Template:PDB Gallery/4069

• 133l: ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS

  133l: ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS

• 134l: ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS

  134l: ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS

• 1b5u: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANT

  1b5u: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANT

• 1b5v: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

  1b5v: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

• 1b5w: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

  1b5w: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

• 1b5x: Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and x-ray analysis of six ser->ala mutants

  1b5x: Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and x-ray analysis of six ser->ala mutants

• 1b5y: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

  1b5y: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

• 1b5z: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

  1b5z: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

• 1b7l: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

  1b7l: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

• 1b7m: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

  1b7m: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

• 1b7n: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

  1b7n: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

• 1b7o: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

  1b7o: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

• 1b7p: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

  1b7p: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

• 1b7q: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

  1b7q: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

• 1b7r: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

  1b7r: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

• 1b7s: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

  1b7s: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

• 1bb3: HUMAN LYSOZYME MUTANT A96L

  1bb3: HUMAN LYSOZYME MUTANT A96L

• 1bb4: HUMAN LYSOZYME DOUBLE MUTANT A96L, W109H

  1bb4: HUMAN LYSOZYME DOUBLE MUTANT A96L, W109H

• 1bb5: HUMAN LYSOZYME MUTANT A96L COMPLEXED WITH CHITOTRIOSE

  1bb5: HUMAN LYSOZYME MUTANT A96L COMPLEXED WITH CHITOTRIOSE

• 1c43: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES

  1c43: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES

• 1c45: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES

  1c45: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES

• 1c46: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES

  1c46: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES

• 1c7p: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME WITH FOUR EXTRA RESIDUES (EAEA) AT THE N-TERMINAL

  1c7p: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME WITH FOUR EXTRA RESIDUES (EAEA) AT THE N-TERMINAL

• 1cj6: T11A MUTANT HUMAN LYSOZYME

  1cj6: T11A MUTANT HUMAN LYSOZYME

• 1cj7: T11V MUTANT HUMAN LYSOZYME

  1cj7: T11V MUTANT HUMAN LYSOZYME

• 1cj8: T40A MUTANT HUMAN LYSOZYME

  1cj8: T40A MUTANT HUMAN LYSOZYME

• 1cj9: T40V MUTANT HUMAN LYSOZYME

  1cj9: T40V MUTANT HUMAN LYSOZYME

• 1ckc: T43A MUTANT HUMAN LYSOZYME

  1ckc: T43A MUTANT HUMAN LYSOZYME

• 1ckd: T43V MUTANT HUMAN LYSOZYME

  1ckd: T43V MUTANT HUMAN LYSOZYME

• 1ckf: T52A MUTANT HUMAN LYSOZYME

  1ckf: T52A MUTANT HUMAN LYSOZYME

• 1ckg: T52V MUTANT HUMAN LYSOZYME

  1ckg: T52V MUTANT HUMAN LYSOZYME

• 1ckh: T70V MUTANT HUMAN LYSOZYME

  1ckh: T70V MUTANT HUMAN LYSOZYME

• 1d6p: HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE

  1d6p: HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE

• 1d6q: HUMAN LYSOZYME E102 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL GLYCOSIDE OF N-ACETYLLACTOSAMINE

  1d6q: HUMAN LYSOZYME E102 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL GLYCOSIDE OF N-ACETYLLACTOSAMINE

• 1di3: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME

  1di3: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME

• 1di4: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME

  1di4: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME

• 1di5: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME

  1di5: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME

• 1eq4: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME

  1eq4: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME

• 1eq5: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME

  1eq5: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME

• 1eqe: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME

  1eqe: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME

• 1gay: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gay: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gaz: Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions

  1gaz: Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions

• 1gb0: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gb0: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gb2: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gb2: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gb3: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gb3: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gb5: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gb5: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gb6: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gb6: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gb7: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gb7: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gb8: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gb8: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gb9: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gb9: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gbo: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gbo: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gbw: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gbw: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gbx: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gbx: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gby: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gby: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gbz: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gbz: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gdw: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

  1gdw: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

• 1gdx: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

  1gdx: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

• 1ge0: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

  1ge0: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

• 1ge1: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

  1ge1: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

• 1ge2: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

  1ge2: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

• 1ge3: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

  1ge3: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

• 1ge4: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

  1ge4: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS

• 1gev: BURIED POLAR MUTANT HUMAN LYSOZYME

  1gev: BURIED POLAR MUTANT HUMAN LYSOZYME

• 1gez: BURIED POLAR MUTANT HUMAN LYSOZYME

  1gez: BURIED POLAR MUTANT HUMAN LYSOZYME

• 1gf0: BURIED POLAR MUTANT HUMAN LYSOZYME

  1gf0: BURIED POLAR MUTANT HUMAN LYSOZYME

• 1gf3: BURIED POLAR MUTANT HUMAN LYSOZYME

  1gf3: BURIED POLAR MUTANT HUMAN LYSOZYME

• 1gf4: BURIED POLAR MUTANT HUMAN LYSOZYME

  1gf4: BURIED POLAR MUTANT HUMAN LYSOZYME

• 1gf5: BURIED POLAR MUTANT HUMAN LYSOZYME

  1gf5: BURIED POLAR MUTANT HUMAN LYSOZYME

• 1gf6: BURIED POLAR MUTANT HUMAN LYSOZYME

  1gf6: BURIED POLAR MUTANT HUMAN LYSOZYME

• 1gf7: BURIED POLAR MUTANT HUMAN LYSOZYME

  1gf7: BURIED POLAR MUTANT HUMAN LYSOZYME

• 1gf8: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gf8: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gf9: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gf9: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gfa: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gfa: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gfe: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gfe: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gfg: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gfg: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gfh: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gfh: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gfj: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gfj: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gfk: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gfk: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gfr: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gfr: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gft: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gft: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gfu: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gfu: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1gfv: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1gfv: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1hnl: CRYSTAL STRUCTURE OF A GLUTATHIONYLATED HUMAN LYSOZYME: A FOLDING INTERMEDIATE MIMIC IN THE FORMATION OF A DISULFIDE BOND

  1hnl: CRYSTAL STRUCTURE OF A GLUTATHIONYLATED HUMAN LYSOZYME: A FOLDING INTERMEDIATE MIMIC IN THE FORMATION OF A DISULFIDE BOND

• 1i1z: MUTANT HUMAN LYSOZYME (Q86D)

  1i1z: MUTANT HUMAN LYSOZYME (Q86D)

• 1i20: MUTANT HUMAN LYSOZYME (A92D)

  1i20: MUTANT HUMAN LYSOZYME (A92D)

• 1i22: MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)

  1i22: MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)

• 1inu: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

  1inu: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

• 1ioc: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T

  1ioc: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T

• 1ip1: G37A HUMAN LYSOZYME

  1ip1: G37A HUMAN LYSOZYME

• 1ip2: G48A HUMAN LYSOZYME

  1ip2: G48A HUMAN LYSOZYME

• 1ip3: G68A HUMAN LYSOZYME

  1ip3: G68A HUMAN LYSOZYME

• 1ip4: G72A HUMAN LYSOZYME

  1ip4: G72A HUMAN LYSOZYME

• 1ip5: G105A HUMAN LYSOZYME

  1ip5: G105A HUMAN LYSOZYME

• 1ip6: G127A HUMAN LYSOZYME

  1ip6: G127A HUMAN LYSOZYME

• 1ip7: G129A HUMAN LYSOZYME

  1ip7: G129A HUMAN LYSOZYME

• 1iwt: Crystal Structure Analysis of Human lysozyme at 113K.

  1iwt: Crystal Structure Analysis of Human lysozyme at 113K.

• 1iwu: Crystal Structure Analysis of Human lysozyme at 127K.

  1iwu: Crystal Structure Analysis of Human lysozyme at 127K.

• 1iwv: Crystal Structure Analysis of Human lysozyme at 147K.

  1iwv: Crystal Structure Analysis of Human lysozyme at 147K.

• 1iww: Crystal Structure Analysis of Human lysozyme at 152K.

  1iww: Crystal Structure Analysis of Human lysozyme at 152K.

• 1iwx: Crystal Structure Analysis of Human lysozyme at 161K.

  1iwx: Crystal Structure Analysis of Human lysozyme at 161K.

• 1iwy: Crystal Structure Analysis of Human lysozyme at 170K.

  1iwy: Crystal Structure Analysis of Human lysozyme at 170K.

• 1iwz: Crystal Structure Analysis of Human lysozyme at 178K.

  1iwz: Crystal Structure Analysis of Human lysozyme at 178K.

• 1ix0: I59A-3SS human lysozyme

  1ix0: I59A-3SS human lysozyme

• 1iy3: Solution Structure of the Human lysozyme at 4 degree C

  1iy3: Solution Structure of the Human lysozyme at 4 degree C

• 1iy4: Solution structure of the human lysozyme at 35 degree C

  1iy4: Solution structure of the human lysozyme at 35 degree C

• 1jka: HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ASP

  1jka: HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ASP

• 1jkb: HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ALA

  1jkb: HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ALA

• 1jkc: HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY PHE

  1jkc: HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY PHE

• 1jkd: HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY ALA

  1jkd: HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY ALA

• 1jsf: FULL-MATRIX LEAST-SQUARES REFINEMENT OF HUMAN LYSOZYME

  1jsf: FULL-MATRIX LEAST-SQUARES REFINEMENT OF HUMAN LYSOZYME

• 1jwr: Crystal structure of human lysozyme at 100 K

  1jwr: Crystal structure of human lysozyme at 100 K

• 1laa: X-RAY STRUCTURE OF GLU 53 HUMAN LYSOZYME

  1laa: X-RAY STRUCTURE OF GLU 53 HUMAN LYSOZYME

• 1lhh: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

  1lhh: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

• 1lhi: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

  1lhi: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

• 1lhj: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

  1lhj: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

• 1lhk: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

  1lhk: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

• 1lhl: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

  1lhl: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

• 1lhm: THE CRYSTAL STRUCTURE OF A MUTANT LYSOZYME C77(SLASH)95A WITH INCREASED SECRETION EFFICIENCY IN YEAST

  1lhm: THE CRYSTAL STRUCTURE OF A MUTANT LYSOZYME C77(SLASH)95A WITH INCREASED SECRETION EFFICIENCY IN YEAST

• 1lmt: STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME

  1lmt: STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME

• 1loz: AMYLOIDOGENIC VARIANT (I56T) VARIANT OF HUMAN LYSOZYME

  1loz: AMYLOIDOGENIC VARIANT (I56T) VARIANT OF HUMAN LYSOZYME

• 1lyy: AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME

  1lyy: AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME

• 1lz1: REFINEMENT OF HUMAN LYSOZYME AT 1.5 ANGSTROMS RESOLUTION. ANALYSIS OF NON-BONDED AND HYDROGEN-BOND INTERACTIONS

  1lz1: REFINEMENT OF HUMAN LYSOZYME AT 1.5 ANGSTROMS RESOLUTION. ANALYSIS OF NON-BONDED AND HYDROGEN-BOND INTERACTIONS

• 1lz4: ENTHALPIC DESTABILIZATION OF A MUTANT HUMAN LYSOZYME LACKING A DISULFIDE BRIDGE BETWEEN CYSTEINE-77 AND CYSTEINE-95

  1lz4: ENTHALPIC DESTABILIZATION OF A MUTANT HUMAN LYSOZYME LACKING A DISULFIDE BRIDGE BETWEEN CYSTEINE-77 AND CYSTEINE-95

• 1lz5: STRUCTURAL AND FUNCTIONAL ANALYSES OF THE ARG-GLY-ASP SEQUENCE INTRODUCED INTO HUMAN LYSOZYME

  1lz5: STRUCTURAL AND FUNCTIONAL ANALYSES OF THE ARG-GLY-ASP SEQUENCE INTRODUCED INTO HUMAN LYSOZYME

• 1lz6: STRUCTURAL AND FUNCTIONAL ANALYSES OF THE ARG-GLY-ASP SEQUENCE INTRODUCED INTO HUMAN LYSOZYME

  1lz6: STRUCTURAL AND FUNCTIONAL ANALYSES OF THE ARG-GLY-ASP SEQUENCE INTRODUCED INTO HUMAN LYSOZYME

• 1lzr: STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0

  1lzr: STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0

• 1lzs: STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0

  1lzs: STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0

• 1op9: Complex of human lysozyme with camelid VHH HL6 antibody fragment

  1op9: Complex of human lysozyme with camelid VHH HL6 antibody fragment

• 1oua: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE I56T MUTANT

  1oua: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE I56T MUTANT

• 1oub: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V100A MUTANT

  1oub: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V100A MUTANT

• 1ouc: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT

  1ouc: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT

• 1oud: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT

  1oud: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT

• 1oue: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V125A MUTANT

  1oue: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V125A MUTANT

• 1ouf: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V130A MUTANT

  1ouf: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V130A MUTANT

• 1oug: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V2A MUTANT

  1oug: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V2A MUTANT

• 1ouh: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V74A MUTANT

  1ouh: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V74A MUTANT

• 1oui: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V93A MUTANT

  1oui: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V93A MUTANT

• 1ouj: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V99A MUTANT

  1ouj: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V99A MUTANT

• 1qsw: CRYSTAL STRUCTURE ANALYSIS OF A HUMAN LYSOZYME MUTANT W64C C65A

  1qsw: CRYSTAL STRUCTURE ANALYSIS OF A HUMAN LYSOZYME MUTANT W64C C65A

• 1re2: HUMAN LYSOZYME LABELLED WITH TWO 2',3'-EPOXYPROPYL BETA-GLYCOSIDE OF N-ACETYLLACTOSAMINE

  1re2: HUMAN LYSOZYME LABELLED WITH TWO 2',3'-EPOXYPROPYL BETA-GLYCOSIDE OF N-ACETYLLACTOSAMINE

• 1rem: HUMAN LYSOZYME WITH MAN-B1,4-GLCNAC COVALENTLY ATTACHED TO ASP53

  1rem: HUMAN LYSOZYME WITH MAN-B1,4-GLCNAC COVALENTLY ATTACHED TO ASP53

• 1rex: NATIVE HUMAN LYSOZYME

  1rex: NATIVE HUMAN LYSOZYME

• 1rey: HUMAN LYSOZYME-N,N'-DIACETYLCHITOBIOSE COMPLEX

  1rey: HUMAN LYSOZYME-N,N'-DIACETYLCHITOBIOSE COMPLEX

• 1rez: HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX

  1rez: HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX

• 1tay: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME

  1tay: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME

• 1tby: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME

  1tby: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME

• 1tcy: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME

  1tcy: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME

• 1tdy: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME

  1tdy: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME

• 1ubz: Crystal structure of Glu102-mutant human lysozyme doubly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine

  1ubz: Crystal structure of Glu102-mutant human lysozyme doubly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine

• 1w08: STRUCTURE OF T70N HUMAN LYSOZYME

  1w08: STRUCTURE OF T70N HUMAN LYSOZYME

• 1wqm: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  1wqm: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 1wqn: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  1wqn: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 1wqo: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  1wqo: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 1wqp: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  1wqp: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 1wqq: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  1wqq: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 1wqr: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  1wqr: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 1yam: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

  1yam: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

• 1yan: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

  1yan: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

• 1yao: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

  1yao: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

• 1yap: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

  1yap: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

• 1yaq: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

  1yaq: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

• 207l: MUTANT HUMAN LYSOZYME C77A

  207l: MUTANT HUMAN LYSOZYME C77A

• 208l: MUTANT HUMAN LYSOZYME C77A

  208l: MUTANT HUMAN LYSOZYME C77A

• 2bqa: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqa: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqb: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqb: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqc: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqc: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqd: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqd: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqe: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqe: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqf: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqf: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqg: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqg: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqh: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqh: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqi: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqi: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqj: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqj: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqk: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqk: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bql: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bql: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqm: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqm: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqn: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqn: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2bqo: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2bqo: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2hea: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

  2hea: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

• 2heb: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

  2heb: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

• 2hec: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

  2hec: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

• 2hed: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

  2hed: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

• 2hee: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

  2hee: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

• 2hef: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

  2hef: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

• 2lhm: CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE

  2lhm: CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE

• 2mea: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS

  2mea: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS

• 2meb: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS

  2meb: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS

• 2mec: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS

  2mec: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS

• 2med: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2med: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2mee: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2mee: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2mef: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2mef: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2meg: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS.

  2meg: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS.

• 2meh: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2meh: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2mei: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

  2mei: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

• 2nwd: Structure of chemically synthesized human lysozyme at 1 Angstrom resolution

  2nwd: Structure of chemically synthesized human lysozyme at 1 Angstrom resolution

• 3lhm: CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE

  3lhm: CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE