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)