Usages in wwPDB of concept: c_0501
nUsages: 627; SSE string: HEEHHHH
102l:A     (ILE3) to   (MET106)  HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
107l:A     (ILE3) to   (MET106)  STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
108l:A     (ILE3) to   (MET106)  STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
109l:A     (ILE3) to   (MET106)  STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
110l:A     (ILE3) to   (GLY107)  STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
111l:A     (ILE3) to   (GLY107)  STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
112l:A     (ILE3) to   (GLY107)  STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
113l:A     (ILE3) to   (GLY107)  STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
114l:A     (ILE3) to   (GLY107)  STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
115l:A     (ILE3) to   (GLY107)  STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
118l:A     (ILE3) to   (MET106)  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  |   HYDROLASE(O-GLYCOSYL) 
119l:A     (ILE3) to   (GLY107)  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  |   HYDROLASE(O-GLYCOSYL) 
120l:A     (ILE3) to   (MET106)  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  |   HYDROLASE(O-GLYCOSYL) 
122l:A     (ILE3) to   (GLY107)  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  |   HYDROLASE(O-GLYCOSYL) 
123l:A     (ILE3) to   (MET106)  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  |   HYDROLASE(O-GLYCOSYL) 
125l:A     (ILE3) to   (GLY107)  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  |   HYDROLASE(O-GLYCOSYL) 
126l:A     (ILE3) to   (MET106)  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  |   HYDROLASE(O-GLYCOSYL) 
127l:A     (ILE3) to   (MET106)  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  |   HYDROLASE(O-GLYCOSYL) 
128l:A     (ILE3) to   (MET106)  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  |   HYDROLASE(O-GLYCOSYL) 
129l:A     (ILE3) to   (MET106)  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  |   HYDROLASE(O-GLYCOSYL) 
130l:A     (ILE3) to   (MET106)  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  |   HYDROLASE(O-GLYCOSYL) 
131l:A     (ILE3) to   (MET106)  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  |   HYDROLASE(O-GLYCOSYL) 
138l:A     (ILE3) to   (MET106)  RAPID CRYSTALLIZATION OF T4 LYSOZYME BY INTERMOLECULAR DISULFIDE CROSSLINKING  |   HYDROLASE(O-GLYCOSYL) 
140l:A     (ILE3) to   (GLY107)  ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
141l:A     (ILE3) to   (MET106)  ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
144l:A     (ILE3) to   (MET106)  ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
143l:A     (ILE3) to   (MET106)  ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
146l:A     (ILE3) to   (MET106)  ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
147l:A     (ILE3) to   (MET106)  ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
148l:E     (ILE3) to   (MET106)  A COVALENT ENZYME-SUBSTRATE INTERMEDIATE WITH SACCHARIDE DISTORTION IN A MUTANT T4 LYSOZYME  |   O-GLYCOSYL, HYDROLASE-HYDROLASE SUBSTRATE COMPLEX 
149l:A     (ASN2) to   (MET106)  CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
155l:A     (ILE3) to   (MET106)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
156l:A     (ILE3) to   (MET106)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
157l:A     (ILE3) to   (MET106)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
160l:A     (ILE3) to   (MET106)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
162l:A     (ILE3) to   (GLY107)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
163l:A     (ILE3) to   (MET106)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
164l:A     (ILE3) to   (MET106)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
165l:A     (ILE3) to   (MET106)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
167l:A     (ASN2) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
167l:B     (ASN2) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
168l:D     (ASN2) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
169l:B     (ASN2) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
169l:E     (ILE3) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
170l:A     (ILE3) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
171l:A     (ILE3) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
172l:A     (CYS3) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
173l:A     (ILE3) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
175l:A     (PHE4) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
175l:B     (ILE3) to   (GLY107)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
176l:A     (ILE3) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
176l:B     (ILE3) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
177l:A     (ILE3) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
180l:A     (ILE3) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   COMPLEX (HYDROLASE/CELL WALL) 
178l:A     (ASN2) to   (MET106)  PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
181l:A     (ILE3) to   (GLY107)  SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY  |   HYDROLASE (O-GLYCOSYL) 
182l:A     (ILE3) to   (GLY107)  SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY  |   HYDROLASE (O-GLYCOSYL) 
183l:A     (ASN2) to   (GLY107)  SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY  |   HYDROLASE (O-GLYCOSYL) 
184l:A     (ILE3) to   (MET106)  SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY  |   HYDROLASE (O-GLYCOSYL) 
185l:A     (ILE3) to   (GLY107)  SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY  |   HYDROLASE (O-GLYCOSYL) 
186l:A     (ILE3) to   (MET106)  SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY  |   HYDROLASE (O-GLYCOSYL) 
187l:A     (ILE3) to   (GLY107)  SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY  |   HYDROLASE (O-GLYCOSYL) 
189l:A     (ASN2) to   (MET106)  ENHANCEMENT OF PROTEIN STABILITY BY THE COMBINATION OF POINT MUTATIONS IN T4 LYSOZYME IS ADDITIVE  |   HYDROLASE (O-GLYCOSYL) 
190l:A     (ILE3) to   (GLY107)  A HELIX INITIATION SIGNAL IN T4 LYSOZYME IDENTIFIED BY POLYALANINE MUTAGENESIS  |   HYDROLASE (0-GLYCOSYL) 
192l:A     (ILE3) to   (MET106)  A HELIX INITIATION SIGNAL IN T4 LYSOZYME IDENTIFIED BY POLYALANINE MUTAGENESIS  |   HYDROLASE (O-GLYCOSYL) 
195l:A     (ILE3) to   (MET106)  THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME  |   CAVITIES, CORE-PACKING, PROTEIN STABILITY, HYDROLASE (O- GLYCOSYL) 
196l:A     (ILE3) to   (MET106)  THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME  |   CAVITIES, CORE-PACKING, PROTEIN STABILITY, HYDROLASE (O- GLYCOSYL) 
198l:A     (ILE3) to   (GLY107)  THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME  |   CAVITIES, CORE-PACKING, PROTEIN STABILITY, HYDROLASE (O- GLYCOSYL) 
199l:A     (ILE3) to   (GLY107)  THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME  |   CAVITIES, CORE-PACKING, PROTEIN STABILITY, HYDROLASE (O- GLYCOSYL) 
2oe4:X     (ILE3) to   (MET106)  HIGH PRESSURE PSUEDO WILD TYPE T4 LYSOZYME  |   HIGH-PRESSURE, T4 LYZOYME, HYDROLASE 
2oe7:X     (ILE3) to   (MET106)  HIGH-PRESSURE T4 LYSOZYME  |   HIGH-PRESSURE, T4 LYSOZYME, HYDROLASE 
2oea:X     (ILE3) to   (MET106)  HIGH-PRESSURE STRUCTURE OF PSEUDO-WT T4 LYSOZYME  |   HIGH-PRESSURE, T4 LYSOZYME, HYDROLASE 
1nhb:A     (ILE3) to   (GLY107)  SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY  |   HYDROLASE (O-GLYCOSYL) 
3run:A     (ILE3) to   (MET106)  NEW STRATEGY TO ANALYZE STRUCTURES OF GLYCOPEPTIDE ANTIBIOTIC-TARGET COMPLEXES  |   ANTIBIOTIC, GLYCOPEPTIDE, NATIVE PROTEIN LIGATION, FUSION, CARBOXYMETHYLATION OF CYSTEINE, VANCOMYCIN, HYDROLASE-ANTIBIOTIC COMPLEX 
2oty:X     (ILE3) to   (MET106)  1,2-DICHLOROBENZENE IN COMPLEX WITH T4 LYSOZYME L99A  |   HYDROLASE, PROTEIN-LIGAND COMPLEX, MODEL SYSTEM 
2otz:X     (ILE3) to   (MET106)  N-METHYLANILINE IN COMPLEX WITH T4 LYSOZYME L99A  |   HYDROLASE, PROTEIN-LIGAND COMPLEX, MODEL SYSTEM 
2ou0:X     (ILE3) to   (MET106)  1-METHYLPYRROLE IN COMPLEX WITH T4 LYSOZYME L99A  |   HYDROLASE, PROTEIN-LIGAND COMPLEX, MODEL SYSTEM 
2ou8:A     (ILE3) to   (MET106)  STRUCTURE OF SPIN-LABELED T4 LYSOZYME MUTANT T115R1 AT ROOM TEMPERATURE  |   NITROXIDE, SPIN LABEL, T4 LYSOZYME, ELECTRON PARAMAGNETIC RESONANCE, EPR, HYDROLASE 
2ou9:A     (ILE3) to   (MET106)  STRUCTURE OF SPIN-LABELED T4 LYSOZYME MUTANT T115R1/R119A  |   NITROXIDE, SPIN LABEL, T4 LYSOZYME, ELECTRON PARAMAGNETIC RESONANCE, EPR, HYDROLASE 
2b6t:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A AT 200 MPA  |   ANTIMICROBIAL, HYDROLASE 
2b6w:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A AT 200 MPA  |   HIGH PRESSURE, T4 LYSOZYME, HYDROLASE 
2b6x:A     (ILE3) to   (GLY107)  T4 LYSOZYME MUTANT L99A AT 200 MPA  |   HIGH PRESSURE, T4 LYSOZYME, HYDROLASE 
2b6y:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A AT AMBIENT PRESSURE  |   HIGH PRESSURE, T4 LYSOZYME, HYDROLASE 
2b6z:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A AT AMBIENT PRESSURE  |   HIGH PRESSURE, T4 LYSOZYME, HYDROLASE 
2b70:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A AT AMBIENT PRESSURE  |   HIGH PRESSURE, T4 LYSOZYME, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC, HYDROLASE 
2b72:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A AT 100 MPA  |   HIGH PRESSURE, T4 LYSOZYME, CAVITY, HYDROLASE 
2b73:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A AT 100 MPA  |   HIGH PRESSURE, T4 LYSOZYME, CAVITY, HYDROLASE 
2b74:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A AT 100 MPA  |   T4 LYSOZYME, HIGH PRESSURE, CAVITY, HYDROLASE 
2b7x:A     (ILE3) to   (MET112)  SEQUENTIAL REORGANIZATION OF BETA-SHEET TOPOLOGY BY INSERTION OF A SINGLE STRAND  |   SEQUENCE DUPLICATION, PROTEIN DESIGN, STRUCTURAL SWITCHES, TANDEM REPEAT, HYDROLASE 
2b7x:D     (ASN2) to   (MET112)  SEQUENTIAL REORGANIZATION OF BETA-SHEET TOPOLOGY BY INSERTION OF A SINGLE STRAND  |   SEQUENCE DUPLICATION, PROTEIN DESIGN, STRUCTURAL SWITCHES, TANDEM REPEAT, HYDROLASE 
1b6i:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT WITH CYS 54 REPLACED BY THR, CYS 97 REPLACED BY ALA, THR 21 REPLACED BY CYS AND LYS 124 REPLACED BY CYS (C54T,C97A,T21C,K124C)  |   HYDROLASE(O-GLYCOSYL) 
3f8v:A     (ILE3) to   (MET106)  EVAULAUTION AT ATOMIC RESOLUTION OF THE ROLE OF STRAIN IN DESTABILIZING THE TEMPERATURE SENSITIVE T4 LYSOZYME MUTANT ARG96-->HIS  |   ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE, T4 LYSOZYME, BOND ANGLE STRAIN, ROTAMER STRAIN, TEMPERATURE SENSITIVE MUTANT 
3f9l:A     (ILE3) to   (MET106)  EVAULAUTION AT ATOMIC RESOLUTION OF THE ROLE OF STRAIN IN DESTABILIZING THE TEMPERATURE SENSITIVE T4 LYSOZYME MUTANT ARG96-->HIS  |   ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE, T4 LYSOZYME, BOND ANGLE STRAIN, ROTAMER STRAIN, TEMPERATURE SENSITIVE MUTANT 
3fa0:A     (ILE3) to   (MET106)  EVAULAUTION AT ATOMIC RESOLUTION OF THE ROLE OF STRAIN IN DESTABILIZING THE TEMPERATURE SENSITIVE T4 LYSOZYME MUTANT ARG96-->HIS  |   ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE, T4 LYSOZYME, BOND ANGLE STRAIN, ROTAMER STRAIN, TEMPERATURE SENSITIVE MUTANT 
3fad:A     (ILE3) to   (MET106)  EVAULAUTION AT ATOMIC RESOLUTION OF THE ROLE OF STRAIN IN DESTABILIZING THE TEMPERATURE SENSITIVE T4 LYSOZYME MUTANT ARG96-->HIS  |   ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE, T4 LYSOZYME, BOND ANGLE STRAIN, ROTAMER STRAIN, TEMPERATURE SENSITIVE MUTANT 
3sb6:A     (ILE3) to   (MET106)  CU-MEDIATED DIMER OF T4 LYSOZYME D61H/K65H/R76H/R80H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sb6:B     (ILE3) to   (MET106)  CU-MEDIATED DIMER OF T4 LYSOZYME D61H/K65H/R76H/R80H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sb5:B     (ILE3) to   (GLN105)  ZN-MEDIATED TRIMER OF T4 LYSOZYME R125C/E128C BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sb5:C     (ASN2) to   (GLN105)  ZN-MEDIATED TRIMER OF T4 LYSOZYME R125C/E128C BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sb5:D     (ILE3) to   (MET106)  ZN-MEDIATED TRIMER OF T4 LYSOZYME R125C/E128C BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sb8:A     (ILE3) to   (GLY107)  CU-MEDIATED DIMER OF T4 LYSOZYME D61H/K65H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sb8:B     (ILE3) to   (MET106)  CU-MEDIATED DIMER OF T4 LYSOZYME D61H/K65H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sb8:C     (ASN2) to   (MET106)  CU-MEDIATED DIMER OF T4 LYSOZYME D61H/K65H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sb9:A     (ASN2) to   (MET106)  CU-MEDIATED DIMER OF T4 LYSOZYME R76H/R80H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sba:A     (ILE3) to   (MET106)  ZN-MEDIATED HEXAMER OF T4 LYSOZYME R76H/R80H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sba:B     (ASN2) to   (MET106)  ZN-MEDIATED HEXAMER OF T4 LYSOZYME R76H/R80H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sba:C     (ASN2) to   (MET106)  ZN-MEDIATED HEXAMER OF T4 LYSOZYME R76H/R80H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sba:D     (ASN2) to   (MET106)  ZN-MEDIATED HEXAMER OF T4 LYSOZYME R76H/R80H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sba:E     (ILE3) to   (MET106)  ZN-MEDIATED HEXAMER OF T4 LYSOZYME R76H/R80H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sba:F     (ASN2) to   (MET106)  ZN-MEDIATED HEXAMER OF T4 LYSOZYME R76H/R80H BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
3sbb:C     (ILE3) to   (MET106)  DISULPHIDE-MEDIATED TETRAMER OF T4 LYSOZYME R76C/R80C BY SYNTHETIC SYMMETRIZATION  |   METAL-MEDIATED SYNTHETIC SYMMETRIZATION, SYNTHETIC SYMMETRIZATION, HYDROLASE 
4xee:A  (ILE1003) to  (MET1106)  STRUCTURE OF ACTIVE-LIKE NEUROTENSIN RECEPTOR  |   MEMBRANE PROTEIN, G PROTEIN-COUPLED RECEPTOR, GPCR, NEUROTENSIN RECEPTOR, NTSR1, SIGNALING PROTEIN, HYDROLASE 
4xes:A  (ILE1003) to  (MET1106)  STRUCTURE OF ACTIVE-LIKE NEUROTENSIN RECEPTOR  |   MEMBRANE PROTEIN, G PROTEIN-COUPLED RECEPTOR, GPCR, NEUROTENSIN RECEPTOR, NTSR1, SIGNALING PROTEIN, HYDROLASE 
1c60:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/F153A IN THE PRESENCE OF 8 ATM ARGON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c61:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/F153A IN THE PRESENCE OF 8 ATM KRYPTON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c63:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L121A IN THE PRESENCE OF 8 ATM ARGON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c64:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L121A IN THE PRESENCE OF 8 ATM KRYPTON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c65:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L121A IN THE PRESENCE OF 8 ATM XENON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c66:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L121A/L133A IN THE PRESENCE OF 8 ATM ARGON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c67:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L121A/L133A IN THE PRESENCE OF 8 ATM KRYPTON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c68:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L121A/L133A IN THE PRESENCE OF 8 ATM XENON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6a:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L133A IN THE PRESENCE OF 8 ATM KRYPTON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6b:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L133A IN THE PRESENCE OF 8 ATM XENON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6d:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 16 ATM KRYPTON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6e:A     (ILE3) to   (GLY107)  T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 2 ATM XENON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6h:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 4 ATM XENON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6i:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 8 ATM ARGON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6j:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 8 ATM KRYPTON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6k:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 8 ATM XENON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6l:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L99A/F153A IN THE PRESENCE OF 8 ATM ARGON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6m:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L99A/F153A IN THE PRESENCE OF 8 ATM KRYPTON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6p:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A IN THE PRESENCE OF 8 ATM ARGON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6q:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A IN THE PRESENCE OF 8 ATM KRYPTON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6t:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A IN THE PRESENCE OF 8 ATM XENON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
3fi5:A     (ILE3) to   (GLY107)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT R96W  |   ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE, T4 LYSOZYME, ELECTROSTATICS, STRAIN, PROTEIN STABILITY 
3fi5:B     (ILE3) to   (GLY107)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT R96W  |   ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE, T4 LYSOZYME, ELECTROSTATICS, STRAIN, PROTEIN STABILITY 
3fi5:C     (ILE3) to   (GLY107)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT R96W  |   ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE, T4 LYSOZYME, ELECTROSTATICS, STRAIN, PROTEIN STABILITY 
3fi5:D     (ILE3) to   (GLY107)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT R96W  |   ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE, T4 LYSOZYME, ELECTROSTATICS, STRAIN, PROTEIN STABILITY 
4i7j:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH BENZENE BOUND  |   HYDROLASE 
4i7j:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH BENZENE BOUND  |   HYDROLASE 
4i7k:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH TOLUENE BOUND  |   HYDROLASE 
4i7k:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH TOLUENE BOUND  |   HYDROLASE 
4i7l:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH PHENOL BOUND  |   HYDROLASE 
4i7l:B     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH PHENOL BOUND  |   HYDROLASE 
4i7m:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 2-ALLYLPHENOL BOUND  |   HYDROLASE 
4i7m:B     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 2-ALLYLPHENOL BOUND  |   HYDROLASE 
4i7n:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 1-PHENYL-2-PROPYN-1-OL BOUND  |   HYDROLASE 
4i7n:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH 1-PHENYL-2-PROPYN-1-OL BOUND  |   HYDROLASE 
4i7q:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 4-TRIFLUOROMETHYLIMIDAZOLE BOUND  |   HYDROLASE 
4i7q:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH 4-TRIFLUOROMETHYLIMIDAZOLE BOUND  |   HYDROLASE 
4i7p:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 4-BROMOIMIDAZOLE BOUND  |   HYDROLASE 
4i7p:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH 4-BROMOIMIDAZOLE BOUND  |   HYDROLASE 
4i7r:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 2-(PYRAZOLO-1-YL) ETHANOL BOUND  |   HYDROLASE 
4i7r:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH 2-(PYRAZOLO-1-YL) ETHANOL BOUND  |   HYDROLASE 
4i7s:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 3-TRIFLUOROMETHYL-5-METHYL PYRAZOLE BOUND  |   HYDROLASE 
4i7s:B     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 3-TRIFLUOROMETHYL-5-METHYL PYRAZOLE BOUND  |   HYDROLASE 
4i7t:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH 2-BROMO-5-HYDROXYBENZALDEHYDE BOUND  |   HYDROLASE 
4iap:A  (ILE1003) to  (MET1106)  CRYSTAL STRUCTURE OF PH DOMAIN OF OSH3 FROM SACCHAROMYCES CEREVISIAE  |   PH DOMAIN, BETA SANDWITCH, TARGETING, PHOSPHOINOSITIDES, LIPID BINDING PROTEIN- HYDRORASE COMPLEX 
4iap:B  (ILE1003) to  (MET1106)  CRYSTAL STRUCTURE OF PH DOMAIN OF OSH3 FROM SACCHAROMYCES CEREVISIAE  |   PH DOMAIN, BETA SANDWITCH, TARGETING, PHOSPHOINOSITIDES, LIPID BINDING PROTEIN- HYDRORASE COMPLEX 
1ov5:A     (ILE3) to   (MET106)  T4 LYSOZYME CAVITY MUTANT L99A/M102Q BOUND WITH 2- ALLYLPHENOL  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1ov7:A     (ILE3) to   (MET106)  T4 LYSOZYME CAVITY MUTANT L99A/M102Q BOUND WITH 2-ALLYL-6- METHYL-PHENOL  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1ovh:A     (ILE3) to   (MET106)  T4 LYSOZYME CAVITY MUTANT L99A/M102Q BOUND WITH 2-CHLORO-6- METHYL-ANILINE  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1ovj:A     (ILE3) to   (MET106)  T4 LYSOZYME CAVITY MUTANT L99A/M102Q BOUND WITH 3-FLUORO-2- METHYL_ANILINE  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1ovk:A     (ILE3) to   (MET106)  T4 LYSOZYME CAVITY MUTANT L99A/M102Q BOUND WITH N-ALLYL- ANILINE  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1owy:A     (ILE3) to   (MET106)  T4 LYSOZYME CAVITY MUTANT L99A/M102Q BOUND WITH 2-PROPYL- ANILINE  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1owz:A     (PHE4) to   (MET106)  T4 LYSOZYME CAVITY MUTANT L99A/M102Q BOUND WITH 4- FLUOROPHENETHYL ALCOHOL  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1cu0:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT I78M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING, HYDROLASE 
1cu3:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT V87M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING, HYDROLASE 
1cu5:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L91M  |   T4 LYSOXYME, METHIONINE CORE MUTANT, PROTEIN FOLDING, HYDROLASE 
1cup:A     (ILE3) to   (MET106)  METHIONINE CORE MUTANT OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING, HYDROLASE 
1cuq:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT V103M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING, HYDROLASE 
1cv0:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT F104M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING, HYDROLASE 
1cv1:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT V111M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING, HYDROLASE 
1cv3:A     (ILE3) to   (GLY107)  T4 LYSOZYME MUTANT L121M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING, HYDROLASE 
1cv5:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L133M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1cvk:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L118A  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, CAVITY-FORMING MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1oyu:A     (ASN2) to   (MET117)  LONG-DISTANCE CONFORMATIONAL CHANGES IN A PROTEIN ENGINEERED BY MODULATED SEQUENCE DUPLICATION  |   SEQUENCE DUPLICATION, DESIGN OF STRUCTURAL SWITCHES, TANDEM REPEAT, PROTEIN DESIGN, HYDROLASE 
1cx6:A     (ILE3) to   (MSE106)  T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, SELENOMETHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1p2r:A     (ILE3) to   (MET106)  T4 LYSOZYME CORE REPACKING MUTANT I78V/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
2q9d:A     (ILE3) to   (MET106)  STRUCTURE OF SPIN-LABELED T4 LYSOZYME MUTANT A41R1  |   NITROXIDE, SPIN LABEL, T4 LYSOZYME, ELECTRON PARAMAGNETIC RESONANCE, EPR, HYDROLASE 
1p36:A     (ILE3) to   (MET106)  T4 LYOSZYME CORE REPACKING MUTANT I100V/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1p37:A     (ILE3) to   (ILE106)  T4 LYSOZYME CORE REPACKING BACK-REVERTANT L102M/CORE10  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
2q9e:A     (ILE3) to   (MET106)  STRUCTURE OF SPIN-LABELED T4 LYSOZYME MUTANT S44R1  |   NITROXIDE, SPIN LABEL, T4 LYSOZYME, ELECTRON PARAMAGNETIC RESONANCE, EPR, HYDROLASE 
2q9e:B     (ILE3) to   (MET106)  STRUCTURE OF SPIN-LABELED T4 LYSOZYME MUTANT S44R1  |   NITROXIDE, SPIN LABEL, T4 LYSOZYME, ELECTRON PARAMAGNETIC RESONANCE, EPR, HYDROLASE 
2q9e:C     (ILE3) to   (MET106)  STRUCTURE OF SPIN-LABELED T4 LYSOZYME MUTANT S44R1  |   NITROXIDE, SPIN LABEL, T4 LYSOZYME, ELECTRON PARAMAGNETIC RESONANCE, EPR, HYDROLASE 
1p3n:A     (ILE3) to   (ILE106)  CORE REDESIGN BACK-REVERTANT I103V/CORE10  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1p46:A     (ILE3) to   (GLY107)  T4 LYSOZYME CORE REPACKING MUTANT M106I/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1d2w:A     (ILE3) to   (MET106)  N-TERMINAL DOMAIN CORE METHIONINE MUTATION  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1d2y:A     (ILE3) to   (MET106)  N-TERMINAL DOMAIN CORE METHIONINE MUTATION  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1d3f:A     (ILE3) to   (GLY107)  N-TERMINAL DOMAIN CORE METHIONINE MUTATION  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1d3j:A     (ILE3) to   (MET106)  N-TERMINAL DOMAIN CORE METHIONINE MUTATION  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1d3m:A     (ILE3) to   (MET106)  METHIONINE CORE MUTATION  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1d3n:A     (ILE3) to   (MSE106)  METHIONINE CORE MUTATION  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, SELENOMETHIONINE, PROTEIN ENGINEERING, PROTEIN FOLDING 
1p56:A     (ILE3) to   (MET106)  DUPLICATION-EXTENSION OF HELIX A OF T4 LYSOZYME  |   SEQUENCE DUPLICATION, FOLDING PROPENSITY, COMPLETION FOLDING EXPERIMENT, HYDROLASE 
1p64:A     (ILE3) to   (MET106)  T4 LYSOZYME CORE REPACKING MUTANT L133F/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1p6y:A     (ILE3) to   (MET106)  T4 LYSOZYME CORE REPACKING MUTANT M120Y/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1p7s:A     (ILE3) to   (MET106)  T4 LYSOZYME CORE REPACKING MUTANT V103I/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
3g3w:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF SPIN LABELED T4 LYSOZYME (T151R1) AT 291 K  |   MODIFIED CYSTEINE, NITROXIDE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3g3x:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF SPIN LABELED T4 LYSOZYME (T151R1) AT 100 K  |   HYDROLASE, MODIFIED CYSTEINE, NITROXIDE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE 
1d9w:A     (ILE3) to   (MET106)  BACTERIOPHAGE T4 LYSOZYME MUTANT  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, HELIX CAPPING, HELIX DIPOLE, HYDROLASE 
4xsj:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN MITOCHONDRIAL CALCIUM UNIPORTER FUSED WITH T4 LYSOZYME  |   MEMBRANE PROTEIN, CALCIUM CHANNEL, MITOCHONDRIA, TRANSPORT PROTEIN 
2cuu:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF SPIN LABELED T4 LYSOZYME (V131R1)  |   NITROXIDE SPIN LABEL, EPR, MODIFIED CYSTEINE, HYDROLASE 
1pqd:A     (ILE3) to   (ILE106)  T4 LYSOZYME CORE REPACKING MUTANT CORE10/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1pqi:A     (ILE3) to   (MET106)  T4 LYSOZYME CORE REPACKING MUTANT I118L/CORE7/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1pqj:A     (ILE3) to   (ILE106)  T4 LYSOZYME CORE REPACKING MUTANT A111V/CORE10/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1pqk:B     (ILE3) to   (MET106)  REPACKING OF THE CORE OF T4 LYSOZYME BY AUTOMATED DESIGN  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1pqk:C     (ASN2) to   (MET106)  REPACKING OF THE CORE OF T4 LYSOZYME BY AUTOMATED DESIGN  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1pqo:A     (ILE3) to   (MET106)  T4 LYSOZYME CORE REPACKING MUTANT L118I/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1dya:A     (ILE3) to   (GLY107)  DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
1dyc:A     (ILE3) to   (GLY107)  DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
1dyd:A     (ILE3) to   (MET106)  DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
1dyf:A     (ILE3) to   (GLY107)  DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
1dyg:A     (ILE3) to   (MET106)  DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
3gui:A     (ILE3) to   (GLN105)  T4 LYSOZYME M102E/L99A MUTANT WITH BURIED CHARGE IN APOLAR CAVITY--APO STRUCTURE  |   T4 LYSOZYME, APOLAR CAVITY, BURIED CHARGE, LIGAND BINDING, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3guj:A     (ILE3) to   (GLN105)  T4 LYSOZYME M102E/L99A MUTANT WITH BURIED CHARGE IN APOLAR CAVITY-- BENZENE BINDING  |   T4 LYSOZYME, APOLAR CAVITY, BURIED CHARGE, LIGAND BINDING, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3gul:A     (ILE3) to   (GLN105)  T4 LYSOZYME M102E/L99A MUTANT WITH BURIED CHARGE IN APOLAR CAVITY-- ETHYLBENZENE BINDING  |   T4 LYSOZYME, APOLAR CAVITY, BURIED CHARGE, LIGAND BINDING, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3gum:A     (PHE4) to   (GLN105)  T4 LYSOZYME M102E/L99A MUTANT WITH BURIED CHARGE IN APOLAR CAVITY--P- XYLENE BINDING  |   T4 LYSOZYME, APOLAR CAVITY, BURIED CHARGE, LIGAND BINDING, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3gum:B     (ILE3) to   (GLN105)  T4 LYSOZYME M102E/L99A MUTANT WITH BURIED CHARGE IN APOLAR CAVITY--P- XYLENE BINDING  |   T4 LYSOZYME, APOLAR CAVITY, BURIED CHARGE, LIGAND BINDING, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3gup:A     (ILE3) to   (GLN105)  T4 LYSOZYME M102E/L99A MUTANT WITH BURIED CHARGE IN APOLAR CAVITY-- PYRIDINE BINDING  |   T4 LYSOZYME, APOLAR CAVITY, BURIED CHARGE, LIGAND BINDING, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3gup:B     (ILE3) to   (GLN105)  T4 LYSOZYME M102E/L99A MUTANT WITH BURIED CHARGE IN APOLAR CAVITY-- PYRIDINE BINDING  |   T4 LYSOZYME, APOLAR CAVITY, BURIED CHARGE, LIGAND BINDING, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3guo:B     (ILE3) to   (GLN105)  T4 LYSOZYME M102E/L99A MUTANT WITH BURIED CHARGE IN APOLAR CAVITY-- PHENOL BINDING  |   T4 LYSOZYME, APOLAR CAVITY, BURIED CHARGE, LIGAND BINDING, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
2ray:X     (ILE3) to   (MET106)  BETA-CHLOROPHENETOLE IN COMPLEX WITH T4 LYSOZYME L99A  |   PROTEIN CAVITIES, HYDROLASE 
2rb0:X     (ILE3) to   (MET106)  2,6-DIFLUOROBENZYLBROMIDE COMPLEX WITH T4 LYSOZYME L99A  |   PROTEIN CAVITIES, HYDROLASE 
2rb2:X     (ILE3) to   (MET106)  3-METHYLBENZYLAZIDE IN COMPLEX WITH T4 LYSOZYME L99A  |   PROTEIN CAVITIES, HYDROLASE 
2rbn:A     (ILE3) to   (MET106)  N-PHENYLGLYCINONITRILE IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   PROTEIN CAVITIES, HYDROLASE 
2rbp:A     (ILE3) to   (GLY107)  2-(N-PROPYLTHIO)ETHANOL IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   PROTEIN CAVITIES, HYDROLASE 
2rbq:A     (ILE3) to   (MET106)  3-METHYLBENZYLAZIDE IN COMPLEX WITH T4 L99A/M102Q  |   PROTEIN CAVITIES, HYDROLASE 
2rbr:A     (ILE3) to   (GLY107)  2-PHENOXYETHANOL IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   PROTEIN CAVITIES, HYDROLASE 
2rbs:A     (ILE3) to   (MET106)  (R)(+)-3-CHLORO-1-PHENYL-1-PROPANOL IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   PROTEIN CAVITIES, HYDROLASE 
4yc4:A  (GLY1001) to  (MET1108)  CRYSTAL STRUCTURE OF PHOSPHATIDYL INOSITOL 4-KINASE II ALPHA IN COMPLEX WITH NUCLEOTIDE ANALOG  |   KINASE, COMPLEX, INHIBITOR, TRANSFERASE 
2rh1:A  (ILE1003) to  (MET1106)  HIGH RESOLUTION CRYSTAL STRUCTURE OF HUMAN B2-ADRENERGIC G PROTEIN- COUPLED RECEPTOR.  |   GPCR, 7TM, ADRENERGIC, FUSION, LIPIDIC CUBIC PHASE, LIPIDIC, MESOPHASE, CHOLESTEROL, MEMBRANE PROTEIN, MEMBRANE PROTEIN - HYDROLASE COMPLEX, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D 
1epy:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT, T21H/C54T/C97A/Q141H/T142H  |   METAL BINDING, HYDROLASE 
1qs5:A     (PHE4) to   (MET106)  THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME  |   STRAIN, STABILITY, MUTANT, T4 LYSOZYME, HYDROLASE 
1qs9:A     (ILE3) to   (MET106)  THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME  |   STRAIN, STABILITY, MUTANT, T4 LYSOZYME, HYDROLASE 
1qsb:A     (ILE3) to   (MET106)  THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME  |   STRAIN, STABILITY, MUTANT, T4 LYSOZYME, HYDROLASE 
1qsq:A     (ILE3) to   (GLY107)  CAVITY CREATING MUTATION  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, CAVITY MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1qt3:A     (ILE3) to   (MET106)  T26D MUTANT OF T4 LYSOZYME  |   HYDROLASE 
1qt4:A     (ILE3) to   (MET106)  T26Q MUTANT OF T4 LYSOZYME  |   HYDROLASE 
1qt5:A     (ILE3) to   (MET106)  D20E MUTANT STRUCTURE OF T4 LYSOZYME  |   HYDROLASE 
1qt7:A     (ILE3) to   (MET106)  E11N MUTANT OF T4 LYSOZYME  |   HYDROLASE 
1qt8:A     (ILE3) to   (MET106)  T26H MUTANT OF T4 LYSOZYME  |   HYDROLASE 
1qtd:A     (ASN2) to   (MET106)  THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME  |   STRAIN, STABILITY, MUTANT, T4 LYSOZYME, HYDROLASE 
1qth:A     (ILE3) to   (MET106)  THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME  |   STRAIN, STABILITY, MUTANT, T4 LYSOZYME, HYDROLASE 
1qtv:A     (ILE3) to   (MET106)  T26E APO STRUCTURE OF T4 LYSOZYME  |   HYDROLASE 
1qtz:A     (ILE3) to   (MET106)  D20C MUTANT OF T4 LYSOZYME  |   HYDROLASE 
1qud:A     (ILE3) to   (MET106)  L99G MUTANT OF T4 LYSOZYME  |   HYDROLASE 
1qug:A     (ILE3) to   (MET106)  E108V MUTANT OF T4 LYSOZYME  |   HYDROLASE 
1quh:A     (ILE3) to   (MET106)  L99G/E108V MUTANT OF T4 LYSOZYME  |   HYDROLASE 
3hh3:A     (ILE3) to   (MET106)  NEW AZABORINE COMPOUNDS BIND TO THE T4 LYSOZYME L99A CAVITY - 1,2-DIHYDRO-1,2-AZABORINE  |   AZABORINE, T4 LYSOZYME, LIGAND BINDING, HYDROPHOBIC CAVITY, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3hh4:A     (ILE3) to   (MET106)  NEW AZABORINE COMPOUNDS BIND TO THE T4 LYSOZYME L99A CAVITY - BENZENE AS CONTROL  |   AZABORINE, T4 LYSOZYME, LIGAND BINDING, HYDROPHOBIC CAVITY, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3hh5:A     (ILE3) to   (MET106)  NEW AZABORINE COMPOUNDS BIND TO THE T4 LYSOZYME L99A CAVITY - 1-ETHYL-2-HYDRO-1,2-AZABORINE  |   AZABORINE, T4 LYSOZYME, LIGAND BINDING, HYDROPHOBIC CAVITY, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3hh6:A     (ILE3) to   (MET106)  NEW AZABORINE COMPOUNDS BIND TO THE T4 LYSOZYME L99A CAVITY - ETHYLBENZENE AS CONTROL  |   AZABORINE, T4 LYSOZYME, LIGAND BINDING, HYDROPHOBIC CAVITY, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
2f2q:A     (ILE3) to   (MET117)  HIGH RESOLUTION CRYSTAL STRCUTURE OF T4 LYSOSYME MUTANT L20R63/A LIGANDED TO GUANIDINIUM ION  |   MOLECULAR SWITCH, T4 LYSOZYME, NANO-BITECHNOLOGY, PROTEIN ENGINEERING, PROTEIN DESIGN, HYDROLASE 
2f32:A     (ILE3) to   (MET117)  XRAY CRYSTAL STRUCTURE OF LYSOZYME MUTANT L20/R63A LIGANDED TO ETHYLGUANIDINIUM  |   MOLECULAR SWITCH, T4 LYSOZYME, NANO-BITECHNOLOGY, PROTEIN ENGINEERING, PROTEIN DESIGN, HYDROLASE 
2f47:A     (ILE3) to   (MET117)  XRAY CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT L20/R63A LIGANDED TO METHYLGUANIDINIUM  |   MOLECULAR SWITCH, T4 LYSOZYME, NANO-BITECHNOLOGY, PROTEIN ENGINEERING, PROTEIN DESIGN, HYDROLASE 
4yx7:C    (ILE36) to   (MET139)  COMPLEX OF SPAO(SPOA1,2) AND ORGB(APAR)::T4LYSOZYME FUSION PROTEIN  |   TYPE III SECRETION SYSTEM, PROTEIN TRANSPORT 
4yxa:F    (ILE36) to   (MET139)  COMPLEX OF SPAO(SPOA1,2 SEMET) AND ORGB(APAR)::T4LYSOZYME FUSION PROTEIN  |   TYPE III SECRETION SYSTEM, PROTEIN TRANSPORT 
4yxc:A    (ILE24) to   (MET127)  COMPLEX OF FLIM(SPOA)::FLIN FUSION PROTEIN AND FLIH(APAR)::T4LYSOZYME FUSION PROTEIN  |   TYPE III SECRETION SYSTEM, PROTEIN TRANSPORT 
1g06:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149S  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
1g07:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149C  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
1g0g:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152A  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
1g0j:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152S  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
1g0k:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152C  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
1g0l:A     (ILE3) to   (GLY107)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152V  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
1g1v:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/I58T  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, HYDRATED CAVITIES 
1g1w:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/Q105M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, HYDRATED CAVITIES 
3uon:A  (ASN1002) to  (MET1106)  STRUCTURE OF THE HUMAN M2 MUSCARINIC ACETYLCHOLINE RECEPTOR BOUND TO AN ANTAGONIST  |   G PROTEIN-COUPLED RECEPTOR, GPCR, ACETYLCHOLINE RECEPTOR, SIGNALING PROTEIN-ANTAGONIST COMPLEX 
3ht6:A     (ILE3) to   (MET106)  2-METHYLPHENOL IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3ht7:A     (ILE3) to   (MET106)  2-ETHYLPHENOL IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3ht8:A     (ILE3) to   (MET106)  5-CHLORO-2-METHYLPHENOL IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL, HYDROLASE 
3ht9:A     (ILE3) to   (MET106)  2-METHOXYPHENOL IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL, HYDROLASE 
3htb:A     (ILE3) to   (MET106)  2-PROPYLPHENOL IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3htd:A     (ILE3) to   (MET106)  (Z)-THIOPHENE-2-CARBOXALDOXIME IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3htf:A     (ILE3) to   (MET106)  4-CHLORO-1H-PYRAZOLE IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3htg:A     (ILE3) to   (MET106)  2-ETHOXY-3,4-DIHYDRO-2H-PYRAN IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3hu8:A     (ILE3) to   (MET106)  2-ETHOXYPHENOL IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3hu9:A     (ILE3) to   (MET106)  NITROSOBENZENE IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3hua:A     (ILE3) to   (GLY107)  4,5,6,7-TETRAHYDROINDOLE IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3huk:A     (ILE3) to   (MET106)  BENZYLACETATE IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3huq:A     (ILE3) to   (MET106)  THIENO[3,2-B]THIOPHENE IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   HYDROLASE,GLYCOSIDASE, BACTERIOLYTIC ENZYME, ANTIMICROBIAL 
3hwl:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF T4 LYSOZYME WITH THE UNNATURAL AMINO ACID P- ACETYL-L-PHENYLALANINE INCORPORATED AT POSITION 131  |   UNNATURAL AMINO ACID, P-ACETYL-PHENYLALANINE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
1ssw:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF PHAGE T4 LYSOZYME MUTANT Y24A/Y25A/T26A/I27A/C54T/C97A  |   HYDROLASE, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
1ssy:A     (ASN2) to   (MET106)  CRYSTAL STRUCTURE OF PHAGE T4 LYSOZYME MUTANT G28A/I29A/G30A/C54T/C97A  |   HYDROLASE, GLYCOSIDASE, BACTERIOLYTIC ENZYME, 3D-STRUCTURE 
1ssy:B     (ILE3) to   (GLY107)  CRYSTAL STRUCTURE OF PHAGE T4 LYSOZYME MUTANT G28A/I29A/G30A/C54T/C97A  |   HYDROLASE, GLYCOSIDASE, BACTERIOLYTIC ENZYME, 3D-STRUCTURE 
1sx2:A     (ILE3) to   (GLY107)  USE OF A HALIDE BINDING SITE TO BYPASS THE 1000-ATOM LIMIT TO STRUCTURE DETERMINATION BY DIRECT METHODS  |   RB+ BINDING SITES; AB INITIO DIRECT METHODS, HYDROLASE 
1t6h:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE T4 LYSOZYME INCORPORATING AN UNNATURAL AMINO ACID P-IODO-L-PHENYLALANINE AT POSITION 153  |   IODOPHE, SAD PHASING, UNNATURAL AMINO ACID, HYDROLASE 
1t8a:A     (ILE3) to   (MET117)  USE OF SEQUENCE DUPLICATION TO ENGINEER A LIGAND-TRIGGERED LONG-DISTANCE MOLECULAR SWITCH IN T4 LYSOSYME  |   MOLECULAR SWITCH, T4 LYSOZYME, NANO-BITECHNOLOGY, PROTEIN ENGINEERING, PROTEIN DESIGN, HYDROLASE 
1t97:A     (ILE3) to   (MET117)  USE OF SEQUENCE DUPLICATION TO ENGINEER A LIGAND-TRIGGERED LONG-DISTANCE MOLECULAR SWITCH IN T4 LYSOSYME  |   MOLECULAR SWITCH, T4 LYSOZYME, NANO-BIOTECHNOLOGY, PROTEIN ENGINEERING, PROTEIN DESIGN, SEQUENCE DUPLICATION, HYDROLASE 
4ldl:A   (PHE869) to   (MET971)  STRUCTURE OF BETA2 ADRENOCEPTOR BOUND TO HYDROXYBENZYLISOPROTERENOL AND AN ENGINEERED NANOBODY  |   G PROTEIN COUPLED RECEPTOR, MEMBRANE PROTEIN-HYDROLASE COMPLEX 
1tla:A     (ILE3) to   (MET106)  HYDROPHOBIC CORE REPACKING AND AROMATIC-AROMATIC INTERACTION IN THE THERMOSTABLE MUTANT OF T4 LYSOZYME SER 117 (RIGHT ARROW) PHE  |   HYDROLASE (O-GLYCOSYL) 
3vw7:A  (ILE1003) to  (MET1106)  CRYSTAL STRUCTURE OF HUMAN PROTEASE-ACTIVATED RECEPTOR 1 (PAR1) BOUND WITH ANTAGONIST VORAPAXAR AT 2.2 ANGSTROM  |   HIGH RESOLUTION STRUCTURE, PROTEASE-ACTIVATED RECEPTOR 1, INACTIVE CONFORMATION, ANTAGONIST VORAPAXAR, G PROTEIN-COUPLED RECEPTOR, SIGNALING PROTEIN, MEMBRANE PROTEIN, THROMBIN RECEPTOR-ANTAGONIST COMPLEX, SIGNALING PROTEIN-ANTAGONIST COMPLEX 
2huk:A     (ILE3) to   (GLN105)  CRYSTAL STRUCTURE OF T4 LYSOZYME V131C SYNTHETIC DIMER  |   T4 LYSOZYME SYNTHETIC DIMER, HYDROLASE 
2igc:A     (ILE3) to   (MET106)  STRUCTURE OF SPIN LABELED T4 LYSOZYME MUTANT T115R1A  |   NITROXIDE, SPIN LABEL, EPR, T4 LYSOZYME, HYDROLASE 
1jqu:A     (ASN2) to   (MET106)  ARE CARBOXY TERMINII OF HELICES CODED BY THE LOCAL SEQUENCE OR BY TERTIARY STRUCTURE CONTACTS  |   GLYCINE HELIX TERMINII, SCHELLMAN MOTIF, ALPHA-L MOTIF, HYDROLASE 
1jqu:B     (ILE3) to   (MET106)  ARE CARBOXY TERMINII OF HELICES CODED BY THE LOCAL SEQUENCE OR BY TERTIARY STRUCTURE CONTACTS  |   GLYCINE HELIX TERMINII, SCHELLMAN MOTIF, ALPHA-L MOTIF, HYDROLASE 
1jqu:D     (ASN2) to   (MET106)  ARE CARBOXY TERMINII OF HELICES CODED BY THE LOCAL SEQUENCE OR BY TERTIARY STRUCTURE CONTACTS  |   GLYCINE HELIX TERMINII, SCHELLMAN MOTIF, ALPHA-L MOTIF, HYDROLASE 
1jtm:A     (ILE3) to   (GLY107)  ALTERNATIVE STRUCTURES OF A SEQUENCE EXTENDED T4 LYSOZYME SHOW THAT THE HIGHLY CONSERVED BETA-SHEET HAS WEAK INTRINSIC FOLDING PROPENSITY  |   SEQUENCE DUPLICATION, CONTEXT DEPENDENT FOLDING, SEQUENCE REPEAT, HYDROLASE 
1jtn:A     (ASN2) to   (MET106)  ALTERNATIVE STRUCTURES OF A SEQUENCE EXTENDED T4 LYSOZYME SHOW THAT THE HIGHLY CONSERVED BETA-SHEET REGION HAS WEAK INTRINSIC FOLDING PROPENSITY  |   SEQUENCE DUPLICATION, CONTEXT DEPENDENT FOLDING, SEQUENCE REPEAT, HYDROLASE 
1jtn:B     (PHE4) to   (GLY107)  ALTERNATIVE STRUCTURES OF A SEQUENCE EXTENDED T4 LYSOZYME SHOW THAT THE HIGHLY CONSERVED BETA-SHEET REGION HAS WEAK INTRINSIC FOLDING PROPENSITY  |   SEQUENCE DUPLICATION, CONTEXT DEPENDENT FOLDING, SEQUENCE REPEAT, HYDROLASE 
5bz6:A     (PHE4) to   (MET106)  CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN SINGLE MUTANT (S92A) OF THE HUMAN MITOCHONDRIAL CALCIUM UNIPORTER FUSED WITH T4 LYSOZYME  |   MEMBRANE PROTEIN, CALCIUM CHANNEL, MITOCHONDRIA, TRANSPORT PROTEIN 
2lcb:A     (ILE3) to   (PHE104)  SOLUTION STRUCTURE OF A MINOR AND TRANSIENTLY FORMED STATE OF A T4 LYSOZYME MUTANT  |   EXCITED STATE, HYDROLASE 
2lzm:A     (ILE3) to   (GLY107)  STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME REFINED AT 1.7 ANGSTROMS RESOLUTION  |   HYDROLASE (O-GLYCOSYL) 
1ks3:A     (ILE3) to   (MET106)  METHIONINE CORE MUTANT OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1kw5:A     (ILE3) to   (MET106)  METHIONINE CORE MUTANT OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1kw7:A     (ILE3) to   (MET106)  METHIONINE CORE MUTANT OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1ky0:A     (ILE3) to   (MET106)  METHIONINE CORE MUTANT OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1ky1:A     (ILE3) to   (MET106)  METHIONINE CORE MUTANT OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1l00:A     (ILE3) to   (MET106)  PERTURBATION OF TRP 138 IN T4 LYSOZYME BY MUTATIONS AT GLN 105 USED TO CORRELATE CHANGES IN STRUCTURE, STABILITY, SOLVATION, AND SPECTROSCOPIC PROPERTIES  |   HYDROLASE(O-GLYCOSYL) 
1l01:A     (ILE3) to   (GLY107)  STRUCTURAL STUDIES OF MUTANTS OF THE LYSOZYME OF BACTERIOPHAGE T4. THE TEMPERATURE-SENSITIVE MUTANT PROTEIN THR157 (RIGHT ARROW) ILE  |   HYDROLASE (O-GLYCOSYL) 
1l02:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l03:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l04:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l05:A     (ILE3) to   (MET106)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l06:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l07:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l08:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l09:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l0j:A     (ILE3) to   (MET106)  METHIONINE CORE MUTANT OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1l0k:A     (ILE3) to   (MET106)  METHIONINE CORE MUTANT OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1l10:A     (ILE3) to   (GLY107)  STRUCTURAL STUDIES OF MUTANTS OF THE LYSOZYME OF BACTERIOPHAGE T4. THE TEMPERATURE-SENSITIVE MUTANT PROTEIN THR157 (RIGHT ARROW) ILE  |   HYDROLASE (O-GLYCOSYL) 
1l12:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l13:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l15:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l17:A     (VAL3) to   (GLY107)  HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3  |   HYDROLASE (O-GLYCOSYL) 
1l18:A     (TYR3) to   (GLY107)  HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3  |   HYDROLASE (O-GLYCOSYL) 
1l19:A     (ILE3) to   (GLY107)  ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES  |   HYDROLASE (O-GLYCOSYL) 
1l20:A     (ILE3) to   (GLY107)  ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES  |   HYDROLASE (O-GLYCOSYL) 
1l21:A     (ILE3) to   (GLN105)  CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l23:A     (ILE3) to   (GLY107)  ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING  |   HYDROLASE (O-GLYCOSYL) 
1l24:A     (ILE3) to   (GLY107)  ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING  |   HYDROLASE (O-GLYCOSYL) 
1l25:A     (ILE3) to   (MET106)  REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l26:A     (ILE3) to   (GLY107)  REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l27:A     (ILE3) to   (GLY107)  REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l29:A     (ILE3) to   (GLY107)  REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l30:A     (ILE3) to   (GLY107)  REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l31:A     (ILE3) to   (GLY107)  REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l32:A     (ILE3) to   (GLY107)  REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l34:A     (ILE3) to   (GLY107)  HIGH-RESOLUTION STRUCTURE OF THE TEMPERATURE-SENSITIVE MUTANT OF PHAGE LYSOZYME, ARG 96 (RIGHT ARROW) HIS  |   HYDROLASE (O-GLYCOSYL) 
1l35:A     (ILE3) to   (MET106)  STRUCTURE OF A THERMOSTABLE DISULFIDE-BRIDGE MUTANT OF PHAGE T4 LYSOZYME SHOWS THAT AN ENGINEERED CROSSLINK IN A FLEXIBLE REGION DOES NOT INCREASE THE RIGIDITY OF THE FOLDED PROTEIN  |   HYDROLASE (O-GLYCOSYL) 
1l36:A     (ILE3) to   (MET106)  TOWARD A SIMPLIFICATION OF THE PROTEIN FOLDING PROBLEM: A STABILIZING POLYALANINE ALPHA-HELIX ENGINEERED IN T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l37:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS  |   HYDROLASE (O-GLYCOSYL) 
1l38:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS  |   HYDROLASE (O-GLYCOSYL) 
1l39:A     (ILE3) to   (MET106)  CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS  |   HYDROLASE (O-GLYCOSYL) 
1l41:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS  |   HYDROLASE (O-GLYCOSYL) 
1l42:A     (ILE3) to   (GLY107)  CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l43:A     (ILE3) to   (GLY107)  CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l45:A     (ILE3) to   (GLY107)  CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l47:A     (ILE3) to   (GLY107)  CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l48:A     (ILE3) to   (MET106)  STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA- HELICES IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l49:A     (ILE3) to   (MET106)  STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA- HELICES IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l50:A     (ILE3) to   (MET106)  STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA- HELICES IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l51:A     (ILE3) to   (MET106)  STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA- HELICES IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l52:A     (ILE3) to   (MET106)  STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA- HELICES IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l53:A     (ILE3) to   (GLY107)  STRUCTURAL AND THERMODYNAMIC ANALYSIS OF THE PACKING OF TWO ALPHA- HELICES IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l54:A     (PHE4) to   (MET106)  THE STRUCTURAL AND THERMODYNAMIC CONSEQUENCES OF BURYING A CHARGED RESIDUE WITHIN THE HYDROPHOBIC CORE OF T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l55:A     (ILE3) to   (MET106)  ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l57:A     (ILE3) to   (GLY107)  ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l58:A     (ILE3) to   (MET106)  ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l59:A     (ILE3) to   (MET106)  ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
2ntg:A     (ILE3) to   (MET106)  STRUCTURE OF SPIN-LABELED T4 LYSOZYME MUTANT T115R7  |   NITROXIDE, SPIN LABEL, T4 LYSOZYME, ELECTRON PARAMAGNETIC RESONANCE, EPR, HYDROLASE 
2nth:A     (ILE3) to   (MET106)  STRUCTURE OF SPIN-LABELED T4 LYSOZYME MUTANT L118R1  |   NITROXIDE, SPIN LABEL, T4 LYSOZYME, ELECTRON PARAMAGNETIC RESONANCE, EPR, HYDROLASE 
1l60:A     (ILE3) to   (GLY107)  ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l62:A     (ILE3) to   (GLY107)  ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l64:A     (ILE3) to   (MET106)  TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES  |   HYDROLASE (O-GLYCOSYL) 
1l65:A     (ILE3) to   (GLY107)  TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES  |   HYDROLASE (O-GLYCOSYL) 
1l67:A     (ILE3) to   (MET106)  TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES  |   HYDROLASE (O-GLYCOSYL) 
1l68:A     (ILE3) to   (MET106)  TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES  |   HYDROLASE (O-GLYCOSYL) 
1l69:A     (ILE3) to   (GLY107)  MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA- HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l70:A     (ILE3) to   (GLY107)  MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA- HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l71:A     (ILE3) to   (GLY107)  MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA- HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l72:A     (ILE3) to   (GLY107)  MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA- HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l73:A     (ILE3) to   (MET106)  MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA- HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l74:A     (ILE3) to   (MET106)  MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA- HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l75:A     (ASN2) to   (MET106)  MULTIPLE STABILIZING ALANINE REPLACEMENTS WITHIN ALPHA- HELIX 126-134 OF T4 LYSOZYME HAVE INDEPENDENT, ADDITIVE EFFECTS ON BOTH STRUCTURE AND STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l76:A     (ILE3) to   (GLY107)  TOLERANCE OF T4 LYSOZYME TO PROLINE SUBSTITUTIONS WITHIN THE LONG INTERDOMAIN ALPHA-HELIX ILLUSTRATES THE ADAPTABILITY OF PROTEINS TO POTENTIALLY DESTABILIZING LESIONS  |   HYDROLASE (O-GLYCOSYL) 
1l77:A     (ILE3) to   (MET106)  DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l79:A     (ILE3) to   (GLY107)  DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l80:A     (ILE3) to   (MET106)  DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l81:A     (ILE3) to   (MET106)  DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l82:A     (ILE3) to   (MET106)  DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l83:A     (ILE3) to   (GLY107)  A CAVITY-CONTAINING MUTANT OF T4 LYSOZYME IS STABILIZED BY BURIED BENZENE  |   HYDROLASE(O-GLYCOSYL) 
1l85:A     (ILE3) to   (MET106)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l87:A     (ILE3) to   (GLY107)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l88:A     (ILE3) to   (MET106)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l89:A     (ILE3) to   (MET106)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l91:A     (ILE3) to   (GLY107)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l93:A     (ILE3) to   (MET106)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l94:A     (ILE3) to   (MET106)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l95:A     (ILE3) to   (GLY107)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l98:A     (ILE3) to   (GLY107)  PERTURBATION OF TRP 138 IN T4 LYSOZYME BY MUTATIONS AT GLN 105 USED TO CORRELATE CHANGES IN STRUCTURE, STABILITY, SOLVATION, AND SPECTROSCOPIC PROPERTIES  |   HYDROLASE(O-GLYCOSYL) 
1l99:A     (ILE3) to   (GLY107)  PERTURBATION OF TRP 138 IN T4 LYSOZYME BY MUTATIONS AT GLN 105 USED TO CORRELATE CHANGES IN STRUCTURE, STABILITY, SOLVATION, AND SPECTROSCOPIC PROPERTIES  |   HYDROLASE(O-GLYCOSYL) 
5cgd:A   (ILE642) to  (MET1106)  STRUCTURE OF THE HUMAN CLASS C GPCR METABOTROPIC GLUTAMATE RECEPTOR 5 TRANSMEMBRANE DOMAIN IN COMPLEX WITH THE NEGATIVE ALLOSTERIC MODULATOR 3-CHLORO-5-[6-(5-FLUOROPYRIDIN-2-YL)PYRIMIDIN-4- YL]BENZONITRILE - (HTL14242)  |   7TM, RECEPTOR, GPCR, MEMBRANE-PROTEIN, SIGNALING PROTEIN 
1lgu:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A/M102Q  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1lgw:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A/M102Q BOUND BY 2-FLUOROANILINE  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1lgx:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A/M102Q BOUND BY 3,5-DIFLUOROANILINE  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1li2:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A/M102Q BOUND BY PHENOL  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1li3:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A/M102Q BOUND BY 3-CHLOROPHENOL  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1li6:A     (ILE3) to   (GLY107)  T4 LYSOZYME MUTANT L99A/M102Q BOUND BY 5-METHYLPYRROLE  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1llh:A     (ILE3) to   (MET106)  ARE CARBOXY TERMINII OF HELICES CODED BY THE LOCAL SEQUENCE OR BY TERTIARY STRUCTURE CONTACTS  |   HELIX TERMINII, SCHELLMAN MOTIF, ALPHA-L MOTIF, HYDROLASE 
2z6b:A   (SER175) to   (MET284)  CRYSTAL STRUCTURE ANALYSIS OF (GP27-GP5)3 CONJUGATED WITH FE(III) PROTOPORPHYRIN  |   PROTEIN CONTAINING METAL COMPLEXES, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE, LATE PROTEIN, VIRION, HYDROLASE/STRUCTURAL PROTEIN COMPLEX 
1lpy:A     (ILE3) to   (MSE106)  MULTIPLE METHIONINE SUBSTITUTIONS IN T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1lw9:A     (ILE3) to   (MET106)  MULTIPLE METHIONINE SUBSTITUTIONS ARE TOLERATED IN T4 LYSOZYME AND HAVE COUPLED EFFECTS ON FOLDING AND STABILITY  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1lwg:A     (ILE3) to   (MET106)  MULTIPLE METHIONINE SUBSTITUTIONS ARE TOLERATED IN T4 LYSOZYME AND HAVE COUPLED EFFECTS ON FOLDING AND STABILITY  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING, HYDROLASE 
1lwk:A     (ILE3) to   (MSE106)  MULTIPLE METHIONINE SUBSTITUTIONS ARE TOLERATED IN T4 LYSOZYME AND HAVE COUPLED EFFECTS ON FOLDING AND STABILITY  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1lyd:A     (ILE3) to   (GLY107)  CRYSTAL STRUCTURE OF T4-LYSOZYME GENERATED FROM SYNTHETIC CODING DNA EXPRESSED IN ESCHERICHIA COLI  |   HYDROLASE (O-GLYCOSYL) 
1lyf:A     (ILE3) to   (MET106)  DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59  |   HYDROLASE(O-GLYCOSYL) 
1lyg:A     (ILE3) to   (GLY107)  DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59  |   HYDROLASE(O-GLYCOSYL) 
1lyh:A     (ILE3) to   (MET106)  DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59  |   HYDROLASE(O-GLYCOSYL) 
1lyi:A     (ILE3) to   (GLY107)  DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59  |   HYDROLASE(O-GLYCOSYL) 
1lyj:A     (ILE3) to   (GLY107)  DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59  |   HYDROLASE(O-GLYCOSYL) 
2o79:A     (ILE3) to   (MET106)  T4 LYSOZYME WITH C-TERMINAL EXTENSION  |   PROTEIN STABILITY, PROTEIN FOLDING, LYSOZYME, CIRCULAR PERMUTANT, HYDROLASE 
4oo9:A   (ILE642) to  (MET1106)  STRUCTURE OF THE HUMAN CLASS C GPCR METABOTROPIC GLUTAMATE RECEPTOR 5 TRANSMEMBRANE DOMAIN IN COMPLEX WITH THE NEGATIVE ALLOSTERIC MODULATOR MAVOGLURANT  |   7TM, RECEPTOR, G-PROTEIN, CYSTEINE-S-ACETAMIDE, MEMBRANE PROTEIN 
5d5a:A  (ASN1002) to  (MET1106)  IN MESO IN SITU SERIAL X-RAY CRYSTALLOGRAPHY STRUCTURE OF THE BETA2- ADRENERGIC RECEPTOR AT 100 K  |   MEMBRANE PROTEIN, HYDROLASE, MEMBRANE PROTEIN-HYDROLASE COMPLEX 
3l2x:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF SPIN LABELED T4 LYSOZYME MUTANT 115-119RX  |   HYDROLASE, NITROXIDE SPIN LABEL, EPR, MODIFIED CYSTEINE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE 
3l64:A     (ILE3) to   (MET106)  T4 LYSOZYME S44E/WT*  |   HYDROLASE (O-GLYCOSYL), ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
4pla:A  (GLY1001) to  (MET1108)  CRYSTAL STRUCTURE OF PHOSPHATIDYL INOSITOL 4-KINASE II ALPHA IN COMPLEX WITH ATP  |   PHOSPHATIDYL INOSITOL, 4-KINASE, ATP, LIPID, TRANSFERASE, HYDROLASE 
1zur:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF SPIN LABELED T4 LYSOZYME (V131R1F)  |   NITROXIDE SPIN LABEL, EPR, MODIFIED CYSTEINE, HYDROLASE 
1zwn:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF SPIN LABELED T4 LYSOZYME (V131R1B)  |   NITROXIDE SPIN LABEL, EPR, MODIFIED CYSTEINE, HYDROLASE 
1zyt:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF SPIN LABELED T4 LYSOZYME (A82R1)  |   NITROXIDE SPIN LABEL, MODIFIED CYSTEINE, HYDROLASE 
200l:A     (ILE3) to   (MET106)  THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME  |   CAVITIES, CORE-PACKING, PROTEIN STABILITY, HYDROLASE (O- GLYCOSYL) 
201l:A     (PHE4) to   (MET106)  HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
201l:B     (ILE3) to   (MET106)  HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
210l:A     (ILE3) to   (MET106)  PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), M13 PLASMID, BACTERIOLYTIC ENZYME 
212l:A     (ILE3) to   (MET106)  PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), GLYCOSIDASE, BACTERIOLYTIC ENZYME 
213l:A     (ILE3) to   (MET106)  PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), GLYCOSIDASE, BACTERIOLYTIC ENZYME 
214l:A     (ILE3) to   (MET106)  PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), GLYCOSIDASE, BACTERIOLYTIC ENZYME 
218l:A     (ILE3) to   (MET106)  PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), GLYCOSIDASE, BACTERIOLYTIC ENZYME 
219l:A     (ILE3) to   (MET106)  PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), GLYCOSIDASE, BACTERIOLYTIC ENZYME 
220l:A     (ILE3) to   (MET106)  GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS  |   HYDROLASE, O-GLYCOSYL, T4 LYSOZYME, CAVITY MUTANTS, LIGAND BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
222l:A     (ILE3) to   (MET106)  GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS  |   HYDROLASE, O-GLYCOSYL, T4 LYSOZYME, CAVITY MUTANTS, LIGAND BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
223l:A     (ILE3) to   (MET106)  GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS  |   HYDROLASE, O-GLYCOSYL, T4 LYSOZYME, CAVITY MUTANTS, LIGAND BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
224l:A     (ILE3) to   (MET106)  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  |   HYDROLASE(O-GLYCOSYL) 
225l:A     (ILE3) to   (GLY107)  GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS  |   HYDROLASE, O-GLYCOSYL, T4 LYSOZYME, CAVITY MUTANTS, LIGAND BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
227l:A     (ILE3) to   (MET106)  GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS  |   HYDROLASE, O-GLYCOSYL, T4 LYSOZYME, CAVITY MUTANTS, LIGAND BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
228l:A     (ILE3) to   (GLY107)  GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS  |   HYDROLASE, O-GLYCOSYL, T4 LYSOZYME, CAVITY MUTANTS, LIGAND BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
229l:A     (ILE3) to   (GLY107)  GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS  |   HYDROLASE, O-GLYCOSYL, T4 LYSOZYME, CAVITY MUTANTS, LIGAND BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
230l:A     (ASN2) to   (MET106)  T4 LYSOZYME MUTANT M6L  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE 
232l:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT M120K  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE 
233l:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT M120L  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE 
235l:A     (ILE3) to   (GLY107)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
236l:A     (ILE3) to   (GLY107)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
237l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
238l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
239l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
240l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
241l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
242l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
244l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
245l:A     (ASN2) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
247l:A     (ILE3) to   (GLY107)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
248l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
250l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
252l:A     (ILE3) to   (GLY107)  GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS  |   HYDROLASE, O-GLYCOSYL, T4 LYSOZYME, CAVITY MUTANTS, LIGAND BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN, MULTIPLE CONFORMATIONS 
253l:A     (ILE3) to   (MET106)  LYSOZYME  |   HYDROLASE, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
254l:A     (ILE3) to   (MET106)  LYSOZYME  |   HYDROLASE, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
255l:A     (ILE3) to   (MET106)  HYDROLASE  |   HYDROLASE, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
256l:A     (ILE3) to   (MET106)  BACTERIOPHAGE T4 LYSOZYME  |   LYSOZYME, HYDROLASE 
257l:A     (ILE3) to   (MET106)  AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METAL BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
258l:A     (ILE3) to   (MET106)  AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METAL BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
259l:A     (ILE3) to   (MET106)  AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METAL BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
260l:A     (ILE3) to   (GLY107)  AN ADAPTABLE METAL-BINDING SITE ENGINEERED INTO T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METAL BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN, HYDROLASE 
262l:A     (ASN2) to   (MET117)  STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, ENGINEERED TANDEM REPEAT, PROTEIN ENGINEERING, PROTEIN DESIGN 
262l:B     (ILE3) to   (MET117)  STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, ENGINEERED TANDEM REPEAT, PROTEIN ENGINEERING, PROTEIN DESIGN 
3lzm:A     (ILE3) to   (GLY107)  STRUCTURAL STUDIES OF MUTANTS OF T4 LYSOZYME THAT ALTER HYDROPHOBIC STABILIZATION  |   HYDROLASE (O-GLYCOSYL) 
2a4t:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF SPIN LABELED T4 LYSOZYME (V131R7)  |   NITROXIDE SPIN LABEL, EPR, MODIFIED CYSTEINE, HYDROLASE 
4qkx:A   (ILE868) to   (MET971)  STRUCTURE OF BETA2 ADRENOCEPTOR BOUND TO A COVALENT AGONIST AND AN ENGINEERED NANOBODY  |   7-TRANSMEMBRANE HELICES, SIGNAL TRANSDUCTION, G PROTEINS, MEMBRANE, MEMBRANE PROTEIN-IMMUNE SYSTEM COMPLEX 
3c7w:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF ALL 20 AMINO ACIDS AT SITE 96 TO THE STABILITY AND STRUCTURE OF T4 LYSOZYME  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE- SENSITIVE MUTANT, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3c7y:A     (ILE3) to   (MET106)  MUTANT R96A OF T4 LYSOZYME IN WILDTYPE BACKGROUND AT 298K  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE- SENSITIVE MUTANT, HYDROLASE 
3c7z:A     (ILE3) to   (GLY107)  T4 LYSOZYME MUTANT D89A/R96H AT ROOM TEMPERATURE  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE- SENSITIVE MUTANT, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3c80:A     (ILE3) to   (GLN105)  T4 LYSOZYME MUTANT R96Y AT ROOM TEMPERATURE  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE- SENSITIVE MUTANT, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3c81:A     (ILE3) to   (GLY107)  MUTANT K85A OF T4 LYSOZYME IN WILDTYPE BACKGROUND AT ROOM TEMPERATURE  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE- SENSITIVE MUTANT, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3c82:A     (ILE3) to   (GLY107)  BACTERIOPHAGE LYSOZYME T4 LYSOZYME MUTANT K85A/R96H  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE- SENSITIVE MUTANT, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3c83:A     (ILE3) to   (GLY107)  BACTERIOPHAGE T4 LYSOZYME MUTANT D89A IN WILDTYPE BACKGROUND AT ROOM TEMPERATURE  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE- SENSITIVE MUTANT, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3c8q:A     (ILE3) to   (GLY107)  CONTRIBUTION OF ALL 20 AMINO ACIDS AT SITE 96 TO THE STABILITY AND STRUCTURE OF T4 LYSOZYME  |   ELECTROSTATICS, MUTATIONAL ANALYSIS, CHARGE BURIAL, THERMAL STABILITY, STERIC STRAIN, HYDROGEN BONDING, PKA SHIFT, T4 LYSOZYME, PROTEIN ENGINEERING, ELECTROSTATIC CALCULATIONS, HYDROLASE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE 
3c8r:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF ALL 20 AMINO ACIDS AT SITE 96 TO STABILITY AND STRUCTURE OF T4 LYSOZYME  |   R96G, T4 LYSOZYME, PROTEIN ELECTROSTATICS, PROTEIN ENGINEERING, PROTEIN STABILITY, STRAIN, TEMPERATURE- SENSITIVE MUTANT, THERMAL STABILITY, HYDROGEN BONDING, CHARGE BURIAL, PROTEIN STRUCTURE, HYDROLASE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE 
3c8s:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF ALL 20 AMINO ACIDS AT SITE 96 TO THE STABILITY AND STRUCTURE OF T4 LYSOZYME  |   T4 LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE-SENSITIVE MUTANT, HYDROLASE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE 
3cdo:A     (ILE3) to   (GLY107)  BACTERIOPHAGE T4 LYSOZYME MUTANT R96V IN WILDTYPE BACKGROUND AT LOW TEMPERATURE  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE-SENSITIVE MUTANT, PHOSPHATE BINDING SITE, MPD BINDING SITE, CHLORIDE BINDING SITE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3cdo:B     (ILE3) to   (MET106)  BACTERIOPHAGE T4 LYSOZYME MUTANT R96V IN WILDTYPE BACKGROUND AT LOW TEMPERATURE  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE-SENSITIVE MUTANT, PHOSPHATE BINDING SITE, MPD BINDING SITE, CHLORIDE BINDING SITE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3cdo:C     (PHE4) to   (GLY107)  BACTERIOPHAGE T4 LYSOZYME MUTANT R96V IN WILDTYPE BACKGROUND AT LOW TEMPERATURE  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE-SENSITIVE MUTANT, PHOSPHATE BINDING SITE, MPD BINDING SITE, CHLORIDE BINDING SITE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3cdo:D     (ILE3) to   (GLY107)  BACTERIOPHAGE T4 LYSOZYME MUTANT R96V IN WILDTYPE BACKGROUND AT LOW TEMPERATURE  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE-SENSITIVE MUTANT, PHOSPHATE BINDING SITE, MPD BINDING SITE, CHLORIDE BINDING SITE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3cdq:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF ALL 20 AMINO ACIDS AT SITE 96 TO THE STABILITY AND STRUCTURE OF T4 LYSOZYME  |   T4 LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE-SENSITIVE MUTANT, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3cdr:A     (ILE3) to   (GLY107)  R96Q MUTANT OF WILDTYPE PHAGE T4 LYSOZYME AT 298 K  |   T4 LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE-SENSITIVE MUTANT, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3cdv:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF ALL 20 AMINO ACIDS AT SITE 96 TO THE STABILITY AND STRUCTURE OF T4 LYSOZYME  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERING, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE- SENSITIVE MUTANT, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3ny8:A  (ILE1003) to  (MET1106)  CRYSTAL STRUCTURE OF THE HUMAN BETA2 ADRENERGIC RECEPTOR IN COMPLEX WITH THE INVERSE AGONIST ICI 118,551  |   G PROTEIN-COUPLED RECEPTOR, LYSOZYME, FUSION, TRANSDUCER, ADRENERGIC, G-PROTEINS, ARRESTINS, ADRENALIN, ICI 118,551, GLYCOSYLATION, PALMITOYLATION, PHOSPHORYLATION, MEMBRANE PROTEIN, HYDROLASE, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D 
4s0w:A     (ILE3) to   (MET106)  WILD TYPE T4 LYSOZYME STRUCTURE  |   HYDROLASE 
5g27:A     (ILE3) to   (MET106)  STRUCTURE OF SPIN-LABELLED T4 LYSOZYME MUTANT L118C-R1 AT ROOM TEMPERATURE  |   HYDROLASE, T4 LYSOZYME, EPR, ESR, ELECTRON, PARAMAGNETIC, SPIN, RESONANCE, LABELLING 
3d4s:A  (ILE1003) to  (MET1106)  CHOLESTEROL BOUND FORM OF HUMAN BETA2 ADRENERGIC RECEPTOR.  |   GPCR, MEMBRANE PROTEIN, LYSOZYME, FUSION, ADRENERGIC, TIMOLOL, G- PROTEIN COUPLED RECEPTOR, GLYCOPROTEIN, LIPOPROTEIN, PALMITATE, PHOSPHOPROTEIN, RECEPTOR, TRANSDUCER, TRANSMEMBRANE, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D 
4tn3:A   (ASN305) to   (MET409)  STRUCTURE OF THE BBOX-COILED-COIL REGION OF RHESUS TRIM5ALPHA  |   TRIM PROTEIN COILED-COIL SCAFFOLD RETROVIRAL RESTRICTION FACTOR, ANTIVIRAL PROTEIN 
3oe8:C  (ILE1003) to  (MET1106)  CRYSTAL STRUCTURE OF THE CXCR4 CHEMOKINE RECEPTOR IN COMPLEX WITH A SMALL MOLECULE ANTAGONIST IT1T IN P1 SPACEGROUP  |   STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D, 7TM, G PROTEIN-COUPLED RECEPTOR, GPCR, SIGNAL TRANSDUCTION, HYDROLASE, CANCER, HIV-1 CO-RECEPTOR, CHEMOTAXIS, CHEMOKINE, CXCL12, SDF1, ISOTHIOUREA, CHIMERA, T4L FUSION, MEMBRANE PROTEIN, TRANSMEMBRANE, SINGNALING PROTEIN, PSI-BIOLOGY, GPCR NETWORK, SIGNALING PROTEIN 
5glh:A   (CYS283) to  (MET1106)  HUMAN ENDOTHELIN RECEPTOR TYPE-B IN COMPLEX WITH ET-1  |   ALPHA HELICAL, SIGNALING PROTEIN 
3dke:X     (ILE3) to   (MSE106)  POLAR AND NON-POLAR CAVITIES IN PHAGE T4 LYSOZYME  |   T4 LYSOZYME, CAVITY, EXPERIMENTAL PHASES, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3dmv:A     (ILE3) to   (MET106)  FREE OF LIGAND BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT  |   T4 LYSOZYME, HALOGEN BOND, CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3dmx:A     (ILE3) to   (MET106)  BENZENE BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT  |   T4 LYSOZYME, HALOGEN BOND, HYDROPHOBIC CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3dmz:A     (ILE3) to   (MET106)  HEXAFLUOROBENZENE BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT  |   T4 LYSOZYME, HALOGEN BOND, HYDROPHOBIC CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3dn0:A     (ILE3) to   (MET106)  PENTAFLUOROBENZENE BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT  |   T4 LYSOZYME, HALOGEN BOND, HYDROPHOBIC CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3dn1:A     (ILE3) to   (MET106)  CHLOROPENTAFLUOROBENZENE BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT  |   T4 LYSOZYME, HALOGEN BOND, HYDROPHOBIC CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3dn2:A     (ILE3) to   (MET106)  BROMOPENTAFLUOROBENZENE BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT  |   T4 LYSOZYME, HALOGEN BOND, HYDROPHOBIC CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3dn3:A     (ILE3) to   (MET106)  IODOPENTAFLUOROBENZENE BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT  |   T4 LYSOZYME, HALOGEN BOND, HYDROPHOBIC CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3dn6:A     (ILE3) to   (MET106)  1,3,5-TRIFLUORO-2,4,6-TRICHLOROBENZENE BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT  |   T4 LYSOZYME, HALOGEN BOND, HYDROPHOBIC CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3dna:A     (ILE3) to   (MSE106)  IODOBENZENE BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT (SELENO VERSION)  |   T4 LYSOZYME, HALOGEN BOND, HYDROPHOBIC CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
4dkl:A  (ILE1003) to  (MET1106)  CRYSTAL STRUCTURE OF THE MU-OPIOID RECEPTOR BOUND TO A MORPHINAN ANTAGONIST  |   G-PROTEIN COUPLED RECEPTOR, 7 TRANSMEMBRANE RECEPTOR, SIGNALING PROTEIN-ANTAGONIST COMPLEX 
3pbl:B  (ILE1003) to  (MET1106)  STRUCTURE OF THE HUMAN DOPAMINE D3 RECEPTOR IN COMPLEX WITH ETICLOPRIDE  |   STRUCTURAL GENOMICS, PSI-2, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE, ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D, 7TM, G PROTEIN-COUPLED RECEPTOR, GPCR, GPCR NETWORK, SIGNAL TRANSDUCTION, HYDROLASE, ETICLOPRIDE, DOPAMINE, NEUROTRANSMITTER, CHIMERA, T4L FUSION, MEMBRANE PROTEIN, TRANSMEMBRANE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX 
5i0n:A  (GLY1001) to  (MET1108)  PI4K IIALPHA BOUND TO CALCIUM  |   KINASE, CALCIUM, TRANSFERASE 
4e97:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 2-MERCAPTOETHANOL BOUND  |   HYDROLASE, ALKYLATION WITH 2-MERCAPTOETHANOL 
4e97:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH 2-MERCAPTOETHANOL BOUND  |   HYDROLASE, ALKYLATION WITH 2-MERCAPTOETHANOL 
4ej4:A  (ILE1003) to  (MET1106)  STRUCTURE OF THE DELTA OPIOID RECEPTOR BOUND TO NALTRINDOLE  |   G-PROTEIN COUPLED RECEPTOR, 7 TRANSMEMBRANE RECEPTOR, OPIOID RECEPTOR, SIGNALING PROTEIN, HYDROLASE-ANTAGONIST COMPLEX 
4ekp:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH NITROBENZENE BOUND  |   HYDROLASE, ALKYLATION OF CYS97 
4ekp:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH NITROBENZENE BOUND  |   HYDROLASE, ALKYLATION OF CYS97 
4ekq:A     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH 4-NITROPHENOL BOUND  |   HYDROLASE, ALKYLATION OF CYS97 
4ekq:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH 4-NITROPHENOL BOUND  |   HYDROLASE, ALKYLATION OF CYS97 
4ekr:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 2-CYANOPHENOL BOUND  |   HYDROLASE, ALKYLATION OF CYS97 
4ekr:B     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 2-CYANOPHENOL BOUND  |   HYDROLASE, ALKYLATION OF CYS97 
4eks:A     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH ISOXAZOLE BOUND  |   HYDROLASE, ALKYLATION OF CYS97 
4eks:B     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102H WITH ISOXAZOLE BOUND  |   HYDROLASE, ALKYLATION OF CYS97 
4exm:C   (ILE171) to   (GLN275)  THE CRYSTAL STRUCTURE OF AN ENGINEERED PHAGE LYSIN CONTAINING THE BINDING DOMAIN OF PESTICIN AND THE KILLING DOMAIN OF T4-LYSOZYME  |   BACTERIAL LYSIN, TOXIN, HYDROLASE 
4w51:A     (ILE3) to   (MET106)  T4 LYSOZYME L99A WITH NO LIGAND BOUND  |   HYDROLASE 
4w52:A     (ILE3) to   (GLY107)  T4 LYSOZYME L99A WITH BENZENE BOUND  |   HYDROLASE 
4w53:A     (ILE3) to   (GLY107)  T4 LYSOZYME L99A WITH TOLUENE BOUND  |   HYDROLASE 
4w54:A     (ILE3) to   (GLY107)  T4 LYSOZYME L99A WITH ETHYLBENZENE BOUND  |   HYDROLASE 
4w57:A     (ILE3) to   (GLY107)  T4 LYSOZYME L99A WITH N-BUTYLBENZENE BOUND  |   HYDROLASE 
4w58:A     (ILE3) to   (MET106)  T4 LYSOZYME L99A WITH N-PENTYLBENZENE BOUND  |   HYDROLASE 
4w59:A     (ILE3) to   (MET106)  T4 LYSOZYME L99A WITH N-HEXYLBENZENE BOUND  |   HYDROLASE 
5jdt:A     (ILE3) to   (GLY107)  STRUCTURE OF SPIN-LABELLED T4 LYSOZYME MUTANT L118C-R1 AT 100K  |   NITROXIDE, SPIN LABEL, T4 LYSOZYME, ELECTRON PARAMAGNETIC RESONANCE, HYDROLASE 
5jws:A     (ILE3) to   (MET106)  T4 LYSOZYME L99A WITH 1-HYDRO-2-ETHYL-1,2-AZABORINE BOUND  |   PHAGE LYSOZYME AZABORINE, HYDROLASE 
5jwt:A     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102Q WITH BENZENE BOUND  |   PHAGE LYSOZYME AZABORINE, HYDROLASE 
5jwu:A     (ILE3) to   (GLY107)  T4 LYSOZYME L99A/M102Q WITH 1,2-DIHYDRO-1,2-AZABORINE BOUND  |   PHAGE LYSOZYME AZABORINE, HYDROLASE 
5jwv:A     (ILE3) to   (MET106)  T4 LYSOZYME L99A/M102Q WITH ETHYLBENZENE BOUND  |   PHAGE LYSOZYME AZABORINE, HYDROLASE 
5jww:A     (ILE3) to   (GLY107)  T4 LYSOZYME L99A/M102Q WITH 1-HYDRO-2-ETHYL-1,2-AZABORINE BOUND  |   PHAGE LYSOZYME AZABORINE, HYDROLASE 
6lzm:A     (ILE3) to   (MET106)  COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS  |   HYDROLASE (O-GLYCOSYL) 
139l:A     (ILE3) to   (GLY107)  RAPID CRYSTALLIZATION OF T4 LYSOZYME BY INTERMOLECULAR DISULFIDE CROSSLINKING  |   HYDROLASE(O-GLYCOSYL) 
142l:A     (ILE3) to   (GLY107)  ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
145l:A     (ILE3) to   (GLY107)  ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
150l:A     (ILE3) to   (GLY107)  CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
150l:B     (ASN2) to   (MET106)  CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
150l:C     (ILE3) to   (MET106)  CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
158l:A     (ILE3) to   (MET106)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
159l:A     (ILE3) to   (MET106)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
161l:A     (ILE3) to   (MET106)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
166l:A     (ILE3) to   (GLY107)  CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND  |   HYDROLASE(O-GLYCOSYL) 
188l:A     (ILE3) to   (MET106)  SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY  |   HYDROLASE (O-GLYCOSYL) 
191l:A     (ILE3) to   (MET106)  A HELIX INITIATION SIGNAL IN T4 LYSOZYME IDENTIFIED BY POLYALANINE MUTAGENESIS  |   HYDROLASE (O-GLYCOSYL) 
197l:A     (ILE3) to   (GLY107)  THERMODYNAMIC AND STRUCTURAL COMPENSATION IN "SIZE-SWITCH" CORE-REPACKING VARIANTS OF T4 LYSOZYME  |   CAVITIES, CORE-PACKING, PROTEIN STABILITY, HYDROLASE (O- GLYCOSYL) 
2oe9:X     (ILE3) to   (MET106)  HIGH-PRESSURE STRUCTURE OF PSEUDO-WT T4 LYSOZYME  |   HIGH-PRESSURE, T4 LYSOZYME, HYDROLASE 
2b75:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L99A AT 150 MPA  |   T4 LYSOZYME, HIGH PRESSURE, CAVITY, HYDROLASE 
1c62:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/F153A IN THE PRESENCE OF 8 ATM XENON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c69:A     (ILE3) to   (GLY107)  T4 LYSOZYME MUTANT C54T/C97A/L133A IN THE PRESENCE OF 8 ATM ARGON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6c:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 16 ATM ARGON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6f:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 32 ATM ARGON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
1c6g:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 4 ATM KRYPTON  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, NOBLE GAS BINDING 
4i7o:A     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 2-AMINO-5-CHLOROTHIAZOLE BOUND  |   HYDROLASE 
4i7o:B     (ILE3) to   (GLN105)  T4 LYSOZYME L99A/M102H WITH 2-AMINO-5-CHLOROTHIAZOLE BOUND  |   HYDROLASE 
1ctw:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT I78A  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, CAVITY MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING, HYDROLASE 
1cu2:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L84M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING, HYDROLASE 
1cu6:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L91A  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, CAVITY FORMING MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1cv4:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT L118M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1cv6:A     (PHE4) to   (MET106)  T4 LYSOZYME MUTANT V149M  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1cx7:A     (ILE3) to   (MET106)  T4 LYSOZYME METHIONINE CORE MUTANT  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, METHIONINE CORE MUTANT, PROTEIN ENGINEERING, PROTEIN FOLDING 
1p2l:A     (ILE3) to   (MET106)  T4 LYSOZYME CORE REPACKING MUTANT V87I/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
3g3v:A     (ILE3) to   (GLY107)  CRYSTAL STRUCTURE OF SPIN LABELED T4 LYSOZYME (V131R1) AT 291 K  |   MODIFIED CYSTEINE, NITROXIDE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
1pqm:A     (ILE3) to   (MET106)  T4 LYSOZYME CORE REPACKING MUTANT V149I/T152V/TA  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, DESIGNED CORE MUTANT, AUTOMATED PROTEIN DESIGN, PROTEIN ENGINEERING, PROTEIN FOLDING, PROTEIN STABILITY, CORE REPACKING, BACK REVERTANT, DEAD-END ELIMINATION THEOREM, SIDE-CHAIN PACKING, OPTIMIZED ROTAMER COMBINATIONS, ORBIT 
1dyb:A     (ILE3) to   (GLY107)  DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
1dye:A     (ILE3) to   (GLY107)  DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
2raz:X     (ILE3) to   (MET106)  4-(METHYLTHIO)NITROBENZENE IN COMPLEX WITH T4 LYSOZYME L99A  |   PROTEIN CAVITIES, HYDROLASE 
2rb1:X     (ILE3) to   (MET106)  2-ETHOXYPHENOL IN COMPLEX WITH T4 LYSOZYME L99A  |   PROTEIN CAVITIES, HYDROLASE 
2rbo:A     (ILE3) to   (MET106)  2-NITROTHIOPHENE IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   PROTEIN CAVITIES, HYDROLASE 
1qt6:A     (ILE3) to   (MET106)  E11H MUTANT OF T4 LYSOZYME  |   HYDROLASE 
1qtb:A     (ILE3) to   (MET106)  THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME  |   STRAIN, STABILITY, MUTANT, T4 LYSOZYME, HYDROLASE 
1qtc:A     (PHE4) to   (MET106)  THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME  |   STRAIN, STABILITY, MUTANT, T4 LYSOZYME, HYDROLASE 
1quo:A     (ILE3) to   (MET106)  L99A/E108V MUTANT OF T4 LYSOZYME  |   HYDROLASE 
1g0m:A     (ILE3) to   (GLY107)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT T152I  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
1g0p:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149G  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
1g0q:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149I  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
1swy:A     (ILE3) to   (GLN105)  USE OF A HALIDE BINDING SITE TO BYPASS THE 1000-ATOM LIMIT TO AB INITIO STRUCTURE DETERMINATION  |   RB+ BINDING SITES, AB INITIO DIRECT METHODS, HYDROLASE 
1swz:A     (ILE3) to   (GLY107)  USE OF AN ION-BINDING SITE TO BYPASS THE 1000-ATOM LIMIT TO AB INITIO STRUCTURE DETERMINATION BY DIRECT METHODS  |   RB+ BINDING SITE, AB INITIO DIRECT METHODS, HYDROLASE 
1sx7:A     (ILE3) to   (PHE104)  USE OF AN ION-BINDING SITE TO BYPASS THE 1000-ATOM LIMIT TO AB INITIO STRUCTURE DETERMINATION BY DIRECT METHODS  |   AB INITIO DIRECT METHODS, HYDROLASE 
1i6s:A     (ILE3) to   (MET106)  T4 LYSOZYME MUTANT C54T/C97A/N101A  |   HYDROLASE (O-GLYCOSYL), T4 LYSOZYME, HYDRATED CAVITIES 
4lzm:A     (ILE3) to   (GLY107)  COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS  |   HYDROLASE (O-GLYCOSYL) 
5b2g:G  (ILE1003) to  (MET1106)  CRYSTAL STRUCTURE OF HUMAN CLAUDIN-4 IN COMPLEX WITH C-TERMINAL FRAGMENT OF CLOSTRIDIUM PERFRINGENS ENTEROTOXIN  |   MEMBRANE PROTEIN, COMPLEX, CELL-FREE PROTEIN EXPRESSION SYSTEM 
1wth:A   (SER175) to   (MET284)  CRYSTAL STRUCTURE OF GP5-S351L MUTANT AND GP27 COMPLEX  |   TRIPLE-STRANDED BETA-HELIX, OB FOLD, PSEUDOHEXAMER, T4 TAIL LYSOZYME, HUB, GP5-GP27, HYDROLASE-STRUCTURAL PROTEIN COMPLEX 
2l78:A     (ILE3) to   (GLY107)  DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
2lc9:A     (ILE3) to   (VAL103)  SOLUTION STRUCTURE OF A MINOR AND TRANSIENTLY FORMED STATE OF A T4 LYSOZYME MUTANT  |   HYDROLASE 
1kni:A     (ILE3) to   (MET106)  STABILIZING DISULFIDE BRIDGE MUTANT OF T4 LYSOZYME  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1xep:A     (ILE3) to   (GLY107)  CATECHOL IN COMPLEX WITH T4 LYSOZYME L99A/M102Q  |   GLYCOSIDASE, BACTERIOLYTIC ENZYME, HYDROLASE 
1l11:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l14:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l16:A     (ILE3) to   (MET106)  STRUCTURAL ANALYSIS OF THE TEMPERATURE-SENSITIVE MUTANT OF BACTERIOPHAGE T4 LYSOZYME, GLYCINE 156 (RIGHT ARROW) ASPARTIC ACID  |   HYDROLASE (O-GLYCOSYL) 
1l22:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l28:A     (ILE3) to   (GLY107)  REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l33:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF LEFT-HANDED HELICAL RESIDUES TO THE STRUCTURE AND STABILITY OF BACTERIOPHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l40:A     (ILE3) to   (MET106)  CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS  |   HYDROLASE (O-GLYCOSYL) 
1l44:A     (ILE3) to   (GLY107)  CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l46:A     (ILE3) to   (GLY107)  CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY  |   HYDROLASE (O-GLYCOSYL) 
1l56:A     (ILE3) to   (MET106)  ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l61:A     (ILE3) to   (MET106)  ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l63:A     (ILE3) to   (MET106)  ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL) 
1l66:A     (ILE3) to   (MET106)  TOLERANCE OF T4 LYSOZYME TO MULTIPLE XAA (RIGHT ARROW) ALA SUBSTITUTIONS: A POLYALANINE ALPHA-HELIX CONTAINING TEN CONSECUTIVE ALANINES  |   HYDROLASE (O-GLYCOSYL) 
1l84:A     (ILE3) to   (GLY107)  A CAVITY-CONTAINING MUTANT OF T4 LYSOZYME IS STABILIZED BY BURIED BENZENE  |   HYDROLASE(O-GLYCOSYL) 
1l86:A     (ILE3) to   (MET106)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l90:A     (ILE3) to   (GLY107)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l92:A     (ILE3) to   (MET106)  SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES  |   HYDROLASE(O-GLYCOSYL) 
1l96:A     (PRO3) to   (GLY107)  STRUCTURE OF A HINGE-BENDING BACTERIOPHAGE T4 LYSOZYME MUTANT, ILE3-> PRO  |   HYDROLASE(O-GLYCOSYL) 
1l97:B     (PRO3) to   (GLY107)  STRUCTURE OF A HINGE-BENDING BACTERIOPHAGE T4 LYSOZYME MUTANT, ILE3-> PRO  |   HYDROLASE(O-GLYCOSYL) 
3k2r:A     (ILE3) to   (MET106)  CRYSTAL STRUCTURE OF SPIN LABELED T4 LYSOZYME MUTANT K65V1/R76V1  |   NITROXIDE SPIN LABEL, EPR, MODIFIED CYSTEINE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
1lye:A     (ILE3) to   (GLY107)  DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59  |   HYDROLASE(O-GLYCOSYL) 
4phu:A  (PHE1004) to  (MET1106)  CRYSTAL STRUCTURE OF HUMAN GPR40 BOUND TO ALLOSTERIC AGONIST TAK-875  |   GPR40, FATTY ACID BINDING PROTEIN, CLASS A, G-PROTEIN COUPLED RECEPTOR, TYPE II DIABETES, TAK-875, FASIGLIFAM, FATTY ACID BINDING PROTEIN-HYDROLASE COMPLEX 
206l:A     (ILE3) to   (MET106)  PHAGE T4 LYSOZYME  |   HYDROLASE, O-GLYCOSYL, HYDROLASE (O-GLYCOSYL) 
211l:A     (ILE3) to   (GLY107)  PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), GLYCOSIDASE, BACTERIOLYTIC ENZYME 
215l:A     (ILE3) to   (GLY107)  PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME  |   HYDROLASE (O-GLYCOSYL), GLYCOSIDASE, BACTERIOLYTIC ENZYME 
217l:A     (ILE3) to   (MET106)  STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME  |   HYDROLASE(O-GLYCOSYL) 
221l:A     (ILE3) to   (GLY107)  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  |   HYDROLASE(O-GLYCOSYL) 
226l:A     (ILE3) to   (GLY107)  GENERATING LIGAND BINDING SITES IN T4 LYSOZYME USING DEFICIENCY-CREATING SUBSTITUTIONS  |   HYDROLASE, O-GLYCOSYL, T4 LYSOZYME, CAVITY MUTANTS, LIGAND BINDING, PROTEIN ENGINEERING, PROTEIN DESIGN 
231l:A     (ILE3) to   (LYS106)  T4 LYSOZYME MUTANT M106K  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE 
234l:A     (ILE3) to   (GLY107)  T4 LYSOZYME MUTANT M106L  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE 
243l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
246l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
249l:A     (ILE3) to   (MET106)  THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT  |   HYDROLASE, O-GLYCOSYL, GLYCOSIDASE, BACTERIOLYTIC ENZYME 
5ee7:A  (ASN1000) to  (GLN1103)  CRYSTAL STRUCTURE OF THE HUMAN GLUCAGON RECEPTOR (GCGR) IN COMPLEX WITH THE ANTAGONIST MK-0893  |   GPCR, SIGNALING PROTEIN, 7TM 
3cdt:A     (ILE3) to   (GLY107)  CONTRIBUTIONS OF ALL 20 AMINO ACIDS AT SITE 96 TO THE STABILITY AND STRUCTURE OF T4 LYSOZYME  |   BACTERIOPHAGE T4 LYSOZYME, VIRAL LYSOZYME, MUTATIONAL ANALYSIS, PROTEIN ENGINEERNG, THERMAL STABILITY, PROTEIN STABILITY, PROTEIN ELECTROSTATICS, PROTEIN STRUCTURE, CATION BINDING, CHARGE BURIAL, HYDROGEN BONDING, HELIX DIPOLE, PROTEIN CREVICES, STERIC STRAIN, TEMPERATURE- SENSITIVE MUTANT, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3ny9:A  (ILE1003) to  (MET1106)  CRYSTAL STRUCTURE OF THE HUMAN BETA2 ADRENERGIC RECEPTOR IN COMPLEX WITH A NOVEL INVERSE AGONIST  |   G PROTEIN-COUPLED RECEPTOR, LYSOZYME, FUSION, TRANSDUCER, ADRENERGIC, G-PROTEINS, ARRESTINS, ADRENALIN, COMPOUND 2, GLYCOSYLATION, PALMITOYLATION, PHOSPHORYLATION, MEMBRANE PROTEIN, HYDROLASE, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D 
3oe0:A   (ASP193) to  (MET1106)  CRYSTAL STRUCTURE OF THE CXCR4 CHEMOKINE RECEPTOR IN COMPLEX WITH A CYCLIC PEPTIDE ANTAGONIST CVX15  |   STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D, 7TM, G PROTEIN-COUPLED RECEPTOR, GPCR, SIGNAL TRANSDUCTION, HYDROLASE, CANCER, HIV-1 CO-RECEPTOR, CHEMOKINE, CXCL12, CHIMERA, T4L FUSION, MEMBRANE PROTEIN, TRANSMEMBRANE, ANTIMICROBIAL, ANTIBIOTIC, POLYPHEMUSIN, SIGNALING PROTEIN, HYDROLASE-ANTIBIOTIC COMPLEX, PSI- BIOLOGY, GPCR NETWORK 
3oe9:A   (ASP193) to  (MET1106)  CRYSTAL STRUCTURE OF THE CHEMOKINE CXCR4 RECEPTOR IN COMPLEX WITH A SMALL MOLECULE ANTAGONIST IT1T IN P1 SPACEGROUP  |   STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D, 7TM, G PROTEIN-COUPLED RECEPTOR, GPCR, SIGNAL TRANSDUCTION, CHEMOTAXIS, HYDROLASE, CANCER, HIV-1 CO-RECEPTOR, CHEMOKINE, CXCL12, SDF1, ISOTHIOUREA, IT1T, CHIMERA, T4L FUSION, MEMBRANE PROTEIN, TRANSMEMBRANE, SINGNALING PROTEIN, PSI-BIOLOGY, GPCR NETWORK, SIGNALING PROTEIN 
3dn4:A     (ILE3) to   (MET106)  IODOBENZENE BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT  |   T4 LYSOZYME, HALOGEN BOND, HYDROPHOBIC CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
3dn8:A     (ILE3) to   (MSE106)  IODOPENTAFLUOROBENZENE BINDING IN THE HYDROPHOBIC CAVITY OF T4 LYSOZYME L99A MUTANT (SELENO VERSION)  |   T4 LYSOZYME, HALOGEN BOND, HYDROPHOBIC CAVITY, HALOGENATED BENZENE, ANTIMICROBIAL, BACTERIOLYTIC ENZYME, GLYCOSIDASE, HYDROLASE 
4w55:A     (ILE3) to   (GLY107)  T4 LYSOZYME L99A WITH N-PROPYLBENZENE BOUND  |   HYDROLASE 
4w56:A     (ILE3) to   (GLY107)  T4 LYSOZYME L99A WITH SEC-BUTYLBENZENE BOUND  |   HYDROLASE 
5lzm:A     (ILE3) to   (GLY107)  COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS  |   HYDROLASE (O-GLYCOSYL) 
7lzm:A     (ILE3) to   (GLY107)  COMPARISON OF THE CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME AT LOW, MEDIUM, AND HIGH IONIC STRENGTHS  |   HYDROLASE (O-GLYCOSYL)