysozyme
  • BMRB 4876 - PDB 1I56 - 1H,13C,15N assignment of Ca2+-bound state of Canine Milk Lysozyme at 30deg
  • BMRB 4883 - PDB 1I56 - H,15N assignment of Ca2+-free state of Canine Milk Lysozyme at 20deg
  • BMRB 5130 - PDB 1IY3 - Assignment of 1H, 13C and 15N resonances of Human Lysozyme at 35 C
  • BMRB 5142 - PDB 1IY3 - Assignment of 1H, 13C and 15N resonances of Human Lysozyme at 4 C
  • BMRB 6622 - PDB 1E8L - Backbone 1H, 13C, and 15N Chemical Shift Assignments for HEWL-SMe

BMRB entries for Lysozyme

  • 76 - Assignment of resonances in the 1H NMR spectrum of human lysozyme
  • 568 - Applications of Natural-Abundance Carbon-13 NMR to Studies of Proteins and Glycoproteins
  • 569 - A Structural Study of the Hydrophobic Box Region of Lysozyme in Solution Using Nuclear Overhauser Effects
  • 791 - Proton NMR Detection of Long-Range Heteronuclear Multiquantum Coherences in Proteins: The Complete Assignment of the Quaternary Aromatic 13C Shifts in Lysozyme
  • 887 - pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme
  • 888 - pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme
  • 915 - Assignment of the Backbone 1H and 15N NMR Resonances of Bacteriophage T4 Lysozyme
  • 1104 - Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy
  • 1105 - Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy
  • 1650 - Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme
  • 1651 - Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme
  • 1653 - Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme
  • 1669 - A structural study of calcium-binding equine lysozome by two-dimensional 1H-NMR
  • 1770 - 1H-NMR Study of the Intramolecular Interaction of a Substrate Analogue Covalently Attached to Aspartic Acid-101 in Lysozyme
  • 1771 - 1H-NMR Study of the Intramolecular Interaction of a Substrate Analogue Covalently Attached to Aspartic Acid-101 in Lysozyme
  • 1772 - 1H-NMR Study of the Intramolecular Interaction of a Substrate Analogue Covalently Attached to Aspartic Acid-101 in Lysozyme
  • 1773 - 1H-NMR Study of the Intramolecular Interaction of a Substrate Analogue Covalently Attached to Aspartic Acid-101 in Lysozyme
  • 1798 - Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state
  • 1799 - Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state
  • 1800 - Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state
  • 1801 - Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state
  • 1802 - Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state
  • 1803 - Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state
  • 1865 - Studies of Individual Carbon Sites of Hen Egg White Lysozyme by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy
  • 1881 - Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme
  • 1882 - Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme
  • 1883 - Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme
  • 1884 - Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme
  • 1975 - N.m.r. study of conformational changes in lysozyme around the thermal transition point
  • 1977 - N.m.r. study of conformational changes in lysozyme around the thermal transition point
  • 2231 - Preparation of a Lysozyme Derivative in Which Two Domains Are Cross-Linked Intramolecularly between Trp62 and Asp101
  • 2232 - Preparation of a Lysozyme Derivative in Which Two Domains Are Cross-Linked Intramolecularly between Trp62 and Asp101
  • 2446 - Studies of beta-Sheet Structure in Lysozyme by Proton Nuclear Magnetic Resonance. Assignments and Analysis of Spin-Spin Coupling Constants
  • 2542 - 1H and 15N NMR Study of Human Lysozyme
  • 2786 - Complete Assignment of Aromatic 1H Nuclear Magnetic Resonances of the Tyrosine Residues of Hen Lysozyme
  • 2858 - Comparisons of Ring-Current Shifts Calculated from the Crystal Structure of Egg White Lysozyme of Hen with the Proton Nuclear Magnetic Resonance Spectrum of Lysozyme in Solution
  • 2917 - Study of Tryptophan Residues of Lysozyme Using 1H Nuclear Magnetic Resonance
  • 2957 - Complete Assignment of the 1H NMR Spectrum of the Aromatic Residues of Lysozyme
  • 3441 - 1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme
  • 4562 - 1H and 13C chemical shift assignments of native hen egg white lysozyme
  • 4831 - Backbone 1H, 13C, and 15N Chemical Shift Assignments for Lysozyme
  • 4887 - 1H,15N assignment of Ca2+-bound state of Canine Milk Lysozyme at 20deg
  • 4943 - 1H Chemical shift Assignments for Lysozymes marketed by Seikagaku and Sigma companies at pH 3.8, 308K
  • 5068 - Recombinant hen lysozyme containing the extra N-terminal Met as the standard reference for the study of hen lysozyme variants
  • 5069 - NMR Structural Study of Two-Disulfide Variant of hen Lysozyme: 2SS[6-127, 30-115]-A Disulfide Intermediate with a Partly Unfolded Structure
  • 5123 - Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy
  • 5124 - Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy
  • 5125 - Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy
  • 5803 - Three-disulfide variant of hen lysozyme: C64A/C80A
  • 5804 - Three-disulfide variant of hen lysozyme: C76A/C94A
  • 6415 - Three-disulfide variant of hen lysozyme: C30A/C115A

PDB Lysozyme NMR studies

  • 1E8L - NMR SOLUTION STRUCTURE OF HEN LYSOZYME
  • 1GXV - SOLUTION STRUCTURE OF LYSOZYME AT LOW AND HIGH PRESSURE
  • 1GXX - SOLUTION STRUCTURE OF LYSOZYME AT LOW AND HIGH PRESSURE
  • 1I56 - SOLUTION STRUCTURE OF CA2+-BOUND STATE OF CANINE MILK LYSOZYME
  • 1IVM - Solution structure of mouse lysozyme M
  • 1IY3 - Solution structure of Human lysozyme at 4 degrees C
  • 1IY4 - Solution structure of Human lysozyme at 35 degrees C